LOCUS       NP_001361188             862 aa            linear   PRI 21-NOV-2025
DEFINITION  interleukin-12 receptor subunit beta-2 isoform a precursor [Homo
            sapiens].
ACCESSION   NP_001361188 XP_005270882
VERSION     NP_001361188.1
DBSOURCE    REFSEQ: accession NM_001374259.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Chen,H., Ge,X., Li,C., Zeng,J. and Wang,X.
  TITLE     Structure and assembly of the human IL-12 signaling complex
  JOURNAL   Structure 32 (10), 1640-1651 (2024)
   PUBMED   39111304
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Zare,M., Hesampour,F., Poordast,T., Valibeigi,M., Enayatmehri,M.,
            Ahmadi,S., Nasri,F. and Gharesi-Fard,B.
  TITLE     Association between gene polymorphisms of IL-12, IL-12 receptor and
            IL-27 and organ involvement in Iranian endometriosis patients
  JOURNAL   Int J Immunogenet 50 (1), 24-33 (2023)
   PUBMED   36328955
  REMARK    GeneRIF: Association between gene polymorphisms of IL-12, IL-12
            receptor and IL-27 and organ involvement in Iranian endometriosis
            patients.
REFERENCE   3  (residues 1 to 862)
  AUTHORS   Fu,Y., Liu,L. and Wu,H.
  TITLE     Role of Genetic Polymorphisms in IL12Rbeta2 in Chronic Obstructive
            Pulmonary Disease
  JOURNAL   Int J Chron Obstruct Pulmon Dis 17, 1671-1683 (2022)
   PUBMED   35923356
  REMARK    GeneRIF: Role of Genetic Polymorphisms in IL12Rbeta2 in Chronic
            Obstructive Pulmonary Disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 862)
  AUTHORS   Ye,C., Yano,H., Workman,C.J. and Vignali,D.A.A.
  TITLE     Interleukin-35: Structure, Function and Its Impact on
            Immune-Related Diseases
  JOURNAL   J Interferon Cytokine Res 41 (11), 391-406 (2021)
   PUBMED   34788131
  REMARK    Review article
REFERENCE   5  (residues 1 to 862)
  AUTHORS   Wang,X., Zhou,S., Fan,M., Wang,P., Fang,H., Bian,F., Huang,T. and
            Du,X.
  TITLE     Expressions of IL-12 and its receptors in patients with lumbar disc
            herniation and their relationship with clinical efficacy
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 66 (7), 5-11 (2020)
   PUBMED   33287915
  REMARK    GeneRIF: Expressions of IL-12 and its receptors in patients with
            lumbar disc herniation and their relationship with clinical
            efficacy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 862)
  AUTHORS   Rogge,L., Barberis-Maino,L., Biffi,M., Passini,N., Presky,D.H.,
            Gubler,U. and Sinigaglia,F.
  TITLE     Selective expression of an interleukin-12 receptor component by
            human T helper 1 cells
  JOURNAL   J Exp Med 185 (5), 825-831 (1997)
   PUBMED   9120388
REFERENCE   7  (residues 1 to 862)
  AUTHORS   Presky,D.H., Yang,H., Minetti,L.J., Chua,A.O., Nabavi,N., Wu,C.Y.,
            Gately,M.K. and Gubler,U.
  TITLE     A functional interleukin 12 receptor complex is composed of two
            beta-type cytokine receptor subunits
  JOURNAL   Proc Natl Acad Sci U S A 93 (24), 14002-14007 (1996)
   PUBMED   8943050
REFERENCE   8  (residues 1 to 862)
  AUTHORS   Bacon,C.M., Petricoin,E.F. 3rd, Ortaldo,J.R., Rees,R.C.,
            Larner,A.C., Johnston,J.A. and O'Shea,J.J.
  TITLE     Interleukin 12 induces tyrosine phosphorylation and activation of
            STAT4 in human lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 92 (16), 7307-7311 (1995)
   PUBMED   7638186
REFERENCE   9  (residues 1 to 862)
  AUTHORS   Bacon,C.M., McVicar,D.W., Ortaldo,J.R., Rees,R.C., O'Shea,J.J. and
            Johnston,J.A.
  TITLE     Interleukin 12 (IL-12) induces tyrosine phosphorylation of JAK2 and
            TYK2: differential use of Janus family tyrosine kinases by IL-2 and
            IL-12
  JOURNAL   J Exp Med 181 (1), 399-404 (1995)
   PUBMED   7528775
REFERENCE   10 (residues 1 to 862)
  AUTHORS   Chua,A.O., Chizzonite,R., Desai,B.B., Truitt,T.P., Nunes,P.,
            Minetti,L.J., Warrier,R.R., Presky,D.H., Levine,J.F., Gately,M.K.
            et al.
  TITLE     Expression cloning of a human IL-12 receptor component. A new
            member of the cytokine receptor superfamily with strong homology to
            gp130
  JOURNAL   J Immunol 153 (1), 128-136 (1994)
   PUBMED   7911493
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL389925.10 and AL358512.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 17, 2019 this sequence version replaced XP_005270882.1.
            
            Summary: The protein encoded by this gene is a type I transmembrane
            protein identified as a subunit of the interleukin 12 receptor
            complex. The coexpression of this and IL12RB1 proteins was shown to
            lead to the formation of high-affinity IL12 binding sites and
            reconstitution of IL12 dependent signaling. The expression of this
            gene is up-regulated by interferon gamma in Th1 cells, and plays a
            role in Th1 cell differentiation. The up-regulation of this gene is
            found to be associated with a number of infectious diseases, such
            as Crohn's disease and leprosy, which is thought to contribute to
            the inflammatory response and host defense. Several transcript
            variants encoding different isoforms and non-protein coding
            transcripts have been found for this gene. [provided by RefSeq, Apr
            2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3202244.1,
                                           SRR18074967.1832.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000674203.2/ ENSP00000501329.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..862
                     /product="interleukin-12 receptor subunit beta-2 isoform a
                     precursor"
                     /note="interleukin-12 receptor beta-2 chain; IL-12R
                     subunit beta-2; IL-12 receptor subunit beta-2; interleukin
                     12 receptor, beta 2"
                     /calculated_mol_wt=94482
     sig_peptide     1..23
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
                     /calculated_mol_wt=2671
     mat_peptide     24..862
                     /product="Interleukin-12 receptor subunit beta-2.
                     /id=PRO_0000010920"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99665.1)"
                     /calculated_mol_wt=94482
     Region          28..110
                     /region_name="Lep_receptor_Ig"
                     /note="Ig-like C2-type domain; pfam06328"
                     /db_xref="CDD:461878"
     Site            48
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Site            129
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Region          224..316
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(224,286,304)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Region          305..309
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99665.1)"
     Site            order(305..306,308..309)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            347
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Region          <368..>608
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            376
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Region          423..511
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            480
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Site            order(507..508,510..511)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            623..643
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99665.1)"
     Region          662..670
                     /region_name="Box 1 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99665.1)"
     Region          725..755
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99665.1)"
     Region          796..801
                     /region_name="Required for STAT4 binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99665.1)"
     Site            800
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:10415122; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     CDS             1..862
                     /gene="IL12RB2"
                     /coded_by="NM_001374259.2:220..2808"
                     /note="isoform a precursor is encoded by transcript
                     variant 8"
                     /db_xref="CCDS:CCDS638.1"
                     /db_xref="GeneID:3595"
                     /db_xref="HGNC:HGNC:5972"
                     /db_xref="MIM:601642"
ORIGIN      
        1 mahtfrgcsl afmfiitwll ikakidackr gdvtvkpshv illgstvnit cslkprqgcf
       61 hysrrnklil ykfdrrinfh hghslnsqvt glplgttlfv cklacinsde iqicgaeifv
      121 gvapeqpqnl sciqkgeqgt vactwergrd thlyteytlq lsgpknltwq kqckdiycdy
      181 ldfginltpe spesnftakv tavnslgsss slpstftfld ivrplppwdi rikfqkasvs
      241 rctlywrdeg lvllnrlryr psnsrlwnmv nvtkakgrhd lldlkpftey efqissklhl
      301 ykgswsdwse slraqtpeee ptgmldvwym krhidysrqq islfwknlsv seargkilhy
      361 qvtlqeltgg kamtqnitgh tswttviprt gnwavavsaa nskgsslptr inimnlceag
      421 llaprqvsan segmdnilvt wqpprkdpsa vqeyvvewre lhpggdtqvp lnwlrsrpyn
      481 vsalisenik syicyeirvy alsgdqggcs silgnskhka plsgphinai teekgsilis
      541 wnsipvqeqm gcllhyriyw kerdsnsqpq lceipyrvsq nshpinslqp rvtyvlwmta
      601 ltaagesshg nerefclqgk anwmafvaps iciaiimvgi fsthyfqqkv fvllaalrpq
      661 wcsreipdpa nstcakkypi aeektqlpld rllidwptpe dpeplvisev lhqvtpvfrh
      721 ppcsnwpqre kgiqghqase kdmmhsassp pppralqaes rqlvdlykvl esrgsdpkpe
      781 npacpwtvlp agdlpthdgy lpsniddlps heapladsle elepqhisls vfpssslhpl
      841 tfscgdkltl dqlkmrcdsl ml
//
LOCUS       NP_001271200             731 aa            linear   PRI 21-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 3 isoform c [Homo
            sapiens].
ACCESSION   NP_001271200
VERSION     NP_001271200.1
DBSOURCE    REFSEQ: accession NM_001284271.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Makhlouf,L., Peter,J.J., Magnussen,H.M., Thakur,R., Millrine,D.,
            Minshull,T.C., Harrison,G., Varghese,J., Lamoliatte,F.,
            Foglizzo,M., Macartney,T., Calabrese,A.N., Zeqiraj,E. and
            Kulathu,Y.
  TITLE     The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER
            translocons
  JOURNAL   Nature 627 (8003), 437-444 (2024)
   PUBMED   38383789
REFERENCE   3  (residues 1 to 731)
  AUTHORS   DaRosa,P.A., Penchev,I., Gumbin,S.C., Scavone,F., Wachalska,M.,
            Paulo,J.A., Ordureau,A., Peter,J.J., Kulathu,Y., Harper,J.W.,
            Becker,T., Beckmann,R. and Kopito,R.R.
  TITLE     UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from
            the ER
  JOURNAL   Nature 627 (8003), 445-452 (2024)
   PUBMED   38383785
REFERENCE   4  (residues 1 to 731)
  AUTHORS   Ao,Y.Q., Gao,J., Jin,C., Wang,S., Zhang,L.C., Deng,J., Chen,Z.W.,
            Wang,H.K., Jiang,J.H. and Ding,J.Y.
  TITLE     ASCC3 promotes the immunosuppression and progression of non-small
            cell lung cancer by impairing the type I interferon response via
            CAND1-mediated ubiquitination inhibition of STAT3
  JOURNAL   J Immunother Cancer 11 (12), e007766 (2023)
   PUBMED   38148115
  REMARK    GeneRIF: ASCC3 promotes the immunosuppression and progression of
            non-small cell lung cancer by impairing the type I interferon
            response via CAND1-mediated ubiquitination inhibition of STAT3.
            Erratum:[J Immunother Cancer. 2024 Jul 10;12(7):e007766corr1. doi:
            10.1136/jitc-2023-007766corr1. PMID: 38986545]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 731)
  AUTHORS   Li,J., Ding,S.C., Cho,H., Chung,B.C., Gale,M. Jr., Chanda,S.K. and
            Diamond,M.S.
  TITLE     A short hairpin RNA screen of interferon-stimulated genes
            identifies a novel negative regulator of the cellular antiviral
            response
  JOURNAL   mBio 4 (3), e00385-e00313 (2013)
   PUBMED   23781071
  REMARK    GeneRIF: Silencing of ASCC3 resulted in upregulation of multiple
            antiviral interferon-stimulated genes, which correlated with
            inhibition of infection of several positive-strand RNA viruses.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 731)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 731)
  AUTHORS   Dango,S., Mosammaparast,N., Sowa,M.E., Xiong,L.J., Wu,F., Park,K.,
            Rubin,M., Gygi,S., Harper,J.W. and Shi,Y.
  TITLE     DNA unwinding by ASCC3 helicase is coupled to ALKBH3-dependent DNA
            alkylation repair and cancer cell proliferation
  JOURNAL   Mol Cell 44 (3), 373-384 (2011)
   PUBMED   22055184
  REMARK    GeneRIF: DNA unwinding by ASCC3 helicase is coupled to
            ALKBH3-dependent DNA alkylation repair and cancer cell
            proliferation.
REFERENCE   8  (residues 1 to 731)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   9  (residues 1 to 731)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
REFERENCE   10 (residues 1 to 731)
  AUTHORS   Coulie,P.G., Ikeda,H., Baurain,J.F. and Chiari,R.
  TITLE     Antitumor immunity at work in a melanoma patient
  JOURNAL   Adv Cancer Res 76, 213-242 (1999)
   PUBMED   10218103
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC026066.1, AL133338.8 and
            AL591585.7.
            
            Summary: This gene encodes a protein that belongs to a family of
            helicases that are involved in the ATP-dependent unwinding of
            nucleic acid duplexes. The encoded protein is the largest subunit
            of the activating signal cointegrator 1 complex that is involved in
            DNA repair and resistance to alkylation damage. Alternate splicing
            results in multiple transcript variants. [provided by RefSeq, Sep
            2013].
            
            Transcript Variant: This variant (3) lacks several exons in the 3'
            coding region and its 3' terminal exon extends past a splice site
            that is used in variant 1. This results in a novel 3' coding region
            and 3' UTR compared to variant 1. The encoded protein (isoform c)
            has a distinct C-terminus and is shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC026066.1, SRR11853560.25120.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q16.3"
     Protein         1..731
                     /product="activating signal cointegrator 1 complex subunit
                     3 isoform c"
                     /EC_number="5.6.2.4"
                     /note="RNA helicase family; ASC-1 complex subunit P200;
                     helicase, ATP binding 1; trip4 complex subunit p200"
                     /calculated_mol_wt=83545
     Region          1..400
                     /region_name="Required for interaction with ASCC2.
                     /evidence=ECO:0000269|PubMed:29997253"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3C0.3)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3C0.3)"
     Region          476..673
                     /region_name="DEXHc_ASCC3_1"
                     /note="N-terminal DEXH-box helicase domain of Activating
                     signal cointegrator 1 complex subunit 3; cd18020"
                     /db_xref="CDD:350778"
     Site            order(476..478,481,501..507)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350778"
     Site            order(539..540,567,584,586..587,590,620)
                     /site_type="other"
                     /note="nucleic acid binding site [nucleotide binding]"
                     /db_xref="CDD:350778"
     Site            572
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8N3C0.3)"
     Region          611..614
                     /region_name="DEVH box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3C0.3)"
     CDS             1..731
                     /gene="ASCC3"
                     /gene_synonym="ASC1p200; HELIC1; MRT81; RNAH"
                     /coded_by="NM_001284271.2:311..2506"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS75497.1"
                     /db_xref="GeneID:10973"
                     /db_xref="HGNC:HGNC:18697"
                     /db_xref="MIM:614217"
ORIGIN      
        1 malprltgal rsfsnvtkqd nyneevadlk ikrsklheqv ldlgltwkki ikflneklek
       61 skmqsinedl kdilhaakqi vgtdngreai esgaaflfmt fhlkdsvghk etkaikqmfg
      121 pfpsssataa cnatnriish fsqddltalv qmtekehgdr vffgknlafs fdmhdldhfd
      181 elpingetqk tisldykkfl nehlqeactp elkpvektng sflwceveky lnstlkemte
      241 vprvedlcct lydmlasiks gdelqdelfe llgpegleli ekllqnriti vdrflnssnd
      301 hrfqalqdnc kkilgenakp nygcqvtiqs eqekqlmkqy rreekriarr ekkagedlev
      361 seglmcfdpk elriqreqal lnarsvpils rqrdadveki hyphvydsqa eamktsafia
      421 gakmilpegi qrennklyee vripysepmp lsfeekpvyi qdldeigqla fkgmkrlnri
      481 qsivfetayn tnenmlicap tgagktniam ltvlheirqh fqqgvikkne fkivyvapmk
      541 alaaemtdyf srrleplgii vkeltgdmql skseilrtqm lvttpekwdv vtrksvgdva
      601 lsqivrllil devhllhedr gpvlesivar tlrqvestqs mirilglsat lpnyldvatf
      661 lhvnpyiglf ffdgrfrpvp lgqtflgikc ankmqqlnnm devcyenvlk qvkaghqvhl
      721 fylllhlfic f
//
LOCUS       NP_001310253             384 aa            linear   PRI 21-NOV-2025
DEFINITION  mitogen-activated protein kinase 8 isoform alpha1 [Homo sapiens].
ACCESSION   NP_001310253
VERSION     NP_001310253.1
DBSOURCE    REFSEQ: accession NM_001323324.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Liu,X., Ye,Z., Rao,D., Chen,Q. and Zhang,Z.
  TITLE     DUSP4 maintains the survival and LSD1 protein stability in
            esophageal squamous cell carcinoma cells by inhibiting JNK
            signaling-dependent autophagy
  JOURNAL   In Vitro Cell Dev Biol Anim 60 (2), 115-122 (2024)
   PUBMED   38286920
  REMARK    GeneRIF: DUSP4 maintains the survival and LSD1 protein stability in
            esophageal squamous cell carcinoma cells by inhibiting JNK
            signaling-dependent autophagy.
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Louw-du Toit,R., Simons,M. and Africander,D.
  TITLE     Progestins and breast cancer hallmarks: The role of the ERK1/2 and
            JNK pathways in estrogen receptor positive breast cancer cells
  JOURNAL   J Steroid Biochem Mol Biol 237, 106440 (2024)
   PUBMED   38048919
  REMARK    GeneRIF: Progestins and breast cancer hallmarks: The role of the
            ERK1/2 and JNK pathways in estrogen receptor positive breast cancer
            cells.
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Chai,F., Peng,H., Qin,L., Liu,C., Zeng,Y., Wang,R., Xu,G., Wang,R.,
            Wei,G., Huang,H., Lan,Y., Chen,W. and Wang,C.
  TITLE     MicroRNA miR-181d-5p regulates the MAPK signaling pathway by
            targeting mitogen-activated protein kinase 8 (MAPK8) to improve
            lupus nephritis
  JOURNAL   Gene 893, 147961 (2024)
   PUBMED   37931853
  REMARK    GeneRIF: MicroRNA miR-181d-5p regulates the MAPK signaling pathway
            by targeting mitogen-activated protein kinase 8 (MAPK8) to improve
            lupus nephritis.
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Feng,Y., Cao,H., Wang,D., Chen,L., Gao,R. and Sun,P.
  TITLE     JNK promotes the progression of castration-resistant prostate
            cancer
  JOURNAL   Acta Biochim Pol 70 (4), 817-822 (2023)
   PUBMED   38099475
  REMARK    GeneRIF: JNK promotes the progression of castration-resistant
            prostate cancer.
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Kharbanda,S., Saleem,A., Shafman,T., Emoto,Y., Taneja,N., Rubin,E.,
            Weichselbaum,R., Woodgett,J., Avruch,J., Kyriakis,J. et al.
  TITLE     Ionizing radiation stimulates a Grb2-mediated association of the
            stress-activated protein kinase with phosphatidylinositol 3-kinase
  JOURNAL   J Biol Chem 270 (32), 18871-18874 (1995)
   PUBMED   7642542
REFERENCE   7  (residues 1 to 384)
  AUTHORS   van Dam,H., Wilhelm,D., Herr,I., Steffen,A., Herrlich,P. and
            Angel,P.
  TITLE     ATF-2 is preferentially activated by stress-activated protein
            kinases to mediate c-jun induction in response to genotoxic agents
  JOURNAL   EMBO J 14 (8), 1798-1811 (1995)
   PUBMED   7737130
REFERENCE   8  (residues 1 to 384)
  AUTHORS   Livingstone,C., Patel,G. and Jones,N.
  TITLE     ATF-2 contains a phosphorylation-dependent transcriptional
            activation domain
  JOURNAL   EMBO J 14 (8), 1785-1797 (1995)
   PUBMED   7737129
REFERENCE   9  (residues 1 to 384)
  AUTHORS   Derijard,B., Raingeaud,J., Barrett,T., Wu,I.H., Han,J.,
            Ulevitch,R.J. and Davis,R.J.
  TITLE     Independent human MAP-kinase signal transduction pathways defined
            by MEK and MKK isoforms
  JOURNAL   Science 267 (5198), 682-685 (1995)
   PUBMED   7839144
  REMARK    Erratum:[Science 1995 Jul 7;269(5220):17]
REFERENCE   10 (residues 1 to 384)
  AUTHORS   Seth,A., Alvarez,E., Gupta,S. and Davis,R.J.
  TITLE     A phosphorylation site located in the NH2-terminal domain of c-Myc
            increases transactivation of gene expression
  JOURNAL   J Biol Chem 266 (35), 23521-23524 (1991)
   PUBMED   1748630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC074325.7 and AC016397.6.
            
            Summary: The protein encoded by this gene is a member of the MAP
            kinase family. MAP kinases act as an integration point for multiple
            biochemical signals, and are involved in a wide variety of cellular
            processes such as proliferation, differentiation, transcription
            regulation and development. This kinase is activated by various
            cell stimuli, and targets specific transcription factors, and thus
            mediates immediate-early gene expression in response to cell
            stimuli. The activation of this kinase by tumor-necrosis factor
            alpha (TNF-alpha) is found to be required for TNF-alpha induced
            apoptosis. This kinase is also involved in UV radiation induced
            apoptosis, which is thought to be related to cytochrom c-mediated
            cell death pathway. Studies of the mouse counterpart of this gene
            suggested that this kinase play a key role in T cell proliferation,
            apoptosis and differentiation. Several alternatively spliced
            transcript variants encoding distinct isoforms have been reported.
            [provided by RefSeq, Apr 2016].
            
            Transcript Variant: This variant (10), along with variants JNK1-a1,
            12, and 13, encodes isoform alpha1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.82003.1,
                                           SRR1803614.246087.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q11.22"
     Protein         1..384
                     /product="mitogen-activated protein kinase 8 isoform
                     alpha1"
                     /EC_number="2.7.11.24"
                     /note="JUN N-terminal kinase; c-Jun N-terminal kinase 1;
                     MAP kinase 8; stress-activated protein kinase 1;
                     stress-activated protein kinase 1c"
                     /calculated_mol_wt=44098
     Region          25..360
                     /region_name="STKc_JNK"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     c-Jun N-terminal Kinase; cd07850"
                     /db_xref="CDD:270840"
     Site            order(32..38,40,53,55,72,86,108..114,116..117,151,153,
                     155..156,158,168..169,172,183,185..188,190,227)
                     /site_type="active"
                     /db_xref="CDD:270840"
     Site            order(32..38,40,53,55,86,108..114,158,168)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270840"
     Site            order(72,116,151,153,172,183,185..188,190,227)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270840"
     Site            order(112,118,127,130,159..163,323..324,326,329)
                     /site_type="other"
                     /note="KIM docking site [polypeptide binding]"
                     /db_xref="CDD:270840"
     Site            order(168..178,182..190)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270840"
     Region          183..185
                     /region_name="TXY"
                     /note="propagated from UniProtKB/Swiss-Prot (P45983.2)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAP2K7.
                     /evidence=ECO:0000269|PubMed:11062067; propagated from
                     UniProtKB/Swiss-Prot (P45983.2)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by MAP2K4.
                     /evidence=ECO:0000269|PubMed:11062067; propagated from
                     UniProtKB/Swiss-Prot (P45983.2)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P45983.2)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91Y86; Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P45983.2)"
     CDS             1..384
                     /gene="MAPK8"
                     /gene_synonym="JNK; JNK-46; JNK1; JNK1A2; JNK21B1/2;
                     PRKM8; SAPK1; SAPK1c"
                     /coded_by="NM_001323324.2:195..1349"
                     /note="isoform alpha1 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS7225.1"
                     /db_xref="GeneID:5599"
                     /db_xref="HGNC:HGNC:6881"
                     /db_xref="MIM:601158"
ORIGIN      
        1 msrskrdnnf ysveigdstf tvlkryqnlk pigsgaqgiv caaydailer nvaikklsrp
       61 fqnqthakra yrelvlmkcv nhkniiglln vftpqkslee fqdvyivmel mdanlcqviq
      121 meldhermsy llyqmlcgik hlhsagiihr dlkpsnivvk sdctlkildf glartagtsf
      181 mmtpyvvtry yrapevilgm gykenvdlws vgcimgemvc hkilfpgrdy idqwnkvieq
      241 lgtpcpefmk klqptvrtyv enrpkyagys feklfpdvlf padsehnklk asqardllsk
      301 mlvidaskri svdealqhpy invwydpsea eapppkipdk qlderehtie ewkeliykev
      361 mdleertkng virgqpspla qvqq
//
LOCUS       NP_001362653             425 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform aaa [Homo sapiens].
ACCESSION   NP_001362653 XP_016858631
VERSION     NP_001362653.1
DBSOURCE    REFSEQ: accession NM_001375724.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 425)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 425)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 425)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            On Oct 31, 2019 this sequence version replaced XP_016858631.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2383994.1,
                                           SRR18074967.917510.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..425
                     /product="abl interactor 2 isoform aaa"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=46641
     Region          93..156
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          364..424
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(372,374,377,381,399..400,413,415..416)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..425
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375724.1:122..1399"
                     /note="isoform aaa is encoded by transcript variant 58"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqs adkqraleet kayttqslas
       61 vaylintlan nvlqmldiqa sqlrrmessi nhisqtvdih kekvarreig ilttnkntsr
      121 thkiiapanl erpvryirkp idytilddig hgvkvstqnm kmgglprttp ptqkppsppm
      181 sgkgtlgsgs sggshpssrs ssrensgsgs vgvpiavptp sppsvfpghp vqfysmnrpa
      241 srhtpptigg slpyrrppsi tsqtslqnqm nggpfysqnp vslappppsi lqvtpqlplm
      301 gfvarvqeni sdtppppppv eepvfdespp pppppedyee eeaavveysd pyaeedppwa
      361 prsylekvva iydytkdked elsfqegaii yvikknddgw yegvmngvtg lfpgnyvesi
      421 mhyse
//
LOCUS       NP_001306010             107 aa            linear   PRI 21-NOV-2025
DEFINITION  high mobility group protein HMG-I/HMG-Y isoform a [Homo sapiens].
ACCESSION   NP_001306010
VERSION     NP_001306010.1
DBSOURCE    REFSEQ: accession NM_001319081.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Olan,I., Ando-Kuri,M., Parry,A.J., Handa,T., Schoenfelder,S.,
            Fraser,P., Ohkawa,Y., Kimura,H., Narita,M. and Narita,M.
  TITLE     HMGA1 orchestrates chromatin compartmentalization and sequesters
            genes into 3D networks coordinating senescence heterogeneity
  JOURNAL   Nat Commun 15 (1), 6891 (2024)
   PUBMED   39134516
  REMARK    GeneRIF: HMGA1 orchestrates chromatin compartmentalization and
            sequesters genes into 3D networks coordinating senescence
            heterogeneity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Li,K.J., Hong,Y., Yu,Y.Z., Xie,Z., Lv,D.J., Wang,C., Xie,T.,
            Chen,H., Chen,Z.S., Zeng,J. and Zhao,S.C.
  TITLE     NAT10 Promotes Prostate Cancer Growth and Metastasis by Acetylating
            mRNAs of HMGA1 and KRT8
  JOURNAL   Adv Sci (Weinh) 11 (32), e2310131 (2024)
   PUBMED   38922788
  REMARK    GeneRIF: NAT10 Promotes Prostate Cancer Growth and Metastasis by
            Acetylating mRNAs of HMGA1 and KRT8.
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Wang,L., Zhang,J., Xia,M., Liu,C., Zu,X. and Zhong,J.
  TITLE     High Mobility Group A1 (HMGA1): Structure, Biological Function, and
            Therapeutic Potential
  JOURNAL   Int J Biol Sci 18 (11), 4414-4431 (2022)
   PUBMED   35864955
  REMARK    GeneRIF: High Mobility Group A1 (HMGA1): Structure, Biological
            Function, and Therapeutic Potential.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 107)
  AUTHORS   Sumter,T.F., Xian,L., Huso,T., Koo,M., Chang,Y.T., Almasri,T.N.,
            Chia,L., Inglis,C., Reid,D. and Resar,L.M.
  TITLE     The High Mobility Group A1 (HMGA1) Transcriptome in Cancer and
            Development
  JOURNAL   Curr Mol Med 16 (4), 353-393 (2016)
   PUBMED   26980699
  REMARK    Review article
REFERENCE   6  (residues 1 to 107)
  AUTHORS   Friedmann,M., Holth,L.T., Zoghbi,H.Y. and Reeves,R.
  TITLE     Organization, inducible-expression and chromosome localization of
            the human HMG-I(Y) nonhistone protein gene
  JOURNAL   Nucleic Acids Res 21 (18), 4259-4267 (1993)
   PUBMED   8414980
REFERENCE   7  (residues 1 to 107)
  AUTHORS   Nissen,M.S., Langan,T.A. and Reeves,R.
  TITLE     Phosphorylation by cdc2 kinase modulates DNA binding activity of
            high mobility group I nonhistone chromatin protein
  JOURNAL   J Biol Chem 266 (30), 19945-19952 (1991)
   PUBMED   1939057
REFERENCE   8  (residues 1 to 107)
  AUTHORS   Reeves,R. and Nissen,M.S.
  TITLE     The A.T-DNA-binding domain of mammalian high mobility group I
            chromosomal proteins. A novel peptide motif for recognizing DNA
            structure
  JOURNAL   J Biol Chem 265 (15), 8573-8582 (1990)
   PUBMED   1692833
REFERENCE   9  (residues 1 to 107)
  AUTHORS   Eckner,R. and Birnstiel,M.L.
  TITLE     Cloning of cDNAs coding for human HMG I and HMG Y proteins: both
            are capable of binding to the octamer sequence motif
  JOURNAL   Nucleic Acids Res 17 (15), 5947-5959 (1989)
   PUBMED   2505228
REFERENCE   10 (residues 1 to 107)
  AUTHORS   Johnson,K.R., Lehn,D.A. and Reeves,R.
  TITLE     Alternative processing of mRNAs encoding mammalian chromosomal
            high-mobility-group proteins HMG-I and HMG-Y
  JOURNAL   Mol Cell Biol 9 (5), 2114-2123 (1989)
   PUBMED   2701943
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA049639.1, CX785762.1,
            AL354740.29 and BC008832.2.
            
            Summary: This gene encodes a chromatin-associated protein involved
            in the regulation of gene transcription, integration of
            retroviruses into chromosomes, and the metastatic progression of
            cancer cells. The encoded protein preferentially binds to the minor
            groove of AT-rich regions in double-stranded DNA. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. Pseudogenes of this gene have been identified on
            multiple chromosomes. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (13) uses an alternate splice site
            and lacks an exon in the 5' UTR compared to variant 1. Variants 1,
            3, 9, 10, 12, and 13 encode isoform (a, also called HMG-I).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.449045.1, CX785762.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..107
                     /product="high mobility group protein HMG-I/HMG-Y isoform
                     a"
                     /note="nonhistone chromosomal high-mobility group protein
                     HMG-I/HMG-Y; high mobility group protein HMG-I/HMG-Y; high
                     mobility group protein R; high mobility group protein A1"
                     /calculated_mol_wt=11545
     Region          1..107
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17096.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P17095; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            7
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P17095; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            15
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            26
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:12653562,
                     ECO:0000269|PubMed:15835918; Omega-N-methylarginine,
                     alternate. /evidence=ECO:0000269|PubMed:12653562,
                     ECO:0000269|PubMed:15835918; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by HIPK2 and CDC2.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P17096.3)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17960875,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P17096.3)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P17096.3)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Region          53..77
                     /region_name="Interaction with HIPK2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P17096.3)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by HIPK2 and CDC2.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P17096.3)"
     Site            58
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6, alternate.
                     /evidence=ECO:0000269|PubMed:16159886;
                     Omega-N-methylarginine, by PRMT6, alternate.
                     /evidence=ECO:0000269|PubMed:16159886; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            60
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6, alternate.
                     /evidence=ECO:0000269|PubMed:16159886;
                     Omega-N-methylarginine, by PRMT6, alternate.
                     /evidence=ECO:0000269|PubMed:16159886; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17960875; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by HIPK2 and CDC2.
                     /evidence=ECO:0000269|PubMed:12653562; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15835918,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P17096.3)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK.
                     /evidence=ECO:0000269|PubMed:15835918,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P17096.3)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK.
                     /evidence=ECO:0000269|PubMed:15835918,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     CDS             1..107
                     /gene="HMGA1"
                     /gene_synonym="HMG-R; HMGA1A; HMGIY"
                     /coded_by="NM_001319081.2:134..457"
                     /note="isoform a is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS4789.1"
                     /db_xref="GeneID:3159"
                     /db_xref="HGNC:HGNC:5010"
                     /db_xref="MIM:600701"
ORIGIN      
        1 msessskssq plaskqekdg tekrgrgrpr kqppvspgta lvgsqkepse vptpkrprgr
       61 pkgsknkgaa ktrkttttpg rkprgrpkkl ekeeeegisq esseeeq
//
LOCUS       NP_001163878             109 aa            linear   PRI 21-NOV-2025
DEFINITION  cyclin-dependent kinase 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001163878
VERSION     NP_001163878.1
DBSOURCE    REFSEQ: accession NM_001170407.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Zhou,L., Chen,Z., Zou,Y., Zhang,X., Wang,Z., Zhu,H., Lin,J.,
            Huang,Z., Zheng,L., Chen,J., Xie,M., Zhang,M., Zhang,R., Zhu,M.,
            Wang,Z., Zhou,H., Gao,S., Yin,Y., Wu,Y. and Kang,T.
  TITLE     ASB7 is a negative regulator of H3K9me3 homeostasis
  JOURNAL   Science 389 (6757), 309-316 (2025)
   PUBMED   40440427
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Van Matre,S., Huq,S., Akana,L., Eldridge,D.E., Zuniga,O.,
            Rodrigues,H. and Wolfe,A.R.
  TITLE     Enhanced radiosensitivity of pancreatic cancer achieved through
            inhibition of Cyclin-dependent kinase 1
  JOURNAL   Radiother Oncol 200, 110531 (2024)
   PUBMED   39270987
  REMARK    GeneRIF: Enhanced radiosensitivity of pancreatic cancer achieved
            through inhibition of Cyclin-dependent kinase 1.
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Vishwakarma,K.K., Kolthur,U.S. and Venkatramani,R.
  TITLE     Multiple Functional Protein-Protein Interaction Interfaces
            Allosterically Regulate ATP-Binding in Cyclin-Dependent Kinase-1
  JOURNAL   Proteins 92 (11), 1329-1342 (2024)
   PUBMED   39012208
  REMARK    GeneRIF: Multiple Functional Protein-Protein Interaction Interfaces
            Allosterically Regulate ATP-Binding in Cyclin-Dependent Kinase-1.
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Luo,C., He,J., Yang,Y., Wu,K., Fu,X., Cheng,J., Ming,Y., Liu,W. and
            Peng,Y.
  TITLE     SRSF9 promotes cell proliferation and migration of glioblastoma
            through enhancing CDK1 expression
  JOURNAL   J Cancer Res Clin Oncol 150 (6), 292 (2024)
   PUBMED   38842611
  REMARK    GeneRIF: SRSF9 promotes cell proliferation and migration of
            glioblastoma through enhancing CDK1 expression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 109)
  AUTHORS   Parker,L.L. and Piwnica-Worms,H.
  TITLE     Inactivation of the p34cdc2-cyclin B complex by the human WEE1
            tyrosine kinase
  JOURNAL   Science 257 (5078), 1955-1957 (1992)
   PUBMED   1384126
REFERENCE   6  (residues 1 to 109)
  AUTHORS   Dutta,A. and Stillman,B.
  TITLE     cdc2 family kinases phosphorylate a human cell DNA replication
            factor, RPA, and activate DNA replication
  JOURNAL   EMBO J 11 (6), 2189-2199 (1992)
   PUBMED   1318195
REFERENCE   7  (residues 1 to 109)
  AUTHORS   Pagano,M., Pepperkok,R., Verde,F., Ansorge,W. and Draetta,G.
  TITLE     Cyclin A is required at two points in the human cell cycle
  JOURNAL   EMBO J 11 (3), 961-971 (1992)
   PUBMED   1312467
REFERENCE   8  (residues 1 to 109)
  AUTHORS   Azzi,L., Meijer,L., Reed,S.I., Pidikiti,R. and Tung,H.Y.
  TITLE     Interaction between the cell-cycle-control proteins p34cdc2 and
            p9CKShs2. Evidence for two cooperative binding domains in p9CKShs2
  JOURNAL   Eur J Biochem 203 (3), 353-360 (1992)
   PUBMED   1310466
REFERENCE   9  (residues 1 to 109)
  AUTHORS   Nazarenko,S.A., Ostroverhova,N.V. and Spurr,N.K.
  TITLE     Regional assignment of the human cell cycle control gene CDC2 to
            chromosome 10q21 by in situ hybridization
  JOURNAL   Hum Genet 87 (5), 621-622 (1991)
   PUBMED   1916766
REFERENCE   10 (residues 1 to 109)
  AUTHORS   Lee,M.G. and Nurse,P.
  TITLE     Complementation used to clone a human homologue of the fission
            yeast cell cycle control gene cdc2
  JOURNAL   Nature 327 (6117), 31-35 (1987)
   PUBMED   3553962
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG723076.1, AK295741.1,
            AA459484.1 and AC022390.9.
            
            Summary: The protein encoded by this gene is a member of the
            Ser/Thr protein kinase family. This protein is a catalytic subunit
            of the highly conserved protein kinase complex known as M-phase
            promoting factor (MPF), which is essential for G2/M phase
            transitions of eukaryotic cell cycle. Mitotic cyclins stably
            associate with this protein and function as regulatory subunits.
            The kinase activity of this protein is controlled by cyclin
            accumulation and destruction through the cell cycle. The
            phosphorylation and dephosphorylation of this protein also play
            important regulatory roles in cell cycle control. Alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2023].
            
            Transcript Variant: This variant (5) differs in the 3' coding
            region and 3' UTR, compared to variant 1. The resulting isoform (4)
            has a distinct C-terminus and is shorter than isoform 1. Both
            variants 4 and 5 encode the same isoform (4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2722666.1,
                                           SRR18074969.2879222.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.2"
     Protein         1..109
                     /product="cyclin-dependent kinase 1 isoform 4"
                     /EC_number="2.7.11.23"
                     /EC_number="2.7.11.22"
                     /note="cell division cycle 2, G1 to S and G2 to M; cell
                     division control protein 2 homolog; p34 protein kinase;
                     cell cycle controller CDC2; cell division protein kinase
                     1"
                     /calculated_mol_wt=12335
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P06493.3)"
     Region          3..>106
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by PKR.
                     /evidence=ECO:0000269|PubMed:20395957; propagated from
                     UniProtKB/Swiss-Prot (P06493.3)"
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P06493.3)"
     Site            9
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P11440; propagated from
                     UniProtKB/Swiss-Prot (P06493.3)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKMYT1.
                     /evidence=ECO:0000269|PubMed:7569953,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (P06493.3)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by PKMYT1, WEE1, WEE2 and
                     PKC/PRKCD. /evidence=ECO:0000269|PubMed:19917613,
                     ECO:0000269|PubMed:29606300, ECO:0000269|PubMed:7569953,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (P06493.3)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P06493.3)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P06493.3)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P06493.3)"
     CDS             1..109
                     /gene="CDK1"
                     /gene_synonym="CDC2; CDC28A; P34CDC2"
                     /coded_by="NM_001170407.2:119..448"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:983"
                     /db_xref="HGNC:HGNC:1722"
                     /db_xref="MIM:116940"
ORIGIN      
        1 medytkieki gegtygvvyk grhkttgqvv amkkirlese eegvpstair eisllkelrh
       61 pnivslqdvl mqdsrlylif eflsmdlkky ldsippgqym dsslvkvka
//
LOCUS       NP_001362682             322 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform eeee [Homo sapiens].
ACCESSION   NP_001362682
VERSION     NP_001362682.1
DBSOURCE    REFSEQ: accession NM_001375753.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 322)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 322)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 322)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 322)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.206482.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2156670, SAMEA2159764
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..322
                     /product="abl interactor 2 isoform eeee"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=35079
     Region          19..82
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          262..>296
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     CDS             1..322
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375753.1:468..1436"
                     /note="isoform eeee is encoded by transcript variant 88"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 mldiqasqlr rmessinhis qtvdihkekv arreigiltt nkntsrthki iapanlerpv
       61 ryirkpidyt ilddighgvk vstqnmkmgg lprttpptqk ppsppmsgkg tlgssgssgg
      121 shpssrsssr ensgsgsvgv piavptpspp svfpghpvqf ysmnrpasrh tpptiggslp
      181 yrrppsitsq tslqnqmngg pfysqnpvsd tppppppvee pvfdespppp pppedyeeee
      241 aavveysdpy aeedppwapr sylekvvaiy dytkdkedel sfqegaiiyv ikknddvlkt
      301 kqaeseqmdl saiictmlsc ld
//
LOCUS       NP_742112                492 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 5 [Homo sapiens].
ACCESSION   NP_742112
VERSION     NP_742112.1
DBSOURCE    REFSEQ: accession NM_172114.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 492)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 492)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 492)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 492)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 492)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 492)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AI057019.1, DA113081.1,
            AB209288.1 and BC032784.1.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB209288.1, SRR1803613.201015.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..492
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 5"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=55529
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          360..487
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..492
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_172114.2:671..2149"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS47127.1"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkep qttvihnpdg nkestessnt tiededvkar
      361 kqeiikvteq lieainngdf eaytkicdpg ltafepealg nlvegmdfhr fyfenalsks
      421 nkpihtiiln phvhlvgdda aciayirltq ymdgsgmpkt mqseetrvwh rrdgkwqnvh
      481 fhrsgsptvp ik
//
LOCUS       NP_001358210             226 aa            linear   PRI 21-NOV-2025
DEFINITION  V-type proton ATPase subunit E 2 [Homo sapiens].
ACCESSION   NP_001358210 XP_016860715
VERSION     NP_001358210.1
DBSOURCE    REFSEQ: accession NM_001371281.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Hohn,A., Sittig,A., Jung,T., Grimm,S. and Grune,T.
  TITLE     Lipofuscin is formed independently of macroautophagy and lysosomal
            activity in stress-induced prematurely senescent human fibroblasts
  JOURNAL   Free Radic Biol Med 53 (9), 1760-1769 (2012)
   PUBMED   22982048
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Kawasaki-Nishi,S., Nishi,T. and Forgac,M.
  TITLE     Proton translocation driven by ATP hydrolysis in V-ATPases
  JOURNAL   FEBS Lett 545 (1), 76-85 (2003)
   PUBMED   12788495
  REMARK    Review article
REFERENCE   7  (residues 1 to 226)
  AUTHORS   Imai-Senga,Y., Sun-Wada,G.H., Wada,Y. and Futai,M.
  TITLE     A human gene, ATP6E1, encoding a testis-specific isoform of
            H(+)-ATPase subunit E
  JOURNAL   Gene 289 (1-2), 7-12 (2002)
   PUBMED   12036578
REFERENCE   8  (residues 1 to 226)
  AUTHORS   Nishi,T. and Forgac,M.
  TITLE     The vacuolar (H+)-ATPases--nature's most versatile proton pumps
  JOURNAL   Nat Rev Mol Cell Biol 3 (2), 94-103 (2002)
   PUBMED   11836511
  REMARK    Review article
REFERENCE   9  (residues 1 to 226)
  AUTHORS   Breton,S., Wiederhold,T., Marshansky,V., Nsumu,N.N., Ramesh,V. and
            Brown,D.
  TITLE     The B1 subunit of the H+ATPase is a PDZ domain-binding protein.
            Colocalization with NHE-RF in renal B-intercalated cells
  JOURNAL   J Biol Chem 275 (24), 18219-18224 (2000)
   PUBMED   10748165
  REMARK    GeneRIF: Rat vacuolar H(+)ATPase associates with NHE-RF (Na(+)/H(+)
            exchanger regulatory factor); the E subunit was
            co-immunoprecipitated from rat kidney cytosol with NHE-RF
            antibodies.
REFERENCE   10 (residues 1 to 226)
  AUTHORS   Dautry-Varsat,A.
  TITLE     Receptor-mediated endocytosis: the intracellular journey of
            transferrin and its receptor
  JOURNAL   Biochimie 68 (3), 375-381 (1986)
   PUBMED   2874839
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC018682.4.
            
            On Jul 6, 2019 this sequence version replaced XP_016860715.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.70106.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2147975
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p21"
     Protein         1..226
                     /product="V-type proton ATPase subunit E 2"
                     /note="vacuolar-type proton-translocating ATPase subunit
                     E1; V-ATPase subunit E 2; vacuolar proton pump subunit E
                     2; ATPase, H+ transporting, lysosomal 31kDa, V1 subunit
                     E2; testis secretory sperm-binding protein Li 235P"
                     /calculated_mol_wt=25943
     Region          18..216
                     /region_name="vATP-synt_E"
                     /note="ATP synthase (E/31 kDa) subunit; pfam01991"
                     /db_xref="CDD:396537"
     CDS             1..226
                     /gene="ATP6V1E2"
                     /gene_synonym="ATP6E1; ATP6EL2; ATP6V1EL2; VMA4"
                     /coded_by="NM_001371281.1:1677..2357"
                     /db_xref="CCDS:CCDS1826.1"
                     /db_xref="GeneID:90423"
                     /db_xref="HGNC:HGNC:18125"
                     /db_xref="MIM:617385"
ORIGIN      
        1 malsdvdvkk qikhmmafie qeanekaeei dakaeeefni ekgrlvqtqr lkimeyyekk
       61 ekqieqqkki lmstmrnqar lkvlrarndl isdllseakl rlsrivedpe vyqglldklv
      121 lqgllrllep vmivrcrpqd lllveaavqk aipeymtisq khvevqidke aylavnaagg
      181 vevysgnqri kvsntlesrl dlsakqkmpe irmalfgant nrkffi
//
LOCUS       NP_062539                672 aa            linear   PRI 21-NOV-2025
DEFINITION  glycerophosphocholine phosphodiesterase GPCPD1 [Homo sapiens].
ACCESSION   NP_062539
VERSION     NP_062539.1
DBSOURCE    REFSEQ: accession NM_019593.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Glotzbach,A., Rohlf,K., Gonscharow,A., Luke,S., Demirci,O.,
            Begher-Tibbe,B., Overbeck,N., Reinders,J., Cadenas,C.,
            Hengstler,J.G., Edlund,K. and Marchan,R.
  TITLE     EDI3 knockdown in ER-HER2+ breast cancer cells reduces tumor burden
            and improves survival in two mouse models of experimental
            metastasis
  JOURNAL   Breast Cancer Res 26 (1), 87 (2024)
   PUBMED   38816770
  REMARK    GeneRIF: EDI3 knockdown in ER-HER2+ breast cancer cells reduces
            tumor burden and improves survival in two mouse models of
            experimental metastasis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 672)
  AUTHORS   Cikes,D., Leutner,M., Cronin,S.J.F., Novatchkova,M., Pfleger,L.,
            Klepochova,R., Lair,B., Lac,M., Bergoglio,C., Viguerie,N.,
            Durnberger,G., Roitinger,E., Grivej,M., Rullman,E., Gustafsson,T.,
            Hagelkruys,A., Tavernier,G., Bourlier,V., Knauf,C., Krebs,M.,
            Kautzky-Willer,A., Moro,C., Krssak,M., Orthofer,M. and
            Penninger,J.M.
  TITLE     Gpcpd1-GPC metabolic pathway is dysfunctional in aging and its
            deficiency severely perturbs glucose metabolism
  JOURNAL   Nat Aging 4 (1), 80-94 (2024)
   PUBMED   38238601
  REMARK    GeneRIF: Gpcpd1-GPC metabolic pathway is dysfunctional in aging and
            its deficiency severely perturbs glucose metabolism.
REFERENCE   4  (residues 1 to 672)
  AUTHORS   Liu,Y., Zhang,H., Liu,Y., Zhang,S., Su,P., Wang,L., Li,Y.,
            Liang,Y., Wang,X., Zhao,W., Chen,B., Luo,D., Zhang,N. and Yang,Q.
  TITLE     Hypoxia-induced GPCPD1 depalmitoylation triggers mitophagy via
            regulating PRKN-mediated ubiquitination of VDAC1
  JOURNAL   Autophagy 19 (9), 2443-2463 (2023)
   PUBMED   36803235
  REMARK    GeneRIF: Hypoxia-induced GPCPD1 depalmitoylation triggers mitophagy
            via regulating PRKN-mediated ubiquitination of VDAC1.
REFERENCE   5  (residues 1 to 672)
  AUTHORS   Keller,M., Rohlf,K., Glotzbach,A., Leonhardt,G., Luke,S.,
            Derksen,K., Demirci,O., Gocener,D., AlWahsh,M., Lambert,J.,
            Lindskog,C., Schmidt,M., Brenner,W., Baumann,M., Zent,E.,
            Zischinsky,M.L., Hellwig,B., Madjar,K., Rahnenfuhrer,J.,
            Overbeck,N., Reinders,J., Cadenas,C., Hengstler,J.G., Edlund,K. and
            Marchan,R.
  TITLE     Inhibiting the glycerophosphodiesterase EDI3 in ER-HER2+ breast
            cancer cells resistant to HER2-targeted therapy reduces viability
            and tumour growth
  JOURNAL   J Exp Clin Cancer Res 42 (1), 25 (2023)
   PUBMED   36670508
  REMARK    GeneRIF: Inhibiting the glycerophosphodiesterase EDI3 in ER-HER2+
            breast cancer cells resistant to HER2-targeted therapy reduces
            viability and tumour growth.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 672)
  AUTHORS   Lesjak,M.S., Marchan,R., Stewart,J.D., Rempel,E., Rahnenfuhrer,J.
            and Hengstler,J.G.
  TITLE     EDI3 links choline metabolism to integrin expression, cell adhesion
            and spreading
  JOURNAL   Cell Adh Migr 8 (5), 499-508 (2014)
   PUBMED   25482527
  REMARK    GeneRIF: EDI3 links choline metabolism to integrin expression, cell
            adhesion and spreading
REFERENCE   7  (residues 1 to 672)
  AUTHORS   Stewart,J.D., Marchan,R., Lesjak,M.S., Lambert,J., Hergenroeder,R.,
            Ellis,J.K., Lau,C.H., Keun,H.C., Schmitz,G., Schiller,J.,
            Eibisch,M., Hedberg,C., Waldmann,H., Lausch,E., Tanner,B.,
            Sehouli,J., Sagemueller,J., Staude,H., Steiner,E. and
            Hengstler,J.G.
  TITLE     Choline-releasing glycerophosphodiesterase EDI3 drives tumor cell
            migration and metastasis
  JOURNAL   Proc Natl Acad Sci U S A 109 (21), 8155-8160 (2012)
   PUBMED   22570503
  REMARK    GeneRIF: We have identified EDI3, a key enzyme controlling GPC and
            choline metabolism; Because inhibition of it corrects the GPC/PC
            ratio and decreases the migration capacity of tumor cells, it
            represents a possible target for therapeutic intervention.
REFERENCE   8  (residues 1 to 672)
  AUTHORS   Bakken,T.E., Roddey,J.C., Djurovic,S., Akshoomoff,N., Amaral,D.G.,
            Bloss,C.S., Casey,B.J., Chang,L., Ernst,T.M., Gruen,J.R.,
            Jernigan,T.L., Kaufmann,W.E., Kenet,T., Kennedy,D.N.,
            Kuperman,J.M., Murray,S.S., Sowell,E.R., Rimol,L.M.,
            Mattingsdal,M., Melle,I., Agartz,I., Andreassen,O.A., Schork,N.J.,
            Dale,A.M., Weiner,M., Aisen,P., Petersen,R., Jack,C.R. Jr.,
            Jagust,W., Trojanowki,J.Q., Toga,A.W., Beckett,L., Green,R.C.,
            Saykin,A.J., Morris,J., Liu,E., Montine,T., Gamst,A., Thomas,R.G.,
            Donohue,M., Walter,S., Gessert,D., Sather,T., Harvey,D., Kornak,J.,
            Dale,A., Bernstein,M., Felmlee,J., Fox,N., Thompson,P., Schuff,N.,
            Alexander,G., DeCarli,C., Bandy,D., Koeppe,R.A., Foster,N.,
            Reiman,E.M., Chen,K., Mathis,C., Cairns,N.J., Taylor-Reinwald,L.,
            Trojanowki,J.Q., Shaw,L., Lee,V.M., Korecka,M., Crawford,K.,
            Neu,S., Foroud,T.M., Potkin,S., Shen,L., Kachaturian,Z., Frank,R.,
            Snyder,P.J., Molchan,S., Kaye,J., Quinn,J., Lind,B., Dolen,S.,
            Schneider,L.S., Pawluczyk,S., Spann,B.M., Brewer,J., Vanderswag,H.,
            Heidebrink,J.L., Lord,J.L., Johnson,K., Doody,R.S.,
            Villanueva-Meyer,J., Chowdhury,M., Stern,Y., Honig,L.S., Bell,K.L.,
            Morris,J.C., Ances,B., Carroll,M., Leon,S., Mintun,M.A.,
            Schneider,S., Marson,D., Griffith,R., Clark,D., Grossman,H.,
            Mitsis,E., Romirowsky,A., deToledo-Morrell,L., Shah,R.C., Duara,R.,
            Varon,D., Roberts,P., Albert,M., Onyike,C., Kielb,S., Rusinek,H.,
            de Leon,M.J., Glodzik,L., De Santi,S., Doraiswamy,P.M.,
            Petrella,J.R., Coleman,R.E., Arnold,S.E., Karlawish,J.H., Wolk,D.,
            Smith,C.D., Jicha,G., Hardy,P., Lopez,O.L., Oakley,M.,
            Simpson,D.M., Porsteinsson,A.P., Goldstein,B.S., Martin,K.,
            Makino,K.M., Ismail,M.S., Brand,C., Mulnard,R.A., Thai,G.,
            Mc-Adams-Ortiz,C., Womack,K., Mathews,D., Quiceno,M.,
            Diaz-Arrastia,R., King,R., Weiner,M., Martin-Cook,K., DeVous,M.,
            Levey,A.I., Lah,J.J., Cellar,J.S., Burns,J.M., Anderson,H.S.,
            Swerdlow,R.H., Apostolova,L., Lu,P.H., Bartzokis,G.,
            Silverman,D.H., Graff-Radford,N.R., Parfitt,F., Johnson,H.,
            Farlow,M.R., Hake,A.M., Matthews,B.R., Herring,S., van Dyck,C.H.,
            Carson,R.E., MacAvoy,M.G., Chertkow,H., Bergman,H., Hosein,C.,
            Black,S., Stefanovic,B., Caldwell,C., Ging-Yuek, Hsiung,R.,
            Feldman,H., Mudge,B., Assaly,M., Kertesz,A., Rogers,J., Trost,D.,
            Bernick,C., Munic,D., Kerwin,D., Mesulam,M.M., Lipowski,K.,
            Wu,C.K., Johnson,N., Sadowsky,C., Martinez,W., Villena,T.,
            Turner,R.S., Johnson,K., Reynolds,B., Sperling,R.A., Johnson,K.A.,
            Marshall,G., Frey,M., Yesavage,J., Taylor,J.L., Lane,B., Rosen,A.,
            Tinklenberg,J., Sabbagh,M., Belden,C., Jacobson,S., Kowall,N.,
            Killiany,R., Budson,A.E., Norbash,A., Johnson,P.L., Obisesan,T.O.,
            Wolday,S., Bwayo,S.K., Lerner,A., Hudson,L., Ogrocki,P.,
            Fletcher,E., Carmichael,O., Olichney,J., Kittur,S., Borrie,M.,
            Lee,T.Y., Bartha,R., Johnson,S., Asthana,S., Carlsson,C.M.,
            Potkin,S.G., Preda,A., Nguyen,D., Tariot,P., Fleisher,A.,
            Reeder,S., Bates,V., Capote,H., Rainka,M., Scharre,D.W., Kataki,M.,
            Zimmerman,E.A., Celmins,D., Brown,A.D., Pearlson,G.D., Blank,K.,
            Anderson,K., Santulli,R.B., Schwartz,E.S., Sink,K.M.,
            Williamson,J.D., Garg,P., Watkins,F., Ott,B.R., Querfurth,H.,
            Tremont,G., Salloway,S., Malloy,P., Correia,S., Rosen,H.J.,
            Miller,B.L., Mintzer,J., Longmire,C.F., Spicer,K., Finger,E.,
            Rachinsky,I., Drost,D., Jernigan,T., McCabe,C., Grant,E., Ernst,T.,
            Kuperman,J., Chung,Y., Murray,S., Bloss,C., Darst,B., Pritchett,L.,
            Saito,A., Amaral,D., DiNino,M., Eyngorina,B., Sowell,E.,
            Houston,S., Soderberg,L., Kaufmann,W., van Zijl,P.,
            Rizzo-Busack,H., Javid,M., Mehta,N., Ruberry,E., Powers,A.,
            Rosen,B., Gebhard,N., Manigan,H., Frazier,J., Kennedy,D.,
            Yakutis,L., Hill,M., Gruen,J., Bosson-Heenan,J. and Carlson,H.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative; Pediatric Imaging,
            Neurocognition, and Genetics Study
  TITLE     Association of common genetic variants in GPCPD1 with scaling of
            visual cortical surface area in humans
  JOURNAL   Proc Natl Acad Sci U S A 109 (10), 3985-3990 (2012)
   PUBMED   22343285
  REMARK    GeneRIF: common genetic variants in GPCPD1 are associated with
            scaling of visual cortical surface area in humans
REFERENCE   9  (residues 1 to 672)
  AUTHORS   Okazaki,Y., Ohshima,N., Yoshizawa,I., Kamei,Y., Mariggio,S.,
            Okamoto,K., Maeda,M., Nogusa,Y., Fujioka,Y., Izumi,T., Ogawa,Y.,
            Shiro,Y., Wada,M., Kato,N., Corda,D. and Yanaka,N.
  TITLE     A novel glycerophosphodiester phosphodiesterase, GDE5, controls
            skeletal muscle development via a non-enzymatic mechanism
  JOURNAL   J Biol Chem 285 (36), 27652-27663 (2010)
   PUBMED   20576599
REFERENCE   10 (residues 1 to 672)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC027588.2, BI561344.1, AL049446.1, AB037855.1, BG674365.1,
            T79323.1 and BP421674.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB037855.1, SRR11853563.20187.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379019.7/ ENSP00000368305.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.3"
     Protein         1..672
                     /product="glycerophosphocholine phosphodiesterase GPCPD1"
                     /EC_number="3.1.4.2"
                     /note="preimplantation protein 4; glycerophosphocholine
                     phosphodiesterase GDE1 homolog; putative
                     glycerophosphodiester phosphodiesterase 5; putative
                     glycerophosphocholine phosphodiesterase GPCPD1;
                     endometrial differential 3"
                     /calculated_mol_wt=75904
     Region          4..127
                     /region_name="CBM20_Prei4"
                     /note="Prei4, N-terminal CBM20 (carbohydrate-binding
                     module, family 20) domain. Preimplantation protein 4
                     (Prei4) is a protein of unknown function that is expressed
                     during mouse preimplantation embryogenesis. In addition to
                     the N-terminal CBM20 domain, Prei4...; cd05814"
                     /db_xref="CDD:99888"
     Site            order(14..19,42,50,52)
                     /site_type="other"
                     /note="starch binding site 2 [chemical binding]"
                     /db_xref="CDD:99888"
     Site            order(32,67,90..91,96)
                     /site_type="other"
                     /note="starch binding site 1 [chemical binding]"
                     /db_xref="CDD:99888"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NPB8.2)"
     Region          319..611
                     /region_name="GDPD_GDE5"
                     /note="Glycerophosphodiester phosphodiesterase domain of
                     putative mammalian glycerophosphodiester phosphodiesterase
                     GDE5 and similar proteins; cd08607"
                     /db_xref="CDD:176549"
     Site            order(323,358,360,373,457,502,585)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176549"
     Site            order(323,373)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176549"
     Site            order(358,360,457)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:176549"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0L9; propagated from
                     UniProtKB/Swiss-Prot (Q9NPB8.2)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0L9; propagated from
                     UniProtKB/Swiss-Prot (Q9NPB8.2)"
     CDS             1..672
                     /gene="GPCPD1"
                     /gene_synonym="EDI3; GDE5; GDPD6; PREI4"
                     /coded_by="NM_019593.5:194..2212"
                     /db_xref="CCDS:CCDS13090.1"
                     /db_xref="GeneID:56261"
                     /db_xref="HGNC:HGNC:26957"
                     /db_xref="MIM:614124"
ORIGIN      
        1 mtpsqvafei rgtllpgevf aicgscdalg nwnpqnaval lpendtgesm lwkativlsr
       61 gvsvqyryfk gyflepktig gpcqvivhkw ethlqprsit pleseiiidd gqfgihngve
      121 tldsgwltcq teirlrlhys ekppvsitkk klkksrfrvk ltlegleedd ddrvsptvlh
      181 kmsnsleisl isdnefkcrh sqpecgyglq pdrwteysiq tmepdnleli fdffeedlse
      241 hvvqgdalpg hvgtacllss tiaesgksag iltlpimsrn srktigkvrv dyiiikplpg
      301 yscdmkssfs kywkpripld vghrgagnst ttaqlakvqe ntiaslrnaa shgaafvefd
      361 vhlskdfvpv vyhdltcclt mkkkfdadpv elfeipvkel tfdqlqllkl thvtalkskd
      421 rkesvvqeen sfsenqpfps lkmvleslpe dvgfnieikw icqqrdgmwd gnlstyfdmn
      481 lfldiilktv lensgkrriv fssfdadict mvrqkqnkyp ilfltqgkse iypelmdlrs
      541 rttpiamsfa qfenllginv htedllrnps yiqeakakgl vifcwgddtn dpenrrklke
      601 lgvngliydr iydwmpeqpn ifqveqlerl kqelpelksc lcptvsrfvp sslcgesdih
      661 vdangidnve na
//
LOCUS       NP_861546                590 aa            linear   PRI 21-NOV-2025
DEFINITION  merlin isoform 2 [Homo sapiens].
ACCESSION   NP_861546
VERSION     NP_861546.1
DBSOURCE    REFSEQ: accession NM_181825.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 590)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 590)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 590)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 590)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 590)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 590)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 590)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 590)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF369701.1.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Transcript Variant: This variant (12) includes an alternate exon
            and differs in the 3' UTR, compared to variant 1. The resulting
            protein (isoform 2), one of the two predominant isoforms, has a
            distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF369701.1, AF369662.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..590
                     /product="merlin isoform 2"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=68959
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35240.1)"
     Region          23..222
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          216..312
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(258..259,261..267,276,297,300..301,304)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(258,261..268,276,297,300..301,304)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(294,298)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            297..312
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          307..>367
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          346..465
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          518..>579
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PAK.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (P35240.1)"
     CDS             1..590
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_181825.3:367..2139"
                     /note="isoform 2 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS13862.1"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 magaiasrms fsslkrkqpk tftvrivtmd aemefncemk wkgkdlfdlv crtlglretw
       61 ffglqytikd tvawlkmdkk vldhdvskee pvtfhflakf ypenaeeelv qeitqhlffl
      121 qvkkqildek iycppeasvl lasyavqaky gdydpsvhkr gflaqeellp krvinlyqmt
      181 pemweerita wyaehrgrar deaemeylki aqdlemygvn yfairnkkgt elllgvdalg
      241 lhiydpenrl tpkisfpwne irnisysdke ftikpldkki dvfkfnsskl rvnklilqlc
      301 ignhdlfmrr rkadslevqq mkaqareeka rkqmerqrla rekqmreeae rtrdelerrl
      361 lqmkeeatma nealmrseet adllaekaqi teeeakllaq kaaeaeqemq rikatairte
      421 eekrlmeqkv leaevlalkm aeeserrake adqlkqdlqe areaerrakq klleiatkpt
      481 yppmnpipap lppdipsfnl igdslsfdfk dtdmkrlsme iekekveyme kskhlqeqln
      541 elkteiealk lkeretaldi lhnensdrgg sskhntikkp qaqgrrpici
//
LOCUS       NP_001248342             401 aa            linear   PRI 21-NOV-2025
DEFINITION  dynactin subunit 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001248342
VERSION     NP_001248342.1
DBSOURCE    REFSEQ: accession NM_001261413.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Xu,S., Xing,J., Li,K., Qiao,L., Zhang,C., Ren,Y. and Liu,Y.
  TITLE     Pan-cancer analysis of DCTN2 and its tumour-promoting role in HCC
            by modulating the AKT pathway
  JOURNAL   J Cell Mol Med 28 (11), e18450 (2024)
   PUBMED   38842133
  REMARK    GeneRIF: Pan-cancer analysis of DCTN2 and its tumour-promoting role
            in HCC by modulating the AKT pathway.
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Li,Y.F., Shi,L.J., Wang,P., Wang,J.W., Shi,G.Y. and Lee,S.C.
  TITLE     Binding between ROCK1 and DCTN2 triggers diabetes-associated
            centrosome amplification in colon cancer cells
  JOURNAL   Oncol Rep 46 (1) (2021)
   PUBMED   34080666
  REMARK    GeneRIF: Binding between ROCK1 and DCTN2 triggers
            diabetesassociated centrosome amplification in colon cancer cells.
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 401)
  AUTHORS   Eckley,D.M., Gill,S.R., Melkonian,K.A., Bingham,J.B., Goodson,H.V.,
            Heuser,J.E. and Schroer,T.A.
  TITLE     Analysis of dynactin subcomplexes reveals a novel actin-related
            protein associated with the arp1 minifilament pointed end
  JOURNAL   J Cell Biol 147 (2), 307-320 (1999)
   PUBMED   10525537
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Berrueta,L., Tirnauer,J.S., Schuyler,S.C., Pellman,D. and
            Bierer,B.E.
  TITLE     The APC-associated protein EB1 associates with components of the
            dynactin complex and cytoplasmic dynein intermediate chain
  JOURNAL   Curr Biol 9 (8), 425-428 (1999)
   PUBMED   10226031
REFERENCE   8  (residues 1 to 401)
  AUTHORS   Starr,D.A., Williams,B.C., Hays,T.S. and Goldberg,M.L.
  TITLE     ZW10 helps recruit dynactin and dynein to the kinetochore
  JOURNAL   J Cell Biol 142 (3), 763-774 (1998)
   PUBMED   9700164
REFERENCE   9  (residues 1 to 401)
  AUTHORS   Echeverri,C.J., Paschal,B.M., Vaughan,K.T. and Vallee,R.B.
  TITLE     Molecular characterization of the 50-kD subunit of dynactin reveals
            function for the complex in chromosome alignment and spindle
            organization during mitosis
  JOURNAL   J Cell Biol 132 (4), 617-633 (1996)
   PUBMED   8647893
REFERENCE   10 (residues 1 to 401)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB027733.1, BC009468.1 and
            DB569305.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a 50-kD subunit of dynactin, a
            macromolecular complex consisting of 10-11 subunits ranging in size
            from 22 to 150 kD. Dynactin binds to both microtubules and
            cytoplasmic dynein. It is involved in a diverse array of cellular
            functions, including ER-to-Golgi transport, the centripetal
            movement of lysosomes and endosomes, spindle formation, chromosome
            movement, nuclear positioning, and axonogenesis. This subunit is
            present in 4-5 copies per dynactin molecule. It contains three
            short alpha-helical coiled-coil domains that may mediate
            association with self or other dynactin subunits. It may interact
            directly with the largest subunit (p150) of dynactin and may affix
            p150 in place. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been found for this gene. [provided
            by RefSeq, May 2012].
            
            Transcript Variant: This variant (3) lacks two exons in the 5'
            coding region but maintains the reading frame, compared to variant
            1. The resulting isoform (3) lacks an internal segment, compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: GQ891494.1, BC000718.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000548249.6/ ENSP00000447824.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..401
                     /product="dynactin subunit 2 isoform 3"
                     /note="p50 dynamitin; dynactin complex 50 kDa subunit;
                     epididymis secretory protein Li 77; 50 kDa
                     dynein-associated polypeptide; dynactin 2 (p50);
                     epididymis secretory sperm binding protein"
                     /calculated_mol_wt=44100
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13561.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.7,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q13561.4)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15144186; propagated from
                     UniProtKB/Swiss-Prot (Q13561.4)"
     Region          16..399
                     /region_name="Dynamitin"
                     /note="pfam04912"
                     /db_xref="CDD:461477"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13561.4)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q99KJ8; propagated from
                     UniProtKB/Swiss-Prot (Q13561.4)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13561.4)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13561.4)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99KJ8; propagated from
                     UniProtKB/Swiss-Prot (Q13561.4)"
     CDS             1..401
                     /gene="DCTN2"
                     /gene_synonym="DCTN50; DYNAMITIN; HEL-S-77; RBP50"
                     /coded_by="NM_001261413.2:130..1335"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58245.1"
                     /db_xref="GeneID:10540"
                     /db_xref="HGNC:HGNC:2712"
                     /db_xref="MIM:607376"
ORIGIN      
        1 madpkyadlp giarnepdvy etsdlpeddq aefdaeelts tsvehiivnp naaydkfkdk
       61 rvgtkgldfs drigktkrtg yesgeyemlg eglgvketpq qkyqrllhev qeltteveki
      121 kttvkesate ekltpvllak qlaalkqqlv ashlekllgp daainltdpd galakrlllq
      181 leatknskgg sggkttgtpp dsslvtyelh srpeqdkfsq aakvaelekr lteletavrc
      241 dqdaqnplsa glqgaclmet vellqakvsa ldlavldqve arlqsvlgkv neiakhkasv
      301 edadtqskvh qlyetiqrws piastlpelv qrlvtikqlh eqamqfgqll thldttqqmi
      361 anslkdnttl ltqvqttmre nlatvegnfa sidermkklg k
//
LOCUS       NP_001229791             338 aa            linear   PRI 21-NOV-2025
DEFINITION  cAMP-dependent protein kinase catalytic subunit beta isoform 9
            [Homo sapiens].
ACCESSION   NP_001229791
VERSION     NP_001229791.1
DBSOURCE    REFSEQ: accession NM_001242862.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Tanaka,M., Takeshita,K., Kunita,A., Hasegawa,K. and Ushiku,T.
  TITLE     PRKACA/PRKACB Fusions in Pancreatobiliary Intraductal Oncocytic
            Papillary Neoplasms Including Those With Atypical Morphology: An
            Analysis of 22 Cases Expanding Morphologic Spectrum
  JOURNAL   Am J Surg Pathol 48 (8), 1032-1040 (2024)
   PUBMED   38841868
  REMARK    GeneRIF: PRKACA/PRKACB Fusions in Pancreatobiliary Intraductal
            Oncocytic Papillary Neoplasms Including Those With Atypical
            Morphology: An Analysis of 22 Cases Expanding Morphologic Spectrum.
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Pei,W., Yin,W., Yu,T., Zhang,X., Zhang,Q., Yang,X., Shi,C., Shen,W.
            and Liu,G.
  TITLE     Dual-Specificity Phosphatase 4 Promotes Malignant Features in
            Colorectal Cancer Through Cyclic-AMP Response Element Binding
            Protein/Protein Kinase CAMP-Activated Catalytic Subunit Beta
            Activation
  JOURNAL   Dig Dis Sci 69 (8), 2856-2874 (2024)
   PUBMED   38824257
  REMARK    GeneRIF: Dual-Specificity Phosphatase 4 Promotes Malignant Features
            in Colorectal Cancer Through Cyclic-AMP Response Element Binding
            Protein/Protein Kinase CAMP-Activated Catalytic Subunit Beta
            Activation.
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Itoh,T., Omori,Y., Seino,M., Hirose,K., Date,F., Ono,Y.,
            Mizukami,Y., Aoki,S., Ishida,M., Mizuma,M., Morikawa,T.,
            Higuchi,R., Honda,G., Okamura,Y., Kinoshita,K., Unno,M. and
            Furukawa,T.
  TITLE     Gene Rearrangement and Expression of PRKACA and PRKACB Govern
            Morphobiology of Pancreatobiliary Oncocytic Neoplasms
  JOURNAL   Mod Pathol 37 (1), 100358 (2024)
   PUBMED   37871652
  REMARK    GeneRIF: Gene Rearrangement and Expression of PRKACA and PRKACB
            Govern Morphobiology of Pancreatobiliary Oncocytic Neoplasms.
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Maimaitiaili,Y., Fukumura,Y., Hirabayashi,K., Kinowaki,Y.,
            Naito,Y., Saito,A., Rong,L., Nakahodo,J. and Yao,T.
  TITLE     Investigation of -PRKACA/-PRKACB fusion genes in oncocytic tumors
            of the pancreatobiliary and other systems
  JOURNAL   Virchows Arch 481 (6), 865-876 (2022)
   PUBMED   36152045
  REMARK    GeneRIF: Investigation of -PRKACA/-PRKACB fusion genes in oncocytic
            tumors of the pancreatobiliary and other systems.
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Orstavik,S., Reinton,N., Frengen,E., Langeland,B.T., Jahnsen,T. and
            Skalhegg,B.S.
  TITLE     Identification of novel splice variants of the human catalytic
            subunit Cbeta of cAMP-dependent protein kinase
  JOURNAL   Eur J Biochem 268 (19), 5066-5073 (2001)
   PUBMED   11589697
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Scarpetta,M.A. and Uhler,M.D.
  TITLE     Evidence for two additional isoforms of the endogenous protein
            kinase inhibitor of cAMP-dependent protein kinase in mouse
  JOURNAL   J Biol Chem 268 (15), 10927-10931 (1993)
   PUBMED   7684369
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Da Silva,J.D., Tkachenko,N. and Soares,A.R.
  TITLE     Ellis-van Creveld Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37903214
REFERENCE   8  (residues 1 to 338)
  AUTHORS   Simard,J., Berube,D., Sandberg,M., Grzeschik,K.H., Gagne,R.,
            Hansson,V. and Jahnsen,T.
  TITLE     Assignment of the gene encoding the catalytic subunit C beta of
            cAMP-dependent protein kinase to the p36 band on chromosome 1
  JOURNAL   Hum Genet 88 (6), 653-657 (1992)
   PUBMED   1551670
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Beebe,S.J., Oyen,O., Sandberg,M., Froysa,A., Hansson,V. and
            Jahnsen,T.
  TITLE     Molecular cloning of a tissue-specific protein kinase (C gamma)
            from human testis--representing a third isoform for the catalytic
            subunit of cAMP-dependent protein kinase
  JOURNAL   Mol Endocrinol 4 (3), 465-475 (1990)
   PUBMED   2342480
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Taylor,S.S., Buechler,J.A. and Yonemoto,W.
  TITLE     cAMP-dependent protein kinase: framework for a diverse family of
            regulatory enzymes
  JOURNAL   Annu Rev Biochem 59, 971-1005 (1990)
   PUBMED   2165385
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA228647.1, AK316115.1,
            BX641026.1 and AL450063.14.
            
            Summary: The protein encoded by this gene is a member of the
            serine/threonine protein kinase family. The encoded protein is a
            catalytic subunit of cAMP (cyclic AMP)-dependent protein kinase,
            which mediates signalling though cAMP. cAMP signaling is important
            to a number of processes, including cell proliferaton and
            differentiation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2014].
            
            Transcript Variant: This variant (9) differs in the 5' exon
            structure, compared to variant 1. The encoded isoform (9) has a
            distinct N-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.79815.1,
                                           SRR1803612.130609.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2150585
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.1"
     Protein         1..338
                     /product="cAMP-dependent protein kinase catalytic subunit
                     beta isoform 9"
                     /EC_number="2.7.11.11"
                     /note="protein kinase A catalytic subunit beta; protein
                     kinase, cAMP-dependent, catalytic, beta; protein kinase,
                     cAMP-dependent, beta catalytic subunit"
                     /calculated_mol_wt=39105
     Region          29..318
                     /region_name="STKc_PKA"
                     /note="Catalytic subunit of the Serine/Threonine Kinase,
                     cAMP-dependent protein kinase; cd14209"
                     /db_xref="CDD:271111"
     Site            order(37..43,45,58,60,92,108..111,115,154,156,158..159,
                     161,171..172,315)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271111"
     Site            order(38..43,45,58,60,70,92,108..109,111,115,117,121,154,
                     156..159,161,171..172,175,186,188..191,218,222..224,
                     227..229,231,234,315,318)
                     /site_type="active"
                     /db_xref="CDD:271111"
     Site            order(39,41..42,70..72,115,117,121,154,156..158,175,
                     186..191,218,222..224,227..229,231,234..235,318)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271111"
     Site            order(41,71..72,74..75,115,117,121,156..158,175,182,
                     184..189,192,199..201,218,231..232,235..236,239,318)
                     /site_type="other"
                     /note="regulatory subunit interface [polypeptide binding]"
                     /db_xref="CDD:271111"
     Site            171..191
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271111"
     CDS             1..338
                     /gene="PRKACB"
                     /gene_synonym="CAFD2; PKA C-beta; PKACB"
                     /coded_by="NM_001242862.3:24..1040"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS72816.1"
                     /db_xref="GeneID:5567"
                     /db_xref="HGNC:HGNC:9381"
                     /db_xref="MIM:176892"
ORIGIN      
        1 mlllsssisl ykdrnearli ssqnnagled ferkktlgtg sfgrvmlvkh kateqyyamk
       61 ildkqkvvkl kqiehtlnek rilqavnfpf lvrleyafkd nsnlymvmey vpggemfshl
      121 rrigrfseph arfyaaqivl tfeylhsldl iyrdlkpenl lidhqgyiqv tdfgfakrvk
      181 grtwtlcgtp eylapeiils kgynkavdww algvliyema agyppffadq piqiyekivs
      241 gkvrfpshfs sdlkdllrnl lqvdltkrfg nlkngvsdik thkwfattdw iaiyqrkvea
      301 pfipkfrgsg dtsnfddyee edirvsitek cakefgef
//
LOCUS       NP_001336016             659 aa            linear   PRI 21-NOV-2025
DEFINITION  TBC1 domain family member 5 isoform e [Homo sapiens].
ACCESSION   NP_001336016 XP_016863053
VERSION     NP_001336016.1
DBSOURCE    REFSEQ: accession NM_001349087.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Tu,Y.X.I., Sydor,A.M., Coyaud,E., Laurent,E.M.N., Dyer,D.,
            Mellouk,N., St-Germain,J., Vernon,R.M., Forman-Kay,J.D., Li,T.,
            Hua,R., Zhao,K., Ridgway,N.D., Kim,P.K., Raught,B. and Brumell,J.H.
  TITLE     Global Proximity Interactome of the Human Macroautophagy Pathway
  JOURNAL   Autophagy 18 (5), 1174-1186 (2022)
   PUBMED   34524948
REFERENCE   4  (residues 1 to 659)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 659)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 659)
  AUTHORS   Seaman,M.N., Harbour,M.E., Tattersall,D., Read,E. and Bright,N.
  TITLE     Membrane recruitment of the cargo-selective retromer subcomplex is
            catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP
            TBC1D5
  JOURNAL   J Cell Sci 122 (Pt 14), 2371-2382 (2009)
   PUBMED   19531583
  REMARK    GeneRIF: Membrane recruitment of the cargo-selective retromer
            subcomplex VPS35/29/26 is catalysed by the small GTPase Rab7 and
            inhibited by the Rab-GAP TBC1D5.
REFERENCE   7  (residues 1 to 659)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
REFERENCE   8  (residues 1 to 659)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   9  (residues 1 to 659)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 659)
  AUTHORS   Brill,L.M., Salomon,A.R., Ficarro,S.B., Mukherji,M.,
            Stettler-Gill,M. and Peters,E.C.
  TITLE     Robust phosphoproteomic profiling of tyrosine phosphorylation sites
            from human T cells using immobilized metal affinity chromatography
            and tandem mass spectrometry
  JOURNAL   Anal Chem 76 (10), 2763-2772 (2004)
   PUBMED   15144186
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104451.2, AC144531.2, AC090960.3 and AC090644.2.
            
            On Mar 3, 2017 this sequence version replaced XP_016863053.1.
            
            Transcript Variant: This variant (17), as well as variants 18, 19,
            20, and 21, encodes isoform e.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1962226.1,
                                           SRR14038192.3319815.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..659
                     /product="TBC1 domain family member 5 isoform e"
                     /calculated_mol_wt=73027
     Region          19..245
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     CDS             1..659
                     /gene="TBC1D5"
                     /coded_by="NM_001349087.2:590..2569"
                     /note="isoform e is encoded by transcript variant 17"
                     /db_xref="GeneID:9779"
                     /db_xref="HGNC:HGNC:19166"
                     /db_xref="MIM:615740"
ORIGIN      
        1 minnplsqde gslwnkffqd kelrsmieqd vkrtfpemqf fqqenvrkil tdvlfcyare
       61 neqllykqgm hellapivfv lhcdhqaflh asesaqpsee mktvlnpeyl ehdayavfsq
      121 lmetaepwfs tfehdgqkgk etlmtpipfa rpqdlgptia ivtkvnqiqd hllkkhdiel
      181 ymhlnrleia pqiyglrwvr llfgrefplq dllvvwdalf adglslglvd yifvamllyi
      241 rdalissnyq tclgllmhyp figdvhslil kalflrdpkr nprpvtyqfh pnldyykarg
      301 adlmnksrtn akgaplnink vsnslinfgr klispamapg saggpvpggn ssssssvvip
      361 trtsaeapsh hlqqqqqqqr lmksesmpvq lnkglsskni ssspsveslp ggreftgspp
      421 ssatkkdsff snisrsrshs ktmgrkesee eleaqisflq gqlndldamc kycakvmdth
      481 lvniqdvilq enlekedqil vslaglkqik dilkgslrfn qsqleaeene qitiadnhyc
      541 ssgqgqgrgq gqsvqmsgai kqassetpgc tdrgnsddfi liskdddgss argsfsgqaq
      601 plrtlrstsg ksqapvcspl vfsdplmgpa sasssnpsss pdddsskdsg ftivspldi
//
LOCUS       NP_001161842            1730 aa            linear   PRI 21-NOV-2025
DEFINITION  cullin-7 isoform 1 [Homo sapiens].
ACCESSION   NP_001161842
VERSION     NP_001161842.2
DBSOURCE    REFSEQ: accession NM_001168370.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1730)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1730)
  AUTHORS   Zhou,H.L., Grimmett,Z.W., Venetos,N.M., Stomberski,C.T., Qian,Z.,
            McLaughlin,P.J., Bansal,P.K., Zhang,R., Reynolds,J.D., Premont,R.T.
            and Stamler,J.S.
  TITLE     An enzyme that selectively S-nitrosylates proteins to regulate
            insulin signaling
  JOURNAL   Cell 186 (26), 5812-5825 (2023)
   PUBMED   38056462
REFERENCE   3  (residues 1 to 1730)
  AUTHORS   Wang,C., Zhao,Z., Zhang,Y., Liang,W., Zhou,C., Lin,W., He,Y.,
            Wu,M., Meng,Z., Liao,Y., Li,M., El Akkawi,M., Zhao,J. and He,Y.
  TITLE     Identification and verification of the prognostic value of CUL7 in
            colon adenocarcinoma
  JOURNAL   Front Immunol 13, 1043512 (2022)
   PUBMED   36304472
  REMARK    GeneRIF: Identification and verification of the prognostic value of
            CUL7 in colon adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1730)
  AUTHORS   Hopf,L.V.M., Baek,K., Klugel,M., von Gronau,S., Xiong,Y. and
            Schulman,B.A.
  TITLE     Structure of CRL7FBXW8 reveals coupling with CUL1-RBX1/ROC1 for
            multi-cullin-RING E3-catalyzed ubiquitin ligation
  JOURNAL   Nat Struct Mol Biol 29 (9), 854-862 (2022)
   PUBMED   35982156
REFERENCE   5  (residues 1 to 1730)
  AUTHORS   Goos,H., Kinnunen,M., Salokas,K., Tan,Z., Liu,X., Yadav,L.,
            Zhang,Q., Wei,G.H. and Varjosalo,M.
  TITLE     Human transcription factor protein interaction networks
  JOURNAL   Nat Commun 13 (1), 766 (2022)
   PUBMED   35140242
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1730)
  AUTHORS   Arai,T., Kasper,J.S., Skaar,J.R., Ali,S.H., Takahashi,C. and
            DeCaprio,J.A.
  TITLE     Targeted disruption of p185/Cul7 gene results in abnormal vascular
            morphogenesis
  JOURNAL   Proc Natl Acad Sci U S A 100 (17), 9855-9860 (2003)
   PUBMED   12904573
REFERENCE   7  (residues 1 to 1730)
  AUTHORS   Dias,D.C., Dolios,G., Wang,R. and Pan,Z.Q.
  TITLE     CUL7: A DOC domain-containing cullin selectively binds Skp1.Fbx29
            to form an SCF-like complex
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16601-16606 (2002)
   PUBMED   12481031
REFERENCE   8  (residues 1 to 1730)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   9  (residues 1 to 1730)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   10 (residues 1 to 1730)
  AUTHORS   Akilapa,R., Irving,M. and Holder-Espinasse,M.
  TITLE     3-M Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355385.15 and AL136304.10.
            
            On Oct 18, 2019 this sequence version replaced NP_001161842.1.
            
            Summary: The protein encoded by this gene is a component of an E3
            ubiquitin-protein ligase complex. The encoded protein interacts
            with TP53, CUL9, and FBXW8 proteins. Defects in this gene are a
            cause of 3M syndrome type 1 (3M1). Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Dec 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302668.1, SRR18074967.4017936.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1730
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..1730
                     /product="cullin-7 isoform 1"
                     /calculated_mol_wt=194288
     Region          347..389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14999.2)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14999.2)"
     Region          394..466
                     /region_name="Cul7"
                     /note="Mouse development and cellular proliferation
                     protein Cullin-7; pfam11515"
                     /db_xref="CDD:463286"
     Region          633..655
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14999.2)"
     Region          870..1000
                     /region_name="APC10-CUL7"
                     /note="APC10-like DOC1 domain of CUL7, subunit of the
                     SCF-ROC1-like E3 ubiquitin ligase complex that mediates
                     substrate ubiquitination; cd08665"
                     /db_xref="CDD:176486"
     Site            order(896,924,930,932,992)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:176486"
     Region          <1249..1538
                     /region_name="Cullin"
                     /note="Cullin family; pfam00888"
                     /db_xref="CDD:459983"
     Region          1377..1402
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14999.2)"
     Region          1593..1671
                     /region_name="Cullin_Nedd8"
                     /note="Cullin protein neddylation domain; smart00884"
                     /db_xref="CDD:214883"
     CDS             1..1730
                     /gene="CUL7"
                     /gene_synonym="3M1; CUL-7; dJ20C7.5; KIAA0076"
                     /coded_by="NM_001168370.2:150..5342"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS55003.2"
                     /db_xref="GeneID:9820"
                     /db_xref="HGNC:HGNC:21024"
                     /db_xref="MIM:609577"
ORIGIN      
        1 mvgelryref rvplgpglha ypdelirqrv ghdghpeyqi rwlilrrgde gdggsgqvdc
       61 kaehillwms kdeiyanchk mlgedgqvig psqesagevg aldksvleem etdvksliqr
      121 alrqleecvg tippapllht vhvlsayasi epltgvfkdp rvldllmhml sspdyqirws
      181 agrmiqalss hdagegqcge egkageglgr lrdsqdtvag asdlirtrtq illslsqqea
      241 iekhldfdsr callalfaqa tlsehpmsfe giqlpqvpgr vlfslvkryl hvtslldqln
      301 dsaaepgaqn tsapeelsge rgqlelefsm amgtliselv qamrwdqasd rprssarspg
      361 sifqpqladv spglpaaqaq psfrrsrrfr prsefasgnt yalyvrdtlq pgmrvrmldd
      421 yeeisagdeg efrqsnngvp pvqvfwestg rtywvhwhml eilgfeedie dmveadeyqg
      481 avasrvlgra lpawrwrpmt elyavpyvlp ededteeceh ltlaewwell ffikkldgpd
      541 hqevlqilqe nldgeildde ilaelavpie laqdllltlp qrlndsalrd linchvykky
      601 gpealagnqa ypslleaqed vllldaqaqa kdsedaakve akeppsqspn tplqrlvegy
      661 gpagkilldl eqalssegtq enkvkplllq lqrqpqpfla lmqsldtpet nrtlhltvlr
      721 ilkqlvdfpe alllpwheav dacmaclrsp ntdrevlqel ifflhrltsv srdyavvlnq
      781 lgardaiska lekhlgklel aqelrdmvfk cekhahlyrk litnilggci qmvlgqiedh
      841 rrthqpinip ffdvflrylc qgssvevked kcwekvevss nphraskltd hnpktywesn
      901 gsagshyitl hmrrgilirq ltllvaseds symparvvvc ggdstsslht elnsvnvmps
      961 asrvillenl trfwpiiqir ikrcqqggid trirgleilg pkptfwpvfr eqlcrhtrlf
     1021 ymvraqawsq dmaedrrsll hlssrlngal rqeqnfadrf lpddeaaqal gktcwealvs
     1081 pvvqnitspd edgisplgwl ldqylecqea vfnpqsrgpa ffsrvrrlth llvhvepcea
     1141 pppvvatprp kgrnrshdws slatrglpss imrnltrcwr avvekqvnnf ltsswrdddf
     1201 vprycehfni lqnssselfg praafllalq ngcagallkl pflkaahvse qfarhidqqi
     1261 qgsriggaqe merlaqlqqc lqavlifsgl eiattfehyy qhymadrllg vvsswlegav
     1321 leqigpcfpn rlpqqmlqsl stskelqrqf hvyqlqqldq ellkledtek kiqvglgasg
     1381 kehksekeee agaaavvdva egeeeeeene dlyyegampe vsvlvlsrhs wpvasichtl
     1441 nprtclpsyl rgtlnrysnf ynksqshpal ergsqrrlqw twlgwaelqf gnqtlhvstv
     1501 qmwlllylnd lkavsvesll afsglsadml nqaigpltss rgpldlheqk dipggvlkir
     1561 dgskeprsrw divrlippqt ylqaegedgq nlekrrnlln clivrilkah gdeglhidql
     1621 vclvleawqk gpcpprglvs slgkgsacss tdvlscilhl lgkgtlrrhd drpqvlsyav
     1681 pvtvmephte slnpgssgpn ppltfhtlqi rsrgvpyasc tatqsfstfr
//
LOCUS       NP_001358061            1184 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal cell adhesion molecule isoform J precursor [Homo sapiens].
ACCESSION   NP_001358061
VERSION     NP_001358061.1
DBSOURCE    REFSEQ: accession NM_001371132.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1184)
  AUTHORS   Wang,C., Wang,Z., Fu,L., Du,J., Ji,F. and Qiu,X.
  TITLE     CircNRCAM up-regulates NRCAM to promote papillary thyroid carcinoma
            progression
  JOURNAL   J Endocrinol Invest 47 (5), 1215-1226 (2024)
   PUBMED   38485895
  REMARK    GeneRIF: CircNRCAM up-regulates NRCAM to promote papillary thyroid
            carcinoma progression.
REFERENCE   2  (residues 1 to 1184)
  AUTHORS   Zhou,L., He,L., Liu,C.H., Qiu,H., Zheng,L., Sample,K.M., Wu,Q.,
            Li,J., Xie,K., Ampuero,J., Li,Z., Lv,D., Liu,M., Romero-Gomez,M.,
            Hu,Y. and Tang,H.
  TITLE     Liver cancer stem cell dissemination and metastasis: uncovering the
            role of NRCAM in hepatocellular carcinoma
  JOURNAL   J Exp Clin Cancer Res 42 (1), 311 (2023)
   PUBMED   37993901
  REMARK    GeneRIF: Liver cancer stem cell dissemination and metastasis:
            uncovering the role of NRCAM in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1184)
  AUTHORS   Sannes,A.C., Christensen,J.O., Nielsen,M.B. and Gjerstad,J.
  TITLE     Stress-induced headache in the general working population is
            moderated by the NRCAM rs2300043 genotype
  JOURNAL   Scand J Pain 23 (2), 326-332 (2022)
   PUBMED   36181733
  REMARK    GeneRIF: Stress-induced headache in the general working population
            is moderated by the NRCAM rs2300043 genotype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1184)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 1184)
  AUTHORS   Bai,C. and Chen,D.G.
  TITLE     NRCAM acts as a prognostic biomarker and promotes the tumor
            progression in gastric cancer via EMT pathway
  JOURNAL   Tissue Cell 77, 101859 (2022)
   PUBMED   35763884
  REMARK    GeneRIF: NRCAM acts as a prognostic biomarker and promotes the
            tumor progression in gastric cancer via EMT pathway.
REFERENCE   6  (residues 1 to 1184)
  AUTHORS   Wang,B., Williams,H., Du,J.S., Terrett,J. and Kenwrick,S.
  TITLE     Alternative splicing of human NrCAM in neural and nonneural tissues
  JOURNAL   Mol Cell Neurosci 10 (5-6), 287-295 (1998)
   PUBMED   9604207
REFERENCE   7  (residues 1 to 1184)
  AUTHORS   Grumet,M.
  TITLE     Nr-CAM: a cell adhesion molecule with ligand and receptor functions
  JOURNAL   Cell Tissue Res 290 (2), 423-428 (1997)
   PUBMED   9321706
  REMARK    Review article
REFERENCE   8  (residues 1 to 1184)
  AUTHORS   Sakurai,T., Lustig,M., Nativ,M., Hemperly,J.J., Schlessinger,J.,
            Peles,E. and Grumet,M.
  TITLE     Induction of neurite outgrowth through contactin and Nr-CAM by
            extracellular regions of glial receptor tyrosine phosphatase beta
  JOURNAL   J Cell Biol 136 (4), 907-918 (1997)
   PUBMED   9049255
REFERENCE   9  (residues 1 to 1184)
  AUTHORS   Volkmer,H., Leuschner,R., Zacharias,U. and Rathjen,F.G.
  TITLE     Neurofascin induces neurites by heterophilic interactions with
            axonal NrCAM while NrCAM requires F11 on the axonal surface to
            extend neurites
  JOURNAL   J Cell Biol 135 (4), 1059-1069 (1996)
   PUBMED   8922386
REFERENCE   10 (residues 1 to 1184)
  AUTHORS   Lane,R.P., Chen,X.N., Yamakawa,K., Vielmetter,J., Korenberg,J.R.
            and Dreyer,W.J.
  TITLE     Characterization of a highly conserved human homolog to the chicken
            neural cell surface protein Bravo/Nr-CAM that maps to chromosome
            band 7q31
  JOURNAL   Genomics 35 (3), 456-465 (1996)
   PUBMED   8812479
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005058.1, AC007567.2 and
            AC005683.2.
            
            Summary: Cell adhesion molecules (CAMs) are members of the
            immunoglobulin superfamily. This gene encodes a neuronal cell
            adhesion molecule with multiple immunoglobulin-like C2-type domains
            and fibronectin type-III domains. This ankyrin-binding protein is
            involved in neuron-neuron adhesion and promotes directional
            signaling during axonal cone growth. This gene is also expressed in
            non-neural tissues and may play a general role in cell-cell
            communication via signaling from its intracellular domain to the
            actin cytoskeleton during directional cell migration. Allelic
            variants of this gene have been associated with autism and
            addiction vulnerability. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (32), as well as variant 31,
            encodes isoform J.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1965299, SAMEA1966682
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1184
                     /product="neuronal cell adhesion molecule isoform J
                     precursor"
                     /note="NgCAM-related cell adhesion molecule; neuronal
                     surface protein Bravo"
                     /calculated_mol_wt=127685
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3315
     Region          46..140
                     /region_name="IgI_NrCAM"
                     /note="Immunoglobulin (Ig)-like domain of NrCAM (Ng
                     (neuronglia) CAM-related cell adhesion molecule); member
                     of the I-set of Ig superfamily (IgSF) domains; cd05874"
                     /db_xref="CDD:409458"
     Region          46..50
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409458"
     Region          55..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409458"
     Region          64..71
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409458"
     Region          77..82
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409458"
     Region          85..87
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409458"
     Region          94..97
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409458"
     Region          102..106
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409458"
     Region          119..127
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409458"
     Region          130..140
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409458"
     Region          149..238
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          163..167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          177..181
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          200..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          215..220
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          231..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          258..339
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          269..273
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          282..286
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          304..308
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          318..323
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          331..334
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          343..431
                     /region_name="Ig4_NrCAM"
                     /note="Fourth immunoglobulin (Ig)-like domain of NrCAM
                     (NgCAM-related cell adhesion molecule); cd05868"
                     /db_xref="CDD:409454"
     Region          359..363
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409454"
     Region          372..376
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409454"
     Region          396..400
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409454"
     Region          410..415
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409454"
     Region          423..426
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409454"
     Region          440..523
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          453..457
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          466..470
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          489..493
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          503..508
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          516..519
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          529..614
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          544..548
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          559..563
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          580..>1052
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          594..599
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          607..610
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          628..718
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(628,694,709)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(710..711,713..714)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1071..1160
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     CDS             1..1184
                     /gene="NRCAM"
                     /gene_synonym="NEDNMS"
                     /coded_by="NM_001371132.1:644..4198"
                     /note="isoform J precursor is encoded by transcript
                     variant 32"
                     /db_xref="GeneID:4897"
                     /db_xref="HGNC:HGNC:7994"
                     /db_xref="MIM:601581"
ORIGIN      
        1 mqlkimpkkk rlsagrvpli lflcqmisal evpldpklle dlvqpptitq qspkdyiidp
       61 reniviqcea kgkpppsfsw trngthfdid kdplvtmkpg tgtliinims egkaetyegv
      121 yqctarnerg aavsnnivvr psrsplwtke klepitlqsg qslvlpcrpp iglpppiifw
      181 mdnsfqrlpq servsqglng dlyfsnvlpe dtredyicya rfnhtqtiqq kqpisvkvis
      241 akssrerppt fltpegnasn keelrgnvls leciaeglpt piiywakedg mlpknrtvyk
      301 nfektlqiih vseadsgnyq ciaknalgai hhtisvrvka apywitapqn lvlspgedgt
      361 licrangnpk priswltngv pieiapddps rkidgdtiif snvqerssav yqcnasneyg
      421 yllanafvnv laeppriltp antlyqvian rpalldcaff gsplptiewf kgakgsalhe
      481 diyvlhengt leipvaqkds tgtytcvarn klgmaknevh leikdptwiv kqpeyavvqr
      541 gsmvsfeckv khdhtlsltv lwlkdnrelp sderftvdkd hlvvadvsdd dsgtytcvan
      601 ttldsvsasa vlsvvaptpt papvydvpnp pfdleltdql dksvqlswtp gddnnspitk
      661 fiieyedamh kpglwhhqte vsgtqttaql klspyvnysf rvmavnsigk slpseaseqy
      721 ltkasepdkn ptaveglgse pdnlvitwkp lngfesngpg lqykvswrqk dgddewtsvv
      781 vanvskyivs gtptfvpyli kvqalndmgf apepavvmgh sgedlpmvap gnvrvnvvns
      841 tlaevhwdpv plksirghlq gyriyywktq ssskrnrrhi ekkiltfqgs kthgmlpgle
      901 pfshytlnvr vvngkgegpa spdrvfntpe gvpsapsslk ivnptldslt lewdppshpn
      961 gilteytlky qpinsthelg plvdlkipan ktrwtlknln fstrykfyfy aqtsagsgsq
     1021 iteeavttvd egagkamasr qvdiatqgwf iglmcavall ilillivcfi rrnkggkypv
     1081 kekedahadp eiqpmkeddg tfgeysdaed hkplkkgsrt psdrtvkked sddslvdyge
     1141 gvngqfnedg sfigqysgkk ekepaegnes seapspvnam nsfv
//
LOCUS       NP_067054                758 aa            linear   PRI 21-NOV-2025
DEFINITION  splicing factor Cactin [Homo sapiens].
ACCESSION   NP_067054 XP_950028
VERSION     NP_067054.1
DBSOURCE    REFSEQ: accession NM_021231.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   2  (residues 1 to 758)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 758)
  AUTHORS   Zanini,I.M., Soneson,C., Lorenzi,L.E. and Azzalin,C.M.
  TITLE     Human cactin interacts with DHX8 and SRRM2 to assure efficient
            pre-mRNA splicing and sister chromatid cohesion
  JOURNAL   J Cell Sci 130 (4), 767-778 (2017)
   PUBMED   28062851
  REMARK    GeneRIF: cellular complexes comprising cactin, DHX8 and SRRM2
            sustain precise chromosome segregation, genome stability and cell
            proliferation by allowing faithful splicing of specific pre-mRNAs.
REFERENCE   4  (residues 1 to 758)
  AUTHORS   Suzuki,M., Watanabe,M., Nakamaru,Y., Takagi,D., Takahashi,H.,
            Fukuda,S. and Hatakeyama,S.
  TITLE     TRIM39 negatively regulates the NFkappaB-mediated signaling pathway
            through stabilization of Cactin
  JOURNAL   Cell Mol Life Sci 73 (5), 1085-1101 (2016)
   PUBMED   26363554
  REMARK    GeneRIF: TRIM39 negatively regulates the NFkappaB signaling pathway
            possibly via stabilization of cactin.
REFERENCE   5  (residues 1 to 758)
  AUTHORS   Yamada,H., Kikuchi,T., Masumoto,T., Wei,F.Y., Abe,T., Takeda,T.,
            Nishiki,T., Tomizawa,K., Watanabe,M., Matsui,H. and Takei,K.
  TITLE     Possible role of cortactin phosphorylation by protein kinase Calpha
            in actin-bundle formation at growth cone
  JOURNAL   Biol Cell 107 (9), 319-330 (2015)
   PUBMED   26033110
  REMARK    GeneRIF: results indicate that PKC-mediated cortactin
            phosphorylation might be implicated in the maintenance of growth
            cone
REFERENCE   6  (residues 1 to 758)
  AUTHORS   Sogayar,M.C., Camargo,A.A., Bettoni,F., Carraro,D.M., Pires,L.C.,
            Parmigiani,R.B., Ferreira,E.N., de Sa Moreira,E., do Rosario D de O
            Latorre,M., Simpson,A.J., Cruz,L.O., Degaki,T.L., Festa,F.,
            Massirer,K.B., Sogayar,M.C., Filho,F.C., Camargo,L.P., Cunha,M.A.,
            De Souza,S.J., Faria,M. Jr., Giuliatti,S., Kopp,L., de
            Oliveira,P.S., Paiva,P.B., Pereira,A.A., Pinheiro,D.G., Puga,R.D.,
            S de Souza,J.E., Albuquerque,D.M., Andrade,L.E., Baia,G.S.,
            Briones,M.R., Cavaleiro-Luna,A.M., Cerutti,J.M., Costa,F.F.,
            Costanzi-Strauss,E., Espreafico,E.M., Ferrasi,A.C., Ferro,E.S.,
            Fortes,M.A., Furchi,J.R., Giannella-Neto,D., Goldman,G.H.,
            Goldman,M.H., Gruber,A., Guimaraes,G.S., Hackel,C.,
            Henrique-Silva,F., Kimura,E.T., Leoni,S.G., Macedo,C., Malnic,B.,
            Manzini,B. CV, Marie,S.K., Martinez-Rossi,N.M., Menossi,M.,
            Miracca,E.C., Nagai,M.A., Nobrega,F.G., Nobrega,M.P.,
            Oba-Shinjo,S.M., Oliveira,M.K., Orabona,G.M., Otsuka,A.Y.,
            Paco-Larson,M.L., Paixao,B.M., Pandolfi,J.R., Pardini,M.I., Passos
            Bueno,M.R., Passos,G.A., Pesquero,J.B., Pessoa,J.G., Rahal,P.,
            Rainho,C.A., Reis,C.P., Ricca,T.I., Rodrigues,V., Rogatto,S.R.,
            Romano,C.M., Romeiro,J.G., Rossi,A., Sa,R.G., Sales,M.M.,
            Sant'Anna,S.C., Santarosa,P.L., Segato,F., Silva,W.A. Jr.,
            Silva,I.D., Silva,N.P., Soares-Costa,A., Sonati,M.F., Strauss,B.E.,
            Tajara,E.H., Valentini,S.R., Villanova,F.E., Ward,L.S. and
            Zanette,D.L.
  CONSRTM   Ludwig-FAPESP Transcript Finishing Initiative
  TITLE     A transcript finishing initiative for closing gaps in the human
            transcriptome
  JOURNAL   Genome Res 14 (7), 1413-1423 (2004)
   PUBMED   15197164
REFERENCE   7  (residues 1 to 758)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 758)
  AUTHORS   Lehner,B., Semple,J.I., Brown,S.E., Counsell,D., Campbell,R.D. and
            Sanderson,C.M.
  TITLE     Analysis of a high-throughput yeast two-hybrid system and its use
            to predict the function of intracellular proteins encoded within
            the human MHC class III region
  JOURNAL   Genomics 83 (1), 153-167 (2004)
   PUBMED   14667819
REFERENCE   9  (residues 1 to 758)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   10 (residues 1 to 758)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CN305928.1, BF196424.1, CO248922.1, AW027691.1, CF272634.1,
            AC005175.1 and BC019848.1.
            
            On Mar 9, 2007 this sequence version replaced XP_950028.1.
            
            Transcript Variant: This variant (2) differs in the 3' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2151119,
                              SAMEA2155371 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..758
                     /product="splicing factor Cactin"
                     /note="functional spliceosome-associated protein c; NY REN
                     24 antigen; renal carcinoma antigen NY-REN-24"
                     /calculated_mol_wt=88571
     Region          1..140
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUQ7.3)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CS00; propagated from
                     UniProtKB/Swiss-Prot (Q8WUQ7.3)"
     Region          155..181
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUQ7.3)"
     Region          <214..>272
                     /region_name="PTZ00266"
                     /note="NIMA-related protein kinase; Provisional"
                     /db_xref="CDD:173502"
     Region          270..457
                     /region_name="Cactin_mid"
                     /note="Conserved mid region of cactin; pfam10312"
                     /db_xref="CDD:463049"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUQ7.3)"
     Region          477..536
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUQ7.3)"
     Site            559
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WUQ7.3)"
     Region          634..758
                     /region_name="CactinC_cactus"
                     /note="Cactus-binding C-terminus of cactin protein;
                     pfam09732"
                     /db_xref="CDD:401611"
     CDS             1..758
                     /gene="CACTIN"
                     /gene_synonym="C19orf29; fSAPc; NY-REN-24"
                     /coded_by="NM_021231.2:29..2305"
                     /db_xref="CCDS:CCDS45920.1"
                     /db_xref="GeneID:58509"
                     /db_xref="HGNC:HGNC:29938"
                     /db_xref="MIM:618536"
ORIGIN      
        1 mgrdtrsrsr sagrrgrrrq sqsgsrsrsr shgrrnrrrr edegrrrrrr rsrerrsdse
       61 eerwqrsgmr srspprpkwh srdgssqsds geeqsrgqwa rrrrrarsws psssasssas
      121 pgrsqspraa aaalsqqqsl qerlrlreer kqqeelmkaf etpeekrarr lakkeakerk
      181 krekmgwgee ymgytntdnp fgdnnllgtf iwnkalekkg ishleekelk ernkriqedn
      241 rlelqkvkql rlererekam reqelemlqr ekeaehfktw eeqednfhlq qaklrskiri
      301 rdgrakpidl lakyisaedd dlavemhepy tflngltvad medllediqv ymeleqgkna
      361 dfwrdmttit edeisklrkl easgkgpger regvnasvss dvqsvfkgkt ynqlqvifqg
      421 iegkiraggp nldmgywesl lqqlrahmar arlrerhqdv lrqklyklkq eqgveseplf
      481 pilkqepqsp srslepedaa ptppgpsseg gpaeaevdga tptegdgdgd gegegegeav
      541 lmeedliqqs lddydagrys prlltahelp ldahvlepde dlqrlqlsrq qlqvtgdase
      601 saediffrra kegmgqdeaq fsvempltgk aylwadkyrp rkprffnrvh tgfewnkynq
      661 thydfdnppp kivqgykfni fypdlidkrs tpeyfleaca dnkdfailrf hagppyedia
      721 fkivnrewey shrhgfrcqf angifqlwfh fkryryrr
//
LOCUS       NP_001351416             572 aa            linear   PRI 21-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001351416 XP_006714814
VERSION     NP_001351416.1
DBSOURCE    REFSEQ: accession NM_001364487.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 572)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 572)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 572)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 572)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008641.7.
            
            On Jun 19, 2018 this sequence version replaced XP_006714814.1.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Transcript Variant: This variant (12) lacks an alternate in-frame
            exon and uses an alternate splice junction compared to variant 1.
            The resulting isoform (5) has a shorter and distinct C-terminus
            compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.290207.1,
                                           SRR14038194.3143257.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..572
                     /product="TNFAIP3-interacting protein 1 isoform 5"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=64369
     Region          14..>149
                     /region_name="Speriolin_N"
                     /note="Speriolin N terminus; pfam15058"
                     /db_xref="CDD:434426"
     Region          <214..>251
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          <298..>529
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..572
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001364487.2:192..1910"
                     /note="isoform 5 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS58984.1"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 megrgpyriy dpggsvpsge asaaferlvk ensrlkekmq gikmlgelle esqmeatrlr
       61 qkaeelvkdn ellpppspsl gsfdplaelt gkdsnvtasp tapacpsdkp apvqkppssg
      121 tssefevvtp eeqnspesss hanamalgpl predgnlmlh lqrlettlsv caeepdhgql
      181 fthlgrmale fnrlaskvhk neqrtsilqt lceqlrkene alkakldkgl eqrdqaaerl
      241 reenlelkkl lmsngnkega sgrpgspkme gtgkkavagq qqasvtagkv pevvalgaae
      301 kkvkmleqqr sellevnkqw dqhfrsmkqq yeqkitelrq kladlqkqvt dleaereqkq
      361 rdfdrkllla kskiemeetd keqltaeake lrqkvkylqd qlspltrqre yqekeiqrln
      421 kaleealsiq tppsspptaf gspegagall rkqelvtqne llkqqvkife edfqrersdr
      481 ermneekeel kkqveklqaq vtlsnaqlka fkdeekarea lrqqkrkakp eytwrlpcgg
      541 vrnpnqssqv mdpptarpte pespkndreg pq
//
LOCUS       NP_001245327             103 aa            linear   PRI 21-NOV-2025
DEFINITION  dynein axonemal assembly factor 19 isoform 3 [Homo sapiens].
ACCESSION   NP_001245327 XP_005257410
VERSION     NP_001245327.1
DBSOURCE    REFSEQ: accession NM_001258398.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Zubair,M., Khan,R., Ma,A., Hameed,U., Khan,M., Abbas,T., Ahmad,R.,
            Zhou,J.T., Shah,W., Hussain,A., Ahmed,N., Khan,I., Khan,K.,
            Zhang,Y.W., Zhang,H., Wu,L.M. and Shi,Q.H.
  TITLE     A recurrent homozygous missense mutation in CCDC103 causes
            asthenoteratozoospermia due to disorganized dynein arms
  JOURNAL   Asian J Androl 24 (3), 255-259 (2022)
   PUBMED   35259782
  REMARK    GeneRIF: A recurrent homozygous missense mutation in CCDC103 causes
            asthenoteratozoospermia due to disorganized dynein arms.
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 103)
  AUTHORS   King,S.M. and Patel-King,R.S.
  TITLE     The outer dynein arm assembly factor CCDC103 forms molecular
            scaffolds through multiple self-interaction sites
  JOURNAL   Cytoskeleton (Hoboken) 77 (1-2), 25-35 (2020)
   PUBMED   31858719
  REMARK    GeneRIF: The outer dynein arm assembly factor CCDC103 forms
            molecular scaffolds through multiple self-interaction sites.
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 103)
  AUTHORS   Shoemark,A., Moya,E., Hirst,R.A., Patel,M.P., Robson,E.A.,
            Hayward,J., Scully,J., Fassad,M.R., Lamb,W., Schmidts,M., Dixon,M.,
            Patel-King,R.S., Rogers,A.V., Rutman,A., Jackson,C.L., Goggin,P.,
            Rubbo,B., Ollosson,S., Carr,S., Walker,W., Adler,B.,
            Loebinger,M.R., Wilson,R., Bush,A., Williams,H., Boustred,C.,
            Jenkins,L., Sheridan,E., Chung,E.M.K., Watson,C.M., Cullup,T.,
            Lucas,J.S., Kenia,P., O'Callaghan,C., King,S.M., Hogg,C. and
            Mitchison,H.M.
  TITLE     High prevalence of CCDC103 p.His154Pro mutation causing primary
            ciliary dyskinesia disrupts protein oligomerisation and is
            associated with normal diagnostic investigations
  JOURNAL   Thorax 73 (2), 157-166 (2018)
   PUBMED   28790179
  REMARK    GeneRIF: The CCDC103 p.His154Pro mutation is more prevalent than
            previously thought in the South Asian community in the UK and
            causes primary ciliary dyskinesia that can be difficult to diagnose
            using pathology-based clinical tests.
REFERENCE   7  (residues 1 to 103)
  AUTHORS   Casey,J.P., Goggin,P., McDaid,J., White,M., Ennis,S., Betts,D.R.,
            Lucas,J.S., Elnazir,B. and Lynch,S.A.
  TITLE     A case report of primary ciliary dyskinesia, laterality defects and
            developmental delay caused by the co-existence of a single gene and
            chromosome disorder
  JOURNAL   BMC Med Genet 16, 45 (2015)
   PUBMED   26123568
  REMARK    GeneRIF: A variable and complex phenotype caused by the
            co-inheritance of a single gene mutation in CCDC103 and a
            microduplication at 17q12, both on chromosome 17.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 103)
  AUTHORS   Tarkar,A., Loges,N.T., Slagle,C.E., Francis,R., Dougherty,G.W.,
            Tamayo,J.V., Shook,B., Cantino,M., Schwartz,D., Jahnke,C.,
            Olbrich,H., Werner,C., Raidt,J., Pennekamp,P., Abouhamed,M.,
            Hjeij,R., Kohler,G., Griese,M., Li,Y., Lemke,K., Klena,N., Liu,X.,
            Gabriel,G., Tobita,K., Jaspers,M., Morgan,L.C., Shapiro,A.J.,
            Letteboer,S.J., Mans,D.A., Carson,J.L., Leigh,M.W., Wolf,W.E.,
            Chen,S., Lucas,J.S., Onoufriadis,A., Plagnol,V., Schmidts,M.,
            Boldt,K., Roepman,R., Zariwala,M.A., Lo,C.W., Mitchison,H.M.,
            Knowles,M.R., Burdine,R.D., Loturco,J.J. and Omran,H.
  CONSRTM   UK10K
  TITLE     DYX1C1 is required for axonemal dynein assembly and ciliary
            motility
  JOURNAL   Nat Genet 45 (9), 995-1003 (2013)
   PUBMED   23872636
REFERENCE   9  (residues 1 to 103)
  AUTHORS   Panizzi,J.R., Becker-Heck,A., Castleman,V.H., Al-Mutairi,D.A.,
            Liu,Y., Loges,N.T., Pathak,N., Austin-Tse,C., Sheridan,E.,
            Schmidts,M., Olbrich,H., Werner,C., Haffner,K., Hellman,N.,
            Chodhari,R., Gupta,A., Kramer-Zucker,A., Olale,F., Burdine,R.D.,
            Schier,A.F., O'Callaghan,C., Chung,E.M., Reinhardt,R.,
            Mitchison,H.M., King,S.M., Omran,H. and Drummond,I.A.
  TITLE     CCDC103 mutations cause primary ciliary dyskinesia by disrupting
            assembly of ciliary dynein arms
  JOURNAL   Nat Genet 44 (6), 714-719 (2012)
   PUBMED   22581229
  REMARK    GeneRIF: These results identify Ccdc103 as a dynein arm attachment
            factor that causes primary ciliary dyskinesia when mutated.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 103)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC015936.14.
            
            On Aug 31, 2013 this sequence version replaced XP_005257410.1.
            
            Sequence Note:.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB451789.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968968,
                                           SAMEA1970526 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..103
                     /product="dynein axonemal assembly factor 19 isoform 3"
                     /note="coiled-coil domain-containing protein 103;
                     coiled-coil domain containing 103"
                     /calculated_mol_wt=11606
     Region          7..74
                     /region_name="Dynein_attach_N"
                     /note="Dynein attachment factor N-terminus; pfam15867"
                     /db_xref="CDD:464912"
     CDS             1..103
                     /gene="DNAAF19"
                     /gene_synonym="CCDC103; CILD17; PR46b; SMH"
                     /coded_by="NM_001258398.3:125..436"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:388389"
                     /db_xref="HGNC:HGNC:32700"
                     /db_xref="MIM:614677"
ORIGIN      
        1 merndiinfk alekelqaal tadekykren aaklraveqr vasyeefrgi vlashlkple
       61 rkdkmggkrt vpwnchtiqg rtfqdvatei spvespppar dvc
//
LOCUS       NP_001376517             114 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerases I, II, and III subunit RPABC3 isoform
            3 [Homo sapiens].
ACCESSION   NP_001376517
VERSION     NP_001376517.1
DBSOURCE    REFSEQ: accession NM_001389588.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Zhao,D., Liu,W., Chen,K., Wu,Z., Yang,H. and Xu,Y.
  TITLE     Structure of the human RNA polymerase I elongation complex
  JOURNAL   Cell Discov 7 (1), 97 (2021)
   PUBMED   34671025
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   6  (residues 1 to 114)
  AUTHORS   Kato,H., Sumimoto,H., Pognonec,P., Chen,C.H., Rosen,C.A. and
            Roeder,R.G.
  TITLE     HIV-1 Tat acts as a processivity factor in vitro in conjunction
            with cellular elongation factors
  JOURNAL   Genes Dev 6 (4), 655-666 (1992)
   PUBMED   1559613
REFERENCE   7  (residues 1 to 114)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
REFERENCE   8  (residues 1 to 114)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 114)
  AUTHORS   Southgate,C., Zapp,M.L. and Green,M.R.
  TITLE     Activation of transcription by HIV-1 Tat protein tethered to
            nascent RNA through another protein
  JOURNAL   Nature 345 (6276), 640-642 (1990)
   PUBMED   2190099
REFERENCE   10 (residues 1 to 114)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078797.20.
            
            Summary: The three eukaryotic RNA polymerases are complex
            multisubunit enzymes that play a central role in the transcription
            of nuclear genes. This gene encodes an essential and highly
            conserved subunit of RNA polymerase II that is shared by the other
            two eukaryotic DNA-directed RNA polymerases, I and III. Alternative
            splicing results in multiple transcript variants of this gene.
            [provided by RefSeq, Jul 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BU933141.1, BE262963.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2152568 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..114
                     /product="DNA-directed RNA polymerases I, II, and III
                     subunit RPABC3 isoform 3"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerases I, II, and III subunit
                     RPABC3; RPB8 homolog; DNA-directed RNA polymerase II
                     subunit H; DNA-directed RNA polymerases I, II, and III
                     17.1 kDa polypeptide; polymerase (RNA) II (DNA directed)
                     polypeptide H; polymerase (RNA) II subunit H"
                     /calculated_mol_wt=12827
     Region          <1..111
                     /region_name="RPOL8c"
                     /note="RNA polymerase subunit 8; smart00658"
                     /db_xref="CDD:197821"
     CDS             1..114
                     /gene="POLR2H"
                     /gene_synonym="RPABC3; RPB17; RPB8"
                     /coded_by="NM_001389588.1:614..958"
                     /note="isoform 3 is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS63861.1"
                     /db_xref="GeneID:5437"
                     /db_xref="HGNC:HGNC:9195"
                     /db_xref="MIM:606023"
ORIGIN      
        1 mdlildvniq iypvdlgdkf rlviastlye dgtlddgeyn ptddrpsrad qfeyvmygkv
       61 yriegdetst eaatrlsayv syggllmrlq gdannlhgfe vdsrvyllmk klaf
//
LOCUS       NP_001335431            1081 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 2 isoform w [Homo
            sapiens].
ACCESSION   NP_001335431 XP_016869535
VERSION     NP_001335431.1
DBSOURCE    REFSEQ: accession NM_001348502.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Mechaussier,S., Almoallem,B., Zeitz,C., Van Schil,K., Jeddawi,L.,
            Van Dorpe,J., Duenas Rey,A., Condroyer,C., Pelle,O., Polak,M.,
            Boddaert,N., Bahi-Buisson,N., Cavallin,M., Bacquet,J.L.,
            Mouallem-Beziere,A., Zambrowski,O., Sahel,J.A., Audo,I., Kaplan,J.,
            Rozet,J.M., De Baere,E. and Perrault,I.
  TITLE     Loss of Function of RIMS2 Causes a Syndromic Congenital Cone-Rod
            Synaptic Disease with Neurodevelopmental and Pancreatic Involvement
  JOURNAL   Am J Hum Genet 106 (6), 859-871 (2020)
   PUBMED   32470375
  REMARK    GeneRIF: Loss of Function of RIMS2 Causes a Syndromic Congenital
            Cone-Rod Synaptic Disease with Neurodevelopmental and Pancreatic
            Involvement.
            Erratum:[Am J Hum Genet. 2020 Sep 3;107(3):580. doi:
            10.1016/j.ajhg.2020.08.004. PMID: 32888510]
REFERENCE   4  (residues 1 to 1081)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 1081)
  AUTHORS   Kim,K.T., Lee,J.S., Lee,B.W., Seok,H., Jeon,H.S., Kim,J.H. and
            Chung,J.H.
  TITLE     Association between regulating synaptic membrane exocytosis 2 gene
            polymorphisms and degenerative lumbar scoliosis
  JOURNAL   Biomed Rep 1 (4), 619-623 (2013)
   PUBMED   24648997
REFERENCE   6  (residues 1 to 1081)
  AUTHORS   Sun,L., Bittner,M.A. and Holz,R.W.
  TITLE     Rim, a component of the presynaptic active zone and modulator of
            exocytosis, binds 14-3-3 through its N terminus
  JOURNAL   J Biol Chem 278 (40), 38301-38309 (2003)
   PUBMED   12871946
REFERENCE   7  (residues 1 to 1081)
  AUTHORS   Fukuda,M.
  TITLE     Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and
            Noc2. Identification of a critical determinant of Rab3A/Rab27A
            recognition by Rim2
  JOURNAL   J Biol Chem 278 (17), 15373-15380 (2003)
   PUBMED   12578829
REFERENCE   8  (residues 1 to 1081)
  AUTHORS   Wang,Y. and Sudhof,T.C.
  TITLE     Genomic definition of RIM proteins: evolutionary amplification of a
            family of synaptic regulatory proteins
  JOURNAL   Genomics 81 (2), 126-137 (2003)
   PUBMED   12620390
REFERENCE   9  (residues 1 to 1081)
  AUTHORS   Kashima,Y., Miki,T., Shibasaki,T., Ozaki,N., Miyazaki,M., Yano,H.
            and Seino,S.
  TITLE     Critical role of cAMP-GEFII--Rim2 complex in incretin-potentiated
            insulin secretion
  JOURNAL   J Biol Chem 276 (49), 46046-46053 (2001)
   PUBMED   11598134
REFERENCE   10 (residues 1 to 1081)
  AUTHORS   Fenster,S.D., Chung,W.J., Zhai,R., Cases-Langhoff,C., Voss,B.,
            Garner,A.M., Kaempf,U., Kindler,S., Gundelfinger,E.D. and
            Garner,C.C.
  TITLE     Piccolo, a presynaptic zinc finger protein structurally related to
            bassoon
  JOURNAL   Neuron 25 (1), 203-214 (2000)
   PUBMED   10707984
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC090686.4, AP001572.3,
            AC107933.6 and AP002849.2.
            
            On Feb 4, 2017 this sequence version replaced XP_016869535.1.
            
            Summary: The protein encoded by this gene is a presynaptic protein
            that interacts with RAB3, a protein important for normal
            neurotransmitter release. The encoded protein can also bind several
            other synaptic proteins, including UNC-13 homolog B,
            ELKS/Rab6-interacting/CAST family member 1, and synaptotagmin 1.
            This protein is involved in synaptic membrane exocytosis.
            Polymorphisms in this gene have been associated with degenerative
            lumbar scoliosis. [provided by RefSeq, Feb 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.240179.1,
                                           SRR1803616.265847.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..1081
                     /product="regulating synaptic membrane exocytosis protein
                     2 isoform w"
                     /note="RAB3 interacting protein 3; regulating synaptic
                     membrane exocytosis protein 2; nuclear protein; non-small
                     cell lung cancer RimL3a protein; non-small cell lung
                     cancer RimL3c protein; rab3-interacting molecule 2;
                     rab-3-interacting protein 3; rab-3-interacting molecule 2;
                     Rab3-interacting protein"
                     /calculated_mol_wt=123070
     Region          384..483
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(408..414,429,432,462,466,469..470)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          535..661
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(566,572,627,629,637)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          912..1057
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(969,973..974,976,979,1007,1009,1011,1055..1056)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..1081
                     /gene="RIMS2"
                     /gene_synonym="CRSDS; OBOE; RAB3IP3; RIM2"
                     /coded_by="NM_001348502.2:289..3534"
                     /note="isoform w is encoded by transcript variant 23"
                     /db_xref="CCDS:CCDS94332.1"
                     /db_xref="GeneID:9699"
                     /db_xref="HGNC:HGNC:17283"
                     /db_xref="MIM:606630"
ORIGIN      
        1 mqfetlrqvc nsvlshfhgv fssppnilqn elfgqtlnna rkrspsvsrd qnrrydqree
       61 reeysqyats dtamprspsd yadrrsqhep qfyedsdhls yrdsnrrshr hskeyivdde
      121 dvesrdeyer qrreeeyqsr yrsdpnlary pvkpqpyeeq mrihaevsra rherrhsdvs
      181 lanadledsr ismlrmdrps rqrsiserra amenqrsysm ertreaqgps syaqrttnhs
      241 pptprrsplp idrpdlrrtd slrkqhhldp ssavrktkre kmetmlrnds lssdqsesvr
      301 ppppkphksk kggkmrqisl ssseeelast peytscddve iesesvsekg dmdynwldht
      361 swhsseaspm slhpvtwqps kdgdrligri llnkrlkdgs vprdsgamlg lkvvggkmte
      421 sgrlcafitk vkkgsladtv ghlrpgdevl ewngrllqga tfeevyniil eskpepqvel
      481 vvsrpigdip ripdsthaql esssssfesq kmdrpsisvt spmspgmlrd vpqflsgqls
      541 iklwfdkvgh qlivtilgak dlpsredgrp rnpyvkiyfl pdrsdknkrr tktvkktlep
      601 kwnqtfiysp vhrrefrerm leitlwdqar vreeeseflg eilieletal lddephwykl
      661 qthdvsslpl phpspymprr qlhgesptrr lqrskrisds evsdydcddg igvvsdyrhd
      721 grdlqsstls vpeqvmssnh cspsgsphrv dvigrtrsws psvpppqsrn veqglrgtrt
      781 mtghyntisr mdrhrvmddh yspdrdrshp rtgsvqtsps stpvagrrgr qlpqlppkgt
      841 ldrkaggkkl rstvqrstet glavemrnwm trqasrestd gsmnsysseg nlifpgvrla
      901 sdsqfsdfld glgpaqlvgr qtlatpamgd iqvgmmdkkg qleveiirar glvvkpgskt
      961 lpapyvkvyl ldngvciakk ktkvarktle plyqqllsfe espqgkvlqi ivwgdygrmd
     1021 hksfmgvaqi lldelelsnm vigwfklfpp sslvdptlap ltrrasqssl esstgpsysr
     1081 s
//
LOCUS       NP_001352356             259 aa            linear   PRI 21-NOV-2025
DEFINITION  TRPM8 channel-associated factor 2 isoform D [Homo sapiens].
ACCESSION   NP_001352356
VERSION     NP_001352356.1
DBSOURCE    REFSEQ: accession NM_001365427.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Yun,D., Liang,J., Wang,X., Fan,J., Wang,X., Li,J., Ren,X., Liu,J.,
            Ren,X., Zhang,H., Shang,G., Jin,W., Chen,L., Li,T., Zhang,C., Yu,S.
            and Yang,X.
  TITLE     TCAF2 drives glioma cellular migratory/invasion properties through
            STAT3 signaling
  JOURNAL   Mol Cell Biochem 479 (7), 1801-1815 (2024)
   PUBMED   38019450
  REMARK    GeneRIF: TCAF2 drives glioma cellular migratory/invasion properties
            through STAT3 signaling.
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Li,Y., Li,J., Chen,H., Lu,B., Lu,F., Chen,H., Liu,H. and Qian,C.
  TITLE     TCAF2 is associated with the immune microenvironment, promotes
            pathogenesis, and impairs prognosis in glioma
  JOURNAL   Gene 883, 147667 (2023)
   PUBMED   37506986
  REMARK    GeneRIF: TCAF2 is associated with the immune microenvironment,
            promotes pathogenesis, and impairs prognosis in glioma.
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Li,X., Qi,Q., Li,Y., Miao,Q., Yin,W., Pan,J., Zhao,Z., Chen,X.,
            Yang,F., Zhou,X., Huang,M., Wang,C., Deng,L., Huang,D., Qi,M.,
            Fan,S., Zhang,Y., Qiu,S., Deng,W., Liu,T., Chen,M., Ye,W. and
            Zhang,D.
  TITLE     TCAF2 in Pericytes Promotes Colorectal Cancer Liver Metastasis via
            Inhibiting Cold-Sensing TRPM8 Channel
  JOURNAL   Adv Sci (Weinh) 10 (30), e2302717 (2023)
   PUBMED   37635201
  REMARK    GeneRIF: TCAF2 in Pericytes Promotes Colorectal Cancer Liver
            Metastasis via Inhibiting Cold-Sensing TRPM8 Channel.
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Hsieh,P., Dang,V., Vollger,M.R., Mao,Y., Huang,T.H., Dishuck,P.C.,
            Baker,C., Cantsilieris,S., Lewis,A.P., Munson,K.M., Sorensen,M.,
            Welch,A.E., Underwood,J.G. and Eichler,E.E.
  TITLE     Evidence for opposing selective forces operating on human-specific
            duplicated TCAF genes in Neanderthals and humans
  JOURNAL   Nat Commun 12 (1), 5118 (2021)
   PUBMED   34433829
  REMARK    GeneRIF: Evidence for opposing selective forces operating on
            human-specific duplicated TCAF genes in Neanderthals and humans.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 259)
  AUTHORS   Gkika,D., Lemonnier,L., Shapovalov,G., Gordienko,D., Poux,C.,
            Bernardini,M., Bokhobza,A., Bidaux,G., Degerny,C., Verreman,K.,
            Guarmit,B., Benahmed,M., de Launoit,Y., Bindels,R.J., Fiorio Pla,A.
            and Prevarskaya,N.
  TITLE     TRP channel-associated factors are a novel protein family that
            regulates TRPM8 trafficking and activity
  JOURNAL   J Cell Biol 208 (1), 89-107 (2015)
   PUBMED   25559186
  REMARK    GeneRIF: Report novel TRP channel-associated factors that modulate
            TRPM8 activity.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK315909.1 and AC073264.5.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.56275.1,
                                           SRR14038195.2772630.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q35"
     Protein         1..259
                     /product="TRPM8 channel-associated factor 2 isoform D"
                     /note="family with sequence similarity 139, member A;
                     protein FAM115C; family with sequence similarity 115,
                     member C; TRP channel-associated factor 2"
                     /calculated_mol_wt=27319
     CDS             1..259
                     /gene="TCAF2"
                     /gene_synonym="FAM115C; FAM139A; GATD9; GATD9B"
                     /coded_by="NM_001365427.2:62..841"
                     /note="isoform D is encoded by transcript variant 5"
                     /db_xref="GeneID:285966"
                     /db_xref="HGNC:HGNC:26878"
                     /db_xref="MIM:616252"
ORIGIN      
        1 matiaaaafe almdgvtcwd vprgpipsel lligeaafpv mvndkgqvli aassygrgrl
       61 vvvshegyls haglasflln avswlcpcpg apvgvrpsla plvnilqdag leaqvkpepg
      121 eplgvycina yndtltatli qfvkhgggll iggqawywas qhgpdkvlsr fpgnkvtsva
      181 gvyftdtygd rdrfkvskkv pkiplhvrri pwehppaeic tsatilsgrr kgkgsaasla
      241 taciissqrr stgsgsfra
//
LOCUS       NP_001305257            1184 aa            linear   PRI 21-NOV-2025
DEFINITION  wings apart-like protein homolog isoform 2 [Homo sapiens].
ACCESSION   NP_001305257 XP_006717792
VERSION     NP_001305257.1
DBSOURCE    REFSEQ: accession NM_001318328.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1184)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1184)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1184)
  AUTHORS   Haarhuis,J.H.I., van der Weide,R.H., Blomen,V.A., Flach,K.D.,
            Teunissen,H., Willems,L., Brummelkamp,T.R., Rowland,B.D. and de
            Wit,E.
  TITLE     A Mediator-cohesin axis controls heterochromatin domain formation
  JOURNAL   Nat Commun 13 (1), 754 (2022)
   PUBMED   35136067
  REMARK    GeneRIF: A Mediator-cohesin axis controls heterochromatin domain
            formation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1184)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1184)
  AUTHORS   Kumagai,K., Takanashi,M., Ohno,S.I., Harada,Y., Fujita,K.,
            Oikawa,K., Sudo,K., Ikeda,S.I., Nishi,H., Oikawa,K. and Kuroda,M.
  TITLE     WAPL induces cervical intraepithelial neoplasia modulated with
            estrogen signaling without HPV E6/E7
  JOURNAL   Oncogene 40 (21), 3695-3706 (2021)
   PUBMED   33947962
  REMARK    GeneRIF: WAPL induces cervical intraepithelial neoplasia modulated
            with estrogen signaling without HPV E6/E7.
REFERENCE   6  (residues 1 to 1184)
  AUTHORS   Kuroda,M., Oikawa,K., Ohbayashi,T., Yoshida,K., Yamada,K.,
            Mimura,J., Matsuda,Y., Fujii-Kuriyama,Y. and Mukai,K.
  TITLE     A dioxin sensitive gene, mammalian WAPL, is implicated in
            spermatogenesis
  JOURNAL   FEBS Lett 579 (1), 167-172 (2005)
   PUBMED   15620708
REFERENCE   7  (residues 1 to 1184)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   8  (residues 1 to 1184)
  AUTHORS   Kwiatkowski,B.A., Ragoczy,T., Ehly,J. and Schubach,W.H.
  TITLE     Identification and cloning of a novel chromatin-associated protein
            partner of Epstein-Barr nuclear protein 2
  JOURNAL   Exp Cell Res 300 (1), 223-233 (2004)
   PUBMED   15383329
  REMARK    GeneRIF: FOE encodes a protein of 1227 amino acids with a
            functional bipartite nuclear localization signal, an arginine-rich
            motif, a putative nuclear export signal as well as with three
            highly acidic regions and a predicted coiled-coil domain.
REFERENCE   9  (residues 1 to 1184)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   10 (residues 1 to 1184)
  AUTHORS   Fallone,C.A.
  TITLE     Epidemiology of the antibiotic resistance of Helicobacter pylori in
            Canada
  JOURNAL   Can J Gastroenterol 14 (10), 879-882 (2000)
   PUBMED   11111111
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL731569.18 and AL844892.5.
            
            On Jan 1, 2016 this sequence version replaced XP_006717792.1.
            
            Transcript Variant: This variant (2) uses an alternate, in-frame
            splice site in the 5' coding region compared to variant 1. It
            encodes isoform 2, which is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC140858.1, SRR11853566.3612.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.2"
     Protein         1..1184
                     /product="wings apart-like protein homolog isoform 2"
                     /note="friend of EBNA2 (Epstein-Barr virus nuclear protein
                     2); wings apart-like protein homolog; friend of EBNA2
                     protein"
                     /calculated_mol_wt=132095
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Region          46..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Region          73..75
                     /region_name="FGF motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            168
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Region          429..431
                     /region_name="FGF motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Region          453..455
                     /region_name="FGF motif 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Region          632..992
                     /region_name="WAPL"
                     /note="Wings apart-like protein regulation of
                     heterochromatin; pfam07814"
                     /db_xref="CDD:462278"
     Site            898
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     CDS             1..1184
                     /gene="WAPL"
                     /gene_synonym="FOE; KIAA0261; WAPAL"
                     /coded_by="NM_001318328.2:451..4005"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:23063"
                     /db_xref="HGNC:HGNC:23293"
                     /db_xref="MIM:610754"
ORIGIN      
        1 mtsrfgktys rkggngsskf devfsnkrtt lstkwgettf maklgqkrpn fkpdiqeipk
       61 kpkveeestg dpfgfdsdde slpvssknla qvkcssyses seaaqleevt svleanskis
      121 hvvvedtvvs dkcfpledtl lgkekstnri veddasissc nklitsdkve nfheehekns
      181 hhihknadds tkkpnaettv aseiketndt wnsqfgkrpe spseispikg svrtglfewd
      241 ndfedirsed cilsldsdpl lemkdddfkn rlenlneaie edivqsvlrp tncrtycran
      301 ktkssqgasn fdklmdgtsq alakansess kdglnqakkg gvscgtsfrg tvgrtrdytv
      361 lhpsclsvcn vtiqdtmers mdeftastpa dlgeagrlrk kadiatsktt trfrpsntks
      421 kkdvkleffg fedhetggde ggsgssnyki kyfgfddlse seddedddcq verktskkrt
      481 ktapspslqp ppesndnsqd sqsgtnnaed lpgvpesvkk pinkqgdksk entrkifsgp
      541 krsptkavyn arhwnhpdse elpgppvvkp qsvtvrlssk epnqkddgvf kapappskvi
      601 ktvtiptqpy qdivtalkcr redkelytvv qhvkhfndvv efgenqeftd dieyllsglk
      661 stqplntrcl svislatkca mpsfrmhlra hgmvamvfkt lddsqhhqnl slctaalmyi
      721 lsrdrlnmdl drasldlmir lleleqdass akllnekdmn kikekirrlc etvhnkhldl
      781 enittghlam etllsltskr agdwfkeelr llggldhivd kvkecvdhls rdedeeklva
      841 slwgaerclr vlesvtvhnp enqsyliayk dsqlivssak alqhceeliq qynraedsic
      901 ladskplphq nvtnhvgkav edcmraiigv llnltndnew gstktgeqdg ligtalncvl
      961 qvpkylpqeq rfdirvlglg llinlveysa rnrhclvnme tscsfdssic sgegddslri
     1021 ggqvhavqal vqlflerera aqlaesktde likdapttqh dksgewqets geiqwvstek
     1081 tdgteekhkk eeedeeldln kalqhagkhm edcivasyta lllgclcqes pinvttvrey
     1141 lpegdfsimt emlkkflsfm nltcavgttg qksisrviey lehc
//
LOCUS       NP_937859                240 aa            linear   PRI 21-NOV-2025
DEFINITION  small nuclear ribonucleoprotein-associated proteins B and B'
            isoform B' [Homo sapiens].
ACCESSION   NP_937859
VERSION     NP_937859.1
DBSOURCE    REFSEQ: accession NM_198216.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Schneider,S., Brandina,I., Peter,D., Lagad,S., Fraudeau,A.,
            Portell-Montserrat,J., Tholen,J., Zhao,J. and Galej,W.P.
  TITLE     Structure of the human 20S U5 snRNP
  JOURNAL   Nat Struct Mol Biol 31 (5), 752-756 (2024)
   PUBMED   38467877
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Chu,J.L. and Elkon,K.B.
  TITLE     The small nuclear ribonucleoproteins, SmB and B', are products of a
            single gene
  JOURNAL   Gene 97 (2), 311-312 (1991)
   PUBMED   1825643
REFERENCE   7  (residues 1 to 240)
  AUTHORS   Sharpe,N.G., Williams,D.G. and Latchman,D.S.
  TITLE     Regulated expression of the small nuclear ribonucleoprotein
            particle protein SmN in embryonic stem cell differentiation
  JOURNAL   Mol Cell Biol 10 (12), 6817-6820 (1990)
   PUBMED   2174118
REFERENCE   8  (residues 1 to 240)
  AUTHORS   Elkon,K.B., Hines,J.J., Chu,J.L. and Parnassa,A.
  TITLE     Epitope mapping of recombinant HeLa SmB and B' peptides obtained by
            the polymerase chain reaction
  JOURNAL   J Immunol 145 (2), 636-643 (1990)
   PUBMED   1694885
REFERENCE   9  (residues 1 to 240)
  AUTHORS   Schmauss,C. and Lerner,M.R.
  TITLE     The closely related small nuclear ribonucleoprotein polypeptides N
            and B/B' are distinguishable by antibodies as well as by
            differences in their mRNAs and gene structures
  JOURNAL   J Biol Chem 265 (18), 10733-10739 (1990)
   PUBMED   1693924
REFERENCE   10 (residues 1 to 240)
  AUTHORS   Schmauss,C., McAllister,G., Ohosone,Y., Hardin,J.A. and Lerner,M.R.
  TITLE     A comparison of snRNP-associated Sm-autoantigens: human N, rat N
            and human B/B'
  JOURNAL   Nucleic Acids Res 17 (4), 1733-1743 (1989)
   PUBMED   2522186
  REMARK    Erratum:[Nucleic Acids Res 1989 Aug 25;17(16):6777]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM559678.1 and X17568.1.
            
            Summary: The protein encoded by this gene is one of several nuclear
            proteins that are found in common among U1, U2, U4/U6, and U5 small
            ribonucleoprotein particles (snRNPs). These snRNPs are involved in
            pre-mRNA splicing, and the encoded protein may also play a role in
            pre-mRNA splicing or snRNP structure. Autoantibodies from patients
            with systemic lupus erythematosus frequently recognize epitopes on
            the encoded protein. Two transcript variants encoding different
            isoforms (B and B') have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (B').
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.584125.1,
                                           SRR1163658.213972.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..240
                     /product="small nuclear ribonucleoprotein-associated
                     proteins B and B' isoform B'"
                     /note="Sm protein B/B'; small nuclear ribonucleoprotein
                     polypeptides B and B'; small nuclear
                     ribonucleoprotein-associated proteins B and B'; B
                     polypeptide of Sm protein; small nuclear ribonucleoprotein
                     polypeptide B; sm-B/Sm-B'"
                     /calculated_mol_wt=24479
     Region          5..83
                     /region_name="Sm_B"
                     /note="Sm protein B; cd01717"
                     /db_xref="CDD:212464"
     Site            order(8,14,22..23,32,36,43..44,69..82)
                     /site_type="other"
                     /note="heptamer interface [polypeptide binding]"
                     /db_xref="CDD:212464"
     Site            order(17..23,25..37,39..43)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212464"
     Site            order(20..25,27,33..34,37,39,41,60,65,67,69..79)
                     /site_type="other"
                     /note="putative hexamer interface [polypeptide binding]"
                     /db_xref="CDD:212464"
     Site            order(36..39,49,59..61,73,75)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212464"
     Site            69..80
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212464"
     Site            108
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; Dimethylated
                     arginine, in A2780 ovarian carcinoma cell line.
                     /evidence=ECO:0000269|Ref.10; Omega-N-methylarginine,
                     alternate. /evidence=ECO:0007744|PubMed:24129315;
                     propagated from UniProtKB/Swiss-Prot (P14678.2)"
     Site            112
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; Dimethylated
                     arginine, in A2780 ovarian carcinoma cell line.
                     /evidence=ECO:0000269|Ref.10; Omega-N-methylarginine,
                     alternate. /evidence=ECO:0007744|PubMed:24129315;
                     propagated from UniProtKB/Swiss-Prot (P14678.2)"
     Site            147
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000269|Ref.10; propagated from
                     UniProtKB/Swiss-Prot (P14678.2)"
     Region          163..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P14678.2)"
     Site            172
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P63162; propagated from
                     UniProtKB/Swiss-Prot (P14678.2)"
     Region          175..236
                     /region_name="Repeat-rich region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14678.2)"
     CDS             1..240
                     /gene="SNRPB"
                     /gene_synonym="CCMS; COD; Sm-B/B'; SmB/B'; SmB/SmB';
                     snRNP-B; SNRPB1"
                     /coded_by="NM_198216.2:100..822"
                     /note="isoform B' is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13026.1"
                     /db_xref="GeneID:6628"
                     /db_xref="HGNC:HGNC:11153"
                     /db_xref="MIM:182282"
ORIGIN      
        1 mtvgksskml qhidyrmrci lqdgrifigt fkafdkhmnl ilcdcdefrk ikpknskqae
       61 reekrvlglv llrgenlvsm tvegpppkdt giarvplaga aggpgigraa grgipagvpm
      121 pqapaglagp vrgvggpsqq vmtpqgrgtv aaaaaaatas iagaptqypp grggppppmg
      181 rgapppgmmg pppgmrppmg ppmgippgrg tpmgmpppgm rppppgmrgp pppgmrpprp
//
LOCUS       NP_001231812             166 aa            linear   PRI 21-NOV-2025
DEFINITION  dihydrolipoyllysine-residue succinyltransferase component of
            2-oxoglutarate dehydrogenase complex, mitochondrial isoform 2
            precursor [Homo sapiens].
ACCESSION   NP_001231812
VERSION     NP_001231812.1
DBSOURCE    REFSEQ: accession NM_001244883.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Hevler,J.F., Albanese,P., Cabrera-Orefice,A., Potter,A.,
            Jankevics,A., Misic,J., Scheltema,R.A., Brandt,U., Arnold,S. and
            Heck,A.J.R.
  TITLE     MRPS36 provides a structural link in the eukaryotic 2-oxoglutarate
            dehydrogenase complex
  JOURNAL   Open Biol 13 (3), 220363 (2023)
   PUBMED   36854377
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Anderson,N.M., Qin,X., Finan,J.M., Lam,A., Athoe,J., Missiaen,R.,
            Skuli,N., Kennedy,A., Saini,A.S., Tao,T., Zhu,S., Nissim,I.,
            Look,A.T., Qing,G., Simon,M.C. and Feng,H.
  TITLE     Metabolic Enzyme DLST Promotes Tumor Aggression and Reveals a
            Vulnerability to OXPHOS Inhibition in High-Risk Neuroblastoma
  JOURNAL   Cancer Res 81 (17), 4417-4430 (2021)
   PUBMED   34233924
  REMARK    GeneRIF: Metabolic Enzyme DLST Promotes Tumor Aggression and
            Reveals a Vulnerability to OXPHOS Inhibition in High-Risk
            Neuroblastoma.
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Buffet,A., Zhang,J., Rebel,H., Corssmit,E.P.M., Jansen,J.C.,
            Hensen,E.F., Bovee,J.V.M.G., Morini,A., Gimenez-Roqueplo,A.P.,
            Hes,F.J., Devilee,P., Favier,J. and Bayley,J.P.
  TITLE     Germline DLST Variants Promote Epigenetic Modifications in
            Pheochromocytoma-Paraganglioma
  JOURNAL   J Clin Endocrinol Metab 106 (2), 459-471 (2021)
   PUBMED   33180916
  REMARK    GeneRIF: Germline DLST Variants Promote Epigenetic Modifications in
            Pheochromocytoma-Paraganglioma.
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 166)
  AUTHORS   Chuang,D.T., Fisher,C.W., Lau,K.S., Griffin,T.A., Wynn,R.M. and
            Cox,R.P.
  TITLE     Maple syrup urine disease: domain structure, mutations and exon
            skipping in the dihydrolipoyl transacylase (E2) component of the
            branched-chain alpha-keto acid dehydrogenase complex
  JOURNAL   Mol Biol Med 8 (1), 49-63 (1991)
   PUBMED   1943690
REFERENCE   7  (residues 1 to 166)
  AUTHORS   Reed,L.J. and Hackert,M.L.
  TITLE     Structure-function relationships in dihydrolipoamide
            acyltransferases
  JOURNAL   J Biol Chem 265 (16), 8971-8974 (1990)
   PUBMED   2188967
  REMARK    Review article
REFERENCE   8  (residues 1 to 166)
  AUTHORS   Fregeau,D.R., Prindiville,T., Coppel,R.L., Kaplan,M., Dickson,E.R.
            and Gershwin,M.E.
  TITLE     Inhibition of alpha-ketoglutarate dehydrogenase activity by a
            distinct population of autoantibodies recognizing dihydrolipoamide
            succinyltransferase in primary biliary cirrhosis
  JOURNAL   Hepatology 11 (6), 975-981 (1990)
   PUBMED   2365294
REFERENCE   9  (residues 1 to 166)
  AUTHORS   Ono,K., Hakozaki,M., Kimura,A. and Kochi,H.
  TITLE     Purification, resolution, and reconstitution of rat liver
            branched-chain alpha-keto acid dehydrogenase complex
  JOURNAL   J Biochem 101 (1), 19-27 (1987)
   PUBMED   3571202
REFERENCE   10 (residues 1 to 166)
  AUTHORS   Kochi,H., Seino,H. and Ono,K.
  TITLE     Inhibition of glycine oxidation by pyruvate, alpha-ketoglutarate,
            and branched-chain alpha-keto acids in rat liver mitochondria:
            presence of interaction between the glycine cleavage system and
            alpha-keto acid dehydrogenase complexes
  JOURNAL   Arch Biochem Biophys 249 (2), 263-272 (1986)
   PUBMED   3753002
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC338747.1, AK300396.1,
            DA995927.1 and AC006530.4.
            
            Summary: This gene encodes a mitochondrial protein that belongs to
            the 2-oxoacid dehydrogenase family. This protein is one of the
            three components (the E2 component) of the 2-oxoglutarate
            dehydrogenase complex that catalyzes the overall conversion of
            2-oxoglutarate to succinyl-CoA and CO(2). Alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Transcript Variant: This variant (2) differs at the 3' end compared
            to variant 1. This results in a shorter isoform (2) with a distinct
            C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK300396.1, HY180550.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..166
                     /product="dihydrolipoyllysine-residue succinyltransferase
                     component of 2-oxoglutarate dehydrogenase complex,
                     mitochondrial isoform 2 precursor"
                     /EC_number="2.3.1.61"
                     /note="dihydrolipoyllysine-residue succinyltransferase
                     component of 2-oxoglutarate dehydrogenase complex,
                     mitochondrial; E2K; OGDC-E2; dihydrolipoamide
                     S-succinyltransferase (E2 component of 2-oxo-glutarate
                     complex)"
                     /calculated_mol_wt=10511
     transit_peptide 1..67
                     /calculated_mol_wt=7384
     mat_peptide     68..166
                     /product="dihydrolipoyllysine-residue succinyltransferase
                     component of 2-oxoglutarate dehydrogenase complex,
                     mitochondrial isoform 2"
                     /calculated_mol_wt=10511
     Region          71..>149
                     /region_name="sucB"
                     /note="2-oxoglutarate dehydrogenase complex
                     dihydrolipoamide succinyltransferase (E2 component);
                     TIGR01347"
                     /db_xref="CDD:273565"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (P36957.4)"
     CDS             1..166
                     /gene="DLST"
                     /gene_synonym="DLTS; KGD2; PGL7; PPGL7"
                     /coded_by="NM_001244883.2:39..539"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:1743"
                     /db_xref="HGNC:HGNC:2911"
                     /db_xref="MIM:126063"
ORIGIN      
        1 mlsrsrcvsr afsrslsafq kgncplgrrs lpgvslcqgp gypnsrkvvi nnsvfsvrff
       61 rttavckddl vtvktpafae svtegdvrwe kavgdtvaed evvceietdk tsvqvpspan
      121 gvieallvpd ggkveggtpl ftlrktggke vllvvkvssv pswdwd
//
LOCUS       NP_001028777             882 aa            linear   PRI 21-NOV-2025
DEFINITION  protein PTHB1 isoform 4 [Homo sapiens].
ACCESSION   NP_001028777
VERSION     NP_001028777.1
DBSOURCE    REFSEQ: accession NM_001033605.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 882)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 882)
  AUTHORS   Zhang,Y., Xu,M., Zhang,M., Yang,G. and Li,X.
  TITLE     A Novel BBS9 Mutation Identified via Whole-Exome Sequencing in a
            Chinese Family with Bardet-Biedl Syndrome
  JOURNAL   Biomed Res Int 2021, 4514967 (2021)
   PUBMED   34692830
  REMARK    GeneRIF: A Novel BBS9 Mutation Identified via Whole-Exome
            Sequencing in a Chinese Family with Bardet-Biedl Syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 882)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 882)
  AUTHORS   Jeziorny,K., Antosik,K., Jakiel,P., Mlynarski,W., Borowiec,M. and
            Zmyslowska,A.
  TITLE     Next-Generation Sequencing in the Diagnosis of Patients with
            Bardet-Biedl Syndrome-New Variants and Relationship with
            Hyperglycemia and Insulin Resistance
  JOURNAL   Genes (Basel) 11 (11), 1283 (2020)
   PUBMED   33138063
  REMARK    GeneRIF: Next-Generation Sequencing in the Diagnosis of Patients
            with Bardet-Biedl Syndrome-New Variants and Relationship with
            Hyperglycemia and Insulin Resistance.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 882)
  AUTHORS   Nachury,M.V., Loktev,A.V., Zhang,Q., Westlake,C.J., Peranen,J.,
            Merdes,A., Slusarski,D.C., Scheller,R.H., Bazan,J.F.,
            Sheffield,V.C. and Jackson,P.K.
  TITLE     A core complex of BBS proteins cooperates with the GTPase Rab8 to
            promote ciliary membrane biogenesis
  JOURNAL   Cell 129 (6), 1201-1213 (2007)
   PUBMED   17574030
REFERENCE   6  (residues 1 to 882)
  AUTHORS   Nishimura,D.Y., Swiderski,R.E., Searby,C.C., Berg,E.M.,
            Ferguson,A.L., Hennekam,R., Merin,S., Weleber,R.G., Biesecker,L.G.,
            Stone,E.M. and Sheffield,V.C.
  TITLE     Comparative genomics and gene expression analysis identifies BBS9,
            a new Bardet-Biedl syndrome gene
  JOURNAL   Am J Hum Genet 77 (6), 1021-1033 (2005)
   PUBMED   16380913
  REMARK    GeneRIF: Comparative genomics and gene expression analysis
            identifies PHTB1 protein as BBS9, a new Bardet-Biedl syndrome gene.
REFERENCE   7  (residues 1 to 882)
  AUTHORS   Vernon,E.G., Malik,K., Reynolds,P., Powlesland,R., Dallosso,A.R.,
            Jackson,S., Henthorn,K., Green,E.D. and Brown,K.W.
  TITLE     The parathyroid hormone-responsive B1 gene is interrupted by a
            t(1;7)(q42;p15) breakpoint associated with Wilms' tumour
  JOURNAL   Oncogene 22 (9), 1371-1380 (2003)
   PUBMED   12618763
  REMARK    GeneRIF: gene is interrupted by a t(1;7)(q42;p15) breakpoint
            associated with Wilms' tumour; new alternately spliced isoforms
            were found in a wide range of adult and foetal tissues
REFERENCE   8  (residues 1 to 882)
  AUTHORS   Adams,A.E., Rosenblatt,M. and Suva,L.J.
  TITLE     Identification of a novel parathyroid hormone-responsive gene in
            human osteoblastic cells
  JOURNAL   Bone 24 (4), 305-313 (1999)
   PUBMED   10221542
REFERENCE   9  (residues 1 to 882)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 882)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL704922.1, BC103831.2,
            BI254810.1, U85994.1 and AC078833.5.
            
            Summary: This gene is downregulated by parathyroid hormone in
            osteoblastic cells, and therefore is thought to be involved in
            parathyroid hormone action in bones. The exact function of this
            gene has not yet been determined. Alternatively spliced transcript
            variants encoding different isoforms have been identified.
            [provided by RefSeq, Jan 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3979662.1,
                                           SRR14038196.3626787.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..882
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.3"
     Protein         1..882
                     /product="protein PTHB1 isoform 4"
                     /note="protein PTHB1; PTH-responsive osteosarcoma B1
                     protein; bardet-Biedl syndrome 9 protein; parathyroid
                     hormone-responsive B1 gene protein"
                     /calculated_mol_wt=98552
     Region          1..418
                     /region_name="PHTB1_N"
                     /note="PTHB1 N-terminus; pfam14727"
                     /db_xref="CDD:464284"
     Region          1..407
                     /region_name="Seven-bladed beta-propeller.
                     /evidence=ECO:0000269|PubMed:26085087"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SYG4.1)"
     Site            141
                     /site_type="other"
                     /note="Critical for protein stability.
                     /evidence=ECO:0000269|PubMed:26085087; propagated from
                     UniProtKB/Swiss-Prot (Q3SYG4.1)"
     Region          441..814
                     /region_name="PHTB1_C"
                     /note="PTHB1 C-terminus; pfam14728"
                     /db_xref="CDD:464285"
     Region          680..760
                     /region_name="Interaction with LZTL1.
                     /evidence=ECO:0000269|PubMed:22072986"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SYG4.1)"
     Region          845..882
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SYG4.1)"
     CDS             1..882
                     /gene="BBS9"
                     /gene_synonym="B1; C18; D1; PTHB1"
                     /coded_by="NM_001033605.2:490..3138"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS34618.1"
                     /db_xref="GeneID:27241"
                     /db_xref="HGNC:HGNC:30000"
                     /db_xref="MIM:607968"
ORIGIN      
        1 mslfkardww stilgdkeef dqgclclanv dnsgngqdki ivgsfmgylr ifsphpaktg
       61 dgaqaedlll evdlrdpvlq vevgkfvsgt emlhlavlhs rklcvysvsg tlgnvehgnq
      121 cqmklmyehn lqrtacnmty gsfggvkgrd liciqsmdgm lmvfeqesya fgrflpgfll
      181 pgplayssrt dsfltvsscq qvesykyqvl afatdadkrq eteqqklgsg krlvvdwtln
      241 igeqaldici vsfnqsassv fvlgernffc lkdngqirfm kkldwspscf lpycsvsegt
      301 intlignhnn mlhiyqdvtl kwatqlphip vavrvgclhd lkgvivtlsd dghlqcsylg
      361 tdpslfqapn vqsrelnyde ldvemkelqk iikdvnksqg vwpmteredd lnvsvvvspn
      421 fdsvsqatdv evgtdlvpsv tvkvtlqnrv ilqkaklsvy vqppleltcd qftfefmtpd
      481 ltrtvsfsvy lkrsytpsel egnavvsysr ptgiprviqc kfrlplklic lpgqpsktas
      541 hkitidtnks pvsllslfpg fasqsdddqv nvmgfhflgg aritvlaskt sqryriqseq
      601 fedlwlitne lilrlqeyfe kqgvkdfacs fsgsiplqey felidhhfel ringekleel
      661 lseravqfra iqrrllarfk dktpaplqhl dtlldgtykq vialadavee nqgnlfqsft
      721 rlksathlvi llialwqkls adqvaileaa flplqedtqe lgweetvdaa ishllktcls
      781 ksskeqalnl nsqlnipkdt sqlkkhitll cdrlskggrl clstdaaapq tmvmpggctt
      841 ipesdleers veqdstelft nhrhltaetp rpevsplqgv se
//
LOCUS       NP_001269814             204 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase III subunit RPC8 isoform a [Homo
            sapiens].
ACCESSION   NP_001269814
VERSION     NP_001269814.1
DBSOURCE    REFSEQ: accession NM_001282885.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Ramsay,E.P., Abascal-Palacios,G., Daiss,J.L., King,H., Gouge,J.,
            Pilsl,M., Beuron,F., Morris,E., Gunkel,P., Engel,C. and Vannini,A.
  TITLE     Structure of human RNA polymerase III
  JOURNAL   Nat Commun 11 (1), 6409 (2020)
   PUBMED   33335104
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Franca,M.M., Han,X., Funari,M.F.A., Lerario,A.M., Nishi,M.Y.,
            Fontenele,E.G.P., Domenice,S., Jorge,A.A.L., Garcia-Galiano,D.,
            Elias,C.F. and Mendonca,B.B.
  TITLE     Exome Sequencing Reveals the POLR3H Gene as a Novel Cause of
            Primary Ovarian Insufficiency
  JOURNAL   J Clin Endocrinol Metab 104 (7), 2827-2841 (2019)
   PUBMED   30830215
  REMARK    GeneRIF: A pathogenic homozygous missense mutation (c.149A>G;
            p.Asp50Gly) in the POLR3H gene in two unrelated families with
            primary ovarian insufficiency was identified.
REFERENCE   6  (residues 1 to 204)
  AUTHORS   Owen,T.J., O'Neil,J.D., Dawson,C.W., Hu,C., Chen,X., Yao,Y.,
            Wood,V.H., Mitchell,L.E., White,R.J., Young,L.S. and Arrand,J.R.
  TITLE     Epstein-Barr virus-encoded EBNA1 enhances RNA polymerase
            III-dependent EBER expression through induction of EBER-associated
            cellular transcription factors
  JOURNAL   Mol Cancer 9, 241 (2010)
   PUBMED   20843307
  REMARK    GeneRIF: Findings reveal that RNA polymerase III-dependent EBER
            expression through induction of cellular transcription factors and
            add to the repertoire of EBNA1's transcription-regulatory
            properties.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 204)
  AUTHORS   Greco-Stewart,V.S., Schissel,E. and Pelchat,M.
  TITLE     The hepatitis delta virus RNA genome interacts with the human RNA
            polymerases I and III
  JOURNAL   Virology 386 (1), 12-15 (2009)
   PUBMED   19246067
  REMARK    GeneRIF: The authors demonstrate the interaction of both RNA
            polymerase I and III with hepatitis delta virus RNA, both in vitro
            and in human cells.
REFERENCE   8  (residues 1 to 204)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   9  (residues 1 to 204)
  AUTHORS   Hu,P., Wu,S., Sun,Y., Yuan,C.C., Kobayashi,R., Myers,M.P. and
            Hernandez,N.
  TITLE     Characterization of human RNA polymerase III identifies orthologues
            for Saccharomyces cerevisiae RNA polymerase III subunits
  JOURNAL   Mol Cell Biol 22 (22), 8044-8055 (2002)
   PUBMED   12391170
REFERENCE   10 (residues 1 to 204)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA449644.1, BU173504.1, AB051452.1, AK000365.1, AL023553.5 and
            BM701572.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR,
            compared to variant 1. Variants 1, 3, 5, and 6 encode the same
            isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.159366.1,
                                           SRR14372079.979616.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..204
                     /product="DNA-directed RNA polymerase III subunit RPC8
                     isoform a"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerase III subunit RPC8;
                     polymerase (RNA) III subunit H; RNA nucleotidyltransferase
                     (DNA-directed); RNA polymerase III subunit C8;
                     DNA-directed RNA polymerase III subunit H; DNA-directed
                     RNA polymerase III subunit 22.9 kDa polypeptide;
                     polymerase (RNA) III (DNA directed) polypeptide H
                     (22.9kD)"
                     /calculated_mol_wt=22787
     Region          2..81
                     /region_name="RNAP_III_Rpc25_N"
                     /note="Rpc25, N-terminal ribonucleoprotein (RNP) domain.
                     Rpc25 is a subunit of eukaryotic RNA polymerase (RNAP) III
                     and is homologous to Rpa43 of eukaryotic RNAP I, Rpb7 of
                     eukaryotic RNAP II, and RpoE of archaeal RNAP. Rpc25 has
                     two domains, an N-terminal RNP...; cd04330"
                     /db_xref="CDD:239822"
     Site            order(2..6,8,28,31..32,46..49,73,78,80)
                     /site_type="other"
                     /note="Rpc17 interaction site [polypeptide binding]"
                     /db_xref="CDD:239822"
     Region          83..201
                     /region_name="RNA_pol_Rbc25"
                     /note="RNA polymerase III subunit Rpc25; pfam08292"
                     /db_xref="CDD:400543"
     Region          158..179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y535.1)"
     CDS             1..204
                     /gene="POLR3H"
                     /gene_synonym="C25; RPC22.9; RPC8"
                     /coded_by="NM_001282885.2:57..671"
                     /note="isoform a is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS14018.1"
                     /db_xref="GeneID:171568"
                     /db_xref="HGNC:HGNC:30349"
                     /db_xref="MIM:619801"
ORIGIN      
        1 mfvlvemvdt vrippwqfer klndsiaeel nkklankvvy nvglciclfd itkledayvf
       61 pgdgashtkv hfrcvvfhpf ldeiligkik gcspegvhvs lgffddilip peslqqpakf
      121 deaeqvwvwe yeteegahdl ymdtgeeirf rvvdesfvdt sptgpssada ttsseelpkk
      181 eapytlvgsi sepglgllsw wtsn
//
LOCUS       NP_001362987             185 aa            linear   PRI 21-NOV-2025
DEFINITION  homeobox expressed in ES cells 1 [Homo sapiens].
ACCESSION   NP_001362987 XP_024309577
VERSION     NP_001362987.1
DBSOURCE    REFSEQ: accession NM_001376058.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Alesi,V., Dentici,M.L., Genovese,S., Loddo,S., Bellacchio,E.,
            Orlando,V., Di Tommaso,S., Catino,G., Calacci,C., Calvieri,G.,
            Pompili,D., Ubertini,G., Dallapiccola,B., Capolino,R. and
            Novelli,A.
  TITLE     Homozygous HESX1 and COL1A1 Gene Variants in a Boy with Growth
            Hormone Deficiency and Early Onset Osteoporosis
  JOURNAL   Int J Mol Sci 22 (2), 750 (2021)
   PUBMED   33451138
  REMARK    GeneRIF: Homozygous HESX1 and COL1A1 Gene Variants in a Boy with
            Growth Hormone Deficiency and Early Onset Osteoporosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Li,Y., Wang,R., Qiao,N., Peng,G., Zhang,K., Tang,K., Han,J.J. and
            Jing,N.
  TITLE     Transcriptome analysis reveals determinant stages controlling human
            embryonic stem cell commitment to neuronal cells
  JOURNAL   J Biol Chem 292 (48), 19590-19604 (2017)
   PUBMED   28972157
REFERENCE   5  (residues 1 to 185)
  AUTHORS   Madeira,J.L., Nishi,M.Y., Nakaguma,M., Benedetti,A.F.,
            Biscotto,I.P., Fernandes,T., Pequeno,T., Figueiredo,T.,
            Franca,M.M., Correa,F.A., Otto,A.P., Abrao,M., Miras,M.B.,
            Santos,S., Jorge,A.A., Costalonga,E.F., Mendonca,B.B., Arnhold,I.J.
            and Carvalho,L.R.
  TITLE     Molecular analysis of brazilian patients with combined pituitary
            hormone deficiency and orthotopic posterior pituitary lobe reveals
            eight different PROP1 alterations with three novel mutations
  JOURNAL   Clin Endocrinol (Oxf) 87 (6), 725-732 (2017)
   PUBMED   28734020
  REMARK    GeneRIF: Study did not identify HESX1 and LHX3 mutations by Sanger
            in brazilian patients with combined pituitary hormone deficiency
REFERENCE   6  (residues 1 to 185)
  AUTHORS   Dattani,M.T., Martinez-Barbera,J.P., Thomas,P.Q., Brickman,J.M.,
            Gupta,R., Martensson,I.L., Toresson,H., Fox,M., Wales,J.K.,
            Hindmarsh,P.C., Krauss,S., Beddington,R.S. and Robinson,I.C.
  TITLE     Mutations in the homeobox gene HESX1/Hesx1 associated with
            septo-optic dysplasia in human and mouse
  JOURNAL   Nat Genet 19 (2), 125-133 (1998)
   PUBMED   9620767
REFERENCE   7  (residues 1 to 185)
  AUTHORS   Kazanskaya,O.V., Severtzova,E.A., Barth,K.A., Ermakova,G.V.,
            Lukyanov,S.A., Benyumov,A.O., Pannese,M., Boncinelli,E.,
            Wilson,S.W. and Zaraisky,A.G.
  TITLE     Anf: a novel class of vertebrate homeobox genes expressed at the
            anterior end of the main embryonic axis
  JOURNAL   Gene 200 (1-2), 25-34 (1997)
   PUBMED   9373136
REFERENCE   8  (residues 1 to 185)
  AUTHORS   Wales,J.K. and Quarrell,O.W.
  TITLE     Evidence for possible Mendelian inheritance of septo-optic
            dysplasia
  JOURNAL   Acta Paediatr 85 (3), 391-392 (1996)
   PUBMED   8696006
REFERENCE   9  (residues 1 to 185)
  AUTHORS   Thomas,P.Q., Johnson,B.V., Rathjen,J. and Rathjen,P.D.
  TITLE     Sequence, genomic organization, and expression of the novel
            homeobox gene Hesx1
  JOURNAL   J Biol Chem 270 (8), 3869-3875 (1995)
   PUBMED   7876132
REFERENCE   10 (residues 1 to 185)
  AUTHORS   Bardakjian,T., Weiss,A. and Schneider,A.
  TITLE     Microphthalmia/Anophthalmia/Coloboma Spectrum - RETIRED CHAPTER,
            FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301552
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093928.2.
            
            On Nov 8, 2019 this sequence version replaced XP_024309577.1.
            
            Summary: This gene encodes a conserved homeobox protein that is a
            transcriptional repressor in the developing forebrain and pituitary
            gland. Mutations in this gene are associated with septooptic
            dysplasia, HESX1-related growth hormone deficiency, and combined
            pituitary hormone deficiency. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.73537.1,
                                           SRR18074968.2042808.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.3"
     Protein         1..185
                     /product="homeobox expressed in ES cells 1"
                     /note="Rathke pouch homeobox; homeobox protein ANF;
                     Rathke's pouch homeobox"
                     /calculated_mol_wt=21278
     Region          109..165
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     CDS             1..185
                     /gene="HESX1"
                     /gene_synonym="ANF; CPHD5; RPX"
                     /coded_by="NM_001376058.1:401..958"
                     /db_xref="CCDS:CCDS2881.1"
                     /db_xref="GeneID:8820"
                     /db_xref="HGNC:HGNC:4877"
                     /db_xref="MIM:601802"
ORIGIN      
        1 mspslqegaq lgenkpstcs fsierilgld qkkdcvplmk phrpwadtcs ssgkdgnlcl
       61 hvpnppsgis fpsvvdhpmp eeraskyeny fsaserlslk relswyrgrr prtaftqnqi
      121 evlenvfrvn cypgidired laqklnleed riqiwfqnrr aklkrshres qflmakknfn
      181 tnlle
//
LOCUS       NP_001382230            2428 aa            linear   PRI 21-NOV-2025
DEFINITION  myomegalin isoform 20 [Homo sapiens].
ACCESSION   NP_001382230
VERSION     NP_001382230.1
DBSOURCE    REFSEQ: accession NM_001395301.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2428)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2428)
  AUTHORS   Pan,R., Dai,J., Liang,W., Wang,H., Ye,L., Ye,S., Lin,Z., Huang,S.,
            Xiong,Y., Zhang,L., Lu,L., Wang,O., Shen,X., Liao,W. and Lu,X.
  TITLE     PDE4DIP contributes to colorectal cancer growth and chemoresistance
            through modulation of the NF1/RAS signaling axis
  JOURNAL   Cell Death Dis 14 (6), 373 (2023)
   PUBMED   37355626
  REMARK    GeneRIF: PDE4DIP contributes to colorectal cancer growth and
            chemoresistance through modulation of the NF1/RAS signaling axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2428)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   4  (residues 1 to 2428)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 2428)
  AUTHORS   Abou Ziki,M.D., Bhat,N., Neogi,A., Driscoll,T.P., Ugwu,N., Liu,Y.,
            Smith,E., Abboud,J.M., Chouairi,S., Schwartz,M.A., Akar,J.G. and
            Mani,A.
  TITLE     Epistatic interaction of PDE4DIP and DES mutations in familial
            atrial fibrillation with slow conduction
  JOURNAL   Hum Mutat 42 (10), 1279-1293 (2021)
   PUBMED   34289528
  REMARK    GeneRIF: Epistatic interaction of PDE4DIP and DES mutations in
            familial atrial fibrillation with slow conduction.
REFERENCE   6  (residues 1 to 2428)
  AUTHORS   Shimada,H., Kuboshima,M., Shiratori,T., Nabeya,Y., Takeuchi,A.,
            Takagi,H., Nomura,F., Takiguchi,M., Ochiai,T. and Hiwasa,T.
  TITLE     Serum anti-myomegalin antibodies in patients with esophageal
            squamous cell carcinoma
  JOURNAL   Int J Oncol 30 (1), 97-103 (2007)
   PUBMED   17143517
  REMARK    GeneRIF: MMGL-antibody is significantly with a favorable prognosis.
            Consequently, MMGL-anatibodies may be a useful tumor marker to
            diagnose and establish a prognosis in patients with esophageal
            squamous cell carcinoma.
REFERENCE   7  (residues 1 to 2428)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 2428)
  AUTHORS   Soejima,H., Kawamoto,S., Akai,J., Miyoshi,O., Arai,Y., Morohka,T.,
            Matsuo,S., Niikawa,N., Kimura,A., Okubo,K. and Mukai,T.
  TITLE     Isolation of novel heart-specific genes using the BodyMap database
  JOURNAL   Genomics 74 (1), 115-120 (2001)
   PUBMED   11374908
REFERENCE   9  (residues 1 to 2428)
  AUTHORS   Verde,I., Pahlke,G., Salanova,M., Zhang,G., Wang,S., Coletti,D.,
            Onuffer,J., Jin,S.L. and Conti,M.
  TITLE     Myomegalin is a novel protein of the golgi/centrosome that
            interacts with a cyclic nucleotide phosphodiesterase
  JOURNAL   J Biol Chem 276 (14), 11189-11198 (2001)
   PUBMED   11134006
REFERENCE   10 (residues 1 to 2428)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC239802.3 and AC239804.2.
            
            Summary: The protein encoded by this gene serves to anchor
            phosphodiesterase 4D to the Golgi/centrosome region of the cell.
            Defects in this gene may be a cause of myeloproliferative disorder
            (MBD) associated with eosinophilia. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..2428
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     Protein         1..2428
                     /product="myomegalin isoform 20"
                     /note="myomegalin; cardiomyopathy-associated protein 2"
                     /calculated_mol_wt=272554
     Region          1..376
                     /region_name="SMYLE_N"
                     /note="Short myomegalin-like EB1 binding proteins,
                     N-terminal domain; pfam18615"
                     /db_xref="CDD:465822"
     Region          403..1201
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1714..1783
                     /region_name="Olduvai"
                     /note="Olduvai domain; pfam06758"
                     /db_xref="CDD:429104"
     Region          <2003..>2180
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          <2105..2279
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     CDS             1..2428
                     /gene="PDE4DIP"
                     /gene_synonym="CMYA2; MMGL"
                     /coded_by="NM_001395301.1:408..7694"
                     /note="isoform 20 is encoded by transcript variant 20"
                     /db_xref="GeneID:9659"
                     /db_xref="HGNC:HGNC:15580"
                     /db_xref="MIM:608117"
ORIGIN      
        1 mkeicricar elcgnqrrwi fhtasklnlq vllshvlgkd vprdgkaefa cskcafmldr
       61 iyrfdtviar iealsierlq klllekdrlk fciasmyrkn nddsgaeika gngtvdmsvl
      121 pdarysallq edfaysgfec wvenedqiqe phschgsegp gnrprrcrgc aalrvadsdy
      181 eaickvprkv arsiscgpss rwstsictee palsevgppd lastkvppdg esmeeetpgs
      241 svesldasvq asppqqkdee tersakelgk cdccsddqap qhgcnhklel alsmikgldy
      301 kpiqsprgsr lpipvksslp gakpgpsmtd gvssgflnrs lkplyktpvs yplelsdlqe
      361 lwddlcedyl plrvqpmtee llkqqklnsh ettitqqsvs dshlaelqek iqqteatnki
      421 lqeklnemsy elkcaqessq kqdgtiqnlk etlksreret eelyqviegq ndtmaklrem
      481 lhqsqlgqlh ssegtspaqq qvalldlqsa lfcsqleiqk lqrvvrqker qladakqcvq
      541 fveaaahese qqkeaswkhn qelrkalqql qeelqnksqq lraweaekyn eirtqeqniq
      601 hlnhslshke qllqefrell qyrdnsdktl eanemllekl rqrihdkava leraidekfs
      661 aleekekelr qlrlavrerd hdlerlrdvl ssneatmqsm esllrakgle veqlsttcqn
      721 lqwlkeemet kfsrwqkeqe siiqqlqtsl hdrnkevedl satllcklgp gqseiaeelc
      781 qrlqrkerml qdllsdrnkq vlehemeiqg llqsvstreq esqaaaeklv qalmernsel
      841 qalrqylggr dslmsqapis nqqaevtptg rlgkqtdqgs mqipsrddst sltakedvsi
      901 prstlgdldt vaglekelsn akeelelmak keresqmels alqsmmavqe eelqvqaadm
      961 esltrniqik edlikdlqmq lvdpedipam erltqevlll rekvasvesq gqeisgnrrq
     1021 qlllmleglv dersrlneal qaerqlyssl vkfhahpess erdrtlqvel egaqvlrsrl
     1081 eevlgrsler lnrletlaai ggaaagddte dtsteftdsi eeeaahhshq qlvkvaleks
     1141 latvetqnps fsppspmggd snrclqeeml hlraefhqhl eekrkaeeel kelkaqieea
     1201 gfssvshirn tmlslclena elkeqmgeam sdgweieedk ekgevmvetv vtkeglsess
     1261 lqaefrklqg klknahniin llkeqlvlss kegnskltpe llvhltstie rintelvgsp
     1321 gkhqhqeegn vtvrpfprpq sldlgatftv dahqldnqsq prdpgpqsaf slpgstqhlr
     1381 sqlsqckqry qdlqekllls eatvfaqane lekyrvmlse slvkqdskqi qvdlqdlgye
     1441 tcgrseneae reettspece ehnslkemvl meglcseqgr rgstlassse rkplenqlgk
     1501 qeefrvygks enilvlrkdi kdlkaqlqna nkviqnlksr vrslsvtsdy ssslerprkl
     1561 ravgtlegss phsvpdedeg wlsdgtgafy spglqakkdl esliqrvsql eaqlpkngle
     1621 eklaeelrsa swpgkydsli qdqarelsyl rqkiregrgi cylitrhakd tvksfedllr
     1681 sndidyylgq sfreqlaqgs qlterltskl stkdhksekd qagleplalr lsrelqekek
     1741 vievlqakld arsltpsssh alsdshrsps stsflsdele acsdmdivse ythyeekkas
     1801 pshsdsihhs shsavlsskp sstsasqgak aesnsnpisl ptpqntpkea nqahsgfhfh
     1861 sipklaslpq aplpsapssf lpfsptgpll lgccetpvvs laeaqqelqm lqkqlgesas
     1921 tvppastatl lsndleadss yylnsaqphs pprgtielgr ilepgylgss gkwdvmrpqk
     1981 gsvsgdlssg ssvyqlnskp tgadlleehl geirnlrqrl eesicindrl reqlehrlts
     2041 targrgstsn fysqglesip qlcnenrvlr ednrrlqaql shvsrehsqe teslrealls
     2101 srshlqelek elehqkverq qlledlrekq qevlhfreer lslqendsrl qhklvllqqq
     2161 ceekqqlfes lqselqiyea lygnskkglk dsavsppvrd vgmnspalvf pssasstpgs
     2221 etpiinrang lgldtspvmk tppklegdat dgsfankhgr hvighiddys alrqqiaegk
     2281 llvkkivslv rsacsfpgle aqgtevlgsk gihelrssts alhhaleesa slltmfwraa
     2341 lpsthipvlp gkvgestere llelrtkvsk qerllqstte hlknanqqke smeqfivsql
     2401 trthdvlkka rtnlevkslr alpctpal
//
LOCUS       NP_001340499             799 aa            linear   PRI 21-NOV-2025
DEFINITION  intraflagellar transport protein 88 homolog isoform 5 [Homo
            sapiens].
ACCESSION   NP_001340499 XP_016876249
VERSION     NP_001340499.1
DBSOURCE    REFSEQ: accession NM_001353570.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 799)
  AUTHORS   Thuy,P.X., Jang,T.K. and Moon,E.Y.
  TITLE     Vinblastine Resistance Is Associated with Nephronophthisis
            3-Mediated Primary Cilia via Intraflagellar Transport Protein 88
            and Apoptosis-Antagonizing Transcription Factor
  JOURNAL   Int J Mol Sci 25 (19), 10369 (2024)
   PUBMED   39408701
  REMARK    GeneRIF: Vinblastine Resistance Is Associated with Nephronophthisis
            3-Mediated Primary Cilia via Intraflagellar Transport Protein 88
            and Apoptosis-Antagonizing Transcription Factor.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 799)
  AUTHORS   Odabasi,E., Conkar,D., Deretic,J., Batman,U., Frikstad,K.M.,
            Patzke,S. and Firat-Karalar,E.N.
  TITLE     CCDC66 regulates primary cilium length and signaling via
            interactions with transition zone and axonemal proteins
  JOURNAL   J Cell Sci 136 (3) (2023)
   PUBMED   36606424
REFERENCE   4  (residues 1 to 799)
  AUTHORS   Chan,H.Y.E. and Chen,Z.S.
  TITLE     Multifaceted investigation underlies diverse mechanisms
            contributing to the downregulation of Hedgehog pathway-associated
            genes INTU and IFT88 in lung adenocarcinoma and uterine corpus
            endometrial carcinoma
  JOURNAL   Aging (Albany NY) 14 (19), 7794-7823 (2022)
   PUBMED   36084949
  REMARK    GeneRIF: Multifaceted investigation underlies diverse mechanisms
            contributing to the downregulation of Hedgehog pathway-associated
            genes INTU and IFT88 in lung adenocarcinoma and uterine corpus
            endometrial carcinoma.
REFERENCE   5  (residues 1 to 799)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 799)
  AUTHORS   Khanna,H., Hurd,T.W., Lillo,C., Shu,X., Parapuram,S.K., He,S.,
            Akimoto,M., Wright,A.F., Margolis,B., Williams,D.S. and Swaroop,A.
  TITLE     RPGR-ORF15, which is mutated in retinitis pigmentosa, associates
            with SMC1, SMC3, and microtubule transport proteins
  JOURNAL   J Biol Chem 280 (39), 33580-33587 (2005)
   PUBMED   16043481
REFERENCE   7  (residues 1 to 799)
  AUTHORS   Lehner,B., Semple,J.I., Brown,S.E., Counsell,D., Campbell,R.D. and
            Sanderson,C.M.
  TITLE     Analysis of a high-throughput yeast two-hybrid system and its use
            to predict the function of intracellular proteins encoded within
            the human MHC class III region
  JOURNAL   Genomics 83 (1), 153-167 (2004)
   PUBMED   14667819
REFERENCE   8  (residues 1 to 799)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   9  (residues 1 to 799)
  AUTHORS   Murcia,N.S., Sweeney,W.E. Jr. and Avner,E.D.
  TITLE     New insights into the molecular pathophysiology of polycystic
            kidney disease
  JOURNAL   Kidney Int 55 (4), 1187-1197 (1999)
   PUBMED   10200981
  REMARK    Review article
REFERENCE   10 (residues 1 to 799)
  AUTHORS   Schrick,J.J., Onuchic,L.F., Reeders,S.T., Korenberg,J., Chen,X.N.,
            Moyer,J.H., Wilkinson,J.E. and Woychik,R.P.
  TITLE     Characterization of the human homologue of the mouse Tg737
            candidate polycystic kidney disease gene
  JOURNAL   Hum Mol Genet 4 (4), 559-567 (1995)
   PUBMED   7633404
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590096.16 and AL161772.17.
            
            On Jul 19, 2017 this sequence version replaced XP_016876249.1.
            
            Summary: This gene encodes a member of the tetratrico peptide
            repeat (TPR) family. The encoded protein is involved in cilium
            biogenesis. Mutations of a similar gene in mouse can cause
            polycystic kidney disease. Several transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2017].
            
            Transcript Variant: This variant (11), as well as variant 10,
            encodes isoform 5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803616.84260.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.11"
     Protein         1..799
                     /product="intraflagellar transport protein 88 homolog
                     isoform 5"
                     /note="polaris homolog; tetratricopeptide repeat domain
                     10; TPR repeat protein 10; recessive polycystic kidney
                     disease protein Tg737 homolog; probe hTg737 (polycystic
                     kidney disease, autosomal recessive); intraflagellar
                     transport protein 88 homolog; intraflagellar transport 88
                     homolog; tetratricopeptide repeat protein 10; testicular
                     tissue protein Li 93"
                     /calculated_mol_wt=90400
     Region          206..234
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(207,210..211,214..215,217,243,246..247,250..251,
                     253..254,282,285..286,289..290,293)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          210..552
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          241..271
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          281..307
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          394..417
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          427..453
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          434..688
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          459..487
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(460,463..464,467..468,470,494,497..498,501..502,
                     504..505,528,531..532,535..536,539)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          492..522
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          527..555
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          561..589
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          595..621
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          629..653
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          663..690
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..799
                     /gene="IFT88"
                     /gene_synonym="D13S1056E; DAF19; hTg737; TG737; TTC10"
                     /coded_by="NM_001353570.2:309..2708"
                     /note="isoform 5 is encoded by transcript variant 11"
                     /db_xref="GeneID:8100"
                     /db_xref="HGNC:HGNC:20606"
                     /db_xref="MIM:600595"
ORIGIN      
        1 mkftntkvqm mqnvhlapet deddlysgyn dynpiydiee lendaafqqa vrtshgrrpp
       61 itakisstav trpiatgygs ktslassigr pmtgaiqdgv trpmtavraa gftkaalrgs
      121 afdplsqsrg paspleakkk dspeekikql ekevnelvee scianscgdl klalekakda
      181 grkervlvrq reqvttpeni nldltysvlf nlasqysvne myaealntyq vivknkmfsn
      241 agilkmnmgn iylkqrnysk aikfyrmald qvpsvnkqmr ikimqnigvt fiqadrekmk
      301 kafqklitvp leidedkyis psddphtnlv teaikndhlr qmererkama ekyimtsakl
      361 iapvietsfa agydwcvevv kasqyvelan dleinkavty lrqkdynqav eilkvlekkd
      421 srvksaaatn lsalyymgkd faqassyadi avnsdrynpa altnkgntvf angdyekaae
      481 fykealrnds sctealynig ltyeklnrld ealdcflklh ailrnsaevl yqianiyelm
      541 enpsqaiewl mqvvsviptd pqvlsklgel ydregdksqa fqyyyesyry fpcnieview
      601 lgayyidtqf wekaiqyfer asliqptqvk wqlmvascfr rsgnyqkald tykdthrkfp
      661 enveclrflv rlctdlglkd aqeyarklkr lekmkeireq riksgrdgsg gsrgkregsa
      721 sgdsgqnysa sskgerlsar lralpgtnep yesssnkeid asyvdplgpq ierpktaakk
      781 rideddfade elgddllpe
//
LOCUS       NP_001164110             275 aa            linear   PRI 21-NOV-2025
DEFINITION  cyclin-dependent kinase 20 isoform 4 [Homo sapiens].
ACCESSION   NP_001164110
VERSION     NP_001164110.1
DBSOURCE    REFSEQ: accession NM_001170639.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Chivukula,S. and Malkhed,V.
  TITLE     The Role of CDK20 Protein in Carcinogenesis
  JOURNAL   Curr Drug Targets 24 (10), 790-796 (2023)
   PUBMED   37469151
  REMARK    GeneRIF: The Role of CDK20 Protein in Carcinogenesis.
            Review article
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Satoda,Y., Noguchi,T., Fujii,T., Taniguchi,A., Katoh,Y. and
            Nakayama,K.
  TITLE     BROMI/TBC1D32 together with CCRK/CDK20 and FAM149B1/JBTS36
            contributes to intraflagellar transport turnaround involving
            ICK/CILK1
  JOURNAL   Mol Biol Cell 33 (9), ar79 (2022)
   PUBMED   35609210
  REMARK    GeneRIF: BROMI/TBC1D32 together with CCRK/CDK20 and FAM149B1/JBTS36
            contributes to intraflagellar transport turnaround involving
            ICK/CILK1.
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Zhou,J., Liu,M., Sun,H., Feng,Y., Xu,L., Chan,A.W.H., Tong,J.H.,
            Wong,J., Chong,C.C.N., Lai,P.B.S., Wang,H.K., Tsang,S.W.,
            Goodwin,T., Liu,R., Huang,L., Chen,Z., Sung,J.J., Chow,K.L.,
            To,K.F. and Cheng,A.S.
  TITLE     Hepatoma-intrinsic CCRK inhibition diminishes myeloid-derived
            suppressor cell immunosuppression and enhances immune-checkpoint
            blockade efficacy
  JOURNAL   Gut 67 (5), 931-944 (2018)
   PUBMED   28939663
  REMARK    GeneRIF: Results delineate an immunosuppressive mechanism of the
            hepatoma-intrinsic CCRK signalling and highlight an overexpressed
            kinase target whose inhibition might empower hepatocellular
            carcinoma immunotherapy
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Wu,G.Q., Xie,D., Yang,G.F., Liao,Y.J., Mai,S.J., Deng,H.X., Sze,J.,
            Guan,X.Y., Zeng,Y.X., Lin,M.C. and Kung,H.F.
  TITLE     Cell cycle-related kinase supports ovarian carcinoma cell
            proliferation via regulation of cyclin D1 and is a predictor of
            outcome in patients with ovarian carcinoma
  JOURNAL   Int J Cancer 125 (11), 2631-2642 (2009)
   PUBMED   19672860
  REMARK    GeneRIF: Overexpression of CCRK is associated with ovarian
            carcinoma.
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Malumbres,M., Harlow,E., Hunt,T., Hunter,T., Lahti,J.M.,
            Manning,G., Morgan,D.O., Tsai,L.H. and Wolgemuth,D.J.
  TITLE     Cyclin-dependent kinases: a family portrait
  JOURNAL   Nat Cell Biol 11 (11), 1275-1276 (2009)
   PUBMED   19884882
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Qiu,H., Dai,H., Jain,K., Shah,R., Hong,C., Pain,J., Tian,B.,
            Vatner,D.E., Vatner,S.F. and Depre,C.
  TITLE     Characterization of a novel cardiac isoform of the cell
            cycle-related kinase that is regulated during heart failure
  JOURNAL   J Biol Chem 283 (32), 22157-22165 (2008)
   PUBMED   18508765
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Wohlbold,L., Larochelle,S., Liao,J.C., Livshits,G., Singer,J.,
            Shokat,K.M. and Fisher,R.P.
  TITLE     The cyclin-dependent kinase (CDK) family member PNQALRE/CCRK
            supports cell proliferation but has no intrinsic CDK-activating
            kinase (CAK) activity
  JOURNAL   Cell Cycle 5 (5), 546-554 (2006)
   PUBMED   16552187
  REMARK    GeneRIF: Depletion of PNQALRE by >80% due to RNA interference
            (RNAi) impairs cell proliferation, but fails to arrest the cell
            cycle at a discrete point.
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Liu,Y., Wu,C. and Galaktionov,K.
  TITLE     p42, a novel cyclin-dependent kinase-activating kinase in mammalian
            cells
  JOURNAL   J Biol Chem 279 (6), 4507-4514 (2004)
   PUBMED   14597612
  REMARK    GeneRIF: identification of p42, a novel cyclin-dependent
            kinase-activating kinase (CAK) activity in human cells; p42 is
            essential for the phosphorylation of Thr-160 and activation of CDK2
            and is indispensable for cell growth
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB992644.1, AK075325.1,
            AY904367.1, BC002655.2, AL353572.13, AI479563.1 and BM982394.1.
            
            Summary: The protein encoded by this gene contains a kinase domain
            most closely related to the cyclin-dependent protein kinases. The
            encoded kinase may activate cyclin-dependent kinase 2 and is
            involved in cell growth. Alternatively spliced transcript variants
            encoding distinct isoforms have been reported. [provided by RefSeq,
            Dec 2009].
            
            Transcript Variant: This variant (4) uses an alternate in-frame
            splice site in the 5' coding region, and an alternate splice site
            in the 3' coding region, which results in a frameshift compared to
            variant 1. This results in a shorter protein (isoform 4), compared
            to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC002655.2, KU178572.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.1"
     Protein         1..275
                     /product="cyclin-dependent kinase 20 isoform 4"
                     /EC_number="2.7.11.22"
                     /note="cell division protein kinase 20; CAK-kinase p42;
                     CDK-activating kinase p42; cyclin-kinase-activating kinase
                     p42; cyclin-dependent protein kinase H; cell cycle-related
                     kinase"
                     /calculated_mol_wt=30440
     Region          3..273
                     /region_name="STKc_CCRK"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Cell Cycle-Related Kinase; cd07832"
                     /db_xref="CDD:270826"
     Site            order(10..14,18,31,33,50,65,81..84,87,89..90,127,129,
                     131..132,134,145,148,161,163..166,185)
                     /site_type="active"
                     /db_xref="CDD:270826"
     Site            order(10..14,18,31,33,65,81..84,87,127,129,131..132,134,
                     145)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270826"
     Site            order(50,89,127,129,148,161,163..166,185)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270826"
     Site            order(144..155,160..167)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270826"
     CDS             1..275
                     /gene="CDK20"
                     /gene_synonym="CCRK; CDCH; P42; PNQALRE"
                     /coded_by="NM_001170639.2:88..915"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS65075.1"
                     /db_xref="GeneID:23552"
                     /db_xref="HGNC:HGNC:21420"
                     /db_xref="MIM:610076"
ORIGIN      
        1 mdqycilgri gegahgivfk akhvetgeiv alkkvalrrl edgfpnqalr eikalqemed
       61 nqyvvqlkav fphgggfvla fefmlsdlae vvrhaqrpla qaqvksylqm llkgvafcha
      121 nnivhrdlkp anllisasgq lkiadfglar vfspdgsrly thqvatrsvg cimgellngs
      181 plfpgkndie qlcyvlrilg tpnpqvwpel telpdynkis fkeqvpmple evlpdvspqa
      241 ldllgqflly pphqriaask lpclpihlsc rflsv
//
LOCUS       NP_001339316             514 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase 33 isoform a [Homo sapiens].
ACCESSION   NP_001339316 XP_011518594
VERSION     NP_001339316.1
DBSOURCE    REFSEQ: accession NM_001352387.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Yu,W., Li,Y., Chen,H., Cui,Y., Situ,C., Yao,L., Zhang,X., Lu,S.,
            Liu,L., Li,L., Ren,J., Guo,Y., Huo,Z., Chen,Y., Li,H., Jiang,T.,
            Gu,Y., Wang,C., Zhu,T., Li,Y., Hu,Z. and Guo,X.
  TITLE     STK33 Phosphorylates Fibrous Sheath Protein AKAP3/4 to Regulate
            Sperm Flagella Assembly in Spermiogenesis
  JOURNAL   Mol Cell Proteomics 22 (6), 100564 (2023)
   PUBMED   37146716
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Li,X., Lin,M., Liu,M., Ye,H. and Qin,S.
  TITLE     Interaction between STK33 and autophagy promoted renal cell
            carcinoma metastasis by regulating mTOR/ULK1 signaling pathway
  JOURNAL   Mol Biol Rep 50 (6), 5059-5067 (2023)
   PUBMED   37101009
  REMARK    GeneRIF: Interaction between STK33 and autophagy promoted renal
            cell carcinoma metastasis by regulating mTOR/ULK1 signaling
            pathway.
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Ma,H., Zhang,B., Khan,A., Zhao,D., Ma,A., Zhou,J., Khan,I.,
            Khan,K., Zhang,H., Zhang,Y., Jiang,X., Dil,S., Zeb,A., Rahim,F. and
            Shi,Q.
  TITLE     Novel frameshift mutation in STK33 is associated with
            asthenozoospermia and multiple morphological abnormalities of the
            flagella
  JOURNAL   Hum Mol Genet 30 (21), 1977-1984 (2021)
   PUBMED   34155512
  REMARK    GeneRIF: Novel frameshift mutation in STK33 is associated with
            asthenozoospermia and multiple morphological abnormalities of the
            flagella.
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Xie,Y., Lv,X., Ni,D., Liu,J., Hu,Y., Liu,Y., Liu,Y., Liu,R.,
            Zhao,H., Lu,Z. and Zhou,Q.
  TITLE     HPD degradation regulated by the TTC36-STK33-PELI1 signaling axis
            induces tyrosinemia and neurological damage
  JOURNAL   Nat Commun 10 (1), 4266 (2019)
   PUBMED   31537781
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Zhang,S., Wu,H., Wang,K. and Liu,M.
  TITLE     STK33/ERK2 signal pathway contribute the tumorigenesis of
            colorectal cancer HCT15 cells
  JOURNAL   Biosci Rep 39 (3) (2019)
   PUBMED   30760631
  REMARK    GeneRIF: Data show that serine/threonine kinase 33 (STK33) can bind
            with extracellular signal-regulated kinase 2 (ERK2) and take part
            in the regulation of ERKs signaling pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Melen,E., Himes,B.E., Brehm,J.M., Boutaoui,N., Klanderman,B.J.,
            Sylvia,J.S. and Lasky-Su,J.
  TITLE     Analyses of shared genetic factors between asthma and obesity in
            children
  JOURNAL   J Allergy Clin Immunol 126 (3), 631-7 (2010)
   PUBMED   20816195
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Willer,C.J., Speliotes,E.K., Loos,R.J., Li,S., Lindgren,C.M.,
            Heid,I.M., Berndt,S.I., Elliott,A.L., Jackson,A.U., Lamina,C.,
            Lettre,G., Lim,N., Lyon,H.N., McCarroll,S.A., Papadakis,K., Qi,L.,
            Randall,J.C., Roccasecca,R.M., Sanna,S., Scheet,P., Weedon,M.N.,
            Wheeler,E., Zhao,J.H., Jacobs,L.C., Prokopenko,I., Soranzo,N.,
            Tanaka,T., Timpson,N.J., Almgren,P., Bennett,A., Bergman,R.N.,
            Bingham,S.A., Bonnycastle,L.L., Brown,M., Burtt,N.P., Chines,P.,
            Coin,L., Collins,F.S., Connell,J.M., Cooper,C., Smith,G.D.,
            Dennison,E.M., Deodhar,P., Elliott,P., Erdos,M.R., Estrada,K.,
            Evans,D.M., Gianniny,L., Gieger,C., Gillson,C.J., Guiducci,C.,
            Hackett,R., Hadley,D., Hall,A.S., Havulinna,A.S., Hebebrand,J.,
            Hofman,A., Isomaa,B., Jacobs,K.B., Johnson,T., Jousilahti,P.,
            Jovanovic,Z., Khaw,K.T., Kraft,P., Kuokkanen,M., Kuusisto,J.,
            Laitinen,J., Lakatta,E.G., Luan,J., Luben,R.N., Mangino,M.,
            McArdle,W.L., Meitinger,T., Mulas,A., Munroe,P.B., Narisu,N.,
            Ness,A.R., Northstone,K., O'Rahilly,S., Purmann,C., Rees,M.G.,
            Ridderstrale,M., Ring,S.M., Rivadeneira,F., Ruokonen,A.,
            Sandhu,M.S., Saramies,J., Scott,L.J., Scuteri,A., Silander,K.,
            Sims,M.A., Song,K., Stephens,J., Stevens,S., Stringham,H.M.,
            Tung,Y.C., Valle,T.T., Van Duijn,C.M., Vimaleswaran,K.S.,
            Vollenweider,P., Waeber,G., Wallace,C., Watanabe,R.M.,
            Waterworth,D.M., Watkins,N., Witteman,J.C., Zeggini,E., Zhai,G.,
            Zillikens,M.C., Altshuler,D., Caulfield,M.J., Chanock,S.J.,
            Farooqi,I.S., Ferrucci,L., Guralnik,J.M., Hattersley,A.T., Hu,F.B.,
            Jarvelin,M.R., Laakso,M., Mooser,V., Ong,K.K., Ouwehand,W.H.,
            Salomaa,V., Samani,N.J., Spector,T.D., Tuomi,T., Tuomilehto,J.,
            Uda,M., Uitterlinden,A.G., Wareham,N.J., Deloukas,P.,
            Frayling,T.M., Groop,L.C., Hayes,R.B., Hunter,D.J., Mohlke,K.L.,
            Peltonen,L., Schlessinger,D., Strachan,D.P., Wichmann,H.E.,
            McCarthy,M.I., Boehnke,M., Barroso,I., Abecasis,G.R. and
            Hirschhorn,J.N.
  CONSRTM   Wellcome Trust Case Control Consortium; Genetic Investigation of
            ANthropometric Traits Consortium
  TITLE     Six new loci associated with body mass index highlight a neuronal
            influence on body weight regulation
  JOURNAL   Nat Genet 41 (1), 25-34 (2009)
   PUBMED   19079261
REFERENCE   8  (residues 1 to 514)
  AUTHORS   Mujica,A.O., Brauksiepe,B., Saaler-Reinhardt,S., Reuss,S. and
            Schmidt,E.R.
  TITLE     Differential expression pattern of the novel serine/threonine
            kinase, STK33, in mice and men
  JOURNAL   FEBS J 272 (19), 4884-4898 (2005)
   PUBMED   16176263
  REMARK    GeneRIF: STK33/Stk33 expression pattern resembles those of some
            related members of the calcium/calmodulin dependent kinase group
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Mujica,A.O., Hankeln,T. and Schmidt,E.R.
  TITLE     A novel serine/threonine kinase gene, STK33, on human chromosome
            11p15.3
  JOURNAL   Gene 280 (1-2), 175-181 (2001)
   PUBMED   11738831
REFERENCE   10 (residues 1 to 514)
  AUTHORS   Amid,C., Bahr,A., Mujica,A., Sampson,N., Bikar,S.E.,
            Winterpacht,A., Zabel,B., Hankeln,T. and Schmidt,E.R.
  TITLE     Comparative genomic sequencing reveals a strikingly similar
            architecture of a conserved syntenic region on human chromosome
            11p15.3 (including gene ST5) and mouse chromosome 7
  JOURNAL   Cytogenet Cell Genet 93 (3-4), 284-290 (2001)
   PUBMED   11528127
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104360.8 and AC105357.7.
            
            On Jun 13, 2017 this sequence version replaced XP_011518594.1.
            
            Transcript Variant: This variant (5), as well as variants 1, 4, and
            6-11, encodes isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1432242.1,
                                           SRR18074968.2643772.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..514
                     /product="serine/threonine-protein kinase 33 isoform a"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase 33"
                     /calculated_mol_wt=57700
     Region          65..91
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYT3.1)"
     Region          114..381
                     /region_name="STKc_STK33"
                     /note="Catalytic domain of Serine/Threonine Kinase 33;
                     cd14097"
                     /db_xref="CDD:270999"
     Site            order(122..126,130,143,145,176,192..195,199,201,237..238,
                     240,242..243,245,264..265,268,284..288,290)
                     /site_type="active"
                     /db_xref="CDD:270999"
     Site            order(122..125,130,143,145,176,192..195,199,242..243,245,
                     264..265)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270999"
     Site            order(126,199,201,237..238,240,242,268,284..288,290)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270999"
     Site            order(264..278,280..288)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270999"
     Region          402..468
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYT3.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q924X7; propagated from
                     UniProtKB/Swiss-Prot (Q9BYT3.1)"
     Region          485..514
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYT3.1)"
     CDS             1..514
                     /gene="STK33"
                     /gene_synonym="SPGF93"
                     /coded_by="NM_001352387.2:342..1886"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS7789.1"
                     /db_xref="GeneID:65975"
                     /db_xref="HGNC:HGNC:14568"
                     /db_xref="MIM:607670"
ORIGIN      
        1 madsgldkks tkcpdcssas qkdvlcvcss ktrvppvlvv emsqtssigs aeslislerk
       61 kekninrdit srkdlpsrts nverkasqqq wgrgnftegk vphirienga aieeiytfgr
      121 ilgkgsfgiv ieatdketet kwaikkvnke kagssavkll erevnilksv khehiihleq
      181 vfetpkkmyl vmelcedgel keildrkghf senetrwiiq slasaiaylh nndivhrdlk
      241 lenimvkssl iddnneinln ikvtdfglav kkqsrseaml qatcgtpiym apevisahdy
      301 sqqcdiwsig vvmymllrge ppflasseek lfelirkgel hfenavwnsi sdcaksvlkq
      361 lmkvdpahri takelldnqw ltgnklssvr ptnvlemmke wknnpesvee ntteeknkps
      421 teeklksyqp wgnvpdanyt sdeeeekqst ayekqfpats kdnfdmcsss ftsskllpae
      481 ikgemektpv tpsqgtatky paksgalsrt kkkl
//
LOCUS       NP_001382615            1828 aa            linear   PRI 21-NOV-2025
DEFINITION  endoribonuclease Dicer isoform 4 [Homo sapiens].
ACCESSION   NP_001382615
VERSION     NP_001382615.1
DBSOURCE    REFSEQ: accession NM_001395686.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1828)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1828)
  AUTHORS   Rojo-Pardillo,M., Godefroid,L., Dom,G., Lefort,A., Libert,F.,
            Robaye,B. and Maenhaut,C.
  TITLE     Understanding the Dosage-Dependent Role of Dicer1 in Thyroid
            Tumorigenesis
  JOURNAL   Int J Mol Sci 25 (19), 10701 (2024)
   PUBMED   39409030
  REMARK    GeneRIF: Understanding the Dosage-Dependent Role of Dicer1 in
            Thyroid Tumorigenesis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1828)
  AUTHORS   Mastnikova,K., Bulanova Pekova,B., Kuklikova,V., Vaclavikova,E.,
            Carkova,J., Katra,R., Fialova,L., Vlcek,P., Kodetova,D.,
            Chovanec,M., Drozenova,J., Matej,R., Pacesova,P., Novak,Z.,
            Procykova,K., Vcelak,J. and Bendlova,B.
  TITLE     DICER1 Variants in Pediatric and Young Adult Thyroid Nodules
  JOURNAL   Thyroid 34 (10), 1225-1233 (2024)
   PUBMED   39283830
  REMARK    GeneRIF: DICER1 Variants in Pediatric and Young Adult Thyroid
            Nodules.
REFERENCE   4  (residues 1 to 1828)
  AUTHORS   Dashti,N.K., Swanson,A.A., Bentz,J., Xing,D., Chrisinger,J.S.A.,
            Balzer,B., Guo,R., Schoolmeester,J.K. and Maluf,H.
  TITLE     DICER1-sarcomas of GYN tract: Expanding on an emerging entity
  JOURNAL   Hum Pathol 152, 105636 (2024)
   PUBMED   39127354
  REMARK    GeneRIF: DICER1-sarcomas of GYN tract: Expanding on an emerging
            entity.
REFERENCE   5  (residues 1 to 1828)
  AUTHORS   Irvin-Wilson,C.V. and Chaudhuri,G.
  TITLE     Alternative initiation and splicing in dicer gene expression in
            human breast cells
  JOURNAL   Breast Cancer Res 7 (4), R563-R569 (2005)
   PUBMED   15987463
REFERENCE   6  (residues 1 to 1828)
  AUTHORS   Bignell,G.R., Canzian,F., Shayeghi,M., Stark,M., Shugart,Y.Y.,
            Biggs,P., Mangion,J., Hamoudi,R., Rosenblatt,J., Buu,P., Sun,S.,
            Stoffer,S.S., Goldgar,D.E., Romeo,G., Houlston,R.S., Narod,S.A.,
            Stratton,M.R. and Foulkes,W.D.
  TITLE     Familial nontoxic multinodular thyroid goiter locus maps to
            chromosome 14q but does not account for familial nonmedullary
            thyroid cancer
  JOURNAL   Am J Hum Genet 61 (5), 1123-1130 (1997)
   PUBMED   9345104
REFERENCE   7  (residues 1 to 1828)
  AUTHORS   Schultz,K.A.P., Stewart,D.R., Kamihara,J., Bauer,A.J.,
            Merideth,M.A., Stratton,P., Huryn,L.A., Harris,A.K., Doros,L.,
            Field,A., Carr,A.G., Dehner,L.P., Messinger,Y. and Hill,D.A.
  TITLE     DICER1 Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24761742
REFERENCE   8  (residues 1 to 1828)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   9  (residues 1 to 1828)
  AUTHORS   Couch,R.M., Hughes,I.A., DeSa,D.J., Schiffrin,A., Guyda,H. and
            Winter,J.S.
  TITLE     An autosomal dominant form of adolescent multinodular goiter
  JOURNAL   Am J Hum Genet 39 (6), 811-816 (1986)
   PUBMED   3799599
REFERENCE   10 (residues 1 to 1828)
  AUTHORS   Murray,I.P., Thomson,J.A., McGirr,E.M., Macdonald,E.M.,
            Kennedy,J.S. and McLennan,I.
  TITLE     Unusual familial goiter associated with intrathyroidal
            calcification
  JOURNAL   J Clin Endocrinol Metab 26 (10), 1039-1049 (1966)
   PUBMED   4162574
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL356017.3 and AL390254.6.
            
            Summary: This gene encodes a protein possessing an RNA helicase
            motif containing a DEXH box in its amino terminus and an RNA motif
            in the carboxy terminus. The encoded protein functions as a
            ribonuclease and is required by the RNA interference and small
            temporal RNA (stRNA) pathways to produce the active small RNA
            component that represses gene expression. This protein also acts as
            a strong antiviral agent with activity against RNA viruses,
            including the Zika and SARS-CoV-2 viruses. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jul
            2021].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1828
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.13"
     Protein         1..1828
                     /product="endoribonuclease Dicer isoform 4"
                     /EC_number="3.1.26.3"
                     /note="dicer 1, double-stranded RNA-specific
                     endoribonuclease; helicase with RNAse motif;
                     endoribonuclease Dicer; helicase MOI; Dicer1, Dcr-1
                     homolog; dicer 1, ribonuclease type III"
                     /calculated_mol_wt=208224
     Region          <11..145
                     /region_name="DEXHc_dicer"
                     /note="DEXH-box helicase domain of endoribonuclease Dicer;
                     cd18034"
                     /db_xref="CDD:350792"
     Site            order(31..32,57,59..60,63,88..90)
                     /site_type="other"
                     /note="nucleic acid binding site [nucleotide binding]"
                     /db_xref="CDD:350792"
     Region          177..271
                     /region_name="Dicer_PBD"
                     /note="Partner-binding domain of the endoribonuclease
                     Dicer; cd15903"
                     /db_xref="CDD:277191"
     Site            order(182..183,186,188..189,248..249,252..253,256,
                     259..260,263)
                     /site_type="other"
                     /note="Trbp binding interface [polypeptide binding]"
                     /db_xref="CDD:277191"
     Region          278..470
                     /region_name="SF2_C_dicer"
                     /note="C-terminal helicase domain of the endoribonuclease
                     Dicer; cd18802"
                     /db_xref="CDD:350189"
     Site            order(355..357,427,446,448)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350189"
     Site            order(431,433,458,460)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350189"
     Region          536..624
                     /region_name="Dicer_dimer"
                     /note="Dicer dimerization domain; pfam03368"
                     /db_xref="CDD:460900"
     Region          792..914
                     /region_name="PAZ_dicer_like"
                     /note="PAZ domain, dicer_like subfamily. Dicer is an RNAse
                     involved in cleaving dsRNA in the RNA interference
                     pathway. It generates dsRNAs which are approximately 20 bp
                     long (siRNAs), which in turn target hydrolysis of
                     homologous RNAs. PAZ domains are named...; cd02843"
                     /db_xref="CDD:239209"
     Site            order(855,868,874,878,896,904,906)
                     /site_type="other"
                     /note="nucleic acid-binding interface [nucleotide
                     binding]"
                     /db_xref="CDD:239209"
     Region          1202..>1293
                     /region_name="RIBOc"
                     /note="Ribonuclease III family; smart00535"
                     /db_xref="CDD:197778"
     Site            order(1219..1220,1223..1224,1227,1230..1231,1234..1235,
                     1237..1239,1249)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238333"
     Region          1588..1752
                     /region_name="RIBOc"
                     /note="Ribonuclease III C terminal domain. This group
                     consists of eukaryotic, bacterial and archeal ribonuclease
                     III (RNAse III) proteins. RNAse III is a double stranded
                     RNA-specific endonuclease. Prokaryotic RNAse III is
                     important in post-transcriptional...; cd00593"
                     /db_xref="CDD:238333"
     Site            order(1608..1609,1612..1613,1616,1619..1620,1623..1624,
                     1626..1628,1638,1726,1737)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238333"
     Site            order(1608,1611,1615,1716,1719)
                     /site_type="active"
                     /db_xref="CDD:238333"
     Site            order(1611,1716,1719)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:238333"
     Region          1757..1819
                     /region_name="DSRM_DICER"
                     /note="double-stranded RNA binding motif of
                     endoribonuclease Dicer and similar proteins; cd10843"
                     /db_xref="CDD:380680"
     Site            order(1757..1758,1760..1761,1764..1765,1768..1769,1773,
                     1778..1780,1782,1784,1801..1804,1807)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380680"
     CDS             1..1828
                     /gene="DICER1"
                     /gene_synonym="aviD; DCR1; Dicer; Dicer1e; GLOW; HERNA;
                     K12H4.8-LIKE; MNG1; RMSE2"
                     /coded_by="NM_001395686.1:620..6106"
                     /note="isoform 4 is encoded by transcript variant 15"
                     /db_xref="GeneID:23405"
                     /db_xref="HGNC:HGNC:17098"
                     /db_xref="MIM:606241"
ORIGIN      
        1 mekgrcswst lvaqqvsavr thsdlkvgey snlevnaswt kerwnqeftk hqvlimtcyv
       61 alnvlkngyl slsdinllvf dechlaildh pyreimklce ncpscprilg ltasilngkc
      121 dpeeleekiq klekilksna etatdlvvld rytsqpceiv vdcgpftdrs glyerllmel
      181 eealnfindc nisvhskerd stliskqils dcravlvvlg pwcadkvagm mvrelqkyik
      241 heqeelhrkf llftdtflrk ihalceehfs pasldlkfvt pkviklleil rkykpyerqq
      301 fesvewynnr nqdnyvswsd sedddedeei eekekpetnf pspftnilcg iifverryta
      361 vvlnrlikea gkqdpelayi ssnfitghgi gknqprnkqm eaefrkqeev lrkfrahetn
      421 lliatsivee gvdipkcnlv vrfdlpteyr syvqskgrar apisnyimla dtdkiksfee
      481 dlktykaiek ilrnkcsksv dtgetdidpv mddddvfppy vlrpddggpr vtintaighi
      541 nrycarlpsd pfthlapkcr trelpdgtfy stlylpinsp lrasivgppm scvrlaervv
      601 alicceklhk igelddhlmp vgketvkyee eldlhdeeet svpgrpgstk rrqcypkaip
      661 eclrdsyprp dqpcylyvig mvlttplpde lnfrrrklyp pedttrcfgi ltakpipqip
      721 hfpvytrsge vtisielkks gfmlslqmle litrlhqyif shilrlekpa lefkptdads
      781 aycvlplnvv ndsstldidf kfmediekse arigipstky tketpfvfkl edyqdaviip
      841 ryrnfdqphr fyvadvytdl tplskfpspe yetfaeyykt kynldltnln qplldvdhts
      901 srlnlltprh lnqkgkalpl ssaekrkakw eslqnkqilv pelcaihpip aslwrkavcl
      961 psilyrlhcl ltaeelraqt asdagvgvrs lpadfrypnl dfgwkksids ksfisisnss
     1021 saendnyckh stivpenaah qganrtssle nhdqmsvncr tllsespgkl hvevsadlta
     1081 inglsynqnl angsydlanr dfcqgnqlny ykqeipvqpt tsysiqnlys yenqpqpsde
     1141 ctllsnkyld gnankstsdg spvmavmpgt tdtiqvlkgr mdseqspsig yssrtlgpnp
     1201 glilqaltls nasdgfnler lemlgdsflk haittylfct ypdahegrls ymrskkvsnc
     1261 nlyrlgkkkg lpsrmvvsif dppvnwlppg yvvnqdksnt dkwekdemtk dcmlangkld
     1321 edyeeedeee eslmwrapke eadyeddfle ydqehirfid nmlmgsgafv kkislspfst
     1381 tdsayewkmp kksslgsmpf ssdfedfdys swdamcyldp skaveeddfv vgfwnpseen
     1441 cgvdtgkqsi sydlhteqci adksiadcve allgcyltsc geraaqlflc slglkvlpvi
     1501 krtdrekalc ptrenfnsqq knlsvscaaa svassrssvl kdseygclki pprcmfdhpd
     1561 adktlnhlis gfenfekkin yrfknkayll qafthasyhy ntitdcyqrl eflgdaildy
     1621 litkhlyedp rqhspgvltd lrsalvnnti faslavkydy hkyfkavspe lfhviddfvq
     1681 fqleknemqg mdselrrsee deekeediev pkamgdifes lagaiymdsg msletvwqvy
     1741 ypmmrpliek fsanvprspv rellemepet akfspaerty dgkvrvtvev vgkgkfkgvg
     1801 rsyriaksaa arralrslka nqpqvpns
//
LOCUS       NP_001032583              89 aa            linear   PRI 21-NOV-2025
DEFINITION  dynein light chain 1, cytoplasmic [Homo sapiens].
ACCESSION   NP_001032583
VERSION     NP_001032583.1
DBSOURCE    REFSEQ: accession NM_001037494.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Greenwood,M., Gillard,B.T., Murphy,D. and Greenwood,M.P.
  TITLE     Dimerization of hub protein DYNLL1 and bZIP transcription factor
            CREB3L1 enhances transcriptional activation of CREB3L1 target genes
            like arginine vasopressin
  JOURNAL   Peptides 179, 171269 (2024)
   PUBMED   38960286
  REMARK    GeneRIF: Dimerization of hub protein DYNLL1 and bZIP transcription
            factor CREB3L1 enhances transcriptional activation of CREB3L1
            target genes like arginine vasopressin.
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Swift,M.L., Zhou,R., Syed,A., Moreau,L.A., Tomasik,B., Tainer,J.A.,
            Konstantinopoulos,P.A., D'Andrea,A.D., He,Y.J. and Chowdhury,D.
  TITLE     Dynamics of the DYNLL1-MRE11 complex regulate DNA end resection and
            recruitment of Shieldin to DSBs
  JOURNAL   Nat Struct Mol Biol 30 (10), 1456-1467 (2023)
   PUBMED   37696958
REFERENCE   4  (residues 1 to 89)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 89)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 89)
  AUTHORS   Crepieux,P., Kwon,H., Leclerc,N., Spencer,W., Richard,S., Lin,R.
            and Hiscott,J.
  TITLE     I kappaB alpha physically interacts with a cytoskeleton-associated
            protein through its signal response domain
  JOURNAL   Mol Cell Biol 17 (12), 7375-7385 (1997)
   PUBMED   9372968
REFERENCE   7  (residues 1 to 89)
  AUTHORS   Jaffrey,S.R. and Snyder,S.H.
  TITLE     PIN: an associated protein inhibitor of neuronal nitric oxide
            synthase
  JOURNAL   Science 274 (5288), 774-777 (1996)
   PUBMED   8864115
REFERENCE   8  (residues 1 to 89)
  AUTHORS   Dick,T., Ray,K., Salz,H.K. and Chia,W.
  TITLE     Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects
            and apoptotic cell death in Drosophila melanogaster
  JOURNAL   Mol Cell Biol 16 (5), 1966-1977 (1996)
   PUBMED   8628263
REFERENCE   9  (residues 1 to 89)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   10 (residues 1 to 89)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL021546.1, BG474448.1,
            CB992195.1, CD678447.1 and BI491360.1.
            
            Summary: Cytoplasmic dyneins are large enzyme complexes with a
            molecular mass of about 1,200 kD. They contain two force-producing
            heads formed primarily from dynein heavy chains, and stalks linking
            the heads to a basal domain, which contains a varying number of
            accessory intermediate chains. The complex is involved in
            intracellular transport and motility. The protein described in this
            record is a light chain and exists as part of this complex but also
            physically interacts with and inhibits the activity of neuronal
            nitric oxide synthase. Binding of this protein destabilizes the
            neuronal nitric oxide synthase dimer, a conformation necessary for
            activity, and it may regulate numerous biologic processes through
            its effects on nitric oxide synthase activity. Alternate
            transcriptional splice variants have been characterized. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. . Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.510238.1,
                                           DRR138512.19037.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..89
                     /product="dynein light chain 1, cytoplasmic"
                     /note="protein inhibitor of neuronal nitric oxide
                     synthase; dynein, cytoplasmic, light polypeptide 1; 8 kDa
                     dynein light chain; cytoplasmic dynein light polypeptide"
                     /calculated_mol_wt=10235
     Region          5..88
                     /region_name="DLC-like_DYNLL1_DYNLL2"
                     /note="dynein light chain (DLC)-like domain found in the
                     cytoplasmic dynein light chain 1 (DYNLL1) family; cd21452"
                     /db_xref="CDD:412000"
     Site            36
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P63167.1)"
     Region          67..89
                     /region_name="Interaction with ESR1.
                     /evidence=ECO:0000269|PubMed:15891768"
                     /note="propagated from UniProtKB/Swiss-Prot (P63167.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15193260,
                     ECO:0000269|PubMed:30464262, ECO:0000269|PubMed:37696958;
                     propagated from UniProtKB/Swiss-Prot (P63167.1)"
     CDS             1..89
                     /gene="DYNLL1"
                     /gene_synonym="DLC1; DLC8; DNCL1; DNCLC1; hdlc1; LC8;
                     LC8a; PIN"
                     /coded_by="NM_001037494.2:270..539"
                     /db_xref="CCDS:CCDS9200.1"
                     /db_xref="GeneID:8655"
                     /db_xref="HGNC:HGNC:15476"
                     /db_xref="MIM:601562"
ORIGIN      
        1 mcdrkavikn admseemqqd svecatqale kyniekdiaa hikkefdkky nptwhcivgr
       61 nfgsyvthet khfiyfylgq vaillfksg
//
LOCUS       NP_598194                350 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA repair protein RAD51 homolog 2 isoform 2 [Homo sapiens].
ACCESSION   NP_598194
VERSION     NP_598194.1
DBSOURCE    REFSEQ: accession NM_133510.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Slupianek,A., Jozwiakowski,S.K., Gurdek,E. and Skorski,T.
  TITLE     BCR/ABL kinase interacts with and phosphorylates the RAD51 paralog,
            RAD51B
  JOURNAL   Leukemia 23 (12), 2308-2310 (2009)
   PUBMED   19657362
  REMARK    GeneRIF: BCR/ABL fragments were used for identifying the sites of
            BCR/ABL interaction with RAD51B
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Thomas,G., Jacobs,K.B., Kraft,P., Yeager,M., Wacholder,S.,
            Cox,D.G., Hankinson,S.E., Hutchinson,A., Wang,Z., Yu,K.,
            Chatterjee,N., Garcia-Closas,M., Gonzalez-Bosquet,J.,
            Prokunina-Olsson,L., Orr,N., Willett,W.C., Colditz,G.A.,
            Ziegler,R.G., Berg,C.D., Buys,S.S., McCarty,C.A., Feigelson,H.S.,
            Calle,E.E., Thun,M.J., Diver,R., Prentice,R., Jackson,R.,
            Kooperberg,C., Chlebowski,R., Lissowska,J., Peplonska,B.,
            Brinton,L.A., Sigurdson,A., Doody,M., Bhatti,P., Alexander,B.H.,
            Buring,J., Lee,I.M., Vatten,L.J., Hveem,K., Kumle,M., Hayes,R.B.,
            Tucker,M., Gerhard,D.S., Fraumeni,J.F. Jr., Hoover,R.N.,
            Chanock,S.J. and Hunter,D.J.
  TITLE     A multistage genome-wide association study in breast cancer
            identifies two new risk alleles at 1p11.2 and 14q24.1 (RAD51L1)
  JOURNAL   Nat Genet 41 (5), 579-584 (2009)
   PUBMED   19330030
  REMARK    GeneRIF: A multistage genome-wide association study in breast
            cancer identifies two new risk alleles at 1p11.2 and 14q24.1
            (RAD51L1).
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Quade,B.J., Weremowicz,S., Neskey,D.M., Vanni,R., Ladd,C., Dal
            Cin,P. and Morton,C.C.
  TITLE     Fusion transcripts involving HMGA2 are not a common molecular
            mechanism in uterine leiomyomata with rearrangements in 12q15
  JOURNAL   Cancer Res 63 (6), 1351-1358 (2003)
   PUBMED   12649198
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Lio,Y.C., Mazin,A.V., Kowalczykowski,S.C. and Chen,D.J.
  TITLE     Complex formation by the human Rad51B and Rad51C DNA repair
            proteins and their activities in vitro
  JOURNAL   J Biol Chem 278 (4), 2469-2478 (2003)
   PUBMED   12427746
  REMARK    GeneRIF: Rad51B and Rad51C function through interactions with the
            human Rad51 recombinase and play a crucial role in the homologous
            recombinational repair pathway
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Masson,J.Y., Tarsounas,M.C., Stasiak,A.Z., Stasiak,A., Shah,R.,
            McIlwraith,M.J., Benson,F.E. and West,S.C.
  TITLE     Identification and purification of two distinct complexes
            containing the five RAD51 paralogs
  JOURNAL   Genes Dev 15 (24), 3296-3307 (2001)
   PUBMED   11751635
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Takata,M., Sasaki,M.S., Sonoda,E., Fukushima,T., Morrison,C.,
            Albala,J.S., Swagemakers,S.M., Kanaar,R., Thompson,L.H. and
            Takeda,S.
  TITLE     The Rad51 paralog Rad51B promotes homologous recombinational repair
  JOURNAL   Mol Cell Biol 20 (17), 6476-6482 (2000)
   PUBMED   10938124
REFERENCE   8  (residues 1 to 350)
  AUTHORS   Cartwright,R., Dunn,A.M., Simpson,P.J., Tambini,C.E. and Thacker,J.
  TITLE     Isolation of novel human and mouse genes of the recA/RAD51
            recombination-repair gene family
  JOURNAL   Nucleic Acids Res 26 (7), 1653-1659 (1998)
   PUBMED   9512535
REFERENCE   9  (residues 1 to 350)
  AUTHORS   Albala,J.S., Thelen,M.P., Prange,C., Fan,W., Christensen,M.,
            Thompson,L.H. and Lennon,G.G.
  TITLE     Identification of a novel human RAD51 homolog, RAD51B
  JOURNAL   Genomics 46 (3), 476-479 (1997)
   PUBMED   9441753
  REMARK    Erratum:[Genomics 1998 Aug 1;51(3):480]
REFERENCE   10 (residues 1 to 350)
  AUTHORS   Rice,M.C., Smith,S.T., Bullrich,F., Havre,P. and Kmiec,E.B.
  TITLE     Isolation of human and mouse genes based on homology to REC2, a
            recombinational repair gene from the fungus Ustilago maydis
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7417-7422 (1997)
   PUBMED   9207106
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL597484.1, BX161515.1 and
            Y15571.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the RAD51
            protein family. RAD51 family members are evolutionarily conserved
            proteins essential for DNA repair by homologous recombination. This
            protein has been shown to form a stable heterodimer with the family
            member RAD51C, which further interacts with the other family
            members, such as RAD51, XRCC2, and XRCC3. Overexpression of this
            gene was found to cause cell cycle G1 delay and cell apoptosis,
            which suggested a role of this protein in sensing DNA damage.
            Rearrangements between this locus and high mobility group AT-hook 2
            (HMGA2, GeneID 8091) have been observed in uterine leiomyomata.
            [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (2) has an alternate exon at the
            3' end compared to the longest variant (3). The resulting isoform
            (2) has a distinct and shorter C-terminus, as compared to isoform
            3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y15571.1, ERR279856.1869.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000471583.6/ ENSP00000418859.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.1"
     Protein         1..350
                     /product="DNA repair protein RAD51 homolog 2 isoform 2"
                     /note="RecA-like protein; recombination repair protein;
                     DNA repair protein RAD51 homolog 2; RAD51 homolog B"
                     /calculated_mol_wt=38173
     Region          1..75
                     /region_name="Interaction with RAD51C"
                     /note="propagated from UniProtKB/Swiss-Prot (O15315.2)"
     Region          91..327
                     /region_name="Rad51B"
                     /note="RAD51B recombinase; cd19493"
                     /db_xref="CDD:410901"
     Site            order(111..116,144,210,258,312)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:410901"
     Site            252..253
                     /site_type="other"
                     /note="Breakpoint for translocation to form HMGA2-RAD51B;
                     propagated from UniProtKB/Swiss-Prot (O15315.2)"
     CDS             1..350
                     /gene="RAD51B"
                     /gene_synonym="R51H2; RAD51L1; REC2"
                     /coded_by="NM_133510.4:78..1130"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9790.1"
                     /db_xref="GeneID:5890"
                     /db_xref="HGNC:HGNC:9822"
                     /db_xref="MIM:602948"
ORIGIN      
        1 mgskklkrvg lsqelcdrls rhqiltcqdf lclsplelmk vtglsyrgvh ellcmvsrac
       61 apkmqtaygi kaqrsadfsp aflsttlsal dealhggvac gslteitgpp gcgktqfcim
      121 msilatlptn mgglegavvy idtesafsae rlveiaesrf pryfnteekl lltsskvhly
      181 reltcdevlq riesleeeii skgiklvild svasvvrkef daqlqgnlke rnkflareas
      241 slkylaeefs ipviltnqit thlsgalasq adlvspaddl slsegtsgss cviaalgntw
      301 shsvntrlil qyldserrqi liaksplapf tsfvytikee glvlqgqekp
//
LOCUS       NP_001363702             543 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 32 [Homo sapiens].
ACCESSION   NP_001363702 XP_016864157
VERSION     NP_001363702.1
DBSOURCE    REFSEQ: accession NM_001376773.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Muckenfuss,L.M., Migenda Herranz,A.C., Boneberg,F.M., Clerici,M.
            and Jinek,M.
  TITLE     Fip1 is a multivalent interaction scaffold for processing factors
            in human mRNA 3' end biogenesis
  JOURNAL   Elife 11, e80332 (2022)
   PUBMED   36073787
  REMARK    GeneRIF: Fip1 is a multivalent interaction scaffold for processing
            factors in human mRNA 3' end biogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Tennenbaum,J., Groh,M., Venditti,L., Campos-Gazeau,F., Chalayer,E.,
            De Broucker,T., Hamidou,M., Hunault,M., Lyoubi,A., Meunier,R.,
            Muron,T., Sene,D., Slama,B., Guidoux,C., Lefevre,G., Kahn,J.E.,
            Denier,C. and Rohmer,J.
  TITLE     FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a Treatable
            Cause of Watershed Infarction
  JOURNAL   Stroke 52 (10), e605-e609 (2021)
   PUBMED   34304603
  REMARK    GeneRIF: FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a
            Treatable Cause of Watershed Infarction.
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 543)
  AUTHORS   Helbig,G., Lewandowski,K., Swiderska,A., Rodzaj,M., Seferynska,I.
            and Gajkowska-Kulik,J.
  TITLE     Exquisite response to imatinib mesylate in FIP1L1-PDGFRA-mutated
            hypereosinophilic syndrome: a 12-year experience of the Polish
            Hypereosinophilic Syndrome Study Group
  JOURNAL   Pol Arch Intern Med 130 (3), 255-257 (2020)
   PUBMED   32125294
  REMARK    GeneRIF: Exquisite response to imatinib mesylate in
            FIP1L1-PDGFRA-mutated hypereosinophilic syndrome: a 12-year
            experience of the Polish Hypereosinophilic Syndrome Study Group.
REFERENCE   6  (residues 1 to 543)
  AUTHORS   Cools,J., Quentmeier,H., Huntly,B.J., Marynen,P., Griffin,J.D.,
            Drexler,H.G. and Gilliland,D.G.
  TITLE     The EOL-1 cell line as an in vitro model for the study of
            FIP1L1-PDGFRA-positive chronic eosinophilic leukemia
  JOURNAL   Blood 103 (7), 2802-2805 (2004)
   PUBMED   14630792
  REMARK    GeneRIF: results indicate that the fusion of FIP1L1 to PDGFRA
            occurs rarely in leukemia cell lines
REFERENCE   7  (residues 1 to 543)
  AUTHORS   Kaufmann,I., Martin,G., Friedlein,A., Langen,H. and Keller,W.
  TITLE     Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements
            and stimulates poly(A) polymerase
  JOURNAL   EMBO J 23 (3), 616-626 (2004)
   PUBMED   14749727
REFERENCE   8  (residues 1 to 543)
  AUTHORS   Pardanani,A., Ketterling,R.P., Brockman,S.R., Flynn,H.C.,
            Paternoster,S.F., Shearer,B.M., Reeder,T.L., Li,C.Y., Cross,N.C.,
            Cools,J., Gilliland,D.G., Dewald,G.W. and Tefferi,A.
  TITLE     CHIC2 deletion, a surrogate for FIP1L1-PDGFRA fusion, occurs in
            systemic mastocytosis associated with eosinophilia and predicts
            response to imatinib mesylate therapy
  JOURNAL   Blood 102 (9), 3093-3096 (2003)
   PUBMED   12842979
  REMARK    GeneRIF: observations suggest that the FIP1L1-PDGFRA rearrangement
            occurs in an early hematopoietic progenitor and suggests that the
            molecular pathogenesis for a subset of SMCD patients is similar to
            that of HES
REFERENCE   9  (residues 1 to 543)
  AUTHORS   Griffin,J.H., Leung,J., Bruner,R.J., Caligiuri,M.A. and
            Briesewitz,R.
  TITLE     Discovery of a fusion kinase in EOL-1 cells and idiopathic
            hypereosinophilic syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (13), 7830-7835 (2003)
   PUBMED   12808148
REFERENCE   10 (residues 1 to 543)
  AUTHORS   Cools,J., DeAngelo,D.J., Gotlib,J., Stover,E.H., Legare,R.D.,
            Cortes,J., Kutok,J., Clark,J., Galinsky,I., Griffin,J.D.,
            Cross,N.C., Tefferi,A., Malone,J., Alam,R., Schrier,S.L.,
            Schmid,J., Rose,M., Vandenberghe,P., Verhoef,G., Boogaerts,M.,
            Wlodarska,I., Kantarjian,H., Marynen,P., Coutre,S.E., Stone,R. and
            Gilliland,D.G.
  TITLE     A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes
            as a therapeutic target of imatinib in idiopathic hypereosinophilic
            syndrome
  JOURNAL   N Engl J Med 348 (13), 1201-1214 (2003)
   PUBMED   12660384
  REMARK    GeneRIF: The hypereosinophilic syndrome may result from a novel
            fusion tyrosine kinase - FIP1L1-PDGFRalpha - that is a consequence
            of an interstitial chromosomal deletion.
            GeneRIF: Describes the fusion gene Fip1-like-1-PDGFRalpha in
            patients with idiopathic hypereosinophilic syndrome, mostly
            responsive to imatinib therapy.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098821.3 and AC058822.6.
            
            On Nov 20, 2019 this sequence version replaced XP_016864157.1.
            
            Summary: This gene encodes a subunit of the CPSF (cleavage and
            polyadenylation specificity factor) complex that polyadenylates the
            3' end of mRNA precursors. This gene, the homolog of yeast Fip1
            (factor interacting with PAP), binds to U-rich sequences of
            pre-mRNA and stimulates poly(A) polymerase activity. Its N-terminus
            contains a PAP-binding site and its C-terminus an RNA-binding
            domain. An interstitial chromosomal deletion on 4q12 creates an
            in-frame fusion of human genes FIP1L1 and PDGFRA (platelet-derived
            growth factor receptor, alpha). The FIP1L1-PDGFRA fusion gene
            encodes a constitutively activated tyrosine kinase that joins the
            first 233 amino acids of FIP1L1 to the last 523 amino acids of
            PDGFRA. This gene fusion and chromosomal deletion is the cause of
            some forms of idiopathic hypereosinophilic syndrome (HES). This
            syndrome, recently reclassified as chronic eosinophilic leukemia
            (CEL), is responsive to treatment with tyrosine kinase inhibitors.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1885766.1,
                                           SRR14038193.586600.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..543
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     32"
                     /note="rearranged in hypereosinophilia; pre-mRNA
                     3'-end-processing factor FIP1; FIP1-like 1 protein; factor
                     interacting with PAP; FIP1 like 1; FIP1L1 cleavage and
                     polyadenylation specific factor subunit"
                     /calculated_mol_wt=60798
     Region          139..181
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     CDS             1..543
                     /gene="FIP1L1"
                     /gene_synonym="FIP1; hFip1; Rhe"
                     /coded_by="NM_001376773.1:199..1830"
                     /note="isoform 32 is encoded by transcript variant 32"
                     /db_xref="CCDS:CCDS93517.1"
                     /db_xref="GeneID:81608"
                     /db_xref="HGNC:HGNC:19124"
                     /db_xref="MIM:607686"
ORIGIN      
        1 msageverlv selsggtggd eeeewlygde neverpeeen asanppsgie detaengvpk
       61 pkvtetedds dsdsdddedd vhvtigdikt gapqygsygt apvnlniktg grvygttgtk
      121 vkgvdldapg singvpllev dldsfedkpw rkpgadlsdy fnygfnedtw kaycekqkri
      181 rmglevipvt sttnkitaed ctmevtpgae iqdgrfnlfk vqqgrtgnse ketalpstka
      241 eftsppslfk tglppsrrlp gaidvigqti tisrvegrrr anensniqvl sersatevdn
      301 nfskpppffp pgappthlpp ppflpppptv stapplippp gfppppgapp psliptiesg
      361 hssgydsrsa rafpygnvaf phlpgsapsw pslvdtskqw dyyarrekdr drerdrdrer
      421 drdrdrerer trerererdh sptpsvfnsd eeryryreya ergyerhras rekeerhrer
      481 rhrekeetrh kssrsnsrrr heseegdshr rhkhkkskrs kegkeagsep apeqesteat
      541 pae
//
LOCUS       NP_957516                606 aa            linear   PRI 21-NOV-2025
DEFINITION  melanoma-associated antigen D2 [Homo sapiens].
ACCESSION   NP_957516
VERSION     NP_957516.1
DBSOURCE    REFSEQ: accession NM_201222.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Yan,X., Hu,Y., Zhang,X., Gao,X., Zhao,Y., Peng,H., Ouyang,L. and
            Zhang,C.
  TITLE     Identification of a novel intronic mutation of MAGED2 gene in a
            Chinese family with antenatal Bartter syndrome
  JOURNAL   BMC Med Genomics 17 (1), 23 (2024)
   PUBMED   38238844
  REMARK    GeneRIF: Identification of a novel intronic mutation of MAGED2 gene
            in a Chinese family with antenatal Bartter syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Shi,X., Liu,C., Zheng,W., Cao,X., Li,W., Zhang,D., Zhu,J., Zhang,X.
            and Chen,Y.
  TITLE     Proteomic Analysis Revealed the Potential Role of MAGE-D2 in the
            Therapeutic Targeting of Triple-Negative Breast Cancer
  JOURNAL   Mol Cell Proteomics 23 (1), 100703 (2024)
   PUBMED   38128647
  REMARK    GeneRIF: Proteomic Analysis Revealed the Potential Role of MAGE-D2
            in the Therapeutic Targeting of Triple-Negative Breast Cancer.
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Nasrah,S., Radi,A., Daberkow,J.K., Hummler,H., Weber,S.,
            Seaayfan,E. and Komhoff,M.
  TITLE     MAGED2 Depletion Promotes Stress-Induced Autophagy by Impairing the
            cAMP/PKA Pathway
  JOURNAL   Int J Mol Sci 24 (17), 13433 (2023)
   PUBMED   37686237
  REMARK    GeneRIF: MAGED2 Depletion Promotes Stress-Induced Autophagy by
            Impairing the cAMP/PKA Pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Seaayfan,E., Nasrah,S., Quell,L., Radi,A., Kleim,M.,
            Schermuly,R.T., Weber,S., Laghmani,K. and Komhoff,M.
  TITLE     Reciprocal Regulation of MAGED2 and HIF-1alpha Augments Their
            Expression under Hypoxia: Role of cAMP and PKA Type II
  JOURNAL   Cells 11 (21), 3424 (2022)
   PUBMED   36359819
  REMARK    GeneRIF: Reciprocal Regulation of MAGED2 and HIF-1alpha Augments
            Their Expression under Hypoxia: Role of cAMP and PKA Type II.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 606)
  AUTHORS   Harper,R., Xu,C., Di,P., Chen,Y., Privalsky,M. and Wu,R.
  TITLE     Identification of a novel MAGE D2 antisense RNA transcript in human
            tissues
  JOURNAL   Biochem Biophys Res Commun 324 (1), 199-204 (2004)
   PUBMED   15465002
  REMARK    GeneRIF: Results identified a cDNA clone, corresponding to MAGE D2
            mRNA, from primary human bronchial epithelial cells which exhibits
            increased expression in vitro after treatment with all-trans
            retinoic acid.
REFERENCE   7  (residues 1 to 606)
  AUTHORS   Bertrand,M., Huijbers,I., Chomez,P. and De Backer,O.
  TITLE     Comparative expression analysis of the MAGED genes during
            embryogenesis and brain development
  JOURNAL   Dev Dyn 230 (2), 325-334 (2004)
   PUBMED   15162511
  REMARK    GeneRIF: Maged2 is mainly expressed in tissues of mesodermal origin
REFERENCE   8  (residues 1 to 606)
  AUTHORS   Langnaese,K., Kloos,D.U., Wehnert,M., Seidel,B. and Wieacker,P.
  TITLE     Expression pattern and further characterization of human MAGED2 and
            identification of rodent orthologues
  JOURNAL   Cytogenet Cell Genet 94 (3-4), 233-240 (2001)
   PUBMED   11856887
  REMARK    GeneRIF: Expression pattern and further characterization of human
            MAGED2 and identification of rodent orthologues
REFERENCE   9  (residues 1 to 606)
  AUTHORS   Kurt,R.A., Urba,W.J. and Schoof,D.D.
  TITLE     Isolation of genes overexpressed in freshly isolated breast cancer
            specimens
  JOURNAL   Breast Cancer Res Treat 59 (1), 41-48 (2000)
   PUBMED   10752678
REFERENCE   10 (residues 1 to 606)
  AUTHORS   Lucas,S., Brasseur,F. and Boon,T.
  TITLE     A new MAGE gene with ubiquitous expression does not code for known
            MAGE antigens recognized by T cells
  JOURNAL   Cancer Res 59 (16), 4100-4103 (1999)
   PUBMED   10463614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM043994.1, BC000304.2 and
            BX647995.1.
            
            Summary: This gene is a member of the MAGED gene family. The MAGED
            genes are clustered on chromosome Xp11. This gene is located in
            Xp11.2, a hot spot for X-linked intellectual disability (XLID).
            Mutations in this gene cause a form of transient antenatal
            Bartter's syndrome. This gene may also be involved in several types
            of cancer, including breast cancer and melanoma. The protein
            encoded by this gene is progressively recruited from the cytoplasm
            to the nucleoplasm during the interphase and after nucleolar stress
            and is thus thought to play a role in cell cycle regulation.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jul 2017].
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 2. Variants 1, 2, and 3 encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.903912.1, BX647995.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.21"
     Protein         1..606
                     /product="melanoma-associated antigen D2"
                     /note="MAGE-D2 antigen; breast cancer-associated gene 1
                     protein; hepatocellular carcinoma-associated protein
                     JCL-1; melanoma antigen family D, 2; melanoma antigen
                     family D2"
                     /calculated_mol_wt=64823
     Region          1..204
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Region          <11..161
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648;
                     propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Region          248..275
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Region          286..454
                     /region_name="MAGE"
                     /note="MAGE homology domain; pfam01454"
                     /db_xref="CDD:426270"
     Region          534..563
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     CDS             1..606
                     /gene="MAGED2"
                     /gene_synonym="11B6; BARTS5; BCG-1; BCG1; HCA10; MAGE-D2"
                     /coded_by="NM_201222.3:173..1993"
                     /db_xref="CCDS:CCDS14362.1"
                     /db_xref="GeneID:10916"
                     /db_xref="HGNC:HGNC:16353"
                     /db_xref="MIM:300470"
ORIGIN      
        1 msdtsesgag ltrfqaease kdsssmmqtl ltvtqnvevp etpkaskale vsedvkvska
       61 sgvskatevs ktpeareapa tqassttqlt dtqvlaaenk slaadtkkqn adpqavtmpa
      121 tetkkvshva dtkvntkaqe teaapsqapa depepesaaa qsqenqdtrp kvkakkarkv
      181 khldgeedgs sdqsqasgtt ggrrvskalm asmarrasrg piafwarras rtrlaawarr
      241 allslrspka rrgkarrraa klqssqepea ppprdvallq grandlvkyl lakdqtkipi
      301 krsdmlkdii keytdvypei ieragyslek vfgiqlkeid kndhlyills tleptdagil
      361 gttkdspklg llmvllsiif mngnrsseav iwevlrklgl rpgihhslfg dvkklitdef
      421 vkqkyldyar vpnsnppeye ffwglrsyye tskmkvlkfa ckvqkkdpke waaqyreame
      481 adlkaaaeaa aeakaraeir armgiglgse naagpcnwde adigpwakar iqagaeakak
      541 aqesgsastg aststnnsas asastsggfs agasltatlt fglfaglgga gastsgssga
      601 cgfsyk
//
LOCUS       NP_001036215            1268 aa            linear   PRI 21-NOV-2025
DEFINITION  cohesin subunit SA-2 isoform a [Homo sapiens].
ACCESSION   NP_001036215
VERSION     NP_001036215.1
DBSOURCE    REFSEQ: accession NM_001042750.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1268)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1268)
  AUTHORS   Fischer,A., Hernandez-Rodriguez,B., Mulet-Lazaro,R., Nuetzel,M.,
            Holzl,F., van Herk,S., Kavelaars,F.G., Stanewsky,H., Ackermann,U.,
            Niang,A.H., Diaz,N., Reuschel,E., Strieder,N., Hernandez-Lopez,I.,
            Valk,P.J.M., Vaquerizas,J.M., Rehli,M., Delwel,R. and Gebhard,C.
  TITLE     STAG2 mutations reshape the cohesin-structured spatial chromatin
            architecture to drive gene regulation in acute myeloid leukemia
  JOURNAL   Cell Rep 43 (8), 114498 (2024)
   PUBMED   39084219
  REMARK    GeneRIF: STAG2 mutations reshape the cohesin-structured spatial
            chromatin architecture to drive gene regulation in acute myeloid
            leukemia.
REFERENCE   3  (residues 1 to 1268)
  AUTHORS   Huber,J., Tanasie,N.L., Zernia,S. and Stigler,J.
  TITLE     Single-molecule imaging reveals a direct role of CTCF's zinc
            fingers in SA interaction and cluster-dependent RNA recruitment
  JOURNAL   Nucleic Acids Res 52 (11), 6490-6506 (2024)
   PUBMED   38742641
  REMARK    GeneRIF: Single-molecule imaging reveals a direct role of CTCF's
            zinc fingers in SA interaction and cluster-dependent RNA
            recruitment.
REFERENCE   4  (residues 1 to 1268)
  AUTHORS   Xu,W., Kim,J.S., Yang,T., Ya,A., Sadzewicz,L., Tallon,L.,
            Harris,B.T., Sarkaria,J., Jin,F. and Waldman,T.
  TITLE     STAG2 mutations regulate 3D genome organization, chromatin loops,
            and Polycomb signaling in glioblastoma multiforme
  JOURNAL   J Biol Chem 300 (6), 107341 (2024)
   PUBMED   38705393
  REMARK    GeneRIF: STAG2 mutations regulate 3D genome organization, chromatin
            loops, and Polycomb signaling in glioblastoma multiforme.
REFERENCE   5  (residues 1 to 1268)
  AUTHORS   Ros-Pardo,D., Gomez-Puertas,P. and Marcos-Alcalde,I.
  TITLE     STAG2: Computational Analysis of Missense Variants Involved in
            Disease
  JOURNAL   Int J Mol Sci 25 (2), 1280 (2024)
   PUBMED   38279279
  REMARK    GeneRIF: STAG2: Computational Analysis of Missense Variants
            Involved in Disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1268)
  AUTHORS   Gregson,H.C., Schmiesing,J.A., Kim,J.S., Kobayashi,T., Zhou,S. and
            Yokomori,K.
  TITLE     A potential role for human cohesin in mitotic spindle aster
            assembly
  JOURNAL   J Biol Chem 276 (50), 47575-47582 (2001)
   PUBMED   11590136
REFERENCE   7  (residues 1 to 1268)
  AUTHORS   Sumara,I., Vorlaufer,E., Gieffers,C., Peters,B.H. and Peters,J.M.
  TITLE     Characterization of vertebrate cohesin complexes and their
            regulation in prophase
  JOURNAL   J Cell Biol 151 (4), 749-762 (2000)
   PUBMED   11076961
REFERENCE   8  (residues 1 to 1268)
  AUTHORS   Carramolino,L., Lee,B.C., Zaballos,A., Peled,A., Barthelemy,I.,
            Shav-Tal,Y., Prieto,I., Carmi,P., Gothelf,Y., Gonzalez de
            Buitrago,G., Aracil,M., Marquez,G., Barbero,J.L. and Zipori,D.
  TITLE     SA-1, a nuclear protein encoded by one member of a novel gene
            family: molecular cloning and detection in hemopoietic organs
  JOURNAL   Gene 195 (2), 151-159 (1997)
   PUBMED   9305759
  REMARK    Erratum:[Gene 1998 Jan 12;206(2):283]
REFERENCE   9  (residues 1 to 1268)
  AUTHORS   Wu,C., Friedlander,P., Lamoureux,C., Zannis-Hadjopoulos,M. and
            Price,G.B.
  TITLE     cDNA clones contain autonomous replication activity
  JOURNAL   Biochim Biophys Acta 1174 (3), 241-257 (1993)
   PUBMED   7690594
REFERENCE   10 (residues 1 to 1268)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA214149.1, CR749433.1,
            BC001765.1, CB250478.1, BC017095.1 and AA428995.1.
            
            Summary: The protein encoded by this gene is a subunit of the
            cohesin complex, which regulates the separation of sister
            chromatids during cell division. Targeted inactivation of this gene
            results in chromatid cohesion defects and aneuploidy, suggesting
            that genetic disruption of cohesin is a cause of aneuploidy in
            human cancer. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2013].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749433.1, SRR14038194.1284828.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371145.8/ ENSP00000360187.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1268
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..1268
                     /product="cohesin subunit SA-2 isoform a"
                     /note="SCC3 homolog 2; cohesin subunit SA-2; SA2
                     stromalin; sister chromatid cohesion 3 homolog B; stromal
                     antigen 2"
                     /calculated_mol_wt=145621
     Region          102..>395
                     /region_name="IRR1"
                     /note="Cohesin [Cell division and chromosome
                     partitioning]; COG5537"
                     /db_xref="CDD:227824"
     Region          157..270
                     /region_name="STAG"
                     /note="STAG domain; pfam08514"
                     /db_xref="CDD:462502"
     CDS             1..1268
                     /gene="STAG2"
                     /gene_synonym="bA517O1.1; HPE13; MKMS; NEDXCF; SA-2; SA2;
                     SCC3B"
                     /coded_by="NM_001042750.2:314..4120"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43990.1"
                     /db_xref="GeneID:10735"
                     /db_xref="HGNC:HGNC:11355"
                     /db_xref="MIM:300826"
ORIGIN      
        1 miaapeiptd fnllqeseth fssdtdfedi egknqkqgkg ktckkgkkgp aekgkggngg
       61 gkppsgpnrm nghhqqngve nmmlfevvkm gksamqsvvd dwiesykhdr dialldlinf
      121 fiqcsgckgv vtaemfrhmq nseiirkmte efdedsgdyp ltmagpqwkk fkssfcefig
      181 vlvrqcqysi iydeymmdtv islltglsds qvrafrhtst laamklmtal vnvalnlsin
      241 mdntqrqyea ernkmigkra nerlelllqk rkelqenqde ienmmnaifk gvfvhryrda
      301 iaeiraicie eigiwmkmys daflndsylk yvgwtmhdkq gevrlkclta lqglyynkel
      361 nsklelftsr fkdrivsmtl dkeydvavqa iklltlvlqs seevltaedc envyhlvysa
      421 hrpvavaage flykklfsrr dpeedgmmkr rgrqgpnanl vktlvfffle selhehaayl
      481 vdsmwdcate llkdwecmns llleeplsge ealtdrqesa lieimlctir qaaechppvg
      541 rgtgkrvlta kekktqlddr tkitelfava lpqllakysv daekvtnllq lpqyfdleiy
      601 ttgrlekhld allrqirniv ekhtdtdvle acsktyhalc neeftifnrv disrsqlide
      661 ladkfnrlle dflqegeepd eddayqvlst lkritafhna hdlskwdlfa cnykllktgi
      721 engdmpeqiv ihalqcthyv ilwqlakite ssstkedllr lkkqmrvfcq icqhyltnvn
      781 ttvkeqafti lcdilmifsh qimsggrdml eplvytpdss lqsellsfil dhvfieqddd
      841 nnsadgqqed easkiealhk rrnllaafck livytvvemn taadifkqym kyyndygdii
      901 ketmsktrqi dkiqcaktli lslqqlfnem iqengynfdr ssstfsgike larrfaltfg
      961 ldqlktreai amlhkdgief afkepnpqge shpplnlafl dilsefsskl lrqdkrtvyv
     1021 ylekfmtfqm slrredvwlp lmsyrnslla ggdddtmsvi sgissrgstv rskkskpstg
     1081 krkvvegmql slteessssd smwlsreqtl htpvmmqtpq ltstimrepk rlrpedsfms
     1141 vypmqtehhq tpldyntqvt wmlaqrqqee arqqqeraam syvklrtnlq hairrgtslm
     1201 eddeepived vmmssegrie dlnegmdfdt mdidlppskn rrertelkpd ffdpasimde
     1261 svlgvsmf
//
LOCUS       NP_001131136             503 aa            linear   PRI 21-NOV-2025
DEFINITION  anaphase-promoting complex subunit 7 isoform b [Homo sapiens].
ACCESSION   NP_001131136
VERSION     NP_001131136.2
DBSOURCE    REFSEQ: accession NM_001137664.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Ferguson,C.J., Urso,O., Bodrug,T., Gassaway,B.M., Watson,E.R.,
            Prabu,J.R., Lara-Gonzalez,P., Martinez-Chacin,R.C., Wu,D.Y.,
            Brigatti,K.W., Puffenberger,E.G., Taylor,C.M., Haas-Givler,B.,
            Jinks,R.N., Strauss,K.A., Desai,A., Gabel,H.W., Gygi,S.P.,
            Schulman,B.A., Brown,N.G. and Bonni,A.
  TITLE     APC7 mediates ubiquitin signaling in constitutive heterochromatin
            in the developing mammalian brain
  JOURNAL   Mol Cell 82 (1), 90-105 (2022)
   PUBMED   34942119
  REMARK    GeneRIF: APC7 mediates ubiquitin signaling in constitutive
            heterochromatin in the developing mammalian brain.
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Wild,T., Budzowska,M., Hellmuth,S., Eibes,S., Karemore,G.,
            Barisic,M., Stemmann,O. and Choudhary,C.
  TITLE     Deletion of APC7 or APC16 Allows Proliferation of Human Cells
            without the Spindle Assembly Checkpoint
  JOURNAL   Cell Rep 25 (9), 2317-2328 (2018)
   PUBMED   30485802
  REMARK    GeneRIF: the contribution of the anaphase-promoting
            complex/cyclosome subunits APC7 and APC16 to APC/C composition and
            function in human cells.
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Yau,R.G., Doerner,K., Castellanos,E.R., Haakonsen,D.L., Werner,A.,
            Wang,N., Yang,X.W., Martinez-Martin,N., Matsumoto,M.L., Dixit,V.M.
            and Rape,M.
  TITLE     Assembly and Function of Heterotypic Ubiquitin Chains in Cell-Cycle
            and Protein Quality Control
  JOURNAL   Cell 171 (4), 918-933 (2017)
   PUBMED   29033132
REFERENCE   5  (residues 1 to 503)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 503)
  AUTHORS   Sudakin,V., Chan,G.K. and Yen,T.J.
  TITLE     Checkpoint inhibition of the APC/C in HeLa cells is mediated by a
            complex of BUBR1, BUB3, CDC20, and MAD2
  JOURNAL   J Cell Biol 154 (5), 925-936 (2001)
   PUBMED   11535616
REFERENCE   7  (residues 1 to 503)
  AUTHORS   Gieffers,C., Peters,B.H., Kramer,E.R., Dotti,C.G. and Peters,J.M.
  TITLE     Expression of the CDH1-associated form of the anaphase-promoting
            complex in postmitotic neurons
  JOURNAL   Proc Natl Acad Sci U S A 96 (20), 11317-11322 (1999)
   PUBMED   10500174
REFERENCE   8  (residues 1 to 503)
  AUTHORS   Chan,G.K., Jablonski,S.A., Sudakin,V., Hittle,J.C. and Yen,T.J.
  TITLE     Human BUBR1 is a mitotic checkpoint kinase that monitors CENP-E
            functions at kinetochores and binds the cyclosome/APC
  JOURNAL   J Cell Biol 146 (5), 941-954 (1999)
   PUBMED   10477750
REFERENCE   9  (residues 1 to 503)
  AUTHORS   Grossberger,R., Gieffers,C., Zachariae,W., Podtelejnikov,A.V.,
            Schleiffer,A., Nasmyth,K., Mann,M. and Peters,J.M.
  TITLE     Characterization of the DOC1/APC10 subunit of the yeast and the
            human anaphase-promoting complex
  JOURNAL   J Biol Chem 274 (20), 14500-14507 (1999)
   PUBMED   10318877
REFERENCE   10 (residues 1 to 503)
  AUTHORS   Yu,H., Peters,J.M., King,R.W., Page,A.M., Hieter,P. and
            Kirschner,M.W.
  TITLE     Identification of a cullin homology region in a subunit of the
            anaphase-promoting complex
  JOURNAL   Science 279 (5354), 1219-1222 (1998)
   PUBMED   9469815
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC144548.8.
            
            On Dec 15, 2020 this sequence version replaced NP_001131136.1.
            
            Summary: This gene encodes a tetratricopeptide repeat containing
            component of the anaphase promoting complex/cyclosome (APC/C), a
            large E3 ubiquitin ligase that controls cell cycle progression by
            targeting a number of cell cycle regulators such as B-type cyclins
            for 26S proteasome-mediated degradation through ubiquitination. The
            encoded protein is required for proper protein ubiquitination
            function of APC/C and for the interaction of APC/C with certain
            transcription coactivators. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2008].
            
            Transcript Variant: This variant (2) differs in the 3' UTR and 3'
            coding region (compared to variant 1), which results in a
            frameshift. It encodes isoform b which has a shorter and distinct
            C-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC040130.1, AK021809.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..503
                     /product="anaphase-promoting complex subunit 7 isoform b"
                     /note="cyclosome subunit 7"
                     /calculated_mol_wt=56149
     Region          <99..392
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          101..134
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJX3.5)"
     Region          169..202
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJX3.5)"
     Region          203..236
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJX3.5)"
     Site            229
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVM3; propagated from
                     UniProtKB/Swiss-Prot (Q9UJX3.5)"
     Region          237..270
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJX3.5)"
     Region          305..>503
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(313..314,316,340,343..344,347..348,350..351,374,
                     377..378,381..382,385)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          338..368
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          339..372
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJX3.5)"
     Region          373..406
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJX3.5)"
     Region          407..441
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJX3.5)"
     Region          442..474
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJX3.5)"
     Region          442..470
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          475..503
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..503
                     /gene="ANAPC7"
                     /gene_synonym="APC7; FERBON"
                     /coded_by="NM_001137664.2:82..1593"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44971.2"
                     /db_xref="GeneID:51434"
                     /db_xref="HGNC:HGNC:17380"
                     /db_xref="MIM:606949"
ORIGIN      
        1 mnvidhvrdm aaaglhsnvr llssllltms nnnpelfspp qkyqllvyha dslfhdkeyr
       61 navskytmal qqkkalskts kvrpstgnsa stpqsqclps eievkykmae cytmlkqdkd
      121 aiaildgips rqrtpkinmm lanlykkagq erpsvtsyke vlrqcplald ailgllslsv
      181 kgaevasmtm nviqtvpnld wlsvwikaya fvhtgdnsra isticslekk sllrdnvdll
      241 gsladlyfra gdnknsvlkf eqaqmldpyl ikgmdvygyl laregrledv enlgcrlfni
      301 sdqhaepwvv sgchsfyskr ysralylgak aiqlnsnsvq alllkgaalr nmgrvqeaii
      361 hfreairlap crldcyegli ecylasnsir eamvmannvy ktlganaqtl tllatvcled
      421 pvtqekaktl ldkaltqrpd yikavvkkae llsreqkyed giallrnala nqsdcvlhri
      481 lgdflvavne yqeamdqysi alr
//
LOCUS       NP_001317946             245 aa            linear   PRI 21-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4E isoform 4 [Homo
            sapiens].
ACCESSION   NP_001317946 XP_006714189
VERSION     NP_001317946.1
DBSOURCE    REFSEQ: accession NM_001331017.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Nicholson-Shaw,T., Dowdle,M.E., Ajaj,Y., Perelis,M., Fulzele,A.,
            Yeo,G.W., Bennett,E.J. and Lykke-Andersen,J.
  TITLE     Human CCR4 deadenylase homolog Angel1 is a non-stop mRNA decay
            factor
  JOURNAL   RNA 31 (8), 1195-1205 (2025)
   PUBMED   40441874
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Yang,G., Smibert,C.A., Kaplan,D.R. and Miller,F.D.
  TITLE     An eIF4E1/4E-T complex determines the genesis of neurons from
            precursors by translationally repressing a proneurogenic
            transcription program
  JOURNAL   Neuron 84 (4), 723-739 (2014)
   PUBMED   25456498
  REMARK    GeneRIF: neural precursors are transcriptionally primed to generate
            neurons, but an eIF4E/4E-T complex sequesters and represses
            translation of proneurogenic proteins to determine appropriate
            neurogenesis.
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Feoktistova,K., Tuvshintogs,E., Do,A. and Fraser,C.S.
  TITLE     Human eIF4E promotes mRNA restructuring by stimulating eIF4A
            helicase activity
  JOURNAL   Proc Natl Acad Sci U S A 110 (33), 13339-13344 (2013)
   PUBMED   23901100
  REMARK    GeneRIF: Human eIF4E promotes mRNA restructuring by stimulating
            eIF4A helicase activity.
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Xu,X., Vatsyayan,J., Gao,C., Bakkenist,C.J. and Hu,J.
  TITLE     Sumoylation of eIF4E activates mRNA translation
  JOURNAL   EMBO Rep 11 (4), 299-304 (2010)
   PUBMED   20224576
  REMARK    GeneRIF: The findings suggest further that eIF4E sumoylation is a
            new fundamental regulatory mechanism of protein synthesis and might
            be important in promoting human cancers.
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Brown,C.J., McNae,I., Fischer,P.M. and Walkinshaw,M.D.
  TITLE     Crystallographic and mass spectrometric characterisation of eIF4E
            with N7-alkylated cap derivatives
  JOURNAL   J Mol Biol 372 (1), 7-15 (2007)
   PUBMED   17631896
  REMARK    GeneRIF: Crystallographic and mass spectrometric characterisation
            of eIF4E with N7-alkylated cap derivatives.
            Review article
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Tomoo,K., Shen,X., Okabe,K., Nozoe,Y., Fukuhara,S., Morino,S.,
            Ishida,T., Taniguchi,T., Hasegawa,H., Terashima,A., Sasaki,M.,
            Katsuya,Y., Kitamura,K., Miyoshi,H., Ishikawa,M. and Miura,K.
  TITLE     Crystal structures of 7-methylguanosine 5'-triphosphate (m(7)GTP)-
            and P(1)-7-methylguanosine-P(3)-adenosine-5',5'-triphosphate
            (m(7)GpppA)-bound human full-length eukaryotic initiation factor
            4E: biological importance of the C-terminal flexible region
  JOURNAL   Biochem J 362 (Pt 3), 539-544 (2002)
   PUBMED   11879179
  REMARK    GeneRIF: The crystal structures of the full-length human eukaryotic
            initiation factor (eIF) 4E complexed with two mRNA cap analogues
REFERENCE   8  (residues 1 to 245)
  AUTHORS   Lejbkowicz,F., Goyer,C., Darveau,A., Neron,S., Lemieux,R. and
            Sonenberg,N.
  TITLE     A fraction of the mRNA 5' cap-binding protein, eukaryotic
            initiation factor 4E, localizes to the nucleus
  JOURNAL   Proc Natl Acad Sci U S A 89 (20), 9612-9616 (1992)
   PUBMED   1384058
REFERENCE   9  (residues 1 to 245)
  AUTHORS   Ueda,H., Iyo,H., Doi,M., Inoue,M., Ishida,T., Morioka,H.,
            Tanaka,T., Nishikawa,S. and Uesugi,S.
  TITLE     Combination of Trp and Glu residues for recognition of mRNA cap
            structure. Analysis of m7G base recognition site of human cap
            binding protein (IF-4E) by site-directed mutagenesis
  JOURNAL   FEBS Lett 280 (2), 207-210 (1991)
   PUBMED   1672854
REFERENCE   10 (residues 1 to 245)
  AUTHORS   Rychlik,W., Domier,L.L., Gardner,P.R., Hellmann,G.M. and
            Rhoads,R.E.
  TITLE     Amino acid sequence of the mRNA cap-binding protein from human
            tissues
  JOURNAL   Proc Natl Acad Sci U S A 84 (4), 945-949 (1987)
   PUBMED   3469651
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1992 Feb 1;89(3):1148. doi:
            10.1073/pnas.89.3.1148a. PMID: 1736299]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC035166.1, BY994926.1,
            M15353.1 and AC093836.3.
            
            On Sep 3, 2016 this sequence version replaced XP_006714189.1.
            
            Summary: The protein encoded by this gene is a component of the
            eukaryotic translation initiation factor 4F complex, which
            recognizes the 7-methylguanosine cap structure at the 5' end of
            messenger RNAs. The encoded protein aids in translation initiation
            by recruiting ribosomes to the 5'-cap structure. Association of
            this protein with the 4F complex is the rate-limiting step in
            translation initiation. This gene acts as a proto-oncogene, and its
            expression and activation is associated with transformation and
            tumorigenesis. Several pseudogenes of this gene are found on other
            chromosomes. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (4) differs in its 5' UTR and
            contains an alternate exon in its 5' coding region compared to
            variant 1. This variant represents translation initiation at an
            alternate start codon compared to variant 1; the 5'-most initiation
            codon, as used in variant 1, is associated with a truncated ORF
            that would render the transcript a candidate for nonsense-mediated
            decay (NMD). Leaky scanning may allow translation initiation at the
            alternate start codon to encode an isoform (4) that has a longer
            and distinct N-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2686322.1,
                                           SRR14038193.2277031.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..245
                     /product="eukaryotic translation initiation factor 4E
                     isoform 4"
                     /note="mRNA cap-binding protein; eIF-4F 25 kDa subunit;
                     eukaryotic translation initiation factor 4E-like 1"
                     /calculated_mol_wt=28381
     Region          66..225
                     /region_name="IF4E"
                     /note="Eukaryotic initiation factor 4E; pfam01652"
                     /db_xref="CDD:460281"
     CDS             1..245
                     /gene="EIF4E"
                     /gene_synonym="AUTS19; CBP; eIF-4E; EIF4E1; EIF4EL1;
                     EIF4F"
                     /coded_by="NM_001331017.2:220..957"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS82940.1"
                     /db_xref="GeneID:1977"
                     /db_xref="HGNC:HGNC:3287"
                     /db_xref="MIM:133440"
ORIGIN      
        1 mkkkqnkker kkmraedgen daikkqaesl resqettptp npptteeekt esnqevanpe
       61 hyikhplqnr walwffkndk sktwqanlrl iskfdtvedf walynhiqls snlmpgcdys
      121 lfkdgiepmw edeknkrggr wlitlnkqqr rsdldrfwle tllcligesf ddysddvcga
      181 vvnvrakgdk iaiwttecen reavthigrv ykerlglppk ivigyqshad tatksgsttk
      241 nrfvv
//
LOCUS       NP_001309792             324 aa            linear   PRI 21-NOV-2025
DEFINITION  NIPA-like protein 3 isoform c [Homo sapiens].
ACCESSION   NP_001309792
VERSION     NP_001309792.1
DBSOURCE    REFSEQ: accession NM_001322863.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Grzmil,P., Konietzko,J., Boehm,D., Holter,S.M.,
            Aguilar-Pimentel,A., Javaheri,A., Kalaydjiev,S., Adler,T.,
            Bolle,I., Adham,I., Dixkens,C., Wolf,S., Fuchs,H.,
            Gailus-Durner,V., Wurst,W., Ollert,M., Busch,D.H., Schulz,H., de
            Angelis,M.H. and Burfeind,P.
  TITLE     Targeted disruption of the mouse Npal3 gene leads to deficits in
            behavior, increased IgE levels, and impaired lung function
  JOURNAL   Cytogenet Genome Res 125 (3), 186-200 (2009)
   PUBMED   19738379
  REMARK    GeneRIF: Study demonstrates that both human NPAL3 and mouse NPAL3
            are ubiquitously expressed and encode highly conserved proteins
            Erratum:[Cytogenet Genome Res. 2009;125(4):285. Hoelter, S M
            [corrected to Holter, S M]; Aguilar, A [corrected to
            Aguilar-Pimentel, A]; Gailus-Durne, V [corrected to Gailus-Durner,
            V]; Busch, D [corrected to Busch, D H]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL031431.8.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2464592.1,
                                           SRR14038197.2613025.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..324
                     /product="NIPA-like protein 3 isoform c"
                     /note="NIPA-like protein 3"
                     /calculated_mol_wt=35633
     Region          1..244
                     /region_name="EamA"
                     /note="EamA-like transporter family; cl23754"
                     /db_xref="CDD:474045"
     CDS             1..324
                     /gene="NIPAL3"
                     /gene_synonym="DJ462O23.2; NPAL3; SLC57A5"
                     /coded_by="NM_001322863.2:689..1663"
                     /note="isoform c is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS81282.1"
                     /db_xref="GeneID:57185"
                     /db_xref="HGNC:HGNC:25233"
                     /db_xref="MIM:620034"
ORIGIN      
        1 mllgelgvfa syafaplsli vplsavsvia saiigiifik ekwkpkdflr ryvlsfvgcg
       61 lavvgtyllv tfapnshekm tgenvtrhlv swpfllymlv eiilfcllly fykeknanni
      121 vvilllvall gsmtvvtvka vagmlvlsiq gnlqldypif yvmfvcmvat avyqaaflsq
      181 asqmydssli asvgyilstt iaitagaify ldfigedvlh icmfalgcli aflgvflitr
      241 nrkkpipfep yismdampgm qnmhdkgmtv qpelkasfsy galenndnis eiyapatlpv
      301 mqeehgsrsa sgvpyrvleh tkke
//
LOCUS       NP_001381705             452 aa            linear   PRI 21-NOV-2025
DEFINITION  COP9 signalosome complex subunit 1 isoform 20 [Homo sapiens].
ACCESSION   NP_001381705
VERSION     NP_001381705.1
DBSOURCE    REFSEQ: accession NM_001394776.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Wei,H., Niu,Z., Ji,R., Jiang,W., Tang,J., Meng,Z., Cao,X., Zhang,X.
            and Liu,X.
  TITLE     Bioinformatics analysis of GPS1 expression and biological function
            in breast cancer
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 52 (2024)
   PUBMED   38289496
  REMARK    GeneRIF: Bioinformatics analysis of GPS1 expression and biological
            function in breast cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Fu,H., Zhang,Y., Chen,Y., Chen,J. and Chen,P.
  TITLE     CSN1 facilitates proliferation and migration of hepatocellular
            carcinoma cells by upregulating cyclin A2 expression
  JOURNAL   Mol Med Rep 23 (1) (2021)
   PUBMED   33200803
  REMARK    GeneRIF: CSN1 facilitates proliferation and migration of
            hepatocellular carcinoma cells by upregulating cyclin A2
            expression.
REFERENCE   5  (residues 1 to 452)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 452)
  AUTHORS   Lyapina,S., Cope,G., Shevchenko,A., Serino,G., Tsuge,T., Zhou,C.,
            Wolf,D.A., Wei,N., Shevchenko,A. and Deshaies,R.J.
  TITLE     Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome
  JOURNAL   Science 292 (5520), 1382-1385 (2001)
   PUBMED   11337588
REFERENCE   7  (residues 1 to 452)
  AUTHORS   Bech-Otschir,D., Kraft,R., Huang,X., Henklein,P., Kapelari,B.,
            Pollmann,C. and Dubiel,W.
  TITLE     COP9 signalosome-specific phosphorylation targets p53 to
            degradation by the ubiquitin system
  JOURNAL   EMBO J 20 (7), 1630-1639 (2001)
   PUBMED   11285227
REFERENCE   8  (residues 1 to 452)
  AUTHORS   Tsuge,T., Matsui,M. and Wei,N.
  TITLE     The subunit 1 of the COP9 signalosome suppresses gene expression
            through its N-terminal domain and incorporates into the complex
            through the PCI domain
  JOURNAL   J Mol Biol 305 (1), 1-9 (2001)
   PUBMED   11114242
  REMARK    GeneRIF: The N-terminal half of CSN1/GPS1 is required to repress
            c-fos expression and to inhibit AP-1 and SRE transactivation, while
            the C-terminal half allows integration of the protein into the COP9
            signalosome.
REFERENCE   9  (residues 1 to 452)
  AUTHORS   Seeger,M., Kraft,R., Ferrell,K., Bech-Otschir,D., Dumdey,R.,
            Schade,R., Gordon,C., Naumann,M. and Dubiel,W.
  TITLE     A novel protein complex involved in signal transduction possessing
            similarities to 26S proteasome subunits
  JOURNAL   FASEB J 12 (6), 469-478 (1998)
   PUBMED   9535219
REFERENCE   10 (residues 1 to 452)
  AUTHORS   Spain,B.H., Bowdish,K.S., Pacal,A.R., Staub,S.F., Koo,D.,
            Chang,C.Y., Xie,W. and Colicelli,J.
  TITLE     Two human cDNAs, including a homolog of Arabidopsis FUS6 (COP11),
            suppress G-protein- and mitogen-activated protein kinase-mediated
            signal transduction in yeast and mammalian cells
  JOURNAL   Mol Cell Biol 16 (12), 6698-6706 (1996)
   PUBMED   8943324
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC135056.4.
            
            Summary: This gene is known to suppress G-protein and
            mitogen-activated signal transduction in mammalian cells. The
            encoded protein shares significant similarity with Arabidopsis
            FUS6, which is a regulator of light-mediated signal transduction in
            plant cells. [provided by RefSeq, Mar 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..452
                     /product="COP9 signalosome complex subunit 1 isoform 20"
                     /note="COP9 signalosome complex subunit 1; JAB1-containing
                     signalosome subunit 1"
                     /calculated_mol_wt=50843
     Region          115..297
                     /region_name="RPN7"
                     /note="26S proteasome subunit RPN7; pfam10602"
                     /db_xref="CDD:431387"
     Region          336..404
                     /region_name="PINT"
                     /note="motif in proteasome subunits, Int-6, Nip-1 and
                     TRIP-15; smart00088"
                     /db_xref="CDD:214509"
     CDS             1..452
                     /gene="GPS1"
                     /gene_synonym="COPS1; CSN1; SGN1"
                     /coded_by="NM_001394776.1:184..1542"
                     /note="isoform 20 is encoded by transcript variant 27"
                     /db_xref="GeneID:2873"
                     /db_xref="HGNC:HGNC:4549"
                     /db_xref="MIM:601934"
ORIGIN      
        1 mlqgavepmq idvdpqedpq napdvnyvve npsldleqya asysglmrie rlqfiadhcp
       61 tlrvealkma lsfvqrtfnv dmyeeihrkl seatrelqna pdaipesgve ppaldtawve
      121 atrkkallkl ekldtdlkny kgnsikesir rghddlgdhy ldcgdlsnal kcysrardyc
      181 tsakhvinmc lnvikvsvyl qnwshvlsyv skaestpeia eqrgerdsqt qailtklkca
      241 aglaelaark ykqaakclll asfdhcdfpe llspsnvaiy gglcalatfd rqelqrnvis
      301 sssfklflel epqvrdiifk fyeskyascl kmldemkyfs pyvsadmhrm aaafnttvaa
      361 ledeltqlil eglisarvds hskilyardv dqrsttfeks llmgkefqrr akammlraav
      421 lrnqihvksp pregsqgelt pansqsrmst nm
//
LOCUS       NP_001352565            1629 aa            linear   PRI 21-NOV-2025
DEFINITION  protein TASOR isoform e [Homo sapiens].
ACCESSION   NP_001352565 XP_006713140
VERSION     NP_001352565.1
DBSOURCE    REFSEQ: accession NM_001365636.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1629)
  AUTHORS   Jensvold,Z.D., Flood,J.R., Christenson,A.E. and Lewis,P.W.
  TITLE     Interplay between Two Paralogous Human Silencing Hub (HuSH)
            Complexes in Regulating LINE-1 Element Silencing
  JOURNAL   Nat Commun 15 (1), 9492 (2024)
   PUBMED   39489739
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1629)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   3  (residues 1 to 1629)
  AUTHORS   Vauthier,V., Lasserre,A., Morel,M., Versapuech,M.,
            Berlioz-Torrent,C., Zamborlini,A., Margottin-Goguet,F. and
            Matkovic,R.
  TITLE     HUSH-mediated HIV silencing is independent of TASOR phosphorylation
            on threonine 819
  JOURNAL   Retrovirology 19 (1), 23 (2022)
   PUBMED   36309692
  REMARK    GeneRIF: HUSH-mediated HIV silencing is independent of TASOR
            phosphorylation on threonine 819.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1629)
  AUTHORS   Matkovic,R., Morel,M., Lanciano,S., Larrous,P., Martin,B.,
            Bejjani,F., Vauthier,V., Hansen,M.M.K., Emiliani,S., Cristofari,G.,
            Gallois-Montbrun,S. and Margottin-Goguet,F.
  TITLE     TASOR epigenetic repressor cooperates with a CNOT1 RNA degradation
            pathway to repress HIV
  JOURNAL   Nat Commun 13 (1), 66 (2022)
   PUBMED   35013187
  REMARK    GeneRIF: TASOR epigenetic repressor cooperates with a CNOT1 RNA
            degradation pathway to repress HIV.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1629)
  AUTHORS   Douse,C.H., Tchasovnikarova,I.A., Timms,R.T., Protasio,A.V.,
            Seczynska,M., Prigozhin,D.M., Albecka,A., Wagstaff,J.,
            Williamson,J.C., Freund,S.M.V., Lehner,P.J. and Modis,Y.
  TITLE     TASOR is a pseudo-PARP that directs HUSH complex assembly and
            epigenetic transposon control
  JOURNAL   Nat Commun 11 (1), 4940 (2020)
   PUBMED   33009411
  REMARK    GeneRIF: TASOR is a pseudo-PARP that directs HUSH complex assembly
            and epigenetic transposon control.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1629)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   7  (residues 1 to 1629)
  AUTHORS   Lango Allen,H., Estrada,K., Lettre,G., Berndt,S.I., Weedon,M.N.,
            Rivadeneira,F., Willer,C.J., Jackson,A.U., Vedantam,S.,
            Raychaudhuri,S., Ferreira,T., Wood,A.R., Weyant,R.J., Segre,A.V.,
            Speliotes,E.K., Wheeler,E., Soranzo,N., Park,J.H., Yang,J.,
            Gudbjartsson,D., Heard-Costa,N.L., Randall,J.C., Qi,L., Vernon
            Smith,A., Magi,R., Pastinen,T., Liang,L., Heid,I.M., Luan,J.,
            Thorleifsson,G., Winkler,T.W., Goddard,M.E., Sin Lo,K., Palmer,C.,
            Workalemahu,T., Aulchenko,Y.S., Johansson,A., Zillikens,M.C.,
            Feitosa,M.F., Esko,T., Johnson,T., Ketkar,S., Kraft,P., Mangino,M.,
            Prokopenko,I., Absher,D., Albrecht,E., Ernst,F., Glazer,N.L.,
            Hayward,C., Hottenga,J.J., Jacobs,K.B., Knowles,J.W., Kutalik,Z.,
            Monda,K.L., Polasek,O., Preuss,M., Rayner,N.W., Robertson,N.R.,
            Steinthorsdottir,V., Tyrer,J.P., Voight,B.F., Wiklund,F., Xu,J.,
            Zhao,J.H., Nyholt,D.R., Pellikka,N., Perola,M., Perry,J.R.,
            Surakka,I., Tammesoo,M.L., Altmaier,E.L., Amin,N., Aspelund,T.,
            Bhangale,T., Boucher,G., Chasman,D.I., Chen,C., Coin,L.,
            Cooper,M.N., Dixon,A.L., Gibson,Q., Grundberg,E., Hao,K., Juhani
            Junttila,M., Kaplan,L.M., Kettunen,J., Konig,I.R., Kwan,T.,
            Lawrence,R.W., Levinson,D.F., Lorentzon,M., McKnight,B.,
            Morris,A.P., Muller,M., Suh Ngwa,J., Purcell,S., Rafelt,S.,
            Salem,R.M., Salvi,E., Sanna,S., Shi,J., Sovio,U., Thompson,J.R.,
            Turchin,M.C., Vandenput,L., Verlaan,D.J., Vitart,V., White,C.C.,
            Ziegler,A., Almgren,P., Balmforth,A.J., Campbell,H., Citterio,L.,
            De Grandi,A., Dominiczak,A., Duan,J., Elliott,P., Elosua,R.,
            Eriksson,J.G., Freimer,N.B., Geus,E.J., Glorioso,N., Haiqing,S.,
            Hartikainen,A.L., Havulinna,A.S., Hicks,A.A., Hui,J., Igl,W.,
            Illig,T., Jula,A., Kajantie,E., Kilpelainen,T.O., Koiranen,M.,
            Kolcic,I., Koskinen,S., Kovacs,P., Laitinen,J., Liu,J., Lokki,M.L.,
            Marusic,A., Maschio,A., Meitinger,T., Mulas,A., Pare,G.,
            Parker,A.N., Peden,J.F., Petersmann,A., Pichler,I.,
            Pietilainen,K.H., Pouta,A., Ridderstrale,M., Rotter,J.I.,
            Sambrook,J.G., Sanders,A.R., Schmidt,C.O., Sinisalo,J., Smit,J.H.,
            Stringham,H.M., Bragi Walters,G., Widen,E., Wild,S.H.,
            Willemsen,G., Zagato,L., Zgaga,L., Zitting,P., Alavere,H.,
            Farrall,M., McArdle,W.L., Nelis,M., Peters,M.J., Ripatti,S., van
            Meurs,J.B., Aben,K.K., Ardlie,K.G., Beckmann,J.S., Beilby,J.P.,
            Bergman,R.N., Bergmann,S., Collins,F.S., Cusi,D., den Heijer,M.,
            Eiriksdottir,G., Gejman,P.V., Hall,A.S., Hamsten,A., Huikuri,H.V.,
            Iribarren,C., Kahonen,M., Kaprio,J., Kathiresan,S., Kiemeney,L.,
            Kocher,T., Launer,L.J., Lehtimaki,T., Melander,O., Mosley,T.H. Jr.,
            Musk,A.W., Nieminen,M.S., O'Donnell,C.J., Ohlsson,C., Oostra,B.,
            Palmer,L.J., Raitakari,O., Ridker,P.M., Rioux,J.D., Rissanen,A.,
            Rivolta,C., Schunkert,H., Shuldiner,A.R., Siscovick,D.S.,
            Stumvoll,M., Tonjes,A., Tuomilehto,J., van Ommen,G.J., Viikari,J.,
            Heath,A.C., Martin,N.G., Montgomery,G.W., Province,M.A., Kayser,M.,
            Arnold,A.M., Atwood,L.D., Boerwinkle,E., Chanock,S.J., Deloukas,P.,
            Gieger,C., Gronberg,H., Hall,P., Hattersley,A.T., Hengstenberg,C.,
            Hoffman,W., Lathrop,G.M., Salomaa,V., Schreiber,S., Uda,M.,
            Waterworth,D., Wright,A.F., Assimes,T.L., Barroso,I., Hofman,A.,
            Mohlke,K.L., Boomsma,D.I., Caulfield,M.J., Cupples,L.A.,
            Erdmann,J., Fox,C.S., Gudnason,V., Gyllensten,U., Harris,T.B.,
            Hayes,R.B., Jarvelin,M.R., Mooser,V., Munroe,P.B., Ouwehand,W.H.,
            Penninx,B.W., Pramstaller,P.P., Quertermous,T., Rudan,I.,
            Samani,N.J., Spector,T.D., Volzke,H., Watkins,H., Wilson,J.F.,
            Groop,L.C., Haritunians,T., Hu,F.B., Kaplan,R.C., Metspalu,A.,
            North,K.E., Schlessinger,D., Wareham,N.J., Hunter,D.J.,
            O'Connell,J.R., Strachan,D.P., Wichmann,H.E., Borecki,I.B., van
            Duijn,C.M., Schadt,E.E., Thorsteinsdottir,U., Peltonen,L.,
            Uitterlinden,A.G., Visscher,P.M., Chatterjee,N., Loos,R.J.,
            Boehnke,M., McCarthy,M.I., Ingelsson,E., Lindgren,C.M.,
            Abecasis,G.R., Stefansson,K., Frayling,T.M. and Hirschhorn,J.N.
  TITLE     Hundreds of variants clustered in genomic loci and biological
            pathways affect human height
  JOURNAL   Nature 467 (7317), 832-838 (2010)
   PUBMED   20881960
REFERENCE   8  (residues 1 to 1629)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   9  (residues 1 to 1629)
  AUTHORS   Eichmuller,S., Usener,D., Dummer,R., Stein,A., Thiel,D. and
            Schadendorf,D.
  TITLE     Serological detection of cutaneous T-cell lymphoma-associated
            antigens
  JOURNAL   Proc Natl Acad Sci U S A 98 (2), 629-634 (2001)
   PUBMED   11149944
REFERENCE   10 (residues 1 to 1629)
  AUTHORS   Li,Q., Wen,H. and Ao,S.
  TITLE     Identification and cloning of the cDNA of a Rb-associated protein
            RAP140a
  JOURNAL   Sci China C Life Sci 43 (6), 637-647 (2000)
   PUBMED   18726359
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099781.2.
            
            On Sep 6, 2018 this sequence version replaced XP_006713140.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.150740.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1629
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.3"
     Protein         1..1629
                     /product="protein TASOR isoform e"
                     /note="retinoblastoma-associated protein 140; CTCL tumor
                     antigen se89-1; retinoblastoma-associated protein RAP140;
                     protein FAM208A; transgene activation suppressor protein;
                     protein TASOR; family with sequence similarity 208 member
                     A"
                     /calculated_mol_wt=184239
     Region          166..319
                     /region_name="DUF3715"
                     /note="Protein of unknown function (DUF3715); pfam12509"
                     /db_xref="CDD:463613"
     Region          973..1054
                     /region_name="TASOR_PBD"
                     /note="periphilin binding domain of protein TASOR and
                     similar proteins; cd22569"
                     /db_xref="CDD:439336"
     Site            order(973,975..977,979..980,983..984,987..988,990..991,
                     994..995,998..999,1002,1004..1011,1031,1033..1037,
                     1040..1041,1043..1044,1047..1048,1051..1052)
                     /site_type="other"
                     /note="periphilin binding site [polypeptide binding]"
                     /db_xref="CDD:439336"
     CDS             1..1629
                     /gene="TASOR"
                     /gene_synonym="C3orf63; FAM208A; RAP140; se89-1; TASOR1"
                     /coded_by="NM_001365636.2:260..5149"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="GeneID:23272"
                     /db_xref="HGNC:HGNC:30314"
                     /db_xref="MIM:616493"
ORIGIN      
        1 mataveteac qptdaswesg gggddemkqa lpelessqqn ggggglniae psggagreen
       61 agaeaaqsls heqpqdssea gaaalprgpe eperpvrrsf qiprksrekk alfqpltpgs
      121 refedvvnil hssyleptsv tnfnyrracl vhnellekef tekrrelkfd grldkelses
      181 yaflmvdryq vqticekglh vgqskitilg spsmgvylsr yadllqanpl dtgamgdvvi
      241 fkimkgkiks iydpmgvksl esmlnksald ptpkhechvs knanritsll ayrayeltqy
      301 yfyeygfdel rrrprhvcpy avvsftykdd iqtpkfvpss rsnsfntdrn idkynytlwk
      361 gqllnkgkll cyislrsatr aflpiklpek ldvetvmsid hlkqkippal fyketylgpn
      421 evlkngmycs lyevvektri gsnmesllqk ldreklvlvk plgdrgylfl lspyqmvppy
      481 eyqtaksrvl halflfqepr sivtsqkgst naapqerhes mpdvlkiaqf lqfsliqcrk
      541 efknisainf hsvvekyvse ffkrgfgsgk refimfpyds rlddkkflys aprnkshidt
      601 clhayifrpe vyqlpicklk elfeenrklq qfsplsdyeg qeeemngtkm kfgkrnnsrg
      661 eaiisgkqrs shsldydkdr vkelinliqc rkksvggdsd tedmrsktvl krkledlpen
      721 mrklaktsnl senchlyees pqpigslghd adlrrqqqdt cnsgiadihr lfnwlsetla
      781 narhsdaslt dtvnkalgls tddayeelrq kheyelnstp dkkdyeqptc akvenaqfkg
      841 tqslllevda tskysvaist sevgtdhklh lkedpnlisv nnfedcslcp svpiehgfrr
      901 qqsksnnvee teihwklipi tggnarsped qlgkhgekqt pdtlkgtted dvltgqveeq
      961 cvpaaeaepp avsettertv lgeynlfsrk ieeilkqknv syvstvstpi fstqekmkrl
     1021 sefiysktsk agvqefvdgl heklntiiik asakggnlpp vspndsgaki asnplerhvi
     1081 pvsssdfnnk hlleplcsdp lkdtnsdeqh stsaltevem nqpqhatelm vtsdhivpgd
     1141 marepveett kspsdvnisa qpalsnfisq lepevfnslv kimkdvqknt vkfyiheeee
     1201 svlckeikey liklgntech peqflerrsk ldklliiiqn ediagfihki pglvtlkklp
     1261 cvsfagvdsl ddvknhtyne lfvsggfivs desilnpevv tvenlknflt fleelstpeg
     1321 kwqwkvhckf qkklkelgrl nakalslltl lnvyqkkhlv eilsyhncds qtrnapeldc
     1381 lirlqaqniq qrhivfltek nikmlssytd ngivvataed fmqnfknlvg yhnsiteenl
     1441 pqlganenle sqsallende kdeedmslds gdeishievc snfhseiwek etkgsrgtdq
     1501 kkntqielqs spdvqnslle dktyldseer tsidivcseg ensnsteqds ysnfqvyhsq
     1561 lnmshqfshf nvlthqtflg tpyalsssqs qenenyflsa ytesldrdks ppplswgksd
     1621 ssrpysqek
//
LOCUS       NP_001387300             235 aa            linear   PRI 21-NOV-2025
DEFINITION  single-stranded DNA-binding protein 2 isoform 36 [Homo sapiens].
ACCESSION   NP_001387300
VERSION     NP_001387300.1
DBSOURCE    REFSEQ: accession NM_001400371.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Schwab,C., Roberts,K., Boer,J.M., Gohring,G., Steinemann,D.,
            Vora,A., Macartney,C., Hough,R., Thorn,Z., Dillon,R., Escherich,G.,
            Cazzaniga,G., Schlegelberger,B., Loh,M., den Boer,M.L.,
            Moorman,A.V. and Harrison,C.J.
  TITLE     SSBP2-CSF1R is a recurrent fusion in B-lineage acute lymphoblastic
            leukemia with diverse genetic presentation and variable outcome
  JOURNAL   Blood 137 (13), 1835-1838 (2021)
   PUBMED   33197935
  REMARK    GeneRIF: SSBP2-CSF1R is a recurrent fusion in B-lineage acute
            lymphoblastic leukemia with diverse genetic presentation and
            variable outcome.
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Wang,H., Kim,J., Wang,Z., Yan,X.X., Dean,A. and Xu,W.
  TITLE     Crystal structure of human LDB1 in complex with SSBP2
  JOURNAL   Proc Natl Acad Sci U S A 117 (2), 1042-1048 (2020)
   PUBMED   31892537
  REMARK    GeneRIF: Single-stranded DNA binding proteins (SSBPs) interact
            specifically with the LDB/Chip conserved domain (LCCD) of LDB
            proteins and stabilize LDBs by preventing their proteasomal
            degradation, thus promoting their functions in gene regulation.
REFERENCE   5  (residues 1 to 235)
  AUTHORS   Kim,H., Kim,Y., Bang,S., Park,S., Jee,S., Sim,J., Shin,S.J.,
            Paik,S.S. and Jang,K.
  TITLE     Low Expression of Single-stranded DNA Binding Protein 2 (SSBP2)
            Predicts Unfavourable Postoperative Outcomes in Patients With Clear
            Cell Renal Cell Carcinoma
  JOURNAL   In Vivo 34 (1), 101-107 (2020)
   PUBMED   31882468
  REMARK    GeneRIF: CcRCC with low SSBP2 expression was associated with
            adverse clinicopathological characteristics and poor patient
            outcomes.
REFERENCE   6  (residues 1 to 235)
  AUTHORS   Fleisig,H.B., Orazio,N.I., Liang,H., Tyler,A.F., Adams,H.P.,
            Weitzman,M.D. and Nagarajan,L.
  TITLE     Adenoviral E1B55K oncoprotein sequesters candidate leukemia
            suppressor sequence-specific single-stranded DNA-binding protein 2
            into aggresomes
  JOURNAL   Oncogene 26 (33), 4797-4805 (2007)
   PUBMED   17311003
  REMARK    GeneRIF: Results suggest that subverting SSBP2 function by
            oncoprotein E1B55K may contribute to cell transformation by viral
            oncoproteins.
REFERENCE   7  (residues 1 to 235)
  AUTHORS   Liang,H., Samanta,S. and Nagarajan,L.
  TITLE     SSBP2, a candidate tumor suppressor gene, induces growth arrest and
            differentiation of myeloid leukemia cells
  JOURNAL   Oncogene 24 (16), 2625-2634 (2005)
   PUBMED   15782145
  REMARK    GeneRIF: Our findings are consistent with human SSBP2 being a novel
            regulator of hematopoietic growth and differentiation, whose loss
            confers a block in differentiation advantage to myeloid leukemic
            cells.
REFERENCE   8  (residues 1 to 235)
  AUTHORS   Castro,P., Liang,H., Liang,J.C. and Nagarajan,L.
  TITLE     A novel, evolutionarily conserved gene family with putative
            sequence-specific single-stranded DNA-binding activity
  JOURNAL   Genomics 80 (1), 78-85 (2002)
   PUBMED   12079286
  REMARK    GeneRIF: Member of a closely related, evolutionarily conserved, and
            ubiquitously expressed gene family, potential tumor suppressor
REFERENCE   9  (residues 1 to 235)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 235)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016562.7, AC093250.3,
            AC026419.5 and AC010623.10.
            
            Summary: This gene encodes a subunit of a protein complex that
            interacts with single-stranded DNA and is involved in the DNA
            damage response and maintenance of genome stability. The encoded
            protein may also play a role in telomere repair. A variant of this
            gene may be associated with survival in human glioblastoma
            patients. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.729154.1,
                                           SRR18074967.2246835.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.1"
     Protein         1..235
                     /product="single-stranded DNA-binding protein 2 isoform
                     36"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein 2"
                     /calculated_mol_wt=23794
     Region          <13..212
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     CDS             1..235
                     /gene="SSBP2"
                     /gene_synonym="HSPC116; SOSS-B2"
                     /coded_by="NM_001400371.1:282..989"
                     /note="isoform 36 is encoded by transcript variant 40"
                     /db_xref="GeneID:23635"
                     /db_xref="HGNC:HGNC:15831"
                     /db_xref="MIM:607389"
ORIGIN      
        1 msprypggpr pplripnqal ggvpgsqpll psgmdptrqq ghpnmggpmq rmtpprgmvp
       61 lgpqnyggam rpplnalggp gmpgmnmgpg ggrpwpnptn ansipyssas pgnyvgppgg
      121 ggppgtpimp spadstnsgd nmytlmnavp pgpnrpnfpm gpgsdgpmgg lggmeshhmn
      181 gslgsgdmds isknspnnms lsnqpgtprd dgemggnfln pfqsesysps mtmsv
//
LOCUS       NP_001308435             264 aa            linear   PRI 21-NOV-2025
DEFINITION  septin-10 isoform 12 [Homo sapiens].
ACCESSION   NP_001308435
VERSION     NP_001308435.1
DBSOURCE    REFSEQ: accession NM_001321506.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Weiler,S.M.E., Bissinger,M., Rose,F., von Bubnoff,F., Lutz,T.,
            Ori,A., Schirmacher,P. and Breuhahn,K.
  TITLE     SEPTIN10-mediated crosstalk between cytoskeletal networks controls
            mechanotransduction and oncogenic YAP/TAZ signaling
  JOURNAL   Cancer Lett 584, 216637 (2024)
   PUBMED   38242197
  REMARK    GeneRIF: SEPTIN10-mediated crosstalk between cytoskeletal networks
            controls mechanotransduction and oncogenic YAP/TAZ signaling.
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Shen,B., Gao,H., Zhang,D., Yu,H., Chen,J., Huang,S., Gu,P. and
            Zhong,Y.
  TITLE     miR-124-3p regulates the proliferation and differentiation of
            retinal progenitor cells through SEPT10
  JOURNAL   Cell Tissue Res 392 (3), 689-704 (2023)
   PUBMED   36802303
  REMARK    GeneRIF: miR-124-3p regulates the proliferation and differentiation
            of retinal progenitor cells through SEPT10.
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Zhu,H., Tang,X., Zhang,H., Zhou,M., Liu,H., Chu,H. and Zhang,Z.
  TITLE     Exosomal circCLIP1 regulates PM2.5-induced airway obstruction via
            targeting SEPT10 in vitro
  JOURNAL   Ecotoxicol Environ Saf 254, 114750 (2023)
   PUBMED   36950992
  REMARK    GeneRIF: Exosomal circCLIP1 regulates PM2.5-induced airway
            obstruction via targeting SEPT10 in vitro.
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Xu,M., Takanashi,M., Oikawa,K., Nishi,H., Isaka,K., Yoshimoto,T.,
            Ohyashiki,J. and Kuroda,M.
  TITLE     Identification of a novel role of Septin 10 in
            paclitaxel-resistance in cancers through a functional genomics
            screen
  JOURNAL   Cancer Sci 103 (4), 821-827 (2012)
   PUBMED   22320903
  REMARK    GeneRIF: we found that paclitaxel-resistant tumors had decreased
            expression of SEPT10.
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Liu,M., Shen,S., Chen,F., Yu,W. and Yu,L.
  TITLE     Linking the septin expression with carcinogenesis
  JOURNAL   Mol Biol Rep 37 (7), 3601-3608 (2010)
   PUBMED   20195767
REFERENCE   8  (residues 1 to 264)
  AUTHORS   Benedetti,D., Bomben,R., Dal-Bo,M., Marconi,D., Zucchetto,A.,
            Degan,M., Forconi,F., Del-Poeta,G., Gaidano,G. and Gattei,V.
  TITLE     Are surrogates of IGHV gene mutational status useful in B-cell
            chronic lymphocytic leukemia? The example of Septin-10
  JOURNAL   Leukemia 22 (1), 224-226 (2008)
   PUBMED   17657217
  REMARK    GeneRIF: Lack of SEPT10 transcript is associated with B-cell
            chronic lymphocytic leukemia
REFERENCE   9  (residues 1 to 264)
  AUTHORS   Sui,L., Zhang,W., Liu,Q., Chen,T., Li,N., Wan,T., Yu,M. and Cao,X.
  TITLE     Cloning and functional characterization of human septin 10, a novel
            member of septin family cloned from dendritic cells
  JOURNAL   Biochem Biophys Res Commun 304 (2), 393-398 (2003)
   PUBMED   12711328
  REMARK    GeneRIF: Cloning and functional characterization of septin 10.
REFERENCE   10 (residues 1 to 264)
  AUTHORS   Macara,I.G., Baldarelli,R., Field,C.M., Glotzer,M., Hayashi,Y.,
            Hsu,S.C., Kennedy,M.B., Kinoshita,M., Longtine,M., Low,C.,
            Maltais,L.J., McKenzie,L., Mitchison,T.J., Nishikawa,T., Noda,M.,
            Petty,E.M., Peifer,M., Pringle,J.R., Robinson,P.J., Roth,D.,
            Russell,S.E., Stuhlmann,H., Tanaka,M., Tanaka,T., Trimble,W.S.,
            Ware,J., Zeleznik-Le,N.J. and Zieger,B.
  TITLE     Mammalian septins nomenclature
  JOURNAL   Mol Biol Cell 13 (12), 4111-4113 (2002)
   PUBMED   12475938
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011753.6 and AC140485.3.
            
            Summary: This gene encodes a member of the septin family of
            cytoskeletal proteins with GTPase activity. This protein localizes
            to the cytoplasm and nucleus and displays GTP-binding and GTPase
            activity. A pseudogene for this gene is located on chromosome 8.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Apr 2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3150620.1,
                                           SRR14038191.30858.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..264
                     /product="septin-10 isoform 12"
                     /calculated_mol_wt=30813
     Region          <10..141
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            18..21
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206648"
     Site            72..74
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206648"
     CDS             1..264
                     /gene="SEPTIN10"
                     /gene_synonym="SEPT10; Septin-10"
                     /coded_by="NM_001321506.2:140..934"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="GeneID:151011"
                     /db_xref="HGNC:HGNC:14349"
                     /db_xref="MIM:611737"
ORIGIN      
        1 massevarhl vniipviaka dtvsktelqk fkiklmselv sngvqiyqfp tdddtiakvn
       61 aamngqlpfa vvgsmdevkv gnkmvkarqy pwgvvqvene nhcdfvklre mlictnmedl
      121 reqthtrhye lyrrckleem gftdvgpenk pvsvqetyea krhefhgerq rkeeemkqmf
      181 vqrvkekeai lkeaerelqa kfehlkrlhq eermkleekr rlleeeiiaf skkkatseif
      241 hsqsflatgs nlrkdkdrkn snfl
//
LOCUS       NP_001372254            1032 aa            linear   PRI 21-NOV-2025
DEFINITION  C2 domain-containing protein 5 isoform i [Homo sapiens].
ACCESSION   NP_001372254 XP_016875765
VERSION     NP_001372254.1
DBSOURCE    REFSEQ: accession NM_001385325.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1032)
  AUTHORS   Chapman,D.E., Reddy,B.J.N., Huy,B., Bovyn,M.J., Cruz,S.J.S.,
            Al-Shammari,Z.M., Han,H., Wang,W., Smith,D.S. and Gross,S.P.
  TITLE     Regulation of in vivo dynein force production by CDK5 and
            14-3-3epsilon and KIAA0528
  JOURNAL   Nat Commun 10 (1), 228 (2019)
   PUBMED   30651536
  REMARK    GeneRIF: Study finds that CDK5, 14-3-3 epsilon, and KIAA0528 are
            all essential for cytoplasmic dynein force adaptation and that they
            regulate the transport of lipid droplets, lysosomes, and
            mitochondria.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1032)
  AUTHORS   Lu,Y., Ma,J., Li,Y., Huang,J., Zhang,S., Yin,Z., Ren,J., Huang,K.,
            Wu,G., Yang,K. and Xu,S.
  TITLE     CDP138 silencing inhibits TGF-beta/Smad signaling to impair
            radioresistance and metastasis via GDF15 in lung cancer
  JOURNAL   Cell Death Dis 8 (9), e3036 (2017)
   PUBMED   28880265
  REMARK    GeneRIF: Enhanced radiosensitivity and decreased migration in cells
            caused by CDP138 knockdown are partially dependent on GDF15
            inhibition.
            Erratum:[Cell Death Dis. 2024 Jul 31;15(7):549. doi:
            10.1038/s41419-024-06823-2. PMID: 39085215]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1032)
  AUTHORS   Xu,S., Li,X., Gong,Z., Wang,W., Li,Y., Nair,B.C., Piao,H., Yang,K.,
            Wu,G. and Chen,J.
  TITLE     Proteomic analysis of the human cyclin-dependent kinase family
            reveals a novel CDK5 complex involved in cell growth and migration
  JOURNAL   Mol Cell Proteomics 13 (11), 2986-3000 (2014)
   PUBMED   25096995
REFERENCE   7  (residues 1 to 1032)
  AUTHORS   Xie,X., Gong,Z., Mansuy-Aubert,V., Zhou,Q.L., Tatulian,S.A.,
            Sehrt,D., Gnad,F., Brill,L.M., Motamedchaboki,K., Chen,Y.,
            Czech,M.P., Mann,M., Kruger,M. and Jiang,Z.Y.
  TITLE     C2 domain-containing phosphoprotein CDP138 regulates GLUT4
            insertion into the plasma membrane
  JOURNAL   Cell Metab 14 (3), 378-389 (2011)
   PUBMED   21907143
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC053513.4.
            
            On Jul 15, 2020 this sequence version replaced XP_016875765.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.150908.1,
                                           SRR1660803.29147.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..1032
                     /product="C2 domain-containing protein 5 isoform i"
                     /note="138 kDa C2 domain-containing phosphoprotein; C2
                     domain-containing protein 5"
                     /calculated_mol_wt=113835
     Region          5..114
                     /region_name="C2_KIAA0528-like"
                     /note="C2 domain found in the Human KIAA0528 cDNA clone;
                     cd08688"
                     /db_xref="CDD:176070"
     CDS             1..1032
                     /gene="C2CD5"
                     /gene_synonym="CDP138; KIAA0528"
                     /coded_by="NM_001385325.1:253..3351"
                     /note="isoform i is encoded by transcript variant 10"
                     /db_xref="GeneID:9847"
                     /db_xref="HGNC:HGNC:29062"
                     /db_xref="MIM:618044"
ORIGIN      
        1 mpgklkvkiv agrhlpvmdr asdltdafve vkfgnttfkt dvylkslnpq wnsewfkfev
       61 ddedlqdepl qitvldhdty sandaigkvy ididpllyse aatvisgwfp iydtihgirg
      121 einvvvkvdl fndlnrfrqs scgvkffctt sipkcyravi ihgfveelvv nedpeyqwid
      181 rirtprasne arqrlislms gelqrkiglk vlemrgnavv gylqcfdleg esglvvraig
      241 tactldklss paaflpacns pskemkespl vhppshgcrs thnspihtat gsrltqnfsv
      301 svptliytgm gsgsagkegg pfkallrqqt qsaleqrefp fftltafppg flvhvggvvs
      361 arsvklldri hnpdepetrd awwaeirqei kshakalgch avvgysests iceevcilsa
      421 sgtaavlnpr flqdgtvegc leqrleenlp trcgfchipy delnmpfpah ltycyncrkq
      481 kvpdvlftti dlptdatvig kgcliqarlc rlkkkaqaea nataisnllp fmeyevhtql
      541 mnklklkgmn alfglriqit vgenmlmgla satgvylaal ptpggiqiag ktpndgsyeq
      601 hishmqkkin dtiaknkely einppeisee iigspipepr qrsrllrsqs essdevteld
      661 lshgkkdafv leiddtdame dvhslltdvp ppsgfyscnt eimpginnwt seiqmftsvr
      721 virlsslnlt nqalnknfnd lcenllksly fklrsmipcc lchvnftvsl pedeliqvtv
      781 tavaitfdkn qalqttktpv ekslqrastd neellqfple lcsdslpshp fppakehles
      841 assnsgipaa qrdrcsswie liklkaqtir rgsikttmtv ekaspvgdgn frnrsappca
      901 nstvgvvkmt plsfipgaki tkylgiinmf firettslre eggvsgflha fiaevfamvr
      961 ahvaalggna vvsyimkqcv fmenpnknqa qclinvsgda vvfvresdle vvssqqpttn
     1021 cqssctegev tt
//
LOCUS       NP_001193995             352 aa            linear   PRI 21-NOV-2025
DEFINITION  coxsackievirus and adenovirus receptor isoform 5 precursor [Homo
            sapiens].
ACCESSION   NP_001193995
VERSION     NP_001193995.1
DBSOURCE    REFSEQ: accession NM_001207066.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Tan,H.J., Deng,Z.H., Zhang,C., Deng,H.W. and Xiao,H.M.
  TITLE     CXADR promote epithelial-mesenchymal transition in endometriosis by
            modulating AKT/GSK-3beta signaling
  JOURNAL   Cell Cycle 22 (21-22), 2436-2448 (2023)
   PUBMED   38146657
  REMARK    GeneRIF: CXADR promote epithelial-mesenchymal transition in
            endometriosis by modulating AKT/GSK-3beta signaling.
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Oliviero,F., Klement,W., Mary,L., Dauwe,Y., Lippi,Y., Naylies,C.,
            Gayrard,V., Marchi,N. and Mselli-Lakhal,L.
  TITLE     CAR Protects Females from Diet-Induced Steatosis and Associated
            Metabolic Disorders
  JOURNAL   Cells 12 (18), 2218 (2023)
   PUBMED   37759441
  REMARK    GeneRIF: CAR Protects Females from Diet-Induced Steatosis and
            Associated Metabolic Disorders.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Nilchian,A., Plant,E., Parniewska,M.M., Santiago,A., Rossignoli,A.,
            Skogsberg,J., Hedin,U., Matic,L. and Fuxe,J.
  TITLE     Induction of the Coxsackievirus and Adenovirus Receptor in
            Macrophages During the Formation of Atherosclerotic Plaques
  JOURNAL   J Infect Dis 222 (12), 2041-2051 (2020)
   PUBMED   32852032
  REMARK    GeneRIF: Induction of the Coxsackievirus and Adenovirus Receptor in
            Macrophages During the Formation of Atherosclerotic Plaques.
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Herrmann,L., Filip,A., Lapuente,D., Tenbusch,M., Niehaus,K.,
            Rudolph,V. and Farr,M.
  TITLE     Naturally occurring variants in the transmembrane and cytoplasmic
            domains of the human Coxsackie- and adenovirus receptor have no
            impact on virus internalisation
  JOURNAL   Biochem Biophys Res Commun 527 (2), 401-405 (2020)
   PUBMED   32334832
  REMARK    GeneRIF: Naturally occurring variants in the transmembrane and
            cytoplasmic domains of the human Coxsackie- and adenovirus receptor
            have no impact on virus internalisation.
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Fechner,H., Haack,A., Wang,H., Wang,X., Eizema,K., Pauschinger,M.,
            Schoemaker,R., Veghel,R., Houtsmuller,A., Schultheiss,H.P.,
            Lamers,J. and Poller,W.
  TITLE     Expression of coxsackie adenovirus receptor and alphav-integrin
            does not correlate with adenovector targeting in vivo indicating
            anatomical vector barriers
  JOURNAL   Gene Ther 6 (9), 1520-1535 (1999)
   PUBMED   10490761
REFERENCE   7  (residues 1 to 352)
  AUTHORS   Bergelson,J.M., Krithivas,A., Celi,L., Droguett,G., Horwitz,M.S.,
            Wickham,T., Crowell,R.L. and Finberg,R.W.
  TITLE     The murine CAR homolog is a receptor for coxsackie B viruses and
            adenoviruses
  JOURNAL   J Virol 72 (1), 415-419 (1998)
   PUBMED   9420240
REFERENCE   8  (residues 1 to 352)
  AUTHORS   Carson,S.D., Chapman,N.N. and Tracy,S.M.
  TITLE     Purification of the putative coxsackievirus B receptor from HeLa
            cells
  JOURNAL   Biochem Biophys Res Commun 233 (2), 325-328 (1997)
   PUBMED   9144533
REFERENCE   9  (residues 1 to 352)
  AUTHORS   Tomko,R.P., Xu,R. and Philipson,L.
  TITLE     HCAR and MCAR: the human and mouse cellular receptors for subgroup
            C adenoviruses and group B coxsackieviruses
  JOURNAL   Proc Natl Acad Sci U S A 94 (7), 3352-3356 (1997)
   PUBMED   9096397
REFERENCE   10 (residues 1 to 352)
  AUTHORS   Bergelson,J.M., Cunningham,J.A., Droguett,G., Kurt-Jones,E.A.,
            Krithivas,A., Hong,J.S., Horwitz,M.S., Crowell,R.L. and
            Finberg,R.W.
  TITLE     Isolation of a common receptor for Coxsackie B viruses and
            adenoviruses 2 and 5
  JOURNAL   Science 275 (5304), 1320-1323 (1997)
   PUBMED   9036860
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CV570985.1 and AP000967.2.
            
            Summary: The protein encoded by this gene is a type I membrane
            receptor for group B coxsackieviruses and subgroup C adenoviruses.
            Several transcript variants encoding different isoforms have been
            found for this gene. Pseudogenes of this gene are found on
            chromosomes 15, 18, and 21. [provided by RefSeq, May 2011].
            
            Transcript Variant: This variant (5, alternatively referred to as
            CAREx8) differs in the 3' UTR and coding sequence compared to
            variant 1. The resulting isoform (5) has a shorter and distinct
            C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.166234.1,
                                           SRR5189667.362007.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.1"
     Protein         1..352
                     /product="coxsackievirus and adenovirus receptor isoform 5
                     precursor"
                     /note="46 kD coxsackievirus and adenovirus receptor (CAR)
                     protein; HCVADR; CVB3-binding protein; coxsackievirus
                     B-adenovirus receptor; coxsackie virus and adenovirus
                     receptor; CXADR Ig-like cell adhesion molecule"
                     /calculated_mol_wt=36885
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2071
     mat_peptide     20..352
                     /product="coxsackievirus and adenovirus receptor isoform
                     5"
                     /calculated_mol_wt=36885
     Region          20..136
                     /region_name="IgV_CAR_like"
                     /note="Immunoglobulin Variable (V) domain of the
                     Coxsackievirus and Adenovirus Receptor (CAR), and similar
                     proteins; cd20960"
                     /db_xref="CDD:409552"
     Region          20..44
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409552"
     Region          20..22
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409552"
     Region          26..31
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409552"
     Region          35..45
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409552"
     Region          45..53
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409552"
     Region          53..59
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409552"
     Region          54..59
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409552"
     Region          60..88
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409552"
     Region          69..75
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409552"
     Region          78..81
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409552"
     Region          89..123
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409552"
     Region          90..93
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409552"
     Region          101..110
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409552"
     Region          116..124
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409552"
     Region          116..124
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409552"
     Region          124..127
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409552"
     Region          128..136
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409552"
     Region          128..136
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409552"
     Region          155..229
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          158..162
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          172..178
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          195..199
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          209..214
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          222..225
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..352
                     /gene="CXADR"
                     /gene_synonym="CAR; CAR4/6; HCAR"
                     /coded_by="NM_001207066.2:88..1146"
                     /note="isoform 5 precursor is encoded by transcript
                     variant 5"
                     /db_xref="CCDS:CCDS56204.1"
                     /db_xref="GeneID:1525"
                     /db_xref="HGNC:HGNC:2559"
                     /db_xref="MIM:602621"
ORIGIN      
        1 malllcfvll cgvvdfarsl sittpeemie kakgetaylp ckftlspedq gpldiewlis
       61 padnqkvdqv iilysgdkiy ddyypdlkgr vhftsndlks gdasinvtnl qlsdigtyqc
      121 kvkkapgvan kkihlvvlvk psgarcyvdg seeigsdfki kcepkegslp lqyewqklsd
      181 sqkmptswla emtssvisvk nasseysgty sctvrnrvgs dqcllrlnvv ppsnkaglia
      241 gaiigtllal aligliifcc rkkrreekye kevhhdired vpppksrtst arsyigsnhs
      301 slgsmspsnm egysktqynq vpsedfertp qsptlppakf kypyktdgit vv
//
LOCUS       NP_001363698             552 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 28 [Homo sapiens].
ACCESSION   NP_001363698 XP_016864156
VERSION     NP_001363698.1
DBSOURCE    REFSEQ: accession NM_001376769.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Muckenfuss,L.M., Migenda Herranz,A.C., Boneberg,F.M., Clerici,M.
            and Jinek,M.
  TITLE     Fip1 is a multivalent interaction scaffold for processing factors
            in human mRNA 3' end biogenesis
  JOURNAL   Elife 11, e80332 (2022)
   PUBMED   36073787
  REMARK    GeneRIF: Fip1 is a multivalent interaction scaffold for processing
            factors in human mRNA 3' end biogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Tennenbaum,J., Groh,M., Venditti,L., Campos-Gazeau,F., Chalayer,E.,
            De Broucker,T., Hamidou,M., Hunault,M., Lyoubi,A., Meunier,R.,
            Muron,T., Sene,D., Slama,B., Guidoux,C., Lefevre,G., Kahn,J.E.,
            Denier,C. and Rohmer,J.
  TITLE     FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a Treatable
            Cause of Watershed Infarction
  JOURNAL   Stroke 52 (10), e605-e609 (2021)
   PUBMED   34304603
  REMARK    GeneRIF: FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a
            Treatable Cause of Watershed Infarction.
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 552)
  AUTHORS   Helbig,G., Lewandowski,K., Swiderska,A., Rodzaj,M., Seferynska,I.
            and Gajkowska-Kulik,J.
  TITLE     Exquisite response to imatinib mesylate in FIP1L1-PDGFRA-mutated
            hypereosinophilic syndrome: a 12-year experience of the Polish
            Hypereosinophilic Syndrome Study Group
  JOURNAL   Pol Arch Intern Med 130 (3), 255-257 (2020)
   PUBMED   32125294
  REMARK    GeneRIF: Exquisite response to imatinib mesylate in
            FIP1L1-PDGFRA-mutated hypereosinophilic syndrome: a 12-year
            experience of the Polish Hypereosinophilic Syndrome Study Group.
REFERENCE   6  (residues 1 to 552)
  AUTHORS   Cools,J., Quentmeier,H., Huntly,B.J., Marynen,P., Griffin,J.D.,
            Drexler,H.G. and Gilliland,D.G.
  TITLE     The EOL-1 cell line as an in vitro model for the study of
            FIP1L1-PDGFRA-positive chronic eosinophilic leukemia
  JOURNAL   Blood 103 (7), 2802-2805 (2004)
   PUBMED   14630792
  REMARK    GeneRIF: results indicate that the fusion of FIP1L1 to PDGFRA
            occurs rarely in leukemia cell lines
REFERENCE   7  (residues 1 to 552)
  AUTHORS   Kaufmann,I., Martin,G., Friedlein,A., Langen,H. and Keller,W.
  TITLE     Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements
            and stimulates poly(A) polymerase
  JOURNAL   EMBO J 23 (3), 616-626 (2004)
   PUBMED   14749727
REFERENCE   8  (residues 1 to 552)
  AUTHORS   Pardanani,A., Ketterling,R.P., Brockman,S.R., Flynn,H.C.,
            Paternoster,S.F., Shearer,B.M., Reeder,T.L., Li,C.Y., Cross,N.C.,
            Cools,J., Gilliland,D.G., Dewald,G.W. and Tefferi,A.
  TITLE     CHIC2 deletion, a surrogate for FIP1L1-PDGFRA fusion, occurs in
            systemic mastocytosis associated with eosinophilia and predicts
            response to imatinib mesylate therapy
  JOURNAL   Blood 102 (9), 3093-3096 (2003)
   PUBMED   12842979
  REMARK    GeneRIF: observations suggest that the FIP1L1-PDGFRA rearrangement
            occurs in an early hematopoietic progenitor and suggests that the
            molecular pathogenesis for a subset of SMCD patients is similar to
            that of HES
REFERENCE   9  (residues 1 to 552)
  AUTHORS   Griffin,J.H., Leung,J., Bruner,R.J., Caligiuri,M.A. and
            Briesewitz,R.
  TITLE     Discovery of a fusion kinase in EOL-1 cells and idiopathic
            hypereosinophilic syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (13), 7830-7835 (2003)
   PUBMED   12808148
REFERENCE   10 (residues 1 to 552)
  AUTHORS   Cools,J., DeAngelo,D.J., Gotlib,J., Stover,E.H., Legare,R.D.,
            Cortes,J., Kutok,J., Clark,J., Galinsky,I., Griffin,J.D.,
            Cross,N.C., Tefferi,A., Malone,J., Alam,R., Schrier,S.L.,
            Schmid,J., Rose,M., Vandenberghe,P., Verhoef,G., Boogaerts,M.,
            Wlodarska,I., Kantarjian,H., Marynen,P., Coutre,S.E., Stone,R. and
            Gilliland,D.G.
  TITLE     A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes
            as a therapeutic target of imatinib in idiopathic hypereosinophilic
            syndrome
  JOURNAL   N Engl J Med 348 (13), 1201-1214 (2003)
   PUBMED   12660384
  REMARK    GeneRIF: The hypereosinophilic syndrome may result from a novel
            fusion tyrosine kinase - FIP1L1-PDGFRalpha - that is a consequence
            of an interstitial chromosomal deletion.
            GeneRIF: Describes the fusion gene Fip1-like-1-PDGFRalpha in
            patients with idiopathic hypereosinophilic syndrome, mostly
            responsive to imatinib therapy.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098821.3 and AC058822.6.
            
            On Nov 20, 2019 this sequence version replaced XP_016864156.1.
            
            Summary: This gene encodes a subunit of the CPSF (cleavage and
            polyadenylation specificity factor) complex that polyadenylates the
            3' end of mRNA precursors. This gene, the homolog of yeast Fip1
            (factor interacting with PAP), binds to U-rich sequences of
            pre-mRNA and stimulates poly(A) polymerase activity. Its N-terminus
            contains a PAP-binding site and its C-terminus an RNA-binding
            domain. An interstitial chromosomal deletion on 4q12 creates an
            in-frame fusion of human genes FIP1L1 and PDGFRA (platelet-derived
            growth factor receptor, alpha). The FIP1L1-PDGFRA fusion gene
            encodes a constitutively activated tyrosine kinase that joins the
            first 233 amino acids of FIP1L1 to the last 523 amino acids of
            PDGFRA. This gene fusion and chromosomal deletion is the cause of
            some forms of idiopathic hypereosinophilic syndrome (HES). This
            syndrome, recently reclassified as chronic eosinophilic leukemia
            (CEL), is responsive to treatment with tyrosine kinase inhibitors.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1339504.1,
                                           SRR3476690.841036.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..552
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     28"
                     /note="rearranged in hypereosinophilia; pre-mRNA
                     3'-end-processing factor FIP1; FIP1-like 1 protein; factor
                     interacting with PAP; FIP1 like 1; FIP1L1 cleavage and
                     polyadenylation specific factor subunit"
                     /calculated_mol_wt=61671
     Region          139..181
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     CDS             1..552
                     /gene="FIP1L1"
                     /gene_synonym="FIP1; hFip1; Rhe"
                     /coded_by="NM_001376769.1:199..1857"
                     /note="isoform 28 is encoded by transcript variant 28"
                     /db_xref="CCDS:CCDS93516.1"
                     /db_xref="GeneID:81608"
                     /db_xref="HGNC:HGNC:19124"
                     /db_xref="MIM:607686"
ORIGIN      
        1 msageverlv selsggtggd eeeewlygde neverpeeen asanppsgie detaengvpk
       61 pkvtetedds dsdsdddedd vhvtigdikt gapqygsygt apvnlniktg grvygttgtk
      121 vkgvdldapg singvpllev dldsfedkpw rkpgadlsdy fnygfnedtw kaycekqkri
      181 rmglevipvt sttnkitaed ctmevtpgae iqdgrfnlfk vqqgrtgnse ketalpstka
      241 eftsppslfk tglppsrrlp gaidvigqti tisrvegrrr anensniqvl sersatevdn
      301 nfskpppffp pgappthlpp ppflpppptv stapplippp gipitvpppg fppppgappp
      361 sliptiesgh ssgydsrsar afpygnvafp hlpgsapswp slvdtskqwd yyarrekdrd
      421 rerdrdrerd rdrdrerert rerererdhs ptpsvfnsde eryryreyae rgyerhrasr
      481 ekeerhrerr hrekeetrhk ssrsnsrrrh eseegdshrr hkhkkskrsk egkeagsepa
      541 peqesteatp ae
//
LOCUS       NP_001155056             913 aa            linear   PRI 21-NOV-2025
DEFINITION  testis-expressed protein 10 isoform 2 [Homo sapiens].
ACCESSION   NP_001155056
VERSION     NP_001155056.1
DBSOURCE    REFSEQ: accession NM_001161584.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Gordon,J., Chapus,F.L., Viverette,E.G., Williams,J.G.,
            Deterding,L.J., Krahn,J.M., Borgnia,M.J., Rodriguez,J., Warren,A.J.
            and Stanley,R.E.
  TITLE     Cryo-EM reveals the architecture of the PELP1-WDR18 molecular
            scaffold
  JOURNAL   Nat Commun 13 (1), 6783 (2022)
   PUBMED   36351913
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Zhou,H., Stein,C.B., Shafiq,T.A., Shipkovenska,G., Kalocsay,M.,
            Paulo,J.A., Zhang,J., Luo,Z., Gygi,S.P., Adelman,K. and Moazed,D.
  TITLE     Rixosomal RNA degradation contributes to silencing of Polycomb
            target genes
  JOURNAL   Nature 604 (7904), 167-174 (2022)
   PUBMED   35355014
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Liang,J.H., Xu,Q.D. and Gu,S.G.
  TITLE     LncRNA RSU1P2-microRNA let-7a-Testis-Expressed Protein 10 axis
            modulates tumorigenesis and cancer stem cell-like properties in
            liver cancer
  JOURNAL   Bioengineered 13 (2), 4285-4300 (2022)
   PUBMED   35156514
  REMARK    GeneRIF: LncRNA RSU1P2-microRNA let-7a-Testis-Expressed Protein 10
            axis modulates tumorigenesis and cancer stem cell-like properties
            in liver cancer.
REFERENCE   4  (residues 1 to 913)
  AUTHORS   Luo,S., Wang,W., Feng,J. and Li,R.
  TITLE     TEX10 Promotes the Tumorigenesis and Radiotherapy Resistance of
            Urinary Bladder Carcinoma by Stabilizing XRCC6
  JOURNAL   J Immunol Res 2021, 5975893 (2021)
   PUBMED   34966825
  REMARK    GeneRIF: TEX10 Promotes the Tumorigenesis and Radiotherapy
            Resistance of Urinary Bladder Carcinoma by Stabilizing XRCC6.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 913)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 913)
  AUTHORS   Ding,J., Huang,X., Shao,N., Zhou,H., Lee,D.F., Faiola,F.,
            Fidalgo,M., Guallar,D., Saunders,A., Shliaha,P.V., Wang,H.,
            Waghray,A., Papatsenko,D., Sanchez-Priego,C., Li,D., Yuan,Y.,
            Lemischka,I.R., Shen,L., Kelley,K., Deng,H., Shen,X. and Wang,J.
  TITLE     Tex10 Coordinates Epigenetic Control of Super-Enhancer Activity in
            Pluripotency and Reprogramming
  JOURNAL   Cell Stem Cell 16 (6), 653-668 (2015)
   PUBMED   25936917
  REMARK    GeneRIF: Tex10 is a core component of the pluripotency network.
REFERENCE   7  (residues 1 to 913)
  AUTHORS   Fanis,P., Gillemans,N., Aghajanirefah,A., Pourfarzad,F.,
            Demmers,J., Esteghamat,F., Vadlamudi,R.K., Grosveld,F.,
            Philipsen,S. and van Dijk,T.B.
  TITLE     Five friends of methylated chromatin target of
            protein-arginine-methyltransferase[prmt]-1 (chtop), a complex
            linking arginine methylation to desumoylation
  JOURNAL   Mol Cell Proteomics 11 (11), 1263-1273 (2012)
   PUBMED   22872859
  REMARK    GeneRIF: Recruitment of the protein complex 5FMC to Zbp-89, a
            zinc-finger transcription factor, affects its sumoylation status
            and transactivation potential.[5FMC]
REFERENCE   8  (residues 1 to 913)
  AUTHORS   Yoshitake,H., Yokoi,H., Ishikawa,H., Maruyama,M., Endo,S.,
            Nojima,M., Yoshida,K., Yoshikawa,H., Suzuki,F., Takamori,K.,
            Fujiwara,H. and Araki,Y.
  TITLE     Overexpression of TEX101, a potential novel cancer marker, in head
            and neck squamous cell carcinoma
  JOURNAL   Cancer Biomark 12 (3), 141-148 (2012)
   PUBMED   23481573
  REMARK    GeneRIF: Data suggest that TEX101 is a cancer-related protein and
            may be useful as a marker for prognosis/diagnosis of and neck
            squamous cell carcinomas (HNSCC).
REFERENCE   9  (residues 1 to 913)
  AUTHORS   Finkbeiner,E., Haindl,M. and Muller,S.
  TITLE     The SUMO system controls nucleolar partitioning of a novel
            mammalian ribosome biogenesis complex
  JOURNAL   EMBO J 30 (6), 1067-1078 (2011)
   PUBMED   21326211
  REMARK    GeneRIF: These data define the PELP1-TEX10-WDR18 complex as a
            regulator of ribosome biogenesis and suggests that its
            SUMO-controlled distribution coordinates the rate of ribosome
            formation.
REFERENCE   10 (residues 1 to 913)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK302619.1 and AA436854.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR and has
            multiple coding region differences, compared to variant 1. These
            differences causes translation initiation at an alternate AUG and
            result in an isoform (2) that is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302619.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.1"
     Protein         1..913
                     /product="testis-expressed protein 10 isoform 2"
                     /note="testis expressed gene 10; testis-expressed sequence
                     10 protein; testis-expressed protein 10"
                     /calculated_mol_wt=103784
     Region          135..238
                     /region_name="Ipi1_N"
                     /note="Rix1 complex component involved in 60S ribosome
                     maturation; pfam12333"
                     /db_xref="CDD:463535"
     CDS             1..913
                     /gene="TEX10"
                     /gene_synonym="bA208F1.2; Ipi1"
                     /coded_by="NM_001161584.2:151..2892"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55330.1"
                     /db_xref="GeneID:54881"
                     /db_xref="HGNC:HGNC:25988"
                     /db_xref="MIM:616717"
ORIGIN      
        1 msrmtkkrkr qhdfqkvklk vgkkkpklqn atptnfktkt ihlpeqlked gtlptnnrkl
       61 nikdllsqmh hynagvkqsa llglkdllsq ypfiidahls nilsevtavf tdkdanvrla
      121 avqllqflap kiraeqispf fplvsahlss amthitegiq edslkvldil leqypalitg
      181 rssillknfv elishqqlsk glinrdrsqs wilsvnpnrr ltsqqwrlkv lvrlskflqa
      241 ladgssrlre seglqeqken phatsnsifi nwkehandqq hiqvyenggs qpnvssqfrl
      301 rylvgglsgv deglsstenl kgfieiiipl liecwveavp pqlatpvgng iereplqvmq
      361 qvlniisllw klskqqdeth kleswlrkny lidfkhhfms rfpyvlkeit khkrkepnks
      421 ikhctvlsnn idhlllnltl sdimvslana stlqkdcswi emirkfvtet ledgsrlnsk
      481 qlnrllgvsw rlmqiqpnre dtetlikavy tlyqqrglil pvrtlllkff skiyqteelr
      541 scrfryrskv lsrwlaglpl qlahlgsrnp elstqlidii htaaaranke llkslqatal
      601 riydpqegav vvlpadsqqr lvqlvyflps lpadllsrls rccimgrlss slaamligil
      661 hmrssfsgwk ysakdwlmsd vdyfsflfst ltgfskeelt wlqslrgvph viqtqlspvl
      721 lyltdldqfl hhwdvteavf hsllvipars qnfdilqsai skhlvgltvi pdstagcvfg
      781 vicklldhtc vvsetllpfl asccysllyf lltiekgeae hlrkrlmlqs lrvnrvgpee
      841 lpvvgqllrl llqhaplrth mltnailvqq iiknittlks gsvqeqwltd lhycfnvyit
      901 ghpqgpsala tvy
//
LOCUS       NP_001337364             995 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 1 isoform 31 [Homo
            sapiens].
ACCESSION   NP_001337364
VERSION     NP_001337364.1
DBSOURCE    REFSEQ: accession NM_001350435.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 995)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 995)
  AUTHORS   Ruhle,F., Witten,A., Barysenka,A., Huge,A., Arning,A., Heller,C.,
            Krumpel,A., Mesters,R., Franke,A., Lieb,W., Riemenschneider,M.,
            Hiersche,M., Limperger,V., Nowak-Gottl,U. and Stoll,M.
  TITLE     Rare genetic variants in SMAP1, B3GAT2, and RIMS1 contribute to
            pediatric venous thromboembolism
  JOURNAL   Blood 129 (6), 783-790 (2017)
   PUBMED   28011674
  REMARK    GeneRIF: The study identified a region on chromosome 6 comprising
            the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus
            for pediatric venous thromboembolism.
REFERENCE   6  (residues 1 to 995)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 995)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
REFERENCE   8  (residues 1 to 995)
  AUTHORS   Schoch,S., Castillo,P.E., Jo,T., Mukherjee,K., Geppert,M., Wang,Y.,
            Schmitz,F., Malenka,R.C. and Sudhof,T.C.
  TITLE     RIM1alpha forms a protein scaffold for regulating neurotransmitter
            release at the active zone
  JOURNAL   Nature 415 (6869), 321-326 (2002)
   PUBMED   11797009
REFERENCE   9  (residues 1 to 995)
  AUTHORS   Coppola,T., Magnin-Luthi,S., Perret-Menoud,V., Gattesco,S.,
            Schiavo,G. and Regazzi,R.
  TITLE     Direct interaction of the Rab3 effector RIM with Ca2+ channels,
            SNAP-25, and synaptotagmin
  JOURNAL   J Biol Chem 276 (35), 32756-32762 (2001)
   PUBMED   11438518
REFERENCE   10 (residues 1 to 995)
  AUTHORS   Betz,A., Thakur,P., Junge,H.J., Ashery,U., Rhee,J.S., Scheuss,V.,
            Rosenmund,C., Rettig,J. and Brose,N.
  TITLE     Functional interaction of the active zone proteins Munc13-1 and
            RIM1 in synaptic vesicle priming
  JOURNAL   Neuron 30 (1), 183-196 (2001)
   PUBMED   11343654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590011.5, AL445256.18 and
            AL035633.18.
            
            Summary: The protein encoded by this gene is a RAS gene superfamily
            member that regulates synaptic vesicle exocytosis. This gene also
            plays a role in the regulation of voltage-gated calcium channels
            during neurotransmitter and insulin release. Mutations have
            suggested a role cognition and have been identified as the cause of
            cone-rod dystrophy type 7. Multiple transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Mar 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.196696.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..995
                     /product="regulating synaptic membrane exocytosis protein
                     1 isoform 31"
                     /note="RAB3-interacting protein 2; rab3-interacting
                     molecule 1; rab-3-interacting protein 2"
                     /calculated_mol_wt=111071
     Region          68..164
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(89..95,110,113,143,147,150..151)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          216..342
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(247,253,308,310,318)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          345..>562
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          826..971
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(883,887..888,890,893,921,923,925,969..970)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..995
                     /gene="RIMS1"
                     /gene_synonym="CORD7; RAB3IP2; RIM; RIM1"
                     /coded_by="NM_001350435.2:231..3218"
                     /note="isoform 31 is encoded by transcript variant 31"
                     /db_xref="GeneID:22999"
                     /db_xref="HGNC:HGNC:17282"
                     /db_xref="MIM:606629"
ORIGIN      
        1 mcapgihvss egweevrsvd seegtiearr avagdldyyw ldpatwhsre tspisshpvt
       61 wqpskegdrl igrvilnkrt tmpkdsgall glkvvggkmt dlgrlgafit kvkkgsladv
      121 vghlragdev lewngkplpg atneevynii lesksepqve iivsrpigdi pripesshpp
      181 lesssssfes qkmerpsisv isptspgalk dapqvlpgql svklwydkvg hqlivnvlqa
      241 tdlparvdgr prnpyvkmyf lpdrsdkskr rtktvkkile pkwnqtfvys hvhrrdfrer
      301 mleitvwdqp rvqeeesefl geilieleta llddephwyk lqthdesslp lpqpspfmpr
      361 rhihgesssk klqrsqrisd sdisdyevdd gigvvppgyr ssareskstt ltvpeqqrtt
      421 hhrsrsvsph rgndqgkprs rlpnvplqrs ldeihptrrs rsptrhhdas rspvdhrtrd
      481 vdsqylseqd selqpfldra rsastnclrp dtslhspere rgrwspsldr rrppspriqi
      541 qhaspendrm hrqrsptqsp padtsfssrr grqlpqvpvr sgsieqaslv veertrqmkm
      601 kvhrfkqttg sgssqeldre qyskynihkd qyrscdnvsa kssdsdvsdv saisrtssas
      661 rlsstsfmse qserprgris sftpkmqgrr mgtsgrsimk stsvsgemyt lehndgsqsd
      721 tavgtvgagg kkrrsslsak vvaivsrrsr stsqlsqtes ghkklkstiq rstetgmaae
      781 mrkmvrqpsr estdgsinsy ssegnlifpg vrlgadsqfs dfldglgpaq lvgrqtlatp
      841 amgdiqigme dkkgqlevev irarsltqkp gskstpapyv kvyllengac iakkktriar
      901 ktldplyqqs lvfdespqgk vlqvivwgdy grmdhkcfmg vaqilleeld lssmvigwyk
      961 lfppsslvdp tltpltrras qsslesstgp pcirs
//
LOCUS       NP_008945                870 aa            linear   PRI 21-NOV-2025
DEFINITION  NEDD4-like E3 ubiquitin-protein ligase WWP2 isoform WWP2-FL [Homo
            sapiens].
ACCESSION   NP_008945
VERSION     NP_008945.2
DBSOURCE    REFSEQ: accession NM_007014.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 870)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 870)
  AUTHORS   Wang,H., Lian,X., Wang,K. and Wang,S.
  TITLE     WWP2 binds to NKRF, enhances the NF-kappaB signaling, and promotes
            malignant phenotypes of acute myeloid leukemia cells
  JOURNAL   Biochem Cell Biol 102 (1), 85-95 (2024)
   PUBMED   37921219
  REMARK    GeneRIF: WWP2 binds to NKRF, enhances the NF-kappaB signaling, and
            promotes malignant phenotypes of acute myeloid leukemia cells.
REFERENCE   3  (residues 1 to 870)
  AUTHORS   Lee,K.T., Pranoto,I.K.A., Kim,S.Y., Choi,H.J., To,N.B., Chae,H.,
            Lee,J.Y., Kim,J.E., Kwon,Y.V. and Nam,J.W.
  TITLE     Comparative interactome analysis of alpha-arrestin families in
            human and Drosophila
  JOURNAL   Elife 12, 88328 (2024)
   PUBMED   38270169
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 870)
  AUTHORS   Chantry,A.
  TITLE     WWP2 ubiquitin ligase and its isoforms: new biological insight and
            promising disease targets
  JOURNAL   Cell Cycle 10 (15), 2437-2439 (2011)
   PUBMED   21750408
REFERENCE   5  (residues 1 to 870)
  AUTHORS   Soond,S.M. and Chantry,A.
  TITLE     Selective targeting of activating and inhibitory Smads by distinct
            WWP2 ubiquitin ligase isoforms differentially modulates TGFbeta
            signalling and EMT
  JOURNAL   Oncogene 30 (21), 2451-2462 (2011)
   PUBMED   21258410
  REMARK    GeneRIF: Data show that the WWP2-N isoform interacts with Smad2 and
            Smad3, whereas WWP2-C interacts only with Smad7.
REFERENCE   6  (residues 1 to 870)
  AUTHORS   McDonald,F.J., Western,A.H., McNeil,J.D., Thomas,B.C., Olson,D.R.
            and Snyder,P.M.
  TITLE     Ubiquitin-protein ligase WWP2 binds to and downregulates the
            epithelial Na(+) channel
  JOURNAL   Am J Physiol Renal Physiol 283 (3), F431-F436 (2002)
   PUBMED   12167593
  REMARK    GeneRIF: expression, binding, and functional data all suggest that
            WWP2 is a candidate to regulate ENaC-mediated Na(+) transport in
            epithelia
REFERENCE   7  (residues 1 to 870)
  AUTHORS   Harvey,K.F., Shearwin-Whyatt,L.M., Fotia,A., Parton,R.G. and
            Kumar,S.
  TITLE     N4WBP5, a potential target for ubiquitination by the Nedd4 family
            of proteins, is a novel Golgi-associated protein
  JOURNAL   J Biol Chem 277 (11), 9307-9317 (2002)
   PUBMED   11748237
REFERENCE   8  (residues 1 to 870)
  AUTHORS   Wood,J.D., Yuan,J., Margolis,R.L., Colomer,V., Duan,K., Kushi,J.,
            Kaminsky,Z., Kleiderlein,J.J., Sharp,A.H. and Ross,C.A.
  TITLE     Atrophin-1, the DRPLA gene product, interacts with two families of
            WW domain-containing proteins
  JOURNAL   Mol Cell Neurosci 11 (3), 149-160 (1998)
   PUBMED   9647693
REFERENCE   9  (residues 1 to 870)
  AUTHORS   Jonsson,A.B.
  TITLE     Identification of a human cDNA clone that mediates adherence of
            pathogenic Neisseria to non-binding cells
  JOURNAL   FEMS Microbiol Lett 162 (1), 25-30 (1998)
   PUBMED   9595660
REFERENCE   10 (residues 1 to 870)
  AUTHORS   Pirozzi,G., McConnell,S.J., Uveges,A.J., Carter,J.M., Sparks,A.B.,
            Kay,B.K. and Fowlkes,D.M.
  TITLE     Identification of novel human WW domain-containing proteins by
            cloning of ligand targets
  JOURNAL   J Biol Chem 272 (23), 14611-14616 (1997)
   PUBMED   9169421
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC402912.1, U96114.2 and
            JN712744.1.
            
            On Jan 13, 2004 this sequence version replaced NP_008945.1.
            
            Summary: This gene encodes a member of the Nedd4 family of E3
            ligases, which play an important role in protein ubiquitination.
            The encoded protein contains four WW domains and may play a role in
            multiple processes including chondrogenesis and the regulation of
            oncogenic signaling pathways via interactions with Smad proteins
            and the tumor suppressor PTEN. Alternatively spliced transcript
            variants encoding multiple isoforms have been observed for this
            gene, and a pseudogene of this gene is located on the long arm of
            chromosome 10. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (WWP2-FL). Variants 1
            and 5 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.199885.1,
                                           SRR1803612.84429.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..870
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..870
                     /product="NEDD4-like E3 ubiquitin-protein ligase WWP2
                     isoform WWP2-FL"
                     /EC_number="2.3.2.26"
                     /note="atrophin-1 interacting protein 2; NEDD4-like E3
                     ubiquitin-protein ligase WWP2; HECT-type E3 ubiquitin
                     transferase WWP2"
                     /calculated_mol_wt=98781
     Region          17..142
                     /region_name="C2_E3_ubiquitin_ligase"
                     /note="C2 domain present in E3 ubiquitin ligase; cd04021"
                     /db_xref="CDD:175988"
     Region          151..299
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00308.2)"
     Region          <164..343
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O00308.2)"
     Region          302..331
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          332..361
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          407..435
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          447..477
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(461,472)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          516..868
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(521,551,562,623,797,832..833,836..840,860,867)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(651,654..655,657..658,661,668,670,673..674,676,682,
                     687,704,708)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..870
                     /gene="WWP2"
                     /gene_synonym="AIP2; WWp2-like"
                     /coded_by="NM_007014.5:129..2741"
                     /note="isoform WWP2-FL is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10885.1"
                     /db_xref="GeneID:11060"
                     /db_xref="HGNC:HGNC:16804"
                     /db_xref="MIM:602308"
ORIGIN      
        1 masasssrag valpfeksql tlkvvsakpk vhnrqprins yvevavdglp setkktgkri
       61 gssellwnei iilnvtaqsh ldlkvwscht lrnellgtas vnlsnvlknn ggkmenmqlt
      121 lnlqtenkgs vvsggeltif ldgptvdlgn vpngsaltdg sqlpsrdssg tavapenrhq
      181 ppstncfggr srthrhsgas arttpatgeq spgarsrhrq pvknsghsgl angtvndept
      241 tatdpeepsv vgvtsppaap lsvtpnpntt slpapatpae geepstsgtq qlpaaaqapd
      301 alpagweqre lpngrvyyvd hntktttwer plppgwekrt dprgrfyyvd hntrtttwqr
      361 ptaeyvrnye qwqsqrnqlq gamqhfsqrf lyqsssastd hdplgplppg wekrqdngrv
      421 yyvnhntrtt qwedprtqgm iqepalppgw emkytsegvr yfvdhntrtt tfkdprpgfe
      481 sgtkqgspga ydrsfrwkyh qfrflchsna lpshvkisvs rqtlfedsfq qimnmkpydl
      541 rrrlyiimrg eegldyggia rewffllshe vlnpmyclfe yagknnyclq inpassinpd
      601 hltyfrfigr fiamalyhgk fidtgftlpf ykrmlnkrpt lkdlesidpe fynsivwike
      661 nnleecglel yfiqdmeilg kvtthelkeg gesirvteen keeyimlltd wrftrgveeq
      721 tkafldgfne vaplewlryf dekelelmlc gmqeidmsdw qkstiyrhyt knskqiqwfw
      781 qvvkemdnek rirllqfvtg tcrlpvggfa eligsngpqk fcidkvgket wlprshtcfn
      841 rldlppyksy eqlrekllya ieetegfgqe
//
LOCUS       NP_001316422             306 aa            linear   PRI 21-NOV-2025
DEFINITION  ER membrane protein complex subunit 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001316422
VERSION     NP_001316422.1
DBSOURCE    REFSEQ: accession NM_001329493.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Pleiner,T., Hazu,M., Tomaleri,G.P., Januszyk,K., Oania,R.S.,
            Sweredoski,M.J., Moradian,A., Guna,A. and Voorhees,R.M.
  TITLE     WNK1 is an assembly factor for the human ER membrane protein
            complex
  JOURNAL   Mol Cell 81 (13), 2693-2704 (2021)
   PUBMED   33964204
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Pleiner,T., Tomaleri,G.P., Januszyk,K., Inglis,A.J., Hazu,M. and
            Voorhees,R.M.
  TITLE     Structural basis for membrane insertion by the human ER membrane
            protein complex
  JOURNAL   Science 369 (6502), 433-436 (2020)
   PUBMED   32439656
REFERENCE   6  (residues 1 to 306)
  AUTHORS   Guna,A., Volkmar,N., Christianson,J.C. and Hegde,R.S.
  TITLE     The ER membrane protein complex is a transmembrane domain insertase
  JOURNAL   Science 359 (6374), 470-473 (2018)
   PUBMED   29242231
REFERENCE   7  (residues 1 to 306)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 306)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   9  (residues 1 to 306)
  AUTHORS   Ma,H., Dang,Y., Wu,Y., Jia,G., Anaya,E., Zhang,J., Abraham,S.,
            Choi,J.G., Shi,G., Qi,L., Manjunath,N. and Wu,H.
  TITLE     A CRISPR-Based Screen Identifies Genes Essential for
            West-Nile-Virus-Induced Cell Death
  JOURNAL   Cell Rep 12 (4), 673-683 (2015)
   PUBMED   26190106
REFERENCE   10 (residues 1 to 306)
  AUTHORS   Christianson,J.C., Olzmann,J.A., Shaler,T.A., Sowa,M.E.,
            Bennett,E.J., Richter,C.M., Tyler,R.E., Greenblatt,E.J.,
            Harper,J.W. and Kopito,R.R.
  TITLE     Defining human ERAD networks through an integrative mapping
            strategy
  JOURNAL   Nat Cell Biol 14 (1), 93-105 (2011)
   PUBMED   22119785
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP002088.2 and AC022634.8.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2881019.1,
                                           SRR14038195.167062.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q23.1"
     Protein         1..306
                     /product="ER membrane protein complex subunit 2 isoform 1"
                     /note="tetratricopeptide repeat protein 35; TPR repeat
                     protein 35; tetratricopeptide repeat domain 35"
                     /calculated_mol_wt=35845
     Region          64..>244
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Site            order(104..105,107,131,134..135,138..139,141..142,165,
                     168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          129..159
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          164..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          197..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..306
                     /gene="EMC2"
                     /gene_synonym="KIAA0103; TTC35"
                     /coded_by="NM_001329493.2:36..956"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:9694"
                     /db_xref="HGNC:HGNC:28963"
                     /db_xref="MIM:607722"
ORIGIN      
        1 makvselydv tweemrdkmr kwreensrns eqivevgeel ineyasklgd diffplyvyl
       61 vwiiyeqvmi aaldygrddl alfclqelrr qfpgshrvkr ltgmrfeame ryddaiqlyd
      121 rilqedptnt aarkrkiair kaqgknveai relneyleqf vgdqeawhel aelyinehdy
      181 akaafcleel mmtnphnhly cqqyaevkyt qgglenlels rkyfaqalkl nnrnmralfg
      241 lymsashias npkasaktkk dnmkyaswaa sqinrayqfa grskketkys lkavedmlet
      301 lqitqs
//
LOCUS       NP_001095124             660 aa            linear   PRI 21-NOV-2025
DEFINITION  CXXC-type zinc finger protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001095124
VERSION     NP_001095124.1
DBSOURCE    REFSEQ: accession NM_001101654.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Li,C., Zhang,Y., Shen,J., Bao,H., Zhao,Y., Li,D., Li,S., Liu,Y.,
            Yang,J., Zhou,Z., Gao,K., Zhao,L., Pei,Y., Lu,Y., Pan,Z. and Cai,B.
  TITLE     Cfp1 Controls Cardiomyocyte Maturation by Modifying Histone H3K4me3
            of Structural, Metabolic, and Contractile Related Genes
  JOURNAL   Adv Sci (Weinh) 11 (11), e2305992 (2024)
   PUBMED   38196272
  REMARK    GeneRIF: Cfp1 Controls Cardiomyocyte Maturation by Modifying
            Histone H3K4me3 of Structural, Metabolic, and Contractile Related
            Genes.
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Yang,S.C., Park,M., Hong,K.H., La,H., Park,C., Wang,P., Li,G.,
            Chen,Q., Choi,Y., DeMayo,F.J., Lydon,J.P., Skalnik,D.G., Lim,H.J.,
            Hong,S.H., Park,S.H., Kim,Y.S., Kim,H.R. and Song,H.
  TITLE     CFP1 governs uterine epigenetic landscapes to intervene in
            progesterone responses for uterine physiology and suppression of
            endometriosis
  JOURNAL   Nat Commun 14 (1), 3220 (2023)
   PUBMED   37270588
  REMARK    GeneRIF: CFP1 governs uterine epigenetic landscapes to intervene in
            progesterone responses for uterine physiology and suppression of
            endometriosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Yang,L.Q., Hu,H.Y., Han,Y., Tang,Z.Y., Gao,J., Zhou,Q.Y., Liu,Y.X.,
            Chen,H.S., Xu,T.N., Ao,L., Xu,Y., Che,X., Jiang,Y.B., Xu,C.W.,
            Zhang,X.C., Jiang,Y.X., Heger,M., Wang,X.M., Cheng,S.Q. and
            Pan,W.W.
  TITLE     CpG-binding protein CFP1 promotes ovarian cancer cell proliferation
            by regulating BST2 transcription
  JOURNAL   Cancer Gene Ther 29 (12), 1895-1907 (2022)
   PUBMED   35864225
  REMARK    GeneRIF: CpG-binding protein CFP1 promotes ovarian cancer cell
            proliferation by regulating BST2 transcription.
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Yang,Y., Yang,Y., Chan,K. and Couture,J.F.
  TITLE     Analyzing the impact of CFP1 mutational landscape on epigenetic
            signaling
  JOURNAL   FASEB J 35 (8), e21790 (2021)
   PUBMED   34320252
  REMARK    GeneRIF: Analyzing the impact of CFP1 mutational landscape on
            epigenetic signaling.
            Review article
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Lee,J.H., Voo,K.S. and Skalnik,D.G.
  TITLE     Identification and characterization of the DNA binding domain of
            CpG-binding protein
  JOURNAL   J Biol Chem 276 (48), 44669-44676 (2001)
   PUBMED   11572867
REFERENCE   7  (residues 1 to 660)
  AUTHORS   Carlone,D.L. and Skalnik,D.G.
  TITLE     CpG binding protein is crucial for early embryonic development
  JOURNAL   Mol Cell Biol 21 (22), 7601-7606 (2001)
   PUBMED   11604496
REFERENCE   8  (residues 1 to 660)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 660)
  AUTHORS   Fujino,T., Hasegawa,M., Shibata,S., Kishimoto,T., Imai,S. and
            Takano,T.
  TITLE     PCCX1, a novel DNA-binding protein with PHD finger and CXXC domain,
            is regulated by proteolysis
  JOURNAL   Biochem Biophys Res Commun 271 (2), 305-310 (2000)
   PUBMED   10799292
REFERENCE   10 (residues 1 to 660)
  AUTHORS   Voo,K.S., Carlone,D.L., Jacobsen,B.M., Flodin,A. and Skalnik,D.G.
  TITLE     Cloning of a mammalian transcriptional activator that binds
            unmethylated CpG motifs and shares a CXXC domain with DNA
            methyltransferase, human trithorax, and methyl-CpG binding domain
            protein 1
  JOURNAL   Mol Cell Biol 20 (6), 2108-2121 (2000)
   PUBMED   10688657
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB031069.1 and BC015733.1.
            
            Summary: This gene encodes a protein that functions as a
            transcriptional activator that binds specifically to non-methylated
            CpG motifs through its CXXC domain. The protein is a component of
            the SETD1 complex, regulates gene expression and is essential for
            vertebrate development. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC015733.1, SRR11853563.15748.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..660
                     /product="CXXC-type zinc finger protein 1 isoform 1"
                     /note="DNA-binding protein with PHD finger and CXXC
                     domain; CXXC finger 1 (PHD domain); zinc finger, CpG
                     binding-type containing 1; CpG binding protein;
                     cpG-binding protein; CXXC-type zinc finger protein 1; PHD
                     finger and CXXC domain-containing protein 1"
                     /calculated_mol_wt=76096
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Region          28..73
                     /region_name="PHD_Cfp1"
                     /note="PHD finger found in CXXC-type zinc finger protein 1
                     (Cfp1); cd15553"
                     /db_xref="CDD:277028"
     Site            order(28,39..43,47,68)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277028"
     Region          84..162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Region          162..208
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          219..287
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Region          404..640
                     /region_name="CpG_bind_C"
                     /note="CpG binding protein C-terminal domain; pfam12269"
                     /db_xref="CDD:463514"
     CDS             1..660
                     /gene="CXXC1"
                     /gene_synonym="2410002I16Rik; 5830420C16Rik; CFP1; CGBP;
                     hCGBP; HsT2645; PCCX1; PHF18; SPP1; ZCGPC1"
                     /coded_by="NM_001101654.2:104..2086"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45866.1"
                     /db_xref="GeneID:30827"
                     /db_xref="HGNC:HGNC:24343"
                     /db_xref="MIM:609150"
ORIGIN      
        1 megdgsdpep pdagedskse ngenapiyci crkpdincfm igcdncnewf hgdciritek
       61 makairewyc recrekdpkl eiryrhkksr erdgnerdss eprdegggrk rpvpdpdlqr
      121 ragsgtgvga mlargsasph ksspqplvat psqhhqqqqq qikrsarmcg eceacrrted
      181 cghcdfcrdm kkfggpnkir qkcrlrqcql raresykyfp sslspvtpse slprprrplp
      241 tqqqpqpsqk lgriredega vasstvkepp eatatpepls dedlpldpdl yqdfcagafd
      301 dhglpwmsdt eespfldpal rkravkvkhv krrekksekk vmerkeeryk rhrqkqkhkd
      361 kwkhperada kdpaslpqcl gpgcvrpaqp sskycsddcg mklaanriye ilpqriqqwq
      421 qspciaeehg kkllerirre qqsartrlqe merrfhelea iilrakqqav redeesnegd
      481 sddtdlqifc vscghpinpr valrhmercy akyesqtsfg smyptriega trlfcdvynp
      541 qsktyckrlq vlcpehsrdp kvpadevcgc plvrdvfelt gdfcrlpkrq cnrhycwekl
      601 rraevdlerv rvwykldelf eqernvrtam tnragllalm lhqtiqhdpl ttdlrssadr
//
LOCUS       NP_001128302            1196 aa            linear   PRI 21-NOV-2025
DEFINITION  jouberin isoform a [Homo sapiens].
ACCESSION   NP_001128302
VERSION     NP_001128302.1
DBSOURCE    REFSEQ: accession NM_001134830.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1196)
  AUTHORS   Sakrajda,K., Bilska,K., Czerski,P.M., Narozna,B.,
            Dmitrzak-Weglarz,M., Heilmann-Heimbach,S., Brockschmidt,F.F.,
            Herms,S., Nothen,M.M., Cichon,S., Wieckowska,B., Rybakowski,J.K.,
            Pawlak,J. and Szczepankiewicz,A.
  TITLE     Abelson Helper Integration Site 1 haplotypes and peripheral blood
            expression associates with lithium response and immunomodulation in
            bipolar patients
  JOURNAL   Psychopharmacology (Berl) 241 (4), 727-738 (2024)
   PUBMED   38036661
  REMARK    GeneRIF: Abelson Helper Integration Site 1 haplotypes and
            peripheral blood expression associates with lithium response and
            immunomodulation in bipolar patients.
REFERENCE   2  (residues 1 to 1196)
  AUTHORS   Karamzade,A., Babaei,M., Saberi,M., Golchin,N., Khalil Nejad Sani
            Banaei,A., Eshaghkhani,Y., Golchehre,Z. and Keramatipour,M.
  TITLE     Identification of a novel truncating variant in AHI1 gene and a
            brief review on mutations spectrum
  JOURNAL   Mol Biol Rep 48 (6), 5339-5345 (2021)
   PUBMED   34191236
  REMARK    GeneRIF: Identification of a novel truncating variant in AHI1 gene
            and a brief review on mutations spectrum.
            Review article
REFERENCE   3  (residues 1 to 1196)
  AUTHORS   Bai,Z., Hu,S., Liu,N., Wu,Q. and Kong,X.
  TITLE     [Genetic testing and prenatal diagnosis for two families affected
            with Joubert syndrome]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 37 (5), 509-513 (2020)
   PUBMED   32335874
  REMARK    GeneRIF: The proband of family 1 with Joubert syndrome was found to
            harbor homozygous c.2072delT (p.F691S*fs19) frameshift variant of
            the AHI1 gene, which may cause premature termination of translation
            of the Abelson helper integration site 1 after the 691st amino acid
REFERENCE   4  (residues 1 to 1196)
  AUTHORS   Sheu,J.J., Yang,L.Y., Sanotra,M.R., Wang,S.T., Lu,H.T., Kam,R.S.Y.,
            Hsu,I.U., Kao,S.H., Lee,C.K., Shieh,J.C. and Lin,Y.F.
  TITLE     Reduction of AHI1 in the serum of Taiwanese with probable
            Alzheimer's disease
  JOURNAL   Clin Biochem 76, 24-30 (2020)
   PUBMED   31786207
  REMARK    GeneRIF: An early event of AHI1 reduction in the body of AD
            patients was observed. Serum AHI1 may be valuable for early
            diagnosis of Alzheimer disease
REFERENCE   5  (residues 1 to 1196)
  AUTHORS   Close,J., Game,L., Clark,B., Bergounioux,J., Gerovassili,A. and
            Thein,S.L.
  TITLE     Genome annotation of a 1.5 Mb region of human chromosome 6q23
            encompassing a quantitative trait locus for fetal hemoglobin
            expression in adults
  JOURNAL   BMC Genomics 5 (1), 33 (2004)
   PUBMED   15169551
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1196)
  AUTHORS   Jiang,X., Zhao,Y., Chan,W.Y., Vercauteren,S., Pang,E., Kennedy,S.,
            Nicolini,F., Eaves,A. and Eaves,C.
  TITLE     Deregulated expression in Ph+ human leukemias of AHI-1, a gene
            activated by insertional mutagenesis in mouse models of leukemia
  JOURNAL   Blood 103 (10), 3897-3904 (2004)
   PUBMED   14751929
  REMARK    GeneRIF: in both mice and humans, Ahi-1/AHI-1 expression is highest
            in the most primitive hematopoietic cells with specific patterns of
            down-regulation in different lineages. Cells from CML patients show
            elevated AHI-1 transcripts in all disease phases
REFERENCE   7  (residues 1 to 1196)
  AUTHORS   Lagier-Tourenne,C., Boltshauser,E., Breivik,N., Gribaa,M.,
            Betard,C., Barbot,C. and Koenig,M.
  TITLE     Homozygosity mapping of a third Joubert syndrome locus to 6q23
  JOURNAL   J Med Genet 41 (4), 273-277 (2004)
   PUBMED   15060101
REFERENCE   8  (residues 1 to 1196)
  AUTHORS   Jiang,X., Hanna,Z., Kaouass,M., Girard,L. and Jolicoeur,P.
  TITLE     Ahi-1, a novel gene encoding a modular protein with WD40-repeat and
            SH3 domains, is targeted by the Ahi-1 and Mis-2 provirus
            integrations
  JOURNAL   J Virol 76 (18), 9046-9059 (2002)
   PUBMED   12186888
REFERENCE   9  (residues 1 to 1196)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 1196)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AJ459824.1, AI300295.1 and
            AL023693.25.
            
            Summary: This gene is apparently required for both cerebellar and
            cortical development in humans. This gene mutations cause specific
            forms of Joubert syndrome-related disorders. Joubert syndrome (JS)
            is a recessively inherited developmental brain disorder with
            several identified causative chromosomal loci. Alternatively
            spliced transcript variants encoding different isoforms have been
            identified. [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (3) differs in the 5', compared to
            variant 1. Variants 1-3 and 5 all encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ606362.1, AK092262.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q23.3"
     Protein         1..1196
                     /product="jouberin isoform a"
                     /note="contatins SH3 and WD40 domains; abelson helper
                     integration site 1 protein homolog"
                     /calculated_mol_wt=136985
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N157.1)"
     Region          56..186
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N157.1)"
     Region          141..434
                     /region_name="Interaction with HAP1.
                     /evidence=ECO:0000269|PubMed:23532844"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N157.1)"
     Region          215..242
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N157.1)"
     Region          254..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N157.1)"
     Region          <587..897
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          607..649
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N157.1)"
     Region          612..652
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          652..691
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N157.1)"
     Region          658..695
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          695..735
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N157.1)"
     Region          700..737
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          742..781
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N157.1)"
     Region          748..783
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          797..837
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N157.1)"
     Region          803..840
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          841..880
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N157.1)"
     Region          885..926
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N157.1)"
     Site            1002
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N157.1)"
     Region          1055..1106
                     /region_name="SH3_AHI-1"
                     /note="Src Homology 3 domain of Abelson helper integration
                     site-1 (AHI-1); cd11812"
                     /db_xref="CDD:212746"
     Site            order(1060,1062,1065,1069,1087..1088,1102,1104..1105)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212746"
     Region          1115..1196
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N157.1)"
     Site            1123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N157.1)"
     CDS             1..1196
                     /gene="AHI1"
                     /gene_synonym="AHI-1; dJ71N10.1; JBTS3; ORF1"
                     /coded_by="NM_001134830.2:213..3803"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS47483.1"
                     /db_xref="GeneID:54806"
                     /db_xref="HGNC:HGNC:21575"
                     /db_xref="MIM:608894"
ORIGIN      
        1 mptaeseakv ktkvrfeell kthsdlmrek kklkkklvrs eenispdtir snlhymkett
       61 sddpdtirsn lphikettsd dvsaantnnl kkstrvtknk lrntqlaten pngdasveed
      121 kqgkpnkkvi ktvpqlttqd lkpetpenkv dsthqkthtk pqpgvdhqks ekanegreet
      181 dleedeelmq ayqchvteem akeikrkirk klkeqltyfp sdtlfhddkl ssekrkkkke
      241 vpvfskaets tltisgdtve geqkkessvr svssdshqdd eissmeqste dsmqddtkpk
      301 pkktkkktka vadnnedvdg dgvheitsrd spvypkclld ddlvlgvyih rtdrlksdfm
      361 ishpmvkihv vdehtgqyvk kddsgrpvss yyekenvdyi lpimtqpydf kqlksrlpew
      421 eeqivfnenf pyllrgsdes pkvilffeil dflsvdeikn nsevqnqecg frkiawaflk
      481 llgangnani nsklrlqlyy pptkprspls vveafewwsk cprnhypstl yvtvrglkvp
      541 dcikpsyrsm malqeekgkp vhcerhhess svdtepglee skevikwkrl pgqacripnk
      601 hlfslnager gcfcldfshn grilaaacas rdgypiilye ipsgrfmrel cghlniiydl
      661 swskddhyil tsssdgtari wkneinntnt frvlphpsfv ytakfhpavr elvvtgcyds
      721 miriwkvemr edsailvrqf dvhksfinsl cfdteghhmy sgdctgvivv wntyvkindl
      781 ehsvhhwtin keiketefkg ipisyleihp ngkrllihtk dstlrimdlr ilvarkfvga
      841 anyrekihst ltpcgtflfa gsedgivyvw npetgeqvam ysdlpfkspi rdisyhpfen
      901 mvafcafgqn epillyiydf hvaqqeaemf kryngtfplp gihqsqdalc tcpklphqgs
      961 fqidefvhte ssstkmqlvk qrletvtevi rscaakvnkn lsftsppavs sqqsklkqsn
     1021 mltaqeilhq fgftqtgiis ierkpcnhqv dtaptvvaly dytanrsdel tihrgdiirv
     1081 ffkdnedwwy gsigkgqegy fpanhvaset lyqelppeik erspplspee ktkiekspap
     1141 qkqsinknks qdfrlgsesm thsemrkeqs hedqghimdt rmrknkqagr kvtlie
//
LOCUS       NP_001305896             492 aa            linear   PRI 21-NOV-2025
DEFINITION  translation initiation factor eIF2B subunit delta isoform 6 [Homo
            sapiens].
ACCESSION   NP_001305896
VERSION     NP_001305896.1
DBSOURCE    REFSEQ: accession NM_001318967.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Shivaram,S., Nagappa,M., Seshagiri,D.V., Saini,J., Govindaraj,P.,
            Sinha,S., Bindu,P.S. and Taly,A.B.
  TITLE     Leukodystrophy Due to eIF2B Mutations in Adults
  JOURNAL   Can J Neurol Sci 49 (5), 708-712 (2022)
   PUBMED   34663487
  REMARK    GeneRIF: Leukodystrophy Due to eIF2B Mutations in Adults.
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 492)
  AUTHORS   Yang,W. and Hinnebusch,A.G.
  TITLE     Identification of a regulatory subcomplex in the guanine nucleotide
            exchange factor eIF2B that mediates inhibition by phosphorylated
            eIF2
  JOURNAL   Mol Cell Biol 16 (11), 6603-6616 (1996)
   PUBMED   8887689
REFERENCE   6  (residues 1 to 492)
  AUTHORS   Price,N.T., Mellor,H., Craddock,B.L., Flowers,K.M., Kimball,S.R.,
            Wilmer,T., Jefferson,L.S. and Proud,C.G.
  TITLE     eIF2B, the guanine nucleotide-exchange factor for eukaryotic
            initiation factor 2. Sequence conservation between the alpha, beta
            and delta subunits of eIF2B from mammals and yeast
  JOURNAL   Biochem J 318 (Pt 2) (Pt 2), 637-643 (1996)
   PUBMED   8929216
REFERENCE   7  (residues 1 to 492)
  AUTHORS   Welsh,G.I., Miyamoto,S., Price,N.T., Safer,B. and Proud,C.G.
  TITLE     T-cell activation leads to rapid stimulation of translation
            initiation factor eIF2B and inactivation of glycogen synthase
            kinase-3
  JOURNAL   J Biol Chem 271 (19), 11410-11413 (1996)
   PUBMED   8626696
REFERENCE   8  (residues 1 to 492)
  AUTHORS   Henderson,R.A., Krissansen,G.W., Yong,R.Y., Leung,E., Watson,J.D.
            and Dholakia,J.N.
  TITLE     The delta-subunit of murine guanine nucleotide exchange factor
            eIF-2B. Characterization of cDNAs predicts isoforms differing at
            the amino-terminal end
  JOURNAL   J Biol Chem 269 (48), 30517-30523 (1994)
   PUBMED   7982969
REFERENCE   9  (residues 1 to 492)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   10 (residues 1 to 492)
  AUTHORS   van der Knaap,M.S., Fogli,A., Boespflug-Tanguy,O., Abbink,T.E.M.
            and Schiffmann,R.
  TITLE     Childhood Ataxia with Central Nervous System Hypomyelination /
            Vanishing White Matter
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301435
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JQ991007.1, AF057699.1,
            AC074117.7 and AF112207.1.
            
            Summary: Eukaryotic initiation factor 2B (EIF2B), which is
            necessary for protein synthesis, is a GTP exchange factor composed
            of five different subunits. The protein encoded by this gene is the
            fourth, or delta, subunit. Defects in this gene are a cause of
            leukoencephalopathy with vanishing white matter (VWM) and
            ovarioleukodystrophy. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (6) differs in the 5' UTR and
            coding sequence and uses an alternate in-frame splice junction
            compared to variant 4. The resulting isoform (6) is shorter at the
            N-terminus and lacks an alternate internal aa compared to isoform
            4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF057699.1, SRR13170464.1296139.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..492
                     /product="translation initiation factor eIF2B subunit
                     delta isoform 6"
                     /note="translation initiation factor eIF-2b delta subunit;
                     translation initiation factor eIF-2B subunit delta; eIF-2B
                     GDP-GTP exchange factor subunit delta; eukaryotic
                     translation initiation factor 2B subunit 4 delta;
                     eukaryotic translation initiation factor 2B, subunit 4
                     delta, 67kDa; eIF2B GDP-GTP exchange factor subunit delta;
                     translation initiation factor eIF2B subunit delta"
                     /calculated_mol_wt=54435
     Region          188..478
                     /region_name="IF-2B"
                     /note="Initiation factor 2 subunit family; pfam01008"
                     /db_xref="CDD:395798"
     CDS             1..492
                     /gene="EIF2B4"
                     /gene_synonym="EIF-2B; EIF2B; EIF2Bdelta; VWM4"
                     /coded_by="NM_001318967.2:111..1589"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:8890"
                     /db_xref="HGNC:HGNC:3260"
                     /db_xref="MIM:606687"
ORIGIN      
        1 mtkeeklqlr kekkqqkkkr keekgaepet gsavsaaqcq gptrelpesg iqlgtprekv
       61 pagrskaelr aerrakqeae ralkqarkge qggpppkasp stagetpsgv krlpeypqvd
      121 dlllrrlvkk perqqvptrk dygskvslfs hlpqysrqns ltqfmsipss vihpamvrlg
      181 lqysqglvsg snarciallr alqqviqdyt tppneelsrd lvnklkpyms fltqcrplsa
      241 smhnaikfln keitsvgssk reeeakselr aaidryvqek ivlaaqaisr fayqkisngd
      301 vilvygcssl vsrilqeawt egrrfrvvvv dsrpwlegrh tlrslvhagv pasyllipaa
      361 syvlpevskv llgahallan gsvmsrvgta qlalvarahn vpvlvccety kfcervqtda
      421 fvsnelddpd dlqckrgehv alanwqnhas lrllnlvydv tppelvdlvi telgmipcss
      481 vpvvlrvkss dq
//
LOCUS       NP_001070956             395 aa            linear   PRI 21-NOV-2025
DEFINITION  protein GNAS isoform f [Homo sapiens].
ACCESSION   NP_001070956
VERSION     NP_001070956.1
DBSOURCE    REFSEQ: accession NM_001077488.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Lin,J., Nie,Q., Cheng,J., Zhong,Y.N., Zhang,T., Zhang,X., Ge,X.,
            Ding,Y., Niu,C., Gao,Y., Wang,K., Gao,M., Wang,X., Chen,W., Yun,C.,
            Ye,C., Xu,J., Shaoyong,W., Zhang,L., Shang,P., Luo,X., Zhang,Z.,
            Zheng,X., Sha,X., Zhang,J., Nie,S., Zhang,X., Ren,F., Liu,H.,
            Dong,E., Yu,X., Ji,L., Pang,Y., Sun,J.P. and Jiang,C.
  TITLE     A microbial amino-acid-conjugated bile acid, tryptophan-cholic
            acid, improves glucose homeostasis via the orphan receptor MRGPRE
  JOURNAL   Cell 188 (17), 4530-4548 (2025)
   PUBMED   40446798
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Crane,J.L., Shamblott,M.J., Axelman,J., Hsu,S., Levine,M.A. and
            Germain-Lee,E.L.
  TITLE     Imprinting status of Galpha(s), NESP55, and XLalphas in cell
            cultures derived from human embryonic germ cells: GNAS imprinting
            in human embryonic germ cells
  JOURNAL   Clin Transl Sci 2 (5), 355-360 (2009)
   PUBMED   20443919
  REMARK    GeneRIF: analysis of the imprinting Status of Galpha(s), NESP55,
            and XLalphas in cell cultures derived from human embryonic germ
            cells
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Bastepe,M.
  TITLE     The GNAS Locus: Quintessential Complex Gene Encoding Gsalpha,
            XLalphas, and other Imprinted Transcripts
  JOURNAL   Curr Genomics 8 (6), 398-414 (2007)
   PUBMED   19412439
  REMARK    GeneRIF: GNAS locus has a highly complex imprinted expression
            pattern, giving rise to transcripts (including non-coding) that are
            maternally, paternally, or biallelically expressed.
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Jakobsen,A.M., Ahlman,H., Kolby,L., Abrahamsson,J.,
            Fischer-Colbrie,R. and Nilsson,O.
  TITLE     NESP55, a novel chromogranin-like peptide, is expressed in
            endocrine tumours of the pancreas and adrenal medulla but not in
            ileal carcinoids
  JOURNAL   Br J Cancer 88 (11), 1746-1754 (2003)
   PUBMED   12771991
  REMARK    GeneRIF: Neuroendocrine secretory protein 55 is found in a subset
            of neuroendocrine tumours showing differentiation towards adrenal
            chromaffin cells and pancreatic islets cells and not in ileal
            carcinoids
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Freson,K., Jaeken,J., Van Helvoirt,M., de Zegher,F.,
            Wittevrongel,C., Thys,C., Hoylaerts,M.F., Vermylen,J. and Van
            Geet,C.
  TITLE     Functional polymorphisms in the paternally expressed XLalphas and
            its cofactor ALEX decrease their mutual interaction and enhance
            receptor-mediated cAMP formation
  JOURNAL   Hum Mol Genet 12 (10), 1121-1130 (2003)
   PUBMED   12719376
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Weiss,U., Ischia,R., Eder,S., Lovisetti-Scamihorn,P., Bauer,R. and
            Fischer-Colbrie,R.
  TITLE     Neuroendocrine secretory protein 55 (NESP55): alternative splicing
            onto transcripts of the GNAS gene and posttranslational processing
            of a maternally expressed protein
  JOURNAL   Neuroendocrinology 71 (3), 177-186 (2000)
   PUBMED   10729789
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Ischia,R., Lovisetti-Scamihorn,P., Hogue-Angeletti,R.,
            Wolkersdorfer,M., Winkler,H. and Fischer-Colbrie,R.
  TITLE     Molecular cloning and characterization of NESP55, a novel
            chromogranin-like precursor of a peptide with 5-HT1B receptor
            antagonist activity
  JOURNAL   J Biol Chem 272 (17), 11657-11662 (1997)
   PUBMED   9111083
REFERENCE   8  (residues 1 to 395)
  AUTHORS   Haldeman-Englert,C.R., Hurst,A.C.E. and Levine,M.A.
  TITLE     Disorders of GNAS Inactivation
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29072892
REFERENCE   9  (residues 1 to 395)
  AUTHORS   Szymczuk,V., Florenzano,P., de Castro,L.F., Collins,M.T. and
            Boyce,A.M.
  TITLE     Fibrous Dysplasia / McCune-Albright Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719192
REFERENCE   10 (residues 1 to 395)
  AUTHORS   Weinstein,L.S., Gejman,P.V., de Mazancourt,P., American,N. and
            Spiegel,A.M.
  TITLE     A heterozygous 4-bp deletion mutation in the Gs alpha gene (GNAS1)
            in a patient with Albright hereditary osteodystrophy
  JOURNAL   Genomics 13 (4), 1319-1321 (1992)
   PUBMED   1505964
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC089157.1, M14631.1,
            AF493897.1, AF105253.1 and BC008855.2.
            
            Summary: This locus has a highly complex imprinted expression
            pattern. It gives rise to maternally, paternally, and biallelically
            expressed transcripts that are derived from four alternative
            promoters and 5' exons. Some transcripts contain a differentially
            methylated region (DMR) at their 5' exons, and this DMR is commonly
            found in imprinted genes and correlates with transcript expression.
            An antisense transcript is produced from an overlapping locus on
            the opposite strand. One of the transcripts produced from this
            locus, and the antisense transcript, are paternally expressed
            noncoding RNAs, and may regulate imprinting in this region. In
            addition, one of the transcripts contains a second overlapping ORF,
            which encodes a structurally unrelated protein - Alex. Alternative
            splicing of downstream exons is also observed, which results in
            different forms of the stimulatory G-protein alpha subunit, a key
            element of the classical signal transduction pathway linking
            receptor-ligand interactions with the activation of adenylyl
            cyclase and a variety of cellular reponses. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            Mutations in this gene result in pseudohypoparathyroidism type 1a,
            pseudohypoparathyroidism type 1b, Albright hereditary
            osteodystrophy, pseudopseudohypoparathyroidism, McCune-Albright
            syndrome, progressive osseus heteroplasia, polyostotic fibrous
            dysplasia of bone, and some pituitary tumors. [provided by RefSeq,
            Aug 2012].
            
            Transcript Variant: This variant (6) is biallelically expressed and
            uses an alternate in frame splice site, compared to variant 1. It
            encodes isoform f which has an additional amino acid in the
            internal region compared to isoform GNASL.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M14631.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 19412439
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.32"
     Protein         1..395
                     /product="protein GNAS isoform f"
                     /note="secretogranin VI; G protein subunit alpha S;
                     guanine nucleotide binding protein (G protein), alpha
                     stimulating activity polypeptide 1; guanine nucleotide
                     regulatory protein; adenylate cyclase-stimulating G alpha
                     protein; protein ALEX; extra large alphas protein;
                     alternative gene product encoded by XL-exon"
                     /calculated_mol_wt=45621
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63092.1)"
     Region          41..389
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Region          42..55
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P63092.1)"
     Site            order(47,52..54,205,224,227,293..294,296,366..367)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206639"
     Site            47..54
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206639"
     Site            order(48..50,94,98,102,105,108..109,129,132,173,202,227,
                     235,239)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Region          197..205
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P63092.1)"
     Site            200..208
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            205
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(206,208,210,221,223,227..229,231,234..235,237..240)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(208,233,236..237,240)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Region          220..229
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P63092.1)"
     Site            224..227
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            225..241
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Region          289..296
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P63092.1)"
     Site            293..296
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P63092.1)"
     Site            order(358..369,371..374)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Region          365..370
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P63092.1)"
     Site            366..368
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..395
                     /gene="GNAS"
                     /gene_synonym="AHO; AIMAH1; C20orf45; GNAS1; GPSA; GSA;
                     GSP; NESP; PITA3; POH; SCG6; SgVI"
                     /coded_by="NM_001077488.5:307..1494"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS46623.1"
                     /db_xref="GeneID:2778"
                     /db_xref="HGNC:HGNC:4392"
                     /db_xref="MIM:139320"
ORIGIN      
        1 mgclgnskte dqrneekaqr eankkiekql qkdkqvyrat hrllllgage sgkstivkqm
       61 rilhvngfng eggeedpqaa rsnsdgseka tkvqdiknnl keaietivaa msnlvppvel
      121 anpenqfrvd yilsvmnvpd fdfppefyeh akalwedegv racyersney qlidcaqyfl
      181 dkidvikqad yvpsdqdllr crvltsgife tkfqvdkvnf hmfdvggqrd errkwiqcfn
      241 dvtaiifvva sssynmvire dnqtnrlqea lnlfksiwnn rwlrtisvil flnkqdllae
      301 kvlagkskie dyfpefaryt tpedatpepg edprvtraky firdeflris tasgdgrhyc
      361 yphftcavdt enirrvfndc rdiiqrmhlr qyell
//
LOCUS       NP_001070965             167 aa            linear   PRI 21-NOV-2025
DEFINITION  proline-rich protein 3 isoform b [Homo sapiens].
ACCESSION   NP_001070965
VERSION     NP_001070965.1
DBSOURCE    REFSEQ: accession NM_001077497.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 167)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 167)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 167)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 167)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 167)
  AUTHORS   Barcellos,L.F., May,S.L., Ramsay,P.P., Quach,H.L., Lane,J.A.,
            Nititham,J., Noble,J.A., Taylor,K.E., Quach,D.L., Chung,S.A.,
            Kelly,J.A., Moser,K.L., Behrens,T.W., Seldin,M.F., Thomson,G.,
            Harley,J.B., Gaffney,P.M. and Criswell,L.A.
  TITLE     High-density SNP screening of the major histocompatibility complex
            in systemic lupus erythematosus demonstrates strong evidence for
            independent susceptibility regions
  JOURNAL   PLoS Genet 5 (10), e1000696 (2009)
   PUBMED   19851445
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 167)
  AUTHORS   Paladini,F., Belfiore,F., Cocco,E., Carcassi,C., Cauli,A.,
            Vacca,A., Fiorillo,M.T., Mathieu,A., Cascino,I. and Sorrentino,R.
  TITLE     HLA-E gene polymorphism associates with ankylosing spondylitis in
            Sardinia
  JOURNAL   Arthritis Res Ther 11 (6), R171 (2009)
   PUBMED   19912639
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 167)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL662800.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK074531.1, SRR14038196.2461993.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..167
                     /product="proline-rich protein 3 isoform b"
                     /note="proline-rich polypeptide 3; proline-rich protein 3;
                     MHC class I region proline-rich protein CAT56"
                     /calculated_mol_wt=18513
     Region          136..160
                     /region_name="zf-CCCH"
                     /note="Zinc finger C-x8-C-x5-C-x3-H type (and similar);
                     pfam00642"
                     /db_xref="CDD:459885"
     CDS             1..167
                     /gene="PRR3"
                     /gene_synonym="CAT56"
                     /coded_by="NM_001077497.3:637..1140"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43441.1"
                     /db_xref="GeneID:80742"
                     /db_xref="HGNC:HGNC:21149"
ORIGIN      
        1 mpkrkkqnhh qpptqqqppl pereetgdee dgspialhrg ppgsrgplip pllslppppw
       61 grgpirrglg prsspygrgw wgvnaeppfp gpghggptrg sfhkeqrnpr rlkswslikn
      121 tcppkddpqv medksdrpvc rhfakkghcr yedlcafyhp gvngppl
//
LOCUS       NP_001333271             480 aa            linear   PRI 21-NOV-2025
DEFINITION  autophagy-related protein 13 isoform f [Homo sapiens].
ACCESSION   NP_001333271 XP_016874104
VERSION     NP_001333271.1
DBSOURCE    REFSEQ: accession NM_001346342.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Patel,A. and Faesen,A.C.
  TITLE     Metamorphosis by ATG13 and ATG101 in human autophagy initiation
  JOURNAL   Autophagy 20 (4), 968-969 (2024)
   PUBMED   37394799
  REMARK    GeneRIF: Metamorphosis by ATG13 and ATG101 in human autophagy
            initiation.
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Nguyen,A. and Faesen,A.C.
  TITLE     The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis
  JOURNAL   FEBS Lett 598 (1), 114-126 (2024)
   PUBMED   37567770
  REMARK    GeneRIF: The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis.
            Review article
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Karabi,Z., Moradian,F. and Kheirabadi,M.
  TITLE     The effect of lactoferrin on ULK1 and ATG13 genes expression in
            breast cancer cell line MCF7 and bioinformatics studies of protein
            interaction between lactoferrin and the autophagy initiation
            complex
  JOURNAL   Cell Biochem Biophys 80 (4), 795-806 (2022)
   PUBMED   36169801
  REMARK    GeneRIF: The effect of lactoferrin on ULK1 and ATG13 genes
            expression in breast cancer cell line MCF7 and bioinformatics
            studies of protein interaction between lactoferrin and the
            autophagy initiation complex.
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Gottschalk,G., Peterson,D., Knox,K., Maynard,M., Whelan,R.J. and
            Roy,A.
  TITLE     Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE)
  JOURNAL   Mol Cell Neurosci 120, 103731 (2022)
   PUBMED   35487443
  REMARK    GeneRIF: Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE).
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Jung,C.H., Jun,C.B., Ro,S.H., Kim,Y.M., Otto,N.M., Cao,J., Kundu,M.
            and Kim,D.H.
  TITLE     ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy
            machinery
  JOURNAL   Mol Biol Cell 20 (7), 1992-2003 (2009)
   PUBMED   19225151
  REMARK    GeneRIF: The ULK-Atg13-FIP200 complexes are direct targets of mTOR
            and important regulators of autophagy in response to mTOR
            signaling.
REFERENCE   7  (residues 1 to 480)
  AUTHORS   Hosokawa,N., Hara,T., Kaizuka,T., Kishi,C., Takamura,A., Miura,Y.,
            Iemura,S., Natsume,T., Takehana,K., Yamada,N., Guan,J.L., Oshiro,N.
            and Mizushima,N.
  TITLE     Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200
            complex required for autophagy
  JOURNAL   Mol Biol Cell 20 (7), 1981-1991 (2009)
   PUBMED   19211835
  REMARK    GeneRIF: mTORC1 suppresses autophagy through direct regulation of
            the approximately 3-MDa ULK1-Atg13-FIP200 complex.
REFERENCE   8  (residues 1 to 480)
  AUTHORS   Chan,E.Y., Longatti,A., McKnight,N.C. and Tooze,S.A.
  TITLE     Kinase-inactivated ULK proteins inhibit autophagy via their
            conserved C-terminal domains using an Atg13-independent mechanism
  JOURNAL   Mol Cell Biol 29 (1), 157-171 (2009)
   PUBMED   18936157
  REMARK    GeneRIF: The functions of ULK1 and ULK2 are controlled by
            autophosphorylation and conformational changes involving exposure
            of the C-terminal domain and interaction with the putative human
            homologue of Atg13.
            GeneRIF: The gene product is the functional homologue of yeast
            Atg13, and required for autophagy in mammalian cells.
REFERENCE   9  (residues 1 to 480)
  AUTHORS   Meijer,W.H., van der Klei,I.J., Veenhuis,M. and Kiel,J.A.
  TITLE     ATG genes involved in non-selective autophagy are conserved from
            yeast to man, but the selective Cvt and pexophagy pathways also
            require organism-specific genes
  JOURNAL   Autophagy 3 (2), 106-116 (2007)
   PUBMED   17204848
REFERENCE   10 (residues 1 to 480)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC127035.6 and AC115088.6.
            
            On Oct 9, 2016 this sequence version replaced XP_016874104.1.
            
            Summary: The protein encoded by this gene is an autophagy factor
            and a target of the TOR kinase signaling pathway. The encoded
            protein is essential for autophagosome formation and mitophagy.
            [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (36), as well as variants 2, 5,
            and 37-45, encodes isoform f.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2177523.1,
                                           SRR1803616.71204.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..480
                     /product="autophagy-related protein 13 isoform f"
                     /note="autophagy-related protein 13; ATG13 autophagy
                     related 13 homolog"
                     /calculated_mol_wt=52692
     Region          19..192
                     /region_name="ATG13"
                     /note="Autophagy-related protein 13; pfam10033"
                     /db_xref="CDD:431003"
     CDS             1..480
                     /gene="ATG13"
                     /gene_synonym="KIAA0652; PARATARG8"
                     /coded_by="NM_001346342.2:546..1988"
                     /note="isoform f is encoded by transcript variant 36"
                     /db_xref="CCDS:CCDS7921.1"
                     /db_xref="GeneID:9776"
                     /db_xref="HGNC:HGNC:29091"
                     /db_xref="MIM:615088"
ORIGIN      
        1 metdlnsqdr kdldkfikff alktvqvivq arlgekictr ssssptgsdw fnlaikdipe
       61 vtheakkala gqlpavgrsm cveislktse gdsmeleiwc lemnekcdke ikvsytvynr
      121 lslllkslla itrvtpayrl srkqgheyvi lyriyfgevq lsglgegfqt vrvgtvgtpv
      181 gtitlscayr inlafmstrq fertppimgi iidhfvdrpy pssspmhpcn yrtagedtgv
      241 iypsvedsqe vcttsfstsp psqlmvpgke ggvplapnqp vhgtqadqer latctpsdrt
      301 hcaatpssse dtetvsnsse grasphdvle tifvrkvgaf vnkpinqvtl tsldipfamf
      361 apknleledt dpmvnppdsp etesplqgsl hsdgssggss gnthddfvmi dfkpafskdd
      421 ilpmdlgtfy refqnppqls slsidigaqs maedldslpe klavheknvr efdafvetlq
//
LOCUS       NP_001387275             332 aa            linear   PRI 21-NOV-2025
DEFINITION  single-stranded DNA-binding protein 2 isoform 15 [Homo sapiens].
ACCESSION   NP_001387275
VERSION     NP_001387275.1
DBSOURCE    REFSEQ: accession NM_001400346.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Schwab,C., Roberts,K., Boer,J.M., Gohring,G., Steinemann,D.,
            Vora,A., Macartney,C., Hough,R., Thorn,Z., Dillon,R., Escherich,G.,
            Cazzaniga,G., Schlegelberger,B., Loh,M., den Boer,M.L.,
            Moorman,A.V. and Harrison,C.J.
  TITLE     SSBP2-CSF1R is a recurrent fusion in B-lineage acute lymphoblastic
            leukemia with diverse genetic presentation and variable outcome
  JOURNAL   Blood 137 (13), 1835-1838 (2021)
   PUBMED   33197935
  REMARK    GeneRIF: SSBP2-CSF1R is a recurrent fusion in B-lineage acute
            lymphoblastic leukemia with diverse genetic presentation and
            variable outcome.
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Wang,H., Kim,J., Wang,Z., Yan,X.X., Dean,A. and Xu,W.
  TITLE     Crystal structure of human LDB1 in complex with SSBP2
  JOURNAL   Proc Natl Acad Sci U S A 117 (2), 1042-1048 (2020)
   PUBMED   31892537
  REMARK    GeneRIF: Single-stranded DNA binding proteins (SSBPs) interact
            specifically with the LDB/Chip conserved domain (LCCD) of LDB
            proteins and stabilize LDBs by preventing their proteasomal
            degradation, thus promoting their functions in gene regulation.
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Kim,H., Kim,Y., Bang,S., Park,S., Jee,S., Sim,J., Shin,S.J.,
            Paik,S.S. and Jang,K.
  TITLE     Low Expression of Single-stranded DNA Binding Protein 2 (SSBP2)
            Predicts Unfavourable Postoperative Outcomes in Patients With Clear
            Cell Renal Cell Carcinoma
  JOURNAL   In Vivo 34 (1), 101-107 (2020)
   PUBMED   31882468
  REMARK    GeneRIF: CcRCC with low SSBP2 expression was associated with
            adverse clinicopathological characteristics and poor patient
            outcomes.
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Fleisig,H.B., Orazio,N.I., Liang,H., Tyler,A.F., Adams,H.P.,
            Weitzman,M.D. and Nagarajan,L.
  TITLE     Adenoviral E1B55K oncoprotein sequesters candidate leukemia
            suppressor sequence-specific single-stranded DNA-binding protein 2
            into aggresomes
  JOURNAL   Oncogene 26 (33), 4797-4805 (2007)
   PUBMED   17311003
  REMARK    GeneRIF: Results suggest that subverting SSBP2 function by
            oncoprotein E1B55K may contribute to cell transformation by viral
            oncoproteins.
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Liang,H., Samanta,S. and Nagarajan,L.
  TITLE     SSBP2, a candidate tumor suppressor gene, induces growth arrest and
            differentiation of myeloid leukemia cells
  JOURNAL   Oncogene 24 (16), 2625-2634 (2005)
   PUBMED   15782145
  REMARK    GeneRIF: Our findings are consistent with human SSBP2 being a novel
            regulator of hematopoietic growth and differentiation, whose loss
            confers a block in differentiation advantage to myeloid leukemic
            cells.
REFERENCE   8  (residues 1 to 332)
  AUTHORS   Castro,P., Liang,H., Liang,J.C. and Nagarajan,L.
  TITLE     A novel, evolutionarily conserved gene family with putative
            sequence-specific single-stranded DNA-binding activity
  JOURNAL   Genomics 80 (1), 78-85 (2002)
   PUBMED   12079286
  REMARK    GeneRIF: Member of a closely related, evolutionarily conserved, and
            ubiquitously expressed gene family, potential tumor suppressor
REFERENCE   9  (residues 1 to 332)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 332)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016562.7, AC093250.3,
            AC026419.5 and AC010623.10.
            
            Summary: This gene encodes a subunit of a protein complex that
            interacts with single-stranded DNA and is involved in the DNA
            damage response and maintenance of genome stability. The encoded
            protein may also play a role in telomere repair. A variant of this
            gene may be associated with survival in human glioblastoma
            patients. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.81867.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.1"
     Protein         1..332
                     /product="single-stranded DNA-binding protein 2 isoform
                     15"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein 2"
                     /calculated_mol_wt=34670
     Region          19..45
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          83..309
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     CDS             1..332
                     /gene="SSBP2"
                     /gene_synonym="HSPC116; SOSS-B2"
                     /coded_by="NM_001400346.1:56..1054"
                     /note="isoform 15 is encoded by transcript variant 17"
                     /db_xref="GeneID:23635"
                     /db_xref="HGNC:HGNC:15831"
                     /db_xref="MIM:607389"
ORIGIN      
        1 mygkgksnss avpsdsqare klalyvyeyl lhvgaqksaq tflseirwek nitlgeppgf
       61 lhswwcvfwd lycaaperre tcehsseaka fhdysaaaap spvlgnippg dgmpvgpvpp
      121 gffqpllpsg mdptrqqghp nmggpmqrmt pprgmvplgp qnyggamrpp lnalggpgmp
      181 gmnmgpgggr pwpnptnans ipyssaspgn yvgppggggp pgtpimpspa dstnsgdnmy
      241 tlmnavppgp nrpnfpmgpg sdgpmgglgg meshhmngsl gsgdmdsisk nspnnmslsn
      301 qpgtprddge mggnflnpfq sesyspsmtm sv
//
LOCUS       NP_001340177             324 aa            linear   PRI 21-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 1 [Homo sapiens].
ACCESSION   NP_001340177 XP_016869035
VERSION     NP_001340177.1
DBSOURCE    REFSEQ: accession NM_001353248.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            On Jul 1, 2017 this sequence version replaced XP_016869035.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1471992.1,
                                           SRR18074967.1790152.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 1"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=36617
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353248.2:377..1351"
                     /note="isoform 1 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS6361.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mgnllkvltc tdleqgpnff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqik smlq
//
LOCUS       NP_001366483             859 aa            linear   PRI 21-NOV-2025
DEFINITION  KN motif and ankyrin repeat domain-containing protein 2 isoform 1
            [Homo sapiens].
ACCESSION   NP_001366483
VERSION     NP_001366483.1
DBSOURCE    REFSEQ: accession NM_001379554.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Loncaric,M., Stojanovic,N., Rac-Justament,A., Coopmans,K.,
            Majhen,D., Humphries,J.D., Humphries,M.J. and Ambriovic-Ristov,A.
  TITLE     Talin2 and KANK2 functionally interact to regulate microtubule
            dynamics, paclitaxel sensitivity and cell migration in the
            MDA-MB-435S melanoma cell line
  JOURNAL   Cell Mol Biol Lett 28 (1), 56 (2023)
   PUBMED   37460977
  REMARK    GeneRIF: Talin2 and KANK2 functionally interact to regulate
            microtubule dynamics, paclitaxel sensitivity and cell migration in
            the MDA-MB-435S melanoma cell line.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 859)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 859)
  AUTHORS   Xu,Y., Guo,C., Pan,W., Zhao,C., Ding,Y., Xie,X., Wei,Z., Sun,Y. and
            Yu,C.
  TITLE     Nephrotic-syndrome-associated mutation of KANK2 induces pathologic
            binding competition with physiological interactor KIF21A
  JOURNAL   J Biol Chem 297 (2), 100958 (2021)
   PUBMED   34274317
  REMARK    GeneRIF: Nephrotic-syndrome-associated mutation of KANK2 induces
            pathologic binding competition with physiological interactor
            KIF21A.
REFERENCE   5  (residues 1 to 859)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 859)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   7  (residues 1 to 859)
  AUTHORS   Kakinuma,N., Zhu,Y., Wang,Y., Roy,B.C. and Kiyama,R.
  TITLE     Kank proteins: structure, functions and diseases
  JOURNAL   Cell Mol Life Sci 66 (16), 2651-2659 (2009)
   PUBMED   19554261
  REMARK    Review article
REFERENCE   8  (residues 1 to 859)
  AUTHORS   Zhu,Y., Kakinuma,N., Wang,Y. and Kiyama,R.
  TITLE     Kank proteins: a new family of ankyrin-repeat domain-containing
            proteins
  JOURNAL   Biochim Biophys Acta 1780 (2), 128-133 (2008)
   PUBMED   17996375
REFERENCE   9  (residues 1 to 859)
  AUTHORS   Zhang,Y., Zhang,H., Liang,J., Yu,W. and Shang,Y.
  TITLE     SIP, a novel ankyrin repeat containing protein, sequesters steroid
            receptor coactivators in the cytoplasm
  JOURNAL   EMBO J 26 (11), 2645-2657 (2007)
   PUBMED   17476305
  REMARK    GeneRIF: SIP, a novel ankyrin repeat containing protein, sequesters
            steroid receptor coactivators in the cytoplasm.
REFERENCE   10 (residues 1 to 859)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009000.6 and AC011485.6.
            
            Summary: This gene encodes a member of the KN motif and ankyrin
            repeat domains (KANK) family of proteins, which play a role in
            cytoskeletal formation by regulating actin polymerization. The
            encoded protein functions in the sequestration of steroid receptor
            coactivators and possibly other proteins. Mutations in this gene
            are associated with impaired kidney podocyte function and nephrotic
            syndrome, and keratoderma and woolly hair. [provided by RefSeq, Jul
            2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.2630922.1,
                                           SRR14038191.2148439.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..859
                     /product="KN motif and ankyrin repeat domain-containing
                     protein 2 isoform 1"
                     /note="KN motif and ankyrin repeat domain-containing
                     protein 2; kidney ankyrin repeat-containing protein 2;
                     SRC1-interacting protein; matrix-remodeling-associated
                     protein 3; ankyrin repeat domain-containing protein 25;
                     SRC-interacting protein; steroid receptor coactivator
                     interacting protein"
                     /calculated_mol_wt=91791
     Region          1..72
                     /region_name="Interaction with AIFM1.
                     /evidence=ECO:0000269|PubMed:22371500"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          31..69
                     /region_name="KN_motif"
                     /note="KN motif; pfam12075"
                     /db_xref="CDD:432311"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BX02; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BX02; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BX02; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            105
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          139..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BX02; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          304..325
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          <450..593
                     /region_name="LGT"
                     /note="Prolipoprotein diacylglyceryl transferase; cl00478"
                     /db_xref="CDD:469786"
     Site            472
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          622..659
                     /region_name="ANK 0, degenerate.
                     /evidence=ECO:0000269|PubMed:29183992"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          636..672
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <658..833
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          674..706
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          674..704
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          677..843
                     /region_name="Interaction with NCOA1.
                     /evidence=ECO:0000269|PubMed:17476305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          708..743
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          747..777
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(748,752..753,756..758,760..761,765,768,777,779,781,
                     785..786,789..791,793..794,798,801,811,813,815,819..820,
                     823..825,827..828,832,835)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          779..811
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..859
                     /gene="KANK2"
                     /gene_synonym="ANKRD25; MXRA3; NPHS16; PPKWH; SIP"
                     /coded_by="NM_001379554.1:504..3083"
                     /note="isoform 1 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS54219.1"
                     /db_xref="GeneID:25959"
                     /db_xref="HGNC:HGNC:29300"
                     /db_xref="MIM:614610"
ORIGIN      
        1 maqvlhvpap fpgtpgpasp pafpakdpdp pysvetpygy rldldflkyv ddiekghtlr
       61 rvavqrrprl sslprgpgsw wtsteslcsn asgdsrhsay sycgrgfypq ygaletrggf
      121 nprvertlld arrrledqaa tptglgsltp saagstaslv gvglppptpr ssglstpvpp
      181 saghlahvre qmagalrklr qleeqvklip vlqvklsvlq eekrqltvql ksqkflghpt
      241 agrgrselcl dlpdppedpv aletrsvgtw vrerdlgmpd geaalaakva vletqlkkal
      301 qelqaaqarq adpqpqawpp pdspvrvdtv rvvegpreve vvastaagap aqraqslepy
      361 gtglralamp grpesppvfr sqevvetmcp vpaaatsnvh mvkkisiter scdgaaglpe
      421 vpaesssspp gsevasltqp ekstgrvptq epthreptrq aasqeseeag gtapplsspp
      481 ggppagvrsi mkrkeevadp tahrrslqfv gvnggyesss edsstaenis dndsteneap
      541 eprervpsva eapqlrpagt aaaktsrqec qlsresqhip taegasgsnt eeeirmelsp
      601 dlisaclale kyldnpnalt erelkvaytt vlqewlrlac rsdahpelvr rhlvtframs
      661 arlldyvvni adsngntalh ysvshanfpv vqqlldsgvc kvdkqnragy spimltalat
      721 lktqddietv lqlfrlgnin akasqagqta lmlavshgrv dvvkallace advnvqdddg
      781 stalmcaceh ghkeiaglll avpscdislt drdgstalmv aldagqseia smlysrmnik
      841 csfapmsdde sptsssaee
//
LOCUS       NP_001372132            1214 aa            linear   PRI 21-NOV-2025
DEFINITION  non-receptor tyrosine-protein kinase TYK2 isoform 9 [Homo sapiens].
ACCESSION   NP_001372132
VERSION     NP_001372132.1
DBSOURCE    REFSEQ: accession NM_001385203.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1214)
  AUTHORS   Chen,H., Ge,X., Li,C., Zeng,J. and Wang,X.
  TITLE     Structure and assembly of the human IL-12 signaling complex
  JOURNAL   Structure 32 (10), 1640-1651 (2024)
   PUBMED   39111304
REFERENCE   2  (residues 1 to 1214)
  AUTHORS   Lesgidou,N. and Vlassi,M.
  TITLE     Community analysis of large-scale molecular dynamics simulations
            elucidated dynamics-driven allostery in tyrosine kinase 2
  JOURNAL   Proteins 92 (4), 474-498 (2024)
   PUBMED   37950407
  REMARK    GeneRIF: Community analysis of large-scale molecular dynamics
            simulations elucidated dynamics-driven allostery in tyrosine kinase
            2.
REFERENCE   3  (residues 1 to 1214)
  AUTHORS   Zhang,M., Liu,Z., Zhu,Y., Wu,K., Zhou,L., Peng,Y., Pan,J., Chen,B.,
            Wang,X. and Chen,S.
  TITLE     Associations of genetic variants within TYK2 with pulmonary
            tuberculosis among Chinese population
  JOURNAL   Mol Genet Genomic Med 12 (2), e2386 (2024)
   PUBMED   38337161
  REMARK    GeneRIF: Associations of genetic variants within TYK2 with
            pulmonary tuberculosis among Chinese population.
REFERENCE   4  (residues 1 to 1214)
  AUTHORS   Benmansour,R., Tagajdid,M.R., El Hamzaoui,H., Fjouji,S., Doghmi,N.,
            Houba,A., Belbacha,I., Elkochri,S., Aabi,R., Elannaz,H.,
            Laraqui,A., El Mchichi,B., Chmitah,T., Touil,N., Ennibi,K.,
            Eljaoudi,R., Elmir,E., Amine Lahlou,I. and Oumzil,H.
  TITLE     TYK2, IFITM3, IFNAR2 and OAS3 single-nucleotide polymorphisms among
            severe COVID-19 ICU patients in Morocco
  JOURNAL   Int J Immunopathol Pharmacol 38, 3946320241257241 (2024)
   PUBMED   38760017
  REMARK    GeneRIF: TYK2, IFITM3, IFNAR2 and OAS3 single-nucleotide
            polymorphisms among severe COVID-19 ICU patients in Morocco.
REFERENCE   5  (residues 1 to 1214)
  AUTHORS   Yang,Z., Xiang,Q. and Nicholas,J.
  TITLE     Direct and biologically significant interactions of human
            herpesvirus 8 interferon regulatory factor 1 with STAT3 and Janus
            kinase TYK2
  JOURNAL   PLoS Pathog 19 (11), e1011806 (2023)
   PUBMED   37983265
  REMARK    GeneRIF: Direct and biologically significant interactions of human
            herpesvirus 8 interferon regulatory factor 1 with STAT3 and Janus
            kinase TYK2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1214)
  AUTHORS   Tavernier,J., Tuypens,T., Plaetinck,G., Verhee,A., Fiers,W. and
            Devos,R.
  TITLE     Molecular basis of the membrane-anchored and two soluble isoforms
            of the human interleukin 5 receptor alpha subunit
  JOURNAL   Proc Natl Acad Sci U S A 89 (15), 7041-7045 (1992)
   PUBMED   1495999
REFERENCE   7  (residues 1 to 1214)
  AUTHORS   Velazquez,L., Fellous,M., Stark,G.R. and Pellegrini,S.
  TITLE     A protein tyrosine kinase in the interferon alpha/beta signaling
            pathway
  JOURNAL   Cell 70 (2), 313-322 (1992)
   PUBMED   1386289
REFERENCE   8  (residues 1 to 1214)
  AUTHORS   Partanen,J., Makela,T.P., Alitalo,R., Lehvaslaiho,H. and Alitalo,K.
  TITLE     Putative tyrosine kinases expressed in K-562 human leukemia cells
  JOURNAL   Proc Natl Acad Sci U S A 87 (22), 8913-8917 (1990)
   PUBMED   2247464
REFERENCE   9  (residues 1 to 1214)
  AUTHORS   Firmbach-Kraft,I., Byers,M., Shows,T., Dalla-Favera,R. and
            Krolewski,J.J.
  TITLE     tyk2, prototype of a novel class of non-receptor tyrosine kinase
            genes
  JOURNAL   Oncogene 5 (9), 1329-1336 (1990)
   PUBMED   2216457
REFERENCE   10 (residues 1 to 1214)
  AUTHORS   Krolewski,J.J., Lee,R., Eddy,R., Shows,T.B. and Dalla-Favera,R.
  TITLE     Identification and chromosomal mapping of new human tyrosine kinase
            genes
  JOURNAL   Oncogene 5 (3), 277-282 (1990)
   PUBMED   2156206
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011557.7.
            
            Summary: This gene encodes a member of the tyrosine kinase and,
            more specifically, the Janus kinases (JAKs) protein families. This
            protein associates with the cytoplasmic domain of type I and type
            II cytokine receptors and promulgate cytokine signals by
            phosphorylating receptor subunits. It is also a component of both
            the type I and type III interferon signaling pathways. As such, it
            may play a role in anti-viral immunity. A mutation in this gene has
            been associated with Immunodeficiency 35. [provided by RefSeq, Sep
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1705213.1,
                                           SRR14038194.3185970.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1214
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..1214
                     /product="non-receptor tyrosine-protein kinase TYK2
                     isoform 9"
                     /EC_number="2.7.10.2"
                     /note="non-receptor tyrosine-protein kinase TYK2"
                     /calculated_mol_wt=136293
     Region          28..125
                     /region_name="FERM_F1"
                     /note="FERM F1 ubiquitin-like domain; pfam18379"
                     /db_xref="CDD:465733"
     Region          143..266
                     /region_name="FERM_F2"
                     /note="FERM F2 acyl-CoA binding protein-like domain;
                     pfam18377"
                     /db_xref="CDD:436450"
     Region          285..432
                     /region_name="Jak1_Phl"
                     /note="Jak1 pleckstrin homology-like domain; pfam17887"
                     /db_xref="CDD:465552"
     Region          437..534
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(457,474,504,506)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198244"
     Site            order(505,532)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198244"
     Region          589..867
                     /region_name="PTK_Tyk2_rpt1"
                     /note="Pseudokinase (repeat 1) domain of the Protein
                     Tyrosine Kinase, Tyrosine kinase 2; cd05076"
                     /db_xref="CDD:270661"
     Region          919..1201
                     /region_name="PTKc_Tyk2_rpt2"
                     /note="Catalytic (repeat 2) domain of the Protein Tyrosine
                     Kinase, Tyrosine kinase 2; cd05080"
                     /db_xref="CDD:270664"
     Site            order(930..931,933,938,955,957,987,1005..1009,1011,1050,
                     1054..1055,1057,1067..1068,1087..1091,1100,1148)
                     /site_type="active"
                     /db_xref="CDD:270664"
     Site            order(930..931,933,938,955,957,987,1005..1009,1011,
                     1054..1055,1057,1067..1068)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270664"
     Site            order(1050,1054,1087..1091,1100,1148)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270664"
     Site            1067..1093
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270664"
     CDS             1..1214
                     /gene="TYK2"
                     /gene_synonym="IMD35; JTK1"
                     /coded_by="NM_001385203.1:379..4023"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:7297"
                     /db_xref="HGNC:HGNC:12440"
                     /db_xref="MIM:176941"
ORIGIN      
        1 mplrhwgmar gskpvgdgaq pmaamgglkv llhwagpggg epwvtfsess ltaeevcihi
       61 ahkvgitppc fnlfalfdaq aqvwlppnhi leiprdaslm lyfrirfyfr nwhgmnprep
      121 avyrcgppgt eassdqtaqg mqlldpasfe ylfeqgkhef vndvaslwel steeeihhfk
      181 neslgmaflh lchlalrhgi pleevakkts fkdciprsfr rhirqhsalt rlrlrnvfrr
      241 flrdfqpgrl sqqmvmvkyl atlerlaprf gtervpvchl rllaqaegep cyirdsgvap
      301 tdpgpesaag ppthevlvtg tggiqwwpve eevnkeegss gssgrnpqas lfgkkakahk
      361 avgqpadrpr eplwayfcdf rdithvvlke hcvsihrqdn kclelslpsr aaalsfvslv
      421 dgyfrltads shylchevap prlvmsirdg ihgpllepfv qaklrpedgl ylihwstshp
      481 yrliltvaqr sqapdgmqsl rlrkfpieqq dgafvlegwg rsfpsvrelg aalqgcllra
      541 gddcfslrrc clpqpgetsn liimrgaras prtlnlsqls fhrvdqkeit qlshlgqgtr
      601 tnvyegrlrv egsgdpeegk mddedplvpg rdrgqelrvv lkvldpshhd ialafyetas
      661 lmsqvshthl afvhgvcvrg penimvteyv ehgpldvwlr rerghvpmaw kmvvaqqlas
      721 alsylenknl vhgnvcgrni llarlglaeg tspfiklsdp gvglgalsre erveripwla
      781 peclpggans lstamdkwgf gatlleicfd geaplqsrsp sekehfyqrq hrlpepscpq
      841 latltsqclt yeptqrpsfr tilrdltrlq phkrgfhhvv qaglelpgss dlpasasqtd
      901 ladvltvnpd spasdptvfh krylkkirdl geghfgkvsl ycydptndgt gemvavkalk
      961 adcgpqhrsg wkqeidilrt lyhehiikyk gccedqgeks lqlvmeyvpl gslrdylprh
     1021 siglaqlllf aqqicegmay lhaqhyihrd laarnvlldn drlvkigdfg lakavpeghe
     1081 yyrvredgds pvfwyapecl keykfyyasd vwsfgvtlye llthcdssqs pptkflelig
     1141 iaqgqmtvlr ltellerger lprpdkcpce vyhlmkncwe teasfrptfe nlipilktvh
     1201 ekyqgqapsv fsvc
//
LOCUS       NP_001365028             306 aa            linear   PRI 21-NOV-2025
DEFINITION  low-density lipoprotein receptor class A domain-containing protein
            4 isoform alpha 1 [Homo sapiens].
ACCESSION   NP_001365028 XP_024307016
VERSION     NP_001365028.1
DBSOURCE    REFSEQ: accession NM_001378099.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Xie,W., Xiao,H., Luo,J., Zhao,L., Jin,F., Ma,J., Li,J., Xiong,K.,
            Chen,C. and Wang,G.
  TITLE     Identification of low-density lipoprotein receptor class A domain
            containing 4 (LDLRAD4) as a prognostic indicator in primary
            gastrointestinal stromal tumors
  JOURNAL   Curr Probl Cancer 44 (6), 100593 (2020)
   PUBMED   32507364
  REMARK    GeneRIF: Identification of low-density lipoprotein receptor class A
            domain containing 4 (LDLRAD4) as a prognostic indicator in primary
            gastrointestinal stromal tumors.
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 306)
  AUTHORS   Meerabux,J.M., Ohba,H., Iwayama,Y., Maekawa,M.,
            Detera-Wadleigh,S.D., DeLisi,L.E. and Yoshikawa,T.
  TITLE     Analysis of a t(18;21)(p11.1;p11.1) translocation in a family with
            schizophrenia
  JOURNAL   J Hum Genet 54 (7), 386-391 (2009)
   PUBMED   19461657
REFERENCE   7  (residues 1 to 306)
  AUTHORS   Kikuchi,M., Yamada,K., Toyota,T. and Yoshikawa,T.
  TITLE     C18orf1 located on chromosome 18p11.2 may confer susceptibility to
            schizophrenia
  JOURNAL   J Med Dent Sci 50 (3), 225-229 (2003)
   PUBMED   15074360
REFERENCE   8  (residues 1 to 306)
  AUTHORS   Yoshikawa,T., Sanders,A.R., Esterling,L.E. and Detera-Wadleigh,S.D.
  TITLE     Multiple transcriptional variants and RNA editing in C18orf1, a
            novel gene with LDLRA and transmembrane domains on 18p11.2
  JOURNAL   Genomics 47 (2), 246-257 (1998)
   PUBMED   9479497
REFERENCE   9  (residues 1 to 306)
  AUTHORS   Esterling,L.E., Cox Matise,T., Sanders,A.R., Yoshikawa,T.,
            Overhauser,J., Gershon,E.S., Moskowitz,M.T. and
            Detera-Wadleigh,S.D.
  TITLE     An integrated physical map of 18p11.2: a susceptibility region for
            bipolar disorder
  JOURNAL   Mol Psychiatry 2 (6), 501-504 (1997)
   PUBMED   9399696
REFERENCE   10 (residues 1 to 306)
  AUTHORS   Yoshikawa,T., Sanders,A.R., Esterling,L.E., Overhauser,J.,
            Garnes,J.A., Lennon,G., Grewal,R. and Detera-Wadleigh,S.D.
  TITLE     Isolation of chromosome 18-specific brain transcripts as positional
            candidates for bipolar disorder
  JOURNAL   Am J Med Genet 74 (2), 140-149 (1997)
   PUBMED   9129712
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP002505.3, AP002439.3 and AP001010.4.
            
            On Jan 28, 2020 this sequence version replaced XP_024307016.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.250017.1,
                                           SRR1803617.134614.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467143, SAMEA2467144
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.21"
     Protein         1..306
                     /product="low-density lipoprotein receptor class A
                     domain-containing protein 4 isoform alpha 1"
                     /note="clone 22; low-density lipoprotein receptor class A
                     domain-containing protein 4"
                     /calculated_mol_wt=33769
     Region          16..47
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(17,25,37..38)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(30,33,37,43..44)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            40..44
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            65..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15165.1)"
     Region          180..183
                     /region_name="PPxY motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O15165.1)"
     Region          208..211
                     /region_name="SMAD interaction motif (SIM)"
                     /note="propagated from UniProtKB/Swiss-Prot (O15165.1)"
     Region          252..255
                     /region_name="PPxY motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O15165.1)"
     Region          286..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15165.1)"
     CDS             1..306
                     /gene="LDLRAD4"
                     /gene_synonym="C18orf1"
                     /coded_by="NM_001378099.1:648..1568"
                     /note="isoform alpha 1 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS32793.1"
                     /db_xref="GeneID:753"
                     /db_xref="HGNC:HGNC:1224"
                     /db_xref="MIM:606571"
ORIGIN      
        1 mpeagfqatn afteckftct sgkclylgsl vcnqqndcgd nsdeencllv tehpppgifn
       61 selefaqiii ivvvvtvmvv vivcllnhyk vstrsfinrp nqsrrredgl pqegclwpsd
      121 saaprlgase imhaprsrdr ftapsfiqrd rfsrfqptyp yvqheidlpp tislsdgeep
      181 ppyqgpctlq lrdpeqqmel nresvrappn rtifdsdlid iamysggpcp pssnsgisas
      241 tcssngrmeg ppptysevmg hhpgasflhh qrsnahrgsr lqfqqnnaes tivpikgkdr
      301 kpgnlv
//
LOCUS       NP_001258718             612 aa            linear   PRI 21-NOV-2025
DEFINITION  cytoplasmic dynein 1 intermediate chain 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001258718
VERSION     NP_001258718.1
DBSOURCE    REFSEQ: accession NM_001271789.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 612)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 612)
  AUTHORS   Habu,T. and Kim,J.
  TITLE     Dynein intermediate chain 2c (DNCI2c) complex is essential for
            exiting Mad2-dependent spindle assembly checkpoint
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1868 (12), 119120 (2021)
   PUBMED   34400173
  REMARK    GeneRIF: Dynein intermediate chain 2c (DNCI2c) complex is essential
            for exiting Mad2-dependent spindle assembly checkpoint.
REFERENCE   5  (residues 1 to 612)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 612)
  AUTHORS   Sivaram,M.V., Wadzinski,T.L., Redick,S.D., Manna,T. and Doxsey,S.J.
  TITLE     Dynein light intermediate chain 1 is required for progress through
            the spindle assembly checkpoint
  JOURNAL   EMBO J 28 (7), 902-914 (2009)
   PUBMED   19229290
REFERENCE   7  (residues 1 to 612)
  AUTHORS   Pfister,K.K., Fisher,E.M., Gibbons,I.R., Hays,T.S., Holzbaur,E.L.,
            McIntosh,J.R., Porter,M.E., Schroer,T.A., Vaughan,K.T.,
            Witman,G.B., King,S.M. and Vallee,R.B.
  TITLE     Cytoplasmic dynein nomenclature
  JOURNAL   J Cell Biol 171 (3), 411-413 (2005)
   PUBMED   16260502
REFERENCE   8  (residues 1 to 612)
  AUTHORS   Davies,T.H., Ning,Y.M. and Sanchez,E.R.
  TITLE     A new first step in activation of steroid receptors:
            hormone-induced switching of FKBP51 and FKBP52 immunophilins
  JOURNAL   J Biol Chem 277 (7), 4597-4600 (2002)
   PUBMED   11751894
REFERENCE   9  (residues 1 to 612)
  AUTHORS   Crackower,M.A., Sinasac,D.S., Xia,J., Motoyama,J., Prochazka,M.,
            Rommens,J.M., Scherer,S.W. and Tsui,L.C.
  TITLE     Cloning and characterization of two cytoplasmic dynein intermediate
            chain genes in mouse and human
  JOURNAL   Genomics 55 (3), 257-267 (1999)
   PUBMED   10049579
REFERENCE   10 (residues 1 to 612)
  AUTHORS   Vaughan,K.T. and Vallee,R.B.
  TITLE     Cytoplasmic dynein binds dynactin through a direct interaction
            between the intermediate chains and p150Glued
  JOURNAL   J Cell Biol 131 (6 Pt 1), 1507-1516 (1995)
   PUBMED   8522607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC064826.6, AF250307.1 and
            AC068039.6.
            
            Summary: This gene encodes a member of the dynein intermediate
            chain family. The encoded protein is a non-catalytic component of
            the cytoplasmic dynein 1 complex, which acts as a retrograde
            microtubule motor to transport organelles and vesicles. A
            pseudogene of this gene is located on chromosome 10. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Nov 2012].
            
            Transcript Variant: This variant (6) differs in the 5' UTR and in
            the coding region but maintains the reading frame, compared to
            variant 1. The encoded isoform (3) is shorter, compared to isoform
            1. Both variants 5 and 6 encode the same isoform (3).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.65550.1,
                                           SRR1803617.147115.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..612
                     /product="cytoplasmic dynein 1 intermediate chain 2
                     isoform 3"
                     /note="dynein, cytoplasmic, intermediate polypeptide 2; DH
                     IC-2; dynein intermediate chain 2, cytosolic; testis
                     tissue sperm-binding protein Li 66n"
                     /calculated_mol_wt=68295
     Region          107..137
                     /region_name="Dynein_IC2"
                     /note="Cytoplasmic dynein 1 intermediate chain 2;
                     pfam11540"
                     /db_xref="CDD:463291"
     Region          250..572
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(253,270,284,290..291,303..304,323,328,334..335,
                     353..354,373,378,384..385,414,431,436,448..449,473,477,
                     483..484,496..497,515,520,526..527,542..543,561,565,
                     571..572)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          256..305
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          313..351
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          359..400
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          408..455
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          463..495
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          501..539
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          547..573
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..612
                     /gene="DYNC1I2"
                     /gene_synonym="DIC74; DNCI2; IC2; NEDMIBA"
                     /coded_by="NM_001271789.2:129..1967"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS63056.1"
                     /db_xref="GeneID:1781"
                     /db_xref="HGNC:HGNC:2964"
                     /db_xref="MIM:603331"
ORIGIN      
        1 msdkselkae lerkkqrlaq ireekkrkee erkkketdqk keavapvqee sdlekkrrea
       61 eallqsmglt pespivpppm spssksvstp seagsqdsgd gavgsrrgpi klgmakitqv
      121 dfppreivty tketqtpvma qpkedeeedd dvvapkppie peeektlkkd eendskapph
      181 elteeekqqi lhseeflsff dhstrivera lseqiniffd ysgrdledke geiqagakls
      241 lnrqffderw skhrvvscld wssqypellv asynnnedap hepdgvalvw nmkykkttpe
      301 yvfhcqsavm satfakfhpn lvvggtysgq ivlwdnrsnk rtpvqrtpls aaahthpvyc
      361 vnvvgtqnah nlisistdgk icswsldmls hpqdsmelvh kqskavavts msfpvgdvnn
      421 fvvgseegsv ytacrhgska gisemfeghq gpitgihcha avgavdfshl fvtssfdwtv
      481 klwttknnkp lysfednady vydvmwspth palfacvdgm grldlwnlnn dtevptasis
      541 vegnpalnrv rwthsgreia vgdsegqivi ydvgeqiavp rndewarfgr tlaeinanra
      601 daeeeaatri pa
//
LOCUS       NP_001020267             250 aa            linear   PRI 21-NOV-2025
DEFINITION  proteasome subunit alpha-type 8 isoform 2 [Homo sapiens].
ACCESSION   NP_001020267
VERSION     NP_001020267.1
DBSOURCE    REFSEQ: accession NM_001025096.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Zivkovic,D., Sanchez Dafun,A., Menneteau,T., Schahl,A., Lise,S.,
            Kervarrec,C., Toste Rego,A., da Fonseca,P.C.A., Chavent,M.,
            Pineau,C., Burlet-Schiltz,O., Marcoux,J. and Bousquet,M.P.
  TITLE     Proteasome complexes experience profound structural and functional
            rearrangements throughout mammalian spermatogenesis
  JOURNAL   Proc Natl Acad Sci U S A 119 (15), e2116826119 (2022)
   PUBMED   35377789
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Teumer,A., Holtfreter,B., Volker,U., Petersmann,A., Nauck,M.,
            Biffar,R., Volzke,H., Kroemer,H.K., Meisel,P., Homuth,G. and
            Kocher,T.
  TITLE     Genome-wide association study of chronic periodontitis in a general
            German population
  JOURNAL   J Clin Periodontol 40 (11), 977-985 (2013)
   PUBMED   24024966
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Kirin,M., Chandra,A., Charteris,D.G., Hayward,C., Campbell,S.,
            Celap,I., Bencic,G., Vatavuk,Z., Kirac,I., Richards,A.J.,
            Tenesa,A., Snead,M.P., Fleck,B.W., Singh,J., Harsum,S.,
            Maclaren,R.E., den Hollander,A.I., Dunlop,M.G., Hoyng,C.B.,
            Wright,A.F., Campbell,H., Vitart,V. and Mitry,D.
  TITLE     Genome-wide association study identifies genetic risk underlying
            primary rhegmatogenous retinal detachment
  JOURNAL   Hum Mol Genet 22 (15), 3174-3185 (2013)
   PUBMED   23585552
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Qian,M.X., Pang,Y., Liu,C.H., Haratake,K., Du,B.Y., Ji,D.Y.,
            Wang,G.F., Zhu,Q.Q., Song,W., Yu,Y., Zhang,X.X., Huang,H.T.,
            Miao,S., Chen,L.B., Zhang,Z.H., Liang,Y.N., Liu,S., Cha,H.,
            Yang,D., Zhai,Y., Komatsu,T., Tsuruta,F., Li,H., Cao,C., Li,W.,
            Li,G.H., Cheng,Y., Chiba,T., Wang,L., Goldberg,A.L., Shen,Y. and
            Qiu,X.B.
  TITLE     Acetylation-mediated proteasomal degradation of core histones
            during DNA repair and spermatogenesis
  JOURNAL   Cell 153 (5), 1012-1024 (2013)
   PUBMED   23706739
REFERENCE   5  (residues 1 to 250)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Nusbaum,C., Zody,M.C., Borowsky,M.L., Kamal,M., Kodira,C.D.,
            Taylor,T.D., Whittaker,C.A., Chang,J.L., Cuomo,C.A., Dewar,K.,
            FitzGerald,M.G., Yang,X., Abouelleil,A., Allen,N.R., Anderson,S.,
            Bloom,T., Bugalter,B., Butler,J., Cook,A., DeCaprio,D., Engels,R.,
            Garber,M., Gnirke,A., Hafez,N., Hall,J.L., Norman,C.H., Itoh,T.,
            Jaffe,D.B., Kuroki,Y., Lehoczky,J., Lui,A., Macdonald,P.,
            Mauceli,E., Mikkelsen,T.S., Naylor,J.W., Nicol,R., Nguyen,C.,
            Noguchi,H., O'Leary,S.B., O'Neill,K., Piqani,B., Smith,C.L.,
            Talamas,J.A., Topham,K., Totoki,Y., Toyoda,A., Wain,H.M.,
            Young,S.K., Zeng,Q., Zimmer,A.R., Fujiyama,A., Hattori,M.,
            Birren,B.W., Sakaki,Y. and Lander,E.S.
  TITLE     DNA sequence and analysis of human chromosome 18
  JOURNAL   Nature 437 (7058), 551-555 (2005)
   PUBMED   16177791
  REMARK    Erratum:[Nature. 2005 Dec 1;438(7068):696. O'Neill, Keith [added]]
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Margottin-Goguet,F., Hsu,J.Y., Loktev,A., Hsieh,H.M., Reimann,J.D.
            and Jackson,P.K.
  TITLE     Prophase destruction of Emi1 by the SCF(betaTrCP/Slimb) ubiquitin
            ligase activates the anaphase promoting complex to allow
            progression beyond prometaphase
  JOURNAL   Dev Cell 4 (6), 813-826 (2003)
   PUBMED   12791267
REFERENCE   8  (residues 1 to 250)
  AUTHORS   Claverol,S., Burlet-Schiltz,O., Girbal-Neuhauser,E., Gairin,J.E.
            and Monsarrat,B.
  TITLE     Mapping and structural dissection of human 20 S proteasome using
            proteomic approaches
  JOURNAL   Mol Cell Proteomics 1 (8), 567-578 (2002)
   PUBMED   12376572
  REMARK    GeneRIF: This article provides an overview of some of the
            components in the human 20 S proteasome.
REFERENCE   9  (residues 1 to 250)
  AUTHORS   Geley,S., Kramer,E., Gieffers,C., Gannon,J., Peters,J.M. and
            Hunt,T.
  TITLE     Anaphase-promoting complex/cyclosome-dependent proteolysis of human
            cyclin A starts at the beginning of mitosis and is not subject to
            the spindle assembly checkpoint
  JOURNAL   J Cell Biol 153 (1), 137-148 (2001)
   PUBMED   11285280
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC042820.1 and BC025393.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the coding region, compared to variant 1, resulting
            in a shorter isoform (2).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.156840.1,
                                           SRR1803613.290871.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000415576.7/ ENSP00000409284.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q11.2"
     Protein         1..250
                     /product="proteasome subunit alpha-type 8 isoform 2"
                     /EC_number="3.4.25.1"
                     /note="proteasome (prosome, macropain) subunit, alpha
                     type, 8; proteasome subunit alpha-type 8; proteasome
                     subunit alpha 8; alpha4s; proteasome alpha 4 subunit"
                     /calculated_mol_wt=27712
     Region          5..213
                     /region_name="proteasome_alpha_type_7"
                     /note="The 20S proteasome, multisubunit proteolytic
                     complex, is the central enzyme of nonlysosomal protein
                     degradation in both the cytosol and nucleus. It is
                     composed of 28 subunits arranged as four homoheptameric
                     rings that stack on top of one another forming...;
                     cd03755"
                     /db_xref="CDD:239724"
     Site            order(7..10,12..13,15..16,20,23,26..27,30,38,53,55..56,
                     79..81,83..84,115,118,121..122,125..129,147,152..153,155,
                     157..158,160)
                     /site_type="other"
                     /note="alpha subunit interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239724"
     Site            order(32,48,50,63,165)
                     /site_type="active"
                     /db_xref="CDD:239724"
     CDS             1..250
                     /gene="PSMA8"
                     /gene_synonym="PSMA7L"
                     /coded_by="NM_001025096.2:98..850"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45842.1"
                     /db_xref="GeneID:143471"
                     /db_xref="HGNC:HGNC:22985"
                     /db_xref="MIM:617841"
ORIGIN      
        1 masrydrait vfspdghlfq veyaqeavkk gstavgirgt nivvlgvekk svaklqdert
       61 vrkicalddh vcmafaglta darvvinrar vecqshkltv edpvtveyit rfiatlkqky
      121 tqsngrrpfg isalivgfdd dgisrlyqtd psgtyhawka naigrsaktv refleknyte
      181 daiasdseai klaikallev vqsggkniel aiirrnqplk mfsakevely vteiekekee
      241 aekkkskksv
//
LOCUS       NP_005766                671 aa            linear   PRI 21-NOV-2025
DEFINITION  vinexin isoform 1 [Homo sapiens].
ACCESSION   NP_005766
VERSION     NP_005766.3
DBSOURCE    REFSEQ: accession NM_005775.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Pu,J., Wang,B., Zhang,D., Wang,K., Yang,Z., Zhu,P. and Song,Q.
  TITLE     UBE2T mediates SORBS3 ubiquitination to enhance IL-6/STAT3
            signaling and promote lung adenocarcinoma progression
  JOURNAL   J Biochem Mol Toxicol 38 (6), e23743 (2024)
   PUBMED   38816989
  REMARK    GeneRIF: UBE2T mediates SORBS3 ubiquitination to enhance IL-6/STAT3
            signaling and promote lung adenocarcinoma progression.
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Park,S.J., Frake,R.A. and Rubinsztein,D.C.
  TITLE     Increased SORBS3 expression in brain ageing contributes to
            autophagic decline via YAP1-WWTR1/TAZ signaling
  JOURNAL   Autophagy 19 (3), 943-944 (2023)
   PUBMED   35822241
  REMARK    GeneRIF: Increased SORBS3 expression in brain ageing contributes to
            autophagic decline via YAP1-WWTR1/TAZ signaling.
REFERENCE   4  (residues 1 to 671)
  AUTHORS   Park,S.J., Frake,R.A., Karabiyik,C., Son,S.M., Siddiqi,F.H.,
            Bento,C.F., Sterk,P., Vicinanza,M., Pavel,M. and Rubinsztein,D.C.
  TITLE     Vinexin contributes to autophagic decline in brain ageing across
            species
  JOURNAL   Cell Death Differ 29 (5), 1055-1070 (2022)
   PUBMED   34848853
  REMARK    GeneRIF: Vinexin contributes to autophagic decline in brain ageing
            across species.
REFERENCE   5  (residues 1 to 671)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 671)
  AUTHORS   Wakabayashi,M., Ito,T., Mitsushima,M., Aizawa,S., Ueda,K.,
            Amachi,T. and Kioka,N.
  TITLE     Interaction of lp-dlg/KIAA0583, a membrane-associated guanylate
            kinase family protein, with vinexin and beta-catenin at sites of
            cell-cell contact
  JOURNAL   J Biol Chem 278 (24), 21709-21714 (2003)
   PUBMED   12657639
REFERENCE   7  (residues 1 to 671)
  AUTHORS   Townson,S.M., Dobrzycka,K.M., Lee,A.V., Air,M., Deng,W., Kang,K.,
            Jiang,S., Kioka,N., Michaelis,K. and Oesterreich,S.
  TITLE     SAFB2, a new scaffold attachment factor homolog and estrogen
            receptor corepressor
  JOURNAL   J Biol Chem 278 (22), 20059-20068 (2003)
   PUBMED   12660241
REFERENCE   8  (residues 1 to 671)
  AUTHORS   Kioka,N.
  TITLE     [A novel adaptor protein family regulating cytoskeletal
            organization and signal transduction--Vinexin, CAP/ponsin, ArgBP2]
  JOURNAL   Seikagaku 74 (11), 1356-1360 (2002)
   PUBMED   12510380
  REMARK    GeneRIF: regulates cytoskeletal organization and signal
            transduction--review
            Review article
REFERENCE   9  (residues 1 to 671)
  AUTHORS   Akamatsu,M., Aota,S., Suwa,A., Ueda,K., Amachi,T., Yamada,K.M.,
            Akiyama,S.K. and Kioka,N.
  TITLE     Vinexin forms a signaling complex with Sos and modulates epidermal
            growth factor-induced c-Jun N-terminal kinase/stress-activated
            protein kinase activities
  JOURNAL   J Biol Chem 274 (50), 35933-35937 (1999)
   PUBMED   10585480
REFERENCE   10 (residues 1 to 671)
  AUTHORS   Kioka,N., Sakata,S., Kawauchi,T., Amachi,T., Akiyama,S.K.,
            Okazaki,K., Yaen,C., Yamada,K.M. and Aota,S.
  TITLE     Vinexin: a novel vinculin-binding protein with multiple SH3 domains
            enhances actin cytoskeletal organization
  JOURNAL   J Cell Biol 144 (1), 59-69 (1999)
   PUBMED   9885244
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC091514.1, AF037261.1,
            CF456833.1, BM999851.1 and AC037459.16.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 10, 2007 this sequence version replaced NP_005766.2.
            
            Summary: This gene encodes an SH3 domain-containing adaptor
            protein. The presence of SH3 domains play a role in this protein's
            ability to bind other cytoplasmic molecules and contribute to
            cystoskeletal organization, cell adhesion and migration, signaling,
            and gene expression. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091514.1, AF037261.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000240123.12/ ENSP00000240123.7
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..671
                     /product="vinexin isoform 1"
                     /note="vinexin beta (SH3-containing adaptor molecule-1);
                     sorbin and SH3 domain-containing protein 3"
                     /calculated_mol_wt=75210
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O60504.2)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O60504.2)"
     Region          46..111
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60504.2)"
     Region          <79..>599
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     Region          116..165
                     /region_name="Sorb"
                     /note="Sorbin homologous domain; smart00459"
                     /db_xref="CDD:128735"
     Region          166..215
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60504.2)"
     Region          249..268
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60504.2)"
     Region          295..324
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60504.2)"
     Region          337..383
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60504.2)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60504.2)"
     Region          380..515
                     /region_name="Binds to vinculin"
                     /note="propagated from UniProtKB/Swiss-Prot (O60504.2)"
     Region          383..437
                     /region_name="SH3_Vinexin_1"
                     /note="First Src Homology 3 domain of Vinexin, also called
                     Sorbin and SH3 domain containing 3 (Sorbs3); cd11921"
                     /db_xref="CDD:212854"
     Site            order(389,391,394,398,416..417,430,432..433)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212854"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60504.2)"
     Region          457..512
                     /region_name="SH3_Vinexin_2"
                     /note="Second Src Homology 3 domain of Vinexin, also
                     called Sorbin and SH3 domain containing 3 (Sorbs3);
                     cd11924"
                     /db_xref="CDD:212857"
     Site            order(463,465,468,472,490..491,506,508..509)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212857"
     Region          519..611
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60504.2)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60504.2)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60504.2)"
     Site            545
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O60504.2)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60504.2)"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O60504.2)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O60504.2)"
     Region          612..671
                     /region_name="Binds to SOS"
                     /note="propagated from UniProtKB/Swiss-Prot (O60504.2)"
     Region          614..671
                     /region_name="SH3_Vinexin_3"
                     /note="Third (or C-terminal) Src Homology 3 domain of
                     Vinexin, also called Sorbin and SH3 domain containing 3
                     (Sorbs3); cd11918"
                     /db_xref="CDD:212851"
     Site            order(621,623,626,630,648..649,664,666..667)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212851"
     CDS             1..671
                     /gene="SORBS3"
                     /gene_synonym="SCAM-1; SCAM1; SH3D4"
                     /coded_by="NM_005775.5:152..2167"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6031.1"
                     /db_xref="GeneID:10174"
                     /db_xref="HGNC:HGNC:30907"
                     /db_xref="MIM:610795"
ORIGIN      
        1 mqgpprslra glslddfipg hlqshigsss rgtrvpvirn ggsntlnfqf hdpaprtvcn
       61 ggytprrdas qhpdpawyqt wpgpgskpsa stkipasqht qnwsatwtkd skrrdkrwvk
      121 yegigpvdes gmpiaprssv drprdwyrrm fqqihrkmpd lqldwtfeep prdprhlgaq
      181 qrpahrpgpa tsssgrswdh seelprstfn yrpgafstvl qpsnqvlrrr ekvdnvwtee
      241 swnqflqele tgqrpkkplv ddpgekpsqp ievllerela elsaeldkdl raietrlpsp
      301 ksspaprrap eqrppagpas awsssyphap ylgsarslsp hkmadggspf lgrrdfvyps
      361 strdpsasng ggsparreek krkaarlkfd fqaqspkelt lqkgdivyih kevdknwleg
      421 ehhgrlgifp anyvevlpad eipkpikppt yqvleygeav aqytfkgdle velsfrkgeh
      481 iclirkvnen wyegritgtg rqgifpasyv qvsreprlrl cddgpqlpts prltaaarsa
      541 rhpsspsalr spadpidlgg qtsprrtgfs fptqeprpqt qnlgtpgpal shsrgpshpl
      601 dlgtsspnts qihwtpyram yqyrpqnede lelregdrvd vmqqcddgwf vgvsrrtqkf
      661 gtfpgnyvap v
//
LOCUS       NP_001274671             417 aa            linear   PRI 21-NOV-2025
DEFINITION  squalene synthase isoform 1 [Homo sapiens].
ACCESSION   NP_001274671 XP_005272431
VERSION     NP_001274671.1
DBSOURCE    REFSEQ: accession NM_001287742.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Kanmalar,M., Kamal,R., Abdul Sani,S.F., Pathmanathan,D., Bm
            Said,N.A., Paramanantham,Y., Abd Jamil,A.H., Mun,K.S.,
            Kuppusamy,S., Almugren,K.S., Almajid,H.F. and Bradley,D.A.
  TITLE     Spectroscopic diagnosis and metabolite characterization of
            cisplatin resistance regulated by FDFT1 in bladder cancer tissue
  JOURNAL   Appl Radiat Isot 210, 111372 (2024)
   PUBMED   38810354
  REMARK    GeneRIF: Spectroscopic diagnosis and metabolite characterization of
            cisplatin resistance regulated by FDFT1 in bladder cancer tissue.
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Avci,D., Heidasch,R., Costa,M., Luchtenborg,C., Kale,D., Brugger,B.
            and Lemberg,M.K.
  TITLE     Intramembrane protease SPP defines a cholesterol-regulated
            abundance control of the mevalonate pathway enzyme squalene
            synthase
  JOURNAL   J Biol Chem 300 (2), 105644 (2024)
   PUBMED   38218226
  REMARK    GeneRIF: Intramembrane protease SPP defines a cholesterol-regulated
            abundance control of the mevalonate pathway enzyme squalene
            synthase.
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Jiang,H., Tang,E., Chen,Y., Liu,H., Zhao,Y., Lin,M. and He,L.
  TITLE     Squalene synthase predicts poor prognosis in stage I-III colon
            adenocarcinoma and synergizes squalene epoxidase to promote tumor
            progression
  JOURNAL   Cancer Sci 113 (3), 971-985 (2022)
   PUBMED   34939274
  REMARK    GeneRIF: Squalene synthase predicts poor prognosis in stage I-III
            colon adenocarcinoma and synergizes squalene epoxidase to promote
            tumor progression.
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Nakae,A., Kodama,M., Okamoto,T., Tokunaga,M., Shimura,H.,
            Hashimoto,K., Sawada,K., Kodama,T., Copeland,N.G., Jenkins,N.A. and
            Kimura,T.
  TITLE     Ubiquitin specific peptidase 32 acts as an oncogene in epithelial
            ovarian cancer by deubiquitylating farnesyl-diphosphate
            farnesyltransferase 1
  JOURNAL   Biochem Biophys Res Commun 552, 120-127 (2021)
   PUBMED   33744759
  REMARK    GeneRIF: Ubiquitin specific peptidase 32 acts as an oncogene in
            epithelial ovarian cancer by deubiquitylating farnesyl-diphosphate
            farnesyltransferase 1.
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Guan,G., Jiang,G., Koch,R.L. and Shechter,I.
  TITLE     Molecular cloning and functional analysis of the promoter of the
            human squalene synthase gene
  JOURNAL   J Biol Chem 270 (37), 21958-21965 (1995)
   PUBMED   7665618
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Soltis,D.A., McMahon,G., Caplan,S.L., Dudas,D.A., Chamberlin,H.A.,
            Vattay,A., Dottavio,D., Rucker,M.L., Engstrom,R.G.,
            Cornell-Kennon,S.A. et al.
  TITLE     Expression, purification, and characterization of the human
            squalene synthase: use of yeast and baculoviral systems
  JOURNAL   Arch Biochem Biophys 316 (2), 713-723 (1995)
   PUBMED   7864626
REFERENCE   8  (residues 1 to 417)
  AUTHORS   Shechter,I., Conrad,D.G., Hart,I., Berger,R.C., McKenzie,T.L.,
            Bleskan,J. and Patterson,D.
  TITLE     Localization of the squalene synthase gene (FDFT1) to human
            chromosome 8p22-p23.1
  JOURNAL   Genomics 20 (1), 116-118 (1994)
   PUBMED   8020937
REFERENCE   9  (residues 1 to 417)
  AUTHORS   Jiang,G., McKenzie,T.L., Conrad,D.G. and Shechter,I.
  TITLE     Transcriptional regulation by lovastatin and 25-hydroxycholesterol
            in HepG2 cells and molecular cloning and expression of the cDNA for
            the human hepatic squalene synthase
  JOURNAL   J Biol Chem 268 (17), 12818-12824 (1993)
   PUBMED   7685352
REFERENCE   10 (residues 1 to 417)
  AUTHORS   Coman,D., Vissers,L., Waterham,H., Christodoulou,J., Wevers,R.A.
            and Pitt,J.
  TITLE     Squalene Synthase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   32027475
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC069185.7.
            
            On Dec 19, 2013 this sequence version replaced XP_005272431.1.
            
            Summary: This gene encodes a membrane-associated enzyme located at
            a branch point in the mevalonate pathway. The encoded protein is
            the first specific enzyme in cholesterol biosynthesis, catalyzing
            the dimerization of two molecules of farnesyl diphosphate in a
            two-step reaction to form squalene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript (1) and encodes the longest isoform (1). Variants 1-3
            encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC009251.2, L06105.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968968, SAMEA1970526 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p23.1"
     Protein         1..417
                     /product="squalene synthase isoform 1"
                     /EC_number="2.5.1.21"
                     /note="presqualene-di-diphosphate synthase; squalene
                     synthase; FPP:FPP farnesyltransferase; squalene
                     synthetase"
                     /calculated_mol_wt=47984
     Region          38..370
                     /region_name="squal_synth"
                     /note="farnesyl-diphosphate farnesyltransferase;
                     TIGR01559"
                     /db_xref="CDD:188157"
     Site            order(50..54,315..318)
                     /site_type="active"
                     /note="active site lid residues [active]"
                     /db_xref="CDD:173831"
     Site            order(52,54,73,77,80,84,171,176,180,208,211,218..219,
                     222..223,228,288..289)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:173831"
     Site            order(54,73,80,84,171,179,183,211,218..219,223,228,
                     288..289,293)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:173831"
     Site            order(80..84,219..223)
                     /site_type="active"
                     /note="substrate-Mg2+ binding site [active]"
                     /db_xref="CDD:173831"
     Site            80..84
                     /site_type="other"
                     /note="aspartate-rich region 1"
                     /db_xref="CDD:173831"
     Site            219..223
                     /site_type="other"
                     /note="aspartate-rich region 2"
                     /db_xref="CDD:173831"
     Site            284..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P37268.1)"
     Site            384..404
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P37268.1)"
     CDS             1..417
                     /gene="FDFT1"
                     /gene_synonym="DGPT; ERG9; SQS; SQSD; SS"
                     /coded_by="NM_001287742.2:703..1956"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5985.1"
                     /db_xref="GeneID:2222"
                     /db_xref="HGNC:HGNC:3629"
                     /db_xref="MIM:184420"
ORIGIN      
        1 mefvkclghp eefynlvrfr iggkrkvmpk mdqdslsssl ktcykylnqt srsfaaviqa
       61 ldgemrnavc ifylvlrald tleddmtisv ekkvpllhnf hsflyqpdwr fmeskekdrq
      121 vledfptisl efrnlaekyq tviadicrrm gigmaefldk hvtseqewdk ychyvaglvg
      181 iglsrlfsas efedplvged teransmglf lqktniirdy ledqqggref wpqevwsryv
      241 kklgdfakpe nidlavqcln elitnalhhi pdvitylsrl rnqsvfnfca ipqvmaiatl
      301 aacynnqqvf kgavkirkgq avtlmmdatn mpavkaiiyq ymeeiyhrip dsdpsssktr
      361 qiistirtqn lpncqlisrs hyspiylsfv mllaalswqy lttlsqvted yvqtgeh
//
LOCUS       NP_001032955             904 aa            linear   PRI 21-NOV-2025
DEFINITION  RANBP2-like and GRIP domain-containing protein 5/6 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001032955 XP_005263814
VERSION     NP_001032955.1
DBSOURCE    REFSEQ: accession NM_001037866.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 904)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 904)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 904)
  AUTHORS   Sugis,E., Dauvillier,J., Leontjeva,A., Adler,P., Hindie,V.,
            Moncion,T., Collura,V., Daudin,R., Loe-Mie,Y., Herault,Y.,
            Lambert,J.C., Hermjakob,H., Pupko,T., Rain,J.C., Xenarios,I.,
            Vilo,J., Simonneau,M. and Peterson,H.
  TITLE     HENA, heterogeneous network-based data set for Alzheimer's disease
  JOURNAL   Sci Data 6 (1), 151 (2019)
   PUBMED   31413325
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 904)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 904)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 904)
  AUTHORS   Dephoure,N., Zhou,C., Villen,J., Beausoleil,S.A., Bakalarski,C.E.,
            Elledge,S.J. and Gygi,S.P.
  TITLE     A quantitative atlas of mitotic phosphorylation
  JOURNAL   Proc Natl Acad Sci U S A 105 (31), 10762-10767 (2008)
   PUBMED   18669648
REFERENCE   7  (residues 1 to 904)
  AUTHORS   Cantin,G.T., Yi,W., Lu,B., Park,S.K., Xu,T., Lee,J.D. and
            Yates,J.R. 3rd.
  TITLE     Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
            efficient phosphoproteomic analysis
  JOURNAL   J Proteome Res 7 (3), 1346-1351 (2008)
   PUBMED   18220336
REFERENCE   8  (residues 1 to 904)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   9  (residues 1 to 904)
  AUTHORS   Ciccarelli,F.D., von Mering,C., Suyama,M., Harrington,E.D.,
            Izaurralde,E. and Bork,P.
  TITLE     Complex genomic rearrangements lead to novel primate gene function
  JOURNAL   Genome Res 15 (3), 343-351 (2005)
   PUBMED   15710750
REFERENCE   10 (residues 1 to 904)
  AUTHORS   Nothwang,H.G., Rensing,C., Kubler,M., Denich,D., Brandl,B.,
            Stubanus,M., Haaf,T., Kurnit,D. and Hildebrandt,F.
  TITLE     Identification of a novel Ran binding protein 2 related gene
            (RANBP2L1) and detection of a gene cluster on human chromosome
            2q11-q12
  JOURNAL   Genomics 47 (3), 383-392 (1998)
   PUBMED   9480752
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC226101.3 and AC108938.3.
            
            On Aug 31, 2013 this sequence version replaced XP_005263814.1.
            
            Transcript Variant: This variant (2) uses an alternate splice
            pattern in the 3' coding region and 3' UTR, compared to variant 1.
            The resulting isoform (2) has a substantially shorter and distinct
            C-terminus, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.2741652.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..904
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..904
                     /product="RANBP2-like and GRIP domain-containing protein
                     5/6 isoform 2"
                     /note="RANBP2-like and GRIP domain-containing protein 7;
                     RANBP2-like and GRIP domain-containing protein 5/6;
                     ranBP2-like 1/2; ran-binding protein 2-like 1/2"
                     /calculated_mol_wt=103203
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q99666.3)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99666.3)"
     Region          26..59
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99666.3)"
     Region          <33..222
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(34..35,37,61,64..65,68..69,71..72,95,98..99,
                     102..103,106)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          59..89
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          60..93
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99666.3)"
     Region          648..681
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99666.3)"
     Region          760..804
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99666.3)"
     CDS             1..904
                     /gene="RGPD6"
                     /gene_synonym="RanBP2L1; RanBP2L2; RGP6; RGPD7"
                     /coded_by="NM_001037866.2:199..2913"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42729.1"
                     /db_xref="GeneID:729540"
                     /db_xref="HGNC:HGNC:32419"
                     /db_xref="MIM:612709"
ORIGIN      
        1 mrrskadver yvasvlgltp sprqksmkgf yfaklyyeak eydlakkyic tyinvqerdp
       61 kahrflglly eleentekav ecyrrsveln ptqkdlvlki aellckndvt dgrakywver
      121 aaklfpgspa iyklkeqlld cegedgwnkl fdliqselyv rpddvhvnir lvelyrstkr
      181 lkdavahche aernialrss lewnscvvqt lkeyleslqc lesdksdwqa tntdlllaya
      241 nlmlltlstr dvqenrelle sfdsalqsak sslggndels atflemkghf ymyagslllk
      301 mgqhgnnvqw ralselaalc yliafqvprp kiklregkag qnllemmacd rlsqsghmll
      361 slsrgkqdfl kevvetfank igqsalydal fssqspkdts flgsddigki dvqepeledl
      421 arydvgaira hngslqhltw lglqwnslpa lpgirkwlkq lfhrlphets rletnapesi
      481 cildlevfll gvvytshlql kekcnshhss yqplclpfpv ckqlcterqk swwdavctli
      541 hrkavpgnla klrllvqhei ntlraqekhg lqpallvhwa kylqktgsgl nsfygqleyi
      601 grsvhywkkv lpllkiikkn sipepidplf khfhsvdiqa seiveyeeda hitfamldav
      661 ngniedavta fesiksvvsy wnlalifhrk aediendals peeqeecrny ltktrdylik
      721 iiddgdsnls vvkklpvple svkqmlnsvm qeledysegg plykngslrn adseikhstp
      781 sptkyslsps ksykyspetp prwtedrnsl lnmicqqvea ikkemqelkl nssksasrhr
      841 wptenygpds vpdgyqgsqt fhgaplteaa hrhftiekhg dskwiiyrft kqlcgterar
      901 akis
//
LOCUS       NP_001186709              84 aa            linear   PRI 21-NOV-2025
DEFINITION  proteasome subunit beta type-2 isoform 3 [Homo sapiens].
ACCESSION   NP_001186709
VERSION     NP_001186709.1
DBSOURCE    REFSEQ: accession NM_001199780.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   3  (residues 1 to 84)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   4  (residues 1 to 84)
  AUTHORS   Zivkovic,D., Sanchez Dafun,A., Menneteau,T., Schahl,A., Lise,S.,
            Kervarrec,C., Toste Rego,A., da Fonseca,P.C.A., Chavent,M.,
            Pineau,C., Burlet-Schiltz,O., Marcoux,J. and Bousquet,M.P.
  TITLE     Proteasome complexes experience profound structural and functional
            rearrangements throughout mammalian spermatogenesis
  JOURNAL   Proc Natl Acad Sci U S A 119 (15), e2116826119 (2022)
   PUBMED   35377789
REFERENCE   5  (residues 1 to 84)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 84)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   7  (residues 1 to 84)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   8  (residues 1 to 84)
  AUTHORS   Nothwang,H.G., Tamura,T., Tanaka,K. and Ichihara,A.
  TITLE     Sequence analyses and inter-species comparisons of three novel
            human proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine
            potential proteolytic active-site residues
  JOURNAL   Biochim Biophys Acta 1219 (2), 361-368 (1994)
   PUBMED   7918633
REFERENCE   9  (residues 1 to 84)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 84)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK310023.1, AL157951.5 and
            BM664618.1.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            member of the proteasome B-type family, also known as the T1B
            family, that is a 20S core beta subunit. Multiple alternatively
            spliced transcript variants encoding distinct isoforms have been
            found for this gene. [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (3) lacks two exons from the 5'
            end and has an alternate 5' exon, as compared to variant 1. The
            resulting isoform (3) is shorter at the N-terminus, as compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK310023.1, DA917638.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..84
                     /product="proteasome subunit beta type-2 isoform 3"
                     /EC_number="3.4.25.1"
                     /note="macropain subunit C7-I; multicatalytic
                     endopeptidase complex subunit C7-1; proteasome component
                     C7-I; proteasome subunit, beta type, 2; proteasome beta 2
                     subunit; multicatalytic endopeptidase complex subunit
                     C7-I; proteasome subunit beta 2; proteasome subunit beta4;
                     beta-4; proteasome (prosome, macropain) subunit, beta
                     type, 2; testicular tissue protein Li 152; proteasome
                     subunit beta-4"
                     /calculated_mol_wt=9426
     Region          <1..75
                     /region_name="Ntn_hydrolase"
                     /note="The Ntn hydrolases (N-terminal nucleophile) are a
                     diverse superfamily of of enzymes that are activated
                     autocatalytically via an N-terminally lcated nucleophilic
                     amino acid. N-terminal nucleophile (NTN-) hydrolase
                     superfamily, which contains a...; cl00467"
                     /db_xref="CDD:469781"
     CDS             1..84
                     /gene="PSMB2"
                     /gene_synonym="HC7-I"
                     /coded_by="NM_001199780.2:240..494"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS72755.1"
                     /db_xref="GeneID:5690"
                     /db_xref="HGNC:HGNC:9539"
                     /db_xref="MIM:602175"
ORIGIN      
        1 mdylaalaka pfaahgygaf ltlsildryy tptisrerav ellrkcleel qkrfilnlpt
       61 fsvriidkng ihdldnisfp kqgs
//
LOCUS       NP_001381783             560 aa            linear   PRI 21-NOV-2025
DEFINITION  kinesin light chain 1 isoform 26 [Homo sapiens].
ACCESSION   NP_001381783
VERSION     NP_001381783.1
DBSOURCE    REFSEQ: accession NM_001394854.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 560)
  AUTHORS   Kikuchi,M., Viet,J., Nagata,K., Sato,M., David,G., Audic,Y.,
            Silverman,M.A., Yamamoto,M., Akatsu,H., Hashizume,Y., Takeda,S.,
            Akamine,S., Miyamoto,T., Uozumi,R., Gotoh,S., Mori,K., Ikeda,M.,
            Paillard,L. and Morihara,T.
  TITLE     Gene-gene functional relationships in Alzheimer's disease: CELF1
            regulates KLC1 alternative splicing
  JOURNAL   Biochem Biophys Res Commun 721, 150025 (2024)
   PUBMED   38768546
  REMARK    GeneRIF: Gene-gene functional relationships in Alzheimer's disease:
            CELF1 regulates KLC1 alternative splicing.
REFERENCE   4  (residues 1 to 560)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 560)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   6  (residues 1 to 560)
  AUTHORS   Gyoeva,F.K., Bybikova,E.M. and Minin,A.A.
  TITLE     An isoform of kinesin light chain specific for the Golgi complex
  JOURNAL   J Cell Sci 113 (Pt 11), 2047-2054 (2000)
   PUBMED   10806115
REFERENCE   7  (residues 1 to 560)
  AUTHORS   Khodjakov,A., Lizunova,E.M., Minin,A.A., Koonce,M.P. and
            Gyoeva,F.K.
  TITLE     A specific light chain of kinesin associates with mitochondria in
            cultured cells
  JOURNAL   Mol Biol Cell 9 (2), 333-343 (1998)
   PUBMED   9450959
REFERENCE   8  (residues 1 to 560)
  AUTHORS   Chernajovsky,Y., Brown,A. and Clark,J.
  TITLE     Human kinesin light (beta) chain gene: DNA sequence and functional
            characterization of its promoter and first exon
  JOURNAL   DNA Cell Biol 15 (11), 965-974 (1996)
   PUBMED   8945637
REFERENCE   9  (residues 1 to 560)
  AUTHORS   Goedert,M., Marsh,S. and Carter,N.
  TITLE     Localization of the human kinesin light chain gene (KNS2) to
            chromosome 14q32.3 by fluorescence in situ hybridization
  JOURNAL   Genomics 32 (1), 173-175 (1996)
   PUBMED   8786116
REFERENCE   10 (residues 1 to 560)
  AUTHORS   Cabeza-Arvelaiz,Y., Shih,L.C., Hardman,N., Asselbergs,F., Bilbe,G.,
            Schmitz,A., White,B., Siciliano,M.J. and Lachman,L.B.
  TITLE     Cloning and genetic characterization of the human kinesin
            light-chain (KLC) gene
  JOURNAL   DNA Cell Biol 12 (10), 881-892 (1993)
   PUBMED   8274221
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139300.6 and AL049840.8.
            
            Summary: Conventional kinesin is a tetrameric molecule composed of
            two heavy chains and two light chains, and transports various
            cargos along microtubules toward their plus ends. The heavy chains
            provide the motor activity, while the light chains bind to various
            cargos. This gene encodes a member of the kinesin light chain
            family. It associates with kinesin heavy chain through an
            N-terminal domain, and six tetratricopeptide repeat (TPR) motifs
            are thought to be involved in binding of cargos such as vesicles,
            mitochondria, and the Golgi complex. Thus, kinesin light chains
            function as adapter molecules and not motors per se. Although
            previously named 'kinesin 2', this gene is not a member of the
            kinesin-2 / kinesin heavy chain subfamily of kinesin motor
            proteins. Extensive alternative splicing produces isoforms with
            different C-termini that are proposed to bind to different cargos;
            however, the full-length nature and/or biological validity of most
            of these variants have not been determined. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1738561.1,
                                           SRR14038196.2427202.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..560
                     /product="kinesin light chain 1 isoform 26"
                     /EC_number="2.7.1.21"
                     /note="kinesin 2 60/70kDa; medulloblastoma antigen
                     MU-MB-2.50"
                     /calculated_mol_wt=63612
     Region          35..>149
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          155..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P37285; propagated from
                     UniProtKB/Swiss-Prot (Q07866.2)"
     Region          210..435
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          213..246
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Region          214..241
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          255..288
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Region          255..283
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          297..330
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Region          297..325
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(298,301..302,305..306,308,340,343..344,347..348,
                     350..351,382,385..386,389..390,393)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          338..368
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          339..372
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Region          381..414
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Region          381..408
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O88447; propagated from
                     UniProtKB/Swiss-Prot (Q07866.2)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:21385839; propagated from
                     UniProtKB/Swiss-Prot (Q07866.2)"
     Region          464..497
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:20074060; propagated from
                     UniProtKB/Swiss-Prot (Q07866.2)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:20074060; propagated from
                     UniProtKB/Swiss-Prot (Q07866.2)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     CDS             1..560
                     /gene="KLC1"
                     /gene_synonym="KLC; KNS2; KNS2A"
                     /coded_by="NM_001394854.1:286..1968"
                     /note="isoform 26 is encoded by transcript variant 26"
                     /db_xref="GeneID:3831"
                     /db_xref="HGNC:HGNC:6387"
                     /db_xref="MIM:600025"
ORIGIN      
        1 mydnmstmvy ikedkleklt qdeiisktkq viqglealkn ehnsilqsll etlkclkkdd
       61 esnlveeksn mirkslemle lglseaqvmm alsnhlnave sekqklraqv rrlcqenqwl
      121 rdelantqqk lqkseqsvaq leeekkhlef mnqlkkyddd ispsedkdtd stkeplddlf
      181 pndeddpgqg iqqqhssaaa aaqqggyeip arlrtlhnlv iqyasqgrye vavplckqal
      241 edlektsghd hpdvatmlni lalvyrdqnk ykdaanllnd alairektlg kdhpavaatl
      301 nnlavlygkr gkykeaeplc kraleirekv lgkdhpdvak qlnnlallcq nqgkyeevey
      361 yyqraleiyq tklgpddpnv aktknnlasc ylkqgkfkqa etlykeiltr aherefgsvd
      421 denkpiwmha eereeckgkq kdgtsfgeyg gwykackvds ptvtttlknl galyrrqgkf
      481 eaaetleeaa mrsrkqgldn vhkqrvaevl ndpenmekrr sreslnvdvv kyesgpdgge
      541 evsmsvewng heacqlsecp
//
LOCUS       NP_001171701            1785 aa            linear   PRI 21-NOV-2025
DEFINITION  BCL-6 corepressor-like protein 1 isoform 1a [Homo sapiens].
ACCESSION   NP_001171701 XP_005262509
VERSION     NP_001171701.1
DBSOURCE    REFSEQ: accession NM_001184772.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1785)
  AUTHORS   Luo,C., Chen,Z., Meng,L., Tan,C., He,W., Tu,C., Du,J., Lu,G.X.,
            Lin,G., Tan,Y.Q. and Hu,T.Y.
  TITLE     A hemizygous loss-of-function variant in BCORL1 is associated with
            male infertility and oligoasthenoteratozoospermia
  JOURNAL   Clin Genet 106 (1), 27-36 (2024)
   PUBMED   38342987
  REMARK    GeneRIF: A hemizygous loss-of-function variant in BCORL1 is
            associated with male infertility and oligoasthenoteratozoospermia.
REFERENCE   2  (residues 1 to 1785)
  AUTHORS   Kommoss,F.K.F., Chiang,S., Kobel,M., Koelsche,C., Chang,K.T.,
            Irving,J.A., Dickson,B., Thiryayi,S., Rouzbahman,M., Rasty,G., von
            Deimling,A., Lee,C.H. and Turashvili,G.
  TITLE     Endometrial Stromal Sarcomas With BCOR Internal Tandem Duplication
            and Variant BCOR/BCORL1 Rearrangements Resemble High-grade
            Endometrial Stromal Sarcomas With Recurrent CDK4 Pathway
            Alterations and MDM2 Amplifications
  JOURNAL   Am J Surg Pathol 46 (8), 1142-1152 (2022)
   PUBMED   35499168
  REMARK    GeneRIF: Endometrial Stromal Sarcomas With BCOR Internal Tandem
            Duplication and Variant BCOR/BCORL1 Rearrangements Resemble
            High-grade Endometrial Stromal Sarcomas With Recurrent CDK4 Pathway
            Alterations and MDM2 Amplifications.
REFERENCE   3  (residues 1 to 1785)
  AUTHORS   Schaefer,E.J., Wang,H.C., Karp,H.Q., Meyer,C.A., Cejas,P.,
            Gearhart,M.D., Adelman,E.R., Fares,I., Apffel,A., Lim,K., Xie,Y.,
            Gibson,C.J., Schenone,M., Murdock,H.M., Wang,E.S., Gondek,L.P.,
            Carroll,M.P., Vedula,R.S., Winer,E.S., Garcia,J.S., Stone,R.M.,
            Luskin,M.R., Carr,S.A., Long,H.W., Bardwell,V.J., Figueroa,M.E. and
            Lindsley,R.C.
  TITLE     BCOR and BCORL1 Mutations Drive Epigenetic Reprogramming and
            Oncogenic Signaling by Unlinking PRC1.1 from Target Genes
  JOURNAL   Blood Cancer Discov 3 (2), 116-135 (2022)
   PUBMED   35015684
  REMARK    GeneRIF: BCOR and BCORL1 Mutations Drive Epigenetic Reprogramming
            and Oncogenic Signaling by Unlinking PRC1.1 from Target Genes.
REFERENCE   4  (residues 1 to 1785)
  AUTHORS   Gafner,M., Michelson,M., Argilli,E., Yosovich,K., Sherr,E.H.,
            Parks,K.C., England,E.M., Hady-Cohen,R., Leibovitz,Z., Lev,D.,
            Michaeli-Yosef,Y., Lerman-Sagie,T. and Blumkin,L.
  TITLE     Major brain malformations: corpus callosum dysgenesis, agenesis of
            septum pellucidum and polymicrogyria in patients with
            BCORL1-related disorders
  JOURNAL   J Hum Genet 67 (2), 95-101 (2022)
   PUBMED   34400773
  REMARK    GeneRIF: Major brain malformations: corpus callosum dysgenesis,
            agenesis of septum pellucidum and polymicrogyria in patients with
            BCORL1-related disorders.
REFERENCE   5  (residues 1 to 1785)
  AUTHORS   Junco,S.E., Wang,R., Gaipa,J.C., Taylor,A.B., Schirf,V.,
            Gearhart,M.D., Bardwell,V.J., Demeler,B., Hart,P.J. and Kim,C.A.
  TITLE     Structure of the polycomb group protein PCGF1 in complex with BCOR
            reveals basis for binding selectivity of PCGF homologs
  JOURNAL   Structure 21 (4), 665-671 (2013)
   PUBMED   23523425
REFERENCE   6  (residues 1 to 1785)
  AUTHORS   Shaffer,J.R., Feingold,E., Wang,X., Lee,M., Tcuenco,K., Weeks,D.E.,
            Weyant,R.J., Crout,R., McNeil,D.W. and Marazita,M.L.
  TITLE     GWAS of dental caries patterns in the permanent dentition
  JOURNAL   J Dent Res 92 (1), 38-44 (2013)
   PUBMED   23064961
REFERENCE   7  (residues 1 to 1785)
  AUTHORS   Gao,Z., Zhang,J., Bonasio,R., Strino,F., Sawai,A., Parisi,F.,
            Kluger,Y. and Reinberg,D.
  TITLE     PCGF homologs, CBX proteins, and RYBP define functionally distinct
            PRC1 family complexes
  JOURNAL   Mol Cell 45 (3), 344-356 (2012)
   PUBMED   22325352
REFERENCE   8  (residues 1 to 1785)
  AUTHORS   Li,M., Collins,R., Jiao,Y., Ouillette,P., Bixby,D., Erba,H.,
            Vogelstein,B., Kinzler,K.W., Papadopoulos,N. and Malek,S.N.
  TITLE     Somatic mutations in the transcriptional corepressor gene BCORL1 in
            adult acute myelogenous leukemia
  JOURNAL   Blood 118 (22), 5914-5917 (2011)
   PUBMED   21989985
  REMARK    GeneRIF: BCORL1 by genetic criteria is a novel candidate tumor
            suppressor gene, joining the growing list of genes recurrently
            mutated in acute myelogenous leukemia.
REFERENCE   9  (residues 1 to 1785)
  AUTHORS   Pagan,J.K., Arnold,J., Hanchard,K.J., Kumar,R., Bruno,T.,
            Jones,M.J., Richard,D.J., Forrest,A., Spurdle,A., Verdin,E.,
            Crossley,M., Fanciulli,M., Chenevix-Trench,G., Young,D.B. and
            Khanna,K.K.
  TITLE     A novel corepressor, BCoR-L1, represses transcription through an
            interaction with CtBP
  JOURNAL   J Biol Chem 282 (20), 15248-15257 (2007)
   PUBMED   17379597
REFERENCE   10 (residues 1 to 1785)
  AUTHORS   Lose,F., Arnold,J., Young,D.B., Brown,C.J., Mann,G.J., Pupo,G.M.,
            Khanna,K.K., Chenevix-Trench,G. and Spurdle,A.B.
  CONSRTM   Kathleen Cuningham Foundation Consortium for Research into Familial
            Breast Cancer
  TITLE     BCoR-L1 variation and breast cancer
  JOURNAL   Breast Cancer Res 9 (4), R54 (2007)
   PUBMED   17697391
  REMARK    GeneRIF: Dysregulated BCoR-L1 expression is associated with breast
            cancer
            Erratum:[Breast Cancer Res. 2008;10(5):406]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL034405.16, Z82208.1,
            KF459400.1 and AL136450.8.
            
            On Apr 2, 2020 this sequence version replaced XP_005262509.2.
            
            Summary: The protein encoded by this gene is a transcriptional
            corepressor that is found tethered to promoter regions by
            DNA-binding proteins. The encoded protein can interact with several
            different class II histone deacetylases to repress transcription.
            Two transcript variants encoding different isoforms have been found
            for this gene. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1998757.1,
                                           SRR14038195.2780982.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1785
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.1"
     Protein         1..1785
                     /product="BCL-6 corepressor-like protein 1 isoform 1a"
                     /note="BCoR-like protein 1"
                     /calculated_mol_wt=190431
     Region          65..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          113..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          <198..636
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          343..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          527..550
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          562..646
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          753..781
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          876..901
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          937..977
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1029
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1033
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1107..1293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1312..1487
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1328..1336
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          <1494..>1603
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1496..1527
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1497,1501..1502,1505..1507,1509..1510,1514,1517,
                     1527,1529,1531,1535..1536,1539..1541,1543..1544,1548,1551,
                     1560,1562,1564,1568..1569,1572..1574,1576..1577,1581,1584)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1529..1560
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1529..1558
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1562..1591
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1562..1591
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1595..1623
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1666..1779
                     /region_name="PUFD_like_1"
                     /note="PCGF Ub-like fold discriminator of BCOR-like 1;
                     cd14260"
                     /db_xref="CDD:271223"
     Region          1668..1785
                     /region_name="PCGF Ub-like fold domain (PUFD), required
                     for the interaction with the KDM2B-SKP1 heterodimeric
                     complex. /evidence=ECO:0000269|PubMed:27568929"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            order(1668,1670..1680,1682,1684,1693..1695,1697,
                     1738..1739,1741,1744,1766,1777,1779)
                     /site_type="other"
                     /note="RAWUL domain interface [polypeptide binding]"
                     /db_xref="CDD:271223"
     CDS             1..1785
                     /gene="BCORL1"
                     /gene_synonym="BCoR-L1; CXorf10; SHUVER"
                     /coded_by="NM_001184772.3:480..5837"
                     /note="isoform 1a is encoded by transcript variant 1a"
                     /db_xref="CCDS:CCDS94663.1"
                     /db_xref="GeneID:63035"
                     /db_xref="HGNC:HGNC:25657"
                     /db_xref="MIM:300688"
ORIGIN      
        1 mistaplysg vhnwtssdri rmcgineerr aplsdeestt gdcqhfgsqe fcvsssfskv
       61 eltavgsgsn argadpdgsa teklghksed kpddpqpkmd yagnvaeaeg llvplsspgd
      121 glklpasdsa easnsradcs wtplntqmsk qvdcspagvk aldsrqgvge kntfilatlg
      181 tgvpvegtlp lvttnfsplp apicppapgs asvphsvpda fqvplsvpap vphsglvpvq
      241 vatsvpapsp plapvpalap appsvptlis dsnplsvsas vlvpvpasap psgpvplsap
      301 apaplsvpvs applaliqap vppsaptlvl apvptpvlap mpastppaap appsvpmptp
      361 tpssgppstp tlipafaptp vpaptpapif tpaptpmpaa tpaaiptsap ipasfslsrv
      421 cfpaaqapam qkvplsfqpg tvltpsqplv yipppscgqp lsvatlpttl gvsstltlpv
      481 lpsylqdrcl pgvlaspelr sypyafsvar pltsdsklvs levnrlpcts psgstttqpa
      541 pdgvpgplad tslvtasakv lptpqpllpa psgssapphp akmpsgteqq tegtsvtfsp
      601 lksppqlere masppecsem pldlssksnr qklplpnqrk tppmpvltpv htsskallst
      661 vlsrsqrttq aaggnvtscl gstsspfvif peivrngdps twvknstali stipgtyvgv
      721 anpvpaslll nkdpnlglnr dprhlpkqep isiidqgepk gtgatcgkkg sqagaegqps
      781 tvkrytpari apglpgcqtk elslwkptgp aniyprcsvn gkptstqvlp vgwspyhqas
      841 llsigissag qltpsqgapi rptsvvsefs gvpslsssea vhglpegqpr pggsfvpeqd
      901 pvtknktcri aakpyeeqvn pvlltlspqt gtlalsvqps ggdirmnqgp eeseshlcsd
      961 stpkmegpqg acglklagdt kpknqvlaty mshelvlatp qnlpkmpelp llphdshpke
     1021 lildvvpssr rgssterpql gsqvdlgrvk mekvdgdvvf nlatcfradg lpvapqrgqa
     1081 evrakagqar vkqesvgvfa cknkwqpddv teslppkkmk cgkekdseeq qlqpqakavv
     1141 rsshrpkcrk lpsdpqestk ksprgasdsg kehngvrgkh khrkptkpes qspgkradsh
     1201 eegslekkak ssfrdfipvv lstrtrsqsg sicssfagma dsdmgsqevf pteeeeevtp
     1261 tpakrrkvrk tqrdtqyrsh haqdksllsq grrhlwrare mpwrteaarq mwdtneeeee
     1321 eeeegllkrk krrrqksrky qtgeylteqe deqrrkgrad lkarkqktss sqslehrlrn
     1381 rnlllpnkvq gisdspngfl pnnleepacl ensekpsgkr kcktkhmatv seeakgkgrw
     1441 sqqktrspks ptpvkptepc tpsksrsass eeasesptar qippearrli vnknagetll
     1501 qraarlgykd vvlyclqkds edvnhrdnag ytalheacsr gwtdilnill ehganvncsa
     1561 qdgtrpvhda vvndnletiw lllsygadpt latysgqtam klassdtmkr flsdhlsdlq
     1621 graegdpgvs wdfysssvle ekdgfacdll hnppgssdqe gddpmeeddf mfelsdkpll
     1681 pcynlqvsvs rgpcnwflfs dvlkrlklss rifqarfphf eittmpkaef yrqvassqll
     1741 tpaerpggld drsppgsset velvryepdl lrllgsevef qscns
//
LOCUS       NP_001288721             192 aa            linear   PRI 21-NOV-2025
DEFINITION  tRNA N(3)-cytidine methyltransferase METTL6 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001288721
VERSION     NP_001288721.1
DBSOURCE    REFSEQ: accession NM_001301792.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Throll,P., G Dolce,L., Rico-Lastres,P., Arnold,K., Tengo,L.,
            Basu,S., Kaiser,S., Schneider,R. and Kowalinski,E.
  TITLE     Structural basis of tRNA recognition by the m3C RNA
            methyltransferase METTL6 in complex with SerRS seryl-tRNA
            synthetase
  JOURNAL   Nat Struct Mol Biol 31 (10), 1614-1624 (2024)
   PUBMED   38918637
  REMARK    Erratum:[Nat Struct Mol Biol. 2025 Feb;32(2):405. doi:
            10.1038/s41594-025-01508-6. PMID: 39905155]
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Li,S., Zhou,H., Liao,S., Wang,X., Zhu,Z., Zhang,J. and Xu,C.
  TITLE     Structural basis for METTL6-mediated m3C RNA methylation
  JOURNAL   Biochem Biophys Res Commun 589, 159-164 (2022)
   PUBMED   34922197
  REMARK    GeneRIF: Structural basis for METTL6-mediated m3C RNA methylation.
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Chen,R., Zhou,J., Liu,L., Mao,X.L., Zhou,X. and Xie,W.
  TITLE     Crystal structure of human METTL6, the m3C methyltransferase
  JOURNAL   Commun Biol 4 (1), 1361 (2021)
   PUBMED   34862464
  REMARK    GeneRIF: Crystal structure of human METTL6, the m(3)C
            methyltransferase.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Mao,X.L., Li,Z.H., Huang,M.H., Wang,J.T., Zhou,J.B., Li,Q.R.,
            Xu,H., Wang,X.J. and Zhou,X.L.
  TITLE     Mutually exclusive substrate selection strategy by human m3C RNA
            transferases METTL2A and METTL6
  JOURNAL   Nucleic Acids Res 49 (14), 8309-8323 (2021)
   PUBMED   34268557
  REMARK    GeneRIF: Mutually exclusive substrate selection strategy by human
            m3C RNA transferases METTL2A and METTL6.
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Ignatova,V.V., Kaiser,S., Ho,J.S.Y., Bing,X., Stolz,P., Tan,Y.X.,
            Lee,C.L., Gay,F.P.H., Lastres,P.R., Gerlini,R., Rathkolb,B.,
            Aguilar-Pimentel,A., Sanz-Moreno,A., Klein-Rodewald,T.,
            Calzada-Wack,J., Ibragimov,E., Valenta,M., Lukauskas,S., Pavesi,A.,
            Marschall,S., Leuchtenberger,S., Fuchs,H., Gailus-Durner,V., de
            Angelis,M.H., Bultmann,S., Rando,O.J., Guccione,E., Kellner,S.M.
            and Schneider,R.
  TITLE     METTL6 is a tRNA m3C methyltransferase that regulates pluripotency
            and tumor cell growth
  JOURNAL   Sci Adv 6 (35), eaaz4551 (2020)
   PUBMED   32923617
  REMARK    GeneRIF: METTL6 is a tRNA m(3)C methyltransferase that regulates
            pluripotency and tumor cell growth.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 192)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 192)
  AUTHORS   Xu,L., Liu,X., Sheng,N., Oo,K.S., Liang,J., Chionh,Y.H., Xu,J.,
            Ye,F., Gao,Y.G., Dedon,P.C. and Fu,X.Y.
  TITLE     Three distinct 3-methylcytidine (m3C) methyltransferases modify
            tRNA and mRNA in mice and humans
  JOURNAL   J Biol Chem 292 (35), 14695-14703 (2017)
   PUBMED   28655767
  REMARK    GeneRIF: Data, including data from studies using mutant/knockout
            mice and cell lines from such mice, suggest that METTL2 and METTL6
            (but not METTL8) contribute to post-transcriptional methylation of
            cytidine (formation of 3-methylcytidine) in tRNA; METTL2 methylates
            tRNA(Thr) and tRNA(Arg); METTL6 interacts with seryl-tRNA
            synthetase and methylates tRNA(Ser); METTL8 catalyzes
            post-transcriptional methylation of cytidine in mRNA.
REFERENCE   8  (residues 1 to 192)
  AUTHORS   Fleming,I.M., Paris,Z., Gaston,K.W., Balakrishnan,R., Fredrick,K.,
            Rubio,M.A. and Alfonzo,J.D.
  TITLE     A tRNA methyltransferase paralog is important for ribosome
            stability and cell division in Trypanosoma brucei
  JOURNAL   Sci Rep 6, 21438 (2016)
   PUBMED   26888608
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 192)
  AUTHORS   McArdle,P.F., Parsa,A., Chang,Y.P., Weir,M.R., O'Connell,J.R.,
            Mitchell,B.D. and Shuldiner,A.R.
  TITLE     Association of a common nonsynonymous variant in GLUT9 with serum
            uric acid levels in old order amish
  JOURNAL   Arthritis Rheum 58 (9), 2874-2881 (2008)
   PUBMED   18759275
REFERENCE   10 (residues 1 to 192)
  AUTHORS   Auffray,C., Behar,G., Bois,F., Bouchier,C., Da Silva,C.,
            Devignes,M.D., Duprat,S., Houlgatte,R., Jumeau,M.N., Lamy,B. et al.
  TITLE     [IMAGE: molecular integration of the analysis of the human genome
            and its expression]
  JOURNAL   C R Acad Sci III 318 (2), 263-272 (1995)
   PUBMED   7757816
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG701912.1, AC027125.5, BC022400.1, BI913767.1, CX872865.1 and
            Z44406.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            lacks an exon in the 3' coding region, which results in a
            frameshift and an early stop codon, compared to variant 1. The
            encoded isoform (4) is shorter and has a distinct C-terminus,
            compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI913767.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.1"
     Protein         1..192
                     /product="tRNA N(3)-cytidine methyltransferase METTL6
                     isoform 4"
                     /EC_number="2.1.1.-"
                     /note="methyltransferase-like protein 6; tRNA
                     N(3)-methylcytidine methyltransferase METTL6;
                     methyltransferase like 6; methyltransferase 6,
                     methylcytidine; methyltransferase 6, RNA N3-cytidine; tRNA
                     N(3)-cytidine methyltransferase METTL6"
                     /calculated_mol_wt=22635
     Region          84..177
                     /region_name="Methyltransf_12"
                     /note="Methyltransferase domain; pfam08242"
                     /db_xref="CDD:400515"
     Site            order(86..92,110..111,135..137,157)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
     CDS             1..192
                     /gene="METTL6"
                     /gene_synonym="hMETTL6"
                     /coded_by="NM_001301792.2:296..874"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:131965"
                     /db_xref="HGNC:HGNC:28343"
                     /db_xref="MIM:618903"
ORIGIN      
        1 maslqrkglq ariltseeee klkrdqtlvs dfkqqkleqe aqknwdlfyk rnstnffkdr
       61 hwttrefeel rscrefedqk ltmleagcgv gnclfpllee dpnifayacd fspraieyvk
      121 qnplydterc kvfqcdltkd dlldhvppes vdvvmlifvl savhpdkmhl vlqniyktsw
      181 lsslwtqvmk kw
//
LOCUS       NP_001131077             331 aa            linear   PRI 21-NOV-2025
DEFINITION  gamma-parvin [Homo sapiens].
ACCESSION   NP_001131077
VERSION     NP_001131077.1
DBSOURCE    REFSEQ: accession NM_001137605.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 331)
  AUTHORS   Yoshimi,R., Yamaji,S., Suzuki,A., Mishima,W., Okamura,M., Obana,T.,
            Matsuda,C., Miwa,Y., Ohno,S. and Ishigatsubo,Y.
  TITLE     The gamma-parvin-integrin-linked kinase complex is critically
            involved in leukocyte-substrate interaction
  JOURNAL   J Immunol 176 (6), 3611-3624 (2006)
   PUBMED   16517730
  REMARK    GeneRIF: integrin-linked kinase-gamma-parvin complex is critically
            involved in the initial integrin signaling for leukocyte migration
REFERENCE   7  (residues 1 to 331)
  AUTHORS   Alonso,M.E., Bello,M.J., de Campos,J.M., Isla,A., Vaquero,J.,
            Gutierrez,M., Sarasa,J.L. and Rey,J.A.
  TITLE     No evidence of INI1hSNF5 (SMARCB1) and PARVG point mutations in
            oligodendroglial neoplasms
  JOURNAL   Cancer Genet Cytogenet 160 (2), 169-173 (2005)
   PUBMED   15993274
  REMARK    GeneRIF: INI1hSNF5 and PARVG do not seem to be the tumor suppressor
            genes involved in oligodendroglioma development and progression
REFERENCE   8  (residues 1 to 331)
  AUTHORS   Collins,J.E., Goward,M.E., Cole,C.G., Smink,L.J., Huckle,E.J.,
            Knowles,S., Bye,J.M., Beare,D.M. and Dunham,I.
  TITLE     Reevaluating human gene annotation: a second-generation analysis of
            chromosome 22
  JOURNAL   Genome Res 13 (1), 27-36 (2003)
   PUBMED   12529303
REFERENCE   9  (residues 1 to 331)
  AUTHORS   Korenbaum,E., Olski,T.M. and Noegel,A.A.
  TITLE     Genomic organization and expression profile of the parvin family of
            focal adhesion proteins in mice and humans
  JOURNAL   Gene 279 (1), 69-79 (2001)
   PUBMED   11722847
  REMARK    GeneRIF: Mammalian parvins are likely to have arisen late in
            evolution from gene duplication as they share a remarkably similar
            exon/intron organization.
REFERENCE   10 (residues 1 to 331)
  AUTHORS   Olski,T.M., Noegel,A.A. and Korenbaum,E.
  TITLE     Parvin, a 42 kDa focal adhesion protein, related to the
            alpha-actinin superfamily
  JOURNAL   J Cell Sci 114 (Pt 3), 525-538 (2001)
   PUBMED   11171322
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL031595.4, BP299653.1, AF237772.1 and AI075834.1.
            
            Summary: Members of the parvin family, including PARVG, are
            actin-binding proteins associated with focal contacts.[supplied by
            OMIM, Aug 2004].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein. This
            variant lacks full-length support and thus it has an inferred exon
            combination; the alternate 5' exon, which extends the gene range,
            is well-supported by partial transcript data.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: CR456480.2, SRR14038194.1828662.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2144333, SAMEA2149004 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.31"
     Protein         1..331
                     /product="gamma-parvin"
                     /calculated_mol_wt=37354
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q9HBI0.1)"
     Region          17..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBI0.1)"
     Region          45..150
                     /region_name="CH_PARVG_rpt1"
                     /note="first calponin homology (CH) domain found in
                     gamma-parvin; cd21305"
                     /db_xref="CDD:409154"
     Site            order(46,50,101,103..104,107..108,110,122..130,135,
                     137..138,140..141,144..145,148)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409154"
     Region          196..317
                     /region_name="CH_PARVG_rpt2"
                     /note="second calponin homology (CH) domain found in
                     gamma-parvin; cd21307"
                     /db_xref="CDD:409156"
     Site            order(212,216,270,272..273,276..277,279,288..296,301,
                     303..304,306..307,310..311,314)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409156"
     CDS             1..331
                     /gene="PARVG"
                     /coded_by="NM_001137605.3:430..1425"
                     /db_xref="GeneID:64098"
                     /db_xref="HGNC:HGNC:14654"
                     /db_xref="MIM:608122"
ORIGIN      
        1 mepeflydll qlpkgveppa eeelskggkk kylpptsrkd pkfeelqkvl mewinatllp
       61 ehivvrslee dmfdglilhh lfqrlaalkl eaedialtat sqkhkltvvl eavnrslqle
      121 ewqakwsves ifnkdllstl hllvalakrf qpdlslptnv qvevitiest ksglkseklv
      181 eqlteystdk deppkdvfde lfklapekvn avkeaivnfv nqkldrlgls vqnldtqfad
      241 gvilllligq legfflhlke fyltpnspae mlhnvtlale llkdegllsc pvspedivnk
      301 dakstlrvly glfckhtqka hrdrtphgap n
//
LOCUS       NP_001366236             276 aa            linear   PRI 21-NOV-2025
DEFINITION  complement factor H-related protein 1 isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_001366236
VERSION     NP_001366236.1
DBSOURCE    REFSEQ: accession NM_001379307.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Liu,Y., Shen,T., Liu,J., Yu,X., Li,Q., Chen,T. and Jiang,T.
  TITLE     CFHR1 involvement in bile duct carcinoma: Insights from a data
            mining study
  JOURNAL   Anal Biochem 688, 115474 (2024)
   PUBMED   38286352
  REMARK    GeneRIF: CFHR1 involvement in bile duct carcinoma: Insights from a
            data mining study.
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Hamza,A., El-Sissy,C., Yousfi,N., Martins,P.V., Rafat,C.,
            Masliah-Planchon,J., Fremeaux-Bacchi,V. and Mesnard,L.
  TITLE     The absence of CFHR3 and CFHR1 genes from the T2T-CHM13 assembly
            can limit the molecular diagnosis of complement-related diseases
  JOURNAL   Eur J Hum Genet 31 (7), 730-732 (2023)
   PUBMED   37032353
  REMARK    GeneRIF: The absence of CFHR3 and CFHR1 genes from the T2T-CHM13
            assembly can limit the molecular diagnosis of complement-related
            diseases.
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Sugawara,Y., Kato,H., Nagasaki,M., Yoshida,Y., Fujisawa,M.,
            Minegishi,N., Yamamoto,M. and Nangaku,M.
  TITLE     CFH-CFHR1 hybrid genes in two cases of atypical hemolytic uremic
            syndrome
  JOURNAL   J Hum Genet 68 (6), 427-430 (2023)
   PUBMED   36755127
  REMARK    GeneRIF: CFH-CFHR1 hybrid genes in two cases of atypical hemolytic
            uremic syndrome.
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Piras,R., Valoti,E., Alberti,M., Bresin,E., Mele,C., Breno,M.,
            Liguori,L., Donadelli,R., Rigoldi,M., Benigni,A., Remuzzi,G. and
            Noris,M.
  TITLE     CFH and CFHR structural variants in atypical Hemolytic Uremic
            Syndrome: Prevalence, genomic characterization and impact on
            outcome
  JOURNAL   Front Immunol 13, 1011580 (2023)
   PUBMED   36793547
  REMARK    GeneRIF: CFH and CFHR structural variants in atypical Hemolytic
            Uremic Syndrome: Prevalence, genomic characterization and impact on
            outcome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Zipfel,P.F. and Skerka,C.
  TITLE     Complement factor H and related proteins: an expanding family of
            complement-regulatory proteins?
  JOURNAL   Immunol Today 15 (3), 121-126 (1994)
   PUBMED   8172644
  REMARK    Review article
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Martin,B. and Smith,R.J.H.
  TITLE     C3 Glomerulopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301598
REFERENCE   7  (residues 1 to 276)
  AUTHORS   Noris,M., Bresin,E., Mele,C. and Remuzzi,G.
  TITLE     Genetic Atypical Hemolytic-Uremic Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301541
REFERENCE   8  (residues 1 to 276)
  AUTHORS   Skerka,C., Horstmann,R.D. and Zipfel,P.F.
  TITLE     Molecular cloning of a human serum protein structurally related to
            complement factor H
  JOURNAL   J Biol Chem 266 (18), 12015-12020 (1991)
   PUBMED   1711047
REFERENCE   9  (residues 1 to 276)
  AUTHORS   Estaller,C., Koistinen,V., Schwaeble,W., Dierich,M.P. and
            Weiss,E.H.
  TITLE     Cloning of the 1.4-kb mRNA species of human complement factor H
            reveals a novel member of the short consensus repeat family related
            to the carboxy terminal of the classical 150-kDa molecule
  JOURNAL   J Immunol 146 (9), 3190-3196 (1991)
   PUBMED   1826708
REFERENCE   10 (residues 1 to 276)
  AUTHORS   Timmann,C., Leippe,M. and Horstmann,R.D.
  TITLE     Two major serum components antigenically related to complement
            factor H are different glycosylation forms of a single protein with
            no factor H-like complement regulatory functions
  JOURNAL   J Immunol 146 (4), 1265-1270 (1991)
   PUBMED   1825108
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049741.8.
            
            Summary: This gene encodes a secreted protein belonging to the
            complement factor H protein family. It binds to Pseudomonas
            aeruginosa elongation factor Tuf together with plasminogen, which
            is proteolytically activated. It is proposed that Tuf acts as a
            virulence factor by acquiring host proteins to the pathogen
            surface, controlling complement, and facilitating tissue invasion.
            Mutations in this gene are associated with an increased risk of
            atypical hemolytic-uremic syndrome. [provided by RefSeq, Oct 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.141568.1,
                                           DRR138522.285408.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q31.3"
     Protein         1..276
                     /product="complement factor H-related protein 1 isoform 3
                     precursor"
                     /note="complement factor H-related 1 pseudogene; H factor
                     (complement)-like 1; H factor (complement)-like 2;
                     complement factor H-related protein 1; H-factor-like 1; h
                     factor-like protein 1"
                     /calculated_mol_wt=29370
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1930
     Region          53..275
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     CDS             1..276
                     /gene="CFHR1"
                     /gene_synonym="CFHL; CFHL1; CFHL1P; CFHR1P; FHL-1; FHR-1;
                     FHR1; H36; H36-1; H36-2; HFL1; HFL2"
                     /coded_by="NM_001379307.1:115..945"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS91131.1"
                     /db_xref="GeneID:3078"
                     /db_xref="HGNC:HGNC:4888"
                     /db_xref="MIM:134371"
ORIGIN      
        1 mwllvsvili srissvggee egwsptpkcl rlcffpfven ghsessgqth legdtvqiic
       61 ntgyrlqnne nniscvergw stppkcrstd tscvnpptvq nahilsrqms kypsgervry
      121 ecrspyemfg deevmclngn wteppqckds tgkcgppppi dngditsfpl svyapassve
      181 yqcqnlyqle gnkritcrng qwseppkclh pcvisreime nynialrwta kqklylrtge
      241 saefvckrgy rlssrshtlr ttcwdgkley ptcakr
//
LOCUS       NP_001129071             442 aa            linear   PRI 21-NOV-2025
DEFINITION  transforming growth factor beta-2 proprotein isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_001129071
VERSION     NP_001129071.1
DBSOURCE    REFSEQ: accession NM_001135599.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Wang,Z., Kometani,M., Zeitlin,L., Wilnai,Y., Kinoshita,A.,
            Yoshiura,K.I., Ninomiya,H., Imamura,T., Guo,L., Xue,J., Yan,L.,
            Ohashi,H., Pretemer,Y., Kawai,S., Shiina,M., Ogata,K., Cohn,D.H.,
            Matsumoto,N., Nishimura,G., Toguchida,J., Miyake,N. and Ikegawa,S.
  TITLE     Heterozygous mutations in the straitjacket region of the
            latency-associated peptide domain of TGFB2 cause Camurati-Engelmann
            disease type II
  JOURNAL   J Hum Genet 69 (11), 599-605 (2024)
   PUBMED   39014191
  REMARK    GeneRIF: Heterozygous mutations in the straitjacket region of the
            latency-associated peptide domain of TGFB2 cause Camurati-Engelmann
            disease type II.
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Usman,K., Fouadi,M., Nwozor,K.O., Aminazadeh,F., Nair,P., Luo,H.,
            Sin,D.D., Osei,E.T. and Hackett,T.L.
  TITLE     Interleukin-1alpha inhibits transforming growth factor-beta1 and
            beta2-induced extracellular matrix production, remodeling and
            signaling in human lung fibroblasts: Master regulator in lung
            mucosal repair
  JOURNAL   Matrix Biol 132, 47-58 (2024)
   PUBMED   39147560
  REMARK    GeneRIF: Interleukin-1alpha inhibits transforming growth
            factor-beta1 and beta2-induced extracellular matrix production,
            remodeling and signaling in human lung fibroblasts: Master
            regulator in lung mucosal repair.
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Jafarian,M., Hasannia,T., Badameh,P., Behmanesh,M. and Soltani,B.M.
  TITLE     Introduction of miR-3613-3p as a regulator of transforming growth
            factor-beta (TGF-beta) signaling pathway in colorectal cancer
  JOURNAL   Mol Biol Rep 51 (1), 728 (2024)
   PUBMED   38861185
  REMARK    GeneRIF: Introduction of miR-3613-3p as a regulator of transforming
            growth factor-beta (TGF-beta) signaling pathway in colorectal
            cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Hu,X., Li,D., Zhan,J., Yang,C., Wang,P., Meng,X., Xu,S., Che,X. and
            Xu,L.
  TITLE     microRNA-141-3p Suppressed the Progression of the Clear Cell Renal
            Cell Carcinoma by Targeting Transforming Growth Factor Beta 2 Gene
            Expression
  JOURNAL   DNA Cell Biol 43 (5), 245-257 (2024)
   PUBMED   38489601
  REMARK    GeneRIF: microRNA-141-3p Suppressed the Progression of the Clear
            Cell Renal Cell Carcinoma by Targeting Transforming Growth Factor
            Beta 2 Gene Expression.
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Loeys,B.L. and Dietz,H.C.
  TITLE     Loeys-Dietz Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301312
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Milewicz,D.M. and Cecchi,A.C.
  TITLE     Heritable Thoracic Aortic Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301299
REFERENCE   7  (residues 1 to 442)
  AUTHORS   Wrana,J.L., Attisano,L., Carcamo,J., Zentella,A., Doody,J.,
            Laiho,M., Wang,X.F. and Massague,J.
  TITLE     TGF beta signals through a heteromeric protein kinase receptor
            complex
  JOURNAL   Cell 71 (6), 1003-1014 (1992)
   PUBMED   1333888
REFERENCE   8  (residues 1 to 442)
  AUTHORS   Schlunegger,M.P. and Grutter,M.G.
  TITLE     An unusual feature revealed by the crystal structure at 2.2 A
            resolution of human transforming growth factor-beta 2
  JOURNAL   Nature 358 (6385), 430-434 (1992)
   PUBMED   1641027
REFERENCE   9  (residues 1 to 442)
  AUTHORS   Daopin,S., Piez,K.A., Ogawa,Y. and Davies,D.R.
  TITLE     Crystal structure of transforming growth factor-beta 2: an unusual
            fold for the superfamily
  JOURNAL   Science 257 (5068), 369-373 (1992)
   PUBMED   1631557
REFERENCE   10 (residues 1 to 442)
  AUTHORS   Noma,T., Glick,A.B., Geiser,A.G., O'Reilly,M.A., Miller,J.,
            Roberts,A.B. and Sporn,M.B.
  TITLE     Molecular cloning and structure of the human transforming growth
            factor-beta 2 gene promoter
  JOURNAL   Growth Factors 4 (4), 247-255 (1991)
   PUBMED   1764261
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC096638.2.
            
            Summary: This gene encodes a secreted ligand of the TGF-beta
            (transforming growth factor-beta) superfamily of proteins. Ligands
            of this family bind various TGF-beta receptors leading to
            recruitment and activation of SMAD family transcription factors
            that regulate gene expression. The encoded preproprotein is
            proteolytically processed to generate a latency-associated peptide
            (LAP) and a mature peptide, and is found in either a latent form
            composed of a mature peptide homodimer, a LAP homodimer, and a
            latent TGF-beta binding protein, or in an active form consisting
            solely of the mature peptide homodimer. The mature peptide may also
            form heterodimers with other TGF-beta family members. Disruption of
            the TGF-beta/SMAD pathway has been implicated in a variety of human
            cancers. A chromosomal translocation that includes this gene is
            associated with Peters' anomaly, a congenital defect of the
            anterior chamber of the eye. Mutations in this gene may be
            associated with Loeys-Dietz syndrome. This gene encodes multiple
            isoforms that may undergo similar proteolytic processing. [provided
            by RefSeq, Aug 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1). This isoform (1) may
            undergo proteolytic processing similar to isoform 2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.15473.1, M19154.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..442
                     /product="transforming growth factor beta-2 proprotein
                     isoform 1 precursor"
                     /note="cetermin; polyergin; BSC-1 cell growth inhibitor;
                     glioblastoma-derived T-cell suppressor factor;
                     prepro-transforming growth factor beta-2; transforming
                     growth factor beta-2 proprotein"
                     /calculated_mol_wt=48361
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2231
     Region          21..256
                     /region_name="TGFb_propeptide"
                     /note="TGF-beta propeptide; cl46657"
                     /db_xref="CDD:480997"
     Region          345..441
                     /region_name="TGF_beta_TGFB2"
                     /note="transforming growth factor beta (TGF-beta) like
                     domain found in transforming growth factor beta-2
                     (TGF-beta-2) and similar proteins; cd19385"
                     /db_xref="CDD:381655"
     Site            order(350..352,354,356..358,360,369,371..375,386..388,
                     390..392,394..395,398..399,403..405,407..410,413,431..436)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381655"
     Site            order(361..362,364,421..424)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:381655"
     CDS             1..442
                     /gene="TGFB2"
                     /gene_synonym="CAEND2; G-TSF; LDS4; TGF-beta2"
                     /coded_by="NM_001135599.4:1367..2695"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS44318.1"
                     /db_xref="GeneID:7042"
                     /db_xref="HGNC:HGNC:11768"
                     /db_xref="MIM:190220"
ORIGIN      
        1 mhycvlsafl ilhlvtvals lstcstldmd qfmrkrieai rgqilsklkl tsppedypep
       61 eevppevisi ynstrdllqe kasrraaace rersdeeyya kevykidmpp ffpsetvcpv
      121 vttpsgsvgs lcsrqsqvlc gyldaipptf yrpyfrivrf dvsameknas nlvkaefrvf
      181 rlqnpkarvp eqrielyqil kskdltsptq ryidskvvkt raegewlsfd vtdavhewlh
      241 hkdrnlgfki slhcpcctfv psnnyiipnk seelearfag idgtstytsg dqktikstrk
      301 knsgktphll lmllpsyrle sqqtnrrkkr aldaaycfrn vqdncclrpl yidfkrdlgw
      361 kwihepkgyn anfcagacpy lwssdtqhsr vlslyntinp easaspccvs qdlepltily
      421 yigktpkieq lsnmivksck cs
//
LOCUS       NP_001353335              96 aa            linear   PRI 21-NOV-2025
DEFINITION  protein S100-A2 isoform 2 [Homo sapiens].
ACCESSION   NP_001353335
VERSION     NP_001353335.1
DBSOURCE    REFSEQ: accession NM_001366406.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Zeng,T., Ren,W., Zeng,H., Wang,D., Wu,X. and Xu,G.
  TITLE     TFAP2A Activates S100A2 to Mediate Glutamine Metabolism and Promote
            Lung Adenocarcinoma Metastasis
  JOURNAL   Clin Respir J 18 (8), e13825 (2024)
   PUBMED   39187936
  REMARK    GeneRIF: TFAP2A Activates S100A2 to Mediate Glutamine Metabolism
            and Promote Lung Adenocarcinoma Metastasis.
REFERENCE   3  (residues 1 to 96)
  AUTHORS   Yang,J., Wan,S., Zhao,M., Cai,H., Gao,Y. and Wang,H.
  TITLE     Multi-omics Analysis Identifies Hypoxia Subtypes and S100A2 as an
            Immunosuppressive Factor in Cervical Cancer
  JOURNAL   Reprod Sci 31 (1), 107-121 (2024)
   PUBMED   37648942
  REMARK    GeneRIF: Multi-omics Analysis Identifies Hypoxia Subtypes and
            S100A2 as an Immunosuppressive Factor in Cervical Cancer.
REFERENCE   4  (residues 1 to 96)
  AUTHORS   Zhang,J., Wang,Z., Liang,Z., Jin,C., Shi,Y., Fan,M., Hu,X. and
            Wan,Y.
  TITLE     NFIC1 inhibits the migration and invasion of MDA-MB-231 cells
            through S100A2-mediated inactivation of MEK/ERK pathway
  JOURNAL   Arch Biochem Biophys 734, 109497 (2023)
   PUBMED   36574914
  REMARK    GeneRIF: NFIC1 inhibits the migration and invasion of MDA-MB-231
            cells through S100A2-mediated inactivation of MEK/ERK pathway.
REFERENCE   5  (residues 1 to 96)
  AUTHORS   Yan,J., Huang,Y.J., Huang,Q.Y., Liu,P.X. and Wang,C.S.
  TITLE     Transcriptional activation of S100A2 expression by HIF-1alpha via
            binding to the hypomethylated hypoxia response elements in HCC
            cells
  JOURNAL   Mol Carcinog 61 (5), 494-507 (2022)
   PUBMED   35107180
  REMARK    GeneRIF: Transcriptional activation of S100A2 expression by
            HIF-1alpha via binding to the hypomethylated hypoxia response
            elements in HCC cells.
REFERENCE   6  (residues 1 to 96)
  AUTHORS   Schafer,B.W. and Heizmann,C.W.
  TITLE     The S100 family of EF-hand calcium-binding proteins: functions and
            pathology
  JOURNAL   Trends Biochem Sci 21 (4), 134-140 (1996)
   PUBMED   8701470
  REMARK    Review article
REFERENCE   7  (residues 1 to 96)
  AUTHORS   Schafer,B.W., Wicki,R., Engelkamp,D., Mattei,M.G. and Heizmann,C.W.
  TITLE     Isolation of a YAC clone covering a cluster of nine S100 genes on
            human chromosome 1q21: rationale for a new nomenclature of the S100
            calcium-binding protein family
  JOURNAL   Genomics 25 (3), 638-643 (1995)
   PUBMED   7759097
REFERENCE   8  (residues 1 to 96)
  AUTHORS   Engelkamp,D., Schafer,B.W., Mattei,M.G., Erne,P. and Heizmann,C.W.
  TITLE     Six S100 genes are clustered on human chromosome 1q21:
            identification of two genes coding for the two previously
            unreported calcium-binding proteins S100D and S100E
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6547-6551 (1993)
   PUBMED   8341667
REFERENCE   9  (residues 1 to 96)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 96)
  AUTHORS   Lee,S.W., Tomasetto,C., Swisshelm,K., Keyomarsi,K. and Sager,R.
  TITLE     Down-regulation of a member of the S100 gene family in mammary
            carcinoma cells and reexpression by azadeoxycytidine treatment
  JOURNAL   Proc Natl Acad Sci U S A 89 (6), 2504-2508 (1992)
   PUBMED   1372446
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX470102.12.
            
            Summary: The protein encoded by this gene is a member of the S100
            family of proteins containing 2 EF-hand calcium-binding motifs.
            S100 proteins are localized in the cytoplasm and/or nucleus of a
            wide range of cells, and involved in the regulation of a number of
            cellular processes such as cell cycle progression and
            differentiation. S100 genes include at least 13 members which are
            located as a cluster on chromosome 1q21. This protein may have a
            tumor suppressor function. Chromosomal rearrangements and altered
            expression of this gene have been implicated in breast cancer.
            [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.229836.1,
                                           DRR138524.576228.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..96
                     /product="protein S100-A2 isoform 2"
                     /note="protein S100-A2"
                     /calculated_mol_wt=10970
     Region          4..>56
                     /region_name="S-100"
                     /note="S-100 domain, which represents the largest family
                     within the superfamily of proteins carrying the Ca-binding
                     EF-hand motif. Note that this S-100 hierarchy contains
                     only S-100 EF-hand domains, other EF-hands have been
                     modeled separately. S100 proteins are...; cd00213"
                     /db_xref="CDD:238131"
     CDS             1..96
                     /gene="S100A2"
                     /gene_synonym="CAN19; S100L"
                     /coded_by="NM_001366406.1:11..301"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS91059.1"
                     /db_xref="GeneID:6273"
                     /db_xref="HGNC:HGNC:10492"
                     /db_xref="MIM:176993"
ORIGIN      
        1 mmcssleqal avlvttfhky scqegdkfkl skgemkellh kelpsfvghs repcavrafr
       61 vhlfnpvigd lrnqspegks dcpkitqhwr kwmrrg
//
LOCUS       NP_003680                359 aa            linear   PRI 21-NOV-2025
DEFINITION  aflatoxin B1 aldehyde reductase member 2 isoform 1 [Homo sapiens].
ACCESSION   NP_003680
VERSION     NP_003680.2
DBSOURCE    REFSEQ: accession NM_003689.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 359)
  AUTHORS   Jordanova,A., Irobi,J., Thomas,F.P., Van Dijck,P., Meerschaert,K.,
            Dewil,M., Dierick,I., Jacobs,A., De Vriendt,E., Guergueltcheva,V.,
            Rao,C.V., Tournev,I., Gondim,F.A., D'Hooghe,M., Van Gerwen,V.,
            Callaerts,P., Van Den Bosch,L., Timmermans,J.P., Robberecht,W.,
            Gettemans,J., Thevelein,J.M., De Jonghe,P., Kremensky,I. and
            Timmerman,V.
  TITLE     Disrupted function and axonal distribution of mutant tyrosyl-tRNA
            synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy
  JOURNAL   Nat Genet 38 (2), 197-202 (2006)
   PUBMED   16429158
REFERENCE   7  (residues 1 to 359)
  AUTHORS   Praml,C., Savelyeva,L. and Schwab,M.
  TITLE     Aflatoxin B1 aldehyde reductase (AFAR) genes cluster at 1p35-1p36.1
            in a region frequently altered in human tumour cells
  JOURNAL   Oncogene 22 (30), 4765-4773 (2003)
   PUBMED   12879023
  REMARK    GeneRIF: structure and tissue-related expression of AFAR genes on
            chromosome 1
REFERENCE   8  (residues 1 to 359)
  AUTHORS   Kelly,V.P., Sherratt,P.J., Crouch,D.H. and Hayes,J.D.
  TITLE     Novel homodimeric and heterodimeric rat gamma-hydroxybutyrate
            synthases that associate with the Golgi apparatus define a distinct
            subclass of aldo-keto reductase 7 family proteins
  JOURNAL   Biochem J 366 (Pt 3), 847-861 (2002)
   PUBMED   12071861
REFERENCE   9  (residues 1 to 359)
  AUTHORS   Praml,C., Savelyeva,L., Perri,P. and Schwab,M.
  TITLE     Cloning of the human aflatoxin B1-aldehyde reductase gene at
            1p35-1p36.1 in a region frequently altered in human tumor cells
  JOURNAL   Cancer Res 58 (22), 5014-5018 (1998)
   PUBMED   9823300
  REMARK    Erratum:[Cancer Res 1999 Jun 15;59(12):3019]
REFERENCE   10 (residues 1 to 359)
  AUTHORS   Ireland,L.S., Harrison,D.J., Neal,G.E. and Hayes,J.D.
  TITLE     Molecular cloning, expression and catalytic activity of a human
            AKR7 member of the aldo-keto reductase superfamily: evidence that
            the major 2-carboxybenzaldehyde reductase from human liver is a
            homologue of rat aflatoxin B1-aldehyde reductase
  JOURNAL   Biochem J 332 (Pt 1) (Pt 1), 21-34 (1998)
   PUBMED   9576847
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL035413.19.
            
            On Jan 26, 2004 this sequence version replaced NP_003680.1.
            
            Summary: The protein encoded by this gene belongs to the aldo/keto
            reductase (AKR) superfamily and AKR7 family, which are involved in
            the detoxification of aldehydes and ketones. The AKR7 family
            consists of 3 genes that are present in a cluster on the p arm of
            chromosome 1. This protein, thought to be localized in the golgi,
            catalyzes the NADPH-dependent reduction of succinic semialdehyde to
            the endogenous neuromodulator, gamma-hydroxybutyrate. It may also
            function as a detoxication enzyme in the reduction of aflatoxin B1
            and 2-carboxybenzaldehyde. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Mar 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU794591.1, BK000395.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000235835.8/ ENSP00000235835.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.13"
     Protein         1..359
                     /product="aflatoxin B1 aldehyde reductase member 2 isoform
                     1"
                     /EC_number="1.1.1.n11"
                     /note="aflatoxin beta1 aldehyde reductase;
                     aldoketoreductase 7; aflatoxin B1 aldehyde reductase
                     member 2; AFB1-AR 1; SSA reductase; AFB1 aldehyde
                     reductase 1; succinic semialdehyde reductase; HEL-S-166mP;
                     epididymis secretory sperm binding protein Li 166mP;
                     aflatoxin aldehyde reductase"
                     /calculated_mol_wt=35600
     transit_peptide 1..38
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O43488.3)"
                     /calculated_mol_wt=4007
     Region          38..347
                     /region_name="AKR_AKR7A1-5"
                     /note="AKR7A family of aldo-keto reductase (AKR); cd19075"
                     /db_xref="CDD:381301"
     mat_peptide     39..359
                     /product="Aflatoxin B1 aldehyde reductase member 2.
                     /id=PRO_0000070375"
                     /note="propagated from UniProtKB/Swiss-Prot (O43488.3)"
                     /calculated_mol_wt=35600
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CG76; propagated from
                     UniProtKB/Swiss-Prot (O43488.3)"
     Site            order(43..45,50,72,77,105,109,141,171..172,197,225..231,
                     234,236..237,249..250,256,260,263,292,314..318,322,
                     325..326)
                     /site_type="active"
                     /db_xref="CDD:381301"
     Site            order(72,77,105,141)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381301"
     Site            105
                     /site_type="other"
                     /note="Lowers pKa of active site Tyr.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O43488.3)"
     Site            128
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8CG76; propagated from
                     UniProtKB/Swiss-Prot (O43488.3)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43488.3)"
     CDS             1..359
                     /gene="AKR7A2"
                     /gene_synonym="AFAR; AFAR1; AFB1-AR1; AKR7"
                     /coded_by="NM_003689.4:21..1100"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS194.1"
                     /db_xref="GeneID:8574"
                     /db_xref="HGNC:HGNC:389"
                     /db_xref="MIM:603418"
ORIGIN      
        1 mlsaasrvvs raavhcalrs pppearalam srpppprvas vlgtmemgrr mdapasaaav
       61 raflerghte ldtafmysdg qsetilgglg lglgggdcrv kiatkanpwd gkslkpdsvr
      121 sqletslkrl qcpqvdlfyl hapdhgtpve etlhacqrlh qegkfvelgl snyaswevae
      181 ictlcksngw ilptvyqgmy nattrqvete lfpclrhfgl rfyaynplag glltgkykye
      241 dkdgkqpvgr ffgnswaety rnrfwkehhf eaialvekal qaaygasaps vtsaalrwmy
      301 hhsqlqgahg davilgmssl eqleqnlaat eegplepavv dafnqawhlv ahecpnyfr
//
LOCUS       NP_001304746              85 aa            linear   PRI 21-NOV-2025
DEFINITION  sodium/bile acid cotransporter 7 isoform f [Homo sapiens].
ACCESSION   NP_001304746
VERSION     NP_001304746.1
DBSOURCE    REFSEQ: accession NM_001317817.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Zhang,W., Yao,Z., Guo,R., Cao,J., Li,W., Hao,C. and Zhang,X.
  TITLE     Identification of novel homozygous nonsense SLC10A7 variant causing
            short stature, amelogenesis imperfecta, and skeletal dysplasia with
            scoliosis and surgical management of spine
  JOURNAL   Orphanet J Rare Dis 18 (1), 371 (2023)
   PUBMED   38037133
  REMARK    GeneRIF: Identification of novel homozygous nonsense SLC10A7
            variant causing short stature, amelogenesis imperfecta, and
            skeletal dysplasia with scoliosis and surgical management of spine.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Durin,Z., Dubail,J., Layotte,A., Legrand,D., Cormier-Daire,V. and
            Foulquier,F.
  TITLE     SLC10A7, an orphan member of the SLC10 family involved in
            congenital disorders of glycosylation
  JOURNAL   Hum Genet 141 (7), 1287-1298 (2022)
   PUBMED   34999954
  REMARK    GeneRIF: SLC10A7, an orphan member of the SLC10 family involved in
            congenital disorders of glycosylation.
REFERENCE   4  (residues 1 to 85)
  AUTHORS   Li,C., Liu,Y., Lv,Z., Zheng,H., Li,Z., Zhang,J., Bao,H., Zhang,S.,
            Xiong,J., Jin,H., Yu,L., Ai,S., Wang,Y., Xiao,X., Su,T. and
            Liang,P.
  TITLE     Circular RNA circHECTD1 facilitates glioma progression by
            regulating the miR-296-3p/SLC10A7 axis
  JOURNAL   J Cell Physiol 236 (8), 5953-5965 (2021)
   PUBMED   33561315
  REMARK    GeneRIF: Circular RNA circHECTD1 facilitates glioma progression by
            regulating the miR-296-3p/SLC10A7 axis.
REFERENCE   5  (residues 1 to 85)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 85)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 85)
  AUTHORS   Godoy,J.R., Fernandes,C., Doring,B., Beuerlein,K., Petzinger,E. and
            Geyer,J.
  TITLE     Molecular and phylogenetic characterization of a novel putative
            membrane transporter (SLC10A7), conserved in vertebrates and
            bacteria
  JOURNAL   Eur J Cell Biol 86 (8), 445-460 (2007)
   PUBMED   17628207
  REMARK    GeneRIF: Molecular characterization and expression analysis of a
            novel member of the SLC10 family, SLC10A7, previously known as
            C4orf13, is reported
REFERENCE   8  (residues 1 to 85)
  AUTHORS   Zou,X., Wang,D., Qiu,G., Ji,C., Jin,F., Wu,M., Zheng,H., Li,X.,
            Sun,L., Wang,Y., Tang,R., Zhao,R.C. and Mao,Y.
  TITLE     Molecular cloning and characterization of a novel human C4orf13
            gene, tentatively a member of the sodium bile acid cotransporter
            family
  JOURNAL   Biochem Genet 43 (3-4), 165-173 (2005)
   PUBMED   15932064
  REMARK    GeneRIF: cloning and characterization; mapped to chromosome 4q31.2
            and contains 12 exons; widely expressed in human tissues
REFERENCE   9  (residues 1 to 85)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 85)
  AUTHORS   Teng,C.S.
  TITLE     Biological activity in the repopulating rat spermatocyte after the
            withdrawal of gossypol treatment. V. Inhibition and recovery of
            microtubular dynein
  JOURNAL   Contraception 51 (5), 313-318 (1995)
   PUBMED   7628207
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB205503.1, BC120971.1, AC106879.4 and AL136728.1.
            
            Transcript Variant: This variant (6) lacks many exons and its
            3'-terminal exon extends past a splice site that is used in variant
            2. The encoded isoform (f) has a significantly shorter and distinct
            C-terminus, compared to isoform b.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.3530363.1,
                                           SRR14038196.238724.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.22"
     Protein         1..85
                     /product="sodium/bile acid cotransporter 7 isoform f"
                     /note="sodium/bile acid cotransporter 7; SBF-domain
                     containing protein; Na(+)/bile acid cotransporter 7;
                     solute carrier family 10 (sodium/bile acid cotransporter
                     family), member 7"
                     /calculated_mol_wt=9265
     Region          10..>75
                     /region_name="SBF"
                     /note="Sodium Bile acid symporter family; cl19217"
                     /db_xref="CDD:450274"
     CDS             1..85
                     /gene="SLC10A7"
                     /gene_synonym="C4orf13; P7; SSASKS"
                     /coded_by="NM_001317817.2:224..481"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS82962.1"
                     /db_xref="GeneID:84068"
                     /db_xref="HGNC:HGNC:23088"
                     /db_xref="MIM:611459"
ORIGIN      
        1 mrllermrkd wfmvgivlai agaklepsig vnggplkpei tvsyiavati ffnsglslkt
       61 efadsrlhas acvfcsdfnq gswwk
//
LOCUS       NP_001362603             540 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform n [Homo sapiens].
ACCESSION   NP_001362603 XP_016858609
VERSION     NP_001362603.1
DBSOURCE    REFSEQ: accession NM_001375674.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 540)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 540)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 540)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 540)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 540)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 540)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 540)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            On Oct 31, 2019 this sequence version replaced XP_016858609.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..540
                     /product="abl interactor 2 isoform n"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=58394
     Region          93..156
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          <269..405
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          480..>514
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     CDS             1..540
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375674.1:122..1744"
                     /note="isoform n is encoded by transcript variant 19"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqs adkqraleet kayttqslas
       61 vaylintlan nvlqmldiqa sqlrrmessi nhisqtvdih kekvarreig ilttnkntsr
      121 thkiiapanl erpvryirkp idytilddig hgvkwllrfk vstqnmkmgg lprttpptqk
      181 ppsppmsgkg tlgrhspyrt lepvrppvvp ndyvpsptrn mapsqqspvr tasvnqrnrt
      241 yssgssggsh pssrsssren sgsgsvgvpi avptpsppsv fpapagsagt pplpatsasa
      301 paplvpatvp sstapdaaag gaqtladgft sptppvvsst pptghpvqfy smnrpasrht
      361 pptiggslpy rrppsitsqt slqnqmnggp fysqnpvsla ppppsilqvt pqlplmgfva
      421 rvqenisdtp pppppveepv fdespppppp pedyeeeeaa vveysdpyae edppwaprsy
      481 lekvvaiydy tkdkedelsf qegaiiyvik knddvlktkq aeseqmdlsa iictmlscld
//
LOCUS       NP_001362275             453 aa            linear   PRI 21-NOV-2025
DEFINITION  gamma-aminobutyric acid receptor subunit gamma-2 isoform 11
            precursor [Homo sapiens].
ACCESSION   NP_001362275
VERSION     NP_001362275.1
DBSOURCE    REFSEQ: accession NM_001375346.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Zhou,J., Noviello,C.M., Teng,J., Moore,H., Lega,B. and Hibbs,R.E.
  TITLE     Resolving native GABAA receptor structures from the human brain
  JOURNAL   Nature 638 (8050), 562-568 (2025)
   PUBMED   39843743
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Sui,J., Zhan,L., Ji,S., Wu,W., Chen,Y., Yun,F., Liang,W., Wang,J.,
            Cao,M., Shen,D. and Zhang,Q.
  TITLE     Differential inflammation responses determine the variable
            phenotypes of epilepsy induced by GABRG2 mutations
  JOURNAL   CNS Neurosci Ther 30 (2), e14583 (2024)
   PUBMED   38357846
  REMARK    GeneRIF: Differential inflammation responses determine the variable
            phenotypes of epilepsy induced by GABRG2 mutations.
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Zhang,Q., Forster-Gibson,C., Bercovici,E., Bernardo,A., Ding,F.,
            Shen,W., Langer,K., Rex,T. and Kang,J.Q.
  TITLE     Epilepsy plus blindness in microdeletion of GABRA1 and GABRG2 in
            mouse and human
  JOURNAL   Exp Neurol 369, 114537 (2023)
   PUBMED   37703949
  REMARK    GeneRIF: Epilepsy plus blindness in microdeletion of GABRA1 and
            GABRG2 in mouse and human.
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Ma,M., Zhao,J., Xie,D. and Chen,J.
  TITLE     Association between GABRG2 Gene Single Nucleotide Polymorphisms and
            Susceptibility to Ischemic Stroke in a Chinese Population
  JOURNAL   J Integr Neurosci 22 (6), 151 (2023)
   PUBMED   38176934
  REMARK    GeneRIF: Association between GABRG2 Gene Single Nucleotide
            Polymorphisms and Susceptibility to Ischemic Stroke in a Chinese
            Population.
REFERENCE   5  (residues 1 to 453)
  AUTHORS   Bengtsson,S.K.S., Sjostedt,J., Malinina,E., Das,R., Doverskog,M.,
            Johansson,M., Haage,D. and Backstrom,T.
  TITLE     Extra-Synaptic GABAA Receptor Potentiation and Neurosteroid-Induced
            Learning Deficits Are Inhibited by GR3027, a GABAA Modulating
            Steroid Antagonist
  JOURNAL   Biomolecules 13 (10), 1496 (2023)
   PUBMED   37892178
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 453)
  AUTHORS   Kostrzewa,M., Kohler,A., Eppelt,K., Hellam,L., Fairweather,N.D.,
            Levy,E.R., Monaco,A.P. and Muller,U.
  TITLE     Assignment of genes encoding GABAA receptor subunits alpha 1, alpha
            6, beta 2, and gamma 2 to a YAC contig of 5q33
  JOURNAL   Eur J Hum Genet 4 (4), 199-204 (1996)
   PUBMED   8875185
REFERENCE   7  (residues 1 to 453)
  AUTHORS   Russek,S.J. and Farb,D.H.
  TITLE     Mapping of the beta 2 subunit gene (GABRB2) to microdissected human
            chromosome 5q34-q35 defines a gene cluster for the most abundant
            GABAA receptor isoform
  JOURNAL   Genomics 23 (3), 528-533 (1994)
   PUBMED   7851879
REFERENCE   8  (residues 1 to 453)
  AUTHORS   Moss,S.J., Doherty,C.A. and Huganir,R.L.
  TITLE     Identification of the cAMP-dependent protein kinase and protein
            kinase C phosphorylation sites within the major intracellular
            domains of the beta 1, gamma 2S, and gamma 2L subunits of the
            gamma-aminobutyric acid type A receptor
  JOURNAL   J Biol Chem 267 (20), 14470-14476 (1992)
   PUBMED   1321150
REFERENCE   9  (residues 1 to 453)
  AUTHORS   Wilcox,A.S., Warrington,J.A., Gardiner,K., Berger,R., Whiting,P.,
            Altherr,M.R., Wasmuth,J.J., Patterson,D. and Sikela,J.M.
  TITLE     Human chromosomal localization of genes encoding the gamma 1 and
            gamma 2 subunits of the gamma-aminobutyric acid receptor indicates
            that members of this gene family are often clustered in the genome
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5857-5861 (1992)
   PUBMED   1321425
REFERENCE   10 (residues 1 to 453)
  AUTHORS   Pritchett,D.B., Sontheimer,H., Shivers,B.D., Ymer,S.,
            Kettenmann,H., Schofield,P.R. and Seeburg,P.H.
  TITLE     Importance of a novel GABAA receptor subunit for benzodiazepine
            pharmacology
  JOURNAL   Nature 338 (6216), 582-585 (1989)
   PUBMED   2538761
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008611.6, AC091926.4 and
            AC091984.3.
            
            Summary: This gene encodes a gamma-aminobutyric acid (GABA)
            receptor. GABA is the major inhibitory neurotransmitter in the
            mammlian brain, where it acts at GABA-A receptors, which are
            ligand-gated chloride channels. GABA-A receptors are pentameric,
            consisting of proteins from several subunit classes: alpha, beta,
            gamma, delta and rho. Mutations in this gene have been associated
            with epilepsy and febrile seizures. Multiple transcript variants
            encoding different isoforms have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.647.1,
                                           SRR1660803.120197.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..453
                     /product="gamma-aminobutyric acid receptor subunit gamma-2
                     isoform 11 precursor"
                     /note="gamma-aminobutyric acid receptor subunit gamma-2;
                     GABA(A) receptor subunit gamma-2; GABA(A) receptor, gamma
                     2; gamma-aminobutyric acid (GABA) A receptor, gamma 2;
                     gamma-aminobutyric acid type A receptor gamma2 subunit;
                     GABAAR subunit gamma-2"
                     /calculated_mol_wt=50749
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2083
     Region          47..450
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     Region          68..249
                     /region_name="LGIC_ECD_GABAAR_G"
                     /note="extracellular domain of gamma-aminobutyric acid
                     receptor subunit gamma; cd19000"
                     /db_xref="CDD:349801"
     Site            order(75,94)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:349801"
     Site            order(78,80..81,86..87,94,96..97,114,116..117,126..131,
                     134,136,138..139,145..147,149,159..161,189,249)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349801"
     Region          168..182
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349801"
     CDS             1..453
                     /gene="GABRG2"
                     /gene_synonym="CAE2; DEE74; ECA2; EIEE74; FEB8; GEFSP3"
                     /coded_by="NM_001375346.1:181..1542"
                     /note="isoform 11 precursor is encoded by transcript
                     variant 11"
                     /db_xref="CCDS:CCDS93814.1"
                     /db_xref="GeneID:2566"
                     /db_xref="HGNC:HGNC:4087"
                     /db_xref="MIM:137164"
ORIGIN      
        1 mtvwilllls lypgftsqks dddyedyasn ktwvltpkvp egdvtvilnn llegydnklr
       61 pdigvkptli htdmyvnsig pvnainmeyt idiffaqtwy drrlkfnsti kvlrlnsnmv
      121 gkiwipdtff rnskkadahw ittpnrmlri wndgrvlytl rltidaecql qlhnfpmdeh
      181 scplefssyg ypreeivyqw krssvevgdt rswrlyqfsf vglrnttevv kttsgdyvvm
      241 svyfdlsrrm gyftiqtyip ctlivvlswv sfwinkdavp artslgittv ltmttlstia
      301 rkslpkvsyv tamdlfvsvc fifvfsalve ygtlhyfvsn rkpskdkdkk kknpllrmfs
      361 fkaptidirp rsatiqmnna thlqerdeey gyecldgkdc asffccfedc rtgawrhgri
      421 hiriakmdsy ariffptafc lfnlvywvsy lyl
//
LOCUS       NP_612352                315 aa            linear   PRI 21-NOV-2025
DEFINITION  kinesin light chain 4 isoform c [Homo sapiens].
ACCESSION   NP_612352
VERSION     NP_612352.1
DBSOURCE    REFSEQ: accession NM_138343.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 315)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   7  (residues 1 to 315)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 315)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   9  (residues 1 to 315)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   10 (residues 1 to 315)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA782235.1 and BC012357.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR and the
            5' coding region and contains a 3' terminal exon that extends past
            a splice site, compared to variant 3. It encodes isoform c, which
            is shorter and has a distinct C-terminus, compared to isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012357.1, BQ943732.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..315
                     /product="kinesin light chain 4 isoform c"
                     /note="kinesin-like protein 8"
                     /calculated_mol_wt=34971
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Region          33..>148
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          55..88
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Region          134..>294
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          154..201
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBS5; propagated from
                     UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Region          210..285
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          211..244
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Region          212..239
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          252..282
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          253..286
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSK0.3)"
     CDS             1..315
                     /gene="KLC4"
                     /gene_synonym="bA387M24.3; CONDRHN; KNSL8"
                     /coded_by="NM_138343.4:81..1028"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS47429.1"
                     /db_xref="GeneID:89953"
                     /db_xref="HGNC:HGNC:21624"
                     /db_xref="MIM:620909"
ORIGIN      
        1 msglvlgqrd epaghrlsqe eilgstrlvs qglealrseh qavlqslsqt ieclqqgghe
       61 eglvhekarq lrrsmeniel glseaqvmla lashlstves ekqklraqvr rlcqenqwlr
      121 delagtqqrl qrseqavaql eeekkhlefl gqlrqydedg htseekegda tkdslddlfp
      181 neeeedpsng lsrgqgataa qqggyeipar lrtlhnlviq yaaqgryeva vplckqaled
      241 lertsgrghp dvatmlnila lvyrdqnkyk eaahllndal sirestlgpd hpavsipcpp
      301 hptprtphhc cfgls
//
LOCUS       NP_001269091             301 aa            linear   PRI 21-NOV-2025
DEFINITION  F-actin-capping protein subunit beta isoform 4 [Homo sapiens].
ACCESSION   NP_001269091
VERSION     NP_001269091.1
DBSOURCE    REFSEQ: accession NM_001282162.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Carman,P.J., Barrie,K.R., Rebowski,G. and Dominguez,R.
  TITLE     Structures of the free and capped ends of the actin filament
  JOURNAL   Science 380 (6651), 1287-1292 (2023)
   PUBMED   37228182
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Wells,C.D., Fawcett,J.P., Traweger,A., Yamanaka,Y., Goudreault,M.,
            Elder,K., Kulkarni,S., Gish,G., Virag,C., Lim,C., Colwill,K.,
            Starostine,A., Metalnikov,P. and Pawson,T.
  TITLE     A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
            proteins in epithelial cells
  JOURNAL   Cell 125 (3), 535-548 (2006)
   PUBMED   16678097
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Yang,C., Pring,M., Wear,M.A., Huang,M., Cooper,J.A., Svitkina,T.M.
            and Zigmond,S.H.
  TITLE     Mammalian CARMIL inhibits actin filament capping by capping protein
  JOURNAL   Dev Cell 9 (2), 209-221 (2005)
   PUBMED   16054028
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Olavesen,M.G., Bentley,E., Mason,R.V., Stephens,R.J. and
            Ragoussis,J.
  TITLE     Fine mapping of 39 ESTs on human chromosome 6p23-p25
  JOURNAL   Genomics 46 (2), 303-306 (1997)
   PUBMED   9417921
REFERENCE   8  (residues 1 to 301)
  AUTHORS   Kuhlman,P.A. and Fowler,V.M.
  TITLE     Purification and characterization of an alpha 1 beta 2 isoform of
            CapZ from human erythrocytes: cytosolic location and inability to
            bind to Mg2+ ghosts suggest that erythrocyte actin filaments are
            capped by adducin
  JOURNAL   Biochemistry 36 (44), 13461-13472 (1997)
   PUBMED   9354614
REFERENCE   9  (residues 1 to 301)
  AUTHORS   Hart,M.C., Korshunova,Y.O. and Cooper,J.A.
  TITLE     Vertebrates have conserved capping protein alpha isoforms with
            specific expression patterns
  JOURNAL   Cell Motil Cytoskeleton 38 (2), 120-132 (1997)
   PUBMED   9331217
REFERENCE   10 (residues 1 to 301)
  AUTHORS   Barron-Casella,E.A., Torres,M.A., Scherer,S.W., Heng,H.H.,
            Tsui,L.C. and Casella,J.F.
  TITLE     Sequence analysis and chromosomal localization of human Cap Z.
            Conserved residues within the actin-binding domain may link Cap Z
            to gelsolin/severin and profilin protein families
  JOURNAL   J Biol Chem 270 (37), 21472-21479 (1995)
   PUBMED   7665558
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK301442.1, BC107752.1,
            BC008095.1 and BQ773230.1.
            
            Summary: This gene encodes the beta subunit of the barbed-end actin
            binding protein, which belongs to the F-actin capping protein
            family. The capping protein is a heterodimeric actin capping
            protein that blocks actin filament assembly and disassembly at the
            fast growing (barbed) filament ends and functions in regulating
            actin filament dynamics as well as in stabilizing actin filament
            lengths in muscle and nonmuscle cells. A pseudogene of this gene is
            located on the long arm of chromosome 2. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found.[provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (4) uses an alternate 5' terminal
            exon, and thus differs in the 5' UTR and 5' coding region, compared
            to variant 1. These differences cause translation initiation at an
            alternate AUG and result in an isoform (4) with a longer and
            distinct N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.7734.1,
                                           SRR5189667.363974.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.13"
     Protein         1..301
                     /product="F-actin-capping protein subunit beta isoform 4"
                     /note="F-actin-capping protein subunit beta; capZ beta;
                     epididymis secretory sperm binding protein; capping
                     protein (actin filament) muscle Z-line, beta; capping
                     actin protein of muscle Z-line beta subunit"
                     /calculated_mol_wt=33650
     Region          40..268
                     /region_name="F_actin_cap_B"
                     /note="F-actin capping protein, beta subunit; pfam01115"
                     /db_xref="CDD:460070"
     CDS             1..301
                     /gene="CAPZB"
                     /gene_synonym="CAPB; CAPPB; CAPZ"
                     /coded_by="NM_001282162.2:17..922"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS72718.1"
                     /db_xref="GeneID:832"
                     /db_xref="HGNC:HGNC:1491"
                     /db_xref="MIM:601572"
ORIGIN      
        1 mhpsrrslpf plncqlarvg tadygspsdq sdqqldcald lmrrlppqqi eknlsdlidl
       61 vpslcedlls svdqplkiar dkvvgkdyll cdynrdgdsy rspwsnkydp pledgampsa
      121 rlrklevean nafdqyrdly feggvssvyl wdldhgfagv ilikkagdgs kkikgcwdsi
      181 hvvevqekss grtahyklts tvmlwlqtnk sgsgtmnlgg sltrqmekde tvsdcsphia
      241 nigrlvedme nkirstlnei yfgktkdivn glrsvqtfad kskqealknd lvealkrkqq
      301 c
//
LOCUS       NP_001276897             514 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2B catalytic subunit beta
            isoform isoform d [Homo sapiens].
ACCESSION   NP_001276897
VERSION     NP_001276897.1
DBSOURCE    REFSEQ: accession NM_001289968.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Gazzeri,S., Zubchuk,N., Montaudon,E., Nemati,F., Huot-Marchand,S.,
            Berardi,G., Pucciarelli,A., Dib,Y., Nerini,D., Oddou,C., Pezet,M.,
            David-Boudet,L., Ardin,C., de Fraipont,F., Maraver,A., Girard,N.,
            Decaudin,D., Toffart,A.C. and Eymin,B.
  TITLE     PPP3CB overexpression mediates EGFR TKI resistance in lung tumors
            via calcineurin/MEK/ERK signaling
  JOURNAL   Life Sci Alliance 7 (12), e202402873 (2024)
   PUBMED   39353739
  REMARK    GeneRIF: PPP3CB overexpression mediates EGFR TKI resistance in lung
            tumors via calcineurin/MEK/ERK signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Zhang,Z., Chen,C., Yang,F., Zeng,Y.X., Sun,P., Liu,P. and Li,X.
  TITLE     Itaconate is a lysosomal inducer that promotes antibacterial innate
            immunity
  JOURNAL   Mol Cell 82 (15), 2844-2857 (2022)
   PUBMED   35662396
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Miyata,H., Oura,S., Morohoshi,A., Shimada,K., Mashiko,D., Oyama,Y.,
            Kaneda,Y., Matsumura,T., Abbasi,F. and Ikawa,M.
  TITLE     SPATA33 localizes calcineurin to the mitochondria and regulates
            sperm motility in mice
  JOURNAL   Proc Natl Acad Sci U S A 118 (35) (2021)
   PUBMED   34446558
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Chen,M.X., Chen,Y.H. and Cohen,P.T.
  TITLE     Polymerase chain reactions using Saccharomyces, Drosophila and
            human DNA predict a large family of protein serine/threonine
            phosphatases
  JOURNAL   FEBS Lett 306 (1), 54-58 (1992)
   PUBMED   1321058
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Giri,P.R., Higuchi,S. and Kincaid,R.L.
  TITLE     Chromosomal mapping of the human genes for the calmodulin-dependent
            protein phosphatase (calcineurin) catalytic subunit
  JOURNAL   Biochem Biophys Res Commun 181 (1), 252-258 (1991)
   PUBMED   1659808
REFERENCE   8  (residues 1 to 514)
  AUTHORS   McPartlin,A.E., Barker,H.M. and Cohen,P.T.
  TITLE     Identification of a third alternatively spliced cDNA encoding the
            catalytic subunit of protein phosphatase 2B beta
  JOURNAL   Biochim Biophys Acta 1088 (2), 308-310 (1991)
   PUBMED   1848109
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Guerini,D. and Klee,C.B.
  TITLE     Cloning of human calcineurin A: evidence for two isozymes and
            identification of a polyproline structural domain
  JOURNAL   Proc Natl Acad Sci U S A 86 (23), 9183-9187 (1989)
   PUBMED   2556704
REFERENCE   10 (residues 1 to 514)
  AUTHORS   Guerini,D., Krinks,M.H., Sikela,J.M., Hahn,W.E. and Klee,C.B.
  TITLE     Isolation and sequence of a cDNA clone for human calcineurin B, the
            Ca2+-binding subunit of the Ca2+/calmodulin-stimulated protein
            phosphatase
  JOURNAL   DNA 8 (9), 675-682 (1989)
   PUBMED   2558868
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA128707.1, M29550.1, AK301582.1 and CA429703.1.
            
            Transcript Variant: This variant (4) has multiple differences in
            the coding region, one of which results in a frameshift and early
            stop codon, compared to variant 1. The resulting protein (isoform
            d) has a distinct C-terminus and is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M29550.1, SRR14038191.219638.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..514
                     /product="serine/threonine-protein phosphatase 2B
                     catalytic subunit beta isoform isoform d"
                     /EC_number="3.1.3.16"
                     /note="calcineurin A beta; CAM-PRP catalytic subunit;
                     calcineurin A2; protein phosphatase 3, catalytic subunit,
                     beta isozyme; protein phosphatase from PCR fragment H32;
                     CNA beta"
                     /calculated_mol_wt=57882
     Region          50..372
                     /region_name="MPP_PP2B"
                     /note="PP2B, metallophosphatase domain; cd07416"
                     /db_xref="CDD:277361"
     Site            order(62,64,99,101,127,177,186,226,308,341,368)
                     /site_type="other"
                     /note="CN-CyPA-CsA complex [polypeptide binding]"
                     /db_xref="CDD:277361"
     Site            order(99,101,127,131,177..178,226,259,281,308,310)
                     /site_type="active"
                     /db_xref="CDD:277361"
     Site            order(99,101,127,177,226,308)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277361"
     CDS             1..514
                     /gene="PPP3CB"
                     /gene_synonym="CALNA2; CALNB; CNA2; PP2Bbeta"
                     /coded_by="NM_001289968.2:136..1680"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:5532"
                     /db_xref="HGNC:HGNC:9315"
                     /db_xref="MIM:114106"
ORIGIN      
        1 maapeparaa pppppppppp pgadrvvkav pfppthrlts eevfdldgip rvdvlknhlv
       61 kegrvdeeia lriinegaai lrrektmiev eapitvcgdi hgqffdlmkl fevggspant
      121 rylflgdyvd rgyfsiehvl gtedisinph nninecvlyl wvlkilypst lfllrgnhec
      181 rhlteyftfk qeckikyser vyeacmeafd slplaallnq qflcvhggls peihtlddir
      241 rldrfkeppa fgpmcdllws dpsedfgnek sqehfshntv rgcsyfynyp avceflqnnn
      301 llsiirahea qdagyrmyrk sqttgfpsli tifsapnyld vynnkaavlk yennvmnirq
      361 fncsphpywl pnfmdvftws lpfvgekvte mlvnvlsics ddelmteged qfdgsaaark
      421 eiirnkirai gkmarvfsvl reesesvltl kgltptgmlp sgvlaggrqt lqsgndvmql
      481 avpqmdwgtp hsfannshna crefllffss clss
//
LOCUS       NP_001335430            1275 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 2 isoform v [Homo
            sapiens].
ACCESSION   NP_001335430 XP_016869530
VERSION     NP_001335430.1
DBSOURCE    REFSEQ: accession NM_001348501.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1275)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1275)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   3  (residues 1 to 1275)
  AUTHORS   Mechaussier,S., Almoallem,B., Zeitz,C., Van Schil,K., Jeddawi,L.,
            Van Dorpe,J., Duenas Rey,A., Condroyer,C., Pelle,O., Polak,M.,
            Boddaert,N., Bahi-Buisson,N., Cavallin,M., Bacquet,J.L.,
            Mouallem-Beziere,A., Zambrowski,O., Sahel,J.A., Audo,I., Kaplan,J.,
            Rozet,J.M., De Baere,E. and Perrault,I.
  TITLE     Loss of Function of RIMS2 Causes a Syndromic Congenital Cone-Rod
            Synaptic Disease with Neurodevelopmental and Pancreatic Involvement
  JOURNAL   Am J Hum Genet 106 (6), 859-871 (2020)
   PUBMED   32470375
  REMARK    GeneRIF: Loss of Function of RIMS2 Causes a Syndromic Congenital
            Cone-Rod Synaptic Disease with Neurodevelopmental and Pancreatic
            Involvement.
            Erratum:[Am J Hum Genet. 2020 Sep 3;107(3):580. doi:
            10.1016/j.ajhg.2020.08.004. PMID: 32888510]
REFERENCE   4  (residues 1 to 1275)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 1275)
  AUTHORS   Kim,K.T., Lee,J.S., Lee,B.W., Seok,H., Jeon,H.S., Kim,J.H. and
            Chung,J.H.
  TITLE     Association between regulating synaptic membrane exocytosis 2 gene
            polymorphisms and degenerative lumbar scoliosis
  JOURNAL   Biomed Rep 1 (4), 619-623 (2013)
   PUBMED   24648997
REFERENCE   6  (residues 1 to 1275)
  AUTHORS   Sun,L., Bittner,M.A. and Holz,R.W.
  TITLE     Rim, a component of the presynaptic active zone and modulator of
            exocytosis, binds 14-3-3 through its N terminus
  JOURNAL   J Biol Chem 278 (40), 38301-38309 (2003)
   PUBMED   12871946
REFERENCE   7  (residues 1 to 1275)
  AUTHORS   Fukuda,M.
  TITLE     Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and
            Noc2. Identification of a critical determinant of Rab3A/Rab27A
            recognition by Rim2
  JOURNAL   J Biol Chem 278 (17), 15373-15380 (2003)
   PUBMED   12578829
REFERENCE   8  (residues 1 to 1275)
  AUTHORS   Wang,Y. and Sudhof,T.C.
  TITLE     Genomic definition of RIM proteins: evolutionary amplification of a
            family of synaptic regulatory proteins
  JOURNAL   Genomics 81 (2), 126-137 (2003)
   PUBMED   12620390
REFERENCE   9  (residues 1 to 1275)
  AUTHORS   Kashima,Y., Miki,T., Shibasaki,T., Ozaki,N., Miyazaki,M., Yano,H.
            and Seino,S.
  TITLE     Critical role of cAMP-GEFII--Rim2 complex in incretin-potentiated
            insulin secretion
  JOURNAL   J Biol Chem 276 (49), 46046-46053 (2001)
   PUBMED   11598134
REFERENCE   10 (residues 1 to 1275)
  AUTHORS   Fenster,S.D., Chung,W.J., Zhai,R., Cases-Langhoff,C., Voss,B.,
            Garner,A.M., Kaempf,U., Kindler,S., Gundelfinger,E.D. and
            Garner,C.C.
  TITLE     Piccolo, a presynaptic zinc finger protein structurally related to
            bassoon
  JOURNAL   Neuron 25 (1), 203-214 (2000)
   PUBMED   10707984
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC090686.4, AP001572.3,
            AC107933.6 and AP002849.2.
            
            On Feb 4, 2017 this sequence version replaced XP_016869530.1.
            
            Summary: The protein encoded by this gene is a presynaptic protein
            that interacts with RAB3, a protein important for normal
            neurotransmitter release. The encoded protein can also bind several
            other synaptic proteins, including UNC-13 homolog B,
            ELKS/Rab6-interacting/CAST family member 1, and synaptotagmin 1.
            This protein is involved in synaptic membrane exocytosis.
            Polymorphisms in this gene have been associated with degenerative
            lumbar scoliosis. [provided by RefSeq, Feb 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.194561.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..1275
                     /product="regulating synaptic membrane exocytosis protein
                     2 isoform v"
                     /note="RAB3 interacting protein 3; regulating synaptic
                     membrane exocytosis protein 2; nuclear protein; non-small
                     cell lung cancer RimL3a protein; non-small cell lung
                     cancer RimL3c protein; rab3-interacting molecule 2;
                     rab-3-interacting protein 3; rab-3-interacting molecule 2;
                     Rab3-interacting protein"
                     /calculated_mol_wt=144311
     Region          384..483
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(408..414,429,432,462,466,469..470)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          535..661
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(566,572,627,629,637)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          1106..1251
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(1163,1167..1168,1170,1173,1201,1203,1205,1249..1250)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..1275
                     /gene="RIMS2"
                     /gene_synonym="CRSDS; OBOE; RAB3IP3; RIM2"
                     /coded_by="NM_001348501.2:289..4116"
                     /note="isoform v is encoded by transcript variant 22"
                     /db_xref="GeneID:9699"
                     /db_xref="HGNC:HGNC:17283"
                     /db_xref="MIM:606630"
ORIGIN      
        1 mqfetlrqvc nsvlshfhgv fssppnilqn elfgqtlnna rkrspsvsrd qnrrydqree
       61 reeysqyats dtamprspsd yadrrsqhep qfyedsdhls yrdsnrrshr hskeyivdde
      121 dvesrdeyer qrreeeyqsr yrsdpnlary pvkpqpyeeq mrihaevsra rherrhsdvs
      181 lanadledsr ismlrmdrps rqrsiserra amenqrsysm ertreaqgps syaqrttnhs
      241 pptprrsplp idrpdlrrtd slrkqhhldp ssavrktkre kmetmlrnds lssdqsesvr
      301 ppppkphksk kggkmrqisl ssseeelast peytscddve iesesvsekg dmdynwldht
      361 swhsseaspm slhpvtwqps kdgdrligri llnkrlkdgs vprdsgamlg lkvvggkmte
      421 sgrlcafitk vkkgsladtv ghlrpgdevl ewngrllqga tfeevyniil eskpepqvel
      481 vvsrpigdip ripdsthaql esssssfesq kmdrpsisvt spmspgmlrd vpqflsgqls
      541 iklwfdkvgh qlivtilgak dlpsredgrp rnpyvkiyfl pdrsdknkrr tktvkktlep
      601 kwnqtfiysp vhrrefrerm leitlwdqar vreeeseflg eilieletal lddephwykl
      661 qthdvsslpl phpspymprr qlhgesptrr lqrskrisds evsdydcddg igvvsdyrhd
      721 grdlqsstls vpeqvmssnh cspsgsphrv dvigrtrsws psvpppqsrn veqglrgtrt
      781 mtghyntisr mdrhrvmddh yspdrdrshp rtgsvqtsps stpvagrrgr qlpqlppkgt
      841 ldrnngvkei epyeeeldst rrryagtmdi eernrqmkin kykqvagsdp rleqdyhsky
      901 rsgwdphrga dnvstkssds dvsdisavsr tssasrfsst symsvqserp ggnkkisvft
      961 skmqsrqmgi sgknmtksts isgdmcslek ndgsqsdtav gtlgtsgkkr rsslgakmva
     1021 ivglsrksrs asqlsqteag gkklrstvqr stetglavem rnwmtrqasr estdgsmnsy
     1081 ssegnlifpg vrlasdsqfs dfldglgpaq lvgrqtlatp amgdiqvgmm dkkgqlevei
     1141 irarglvvkp gsktlpapyv kvylldngvc iakkktkvar ktleplyqql lsfeespqgk
     1201 vlqiivwgdy grmdhksfmg vaqilldele lsnmvigwfk lfppsslvdp tlapltrras
     1261 qsslesstgp sysrs
//
LOCUS       NP_612211                204 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase III subunit RPC8 isoform a [Homo
            sapiens].
ACCESSION   NP_612211
VERSION     NP_612211.1
DBSOURCE    REFSEQ: accession NM_138338.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Ramsay,E.P., Abascal-Palacios,G., Daiss,J.L., King,H., Gouge,J.,
            Pilsl,M., Beuron,F., Morris,E., Gunkel,P., Engel,C. and Vannini,A.
  TITLE     Structure of human RNA polymerase III
  JOURNAL   Nat Commun 11 (1), 6409 (2020)
   PUBMED   33335104
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Franca,M.M., Han,X., Funari,M.F.A., Lerario,A.M., Nishi,M.Y.,
            Fontenele,E.G.P., Domenice,S., Jorge,A.A.L., Garcia-Galiano,D.,
            Elias,C.F. and Mendonca,B.B.
  TITLE     Exome Sequencing Reveals the POLR3H Gene as a Novel Cause of
            Primary Ovarian Insufficiency
  JOURNAL   J Clin Endocrinol Metab 104 (7), 2827-2841 (2019)
   PUBMED   30830215
  REMARK    GeneRIF: A pathogenic homozygous missense mutation (c.149A>G;
            p.Asp50Gly) in the POLR3H gene in two unrelated families with
            primary ovarian insufficiency was identified.
REFERENCE   6  (residues 1 to 204)
  AUTHORS   Owen,T.J., O'Neil,J.D., Dawson,C.W., Hu,C., Chen,X., Yao,Y.,
            Wood,V.H., Mitchell,L.E., White,R.J., Young,L.S. and Arrand,J.R.
  TITLE     Epstein-Barr virus-encoded EBNA1 enhances RNA polymerase
            III-dependent EBER expression through induction of EBER-associated
            cellular transcription factors
  JOURNAL   Mol Cancer 9, 241 (2010)
   PUBMED   20843307
  REMARK    GeneRIF: Findings reveal that RNA polymerase III-dependent EBER
            expression through induction of cellular transcription factors and
            add to the repertoire of EBNA1's transcription-regulatory
            properties.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 204)
  AUTHORS   Greco-Stewart,V.S., Schissel,E. and Pelchat,M.
  TITLE     The hepatitis delta virus RNA genome interacts with the human RNA
            polymerases I and III
  JOURNAL   Virology 386 (1), 12-15 (2009)
   PUBMED   19246067
  REMARK    GeneRIF: The authors demonstrate the interaction of both RNA
            polymerase I and III with hepatitis delta virus RNA, both in vitro
            and in human cells.
REFERENCE   8  (residues 1 to 204)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   9  (residues 1 to 204)
  AUTHORS   Hu,P., Wu,S., Sun,Y., Yuan,C.C., Kobayashi,R., Myers,M.P. and
            Hernandez,N.
  TITLE     Characterization of human RNA polymerase III identifies orthologues
            for Saccharomyces cerevisiae RNA polymerase III subunits
  JOURNAL   Mol Cell Biol 22 (22), 8044-8055 (2002)
   PUBMED   12391170
REFERENCE   10 (residues 1 to 204)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA504810.1, AB051452.1, AK000365.1, AL023553.5 and BM701572.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a). Variants 1, 3, 5, and 6 encode the same isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2734671.1,
                                           SRR14038195.1086791.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..204
                     /product="DNA-directed RNA polymerase III subunit RPC8
                     isoform a"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerase III subunit RPC8;
                     polymerase (RNA) III subunit H; RNA nucleotidyltransferase
                     (DNA-directed); RNA polymerase III subunit C8;
                     DNA-directed RNA polymerase III subunit H; DNA-directed
                     RNA polymerase III subunit 22.9 kDa polypeptide;
                     polymerase (RNA) III (DNA directed) polypeptide H
                     (22.9kD)"
                     /calculated_mol_wt=22787
     Region          2..81
                     /region_name="RNAP_III_Rpc25_N"
                     /note="Rpc25, N-terminal ribonucleoprotein (RNP) domain.
                     Rpc25 is a subunit of eukaryotic RNA polymerase (RNAP) III
                     and is homologous to Rpa43 of eukaryotic RNAP I, Rpb7 of
                     eukaryotic RNAP II, and RpoE of archaeal RNAP. Rpc25 has
                     two domains, an N-terminal RNP...; cd04330"
                     /db_xref="CDD:239822"
     Site            order(2..6,8,28,31..32,46..49,73,78,80)
                     /site_type="other"
                     /note="Rpc17 interaction site [polypeptide binding]"
                     /db_xref="CDD:239822"
     Region          83..201
                     /region_name="RNA_pol_Rbc25"
                     /note="RNA polymerase III subunit Rpc25; pfam08292"
                     /db_xref="CDD:400543"
     Region          158..179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y535.1)"
     CDS             1..204
                     /gene="POLR3H"
                     /gene_synonym="C25; RPC22.9; RPC8"
                     /coded_by="NM_138338.5:64..678"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14018.1"
                     /db_xref="GeneID:171568"
                     /db_xref="HGNC:HGNC:30349"
                     /db_xref="MIM:619801"
ORIGIN      
        1 mfvlvemvdt vrippwqfer klndsiaeel nkklankvvy nvglciclfd itkledayvf
       61 pgdgashtkv hfrcvvfhpf ldeiligkik gcspegvhvs lgffddilip peslqqpakf
      121 deaeqvwvwe yeteegahdl ymdtgeeirf rvvdesfvdt sptgpssada ttsseelpkk
      181 eapytlvgsi sepglgllsw wtsn
//
LOCUS       NP_001385214             200 aa            linear   PRI 21-NOV-2025
DEFINITION  TIMELESS-interacting protein isoform 2 [Homo sapiens].
ACCESSION   NP_001385214 XP_016877880
VERSION     NP_001385214.1
DBSOURCE    REFSEQ: accession NM_001398285.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Arai,H., Xiao,Y., Millstein,J., Wang,J., Battaglin,F.,
            Kawanishi,N., Jayachandran,P., Soni,S., Zhang,W., Mancao,C.,
            Salhia,B., Mumenthaler,S.M., Parikh,A.R. and Lenz,H.J.
  TITLE     Germline polymorphisms in genes maintaining the replication fork
            predict the efficacy of oxaliplatin and irinotecan in patients with
            metastatic colorectal cancer
  JOURNAL   Br J Cancer 126 (1), 72-78 (2022)
   PUBMED   34689170
  REMARK    GeneRIF: Germline polymorphisms in genes maintaining the
            replication fork predict the efficacy of oxaliplatin and irinotecan
            in patients with metastatic colorectal cancer.
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Grabarczyk,D.B.
  TITLE     The Fork Protection Complex: A Regulatory Hub at the Head of the
            Replisome
  JOURNAL   Subcell Biochem 99, 83-107 (2022)
   PUBMED   36151374
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Lerner,L.K., Holzer,S., Kilkenny,M.L., Svikovic,S., Murat,P.,
            Schiavone,D., Eldridge,C.B., Bittleston,A., Maman,J.D., Branzei,D.,
            Stott,K., Pellegrini,L. and Sale,J.E.
  TITLE     Timeless couples G-quadruplex detection with processing by DDX11
            helicase during DNA replication
  JOURNAL   EMBO J 39 (18), e104185 (2020)
   PUBMED   32705708
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 200)
  AUTHORS   Gotter,A.L., Suppa,C. and Emanuel,B.S.
  TITLE     Mammalian TIMELESS and Tipin are evolutionarily conserved
            replication fork-associated factors
  JOURNAL   J Mol Biol 366 (1), 36-52 (2007)
   PUBMED   17141802
  REMARK    GeneRIF: TIM and Tipin are functional orthologs of their
            replisome-associated yeast counterparts capable of coordinating
            replication with genotoxic stress responses, and distinguishes
            mammalian TIM from the circadian-specific paralogs.
REFERENCE   7  (residues 1 to 200)
  AUTHORS   Yoshizawa-Sugata,N. and Masai,H.
  TITLE     Human Tim/Timeless-interacting protein, Tipin, is required for
            efficient progression of S phase and DNA replication checkpoint
  JOURNAL   J Biol Chem 282 (4), 2729-2740 (2007)
   PUBMED   17102137
  REMARK    GeneRIF: Tipin is a checkpoint mediator that cooperates with Tim
            and may regulate the nuclear relocation of Claspin in response to
            replication checkpoint
REFERENCE   8  (residues 1 to 200)
  AUTHORS   Chou,D.M. and Elledge,S.J.
  TITLE     Tipin and Timeless form a mutually protective complex required for
            genotoxic stress resistance and checkpoint function
  JOURNAL   Proc Natl Acad Sci U S A 103 (48), 18143-18147 (2006)
   PUBMED   17116885
  REMARK    GeneRIF: observation explains the similar checkpoint phenotypes
            observed in both Tipin- and Timeless-depleted cells
REFERENCE   9  (residues 1 to 200)
  AUTHORS   Gotter,A.L.
  TITLE     Tipin, a novel timeless-interacting protein, is developmentally
            co-expressed with timeless and disrupts its self-association
  JOURNAL   J Mol Biol 331 (1), 167-176 (2003)
   PUBMED   12875843
REFERENCE   10 (residues 1 to 200)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            
            On Dec 14, 2021 this sequence version replaced XP_016877880.1.
            
            Summary: The protein encoded by this gene is part of the replisome
            complex, a group of proteins that support DNA replication. It binds
            TIM, which is involved in circadian rhythm regulation, and aids in
            protecting cells against DNA damage and stress. Two pseudogenes and
            two transcript variants encoding different isoforms have been found
            for this gene. [provided by RefSeq, Jul 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2900048.1,
                                           SRR1803613.329262.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..200
                     /product="TIMELESS-interacting protein isoform 2"
                     /note="timeless-interacting protein; CSM3 homolog"
                     /calculated_mol_wt=23152
     Region          <2..47
                     /region_name="Swi3"
                     /note="Replication Fork Protection Component Swi3;
                     pfam07962"
                     /db_xref="CDD:462324"
     CDS             1..200
                     /gene="TIPIN"
                     /coded_by="NM_001398285.1:304..906"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:54962"
                     /db_xref="HGNC:HGNC:30750"
                     /db_xref="MIM:610716"
ORIGIN      
        1 mlirhmehwa hrlfpklqfe dfidrveylg skkevqtclk rirldlpilh edfvsnndev
       61 aennehdvts teldpfltnl sesemfasel srslteeqqq riernkqlal errqakllsn
      121 sqtlgndmlm ntprahtvee vntdedqkee snglnedild npcndaiant lneeetlldq
      181 sfknvqqqld atsrnitear
//
LOCUS       NP_001356346             273 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA excision repair protein ERCC-1 isoform 3 [Homo sapiens].
ACCESSION   NP_001356346 XP_016881955
VERSION     NP_001356346.1
DBSOURCE    REFSEQ: accession NM_001369417.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Khalouei,A., Masoumi-Ardakani,Y., Jafarzaheh,A., Kalantari
            Khandani,B., Sedghy,F., Khosravi Mashizi,A., Yaghoobi,M.M.,
            Zangouey,M. and Shahouzehi,B.
  TITLE     Association of ERCC1 Gene Polymorphisms (rs3212986 and rs11615)
            With the Risk of Lung Cancer in a Population From Southeast Iran
  JOURNAL   J Res Health Sci 24 (4), e00631 (2024)
   PUBMED   39431656
  REMARK    GeneRIF: Association of ERCC1 Gene Polymorphisms (rs3212986 and
            rs11615) With the Risk of Lung Cancer in a Population From
            Southeast Iran.
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Imani,M.M., Akbari,S., Shalchi,M., Sadeghi,E. and Sadeghi,M.
  TITLE     Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis
  JOURNAL   Arch Oral Biol 162, 105955 (2024)
   PUBMED   38479279
  REMARK    GeneRIF: Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis.
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Jamai,D., Gargouri,R., Selmi,B. and Khabir,A.
  TITLE     ERCC1 and MGMT Methylation as a Predictive Marker of Relapse and
            FOLFOX Response in Colorectal Cancer Patients from South Tunisia
  JOURNAL   Genes (Basel) 14 (7), 1467 (2023)
   PUBMED   37510370
  REMARK    GeneRIF: ERCC1 and MGMT Methylation as a Predictive Marker of
            Relapse and FOLFOX Response in Colorectal Cancer Patients from
            South Tunisia.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Liu,P., Perryman,M.B., Liao,W. and Siciliano,M.J.
  TITLE     Efficiency and limitations of the hn-cDNA library approach for the
            isolation of human transcribed genes from hybrid cells
  JOURNAL   Somat Cell Mol Genet 18 (1), 7-18 (1992)
   PUBMED   1372133
REFERENCE   7  (residues 1 to 273)
  AUTHORS   van Duin,M., van Den Tol,J., Hoeijmakers,J.H., Bootsma,D.,
            Rupp,I.P., Reynolds,P., Prakash,L. and Prakash,S.
  TITLE     Conserved pattern of antisense overlapping transcription in the
            homologous human ERCC-1 and yeast RAD10 DNA repair gene regions
  JOURNAL   Mol Cell Biol 9 (4), 1794-1798 (1989)
   PUBMED   2471070
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Hoeijmakers,J.H.
  TITLE     Characterization of genes and proteins involved in excision repair
            of human cells
  JOURNAL   J Cell Sci Suppl 6, 111-125 (1987)
   PUBMED   2821019
REFERENCE   9  (residues 1 to 273)
  AUTHORS   van Duin,M., de Wit,J., Odijk,H., Westerveld,A., Yasui,A.,
            Koken,M.H., Hoeijmakers,J.H. and Bootsma,D.
  TITLE     Molecular characterization of the human excision repair gene
            ERCC-1: cDNA cloning and amino acid homology with the yeast DNA
            repair gene RAD10
  JOURNAL   Cell 44 (6), 913-923 (1986)
   PUBMED   2420469
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Westerveld,A., Hoeijmakers,J.H., van Duin,M., de Wit,J., Odijk,H.,
            Pastink,A., Wood,R.D. and Bootsma,D.
  TITLE     Molecular cloning of a human DNA repair gene
  JOURNAL   Nature 310 (5976), 425-429 (1984)
   PUBMED   6462228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC138128.1, AC139353.3 and
            AC092309.3.
            
            On Apr 9, 2019 this sequence version replaced XP_016881955.1.
            
            Summary: The product of this gene functions in the nucleotide
            excision repair pathway, and is required for the repair of DNA
            lesions such as those induced by UV light or formed by
            electrophilic compounds including cisplatin. The encoded protein
            forms a heterodimer with the XPF endonuclease (also known as
            ERCC4), and the heterodimeric endonuclease catalyzes the 5'
            incision in the process of excising the DNA lesion. The
            heterodimeric endonuclease is also involved in recombinational DNA
            repair and in the repair of inter-strand crosslinks. Mutations in
            this gene result in cerebrooculofacioskeletal syndrome, and
            polymorphisms that alter expression of this gene may play a role in
            carcinogenesis. Multiple transcript variants encoding different
            isoforms have been found for this gene. The last exon of this gene
            overlaps with the CD3e molecule, epsilon associated protein gene on
            the opposite strand. [provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.299199.1,
                                           SRR14038194.191105.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..273
                     /product="DNA excision repair protein ERCC-1 isoform 3"
                     /note="DNA excision repair protein ERCC-1; excision repair
                     cross-complementation group 1; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 1 (includes overlapping antisense
                     sequence)"
                     /calculated_mol_wt=29862
     Region          99..226
                     /region_name="ERCC1_C-like"
                     /note="Central domain of ERCC1; cd22325"
                     /db_xref="CDD:411729"
     Site            order(117..119,166,179,183,186,189..190,193..198,200,204,
                     207..208,210..212,214..216,218..219,221..222)
                     /site_type="other"
                     /note="XPF interaction interface [polypeptide binding]"
                     /db_xref="CDD:411729"
     Region          235..264
                     /region_name="HHH"
                     /note="Helix-hairpin-helix motif; pfam00633"
                     /db_xref="CDD:425789"
     CDS             1..273
                     /gene="ERCC1"
                     /gene_synonym="COFS4; RAD10; UV20"
                     /coded_by="NM_001369417.1:206..1027"
                     /note="isoform 3 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS54279.1"
                     /db_xref="GeneID:2067"
                     /db_xref="HGNC:HGNC:3433"
                     /db_xref="MIM:126380"
ORIGIN      
        1 mdpgkdkegv pqpsgppark kfvipldede vppgvakplf rstqslptvd tsaqaapqty
       61 aeyaisqple gagatcptgs eplagetpnq alkpgaksns iivsprqrgn pvlkfvrnvp
      121 wefgdvipdy vlgqstcalf lslryhnlhp dyihgrlqsl gknfalrvll vqvdvkdpqq
      181 alkelakmci ladctlilaw speeagryle tykayeqkpa dllmekleqd fvsrsleqli
      241 aasredlalc pglgpqkarr lfdvlhepfl kvp
//
LOCUS       NP_001387199             275 aa            linear   PRI 21-NOV-2025
DEFINITION  carboxy-terminal domain RNA polymerase II polypeptide A small
            phosphatase 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001387199 XP_016860107
VERSION     NP_001387199.1
DBSOURCE    REFSEQ: accession NM_001400270.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Gervasi,N.M., Dimtchev,A., Clark,D.M., Dingle,M., Pisarchik,A.V.
            and Nesti,L.J.
  TITLE     C-terminal domain small phosphatase 1 (CTDSP1) regulates growth
            factor expression and axonal regeneration in peripheral nerve
            tissue
  JOURNAL   Sci Rep 11 (1), 14462 (2021)
   PUBMED   34262056
  REMARK    GeneRIF: C-terminal domain small phosphatase 1 (CTDSP1) regulates
            growth factor expression and axonal regeneration in peripheral
            nerve tissue.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Yang,X., Chen,Y., Zhou,Y., Wu,C., Li,Q., Wu,J., Hu,W.W., Zhao,W.Q.,
            Wei,W., Wu,C.P., Jiang,J.T. and Ji,M.
  TITLE     GPC5 suppresses lung cancer progression and metastasis via
            intracellular CTDSP1/AhR/ARNT signaling axis and extracellular
            exosome secretion
  JOURNAL   Oncogene 40 (25), 4307-4323 (2021)
   PUBMED   34079082
  REMARK    GeneRIF: GPC5 suppresses lung cancer progression and metastasis via
            intracellular CTDSP1/AhR/ARNT signaling axis and extracellular
            exosome secretion.
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Qian,W., Li,Q., Wu,X., Li,W., Li,Q., Zhang,J., Li,M., Zhang,D.,
            Zhao,H., Zou,X., Jia,H., Zhang,L., Yang,X.D. and Hou,Z.
  TITLE     Deubiquitinase USP29 promotes gastric cancer cell migration by
            cooperating with phosphatase SCP1 to stabilize Snail protein
  JOURNAL   Oncogene 39 (44), 6802-6815 (2020)
   PUBMED   32973332
  REMARK    GeneRIF: Deubiquitinase USP29 promotes gastric cancer cell
            migration by cooperating with phosphatase SCP1 to stabilize Snail
            protein.
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Knockaert,M., Sapkota,G., Alarcon,C., Massague,J. and
            Brivanlou,A.H.
  TITLE     Unique players in the BMP pathway: small C-terminal domain
            phosphatases dephosphorylate Smad1 to attenuate BMP signaling
  JOURNAL   Proc Natl Acad Sci U S A 103 (32), 11940-11945 (2006)
   PUBMED   16882717
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Yeo,M., Lee,S.K., Lee,B., Ruiz,E.C., Pfaff,S.L. and Gill,G.N.
  TITLE     Small CTD phosphatases function in silencing neuronal gene
            expression
  JOURNAL   Science 307 (5709), 596-600 (2005)
   PUBMED   15681389
  REMARK    GeneRIF: results show that REST/NRSF recruits SCPs to neuronal
            genes that contain RE-1 elements, leading to neuronal gene
            silencing in non-neuronal cells
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Yeo,M., Lin,P.S., Dahmus,M.E. and Gill,G.N.
  TITLE     A novel RNA polymerase II C-terminal domain phosphatase that
            preferentially dephosphorylates serine 5
  JOURNAL   J Biol Chem 278 (28), 26078-26085 (2003)
   PUBMED   12721286
  REMARK    GeneRIF: SCP1 may play a role in the regulation of gene expression,
            possibly by controlling the transition from initiation/capping to
            processive transcript elongation
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Ma,X., Wright,J., Dou,S., Olsen,P., Teeter,L., Adams,G. and
            Graviss,E.
  TITLE     Ethnic divergence and linkage disequilibrium of novel SNPs in the
            human NLI-IF gene: evidence of human origin and lack of association
            with tuberculosis susceptibility
  JOURNAL   J Hum Genet 47 (3), 140-145 (2002)
   PUBMED   11950066
  REMARK    GeneRIF: Polymorphisms vary significantly between races; Not
            associated with TB susceptibility in Caucasians.
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Marquet,S., Lepage,P., Hudson,T.J., Musser,J.M. and Schurr,E.
  TITLE     Complete nucleotide sequence and genomic structure of the human
            NRAMP1 gene region on chromosome region 2q35
  JOURNAL   Mamm Genome 11 (9), 755-762 (2000)
   PUBMED   10967134
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021016.5.
            
            On Jan 21, 2022 this sequence version replaced XP_016860107.1.
            
            Summary: This gene encodes a member of the small C-terminal domain
            phosphatase (SCP) family of nuclear phosphatases. These proteins
            play a role in transcriptional regulation through specific
            dephosphorylation of phosphoserine 5 within tandem heptapeptide
            repeats of the C-terminal domain of RNA polymerase II. The encoded
            protein plays a role in neuronal gene silencing in non-neuronal
            cells, and may also inhibit osteoblast differentiation.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene. [provided by RefSeq, Oct
            2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BQ719575.1, ERR4352443.695261.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..275
                     /product="carboxy-terminal domain RNA polymerase II
                     polypeptide A small phosphatase 1 isoform 5"
                     /EC_number="3.1.3.16"
                     /note="NLI-interacting factor 3; small C-terminal domain
                     phosphatase 1; nuclear LIM interactor-interacting factor
                     3; CTD (carboxy-terminal domain, RNA polymerase II,
                     polypeptide A) small phosphatase 1"
                     /calculated_mol_wt=29875
     Region          89..219
                     /region_name="HIF-SF_euk"
                     /note="Dullard-like phosphatase domain; TIGR02251"
                     /db_xref="CDD:274055"
     Site            order(95..99,103..104,150..153,157,189,205..206,208..210)
                     /site_type="active"
                     /db_xref="CDD:319823"
     CDS             1..275
                     /gene="CTDSP1"
                     /gene_synonym="NIF3; NLI-IF; NLIIF; SCP1"
                     /coded_by="NM_001400270.1:224..1051"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:58190"
                     /db_xref="HGNC:HGNC:21614"
                     /db_xref="MIM:605323"
ORIGIN      
        1 mdssavitqi skeeargplr gkgdqksaas qkprsrgilh slfccvcrdd gealpahsga
       61 pllveengai pktpvqyllp eakaqdsdki cvvidldetl vhssfkpvnn adfiipveid
      121 gvvhqvyvlk rphvdeflqr mgelfecvlf taslakyadp vadlldkwga frarlfresc
      181 vfhrgnyvkd lsrlgrdlrr vlildnspas yvfhpdnavs agwtgtgtga etqegvspfr
      241 ppwplgspvg gwvpsqsflh slpvpaahsp hppal
//
LOCUS       NP_001156729            1932 aa            linear   PRI 21-NOV-2025
DEFINITION  plexin-B3 isoform 2 [Homo sapiens].
ACCESSION   NP_001156729
VERSION     NP_001156729.1
DBSOURCE    REFSEQ: accession NM_001163257.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1932)
  AUTHORS   Zuo,Q., Yang,Y., Lyu,Y., Yang,C., Chen,C., Salman,S., Huang,T.Y.,
            Wicks,E.E., Jackson,W. 3rd, Datan,E., Qin,W. and Semenza,G.L.
  TITLE     Plexin-B3 expression stimulates MET signaling, breast cancer stem
            cell specification, and lung metastasis
  JOURNAL   Cell Rep 42 (3), 112164 (2023)
   PUBMED   36857181
  REMARK    GeneRIF: Plexin-B3 expression stimulates MET signaling, breast
            cancer stem cell specification, and lung metastasis.
REFERENCE   2  (residues 1 to 1932)
  AUTHORS   Wang,K., He,M., Fan,X., Zhou,J., Yang,J., Wang,L., Zhao,Z., Dai,C.
            and Zhang,Z.
  TITLE     SEMA5A-PLXNB3 Axis Promotes PDAC Liver Metastasis Outgrowth through
            Enhancing the Warburg Effect
  JOURNAL   J Immunol Res 2023, 3274467 (2023)
   PUBMED   36741230
  REMARK    GeneRIF: SEMA5A-PLXNB3 Axis Promotes PDAC Liver Metastasis
            Outgrowth through Enhancing the Warburg Effect.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1932)
  AUTHORS   Kuhlmann,L., Govindarajan,M., Mejia-Guerrero,S., Ignatchenko,V.,
            Liu,L.Y., Grunwald,B.T., Cruickshank,J., Berman,H., Khokha,R. and
            Kislinger,T.
  TITLE     Glycoproteomics Identifies Plexin-B3 as a Targetable Cell Surface
            Protein Required for the Growth and Invasion of Triple-Negative
            Breast Cancer Cells
  JOURNAL   J Proteome Res 21 (9), 2224-2236 (2022)
   PUBMED   35981243
  REMARK    GeneRIF: Glycoproteomics Identifies Plexin-B3 as a Targetable Cell
            Surface Protein Required for the Growth and Invasion of
            Triple-Negative Breast Cancer Cells.
REFERENCE   4  (residues 1 to 1932)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 1932)
  AUTHORS   Nihonmatsu-Kikuchi,N., Yu,X.J., Matsuda,Y., Ozawa,N., Ito,T.,
            Satou,K., Kaname,T., Iwasaki,Y., Akagi,A., Yoshida,M., Toru,S.,
            Hirokawa,K., Takashima,A., Hasegawa,M., Uchihara,T. and
            Tatebayashi,Y.
  TITLE     Essential roles of plexin-B3+ oligodendrocyte precursor cells in
            the pathogenesis of Alzheimer's disease
  JOURNAL   Commun Biol 4 (1), 870 (2021)
   PUBMED   34267322
  REMARK    GeneRIF: Essential roles of plexin-B3(+) oligodendrocyte precursor
            cells in the pathogenesis of Alzheimer's disease.
            Erratum:[Commun Biol. 2021 Dec 2;4(1):1372. doi:
            10.1038/s42003-021-02905-5. PMID: 34857866]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1932)
  AUTHORS   Conrotto,P., Corso,S., Gamberini,S., Comoglio,P.M. and Giordano,S.
  TITLE     Interplay between scatter factor receptors and B plexins controls
            invasive growth
  JOURNAL   Oncogene 23 (30), 5131-5137 (2004)
   PUBMED   15184888
REFERENCE   7  (residues 1 to 1932)
  AUTHORS   Artigiani,S., Conrotto,P., Fazzari,P., Gilestro,G.F., Barberis,D.,
            Giordano,S., Comoglio,P.M. and Tamagnone,L.
  TITLE     Plexin-B3 is a functional receptor for semaphorin 5A
  JOURNAL   EMBO Rep 5 (7), 710-714 (2004)
   PUBMED   15218527
  REMARK    GeneRIF: Plexin-B3 is a functional receptor for semaphorin 5A
REFERENCE   8  (residues 1 to 1932)
  AUTHORS   Perrot,V., Vazquez-Prado,J. and Gutkind,J.S.
  TITLE     Plexin B regulates Rho through the guanine nucleotide exchange
            factors leukemia-associated Rho GEF (LARG) and PDZ-RhoGEF
  JOURNAL   J Biol Chem 277 (45), 43115-43120 (2002)
   PUBMED   12183458
REFERENCE   9  (residues 1 to 1932)
  AUTHORS   Tamagnone,L., Artigiani,S., Chen,H., He,Z., Ming,G.I., Song,H.,
            Chedotal,A., Winberg,M.L., Goodman,C.S., Poo,M., Tessier-Lavigne,M.
            and Comoglio,P.M.
  TITLE     Plexins are a large family of receptors for transmembrane,
            secreted, and GPI-anchored semaphorins in vertebrates
  JOURNAL   Cell 99 (1), 71-80 (1999)
   PUBMED   10520995
  REMARK    Erratum:[Cell 2001 Jan 26;104(2):following 320]
REFERENCE   10 (residues 1 to 1932)
  AUTHORS   Sandoval,N., Bauer,D., Brenner,V., Coy,J.F., Drescher,B.,
            Kioschis,P., Korn,B., Nyakatura,G., Poustka,A., Reichwald,K.,
            Rosenthal,A. and Platzer,M.
  TITLE     The genomic organization of a human creatine transporter (CRTR)
            gene located in Xq28
  JOURNAL   Genomics 35 (2), 383-385 (1996)
   PUBMED   8661155
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK292535.1, AK307894.1,
            AF149019.1 and AK295762.1.
            
            Summary: The protein encoded by this gene is a member of the plexin
            family. It functions as a receptor for semaphorin 5A, and plays a
            role in axon guidance, invasive growth and cell migration.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2009].
            
            Transcript Variant: This variant (2) contains an additional exon in
            the 5' region compared to variant 1. This results in translation
            initiation from a start codon (with a strong Kozak signal) found in
            this exon, and a longer isoform (2) with a distinct N-terminus
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AK295762.1 [ECO:0000331]
            RNAseq introns       :: partial sample support SAMEA2145743,
                                    SAMEA2153980 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1932
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..1932
                     /product="plexin-B3 isoform 2"
                     /note="plexin 6"
                     /calculated_mol_wt=209171
     Region          70..495
                     /region_name="Sema_plexin_B3"
                     /note="The Sema domain, a protein interacting module, of
                     Plexin B3; cd11277"
                     /db_xref="CDD:200538"
     Site            order(122..124,241,246,251..252,274,383..384,391,396..398)
                     /site_type="other"
                     /note="putative Semaphorin binding site [polypeptide
                     binding]"
                     /db_xref="CDD:200538"
     Region          497..548
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          556..642
                     /region_name="TIG_plexin"
                     /note="TIG domain; pfam17960"
                     /db_xref="CDD:465588"
     Region          656..690
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          712..809
                     /region_name="TIG_2"
                     /note="TIG domain found in plexin; pfam18020"
                     /db_xref="CDD:465619"
     Region          858..949
                     /region_name="IPT_plexin_repeat1"
                     /note="First repeat of the IPT domain of Plexins and Cell
                     Surface Receptors (PCSR) . Plexins are involved in the
                     regulation of cell proliferation and of cellular adhesion
                     and repulsion receptors. In general, there are three
                     copies of the IPT domain present...; cd01180"
                     /db_xref="CDD:238585"
     Region          950..1035
                     /region_name="IPT_plexin_repeat2"
                     /note="Second repeat of the IPT domain of Plexins and Cell
                     Surface Receptors (PCSR) . Plexins are involved in the
                     regulation of cell proliferation and of cellular adhesion
                     and repulsion receptors. In general, there are three
                     copies of the IPT domain present...; cd01179"
                     /db_xref="CDD:238584"
     Region          1038..1169
                     /region_name="IPT"
                     /note="Immunoglobulin-like fold, Plexins, Transcription
                     factors (IPT). IPTs are also known as Transcription factor
                     ImmunoGlobin (TIG) domains. They are present in
                     intracellular transcription factors, cell surface
                     receptors (such as plexins and scatter factor...; cl15674"
                     /db_xref="CDD:472823"
     Region          <1199..1265
                     /region_name="TIG"
                     /note="IPT/TIG domain; pfam01833"
                     /db_xref="CDD:460355"
     Region          1350..1894
                     /region_name="Plexin_cytopl"
                     /note="Plexin cytoplasmic RasGAP domain; pfam08337"
                     /db_xref="CDD:462434"
     CDS             1..1932
                     /gene="PLXNB3"
                     /gene_synonym="PLEXB3; PLEXR; PLXN6"
                     /coded_by="NM_001163257.2:219..6017"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55536.1"
                     /db_xref="GeneID:5365"
                     /db_xref="HGNC:HGNC:9105"
                     /db_xref="MIM:300214"
ORIGIN      
        1 meltpasslt csllsprlpg sfpqlrrvpp csrpwlpkap vmarwppfgl cllllllspp
       61 plpltgahrf sapnttlnhl alapgrgtly vgavnrlfql spelqleava vtgpvidspd
      121 cvpfrdpaec pqaqltdnan qlllvssraq elvacgqvrq gvcetrrlgd vaevlyqaed
      181 pgdgqfvaan tpgvatvglv vplpgrdlll varglagkls agvpplairq lagsqpfsse
      241 glgrlvvgdf sdynnsyvga fadarsayfv frrrgaraqa eyrsyvarvc lgdtnlysyv
      301 evplacqgqg liqaaflapg tllgvfaagp rgtqaalcaf pmvelgasme qarrlcytag
      361 grgpsgaeea tveygvtsrc vtlpldspes ypcgdehtps piagrqplev qpllklgqpv
      421 savaalqadg hmiaflgdtq gqlykvflhg sqgqvyhsqq vgppgsaisp dllldssgsh
      481 lyvltahqvd ripvaacpqf pdcasclqaq dplcgwcvlq grctrkgqcg ragqlnqwlw
      541 syeedshclh iqsllpghhp rqeqgqvtls vprlpildad eyfhcafgdy dslahvegph
      601 vacvtppqdq vplnppgtdh vtvplalmfe dvtvaatnfs fydcsavqal eaaapcracv
      661 gsiwrchwcp qsshcvygeh cpegertiys aqevdiqvrg pgacpqvegl agphlvpvgw
      721 eshlalrvrn lqhfrglpas fhcwlelpge lrglpatlee tagdsglihc qahqfypsms
      781 qrelpvpiyv tqgeaqrldn thalyvilyd camghpdcsh cqaanrslgc lwcadgqpac
      841 rygplcppga vellcpapsi davepltgpp egglaltilg snlgrafadv qyavsvasrp
      901 cnpepslyrt sarivcvtsp apngttgpvr vaiksqppgi ssqhftyqdp vllslsprwg
      961 pqaggtqlti rgqhlqtggn tsafvggqpc pilepvcpea ivcrtrpqaa pgeaavlvvf
     1021 ghaqrtllas pfrytanpql vaaepsasfr gggrlirvrg tgldvvqrpl lsvwleadae
     1081 vqasraqpqd pqprrscgap aadpqaciql gggllqcstv csvnssslll crspavpdra
     1141 hpqrvfftld nvqvdfasas ggqgflyqpn prlaplsreg parpyrlkpg hvldvegegl
     1201 nlgiskeevr vhigrgeclv ktltrthlyc eppahapqpa ngsglpqfvv qmgnvqlalg
     1261 pvqyeaeppl safpveaqag vgmgaavlia avllltlmyr hkskqalrdy qkvlvqlesl
     1321 etgvgdqcrk eftdlmtemt dlssdlegsg ipfldyrtya eraffpghgg cplqpkpegp
     1381 gedghcatvr qgltqlsnll nsklflltli htleeqpsfs qrdrchvasl lslalhgkle
     1441 yltdimrtll gdlaahyvhr npklmlrrte tmveklltnw lsiclyaflr evageplyml
     1501 fraiqyqvdk gpvdavtgka krtlndsrll redvefqplt lmvlvgpgag gaagssemqr
     1561 vparvldtdt itqvkekvld qvykgtpfsq rpsvhaldle wrsglaghlt lsdedltsvt
     1621 qnhwkrlntl qhykvpdgat vglvpqlhrg stisqslaqr cplgeniptl edgeeggvcl
     1681 whlvkateep egakvrcssl rereparaka ipeiyltrll smkgtlqkfv ddtfqailsv
     1741 nrpipiavky lfdlldelae khgiedpgtl hiwktnslll rfwvnalknp qlifdvrvsd
     1801 nvdailavia qtfidsctts ehkvgrdspv nkllyareip rykqmveryy adirqsspas
     1861 yqemnsalae lsgnytsaph clealqelyn hihryydqii saleedpvgq klqlacrlqq
     1921 vaalvenkvt dl
//
LOCUS       NP_001289550             617 aa            linear   PRI 21-NOV-2025
DEFINITION  acetylcholinesterase isoform E4-E5 precursor [Homo sapiens].
ACCESSION   NP_001289550 XP_005250414
VERSION     NP_001289550.1
DBSOURCE    REFSEQ: accession NM_001302621.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Kongkaew,N., Hengphasatporn,K., Shigeta,Y., Rungrotmongkol,T. and
            Harada,R.
  TITLE     Preferential Door for Ligand Binding and Unbinding Pathways in
            Inhibited Human Acetylcholinesterase
  JOURNAL   J Phys Chem Lett 15 (21), 5696-5704 (2024)
   PUBMED   38768263
  REMARK    GeneRIF: Preferential Door for Ligand Binding and Unbinding
            Pathways in Inhibited Human Acetylcholinesterase.
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Chen,M., Zhang,C., Li,H., Zheng,S., Li,Y., Yuan,M., Chen,Y., Wu,J.
            and Sun,Q.
  TITLE     PLA2G4A and ACHE modulate lipid profiles via glycerophospholipid
            metabolism in platinum-resistant gastric cancer
  JOURNAL   J Transl Med 22 (1), 249 (2024)
   PUBMED   38454407
  REMARK    GeneRIF: PLA2G4A and ACHE modulate lipid profiles via
            glycerophospholipid metabolism in platinum-resistant gastric
            cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 617)
  AUTHORS   Joda,M., Waters,K.A. and Machaalani,R.
  TITLE     Choline-acetyltransferase (ChAT) and acetylcholinesterase (AChE) in
            the human infant dorsal motor nucleus of the Vagus (DMNV), and
            alterations according to sudden infant death syndrome (SIDS)
            category
  JOURNAL   Neurobiol Dis 188, 106319 (2023)
   PUBMED   37813167
  REMARK    GeneRIF: Choline-acetyltransferase (ChAT) and acetylcholinesterase
            (AChE) in the human infant dorsal motor nucleus of the Vagus
            (DMNV), and alterations according to sudden infant death syndrome
            (SIDS) category.
REFERENCE   4  (residues 1 to 617)
  AUTHORS   Budhbhatti,U., Chauhan,A., Bhatt,D., Parmar,C., Damani,V., Patel,A.
            and Joshi,C.
  TITLE     Association of NOTCH4 and ACHE gene polymorphism in Alzheimer's
            disease of Gujarat cohort
  JOURNAL   Neurosci Lett 814, 137428 (2023)
   PUBMED   37544578
  REMARK    GeneRIF: Association of NOTCH4 and ACHE gene polymorphism in
            Alzheimer's disease of Gujarat cohort.
REFERENCE   5  (residues 1 to 617)
  AUTHORS   Ohno,K., Brengman,J., Tsujino,A. and Engel,A.G.
  TITLE     Human endplate acetylcholinesterase deficiency caused by mutations
            in the collagen-like tail subunit (ColQ) of the asymmetric enzyme
  JOURNAL   Proc Natl Acad Sci U S A 95 (16), 9654-9659 (1998)
   PUBMED   9689136
REFERENCE   6  (residues 1 to 617)
  AUTHORS   Bartels,C.F., Zelinski,T. and Lockridge,O.
  TITLE     Mutation at codon 322 in the human acetylcholinesterase (ACHE) gene
            accounts for YT blood group polymorphism
  JOURNAL   Am J Hum Genet 52 (5), 928-936 (1993)
   PUBMED   8488842
REFERENCE   7  (residues 1 to 617)
  AUTHORS   Spring,F.A., Gardner,B. and Anstee,D.J.
  TITLE     Evidence that the antigens of the Yt blood group system are located
            on human erythrocyte acetylcholinesterase
  JOURNAL   Blood 80 (8), 2136-2141 (1992)
   PUBMED   1391965
REFERENCE   8  (residues 1 to 617)
  AUTHORS   Shafferman,A., Kronman,C., Flashner,Y., Leitner,M., Grosfeld,H.,
            Ordentlich,A., Gozes,Y., Cohen,S., Ariel,N., Barak,D. et al.
  TITLE     Mutagenesis of human acetylcholinesterase. Identification of
            residues involved in catalytic activity and in polypeptide folding
  JOURNAL   J Biol Chem 267 (25), 17640-17648 (1992)
   PUBMED   1517212
REFERENCE   9  (residues 1 to 617)
  AUTHORS   Ehrlich,G., Viegas-Pequignot,E., Ginzberg,D., Sindel,L., Soreq,H.
            and Zakut,H.
  TITLE     Mapping the human acetylcholinesterase gene to chromosome 7q22 by
            fluorescent in situ hybridization coupled with selective PCR
            amplification from a somatic hybrid cell panel and
            chromosome-sorted DNA libraries
  JOURNAL   Genomics 13 (4), 1192-1197 (1992)
   PUBMED   1380483
REFERENCE   10 (residues 1 to 617)
  AUTHORS   Getman,D.K., Eubanks,J.H., Camp,S., Evans,G.A. and Taylor,P.
  TITLE     The human gene encoding acetylcholinesterase is located on the long
            arm of chromosome 7
  JOURNAL   Am J Hum Genet 51 (1), 170-177 (1992)
   PUBMED   1609795
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011895.4, BC105060.1 and
            AI831696.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 7, 2014 this sequence version replaced XP_005250414.1.
            
            Summary: Acetylcholinesterase hydrolyzes the neurotransmitter,
            acetylcholine at neuromuscular junctions and brain cholinergic
            synapses, and thus terminates signal transmission. It is also found
            on the red blood cell membranes, where it constitutes the Yt blood
            group antigen. Acetylcholinesterase exists in multiple molecular
            forms which possess similar catalytic properties, but differ in
            their oligomeric assembly and mode of cell attachment to the cell
            surface. It is encoded by the single ACHE gene, and the structural
            diversity in the gene products arises from alternative mRNA
            splicing, and post-translational associations of catalytic and
            structural subunits. The major form of acetylcholinesterase found
            in brain, muscle and other tissues is the hydrophilic species,
            which forms disulfide-linked oligomers with collagenous, or
            lipid-containing structural subunits. The other, alternatively
            spliced form, expressed primarily in the erythroid tissues, differs
            at the C-terminal end, and contains a cleavable hydrophobic peptide
            with a GPI-anchor site. It associates with the membranes through
            the phosphoinositide (PI) moieties added post-translationally. AChE
            activity may constitute a sensitive biomarker of RBC ageing in
            vivo, and thus, may be of aid in understanding the effects of
            transfusion[provided by RefSeq, Sep 2019].
            
            Transcript Variant: This variant (4) uses an alternate splice site
            in the 5' UTR, lacks an exon in 3' UTR and 3' coding region and
            uses an alternate terminal exon, compared to isoform E4-E6. The
            encoded isoform (4) is longer and has a distinct C-terminus
            compared to isoform E4-E6.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105060.1, SRR18074967.1649057.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..617
                     /product="acetylcholinesterase isoform E4-E5 precursor"
                     /EC_number="3.1.1.7"
                     /note="Yt blood group; apoptosis-related
                     acetylcholinesterase; acetylcholinesterase (Cartwright
                     blood group)"
                     /calculated_mol_wt=64156
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3238
     Region          37..563
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            order(151..153,233..235,238,393,397..398,433,479,482)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(234,365,478)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     CDS             1..617
                     /gene="ACHE"
                     /gene_synonym="ACEE; ARACHE; N-ACHE; YT"
                     /coded_by="NM_001302621.3:111..1964"
                     /note="isoform E4-E5 precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS5710.1"
                     /db_xref="GeneID:43"
                     /db_xref="HGNC:HGNC:108"
                     /db_xref="MIM:100740"
ORIGIN      
        1 mrppqcllht pslaspllll llwllgggvg aegredaell vtvrggrlrg irlktpggpv
       61 saflgipfae ppmgprrflp pepkqpwsgv vdattfqsvc yqyvdtlypg fegtemwnpn
      121 relsedclyl nvwtpyprpt sptpvlvwiy gggfysgass ldvydgrflv qaertvlvsm
      181 nyrvgafgfl alpgsreapg nvglldqrla lqwvqenvaa fggdptsvtl fgesagaasv
      241 gmhllsppsr glfhravlqs gapngpwatv gmgearrrat qlahlvgcpp ggtggndtel
      301 vaclrtrpaq vlvnhewhvl pqesvfrfsf vpvvdgdfls dtpealinag dfhglqvlvg
      361 vvkdegsyfl vygapgfskd neslisraef lagvrvgvpq vsdlaaeavv lhytdwlhpe
      421 dparlreals dvvgdhnvvc pvaqlagrla aqgarvyayv fehrastlsw plwmgvphgy
      481 eiefifgipl dpsrnytaee kifaqrlmry wanfartgdp neprdpkapq wppytagaqq
      541 yvsldlrple vrrglraqac afwnrflpkl lsataseaps tcpgfthgea aprpglplpl
      601 lllhqllllf lshlrrl
//
LOCUS       NP_001317014            1498 aa            linear   PRI 21-NOV-2025
DEFINITION  neurexin-1 isoform alpha8 precursor [Homo sapiens].
ACCESSION   NP_001317014 XP_016860808
VERSION     NP_001317014.1
DBSOURCE    REFSEQ: accession NM_001330085.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1498)
  AUTHORS   Sebastian,R., Jin,K., Pavon,N., Bansal,R., Potter,A., Song,Y.,
            Babu,J., Gabriel,R., Sun,Y., Aronow,B. and Pak,C.
  TITLE     Schizophrenia-associated NRXN1 deletions induce
            developmental-timing- and cell-type-specific vulnerabilities in
            human brain organoids
  JOURNAL   Nat Commun 14 (1), 3770 (2023)
   PUBMED   37355690
  REMARK    GeneRIF: Schizophrenia-associated NRXN1 deletions induce
            developmental-timing- and cell-type-specific vulnerabilities in
            human brain organoids.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1498)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1498)
  AUTHORS   Rhoades,R., Henry,B., Prichett,D., Fang,Y. and Teng,S.
  TITLE     Computational Saturation Mutagenesis to Investigate the Effects of
            Neurexin-1 Mutations on AlphaFold Structure
  JOURNAL   Genes (Basel) 13 (5), 789 (2022)
   PUBMED   35627176
  REMARK    GeneRIF: Computational Saturation Mutagenesis to Investigate the
            Effects of Neurexin-1 Mutations on AlphaFold Structure.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1498)
  AUTHORS   Aksu Uzunhan,T. and Ayaz,A.
  TITLE     Homozygous exonic and intragenic NRXN1 deletion presenting as
            either West syndrome or autism spectrum disorder in two siblings
  JOURNAL   Clin Neurol Neurosurg 214, 107141 (2022)
   PUBMED   35101781
  REMARK    GeneRIF: Homozygous exonic and intragenic NRXN1 deletion presenting
            as either West syndrome or autism spectrum disorder in two
            siblings.
REFERENCE   5  (residues 1 to 1498)
  AUTHORS   Yan,Q., Weyn-Vanhentenryck,S.M., Wu,J., Sloan,S.A., Zhang,Y.,
            Chen,K., Wu,J.Q., Barres,B.A. and Zhang,C.
  TITLE     Systematic discovery of regulated and conserved alternative exons
            in the mammalian brain reveals NMD modulating chromatin regulators
  JOURNAL   Proc Natl Acad Sci U S A 112 (11), 3445-3450 (2015)
   PUBMED   25737549
REFERENCE   6  (residues 1 to 1498)
  AUTHORS   Tabuchi,K. and Sudhof,T.C.
  TITLE     Structure and evolution of neurexin genes: insight into the
            mechanism of alternative splicing
  JOURNAL   Genomics 79 (6), 849-859 (2002)
   PUBMED   12036300
REFERENCE   7  (residues 1 to 1498)
  AUTHORS   Rowen,L., Young,J., Birditt,B., Kaur,A., Madan,A., Philipps,D.L.,
            Qin,S., Minx,P., Wilson,R.K., Hood,L. and Graveley,B.R.
  TITLE     Analysis of the human neurexin genes: alternative splicing and the
            generation of protein diversity
  JOURNAL   Genomics 79 (4), 587-597 (2002)
   PUBMED   11944992
REFERENCE   8  (residues 1 to 1498)
  AUTHORS   Ichtchenko,K., Hata,Y., Nguyen,T., Ullrich,B., Missler,M.,
            Moomaw,C. and Sudhof,T.C.
  TITLE     Neuroligin 1: a splice site-specific ligand for beta-neurexins
  JOURNAL   Cell 81 (3), 435-443 (1995)
   PUBMED   7736595
REFERENCE   9  (residues 1 to 1498)
  AUTHORS   Ullrich,B., Ushkaryov,Y.A. and Sudhof,T.C.
  TITLE     Cartography of neurexins: more than 1000 isoforms generated by
            alternative splicing and expressed in distinct subsets of neurons
  JOURNAL   Neuron 14 (3), 497-507 (1995)
   PUBMED   7695896
REFERENCE   10 (residues 1 to 1498)
  AUTHORS   Ushkaryov,Y.A., Petrenko,A.G., Geppert,M. and Sudhof,T.C.
  TITLE     Neurexins: synaptic cell surface proteins related to the
            alpha-latrotoxin receptor and laminin
  JOURNAL   Science 257 (5066), 50-56 (1992)
   PUBMED   1621094
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007682.3, AC009234.3,
            AC007462.3, AC068725.5, AC069550.4 and AC078994.3.
            
            On Aug 16, 2016 this sequence version replaced XP_016860808.1.
            
            Summary: This gene encodes a single-pass type I membrane protein
            that belongs to the neurexin family. Neurexins are cell-surface
            receptors that bind neuroligins to form Ca(2+)-dependent
            neurexin/neuroligin complexes at synapses in the central nervous
            system. This complex is required for efficient neurotransmission
            and is involved in the formation of synaptic contacts. Three
            members of this gene family have been studied in detail and are
            estimated to generate over 3,000 variants through the use of two
            alternative promoters (alpha and beta) and extensive alternative
            splicing in each family member. Recently, a third promoter (gamma)
            was identified for this gene in the 3' region. Mutations in this
            gene are associated with Pitt-Hopkins-like syndrome-2 and may
            contribute to susceptibility to schizophrenia. [provided by RefSeq,
            Aug 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1498
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.3"
     Protein         1..1498
                     /product="neurexin-1 isoform alpha8 precursor"
                     /note="neurexin I"
                     /calculated_mol_wt=161319
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3097
     Region          30..190
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Region          307..446
                     /region_name="LamG"
                     /note="Laminin G domain; smart00282"
                     /db_xref="CDD:214598"
     Region          503..652
                     /region_name="LamG"
                     /note="Laminin G domain; smart00282"
                     /db_xref="CDD:214598"
     Region          680..713
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          746..867
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          924..1052
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          1147..1295
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          1443..1461
                     /region_name="4.1m"
                     /note="putative band 4.1 homologues' binding motif;
                     smart00294"
                     /db_xref="CDD:128590"
     CDS             1..1498
                     /gene="NRXN1"
                     /gene_synonym="Hs.22998; PTHSL2; SCZD17"
                     /coded_by="NM_001330085.2:1074..5570"
                     /note="isoform alpha8 precursor is encoded by transcript
                     variant alpha8"
                     /db_xref="GeneID:9378"
                     /db_xref="HGNC:HGNC:8008"
                     /db_xref="MIM:600565"
ORIGIN      
        1 mgtallqrgg cfllclslll lgcwaelgsg lefpgaegqw trfpkwnacc esemsfqlkt
       61 rsarglvlyf ddegfcdfle liltrggrlq lsfsifcaep atlladtpvn dgawhsvrir
      121 rqfrnttlfi dqveakwvev kskrrdmtvf sglfvgglpp elraaalklt lasvrerepf
      181 kgwirdvrvn ssqvlpvdsg evklddeppn sgggspceag eegeggvcln ggvcsvvddq
      241 avcdcsrtgf rgkdcsqedn nveglahlmm gdqgkskgke eyiatfkgse yfcydlsqnp
      301 iqsssdeitl sfktlqrngl mlhtgksady vnlalkngav slvinlgsga fealvepvng
      361 kfndnawhdv kvtrnlrqhs gighamvtis vdgiltttgy tqedytmlgs ddffyvggsp
      421 stadlpgspv snnfmgclke vvyknndvrl elsrlakqgd pkmkihgvva fkcenvatld
      481 pitfetpesf islpkwnakk tgsisfdfrt tepnglilfs hgkprhqkda khpqmikvdf
      541 faiemldghl yllldmgsgt ikikallkkv ndgewyhvdf qrdgrsgtis vntlrtpyta
      601 pgeseildld delylgglpe nkaglvfpte vwtallnygy vgcirdlfid gqskdirqma
      661 evqstagvkp scsketakpc lsnpcknngm crdgwnryvc dcsgtgylgr scereatvls
      721 ydgsmfmkiq lpvvmhteae dvslrfrsqr aygilmatts rdsadtlrle ldagrvkltv
      781 nlgkgpetlf agynlndnew htvrvvrrgk slkltvddqq amtgqmagdh trlefhniet
      841 giiterryls svpsnfighl qsltfngmay idlckngdid ycelnarfgf rniiadpvtf
      901 ktkssyvala tlqaytsmhl ffqfkttsld glilynsgdg ndfivvelvk gylhyvfdlg
      961 nganlikgss nkplndnqwh nvmisrdtsn lhtvkidtki ttqitagarn ldlksdlyig
     1021 gvaketyksl pklvhakegf qgclasvdln grlpdlisda lfcngqierg cegpsttcqe
     1081 dscsnqgvcl qqwdgfscdc smtsfsgplc ndpgttyifs kgggqitykw ppndrpstra
     1141 drlaigfstv qkeavlvrvd sssglgdyle lhihqgkigv kfnvgtddia ieesnaiind
     1201 gkyhvvrftr sggnatlqvd swpvierypa gnndnerlai arqripyrlg rvvdewlldk
     1261 grqltifnsq atiiiggkeq gqpfqgqlsg lyynglkvln maaendania ivgnvrlvge
     1321 vpssmttest atamqsemst simettttla tstarrgkpp tkepisqttd dilvasaecp
     1381 sddedidpce pssgglanpt raggrepypg saeviresss ttgmvvgiva aaalcilill
     1441 yamykyrnrd egsyhvdesr nyisnsaqsn gavvkekqps sakssnknkk nkdkeyyv
//
LOCUS       NP_001362765             403 aa            linear   PRI 21-NOV-2025
DEFINITION  WAS/WASL-interacting protein family member 1 isoform c [Homo
            sapiens].
ACCESSION   NP_001362765
VERSION     NP_001362765.1
DBSOURCE    REFSEQ: accession NM_001375836.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Dong,Y., Jin,Q., Sun,M., Qi,D., Qu,H., Wang,X. and Quan,C.
  TITLE     CLDN6 inhibits breast cancer metastasis through WIP-dependent actin
            cytoskeleton-mediated autophagy
  JOURNAL   J Exp Clin Cancer Res 42 (1), 68 (2023)
   PUBMED   36935496
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Sokolik,C.G., Qassem,N. and Chill,J.H.
  TITLE     The Disordered Cellular Multi-Tasker WIP and Its Protein-Protein
            Interactions: A Structural View
  JOURNAL   Biomolecules 10 (7), 1084 (2020)
   PUBMED   32708183
  REMARK    GeneRIF: The Disordered Cellular Multi-Tasker WIP and Its
            Protein-Protein Interactions: A Structural View.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 403)
  AUTHORS   Vaduva,G., Martinez-Quiles,N., Anton,I.M., Martin,N.C., Geha,R.S.,
            Hopper,A.K. and Ramesh,N.
  TITLE     The human WASP-interacting protein, WIP, activates the cell
            polarity pathway in yeast
  JOURNAL   J Biol Chem 274 (24), 17103-17108 (1999)
   PUBMED   10358064
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Stewart,D.M., Tian,L. and Nelson,D.L.
  TITLE     Mutations that cause the Wiskott-Aldrich syndrome impair the
            interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP
            interacting protein
  JOURNAL   J Immunol 162 (8), 5019-5024 (1999)
   PUBMED   10202051
REFERENCE   8  (residues 1 to 403)
  AUTHORS   Ramesh,N., Anton,I.M., Martinez-Quiles,N. and Geha,R.S.
  TITLE     Waltzing with WASP
  JOURNAL   Trends Cell Biol 9 (1), 15-19 (1999)
   PUBMED   10087612
  REMARK    Review article
REFERENCE   9  (residues 1 to 403)
  AUTHORS   Anton,I.M., Lu,W., Mayer,B.J., Ramesh,N. and Geha,R.S.
  TITLE     The Wiskott-Aldrich syndrome protein-interacting protein (WIP)
            binds to the adaptor protein Nck
  JOURNAL   J Biol Chem 273 (33), 20992-20995 (1998)
   PUBMED   9694849
REFERENCE   10 (residues 1 to 403)
  AUTHORS   Ramesh,N., Anton,I.M., Hartwig,J.H. and Geha,R.S.
  TITLE     WIP, a protein associated with wiskott-aldrich syndrome protein,
            induces actin polymerization and redistribution in lymphoid cells
  JOURNAL   Proc Natl Acad Sci U S A 94 (26), 14671-14676 (1997)
   PUBMED   9405671
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104595.6 and AC010894.10.
            
            Summary: This gene encodes a protein that plays an important role
            in the organization of the actin cytoskeleton. The encoded protein
            binds to a region of Wiskott-Aldrich syndrome protein that is
            frequently mutated in Wiskott-Aldrich syndrome, an X-linked
            recessive disorder. Impairment of the interaction between these two
            proteins may contribute to the disease. Two transcript variants
            encoding the same protein have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (7), as well as variants 8 and 9,
            encodes isoform c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110288.1, SRR14038192.3083352.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..403
                     /product="WAS/WASL-interacting protein family member 1
                     isoform c"
                     /note="Wiskott-Aldrich syndrome protein interacting
                     protein; protein PRPL-2; WASP-interacting protein;
                     testicular tissue protein Li 226"
                     /calculated_mol_wt=40332
     Region          29..60
                     /region_name="WH2_WAS_WASL-1"
                     /note="Wiskott Aldrich syndrome homology region 2 (WH2
                     motif) in WAS/WASL-interacting protein family member 1;
                     cd22076"
                     /db_xref="CDD:409219"
     Site            order(29..33,35..37,39..41,44,46..60)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409219"
     Region          46..49
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409219"
     CDS             1..403
                     /gene="WIPF1"
                     /gene_synonym="PRPL-2; WAS2; WASPIP; WIP"
                     /coded_by="NM_001375836.1:179..1390"
                     /note="isoform c is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS92900.1"
                     /db_xref="GeneID:7456"
                     /db_xref="HGNC:HGNC:12736"
                     /db_xref="MIM:602357"
ORIGIN      
        1 mpvppppapp ppptfalant ekptlnkteq agrnallsdi skgkklkktv tndrsapild
       61 kpkgagaggg gggfgggggf gggggggggg sfggggppgl gglfqagmpk lrstanrdnd
      121 sggsrppllp pggrstsakp fsppsgpgrf pvpspghrsg ppepqrnrmp pprpdvgskp
      181 dsipppvpst prpiqssphn rgsppvpggp rqpspgptpp pfpgnrgtal gggsirqspl
      241 sssspfsnrp plpptpsral ddkppppppp vgnrpsihre avpppppqnn kppvpstprp
      301 sassqapppp pppsrpgppp lppsssgnde tprlpqrnls lssstpplps pgrsgplppp
      361 pserppppvr dppgrsgmtr rgvscfqnpa cpnvpiilsv kiv
//
LOCUS       NP_001371285             397 aa            linear   PRI 21-NOV-2025
DEFINITION  double-strand-break repair protein rad21-like protein 1 isoform 3
            [Homo sapiens].
ACCESSION   NP_001371285
VERSION     NP_001371285.1
DBSOURCE    REFSEQ: accession NM_001384356.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Shi,Z., Gao,H., Bai,X.C. and Yu,H.
  TITLE     Cryo-EM structure of the human cohesin-NIPBL-DNA complex
  JOURNAL   Science 368 (6498), 1454-1459 (2020)
   PUBMED   32409525
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Minase,G., Miyamoto,T., Miyagawa,Y., Iijima,M., Ueda,H., Saijo,Y.,
            Namiki,M. and Sengoku,K.
  TITLE     Single-nucleotide polymorphisms in the human RAD21L gene may be a
            genetic risk factor for Japanese patients with azoospermia caused
            by meiotic arrest and Sertoli cell-only syndrome
  JOURNAL   Hum Fertil (Camb) 20 (3), 217-220 (2017)
   PUBMED   28635411
  REMARK    GeneRIF: The association of three single-nucleotide polymorphisms
            with azoospermia, especially Sertoli cell-only syndrome, was
            studied in Japanese men.
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Li,L., Fridley,B.L., Kalari,K., Niu,N., Jenkins,G., Batzler,A.,
            Abo,R.P., Schaid,D. and Wang,L.
  TITLE     Discovery of genetic biomarkers contributing to variation in drug
            response of cytidine analogues using human lymphoblastoid cell
            lines
  JOURNAL   BMC Genomics 15, 93 (2014)
   PUBMED   24483146
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Gutierrez-Caballero,C., Herran,Y., Sanchez-Martin,M., Suja,J.A.,
            Barbero,J.L., Llano,E. and Pendas,A.M.
  TITLE     Identification and molecular characterization of the mammalian
            alpha-kleisin RAD21L
  JOURNAL   Cell Cycle 10 (9), 1477-1487 (2011)
   PUBMED   21527826
  REMARK    GeneRIF: RAD21L is identified as a novel cohesin complex subunit
            homologous to mammalian RAD21/REC8/alpha-kleisin subfamily.
REFERENCE   5  (residues 1 to 397)
  AUTHORS   Baranzini,S.E., Wang,J., Gibson,R.A., Galwey,N., Naegelin,Y.,
            Barkhof,F., Radue,E.W., Lindberg,R.L., Uitdehaag,B.M.,
            Johnson,M.R., Angelakopoulou,A., Hall,L., Richardson,J.C.,
            Prinjha,R.K., Gass,A., Geurts,J.J., Kragt,J., Sombekke,M.,
            Vrenken,H., Qualley,P., Lincoln,R.R., Gomez,R., Caillier,S.J.,
            George,M.F., Mousavi,H., Guerrero,R., Okuda,D.T., Cree,B.A.,
            Green,A.J., Waubant,E., Goodin,D.S., Pelletier,D., Matthews,P.M.,
            Hauser,S.L., Kappos,L., Polman,C.H. and Oksenberg,J.R.
  TITLE     Genome-wide association analysis of susceptibility and clinical
            phenotype in multiple sclerosis
  JOURNAL   Hum Mol Genet 18 (4), 767-778 (2009)
   PUBMED   19010793
REFERENCE   6  (residues 1 to 397)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL031665.19.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.557684.1,
                                           SRR14038194.3960188.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..397
                     /product="double-strand-break repair protein rad21-like
                     protein 1 isoform 3"
                     /note="double-strand-break repair protein rad21-like
                     protein 1; RAD21-like 1"
                     /calculated_mol_wt=45004
     Region          131..211
                     /region_name="Rad21_Rec8_M_NXP1-like"
                     /note="Middle HEAT-repeat binding domain found in Homo
                     sapiens nuclear matrix protein 1 (NXP-1) and similar
                     proteins; cd21792"
                     /db_xref="CDD:439294"
     Site            order(137..139,142..149,152,155..156,158..159,161..168,
                     170..176,178..180,183..184,187..197,199..200,203..204,
                     206..211)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:439294"
     Region          343..394
                     /region_name="Rad21_Rec8"
                     /note="Conserved region of Rad21 / Rec8 like protein;
                     pfam04824"
                     /db_xref="CDD:335912"
     CDS             1..397
                     /gene="RAD21L1"
                     /gene_synonym="dJ545L17.2; RAD21L"
                     /coded_by="NM_001384356.1:187..1380"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:642636"
                     /db_xref="HGNC:HGNC:16271"
                     /db_xref="MIM:619533"
ORIGIN      
        1 mnaidvsehf tqnqsrpeei tlrenfdndl ifqaesfgee seilrrhsff ddnillnssg
       61 pliehssgsl tgerslfyds gdgfgdegaa gemidnllqd dqnilledmh lnreislpse
      121 ppnsladiae krkgkkrrll idpikelssk vihkqltsfa dtlmvlelap ptqrlmmwkk
      181 rggvhtllst aaqdlihael kmlftkcfls sgfklgrkmi qkesvreevg nqnivetsmm
      241 qepnyqqels kpqtwkdvig gsqhsshedt nkninseqdi vemvslaaee sslmndlfaq
      301 eieyspvele slsneeniet erwngrilqm lnrlresnkm gmqsfslmkl crnsdrkqaa
      361 akfysflvlk kqlaielsqs apyadiiatm gpmfyni
//
LOCUS       NP_001289675             127 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor ligand superfamily member 6 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001289675
VERSION     NP_001289675.1
DBSOURCE    REFSEQ: accession NM_001302746.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Schmid,A., Bello,C. and Becker,C.F.W.
  TITLE     Synthesis of N-Glycosylated Soluble Fas Ligand
  JOURNAL   Chemistry 30 (24), e202400120 (2024)
   PUBMED   38363216
  REMARK    GeneRIF: Synthesis of N-Glycosylated Soluble Fas Ligand.
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Lebrault,E., Oblet,C., Kurma,K., Levoin,N., Jeannet,R., Jean,M.,
            Vacher,P. and Legembre,P.
  TITLE     CD95L concatemers highlight different stoichiometries of
            CD95-mediated apoptotic and nonapoptotic pathways
  JOURNAL   Eur J Immunol 54 (1), e2350626 (2024)
   PUBMED   37837385
  REMARK    GeneRIF: CD95L concatemers highlight different stoichiometries of
            CD95-mediated apoptotic and nonapoptotic pathways.
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Choy,J.C.
  TITLE     The complex web of FasL: cell type-specific roles in affecting and
            controlling acute graft-vs-host disease
  JOURNAL   J Leukoc Biol 114 (3), 202-204 (2023)
   PUBMED   37431614
  REMARK    GeneRIF: The complex web of FasL: cell type-specific roles in
            affecting and controlling acute graft-vs-host disease.
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Souza,I.P., Amoras,E.D.S.G., Sousa,F.D.M., Sousa,P.V.N.R.,
            Lima,S.S., Cayres-Vallinoto,I.M.V., Ishak,R., Vallinoto,A.C.R. and
            Queiroz,M.A.F.
  TITLE     Plasma Levels of sFas-sFasL and FASL Gene Expression Are Associated
            with Tuberculosis
  JOURNAL   Biomolecules 13 (1), 80 (2022)
   PUBMED   36671466
  REMARK    GeneRIF: Plasma Levels of sFas-sFasL and FASL Gene Expression Are
            Associated with Tuberculosis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Boldin,M.P., Varfolomeev,E.E., Pancer,Z., Mett,I.L., Camonis,J.H.
            and Wallach,D.
  TITLE     A novel protein that interacts with the death domain of Fas/APO1
            contains a sequence motif related to the death domain
  JOURNAL   J Biol Chem 270 (14), 7795-7798 (1995)
   PUBMED   7536190
REFERENCE   7  (residues 1 to 127)
  AUTHORS   Brunner,T., Mogil,R.J., LaFace,D., Yoo,N.J., Mahboubi,A.,
            Echeverri,F., Martin,S.J., Force,W.R., Lynch,D.H., Ware,C.F. et al.
  TITLE     Cell-autonomous Fas (CD95)/Fas-ligand interaction mediates
            activation-induced apoptosis in T-cell hybridomas
  JOURNAL   Nature 373 (6513), 441-444 (1995)
   PUBMED   7530336
REFERENCE   8  (residues 1 to 127)
  AUTHORS   Alderson,M.R., Tough,T.W., Davis-Smith,T., Braddy,S., Falk,B.,
            Schooley,K.A., Goodwin,R.G., Smith,C.A., Ramsdell,F. and Lynch,D.H.
  TITLE     Fas ligand mediates activation-induced cell death in human T
            lymphocytes
  JOURNAL   J Exp Med 181 (1), 71-77 (1995)
   PUBMED   7528780
REFERENCE   9  (residues 1 to 127)
  AUTHORS   Suda,T., Takahashi,T., Golstein,P. and Nagata,S.
  TITLE     Molecular cloning and expression of the Fas ligand, a novel member
            of the tumor necrosis factor family
  JOURNAL   Cell 75 (6), 1169-1178 (1993)
   PUBMED   7505205
REFERENCE   10 (residues 1 to 127)
  AUTHORS   Bleesing,J.J.H., Nagaraj,C.B. and Zhang,K.
  TITLE     Autoimmune Lymphoproliferative Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301287
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA916336.1, AF288573.1,
            X89102.1 and Z96050.1.
            
            Summary: This gene is a member of the tumor necrosis factor
            superfamily. The primary function of the encoded transmembrane
            protein is the induction of apoptosis triggered by binding to FAS.
            The FAS/FASLG signaling pathway is essential for immune system
            regulation, including activation-induced cell death (AICD) of T
            cells and cytotoxic T lymphocyte induced cell death. It has also
            been implicated in the progression of several cancers. Defects in
            this gene may be related to some cases of systemic lupus
            erythematosus (SLE). Alternatively spliced transcript variants have
            been described. [provided by RefSeq, Nov 2014].
            
            Transcript Variant: This variant (2) lacks an exon in the 5' coding
            region, which results in a frameshift and an early stop codon,
            compared to variant 1. The encoded isoform (2) is shorter and has a
            distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF288573.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.3"
     Protein         1..127
                     /product="tumor necrosis factor ligand superfamily member
                     6 isoform 2"
                     /note="CD95 ligand; apoptosis (APO-1) antigen ligand 1;
                     tumor necrosis factor ligand superfamily member 6; fas
                     antigen ligand; apoptosis antigen ligand; mutant tumor
                     necrosis factor family member 6; Fas ligand (TNF
                     superfamily, member 6); tumor necrosis factor ligand 1A"
                     /calculated_mol_wt=13875
     mat_peptide     1..81
                     /product="FasL intracellular domain. /id=PRO_0000416842"
                     /note="propagated from UniProtKB/Swiss-Prot (P48023.1)"
                     /calculated_mol_wt=8798
     Region          20..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48023.1)"
     Site            81..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48023.1)"
     Site            81..82
                     /site_type="cleavage"
                     /note="Cleavage, by SPPL2A. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P48023.1)"
     CDS             1..127
                     /gene="FASLG"
                     /gene_synonym="ALPS1B; APT1LG1; APTL; CD178; CD95-L;
                     CD95L; FASL; TNFSF6; TNLG1A"
                     /coded_by="NM_001302746.2:100..483"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS76243.1"
                     /db_xref="GeneID:356"
                     /db_xref="HGNC:HGNC:11936"
                     /db_xref="MIM:134638"
ORIGIN      
        1 mqqpfnypyp qiywvdssas spwappgtvl pcptsvprrp gqrrpppppp ppplpppppp
       61 pplpplplpp lkkrgnhstg lcllvmffmv lvalvglglg mfqlfhlqke laelreatpv
      121 hplkkrs
//
LOCUS       NP_001122092             553 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase PAK 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001122092
VERSION     NP_001122092.1
DBSOURCE    REFSEQ: accession NM_001128620.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Kervarrec,T., Westphal,D., Pissaloux,D., Legrand,M., Tirode,F.,
            Neuhart,A., Drouot,F., Becker,J.C., Macagno,N., Seris,A.,
            Jouary,T., Beltzung,F., Jullie,M.L., Harms,P.W., Cribier,B.,
            Mourah,S., Jouenne,F., Fromont,G., Louveau,B., Mancini,M.,
            Kazakov,D.V., de la Fouchardiere,A. and Battistella,M.
  TITLE     Porocarcinomas with PAK1/2/3 fusions: a series of 12 cases
  JOURNAL   Histopathology 85 (4), 566-578 (2024)
   PUBMED   38785043
  REMARK    GeneRIF: Porocarcinomas with PAK1/2/3 fusions: a series of 12
            cases.
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Zhao,P., Zhang,J., Song,W., Qi,D., Huang,Y., Su,Y., Wu,R., Zhang,L.
            and Zhang,S.
  TITLE     Incarvine C and its analogues inhibit the formation of cell
            cytoskeleton by targeting Rac1
  JOURNAL   Bioorg Chem 149, 107512 (2024)
   PUBMED   38833990
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Xu,M.H., Zheng,Y.M., Liang,B.G., Xu,W.X., Cao,J., Wang,P.,
            Dong,Z.Y., Zhou,C.H., Sun,H.C., Ren,N., Ke,A.W. and Shen,Y.H.
  TITLE     Deubiquitination of CIB1 by USP14 promotes lenvatinib resistance
            via the PAK1-ERK1/2 axis in hepatocellular carcinoma
  JOURNAL   Int J Biol Sci 20 (9), 3269-3284 (2024)
   PUBMED   38993552
  REMARK    GeneRIF: Deubiquitination of CIB1 by USP14 promotes lenvatinib
            resistance via the PAK1-ERK1/2 axis in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 553)
  AUTHORS   Luo,Q., Raulston,E.G., Prado,M.A., Wu,X., Gritsman,K., Whalen,K.S.,
            Yan,K., Booth,C.A.G., Xu,R., van Galen,P., Doench,J.G., Shimony,S.,
            Long,H.W., Neuberg,D.S., Paulo,J.A. and Lane,A.A.
  TITLE     Targetable leukaemia dependency on noncanonical PI3Kgamma
            signalling
  JOURNAL   Nature 630 (8015), 198-205 (2024)
   PUBMED   38720074
  REMARK    GeneRIF: Targetable leukaemia dependency on noncanonical PI3Kgamma
            signalling.
REFERENCE   6  (residues 1 to 553)
  AUTHORS   Manser,E., Huang,H.Y., Loo,T.H., Chen,X.Q., Dong,J.M., Leung,T. and
            Lim,L.
  TITLE     Expression of constitutively active alpha-PAK reveals effects of
            the kinase on actin and focal complexes
  JOURNAL   Mol Cell Biol 17 (3), 1129-1143 (1997)
   PUBMED   9032240
REFERENCE   7  (residues 1 to 553)
  AUTHORS   Bokoch,G.M., Wang,Y., Bohl,B.P., Sells,M.A., Quilliam,L.A. and
            Knaus,U.G.
  TITLE     Interaction of the Nck adapter protein with p21-activated kinase
            (PAK1)
  JOURNAL   J Biol Chem 271 (42), 25746-25749 (1996)
   PUBMED   8824201
REFERENCE   8  (residues 1 to 553)
  AUTHORS   Brown,J.L., Stowers,L., Baer,M., Trejo,J., Coughlin,S. and Chant,J.
  TITLE     Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase
            pathway
  JOURNAL   Curr Biol 6 (5), 598-605 (1996)
   PUBMED   8805275
REFERENCE   9  (residues 1 to 553)
  AUTHORS   Martin,G.A., Bollag,G., McCormick,F. and Abo,A.
  TITLE     A novel serine kinase activated by rac1/CDC42Hs-dependent
            autophosphorylation is related to PAK65 and STE20
  JOURNAL   EMBO J 14 (9), 1970-1978 (1995)
   PUBMED   7744004
  REMARK    Erratum:[EMBO J. 1995 Sep 1;14(17):4385. doi:
            10.1002/j.1460-2075.1995.tb00113.x. PMID: 7556080]
REFERENCE   10 (residues 1 to 553)
  AUTHORS   Manser,E., Leung,T., Salihuddin,H., Zhao,Z.S. and Lim,L.
  TITLE     A brain serine/threonine protein kinase activated by Cdc42 and Rac1
  JOURNAL   Nature 367 (6458), 40-46 (1994)
   PUBMED   8107774
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003680.2 and AP000486.6.
            
            Summary: This gene encodes a family member of serine/threonine
            p21-activating kinases, known as PAK proteins. These proteins are
            critical effectors that link RhoGTPases to cytoskeleton
            reorganization and nuclear signaling, and they serve as targets for
            the small GTP binding proteins Cdc42 and Rac. This specific family
            member regulates cell motility and morphology. Mutations in this
            gene have been associated with macrocephaly, seizures, and speech
            delay. Overexpression of this gene is also reported in many cancer
            types, and particularly in breast cancer. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1673051.1,
                                           SRR14038192.2157953.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.5-q14.1"
     Protein         1..553
                     /product="serine/threonine-protein kinase PAK 1 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="p21/Cdc42/Rac1-activated kinase 1 (yeast
                     Ste20-related); p21/Cdc42/Rac1-activated kinase 1 (STE20
                     homolog, yeast); serine/threonine-protein kinase PAK 1;
                     p21 protein (Cdc42/Rac)-activated kinase 1"
                     /calculated_mol_wt=61501
     Region          1..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB and autocatalysis.
                     /evidence=ECO:0000269|PubMed:14585966,
                     ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          70..140
                     /region_name="Autoregulatory region.
                     /evidence=ECO:0000269|PubMed:22153498"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Region          74..132
                     /region_name="PBD"
                     /note="P21-Rho-binding domain; pfam00786"
                     /db_xref="CDD:395634"
     Site            order(75,78,81,83,86,103,107)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238526"
     Region          75..105
                     /region_name="GTPase-binding.
                     /evidence=ECO:0000269|PubMed:22153498"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by OXSR1.
                     /evidence=ECO:0000250|UniProtKB:P35465; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20417602,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000269|PubMed:17726028,
                     ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          159..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17989089,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20417602; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000269|PubMed:17726028; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          211..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17989089,
                     ECO:0000269|PubMed:23260667, ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88643; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88643; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          262..517
                     /region_name="STKc_PAK_I"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Group I p21-activated kinase; cd06647"
                     /db_xref="CDD:270814"
     Site            order(276..280,284,297,299,328,344..348,350..351,354,389,
                     391..394,396,406..407,410,423..427,429,456,465..467)
                     /site_type="active"
                     /db_xref="CDD:270814"
     Site            order(276..280,284,297,299,328,344..348,350..351,354,
                     393..394,396,406..407)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270814"
     Site            order(279..280,389,391..393,410,423..427,429,456,465..467)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270814"
     Site            order(281,315,384,386..389,407..408,435..436,438,443,468,
                     471,474)
                     /site_type="other"
                     /note="AID interaction site [polypeptide binding]"
                     /db_xref="CDD:270814"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000269|PubMed:17726028,
                     ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            406..429
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270814"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis, BRSK2 and
                     PDPK1. /evidence=ECO:0000269|PubMed:10551809,
                     ECO:0000269|PubMed:10995762, ECO:0000269|PubMed:22153498,
                     ECO:0000269|PubMed:22669945; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     CDS             1..553
                     /gene="PAK1"
                     /gene_synonym="alpha-PAK; IDDMSSD; p65-PAK; PAKalpha"
                     /coded_by="NM_001128620.2:565..2226"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44687.1"
                     /db_xref="GeneID:5058"
                     /db_xref="HGNC:HGNC:8590"
                     /db_xref="MIM:602590"
ORIGIN      
        1 msnngldiqd kppappmrnt stmigagskd agtlnhgskp lppnpeekkk kdrfyrsilp
       61 gdktnkkkek erpeislpsd fehtihvgfd avtgeftgmp eqwarllqts nitkseqkkn
      121 pqavldvlef ynskktsnsq kymsftdksa edynssnaln vkavsetpav ppvsededdd
      181 dddatpppvi aprpehtksv ytrsvieplp vtptrdvats pisptenntt ppdaltrnte
      241 kqkkkpkmsd eeileklrsi vsvgdpkkky trfekigqga sgtvytamdv atgqevaikq
      301 mnlqqqpkke liineilvmr enknpnivny ldsylvgdel wvvmeylagg sltdvvtetc
      361 mdegqiaavc reclqalefl hsnqvihrdi ksdnillgmd gsvkltdfgf caqitpeqsk
      421 rstmvgtpyw mapevvtrka ygpkvdiwsl gimaiemieg eppylnenpl ralyliatng
      481 tpelqnpekl saifrdflnr clemdvekrg sakellqvrk lrfqvfsnfs miaasipedc
      541 qaplqphstd ccs
//
LOCUS       NP_001349878             756 aa            linear   PRI 21-NOV-2025
DEFINITION  xylosyl- and glucuronyltransferase LARGE1 isoform 1 [Homo sapiens].
ACCESSION   NP_001349878 XP_011528812
VERSION     NP_001349878.1
DBSOURCE    REFSEQ: accession NM_001362949.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Botti-Lodovico,Y., Nair,P., Nosamiefan,D., Stremlau,M.,
            Schaffner,S., Agignoae,S.V., Aiyepada,J.O., Ajogbasile,F.V.,
            Akpede,G.O., Alhasan,F., Andersen,K.G., Asogun,D.A., Ayodeji,O.O.,
            Badiane,A.S., Barnes,K., Bauer,M.R., Bell-Kareem,A., Benard,M.E.,
            Benevolence,E.O., Blessing,O., Boehm,C.K., Boisen,M.L., Bond,N.G.,
            Branco,L.M., Butts,M.J., Carter,A., Colubri,A., Deme,A.B.,
            DeRuff,K.C., Diedhiou,Y., Edamhande,A.P., Elhamoumi,S., Engel,E.J.,
            Eromon,P., Fallah,M., Folarin,O.A., Fry,B., Garry,R., Gaye,A.,
            Gbakie,M., Gevao,S.M., Gionet,G., Gladden-Young,A., Goba,A.,
            Gomis,J.F., Happi,A.N., Houghton,M., Ihekwuazu,C., Iruolagbe,C.O.,
            Jackson,J., Jalloh,S., Johnson,J., Kanneh,L., Kayode,A.,
            Kemball,M., Kingsley,O.C., Koroma,V., Kotliar,D., Mehta,S.,
            Metsky,H.C., Michael,A., Mirhashemi,M.E., Modjarrad,K., Momoh,M.,
            Myhrvold,C.A., Naregose,O.G., Ndiaye,T., Ndiaye,M., Ndiaye,A.,
            Normandin,E., Odia,I., Oguzie,J.U., Okogbenin,S.A., Okokhere,P.O.,
            Okolie,J., Olawoye,I.B., Olumade,T.J., Oluniyi,P.E., Omoregie,O.,
            Park,D.J., Paye,M.F., Petros,B., Philippakis,A.A., Priscilla,A.,
            Ricks,A., Rimoin,A., Sandi,J.D., Schieffelin,J.S., Schreiber,M.,
            Seck,M.C., Siddiqui,S., Siddle,K., Smither,A.R., Sy,M., Sy,N.,
            Tomkins-Tinch,C.H., Tomori,O., Ugwu,C., Uwanibe,J.N., Uyigue,E.A.,
            Victoria,D.I., Vinze,A., Vodzak,M.E., Welch,N., Wurie,H.I.,
            Zoumarou,D., Grant,D.S., Ndiaye,D., MacInnis,B., Sabeti,P.C. and
            Happi,C.
  TITLE     The Origins and Future of Sentinel: An Early-Warning System for
            Pandemic Preemption and Response
  JOURNAL   Viruses 13 (8), 1605 (2021)
   PUBMED   34452470
  REMARK    GeneRIF: The Origins and Future of Sentinel: An Early-Warning
            System for Pandemic Preemption and Response.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Wang,M., Tao,H. and Huang,P.
  TITLE     Clinical significance of LARGE1 in progression of liver cancer and
            the underlying mechanism
  JOURNAL   Gene 779, 145493 (2021)
   PUBMED   33588034
  REMARK    GeneRIF: Clinical significance of LARGE1 in progression of liver
            cancer and the underlying mechanism.
REFERENCE   3  (residues 1 to 756)
  AUTHORS   Walimbe,A.S., Okuma,H., Joseph,S., Yang,T., Yonekawa,T., Hord,J.M.,
            Venzke,D., Anderson,M.E., Torelli,S., Manzur,A., Devereaux,M.,
            Cuellar,M., Prouty,S., Ocampo Landa,S., Yu,L., Xiao,J., Dixon,J.E.,
            Muntoni,F. and Campbell,K.P.
  TITLE     POMK regulates dystroglycan function via LARGE1-mediated elongation
            of matriglycan
  JOURNAL   Elife 9, e61388 (2020)
   PUBMED   32975514
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 756)
  AUTHORS   Beltran,D., Anderson,M.E., Bharathy,N., Settelmeyer,T.P.,
            Svalina,M.N., Bajwa,Z., Shern,J.F., Gultekin,S.H., Cuellar,M.A.,
            Yonekawa,T., Keller,C. and Campbell,K.P.
  TITLE     Exogenous expression of the glycosyltransferase LARGE1 restores
            alpha-dystroglycan matriglycan and laminin binding in
            rhabdomyosarcoma
  JOURNAL   Skelet Muscle 9 (1), 11 (2019)
   PUBMED   31054580
  REMARK    GeneRIF: findings demonstrate that a lack of matriglycan on
            alpha-dystroglycan is a common feature in rhabdomyosarcoma due to
            the downregulation of LARGE1, and that ectopic expression of LARGE1
            can restore matriglycan modifications and the ability of
            alpha-dystroglycan to function as an extracellular matrix receptor
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 756)
  AUTHORS   Gao,G., Johnson,S.H., Vasmatzis,G., Pauley,C.E., Tombers,N.M.,
            Kasperbauer,J.L. and Smith,D.I.
  TITLE     Common fragile sites (CFS) and extremely large CFS genes are
            targets for human papillomavirus integrations and chromosome
            rearrangements in oropharyngeal squamous cell carcinoma
  JOURNAL   Genes Chromosomes Cancer 56 (1), 59-74 (2017)
   PUBMED   27636103
  REMARK    GeneRIF: Large1 gene is a target for human papillomavirus
            integrations and chromosome rearrangements in oropharyngeal
            squamous cell carcinoma.
REFERENCE   6  (residues 1 to 756)
  AUTHORS   Michele,D.E., Barresi,R., Kanagawa,M., Saito,F., Cohn,R.D.,
            Satz,J.S., Dollar,J., Nishino,I., Kelley,R.I., Somer,H., Straub,V.,
            Mathews,K.D., Moore,S.A. and Campbell,K.P.
  TITLE     Post-translational disruption of dystroglycan-ligand interactions
            in congenital muscular dystrophies
  JOURNAL   Nature 418 (6896), 417-422 (2002)
   PUBMED   12140558
REFERENCE   7  (residues 1 to 756)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   8  (residues 1 to 756)
  AUTHORS   Peyrard,M., Seroussi,E., Sandberg-Nordqvist,A.C., Xie,Y.G.,
            Han,F.Y., Fransson,I., Collins,J., Dunham,I., Kost-Alimova,M.,
            Imreh,S. and Dumanski,J.P.
  TITLE     The human LARGE gene from 22q12.3-q13.1 is a new, distinct member
            of the glycosyltransferase gene family
  JOURNAL   Proc Natl Acad Sci U S A 96 (2), 598-603 (1999)
   PUBMED   9892679
REFERENCE   9  (residues 1 to 756)
  AUTHORS   Montanaro,F., Gee,S.H., Jacobson,C., Lindenbaum,M.H., Froehner,S.C.
            and Carbonetto,S.
  TITLE     Laminin and alpha-dystroglycan mediate acetylcholine receptor
            aggregation via a MuSK-independent pathway
  JOURNAL   J Neurosci 18 (4), 1250-1260 (1998)
   PUBMED   9454835
REFERENCE   10 (residues 1 to 756)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z73429.1, Z69715.2, AL096754.1,
            Z68287.1, Z69042.1, Z70288.1, Z69943.3, AL008715.1, Z82173.2 and
            AL008630.1.
            
            On May 3, 2018 this sequence version replaced XP_011528812.1.
            
            Summary: This gene encodes a member of the
            N-acetylglucosaminyltransferase gene family. It encodes a
            glycosyltransferase which participates in glycosylation of
            alpha-dystroglycan, and may carry out the synthesis of glycoprotein
            and glycosphingolipid sugar chains. It may also be involved in the
            addition of a repeated disaccharide unit. The protein encoded by
            this gene is the glycotransferase that adds the final xylose and
            glucuronic acid to alpha-dystroglycan and thereby allows
            alpha-dystroglycan to bind ligands including laminin 211 and
            neurexin. Mutations in this gene cause several forms of congenital
            muscular dystrophy characterized by cognitive disability and
            abnormal glycosylation of alpha-dystroglycan. Alternative splicing
            of this gene results in multiple transcript variants that encode
            the same protein. [provided by RefSeq, May 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.162764.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..756
                     /product="xylosyl- and glucuronyltransferase LARGE1
                     isoform 1"
                     /note="acetylglucosaminyltransferase-like protein;
                     glycosyltransferase-like protein LARGE1;
                     acetylglucosaminyltransferase-like 1A; xylosyl- and
                     glucuronyltransferase LARGE1"
                     /calculated_mol_wt=87935
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95461.1)"
     Region          43..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95461.1)"
     Region          81..109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95461.1)"
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95461.1)"
     Site            122
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95461.1)"
     Region          138..417
                     /region_name="GT8_LARGE_C"
                     /note="LARGE catalytic domain has closest homology to GT8
                     glycosyltransferase involved in lipooligosaccharide
                     synthesis; cd06431"
                     /db_xref="CDD:133053"
     Region          138..413
                     /region_name="Xylosyltransferase activity.
                     /evidence=ECO:0000305|PubMed:22223806"
                     /note="propagated from UniProtKB/Swiss-Prot (O95461.1)"
     Site            order(143..145,148..149,224,240,242..244,272,296..298,
                     334..335,360..361,380,382..383,386)
                     /site_type="active"
                     /note="putative ligand binding site [active]"
                     /db_xref="CDD:133053"
     Site            148
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95461.1)"
     Site            order(242,244,380)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:133053"
     Site            272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95461.1)"
     Region          414..756
                     /region_name="Glucuronyltransferase activity.
                     /evidence=ECO:0000305|PubMed:22223806"
                     /note="propagated from UniProtKB/Swiss-Prot (O95461.1)"
     Region          473..743
                     /region_name="Glyco_transf_49"
                     /note="Glycosyl-transferase for dystroglycan; pfam13896"
                     /db_xref="CDD:464027"
     CDS             1..756
                     /gene="LARGE1"
                     /gene_synonym="LARGE; MDC1D; MDDGA6; MDDGB6"
                     /coded_by="NM_001362949.2:350..2620"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS13912.1"
                     /db_xref="GeneID:9215"
                     /db_xref="HGNC:HGNC:6511"
                     /db_xref="MIM:603590"
ORIGIN      
        1 mlgicrgrrk flaaslsllc ipaitwiylf sgsfedgkpv slsplesqah sprytassqr
       61 ereslevrmr eveeenralr rqlslaqgra pshrrgnhsk tysmeegtgd senlragiva
      121 gnssecgqqp vvekcetihv aivcagynas rdvvtlvksv lfhrrnplhf hliadsiaeq
      181 ilatlfqtwm vpavrvdfyn adelksevsw ipnkhysgiy glmklvltkt lpanlerviv
      241 ldtditfatd iaelwavfhk fkgqqvlglv enqsdwylgn lwknhrpwpa lgrgyntgvi
      301 lllldklrkm kweqmwrlta erelmgmlst sladqdifna vikqnpflvy qlpcfwnvql
      361 sdhtrseqcy rdvsdlkvih wnspkklrvk nkhveffrnl yltfleydgn llrrelfgcp
      421 seadvnsenl qkqlselded dlcyefrrer ftvhrthlyf lhyeyepaad stdvtlvaql
      481 smdrlqmlea ickhwegpis lalylsdaea qqflryaqgs evlmsrhnvg yhivykegqf
      541 ypvnllrnva mkhistpymf lsdidflpmy glyeylrksv iqldlantkk amivpafetl
      601 ryrlsfpksk aellsmldmg tlftfryhvw tkghaptnfa kwrtattpyr veweadfepy
      661 vvvrrdcpey drrfvgfgwn kvahimeldv qeyefivlpn aymihmphap sfditkfrsn
      721 kqyriclktl keefqqdmsr rygfaalkyl taenns
//
LOCUS       NP_001385423             632 aa            linear   PRI 21-NOV-2025
DEFINITION  nuclear cap-binding protein subunit 3 isoform 2 [Homo sapiens].
ACCESSION   NP_001385423 XP_005256774
VERSION     NP_001385423.1
DBSOURCE    REFSEQ: accession NM_001398494.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 632)
  AUTHORS   Dou,Y., Barbosa,I., Jiang,H., Iasillo,C., Molloy,K.R.,
            Schulze,W.M., Cusack,S., Schmid,M., Le Hir,H., LaCava,J. and
            Jensen,T.H.
  TITLE     NCBP3 positively impacts mRNA biogenesis
  JOURNAL   Nucleic Acids Res 48 (18), 10413-10427 (2020)
   PUBMED   32960271
  REMARK    GeneRIF: NCBP3 positively impacts mRNA biogenesis.
REFERENCE   5  (residues 1 to 632)
  AUTHORS   Dou,Y., Kalmykova,S., Pashkova,M., Oghbaie,M., Jiang,H.,
            Molloy,K.R., Chait,B.T., Rout,M.P., Fenyo,D., Jensen,T.H.,
            Altukhov,I. and LaCava,J.
  TITLE     Affinity proteomic dissection of the human nuclear cap-binding
            complex interactome
  JOURNAL   Nucleic Acids Res 48 (18), 10456-10469 (2020)
   PUBMED   32960270
  REMARK    GeneRIF: Affinity proteomic dissection of the human nuclear
            cap-binding complex interactome.
REFERENCE   6  (residues 1 to 632)
  AUTHORS   Gebhardt,A., Habjan,M., Benda,C., Meiler,A., Haas,D.A., Hein,M.Y.,
            Mann,A., Mann,M., Habermann,B. and Pichlmair,A.
  TITLE     mRNA export through an additional cap-binding complex consisting of
            NCBP1 and NCBP3
  JOURNAL   Nat Commun 6, 8192 (2015)
   PUBMED   26382858
  REMARK    GeneRIF: NCBP3 binds mRNA, associates with components of the mRNA
            processing machinery and contributes to poly(A) RNA export. Study
            proposes the existence of an alternative cap-binding complex
            involving NCBP1 and NCBP3 that plays a key role in mRNA biogenesis.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 632)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 632)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 632)
  AUTHORS   Hegele,A., Kamburov,A., Grossmann,A., Sourlis,C., Wowro,S.,
            Weimann,M., Will,C.L., Pena,V., Luhrmann,R. and Stelzl,U.
  TITLE     Dynamic protein-protein interaction wiring of the human spliceosome
  JOURNAL   Mol Cell 45 (4), 567-580 (2012)
   PUBMED   22365833
REFERENCE   10 (residues 1 to 632)
  AUTHORS   Robinson,P.W., Green,S.J., Carter,C., Coadwell,J. and Kilshaw,P.J.
  TITLE     Studies on transcriptional regulation of the mucosal T-cell
            integrin alphaEbeta7 (CD103)
  JOURNAL   Immunology 103 (2), 146-154 (2001)
   PUBMED   11412301
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005940.3, AC116914.5, KC877636.1 and KC877633.1.
            
            On Dec 17, 2021 this sequence version replaced XP_005256774.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2715813.1,
                                           SRR14038191.1700110.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..632
                     /product="nuclear cap-binding protein subunit 3 isoform 2"
                     /note="CTD-3195I5.1; CTD-3195I5.5; nuclear cap-binding
                     protein subunit 3"
                     /calculated_mol_wt=71928
     Region          15..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53F19.2)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53F19.2)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53F19.2)"
     Region          123..175
                     /region_name="NCBP3"
                     /note="Nuclear cap-binding protein subunit 3; pfam10309"
                     /db_xref="CDD:463048"
     Region          126..187
                     /region_name="RNA recognition motif (RRM) domain.
                     /evidence=ECO:0000303|PubMed:26382858"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53F19.2)"
     Region          155..158
                     /region_name="WLDD motif, essential for
                     7-methylguanosine-containing mRNA cap binding.
                     /evidence=ECO:0000269|PubMed:26382858"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53F19.2)"
     Region          185..233
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53F19.2)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q53F19.2)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q53F19.2)"
     Region          332..419
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53F19.2)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q53F19.2)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53F19.2)"
     CDS             1..632
                     /gene="NCBP3"
                     /gene_synonym="C17orf85; ELG; HSA277841"
                     /coded_by="NM_001398494.1:24..1922"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:55421"
                     /db_xref="HGNC:HGNC:24612"
                     /db_xref="MIM:616624"
ORIGIN      
        1 maavrglrvs vkaeapagpa lglpspeaes gvdrgepepm eveegeleiv pvrrslkeli
       61 pdtsrryenk agsfitgidv tskeaiekke qrakrfhfrs evnlaqrnva ldrdmmkkai
      121 pkvrletiyi cgvdemstqd vfsyfkeypp ahiewlddts cnvvwldemt atralinmss
      181 lpaqdkirsr dasedksaek rkkdkqedss dddeaeegev edenssdvel dtlsqveees
      241 llrndlrpan klakgnrlfm rfatkddkke lgaarrsqyy mkygnpnygg mkgilsnswk
      301 rryhsrriqr dvikkralig ddvgltsykh rhsglvnvpe epieeeeeee eeeeeeeeed
      361 qdmdaddrvv veyheelpal kqprersasr rssasssdsd emdydlelkm istpspkksm
      421 kmtmyadeve sqlknirnsm radsvsssni knrignklpp ekfadvrhll dekrqhsrpr
      481 ppvsstksdi rqrlgkrphs pekafssnpv vrrepssdvh srlgvprqds kglyadtrek
      541 ksgnlwtrlg sapktkeknt kkvdhrapga eeddselqra wgalikekeq srqkksrcyq
      601 hpfpkksqfp gaywtsfege eegsgqltlp gp
//
LOCUS       NP_001073341             895 aa            linear   PRI 21-NOV-2025
DEFINITION  cullin-4B isoform 2 [Homo sapiens].
ACCESSION   NP_001073341
VERSION     NP_001073341.1
DBSOURCE    REFSEQ: accession NM_001079872.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 895)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 895)
  AUTHORS   Wang,X., Xue,Q., Duan,Q., Sun,Z., Wu,Y., Yang,S., Xu,P., Cao,H.,
            Liao,F., Wang,X. and Miao,C.
  TITLE     Circ_0011058 alleviates RA pathology through the
            circ_0011058/miR-335-5p/CUL4B signal axis
  JOURNAL   Autoimmunity 57 (1), 2299587 (2024)
   PUBMED   38254314
  REMARK    GeneRIF: Circ_0011058 alleviates RA pathology through the
            circ_0011058/miR-335-5p/CUL4B signal axis.
REFERENCE   3  (residues 1 to 895)
  AUTHORS   Karaosmanoglu,C., Yildiz,S.H., Akdogan,M. and Erdogan,M.O.
  TITLE     Association of CUL4B with the pathogenesis of age-related cataract
  JOURNAL   Int Ophthalmol 44 (1), 288 (2024)
   PUBMED   38937308
  REMARK    GeneRIF: Association of CUL4B with the pathogenesis of age-related
            cataract.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 895)
  AUTHORS   Wu,R., Li,X., Meng,Z., Li,P., He,Z. and Liang,L.
  TITLE     Phenotypic and genetic analysis of children with unexplained
            neurodevelopmental delay and neurodevelopmental comorbidities in a
            Chinese cohort using trio-based whole-exome sequencing
  JOURNAL   Orphanet J Rare Dis 19 (1), 205 (2024)
   PUBMED   38764027
  REMARK    GeneRIF: Phenotypic and genetic analysis of children with
            unexplained neurodevelopmental delay and neurodevelopmental
            comorbidities in a Chinese cohort using trio-based whole-exome
            sequencing.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 895)
  AUTHORS   Ma,Y., Liu,X., Zhou,M., Sun,W., Jiang,B., Liu,Q., Wang,M., Zou,Y.,
            Liu,Q., Gong,Y. and Sun,G.
  TITLE     CUL4B mutations impair human cortical neurogenesis through
            PP2A-dependent inhibition of AKT and ERK
  JOURNAL   Cell Death Dis 15 (2), 121 (2024)
   PUBMED   38331954
  REMARK    GeneRIF: CUL4B mutations impair human cortical neurogenesis through
            PP2A-dependent inhibition of AKT and ERK.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 895)
  AUTHORS   Jones,E.A., Clement-Jones,M. and Wilson,D.I.
  TITLE     JAGGED1 expression in human embryos: correlation with the Alagille
            syndrome phenotype
  JOURNAL   J Med Genet 37 (9), 658-662 (2000)
   PUBMED   10978356
REFERENCE   7  (residues 1 to 895)
  AUTHORS   Hori,T., Osaka,F., Chiba,T., Miyamoto,C., Okabayashi,K.,
            Shimbara,N., Kato,S. and Tanaka,K.
  TITLE     Covalent modification of all members of human cullin family
            proteins by NEDD8
  JOURNAL   Oncogene 18 (48), 6829-6834 (1999)
   PUBMED   10597293
REFERENCE   8  (residues 1 to 895)
  AUTHORS   Wada,H., Yeh,E.T. and Kamitani,T.
  TITLE     Identification of NEDD8-conjugation site in human cullin-2
  JOURNAL   Biochem Biophys Res Commun 257 (1), 100-105 (1999)
   PUBMED   10092517
REFERENCE   9  (residues 1 to 895)
  AUTHORS   Ohta,T., Michel,J.J., Schottelius,A.J. and Xiong,Y.
  TITLE     ROC1, a homolog of APC11, represents a family of cullin partners
            with an associated ubiquitin ligase activity
  JOURNAL   Mol Cell 3 (4), 535-541 (1999)
   PUBMED   10230407
REFERENCE   10 (residues 1 to 895)
  AUTHORS   Kipreos,E.T., Lander,L.E., Wing,J.P., He,W.W. and Hedgecock,E.M.
  TITLE     cul-1 is required for cell cycle exit in C. elegans and identifies
            a novel gene family
  JOURNAL   Cell 85 (6), 829-839 (1996)
   PUBMED   8681378
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX647096.1, BX537787.1,
            AY365125.1, AC002476.1 and CV573599.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the cullin family. The encoded
            protein forms a complex that functions as an E3 ubiquitin ligase
            and catalyzes the polyubiquitination of specific protein substrates
            in the cell. The protein interacts with a ring finger protein, and
            is required for the proteolysis of several regulators of DNA
            replication including chromatin licensing and DNA replication
            factor 1 and cyclin E. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) contains a distinct 5' UTR and
            lacks an in-frame portion of the 5' coding region, compared to
            variant 1. The resulting isoform (2) has a shorter and unique
            N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647096.1, CR936722.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371322.11/ ENSP00000360373.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq24"
     Protein         1..895
                     /product="cullin-4B isoform 2"
                     /calculated_mol_wt=102168
     Region          199..796
                     /region_name="Cullin"
                     /note="Cullin family; pfam00888"
                     /db_xref="CDD:459983"
     Region          824..889
                     /region_name="Cullin_Nedd8"
                     /note="Cullin protein neddylation domain; smart00884"
                     /db_xref="CDD:214883"
     CDS             1..895
                     /gene="CUL4B"
                     /gene_synonym="CUL-4B; MRXHF2; MRXS15; MRXSC; SFM2"
                     /coded_by="NM_001079872.2:325..3012"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43987.1"
                     /db_xref="GeneID:8450"
                     /db_xref="HGNC:HGNC:2555"
                     /db_xref="MIM:300304"
ORIGIN      
        1 mfptgfssps psaaaaaqev rsatdgntst tpptsakkrk lnsssssssn ssneredfds
       61 tssssstppl qprdsaspst ssfclgvsva asshvpiqkk lrfedtlefv gfdakmaees
      121 sssssssspt aatsqqqqlk nksilissva svhhanglak ssttvssfan skpgsakklv
      181 iknfkdkpkl penytdetwq klkeaveaiq nstsikynle elyqavenlc sykisanlyk
      241 qlrqicedhi kaqihqfred sldsvlflkk idrcwqnhcr qmimirsifl fldrtyvlqn
      301 smlpsiwdmg lelfrahiis dqkvqnktid gilllierer ngeaidrsll rsllsmlsdl
      361 qiyqdsfeqr fleetnrlya aegqklmqer evpeylhhvn krleeeadrl ityldqttqk
      421 sliatvekql lgehltailq kglnnllden riqdlsllyq lfsrvrggvq vllqqwieyi
      481 kafgstivin pekdktmvqe lldfkdkvdh iidicflkne kfinamkeaf etfinkrpnk
      541 paeliakyvd sklragnkea tdeelekmld kimiifrfiy gkdvfeafyk kdlakrllvg
      601 ksasvdaeks mlsklkhecg aaftsklegm fkdmelskdi miqfkqymqn qnvpgnielt
      661 vniltmgywp tyvpmevhlp pemvklqeif ktfylgkhsg rklqwqstlg hcvlkaefke
      721 gkkelqvslf qtlvllmfne geefsleeik qatgiedgel rrtlqslacg karvlaknpk
      781 gkdiedgdkf icnddfkhkl frikinqiqm ketveeqast tervfqdrqy qidaaivrim
      841 kmrktlshnl lvsevynqlk fpvkpadlkk rieslidrdy merdkenpnq ynyia
//
LOCUS       NP_001275717             389 aa            linear   PRI 21-NOV-2025
DEFINITION  TOM1-like protein 2 isoform 6 [Homo sapiens].
ACCESSION   NP_001275717 XP_005256524
VERSION     NP_001275717.1
DBSOURCE    REFSEQ: accession NM_001288788.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Shinde,S.R., Mick,D.U., Aoki,E., Rodrigues,R.B., Gygi,S.P. and
            Nachury,M.V.
  TITLE     The ancestral ESCRT protein TOM1L2 selects ubiquitinated cargoes
            for retrieval from cilia
  JOURNAL   Dev Cell 58 (8), 677-693 (2023)
   PUBMED   37019113
  REMARK    GeneRIF: The ancestral ESCRT protein TOM1L2 selects ubiquitinated
            cargoes for retrieval from cilia.
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 389)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 389)
  AUTHORS   Zhang,Y., Wolf-Yadlin,A., Ross,P.L., Pappin,D.J., Rush,J.,
            Lauffenburger,D.A. and White,F.M.
  TITLE     Time-resolved mass spectrometry of tyrosine phosphorylation sites
            in the epidermal growth factor receptor signaling network reveals
            dynamic modules
  JOURNAL   Mol Cell Proteomics 4 (9), 1240-1250 (2005)
   PUBMED   15951569
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   8  (residues 1 to 389)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   9  (residues 1 to 389)
  AUTHORS   Bi,W., Yan,J., Stankiewicz,P., Park,S.S., Walz,K., Boerkoel,C.F.,
            Potocki,L., Shaffer,L.G., Devriendt,K., Nowaczyk,M.J., Inoue,K. and
            Lupski,J.R.
  TITLE     Genes in a refined Smith-Magenis syndrome critical deletion
            interval on chromosome 17p11.2 and the syntenic region of the mouse
  JOURNAL   Genome Res 12 (5), 713-728 (2002)
   PUBMED   11997338
REFERENCE   10 (residues 1 to 389)
  AUTHORS   Seranski,P., Heiss,N.S., Dhorne-Pollet,S., Radelof,U., Korn,B.,
            Hennig,S., Backes,E., Schmidt,S., Wiemann,S., Schwarz,C.E.,
            Lehrach,H. and Poustka,A.
  TITLE     Transcription mapping in a medulloblastoma breakpoint interval and
            Smith-Magenis syndrome candidate region: identification of 53
            transcriptional units and new candidate genes
  JOURNAL   Genomics 56 (1), 1-11 (1999)
   PUBMED   10036180
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA235267.1, AK295111.1,
            AK301944.1, AC122129.9 and BM976586.1.
            
            On Jan 4, 2014 this sequence version replaced XP_005256524.1.
            
            Summary: This gene belongs to a small gene family whose members
            have an N-terminal VHS domain followed by a GAT domain; domains
            which typically participate in vesicular trafficking. The canonical
            protein encoded by this gene also has a C-terminal clathrin binding
            motif. This protein has been shown to interact with Tollip,
            clathrin and ubiquitin and is thought to play a role in endosomal
            sorting. This gene resides in the 3.7 Mb deletion of chromosome
            region 17p11.2 that is associated with Smith-Magenis syndrome.
            Alternative splicing results in multiple transcript variants
            encoding distinct proteins. [provided by RefSeq, Apr 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.4547996.1, AK295111.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..389
                     /product="TOM1-like protein 2 isoform 6"
                     /note="TOM1-like protein 2; target of myb1-like 2; target
                     of Myb-like protein 2"
                     /calculated_mol_wt=42747
     Region          12..122
                     /region_name="VHS_ENTH_ANTH"
                     /note="VHS, ENTH and ANTH domain superfamily; cl02544"
                     /db_xref="CDD:470608"
     Region          122..211
                     /region_name="GAT_SF"
                     /note="GAT domain found in eukaryotic GGAs, metazoan
                     Tom1-like proteins, metazoan STAMs, fungal Vps27, and
                     similar proteins; cl03906"
                     /db_xref="CDD:470905"
     CDS             1..389
                     /gene="TOM1L2"
                     /coded_by="NM_001288788.2:88..1257"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS74001.1"
                     /db_xref="GeneID:146691"
                     /db_xref="HGNC:HGNC:11984"
                     /db_xref="MIM:615519"
ORIGIN      
        1 mefllgnpfs tpvgqcleka tdgslqsedw tlnmeicdii neteegpkda iralkkrlng
       61 nrnyrevmla ltvletcvkn cghrfhilva nrdfidsvlv kiispknnpp tivqdkvlal
      121 iqiarlrsel dvvrgntkvm semltemvpg qedssdlell qelnrtcram qqrivelisr
      181 vsneevteel lhvnddlnnv flryerfery rsgrsvqnas ngvlnevted nlidlgpgsp
      241 avvspmvgnt appsslssql agldlgtesv sgtlsslqqc nprdgfdmfa qtrgnslaeq
      301 rktvtyedpq avgglasald nrkqssegkg ddleegvtse efdkfleera kaaemvpdlp
      361 sppmeapapa snpsgrkkpe rsedalfal
//
LOCUS       NP_004004               1225 aa            linear   PRI 21-NOV-2025
DEFINITION  dystrophin isoform Dp140 [Homo sapiens].
ACCESSION   NP_004004
VERSION     NP_004004.2
DBSOURCE    REFSEQ: accession NM_004013.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1225)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1225)
  AUTHORS   Chen,L., Luo,X., Wang,H., Tian,Y. and Liu,Y.
  TITLE     Identifying inversions with breakpoints in the Dystrophin gene
            through long-read sequencing: report of two cases
  JOURNAL   BMC Med Genomics 17 (1), 227 (2024)
   PUBMED   39251998
  REMARK    GeneRIF: Identifying inversions with breakpoints in the Dystrophin
            gene through long-read sequencing: report of two cases.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1225)
  AUTHORS   Davies,K.E. and Vogt,J.
  TITLE     Long-term clinical follow-up of a family with Becker muscular
            dystrophy associated with a large deletion in the DMD gene
  JOURNAL   Neuromuscul Disord 39, 5-9 (2024)
   PUBMED   38653179
  REMARK    GeneRIF: Long-term clinical follow-up of a family with Becker
            muscular dystrophy associated with a large deletion in the DMD
            gene.
            Erratum:[Neuromuscul Disord. 2024 Jun;39:54. doi:
            10.1016/j.nmd.2024.05.010. PMID: 38801812]
REFERENCE   4  (residues 1 to 1225)
  AUTHORS   Achermann,J.C. and Vilain,E.J.
  TITLE     NR0B1-Related Adrenal Hypoplasia Congenita
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301604
REFERENCE   5  (residues 1 to 1225)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   6  (residues 1 to 1225)
  AUTHORS   Darras,B.T., Urion,D.K. and Ghosh,P.S.
  TITLE     Dystrophinopathies
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301298
REFERENCE   7  (residues 1 to 1225)
  AUTHORS   Nigro,V., Politano,L., Nigro,G., Romano,S.C., Molinari,A.M. and
            Puca,G.A.
  TITLE     Detection of a nonsense mutation in the dystrophin gene by multiple
            SSCP
  JOURNAL   Hum Mol Genet 1 (7), 517-520 (1992)
   PUBMED   1307253
REFERENCE   8  (residues 1 to 1225)
  AUTHORS   Gorecki,D.C., Monaco,A.P., Derry,J.M., Walker,A.P., Barnard,E.A.
            and Barnard,P.J.
  TITLE     Expression of four alternative dystrophin transcripts in brain
            regions regulated by different promoters
  JOURNAL   Hum Mol Genet 1 (7), 505-510 (1992)
   PUBMED   1307251
REFERENCE   9  (residues 1 to 1225)
  AUTHORS   Lederfein,D., Levy,Z., Augier,N., Mornet,D., Morris,G., Fuchs,O.,
            Yaffe,D. and Nudel,U.
  TITLE     A 71-kilodalton protein is a major product of the Duchenne muscular
            dystrophy gene in brain and other nonmuscle tissues
  JOURNAL   Proc Natl Acad Sci U S A 89 (12), 5346-5350 (1992)
   PUBMED   1319059
REFERENCE   10 (residues 1 to 1225)
  AUTHORS   Koenig,M., Monaco,A.P. and Kunkel,L.M.
  TITLE     The complete sequence of dystrophin predicts a rod-shaped
            cytoskeletal protein
  JOURNAL   Cell 53 (2), 219-228 (1988)
   PUBMED   3282674
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078957.16, AC093193.11,
            AC079864.22, AC093167.11, AC079175.24, AC079177.21, AC090632.13,
            AC078958.30, AC079143.17 and AC006061.1.
            
            On Aug 13, 2020 this sequence version replaced NP_004004.1.
            
            Summary: This gene spans a genomic range of greater than 2 Mb and
            encodes a large protein containing an N-terminal actin-binding
            domain and multiple spectrin repeats. The encoded protein forms a
            component of the dystrophin-glycoprotein complex (DGC), which
            bridges the inner cytoskeleton and the extracellular matrix.
            Deletions, duplications, and point mutations at this gene locus may
            cause Duchenne muscular dystrophy (DMD), Becker muscular dystrophy
            (BMD), or cardiomyopathy. Alternative promoter usage and
            alternative splicing result in numerous distinct transcript
            variants and protein isoforms for this gene. [provided by RefSeq,
            Dec 2016].
            
            Transcript Variant: Dp140 transcripts use exons 45-79, starting at
            a promoter/exon 1 located in intron 44. Dp140 transcripts have a
            long (1 kb) 5' UTR since translation is initiated in exon 51
            (corresponding to aa 2461 of dystrophin). In addition to the
            alternative promoter and exon 1, differential splicing of exons
            71-74 and 78 produces at least five Dp140 isoforms. Of these, this
            transcript (Dp140) contains all of the exons.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC127103.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp21.2-p21.1"
     Protein         1..1225
                     /product="dystrophin isoform Dp140"
                     /note="mutant dystrophin"
                     /calculated_mol_wt=141269
     Region          <1..580
                     /region_name="central rod domain"
     Region          <1..10
                     /region_name="hinge region 3"
     Region          11..117
                     /region_name="repeat region 20"
     Region          12..228
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          118..226
                     /region_name="repeat region 21"
     Site            118..123
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          227..342
                     /region_name="repeat region 22"
     Region          230..473
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          343..471
                     /region_name="repeat region 23"
     Site            343..348
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          472..580
                     /region_name="repeat region 24"
     Region          474..580
                     /region_name="Spectrin"
                     /note="Spectrin repeat; pfam00435"
                     /db_xref="CDD:395348"
     Region          554..652
                     /region_name="hinge region 4"
     Site            581..585
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          596..632
                     /region_name="WW-domain"
     Region          599..628
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(612,623)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Site            620..948
                     /site_type="binding"
                     /note="dystroglycan binding site"
     Region          640..840
                     /region_name="Cysteine-rich domain"
     Region          665..826
                     /region_name="EFh_DMD"
                     /note="EF-hand-like motif found in dystrophin; cd16246"
                     /db_xref="CDD:320004"
     Site            order(665..666,668..669,687,691,695,697..698,701,712..718,
                     720..721,724,730,743,784..785,787)
                     /site_type="other"
                     /note="Domain interface"
                     /db_xref="CDD:320004"
     Region          665..704
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          670..697
                     /region_name="EF-hand 1"
     Region          711..745
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          718..746
                     /region_name="EF-hand 2"
     Site            728..730
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:320004"
     Region          751..787
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          800..826
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          840..1225
                     /region_name="Carboxy-terminal region"
     Region          847..894
                     /region_name="ZZ-domain"
     Region          851..899
                     /region_name="ZZ_dystrophin"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     dystrophin and dystrobrevin. The ZZ motif coordinates two
                     zinc ions and most likely participates in ligand binding
                     or molecular scaffolding. Dystrophin attaches actin
                     filaments to an integral membrane...; cd02334"
                     /db_xref="CDD:239074"
     Site            order(853,856,868,871,877,880,890,894)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(853,856,877,880)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(854,865,867,873,875)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(866,881,896,899)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(868,871,890,894)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239074"
     Site            984..1034
                     /site_type="binding"
                     /note="alpha1-syntrophin binding site"
     Site            1035..1075
                     /site_type="binding"
                     /note="beta1-syntrophin binding site"
     Region          1098..1133
                     /region_name="(Leu)6-heptad repeat"
     CDS             1..1225
                     /gene="DMD"
                     /gene_synonym="BMD; CMD3B; DXS142; DXS164; DXS206; DXS230;
                     DXS239; DXS268; DXS269; DXS270; DXS272; MRX85"
                     /coded_by="NM_004013.3:1042..4719"
                     /note="isoform Dp140 is encoded by transcript variant
                     Dp140"
                     /db_xref="CCDS:CCDS48091.1"
                     /db_xref="GeneID:1756"
                     /db_xref="HGNC:HGNC:2928"
                     /db_xref="MIM:300377"
ORIGIN      
        1 mpsslmlevp aladfnrawt eltdwlslld qviksqrvmv gdledinemi ikqkatmqdl
       61 eqrrpqleel itaaqnlknk tsnqeartii tdrieriqnq wdevqehlqn rrqqlnemlk
      121 dstqwleake eaeqvlgqar akleswkegp ytvdaiqkki tetkqlakdl rqwqtnvdva
      181 ndlalkllrd ysaddtrkvh miteninasw rsihkrvser eaaleethrl lqqfpldlek
      241 flawlteaet tanvlqdatr kerlledskg vkelmkqwqd lqgeieahtd vyhnldensq
      301 kilrslegsd davllqrrld nmnfkwselr kkslnirshl eassdqwkrl hlslqellvw
      361 lqlkddelsr qapiggdfpa vqkqndvhra fkrelktkep vimstletvr iflteqpleg
      421 leklyqepre lppeeraqnv trllrkqaee vnteweklnl hsadwqrkid etlerlrelq
      481 eatdeldlkl rqaevikgsw qpvgdllids lqdhlekvka lrgeiaplke nvshvndlar
      541 qlttlgiqls pynlstledl ntrwkllqva vedrvrqlhe ahrdfgpasq hflstsvqgp
      601 weraispnkv pyyinhetqt tcwdhpkmte lyqsladlnn vrfsayrtam klrrlqkalc
      661 ldllslsaac daldqhnlkq ndqpmdilqi inclttiydr leqehnnlvn vplcvdmcln
      721 wllnvydtgr tgrirvlsfk tgiislckah ledkyrylfk qvasstgfcd qrrlglllhd
      781 siqiprqlge vasfggsnie psvrscfqfa nnkpeieaal fldwmrlepq smvwlpvlhr
      841 vaaaetakhq akcnickecp iigfryrslk hfnydicqsc ffsgrvakgh kmhypmveyc
      901 tpttsgedvr dfakvlknkf rtkryfakhp rmgylpvqtv legdnmetpv tlinfwpvds
      961 apasspqlsh ddthsriehy asrlaemens ngsylndsis pnesiddehl liqhycqsln
     1021 qdsplsqprs paqilisles eergeleril adleeenrnl qaeydrlkqq hehkglsplp
     1081 sppemmptsp qsprdaelia eakllrqhkg rlearmqile dhnkqlesql hrlrqlleqp
     1141 qaeakvngtt vsspstslqr sdssqpmllr vvgsqtsdsm geedllsppq dtstgleevm
     1201 eqlnnsfpss rgrntpgkpm redtm
//
LOCUS       NP_001243547             772 aa            linear   PRI 21-NOV-2025
DEFINITION  gamma-tubulin complex component 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001243547
VERSION     NP_001243547.1
DBSOURCE    REFSEQ: accession NM_001256618.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 772)
  AUTHORS   Serna,M., Zimmermann,F., Vineethakumari,C., Gonzalez-Rodriguez,N.,
            Llorca,O. and Luders,J.
  TITLE     CDK5RAP2 activates microtubule nucleator gammaTuRC by facilitating
            template formation and actin release
  JOURNAL   Dev Cell 59 (23), 3175-3188 (2024)
   PUBMED   39321809
REFERENCE   2  (residues 1 to 772)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 772)
  AUTHORS   Mitani,T., Punetha,J., Akalin,I., Pehlivan,D., Dawidziuk,M., Coban
            Akdemir,Z., Yilmaz,S., Aslan,E., Hunter,J.V., Hijazi,H.,
            Grochowski,C.M., Jhangiani,S.N., Karaca,E., Fatih,J.M.,
            Iwanowski,P., Gambin,T., Wlasienko,P., Goszczanska-Ciuchta,A.,
            Bekiesinska-Figatowska,M., Hosseini,M., Arzhangi,S., Najmabadi,H.,
            Rosenfeld,J.A., Du,H., Marafi,D., Blaser,S., Teitelbaum,R.,
            Silver,R., Posey,J.E., Ropers,H.H., Gibbs,R.A., Wiszniewski,W.,
            Lupski,J.R., Chitayat,D., Kahrizi,K. and Gawlinski,P.
  CONSRTM   Baylor-Hopkins Center for Mendelian Genomics
  TITLE     Bi-allelic Pathogenic Variants in TUBGCP2 Cause Microcephaly and
            Lissencephaly Spectrum Disorders
  JOURNAL   Am J Hum Genet 105 (5), 1005-1015 (2019)
   PUBMED   31630790
  REMARK    GeneRIF: Pathogenic variants in TUBGCP2 cause an autosomal
            recessive neurodevelopmental trait consisting of a neuronal
            migration disorder.
REFERENCE   4  (residues 1 to 772)
  AUTHORS   Madarampalli,B., Yuan,Y., Liu,D., Lengel,K., Xu,Y., Li,G., Yang,J.,
            Liu,X., Lu,Z. and Liu,D.X.
  TITLE     ATF5 Connects the Pericentriolar Materials to the Proximal End of
            the Mother Centriole
  JOURNAL   Cell 162 (3), 580-592 (2015)
   PUBMED   26213385
REFERENCE   5  (residues 1 to 772)
  AUTHORS   Riehlman,T.D., Olmsted,Z.T., Branca,C.N., Winnie,A.M., Seo,L.,
            Cruz,L.O. and Paluh,J.L.
  TITLE     Functional replacement of fission yeast gamma-tubulin small complex
            proteins Alp4 and Alp6 by human GCP2 and GCP3
  JOURNAL   J Cell Sci 126 (Pt 19), 4406-4413 (2013)
   PUBMED   23886939
  REMARK    GeneRIF: Authors show genetically that GCP3/Spc98 function is fully
            conserved with Alp6 across species but that functional differences
            exist between GCP2/Spc97 and Alp4.
REFERENCE   6  (residues 1 to 772)
  AUTHORS   Haren,L. and Merdes,A.
  TITLE     Direct binding of NuMA to tubulin is mediated by a novel sequence
            motif in the tail domain that bundles and stabilizes microtubules
  JOURNAL   J Cell Sci 115 (Pt 9), 1815-1824 (2002)
   PUBMED   11956313
REFERENCE   7  (residues 1 to 772)
  AUTHORS   Murphy,S.M., Preble,A.M., Patel,U.K., O'Connell,K.L., Dias,D.P.,
            Moritz,M., Agard,D., Stults,J.T. and Stearns,T.
  TITLE     GCP5 and GCP6: two new members of the human gamma-tubulin complex
  JOURNAL   Mol Biol Cell 12 (11), 3340-3352 (2001)
   PUBMED   11694571
REFERENCE   8  (residues 1 to 772)
  AUTHORS   Murphy,S.M., Urbani,L. and Stearns,T.
  TITLE     The mammalian gamma-tubulin complex contains homologues of the
            yeast spindle pole body components spc97p and spc98p
  JOURNAL   J Cell Biol 141 (3), 663-674 (1998)
   PUBMED   9566967
REFERENCE   9  (residues 1 to 772)
  AUTHORS   Hsu,H.L. and Yeh,N.H.
  TITLE     Dynamic changes of NuMA during the cell cycle and possible
            appearance of a truncated form of NuMA during apoptosis
  JOURNAL   J Cell Sci 109 (Pt 2), 277-288 (1996)
   PUBMED   8838651
REFERENCE   10 (residues 1 to 772)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK297251.1, AL592071.13 and AA377890.1.
            
            Transcript Variant: This variant (3) uses a downstream, in-frame
            start codon and lacks two exons in the coding region, but maintains
            the reading frame, compared to variant 1. The encoded isoform (3)
            is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297251.1, SRR7410570.467877.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..772
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.3"
     Protein         1..772
                     /product="gamma-tubulin complex component 2 isoform 3"
                     /note="gamma-tubulin complex component 2; gamma-ring
                     complex protein 103 kDa; spindle pole body protein Spc97
                     homolog; hGrip103; tubulin gamma complex associated
                     protein 2"
                     /calculated_mol_wt=87960
     Region          88..376
                     /region_name="GCP_N_terminal"
                     /note="Gamma tubulin complex component N-terminal;
                     pfam17681"
                     /db_xref="CDD:465456"
     Region          379..735
                     /region_name="GCP_C_terminal"
                     /note="Gamma tubulin complex component C-terminal;
                     pfam04130"
                     /db_xref="CDD:461187"
     CDS             1..772
                     /gene="TUBGCP2"
                     /gene_synonym="ALP4; GCP-2; GCP2; Grip103; h103p; hGCP2;
                     hSpc97; PAMDDFS; SPBC97; SPC97; Spc97p"
                     /coded_by="NM_001256618.2:291..2609"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58104.1"
                     /db_xref="GeneID:10844"
                     /db_xref="HGNC:HGNC:18599"
                     /db_xref="MIM:617817"
ORIGIN      
        1 mqeleelrkq lgsvatgstl qqslelkrkm lrdkqnkkns gqhlpifpaw vyerpaligd
       61 fligagistd talpigtlpl asqesavved llyvlvgvdg ryvsaqplag rqsrtflvdp
      121 nldlsirelv hrilpvaasy savtrfieek ssfeygqvnh alaaamrtlv kehlilvsql
      181 eqlhrqglls lqklwfyiqp amrtmdilas latsvdkgec lggstlsllh drsfsytgds
      241 qaqelclylt kaasapyfev lekwiyrgii hdpysefmve ehelrkeriq edyndkywdq
      301 rytivqqqip sflqkmadki lstgkylnvv recghdvtcp vakeiiytlk erayveqiek
      361 afnyaskvll dflmeekelv ahlrsikryf lmdqgdffvh fmdlaeeelr kpveditppr
      421 leallelalr mstantdpfk ddlkidlmph dlitqllrvl aietkqekam ahadptelal
      481 sgleafsfdy ivkwplslii nrkaltryqm lfrhmfyckh verqlcsvwi snktakqhsl
      541 hsaqwfagaf tlrqrmlnfv qniqyymmfe vmeptwhile knlksasnid dvlghhtgfl
      601 dtclkdcmlt npellkvfsk lmsvcvmftn cmqkftqsmk ldgelggqtl ehstvlglpa
      661 gaeerarkel arkhlaehad tvqlvsgfea tinkfdknfs ahlldllarl siystsdceh
      721 gmasvisrld fngfyterle rlsaersqka tpqvpvlrgp papaprvavt aq
//
LOCUS       NP_001374708             154 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor protein D52 isoform 9 [Homo sapiens].
ACCESSION   NP_001374708
VERSION     NP_001374708.1
DBSOURCE    REFSEQ: accession NM_001387779.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Zhang,J., Li,Z., Han,J., Tian,Z., Meng,Q. and Niu,W.
  TITLE     KLF7 enhances the invasion and migration of colorectal cancer cells
            via the miR-139-5p/TPD52 axis
  JOURNAL   Cancer Biol Ther 25 (1), 2385172 (2024)
   PUBMED   39097779
  REMARK    GeneRIF: KLF7 enhances the invasion and migration of colorectal
            cancer cells via the miR-139-5p/TPD52 axis.
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Li,Y., Zhu,X., Zhang,C., Yin,Y., Chen,L., Liu,Y., He,A. and Xia,F.
  TITLE     Long noncoding RNA FTX promotes epithelial-mesenchymal transition
            of epithelial ovarian cancer through modulating miR-7515/TPD52 and
            activating Met/Akt/mTOR
  JOURNAL   Histol Histopathol 38 (12), 1487-1498 (2023)
   PUBMED   37140169
  REMARK    GeneRIF: Long noncoding RNA FTX promotes epithelial-mesenchymal
            transition of epithelial ovarian cancer through modulating
            miR-7515/TPD52 and activating Met/Akt/mTOR.
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Khan,K., Zafar,S., Badshah,Y., Ashraf,N.M., Rafiq,M., Danish,L.,
            Shabbir,M., Trembley,J.H., Afsar,T., Almajwal,A. and Razak,S.
  TITLE     Cross talk of tumor protein D52 (TPD52) with KLF9, PKCepsilon, and
            MicroRNA 223 in ovarian cancer
  JOURNAL   J Ovarian Res 16 (1), 202 (2023)
   PUBMED   37833790
  REMARK    GeneRIF: Cross talk of tumor protein D52 (TPD52) with KLF9,
            PKCepsilon, and MicroRNA 223 in ovarian cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Liu,S., Hu,C., Li,M., Zhou,W., Wang,R. and Xiao,Y.
  TITLE     Androgen receptor suppresses lung cancer invasion and increases
            cisplatin response via decreasing TPD52 expression
  JOURNAL   Int J Biol Sci 19 (12), 3709-3725 (2023)
   PUBMED   37564195
  REMARK    GeneRIF: Androgen receptor suppresses lung cancer invasion and
            increases cisplatin response via decreasing TPD52 expression.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Wang,R., He,H., Sun,X., Xu,J., Marshall,F.F., Zhau,H., Chung,L.W.,
            Fu,H. and He,D.
  TITLE     Transcription variants of the prostate-specific PrLZ gene and their
            interaction with 14-3-3 proteins
  JOURNAL   Biochem Biophys Res Commun 389 (3), 455-460 (2009)
   PUBMED   19732746
  REMARK    GeneRIF: Alternative splicing may contribute to abnormally enhanced
            PrLZ levels in prostate cancer, and interaction with 14-3-3
            proteins may be a mechanism by which PrLZ promotes cell
            proliferation and survival during prostate cancer development and
            progression.
REFERENCE   7  (residues 1 to 154)
  AUTHORS   Byrne,J.A., Nourse,C.R., Basset,P. and Gunning,P.
  TITLE     Identification of homo- and heteromeric interactions between
            members of the breast carcinoma-associated D52 protein family using
            the yeast two-hybrid system
  JOURNAL   Oncogene 16 (7), 873-881 (1998)
   PUBMED   9484778
REFERENCE   8  (residues 1 to 154)
  AUTHORS   Byrne,J.A., Mattei,M.G. and Basset,P.
  TITLE     Definition of the tumor protein D52 (TPD52) gene family through
            cloning of D52 homologues in human (hD53) and mouse (mD52)
  JOURNAL   Genomics 35 (3), 523-532 (1996)
   PUBMED   8812487
REFERENCE   9  (residues 1 to 154)
  AUTHORS   Chen,S.L., Maroulakou,I.G., Green,J.E., Romano-Spica,V., Modi,W.,
            Lautenberger,J. and Bhat,N.K.
  TITLE     Isolation and characterization of a novel gene expressed in
            multiple cancers
  JOURNAL   Oncogene 12 (4), 741-751 (1996)
   PUBMED   8632896
REFERENCE   10 (residues 1 to 154)
  AUTHORS   Byrne,J.A., Tomasetto,C., Garnier,J.M., Rouyer,N., Mattei,M.G.,
            Bellocq,J.P., Rio,M.C. and Basset,P.
  TITLE     A screening method to identify genes commonly overexpressed in
            carcinomas and the identification of a novel complementary DNA
            sequence
  JOURNAL   Cancer Res 55 (13), 2896-2903 (1995)
   PUBMED   7796418
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009686.14.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.977536.1,
                                           SRR11853565.27608.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.13"
     Protein         1..154
                     /product="tumor protein D52 isoform 9"
                     /EC_number="2.7.1.21"
                     /note="prostate and colon associated protein; prostate
                     leucine zipper; protein N8"
                     /calculated_mol_wt=16783
     Region          44..138
                     /region_name="TPD52"
                     /note="Tumour protein D52 family; pfam04201"
                     /db_xref="CDD:461225"
     CDS             1..154
                     /gene="TPD52"
                     /gene_synonym="D52; hD52; N8L; PC-1; PrLZ"
                     /coded_by="NM_001387779.1:122..586"
                     /note="isoform 9 is encoded by transcript variant 14"
                     /db_xref="GeneID:7163"
                     /db_xref="HGNC:HGNC:12005"
                     /db_xref="MIM:604068"
ORIGIN      
        1 mdrgeqgllr tdpvpeeged vaatisatet lseeeqeelr relakveeei qtlsqvlaak
       61 ekhlaeikrk lginslqelk qniakgwqdv tatsaykkts etlsqagqka saafssvgsv
      121 itkkledvkn sptfksfeek venlkahpss ilst
//
LOCUS       NP_000312                928 aa            linear   PRI 21-NOV-2025
DEFINITION  retinoblastoma-associated protein isoform 1 [Homo sapiens].
ACCESSION   NP_000312
VERSION     NP_000312.2
DBSOURCE    REFSEQ: accession NM_000321.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 928)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 928)
  AUTHORS   Castro,A., Ruiz Rivera,A., Moorman,C.C., Wolf-Saxon,E.R.,
            Mims,H.N., Vasquez Meza,V.I., Rangel,M.A., Loera,M.M., Bond,I.C.,
            Buchanan,S.B., Villarreal,E., Tripathi,S., Rubin,S.M. and
            Burke,J.R.
  TITLE     Structural and functional analysis of cancer-associated missense
            variants in the retinoblastoma protein pocket domain
  JOURNAL   J Biol Chem 301 (3), 108284 (2025)
   PUBMED   39938803
REFERENCE   3  (residues 1 to 928)
  AUTHORS   Zhang,S., Valenzuela,L.F., Zatulovskiy,E., Mangiante,L., Curtis,C.
            and Skotheim,J.M.
  TITLE     The G1-S transition is promoted by Rb degradation via the E3 ligase
            UBR5
  JOURNAL   Sci Adv 10 (43), eadq6858 (2024)
   PUBMED   39441926
  REMARK    GeneRIF: The G1-S transition is promoted by Rb degradation via the
            E3 ligase UBR5.
REFERENCE   4  (residues 1 to 928)
  AUTHORS   Schwartz,C.J., Marra,A., Selenica,P., Gazzo,A., Tan,K., Ross,D.,
            Razavi,P., Chandarlapaty,S., Weigelt,B., Reis-Filho,J.S., Brogi,E.,
            Pareja,F. and Wen,H.Y.
  TITLE     RB1 Genetic Alterations in Estrogen Receptor-Positive Breast
            Carcinomas: Correlation With Neuroendocrine Differentiation
  JOURNAL   Mod Pathol 37 (8), 100541 (2024)
   PUBMED   38897452
  REMARK    GeneRIF: RB1 Genetic Alterations in Estrogen Receptor-Positive
            Breast Carcinomas: Correlation With Neuroendocrine Differentiation.
REFERENCE   5  (residues 1 to 928)
  AUTHORS   Konagaya,Y., Rosenthal,D., Ratnayeke,N., Fan,Y. and Meyer,T.
  TITLE     An intermediate Rb-E2F activity state safeguards proliferation
            commitment
  JOURNAL   Nature 631 (8020), 424-431 (2024)
   PUBMED   38926571
  REMARK    GeneRIF: An intermediate Rb-E2F activity state safeguards
            proliferation commitment.
REFERENCE   6  (residues 1 to 928)
  AUTHORS   Lohmann,D.R. and Gallie,B.L.
  TITLE     Retinoblastoma
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301625
REFERENCE   7  (residues 1 to 928)
  AUTHORS   Dyson,N., Guida,P., Munger,K. and Harlow,E.
  TITLE     Homologous sequences in adenovirus E1A and human papillomavirus E7
            proteins mediate interaction with the same set of cellular proteins
  JOURNAL   J Virol 66 (12), 6893-6902 (1992)
   PUBMED   1331501
REFERENCE   8  (residues 1 to 928)
  AUTHORS   Huang,S., Shin,E., Sheppard,K.A., Chokroverty,L., Shan,B.,
            Qian,Y.W., Lee,E.Y. and Yee,A.S.
  TITLE     The retinoblastoma protein region required for interaction with the
            E2F transcription factor includes the T/E1A binding and
            carboxy-terminal sequences
  JOURNAL   DNA Cell Biol 11 (7), 539-548 (1992)
   PUBMED   1388726
REFERENCE   9  (residues 1 to 928)
  AUTHORS   Onadim,Z., Hogg,A., Baird,P.N. and Cowell,J.K.
  TITLE     Oncogenic point mutations in exon 20 of the RB1 gene in families
            showing incomplete penetrance and mild expression of the
            retinoblastoma phenotype
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 6177-6181 (1992)
   PUBMED   1352883
REFERENCE   10 (residues 1 to 928)
  AUTHORS   Hogg,A., Onadim,Z., Baird,P.N. and Cowell,J.K.
  TITLE     Detection of heterozygous mutations in the RB1 gene in
            retinoblastoma patients using single-strand conformation
            polymorphism analysis and polymerase chain reaction sequencing
  JOURNAL   Oncogene 7 (7), 1445-1451 (1992)
   PUBMED   1352398
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL392048.9, BC040540.1 and
            L41870.1.
            
            On Jun 9, 2006 this sequence version replaced NP_000312.1.
            
            Summary: The protein encoded by this gene is a negative regulator
            of the cell cycle and was the first tumor suppressor gene found.
            The encoded protein also stabilizes constitutive heterochromatin to
            maintain the overall chromatin structure. The active,
            hypophosphorylated form of the protein binds transcription factor
            E2F1. Defects in this gene are a cause of childhood cancer
            retinoblastoma (RB), bladder cancer, and osteogenic sarcoma.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC040540.1, L41870.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000267163.6/ ENSP00000267163.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..928
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.2"
     Protein         1..928
                     /product="retinoblastoma-associated protein isoform 1"
                     /note="retinoblastoma-associated protein;
                     prepro-retinoblastoma-associated protein; protein
                     phosphatase 1, regulatory subunit 130; retinoblastoma
                     suspectibility protein; retinoblastoma 1"
                     /calculated_mol_wt=106029
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            2
                     /site_type="methylation"
                     /note="N,N-dimethylproline.
                     /evidence=ECO:0000250|UniProtKB:P13405; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Region          114..227
                     /region_name="DUF3452"
                     /note="Domain of unknown function (DUF3452); pfam11934"
                     /db_xref="CDD:463402"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:1756735,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:1756735,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Region          373..771
                     /region_name="Pocket, binds T and E1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Region          373..579
                     /region_name="Domain A"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Region          373..573
                     /region_name="RB_A"
                     /note="Retinoblastoma-associated protein A domain;
                     pfam01858"
                     /db_xref="CDD:460364"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:1756735,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK2.
                     /evidence=ECO:0000269|PubMed:10499802; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Region          580..639
                     /region_name="Spacer"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13405; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Region          610..632
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CHEK2 and CHEK1.
                     /evidence=ECO:0000269|PubMed:17380128,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Region          640..771
                     /region_name="Domain B"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Region          645..771
                     /region_name="CYCLIN_RB"
                     /note="cyclin box found in retinoblastoma-associated
                     protein (RB) and similar proteins; cd20599"
                     /db_xref="CDD:410302"
     Site            order(645,649,652..653,656,660)
                     /site_type="other"
                     /note="E2F transcription factor binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410302"
     Site            order(709,713..714,720..721,753,756..757,761)
                     /site_type="other"
                     /note="LxCxE peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410302"
     Region          763..928
                     /region_name="Interaction with LIMD1.
                     /evidence=ECO:0000269|PubMed:15542589"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Region          768..925
                     /region_name="Rb_C"
                     /note="Rb C-terminal domain; pfam08934"
                     /db_xref="CDD:462639"
     Region          771..928
                     /region_name="Domain C, mediates interaction with E4F1.
                     /evidence=ECO:0000269|PubMed:10869426"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            780
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            788
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            795
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            807
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1 and CDK3.
                     /evidence=ECO:0000269|PubMed:15084261,
                     ECO:0000269|PubMed:1756735, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            810
                     /site_type="methylation"
                     /note="N6-methyllysine, by SMYD2.
                     /evidence=ECO:0000269|PubMed:22787429; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            811
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1 and CDK3.
                     /evidence=ECO:0000269|PubMed:15084261,
                     ECO:0000269|PubMed:1756735, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK6.
                     /evidence=ECO:0000269|PubMed:15809340,
                     ECO:0000269|PubMed:16360038, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            823
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            826
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK4.
                     /evidence=ECO:0000269|PubMed:15809340,
                     ECO:0000269|PubMed:16360038, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            841
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            855
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Region          860..928
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Region          860..876
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:P13405"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            860
                     /site_type="methylation"
                     /note="N6-methyllysine, by SMYD2.
                     /evidence=ECO:0000269|PubMed:20870719; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            873
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by PCAF.
                     /evidence=ECO:0000269|PubMed:20940255; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            874
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by PCAF.
                     /evidence=ECO:0000269|PubMed:20940255; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     CDS             1..928
                     /gene="RB1"
                     /gene_synonym="OSRC; p105-Rb; p110-RB1; pp110; PPP1R130;
                     pRb; RB"
                     /coded_by="NM_000321.3:163..2949"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31973.1"
                     /db_xref="GeneID:5925"
                     /db_xref="HGNC:HGNC:9884"
                     /db_xref="MIM:614041"
ORIGIN      
        1 mppktprkta ataaaaaaep papppppppe edpeqdsgpe dlplvrlefe eteepdftal
       61 cqklkipdhv rerawltwek vssvdgvlgg yiqkkkelwg icifiaavdl demsftftel
      121 qknieisvhk ffnllkeidt stkvdnamsr llkkydvlfa lfsklertce liyltqpsss
      181 isteinsalv lkvswitfll akgevlqmed dlvisfqlml cvldyfikls ppmllkepyk
      241 tavipingsp rtprrgqnrs ariakqlend triievlcke hecnidevkn vyfknfipfm
      301 nslglvtsng lpevenlskr yeeiylknkd ldarlfldhd ktlqtdsids fetqrtprks
      361 nldeevnvip phtpvrtvmn tiqqlmmiln sasdqpsenl isyfnnctvn pkesilkrvk
      421 digyifkekf akavgqgcve igsqryklgv rlyyrvmesm lkseeerlsi qnfskllndn
      481 ifhmsllaca levvmatysr stsqnldsgt dlsfpwilnv lnlkafdfyk viesfikaeg
      541 nltremikhl ercehrimes lawlsdsplf dlikqskdre gptdhlesac plnlplqnnh
      601 taadmylspv rspkkkgstt rvnstanaet qatsafqtqk plkstslslf ykkvyrlayl
      661 rlntlcerll sehpelehii wtlfqhtlqn eyelmrdrhl dqimmcsmyg ickvknidlk
      721 fkiivtaykd lphavqetfk rvlikeeeyd siivfynsvf mqrlktnilq yastrpptls
      781 piphiprspy kfpssplrip ggniyisplk spykiseglp tptkmtprsr ilvsigesfg
      841 tsekfqkinq mvcnsdrvlk rsaegsnppk plkklrfdie gsdeadgskh lpgeskfqqk
      901 laemtstrtr mqkqkmndsm dtsnkeek
//
LOCUS       NP_001381689             531 aa            linear   PRI 21-NOV-2025
DEFINITION  COP9 signalosome complex subunit 1 isoform 11 [Homo sapiens].
ACCESSION   NP_001381689
VERSION     NP_001381689.1
DBSOURCE    REFSEQ: accession NM_001394760.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Wei,H., Niu,Z., Ji,R., Jiang,W., Tang,J., Meng,Z., Cao,X., Zhang,X.
            and Liu,X.
  TITLE     Bioinformatics analysis of GPS1 expression and biological function
            in breast cancer
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 52 (2024)
   PUBMED   38289496
  REMARK    GeneRIF: Bioinformatics analysis of GPS1 expression and biological
            function in breast cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Fu,H., Zhang,Y., Chen,Y., Chen,J. and Chen,P.
  TITLE     CSN1 facilitates proliferation and migration of hepatocellular
            carcinoma cells by upregulating cyclin A2 expression
  JOURNAL   Mol Med Rep 23 (1) (2021)
   PUBMED   33200803
  REMARK    GeneRIF: CSN1 facilitates proliferation and migration of
            hepatocellular carcinoma cells by upregulating cyclin A2
            expression.
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Lyapina,S., Cope,G., Shevchenko,A., Serino,G., Tsuge,T., Zhou,C.,
            Wolf,D.A., Wei,N., Shevchenko,A. and Deshaies,R.J.
  TITLE     Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome
  JOURNAL   Science 292 (5520), 1382-1385 (2001)
   PUBMED   11337588
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Bech-Otschir,D., Kraft,R., Huang,X., Henklein,P., Kapelari,B.,
            Pollmann,C. and Dubiel,W.
  TITLE     COP9 signalosome-specific phosphorylation targets p53 to
            degradation by the ubiquitin system
  JOURNAL   EMBO J 20 (7), 1630-1639 (2001)
   PUBMED   11285227
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Tsuge,T., Matsui,M. and Wei,N.
  TITLE     The subunit 1 of the COP9 signalosome suppresses gene expression
            through its N-terminal domain and incorporates into the complex
            through the PCI domain
  JOURNAL   J Mol Biol 305 (1), 1-9 (2001)
   PUBMED   11114242
  REMARK    GeneRIF: The N-terminal half of CSN1/GPS1 is required to repress
            c-fos expression and to inhibit AP-1 and SRE transactivation, while
            the C-terminal half allows integration of the protein into the COP9
            signalosome.
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Seeger,M., Kraft,R., Ferrell,K., Bech-Otschir,D., Dumdey,R.,
            Schade,R., Gordon,C., Naumann,M. and Dubiel,W.
  TITLE     A novel protein complex involved in signal transduction possessing
            similarities to 26S proteasome subunits
  JOURNAL   FASEB J 12 (6), 469-478 (1998)
   PUBMED   9535219
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Spain,B.H., Bowdish,K.S., Pacal,A.R., Staub,S.F., Koo,D.,
            Chang,C.Y., Xie,W. and Colicelli,J.
  TITLE     Two human cDNAs, including a homolog of Arabidopsis FUS6 (COP11),
            suppress G-protein- and mitogen-activated protein kinase-mediated
            signal transduction in yeast and mammalian cells
  JOURNAL   Mol Cell Biol 16 (12), 6698-6706 (1996)
   PUBMED   8943324
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC135056.4.
            
            Summary: This gene is known to suppress G-protein and
            mitogen-activated signal transduction in mammalian cells. The
            encoded protein shares significant similarity with Arabidopsis
            FUS6, which is a regulator of light-mediated signal transduction in
            plant cells. [provided by RefSeq, Mar 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.2614264.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..531
                     /product="COP9 signalosome complex subunit 1 isoform 11"
                     /note="COP9 signalosome complex subunit 1; JAB1-containing
                     signalosome subunit 1"
                     /calculated_mol_wt=59363
     Region          167..349
                     /region_name="RPN7"
                     /note="26S proteasome subunit RPN7; pfam10602"
                     /db_xref="CDD:431387"
     Region          364..468
                     /region_name="PCI"
                     /note="PCI domain; pfam01399"
                     /db_xref="CDD:460195"
     CDS             1..531
                     /gene="GPS1"
                     /gene_synonym="COPS1; CSN1; SGN1"
                     /coded_by="NM_001394760.1:112..1707"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:2873"
                     /db_xref="HGNC:HGNC:4549"
                     /db_xref="MIM:601934"
ORIGIN      
        1 mrdssapssa sssvtdlyct phssrsdlvl pgtagdfsls aslsactlly egavepmqid
       61 vdpqedpqna pdvnyvvenp sldleqyaas ysglmrierl qfiadhcptl rvealkmals
      121 fvqrtfnvdm yeeihrklse atrsslrelq napdaipesg veppaldtaw veatrkkall
      181 klekldtdlk nykgnsikes irrghddlgd hyldcgdlsn alkcysrard yctsakhvin
      241 mclnvikvsv ylqnwshvls yvskaestpe iaeqrgerds qtqailtklk caaglaelaa
      301 rkykqaakcl llasfdhcdf pellspsnva iygglcalat fdrqelqrnv issssfklfl
      361 elepqvrdii fkfyeskyas clkmldemkd nllldmylap hvrtlytqir nraliqyfsp
      421 yvsadmhrma aafnttvaal edeltqlile glisarvdsh skilyardvd qrsttfeksl
      481 lmgkefqrra kammlraavl rnqihvkspp regsqgeltp ansqsrmstn m
//
LOCUS       NP_055459               2346 aa            linear   PRI 21-NOV-2025
DEFINITION  myomegalin isoform 1 [Homo sapiens].
ACCESSION   NP_055459 XP_290895
VERSION     NP_055459.5
DBSOURCE    REFSEQ: accession NM_014644.7
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2346)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2346)
  AUTHORS   Pan,R., Dai,J., Liang,W., Wang,H., Ye,L., Ye,S., Lin,Z., Huang,S.,
            Xiong,Y., Zhang,L., Lu,L., Wang,O., Shen,X., Liao,W. and Lu,X.
  TITLE     PDE4DIP contributes to colorectal cancer growth and chemoresistance
            through modulation of the NF1/RAS signaling axis
  JOURNAL   Cell Death Dis 14 (6), 373 (2023)
   PUBMED   37355626
  REMARK    GeneRIF: PDE4DIP contributes to colorectal cancer growth and
            chemoresistance through modulation of the NF1/RAS signaling axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2346)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   4  (residues 1 to 2346)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 2346)
  AUTHORS   Abou Ziki,M.D., Bhat,N., Neogi,A., Driscoll,T.P., Ugwu,N., Liu,Y.,
            Smith,E., Abboud,J.M., Chouairi,S., Schwartz,M.A., Akar,J.G. and
            Mani,A.
  TITLE     Epistatic interaction of PDE4DIP and DES mutations in familial
            atrial fibrillation with slow conduction
  JOURNAL   Hum Mutat 42 (10), 1279-1293 (2021)
   PUBMED   34289528
  REMARK    GeneRIF: Epistatic interaction of PDE4DIP and DES mutations in
            familial atrial fibrillation with slow conduction.
REFERENCE   6  (residues 1 to 2346)
  AUTHORS   Shimada,H., Kuboshima,M., Shiratori,T., Nabeya,Y., Takeuchi,A.,
            Takagi,H., Nomura,F., Takiguchi,M., Ochiai,T. and Hiwasa,T.
  TITLE     Serum anti-myomegalin antibodies in patients with esophageal
            squamous cell carcinoma
  JOURNAL   Int J Oncol 30 (1), 97-103 (2007)
   PUBMED   17143517
  REMARK    GeneRIF: MMGL-antibody is significantly with a favorable prognosis.
            Consequently, MMGL-anatibodies may be a useful tumor marker to
            diagnose and establish a prognosis in patients with esophageal
            squamous cell carcinoma.
REFERENCE   7  (residues 1 to 2346)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 2346)
  AUTHORS   Soejima,H., Kawamoto,S., Akai,J., Miyoshi,O., Arai,Y., Morohka,T.,
            Matsuo,S., Niikawa,N., Kimura,A., Okubo,K. and Mukai,T.
  TITLE     Isolation of novel heart-specific genes using the BodyMap database
  JOURNAL   Genomics 74 (1), 115-120 (2001)
   PUBMED   11374908
REFERENCE   9  (residues 1 to 2346)
  AUTHORS   Verde,I., Pahlke,G., Salanova,M., Zhang,G., Wang,S., Coletti,D.,
            Onuffer,J., Jin,S.L. and Conti,M.
  TITLE     Myomegalin is a novel protein of the golgi/centrosome that
            interacts with a cyclic nucleotide phosphodiesterase
  JOURNAL   J Biol Chem 276 (14), 11189-11198 (2001)
   PUBMED   11134006
REFERENCE   10 (residues 1 to 2346)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC239802.3 and AC239804.2.
            
            On Jul 18, 2013 this sequence version replaced NP_055459.4.
            
            Summary: The protein encoded by this gene serves to anchor
            phosphodiesterase 4D to the Golgi/centrosome region of the cell.
            Defects in this gene may be a cause of myeloproliferative disorder
            (MBD) associated with eosinophilia. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL833273.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2346
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     Protein         1..2346
                     /product="myomegalin isoform 1"
                     /note="myomegalin; cardiomyopathy-associated protein 2"
                     /calculated_mol_wt=264973
     Region          6..73
                     /region_name="Cnn_1N"
                     /note="Centrosomin N-terminal motif 1; pfam07989"
                     /db_xref="CDD:462333"
     Region          <31..679
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5VU43.3)"
     Region          388..1111
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          698..732
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VU43.3)"
     Site            704
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5VU43.3)"
     Site            742..743
                     /site_type="other"
                     /note="Breakpoint for insertion to form PDE4DIP-PDGFRB
                     fusion protein; propagated from UniProtKB/Swiss-Prot
                     (Q5VU43.3)"
     Region          1193..1214
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VU43.3)"
     Region          1552..1621
                     /region_name="Olduvai"
                     /note="Olduvai domain; pfam06758"
                     /db_xref="CDD:429104"
     Region          1591..1614
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VU43.3)"
     Region          1633..1690
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VU43.3)"
     Region          <1841..>2018
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          2081..2103
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VU43.3)"
     Region          2127..2156
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VU43.3)"
     CDS             1..2346
                     /gene="PDE4DIP"
                     /gene_synonym="CMYA2; MMGL"
                     /coded_by="NM_014644.7:149..7189"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS72891.1"
                     /db_xref="GeneID:9659"
                     /db_xref="HGNC:HGNC:15580"
                     /db_xref="MIM:608117"
ORIGIN      
        1 msngyrtlsq hlndlkkenf slklriyfle ermqqkyeas rediykrnie lkveveslkr
       61 elqdkkqhld ktwadvenln sqneaelrrq feerqqeteh vyellenkiq llqeesrlak
      121 neaarmaalv eaekecnlel seklkgvtkn wedvpgdqvk pdqytealaq rdkrieelnq
      181 slaaqerlve qlsrekqqll hlleeptsme vqpmteellk qqklnshett itqqsvsdsh
      241 laelqekiqq teatnkilqe klnemsyelk caqessqkqd gtiqnlketl ksrereteel
      301 yqviegqndt maklremlhq sqlgqlhsse gtspaqqqva lldlqsalfc sqleiqklqr
      361 vvrqkerqla dakqcvqfve aaaheseqqk easwkhnqel rkalqqlqee lqnksqqlra
      421 weaekyneir tqeqniqhln hslshkeqll qefrellqyr dnsdktlean emlleklrqr
      481 ihdkavaler aidekfsale ekekelrqlr lavrerdhdl erlrdvlssn eatmqsmesl
      541 lrakgleveq lsttcqnlqw lkeemetkfs rwqkeqesii qqlqtslhdr nkevedlsat
      601 llcklgpgqs eiaeelcqrl qrkermlqdl lsdrnkqvle hemeiqgllq svstreqesq
      661 aaaeklvqal mernselqal rqylggrdsl msqapisnqq aevtptgrlg kqtdqgsmqi
      721 psrddstslt akedvsiprs tlgdldtvag lekelsnake elelmakker esqmelsalq
      781 smmavqeeel qvqaadmesl trniqikedl ikdlqmqlvd pedipamerl tqevlllrek
      841 vasvesqgqe isgnrrqqll lmleglvder srlnealqae rqlysslvkf hahpesserd
      901 rtlqvelega qvlrsrleev lgrslerlnr letlaaigga aagddtedts teftdsieee
      961 aahhshqqlv kvalekslat vetqnpsfsp pspmggdsnr clqeemlhlr aefhqhleek
     1021 rkaeeelkel kaqieeagfs svshirntml slclenaelk eqmgeamsdg weieedkekg
     1081 evmvetvvtk eglsesslqa efrklqgklk nahniinllk eqlvlsskeg nskltpellv
     1141 hltstierin telvgspgkh qhqeegnvtv rpfprpqsld lgatftvdah qldnqsqprd
     1201 pgpqsafslp gstqhlrsql sqckqryqdl qeklllseat vfaqanelek yrvmltgesl
     1261 vkqdskqiqv dlqdlgyetc grseneaere ettspeceeh nslkemvlme glcseqgrrg
     1321 stlassserk plenqlgkqe efrvygksen ilvlrkdikd lkaqlqnank viqnlksrvr
     1381 slsvtsdyss slerprklra vgtlegssph svpdedegwl sdgtgafysp glqakkdles
     1441 liqrvsqlea qlpkngleek laeelrsasw pgkydsliqd qarelsylrq kiregrgicy
     1501 litrhakdtv ksfedllrsn didyylgqsf reqlaqgsql terltsklst kdhksekdqa
     1561 gleplalrls relqekekvi evlqakldar sltpssshal sdshrspsst sflsdeleac
     1621 sdmdivseyt hyeekkasps hsdsihhssh savlsskpss tsasqgakae snsnpislpt
     1681 pqntpkeanq ahsgfhfhsi pklaslpqap lpsapssflp fsptgplllg ccetpvvsla
     1741 eaqqelqmlq kqlgesastv ppastatlls ndleadssyy lnsaqphspp rgtielgril
     1801 epgylgssgk wdvmrpqkgs vsgdlssgss vyqlnskptg adlleehlge irnlrqrlee
     1861 sicindrlre qlehrltsta rgrgstsnfy sqglesipql cnenrvlred nrrlqaqlsh
     1921 vsrehsqete slreallssr shlqelekel ehqkverqql ledlrekqqe vlhfreerls
     1981 lqendsrlqh klvllqqqce ekqqlfeslq selqiyealy gnskkglkay sldachqipl
     2041 ssdlshlvae vralrgqleq siqgnnclrl qlqqqlesga gkaslspssi nqnfpastdp
     2101 gnkqlllqds avsppvrdvg mnspalvfps sasstpgset piinranglg ldtspvmktp
     2161 pklegdatdg sfankhgrhv ighiddysal rqqiaegkll vkkivslvrs acsfpgleaq
     2221 gtevlgskgi helrsstsal hhaleesasl ltmfwraalp sthipvlpgk vgesterell
     2281 elrtkvskqe rllqsttehl knanqqkesm eqfivsqltr thdvlkkart nlevkslral
     2341 pctpal
//
LOCUS       NP_001333253             517 aa            linear   PRI 21-NOV-2025
DEFINITION  autophagy-related protein 13 isoform c [Homo sapiens].
ACCESSION   NP_001333253 XP_016874093
VERSION     NP_001333253.1
DBSOURCE    REFSEQ: accession NM_001346324.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Patel,A. and Faesen,A.C.
  TITLE     Metamorphosis by ATG13 and ATG101 in human autophagy initiation
  JOURNAL   Autophagy 20 (4), 968-969 (2024)
   PUBMED   37394799
  REMARK    GeneRIF: Metamorphosis by ATG13 and ATG101 in human autophagy
            initiation.
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Nguyen,A. and Faesen,A.C.
  TITLE     The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis
  JOURNAL   FEBS Lett 598 (1), 114-126 (2024)
   PUBMED   37567770
  REMARK    GeneRIF: The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis.
            Review article
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Karabi,Z., Moradian,F. and Kheirabadi,M.
  TITLE     The effect of lactoferrin on ULK1 and ATG13 genes expression in
            breast cancer cell line MCF7 and bioinformatics studies of protein
            interaction between lactoferrin and the autophagy initiation
            complex
  JOURNAL   Cell Biochem Biophys 80 (4), 795-806 (2022)
   PUBMED   36169801
  REMARK    GeneRIF: The effect of lactoferrin on ULK1 and ATG13 genes
            expression in breast cancer cell line MCF7 and bioinformatics
            studies of protein interaction between lactoferrin and the
            autophagy initiation complex.
REFERENCE   5  (residues 1 to 517)
  AUTHORS   Gottschalk,G., Peterson,D., Knox,K., Maynard,M., Whelan,R.J. and
            Roy,A.
  TITLE     Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE)
  JOURNAL   Mol Cell Neurosci 120, 103731 (2022)
   PUBMED   35487443
  REMARK    GeneRIF: Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE).
REFERENCE   6  (residues 1 to 517)
  AUTHORS   Jung,C.H., Jun,C.B., Ro,S.H., Kim,Y.M., Otto,N.M., Cao,J., Kundu,M.
            and Kim,D.H.
  TITLE     ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy
            machinery
  JOURNAL   Mol Biol Cell 20 (7), 1992-2003 (2009)
   PUBMED   19225151
  REMARK    GeneRIF: The ULK-Atg13-FIP200 complexes are direct targets of mTOR
            and important regulators of autophagy in response to mTOR
            signaling.
REFERENCE   7  (residues 1 to 517)
  AUTHORS   Hosokawa,N., Hara,T., Kaizuka,T., Kishi,C., Takamura,A., Miura,Y.,
            Iemura,S., Natsume,T., Takehana,K., Yamada,N., Guan,J.L., Oshiro,N.
            and Mizushima,N.
  TITLE     Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200
            complex required for autophagy
  JOURNAL   Mol Biol Cell 20 (7), 1981-1991 (2009)
   PUBMED   19211835
  REMARK    GeneRIF: mTORC1 suppresses autophagy through direct regulation of
            the approximately 3-MDa ULK1-Atg13-FIP200 complex.
REFERENCE   8  (residues 1 to 517)
  AUTHORS   Chan,E.Y., Longatti,A., McKnight,N.C. and Tooze,S.A.
  TITLE     Kinase-inactivated ULK proteins inhibit autophagy via their
            conserved C-terminal domains using an Atg13-independent mechanism
  JOURNAL   Mol Cell Biol 29 (1), 157-171 (2009)
   PUBMED   18936157
  REMARK    GeneRIF: The functions of ULK1 and ULK2 are controlled by
            autophosphorylation and conformational changes involving exposure
            of the C-terminal domain and interaction with the putative human
            homologue of Atg13.
            GeneRIF: The gene product is the functional homologue of yeast
            Atg13, and required for autophagy in mammalian cells.
REFERENCE   9  (residues 1 to 517)
  AUTHORS   Meijer,W.H., van der Klei,I.J., Veenhuis,M. and Kiel,J.A.
  TITLE     ATG genes involved in non-selective autophagy are conserved from
            yeast to man, but the selective Cvt and pexophagy pathways also
            require organism-specific genes
  JOURNAL   Autophagy 3 (2), 106-116 (2007)
   PUBMED   17204848
REFERENCE   10 (residues 1 to 517)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC127035.6 and AC115088.6.
            
            On Oct 9, 2016 this sequence version replaced XP_016874093.1.
            
            Summary: The protein encoded by this gene is an autophagy factor
            and a target of the TOR kinase signaling pathway. The encoded
            protein is essential for autophagosome formation and mitophagy.
            [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (20), as well as variants 1, 4,
            15-19, and 21-28, encodes isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.279823.1,
                                           SRR1660805.25582.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..517
                     /product="autophagy-related protein 13 isoform c"
                     /note="autophagy-related protein 13; ATG13 autophagy
                     related 13 homolog"
                     /calculated_mol_wt=56441
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O75143.1)"
     Region          19..192
                     /region_name="ATG13"
                     /note="Autophagy-related protein 13; pfam10033"
                     /db_xref="CDD:431003"
     Region          127..134
                     /region_name="Important for interaction with ATG101.
                     /evidence=ECO:0000269|PubMed:26299944"
                     /note="propagated from UniProtKB/Swiss-Prot (O75143.1)"
     Region          305..324
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75143.1)"
     Region          332..361
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75143.1)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ULK1.
                     /evidence=ECO:0000269|PubMed:21855797,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75143.1)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75143.1)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75143.1)"
     Region          405..439
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75143.1)"
     Region          444..447
                     /region_name="LIR. /evidence=ECO:0000305|PubMed:24290141"
                     /note="propagated from UniProtKB/Swiss-Prot (O75143.1)"
     CDS             1..517
                     /gene="ATG13"
                     /gene_synonym="KIAA0652; PARATARG8"
                     /coded_by="NM_001346324.2:468..2021"
                     /note="isoform c is encoded by transcript variant 20"
                     /db_xref="CCDS:CCDS44582.1"
                     /db_xref="GeneID:9776"
                     /db_xref="HGNC:HGNC:29091"
                     /db_xref="MIM:615088"
ORIGIN      
        1 metdlnsqdr kdldkfikff alktvqvivq arlgekictr ssssptgsdw fnlaikdipe
       61 vtheakkala gqlpavgrsm cveislktse gdsmeleiwc lemnekcdke ikvsytvynr
      121 lslllkslla itrvtpayrl srkqgheyvi lyriyfgevq lsglgegfqt vrvgtvgtpv
      181 gtitlscayr inlafmstrq fertppimgi iidhfvdrpy pssspmhpcn yrtagedtgv
      241 iypsvedsqe vcttsfstsp psqlsssrls yqpaalgvgs adlaypvvfa aglnathphq
      301 lmvpgkeggv plapnqpvhg tqadqerlat ctpsdrthca atpsssedte tvsnssegra
      361 sphdvletif vrkvgafvnk pinqvtltsl dipfamfapk nleledtdpm vnppdspete
      421 splqgslhsd gssggssgnt hddfvmidfk pafskddilp mdlgtfyref qnppqlssls
      481 idigaqsmae dldslpekla vheknvrefd afvetlq
//
LOCUS       NP_741960                478 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit alpha
            isoform 2 [Homo sapiens].
ACCESSION   NP_741960
VERSION     NP_741960.1
DBSOURCE    REFSEQ: accession NM_171825.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Zheng,P., Hu,Z., Shen,Y., Gu,L., Ouyang,Y., Duan,Y., Ji,G.,
            Dong,B., Lin,Y., Wen,T., Tian,Q., Hou,Y., Zhou,Q., Sun,X., Chen,X.,
            Wang,K.L., Luo,S., Wu,S., Sun,Y., Li,M., Xiao,L., Wu,Q., Meng,Y.,
            Liu,G., Wang,Z., Bai,X., Duan,S., Ding,Y., Bi,Y., Wang,Y., Li,G.,
            Liu,X., Lu,Z., Wu,X., Tang,Z. and Xu,D.
  TITLE     PSAT1 impairs ferroptosis and reduces immunotherapy efficacy via
            GPX4 hydroxylation
  JOURNAL   Nat Chem Biol 21 (9), 1420-1432 (2025)
   PUBMED   40281343
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Lin,J., Xia,H., Yu,J., Wang,Y., Wang,H., Xie,D., Cheng,C., Lu,L.,
            Bian,T., Wu,Y. and Liu,Q.
  TITLE     circADAMTS6 via stabilizing CAMK2A is involved in smoking-induced
            emphysema through driving M2 macrophage polarization
  JOURNAL   Environ Int 190, 108832 (2024)
   PUBMED   38936066
  REMARK    GeneRIF: circADAMTS6 via stabilizing CAMK2A is involved in
            smoking-induced emphysema through driving M2 macrophage
            polarization.
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Zhang,Y., Xia,M., Zhao,T., Zhang,Q., Li,R. and Yang,L.
  TITLE     Camk2a suppresses denervated muscle atrophy by maintaining the Ca2+
            homeostasis in muscle cells
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (11), 25-29 (2023)
   PUBMED   38015546
  REMARK    GeneRIF: Camk2a suppresses denervated muscle atrophy by maintaining
            the Ca2+ homeostasis in muscle cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Alphonse,N., Wanford,J.J., Voak,A.A., Gay,J., Venkhaya,S.,
            Burroughs,O., Mathew,S., Lee,T., Evans,S.L., Zhao,W., Frowde,K.,
            Alrehaili,A., Dickenson,R.E., Munk,M., Panina,S., Mahmood,I.F.,
            Llorian,M., Stanifer,M.L., Boulant,S., Berchtold,M.W.,
            Bergeron,J.R.C., Wack,A., Lesser,C.F. and Odendall,C.
  TITLE     A family of conserved bacterial virulence factors dampens
            interferon responses by blocking calcium signaling
  JOURNAL   Cell 185 (13), 2354-2369 (2022)
   PUBMED   35568036
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Bredt,D.S., Ferris,C.D. and Snyder,S.H.
  TITLE     Nitric oxide synthase regulatory sites. Phosphorylation by cyclic
            AMP-dependent protein kinase, protein kinase C, and
            calcium/calmodulin protein kinase; identification of flavin and
            calmodulin binding sites
  JOURNAL   J Biol Chem 267 (16), 10976-10981 (1992)
   PUBMED   1375933
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Omary,M.B., Baxter,G.T., Chou,C.F., Riopel,C.L., Lin,W.Y. and
            Strulovici,B.
  TITLE     PKC epsilon-related kinase associates with and phosphorylates
            cytokeratin 8 and 18
  JOURNAL   J Cell Biol 117 (3), 583-593 (1992)
   PUBMED   1374067
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Wegner,M., Cao,Z. and Rosenfeld,M.G.
  TITLE     Calcium-regulated phosphorylation within the leucine zipper of
            C/EBP beta
  JOURNAL   Science 256 (5055), 370-373 (1992)
   PUBMED   1314426
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Tokui,T., Yamauchi,T., Yano,T., Nishi,Y., Kusagawa,M., Yatani,R.
            and Inagaki,M.
  TITLE     Ca2(+)-calmodulin-dependent protein kinase II phosphorylates
            various types of non-epithelial intermediate filament proteins
  JOURNAL   Biochem Biophys Res Commun 169 (3), 896-904 (1990)
   PUBMED   2114109
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB023185.1, BF951952.1,
            AC011372.7 and BC040457.1.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinases family, and to the Ca(2+)/calmodulin-dependent
            protein kinases subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. This calcium
            calmodulin-dependent protein kinase is composed of four different
            chains: alpha, beta, gamma, and delta. The alpha chain encoded by
            this gene is required for hippocampal long-term potentiation (LTP)
            and spatial learning. In addition to its calcium-calmodulin
            (CaM)-dependent activity, this protein can undergo
            autophosphorylation, resulting in CaM-independent activity. Several
            transcript variants encoding distinct isoforms have been identified
            for this gene. [provided by RefSeq, Jun 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB023185.1, BC040457.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..478
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit alpha isoform 2"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II alpha; CaM-kinase II alpha chain;
                     calcium/calmodulin-dependent protein kinase II alpha-B
                     subunit; CaM kinase II alpha subunit; CaMK-II alpha
                     subunit; calcium/calmodulin-dependent protein kinase type
                     II alpha chain; calcium/calmodulin-dependent protein
                     kinase type II subunit alpha; caMK-II subunit alpha; caM
                     kinase II subunit alpha"
                     /calculated_mol_wt=53957
     Region          11..302
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Site            order(19..23,27,40,42,73,89..92,96,98,134..135,137,
                     139..140,142,155..156,159,174..178,180)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(19..22,27,40,42,73,89..92,96,139..140,142,155..156)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(23,96,98,134..135,137,139,159,174..178,180)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(155..165,168..178)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11275; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P11275; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Region          290..300
                     /region_name="calmodulin-binding domain"
     Site            order(293,295..302)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          310..320
                     /region_name="Interaction with BAALC.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Region          314..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     Region          346..473
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11798; propagated from
                     UniProtKB/Swiss-Prot (Q9UQM7.2)"
     CDS             1..478
                     /gene="CAMK2A"
                     /gene_synonym="CAMKA; CaMKIIalpha; CaMKIINalpha; MRD53;
                     MRT63"
                     /coded_by="NM_171825.3:149..1585"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43386.1"
                     /db_xref="GeneID:815"
                     /db_xref="HGNC:HGNC:1460"
                     /db_xref="MIM:114078"
ORIGIN      
        1 matitctrft eeyqlfeelg kgafsvvrrc vkvlagqeya akiintkkls ardhqklere
       61 aricrllkhp nivrlhdsis eeghhylifd lvtggelfed ivareyysea dashciqqil
      121 eavlhchqmg vvhrdlkpen lllasklkga avkladfgla ievegeqqaw fgfagtpgyl
      181 spevlrkdpy gkpvdlwacg vilyillvgy ppfwdedqhr lyqqikagay dfpspewdtv
      241 tpeakdlink mltinpskri taaealkhpw ishrstvasc mhrqetvdcl kkfnarrklk
      301 gailttmlat rnfsggksgg nkksdgvkes sestnttied edtkvrkqei ikvteqliea
      361 isngdfesyt kmcdpgmtaf epealgnlve gldfhrfyfe nlwsrnskpv httilnphih
      421 lmgdesacia yiritqylda ggiprtaqse etrvwhrrdg kwqivhfhrs gapsvlph
//
LOCUS       NP_001116142            1210 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphorylase b kinase regulatory subunit alpha, skeletal muscle
            isoform isoform 2 [Homo sapiens].
ACCESSION   NP_001116142
VERSION     NP_001116142.1
DBSOURCE    REFSEQ: accession NM_001122670.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1210)
  AUTHORS   Yang,X., Zhu,M., Lu,X., Wang,Y. and Xiao,J.
  TITLE     Architecture and activation of human muscle phosphorylase kinase
  JOURNAL   Nat Commun 15 (1), 2719 (2024)
   PUBMED   38548794
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1210)
  AUTHORS   Bisciglia,M., Froissart,R., Bedat-Millet,A.L., Romero,N.B.,
            Pettazzoni,M., Hogrel,J.Y., Petit,F.M. and Stojkovic,T.
  TITLE     A novel PHKA1 mutation associating myopathy and cognitive
            impairment: Expanding the spectrum of phosphorylase kinase b (PhK)
            deficiency
  JOURNAL   J Neurol Sci 424, 117391 (2021)
   PUBMED   33799212
  REMARK    GeneRIF: A novel PHKA1 mutation associating myopathy and cognitive
            impairment: Expanding the spectrum of phosphorylase kinase b (PhK)
            deficiency.
REFERENCE   3  (residues 1 to 1210)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1210)
  AUTHORS   Preisler,N., Orngreen,M.C., Echaniz-Laguna,A., Laforet,P.,
            Lonsdorfer-Wolf,E., Doutreleau,S., Geny,B., Akman,H.O., Dimauro,S.
            and Vissing,J.
  TITLE     Muscle phosphorylase kinase deficiency: a neutral metabolic variant
            or a disease?
  JOURNAL   Neurology 78 (4), 265-268 (2012)
   PUBMED   22238410
  REMARK    GeneRIF: muscle PHKA deficiency may present as an almost
            asymptomatic condition, despite a mild impairment of muscle
REFERENCE   5  (residues 1 to 1210)
  AUTHORS   Echaniz-Laguna,A., Akman,H.O., Mohr,M., Tranchant,C.,
            Talmant-Verbist,V., Rolland,M.O. and Dimauro,S.
  TITLE     Muscle phosphorylase b kinase deficiency revisited
  JOURNAL   Neuromuscul Disord 20 (2), 125-127 (2010)
   PUBMED   20080404
REFERENCE   6  (residues 1 to 1210)
  AUTHORS   Gossen,M., Wullrich,A. and Kilimann,M.W.
  TITLE     Dinucleotide repeat polymorphism within the PHKA1 gene at Xq12-q13
  JOURNAL   Hum Genet 95 (4), 469-470 (1995)
   PUBMED   7705849
REFERENCE   7  (residues 1 to 1210)
  AUTHORS   Wehner,M., Clemens,P.R., Engel,A.G. and Kilimann,M.W.
  TITLE     Human muscle glycogenosis due to phosphorylase kinase deficiency
            associated with a nonsense mutation in the muscle isoform of the
            alpha subunit
  JOURNAL   Hum Mol Genet 3 (11), 1983-1987 (1994)
   PUBMED   7874115
REFERENCE   8  (residues 1 to 1210)
  AUTHORS   Herbert,M., Goldstein,J.L., Rehder,C., Austin,S., Kishnani,P.S. and
            Bali,D.S.
  TITLE     Phosphorylase Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21634085
REFERENCE   9  (residues 1 to 1210)
  AUTHORS   Meyer,H.E., Meyer,G.F., Dirks,H. and Heilmeyer,L.M. Jr.
  TITLE     Localization of phosphoserine residues in the alpha subunit of
            rabbit skeletal muscle phosphorylase kinase
  JOURNAL   Eur J Biochem 188 (2), 367-376 (1990)
   PUBMED   2108025
REFERENCE   10 (residues 1 to 1210)
  AUTHORS   Francke,U., Darras,B.T., Zander,N.F. and Kilimann,M.W.
  TITLE     Assignment of human genes for phosphorylase kinase subunits alpha
            (PHKA) to Xq12-q13 and beta (PHKB) to 16q12-q13
  JOURNAL   Am J Hum Genet 45 (2), 276-282 (1989)
   PUBMED   2757032
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC240504.3, DR002787.1,
            BC104944.1, X73874.1, BJ998054.1, BX647542.1 and AW450116.1.
            
            Summary: Phosphorylase kinase is a polymer of 16 subunits, four
            each of alpha, beta, gamma and delta. The alpha subunit includes
            the skeletal muscle and hepatic isoforms, and the skeletal muscle
            isoform is encoded by this gene. The beta subunit is the same in
            both the muscle and hepatic isoforms, and encoded by one gene. The
            gamma subunit also includes the skeletal muscle and hepatic
            isoforms, which are encoded by two different genes. The delta
            subunit is a calmodulin and can be encoded by three different
            genes. The gamma subunits contain the active site of the enzyme,
            whereas the alpha and beta subunits have regulatory functions
            controlled by phosphorylation. The delta subunit mediates the
            dependence of the enzyme on calcium concentration. Mutations in
            this gene cause glycogen storage disease type 9D, also known as
            X-linked muscle glycogenosis. Alternatively spliced transcript
            variants encoding different isoforms have been identified in this
            gene. A pseudogene has been found on chromosome 1.[provided by
            RefSeq, Feb 2010].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 3' coding region, compared to variant 1, resulting in a
            shorter protein (isoform 2), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.797814.1,
                                           SRR11853566.29841.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..1210
                     /product="phosphorylase b kinase regulatory subunit alpha,
                     skeletal muscle isoform isoform 2"
                     /EC_number="2.7.11.19"
                     /note="phosphorylase kinase, alpha 1 (muscle), muscle
                     glycogenosis; phosphorylase kinase alpha M subunit"
                     /calculated_mol_wt=135678
     Region          8..>439
                     /region_name="Glyco_hydro_15"
                     /note="Glycosyl hydrolases family 15; pfam00723"
                     /db_xref="CDD:395586"
     Site            629
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64649; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Site            735
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Site            758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Region          <804..922
                     /region_name="Bac_rhamnosid6H"
                     /note="Bacterial alpha-L-rhamnosidase 6 hairpin
                     glycosidase domain; cl46875"
                     /db_xref="CDD:481215"
     Region          810..840
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P46020.2)"
     Region          933..>1121
                     /region_name="KPBB_C"
                     /note="Phosphorylase b kinase C-terminal domain;
                     pfam19292"
                     /db_xref="CDD:437124"
     Site            972
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46020.2)"
     Site            981
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Site            985
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46020.2)"
     Site            1007
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P18688; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Region          1033..1073
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P46020.2)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64649; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     CDS             1..1210
                     /gene="PHKA1"
                     /gene_synonym="PHKA"
                     /coded_by="NM_001122670.2:427..4059"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS48137.1"
                     /db_xref="GeneID:5255"
                     /db_xref="HGNC:HGNC:8925"
                     /db_xref="MIM:311870"
ORIGIN      
        1 mrsrsnsgvr ldgyarlvqq tilchqnpvt gllpasydqk dawvrdnvys ilavwglgla
       61 yrknadrded kakayeleqs vvklmrgllh cmirqvdkve sfkysqstkd slhakyntkt
      121 catvvgddqw ghlqldatsv yllflaqmta sglhiihsld evnfiqnlvf yieaayktad
      181 fgiwergdkt nqgiselnas svgmakaale aldeldlfgv kggpqsvihv ladevqhcqs
      241 ilnsllpras tskevdasll svvsfpafav edsqlveltk qeiitklqgr ygccrflrdg
      301 yktpkedpnr lyyepaelkl feniecewpl fwtyfildgv fsgnaeqvqe ykealeavli
      361 kgkngvpllp elysvppdrv deeyqnphtv drvpmgklph mwgqslyilg slmaegflap
      421 geidplnrrf stvpkpdvvv qvsilaetee iktilkdkgi yvetiaevyp irvqparils
      481 hiysslgcnn rmklsgrpyr hmgvlgtskl ydirktiftf tpqfidqqqf ylaldnkmiv
      541 emlrtdlsyl csrwrmtgqp titfpishsm ldedgtslns silaalrkmq dgyfggarvq
      601 tgklsefltt sccthlsfmd pgpegklyse dyddnydyle sgnwmndyds tsharcgdev
      661 aryldhllah taphpklapt sqkggldrfq aavqttcdlm slvtkakelh vqnvhmylpt
      721 klfqasrpsf nlldsphprq enqvpsvrve ihlprdqsge vdfkalvlql ketsslqeqa
      781 dilymlytmk gpdwntelyn ersatvrell telygkvgei rhwgliryis gilrkkveal
      841 deactdllsh qkhltvglpp eprektisap lpyealtqli deasegdmsi siltqeimvy
      901 lamymrtqpg lfaemfrlri gliiqvmate lahslrcsae eateglmnls psamknllhh
      961 ilsgkefgve rsvrptdsnv spaisiheig avgatktert gimqlkseik qspgtsmtps
     1021 sgsfpsaydq qsskdsrqgq wqrrrrldga lnrvpvgfyq kvwkvlqkch glsvegfvlp
     1081 ssttremtpg eikfsvhves vlnrvpqpey rqllveailv ltmladieih sigsiiavek
     1141 ivhiandlfl qeqktlgadd tmlakdpasg ictllydsap sgrfgtmtyl skaaatyvqe
     1201 flphsicamq
//
LOCUS       NP_001387089            1225 aa            linear   PRI 21-NOV-2025
DEFINITION  protein transport protein Sec31A isoform 11 [Homo sapiens].
ACCESSION   NP_001387089
VERSION     NP_001387089.1
DBSOURCE    REFSEQ: accession NM_001400160.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1225)
  AUTHORS   Tobias,E.S., Lucas-Herald,A.K., Sagar,D., Montezano,A.C.,
            Rios,F.J., De Lucca Camargo,L., Hamilton,G., Gazdagh,G.,
            Diver,L.A., Williams,N., Herzyk,P., Touyz,R.M., Greenfield,A.,
            McGowan,R. and Ahmed,S.F.
  TITLE     SEC31A may be associated with pituitary hormone deficiency and
            gonadal dysgenesis
  JOURNAL   Endocrine 84 (2), 345-349 (2024)
   PUBMED   38400880
  REMARK    GeneRIF: SEC31A may be associated with pituitary hormone deficiency
            and gonadal dysgenesis.
REFERENCE   2  (residues 1 to 1225)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1225)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1225)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1225)
  AUTHORS   Jin,L., Pahuja,K.B., Wickliffe,K.E., Gorur,A., Baumgartel,C.,
            Schekman,R. and Rape,M.
  TITLE     Ubiquitin-dependent regulation of COPII coat size and function
  JOURNAL   Nature 482 (7386), 495-500 (2012)
   PUBMED   22358839
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1225)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1225)
  AUTHORS   Kim,J.H., Hong,J.A., Pih,K.T. and Hwang,I.
  TITLE     Identification and isolation of differentially expressed genes in
            osmotically stressed human oral keratinocytes
  JOURNAL   Arch Oral Biol 46 (4), 335-341 (2001)
   PUBMED   11269867
REFERENCE   8  (residues 1 to 1225)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 1225)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   10 (residues 1 to 1225)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021105.13 and AC108469.5.
            
            Summary: The protein encoded by this gene shares similarity with
            the yeast Sec31 protein, and is a component of the outer layer of
            the coat protein complex II (COPII). The encoded protein is
            involved in vesicle budding from the endoplasmic reticulum (ER) and
            contains multiple WD repeats near the N-terminus and a proline-rich
            region in the C-terminal half. It associates with the protein
            encoded by the SEC13 homolog, nuclear pore and COPII coat complex
            component (SEC13), and is required for ER-Golgi transport.
            Monoubiquitylation of this protein by CUL3-KLHL12 was found to
            regulate the size of COPII coats to accommodate unusually shaped
            cargo. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1781116.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..1225
                     /product="protein transport protein Sec31A isoform 11"
                     /note="yeast Sec31p homolog; protein transport protein
                     Sec31A; web1-like protein; SEC31 homolog A, COPII coat
                     complex component; SEC31-related protein A; SEC31-like
                     protein 1; SEC31 homolog A, COPII coating complex
                     component"
                     /calculated_mol_wt=133397
     Region          13..332
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(26,40,46..47,52..53,91,95,101..102,117,121,139,144,
                     150..151,164,185,190,196..197,209..210,231,235,244..245,
                     258..259,277,282,288..289,301..302,320,325,331..332)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          70..119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          125..162
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          172..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          263..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          306..331
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <547..>670
                     /region_name="ACE1-Sec16-like"
                     /note="Ancestral coatomer element 1 (ACE1) of COPII coat
                     complex assembly protein Sec16; cl14807"
                     /db_xref="CDD:449359"
     Site            order(548..552,554,556,567,569,570..571,573..574,578,584,
                     592,604,607,632..633)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187750"
     Region          750..>1103
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     CDS             1..1225
                     /gene="SEC31A"
                     /gene_synonym="ABP125; ABP130; HPBKS; HSPC275; HSPC334;
                     NEDSOSB; SEC31L1"
                     /coded_by="NM_001400160.1:320..3997"
                     /note="isoform 11 is encoded by transcript variant 17"
                     /db_xref="GeneID:22872"
                     /db_xref="HGNC:HGNC:17052"
                     /db_xref="MIM:610257"
ORIGIN      
        1 mklkevdrta mqawspaqnh piylatgtsa qqldatfstn asleifeldl sdpsldmksc
       61 atfssshryh kliwgpykmd skgdvsgvli aggengniil ydpskiiagd kevviaqndk
      121 htgpvraldv nifqtnlvas ganeseiyiw dlnnfatpmt pgaktqpped isciawnrqv
      181 qhilasasps gratvwdlrk nepiikvsdh snrmhcsgla whpdvatqmv laseddrlpv
      241 iqmwdlrfas splrvlenha rgilaiawsm adpelllscg kdakilcsnp ntgevlyelp
      301 tntqwcfdiq wcprnpavls aasfdgrisv ysimggstdg lrqkqvdkls ssfgnldpfg
      361 tgqplpplqi pqqtaqhsiv lplkkppkwi rrpvgasfsf ggklvtfenv rmpshqgaeq
      421 qqqqhhvfis qvvtekefls rsdqlqqavq sqgfinycqk kidasqtefe knvwsflkvn
      481 feddsrgkyl ellgyrkedl gkkialalnk vdganvhike ekeeseflps sggtfnisvs
      541 gdidglitqa lltgnfesav dlclhdnrma daiilaiagg qellartqkk yfaksqskit
      601 rlitavvmkn wkeivescdl knwrealaav ltyakpdefs alcdllgtrl enegdsllqt
      661 qaclcyicag nveklvacwt kaqdgshpls lqdliekvvi lrkavqltqa mdtstvgvll
      721 aakmsqyanl laaqgsiaaa laflpdntnq pnimqlrdrl craqgepvag hespkipyek
      781 qqlpkgrpgp vaghhqmprv qtqqyyphvr iaptvttwsn ktptalpshp paaspsdtqg
      841 enppppgfim hgnvnpnaag qlptspghmh tqvppypqpq pyqpaqpypf gtggsamyrp
      901 qqpvapptsn aypntpyiss assytgqsql yaaqhqassp tsspatsfpp ppssgasfqh
      961 ggpgappsss ayalppgttg tlpaaselpa sqrtgpqngw ndppalnrvp kkkkmpenfm
     1021 ppvpitspim nplgdpqsqm lqqqpsapvp lssqssfpqp hlpggqpfhg vqqplgqtgm
     1081 ppsfskpnie gapgapignt fqhvqslptk kitkkpipde hlilkttfed liqrclssat
     1141 dpqtkrkldd askrleflyd klreqtlspt itsglhniar sietrnyseg ltmhthivst
     1201 snfsetsafm pvlkvvltqa nklgv
//
LOCUS       NP_001340975             862 aa            linear   PRI 21-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 7 isoform i [Homo sapiens].
ACCESSION   NP_001340975
VERSION     NP_001340975.1
DBSOURCE    REFSEQ: accession NM_001354046.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 862)
  AUTHORS   Kawase,N., Sugihara,A., Kajiwara,K., Hiroshima,M., Akamatsu,K.,
            Nada,S., Matsumoto,K., Ueda,M. and Okada,M.
  TITLE     SRC kinase activator CDCP1 promotes hepatocyte growth
            factor-induced cell migration/invasion of a subset of breast cancer
            cells
  JOURNAL   J Biol Chem 298 (3), 101630 (2022)
   PUBMED   35085554
  REMARK    GeneRIF: SRC kinase activator CDCP1 promotes hepatocyte growth
            factor-induced cell migration/invasion of a subset of breast cancer
            cells.
REFERENCE   4  (residues 1 to 862)
  AUTHORS   Keum,S., Yang,S.J., Park,E., Kang,T., Choi,J.H., Jeong,J.,
            Hwang,Y.E., Kim,J.W., Park,D. and Rhee,S.
  TITLE     Beta-Pix-dynamin 2 complex promotes colorectal cancer progression
            by facilitating membrane dynamics
  JOURNAL   Cell Oncol (Dordr) 44 (6), 1287-1305 (2021)
   PUBMED   34582006
  REMARK    GeneRIF: Beta-Pix-dynamin 2 complex promotes colorectal cancer
            progression by facilitating membrane dynamics.
REFERENCE   5  (residues 1 to 862)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 862)
  AUTHORS   Turner,C.E., Brown,M.C., Perrotta,J.A., Riedy,M.C.,
            Nikolopoulos,S.N., McDonald,A.R., Bagrodia,S., Thomas,S. and
            Leventhal,P.S.
  TITLE     Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin
            repeat, ARF-GAP protein: A role in cytoskeletal remodeling
  JOURNAL   J Cell Biol 145 (4), 851-863 (1999)
   PUBMED   10330411
REFERENCE   7  (residues 1 to 862)
  AUTHORS   Aghazadeh,B., Zhu,K., Kubiseski,T.J., Liu,G.A., Pawson,T., Zheng,Y.
            and Rosen,M.K.
  TITLE     Structure and mutagenesis of the Dbl homology domain
  JOURNAL   Nat Struct Biol 5 (12), 1098-1107 (1998)
   PUBMED   9846881
REFERENCE   8  (residues 1 to 862)
  AUTHORS   Bagrodia,S., Taylor,S.J., Jordon,K.A., Van Aelst,L. and
            Cerione,R.A.
  TITLE     A novel regulator of p21-activated kinases
  JOURNAL   J Biol Chem 273 (37), 23633-23636 (1998)
   PUBMED   9726964
REFERENCE   9  (residues 1 to 862)
  AUTHORS   Manser,E., Loo,T.H., Koh,C.G., Zhao,Z.S., Chen,X.Q., Tan,L.,
            Tan,I., Leung,T. and Lim,L.
  TITLE     PAK kinases are directly coupled to the PIX family of nucleotide
            exchange factors
  JOURNAL   Mol Cell 1 (2), 183-192 (1998)
   PUBMED   9659915
REFERENCE   10 (residues 1 to 862)
  AUTHORS   Oh,W.K., Yoo,J.C., Jo,D., Song,Y.H., Kim,M.G. and Park,D.
  TITLE     Cloning of a SH3 domain-containing proline-rich protein, p85SPR,
            and its localization in focal adhesion
  JOURNAL   Biochem Biophys Res Commun 235 (3), 794-798 (1997)
   PUBMED   9207241
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL353704.10, AL390754.18 and
            AL139086.12.
            
            Summary: This gene encodes a protein that belongs to a family of
            cytoplasmic proteins that activate the Ras-like family of Rho
            proteins by exchanging bound GDP for GTP. It forms a complex with
            the small GTP binding protein Rac1 and recruits Rac1 to membrane
            ruffles and to focal adhesions. Multiple alternatively spliced
            transcript variants encoding different isoforms have been observed
            for this gene. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (12) encodes the longest isoform
            (i).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.57737.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000646102.2/ ENSP00000495631.1
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..862
                     /product="rho guanine nucleotide exchange factor 7 isoform
                     i"
                     /note="SH3 domain-containing proline-rich protein;
                     PAK-interacting exchange factor beta; Rho guanine
                     nucleotide exchange factor (GEF) 7"
                     /calculated_mol_wt=97022
     Region          3..115
                     /region_name="CH_betaPIX"
                     /note="calponin homology (CH) domain found in beta-Pak
                     Interactive eXchange factor; cd21266"
                     /db_xref="CDD:409115"
     Site            order(3,7,65,67..68,71..72,74,82..90,96,98..99,101..102,
                     105..106,109)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409115"
     Region          117..163
                     /region_name="RhoGEF67_u1"
                     /note="Unstructured region one on RhoGEF 6 and 7;
                     pfam16615"
                     /db_xref="CDD:465201"
     Region          167..220
                     /region_name="SH3_betaPIX"
                     /note="Src Homology 3 domain of beta-Pak Interactive
                     eXchange factor; cd12061"
                     /db_xref="CDD:212994"
     Site            order(172,174,177,180..181,196,198..200,211,213,215..216)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212994"
     Region          251..428
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(257,261,355,379..380,383..384,386..387,390..391,
                     394..395,398,424,428)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          459..557
                     /region_name="PH_Cool_Pix"
                     /note="Cloned out of library/PAK-interactive exchange
                     factor pleckstrin homology (PH) domain; cd01225"
                     /db_xref="CDD:269932"
     Region          617..707
                     /region_name="RhoGEF67_u2"
                     /note="Unstructured region two on RhoGEF 6 and 7;
                     pfam16614"
                     /db_xref="CDD:465200"
     Region          777..861
                     /region_name="betaPIX_CC"
                     /note="betaPIX coiled coil; pfam16523"
                     /db_xref="CDD:465158"
     CDS             1..862
                     /gene="ARHGEF7"
                     /gene_synonym="BETA-PIX; COOL-1; COOL1; Nbla10314; P50;
                     P50BP; P85; P85COOL1; P85SPR; PAK3; PIXB"
                     /coded_by="NM_001354046.2:218..2806"
                     /note="isoform i is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS86360.1"
                     /db_xref="GeneID:8874"
                     /db_xref="HGNC:HGNC:15607"
                     /db_xref="MIM:605477"
ORIGIN      
        1 mnsaeqtvtw litlgvlesp kktisdpegf lqaslkdgvv lcrllerllp gtiekvypep
       61 rseseclsni reflrgcgas lrletfdand lyqgqnfnkv lsslvtlnkv tadiglgsds
      121 vcarpsshri ksfdslgsqs lhtrtsklfq gqyrsldmtd nsnnqlvvra kfnfqqtned
      181 elsfskgdvi hvtrveeggw wegtlngrtg wfpsnyvrev kasekpvspk sgtlksppkg
      241 fdttainksy ynvvlqnile teneyskelq tvlstylrpl qtseklssan isylmgnlee
      301 icsfqqmlvq sleectklpe aqqrvggcfl nlmpqmktly ltycanhpsa vnvltehsee
      361 lgefmetkga sspgilvltt glskpfmrld kyptllkele rhmedyhtdr qdiqksmaaf
      421 knlsaqcqev rkrkelelqi lteairnweg ddiktlgnvt ymsqvliqca gseekneryl
      481 llfpnvllml sasprmsgfi yqgklpttgm titkledsen hrnafeisgs mierilvscn
      541 nqqdlqewve hlqkqtkvts vgnptikphs vpshtlpshp vtpsskhads kpapltpayh
      601 tlphpshhgt phttinwgpl eppktpkpws lsclrpappl rpsaalcyke dlskspktmk
      661 kllpkrkper kpsdeefasr kstaaleeda qilkvieayc tsaktrqtln stwqgtdlmh
      721 nhvladddqp sldslgrrss lsrlepsdls edsdydsiwt ahsyrmgsts rsrkesapqv
      781 llpeeekiiv eetksngqtv ieekslvdtv yalkdevqel rqdnkkmkks leeeqrarkd
      841 leklvrkvlk nmndpawdet nl
//
LOCUS       NP_001124150             237 aa            linear   PRI 21-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4E isoform 3 [Homo
            sapiens].
ACCESSION   NP_001124150
VERSION     NP_001124150.1
DBSOURCE    REFSEQ: accession NM_001130678.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Nicholson-Shaw,T., Dowdle,M.E., Ajaj,Y., Perelis,M., Fulzele,A.,
            Yeo,G.W., Bennett,E.J. and Lykke-Andersen,J.
  TITLE     Human CCR4 deadenylase homolog Angel1 is a non-stop mRNA decay
            factor
  JOURNAL   RNA 31 (8), 1195-1205 (2025)
   PUBMED   40441874
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Yang,G., Smibert,C.A., Kaplan,D.R. and Miller,F.D.
  TITLE     An eIF4E1/4E-T complex determines the genesis of neurons from
            precursors by translationally repressing a proneurogenic
            transcription program
  JOURNAL   Neuron 84 (4), 723-739 (2014)
   PUBMED   25456498
  REMARK    GeneRIF: neural precursors are transcriptionally primed to generate
            neurons, but an eIF4E/4E-T complex sequesters and represses
            translation of proneurogenic proteins to determine appropriate
            neurogenesis.
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Feoktistova,K., Tuvshintogs,E., Do,A. and Fraser,C.S.
  TITLE     Human eIF4E promotes mRNA restructuring by stimulating eIF4A
            helicase activity
  JOURNAL   Proc Natl Acad Sci U S A 110 (33), 13339-13344 (2013)
   PUBMED   23901100
  REMARK    GeneRIF: Human eIF4E promotes mRNA restructuring by stimulating
            eIF4A helicase activity.
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Xu,X., Vatsyayan,J., Gao,C., Bakkenist,C.J. and Hu,J.
  TITLE     Sumoylation of eIF4E activates mRNA translation
  JOURNAL   EMBO Rep 11 (4), 299-304 (2010)
   PUBMED   20224576
  REMARK    GeneRIF: The findings suggest further that eIF4E sumoylation is a
            new fundamental regulatory mechanism of protein synthesis and might
            be important in promoting human cancers.
REFERENCE   6  (residues 1 to 237)
  AUTHORS   Brown,C.J., McNae,I., Fischer,P.M. and Walkinshaw,M.D.
  TITLE     Crystallographic and mass spectrometric characterisation of eIF4E
            with N7-alkylated cap derivatives
  JOURNAL   J Mol Biol 372 (1), 7-15 (2007)
   PUBMED   17631896
  REMARK    GeneRIF: Crystallographic and mass spectrometric characterisation
            of eIF4E with N7-alkylated cap derivatives.
            Review article
REFERENCE   7  (residues 1 to 237)
  AUTHORS   Tomoo,K., Shen,X., Okabe,K., Nozoe,Y., Fukuhara,S., Morino,S.,
            Ishida,T., Taniguchi,T., Hasegawa,H., Terashima,A., Sasaki,M.,
            Katsuya,Y., Kitamura,K., Miyoshi,H., Ishikawa,M. and Miura,K.
  TITLE     Crystal structures of 7-methylguanosine 5'-triphosphate (m(7)GTP)-
            and P(1)-7-methylguanosine-P(3)-adenosine-5',5'-triphosphate
            (m(7)GpppA)-bound human full-length eukaryotic initiation factor
            4E: biological importance of the C-terminal flexible region
  JOURNAL   Biochem J 362 (Pt 3), 539-544 (2002)
   PUBMED   11879179
  REMARK    GeneRIF: The crystal structures of the full-length human eukaryotic
            initiation factor (eIF) 4E complexed with two mRNA cap analogues
REFERENCE   8  (residues 1 to 237)
  AUTHORS   Lejbkowicz,F., Goyer,C., Darveau,A., Neron,S., Lemieux,R. and
            Sonenberg,N.
  TITLE     A fraction of the mRNA 5' cap-binding protein, eukaryotic
            initiation factor 4E, localizes to the nucleus
  JOURNAL   Proc Natl Acad Sci U S A 89 (20), 9612-9616 (1992)
   PUBMED   1384058
REFERENCE   9  (residues 1 to 237)
  AUTHORS   Ueda,H., Iyo,H., Doi,M., Inoue,M., Ishida,T., Morioka,H.,
            Tanaka,T., Nishikawa,S. and Uesugi,S.
  TITLE     Combination of Trp and Glu residues for recognition of mRNA cap
            structure. Analysis of m7G base recognition site of human cap
            binding protein (IF-4E) by site-directed mutagenesis
  JOURNAL   FEBS Lett 280 (2), 207-210 (1991)
   PUBMED   1672854
REFERENCE   10 (residues 1 to 237)
  AUTHORS   Rychlik,W., Domier,L.L., Gardner,P.R., Hellmann,G.M. and
            Rhoads,R.E.
  TITLE     Amino acid sequence of the mRNA cap-binding protein from human
            tissues
  JOURNAL   Proc Natl Acad Sci U S A 84 (4), 945-949 (1987)
   PUBMED   3469651
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1992 Feb 1;89(3):1148. doi:
            10.1073/pnas.89.3.1148a. PMID: 1736299]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC019131.7, DC388666.1,
            BC107715.1 and AC093836.3.
            
            Summary: The protein encoded by this gene is a component of the
            eukaryotic translation initiation factor 4F complex, which
            recognizes the 7-methylguanosine cap structure at the 5' end of
            messenger RNAs. The encoded protein aids in translation initiation
            by recruiting ribosomes to the 5'-cap structure. Association of
            this protein with the 4F complex is the rate-limiting step in
            translation initiation. This gene acts as a proto-oncogene, and its
            expression and activation is associated with transformation and
            tumorigenesis. Several pseudogenes of this gene are found on other
            chromosomes. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (3) uses an alternate 5'-terminal
            exon, which results in a different 5' UTR and use of an alternate
            translation start codon compared to variant 1. It encodes isoform
            3, which has a distinct N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because transcript sequence consistent with
            the reference genome assembly was not available for all regions of
            the RefSeq transcript. The extent of this transcript is supported
            by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.273343.1, AK300982.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..237
                     /product="eukaryotic translation initiation factor 4E
                     isoform 3"
                     /note="mRNA cap-binding protein; eIF-4F 25 kDa subunit;
                     eukaryotic translation initiation factor 4E-like 1"
                     /calculated_mol_wt=27129
     Region          58..217
                     /region_name="IF4E"
                     /note="Eukaryotic initiation factor 4E; pfam01652"
                     /db_xref="CDD:460281"
     CDS             1..237
                     /gene="EIF4E"
                     /gene_synonym="AUTS19; CBP; eIF-4E; EIF4E1; EIF4EL1;
                     EIF4F"
                     /coded_by="NM_001130678.4:162..875"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS47109.1"
                     /db_xref="GeneID:1977"
                     /db_xref="HGNC:HGNC:3287"
                     /db_xref="MIM:133440"
ORIGIN      
        1 mldltsrgqv gtsrrmaeaa csahflettp tpnpptteee ktesnqevan pehyikhplq
       61 nrwalwffkn dksktwqanl rliskfdtve dfwalynhiq lssnlmpgcd yslfkdgiep
      121 mwedeknkrg grwlitlnkq qrrsdldrfw letllclige sfddysddvc gavvnvrakg
      181 dkiaiwttec enreavthig rvykerlglp pkivigyqsh adtatksgst tknrfvv
//
LOCUS       NP_733779                163 aa            linear   PRI 21-NOV-2025
DEFINITION  S-phase kinase-associated protein 1 isoform b [Homo sapiens].
ACCESSION   NP_733779
VERSION     NP_733779.1
DBSOURCE    REFSEQ: accession NM_170679.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Luo,C., Chen,Z., Meng,L., Tan,C., He,W., Tu,C., Du,J., Lu,G.X.,
            Lin,G., Tan,Y.Q. and Hu,T.Y.
  TITLE     A hemizygous loss-of-function variant in BCORL1 is associated with
            male infertility and oligoasthenoteratozoospermia
  JOURNAL   Clin Genet 106 (1), 27-36 (2024)
   PUBMED   38342987
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Chen,Z., Li,Y., He,K., Yang,J., Deng,Q., Chen,Y. and Fu,Z.
  TITLE     CircGPRC5A enhances colorectal cancer progress by stabilizing
            PPP1CA and inducing YAP dephosphorylation
  JOURNAL   J Exp Clin Cancer Res 42 (1), 334 (2023)
   PUBMED   38057879
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Li,J., Krause,G.J., Gui,Q., Kaushik,S., Rona,G., Zhang,Q.,
            Liang,F.X., Dhabaria,A., Anerillas,C., Martindale,J.L.,
            Vasilyev,N., Askenazi,M., Ueberheide,B., Nudler,E., Gorospe,M.,
            Cuervo,A.M. and Pagano,M.
  TITLE     A noncanonical function of SKP1 regulates the switch between
            autophagy and unconventional secretion
  JOURNAL   Sci Adv 9 (41), eadh1134 (2023)
   PUBMED   37831778
  REMARK    GeneRIF: A noncanonical function of SKP1 regulates the switch
            between autophagy and unconventional secretion.
REFERENCE   5  (residues 1 to 163)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 163)
  AUTHORS   Bai,C., Sen,P., Hofmann,K., Ma,L., Goebl,M., Harper,J.W. and
            Elledge,S.J.
  TITLE     SKP1 connects cell cycle regulators to the ubiquitin proteolysis
            machinery through a novel motif, the F-box
  JOURNAL   Cell 86 (2), 263-274 (1996)
   PUBMED   8706131
REFERENCE   7  (residues 1 to 163)
  AUTHORS   Demetrick,D.J., Zhang,H. and Beach,D.H.
  TITLE     Chromosomal mapping of the genes for the human CDK2/cyclin
            A-associated proteins p19 (SKP1A and SKP1B) and p45 (SKP2)
  JOURNAL   Cytogenet Cell Genet 73 (1-2), 104-107 (1996)
   PUBMED   8646875
REFERENCE   8  (residues 1 to 163)
  AUTHORS   Zhang,H., Kobayashi,R., Galaktionov,K. and Beach,D.
  TITLE     p19Skp1 and p45Skp2 are essential elements of the cyclin A-CDK2 S
            phase kinase
  JOURNAL   Cell 82 (6), 915-925 (1995)
   PUBMED   7553852
REFERENCE   9  (residues 1 to 163)
  AUTHORS   Sowden,J., Morrison,K., Schofield,J., Putt,W. and Edwards,Y.
  TITLE     A novel cDNA with homology to an RNA polymerase II elongation
            factor maps to human chromosome 5q31 (TCEB1L) and to mouse
            chromosome 11 (Tceb1l)
  JOURNAL   Genomics 29 (1), 145-151 (1995)
   PUBMED   8530064
REFERENCE   10 (residues 1 to 163)
  AUTHORS   Chen,H., Thalmann,I., Adams,J.C., Avraham,K.B., Copeland,N.G.,
            Jenkins,N.A., Beier,D.R., Corey,D.P., Thalmann,R. and Duyk,G.M.
  TITLE     cDNA cloning, tissue distribution, and chromosomal localization of
            Ocp2, a gene encoding a putative transcription-associated factor
            predominantly expressed in the auditory organs
  JOURNAL   Genomics 27 (3), 389-398 (1995)
   PUBMED   7558018
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z47087.1, BC065730.1, AI028694.1, BQ632052.1, AI025746.1 and
            AC011336.5.
            
            Summary: This gene encodes a component of SCF complexes, which are
            composed of this protein, cullin 1, a ring-box protein, and one
            member of the F-box family of proteins. This protein binds directly
            to the F-box motif found in F-box proteins. SCF complexes are
            involved in the regulated ubiquitination of specific protein
            substrates, which targets them for degradation by the proteosome.
            Specific F-box proteins recognize different target protein(s), and
            many specific SCF substrates have been identified including
            regulators of cell cycle progression and development. Studies have
            also characterized the protein as an RNA polymerase II elongation
            factor. Alternative splicing of this gene results in two transcript
            variants. A related pseudogene has been identified on chromosome 7.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) utilizes an alternate splice
            site in the 3' coding region, compared to variant 1.  This results
            in a frameshift and slightly longer protein (isoform b), compared
            to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.197332.1,
                                           SRR1803617.267145.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000353411.11/ ENSP00000231487.9
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.1"
     Protein         1..163
                     /product="S-phase kinase-associated protein 1 isoform b"
                     /EC_number="3.1.1.3"
                     /note="organ of Corti protein 2; RNA polymerase II
                     elongation factor-like protein OCP2; cyclin
                     A/CDK2-associated p19; SIII; OCP-2; p19skp1; organ of
                     Corti protein II; cyclin-A/CDK2-associated protein p19;
                     transcription elongation factor B polypeptide 1-like"
                     /calculated_mol_wt=18527
     Region          4..127
                     /region_name="BTB_POZ_SKP1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ
                     (poxvirus and zinc finger) domain found in S-phase
                     kinase-associated protein 1 (SKP1) and similar proteins;
                     cd18322"
                     /db_xref="CDD:349631"
     Site            order(25..26,30,34,38,43..44,46,48..49,105,108..109,111)
                     /site_type="other"
                     /note="cullin binding site [polypeptide binding]"
                     /db_xref="CDD:349631"
     Region          63..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P63208.2)"
     Site            order(97,101,105,108,113,117,120..121,123..124,127)
                     /site_type="other"
                     /note="F-box protein binding site [polypeptide binding]"
                     /db_xref="CDD:349631"
     Region          104..163
                     /region_name="Interaction with the F-box domain of F-box
                     proteins. /evidence=ECO:0000269|PubMed:35982156,
                     ECO:0007744|PDB:7Z8B"
                     /note="propagated from UniProtKB/Swiss-Prot (P63208.2)"
     Region          113..160
                     /region_name="Skp1"
                     /note="Skp1 family, dimerization domain; pfam01466"
                     /db_xref="CDD:460222"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P63208.2)"
     CDS             1..163
                     /gene="SKP1"
                     /gene_synonym="EMC19; OCP-II; OCP2; p19A; SKP1A; TCEB1L"
                     /coded_by="NM_170679.3:97..588"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4171.1"
                     /db_xref="GeneID:6500"
                     /db_xref="HGNC:HGNC:10899"
                     /db_xref="MIM:601434"
ORIGIN      
        1 mpsiklqssd geifevdvei akqsvtiktm ledlgmddeg dddpvplpnv naailkkviq
       61 wcthhkddpp ppeddenkek rtddipvwdq eflkvdqgtl felilaanyl dikglldvtc
      121 ktvanmikgk tpeeirktfn ikndfteeee aqvrkenqwc eek
//
LOCUS       NP_001341739             792 aa            linear   PRI 21-NOV-2025
DEFINITION  fibroblast growth factor receptor 3 isoform 5 precursor [Homo
            sapiens].
ACCESSION   NP_001341739
VERSION     NP_001341739.1
DBSOURCE    REFSEQ: accession NM_001354810.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 792)
  AUTHORS   Noeraparast,M., Krajina,K., Pichler,R., Niedersuss-Beke,D.,
            Shariat,S.F., Grunwald,V., Ahyai,S. and Pichler,M.
  TITLE     FGFR3 alterations in bladder cancer: Sensitivity and resistance to
            targeted therapies
  JOURNAL   Cancer Commun (Lond) 44 (10), 1189-1208 (2024)
   PUBMED   39161208
  REMARK    GeneRIF: FGFR3 alterations in bladder cancer: Sensitivity and
            resistance to targeted therapies.
            Review article
REFERENCE   2  (residues 1 to 792)
  AUTHORS   Kobatake,K., Ikeda,K., Kohada,Y., Tasaka,R., Takemoto,K.,
            Fukushima,T., Miyamoto,S., Sekino,Y., Kitano,H., Goto,K., Hieda,K.,
            Goriki,A., Hayashi,T. and Hinata,N.
  TITLE     Muscle-Invasive Bladder Cancer With Hydronephrosis Exhibits a High
            Frequency of Mutations in Fibroblast Growth Factor Receptor 3 Gene
  JOURNAL   Anticancer Res 44 (5), 1947-1954 (2024)
   PUBMED   38677755
  REMARK    GeneRIF: Muscle-Invasive Bladder Cancer With Hydronephrosis
            Exhibits a High Frequency of Mutations in Fibroblast Growth Factor
            Receptor 3 Gene.
REFERENCE   3  (residues 1 to 792)
  AUTHORS   Shen,N., Zhang,J., Xia,Y., Shen,X.X., Wang,J., Jin,Y.Y., Zhang,R.,
            Li,J.Y. and Chen,L.J.
  TITLE     [Clinical characteristics and prognosis of newly diagnosed multiple
            myeloma patients with FGFR3 gene mutations]
  JOURNAL   Zhonghua Xue Ye Xue Za Zhi 44 (12), 989-994 (2023)
   PUBMED   38503521
  REMARK    GeneRIF: [Clinical characteristics and prognosis of newly diagnosed
            multiple myeloma patients with FGFR3 gene mutations].
REFERENCE   4  (residues 1 to 792)
  AUTHORS   Bober,M.B., Bellus,G.A., Cheung,M.S., Jain,M., Nikkel,S.M. and
            Tiller,G.E.
  TITLE     Hypochondroplasia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301650
REFERENCE   5  (residues 1 to 792)
  AUTHORS   Wenger,T., Miller,D. and Evans,K.
  TITLE     FGFR Craniosynostosis Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301628
REFERENCE   6  (residues 1 to 792)
  AUTHORS   Kruszka,P., Rolle,M., Kahle,K.T. and Muenke,M.
  TITLE     Muenke Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301588
REFERENCE   7  (residues 1 to 792)
  AUTHORS   French,T. and Savarirayan,R.
  TITLE     Thanatophoric Dysplasia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301540
REFERENCE   8  (residues 1 to 792)
  AUTHORS   Legare,J.M. and Modaff,P.
  TITLE     Achondroplasia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301331
REFERENCE   9  (residues 1 to 792)
  AUTHORS   Thompson,L.M., Plummer,S., Schalling,M., Altherr,M.R.,
            Gusella,J.F., Housman,D.E. and Wasmuth,J.J.
  TITLE     A gene encoding a fibroblast growth factor receptor isolated from
            the Huntington disease gene region of human chromosome 4
  JOURNAL   Genomics 11 (4), 1133-1142 (1991)
   PUBMED   1664411
REFERENCE   10 (residues 1 to 792)
  AUTHORS   Keegan,K., Johnson,D.E., Williams,L.T. and Hayman,M.J.
  TITLE     Isolation of an additional member of the fibroblast growth factor
            receptor family, FGFR-3
  JOURNAL   Proc Natl Acad Sci U S A 88 (4), 1095-1099 (1991)
   PUBMED   1847508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016773.8.
            
            Summary: This gene encodes a member of the fibroblast growth factor
            receptor (FGFR) family, with its amino acid sequence being highly
            conserved between members and among divergent species. FGFR family
            members differ from one another in their ligand affinities and
            tissue distribution. A full-length representative protein would
            consist of an extracellular region, composed of three
            immunoglobulin-like domains, a single hydrophobic membrane-spanning
            segment and a cytoplasmic tyrosine kinase domain. The extracellular
            portion of the protein interacts with fibroblast growth factors,
            setting in motion a cascade of downstream signals, ultimately
            influencing mitogenesis and differentiation. This particular family
            member binds acidic and basic fibroblast growth hormone and plays a
            role in bone development and maintenance. Mutations in this gene
            lead to craniosynostosis and multiple types of skeletal dysplasia.
            [provided by RefSeq, Aug 2017].
            
            Transcript Variant: This variant (5) lacks two alternate coding
            exons, contains another alternate coding exon, and uses an
            alternate in-frame splice junction compared to variant 3. The
            resulting isoform (5) has multiple differences compared to isoform
            3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB209441.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158188 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..792
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..792
                     /product="fibroblast growth factor receptor 3 isoform 5
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="hydroxyaryl-protein kinase; tyrosine kinase JTK4;
                     FGFR-3; fibroblast growth factor receptor 3-S"
                     /calculated_mol_wt=83283
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1946
     Region          37..109
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          57..61
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          69..75
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          92..96
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            98
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22607.1)"
     Region          126..153
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22607.1)"
     Region          151..245
                     /region_name="IgI_2_FGFR"
                     /note="Second immunoglobulin (Ig)-like domain of
                     fibroblast growth factor (FGF) receptor; member of the
                     I-set of IgSF domains; cd05857"
                     /db_xref="CDD:409443"
     Region          151..154
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409443"
     Region          162..167
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409443"
     Site            order(163,165,167)
                     /site_type="other"
                     /note="FGF binding site [polypeptide binding]"
                     /db_xref="CDD:409443"
     Site            order(164,171..173,175)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409443"
     Region          171..179
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409443"
     Region          185..190
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409443"
     Region          193..195
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409443"
     Region          204..207
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409443"
     Region          211..216
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409443"
     Region          225..232
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409443"
     Site            225
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22607.1)"
     Region          235..245
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409443"
     Region          253..357
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            262
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22607.1)"
     Region          271..275
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          284..288
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            294
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22607.1)"
     Site            315
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22607.1)"
     Region          322..326
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            328
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22607.1)"
     Region          336..341
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          349..352
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            376..396
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22607.1)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61851; propagated from
                     UniProtKB/Swiss-Prot (P22607.1)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61851; propagated from
                     UniProtKB/Swiss-Prot (P22607.1)"
     Region          460..>654
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(479..482,485,487,507,509,540,556..559,618,622..623,
                     625,635..636)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:8754806; propagated from
                     UniProtKB/Swiss-Prot (P22607.1)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:8754806; propagated from
                     UniProtKB/Swiss-Prot (P22607.1)"
     CDS             1..792
                     /gene="FGFR3"
                     /gene_synonym="ACH; CD333; CEK2; HSFGFR3EX; JTK4"
                     /coded_by="NM_001354810.2:276..2654"
                     /note="isoform 5 precursor is encoded by transcript
                     variant 5"
                     /db_xref="CCDS:CCDS87200.1"
                     /db_xref="GeneID:2261"
                     /db_xref="HGNC:HGNC:3690"
                     /db_xref="MIM:134934"
ORIGIN      
        1 mgapacalal cvavaivaga sseslgteqr vvgraaevpg pepgqqeqlv fgsgdavels
       61 cpppgggpmg ptvwvkdgtg lvpservlvg pqrlqvlnas hedsgayscr qrltqrvlch
      121 fsvrvtdaps sgddedgede aedtgvdtga pywtrpermd kkllavpaan tvrfrcpaag
      181 nptpsiswlk ngrefrgehr iggiklrhqq wslvmesvvp sdrgnytcvv enkfgsirqt
      241 ytldvlersp hrpilqaglp anqtavlgsd vefhckvysd aqphiqwlkh vevngskvgp
      301 dgtpyvtvlk taganttdke levlslhnvt fedageytcl agnsigfshh sawlvvlpae
      361 eelveadeag svyagilsyg vgfflfilvv aavtlcrlrs ppkkglgspt vhkisrfplk
      421 rqqvslesna smssntplvr iarlssgegp tlanvselel padpkwelsr arltlgkplg
      481 egcfgqvvma eaigidkdra akpvtvavkm lkddatdkdl sdlvsememm kmigkhknii
      541 nllgactqgg plyvlveyaa kgnlreflra rrppgldysf dtckppeeql tfkdlvscay
      601 qvargmeyla sqkcihrdla arnvlvtedn vmkiadfgla rdvhnldyyk kttnlvlwgp
      661 algdlhaggl pvprhpcgga lqaaeggpph gqarqlhtrp vhdhagvlac ralpeahlqa
      721 agggpgpcpy rdvhrrvpgp vgafravlpg wpghpqlqll rgrlrvcprp aapgptqqwg
      781 ladvkghwsp tm
//
LOCUS       NP_001363280             810 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger CCCH domain-containing protein 11A isoform 1 [Homo
            sapiens].
ACCESSION   NP_001363280
VERSION     NP_001363280.1
DBSOURCE    REFSEQ: accession NM_001376351.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Kases,K., Schubert,E., Hajikhezri,Z., Larsson,M., Devi,P.,
            Darweesh,M., Andersson,L., Akusjarvi,G., Punga,T. and Younis,S.
  TITLE     The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts
  JOURNAL   J Biol Chem 299 (8), 104959 (2023)
   PUBMED   37356722
  REMARK    GeneRIF: The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts.
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 810)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 810)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114402.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.86928.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..810
                     /product="zinc finger CCCH domain-containing protein 11A
                     isoform 1"
                     /note="zinc finger CCCH-type domain containing 11A; zinc
                     finger CCCH domain-containing protein 11A"
                     /calculated_mol_wt=89000
     Region          1..110
                     /region_name="zf-CCCH_3"
                     /note="Zinc-finger containing family; pfam15663"
                     /db_xref="CDD:464787"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          139..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          223..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          285..351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          367..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          482..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          715..768
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     CDS             1..810
                     /gene="ZC3H11A"
                     /gene_synonym="ZC3HDC11A"
                     /coded_by="NM_001376351.1:888..3320"
                     /note="isoform 1 is encoded by transcript variant 27"
                     /db_xref="CCDS:CCDS30978.1"
                     /db_xref="GeneID:9877"
                     /db_xref="HGNC:HGNC:29093"
                     /db_xref="MIM:613513"
ORIGIN      
        1 mpnqgedcyf ffystctkgd scpfrhceaa ignetvctlw qegrcfrqvc rfrhmeidkk
       61 rseipcywen qptgcqklnc afhhnrgryv dglflppskt vlptvpespe eevkasqlsv
      121 qqnklsvqsn pspqlrsvmk vessenvpsp thppvvinaa dddeddddqf seegdetktp
      181 tlqptpevhn glrvtsvrkp avnikqgecl nfgiktleei kskkmkeksk kqgegssgvs
      241 slllhpepvp gpekenvrtv vrtvtlstkq geeplvrlsl terlgkrkfs aggdsdpplk
      301 rslaqrlgkk veapetnidk tpkkaqvsks lkerlgmsad pdnedatdkv nkvgeihvkt
      361 leeilleras qkrgelqtkl ktegpsktdd stsgarssst iriktfsevl aekkhrqqea
      421 erqkskkdtt ciklkidsei kktvvlppiv asrgqseepa gktksmqevh iktleeikle
      481 kalrvqqsse sstsspsqhe atpgarrllr itkrtgmkee knlqegnevd sqssirteak
      541 easgettgvd itkiqvkrce tmrekhmqkq qereksvltp lrgdvascnt qvaekpvlta
      601 vpgitrhltk rlptkssqkv evetsgigds llnvkcaaqt lekrgkakpk vnvkpsvvkv
      661 vsspklapkr kavemhaavi aavkplssss vlqeppakka avavvplvse dksvtvpeae
      721 nprdslvlpp tqsssdsspp evsgpsssqm smktrrlssa stgkpplsve ddfekliwei
      781 sggkleaeid ldpgkdeddl llelsemids
//
LOCUS       NP_057293                140 aa            linear   PRI 21-NOV-2025
DEFINITION  trafficking protein particle complex subunit 2-like protein isoform
            2 [Homo sapiens].
ACCESSION   NP_057293
VERSION     NP_057293.1
DBSOURCE    REFSEQ: accession NM_016209.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Abaji,M., Mignon-Ravix,C., Gorokhova,S., Cacciagli,P., Mortreux,J.,
            Molinari,F., Chabrol,B., Sigaudy,S., Villard,L. and Riccardi,F.
  TITLE     TRAPPC2L-related disorder: first homozygous protein-truncating
            variant and further delineation of the phenotype
  JOURNAL   J Med Genet 60 (10), 1021-1025 (2023)
   PUBMED   36849228
  REMARK    GeneRIF: TRAPPC2L-related disorder: first homozygous
            protein-truncating variant and further delineation of the
            phenotype.
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Al-Deri,N., Okur,V., Ahimaz,P., Milev,M., Valivullah,Z., Hagen,J.,
            Sheng,Y., Chung,W., Sacher,M. and Ganapathi,M.
  TITLE     A novel homozygous variant in TRAPPC2L results in a
            neurodevelopmental disorder and disrupts TRAPP complex function
  JOURNAL   J Med Genet 58 (9), 592-601 (2021)
   PUBMED   32843486
  REMARK    GeneRIF: A novel homozygous variant in TRAPPC2L results in a
            neurodevelopmental disorder and disrupts TRAPP complex function.
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Scrivens,P.J., Noueihed,B., Shahrzad,N., Hul,S., Brunet,S. and
            Sacher,M.
  TITLE     C4orf41 and TTC-15 are mammalian TRAPP components with a role at an
            early stage in ER-to-Golgi trafficking
  JOURNAL   Mol Biol Cell 22 (12), 2083-2093 (2011)
   PUBMED   21525244
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Choi,C., Davey,M., Schluter,C., Pandher,P., Fang,Y., Foster,L.J.
            and Conibear,E.
  TITLE     Organization and assembly of the TRAPPII complex
  JOURNAL   Traffic 12 (6), 715-725 (2011)
   PUBMED   21453443
REFERENCE   8  (residues 1 to 140)
  AUTHORS   Westlake,C.J., Baye,L.M., Nachury,M.V., Wright,K.J., Ervin,K.E.,
            Phu,L., Chalouni,C., Beck,J.S., Kirkpatrick,D.S., Slusarski,D.C.,
            Sheffield,V.C., Scheller,R.H. and Jackson,P.K.
  TITLE     Primary cilia membrane assembly is initiated by Rab11 and transport
            protein particle II (TRAPPII) complex-dependent trafficking of
            Rabin8 to the centrosome
  JOURNAL   Proc Natl Acad Sci U S A 108 (7), 2759-2764 (2011)
   PUBMED   21273506
REFERENCE   9  (residues 1 to 140)
  AUTHORS   Garcia,S.A. and Nagai,M.A.
  TITLE     Transcriptional regulation of bidirectional gene pairs by
            17-beta-estradiol in MCF-7 breast cancer cells
  JOURNAL   Braz J Med Biol Res 44 (2), 112-122 (2011)
   PUBMED   21180879
REFERENCE   10 (residues 1 to 140)
  AUTHORS   Scrivens,P.J., Shahrzad,N., Moores,A., Morin,A., Brunet,S. and
            Sacher,M.
  TITLE     TRAPPC2L is a novel, highly conserved TRAPP-interacting protein
  JOURNAL   Traffic 10 (6), 724-736 (2009)
   PUBMED   19416478
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC105809.1, BC011369.1 and
            BC017440.1.
            
            Summary: This gene encodes a protein that interacts with the
            tethering factor trafficking protein particle (TRAPP complex).
            TRAPP complexes mediate the contact between vescicles and target
            membranes, and thus, are involved in vescicle-mediated transport of
            proteins and lipids. The encoded protein is related to the X-linked
            trafficking protein particle complex 2. A related pseudogene is
            located on the X chromosome. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region, compared to variant 1. It
            encodes isoform 2, which is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.475947.1,
                                           SRR3476690.200809.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..140
                     /product="trafficking protein particle complex subunit
                     2-like protein isoform 2"
                     /note="hematopoietic stem/progenitor cells 176;
                     trafficking protein particle complex subunit 2-like
                     protein; trafficking protein particle complex 2 like"
                     /calculated_mol_wt=16015
     Region          3..136
                     /region_name="TRAPPC2L"
                     /note="Trafficking protein particle complex subunit
                     2-like; cd14854"
                     /db_xref="CDD:341444"
     CDS             1..140
                     /gene="TRAPPC2L"
                     /gene_synonym="HSPC176; PERRB"
                     /coded_by="NM_016209.5:25..447"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10971.1"
                     /db_xref="GeneID:51693"
                     /db_xref="HGNC:HGNC:30887"
                     /db_xref="MIM:610970"
ORIGIN      
        1 mavciaviak enyplyirst ptenelkfhy mvhtsldvvd ekisamgkal vdqrelylgl
       61 lyptedykvy gyvtnskvkf vmvvdssnta lrdneirsmf rklhnsytdv mcnpfynpgd
      121 riqssrafdn mvtsmmiqvc
//
LOCUS       NP_705842                316 aa            linear   PRI 21-NOV-2025
DEFINITION  dnaJ homolog subfamily B member 13 isoform 1 [Homo sapiens].
ACCESSION   NP_705842 XP_350842
VERSION     NP_705842.2
DBSOURCE    REFSEQ: accession NM_153614.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Zhang,X., Xiao,Z., Zhang,J., Xu,C., Liu,S., Cheng,L., Zhou,S.,
            Zhao,S., Zhang,Y., Wu,J., Wang,Y. and Liu,M.
  TITLE     Differential requirements of IQUB for the assembly of radial spoke
            1 and the motility of mouse cilia and flagella
  JOURNAL   Cell Rep 41 (8), 111683 (2022)
   PUBMED   36417862
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Liu,M., Li,J., Jiang,C., Zhou,Y., Sun,Y., Yang,Y. and Shen,Y.
  TITLE     A novel homozygous mutation in DNAJB13-a gene associated with the
            sperm axoneme-leads to teratozoospermia
  JOURNAL   J Assist Reprod Genet 39 (3), 757-764 (2022)
   PUBMED   35166991
  REMARK    GeneRIF: A novel homozygous mutation in DNAJB13-a gene associated
            with the sperm axoneme-leads to teratozoospermia.
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Li,W.N., Zhu,L., Jia,M.M., Yin,S.L., Lu,G.X. and Liu,G.
  TITLE     Missense mutation in DNAJB13 gene correlated with male fertility in
            asthenozoospermia
  JOURNAL   Andrology 8 (2), 299-306 (2020)
   PUBMED   31342671
  REMARK    GeneRIF: Missense mutation in DNAJB13 gene correlated with male
            fertility in asthenozoospermia.
REFERENCE   5  (residues 1 to 316)
  AUTHORS   El Khouri,E., Thomas,L., Jeanson,L., Bequignon,E., Vallette,B.,
            Duquesnoy,P., Montantin,G., Copin,B., Dastot-Le Moal,F.,
            Blanchon,S., Papon,J.F., Lores,P., Yuan,L., Collot,N., Tissier,S.,
            Faucon,C., Gacon,G., Patrat,C., Wolf,J.P., Dulioust,E.,
            Crestani,B., Escudier,E., Coste,A., Legendre,M., Toure,A. and
            Amselem,S.
  TITLE     Mutations in DNAJB13, Encoding an HSP40 Family Member, Cause
            Primary Ciliary Dyskinesia and Male Infertility
  JOURNAL   Am J Hum Genet 99 (2), 489-500 (2016)
   PUBMED   27486783
  REMARK    GeneRIF: this study, which establishes mutations in DNAJB13 as a
            cause of PCD, unveils the key role played by DNAJB13 in the proper
            formation and function of ciliary and flagellar axonemes in humans
REFERENCE   6  (residues 1 to 316)
  AUTHORS   Li,W. and Liu,G.
  TITLE     DNAJB13, a type II HSP40 family member, localizes to the spermatids
            and spermatozoa during mouse spermatogenesis
  JOURNAL   BMC Dev Biol 14, 38 (2014)
   PUBMED   25233908
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 316)
  AUTHORS   Toure,A., Rode,B., Hunnicutt,G.R., Escalier,D. and Gacon,G.
  TITLE     Septins at the annulus of mammalian sperm
  JOURNAL   Biol Chem 392 (8-9), 799-803 (2011)
   PUBMED   21740329
  REMARK    Review article
REFERENCE   8  (residues 1 to 316)
  AUTHORS   Liu,G., Lu,G.X. and Xing,X.W.
  TITLE     Molecular cloning of TSARG6 gene related to apoptosis in human
            spermatogenic cells
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 36 (2), 93-98 (2004)
   PUBMED   14970903
  REMARK    GeneRIF: TSARG6 is specifically expressed in adult testis with a
            transcript of 1.8 kb, which has a role in spermatogenesis and
            apoptosis
REFERENCE   9  (residues 1 to 316)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY138810.2 and AY325766.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Dec 17, 2003 this sequence version replaced
            XP_350842.1, NP_705842.1.
            
            Summary: This gene encodes a member of the heat shock protein 40
            co-chaperone family which is produced in large amounts in the
            testis and is located on the radial spokes of the axoneme in human
            sperm flagella and other flagellar structures. The encoded protein
            associates with the sperm annulus, as part of the septin complex,
            through direct interaction with septin 4, during sperm terminal
            differentiation. Naturally occurring mutations in this gene are
            associated with primary ciliary dyskinesia and male infertility.
            [provided by RefSeq, Apr 2017].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY325766.1, AY138810.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000339764.6/ ENSP00000344431.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..316
                     /product="dnaJ homolog subfamily B member 13 isoform 1"
                     /note="DnaJ (Hsp40) related, subfamily B, member 13;
                     radial spoke 16 homolog A; dnaJ homolog subfamily B member
                     13; DnaJ-like protein; testis and spermatogenesis
                     cell-related protein 6; testis spermatocyte
                     apoptosis-related gene 6 protein; testis spermatogenesis
                     apoptosis-related gene 3 protein; testis spermatogenesis
                     apoptosis-related gene 6 protein; DnaJ (Hsp40) homolog,
                     subfamily B, member 13"
                     /calculated_mol_wt=35987
     Region          5..311
                     /region_name="PTZ00037"
                     /note="DnaJ_C chaperone protein; Provisional"
                     /db_xref="CDD:240236"
     CDS             1..316
                     /gene="DNAJB13"
                     /gene_synonym="CILD34; RSPH16A; TSARG5; TSARG6"
                     /coded_by="NM_153614.4:45..995"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8227.1"
                     /db_xref="GeneID:374407"
                     /db_xref="HGNC:HGNC:30718"
                     /db_xref="MIM:610263"
ORIGIN      
        1 mgqdyysvlg itrnsedaqi kqayrrlalk hhplksneps saeifrqiae aydvlsdpmk
       61 rgiydkfgee glkggiplef gsqtpwttgy vfhgkpekvf heffggnnpf seffdaegse
      121 vdlnfgglqg rgvkkqdpqv erdlylsled lffgctkkik isrrvlnedg ysstikdkil
      181 tidvkpgwrq gtritfekeg dqgpniipad iifivkeklh prfrrendnl ffvnpiplgk
      241 altcctvevr tlddrllnip indiihpkyf kkvpgegmpl pedptkkgdl fiffdiqfpt
      301 rltpqkkqml rqallt
//
LOCUS       NP_001310189             397 aa            linear   PRI 21-NOV-2025
DEFINITION  kelch-like protein 32 isoform l [Homo sapiens].
ACCESSION   NP_001310189 XP_005266872
VERSION     NP_001310189.1
DBSOURCE    REFSEQ: accession NM_001323260.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Simino,J., Shi,G., Bis,J.C., Chasman,D.I., Ehret,G.B., Gu,X.,
            Guo,X., Hwang,S.J., Sijbrands,E., Smith,A.V., Verwoert,G.C.,
            Bragg-Gresham,J.L., Cadby,G., Chen,P., Cheng,C.Y., Corre,T., de
            Boer,R.A., Goel,A., Johnson,T., Khor,C.C., Lluis-Ganella,C.,
            Luan,J., Lyytikainen,L.P., Nolte,I.M., Sim,X., Sober,S., van der
            Most,P.J., Verweij,N., Zhao,J.H., Amin,N., Boerwinkle,E.,
            Bouchard,C., Dehghan,A., Eiriksdottir,G., Elosua,R., Franco,O.H.,
            Gieger,C., Harris,T.B., Hercberg,S., Hofman,A., James,A.L.,
            Johnson,A.D., Kahonen,M., Khaw,K.T., Kutalik,Z., Larson,M.G.,
            Launer,L.J., Li,G., Liu,J., Liu,K., Morrison,A.C., Navis,G.,
            Ong,R.T., Papanicolau,G.J., Penninx,B.W., Psaty,B.M., Raffel,L.J.,
            Raitakari,O.T., Rice,K., Rivadeneira,F., Rose,L.M., Sanna,S.,
            Scott,R.A., Siscovick,D.S., Stolk,R.P., Uitterlinden,A.G.,
            Vaidya,D., van der Klauw,M.M., Vasan,R.S., Vithana,E.N., Volker,U.,
            Volzke,H., Watkins,H., Young,T.L., Aung,T., Bochud,M., Farrall,M.,
            Hartman,C.A., Laan,M., Lakatta,E.G., Lehtimaki,T., Loos,R.J.,
            Lucas,G., Meneton,P., Palmer,L.J., Rettig,R., Snieder,H., Tai,E.S.,
            Teo,Y.Y., van der Harst,P., Wareham,N.J., Wijmenga,C., Wong,T.Y.,
            Fornage,M., Gudnason,V., Levy,D., Palmas,W., Ridker,P.M.,
            Rotter,J.I., van Duijn,C.M., Witteman,J.C., Chakravarti,A. and
            Rao,D.C.
  CONSRTM   LifeLines Cohort Study
  TITLE     Gene-age interactions in blood pressure regulation: a large-scale
            investigation with the CHARGE, Global BPgen, and ICBP Consortia
  JOURNAL   Am J Hum Genet 95 (1), 24-38 (2014)
   PUBMED   24954895
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Leone,M.A., Barizzone,N., Esposito,F., Lucenti,A., Harbo,H.F.,
            Goris,A., Kockum,I., Oturai,A.B., Celius,E.G., Mero,I.L.,
            Dubois,B., Olsson,T., Sondergaard,H.B., Cusi,D., Lupoli,S.,
            Andreassen,B.K., Myhr,K.M., Guerini,F.R., Comi,G.,
            Martinelli-Boneschi,F. and D'Alfonso,S.
  CONSRTM   International Multiple Sclerosis Genetics Consortium; Wellcome
            Trust Case Control Consortium 2; PROGEMUS Group; PROGRESSO Group
  TITLE     Association of genetic markers with CSF oligoclonal bands in
            multiple sclerosis patients
  JOURNAL   PLoS One 8 (6), e64408 (2013)
   PUBMED   23785401
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 397)
  AUTHORS   Monda,K.L., Chen,G.K., Taylor,K.C., Palmer,C., Edwards,T.L.,
            Lange,L.A., Ng,M.C., Adeyemo,A.A., Allison,M.A., Bielak,L.F.,
            Chen,G., Graff,M., Irvin,M.R., Rhie,S.K., Li,G., Liu,Y., Liu,Y.,
            Lu,Y., Nalls,M.A., Sun,Y.V., Wojczynski,M.K., Yanek,L.R.,
            Aldrich,M.C., Ademola,A., Amos,C.I., Bandera,E.V., Bock,C.H.,
            Britton,A., Broeckel,U., Cai,Q., Caporaso,N.E., Carlson,C.S.,
            Carpten,J., Casey,G., Chen,W.M., Chen,F., Chen,Y.D., Chiang,C.W.,
            Coetzee,G.A., Demerath,E., Deming-Halverson,S.L., Driver,R.W.,
            Dubbert,P., Feitosa,M.F., Feng,Y., Freedman,B.I., Gillanders,E.M.,
            Gottesman,O., Guo,X., Haritunians,T., Harris,T., Harris,C.C.,
            Hennis,A.J., Hernandez,D.G., McNeill,L.H., Howard,T.D.,
            Howard,B.V., Howard,V.J., Johnson,K.C., Kang,S.J., Keating,B.J.,
            Kolb,S., Kuller,L.H., Kutlar,A., Langefeld,C.D., Lettre,G.,
            Lohman,K., Lotay,V., Lyon,H., Manson,J.E., Maixner,W., Meng,Y.A.,
            Monroe,K.R., Morhason-Bello,I., Murphy,A.B., Mychaleckyj,J.C.,
            Nadukuru,R., Nathanson,K.L., Nayak,U., N'diaye,A., Nemesure,B.,
            Wu,S.Y., Leske,M.C., Neslund-Dudas,C., Neuhouser,M., Nyante,S.,
            Ochs-Balcom,H., Ogunniyi,A., Ogundiran,T.O., Ojengbede,O.,
            Olopade,O.I., Palmer,J.R., Ruiz-Narvaez,E.A., Palmer,N.D.,
            Press,M.F., Rampersaud,E., Rasmussen-Torvik,L.J.,
            Rodriguez-Gil,J.L., Salako,B., Schadt,E.E., Schwartz,A.G.,
            Shriner,D.A., Siscovick,D., Smith,S.B., Wassertheil-Smoller,S.,
            Speliotes,E.K., Spitz,M.R., Sucheston,L., Taylor,H., Tayo,B.O.,
            Tucker,M.A., Van Den Berg,D.J., Edwards,D.R., Wang,Z.,
            Wiencke,J.K., Winkler,T.W., Witte,J.S., Wrensch,M., Wu,X.,
            Yang,J.J., Levin,A.M., Young,T.R., Zakai,N.A., Cushman,M.,
            Zanetti,K.A., Zhao,J.H., Zhao,W., Zheng,Y., Zhou,J., Ziegler,R.G.,
            Zmuda,J.M., Fernandes,J.K., Gilkeson,G.S., Kamen,D.L., Hunt,K.J.,
            Spruill,I.J., Ambrosone,C.B., Ambs,S., Arnett,D.K., Atwood,L.,
            Becker,D.M., Berndt,S.I., Bernstein,L., Blot,W.J., Borecki,I.B.,
            Bottinger,E.P., Bowden,D.W., Burke,G., Chanock,S.J., Cooper,R.S.,
            Ding,J., Duggan,D., Evans,M.K., Fox,C., Garvey,W.T.,
            Bradfield,J.P., Hakonarson,H., Grant,S.F., Hsing,A., Chu,L.,
            Hu,J.J., Huo,D., Ingles,S.A., John,E.M., Jordan,J.M.,
            Kabagambe,E.K., Kardia,S.L., Kittles,R.A., Goodman,P.J.,
            Klein,E.A., Kolonel,L.N., Le Marchand,L., Liu,S., McKnight,B.,
            Millikan,R.C., Mosley,T.H., Padhukasahasram,B., Williams,L.K.,
            Patel,S.R., Peters,U., Pettaway,C.A., Peyser,P.A., Psaty,B.M.,
            Redline,S., Rotimi,C.N., Rybicki,B.A., Sale,M.M., Schreiner,P.J.,
            Signorello,L.B., Singleton,A.B., Stanford,J.L., Strom,S.S.,
            Thun,M.J., Vitolins,M., Zheng,W., Moore,J.H., Williams,S.M.,
            Ketkar,S., Zhu,X., Zonderman,A.B., Kooperberg,C.,
            Papanicolaou,G.J., Henderson,B.E., Reiner,A.P., Hirschhorn,J.N.,
            Loos,R.J., North,K.E. and Haiman,C.A.
  CONSRTM   NABEC Consortium; UKBEC Consortium; BioBank Japan Project; AGEN
            Consortium
  TITLE     A meta-analysis identifies new loci associated with body mass index
            in individuals of African ancestry
  JOURNAL   Nat Genet 45 (6), 690-696 (2013)
   PUBMED   23583978
REFERENCE   6  (residues 1 to 397)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA296671.1, AK055292.1, DA255882.1 and AB067487.1.
            
            On Apr 16, 2016 this sequence version replaced XP_005266872.1.
            
            Transcript Variant: This variant (15) uses an alternate splice site
            in an internal exon, and it thus differs in its 5' UTR and
            initiates translation from a downstream in-frame start codon,
            compared to variant 1. The encoded isoform (l) is shorter at the
            N-terminus, compared to isoform a. Both variants 15 and 16 encode
            isoform l.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.78790.1,
                                           SRR1660809.33707.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q16.1"
     Protein         1..397
                     /product="kelch-like protein 32 isoform l"
                     /note="BTB and kelch domain containing 5; kelch-like
                     protein 32"
                     /calculated_mol_wt=44900
     Region          68..123
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     Region          101..372
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          113..161
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          165..210
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          213..259
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          261..311
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     CDS             1..397
                     /gene="KLHL32"
                     /gene_synonym="BKLHD5; dJ21F7.1; KIAA1900; UG0030H05"
                     /coded_by="NM_001323260.2:1030..2223"
                     /note="isoform l is encoded by transcript variant 15"
                     /db_xref="GeneID:114792"
                     /db_xref="HGNC:HGNC:21221"
ORIGIN      
        1 mdellqyirf glmdvdtlht valshplvqa setatalvne aleyhqsiya qpvwqtrrtk
       61 prfqsdtlyi iggkkrevck vkelryfnpv dqenaliaai anwselapmp vgrshhcvav
      121 mgdflfvagg evehasgrtc avrtacrydp rsnswaeiap mkncrehfvl gameeylyav
      181 ggrnelrqvl ptverycpkk nkwtfvqsfd rslschagyv adgllwisgg vtntaqyqnr
      241 lmvyepnqnk wisrspmlqr rvyhsmaavq rklyvlggnd ldynndrilv rhidsynidt
      301 dqwtrcnfnl ltgqnesgva vhngriylvg gysiwtnepl aciqvldvsr egkeevfygp
      361 tlpfasngia acflpapyft cpnlqtlqvp hhrigti
//
LOCUS       NP_001243308             467 aa            linear   PRI 21-NOV-2025
DEFINITION  mini-chromosome maintenance complex-binding protein isoform 3 [Homo
            sapiens].
ACCESSION   NP_001243308
VERSION     NP_001243308.1
DBSOURCE    REFSEQ: accession NM_001256379.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Saito,Y., Santosa,V., Ishiguro,K.I. and Kanemaki,M.T.
  TITLE     MCMBP promotes the assembly of the MCM2-7 hetero-hexamer to ensure
            robust DNA replication in human cells
  JOURNAL   Elife 11, e77393 (2022)
   PUBMED   35438632
  REMARK    GeneRIF: MCMBP promotes the assembly of the MCM2-7 hetero-hexamer
            to ensure robust DNA replication in human cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Nishiyama,A., Frappier,L. and Mechali,M.
  TITLE     MCM-BP regulates unloading of the MCM2-7 helicase in late S phase
  JOURNAL   Genes Dev 25 (2), 165-175 (2011)
   PUBMED   21196493
  REMARK    GeneRIF: MCM-BP silencing in human cells also delays MCM
            dissociation in late S phase
REFERENCE   7  (residues 1 to 467)
  AUTHORS   Takahashi,N., Quimbaya,M., Schubert,V., Lammens,T., Vandepoele,K.,
            Schubert,I., Matsui,M., Inze,D., Berx,G. and De Veylder,L.
  TITLE     The MCM-binding protein ETG1 aids sister chromatid cohesion
            required for postreplicative homologous recombination repair
  JOURNAL   PLoS Genet 6 (1), e1000817 (2010)
   PUBMED   20090939
  REMARK    GeneRIF: Knockdown of the human ETG1 results in defective chromatid
            cohesion.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 467)
  AUTHORS   Sakwe,A.M., Nguyen,T., Athanasopoulos,V., Shire,K. and Frappier,L.
  TITLE     Identification and characterization of a novel component of the
            human minichromosome maintenance complex
  JOURNAL   Mol Cell Biol 27 (8), 3044-3055 (2007)
   PUBMED   17296731
  REMARK    GeneRIF: MCM-BP is conserved in multicellular eukaryotes and shares
            limited homology with MCM proteins. MCM-BP formed a complex with
            MCM3 to MCM7, which excluded MCM2.
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   10 (residues 1 to 467)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK094075.1 and AC027672.12.
            
            Summary: This gene encodes a protein which is a component of the
            hexameric minichromosome maintenance (MCM) complex which regulates
            initiation and elongation of DNA. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2012].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding region, and uses a downstream start codon compared to
            variant 1. The resulting protein (isoform 3) is shorter and has a
            shorter N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK094075.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.11"
     Protein         1..467
                     /product="mini-chromosome maintenance complex-binding
                     protein isoform 3"
                     /note="MCM-binding protein; mini-chromosome maintenance
                     complex-binding protein"
                     /calculated_mol_wt=52521
     Region          <1..453
                     /region_name="MCM_bind"
                     /note="Mini-chromosome maintenance replisome factor;
                     pfam09739"
                     /db_xref="CDD:462870"
     CDS             1..467
                     /gene="MCMBP"
                     /gene_synonym="C10orf119; MCM-BP"
                     /coded_by="NM_001256379.2:582..1985"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:79892"
                     /db_xref="HGNC:HGNC:25782"
                     /db_xref="MIM:610909"
ORIGIN      
        1 mdlqpnkqkd qhagarqags vgglqwcgep krleteastg qqlnslnlss pfdlnfplpg
       61 ekgpaclvkv yedwdcfkvn dilelygils vdpvlsilnn derdasalld pmectdtaee
      121 qrvhsppasl vprihvilaq klqhinpllp aclnkeeskt fvssfmsels pvraellgfl
      181 thallgdsla aeylilhlis tvytrrdvlp lgkftvnlsg cprnstfteh lyriiqhlvp
      241 asfrlqmtie nmnhlkfiph kdytanrlvs gllqlpsnts lvidetlleq gqldtpgvhn
      301 vtalsnlitw qkvdydfsyh qmefpcninv fitsegrsll padcqihlqp qlippnmeey
      361 mnsllsavlp svlnkfriyl tllrfleysi sdeitkaved dfvemrkndp qsitaddlhq
      421 llvvarclsl sagqttlsre rwlrakqles lrrtrlqqqk cvngnel
//
LOCUS       NP_277051                140 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor protein D55 isoform 1 [Homo sapiens].
ACCESSION   NP_277051
VERSION     NP_277051.4
DBSOURCE    REFSEQ: accession NM_033516.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Divaris,K., Monda,K.L., North,K.E., Olshan,A.F., Lange,E.M.,
            Moss,K., Barros,S.P., Beck,J.D. and Offenbacher,S.
  TITLE     Genome-wide association study of periodontal pathogen colonization
  JOURNAL   J Dent Res 91 (7 Suppl), 21S-28S (2012)
   PUBMED   22699663
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Cao,Q., Chen,J., Zhu,L., Liu,Y., Zhou,Z., Sha,J., Wang,S. and Li,J.
  TITLE     A testis-specific and testis developmentally regulated tumor
            protein D52 (TPD52)-like protein TPD52L3/hD55 interacts with TPD52
            family proteins
  JOURNAL   Biochem Biophys Res Commun 344 (3), 798-806 (2006)
   PUBMED   16631610
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133480.9.
            
            On Jun 2, 2019 this sequence version replaced NP_277051.3.
            
            Summary: This gene encodes a member of the tumor protein D52-like
            family of proteins. These proteins are characterized by an
            N-terminal coiled-coil motif that is used to form homo- and
            heteromeric complexes with other tumor protein D52-like proteins.
            The encoded protein may play a role in spermatogenesis. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AK057479.1, AY032877.1 [ECO:0000345]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.1"
     Protein         1..140
                     /product="tumor protein D55 isoform 1"
                     /note="tumor protein D55; testis development protein
                     NYD-SP25; protein kinase NYD-SP25; testis tissue
                     sperm-binding protein Li 87P; tumor protein D52 like 3"
                     /calculated_mol_wt=15372
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J77.2)"
     Region          24..122
                     /region_name="TPD52"
                     /note="Tumour protein D52 family; pfam04201"
                     /db_xref="CDD:461225"
     CDS             1..140
                     /gene="TPD52L3"
                     /gene_synonym="D55; hD55; NYDSP25; TPD55"
                     /coded_by="NM_033516.6:222..644"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34986.1"
                     /db_xref="GeneID:89882"
                     /db_xref="HGNC:HGNC:23382"
                     /db_xref="MIM:617567"
ORIGIN      
        1 mphartetsv gtyeshstse ledltepeqr elktkltkle aeivtlrhvl aakerrcgel
       61 krklgltalv glrqnlsksw ldvqvsntyv kqktsaalst mgtlicrklg gvkksatfrs
      121 feglmgtiks kvsggkrawp
//
LOCUS       NP_006290                394 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger and SCAN domain-containing protein 9 isoform 2 [Homo
            sapiens].
ACCESSION   NP_006290
VERSION     NP_006290.1
DBSOURCE    REFSEQ: accession NM_006299.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Ravasi,T., Suzuki,H., Cannistraci,C.V., Katayama,S., Bajic,V.B.,
            Tan,K., Akalin,A., Schmeier,S., Kanamori-Katayama,M., Bertin,N.,
            Carninci,P., Daub,C.O., Forrest,A.R., Gough,J., Grimmond,S.,
            Han,J.H., Hashimoto,T., Hide,W., Hofmann,O., Kamburov,A., Kaur,M.,
            Kawaji,H., Kubosaki,A., Lassmann,T., van Nimwegen,E.,
            MacPherson,C.R., Ogawa,C., Radovanovic,A., Schwartz,A.,
            Teasdale,R.D., Tegner,J., Lenhard,B., Teichmann,S.A., Arakawa,T.,
            Ninomiya,N., Murakami,K., Tagami,M., Fukuda,S., Imamura,K., Kai,C.,
            Ishihara,R., Kitazume,Y., Kawai,J., Hume,D.A., Ideker,T. and
            Hayashizaki,Y.
  TITLE     An atlas of combinatorial transcriptional regulation in mouse and
            man
  JOURNAL   Cell 140 (5), 744-752 (2010)
   PUBMED   20211142
  REMARK    Erratum:[Cell. 2010 Apr 16;141(2):369. Kamburov, Atanas [added];
            Kaur, Mandeep [added]; MacPherson, Cameron Ross [added];
            Radovanovic, Aleksandar [added]; Schwartz, Ariel [added]]
REFERENCE   8  (residues 1 to 394)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   9  (residues 1 to 394)
  AUTHORS   Williams,A.J., Blacklow,S.C. and Collins,T.
  TITLE     The zinc finger-associated SCAN box is a conserved oligomerization
            domain
  JOURNAL   Mol Cell Biol 19 (12), 8526-8535 (1999)
   PUBMED   10567577
REFERENCE   10 (residues 1 to 394)
  AUTHORS   Lee,P.L., Gelbart,T., West,C., Adams,M., Blackstone,R. and
            Beutler,E.
  TITLE     Three genes encoding zinc finger proteins on human chromosome
            6p21.3: members of a new subclass of the Kruppel gene family
            containing the conserved SCAN box domain
  JOURNAL   Genomics 43 (2), 191-201 (1997)
   PUBMED   9244436
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK304013.1, BC010374.1 and AK226035.1.
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            CDS, as compared to variant 1. The resulting isoform (2) lacks an
            internal segment, as compared to isoform 1. Variants 2 and 3 encode
            the same isoform 2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.189509.1,
                                           SRR1660803.222508.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000252207.10/ ENSP00000252207.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.1"
     Protein         1..394
                     /product="zinc finger and SCAN domain-containing protein 9
                     isoform 2"
                     /note="cell proliferation-inducing protein 12; cell
                     proliferation-inducing gene 12 protein; zinc finger and
                     SCAN domain-containing protein 9; zinc finger protein 193"
                     /calculated_mol_wt=45823
     Region          48..160
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          <253..389
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          256..276
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(261,263,265,267..268,271..272,275,289,291,295..296,
                     299..300,303,317,319,321,323..324,327..328,331)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          284..304
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          312..332
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          340..360
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          368..388
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..394
                     /gene="ZSCAN9"
                     /gene_synonym="PRD51; ZNF193"
                     /coded_by="NM_006299.5:166..1350"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4646.1"
                     /db_xref="GeneID:7746"
                     /db_xref="HGNC:HGNC:12984"
                     /db_xref="MIM:602246"
ORIGIN      
        1 mntnskevls lgvqvpeawe elltmkveak shlqwqesrl krsnplarei frrhfrqlcy
       61 qetpgpreal trlqelcyqw lrphvstkeq ildllvleqf lsilpkelqg wvrehcpesg
      121 eeavilledl ereldepqhe mvahrhrqev lckemvplae qtpltlqsqp kepqltcdsa
      181 qkchsigetd evtktedrel vlrkdcpkiv ephgkmfneq twevsqqdps hgevgehkdr
      241 ierqwgnllg egqhkcdecg ksftqssgli rhqrihtger pyecnecgka fsrssglfnh
      301 rgihniqkry hckecgkvfs qsagliqhqr ihkgekpyqc sqcsksysrr sfliehqrsh
      361 tgerphqcie cgksfnrhcn lirhqkihtv aelv
//
LOCUS       NP_004190                535 aa            linear   PRI 21-NOV-2025
DEFINITION  prolyl 4-hydroxylase subunit alpha-2 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_004190
VERSION     NP_004190.1
DBSOURCE    REFSEQ: accession NM_004199.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Dang,X., Chen,X., Liang,Z., Dai,Z., Ding,W., Song,J. and Fu,J.
  TITLE     P4HA2 promotes tumor progression and is transcriptionally regulated
            by SP1 in colorectal cancer
  JOURNAL   Cancer Biol Ther 25 (1), 2361594 (2024)
   PUBMED   38857058
  REMARK    GeneRIF: P4HA2 promotes tumor progression and is transcriptionally
            regulated by SP1 in colorectal cancer.
REFERENCE   3  (residues 1 to 535)
  AUTHORS   El-Deek,H.E.M., El-Naggar,M.S., Morsy,A.M.M., Sedik,M.F.,
            Osman,H.A. and Ahmed,A.M.
  TITLE     P4HA2 involved in SLUG-associated EMT predicts poor prognosis of
            patients with KRAS-positive colorectal cancer
  JOURNAL   Med Mol Morphol 57 (3), 167-176 (2024)
   PUBMED   38522060
  REMARK    GeneRIF: P4HA2 involved in SLUG-associated EMT predicts poor
            prognosis of patients with KRAS-positive colorectal cancer.
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Chi,Z., Wang,Q., Wang,X., Li,D., Tong,L., Shi,Y., Yang,F., Guo,Q.,
            Zheng,J. and Chen,Z.
  TITLE     P4HA2 promotes proliferation, invasion, and metastasis through
            regulation of the PI3K/AKT signaling pathway in oral squamous cell
            carcinoma
  JOURNAL   Sci Rep 14 (1), 15023 (2024)
   PUBMED   38951593
  REMARK    GeneRIF: P4HA2 promotes proliferation, invasion, and metastasis
            through regulation of the PI3K/AKT signaling pathway in oral
            squamous cell carcinoma.
            Erratum:[Sci Rep. 2024 Oct 28;14(1):25836. doi:
            10.1038/s41598-024-76811-1. PMID: 39468141]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 535)
  AUTHORS   Wu,Y.L., Liu,W., Zhao,T. and Jin,J.
  TITLE     P4HA2 contributes to head and neck squamous cell carcinoma
            progression and EMT through PI3K/AKT signaling pathway
  JOURNAL   Med Oncol 41 (6), 163 (2024)
   PUBMED   38777998
  REMARK    GeneRIF: P4HA2 contributes to head and neck squamous cell carcinoma
            progression and EMT through PI3K/AKT signaling pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 535)
  AUTHORS   Lehner,B., Semple,J.I., Brown,S.E., Counsell,D., Campbell,R.D. and
            Sanderson,C.M.
  TITLE     Analysis of a high-throughput yeast two-hybrid system and its use
            to predict the function of intracellular proteins encoded within
            the human MHC class III region
  JOURNAL   Genomics 83 (1), 153-167 (2004)
   PUBMED   14667819
REFERENCE   7  (residues 1 to 535)
  AUTHORS   Kukkola,L., Hieta,R., Kivirikko,K.I. and Myllyharju,J.
  TITLE     Identification and characterization of a third human, rat, and
            mouse collagen prolyl 4-hydroxylase isoenzyme
  JOURNAL   J Biol Chem 278 (48), 47685-47693 (2003)
   PUBMED   14500733
REFERENCE   8  (residues 1 to 535)
  AUTHORS   Hieta,R., Kukkola,L., Permi,P., Pirila,P., Kivirikko,K.I.,
            Kilpelainen,I. and Myllyharju,J.
  TITLE     The peptide-substrate-binding domain of human collagen prolyl
            4-hydroxylases. Backbone assignments, secondary structure, and
            binding of proline-rich peptides
  JOURNAL   J Biol Chem 278 (37), 34966-34974 (2003)
   PUBMED   12824157
  REMARK    GeneRIF: the substrate specificity, binding site and conformation
            of this enzyme
REFERENCE   9  (residues 1 to 535)
  AUTHORS   Nokelainen,M., Nissi,R., Kukkola,L., Helaakoski,T. and
            Myllyharju,J.
  TITLE     Characterization of the human and mouse genes for the alpha subunit
            of type II prolyl 4-hydroxylase. Identification of a previously
            unknown alternatively spliced exon and its expression in various
            tissues
  JOURNAL   Eur J Biochem 268 (20), 5300-5309 (2001)
   PUBMED   11606192
REFERENCE   10 (residues 1 to 535)
  AUTHORS   Annunen,P., Helaakoski,T., Myllyharju,J., Veijola,J.,
            Pihlajaniemi,T. and Kivirikko,K.I.
  TITLE     Cloning of the human prolyl 4-hydroxylase alpha subunit isoform
            alpha(II) and characterization of the type II enzyme tetramer. The
            alpha(I) and alpha(II) subunits do not form a mixed
            alpha(I)alpha(II)beta2 tetramer
  JOURNAL   J Biol Chem 272 (28), 17342-17348 (1997)
   PUBMED   9211872
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC034220.5, U90441.1,
            BC025960.1 and AC063976.5.
            
            Summary: This gene encodes a component of prolyl 4-hydroxylase, a
            key enzyme in collagen synthesis composed of two identical alpha
            subunits and two beta subunits. The encoded protein is one of
            several different types of alpha subunits and provides the major
            part of the catalytic site of the active enzyme. In collagen and
            related proteins, prolyl 4-hydroxylase catalyzes the formation of
            4-hydroxyproline that is essential to the proper three-dimensional
            folding of newly synthesized procollagen chains. Alternatively
            spliced transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1), also known as IIb, encodes
            the longest isoform (1). Variants 1, 5, and 6 all encode the same
            isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U90441.1, SRR14038196.2469953.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.1"
     Protein         1..535
                     /product="prolyl 4-hydroxylase subunit alpha-2 isoform 1
                     precursor"
                     /EC_number="1.14.11.2"
                     /note="C-P4Halpha(II); collagen prolyl 4-hydroxylase
                     alpha(II); procollagen-proline, 2-oxoglutarate
                     4-dioxygenase (proline 4-hydroxylase), alpha polypeptide
                     II; 4-PH alpha 2; prolyl 4-hydroxylase, alpha polypeptide
                     II; procollagen-proline,2-oxoglutarate-4-dioxygenase
                     subunit alpha-2; lncRNA promotes epithelial-mesenchymal
                     transition"
                     /calculated_mol_wt=58566
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2354
     mat_peptide     22..535
                     /product="Prolyl 4-hydroxylase subunit alpha-2.
                     /id=PRO_0000022726"
                     /note="propagated from UniProtKB/Swiss-Prot (O15460.1)"
                     /calculated_mol_wt=58566
     Region          26..157
                     /region_name="P4Ha_N"
                     /note="Prolyl 4-Hydroxylase alpha-subunit, N-terminal
                     region; pfam08336"
                     /db_xref="CDD:462433"
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O15460.1)"
     Region          159..>272
                     /region_name="BamD"
                     /note="Outer membrane protein assembly factor BamD,
                     BamD/ComL family [Cell wall/membrane/envelope biogenesis];
                     COG4105"
                     /db_xref="CDD:443281"
     Region          207..240
                     /region_name="TPR"
                     /note="propagated from UniProtKB/Swiss-Prot (O15460.1)"
     Site            264
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O15460.1)"
     Region          346..519
                     /region_name="P4Hc"
                     /note="Prolyl 4-hydroxylase alpha subunit homologues;
                     smart00702"
                     /db_xref="CDD:214780"
     CDS             1..535
                     /gene="P4HA2"
                     /gene_synonym="lncRNA-PE; MYP25"
                     /coded_by="NM_004199.3:414..2021"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4151.1"
                     /db_xref="GeneID:8974"
                     /db_xref="HGNC:HGNC:8547"
                     /db_xref="MIM:600608"
ORIGIN      
        1 mklwvsallm awfgvlscvq aefftsighm tdliyaekel vqslkeyilv eeaklskiks
       61 wankmealts ksaadaegyl ahpvnayklv krlntdwpal edlvlqdsaa gfianlsvqr
      121 qffptdedei gaakalmrlq dtyrldpgti srgelpgtky qamlsvddcf gmgrsayneg
      181 dyyhtvlwme qvlkqldage eatttksqvl dylsyavfql gdlhralelt rrllsldpsh
      241 eraggnlryf eqlleeerek tltnqteael atpegiyerp vdylperdvy eslcrgegvk
      301 ltprrqkrlf cryhhgnrap qlliapfkee dewdsphivr yydvmsdeei erikeiakpk
      361 laratvrdpk tgvltvasyr vsksswleed ddpvvarvnr rmqhitgltv ktaellqvan
      421 ygvggqyeph fdfsrnderd tfkhlgtgnr vatflnymsd veaggatvfp dlgaaiwpkk
      481 gtavfwynll rsgegdyrtr haacpvlvgc kwvsnkwfhe rgqeflrpcg stevd
//
LOCUS       NP_001295134             133 aa            linear   PRI 21-NOV-2025
DEFINITION  translocon-associated protein subunit gamma isoform 3 [Homo
            sapiens].
ACCESSION   NP_001295134
VERSION     NP_001295134.1
DBSOURCE    REFSEQ: accession NM_001308205.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Hu,Q., Wu,G., Ma,H., Zhang,J. and Yang,Z.
  TITLE     Signal sequence receptor subunit 3: A novel indicator of
            immunosuppressive tumor microenvironment and clinical benefits from
            immunotherapy
  JOURNAL   Cell Signal 111, 110871 (2023)
   PUBMED   37652395
  REMARK    GeneRIF: Signal sequence receptor subunit 3: A novel indicator of
            immunosuppressive tumor microenvironment and clinical benefits from
            immunotherapy.
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Gemmer,M., Chaillet,M.L., van Loenhout,J., Cuevas Arenas,R.,
            Vismpas,D., Grollers-Mulderij,M., Koh,F.A., Albanese,P.,
            Scheltema,R.A., Howes,S.C., Kotecha,A., Fedry,J. and Forster,F.
  TITLE     Visualization of translation and protein biogenesis at the ER
            membrane
  JOURNAL   Nature 614 (7946), 160-167 (2023)
   PUBMED   36697828
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Dmello,C., Sonabend,A., Arrieta,V.A., Zhang,D.Y., Kanojia,D.,
            Chen,L., Gould,A., Zhang,J., Kang,S.J., Winter,J., Horbinski,C.,
            Amidei,C., Gyorffy,B., Cordero,A., Chang,C.L., Castro,B., Hsu,P.,
            Ahmed,A.U., Lesniak,M.S., Stupp,R. and Sonabend,A.M.
  TITLE     Translocon-associated Protein Subunit SSR3 Determines and Predicts
            Susceptibility to Paclitaxel in Breast Cancer and Glioblastoma
  JOURNAL   Clin Cancer Res 28 (14), 3156-3169 (2022)
   PUBMED   35552677
  REMARK    GeneRIF: Translocon-associated Protein Subunit SSR3 Determines and
            Predicts Susceptibility to Paclitaxel in Breast Cancer and
            Glioblastoma.
REFERENCE   4  (residues 1 to 133)
  AUTHORS   Xu,X., Huang,Y., Li,X., Arvan,P. and Liu,M.
  TITLE     The Role of TRAPgamma/SSR3 in Preproinsulin Translocation Into the
            Endoplasmic Reticulum
  JOURNAL   Diabetes 71 (3), 440-452 (2022)
   PUBMED   34857543
  REMARK    GeneRIF: The Role of TRAPgamma/SSR3 in Preproinsulin Translocation
            Into the Endoplasmic Reticulum.
REFERENCE   5  (residues 1 to 133)
  AUTHORS   Dittner-Moormann,S., Lourenco,C.M., Reunert,J., Nishinakamura,R.,
            Tanaka,S.S., Werner,C., Debus,V., Zimmer,K.P., Wetzel,G.,
            Naim,H.Y., Wada,Y., Rust,S. and Marquardt,T.
  TITLE     TRAPgamma-CDG shows asymmetric glycosylation and an effect on
            processing of proteins required in higher organisms
  JOURNAL   J Med Genet 58 (3), 213-216 (2021)
   PUBMED   32332102
  REMARK    GeneRIF: TRAPgamma-CDG shows asymmetric glycosylation and an effect
            on processing of proteins required in higher organisms.
REFERENCE   6  (residues 1 to 133)
  AUTHORS   Ng,B.G., Lourenco,C.M., Losfeld,M.E., Buckingham,K.J., Kircher,M.,
            Nickerson,D.A., Shendure,J., Bamshad,M.J. and Freeze,H.H.
  CONSRTM   University of Washington Center for Mendelian Genomics
  TITLE     Mutations in the translocon-associated protein complex subunit SSR3
            cause a novel congenital disorder of glycosylation
  JOURNAL   J Inherit Metab Dis 42 (5), 993-997 (2019)
   PUBMED   30945312
  REMARK    GeneRIF: Mutations in the translocon-associated protein complex
            subunit SSR3 cause a novel congenital disorder of glycosylation.
REFERENCE   7  (residues 1 to 133)
  AUTHORS   Huang,S., Zhong,W., Shi,Z., Wang,K., Jin,H., Zhang,Z., Wang,H.,
            Wei,Y., Chen,S., Zhou,Q. and He,X.
  TITLE     Overexpression of signal sequence receptor gamma predicts poor
            survival in patients with hepatocellular carcinoma
  JOURNAL   Hum Pathol 81, 47-54 (2018)
   PUBMED   29940286
  REMARK    GeneRIF: SSR3 acts as an oncogene in hepatocellular carcinoma with
            overexpression predicting poor survival.
REFERENCE   8  (residues 1 to 133)
  AUTHORS   Pfeffer,S., Dudek,J., Schaffer,M., Ng,B.G., Albert,S.,
            Plitzko,J.M., Baumeister,W., Zimmermann,R., Freeze,H.H., Engel,B.D.
            and Forster,F.
  TITLE     Dissecting the molecular organization of the translocon-associated
            protein complex
  JOURNAL   Nat Commun 8, 14516 (2017)
   PUBMED   28218252
  REMARK    GeneRIF: Data suggest that the mutation leads to complete absence
            of TRAP gamma (SSR3).
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 133)
  AUTHORS   Chen,H.Z., Wen,Q., Wang,W.J., He,J.P. and Wu,Q.
  TITLE     The orphan nuclear receptor TR3/Nur77 regulates ER stress and
            induces apoptosis via interaction with TRAPgamma
  JOURNAL   Int J Biochem Cell Biol 45 (8), 1600-1609 (2013)
   PUBMED   23660295
  REMARK    GeneRIF: translocon-associated protein subunit gamma (TRAPgamma)
            was identified as a novel TR3 binding partner.
REFERENCE   10 (residues 1 to 133)
  AUTHORS   Hartmann,E., Gorlich,D., Kostka,S., Otto,A., Kraft,R., Knespel,S.,
            Burger,E., Rapoport,T.A. and Prehn,S.
  TITLE     A tetrameric complex of membrane proteins in the endoplasmic
            reticulum
  JOURNAL   Eur J Biochem 214 (2), 375-381 (1993)
   PUBMED   7916687
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA725890.1, BC017203.1,
            AF110647.1, CX786292.1, CN409041.1, BM988383.1, BU532041.1,
            BJ997360.1, AC092927.5 and AI225105.1.
            
            Summary: The signal sequence receptor (SSR) is a glycosylated
            endoplasmic reticulum (ER) membrane receptor associated with
            protein translocation across the ER membrane. The SSR is comprised
            of four membrane proteins/subunits: alpha, beta, gamma, and delta.
            The first two are glycosylated subunits and the latter two are
            non-glycosylated subunits. This gene encodes the gamma subunit,
            which is predicted to span the membrane four times. [provided by
            RefSeq, Aug 2010].
            
            Transcript Variant: This variant (4) lacks a 5' exon, contains an
            alternate 5' terminal exon, uses a downstream start codon, and uses
            an alternate in-frame splice site in the central coding region,
            compared to variant 1. It encodes isoform 3 which is shorter
            compared to isoform 1. Both variants 3 and 4 encode the same
            isoform (3).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA725890.1, SRR14243140.10969112.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.31"
     Protein         1..133
                     /product="translocon-associated protein subunit gamma
                     isoform 3"
                     /note="translocon-associated protein gamma subunit;
                     TRAP-gamma; SSR gamma; translocon-associated protein
                     subunit gamma; TRAP-complex gamma subunit; signal sequence
                     receptor subunit gamma; signal sequence receptor, gamma
                     (translocon-associated protein gamma)"
                     /calculated_mol_wt=14982
     Region          <1..131
                     /region_name="TRAP-gamma"
                     /note="Translocon-associated protein, gamma subunit
                     (TRAP-gamma); pfam07074"
                     /db_xref="CDD:399809"
     CDS             1..133
                     /gene="SSR3"
                     /gene_synonym="TRAPG"
                     /coded_by="NM_001308205.2:157..558"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS82865.1"
                     /db_xref="GeneID:6747"
                     /db_xref="HGNC:HGNC:11325"
                     /db_xref="MIM:606213"
ORIGIN      
        1 mdliqsavly svmtlvstyl vafayknvkf vlkhkvaqkr edavskevtr klseadnrkm
       61 srkekderil wkknevadye attfsifynn tlflvvviva sffilknfnp tvnyilsisa
      121 ssgliallst gsk
//
LOCUS       NP_001129115             467 aa            linear   PRI 21-NOV-2025
DEFINITION  dynactin subunit 4 isoform a [Homo sapiens].
ACCESSION   NP_001129115
VERSION     NP_001129115.1
DBSOURCE    REFSEQ: accession NM_001135643.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Su,X., Li,H., Chen,S. and Qin,C.
  TITLE     Study on the Prognostic Values of Dynactin Genes in Low-Grade
            Glioma
  JOURNAL   Technol Cancer Res Treat 20, 15330338211010143 (2021)
   PUBMED   33896271
  REMARK    GeneRIF: Study on the Prognostic Values of Dynactin Genes in
            Low-Grade Glioma.
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Ayalon,G., Davis,J.Q., Scotland,P.B. and Bennett,V.
  TITLE     An ankyrin-based mechanism for functional organization of
            dystrophin and dystroglycan
  JOURNAL   Cell 135 (7), 1189-1200 (2008)
   PUBMED   19109891
REFERENCE   7  (residues 1 to 467)
  AUTHORS   Lim,C.M., Cater,M.A., Mercer,J.F. and La Fontaine,S.
  TITLE     Copper-dependent interaction of dynactin subunit p62 with the N
            terminus of ATP7B but not ATP7A
  JOURNAL   J Biol Chem 281 (20), 14006-14014 (2006)
   PUBMED   16554302
  REMARK    GeneRIF: ATP7B interaction with p62 is a key component of the
            copper-induced trafficking pathway that delivers ATP7B to subapical
            vesicles of hepatocytes for the removal of excess copper into bile
REFERENCE   8  (residues 1 to 467)
  AUTHORS   Boultwood,J., Fidler,C., Strickson,A.J., Watkins,F., Kostrzewa,M.,
            Jaju,R.J., Muller,U. and Wainscoat,J.S.
  TITLE     Transcription mapping of the 5q- syndrome critical region: cloning
            of two novel genes and sequencing, expression, and mapping of a
            further six novel cDNAs
  JOURNAL   Genomics 66 (1), 26-34 (2000)
   PUBMED   10843801
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Karki,S., Tokito,M.K. and Holzbaur,E.L.
  TITLE     A dynactin subunit with a highly conserved cysteine-rich motif
            interacts directly with Arp1
  JOURNAL   J Biol Chem 275 (7), 4834-4839 (2000)
   PUBMED   10671518
REFERENCE   10 (residues 1 to 467)
  AUTHORS   Bingham,J.B. and Schroer,T.A.
  TITLE     Self-regulated polymerization of the actin-related protein Arp1
  JOURNAL   Curr Biol 9 (4), 223-226 (1999)
   PUBMED   10074429
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC321382.1, AK307757.1, AL162085.1 and AC008453.6.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK307757.1, SRR1803617.268716.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..467
                     /product="dynactin subunit 4 isoform a"
                     /note="dynactin p62 subunit; dynactin subunit p62;
                     dynactin 4 (p62)"
                     /calculated_mol_wt=53021
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9UJW0.1)"
     Region          23..348
                     /region_name="Dynactin_p62"
                     /note="Dynactin p62 family; pfam05502"
                     /db_xref="CDD:428497"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UJW0.1)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUR2; propagated from
                     UniProtKB/Swiss-Prot (Q9UJW0.1)"
     CDS             1..467
                     /gene="DCTN4"
                     /gene_synonym="DYN4; P62"
                     /coded_by="NM_001135643.2:25..1428"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47310.1"
                     /db_xref="GeneID:51164"
                     /db_xref="HGNC:HGNC:15518"
                     /db_xref="MIM:614758"
ORIGIN      
        1 masllqsdrv lylvqgekkv raplsqlyfc rycselrsle cvshevdshy cpsclenmps
       61 aeaklkknrc ancfdcpgcm htlstratsi stqlpddpak ttmkkayyla cgfcrwtsrd
      121 vgmadksvas ggwqepenph tqrmnkliey yqqlaqkekv erdrkklarr rnymplafsq
      181 htihvvdkyg lgtrlqrpra gasistlagl slkegedqke ikiepaqavd eveplpedyy
      241 trpvnltevt tlqqrllqpd fqpvcasqly prhkhllikr slrcrkcehn lskpefnpts
      301 ikfkiqlvav nyipevrims ipnlrymkes qvlltltnpv enlthvtlfe ceegdpddin
      361 stakvvvppk elvlagkdaa aeydelaepq dfqddpdiia frkankvgif ikvtpqreeg
      421 evtvcfkmkh dfknlaapir pieesdqgte viwltqhvel slgpllp
//
LOCUS       NP_001372185             173 aa            linear   PRI 21-NOV-2025
DEFINITION  protein tyrosine phosphatase type IVA 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001372185
VERSION     NP_001372185.1
DBSOURCE    REFSEQ: accession NM_001385256.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Cho,M.J., Lee,D.G., Lee,J.W., Hwang,B., Yoon,S.J., Lee,S.J.,
            Park,Y.J., Park,S.H., Lee,H.G., Kim,Y.H., Lee,C.H., Lee,J.,
            Lee,N.K., Han,T.S., Cho,H.S., Moon,J.H., Lee,G.S., Bae,K.H.,
            Hwang,G.S., Lee,S.H., Chung,S.J., Shim,S., Cho,J., Oh,G.T.,
            Kwon,Y.G., Park,J.G. and Min,J.K.
  TITLE     Endothelial PTP4A1 mitigates vascular inflammation via USF1/A20
            axis-mediated NF-kappaB inactivation
  JOURNAL   Cardiovasc Res 119 (5), 1265-1278 (2023)
   PUBMED   36534975
  REMARK    GeneRIF: Endothelial PTP4A1 mitigates vascular inflammation via
            USF1/A20 axis-mediated NF-kappaB inactivation.
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Hu,H., Ye,L. and Liu,Z.
  TITLE     GINS2 regulates the proliferation and apoptosis of colon cancer
            cells through PTP4A1
  JOURNAL   Mol Med Rep 25 (4) (2022)
   PUBMED   35137928
  REMARK    GeneRIF: GINS2 regulates the proliferation and apoptosis of colon
            cancer cells through PTP4A1.
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 173)
  AUTHORS   Li,O., Jiang,B., Yi,W.M., Zhang,Y., Yang,P.Z., Guo,C., Sun,Z.P. and
            Peng,C.
  TITLE     LncRNA NEAT1 promotes cell proliferation, migration, and invasion
            via the miR-186-5p/PTP4A1 axis in cholangiocarcinoma
  JOURNAL   Kaohsiung J Med Sci 37 (5), 379-391 (2021)
   PUBMED   33502823
  REMARK    GeneRIF: LncRNA NEAT1 promotes cell proliferation, migration, and
            invasion via the miR-186-5p/PTP4A1 axis in cholangiocarcinoma.
REFERENCE   6  (residues 1 to 173)
  AUTHORS   Andreev,D.E., O'Connor,P.B., Fahey,C., Kenny,E.M., Terenin,I.M.,
            Dmitriev,S.E., Cormican,P., Morris,D.W., Shatsky,I.N. and
            Baranov,P.V.
  TITLE     Translation of 5' leaders is pervasive in genes resistant to eIF2
            repression
  JOURNAL   Elife 4, e03971 (2015)
   PUBMED   25621764
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 173)
  AUTHORS   Tsujimoto,H., Nishizuka,S., Redpath,J.L. and Stanbridge,E.J.
  TITLE     Differential gene expression in tumorigenic and nontumorigenic HeLa
            x normal human fibroblast hybrid cells
  JOURNAL   Mol Carcinog 26 (4), 298-304 (1999)
   PUBMED   10569806
REFERENCE   8  (residues 1 to 173)
  AUTHORS   Peng,Y., Genin,A., Spinner,N.B., Diamond,R.H. and Taub,R.
  TITLE     The gene encoding human nuclear protein tyrosine phosphatase,
            PRL-1. Cloning, chromosomal localization, and identification of an
            intron enhancer
  JOURNAL   J Biol Chem 273 (27), 17286-17295 (1998)
   PUBMED   9642300
REFERENCE   9  (residues 1 to 173)
  AUTHORS   Dayton,M.A. and Knobloch,T.J.
  TITLE     Multiple phosphotyrosine phosphatase mRNAs are expressed in the
            human lung fibroblast cell line WI-38
  JOURNAL   Recept Signal Transduct 7 (4), 241-256 (1997)
   PUBMED   9633825
REFERENCE   10 (residues 1 to 173)
  AUTHORS   Cates,C.A., Michael,R.L., Stayrook,K.R., Harvey,K.A., Burke,Y.D.,
            Randall,S.K., Crowell,P.L. and Crowell,D.N.
  TITLE     Prenylation of oncogenic human PTP(CAAX) protein tyrosine
            phosphatases
  JOURNAL   Cancer Lett 110 (1-2), 49-55 (1996)
   PUBMED   9018080
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL135905.6.
            
            Summary: This gene encodes a member of a small class of prenylated
            protein tyrosine phosphatases (PTPs), which contain a PTP domain
            and a characteristic C-terminal prenylation motif. The encoded
            protein is a cell signaling molecule that plays regulatory roles in
            a variety of cellular processes, including cell proliferation and
            migration. The protein may also be involved in cancer development
            and metastasis. This tyrosine phosphatase is a nuclear protein, but
            may associate with plasma membrane by means of its prenylation
            motif. Pseudogenes related to this gene are located on chromosomes
            1, 2, 5, 7, 11 and X. [provided by RefSeq, Jun 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749458.1, SRR14038195.1842915.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465405, SAMN04284274
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q12"
     Protein         1..173
                     /product="protein tyrosine phosphatase type IVA 1 isoform
                     1"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase type IVA protein 1;
                     protein-tyrosine phosphatase of regenerating liver 1;
                     PVT1/PTP4A1 fusion; protein tyrosine phosphatase type IVA,
                     member 1"
                     /calculated_mol_wt=19684
     mat_peptide     1..170
                     /product="Protein tyrosine phosphatase type IVA 1.
                     /id=PRO_0000094780"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93096.2)"
                     /calculated_mol_wt=19471
     Region          1..167
                     /region_name="PTP-IVa1"
                     /note="protein tyrosine phosphatase type IVA 1; cd18537"
                     /db_xref="CDD:350513"
     Site            order(5,7,72..73,108..110,137..140,142,144)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:350513"
     Site            order(47,53..54,56,59,64..68)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:350513"
     Region          97..132
                     /region_name="Interaction with ATF5.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93096.2)"
     Site            170
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q93096.2)"
     CDS             1..173
                     /gene="PTP4A1"
                     /gene_synonym="HH72; PRL-1; PRL1; PTP(CAAX1); PTPCAAX1"
                     /coded_by="NM_001385256.1:987..1508"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS4965.1"
                     /db_xref="GeneID:7803"
                     /db_xref="HGNC:HGNC:9634"
                     /db_xref="MIM:601585"
ORIGIN      
        1 marmnrpapv evtyknmrfl ithnptnatl nkfieelkky gvttivrvce atydttlvek
       61 egihvldwpf ddgappsnqi vddwlslvki kfreepgcci avhcvaglgr apvlvalali
      121 eggmkyedav qfirqkrrga fnskqllyle kyrpkmrlrf kdsnghrnnc ciq
//
LOCUS       NP_001373865            1783 aa            linear   PRI 21-NOV-2025
DEFINITION  signal-induced proliferation-associated 1-like protein 1 isoform 2
            [Homo sapiens].
ACCESSION   NP_001373865 XP_024305299
VERSION     NP_001373865.1
DBSOURCE    REFSEQ: accession NM_001386936.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1783)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   2  (residues 1 to 1783)
  AUTHORS   Bentley,S.R., Guella,I., Sherman,H.E., Neuendorf,H.M., Sykes,A.M.,
            Fowdar,J.Y., Silburn,P.A., Wood,S.A., Farrer,M.J. and Mellick,G.D.
  TITLE     Hunting for Familial Parkinson's Disease Mutations in the Post
            Genome Era
  JOURNAL   Genes (Basel) 12 (3), 430 (2021)
   PUBMED   33802862
  REMARK    GeneRIF: Hunting for Familial Parkinson's Disease Mutations in the
            Post Genome Era.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1783)
  AUTHORS   Dolnik,A., Kanwal,N., Mackert,S., Halbedl,S., Proepper,C.,
            Bockmann,J., Schoen,M., Boeckers,T.M., Kuhl,S.J. and
            Schmeisser,M.J.
  TITLE     Sipa1l3/SPAR3 is targeted to postsynaptic specializations and
            interacts with the Fezzin ProSAPiP1/Lzts3
  JOURNAL   J Neurochem 136 (1), 28-35 (2016)
   PUBMED   26364583
  REMARK    GeneRIF: Sipa1L1 is conserved across species, has a distinct
            expression pattern in brain and is localized to excitatory
            postsynapses.
REFERENCE   4  (residues 1 to 1783)
  AUTHORS   Quillen,E.E., Chen,X.D., Almasy,L., Yang,F., He,H., Li,X.,
            Wang,X.Y., Liu,T.Q., Hao,W., Deng,H.W., Kranzler,H.R. and
            Gelernter,J.
  TITLE     ALDH2 is associated to alcohol dependence and is the major genetic
            determinant of 'daily maximum drinks' in a GWAS study of an
            isolated rural Chinese sample
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 165B (2), 103-110 (2014)
   PUBMED   24277619
REFERENCE   5  (residues 1 to 1783)
  AUTHORS   Neveu,G., Cassonnet,P., Vidalain,P.O., Rolloy,C., Mendoza,J.,
            Jones,L., Tangy,F., Muller,M., Demeret,C., Tafforeau,L.,
            Lotteau,V., Rabourdin-Combe,C., Trave,G., Dricot,A., Hill,D.E.,
            Vidal,M., Favre,M. and Jacob,Y.
  TITLE     Comparative analysis of virus-host interactomes with a mammalian
            high-throughput protein complementation assay based on Gaussia
            princeps luciferase
  JOURNAL   Methods 58 (4), 349-359 (2012)
   PUBMED   22898364
REFERENCE   6  (residues 1 to 1783)
  AUTHORS   Benzinger,A., Muster,N., Koch,H.B., Yates,J.R. 3rd and Hermeking,H.
  TITLE     Targeted proteomic analysis of 14-3-3 sigma, a p53 effector
            commonly silenced in cancer
  JOURNAL   Mol Cell Proteomics 4 (6), 785-795 (2005)
   PUBMED   15778465
REFERENCE   7  (residues 1 to 1783)
  AUTHORS   Chih,D.Y., Park,D.J., Gross,M., Idos,G., Vuong,P.T., Hirama,T.,
            Chumakov,A.M., Said,J. and Koeffler,H.P.
  TITLE     Protein partners of C/EBPepsilon
  JOURNAL   Exp Hematol 32 (12), 1173-1181 (2004)
   PUBMED   15588942
REFERENCE   8  (residues 1 to 1783)
  AUTHORS   Lu,Z., Hu,X., Li,Y., Zheng,L., Zhou,Y., Jiang,H., Ning,T.,
            Basang,Z., Zhang,C. and Ke,Y.
  TITLE     Human papillomavirus 16 E6 oncoprotein interferences with insulin
            signaling pathway by binding to tuberin
  JOURNAL   J Biol Chem 279 (34), 35664-35670 (2004)
   PUBMED   15175323
REFERENCE   9  (residues 1 to 1783)
  AUTHORS   Pak,D.T., Yang,S., Rudolph-Correia,S., Kim,E. and Sheng,M.
  TITLE     Regulation of dendritic spine morphology by SPAR, a
            PSD-95-associated RapGAP
  JOURNAL   Neuron 31 (2), 289-303 (2001)
   PUBMED   11502259
REFERENCE   10 (residues 1 to 1783)
  AUTHORS   Gao,Q., Srinivasan,S., Boyer,S.N., Wazer,D.E. and Band,V.
  TITLE     The E6 oncoproteins of high-risk papillomaviruses bind to a novel
            putative GAP protein, E6TP1, and target it for degradation
  JOURNAL   Mol Cell Biol 19 (1), 733-744 (1999)
   PUBMED   9858596
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005476.4, AC004968.1, AC004974.1 and AC004900.2.
            
            On Sep 16, 2020 this sequence version replaced XP_024305299.1.
            
            Transcript Variant: This variant (10), as well as variant 2,
            encodes isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.10286.1,
                                           SRR18074969.845800.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381232.8/ ENSP00000370630.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1783
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.2"
     Protein         1..1783
                     /product="signal-induced proliferation-associated 1-like
                     protein 1 isoform 2"
                     /note="signal-induced proliferation-associated 1-like
                     protein 1; SIPA1-like protein 1; high-risk human papilloma
                     viruses E6 oncoproteins targeted protein 1;
                     spine-associated RapGAP 1"
                     /calculated_mol_wt=197365
     Region          1..157
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Region          277..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Region          380..401
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Region          629..809
                     /region_name="Rap_GAP"
                     /note="Rap/ran-GAP; pfam02145"
                     /db_xref="CDD:460463"
     Region          953..1025
                     /region_name="PDZ_SIPA1-like"
                     /note="PDZ domain of signal-induced
                     proliferation-associated protein 1 (SIPA1), and related
                     domains; cd06745"
                     /db_xref="CDD:467227"
     Site            order(963..969,975,978,1007,1011,1014..1015)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467227"
     Region          1067..1128
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            1078
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1087
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Region          1144..1207
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            1149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1181
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Region          1247..1285
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            1249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1305
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:O35412; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Region          1306..1345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            1309
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:O35412; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1328
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5.
                     /evidence=ECO:0000250|UniProtKB:O35412; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Region          1358..1454
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            1369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Region          1483..1728
                     /region_name="SPAR_C"
                     /note="C-terminal domain of SPAR protein; pfam11881"
                     /db_xref="CDD:463383"
     Region          1484..1515
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            1507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            1530
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1533
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1564
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            1567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1580
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1582
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1629
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1690
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1707
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1708
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Region          1716..1771
                     /region_name="ZapB"
                     /note="Cell division protein ZapB; pfam06005"
                     /db_xref="CDD:428718"
     CDS             1..1783
                     /gene="SIPA1L1"
                     /gene_synonym="E6TP1; SPAR1"
                     /coded_by="NM_001386936.1:553..5904"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS61490.1"
                     /db_xref="GeneID:26037"
                     /db_xref="HGNC:HGNC:20284"
                     /db_xref="MIM:617504"
ORIGIN      
        1 mtslkrsqte rplatdrasv vgtdgtpkvh tddfymrrfr sqngslgssv mapvgpprse
       61 gshhitstpg vpkmgvrari adwpprkeni kessrssqei etsscldsls sksspvsqgs
      121 svslnsndsa mlksiqntlk nktrpsenmd srflmpeayp ssprkalrri rqrsnsditi
      181 seldvdsfde cisptyktgp slhreygsts sidkqgtsge sffdllkgyk ddksdrgptp
      241 tklsdflitg ggkgsgfsld vidgpisqre nlrlfkerek plkrrskset gdssifrklr
      301 nakgeelgks sdlednrsed svrpwtcpkc fahydvqsil fdlneaimnr hnvikrrntt
      361 tgasaaavas lvsgplshsa sfsspmgste dlnskgslsm dqgddksnel vmscpyfrne
      421 iggegerkis lsksnsgsfs gcesasfest lsshctnagv avlevpkenl vlhldrvkry
      481 ivehvdlgay yyrkffyqke hwnyfgaden lgpvavsirr ekpdemkeng spynyriifr
      541 tselmtlrgs vledaipsta khstarglpl kevlehvvpe lnvqclrlaf ntpkvteqlm
      601 kldeqglnyq qkvgimycka gqsteeemyn nesagpafee flqllgervr lkgfekyraq
      661 ldtktdstgt hslyttykdy eimfhvstml pytpnnkqql lrkrhigndi vtivfqepga
      721 qpfspknirs hfqhvfvivr vhnpcsdsvc ysvavtrsrd vpsfgppipk gvtfpksnvf
      781 rdfllakvin aenaahksek framatrtrq eylkdlaekn vtntpidpsg kfpfislask
      841 kkekskpypg aelssmgaiv wavraedynk ameldcllgi snefivlieq etksvvfncs
      901 crdvigwtst dtslkifyer gecvsvgsfi nieeikeivk rlqfvskgce svemtlrrng
      961 lgqlgfhvny egivadvepy gyawqaglrq gsrlveickv avatlsheqm idllrtsvtv
     1021 kvviipphdd ctprrscset yrmpvmeykm negvsyefkf pfrnnnkwqr naskgphspq
     1081 vpsqvqspmt srlnagkgdg kmppperaan iprsissdgr plerrlspgs diyvtvssma
     1141 larsqcrnsp snlssssdtg svggtyrqks mpegfgvsrr spasidrqnt qsdiggsgks
     1201 tpswqrseds iadqmeptch lpavskvlpa frespsgrlm rqdpvvhlsp nkqghsdshy
     1261 sshsssntls snassahsde kwydgdrtes elnsynylqg tsadsgidtt sygpshgsta
     1321 slgaatsspr sgpgkekvap lwhsssevis madrtletes hgldrktess lsldihsksq
     1381 agstpltren stfsindaas htstmssrhs aspvvftsar sspkeelhpa apsqlapsfs
     1441 sssssssgpr sfyprqgats kyligwkkpe gtinsvgfmd trkrhqsdgn eiahtrlras
     1501 trdlraspkp tskstieedl kklidlespt pesqksfkfh alsspqspfp stptsrralh
     1561 rtlsdesiyn sqrehfftsr aslldqalpn dvlfsstyps lpkslplrrp sytlgmkslh
     1621 gefsasdssl tdiqetrrqp mpdpglmplp dtaadldwsn lvdaakayev qrasffaasd
     1681 enhrplsaas nsdqledqal aqmkpysssk dssptlaskv dqlegmlkml redlkkeked
     1741 kahlqaevqh lrednlrlqe esqnasdklk kftewvfnti dms
//
LOCUS       NP_001290371             286 aa            linear   PRI 21-NOV-2025
DEFINITION  protein HEXIM2 isoform 1 [Homo sapiens].
ACCESSION   NP_001290371
VERSION     NP_001290371.1
DBSOURCE    REFSEQ: accession NM_001303442.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Walker,F.M., Sobral,L.M., Danis,E., Sanford,B., Donthula,S.,
            Balakrishnan,I., Wang,D., Pierce,A., Karam,S.D., Kargar,S.,
            Serkova,N.J., Foreman,N.K., Venkataraman,S., Dowell,R., Vibhakar,R.
            and Dahl,N.A.
  TITLE     Rapid P-TEFb-dependent transcriptional reorganization underpins the
            glioma adaptive response to radiotherapy
  JOURNAL   Nat Commun 15 (1), 4616 (2024)
   PUBMED   38816355
  REMARK    GeneRIF: Rapid P-TEFb-dependent transcriptional reorganization
            underpins the glioma adaptive response to radiotherapy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Li,Q., Price,J.P., Byers,S.A., Cheng,D., Peng,J. and Price,D.H.
  TITLE     Analysis of the large inactive P-TEFb complex indicates that it
            contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two
            P-TEFb molecules containing Cdk9 phosphorylated at threonine 186
  JOURNAL   J Biol Chem 280 (31), 28819-28826 (2005)
   PUBMED   15965233
  REMARK    GeneRIF: Positive transcription elongation factor b regulates
            eukaryotic gene expression at the level of elongation and is
            controlled by the reversible association with HEXIM2.
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Fraldi,A., Varrone,F., Napolitano,G., Michels,A.A., Majello,B.,
            Bensaude,O. and Lania,L.
  TITLE     Inhibition of Tat activity by the HEXIM1 protein
  JOURNAL   Retrovirology 2, 42 (2005)
   PUBMED   15992410
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 286)
  AUTHORS   Byers,S.A., Price,J.P., Cooper,J.J., Li,Q. and Price,D.H.
  TITLE     HEXIM2, a HEXIM1-related protein, regulates positive transcription
            elongation factor b through association with 7SK
  JOURNAL   J Biol Chem 280 (16), 16360-16367 (2005)
   PUBMED   15713662
  REMARK    GeneRIF: utilization of HEXIM1 or HEXIM2 to bind and inhibit P-TEFb
            can be differentially regulated in vivo.
REFERENCE   9  (residues 1 to 286)
  AUTHORS   Yik,J.H., Chen,R., Pezda,A.C. and Zhou,Q.
  TITLE     Compensatory contributions of HEXIM1 and HEXIM2 in maintaining the
            balance of active and inactive positive transcription elongation
            factor b complexes for control of transcription
  JOURNAL   J Biol Chem 280 (16), 16368-16376 (2005)
   PUBMED   15713661
  REMARK    GeneRIF: HEXIM2 can functionally and quantitatively compensate for
            the loss of HEXIM1
REFERENCE   10 (residues 1 to 286)
  AUTHORS   Michels,A.A., Nguyen,V.T., Fraldi,A., Labas,V., Edwards,M.,
            Bonnet,F., Lania,L. and Bensaude,O.
  TITLE     MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a
            transcription-dependent manner
  JOURNAL   Mol Cell Biol 23 (14), 4859-4869 (2003)
   PUBMED   12832472
  REMARK    Erratum:[Mol Cell Biol. 2003 Dec;23(24):9405]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI829844.1, CN425800.1 and
            BC025970.1.
            
            Summary: This gene encodes a member of the HEXIM family of
            proteins. This protein is a component of the 7SK small nuclear
            ribonucleoprotein. This protein has been found to negatively
            regulate the kinase activity of the cyclin-dependent kinase P-TEFb,
            which phosphorylates multiple target proteins to promote
            transcriptional elongation. This gene is located approximately 7 kb
            downstream from related family member HEXIM1 on chromosome 17.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2015].
            
            Transcript Variant: This variant (8) differs in the 5' UTR compared
            to variant 1. Variants 1-9 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025970.1, SRR18074968.3692520.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..286
                     /product="protein HEXIM2 isoform 1"
                     /note="hexamethylene-bis-acetamide-inducible transcript 2;
                     hexamethylene bis-acetamide inducible 2; MAQ1 paralog;
                     protein HEXIM2; hexamethylene bis-acetamide-inducible
                     protein 2; hexamethylene bisacetamide inducible 2"
                     /calculated_mol_wt=32287
     Region          1..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Region          102..227
                     /region_name="HEXIM"
                     /note="Hexamethylene bis-acetamide-inducible protein;
                     pfam15313"
                     /db_xref="CDD:464638"
     Region          140..143
                     /region_name="Interaction with P-TEFb"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Region          216..>271
                     /region_name="YabA"
                     /note="Regulator of replication initiation timing YabA
                     [Replication, recombination and repair]; COG4467"
                     /db_xref="CDD:443564"
     Region          226..286
                     /region_name="Interaction with CCNT1, HEXIM1 and HEXIM2.
                     /evidence=ECO:0000269|PubMed:15713661,
                     ECO:0000269|PubMed:15994294"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     CDS             1..286
                     /gene="HEXIM2"
                     /gene_synonym="L3"
                     /coded_by="NM_001303442.2:110..970"
                     /note="isoform 1 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS11496.1"
                     /db_xref="GeneID:124790"
                     /db_xref="HGNC:HGNC:28591"
                     /db_xref="MIM:615695"
ORIGIN      
        1 mmatpnqtac naespvalee aktsgapgsp qtpperhdsg gslpltprme shsededlag
       61 avgglgwnsr sprtqspggc saeavlarkk hrrrpskrkr hwrpylelsw aekqqrderq
      121 sqrasrvree mfakgqpvap ynttqflmnd rdpeepnldv phgishpgss geseagdsdg
      181 rgrahgefqr kdfsetyerf hteslqgrsk qelvrdylel ekrlsqaeee trrlqqlqac
      241 tgqqscrqve elaaevqrlr tenqrlrqen qmwnregcrc deepgt
//
LOCUS       NP_001284506             130 aa            linear   PRI 21-NOV-2025
DEFINITION  astrocytic phosphoprotein PEA-15 isoform b [Homo sapiens].
ACCESSION   NP_001284506
VERSION     NP_001284506.1
DBSOURCE    REFSEQ: accession NM_001297577.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Li,L., Wang,N., Xiong,Y., Guo,G., Zhu,M. and Gu,Y.
  TITLE     Transcription Factor FOSL1 Enhances Drug Resistance of Breast
            Cancer through DUSP7-Mediated Dephosphorylation of PEA15
  JOURNAL   Mol Cancer Res 20 (4), 515-526 (2022)
   PUBMED   34907034
  REMARK    GeneRIF: Transcription Factor FOSL1 Enhances Drug Resistance of
            Breast Cancer through DUSP7-Mediated Dephosphorylation of PEA15.
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Ikedife,J., He,J. and Wei,Y.
  TITLE     PEA-15 engages in allosteric interactions using a common scaffold
            in a phosphorylation-dependent manner
  JOURNAL   Sci Rep 12 (1), 116 (2022)
   PUBMED   34997083
  REMARK    GeneRIF: PEA-15 engages in allosteric interactions using a common
            scaffold in a phosphorylation-dependent manner.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Fiory,F., Formisano,P., Perruolo,G. and Beguinot,F.
  TITLE     Frontiers: PED/PEA-15, a multifunctional protein controlling cell
            survival and glucose metabolism
  JOURNAL   Am J Physiol Endocrinol Metab 297 (3), E592-E601 (2009)
   PUBMED   19531639
  REMARK    GeneRIF: Strategies are being devised to target key signaling
            events in PED/PEA-15 action aimed at improving glucose tolerance
            and at facilitating cancer cell death.
            Review article
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Wolford,J.K., Bogardus,C., Ossowski,V. and Prochazka,M.
  TITLE     Molecular characterization of the human PEA15 gene on 1q21-q22 and
            association with type 2 diabetes mellitus in Pima Indians
  JOURNAL   Gene 241 (1), 143-148 (2000)
   PUBMED   10607908
REFERENCE   6  (residues 1 to 130)
  AUTHORS   Condorelli,G., Vigliotta,G., Iavarone,C., Caruso,M.,
            Tocchetti,C.G., Andreozzi,F., Cafieri,A., Tecce,M.F., Formisano,P.,
            Beguinot,L. and Beguinot,F.
  TITLE     PED/PEA-15 gene controls glucose transport and is overexpressed in
            type 2 diabetes mellitus
  JOURNAL   EMBO J 17 (14), 3858-3866 (1998)
   PUBMED   9670003
REFERENCE   7  (residues 1 to 130)
  AUTHORS   Hwang,S., Kuo,W.L., Cochran,J.F., Guzman,R.C., Tsukamoto,T.,
            Bandyopadhyay,G., Myambo,K. and Collins,C.C.
  TITLE     Assignment of HMAT1, the human homolog of the murine mammary
            transforming gene (MAT1) associated with tumorigenesis, to 1q21.1,
            a region frequently gained in human breast cancers
  JOURNAL   Genomics 42 (3), 540-542 (1997)
   PUBMED   9205133
REFERENCE   8  (residues 1 to 130)
  AUTHORS   Estelles,A., Yokoyama,M., Nothias,F., Vincent,J.D., Glowinski,J.,
            Vernier,P. and Chneiweiss,H.
  TITLE     The major astrocytic phosphoprotein PEA-15 is encoded by two mRNAs
            conserved on their full length in mouse and human
  JOURNAL   J Biol Chem 271 (25), 14800-14806 (1996)
   PUBMED   8662970
REFERENCE   9  (residues 1 to 130)
  AUTHORS   Danziger,N., Yokoyama,M., Jay,T., Cordier,J., Glowinski,J. and
            Chneiweiss,H.
  TITLE     Cellular expression, developmental regulation, and phylogenic
            conservation of PEA-15, the astrocytic major phosphoprotein and
            protein kinase C substrate
  JOURNAL   J Neurochem 64 (3), 1016-1025 (1995)
   PUBMED   7861130
REFERENCE   10 (residues 1 to 130)
  AUTHORS   Araujo,H., Danziger,N., Cordier,J., Glowinski,J. and Chneiweiss,H.
  TITLE     Characterization of PEA-15, a major substrate for protein kinase C
            in astrocytes
  JOURNAL   J Biol Chem 268 (8), 5911-5920 (1993)
   PUBMED   8449955
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA131259.1, DA707281.1,
            BC022554.1 and BC010469.1.
            
            Summary: This gene encodes a death effector domain-containing
            protein that functions as a negative regulator of apoptosis. The
            encoded protein is an endogenous substrate for protein kinase C.
            This protein is also overexpressed in type 2 diabetes mellitus,
            where it may contribute to insulin resistance in glucose uptake.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (3) lacks an alternate exon in the
            5' region and initiates translation at a downstream in-frame start
            codon, compared to variant 1. The encoded isoform (b) has a shorter
            N-terminus than isoform a. Variants 2 and 3 encode the same isoform
            (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.111935.1,
                                           SRR3476690.1142319.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.2"
     Protein         1..130
                     /product="astrocytic phosphoprotein PEA-15 isoform b"
                     /note="homolog of mouse MAT-1 oncogene; astrocytic
                     phosphoprotein PEA-15; phosphoprotein enriched in
                     diabetes; 15 kDa phosphoprotein enriched in astrocytes;
                     mammary transforming gene 1, mouse, homolog of;
                     phosphoprotein enriched in astrocytes 15; proliferation
                     and apoptosis adaptor 15"
                     /calculated_mol_wt=14909
     Region          2..85
                     /region_name="DED_PEA15"
                     /note="Death Effector Domain of Astrocyte phosphoprotein
                     PEA-15; cd08338"
                     /db_xref="CDD:260045"
     Site            order(14,19,68..69,71..74,76..77,80)
                     /site_type="other"
                     /note="ERK2 interaction site [polypeptide binding]"
                     /db_xref="CDD:260045"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15121.2)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62048; propagated from
                     UniProtKB/Swiss-Prot (Q15121.2)"
     Region          98..107
                     /region_name="Microtubule-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15121.2)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15121.2)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15121.2)"
     Region          122..129
                     /region_name="Microtubule-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15121.2)"
     CDS             1..130
                     /gene="PEA15"
                     /gene_synonym="HMAT1; HUMMAT1H; MAT1; MAT1H; PEA-15; PED;
                     PED-PEA15; PED/PEA15"
                     /coded_by="NM_001297577.2:247..639"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS1199.1"
                     /db_xref="GeneID:8682"
                     /db_xref="HGNC:HGNC:8822"
                     /db_xref="MIM:603434"
ORIGIN      
        1 maeygtllqd ltnnitledl eqlksacked ipsekseeit tgsawfsfle shnkldkdnl
       61 syiehifeis rrpdlltmvv dyrtrvlkis eedeldtklt ripsakkykd iirqpseeei
      121 iklapppkka
//
LOCUS       NP_055860               1190 aa            linear   PRI 21-NOV-2025
DEFINITION  wings apart-like protein homolog isoform 1 [Homo sapiens].
ACCESSION   NP_055860 XP_290471
VERSION     NP_055860.1
DBSOURCE    REFSEQ: accession NM_015045.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1190)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1190)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1190)
  AUTHORS   Haarhuis,J.H.I., van der Weide,R.H., Blomen,V.A., Flach,K.D.,
            Teunissen,H., Willems,L., Brummelkamp,T.R., Rowland,B.D. and de
            Wit,E.
  TITLE     A Mediator-cohesin axis controls heterochromatin domain formation
  JOURNAL   Nat Commun 13 (1), 754 (2022)
   PUBMED   35136067
  REMARK    GeneRIF: A Mediator-cohesin axis controls heterochromatin domain
            formation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1190)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1190)
  AUTHORS   Kumagai,K., Takanashi,M., Ohno,S.I., Harada,Y., Fujita,K.,
            Oikawa,K., Sudo,K., Ikeda,S.I., Nishi,H., Oikawa,K. and Kuroda,M.
  TITLE     WAPL induces cervical intraepithelial neoplasia modulated with
            estrogen signaling without HPV E6/E7
  JOURNAL   Oncogene 40 (21), 3695-3706 (2021)
   PUBMED   33947962
  REMARK    GeneRIF: WAPL induces cervical intraepithelial neoplasia modulated
            with estrogen signaling without HPV E6/E7.
REFERENCE   6  (residues 1 to 1190)
  AUTHORS   Kuroda,M., Oikawa,K., Ohbayashi,T., Yoshida,K., Yamada,K.,
            Mimura,J., Matsuda,Y., Fujii-Kuriyama,Y. and Mukai,K.
  TITLE     A dioxin sensitive gene, mammalian WAPL, is implicated in
            spermatogenesis
  JOURNAL   FEBS Lett 579 (1), 167-172 (2005)
   PUBMED   15620708
REFERENCE   7  (residues 1 to 1190)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   8  (residues 1 to 1190)
  AUTHORS   Kwiatkowski,B.A., Ragoczy,T., Ehly,J. and Schubach,W.H.
  TITLE     Identification and cloning of a novel chromatin-associated protein
            partner of Epstein-Barr nuclear protein 2
  JOURNAL   Exp Cell Res 300 (1), 223-233 (2004)
   PUBMED   15383329
  REMARK    GeneRIF: FOE encodes a protein of 1227 amino acids with a
            functional bipartite nuclear localization signal, an arginine-rich
            motif, a putative nuclear export signal as well as with three
            highly acidic regions and a predicted coiled-coil domain.
REFERENCE   9  (residues 1 to 1190)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   10 (residues 1 to 1190)
  AUTHORS   Fallone,C.A.
  TITLE     Epidemiology of the antibiotic resistance of Helicobacter pylori in
            Canada
  JOURNAL   Can J Gastroenterol 14 (10), 879-882 (2000)
   PUBMED   11111111
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL731569.18 and AL844892.5.
            
            On Mar 22, 2004 this sequence version replaced XP_290471.3.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2491898.1, AB065003.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000298767.10/ ENSP00000298767.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1190
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.2"
     Protein         1..1190
                     /product="wings apart-like protein homolog isoform 1"
                     /note="friend of EBNA2 (Epstein-Barr virus nuclear protein
                     2); wings apart-like protein homolog; friend of EBNA2
                     protein"
                     /calculated_mol_wt=132815
     Region          1..659
                     /region_name="Mediates interaction with the cohesin
                     complex"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Region          46..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Region          73..75
                     /region_name="FGF motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            168
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Region          429..431
                     /region_name="FGF motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Region          453..455
                     /region_name="FGF motif 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Region          459..553
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     Region          638..998
                     /region_name="WAPL"
                     /note="Wings apart-like protein regulation of
                     heterochromatin; pfam07814"
                     /db_xref="CDD:462278"
     Site            904
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z5K2.1)"
     CDS             1..1190
                     /gene="WAPL"
                     /gene_synonym="FOE; KIAA0261; WAPAL"
                     /coded_by="NM_015045.5:451..4023"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7375.1"
                     /db_xref="GeneID:23063"
                     /db_xref="HGNC:HGNC:23293"
                     /db_xref="MIM:610754"
ORIGIN      
        1 mtsrfgktys rkggngsskf devfsnkrtt lstkwgettf maklgqkrpn fkpdiqeipk
       61 kpkveeestg dpfgfdsdde slpvssknla qvkcssyses seaaqleevt svleanskis
      121 hvvvedtvvs dkcfpledtl lgkekstnri veddasissc nklitsdkve nfheehekns
      181 hhihknadds tkkpnaettv aseiketndt wnsqfgkrpe spseispikg svrtglfewd
      241 ndfedirsed cilsldsdpl lemkdddfkn rlenlneaie edivqsvlrp tncrtycran
      301 ktkssqgasn fdklmdgtsq alakansess kdglnqakkg gvscgtsfrg tvgrtrdytv
      361 lhpsclsvcn vtiqdtmers mdeftastpa dlgeagrlrk kadiatsktt trfrpsntks
      421 kkdvkleffg fedhetggde ggsgssnyki kyfgfddlse seddedddcq verktskkrt
      481 ktapspslqp ppesndnsqd sqsgtnnaen ldftedlpgv pesvkkpink qgdkskentr
      541 kifsgpkrsp tkavynarhw nhpdseelpg ppvvkpqsvt vrlsskepnq kddgvfkapa
      601 ppskviktvt iptqpyqdiv talkcrredk elytvvqhvk hfndvvefge nqeftddiey
      661 llsglkstqp lntrclsvis latkcampsf rmhlrahgmv amvfktldds qhhqnlslct
      721 aalmyilsrd rlnmdldras ldlmirllel eqdassakll nekdmnkike kirrlcetvh
      781 nkhldlenit tghlametll sltskragdw fkeelrllgg ldhivdkvke cvdhlsrded
      841 eeklvaslwg aerclrvles vtvhnpenqs yliaykdsql ivssakalqh ceeliqqynr
      901 aedsiclads kplphqnvtn hvgkavedcm raiigvllnl tndnewgstk tgeqdgligt
      961 alncvlqvpk ylpqeqrfdi rvlglgllin lveysarnrh clvnmetscs fdssicsgeg
     1021 ddslriggqv havqalvqlf lereraaqla esktdelikd apttqhdksg ewqetsgeiq
     1081 wvstektdgt eekhkkeeed eeldlnkalq hagkhmedci vasytalllg clcqespinv
     1141 ttvreylpeg dfsimtemlk kflsfmnltc avgttgqksi srvieylehc
//
LOCUS       NP_001382178             242 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb group RING finger protein 3 isoform a [Homo sapiens].
ACCESSION   NP_001382178
VERSION     NP_001382178.1
DBSOURCE    REFSEQ: accession NM_001395249.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Hu,Y., Cheng,Y., Jiang,X., Zhang,Y., Wang,H., Ren,H., Xu,Y.,
            Jiang,J., Wang,Q., Su,H., Zhang,B. and Qiu,X.
  TITLE     PCGF3 promotes the proliferation and migration of non-small cell
            lung cancer cells via the PI3K/AKT signaling pathway
  JOURNAL   Exp Cell Res 400 (2), 112496 (2021)
   PUBMED   33485844
  REMARK    GeneRIF: PCGF3 promotes the proliferation and migration of
            non-small cell lung cancer cells via the PI3K/AKT signaling
            pathway.
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Mu,G., Xiang,Q., Zhang,Z., Liu,C., Zhang,H., Liu,Z., Pang,X.,
            Jiang,J., Xie,Q., Zhou,S., Wang,Z., Hu,K., Wang,Z., Jiang,S.,
            Qin,X. and Cui,Y.
  TITLE     PNPT1 and PCGF3 variants associated with angiotensin-converting
            enzyme inhibitor-induced cough: a nested case-control genome-wide
            study
  JOURNAL   Pharmacogenomics 21 (9), 601-614 (2020)
   PUBMED   32397904
  REMARK    GeneRIF: PNPT1 and PCGF3 variants associated with
            angiotensin-converting enzyme inhibitor-induced cough: a nested
            case-control genome-wide study.
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Purohit,G., Mukherjee,A.K., Sharma,S. and Chowdhury,S.
  TITLE     Extratelomeric Binding of the Telomere Binding Protein TRF2 at the
            PCGF3 Promoter Is G-Quadruplex Motif-Dependent
  JOURNAL   Biochemistry 57 (16), 2317-2324 (2018)
   PUBMED   29589913
  REMARK    GeneRIF: We demonstrate that promoter binding by TRF2 mediates
            PCGF3 promoter activity, and both the N-terminal and C-terminal
            domains of TRF2 are necessary for promoter activity.
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Marcon,E., Ni,Z., Pu,S., Turinsky,A.L., Trimble,S.S., Olsen,J.B.,
            Silverman-Gavrila,R., Silverman-Gavrila,L., Phanse,S., Guo,H.,
            Zhong,G., Guo,X., Young,P., Bailey,S., Roudeva,D., Zhao,D.,
            Hewel,J., Li,J., Graslund,S., Paduch,M., Kossiakoff,A.A.,
            Lupien,M., Emili,A., Wodak,S.J. and Greenblatt,J.
  TITLE     Human-chromatin-related protein interactions identify a demethylase
            complex required for chromosome segregation
  JOURNAL   Cell Rep 8 (1), 297-310 (2014)
   PUBMED   24981860
REFERENCE   7  (residues 1 to 242)
  AUTHORS   Woodsmith,J., Jenn,R.C. and Sanderson,C.M.
  TITLE     Systematic analysis of dimeric E3-RING interactions reveals
            increased combinatorial complexity in human ubiquitination networks
  JOURNAL   Mol Cell Proteomics 11 (7), M111.016162 (2012)
   PUBMED   22493164
REFERENCE   8  (residues 1 to 242)
  AUTHORS   Oudot-Mellakh,T., Cohen,W., Germain,M., Saut,N., Kallel,C.,
            Zelenika,D., Lathrop,M., Tregouet,D.A. and Morange,P.E.
  TITLE     Genome wide association study for plasma levels of natural
            anticoagulant inhibitors and protein C anticoagulant pathway: the
            MARTHA project
  JOURNAL   Br J Haematol 157 (2), 230-239 (2012)
   PUBMED   22443383
REFERENCE   9  (residues 1 to 242)
  AUTHORS   Gao,Z., Zhang,J., Bonasio,R., Strino,F., Sawai,A., Parisi,F.,
            Kluger,Y. and Reinberg,D.
  TITLE     PCGF homologs, CBX proteins, and RYBP define functionally distinct
            PRC1 family complexes
  JOURNAL   Mol Cell 45 (3), 344-356 (2012)
   PUBMED   22325352
REFERENCE   10 (residues 1 to 242)
  AUTHORS   Vandamme,J., Volkel,P., Rosnoblet,C., Le Faou,P. and Angrand,P.O.
  TITLE     Interaction proteomics analysis of polycomb proteins defines
            distinct PRC1 complexes in mammalian cells
  JOURNAL   Mol Cell Proteomics 10 (4), M110.002642 (2011)
   PUBMED   21282530
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107464.5 and AC139887.3.
            
            Summary: The protein encoded by this gene contains a C3HC4 type
            RING finger, which is a motif known to be involved in
            protein-protein interactions. The specific function of this protein
            has not yet been determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.215888.1,
                                           SRR1660809.189977.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..242
                     /product="polycomb group RING finger protein 3 isoform a"
                     /note="ring finger protein 3; polycomb group RING finger
                     protein 3; RING finger protein 3A"
                     /calculated_mol_wt=27984
     Region          4..69
                     /region_name="RING-HC_PCGF3"
                     /note="RING finger found in polycomb group RING finger
                     protein 3 (PCGF3) and similar proteins; cd16735"
                     /db_xref="CDD:438393"
     Site            order(16,20,22..23,26,28..29,31..35,38..41,43..44)
                     /site_type="other"
                     /note="putative heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:438393"
     Region          115..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KNV8.1)"
     Region          132..242
                     /region_name="Interaction with BCORL1.
                     /evidence=ECO:0000269|PubMed:27568929"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KNV8.1)"
     Region          154..236
                     /region_name="RAWUL_PCGF3"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in polycomb group RING finger protein
                     3 (PCGF3) and similar proteins; cd17083"
                     /db_xref="CDD:340603"
     CDS             1..242
                     /gene="PCGF3"
                     /gene_synonym="DONG1; RNF3; RNF3A"
                     /coded_by="NM_001395249.1:264..992"
                     /note="isoform a is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS3339.2"
                     /db_xref="GeneID:10336"
                     /db_xref="HGNC:HGNC:10066"
                     /db_xref="MIM:617543"
ORIGIN      
        1 mltrkiklwd inahitcrlc sgylidattv teclhtfcrs clvkyleenn tcptcrivih
       61 qshplqyigh drtmqdivyk lvpglqeaem rkqrefyhkl gmevpgdikg etcsakqhld
      121 shrngetkad dssnkeaaee kpeedndyhr sdeqvsicle cnssklrglk rkwircsaqa
      181 tvlhlkkfia kklnlssfne ldilcneeil gkdhtlkfvv vtrwrfkkap lllhyrpkmd
      241 ll
//
LOCUS       NP_055599               1522 aa            linear   PRI 21-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 11 isoform 1 [Homo sapiens].
ACCESSION   NP_055599
VERSION     NP_055599.1
DBSOURCE    REFSEQ: accession NM_014784.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1522)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1522)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   3  (residues 1 to 1522)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1522)
  AUTHORS   Castillo-Kauil,A., Garcia-Jimenez,I., Cervantes-Villagrana,R.D.,
            Adame-Garcia,S.R., Beltran-Navarro,Y.M., Gutkind,J.S.,
            Reyes-Cruz,G. and Vazquez-Prado,J.
  TITLE     Galphas directly drives PDZ-RhoGEF signaling to Cdc42
  JOURNAL   J Biol Chem 295 (50), 16920-16928 (2020)
   PUBMED   33023908
  REMARK    GeneRIF: Galphas directly drives PDZ-RhoGEF signaling to Cdc42.
REFERENCE   5  (residues 1 to 1522)
  AUTHORS   Du,J., Zhu,Z., Xu,L., Chen,X., Li,X., Lan,T., Li,W., Yuan,K. and
            Zeng,Y.
  TITLE     ARHGEF11 promotes proliferation and epithelial-mesenchymal
            transition of hepatocellular carcinoma through activation of
            beta-catenin pathway
  JOURNAL   Aging (Albany NY) 12 (20), 20235-20253 (2020)
   PUBMED   33122451
  REMARK    GeneRIF: ARHGEF11 promotes proliferation and epithelial-mesenchymal
            transition of hepatocellular carcinoma through activation of
            beta-catenin pathway.
REFERENCE   6  (residues 1 to 1522)
  AUTHORS   Longenecker,K.L., Lewis,M.E., Chikumi,H., Gutkind,J.S. and
            Derewenda,Z.S.
  TITLE     Structure of the RGS-like domain from PDZ-RhoGEF: linking
            heterotrimeric g protein-coupled signaling to Rho GTPases
  JOURNAL   Structure 9 (7), 559-569 (2001)
   PUBMED   11470431
REFERENCE   7  (residues 1 to 1522)
  AUTHORS   Jackson,M., Song,W., Liu,M.Y., Jin,L., Dykes-Hoberg,M., Lin,C.I.,
            Bowers,W.J., Federoff,H.J., Sternweis,P.C. and Rothstein,J.D.
  TITLE     Modulation of the neuronal glutamate transporter EAAT4 by two
            interacting proteins
  JOURNAL   Nature 410 (6824), 89-93 (2001)
   PUBMED   11242047
REFERENCE   8  (residues 1 to 1522)
  AUTHORS   Togashi,H., Nagata,K., Takagishi,M., Saitoh,N. and Inagaki,M.
  TITLE     Functions of a rho-specific guanine nucleotide exchange factor in
            neurite retraction. Possible role of a proline-rich motif of
            KIAA0380 in localization
  JOURNAL   J Biol Chem 275 (38), 29570-29578 (2000)
   PUBMED   10900204
REFERENCE   9  (residues 1 to 1522)
  AUTHORS   Rumenapp,U., Blomquist,A., Schworer,G., Schablowski,H., Psoma,A.
            and Jakobs,K.H.
  TITLE     Rho-specific binding and guanine nucleotide exchange catalysis by
            KIAA0380, a dbl family member
  JOURNAL   FEBS Lett 459 (3), 313-318 (1999)
   PUBMED   10526156
  REMARK    Erratum:[FEBS Lett 2000 Feb 4;467(1):134-5]
REFERENCE   10 (residues 1 to 1522)
  AUTHORS   Fukuhara,S., Murga,C., Zohar,M., Igishi,T. and Gutkind,J.S.
  TITLE     A novel PDZ domain containing guanine nucleotide exchange factor
            links heterotrimeric G proteins to Rho
  JOURNAL   J Biol Chem 274 (9), 5868-5879 (1999)
   PUBMED   10026210
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157713.10, BC057394.2 and
            AB002378.1.
            
            Summary: Rho GTPases play a fundamental role in numerous cellular
            processes that are initiated by extracellular stimuli that work
            through G protein coupled receptors. The encoded protein may form a
            complex with G proteins and stimulate Rho-dependent signals. A
            similar protein in rat interacts with glutamate transporter EAAT4
            and modulates its glutamate transport activity. Expression of the
            rat protein induces the reorganization of the actin cytoskeleton
            and its overexpression induces the formation of membrane ruffling
            and filopodia. Two alternative transcripts encoding different
            isoforms have been described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the predominant
            isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB002378.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1522
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.1"
     Protein         1..1522
                     /product="rho guanine nucleotide exchange factor 11
                     isoform 1"
                     /note="Rho guanine exchange factor (GEF) 11; RhoA-specific
                     guanine nucleotide exchange factor; RhoGEF glutamate
                     transport modulator; glutamate transporter
                     EAAT4-associated protein 48; Rho guanine nucleotide
                     exchange factor (GEF) 11"
                     /calculated_mol_wt=167574
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15085.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ES67; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Region          45..120
                     /region_name="PDZ_ARHGEF11-12-like"
                     /note="PDZ domain of ARHGEF11, ARHGEF12, and related
                     domains; cd23069"
                     /db_xref="CDD:467282"
     Site            order(56..62,70,73,102,106,109..110)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467282"
     Region          128..175
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15085.1)"
     Region          200..231
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15085.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ES67; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Region          263..286
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15085.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ES67; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Region          290..434
                     /region_name="RGS_PDZRhoGEF"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the PDZ-Rho guanine nucleotide exchange factor (RhoGEF)
                     protein; cd08753"
                     /db_xref="CDD:188707"
     Site            order(290..296,298..300,332..335,422,424..427,429..431,
                     434)
                     /site_type="other"
                     /note="G-alpha-13 interaction site"
                     /db_xref="CDD:188707"
     Region          490..555
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15085.1)"
     Site            556
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Region          573..680
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15085.1)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Site            663
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O15085.1)"
     Site            672
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Region          735..921
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(741,745,844,872..873,876..877,879..880,883..884,
                     887..888,891,917,921)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          939..1081
                     /region_name="PH_PRG"
                     /note="PDZ Rho guanine nucleotide exchange factor
                     Pleckstrin homology (PH) domain; cd13391"
                     /db_xref="CDD:275426"
     Site            order(978,1032,1034..1035,1037..1038,1044,1046,1048..1050,
                     1052,1055..1056)
                     /site_type="other"
                     /note="activated RhoA binding site [polypeptide binding]"
                     /db_xref="CDD:275426"
     Site            order(1037..1041,1063..1064)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:275426"
     Site            order(1065,1068)
                     /site_type="other"
                     /note="RhoA binding site [polypeptide binding]"
                     /db_xref="CDD:275426"
     Region          1084..1141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15085.1)"
     Site            1155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Region          1172..>1522
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          1223..1320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15085.1)"
     Site            1295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Site            1300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Region          1332..1423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15085.1)"
     Region          1453..1522
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15085.1)"
     Site            1457
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Site            1458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Site            1462
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Site            1475
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     Site            1480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15085.1)"
     CDS             1..1522
                     /gene="ARHGEF11"
                     /gene_synonym="GTRAP48; PDZ-RHOGEF"
                     /coded_by="NM_014784.4:1413..5981"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1162.1"
                     /db_xref="GeneID:9826"
                     /db_xref="HGNC:HGNC:14580"
                     /db_xref="MIM:605708"
ORIGIN      
        1 msvrlpqsid rlsslsslgd saperkspsh hrqpsdaset tglvqrcvii qkdqhgfgft
       61 vsgdrivlvq svrpggaamk agvkegdrii kvngtmvtns shlevvklik sgayvaltll
      121 gsspssmgis glqqdpspag apritsvips pppppplppp qritgpkplq dpevqkhatq
      181 ilrnmlrqee kelqdilply gdtsqrpseg rlsldsqegd sgldsgterf pslseslmnr
      241 nsvlsdpgld sprtspvima rvaqhhrrqg sdaavpstgd qgvdqspkpl iigpeedydp
      301 gyfnnesdii fqdleklksr pahlgvflry ifsqadpspl lfylcaevyq qaspkdsrsl
      361 gkdiwnifle knaplrvkip emlqaeidsr lrnsedargv lceaqeaamp eiqeqihdyr
      421 tkrtlglgsl ygendlldld gdplrerqva ekqlaalgdi lskyeedrsa pmdfalntym
      481 shagirlrea rpsntaekaq sapdkdkwlp ffpktkkssn skkekdaled kkrnpilkyi
      541 gkpksssqst fhiplspvev kpgnvrniiq hfennqqyda pepgtqrlst gsfpedlles
      601 dssrseirlg rseslkgree mkrsrkaenv prsrsdvdmd aaaeatrlhq sassstssls
      661 trslenptpp ftpkmgrrsi espslgfctd tllphlledd lgqlsdlepe pdaqnwqhtv
      721 gkdvvagltq reidrqevin elfvteashl rtlrvldlif yqrmkkenlm preelarlfp
      781 nlpelieihn swceamkklr eegpiikeis dlmlarfdgp areelqqvaa qfcsyqsial
      841 eliktkqrke srfqlfmqea eshpqcrrlq lrdliisemq rltkypllle siikhteggt
      901 seheklcrar dqcreilkyv neavkqtenr hrlegyqkrl datalerasn plaaefksld
      961 lttrkmiheg pltwriskdk tldlhvllle dllvllqkqd eklllkchsk tavgssdskq
     1021 tfspvlklna vlirsvatdk raffiictsk lgppqiyelv altssdkntw melleeavrn
     1081 atrhpgaapm pvhppppgpr epaqqgptps rvelddsdvf hgepepeelp ggtgsqqrvq
     1141 gkhqvlledp eqegsaeeee lgvlpcpsts ldgenrgirt rnpihlafpg plfmeglads
     1201 aledvenlrh lilwsllpgh tmetqaaqep eddltptpsv isvtshpwdp gspgqappgg
     1261 egdntqlagl egerpeqedm glcslehlpp rtrnsgiwes peldrnlaed assteaaggy
     1321 kvvrkaevag skvvpalpes gqsepgppev eggtkatgnc fyvsmpsgpp dsstdhseap
     1381 msppqpdslp agqtepqpql qggnddprrp srsppslalr dvgmifhtie qltlklnrlk
     1441 dmelahrell kslggessgg ttpvgsfhte aarwtdgsls ppakeplasd srnshelgpc
     1501 pedgsdaple dstadaaasp gp
//
LOCUS       NP_001380285             340 aa            linear   PRI 21-NOV-2025
DEFINITION  citramalyl-CoA lyase, mitochondrial isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001380285
VERSION     NP_001380285.1
DBSOURCE    REFSEQ: accession NM_001393356.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Griffith,C.M., Conrotte,J.F., Paydar,P., Xie,X.,
            Heins-Marroquin,U., Gavotto,F., Jager,C., Ellens,K.W. and
            Linster,C.L.
  TITLE     CLYBL averts vitamin B12 depletion by repairing malyl-CoA
  JOURNAL   Nat Chem Biol 21 (6), 906-915 (2025)
   PUBMED   40108300
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Shen,H., Campanello,G.C., Flicker,D., Grabarek,Z., Hu,J., Luo,C.,
            Banerjee,R. and Mootha,V.K.
  TITLE     The Human Knockout Gene CLYBL Connects Itaconate to Vitamin B12
  JOURNAL   Cell 171 (4), 771-782 (2017)
   PUBMED   29056341
  REMARK    GeneRIF: Study reports that CLYBL loss leads to a cell-autonomous
            defect in the mitochondrial B12 metabolism and that itaconyl-CoA is
            a cofactor-inactivating, substrate-analog inhibitor of the
            mitochondrial B12-dependent methylmalonyl-CoA mutase
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Bossini-Castillo,L., de Kovel,C., Kallberg,H., van 't Slot,R.,
            Italiaander,A., Coenen,M., Tak,P.P., Posthumus,M.D., Wijmenga,C.,
            Huizinga,T., van der Helm-van Mil,A.H., Stoeken-Rijsbergen,G.,
            Rodriguez-Rodriguez,L., Balsa,A., Gonzalez-Alvaro,I.,
            Gonzalez-Gay,M.A., Gomez-Vaquero,C., Franke,B., Vermeulen,S., van
            der Horst-Bruinsma,Ie., Dijkmans,B.A., Wolbink,G.J., Ophoff,R.A.,
            Maehlen,M.T., van Riel,P., Merriman,M., Klareskog,L., Lie,B.A.,
            Merriman,T., Crusius,J.B., Brouwer,E., Martin,J., de Vries,N.,
            Toes,R., Padyukov,L. and Koeleman,B.P.
  CONSRTM   LifeLines Cohort Study
  TITLE     A genome-wide association study of rheumatoid arthritis without
            antibodies against citrullinated peptides
  JOURNAL   Ann Rheum Dis 74 (3), e15 (2015)
   PUBMED   24532677
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Strittmatter,L., Li,Y., Nakatsuka,N.J., Calvo,S.E., Grabarek,Z. and
            Mootha,V.K.
  TITLE     CLYBL is a polymorphic human enzyme with malate synthase and
            beta-methylmalate synthase activity
  JOURNAL   Hum Mol Genet 23 (9), 2313-2323 (2014)
   PUBMED   24334609
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Lin,X., Lu,D., Gao,Y., Tao,S., Yang,X., Feng,J., Tan,A., Zhang,H.,
            Hu,Y., Qin,X., Kim,S.T., Peng,T., Li,L., Mo,L., Zhang,S.,
            Trent,J.M., Mo,Z., Zheng,S.L., Xu,J. and Sun,J.
  TITLE     Genome-wide association study identifies novel loci associated with
            serum level of vitamin B12 in Chinese men
  JOURNAL   Hum Mol Genet 21 (11), 2610-2617 (2012)
   PUBMED   22367966
REFERENCE   7  (residues 1 to 340)
  AUTHORS   Morikawa,J., Nishimura,Y., Uchida,A. and Tanaka,T.
  TITLE     Molecular cloning of novel mouse and human putative citrate lyase
            beta-subunit
  JOURNAL   Biochem Biophys Res Commun 289 (5), 1282-1286 (2001)
   PUBMED   11741334
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL139035.27 and AL137139.9.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1968832 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q32.3"
     Protein         1..340
                     /product="citramalyl-CoA lyase, mitochondrial isoform 1
                     precursor"
                     /EC_number="2.3.3.9"
                     /EC_number="4.1.3.25"
                     /EC_number="3.1.2.30"
                     /note="citrate lyase subunit beta-like protein,
                     mitochondrial; malate synthase; beta-methylmalate
                     synthase; citramalyl-CoA lyase, mitochondrial;
                     (3S)-malyl-CoA thioesterase; citrate lyase beta like"
                     /calculated_mol_wt=35015
     transit_peptide 1..22
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q8N0X4.2)"
                     /calculated_mol_wt=2363
     mat_peptide     23..340
                     /product="Citramalyl-CoA lyase, mitochondrial.
                     /id=PRO_0000286389"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N0X4.2)"
                     /calculated_mol_wt=35015
     Region          44..340
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
     Site            57
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8R4N0; propagated from
                     UniProtKB/Swiss-Prot (Q8N0X4.2)"
     Site            61
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8R4N0; propagated from
                     UniProtKB/Swiss-Prot (Q8N0X4.2)"
     Site            82
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8R4N0; propagated from
                     UniProtKB/Swiss-Prot (Q8N0X4.2)"
     Site            92
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8R4N0; propagated from
                     UniProtKB/Swiss-Prot (Q8N0X4.2)"
     CDS             1..340
                     /gene="CLYBL"
                     /gene_synonym="CLB"
                     /coded_by="NM_001393356.1:7..1029"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS32002.1"
                     /db_xref="GeneID:171425"
                     /db_xref="HGNC:HGNC:18355"
                     /db_xref="MIM:609686"
ORIGIN      
        1 malrllrraa rgaaaaallr lkaslaadip rlgysssshh kyiprravly vpgndekkik
       61 kipslnvdca vldcedgvaa nkknearlri vktledidlg ptekcvrvns vssglaeedl
      121 etllqsrvlp sslmlpkves peeiqwfadk fsfhlkgrkl eqpmnlipfv etamgllnfk
      181 avceetlkvg pqvglfldav vfggedfras igatssketl dilyarqkiv viakafglqa
      241 idlvyidfrd gagllrqsre gaamgftgkq vihpnqiavv qeqfspspek ikwaeeliaa
      301 fkehqqlgkg aftfqgsmid mpllkqaqnt vtlatsikek
//
LOCUS       NP_001135891             288 aa            linear   PRI 21-NOV-2025
DEFINITION  mortality factor 4-like protein 2 [Homo sapiens].
ACCESSION   NP_001135891
VERSION     NP_001135891.1
DBSOURCE    REFSEQ: accession NM_001142419.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Kooblall,K.G., Stokes,V.J., Shariq,O.A., English,K.A.,
            Stevenson,M., Broxholme,J., Wright,B., Lockstone,H.E., Buck,D.,
            Grozinsky-Glasberg,S., Yates,C.J., Thakker,R.V. and Lines,K.E.
  TITLE     miR-3156-5p is downregulated in serum of MEN1 patients and
            regulates expression of MORF4L2
  JOURNAL   Endocr Relat Cancer 29 (10), 557-568 (2022)
   PUBMED   35900839
  REMARK    GeneRIF: miR-3156-5p is downregulated in serum of MEN1 patients and
            regulates expression of MORF4L2.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Zheng,X., Sun,Z., Yu,L., Shi,D., Zhu,M., Yao,H. and Li,L.
  TITLE     Interactome Analysis of the Nucleocapsid Protein of SARS-CoV-2
            Virus
  JOURNAL   Pathogens 10 (9), 1155 (2021)
   PUBMED   34578187
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Cai,Y., Jin,J., Tomomori-Sato,C., Sato,S., Sorokina,I.,
            Parmely,T.J., Conaway,R.C. and Conaway,J.W.
  TITLE     Identification of new subunits of the multiprotein mammalian
            TRRAP/TIP60-containing histone acetyltransferase complex
  JOURNAL   J Biol Chem 278 (44), 42733-42736 (2003)
   PUBMED   12963728
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Yochum,G.S. and Ayer,D.E.
  TITLE     Role for the mortality factors MORF4, MRGX, and MRG15 in
            transcriptional repression via associations with Pf1, mSin3A, and
            Transducin-Like Enhancer of Split
  JOURNAL   Mol Cell Biol 22 (22), 7868-7876 (2002)
   PUBMED   12391155
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Sakai,K., Shirakawa,T., Li,Y., Kitagawa,Y. and Hirose,G.
  TITLE     Interaction of a paraneoplastic cerebellar degeneration-associated
            neuronal protein with the nuclear helix-loop-helix leucine zipper
            protein MRG X
  JOURNAL   Mol Cell Neurosci 19 (4), 477-484 (2002)
   PUBMED   11988016
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Hoja,M.R., Wahlestedt,C. and Hoog,C.
  TITLE     A visual intracellular classification strategy for uncharacterized
            human proteins
  JOURNAL   Exp Cell Res 259 (1), 239-246 (2000)
   PUBMED   10942595
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Bertram,M.J., Berube,N.G., Hang-Swanson,X., Ran,Q., Leung,J.K.,
            Bryce,S., Spurgers,K., Bick,R.J., Baldini,A., Ning,Y., Clark,L.J.,
            Parkinson,E.K., Barrett,J.C., Smith,J.R. and Pereira-Smith,O.M.
  TITLE     Identification of a gene that reverses the immortal phenotype of a
            subset of cells and is a member of a novel family of transcription
            factor-like genes
  JOURNAL   Mol Cell Biol 19 (2), 1479-1485 (1999)
   PUBMED   9891081
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA268606.1, AL049610.9 and BC093013.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.679611.1,
                                           SRR18074968.3415192.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.2"
     Protein         1..288
                     /product="mortality factor 4-like protein 2"
                     /note="MSL3-2 protein; protein MSL3-2; MORF-related gene X
                     protein; transcription factor-like protein MRGX"
                     /calculated_mol_wt=32177
     Region          1..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15014.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15014.1)"
     Region          102..276
                     /region_name="MRG"
                     /note="pfam05712"
                     /db_xref="CDD:461721"
     CDS             1..288
                     /gene="MORF4L2"
                     /gene_synonym="MORFL2; MRGX"
                     /coded_by="NM_001142419.2:327..1193"
                     /db_xref="CCDS:CCDS14512.1"
                     /db_xref="GeneID:9643"
                     /db_xref="HGNC:HGNC:16849"
                     /db_xref="MIM:300409"
ORIGIN      
        1 mssrkqgsqp rgqqsaeeen fkkptrsnmq rskmrgassg kktagpqqkn lepalpgrwg
       61 grsaenppsg svrktrknkq ktpgngdggs tseapqpprk kraradptve seeafknrme
      121 vkvkipeelk pwlvedwdlv trqkqlfqlp akknvdaile eyanckksqg nvdnkeyavn
      181 evvagikeyf nvmlgtqlly kferpqyaei llahpdapms qvygaphllr lfvrigamla
      241 ytpldeksla lllgylhdfl kylaknsasl ftasdykvas aeyhrkal
//
LOCUS       NP_001157973             985 aa            linear   PRI 21-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4E transporter isoform a
            [Homo sapiens].
ACCESSION   NP_001157973
VERSION     NP_001157973.1
DBSOURCE    REFSEQ: accession NM_001164501.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 985)
  AUTHORS   Ding,Y., Chen,S., Jin,J., Sun,Y., Chu,C., Kee,K., Xin,M. and Li,L.
  TITLE     POI-associated EIF4ENIF1 mutations exhibit impaired translation
            regulation abilities
  JOURNAL   Gene 917, 148456 (2024)
   PUBMED   38604507
  REMARK    GeneRIF: POI-associated EIF4ENIF1 mutations exhibit impaired
            translation regulation abilities.
REFERENCE   4  (residues 1 to 985)
  AUTHORS   Zuberek,J., Warzecha,M., Dobrowolski,M. and Modrak-Wojcik,A.
  TITLE     An intramolecular disulphide bond in human 4E-T affects its binding
            to eIF4E1a protein
  JOURNAL   Eur Biophys J 52 (6-7), 497-510 (2023)
   PUBMED   37798395
  REMARK    GeneRIF: An intramolecular disulphide bond in human 4E-T affects
            its binding to eIF4E1a protein.
REFERENCE   5  (residues 1 to 985)
  AUTHORS   Shang,L., Ren,S., Yang,X., Zhang,F., Jin,L., Zhang,X. and Wu,Y.
  TITLE     EIF4ENIF1 variants in two patients with non-syndromic premature
            ovarian insufficiency
  JOURNAL   Eur J Med Genet 65 (10), 104597 (2022)
   PUBMED   36030004
  REMARK    GeneRIF: EIF4ENIF1 variants in two patients with non-syndromic
            premature ovarian insufficiency.
REFERENCE   6  (residues 1 to 985)
  AUTHORS   Andrei,M.A., Ingelfinger,D., Heintzmann,R., Achsel,T.,
            Rivera-Pomar,R. and Luhrmann,R.
  TITLE     A role for eIF4E and eIF4E-transporter in targeting mRNPs to
            mammalian processing bodies
  JOURNAL   RNA 11 (5), 717-727 (2005)
   PUBMED   15840819
  REMARK    GeneRIF: human P bodies contain the cap-binding protein eIF4E and
            the related factor eIF4E-transporter (eIF4E-T), suggesting novel
            roles for these proteins in targeting mRNAs for 5' --> 3'
            degradation
REFERENCE   7  (residues 1 to 985)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   8  (residues 1 to 985)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   9  (residues 1 to 985)
  AUTHORS   Warner,D.R., Roberts,E.A., Greene,R.M. and Pisano,M.M.
  TITLE     Identification of novel Smad binding proteins
  JOURNAL   Biochem Biophys Res Commun 312 (4), 1185-1190 (2003)
   PUBMED   14651998
REFERENCE   10 (residues 1 to 985)
  AUTHORS   Dostie,J., Ferraiuolo,M., Pause,A., Adam,S.A. and Sonenberg,N.
  TITLE     A novel shuttling protein, 4E-T, mediates the nuclear import of the
            mRNA 5' cap-binding protein, eIF4E
  JOURNAL   EMBO J 19 (12), 3142-3156 (2000)
   PUBMED   10856257
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA336484.1, BC033028.1,
            AK314636.1 and BC032941.1.
            
            Summary: The protein encoded by this gene is a nucleocytoplasmic
            shuttle protein for the translation initiation factor eIF4E. This
            shuttle protein interacts with the importin alpha-beta complex to
            mediate nuclear import of eIF4E. It is predominantly cytoplasmic;
            its own nuclear import is regulated by a nuclear localization
            signal and nuclear export signals. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2009].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033028.1, SRR1803614.205155.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..985
                     /product="eukaryotic translation initiation factor 4E
                     transporter isoform a"
                     /note="2610509L04Rik; eukaryotic translation initiation
                     factor 4E transporter; eIF4E transporter; 4E-transporter"
                     /calculated_mol_wt=108070
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          30..711
                     /region_name="EIF4E-T"
                     /note="Nucleocytoplasmic shuttling protein for mRNA
                     cap-binding EIF4E; pfam10477"
                     /db_xref="CDD:371079"
     Region          30..36
                     /region_name="YXXXXLphi motif.
                     /evidence=ECO:0000269|PubMed:10856257,
                     ECO:0000269|PubMed:24335285"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          131..161
                     /region_name="Interaction with CSDE1.
                     /evidence=ECO:0000269|PubMed:27342281"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          195..211
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000305|PubMed:10856257"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          208..230
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          219..240
                     /region_name="Interaction with DDX6.
                     /evidence=ECO:0000269|PubMed:27342281"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22966201,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22966201; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          438..447
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000305|PubMed:10856257"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          448..490
                     /region_name="Interaction with LSM14A.
                     /evidence=ECO:0000269|PubMed:26027925"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            486
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            513
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22966201,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            587
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22966201,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          613..638
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000305|PubMed:10856257"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          664..693
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22966201,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          695..713
                     /region_name="Interaction with PATL1.
                     /evidence=ECO:0000269|PubMed:26027925"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          707..803
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          748..>935
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Site            752
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22966201; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            920
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          922..953
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          940..985
                     /region_name="Interaction with LSM14A.
                     /evidence=ECO:0000269|PubMed:26027925"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            951
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     CDS             1..985
                     /gene="EIF4ENIF1"
                     /gene_synonym="4E-T; Clast4"
                     /coded_by="NM_001164501.2:194..3151"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS13898.1"
                     /db_xref="GeneID:56478"
                     /db_xref="HGNC:HGNC:16687"
                     /db_xref="MIM:607445"
ORIGIN      
        1 mdrrsmgete sgdafldlkk ppaskcphry tkeelldike lphskqrpsc lsekydsdgv
       61 wdpekwhasl ypasgrsspv eslkkeldtd rpslvrrivd prervkeddl dvvlspqrrs
      121 fgggchvtaa vssrrsgspl ekdsdglrll ggrrigsgri isartfekdh rlsdkdlrdl
      181 rdrdrerdfk dkrfrrefgd skrvfgerrr ndsyteeepe wfsagptsqs etieltgfdd
      241 kileedhkgr krtrrrtasv kegivecngg vaeedevevi laqepaadqe vprdavlpeq
      301 spgdfdfnef fnldkvpcla smiedvlgeg svsasrfsrw fsnpsrsgsr ssslgstphe
      361 elerlagleq ailspgqnsg nyfapipled haenkvdile mlqkakvdlk pllsslsank
      421 eklkesshsg vvlsveevea glkglkvdqq vknstpfmae hleetlsavt nnrqlkkdgd
      481 mtafnklvst mkasgtlpsq pkvsrnlesh lmspaeipgq pvpknilqel lgqpvqrpas
      541 snllsglmgs lepttsllgq rapspplsqv fqtraasady lrpripspig ftpgpqqllg
      601 dpfqgmrkpm spitaqmsql elqqaalegl alphdlavqa anfyqpgfgk pqvdrtrdgf
      661 rnrqqrvtks papvhrgnss spapaasits mlspsftpts virkmyeske kskeepasgk
      721 aalgdskedt qkaseenlls sssvpsadrd sspttnskls alqrsscstp lsqanrytke
      781 qdyrpkatgr ktptlaspvp ttpflrpvhq vplvphvpmv rpahqlhpgl vqrmlaqgvh
      841 pqhlpsllqt gvlppgmdls hlqgisgpil gqpfyplpaa shpllnprpg tplhlamvqq
      901 qlqrsvlhpp gsgshaaavs vqttpqnvps rsglphmhsq lehrpsqrss spvglakwfg
      961 sdvlqqplps mpakvisvde leyrq
//
LOCUS       NP_001310470             325 aa            linear   PRI 21-NOV-2025
DEFINITION  F-box/WD repeat-containing protein 4 isoform 2 [Homo sapiens].
ACCESSION   NP_001310470
VERSION     NP_001310470.1
DBSOURCE    REFSEQ: accession NM_001323541.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Song,W., Fu,J., Wu,J., Ren,J., Xiang,R., Kong,C. and Fu,T.
  TITLE     CircFBXW4 Suppresses Colorectal Cancer Progression by Regulating
            the MiR-338-5p/SLC5A7 Axis
  JOURNAL   Adv Sci (Weinh) 11 (18), e2300129 (2024)
   PUBMED   38461489
  REMARK    GeneRIF: CircFBXW4 Suppresses Colorectal Cancer Progression by
            Regulating the MiR-338-5p/SLC5A7 Axis.
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Hauri,S., Comoglio,F., Seimiya,M., Gerstung,M., Glatter,T.,
            Hansen,K., Aebersold,R., Paro,R., Gstaiger,M. and Beisel,C.
  TITLE     A High-Density Map for Navigating the Human Polycomb Complexome
  JOURNAL   Cell Rep 17 (2), 583-595 (2016)
   PUBMED   27705803
REFERENCE   6  (residues 1 to 325)
  AUTHORS   de Mollerat,X.J., Gurrieri,F., Morgan,C.T., Sangiorgi,E.,
            Everman,D.B., Gaspari,P., Amiel,J., Bamshad,M.J., Lyle,R.,
            Blouin,J.L., Allanson,J.E., Le Marec,B., Wilson,M., Braverman,N.E.,
            Radhakrishna,U., Delozier-Blanchet,C., Abbott,A., Elghouzzi,V.,
            Antonarakis,S., Stevenson,R.E., Munnich,A., Neri,G. and
            Schwartz,C.E.
  TITLE     A genomic rearrangement resulting in a tandem duplication is
            associated with split hand-split foot malformation 3 (SHFM3) at
            10q24
  JOURNAL   Hum Mol Genet 12 (16), 1959-1971 (2003)
   PUBMED   12913067
  REMARK    GeneRIF: a complex rearrangement associated with a approximately
            0.5 Mb tandem duplication ion containing a disrupted extra copy of
            the DACTYLIN gene and the entire LBX1 and beta-TRCP genes.
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Ilyin,G.P., Rialland,M., Pigeon,C. and Guguen-Guillouzo,C.
  TITLE     cDNA cloning and expression analysis of new members of the
            mammalian F-box protein family
  JOURNAL   Genomics 67 (1), 40-47 (2000)
   PUBMED   10945468
REFERENCE   8  (residues 1 to 325)
  AUTHORS   Ianakiev,P., Kilpatrick,M.W., Dealy,C., Kosher,R., Korenberg,J.R.,
            Chen,X.N. and Tsipouras,P.
  TITLE     A novel human gene encoding an F-box/WD40 containing protein maps
            in the SHFM3 critical region on 10q24
  JOURNAL   Biochem Biophys Res Commun 261 (1), 64-70 (1999)
   PUBMED   10405324
REFERENCE   9  (residues 1 to 325)
  AUTHORS   Gurrieri,F., Prinos,P., Tackels,D., Kilpatrick,M.W., Allanson,J.,
            Genuardi,M., Vuckov,A., Nanni,L., Sangiorgi,E., Garofalo,G.,
            Nunes,M.E., Neri,G., Schwartz,C. and Tsipouras,P.
  TITLE     A split hand-split foot (SHFM3) gene is located at 10q24-->25
  JOURNAL   Am J Med Genet 62 (4), 427-436 (1996)
   PUBMED   8723077
REFERENCE   10 (residues 1 to 325)
  AUTHORS   Palmer,S.E., Scherer,S.W., Kukolich,M., Wijsman,E.M., Tsui,L.C.,
            Stephens,K. and Evans,J.P.
  TITLE     Evidence for locus heterogeneity in human autosomal dominant split
            hand/split foot malformation
  JOURNAL   Am J Hum Genet 55 (1), 21-26 (1994)
   PUBMED   7912888
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010789.9, AL627144.7 and
            AL627424.8.
            
            Summary: This gene is a member of the F-box/WD-40 gene family,
            which recruit specific target proteins through their WD-40
            protein-protein binding domains for ubiquitin mediated degradation.
            In mouse, a highly similar protein is thought to be responsible for
            maintaining the apical ectodermal ridge of developing limb buds;
            disruption of the mouse gene results in the absence of central
            digits, underdeveloped or absent metacarpal/metatarsal bones and
            syndactyly. This phenotype is remarkably similar to split
            hand-split foot malformation in humans, a clinically heterogeneous
            condition with a variety of modes of transmission. An autosomal
            recessive form has been mapped to the chromosomal region where this
            gene is located, and complex rearrangements involving duplications
            of this gene and others have been associated with the condition. A
            pseudogene of this locus has been mapped to one of the introns of
            the BCR gene on chromosome 22. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BQ943924.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..325
                     /product="F-box/WD repeat-containing protein 4 isoform 2"
                     /note="F-box and WD-40 domain protein 4; F-box/WD repeat
                     protein 4; dactylin; F-box/WD repeat-containing protein 4;
                     F-box and WD-40 domain-containing protein 4; epididymis
                     secretory sperm binding protein"
                     /calculated_mol_wt=36461
     Region          <57..288
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          119..155
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          160..200
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          210..246
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          253..289
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..325
                     /gene="FBXW4"
                     /gene_synonym="DAC; FBW4; FBWD4; SHFM3; SHSF3"
                     /coded_by="NM_001323541.2:58..1035"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:6468"
                     /db_xref="HGNC:HGNC:10847"
                     /db_xref="MIM:608071"
ORIGIN      
        1 mtsvpvkerv kvsqnwrlgr cregillkwr csqmpwmqle ddslyisqan filayqfrpd
       61 gaslnrrplg vfaghdedvc hfvlanshiv saggdgkigi hkihstftvk ysaheqevnc
      121 vdckggiivs gsrdrtakvw plasgrlgqc lhtiqtedrv wsiaisplls sfvtgtaccg
      181 hfsplriwdl nsgqlmthlg sdfppgagvl dvmyespftl lscgydtyvr ywdlrtsvrk
      241 cvmeweephd stlyclqtdg nhllatgssy ygvvrlwdrr qraclhafpl tstplsspvy
      301 clrlttkhly aalsynlhvl dfqnp
//
LOCUS       NP_001341360             912 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA-processing factor 40 homolog A isoform 2 [Homo sapiens].
ACCESSION   NP_001341360 XP_016859944
VERSION     NP_001341360.1
DBSOURCE    REFSEQ: accession NM_001354431.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 912)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 912)
  AUTHORS   Choudhary,B. and Norris,A.
  TITLE     Conserved role for spliceosomal component PRPF40A in microexon
            splicing
  JOURNAL   RNA 31 (1), 43-50 (2024)
   PUBMED   39389624
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 912)
  AUTHORS   Martinez-Lumbreras,S., Trager,L.K., Mulorz,M.M., Payr,M.,
            Dikaya,V., Hipp,C., Konig,J. and Sattler,M.
  TITLE     Intramolecular autoinhibition regulates the selectivity of PRPF40A
            tandem WW domains for proline-rich motifs
  JOURNAL   Nat Commun 15 (1), 3888 (2024)
   PUBMED   38719828
  REMARK    GeneRIF: Intramolecular autoinhibition regulates the selectivity of
            PRPF40A tandem WW domains for proline-rich motifs.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 912)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 912)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 912)
  AUTHORS   Allen,M., Friedler,A., Schon,O. and Bycroft,M.
  TITLE     The structure of an FF domain from human HYPA/FBP11
  JOURNAL   J Mol Biol 323 (3), 411-416 (2002)
   PUBMED   12381297
  REMARK    GeneRIF: Data describe the structure of an FF domain from
            HYPA/FBP11, which differs from those of other
            phosphopeptide-binding domains and represents a novel
            phosphopeptide-binding fold.
REFERENCE   7  (residues 1 to 912)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   8  (residues 1 to 912)
  AUTHORS   Bedford,M.T., Reed,R. and Leder,P.
  TITLE     WW domain-mediated interactions reveal a spliceosome-associated
            protein that binds a third class of proline-rich motif: the proline
            glycine and methionine-rich motif
  JOURNAL   Proc Natl Acad Sci U S A 95 (18), 10602-10607 (1998)
   PUBMED   9724750
REFERENCE   9  (residues 1 to 912)
  AUTHORS   Faber,P.W., Barnes,G.T., Srinidhi,J., Chen,J., Gusella,J.F. and
            MacDonald,M.E.
  TITLE     Huntingtin interacts with a family of WW domain proteins
  JOURNAL   Hum Mol Genet 7 (9), 1463-1474 (1998)
   PUBMED   9700202
REFERENCE   10 (residues 1 to 912)
  AUTHORS   Chan,D.C., Bedford,M.T. and Leder,P.
  TITLE     Formin binding proteins bear WWP/WW domains that bind proline-rich
            peptides and functionally resemble SH3 domains
  JOURNAL   EMBO J 15 (5), 1045-1054 (1996)
   PUBMED   8605874
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079344.5 and AC012443.8.
            
            On Sep 13, 2017 this sequence version replaced XP_016859944.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (2) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..912
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q23.3"
     Protein         1..912
                     /product="pre-mRNA-processing factor 40 homolog A isoform
                     2"
                     /note="formin binding protein 3; Huntingtin-interacting
                     protein A; NY-REN-6 antigen; Fas-ligand associated factor
                     1; formin-binding protein 11; huntingtin yeast partner A;
                     fas ligand-associated factor 1; pre-mRNA processing factor
                     40 homolog A; renal carcinoma antigen NY-REN-6;
                     huntingtin-interacting protein 10; PRP40 pre-mRNA
                     processing factor 40 homolog A"
                     /calculated_mol_wt=103898
     Region          110..751
                     /region_name="PRP40"
                     /note="Splicing factor [RNA processing and modification];
                     COG5104"
                     /db_xref="CDD:227435"
     CDS             1..912
                     /gene="PRPF40A"
                     /gene_synonym="FBP-11; FBP11; FLAF1; FNBP3; HIP-10; HIP10;
                     HYPA; NY-REN-6; Prp40"
                     /coded_by="NM_001354431.4:376..3114"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:55660"
                     /db_xref="HGNC:HGNC:16463"
                     /db_xref="MIM:612941"
ORIGIN      
        1 mcsgsgrrrs slsptmrpgt gaergglmmg hpgmhyapmg mhpmgqranm ppvphgmmpq
       61 mmppmggppm gqmpgmmssv mpgmmmshms qasmqpalpp gvnsmdvaag tasgaksmwt
      121 ehkspdgrty yyntetkqst wekpddlktp aeqllskcpw keyksdsgkp yyynsqtkes
      181 rwakpkeled leamikaees skqeecttts tapvptteip ttmstmaaae aaaavvaaaa
      241 aaaaaaaaan anastsasnt vsgtvpvvpe pevtsivatv vdnentvtis teeqaqltst
      301 paiqdqsvev ssntgeetsk qetvadftpk keeeesqpak ktytwntkee akqafkellk
      361 ekrvpsnasw eqamkmiind prysalakls ekkqafnayk vqtekeekee arskykeake
      421 sfqrflenhe kmtsttrykk aeqmfgemev wnaiserdrl eiyedvlffl skkekeqakq
      481 lrkrnwealk nildnmanvt ysttwseaqq ylmdnptfae deelqnmdke dalicfeehi
      541 ralekeeeee kqksllrerr rqrknresfq ifldelhehg qlhsmsswme lyptissdir
      601 ftnmlgqpgs taldlfkfyv edlkaryhde kkiikdilkd kgfvvevntt fedfvaiiss
      661 tkrsttldag niklafnsll ekaearerer ekeearkmkr kesafksmlk qaappielda
      721 vwedirerfv kepafeditl eserkrifkd fmhvlehecq hhhsknkkhs kkskkhhrkr
      781 srsrsgsdsd dddshskkkr qrsesrsase hsssaesers ykkskkhkkk skkrrhksds
      841 pesdaerekd kkekdresek drtrqrsesk hkspkkktgk dsgnwdtsgs elsegelekr
      901 rrtlleqldd dq
//
LOCUS       NP_001365776             243 aa            linear   PRI 21-NOV-2025
DEFINITION  myeloid leukemia factor 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001365776
VERSION     NP_001365776.1
DBSOURCE    REFSEQ: accession NM_001378847.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Tang,Z., Yang,Y., Chen,W. and Liang,T.
  TITLE     Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling
  JOURNAL   Hepatol Commun 7 (8), e0204 (2023)
   PUBMED   37486965
  REMARK    GeneRIF: Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Huang,D., Liu,C., Sun,X., Sun,X., Qu,Y., Tang,Y., Li,G. and Tong,T.
  TITLE     CRL4DCAF8 and USP11 oppositely regulate the stability of myeloid
            leukemia factors (MLFs)
  JOURNAL   Biochem Biophys Res Commun 529 (2), 127-132 (2020)
   PUBMED   32703400
  REMARK    GeneRIF: CRL4(DCAF8) and USP11 oppositely regulate the stability of
            myeloid leukemia factors (MLFs).
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Darracq,A., Pak,H., Bourgoin,V., Zmiri,F., Dellaire,G., Affar,E.B.
            and Milot,E.
  TITLE     NPM and NPM-MLF1 interact with chromatin remodeling complexes and
            influence their recruitment to specific genes
  JOURNAL   PLoS Genet 15 (11), e1008463 (2019)
   PUBMED   31675375
  REMARK    GeneRIF: the abnormal gene regulation imposed by NPM-MLF1 can be
            characterized by the enhanced recruitment of NuRD to gene
            regulatory regions. Thus, different mechanisms would orchestrate
            the dysregulation of NPM function in NPMc+- versus
            NPM1-MLF1-associated leukemia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Yoneda-Kato,N., Tomoda,K., Umehara,M., Arata,Y. and Kato,J.Y.
  TITLE     Myeloid leukemia factor 1 regulates p53 by suppressing COP1 via
            COP9 signalosome subunit 3
  JOURNAL   EMBO J 24 (9), 1739-1749 (2005)
   PUBMED   15861129
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Hanissian,S.H., Akbar,U., Teng,B., Janjetovic,Z., Hoffmann,A.,
            Hitzler,J.K., Iscove,N., Hamre,K., Du,X., Tong,Y., Mukatira,S.,
            Robertson,J.H. and Morris,S.W.
  TITLE     cDNA cloning and characterization of a novel gene encoding the
            MLF1-interacting protein MLF1IP
  JOURNAL   Oncogene 23 (20), 3700-3707 (2004)
   PUBMED   15116101
REFERENCE   8  (residues 1 to 243)
  AUTHORS   Arber,D.A., Chang,K.L., Lyda,M.H., Bedell,V., Spielberger,R. and
            Slovak,M.L.
  TITLE     Detection of NPM/MLF1 fusion in t(3;5)-positive acute myeloid
            leukemia and myelodysplasia
  JOURNAL   Hum Pathol 34 (8), 809-813 (2003)
   PUBMED   14506644
  REMARK    GeneRIF: These findings suggest that an NPM/MLF1 fusion is the
            primary molecular abnormality in t(3;5) MDS and AML with
            multilineage dysplasia, and that cases with NPM/MLF1 may be
            clinically distinct from other MDS-associated disease
REFERENCE   9  (residues 1 to 243)
  AUTHORS   Lim,R., Winteringham,L.N., Williams,J.H., McCulloch,R.K.,
            Ingley,E., Tiao,J.Y., Lalonde,J.P., Tsai,S., Tilbrook,P.A., Sun,Y.,
            Wu,X., Morris,S.W. and Klinken,S.P.
  TITLE     MADM, a novel adaptor protein that mediates phosphorylation of the
            14-3-3 binding site of myeloid leukemia factor 1
  JOURNAL   J Biol Chem 277 (43), 40997-41008 (2002)
   PUBMED   12176995
  REMARK    GeneRIF: phosphorylation of 14-3-3 binding site by MADM
REFERENCE   10 (residues 1 to 243)
  AUTHORS   Yoneda-Kato,N., Look,A.T., Kirstein,M.N., Valentine,M.B.,
            Raimondi,S.C., Cohen,K.J., Carroll,A.J. and Morris,S.W.
  TITLE     The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid
            leukemia produces a novel fusion gene, NPM-MLF1
  JOURNAL   Oncogene 12 (2), 265-275 (1996)
   PUBMED   8570204
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106707.9 and AC025033.20.
            
            Summary: This gene encodes an oncoprotein which is thought to play
            a role in the phenotypic determination of hemopoetic cells.
            Translocations between this gene and nucleophosmin have been
            associated with myelodysplastic syndrome and acute myeloid
            leukemia. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1660803.141370.1, SRR12921934.1001359.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.32"
     Protein         1..243
                     /product="myeloid leukemia factor 1 isoform 2"
                     /note="myelodysplasia-myeloid leukemia factor 1; testis
                     tissue sperm-binding protein Li 49e"
                     /calculated_mol_wt=27494
     Region          1..177
                     /region_name="Mlf1IP"
                     /note="Myelodysplasia-myeloid leukemia factor
                     1-interacting protein; pfam10248"
                     /db_xref="CDD:463022"
     CDS             1..243
                     /gene="MLF1"
                     /coded_by="NM_001378847.1:574..1305"
                     /note="isoform 2 is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS46945.1"
                     /db_xref="GeneID:4291"
                     /db_xref="HGNC:HGNC:7125"
                     /db_xref="MIM:601402"
ORIGIN      
        1 mrqmirsfse pfgrdllsis dgrgrahnrr ghndgedslt htdvssfqtm dqmvsnmrny
       61 mqklernfgq lsvdpnghsf csssvmtysk igdeppkvfq astqtrrapg giketrkamr
      121 dsdsglekma ighhihdrah vikksknkkt gdeevnqefi nmnesdahaf deewqsevlk
      181 ykpgrhnlgn trmrsvghen pgsrelkrre kpqqspaieh grrsnvlgdk lhikgssvks
      241 nkk
//
LOCUS       NP_001338267             336 aa            linear   PRI 21-NOV-2025
DEFINITION  interleukin-1 receptor-associated kinase 4 isoform b [Homo
            sapiens].
ACCESSION   NP_001338267 XP_006719502
VERSION     NP_001338267.1
DBSOURCE    REFSEQ: accession NM_001351338.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Fisch,D., Zhang,T., Sun,H., Ma,W., Tan,Y., Gygi,S.P., Higgins,D.E.
            and Kagan,J.C.
  TITLE     Molecular definition of the endogenous Toll-like receptor
            signalling pathways
  JOURNAL   Nature 631 (8021), 635-644 (2024)
   PUBMED   38961291
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Liu,Y., Yuan,J., Zhang,Y., Qin,F., Bai,X., Sun,W., Chen,T., Liu,F.,
            Zheng,Y., Qi,X., Zhao,W., Liu,B. and Gao,C.
  TITLE     OTUD5 promotes the inflammatory immune response by enhancing MyD88
            oligomerization and Myddosome formation
  JOURNAL   Cell Death Differ 31 (6), 753-767 (2024)
   PUBMED   38605168
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Peterson,J., Balogh Sivars,K., Bianco,A. and Roper,K.
  TITLE     Toll-like receptor signalling via IRAK4 affects epithelial
            integrity and tightness through regulation of junctional tension
  JOURNAL   Development 150 (24) (2023)
   PUBMED   37997696
  REMARK    GeneRIF: Toll-like receptor signalling via IRAK4 affects epithelial
            integrity and tightness through regulation of junctional tension.
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Cooray,S., Price-Kuehne,F., Hong,Y., Omoyinmi,E., Burleigh,A.,
            Gilmour,K.C., Ahmad,B., Choi,S., Bahar,M.W., Torpiano,P.,
            Gagunashvili,A., Jensen,B., Bellos,E., Sancho-Shimizu,V.,
            Herberg,J.A., Mankad,K., Kumar,A., Kaliakatsos,M., Worth,A.J.J.,
            Eleftheriou,D., Whittaker,E. and Brogan,P.A.
  TITLE     Neuroinflammation, autoinflammation, splenomegaly and anemia caused
            by bi-allelic mutations in IRAK4
  JOURNAL   Front Immunol 14, 1231749 (2023)
   PUBMED   37744344
  REMARK    GeneRIF: Neuroinflammation, autoinflammation, splenomegaly and
            anemia caused by bi-allelic mutations in IRAK4.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Wang,Z., Liu,J., Sudom,A., Ayres,M., Li,S., Wesche,H., Powers,J.P.
            and Walker,N.P.
  TITLE     Crystal structures of IRAK-4 kinase in complex with inhibitors: a
            serine/threonine kinase with tyrosine as a gatekeeper
  JOURNAL   Structure 14 (12), 1835-1844 (2006)
   PUBMED   17161373
  REMARK    GeneRIF: crystallographic analysis of IRAK-4 kinase in complex with
            inhibitors
REFERENCE   6  (residues 1 to 336)
  AUTHORS   Suzuki,N. and Saito,T.
  TITLE     IRAK-4--a shared NF-kappaB activator in innate and acquired
            immunity
  JOURNAL   Trends Immunol 27 (12), 566-572 (2006)
   PUBMED   17046325
  REMARK    GeneRIF: Although each system seems to possess distinct activation
            mechanisms, interleukin-1 receptor-associated kinase (IRAK)-4 is
            essential for NF-kappaB activation in Toll-like receptor (TLR) and
            T-cell receptor (TCR) signaling pathways.
            Review article
REFERENCE   7  (residues 1 to 336)
  AUTHORS   Burns,K., Clatworthy,J., Martin,L., Martinon,F., Plumpton,C.,
            Maschera,B., Lewis,A., Ray,K., Tschopp,J. and Volpe,F.
  TITLE     Tollip, a new component of the IL-1RI pathway, links IRAK to the
            IL-1 receptor
  JOURNAL   Nat Cell Biol 2 (6), 346-351 (2000)
   PUBMED   10854325
REFERENCE   8  (residues 1 to 336)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   9  (residues 1 to 336)
  AUTHORS   Scherer,D.C., Brockman,J.A., Chen,Z., Maniatis,T. and Ballard,D.W.
  TITLE     Signal-induced degradation of I kappa B alpha requires
            site-specific ubiquitination
  JOURNAL   Proc Natl Acad Sci U S A 92 (24), 11259-11263 (1995)
   PUBMED   7479976
REFERENCE   10 (residues 1 to 336)
  AUTHORS   Siu,G., Strauss,E.C., Lai,E. and Hood,L.E.
  TITLE     Analysis of a human V beta gene subfamily
  JOURNAL   J Exp Med 164 (5), 1600-1614 (1986)
   PUBMED   3772297
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093012.9 and AK027301.2.
            
            On May 6, 2017 this sequence version replaced XP_006719502.1.
            
            Summary: This gene encodes a kinase that activates NF-kappaB in
            both the Toll-like receptor (TLR) and T-cell receptor (TCR)
            signaling pathways. The protein is essential for most innate immune
            responses. Mutations in this gene result in IRAK4 deficiency and
            recurrent invasive pneumococcal disease. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (6), as well as variants 3-5 and
            7-10, encodes isoform b.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2941474.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..336
                     /product="interleukin-1 receptor-associated kinase 4
                     isoform b"
                     /EC_number="2.7.11.1"
                     /note="renal carcinoma antigen NY-REN-64"
                     /calculated_mol_wt=37543
     Region          46..333
                     /region_name="STKc_IRAK4"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Interleukin-1 Receptor Associated Kinase 4; cd14158"
                     /db_xref="CDD:271060"
     Site            order(68..72,76,87,89,122,138..141,145,147,187,189,
                     191..192,194,205,208,226..229)
                     /site_type="active"
                     /db_xref="CDD:271060"
     Site            order(68..72,76,87,89,122,138..141,145,187,189,191..192,
                     194,205)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271060"
     Site            order(72,145,147,187,189,191,208,226..229)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271060"
     Site            order(204..216,218..229)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271060"
     CDS             1..336
                     /gene="IRAK4"
                     /gene_synonym="IMD67; IPD1; IRAK-4; NY-REN-64; REN64"
                     /coded_by="NM_001351338.2:926..1936"
                     /note="isoform b is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS44862.1"
                     /db_xref="GeneID:51135"
                     /db_xref="HGNC:HGNC:17967"
                     /db_xref="MIM:606883"
ORIGIN      
        1 mpfcdkdrtl mtpvqnleqs ymppdssspe nkslevsdtr fhsfsfyelk nvtnnfderp
       61 isvggnkmge ggfgvvykgy vnnttvavkk laamvditte elkqqfdqei kvmakcqhen
      121 lvellgfssd gddlclvyvy mpngslldrl scldgtppls whmrckiaqg aanginflhe
      181 nhhihrdiks anilldeaft akisdfglar asekfaqtvm tsrivgttay mapealrgei
      241 tpksdiysfg vvlleiitgl pavdehrepq llldikeeie deektiedyi dkkmndadst
      301 sveamysvas qclhekknkr pdikkvqqll qemtas
//
LOCUS       NP_001158028             201 aa            linear   PRI 21-NOV-2025
DEFINITION  disrupted in schizophrenia 1 protein isoform t [Homo sapiens].
ACCESSION   NP_001158028
VERSION     NP_001158028.1
DBSOURCE    REFSEQ: accession NM_001164556.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Pils,M., Rutsch,J., Eren,F., Engberg,G., Piehl,F., Cervenka,S.,
            Sellgren,C., Trossbach,S., Willbold,D., Erhardt,S., Bannach,O. and
            Korth,C.
  TITLE     Disrupted-in-schizophrenia 1 protein aggregates in cerebrospinal
            fluid are elevated in patients with first-episode psychosis
  JOURNAL   Psychiatry Clin Neurosci 77 (12), 665-671 (2023)
   PUBMED   37668563
  REMARK    GeneRIF: Disrupted-in-schizophrenia 1 protein aggregates in
            cerebrospinal fluid are elevated in patients with first-episode
            psychosis.
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Habibi,S., Yaghoubzad-Maleki,M., Heshmati,E. and Khalifeh,K.
  TITLE     Effects of representative point mutations on dynamic behavior of
            the DISC1-Ndel1 complex: a molecular dynamics study
  JOURNAL   J Biomol Struct Dyn 41 (22), 13228-13234 (2023)
   PUBMED   36858606
  REMARK    GeneRIF: Effects of representative point mutations on dynamic
            behavior of the DISC1-Ndel1 complex: a molecular dynamics study.
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Li,W., Jiang,H., Chen,X., Yang,K., Deng,X., Tang,Z., Hu,Z.,
            Zhang,X., Lin,S., Zou,Y. and Wu,H.
  TITLE     The variants in PTPRB, TRAF3IP3, and DISC1 genes were associated
            with Graves' disease in the Chinese population
  JOURNAL   Medicine (Baltimore) 101 (45), e31501 (2022)
   PUBMED   36397361
  REMARK    GeneRIF: The variants in PTPRB, TRAF3IP3, and DISC1 genes were
            associated with Graves' disease in the Chinese population.
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Guardiola-Ripoll,M., Sotero-Moreno,A., Almodovar-Paya,C.,
            Hostalet,N., Guerrero-Pedraza,A., Ramiro,N., Ortiz-Gil,J.,
            Arias,B., Madre,M., Soler-Vidal,J., Salvador,R., McKenna,P.J.,
            Pomarol-Clotet,E. and Fatjo-Vilas,M.
  TITLE     Combining fMRI and DISC1 gene haplotypes to understand working
            memory-related brain activity in schizophrenia
  JOURNAL   Sci Rep 12 (1), 7351 (2022)
   PUBMED   35513527
  REMARK    GeneRIF: Combining fMRI and DISC1 gene haplotypes to understand
            working memory-related brain activity in schizophrenia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 201)
  AUTHORS   Ozeki,Y., Tomoda,T., Kleiderlein,J., Kamiya,A., Bord,L., Fujii,K.,
            Okawa,M., Yamada,N., Hatten,M.E., Snyder,S.H., Ross,C.A. and
            Sawa,A.
  TITLE     Disrupted-in-Schizophrenia-1 (DISC-1): mutant truncation prevents
            binding to NudE-like (NUDEL) and inhibits neurite outgrowth
  JOURNAL   Proc Natl Acad Sci U S A 100 (1), 289-294 (2003)
   PUBMED   12506198
  REMARK    GeneRIF: Mutant truncation prevents binding to NudE-like (NUDEL)
            and inhibits neurite outgrowth
            Erratum:[Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13969]
REFERENCE   7  (residues 1 to 201)
  AUTHORS   Blackwood,D.H., Fordyce,A., Walker,M.T., St Clair,D.M.,
            Porteous,D.J. and Muir,W.J.
  TITLE     Schizophrenia and affective disorders--cosegregation with a
            translocation at chromosome 1q42 that directly disrupts
            brain-expressed genes: clinical and P300 findings in a family
  JOURNAL   Am J Hum Genet 69 (2), 428-433 (2001)
   PUBMED   11443544
REFERENCE   8  (residues 1 to 201)
  AUTHORS   Ekelund,J., Hovatta,I., Parker,A., Paunio,T., Varilo,T., Martin,R.,
            Suhonen,J., Ellonen,P., Chan,G., Sinsheimer,J.S., Sobel,E.,
            Juvonen,H., Arajarvi,R., Partonen,T., Suvisaari,J., Lonnqvist,J.,
            Meyer,J. and Peltonen,L.
  TITLE     Chromosome 1 loci in Finnish schizophrenia families
  JOURNAL   Hum Mol Genet 10 (15), 1611-1617 (2001)
   PUBMED   11468279
REFERENCE   9  (residues 1 to 201)
  AUTHORS   Millar,J.K., Christie,S., Semple,C.A. and Porteous,D.J.
  TITLE     Chromosomal location and genomic structure of the human
            translin-associated factor X gene (TRAX; TSNAX) revealed by
            intergenic splicing to DISC1, a gene disrupted by a translocation
            segregating with schizophrenia
  JOURNAL   Genomics 67 (1), 69-77 (2000)
   PUBMED   10945471
REFERENCE   10 (residues 1 to 201)
  AUTHORS   Millar,J.K., Wilson-Annan,J.C., Anderson,S., Christie,S.,
            Taylor,M.S., Semple,C.A., Devon,R.S., St Clair,D.M., Muir,W.J.,
            Blackwood,D.H. and Porteous,D.J.
  TITLE     Disruption of two novel genes by a translocation co-segregating
            with schizophrenia
  JOURNAL   Hum Mol Genet 9 (9), 1415-1423 (2000)
   PUBMED   10814723
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL626763.11 and FJ804204.1.
            
            Summary: This gene encodes a protein with multiple coiled coil
            motifs which is located in the nucleus, cytoplasm and mitochondria.
            The protein is involved in neurite outgrowth and cortical
            development through its interaction with other proteins. This gene
            is disrupted in a t(1;11)(q42.1;q14.3) translocation which
            segregates with schizophrenia and related psychiatric disorders in
            a large Scottish family. Alternate transcriptional splice variants,
            encoding different isoforms, have been characterized. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (t) lacks four internal exons and
            multiple 3' exons but has an alternate 3' segment, as compared to
            variant L. The resulting isoform (t, also known as isoform 34) is
            the shortest, and has a distinct C-terminus, as compared to isoform
            L.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ804204.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.2"
     Protein         1..201
                     /product="disrupted in schizophrenia 1 protein isoform t"
                     /note="disrupted in schizophrenia 1 protein"
                     /calculated_mol_wt=22067
     CDS             1..201
                     /gene="DISC1"
                     /gene_synonym="C1orf136; SCZD9"
                     /coded_by="NM_001164556.2:79..684"
                     /note="isoform t is encoded by transcript variant t"
                     /db_xref="CCDS:CCDS59207.1"
                     /db_xref="GeneID:27185"
                     /db_xref="HGNC:HGNC:2888"
                     /db_xref="MIM:605210"
ORIGIN      
        1 mpgggpqgap aaaggggvsh raaetlqqrl edleqekisl hfqlpsrqpa lssflghlaa
       61 qvqaalrrga tqqasgddth tplrmeprll eptaqdslhv sitrrdwllq ekqqlqkeie
      121 alqarmfvle akdqqlrrei eeqeqqlqwq gcdltplvgq lslgqlqevs kalqdtlasa
      181 gqipfhaepp etirrkpfld g
//
LOCUS       NP_001333275             480 aa            linear   PRI 21-NOV-2025
DEFINITION  autophagy-related protein 13 isoform f [Homo sapiens].
ACCESSION   NP_001333275 XP_016874103
VERSION     NP_001333275.1
DBSOURCE    REFSEQ: accession NM_001346346.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Patel,A. and Faesen,A.C.
  TITLE     Metamorphosis by ATG13 and ATG101 in human autophagy initiation
  JOURNAL   Autophagy 20 (4), 968-969 (2024)
   PUBMED   37394799
  REMARK    GeneRIF: Metamorphosis by ATG13 and ATG101 in human autophagy
            initiation.
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Nguyen,A. and Faesen,A.C.
  TITLE     The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis
  JOURNAL   FEBS Lett 598 (1), 114-126 (2024)
   PUBMED   37567770
  REMARK    GeneRIF: The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis.
            Review article
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Karabi,Z., Moradian,F. and Kheirabadi,M.
  TITLE     The effect of lactoferrin on ULK1 and ATG13 genes expression in
            breast cancer cell line MCF7 and bioinformatics studies of protein
            interaction between lactoferrin and the autophagy initiation
            complex
  JOURNAL   Cell Biochem Biophys 80 (4), 795-806 (2022)
   PUBMED   36169801
  REMARK    GeneRIF: The effect of lactoferrin on ULK1 and ATG13 genes
            expression in breast cancer cell line MCF7 and bioinformatics
            studies of protein interaction between lactoferrin and the
            autophagy initiation complex.
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Gottschalk,G., Peterson,D., Knox,K., Maynard,M., Whelan,R.J. and
            Roy,A.
  TITLE     Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE)
  JOURNAL   Mol Cell Neurosci 120, 103731 (2022)
   PUBMED   35487443
  REMARK    GeneRIF: Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE).
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Jung,C.H., Jun,C.B., Ro,S.H., Kim,Y.M., Otto,N.M., Cao,J., Kundu,M.
            and Kim,D.H.
  TITLE     ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy
            machinery
  JOURNAL   Mol Biol Cell 20 (7), 1992-2003 (2009)
   PUBMED   19225151
  REMARK    GeneRIF: The ULK-Atg13-FIP200 complexes are direct targets of mTOR
            and important regulators of autophagy in response to mTOR
            signaling.
REFERENCE   7  (residues 1 to 480)
  AUTHORS   Hosokawa,N., Hara,T., Kaizuka,T., Kishi,C., Takamura,A., Miura,Y.,
            Iemura,S., Natsume,T., Takehana,K., Yamada,N., Guan,J.L., Oshiro,N.
            and Mizushima,N.
  TITLE     Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200
            complex required for autophagy
  JOURNAL   Mol Biol Cell 20 (7), 1981-1991 (2009)
   PUBMED   19211835
  REMARK    GeneRIF: mTORC1 suppresses autophagy through direct regulation of
            the approximately 3-MDa ULK1-Atg13-FIP200 complex.
REFERENCE   8  (residues 1 to 480)
  AUTHORS   Chan,E.Y., Longatti,A., McKnight,N.C. and Tooze,S.A.
  TITLE     Kinase-inactivated ULK proteins inhibit autophagy via their
            conserved C-terminal domains using an Atg13-independent mechanism
  JOURNAL   Mol Cell Biol 29 (1), 157-171 (2009)
   PUBMED   18936157
  REMARK    GeneRIF: The functions of ULK1 and ULK2 are controlled by
            autophosphorylation and conformational changes involving exposure
            of the C-terminal domain and interaction with the putative human
            homologue of Atg13.
            GeneRIF: The gene product is the functional homologue of yeast
            Atg13, and required for autophagy in mammalian cells.
REFERENCE   9  (residues 1 to 480)
  AUTHORS   Meijer,W.H., van der Klei,I.J., Veenhuis,M. and Kiel,J.A.
  TITLE     ATG genes involved in non-selective autophagy are conserved from
            yeast to man, but the selective Cvt and pexophagy pathways also
            require organism-specific genes
  JOURNAL   Autophagy 3 (2), 106-116 (2007)
   PUBMED   17204848
REFERENCE   10 (residues 1 to 480)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC127035.6 and AC115088.6.
            
            On Oct 9, 2016 this sequence version replaced XP_016874103.1.
            
            Summary: The protein encoded by this gene is an autophagy factor
            and a target of the TOR kinase signaling pathway. The encoded
            protein is essential for autophagosome formation and mitophagy.
            [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (38), as well as variants 2, 5,
            36-37, and 39-45, encodes isoform f.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.366829.1,
                                           SRR11853565.4866.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..480
                     /product="autophagy-related protein 13 isoform f"
                     /note="autophagy-related protein 13; ATG13 autophagy
                     related 13 homolog"
                     /calculated_mol_wt=52692
     Region          19..192
                     /region_name="ATG13"
                     /note="Autophagy-related protein 13; pfam10033"
                     /db_xref="CDD:431003"
     CDS             1..480
                     /gene="ATG13"
                     /gene_synonym="KIAA0652; PARATARG8"
                     /coded_by="NM_001346346.2:459..1901"
                     /note="isoform f is encoded by transcript variant 38"
                     /db_xref="CCDS:CCDS7921.1"
                     /db_xref="GeneID:9776"
                     /db_xref="HGNC:HGNC:29091"
                     /db_xref="MIM:615088"
ORIGIN      
        1 metdlnsqdr kdldkfikff alktvqvivq arlgekictr ssssptgsdw fnlaikdipe
       61 vtheakkala gqlpavgrsm cveislktse gdsmeleiwc lemnekcdke ikvsytvynr
      121 lslllkslla itrvtpayrl srkqgheyvi lyriyfgevq lsglgegfqt vrvgtvgtpv
      181 gtitlscayr inlafmstrq fertppimgi iidhfvdrpy pssspmhpcn yrtagedtgv
      241 iypsvedsqe vcttsfstsp psqlmvpgke ggvplapnqp vhgtqadqer latctpsdrt
      301 hcaatpssse dtetvsnsse grasphdvle tifvrkvgaf vnkpinqvtl tsldipfamf
      361 apknleledt dpmvnppdsp etesplqgsl hsdgssggss gnthddfvmi dfkpafskdd
      421 ilpmdlgtfy refqnppqls slsidigaqs maedldslpe klavheknvr efdafvetlq
//
LOCUS       NP_001386901             301 aa            linear   PRI 21-NOV-2025
DEFINITION  lipoamide acyltransferase component of branched-chain alpha-keto
            acid dehydrogenase complex, mitochondrial isoform 2 [Homo sapiens].
ACCESSION   NP_001386901
VERSION     NP_001386901.1
DBSOURCE    REFSEQ: accession NM_001399972.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Hwang,R.D., Lu,Y., Tang,Q., Periz,G., Park,G., Li,X., Xiang,Q.,
            Liu,Y., Zhang,T. and Wang,J.
  TITLE     DBT is a metabolic switch for maintenance of proteostasis under
            proteasomal impairment
  JOURNAL   Elife 12, 91002 (2024)
   PUBMED   39255192
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Zhang,C., Huang,G., Yang,J., Jiang,Y., Huang,R., Ye,Z., Huang,Y.,
            Hu,H. and Xi,X.
  TITLE     Overexpression of DBT suppresses the aggressiveness of renal clear
            cell carcinoma and correlates with immune infiltration
  JOURNAL   Front Immunol 14, 1197011 (2023)
   PUBMED   37383233
  REMARK    GeneRIF: Overexpression of DBT suppresses the aggressiveness of
            renal clear cell carcinoma and correlates with immune infiltration.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Alijanpour,M., Jazayeri,O., Soleimani Amiri,S. and Brosens,E.
  TITLE     Pathogenic Homozygous Mutations in the DBT Gene (c.1174A>C) Result
            in Maple Syrup Urine Disease in a rs12021720 Carrier
  JOURNAL   Lab Med 53 (6), 596-601 (2022)
   PUBMED   35657820
  REMARK    GeneRIF: Pathogenic Homozygous Mutations in the DBT Gene
            (c.1174A>C) Result in Maple Syrup Urine Disease in a rs12021720
            Carrier.
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Tsuruta,M., Mitsubuchi,H., Mardy,S., Miura,Y., Hayashida,Y.,
            Kinugasa,A., Ishitsu,T., Matsuda,I. and Indo,Y.
  TITLE     Molecular basis of intermittent maple syrup urine disease: novel
            mutations in the E2 gene of the branched-chain alpha-keto acid
            dehydrogenase complex
  JOURNAL   J Hum Genet 43 (2), 91-100 (1998)
   PUBMED   9621512
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Strauss,K.A., Puffenberger,E.G. and Carson,V.J.
  TITLE     Maple Syrup Urine Disease
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301495
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Lau,K.S., Herring,W.J., Chuang,J.L., McKean,M., Danner,D.J.,
            Cox,R.P. and Chuang,D.T.
  TITLE     Structure of the gene encoding dihydrolipoyl transacylase (E2)
            component of human branched chain alpha-keto acid dehydrogenase
            complex and characterization of an E2 pseudogene
  JOURNAL   J Biol Chem 267 (33), 24090-24096 (1992)
   PUBMED   1429740
REFERENCE   8  (residues 1 to 301)
  AUTHORS   Lau,K.S., Chuang,J.L., Herring,W.J., Danner,D.J., Cox,R.P. and
            Chuang,D.T.
  TITLE     The complete cDNA sequence for dihydrolipoyl transacylase (E2) of
            human branched-chain alpha-keto acid dehydrogenase complex
  JOURNAL   Biochim Biophys Acta 1132 (3), 319-321 (1992)
   PUBMED   1420314
REFERENCE   9  (residues 1 to 301)
  AUTHORS   Zneimer,S.M., Lau,K.S., Eddy,R.L., Shows,T.B., Chuang,J.L.,
            Chuang,D.T. and Cox,R.P.
  TITLE     Regional assignment of two genes of the human branched-chain
            alpha-keto acid dehydrogenase complex: the E1 beta gene (BCKDHB) to
            chromosome 6p21-22 and the E2 gene (DBT) to chromosome 1p31
  JOURNAL   Genomics 10 (3), 740-747 (1991)
   PUBMED   1889817
REFERENCE   10 (residues 1 to 301)
  AUTHORS   Fisher,C.W., Lau,K.S., Fisher,C.R., Wynn,R.M., Cox,R.P. and
            Chuang,D.T.
  TITLE     A 17-bp insertion and a Phe215----Cys missense mutation in the
            dihydrolipoyl transacylase (E2) mRNA from a thiamine-responsive
            maple syrup urine disease patient WG-34
  JOURNAL   Biochem Biophys Res Commun 174 (2), 804-809 (1991)
   PUBMED   1847055
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445928.8.
            
            Summary: The branched-chain alpha-keto acid dehydrogenase complex
            (BCKD) is an inner-mitochondrial enzyme complex involved in the
            breakdown of the branched-chain amino acids isoleucine, leucine,
            and valine. The BCKD complex is thought to be composed of a core of
            24 transacylase (E2) subunits, and associated decarboxylase (E1),
            dehydrogenase (E3), and regulatory subunits. This gene encodes the
            transacylase (E2) subunit. Mutations in this gene result in maple
            syrup urine disease, type 2. Alternatively spliced transcript
            variants have been described, but their biological validity has not
            been determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR7346977.1880361.1 [ECO:0000331]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p21.2"
     Protein         1..301
                     /product="lipoamide acyltransferase component of
                     branched-chain alpha-keto acid dehydrogenase complex,
                     mitochondrial isoform 2"
                     /EC_number="2.3.1.168"
                     /note="branched chain acyltransferase, E2 component;
                     dihydrolipoyl transacylase; dihydrolipoyllysine-residue
                     (2-methylpropanoyl)transferase; lipoamide acyltransferase
                     component of mitochondrial branched-chain alpha-keto acid
                     dehydrogenase complex; BCKAD E2 subunit; mitochondrial
                     branched chain alpha-keto acid dehydrogenase transacylase
                     subunit (E2b); E2 component of branched chain alpha-keto
                     acid dehydrogenase complex; branched chain 2-oxo-acid
                     dehydrogenase complex component E2; 52 kDa mitochondrial
                     autoantigen of primary biliary cirrhosis; lipoamide
                     acyltransferase component of branched-chain alpha-keto
                     acid dehydrogenase complex, mitochondrial; branched-chain
                     alpha-keto acid dehydrogenase complex component E2;
                     dihydrolipoamide acetyltransferase component of
                     branched-chain alpha-keto acid dehydrogenase complex"
                     /calculated_mol_wt=32846
     Region          <2..301
                     /region_name="PLN02528"
                     /note="2-oxoisovalerate dehydrogenase E2 component"
                     /db_xref="CDD:215289"
     CDS             1..301
                     /gene="DBT"
                     /gene_synonym="BCATE2; BCKAD-E2; BCKADE2; BCKDH-E2;
                     BCOADC-E2; E2; E2B"
                     /coded_by="NM_001399972.1:618..1523"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS91012.1"
                     /db_xref="GeneID:1629"
                     /db_xref="HGNC:HGNC:2698"
                     /db_xref="MIM:248610"
ORIGIN      
        1 menniklsev vgsgkdgril kedilnylek qtgailppsp kveimppppk pkdmtvpilv
       61 skppvftgkd ktepikgfqk amvktmsaal kiphfgycde idltelvklr eelkpiafar
      121 giklsfmpff lkaaslgllq fpilnasvde ncqnitykas hnigiamdte qglivpnvkn
      181 vqicsifdia telnrlqklg svsqlsttdl tggtftlsni gsiggtfakp vimppevaig
      241 algsikaipr fnqkgevyka qimnvswsad hrvidgatms rfsnlwksyl enpafmlldl
      301 k
//
LOCUS       NP_001006617             263 aa            linear   PRI 21-NOV-2025
DEFINITION  tetraspanin-17 isoform c [Homo sapiens].
ACCESSION   NP_001006617
VERSION     NP_001006617.2
DBSOURCE    REFSEQ: accession NM_001006616.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Guo,X.B., Zhang,X.C., Chen,P., Ma,L.M. and Shen,Z.Q.
  TITLE     miR-378a-3p inhibits cellular proliferation and migration in
            glioblastoma multiforme by targeting tetraspanin 17
  JOURNAL   Oncol Rep 42 (5), 1957-1971 (2019)
   PUBMED   31432186
  REMARK    GeneRIF: Data suggested that increased miR378a3p and decreased
            TSPAN17 levels were associated with improved survival in
            glioblastoma multiforme (GBM). Additionally, high levels of TSPAN17
            were linked to the poor prognosis of patients with GBM aged 5060,
            larger tumor sizes and an advanced World Health Organization stage.
            TSPAN17 was identified and confirmed as a direct target of miR378a.
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Reyat,J.S., Chimen,M., Noy,P.J., Szyroka,J., Rainger,G.E. and
            Tomlinson,M.G.
  TITLE     ADAM10-Interacting Tetraspanins Tspan5 and Tspan17 Regulate
            VE-Cadherin Expression and Promote T Lymphocyte Transmigration
  JOURNAL   J Immunol 199 (2), 666-676 (2017)
   PUBMED   28600292
  REMARK    GeneRIF: Endothelial Tspan5- and Tspan17-ADAM10 complexes may
            regulate inflammation by maintaining normal VE-cadherin expression
            and promoting T lymphocyte transmigration.
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Dornier,E., Coumailleau,F., Ottavi,J.F., Moretti,J., Boucheix,C.,
            Mauduit,P., Schweisguth,F. and Rubinstein,E.
  TITLE     TspanC8 tetraspanins regulate ADAM10/Kuzbanian trafficking and
            promote Notch activation in flies and mammals
  JOURNAL   J Cell Biol 199 (3), 481-496 (2012)
   PUBMED   23091066
  REMARK    Erratum:[J Cell Biol. 2016 May 23;213(4):495-6. doi:
            10.1083/jcb.20120113304262016c. PMID: 27185832]
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091934.2.
            
            On Jun 10, 2010 this sequence version replaced NP_001006617.1.
            
            Summary: This gene encodes a member of the transmembrane 4
            superfamily. It is characterized by four tetraspanin transmembrane
            segments. The function of this gene has not yet been determined.
            [provided by RefSeq, Mar 2014].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice site in the central coding region, and an alternate splice
            site that causes a frameshift in the 3' coding region, compared to
            variant 1. The resulting isoform (c) has a distinct C-terminus and
            is shorter than isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138512.109574.1,
                                           SRR1803614.261303.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.2"
     Protein         1..263
                     /product="tetraspanin-17 isoform c"
                     /EC_number="3.6.5.3"
                     /note="F-box only protein 23, transmembrane 4 superfamily
                     member 17; tetraspan protein SB134"
                     /calculated_mol_wt=29438
     Region          18..259
                     /region_name="Tetraspanin"
                     /note="Tetraspanin family; pfam00335"
                     /db_xref="CDD:459767"
     Site            20..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FV3.2)"
     Site            51
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96FV3.2)"
     Site            64..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FV3.2)"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FV3.2)"
     Region          115..235
                     /region_name="TM4SF9_like_LEL"
                     /note="Tetraspanin, extracellular domain or large
                     extracellular loop (LEL), TM4SF9_like subfamily.
                     Tetraspanins are trans-membrane proteins with 4
                     trans-membrane segments. Both the N- and C-termini lie on
                     the intracellular side of the membrane. This alignment...;
                     cd03159"
                     /db_xref="CDD:239412"
     Site            order(116,121,125,127..128,131,145,148..149,152..153)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239412"
     Site            171
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96FV3.2)"
     Site            235..255
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FV3.2)"
     CDS             1..263
                     /gene="TSPAN17"
                     /gene_synonym="FBX23; FBXO23; TM4SF17"
                     /coded_by="NM_001006616.3:133..924"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS47346.2"
                     /db_xref="GeneID:26262"
                     /db_xref="HGNC:HGNC:13594"
                     /db_xref="MIM:620446"
ORIGIN      
        1 mpgkhqhfqe pevgccgkyf lfgfnivfwv lgalflaigl wawgekgvls nisaltdlgg
       61 ldpvwlfvvv ggvmsvlgfa gcigalrent fllkffsvfl glifflelat gilafvfkdw
      121 irdqlnlfin nnvkayrddi dlqnlidfaq eywsccgarg pndwnlniyf nctdlnpsre
      181 rcgvpfsccv rdpaedvlnt qcgydvrlkl eleqqgfiht kgcvgqfekw lqdnlivvag
      241 vfmgiallqi fgiclaqnle qme
//
LOCUS       NP_005656                810 aa            linear   PRI 21-NOV-2025
DEFINITION  ecotropic viral integration site 5 protein homolog isoform 2 [Homo
            sapiens].
ACCESSION   NP_005656 XP_496372 XP_498930
VERSION     NP_005656.4
DBSOURCE    REFSEQ: accession NM_005665.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Cai,T., Zhou,J., Zeng,Y., Du,W., Zhang,Y., Liu,T., Fu,Y.,
            Huang,J.A., Qian,Q., Zhu,J., Ling,C. and Liu,Z.
  TITLE     EVI5 is an oncogene that regulates the proliferation and metastasis
            of NSCLC cells
  JOURNAL   J Exp Clin Cancer Res 39 (1), 84 (2020)
   PUBMED   32393392
  REMARK    GeneRIF: EVI5 is an oncogene that regulates the proliferation and
            metastasis of NSCLC cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 810)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   7  (residues 1 to 810)
  AUTHORS   Eldridge,A.G., Loktev,A.V., Hansen,D.V., Verschuren,E.W.,
            Reimann,J.D. and Jackson,P.K.
  TITLE     The evi5 oncogene regulates cyclin accumulation by stabilizing the
            anaphase-promoting complex inhibitor emi1
  JOURNAL   Cell 124 (2), 367-380 (2006)
   PUBMED   16439210
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Faitar,S.L., Dabbeekeh,J.T., Ranalli,T.A. and Cowell,J.K.
  TITLE     EVI5 is a novel centrosomal protein that binds to alpha- and
            gamma-tubulin
  JOURNAL   Genomics 86 (5), 594-605 (2005)
   PUBMED   16033705
  REMARK    GeneRIF: a novel centrosomal protein with a complex expression
            pattern and subcellular localization, possibly involved in
            centrosome stability and dynamics
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Roberts,T., Chernova,O. and Cowell,J.K.
  TITLE     NB4S, a member of the TBC1 domain family of genes, is truncated as
            a result of a constitutional t(1;10)(p22;q21) chromosome
            translocation in a patient with stage 4S neuroblastoma
  JOURNAL   Hum Mol Genet 7 (7), 1169-1178 (1998)
   PUBMED   9618176
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL133332.12, AF008915.1, CN334472.1, AC104332.2, AB209513.1,
            AC104456.2 and AA725529.1.
            
            On Jun 29, 2005 this sequence version replaced NP_005656.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.1"
     Protein         1..810
                     /product="ecotropic viral integration site 5 protein
                     homolog isoform 2"
                     /note="ecotropic viral integration site 5 protein homolog;
                     dJ846D11.1 (ecotropic viral integration site 5);
                     neuroblastoma stage 4S gene protein"
                     /calculated_mol_wt=92818
     Region          1..483
                     /region_name="Interaction with alpha-tubulin,
                     gamma-tubulin, BIRC5 and FBXO5.
                     /evidence=ECO:0000269|PubMed:16439210,
                     ECO:0000269|PubMed:16764853"
                     /note="propagated from UniProtKB/Swiss-Prot (O60447.3)"
     Region          49..80
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60447.3)"
     Region          98..123
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60447.3)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60447.3)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97366; propagated from
                     UniProtKB/Swiss-Prot (O60447.3)"
     Region          128..693
                     /region_name="Dimerization"
                     /note="propagated from UniProtKB/Swiss-Prot (O60447.3)"
     Region          160..368
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Region          377..810
                     /region_name="Targeting to the centrosomes"
                     /note="propagated from UniProtKB/Swiss-Prot (O60447.3)"
     Region          453..>493
                     /region_name="DUF1129"
                     /note="Protein of unknown function (DUF1129); cl11555"
                     /db_xref="CDD:472220"
     Region          487..810
                     /region_name="Interaction with AURKB and INCENP.
                     /evidence=ECO:0000269|PubMed:16764853"
                     /note="propagated from UniProtKB/Swiss-Prot (O60447.3)"
     Region          <492..>707
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60447.3)"
     Site            594
                     /site_type="other"
                     /note="Breakpoint for translocation to form EVI5-TRNG10
                     fusion protein; propagated from UniProtKB/Swiss-Prot
                     (O60447.3)"
     Site            689
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60447.3)"
     Region          756..810
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60447.3)"
     Site            776
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O60447.3)"
     Site            778
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97366; propagated from
                     UniProtKB/Swiss-Prot (O60447.3)"
     CDS             1..810
                     /gene="EVI5"
                     /gene_synonym="EVI-5; NB4S"
                     /coded_by="NM_005665.6:17..2449"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS30774.1"
                     /db_xref="GeneID:7813"
                     /db_xref="HGNC:HGNC:3501"
                     /db_xref="MIM:602942"
ORIGIN      
        1 mvtnkmtaaf rnpsgkqvat dkvaeklsst lswvkntvsh tvsqmasqva spstslhtts
       61 ssttlstpal spsspsqlsp ddlellakle eqnrlletds kslrsvngsr rnsgsslvss
      121 ssassnlshl eedswilwgr ivnewedvrk kkekqvkelv hkgiphhfra ivwqllcsaq
      181 smpikdqyse llkmtspcek lirrdiarty pehnffkekd slgqevlfnv mkayslvdre
      241 vgycqgsafi vglllmqmpe eeafcvfvkl mqdyrlrelf kpsmaelglc myqfecmiqe
      301 hlpelfvhfq sqsfhtsmya sswfltiflt tfplpiatri fdifmsegle ivfrvglall
      361 qmnqaelmql dmegmlqhfq kviphqfdgv pdkliqaayq vkynskkmkk lekeyttikt
      421 kemeeqveik rlrtenrllk qrietlekhk cssnynedfv lqlekelvqa rlseaesqca
      481 lkemqdkvld iekrnnslpd enniarlqee liavklreae aimglkelrq qvkdleehwq
      541 rhlarttgrw kdppkknamn elqdelmtir lreaetqaei reikqrmmem etqnqinsnh
      601 lrraeqevis lqekvqylsa qnkglltqls eakrkqaeie cknkeevmav rlreadsiaa
      661 vaelrqhiae leiqkeegkl qgqlnksdsn qyigelkdqi aelnhelrcl kgqrgfsgqp
      721 pfdgihivnh ligddesfhs sdedfidnsl qetgvgfplh gksgsmsldp avadgseset
      781 edsvletres nqvvqkerpp rrresysttv
//
LOCUS       NP_001382624            1715 aa            linear   PRI 21-NOV-2025
DEFINITION  endoribonuclease Dicer isoform 7 [Homo sapiens].
ACCESSION   NP_001382624
VERSION     NP_001382624.1
DBSOURCE    REFSEQ: accession NM_001395695.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1715)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1715)
  AUTHORS   Rojo-Pardillo,M., Godefroid,L., Dom,G., Lefort,A., Libert,F.,
            Robaye,B. and Maenhaut,C.
  TITLE     Understanding the Dosage-Dependent Role of Dicer1 in Thyroid
            Tumorigenesis
  JOURNAL   Int J Mol Sci 25 (19), 10701 (2024)
   PUBMED   39409030
  REMARK    GeneRIF: Understanding the Dosage-Dependent Role of Dicer1 in
            Thyroid Tumorigenesis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1715)
  AUTHORS   Mastnikova,K., Bulanova Pekova,B., Kuklikova,V., Vaclavikova,E.,
            Carkova,J., Katra,R., Fialova,L., Vlcek,P., Kodetova,D.,
            Chovanec,M., Drozenova,J., Matej,R., Pacesova,P., Novak,Z.,
            Procykova,K., Vcelak,J. and Bendlova,B.
  TITLE     DICER1 Variants in Pediatric and Young Adult Thyroid Nodules
  JOURNAL   Thyroid 34 (10), 1225-1233 (2024)
   PUBMED   39283830
  REMARK    GeneRIF: DICER1 Variants in Pediatric and Young Adult Thyroid
            Nodules.
REFERENCE   4  (residues 1 to 1715)
  AUTHORS   Dashti,N.K., Swanson,A.A., Bentz,J., Xing,D., Chrisinger,J.S.A.,
            Balzer,B., Guo,R., Schoolmeester,J.K. and Maluf,H.
  TITLE     DICER1-sarcomas of GYN tract: Expanding on an emerging entity
  JOURNAL   Hum Pathol 152, 105636 (2024)
   PUBMED   39127354
  REMARK    GeneRIF: DICER1-sarcomas of GYN tract: Expanding on an emerging
            entity.
REFERENCE   5  (residues 1 to 1715)
  AUTHORS   Irvin-Wilson,C.V. and Chaudhuri,G.
  TITLE     Alternative initiation and splicing in dicer gene expression in
            human breast cells
  JOURNAL   Breast Cancer Res 7 (4), R563-R569 (2005)
   PUBMED   15987463
REFERENCE   6  (residues 1 to 1715)
  AUTHORS   Bignell,G.R., Canzian,F., Shayeghi,M., Stark,M., Shugart,Y.Y.,
            Biggs,P., Mangion,J., Hamoudi,R., Rosenblatt,J., Buu,P., Sun,S.,
            Stoffer,S.S., Goldgar,D.E., Romeo,G., Houlston,R.S., Narod,S.A.,
            Stratton,M.R. and Foulkes,W.D.
  TITLE     Familial nontoxic multinodular thyroid goiter locus maps to
            chromosome 14q but does not account for familial nonmedullary
            thyroid cancer
  JOURNAL   Am J Hum Genet 61 (5), 1123-1130 (1997)
   PUBMED   9345104
REFERENCE   7  (residues 1 to 1715)
  AUTHORS   Schultz,K.A.P., Stewart,D.R., Kamihara,J., Bauer,A.J.,
            Merideth,M.A., Stratton,P., Huryn,L.A., Harris,A.K., Doros,L.,
            Field,A., Carr,A.G., Dehner,L.P., Messinger,Y. and Hill,D.A.
  TITLE     DICER1 Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24761742
REFERENCE   8  (residues 1 to 1715)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   9  (residues 1 to 1715)
  AUTHORS   Couch,R.M., Hughes,I.A., DeSa,D.J., Schiffrin,A., Guyda,H. and
            Winter,J.S.
  TITLE     An autosomal dominant form of adolescent multinodular goiter
  JOURNAL   Am J Hum Genet 39 (6), 811-816 (1986)
   PUBMED   3799599
REFERENCE   10 (residues 1 to 1715)
  AUTHORS   Murray,I.P., Thomson,J.A., McGirr,E.M., Macdonald,E.M.,
            Kennedy,J.S. and McLennan,I.
  TITLE     Unusual familial goiter associated with intrathyroidal
            calcification
  JOURNAL   J Clin Endocrinol Metab 26 (10), 1039-1049 (1966)
   PUBMED   4162574
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL356017.3 and AL390254.6.
            
            Summary: This gene encodes a protein possessing an RNA helicase
            motif containing a DEXH box in its amino terminus and an RNA motif
            in the carboxy terminus. The encoded protein functions as a
            ribonuclease and is required by the RNA interference and small
            temporal RNA (stRNA) pathways to produce the active small RNA
            component that represses gene expression. This protein also acts as
            a strong antiviral agent with activity against RNA viruses,
            including the Zika and SARS-CoV-2 viruses. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jul
            2021].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1715
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.13"
     Protein         1..1715
                     /product="endoribonuclease Dicer isoform 7"
                     /EC_number="3.1.26.3"
                     /note="dicer 1, double-stranded RNA-specific
                     endoribonuclease; helicase with RNAse motif;
                     endoribonuclease Dicer; helicase MOI; Dicer1, Dcr-1
                     homolog; dicer 1, ribonuclease type III"
                     /calculated_mol_wt=194958
     Region          42..239
                     /region_name="DEXHc_dicer"
                     /note="DEXH-box helicase domain of endoribonuclease Dicer;
                     cd18034"
                     /db_xref="CDD:350792"
     Site            order(42..45,48,65..72,113,176,207)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350792"
     Site            order(101..102,125..126,151,153..154,157,182..184)
                     /site_type="other"
                     /note="nucleic acid binding site [nucleotide binding]"
                     /db_xref="CDD:350792"
     Region          175..178
                     /region_name="DECH box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Region          256..595
                     /region_name="Required for interaction with PRKRA and
                     TARBP2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Region          271..365
                     /region_name="Dicer_PBD"
                     /note="Partner-binding domain of the endoribonuclease
                     Dicer; cd15903"
                     /db_xref="CDD:277191"
     Site            order(276..277,280,282..283,342..343,346..347,350,
                     353..354,357)
                     /site_type="other"
                     /note="Trbp binding interface [polypeptide binding]"
                     /db_xref="CDD:277191"
     Region          372..564
                     /region_name="SF2_C_dicer"
                     /note="C-terminal helicase domain of the endoribonuclease
                     Dicer; cd18802"
                     /db_xref="CDD:350189"
     Region          409..433
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            order(449..451,521,540,542)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350189"
     Site            order(525,527,552,554)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350189"
     Region          630..718
                     /region_name="Dicer_dimer"
                     /note="Dicer dimerization domain; pfam03368"
                     /db_xref="CDD:460900"
     Region          886..1008
                     /region_name="PAZ_dicer_like"
                     /note="PAZ domain, dicer_like subfamily. Dicer is an RNAse
                     involved in cleaving dsRNA in the RNA interference
                     pathway. It generates dsRNAs which are approximately 20 bp
                     long (siRNAs), which in turn target hydrolysis of
                     homologous RNAs. PAZ domains are named...; cd02843"
                     /db_xref="CDD:239209"
     Site            order(949,962,968,972,990,998,1000)
                     /site_type="other"
                     /note="nucleic acid-binding interface [nucleotide
                     binding]"
                     /db_xref="CDD:239209"
     Site            1016
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            1160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Region          1296..>1387
                     /region_name="RIBOc"
                     /note="Ribonuclease III family; smart00535"
                     /db_xref="CDD:197778"
     Site            order(1313..1314,1317..1318,1321,1324..1325,1328..1329,
                     1331..1333,1343)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238333"
     Site            1460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            1468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R418; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            1470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Region          1669..>1708
                     /region_name="RIBOc"
                     /note="Ribonuclease III C terminal domain. This group
                     consists of eukaryotic, bacterial and archeal ribonuclease
                     III (RNAse III) proteins. RNAse III is a double stranded
                     RNA-specific endonuclease. Prokaryotic RNAse III is
                     important in post-transcriptional...; cl00258"
                     /db_xref="CDD:469693"
     CDS             1..1715
                     /gene="DICER1"
                     /gene_synonym="aviD; DCR1; Dicer; Dicer1e; GLOW; HERNA;
                     K12H4.8-LIKE; MNG1; RMSE2"
                     /coded_by="NM_001395695.1:447..5594"
                     /note="isoform 7 is encoded by transcript variant 24"
                     /db_xref="CCDS:CCDS91926.1"
                     /db_xref="GeneID:23405"
                     /db_xref="HGNC:HGNC:17098"
                     /db_xref="MIM:606241"
ORIGIN      
        1 mkspalqpls maglqlmtpa sspmgpffgl pwqqeaihdn iytprkyqve lleaaldhnt
       61 ivclntgsgk tfiavlltke lsyqirgdfs rngkrtvflv nsanqvaqqv savrthsdlk
      121 vgeysnlevn aswtkerwnq eftkhqvlim tcyvalnvlk ngylslsdin llvfdechla
      181 ildhpyreim klcencpscp rilgltasil ngkcdpeele ekiqklekil ksnaetatdl
      241 vvldrytsqp ceivvdcgpf tdrsglyerl lmeleealnf indcnisvhs kerdstlisk
      301 qilsdcravl vvlgpwcadk vagmmvrelq kyikheqeel hrkfllftdt flrkihalce
      361 ehfspasldl kfvtpkvikl leilrkykpy erqqfesvew ynnrnqdnyv swsdseddde
      421 deeieekekp etnfpspftn ilcgiifver rytavvlnrl ikeagkqdpe layissnfit
      481 ghgigknqpr nkqmeaefrk qeevlrkfra hetnlliats iveegvdipk cnlvvrfdlp
      541 teyrsyvqsk grarapisny imladtdkik sfeedlktyk aiekilrnkc sksvdtgetd
      601 idpvmddddv fppyvlrpdd ggprvtinta ighinrycar lpsdpfthla pkcrtrelpd
      661 gtfystlylp insplrasiv gppmscvrla ervvalicce klhkigeldd hlmpvgketv
      721 kyeeeldlhd eeetsvpgrp gstkrrqcyp kaipeclrds yprpdqpcyl yvigmvlttp
      781 lpdelnfrrr klyppedttr cfgiltakpi pqiphfpvyt rsgevtisie lkksgfmlsl
      841 qmlelitrlh qyifshilrl ekpalefkpt dadsaycvlp lnvvndsstl didfkfmedi
      901 eksearigip stkytketpf vfkledyqda viipryrnfd qphrfyvadv ytdltplskf
      961 pspeyetfae yyktkynldl tnlnqplldv dhtssrlnll tprhlnqkgk alplssaekr
     1021 kakweslqnk qilvpelcai hpipaslwrk avclpsilyr lhclltaeel raqtasdagv
     1081 gvrslpadfr ypnldfgwkk sidsksfisi snsssaendn yckhstivpe naahqganrt
     1141 sslenhdqms vncrtllses pgklhvevsa dltainglsy nqnlangsyd lanrdfcqgn
     1201 qlnyykqeip vqpttsysiq nlysyenqpq psdectllsn kyldgnanks tsdgspvmav
     1261 mpgttdtiqv lkgrmdseqs psigyssrtl gpnpglilqa ltlsnasdgf nlerlemlgd
     1321 sflkhaitty lfctypdahe grlsymrskk vsncnlyrlg kkkglpsrmv vsifdppvnw
     1381 lppgyvvnqd ksntdkwekd emtkdcmlan gkldedyeee deeeeslmwr apkeeadyed
     1441 dfleydqehi rfidnmlmgs gafvkkisls pfsttdsaye wkmpkksslg smpfssdfed
     1501 fdysswdamc yldpskavee ddfvvgfwnp seencgvdtg kqsisydlht eqciadksia
     1561 dcveallgcy ltscgeraaq lflcslglkv lpvikrtdre kalcptrenf nsqqknlsvs
     1621 caaasvassr ssvlkdseyg clkipprcmf dhpdadktln hlisgfenfe kkinyrfknk
     1681 ayllqaftha syhyntitgk epttrlhfwe netlc
//
LOCUS       NP_001256970             177 aa            linear   PRI 21-NOV-2025
DEFINITION  DPY30 domain-containing protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001256970
VERSION     NP_001256970.1
DBSOURCE    REFSEQ: accession NM_001270041.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Kuhl,A., Melberg,A., Meinl,E., Nurnberg,G., Nurnberg,P.,
            Kehrer-Sawatzki,H. and Jenne,D.E.
  TITLE     Myofibrillar myopathy with arrhythmogenic right ventricular
            cardiomyopathy 7: corroboration and narrowing of the critical
            region on 10q22.3
  JOURNAL   Eur J Hum Genet 16 (3), 367-373 (2008)
   PUBMED   18197198
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA590784.1 and BC018606.2.
            
            Summary: This gene encodes a member of a family of proteins that
            contains a DPY30 domain. This gene locus overlaps with a closely
            related gene on the opposite strand. Alternative splicing results
            in multiple transcript variants. [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (2) lacks an exon in the 5' UTR,
            compared to variant 1. Variants 1 and 2 encode the same protein
            (isoform 1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.464959.1,
                                           ERR4352443.359624.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.1"
     Protein         1..177
                     /product="DPY30 domain-containing protein 2 isoform 1"
                     /note="DPY30 domain-containing protein 2"
                     /calculated_mol_wt=20455
     Region          2..45
                     /region_name="DD_DYDC-like"
                     /note="dimerization/docking (D/D) domain found in the
                     DPY30 domain-containing protein (DYDC)-like family;
                     cd22966"
                     /db_xref="CDD:438535"
     CDS             1..177
                     /gene="DYDC2"
                     /coded_by="NM_001270041.2:55..588"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS7367.1"
                     /db_xref="GeneID:84332"
                     /db_xref="HGNC:HGNC:23468"
ORIGIN      
        1 metnylkrcf gnclaqalae vakvrpsdpi eylahwlyhy rktakakeen rekkihlqee
       61 ydsslkemem temlkqeeyq iqqncekchk eltsetvstk ktifmqedtn plekealkqe
      121 flpgtsslip gmpqqvppse sagqidqnfk mpqeinykea fqhevahemp pgskspf
//
LOCUS       NP_001387093            1220 aa            linear   PRI 21-NOV-2025
DEFINITION  protein transport protein Sec31A isoform 1 [Homo sapiens].
ACCESSION   NP_001387093
VERSION     NP_001387093.1
DBSOURCE    REFSEQ: accession NM_001400164.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1220)
  AUTHORS   Tobias,E.S., Lucas-Herald,A.K., Sagar,D., Montezano,A.C.,
            Rios,F.J., De Lucca Camargo,L., Hamilton,G., Gazdagh,G.,
            Diver,L.A., Williams,N., Herzyk,P., Touyz,R.M., Greenfield,A.,
            McGowan,R. and Ahmed,S.F.
  TITLE     SEC31A may be associated with pituitary hormone deficiency and
            gonadal dysgenesis
  JOURNAL   Endocrine 84 (2), 345-349 (2024)
   PUBMED   38400880
  REMARK    GeneRIF: SEC31A may be associated with pituitary hormone deficiency
            and gonadal dysgenesis.
REFERENCE   2  (residues 1 to 1220)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1220)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1220)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1220)
  AUTHORS   Jin,L., Pahuja,K.B., Wickliffe,K.E., Gorur,A., Baumgartel,C.,
            Schekman,R. and Rape,M.
  TITLE     Ubiquitin-dependent regulation of COPII coat size and function
  JOURNAL   Nature 482 (7386), 495-500 (2012)
   PUBMED   22358839
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1220)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1220)
  AUTHORS   Kim,J.H., Hong,J.A., Pih,K.T. and Hwang,I.
  TITLE     Identification and isolation of differentially expressed genes in
            osmotically stressed human oral keratinocytes
  JOURNAL   Arch Oral Biol 46 (4), 335-341 (2001)
   PUBMED   11269867
REFERENCE   8  (residues 1 to 1220)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 1220)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   10 (residues 1 to 1220)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021105.13 and AC108469.5.
            
            Summary: The protein encoded by this gene shares similarity with
            the yeast Sec31 protein, and is a component of the outer layer of
            the coat protein complex II (COPII). The encoded protein is
            involved in vesicle budding from the endoplasmic reticulum (ER) and
            contains multiple WD repeats near the N-terminus and a proline-rich
            region in the C-terminal half. It associates with the protein
            encoded by the SEC13 homolog, nuclear pore and COPII coat complex
            component (SEC13), and is required for ER-Golgi transport.
            Monoubiquitylation of this protein by CUL3-KLHL12 was found to
            regulate the size of COPII coats to accommodate unusually shaped
            cargo. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.80908.1,
                                           SRR14038192.1986283.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1220
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..1220
                     /product="protein transport protein Sec31A isoform 1"
                     /note="yeast Sec31p homolog; protein transport protein
                     Sec31A; web1-like protein; SEC31 homolog A, COPII coat
                     complex component; SEC31-related protein A; SEC31-like
                     protein 1; SEC31 homolog A, COPII coating complex
                     component"
                     /calculated_mol_wt=132884
     Region          4..47
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          13..332
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(26,40,46..47,52..53,91,95,101..102,117,121,139,144,
                     150..151,164,185,190,196..197,209..210,231,235,244..245,
                     258..259,277,282,288..289,301..302,320,325,331..332)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          68..111
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          70..119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          120..160
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          125..162
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          161..471
                     /region_name="Interaction with SEC13.
                     /evidence=ECO:0000269|PubMed:16957052"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          172..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          263..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          306..331
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94979.3)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (O94979.3)"
     Region          <573..>696
                     /region_name="ACE1-Sec16-like"
                     /note="Ancestral coatomer element 1 (ACE1) of COPII coat
                     complex assembly protein Sec16; cl14807"
                     /db_xref="CDD:449359"
     Site            order(574..578,580,582,593,595,596..597,599..600,604,610,
                     618,630,633,658..659)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187736"
     Region          791..908
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Site            799
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          800..1113
                     /region_name="Interaction with PDCD6.
                     /evidence=ECO:0000269|PubMed:16957052"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          <800..>1098
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          842..848
                     /region_name="ALG-2-binding site motif-2 (ABS-2)"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          924..1096
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Site            1161
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94979.3)"
     Site            1163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O94979.3)"
     CDS             1..1220
                     /gene="SEC31A"
                     /gene_synonym="ABP125; ABP130; HPBKS; HSPC275; HSPC334;
                     NEDSOSB; SEC31L1"
                     /coded_by="NM_001400164.1:68..3730"
                     /note="isoform 1 is encoded by transcript variant 20"
                     /db_xref="CCDS:CCDS3596.1"
                     /db_xref="GeneID:22872"
                     /db_xref="HGNC:HGNC:17052"
                     /db_xref="MIM:610257"
ORIGIN      
        1 mklkevdrta mqawspaqnh piylatgtsa qqldatfstn asleifeldl sdpsldmksc
       61 atfssshryh kliwgpykmd skgdvsgvli aggengniil ydpskiiagd kevviaqndk
      121 htgpvraldv nifqtnlvas ganeseiyiw dlnnfatpmt pgaktqpped isciawnrqv
      181 qhilasasps gratvwdlrk nepiikvsdh snrmhcsgla whpdvatqmv laseddrlpv
      241 iqmwdlrfas splrvlenha rgilaiawsm adpelllscg kdakilcsnp ntgevlyelp
      301 tntqwcfdiq wcprnpavls aasfdgrisv ysimggstdg lrqkqvdkls ssfgnldpfg
      361 tgqplpplqi pqqtaqhsiv lplkkppkwi rrpvgasfsf ggklvtfenv rmpshqgaeq
      421 qqqqhhvfis qvvtekefls rsdqlqqavq sqgfinycqk kidasqtefe knvwsflkvn
      481 feddsrgkyl ellgyrkedl gkkialalnk vdganvalkd sdqvaqsdge espaaeeqll
      541 gehikeekee seflpssggt fnisvsgdid glitqalltg nfesavdlcl hdnrmadaii
      601 laiaggqell artqkkyfak sqskitrlit avvmknwkei vescdlknwr ealaavltya
      661 kpdefsalcd llgtrleneg dsllqtqacl cyicagnvek lvacwtkaqd gshplslqdl
      721 iekvvilrka vqltqamdts tvgvllaakm sqyanllaaq gsiaaalafl pdntnqpnim
      781 qlrdrlcraq gepvaghesp kipyekqqlp kgrpgpvagh hqmprvqtqq yyphgenppp
      841 pgfimhgnvn pnaagqlpts pghmhtqvpp ypqpqpyqpa qpypfgtggs amyrpqqpva
      901 pptsnaypnt pyissassyt gqsqlyaaqh qassptsspa tsfppppssg asfqhggpga
      961 ppsssayalp pgttgtlpaa selpasqrtg pqngwndppa lnrvpkkkkm penfmppvpi
     1021 tspimnplgd pqsqmlqqqp sapvplssqs sfpqphlpgg qpfhgvqqpl gqtgmppsfs
     1081 kpniegapga pigntfqhvq slptkkitkk pipdehlilk ttfedliqrc lssatdpqtk
     1141 rklddaskrl eflydklreq tlsptitsgl hniarsietr nysegltmht hivstsnfse
     1201 tsafmpvlkv vltqanklgv
//
LOCUS       NP_055617               1000 aa            linear   PRI 21-NOV-2025
DEFINITION  C2 domain-containing protein 5 isoform e [Homo sapiens].
ACCESSION   NP_055617
VERSION     NP_055617.1
DBSOURCE    REFSEQ: accession NM_014802.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1000)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1000)
  AUTHORS   Chapman,D.E., Reddy,B.J.N., Huy,B., Bovyn,M.J., Cruz,S.J.S.,
            Al-Shammari,Z.M., Han,H., Wang,W., Smith,D.S. and Gross,S.P.
  TITLE     Regulation of in vivo dynein force production by CDK5 and
            14-3-3epsilon and KIAA0528
  JOURNAL   Nat Commun 10 (1), 228 (2019)
   PUBMED   30651536
  REMARK    GeneRIF: Study finds that CDK5, 14-3-3 epsilon, and KIAA0528 are
            all essential for cytoplasmic dynein force adaptation and that they
            regulate the transport of lipid droplets, lysosomes, and
            mitochondria.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1000)
  AUTHORS   Lu,Y., Ma,J., Li,Y., Huang,J., Zhang,S., Yin,Z., Ren,J., Huang,K.,
            Wu,G., Yang,K. and Xu,S.
  TITLE     CDP138 silencing inhibits TGF-beta/Smad signaling to impair
            radioresistance and metastasis via GDF15 in lung cancer
  JOURNAL   Cell Death Dis 8 (9), e3036 (2017)
   PUBMED   28880265
  REMARK    GeneRIF: Enhanced radiosensitivity and decreased migration in cells
            caused by CDP138 knockdown are partially dependent on GDF15
            inhibition.
            Erratum:[Cell Death Dis. 2024 Jul 31;15(7):549. doi:
            10.1038/s41419-024-06823-2. PMID: 39085215]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1000)
  AUTHORS   Xu,S., Li,X., Gong,Z., Wang,W., Li,Y., Nair,B.C., Piao,H., Yang,K.,
            Wu,G. and Chen,J.
  TITLE     Proteomic analysis of the human cyclin-dependent kinase family
            reveals a novel CDK5 complex involved in cell growth and migration
  JOURNAL   Mol Cell Proteomics 13 (11), 2986-3000 (2014)
   PUBMED   25096995
REFERENCE   7  (residues 1 to 1000)
  AUTHORS   Xie,X., Gong,Z., Mansuy-Aubert,V., Zhou,Q.L., Tatulian,S.A.,
            Sehrt,D., Gnad,F., Brill,L.M., Motamedchaboki,K., Chen,Y.,
            Czech,M.P., Mann,M., Kruger,M. and Jiang,Z.Y.
  TITLE     C2 domain-containing phosphoprotein CDP138 regulates GLUT4
            insertion into the plasma membrane
  JOURNAL   Cell Metab 14 (3), 378-389 (2011)
   PUBMED   21907143
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK310753.1, AY166851.1 and BP418369.1.
            
            Transcript Variant: This variant (6) lacks two alternate exons, but
            maintains the reading frame, compared to variant 1. The encoded
            isoform (e) is shorter than isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY166851.1, SRR18074969.2431812.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..1000
                     /product="C2 domain-containing protein 5 isoform e"
                     /note="138 kDa C2 domain-containing phosphoprotein; C2
                     domain-containing protein 5"
                     /calculated_mol_wt=110316
     Region          5..114
                     /region_name="C2_KIAA0528-like"
                     /note="C2 domain found in the Human KIAA0528 cDNA clone;
                     cd08688"
                     /db_xref="CDD:176070"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT2.
                     /evidence=ECO:0000269|PubMed:21907143; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:21907143; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Region          265..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TPS5; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            305
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TPS5; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            601
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Region          639..669
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TPS5; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            659
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TPS5; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            666
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            807
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            817
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TPS5; propagated from
                     UniProtKB/Swiss-Prot (Q86YS7.1)"
     Site            852
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q86YS7.1)"
     CDS             1..1000
                     /gene="C2CD5"
                     /gene_synonym="CDP138; KIAA0528"
                     /coded_by="NM_014802.3:253..3255"
                     /note="isoform e is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS31758.1"
                     /db_xref="GeneID:9847"
                     /db_xref="HGNC:HGNC:29062"
                     /db_xref="MIM:618044"
ORIGIN      
        1 mpgklkvkiv agrhlpvmdr asdltdafve vkfgnttfkt dvylkslnpq wnsewfkfev
       61 ddedlqdepl qitvldhdty sandaigkvy ididpllyse aatvisgwfp iydtihgirg
      121 einvvvkvdl fndlnrfrqs scgvkffctt sipkcyravi ihgfveelvv nedpeyqwid
      181 rirtprasne arqrlislms gelqrkiglk vlemrgnavv gylqcfdleg esglvvraig
      241 tactldklss paaflpacns pskemkeipf nedpnpnths sgpstplknq tysfspsksy
      301 srqssssdtd lsltpktgmg sgsagkeggp fkallrqqtq saleqrefpf ftltafppgf
      361 lvhvggvvsa rsvklldrih npdepetrda wwaeirqeik shakalgcha vvgysestsi
      421 ceevcilsas gtaavlnprf lqdgtvegcl eqrleenlpt rcgfchipyd elnmpfpahl
      481 tycyncrkqk vpdvlfttid lptdatvigk gcliqarlcr lkkkaqaean ataisnllpf
      541 meyevhtqlm nklklkgmna lfglriqitv genmlmglas atgvylaalp tpggiqiagk
      601 tpndgsyeqh ishmqkkind tiaknkelye inppeiseei igspipeprq rsrllrsqse
      661 ssdevteldl shgkkdafvl eiddtdamed vhslltdvpp psgfyscnte impginnwts
      721 eiqmftsvrv irlsslnltn qalnknfndl cenllkslyf klrsmipccl chvnftvslp
      781 edeliqvtvt avaitfdknq alqttktpve kslqrastdn eellqfplel csdslpshpf
      841 ppakamtvek aspvgdgnfr nrsappcans tvgvvkmtpl sfipgakitk ylgiinmffi
      901 rettslreeg gvsgflhafi aevfamvrah vaalggnavv syimkqcvfm enpnknqaqc
      961 linvsgdavv fvresdlevv ssqqpttncq ssctegevtt
//
LOCUS       NP_001363710             523 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 40 [Homo sapiens].
ACCESSION   NP_001363710
VERSION     NP_001363710.1
DBSOURCE    REFSEQ: accession NM_001376781.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Muckenfuss,L.M., Migenda Herranz,A.C., Boneberg,F.M., Clerici,M.
            and Jinek,M.
  TITLE     Fip1 is a multivalent interaction scaffold for processing factors
            in human mRNA 3' end biogenesis
  JOURNAL   Elife 11, e80332 (2022)
   PUBMED   36073787
  REMARK    GeneRIF: Fip1 is a multivalent interaction scaffold for processing
            factors in human mRNA 3' end biogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Tennenbaum,J., Groh,M., Venditti,L., Campos-Gazeau,F., Chalayer,E.,
            De Broucker,T., Hamidou,M., Hunault,M., Lyoubi,A., Meunier,R.,
            Muron,T., Sene,D., Slama,B., Guidoux,C., Lefevre,G., Kahn,J.E.,
            Denier,C. and Rohmer,J.
  TITLE     FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a Treatable
            Cause of Watershed Infarction
  JOURNAL   Stroke 52 (10), e605-e609 (2021)
   PUBMED   34304603
  REMARK    GeneRIF: FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a
            Treatable Cause of Watershed Infarction.
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 523)
  AUTHORS   Helbig,G., Lewandowski,K., Swiderska,A., Rodzaj,M., Seferynska,I.
            and Gajkowska-Kulik,J.
  TITLE     Exquisite response to imatinib mesylate in FIP1L1-PDGFRA-mutated
            hypereosinophilic syndrome: a 12-year experience of the Polish
            Hypereosinophilic Syndrome Study Group
  JOURNAL   Pol Arch Intern Med 130 (3), 255-257 (2020)
   PUBMED   32125294
  REMARK    GeneRIF: Exquisite response to imatinib mesylate in
            FIP1L1-PDGFRA-mutated hypereosinophilic syndrome: a 12-year
            experience of the Polish Hypereosinophilic Syndrome Study Group.
REFERENCE   6  (residues 1 to 523)
  AUTHORS   Cools,J., Quentmeier,H., Huntly,B.J., Marynen,P., Griffin,J.D.,
            Drexler,H.G. and Gilliland,D.G.
  TITLE     The EOL-1 cell line as an in vitro model for the study of
            FIP1L1-PDGFRA-positive chronic eosinophilic leukemia
  JOURNAL   Blood 103 (7), 2802-2805 (2004)
   PUBMED   14630792
  REMARK    GeneRIF: results indicate that the fusion of FIP1L1 to PDGFRA
            occurs rarely in leukemia cell lines
REFERENCE   7  (residues 1 to 523)
  AUTHORS   Kaufmann,I., Martin,G., Friedlein,A., Langen,H. and Keller,W.
  TITLE     Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements
            and stimulates poly(A) polymerase
  JOURNAL   EMBO J 23 (3), 616-626 (2004)
   PUBMED   14749727
REFERENCE   8  (residues 1 to 523)
  AUTHORS   Pardanani,A., Ketterling,R.P., Brockman,S.R., Flynn,H.C.,
            Paternoster,S.F., Shearer,B.M., Reeder,T.L., Li,C.Y., Cross,N.C.,
            Cools,J., Gilliland,D.G., Dewald,G.W. and Tefferi,A.
  TITLE     CHIC2 deletion, a surrogate for FIP1L1-PDGFRA fusion, occurs in
            systemic mastocytosis associated with eosinophilia and predicts
            response to imatinib mesylate therapy
  JOURNAL   Blood 102 (9), 3093-3096 (2003)
   PUBMED   12842979
  REMARK    GeneRIF: observations suggest that the FIP1L1-PDGFRA rearrangement
            occurs in an early hematopoietic progenitor and suggests that the
            molecular pathogenesis for a subset of SMCD patients is similar to
            that of HES
REFERENCE   9  (residues 1 to 523)
  AUTHORS   Griffin,J.H., Leung,J., Bruner,R.J., Caligiuri,M.A. and
            Briesewitz,R.
  TITLE     Discovery of a fusion kinase in EOL-1 cells and idiopathic
            hypereosinophilic syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (13), 7830-7835 (2003)
   PUBMED   12808148
REFERENCE   10 (residues 1 to 523)
  AUTHORS   Cools,J., DeAngelo,D.J., Gotlib,J., Stover,E.H., Legare,R.D.,
            Cortes,J., Kutok,J., Clark,J., Galinsky,I., Griffin,J.D.,
            Cross,N.C., Tefferi,A., Malone,J., Alam,R., Schrier,S.L.,
            Schmid,J., Rose,M., Vandenberghe,P., Verhoef,G., Boogaerts,M.,
            Wlodarska,I., Kantarjian,H., Marynen,P., Coutre,S.E., Stone,R. and
            Gilliland,D.G.
  TITLE     A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes
            as a therapeutic target of imatinib in idiopathic hypereosinophilic
            syndrome
  JOURNAL   N Engl J Med 348 (13), 1201-1214 (2003)
   PUBMED   12660384
  REMARK    GeneRIF: The hypereosinophilic syndrome may result from a novel
            fusion tyrosine kinase - FIP1L1-PDGFRalpha - that is a consequence
            of an interstitial chromosomal deletion.
            GeneRIF: Describes the fusion gene Fip1-like-1-PDGFRalpha in
            patients with idiopathic hypereosinophilic syndrome, mostly
            responsive to imatinib therapy.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098821.3 and AC058822.6.
            
            Summary: This gene encodes a subunit of the CPSF (cleavage and
            polyadenylation specificity factor) complex that polyadenylates the
            3' end of mRNA precursors. This gene, the homolog of yeast Fip1
            (factor interacting with PAP), binds to U-rich sequences of
            pre-mRNA and stimulates poly(A) polymerase activity. Its N-terminus
            contains a PAP-binding site and its C-terminus an RNA-binding
            domain. An interstitial chromosomal deletion on 4q12 creates an
            in-frame fusion of human genes FIP1L1 and PDGFRA (platelet-derived
            growth factor receptor, alpha). The FIP1L1-PDGFRA fusion gene
            encodes a constitutively activated tyrosine kinase that joins the
            first 233 amino acids of FIP1L1 to the last 523 amino acids of
            PDGFRA. This gene fusion and chromosomal deletion is the cause of
            some forms of idiopathic hypereosinophilic syndrome (HES). This
            syndrome, recently reclassified as chronic eosinophilic leukemia
            (CEL), is responsive to treatment with tyrosine kinase inhibitors.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.44475.1,
                                           SRR14372079.3597727.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..523
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     40"
                     /note="rearranged in hypereosinophilia; pre-mRNA
                     3'-end-processing factor FIP1; FIP1-like 1 protein; factor
                     interacting with PAP; FIP1 like 1; FIP1L1 cleavage and
                     polyadenylation specific factor subunit"
                     /calculated_mol_wt=58617
     Region          139..181
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     CDS             1..523
                     /gene="FIP1L1"
                     /gene_synonym="FIP1; hFip1; Rhe"
                     /coded_by="NM_001376781.1:199..1770"
                     /note="isoform 40 is encoded by transcript variant 40"
                     /db_xref="CCDS:CCDS93523.1"
                     /db_xref="GeneID:81608"
                     /db_xref="HGNC:HGNC:19124"
                     /db_xref="MIM:607686"
ORIGIN      
        1 msageverlv selsggtggd eeeewlygde neverpeeen asanppsgie detaengvpk
       61 pkvtetedds dsdsdddedd vhvtigdikt gapqygsygt apvnlniktg grvygttgtk
      121 vkgvdldapg singvpllev dldsfedkpw rkpgadlsdy fnygfnedtw kaycekqkri
      181 rmglevipvt sttnkitvqq grtgnseket alpstkaeft sppslfktgl ppsrrlpgai
      241 dvigqtitis rvegrrrane nsniqvlser satevdnnfs kpppffppga ppthlppppf
      301 lpppptvsta pplipppgfp pppgapppsl iptiesghss gydsrsaraf pygnvafphl
      361 pgsapswpsl vdtskqwdyy arrekdrdre rdrdrerdrd rdrerertre rererdhspt
      421 psvfnrfvgd eeryryreya ergyerhras rekeerhrer rhrekeetrh kssrsnsrrr
      481 heseegdshr rhkhkkskrs kegkeagsep apeqesteat pae
//
LOCUS       NP_001313508             261 aa            linear   PRI 21-NOV-2025
DEFINITION  syntaxin-7 isoform a [Homo sapiens].
ACCESSION   NP_001313508
VERSION     NP_001313508.1
DBSOURCE    REFSEQ: accession NM_001326579.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Wu,J., Zhang,H., Yang,L., Chen,Y., Li,J., Yang,M., Zhang,X., He,C.,
            Wang,X. and Xu,X.
  TITLE     Syntaxin 7 modulates seizure activity in epilepsy
  JOURNAL   Neurobiol Dis 181, 106118 (2023)
   PUBMED   37031804
  REMARK    GeneRIF: Syntaxin 7 modulates seizure activity in epilepsy.
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Parveen,S., Khamari,A., Raju,J., Coppolino,M.G. and Datta,S.
  TITLE     Syntaxin 7 contributes to breast cancer cell invasion by promoting
            invadopodia formation
  JOURNAL   J Cell Sci 135 (12) (2022)
   PUBMED   35762511
  REMARK    GeneRIF: Syntaxin 7 contributes to breast cancer cell invasion by
            promoting invadopodia formation.
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Miao,G., Zhao,H., Li,Y., Ji,M., Chen,Y., Shi,Y., Bi,Y., Wang,P. and
            Zhang,H.
  TITLE     ORF3a of the COVID-19 virus SARS-CoV-2 blocks HOPS complex-mediated
            assembly of the SNARE complex required for autolysosome formation
  JOURNAL   Dev Cell 56 (4), 427-442 (2021)
   PUBMED   33422265
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Nakamura,N., Yamamoto,A., Wada,Y. and Futai,M.
  TITLE     Syntaxin 7 mediates endocytic trafficking to late endosomes
  JOURNAL   J Biol Chem 275 (9), 6523-6529 (2000)
   PUBMED   10692457
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Prekeris,R., Yang,B., Oorschot,V., Klumperman,J. and Scheller,R.H.
  TITLE     Differential roles of syntaxin 7 and syntaxin 8 in endosomal
            trafficking
  JOURNAL   Mol Biol Cell 10 (11), 3891-3908 (1999)
   PUBMED   10564279
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Steegmaier,M., Yang,B., Yoo,J.S., Huang,B., Shen,M., Yu,S., Luo,Y.
            and Scheller,R.H.
  TITLE     Three novel proteins of the syntaxin/SNAP-25 family
  JOURNAL   J Biol Chem 273 (51), 34171-34179 (1998)
   PUBMED   9852078
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Wong,S.H., Xu,Y., Zhang,T. and Hong,W.
  TITLE     Syntaxin 7, a novel syntaxin member associated with the early
            endosomal compartment
  JOURNAL   J Biol Chem 273 (1), 375-380 (1998)
   PUBMED   9417091
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Wang,H., Frelin,L. and Pevsner,J.
  TITLE     Human syntaxin 7: a Pep12p/Vps6p homologue implicated in vesicle
            trafficking to lysosomes
  JOURNAL   Gene 199 (1-2), 39-48 (1997)
   PUBMED   9358037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL589691.4 and AL357034.18.
            
            Summary: The protein encoded by this gene is a syntaxin family
            membrane receptor involved in vesicle transport. The encoded
            protein binds alpha-SNAP, an important regulator of transport
            vesicle fusion. Along with syntaxin 13, this protein plays a role
            in the ordered fusion of endosomes and lysosomes with the
            phagosome. [provided by RefSeq, May 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, and 3 all encode the same isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.347881.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q23.2"
     Protein         1..261
                     /product="syntaxin-7 isoform a"
                     /calculated_mol_wt=29684
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:12665801,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (O15400.4)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15400.4)"
     Region          18..119
                     /region_name="Syntaxin_2"
                     /note="Syntaxin-like protein; pfam14523"
                     /db_xref="CDD:464199"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15400.4)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15400.4)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O70439; propagated from
                     UniProtKB/Swiss-Prot (O15400.4)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70439; propagated from
                     UniProtKB/Swiss-Prot (O15400.4)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15400.4)"
     Region          129..148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15400.4)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O15400.4)"
     Region          168..227
                     /region_name="SNARE_syntaxin7"
                     /note="SNARE motif of syntaxin 7; cd15875"
                     /db_xref="CDD:277228"
     Site            order(171..172,174..176,178..179,181..183,185..186,
                     188..193,195..197,199..200,202..204,206..207,209..214,
                     216..221,223..225)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277228"
     Site            199
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277228"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O15400.4)"
     Site            239..259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15400.4)"
     CDS             1..261
                     /gene="STX7"
                     /coded_by="NM_001326579.2:115..900"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS5153.1"
                     /db_xref="GeneID:8417"
                     /db_xref="HGNC:HGNC:11442"
                     /db_xref="MIM:603217"
ORIGIN      
        1 msytpgvggd paqlaqriss niqkitqcsv eiqrtlnqlg tpqdspelrq qlqqkqqytn
       61 qlaketdkyi kefgslpttp seqrqrkiqk drlvaeftts ltnfqkvqrq aaerekefva
      121 rvrassrvsg sfpedssker nlvswesqtq pqvqvqdeei teddlrlihe ressirqlea
      181 dimdineifk dlgmmiheqg dvidsieanv enaevhvqqa nqqlsraady qrksrktlci
      241 iililvigva iisliiwgln h
//
LOCUS       NP_001362957             523 aa            linear   PRI 21-NOV-2025
DEFINITION  protein 4.1 isoform 23 [Homo sapiens].
ACCESSION   NP_001362957 XP_016856093
VERSION     NP_001362957.1
DBSOURCE    REFSEQ: accession NM_001376028.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Terada,N., Saitoh,Y., Saito,M., Yamada,T., Kamijo,A., Yoshizawa,T.
            and Sakamoto,T.
  TITLE     Recent Progress on Genetically Modified Animal Models for Membrane
            Skeletal Proteins: The 4.1 and MPP Families
  JOURNAL   Genes (Basel) 14 (10), 1942 (2023)
   PUBMED   37895291
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 523)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 523)
  AUTHORS   Dalla Venezia,N., Gilsanz,F., Alloisio,N., Ducluzeau,M.T.,
            Benz,E.J. Jr. and Delaunay,J.
  TITLE     Homozygous 4.1(-) hereditary elliptocytosis associated with a point
            mutation in the downstream initiation codon of protein 4.1 gene
  JOURNAL   J Clin Invest 90 (5), 1713-1717 (1992)
   PUBMED   1430200
REFERENCE   7  (residues 1 to 523)
  AUTHORS   Jons,T. and Drenckhahn,D.
  TITLE     Identification of the binding interface involved in linkage of
            cytoskeletal protein 4.1 to the erythrocyte anion exchanger
  JOURNAL   EMBO J 11 (8), 2863-2867 (1992)
   PUBMED   1639060
REFERENCE   8  (residues 1 to 523)
  AUTHORS   Subrahmanyam,G., Bertics,P.J. and Anderson,R.A.
  TITLE     Phosphorylation of protein 4.1 on tyrosine-418 modulates its
            function in vitro
  JOURNAL   Proc Natl Acad Sci U S A 88 (12), 5222-5226 (1991)
   PUBMED   1647028
REFERENCE   9  (residues 1 to 523)
  AUTHORS   Conboy,J.G., Chan,J.Y., Chasis,J.A., Kan,Y.W. and Mohandas,N.
  TITLE     Tissue- and development-specific alternative RNA splicing regulates
            expression of multiple isoforms of erythroid membrane protein 4.1
  JOURNAL   J Biol Chem 266 (13), 8273-8280 (1991)
   PUBMED   2022644
REFERENCE   10 (residues 1 to 523)
  AUTHORS   Horne,W.C., Prinz,W.C. and Tang,E.K.
  TITLE     Identification of two cAMP-dependent phosphorylation sites on
            erythrocyte protein 4.1
  JOURNAL   Biochim Biophys Acta 1055 (1), 87-92 (1990)
   PUBMED   2171679
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL009181.1, AL138785.8 and
            AL357500.17.
            
            On Nov 7, 2019 this sequence version replaced XP_016856093.1.
            
            Summary: The protein encoded by this gene, together with spectrin
            and actin, constitute the red cell membrane cytoskeletal network.
            This complex plays a critical role in erythrocyte shape and
            deformability. Mutations in this gene are associated with type 1
            elliptocytosis (EL1). Alternatively spliced transcript variants
            encoding different isoforms have been described for this
            gene.[provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.245300.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2156099, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.3"
     Protein         1..523
                     /product="protein 4.1 isoform 23"
                     /note="protein 4.1; erythrocyte surface protein band 4.1;
                     P4.1; EPB4.1; elliptocytosis 1, RH-linked"
                     /calculated_mol_wt=59195
     Region          2..192
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          187..280
                     /region_name="FERM_C_4_1_family"
                     /note="FERM domain C-lobe of Protein 4.1 family; cd13184"
                     /db_xref="CDD:270005"
     Site            order(196,213,215,221)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270005"
     Site            order(225,230..233,268,272,275..276)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Site            268..279
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Region          290..333
                     /region_name="FA"
                     /note="FERM adjacent (FA); pfam08736"
                     /db_xref="CDD:462582"
     Region          405..451
                     /region_name="SAB"
                     /note="SAB domain; pfam04382"
                     /db_xref="CDD:461285"
     CDS             1..523
                     /gene="EPB41"
                     /gene_synonym="4.1R; EL1; HE"
                     /coded_by="NM_001376028.1:729..2300"
                     /note="isoform 23 is encoded by transcript variant 22"
                     /db_xref="GeneID:2035"
                     /db_xref="HGNC:HGNC:3377"
                     /db_xref="MIM:130500"
ORIGIN      
        1 mhckvslldd tvyecvvekh akgqdllkrv cehlnlleed yfglaiwdna tsktwldsak
       61 eikkqvrgvp wnftfnvkfy ppdpaqlted itryylclql rqdivagrlp csfatlallg
      121 sytiqselgd ydpelhgvdy vsdfklapnq tkeleekvme lhksyrsmtp aqadleflen
      181 akklsmygvd lhkakdlegv diilgvcssg llvykdklri nrfpwpkvlk isykrssffi
      241 kirpgeqeqy estigfklps yraakklwkv cvehhtffrl tstdtipksk flalgskfry
      301 sgrtqaqtrq asalidrpap hfertaskra srsldgaavd sadrsprpts apaitqgqva
      361 eggvldasak ktvvpkaqke tvkaevkked eppeqaepep teawkdldks qeeikkhhas
      421 iselkknfme svpeprpsew dkrlsthspf rtlningqip tgegvkktsv lpserkvggp
      481 espsyflpdt yhlgvckepv lnfqtdqrrl aqlrelrakf fls
//
LOCUS       NP_001362690            1076 aa            linear   PRI 21-NOV-2025
DEFINITION  GRB10-interacting GYF protein 1 isoform a [Homo sapiens].
ACCESSION   NP_001362690 XP_016868018
VERSION     NP_001362690.1
DBSOURCE    REFSEQ: accession NM_001375761.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Lee,C.Y., Hubrich,D., Varga,J.K., Schafer,C., Welzel,M.,
            Schumbera,E., Djokic,M., Strom,J.M., Schonfeld,J., Geist,J.L.,
            Polat,F., Gibson,T.J., Keller Valsecchi,C.I., Kumar,M.,
            Schueler-Furman,O. and Luck,K.
  TITLE     Systematic discovery of protein interaction interfaces using
            AlphaFold and experimental validation
  JOURNAL   Mol Syst Biol 20 (2), 75-97 (2024)
   PUBMED   38225382
REFERENCE   4  (residues 1 to 1076)
  AUTHORS   Zhu,L., Yao,Z., Luo,Q., Liu,Y., Zhao,W., Shao,C., Shao,S. and
            Cui,F.
  TITLE     Low Expression of GIGYF1 Inhibits Metastasis, Proliferation, and
            Promotes Apoptosis and Autophagy of Gastric Cancer Cells
  JOURNAL   Int J Med Sci 20 (8), 1038-1045 (2023)
   PUBMED   37484805
  REMARK    GeneRIF: Low Expression of GIGYF1 Inhibits Metastasis,
            Proliferation, and Promotes Apoptosis and Autophagy of Gastric
            Cancer Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1076)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1076)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 1076)
  AUTHORS   Ajiro,M., Nishidate,T., Katagiri,T. and Nakamura,Y.
  TITLE     Critical involvement of RQCD1 in the EGFR-Akt pathway in mammary
            carcinogenesis
  JOURNAL   Int J Oncol 37 (5), 1085-1093 (2010)
   PUBMED   20878056
REFERENCE   8  (residues 1 to 1076)
  AUTHORS   Kofler,M.M. and Freund,C.
  TITLE     The GYF domain
  JOURNAL   FEBS J 273 (2), 245-256 (2006)
   PUBMED   16403013
  REMARK    Review article
REFERENCE   9  (residues 1 to 1076)
  AUTHORS   Giovannone,B., Lee,E., Laviola,L., Giorgino,F., Cleveland,K.A. and
            Smith,R.J.
  TITLE     Two novel proteins that are linked to insulin-like growth factor
            (IGF-I) receptors by the Grb10 adapter and modulate IGF-I signaling
  JOURNAL   J Biol Chem 278 (34), 31564-31573 (2003)
   PUBMED   12771153
REFERENCE   10 (residues 1 to 1076)
  AUTHORS   Wilson,M.D., Riemer,C., Martindale,D.W., Schnupf,P., Boright,A.P.,
            Cheung,T.L., Hardy,D.M., Schwartz,S., Scherer,S.W., Tsui,L.C.,
            Miller,W. and Koop,B.F.
  TITLE     Comparative analysis of the gene-dense ACHE/TFR2 region on human
            chromosome 7q22 with the orthologous region on mouse chromosome 5
  JOURNAL   Nucleic Acids Res 29 (6), 1352-1365 (2001)
   PUBMED   11239002
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009488.5.
            
            On Nov 1, 2019 this sequence version replaced XP_016868018.1.
            
            Summary: This gene encodes a member of the gyf family of adaptor
            proteins. The encoded protein contains a gyf protein interaction
            domain. It binds growth factor receptor bound 10, another adaptor
            protein that binds activated insulin-like growth factor 1 and
            insulin receptors and regulates receptor signaling. [provided by
            RefSeq, Apr 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038194.3536053.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..1076
                     /product="GRB10-interacting GYF protein 1 isoform a"
                     /note="postmeiotic segregation increased 2-like 12; PERQ
                     amino acid-rich with GYF domain-containing protein 1"
                     /calculated_mol_wt=118648
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Region          105..422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75420.2)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MR1; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Region          476..529
                     /region_name="GYF"
                     /note="GYF domain: contains conserved Gly-Tyr-Phe
                     residues; Proline-binding domain in CD2-binding and other
                     proteins. Involved in signaling lymphocyte activity. Also
                     present in other unrelated proteins (mainly unknown)
                     derived from diverse eukaryotic species; cd00072"
                     /db_xref="CDD:238027"
     Site            488..504
                     /site_type="active"
                     /note="proline binding motif [active]"
                     /db_xref="CDD:238027"
     Site            order(498,503..504)
                     /site_type="active"
                     /note="proline interaction residues [active]"
                     /db_xref="CDD:238027"
     Site            538
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Region          621..640
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75420.2)"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Region          696..724
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75420.2)"
     Region          825..879
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75420.2)"
     Site            862
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     CDS             1..1076
                     /gene="GIGYF1"
                     /gene_synonym="GYF1; PERQ1"
                     /coded_by="NM_001375761.1:576..3806"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:64599"
                     /db_xref="HGNC:HGNC:9126"
                     /db_xref="MIM:612064"
ORIGIN      
        1 maaetlnfgp ewlralsggg svaspppspa mpkykladyr ygreemlaly vkenkvpeel
       61 qdkefaavlq deplqplale plteeeqrnf slsvnsvavl rlmgkgagpp lagtsrgrgs
      121 trsrgrgrgd scfyqrsiee gdgafgrspr eiqrsqswdd rgerrfeksa rrdgarcgfe
      181 eggagprkeh arsdsenwrs lreeqeeeee gswrlgagpr rdgdrwrsas pdggprsagw
      241 rehgerrrkf efdlrgdrgg cgeeegrggg gsshlrrcra pegfeedkdg lpewcldded
      301 eemgtfdasg aflplkkgpk epipeeqeld fqgleeeeep segleeegpe aggkeltplp
      361 pqeeksssps plptlgplwg tngdgdetae keppaaeddi rgiqlspgvg ssagppgdle
      421 ddeglkhlqq eaeklvaslq dssleeeqft aamqtqglrh saaatalpls hgaarkwfyk
      481 dpqgeiqgpf ttqemaewfq agyfsmsllv krgcdegfqp lgevikmwgr vpfapgpspp
      541 pllgnmdqer lkkqqelaaa alyqqlqhqq flqlvssrql pqcalrekaa lgdltppppp
      601 ppqqqqqqlt aflqqlqalk pprggdqnll ptmsrslsvp dsgrlwdvht sassqsggea
      661 slwdipinss tqgpileqlq lqhkfqerre velrakreee erkrreekrr qqqqeeqkrr
      721 qeeeelfrrk hvrqqelllk llqqqqavpv ppapsspppl waglakqgls mktllelqle
      781 gerqlhkqpp preparaqap nhrvqlgglg taplnqwvse agplwggpdk sgggssglgl
      841 wedtpksggs lvrglglkns rsspslsdsy shlsgrpirk kteeeekllk llqgiprpqd
      901 gftqwceqml htlsatgsld vpmavailke vespydvhdy irsclgdtle akefakqfle
      961 rrakqkasqq rqqqqeawls saslqtafqa nhstklgpge gskakrralm lhsdpsilge
     1021 lgwgrsgtsl aqgrrspges sdaasprlqg tpctdllvrs rawmttdqpg ppapgl
//
LOCUS       NP_001373390             453 aa            linear   PRI 21-NOV-2025
DEFINITION  plasminogen activator inhibitor 1 isoform 7 precursor [Homo
            sapiens].
ACCESSION   NP_001373390
VERSION     NP_001373390.1
DBSOURCE    REFSEQ: accession NM_001386461.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Doelker,T., Gallwas,J. and Grundker,C.
  TITLE     Suppressing Expression of SERPINE1/PAI1 Through Activation of GPER1
            Reduces Progression of Vulvar Carcinoma
  JOURNAL   Cancer Genomics Proteomics 21 (6), 566-579 (2024)
   PUBMED   39467628
  REMARK    GeneRIF: Suppressing Expression of SERPINE1/PAI1 Through Activation
            of GPER1 Reduces Progression of Vulvar Carcinoma.
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Khoukaz,H.B., Vadali,M., Schoenherr,A., Ramirez-Perez,F.I.,
            Morales-Quinones,M., Sun,Z., Fujie,S., Foote,C.A., Lyu,Z., Zeng,S.,
            Augenreich,M.A., Cai,D., Chen,S.Y., Joshi,T., Ji,Y., Hill,M.A.,
            Martinez-Lemus,L.A. and Fay,W.P.
  TITLE     PAI-1 Regulates the Cytoskeleton and Intrinsic Stiffness of
            Vascular Smooth Muscle Cells
  JOURNAL   Arterioscler Thromb Vasc Biol 44 (10), 2191-2203 (2024)
   PUBMED   38868940
  REMARK    GeneRIF: PAI-1 Regulates the Cytoskeleton and Intrinsic Stiffness
            of Vascular Smooth Muscle Cells.
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Guo,X., Zhou,H., Liu,Y., Xu,W., Kanwore,K. and Zhang,L.
  TITLE     Glial-Cell-Line-Derived Neurotrophic Factor Promotes Glioblastoma
            Cell Migration and Invasion via the SMAD2/3-SERPINE1-Signaling Axis
  JOURNAL   Int J Mol Sci 25 (18), 10229 (2024)
   PUBMED   39337713
  REMARK    GeneRIF: Glial-Cell-Line-Derived Neurotrophic Factor Promotes
            Glioblastoma Cell Migration and Invasion via the
            SMAD2/3-SERPINE1-Signaling Axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 453)
  AUTHORS   Yatsenko,T., Rios,R., Nogueira,T., Salama,Y., Takahashi,S.,
            Adachi,E., Tabe,Y., Hattori,N., Osada,T., Naito,T., Takahashi,K.,
            Hattori,K. and Heissig,B.
  TITLE     The influence of 4G/5G polymorphism in the
            plasminogen-activator-inhibitor-1 promoter on COVID-19 severity and
            endothelial dysfunction
  JOURNAL   Front Immunol 15, 1445294 (2024)
   PUBMED   39281671
  REMARK    GeneRIF: The influence of 4G/5G polymorphism in the
            plasminogen-activator-inhibitor-1 promoter on COVID-19 severity and
            endothelial dysfunction.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 453)
  AUTHORS   Heiman,M., Gupta,S., Lewandowska,M. and Shapiro,A.D.
  TITLE     Complete Plasminogen Activator Inhibitor 1 Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   28771291
REFERENCE   7  (residues 1 to 453)
  AUTHORS   Fay,W.P., Shapiro,A.D., Shih,J.L., Schleef,R.R. and Ginsburg,D.
  TITLE     Brief report: complete deficiency of plasminogen-activator
            inhibitor type 1 due to a frame-shift mutation
  JOURNAL   N Engl J Med 327 (24), 1729-1733 (1992)
   PUBMED   1435917
REFERENCE   8  (residues 1 to 453)
  AUTHORS   Koh,S.C., Wong,P.C., Yuen,R., Chua,S.E., Ng,B.L. and Ratnam,S.S.
  TITLE     Concentration of plasminogen activators and inhibitor in the human
            endometrium at different phases of the menstrual cycle
  JOURNAL   J Reprod Fertil 96 (2), 407-413 (1992)
   PUBMED   1339823
REFERENCE   9  (residues 1 to 453)
  AUTHORS   Hagege,J., Peraldi,M.N., Rondeau,E., Adida,C., Delarue,F.,
            Medcalf,R., Schleuning,W.D. and Sraer,J.D.
  TITLE     Plasminogen activator inhibitor-1 deposition in the extracellular
            matrix of cultured human mesangial cells
  JOURNAL   Am J Pathol 141 (1), 117-128 (1992)
   PUBMED   1632457
REFERENCE   10 (residues 1 to 453)
  AUTHORS   Ehrlich,H.J., Gebbink,R.K., Keijer,J., Linders,M., Preissner,K.T.
            and Pannekoek,H.
  TITLE     Alteration of serpin specificity by a protein cofactor. Vitronectin
            endows plasminogen activator inhibitor 1 with thrombin inhibitory
            properties
  JOURNAL   J Biol Chem 265 (22), 13029-13035 (1990)
   PUBMED   1695900
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004876.2.
            
            Summary: This gene encodes a member of the serine proteinase
            inhibitor (serpin) superfamily. This member is the principal
            inhibitor of tissue plasminogen activator (tPA) and urokinase
            (uPA), and hence is an inhibitor of fibrinolysis. The protein also
            functions as a component of innate antiviral immunity. Defects in
            this gene are the cause of plasminogen activator inhibitor-1
            deficiency (PAI-1 deficiency), and high concentrations of the gene
            product are associated with thrombophilia. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1965299, SAMEA1966682
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..453
                     /product="plasminogen activator inhibitor 1 isoform 7
                     precursor"
                     /note="serine (or cysteine) proteinase inhibitor, clade E
                     (nexin, plasminogen activator inhibitor type 1), member 1;
                     endothelial plasminogen activator inhibitor; serpin E1;
                     serpin peptidase inhibitor, clade E (nexin, plasminogen
                     activator inhibitor type 1), member 1"
                     /calculated_mol_wt=48161
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2309
     Region          29..366
                     /region_name="serpin"
                     /note="SERine Proteinase INhibitors (serpin) family;
                     cl38926"
                     /db_xref="CDD:476815"
     Site            232
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05121.1)"
     Site            288
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05121.1)"
     Site            352
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P05121.1)"
     Site            355..365
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381000"
     CDS             1..453
                     /gene="SERPINE1"
                     /gene_synonym="PAI; PAI-1; PAI1; PLANH1"
                     /coded_by="NM_001386461.1:143..1504"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:5054"
                     /db_xref="HGNC:HGNC:8583"
                     /db_xref="MIM:173360"
ORIGIN      
        1 mqmspaltcl vlglalvfge gsavhhppsy vahlasdfgv rvfqqvaqas kdrnvvfspy
       61 gvasvlamlq lttggetqqq iqaamgfkid dkgmapalrh lykelmgpwn kdeisttdai
      121 fvqrdlklvq gfmphffrlf rstvkqvdfs everarfiin dwvkthtkgm isnllgkgav
      181 dqltrlvlvn alyfngqwkt pfpdssthrr lfhksdgstv svpmmaqtnk fnytefttpd
      241 ghyydilelp yhgdtlsmfi aapyekevpl saltnilsaq lishwkgnmt rlprllvlpk
      301 fsletevdlr kplenlgmtd mfrqfqadft slsdqeplhv aqalqkvkie vnesgtvass
      361 stgafvclve tisvpvtlps llyclpprrr lvtgqrpvee tpfhlrvhcg tghpspvqgc
      421 crwqsecpps cgptllawps pspetvcmgy fgv
//
LOCUS       NP_001366482             859 aa            linear   PRI 21-NOV-2025
DEFINITION  KN motif and ankyrin repeat domain-containing protein 2 isoform 1
            [Homo sapiens].
ACCESSION   NP_001366482
VERSION     NP_001366482.1
DBSOURCE    REFSEQ: accession NM_001379553.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Loncaric,M., Stojanovic,N., Rac-Justament,A., Coopmans,K.,
            Majhen,D., Humphries,J.D., Humphries,M.J. and Ambriovic-Ristov,A.
  TITLE     Talin2 and KANK2 functionally interact to regulate microtubule
            dynamics, paclitaxel sensitivity and cell migration in the
            MDA-MB-435S melanoma cell line
  JOURNAL   Cell Mol Biol Lett 28 (1), 56 (2023)
   PUBMED   37460977
  REMARK    GeneRIF: Talin2 and KANK2 functionally interact to regulate
            microtubule dynamics, paclitaxel sensitivity and cell migration in
            the MDA-MB-435S melanoma cell line.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 859)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 859)
  AUTHORS   Xu,Y., Guo,C., Pan,W., Zhao,C., Ding,Y., Xie,X., Wei,Z., Sun,Y. and
            Yu,C.
  TITLE     Nephrotic-syndrome-associated mutation of KANK2 induces pathologic
            binding competition with physiological interactor KIF21A
  JOURNAL   J Biol Chem 297 (2), 100958 (2021)
   PUBMED   34274317
  REMARK    GeneRIF: Nephrotic-syndrome-associated mutation of KANK2 induces
            pathologic binding competition with physiological interactor
            KIF21A.
REFERENCE   5  (residues 1 to 859)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 859)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   7  (residues 1 to 859)
  AUTHORS   Kakinuma,N., Zhu,Y., Wang,Y., Roy,B.C. and Kiyama,R.
  TITLE     Kank proteins: structure, functions and diseases
  JOURNAL   Cell Mol Life Sci 66 (16), 2651-2659 (2009)
   PUBMED   19554261
  REMARK    Review article
REFERENCE   8  (residues 1 to 859)
  AUTHORS   Zhu,Y., Kakinuma,N., Wang,Y. and Kiyama,R.
  TITLE     Kank proteins: a new family of ankyrin-repeat domain-containing
            proteins
  JOURNAL   Biochim Biophys Acta 1780 (2), 128-133 (2008)
   PUBMED   17996375
REFERENCE   9  (residues 1 to 859)
  AUTHORS   Zhang,Y., Zhang,H., Liang,J., Yu,W. and Shang,Y.
  TITLE     SIP, a novel ankyrin repeat containing protein, sequesters steroid
            receptor coactivators in the cytoplasm
  JOURNAL   EMBO J 26 (11), 2645-2657 (2007)
   PUBMED   17476305
  REMARK    GeneRIF: SIP, a novel ankyrin repeat containing protein, sequesters
            steroid receptor coactivators in the cytoplasm.
REFERENCE   10 (residues 1 to 859)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009000.6 and AC011485.6.
            
            Summary: This gene encodes a member of the KN motif and ankyrin
            repeat domains (KANK) family of proteins, which play a role in
            cytoskeletal formation by regulating actin polymerization. The
            encoded protein functions in the sequestration of steroid receptor
            coactivators and possibly other proteins. Mutations in this gene
            are associated with impaired kidney podocyte function and nephrotic
            syndrome, and keratoderma and woolly hair. [provided by RefSeq, Jul
            2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038197.518222.1, AY639929.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..859
                     /product="KN motif and ankyrin repeat domain-containing
                     protein 2 isoform 1"
                     /note="KN motif and ankyrin repeat domain-containing
                     protein 2; kidney ankyrin repeat-containing protein 2;
                     SRC1-interacting protein; matrix-remodeling-associated
                     protein 3; ankyrin repeat domain-containing protein 25;
                     SRC-interacting protein; steroid receptor coactivator
                     interacting protein"
                     /calculated_mol_wt=91791
     Region          1..72
                     /region_name="Interaction with AIFM1.
                     /evidence=ECO:0000269|PubMed:22371500"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          31..69
                     /region_name="KN_motif"
                     /note="KN motif; pfam12075"
                     /db_xref="CDD:432311"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BX02; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BX02; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BX02; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            105
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          139..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BX02; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          304..325
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          <450..593
                     /region_name="LGT"
                     /note="Prolipoprotein diacylglyceryl transferase; cl00478"
                     /db_xref="CDD:469786"
     Site            472
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          622..659
                     /region_name="ANK 0, degenerate.
                     /evidence=ECO:0000269|PubMed:29183992"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          636..672
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <658..833
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          674..706
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          674..704
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          677..843
                     /region_name="Interaction with NCOA1.
                     /evidence=ECO:0000269|PubMed:17476305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          708..743
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          747..777
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(748,752..753,756..758,760..761,765,768,777,779,781,
                     785..786,789..791,793..794,798,801,811,813,815,819..820,
                     823..825,827..828,832,835)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          779..811
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..859
                     /gene="KANK2"
                     /gene_synonym="ANKRD25; MXRA3; NPHS16; PPKWH; SIP"
                     /coded_by="NM_001379553.1:477..3056"
                     /note="isoform 1 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS54219.1"
                     /db_xref="GeneID:25959"
                     /db_xref="HGNC:HGNC:29300"
                     /db_xref="MIM:614610"
ORIGIN      
        1 maqvlhvpap fpgtpgpasp pafpakdpdp pysvetpygy rldldflkyv ddiekghtlr
       61 rvavqrrprl sslprgpgsw wtsteslcsn asgdsrhsay sycgrgfypq ygaletrggf
      121 nprvertlld arrrledqaa tptglgsltp saagstaslv gvglppptpr ssglstpvpp
      181 saghlahvre qmagalrklr qleeqvklip vlqvklsvlq eekrqltvql ksqkflghpt
      241 agrgrselcl dlpdppedpv aletrsvgtw vrerdlgmpd geaalaakva vletqlkkal
      301 qelqaaqarq adpqpqawpp pdspvrvdtv rvvegpreve vvastaagap aqraqslepy
      361 gtglralamp grpesppvfr sqevvetmcp vpaaatsnvh mvkkisiter scdgaaglpe
      421 vpaesssspp gsevasltqp ekstgrvptq epthreptrq aasqeseeag gtapplsspp
      481 ggppagvrsi mkrkeevadp tahrrslqfv gvnggyesss edsstaenis dndsteneap
      541 eprervpsva eapqlrpagt aaaktsrqec qlsresqhip taegasgsnt eeeirmelsp
      601 dlisaclale kyldnpnalt erelkvaytt vlqewlrlac rsdahpelvr rhlvtframs
      661 arlldyvvni adsngntalh ysvshanfpv vqqlldsgvc kvdkqnragy spimltalat
      721 lktqddietv lqlfrlgnin akasqagqta lmlavshgrv dvvkallace advnvqdddg
      781 stalmcaceh ghkeiaglll avpscdislt drdgstalmv aldagqseia smlysrmnik
      841 csfapmsdde sptsssaee
//
LOCUS       NP_001258211            1922 aa            linear   PRI 21-NOV-2025
DEFINITION  endoribonuclease Dicer isoform 1 [Homo sapiens].
ACCESSION   NP_001258211
VERSION     NP_001258211.1
DBSOURCE    REFSEQ: accession NM_001271282.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1922)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1922)
  AUTHORS   Rojo-Pardillo,M., Godefroid,L., Dom,G., Lefort,A., Libert,F.,
            Robaye,B. and Maenhaut,C.
  TITLE     Understanding the Dosage-Dependent Role of Dicer1 in Thyroid
            Tumorigenesis
  JOURNAL   Int J Mol Sci 25 (19), 10701 (2024)
   PUBMED   39409030
  REMARK    GeneRIF: Understanding the Dosage-Dependent Role of Dicer1 in
            Thyroid Tumorigenesis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1922)
  AUTHORS   Mastnikova,K., Bulanova Pekova,B., Kuklikova,V., Vaclavikova,E.,
            Carkova,J., Katra,R., Fialova,L., Vlcek,P., Kodetova,D.,
            Chovanec,M., Drozenova,J., Matej,R., Pacesova,P., Novak,Z.,
            Procykova,K., Vcelak,J. and Bendlova,B.
  TITLE     DICER1 Variants in Pediatric and Young Adult Thyroid Nodules
  JOURNAL   Thyroid 34 (10), 1225-1233 (2024)
   PUBMED   39283830
  REMARK    GeneRIF: DICER1 Variants in Pediatric and Young Adult Thyroid
            Nodules.
REFERENCE   4  (residues 1 to 1922)
  AUTHORS   Dashti,N.K., Swanson,A.A., Bentz,J., Xing,D., Chrisinger,J.S.A.,
            Balzer,B., Guo,R., Schoolmeester,J.K. and Maluf,H.
  TITLE     DICER1-sarcomas of GYN tract: Expanding on an emerging entity
  JOURNAL   Hum Pathol 152, 105636 (2024)
   PUBMED   39127354
  REMARK    GeneRIF: DICER1-sarcomas of GYN tract: Expanding on an emerging
            entity.
REFERENCE   5  (residues 1 to 1922)
  AUTHORS   Irvin-Wilson,C.V. and Chaudhuri,G.
  TITLE     Alternative initiation and splicing in dicer gene expression in
            human breast cells
  JOURNAL   Breast Cancer Res 7 (4), R563-R569 (2005)
   PUBMED   15987463
REFERENCE   6  (residues 1 to 1922)
  AUTHORS   Bignell,G.R., Canzian,F., Shayeghi,M., Stark,M., Shugart,Y.Y.,
            Biggs,P., Mangion,J., Hamoudi,R., Rosenblatt,J., Buu,P., Sun,S.,
            Stoffer,S.S., Goldgar,D.E., Romeo,G., Houlston,R.S., Narod,S.A.,
            Stratton,M.R. and Foulkes,W.D.
  TITLE     Familial nontoxic multinodular thyroid goiter locus maps to
            chromosome 14q but does not account for familial nonmedullary
            thyroid cancer
  JOURNAL   Am J Hum Genet 61 (5), 1123-1130 (1997)
   PUBMED   9345104
REFERENCE   7  (residues 1 to 1922)
  AUTHORS   Schultz,K.A.P., Stewart,D.R., Kamihara,J., Bauer,A.J.,
            Merideth,M.A., Stratton,P., Huryn,L.A., Harris,A.K., Doros,L.,
            Field,A., Carr,A.G., Dehner,L.P., Messinger,Y. and Hill,D.A.
  TITLE     DICER1 Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24761742
REFERENCE   8  (residues 1 to 1922)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   9  (residues 1 to 1922)
  AUTHORS   Couch,R.M., Hughes,I.A., DeSa,D.J., Schiffrin,A., Guyda,H. and
            Winter,J.S.
  TITLE     An autosomal dominant form of adolescent multinodular goiter
  JOURNAL   Am J Hum Genet 39 (6), 811-816 (1986)
   PUBMED   3799599
REFERENCE   10 (residues 1 to 1922)
  AUTHORS   Murray,I.P., Thomson,J.A., McGirr,E.M., Macdonald,E.M.,
            Kennedy,J.S. and McLennan,I.
  TITLE     Unusual familial goiter associated with intrathyroidal
            calcification
  JOURNAL   J Clin Endocrinol Metab 26 (10), 1039-1049 (1966)
   PUBMED   4162574
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AJ132261.2, AL390254.6 and
            AF007142.1.
            
            Summary: This gene encodes a protein possessing an RNA helicase
            motif containing a DEXH box in its amino terminus and an RNA motif
            in the carboxy terminus. The encoded protein functions as a
            ribonuclease and is required by the RNA interference and small
            temporal RNA (stRNA) pathways to produce the active small RNA
            component that represses gene expression. This protein also acts as
            a strong antiviral agent with activity against RNA viruses,
            including the Zika and SARS-CoV-2 viruses. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jul
            2021].
            
            Transcript Variant: This variant (4) differs in the 5' UTR,
            compared to variant 2. Variants 1, 2, 4 and 5 encode the same
            isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ132261.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1922
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.13"
     Protein         1..1922
                     /product="endoribonuclease Dicer isoform 1"
                     /EC_number="3.1.26.3"
                     /note="dicer 1, double-stranded RNA-specific
                     endoribonuclease; helicase with RNAse motif;
                     endoribonuclease Dicer; helicase MOI; Dicer1, Dcr-1
                     homolog; dicer 1, ribonuclease type III"
                     /calculated_mol_wt=218552
     Region          42..239
                     /region_name="DEXHc_dicer"
                     /note="DEXH-box helicase domain of endoribonuclease Dicer;
                     cd18034"
                     /db_xref="CDD:350792"
     Site            order(42..45,48,65..72,113,176,207)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350792"
     Site            order(101..102,125..126,151,153..154,157,182..184)
                     /site_type="other"
                     /note="nucleic acid binding site [nucleotide binding]"
                     /db_xref="CDD:350792"
     Region          175..178
                     /region_name="DECH box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Region          256..595
                     /region_name="Required for interaction with PRKRA and
                     TARBP2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Region          271..365
                     /region_name="Dicer_PBD"
                     /note="Partner-binding domain of the endoribonuclease
                     Dicer; cd15903"
                     /db_xref="CDD:277191"
     Site            order(276..277,280,282..283,342..343,346..347,350,
                     353..354,357)
                     /site_type="other"
                     /note="Trbp binding interface [polypeptide binding]"
                     /db_xref="CDD:277191"
     Region          372..564
                     /region_name="SF2_C_dicer"
                     /note="C-terminal helicase domain of the endoribonuclease
                     Dicer; cd18802"
                     /db_xref="CDD:350189"
     Region          409..433
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            order(449..451,521,540,542)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350189"
     Site            order(525,527,552,554)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350189"
     Region          630..718
                     /region_name="Dicer_dimer"
                     /note="Dicer dimerization domain; pfam03368"
                     /db_xref="CDD:460900"
     Region          886..1008
                     /region_name="PAZ_dicer_like"
                     /note="PAZ domain, dicer_like subfamily. Dicer is an RNAse
                     involved in cleaving dsRNA in the RNA interference
                     pathway. It generates dsRNAs which are approximately 20 bp
                     long (siRNAs), which in turn target hydrolysis of
                     homologous RNAs. PAZ domains are named...; cd02843"
                     /db_xref="CDD:239209"
     Site            order(949,962,968,972,990,998,1000)
                     /site_type="other"
                     /note="nucleic acid-binding interface [nucleotide
                     binding]"
                     /db_xref="CDD:239209"
     Site            1016
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            1160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Region          1296..>1387
                     /region_name="RIBOc"
                     /note="Ribonuclease III family; smart00535"
                     /db_xref="CDD:197778"
     Site            order(1313..1314,1317..1318,1321,1324..1325,1328..1329,
                     1331..1333,1343)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238333"
     Site            1460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            1468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R418; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            1470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Region          1682..1846
                     /region_name="RIBOc"
                     /note="Ribonuclease III C terminal domain. This group
                     consists of eukaryotic, bacterial and archeal ribonuclease
                     III (RNAse III) proteins. RNAse III is a double stranded
                     RNA-specific endonuclease. Prokaryotic RNAse III is
                     important in post-transcriptional...; cd00593"
                     /db_xref="CDD:238333"
     Site            order(1702..1703,1706..1707,1710,1713..1714,1717..1718,
                     1720..1722,1732,1820,1831)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238333"
     Site            order(1702,1705,1709,1810,1813)
                     /site_type="active"
                     /db_xref="CDD:238333"
     Site            order(1705,1810,1813)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:238333"
     Site            1806
                     /site_type="other"
                     /note="Important for activity.
                     /evidence=ECO:0000250|UniProtKB:Q8R418; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Region          1851..1913
                     /region_name="DSRM_DICER"
                     /note="double-stranded RNA binding motif of
                     endoribonuclease Dicer and similar proteins; cd10843"
                     /db_xref="CDD:380680"
     Site            order(1851..1852,1854..1855,1858..1859,1862..1863,1867,
                     1872..1874,1876,1878,1895..1898,1901)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:380680"
     Site            1868
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     CDS             1..1922
                     /gene="DICER1"
                     /gene_synonym="aviD; DCR1; Dicer; Dicer1e; GLOW; HERNA;
                     K12H4.8-LIKE; MNG1; RMSE2"
                     /coded_by="NM_001271282.3:225..5993"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS9931.1"
                     /db_xref="GeneID:23405"
                     /db_xref="HGNC:HGNC:17098"
                     /db_xref="MIM:606241"
ORIGIN      
        1 mkspalqpls maglqlmtpa sspmgpffgl pwqqeaihdn iytprkyqve lleaaldhnt
       61 ivclntgsgk tfiavlltke lsyqirgdfs rngkrtvflv nsanqvaqqv savrthsdlk
      121 vgeysnlevn aswtkerwnq eftkhqvlim tcyvalnvlk ngylslsdin llvfdechla
      181 ildhpyreim klcencpscp rilgltasil ngkcdpeele ekiqklekil ksnaetatdl
      241 vvldrytsqp ceivvdcgpf tdrsglyerl lmeleealnf indcnisvhs kerdstlisk
      301 qilsdcravl vvlgpwcadk vagmmvrelq kyikheqeel hrkfllftdt flrkihalce
      361 ehfspasldl kfvtpkvikl leilrkykpy erqqfesvew ynnrnqdnyv swsdseddde
      421 deeieekekp etnfpspftn ilcgiifver rytavvlnrl ikeagkqdpe layissnfit
      481 ghgigknqpr nkqmeaefrk qeevlrkfra hetnlliats iveegvdipk cnlvvrfdlp
      541 teyrsyvqsk grarapisny imladtdkik sfeedlktyk aiekilrnkc sksvdtgetd
      601 idpvmddddv fppyvlrpdd ggprvtinta ighinrycar lpsdpfthla pkcrtrelpd
      661 gtfystlylp insplrasiv gppmscvrla ervvalicce klhkigeldd hlmpvgketv
      721 kyeeeldlhd eeetsvpgrp gstkrrqcyp kaipeclrds yprpdqpcyl yvigmvlttp
      781 lpdelnfrrr klyppedttr cfgiltakpi pqiphfpvyt rsgevtisie lkksgfmlsl
      841 qmlelitrlh qyifshilrl ekpalefkpt dadsaycvlp lnvvndsstl didfkfmedi
      901 eksearigip stkytketpf vfkledyqda viipryrnfd qphrfyvadv ytdltplskf
      961 pspeyetfae yyktkynldl tnlnqplldv dhtssrlnll tprhlnqkgk alplssaekr
     1021 kakweslqnk qilvpelcai hpipaslwrk avclpsilyr lhclltaeel raqtasdagv
     1081 gvrslpadfr ypnldfgwkk sidsksfisi snsssaendn yckhstivpe naahqganrt
     1141 sslenhdqms vncrtllses pgklhvevsa dltainglsy nqnlangsyd lanrdfcqgn
     1201 qlnyykqeip vqpttsysiq nlysyenqpq psdectllsn kyldgnanks tsdgspvmav
     1261 mpgttdtiqv lkgrmdseqs psigyssrtl gpnpglilqa ltlsnasdgf nlerlemlgd
     1321 sflkhaitty lfctypdahe grlsymrskk vsncnlyrlg kkkglpsrmv vsifdppvnw
     1381 lppgyvvnqd ksntdkwekd emtkdcmlan gkldedyeee deeeeslmwr apkeeadyed
     1441 dfleydqehi rfidnmlmgs gafvkkisls pfsttdsaye wkmpkksslg smpfssdfed
     1501 fdysswdamc yldpskavee ddfvvgfwnp seencgvdtg kqsisydlht eqciadksia
     1561 dcveallgcy ltscgeraaq lflcslglkv lpvikrtdre kalcptrenf nsqqknlsvs
     1621 caaasvassr ssvlkdseyg clkipprcmf dhpdadktln hlisgfenfe kkinyrfknk
     1681 ayllqaftha syhyntitdc yqrleflgda ildylitkhl yedprqhspg vltdlrsalv
     1741 nntifaslav kydyhkyfka vspelfhvid dfvqfqlekn emqgmdselr rseedeekee
     1801 dievpkamgd ifeslagaiy mdsgmsletv wqvyypmmrp liekfsanvp rspvrellem
     1861 epetakfspa ertydgkvrv tvevvgkgkf kgvgrsyria ksaaarralr slkanqpqvp
     1921 ns
//
LOCUS       NP_001337393             908 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 1 isoform 58 [Homo
            sapiens].
ACCESSION   NP_001337393
VERSION     NP_001337393.1
DBSOURCE    REFSEQ: accession NM_001350464.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 908)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 908)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 908)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 908)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 908)
  AUTHORS   Ruhle,F., Witten,A., Barysenka,A., Huge,A., Arning,A., Heller,C.,
            Krumpel,A., Mesters,R., Franke,A., Lieb,W., Riemenschneider,M.,
            Hiersche,M., Limperger,V., Nowak-Gottl,U. and Stoll,M.
  TITLE     Rare genetic variants in SMAP1, B3GAT2, and RIMS1 contribute to
            pediatric venous thromboembolism
  JOURNAL   Blood 129 (6), 783-790 (2017)
   PUBMED   28011674
  REMARK    GeneRIF: The study identified a region on chromosome 6 comprising
            the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus
            for pediatric venous thromboembolism.
REFERENCE   6  (residues 1 to 908)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 908)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
REFERENCE   8  (residues 1 to 908)
  AUTHORS   Schoch,S., Castillo,P.E., Jo,T., Mukherjee,K., Geppert,M., Wang,Y.,
            Schmitz,F., Malenka,R.C. and Sudhof,T.C.
  TITLE     RIM1alpha forms a protein scaffold for regulating neurotransmitter
            release at the active zone
  JOURNAL   Nature 415 (6869), 321-326 (2002)
   PUBMED   11797009
REFERENCE   9  (residues 1 to 908)
  AUTHORS   Coppola,T., Magnin-Luthi,S., Perret-Menoud,V., Gattesco,S.,
            Schiavo,G. and Regazzi,R.
  TITLE     Direct interaction of the Rab3 effector RIM with Ca2+ channels,
            SNAP-25, and synaptotagmin
  JOURNAL   J Biol Chem 276 (35), 32756-32762 (2001)
   PUBMED   11438518
REFERENCE   10 (residues 1 to 908)
  AUTHORS   Betz,A., Thakur,P., Junge,H.J., Ashery,U., Rhee,J.S., Scheuss,V.,
            Rosenmund,C., Rettig,J. and Brose,N.
  TITLE     Functional interaction of the active zone proteins Munc13-1 and
            RIM1 in synaptic vesicle priming
  JOURNAL   Neuron 30 (1), 183-196 (2001)
   PUBMED   11343654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590011.5, AL445256.18 and
            AL035633.18.
            
            Summary: The protein encoded by this gene is a RAS gene superfamily
            member that regulates synaptic vesicle exocytosis. This gene also
            plays a role in the regulation of voltage-gated calcium channels
            during neurotransmitter and insulin release. Mutations have
            suggested a role cognition and have been identified as the cause of
            cone-rod dystrophy type 7. Multiple transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Mar 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.44568.1,
                                           SRR1803617.4879.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..908
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..908
                     /product="regulating synaptic membrane exocytosis protein
                     1 isoform 58"
                     /note="RAB3-interacting protein 2; rab3-interacting
                     molecule 1; rab-3-interacting protein 2"
                     /calculated_mol_wt=101126
     Region          1..83
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(8..14,29,32,62,66,69..70)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          135..261
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(166,172,227,229,237)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          739..884
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(796,800..801,803,806,834,836,838,882..883)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..908
                     /gene="RIMS1"
                     /gene_synonym="CORD7; RAB3IP2; RIM; RIM1"
                     /coded_by="NM_001350464.2:262..2988"
                     /note="isoform 58 is encoded by transcript variant 58"
                     /db_xref="GeneID:22999"
                     /db_xref="HGNC:HGNC:17282"
                     /db_xref="MIM:606629"
ORIGIN      
        1 mpkdsgallg lkvvggkmtd lgrlgafitk vkkgsladvv ghlragdevl ewngkplpga
       61 tneevyniil esksepqvei ivsrpigdip ripesshppl esssssfesq kmerpsisvi
      121 sptspgalkd apqvlpgqls vklwydkvgh qlivnvlqat dlparvdgrp rnpyvkmyfl
      181 pdrsdkskrr tktvkkilep kwnqtfvysh vhrrdfrerm leitvwdqpr vqeeeseflg
      241 eilieletal lddephwykl qthdesslpl pqpspfmprr hihgessskk lqrsqrisds
      301 disdyevddg igvvppvgyr ssareskstt ltvpeqqrtt hhrsrsvsph rgndqgkprs
      361 rlpnvplqrs ldeihptrrs rsptrhhdas rspvdhrtrd vdsqylseqd sellmlprak
      421 rgrsaeclht tselqpfldr arsastnclr pdtslhsper ermhrqrspt qsppadtsfs
      481 srrgrqlpqv pvrsgsieqa slvveertrq mkmkvhrfkq ttgsgssqel dreqyskyni
      541 hkdqyrscdn vsakssdsdv sdvsaisrts sasrlsstsf mseqserprg rissftpkmq
      601 grrmgtsgrs imkstsvsge mytlehndgs qsdtavgtvg aggkkrrssl sakvvaivsr
      661 rsrstsqlsq tesghkklks tiqrstetgm aaemrkmvrq psrestdgsi nsyssegnli
      721 fpgvrlgads qfsdfldglg paqlvgrqtl atpamgdiqi gmedkkgqle vevirarslt
      781 qkpgskstpa pyvkvyllen gaciakkktr iarktldply qqslvfdesp qgkvlqvivw
      841 gdygrmdhkc fmgvaqille eldlssmvig wyklfppssl vdptltpltr rasqssless
      901 tgppcirs
//
LOCUS       NP_001340521             550 aa            linear   PRI 21-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform e [Homo sapiens].
ACCESSION   NP_001340521 XP_016877022
VERSION     NP_001340521.1
DBSOURCE    REFSEQ: accession NM_001353592.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 550)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 550)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 550)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 550)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            On Jul 19, 2017 this sequence version replaced XP_016877022.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.201375.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..550
                     /product="lysosomal cobalamin transporter ABCD4 isoform e"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=62175
     Region          68..542
                     /region_name="YddA"
                     /note="ABC-type uncharacterized transport system, permease
                     and ATPase components [General function prediction only];
                     COG4178"
                     /db_xref="CDD:443337"
     CDS             1..550
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_001353592.2:23..1675"
                     /note="isoform e is encoded by transcript variant 7"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 mavagpapga garprldlqf lqrflqilkv lfpswssqna lmfltllclt lleqfviyqv
       61 glipsqyygv lgnkdlegfk tltflavmli vlnstlksfd qftcnllyvs wrkdltehlh
      121 rlyfrgrayy tlnvlrddid npdqrisqdv erfcrqlssm askliispft lvyytyqcfq
      181 rfkhmqirvn aepaafyrag hvehmrtdrr lqrllqtqre lmskelwlyi gintfdylgs
      241 ilsyvviaip ifsgvygdls paelstlvsk nafvciylis cftqlidlst tlsdvagyth
      301 rigqlretll dmslksqdce ilgesewgld tppgwpaaep adtafllerv sisapssdkp
      361 likdlslkis egqsllitgn tgtgktsllr vlgglwtstr gsvqmltdfg phgvlflpqk
      421 pfftdgtlre qviyplkevy pdsgsadder ilrflelagl snlvartegl dqqvdwnwyd
      481 vlspgemqrl sfarlfylqp kyavldeats alteevesel yrigqqlgmt fisvghrqsl
      541 ekvpvltrma
//
LOCUS       NP_059145                986 aa            linear   PRI 21-NOV-2025
DEFINITION  ephrin type-B receptor 2 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_059145
VERSION     NP_059145.2
DBSOURCE    REFSEQ: accession NM_017449.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 986)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 986)
  AUTHORS   Overman,R.C., Debreczeni,J.E., Truman,C.M., McAlister,M.S. and
            Attwood,T.K.
  TITLE     Completing the structural family portrait of the human EphB
            tyrosine kinase domains
  JOURNAL   Protein Sci 23 (5), 627-638 (2014)
   PUBMED   24677421
  REMARK    GeneRIF: Comparative crystalisation analysis of the human EphB
            family kinases has yielded new crystal forms of the human EphB2 and
            EphB4 catalytic domains.
REFERENCE   3  (residues 1 to 986)
  AUTHORS   Badzioch,M., Eeles,R., Leblanc,G., Foulkes,W.D., Giles,G.,
            Edwards,S., Goldgar,D., Hopper,J.L., Bishop,D.T., Moller,P.,
            Heimdal,K., Easton,D. and Simard,J.
  TITLE     Suggestive evidence for a site specific prostate cancer gene on
            chromosome 1p36. The CRC/BPG UK Familial Prostate Cancer Study
            Coordinators and Collaborators. The EU Biomed Collaborators
  JOURNAL   J Med Genet 37 (12), 947-949 (2000)
   PUBMED   11186936
REFERENCE   4  (residues 1 to 986)
  AUTHORS   Gibbs,M., Stanford,J.L., McIndoe,R.A., Jarvik,G.P., Kolb,S.,
            Goode,E.L., Chakrabarti,L., Schuster,E.F., Buckley,V.A.,
            Miller,E.L., Brandzel,S., Li,S., Hood,L. and Ostrander,E.A.
  TITLE     Evidence for a rare prostate cancer-susceptibility locus at
            chromosome 1p36
  JOURNAL   Am J Hum Genet 64 (3), 776-787 (1999)
   PUBMED   10053012
REFERENCE   5  (residues 1 to 986)
  AUTHORS   Tang,X.X., Pleasure,D.E., Brodeur,G.M. and Ikegaki,N.
  TITLE     A variant transcript encoding an isoform of the human protein
            tyrosine kinase EPHB2 is generated by alternative splicing and
            alternative use of polyadenylation signals
  JOURNAL   Oncogene 17 (4), 521-526 (1998)
   PUBMED   9696046
REFERENCE   6  (residues 1 to 986)
  AUTHORS   Saito,T., Seki,N., Matsuda,Y., Kitahara,M., Murata,M., Kanda,N.,
            Nomura,N., Yamamoto,T. and Hori,T.A.
  TITLE     Identification of the human ERK gene as a putative receptor
            tyrosine kinase and its chromosomal localization to 1p36.1: a
            comparative mapping of human, mouse, and rat chromosomes
  JOURNAL   Genomics 26 (2), 382-384 (1995)
   PUBMED   7601466
REFERENCE   7  (residues 1 to 986)
  AUTHORS   Fox,G.M., Holst,P.L., Chute,H.T., Lindberg,R.A., Janssen,A.M.,
            Basu,R. and Welcher,A.A.
  TITLE     cDNA cloning and tissue distribution of five human EPH-like
            receptor protein-tyrosine kinases
  JOURNAL   Oncogene 10 (5), 897-905 (1995)
   PUBMED   7898931
REFERENCE   8  (residues 1 to 986)
  AUTHORS   Kiyokawa,E., Takai,S., Tanaka,M., Iwase,T., Suzuki,M., Xiang,Y.Y.,
            Naito,Y., Yamada,K., Sugimura,H. and Kino,I.
  TITLE     Overexpression of ERK, an EPH family receptor protein tyrosine
            kinase, in various human tumors
  JOURNAL   Cancer Res 54 (14), 3645-3650 (1994)
   PUBMED   8033077
REFERENCE   9  (residues 1 to 986)
  AUTHORS   Iwase,T., Tanaka,M., Suzuki,M., Naito,Y., Sugimura,H. and Kino,I.
  TITLE     Identification of protein-tyrosine kinase genes preferentially
            expressed in embryo stomach and gastric cancer
  JOURNAL   Biochem Biophys Res Commun 194 (2), 698-705 (1993)
   PUBMED   7688222
REFERENCE   10 (residues 1 to 986)
  AUTHORS   Chan,J. and Watt,V.M.
  TITLE     eek and erk, new members of the eph subclass of receptor
            protein-tyrosine kinases
  JOURNAL   Oncogene 6 (6), 1057-1061 (1991)
   PUBMED   1648701
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158086.32, AL512444.20 and
            AL035704.9.
            
            On Aug 2, 2006 this sequence version replaced NP_059145.1.
            
            Summary: This gene encodes a member of the Eph receptor family of
            receptor tyrosine kinase transmembrane glycoproteins. These
            receptors are composed of an N-terminal glycosylated ligand-binding
            domain, a transmembrane region and an intracellular kinase domain.
            They bind ligands called ephrins and are involved in diverse
            cellular processes including motility, division, and
            differentiation. A distinguishing characteristic of Eph-ephrin
            signaling is that both receptors and ligands are competent to
            transduce a signaling cascade, resulting in bidirectional
            signaling. This protein belongs to a subgroup of the Eph receptors
            called EphB. Proteins of this subgroup are distinguished from other
            members of the family by sequence homology and preferential binding
            affinity for membrane-bound ephrin-B ligands. Allelic variants are
            associated with prostate and brain cancer susceptibility.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, May 2015].
            
            Transcript Variant: This variant (1) uses an alternate in-frame
            splice site compared to variant 2. It encodes isoform 1, which is
            shorter than isoform 2.
            
            CCDS Note: The coding region has been updated to represent an
            alternative 3' splice pattern, resulting in a shorter and distinct
            C-terminus that is better supported by available transcript and
            homology data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB210018.1, SRR11853558.414.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374630.8/ ENSP00000363761.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..986
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     Protein         1..986
                     /product="ephrin type-B receptor 2 isoform 1 precursor"
                     /EC_number="2.7.10.1"
                     /note="elk-related tyrosine kinase; ephrin type-B receptor
                     2; protein-tyrosine kinase HEK5; eph tyrosine kinase 3;
                     EPH-like kinase 5; tyrosine-protein kinase TYRO5; renal
                     carcinoma antigen NY-REN-47; tyrosine-protein kinase
                     receptor EPH-3; developmentally-regulated Eph-related
                     tyrosine kinase"
                     /calculated_mol_wt=107313
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2579
     Region          19..196
                     /region_name="EphR_LBD_B2"
                     /note="Ligand Binding Domain of Ephrin type-B Receptor 2;
                     cd10477"
                     /db_xref="CDD:198445"
     Site            order(28..30,32,44..47,49,53,55,57,60,93..95,99,101,147,
                     149..156,158..159,184,186,188)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198445"
     Site            265
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29323.5)"
     Site            order(325,400,415)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          326..421
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            336
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29323.5)"
     Site            order(416,418,420..421)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            428
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29323.5)"
     Site            order(436,500,515)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          437..520
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            482
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29323.5)"
     Site            order(516..517,519..520)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            535..536
                     /site_type="cleavage"
                     /note="Cleavage, by a metalloproteinase.
                     /evidence=ECO:0000250|UniProtKB:P54763; propagated from
                     UniProtKB/Swiss-Prot (P29323.5)"
     Region          544..617
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Site            544..564
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29323.5)"
     Site            561..562
                     /site_type="cleavage"
                     /note="Cleavage, by gamma-secretase/PS1.
                     /evidence=ECO:0000250|UniProtKB:P54763; propagated from
                     UniProtKB/Swiss-Prot (P29323.5)"
     Region          616..884
                     /region_name="PTKc_EphR_B"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphB Ephrin Receptors; cd05065"
                     /db_xref="CDD:173638"
     Site            order(627..631,635,651,653,699..700,702,706,746,750..751,
                     753,764,785..789,798,832)
                     /site_type="active"
                     /db_xref="CDD:173638"
     Site            order(627..629,631,635,651,653,699..700,702,706,751,753,
                     764)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173638"
     Site            order(746,750,785..789,798,832)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173638"
     Site            763..791
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173638"
     Region          910..980
                     /region_name="SAM_EPH-B2"
                     /note="SAM domain of EPH-B2 subfamily of tyrosine kinase
                     receptors; cd09552"
                     /db_xref="CDD:188951"
     Site            order(912..913,915,937,943..944,952,960..963,965..966,974,
                     978)
                     /site_type="other"
                     /note="homooligomer interface [polypeptide binding]"
                     /db_xref="CDD:188951"
     Site            order(912,915,921,942,970,973..974)
                     /site_type="other"
                     /note="putative homodimer interface (head-to-head)
                     [polypeptide binding]"
                     /db_xref="CDD:188951"
     Site            order(930,963)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188951"
     Site            order(946..951,954,972,975,978..979)
                     /site_type="other"
                     /note="homodimer interface (tail-to-tail) [polypeptide
                     binding]"
                     /db_xref="CDD:188951"
     Site            983
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P29323.5)"
     Site            984
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P29323.5)"
     CDS             1..986
                     /gene="EPHB2"
                     /gene_synonym="BDPLT22; CAPB; DRT; EK5; EPHT3; ERK; Hek5;
                     PCBC; Tyro5"
                     /coded_by="NM_017449.5:145..3105"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS229.2"
                     /db_xref="GeneID:2048"
                     /db_xref="HGNC:HGNC:3393"
                     /db_xref="MIM:600997"
ORIGIN      
        1 malrrlgaal lllpllaave etlmdsttat aelgwmvhpp sgweevsgyd enmntirtyq
       61 vcnvfessqn nwlrtkfirr rgahrihvem kfsvrdcssi psvpgscket fnlyyyeadf
      121 dsatktfpnw menpwvkvdt iaadesfsqv dlggrvmkin tevrsfgpvs rsgfylafqd
      181 yggcmsliav rvfyrkcpri iqngaifqet lsgaestslv aargsciana eevdvpikly
      241 cngdgewlvp igrcmckagf eavengtvcr gcpsgtfkan qgdeacthcp insrttsega
      301 tncvcrngyy radldpldmp cttipsapqa vissvnetsl mlewtpprds ggredlvyni
      361 ickscgsgrg actrcgdnvq yaprqlglte priyisdlla htqytfeiqa vngvtdqspf
      421 spqfasvnit tnqaapsavs imhqvsrtvd sitlswsqpd qpngvildye lqyyekelse
      481 ynataikspt ntvtvqglka gaiyvfqvra rtvagygrys gkmyfqtmte aeyqtsiqek
      541 lpliigssaa glvfliavvv iaivcnrrgf eradseytdk lqhytsghmt pgmkiyidpf
      601 tyedpneavr efakeidisc vkieqvigag efgevcsghl klpgkreifv aiktlksgyt
      661 ekqrrdflse asimgqfdhp nvihlegvvt kstpvmiite fmengsldsf lrqndgqftv
      721 iqlvgmlrgi aagmkyladm nyvhrdlaar nilvnsnlvc kvsdfglsrf leddtsdpty
      781 tsalggkipi rwtapeaiqy rkftsasdvw sygivmwevm sygerpywdm tnqdvinaie
      841 qdyrlpppmd cpsalhqlml dcwqkdrnhr pkfgqivntl dkmirnpnsl kamaplssgi
      901 nlplldrtip dytsfntvde wleaikmgqy kesfanagft sfdvvsqmmm edilrvgvtl
      961 aghqkkilns iqvmraqmnq iqsvev
//
LOCUS       NP_001386729             312 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc-regulated GTPase metalloprotein activator 1A isoform 8 [Homo
            sapiens].
ACCESSION   NP_001386729
VERSION     NP_001386729.1
DBSOURCE    REFSEQ: accession NM_001399800.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Weiss,A., Murdoch,C.C., Edmonds,K.A., Jordan,M.R., Monteith,A.J.,
            Perera,Y.R., Rodriguez Nassif,A.M., Petoletti,A.M., Beavers,W.N.,
            Munneke,M.J., Drury,S.L., Krystofiak,E.S., Thalluri,K., Wu,H.,
            Kruse,A.R.S., DiMarchi,R.D., Caprioli,R.M., Spraggins,J.M.,
            Chazin,W.J., Giedroc,D.P. and Skaar,E.P.
  TITLE     Zn-regulated GTPase metalloprotein activator 1 modulates vertebrate
            zinc homeostasis
  JOURNAL   Cell 185 (12), 2148-2163 (2022)
   PUBMED   35584702
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Kanda,S., Ohmuraya,M., Akagawa,H., Horita,S., Yoshida,Y.,
            Kaneko,N., Sugawara,N., Ishizuka,K., Miura,K., Harita,Y.,
            Yamamoto,T., Oka,A., Araki,K., Furukawa,T. and Hattori,M.
  TITLE     Deletion in the Cobalamin Synthetase W Domain-Containing Protein 1
            Gene Is associated with Congenital Anomalies of the Kidney and
            Urinary Tract
  JOURNAL   J Am Soc Nephrol 31 (1), 139-147 (2020)
   PUBMED   31862704
  REMARK    GeneRIF: The identification of a deletion in CBWD1 gene in two
            siblings with CAKUT implies a role for CBWD1 in the etiology of
            some cases of CAKUT
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Fan,Y., Newman,T., Linardopoulou,E. and Trask,B.J.
  TITLE     Gene content and function of the ancestral chromosome fusion site
            in human chromosome 2q13-2q14.1 and paralogous regions
  JOURNAL   Genome Res 12 (11), 1663-1672 (2002)
   PUBMED   12421752
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Shi,J., Cai,W., Chen,X., Ying,K., Zhang,K. and Xie,Y.
  TITLE     Identification of dopamine responsive mRNAs in glial cells by
            suppression subtractive hybridization
  JOURNAL   Brain Res 910 (1-2), 29-37 (2001)
   PUBMED   11489251
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Page,N., Butlin,D., Manyonda,I. and Lowry,P.
  TITLE     The development of a genetic profile of placental gene expression
            during the first trimester of pregnancy: a potential tool for
            identifying novel secreted markers
  JOURNAL   Fetal Diagn Ther 15 (4), 237-245 (2000)
   PUBMED   10867487
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL356244.13 and AL449043.16.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.3"
     Protein         1..312
                     /product="zinc-regulated GTPase metalloprotein activator
                     1A isoform 8"
                     /note="COBW-like protein; COBW domain-containing protein
                     1; NPC-A-6 COBW domain-containing protein 1; cobalamin
                     synthetase W domain-containing protein 1; zinc-regulated
                     GTPase metalloprotein activator 1A; COBW domain containing
                     1; cobalamin synthase W domain-containing protein 1"
                     /calculated_mol_wt=34921
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRT8.1)"
     Region          17..24
                     /region_name="psi-PxLVp motif.
                     /evidence=ECO:0000250|UniProtKB:Q8VEH6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRT8.1)"
     Region          40..290
                     /region_name="YejR"
                     /note="Zinc metallochaperone YeiR/ZagA and related
                     GTPases, G3E family [General function prediction only];
                     COG0523"
                     /db_xref="CDD:440289"
     CDS             1..312
                     /gene="ZNG1A"
                     /gene_synonym="CBWD1; COBP"
                     /coded_by="NM_001399800.1:88..1026"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:55871"
                     /db_xref="HGNC:HGNC:17134"
                     /db_xref="MIM:611078"
ORIGIN      
        1 mlpavgsade eedpaeedcp elvpiettqs eeeeksglga kipvtiitgy lgagkttlln
       61 yilteqhskr vavilnefge giitivdsky glkhlteekp dglineatrq valadailin
      121 ktdlvpeedv kklrttirsi nglgqiletq rsrvdlsnvl dlhafdslsg islqkklqhv
      181 pgtqphldqs ivtitfevpg nakeehlnmf iqnllweknv rnkdnhcmev irlkglvsik
      241 dksqqvivqg vhelydleet pvswkddter tnrlvllgrn ldkdilkqlf iatvtetekq
      301 wttrfqedqv ct
//
LOCUS       NP_008960                179 aa            linear   PRI 21-NOV-2025
DEFINITION  stathmin-2 isoform 2 [Homo sapiens].
ACCESSION   NP_008960
VERSION     NP_008960.2
DBSOURCE    REFSEQ: accession NM_007029.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Agra Almeida Quadros,A.R., Li,Z., Wang,X., Ndayambaje,I.S.,
            Aryal,S., Ramesh,N., Nolan,M., Jayakumar,R., Han,Y., Stillman,H.,
            Aguilar,C., Wheeler,H.J., Connors,T., Lopez-Erauskin,J.,
            Baughn,M.W., Melamed,Z., Beccari,M.S., Olmedo Martinez,L.,
            Canori,M., Lee,C.Z., Moran,L., Draper,I., Kopin,A.S., Oakley,D.H.,
            Dickson,D.W., Cleveland,D.W., Hyman,B.T., Das,S., Ertekin-Taner,N.
            and Lagier-Tourenne,C.
  TITLE     Cryptic splicing of stathmin-2 and UNC13A mRNAs is a pathological
            hallmark of TDP-43-associated Alzheimer's disease
  JOURNAL   Acta Neuropathol 147 (1), 9 (2024)
   PUBMED   38175301
  REMARK    GeneRIF: Cryptic splicing of stathmin-2 and UNC13A mRNAs is a
            pathological hallmark of TDP-43-associated Alzheimer's disease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Wood,H.
  TITLE     TDP43 blocks misprocessing of STMN2 RNA
  JOURNAL   Nat Rev Neurol 19 (6), 326 (2023)
   PUBMED   37012364
  REMARK    GeneRIF: TDP43 blocks misprocessing of STMN2 RNA.
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Shao,M., Wang,L., Zhang,Q., Wang,T. and Wang,S.
  TITLE     STMN2 overexpression promotes cell proliferation and EMT in
            pancreatic cancer mediated by WNT/beta-catenin signaling
  JOURNAL   Cancer Gene Ther 30 (3), 472-480 (2023)
   PUBMED   36460804
  REMARK    GeneRIF: STMN2 overexpression promotes cell proliferation and EMT
            in pancreatic cancer mediated by WNT/beta-catenin signaling.
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Doronzio,P.N., Lattante,S., Marangi,G., Martello,F., Conte,A.,
            Bisogni,G., Bernardo,D., Patanella,A.K., Meleo,E., Zollino,M. and
            Sabatelli,M.
  TITLE     Analysis of STMN2 CA repeats in italian ALS patients shows no
            association
  JOURNAL   Amyotroph Lateral Scler Frontotemporal Degener 24 (1-2), 152-154
            (2023)
   PUBMED   35876065
  REMARK    GeneRIF: Analysis of STMN2 CA repeats in italian ALS patients shows
            no association.
REFERENCE   6  (residues 1 to 179)
  AUTHORS   Antonsson,B., Kassel,D.B., Di Paolo,G., Lutjens,R., Riederer,B.M.
            and Grenningloh,G.
  TITLE     Identification of in vitro phosphorylation sites in the growth cone
            protein SCG10. Effect Of phosphorylation site mutants on
            microtubule-destabilizing activity
  JOURNAL   J Biol Chem 273 (14), 8439-8446 (1998)
   PUBMED   9525956
REFERENCE   7  (residues 1 to 179)
  AUTHORS   Antonsson,B., Lutjens,R., Di Paolo,G., Kassel,D., Allet,B.,
            Bernard,A., Catsicas,S. and Grenningloh,G.
  TITLE     Purification, characterization, and in vitro phosphorylation of the
            neuron-specific membrane-associated protein SCG10
  JOURNAL   Protein Expr Purif 9 (3), 363-371 (1997)
   PUBMED   9126608
REFERENCE   8  (residues 1 to 179)
  AUTHORS   Di Paolo,G., Lutjens,R., Pellier,V., Stimpson,S.A., Beuchat,M.H.,
            Catsicas,S. and Grenningloh,G.
  TITLE     Targeting of SCG10 to the area of the Golgi complex is mediated by
            its NH2-terminal region
  JOURNAL   J Biol Chem 272 (8), 5175-5182 (1997)
   PUBMED   9030585
REFERENCE   9  (residues 1 to 179)
  AUTHORS   Okazaki,T., Wang,H., Masliah,E., Cao,M., Johnson,S.A., Sundsmo,M.,
            Saitoh,T. and Mori,N.
  TITLE     SCG10, a neuron-specific growth-associated protein in Alzheimer's
            disease
  JOURNAL   Neurobiol Aging 16 (6), 883-894 (1995)
   PUBMED   8622778
REFERENCE   10 (residues 1 to 179)
  AUTHORS   Schoenherr,C.J. and Anderson,D.J.
  TITLE     The neuron-restrictive silencer factor (NRSF): a coordinate
            repressor of multiple neuron-specific genes
  JOURNAL   Science 267 (5202), 1360-1363 (1995)
   PUBMED   7871435
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC319376.1, AC025599.8 and
            AC016240.23.
            
            On Sep 18, 2003 this sequence version replaced NP_008960.1.
            
            Summary: This gene encodes a member of the stathmin family of
            phosphoproteins. Stathmin proteins function in microtubule dynamics
            and signal transduction. The encoded protein plays a regulatory
            role in neuronal growth and is also thought to be involved in
            osteogenesis. Reductions in the expression of this gene have been
            associated with Down's syndrome and Alzheimer's disease.
            Alternatively spliced transcript variants have been observed for
            this gene. A pseudogene of this gene is located on the long arm of
            chromosome 6. [provided by RefSeq, Nov 2010].
            
            Transcript Variant: This variant (2) lacks an alternate exon, which
            results in a frameshift in the 3' coding region, compared to
            variant 1. The encoded isoform (2) is shorter and has a distinct
            C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.13183.1,
                                           SRR5189652.248641.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000220876.12/ ENSP00000220876.7
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.13"
     Protein         1..179
                     /product="stathmin-2 isoform 2"
                     /note="neuronal growth-associated protein (silencer
                     element); stathmin-like 2; superior cervical ganglia,
                     neural specific 10; neuron-specific growth-associated
                     protein; superior cervical ganglion-10 protein"
                     /calculated_mol_wt=20697
     Region          1..26
                     /region_name="Membrane attachment. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93045.3)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q93045.3)"
     Region          38..173
                     /region_name="Stathmin"
                     /note="Stathmin family; pfam00836"
                     /db_xref="CDD:459956"
     Region          39..96
                     /region_name="Regulatory/phosphorylation domain.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93045.3)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55821, ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q93045.3)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q93045.3)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21818; propagated from
                     UniProtKB/Swiss-Prot (Q93045.3)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P16949, ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q93045.3)"
     CDS             1..179
                     /gene="STMN2"
                     /gene_synonym="SCG10; SCGN10"
                     /coded_by="NM_007029.4:80..619"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43748.1"
                     /db_xref="GeneID:11075"
                     /db_xref="HGNC:HGNC:10577"
                     /db_xref="MIM:600621"
ORIGIN      
        1 maktamayke kmkelsmlsl icscfypepr niniytyddm evkqinkras gqafelilkp
       61 pspiseaprt laspkkkdls leeiqkklea aeerrksqea qvlkqlaekr eherevlqka
      121 leennnfskm aeeklilkme qikenreanl aaiierlqek erhaaevrrn kelqvelsg
//
LOCUS       NP_001374932            1100 aa            linear   PRI 21-NOV-2025
DEFINITION  large proline-rich protein BAG6 isoform 16 [Homo sapiens].
ACCESSION   NP_001374932
VERSION     NP_001374932.1
DBSOURCE    REFSEQ: accession NM_001388003.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1100)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 1100)
  AUTHORS   Alashkar Alhamwe,B., Ponath,V., Alhamdan,F., Dorsam,B.,
            Landwehr,C., Linder,M., Pauck,K., Miethe,S., Garn,H.,
            Finkernagel,F., Brichkina,A., Lauth,M., Tiwari,D.K., Buchholz,M.,
            Bachurski,D., Elmshauser,S., Nist,A., Stiewe,T., Pogge von
            Strandmann,L., Szymanski,W., Beutgen,V., Graumann,J.,
            Teply-Szymanski,J., Keber,C., Denkert,C., Jacob,R., Preusser,C. and
            Pogge von Strandmann,E.
  TITLE     BAG6 restricts pancreatic cancer progression by suppressing the
            release of IL33-presenting extracellular vesicles and the
            activation of mast cells
  JOURNAL   Cell Mol Immunol 21 (8), 918-931 (2024)
   PUBMED   38942797
  REMARK    GeneRIF: BAG6 restricts pancreatic cancer progression by
            suppressing the release of IL33-presenting extracellular vesicles
            and the activation of mast cells.
REFERENCE   3  (residues 1 to 1100)
  AUTHORS   Liu,L., Wu,J., Yan,Y., Cheng,S., Yu,S. and Wang,Y.
  TITLE     DERL2 (derlin 2) stabilizes BAG6 (BAG cochaperone 6) in
            chemotherapy resistance of cholangiocarcinoma
  JOURNAL   J Physiol Biochem 80 (1), 81-97 (2024)
   PUBMED   37815698
  REMARK    GeneRIF: DERL2 (derlin 2) stabilizes BAG6 (BAG cochaperone 6) in
            chemotherapy resistance of cholangiocarcinoma.
REFERENCE   4  (residues 1 to 1100)
  AUTHORS   Roboti,P., Lawless,C. and High,S.
  TITLE     Mitochondrial antiviral-signalling protein is a client of the BAG6
            protein quality control complex
  JOURNAL   J Cell Sci 135 (9) (2022)
   PUBMED   35543156
  REMARK    GeneRIF: Mitochondrial antiviral-signalling protein is a client of
            the BAG6 protein quality control complex.
REFERENCE   5  (residues 1 to 1100)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1100)
  AUTHORS   Ozaki,T., Hanaoka,E., Naka,M., Nakagawara,A. and Sakiyama,S.
  TITLE     Cloning and characterization of rat BAT3 cDNA
  JOURNAL   DNA Cell Biol 18 (6), 503-512 (1999)
   PUBMED   10390159
REFERENCE   7  (residues 1 to 1100)
  AUTHORS   Cross,S.J., Tonks,S., Trowsdale,J. and Campbell,R.D.
  TITLE     Novel detection of restriction fragment length polymorphisms in the
            human major histocompatibility complex
  JOURNAL   Immunogenetics 34 (6), 376-384 (1991)
   PUBMED   1684176
REFERENCE   8  (residues 1 to 1100)
  AUTHORS   Banerji,J., Sands,J., Strominger,J.L. and Spies,T.
  TITLE     A gene pair from the human major histocompatibility complex encodes
            large proline-rich proteins with multiple repeated motifs and a
            single ubiquitin-like domain
  JOURNAL   Proc Natl Acad Sci U S A 87 (6), 2374-2378 (1990)
   PUBMED   2156268
REFERENCE   9  (residues 1 to 1100)
  AUTHORS   Spies,T., Bresnahan,M. and Strominger,J.L.
  TITLE     Human major histocompatibility complex contains a minimum of 19
            genes between the complement cluster and HLA-B
  JOURNAL   Proc Natl Acad Sci U S A 86 (22), 8955-8958 (1989)
   PUBMED   2813433
REFERENCE   10 (residues 1 to 1100)
  AUTHORS   Spies,T., Blanck,G., Bresnahan,M., Sands,J. and Strominger,J.L.
  TITLE     A new cluster of genes within the human major histocompatibility
            complex
  JOURNAL   Science 243 (4888), 214-217 (1989)
   PUBMED   2911734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL662801.7.
            
            Summary: This gene was first characterized as part of a cluster of
            genes located within the human major histocompatibility complex
            class III region. This gene encodes a nuclear protein that is
            cleaved by caspase 3 and is implicated in the control of apoptosis.
            In addition, the protein forms a complex with E1A binding protein
            p300 and is required for the acetylation of p53 in response to DNA
            damage. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1100
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..1100
                     /product="large proline-rich protein BAG6 isoform 16"
                     /note="scythe; large proline-rich protein BAT3; large
                     proline-rich protein BAG6; protein G3; HLA-B-associated
                     transcript 3; protein Scythe; BAG family molecular
                     chaperone regulator 6; BCL2 associated athanogene 6"
                     /calculated_mol_wt=116198
     Region          17..87
                     /region_name="Ubl_BAG6"
                     /note="ubiquitin-like (Ubl) domain found in
                     BCL2-associated athanogene 6 (BAG6) and similar proteins;
                     cd01809"
                     /db_xref="CDD:340507"
     Site            order(22..25,58,60,62..65,83..87)
                     /site_type="other"
                     /note="ZF interaction site [polypeptide binding]"
                     /db_xref="CDD:340507"
     Region          270..386
                     /region_name="BAG6"
                     /note="BCL2-associated athanogene 6; pfam12057"
                     /db_xref="CDD:463449"
     Region          <873..1064
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     CDS             1..1100
                     /gene="BAG6"
                     /gene_synonym="BAG-6; BAT3; D6S52E; G3"
                     /coded_by="NM_001388003.1:158..3460"
                     /note="isoform 16 is encoded by transcript variant 43"
                     /db_xref="CCDS:CCDS93881.1"
                     /db_xref="GeneID:7917"
                     /db_xref="HGNC:HGNC:13919"
                     /db_xref="MIM:142590"
ORIGIN      
        1 mepndststa veepdslevl vktldsqtrt fivgaqmnvk efkehiaasv sipsekqrli
       61 yqgrvlqddk klqeynvggk vihlverapp qthlpsgass gtgsasathg ggsppgtrgp
      121 gasvhdrnan syvmvgtfnl psdgsavdvh inmeqapiqs eprvrlvmaq hmirdiqtll
      181 srmecrggpq pqhsqpppqp pavtpepval ssqtsepves eapprepmea eeveerapaq
      241 npeltpgpap agptpapetn apnhpspaey vevlqelqrl esrlqpflqr yyevlgaaat
      301 tdynnnhegr eedqrlinlv geslrllgnt fvalsdlrcn lactpprhlh vvrpmshytt
      361 pmvlqqaaip iqinvgttvt mtgngtrppp tpnaeapppg pgqassvaps stnvessaeg
      421 apppgpappp atshprviri shqsvepvvm mhmniqgqqv pgfptaptrv viarptppqa
      481 rpshpggppv sgtlqgaglg tnaslaqmvs glvgqllmqp vlvaqgtpgm apppapatas
      541 asagttntat tagpapggpa qppptpqpsm adlqfsqllg nllgpagpga ggsgvaspti
      601 tvampgvpaf lqgmtdflqa tqtapppppp ppppppapeq qtmpppgsps ggagspgglg
      661 leslspefft svvqgvlssl lgslgarags sesiaafiqr lsgssnifep gadgalgffg
      721 allsllcqnf smvdvvmllh ghfqplqrlq pqlrsffhqh ylggqeptps nirmathtli
      781 tgleeyvres fslvqvqpgv diirtnlefl qeqfnsiaah vlhctdsgfg arllelcnqg
      841 lfeclalnlh clggqqmela avingrirrm srgvnpslvs wlttmmglrl qvvlehmpvg
      901 pdailryvrr vgdppqplpe epmevqgaer aspepqrena spapgttaee amsrgpppap
      961 eggsrdeqdg asaetepwaa avppewvpii qqdiqsqrkv kpqpplsday lsgmpakrrk
     1021 tmqgegpqll lseavsraak aagarpltsp eslsrdleap evqesyrqql rsdiqkrlqe
     1081 dpnyspqrfp naqrafaddp
//
LOCUS       NP_004008                604 aa            linear   PRI 21-NOV-2025
DEFINITION  dystrophin isoform Dp71a [Homo sapiens].
ACCESSION   NP_004008
VERSION     NP_004008.1
DBSOURCE    REFSEQ: accession NM_004017.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Chen,L., Luo,X., Wang,H., Tian,Y. and Liu,Y.
  TITLE     Identifying inversions with breakpoints in the Dystrophin gene
            through long-read sequencing: report of two cases
  JOURNAL   BMC Med Genomics 17 (1), 227 (2024)
   PUBMED   39251998
  REMARK    GeneRIF: Identifying inversions with breakpoints in the Dystrophin
            gene through long-read sequencing: report of two cases.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Davies,K.E. and Vogt,J.
  TITLE     Long-term clinical follow-up of a family with Becker muscular
            dystrophy associated with a large deletion in the DMD gene
  JOURNAL   Neuromuscul Disord 39, 5-9 (2024)
   PUBMED   38653179
  REMARK    GeneRIF: Long-term clinical follow-up of a family with Becker
            muscular dystrophy associated with a large deletion in the DMD
            gene.
            Erratum:[Neuromuscul Disord. 2024 Jun;39:54. doi:
            10.1016/j.nmd.2024.05.010. PMID: 38801812]
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Achermann,J.C. and Vilain,E.J.
  TITLE     NR0B1-Related Adrenal Hypoplasia Congenita
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301604
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Darras,B.T., Urion,D.K. and Ghosh,P.S.
  TITLE     Dystrophinopathies
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301298
REFERENCE   7  (residues 1 to 604)
  AUTHORS   Nigro,V., Politano,L., Nigro,G., Romano,S.C., Molinari,A.M. and
            Puca,G.A.
  TITLE     Detection of a nonsense mutation in the dystrophin gene by multiple
            SSCP
  JOURNAL   Hum Mol Genet 1 (7), 517-520 (1992)
   PUBMED   1307253
REFERENCE   8  (residues 1 to 604)
  AUTHORS   Gorecki,D.C., Monaco,A.P., Derry,J.M., Walker,A.P., Barnard,E.A.
            and Barnard,P.J.
  TITLE     Expression of four alternative dystrophin transcripts in brain
            regions regulated by different promoters
  JOURNAL   Hum Mol Genet 1 (7), 505-510 (1992)
   PUBMED   1307251
REFERENCE   9  (residues 1 to 604)
  AUTHORS   Lederfein,D., Levy,Z., Augier,N., Mornet,D., Morris,G., Fuchs,O.,
            Yaffe,D. and Nudel,U.
  TITLE     A 71-kilodalton protein is a major product of the Duchenne muscular
            dystrophy gene in brain and other nonmuscle tissues
  JOURNAL   Proc Natl Acad Sci U S A 89 (12), 5346-5350 (1992)
   PUBMED   1319059
REFERENCE   10 (residues 1 to 604)
  AUTHORS   Koenig,M., Monaco,A.P. and Kunkel,L.M.
  TITLE     The complete sequence of dystrophin predicts a rod-shaped
            cytoskeletal protein
  JOURNAL   Cell 53 (2), 219-228 (1988)
   PUBMED   3282674
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078958.30, BC070078.1,
            M92650.1, BC028720.1 and AC006061.1.
            
            Summary: This gene spans a genomic range of greater than 2 Mb and
            encodes a large protein containing an N-terminal actin-binding
            domain and multiple spectrin repeats. The encoded protein forms a
            component of the dystrophin-glycoprotein complex (DGC), which
            bridges the inner cytoskeleton and the extracellular matrix.
            Deletions, duplications, and point mutations at this gene locus may
            cause Duchenne muscular dystrophy (DMD), Becker muscular dystrophy
            (BMD), or cardiomyopathy. Alternative promoter usage and
            alternative splicing result in numerous distinct transcript
            variants and protein isoforms for this gene. [provided by RefSeq,
            Dec 2016].
            
            Transcript Variant: Dp71 transcripts use exons 63-79 with a novel
            80- to 100-nt exon containing an ATG start site for a new coding
            sequence of 17 nt. The short coding sequence is in-frame with the
            consecutive dystrophin sequence from exon 63. Differential splicing
            of exons 71 and 78 produces at least four Dp71 isoforms. Of these,
            this transcript (Dp71a) lacks exon 71.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070078.1, SRR1803616.225208.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp21.2-p21.1"
     Protein         1..604
                     /product="dystrophin isoform Dp71a"
                     /note="mutant dystrophin"
                     /calculated_mol_wt=68803
     Region          1..7
                     /region_name="dystrophin Dp71/40 unique N-terminus"
     Site            12..340
                     /site_type="binding"
                     /note="dystroglycan binding site"
     Region          32..232
                     /region_name="Cysteine-rich domain"
     Region          57..218
                     /region_name="EFh_DMD"
                     /note="EF-hand-like motif found in dystrophin; cd16246"
                     /db_xref="CDD:320004"
     Site            order(57..58,60..61,79,83,87,89..90,93,104..110,112..113,
                     116,122,135,176..177,179)
                     /site_type="other"
                     /note="Domain interface"
                     /db_xref="CDD:320004"
     Region          57..96
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          62..89
                     /region_name="EF-hand 1"
     Region          103..137
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          110..138
                     /region_name="EF-hand 2"
     Site            120..122
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:320004"
     Region          143..179
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          192..218
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          232..604
                     /region_name="Carboxy-terminal region"
     Region          239..286
                     /region_name="ZZ-domain"
     Region          243..291
                     /region_name="ZZ_dystrophin"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     dystrophin and dystrobrevin. The ZZ motif coordinates two
                     zinc ions and most likely participates in ligand binding
                     or molecular scaffolding. Dystrophin attaches actin
                     filaments to an integral membrane...; cd02334"
                     /db_xref="CDD:239074"
     Site            order(245,248,260,263,269,272,282,286)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(245,248,269,272)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(246,257,259,265,267)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(258,273,288,291)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(260,263,282,286)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239074"
     Region          <331..473
                     /region_name="PRK10619"
                     /note="histidine ABC transporter ATP-binding protein HisP"
                     /db_xref="CDD:182592"
     Site            363..413
                     /site_type="binding"
                     /note="alpha1-syntrophin binding site"
     Region          <414..>518
                     /region_name="GumC"
                     /note="Exopolysaccharide export protein/domain GumC/Wzc1
                     [Cell wall/membrane/envelope biogenesis]; COG3206"
                     /db_xref="CDD:442439"
     Site            414..454
                     /site_type="binding"
                     /note="beta1-syntrophin binding site"
     Region          477..512
                     /region_name="(Leu)6-heptad repeat"
     CDS             1..604
                     /gene="DMD"
                     /gene_synonym="BMD; CMD3B; DXS142; DXS164; DXS206; DXS230;
                     DXS239; DXS268; DXS269; DXS270; DXS272; MRX85"
                     /coded_by="NM_004017.3:126..1940"
                     /note="isoform Dp71a is encoded by transcript variant
                     Dp71a"
                     /db_xref="CCDS:CCDS94585.1"
                     /db_xref="GeneID:1756"
                     /db_xref="HGNC:HGNC:2928"
                     /db_xref="MIM:300377"
ORIGIN      
        1 mreqlkghet qttcwdhpkm telyqsladl nnvrfsayrt amklrrlqka lcldllslsa
       61 acdaldqhnl kqndqpmdil qiinclttiy drleqehnnl vnvplcvdmc lnwllnvydt
      121 grtgrirvls fktgiislck ahledkyryl fkqvasstgf cdqrrlglll hdsiqiprql
      181 gevasfggsn iepsvrscfq fannkpeiea alfldwmrle pqsmvwlpvl hrvaaaetak
      241 hqakcnicke cpiigfryrs lkhfnydicq scffsgrvak ghkmhypmve yctpttsged
      301 vrdfakvlkn kfrtkryfak hprmgylpvq tvlegdnmet passpqlshd dthsriehya
      361 srlaemensn gsylndsisp nesiddehll iqhycqslnq dsplsqprsp aqilislese
      421 ergelerila dleeenrnlq aeydrlkqqh ehkglsplps ppemmptspq sprdaeliae
      481 akllrqhkgr learmqiled hnkqlesqlh rlrqlleqpq aeakvngttv sspstslqrs
      541 dssqpmllrv vgsqtsdsmg eedllsppqd tstgleevme qlnnsfpssr grntpgkpmr
      601 edtm
//
LOCUS       NP_001177649             692 aa            linear   PRI 21-NOV-2025
DEFINITION  inhibitor of nuclear factor kappa-B kinase subunit beta isoform 2
            [Homo sapiens].
ACCESSION   NP_001177649
VERSION     NP_001177649.2
DBSOURCE    REFSEQ: accession NM_001190720.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Chang,X., Guo,Y., Zhang,Q., Zheng,X., Cui,X., Hu,J., Zhang,Z.,
            Zhang,F. and Wang,X.
  TITLE     GRP78 recognizes EV-F 3D protein and activates NF-kappaB to repress
            virus replication by interacting with CHUK/IKBKB
  JOURNAL   J Virol 98 (6), e0026824 (2024)
   PUBMED   38775480
  REMARK    GeneRIF: GRP78 recognizes EV-F 3D protein and activates NF-kappaB
            to repress virus replication by interacting with CHUK/IKBKB.
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Lan,L., Huang,C., Liu,D., Cheng,Y., Tang,R., Gu,J., Geng,L.,
            Cheng,Y. and Gong,S.
  TITLE     WNT2B activates macrophages via NF-kappaB signaling pathway in
            inflammatory bowel disease
  JOURNAL   FASEB J 38 (6), e23551 (2024)
   PUBMED   38489235
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Iguchi,Y., Takahashi,Y., Li,J., Araki,K., Amakusa,Y., Kawakami,Y.,
            Kobayashi,K., Yokoi,S. and Katsuno,M.
  TITLE     IkappaB kinase phosphorylates cytoplasmic TDP-43 and promotes its
            proteasome degradation
  JOURNAL   J Cell Biol 223 (2) (2024)
   PUBMED   38197897
  REMARK    GeneRIF: IkappaB kinase phosphorylates cytoplasmic TDP-43 and
            promotes its proteasome degradation.
REFERENCE   5  (residues 1 to 692)
  AUTHORS   Mahmood,A.A., Abbas,R.F. and Hussein,H.M.
  TITLE     Novel association between single-nucleotide polymorphisms of
            IKKbeta at rs17875746 and rs12676482 and periodontitis
  JOURNAL   Dent Med Probl 60 (4), 627-634 (2023)
   PUBMED   37930783
  REMARK    GeneRIF: Novel association between single-nucleotide polymorphisms
            of IKKbeta at rs17875746 and rs12676482 and periodontitis.
REFERENCE   6  (residues 1 to 692)
  AUTHORS   DiDonato,J., Mercurio,F., Rosette,C., Wu-Li,J., Suyang,H., Ghosh,S.
            and Karin,M.
  TITLE     Mapping of the inducible IkappaB phosphorylation sites that signal
            its ubiquitination and degradation
  JOURNAL   Mol Cell Biol 16 (4), 1295-1304 (1996)
   PUBMED   8657102
REFERENCE   7  (residues 1 to 692)
  AUTHORS   Chen,Z.J., Parent,L. and Maniatis,T.
  TITLE     Site-specific phosphorylation of IkappaBalpha by a novel
            ubiquitination-dependent protein kinase activity
  JOURNAL   Cell 84 (6), 853-862 (1996)
   PUBMED   8601309
REFERENCE   8  (residues 1 to 692)
  AUTHORS   Hiscott,J., Marois,J., Garoufalis,J., D'Addario,M., Roulston,A.,
            Kwan,I., Pepin,N., Lacoste,J., Nguyen,H., Bensi,G. et al.
  TITLE     Characterization of a functional NF-kappa B site in the human
            interleukin 1 beta promoter: evidence for a positive autoregulatory
            loop
  JOURNAL   Mol Cell Biol 13 (10), 6231-6240 (1993)
   PUBMED   8413223
REFERENCE   9  (residues 1 to 692)
  AUTHORS   Ganchi,P.A., Sun,S.C., Greene,W.C. and Ballard,D.W.
  TITLE     I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B
            p65 and requires the transactivation domain to inhibit NF-kappa B
            p65 DNA binding
  JOURNAL   Mol Biol Cell 3 (12), 1339-1352 (1992)
   PUBMED   1493333
REFERENCE   10 (residues 1 to 692)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC083973.14, AK302723.1 and
            AK091297.1.
            
            On Apr 15, 2020 this sequence version replaced NP_001177649.1.
            
            Summary: The protein encoded by this gene phosphorylates the
            inhibitor in the inhibitor/NF-kappa-B complex, causing dissociation
            of the inhibitor and activation of NF-kappa-B. The encoded protein
            itself is found in a complex of proteins. Several transcript
            variants, some protein-coding and some not, have been found for
            this gene. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (2) lacks an exon in the 5'
            region, resulting in an upstream AUG start codon, as compared to
            variant 1. The resulting isoform (2) is slightly shorter and has a
            different N-terminus, as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302723.1, AK316418.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437, SAMEA2159368
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.21"
     Protein         1..692
                     /product="inhibitor of nuclear factor kappa-B kinase
                     subunit beta isoform 2"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.11.10"
                     /note="nuclear factor NF-kappa-B inhibitor kinase beta;
                     I-kappa-B kinase 2; I-kappa-B-kinase beta;
                     serine/threonine protein kinase IKBKB; nuclear factor
                     kappa B kinase subunit beta; inhibitor of kappa light
                     polypeptide gene enhancer in B-cells, kinase beta"
                     /calculated_mol_wt=78974
     Region          1..245
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          246..326
                     /region_name="Ubl_IKKA_like"
                     /note="ubiquitin-like (Ubl) domain found in inhibitor of
                     nuclear factor kappa-B kinases, IKK-alpha and IKK-beta,
                     and similar proteins; cd17046"
                     /db_xref="CDD:340566"
     Region          325..599
                     /region_name="IKBKB_SDD"
                     /note="IQBAL scaffold dimerization domain; pfam18397"
                     /db_xref="CDD:465745"
     Region          642..678
                     /region_name="IKKbetaNEMObind"
                     /note="I-kappa-kinase-beta NEMO binding domain; pfam12179"
                     /db_xref="CDD:463485"
     CDS             1..692
                     /gene="IKBKB"
                     /gene_synonym="IKK-2; IKK-beta; IKK2; IKKB; IMD15; IMD15A;
                     IMD15B; NFKBIKB"
                     /coded_by="NM_001190720.3:256..2334"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55228.2"
                     /db_xref="GeneID:3551"
                     /db_xref="HGNC:HGNC:5960"
                     /db_xref="MIM:603258"
ORIGIN      
        1 mrrlthpnvv aardvpegmq nlapndlpll ameycqggdl rkylnqfenc cglregailt
       61 llsdiasalr ylhenriihr dlkpenivlq qgeqrlihki idlgyakeld qgslctsfvg
      121 tlqylapell eqqkytvtvd ywsfgtlafe citgfrpflp nwqpvqwhsk vrqksevdiv
      181 vsedlngtvk fssslpypnn lnsvlaerle kwlqlmlmwh prqrgtdpty gpngcfkald
      241 dilnlklvhi lnmvtgtiht ypvtedeslq slkariqqdt gipeedqell qeaglalipd
      301 kpatqcisdg klneghtldm dlvflfdnsk ityetqispr pqpesvscil qepkrnlaff
      361 qlrkvwgqvw hsiqtlkedc nrlqqgqraa mmnllrnnsc lskmknsmas msqqlkakld
      421 ffktsiqidl ekyseqtefg itsdklllaw remeqavelc grenevkllv ermmalqtdi
      481 vdlqrspmgr kqggtlddle eqarelyrrl rekprdqrte gdsqemvrll lqaiqsfekk
      541 vrviytqlsk tvvckqkale llpkveevvs lmnedektvv rlqekrqkel wnllkiacsk
      601 vrgpvsgspd smnasrlsqp gqlmsqpsta snslpepakk seelvaeahn lctllenaiq
      661 dtvreqdqsf taldwswlqt eeeehscleq as
//
LOCUS       NP_001364427             299 aa            linear   PRI 21-NOV-2025
DEFINITION  non-homologous end-joining factor 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001364427
VERSION     NP_001364427.1
DBSOURCE    REFSEQ: accession NM_001377498.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Vu,D.D., Bonucci,A., Breniere,M., Cisneros-Aguirre,M.,
            Pelupessy,P., Wang,Z., Carlier,L., Bouvignies,G., Cortes,P.,
            Aggarwal,A.K., Blackledge,M., Gueroui,Z., Belle,V., Stark,J.M.,
            Modesti,M. and Ferrage,F.
  TITLE     Multivalent interactions of the disordered regions of XLF and XRCC4
            foster robust cellular NHEJ and drive the formation of
            ligation-boosting condensates in vitro
  JOURNAL   Nat Struct Mol Biol 31 (11), 1732-1744 (2024)
   PUBMED   38898102
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Seif-El-Dahan,M., Kefala-Stavridi,A., Frit,P., Hardwick,S.W.,
            Chirgadze,D.Y., Maia De Oliviera,T., Andreani,J., Britton,S.,
            Barboule,N., Bossaert,M., Pandurangan,A.P., Meek,K., Blundell,T.L.,
            Ropars,V., Calsou,P., Charbonnier,J.B. and Chaplin,A.K.
  TITLE     PAXX binding to the NHEJ machinery explains functional redundancy
            with XLF
  JOURNAL   Sci Adv 9 (22), eadg2834 (2023)
   PUBMED   37256950
  REMARK    GeneRIF: PAXX binding to the NHEJ machinery explains functional
            redundancy with XLF.
            Erratum:[Sci Adv. 2023 Sep 29;9(39):eadj8489. doi:
            10.1126/sciadv.adj8489. PMID: 37774037]
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Chaplin,A.K., Hardwick,S.W., Stavridi,A.K., Buehl,C.J., Goff,N.J.,
            Ropars,V., Liang,S., De Oliveira,T.M., Chirgadze,D.Y., Meek,K.,
            Charbonnier,J.B. and Blundell,T.L.
  TITLE     Cryo-EM of NHEJ supercomplexes provides insights into DNA repair
  JOURNAL   Mol Cell 81 (16), 3400-3409 (2021)
   PUBMED   34352203
  REMARK    GeneRIF: Cryo-EM of NHEJ supercomplexes provides insights into DNA
            repair.
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Andres,S.N., Modesti,M., Tsai,C.J., Chu,G. and Junop,M.S.
  TITLE     Crystal structure of human XLF: a twist in nonhomologous DNA
            end-joining
  JOURNAL   Mol Cell 28 (6), 1093-1101 (2007)
   PUBMED   18158905
  REMARK    GeneRIF: Mutational analysis of XLF and XRCC4 reveals a potential
            interaction interface, suggesting a mechanism for how XLF
            stimulates the ligation of mismatched ends.
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Tsai,C.J., Kim,S.A. and Chu,G.
  TITLE     Cernunnos/XLF promotes the ligation of mismatched and noncohesive
            DNA ends
  JOURNAL   Proc Natl Acad Sci U S A 104 (19), 7851-7856 (2007)
   PUBMED   17470781
  REMARK    GeneRIF: Cernunnos/XRCC4-like factor promotes a mismatched end
            (MEnd) DNA ligase activity to facilitate joining and to preserve
            DNA sequence.
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Revy,P. and de Villartay,J.P.
  TITLE     [Cernunnos, a novel DNA repair factor essential for the immune
            system]
  JOURNAL   Med Sci (Paris) 22 (6-7), 569-570 (2006)
   PUBMED   16828027
  REMARK    GeneRIF: DNA repair protein involved in lymphocyte activation and
            cell division.
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Callebaut,I., Malivert,L., Fischer,A., Mornon,J.P., Revy,P. and de
            Villartay,J.P.
  TITLE     Cernunnos interacts with the XRCC4 x DNA-ligase IV complex and is
            homologous to the yeast nonhomologous end-joining factor Nej1
  JOURNAL   J Biol Chem 281 (20), 13857-13860 (2006)
   PUBMED   16571728
  REMARK    GeneRIF: Cernunnos physically interacts with the XRCC4 x DNA-ligase
            IV complex
REFERENCE   8  (residues 1 to 299)
  AUTHORS   Ahnesorg,P., Smith,P. and Jackson,S.P.
  TITLE     XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA
            nonhomologous end-joining
  JOURNAL   Cell 124 (2), 301-313 (2006)
   PUBMED   16439205
  REMARK    GeneRIF: Studies on the binding of XLF and its role in DNA repair.
            GeneRIF: The XLF-encoded protein (XRRC4 like factor, FLJ12610) is
            involved in DNA double-strand break repair via nonhomologous
            end-joining and associates with the Ligase IV-XRCC4 complex. XLF is
            mutated in a number of radiosensitive and immuno-deficient
            patients.
REFERENCE   9  (residues 1 to 299)
  AUTHORS   Buck,D., Malivert,L., de Chasseval,R., Barraud,A., Fondaneche,M.C.,
            Sanal,O., Plebani,A., Stephan,J.L., Hufnagel,M., le Deist,F.,
            Fischer,A., Durandy,A., de Villartay,J.P. and Revy,P.
  TITLE     Cernunnos, a novel nonhomologous end-joining factor, is mutated in
            human immunodeficiency with microcephaly
  JOURNAL   Cell 124 (2), 287-299 (2006)
   PUBMED   16439204
  REMARK    GeneRIF: Cernunnos-XLF is a new Non-homologous End Joining pathway
            protein, which if mutated results in several conditions
            -immunodeficiency and developmental anomalies and other conditions,
            which likely result from inability to repair spontaneous DNA
            damage.
REFERENCE   10 (residues 1 to 299)
  AUTHORS   Dai,Y., Kysela,B., Hanakahi,L.A., Manolis,K., Riballo,E., Stumm,M.,
            Harville,T.O., West,S.C., Oettinger,M.A. and Jeggo,P.A.
  TITLE     Nonhomologous end joining and V(D)J recombination require an
            additional factor
  JOURNAL   Proc Natl Acad Sci U S A 100 (5), 2462-2467 (2003)
   PUBMED   12604777
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068946.4 and AC097468.3.
            
            Summary: Double-strand breaks in DNA result from genotoxic stresses
            and are among the most damaging of DNA lesions. This gene encodes a
            DNA repair factor essential for the nonhomologous end-joining
            pathway, which preferentially mediates repair of double-stranded
            breaks. Mutations in this gene cause different kinds of severe
            combined immunodeficiency disorders. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2173844.1,
                                           SRR14038194.4086499.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..299
                     /product="non-homologous end-joining factor 1 isoform 1"
                     /note="XRCC4-like factor; protein cernunnos; nonhomologous
                     end-joining factor 1"
                     /calculated_mol_wt=33206
     Region          1..135
                     /region_name="Globular head.
                     /evidence=ECO:0000305|PubMed:16571728"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Region          12..174
                     /region_name="XLF"
                     /note="XLF-Cernunnos, XRcc4-like factor, NHEJ component;
                     pfam09302"
                     /db_xref="CDD:462749"
     Site            115
                     /site_type="other"
                     /note="Leu-lock. /evidence=ECO:0000303|PubMed:21775435;
                     propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PRKDC.
                     /evidence=ECO:0000269|PubMed:18644470,
                     ECO:0000269|PubMed:22228831, ECO:0000269|PubMed:28500754;
                     propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PRKDC.
                     /evidence=ECO:0000269|PubMed:18644470,
                     ECO:0000269|PubMed:22228831, ECO:0000269|PubMed:28500754;
                     propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Region          224..288
                     /region_name="C-terminal tail.
                     /evidence=ECO:0000250|UniProtKB:A0A1L8ENT6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PRKDC.
                     /evidence=ECO:0000269|PubMed:18644470,
                     ECO:0000269|PubMed:22228831, ECO:0000269|PubMed:28500754;
                     propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PRKDC.
                     /evidence=ECO:0000269|PubMed:18644470,
                     ECO:0000269|PubMed:22228831, ECO:0000269|PubMed:28500754;
                     propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Region          255..299
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18644470,
                     ECO:0000269|PubMed:22228831; propagated from
                     UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:18644470,
                     ECO:0000269|PubMed:22228831; propagated from
                     UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Region          289..299
                     /region_name="XLM. /evidence=ECO:0000305|PubMed:27063109"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     CDS             1..299
                     /gene="NHEJ1"
                     /gene_synonym="IMD124; MCOPCB13; XLF"
                     /coded_by="NM_001377498.1:47..946"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS2432.1"
                     /db_xref="GeneID:79840"
                     /db_xref="HGNC:HGNC:25737"
                     /db_xref="MIM:611290"
ORIGIN      
        1 meeleqgllm qpwawlqlae nsllakvfit kqgyallvsd lqqvwheqvd tsvvsqrake
       61 lnkrltappa aflchldnll rpllkdaahp seatfscdcv adalilrvrs elsglpfywn
      121 fhcmlaspsl vsqhlirplm gmslalqcqv relatllhmk dleiqdyqes gatlirdrlk
      181 tepfeensfl eqfmieklpe acsigdgkpf vmnlqdlyma vttqevqvgq khqgagdpht
      241 snsaslqgid sqcvnqpeql vssaptlsap ekestgtsgp lqrpqlskvk rkkprglfs
//
LOCUS       NP_001374809             745 aa            linear   PRI 21-NOV-2025
DEFINITION  protein mono-ADP-ribosyltransferase PARP9 isoform f [Homo sapiens].
ACCESSION   NP_001374809
VERSION     NP_001374809.1
DBSOURCE    REFSEQ: accession NM_001387880.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 745)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 745)
  AUTHORS   Pandi,K., Angabo,S., Makkawi,H., Benyamini,H., Elgavish,S. and
            Nussbaum,G.
  TITLE     P. gingivalis-Induced TLR2 Interactome Analysis Reveals Association
            with PARP9
  JOURNAL   J Dent Res 103 (3), 329-338 (2024)
   PUBMED   38344758
  REMARK    GeneRIF: P. gingivalis-Induced TLR2 Interactome Analysis Reveals
            Association with PARP9.
REFERENCE   3  (residues 1 to 745)
  AUTHORS   Thirunavukkarasu,S., Ahmed,M., Rosa,B.A., Boothby,M., Cho,S.H.,
            Rangel-Moreno,J., Mbandi,S.K., Schreiber,V., Gupta,A., Zuniga,J.,
            Mitreva,M., Kaushal,D., Scriba,T.J. and Khader,S.A.
  TITLE     Poly(ADP-ribose) polymerase 9 mediates early protection against
            Mycobacterium tuberculosis infection by regulating type I IFN
            production
  JOURNAL   J Clin Invest 133 (12), e158630 (2023)
   PUBMED   37200107
  REMARK    GeneRIF: Poly(ADP-ribose) polymerase 9 mediates early protection
            against Mycobacterium tuberculosis infection by regulating type I
            IFN production.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 745)
  AUTHORS   Russo,L.C., Tomasin,R., Matos,I.A., Manucci,A.C., Sowa,S.T.,
            Dale,K., Caldecott,K.W., Lehtio,L., Schechtman,D., Meotti,F.C.,
            Bruni-Cardoso,A. and Hoch,N.C.
  TITLE     The SARS-CoV-2 Nsp3 macrodomain reverses PARP9/DTX3L-dependent
            ADP-ribosylation induced by interferon signaling
  JOURNAL   J Biol Chem 297 (3), 101041 (2021)
   PUBMED   34358560
  REMARK    GeneRIF: The SARS-CoV-2 Nsp3 macrodomain reverses
            PARP9/DTX3L-dependent ADP-ribosylation induced by interferon
            signaling.
REFERENCE   5  (residues 1 to 745)
  AUTHORS   Xing,J., Zhang,A., Du,Y., Fang,M., Minze,L.J., Liu,Y.J., Li,X.C.
            and Zhang,Z.
  TITLE     Identification of poly(ADP-ribose) polymerase 9 (PARP9) as a
            noncanonical sensor for RNA virus in dendritic cells
  JOURNAL   Nat Commun 12 (1), 2681 (2021)
   PUBMED   33976210
  REMARK    GeneRIF: Identification of poly(ADP-ribose) polymerase 9 (PARP9) as
            a noncanonical sensor for RNA virus in dendritic cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 745)
  AUTHORS   Jha,R., Agarwal,A., Mahfouz,R., Paasch,U., Grunewald,S.,
            Sabanegh,E., Yadav,S.P. and Sharma,R.
  TITLE     Determination of Poly (ADP-ribose) polymerase (PARP) homologues in
            human ejaculated sperm and its correlation with sperm maturation
  JOURNAL   Fertil Steril 91 (3), 782-790 (2009)
   PUBMED   18339380
  REMARK    GeneRIF: Determination of Poly (ADP-ribose) polymerase (PARP)
            homologues in human ejaculated sperm and its correlation with sperm
            maturation.
REFERENCE   7  (residues 1 to 745)
  AUTHORS   Juszczynski,P., Kutok,J.L., Li,C., Mitra,J., Aguiar,R.C. and
            Shipp,M.A.
  TITLE     BAL1 and BBAP are regulated by a gamma interferon-responsive
            bidirectional promoter and are overexpressed in diffuse large
            B-cell lymphomas with a prominent inflammatory infiltrate
  JOURNAL   Mol Cell Biol 26 (14), 5348-5359 (2006)
   PUBMED   16809771
  REMARK    GeneRIF: BAL1 and BBAP are located on chromosome 3q21 in a
            head-to-head orientation and are regulated by a
            IFN-gamma-responsive bidirectional promoter.
REFERENCE   8  (residues 1 to 745)
  AUTHORS   Aguiar,R.C., Takeyama,K., He,C., Kreinbrink,K. and Shipp,M.A.
  TITLE     B-aggressive lymphoma family proteins have unique domains that
            modulate transcription and exhibit poly(ADP-ribose) polymerase
            activity
  JOURNAL   J Biol Chem 280 (40), 33756-33765 (2005)
   PUBMED   16061477
REFERENCE   9  (residues 1 to 745)
  AUTHORS   Takeyama,K., Aguiar,R.C., Gu,L., He,C., Freeman,G.J., Kutok,J.L.,
            Aster,J.C. and Shipp,M.A.
  TITLE     The BAL-binding protein BBAP and related Deltex family members
            exhibit ubiquitin-protein isopeptide ligase activity
  JOURNAL   J Biol Chem 278 (24), 21930-21937 (2003)
   PUBMED   12670957
REFERENCE   10 (residues 1 to 745)
  AUTHORS   Aguiar,R.C., Yakushijin,Y., Kharbanda,S., Salgia,R., Fletcher,J.A.
            and Shipp,M.A.
  TITLE     BAL is a novel risk-related gene in diffuse large B-cell lymphomas
            that enhances cellular migration
  JOURNAL   Blood 96 (13), 4328-4334 (2000)
   PUBMED   11110709
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092908.9.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2415555.1,
                                           SRR14038194.1634975.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..745
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.1"
     Protein         1..745
                     /product="protein mono-ADP-ribosyltransferase PARP9
                     isoform f"
                     /EC_number="2.4.2.30"
                     /note="poly [ADP-ribose] polymerase 9; poly (ADP-ribose)
                     polymerase 9; PARP-9; b aggressive lymphoma protein;
                     ADP-ribosyltransferase diphtheria toxin-like 9; protein
                     mono-ADP-ribosyltransferase PARP9"
                     /calculated_mol_wt=84232
     Region          117..277
                     /region_name="Macro_Af1521_BAL-like"
                     /note="macrodomain, Af1521-like family; cd02907"
                     /db_xref="CDD:394877"
     Site            order(125..127,138..140,144..150,152,238..244)
                     /site_type="other"
                     /note="ADP-ribose binding site [chemical binding]"
                     /db_xref="CDD:394877"
     Region          310..486
                     /region_name="Macro_BAL-like"
                     /note="macrodomain, B-aggressive lymphoma (BAL)-like
                     family; cd02903"
                     /db_xref="CDD:394874"
     Site            order(325..327,337..339,345..348,351,429..435,469,475)
                     /site_type="other"
                     /note="ADP-ribose binding site [chemical binding]"
                     /db_xref="CDD:394874"
     Region          702..>730
                     /region_name="ADP_ribosyl"
                     /note="ADP_ribosylating enzymes catalyze the transfer of
                     ADP_ribose from NAD+ to substrates. Bacterial toxins are
                     cytoplasmic and catalyze the transfer of a single
                     ADP_ribose unit to eukaryotic elongation factor 2, halting
                     protein synthesis and killing the cell; cl00283"
                     /db_xref="CDD:444809"
     CDS             1..745
                     /gene="PARP9"
                     /gene_synonym="ARTD9; BAL; BAL1; MGC:7868"
                     /coded_by="NM_001387880.1:146..2383"
                     /note="isoform f is encoded by transcript variant 19"
                     /db_xref="GeneID:83666"
                     /db_xref="HGNC:HGNC:24118"
                     /db_xref="MIM:612065"
ORIGIN      
        1 mdfsmvagaa ayneksgrit slsllfqkvf aqifpqwrkg nteeclpykc setgalgeny
       61 swqipinhnd fkilknnerq lcevlqnkfg cistlvspvq egnskslqvf rkmltpriel
      121 svwkddltth avdavvnaan edllhgggla lalvkaggfe iqeeskqfva rygkvsagei
      181 avtgagrlpc kqiihavgpr wmewdkqgct gklqraivsi lnyviyknth iktvaipals
      241 sgifqfplnl ctktivetir vslqgkpmms nlkeihlvsn edptvaafka asefilgkse
      301 lgqettpsfn amvvnnltlq ivqghiewqt advivnsvnp hditvgpvak silqqagvem
      361 kseflatkak qfqrsqlvlv tkgfnlfcky iyhvlwhsef pkpqilkham keclekcieq
      421 nitsisfpal gtgnmeikke taaeilfdev ltfakdhvkh qltvkfvifp tdleiykafs
      481 semakrskml slnnysvpqs treekrengl earspainlm gfnveemyea hawiqrilsl
      541 qnhhiiennh ilylgrkehd ilsqlqktss vsiteiispg rteleiegar adlievvmni
      601 edmlckvqee markkerglw rslgqwtiqq qktqdemken iiflkcpvpp tqelldqkkq
      661 fekcglqvlk vekidnevlm aafqrkkkmm eeklhrqpvs hrlfqqvpyq fcnvvcrvgf
      721 qrmystpcgr cqcliigatl wnlvs
//
LOCUS       NP_002884                425 aa            linear   PRI 21-NOV-2025
DEFINITION  histone-binding protein RBBP7 isoform 2 [Homo sapiens].
ACCESSION   NP_002884 XP_001128430 XP_001128441
VERSION     NP_002884.1
DBSOURCE    REFSEQ: accession NM_002893.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Zhan,Y., Yin,A., Su,X., Tang,N., Zhang,Z., Chen,Y., Wang,W. and
            Wang,J.
  TITLE     Interpreting the molecular mechanisms of RBBP4/7 and their roles in
            human diseases (Review)
  JOURNAL   Int J Mol Med 53 (5) (2024)
   PUBMED   38577935
  REMARK    GeneRIF: Interpreting the molecular mechanisms of RBBP4/7 and their
            roles in human diseases (Review).
            Review article
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Fang,Y., Tang,W., Qu,S., Li,Z., Zhang,X., Miao,Y., Zeng,Z. and
            Huang,H.
  TITLE     RBBP7, regulated by SP1, enhances the Warburg effect to facilitate
            the proliferation of hepatocellular carcinoma cells via PI3K/AKT
            signaling
  JOURNAL   J Transl Med 22 (1), 170 (2024)
   PUBMED   38368381
  REMARK    GeneRIF: RBBP7, regulated by SP1, enhances the Warburg effect to
            facilitate the proliferation of hepatocellular carcinoma cells via
            PI3K/AKT signaling.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Li,J., Zheng,H., Hou,J., Chen,J., Zhang,F., Yang,X., Jin,F. and
            Xi,Y.
  TITLE     X-linked RBBP7 mutation causes maturation arrest and testicular
            tumors
  JOURNAL   J Clin Invest 133 (20), e171541 (2023)
   PUBMED   37843278
  REMARK    GeneRIF: X-linked RBBP7 mutation causes maturation arrest and
            testicular tumors.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Guo,L., Xia,Y., Li,H., Wang,Z., Xu,H., Dai,X., Zhang,Y., Zhang,H.,
            Fan,W., Wei,F., Li,Q., Zhang,L., Cao,L., Zhang,S., Hu,W. and Gu,H.
  TITLE     FIT links c-Myc and P53 acetylation by recruiting RBBP7 during
            colorectal carcinogenesis
  JOURNAL   Cancer Gene Ther 30 (8), 1124-1133 (2023)
   PUBMED   37225855
  REMARK    GeneRIF: FIT links c-Myc and P53 acetylation by recruiting RBBP7
            during colorectal carcinogenesis.
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Zhang,Y., Sun,Z.W., Iratni,R., Erdjument-Bromage,H., Tempst,P.,
            Hampsey,M. and Reinberg,D.
  TITLE     SAP30, a novel protein conserved between human and yeast, is a
            component of a histone deacetylase complex
  JOURNAL   Mol Cell 1 (7), 1021-1031 (1998)
   PUBMED   9651585
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Verreault,A., Kaufman,P.D., Kobayashi,R. and Stillman,B.
  TITLE     Nucleosomal DNA regulates the core-histone-binding subunit of the
            human Hat1 acetyltransferase
  JOURNAL   Curr Biol 8 (2), 96-108 (1998)
   PUBMED   9427644
REFERENCE   8  (residues 1 to 425)
  AUTHORS   Zhang,Y., Iratni,R., Erdjument-Bromage,H., Tempst,P. and
            Reinberg,D.
  TITLE     Histone deacetylases and SAP18, a novel polypeptide, are components
            of a human Sin3 complex
  JOURNAL   Cell 89 (3), 357-364 (1997)
   PUBMED   9150135
REFERENCE   9  (residues 1 to 425)
  AUTHORS   Qian,Y.W. and Lee,E.Y.
  TITLE     Dual retinoblastoma-binding proteins with properties related to a
            negative regulator of ras in yeast
  JOURNAL   J Biol Chem 270 (43), 25507-25513 (1995)
   PUBMED   7503932
REFERENCE   10 (residues 1 to 425)
  AUTHORS   Huang,S., Lee,W.H. and Lee,E.Y.
  TITLE     A cellular protein that competes with SV40 T antigen for binding to
            the retinoblastoma gene product
  JOURNAL   Nature 350 (6314), 160-162 (1991)
   PUBMED   2005966
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB460068.1, BC114501.1,
            AL929302.16 and CN414343.1.
            
            On or before Sep 20, 2006 this sequence version replaced
            XP_001128441.1, XP_001128430.1.
            
            Summary: This protein is a ubiquitously expressed nuclear protein
            and belongs to a highly conserved subfamily of WD-repeat proteins.
            It is found among several proteins that binds directly to
            retinoblastoma protein, which regulates cell proliferation. The
            encoded protein is found in many histone deacetylase complexes,
            including mSin3 co-repressor complex. It is also present in protein
            complexes involved in chromatin assembly. This protein can interact
            with BRCA1 tumor-suppressor gene and may have a role in the
            regulation of cell proliferation and differentiation. Two
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Nov 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (2)
            has a shorter and distinct N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3169955.1,
                                           SRR14038197.187113.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380087.7/ ENSP00000369427.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..425
                     /product="histone-binding protein RBBP7 isoform 2"
                     /note="G1/S transition control protein-binding protein
                     RbAp46; histone acetyltransferase type B subunit 2;
                     retinoblastoma-binding protein p46; retinoblastoma-binding
                     protein RbAp46; histone-binding protein RBBP7; RBBP-7;
                     nucleosome-remodeling factor subunit RBAP46;
                     retinoblastoma-binding protein 7"
                     /calculated_mol_wt=47689
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378;
                     N-acetylalanine. /evidence=ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q16576.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16576.1)"
     Site            4
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q16576.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16576.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q16576.1)"
     Region          18..87
                     /region_name="CAF1C_H4-bd"
                     /note="Histone-binding protein RBBP4 or subunit C of CAF1
                     complex; pfam12265"
                     /db_xref="CDD:463513"
     Region          47..122
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16576.1)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q16576.1)"
     Site            119
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60973; propagated from
                     UniProtKB/Swiss-Prot (Q16576.1)"
     Region          127..174
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          128..173
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16576.1)"
     Site            159
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q60973; propagated from
                     UniProtKB/Swiss-Prot (Q16576.1)"
     Region          <171..404
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          179..223
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          181..217
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16576.1)"
     Region          228..269
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16576.1)"
     Region          230..264
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          275..313
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          275..312
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16576.1)"
     Region          318..369
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16576.1)"
     Region          319..370
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16576.1)"
     Region          376..403
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16576.1)"
     Region          376..401
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..425
                     /gene="RBBP7"
                     /gene_synonym="RbAp46; SPGFX9"
                     /coded_by="NM_002893.4:310..1587"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS14179.1"
                     /db_xref="GeneID:5931"
                     /db_xref="HGNC:HGNC:9890"
                     /db_xref="MIM:300825"
ORIGIN      
        1 maskemfedt veervineey kiwkkntpfl ydlvmthalq wpsltvqwlp evtkpegkdy
       61 alhwlvlgth tsdeqnhlvv arvhipndda qfdashcdsd kgefggfgsv tgkieceiki
      121 nhegevnrar ympqnphiia tktpssdvlv fdytkhpakp dpsgecnpdl rlrghqkegy
      181 glswnsnlsg hllsasddht vclwdinagp kegkivdaka iftghsavve dvawhllhes
      241 lfgsvaddqk lmiwdtrsnt tskpshlvda htaevnclsf npysefilat gsadktvalw
      301 dlrnlklklh tfeshkdeif qvhwsphnet ilassgtdrr lnvwdlskig eeqsaedaed
      361 gppellfihg ghtakisdfs wnpnepwvic svsednimqi wqmaeniynd eesdvttsel
      421 egqgs
//
LOCUS       NP_001305453             146 aa            linear   PRI 21-NOV-2025
DEFINITION  trafficking protein particle complex subunit 2-like protein isoform
            1 [Homo sapiens].
ACCESSION   NP_001305453
VERSION     NP_001305453.1
DBSOURCE    REFSEQ: accession NM_001318524.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Abaji,M., Mignon-Ravix,C., Gorokhova,S., Cacciagli,P., Mortreux,J.,
            Molinari,F., Chabrol,B., Sigaudy,S., Villard,L. and Riccardi,F.
  TITLE     TRAPPC2L-related disorder: first homozygous protein-truncating
            variant and further delineation of the phenotype
  JOURNAL   J Med Genet 60 (10), 1021-1025 (2023)
   PUBMED   36849228
  REMARK    GeneRIF: TRAPPC2L-related disorder: first homozygous
            protein-truncating variant and further delineation of the
            phenotype.
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Al-Deri,N., Okur,V., Ahimaz,P., Milev,M., Valivullah,Z., Hagen,J.,
            Sheng,Y., Chung,W., Sacher,M. and Ganapathi,M.
  TITLE     A novel homozygous variant in TRAPPC2L results in a
            neurodevelopmental disorder and disrupts TRAPP complex function
  JOURNAL   J Med Genet 58 (9), 592-601 (2021)
   PUBMED   32843486
  REMARK    GeneRIF: A novel homozygous variant in TRAPPC2L results in a
            neurodevelopmental disorder and disrupts TRAPP complex function.
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Scrivens,P.J., Noueihed,B., Shahrzad,N., Hul,S., Brunet,S. and
            Sacher,M.
  TITLE     C4orf41 and TTC-15 are mammalian TRAPP components with a role at an
            early stage in ER-to-Golgi trafficking
  JOURNAL   Mol Biol Cell 22 (12), 2083-2093 (2011)
   PUBMED   21525244
REFERENCE   7  (residues 1 to 146)
  AUTHORS   Choi,C., Davey,M., Schluter,C., Pandher,P., Fang,Y., Foster,L.J.
            and Conibear,E.
  TITLE     Organization and assembly of the TRAPPII complex
  JOURNAL   Traffic 12 (6), 715-725 (2011)
   PUBMED   21453443
REFERENCE   8  (residues 1 to 146)
  AUTHORS   Westlake,C.J., Baye,L.M., Nachury,M.V., Wright,K.J., Ervin,K.E.,
            Phu,L., Chalouni,C., Beck,J.S., Kirkpatrick,D.S., Slusarski,D.C.,
            Sheffield,V.C., Scheller,R.H. and Jackson,P.K.
  TITLE     Primary cilia membrane assembly is initiated by Rab11 and transport
            protein particle II (TRAPPII) complex-dependent trafficking of
            Rabin8 to the centrosome
  JOURNAL   Proc Natl Acad Sci U S A 108 (7), 2759-2764 (2011)
   PUBMED   21273506
REFERENCE   9  (residues 1 to 146)
  AUTHORS   Garcia,S.A. and Nagai,M.A.
  TITLE     Transcriptional regulation of bidirectional gene pairs by
            17-beta-estradiol in MCF-7 breast cancer cells
  JOURNAL   Braz J Med Biol Res 44 (2), 112-122 (2011)
   PUBMED   21180879
REFERENCE   10 (residues 1 to 146)
  AUTHORS   Scrivens,P.J., Shahrzad,N., Moores,A., Morin,A., Brunet,S. and
            Sacher,M.
  TITLE     TRAPPC2L is a novel, highly conserved TRAPP-interacting protein
  JOURNAL   Traffic 10 (6), 724-736 (2009)
   PUBMED   19416478
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA209193.1, BX419849.2,
            BC011369.1 and BC017440.1.
            
            Summary: This gene encodes a protein that interacts with the
            tethering factor trafficking protein particle (TRAPP complex).
            TRAPP complexes mediate the contact between vescicles and target
            membranes, and thus, are involved in vescicle-mediated transport of
            proteins and lipids. The encoded protein is related to the X-linked
            trafficking protein particle complex 2. A related pseudogene is
            located on the X chromosome. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.47318.1,
                                           SRR1803616.258318.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..146
                     /product="trafficking protein particle complex subunit
                     2-like protein isoform 1"
                     /note="hematopoietic stem/progenitor cells 176;
                     trafficking protein particle complex subunit 2-like
                     protein; trafficking protein particle complex 2 like"
                     /calculated_mol_wt=16545
     Region          3..142
                     /region_name="TRAPPC2L"
                     /note="Trafficking protein particle complex subunit
                     2-like; cd14854"
                     /db_xref="CDD:341444"
     CDS             1..146
                     /gene="TRAPPC2L"
                     /gene_synonym="HSPC176; PERRB"
                     /coded_by="NM_001318524.2:25..465"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS82027.1"
                     /db_xref="GeneID:51693"
                     /db_xref="HGNC:HGNC:30887"
                     /db_xref="MIM:610970"
ORIGIN      
        1 mavciaviak enyplyirst ptenelkfhy mvhtsldvvd ekisamgkal vdqrelylgl
       61 lyptedykvy gyvtnskvkf vmvvdssnta lrdneirsmf rklhnsytdv mcnpfynpgd
      121 riqssgsvsl srafdnmvts mmiqvc
//
LOCUS       NP_001093863             291 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 2 [Homo sapiens].
ACCESSION   NP_001093863
VERSION     NP_001093863.1
DBSOURCE    REFSEQ: accession NM_001100393.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            Transcript Variant: This variant (4) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream start codon, compared to variant 1. Variants 2 through 4
            encode the same isoform (2), which has a shorter N-terminus
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK094543.1, SRR1803616.105524.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..291
                     /product="RNA-binding Raly-like protein isoform 2"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=32199
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          171..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     Region          199..>244
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     Region          249..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     CDS             1..291
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001100393.3:329..1204"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS55253.1"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly rleskepfls
      121 vggyvfdydy yrddfynrlf dyhgrvpppp raviplkrpr vavtttrrgk gvfsmkggsr
      181 stasgstgsk lksdelqtik keltqiktki dsllgrleki ekqqkaeaea qkkqleeslv
      241 liqeecvsei adhsteepae ggpdadgeem tdgieedfde dgghelflqi k
//
LOCUS       NP_001358056            1210 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal cell adhesion molecule isoform Q precursor [Homo sapiens].
ACCESSION   NP_001358056
VERSION     NP_001358056.1
DBSOURCE    REFSEQ: accession NM_001371127.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1210)
  AUTHORS   Wang,C., Wang,Z., Fu,L., Du,J., Ji,F. and Qiu,X.
  TITLE     CircNRCAM up-regulates NRCAM to promote papillary thyroid carcinoma
            progression
  JOURNAL   J Endocrinol Invest 47 (5), 1215-1226 (2024)
   PUBMED   38485895
  REMARK    GeneRIF: CircNRCAM up-regulates NRCAM to promote papillary thyroid
            carcinoma progression.
REFERENCE   2  (residues 1 to 1210)
  AUTHORS   Zhou,L., He,L., Liu,C.H., Qiu,H., Zheng,L., Sample,K.M., Wu,Q.,
            Li,J., Xie,K., Ampuero,J., Li,Z., Lv,D., Liu,M., Romero-Gomez,M.,
            Hu,Y. and Tang,H.
  TITLE     Liver cancer stem cell dissemination and metastasis: uncovering the
            role of NRCAM in hepatocellular carcinoma
  JOURNAL   J Exp Clin Cancer Res 42 (1), 311 (2023)
   PUBMED   37993901
  REMARK    GeneRIF: Liver cancer stem cell dissemination and metastasis:
            uncovering the role of NRCAM in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1210)
  AUTHORS   Sannes,A.C., Christensen,J.O., Nielsen,M.B. and Gjerstad,J.
  TITLE     Stress-induced headache in the general working population is
            moderated by the NRCAM rs2300043 genotype
  JOURNAL   Scand J Pain 23 (2), 326-332 (2022)
   PUBMED   36181733
  REMARK    GeneRIF: Stress-induced headache in the general working population
            is moderated by the NRCAM rs2300043 genotype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1210)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 1210)
  AUTHORS   Bai,C. and Chen,D.G.
  TITLE     NRCAM acts as a prognostic biomarker and promotes the tumor
            progression in gastric cancer via EMT pathway
  JOURNAL   Tissue Cell 77, 101859 (2022)
   PUBMED   35763884
  REMARK    GeneRIF: NRCAM acts as a prognostic biomarker and promotes the
            tumor progression in gastric cancer via EMT pathway.
REFERENCE   6  (residues 1 to 1210)
  AUTHORS   Wang,B., Williams,H., Du,J.S., Terrett,J. and Kenwrick,S.
  TITLE     Alternative splicing of human NrCAM in neural and nonneural tissues
  JOURNAL   Mol Cell Neurosci 10 (5-6), 287-295 (1998)
   PUBMED   9604207
REFERENCE   7  (residues 1 to 1210)
  AUTHORS   Grumet,M.
  TITLE     Nr-CAM: a cell adhesion molecule with ligand and receptor functions
  JOURNAL   Cell Tissue Res 290 (2), 423-428 (1997)
   PUBMED   9321706
  REMARK    Review article
REFERENCE   8  (residues 1 to 1210)
  AUTHORS   Sakurai,T., Lustig,M., Nativ,M., Hemperly,J.J., Schlessinger,J.,
            Peles,E. and Grumet,M.
  TITLE     Induction of neurite outgrowth through contactin and Nr-CAM by
            extracellular regions of glial receptor tyrosine phosphatase beta
  JOURNAL   J Cell Biol 136 (4), 907-918 (1997)
   PUBMED   9049255
REFERENCE   9  (residues 1 to 1210)
  AUTHORS   Volkmer,H., Leuschner,R., Zacharias,U. and Rathjen,F.G.
  TITLE     Neurofascin induces neurites by heterophilic interactions with
            axonal NrCAM while NrCAM requires F11 on the axonal surface to
            extend neurites
  JOURNAL   J Cell Biol 135 (4), 1059-1069 (1996)
   PUBMED   8922386
REFERENCE   10 (residues 1 to 1210)
  AUTHORS   Lane,R.P., Chen,X.N., Yamakawa,K., Vielmetter,J., Korenberg,J.R.
            and Dreyer,W.J.
  TITLE     Characterization of a highly conserved human homolog to the chicken
            neural cell surface protein Bravo/Nr-CAM that maps to chromosome
            band 7q31
  JOURNAL   Genomics 35 (3), 456-465 (1996)
   PUBMED   8812479
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005058.1, AC007567.2 and
            AC005683.2.
            
            Summary: Cell adhesion molecules (CAMs) are members of the
            immunoglobulin superfamily. This gene encodes a neuronal cell
            adhesion molecule with multiple immunoglobulin-like C2-type domains
            and fibronectin type-III domains. This ankyrin-binding protein is
            involved in neuron-neuron adhesion and promotes directional
            signaling during axonal cone growth. This gene is also expressed in
            non-neural tissues and may play a general role in cell-cell
            communication via signaling from its intracellular domain to the
            actin cytoskeleton during directional cell migration. Allelic
            variants of this gene have been associated with autism and
            addiction vulnerability. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1210
                     /product="neuronal cell adhesion molecule isoform Q
                     precursor"
                     /note="NgCAM-related cell adhesion molecule; neuronal
                     surface protein Bravo"
                     /calculated_mol_wt=130460
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3315
     Region          46..140
                     /region_name="IgI_NrCAM"
                     /note="Immunoglobulin (Ig)-like domain of NrCAM (Ng
                     (neuronglia) CAM-related cell adhesion molecule); member
                     of the I-set of Ig superfamily (IgSF) domains; cd05874"
                     /db_xref="CDD:409458"
     Region          46..50
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409458"
     Region          55..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409458"
     Region          64..71
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409458"
     Region          77..82
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409458"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          85..87
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409458"
     Region          94..97
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409458"
     Region          102..106
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409458"
     Region          119..127
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409458"
     Region          130..140
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409458"
     Region          149..238
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          163..167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          177..181
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          200..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          215..220
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          231..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            245
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            251
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            275
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          276..357
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          287..291
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          300..304
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            313
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          322..326
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          336..341
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          349..352
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          361..449
                     /region_name="Ig4_NrCAM"
                     /note="Fourth immunoglobulin (Ig)-like domain of NrCAM
                     (NgCAM-related cell adhesion molecule); cd05868"
                     /db_xref="CDD:409454"
     Region          377..381
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409454"
     Region          390..394
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409454"
     Region          414..418
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409454"
     Region          428..433
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409454"
     Site            432
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          441..444
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409454"
     Region          458..541
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          471..475
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          484..488
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            506
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          507..511
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          521..526
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          534..537
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          545..1059
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            618
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          646..736
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(646,712,727)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            715
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            order(728..729,731..732)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            801
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            857
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            992
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1008
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1018
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          1097..1186
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     CDS             1..1210
                     /gene="NRCAM"
                     /gene_synonym="NEDNMS"
                     /coded_by="NM_001371127.1:526..4158"
                     /note="isoform Q precursor is encoded by transcript
                     variant 46"
                     /db_xref="GeneID:4897"
                     /db_xref="HGNC:HGNC:7994"
                     /db_xref="MIM:601581"
ORIGIN      
        1 mqlkimpkkk rlsagrvpli lflcqmisal evpldpklle dlvqpptitq qspkdyiidp
       61 reniviqcea kgkpppsfsw trngthfdid kdplvtmkpg tgtliinims egkaetyegv
      121 yqctarnerg aavsnnivvr psrsplwtke klepitlqsg qslvlpcrpp iglpppiifw
      181 mdnsfqrlpq servsqglng dlyfsnvlpe dtredyicya rfnhtqtiqq kqpisvkvis
      241 vdelndtiaa nlsdtefyak ssrerpptfl tpegnasnke elrgnvlsle ciaeglptpi
      301 iywakedgml pknrtvyknf ektlqiihvs eadsgnyqci aknalgaihh tisvrvkaap
      361 ywitapqnlv lspgedgtli crangnpkpr iswltngvpi eiapddpsrk idgdtiifsn
      421 vqerssavyq cnasneygyl lanafvnvla eppriltpan tlyqvianrp alldcaffgs
      481 plptiewfkg akgsalhedi yvlhengtle ipvaqkdstg tytcvarnkl gmaknevhle
      541 ikdptwivkq peyavvqrgs mvsfeckvkh dhtlsltvlw lkdnrelpsd erftvdkdhl
      601 vvadvsddds gtytcvantt ldsvsasavl svvaptptpa pvydvpnppf dleltdqldk
      661 svqlswtpgd dnnspitkfi ieyedamhkp glwhhqtevs gtqttaqlkl spyvnysfrv
      721 mavnsigksl pseaseqylt kasepdknpt aveglgsepd nlvitwkpln gfesngpglq
      781 ykvswrqkdg ddewtsvvva nvskyivsgt ptfvpylikv qalndmgfap epavvmghsg
      841 edlpmvapgn vrvnvvnstl aevhwdpvpl ksirghlqgy riyywktqss skrnrrhiek
      901 kiltfqgskt hgmlpglepf shytlnvrvv ngkgegpasp drvfntpegv psapsslkiv
      961 nptldsltle wdppshpngi lteytlkyqp insthelgpl vdlkipankt rwtlknlnfs
     1021 trykfyfyaq tsagsgsqit eeavttvdea gilppdvgag kamasrqvdi atqgwfiglm
     1081 cavallilil livcfirrnk ggkypvkeke dahadpeiqp mkeddgtfge ysdaedhkpl
     1141 kkgsrtpsdr tvkkedsdds lvdygegvng qfnedgsfig qysgkkekep aegnesseap
     1201 spvnamnsfv
//
LOCUS       NP_001362214             140 aa            linear   PRI 21-NOV-2025
DEFINITION  alpha-synuclein isoform NACP140 [Homo sapiens].
ACCESSION   NP_001362214
VERSION     NP_001362214.1
DBSOURCE    REFSEQ: accession NM_001375285.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Aggarwal,L., Karmakar,S. and Biswas,P.
  TITLE     Differentially heterogeneous hydration environment of the familial
            mutants of alpha-synuclein
  JOURNAL   J Chem Phys 161 (15) (2024)
   PUBMED   39412059
  REMARK    GeneRIF: Differentially heterogeneous hydration environment of the
            familial mutants of alpha-synuclein.
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Kametani,F., Tahira,M., Takao,M., Matsubara,T., Hasegawa,K.,
            Yoshida,M., Saito,Y., Murayama,S. and Hasegawa,M.
  TITLE     Analysis and comparison of post-translational modifications of
            alpha-synuclein filaments in multiple system atrophy and dementia
            with Lewy bodies
  JOURNAL   Sci Rep 14 (1), 22892 (2024)
   PUBMED   39358446
  REMARK    GeneRIF: Analysis and comparison of post-translational
            modifications of alpha-synuclein filaments in multiple system
            atrophy and dementia with Lewy bodies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Xia,P., Cao,Y., Zhao,Q. and Li,H.
  TITLE     Energy gap of conformational transition related with temperature
            for the NACore of alpha-synuclein
  JOURNAL   Phys Chem Chem Phys 26 (35), 23062-23072 (2024)
   PUBMED   39175373
  REMARK    GeneRIF: Energy gap of conformational transition related with
            temperature for the NACore of alpha-synuclein.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Tripathi,A., Alnakhala,H., Brontesi,L., Selkoe,D. and Dettmer,U.
  TITLE     RXR nuclear receptor signaling modulates lipid metabolism and
            triggers lysosomal clearance of alpha-synuclein in neuronal models
            of synucleinopathy
  JOURNAL   Cell Mol Life Sci 81 (1), 362 (2024)
   PUBMED   39162859
  REMARK    GeneRIF: RXR nuclear receptor signaling modulates lipid metabolism
            and triggers lysosomal clearance of alpha-synuclein in neuronal
            models of synucleinopathy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Martins,G.F. and Galamba,N.
  TITLE     Wild-Type alpha-Synuclein Structure and Aggregation: A
            Comprehensive Coarse-Grained and All-Atom Molecular Dynamics Study
  JOURNAL   J Chem Inf Model 64 (15), 6115-6131 (2024)
   PUBMED   39046235
  REMARK    GeneRIF: Wild-Type alpha-Synuclein Structure and Aggregation: A
            Comprehensive Coarse-Grained and All-Atom Molecular Dynamics Study.
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Spillantini,M.G., Divane,A. and Goedert,M.
  TITLE     Assignment of human alpha-synuclein (SNCA) and beta-synuclein
            (SNCB) genes to chromosomes 4q21 and 5q35
  JOURNAL   Genomics 27 (2), 379-381 (1995)
   PUBMED   7558013
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Chen,X., de Silva,H.A., Pettenati,M.J., Rao,P.N., St
            George-Hyslop,P., Roses,A.D., Xia,Y., Horsburgh,K., Ueda,K. and
            Saitoh,T.
  TITLE     The human NACP/alpha-synuclein gene: chromosome assignment to
            4q21.3-q22 and TaqI RFLP analysis
  JOURNAL   Genomics 26 (2), 425-427 (1995)
   PUBMED   7601479
REFERENCE   8  (residues 1 to 140)
  AUTHORS   Campion,D., Martin,C., Heilig,R., Charbonnier,F., Moreau,V.,
            Flaman,J.M., Petit,J.L., Hannequin,D., Brice,A. and Frebourg,T.
  TITLE     The NACP/synuclein gene: chromosomal assignment and screening for
            alterations in Alzheimer disease
  JOURNAL   Genomics 26 (2), 254-257 (1995)
   PUBMED   7601450
REFERENCE   9  (residues 1 to 140)
  AUTHORS   Ueda,K., Saitoh,T. and Mori,H.
  TITLE     Tissue-dependent alternative splicing of mRNA for NACP, the
            precursor of non-A beta component of Alzheimer's disease amyloid
  JOURNAL   Biochem Biophys Res Commun 205 (2), 1366-1372 (1994)
   PUBMED   7802671
REFERENCE   10 (residues 1 to 140)
  AUTHORS   Morris,H. and Lim,S.Y.
  TITLE     Monogenic Parkinson Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301402
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093759.3 and AC097478.2.
            
            Summary: Alpha-synuclein is a member of the synuclein family, which
            also includes beta- and gamma-synuclein. Synucleins are abundantly
            expressed in the brain and alpha- and beta-synuclein inhibit
            phospholipase D2 selectively. SNCA may serve to integrate
            presynaptic signaling and membrane trafficking. Defects in SNCA
            have been implicated in the pathogenesis of Parkinson disease. SNCA
            peptides are a major component of amyloid plaques in the brains of
            patients with Alzheimer's disease. Alternatively spliced
            transcripts encoding different isoforms have been identified for
            this gene. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (5), as well as variants 1-3 and
            6-8, encodes isoform NACP140.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.574798.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2145743,
                                           SAMEA2149004 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q22.1"
     Protein         1..140
                     /product="alpha-synuclein isoform NACP140"
                     /note="non A-beta component of AD amyloid; synuclein
                     alpha-140; synuclein, alpha (non A4 component of amyloid
                     precursor); I+/--synuclein"
                     /calculated_mol_wt=14329
     Region          1..131
                     /region_name="Synuclein"
                     /note="pfam01387"
                     /db_xref="CDD:460186"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:22407793; propagated from
                     UniProtKB/Swiss-Prot (P37840.1)"
     Region          20..67
                     /region_name="4 X 11 AA tandem repeats of
                     [EGS]-K-T-K-[EQ]-[GQ]-V-X(4)"
                     /note="propagated from UniProtKB/Swiss-Prot (P37840.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10617630; propagated from
                     UniProtKB/Swiss-Prot (P37840.1)"
     Region          100..140
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P37840.1)"
     Region          111..140
                     /region_name="Interaction with SERF1A.
                     /evidence=ECO:0000269|PubMed:22854022"
                     /note="propagated from UniProtKB/Swiss-Prot (P37840.1)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by FYN.
                     /evidence=ECO:0000269|PubMed:11162638,
                     ECO:0000269|PubMed:12893833; propagated from
                     UniProtKB/Swiss-Prot (P37840.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by BARK1, PLK2, CK2, CK1 and GRK5.
                     /evidence=ECO:0000269|PubMed:10617630,
                     ECO:0000269|PubMed:11813001, ECO:0000269|PubMed:24936070;
                     propagated from UniProtKB/Swiss-Prot (P37840.1)"
     CDS             1..140
                     /gene="SNCA"
                     /gene_synonym="NACP; PARK1; PARK4; PD1"
                     /coded_by="NM_001375285.1:148..570"
                     /note="isoform NACP140 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS3634.1"
                     /db_xref="GeneID:6622"
                     /db_xref="HGNC:HGNC:11138"
                     /db_xref="MIM:163890"
ORIGIN      
        1 mdvfmkglsk akegvvaaae ktkqgvaeaa gktkegvlyv gsktkegvvh gvatvaektk
       61 eqvtnvggav vtgvtavaqk tvegagsiaa atgfvkkdql gkneegapqe giledmpvdp
      121 dneayempse egyqdyepea
//
LOCUS       NP_001382239            2270 aa            linear   PRI 21-NOV-2025
DEFINITION  myomegalin isoform 29 [Homo sapiens].
ACCESSION   NP_001382239
VERSION     NP_001382239.1
DBSOURCE    REFSEQ: accession NM_001395310.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2270)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2270)
  AUTHORS   Pan,R., Dai,J., Liang,W., Wang,H., Ye,L., Ye,S., Lin,Z., Huang,S.,
            Xiong,Y., Zhang,L., Lu,L., Wang,O., Shen,X., Liao,W. and Lu,X.
  TITLE     PDE4DIP contributes to colorectal cancer growth and chemoresistance
            through modulation of the NF1/RAS signaling axis
  JOURNAL   Cell Death Dis 14 (6), 373 (2023)
   PUBMED   37355626
  REMARK    GeneRIF: PDE4DIP contributes to colorectal cancer growth and
            chemoresistance through modulation of the NF1/RAS signaling axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2270)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   4  (residues 1 to 2270)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 2270)
  AUTHORS   Abou Ziki,M.D., Bhat,N., Neogi,A., Driscoll,T.P., Ugwu,N., Liu,Y.,
            Smith,E., Abboud,J.M., Chouairi,S., Schwartz,M.A., Akar,J.G. and
            Mani,A.
  TITLE     Epistatic interaction of PDE4DIP and DES mutations in familial
            atrial fibrillation with slow conduction
  JOURNAL   Hum Mutat 42 (10), 1279-1293 (2021)
   PUBMED   34289528
  REMARK    GeneRIF: Epistatic interaction of PDE4DIP and DES mutations in
            familial atrial fibrillation with slow conduction.
REFERENCE   6  (residues 1 to 2270)
  AUTHORS   Shimada,H., Kuboshima,M., Shiratori,T., Nabeya,Y., Takeuchi,A.,
            Takagi,H., Nomura,F., Takiguchi,M., Ochiai,T. and Hiwasa,T.
  TITLE     Serum anti-myomegalin antibodies in patients with esophageal
            squamous cell carcinoma
  JOURNAL   Int J Oncol 30 (1), 97-103 (2007)
   PUBMED   17143517
  REMARK    GeneRIF: MMGL-antibody is significantly with a favorable prognosis.
            Consequently, MMGL-anatibodies may be a useful tumor marker to
            diagnose and establish a prognosis in patients with esophageal
            squamous cell carcinoma.
REFERENCE   7  (residues 1 to 2270)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 2270)
  AUTHORS   Soejima,H., Kawamoto,S., Akai,J., Miyoshi,O., Arai,Y., Morohka,T.,
            Matsuo,S., Niikawa,N., Kimura,A., Okubo,K. and Mukai,T.
  TITLE     Isolation of novel heart-specific genes using the BodyMap database
  JOURNAL   Genomics 74 (1), 115-120 (2001)
   PUBMED   11374908
REFERENCE   9  (residues 1 to 2270)
  AUTHORS   Verde,I., Pahlke,G., Salanova,M., Zhang,G., Wang,S., Coletti,D.,
            Onuffer,J., Jin,S.L. and Conti,M.
  TITLE     Myomegalin is a novel protein of the golgi/centrosome that
            interacts with a cyclic nucleotide phosphodiesterase
  JOURNAL   J Biol Chem 276 (14), 11189-11198 (2001)
   PUBMED   11134006
REFERENCE   10 (residues 1 to 2270)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC245389.1, AC239802.3 and
            AC239804.2.
            
            Summary: The protein encoded by this gene serves to anchor
            phosphodiesterase 4D to the Golgi/centrosome region of the cell.
            Defects in this gene may be a cause of myeloproliferative disorder
            (MBD) associated with eosinophilia. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..2270
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     Protein         1..2270
                     /product="myomegalin isoform 29"
                     /note="myomegalin; cardiomyopathy-associated protein 2"
                     /calculated_mol_wt=257503
     Region          69..745
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          72..139
                     /region_name="Cnn_1N"
                     /note="Centrosomin N-terminal motif 1; pfam07989"
                     /db_xref="CDD:462333"
     Region          454..1177
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1618..1687
                     /region_name="Olduvai"
                     /note="Olduvai domain; pfam06758"
                     /db_xref="CDD:429104"
     Region          <1845..>2022
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..2270
                     /gene="PDE4DIP"
                     /gene_synonym="CMYA2; MMGL"
                     /coded_by="NM_001395310.1:267..7079"
                     /note="isoform 29 is encoded by transcript variant 29"
                     /db_xref="GeneID:9659"
                     /db_xref="HGNC:HGNC:15580"
                     /db_xref="MIM:608117"
ORIGIN      
        1 meqtwtrdyf aeddgemvpr tshtaaflsd tkdrgppvqs qiwrsgekvp fvqtyslraf
       61 ekppqvqtqa lrdfekhlnd lkkenfslkl riyfleermq qkyeasredi ykrnielkve
      121 veslkrelqd kkqhldktwa dvenlnsqne aelrrqfeer qqetehvyel lenkiqllqe
      181 esrlakneaa rmaalveaek ecnlelsekl kgvtknwedv pgdqvkpdqy tealaqrdkr
      241 ieelnqslaa qerlveqlsr ekqqllhlle eptsmevqpm teellkqqkl nshettitqq
      301 svsdshlael qekiqqteat nkilqeklne msyelkcaqe ssqkqdgtiq nlketlksre
      361 reteelyqvi egqndtmakl remlhqsqlg qlhssegtsp aqqqvalldl qsalfcsqle
      421 iqklqrvvrq kerqladakq cvqfveaaah eseqqkeasw khnqelrkal qqlqeelqnk
      481 sqqlraweae kyneirtqeq niqhlnhsls hkeqllqefr ellqyrdnsd ktleanemll
      541 eklrqrihdk avaleraide kfsaleekek elrqlrlavr erdhdlerlr dvlssneatm
      601 qsmesllrak gleveqlstt cqnlqwlkee metkfsrwqk eqesiiqqlq tslhdrnkev
      661 edlsatllck lgpgqseiae elcqrlqrke rmlqdllsdr nkqvleheme iqgllqsvst
      721 reqesqaaae klvqalmern selqalrqyl ggrdslmsqa pisnqqaevt ptgrlgkqtd
      781 qgsmqipsrd dstsltaked vsiprstlgd ldtvagleke lsnakeelel makkeresqm
      841 elsalqsmma vqeeelqvqa admesltrni qikedlikdl qmqlvdpedi pamerltqev
      901 lllrekvasv esqgqeisgn rrqqlllmle glvdersrln ealqaerqly sslvkfhahp
      961 esserdrtlq velegaqvlr srleevlgrs lerlnrletl aaiggaaagd dtedtsteft
     1021 dsieeeaahh shqqlvkval ekslatvetq npsfsppspm ggdsnrclqe emlhlraefh
     1081 qhleekrkae eelkelkaqi eeagfssvsh irntmlslcl enaelkeqmg eamsdgweie
     1141 edkekgevmv etvvtkegls esslqaefrk lqgklknahn iinllkeqlv lsskegnskl
     1201 tpellvhlts tierintelv gspgkhqhqe egnvtvrpfp rpqsldlgat ftvdahqldn
     1261 qsqprdpgpq safslpgstq hlrsqlsqck qryqdlqekl llseatvfaq anelekyrvm
     1321 ltgeslvkqd skqiqvdlqd lgyetcgrse neaereetts peceehnslk emvlmeglcs
     1381 eqgrrgstla ssserkplen qlgkqeefrv ygksenilvl rkdikdlkaq lqnankviqn
     1441 lksrvrslsv tsdysssler prklravgtl egssphsvpd edegwlsdgt gafyspglqa
     1501 kkdlesliqr vsqleaqlpk ngleeklaee lrsaswpgky dsliqdqare lsylrqkire
     1561 grgicylitr hakdtvksfe dllrsndidy ylgqsfreql aqgsqlterl tsklstkdhk
     1621 sekdqaglep lalrlsrelq ekekvievlq akldarsltp ssshalsdsh rspsstsfls
     1681 deleacsdmd ivseythyee kkaspshsds ihhsshsavl sskpsstsas qgakaesnsn
     1741 pislptpqnt pkeanqahsg astvppasta tllsndlead ssyylnsaqp hspprgtiel
     1801 grilepgylg ssgkwdvmrp qkgsvsgdls sgssvyqlns kptgadllee hlgeirnlrq
     1861 rleesicind rlreqlehrl tstargrgst snfysqgles ipqlcnenrv lrednrrlqa
     1921 qlshvsrehs qeteslreal lssrshlqel ekelehqkve rqqlledlre kqqevlhfre
     1981 erlslqends rlqhklvllq qqceekqqlf eslqselqiy ealygnskkg lkdsavsppv
     2041 rdvgmnspal vfpssasstp gsetpiinra nglgldtspv mktppklegd atdgsfankh
     2101 grhvighidd ysalrqqiae gkllvkkivs lvrsacsfpg leaqgtevlg skgihelrss
     2161 tsalhhalee saslltmfwr aalpsthipv lpgkvgeste rellelrtkv skqerllqst
     2221 tehlknanqq kesmeqfivs qltrthdvlk kartnlevks lralpctpal
//
LOCUS       NP_001364066            1860 aa            linear   PRI 21-NOV-2025
DEFINITION  Golgi-specific brefeldin A-resistance guanine nucleotide exchange
            factor 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001364066 XP_005270318
VERSION     NP_001364066.1
DBSOURCE    REFSEQ: accession NM_001377137.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1860)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1860)
  AUTHORS   Hirano,J., Hayashi,T., Kitamura,K., Nishimura,Y., Shimizu,H.,
            Okamoto,T., Okada,K., Uemura,K., Yeh,M.T., Ono,C., Taguwa,S.,
            Muramatsu,M. and Matsuura,Y.
  TITLE     Enterovirus 3A protein disrupts endoplasmic reticulum homeostasis
            through interaction with GBF1
  JOURNAL   J Virol 98 (7), e0081324 (2024)
   PUBMED   38904364
  REMARK    GeneRIF: Enterovirus 3A protein disrupts endoplasmic reticulum
            homeostasis through interaction with GBF1.
REFERENCE   3  (residues 1 to 1860)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1860)
  AUTHORS   Navare,A.T., Mast,F.D., Olivier,J.P., Bertomeu,T., Neal,M.L.,
            Carpp,L.N., Kaushansky,A., Coulombe-Huntington,J., Tyers,M. and
            Aitchison,J.D.
  TITLE     Viral protein engagement of GBF1 induces host cell vulnerability
            through synthetic lethality
  JOURNAL   J Cell Biol 221 (11) (2022)
   PUBMED   36305789
  REMARK    GeneRIF: Viral protein engagement of GBF1 induces host cell
            vulnerability through synthetic lethality.
REFERENCE   5  (residues 1 to 1860)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1860)
  AUTHORS   Garcia-Mata,R. and Sztul,E.
  TITLE     The membrane-tethering protein p115 interacts with GBF1, an ARF
            guanine-nucleotide-exchange factor
  JOURNAL   EMBO Rep 4 (3), 320-325 (2003)
   PUBMED   12634853
  REMARK    GeneRIF: novel interaction between p115 and Golgi-specific
            brefeldin-A-resistant factor 1 (GBF1)
REFERENCE   7  (residues 1 to 1860)
  AUTHORS   Kawamoto,K., Yoshida,Y., Tamaki,H., Torii,S., Shinotsuka,C.,
            Yamashina,S. and Nakayama,K.
  TITLE     GBF1, a guanine nucleotide exchange factor for ADP-ribosylation
            factors, is localized to the cis-Golgi and involved in membrane
            association of the COPI coat
  JOURNAL   Traffic 3 (7), 483-495 (2002)
   PUBMED   12047556
  REMARK    GeneRIF: detailed subcellular localization to the cis-Golgi
REFERENCE   8  (residues 1 to 1860)
  AUTHORS   Verhoeven,K., Villanova,M., Rossi,A., Malandrini,A., De Jonghe,P.
            and Timmerman,V.
  TITLE     Localization of the gene for the intermediate form of
            Charcot-Marie-Tooth to chromosome 10q24.1-q25.1
  JOURNAL   Am J Hum Genet 69 (4), 889-894 (2001)
   PUBMED   11533914
REFERENCE   9  (residues 1 to 1860)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   10 (residues 1 to 1860)
  AUTHORS   Mansour,S.J., Herbrick,J.A., Scherer,S.W. and Melancon,P.
  TITLE     Human GBF1 is a ubiquitously expressed gene of the sec7 domain
            family mapping to 10q24
  JOURNAL   Genomics 54 (2), 323-327 (1998)
   PUBMED   9828135
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160011.35, AL356420.14 and
            AL121928.13.
            
            On Dec 17, 2019 this sequence version replaced XP_005270318.1.
            
            Summary: This gene encodes a member of the Sec7 domain family. The
            encoded protein is a guanine nucleotide exchange factor that
            regulates the recruitment of proteins to membranes by mediating GDP
            to GTP exchange. The encoded protein is localized to the Golgi
            apparatus and plays a role in vesicular trafficking by activating
            ADP ribosylation factor 1. The encoded protein has also been
            identified as an important host factor for viral replication.
            Multiple transcript variants have been observed for this gene.
            [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (4) encodes the longest isoform
            (4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3449445.1,
                                           SRR14038192.1872814.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369983.5/ ENSP00000359000.4
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1860
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..1860
                     /product="Golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1 isoform 4"
                     /note="golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1; BFA-resistant GEF 1"
                     /calculated_mol_wt=206444
     Region          1..381
                     /region_name="Interaction with RAB1B.
                     /evidence=ECO:0000269|PubMed:17429068"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1..211
                     /region_name="DCB, DCB:DCB domain and DCB:HUS domain
                     interaction. /evidence=ECO:0000250|UniProtKB:Q9R1D7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          215..266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          281..372
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          <430..>1179
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          531..551
                     /region_name="HUS, DCB:HUS domain interaction.
                     /evidence=ECO:0000250|UniProtKB:Q9R1D7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          620..666
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            663
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          700..885
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          887..1371
                     /region_name="Phosphatidylinositol-phosphate binding,
                     required for translocation to the leading edge and for
                     ARF1 activation upon GPCR signaling.
                     /evidence=ECO:0000269|PubMed:22573891"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1285..1336
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1317
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1338
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AMPK.
                     /evidence=ECO:0000269|PubMed:18063581; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1351..1371
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1431..1484
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1726..1809
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1774
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1785
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          <1795..1858
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1860
                     /gene="GBF1"
                     /gene_synonym="ARF1GEF; CMT2GG; CMTDI2; CMTDIA"
                     /coded_by="NM_001377137.1:261..5843"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS91331.1"
                     /db_xref="GeneID:8729"
                     /db_xref="HGNC:HGNC:4181"
                     /db_xref="MIM:603698"
ORIGIN      
        1 mvdkniyiiq geinivvgai krnarwstht pldeerdpll hsfghlkevl nsitelseie
       61 pnvflrpfle virsedttgp itglaltsvn kflsyalidp thegtaegme nmadavthar
      121 fvgtdpasde vvlmkilqvl rtllltpvga hltnesvcei mqscfricfe mrlsellrks
      181 aehtlvdmvq llftrlpqfk eepknyvgtn mkklkmragg msdsskwkkq krsprpprhm
      241 tkvtpgselp tpngttlssn ltggmpfidv ptpissasse aasavvspst dsglefssqt
      301 tskedltdle qpgspgysta tepgsselgv peqpdlqqeg thveksqsas vesipevlee
      361 ctspadhsds asvhdmdyvn prgvrftqss qkegtalvpy glpcirelfr flisltnphd
      421 rhnsevmihm glhlltvale sapvaqcqtl lglikdemcr hlfqllsier lnlyaaslrv
      481 cfllfesmre hlkfqmemyi kklmeiitve npkmpyemke maleaivqlw ripsfvtely
      541 inydcdyycs nlfeeltkll sknafpvsgq lytthllsld alltvidste ahcqakvlns
      601 ltqqekketa rpsceivdgt reasnterta sdgkavgmas dipglhlpgg grlppehgks
      661 gcsdleeavd sgadkkfark pprfscllpd prelieiknk kkllitgteq fnqkpkkgiq
      721 flqekgllti pmdntevaqw lrenprldkk migefvsdrk nidllesfvs tfsfqglrld
      781 ealrlyleaf rlpgeapviq rlleafterw mncngspfan sdacfslaya vimlntdqhn
      841 hnvrkqnapm tleefrknlk gvnggkdfeq diledmyhai kneeivmpee qtglvrenyv
      901 wnvllhrgat pegiflrvpt asydldlftm twgptiaals yvfdksleet iiqkaisgfr
      961 kcamisahyg lsdvfdnlii slckftalss esienlpsvf gsnpkahiaa ktvfhlahrh
     1021 gdilregwkn imeamlqlfr aqllpkamie vedfvdpngk islqreetps nrgestvlsf
     1081 vswltlsgpe qssvrgpste nqeakrvale cikqcdpekm iteskflqle slqelmkalv
     1141 svtpdeetyd eedaafclem llrivlenrd rvgcvwqtvr dhlyhlcvqa qdfcflvera
     1201 vvgllrlair llrreeisaq vllslrilll mkpsvlsrvs hqvayglhel lktnaanihs
     1261 gddwatlftl lecigsgvkp paalqatara dapdagaqsd selpsyhqnd vsldrgytsd
     1321 sevytdhgrp gkihrsatda dvvnsgwlvv gkddvdnskp gpsrpgpspl inqysltvgl
     1381 dlgphdtksl lkcveslsfi vrdaahitpd nfelcvktlr ifveaslngg cksqekrgks
     1441 hkydskgnrf kkkskegsml rrprtssqha srggqsddde degvpasyht vslqvsqdll
     1501 dlmhtlhtra asiysswaee qrhletggqk ieadsrtlwa hcwcpllqgi aclccdarrq
     1561 vrmqaltylq rallvhdlqk ldalewescf nkvlfplltk llenispadv ggmeetrmra
     1621 stllskvflq hlspllslst faalwltild fmdkymhags sdllseaipe slknmllvmd
     1681 taeifhsada rgggpsalwe itweridcfl phlrdelfkq tviqdpmpme pqgqkplasa
     1741 hltsaagdtr tpghppppei pselgacdfe kpespraass sspgspvass psrlsptpdg
     1801 ppplaqppli lqplasplqv gvppmtlpii lnpalieats pvpllatprp tdpiptsevn
//
LOCUS       NP_001372246             679 aa            linear   PRI 21-NOV-2025
DEFINITION  receptor-type tyrosine-protein phosphatase alpha isoform 11 [Homo
            sapiens].
ACCESSION   NP_001372246
VERSION     NP_001372246.1
DBSOURCE    REFSEQ: accession NM_001385317.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 679)
  AUTHORS   Fang,J., Zhang,Y., Huang,C., Lu,R., Yu,J., Chen,R., Wang,Y.,
            Zhao,X., Yu,J. and Huang,J.
  TITLE     Glucose-mediated N-glycosylation of RPTPalpha affects its
            subcellular localization and Src activation
  JOURNAL   Oncogene 42 (14), 1058-1071 (2023)
   PUBMED   36765146
  REMARK    GeneRIF: Glucose-mediated N-glycosylation of RPTPalpha affects its
            subcellular localization and Src activation.
REFERENCE   3  (residues 1 to 679)
  AUTHORS   Hill,M.A., Bentley,S.R., Walker,T.L., Mellick,G.D., Wood,S.A. and
            Sykes,A.M.
  TITLE     Does a rare mutation in PTPRA contribute to the development of
            Parkinson's disease in an Australian multi-incident family?
  JOURNAL   PLoS One 17 (7), e0271499 (2022)
   PUBMED   35900966
  REMARK    GeneRIF: Does a rare mutation in PTPRA contribute to the
            development of Parkinson's disease in an Australian multi-incident
            family?
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 679)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 679)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 679)
  AUTHORS   Zheng,X.M., Wang,Y. and Pallen,C.J.
  TITLE     Cell transformation and activation of pp60c-src by overexpression
            of a protein tyrosine phosphatase
  JOURNAL   Nature 359 (6393), 336-339 (1992)
   PUBMED   1383828
REFERENCE   7  (residues 1 to 679)
  AUTHORS   Rao,V.V., Loffler,C., Sap,J., Schlessinger,J. and Hansmann,I.
  TITLE     The gene for receptor-linked protein-tyrosine-phosphatase (PTPA) is
            assigned to human chromosome 20p12-pter by in situ hybridization
            (ISH and FISH)
  JOURNAL   Genomics 13 (3), 906-907 (1992)
   PUBMED   1639427
REFERENCE   8  (residues 1 to 679)
  AUTHORS   Jirik,F.R., Anderson,L.L. and Duncan,A.M.
  TITLE     The human protein-tyrosine phosphatase PTP alpha/LRP gene (PTPA) is
            assigned to chromosome 20p13
  JOURNAL   Cytogenet Cell Genet 60 (2), 117-118 (1992)
   PUBMED   1611910
REFERENCE   9  (residues 1 to 679)
  AUTHORS   Kaplan,R., Morse,B., Huebner,K., Croce,C., Howk,R., Ravera,M.,
            Ricca,G., Jaye,M. and Schlessinger,J.
  TITLE     Cloning of three human tyrosine phosphatases reveals a multigene
            family of receptor-linked protein-tyrosine-phosphatases expressed
            in brain
  JOURNAL   Proc Natl Acad Sci U S A 87 (18), 7000-7004 (1990)
   PUBMED   2169617
REFERENCE   10 (residues 1 to 679)
  AUTHORS   Sap,J., D'Eustachio,P., Givol,D. and Schlessinger,J.
  TITLE     Cloning and expression of a widely expressed receptor tyrosine
            phosphatase
  JOURNAL   Proc Natl Acad Sci U S A 87 (16), 6112-6116 (1990)
   PUBMED   2166945
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL161656.20 and AL121905.23.
            
            Summary: The protein encoded by this gene is a member of the
            protein tyrosine phosphatase (PTP) family. PTPs are known to be
            signaling molecules that regulate a variety of cellular processes
            including cell growth, differentiation, mitotic cycle, and
            oncogenic transformation. This PTP contains an extracellular
            domain, a single transmembrane segment and two tandem
            intracytoplasmic catalytic domains, and thus represents a
            receptor-type PTP. This PTP has been shown to dephosphorylate and
            activate Src family tyrosine kinases, and is implicated in the
            regulation of integrin signaling, cell adhesion and proliferation.
            Three alternatively spliced variants of this gene, which encode two
            distinct isoforms, have been reported. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.383164.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..679
                     /product="receptor-type tyrosine-protein phosphatase alpha
                     isoform 11"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase, receptor type, alpha
                     polypeptide; PTPase-alpha; Leukocyte common
                     antigen-related peptide (protein tyrosine phosphate);
                     tyrosine phosphatase alpha; PTPLCA-related phosphatase;
                     receptor-type tyrosine-protein phosphatase alpha;
                     protein-tyrosine phosphatase alpha"
                     /calculated_mol_wt=77758
     Region          91..386
                     /region_name="R-PTPc-A-1"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase A, repeat 1; cd14621"
                     /db_xref="CDD:350469"
     Region          440..667
                     /region_name="R-PTPc-A-2"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase A, repeat 2; cd14623"
                     /db_xref="CDD:350471"
     CDS             1..679
                     /gene="PTPRA"
                     /gene_synonym="HEPTP; HLPR; HPTPA; HPTPalpha; LRP; PTPA;
                     PTPRL2; R-PTP-alpha; RPTPA"
                     /coded_by="NM_001385317.1:409..2448"
                     /note="isoform 11 is encoded by transcript variant 18"
                     /db_xref="GeneID:5786"
                     /db_xref="HGNC:HGNC:9664"
                     /db_xref="MIM:176884"
ORIGIN      
        1 mdswfilvll gsglicvsan nattdetpii avmvalssll vivfiiivly mlrfkkykqa
       61 gshsnsfrls ngrtedvepq svpllarsps tnrkypplpv dkleeeinrr maddnklfre
      121 efnalpacpi qatceaaske enkeknryvn ilpydhsrvh ltpvegvpds dyinasfing
      181 yqeknkfiaa qgpkeetvnd fwrmiweqnt ativmvtnlk erkeckcaqy wpdqgcwtyg
      241 nirvsvedvt vlvdytvrkf ciqqvgdmtn rkpqrlitqf hftswpdfgv pftpigmlkf
      301 lkkvkacnpq yagaivvhcs agvgrtgtfv vidamldmmh terkvdvygf vsriraqrcq
      361 mvqtdmqyvf iyqallehyl ygdtelevts lethlqkiyn kipgtsnngl eeefkkltsi
      421 kiqndkmrtg nlpanmkknr vlqiipyefn rviipvkrge entdyvnasf idgyrqkdsy
      481 iasqgpllht iedfwrmiwe wkscsivmlt eleergqekc aqywpsdglv sygditvelk
      541 keeecesytv rdllvtntre nksrqirqfh fhgwpevgip sdgkgmisii aavqkqqqqs
      601 gnhpitvhcs agagrtgtfc alstvlervk aegildvfqt vkslrlqrph mvqtleqyef
      661 cykvvqeyid afsdyanfk
//
LOCUS       NP_001339537             654 aa            linear   PRI 21-NOV-2025
DEFINITION  propionyl-CoA carboxylase alpha chain, mitochondrial isoform g
            [Homo sapiens].
ACCESSION   NP_001339537
VERSION     NP_001339537.1
DBSOURCE    REFSEQ: accession NM_001352608.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 654)
  AUTHORS   Wang,J., Cui,M., Liu,Y., Chen,M., Xu,J., Xia,J., Sun,J., Jiang,L.,
            Fang,W., Song,H. and Cheng,C.
  TITLE     The mitochondrial carboxylase PCCA interacts with Listeria
            monocytogenes phospholipase PlcB to modulate bacterial survival
  JOURNAL   Appl Environ Microbiol 90 (6), e0213523 (2024)
   PUBMED   38727222
  REMARK    GeneRIF: The mitochondrial carboxylase PCCA interacts with Listeria
            monocytogenes phospholipase PlcB to modulate bacterial survival.
REFERENCE   3  (residues 1 to 654)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 654)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 654)
  AUTHORS   Bychkov,I., Galushkin,A., Filatova,A., Nekrasov,A., Kurkina,M.,
            Baydakova,G., Ilyushkina,A., Skoblov,M. and Zakharova,E.
  TITLE     Functional Analysis of the PCCA and PCCB Gene Variants Predicted to
            Affect Splicing
  JOURNAL   Int J Mol Sci 22 (8), 4154 (2021)
   PUBMED   33923806
  REMARK    GeneRIF: Functional Analysis of the PCCA and PCCB Gene Variants
            Predicted to Affect Splicing.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 654)
  AUTHORS   Galarreta Aima,C.I., Shchelochkov,O.A., Jerves Serrano,T. and
            Venditti,C.P.
  TITLE     Propionic Acidemia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22593918
REFERENCE   7  (residues 1 to 654)
  AUTHORS   Kennerknecht,I., Klett,C. and Hameister,H.
  TITLE     Assignment of the human gene propionyl coenzyme A carboxylase,
            alpha-chain, (PCCA) to chromosome 13q32 by in situ hybridization
  JOURNAL   Genomics 14 (2), 550-551 (1992)
   PUBMED   1427880
REFERENCE   8  (residues 1 to 654)
  AUTHORS   Lamhonwah,A.M., Mahuran,D. and Gravel,R.A.
  TITLE     Human mitochondrial propionyl-CoA carboxylase: localization of the
            N-terminus of the pro- and mature alpha chains in the deduced
            primary sequence of a full-length cDNA
  JOURNAL   Nucleic Acids Res 17 (11), 4396 (1989)
   PUBMED   2740237
REFERENCE   9  (residues 1 to 654)
  AUTHORS   Lamhonwah,A.M., Quan,F. and Gravel,R.A.
  TITLE     Sequence homology around the biotin-binding site of human
            propionyl-CoA carboxylase and pyruvate carboxylase
  JOURNAL   Arch Biochem Biophys 254 (2), 631-636 (1987)
   PUBMED   3555348
REFERENCE   10 (residues 1 to 654)
  AUTHORS   Lamhonwah,A.M., Barankiewicz,T.J., Willard,H.F., Mahuran,D.J.,
            Quan,F. and Gravel,R.A.
  TITLE     Isolation of cDNA clones coding for the alpha and beta chains of
            human propionyl-CoA carboxylase: chromosomal assignments and DNA
            polymorphisms associated with PCCA and PCCB genes
  JOURNAL   Proc Natl Acad Sci U S A 83 (13), 4864-4868 (1986)
   PUBMED   3460076
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355338.33, AL356575.8,
            AL353697.21 and AL136526.27.
            
            Summary: The protein encoded by this gene is the alpha subunit of
            the heterodimeric mitochondrial enzyme Propionyl-CoA carboxylase.
            PCCA encodes the biotin-binding region of this enzyme. Mutations in
            either PCCA or PCCB (encoding the beta subunit) lead to an enzyme
            deficiency resulting in propionic acidemia. Multiple transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, May 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.5924.1,
                                           SRR1803612.269480.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q32.3"
     Protein         1..654
                     /product="propionyl-CoA carboxylase alpha chain,
                     mitochondrial isoform g"
                     /EC_number="6.4.1.3"
                     /note="propionyl Coenzyme A carboxylase, alpha
                     polypeptide; propionyl-CoA carboxylase alpha chain,
                     mitochondrial; PCCase alpha subunit; propanoyl-CoA:carbon
                     dioxide ligase alpha subunit; pccA complementation group;
                     propionyl-CoA carboxylase alpha subunit; propionyl CoA
                     carboxylase, alpha polypeptide"
                     /calculated_mol_wt=71426
     Region          37..438
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          451..579
                     /region_name="PCC_BT"
                     /note="Propionyl-coenzyme A carboxylase BT domain;
                     pfam18140"
                     /db_xref="CDD:465666"
     Region          587..653
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(610,619..621,628)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            620
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
     CDS             1..654
                     /gene="PCCA"
                     /coded_by="NM_001352608.2:29..1993"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="GeneID:5095"
                     /db_xref="HGNC:HGNC:8653"
                     /db_xref="MIM:232000"
ORIGIN      
        1 magfwvgtap lvaagrrgrw ppqqlmlsaa lrtlktfdki lvanrgeiac rvirtckkmg
       61 iktvaihsdv dassvhvkma deavcvgpap tsksylnmda imeaikktra qavhpgygfl
      121 senkefarcl aaedvvfigp dthaiqamgd kieskllakk aevntipgfd gvvkdaeeav
      181 riareigypv mikasagggg kgmriawdde etrdgfrlss qeaassfgdd rlliekfidn
      241 prhieiqvlg dkhgnalwln erecsiqrrn qkvveeapsi fldaetrram geqavalara
      301 vkyssagtve flvdskknfy flemntrlqd pyksfglpsi grlsqyqepl hlpgvrvdsg
      361 iqpgsdisiy ydpmisklit ygsdrtealk rmadaldnyv irgvthnial lreviinsrf
      421 vkgdistkfl sdvypdgfkg hmltkseknq llaiasslfv afqlraqhfq ensrmpvikp
      481 dianwelsvk lhdkvhtvva snngsvfsve vdgsklnvts twnlasplls vsvdgtqrtv
      541 qclsreaggn msiqflgtvy kvniltrlaa elnkfmlekv tedtssvlrs pmpgvvvavs
      601 vkpgdavaeg qeicvieamk mqnsmtagkt gtvksvhcqa gdtvgegdll vele
//
LOCUS       NP_001191232             677 aa            linear   PRI 21-NOV-2025
DEFINITION  amyloid-beta precursor protein isoform j precursor [Homo sapiens].
ACCESSION   NP_001191232
VERSION     NP_001191232.1
DBSOURCE    REFSEQ: accession NM_001204303.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Majernikova,N., Marmolejo-Garza,A., Salinas,C.S., Luu,M.D.A.,
            Zhang,Y., Trombetta-Lima,M., Tomin,T., Birner-Gruenberger,R.,
            Lehtonen,S., Koistinaho,J., Wolters,J.C., Ayton,S., den
            Dunnen,W.F.A. and Dolga,A.M.
  TITLE     The link between amyloid beta and ferroptosis pathway in
            Alzheimer's disease progression
  JOURNAL   Cell Death Dis 15 (10), 782 (2024)
   PUBMED   39468028
  REMARK    GeneRIF: The link between amyloid beta and ferroptosis pathway in
            Alzheimer's disease progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 677)
  AUTHORS   Munch,N.S., Das,S. and Seeger,S.
  TITLE     Unveiling the effect of CaCl2 on amyloid beta aggregation via
            supercritical angle Raman and fluorescence spectroscopy and
            microscopy
  JOURNAL   Phys Chem Chem Phys 26 (41), 26266-26276 (2024)
   PUBMED   39371012
  REMARK    GeneRIF: Unveiling the effect of CaCl2 on amyloid beta aggregation
            via supercritical angle Raman and fluorescence spectroscopy and
            microscopy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 677)
  AUTHORS   Tsoy,A., Umbayev,B., Kassenova,A., Kaupbayeva,B. and Askarova,S.
  TITLE     Pathology of Amyloid-beta (Abeta) Peptide Peripheral Clearance in
            Alzheimer's Disease
  JOURNAL   Int J Mol Sci 25 (20), 10964 (2024)
   PUBMED   39456746
  REMARK    GeneRIF: Pathology of Amyloid-beta (Abeta) Peptide Peripheral
            Clearance in Alzheimer's Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 677)
  AUTHORS   Soscia,S.J., Kirby,J.E., Washicosky,K.J., Tucker,S.M.,
            Ingelsson,M., Hyman,B., Burton,M.A., Goldstein,L.E., Duong,S.,
            Tanzi,R.E. and Moir,R.D.
  TITLE     The Alzheimer's disease-associated amyloid beta-protein is an
            antimicrobial peptide
  JOURNAL   PLoS One 5 (3), e9505 (2010)
   PUBMED   20209079
  REMARK    GeneRIF: Alzheimer's disease-associated amyloid beta-protein
            peptides display antimicrobial activity against C. albicans, E.
            coli, S. epidermidis, S. pneumoniae, S. aureus, L. monocytogenes,
            E. faecalis, and S. agalactiae.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 677)
  AUTHORS   Bird,T.D.
  TITLE     Early-Onset Familial Alzheimer Disease - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301414
REFERENCE   7  (residues 1 to 677)
  AUTHORS   Bird,T.D.
  TITLE     Alzheimer Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301340
REFERENCE   8  (residues 1 to 677)
  AUTHORS   Mant,R., Asherson,P., Gill,M., McGuffin,P., Owen,M., Wert,S.E.,
            Gregory,R.J., Smith,A.E., Cohn,J.A., Wilson,J.M. et al.
  TITLE     Schizophrenia scepticism
  JOURNAL   Nat Genet 2 (1), 12 (1992)
   PUBMED   1303244
REFERENCE   9  (residues 1 to 677)
  AUTHORS   Mullan,M., Crawford,F., Axelman,K., Houlden,H., Lilius,L.,
            Winblad,B. and Lannfelt,L.
  TITLE     A pathogenic mutation for probable Alzheimer's disease in the APP
            gene at the N-terminus of beta-amyloid
  JOURNAL   Nat Genet 1 (5), 345-347 (1992)
   PUBMED   1302033
REFERENCE   10 (residues 1 to 677)
  AUTHORS   Hendriks,L., van Duijn,C.M., Cras,P., Cruts,M., Van Hul,W., van
            Harskamp,F., Warren,A., McInnis,M.G., Antonarakis,S.E., Martin,J.J.
            et al.
  TITLE     Presenile dementia and cerebral haemorrhage linked to a mutation at
            codon 692 of the beta-amyloid precursor protein gene
  JOURNAL   Nat Genet 1 (3), 218-221 (1992)
   PUBMED   1303239
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI559391.1, Y00264.1 and
            BM876312.1.
            
            Summary: This gene encodes a cell surface receptor and
            transmembrane precursor protein that is cleaved by secretases to
            form a number of peptides. Some of these peptides are secreted and
            can bind to the acetyltransferase complex APBB1/TIP60 to promote
            transcriptional activation, while others form the protein basis of
            the amyloid plaques found in the brains of patients with Alzheimer
            disease. In addition, two of the peptides are antimicrobial
            peptides, having been shown to have bacteriocidal and antifungal
            activities. Mutations in this gene have been implicated in
            autosomal dominant Alzheimer disease and cerebroarterial
            amyloidosis (cerebral amyloid angiopathy). Multiple transcript
            variants encoding several different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2014].
            
            Transcript Variant: This variant (10) lacks three alternate
            in-frame exons compared to variant 1. The resulting isoform (j,
            also known as L-APP677) has the same N- and C-termini but is
            shorter compared to isoform a. No full-length transcript is
            available for this transcript; however, it is supported by
            PMID:1429732 and other publications.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1355731.1,
                                           SRR14038196.2240194.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            Protein has antimicrobial activity :: PMID: 20209079
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..677
                     /product="amyloid-beta precursor protein isoform j
                     precursor"
                     /note="peptidase nexin-II; cerebral vascular amyloid
                     peptide; protease nexin-II; amyloid beta A4 protein;
                     beta-amyloid peptide; alzheimer disease amyloid protein;
                     beta-amyloid peptide(1-40); beta-amyloid peptide(1-42);
                     amyloid precursor protein; beta-amyloid precursor protein;
                     testicular tissue protein Li 2; amyloid beta (A4)
                     precursor protein; alzheimer disease amyloid A4 protein
                     homolog"
                     /calculated_mol_wt=74997
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1781
     mat_peptide     18..677
                     /product="amyloid-beta precursor protein isoform j"
                     /calculated_mol_wt=74997
     mat_peptide     18..286
                     /product="N-APP. /id=PRO_0000381966"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
                     /calculated_mol_wt=30196
     Region          24..188
                     /region_name="A4_EXTRA"
                     /note="amyloid A4; smart00006"
                     /db_xref="CDD:128326"
     Region          28..123
                     /region_name="GFLD subdomain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01217"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Region          131..189
                     /region_name="CuBD subdomain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01217"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Site            170
                     /site_type="other"
                     /note="Required for Cu(2+) reduction.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01217; propagated
                     from UniProtKB/Swiss-Prot (P05067.3)"
     Region          194..284
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Site            197..198
                     /site_type="cleavage"
                     /note="Cleavage, by caspases.
                     /evidence=ECO:0000269|PubMed:10319819; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:8999878; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:8999878; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            217
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P05067.3)"
     Site            219..220
                     /site_type="cleavage"
                     /note="Cleavage, by caspases.
                     /evidence=ECO:0000269|PubMed:10319819; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            262
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P05067.3)"
     Region          291..473
                     /region_name="APP_E2"
                     /note="E2 domain of amyloid precursor protein; pfam12925"
                     /db_xref="CDD:463752"
     mat_peptide     579..620
                     /product="amyloid-beta precursor protein isoform j"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     20209079]"
                     /exception="alternative processing"
                     /calculated_mol_wt=4514
     mat_peptide     579..618
                     /product="amyloid-beta precursor protein isoform j"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     20209079]"
                     /calculated_mol_wt=4330
     Region          600..674
                     /region_name="JMTM_Notch_APP"
                     /note="juxtamembrane and transmembrane (JMTM) domain found
                     in Notch and APP family proteins; cl41775"
                     /db_xref="CDD:425406"
     Site            order(613..614,616..617,619..625,627..632)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411983"
     CDS             1..677
                     /gene="APP"
                     /gene_synonym="AAA; ABETA; ABPP; AD1; alpha-sAPP; APPI;
                     CTFgamma; CVAP; PN-II; PN2; preA4"
                     /coded_by="NM_001204303.2:151..2184"
                     /note="isoform j precursor is encoded by transcript
                     variant 10"
                     /db_xref="GeneID:351"
                     /db_xref="HGNC:HGNC:620"
                     /db_xref="MIM:104760"
ORIGIN      
        1 mlpglallll aawtaralev ptdgnaglla epqiamfcgr lnmhmnvqng kwdsdpsgtk
       61 tcidtkegil qycqevypel qitnvveanq pvtiqnwckr grkqckthph fvipyrclvg
      121 efvsdallvp dkckflhqer mdvcethlhw htvaketcse kstnlhdygm llpcgidkfr
      181 gvefvccpla eesdnvdsad aeeddsdvww ggadtdyadg sedkvvevae eeevaeveee
      241 eadddedded gdeveeeaee pyeeatertt siattttttt esveevvrvp ttaastpdav
      301 dkyletpgde nehahfqkak erleakhrer msqvmrewee aerqaknlpk adkkaviqhf
      361 qekvesleqe aanerqqlve thmarveaml ndrrrlalen yitalqavpp rprhvfnmlk
      421 kyvraeqkdr qhtlkhfehv rmvdpkkaaq irsqvmthlr viyermnqsl sllynvpava
      481 eeiqdevdel lqkeqnysdd vlanmisepr isygndalmp sltetkttve llpvngefsl
      541 ddlqpwhsfg adsvpanten egsgltnikt eeisevkmda efrhdsgyev hhqklvffae
      601 dvgsnkgaii glmvggvvia tvivitlvml kkkqytsihh gvvevdaavt peerhlskmq
      661 qngyenptyk ffeqmqn
//
LOCUS       NP_001364434             366 aa            linear   PRI 21-NOV-2025
DEFINITION  UDP-glucuronic acid decarboxylase 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001364434 XP_016860498
VERSION     NP_001364434.1
DBSOURCE    REFSEQ: accession NM_001377505.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Jacobs,J., Lyubenova,H., Potelle,S., Kopp,J., Gerin,I., Chan,W.L.,
            Rodriguez de Los Santos,M., Hulsemann,W., Mensah,M.A.,
            Cormier-Daire,V., Joosten,M., Bruggenwirth,H.T., Stuurman,K.E.,
            Miranda,V., Campeau,P.M., Wittler,L., Graff,J., Mundlos,S.,
            Ibrahim,D.M., Van Schaftingen,E., Fischer-Zirnsak,B., Kornak,U.,
            Ehmke,N. and Bommer,G.T.
  TITLE     A missing enzyme-rescue metabolite as cause of a rare skeletal
            dysplasia
  JOURNAL   Nature 646 (8083), 218-226 (2025)
   PUBMED   40836090
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Brewer,G.
  TITLE     UXS1: a sweet spot for cell death
  JOURNAL   Nat Rev Cancer 24 (1), 3 (2024)
   PUBMED   38030856
  REMARK    GeneRIF: UXS1: a sweet spot for cell death.
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Walsh,R.M. Jr., Polizzi,S.J., Kadirvelraj,R., Howard,W.W. and
            Wood,Z.A.
  TITLE     Man o' war mutation in UDP-alpha-D-xylose synthase favors the
            abortive catalytic cycle and uncovers a latent potential for
            hexamer formation
  JOURNAL   Biochemistry 54 (3), 807-819 (2015)
   PUBMED   25521717
  REMARK    GeneRIF: The persistence of a latent hexamer-building interface in
            the human enzyme suggests that the ancestral UXS may have been a
            hexamer.
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Polizzi,S.J., Walsh,R.M. Jr., Le Magueres,P., Criswell,A.R. and
            Wood,Z.A.
  TITLE     Human UDP-alpha-d-xylose synthase forms a catalytically important
            tetramer that has not been observed in crystal structures
  JOURNAL   Biochemistry 52 (22), 3888-3898 (2013)
   PUBMED   23656592
  REMARK    GeneRIF: hUXS forms a tetramer in solution that is important for
            activity. The higher activity of the tetramer coupled with the
            relative instability of the dimeric complex suggests that an
            association-dissociation mechanism may regulate hUXS activity.
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Polizzi,S.J., Walsh,R.M. Jr., Peeples,W.B., Lim,J.M., Wells,L. and
            Wood,Z.A.
  TITLE     Human UDP-alpha-D-xylose synthase and Escherichia coli ArnA
            conserve a conformational shunt that controls whether xylose or
            4-keto-xylose is produced
  JOURNAL   Biochemistry 51 (44), 8844-8855 (2012)
   PUBMED   23072385
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Bakker,H., Oka,T., Ashikov,A., Yadav,A., Berger,M., Rana,N.A.,
            Bai,X., Jigami,Y., Haltiwanger,R.S., Esko,J.D. and
            Gerardy-Schahn,R.
  TITLE     Functional UDP-xylose transport across the endoplasmic
            reticulum/Golgi membrane in a Chinese hamster ovary cell mutant
            defective in UDP-xylose Synthase
  JOURNAL   J Biol Chem 284 (4), 2576-2583 (2009)
   PUBMED   19028698
  REMARK    GeneRIF: Complementation was achieved by expression of a
            cytoplasmic variant of UDP-xylose Synthase, which proves the
            existence of a functional Golgi UDP-xylose transporter[UDP-xylose
            Synthase]
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Hwang,H.Y. and Horvitz,H.R.
  TITLE     The SQV-1 UDP-glucuronic acid decarboxylase and the SQV-7
            nucleotide-sugar transporter may act in the Golgi apparatus to
            affect Caenorhabditis elegans vulval morphogenesis and embryonic
            development
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14218-14223 (2002)
   PUBMED   12391314
REFERENCE   10 (residues 1 to 366)
  AUTHORS   Moriarity,J.L., Hurt,K.J., Resnick,A.C., Storm,P.B., Laroy,W.,
            Schnaar,R.L. and Snyder,S.H.
  TITLE     UDP-glucuronate decarboxylase, a key enzyme in proteoglycan
            synthesis: cloning, characterization, and localization
  JOURNAL   J Biol Chem 277 (19), 16968-16975 (2002)
   PUBMED   11877387
  REMARK    GeneRIF: UDP-glucuronate decarboxylase, a key enzyme in
            proteoglycan synthesis: cloning, characterization, and
            localization.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC018878.8.
            
            On Jan 16, 2020 this sequence version replaced XP_016860498.1.
            
            Summary: This gene encodes an enzyme found in the perinuclear Golgi
            which catalyzes the synthesis of UDP-xylose used in
            glycosaminoglycan (GAG) synthesis on proteoglycans. The GAG chains
            are covalently attached to proteoglycans which participate in
            signaling pathways during development. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Dec 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.80970.1,
                                           SRR14038196.738139.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q12.2"
     Protein         1..366
                     /product="UDP-glucuronic acid decarboxylase 1 isoform 5"
                     /EC_number="4.1.1.35"
                     /note="short chain dehydrogenase/reductase family 6E,
                     member 12; UDP-glucuronic acid decarboxylase 1; UXS-1"
                     /calculated_mol_wt=41389
     Region          4..78
                     /region_name="UXS1_N"
                     /note="UDP-glucuronate decarboxylase N-terminal;
                     pfam11803"
                     /db_xref="CDD:463356"
     Region          89..338
                     /region_name="UGD_SDR_e"
                     /note="UDP-glucuronate decarboxylase (UGD) and related
                     proteins, extended (e) SDRs; cd05230"
                     /db_xref="CDD:187541"
     Site            order(95,97..100,119..124,143..145,159..163,178,200..202,
                     231,235,258..261,272)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:187541"
     Site            order(148..149,184..185,188..189,191..192,245)
                     /site_type="other"
                     /note="putative substrate binding site 2 [chemical
                     binding]"
                     /db_xref="CDD:187541"
     Site            order(165,228,260,271..273,276..277,288..290,295,297)
                     /site_type="other"
                     /note="putative substrate binding site 1 [chemical
                     binding]"
                     /db_xref="CDD:187541"
     Site            order(179,202,231,235)
                     /site_type="active"
                     /db_xref="CDD:187541"
     CDS             1..366
                     /gene="UXS1"
                     /gene_synonym="hUXS; hUXS1; SDR6E1; UGD"
                     /coded_by="NM_001377505.1:61..1161"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:80146"
                     /db_xref="HGNC:HGNC:17729"
                     /db_xref="MIM:609749"
ORIGIN      
        1 mvskallrlv savnrrrmkl llgiallayv asvwgnfvnm rsiqengelk ieskieemve
       61 plrekirdle ksftqkyppv kflsekdrkr ilitggagfv gshltdklmm dghevtvvdn
      121 fftgrkrnve hwighenfel inhdvveply ievdqiyhla spasppnymy npiktlktnt
      181 igtlnmlgla krvgarllla stsevygdpe vhpqsedywg hvnpigprac ydegkrvaet
      241 mcyaymkqeg vevrvarifn tfgprmhmnd grvvsnfilq alqgepltvy gsgsqtrafq
      301 yvsdlvnglv almnsnvssp vnlvpleegl nkaihyfrke leyqannqyi pkpkparikk
      361 grtrhs
//
LOCUS       NP_602299                168 aa            linear   PRI 21-NOV-2025
DEFINITION  regulator of G-protein signaling 3 isoform 4 [Homo sapiens].
ACCESSION   NP_602299
VERSION     NP_602299.1
DBSOURCE    REFSEQ: accession NM_134427.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Kanwal,A., Pardo,J.V. and Naz,S.
  TITLE     RGS3 and IL1RAPL1 missense variants implicate defective
            neurotransmission in early-onset inherited schizophrenias
  JOURNAL   J Psychiatry Neurosci 47 (6), E379-E390 (2022)
   PUBMED   36318984
  REMARK    GeneRIF: RGS3 and IL1RAPL1 missense variants implicate defective
            neurotransmission in early-onset inherited schizophrenias.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Hao,F., Wang,N., Gui,H., Zhang,Y., Wu,Z. and Wang,J.
  TITLE     Pseudogene UBE2MP1 derived transcript enhances in vitro cell
            proliferation and apoptosis resistance of hepatocellular carcinoma
            cells through miR-145-5p/RGS3 axis
  JOURNAL   Aging (Albany NY) 14 (19), 7906-7925 (2022)
   PUBMED   36214767
  REMARK    GeneRIF: Pseudogene UBE2MP1 derived transcript enhances in vitro
            cell proliferation and apoptosis resistance of hepatocellular
            carcinoma cells through miR-145-5p/RGS3 axis.
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 168)
  AUTHORS   Kehrl,J.H., Srikumar,D., Harrison,K., Wilson,G.L. and Shi,C.S.
  TITLE     Additional 5' exons in the RGS3 locus generate multiple mRNA
            transcripts, one of which accounts for the origin of human PDZ-RGS3
  JOURNAL   Genomics 79 (6), 860-868 (2002)
   PUBMED   12036301
REFERENCE   5  (residues 1 to 168)
  AUTHORS   Mittmann,C., Schuler,C., Chung,C.H., Hoppner,G., Nose,M.,
            Kehrl,J.H. and Wieland,T.
  TITLE     Evidence for a short form of RGS3 preferentially expressed in the
            human heart
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 363 (4), 456-463 (2001)
   PUBMED   11330340
REFERENCE   6  (residues 1 to 168)
  AUTHORS   Dulin,N.O., Pratt,P., Tiruppathi,C., Niu,J., Voyno-Yasenetskaya,T.
            and Dunn,M.J.
  TITLE     Regulator of G protein signaling RGS3T is localized to the nucleus
            and induces apoptosis
  JOURNAL   J Biol Chem 275 (28), 21317-21323 (2000)
   PUBMED   10749886
REFERENCE   7  (residues 1 to 168)
  AUTHORS   Dulin,N.O., Sorokin,A., Reed,E., Elliott,S., Kehrl,J.H. and
            Dunn,M.J.
  TITLE     RGS3 inhibits G protein-mediated signaling via translocation to the
            membrane and binding to Galpha11
  JOURNAL   Mol Cell Biol 19 (1), 714-723 (1999)
   PUBMED   9858594
REFERENCE   8  (residues 1 to 168)
  AUTHORS   Chatterjee,T.K., Eapen,A., Kanis,A.B. and Fisher,R.A.
  TITLE     Genomic organization, 5'-flanking region, and chromosomal
            localization of the human RGS3 gene
  JOURNAL   Genomics 45 (2), 429-433 (1997)
   PUBMED   9344672
REFERENCE   9  (residues 1 to 168)
  AUTHORS   Chatterjee,T.K., Eapen,A.K. and Fisher,R.A.
  TITLE     A truncated form of RGS3 negatively regulates G protein-coupled
            receptor stimulation of adenylyl cyclase and phosphoinositide
            phospholipase C
  JOURNAL   J Biol Chem 272 (24), 15481-15487 (1997)
   PUBMED   9182581
REFERENCE   10 (residues 1 to 168)
  AUTHORS   Druey,K.M., Blumer,K.J., Kang,V.H. and Kehrl,J.H.
  TITLE     Inhibition of G-protein-mediated MAP kinase activation by a new
            mammalian gene family
  JOURNAL   Nature 379 (6567), 742-746 (1996)
   PUBMED   8602223
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP257809.1, BE298009.1 and
            BC019039.2.
            
            Summary: This gene encodes a member of the regulator of G-protein
            signaling (RGS) family. This protein is a GTPase-activating protein
            that inhibits G-protein-mediated signal transduction. Alternative
            splicing and the use of alternative promoters results in multiple
            transcript variants encoding different isoforms. Long isoforms are
            largely cytosolic and plasma membrane-associated with a function in
            Wnt signaling and in the epithelial mesenchymal transition, while
            shorter N-terminally-truncated isoforms can be nuclear. [provided
            by RefSeq, Jan 2013].
            
            Transcript Variant: This variant (4) lacks several 5' exons but
            includes an alternate 5' exon, and it thus differs in the 5' UTR,
            lacks a large portion of the 5' coding region, and uses a
            downstream in-frame start codon, compared to variant 6. The encoded
            isoform (4, also known as RGS3S in PubMed ID:11330340) is
            significantly shorter at the N-terminus, compared to isoform 6.
            Both variants 4 and 9 encode isoform 4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BQ953216.1, ERR279856.3768.1 [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..168
                     /product="regulator of G-protein signaling 3 isoform 4"
                     /note="regulator of G-protein signalling 3"
                     /calculated_mol_wt=19325
     Region          44..157
                     /region_name="RGS_RGS3"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the RGS3 protein; cd08713"
                     /db_xref="CDD:188668"
     CDS             1..168
                     /gene="RGS3"
                     /gene_synonym="C2PA; RGP3"
                     /coded_by="NM_134427.3:315..821"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:5998"
                     /db_xref="HGNC:HGNC:9999"
                     /db_xref="MIM:602189"
ORIGIN      
        1 mknklgifrr rnespgappa gkadkmmksf kptseealkw geslekllvh kyglavfqaf
       61 lrtefseenl efwlacedfk kvksqskmas kakkifaeyi aiqackevnl dsytrehtkd
      121 nlqsvtrgcf dlaqkrifgl mekdsyprfl rsdlyldlin qkkmsppl
//
LOCUS       NP_001362674             387 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform www [Homo sapiens].
ACCESSION   NP_001362674
VERSION     NP_001362674.1
DBSOURCE    REFSEQ: accession NM_001375745.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 387)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 387)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 387)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..387
                     /product="abl interactor 2 isoform www"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=41304
     Region          19..82
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          <146..273
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          326..386
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(334,336,339,343,361..362,375,377..378)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..387
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375745.1:468..1631"
                     /note="isoform www is encoded by transcript variant 80"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 mldiqasqlr rmessinhis qtvdihkekv arreigiltt nkntsrthki iapanlerpv
       61 ryirkpidyt ilddighgvk wllrfkvstq nmkmgglprt tpptqkppsp pmsgkgtlgs
      121 gssggshpss rsssrensgs gsvgvpiavp tpsppsvfpa pagsagtppl patsasapap
      181 lvpatvpsst apdaaaggaq tladgftspt ppvvsstppt ghpvqfysmn rpasrhtppt
      241 iggslpyrrp psitsqtslq nqmnggpfys qnpdtppppp pveepvfdes pppppppedy
      301 eeeeaavvey sdpyaeedpp waprsylekv vaiydytkdk edelsfqega iiyvikkndd
      361 gwyegvmngv tglfpgnyve simhyse
//
LOCUS       NP_001371816             719 aa            linear   PRI 21-NOV-2025
DEFINITION  signal transducer and activator of transcription 1-alpha/beta
            isoform 8 [Homo sapiens].
ACCESSION   NP_001371816
VERSION     NP_001371816.1
DBSOURCE    REFSEQ: accession NM_001384887.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 719)
  AUTHORS   Wang,Y., Song,Q., Huang,W., Lin,Y., Wang,X., Wang,C., Willard,B.,
            Zhao,C., Nan,J., Holvey-Bates,E., Wang,Z., Taylor,D., Yang,J. and
            Stark,G.R.
  TITLE     A virus-induced conformational switch of STAT1-STAT2 dimers boosts
            antiviral defenses
  JOURNAL   Cell Res 31 (2), 206-218 (2021)
   PUBMED   32759968
REFERENCE   3  (residues 1 to 719)
  AUTHORS   Decker,T. and Kovarik,P.
  TITLE     Serine phosphorylation of STATs
  JOURNAL   Oncogene 19 (21), 2628-2637 (2000)
   PUBMED   10851062
  REMARK    Review article
REFERENCE   4  (residues 1 to 719)
  AUTHORS   Bowman,T., Garcia,R., Turkson,J. and Jove,R.
  TITLE     STATs in oncogenesis
  JOURNAL   Oncogene 19 (21), 2474-2488 (2000)
   PUBMED   10851046
  REMARK    Review article
REFERENCE   5  (residues 1 to 719)
  AUTHORS   Haddad,B., Pabon-Pena,C.R., Young,H. and Sun,W.H.
  TITLE     Assignment1 of STAT1 to human chromosome 2q32 by FISH and radiation
            hybrids
  JOURNAL   Cytogenet Cell Genet 83 (1-2), 58-59 (1998)
   PUBMED   9925928
REFERENCE   6  (residues 1 to 719)
  AUTHORS   Yan,R., Qureshi,S., Zhong,Z., Wen,Z. and Darnell,J.E. Jr.
  TITLE     The genomic structure of the STAT genes: multiple exons in
            coincident sites in Stat1 and Stat2
  JOURNAL   Nucleic Acids Res 23 (3), 459-463 (1995)
   PUBMED   7885841
REFERENCE   7  (residues 1 to 719)
  AUTHORS   Igarashi,K., Garotta,G., Ozmen,L., Ziemiecki,A., Wilks,A.F.,
            Harpur,A.G., Larner,A.C. and Finbloom,D.S.
  TITLE     Interferon-gamma induces tyrosine phosphorylation of
            interferon-gamma receptor and regulated association of protein
            tyrosine kinases, Jak1 and Jak2, with its receptor
  JOURNAL   J Biol Chem 269 (20), 14333-14336 (1994)
   PUBMED   7514165
REFERENCE   8  (residues 1 to 719)
  AUTHORS   Shuai,K., Horvath,C.M., Huang,L.H., Qureshi,S.A., Cowburn,D. and
            Darnell,J.E. Jr.
  TITLE     Interferon activation of the transcription factor Stat91 involves
            dimerization through SH2-phosphotyrosyl peptide interactions
  JOURNAL   Cell 76 (5), 821-828 (1994)
   PUBMED   7510216
REFERENCE   9  (residues 1 to 719)
  AUTHORS   Schindler,C., Fu,X.Y., Improta,T., Aebersold,R. and Darnell,J.E.
            Jr.
  TITLE     Proteins of transcription factor ISGF-3: one gene encodes the
            91-and 84-kDa ISGF-3 proteins that are activated by interferon
            alpha
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7836-7839 (1992)
   PUBMED   1502203
REFERENCE   10 (residues 1 to 719)
  AUTHORS   Schindler,C., Shuai,K., Prezioso,V.R. and Darnell,J.E. Jr.
  TITLE     Interferon-dependent tyrosine phosphorylation of a latent
            cytoplasmic transcription factor
  JOURNAL   Science 257 (5071), 809-813 (1992)
   PUBMED   1496401
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC067945.4.
            
            Summary: The protein encoded by this gene is a member of the STAT
            protein family. In response to cytokines and growth factors, STAT
            family members are phosphorylated by the receptor associated
            kinases, and then form homo- or heterodimers that translocate to
            the cell nucleus where they act as transcription activators. The
            protein encoded by this gene can be activated by various ligands
            including interferon-alpha, interferon-gamma, EGF, PDGF and IL6.
            This protein mediates the expression of a variety of genes, which
            is thought to be important for cell viability in response to
            different cell stimuli and pathogens. The protein plays an
            important role in immune responses to viral, fungal and
            mycobacterial pathogens. Mutations in this gene are associated with
            Immunodeficiency 31B, 31A, and 31C. [provided by RefSeq, Jun 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1965299, SAMEA1966682
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.2"
     Protein         1..719
                     /product="signal transducer and activator of transcription
                     1-alpha/beta isoform 8"
                     /note="transcription factor ISGF-3 components p91/p84;
                     signal transducer and activator of transcription
                     1-alpha/beta; signal transducer and activator of
                     transcription 1, 91kD; signal transducer and activator of
                     transcription 1, 91kDa"
                     /calculated_mol_wt=83698
     Region          2..121
                     /region_name="STAT_int"
                     /note="STAT protein, protein interaction domain;
                     smart00964"
                     /db_xref="CDD:214942"
     Region          138..313
                     /region_name="STAT1_CCD"
                     /note="Coiled-coil domain of Signal Transducer and
                     Activator of Transcription 1 (STAT1); cd16851"
                     /db_xref="CDD:341076"
     Site            order(164..165,168..169,172,175..176,179,232,236,239..241,
                     243..244,256..257,259..260,263..264,267,271,274,306,
                     309..311)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:341076"
     Site            order(239..241,243..244,256..257,260,263..264,267,271,274,
                     302,306,309..310)
                     /site_type="other"
                     /note="CCD-DBD interface [polypeptide binding]"
                     /db_xref="CDD:341076"
     Region          315..446
                     /region_name="STAT_DBD"
                     /note="DNA-binding domain of Signal Transducer and
                     Activator of Transcription (STAT); cl28920"
                     /db_xref="CDD:355796"
     Region          526..676
                     /region_name="SH2_STAT1"
                     /note="Src homology 2 (SH2) domain found in signal
                     transducer and activator of transcription (STAT) 1
                     proteins; cd10372"
                     /db_xref="CDD:198235"
     Site            order(553,571,599,601)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198235"
     Site            order(600,616)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198235"
     Site            order(610..611,675)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:198235"
     Region          684..708
                     /region_name="STAT1_TAZ2bind"
                     /note="STAT1 TAZ2 binding domain; pfam12162"
                     /db_xref="CDD:432372"
     CDS             1..719
                     /gene="STAT1"
                     /gene_synonym="CANDF7; IMD31A; IMD31B; IMD31C; ISGF-3;
                     STAT91"
                     /coded_by="NM_001384887.1:310..2469"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:6772"
                     /db_xref="HGNC:HGNC:11362"
                     /db_xref="MIM:600555"
ORIGIN      
        1 msqwyelqql dskfleqvhq lyddsfpmei rqylaqwlek qdwehaandv sfatirfhdl
       61 lsqlddqysr fslennfllq hnirkskrnl qdnfqedpiq msmiiysclk eerkilenaq
      121 rfnqaqsgni qstvmldkqk eldskvrnvk dkvmciehei ksledlqdey dfkcktlqnr
      181 ehetngvaks dqkqeqlllk kmylmldnkr kevvhkiiel lnvteltqna lindelvewk
      241 rrqqsacigg ppnacldqlq nwftivaesl qqvrqqlkkl eeleqkytye hdpitknkqv
      301 lwdrtfslfq qliqrllvkl qelnynlkvk vlfdkdvner ntvkgfrkfn ilgthtkvmn
      361 meestngsla aefrhlqlke qknagtrtne gplivteelh slsfetqlcq pglvidlett
      421 slpvvvisnv sqlpsgwasi lwynmlvaep rnlsffltpp carwaqlsev lswqfssvtk
      481 rglnvdqlnm lgekllgpna spdglipwtr fckenindkn fpfwlwiesi lelikkhllp
      541 lwndgcimgf iskererall kdqqpgtfll rfsessrega itftwversq nggepdfhav
      601 epytkkelsa vtfpdiirny kvmaaenipe nplkylypni dkdhafgkyy srpkeapepm
      661 eldgpkgtgy iktelisvse vhpsrlqttd nllpmspeef devsrivgsv efdsmmntv
//
LOCUS       NP_001350032             555 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger protein 250 isoform b [Homo sapiens].
ACCESSION   NP_001350032 XP_024302990
VERSION     NP_001350032.1
DBSOURCE    REFSEQ: accession NM_001363103.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 555)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 555)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   6  (residues 1 to 555)
  AUTHORS   Lorenz,P., Dietmann,S., Wilhelm,T., Koczan,D., Autran,S., Gad,S.,
            Wen,G., Ding,G., Li,Y., Rousseau-Merck,M.F. and Thiesen,H.J.
  TITLE     The ancient mammalian KRAB zinc finger gene cluster on human
            chromosome 8q24.3 illustrates principles of C2H2 zinc finger
            evolution associated with unique expression profiles in human
            tissues
  JOURNAL   BMC Genomics 11, 206 (2010)
   PUBMED   20346131
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 555)
  AUTHORS   Rual,J.F., Hirozane-Kishikawa,T., Hao,T., Bertin,N., Li,S.,
            Dricot,A., Li,N., Rosenberg,J., Lamesch,P., Vidalain,P.O.,
            Clingingsmith,T.R., Hartley,J.L., Esposito,D., Cheo,D., Moore,T.,
            Simmons,B., Sequerra,R., Bosak,S., Doucette-Stamm,L., Le Peuch,C.,
            Vandenhaute,J., Cusick,M.E., Albala,J.S., Hill,D.E. and Vidal,M.
  TITLE     Human ORFeome version 1.1: a platform for reverse proteomics
  JOURNAL   Genome Res 14 (10B), 2128-2135 (2004)
   PUBMED   15489335
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF235103.5, R53168.1, BI820228.1, DB272357.1, BC017091.1,
            CV022909.1 and CA422363.1.
            
            On May 8, 2018 this sequence version replaced XP_024302990.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.288991.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..555
                     /product="zinc finger protein 250 isoform b"
                     /note="zinc finger protein 647; zinc finger protein (clone
                     647)"
                     /calculated_mol_wt=62764
     Region          17..77
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          173..532
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          196..216
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(201,203,205,207..208,211..212,215,229,231,235..236,
                     239..240,243,257,259,261,263..264,267..268,271)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          224..244
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          252..272
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          280..300
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          308..328
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          336..356
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          364..384
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          392..412
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          420..440
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          448..468
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          476..496
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(481,483,485,487..488,491..492,495,509,511,515..516,
                     519..520,523,537,539,541,543..544,547..548,551)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          504..524
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          532..552
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..555
                     /gene="ZNF250"
                     /gene_synonym="ZFP647; ZNF647"
                     /coded_by="NM_001363103.2:221..1888"
                     /note="isoform b is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS55282.1"
                     /db_xref="GeneID:58500"
                     /db_xref="HGNC:HGNC:13044"
ORIGIN      
        1 maaarllpvp agpqakltfe dvavllsqde wdrlcpaqrg lyrnvmmety gnvvslglpg
       61 skpdiisqle rgedpwvldr kgakksqglw sdysdnlkyd httactqqds lscpwecetk
      121 gesqntdlsp kpliseqtvi lgktplgrid qennetkqsf clspnsvdhr evqvlsqsmp
      181 ltphqavpsg erpymcvecg kcfgrsshll qhqrihtgek pyvcsvcgka fsqssvlskh
      241 rrihtgekpy ecnecgkafr vssdlaqhhk ihtgekphec lecrkaftql shliqhqrih
      301 tgerpyvcpl cgkafnhstv lrshqrvhtg ekphrcnecg ktfsvkrtll qhqrihtgek
      361 pytcsecgka fsdrsvliqh hnvhtgekpy ecsecgktfs hrstlmnher ihteekpyac
      421 yecgkafvqh shliqhqrvh tgekpyvcge cghafsarrs liqherihtg ekpfqctecg
      481 kafslkatli vhlrthtgek pyecnscgka fsqysvliqh qrihtgekpy ecgecgrafn
      541 qhghliqhqk vhrkl
//
LOCUS       NP_001371495             694 aa            linear   PRI 21-NOV-2025
DEFINITION  protein Smaug homolog 2 isoform a [Homo sapiens].
ACCESSION   NP_001371495
VERSION     NP_001371495.1
DBSOURCE    REFSEQ: accession NM_001384566.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 694)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 694)
  AUTHORS   Wu,C., Liu,X., Li,B., Sun,G., Peng,C. and Xiang,D.
  TITLE     miR-451 suppresses the malignant characteristics of colorectal
            cancer via targeting SAMD4B
  JOURNAL   Mol Med Rep 24 (2) (2021)
   PUBMED   34109425
  REMARK    GeneRIF: miR451 suppresses the malignant characteristics of
            colorectal cancer via targeting SAMD4B.
REFERENCE   6  (residues 1 to 694)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   7  (residues 1 to 694)
  AUTHORS   Baez,M.V. and Boccaccio,G.L.
  TITLE     Mammalian Smaug is a translational repressor that forms cytoplasmic
            foci similar to stress granules
  JOURNAL   J Biol Chem 280 (52), 43131-43140 (2005)
   PUBMED   16221671
REFERENCE   8  (residues 1 to 694)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   9  (residues 1 to 694)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 694)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011445.6 and AC005239.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. Variants 1 and 3-14 all encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR18074967.1862514.1,
                                    SRR18074969.2917407.1 [ECO:0000331]
            RNAseq introns       :: partial sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..694
                     /product="protein Smaug homolog 2 isoform a"
                     /note="smaug homolog B; protein Smaug homolog 2; smaug 2;
                     SAM domain-containing protein 4B; sterile alpha motif
                     domain-containing protein 4B"
                     /calculated_mol_wt=75353
     Region          158..301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XS6; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XS6; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XS6; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Region          296..358
                     /region_name="SAM_Smaug"
                     /note="SAM domain of Smaug subfamily; cd09557"
                     /db_xref="CDD:188956"
     Site            order(312,314..315,343,346..348,355,357)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:188956"
     Region          407..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            555
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            592
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            600
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            602
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Region          607..643
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     CDS             1..694
                     /gene="SAMD4B"
                     /gene_synonym="Smaug2; SMGB"
                     /coded_by="NM_001384566.1:507..2591"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS33020.1"
                     /db_xref="GeneID:55095"
                     /db_xref="HGNC:HGNC:25492"
                     /db_xref="MIM:619231"
ORIGIN      
        1 mmfrdqvgil agwfkgwnec eqtvallsll krvtrtqarf lqlclehsla dcndihlles
       61 eansaaivsq wqqeskekvv slllshlpll qpgnteakse ymrllqkvla ysiesnafie
      121 esrqllsyal ihpattledr nalalwlshl eerlasgfrs rpepsyhsrq gsdewggpae
      181 lgpgeagpgw qdkpprengh vpfhpsssvp painsigsna ntglpcqihp splkrsmsli
      241 ptspqvpgew pspeelgara afttpdhapl spqssvassg seqteeqgss rntfqedgsg
      301 mkdvpswlks lrlhkyaalf sqmsyeemmt lteqhlesqn vtkgarhkia lsiqklrerq
      361 svlkslekdv leggnlrnal qelqqiiitp ikaysvlqat vaaatttpta kdgapgeppl
      421 pgaepplahp gtdkgteakd ppavenyppp papaptdgse papapvadgd ipsqftrvmg
      481 kvctqllvsr pdeenitsyl qliekclthe aftetqkkrl lswkqqvlkl lrtfprkaal
      541 emqnyrqqkg wafgsnslpi agsvgmgvar rtqrqfpmpp ralppgrmgl lspsgiggvs
      601 prhaltspsl ggqgrqnlwf anpggsnsmp sqsrssvqrt hslpvhsspq ailmfppdcp
      661 vpgpdleinp tleslclsmt ehalgdgtdk tsti
//
LOCUS       NP_001352607             533 aa            linear   PRI 21-NOV-2025
DEFINITION  prolyl 4-hydroxylase subunit alpha-2 isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_001352607 XP_006714792
VERSION     NP_001352607.1
DBSOURCE    REFSEQ: accession NM_001365678.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Dang,X., Chen,X., Liang,Z., Dai,Z., Ding,W., Song,J. and Fu,J.
  TITLE     P4HA2 promotes tumor progression and is transcriptionally regulated
            by SP1 in colorectal cancer
  JOURNAL   Cancer Biol Ther 25 (1), 2361594 (2024)
   PUBMED   38857058
  REMARK    GeneRIF: P4HA2 promotes tumor progression and is transcriptionally
            regulated by SP1 in colorectal cancer.
REFERENCE   3  (residues 1 to 533)
  AUTHORS   El-Deek,H.E.M., El-Naggar,M.S., Morsy,A.M.M., Sedik,M.F.,
            Osman,H.A. and Ahmed,A.M.
  TITLE     P4HA2 involved in SLUG-associated EMT predicts poor prognosis of
            patients with KRAS-positive colorectal cancer
  JOURNAL   Med Mol Morphol 57 (3), 167-176 (2024)
   PUBMED   38522060
  REMARK    GeneRIF: P4HA2 involved in SLUG-associated EMT predicts poor
            prognosis of patients with KRAS-positive colorectal cancer.
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Chi,Z., Wang,Q., Wang,X., Li,D., Tong,L., Shi,Y., Yang,F., Guo,Q.,
            Zheng,J. and Chen,Z.
  TITLE     P4HA2 promotes proliferation, invasion, and metastasis through
            regulation of the PI3K/AKT signaling pathway in oral squamous cell
            carcinoma
  JOURNAL   Sci Rep 14 (1), 15023 (2024)
   PUBMED   38951593
  REMARK    GeneRIF: P4HA2 promotes proliferation, invasion, and metastasis
            through regulation of the PI3K/AKT signaling pathway in oral
            squamous cell carcinoma.
            Erratum:[Sci Rep. 2024 Oct 28;14(1):25836. doi:
            10.1038/s41598-024-76811-1. PMID: 39468141]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 533)
  AUTHORS   Wu,Y.L., Liu,W., Zhao,T. and Jin,J.
  TITLE     P4HA2 contributes to head and neck squamous cell carcinoma
            progression and EMT through PI3K/AKT signaling pathway
  JOURNAL   Med Oncol 41 (6), 163 (2024)
   PUBMED   38777998
  REMARK    GeneRIF: P4HA2 contributes to head and neck squamous cell carcinoma
            progression and EMT through PI3K/AKT signaling pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 533)
  AUTHORS   Lehner,B., Semple,J.I., Brown,S.E., Counsell,D., Campbell,R.D. and
            Sanderson,C.M.
  TITLE     Analysis of a high-throughput yeast two-hybrid system and its use
            to predict the function of intracellular proteins encoded within
            the human MHC class III region
  JOURNAL   Genomics 83 (1), 153-167 (2004)
   PUBMED   14667819
REFERENCE   7  (residues 1 to 533)
  AUTHORS   Kukkola,L., Hieta,R., Kivirikko,K.I. and Myllyharju,J.
  TITLE     Identification and characterization of a third human, rat, and
            mouse collagen prolyl 4-hydroxylase isoenzyme
  JOURNAL   J Biol Chem 278 (48), 47685-47693 (2003)
   PUBMED   14500733
REFERENCE   8  (residues 1 to 533)
  AUTHORS   Hieta,R., Kukkola,L., Permi,P., Pirila,P., Kivirikko,K.I.,
            Kilpelainen,I. and Myllyharju,J.
  TITLE     The peptide-substrate-binding domain of human collagen prolyl
            4-hydroxylases. Backbone assignments, secondary structure, and
            binding of proline-rich peptides
  JOURNAL   J Biol Chem 278 (37), 34966-34974 (2003)
   PUBMED   12824157
  REMARK    GeneRIF: the substrate specificity, binding site and conformation
            of this enzyme
REFERENCE   9  (residues 1 to 533)
  AUTHORS   Nokelainen,M., Nissi,R., Kukkola,L., Helaakoski,T. and
            Myllyharju,J.
  TITLE     Characterization of the human and mouse genes for the alpha subunit
            of type II prolyl 4-hydroxylase. Identification of a previously
            unknown alternatively spliced exon and its expression in various
            tissues
  JOURNAL   Eur J Biochem 268 (20), 5300-5309 (2001)
   PUBMED   11606192
REFERENCE   10 (residues 1 to 533)
  AUTHORS   Annunen,P., Helaakoski,T., Myllyharju,J., Veijola,J.,
            Pihlajaniemi,T. and Kivirikko,K.I.
  TITLE     Cloning of the human prolyl 4-hydroxylase alpha subunit isoform
            alpha(II) and characterization of the type II enzyme tetramer. The
            alpha(I) and alpha(II) subunits do not form a mixed
            alpha(I)alpha(II)beta2 tetramer
  JOURNAL   J Biol Chem 272 (28), 17342-17348 (1997)
   PUBMED   9211872
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC034220.5 and AC063976.5.
            
            On Sep 12, 2018 this sequence version replaced XP_006714792.1.
            
            Summary: This gene encodes a component of prolyl 4-hydroxylase, a
            key enzyme in collagen synthesis composed of two identical alpha
            subunits and two beta subunits. The encoded protein is one of
            several different types of alpha subunits and provides the major
            part of the catalytic site of the active enzyme. In collagen and
            related proteins, prolyl 4-hydroxylase catalyzes the formation of
            4-hydroxyproline that is essential to the proper three-dimensional
            folding of newly synthesized procollagen chains. Alternatively
            spliced transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (7), as well as variants 2, 3, 4,
            8, and 9, all encode the same isoform (2).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.59065.1,
                                           SRR18074969.560150.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.1"
     Protein         1..533
                     /product="prolyl 4-hydroxylase subunit alpha-2 isoform 2
                     precursor"
                     /EC_number="1.14.11.2"
                     /note="C-P4Halpha(II); collagen prolyl 4-hydroxylase
                     alpha(II); procollagen-proline, 2-oxoglutarate
                     4-dioxygenase (proline 4-hydroxylase), alpha polypeptide
                     II; 4-PH alpha 2; prolyl 4-hydroxylase, alpha polypeptide
                     II; procollagen-proline,2-oxoglutarate-4-dioxygenase
                     subunit alpha-2; lncRNA promotes epithelial-mesenchymal
                     transition"
                     /calculated_mol_wt=58297
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2354
     Region          26..157
                     /region_name="P4Ha_N"
                     /note="Prolyl 4-Hydroxylase alpha-subunit, N-terminal
                     region; pfam08336"
                     /db_xref="CDD:462433"
     Region          159..>272
                     /region_name="BamD"
                     /note="Outer membrane protein assembly factor BamD,
                     BamD/ComL family [Cell wall/membrane/envelope biogenesis];
                     COG4105"
                     /db_xref="CDD:443281"
     Region          346..517
                     /region_name="P4Hc"
                     /note="Prolyl 4-hydroxylase alpha subunit homologues;
                     smart00702"
                     /db_xref="CDD:214780"
     CDS             1..533
                     /gene="P4HA2"
                     /gene_synonym="lncRNA-PE; MYP25"
                     /coded_by="NM_001365678.2:256..1857"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 7"
                     /db_xref="CCDS:CCDS34230.1"
                     /db_xref="GeneID:8974"
                     /db_xref="HGNC:HGNC:8547"
                     /db_xref="MIM:600608"
ORIGIN      
        1 mklwvsallm awfgvlscvq aefftsighm tdliyaekel vqslkeyilv eeaklskiks
       61 wankmealts ksaadaegyl ahpvnayklv krlntdwpal edlvlqdsaa gfianlsvqr
      121 qffptdedei gaakalmrlq dtyrldpgti srgelpgtky qamlsvddcf gmgrsayneg
      181 dyyhtvlwme qvlkqldage eatttksqvl dylsyavfql gdlhralelt rrllsldpsh
      241 eraggnlryf eqlleeerek tltnqteael atpegiyerp vdylperdvy eslcrgegvk
      301 ltprrqkrlf cryhhgnrap qlliapfkee dewdsphivr yydvmsdeei erikeiakpk
      361 laratvrdpk tgvltvasyr vsksswleed ddpvvarvnr rmqhitgltv ktaellqvan
      421 ygvggqyeph fdfsrrpfds glktegnrla tflnymsdve aggatvfpdl gaaiwpkkgt
      481 avfwynllrs gegdyrtrha acpvlvgckw vsnkwfherg qeflrpcgst evd
//
LOCUS       NP_001243497             764 aa            linear   PRI 21-NOV-2025
DEFINITION  liprin-beta-2 isoform 2 [Homo sapiens].
ACCESSION   NP_001243497
VERSION     NP_001243497.2
DBSOURCE    REFSEQ: accession NM_001256568.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Wu,Y., Yu,H., Zheng,S.L., Feng,B., Kapron,A.L., Na,R., Boyle,J.L.,
            Shah,S., Shi,Z., Ewing,C.M., Wiley,K.E., Luo,J., Walsh,P.C.,
            Carter,H.B., Helfand,B.T., Cooney,K.A., Xu,J. and Isaacs,W.B.
  TITLE     Germline mutations in PPFIBP2 are associated with lethal prostate
            cancer
  JOURNAL   Prostate 78 (16), 1222-1228 (2018)
   PUBMED   30043417
  REMARK    GeneRIF: germline mutations in a novel gene, PPFIBP2,
            differentiated risk for lethal prostate cancer from low-risk cases
            and were associated with shorter survival times after diagnosis.
REFERENCE   6  (residues 1 to 764)
  AUTHORS   von Thun,A., Birtwistle,M., Kalna,G., Grindlay,J., Strachan,D.,
            Kolch,W., von Kriegsheim,A. and Norman,J.C.
  TITLE     ERK2 drives tumour cell migration in three-dimensional
            microenvironments by suppressing expression of Rab17 and
            liprin-beta2
  JOURNAL   J Cell Sci 125 (Pt 6), 1465-1477 (2012)
   PUBMED   22328529
  REMARK    GeneRIF: Knockdown of either Rab17 or liprin-beta2 restores
            invasiveness of ERK2-depleted cells, indicating that ERK2 drives
            invasion of MDA-MB-231 cells by suppressing expression of these
            genes.
REFERENCE   7  (residues 1 to 764)
  AUTHORS   Colas,E., Perez,C., Cabrera,S., Pedrola,N., Monge,M., Castellvi,J.,
            Eyzaguirre,F., Gregorio,J., Ruiz,A., Llaurado,M., Rigau,M.,
            Garcia,M., Ertekin,T., Montes,M., Lopez-Lopez,R., Carreras,R.,
            Xercavins,J., Ortega,A., Maes,T., Rosell,E., Doll,A., Abal,M.,
            Reventos,J. and Gil-Moreno,A.
  TITLE     Molecular markers of endometrial carcinoma detected in uterine
            aspirates
  JOURNAL   Int J Cancer 129 (10), 2435-2444 (2011)
   PUBMED   21207424
  REMARK    Erratum:[Int J Cancer. 2012 Jun 15;130(12):E4]
REFERENCE   8  (residues 1 to 764)
  AUTHORS   Stafford,R.L., Tang,M.Y., Sawaya,M.R., Phillips,M.L. and Bowie,J.U.
  TITLE     Crystal structure of the central coiled-coil domain from human
            liprin-beta2
  JOURNAL   Biochemistry 50 (18), 3807-3815 (2011)
   PUBMED   21462929
  REMARK    GeneRIF: analysis of crystal structure of the central coiled-coil
            domain from human liprin-beta2
REFERENCE   9  (residues 1 to 764)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 764)
  AUTHORS   Serra-Pages,C., Medley,Q.G., Tang,M., Hart,A. and Streuli,M.
  TITLE     Liprins, a family of LAR transmembrane protein-tyrosine
            phosphatase-interacting proteins
  JOURNAL   J Biol Chem 273 (25), 15611-15620 (1998)
   PUBMED   9624153
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104237.2.
            
            On May 21, 2020 this sequence version replaced NP_001243497.1.
            
            Summary: This gene encodes a member of the LAR protein-tyrosine
            phosphatase-interacting protein (liprin) family. The encoded
            protein is a beta liprin and plays a role in axon guidance and
            neuronal synapse development by recruiting LAR protein-tyrosine
            phosphatases to the plasma membrane. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene. [provided by RefSeq, Feb 2012].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (2) is shorter and has a distinct N-terminus, compared to isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296718.1, SRR11853567.4796.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..764
                     /product="liprin-beta-2 isoform 2"
                     /note="protein tyrosine phosphatase receptor type f
                     polypeptide-interacting protein-binding protein 2; PTPRF
                     interacting protein, binding protein 2 (liprin beta 2);
                     PPFIA binding protein 2"
                     /calculated_mol_wt=86380
     Region          <1..>205
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          443..506
                     /region_name="SAM_liprin-beta1,2_repeat1"
                     /note="SAM domain of liprin-beta1,2 proteins repeat 1;
                     cd09563"
                     /db_xref="CDD:188962"
     Region          517..579
                     /region_name="SAM_liprin-beta1,2_repeat2"
                     /note="SAM domain of liprin-beta1,2 proteins repeat 2;
                     cd09566"
                     /db_xref="CDD:188965"
     Region          602..673
                     /region_name="SAM_liprin-beta1,2_repeat3"
                     /note="SAM domain of liprin-beta proteins repeat 3;
                     cd09569"
                     /db_xref="CDD:188968"
     CDS             1..764
                     /gene="PPFIBP2"
                     /gene_synonym="Cclp1"
                     /coded_by="NM_001256568.2:150..2444"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58116.1"
                     /db_xref="GeneID:8495"
                     /db_xref="HGNC:HGNC:9250"
                     /db_xref="MIM:603142"
ORIGIN      
        1 msseqwprlp gkvsvltdqv eaqgekirdl evcleghqvk lnaaeemlqq ellsrtslet
       61 qkldlmtevs elklklvgme keqreqeekq rkaeellqel rhlkikveel enernqyewk
      121 lkatkaevaq lqeqvalkda eierlhsqls rtaalhsesh terdqeiqrl kmgmetllla
      181 nedkdrriee ltgllnqyrk vkeivmvtqg psertlsine eepeggfskw natnkdpeel
      241 fkqempprcs sptvgppplp qksletraqk klscsledlr sesvdkcmdg nqpfpvlepk
      301 dspflaehky ptlpgklsga tpngeaaksp pticqpdatg ssllrlrdte sgwddtavvn
      361 dlsstssgte sgpqspltpd gkrnpkgikk fwgkirrtqs gnfytdtlgm aefrrgglra
      421 tagprlsrtr dskgqksdan apfaqwster vcawledfgl aqyvifarqw vssghtllta
      481 tpqdmekelg ikhplhrkkl vlavkaintk qeeksalldh iwvtrwlddi glpqykdqfh
      541 esrvdrrmlq yltvndllfl kvtsqlhhls ikcaihvlhv nkfnphclhr rpadesnlsp
      601 sevvqwsnhr vmewlrsvdl aeyapnlrgs gvhggliile prftgdtlam llnippqktl
      661 lrrhlttkfn aligpeaeqe krekmaspay tpltttakvr prklgfshfg nirkkkfdes
      721 tdyicpmeps dgvsdshrvy sgyrglspld apeldgldqv gqis
//
LOCUS       NP_001274073             145 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor protein D52 isoform 7 [Homo sapiens].
ACCESSION   NP_001274073 XP_005251356
VERSION     NP_001274073.1
DBSOURCE    REFSEQ: accession NM_001287144.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Zhang,J., Li,Z., Han,J., Tian,Z., Meng,Q. and Niu,W.
  TITLE     KLF7 enhances the invasion and migration of colorectal cancer cells
            via the miR-139-5p/TPD52 axis
  JOURNAL   Cancer Biol Ther 25 (1), 2385172 (2024)
   PUBMED   39097779
  REMARK    GeneRIF: KLF7 enhances the invasion and migration of colorectal
            cancer cells via the miR-139-5p/TPD52 axis.
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Li,Y., Zhu,X., Zhang,C., Yin,Y., Chen,L., Liu,Y., He,A. and Xia,F.
  TITLE     Long noncoding RNA FTX promotes epithelial-mesenchymal transition
            of epithelial ovarian cancer through modulating miR-7515/TPD52 and
            activating Met/Akt/mTOR
  JOURNAL   Histol Histopathol 38 (12), 1487-1498 (2023)
   PUBMED   37140169
  REMARK    GeneRIF: Long noncoding RNA FTX promotes epithelial-mesenchymal
            transition of epithelial ovarian cancer through modulating
            miR-7515/TPD52 and activating Met/Akt/mTOR.
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Khan,K., Zafar,S., Badshah,Y., Ashraf,N.M., Rafiq,M., Danish,L.,
            Shabbir,M., Trembley,J.H., Afsar,T., Almajwal,A. and Razak,S.
  TITLE     Cross talk of tumor protein D52 (TPD52) with KLF9, PKCepsilon, and
            MicroRNA 223 in ovarian cancer
  JOURNAL   J Ovarian Res 16 (1), 202 (2023)
   PUBMED   37833790
  REMARK    GeneRIF: Cross talk of tumor protein D52 (TPD52) with KLF9,
            PKCepsilon, and MicroRNA 223 in ovarian cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 145)
  AUTHORS   Liu,S., Hu,C., Li,M., Zhou,W., Wang,R. and Xiao,Y.
  TITLE     Androgen receptor suppresses lung cancer invasion and increases
            cisplatin response via decreasing TPD52 expression
  JOURNAL   Int J Biol Sci 19 (12), 3709-3725 (2023)
   PUBMED   37564195
  REMARK    GeneRIF: Androgen receptor suppresses lung cancer invasion and
            increases cisplatin response via decreasing TPD52 expression.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 145)
  AUTHORS   Wang,R., He,H., Sun,X., Xu,J., Marshall,F.F., Zhau,H., Chung,L.W.,
            Fu,H. and He,D.
  TITLE     Transcription variants of the prostate-specific PrLZ gene and their
            interaction with 14-3-3 proteins
  JOURNAL   Biochem Biophys Res Commun 389 (3), 455-460 (2009)
   PUBMED   19732746
  REMARK    GeneRIF: Alternative splicing may contribute to abnormally enhanced
            PrLZ levels in prostate cancer, and interaction with 14-3-3
            proteins may be a mechanism by which PrLZ promotes cell
            proliferation and survival during prostate cancer development and
            progression.
REFERENCE   7  (residues 1 to 145)
  AUTHORS   Byrne,J.A., Nourse,C.R., Basset,P. and Gunning,P.
  TITLE     Identification of homo- and heteromeric interactions between
            members of the breast carcinoma-associated D52 protein family using
            the yeast two-hybrid system
  JOURNAL   Oncogene 16 (7), 873-881 (1998)
   PUBMED   9484778
REFERENCE   8  (residues 1 to 145)
  AUTHORS   Byrne,J.A., Mattei,M.G. and Basset,P.
  TITLE     Definition of the tumor protein D52 (TPD52) gene family through
            cloning of D52 homologues in human (hD53) and mouse (mD52)
  JOURNAL   Genomics 35 (3), 523-532 (1996)
   PUBMED   8812487
REFERENCE   9  (residues 1 to 145)
  AUTHORS   Chen,S.L., Maroulakou,I.G., Green,J.E., Romano-Spica,V., Modi,W.,
            Lautenberger,J. and Bhat,N.K.
  TITLE     Isolation and characterization of a novel gene expressed in
            multiple cancers
  JOURNAL   Oncogene 12 (4), 741-751 (1996)
   PUBMED   8632896
REFERENCE   10 (residues 1 to 145)
  AUTHORS   Byrne,J.A., Tomasetto,C., Garnier,J.M., Rouyer,N., Mattei,M.G.,
            Bellocq,J.P., Rio,M.C. and Basset,P.
  TITLE     A screening method to identify genes commonly overexpressed in
            carcinomas and the identification of a novel complementary DNA
            sequence
  JOURNAL   Cancer Res 55 (13), 2896-2903 (1995)
   PUBMED   7796418
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC331087.1, DA409017.1, U18914.1, DA079836.1, CB128067.1 and
            BU071387.1.
            
            On Nov 27, 2013 this sequence version replaced XP_005251356.1.
            
            Transcript Variant: This variant (7) contains an alternate 5'
            terminal exon and it thus differs in its 5' UTR and 5' coding
            region, it lacks two alternate in-frame exons in the central coding
            region, and it uses an alternate splice site that results in an
            early stop codon, compared to variant 4. The encoded isoform (7)
            has a distinct N-terminus and is shorter than isoform 4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.430038.1,
                                           SRR7346977.1083311.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.13"
     Protein         1..145
                     /product="tumor protein D52 isoform 7"
                     /EC_number="2.7.1.21"
                     /note="prostate and colon associated protein; prostate
                     leucine zipper; protein N8"
                     /calculated_mol_wt=15889
     Region          44..138
                     /region_name="TPD52"
                     /note="Tumour protein D52 family; pfam04201"
                     /db_xref="CDD:461225"
     CDS             1..145
                     /gene="TPD52"
                     /gene_synonym="D52; hD52; N8L; PC-1; PrLZ"
                     /coded_by="NM_001287144.2:122..559"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:7163"
                     /db_xref="HGNC:HGNC:12005"
                     /db_xref="MIM:604068"
ORIGIN      
        1 mdrgeqgllr tdpvpeeged vaatisatet lseeeqeelr relakveeei qtlsqvlaak
       61 ekhlaeikrk lginslqelk qniakgwqdv tatsaykkts etlsqagqka saafssvgsv
      121 itkkledvkn sptfksfeek venlk
//
LOCUS       NP_005080                482 aa            linear   PRI 21-NOV-2025
DEFINITION  U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa
            subunit-related protein 2 [Homo sapiens].
ACCESSION   NP_005080
VERSION     NP_005080.1
DBSOURCE    REFSEQ: accession NM_005089.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Hannes,L., Atzori,M., Goldenberg,A., Argente,J., Attie-Bitach,T.,
            Amiel,J., Attanasio,C., Braslavsky,D.G., Bruel,A.L., Castanet,M.,
            Dubourg,C., Jacobs,A., Lyonnet,S., Martinez-Mayer,J., Perez
            Millan,M.I., Pezzella,N., Pelgrims,E., Aerden,M., Bauters,M.,
            Rochtus,A., Scaglia,P., Swillen,A., Sifrim,A., Tammaro,R.,
            Mau-Them,F.T., Odent,S., Thauvin-Robinet,C., Franco,B. and
            Breckpot,J.
  TITLE     Differential alternative splicing analysis links variation in ZRSR2
            to a novel type of oral-facial-digital syndrome
  JOURNAL   Genet Med 26 (4), 101059 (2024)
   PUBMED   38158857
  REMARK    GeneRIF: Differential alternative splicing analysis links variation
            in ZRSR2 to a novel type of oral-facial-digital syndrome.
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Kwon,Y.S., Jin,S.W. and Song,H.
  TITLE     Global analysis of binding sites of U2AF1 and ZRSR2 reveals RNA
            elements required for mutually exclusive splicing by the U2- and
            U12-type spliceosome
  JOURNAL   Nucleic Acids Res 52 (3), 1420-1434 (2024)
   PUBMED   38088204
  REMARK    GeneRIF: Global analysis of binding sites of U2AF1 and ZRSR2
            reveals RNA elements required for mutually exclusive splicing by
            the U2- and U12-type spliceosome.
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Togami,K., Chung,S.S., Madan,V., Booth,C.A.G., Kenyon,C.M.,
            Cabal-Hierro,L., Taylor,J., Kim,S.S., Griffin,G.K., Ghandi,M.,
            Li,J., Li,Y.Y., Angelot-Delettre,F., Biichle,S., Seiler,M.,
            Buonamici,S., Lovitch,S.B., Louissaint,A. Jr., Morgan,E.A.,
            Jardin,F., Piccaluga,P.P., Weinstock,D.M., Hammerman,P.S., Yang,H.,
            Konopleva,M., Pemmaraju,N., Garnache-Ottou,F., Abdel-Wahab,O.,
            Koeffler,H.P. and Lane,A.A.
  TITLE     Sex-Biased ZRSR2 Mutations in Myeloid Malignancies Impair
            Plasmacytoid Dendritic Cell Activation and Apoptosis
  JOURNAL   Cancer Discov 12 (2), 522-541 (2022)
   PUBMED   34615655
  REMARK    GeneRIF: Sex-Biased ZRSR2 Mutations in Myeloid Malignancies Impair
            Plasmacytoid Dendritic Cell Activation and Apoptosis.
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Will,C.L., Schneider,C., Hossbach,M., Urlaub,H., Rauhut,R.,
            Elbashir,S., Tuschl,T. and Luhrmann,R.
  TITLE     The human 18S U11/U12 snRNP contains a set of novel proteins not
            found in the U2-dependent spliceosome
  JOURNAL   RNA 10 (6), 929-941 (2004)
   PUBMED   15146077
REFERENCE   7  (residues 1 to 482)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   8  (residues 1 to 482)
  AUTHORS   Brunner,B., Todt,T., Lenzner,S., Stout,K., Schulz,U., Ropers,H.H.
            and Kalscheuer,V.M.
  TITLE     Genomic structure and comparative analysis of nine Fugu genes:
            conservation of synteny with human chromosome Xp22.2-p22.1
  JOURNAL   Genome Res 9 (5), 437-448 (1999)
   PUBMED   10330123
REFERENCE   9  (residues 1 to 482)
  AUTHORS   Tronchere,H., Wang,J. and Fu,X.D.
  TITLE     A protein related to splicing factor U2AF35 that interacts with
            U2AF65 and SR proteins in splicing of pre-mRNA
  JOURNAL   Nature 388 (6640), 397-400 (1997)
   PUBMED   9237760
REFERENCE   10 (residues 1 to 482)
  AUTHORS   Kitagawa,K., Wang,X., Hatada,I., Yamaoka,T., Nojima,H., Inazawa,J.,
            Abe,T., Mitsuya,K., Oshimura,M., Murata,A. et al.
  TITLE     Isolation and mapping of human homologues of an imprinted mouse
            gene U2af1-rs1
  JOURNAL   Genomics 30 (2), 257-263 (1995)
   PUBMED   8586425
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC113480.1.
            
            Summary: This gene encodes an essential splicing factor. The
            encoded protein associates with the U2 auxiliary factor
            heterodimer, which is required for the recognition of a functional
            3' splice site in pre-mRNA splicing, and may play a role in network
            interactions during spliceosome assembly. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC050451.1, D49677.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307771.8/ ENSP00000303015.7
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..482
                     /product="U2 small nuclear ribonucleoprotein auxiliary
                     factor 35 kDa subunit-related protein 2"
                     /note="U2AF35-related protein; zinc finger (CCCH type),
                     RNA binding motif and serine/arginine rich 2; U2(RNU2)
                     small nuclear RNA auxiliary factor 1-like 2; U2 small
                     nuclear ribonucleoprotein auxiliary factor, small subunit
                     2; renal carcinoma antigen NY-REN-20"
                     /calculated_mol_wt=57914
     Region          1..59
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15696.2)"
     Region          115..135
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15696.2)"
     Region          167..191
                     /region_name="zf-CCCH"
                     /note="Zinc finger C-x8-C-x5-C-x3-H type (and similar);
                     pfam00642"
                     /db_xref="CDD:459885"
     Region          199..303
                     /region_name="RRM_U2AFBPL"
                     /note="RNA recognition motif (RRM) found in U2 small
                     nuclear ribonucleoprotein auxiliary factor 35 kDa
                     subunit-related protein 1 (U2AFBPL) and similar proteins;
                     cd12540"
                     /db_xref="CDD:409956"
     Region          306..331
                     /region_name="ZnF_C3H1"
                     /note="zinc finger; smart00356"
                     /db_xref="CDD:214632"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15696.2)"
     Region          351..482
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15696.2)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15696.2)"
     CDS             1..482
                     /gene="ZRSR2"
                     /gene_synonym="OFD21; U2AF1-RS2; U2AF1L2; U2AF1RS2; URP;
                     ZC3H22"
                     /coded_by="NM_005089.4:13..1461"
                     /db_xref="CCDS:CCDS14172.1"
                     /db_xref="GeneID:8233"
                     /db_xref="HGNC:HGNC:23019"
                     /db_xref="MIM:300028"
ORIGIN      
        1 maapekmtfp ekpshkkyra alkkekrkkr rqelarlrds glsqkeeeed tfieeqqlee
       61 ekllererqr lheewllreq kaqeefrikk ekeeaakkrq eeqerklkeq weeqqrkere
      121 eeeqkrqekk ekeealqkml dqaeneleng ttwqnpeppv dfrvmekdra ncpfysktga
      181 crfgdrcsrk hnfptssptl liksmfttfg meqcrrddyd pdasleysee etyqqfldfy
      241 edvlpefknv gkviqfkvsc nlephlrgnv yvqyqseeec qaalslfngr wyagrqlqce
      301 fcpvtrwkma icglfeiqqc prgkhcnflh vfrnpnnefw eanrdiylsp drtgssfgkn
      361 serrermghh ddyysrlrgr rnpspdhsyk rngeserkss rhrgkkshkr tsksrerhns
      421 rsrgrnrdrs rdrsrgrgsr srsrsrsrrs rrsrsqsssr srsrgrrrsg nrdrtvqspk
      481 sk
//
LOCUS       NP_001362947             786 aa            linear   PRI 21-NOV-2025
DEFINITION  protein 4.1 isoform 11 [Homo sapiens].
ACCESSION   NP_001362947 XP_016856076
VERSION     NP_001362947.1
DBSOURCE    REFSEQ: accession NM_001376018.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 786)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 786)
  AUTHORS   Terada,N., Saitoh,Y., Saito,M., Yamada,T., Kamijo,A., Yoshizawa,T.
            and Sakamoto,T.
  TITLE     Recent Progress on Genetically Modified Animal Models for Membrane
            Skeletal Proteins: The 4.1 and MPP Families
  JOURNAL   Genes (Basel) 14 (10), 1942 (2023)
   PUBMED   37895291
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 786)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 786)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 786)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 786)
  AUTHORS   Dalla Venezia,N., Gilsanz,F., Alloisio,N., Ducluzeau,M.T.,
            Benz,E.J. Jr. and Delaunay,J.
  TITLE     Homozygous 4.1(-) hereditary elliptocytosis associated with a point
            mutation in the downstream initiation codon of protein 4.1 gene
  JOURNAL   J Clin Invest 90 (5), 1713-1717 (1992)
   PUBMED   1430200
REFERENCE   7  (residues 1 to 786)
  AUTHORS   Jons,T. and Drenckhahn,D.
  TITLE     Identification of the binding interface involved in linkage of
            cytoskeletal protein 4.1 to the erythrocyte anion exchanger
  JOURNAL   EMBO J 11 (8), 2863-2867 (1992)
   PUBMED   1639060
REFERENCE   8  (residues 1 to 786)
  AUTHORS   Subrahmanyam,G., Bertics,P.J. and Anderson,R.A.
  TITLE     Phosphorylation of protein 4.1 on tyrosine-418 modulates its
            function in vitro
  JOURNAL   Proc Natl Acad Sci U S A 88 (12), 5222-5226 (1991)
   PUBMED   1647028
REFERENCE   9  (residues 1 to 786)
  AUTHORS   Conboy,J.G., Chan,J.Y., Chasis,J.A., Kan,Y.W. and Mohandas,N.
  TITLE     Tissue- and development-specific alternative RNA splicing regulates
            expression of multiple isoforms of erythroid membrane protein 4.1
  JOURNAL   J Biol Chem 266 (13), 8273-8280 (1991)
   PUBMED   2022644
REFERENCE   10 (residues 1 to 786)
  AUTHORS   Horne,W.C., Prinz,W.C. and Tang,E.K.
  TITLE     Identification of two cAMP-dependent phosphorylation sites on
            erythrocyte protein 4.1
  JOURNAL   Biochim Biophys Acta 1055 (1), 87-92 (1990)
   PUBMED   2171679
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL009181.1, AL138785.8 and
            AL357500.17.
            
            On Nov 7, 2019 this sequence version replaced XP_016856076.1.
            
            Summary: The protein encoded by this gene, together with spectrin
            and actin, constitute the red cell membrane cytoskeletal network.
            This complex plays a critical role in erythrocyte shape and
            deformability. Mutations in this gene are associated with type 1
            elliptocytosis (EL1). Alternatively spliced transcript variants
            encoding different isoforms have been described for this
            gene.[provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.207499.1,
                                           SRR1803615.234125.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.3"
     Protein         1..786
                     /product="protein 4.1 isoform 11"
                     /note="protein 4.1; erythrocyte surface protein band 4.1;
                     P4.1; EPB4.1; elliptocytosis 1, RH-linked"
                     /calculated_mol_wt=88919
     Region          1..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11171.4)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:15525677,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Region          77..>204
                     /region_name="WTX"
                     /note="WTX protein; pfam09422"
                     /db_xref="CDD:462794"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48193; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Region          136..170
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11171.4)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Region          182..202
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11171.4)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P11171.4)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Region          211..401
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P48193; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Region          396..489
                     /region_name="FERM_C_4_1_family"
                     /note="FERM domain C-lobe of Protein 4.1 family; cd13184"
                     /db_xref="CDD:270005"
     Site            order(405,422,424,430)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270005"
     Site            order(434,439..442,477,481,484..485)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Site            477..488
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Region          499..542
                     /region_name="FA"
                     /note="FERM adjacent (FA); pfam08736"
                     /db_xref="CDD:462582"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:2171679,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Region          585..610
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11171.4)"
     Region          614..712
                     /region_name="Spectrin--actin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P11171.4)"
     Site            659
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by EGFR.
                     /evidence=ECO:0000269|PubMed:1647028,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            663
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48193; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Region          666..714
                     /region_name="SAB"
                     /note="SAB domain; pfam04382"
                     /db_xref="CDD:461285"
     Site            673
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            683
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            708
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:2171679,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            711
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:15525677,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     CDS             1..786
                     /gene="EPB41"
                     /gene_synonym="4.1R; EL1; HE"
                     /coded_by="NM_001376018.1:208..2568"
                     /note="isoform 11 is encoded by transcript variant 12"
                     /db_xref="GeneID:2035"
                     /db_xref="HGNC:HGNC:3377"
                     /db_xref="MIM:130500"
ORIGIN      
        1 mttekslvte aensqhqqke egeeainsgq qepqqeescq taaegdnwce qklkasngdt
       61 pthedltknk ertsesrgls rlfssflkrp ksqvseeegk evesdkekge ggqkeiefgt
      121 sldeeiilka piaapepelk tdpsldlhsl ssaetqpaqe elredpdfei kegegleecs
      181 kievkeespq skaetelkas qkpirkhrnm hckvsllddt vyecvvekha kgqdllkrvc
      241 ehlnlleedy fglaiwdnat sktwldsake ikkqvrgvpw nftfnvkfyp pdpaqltedi
      301 tryylclqlr qdivagrlpc sfatlallgs ytiqselgdy dpelhgvdyv sdfklapnqt
      361 keleekvmel hksyrsmtpa qadleflena kklsmygvdl hkakdlegvd iilgvcssgl
      421 lvykdklrin rfpwpkvlki sykrssffik irpgeqeqye stigfklpsy raakklwkvc
      481 vehhtffrlt stdtipkskf lalgskfrys grtqaqtrqa salidrpaph fertaskras
      541 rsldgaavds adrsprptsa paitqgqvae ggvldasakk tvvpkaqket vkaevkkede
      601 ppeqaepept eawkvekthi evtvptsngd qtqklaekte dlirmrkkkr erldgeniyi
      661 rhsnlmledl dksqeeikkh hasiselkkn fmesvpeprp sewdkrlsth spfrtlning
      721 qiptgegvkk tsvlpserkv ggpespsyfl pdtyhlgvck epvlnfqtdq rrlaqlrelr
      781 akffls
//
LOCUS       NP_001358987             175 aa            linear   PRI 21-NOV-2025
DEFINITION  ephrin-B2 isoform 4 precursor [Homo sapiens].
ACCESSION   NP_001358987
VERSION     NP_001358987.1
DBSOURCE    REFSEQ: accession NM_001372058.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Wang,X., Zhang,Z., Hu,G. and Zhou,X.
  TITLE     Hypoxia-Induced Ephrin-B2 Facilitates Proliferation and Induces
            Glycolytic Metabolism in Cutaneous Squamous Cell Carcinoma by
            Modulating PKM2/HIF-1alpha Axis
  JOURNAL   Discov Med 36 (187), 1692-1702 (2024)
   PUBMED   39190384
  REMARK    GeneRIF: Hypoxia-Induced Ephrin-B2 Facilitates Proliferation and
            Induces Glycolytic Metabolism in Cutaneous Squamous Cell Carcinoma
            by Modulating PKM2/HIF-1alpha Axis.
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Zhang,Q., Li,J., Liu,F., Hu,J., Liu,F., Zou,J. and Wang,X.
  TITLE     Ephrin B2 (EFNB2) potentially protects against intervertebral disc
            degeneration through inhibiting nucleus pulposus cell apoptosis
  JOURNAL   Arch Biochem Biophys 756, 109990 (2024)
   PUBMED   38636690
  REMARK    GeneRIF: Ephrin B2 (EFNB2) potentially protects against
            intervertebral disc degeneration through inhibiting nucleus
            pulposus cell apoptosis.
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Sesen,J., Ghalali,A., Driscoll,J., Martinez,T., Lupieri,A.,
            Zurakowski,D., Alexandrescu,S., Smith,E.R. and Fehnel,K.P.
  TITLE     Discovery and Characterization of Ephrin B2 and EphB4 Dysregulation
            and Novel Mutations in Cerebral Cavernous Malformations: In Vitro
            and Patient-Derived Evidence of Ephrin-Mediated Endothelial Cell
            Pathophysiology
  JOURNAL   Cell Mol Neurobiol 44 (1), 12 (2023)
   PUBMED   38150042
  REMARK    GeneRIF: Discovery and Characterization of Ephrin B2 and EphB4
            Dysregulation and Novel Mutations in Cerebral Cavernous
            Malformations: In Vitro and Patient-Derived Evidence of
            Ephrin-Mediated Endothelial Cell Pathophysiology.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Li,W., Su,S.A., Chen,J., Shen,Y., Ma,H. and Xiang,M.
  TITLE     EphrinB2 drives osteogenic fate of adult cardiac fibroblasts in a
            calcium influx dependent manner
  JOURNAL   Am J Physiol Cell Physiol 325 (1), C69-C78 (2023)
   PUBMED   37212547
  REMARK    GeneRIF: EphrinB2 drives osteogenic fate of adult cardiac
            fibroblasts in a calcium influx dependent manner.
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Holland,S.J., Gale,N.W., Mbamalu,G., Yancopoulos,G.D.,
            Henkemeyer,M. and Pawson,T.
  TITLE     Bidirectional signalling through the EPH-family receptor Nuk and
            its transmembrane ligands
  JOURNAL   Nature 383 (6602), 722-725 (1996)
   PUBMED   8878483
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Cerretti,D.P., Lyman,S.D., Kozlosky,C.J., Copeland,N.G.,
            Gilbert,D.J., Jenkins,N.A., Valentine,V., Kirstein,M.N.,
            Shapiro,D.N. and Morris,S.W.
  TITLE     The genes encoding the eph-related receptor tyrosine kinase ligands
            LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4,
            Epl4) are clustered on human chromosome 1 and mouse chromosome 3
  JOURNAL   Genomics 33 (2), 277-282 (1996)
   PUBMED   8660976
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Cerretti,D.P., Vanden Bos,T., Nelson,N., Kozlosky,C.J., Reddy,P.,
            Maraskovsky,E., Park,L.S., Lyman,S.D., Copeland,N.G., Gilbert,D.J.
            et al.
  TITLE     Isolation of LERK-5: a ligand of the eph-related receptor tyrosine
            kinases
  JOURNAL   Mol Immunol 32 (16), 1197-1205 (1995)
   PUBMED   8559144
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Bennett,B.D., Zeigler,F.C., Gu,Q., Fendly,B., Goddard,A.D.,
            Gillett,N. and Matthews,W.
  TITLE     Molecular cloning of a ligand for the EPH-related receptor
            protein-tyrosine kinase Htk
  JOURNAL   Proc Natl Acad Sci U S A 92 (6), 1866-1870 (1995)
   PUBMED   7534404
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Bonaldo,M.F., Yu,M.T., Jelenc,P., Brown,S., Su,L., Lawton,L.,
            Deaven,L., Efstratiadis,A., Warburton,D. and Soares,M.B.
  TITLE     Selection of cDNAs using chromosome-specific genomic clones:
            application to human chromosome 13
  JOURNAL   Hum Mol Genet 3 (9), 1663-1673 (1994)
   PUBMED   7833926
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138689.22.
            
            Summary: This gene encodes a member of the ephrin (EPH) family. The
            ephrins and EPH-related receptors comprise the largest subfamily of
            receptor protein-tyrosine kinases and have been implicated in
            mediating developmental events, especially in the nervous system
            and in erythropoiesis. Based on their structures and sequence
            relationships, ephrins are divided into the ephrin-A (EFNA) class,
            which are anchored to the membrane by a
            glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB)
            class, which are transmembrane proteins. This gene encodes an EFNB
            class ephrin which binds to the EPHB4 and EPHA3 receptors.
            [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138515.149040.1,
                                           ERR4352443.769730.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA2142853 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q33.3"
     Protein         1..175
                     /product="ephrin-B2 isoform 4 precursor"
                     /note="HTK ligand; ligand of eph-related kinase 5;
                     eph-related receptor tyrosine kinase ligand 5"
                     /calculated_mol_wt=17275
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2945
     Region          29..>136
                     /region_name="Cupredoxin"
                     /note="Cupredoxin superfamily; cl19115"
                     /db_xref="CDD:473140"
     Site            36
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:18488039,
                     ECO:0000269|PubMed:19836338; propagated from
                     UniProtKB/Swiss-Prot (P52799.1)"
     CDS             1..175
                     /gene="EFNB2"
                     /gene_synonym="ephrin-B2; EPLG5; Htk-L; HTKL; LERK5"
                     /coded_by="NM_001372058.1:699..1226"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:1948"
                     /db_xref="HGNC:HGNC:3227"
                     /db_xref="MIM:600527"
ORIGIN      
        1 mavrrdsvwk ycwgvlmvlc rtaisksivl epiywnssns kflpgqglvl ypqigdkldi
       61 icpkvdsktv gqyeyykvym vdkdqadrct ikkentplln cakpdqdikf tikfqefspn
      121 lwglefqknk dyyiisvifv igyssescqr lciwdlggys ttttlplskr nrsts
//
LOCUS       NP_001252510             508 aa            linear   PRI 21-NOV-2025
DEFINITION  TELO2-interacting protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001252510
VERSION     NP_001252510.1
DBSOURCE    REFSEQ: accession NM_001265581.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Kim,Y., Park,J., Joo,S.Y., Kim,B.G., Jo,A., Lee,H. and Cho,Y.
  TITLE     Structure of the Human TELO2-TTI1-TTI2 Complex
  JOURNAL   J Mol Biol 434 (2), 167370 (2022)
   PUBMED   34838521
  REMARK    GeneRIF: Structure of the Human TELO2-TTI1-TTI2 Complex.
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Rao,F., Cha,J., Xu,J., Xu,R., Vandiver,M.S., Tyagi,R., Tokhunts,R.,
            Koldobskiy,M.A., Fu,C., Barrow,R., Wu,M., Fiedler,D., Barrow,J.C.
            and Snyder,S.H.
  TITLE     Inositol pyrophosphates mediate the DNA-PK/ATM-p53 cell death
            pathway by regulating CK2 phosphorylation of Tti1/Tel2
  JOURNAL   Mol Cell 54 (1), 119-132 (2014)
   PUBMED   24657168
  REMARK    Erratum:[Mol Cell. 2020 Aug 20;79(4):702. doi:
            10.1016/j.molcel.2020.07.021. PMID: 32822581]
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Langouet,M., Saadi,A., Rieunier,G., Moutton,S., Siquier-Pernet,K.,
            Fernet,M., Nitschke,P., Munnich,A., Stern,M.H., Chaouch,M. and
            Colleaux,L.
  TITLE     Mutation in TTI2 reveals a role for triple T complex in human brain
            development
  JOURNAL   Hum Mutat 34 (11), 1472-1476 (2013)
   PUBMED   23956177
  REMARK    GeneRIF: The findings emphasises the role of the TTI2 gene in the
            etiology of intellectual disability.
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Takai,H., Xie,Y., de Lange,T. and Pavletich,N.P.
  TITLE     Tel2 structure and function in the Hsp90-dependent maturation of
            mTOR and ATR complexes
  JOURNAL   Genes Dev 24 (18), 2019-2030 (2010)
   PUBMED   20801936
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Hurov,K.E., Cotta-Ramusino,C. and Elledge,S.J.
  TITLE     A genetic screen identifies the Triple T complex required for DNA
            damage signaling and ATM and ATR stability
  JOURNAL   Genes Dev 24 (17), 1939-1950 (2010)
   PUBMED   20810650
  REMARK    GeneRIF: TTI1 and TTI2 protect cells from spontaneous DNA damage,
            and are required for the establishment of the intra-S and G2/M
            checkpoint.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091144.12.
            
            Summary: This gene encodes a regulator of the DNA damage response.
            The protein is a component of the Triple T complex (TTT) which also
            includes telomere length regulation protein and TELO2 interacting
            protein 1. The TTT complex is involved in cellular resistance to
            DNA damage stresses and may act as a regulator of
            phosphoinositide-3-kinase-related protein kinase (PIKK) abundance.
            [provided by RefSeq, May 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX648410.1, SRR18074968.1612159.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p12"
     Protein         1..508
                     /product="TELO2-interacting protein 2 isoform 1"
                     /note="Tel2 interacting protein 2 homolog"
                     /calculated_mol_wt=56784
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXR4.1)"
     Region          <219..384
                     /region_name="Tti2"
                     /note="Tti2 family; pfam10521"
                     /db_xref="CDD:431336"
     CDS             1..508
                     /gene="TTI2"
                     /gene_synonym="C8orf41; MRT39"
                     /coded_by="NM_001265581.2:276..1802"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS6090.1"
                     /db_xref="GeneID:80185"
                     /db_xref="HGNC:HGNC:26262"
                     /db_xref="MIM:614426"
ORIGIN      
        1 meldsaleap sqedsnlsee lshsafgqaf skilhclarp earrgnvkda vlkdlgdlie
       61 atefdrlfeg tgarlrgmpe tlgqvakale kyaapskeee gggdghseaa ekaaqvgllf
      121 lkllgkveta knslvgpawq tglhhlagpv yifaithsle qpwttprsre varevltsll
      181 qvtecgsvag flhgenedek grlsvilgll kpdlykeswk nnpaikhvfs wtlqqvtrpw
      241 lsqhlervlp aslvisddyq tenkilgvhc lhhivlnvpa adllqynraq vlyhaisnhl
      301 ytpehhliqa vllclldlfp ilektlhwkg dgarptthcd evlrlilthm epehrlllrr
      361 tyarnlpafv nrlgiltvrh lkrlerviig ylevydgpee earlkiletl kllmqhtwpr
      421 vscrlvvllk allklicdva rdpnltpesv ksallqeatd clilldrcsq grvkgllaki
      481 pqscedrkvv nyirkvqqvs egapyngt
//
LOCUS       NP_001186672             152 aa            linear   PRI 21-NOV-2025
DEFINITION  dynactin subunit 5 isoform 3 [Homo sapiens].
ACCESSION   NP_001186672
VERSION     NP_001186672.1
DBSOURCE    REFSEQ: accession NM_001199743.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 152)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 152)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 152)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   7  (residues 1 to 152)
  AUTHORS   Olson,J.E., Wang,X., Pankratz,V.S., Fredericksen,Z.S., Vachon,C.M.,
            Vierkant,R.A., Cerhan,J.R. and Couch,F.J.
  TITLE     Centrosome-related genes, genetic variation, and risk of breast
            cancer
  JOURNAL   Breast Cancer Res Treat 125 (1), 221-228 (2011)
   PUBMED   20508983
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 152)
  AUTHORS   Parisi,G., Fornasari,M.S. and Echave,J.
  TITLE     Dynactins p25 and p27 are predicted to adopt the LbetaH fold
  JOURNAL   FEBS Lett 562 (1-3), 1-4 (2004)
   PUBMED   15043994
REFERENCE   9  (residues 1 to 152)
  AUTHORS   Eckley,D.M., Gill,S.R., Melkonian,K.A., Bingham,J.B., Goodson,H.V.,
            Heuser,J.E. and Schroer,T.A.
  TITLE     Analysis of dynactin subcomplexes reveals a novel actin-related
            protein associated with the arp1 minifilament pointed end
  JOURNAL   J Cell Biol 147 (2), 307-320 (1999)
   PUBMED   10525537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA310703.1, CD388246.1 and
            AC008870.8.
            
            Summary: This gene encodes a subunit of dynactin, a component of
            the cytoplasmic dynein motor machinery involved in
            minus-end-directed transport. The encoded protein is a component of
            the pointed-end subcomplex and is thought to bind membranous cargo.
            A pseudogene of this gene is located on the long arm of chromosome
            1. Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene. [provided by RefSeq, Jan
            2011].
            
            Transcript Variant: This variant (4) uses an alternate splice site
            in the 3' coding region, which results in a frameshift, compared to
            variant 1. It encodes isoform 3, which has a shorter and distinct
            C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.144098.1,
                                           SRR6380201.159660.7 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..152
                     /product="dynactin subunit 5 isoform 3"
                     /note="dynactin 4; dynactin subunit p25; dynactin 5 (p25)"
                     /calculated_mol_wt=16502
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9BTE1.1)"
     Region          13..151
                     /region_name="LbH_Dynactin_5"
                     /note="Dynactin 5 (or subunit p25); Dynactin is a major
                     component of the activator complex that stimulates
                     dynein-mediated vesicle transport. Dynactin is a
                     heterocomplex of at least eight subunits, including a
                     150,000-MW protein called Glued, the actin-capping...;
                     cd03359"
                     /db_xref="CDD:100049"
     CDS             1..152
                     /gene="DCTN5"
                     /coded_by="NM_001199743.2:78..536"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS58436.1"
                     /db_xref="GeneID:84516"
                     /db_xref="HGNC:HGNC:24594"
                     /db_xref="MIM:612962"
ORIGIN      
        1 melgellynk seyietasgn kvsrqsvlcg sqnivlngkt ivmndciirg dlanvrvgrh
       61 cvvksrsvir ppfkkfskgv affplhigdh vfieedcvvn aaqigsyvhv gkncvigrrc
      121 vlkdcckild ntvlppetvv ppftvfsgcp ap
//
LOCUS       NP_835145                161 aa            linear   PRI 21-NOV-2025
DEFINITION  structure-specific endonuclease subunit SLX1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_835145
VERSION     NP_835145.1
DBSOURCE    REFSEQ: accession NM_178044.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Payliss,B.J., Patel,A., Sheppard,A.C. and Wyatt,H.D.M.
  TITLE     Exploring the Structures and Functions of Macromolecular
            SLX4-Nuclease Complexes in Genome Stability
  JOURNAL   Front Genet 12, 784167 (2021)
   PUBMED   34804132
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Wan,B., Yin,J., Horvath,K., Sarkar,J., Chen,Y., Wu,J., Wan,K.,
            Lu,J., Gu,P., Yu,E.Y., Lue,N.F., Chang,S., Liu,Y. and Lei,M.
  TITLE     SLX4 assembles a telomere maintenance toolkit by bridging multiple
            endonucleases with telomeres
  JOURNAL   Cell Rep 4 (5), 861-869 (2013)
   PUBMED   24012755
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Fekairi,S., Scaglione,S., Chahwan,C., Taylor,E.R., Tissier,A.,
            Coulon,S., Dong,M.Q., Ruse,C., Yates,J.R. 3rd, Russell,P.,
            Fuchs,R.P., McGowan,C.H. and Gaillard,P.H.L.
  TITLE     Human SLX4 is a Holliday junction resolvase subunit that binds
            multiple DNA repair/recombination endonucleases
  JOURNAL   Cell 138 (1), 78-89 (2009)
   PUBMED   19596236
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Svendsen,J.M., Smogorzewska,A., Sowa,M.E., O'Connell,B.C.,
            Gygi,S.P., Elledge,S.J. and Harper,J.W.
  TITLE     Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and
            is required for DNA repair
  JOURNAL   Cell 138 (1), 63-77 (2009)
   PUBMED   19596235
REFERENCE   5  (residues 1 to 161)
  AUTHORS   Andersen,S.L., Bergstralh,D.T., Kohl,K.P., LaRocque,J.R.,
            Moore,C.B. and Sekelsky,J.
  TITLE     Drosophila MUS312 and the vertebrate ortholog BTBD12 interact with
            DNA structure-specific endonucleases in DNA repair and
            recombination
  JOURNAL   Mol Cell 35 (1), 128-135 (2009)
   PUBMED   19595722
REFERENCE   6  (residues 1 to 161)
  AUTHORS   Munoz,I.M., Hain,K., Declais,A.C., Gardiner,M., Toh,G.W.,
            Sanchez-Pulido,L., Heuckmann,J.M., Toth,R., Macartney,T.,
            Eppink,B., Kanaar,R., Ponting,C.P., Lilley,D.M. and Rouse,J.
  TITLE     Coordination of structure-specific nucleases by human SLX4/BTBD12
            is required for DNA repair
  JOURNAL   Mol Cell 35 (1), 116-127 (2009)
   PUBMED   19595721
REFERENCE   7  (residues 1 to 161)
  AUTHORS   Hildebrandt,M.A., Salavaggione,O.E., Martin,Y.N., Flynn,H.C.,
            Jalal,S., Wieben,E.D. and Weinshilboum,R.M.
  TITLE     Human SULT1A3 pharmacogenetics: gene duplication and functional
            genomic studies
  JOURNAL   Biochem Biophys Res Commun 321 (4), 870-878 (2004)
   PUBMED   15358107
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC133555.3.
            
            Summary: This gene encodes a protein that is an important regulator
            of genome stability. The protein represents the catalytic subunit
            of the SLX1-SLX4 structure-specific endonuclease, which can resolve
            DNA secondary structures that are formed during repair and
            recombination processes. Two identical copies of this gene are
            located on the p arm of chromosome 16 due to a segmental
            duplication; this record represents the more telomeric copy.
            Alternative splicing results in multiple transcript variants.
            Read-through transcription also occurs between this gene and the
            downstream SULT1A4 (sulfotransferase family, cytosolic, 1A,
            phenol-preferring, member 4) gene. [provided by RefSeq, Nov 2010].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the central coding region, compared to variant 1, resulting
            in an isoform (2) that is shorter than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC069007.1, BF976357.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..161
                     /product="structure-specific endonuclease subunit SLX1
                     isoform 2"
                     /note="GIY-YIG domain-containing protein 1; SLX1
                     structure-specific endonuclease subunit homolog B; SLX1
                     homolog B, structure-specific endonuclease subunit"
                     /calculated_mol_wt=17881
     Region          13..82
                     /region_name="GIY-YIG_SLX1"
                     /note="Catalytic GIY-YIG domain of yeast
                     structure-specific endonuclease subunit SLX1 and its
                     eukaryotic homologs; cd10455"
                     /db_xref="CDD:198402"
     Site            order(15..17,31..33)
                     /site_type="other"
                     /note="GIY-YIG motif/motif A"
                     /db_xref="CDD:198402"
     Site            order(17,31,33,41,45,82)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:198402"
     Site            82
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:198402"
     CDS             1..161
                     /gene="SLX1B"
                     /gene_synonym="GIYD2"
                     /coded_by="NM_178044.4:211..696"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10649.1"
                     /db_xref="GeneID:79008"
                     /db_xref="HGNC:HGNC:28748"
                     /db_xref="MIM:615823"
ORIGIN      
        1 mgpagvaarp grffgvylly clnpryrgrv yvgftvntar rvqqhnggrk kggawrtsgr
       61 gpwemvlvvh gfpssvaalr deegplccph pgcllrahvi claeeflqee pgqllplegq
      121 cpcceksllw gdliwlcqmd tekevedsel eeahwtdlle t
//
LOCUS       NP_001305253            2080 aa            linear   PRI 21-NOV-2025
DEFINITION  nuclear pore complex protein Nup214 isoform 3 [Homo sapiens].
ACCESSION   NP_001305253 XP_005272274
VERSION     NP_001305253.1
DBSOURCE    REFSEQ: accession NM_001318324.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2080)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2080)
  AUTHORS   Choi,Y.J., Min,Y.K., Lee,S.T., Choi,J.R. and Shin,S.
  TITLE     NUP214 Rearrangements in Leukemia Patients: A Case Series From a
            Single Institution
  JOURNAL   Ann Lab Med 44 (4), 335-342 (2024)
   PUBMED   38145892
  REMARK    GeneRIF: NUP214 Rearrangements in Leukemia Patients: A Case Series
            From a Single Institution.
REFERENCE   3  (residues 1 to 2080)
  AUTHORS   Wang,J., Zhan,Q.R., Lu,X.X., Zhang,L.J., Wang,X.X. and Zhang,H.Y.
  TITLE     The characteristics and prognostic significance of the
            SET-CAN/NUP214 fusion gene in hematological malignancies: A
            systematic review
  JOURNAL   Medicine (Baltimore) 101 (30), e29294 (2022)
   PUBMED   35905214
  REMARK    GeneRIF: The characteristics and prognostic significance of the
            SET-CAN/NUP214 fusion gene in hematological malignancies: A
            systematic review.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2080)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 2080)
  AUTHORS   Zheng,Y.Z., Wen,J.J., Wang,L.Y., Zheng,H., Hua,X.L., Li,J. and
            Hu,J.D.
  TITLE     [SET-NUP214-positive pediatric acute myeloid leukemia: a report of
            two cases]
  JOURNAL   Zhonghua Xue Ye Xue Za Zhi 42 (9), 769 (2021)
   PUBMED   34753234
  REMARK    GeneRIF: [SET-NUP214-positive pediatric acute myeloid leukemia: a
            report of two cases].
REFERENCE   6  (residues 1 to 2080)
  AUTHORS   Napetschnig,J., Blobel,G. and Hoelz,A.
  TITLE     Crystal structure of the N-terminal domain of the human
            protooncogene Nup214/CAN
  JOURNAL   Proc Natl Acad Sci U S A 104 (6), 1783-1788 (2007)
   PUBMED   17264208
  REMARK    GeneRIF: A mechanism is proposed by which the C-terminal peptide
            extension is involved in nuclear pore complex assembly.
REFERENCE   7  (residues 1 to 2080)
  AUTHORS   Pilz,A., Woodward,K., Povey,S. and Abbott,C.
  TITLE     Comparative mapping of 50 human chromosome 9 loci in the laboratory
            mouse
  JOURNAL   Genomics 25 (1), 139-149 (1995)
   PUBMED   7774911
REFERENCE   8  (residues 1 to 2080)
  AUTHORS   Kraemer,D., Wozniak,R.W., Blobel,G. and Radu,A.
  TITLE     The human CAN protein, a putative oncogene product associated with
            myeloid leukemogenesis, is a nuclear pore complex protein that
            faces the cytoplasm
  JOURNAL   Proc Natl Acad Sci U S A 91 (4), 1519-1523 (1994)
   PUBMED   8108440
REFERENCE   9  (residues 1 to 2080)
  AUTHORS   von Lindern,M., Fornerod,M., van Baal,S., Jaegle,M., de Wit,T.,
            Buijs,A. and Grosveld,G.
  TITLE     The translocation (6;9), associated with a specific subtype of
            acute myeloid leukemia, results in the fusion of two genes, dek and
            can, and the expression of a chimeric, leukemia-specific dek-can
            mRNA
  JOURNAL   Mol Cell Biol 12 (4), 1687-1697 (1992)
   PUBMED   1549122
REFERENCE   10 (residues 1 to 2080)
  AUTHORS   von Lindern,M., Poustka,A., Lerach,H. and Grosveld,G.
  TITLE     The (6;9) chromosome translocation, associated with a specific
            subtype of acute nonlymphocytic leukemia, leads to aberrant
            transcription of a target gene on 9q34
  JOURNAL   Mol Cell Biol 10 (8), 4016-4026 (1990)
   PUBMED   2370860
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC105998.1 and AL157938.22.
            
            On Jan 1, 2016 this sequence version replaced XP_005272274.1.
            
            Summary: The nuclear pore complex is a massive structure that
            extends across the nuclear envelope, forming a gateway that
            regulates the flow of macromolecules between the nucleus and the
            cytoplasm. Nucleoporins are the main components of the nuclear pore
            complex in eukaryotic cells. This gene is a member of the
            FG-repeat-containing nucleoporins. The protein encoded by this gene
            is localized to the cytoplasmic face of the nuclear pore complex
            where it is required for proper cell cycle progression and
            nucleocytoplasmic transport. The 3' portion of this gene forms a
            fusion gene with the DEK gene on chromosome 6 in a t(6,9)
            translocation associated with acute myeloid leukemia and
            myelodysplastic syndrome. Alternative splicing of this gene results
            in multiple transcript variants encoding different isoforms.
            [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (3) uses two alternate splice
            sites at internal exons, compared to variant 2. It encodes isoform
            3, which is shorter than isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105998.1, SRR14038192.2673450.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2080
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..2080
                     /product="nuclear pore complex protein Nup214 isoform 3"
                     /note="CAN protein, putative oncogene; nuclear pore
                     complex protein Nup214; nucleoporin 214kDa"
                     /calculated_mol_wt=212512
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglycine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          39..91
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          41..404
                     /region_name="Seven-bladed beta propeller"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          <94..265
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          96..144
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          152..190
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          155..>216
                     /region_name="ANAPC4_WD40"
                     /note="Anaphase-promoting complex subunit 4 WD40 domain;
                     pfam12894"
                     /db_xref="CDD:403945"
     Region          196..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          243..291
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          304..350
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          362..401
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          422..460
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            444..445
                     /site_type="other"
                     /note="Breakpoint for translocation to form the
                     NUP214-ABL1 fusion protein.
                     /evidence=ECO:0000269|PubMed:15361874; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          450..586
                     /region_name="(Microbial infection) Binds human adenovirus
                     5 (HAdV-5) protein L3 (hexon).
                     /evidence=ECO:0000269|PubMed:25410864"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          489..536
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          <497..>681
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            656
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          730..758
                     /region_name="Leucine-zipper 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            750
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            802..803
                     /site_type="other"
                     /note="Breakpoint; propagated from UniProtKB/Swiss-Prot
                     (P35658.2)"
     Region          851..872
                     /region_name="Leucine-zipper 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            930
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            960
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            964
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          977..999
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            979
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1011
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1013
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          <1023..1702
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1035
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1046
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1071
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          1118..1142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            1124
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1140
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1146
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          1158..1203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            1171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          1224..1306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            1302
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          1327..1398
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            1343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          1399..2074
                     /region_name="18 X 4 AA approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          1417..2075
                     /region_name="11 X 3 AA approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          1428..1457
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          1469..1529
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          1586..>2070
                     /region_name="COG4625"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal beta-barrel porin domain [Function unknown]"
                     /db_xref="CDD:443664"
     Site            1830..1831
                     /site_type="other"
                     /note="Breakpoint for translocation to form the
                     NUP214-ABL1 fusion protein.
                     /evidence=ECO:0000269|PubMed:15361874; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          1874..1893
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          1906..1967
                     /region_name="Nup214_FG"
                     /note="Nucleoporin Nup214 phenylalanine-glycine (FG)
                     domain; pfam18617"
                     /db_xref="CDD:408399"
     Site            1906..1907
                     /site_type="other"
                     /note="Breakpoint for translocation to form the
                     NUP214-ABL1 fusion protein.
                     /evidence=ECO:0000269|PubMed:15361874; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1953
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1957..1958
                     /site_type="other"
                     /note="Breakpoint for translocation to form the
                     NUP214-ABL1 fusion protein.
                     /evidence=ECO:0000269|PubMed:15361874; Breakpoint for
                     translocation to form the NUP214-SQSTM1 fusion protein.
                     /evidence=ECO:0000269|PubMed:20851865; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1975
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            2061..2062
                     /site_type="other"
                     /note="Breakpoint for translocation to form the
                     NUP214-ABL1 fusion protein.
                     /evidence=ECO:0000269|PubMed:15361874; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          2075..2076
                     /region_name="44. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     CDS             1..2080
                     /gene="NUP214"
                     /gene_synonym="CAIN; CAN; IIAE9"
                     /coded_by="NM_001318324.2:120..6362"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS83429.1"
                     /db_xref="GeneID:8021"
                     /db_xref="HGNC:HGNC:8064"
                     /db_xref="MIM:114350"
ORIGIN      
        1 mgdemdamip eremkdfqfr alkkvrifds peelpkerss llavsnkygl vfaggasglq
       61 ifptknlliq nkpgddpnki vdkvqgllvp mkfpihhlal scdnltlsac mmsseygsii
      121 affdvrtfsn eakqqkrpfa yhkllkdagg mvidmkwnpt vpsmvavcla dgsiavlqvt
      181 etvkvcatlp stvavtsvcw spkgkqlavg kqngtvvqyl ptlqekkvip cppfyesdhp
      241 vrvldvlwig tyvfaivyaa adgtletspd vvmallpkke ekhpeifvnf mepcygscte
      301 rqhhyylsyi eewdlvlaas aastevsila rqsdqinwes wlledssrae lpvtdksdds
      361 lpmgvvvdyt nqveitisde ktlppapvlm llstdgvlcp fyminqnpgv ksliktperl
      421 slegerqpks pgstpttpts sqapqkldas aaaapaslpp sspaapiatf sllpaggapt
      481 vfsfgssslk ssatvtgepp syssgsdssk aapgpgpstf sfvppskasl aptpaaspva
      541 psaasfsfgs sgfkptlest pvpsvsapni amkpsfppst savkvnlsen ssqsappmsp
      601 fssaskpaas gplshptpls appssvplks svlpspsagr saqgssspvp smvqksprit
      661 ppaakpgspq akslqpavae kqghqwkdsd pvmagigeei ahfqkeleel kartskacfq
      721 vgtseemkml rtesddlhtf lleikettes lhgdisslkt tllegfagve eareqnernr
      781 dsgylhllyk rpldpkseaq lqeirrlhqy vkfavqdvnd vldlewdqhl eqkkkqrhll
      841 vperetlfnt lannreiinq qrkrlnhlvd slqqlrlykq tslwslssav psqssihsfd
      901 sdleslcnal lkttieshtk slpkvpakls pmkqaqlrnf lakrktppvr stapaslsrs
      961 aflsqryyed ldevsstssv sqslesedar tsckddeavv qaprhapvvr tpsiqpsllp
     1021 haapfakshl vhgsspgvmg tsvatsaski ipqgadstml atktvkhgap spshpisapq
     1081 aaaaaalrrq masqapavnt ltestlknvp qvvnvqelkn npatpstamg ssvpystakt
     1141 phpvltpvaa nqakqgslin slkpsgptpa sgqlssgdka sgtakietav tstpsasgqf
     1201 skpfsfspsg tgfnfgiitp tpssnftaaq gatpstkess qpdafssggg skpsyeaipe
     1261 ssppsgitsa snttpgepaa sssrpvapsg talsttsskl etppsklgel lfpsslaget
     1321 lgsfsglrvg qaddstkptn kasstsltst qptktsgvps gfnftappvl gkhteppvts
     1381 satttsvapp aatstsstav fgslpvtsag ssgvisfggt slsagktsfs fgsqqtnstv
     1441 ppsappptta atplptsfpt lsfgsllssa ttpslpmsag rsteeatssa lpekpgdsev
     1501 sasaasllee qqsaqlpqap pqtsdsvkke pvlaqpavsn sgtaasstsl valsaeatpa
     1561 ttgvpdarte avppassfsv pgqtavtaaa issagpvave tsstpiasst tsivapgpsa
     1621 eaaafgtvts gssvfaqppa assssafnql tnntatapsa tpvfgqvaas tapslfgqqt
     1681 gstastaaat pqvsssgfss pafgttapgv fgqttfgqas vfgqsassaa svfsfsqpgf
     1741 ssvpafgqpa sstptstsgs vfgaasstss sssfsfgqss pntggglfgq snapafgqsp
     1801 gfgqggsvfg gtsaatttaa tsgfsfcqas gfgssntgsv fgqaastggi vfgqqsssss
     1861 gsvfgsgntg rgggffsglg gkpsqdaank npfssasggf gstatsntsn lfgnsgaktf
     1921 ggfasssfge qkptgtfssg ggsvasqgfg fsspnktggf gaapvfgspp tfggspgfgg
     1981 vpafgsapaf tsplgstggk vfgegtaaas aggfgfgsss nttsfgtlas qnaptfgsls
     2041 qqtsgfgtqs sgfsgfgsgt ggfsfgsnns svqgfggwrs
//
LOCUS       NP_001371740             987 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 118 [Homo sapiens].
ACCESSION   NP_001371740
VERSION     NP_001371740.1
DBSOURCE    REFSEQ: accession NM_001384811.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 987)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 987)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 987)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 987)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 987)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 987)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 987)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.38631.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..987
                     /product="microtubule-associated protein 4 isoform 118"
                     /note="MAP-4"
                     /calculated_mol_wt=104151
     Region          <552..829
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <698..972
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          <836..857
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          859..888
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          890..920
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..987
                     /gene="MAP4"
                     /coded_by="NM_001384811.1:96..3059"
                     /note="isoform 118 is encoded by transcript variant 70"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiegsptef leekmayqey pnsqnwpedt nfcfqpeqvv dpiqtdpfkm
      121 yhdddladlv fpssatadts ifagqndplk dsygmspcnt avvpqgwsve alnsphsesf
      181 vspeavaepp qptavplela keiemaseer ppaqaleimm glkttdmaps ketemalakd
      241 malatkteva lakdmesptk ldvtlakdmq psmesdmalv kdmelpteke valvkdvrwp
      301 tetdvssakn vvlpteteva pakdvtllke teraspikmd lapskdmgpp kenkketera
      361 spikmdlaps kdmgppkenk ivpakdlvll seievaqand iissteissa ekvalssete
      421 valardmtlp petnviltkd kalpleaeva pvkdmaqlpe teiapakdva pstvkevgll
      481 kdmsplsete malgkdvtpp petevvlikn vclppemeva ltedqvpalk teaplakdgv
      541 ltlannvtpa kdvpplsete atpvpikdme iaqtqkgise dshleslqdv gqsaaptfmi
      601 spetvtgtgk kcslpaeeds vleklgerkp cnsqpselss etsgiarpee grpvvsgtgn
      661 dittppnkel ppspekktkp iadakapekr aspskpasap asrsgskstq tvaktttaaa
      721 vastgpssrs pstllpkkpt aiktegkpae vkkmtaksvp adlsrpksts tssmkktttl
      781 sgtapaagvv psrvkatpmp srpsttpfid kkptsakpss ttprlsrlat ntsapdlknv
      841 rskvgsteni khqpgggrvq iqnkkvdisk vsskcgskan ikhkpgggdv kiesqklnfk
      901 ekaqakvgsl dnvghlpagg avktegggse aplcpgppag eepaiseaap eagaptsasg
      961 lnghptlsgg gdqreaqtld sqiqetn
//
LOCUS       NP_079352                420 aa            linear   PRI 21-NOV-2025
DEFINITION  UDP-glucuronic acid decarboxylase 1 isoform 2 [Homo sapiens].
ACCESSION   NP_079352
VERSION     NP_079352.2
DBSOURCE    REFSEQ: accession NM_025076.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Jacobs,J., Lyubenova,H., Potelle,S., Kopp,J., Gerin,I., Chan,W.L.,
            Rodriguez de Los Santos,M., Hulsemann,W., Mensah,M.A.,
            Cormier-Daire,V., Joosten,M., Bruggenwirth,H.T., Stuurman,K.E.,
            Miranda,V., Campeau,P.M., Wittler,L., Graff,J., Mundlos,S.,
            Ibrahim,D.M., Van Schaftingen,E., Fischer-Zirnsak,B., Kornak,U.,
            Ehmke,N. and Bommer,G.T.
  TITLE     A missing enzyme-rescue metabolite as cause of a rare skeletal
            dysplasia
  JOURNAL   Nature 646 (8083), 218-226 (2025)
   PUBMED   40836090
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Brewer,G.
  TITLE     UXS1: a sweet spot for cell death
  JOURNAL   Nat Rev Cancer 24 (1), 3 (2024)
   PUBMED   38030856
  REMARK    GeneRIF: UXS1: a sweet spot for cell death.
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Walsh,R.M. Jr., Polizzi,S.J., Kadirvelraj,R., Howard,W.W. and
            Wood,Z.A.
  TITLE     Man o' war mutation in UDP-alpha-D-xylose synthase favors the
            abortive catalytic cycle and uncovers a latent potential for
            hexamer formation
  JOURNAL   Biochemistry 54 (3), 807-819 (2015)
   PUBMED   25521717
  REMARK    GeneRIF: The persistence of a latent hexamer-building interface in
            the human enzyme suggests that the ancestral UXS may have been a
            hexamer.
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Polizzi,S.J., Walsh,R.M. Jr., Le Magueres,P., Criswell,A.R. and
            Wood,Z.A.
  TITLE     Human UDP-alpha-d-xylose synthase forms a catalytically important
            tetramer that has not been observed in crystal structures
  JOURNAL   Biochemistry 52 (22), 3888-3898 (2013)
   PUBMED   23656592
  REMARK    GeneRIF: hUXS forms a tetramer in solution that is important for
            activity. The higher activity of the tetramer coupled with the
            relative instability of the dimeric complex suggests that an
            association-dissociation mechanism may regulate hUXS activity.
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Polizzi,S.J., Walsh,R.M. Jr., Peeples,W.B., Lim,J.M., Wells,L. and
            Wood,Z.A.
  TITLE     Human UDP-alpha-D-xylose synthase and Escherichia coli ArnA
            conserve a conformational shunt that controls whether xylose or
            4-keto-xylose is produced
  JOURNAL   Biochemistry 51 (44), 8844-8855 (2012)
   PUBMED   23072385
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   7  (residues 1 to 420)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   8  (residues 1 to 420)
  AUTHORS   Bakker,H., Oka,T., Ashikov,A., Yadav,A., Berger,M., Rana,N.A.,
            Bai,X., Jigami,Y., Haltiwanger,R.S., Esko,J.D. and
            Gerardy-Schahn,R.
  TITLE     Functional UDP-xylose transport across the endoplasmic
            reticulum/Golgi membrane in a Chinese hamster ovary cell mutant
            defective in UDP-xylose Synthase
  JOURNAL   J Biol Chem 284 (4), 2576-2583 (2009)
   PUBMED   19028698
  REMARK    GeneRIF: Complementation was achieved by expression of a
            cytoplasmic variant of UDP-xylose Synthase, which proves the
            existence of a functional Golgi UDP-xylose transporter[UDP-xylose
            Synthase]
REFERENCE   9  (residues 1 to 420)
  AUTHORS   Hwang,H.Y. and Horvitz,H.R.
  TITLE     The SQV-1 UDP-glucuronic acid decarboxylase and the SQV-7
            nucleotide-sugar transporter may act in the Golgi apparatus to
            affect Caenorhabditis elegans vulval morphogenesis and embryonic
            development
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14218-14223 (2002)
   PUBMED   12391314
REFERENCE   10 (residues 1 to 420)
  AUTHORS   Moriarity,J.L., Hurt,K.J., Resnick,A.C., Storm,P.B., Laroy,W.,
            Schnaar,R.L. and Snyder,S.H.
  TITLE     UDP-glucuronate decarboxylase, a key enzyme in proteoglycan
            synthesis: cloning, characterization, and localization
  JOURNAL   J Biol Chem 277 (19), 16968-16975 (2002)
   PUBMED   11877387
  REMARK    GeneRIF: UDP-glucuronate decarboxylase, a key enzyme in
            proteoglycan synthesis: cloning, characterization, and
            localization.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC018878.8.
            
            On Feb 10, 2004 this sequence version replaced NP_079352.1.
            
            Summary: This gene encodes an enzyme found in the perinuclear Golgi
            which catalyzes the synthesis of UDP-xylose used in
            glycosaminoglycan (GAG) synthesis on proteoglycans. The GAG chains
            are covalently attached to proteoglycans which participate in
            signaling pathways during development. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Dec 2014].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 5' coding region compared to variant 1. The
            resulting protein (isoform 2) is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK075120.1, AY358541.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q12.2"
     Protein         1..420
                     /product="UDP-glucuronic acid decarboxylase 1 isoform 2"
                     /EC_number="4.1.1.35"
                     /note="short chain dehydrogenase/reductase family 6E,
                     member 12; UDP-glucuronic acid decarboxylase 1; UXS-1"
                     /calculated_mol_wt=47446
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:25732826; propagated from
                     UniProtKB/Swiss-Prot (Q8NBZ7.1)"
     Region          4..78
                     /region_name="UXS1_N"
                     /note="UDP-glucuronate decarboxylase N-terminal;
                     pfam11803"
                     /db_xref="CDD:463356"
     Site            20..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBZ7.1)"
     Region          89..392
                     /region_name="UGD_SDR_e"
                     /note="UDP-glucuronate decarboxylase (UGD) and related
                     proteins, extended (e) SDRs; cd05230"
                     /db_xref="CDD:187541"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8NBZ7.1)"
     Site            order(95,97..100,119..124,143..145,159..163,178,200..202,
                     231,235,258..261,272)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:187541"
     Site            order(148..149,184..185,188..189,191..192,245)
                     /site_type="other"
                     /note="putative substrate binding site 2 [chemical
                     binding]"
                     /db_xref="CDD:187541"
     Site            order(165,228,260,271..273,276..277,288..290,295,297,331,
                     357,361)
                     /site_type="other"
                     /note="putative substrate binding site 1 [chemical
                     binding]"
                     /db_xref="CDD:187541"
     Site            order(179,202,231,235)
                     /site_type="active"
                     /db_xref="CDD:187541"
     Site            316
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NBZ7.1)"
     CDS             1..420
                     /gene="UXS1"
                     /gene_synonym="hUXS; hUXS1; SDR6E1; UGD"
                     /coded_by="NM_025076.5:61..1323"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS46378.1"
                     /db_xref="GeneID:80146"
                     /db_xref="HGNC:HGNC:17729"
                     /db_xref="MIM:609749"
ORIGIN      
        1 mvskallrlv savnrrrmkl llgiallayv asvwgnfvnm rsiqengelk ieskieemve
       61 plrekirdle ksftqkyppv kflsekdrkr ilitggagfv gshltdklmm dghevtvvdn
      121 fftgrkrnve hwighenfel inhdvveply ievdqiyhla spasppnymy npiktlktnt
      181 igtlnmlgla krvgarllla stsevygdpe vhpqsedywg hvnpigprac ydegkrvaet
      241 mcyaymkqeg vevrvarifn tfgprmhmnd grvvsnfilq alqgepltvy gsgsqtrafq
      301 yvsdlvnglv almnsnvssp vnlgnpeeht ilefaqlikn lvgsgseiqf lseaqddpqk
      361 rkpdikkakl mlgwepvvpl eeglnkaihy frkeleyqan nqyipkpkpa rikkgrtrhs
//
LOCUS       NP_001120664             179 aa            linear   PRI 21-NOV-2025
DEFINITION  CCHC-type zinc finger nucleic acid binding protein isoform 1 [Homo
            sapiens].
ACCESSION   NP_001120664
VERSION     NP_001120664.1
DBSOURCE    REFSEQ: accession NM_001127192.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Liu,X., Chen,Y., Li,Y., Bai,J., Zeng,Z., Wang,M., Dong,Y. and
            Zhou,Y.
  TITLE     STAU1-mediated CNBP mRNA degradation by LINC00665 alters stem cell
            characteristics in ovarian cancer
  JOURNAL   Biol Direct 19 (1), 59 (2024)
   PUBMED   39080743
  REMARK    GeneRIF: STAU1-mediated CNBP mRNA degradation by LINC00665 alters
            stem cell characteristics in ovarian cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Liu,Y., Jiang,H., Hu,K., Zou,H., Zhang,W., Liu,J. and Jian,X.
  TITLE     CircPRMT5 promotes progression of osteosarcoma by recruiting CNBP
            to regulate the translation and stability of CDK6 mRNA
  JOURNAL   PLoS One 19 (4), e0298947 (2024)
   PUBMED   38626179
  REMARK    GeneRIF: CircPRMT5 promotes progression of osteosarcoma by
            recruiting CNBP to regulate the translation and stability of CDK6
            mRNA.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Gil Rosas,M., Centola,C., Torres,M., Mouguelar,V.S., David,A.P.,
            Piga,E.J., Gomez,D., Calcaterra,N.B., Armas,P. and Coux,G.
  TITLE     The transcription of the main gene associated with Treacher-Collins
            syndrome (TCOF1) is regulated by G-quadruplexes and cellular
            nucleic acid binding protein (CNBP)
  JOURNAL   Sci Rep 14 (1), 7472 (2024)
   PUBMED   38553547
  REMARK    GeneRIF: The transcription of the main gene associated with
            Treacher-Collins syndrome (TCOF1) is regulated by G-quadruplexes
            and cellular nucleic acid binding protein (CNBP).
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Chen,Y., Lei,X., Jiang,Z., Humphries,F., Parsi,K.M., Mustone,N.J.,
            Ramos,I., Mutetwa,T., Fernandez-Sesma,A., Maehr,R., Caffrey,D.R.
            and Fitzgerald,K.A.
  TITLE     Cellular nucleic acid-binding protein restricts SARS-CoV-2 by
            regulating interferon and disrupting RNA-protein condensates
  JOURNAL   Proc Natl Acad Sci U S A 120 (47), e2308355120 (2023)
   PUBMED   37963251
  REMARK    GeneRIF: Cellular nucleic acid-binding protein restricts SARS-CoV-2
            by regulating interferon and disrupting RNA-protein condensates.
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Liu,H., Fang,Y., Hou,B., Lin,Q., Zhang,W., Wang,X., Hu,Y., Xu,G.
            and He,Z.
  TITLE     CircPACRGL promoted cell proliferation, migration and invasion as
            well as inhibited cell apoptosis in colorectal cancer via
            regulation of the miR-330-3p/CNBP axis
  JOURNAL   Mol Cell Biochem 478 (7), 1633-1644 (2023)
   PUBMED   36459268
  REMARK    GeneRIF: CircPACRGL promoted cell proliferation, migration and
            invasion as well as inhibited cell apoptosis in colorectal cancer
            via regulation of the miR-330-3p/CNBP axis.
REFERENCE   6  (residues 1 to 179)
  AUTHORS   Flink,I.L. and Morkin,E.
  TITLE     Organization of the gene encoding cellular nucleic acid-binding
            protein
  JOURNAL   Gene 163 (2), 279-282 (1995)
   PUBMED   7590281
REFERENCE   7  (residues 1 to 179)
  AUTHORS   Warden,C.H., Krisans,S.K., Purcell-Huynh,D., Leete,L.M.,
            Daluiski,A., Diep,A., Taylor,B.A. and Lusis,A.J.
  TITLE     Mouse cellular nucleic acid binding proteins: a highly conserved
            family identified by genetic mapping and sequencing
  JOURNAL   Genomics 24 (1), 14-19 (1994)
   PUBMED   7896269
REFERENCE   8  (residues 1 to 179)
  AUTHORS   Kleefeld,F., Erdmann,H. and Schoser,B.
  TITLE     Myotonic Dystrophy Type 2
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301639
REFERENCE   9  (residues 1 to 179)
  AUTHORS   Lusis,A.J., Rajavashisth,T.B., Klisak,I., Heinzmann,C., Mohandas,T.
            and Sparkes,R.S.
  TITLE     Mapping of the gene for CNBP, a finger protein, to human chromosome
            3q13.3-q24
  JOURNAL   Genomics 8 (2), 411-414 (1990)
   PUBMED   2249857
  REMARK    Erratum:[Genomics 1991 Mar;9(3):564]
REFERENCE   10 (residues 1 to 179)
  AUTHORS   Rajavashisth,T.B., Taylor,A.K., Andalibi,A., Svenson,K.L. and
            Lusis,A.J.
  TITLE     Identification of a zinc finger protein that binds to the sterol
            regulatory element
  JOURNAL   Science 245 (4918), 640-643 (1989)
   PUBMED   2562787
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK292119.1, AC108673.11 and
            BU616793.1.
            
            Summary: This gene encodes a nucleic-acid binding protein with
            seven zinc-finger domains. The protein has a preference for binding
            single stranded DNA and RNA. The protein functions in
            cap-independent translation of ornithine decarboxylase mRNA, and
            may also function in sterol-mediated transcriptional regulation. A
            CCTG expansion from <30 repeats to 75-11000 repeats in the first
            intron of this gene results in myotonic dystrophy type 2. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant represents the longest transcript
            and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.64152.1,
                                           SRR3476690.1077928.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2155590
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.3"
     Protein         1..179
                     /product="CCHC-type zinc finger nucleic acid binding
                     protein isoform 1"
                     /note="zinc finger protein 273; cellular nucleic
                     acid-binding protein; erythroid differentiation-related;
                     zinc finger protein 9 (a cellular retroviral nucleic acid
                     binding protein); sterol regulatory element-binding
                     protein"
                     /calculated_mol_wt=19560
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P62633.1)"
     Site            8
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P53996; propagated from
                     UniProtKB/Swiss-Prot (P62633.1)"
     Region          25..38
                     /region_name="RNA-binding Arg/Gly-rich region (RGG-box).
                     /evidence=ECO:0000269|PubMed:28329689"
                     /note="propagated from UniProtKB/Swiss-Prot (P62633.1)"
     Site            25
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:24726729; propagated from
                     UniProtKB/Swiss-Prot (P62633.1)"
     Site            27
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:24726729; propagated from
                     UniProtKB/Swiss-Prot (P62633.1)"
     Site            32
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P62633.1)"
     Site            34
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P62633.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53996; propagated from
                     UniProtKB/Swiss-Prot (P62633.1)"
     Region          54..173
                     /region_name="PTZ00368"
                     /note="universal minicircle sequence binding protein
                     (UMSBP); Provisional"
                     /db_xref="CDD:173561"
     Site            75
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P62633.1)"
     Site            81
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P62633.1)"
     Site            82
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P62633.1)"
     CDS             1..179
                     /gene="CNBP"
                     /gene_synonym="CNBP1; DM2; PROMM; RNF163; ZCCHC22; ZNF9"
                     /coded_by="NM_001127192.2:136..675"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46906.1"
                     /db_xref="GeneID:7555"
                     /db_xref="HGNC:HGNC:13164"
                     /db_xref="MIM:116955"
ORIGIN      
        1 mssnecfkcg rsghwarecp tgggrgrgmr srgrggftsd rgfqfvsssl pdicyrcges
       61 ghlakdcdlq edveacyncg rgghiakdck epkrereqcc yncgkpghla rdcdhadeqk
      121 cyscgefghi qkdctkvkcy rcgetghvai ncsktsevnc yrcgesghla rectieata
//
LOCUS       NP_001056                455 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 1A isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_001056
VERSION     NP_001056.1
DBSOURCE    REFSEQ: accession NM_001065.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Alam,M.S., Gaida,M.M., Witzel,H.R., Otsuka,S., Abbasi,A.,
            Guerin,T., Abdelmaksoud,A., Wong,N., Cam,M.C., Kozlov,S. and
            Ashwell,J.D.
  TITLE     TNFR1 signaling promotes pancreatic tumor growth by limiting
            dendritic cell number and function
  JOURNAL   Cell Rep Med 5 (9), 101696 (2024)
   PUBMED   39178856
  REMARK    GeneRIF: TNFR1 signaling promotes pancreatic tumor growth by
            limiting dendritic cell number and function.
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Montoya-Buelna,M., Alvarado-Navarro,A., Munoz-Valle,J.F.,
            Lopez-Roa,R.I., Guerrero-Velazquez,C. and Fafutis-Morris,M.
  TITLE     Association of polymorphisms in the TNFA, TNFRSF1A and TNFRSF1B
            genes with lepromatous leprosy in Western Mexican patients
  JOURNAL   J Infect Dev Ctries 18 (5), 770-778 (2024)
   PUBMED   38865403
  REMARK    GeneRIF: Association of polymorphisms in the TNFA, TNFRSF1A and
            TNFRSF1B genes with lepromatous leprosy in Western Mexican
            patients.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 455)
  AUTHORS   da Silva,P.B., Romao-Veiga,M., Ribeiro-Vasques,V.R., Peracoli,J.C.,
            Peracoli,M.T.S. and Amaral,L.M.
  TITLE     Progesterone modulates TNF receptors expression by Jurkat cells
            cultured with plasma from pregnant women with preeclampsia
  JOURNAL   Int Immunopharmacol 130, 111701 (2024)
   PUBMED   38382266
  REMARK    GeneRIF: Progesterone modulates TNF receptors expression by Jurkat
            cells cultured with plasma from pregnant women with preeclampsia.
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Liphaus,B.L., Silva,S.C., Palmeira,P., Silva,C.A.,
            Goldenstein-Schainberg,C. and Carneiro-Sampaio,M.
  TITLE     Reduced expressions of apoptosis-related proteins TRAIL, Bcl-2, and
            TNFR1 in NK cells of juvenile-onset systemic lupus erythematosus
            patients: relations with disease activity, nephritis, and
            neuropsychiatric involvement
  JOURNAL   Front Immunol 15, 1327255 (2024)
   PUBMED   38562920
  REMARK    GeneRIF: Reduced expressions of apoptosis-related proteins TRAIL,
            Bcl-2, and TNFR1 in NK cells of juvenile-onset systemic lupus
            erythematosus patients: relations with disease activity, nephritis,
            and neuropsychiatric involvement.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 455)
  AUTHORS   McDermott,M.F., Aksentijevich,I., Galon,J., McDermott,E.M.,
            Ogunkolade,B.W., Centola,M., Mansfield,E., Gadina,M., Karenko,L.,
            Pettersson,T., McCarthy,J., Frucht,D.M., Aringer,M., Torosyan,Y.,
            Teppo,A.M., Wilson,M., Karaarslan,H.M., Wan,Y., Todd,I., Wood,G.,
            Schlimgen,R., Kumarajeewa,T.R., Cooper,S.M., Vella,J.P., Amos,C.I.,
            Mulley,J., Quane,K.A., Molloy,M.G., Ranki,A., Powell,R.J.,
            Hitman,G.A., O'Shea,J.J. and Kastner,D.L.
  TITLE     Germline mutations in the extracellular domains of the 55 kDa TNF
            receptor, TNFR1, define a family of dominantly inherited
            autoinflammatory syndromes
  JOURNAL   Cell 97 (1), 133-144 (1999)
   PUBMED   10199409
REFERENCE   6  (residues 1 to 455)
  AUTHORS   Deuitch,N., Cudrici,C., Ombrello,A. and Aksentijevich,I.
  TITLE     TNF Receptor-Associated Periodic Fever Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36375008
REFERENCE   7  (residues 1 to 455)
  AUTHORS   Zhang,X.M., Weber,I. and Chen,M.J.
  TITLE     Site-directed mutational analysis of human tumor necrosis
            factor-alpha receptor binding site and structure-functional
            relationship
  JOURNAL   J Biol Chem 267 (33), 24069-24075 (1992)
   PUBMED   1331108
REFERENCE   8  (residues 1 to 455)
  AUTHORS   Fuchs,P., Strehl,S., Dworzak,M., Himmler,A. and Ambros,P.F.
  TITLE     Structure of the human TNF receptor 1 (p60) gene (TNFR1) and
            localization to chromosome 12p13 [corrected]
  JOURNAL   Genomics 13 (1), 219-224 (1992)
   PUBMED   1315717
  REMARK    Erratum:[Genomics 1992 Aug;13(4):1384]
REFERENCE   9  (residues 1 to 455)
  AUTHORS   Derre,J., Kemper,O., Cherif,D., Nophar,Y., Berger,R. and Wallach,D.
  TITLE     The gene for the type 1 tumor necrosis factor receptor (TNF-R1) is
            localized on band 12p13
  JOURNAL   Hum Genet 87 (2), 231-233 (1991)
   PUBMED   1648547
REFERENCE   10 (residues 1 to 455)
  AUTHORS   Belokrylov,G.A. and Zhitnukhin,Iu.L.
  TITLE     [Effect of antibodies to rat and human cerebral cortex and white
            matter on heterologous T- and B-cells]
  JOURNAL   Zh Mikrobiol Epidemiol Immunobiol (9), 66-70 (1976)
   PUBMED   1087798
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK315509.1, M63121.1 and
            BC010140.2.
            
            Summary: This gene encodes a member of the TNF receptor superfamily
            of proteins. The encoded receptor is found in membrane-bound and
            soluble forms that interact with membrane-bound and soluble forms,
            respectively, of its ligand, tumor necrosis factor alpha. Binding
            of membrane-bound tumor necrosis factor alpha to the membrane-bound
            receptor induces receptor trimerization and activation, which plays
            a role in cell survival, apoptosis, and inflammation. Proteolytic
            processing of the encoded receptor results in release of the
            soluble form of the receptor, which can interact with free tumor
            necrosis factor alpha to inhibit inflammation. Mutations in this
            gene underlie tumor necrosis factor receptor-associated periodic
            syndrome (TRAPS), characterized by fever, abdominal pain and other
            features. Mutations in this gene may also be associated with
            multiple sclerosis in human patients. [provided by RefSeq, Sep
            2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M58286.1, M63121.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000162749.7/ ENSP00000162749.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..455
                     /product="tumor necrosis factor receptor superfamily
                     member 1A isoform 1 precursor"
                     /note="tumor necrosis factor-alpha receptor; tumor
                     necrosis factor binding protein 1; tumor necrosis factor
                     receptor type 1; TNF-R1; TNF-RI; TNFR-I; tumor necrosis
                     factor receptor superfamily member 1A"
                     /calculated_mol_wt=47521
     sig_peptide     1..29
                     /note="/evidence=ECO:0000269|PubMed:2158862; propagated
                     from UniProtKB/Swiss-Prot (P19438.1)"
                     /calculated_mol_wt=2993
     mat_peptide     30..455
                     /product="Tumor necrosis factor receptor superfamily
                     member 1A, membrane form. /id=PRO_0000034543"
                     /note="propagated from UniProtKB/Swiss-Prot (P19438.1)"
                     /calculated_mol_wt=47521
     mat_peptide     41..201
                     /product="Tumor necrosis factor-binding protein 1.
                     /id=PRO_0000034544"
                     /note="propagated from UniProtKB/Swiss-Prot (P19438.1)"
                     /calculated_mol_wt=18181
     Region          43..82
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P19438.1)"
     Region          44..175
                     /region_name="TNFRSF1A"
                     /note="Tumor necrosis factor receptor superfamily member
                     1A (TNFRSF1A), also known as TNFR1; cd10576"
                     /db_xref="CDD:276902"
     Site            order(44..46,50,89,98,100..101,103,106,108,122,133,
                     135..136,173,175)
                     /site_type="other"
                     /note="antiparallel homodimerization interface
                     [polypeptide binding]"
                     /db_xref="CDD:276902"
     Region          44..81
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276902"
     Site            order(46..48,60..66,78,83,93,119..120,159,162,165..167,
                     174)
                     /site_type="other"
                     /note="parallel homodimerization interface [polypeptide
                     binding]"
                     /db_xref="CDD:276902"
     Site            54
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19438.1)"
     Region          83..125
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P19438.1)"
     Region          84..125
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276902"
     Site            order(88,98..101,104,106..108,142)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:276902"
     Region          126..166
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P19438.1)"
     Region          127..166
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276902"
     Site            145
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19438.1)"
     Site            151
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19438.1)"
     Region          167..196
                     /region_name="TNFR-Cys 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P19438.1)"
     Site            212..232
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19438.1)"
     Region          250..>366
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          254..273
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P19438.1)"
     Region          338..348
                     /region_name="N-SMase activation domain (NSD)"
                     /note="propagated from UniProtKB/Swiss-Prot (P19438.1)"
     Region          358..438
                     /region_name="Death_TNFR1"
                     /note="Death domain of Tumor Necrosis Factor Receptor 1;
                     cd08313"
                     /db_xref="CDD:176729"
     Site            376
                     /site_type="glycosylation"
                     /note="(Microbial infection) N-beta-linked (GlcNAc)
                     arginine. /evidence=ECO:0000269|PubMed:30979585,
                     ECO:0000305|PubMed:23955153; propagated from
                     UniProtKB/Swiss-Prot (P19438.1)"
     CDS             1..455
                     /gene="TNFRSF1A"
                     /gene_synonym="CD120a; FPF; p55; p55-R; p60; TBP1; TNF-R;
                     TNF-R-I; TNF-R55; TNFAR; TNFR1; TNFR55; TNFR60"
                     /coded_by="NM_001065.4:263..1630"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS8542.1"
                     /db_xref="GeneID:7132"
                     /db_xref="HGNC:HGNC:11916"
                     /db_xref="MIM:191190"
ORIGIN      
        1 mglstvpdll lplvllellv giypsgvigl vphlgdrekr dsvcpqgkyi hpqnnsicct
       61 kchkgtylyn dcpgpgqdtd crecesgsft asenhlrhcl scskcrkemg qveissctvd
      121 rdtvcgcrkn qyrhywsenl fqcfncslcl ngtvhlscqe kqntvctcha gfflrenecv
      181 scsnckksle ctklclpqie nvkgtedsgt tvllplviff glcllsllfi glmyryqrwk
      241 sklysivcgk stpekegele gtttkplapn psfsptpgft ptlgfspvps stftssstyt
      301 pgdcpnfaap rrevappyqg adpilatala sdpipnplqk wedsahkpqs ldtddpatly
      361 avvenvpplr wkefvrrlgl sdheidrlel qngrclreaq ysmlatwrrr tprreatlel
      421 lgrvlrdmdl lgcledieea lcgpaalppa psllr
//
LOCUS       NP_001158022             429 aa            linear   PRI 21-NOV-2025
DEFINITION  disrupted in schizophrenia 1 protein isoform m [Homo sapiens].
ACCESSION   NP_001158022
VERSION     NP_001158022.1
DBSOURCE    REFSEQ: accession NM_001164550.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Pils,M., Rutsch,J., Eren,F., Engberg,G., Piehl,F., Cervenka,S.,
            Sellgren,C., Trossbach,S., Willbold,D., Erhardt,S., Bannach,O. and
            Korth,C.
  TITLE     Disrupted-in-schizophrenia 1 protein aggregates in cerebrospinal
            fluid are elevated in patients with first-episode psychosis
  JOURNAL   Psychiatry Clin Neurosci 77 (12), 665-671 (2023)
   PUBMED   37668563
  REMARK    GeneRIF: Disrupted-in-schizophrenia 1 protein aggregates in
            cerebrospinal fluid are elevated in patients with first-episode
            psychosis.
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Habibi,S., Yaghoubzad-Maleki,M., Heshmati,E. and Khalifeh,K.
  TITLE     Effects of representative point mutations on dynamic behavior of
            the DISC1-Ndel1 complex: a molecular dynamics study
  JOURNAL   J Biomol Struct Dyn 41 (22), 13228-13234 (2023)
   PUBMED   36858606
  REMARK    GeneRIF: Effects of representative point mutations on dynamic
            behavior of the DISC1-Ndel1 complex: a molecular dynamics study.
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Li,W., Jiang,H., Chen,X., Yang,K., Deng,X., Tang,Z., Hu,Z.,
            Zhang,X., Lin,S., Zou,Y. and Wu,H.
  TITLE     The variants in PTPRB, TRAF3IP3, and DISC1 genes were associated
            with Graves' disease in the Chinese population
  JOURNAL   Medicine (Baltimore) 101 (45), e31501 (2022)
   PUBMED   36397361
  REMARK    GeneRIF: The variants in PTPRB, TRAF3IP3, and DISC1 genes were
            associated with Graves' disease in the Chinese population.
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Guardiola-Ripoll,M., Sotero-Moreno,A., Almodovar-Paya,C.,
            Hostalet,N., Guerrero-Pedraza,A., Ramiro,N., Ortiz-Gil,J.,
            Arias,B., Madre,M., Soler-Vidal,J., Salvador,R., McKenna,P.J.,
            Pomarol-Clotet,E. and Fatjo-Vilas,M.
  TITLE     Combining fMRI and DISC1 gene haplotypes to understand working
            memory-related brain activity in schizophrenia
  JOURNAL   Sci Rep 12 (1), 7351 (2022)
   PUBMED   35513527
  REMARK    GeneRIF: Combining fMRI and DISC1 gene haplotypes to understand
            working memory-related brain activity in schizophrenia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Ozeki,Y., Tomoda,T., Kleiderlein,J., Kamiya,A., Bord,L., Fujii,K.,
            Okawa,M., Yamada,N., Hatten,M.E., Snyder,S.H., Ross,C.A. and
            Sawa,A.
  TITLE     Disrupted-in-Schizophrenia-1 (DISC-1): mutant truncation prevents
            binding to NudE-like (NUDEL) and inhibits neurite outgrowth
  JOURNAL   Proc Natl Acad Sci U S A 100 (1), 289-294 (2003)
   PUBMED   12506198
  REMARK    GeneRIF: Mutant truncation prevents binding to NudE-like (NUDEL)
            and inhibits neurite outgrowth
            Erratum:[Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13969]
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Blackwood,D.H., Fordyce,A., Walker,M.T., St Clair,D.M.,
            Porteous,D.J. and Muir,W.J.
  TITLE     Schizophrenia and affective disorders--cosegregation with a
            translocation at chromosome 1q42 that directly disrupts
            brain-expressed genes: clinical and P300 findings in a family
  JOURNAL   Am J Hum Genet 69 (2), 428-433 (2001)
   PUBMED   11443544
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Ekelund,J., Hovatta,I., Parker,A., Paunio,T., Varilo,T., Martin,R.,
            Suhonen,J., Ellonen,P., Chan,G., Sinsheimer,J.S., Sobel,E.,
            Juvonen,H., Arajarvi,R., Partonen,T., Suvisaari,J., Lonnqvist,J.,
            Meyer,J. and Peltonen,L.
  TITLE     Chromosome 1 loci in Finnish schizophrenia families
  JOURNAL   Hum Mol Genet 10 (15), 1611-1617 (2001)
   PUBMED   11468279
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Millar,J.K., Christie,S., Semple,C.A. and Porteous,D.J.
  TITLE     Chromosomal location and genomic structure of the human
            translin-associated factor X gene (TRAX; TSNAX) revealed by
            intergenic splicing to DISC1, a gene disrupted by a translocation
            segregating with schizophrenia
  JOURNAL   Genomics 67 (1), 69-77 (2000)
   PUBMED   10945471
REFERENCE   10 (residues 1 to 429)
  AUTHORS   Millar,J.K., Wilson-Annan,J.C., Anderson,S., Christie,S.,
            Taylor,M.S., Semple,C.A., Devon,R.S., St Clair,D.M., Muir,W.J.,
            Blackwood,D.H. and Porteous,D.J.
  TITLE     Disruption of two novel genes by a translocation co-segregating
            with schizophrenia
  JOURNAL   Hum Mol Genet 9 (9), 1415-1423 (2000)
   PUBMED   10814723
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL626763.11 and FJ804215.1.
            
            Summary: This gene encodes a protein with multiple coiled coil
            motifs which is located in the nucleus, cytoplasm and mitochondria.
            The protein is involved in neurite outgrowth and cortical
            development through its interaction with other proteins. This gene
            is disrupted in a t(1;11)(q42.1;q14.3) translocation which
            segregates with schizophrenia and related psychiatric disorders in
            a large Scottish family. Alternate transcriptional splice variants,
            encoding different isoforms, have been characterized. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (m) lacks multiple 3' exons but
            has two alternate 3' exons, as compared to variant L. The resulting
            isoform (m, also known as isoform 45) is much shorter and has a
            distinct C-terminus, as compared to isoform L.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ804215.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.2"
     Protein         1..429
                     /product="disrupted in schizophrenia 1 protein isoform m"
                     /note="disrupted in schizophrenia 1 protein"
                     /calculated_mol_wt=45255
     Region          1..292
                     /region_name="Interaction with MAP1A.
                     /evidence=ECO:0000269|PubMed:12812986"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRI5.3)"
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRI5.3)"
     Region          179..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRI5.3)"
     Region          197..203
                     /region_name="Interaction with FBXW7.
                     /evidence=ECO:0000269|PubMed:28727686"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRI5.3)"
     Region          221..257
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRI5.3)"
     Region          278..323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRI5.3)"
     CDS             1..429
                     /gene="DISC1"
                     /gene_synonym="C1orf136; SCZD9"
                     /coded_by="NM_001164550.2:79..1368"
                     /note="isoform m is encoded by transcript variant m"
                     /db_xref="GeneID:27185"
                     /db_xref="HGNC:HGNC:2888"
                     /db_xref="MIM:605210"
ORIGIN      
        1 mpgggpqgap aaaggggvsh ragsrdclpp aacfrrrrla rrpgymrsst gpgigflspa
       61 vgtlfrfpgg vsgeeshhse srarqcglds rgllvrspvs ksaaaptvts vrgtsahfgi
      121 qlrggtrlpd rlswpcgpgs agwqqefaam dssetldasw eaacsdgarr vraagslpsa
      181 elssnscspg cgpevpptpp gshsaftssf sfirlslgsa gergeaegcp psreaeshcq
      241 spqemgakaa sldgphedpr clsrpfslla trvsadlaqa arnssrperd mhslpdmdpg
      301 ssssldpsla gcggdgssgs gdahswdtll rkwepvlrdc llrnrrqmev islrlklqkl
      361 qedavenddy dkgshwkgyi fiwgeqqlwi rimkidngkw achsgtfpsf fpepagtncf
      421 gstmeasts
//
LOCUS       NP_001358058            1184 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal cell adhesion molecule isoform J precursor [Homo sapiens].
ACCESSION   NP_001358058
VERSION     NP_001358058.1
DBSOURCE    REFSEQ: accession NM_001371129.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1184)
  AUTHORS   Wang,C., Wang,Z., Fu,L., Du,J., Ji,F. and Qiu,X.
  TITLE     CircNRCAM up-regulates NRCAM to promote papillary thyroid carcinoma
            progression
  JOURNAL   J Endocrinol Invest 47 (5), 1215-1226 (2024)
   PUBMED   38485895
  REMARK    GeneRIF: CircNRCAM up-regulates NRCAM to promote papillary thyroid
            carcinoma progression.
REFERENCE   2  (residues 1 to 1184)
  AUTHORS   Zhou,L., He,L., Liu,C.H., Qiu,H., Zheng,L., Sample,K.M., Wu,Q.,
            Li,J., Xie,K., Ampuero,J., Li,Z., Lv,D., Liu,M., Romero-Gomez,M.,
            Hu,Y. and Tang,H.
  TITLE     Liver cancer stem cell dissemination and metastasis: uncovering the
            role of NRCAM in hepatocellular carcinoma
  JOURNAL   J Exp Clin Cancer Res 42 (1), 311 (2023)
   PUBMED   37993901
  REMARK    GeneRIF: Liver cancer stem cell dissemination and metastasis:
            uncovering the role of NRCAM in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1184)
  AUTHORS   Sannes,A.C., Christensen,J.O., Nielsen,M.B. and Gjerstad,J.
  TITLE     Stress-induced headache in the general working population is
            moderated by the NRCAM rs2300043 genotype
  JOURNAL   Scand J Pain 23 (2), 326-332 (2022)
   PUBMED   36181733
  REMARK    GeneRIF: Stress-induced headache in the general working population
            is moderated by the NRCAM rs2300043 genotype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1184)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 1184)
  AUTHORS   Bai,C. and Chen,D.G.
  TITLE     NRCAM acts as a prognostic biomarker and promotes the tumor
            progression in gastric cancer via EMT pathway
  JOURNAL   Tissue Cell 77, 101859 (2022)
   PUBMED   35763884
  REMARK    GeneRIF: NRCAM acts as a prognostic biomarker and promotes the
            tumor progression in gastric cancer via EMT pathway.
REFERENCE   6  (residues 1 to 1184)
  AUTHORS   Wang,B., Williams,H., Du,J.S., Terrett,J. and Kenwrick,S.
  TITLE     Alternative splicing of human NrCAM in neural and nonneural tissues
  JOURNAL   Mol Cell Neurosci 10 (5-6), 287-295 (1998)
   PUBMED   9604207
REFERENCE   7  (residues 1 to 1184)
  AUTHORS   Grumet,M.
  TITLE     Nr-CAM: a cell adhesion molecule with ligand and receptor functions
  JOURNAL   Cell Tissue Res 290 (2), 423-428 (1997)
   PUBMED   9321706
  REMARK    Review article
REFERENCE   8  (residues 1 to 1184)
  AUTHORS   Sakurai,T., Lustig,M., Nativ,M., Hemperly,J.J., Schlessinger,J.,
            Peles,E. and Grumet,M.
  TITLE     Induction of neurite outgrowth through contactin and Nr-CAM by
            extracellular regions of glial receptor tyrosine phosphatase beta
  JOURNAL   J Cell Biol 136 (4), 907-918 (1997)
   PUBMED   9049255
REFERENCE   9  (residues 1 to 1184)
  AUTHORS   Volkmer,H., Leuschner,R., Zacharias,U. and Rathjen,F.G.
  TITLE     Neurofascin induces neurites by heterophilic interactions with
            axonal NrCAM while NrCAM requires F11 on the axonal surface to
            extend neurites
  JOURNAL   J Cell Biol 135 (4), 1059-1069 (1996)
   PUBMED   8922386
REFERENCE   10 (residues 1 to 1184)
  AUTHORS   Lane,R.P., Chen,X.N., Yamakawa,K., Vielmetter,J., Korenberg,J.R.
            and Dreyer,W.J.
  TITLE     Characterization of a highly conserved human homolog to the chicken
            neural cell surface protein Bravo/Nr-CAM that maps to chromosome
            band 7q31
  JOURNAL   Genomics 35 (3), 456-465 (1996)
   PUBMED   8812479
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005058.1, AC007567.2 and
            AC005683.2.
            
            Summary: Cell adhesion molecules (CAMs) are members of the
            immunoglobulin superfamily. This gene encodes a neuronal cell
            adhesion molecule with multiple immunoglobulin-like C2-type domains
            and fibronectin type-III domains. This ankyrin-binding protein is
            involved in neuron-neuron adhesion and promotes directional
            signaling during axonal cone growth. This gene is also expressed in
            non-neural tissues and may play a general role in cell-cell
            communication via signaling from its intracellular domain to the
            actin cytoskeleton during directional cell migration. Allelic
            variants of this gene have been associated with autism and
            addiction vulnerability. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (31), as well as variant 32,
            encodes isoform J.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1184
                     /product="neuronal cell adhesion molecule isoform J
                     precursor"
                     /note="NgCAM-related cell adhesion molecule; neuronal
                     surface protein Bravo"
                     /calculated_mol_wt=127685
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3315
     Region          46..140
                     /region_name="IgI_NrCAM"
                     /note="Immunoglobulin (Ig)-like domain of NrCAM (Ng
                     (neuronglia) CAM-related cell adhesion molecule); member
                     of the I-set of Ig superfamily (IgSF) domains; cd05874"
                     /db_xref="CDD:409458"
     Region          46..50
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409458"
     Region          55..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409458"
     Region          64..71
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409458"
     Region          77..82
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409458"
     Region          85..87
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409458"
     Region          94..97
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409458"
     Region          102..106
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409458"
     Region          119..127
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409458"
     Region          130..140
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409458"
     Region          149..238
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          163..167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          177..181
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          200..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          215..220
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          231..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          258..339
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          269..273
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          282..286
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          304..308
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          318..323
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          331..334
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          343..431
                     /region_name="Ig4_NrCAM"
                     /note="Fourth immunoglobulin (Ig)-like domain of NrCAM
                     (NgCAM-related cell adhesion molecule); cd05868"
                     /db_xref="CDD:409454"
     Region          359..363
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409454"
     Region          372..376
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409454"
     Region          396..400
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409454"
     Region          410..415
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409454"
     Region          423..426
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409454"
     Region          440..523
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          453..457
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          466..470
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          489..493
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          503..508
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          516..519
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          529..614
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          544..548
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          559..563
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          580..>1052
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          594..599
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          607..610
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          628..718
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(628,694,709)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(710..711,713..714)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1071..1160
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     CDS             1..1184
                     /gene="NRCAM"
                     /gene_synonym="NEDNMS"
                     /coded_by="NM_001371129.1:526..4080"
                     /note="isoform J precursor is encoded by transcript
                     variant 31"
                     /db_xref="GeneID:4897"
                     /db_xref="HGNC:HGNC:7994"
                     /db_xref="MIM:601581"
ORIGIN      
        1 mqlkimpkkk rlsagrvpli lflcqmisal evpldpklle dlvqpptitq qspkdyiidp
       61 reniviqcea kgkpppsfsw trngthfdid kdplvtmkpg tgtliinims egkaetyegv
      121 yqctarnerg aavsnnivvr psrsplwtke klepitlqsg qslvlpcrpp iglpppiifw
      181 mdnsfqrlpq servsqglng dlyfsnvlpe dtredyicya rfnhtqtiqq kqpisvkvis
      241 akssrerppt fltpegnasn keelrgnvls leciaeglpt piiywakedg mlpknrtvyk
      301 nfektlqiih vseadsgnyq ciaknalgai hhtisvrvka apywitapqn lvlspgedgt
      361 licrangnpk priswltngv pieiapddps rkidgdtiif snvqerssav yqcnasneyg
      421 yllanafvnv laeppriltp antlyqvian rpalldcaff gsplptiewf kgakgsalhe
      481 diyvlhengt leipvaqkds tgtytcvarn klgmaknevh leikdptwiv kqpeyavvqr
      541 gsmvsfeckv khdhtlsltv lwlkdnrelp sderftvdkd hlvvadvsdd dsgtytcvan
      601 ttldsvsasa vlsvvaptpt papvydvpnp pfdleltdql dksvqlswtp gddnnspitk
      661 fiieyedamh kpglwhhqte vsgtqttaql klspyvnysf rvmavnsigk slpseaseqy
      721 ltkasepdkn ptaveglgse pdnlvitwkp lngfesngpg lqykvswrqk dgddewtsvv
      781 vanvskyivs gtptfvpyli kvqalndmgf apepavvmgh sgedlpmvap gnvrvnvvns
      841 tlaevhwdpv plksirghlq gyriyywktq ssskrnrrhi ekkiltfqgs kthgmlpgle
      901 pfshytlnvr vvngkgegpa spdrvfntpe gvpsapsslk ivnptldslt lewdppshpn
      961 gilteytlky qpinsthelg plvdlkipan ktrwtlknln fstrykfyfy aqtsagsgsq
     1021 iteeavttvd egagkamasr qvdiatqgwf iglmcavall ilillivcfi rrnkggkypv
     1081 kekedahadp eiqpmkeddg tfgeysdaed hkplkkgsrt psdrtvkked sddslvdyge
     1141 gvngqfnedg sfigqysgkk ekepaegnes seapspvnam nsfv
//
LOCUS       NP_115754                647 aa            linear   PRI 21-NOV-2025
DEFINITION  elongation factor 1-delta isoform 1 [Homo sapiens].
ACCESSION   NP_115754
VERSION     NP_115754.4
DBSOURCE    REFSEQ: accession NM_032378.7
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Wang,R., Lv,C., Li,D., Song,Y. and Yan,Z.
  TITLE     EEF1D stabilized by SRSF9 promotes colorectal cancer via enhancing
            the proliferation and metastasis
  JOURNAL   Int J Cancer 155 (8), 1487-1499 (2024)
   PUBMED   38771720
  REMARK    GeneRIF: EEF1D stabilized by SRSF9 promotes colorectal cancer via
            enhancing the proliferation and metastasis.
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Guo,L., Ren,H., Fan,S., Chao,X., Liu,M., Guan,H. and Wang,J.
  TITLE     Autoantibodies against eukaryotic translation elongation factor 1
            delta in two patients with autoimmune cerebellar ataxia
  JOURNAL   Front Immunol 14, 1289175 (2024)
   PUBMED   38332912
  REMARK    GeneRIF: Autoantibodies against eukaryotic translation elongation
            factor 1 delta in two patients with autoimmune cerebellar ataxia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Negrutskii,B.S., Shalak,V.F., Novosylna,O.V., Porubleva,L.V.,
            Lozhko,D.M. and El'skaya,A.V.
  TITLE     The eEF1 family of mammalian translation elongation factors
  JOURNAL   BBA Adv 3, 100067 (2022)
   PUBMED   37082266
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 647)
  AUTHORS   Kaitsuka,T., Tomizawa,K. and Matsushita,M.
  TITLE     Transformation of eEF1Bdelta into heat-shock response transcription
            factor by alternative splicing
  JOURNAL   EMBO Rep 12 (7), 673-681 (2011)
   PUBMED   21597468
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 647)
  AUTHORS   Jung,M., Kondratyev,A.D. and Dritschilo,A.
  TITLE     Elongation factor 1 delta is enhanced following exposure to
            ionizing radiation
  JOURNAL   Cancer Res 54 (10), 2541-2543 (1994)
   PUBMED   8168075
REFERENCE   7  (residues 1 to 647)
  AUTHORS   Bec,G., Kerjan,P. and Waller,J.P.
  TITLE     Reconstitution in vitro of the valyl-tRNA synthetase-elongation
            factor (EF) 1 beta gamma delta complex. Essential roles of the
            NH2-terminal extension of valyl-tRNA synthetase and of the EF-1
            delta subunit in complex formation
  JOURNAL   J Biol Chem 269 (3), 2086-2092 (1994)
   PUBMED   8294461
REFERENCE   8  (residues 1 to 647)
  AUTHORS   Sanders,J., Raggiaschi,R., Morales,J. and Moller,W.
  TITLE     The human leucine zipper-containing guanine-nucleotide exchange
            protein elongation factor-1 delta
  JOURNAL   Biochim Biophys Acta 1174 (1), 87-90 (1993)
   PUBMED   8334168
REFERENCE   9  (residues 1 to 647)
  AUTHORS   Venema,R.C., Peters,H.I. and Traugh,J.A.
  TITLE     Phosphorylation of elongation factor 1 (EF-1) and valyl-tRNA
            synthetase by protein kinase C and stimulation of EF-1 activity
  JOURNAL   J Biol Chem 266 (19), 12574-12580 (1991)
   PUBMED   2061327
REFERENCE   10 (residues 1 to 647)
  AUTHORS   Motorin,Yu.A., Wolfson,A.D., Orlovsky,A.F. and Gladilin,K.L.
  TITLE     Mammalian valyl-tRNA synthetase forms a complex with the first
            elongation factor
  JOURNAL   FEBS Lett 238 (2), 262-264 (1988)
   PUBMED   3169261
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AC067930.7.
            
            On Jun 2, 2019 this sequence version replaced NP_115754.3.
            
            Summary: This gene encodes a subunit of the elongation factor-1
            complex, which is responsible for the enzymatic delivery of
            aminoacyl tRNAs to the ribosome. This subunit, delta, functions as
            guanine nucleotide exchange factor. It is reported that following
            HIV-1 infection, this subunit interacts with HIV-1 Tat. This
            interaction results in repression of translation of host cell
            proteins and enhanced translation of viral proteins. Several
            alternatively spliced transcript variants encoding multiple
            isoforms have been found for this gene. Related pseudogenes have
            been defined on chromosomes 1, 6, 7, 9, 11, 13, 17, 19.[provided by
            RefSeq, Aug 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1). Variants 1 and 3
            both encode the same isoform (1, also known as L).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225040.1, AK024550.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..647
                     /product="elongation factor 1-delta isoform 1"
                     /note="elongation factor 1-delta; antigen NY-CO-4;
                     EF-1-delta; eukaryotic translation elongation factor 1
                     delta (guanine nucleotide exchange protein)"
                     /calculated_mol_wt=71277
     Region          525..552
                     /region_name="EF-1_beta_acid"
                     /note="Eukaryotic elongation factor 1 beta central acidic
                     region; pfam10587"
                     /db_xref="CDD:463158"
     Region          564..647
                     /region_name="EF1_GNE"
                     /note="EF-1 guanine nucleotide exchange domain; pfam00736"
                     /db_xref="CDD:459919"
     CDS             1..647
                     /gene="EEF1D"
                     /gene_synonym="EF-1D; EF1D; FP1047; NEDTCHAL"
                     /coded_by="NM_032378.7:200..2143"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6404.1"
                     /db_xref="GeneID:1936"
                     /db_xref="HGNC:HGNC:3211"
                     /db_xref="MIM:130592"
ORIGIN      
        1 mrsgkasctl etvwedkhky eeaerrfyeh eatqaaasaq qlpaegpamn gpgqddpeda
       61 deaeapdggs rrdprksqds rkplqkkrkr spksglgpad lallglsaer vwldkslfdq
      121 aessyrqkla dvaaqaawpp alapwglcth gnqvachhvt wgiwvnkssf dqaerafvew
      181 sqalllapdg srrqgtpntg qqvavpdlah qpsppvngqp plgslqalvr evwlekpryd
      241 aaergfyeal fdghppgkvr lqeraglaeg arrgrrdrrg rnilgnkrag lrradgeaps
      301 alpycyflqk daeapwlskp aydsaecrhh aaealrvawc leaaslshrp gprsglsvss
      361 lrpnrkmatn flahekiwfd kfkyddaerr fyeqmngpva gasrqengas vilrdiarar
      421 eniqkslags sgpgassgts gdhgelvvri aslevenqsl rgvvqelqqa isklearlnv
      481 leksspghra tapqtqhvsp mrqveppakk patpaedded ddidlfgsdn eeedkeaaql
      541 reerlrqyae kkakkpalva kssilldvkp wddetdmaql eacvrsiqld glvwgasklv
      601 pvgygirklq iqcvveddkv gtdlleeeit kfeehvqsvd iaafnki
//
LOCUS       NP_001372241             792 aa            linear   PRI 21-NOV-2025
DEFINITION  receptor-type tyrosine-protein phosphatase alpha isoform 6
            precursor [Homo sapiens].
ACCESSION   NP_001372241
VERSION     NP_001372241.1
DBSOURCE    REFSEQ: accession NM_001385312.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 792)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 792)
  AUTHORS   Fang,J., Zhang,Y., Huang,C., Lu,R., Yu,J., Chen,R., Wang,Y.,
            Zhao,X., Yu,J. and Huang,J.
  TITLE     Glucose-mediated N-glycosylation of RPTPalpha affects its
            subcellular localization and Src activation
  JOURNAL   Oncogene 42 (14), 1058-1071 (2023)
   PUBMED   36765146
  REMARK    GeneRIF: Glucose-mediated N-glycosylation of RPTPalpha affects its
            subcellular localization and Src activation.
REFERENCE   3  (residues 1 to 792)
  AUTHORS   Hill,M.A., Bentley,S.R., Walker,T.L., Mellick,G.D., Wood,S.A. and
            Sykes,A.M.
  TITLE     Does a rare mutation in PTPRA contribute to the development of
            Parkinson's disease in an Australian multi-incident family?
  JOURNAL   PLoS One 17 (7), e0271499 (2022)
   PUBMED   35900966
  REMARK    GeneRIF: Does a rare mutation in PTPRA contribute to the
            development of Parkinson's disease in an Australian multi-incident
            family?
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 792)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 792)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 792)
  AUTHORS   Zheng,X.M., Wang,Y. and Pallen,C.J.
  TITLE     Cell transformation and activation of pp60c-src by overexpression
            of a protein tyrosine phosphatase
  JOURNAL   Nature 359 (6393), 336-339 (1992)
   PUBMED   1383828
REFERENCE   7  (residues 1 to 792)
  AUTHORS   Rao,V.V., Loffler,C., Sap,J., Schlessinger,J. and Hansmann,I.
  TITLE     The gene for receptor-linked protein-tyrosine-phosphatase (PTPA) is
            assigned to human chromosome 20p12-pter by in situ hybridization
            (ISH and FISH)
  JOURNAL   Genomics 13 (3), 906-907 (1992)
   PUBMED   1639427
REFERENCE   8  (residues 1 to 792)
  AUTHORS   Jirik,F.R., Anderson,L.L. and Duncan,A.M.
  TITLE     The human protein-tyrosine phosphatase PTP alpha/LRP gene (PTPA) is
            assigned to chromosome 20p13
  JOURNAL   Cytogenet Cell Genet 60 (2), 117-118 (1992)
   PUBMED   1611910
REFERENCE   9  (residues 1 to 792)
  AUTHORS   Kaplan,R., Morse,B., Huebner,K., Croce,C., Howk,R., Ravera,M.,
            Ricca,G., Jaye,M. and Schlessinger,J.
  TITLE     Cloning of three human tyrosine phosphatases reveals a multigene
            family of receptor-linked protein-tyrosine-phosphatases expressed
            in brain
  JOURNAL   Proc Natl Acad Sci U S A 87 (18), 7000-7004 (1990)
   PUBMED   2169617
REFERENCE   10 (residues 1 to 792)
  AUTHORS   Sap,J., D'Eustachio,P., Givol,D. and Schlessinger,J.
  TITLE     Cloning and expression of a widely expressed receptor tyrosine
            phosphatase
  JOURNAL   Proc Natl Acad Sci U S A 87 (16), 6112-6116 (1990)
   PUBMED   2166945
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL161656.20 and AL121905.23.
            
            Summary: The protein encoded by this gene is a member of the
            protein tyrosine phosphatase (PTP) family. PTPs are known to be
            signaling molecules that regulate a variety of cellular processes
            including cell growth, differentiation, mitotic cycle, and
            oncogenic transformation. This PTP contains an extracellular
            domain, a single transmembrane segment and two tandem
            intracytoplasmic catalytic domains, and thus represents a
            receptor-type PTP. This PTP has been shown to dephosphorylate and
            activate Src family tyrosine kinases, and is implicated in the
            regulation of integrin signaling, cell adhesion and proliferation.
            Three alternatively spliced variants of this gene, which encode two
            distinct isoforms, have been reported. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3696890.1,
                                           SRR14038196.2541805.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..792
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..792
                     /product="receptor-type tyrosine-protein phosphatase alpha
                     isoform 6 precursor"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase, receptor type, alpha
                     polypeptide; PTPase-alpha; Leukocyte common
                     antigen-related peptide (protein tyrosine phosphate);
                     tyrosine phosphatase alpha; PTPLCA-related phosphatase;
                     receptor-type tyrosine-protein phosphatase alpha;
                     protein-tyrosine phosphatase alpha"
                     /calculated_mol_wt=87568
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2024
     Site            21
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Site            36
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Region          39..59
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18433.3)"
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Site            80
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Site            86
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Site            124
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Site            143..165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18433.3)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P18052; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P18052; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Region          205..500
                     /region_name="R-PTPc-A-1"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase A, repeat 1; cd14621"
                     /db_xref="CDD:350469"
     Region          554..780
                     /region_name="R-PTPc-A-2"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase A, repeat 2; cd14623"
                     /db_xref="CDD:350471"
     Site            788
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:22801373,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P18433.3)"
     CDS             1..792
                     /gene="PTPRA"
                     /gene_synonym="HEPTP; HLPR; HPTPA; HPTPalpha; LRP; PTPA;
                     PTPRL2; R-PTP-alpha; RPTPA"
                     /coded_by="NM_001385312.1:409..2787"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 13"
                     /db_xref="GeneID:5786"
                     /db_xref="HGNC:HGNC:9664"
                     /db_xref="MIM:176884"
ORIGIN      
        1 mdswfilvll gsglicvsan nattvapsvg itrlinssta epvkeeakts nptssltsls
       61 vaptfspnit lgptylttvn ssdsdngttr tastnsigit ispngtwlpd nqftdartep
      121 wegnsstaat tpetfppsde tpiiavmval ssllvivfii ivlymlrfkk ykqagshsns
      181 frlsngrted vepqsvplla rspstnrkyp plpvdkleee inrrmaddnk lfreefnalp
      241 acpiqatcea askeenkekn ryvnilpydh srvhltpveg vpdsdyinas fingyqeknk
      301 fiaaqgpkee tvndfwrmiw eqntativmv tnlkerkeck caqywpdqgc wtygnirvsv
      361 edvtvlvdyt vrkfciqqvg dmtnrkpqrl itqfhftswp dfgvpftpig mlkflkkvka
      421 cnpqyagaiv vhcsagvgrt gtfvvidaml dmmhterkvd vygfvsrira qrcqmvqtdm
      481 qyvfiyqall ehylygdtel evtslethlq kiynkipgts nngleeefkk ltsikiqndk
      541 mrtgnlpanm kknrvlqiip yefnrviipv krgeentdyv nasfidgyrq kdsyiasqgp
      601 llhtiedfwr miwewkscsi vmlteleerg qekcaqywps dglvsygdit velkkeeece
      661 sytvrdllvt ntrnksrqir qfhfhgwpev gipsdgkgmi siiaavqkqq qqsgnhpitv
      721 hcsagagrtg tfcalstvle rvkaegildv fqtvkslrlq rphmvqtleq yefcykvvqe
      781 yidafsdyan fk
//
LOCUS       NP_001369465             693 aa            linear   PRI 21-NOV-2025
DEFINITION  amyloid beta precursor like protein 2 isoform 20 [Homo sapiens].
ACCESSION   NP_001369465
VERSION     NP_001369465.1
DBSOURCE    REFSEQ: accession NM_001382536.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 693)
  AUTHORS   Tao,Z., Huang,J. and Li,J.
  TITLE     Comprehensive intratumoral heterogeneity landscaping of liver
            hepatocellular carcinoma and discerning of APLP2 in cancer
            progression
  JOURNAL   Environ Toxicol 39 (2), 612-625 (2024)
   PUBMED   37515494
  REMARK    GeneRIF: Comprehensive intratumoral heterogeneity landscaping of
            liver hepatocellular carcinoma and discerning of APLP2 in cancer
            progression.
REFERENCE   3  (residues 1 to 693)
  AUTHORS   Huang,X., Yang,J., Xi,H., Zhang,M., Oh,Y., Jin,Z. and Zheng,Z.
  TITLE     Implication of Amyloid Precursor-like Protein 2 Expression in
            Cutaneous Squamous Cell Carcinoma Pathogenesis
  JOURNAL   In Vivo 38 (1), 399-408 (2024)
   PUBMED   38148084
  REMARK    GeneRIF: Implication of Amyloid Precursor-like Protein 2 Expression
            in Cutaneous Squamous Cell Carcinoma Pathogenesis.
REFERENCE   4  (residues 1 to 693)
  AUTHORS   Chen,J., Tang,F., Li,H., Wu,X., Yang,Y., Liu,Z., Huang,X., Wang,J.,
            Zheng,R., Wang,L., Liu,H., Xu,J., Wang,P. and Liu,F.
  TITLE     Mycobacterium tuberculosis suppresses APLP2 expression to enhance
            its survival in macrophage
  JOURNAL   Int Immunopharmacol 124 (Pt B), 111058 (2023)
   PUBMED   37844466
  REMARK    GeneRIF: Mycobacterium tuberculosis suppresses APLP2 expression to
            enhance its survival in macrophage.
REFERENCE   5  (residues 1 to 693)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 693)
  AUTHORS   Blangy,A., Vidal,F., Cuzin,F., Yang,Y.H., Boulukos,K. and
            Rassoulzadegan,M.
  TITLE     CDEBP, a site-specific DNA-binding protein of the 'APP-like'
            family, is required during the early development of the mouse
  JOURNAL   J Cell Sci 108 (Pt 2), 675-683 (1995)
   PUBMED   7539437
REFERENCE   7  (residues 1 to 693)
  AUTHORS   von der Kammer,H., Hanes,J., Klaudiny,J. and Scheit,K.H.
  TITLE     A human amyloid precursor-like protein is highly homologous to a
            mouse sequence-specific DNA-binding protein
  JOURNAL   DNA Cell Biol 13 (11), 1137-1143 (1994)
   PUBMED   7702756
REFERENCE   8  (residues 1 to 693)
  AUTHORS   Bush,A.I., Pettingell,W.H. Jr., de Paradis,M., Tanzi,R.E. and
            Wasco,W.
  TITLE     The amyloid beta-protein precursor and its mammalian homologues.
            Evidence for a zinc-modulated heparin-binding superfamily
  JOURNAL   J Biol Chem 269 (43), 26618-26621 (1994)
   PUBMED   7929392
REFERENCE   9  (residues 1 to 693)
  AUTHORS   von der Kammer,H., Loffler,C., Hanes,J., Klaudiny,J., Scheit,K.H.
            and Hansmann,I.
  TITLE     The gene for the amyloid precursor-like protein APLP2 is assigned
            to human chromosome 11q23-q25
  JOURNAL   Genomics 20 (2), 308-311 (1994)
   PUBMED   8020984
REFERENCE   10 (residues 1 to 693)
  AUTHORS   Wasco,W., Gurubhagavatula,S., Paradis,M.D., Romano,D.M.,
            Sisodia,S.S., Hyman,B.T., Neve,R.L. and Tanzi,R.E.
  TITLE     Isolation and characterization of APLP2 encoding a homologue of the
            Alzheimer's associated amyloid beta protein precursor
  JOURNAL   Nat Genet 5 (1), 95-100 (1993)
   PUBMED   8220435
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003041.3 and AP001183.6.
            
            Summary: This gene encodes amyloid precursor- like protein 2
            (APLP2), which is a member of the APP (amyloid precursor protein)
            family including APP, APLP1 and APLP2. This protein is ubiquitously
            expressed. It contains heparin-, copper- and zinc- binding domains
            at the N-terminus, BPTI/Kunitz inhibitor and E2 domains in the
            middle region, and transmembrane and intracellular domains at the
            C-terminus. This protein interacts with major histocompatibility
            complex (MHC) class I molecules. The synergy of this protein and
            the APP is required to mediate neuromuscular transmission, spatial
            learning and synaptic plasticity. This protein has been implicated
            in the pathogenesis of Alzheimer's disease. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            identified. [provided by RefSeq, Aug 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2418212.1,
                                           SRR14038194.3288645.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.3"
     Protein         1..693
                     /product="amyloid beta precursor like protein 2 isoform
                     20"
                     /note="amyloid precursor protein homolog HSD-2; CDEI
                     box-binding protein; amyloid beta (A4) precursor-like
                     protein 2; testicular tissue protein Li 23; sperm membrane
                     protein YWK-II"
                     /calculated_mol_wt=79069
     Region          <35..146
                     /region_name="A4_EXTRA"
                     /note="amyloid A4; smart00006"
                     /db_xref="CDD:128326"
     Region          251..302
                     /region_name="Kunitz_ABPP-like"
                     /note="Kunitz domain found in the amyloid-beta precursor
                     protein (ABPP) subfamily; cd22607"
                     /db_xref="CDD:438650"
     Site            order(258..266,281,283,285)
                     /site_type="other"
                     /note="serine protease binding site [polypeptide binding]"
                     /db_xref="CDD:438650"
     Region          307..489
                     /region_name="APP_E2"
                     /note="E2 domain of amyloid precursor protein; pfam12925"
                     /db_xref="CDD:463752"
     Region          610..690
                     /region_name="JMTM_APLP2"
                     /note="juxtamembrane and transmembrane (JMTM) domain found
                     in amyloid-like protein 2 (APLP-2) and similar proteins;
                     cd21709"
                     /db_xref="CDD:411992"
     Site            order(610..611,625,628..629,632..633,635..636,639..640,
                     643,646)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:411992"
     Site            order(611..613,629..630,632..633,635..640,643..648)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:411992"
     CDS             1..693
                     /gene="APLP2"
                     /gene_synonym="APLP-2; APPH; APPL2; CDEBP"
                     /coded_by="NM_001382536.1:85..2166"
                     /note="isoform 20 is encoded by transcript variant 22"
                     /db_xref="GeneID:334"
                     /db_xref="HGNC:HGNC:598"
                     /db_xref="MIM:104776"
ORIGIN      
        1 maatgtaaaa atgrllllll vgltapalal agyiemypel qitnvmeanq rvsidnwcrr
       61 dkkqcksrfv tpfkclvgef vsdvllvpek cqffhkerme vcenhqhwht vvkeacltqg
      121 mtlysygmll pcgvdqfhgt eyvccpqtki igsvskeeee edeeeeeeed eeedydvyks
      181 efpteadled fteaavdedd edeeegeevv edrdyyydtf kgddyneenp tepgsdgtms
      241 dkeithdvka vcsqeamtgp cravmprwyf dlskgkcvrf iyggcggnrn nfesedycma
      301 vckamipptp lptndvdvyf etsaddneha rfqkakeqle irhrnrmdrv kkeweeaelq
      361 aknlpkaerq tliqhfqamv kalekeaase kqqlvethla rveamlndrr rmalenylaa
      421 lqsdpprphr ilqalrryvr aenkdrlhti rhyqhvlavd pekaaqmksq vmthlhviee
      481 rrnqslslly kvpyvaqeiq eeidellqeq radmdqftas isetpvdvrv sseeseeipp
      541 fhpfhpfpal penegsgvge qdggligaee kvinsknkvd enmvidetld vkemifnaer
      601 vggleeeres vgplredfsl sssaligllv iavaiatviv islvmlrkrq ygtishgive
      661 vdpmltpeer hlnkmqnhgy enptykyleq mqi
//
LOCUS       NP_001138995             972 aa            linear   PRI 21-NOV-2025
DEFINITION  ankycorbin isoform c [Homo sapiens].
ACCESSION   NP_001138995
VERSION     NP_001138995.1
DBSOURCE    REFSEQ: accession NM_001145523.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 972)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 972)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 972)
  AUTHORS   Jeong,W., Kwon,H., Park,S.K., Lee,I.S. and Jho,E.H.
  TITLE     Retinoic acid-induced protein 14 links mechanical forces to Hippo
            signaling
  JOURNAL   EMBO Rep 25 (9), 4033-4061 (2024)
   PUBMED   39160347
  REMARK    GeneRIF: Retinoic acid-induced protein 14 links mechanical forces
            to Hippo signaling.
REFERENCE   4  (residues 1 to 972)
  AUTHORS   Zhang,R., Hu,M., Chen,H.N., Wang,X., Xia,Z., Liu,Y., Wang,R.,
            Xia,X., Shu,Y., Du,D., Meng,W., Qi,S., Li,Y., Xu,H., Zhou,Z.G. and
            Dai,L.
  TITLE     Phenotypic Heterogeneity Analysis of APC-Mutant Colon Cancer by
            Proteomics and Phosphoproteomics Identifies RAI14 as a Key
            Prognostic Determinant in East Asians and Westerners
  JOURNAL   Mol Cell Proteomics 22 (5), 100532 (2023)
   PUBMED   36934880
  REMARK    GeneRIF: Phenotypic Heterogeneity Analysis of APC-Mutant Colon
            Cancer by Proteomics and Phosphoproteomics Identifies RAI14 as a
            Key Prognostic Determinant in East Asians and Westerners.
REFERENCE   5  (residues 1 to 972)
  AUTHORS   Arnett,D.K., Li,N., Tang,W., Rao,D.C., Devereux,R.B., Claas,S.A.,
            Kraemer,R. and Broeckel,U.
  TITLE     Genome-wide association study identifies single-nucleotide
            polymorphism in KCNB1 associated with left ventricular mass in
            humans: the HyperGEN Study
  JOURNAL   BMC Med Genet 10, 43 (2009)
   PUBMED   19454037
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 972)
  AUTHORS   Kutty,R.K., Chen,S., Samuel,W., Vijayasarathy,C., Duncan,T.,
            Tsai,J.Y., Fariss,R.N., Carper,D., Jaworski,C. and Wiggert,B.
  TITLE     Cell density-dependent nuclear/cytoplasmic localization of NORPEG
            (RAI14) protein
  JOURNAL   Biochem Biophys Res Commun 345 (4), 1333-1341 (2006)
   PUBMED   16729964
  REMARK    GeneRIF: Subcellular localization of NORPEG in retinal pigment
            epithelial (ARPE-19) cells varies with cell density, with
            predominantly nuclear localization in nonconfluent cells, but a
            cytoplasmic localization in confluent cultures.
REFERENCE   7  (residues 1 to 972)
  AUTHORS   Yuan,W., Zheng,Y., Huo,R., Lu,L., Huang,X.Y., Yin,L.L., Li,J.M.,
            Zhou,Z.M. and Sha,J.H.
  TITLE     Expression of a novel alternative transcript of the novel retinal
            pigment epithelial cell gene NORPEG in human testes
  JOURNAL   Asian J Androl 7 (3), 277-288 (2005)
   PUBMED   16110356
REFERENCE   8  (residues 1 to 972)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   9  (residues 1 to 972)
  AUTHORS   Kutty,R.K., Kutty,G., Samuel,W., Duncan,T., Bridges,C.C.,
            El-Sherbeeny,A., Nagineni,C.N., Smith,S.B. and Wiggert,B.
  TITLE     Molecular characterization and developmental expression of NORPEG,
            a novel gene induced by retinoic acid
  JOURNAL   J Biol Chem 276 (4), 2831-2840 (2001)
   PUBMED   11042181
REFERENCE   10 (residues 1 to 972)
  AUTHORS   Peng,Y.F., Mandai,K., Sakisaka,T., Okabe,N., Yamamoto,Y.,
            Yokoyama,S., Mizoguchi,A., Shiozaki,H., Monden,M. and Takai,Y.
  TITLE     Ankycorbin: a novel actin cytoskeleton-associated protein
  JOURNAL   Genes Cells 5 (12), 1001-1008 (2000)
   PUBMED   11168586
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY354204.2, AY317139.1 and AF155135.1.
            
            Transcript Variant: This variant (5) differs in the 5' UTR, uses an
            alternate 5' coding exon, and initiates translation at an alternate
            start codon, compared to variant 1. The encoded isoform (c) has a
            distinct N-terminus and is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY354204.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..972
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..972
                     /product="ankycorbin isoform c"
                     /note="novel retinal pigment epithelial cell protein;
                     ankycorbin; ankyrin repeat and coiled-coil
                     structure-containing protein; retinoic acid-induced
                     protein 14"
                     /calculated_mol_wt=108949
     Region          1..240
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          15..42
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          44..75
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          78..108
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(110,112,116..117,120..122,124..125,129,132,141,143,
                     145,149..150,153..155,157..158,162,165,174,176,178,
                     182..183,186..188,190..191,195,198,207)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          110..141
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          143..174
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          176..207
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <422..>938
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
     CDS             1..972
                     /gene="RAI14"
                     /gene_synonym="NORPEG; RAI13"
                     /coded_by="NM_001145523.2:153..3071"
                     /note="isoform c is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS54838.1"
                     /db_xref="GeneID:26064"
                     /db_xref="HGNC:HGNC:14873"
                     /db_xref="MIM:606586"
ORIGIN      
        1 meaktnewnk nddrllqave ngdaekvasl lgkkgasatk hdsegktafh laaakghvec
       61 lrvmithgvd vtaqdttghs alhlaaknsh hecirkllqs kcpaesvdss gktalhyaaa
      121 qgclqavqil cehkspinlk dldgniplll avqnghseic hflldhgadv nsrnksgrta
      181 lmlaceigss navealikkg adlnlvdslg ynalhyskls enagiqslll skisqdadlk
      241 tptkpkqhdq vskissersg tpkkrkappp pisptqlsdv ssprsitstp lsgkesvffa
      301 eppfkaeiss irenkdrlsd sttgadslld isseadqqdl lsllqakvas ltlhnkelqd
      361 klqakspkea eadlsfdsyh stqtdlgpsl gkpgetsppd sksspsvlih slgksttdnd
      421 vriqqlqeil qdlqkrless eaerkqlqve lqsrraelvc lnnteisens sdlsqklket
      481 qskyeeamke vlsvqkqmkl glvspesmdn yshfhelrvt eeeinvlkqd lqnaleeser
      541 nkekvrelee klverekgtv ikppveeyee mkssycsvie nmnkekaflf ekyqeaqeei
      601 mklkdtlksq mtqeasdeae dmkeamnrmi delnkqvsel sqlykeaqae ledyrkrksl
      661 edvtaeyihk aeheklmqlt nvsrakaeda lsemksqysk vlneltqlkq lvdaqkensv
      721 sitehlqvit tlrtaakeme ekisnlkehl askevevakl ekqlleekaa mtdamvprss
      781 yeklqssles evsvlasklk esvkekekvh sevvqirsev sqvkrekeni qtllkskeqe
      841 vnellqkfqq aqeelaemkr yaesssklee dkdkkinems kevtklkeal nslsqlsyst
      901 ssskrqsqql ealqqqvkql qnqlaeckkq hqevisvyrm hllyavqgqm dedvqkvlkq
      961 iltmcknqsq kk
//
LOCUS       NP_001332923             617 aa            linear   PRI 21-NOV-2025
DEFINITION  GPI ethanolamine phosphate transferase 2, catalytic subunit isoform
            12 [Homo sapiens].
ACCESSION   NP_001332923 XP_016863812
VERSION     NP_001332923.1
DBSOURCE    REFSEQ: accession NM_001345994.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Tremblay-Laganiere,C., Maroofian,R., Nguyen,T.T.M., Karimiani,E.G.,
            Kirmani,S., Akbar,F., Ibrahim,S., Afroze,B., Doosti,M.,
            Ashrafzadeh,F., Babaei,M., Efthymiou,S., Christoforou,M.,
            Sultan,T., Ladda,R.L., McLaughlin,H.M., Truty,R., Mahida,S.,
            Cohen,J.S., Baranano,K., Ismail,F.Y., Patel,M.S., Lehman,A.,
            Edmondson,A.C., Nagy,A., Walker,M.A., Mercimek-Andrews,S., Maki,Y.,
            Sachdev,R., Macintosh,R., Palmer,E.E., Mancini,G.M.S.,
            Barakat,T.S., Steinfeld,R., Rusch,C.T., Stettner,G.M., Wagner,M.,
            Wortmann,S.B., Kini,U., Brady,A.F., Stals,K.L., Ismayilova,N.,
            Ellard,S., Bernardo,D., Nugent,K., McLean,S.D., Antonarakis,S.E.,
            Houlden,H., Kinoshita,T., Campeau,P.M. and Murakami,Y.
  TITLE     PIGG variant pathogenicity assessment reveals characteristic
            features within 19 families
  JOURNAL   Genet Med 23 (10), 1873-1881 (2021)
   PUBMED   34113002
  REMARK    GeneRIF: PIGG variant pathogenicity assessment reveals
            characteristic features within 19 families.
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Kinoshita,T.
  TITLE     Biosynthesis and biology of mammalian GPI-anchored proteins
  JOURNAL   Open Biol 10 (3), 190290 (2020)
   PUBMED   32156170
  REMARK    Review article
REFERENCE   3  (residues 1 to 617)
  AUTHORS   Parsamanesh,N., Safarpour,H., Etesam,S., Shadmehri,A.A. and
            Miri-Moghaddam,E.
  TITLE     Identification and In Silico Characterization of a Novel Point
            Mutation within the Phosphatidylinositol Glycan Anchor Biosynthesis
            Class G Gene in an Iranian Family with Intellectual Disability
  JOURNAL   J Mol Neurosci 69 (4), 538-545 (2019)
   PUBMED   31414351
  REMARK    GeneRIF: Arg658Gln mutation segregates with nonsyndromic
            intellectual disability in Iranian family.
REFERENCE   4  (residues 1 to 617)
  AUTHORS   Zhao,J.J., Halvardson,J., Knaus,A., Georgii-Hemming,P., Baeck,P.,
            Krawitz,P.M., Thuresson,A.C. and Feuk,L.
  TITLE     Reduced cell surface levels of GPI-linked markers in a new case
            with PIGG loss of function
  JOURNAL   Hum Mutat 38 (10), 1394-1401 (2017)
   PUBMED   28581210
  REMARK    GeneRIF: Based on genetic and functional evidence, we confirm that
            pathogenic variants in PIGG cause an intellectual disability
            syndrome, and we find that loss of function of PIGG is associated
            with Glycosylphosphatidylinositol deficiency
REFERENCE   5  (residues 1 to 617)
  AUTHORS   Huang,X., Dai,F.F., Gaisano,G., Giglou,K., Han,J., Zhang,M.,
            Kittanakom,S., Wong,V., Wei,L., Showalter,A.D., Sloop,K.W.,
            Stagljar,I. and Wheeler,M.B.
  TITLE     The identification of novel proteins that interact with the GLP-1
            receptor and restrain its activity
  JOURNAL   Mol Endocrinol 27 (9), 1550-1563 (2013)
   PUBMED   23864651
REFERENCE   6  (residues 1 to 617)
  AUTHORS   Yoshida,T., Kato,K., Yokoi,K., Oguri,M., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Association of genetic variants with hemorrhagic stroke in Japanese
            individuals
  JOURNAL   Int J Mol Med 25 (4), 649-656 (2010)
   PUBMED   20198315
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 617)
  AUTHORS   Oguri,M., Kato,K., Yokoi,K., Yoshida,T., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Assessment of a polymorphism of SDK1 with hypertension in Japanese
            Individuals
  JOURNAL   Am J Hypertens 23 (1), 70-77 (2010)
   PUBMED   19851296
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 617)
  AUTHORS   Shishioh,N., Hong,Y., Ohishi,K., Ashida,H., Maeda,Y. and
            Kinoshita,T.
  TITLE     GPI7 is the second partner of PIG-F and involved in modification of
            glycosylphosphatidylinositol
  JOURNAL   J Biol Chem 280 (10), 9728-9734 (2005)
   PUBMED   15632136
REFERENCE   9  (residues 1 to 617)
  AUTHORS   Kinoshita,T. and Inoue,N.
  TITLE     Dissecting and manipulating the pathway for
            glycosylphos-phatidylinositol-anchor biosynthesis
  JOURNAL   Curr Opin Chem Biol 4 (6), 632-638 (2000)
   PUBMED   11102867
  REMARK    Review article
REFERENCE   10 (residues 1 to 617)
  AUTHORS   Battaglia,A., Carey,J.C. and South,S.T.
  TITLE     Wolf-Hirschhorn Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301362
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092574.2 and AC116565.4.
            
            On Sep 17, 2016 this sequence version replaced XP_016863812.1.
            
            Summary: This gene encodes an enzyme involved in
            glycosylphosphatidylinositol-anchor biosynthesis. The encoded
            protein, which is localized to the endoplasmic reticulum, is
            involved in transferring ethanoloamine phosphate to mannose 2 of
            glycosylphosphatidylinositol species H7 to form species H8. Allelic
            variants of this gene have been associated with intellectual
            disability, hypotonia, and early-onset seizures. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Sep 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.144602.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..617
                     /product="GPI ethanolamine phosphate transferase 2,
                     catalytic subunit isoform 12"
                     /note="GPI ethanolamine phosphate transferase 2;
                     phosphatidylinositol-glycan biosynthesis class G protein;
                     EMM blood group antigen; LAS21 (GPI7) homolog; GPI
                     ethanolamine phosphate transferase 2, catalytic subunit"
                     /calculated_mol_wt=68079
     Region          <437..599
                     /region_name="PIGO_PIGG"
                     /note="GPI ethanolamine phosphate transferase membrane
                     region; pfam19316"
                     /db_xref="CDD:437148"
     CDS             1..617
                     /gene="PIGG"
                     /gene_synonym="EMM; GPI7; LAS21; MRT53; NEDHSCA; PRO4405;
                     RLGS1930"
                     /coded_by="NM_001345994.2:1575..3428"
                     /note="isoform 12 is encoded by transcript variant 24"
                     /db_xref="GeneID:54872"
                     /db_xref="HGNC:HGNC:25985"
                     /db_xref="MIM:616918"
ORIGIN      
        1 mnerlltgtg dradpgfeqf kmserlhgnw irlyleekhs evlfnlgskv lrqyldalkt
       61 lslslsaqva qydiysmmvl tllllsvpqa lrrkaelevp lsspgfsllf ylvilvlsav
      121 hvivctsaes scyfcglswl aaggvmvlas allcvivsvl tnvlvggntp rknpmhpssr
      181 wseldllill gtaghvlslg assfveeehq twyflvntlc lalsqetyrn yflgddgepp
      241 cglcveqghd gataawqdgp gcdvlerdkg hgspstsevl rgrekwmvla spwlilaccr
      301 llrslnqtgv qwahrpdlgh wltssdhkae lsvlaalsll vvfvlvqrgc spvskaalal
      361 gllgvycyra aigsvrfpwr pdskdiskgi iearfvyvfv lgilftgtkd llksqviaad
      421 fklktvglwe iysglvllaa llfrphnlpv lafslliqtl mtkfiwkplr hdaaeitvmh
      481 ywfgqaffyf qgnsnniatv disagfvgld tyveipavll tafgtyagpv lwashlvhfl
      541 ssetrsgsal shacfcyali csipvftyiv lvtslryhlf iwsvfspkll yegmhllita
      601 avcvfftamd qtrltqs
//
LOCUS       NP_005713                394 aa            linear   PRI 21-NOV-2025
DEFINITION  actin-related protein 2 isoform b [Homo sapiens].
ACCESSION   NP_005713
VERSION     NP_005713.1
DBSOURCE    REFSEQ: accession NM_005722.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Hao,P., Qu,Q., Pang,Z., Li,L., Du,S., Shang,L., Jin,C., Xu,W.,
            Ha,Z., Jiang,Y., Chen,J., Gao,Z., Jin,N., Wang,J. and Li,C.
  TITLE     Interaction of species A rotavirus VP4 with the cellular proteins
            vimentin and actin related protein 2 discovered by a proximity
            interactome assay
  JOURNAL   J Virol 97 (12), e0137623 (2023)
   PUBMED   37991368
  REMARK    GeneRIF: Interaction of species A rotavirus VP4 with the cellular
            proteins vimentin and actin related protein 2 discovered by a
            proximity interactome assay.
REFERENCE   2  (residues 1 to 394)
  AUTHORS   van Eeuwen,T., Boczkowska,M., Rebowski,G., Carman,P.J.,
            Fregoso,F.E. and Dominguez,R.
  TITLE     Transition State of Arp2/3 Complex Activation by Actin-Bound
            Dimeric Nucleation-Promoting Factor
  JOURNAL   Proc Natl Acad Sci U S A 120 (33), e2306165120 (2023)
   PUBMED   37549294
  REMARK    GeneRIF: Transition State of Arp2/3 Complex Activation by
            Actin-Bound Dimeric Nucleation-Promoting Factor.
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Sadhu,L., Tsopoulidis,N., Hasanuzzaman,M., Laketa,V., Way,M. and
            Fackler,O.T.
  TITLE     ARPC5 isoforms and their regulation by calcium-calmodulin-N-WASP
            drive distinct Arp2/3-dependent actin remodeling events in CD4 T
            cells
  JOURNAL   Elife 12, e82450 (2023)
   PUBMED   37162507
  REMARK    GeneRIF: ARPC5 isoforms and their regulation by
            calcium-calmodulin-N-WASP drive distinct Arp2/3-dependent actin
            remodeling events in CD4 T cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Tabata,K., Ishiyama,A., Nakamura,Y., Sasaki,M., Inoue,K. and
            Goto,Y.I.
  TITLE     A familial 2p14 microdeletion disrupting actin-related protein 2
            and Ras-related protein Rab-1A genes with intellectual disability
            and language impairment
  JOURNAL   Eur J Med Genet 65 (3), 104446 (2022)
   PUBMED   35134569
  REMARK    GeneRIF: A familial 2p14 microdeletion disrupting actin-related
            protein 2 and Ras-related protein Rab-1A genes with intellectual
            disability and language impairment.
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Machesky,L.M. and Insall,R.H.
  TITLE     Scar1 and the related Wiskott-Aldrich syndrome protein, WASP,
            regulate the actin cytoskeleton through the Arp2/3 complex
  JOURNAL   Curr Biol 8 (25), 1347-1356 (1998)
   PUBMED   9889097
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Machesky,L.M., Reeves,E., Wientjes,F., Mattheyse,F.J., Grogan,A.,
            Totty,N.F., Burlingame,A.L., Hsuan,J.J. and Segal,A.W.
  TITLE     Mammalian actin-related protein 2/3 complex localizes to regions of
            lamellipodial protrusion and is composed of evolutionarily
            conserved proteins
  JOURNAL   Biochem J 328 (Pt 1) (Pt 1), 105-112 (1997)
   PUBMED   9359840
REFERENCE   8  (residues 1 to 394)
  AUTHORS   Welch,M.D., DePace,A.H., Verma,S., Iwamatsu,A. and Mitchison,T.J.
  TITLE     The human Arp2/3 complex is composed of evolutionarily conserved
            subunits and is localized to cellular regions of dynamic actin
            filament assembly
  JOURNAL   J Cell Biol 138 (2), 375-384 (1997)
   PUBMED   9230079
REFERENCE   9  (residues 1 to 394)
  AUTHORS   Winter,D., Podtelejnikov,A.V., Mann,M. and Li,R.
  TITLE     The complex containing actin-related proteins Arp2 and Arp3 is
            required for the motility and integrity of yeast actin patches
  JOURNAL   Curr Biol 7 (7), 519-529 (1997)
   PUBMED   9210376
  REMARK    Erratum:[Curr Biol 1997 Sep 1;7(9):R593]
REFERENCE   10 (residues 1 to 394)
  AUTHORS   Welch,M.D., Iwamatsu,A. and Mitchison,T.J.
  TITLE     Actin polymerization is induced by Arp2/3 protein complex at the
            surface of Listeria monocytogenes
  JOURNAL   Nature 385 (6613), 265-269 (1997)
   PUBMED   9000076
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC404298.1, AF006082.1,
            AC007318.4 and W15444.1.
            
            Summary: The specific function of this gene has not yet been
            determined; however, the protein it encodes is known to be a major
            constituent of the ARP2/3 complex. This complex is located at the
            cell surface and is essential to cell shape and motility through
            lamellipodial actin assembly and protrusion. Two transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (b) has the same
            N- and C-termini but is shorter compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4643866.14125.1,
                                           ERR4643844.44661.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260641.10/ ENSP00000260641.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p14"
     Protein         1..394
                     /product="actin-related protein 2 isoform b"
                     /note="actin-like protein 2; ARP2 actin related protein 2
                     homolog"
                     /calculated_mol_wt=44630
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P61160.1)"
     Region          7..388
                     /region_name="ASKHA_NBD_Arp2"
                     /note="nucleotide-binding domain (NBD) of actin-related
                     protein2 (Arp2) and similar proteins; cd10220"
                     /db_xref="CDD:466821"
     Site            299
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P61160.1)"
     Site            322
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P61160.1)"
     CDS             1..394
                     /gene="ACTR2"
                     /gene_synonym="ARP2"
                     /coded_by="NM_005722.4:80..1264"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1881.1"
                     /db_xref="GeneID:10097"
                     /db_xref="HGNC:HGNC:169"
                     /db_xref="MIM:604221"
ORIGIN      
        1 mdsqgrkvvv cdngtgfvkc gyagsnfpeh ifpalvgrpi irsttkvgni eikdlmvgde
       61 aselrsmlev nypmengivr nwddmkhlwd ytfgpeklni dtrnckillt eppmnptknr
      121 ekivevmfet yqfsgvyvai qavltlyaqg lltgvvvdsg dgvthicpvy egfslphltr
      181 rldiagrdit rylikllllr gyafnhsadf etvrmikekl cyvgynieqe qklalettvl
      241 vesytlpdgr iikvggerfe apealfqphl invegvgvae llfntiqaad idtrsefykh
      301 ivlsggstmy pglpsrlere lkqlylervl kgdveklskf kiriedpprr khmvflggav
      361 ladimkdkdn fwmtrqeyqe kgvrvleklg vtvr
//
LOCUS       NP_001387117            1207 aa            linear   PRI 21-NOV-2025
DEFINITION  protein transport protein Sec31A isoform 16 [Homo sapiens].
ACCESSION   NP_001387117
VERSION     NP_001387117.1
DBSOURCE    REFSEQ: accession NM_001400188.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1207)
  AUTHORS   Tobias,E.S., Lucas-Herald,A.K., Sagar,D., Montezano,A.C.,
            Rios,F.J., De Lucca Camargo,L., Hamilton,G., Gazdagh,G.,
            Diver,L.A., Williams,N., Herzyk,P., Touyz,R.M., Greenfield,A.,
            McGowan,R. and Ahmed,S.F.
  TITLE     SEC31A may be associated with pituitary hormone deficiency and
            gonadal dysgenesis
  JOURNAL   Endocrine 84 (2), 345-349 (2024)
   PUBMED   38400880
  REMARK    GeneRIF: SEC31A may be associated with pituitary hormone deficiency
            and gonadal dysgenesis.
REFERENCE   2  (residues 1 to 1207)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1207)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1207)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1207)
  AUTHORS   Jin,L., Pahuja,K.B., Wickliffe,K.E., Gorur,A., Baumgartel,C.,
            Schekman,R. and Rape,M.
  TITLE     Ubiquitin-dependent regulation of COPII coat size and function
  JOURNAL   Nature 482 (7386), 495-500 (2012)
   PUBMED   22358839
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1207)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1207)
  AUTHORS   Kim,J.H., Hong,J.A., Pih,K.T. and Hwang,I.
  TITLE     Identification and isolation of differentially expressed genes in
            osmotically stressed human oral keratinocytes
  JOURNAL   Arch Oral Biol 46 (4), 335-341 (2001)
   PUBMED   11269867
REFERENCE   8  (residues 1 to 1207)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 1207)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   10 (residues 1 to 1207)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021105.13 and AC108469.5.
            
            Summary: The protein encoded by this gene shares similarity with
            the yeast Sec31 protein, and is a component of the outer layer of
            the coat protein complex II (COPII). The encoded protein is
            involved in vesicle budding from the endoplasmic reticulum (ER) and
            contains multiple WD repeats near the N-terminus and a proline-rich
            region in the C-terminal half. It associates with the protein
            encoded by the SEC13 homolog, nuclear pore and COPII coat complex
            component (SEC13), and is required for ER-Golgi transport.
            Monoubiquitylation of this protein by CUL3-KLHL12 was found to
            regulate the size of COPII coats to accommodate unusually shaped
            cargo. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2622702.1,
                                           SRR11853567.22998.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1207
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..1207
                     /product="protein transport protein Sec31A isoform 16"
                     /note="yeast Sec31p homolog; protein transport protein
                     Sec31A; web1-like protein; SEC31 homolog A, COPII coat
                     complex component; SEC31-related protein A; SEC31-like
                     protein 1; SEC31 homolog A, COPII coating complex
                     component"
                     /calculated_mol_wt=131670
     Region          13..332
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(26,40,46..47,52..53,91,95,101..102,117,121,139,144,
                     150..151,164,185,190,196..197,209..210,231,235,244..245,
                     258..259,277,282,288..289,301..302,320,325,331..332)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          70..119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          125..162
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          172..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          263..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          306..331
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <547..>670
                     /region_name="ACE1-Sec16-like"
                     /note="Ancestral coatomer element 1 (ACE1) of COPII coat
                     complex assembly protein Sec16; cl14807"
                     /db_xref="CDD:449359"
     Site            order(548..552,554,556,567,569,570..571,573..574,578,584,
                     592,604,607,632..633)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187750"
     Region          877..>1103
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     CDS             1..1207
                     /gene="SEC31A"
                     /gene_synonym="ABP125; ABP130; HPBKS; HSPC275; HSPC334;
                     NEDSOSB; SEC31L1"
                     /coded_by="NM_001400188.1:71..3694"
                     /note="isoform 16 is encoded by transcript variant 28"
                     /db_xref="GeneID:22872"
                     /db_xref="HGNC:HGNC:17052"
                     /db_xref="MIM:610257"
ORIGIN      
        1 mklkevdrta mqawspaqnh piylatgtsa qqldatfstn asleifeldl sdpsldmksc
       61 atfssshryh kliwgpykmd skgdvsgvli aggengniil ydpskiiagd kevviaqndk
      121 htgpvraldv nifqtnlvas ganeseiyiw dlnnfatpmt pgaktqpped isciawnrqv
      181 qhilasasps gratvwdlrk nepiikvsdh snrmhcsgla whpdvatqmv laseddrlpv
      241 iqmwdlrfas splrvlenha rgilaiawsm adpelllscg kdakilcsnp ntgevlyelp
      301 tntqwcfdiq wcprnpavls aasfdgrisv ysimggstdg lrqkqvdkls ssfgnldpfg
      361 tgqplpplqi pqqtaqhsiv lplkkppkwi rrpvgasfsf ggklvtfenv rmpshqgaeq
      421 qqqqhhvfis qvvtekefls rsdqlqqavq sqgfinycqk kidasqtefe knvwsflkvn
      481 feddsrgkyl ellgyrkedl gkkialalnk vdganvhike ekeeseflps sggtfnisvs
      541 gdidglitqa lltgnfesav dlclhdnrma daiilaiagg qellartqkk yfaksqskit
      601 rlitavvmkn wkeivescdl knwrealaav ltyakpdefs alcdllgtrl enegdsllqt
      661 qaclcyicag nveklvacwt kaqdgshpls lqdliekvvi lrkavqltqa mdtstvgvll
      721 aakmsqyanl laaqgsiaaa laflpdntnq pnimqlrdrl craqgepvag hespkipyek
      781 qqlpkgrpgp vaghhqmprv qtqqyyphge nppppgfimh gnvnpnaagq lptspghmht
      841 qvppypqpqp yqpaqpypfg tggsamyrpq qpvapptsna ypntpyissa ssytgqsqly
      901 aaqhqasspt sspatsfppp pssgasfqhg gpgappsssa yalppgttgt lpaaselpas
      961 qrtenqsiqd qapmlegpqn gwndppalnr vpkkkkmpen fmppvpitsp imnplgdpqs
     1021 qmlqqqpsap vplssqssfp qphlpggqpf hgvqqplgqt gmppsfskpn iegapgapig
     1081 ntfqhvqslp tkkitkkpip dehlilkttf edliqrclss atdpqtkrkl ddaskrlefl
     1141 ydklreqtls ptitsglhni arsietrnys egltmhthiv stsnfsetsa fmpvlkvvlt
     1201 qanklgv
//
LOCUS       NP_000085               2944 aa            linear   PRI 21-NOV-2025
DEFINITION  collagen alpha-1(VII) chain precursor [Homo sapiens].
ACCESSION   NP_000085 XP_011531639
VERSION     NP_000085.1
DBSOURCE    REFSEQ: accession NM_000094.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2944)
  AUTHORS   Pironon,N., Bourrat,E., Prost,C., Chen,M., Woodley,D.T., Titeux,M.
            and Hovnanian,A.
  TITLE     Splice modulation strategy applied to deep intronic variants in
            COL7A1 causing recessive dystrophic epidermolysis bullosa
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2401781121 (2024)
   PUBMED   39159368
  REMARK    GeneRIF: Splice modulation strategy applied to deep intronic
            variants in COL7A1 causing recessive dystrophic epidermolysis
            bullosa.
REFERENCE   2  (residues 1 to 2944)
  AUTHORS   Ali,F.M., Zhou,J., Wang,M., Wang,Q., Sun,L., Mshenga,M.M. and Lu,H.
  TITLE     Epidermolysis Bullosa: Two rare case reports of COL7A1 and EBS-GEN
            SEV KRT14 variants with review of literature
  JOURNAL   BMC Pediatr 24 (1), 242 (2024)
   PUBMED   38580989
  REMARK    GeneRIF: Epidermolysis Bullosa: Two rare case reports of COL7A1 and
            EBS-GEN SEV KRT14 variants with review of literature.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2944)
  AUTHORS   Natale,M.I., Manzur,G.B., Lusso,S.B., Cella,E., Giovo,M.E.,
            Andrada,R., Goitia,J., Fernandez,M.F., Della Giovanna,P.S.,
            Guillamondegui,M.J., Dominguez,M., Gutierrez,O., Izquierdo,A.,
            Hernandez Herrera,H., Velazquez Perdomo,L.G., Mistchenko,A.S. and
            Valinotto,L.E.
  TITLE     Analysis of COL7A1 pathogenic variants in a large cohort of
            dystrophic epidermolysis bullosa patients from Argentina reveals a
            new genotype-phenotype correlation
  JOURNAL   Am J Med Genet A 188 (11), 3153-3161 (2022)
   PUBMED   35979658
  REMARK    GeneRIF: Analysis of COL7A1 pathogenic variants in a large cohort
            of dystrophic epidermolysis bullosa patients from Argentina reveals
            a new genotype-phenotype correlation.
REFERENCE   4  (residues 1 to 2944)
  AUTHORS   Chao,Y.C., Hong,J.B., Liu,C., Lee,M.S. and Lin,R.Y.
  TITLE     COL7A1 G2287R mutation with two clinical phenotypes in the same
            family: Bullous dermolysis of the newborn and dystrophic
            epidermolysis bullosa pruriginosa
  JOURNAL   J Dermatol 49 (9), e313-e314 (2022)
   PUBMED   35560343
  REMARK    GeneRIF: COL7A1 G2287R mutation with two clinical phenotypes in the
            same family: Bullous dermolysis of the newborn and dystrophic
            epidermolysis bullosa pruriginosa.
REFERENCE   5  (residues 1 to 2944)
  AUTHORS   Akasaka,E., Nakano,H. and Sawamura,D.
  TITLE     Two cases of the intermediate phenotype of recessive dystrophic
            epidermolysis bullosa harboring the novel COL7A1 mutation c.3570G>A
  JOURNAL   J Dermatol Sci 106 (3), 193-195 (2022)
   PUBMED   35527172
  REMARK    GeneRIF: Two cases of the intermediate phenotype of recessive
            dystrophic epidermolysis bullosa harboring the novel COL7A1
            mutation c.3570G>A.
            Erratum:[J Dermatol Sci. 2022 Oct;108(1):55. doi:
            10.1016/j.jdermsci.2022.11.002. PMID: 36404218]
REFERENCE   6  (residues 1 to 2944)
  AUTHORS   Lucky,A.W., Pope,E. and Crawford,S.
  TITLE     Dystrophic Epidermolysis Bullosa
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301481
REFERENCE   7  (residues 1 to 2944)
  AUTHORS   Gammon,W.R., Abernethy,M.L., Padilla,K.M., Prisayanh,P.S.,
            Cook,M.E., Wright,J., Briggaman,R.A. and Hunt,S.W. 3rd.
  TITLE     Noncollagenous (NC1) domain of collagen VII resembles multidomain
            adhesion proteins involved in tissue-specific organization of
            extracellular matrix
  JOURNAL   J Invest Dermatol 99 (6), 691-696 (1992)
   PUBMED   1469284
REFERENCE   8  (residues 1 to 2944)
  AUTHORS   Christiano,A.M., Rosenbaum,L.M., Chung-Honet,L.C., Parente,M.G.,
            Woodley,D.T., Pan,T.C., Zhang,R.Z., Chu,M.L., Burgeson,R.E. and
            Uitto,J.
  TITLE     The large non-collagenous domain (NC-1) of type VII collagen is
            amino-terminal and chimeric. Homology to cartilage matrix protein,
            the type III domains of fibronectin and the A domains of von
            Willebrand factor
  JOURNAL   Hum Mol Genet 1 (7), 475-481 (1992)
   PUBMED   1307247
REFERENCE   9  (residues 1 to 2944)
  AUTHORS   Tanaka,T., Takahashi,K., Furukawa,F. and Imamura,S.
  TITLE     Molecular cloning and characterization of type VII collagen cDNA
  JOURNAL   Biochem Biophys Res Commun 183 (3), 958-963 (1992)
   PUBMED   1567409
REFERENCE   10 (residues 1 to 2944)
  AUTHORS   Parente,M.G., Chung,L.C., Ryynanen,J., Woodley,D.T., Wynn,K.C.,
            Bauer,E.A., Mattei,M.G., Chu,M.L. and Uitto,J.
  TITLE     Human type VII collagen: cDNA cloning and chromosomal mapping of
            the gene
  JOURNAL   Proc Natl Acad Sci U S A 88 (16), 6931-6935 (1991)
   PUBMED   1871109
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC121252.4.
            
            On Feb 25, 2020 this sequence version replaced XP_011531639.1.
            
            Summary: This gene encodes the alpha chain of type VII collagen.
            The type VII collagen fibril, composed of three identical alpha
            collagen chains, is restricted to the basement zone beneath
            stratified squamous epithelia. It functions as an anchoring fibril
            between the external epithelia and the underlying stroma. Mutations
            in this gene are associated with all forms of dystrophic
            epidermolysis bullosa. In the absence of mutations, however, an
            acquired form of this disease can result from an autoimmune
            response made to type VII collagen. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853566.19427.1,
                                           SRR18074969.701241.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000681320.1/ ENSP00000506558.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2944
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..2944
                     /product="collagen alpha-1(VII) chain precursor"
                     /note="LC collagen; collagen VII, alpha-1 polypeptide;
                     collagen alpha-1(VII) chain; long-chain collagen;
                     collagen, type VII, alpha 1"
                     /calculated_mol_wt=293610
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1629
     mat_peptide     17..2944
                     /product="collagen alpha-1(VII) chain"
                     /calculated_mol_wt=293610
     Region          17..1253
                     /region_name="Nonhelical region (NC1)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02388.2)"
     Region          37..201
                     /region_name="vWA_collagen_alphaI-XII-like"
                     /note="Collagen: The extracellular matrix represents a
                     complex alloy of variable members of diverse protein
                     families defining structural integrity and various
                     physiological functions. The most abundant family is the
                     collagens with more than 20 different...; cd01482"
                     /db_xref="CDD:238759"
     Site            order(44,46,48,117,149)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238759"
     Site            order(46..48,50,117)
                     /site_type="active"
                     /note="integrin-collagen binding site [active]"
                     /db_xref="CDD:238759"
     Region          233..317
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Region          301..813
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            337
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Region          632..651
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02388.2)"
     Region          777..855
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            786
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Site            order(852..853,855..856)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          867..952
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(867,926,941)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(942..943,944..945)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          955..1044
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(955,1020,1035)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(1036..1037,1039..1040)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1054..1227
                     /region_name="VWA"
                     /note="von Willebrand factor type A domain; pfam00092"
                     /db_xref="CDD:459670"
     Site            1109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Region          1170..1172
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02388.2)"
     Region          1239..1941
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02388.2)"
     Region          1254..2784
                     /region_name="Triple-helical region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02388.2)"
     Region          <1254..1565
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          1254..1477
                     /region_name="Interrupted collagenous region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02388.2)"
     Region          1334..1336
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02388.2)"
     Region          <1447..>1693
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <1637..>1881
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          1963..2782
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02388.2)"
     Region          2008..2010
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02388.2)"
     Region          <2022..>2365
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Site            2036
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2537292; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Site            2039
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2537292; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Site            2084
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2537292; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Site            2087
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2537292; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Site            2090
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2537292; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Site            2167
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8051117; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Site            2176
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8051117; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Site            2185
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8051117; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Site            2188
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8051117; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Region          <2287..>2569
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <2481..>2718
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          2553..2555
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02388.2)"
     Site            2625
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine, alternate.
                     /evidence=ECO:0000269|PubMed:8051117; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Site            2625
                     /site_type="glycosylation"
                     /note="O-linked (Gal...) hydroxylysine, alternate;
                     propagated from UniProtKB/Swiss-Prot (Q02388.2)"
     Site            2631
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine, alternate.
                     /evidence=ECO:0000269|PubMed:8051117; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Site            2631
                     /site_type="glycosylation"
                     /note="O-linked (Gal...) hydroxylysine, alternate;
                     propagated from UniProtKB/Swiss-Prot (Q02388.2)"
     Site            2664
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8051117; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Site            2667
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8051117; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Site            2673
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8051117; propagated from
                     UniProtKB/Swiss-Prot (Q02388.2)"
     Region          2737..2783
                     /region_name="Collagen"
                     /note="Collagen triple helix repeat (20 copies);
                     pfam01391"
                     /db_xref="CDD:460189"
     Region          2785..2944
                     /region_name="Nonhelical region (NC2)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02388.2)"
     Region          2837..2872
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02388.2)"
     Region          2874..2929
                     /region_name="Kunitz_collagen_alpha1_VII"
                     /note="Kunitz-type domain from the alpha1 chain of type
                     VII collagen, and similar proteins; cd22627"
                     /db_xref="CDD:438670"
     Site            2886..2887
                     /site_type="other"
                     /note="Reactive bond. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q02388.2)"
     CDS             1..2944
                     /gene="COL7A1"
                     /gene_synonym="EBD1; EBDCT; EBR1; NDNC8"
                     /coded_by="NM_000094.4:64..8898"
                     /db_xref="CCDS:CCDS2773.1"
                     /db_xref="GeneID:1294"
                     /db_xref="HGNC:HGNC:2214"
                     /db_xref="MIM:120120"
ORIGIN      
        1 mtlrllvaal cagilaeapr vraqhrervt ctrlyaadiv flldgsssig rsnfrevrsf
       61 leglvlpfsg aasaqgvrfa tvqysddprt efgldalgsg gdvirairel sykggntrtg
      121 aailhvadhv flpqlarpgv pkvcilitdg ksqdlvdtaa qrlkgqgvkl favgiknadp
      181 eelkrvasqp tsdffffvnd fsilrtllpl vsrrvcttag gvpvtrppdd stsaprdlvl
      241 sepssqslrv qwtaasgpvt gykvqytplt glgqplpser qevnvpaget svrlrglrpl
      301 teyqvtvial yansigeavs gtarttaleg peltiqntta hsllvawrsv pgatgyrvtw
      361 rvlsggptqq qelgpgqgsv llrdlepgtd yevtvstlfg rsvgpatslm artdasveqt
      421 lrpvilgpts illswnlvpe argyrlewrr etgleppqkv vlpsdvtryq ldglqpgtey
      481 rltlytlleg hevatpatvv ptgpelpvsp vtdlqatelp gqrvrvswsp vpgatqyrii
      541 vrstqgvert lvlpgsqtaf dlddvqagls ytvrvsarvg pregsasvlt vrrepetpla
      601 vpglrvvvsd atrvrvawgp vpgasgfris wstgsgpess qtlppdstat ditglqpgtt
      661 yqvavsvlrg reegpaaviv artdplgpvr tvhvtqasss svtitwtrvp gatgyrvswh
      721 sahgpeksql vsgeatvael dglepdteyt vhvrahvagv dgppasvvvr tapepvgrvs
      781 rlqilnassd vlritwvgvt gatayrlawg rseggpmrhq ilpgntdsae irgleggvsy
      841 svrvtalvgd regtpvsivv ttppeappal gtlhvvqrge hslrlrwepv praqgfllhw
      901 qpeggqeqsr vlgpelssyh ldglepatqy rvrlsvlgpa gegpsaevta rtesprvpsi
      961 elrvvdtsid svtlawtpvs rassyilswr plrgpgqevp gspqtlpgis ssqrvtglep
     1021 gvsyifsltp vldgvrgpea svtqtpvcpr gladvvflph atqdnahrae atrrvlerlv
     1081 lalgplgpqa vqvgllsysh rpsplfplng shdlgiilqr irdmpymdps gnnlgtavvt
     1141 ahrymlapda pgrrqhvpgv mvllvdeplr gdifspirea qasglnvvml gmagadpeql
     1201 rrlapgmdsv qtffavddgp sldqavsgla talcqasftt qprpepcpvy cpkgqkgepg
     1261 emglrgqvgp pgdpglpgrt gapgpqgppg satakgergf pgadgrpgsp gragnpgtpg
     1321 apglkgspgl pgprgdpger gprgpkgepg apgqviggeg pglpgrkgdp gpsgppgprg
     1381 plgdpgprgp pglpgtamkg dkgdrgergp pgpgeggiap gepglpglpg spgpqgpvgp
     1441 pgkkgekgds edgapglpgq pgspgeqgpr gppgaigpkg drgfpgplge agekgergpp
     1501 gpagsrglpg vagrpgakgp egppgptgrq gekgepgrpg dpavvgpava gpkgekgdvg
     1561 pagprgatgv qgergppglv lpgdpgpkgd pgdrgpiglt gragppgdsg ppgekgdpgr
     1621 pgppgpvgpr grdgevgekg degppgdpgl pgkagerglr gapgvrgpvg ekgdqgdpge
     1681 dgrngspgss gpkgdrgepg ppgppgrlvd tgpgarekge pgdrgqegpr gpkgdpglpg
     1741 apgergiegf rgppgpqgdp gvrgpagekg drgppgldgr sgldgkpgaa gpsgpngaag
     1801 kagdpgrdgl pglrgeqglp gpsgppglpg kpgedgkpgl ngkngepgdp gedgrkgekg
     1861 dsgasgregr dgpkgergap gilgpqgppg lpgpvgppgq gfpgvpggtg pkgdrgetgs
     1921 kgeqglpger glrgepgsvp nvdrlletag ikasalreiv etwdessgsf lpvperrrgp
     1981 kgdsgeqgpp gkegpigfpg erglkgdrgd pgpqgppgla lgergppgps glagepgkpg
     2041 ipglpgragg vgeagrpger gergekgerg eqgrdgppgl pgtpgppgpp gpkvsvdepg
     2101 pglsgeqgpp glkgakgepg sngdqgpkgd rgvpgikgdr gepgprgqdg npglpgergm
     2161 agpegkpglq gprgppgpvg ghgdpgppga pglagpagpq gpsglkgepg etgppgrglt
     2221 gptgavglpg ppgpsglvgp qgspglpgqv getgkpgapg rdgasgkdgd rgspgvpgsp
     2281 glpgpvgpkg epgptgapgq avvglpgakg ekgapgglag dlvgepgakg drglpgprge
     2341 kgeagragep gdpgedgqkg apgpkgfkgd pgvgvpgspg ppgppgvkgd lglpglpgap
     2401 gvvgfpgqtg prgemgqpgp sgerglagpp gregipgplg ppgppgsvgp pgasglkgdk
     2461 gdpgvglpgp rgergepgir gedgrpgqeg prgltgppgs rgergekgdv gsaglkgdkg
     2521 dsavilgppg prgakgdmge rgprgldgdk gprgdngdpg dkgskgepgd kgsaglpglr
     2581 gllgpqgqpg aagipgdpgs pgkdgvpgir gekgdvgfmg prglkgergv kgacgldgek
     2641 gdkgeagppg rpglaghkge mgepgvpgqs gapgkeglig pkgdrgfdgq pgpkgdqgek
     2701 gergtpgigg fpgpsgndgs agppgppgsv gprgpeglqg qkgergppge rvvgapgvpg
     2761 apgergeqgr pgpagprgek geaalteddi rgfvrqemsq hcacqgqfia sgsrplpsya
     2821 adtagsqlha vpvlrvshae eeervppedd eyseyseysv eeyqdpeapw dsddpcslpl
     2881 degsctaytl rwyhravtgs teachpfvyg gcggnanrfg treacerrcp prvvqsqgtg
     2941 taqd
//
LOCUS       NP_001332919             472 aa            linear   PRI 21-NOV-2025
DEFINITION  GPI ethanolamine phosphate transferase 2, catalytic subunit isoform
            11 [Homo sapiens].
ACCESSION   NP_001332919 XP_016863814
VERSION     NP_001332919.1
DBSOURCE    REFSEQ: accession NM_001345990.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Tremblay-Laganiere,C., Maroofian,R., Nguyen,T.T.M., Karimiani,E.G.,
            Kirmani,S., Akbar,F., Ibrahim,S., Afroze,B., Doosti,M.,
            Ashrafzadeh,F., Babaei,M., Efthymiou,S., Christoforou,M.,
            Sultan,T., Ladda,R.L., McLaughlin,H.M., Truty,R., Mahida,S.,
            Cohen,J.S., Baranano,K., Ismail,F.Y., Patel,M.S., Lehman,A.,
            Edmondson,A.C., Nagy,A., Walker,M.A., Mercimek-Andrews,S., Maki,Y.,
            Sachdev,R., Macintosh,R., Palmer,E.E., Mancini,G.M.S.,
            Barakat,T.S., Steinfeld,R., Rusch,C.T., Stettner,G.M., Wagner,M.,
            Wortmann,S.B., Kini,U., Brady,A.F., Stals,K.L., Ismayilova,N.,
            Ellard,S., Bernardo,D., Nugent,K., McLean,S.D., Antonarakis,S.E.,
            Houlden,H., Kinoshita,T., Campeau,P.M. and Murakami,Y.
  TITLE     PIGG variant pathogenicity assessment reveals characteristic
            features within 19 families
  JOURNAL   Genet Med 23 (10), 1873-1881 (2021)
   PUBMED   34113002
  REMARK    GeneRIF: PIGG variant pathogenicity assessment reveals
            characteristic features within 19 families.
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Kinoshita,T.
  TITLE     Biosynthesis and biology of mammalian GPI-anchored proteins
  JOURNAL   Open Biol 10 (3), 190290 (2020)
   PUBMED   32156170
  REMARK    Review article
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Parsamanesh,N., Safarpour,H., Etesam,S., Shadmehri,A.A. and
            Miri-Moghaddam,E.
  TITLE     Identification and In Silico Characterization of a Novel Point
            Mutation within the Phosphatidylinositol Glycan Anchor Biosynthesis
            Class G Gene in an Iranian Family with Intellectual Disability
  JOURNAL   J Mol Neurosci 69 (4), 538-545 (2019)
   PUBMED   31414351
  REMARK    GeneRIF: Arg658Gln mutation segregates with nonsyndromic
            intellectual disability in Iranian family.
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Zhao,J.J., Halvardson,J., Knaus,A., Georgii-Hemming,P., Baeck,P.,
            Krawitz,P.M., Thuresson,A.C. and Feuk,L.
  TITLE     Reduced cell surface levels of GPI-linked markers in a new case
            with PIGG loss of function
  JOURNAL   Hum Mutat 38 (10), 1394-1401 (2017)
   PUBMED   28581210
  REMARK    GeneRIF: Based on genetic and functional evidence, we confirm that
            pathogenic variants in PIGG cause an intellectual disability
            syndrome, and we find that loss of function of PIGG is associated
            with Glycosylphosphatidylinositol deficiency
REFERENCE   5  (residues 1 to 472)
  AUTHORS   Huang,X., Dai,F.F., Gaisano,G., Giglou,K., Han,J., Zhang,M.,
            Kittanakom,S., Wong,V., Wei,L., Showalter,A.D., Sloop,K.W.,
            Stagljar,I. and Wheeler,M.B.
  TITLE     The identification of novel proteins that interact with the GLP-1
            receptor and restrain its activity
  JOURNAL   Mol Endocrinol 27 (9), 1550-1563 (2013)
   PUBMED   23864651
REFERENCE   6  (residues 1 to 472)
  AUTHORS   Yoshida,T., Kato,K., Yokoi,K., Oguri,M., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Association of genetic variants with hemorrhagic stroke in Japanese
            individuals
  JOURNAL   Int J Mol Med 25 (4), 649-656 (2010)
   PUBMED   20198315
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 472)
  AUTHORS   Oguri,M., Kato,K., Yokoi,K., Yoshida,T., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Assessment of a polymorphism of SDK1 with hypertension in Japanese
            Individuals
  JOURNAL   Am J Hypertens 23 (1), 70-77 (2010)
   PUBMED   19851296
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 472)
  AUTHORS   Shishioh,N., Hong,Y., Ohishi,K., Ashida,H., Maeda,Y. and
            Kinoshita,T.
  TITLE     GPI7 is the second partner of PIG-F and involved in modification of
            glycosylphosphatidylinositol
  JOURNAL   J Biol Chem 280 (10), 9728-9734 (2005)
   PUBMED   15632136
REFERENCE   9  (residues 1 to 472)
  AUTHORS   Kinoshita,T. and Inoue,N.
  TITLE     Dissecting and manipulating the pathway for
            glycosylphos-phatidylinositol-anchor biosynthesis
  JOURNAL   Curr Opin Chem Biol 4 (6), 632-638 (2000)
   PUBMED   11102867
  REMARK    Review article
REFERENCE   10 (residues 1 to 472)
  AUTHORS   Battaglia,A., Carey,J.C. and South,S.T.
  TITLE     Wolf-Hirschhorn Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301362
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092574.2 and AC116565.4.
            
            On Sep 17, 2016 this sequence version replaced XP_016863814.1.
            
            Summary: This gene encodes an enzyme involved in
            glycosylphosphatidylinositol-anchor biosynthesis. The encoded
            protein, which is localized to the endoplasmic reticulum, is
            involved in transferring ethanoloamine phosphate to mannose 2 of
            glycosylphosphatidylinositol species H7 to form species H8. Allelic
            variants of this gene have been associated with intellectual
            disability, hypotonia, and early-onset seizures. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Sep 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.36118.1,
                                           SRR14038193.3897298.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..472
                     /product="GPI ethanolamine phosphate transferase 2,
                     catalytic subunit isoform 11"
                     /note="GPI ethanolamine phosphate transferase 2;
                     phosphatidylinositol-glycan biosynthesis class G protein;
                     EMM blood group antigen; LAS21 (GPI7) homolog; GPI
                     ethanolamine phosphate transferase 2, catalytic subunit"
                     /calculated_mol_wt=51937
     Region          <292..454
                     /region_name="PIGO_PIGG"
                     /note="GPI ethanolamine phosphate transferase membrane
                     region; pfam19316"
                     /db_xref="CDD:437148"
     CDS             1..472
                     /gene="PIGG"
                     /gene_synonym="EMM; GPI7; LAS21; MRT53; NEDHSCA; PRO4405;
                     RLGS1930"
                     /coded_by="NM_001345990.2:1752..3170"
                     /note="isoform 11 is encoded by transcript variant 13"
                     /db_xref="GeneID:54872"
                     /db_xref="HGNC:HGNC:25985"
                     /db_xref="MIM:616918"
ORIGIN      
        1 mvlasallcv ivsvltnvlv ggntprknpm hpssrwseld llillgtagh vlslgassfv
       61 eeehqtwyfl vntlclalsq etyrnyflgd dgeppcglcv eqghdgataa wqdgpgcdvl
      121 erdkghgsps tsevlrgrek wmvlaspwli laccrllrsl nqtgvqwahr pdlghwltss
      181 dhkaelsvla alsllvvfvl vqrgcspvsk aalalgllgv ycyraaigsv rfpwrpdskd
      241 iskgiiearf vyvfvlgilf tgtkdllksq viaadfklkt vglweiysgl vllaallfrp
      301 hnlpvlafsl liqtlmtkfi wkplrhdaae itvmhywfgq affyfqgnsn niatvdisag
      361 fvgldtyvei pavlltafgt yagpvlwash lvhflssetr sgsalshacf cyalicsipv
      421 ftyivlvtsl ryhlfiwsvf spkllyegmh llitaavcvf ftamdqtrlt qs
//
LOCUS       NP_001317043             302 aa            linear   PRI 21-NOV-2025
DEFINITION  voltage-dependent L-type calcium channel subunit beta-4 isoform g
            [Homo sapiens].
ACCESSION   NP_001317043 XP_016860373
VERSION     NP_001317043.1
DBSOURCE    REFSEQ: accession NM_001330114.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Westhoff,M. and Dixon,R.E.
  TITLE     Mechanisms and Regulation of Cardiac CaV1.2 Trafficking
  JOURNAL   Int J Mol Sci 22 (11), 5927 (2021)
   PUBMED   34072954
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Coste de Bagneaux,P., von Elsner,L., Bierhals,T., Campiglio,M.,
            Johannsen,J., Obermair,G.J., Hempel,M., Flucher,B.E. and Kutsche,K.
  TITLE     A homozygous missense variant in CACNB4 encoding the auxiliary
            calcium channel beta4 subunit causes a severe neurodevelopmental
            disorder and impairs channel and non-channel functions
  JOURNAL   PLoS Genet 16 (3), e1008625 (2020)
   PUBMED   32176688
  REMARK    GeneRIF: The homozygous CACNB4 p.(Leu126Pro) variant underlies the
            severe neurological phenotype in the two siblings.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Vendel,A.C., Terry,M.D., Striegel,A.R., Iverson,N.M.,
            Leuranguer,V., Rithner,C.D., Lyons,B.A., Pickard,G.E., Tobet,S.A.
            and Horne,W.A.
  TITLE     Alternative splicing of the voltage-gated Ca2+ channel beta4
            subunit creates a uniquely folded N-terminal protein binding domain
            with cell-specific expression in the cerebellar cortex
  JOURNAL   J Neurosci 26 (10), 2635-2644 (2006)
   PUBMED   16525042
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Helton,T.D. and Horne,W.A.
  TITLE     Alternative splicing of the beta 4 subunit has alpha1 subunit
            subtype-specific effects on Ca2+ channel gating
  JOURNAL   J Neurosci 22 (5), 1573-1582 (2002)
   PUBMED   11880487
REFERENCE   6  (residues 1 to 302)
  AUTHORS   Escayg,A., Jones,J.M., Kearney,J.A., Hitchcock,P.F. and
            Meisler,M.H.
  TITLE     Calcium channel beta 4 (CACNB4): human ortholog of the mouse
            epilepsy gene lethargic
  JOURNAL   Genomics 50 (1), 14-22 (1998)
   PUBMED   9628818
REFERENCE   7  (residues 1 to 302)
  AUTHORS   Burgess,D.L., Jones,J.M., Meisler,M.H. and Noebels,J.L.
  TITLE     Mutation of the Ca2+ channel beta subunit gene Cchb4 is associated
            with ataxia and seizures in the lethargic (lh) mouse
  JOURNAL   Cell 88 (3), 385-392 (1997)
   PUBMED   9039265
REFERENCE   8  (residues 1 to 302)
  AUTHORS   Diriong,S., Lory,P., Williams,M.E., Ellis,S.B., Harpold,M.M. and
            Taviaux,S.
  TITLE     Chromosomal localization of the human genes for alpha 1A, alpha 1B,
            and alpha 1E voltage-dependent Ca2+ channel subunits
  JOURNAL   Genomics 30 (3), 605-609 (1995)
   PUBMED   8825650
REFERENCE   9  (residues 1 to 302)
  AUTHORS   Spacey,S.
  TITLE     Episodic Ataxia Type 2 - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301674
REFERENCE   10 (residues 1 to 302)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068547.7 and AC097448.2.
            
            On Aug 17, 2016 this sequence version replaced XP_016860373.1.
            
            Summary: This gene encodes a member of the beta subunit family of
            voltage-dependent calcium channel complex proteins. Calcium
            channels mediate the influx of calcium ions into the cell upon
            membrane polarization and consist of a complex of alpha-1,
            alpha-2/delta, beta, and gamma subunits in a 1:1:1:1 ratio. Various
            versions of each of these subunits exist, either expressed from
            similar genes or the result of alternative splicing. The protein
            encoded by this locus plays an important role in calcium channel
            function by modulating G protein inhibition, increasing peak
            calcium current, controlling the alpha-1 subunit membrane targeting
            and shifting the voltage dependence of activation and inactivation.
            Certain mutations in this gene have been associated with idiopathic
            generalized epilepsy (IGE), juvenile myoclonic epilepsy (JME), and
            episodic ataxia, type 5. [provided by RefSeq, Aug 2016].
            
            Transcript Variant: This variant (7) represents use of an alternate
            promoter compared to variant 2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1730290.1,
                                           SRR18074967.1506006.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q23.3"
     Protein         1..302
                     /product="voltage-dependent L-type calcium channel subunit
                     beta-4 isoform g"
                     /note="dihydropyridine-sensitive L-type, calcium channel
                     beta-4 subunit; voltage-dependent L-type calcium channel
                     subunit beta-4; calcium channel voltage-dependent subunit
                     beta 4"
                     /calculated_mol_wt=34100
     Region          1..180
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..302
                     /gene="CACNB4"
                     /gene_synonym="CAB4; CACNLB4; EA5; EIG9; EJM; EJM4; EJM6"
                     /coded_by="NM_001330114.2:958..1866"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="GeneID:785"
                     /db_xref="HGNC:HGNC:1404"
                     /db_xref="MIM:601949"
ORIGIN      
        1 mrpvvlvgps lkgyevtdmm qkalfdflkh rfdgrisitr vtadislakr svlnnpskra
       61 iiersntrss laevqseier ifelarslql vvldadtinh paqliktsla piivhvkvss
      121 pkvlqrliks rgksqskhln vqlvaadkla qcppemfdvi ldenqledac ehlgeyleay
      181 wrathttsst pmtpllgrnl gstalspypt aisglqsqrm rhsnhstens pierrslmts
      241 denyhnerar ksrnrlssss qhsrdhyplv eedypdsyqd tykphrnrgs pggyshdsrh
      301 rl
//
LOCUS       NP_001362657             419 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform eee [Homo sapiens].
ACCESSION   NP_001362657
VERSION     NP_001362657.1
DBSOURCE    REFSEQ: accession NM_001375728.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 419)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 419)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 419)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.2646099.1,
                                           SRR1803612.91738.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..419
                     /product="abl interactor 2 isoform eee"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=46067
     Region          39..100
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          358..418
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(366,368,371,375,393..394,407,409..410)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..419
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375728.1:122..1381"
                     /note="isoform eee is encoded by transcript variant 62"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqt vdihkekvar reigilttnk
       61 ntsrthkiia panlerpvry irkpidytil ddighgvkvs tqnmkmgglp rttpptqkpp
      121 sppmsgkgtl grhspyrtle pvrppvvpnd yvpsptrnma psqqspvrta svnqrnrtys
      181 ssgssggshp ssrsssrens gsgsvgvpia vptpsppsvf pghpvqfysm nrpasrhtpp
      241 tiggslpyrr ppsitsqtsl qnqmnggpfy sqnpvslapp ppsilqvtpq lplmgfvarv
      301 qenisdtppp pppveepvfd espppppppe dyeeeeaavv eysdpyaeed ppwaprsyle
      361 kvvaiydytk dkedelsfqe gaiiyvikkn ddgwyegvmn gvtglfpgny vesimhyse
//
LOCUS       NP_001362956             524 aa            linear   PRI 21-NOV-2025
DEFINITION  protein 4.1 isoform 20 [Homo sapiens].
ACCESSION   NP_001362956 XP_016856092
VERSION     NP_001362956.1
DBSOURCE    REFSEQ: accession NM_001376027.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Terada,N., Saitoh,Y., Saito,M., Yamada,T., Kamijo,A., Yoshizawa,T.
            and Sakamoto,T.
  TITLE     Recent Progress on Genetically Modified Animal Models for Membrane
            Skeletal Proteins: The 4.1 and MPP Families
  JOURNAL   Genes (Basel) 14 (10), 1942 (2023)
   PUBMED   37895291
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 524)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 524)
  AUTHORS   Dalla Venezia,N., Gilsanz,F., Alloisio,N., Ducluzeau,M.T.,
            Benz,E.J. Jr. and Delaunay,J.
  TITLE     Homozygous 4.1(-) hereditary elliptocytosis associated with a point
            mutation in the downstream initiation codon of protein 4.1 gene
  JOURNAL   J Clin Invest 90 (5), 1713-1717 (1992)
   PUBMED   1430200
REFERENCE   7  (residues 1 to 524)
  AUTHORS   Jons,T. and Drenckhahn,D.
  TITLE     Identification of the binding interface involved in linkage of
            cytoskeletal protein 4.1 to the erythrocyte anion exchanger
  JOURNAL   EMBO J 11 (8), 2863-2867 (1992)
   PUBMED   1639060
REFERENCE   8  (residues 1 to 524)
  AUTHORS   Subrahmanyam,G., Bertics,P.J. and Anderson,R.A.
  TITLE     Phosphorylation of protein 4.1 on tyrosine-418 modulates its
            function in vitro
  JOURNAL   Proc Natl Acad Sci U S A 88 (12), 5222-5226 (1991)
   PUBMED   1647028
REFERENCE   9  (residues 1 to 524)
  AUTHORS   Conboy,J.G., Chan,J.Y., Chasis,J.A., Kan,Y.W. and Mohandas,N.
  TITLE     Tissue- and development-specific alternative RNA splicing regulates
            expression of multiple isoforms of erythroid membrane protein 4.1
  JOURNAL   J Biol Chem 266 (13), 8273-8280 (1991)
   PUBMED   2022644
REFERENCE   10 (residues 1 to 524)
  AUTHORS   Horne,W.C., Prinz,W.C. and Tang,E.K.
  TITLE     Identification of two cAMP-dependent phosphorylation sites on
            erythrocyte protein 4.1
  JOURNAL   Biochim Biophys Acta 1055 (1), 87-92 (1990)
   PUBMED   2171679
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL009181.1, AL138785.8 and
            AL357500.17.
            
            On Nov 7, 2019 this sequence version replaced XP_016856092.1.
            
            Summary: The protein encoded by this gene, together with spectrin
            and actin, constitute the red cell membrane cytoskeletal network.
            This complex plays a critical role in erythrocyte shape and
            deformability. Mutations in this gene are associated with type 1
            elliptocytosis (EL1). Alternatively spliced transcript variants
            encoding different isoforms have been described for this
            gene.[provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.127587.1,
                                           SRR1803614.204421.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2156099, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.3"
     Protein         1..524
                     /product="protein 4.1 isoform 20"
                     /note="protein 4.1; erythrocyte surface protein band 4.1;
                     P4.1; EPB4.1; elliptocytosis 1, RH-linked"
                     /calculated_mol_wt=59266
     Region          2..192
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          187..280
                     /region_name="FERM_C_4_1_family"
                     /note="FERM domain C-lobe of Protein 4.1 family; cd13184"
                     /db_xref="CDD:270005"
     Site            order(196,213,215,221)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270005"
     Site            order(225,230..233,268,272,275..276)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Site            268..279
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Region          290..333
                     /region_name="FA"
                     /note="FERM adjacent (FA); pfam08736"
                     /db_xref="CDD:462582"
     Region          406..452
                     /region_name="SAB"
                     /note="SAB domain; pfam04382"
                     /db_xref="CDD:461285"
     CDS             1..524
                     /gene="EPB41"
                     /gene_synonym="4.1R; EL1; HE"
                     /coded_by="NM_001376027.1:729..2303"
                     /note="isoform 20 is encoded by transcript variant 21"
                     /db_xref="GeneID:2035"
                     /db_xref="HGNC:HGNC:3377"
                     /db_xref="MIM:130500"
ORIGIN      
        1 mhckvslldd tvyecvvekh akgqdllkrv cehlnlleed yfglaiwdna tsktwldsak
       61 eikkqvrgvp wnftfnvkfy ppdpaqlted itryylclql rqdivagrlp csfatlallg
      121 sytiqselgd ydpelhgvdy vsdfklapnq tkeleekvme lhksyrsmtp aqadleflen
      181 akklsmygvd lhkakdlegv diilgvcssg llvykdklri nrfpwpkvlk isykrssffi
      241 kirpgeqeqy estigfklps yraakklwkv cvehhtffrl tstdtipksk flalgskfry
      301 sgrtqaqtrq asalidrpap hfertaskra srsldgaaav dsadrsprpt sapaitqgqv
      361 aeggvldasa kktvvpkaqk etvkaevkke deppeqaepe pteawkdldk sqeeikkhha
      421 siselkknfm esvpeprpse wdkrlsthsp frtlningqi ptgegvkkts vlpserkvgg
      481 pespsyflpd tyhlgvckep vlnfqtdqrr laqlrelrak ffls
//
LOCUS       NP_001300951             124 aa            linear   PRI 21-NOV-2025
DEFINITION  endoribonuclease YbeY isoform 3 [Homo sapiens].
ACCESSION   NP_001300951
VERSION     NP_001300951.1
DBSOURCE    REFSEQ: accession NM_001314022.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 124)
  AUTHORS   D'Souza,A.R., Van Haute,L., Powell,C.A., Mutti,C.D., Palenikova,P.,
            Rebelo-Guiomar,P., Rorbach,J. and Minczuk,M.
  TITLE     YbeY is required for ribosome small subunit assembly and tRNA
            processing in human mitochondria
  JOURNAL   Nucleic Acids Res 49 (10), 5798-5812 (2021)
   PUBMED   34037799
  REMARK    GeneRIF: YbeY is required for ribosome small subunit assembly and
            tRNA processing in human mitochondria.
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Liao,Z., Schelcher,C. and Smirnov,A.
  TITLE     YbeY, eminence grise of ribosome biogenesis
  JOURNAL   Biochem Soc Trans 49 (2), 727-745 (2021)
   PUBMED   33929506
  REMARK    GeneRIF: YbeY, eminence grise of ribosome biogenesis.
            Review article
REFERENCE   6  (residues 1 to 124)
  AUTHORS   Ghosal,A., Kohrer,C., Babu,V.M.P., Yamanaka,K., Davies,B.W.,
            Jacob,A.I., Ferullo,D.J., Gruber,C.C., Vercruysse,M. and
            Walker,G.C.
  TITLE     C21orf57 is a human homologue of bacterial YbeY proteins
  JOURNAL   Biochem Biophys Res Commun 484 (3), 612-617 (2017)
   PUBMED   28153719
  REMARK    GeneRIF: This observation suggests that the function of HuYbeY in
            human cells is likely regulated through specific interactions with
            partner proteins similarly to the way YbeY is regulated in
            bacteria.
REFERENCE   7  (residues 1 to 124)
  AUTHORS   Uhlen,M., Oksvold,P., Algenas,C., Hamsten,C., Fagerberg,L.,
            Klevebring,D., Lundberg,E., Odeberg,J., Ponten,F., Kondo,T. and
            Sivertsson,A.
  TITLE     Antibody-based protein profiling of the human chromosome 21
  JOURNAL   Mol Cell Proteomics 11 (3), M111.013458 (2012)
   PUBMED   22042635
REFERENCE   8  (residues 1 to 124)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 124)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 124)
  AUTHORS   Reymond,A., Friedli,M., Henrichsen,C.N., Chapot,F., Deutsch,S.,
            Ucla,C., Rossier,C., Lyle,R., Guipponi,M. and Antonarakis,S.E.
  TITLE     From PREDs and open reading frames to cDNA isolation: revisiting
            the human chromosome 21 transcription map
  JOURNAL   Genomics 78 (1-2), 46-54 (2001)
   PUBMED   11707072
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC384882.1, AY040874.1 and
            AP000471.2.
            
            Summary: This gene encodes a highly conserved metalloprotein. A
            similar protein in bacteria acts as an endoribonuclease, and is
            thought to function in ribosomal RNA maturation and ribosome
            assembly. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (3) lacks an alternate, in-frame
            exon in the central coding region, compared to variant 1. The
            encoded isoform (3) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY040874.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..124
                     /product="endoribonuclease YbeY isoform 3"
                     /note="putative metalloprotease C21orf57; rRNA maturation
                     factor homolog; putative ribonuclease; endoribonuclease
                     YbeY; ybeY metallopeptidase (putative)"
                     /calculated_mol_wt=14138
     Region          35..106
                     /region_name="PRK13963"
                     /note="rRNA maturation RNase YbeY; cl46897"
                     /db_xref="CDD:481237"
     CDS             1..124
                     /gene="YBEY"
                     /gene_synonym="C21orf57"
                     /coded_by="NM_001314022.2:441..815"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82687.1"
                     /db_xref="GeneID:54059"
                     /db_xref="HGNC:HGNC:1299"
                     /db_xref="MIM:617461"
ORIGIN      
        1 mslvirnlqr vipirraplr skieivrril gvqkfdlgii cvdnkniqhi nriyrdrnvp
       61 tdvlsfpfhe vtathglchl lgfthgteae wqqmfqkeka vldelgrrtg trlqpltrgl
      121 fggs
//
LOCUS       NP_001362688            1076 aa            linear   PRI 21-NOV-2025
DEFINITION  GRB10-interacting GYF protein 1 isoform a [Homo sapiens].
ACCESSION   NP_001362688 XP_024302639
VERSION     NP_001362688.1
DBSOURCE    REFSEQ: accession NM_001375759.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Lee,C.Y., Hubrich,D., Varga,J.K., Schafer,C., Welzel,M.,
            Schumbera,E., Djokic,M., Strom,J.M., Schonfeld,J., Geist,J.L.,
            Polat,F., Gibson,T.J., Keller Valsecchi,C.I., Kumar,M.,
            Schueler-Furman,O. and Luck,K.
  TITLE     Systematic discovery of protein interaction interfaces using
            AlphaFold and experimental validation
  JOURNAL   Mol Syst Biol 20 (2), 75-97 (2024)
   PUBMED   38225382
REFERENCE   4  (residues 1 to 1076)
  AUTHORS   Zhu,L., Yao,Z., Luo,Q., Liu,Y., Zhao,W., Shao,C., Shao,S. and
            Cui,F.
  TITLE     Low Expression of GIGYF1 Inhibits Metastasis, Proliferation, and
            Promotes Apoptosis and Autophagy of Gastric Cancer Cells
  JOURNAL   Int J Med Sci 20 (8), 1038-1045 (2023)
   PUBMED   37484805
  REMARK    GeneRIF: Low Expression of GIGYF1 Inhibits Metastasis,
            Proliferation, and Promotes Apoptosis and Autophagy of Gastric
            Cancer Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1076)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1076)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 1076)
  AUTHORS   Ajiro,M., Nishidate,T., Katagiri,T. and Nakamura,Y.
  TITLE     Critical involvement of RQCD1 in the EGFR-Akt pathway in mammary
            carcinogenesis
  JOURNAL   Int J Oncol 37 (5), 1085-1093 (2010)
   PUBMED   20878056
REFERENCE   8  (residues 1 to 1076)
  AUTHORS   Kofler,M.M. and Freund,C.
  TITLE     The GYF domain
  JOURNAL   FEBS J 273 (2), 245-256 (2006)
   PUBMED   16403013
  REMARK    Review article
REFERENCE   9  (residues 1 to 1076)
  AUTHORS   Giovannone,B., Lee,E., Laviola,L., Giorgino,F., Cleveland,K.A. and
            Smith,R.J.
  TITLE     Two novel proteins that are linked to insulin-like growth factor
            (IGF-I) receptors by the Grb10 adapter and modulate IGF-I signaling
  JOURNAL   J Biol Chem 278 (34), 31564-31573 (2003)
   PUBMED   12771153
REFERENCE   10 (residues 1 to 1076)
  AUTHORS   Wilson,M.D., Riemer,C., Martindale,D.W., Schnupf,P., Boright,A.P.,
            Cheung,T.L., Hardy,D.M., Schwartz,S., Scherer,S.W., Tsui,L.C.,
            Miller,W. and Koop,B.F.
  TITLE     Comparative analysis of the gene-dense ACHE/TFR2 region on human
            chromosome 7q22 with the orthologous region on mouse chromosome 5
  JOURNAL   Nucleic Acids Res 29 (6), 1352-1365 (2001)
   PUBMED   11239002
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009488.5.
            
            On Nov 1, 2019 this sequence version replaced XP_024302639.1.
            
            Summary: This gene encodes a member of the gyf family of adaptor
            proteins. The encoded protein contains a gyf protein interaction
            domain. It binds growth factor receptor bound 10, another adaptor
            protein that binds activated insulin-like growth factor 1 and
            insulin receptors and regulates receptor signaling. [provided by
            RefSeq, Apr 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038196.2243938.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..1076
                     /product="GRB10-interacting GYF protein 1 isoform a"
                     /note="postmeiotic segregation increased 2-like 12; PERQ
                     amino acid-rich with GYF domain-containing protein 1"
                     /calculated_mol_wt=118648
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Region          105..422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75420.2)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MR1; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Region          476..529
                     /region_name="GYF"
                     /note="GYF domain: contains conserved Gly-Tyr-Phe
                     residues; Proline-binding domain in CD2-binding and other
                     proteins. Involved in signaling lymphocyte activity. Also
                     present in other unrelated proteins (mainly unknown)
                     derived from diverse eukaryotic species; cd00072"
                     /db_xref="CDD:238027"
     Site            488..504
                     /site_type="active"
                     /note="proline binding motif [active]"
                     /db_xref="CDD:238027"
     Site            order(498,503..504)
                     /site_type="active"
                     /note="proline interaction residues [active]"
                     /db_xref="CDD:238027"
     Site            538
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Region          621..640
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75420.2)"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     Region          696..724
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75420.2)"
     Region          825..879
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75420.2)"
     Site            862
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75420.2)"
     CDS             1..1076
                     /gene="GIGYF1"
                     /gene_synonym="GYF1; PERQ1"
                     /coded_by="NM_001375759.1:1413..4643"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:64599"
                     /db_xref="HGNC:HGNC:9126"
                     /db_xref="MIM:612064"
ORIGIN      
        1 maaetlnfgp ewlralsggg svaspppspa mpkykladyr ygreemlaly vkenkvpeel
       61 qdkefaavlq deplqplale plteeeqrnf slsvnsvavl rlmgkgagpp lagtsrgrgs
      121 trsrgrgrgd scfyqrsiee gdgafgrspr eiqrsqswdd rgerrfeksa rrdgarcgfe
      181 eggagprkeh arsdsenwrs lreeqeeeee gswrlgagpr rdgdrwrsas pdggprsagw
      241 rehgerrrkf efdlrgdrgg cgeeegrggg gsshlrrcra pegfeedkdg lpewcldded
      301 eemgtfdasg aflplkkgpk epipeeqeld fqgleeeeep segleeegpe aggkeltplp
      361 pqeeksssps plptlgplwg tngdgdetae keppaaeddi rgiqlspgvg ssagppgdle
      421 ddeglkhlqq eaeklvaslq dssleeeqft aamqtqglrh saaatalpls hgaarkwfyk
      481 dpqgeiqgpf ttqemaewfq agyfsmsllv krgcdegfqp lgevikmwgr vpfapgpspp
      541 pllgnmdqer lkkqqelaaa alyqqlqhqq flqlvssrql pqcalrekaa lgdltppppp
      601 ppqqqqqqlt aflqqlqalk pprggdqnll ptmsrslsvp dsgrlwdvht sassqsggea
      661 slwdipinss tqgpileqlq lqhkfqerre velrakreee erkrreekrr qqqqeeqkrr
      721 qeeeelfrrk hvrqqelllk llqqqqavpv ppapsspppl waglakqgls mktllelqle
      781 gerqlhkqpp preparaqap nhrvqlgglg taplnqwvse agplwggpdk sgggssglgl
      841 wedtpksggs lvrglglkns rsspslsdsy shlsgrpirk kteeeekllk llqgiprpqd
      901 gftqwceqml htlsatgsld vpmavailke vespydvhdy irsclgdtle akefakqfle
      961 rrakqkasqq rqqqqeawls saslqtafqa nhstklgpge gskakrralm lhsdpsilge
     1021 lgwgrsgtsl aqgrrspges sdaasprlqg tpctdllvrs rawmttdqpg ppapgl
//
LOCUS       NP_001337363             866 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 1 isoform 30 [Homo
            sapiens].
ACCESSION   NP_001337363
VERSION     NP_001337363.1
DBSOURCE    REFSEQ: accession NM_001350434.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 866)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 866)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 866)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 866)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 866)
  AUTHORS   Ruhle,F., Witten,A., Barysenka,A., Huge,A., Arning,A., Heller,C.,
            Krumpel,A., Mesters,R., Franke,A., Lieb,W., Riemenschneider,M.,
            Hiersche,M., Limperger,V., Nowak-Gottl,U. and Stoll,M.
  TITLE     Rare genetic variants in SMAP1, B3GAT2, and RIMS1 contribute to
            pediatric venous thromboembolism
  JOURNAL   Blood 129 (6), 783-790 (2017)
   PUBMED   28011674
  REMARK    GeneRIF: The study identified a region on chromosome 6 comprising
            the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus
            for pediatric venous thromboembolism.
REFERENCE   6  (residues 1 to 866)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 866)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
REFERENCE   8  (residues 1 to 866)
  AUTHORS   Schoch,S., Castillo,P.E., Jo,T., Mukherjee,K., Geppert,M., Wang,Y.,
            Schmitz,F., Malenka,R.C. and Sudhof,T.C.
  TITLE     RIM1alpha forms a protein scaffold for regulating neurotransmitter
            release at the active zone
  JOURNAL   Nature 415 (6869), 321-326 (2002)
   PUBMED   11797009
REFERENCE   9  (residues 1 to 866)
  AUTHORS   Coppola,T., Magnin-Luthi,S., Perret-Menoud,V., Gattesco,S.,
            Schiavo,G. and Regazzi,R.
  TITLE     Direct interaction of the Rab3 effector RIM with Ca2+ channels,
            SNAP-25, and synaptotagmin
  JOURNAL   J Biol Chem 276 (35), 32756-32762 (2001)
   PUBMED   11438518
REFERENCE   10 (residues 1 to 866)
  AUTHORS   Betz,A., Thakur,P., Junge,H.J., Ashery,U., Rhee,J.S., Scheuss,V.,
            Rosenmund,C., Rettig,J. and Brose,N.
  TITLE     Functional interaction of the active zone proteins Munc13-1 and
            RIM1 in synaptic vesicle priming
  JOURNAL   Neuron 30 (1), 183-196 (2001)
   PUBMED   11343654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590011.5, AL445256.18 and
            AL035633.18.
            
            Summary: The protein encoded by this gene is a RAS gene superfamily
            member that regulates synaptic vesicle exocytosis. This gene also
            plays a role in the regulation of voltage-gated calcium channels
            during neurotransmitter and insulin release. Mutations have
            suggested a role cognition and have been identified as the cause of
            cone-rod dystrophy type 7. Multiple transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Mar 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.155223.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..866
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..866
                     /product="regulating synaptic membrane exocytosis protein
                     1 isoform 30"
                     /note="RAB3-interacting protein 2; rab3-interacting
                     molecule 1; rab-3-interacting protein 2"
                     /calculated_mol_wt=97211
     Region          68..164
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(89..95,110,113,143,147,150..151)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          216..342
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(247,253,308,310,318)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          697..842
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(754,758..759,761,764,792,794,796,840..841)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..866
                     /gene="RIMS1"
                     /gene_synonym="CORD7; RAB3IP2; RIM; RIM1"
                     /coded_by="NM_001350434.2:231..2831"
                     /note="isoform 30 is encoded by transcript variant 30"
                     /db_xref="GeneID:22999"
                     /db_xref="HGNC:HGNC:17282"
                     /db_xref="MIM:606629"
ORIGIN      
        1 mcapgihvss egweevrsvd seegtiearr avagdldyyw ldpatwhsre tspisshpvt
       61 wqpskegdrl igrvilnkrt tmpkdsgall glkvvggkmt dlgrlgafit kvkkgsladv
      121 vghlragdev lewngkplpg atneevynii lesksepqve iivsrpigdi pripesshpp
      181 lesssssfes qkmerpsisv isptspgalk dapqvlpgql svklwydkvg hqlivnvlqa
      241 tdlparvdgr prnpyvkmyf lpdrsdkskr rtktvkkile pkwnqtfvys hvhrrdfrer
      301 mleitvwdqp rvqeeesefl geilieleta llddephwyk lqthdesslp lpqpspfmpr
      361 rhihgesssk klqrsqrisd sdisdyevdd gigvvppgyr ssareskstt ltvpeqqrtt
      421 hhrsrsvsph rgndqgkprs rlpnvplqrs ldeihptrrs rsptrhhdas rspvdhrtrd
      481 vdsqylseqd sellmlprak rgrsaeclht trhlvrhykt lppkmpllqs sshwniysel
      541 qpfldrarsa stnclrpdts lhspererhs rkserssiqk qtrkgtasda ermhrqrspt
      601 qsppadtsfs srrgrqlpqv pvrsgsieqe sghkklksti qrstetgmaa emrkmvrqps
      661 restdgsins yssegnlifp gvrlgadsqf sdfldglgpa qlvgrqtlat pamgdiqigm
      721 edkkgqleve virarsltqk pgskstpapy vkvyllenga ciakkktria rktldplyqq
      781 slvfdespqg kvlqvivwgd ygrmdhkcfm gvaqilleel dlssmvigwy klfppsslvd
      841 ptltpltrra sqsslesstg ppcirs
//
LOCUS       NP_001386784             511 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 35 [Homo sapiens].
ACCESSION   NP_001386784
VERSION     NP_001386784.1
DBSOURCE    REFSEQ: accession NM_001399855.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 511)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 511)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 511)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..511
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 35"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=57561
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          379..506
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..511
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001399855.1:671..2206"
                     /note="isoform 35 is encoded by transcript variant 38"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaksll kkpdgvkinn kanvvtspke niptpalepq ttvihnpdgn
      361 kestessntt iededvkark qeiikvteql ieainngdfe aytkicdpgl tafepealgn
      421 lvegmdfhrf yfenalsksn kpihtiilnp hvhlvgddaa ciayirltqy mdgsgmpktm
      481 qseetrvwhr rdgkwqnvhf hrsgsptvpi k
//
LOCUS       NP_001373809             670 aa            linear   PRI 21-NOV-2025
DEFINITION  solute carrier organic anion transporter family member 1A2 isoform
            1 [Homo sapiens].
ACCESSION   NP_001373809 XP_005253531
VERSION     NP_001373809.1
DBSOURCE    REFSEQ: accession NM_001386880.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Flogel,S., Tust,M., Boussettaoui,S., Fischer,D. and Grundemann,D.
  TITLE     Enhancing transporter activity in heterologous expression systems
            with SAHA: a 2500-times more potent and odorless alternative to
            butyrate
  JOURNAL   FEBS Open Bio 15 (6), 906-913 (2025)
   PUBMED   40052353
REFERENCE   2  (residues 1 to 670)
  AUTHORS   Kataoka,H., Akiyoshi,T., Uchida,Y., Imaoka,A., Terasaki,T. and
            Ohtani,H.
  TITLE     The Effects of N-Glycosylation on the Expression and Transport
            Activity of OATP1A2 and OATP2B1
  JOURNAL   J Pharm Sci 113 (5), 1376-1384 (2024)
   PUBMED   38432624
  REMARK    GeneRIF: The Effects of N-Glycosylation on the Expression and
            Transport Activity of OATP1A2 and OATP2B1.
REFERENCE   3  (residues 1 to 670)
  AUTHORS   Han,H., Akiyoshi,T., Morita,T., Kataoka,H., Katayama,K., Yajima,K.,
            Imaoka,A. and Ohtani,H.
  TITLE     Comparison of the transport kinetics of fexofenadine and its pH
            dependency among OATP1A2 genetic variants
  JOURNAL   Drug Metab Pharmacokinet 47, 100470 (2022)
   PUBMED   36116173
  REMARK    GeneRIF: Comparison of the transport kinetics of fexofenadine and
            its pH dependency among OATP1A2 genetic variants.
REFERENCE   4  (residues 1 to 670)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 670)
  AUTHORS   Hau,R.K., Klein,R.R., Wright,S.H. and Cherrington,N.J.
  TITLE     Localization of Xenobiotic Transporters Expressed at the Human
            Blood-Testis Barrier
  JOURNAL   Drug Metab Dispos 50 (6), 770-780 (2022)
   PUBMED   35307651
REFERENCE   6  (residues 1 to 670)
  AUTHORS   Kullak-Ublick,G.A., Fisch,T., Oswald,M., Hagenbuch,B., Meier,P.J.,
            Beuers,U. and Paumgartner,G.
  TITLE     Dehydroepiandrosterone sulfate (DHEAS): identification of a carrier
            protein in human liver and brain
  JOURNAL   FEBS Lett 424 (3), 173-176 (1998)
   PUBMED   9539145
REFERENCE   7  (residues 1 to 670)
  AUTHORS   Meier,P.J., Eckhardt,U., Schroeder,A., Hagenbuch,B. and Stieger,B.
  TITLE     Substrate specificity of sinusoidal bile acid and organic anion
            uptake systems in rat and human liver
  JOURNAL   Hepatology 26 (6), 1667-1677 (1997)
   PUBMED   9398014
  REMARK    Review article
REFERENCE   8  (residues 1 to 670)
  AUTHORS   Kullak-Ublick,G.A., Beuers,U., Fahney,C., Hagenbuch,B., Meier,P.J.
            and Paumgartner,G.
  TITLE     Identification and functional characterization of the promoter
            region of the human organic anion transporting polypeptide gene
  JOURNAL   Hepatology 26 (4), 991-997 (1997)
   PUBMED   9328325
REFERENCE   9  (residues 1 to 670)
  AUTHORS   Kullak-Ublick,G.A., Beuers,U., Meier,P.J., Domdey,H. and
            Paumgartner,G.
  TITLE     Assignment of the human organic anion transporting polypeptide
            (OATP) gene to chromosome 12p12 by fluorescence in situ
            hybridization
  JOURNAL   J Hepatol 25 (6), 985-987 (1996)
   PUBMED   9007731
REFERENCE   10 (residues 1 to 670)
  AUTHORS   Kullak-Ublick,G.A., Hagenbuch,B., Stieger,B., Schteingart,C.D.,
            Hofmann,A.F., Wolkoff,A.W. and Meier,P.J.
  TITLE     Molecular and functional characterization of an organic anion
            transporting polypeptide cloned from human liver
  JOURNAL   Gastroenterology 109 (4), 1274-1282 (1995)
   PUBMED   7557095
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022224.22.
            
            On Sep 25, 2020 this sequence version replaced XP_005253531.1.
            
            Summary: This gene encodes a sodium-independent transporter which
            mediates cellular uptake of organic ions in the liver. Its
            substrates include bile acids, bromosulphophthalein, and some
            steroidal compounds. The protein is a member of the SLC21A family
            of solute carriers. Alternative splicing of this gene results in
            multiple transcript variants. [provided by RefSeq, Dec 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.11286.1,
                                           SRR1803615.108954.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145122, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..670
                     /product="solute carrier organic anion transporter family
                     member 1A2 isoform 1"
                     /note="organic anion transporting polypeptide A; solute
                     carrier family 21 (organic anion transporter), member 3;
                     sodium-independent organic anion transporter; OATP-1;
                     solute carrier family 21 member 3; organic
                     anion-transporting polypeptide 1"
                     /calculated_mol_wt=74014
     Region          1..625
                     /region_name="oat"
                     /note="sodium-independent organic anion transporter;
                     TIGR00805"
                     /db_xref="CDD:273279"
     Site            21..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            60..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            87..111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            124
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P46721.1)"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P46721.1)"
     Site            156..184
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            204..224
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            243..267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            312..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            354..377
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            382..405
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            412
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P46721.1)"
     Site            419
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P46721.1)"
     Site            514..536
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            546..571
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            606..623
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     CDS             1..670
                     /gene="SLCO1A2"
                     /gene_synonym="OATP; OATP-A; OATP1A2; SLC21A3"
                     /coded_by="NM_001386880.1:149..2161"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS8686.1"
                     /db_xref="GeneID:6579"
                     /db_xref="HGNC:HGNC:10956"
                     /db_xref="MIM:602883"
ORIGIN      
        1 mgetekriet hrirclsklk mfllaitcaf vsktlsgsym nsmltqierq fniptslvgf
       61 ingsfeignl lliifvsyfg tklhrpimig igcvvmglgc flkslphflm nqyeyestvs
      121 vsgnlssnsf lcmengtqil rptqdpsect kevkslmwvy vlvgnivrgm getpilplgi
      181 syiedfakfe nsplyiglve tgaiigplig lllasfcanv yvdtgfvntd dliitptdtr
      241 wvgawwfgfl icagvnvlta ipffflpntl pkegletnad iiknenedkq keevkkekyg
      301 itkdflpfmk slscnpiyml filvsviqfn afvnmisfmp kyleqqygis ssdaiflmgi
      361 ynlppicigy iigglimkkf kitvkqaahi gcwlslleyl lyflsflmtc enssvvgint
      421 syegipqdly vendifadcn vdcncpskiw dpvcgnngls ylsaclagce tsigtginmv
      481 fqncsciqts gnssavlglc dkgpdcslml qyflilsams sfiyslaaip gymvllrcmk
      541 seekslgvgl htfctrvfag ipapiyfgal mdstclhwgt lkcgesgacr iydsttfryi
      601 ylglpaalrg ssfvpaliil illrkchlpg enassgteli etkvkgkene ckdiyqkstv
      661 lkddelktkl
//
LOCUS       NP_001362883             766 aa            linear   PRI 21-NOV-2025
DEFINITION  protein zer-1 homolog isoform 1 [Homo sapiens].
ACCESSION   NP_001362883 XP_005251702
VERSION     NP_001362883.1
DBSOURCE    REFSEQ: accession NM_001375954.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Yan,X., Li,Y., Wang,G., Zhou,Z., Song,G., Feng,Q., Zhao,Y., Mi,W.,
            Ma,Z. and Dong,C.
  TITLE     Molecular basis for recognition of Gly/N-degrons by CRL2ZYG11B and
            CRL2ZER1
  JOURNAL   Mol Cell 81 (16), 3262-3274 (2021)
   PUBMED   34214466
  REMARK    GeneRIF: Molecular basis for recognition of Gly/N-degrons by
            CRL2(ZYG11B) and CRL2(ZER1).
REFERENCE   2  (residues 1 to 766)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 766)
  AUTHORS   Timms,R.T., Zhang,Z., Rhee,D.Y., Harper,J.W., Koren,I. and
            Elledge,S.J.
  TITLE     A glycine-specific N-degron pathway mediates the quality control of
            protein N-myristoylation
  JOURNAL   Science 365 (6448) (2019)
   PUBMED   31273098
REFERENCE   4  (residues 1 to 766)
  AUTHORS   Wade,T.D., Gordon,S., Medland,S., Bulik,C.M., Heath,A.C.,
            Montgomery,G.W. and Martin,N.G.
  TITLE     Genetic variants associated with disordered eating
  JOURNAL   Int J Eat Disord 46 (6), 594-608 (2013)
   PUBMED   23568457
REFERENCE   5  (residues 1 to 766)
  AUTHORS   Cheng,C.Y., Schache,M., Ikram,M.K., Young,T.L., Guggenheim,J.A.,
            Vitart,V., MacGregor,S., Verhoeven,V.J., Barathi,V.A., Liao,J.,
            Hysi,P.G., Bailey-Wilson,J.E., St Pourcain,B., Kemp,J.P.,
            McMahon,G., Timpson,N.J., Evans,D.M., Montgomery,G.W., Mishra,A.,
            Wang,Y.X., Wang,J.J., Rochtchina,E., Polasek,O., Wright,A.F.,
            Amin,N., van Leeuwen,E.M., Wilson,J.F., Pennell,C.E., van
            Duijn,C.M., de Jong,P.T., Vingerling,J.R., Zhou,X., Chen,P., Li,R.,
            Tay,W.T., Zheng,Y., Chew,M., Burdon,K.P., Craig,J.E., Iyengar,S.K.,
            Igo,R.P. Jr., Lass,J.H. Jr., Chew,E.Y., Haller,T., Mihailov,E.,
            Metspalu,A., Wedenoja,J., Simpson,C.L., Wojciechowski,R., Hohn,R.,
            Mirshahi,A., Zeller,T., Pfeiffer,N., Lackner,K.J., Bettecken,T.,
            Meitinger,T., Oexle,K., Pirastu,M., Portas,L., Nag,A.,
            Williams,K.M., Yonova-Doing,E., Klein,R., Klein,B.E.,
            Hosseini,S.M., Paterson,A.D., Makela,K.M., Lehtimaki,T.,
            Kahonen,M., Raitakari,O., Yoshimura,N., Matsuda,F., Chen,L.J.,
            Pang,C.P., Yip,S.P., Yap,M.K., Meguro,A., Mizuki,N., Inoko,H.,
            Foster,P.J., Zhao,J.H., Vithana,E., Tai,E.S., Fan,Q., Xu,L.,
            Campbell,H., Fleck,B., Rudan,I., Aung,T., Hofman,A.,
            Uitterlinden,A.G., Bencic,G., Khor,C.C., Forward,H., Parssinen,O.,
            Mitchell,P., Rivadeneira,F., Hewitt,A.W., Williams,C., Oostra,B.A.,
            Teo,Y.Y., Hammond,C.J., Stambolian,D., Mackey,D.A., Klaver,C.C.,
            Wong,T.Y., Saw,S.M. and Baird,P.N.
  CONSRTM   Consortium for Refractive Error and Myopia; Fuchs' Genetics
            Multi-Center Study Group; Wellcome Trust Case Control Consortium 2;
            Diabetes Control and Complications Trial/Epidemiology of Diabetes
            Interventions, and Complications Research Group
  TITLE     Nine loci for ocular axial length identified through genome-wide
            association studies, including shared loci with refractive error
  JOURNAL   Am J Hum Genet 93 (2), 264-277 (2013)
   PUBMED   24144296
REFERENCE   6  (residues 1 to 766)
  AUTHORS   Okumura,F., Matsuzaki,M., Nakatsukasa,K. and Kamura,T.
  TITLE     The Role of Elongin BC-Containing Ubiquitin Ligases
  JOURNAL   Front Oncol 2, 10 (2012)
   PUBMED   22649776
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 766)
  AUTHORS   Vasudevan,S., Starostina,N.G. and Kipreos,E.T.
  TITLE     The Caenorhabditis elegans cell-cycle regulator ZYG-11 defines a
            conserved family of CUL-2 complex components
  JOURNAL   EMBO Rep 8 (3), 279-286 (2007)
   PUBMED   17304241
REFERENCE   8  (residues 1 to 766)
  AUTHORS   Feral,C., Wu,Y.Q., Pawlak,A. and Guellaen,G.
  TITLE     Meiotic human sperm cells express a leucine-rich homologue of
            Caenorhabditis elegans early embryogenesis gene, Zyg-11
  JOURNAL   Mol Hum Reprod 7 (12), 1115-1122 (2001)
   PUBMED   11719588
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL441992.17.
            
            On Nov 7, 2019 this sequence version replaced XP_005251702.1.
            
            Summary: This gene encodes a subunit of an E3 ubiquitin ligase
            complex that may be involved in meiosis. The encoded protein
            contains three leucine-rich repeat motifs. [provided by RefSeq, Nov
            2012].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1622352.1,
                                           SRR11853562.32434.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..766
                     /product="protein zer-1 homolog isoform 1"
                     /note="ZYG homolog; protein zer-1 homolog; zyg-11 homolog
                     B-like protein; zyg11b-like protein"
                     /calculated_mol_wt=88039
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          82..104
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          105..130
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          131..176
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          177..200
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          201..223
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          224..247
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          226..245
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          246..268
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          278..302
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          281..324
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          427..467
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          511..556
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Site            order(545,549,553,589,593,597,630,636,640)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          558..600
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          562..600
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          602..643
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          605..641
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          714..756
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     CDS             1..766
                     /gene="ZER1"
                     /gene_synonym="C9orf60; ZYG; ZYG11BL"
                     /coded_by="NM_001375954.1:208..2508"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6910.1"
                     /db_xref="GeneID:10444"
                     /db_xref="HGNC:HGNC:30960"
                     /db_xref="MIM:617764"
ORIGIN      
        1 masdtpeslm alctdfclrn ldgtlgylld ketlrlhpdi flpseicdrl vneyvelvna
       61 acnfephesf fslfsdprst rltrihlred lvqdqdleai rkqdlvelyl tnceklsaks
      121 lqtlrsfsht lvslslfgct nifyeeenpg gcedeylvnp tcqvlvkdft fegfsrlrfl
      181 nlgrmidwvp vesllrplns laaldlsgiq tsdaafltqw kdslvslvly nmdlsddhir
      241 vivqlhklrh ldisrdrlss yykfkltrev lslfvqklgn lmsldisghm ilencsiskm
      301 eeeagqtsie pskssiipfr alkrplqflg lfenslcrlt hipaykvsgd kneeqvlnai
      361 eaytehrpei tsrainllfd iariercnql lralklvita lkchkydrni qvtgsaalfy
      421 ltnseyrseq svklrrqviq vvlngmesyq evtvqrnccl tlcnfsipee lefqyrrvne
      481 lllsilnptr qdesiqriav hlcnalvcqv dndhkeavgk mgfvvtmlkl iqkklldktc
      541 dqvmefswsa lwnitdetpd ncemflnfng mklfldclke fpekqelhrn mlgllgnvae
      601 vkelrpqlmt sqfisvfsnl leskadgiev synacgvlsh imfdgpeawg vcepqreeve
      661 ermwaaiqsw dinsrrniny rsfepilrll pqgispvsqh watwalynlv svypdkycpl
      721 likeggmpll rdiikmatar qetkemarkv iehcsnfkee nmdtsr
//
LOCUS       NP_001372052             617 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 2 isoform g [Homo sapiens].
ACCESSION   NP_001372052
VERSION     NP_001372052.1
DBSOURCE    REFSEQ: accession NM_001385123.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 617)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 617)
  AUTHORS   Freire-Beneitez,V., Pomella,N., Millner,T.O., Dumas,A.A.,
            Niklison-Chirou,M.V., Maniati,E., Wang,J., Rajeeve,V., Cutillas,P.
            and Marino,S.
  TITLE     Elucidation of the BMI1 interactome identifies novel regulatory
            roles in glioblastoma
  JOURNAL   NAR Cancer 3 (1), zcab009 (2021)
   PUBMED   34316702
  REMARK    Erratum:[NAR Cancer. 2021 May 25;3(2):zcab020. doi:
            10.1093/narcan/zcab020. PMID: 34319293]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 617)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 617)
  AUTHORS   Tonkin,E., Hagan,D.M., Li,W. and Strachan,T.
  TITLE     Identification and characterisation of novel mammalian homologues
            of Drosophila polyhomeoticpermits new insights into relationships
            between members of the polyhomeotic family
  JOURNAL   Hum Genet 111 (4-5), 435-442 (2002)
   PUBMED   12384788
REFERENCE   7  (residues 1 to 617)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   8  (residues 1 to 617)
  AUTHORS   Gunther,M., Laithier,M. and Brison,O.
  TITLE     A set of proteins interacting with transcription factor Sp1
            identified in a two-hybrid screening
  JOURNAL   Mol Cell Biochem 210 (1-2), 131-142 (2000)
   PUBMED   10976766
REFERENCE   9  (residues 1 to 617)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   10 (residues 1 to 617)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138837.12 and AL513327.34.
            
            Summary: In Drosophila melanogaster, the 'Polycomb' group (PcG) of
            genes are part of a cellular memory system that is responsible for
            the stable inheritance of gene activity. PcG proteins form a large
            multimeric, chromatin-associated protein complex. The protein
            encoded by this gene has homology to the Drosophila PcG protein
            'polyhomeotic' (Ph) and is known to heterodimerize with EDR1 and
            colocalize with BMI1 in interphase nuclei of human cells. The
            specific function in human cells has not yet been determined. Two
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1965299, SAMEA1966682
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..617
                     /product="polyhomeotic-like protein 2 isoform g"
                     /note="early development regulator 2 (homolog of
                     polyhomeotic 2); polyhomeotic-like protein 2; early
                     development regulatory protein 2; polyhomeotic-like 2"
                     /calculated_mol_wt=66322
     Region          1..76
                     /region_name="Disordered.
                     /evidence=ECO:0000250|UniProtKB:Q9QWH1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXK0.1)"
     Region          33..53
                     /region_name="Interaction with BMI1.
                     /evidence=ECO:0000250|UniProtKB:Q9QWH1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXK0.1)"
     Region          <107..307
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          429..548
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          548..616
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(566..567,601..602,605..606,609)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(577..581,583..584,587..588,592,597)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..617
                     /gene="PHC2"
                     /gene_synonym="EDR2; HPH2; PH2"
                     /coded_by="NM_001385123.1:175..2028"
                     /note="isoform g is encoded by transcript variant 10"
                     /db_xref="GeneID:1912"
                     /db_xref="HGNC:HGNC:3183"
                     /db_xref="MIM:602979"
ORIGIN      
        1 menelpvpht sssacatsst sgassssgcn nsssggsgrp tgpqisvysg ipdrqtvqvi
       61 qqalhrqpst aaqylqqmya aqqqhlmlqt aalqqqhlss aqlqslaavq qpqpqqqqpp
      121 pqqsrpvlqa ephpqlasvs psvalqpsse ahamplgpvt palplqcpta nlhkpggsqq
      181 chpptpdtgp qnghpegvph tpqrrfqhts avilqlqpas pvpqqcvpdd wkevapgeks
      241 vpetrsgpsp hqqaivtamp gglpvptspn iqpspahetg qgivhaltdl sspgmtsgng
      301 nsassiagta pqngenkppq aivkpqilth viegfviqeg aepfpvgrss llvgnlkkky
      361 aqgflpeklp qqdhttttds emeepylqes keegaplklk celcgrvdfa ykfkrskrfc
      421 smacakrynv gctkrvglfh sdrsklqkag aathnrrras kaslppltkd tkkqptgtvp
      481 lsvtaalqlt hsqedssrcs dnssyeepls pisassstsr rrqgqrdlel pdmhmrdlvg
      541 mghhflpsep tkwnvedvye firslpgcqe iaeefraqei dgqallllke dhlmsamnik
      601 lgpalkiyar ismlkds
//
LOCUS       NP_001336752             415 aa            linear   PRI 21-NOV-2025
DEFINITION  sodium-dependent lysophosphatidylcholine symporter 1 isoform 8
            [Homo sapiens].
ACCESSION   NP_001336752
VERSION     NP_001336752.1
DBSOURCE    REFSEQ: accession NM_001349823.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Origuela,V., Ferrer-Aguilar,P., Gazquez,A., Perez-Cruz,M.,
            Gomez-Roig,M.D., Gomez-Llorente,C. and Larque,E.
  TITLE     Placental MFSD2A expression in fetal growth restriction and
            maternal and fetal DHA status
  JOURNAL   Placenta 150, 31-38 (2024)
   PUBMED   38583303
  REMARK    GeneRIF: Placental MFSD2A expression in fetal growth restriction
            and maternal and fetal DHA status.
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Yuan,W., Qiu,Z.M., Li,H., Huang,M., Yuan,J.J., Niu,S.L., Chen,Q.,
            Yang,Q.W. and Ouyang,Q.
  TITLE     Investigation of the Binding Interaction of Mfsd2a with NEDD4-2 via
            Molecular Dynamics Simulations
  JOURNAL   ACS Chem Neurosci 15 (2), 382-393 (2024)
   PUBMED   38155530
  REMARK    GeneRIF: Investigation of the Binding Interaction of Mfsd2a with
            NEDD4-2 via Molecular Dynamics Simulations.
REFERENCE   3  (residues 1 to 415)
  AUTHORS   He,M., Kuk,A.C.Y., Ding,M., Chin,C.F., Galam,D.L.A., Nah,J.M.,
            Tan,B.C., Yeo,H.L., Chua,G.L., Benke,P.I., Wenk,M.R., Ho,L.,
            Torta,F. and Silver,D.L.
  TITLE     Spns1 is a lysophospholipid transporter mediating lysosomal
            phospholipid salvage
  JOURNAL   Proc Natl Acad Sci U S A 119 (40), e2210353119 (2022)
   PUBMED   36161949
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Martinez-Molledo,M., Nji,E. and Reyes,N.
  TITLE     Structural insights into the lysophospholipid brain uptake
            mechanism and its inhibition by syncytin-2
  JOURNAL   Nat Struct Mol Biol 29 (6), 604-612 (2022)
   PUBMED   35710838
  REMARK    GeneRIF: Structural insights into the lysophospholipid brain uptake
            mechanism and its inhibition by syncytin-2.
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Khuller,K., Yigit,G., Martinez Grijalva,C., Altmuller,J.,
            Thiele,H., Nurnberg,P., Elcioglu,N.H., Yeter,B., Hehr,U., Stein,A.,
            Della Marina,A., Koninger,A., Depienne,C., Kaiser,F.J., Wollnik,B.
            and Kuechler,A.
  TITLE     MFSD2A-associated primary microcephaly - Expanding the clinical and
            mutational spectrum of this ultra-rare disease
  JOURNAL   Eur J Med Genet 64 (10), 104310 (2021)
   PUBMED   34400370
  REMARK    GeneRIF: MFSD2A-associated primary microcephaly - Expanding the
            clinical and mutational spectrum of this ultra-rare disease.
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Spinola,M., Falvella,F.S., Colombo,F., Sullivan,J.P., Shames,D.S.,
            Girard,L., Spessotto,P., Minna,J.D. and Dragani,T.A.
  TITLE     MFSD2A is a novel lung tumor suppressor gene modulating cell cycle
            and matrix attachment
  JOURNAL   Mol Cancer 9, 62 (2010)
   PUBMED   20236515
  REMARK    GeneRIF: MFSD2A is a novel lung cancer tumor suppressor gene that
            regulates cell cycle progression and matrix attachment.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Angers,M., Uldry,M., Kong,D., Gimble,J.M. and Jetten,A.M.
  TITLE     Mfsd2a encodes a novel major facilitator superfamily
            domain-containing protein highly induced in brown adipose tissue
            during fasting and adaptive thermogenesis
  JOURNAL   Biochem J 416 (3), 347-355 (2008)
   PUBMED   18694395
  REMARK    GeneRIF: Results identify Mfsd2a (major facilitator superfamily
            domain-containing protein 2a) and an additional closely related
            protein Mfsd2b, and suggest that Mfsd2a plays a role in adaptive
            thermogenesis.
REFERENCE   8  (residues 1 to 415)
  AUTHORS   Esnault,C., Priet,S., Ribet,D., Vernochet,C., Bruls,T.,
            Lavialle,C., Weissenbach,J. and Heidmann,T.
  TITLE     A placenta-specific receptor for the fusogenic, endogenous
            retrovirus-derived, human syncytin-2
  JOURNAL   Proc Natl Acad Sci U S A 105 (45), 17532-17537 (2008)
   PUBMED   18988732
  REMARK    GeneRIF: MFSD2 is a placenta-specific receptor for the fusogenic,
            endogenous retrovirus-derived, human syncytin-2, and plays a role
            in placenta morphogenesis.
REFERENCE   9  (residues 1 to 415)
  AUTHORS   Spinola,M., Falvella,F.S., Galvan,A., Pignatiello,C., Leoni,V.P.,
            Pastorino,U., Paroni,R., Chen,S., Skaug,V., Haugen,A. and
            Dragani,T.A.
  TITLE     Ethnic differences in frequencies of gene polymorphisms in the
            MYCL1 region and modulation of lung cancer patients' survival
  JOURNAL   Lung Cancer 55 (3), 271-277 (2007)
   PUBMED   17145094
  REMARK    GeneRIF: three additional SNPs in the MFSD2 genes showed ethnic
            differences in allelic frequencies
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 415)
  AUTHORS   Yamada,S., Ohira,M., Horie,H., Ando,K., Takayasu,H., Suzuki,Y.,
            Sugano,S., Hirata,T., Goto,T., Matsunaga,T., Hiyama,E., Hayashi,Y.,
            Ando,H., Suita,S., Kaneko,M., Sasaki,F., Hashizume,K., Ohnuma,N.
            and Nakagawara,A.
  TITLE     Expression profiling and differential screening between
            hepatoblastomas and the corresponding normal livers: identification
            of high expression of the PLK1 oncogene as a poor-prognostic
            indicator of hepatoblastomas
  JOURNAL   Oncogene 23 (35), 5901-5911 (2004)
   PUBMED   15221005
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL663070.15.
            
            Summary: The protein encoded by this gene is a transmembrane
            protein and sodium-dependent lysophosphatidylcholine transporter.
            The encoded protein is involved in the establishment of the
            blood-brain barrier and is required for brain growth and function.
            Defects in this gene are a cause of a progressive microcephaly
            syndrome. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (8) encodes isoform 8.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3444292.1,
                                           SRR1660803.158731.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145893, SAMEA2147596
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.2"
     Protein         1..415
                     /product="sodium-dependent lysophosphatidylcholine
                     symporter 1 isoform 8"
                     /note="major facilitator superfamily domain-containing
                     protein 2A; sodium-dependent LPC symporter 1;
                     sodium-dependent lysophosphatidylcholine symporter 1;
                     major facilitator superfamily domain containing 2A"
                     /calculated_mol_wt=46323
     Region          1..381
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            order(43..44,46..48,51,72,75..76,79,186,189..190,193..195,
                     198,226,230,279..280,284,288,313,316..317,320..321,324)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341009"
     CDS             1..415
                     /gene="MFSD2A"
                     /gene_synonym="HsMFSD2A; MCPH15; MFSD2; NEDMISBA; NLS1;
                     SLC59A1"
                     /coded_by="NM_001349823.2:490..1737"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:84879"
                     /db_xref="HGNC:HGNC:25897"
                     /db_xref="MIM:614397"
ORIGIN      
        1 mpwiifstpl aviayfliwf vpdfphgqty wyllfyclfe tmvtcfhvpy saltmfiste
       61 qterdsatay rmtvevlgtv lgtaiqgqiv gqadtpcfqd lnsstvasqs anhthgttsh
      121 retqkaylla agvivciyii cavililgvr eqrepyeaqq sepiayfrgl rlvmshgpyi
      181 klitgflfts lafmlvegnf vlfctytlgf rnefqnllla imlsatltip iwqwfltrfg
      241 kktavyvgis savpflilva lmesnliity avavaagisv aaafllpwsm lpdviddfhl
      301 kqphfhgtep iffsfyvfft kfasgvslgi stlsldfagy qtrgcsqper vkftlnmlvt
      361 mapivlillg lllfkmypid eerrrqnkka lqalrdeass sgcsetdste lasil
//
LOCUS       NP_001254712            1179 aa            linear   PRI 21-NOV-2025
DEFINITION  activating molecule in BECN1-regulated autophagy protein 1 isoform
            3 [Homo sapiens].
ACCESSION   NP_001254712
VERSION     NP_001254712.1
DBSOURCE    REFSEQ: accession NM_001267783.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1179)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1179)
  AUTHORS   Gottlieb,S., Shang,W., Ye,D., Kubo,S., Jiang,P.D., Shafer,S.,
            Xu,L., Zheng,L., Park,A.Y., Song,J., Chan,W., Zeng,Z., He,T.,
            Schwarz,B., Haupl,B., Oellerich,T., Lenardo,M.J. and Yao,Y.
  TITLE     AMBRA1 controls the translation of immune-specific genes in T
            lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2416722121 (2024)
   PUBMED   39436665
  REMARK    GeneRIF: AMBRA1 controls the translation of immune-specific genes
            in T lymphocytes.
REFERENCE   3  (residues 1 to 1179)
  AUTHORS   Sankar,D.S., Kaeser-Pebernard,S., Vionnet,C., Favre,S., de Oliveira
            Marchioro,L., Pillet,B., Zhou,J., Stumpe,M., Kovacs,W.J.,
            Kressler,D., Antonioli,M., Fimia,G.M. and Dengjel,J.
  TITLE     The ULK1 effector BAG2 regulates autophagy initiation by modulating
            AMBRA1 localization
  JOURNAL   Cell Rep 43 (9), 114689 (2024)
   PUBMED   39207901
  REMARK    GeneRIF: The ULK1 effector BAG2 regulates autophagy initiation by
            modulating AMBRA1 localization.
REFERENCE   4  (residues 1 to 1179)
  AUTHORS   Di Leo,L., Pagliuca,C., Kishk,A., Rizza,S., Tsiavou,C.,
            Pecorari,C., Dahl,C., Pacheco,M.P., Tholstrup,R., Brewer,J.R.,
            Berico,P., Hernando,E., Cecconi,F., Ballotti,R., Bertolotto,C.,
            Filomeni,G., Gjerstorff,M.F., Sauter,T., Lovat,P., Guldberg,P. and
            De Zio,D.
  TITLE     AMBRA1 levels predict resistance to MAPK inhibitors in melanoma
  JOURNAL   Proc Natl Acad Sci U S A 121 (25), e2400566121 (2024)
   PUBMED   38870061
  REMARK    GeneRIF: AMBRA1 levels predict resistance to MAPK inhibitors in
            melanoma.
REFERENCE   5  (residues 1 to 1179)
  AUTHORS   Qu,X., Li,X.Y., Feng,Y., Wang,X., Li,L., Wang,Y.P. and Chu,Y.L.
  TITLE     sh- Ambra1 inhibits IRS-1/PI3K/Akt signalling pathway to reduce
            autophagy in gestational diabetes
  JOURNAL   Endokrynol Pol 75 (1), 61-70 (2024)
   PUBMED   38497391
  REMARK    GeneRIF: sh- Ambra1 inhibits IRS-1/PI3K/Akt signalling pathway to
            reduce autophagy in gestational diabetes.
REFERENCE   6  (residues 1 to 1179)
  AUTHORS   Cecconi,F., Di Bartolomeo,S., Nardacci,R., Fuoco,C., Corazzari,M.,
            Giunta,L., Romagnoli,A., Stoykova,A., Chowdhury,K., Fimia,G.M. and
            Piacentini,M.
  TITLE     A novel role for autophagy in neurodevelopment
  JOURNAL   Autophagy 3 (5), 506-508 (2007)
   PUBMED   17622796
REFERENCE   7  (residues 1 to 1179)
  AUTHORS   Le Bot,N.
  TITLE     Autophagy: a new regulator of development
  JOURNAL   Nat Cell Biol 9 (7), 741 (2007)
   PUBMED   17603510
REFERENCE   8  (residues 1 to 1179)
  AUTHORS   Fimia,G.M., Stoykova,A., Romagnoli,A., Giunta,L., Di Bartolomeo,S.,
            Nardacci,R., Corazzari,M., Fuoco,C., Ucar,A., Schwartz,P.,
            Gruss,P., Piacentini,M., Chowdhury,K. and Cecconi,F.
  TITLE     Ambra1 regulates autophagy and development of the nervous system
  JOURNAL   Nature 447 (7148), 1121-1125 (2007)
   PUBMED   17589504
REFERENCE   9  (residues 1 to 1179)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1179)
  AUTHORS   Meyerson,M. and Harlow,E.
  TITLE     Identification of G1 kinase activity for cdk6, a novel cyclin D
            partner
  JOURNAL   Mol Cell Biol 14 (3), 2077-2086 (1994)
   PUBMED   8114739
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB070055.1, AL834190.1 and DQ870924.1.
            
            Transcript Variant: This variant (3) lacks two consecutive exons in
            the coding region, but maintains the reading frame, compared to
            variant 1. The encoded isoform (3) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL834190.1, SRR11853561.4863.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1179
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..1179
                     /product="activating molecule in BECN1-regulated autophagy
                     protein 1 isoform 3"
                     /note="WD repeat domain 94; DDB1 and CUL4 associated
                     factor 3; activating molecule in BECN1-regulated autophagy
                     protein 1; activating molecule in beclin-1-regulated
                     autophagy; autophagy/beclin-1 regulator 1"
                     /calculated_mol_wt=129468
     Region          1..22
                     /region_name="Interaction with DDB1.
                     /evidence=ECO:0000269|PubMed:30166453"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          51..90
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000269|PubMed:23524951; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          56..92
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <59..198
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          93..133
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          99..135
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          135..175
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          140..176
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..1179
                     /gene="AMBRA1"
                     /gene_synonym="DCAF3; WDR94"
                     /coded_by="NM_001267783.2:317..3856"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58132.1"
                     /db_xref="GeneID:55626"
                     /db_xref="HGNC:HGNC:25990"
                     /db_xref="MIM:611359"
ORIGIN      
        1 mkvvpeknav rilwgrerga ramgaqrllq elvedktrwm kwegkrvelp dsprstflla
       61 fspdrtllas thvnhniyit evktgkcvhs lighrrtpwc vtfhptisgl iasgcldgev
      121 riwdlhggse swftdsnnai aslafhptaq llliatanei hfwdwsrrep favvktasem
      181 ervrlvrfdp lghylltaiv npsnqqgdde peipidgtel shyrqrallq sqpvrrtpll
      241 hnflhmlssr ssgiqtepfh ppeqasstqq dqgllnrpsa fstvqsstag ntlrnlslgp
      301 trrslggpls shpsryhrei apgltgsewt rtvlslnsrs eaesmppprt sassvsllsv
      361 lrqqeggsqa svytsategr gfpasglate sdggngssqn nsgsirhelq cdlrrffley
      421 drlqeldqsl sgeapqtqqa qemlnnnies erpgpshqpt phssennsnl srghlnrcra
      481 chnlltfnnd tlrwerttpn yssgeasssw qvpssfesvp ssgsqlpple rtegqtpsss
      541 rlelsssasp qeertvgvaf nqetghweri ytqssrsgtv sqealhqdmp eesseedslr
      601 rlspaayyaq rmiqylsrrd sirqrsmryq qnrlrsstss sssdnqgpsv egtdlefedf
      661 edngdrsrhr aprnarmsap slgrfvprrf llpeylpyag ifhergqpgl athssvnrvl
      721 agavigdgqs avasniantt yrlqwwdftk fdlpeisnas vnvlvqncki yndascdisa
      781 dgqllaafip ssqrgfpdeg ilavyslaph nlgemlytkr fgpnaisvsl spmgryvmvg
      841 lasrrillhp stehmvaqvf rlqqahgget smrrvfnvly pmpadqrrhv sinsarwlpe
      901 pglglaygtn kgdlvicrpe alnsgveyyw dqlnetvftv hsnsrsserp gtsratwrtd
      961 rdmglmnaig lqprnpatsv tsqgtqtlal qlqnaetqte revpepgtaa sgpgegegse
     1021 ygasgedals riqrlmaegg mtavvqreqs ttmasmggfg nniivshrih rssqtgtepg
     1081 aahtsspqps tsrgllpeag qlaerglspr taswdqpgtp greptqptlp ssspvpipvs
     1141 lpsaegptlh celtnnnhll dggssrgdaa gprgeprnr
//
LOCUS       NP_001307827             592 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 8 [Homo sapiens].
ACCESSION   NP_001307827
VERSION     NP_001307827.1
DBSOURCE    REFSEQ: accession NM_001320898.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 592)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 592)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 592)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 592)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 592)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DR002605.1, AK225771.1,
            BC034044.1, AC022400.9, AK131199.1 and AW295338.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.129671.1,
                                           SRR1803613.89191.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..592
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 8"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=65205
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          433..>488
                     /region_name="NTF2_like"
                     /note="Nuclear transport factor 2 (NTF2-like) superfamily.
                     This family includes members of the NTF2 family,
                     Delta-5-3-ketosteroid isomerases, Scytalone Dehydratases,
                     and the beta subunit of Ring hydroxylating dioxygenases.
                     This family is a classic example of...; cl09109"
                     /db_xref="CDD:471850"
     CDS             1..592
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001320898.2:95..1873"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kkrkssssvh
      361 lmepqttvvh natdgikgst escntttede dlkaaplrtg ngssvpegrs srdrtapsag
      421 mqpqpslcss amrkqeiiki teqlieainn gdfeaytkic dpgltsfepe algnlvegmd
      481 fhkfyfenre wvraadillp aplplclcll ltfssqlptf plfdlraall lcmlvplcpd
      541 gcrqaplkal llsskchsfc scfvavpvtt ikltyflpga vayacnpntl gg
//
LOCUS       NP_001387284             310 aa            linear   PRI 21-NOV-2025
DEFINITION  single-stranded DNA-binding protein 2 isoform 23 [Homo sapiens].
ACCESSION   NP_001387284
VERSION     NP_001387284.1
DBSOURCE    REFSEQ: accession NM_001400355.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Schwab,C., Roberts,K., Boer,J.M., Gohring,G., Steinemann,D.,
            Vora,A., Macartney,C., Hough,R., Thorn,Z., Dillon,R., Escherich,G.,
            Cazzaniga,G., Schlegelberger,B., Loh,M., den Boer,M.L.,
            Moorman,A.V. and Harrison,C.J.
  TITLE     SSBP2-CSF1R is a recurrent fusion in B-lineage acute lymphoblastic
            leukemia with diverse genetic presentation and variable outcome
  JOURNAL   Blood 137 (13), 1835-1838 (2021)
   PUBMED   33197935
  REMARK    GeneRIF: SSBP2-CSF1R is a recurrent fusion in B-lineage acute
            lymphoblastic leukemia with diverse genetic presentation and
            variable outcome.
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Wang,H., Kim,J., Wang,Z., Yan,X.X., Dean,A. and Xu,W.
  TITLE     Crystal structure of human LDB1 in complex with SSBP2
  JOURNAL   Proc Natl Acad Sci U S A 117 (2), 1042-1048 (2020)
   PUBMED   31892537
  REMARK    GeneRIF: Single-stranded DNA binding proteins (SSBPs) interact
            specifically with the LDB/Chip conserved domain (LCCD) of LDB
            proteins and stabilize LDBs by preventing their proteasomal
            degradation, thus promoting their functions in gene regulation.
REFERENCE   5  (residues 1 to 310)
  AUTHORS   Kim,H., Kim,Y., Bang,S., Park,S., Jee,S., Sim,J., Shin,S.J.,
            Paik,S.S. and Jang,K.
  TITLE     Low Expression of Single-stranded DNA Binding Protein 2 (SSBP2)
            Predicts Unfavourable Postoperative Outcomes in Patients With Clear
            Cell Renal Cell Carcinoma
  JOURNAL   In Vivo 34 (1), 101-107 (2020)
   PUBMED   31882468
  REMARK    GeneRIF: CcRCC with low SSBP2 expression was associated with
            adverse clinicopathological characteristics and poor patient
            outcomes.
REFERENCE   6  (residues 1 to 310)
  AUTHORS   Fleisig,H.B., Orazio,N.I., Liang,H., Tyler,A.F., Adams,H.P.,
            Weitzman,M.D. and Nagarajan,L.
  TITLE     Adenoviral E1B55K oncoprotein sequesters candidate leukemia
            suppressor sequence-specific single-stranded DNA-binding protein 2
            into aggresomes
  JOURNAL   Oncogene 26 (33), 4797-4805 (2007)
   PUBMED   17311003
  REMARK    GeneRIF: Results suggest that subverting SSBP2 function by
            oncoprotein E1B55K may contribute to cell transformation by viral
            oncoproteins.
REFERENCE   7  (residues 1 to 310)
  AUTHORS   Liang,H., Samanta,S. and Nagarajan,L.
  TITLE     SSBP2, a candidate tumor suppressor gene, induces growth arrest and
            differentiation of myeloid leukemia cells
  JOURNAL   Oncogene 24 (16), 2625-2634 (2005)
   PUBMED   15782145
  REMARK    GeneRIF: Our findings are consistent with human SSBP2 being a novel
            regulator of hematopoietic growth and differentiation, whose loss
            confers a block in differentiation advantage to myeloid leukemic
            cells.
REFERENCE   8  (residues 1 to 310)
  AUTHORS   Castro,P., Liang,H., Liang,J.C. and Nagarajan,L.
  TITLE     A novel, evolutionarily conserved gene family with putative
            sequence-specific single-stranded DNA-binding activity
  JOURNAL   Genomics 80 (1), 78-85 (2002)
   PUBMED   12079286
  REMARK    GeneRIF: Member of a closely related, evolutionarily conserved, and
            ubiquitously expressed gene family, potential tumor suppressor
REFERENCE   9  (residues 1 to 310)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 310)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016562.7, AC093250.3,
            AC026419.5 and AC010623.10.
            
            Summary: This gene encodes a subunit of a protein complex that
            interacts with single-stranded DNA and is involved in the DNA
            damage response and maintenance of genome stability. The encoded
            protein may also play a role in telomere repair. A variant of this
            gene may be associated with survival in human glioblastoma
            patients. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1965299, SAMEA1966682
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.1"
     Protein         1..310
                     /product="single-stranded DNA-binding protein 2 isoform
                     23"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein 2"
                     /calculated_mol_wt=32614
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CYZ8; propagated from
                     UniProtKB/Swiss-Prot (P81877.2)"
     Region          19..45
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          83..287
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     Region          147..171
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P81877.2)"
     CDS             1..310
                     /gene="SSBP2"
                     /gene_synonym="HSPC116; SOSS-B2"
                     /coded_by="NM_001400355.1:56..988"
                     /note="isoform 23 is encoded by transcript variant 26"
                     /db_xref="GeneID:23635"
                     /db_xref="HGNC:HGNC:15831"
                     /db_xref="MIM:607389"
ORIGIN      
        1 mygkgksnss avpsdsqare klalyvyeyl lhvgaqksaq tflseirwek nitlgeppgf
       61 lhswwcvfwd lycaaperre tcehsseaka fhdysaaaap spvlgnippg dgmpvgpvpp
      121 gffqpfmspr ypggprpplr ipnqalggvp gsqpllpsgm dptrqqghpn mggpmqrmtp
      181 prgmvplgpq gppggggppg tpimpspads tnsgdnmytl mnavppgpnr pnfpmgpgsd
      241 gpmgglggme shhmngslgs gdmdsiskns pnnmslsnqp gtprddgemg gnflnpfqse
      301 syspsmtmsv
//
LOCUS       NP_001273103            1051 aa            linear   PRI 21-NOV-2025
DEFINITION  C2 domain-containing protein 5 isoform a [Homo sapiens].
ACCESSION   NP_001273103
VERSION     NP_001273103.1
DBSOURCE    REFSEQ: accession NM_001286174.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1051)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1051)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1051)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1051)
  AUTHORS   Chapman,D.E., Reddy,B.J.N., Huy,B., Bovyn,M.J., Cruz,S.J.S.,
            Al-Shammari,Z.M., Han,H., Wang,W., Smith,D.S. and Gross,S.P.
  TITLE     Regulation of in vivo dynein force production by CDK5 and
            14-3-3epsilon and KIAA0528
  JOURNAL   Nat Commun 10 (1), 228 (2019)
   PUBMED   30651536
  REMARK    GeneRIF: Study finds that CDK5, 14-3-3 epsilon, and KIAA0528 are
            all essential for cytoplasmic dynein force adaptation and that they
            regulate the transport of lipid droplets, lysosomes, and
            mitochondria.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1051)
  AUTHORS   Lu,Y., Ma,J., Li,Y., Huang,J., Zhang,S., Yin,Z., Ren,J., Huang,K.,
            Wu,G., Yang,K. and Xu,S.
  TITLE     CDP138 silencing inhibits TGF-beta/Smad signaling to impair
            radioresistance and metastasis via GDF15 in lung cancer
  JOURNAL   Cell Death Dis 8 (9), e3036 (2017)
   PUBMED   28880265
  REMARK    GeneRIF: Enhanced radiosensitivity and decreased migration in cells
            caused by CDP138 knockdown are partially dependent on GDF15
            inhibition.
            Erratum:[Cell Death Dis. 2024 Jul 31;15(7):549. doi:
            10.1038/s41419-024-06823-2. PMID: 39085215]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1051)
  AUTHORS   Xu,S., Li,X., Gong,Z., Wang,W., Li,Y., Nair,B.C., Piao,H., Yang,K.,
            Wu,G. and Chen,J.
  TITLE     Proteomic analysis of the human cyclin-dependent kinase family
            reveals a novel CDK5 complex involved in cell growth and migration
  JOURNAL   Mol Cell Proteomics 13 (11), 2986-3000 (2014)
   PUBMED   25096995
REFERENCE   7  (residues 1 to 1051)
  AUTHORS   Xie,X., Gong,Z., Mansuy-Aubert,V., Zhou,Q.L., Tatulian,S.A.,
            Sehrt,D., Gnad,F., Brill,L.M., Motamedchaboki,K., Chen,Y.,
            Czech,M.P., Mann,M., Kruger,M. and Jiang,Z.Y.
  TITLE     C2 domain-containing phosphoprotein CDP138 regulates GLUT4
            insertion into the plasma membrane
  JOURNAL   Cell Metab 14 (3), 378-389 (2011)
   PUBMED   21907143
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK299353.1, BP418369.1 and AY166851.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1 and 2 encode the same isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK299353.1, SRR18074967.2239991.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1051
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..1051
                     /product="C2 domain-containing protein 5 isoform a"
                     /note="138 kDa C2 domain-containing phosphoprotein; C2
                     domain-containing protein 5"
                     /calculated_mol_wt=115897
     Region          5..114
                     /region_name="C2_KIAA0528-like"
                     /note="C2 domain found in the Human KIAA0528 cDNA clone;
                     cd08688"
                     /db_xref="CDD:176070"
     CDS             1..1051
                     /gene="C2CD5"
                     /gene_synonym="CDP138; KIAA0528"
                     /coded_by="NM_001286174.3:48..3203"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS66337.1"
                     /db_xref="GeneID:9847"
                     /db_xref="HGNC:HGNC:29062"
                     /db_xref="MIM:618044"
ORIGIN      
        1 mpgklkvkiv agrhlpvmdr asdltdafve vkfgnttfkt dvylkslnpq wnsewfkfev
       61 ddedlqdepl qitvldhdty sandaigkvy ididpllyse aatvisgwfp iydtihgirg
      121 einvvvkvdl fndlnrfrqs scgvkffctt sipkcyravi ihgfveelvv nedpeyqwid
      181 rirtprasne arqrlislms gelqrkiglk vlemrgnavv gylqcfdleg esglvvraig
      241 tactldklss paaflpacns pskemkeipf nedpnpnths sgpstplknq tysfspsksy
      301 srqssssdtd lsltpktgmg sgsagkeggp fkallrqqtq saleqrefpf ftltafppgf
      361 lvhvggvvsa rsvklldrih npdepetrda wwaeirqeik shakalgcha vvgysestsi
      421 ceevcilsas gtaavlnprf lqdgtvegcl eqrleenlpt rcgfchipyd elnmpfpahl
      481 tycyncrkqk vpdvlfttid lptdatvigk gcliqarlcr lkkkaqaean ataisnllpf
      541 meyevhtqlm nklklkgmna lfglriqitv genmlmglas atgvylaalp tpggiqiagk
      601 tpndgsyeqh ishmqkkind tiaknkelye inppeiseei igspipeprq rsrllrsqse
      661 ssdevteldl shgkkdafvl eiddtdamed vhslltdvpp psgfyscnte impginnwts
      721 eiqmftsvrv irlsslnltn qalnknfndl cenllkslyf klrsmipccl chvnftvslp
      781 edeliqvtvt avaitfdknq alqttktpve kslqrastdn eellqfplel csdslpshpf
      841 ppakehlesa ssnsgipaaq ratsvdyssf adrcsswiel iklkaqtirr gsikttmtve
      901 kaspvgdgnf rnrsappcan stvgvvkmtp lsfipgakit kylgiinmff irettslree
      961 ggvsgflhaf iaevfamvra hvaalggnav vsyimkqcvf menpnknqaq clinvsgdav
     1021 vfvresdlev vssqqpttnc qssctegevt t
//
LOCUS       NP_001309783             406 aa            linear   PRI 21-NOV-2025
DEFINITION  NIPA-like protein 3 isoform a [Homo sapiens].
ACCESSION   NP_001309783 XP_011540109
VERSION     NP_001309783.1
DBSOURCE    REFSEQ: accession NM_001322854.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Grzmil,P., Konietzko,J., Boehm,D., Holter,S.M.,
            Aguilar-Pimentel,A., Javaheri,A., Kalaydjiev,S., Adler,T.,
            Bolle,I., Adham,I., Dixkens,C., Wolf,S., Fuchs,H.,
            Gailus-Durner,V., Wurst,W., Ollert,M., Busch,D.H., Schulz,H., de
            Angelis,M.H. and Burfeind,P.
  TITLE     Targeted disruption of the mouse Npal3 gene leads to deficits in
            behavior, increased IgE levels, and impaired lung function
  JOURNAL   Cytogenet Genome Res 125 (3), 186-200 (2009)
   PUBMED   19738379
  REMARK    GeneRIF: Study demonstrates that both human NPAL3 and mouse NPAL3
            are ubiquitously expressed and encode highly conserved proteins
            Erratum:[Cytogenet Genome Res. 2009;125(4):285. Hoelter, S M
            [corrected to Holter, S M]; Aguilar, A [corrected to
            Aguilar-Pimentel, A]; Gailus-Durne, V [corrected to Gailus-Durner,
            V]; Busch, D [corrected to Busch, D H]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL031431.8.
            
            On Apr 14, 2016 this sequence version replaced XP_011540109.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3117424.1,
                                           SRR14038196.2251267.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..406
                     /product="NIPA-like protein 3 isoform a"
                     /note="NIPA-like protein 3"
                     /calculated_mol_wt=44611
     Region          32..326
                     /region_name="EamA"
                     /note="EamA-like transporter family; cl23754"
                     /db_xref="CDD:474045"
     Site            33..53
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            76..96
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            101..121
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            135..155
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            171..191
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            202..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            240..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            271..291
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            300..320
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q6P499.1)"
     CDS             1..406
                     /gene="NIPAL3"
                     /gene_synonym="DJ462O23.2; NPAL3; SLC57A5"
                     /coded_by="NM_001322854.2:509..1729"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS30631.1"
                     /db_xref="GeneID:57185"
                     /db_xref="HGNC:HGNC:25233"
                     /db_xref="MIM:620034"
ORIGIN      
        1 mdgshsaalk lqqlpptsss savseasfsy kenligalla ifghlvvsia lnlqkychir
       61 lagskdpray fktktwwlgl flmllgelgv fasyafapls livplsavsv iasaiigiif
      121 ikekwkpkdf lrryvlsfvg cglavvgtyl lvtfapnshe kmtgenvtrh lvswpfllym
      181 lveiilfcll lyfykeknan nivvilllva llgsmtvvtv kavagmlvls iqgnlqldyp
      241 ifyvmfvcmv atavyqaafl sqasqmydss liasvgyils ttiaitagai fyldfigedv
      301 lhicmfalgc liaflgvfli trnrkkpipf epyismdamp gmqnmhdkgm tvqpelkasf
      361 sygalenndn iseiyapatl pvmqeehgsr sasgvpyrvl ehtkke
//
LOCUS       NP_001305653             518 aa            linear   PRI 21-NOV-2025
DEFINITION  kelch repeat and BTB domain-containing protein 4 isoform b [Homo
            sapiens].
ACCESSION   NP_001305653
VERSION     NP_001305653.1
DBSOURCE    REFSEQ: accession NM_001318724.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Tsay,A. and Wang,J.C.
  TITLE     The Role of PIK3R1 in Metabolic Function and Insulin Sensitivity
  JOURNAL   Int J Mol Sci 24 (16), 12665 (2023)
   PUBMED   37628845
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Chen,Z., Ioris,R.M., Richardson,S., Van Ess,A.N., Vendrell,I.,
            Kessler,B.M., Buffa,F.M., Busino,L., Clifford,S.C., Bullock,A.N.
            and D'Angiolella,V.
  TITLE     Disease-associated KBTBD4 mutations in medulloblastoma elicit
            neomorphic ubiquitylation activity to promote CoREST degradation
  JOURNAL   Cell Death Differ 29 (10), 1955-1969 (2022)
   PUBMED   35379950
  REMARK    GeneRIF: Disease-associated KBTBD4 mutations in medulloblastoma
            elicit neomorphic ubiquitylation activity to promote CoREST
            degradation.
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Uchida,E., Sasaki,A., Shirahata,M., Suzuki,T., Adachi,J.I.,
            Mishima,K., Yasuda,M., Fujimaki,T., Ichimura,K. and Nishikawa,R.
  TITLE     Role of proliferative marker index and KBTBD4 mutation in the
            pathological diagnosis of pineal parenchymal tumors
  JOURNAL   Brain Tumor Pathol 39 (3), 130-138 (2022)
   PUBMED   35000018
  REMARK    GeneRIF: Role of proliferative marker index and KBTBD4 mutation in
            the pathological diagnosis of pineal parenchymal tumors.
REFERENCE   4  (residues 1 to 518)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 518)
  AUTHORS   Leal,L.F., Cavagna,R.O., Campanella,N.C., Mancano,B., Almeida,G.C.,
            Matsushita,M., Almeida Junior,C.R., Saggioro,F., Stavale,J.N.,
            Malheiros,S.M.F., Lima,M., Hajj,G.N.M., Neder,L. and Reis,R.M.
  TITLE     Lack of KBTBD4 Mutations in Molecularly Classified Brazilian
            Medulloblastomas
  JOURNAL   J Neuropathol Exp Neurol 78 (9), 788-790 (2019)
   PUBMED   31403685
  REMARK    GeneRIF: Our findings suggest that KBTBD4 mutations are uncommon in
            Brazilian MBGRP3 and MBGRP4 medulloblastomas subgroups.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104942.5 and KF459542.1.
            
            Transcript Variant: This variant (11) differs in the 5' UTR and
            coding sequence compared to variant 4. The resulting isoform (b) is
            shorter at the N-terminus compared to isoform c. Variants 2, 7, 8,
            10, 11, and 12 all encode the same isoform (b).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.4199022.1,
                                           SRR18074968.2392452.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267751 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..518
                     /product="kelch repeat and BTB domain-containing protein 4
                     isoform b"
                     /note="BTB and kelch domain containing 4; kelch repeat and
                     BTB domain-containing protein 4; BTB and kelch
                     domain-containing protein 4; kelch repeat and BTB (POZ)
                     domain containing 4"
                     /calculated_mol_wt=58013
     Region          13..152
                     /region_name="BTB_POZ_KBTBD4"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch repeat
                     and BTB domain-containing protein 4 (KBTBD4); cd18272"
                     /db_xref="CDD:349581"
     Region          47..479
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          142..229
                     /region_name="BACK_KBTBD4"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch repeat and BTB domain-containing protein 4 (KBTBD4);
                     cd18481"
                     /db_xref="CDD:350556"
     Region          279..314
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          318..365
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          368..414
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          422..467
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     CDS             1..518
                     /gene="KBTBD4"
                     /gene_synonym="BKLHD4; HSPC252"
                     /coded_by="NM_001318724.2:169..1725"
                     /note="isoform b is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS7940.1"
                     /db_xref="GeneID:55709"
                     /db_xref="HGNC:HGNC:23761"
                     /db_xref="MIM:617645"
ORIGIN      
        1 mespeepgas mdenyfvnyt fkdrshsgrv aqgimklcle eelfadvtis vegrefqlhr
       61 lvlsaqscff rsmftsnlke ahnrvivlqd vsesvfqllv dyiyhgtvkl raeelqeiye
      121 vsdmyqltsl feecsrflar tvqvgnclqv mwladrhsdp elytaakhca kthlaqlqnt
      181 eeflhlphrl ltdiisdgvp csqnpteaie awinfnkeer eafaeslrts lkeigenvhi
      241 yligkessrt hslavslhca eddsisvsgq nslchqitaa ckhggdlyvv ggsiprrmwk
      301 cnnatvdwew caplprdrlq htlvsvpgkd aiyslggktl qdtlsnaviy yrvgdnvwte
      361 ttqlevavsg aaganlngii yllggeendl dfftkpsrli qcfdtetdkc hvkpyvlpfa
      421 grmhaavhkd lvfivaegds lvcynpllds ftrlclpeaw ssapslwkia scngsiyvfr
      481 drykkgdant ykldpatsav tvtrgikvll tnlqfvla
//
LOCUS       NP_219363                408 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger protein 764 isoform 1 [Homo sapiens].
ACCESSION   NP_219363
VERSION     NP_219363.2
DBSOURCE    REFSEQ: accession NM_033410.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Helleboid,P.Y., Heusel,M., Duc,J., Piot,C., Thorball,C.W.,
            Coluccio,A., Pontis,J., Imbeault,M., Turelli,P., Aebersold,R. and
            Trono,D.
  TITLE     The interactome of KRAB zinc finger proteins reveals the
            evolutionary history of their functional diversification
  JOURNAL   EMBO J 38 (18), e101220 (2019)
   PUBMED   31403225
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Fadda,A., Syed,N., Mackeh,R., Papadopoulou,A., Suzuki,S.,
            Jithesh,P.V. and Kino,T.
  TITLE     Genome-wide Regulatory Roles of the C2H2-type Zinc Finger Protein
            ZNF764 on the Glucocorticoid Receptor
  JOURNAL   Sci Rep 7, 41598 (2017)
   PUBMED   28139699
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Kino,T., Pavlatou,M.G., Moraitis,A.G., Nemery,R.L., Raygada,M. and
            Stratakis,C.A.
  TITLE     ZNF764 haploinsufficiency may explain partial glucocorticoid,
            androgen, and thyroid hormone resistance associated with 16p11.2
            microdeletion
  JOURNAL   J Clin Endocrinol Metab 97 (8), E1557-E1566 (2012)
   PUBMED   22577170
  REMARK    GeneRIF: effect of ZNF764 on the glucocorticoid receptor
            transcriptional activity was mediated through cooperation with a
            general nuclear hormone receptor coactivator, transcriptional
            intermediary factor 1
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC002310.1, BF725095.1, BC008821.2 and AK093992.1.
            
            On Feb 24, 2010 this sequence version replaced NP_219363.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC008821.2, SRR7346977.1025313.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267770 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..408
                     /product="zinc finger protein 764 isoform 1"
                     /calculated_mol_wt=44812
     Region          26..85
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          91..167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96H86.2)"
     Region          177..197
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          190..212
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          205..225
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          229..>294
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          233..253
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(238,240,242,244..245,248..249,252,266,268,272..273,
                     276..277,280,294,296,298,300..301,304..305,308)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          261..281
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          289..309
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          301..326
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          317..337
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          333..352
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          345..365
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..408
                     /gene="ZNF764"
                     /coded_by="NM_033410.4:193..1419"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10683.1"
                     /db_xref="GeneID:92595"
                     /db_xref="HGNC:HGNC:28200"
                     /db_xref="MIM:619524"
ORIGIN      
        1 mapplaplpp rdpngagpew repgavsfad vavyfcreew gclrpaqral yrdvmretyg
       61 hlsalgiggn kpaliswvee eaelwgpaaq dpevakcqtq tdpadsrnkk kerqregtga
      121 lekpdpvaag spglkspqap sagppygweq lskaphrgrp slcahppvpr adqrhgcyvc
      181 gksfawrstl vehvyshtge kpfhctdcgk gfghasslsk hraihrgerp hrclecgraf
      241 tqrsaltshl rvhtgekpyg cadcgrrfsq ssalyqhrrv hsgetpfpcp dcgrafayps
      301 dlrrhvrtht gekpypcpdc grcfrqssem aahrrthsge kpypcpqcgr rfgqksavak
      361 hqwvhrpgag ghrgrvagrl svtltpghgd ldppvgfqly peifqecg
//
LOCUS       NP_001340223             178 aa            linear   PRI 21-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 2 [Homo sapiens].
ACCESSION   NP_001340223
VERSION     NP_001340223.1
DBSOURCE    REFSEQ: accession NM_001353294.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.498161.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..178
                     /product="CYFIP-related Rac1 interactor B isoform 2"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=20062
     Region          <1..174
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..178
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353294.2:713..1249"
                     /note="isoform 2 is encoded by transcript variant 56"
                     /db_xref="CCDS:CCDS83327.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mtnpaiqndf syyrrtlsrm rinnvpaege nevnnelanr mslfyaeatp mlktlsdatt
       61 kfvsenknlp ienttdclst masvcrvmle tpeyrsrftn eetvsfclrv mvgviilydh
      121 vhpvgafakt skidmkgcik vlkdqppnsv egllnalryt tkhlndetts kqiksmlq
//
LOCUS       NP_001364149            1191 aa            linear   PRI 21-NOV-2025
DEFINITION  plakophilin-4 isoform c [Homo sapiens].
ACCESSION   NP_001364149
VERSION     NP_001364149.1
DBSOURCE    REFSEQ: accession NM_001377220.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1191)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1191)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1191)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1191)
  AUTHORS   Park,S.S., Ponce-Balbuena,D., Kuick,R., Guerrero-Serna,G., Yoon,J.,
            Mellacheruvu,D., Conlon,K.P., Basrur,V., Nesvizhskii,A.I.,
            Jalife,J. and Rual,J.F.
  TITLE     Kir2.1 Interactome Mapping Uncovers PKP4 as a Modulator of the
            Kir2.1-Regulated Inward Rectifier Potassium Currents
  JOURNAL   Mol Cell Proteomics 19 (9), 1436-1449 (2020)
   PUBMED   32541000
  REMARK    GeneRIF: Kir2.1 Interactome Mapping Uncovers PKP4 as a Modulator of
            the Kir2.1-Regulated Inward Rectifier Potassium Currents.
REFERENCE   5  (residues 1 to 1191)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 1191)
  AUTHORS   Stahl,B., Diehlmann,A. and Sudhof,T.C.
  TITLE     Direct interaction of Alzheimer's disease-related presenilin 1 with
            armadillo protein p0071
  JOURNAL   J Biol Chem 274 (14), 9141-9148 (1999)
   PUBMED   10092585
REFERENCE   7  (residues 1 to 1191)
  AUTHORS   Levesque,G., Yu,G., Nishimura,M., Zhang,D.M., Levesque,L., Yu,H.,
            Xu,D., Liang,Y., Rogaeva,E., Ikeda,M., Duthie,M., Murgolo,N.,
            Wang,L., VanderVere,P., Bayne,M.L., Strader,C.D., Rommens,J.M.,
            Fraser,P.E. and St George-Hyslop,P.
  TITLE     Presenilins interact with armadillo proteins including
            neural-specific plakophilin-related protein and beta-catenin
  JOURNAL   J Neurochem 72 (3), 999-1008 (1999)
   PUBMED   10037471
REFERENCE   8  (residues 1 to 1191)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   9  (residues 1 to 1191)
  AUTHORS   Paffenholz,R. and Franke,W.W.
  TITLE     Identification and localization of a neurally expressed member of
            the plakoglobin/armadillo multigene family
  JOURNAL   Differentiation 61 (5), 293-304 (1997)
   PUBMED   9342840
REFERENCE   10 (residues 1 to 1191)
  AUTHORS   Hatzfeld,M. and Nachtsheim,C.
  TITLE     Cloning and characterization of a new armadillo family member,
            p0071, associated with the junctional plaque: evidence for a
            subfamily of closely related proteins
  JOURNAL   J Cell Sci 109 (Pt 11), 2767-2778 (1996)
   PUBMED   8937994
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008070.4 and AC005042.2.
            
            Summary: Armadillo-like proteins are characterized by a series of
            armadillo repeats, first defined in the Drosophila 'armadillo' gene
            product, that are typically 42 to 45 amino acids in length. These
            proteins can be divided into subfamilies based on their number of
            repeats, their overall sequence similarity, and the dispersion of
            the repeats throughout their sequences. Members of the
            p120(ctn)/plakophilin subfamily of Armadillo-like proteins,
            including CTNND1, CTNND2, PKP1, PKP2, PKP4, and ARVCF. PKP4 may be
            a component of desmosomal plaque and other adhesion plaques and is
            thought to be involved in regulating junctional plaque organization
            and cadherin function. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Feb 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1191
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.1"
     Protein         1..1191
                     /product="plakophilin-4 isoform c"
                     /note="catenin 4"
                     /calculated_mol_wt=131639
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          73..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Region          <194..347
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            254
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            270
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Region          290..310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Region          323..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            514
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Region          517..556
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          529..554
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(545,549,553,587,591,595,632,636,640)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          558..597
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          559..598
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          562..598
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          602..643
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          603..643
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          606..641
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          648..699
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          659..701
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          705..750
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          707..748
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          772..809
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            775
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          814..854
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          824..854
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          847..>968
                     /region_name="PLN03200"
                     /note="cellulose synthase-interactive protein;
                     Provisional"
                     /db_xref="CDD:215629"
     Region          861..900
                     /region_name="ARM 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          864..899
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          866..898
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(889,893,897,935,939,943,981,985)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          905..946
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          948..992
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          949..992
                     /region_name="ARM 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          952..987
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            1012
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            1016
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            1044
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Region          1057..1085
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            1090
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            1099
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            1134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     CDS             1..1191
                     /gene="PKP4"
                     /gene_synonym="p0071"
                     /coded_by="NM_001377220.1:1515..5090"
                     /note="isoform c is encoded by transcript variant 8"
                     /db_xref="GeneID:8502"
                     /db_xref="HGNC:HGNC:9026"
                     /db_xref="MIM:604276"
ORIGIN      
        1 mpapeqaslv eegqpqtrqe aastgpgmep ettattilas vkeqelqfqr ltreleverq
       61 ivasqlercr lgaespsias tssteksfpw rstdvpntgv skprvsdavq pnnylirtep
      121 eqgtlyspeq tslhesegsl gnsrsstqmn sysdsgyqea gsfhnsqnvs kadnrqqhsf
      181 igstnnhvvr nsraegqtlv qpsvanramr rvssvpsraq spsyvistgv spsrgslrts
      241 lgsgfgspsv tdprplnpsa yssttlpaar aaspysqrpa sptairrigs vtsrqtsnpn
      301 gptpqyqtta rvgspltltd aqtrvaspsq gqvgssspkr sgmtavpqhl gpslqrtvhd
      361 meqfgqqqyd iyermvpprp dsltglrssy asqhsqlgqd lrsavspdlh itpiyegrty
      421 yspvyrspnh gtvelqgsqt alyrtgsgig nlqrtssqrs tltyqrnnya lnttatyaep
      481 yrpiqyrvqe cnynrlqhav paddgttrsp sidsiqkdpr efawrdpelp evihmlqhqf
      541 psvqanaaay lqhlcfgdnk vkmevcrlgg ikhlvdlldh rvlevqknac galrnlvfgk
      601 stdenkiamk nvggipallr llrksidaev relvtgvlwn lsscdavkmt iirdalstlt
      661 ntvivphsgw nnssfdddhk ikfqtslvlr nttgclrnls sageearkqm rsceglvdsl
      721 lyvihtcvnt sdydsktven cvctlrnlsy rlelevpqar llglnelddl lgkespskds
      781 epscwgkkkk kkkrtpqedq wdgvgpipgl skspkgveml whpsvvkpyl tllaessnpa
      841 tlegsagslq nlsagnwkfa ayiraavrke kglpilvell rmdndrvvss vatalrnmal
      901 dvrnkeligk yamrdlvnrl pggngpsvls detmaaicca lhevtsknme nakaladsgg
      961 ieklvnitkg rgdrsslkvv kaaaqvlntl wqyrdlrsiy kkdgwnqnhf itpvstlerd
     1021 rfkshpslst tnqqmspiiq svgstssspa llgirdprse ydrtqppmqy ynsqgdathk
     1081 glypgsskps piyissyssp areqnrrlqh qqlyysqdds nrknfdayrl ylqsphsyed
     1141 pyfddrvhfp astdystqyg lksttnyvdf ystkrpsyra eqypgspdsw v
//
LOCUS       NP_001362885             766 aa            linear   PRI 21-NOV-2025
DEFINITION  protein zer-1 homolog isoform 1 [Homo sapiens].
ACCESSION   NP_001362885 XP_011516424
VERSION     NP_001362885.1
DBSOURCE    REFSEQ: accession NM_001375956.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Yan,X., Li,Y., Wang,G., Zhou,Z., Song,G., Feng,Q., Zhao,Y., Mi,W.,
            Ma,Z. and Dong,C.
  TITLE     Molecular basis for recognition of Gly/N-degrons by CRL2ZYG11B and
            CRL2ZER1
  JOURNAL   Mol Cell 81 (16), 3262-3274 (2021)
   PUBMED   34214466
  REMARK    GeneRIF: Molecular basis for recognition of Gly/N-degrons by
            CRL2(ZYG11B) and CRL2(ZER1).
REFERENCE   2  (residues 1 to 766)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 766)
  AUTHORS   Timms,R.T., Zhang,Z., Rhee,D.Y., Harper,J.W., Koren,I. and
            Elledge,S.J.
  TITLE     A glycine-specific N-degron pathway mediates the quality control of
            protein N-myristoylation
  JOURNAL   Science 365 (6448) (2019)
   PUBMED   31273098
REFERENCE   4  (residues 1 to 766)
  AUTHORS   Wade,T.D., Gordon,S., Medland,S., Bulik,C.M., Heath,A.C.,
            Montgomery,G.W. and Martin,N.G.
  TITLE     Genetic variants associated with disordered eating
  JOURNAL   Int J Eat Disord 46 (6), 594-608 (2013)
   PUBMED   23568457
REFERENCE   5  (residues 1 to 766)
  AUTHORS   Cheng,C.Y., Schache,M., Ikram,M.K., Young,T.L., Guggenheim,J.A.,
            Vitart,V., MacGregor,S., Verhoeven,V.J., Barathi,V.A., Liao,J.,
            Hysi,P.G., Bailey-Wilson,J.E., St Pourcain,B., Kemp,J.P.,
            McMahon,G., Timpson,N.J., Evans,D.M., Montgomery,G.W., Mishra,A.,
            Wang,Y.X., Wang,J.J., Rochtchina,E., Polasek,O., Wright,A.F.,
            Amin,N., van Leeuwen,E.M., Wilson,J.F., Pennell,C.E., van
            Duijn,C.M., de Jong,P.T., Vingerling,J.R., Zhou,X., Chen,P., Li,R.,
            Tay,W.T., Zheng,Y., Chew,M., Burdon,K.P., Craig,J.E., Iyengar,S.K.,
            Igo,R.P. Jr., Lass,J.H. Jr., Chew,E.Y., Haller,T., Mihailov,E.,
            Metspalu,A., Wedenoja,J., Simpson,C.L., Wojciechowski,R., Hohn,R.,
            Mirshahi,A., Zeller,T., Pfeiffer,N., Lackner,K.J., Bettecken,T.,
            Meitinger,T., Oexle,K., Pirastu,M., Portas,L., Nag,A.,
            Williams,K.M., Yonova-Doing,E., Klein,R., Klein,B.E.,
            Hosseini,S.M., Paterson,A.D., Makela,K.M., Lehtimaki,T.,
            Kahonen,M., Raitakari,O., Yoshimura,N., Matsuda,F., Chen,L.J.,
            Pang,C.P., Yip,S.P., Yap,M.K., Meguro,A., Mizuki,N., Inoko,H.,
            Foster,P.J., Zhao,J.H., Vithana,E., Tai,E.S., Fan,Q., Xu,L.,
            Campbell,H., Fleck,B., Rudan,I., Aung,T., Hofman,A.,
            Uitterlinden,A.G., Bencic,G., Khor,C.C., Forward,H., Parssinen,O.,
            Mitchell,P., Rivadeneira,F., Hewitt,A.W., Williams,C., Oostra,B.A.,
            Teo,Y.Y., Hammond,C.J., Stambolian,D., Mackey,D.A., Klaver,C.C.,
            Wong,T.Y., Saw,S.M. and Baird,P.N.
  CONSRTM   Consortium for Refractive Error and Myopia; Fuchs' Genetics
            Multi-Center Study Group; Wellcome Trust Case Control Consortium 2;
            Diabetes Control and Complications Trial/Epidemiology of Diabetes
            Interventions, and Complications Research Group
  TITLE     Nine loci for ocular axial length identified through genome-wide
            association studies, including shared loci with refractive error
  JOURNAL   Am J Hum Genet 93 (2), 264-277 (2013)
   PUBMED   24144296
REFERENCE   6  (residues 1 to 766)
  AUTHORS   Okumura,F., Matsuzaki,M., Nakatsukasa,K. and Kamura,T.
  TITLE     The Role of Elongin BC-Containing Ubiquitin Ligases
  JOURNAL   Front Oncol 2, 10 (2012)
   PUBMED   22649776
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 766)
  AUTHORS   Vasudevan,S., Starostina,N.G. and Kipreos,E.T.
  TITLE     The Caenorhabditis elegans cell-cycle regulator ZYG-11 defines a
            conserved family of CUL-2 complex components
  JOURNAL   EMBO Rep 8 (3), 279-286 (2007)
   PUBMED   17304241
REFERENCE   8  (residues 1 to 766)
  AUTHORS   Feral,C., Wu,Y.Q., Pawlak,A. and Guellaen,G.
  TITLE     Meiotic human sperm cells express a leucine-rich homologue of
            Caenorhabditis elegans early embryogenesis gene, Zyg-11
  JOURNAL   Mol Hum Reprod 7 (12), 1115-1122 (2001)
   PUBMED   11719588
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL441992.17.
            
            On Nov 7, 2019 this sequence version replaced XP_011516424.1.
            
            Summary: This gene encodes a subunit of an E3 ubiquitin ligase
            complex that may be involved in meiosis. The encoded protein
            contains three leucine-rich repeat motifs. [provided by RefSeq, Nov
            2012].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853560.29052.1,
                                           SRR11853567.30990.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..766
                     /product="protein zer-1 homolog isoform 1"
                     /note="ZYG homolog; protein zer-1 homolog; zyg-11 homolog
                     B-like protein; zyg11b-like protein"
                     /calculated_mol_wt=88039
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          82..104
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          105..130
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          131..176
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          177..200
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          201..223
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          224..247
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          226..245
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          246..268
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          278..302
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          281..324
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          427..467
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          511..556
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Site            order(545,549,553,589,593,597,630,636,640)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          558..600
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          562..600
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          602..643
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          605..641
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          714..756
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     CDS             1..766
                     /gene="ZER1"
                     /gene_synonym="C9orf60; ZYG; ZYG11BL"
                     /coded_by="NM_001375956.1:230..2530"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS6910.1"
                     /db_xref="GeneID:10444"
                     /db_xref="HGNC:HGNC:30960"
                     /db_xref="MIM:617764"
ORIGIN      
        1 masdtpeslm alctdfclrn ldgtlgylld ketlrlhpdi flpseicdrl vneyvelvna
       61 acnfephesf fslfsdprst rltrihlred lvqdqdleai rkqdlvelyl tnceklsaks
      121 lqtlrsfsht lvslslfgct nifyeeenpg gcedeylvnp tcqvlvkdft fegfsrlrfl
      181 nlgrmidwvp vesllrplns laaldlsgiq tsdaafltqw kdslvslvly nmdlsddhir
      241 vivqlhklrh ldisrdrlss yykfkltrev lslfvqklgn lmsldisghm ilencsiskm
      301 eeeagqtsie pskssiipfr alkrplqflg lfenslcrlt hipaykvsgd kneeqvlnai
      361 eaytehrpei tsrainllfd iariercnql lralklvita lkchkydrni qvtgsaalfy
      421 ltnseyrseq svklrrqviq vvlngmesyq evtvqrnccl tlcnfsipee lefqyrrvne
      481 lllsilnptr qdesiqriav hlcnalvcqv dndhkeavgk mgfvvtmlkl iqkklldktc
      541 dqvmefswsa lwnitdetpd ncemflnfng mklfldclke fpekqelhrn mlgllgnvae
      601 vkelrpqlmt sqfisvfsnl leskadgiev synacgvlsh imfdgpeawg vcepqreeve
      661 ermwaaiqsw dinsrrniny rsfepilrll pqgispvsqh watwalynlv svypdkycpl
      721 likeggmpll rdiikmatar qetkemarkv iehcsnfkee nmdtsr
//
LOCUS       NP_001365426             225 aa            linear   PRI 21-NOV-2025
DEFINITION  beta-1,4-galactosyltransferase 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001365426
VERSION     NP_001365426.1
DBSOURCE    REFSEQ: accession NM_001378497.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Zhao,Y., Nayak,S., Raidas,S., Guo,L., Della Gatta,G., Koppolu,S.,
            Halasz,G., Montasser,M.E., Shuldiner,A.R., Mao,Y. and Li,N.
  TITLE     In-Depth Mass Spectrometry Analysis Reveals the Plasma Proteomic
            and N-Glycoproteomic Impact of an Amish-Enriched Cardioprotective
            Variant in B4GALT1
  JOURNAL   Mol Cell Proteomics 22 (8), 100595 (2023)
   PUBMED   37328064
  REMARK    GeneRIF: In-Depth Mass Spectrometry Analysis Reveals the Plasma
            Proteomic and N-Glycoproteomic Impact of an Amish-Enriched
            Cardioprotective Variant in B4GALT1.
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Cui,Y., Li,J., Zhang,P., Yin,D., Wang,Z., Dai,J., Wang,W., Zhang,E.
            and Guo,R.
  TITLE     B4GALT1 promotes immune escape by regulating the expression of
            PD-L1 at multiple levels in lung adenocarcinoma
  JOURNAL   J Exp Clin Cancer Res 42 (1), 146 (2023)
   PUBMED   37303063
  REMARK    GeneRIF: B4GALT1 promotes immune escape by regulating the
            expression of PD-L1 at multiple levels in lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Ghasemi,H., Seghatoleslam,A., Fahmideh Kar,M.A., Mahbudi,L.,
            Fard,B.G. and Jamshidi,M.
  TITLE     Analysis of the Interaction of UBE2Q1 with B4GALT1 and P53:
            Experimental and Molecular Modeling Study
  JOURNAL   Protein Pept Lett 30 (8), 668-678 (2023)
   PUBMED   37198983
  REMARK    GeneRIF: Analysis of the Interaction of UBE2Q1 with B4GALT1 and
            P53: Experimental and Molecular Modeling Study.
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Montasser,M.E., Van Hout,C.V., Miloscio,L., Howard,A.D.,
            Rosenberg,A., Callaway,M., Shen,B., Li,N., Locke,A.E., Verweij,N.,
            De,T., Ferreira,M.A., Lotta,L.A., Baras,A., Daly,T.J.,
            Hartford,S.A., Lin,W., Mao,Y., Ye,B., White,D., Gong,G.,
            Perry,J.A., Ryan,K.A., Fang,Q., Tzoneva,G., Pefanis,E., Hunt,C.,
            Tang,Y., Lee,L., Sztalryd-Woodle,C., Mitchell,B.D., Healy,M.,
            Streeten,E.A., Taylor,S.I., O'Connell,J.R., Economides,A.N., Della
            Gatta,G. and Shuldiner,A.R.
  CONSRTM   Regeneron Genetics Center Collaborationdouble dagger
  TITLE     Genetic and functional evidence links a missense variant in B4GALT1
            to lower LDL and fibrinogen
  JOURNAL   Science 374 (6572), 1221-1227 (2021)
   PUBMED   34855475
  REMARK    GeneRIF: Genetic and functional evidence links a missense variant
            in B4GALT1 to lower LDL and fibrinogen.
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Hathaway,H.J., Evans,S.C., Dubois,D.H., Foote,C.I., Elder,B.H. and
            Shur,B.D.
  TITLE     Mutational analysis of the cytoplasmic domain of
            beta1,4-galactosyltransferase I: influence of phosphorylation on
            cell surface expression
  JOURNAL   J Cell Sci 116 (Pt 21), 4319-4330 (2003)
   PUBMED   12966167
REFERENCE   6  (residues 1 to 225)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Uejima,T., Uemura,M., Nozawa,S. and Narimatsu,H.
  TITLE     Complementary DNA cloning for galactosyltransferase associated with
            tumor and determination of antigenic epitopes recognized by
            specific monoclonal antibodies
  JOURNAL   Cancer Res 52 (22), 6158-6163 (1992)
   PUBMED   1384956
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Lopez,L.C., Youakim,A., Evans,S.C. and Shur,B.D.
  TITLE     Evidence for a molecular distinction between Golgi and cell surface
            forms of beta 1,4-galactosyltransferase
  JOURNAL   J Biol Chem 266 (24), 15984-15991 (1991)
   PUBMED   1714903
REFERENCE   9  (residues 1 to 225)
  AUTHORS   Gerber,A.C., Kozdrowski,I., Wyss,S.R. and Berger,E.G.
  TITLE     The charge heterogeneity of soluble human galactosyltransferases
            isolated from milk, amniotic fluid and malignant ascites
  JOURNAL   Eur J Biochem 93 (3), 453-460 (1979)
   PUBMED   33805
REFERENCE   10 (residues 1 to 225)
  AUTHORS   Brew,K. and Hill,R.L.
  TITLE     Lactose biosynthesis
  JOURNAL   Rev Physiol Biochem Pharmacol 72, 105-158 (1975)
   PUBMED   806951
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL161445.10.
            
            Summary: This gene is one of seven beta-1,4-galactosyltransferase
            (beta4GalT) genes. They encode type II membrane-bound glycoproteins
            that appear to have exclusive specificity for the donor substrate
            UDP-galactose; all transfer galactose in a beta1,4 linkage to
            similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a
            distinct function in the biosynthesis of different glycoconjugates
            and saccharide structures. As type II membrane proteins, they have
            an N-terminal hydrophobic signal sequence that directs the protein
            to the Golgi apparatus and which then remains uncleaved to function
            as a transmembrane anchor. By sequence similarity, the beta4GalTs
            form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and
            beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. This gene is
            unique among the beta4GalT genes because it encodes an enzyme that
            participates both in glycoconjugate and lactose biosynthesis. For
            the first activity, the enzyme adds galactose to
            N-acetylglucosamine residues that are either monosaccharides or the
            nonreducing ends of glycoprotein carbohydrate chains. The second
            activity is restricted to lactating mammary tissues where the
            enzyme forms a heterodimer with alpha-lactalbumin to catalyze
            UDP-galactose + D-glucose <=> UDP + lactose. The two enzymatic
            forms result from alternate transcription initiation sites and
            post-translational processing. Two transcripts, which differ only
            at the 5' end, with approximate lengths of 4.1 kb and 3.9 kb encode
            the same protein. The longer transcript encodes the type II
            membrane-bound, trans-Golgi resident protein involved in
            glycoconjugate biosynthesis. The shorter transcript encodes a
            protein which is cleaved to form the soluble lactose synthase.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC045773.1, SRR18074968.2502997.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968832,
                                           SAMEA2467144 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..225
                     /product="beta-1,4-galactosyltransferase 1 isoform 4"
                     /EC_number="2.4.1.22"
                     /EC_number="2.4.1.90"
                     /EC_number="2.4.1.38"
                     /EC_number="2.4.1.275"
                     /note="glycoprotein-4-beta-galactosyltransferase 2;
                     beta-1,4-GalTase 1; UDP-Gal:betaGlcNAc beta 1,4-
                     galactosyltransferase, polypeptide 1; UDP-Gal:beta-GlcNAc
                     beta-1,4-galactosyltransferase 1;
                     UDP-galactose:beta-N-acetylglucosamine
                     beta-1,4-galactosyltransferase 1; nal synthase; lactose
                     synthase A protein; N-acetyllactosamine synthase;
                     beta-N-acetylglucosaminyl-glycolipid
                     beta-1,4-galactosyltransferase;
                     beta-N-acetylglucosaminylglycopeptide
                     beta-1,4-galactosyltransferase; neolactotriaosylceramide
                     beta-1,4-galactosyltransferase"
                     /calculated_mol_wt=24155
     Site            25..44
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P15291.5)"
     Region          61..117
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15291.5)"
     Site            77..78
                     /site_type="cleavage"
                     /note="Cleavage, to produce soluble form; propagated from
                     UniProtKB/Swiss-Prot (P15291.5)"
     Site            113
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15291.5)"
     Region          138..>216
                     /region_name="Glyco_transf_7N"
                     /note="N-terminal region of glycosyl transferase group 7;
                     pfam13733"
                     /db_xref="CDD:463972"
     CDS             1..225
                     /gene="B4GALT1"
                     /gene_synonym="B4GAL-T1; beta4Gal-T1; CDG2D; CLDLFIB;
                     GGTB2; GT1; GTB"
                     /coded_by="NM_001378497.1:168..845"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS94396.1"
                     /db_xref="GeneID:2683"
                     /db_xref="HGNC:HGNC:924"
                     /db_xref="MIM:137060"
ORIGIN      
        1 mrlrepllsg saampgaslq racrllvavc alhlgvtlvy ylagrdlsrl pqlvgvstpl
       61 qggsnsaaai gqssgelrtg garpppplga ssqprpggds spvvdsgpgp asnltsvpvp
      121 httalslpac peespllvgp mliefnmpvd lelvakqnpn vkmggryapr dcvsphkvai
      181 iipfrnrqeh lkywlyylhp vlqrqqldyg iyvinqyeki rrllw
//
LOCUS       NP_001381575             779 aa            linear   PRI 21-NOV-2025
DEFINITION  coiled-coil alpha-helical rod protein 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001381575
VERSION     NP_001381575.1
DBSOURCE    REFSEQ: accession NM_001394646.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 779)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 779)
  AUTHORS   Xu,X., Qiu,L., Zhang,M. and Wu,G.
  TITLE     Segregation of nascent GPCRs in the ER-to-Golgi transport by CCHCR1
            via direct interaction
  JOURNAL   J Cell Sci 137 (3) (2024)
   PUBMED   38230433
  REMARK    GeneRIF: Segregation of nascent GPCRs in the ER-to-Golgi transport
            by CCHCR1 via direct interaction.
REFERENCE   3  (residues 1 to 779)
  CONSRTM   COVID-19 Host Genetics Initiative
  TITLE     A first update on mapping the human genetic architecture of
            COVID-19
  JOURNAL   Nature 608 (7921), E1-E10 (2022)
   PUBMED   35922517
REFERENCE   4  (residues 1 to 779)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 779)
  AUTHORS   Pisani,C., Onori,A., Gabanella,F., Di Certo,M.G., Passananti,C. and
            Corbi,N.
  TITLE     Identification of protein/mRNA network involving the PSORS1 locus
            gene CCHCR1 and the PSORS4 locus gene HAX1
  JOURNAL   Exp Cell Res 399 (2), 112471 (2021)
   PUBMED   33417922
  REMARK    GeneRIF: Identification of protein/mRNA network involving the
            PSORS1 locus gene CCHCR1 and the PSORS4 locus gene HAX1.
REFERENCE   6  (residues 1 to 779)
  AUTHORS   Xu,Y.C., Wu,R.F., Gu,Y., Yang,Y.S., Yang,M.C., Nwariaku,F.E. and
            Terada,L.S.
  TITLE     Involvement of TRAF4 in oxidative activation of c-Jun N-terminal
            kinase
  JOURNAL   J Biol Chem 277 (31), 28051-28057 (2002)
   PUBMED   12023963
REFERENCE   7  (residues 1 to 779)
  AUTHORS   Asumalahti,K., Veal,C., Laitinen,T., Suomela,S., Allen,M.,
            Elomaa,O., Moser,M., de Cid,R., Ripatti,S., Vorechovsky,I.,
            Marcusson,J.A., Nakagawa,H., Lazaro,C., Estivill,X., Capon,F.,
            Novelli,G., Saarialho-Kere,U., Barker,J., Trembath,R. and Kere,J.
  CONSRTM   Psoriasis Consortium
  TITLE     Coding haplotype analysis supports HCR as the putative
            susceptibility gene for psoriasis at the MHC PSORS1 locus
  JOURNAL   Hum Mol Genet 11 (5), 589-597 (2002)
   PUBMED   11875053
REFERENCE   8  (residues 1 to 779)
  AUTHORS   O'Brien,K.P., Holm,S.J., Nilsson,S., Carlen,L., Rosenmuller,T.,
            Enerback,C., Inerot,A. and Stahle-Backdahl,M.
  TITLE     The HCR gene on 6p21 is unlikely to be a psoriasis susceptibility
            gene
  JOURNAL   J Invest Dermatol 116 (5), 750-754 (2001)
   PUBMED   11348465
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 779)
  AUTHORS   Asumalahti,K., Laitinen,T., Itkonen-Vatjus,R., Lokki,M.L.,
            Suomela,S., Snellman,E., Saarialho-Kere,U. and Kere,J.
  TITLE     A candidate gene for psoriasis near HLA-C, HCR (Pg8), is highly
            polymorphic with a disease-associated susceptibility allele
  JOURNAL   Hum Mol Genet 9 (10), 1533-1542 (2000)
   PUBMED   10888604
  REMARK    Erratum:[Hum Mol Genet 2001 Feb 1;10(3):301]
REFERENCE   10 (residues 1 to 779)
  AUTHORS   Oka,A., Tamiya,G., Tomizawa,M., Ota,M., Katsuyama,Y., Makino,S.,
            Shiina,T., Yoshitome,M., Iizuka,M., Sasao,Y., Iwashita,K.,
            Kawakubo,Y., Sugai,J., Ozawa,A., Ohkido,M., Kimura,M., Bahram,S.
            and Inoko,H.
  TITLE     Association analysis using refined microsatellite markers localizes
            a susceptibility locus for psoriasis vulgaris within a 111 kb
            segment telomeric to the HLA-C gene
  JOURNAL   Hum Mol Genet 8 (12), 2165-2170 (1999)
   PUBMED   10545595
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL662844.12.
            
            Summary: This gene encodes a protein with five coiled-coil
            alpha-helical rod domains that is thought to act as a regulator of
            mRNA metabolism through its interaction with mRNA-decapping protein
            4. It localizes to P-bodies, the site of mRNA metabolism, with an
            N-terminus that is required for this subcellular localization,
            suggesting it is a P-body component. Naturally occurring mutations
            in this gene are associated with psoriasis. [provided by RefSeq,
            May 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..779
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..779
                     /product="coiled-coil alpha-helical rod protein 1 isoform
                     5"
                     /note="HCR (a-helix coiled-coil rod homologue);
                     StAR-binding protein; putative gene 8 protein;
                     alpha-helical coiled-coil rod protein"
                     /calculated_mol_wt=88242
     Region          27..770
                     /region_name="HCR"
                     /note="Alpha helical coiled-coil rod protein (HCR);
                     pfam07111"
                     /db_xref="CDD:284517"
     Region          62..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TD31.2)"
     Region          177..218
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TD31.2)"
     CDS             1..779
                     /gene="CCHCR1"
                     /gene_synonym="C6orf18; HCR; pg8; SBP"
                     /coded_by="NM_001394646.1:199..2538"
                     /note="isoform 5 is encoded by transcript variant 8"
                     /db_xref="GeneID:54535"
                     /db_xref="HGNC:HGNC:13930"
                     /db_xref="MIM:605310"
ORIGIN      
        1 mfppsgstgl ippshfqarp lstlprmapt wlsdiplvqp pghqdvserr ldtqrpqvtm
       61 werdvssdrq epgrrgrswg legsqalsqq aevivrqlqe lrrleeevrl lretslqqkm
      121 rleaqamele alaraekagr aeaeglraal agaevvrknl eegsqrelee vqrlhqeqls
      181 sltqaheeal ssltskaegl ekslssletr rageakelae aqreaellrk qlsktqedle
      241 aqvtlvenlr kyvgeqvpse vhsqtweler qklletmqhl qedrdslhat aellqvrvqs
      301 lthilalqee eltrkvqpsd slepeftrkc qsllnrwrek vfalmvqlka qelehsdsvk
      361 qlkgqvaslq ekvtsqsqeq ailqrslqdk aaevevermg aklelsraqe arrrwqqqta
      421 saeeqlrlvv navsssqiwl ettmakvega aaqlpslnnr lsyavrkvht irgliarkla
      481 laqlrqescp lpppvtdvsl elqqlreern rldaelqlsa rliqqevgra reqgeaerqq
      541 lskvaqqleq elqqtqesla slglqlevar qgqqesteea aslrqeltqq qelygqalqe
      601 kvaevetrlr eqlsdterrl nearrehaka vvslrqiqrr aaqekersqe lrrlqeeark
      661 eegqrlarrl qelerdknlm latlqqegll srykqqrllt vlpslldkkk svvssprppe
      721 csasapvaaa vptresikgs lsvllddlqd lseaiskeea vcqgdnldrc sssnpqmss
//
LOCUS       NP_001363231             455 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase PAK 1 isoform 11 [Homo sapiens].
ACCESSION   NP_001363231
VERSION     NP_001363231.1
DBSOURCE    REFSEQ: accession NM_001376302.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Kervarrec,T., Westphal,D., Pissaloux,D., Legrand,M., Tirode,F.,
            Neuhart,A., Drouot,F., Becker,J.C., Macagno,N., Seris,A.,
            Jouary,T., Beltzung,F., Jullie,M.L., Harms,P.W., Cribier,B.,
            Mourah,S., Jouenne,F., Fromont,G., Louveau,B., Mancini,M.,
            Kazakov,D.V., de la Fouchardiere,A. and Battistella,M.
  TITLE     Porocarcinomas with PAK1/2/3 fusions: a series of 12 cases
  JOURNAL   Histopathology 85 (4), 566-578 (2024)
   PUBMED   38785043
  REMARK    GeneRIF: Porocarcinomas with PAK1/2/3 fusions: a series of 12
            cases.
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Zhao,P., Zhang,J., Song,W., Qi,D., Huang,Y., Su,Y., Wu,R., Zhang,L.
            and Zhang,S.
  TITLE     Incarvine C and its analogues inhibit the formation of cell
            cytoskeleton by targeting Rac1
  JOURNAL   Bioorg Chem 149, 107512 (2024)
   PUBMED   38833990
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Xu,M.H., Zheng,Y.M., Liang,B.G., Xu,W.X., Cao,J., Wang,P.,
            Dong,Z.Y., Zhou,C.H., Sun,H.C., Ren,N., Ke,A.W. and Shen,Y.H.
  TITLE     Deubiquitination of CIB1 by USP14 promotes lenvatinib resistance
            via the PAK1-ERK1/2 axis in hepatocellular carcinoma
  JOURNAL   Int J Biol Sci 20 (9), 3269-3284 (2024)
   PUBMED   38993552
  REMARK    GeneRIF: Deubiquitination of CIB1 by USP14 promotes lenvatinib
            resistance via the PAK1-ERK1/2 axis in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 455)
  AUTHORS   Luo,Q., Raulston,E.G., Prado,M.A., Wu,X., Gritsman,K., Whalen,K.S.,
            Yan,K., Booth,C.A.G., Xu,R., van Galen,P., Doench,J.G., Shimony,S.,
            Long,H.W., Neuberg,D.S., Paulo,J.A. and Lane,A.A.
  TITLE     Targetable leukaemia dependency on noncanonical PI3Kgamma
            signalling
  JOURNAL   Nature 630 (8015), 198-205 (2024)
   PUBMED   38720074
  REMARK    GeneRIF: Targetable leukaemia dependency on noncanonical PI3Kgamma
            signalling.
REFERENCE   6  (residues 1 to 455)
  AUTHORS   Manser,E., Huang,H.Y., Loo,T.H., Chen,X.Q., Dong,J.M., Leung,T. and
            Lim,L.
  TITLE     Expression of constitutively active alpha-PAK reveals effects of
            the kinase on actin and focal complexes
  JOURNAL   Mol Cell Biol 17 (3), 1129-1143 (1997)
   PUBMED   9032240
REFERENCE   7  (residues 1 to 455)
  AUTHORS   Bokoch,G.M., Wang,Y., Bohl,B.P., Sells,M.A., Quilliam,L.A. and
            Knaus,U.G.
  TITLE     Interaction of the Nck adapter protein with p21-activated kinase
            (PAK1)
  JOURNAL   J Biol Chem 271 (42), 25746-25749 (1996)
   PUBMED   8824201
REFERENCE   8  (residues 1 to 455)
  AUTHORS   Brown,J.L., Stowers,L., Baer,M., Trejo,J., Coughlin,S. and Chant,J.
  TITLE     Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase
            pathway
  JOURNAL   Curr Biol 6 (5), 598-605 (1996)
   PUBMED   8805275
REFERENCE   9  (residues 1 to 455)
  AUTHORS   Martin,G.A., Bollag,G., McCormick,F. and Abo,A.
  TITLE     A novel serine kinase activated by rac1/CDC42Hs-dependent
            autophosphorylation is related to PAK65 and STE20
  JOURNAL   EMBO J 14 (9), 1970-1978 (1995)
   PUBMED   7744004
  REMARK    Erratum:[EMBO J. 1995 Sep 1;14(17):4385. doi:
            10.1002/j.1460-2075.1995.tb00113.x. PMID: 7556080]
REFERENCE   10 (residues 1 to 455)
  AUTHORS   Manser,E., Leung,T., Salihuddin,H., Zhao,Z.S. and Lim,L.
  TITLE     A brain serine/threonine protein kinase activated by Cdc42 and Rac1
  JOURNAL   Nature 367 (6458), 40-46 (1994)
   PUBMED   8107774
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000486.6.
            
            Summary: This gene encodes a family member of serine/threonine
            p21-activating kinases, known as PAK proteins. These proteins are
            critical effectors that link RhoGTPases to cytoskeleton
            reorganization and nuclear signaling, and they serve as targets for
            the small GTP binding proteins Cdc42 and Rac. This specific family
            member regulates cell motility and morphology. Mutations in this
            gene have been associated with macrocephaly, seizures, and speech
            delay. Overexpression of this gene is also reported in many cancer
            types, and particularly in breast cancer. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296006.1, SRR14038193.2067304.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.5-q14.1"
     Protein         1..455
                     /product="serine/threonine-protein kinase PAK 1 isoform
                     11"
                     /EC_number="2.7.11.1"
                     /note="p21/Cdc42/Rac1-activated kinase 1 (yeast
                     Ste20-related); p21/Cdc42/Rac1-activated kinase 1 (STE20
                     homolog, yeast); serine/threonine-protein kinase PAK 1;
                     p21 protein (Cdc42/Rac)-activated kinase 1"
                     /calculated_mol_wt=50746
     Region          164..419
                     /region_name="STKc_PAK_I"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Group I p21-activated kinase; cd06647"
                     /db_xref="CDD:270814"
     Site            order(178..182,186,199,201,230,246..250,252..253,256,291,
                     293..296,298,308..309,312,325..329,331,358,367..369)
                     /site_type="active"
                     /db_xref="CDD:270814"
     Site            order(178..182,186,199,201,230,246..250,252..253,256,
                     295..296,298,308..309)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270814"
     Site            order(181..182,291,293..295,312,325..329,331,358,367..369)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270814"
     Site            order(183,217,286,288..291,309..310,337..338,340,345,370,
                     373,376)
                     /site_type="other"
                     /note="AID interaction site [polypeptide binding]"
                     /db_xref="CDD:270814"
     Site            308..331
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270814"
     CDS             1..455
                     /gene="PAK1"
                     /gene_synonym="alpha-PAK; IDDMSSD; p65-PAK; PAKalpha"
                     /coded_by="NM_001376302.1:303..1670"
                     /note="isoform 11 is encoded by transcript variant 32"
                     /db_xref="CCDS:CCDS91544.1"
                     /db_xref="GeneID:5058"
                     /db_xref="HGNC:HGNC:8590"
                     /db_xref="MIM:602590"
ORIGIN      
        1 mpeqwarllq tsnitkseqk knpqavldvl efynskktsn sqkymsftdk saedynssna
       61 lnvkavsetp avppvseded dddddatppp viaprpehtk svytrsviep lpvtptrdva
      121 tspisptenn ttppdaltrn tekqkkkpkm sdeeileklr sivsvgdpkk kytrfekigq
      181 gasgtvytam dvatgqevai kqmnlqqqpk keliineilv mrenknpniv nyldsylvgd
      241 elwvvmeyla ggsltdvvte tcmdegqiaa vcreclqale flhsnqvihr diksdnillg
      301 mdgsvkltdf gfcaqitpeq skrstmvgtp ywmapevvtr kaygpkvdiw slgimaiemi
      361 egeppylnen plralyliat ngtpelqnpe klsaifrdfl nrclemdvek rgsakellqv
      421 rklrfqvfsn fsmiaasipe dcqaplqphs tdccs
//
LOCUS       NP_001371686            1019 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 104 [Homo sapiens].
ACCESSION   NP_001371686
VERSION     NP_001371686.1
DBSOURCE    REFSEQ: accession NM_001384757.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1019)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1019)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1019)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1019)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1019)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1019)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1019)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2423521.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1019
                     /product="microtubule-associated protein 4 isoform 104"
                     /note="MAP-4"
                     /calculated_mol_wt=107337
     Region          <511..855
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <867..888
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          890..919
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          921..951
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1019
                     /gene="MAP4"
                     /coded_by="NM_001384757.1:96..3155"
                     /note="isoform 104 is encoded by transcript variant 30"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiegsptef leekmayqey pnsqnwpedt nfcfqpeqvv dpiqtdpfkm
      121 yhdddladlv fpssatadts ifagqndplk dsyvplelak eiemaseerp paqaleimmg
      181 lkttdmapsk etemalakdm alatkteval akdmesptkl dvtlakdmqp smesdmalvk
      241 dmelptekev alvkdvrwpt etdvssaknv vlptetevap akdvtllket eraspikmdl
      301 apskdmgppk enkketeras pikmdlapsk dmgppkenki vpakdlvlls eievaqandi
      361 issteissae kvalssetev alardmtlpp etnviltkdk alpleaevap vkdmaqlpet
      421 eiapakdvap stvkevgllk dmsplsetem algkdvtppp etevvliknv clppemeval
      481 tedqvpalkt eaplakdgvl tlannvtpak dvpplsetea tpvpikdmei aqtqkgised
      541 shleslqdvg qsaaptfmis petvtgtgkk cslpaeedsv leklgerkpc nsqpselsse
      601 tsgiarpeeg rpvvsgtgnd ittppnkelp pspekktkpl attqpaktst skaktqptsl
      661 pkqpapttig glnkkpmsla sglvpaappk rpavasarps ilpskdvkpk piadakapek
      721 raspskpasa pasrsgskst qtvaktttaa avastgpssr spstllpkkp taiktegkpa
      781 evkkmtaksv padlsrpkst stssmkkttt lsgtapaagv vpsrvkatpm psrpsttpfi
      841 dkkptsakps sttprlsrla tntsapdlkn vrskvgsten ikhqpgggrv qiqnkkvdis
      901 kvsskcgska nikhkpgggd vkiesqklnf kekaqakvgs ldnvghlpag gavktegggs
      961 eaplcpgppa geepaiseaa peagaptsas glnghptlsg ggdqreaqtl dsqiqetsi
//
LOCUS       NP_001316                577 aa            linear   PRI 21-NOV-2025
DEFINITION  cleavage stimulation factor subunit 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001316
VERSION     NP_001316.1
DBSOURCE    REFSEQ: accession NM_001325.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Zheng,Y., Li,X., Deng,S., Zhao,H., Ye,Y., Zhang,S., Huang,X.,
            Bai,R., Zhuang,L., Zhou,Q., Li,M., Su,J., Li,R., Bao,X., Zeng,L.,
            Chen,R., Zheng,J., Lin,D., He,C., Zhang,J. and Zuo,Z.
  TITLE     CSTF2 mediated mRNA N6-methyladenosine modification drives
            pancreatic ductal adenocarcinoma m6A subtypes
  JOURNAL   Nat Commun 14 (1), 6334 (2023)
   PUBMED   37816727
  REMARK    GeneRIF: CSTF2 mediated mRNA N[6]-methyladenosine modification
            drives pancreatic ductal adenocarcinoma m[6]A subtypes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Tan,Y., Zheng,T., Zhang,R., Chen,S., Cheng,Q., Zhang,J., Wang,R.,
            Chen,M. and Na,N.
  TITLE     Alternative polyadenylation writer CSTF2 forms a positive loop with
            FGF2 to promote tubular epithelial-mesenchymal transition and renal
            fibrosis
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1868 (12), 166541 (2022)
   PUBMED   36113752
  REMARK    GeneRIF: Alternative polyadenylation writer CSTF2 forms a positive
            loop with FGF2 to promote tubular epithelial-mesenchymal transition
            and renal fibrosis.
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Zhang,M.H. and Liu,J.
  TITLE     Cleavage stimulation factor 2 promotes malignant progression of
            liver hepatocellular carcinoma by activating phosphatidylinositol
            3'-kinase/protein kinase B/mammalian target of rapamycin pathway
  JOURNAL   Bioengineered 13 (4), 10047-10060 (2022)
   PUBMED   35412944
  REMARK    GeneRIF: Cleavage stimulation factor 2 promotes malignant
            progression of liver hepatocellular carcinoma by activating
            phosphatidylinositol 3'-kinase/protein kinase B/mammalian target of
            rapamycin pathway.
REFERENCE   4  (residues 1 to 577)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   5  (residues 1 to 577)
  AUTHORS   Lin,A., Ji,P., Niu,X., Zhao,X., Chen,Y., Liu,W., Liu,Y., Fan,W.,
            Sun,Y., Miao,C., Zhang,S., Tan,W., Lin,D., Wagner,E.J. and Wu,C.
  TITLE     CstF64-Induced Shortening of the BID 3'UTR Promotes Esophageal
            Squamous Cell Carcinoma Progression by Disrupting ceRNA Cross-talk
            with ZFP36L2
  JOURNAL   Cancer Res 81 (22), 5638-5651 (2021)
   PUBMED   34607841
  REMARK    GeneRIF: CstF64-Induced Shortening of the BID 3'UTR Promotes
            Esophageal Squamous Cell Carcinoma Progression by Disrupting ceRNA
            Cross-talk with ZFP36L2.
REFERENCE   6  (residues 1 to 577)
  AUTHORS   Ruegsegger,U., Beyer,K. and Keller,W.
  TITLE     Purification and characterization of human cleavage factor Im
            involved in the 3' end processing of messenger RNA precursors
  JOURNAL   J Biol Chem 271 (11), 6107-6113 (1996)
   PUBMED   8626397
REFERENCE   7  (residues 1 to 577)
  AUTHORS   Murthy,K.G. and Manley,J.L.
  TITLE     The 160-kD subunit of human cleavage-polyadenylation specificity
            factor coordinates pre-mRNA 3'-end formation
  JOURNAL   Genes Dev 9 (21), 2672-2683 (1995)
   PUBMED   7590244
REFERENCE   8  (residues 1 to 577)
  AUTHORS   Takagaki,Y. and Manley,J.L.
  TITLE     A polyadenylation factor subunit is the human homologue of the
            Drosophila suppressor of forked protein
  JOURNAL   Nature 372 (6505), 471-474 (1994)
   PUBMED   7984242
REFERENCE   9  (residues 1 to 577)
  AUTHORS   Takagaki,Y. and Manley,J.L.
  TITLE     A human polyadenylation factor is a G protein beta-subunit
            homologue
  JOURNAL   J Biol Chem 267 (33), 23471-23474 (1992)
   PUBMED   1358884
REFERENCE   10 (residues 1 to 577)
  AUTHORS   Takagaki,Y., MacDonald,C.C., Shenk,T. and Manley,J.L.
  TITLE     The human 64-kDa polyadenylylation factor contains a
            ribonucleoprotein-type RNA binding domain and unusual auxiliary
            motifs
  JOURNAL   Proc Natl Acad Sci U S A 89 (4), 1403-1407 (1992)
   PUBMED   1741396
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z95327.1, Z83819.1, M85085.1
            and AW016125.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a nuclear protein with an RRM (RNA
            recognition motif) domain. The protein is a member of the cleavage
            stimulation factor (CSTF) complex that is involved in the 3' end
            cleavage and polyadenylation of pre-mRNAs. Specifically, this
            protein binds GU-rich elements within the 3'-untranslated region of
            mRNAs. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the central coding region, compared to variant 1. The
            encoded isoform (2) is shorter, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M85085.1, BC017712.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372972.7/ ENSP00000362063.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..577
                     /product="cleavage stimulation factor subunit 2 isoform 2"
                     /note="CF-1 64 kDa subunit; CSTF 64 kDa subunit; cleavage
                     stimulation factor 64 kDa subunit; cleavage stimulation
                     factor, 3' pre-RNA, subunit 2, 64kD; cleavage stimulation
                     factor, 3' pre-RNA, subunit 2, 64kDa"
                     /calculated_mol_wt=60829
     Region          10..94
                     /region_name="RRM_CSTF2_CSTF2T"
                     /note="RNA recognition motif (RRM) found in cleavage
                     stimulation factor subunit 2 (CSTF2), cleavage stimulation
                     factor subunit 2 tau variant (CSTF2T) and similar
                     proteins; cd12671"
                     /db_xref="CDD:410072"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P33240.1)"
     Site            order(19,46..50,59..61,85,88..90)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:410072"
     Region          108..248
                     /region_name="Interactions with CSTF3 and SYMPK"
                     /note="propagated from UniProtKB/Swiss-Prot (P33240.1)"
     Region          112..191
                     /region_name="CSTF2_hinge"
                     /note="Hinge domain of cleavage stimulation factor subunit
                     2; pfam14327"
                     /db_xref="CDD:433869"
     Region          206..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33240.1)"
     Region          <241..436
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Site            308
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P33240.1)"
     Region          340..409
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33240.1)"
     Region          410..469
                     /region_name="12 X 5 AA tandem repeats of M-E-A-R-[AG]"
                     /note="propagated from UniProtKB/Swiss-Prot (P33240.1)"
     Site            468
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P33240.1)"
     Site            475
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P33240.1)"
     Region          508..532
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33240.1)"
     Region          514..577
                     /region_name="Interaction with RPO2TC1.
                     /evidence=ECO:0000269|PubMed:11389848"
                     /note="propagated from UniProtKB/Swiss-Prot (P33240.1)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (P33240.1)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P33240.1)"
     Region          533..573
                     /region_name="CSTF_C"
                     /note="Transcription termination and cleavage factor
                     C-terminal; pfam14304"
                     /db_xref="CDD:464130"
     CDS             1..577
                     /gene="CSTF2"
                     /gene_synonym="CstF-64; CSTF64; XLID113"
                     /coded_by="NM_001325.3:27..1760"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS14473.1"
                     /db_xref="GeneID:1478"
                     /db_xref="HGNC:HGNC:2484"
                     /db_xref="MIM:300907"
ORIGIN      
        1 magltvrdpa vdrslrsvfv gnipyeatee qlkdifsevg pvvsfrlvyd retgkpkgyg
       61 fceyqdqeta lsamrnlngr efsgralrvd naaseknkee lkslgtgapv iespygetis
      121 pedapesisk avaslppeqm felmkqmklc vqnspqearn mllqnpqlay allqaqvvmr
      181 ivdpeialki lhrqtniptl iagnpqpvhg agpgsgsnvs mnqqnpqapq aqslggmhvn
      241 gapplmqasm qggvpapgqm paavtgpgpg slapgggmqa qvgmpgsgpv smergqvpmq
      301 dpraamqrgs lpanvptprg llgdapndpr ggtllsvtge veprgylgpp hqgppmhhvp
      361 ghesrgppph elrggplpep rplmaeprgp mldqrgppld grggrdprgi dargmearam
      421 eargldargl earamearam earamearam earamevrgm eargmdtrgp vpgprgpips
      481 gmqgpspinm gavvpqgsrq vpvmqgtgmq gasiqggsqp ggfspgqnqv tpqdhekaal
      541 imqvlqltad qiamlppeqr qsililkeqi qkstgap
//
LOCUS       NP_003757                450 aa            linear   PRI 21-NOV-2025
DEFINITION  beclin-1 isoform a [Homo sapiens].
ACCESSION   NP_003757
VERSION     NP_003757.1
DBSOURCE    REFSEQ: accession NM_003766.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Baek,S., Chang,J.W., Yoo,S.M., Choo,J., Jung,S., Nah,J. and
            Jung,Y.K.
  TITLE     TMEM9 activates Rab9-dependent alternative autophagy through
            interaction with Beclin1
  JOURNAL   Cell Mol Life Sci 81 (1), 322 (2024)
   PUBMED   39078420
  REMARK    GeneRIF: TMEM9 activates Rab9-dependent alternative autophagy
            through interaction with Beclin1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Oberstein,A., Jeffrey,P.D. and Shi,Y.
  TITLE     Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1
            is a novel BH3-only protein
  JOURNAL   J Biol Chem 282 (17), 13123-13132 (2007)
   PUBMED   17337444
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Furuya,N., Yu,J., Byfield,M., Pattingre,S. and Levine,B.
  TITLE     The evolutionarily conserved domain of Beclin 1 is required for
            Vps34 binding, autophagy and tumor suppressor function
  JOURNAL   Autophagy 1 (1), 46-52 (2005)
   PUBMED   16874027
  REMARK    GeneRIF: Evolutionarily conserved domain of Beclin 1 is essential
            for Vps34 interaction, autophagy function, and tumor suppressor
            function.
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Aita,V.M., Liang,X.H., Murty,V.V., Pincus,D.L., Yu,W., Cayanis,E.,
            Kalachikov,S., Gilliam,T.C. and Levine,B.
  TITLE     Cloning and genomic organization of beclin 1, a candidate tumor
            suppressor gene on chromosome 17q21
  JOURNAL   Genomics 59 (1), 59-65 (1999)
   PUBMED   10395800
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Liang,X.H., Kleeman,L.K., Jiang,H.H., Gordon,G., Goldman,J.E.,
            Berry,G., Herman,B. and Levine,B.
  TITLE     Protection against fatal Sindbis virus encephalitis by beclin, a
            novel Bcl-2-interacting protein
  JOURNAL   J Virol 72 (11), 8586-8596 (1998)
   PUBMED   9765397
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Panaretou,C., Domin,J., Cockcroft,S. and Waterfield,M.D.
  TITLE     Characterization of p150, an adaptor protein for the human
            phosphatidylinositol (PtdIns) 3-kinase. Substrate presentation by
            phosphatidylinositol transfer protein to the p150.Ptdins 3-kinase
            complex
  JOURNAL   J Biol Chem 272 (4), 2477-2485 (1997)
   PUBMED   8999962
REFERENCE   9  (residues 1 to 450)
  AUTHORS   Rommens,J.M., Durocher,F., McArthur,J., Tonin,P., LeBlanc,J.F.,
            Allen,T., Samson,C., Ferri,L., Narod,S., Morgan,K. et al.
  TITLE     Generation of a transcription map at the HSD17B locus centromeric
            to BRCA1 at 17q21
  JOURNAL   Genomics 28 (3), 530-542 (1995)
   PUBMED   7490091
REFERENCE   10 (residues 1 to 450)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC354547.1 and BC010276.1.
            
            Summary: This gene encodes a protein that regulates autophagy, a
            catabolic process of degradation induced by starvation. The encoded
            protein is a component of the phosphatidylinositol-3-kinase (PI3K)
            complex which mediates vesicle-trafficking processes. This protein
            is thought to play a role in multiple cellular processes, including
            tumorigenesis, neurodegeneration and apoptosis. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Sep 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a). Variants 1 and 2
            encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC010276.1, HM005628.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..450
                     /product="beclin-1 isoform a"
                     /note="beclin 1 (coiled-coil, moesin-like BCL2-interacting
                     protein); beclin1-gamma; beclin1-beta; ATG6 autophagy
                     related 6 homolog; coiled-coil myosin-like
                     BCL2-interacting protein; testis secretory sperm-binding
                     protein Li 215e; beclin 1, autophagy related"
                     /calculated_mol_wt=51765
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:31123703; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Region          48..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:23878393; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:23878393,
                     ECO:0000269|PubMed:25891078; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:25891078; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Region          105..129
                     /region_name="BH3"
                     /note="Beclin-1 BH3 domain, Bcl-2-interacting; pfam15285"
                     /db_xref="CDD:464614"
     Region          108..127
                     /region_name="BH3. /evidence=ECO:0000269|PubMed:17337444"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
     Region          112..159
                     /region_name="Interaction with BCL2 and BCL2L1 isoform
                     Bcl-X(L). /evidence=ECO:0000269|PubMed:17446862"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by DAPK1.
                     /evidence=ECO:0000269|PubMed:19180116; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     mat_peptide     134..450
                     /product="Beclin-1-C 37 kDa.
                     /evidence=ECO:0000305|PubMed:21364619. /id=PRO_0000435036"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
                     /calculated_mol_wt=37303
     Region          135..261
                     /region_name="APG6_N"
                     /note="Apg6 coiled-coil region; pfam17675"
                     /db_xref="CDD:465452"
     mat_peptide     150..450
                     /product="Beclin-1-C 35 kDa.
                     /evidence=ECO:0000305|PubMed:21364619,
                     ECO:0000305|PubMed:26263979. /id=PRO_0000435037"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
                     /calculated_mol_wt=35476
     Region          245..450
                     /region_name="Evolutionary conserved domain (ECD).
                     /evidence=ECO:0000305|PubMed:28445460"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
     Region          267..445
                     /region_name="APG6"
                     /note="Apg6 BARA domain; pfam04111"
                     /db_xref="CDD:461178"
     Region          425..450
                     /region_name="Required for membrane-association.
                     /evidence=ECO:0000269|PubMed:23878393"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
     CDS             1..450
                     /gene="BECN1"
                     /gene_synonym="ATG6; beclin1; VPS30"
                     /coded_by="NM_003766.5:153..1505"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11441.1"
                     /db_xref="GeneID:8678"
                     /db_xref="HGNC:HGNC:1034"
                     /db_xref="MIM:604378"
ORIGIN      
        1 megsktsnns tmqvsfvcqr csqplkldts fkildrvtiq eltaplltta qakpgetqee
       61 etnsgeepfi etprqdgvsr rfipparmms tesansftli geasdggtme nlsrrlkvtg
      121 dlfdimsgqt dvdhplceec tdtlldqldt qlnvtenecq nykrcleile qmneddseql
      181 qmelkelale eerliqeled veknrkivae nlekvqaeae rldqeeaqyq reysefkrqq
      241 lelddelksv enqmryaqtq ldklkktnvf natfhiwhsg qfgtinnfrl grlpsvpvew
      301 neinaawgqt vlllhalank mglkfqryrl vpygnhsyle sltdkskelp lycsgglrff
      361 wdnkfdhamv afldcvqqfk eevekgetrf clpyrmdvek gkiedtggsg gsysiktqfn
      421 seeqwtkalk fmltnlkwgl awvssqfynk
//
LOCUS       NP_001317687             583 aa            linear   PRI 21-NOV-2025
DEFINITION  succinate dehydrogenase [ubiquinone] flavoprotein subunit,
            mitochondrial isoform 3 [Homo sapiens].
ACCESSION   NP_001317687 XP_005248388
VERSION     NP_001317687.1
DBSOURCE    REFSEQ: accession NM_001330758.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Kaplan,A.I., Dwight,T., Luxford,C., Benn,D.E. and
            Clifton-Bligh,R.J.
  TITLE     SDHA-related phaeochromocytoma and paraganglioma: review and
            clinical management
  JOURNAL   Endocr Relat Cancer 31 (10), e240111 (2024)
   PUBMED   39133175
  REMARK    GeneRIF: SDHA-related phaeochromocytoma and paraganglioma: review
            and clinical management.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Liu,J., Wang,Y., Wang,X., Li,Y., Jiang,Y., Li,Y., Zhang,W. and
            Yu,W.
  TITLE     Succinate dehydrogenase A deficient renal cell carcinoma: A rare
            renal tumor distinct from typical Succinate dehydrogenase deficient
            renal cell carcinoma
  JOURNAL   Pathol Res Pract 261, 155459 (2024)
   PUBMED   39083879
  REMARK    GeneRIF: Succinate dehydrogenase A deficient renal cell carcinoma:
            A rare renal tumor distinct from typical Succinate dehydrogenase
            deficient renal cell carcinoma.
REFERENCE   3  (residues 1 to 583)
  AUTHORS   Du,Z., Zhou,X., Lai,Y., Xu,J., Zhang,Y., Zhou,S., Feng,Z., Yu,L.,
            Tang,Y., Wang,W., Yu,L., Tian,C., Ran,T., Chen,H., Guddat,L.W.,
            Liu,F., Gao,Y., Rao,Z. and Gong,H.
  TITLE     Structure of the human respiratory complex II
  JOURNAL   Proc Natl Acad Sci U S A 120 (18), e2216713120 (2023)
   PUBMED   37098072
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Schipani,A., Nannini,M., Astolfi,A. and Pantaleo,M.A.
  TITLE     SDHA Germline Mutations in SDH-Deficient GISTs: A Current Update
  JOURNAL   Genes (Basel) 14 (3), 646 (2023)
   PUBMED   36980917
  REMARK    GeneRIF: SDHA Germline Mutations in SDH-Deficient GISTs: A Current
            Update.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 583)
  AUTHORS   Parfait,B., Chretien,D., Rotig,A., Marsac,C., Munnich,A. and
            Rustin,P.
  TITLE     Compound heterozygous mutations in the flavoprotein gene of the
            respiratory chain complex II in a patient with Leigh syndrome
  JOURNAL   Hum Genet 106 (2), 236-243 (2000)
   PUBMED   10746566
REFERENCE   6  (residues 1 to 583)
  AUTHORS   Bourgeron,T., Rustin,P., Chretien,D., Birch-Machin,M.,
            Bourgeois,M., Viegas-Pequignot,E., Munnich,A. and Rotig,A.
  TITLE     Mutation of a nuclear succinate dehydrogenase gene results in
            mitochondrial respiratory chain deficiency
  JOURNAL   Nat Genet 11 (2), 144-149 (1995)
   PUBMED   7550341
REFERENCE   7  (residues 1 to 583)
  AUTHORS   Hirawake,H., Wang,H., Kuramochi,T., Kojima,S. and Kita,K.
  TITLE     Human complex II (succinate-ubiquinone oxidoreductase): cDNA
            cloning of the flavoprotein (Fp) subunit of liver mitochondria
  JOURNAL   J Biochem 116 (1), 221-227 (1994)
   PUBMED   7798181
REFERENCE   8  (residues 1 to 583)
  AUTHORS   Morris,A.A., Farnsworth,L., Ackrell,B.A., Turnbull,D.M. and
            Birch-Machin,M.A.
  TITLE     The cDNA sequence of the flavoprotein subunit of human heart
            succinate dehydrogenase
  JOURNAL   Biochim Biophys Acta 1185 (1), 125-128 (1994)
   PUBMED   8142412
REFERENCE   9  (residues 1 to 583)
  AUTHORS   Rahman,S., Thorburn,D.R. and Ball,M.
  TITLE     Nuclear Gene-Encoded Leigh Syndrome Spectrum Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26425749
REFERENCE   10 (residues 1 to 583)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021087.5.
            
            On Sep 3, 2016 this sequence version replaced XP_005248388.1.
            
            Summary: This gene encodes a major catalytic subunit of
            succinate-ubiquinone oxidoreductase, a complex of the mitochondrial
            respiratory chain. The complex is composed of four nuclear-encoded
            subunits and is localized in the mitochondrial inner membrane.
            Mutations in this gene have been associated with a form of
            mitochondrial respiratory chain deficiency known as Leigh Syndrome.
            A pseudogene has been identified on chromosome 3q29. Alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jun 2014].
            
            Transcript Variant: This variant (3) lacks two in-frame exons in
            the 3' coding region, compared to variant 1. The encoded isoform
            (3) is shorter than isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2251672.1,
                                           SRR14038191.84221.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.33"
     Protein         1..583
                     /product="succinate dehydrogenase [ubiquinone]
                     flavoprotein subunit, mitochondrial isoform 3"
                     /EC_number="1.3.5.1"
                     /note="succinate dehydrogenase [ubiquinone] flavoprotein
                     subunit, mitochondrial; flavoprotein subunit of complex
                     II; succinate dehydrogenase complex, subunit A,
                     flavoprotein (Fp); malate dehydrogenase [quinone]
                     flavoprotein subunit"
                     /calculated_mol_wt=58959
     transit_peptide 1..42
                     /note="Mitochondrion.
                     /evidence=ECO:0000250|UniProtKB:Q0QF01; propagated from
                     UniProtKB/Swiss-Prot (P31040.2)"
                     /calculated_mol_wt=4626
     Region          40..583
                     /region_name="FAD_binding_2"
                     /note="FAD binding domain; cl46878"
                     /db_xref="CDD:481218"
     Site            167
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (P31040.2)"
     Site            179
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P31040.2)"
     Site            182
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (P31040.2)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:22823520; propagated from
                     UniProtKB/Swiss-Prot (P31040.2)"
     Site            250
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (P31040.2)"
     Site            335
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P31040.2)"
     Site            480
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (P31040.2)"
     Site            485
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (P31040.2)"
     Site            498
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (P31040.2)"
     Site            517
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2B3; propagated from
                     UniProtKB/Swiss-Prot (P31040.2)"
     CDS             1..583
                     /gene="SDHA"
                     /gene_synonym="CMD1GG; FP; MC2DN1; NDAXOA; PGL5; PPGL5;
                     SDH1; SDH2; SDHF"
                     /coded_by="NM_001330758.2:37..1788"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82985.1"
                     /db_xref="GeneID:6389"
                     /db_xref="HGNC:HGNC:10680"
                     /db_xref="MIM:600857"
ORIGIN      
        1 msgvrglsrl lsarrlalak awptvlqtgt rgfhftvdgn krasakvsds isaqypvvdh
       61 efdavvvgag gaglraafgl seagfntacv tklfptrsht vaaqgginaa lgnmeednwr
      121 whfydtvkgs dwlgdqdaih ymteqapaav velenygmpf srtedgkiyq rafggqslkf
      181 gkggqahrcc cvadrtghsl lhtlygrslr ydtsyfveyf aldllmenge crgvialcie
      241 dgsihrirak ntvvatggyg rtyfsctsah tstgdgtami traglpcqdl efvqfhptgi
      301 ygagcliteg crgeggilin sqgerfmery apvakdlasr dvvsrsmtle iregrgcgpe
      361 kdhvylqlhh lppeqlatrl pgisetamif agvdvtkepi pvlptvhynm ggiptnykgq
      421 vlrhvngqdq ivpglyacge aacasvhgan rlganslldl vvfgracals ieescrpgdk
      481 vppikpnage esvmnldklr fadgsirtse lrlsmqkvri deydyskpiq gqqkkpfeeh
      541 wrkhtlsyvd vgtgkvtley rpvidktlne adcatvppai rsy
//
LOCUS       NP_001363701             544 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 31 [Homo sapiens].
ACCESSION   NP_001363701
VERSION     NP_001363701.1
DBSOURCE    REFSEQ: accession NM_001376772.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Muckenfuss,L.M., Migenda Herranz,A.C., Boneberg,F.M., Clerici,M.
            and Jinek,M.
  TITLE     Fip1 is a multivalent interaction scaffold for processing factors
            in human mRNA 3' end biogenesis
  JOURNAL   Elife 11, e80332 (2022)
   PUBMED   36073787
  REMARK    GeneRIF: Fip1 is a multivalent interaction scaffold for processing
            factors in human mRNA 3' end biogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   3  (residues 1 to 544)
  AUTHORS   Tennenbaum,J., Groh,M., Venditti,L., Campos-Gazeau,F., Chalayer,E.,
            De Broucker,T., Hamidou,M., Hunault,M., Lyoubi,A., Meunier,R.,
            Muron,T., Sene,D., Slama,B., Guidoux,C., Lefevre,G., Kahn,J.E.,
            Denier,C. and Rohmer,J.
  TITLE     FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a Treatable
            Cause of Watershed Infarction
  JOURNAL   Stroke 52 (10), e605-e609 (2021)
   PUBMED   34304603
  REMARK    GeneRIF: FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a
            Treatable Cause of Watershed Infarction.
REFERENCE   4  (residues 1 to 544)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 544)
  AUTHORS   Helbig,G., Lewandowski,K., Swiderska,A., Rodzaj,M., Seferynska,I.
            and Gajkowska-Kulik,J.
  TITLE     Exquisite response to imatinib mesylate in FIP1L1-PDGFRA-mutated
            hypereosinophilic syndrome: a 12-year experience of the Polish
            Hypereosinophilic Syndrome Study Group
  JOURNAL   Pol Arch Intern Med 130 (3), 255-257 (2020)
   PUBMED   32125294
  REMARK    GeneRIF: Exquisite response to imatinib mesylate in
            FIP1L1-PDGFRA-mutated hypereosinophilic syndrome: a 12-year
            experience of the Polish Hypereosinophilic Syndrome Study Group.
REFERENCE   6  (residues 1 to 544)
  AUTHORS   Cools,J., Quentmeier,H., Huntly,B.J., Marynen,P., Griffin,J.D.,
            Drexler,H.G. and Gilliland,D.G.
  TITLE     The EOL-1 cell line as an in vitro model for the study of
            FIP1L1-PDGFRA-positive chronic eosinophilic leukemia
  JOURNAL   Blood 103 (7), 2802-2805 (2004)
   PUBMED   14630792
  REMARK    GeneRIF: results indicate that the fusion of FIP1L1 to PDGFRA
            occurs rarely in leukemia cell lines
REFERENCE   7  (residues 1 to 544)
  AUTHORS   Kaufmann,I., Martin,G., Friedlein,A., Langen,H. and Keller,W.
  TITLE     Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements
            and stimulates poly(A) polymerase
  JOURNAL   EMBO J 23 (3), 616-626 (2004)
   PUBMED   14749727
REFERENCE   8  (residues 1 to 544)
  AUTHORS   Pardanani,A., Ketterling,R.P., Brockman,S.R., Flynn,H.C.,
            Paternoster,S.F., Shearer,B.M., Reeder,T.L., Li,C.Y., Cross,N.C.,
            Cools,J., Gilliland,D.G., Dewald,G.W. and Tefferi,A.
  TITLE     CHIC2 deletion, a surrogate for FIP1L1-PDGFRA fusion, occurs in
            systemic mastocytosis associated with eosinophilia and predicts
            response to imatinib mesylate therapy
  JOURNAL   Blood 102 (9), 3093-3096 (2003)
   PUBMED   12842979
  REMARK    GeneRIF: observations suggest that the FIP1L1-PDGFRA rearrangement
            occurs in an early hematopoietic progenitor and suggests that the
            molecular pathogenesis for a subset of SMCD patients is similar to
            that of HES
REFERENCE   9  (residues 1 to 544)
  AUTHORS   Griffin,J.H., Leung,J., Bruner,R.J., Caligiuri,M.A. and
            Briesewitz,R.
  TITLE     Discovery of a fusion kinase in EOL-1 cells and idiopathic
            hypereosinophilic syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (13), 7830-7835 (2003)
   PUBMED   12808148
REFERENCE   10 (residues 1 to 544)
  AUTHORS   Cools,J., DeAngelo,D.J., Gotlib,J., Stover,E.H., Legare,R.D.,
            Cortes,J., Kutok,J., Clark,J., Galinsky,I., Griffin,J.D.,
            Cross,N.C., Tefferi,A., Malone,J., Alam,R., Schrier,S.L.,
            Schmid,J., Rose,M., Vandenberghe,P., Verhoef,G., Boogaerts,M.,
            Wlodarska,I., Kantarjian,H., Marynen,P., Coutre,S.E., Stone,R. and
            Gilliland,D.G.
  TITLE     A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes
            as a therapeutic target of imatinib in idiopathic hypereosinophilic
            syndrome
  JOURNAL   N Engl J Med 348 (13), 1201-1214 (2003)
   PUBMED   12660384
  REMARK    GeneRIF: The hypereosinophilic syndrome may result from a novel
            fusion tyrosine kinase - FIP1L1-PDGFRalpha - that is a consequence
            of an interstitial chromosomal deletion.
            GeneRIF: Describes the fusion gene Fip1-like-1-PDGFRalpha in
            patients with idiopathic hypereosinophilic syndrome, mostly
            responsive to imatinib therapy.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098821.3 and AC058822.6.
            
            Summary: This gene encodes a subunit of the CPSF (cleavage and
            polyadenylation specificity factor) complex that polyadenylates the
            3' end of mRNA precursors. This gene, the homolog of yeast Fip1
            (factor interacting with PAP), binds to U-rich sequences of
            pre-mRNA and stimulates poly(A) polymerase activity. Its N-terminus
            contains a PAP-binding site and its C-terminus an RNA-binding
            domain. An interstitial chromosomal deletion on 4q12 creates an
            in-frame fusion of human genes FIP1L1 and PDGFRA (platelet-derived
            growth factor receptor, alpha). The FIP1L1-PDGFRA fusion gene
            encodes a constitutively activated tyrosine kinase that joins the
            first 233 amino acids of FIP1L1 to the last 523 amino acids of
            PDGFRA. This gene fusion and chromosomal deletion is the cause of
            some forms of idiopathic hypereosinophilic syndrome (HES). This
            syndrome, recently reclassified as chronic eosinophilic leukemia
            (CEL), is responsive to treatment with tyrosine kinase inhibitors.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.161583.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..544
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     31"
                     /note="rearranged in hypereosinophilia; pre-mRNA
                     3'-end-processing factor FIP1; FIP1-like 1 protein; factor
                     interacting with PAP; FIP1 like 1; FIP1L1 cleavage and
                     polyadenylation specific factor subunit"
                     /calculated_mol_wt=60838
     Region          <133..160
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     CDS             1..544
                     /gene="FIP1L1"
                     /gene_synonym="FIP1; hFip1; Rhe"
                     /coded_by="NM_001376772.1:199..1833"
                     /note="isoform 31 is encoded by transcript variant 31"
                     /db_xref="CCDS:CCDS93511.1"
                     /db_xref="GeneID:81608"
                     /db_xref="HGNC:HGNC:19124"
                     /db_xref="MIM:607686"
ORIGIN      
        1 msageverlv selsggtggd eeeewlyggp wdvhvhsdla kdldenever peeenasanp
       61 psgiedetae ngvpkpkvte teddsdsdsd ddeddvhvti gdiktgapqy gsygtapvnl
      121 niktggrvyg ttgadlsdyf nygfnedtwk aycekqkrir mglevipvts ttnkitvqqg
      181 rtgnseketa lpstkaefts ppslfktglp psrnstssqs qtstasrkan ssvgkwqdry
      241 graespdlrr lpgaidvigq titisrvegr rranensniq vlsersatev dnnfskpppf
      301 fppgappthl ppppflpppp tvstapplip ppgipitvpp pgfppppgap ppslipties
      361 ghssgydsrs arafpygnva fphlpgsaps wpslvdtskq wdyyarrekd rdrerdrdre
      421 rdrdrdrere rtrerererd hsptpsvfns deeryryrey aergyerhra srekeerhre
      481 rrhrekeetr hkssrsnsrr rheseegdsh rrhkhkkskr skegkeagse papeqestea
      541 tpae
//
LOCUS       NP_001363816             240 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor ligand superfamily member 14 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001363816 XP_016882906
VERSION     NP_001363816.1
DBSOURCE    REFSEQ: accession NM_001376887.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Kanai,S., Fujiwara,H., Mizuno,S., Kishikawa,T., Nakatsuka,T.,
            Hamada,T., Tanaka,M., Arita,J., Nakai,Y., Isayama,H., Kasuga,M.,
            Tateishi,R., Tateishi,K., Ushiku,T., Hasegawa,K., Koike,K. and
            Fujishiro,M.
  TITLE     Increased expression of TNFRSF14 and LIGHT in biliary epithelial
            cells of patients with primary sclerosing cholangitis
  JOURNAL   Dig Liver Dis 56 (2), 305-311 (2024)
   PUBMED   37722959
  REMARK    GeneRIF: Increased expression of TNFRSF14 and LIGHT in biliary
            epithelial cells of patients with primary sclerosing cholangitis.
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Huang,X.W., Pang,S.W., Yang,L.Z., Han,T., Chen,J.M., Huang,C.W.,
            Liao,L. and Xie,P.J.
  TITLE     TNFSF14 mediates the impact of docosahexaenoic acid on atopic
            dermatitis: a Mendelian randomization study
  JOURNAL   Eur Rev Med Pharmacol Sci 28 (1), 107-117 (2024)
   PUBMED   38235898
  REMARK    GeneRIF: TNFSF14 mediates the impact of docosahexaenoic acid on
            atopic dermatitis: a Mendelian randomization study.
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Zhang,N., Liu,X., Qin,J., Sun,Y., Xiong,H., Lin,B., Liu,K., Tan,B.,
            Zhang,C., Huang,C., Ren,S., Liu,M. and Du,B.
  TITLE     LIGHT/TNFSF14 promotes CAR-T cell trafficking and cytotoxicity
            through reversing immunosuppressive tumor microenvironment
  JOURNAL   Mol Ther 31 (9), 2575-2590 (2023)
   PUBMED   37408308
  REMARK    GeneRIF: LIGHT/TNFSF14 promotes CAR-T cell trafficking and
            cytotoxicity through reversing immunosuppressive tumor
            microenvironment.
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Heo,S.K., Yu,H.M., Kim,D.K., Seo,H.J., Shin,Y., Kim,S.A., Kim,M.,
            Kim,Y., Lee,Y.J., Noh,E.K. and Jo,J.C.
  TITLE     LIGHT (TNFSF14) promotes the differentiation of human bone
            marrow-derived mesenchymal stem cells into functional
            hepatocyte-like cells
  JOURNAL   PLoS One 18 (8), e0289798 (2023)
   PUBMED   37552689
  REMARK    GeneRIF: LIGHT (TNFSF14) promotes the differentiation of human bone
            marrow-derived mesenchymal stem cells into functional
            hepatocyte-like cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Shuptrine,C.W., Perez,V.M., Selitsky,S.R., Schreiber,T.H. and
            Fromm,G.
  TITLE     Shining a LIGHT on myeloid cell targeted immunotherapy
  JOURNAL   Eur J Cancer 187, 147-160 (2023)
   PUBMED   37167762
  REMARK    Review article
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Yu,K.Y., Kwon,B., Ni,J., Zhai,Y., Ebner,R. and Kwon,B.S.
  TITLE     A newly identified member of tumor necrosis factor receptor
            superfamily (TR6) suppresses LIGHT-mediated apoptosis
  JOURNAL   J Biol Chem 274 (20), 13733-13736 (1999)
   PUBMED   10318773
REFERENCE   7  (residues 1 to 240)
  AUTHORS   Harrop,J.A., McDonnell,P.C., Brigham-Burke,M., Lyn,S.D., Minton,J.,
            Tan,K.B., Dede,K., Spampanato,J., Silverman,C., Hensley,P.,
            DiPrinzio,R., Emery,J.G., Deen,K., Eichman,C., Chabot-Fletcher,M.,
            Truneh,A. and Young,P.R.
  TITLE     Herpesvirus entry mediator ligand (HVEM-L), a novel ligand for
            HVEM/TR2, stimulates proliferation of T cells and inhibits HT29
            cell growth
  JOURNAL   J Biol Chem 273 (42), 27548-27556 (1998)
   PUBMED   9765287
REFERENCE   8  (residues 1 to 240)
  AUTHORS   Zhai,Y., Guo,R., Hsu,T.L., Yu,G.L., Ni,J., Kwon,B.S., Jiang,G.W.,
            Lu,J., Tan,J., Ugustus,M., Carter,K., Rojas,L., Zhu,F., Lincoln,C.,
            Endress,G., Xing,L., Wang,S., Oh,K.O., Gentz,R., Ruben,S.,
            Lippman,M.E., Hsieh,S.L. and Yang,D.
  TITLE     LIGHT, a novel ligand for lymphotoxin beta receptor and TR2/HVEM
            induces apoptosis and suppresses in vivo tumor formation via gene
            transfer
  JOURNAL   J Clin Invest 102 (6), 1142-1151 (1998)
   PUBMED   9739048
REFERENCE   9  (residues 1 to 240)
  AUTHORS   Marsters,S.A., Sheridan,J.P., Pitti,R.M., Brush,J., Goddard,A. and
            Ashkenazi,A.
  TITLE     Identification of a ligand for the death-domain-containing receptor
            Apo3
  JOURNAL   Curr Biol 8 (9), 525-528 (1998)
   PUBMED   9560343
REFERENCE   10 (residues 1 to 240)
  AUTHORS   Mauri,D.N., Ebner,R., Montgomery,R.I., Kochel,K.D., Cheung,T.C.,
            Yu,G.L., Ruben,S., Murphy,M., Eisenberg,R.J., Cohen,G.H.,
            Spear,P.G. and Ware,C.F.
  TITLE     LIGHT, a new member of the TNF superfamily, and lymphotoxin alpha
            are ligands for herpesvirus entry mediator
  JOURNAL   Immunity 8 (1), 21-30 (1998)
   PUBMED   9462508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008760.7, BC018058.1 and
            AF064090.1.
            
            On Nov 20, 2019 this sequence version replaced XP_016882906.1.
            
            Summary: The protein encoded by this gene is a member of the tumor
            necrosis factor (TNF) ligand family. This protein is a ligand for
            TNFRSF14, which is a member of the tumor necrosis factor receptor
            superfamily, and which is also known as a herpesvirus entry
            mediator (HVEM). This protein may function as a costimulatory
            factor for the activation of lymphoid cells and as a deterrent to
            infection by herpesvirus. This protein has been shown to stimulate
            the proliferation of T cells, and trigger apoptosis of various
            tumor cells. This protein is also reported to prevent tumor
            necrosis factor alpha mediated apoptosis in primary hepatocyte. Two
            alternatively spliced transcript variant encoding distinct isoforms
            have been reported. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK292037.1, SRR14038194.3250868.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000675206.1/ ENSP00000502837.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..240
                     /product="tumor necrosis factor ligand superfamily member
                     14 isoform 1"
                     /note="tumor necrosis factor ligand 1D; herpesvirus entry
                     mediator ligand; tumor necrosis factor (ligand)
                     superfamily, member 14; tumor necrosis factor superfamily
                     member 14"
                     /calculated_mol_wt=26219
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43557.2)"
     Site            82..83
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43557.2)"
     Region          94..238
                     /region_name="TNF"
                     /note="Tumor Necrosis Factor; TNF superfamily members
                     include the cytokines: TNF (TNF-alpha), LT
                     (lymphotoxin-alpha, TNF-beta), CD40 ligand, Apo2L (TRAIL),
                     Fas ligand, and osteoprotegerin (OPG) ligand. These
                     proteins generally have an intracellular N-terminal...;
                     cd00184"
                     /db_xref="CDD:238108"
     Site            order(97,142,144,202,207,234,238)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:238108"
     Site            102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|Ref.10; propagated from
                     UniProtKB/Swiss-Prot (O43557.2)"
     Site            order(115..116,121,163,170,175)
                     /site_type="active"
                     /note="receptor binding sites [active]"
                     /db_xref="CDD:238108"
     CDS             1..240
                     /gene="TNFSF14"
                     /gene_synonym="CD258; HVEML; LIGHT; LTg"
                     /coded_by="NM_001376887.1:92..814"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS12171.1"
                     /db_xref="GeneID:8740"
                     /db_xref="HGNC:HGNC:11930"
                     /db_xref="MIM:604520"
ORIGIN      
        1 meesvvrpsv fvvdgqtdip ftrlgrshrr qscsvarvgl glllllmgag lavqgwfllq
       61 lhwrlgemvt rlpdgpagsw eqliqerrsh evnpaahltg anssltgsgg pllwetqlgl
      121 aflrglsyhd galvvtkagy yyiyskvqlg gvgcplglas tithglykrt prypeelell
      181 vsqqspcgra tsssrvwwds sflggvvhle agekvvvrvl derlvrlrdg trsyfgafmv
//
LOCUS       NP_001278650            1227 aa            linear   PRI 21-NOV-2025
DEFINITION  cytoplasmic FMR1-interacting protein 2 isoform b [Homo sapiens].
ACCESSION   NP_001278650
VERSION     NP_001278650.1
DBSOURCE    REFSEQ: accession NM_001291721.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1227)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1227)
  AUTHORS   Peng,X., Wellard,N., Ghosh,A., Troakes,C. and Giese,K.P.
  TITLE     Different dysregulations of CYFIP1 and CYFIP2 in distinct types of
            dementia
  JOURNAL   Brain Res Bull 206, 110849 (2024)
   PUBMED   38128786
  REMARK    GeneRIF: Different dysregulations of CYFIP1 and CYFIP2 in distinct
            types of dementia.
REFERENCE   3  (residues 1 to 1227)
  AUTHORS   Peng,Q., Ren,B., Xin,K., Liu,W., Alam,M.S., Yang,Y., Gu,X., Zhu,Y.
            and Tian,Y.
  TITLE     CYFIP2 serves as a prognostic biomarker and correlates with tumor
            immune microenvironment in human cancers
  JOURNAL   Eur J Med Res 28 (1), 364 (2023)
   PUBMED   37735711
  REMARK    GeneRIF: CYFIP2 serves as a prognostic biomarker and correlates
            with tumor immune microenvironment in human cancers.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1227)
  AUTHORS   Biembengut,I.V., Shigunov,P., Frota,N.F., Lourenzoni,M.R. and de
            Souza,T.A.C.B.
  TITLE     Molecular Dynamics of CYFIP2 Protein and Its R87C Variant Related
            to Early Infantile Epileptic Encephalopathy
  JOURNAL   Int J Mol Sci 23 (15), 8708 (2022)
   PUBMED   35955843
  REMARK    GeneRIF: Molecular Dynamics of CYFIP2 Protein and Its R87C Variant
            Related to Early Infantile Epileptic Encephalopathy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1227)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1227)
  AUTHORS   Eden,S., Rohatgi,R., Podtelejnikov,A.V., Mann,M. and Kirschner,M.W.
  TITLE     Mechanism of regulation of WAVE1-induced actin nucleation by Rac1
            and Nck
  JOURNAL   Nature 418 (6899), 790-793 (2002)
   PUBMED   12181570
REFERENCE   7  (residues 1 to 1227)
  AUTHORS   Schenck,A., Bardoni,B., Moro,A., Bagni,C. and Mandel,J.L.
  TITLE     A highly conserved protein family interacting with the fragile X
            mental retardation protein (FMRP) and displaying selective
            interactions with FMRP-related proteins FXR1P and FXR2P
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8844-8849 (2001)
   PUBMED   11438699
REFERENCE   8  (residues 1 to 1227)
  AUTHORS   Saller,E., Tom,E., Brunori,M., Otter,M., Estreicher,A., Mack,D.H.
            and Iggo,R.
  TITLE     Increased apoptosis induction by 121F mutant p53
  JOURNAL   EMBO J 18 (16), 4424-4437 (1999)
   PUBMED   10449408
REFERENCE   9  (residues 1 to 1227)
  AUTHORS   Witke,W., Podtelejnikov,A.V., Di Nardo,A., Sutherland,J.D.,
            Gurniak,C.B., Dotti,C. and Mann,M.
  TITLE     In mouse brain profilin I and profilin II associate with regulators
            of the endocytic pathway and actin assembly
  JOURNAL   EMBO J 17 (4), 967-976 (1998)
   PUBMED   9463375
REFERENCE   10 (residues 1 to 1227)
  AUTHORS   Kitamura,T., Kitamura,Y., Yonezawa,K., Totty,N.F., Gout,I.,
            Hara,K., Waterfield,M.D., Sakaue,M., Ogawa,W. and Kasuga,M.
  TITLE     Molecular cloning of p125Nap1, a protein that associates with an
            SH3 domain of Nck
  JOURNAL   Biochem Biophys Res Commun 219 (2), 509-514 (1996)
   PUBMED   8605018
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG699081.1, AK303702.1, BC011762.1, AL136549.1 and AC008676.6.
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1. The encoded
            isoform (b) is shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.27759.1, AK303702.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1227
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..1227
                     /product="cytoplasmic FMR1-interacting protein 2 isoform
                     b"
                     /note="p53-inducible protein 121"
                     /calculated_mol_wt=142447
     Region          362..1195
                     /region_name="FragX_IP"
                     /note="Cytoplasmic Fragile-X interacting family;
                     pfam05994"
                     /db_xref="CDD:461799"
     CDS             1..1227
                     /gene="CYFIP2"
                     /gene_synonym="DEE65; EIEE65; PIR121"
                     /coded_by="NM_001291721.2:97..3780"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS78078.1"
                     /db_xref="GeneID:26999"
                     /db_xref="HGNC:HGNC:13760"
                     /db_xref="MIM:606323"
ORIGIN      
        1 mtthvtleda lsnvdlleel plpdqqpcie pppssimyqa nfdtnfedrn afvtgiaryi
       61 eqatvhssmv kcneqpnrve iyektvevle pevtklmkfm yfqrkaierf csevkrlcha
      121 errkdfvsea ylltlgkfin mfavldelkn mkcsvkndhs aykraaqflr kmadpqsiqe
      181 sqnlsmflan hnritqclhq qlevipgyee lladivnicv dyyenkmylt psekhmllkv
      241 mgfglylmdg nvsniyklda kkrinlskid kffkqlqvvp lfgdmqiela ryiktsahye
      301 enkskwtctq ssispqynic eqmvqirddh irfiselary snsevvtgsg ldsqksdeey
      361 relfdlalrg lqllskwsah vmevyswklv hptdkfcnkd cpgtaeeyer atrynytsee
      421 kfafveviam ikglqvlmgr mesvfnqair ntiyaalqdf aqvtlreplr qavrkkknvl
      481 isvlqairkt icdweggrep pndpclrgek dpkggfdikv prravgpsst qlymvrtmle
      541 sliadksgsk ktlrssldgp ivlaiedfhk qsfffthlln isealqqccd lsqlwfreff
      601 leltmgrriq fpiemsmpwi ltdhiletke psmmeyvlyp ldlyndsayy altkfkkqfl
      661 ydeieaevnl cfdqfvykla dqifayykam agsvlldkrf raecknygvi ipyppsnrye
      721 tllkqrhvql lgrsidlnrl itqrisaamy ksldqaisrf esedltsive lewlleinrl
      781 thrllckhmt ldsfdamfre anhnvsapyg ritlhvfwel nfdflpnycy ngstnrfvrt
      841 aipftqepqr dkpanvqpyy lygskplnia yshiyssyrn fvgpphfkti crllgyqgia
      901 vvmeellkiv ksllqgtilq yvktlievmp kicrlprhey gspgileffh hqlkdiieya
      961 elktdvfqsl revgnailfc llieqalsqe evcdllhaap fqnilprvyi kegerlevrm
     1021 krleakyapl hlvplierlg tpqqiaiare gdlltkerlc cglsmfevil trirsylqdp
     1081 iwrgppptng vmhvdecvef hrlwsamqfv ycipvgtnef taeqcfgdgl nwagcsiivl
     1141 lgqqrrfdlf dfcyhllkvq rqdgkdeiik nvplkkmadr irkyqilnne vfailnkymk
     1201 svetdsstve hvrcfqppih qslattc
//
LOCUS       NP_694543                707 aa            linear   PRI 21-NOV-2025
DEFINITION  histone-lysine N-methyltransferase EZH2 isoform b [Homo sapiens].
ACCESSION   NP_694543 XP_374578
VERSION     NP_694543.1
DBSOURCE    REFSEQ: accession NM_152998.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Zhang,D., Qiu,Y., Zhang,W., Du,D., Liu,Y., Liu,L., Li,J., Chen,Z.,
            Yu,X., Ye,M., Wang,W., Li,Z. and Shao,J.
  TITLE     Homeobox B9 promotes the invasion and metastasis of hepatocellular
            carcinoma cells via the EZH2-MIR203A-SNAI2 axis
  JOURNAL   J Transl Med 22 (1), 918 (2024)
   PUBMED   39390614
  REMARK    GeneRIF: Homeobox B9 promotes the invasion and metastasis of
            hepatocellular carcinoma cells via the EZH2-MIR203A-SNAI2 axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Mingardo,E., Kalanithy,J.C., Dworschak,G., Ishorst,N., Yilmaz,O.,
            Lindenberg,T., Hollstein,R., Felger,T., Angrand,P.O., Reutter,H.
            and Odermatt,B.
  TITLE     EZH2 specifically regulates ISL1 during embryonic urinary tract
            formation
  JOURNAL   Sci Rep 14 (1), 22909 (2024)
   PUBMED   39358471
  REMARK    GeneRIF: EZH2 specifically regulates ISL1 during embryonic urinary
            tract formation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Gallardo,A., Lopez-Onieva,L., Belmonte-Reche,E.,
            Fernandez-Rengel,I., Serrano-Prados,A., Molina,A., Sanchez-Pozo,A.
            and Landeira,D.
  TITLE     EZH2 represses mesenchymal genes and upholds the epithelial state
            of breast carcinoma cells
  JOURNAL   Cell Death Dis 15 (8), 609 (2024)
   PUBMED   39174513
  REMARK    GeneRIF: EZH2 represses mesenchymal genes and upholds the
            epithelial state of breast carcinoma cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Hu,X., Liu,Y., Shen,H., Zhang,T. and Liang,T.
  TITLE     MTF2 facilitates the advancement of osteosarcoma through mediating
            EZH2/SFRP1/Wnt signaling
  JOURNAL   J Orthop Surg Res 19 (1), 467 (2024)
   PUBMED   39118123
  REMARK    GeneRIF: MTF2 facilitates the advancement of osteosarcoma through
            mediating EZH2/SFRP1/Wnt signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 707)
  AUTHORS   Cardoso,C., Timsit,S., Villard,L., Khrestchatisky,M., Fontes,M. and
            Colleaux,L.
  TITLE     Specific interaction between the XNP/ATR-X gene product and the SET
            domain of the human EZH2 protein
  JOURNAL   Hum Mol Genet 7 (4), 679-684 (1998)
   PUBMED   9499421
REFERENCE   7  (residues 1 to 707)
  AUTHORS   Laible,G., Wolf,A., Dorn,R., Reuter,G., Nislow,C., Lebersorger,A.,
            Popkin,D., Pillus,L. and Jenuwein,T.
  TITLE     Mammalian homologues of the Polycomb-group gene Enhancer of zeste
            mediate gene silencing in Drosophila heterochromatin and at S.
            cerevisiae telomeres
  JOURNAL   EMBO J 16 (11), 3219-3232 (1997)
   PUBMED   9214638
REFERENCE   8  (residues 1 to 707)
  AUTHORS   Chen,H., Rossier,C. and Antonarakis,S.E.
  TITLE     Cloning of a human homolog of the Drosophila enhancer of zeste gene
            (EZH2) that maps to chromosome 21q22.2
  JOURNAL   Genomics 38 (1), 30-37 (1996)
   PUBMED   8954776
REFERENCE   9  (residues 1 to 707)
  AUTHORS   Hobert,O., Jallal,B. and Ullrich,A.
  TITLE     Interaction of Vav with ENX-1, a putative transcriptional regulator
            of homeobox gene expression
  JOURNAL   Mol Cell Biol 16 (6), 3066-3073 (1996)
   PUBMED   8649418
REFERENCE   10 (residues 1 to 707)
  AUTHORS   Ocansey,S. and Tatton-Brown,K.
  TITLE     EZH2-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23865096
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN283479.1, AK314291.1,
            BC010858.2 and BU953788.1.
            
            On Aug 30, 2004 this sequence version replaced XP_374578.1.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein associates
            with the embryonic ectoderm development protein, the VAV1
            oncoprotein, and the X-linked nuclear protein. This protein may
            play a role in the hematopoietic and central nervous systems.
            Multiple alternatively splcied transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Feb 2011].
            
            Transcript Variant: This variant (2) lacks an in-frame exon and an
            in-frame segment in the coding region, as compared to variant 1.
            The resulting isoform (b) lacks two internal segments, as compared
            to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314291.1, SRR11853565.26847.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..707
                     /product="histone-lysine N-methyltransferase EZH2 isoform
                     b"
                     /EC_number="2.1.1.356"
                     /note="lysine N-methyltransferase 6; histone-lysine
                     N-methyltransferase EZH2; enhancer of zeste homolog 2"
                     /calculated_mol_wt=80907
     Region          39..68
                     /region_name="EZH2_WD-Binding"
                     /note="WD repeat binding protein EZH2; pfam11616"
                     /db_xref="CDD:463308"
     Region          119..210
                     /region_name="PRC2_HTH_1"
                     /note="Polycomb repressive complex 2 tri-helical domain;
                     pfam18118"
                     /db_xref="CDD:436286"
     Region          520..551
                     /region_name="preSET_CXC"
                     /note="CXC domain; pfam18264"
                     /db_xref="CDD:408079"
     Region          570..689
                     /region_name="SET_EZH2"
                     /note="SET domain found in enhancer of zeste homolog 2
                     (EZH2) and similar proteins; cd19218"
                     /db_xref="CDD:380995"
     Site            order(574,576..579,581,585,588,590,640..641,644,664,680)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:380995"
     Site            order(582..585,602,609,612..613,616,620,623..629,646..650,
                     658,685,687..688)
                     /site_type="active"
                     /db_xref="CDD:380995"
     Site            order(584..585,618..619,622,624,626,639,646..650,687)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380995"
     Site            order(584..585,618..619,622,624,626,639,646..649)
                     /site_type="inhibition"
                     /note="inhibitor binding site [chemical binding]"
                     /db_xref="CDD:380995"
     Site            order(602,609,612..613,616,620,625,627..629,658,685,
                     687..689)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:380995"
     CDS             1..707
                     /gene="EZH2"
                     /gene_synonym="ENX-1; ENX1; EZH2b; KMT6; KMT6A; WVS; WVS2"
                     /coded_by="NM_152998.3:136..2259"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS5892.1"
                     /db_xref="GeneID:2146"
                     /db_xref="HGNC:HGNC:3527"
                     /db_xref="MIM:601573"
ORIGIN      
        1 mgqtgkksek gpvcwrkrvk seymrlrqlk rfrradevks mfssnrqkil erteilnqew
       61 kqrriqpvhi ltsvsslrgt revedetvlh nipymgdevl dqdgtfieel iknydgkvhg
      121 drecgfinde ifvelvnalg qynddddddd gddpeereek qkdledhrdd kesrpprkfp
      181 sdkifeaiss mfpdkgtaee lkekykelte qqlpgalppe ctpnidgpna ksvqreqslh
      241 sfhtlfcrrc fkydcflhpf hatpntykrk ntetaldnkp cgpqcyqhle gakefaaalt
      301 aeriktppkr pggrrrgrlp nnssrpstpt invleskdtd sdreagtetg genndkeeee
      361 kkdetsssse ansrcqtpik mkpnieppen vewsgaeasm frvligtyyd nfcaiarlig
      421 tktcrqvyef rvkessiiap apaedvdtpp rkkkrkhrlw aahcrkiqlk kdgssnhvyn
      481 yqpcdhprqp cdsscpcvia qnfcekfcqc ssecqnrfpg crckaqcntk qcpcylavre
      541 cdpdlcltcg aadhwdsknv sckncsiqrg skkhlllaps dvagwgifik dpvqknefis
      601 eycgeiisqd eadrrgkvyd kymcsflfnl nndfvvdatr kgnkirfanh svnpncyakv
      661 mmvngdhrig ifakraiqtg eelffdyrys qadalkyvgi eremeip
//
LOCUS       NP_004547                361 aa            linear   PRI 21-NOV-2025
DEFINITION  NF-kappa-B inhibitor epsilon [Homo sapiens].
ACCESSION   NP_004547
VERSION     NP_004547.3
DBSOURCE    REFSEQ: accession NM_004556.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Bonato,A., Chakraborty,S., Bomben,R., Canarutto,G., Felician,G.,
            Martines,C., Zucchetto,A., Pozzo,F., Vujovikj,M., Polesel,J.,
            Chiarenza,A., Del Principe,M.I., Del Poeta,G., D'Arena,G.,
            Marasca,R., Tafuri,A., Laurenti,L., Piazza,S., Dimovski,A.J.,
            Gattei,V. and Efremov,D.G.
  TITLE     NFKBIE mutations are selected by the tumor microenvironment and
            contribute to immune escape in chronic lymphocytic leukemia
  JOURNAL   Leukemia 38 (7), 1511-1521 (2024)
   PUBMED   38486128
  REMARK    GeneRIF: NFKBIE mutations are selected by the tumor
            microenvironment and contribute to immune escape in chronic
            lymphocytic leukemia.
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Bordini,J., Lenzi,C., Frenquelli,M., Morabito,A., Pseftogas,A.,
            Belloni,D., Mansouri,L., Tsiolas,G., Perotta,E., Ranghetti,P.,
            Gandini,F., Genova,F., Hagerstrand,D., Gavriilidis,G., Keisaris,S.,
            Pechlivanis,N., Davi,F., Kay,N.E., Langerak,A.W., Pospisilova,S.,
            Scarfo,L., Makris,A., Psomopoulos,F.E., Stamatopoulos,K.,
            Rosenquist,R., Campanella,A. and Ghia,P.
  TITLE     IkappaBepsilon deficiency accelerates disease development in
            chronic lymphocytic leukemia
  JOURNAL   Leukemia 38 (6), 1287-1298 (2024)
   PUBMED   38575671
  REMARK    GeneRIF: IkappaBepsilon deficiency accelerates disease development
            in chronic lymphocytic leukemia.
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Wang,D., Zheng,X., Chai,L., Zhao,J., Zhu,J., Li,Y., Yang,P., Mao,Q.
            and Xia,H.
  TITLE     FAM76B regulates NF-kappaB-mediated inflammatory pathway by
            influencing the translocation of hnRNPA2B1
  JOURNAL   Elife 12, e85659 (2023)
   PUBMED   37643469
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Goos,H., Kinnunen,M., Salokas,K., Tan,Z., Liu,X., Yadav,L.,
            Zhang,Q., Wei,G.H. and Varjosalo,M.
  TITLE     Human transcription factor protein interaction networks
  JOURNAL   Nat Commun 13 (1), 766 (2022)
   PUBMED   35140242
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 361)
  AUTHORS   Li,Z. and Nabel,G.J.
  TITLE     A new member of the I kappaB protein family, I kappaB epsilon,
            inhibits RelA (p65)-mediated NF-kappaB transcription
  JOURNAL   Mol Cell Biol 17 (10), 6184-6190 (1997)
   PUBMED   9315679
REFERENCE   7  (residues 1 to 361)
  AUTHORS   Curristin,S.M., Bird,K.J., Tubbs,R.J. and Ruddell,A.
  TITLE     VBP and RelA regulate avian leukosis virus long terminal
            repeat-enhanced transcription in B cells
  JOURNAL   J Virol 71 (8), 5972-5981 (1997)
   PUBMED   9223487
REFERENCE   8  (residues 1 to 361)
  AUTHORS   Whiteside,S.T., Epinat,J.C., Rice,N.R. and Israel,A.
  TITLE     I kappa B epsilon, a novel member of the I kappa B family, controls
            RelA and cRel NF-kappa B activity
  JOURNAL   EMBO J 16 (6), 1413-1426 (1997)
   PUBMED   9135156
REFERENCE   9  (residues 1 to 361)
  AUTHORS   Hansen,S.K., Baeuerle,P.A. and Blasi,F.
  TITLE     Purification, reconstitution, and I kappa B association of the
            c-Rel-p65 (RelA) complex, a strong activator of transcription
  JOURNAL   Mol Cell Biol 14 (4), 2593-2603 (1994)
   PUBMED   8139561
REFERENCE   10 (residues 1 to 361)
  AUTHORS   Kumar,S. and Gelinas,C.
  TITLE     I kappa B alpha-mediated inhibition of v-Rel DNA binding requires
            direct interaction with the RXXRXRXXC Rel/kappa B DNA-binding motif
  JOURNAL   Proc Natl Acad Sci U S A 90 (19), 8962-8966 (1993)
   PUBMED   8415639
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U91616.1, BC063609.1 and
            AL139392.10.
            
            On Aug 31, 2019 this sequence version replaced NP_004547.2.
            
            Summary: The protein encoded by this gene binds to components of
            NF-kappa-B, trapping the complex in the cytoplasm and preventing it
            from activating genes in the nucleus. Phosphorylation of the
            encoded protein targets it for destruction by the ubiquitin
            pathway, which activates NF-kappa-B by making it available to
            translocate to the nucleus. [provided by RefSeq, Sep 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC063609.1, SRR11853563.28229.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000619360.6/ ENSP00000480216.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..361
                     /product="NF-kappa-B inhibitor epsilon"
                     /note="ikB-E; ikB-epsilon; NF-kappa-BIE; ikappaBepsilon;
                     I-kappa-B-epsilon; nuclear factor of kappa light
                     polypeptide gene enhancer in B-cells inhibitor, epsilon"
                     /calculated_mol_wt=38388
     Region          116..357
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          119..152
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          154..185
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          187..228
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          231..261
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(232,236..237,240..242,244..245,249,252,261,264,266,
                     270..271,274..276,278..279,283,286,295,297,299,303..304,
                     307..309,311..312,316,319,328)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          264..295
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          297..328
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..361
                     /gene="NFKBIE"
                     /gene_synonym="IKBE"
                     /coded_by="NM_004556.3:206..1291"
                     /db_xref="CCDS:CCDS34463.2"
                     /db_xref="GeneID:4794"
                     /db_xref="HGNC:HGNC:7799"
                     /db_xref="MIM:604548"
ORIGIN      
        1 msearkgpde aeesqydsgi eslrslrslp estsapasgp sdgspqpcth ppgpvkepqe
       61 kedadgerad stygssslty tlsllggpea edpaprlplp hvgalspqql ealtyisedg
      121 dtlvhlavih eapavllccl allpqevldi qnnlyqtalh lavhldqpga vralvlkgas
      181 ralqdrhgdt alhvacqrqh lacarclleg rpepgrgtsh sldlqlqnwq glaclhiatl
      241 qknqplmell lrngadidvq egtsgktalh lavetqergl vqfllqagaq vdarmlngct
      301 plhlaagrgl mgisstlcka gadsllrnve detpqdltee slvllpfddl kisgklllct
      361 d
//
LOCUS       NP_001307545             920 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 1 isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_001307545 XP_005261000
VERSION     NP_001307545.1
DBSOURCE    REFSEQ: accession NM_001320616.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Chatterjee,M., Saha,S., Dutta,N., Sinha,S. and Mukhopadhyay,K.
  TITLE     Kainate receptor subunit 1 (GRIK1) risk variants and GRIK1
            deficiency were detected in the Indian ADHD probands
  JOURNAL   Sci Rep 12 (1), 18449 (2022)
   PUBMED   36323684
  REMARK    GeneRIF: Kainate receptor subunit 1 (GRIK1) risk variants and GRIK1
            deficiency were detected in the Indian ADHD probands.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   3  (residues 1 to 920)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   4  (residues 1 to 920)
  AUTHORS   Hirbec,H., Francis,J.C., Lauri,S.E., Braithwaite,S.P., Coussen,F.,
            Mulle,C., Dev,K.K., Coutinho,V., Meyer,G., Isaac,J.T.,
            Collingridge,G.L. and Henley,J.M.
  TITLE     Rapid and differential regulation of AMPA and kainate receptors at
            hippocampal mossy fibre synapses by PICK1 and GRIP
  JOURNAL   Neuron 37 (4), 625-638 (2003)
   PUBMED   12597860
  REMARK    Erratum:[Neuron. 2003 May 22;38(4):673. Couthino V [corrected to
            Coutinho V]]
REFERENCE   5  (residues 1 to 920)
  AUTHORS   Barbon,A. and Barlati,S.
  TITLE     Genomic organization, proposed alternative splicing mechanisms, and
            RNA editing structure of GRIK1
  JOURNAL   Cytogenet Cell Genet 88 (3-4), 236-239 (2000)
   PUBMED   10828597
REFERENCE   6  (residues 1 to 920)
  AUTHORS   Bortolotto,Z.A., Clarke,V.R., Delany,C.M., Parry,M.C., Smolders,I.,
            Vignes,M., Ho,K.H., Miu,P., Brinton,B.T., Fantaske,R., Ogden,A.,
            Gates,M., Ornstein,P.L., Lodge,D., Bleakman,D. and
            Collingridge,G.L.
  TITLE     Kainate receptors are involved in synaptic plasticity
  JOURNAL   Nature 402 (6759), 297-301 (1999)
   PUBMED   10580501
REFERENCE   7  (residues 1 to 920)
  AUTHORS   Clarke,V.R., Ballyk,B.A., Hoo,K.H., Mandelzys,A., Pellizzari,A.,
            Bath,C.P., Thomas,J., Sharpe,E.F., Davies,C.H., Ornstein,P.L.,
            Schoepp,D.D., Kamboj,R.K., Collingridge,G.L., Lodge,D. and
            Bleakman,D.
  TITLE     A hippocampal GluR5 kainate receptor regulating inhibitory synaptic
            transmission
  JOURNAL   Nature 389 (6651), 599-603 (1997)
   PUBMED   9335499
REFERENCE   8  (residues 1 to 920)
  AUTHORS   Nutt,S.L. and Kamboj,R.K.
  TITLE     RNA editing of human kainate receptor subunits
  JOURNAL   Neuroreport 5 (18), 2625-2629 (1994)
   PUBMED   7696618
REFERENCE   9  (residues 1 to 920)
  AUTHORS   Roche,K.W., Raymond,L.A., Blackstone,C. and Huganir,R.L.
  TITLE     Transmembrane topology of the glutamate receptor subunit GluR6
  JOURNAL   J Biol Chem 269 (16), 11679-11682 (1994)
   PUBMED   8163463
REFERENCE   10 (residues 1 to 920)
  AUTHORS   Gregor,P., O'Hara,B.F., Yang,X. and Uhl,G.R.
  TITLE     Expression and novel subunit isoforms of glutamate receptor genes
            GluR5 and GluR6
  JOURNAL   Neuroreport 4 (12), 1343-1346 (1993)
   PUBMED   8260617
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK296404.1, BC111793.1,
            AJ249208.1 and AA404271.1.
            
            On Mar 2, 2016 this sequence version replaced XP_005261000.1.
            
            Summary: Glutamate receptors are the predominant excitatory
            neurotransmitter receptors in the mammalian brain and are activated
            in a variety of normal neurophysiologic processes. This gene
            product belongs to the kainate family of glutamate receptors, which
            are composed of four subunits and function as ligand-activated ion
            channels. The subunit encoded by this gene is subject to RNA
            editing (CAG->CGG; Q->R) within the second transmembrane domain,
            which is thought to alter the properties of ion flow. Alternative
            splicing, resulting in transcript variants encoding different
            isoforms, has been noted for this gene. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296404.1, SRR1803614.181862.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            undergoes RNA editing :: PMID: 7696618, 10828597
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..920
                     /product="glutamate receptor ionotropic, kainate 1 isoform
                     3 precursor"
                     /note="excitatory amino acid receptor 3; glutamate
                     receptor 5; glutamate receptor ionotropic, kainate 1;
                     GluK1(del_e2)"
                     /calculated_mol_wt=100866
     sig_peptide     1..30
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
                     /calculated_mol_wt=3510
     Region          38..431
                     /region_name="PBP1_iGluR_Kainate"
                     /note="N-terminal leucine-isoleucine-valine binding
                     protein (LIVBP)-like domain of the kainate receptors;
                     cd06382"
                     /db_xref="CDD:380605"
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            order(88..90,94,125,177,180,184,187,190..191,201..204)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380605"
     Site            276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            379
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            428
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            439
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Region          446..815
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            446
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            561
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            577..597
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P39086.1)"
     Site            654..674
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P39086.1)"
     Site            725
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P39086.1)"
     Site            761
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P39086.1)"
     Site            766
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            835..855
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P39086.1)"
     CDS             1..920
                     /gene="GRIK1"
                     /gene_synonym="EAA3; EEA3; GLR5; GluK1; gluR-5; GLUR5"
                     /coded_by="NM_001320616.2:497..3259"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS82658.1"
                     /db_xref="GeneID:2897"
                     /db_xref="HGNC:HGNC:4579"
                     /db_xref="MIM:138245"
ORIGIN      
        1 mehgtllaqp glwtrdtswa llyflcyilp qtapqvlrig gifetvenep vnveelafkf
       61 avtsinrnrt lmpnttltyd iqrinlfdsf easrracdql algvaalfgp shsssvsavq
      121 sicnalevph iqtrwkhpsv dnkdlfyinl ypdyaaisra ildlvlyynw ktvtvvyeds
      181 tglirlqeli kapsryniki kirqlpsgnk dakpllkemk kgkefyvifd cshetaaeil
      241 kqilfmgmmt eyyhyffttl dlfaldlely rysgvnmtgf rllnidnphv ssiiekwsme
      301 rlqapprpet glldgmmtte aalmydavym vaiashrasq ltvsslqchr hkpwrlgprf
      361 mnlikearwd gltghitfnk tnglrkdfdl diislkeegt ekaagevskh lykvwkkigi
      421 wnsnsglnmt dsnkdkssni tdslanrtli vttileepyv myrksdkply gndrfegycl
      481 dllkelsnil gfiydvklvp dgkygaqndk gewngmvkel idhradlava pltityvrek
      541 vidfskpfmt lgisilyrkp ngtnpgvfsf lnplspdiwm yvllaclgvs cvlfviarft
      601 pyewynphpc npdsdvvenn ftllnsfwfg vgalmqqgse lmpkalstri vggiwwfftl
      661 iiissytanl aafltverme spidsaddla kqtkieygav rdgstmtffk kskistyekm
      721 wafmssrqqt alvrnsdegi qrvlttdyal lmestsieyv tqrncnltqi gglidskgyg
      781 vgtpigspyr dkitiailql qeegklhmmk ekwwrgngcp eednkeasal gveniggifi
      841 vlaaglvlsv fvaigefiyk srknndieqc lsfnaimeel gislknqkki kkksrtkgks
      901 sftsiltchq rrtqrketva
//
LOCUS       NP_000446                433 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase STK11 isoform 1 [Homo sapiens].
ACCESSION   NP_000446
VERSION     NP_000446.1
DBSOURCE    REFSEQ: accession NM_000455.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Hou,J., Mei,K., Wang,D., Ke,S., Chen,X., Shang,J., Li,G., Gao,Y.,
            Xiong,H., Zhang,H., Chen,L., Zhang,W., Deng,Y., Hong,X., Liu,D.A.,
            Hu,T., Guo,W. and Zhan,Y.Y.
  TITLE     TGM1/3-mediated transamidation of Exo70 promotes tumor metastasis
            upon LKB1 inactivation
  JOURNAL   Cell Rep 43 (8), 114604 (2024)
   PUBMED   39146185
  REMARK    GeneRIF: TGM1/3-mediated transamidation of Exo70 promotes tumor
            metastasis upon LKB1 inactivation.
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Principe,D.R., Pasquinelli,M.M., Nguyen,R.H., Munshi,H.G.,
            Hulbert,A., Aissa,A.F. and Weinberg,F.
  TITLE     Loss of STK11 Suppresses Lipid Metabolism and Attenuates
            KRAS-Induced Immunogenicity in Patients with Non-Small Cell Lung
            Cancer
  JOURNAL   Cancer Res Commun 4 (8), 2282-2294 (2024)
   PUBMED   39113608
  REMARK    GeneRIF: Loss of STK11 Suppresses Lipid Metabolism and Attenuates
            KRAS-Induced Immunogenicity in Patients with Non-Small Cell Lung
            Cancer.
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Wang,X., Li,Y., Zhang,J., Liu,C., Deng,A. and Li,J.
  TITLE     Genetic variation at a splicing branch point in intron 7 of STK11:
            a rare variant decreasing its expression in a Chinese family with
            Peutz-Jeghers syndrome
  JOURNAL   World J Surg Oncol 22 (1), 202 (2024)
   PUBMED   39080663
  REMARK    GeneRIF: Genetic variation at a splicing branch point in intron 7
            of STK11: a rare variant decreasing its expression in a Chinese
            family with Peutz-Jeghers syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Liu,M., Gu,L., Zhang,Y., Li,Y., Zhang,L., Xin,Y., Wang,Y. and
            Xu,Z.X.
  TITLE     LKB1 inhibits telomerase activity resulting in cellular senescence
            through histone lactylation in lung adenocarcinoma
  JOURNAL   Cancer Lett 595, 217025 (2024)
   PUBMED   38844063
  REMARK    GeneRIF: LKB1 inhibits telomerase activity resulting in cellular
            senescence through histone lactylation in lung adenocarcinoma.
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Bignell,G.R., Barfoot,R., Seal,S., Collins,N., Warren,W. and
            Stratton,M.R.
  TITLE     Low frequency of somatic mutations in the LKB1/Peutz-Jeghers
            syndrome gene in sporadic breast cancer
  JOURNAL   Cancer Res 58 (7), 1384-1386 (1998)
   PUBMED   9537235
REFERENCE   7  (residues 1 to 433)
  AUTHORS   Hemminki,A., Markie,D., Tomlinson,I., Avizienyte,E., Roth,S.,
            Loukola,A., Bignell,G., Warren,W., Aminoff,M., Hoglund,P.,
            Jarvinen,H., Kristo,P., Pelin,K., Ridanpaa,M., Salovaara,R.,
            Toro,T., Bodmer,W., Olschwang,S., Olsen,A.S., Stratton,M.R., de la
            Chapelle,A. and Aaltonen,L.A.
  TITLE     A serine/threonine kinase gene defective in Peutz-Jeghers syndrome
  JOURNAL   Nature 391 (6663), 184-187 (1998)
   PUBMED   9428765
REFERENCE   8  (residues 1 to 433)
  AUTHORS   Jenne,D.E., Reimann,H., Nezu,J., Friedel,W., Loff,S., Jeschke,R.,
            Muller,O., Back,W. and Zimmer,M.
  TITLE     Peutz-Jeghers syndrome is caused by mutations in a novel serine
            threonine kinase
  JOURNAL   Nat Genet 18 (1), 38-43 (1998)
   PUBMED   9425897
REFERENCE   9  (residues 1 to 433)
  AUTHORS   Hemminki,A., Tomlinson,I., Markie,D., Jarvinen,H., Sistonen,P.,
            Bjorkqvist,A.M., Knuutila,S., Salovaara,R., Bodmer,W., Shibata,D.,
            de la Chapelle,A. and Aaltonen,L.A.
  TITLE     Localization of a susceptibility locus for Peutz-Jeghers syndrome
            to 19p using comparative genomic hybridization and targeted linkage
            analysis
  JOURNAL   Nat Genet 15 (1), 87-90 (1997)
   PUBMED   8988175
REFERENCE   10 (residues 1 to 433)
  AUTHORS   McGarrity,T.J., Amos,C.I. and Baker,M.J.
  TITLE     Peutz-Jeghers Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301443
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011544.6, BU174122.1,
            BQ222023.1, BC007981.2, BC019334.1, BU739451.1 and BM993274.1.
            
            Summary: The protein encoded by this gene is a serine/threonine
            kinase that regulates cell polarity and energy metabolism and
            functions as a tumor suppressor. Mutations in this gene have been
            associated with the autosomal dominant Peutz-Jeghers syndrome, as
            well as with skin, pancreatic, and testicular cancers. [provided by
            RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC019334.1, AF035625.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326873.12/ ENSP00000324856.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..433
                     /product="serine/threonine-protein kinase STK11 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase 11;
                     polarization-related protein LKB1; renal carcinoma antigen
                     NY-REN-19; serine/threonine-protein kinase LKB1; liver
                     kinase B1; serine/threonine-protein kinase STK11"
                     /calculated_mol_wt=48505
     mat_peptide     1..430
                     /product="Serine/threonine-protein kinase STK11.
                     /id=PRO_0000086699"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15831.1)"
                     /calculated_mol_wt=48252
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15831.1)"
     Site            44
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:18687677; propagated from
                     UniProtKB/Swiss-Prot (Q15831.1)"
     Region          45..90
                     /region_name="Sufficient for interaction with SIRT1.
                     /evidence=ECO:0000269|PubMed:18687677"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15831.1)"
     Site            48
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:18687677; propagated from
                     UniProtKB/Swiss-Prot (Q15831.1)"
     Region          55..309
                     /region_name="STKc_LKB1"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Liver Kinase B1; cd14119"
                     /db_xref="CDD:271021"
     Site            order(55..59,63,76,78,111,129..132,136,138,176,178,
                     180..181,183,194,197,215..218)
                     /site_type="active"
                     /db_xref="CDD:271021"
     Site            order(55..59,63,76,78,111,129..132,136,176,178,180..181,
                     183,194)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271021"
     Site            order(59,136,138,176,178,180,197,215..218)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271021"
     Site            order(70..74,106,186..187)
                     /site_type="other"
                     /note="STRAD interface [polypeptide binding]"
                     /db_xref="CDD:271021"
     Site            96
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:18687677; propagated from
                     UniProtKB/Swiss-Prot (Q15831.1)"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:18687677; propagated from
                     UniProtKB/Swiss-Prot (Q15831.1)"
     Site            order(100,165,168..169,171,201..207,301,307)
                     /site_type="other"
                     /note="MO25 interface [polypeptide binding]"
                     /db_xref="CDD:271021"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:11430832; propagated from
                     UniProtKB/Swiss-Prot (Q15831.1)"
     Site            193..218
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271021"
     Site            296
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:18687677; propagated from
                     UniProtKB/Swiss-Prot (Q15831.1)"
     Site            311
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:18687677; propagated from
                     UniProtKB/Swiss-Prot (Q15831.1)"
     Region          312..331
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15831.1)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTK7; propagated from
                     UniProtKB/Swiss-Prot (Q15831.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12805220; propagated from
                     UniProtKB/Swiss-Prot (Q15831.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ATM and autocatalysis.
                     /evidence=ECO:0000269|PubMed:12805220; propagated from
                     UniProtKB/Swiss-Prot (Q15831.1)"
     Region          397..433
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15831.1)"
     Site            399
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23612973; propagated from
                     UniProtKB/Swiss-Prot (Q15831.1)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15831.1)"
     Site            416
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:18687677; propagated from
                     UniProtKB/Swiss-Prot (Q15831.1)"
     Site            423
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:18687677; propagated from
                     UniProtKB/Swiss-Prot (Q15831.1)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis, PKA, PKC/PRKCZ and
                     RPS6KA1. /evidence=ECO:0000269|PubMed:18854309; propagated
                     from UniProtKB/Swiss-Prot (Q15831.1)"
     Site            430
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q15831.1)"
     Site            431
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:18687677; propagated from
                     UniProtKB/Swiss-Prot (Q15831.1)"
     CDS             1..433
                     /gene="STK11"
                     /gene_synonym="hLKB1; LKB1; PJS"
                     /coded_by="NM_000455.5:1137..2438"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45896.1"
                     /db_xref="GeneID:6794"
                     /db_xref="HGNC:HGNC:11389"
                     /db_xref="MIM:602216"
ORIGIN      
        1 mevvdpqqlg mftegelmsv gmdtfihrid steviyqprr krakligkyl mgdllgegsy
       61 gkvkevldse tlcrravkil kkkklrripn geanvkkeiq llrrlrhknv iqlvdvlyne
      121 ekqkmymvme ycvcgmqeml dsvpekrfpv cqahgyfcql idgleylhsq givhkdikpg
      181 nlllttggtl kisdlgvaea lhpfaaddtc rtsqgspafq ppeiangldt fsgfkvdiws
      241 agvtlynitt glypfegdni yklfenigkg syaipgdcgp plsdllkgml eyepakrfsi
      301 rqirqhswfr kkhppaeapv pippspdtkd rwrsmtvvpy ledlhgaded edlfdieddi
      361 iytqdftvpg qvpeeeashn gqrrglpkav cmngteaaql stksraegra pnparkacsa
      421 sskirrlsac kqq
//
LOCUS       NP_001193880             465 aa            linear   PRI 21-NOV-2025
DEFINITION  monocarboxylate transporter 4 [Homo sapiens].
ACCESSION   NP_001193880
VERSION     NP_001193880.1
DBSOURCE    REFSEQ: accession NM_001206951.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Yu,T., Liu,Z., Tao,Q., Xu,X., Li,X., Li,Y., Chen,M., Liu,R.,
            Chen,D., Wu,M. and Yu,J.
  TITLE     Targeting tumor-intrinsic SLC16A3 to enhance anti-PD-1 efficacy via
            tumor immune microenvironment reprogramming
  JOURNAL   Cancer Lett 589, 216824 (2024)
   PUBMED   38522774
  REMARK    GeneRIF: Targeting tumor-intrinsic SLC16A3 to enhance anti-PD-1
            efficacy via tumor immune microenvironment reprogramming.
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Li,Q., Li,Z., Li,J., Qin,X., Wu,F. and Chen,C.
  TITLE     Bone Morphogenetic Protein-4 Promotes Phenotypic Modulation via
            SMAD-4/MCT-4 Axis in Vascular Smooth Muscle Cells
  JOURNAL   J Vasc Res 61 (3), 99-108 (2024)
   PUBMED   38151007
  REMARK    GeneRIF: Bone Morphogenetic Protein-4 Promotes Phenotypic
            Modulation via SMAD-4/MCT-4 Axis in Vascular Smooth Muscle Cells.
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Mukai,Y., Yamaguchi,A., Sakuma,T., Nadai,T., Furugen,A., Narumi,K.
            and Kobayashi,M.
  TITLE     Involvement of SLC16A1/MCT1 and SLC16A3/MCT4 in l-lactate transport
            in the hepatocellular carcinoma cell line
  JOURNAL   Biopharm Drug Dispos 43 (5), 183-191 (2022)
   PUBMED   36104287
  REMARK    GeneRIF: Involvement of SLC16A1/MCT1 and SLC16A3/MCT4 in l-lactate
            transport in the hepatocellular carcinoma cell line.
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Manning Fox,J.E., Meredith,D. and Halestrap,A.P.
  TITLE     Characterisation of human monocarboxylate transporter 4
            substantiates its role in lactic acid efflux from skeletal muscle
  JOURNAL   J Physiol 529 Pt 2 (Pt 2), 285-293 (2000)
   PUBMED   11101640
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Kirk,P., Wilson,M.C., Heddle,C., Brown,M.H., Barclay,A.N. and
            Halestrap,A.P.
  TITLE     CD147 is tightly associated with lactate transporters MCT1 and MCT4
            and facilitates their cell surface expression
  JOURNAL   EMBO J 19 (15), 3896-3904 (2000)
   PUBMED   10921872
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Halestrap,A.P. and Price,N.T.
  TITLE     The proton-linked monocarboxylate transporter (MCT) family:
            structure, function and regulation
  JOURNAL   Biochem J 343 Pt 2 (Pt 2), 281-299 (1999)
   PUBMED   10510291
  REMARK    Review article
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Price,N.T., Jackson,V.N. and Halestrap,A.P.
  TITLE     Cloning and sequencing of four new mammalian monocarboxylate
            transporter (MCT) homologues confirms the existence of a
            transporter family with an ancient past
  JOURNAL   Biochem J 329 (Pt 2) (Pt 2), 321-328 (1998)
   PUBMED   9425115
REFERENCE   10 (residues 1 to 465)
  AUTHORS   Cori,C.F.
  TITLE     The glucose-lactic acid cycle and gluconeogenesis
  JOURNAL   Curr Top Cell Regul 18, 377-387 (1981)
   PUBMED   7273846
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC132872.17.
            
            Summary: Lactic acid and pyruvate transport across plasma membranes
            is catalyzed by members of the proton-linked monocarboxylate
            transporter (MCT) family, which has been designated solute carrier
            family-16. Each MCT appears to have slightly different substrate
            and inhibitor specificities and transport kinetics, which are
            related to the metabolic requirements of the tissues in which it is
            found. The MCTs, which include MCT1 (SLC16A1; MIM 600682) and MCT2
            (SLC16A7; MIM 603654), are characterized by 12 predicted
            transmembrane domains (Price et al., 1998 [PubMed
            9425115]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (5) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, 3, 4, 5 and 6 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2600050.1,
                                           SRR18074968.387570.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..465
                     /product="monocarboxylate transporter 4"
                     /note="monocarboxylate transporter 3; solute carrier
                     family 16 (monocarboxylic acid transporters), member 3;
                     solute carrier family 16, member 3 (monocarboxylic acid
                     transporter 4); solute carrier family 16 (monocarboxylate
                     transporter), member 3"
                     /calculated_mol_wt=49338
     Site            18..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Region          21..406
                     /region_name="MFS_MCT3_4"
                     /note="Monocarboxylate transporters 9 and 14, and similar
                     proteins of the Major Facilitator Superfamily of
                     transporters; cd17430"
                     /db_xref="CDD:340988"
     Site            order(32..33,36..37,40,75,126..127,129..131,134,153,
                     156..157,160,235,238..239,242..244,247,274,278,331..332,
                     336,340,356,359..360,363..364,367)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340988"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            85..105
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            110..130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            180..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            228..248
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            265..285
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            295..315
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            318..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            352..372
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            385..405
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Region          419..438
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Region          423..441
                     /region_name="Basolateral sorting signal.
                     /evidence=ECO:0000269|PubMed:21199217"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15427.1)"
     Region          441..465
                     /region_name="Basolateral sorting signal.
                     /evidence=ECO:0000269|PubMed:21199217"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O15427.1)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O15427.1)"
     CDS             1..465
                     /gene="SLC16A3"
                     /gene_synonym="MCT 3; MCT 4; MCT-3; MCT-4; MCT3; MCT4"
                     /coded_by="NM_001206951.2:129..1526"
                     /db_xref="CCDS:CCDS11804.1"
                     /db_xref="GeneID:9123"
                     /db_xref="HGNC:HGNC:10924"
                     /db_xref="MIM:603877"
ORIGIN      
        1 mggavvdegp tgvkapdggw gwavlfgcfv itgfsyafpk avsvffkeli qefgigysdt
       61 awissillam lygtgplcsv cvnrfgcrpv mlvgglfasl gmvaasfcrs iiqvylttgv
      121 itglglalnf qpslimlnry fskrrpmang laaagspvfl calsplgqll qdrygwrggf
      181 lilgglllnc cvcaalmrpl vvtaqpgsgp prpsrrlldl svfrdrgfvl yavaasvmvl
      241 glfvppvfvv syakdlgvpd tkaaflltil gfidifarpa agfvaglgkv rpysvylfsf
      301 smffngladl agstagdygg lvvfciffgi sygmvgalqf evlmaivgth kfssaiglvl
      361 lmeavavlvg ppsggkllda thvymyvfil agaevltssl illlgnffci rkkpkepqpe
      421 vaaaeeeklh kppadsgvdl revehflkae pekngevvht petsv
//
LOCUS       NP_001243731             243 aa            linear   PRI 21-NOV-2025
DEFINITION  small ribosomal subunit protein uS3 isoform 1 [Homo sapiens].
ACCESSION   NP_001243731
VERSION     NP_001243731.1
DBSOURCE    REFSEQ: accession NM_001256802.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Jiang,Z., Yang,G., Wang,G., Wan,J., Zhang,Y., Song,W., Zhang,H.,
            Ni,J., Zhang,H., Luo,M., Wang,K. and Peng,B.
  TITLE     SEC14L3 knockdown inhibited clear cell renal cell carcinoma
            proliferation, metastasis and sunitinib resistance through an
            SEC14L3/RPS3/NFkappaB positive feedback loop
  JOURNAL   J Exp Clin Cancer Res 43 (1), 288 (2024)
   PUBMED   39425205
  REMARK    GeneRIF: SEC14L3 knockdown inhibited clear cell renal cell
            carcinoma proliferation, metastasis and sunitinib resistance
            through an SEC14L3/RPS3/NFkappaB positive feedback loop.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Havkin-Solomon,T., Itzhaki,E., Joffe,N., Reuven,N., Shaul,Y. and
            Dikstein,R.
  TITLE     Selective translational control of cellular and viral mRNAs by RPS3
            mRNA binding
  JOURNAL   Nucleic Acids Res 51 (9), 4208-4222 (2023)
   PUBMED   37070189
  REMARK    GeneRIF: Selective translational control of cellular and viral
            mRNAs by RPS3 mRNA binding.
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Ahn,W.S., Kim,H.D., Kim,T.S., Ahn,M.J., Park,Y.J. and Kim,J.
  TITLE     Phosphorylation of rpS3 by Lyn increases translation of Multi-Drug
            Resistance (MDR1) gene
  JOURNAL   BMB Rep 56 (5), 302-307 (2023)
   PUBMED   36724904
  REMARK    GeneRIF: Phosphorylation of rpS3 by Lyn increases translation of
            Multi-Drug Resistance (MDR1) gene.
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Kim,J., Chubatsu,L.S., Admon,A., Stahl,J., Fellous,R. and Linn,S.
  TITLE     Implication of mammalian ribosomal protein S3 in the processing of
            DNA damage
  JOURNAL   J Biol Chem 270 (23), 13620-13629 (1995)
   PUBMED   7775413
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Polakiewicz,R.D., Munroe,D.J., Sait,S.N., Tycowski,K.T.,
            Nowak,N.J., Shows,T.B., Housman,D.E. and Page,D.C.
  TITLE     Mapping of ribosomal protein S3 and internally nested snoRNA U15A
            gene to human chromosome 11q13.3-q13.5
  JOURNAL   Genomics 25 (2), 577-580 (1995)
   PUBMED   7789996
REFERENCE   8  (residues 1 to 243)
  AUTHORS   Pogue-Geile,K., Geiser,J.R., Shu,M., Miller,C., Wool,I.G.,
            Meisler,A.I. and Pipas,J.M.
  TITLE     Ribosomal protein genes are overexpressed in colorectal cancer:
            isolation of a cDNA clone encoding the human S3 ribosomal protein
  JOURNAL   Mol Cell Biol 11 (8), 3842-3849 (1991)
   PUBMED   1712897
REFERENCE   9  (residues 1 to 243)
  AUTHORS   Bommer,U.A., Lutsch,G., Stahl,J. and Bielka,H.
  TITLE     Eukaryotic initiation factors eIF-2 and eIF-3: interactions,
            structure and localization in ribosomal initiation complexes
  JOURNAL   Biochimie 73 (7-8), 1007-1019 (1991)
   PUBMED   1742346
  REMARK    Review article
REFERENCE   10 (residues 1 to 243)
  AUTHORS   Zhang,X.T., Tan,Y.M. and Tan,Y.H.
  TITLE     Isolation of a cDNA encoding human 40S ribosomal protein s3
  JOURNAL   Nucleic Acids Res 18 (22), 6689 (1990)
   PUBMED   2129557
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC034149.1, AA976344.1 and
            AW134501.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 40S subunit, where it forms part
            of the domain where translation is initiated. The protein belongs
            to the S3P family of ribosomal proteins. Studies of the mouse and
            rat proteins have demonstrated that the protein has an
            extraribosomal role as an endonuclease involved in the repair of
            UV-induced DNA damage. The protein appears to be located in both
            the cytoplasm and nucleus but not in the nucleolus. Higher levels
            of expression of this gene in colon adenocarcinomas and adenomatous
            polyps compared to adjacent normal colonic mucosa have been
            observed. This gene is co-transcribed with the small nucleolar RNA
            genes U15A and U15B, which are located in its first and fifth
            introns, respectively. As is typical for genes encoding ribosomal
            proteins, there are multiple processed pseudogenes of this gene
            dispersed through the genome. Multiple alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, May 2012].
            
            Transcript Variant: This variant (2) differs in the 3' UTR compared
            to variant 1. Variants 1 and 2 both encode the same protein
            (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.161325.1,
                                           SRR5189667.301710.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..243
                     /product="small ribosomal subunit protein uS3 isoform 1"
                     /EC_number="4.2.99.18"
                     /note="IMR-90 ribosomal protein S3; 40S ribosomal protein
                     S3; small ribosomal subunit protein uS3"
                     /calculated_mol_wt=26557
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.10,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Region          4..216
                     /region_name="PTZ00084"
                     /note="40S ribosomal protein S3; Provisional"
                     /db_xref="CDD:240260"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC/PRKCD.
                     /evidence=ECO:0000269|PubMed:19059439; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK.
                     /evidence=ECO:0000269|PubMed:15950189; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            62
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            64
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:19460357; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            65
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:19460357; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            67
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:19460357; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB.
                     /evidence=ECO:0000269|PubMed:20605787; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKB.
                     /evidence=ECO:0000269|PubMed:21399639; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Region          214..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23396.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1 and PKC/PRKCD.
                     /evidence=ECO:0000269|PubMed:19059439,
                     ECO:0000269|PubMed:21871177, ECO:0000269|Ref.12,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16807684; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     CDS             1..243
                     /gene="RPS3"
                     /gene_synonym="S3; uS3"
                     /coded_by="NM_001256802.2:31..762"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS8236.1"
                     /db_xref="GeneID:6188"
                     /db_xref="HGNC:HGNC:10420"
                     /db_xref="MIM:600454"
ORIGIN      
        1 mavqiskkrk fvadgifkae lnefltrela edgysgvevr vtptrteiii latrtqnvlg
       61 ekgrrirelt avvqkrfgfp egsvelyaek vatrglcaia qaeslrykll gglavrracy
      121 gvlrfimesg akgcevvvsg klrgqraksm kfvdglmihs gdpvnyyvdt avrhvllrqg
      181 vlgikvkiml pwdptgkigp kkplpdhvsi vepkdeilpt tpiseqkggk peppampqpv
      241 pta
//
LOCUS       NP_001293084             448 aa            linear   PRI 21-NOV-2025
DEFINITION  T-complex protein 1 subunit epsilon isoform d [Homo sapiens].
ACCESSION   NP_001293084
VERSION     NP_001293084.1
DBSOURCE    REFSEQ: accession NM_001306155.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Wu,S. and Peng,L.
  TITLE     Increased CCT5 expression is a potential unfavourable factor
            promoting the growth of nasopharyngeal carcinoma
  JOURNAL   J Int Med Res 52 (9), 3000605241271754 (2024)
   PUBMED   39286844
  REMARK    GeneRIF: Increased CCT5 expression is a potential unfavourable
            factor promoting the growth of nasopharyngeal carcinoma.
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Scalia,F., Lo Bosco,G., Paladino,L., Vitale,A.M., Noori,L., Conway
            de Macario,E., Macario,A.J.L., Bucchieri,F., Cappello,F. and Lo
            Celso,F.
  TITLE     Structural and Dynamic Disturbances Revealed by Molecular Dynamics
            Simulations Predict the Impact on Function of CCT5 Chaperonin
            Mutations Associated with Rare Severe Distal Neuropathies
  JOURNAL   Int J Mol Sci 24 (3), 2018 (2023)
   PUBMED   36768350
  REMARK    GeneRIF: Structural and Dynamic Disturbances Revealed by Molecular
            Dynamics Simulations Predict the Impact on Function of CCT5
            Chaperonin Mutations Associated with Rare Severe Distal
            Neuropathies.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Sergeeva,O.A., Tran,M.T., Haase-Pettingell,C. and King,J.A.
  TITLE     Biochemical characterization of mutants in chaperonin proteins CCT4
            and CCT5 associated with hereditary sensory neuropathy
  JOURNAL   J Biol Chem 289 (40), 27470-27480 (2014)
   PUBMED   25124038
  REMARK    GeneRIF: H147R CCT5 was not as efficient in chaperoning these
            substrates as wild type CCT5.
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Bouhouche,A., Benomar,A., Bouslam,N., Chkili,T. and Yahyaoui,M.
  TITLE     Mutation in the epsilon subunit of the cytosolic
            chaperonin-containing t-complex peptide-1 (Cct5) gene causes
            autosomal recessive mutilating sensory neuropathy with spastic
            paraplegia
  JOURNAL   J Med Genet 43 (5), 441-443 (2006)
   PUBMED   16399879
  REMARK    GeneRIF: A missense mutation within the CCT5 gene is associated
            with autosomal recessive mutilating sensory neuropathy with spastic
            paraplegia.
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Roperch,J.P., Lethrone,F., Prieur,S., Piouffre,L., Israeli,D.,
            Tuynder,M., Nemani,M., Pasturaud,P., Gendron,M.C., Dausset,J.,
            Oren,M., Amson,R.B. and Telerman,A.
  TITLE     SIAH-1 promotes apoptosis and tumor suppression through a network
            involving the regulation of protein folding, unfolding, and
            trafficking: identification of common effectors with p53 and
            p21(Waf1)
  JOURNAL   Proc Natl Acad Sci U S A 96 (14), 8070-8073 (1999)
   PUBMED   10393949
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Liou,A.K. and Willison,K.R.
  TITLE     Elucidation of the subunit orientation in CCT (chaperonin
            containing TCP1) from the subunit composition of CCT
            micro-complexes
  JOURNAL   EMBO J 16 (14), 4311-4316 (1997)
   PUBMED   9250675
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Roobol,A., Holmes,F.E., Hayes,N.V., Baines,A.J. and Carden,M.J.
  TITLE     Cytoplasmic chaperonin complexes enter neurites developing in vitro
            and differ in subunit composition within single cells
  JOURNAL   J Cell Sci 108 (Pt 4), 1477-1488 (1995)
   PUBMED   7615668
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Kubota,H., Hynes,G., Carne,A., Ashworth,A. and Willison,K.
  TITLE     Identification of six Tcp-1-related genes encoding divergent
            subunits of the TCP-1-containing chaperonin
  JOURNAL   Curr Biol 4 (2), 89-99 (1994)
   PUBMED   7953530
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB449481.1, AC012640.12,
            AK302383.1 and FJ224303.1.
            
            Summary: The protein encoded by this gene is a molecular chaperone
            that is a member of the chaperonin containing TCP1 complex (CCT),
            also known as the TCP1 ring complex (TRiC). This complex consists
            of two identical stacked rings, each containing eight different
            proteins. Unfolded polypeptides enter the central cavity of the
            complex and are folded in an ATP-dependent manner. The complex
            folds various proteins, including actin and tubulin. Mutations in
            this gene cause hereditary sensory and autonomic neuropathy with
            spastic paraplegia (HSNSP). Alternative splicing results in
            multiple transcript variants. Related pseudogenes have been
            identified on chromosomes 5 and 13. [provided by RefSeq, Apr 2015].
            
            Transcript Variant: This variant (4) contains an alternate 5'
            terminal exon, resulting in an alternate 5' UTR and translation
            initiation at a downstream in-frame start codon, and it also lacks
            an in-frame exon in the 5' coding region, compared to variant 1.
            The encoded isoform (d) is shorter at the N-terminus, compared to
            isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302383.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.2"
     Protein         1..448
                     /product="T-complex protein 1 subunit epsilon isoform d"
                     /note="T-complex protein 1 subunit epsilon; epididymis
                     secretory protein Li 69; chaperonin containing TCP1,
                     subunit 5 (epsilon); chaperonin containing T-complex
                     polypeptide 1 subunit 5"
                     /calculated_mol_wt=49395
     Region          1..442
                     /region_name="TCP1_epsilon"
                     /note="TCP-1 (CTT or eukaryotic type II) chaperonin
                     family, epsilon subunit. Chaperonins are involved in
                     productive folding of proteins. They share a common
                     general morphology, a double toroid of 2 stacked rings. In
                     contrast to bacterial group I chaperonins...; cd03339"
                     /db_xref="CDD:239455"
     Site            order(14..16,78,311,329,369,413,415)
                     /site_type="other"
                     /note="ATP/Mg binding site [chemical binding]"
                     /db_xref="CDD:239455"
     Site            order(349,367,376,378..379,382)
                     /site_type="active"
                     /note="stacking interactions [active]"
                     /db_xref="CDD:239455"
     CDS             1..448
                     /gene="CCT5"
                     /gene_synonym="CCT-epsilon; CCTE; HEL-S-69; HSNSP;
                     PNAS-102; TCP-1-epsilon"
                     /coded_by="NM_001306155.2:367..1713"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS82990.1"
                     /db_xref="GeneID:22948"
                     /db_xref="HGNC:HGNC:1618"
                     /db_xref="MIM:610150"
ORIGIN      
        1 maakavantm rtslgpnvla galleeaeql ldrgihpiri adgyeqaarv aiehldkisd
       61 svlvdikdte pliqtakttl gskvvnschr qmaeiavnav ltvadmerrd vdfelikveg
      121 kvggrledtk likgvivdkd fshpqmpkkv edakiailtc pfeppkpktk hkldvtsved
      181 ykalqkyeke kfeemiqqik etganlaicq wgfddeanhl llqnnlpavr wvggpeieli
      241 aiatggrivp rfseltaekl gfaglvqeis fgttkdkmlv ieqcknsrav tifirggnkm
      301 iieeakrslh dalcvirnli rdnrvvyggg aaeiscalav sqeadkcptl eqyamrafad
      361 alevipmals ensgmnpiqt mtevrarqvk emnpalgidc lhkgtndmkq qhvietligk
      421 kqqislatqm vrmilkiddi rkpgesee
//
LOCUS       NP_001265629             114 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerases I, II, and III subunit RPABC3 isoform
            3 [Homo sapiens].
ACCESSION   NP_001265629
VERSION     NP_001265629.1
DBSOURCE    REFSEQ: accession NM_001278700.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Zhao,D., Liu,W., Chen,K., Wu,Z., Yang,H. and Xu,Y.
  TITLE     Structure of the human RNA polymerase I elongation complex
  JOURNAL   Cell Discov 7 (1), 97 (2021)
   PUBMED   34671025
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   6  (residues 1 to 114)
  AUTHORS   Kato,H., Sumimoto,H., Pognonec,P., Chen,C.H., Rosen,C.A. and
            Roeder,R.G.
  TITLE     HIV-1 Tat acts as a processivity factor in vitro in conjunction
            with cellular elongation factors
  JOURNAL   Genes Dev 6 (4), 655-666 (1992)
   PUBMED   1559613
REFERENCE   7  (residues 1 to 114)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
REFERENCE   8  (residues 1 to 114)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 114)
  AUTHORS   Southgate,C., Zapp,M.L. and Green,M.R.
  TITLE     Activation of transcription by HIV-1 Tat protein tethered to
            nascent RNA through another protein
  JOURNAL   Nature 345 (6276), 640-642 (1990)
   PUBMED   2190099
REFERENCE   10 (residues 1 to 114)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078797.20, HY178178.1,
            BM541682.1, Z49199.1, AA431357.1 and BX283032.1.
            
            Summary: The three eukaryotic RNA polymerases are complex
            multisubunit enzymes that play a central role in the transcription
            of nuclear genes. This gene encodes an essential and highly
            conserved subunit of RNA polymerase II that is shared by the other
            two eukaryotic DNA-directed RNA polymerases, I and III. Alternative
            splicing results in multiple transcript variants of this gene.
            [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (4) contains an alternate 5'
            terminal exon, initiates translation at a downstream start codon
            and uses an alternate splice site in the 3' coding region,
            resulting in a frameshift, compared to variant 1. Variants 3 and 4
            encode the same isoform (3), which is shorter and has a distinct
            C-terminus, compared to isoform 1. Variants 3, 4, and 15-18 all
            encode the same isoform (3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM541682.1, HY116571.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..114
                     /product="DNA-directed RNA polymerases I, II, and III
                     subunit RPABC3 isoform 3"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerases I, II, and III subunit
                     RPABC3; RPB8 homolog; DNA-directed RNA polymerase II
                     subunit H; DNA-directed RNA polymerases I, II, and III
                     17.1 kDa polypeptide; polymerase (RNA) II (DNA directed)
                     polypeptide H; polymerase (RNA) II subunit H"
                     /calculated_mol_wt=12827
     Region          <1..111
                     /region_name="RPOL8c"
                     /note="RNA polymerase subunit 8; smart00658"
                     /db_xref="CDD:197821"
     CDS             1..114
                     /gene="POLR2H"
                     /gene_synonym="RPABC3; RPB17; RPB8"
                     /coded_by="NM_001278700.2:473..817"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS63861.1"
                     /db_xref="GeneID:5437"
                     /db_xref="HGNC:HGNC:9195"
                     /db_xref="MIM:606023"
ORIGIN      
        1 mdlildvniq iypvdlgdkf rlviastlye dgtlddgeyn ptddrpsrad qfeyvmygkv
       61 yriegdetst eaatrlsayv syggllmrlq gdannlhgfe vdsrvyllmk klaf
//
LOCUS       NP_001362211             540 aa            linear   PRI 21-NOV-2025
DEFINITION  complement factor I isoform 8 preproprotein [Homo sapiens].
ACCESSION   NP_001362211 XP_016863654
VERSION     NP_001362211.1
DBSOURCE    REFSEQ: accession NM_001375282.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Moreno,R. and Broderick,L.
  TITLE     Complement factor I deficiency: Diverse phenotypes
  JOURNAL   J Allergy Clin Immunol 156 (2), 305-307 (2025)
   PUBMED   40127737
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Schwotzer,N., Fakhouri,F., Martins,P.V., Delmas,Y., Caillard,S.,
            Zuber,J., Moranne,O., Mesnard,L., Fremeaux-Bacchi,V. and
            El-Sissy,C.
  TITLE     Hot Spot of Complement Factor I Rare Variant p.Ile357Met in
            Patients With Hemolytic Uremic Syndrome
  JOURNAL   Am J Kidney Dis 84 (2), 244-249 (2024)
   PUBMED   38423159
  REMARK    GeneRIF: Hot Spot of Complement Factor I Rare Variant p.Ile357Met
            in Patients With Hemolytic Uremic Syndrome.
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Felberg,A., Bienkowski,M., Stokowy,T., Myszczynski,K.,
            Polakiewicz,Z., Kitowska,K., Sadej,R., Mohlin,F., Kuzniewska,A.,
            Kowalska,D., Stasilojc,G., Jongerius,I., Spaapen,R.,
            Mesa-Guzman,M., Montuenga,L.M., Blom,A.M., Pio,R. and Okroj,M.
  TITLE     Elevated expression of complement factor I in lung cancer cells
            associates with shorter survival-Potentially via non-canonical
            mechanism
  JOURNAL   Transl Res 269, 1-13 (2024)
   PUBMED   38395390
  REMARK    GeneRIF: Elevated expression of complement factor I in lung cancer
            cells associates with shorter survival-Potentially via
            non-canonical mechanism.
REFERENCE   4  (residues 1 to 540)
  AUTHORS   Massey,V., Nguyen,C.E., Francois,T., De Bruycker,J.J., Bonnefoy,A.,
            Lapeyraque,A.L. and Decaluwe,H.
  TITLE     CNS Inflammation as the First Sign of Complement Factor I
            Deficiency: A Severe Myelitis Treated With Intense Immunotherapy
            and Eculizumab
  JOURNAL   Neurol Neuroimmunol Neuroinflamm 11 (2), e200191 (2024)
   PUBMED   38134378
  REMARK    GeneRIF: CNS Inflammation as the First Sign of Complement Factor I
            Deficiency.
REFERENCE   5  (residues 1 to 540)
  AUTHORS   van de Ven,J.P., Nilsson,S.C., Tan,P.L., Buitendijk,G.H.,
            Ristau,T., Mohlin,F.C., Nabuurs,S.B., Schoenmaker-Koller,F.E.,
            Smailhodzic,D., Campochiaro,P.A., Zack,D.J., Duvvari,M.R.,
            Bakker,B., Paun,C.C., Boon,C.J., Uitterlinden,A.G., Liakopoulos,S.,
            Klevering,B.J., Fauser,S., Daha,M.R., Katsanis,N., Klaver,C.C.,
            Blom,A.M., Hoyng,C.B. and den Hollander,A.I.
  TITLE     A functional variant in the CFI gene confers a high risk of
            age-related macular degeneration
  JOURNAL   Nat Genet 45 (7), 813-817 (2013)
   PUBMED   23685748
  REMARK    GeneRIF: these findings demonstrate that rare, highly penetrant
            mutations in CFI contribute to the genetic burden of age-related
            macular degeneration.
REFERENCE   6  (residues 1 to 540)
  AUTHORS   Martin,B. and Smith,R.J.H.
  TITLE     C3 Glomerulopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301598
REFERENCE   7  (residues 1 to 540)
  AUTHORS   Noris,M., Bresin,E., Mele,C. and Remuzzi,G.
  TITLE     Genetic Atypical Hemolytic-Uremic Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301541
REFERENCE   8  (residues 1 to 540)
  AUTHORS   DiScipio,R.G.
  TITLE     Ultrastructures and interactions of complement factors H and I
  JOURNAL   J Immunol 149 (8), 2592-2599 (1992)
   PUBMED   1401896
REFERENCE   9  (residues 1 to 540)
  AUTHORS   Shiang,R., Murray,J.C., Morton,C.C., Buetow,K.H., Wasmuth,J.J.,
            Olney,A.H., Sanger,W.G. and Goldberger,G.
  TITLE     Mapping of the human complement factor I gene to 4q25
  JOURNAL   Genomics 4 (1), 82-86 (1989)
   PUBMED   2563353
REFERENCE   10 (residues 1 to 540)
  AUTHORS   Catterall,C.F., Lyons,A., Sim,R.B., Day,A.J. and Harris,T.J.
  TITLE     Characterization of primary amino acid sequence of human complement
            control protein factor I from an analysis of cDNA clones
  JOURNAL   Biochem J 242 (3), 849-856 (1987)
   PUBMED   2954545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC126283.3 and AC004067.1.
            
            On Oct 19, 2019 this sequence version replaced XP_016863654.1.
            
            Summary: This gene encodes a serine proteinase that is essential
            for regulating the complement cascade. The encoded preproprotein is
            cleaved to produce both heavy and light chains, which are linked by
            disulfide bonds to form a heterodimeric glycoprotein. This
            heterodimer can cleave and inactivate the complement components C4b
            and C3b, and it prevents the assembly of the C3 and C5 convertase
            enzymes. Defects in this gene cause complement factor I deficiency,
            an autosomal recessive disease associated with a susceptibility to
            pyogenic infections. Mutations in this gene have been associated
            with a predisposition to atypical hemolytic uremic syndrome, a
            disease characterized by acute renal failure, microangiopathic
            hemolytic anemia and thrombocytopenia. Primary glomerulonephritis
            with immune deposits and age-related macular degeneration are other
            conditions associated with mutations of this gene. [provided by
            RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2954050.1,
                                           SRR14038194.3083854.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..540
                     /product="complement factor I isoform 8 preproprotein"
                     /EC_number="3.4.21.45"
                     /note="C3b-inactivator; Konglutinogen-activating factor;
                     complement factor I heavy chain; complement component I;
                     C3B/C4B inactivator; complement control protein factor I;
                     light chain of factor I"
                     /calculated_mol_wt=58862
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2281
     Region          43..108
                     /region_name="FIMAC"
                     /note="factor I membrane attack complex; smart00057"
                     /db_xref="CDD:214493"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Region          114..215
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     Region          224..256
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(227,235,246..247)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(239,242,246,252..253)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            249..253
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          257..293
                     /region_name="Ldl_recept_a"
                     /note="Low-density lipoprotein receptor domain class A;
                     pfam00057"
                     /db_xref="CDD:395011"
     Site            order(264,272,283..284)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(276,279,283,289..290)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            286..290
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          332..>504
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; smart00020"
                     /db_xref="CDD:214473"
     Site            333
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            457
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Site            487
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     CDS             1..540
                     /gene="CFI"
                     /gene_synonym="AHUS3; ARMD13; C3b-INA; C3BINA; FI; IF;
                     KAF"
                     /coded_by="NM_001375282.1:29..1651"
                     /note="isoform 8 preproprotein is encoded by transcript
                     variant 8"
                     /db_xref="GeneID:3426"
                     /db_xref="HGNC:HGNC:5394"
                     /db_xref="MIM:217030"
ORIGIN      
        1 mkllhvfllf lcfhlrfckv tytsqedlve kkclakkyth lscdkvfcqp wqrciegtcv
       61 cklpyqcpkn gtavcatnrr sfptycqqks leclhpgtkf lnngtctaeg kfsvslkhgn
      121 tdsegivevk lvdqdktmfi cksswsmrea nvacldlgfq qgadtqrrfk lsdlsinste
      181 clhvhcrgle tslaectftk rrtmgyqdfa dvvcytqkad spmddffqcv ngkyisqmka
      241 cdgindcgdq sdelcckacq gkgfhcksgv cipsqyqcng evdcitgede vgcaeeteil
      301 tadmdaerrr iksllpklsc gvknrmhirr krivggkraq lgdlpwqvai kdasgitcgg
      361 iyiggcwilt aahclraskt hryqiwttvv dwihpdlkri vieyvdriif henynagtyq
      421 ndialiemkk dgnkkdcelp rsipacvpws pylfqpndtc ivsgwgrekd nervfslqwg
      481 evklisncsk fygnrfyeke mecaesrsvp qagvqwcnls slqhpstswv qvillppppe
//
LOCUS       NP_001290198            1167 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase II subunit RPB2 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001290198
VERSION     NP_001290198.1
DBSOURCE    REFSEQ: accession NM_001303269.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1167)
  AUTHORS   Lin,H., Cui,Z., E,T., Xu,H., Wang,D., Wang,P., Ruan,X., Liu,L. and
            Xue,Y.
  TITLE     M6A-methylated circPOLR2B forms an R-loop and regulates the
            biological behavior of glioma stem cells through positive feedback
            loops
  JOURNAL   Cell Death Dis 15 (8), 554 (2024)
   PUBMED   39090090
  REMARK    GeneRIF: M6A-methylated circPOLR2B forms an R-loop and regulates
            the biological behavior of glioma stem cells through positive
            feedback loops.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1167)
  AUTHORS   Li,X.L., Xie,Y., Chen,Y.L., Zhang,Z.M., Tao,Y.F., Li,G., Wu,D.,
            Wang,H.R., Zhuo,R., Pan,J.J., Yu,J.J., Jia,S.Q., Zhang,Z.,
            Feng,C.X., Wang,J.W., Fang,F., Qian,G.H., Lu,J., Hu,S.Y., Li,Z.H.
            and Pan,J.
  TITLE     The RNA polymerase II subunit B (RPB2) functions as a growth
            regulator in human glioblastoma
  JOURNAL   Biochem Biophys Res Commun 674, 170-182 (2023)
   PUBMED   37423037
  REMARK    GeneRIF: The RNA polymerase II subunit B (RPB2) functions as a
            growth regulator in human glioblastoma.
REFERENCE   3  (residues 1 to 1167)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1167)
  AUTHORS   Lykke-Andersen,S., Rouviere,J.O. and Jensen,T.H.
  TITLE     ARS2/SRRT: at the nexus of RNA polymerase II transcription,
            transcript maturation and quality control
  JOURNAL   Biochem Soc Trans 49 (3), 1325-1336 (2021)
   PUBMED   34060620
  REMARK    GeneRIF: ARS2/SRRT: at the nexus of RNA polymerase II
            transcription, transcript maturation and quality control.
            Review article
REFERENCE   5  (residues 1 to 1167)
  AUTHORS   Jishage,M., Yu,X., Shi,Y., Ganesan,S.J., Chen,W.Y., Sali,A.,
            Chait,B.T., Asturias,F.J. and Roeder,R.G.
  TITLE     Architecture of Pol II(G) and molecular mechanism of transcription
            regulation by Gdown1
  JOURNAL   Nat Struct Mol Biol 25 (9), 859-867 (2018)
   PUBMED   30190596
REFERENCE   6  (residues 1 to 1167)
  AUTHORS   Schaller,S., Grandemange,S., Shpakovski,G.V., Golemis,E.A.,
            Kedinger,C. and Vigneron,M.
  TITLE     Interactions between the full complement of human RNA polymerase II
            subunits
  JOURNAL   FEBS Lett 461 (3), 253-257 (1999)
   PUBMED   10567706
REFERENCE   7  (residues 1 to 1167)
  AUTHORS   Kershnar,E., Wu,S.Y. and Chiang,C.M.
  TITLE     Immunoaffinity purification and functional characterization of
            human transcription factor IIH and RNA polymerase II from clonal
            cell lines that conditionally express epitope-tagged subunits of
            the multiprotein complexes
  JOURNAL   J Biol Chem 273 (51), 34444-34453 (1998)
   PUBMED   9852112
REFERENCE   8  (residues 1 to 1167)
  AUTHORS   Acker,J., de Graaff,M., Cheynel,I., Khazak,V., Kedinger,C. and
            Vigneron,M.
  TITLE     Interactions between the human RNA polymerase II subunits
  JOURNAL   J Biol Chem 272 (27), 16815-16821 (1997)
   PUBMED   9201987
REFERENCE   9  (residues 1 to 1167)
  AUTHORS   Acker,J., Mattei,M.G., Wintzerith,M., Roeckel,N., Depetris,D.,
            Vigneron,M. and Kedinger,C.
  TITLE     Chromosomal localization of human RNA polymerase II subunit genes
  JOURNAL   Genomics 20 (3), 496-499 (1994)
   PUBMED   8034326
REFERENCE   10 (residues 1 to 1167)
  AUTHORS   Acker,J., Wintzerith,M., Vigneron,M. and Kedinger,C.
  TITLE     Primary structure of the second largest subunit of human RNA
            polymerase II (or B)
  JOURNAL   J Mol Biol 226 (4), 1295-1299 (1992)
   PUBMED   1518060
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK295132.1, BC023503.2 and
            AK294901.1.
            
            Summary: This gene encodes the second largest subunit of RNA
            polymerase II (Pol II), a DNA-dependent RNA polymerase that
            catalyzes the transcription of DNA into precursors of mRNA, snRNA
            and microRNA. This subunit and the largest subunit form opposite
            sides of the center cleft of Pol II. Deletion of the flap loop
            region of this subunit results in a decrease in the rate of
            transcriptional elongation. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Dec 2014].
            
            Transcript Variant: This variant (3) contains an alternate exon in
            its 5' UTR and initiates translation at an in-frame downstream
            start codon, compared to variant 1. This results in isoform 3,
            which has a shorter N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295132.1, SRR14038196.2946110.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1167
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..1167
                     /product="DNA-directed RNA polymerase II subunit RPB2
                     isoform 3"
                     /EC_number="2.7.7.6"
                     /EC_number="2.7.7.48"
                     /note="RNA polymerase II second largest subunit;
                     DNA-directed RNA polymerase II subunit RPB2; RNA
                     polymerase II subunit 2; RNA polymerase II subunit B2;
                     DNA-directed RNA polymerase II subunit B; DNA-directed RNA
                     polymerase II 140 kDa polypeptide; polymerase (RNA) II
                     (DNA directed) polypeptide B, 140kDa; polymerase (RNA) II
                     subunit B; 3'-5' exoribonuclease; RNA-directed RNA
                     polymerase II subunit RPB2"
                     /calculated_mol_wt=132926
     Region          20..1165
                     /region_name="Ricin_B_lectin"
                     /note="Ricin-type beta-trefoil lectin domain; cl47023"
                     /db_xref="CDD:481363"
     CDS             1..1167
                     /gene="POLR2B"
                     /gene_synonym="hRPB140; POL2RB; RPB2"
                     /coded_by="NM_001303269.2:290..3793"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS77915.1"
                     /db_xref="GeneID:5431"
                     /db_xref="HGNC:HGNC:9188"
                     /db_xref="MIM:180661"
ORIGIN      
        1 mqydedddei tpdlwqeacw ivissyfdek glvrqqldsf defiqmsvqr ivedappidl
       61 qaeaqhasge veeppryllk feqiylskpt hwerdgapsp mmpnearlrn ltysaplyvd
      121 itktvikege eqlqtqhqkt figkipimlr stycllnglt drdlcelnec pldpggyfii
      181 ngsekvliaq ekmatntvyv fakkdskyay tgecrsclen ssrptstiwv smlarggqga
      241 kksaigqriv atlpyikqev piiivfralg fvsdrdileh iiydfedpem memvkpslde
      301 afviqeqnva lnfigsrgak pgvtkekrik yakevlqkem lphvgvsdfc etkkayflgy
      361 mvhrlllaal grrelddrdh ygnkrldlag pllaflfrgm fknllkevri yaqkfidrgk
      421 dfnlelaikt riisdglkys latgnwgdqk kahqaragvs qvlnrltfas tlshlrrlns
      481 pigrdgklak prqlhntlwg mvcpaetpeg havglvknla lmayisvgsq pspileflee
      541 wsmenleeis paaiadatki fvngcwvgih kdpeqlmntl rklrrqmdii vsevsmirdi
      601 rereiriytd agricrplli vekqklllkk rhidqlkere ynnyswqdlv asgvveyidt
      661 leeetvmlam tpddlqekev aycstythce ihpsmilgvc asiipfpdhn qsprntyqsa
      721 mgkqamgvyi tnfhvrmdtl ahvlyypqkp lvttrsmeyl rfrelpagin sivaiasytg
      781 ynqedsvimn rsavdrgffr svfyrsykeq eskkgfdqee vfekptretc qgmrhaiydk
      841 ldddgliapg vrvsgddvii gktvtlpene delestnrry tkrdcstflr tsetgivdqv
      901 mvtlnqegyk fckirvrsvr ipqigdkfas rhgqkgtcgi qyrqedmpft cegitpdiii
      961 nphaipsrmt ighlieclqg kvsankgeig datpfndavn vqkisnllsd ygyhlrgnev
     1021 lyngftgrki tsqifigpty yqrlkhmvdd kihsrargpi qilnrqpmeg rsrdgglrfg
     1081 emerdcqiah gaaqflrerl feasdpyqvh vcnlcgimai antrthtyec rgcrnktqis
     1141 lvrmpyackl lfqelmsmsi aprmmsv
//
LOCUS       NP_003890                646 aa            linear   PRI 21-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 7 isoform a [Homo sapiens].
ACCESSION   NP_003890
VERSION     NP_003890.1
DBSOURCE    REFSEQ: accession NM_003899.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Kawase,N., Sugihara,A., Kajiwara,K., Hiroshima,M., Akamatsu,K.,
            Nada,S., Matsumoto,K., Ueda,M. and Okada,M.
  TITLE     SRC kinase activator CDCP1 promotes hepatocyte growth
            factor-induced cell migration/invasion of a subset of breast cancer
            cells
  JOURNAL   J Biol Chem 298 (3), 101630 (2022)
   PUBMED   35085554
  REMARK    GeneRIF: SRC kinase activator CDCP1 promotes hepatocyte growth
            factor-induced cell migration/invasion of a subset of breast cancer
            cells.
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Keum,S., Yang,S.J., Park,E., Kang,T., Choi,J.H., Jeong,J.,
            Hwang,Y.E., Kim,J.W., Park,D. and Rhee,S.
  TITLE     Beta-Pix-dynamin 2 complex promotes colorectal cancer progression
            by facilitating membrane dynamics
  JOURNAL   Cell Oncol (Dordr) 44 (6), 1287-1305 (2021)
   PUBMED   34582006
  REMARK    GeneRIF: Beta-Pix-dynamin 2 complex promotes colorectal cancer
            progression by facilitating membrane dynamics.
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 646)
  AUTHORS   Turner,C.E., Brown,M.C., Perrotta,J.A., Riedy,M.C.,
            Nikolopoulos,S.N., McDonald,A.R., Bagrodia,S., Thomas,S. and
            Leventhal,P.S.
  TITLE     Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin
            repeat, ARF-GAP protein: A role in cytoskeletal remodeling
  JOURNAL   J Cell Biol 145 (4), 851-863 (1999)
   PUBMED   10330411
REFERENCE   7  (residues 1 to 646)
  AUTHORS   Aghazadeh,B., Zhu,K., Kubiseski,T.J., Liu,G.A., Pawson,T., Zheng,Y.
            and Rosen,M.K.
  TITLE     Structure and mutagenesis of the Dbl homology domain
  JOURNAL   Nat Struct Biol 5 (12), 1098-1107 (1998)
   PUBMED   9846881
REFERENCE   8  (residues 1 to 646)
  AUTHORS   Bagrodia,S., Taylor,S.J., Jordon,K.A., Van Aelst,L. and
            Cerione,R.A.
  TITLE     A novel regulator of p21-activated kinases
  JOURNAL   J Biol Chem 273 (37), 23633-23636 (1998)
   PUBMED   9726964
REFERENCE   9  (residues 1 to 646)
  AUTHORS   Manser,E., Loo,T.H., Koh,C.G., Zhao,Z.S., Chen,X.Q., Tan,L.,
            Tan,I., Leung,T. and Lim,L.
  TITLE     PAK kinases are directly coupled to the PIX family of nucleotide
            exchange factors
  JOURNAL   Mol Cell 1 (2), 183-192 (1998)
   PUBMED   9659915
REFERENCE   10 (residues 1 to 646)
  AUTHORS   Oh,W.K., Yoo,J.C., Jo,D., Song,Y.H., Kim,M.G. and Park,D.
  TITLE     Cloning of a SH3 domain-containing proline-rich protein, p85SPR,
            and its localization in focal adhesion
  JOURNAL   Biochem Biophys Res Commun 235 (3), 794-798 (1997)
   PUBMED   9207241
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL353704.10, AL390754.18 and
            AL139086.12.
            
            Summary: This gene encodes a protein that belongs to a family of
            cytoplasmic proteins that activate the Ras-like family of Rho
            proteins by exchanging bound GDP for GTP. It forms a complex with
            the small GTP binding protein Rac1 and recruits Rac1 to membrane
            ruffles and to focal adhesions. Multiple alternatively spliced
            transcript variants encoding different isoforms have been observed
            for this gene. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (1) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and contains a different 3' coding
            region and 3' UTR, compared to variant 1. It initiates translation
            at a downstream start codon. Variants 1, 5, 6, 18, and 19 all
            encode isoform a (also known as p85Cool-1), which has a shorter
            N-terminus and a longer and distinct C-terminus, compared to
            isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D63476.1, SRR1803613.275647.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..646
                     /product="rho guanine nucleotide exchange factor 7 isoform
                     a"
                     /note="SH3 domain-containing proline-rich protein;
                     PAK-interacting exchange factor beta; Rho guanine
                     nucleotide exchange factor (GEF) 7"
                     /calculated_mol_wt=73009
     Region          10..63
                     /region_name="SH3_betaPIX"
                     /note="Src Homology 3 domain of beta-Pak Interactive
                     eXchange factor; cd12061"
                     /db_xref="CDD:212994"
     Site            order(15,17,20,23..24,39,41..43,54,56,58..59)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212994"
     Region          94..271
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(100,104,198,222..223,226..227,229..230,233..234,
                     237..238,241,267,271)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          302..400
                     /region_name="PH_Cool_Pix"
                     /note="Cloned out of library/PAK-interactive exchange
                     factor pleckstrin homology (PH) domain; cd01225"
                     /db_xref="CDD:269932"
     Region          460..550
                     /region_name="RhoGEF67_u2"
                     /note="Unstructured region two on RhoGEF 6 and 7;
                     pfam16614"
                     /db_xref="CDD:465200"
     Region          561..645
                     /region_name="betaPIX_CC"
                     /note="betaPIX coiled coil; pfam16523"
                     /db_xref="CDD:465158"
     CDS             1..646
                     /gene="ARHGEF7"
                     /gene_synonym="BETA-PIX; COOL-1; COOL1; Nbla10314; P50;
                     P50BP; P85; P85COOL1; P85SPR; PAK3; PIXB"
                     /coded_by="NM_003899.5:546..2486"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9521.1"
                     /db_xref="GeneID:8874"
                     /db_xref="HGNC:HGNC:15607"
                     /db_xref="MIM:605477"
ORIGIN      
        1 mtdnsnnqlv vrakfnfqqt nedelsfskg dvihvtrvee ggwwegtlng rtgwfpsnyv
       61 revkasekpv spksgtlksp pkgfdttain ksyynvvlqn ileteneysk elqtvlstyl
      121 rplqtsekls sanisylmgn leeicsfqqm lvqsleectk lpeaqqrvgg cflnlmpqmk
      181 tlyltycanh psavnvlteh seelgefmet kgasspgilv lttglskpfm rldkyptllk
      241 elerhmedyh tdrqdiqksm aafknlsaqc qevrkrkele lqilteairn wegddiktlg
      301 nvtymsqvli qcagseekne rylllfpnvl lmlsasprms gfiyqgklpt tgmtitkled
      361 senhrnafei sgsmierilv scnnqqdlqe wvehlqkqtk vtsvgnptik phsvpshtlp
      421 shpvtpsskh adskpapltp ayhtlphpsh hgtphttinw gpleppktpk pwslsclrpa
      481 pplrpsaalc ykedlskspk tmkkllpkrk perkpsdeef asrkstaale edaqilkvie
      541 ayctsaktrq tlnsssrkes apqvllpeee kiiveetksn gqtvieeksl vdtvyalkde
      601 vqelrqdnkk mkksleeeqr arkdleklvr kvlknmndpa wdetnl
//
LOCUS       NP_570824                206 aa            linear   PRI 21-NOV-2025
DEFINITION  synaptosomal-associated protein 25 isoform SNAP25B [Homo sapiens].
ACCESSION   NP_570824
VERSION     NP_570824.1
DBSOURCE    REFSEQ: accession NM_130811.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Wang,W., Gao,W., Gong,P., Song,W., Bu,X., Hou,J., Zhang,L. and
            Zhao,B.
  TITLE     Neuronal-specific TNFAIP1 ablation attenuates postoperative
            cognitive dysfunction via targeting SNAP25 for K48-linked
            ubiquitination
  JOURNAL   Cell Commun Signal 21 (1), 356 (2023)
   PUBMED   38102610
  REMARK    GeneRIF: Neuronal-specific TNFAIP1 ablation attenuates
            postoperative cognitive dysfunction via targeting SNAP25 for
            K48-linked ubiquitination.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Bolognesi,E., Guerini,F.R., Carta,A., Chiappedi,M., Sotgiu,S.,
            Mensi,M.M., Agliardi,C., Zanzottera,M. and Clerici,M.
  TITLE     The Role of SNAP-25 in Autism Spectrum Disorders Onset Patterns
  JOURNAL   Int J Mol Sci 24 (18), 14042 (2023)
   PUBMED   37762342
  REMARK    GeneRIF: The Role of SNAP-25 in Autism Spectrum Disorders Onset
            Patterns.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Yazar,V., Kuhlwein,J.K., Knehr,A., Grozdanov,V., Ekici,A.B.,
            Ludolph,A.C. and Danzer,K.M.
  TITLE     Impaired ATF3 signaling involves SNAP25 in SOD1 mutant ALS patients
  JOURNAL   Sci Rep 13 (1), 12019 (2023)
   PUBMED   37491426
  REMARK    GeneRIF: Impaired ATF3 signaling involves SNAP25 in SOD1 mutant ALS
            patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Zhang,J., Hou,S., Chi,X.Q., Shan,H.F., Li,X.W., Zhang,Q.J.,
            Wang,J.L. and Kang,C.B.
  TITLE     Role of SNAP25 on the occurrence and development of eosinophilic
            gastritis
  JOURNAL   Medicine (Baltimore) 102 (29), e34377 (2023)
   PUBMED   37478220
  REMARK    GeneRIF: Role of SNAP25 on the occurrence and development of
            eosinophilic gastritis.
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Hanson,P.I., Otto,H., Barton,N. and Jahn,R.
  TITLE     The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce
            a conformational change in syntaxin
  JOURNAL   J Biol Chem 270 (28), 16955-16961 (1995)
   PUBMED   7622514
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Hata,Y. and Sudhof,T.C.
  TITLE     A novel ubiquitous form of Munc-18 interacts with multiple
            syntaxins. Use of the yeast two-hybrid system to study interactions
            between proteins involved in membrane traffic
  JOURNAL   J Biol Chem 270 (22), 13022-13028 (1995)
   PUBMED   7768895
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Chapman,E.R., An,S., Barton,N. and Jahn,R.
  TITLE     SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin
            via domains that may form coiled coils
  JOURNAL   J Biol Chem 269 (44), 27427-27432 (1994)
   PUBMED   7961655
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Zhao,N., Hashida,H., Takahashi,N. and Sakaki,Y.
  TITLE     Cloning and sequence analysis of the human SNAP25 cDNA
  JOURNAL   Gene 145 (2), 313-314 (1994)
   PUBMED   8056350
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Abicht,A., Muller,J.S. and Lochmuller,H.
  TITLE     Congenital Myasthenic Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354824.8 and AL023913.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Synaptic vesicle membrane docking and fusion is mediated
            by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment
            protein receptors) located on the vesicle membrane (v-SNAREs) and
            the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE
            complex consists of a bundle of four helices, one of which is
            supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on
            the plasma membrane, the protein syntaxin supplies one helix and
            the protein encoded by this gene contributes the other two.
            Therefore, this gene product is a presynaptic plasma membrane
            protein involved in the regulation of neurotransmitter release. Two
            alternative transcript variants encoding different protein isoforms
            have been described for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647443.1, D21267.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000254976.7/ ENSP00000254976.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.2"
     Protein         1..206
                     /product="synaptosomal-associated protein 25 isoform
                     SNAP25B"
                     /note="resistance to inhibitors of cholinesterase 4
                     homolog; synaptosome associated protein 25kDa;
                     synaptosomal-associated protein, 25kDa"
                     /calculated_mol_wt=23184
     Region          1..75
                     /region_name="Interaction with CENPF.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P60880.1)"
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60880.1)"
     Region          10..82
                     /region_name="SNARE_SNAP25N"
                     /note="N-terminal SNARE motif of SNAP25; cd15894"
                     /db_xref="CDD:277247"
     Site            order(24..25,28..29,31..33,35..40,42..44,46..47,49..50,
                     53..54,56..61,63..65,67..68,70..75,77..78)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277247"
     Site            53
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277247"
     Region          91..142
                     /region_name="SNAP-25"
                     /note="SNAP-25 family; pfam00835"
                     /db_xref="CDD:459955"
     Region          111..120
                     /region_name="Interaction with ZDHHC17.
                     /evidence=ECO:0000269|PubMed:28757145"
                     /note="propagated from UniProtKB/Swiss-Prot (P60880.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P60879; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     Region          143..201
                     /region_name="SNARE_SNAP25C"
                     /note="C-terminal SNARE motif of SNAP25; cd15885"
                     /db_xref="CDD:277238"
     Site            order(143,145..146,149..154,156..157,160..161,163..165,
                     167..168,171..172,174..175,177..182,184..185,188,191,195,
                     198,201)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277238"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P60879; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     Site            174
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277238"
     Site            180..181
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by C.botulinum
                     neurotoxin type E (BoNT/E).
                     /evidence=ECO:0000269|PubMed:9886085; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P60879; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     Site            197..198
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by C.botulinum
                     neurotoxin type A (BoNT/A, botA).
                     /evidence=ECO:0000269|PubMed:9886085,
                     ECO:0000305|PubMed:15592454; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     Site            198..199
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by C.botulinum
                     neurotoxin type C (BoNT/C).
                     /evidence=ECO:0000269|PubMed:9886085,
                     ECO:0000305|PubMed:15592454; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     CDS             1..206
                     /gene="SNAP25"
                     /gene_synonym="bA416N4.2; CMS18; DEE117; dJ1068F16.2;
                     RIC-4; RIC4; SEC9; SNAP; SNAP-25; SUP"
                     /coded_by="NM_130811.4:212..832"
                     /note="isoform SNAP25B is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS13110.1"
                     /db_xref="GeneID:6616"
                     /db_xref="HGNC:HGNC:11132"
                     /db_xref="MIM:600322"
ORIGIN      
        1 maedadmrne leemqrradq ladeslestr rmlqlveesk dagirtlvml deqgeqleri
       61 eegmdqinkd mkeaeknltd lgkfcglcvc pcnklkssda ykkawgnnqd gvvasqparv
      121 vdereqmais ggfirrvtnd arenemdenl eqvsgiignl rhmaldmgne idtqnrqidr
      181 imekadsnkt rideanqrat kmlgsg
//
LOCUS       NP_001139577             819 aa            linear   PRI 21-NOV-2025
DEFINITION  protein mono-ADP-ribosyltransferase PARP9 isoform b [Homo sapiens].
ACCESSION   NP_001139577
VERSION     NP_001139577.1
DBSOURCE    REFSEQ: accession NM_001146105.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Pandi,K., Angabo,S., Makkawi,H., Benyamini,H., Elgavish,S. and
            Nussbaum,G.
  TITLE     P. gingivalis-Induced TLR2 Interactome Analysis Reveals Association
            with PARP9
  JOURNAL   J Dent Res 103 (3), 329-338 (2024)
   PUBMED   38344758
  REMARK    GeneRIF: P. gingivalis-Induced TLR2 Interactome Analysis Reveals
            Association with PARP9.
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Thirunavukkarasu,S., Ahmed,M., Rosa,B.A., Boothby,M., Cho,S.H.,
            Rangel-Moreno,J., Mbandi,S.K., Schreiber,V., Gupta,A., Zuniga,J.,
            Mitreva,M., Kaushal,D., Scriba,T.J. and Khader,S.A.
  TITLE     Poly(ADP-ribose) polymerase 9 mediates early protection against
            Mycobacterium tuberculosis infection by regulating type I IFN
            production
  JOURNAL   J Clin Invest 133 (12), e158630 (2023)
   PUBMED   37200107
  REMARK    GeneRIF: Poly(ADP-ribose) polymerase 9 mediates early protection
            against Mycobacterium tuberculosis infection by regulating type I
            IFN production.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 819)
  AUTHORS   Russo,L.C., Tomasin,R., Matos,I.A., Manucci,A.C., Sowa,S.T.,
            Dale,K., Caldecott,K.W., Lehtio,L., Schechtman,D., Meotti,F.C.,
            Bruni-Cardoso,A. and Hoch,N.C.
  TITLE     The SARS-CoV-2 Nsp3 macrodomain reverses PARP9/DTX3L-dependent
            ADP-ribosylation induced by interferon signaling
  JOURNAL   J Biol Chem 297 (3), 101041 (2021)
   PUBMED   34358560
  REMARK    GeneRIF: The SARS-CoV-2 Nsp3 macrodomain reverses
            PARP9/DTX3L-dependent ADP-ribosylation induced by interferon
            signaling.
REFERENCE   5  (residues 1 to 819)
  AUTHORS   Xing,J., Zhang,A., Du,Y., Fang,M., Minze,L.J., Liu,Y.J., Li,X.C.
            and Zhang,Z.
  TITLE     Identification of poly(ADP-ribose) polymerase 9 (PARP9) as a
            noncanonical sensor for RNA virus in dendritic cells
  JOURNAL   Nat Commun 12 (1), 2681 (2021)
   PUBMED   33976210
  REMARK    GeneRIF: Identification of poly(ADP-ribose) polymerase 9 (PARP9) as
            a noncanonical sensor for RNA virus in dendritic cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 819)
  AUTHORS   Jha,R., Agarwal,A., Mahfouz,R., Paasch,U., Grunewald,S.,
            Sabanegh,E., Yadav,S.P. and Sharma,R.
  TITLE     Determination of Poly (ADP-ribose) polymerase (PARP) homologues in
            human ejaculated sperm and its correlation with sperm maturation
  JOURNAL   Fertil Steril 91 (3), 782-790 (2009)
   PUBMED   18339380
  REMARK    GeneRIF: Determination of Poly (ADP-ribose) polymerase (PARP)
            homologues in human ejaculated sperm and its correlation with sperm
            maturation.
REFERENCE   7  (residues 1 to 819)
  AUTHORS   Juszczynski,P., Kutok,J.L., Li,C., Mitra,J., Aguiar,R.C. and
            Shipp,M.A.
  TITLE     BAL1 and BBAP are regulated by a gamma interferon-responsive
            bidirectional promoter and are overexpressed in diffuse large
            B-cell lymphomas with a prominent inflammatory infiltrate
  JOURNAL   Mol Cell Biol 26 (14), 5348-5359 (2006)
   PUBMED   16809771
  REMARK    GeneRIF: BAL1 and BBAP are located on chromosome 3q21 in a
            head-to-head orientation and are regulated by a
            IFN-gamma-responsive bidirectional promoter.
REFERENCE   8  (residues 1 to 819)
  AUTHORS   Aguiar,R.C., Takeyama,K., He,C., Kreinbrink,K. and Shipp,M.A.
  TITLE     B-aggressive lymphoma family proteins have unique domains that
            modulate transcription and exhibit poly(ADP-ribose) polymerase
            activity
  JOURNAL   J Biol Chem 280 (40), 33756-33765 (2005)
   PUBMED   16061477
REFERENCE   9  (residues 1 to 819)
  AUTHORS   Takeyama,K., Aguiar,R.C., Gu,L., He,C., Freeman,G.J., Kutok,J.L.,
            Aster,J.C. and Shipp,M.A.
  TITLE     The BAL-binding protein BBAP and related Deltex family members
            exhibit ubiquitin-protein isopeptide ligase activity
  JOURNAL   J Biol Chem 278 (24), 21930-21937 (2003)
   PUBMED   12670957
REFERENCE   10 (residues 1 to 819)
  AUTHORS   Aguiar,R.C., Yakushijin,Y., Kharbanda,S., Salgia,R., Fletcher,J.A.
            and Shipp,M.A.
  TITLE     BAL is a novel risk-related gene in diffuse large B-cell lymphomas
            that enhances cellular migration
  JOURNAL   Blood 96 (13), 4328-4334 (2000)
   PUBMED   11110709
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC368112.1 and BC039580.1.
            
            Transcript Variant: This variant (5) differs in the 5' UTR and uses
            an alternate in-frame splice site in the 5' coding region, compared
            to variant 1. This results in a shorter protein (isoform b),
            compared to isoform a. Variants 3, 4 and 5 encode the same isoform
            (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC039580.1, DRR138522.1371034.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000682323.1/ ENSP00000507390.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.1"
     Protein         1..819
                     /product="protein mono-ADP-ribosyltransferase PARP9
                     isoform b"
                     /EC_number="2.4.2.30"
                     /note="poly [ADP-ribose] polymerase 9; poly (ADP-ribose)
                     polymerase 9; PARP-9; b aggressive lymphoma protein;
                     ADP-ribosyltransferase diphtheria toxin-like 9; protein
                     mono-ADP-ribosyltransferase PARP9"
                     /calculated_mol_wt=92141
     Region          82..242
                     /region_name="Macro_Af1521_BAL-like"
                     /note="macrodomain, Af1521-like family; cd02907"
                     /db_xref="CDD:394877"
     Site            order(90..92,103..105,109..115,117,203..209)
                     /site_type="other"
                     /note="ADP-ribose binding site [chemical binding]"
                     /db_xref="CDD:394877"
     Region          275..451
                     /region_name="Macro_BAL-like"
                     /note="macrodomain, B-aggressive lymphoma (BAL)-like
                     family; cd02903"
                     /db_xref="CDD:394874"
     Site            order(290..292,302..304,310..313,316,394..400,434,440)
                     /site_type="other"
                     /note="ADP-ribose binding site [chemical binding]"
                     /db_xref="CDD:394874"
     Region          667..786
                     /region_name="TCCD_inducible_PARP_like"
                     /note="Poly(ADP-ribose) polymerases catalyse the covalent
                     attachment of ADP-ribose units from NAD+ to itself and to
                     a limited number of other DNA binding proteins, which
                     decreases their affinity for DNA. Poly(ADP-ribose)
                     polymerase is a regulatory component...; cd01439"
                     /db_xref="CDD:238719"
     Site            order(669..673,676,680,684..686,688,701..703,713,769)
                     /site_type="other"
                     /note="nad+ binding pocket [chemical binding]"
                     /db_xref="CDD:238719"
     CDS             1..819
                     /gene="PARP9"
                     /gene_synonym="ARTD9; BAL; BAL1; MGC:7868"
                     /coded_by="NM_001146105.2:146..2605"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS54634.1"
                     /db_xref="GeneID:83666"
                     /db_xref="HGNC:HGNC:24118"
                     /db_xref="MIM:612065"
ORIGIN      
        1 mdfsmvagaa ayneksetga lgenyswqip inhndfkilk nnerqlcevl qnkfgcistl
       61 vspvqegnsk slqvfrkmlt prielsvwkd dltthavdav vnaanedllh ggglalalvk
      121 aggfeiqees kqfvarygkv sageiavtga grlpckqiih avgprwmewd kqgctgklqr
      181 aivsilnyvi yknthiktva ipalssgifq fplnlctkti vetirvslqg kpmmsnlkei
      241 hlvsnedptv aafkaasefi lgkselgqet tpsfnamvvn nltlqivqgh iewqtadviv
      301 nsvnphditv gpvaksilqq agvemksefl atkakqfqrs qlvlvtkgfn lfckyiyhvl
      361 whsefpkpqi lkhamkecle kcieqnitsi sfpalgtgnm eikketaaei lfdevltfak
      421 dhvkhqltvk fvifptdlei ykafssemak rskmlslnny svpqstreek renglearsp
      481 ainlmgfnve emyeahawiq rilslqnhhi iennhilylg rkehdilsql qktssvsite
      541 iispgrtele iegaradlie vvmniedmlc kvqeemarkk erglwrslgq wtiqqqktqd
      601 emkeniiflk cpvpptqell dqkkqfekcg lqvlkvekid nevlmaafqr kkkmmeeklh
      661 rqpvshrlfq qvpyqfcnvv crvgfqrmys tpcdpkygag iyftknlknl aekakkisaa
      721 dkliyvfeae vltgffcqgh plnivpppls pgaidghdsv vdnvsspetf vifsgmqaip
      781 qylwtctqey vqsqdyssgp mrpfaqhpwr gfasgspvd
//
LOCUS       NP_001307813             611 aa            linear   PRI 21-NOV-2025
DEFINITION  cytoplasmic dynein 1 intermediate chain 2 isoform 4 [Homo sapiens].
ACCESSION   NP_001307813 XP_005246426
VERSION     NP_001307813.1
DBSOURCE    REFSEQ: accession NM_001320884.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 611)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 611)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 611)
  AUTHORS   Habu,T. and Kim,J.
  TITLE     Dynein intermediate chain 2c (DNCI2c) complex is essential for
            exiting Mad2-dependent spindle assembly checkpoint
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1868 (12), 119120 (2021)
   PUBMED   34400173
  REMARK    GeneRIF: Dynein intermediate chain 2c (DNCI2c) complex is essential
            for exiting Mad2-dependent spindle assembly checkpoint.
REFERENCE   5  (residues 1 to 611)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 611)
  AUTHORS   Sivaram,M.V., Wadzinski,T.L., Redick,S.D., Manna,T. and Doxsey,S.J.
  TITLE     Dynein light intermediate chain 1 is required for progress through
            the spindle assembly checkpoint
  JOURNAL   EMBO J 28 (7), 902-914 (2009)
   PUBMED   19229290
REFERENCE   7  (residues 1 to 611)
  AUTHORS   Pfister,K.K., Fisher,E.M., Gibbons,I.R., Hays,T.S., Holzbaur,E.L.,
            McIntosh,J.R., Porter,M.E., Schroer,T.A., Vaughan,K.T.,
            Witman,G.B., King,S.M. and Vallee,R.B.
  TITLE     Cytoplasmic dynein nomenclature
  JOURNAL   J Cell Biol 171 (3), 411-413 (2005)
   PUBMED   16260502
REFERENCE   8  (residues 1 to 611)
  AUTHORS   Davies,T.H., Ning,Y.M. and Sanchez,E.R.
  TITLE     A new first step in activation of steroid receptors:
            hormone-induced switching of FKBP51 and FKBP52 immunophilins
  JOURNAL   J Biol Chem 277 (7), 4597-4600 (2002)
   PUBMED   11751894
REFERENCE   9  (residues 1 to 611)
  AUTHORS   Crackower,M.A., Sinasac,D.S., Xia,J., Motoyama,J., Prochazka,M.,
            Rommens,J.M., Scherer,S.W. and Tsui,L.C.
  TITLE     Cloning and characterization of two cytoplasmic dynein intermediate
            chain genes in mouse and human
  JOURNAL   Genomics 55 (3), 257-267 (1999)
   PUBMED   10049579
REFERENCE   10 (residues 1 to 611)
  AUTHORS   Vaughan,K.T. and Vallee,R.B.
  TITLE     Cytoplasmic dynein binds dynactin through a direct interaction
            between the intermediate chains and p150Glued
  JOURNAL   J Cell Biol 131 (6 Pt 1), 1507-1516 (1995)
   PUBMED   8522607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP355434.1, AF250307.1 and
            AC068039.6.
            
            On Mar 9, 2016 this sequence version replaced XP_005246426.1.
            
            Summary: This gene encodes a member of the dynein intermediate
            chain family. The encoded protein is a non-catalytic component of
            the cytoplasmic dynein 1 complex, which acts as a retrograde
            microtubule motor to transport organelles and vesicles. A
            pseudogene of this gene is located on chromosome 10. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Nov 2012].
            
            Transcript Variant: This variant (8) differs in the 5' UTR and in
            the coding region but maintains the reading frame, compared to
            variant 1. The encoded isoform (4) is shorter, compared to isoform
            1. Both variants 7 and 8 encode the same isoform (4).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.97405.1,
                                           SRR1803617.197069.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..611
                     /product="cytoplasmic dynein 1 intermediate chain 2
                     isoform 4"
                     /note="dynein, cytoplasmic, intermediate polypeptide 2; DH
                     IC-2; dynein intermediate chain 2, cytosolic; testis
                     tissue sperm-binding protein Li 66n"
                     /calculated_mol_wt=68167
     Region          107..137
                     /region_name="Dynein_IC2"
                     /note="Cytoplasmic dynein 1 intermediate chain 2;
                     pfam11540"
                     /db_xref="CDD:463291"
     Region          256..305
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <283..573
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          313..351
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          359..400
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          408..455
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          463..495
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          501..539
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          547..573
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..611
                     /gene="DYNC1I2"
                     /gene_synonym="DIC74; DNCI2; IC2; NEDMIBA"
                     /coded_by="NM_001320884.2:129..1964"
                     /note="isoform 4 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS63057.1"
                     /db_xref="GeneID:1781"
                     /db_xref="HGNC:HGNC:2964"
                     /db_xref="MIM:603331"
ORIGIN      
        1 msdkselkae lerkkqrlaq ireekkrkee erkkketdqk keavapvqee sdlekkrrea
       61 eallqsmglt pespivpppm spssksvstp seagsqdsgd gavgsrrgpi klgmakitqv
      121 dfppreivty tketqtpvma qpkedeeedd dvvapkppie peeektlkkd eendskapph
      181 elteeekqqi lhseeflsff dhstrivera lseqiniffd ysgrdledke geiqagakls
      241 lnrqffderw skhrvvscld wssqypellv asynnnedap hepdgvalvw nmkykkttpe
      301 yvfhcqsavm satfakfhpn lvvggtysgq ivlwdnrsnk rtpvqrtpls aaahthpvyc
      361 vnvvgtqnah nlisistdgk icswsldmls hpqdsmelvh kqskavavts msfpvgdvnn
      421 fvvgseegsv ytacrhgska gisemfeghq gpitgihcha avgavdfshl fvtssfdwtv
      481 klwttknnkp lysfednady vydvmwspth palfacvdgm grldlwnlnn dtevptasis
      541 vegnpalnrv rwthsgreia vgdsegqivi ydvgeiavpr ndewarfgrt laeinanrad
      601 aeeeaatrip a
//
LOCUS       NP_001335672            1310 aa            linear   PRI 21-NOV-2025
DEFINITION  kinase D-interacting substrate of 220 kDa isoform 10 [Homo
            sapiens].
ACCESSION   NP_001335672
VERSION     NP_001335672.1
DBSOURCE    REFSEQ: accession NM_001348743.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1310)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1310)
  AUTHORS   Zhang,J., Zhang,Y., Shang,Q., Cheng,Y., Su,Y., Zhang,J., Wang,T.,
            Ding,J., Li,Y., Xie,Y. and Xing,Q.
  TITLE     Gain-of-Function KIDINS220 Variants Disrupt Neuronal Development
            and Cause Cerebral Palsy
  JOURNAL   Mov Disord 39 (3), 498-509 (2024)
   PUBMED   38148610
  REMARK    GeneRIF: Gain-of-Function KIDINS220 Variants Disrupt Neuronal
            Development and Cause Cerebral Palsy.
REFERENCE   3  (residues 1 to 1310)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1310)
  AUTHORS   Bondeson,D.P., Paolella,B.R., Asfaw,A., Rothberg,M.V.,
            Skipper,T.A., Langan,C., Mesa,G., Gonzalez,A., Surface,L.E.,
            Ito,K., Kazachkova,M., Colgan,W.N., Warren,A., Dempster,J.M.,
            Krill-Burger,J.M., Ericsson,M., Tang,A.A., Fung,I., Chambers,E.S.,
            Abdusamad,M., Dumont,N., Doench,J.G., Piccioni,F., Root,D.E.,
            Boehm,J., Hahn,W.C., Mannstadt,M., McFarland,J.M., Vazquez,F. and
            Golub,T.R.
  TITLE     Phosphate dysregulation via the XPR1-KIDINS220 protein complex is a
            therapeutic vulnerability in ovarian cancer
  JOURNAL   Nat Cancer 3 (6), 681-695 (2022)
   PUBMED   35437317
  REMARK    GeneRIF: Phosphate dysregulation via the XPR1-KIDINS220 protein
            complex is a therapeutic vulnerability in ovarian cancer.
REFERENCE   5  (residues 1 to 1310)
  AUTHORS   Scholz-Starke,J. and Cesca,F.
  TITLE     Stepping Out of the Shade: Control of Neuronal Activity by the
            Scaffold Protein Kidins220/ARMS
  JOURNAL   Front Cell Neurosci 10, 68 (2016)
   PUBMED   27013979
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1310)
  AUTHORS   Arevalo,J.C., Yano,H., Teng,K.K. and Chao,M.V.
  TITLE     A unique pathway for sustained neurotrophin signaling through an
            ankyrin-rich membrane-spanning protein
  JOURNAL   EMBO J 23 (12), 2358-2368 (2004)
   PUBMED   15167895
REFERENCE   7  (residues 1 to 1310)
  AUTHORS   Riol-Blanco,L., Iglesias,T., Sanchez-Sanchez,N., de la Rosa,G.,
            Sanchez-Ruiloba,L., Cabrera-Poch,N., Torres,A., Longo,I.,
            Garcia-Bordas,J., Longo,N., Tejedor,A., Sanchez-Mateos,P. and
            Rodriguez-Fernandez,J.L.
  TITLE     The neuronal protein Kidins220 localizes in a raft compartment at
            the leading edge of motile immature dendritic cells
  JOURNAL   Eur J Immunol 34 (1), 108-118 (2004)
   PUBMED   14971036
REFERENCE   8  (residues 1 to 1310)
  AUTHORS   Kong,H., Boulter,J., Weber,J.L., Lai,C. and Chao,M.V.
  TITLE     An evolutionarily conserved transmembrane protein that is a novel
            downstream target of neurotrophin and ephrin receptors
  JOURNAL   J Neurosci 21 (1), 176-185 (2001)
   PUBMED   11150334
REFERENCE   9  (residues 1 to 1310)
  AUTHORS   Iglesias,T., Cabrera-Poch,N., Mitchell,M.P., Naven,T.J.,
            Rozengurt,E. and Schiavo,G.
  TITLE     Identification and cloning of Kidins220, a novel neuronal substrate
            of protein kinase D
  JOURNAL   J Biol Chem 275 (51), 40048-40056 (2000)
   PUBMED   10998417
REFERENCE   10 (residues 1 to 1310)
  AUTHORS   Kaplan,D.R. and Miller,F.D.
  TITLE     Signal transduction by the neurotrophin receptors
  JOURNAL   Curr Opin Cell Biol 9 (2), 213-221 (1997)
   PUBMED   9069267
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012495.9, AC011747.8 and
            AK094521.1.
            
            Summary: This gene encodes a transmembrane protein that is
            preferentially expressed in the nervous system where it controls
            neuronal cell survival, differentiation into exons and dendrites,
            and synaptic plasticity. The encoded protein interacts with
            membrane receptors, cytosolic signaling components, and
            cytoskeletal proteins, serving as a scaffold that mediates
            crosstalk between the neurotrophin pathway and several other
            intracellular signaling pathways. Aberrant expression of this gene
            is associated with the onset of various neuropsychiatric disorders
            and neurodegenerative diseases, including Alzheimer's disease.
            Naturally occurring mutations in this gene are associated with a
            syndrome characterized by spastic paraplegia, intellectual
            disability, nystagmus and obesity. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Feb 2017].
            
            Transcript Variant: This variant (13) has multiple coding region
            differences and differs in the 3' UTR, compared to variant 1. The
            encoded isoform (13) is shorter and has a distinct C-terminus,
            compared to isoform 1. Variants 11-13 encode the same isoform (10).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.214095.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1310
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.1"
     Protein         1..1310
                     /product="kinase D-interacting substrate of 220 kDa
                     isoform 10"
                     /note="ankyrin repeat-rich membrane-spanning protein;
                     kinase D-interacting substrate 220kDa"
                     /calculated_mol_wt=145789
     Region          18..306
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          38..68
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(39,43..44,47..49,51..52,56,59,68,70,72,76..77,
                     80..82,84..85,89,92,101,103,105,109..110,113..115,
                     117..118,122,125)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          70..101
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          103..132
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          169..197
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          235..266
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          268..298
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          273..365
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Region          301..331
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          334..365
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <348..412
                     /region_name="PHA02736"
                     /note="Viral ankyrin protein; Provisional"
                     /db_xref="CDD:165103"
     Region          440..953
                     /region_name="KAP_NTPase"
                     /note="KAP family P-loop domain; pfam07693"
                     /db_xref="CDD:462231"
     CDS             1..1310
                     /gene="KIDINS220"
                     /gene_synonym="ARMS; SINO; VENARG"
                     /coded_by="NM_001348743.2:171..4103"
                     /note="isoform 10 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS92712.1"
                     /db_xref="GeneID:57498"
                     /db_xref="HGNC:HGNC:29508"
                     /db_xref="MIM:615759"
ORIGIN      
        1 msvlisqsvi nyveeenipa lkallekckd vdernecgqt plmiaaeqgn leivkelikn
       61 gancnledld nwtalisask eghvhiveel lkcgvnlehr dmggwtalmw acykgrtdvv
      121 elllshganp svtglysvyp iiwaagrgha divhlllqng akvncsdkyg ttplvwaark
      181 ghlecvkhll amgadvdqeg ansmtaliva vkggytqsvk eilkrnpnvn ltdkdgntal
      241 miaskeghte ivqdlldagt yvnipdrsgd tvligavrgg hveivrallq kyadidirgq
      301 dnktalywav ekgnatmvrd ilqcnpdtei ctkdgetpli katkmrniev vellldkgak
      361 vsavdkkgdt plhiairgrs rklaelllrn pkdgrllyrp nkagetpyni dcshqksilt
      421 qifgarhlsp tetdgdmlgy dlyssaladi lseptmqppi cvglyaqwgs gksfllkkle
      481 demktfagqq ieplfqfswl ivfltlllcg glgllfaftv hpnlgiavsl sflallyiff
      541 iviyfggrre geswnwawvl strlarhigy lelllklmfv nppelpeqtt kalpvrflft
      601 dynrlssvgg etslaemiat lsdacerefg flatrlfrvf ktedtqgkkk wkktcclpsf
      661 viflfiigci isgitllaif rvdpkhltvn avlisiasvv glafvlncrt wwqvldslln
      721 sqrkrlhnaa sklhklkseg fmkvlkceve lmarmaktid sftqnqtrlv viidgldace
      781 qdkvlqmldt vrvlfskgpf iaifasdphi iikainqnln svlrdsning hdymrnivhl
      841 pvflnsrgls narkflvtsa tngdvpcsdt tgiqedadrr vsqnslgemt klgsktalnr
      901 rdtyrrrqmq rtitrqmsfd ltkllvtedw fsdispqtmr rllnivsvtg rllranqisf
      961 nwdrlaswin lteqwpyrts wlilyleete gipdqmtlkt iyerisknip ttkdveplle
     1021 idgdirnfev flssrtpvlv ardvkvflpc tvnldpklre iiadvraare qisigglayp
     1081 plplhegppr apsgysqpps vcsstsfngp faggvvspqp hssyysgmtg pqhpfynrgs
     1141 gpapgpvvll nslnvdavce klkqiegldq smlpqyctti kkaningrvl aqcnidelkk
     1201 emnmnfgdwh lfrstvlemr naeshvvped prflsesssg paphgeparr ashnelphte
     1261 lssqtpytln fsfeelntlg ldegaprhsn lswqeenagl eidsssedpd
//
LOCUS       NP_001159367             240 aa            linear   PRI 21-NOV-2025
DEFINITION  CD320 antigen isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001159367
VERSION     NP_001159367.1
DBSOURCE    REFSEQ: accession NM_001165895.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   McCaddon,A., Carr,D.F., Peter,H., Moat,S.J. and Quadros,E.V.
  TITLE     Transcobalamin receptor gene polymorphisms and mutation in an
            elderly population
  JOURNAL   Clin Nutr ESPEN 55, 425-427 (2023)
   PUBMED   37202078
  REMARK    GeneRIF: Transcobalamin receptor gene polymorphisms and mutation in
            an elderly population.
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Pangilinan,F., Watkins,D., Bernard,D., Chen,Y., Dong,N., Wu,Q.,
            Ozel-Abaan,H., Kaur,M., Caggana,M., Morrissey,M., Browne,M.L.,
            Mills,J.L., Van Ryzin,C., Shchelochkov,O., Sloan,J., Venditti,C.P.,
            Sarafoglou,K., Rosenblatt,D.S., Kay,D.M. and Brody,L.C.
  TITLE     Probing the functional consequence and clinical relevance of CD320
            p.E88del, a variant in the transcobalamin receptor gene
  JOURNAL   Am J Med Genet A 188 (4), 1124-1141 (2022)
   PUBMED   35107211
  REMARK    GeneRIF: Probing the functional consequence and clinical relevance
            of CD320 p.E88del, a variant in the transcobalamin receptor gene.
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Boachie,J., Adaikalakoteswari,A., Goljan,I., Samavat,J.,
            Cagampang,F.R. and Saravanan,P.
  TITLE     Intracellular and Tissue Levels of Vitamin B12 in Hepatocytes Are
            Modulated by CD320 Receptor and TCN2 Transporter
  JOURNAL   Int J Mol Sci 22 (6), 3089 (2021)
   PUBMED   33803025
  REMARK    GeneRIF: Intracellular and Tissue Levels of Vitamin B12 in
            Hepatocytes Are Modulated by CD320 Receptor and TCN2 Transporter.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Gick,G.G., Arora,K., Sequeira,J.M., Nakayama,Y., Lai,S.C. and
            Quadros,E.V.
  TITLE     Cellular uptake of vitamin B12: Role and fate of TCblR/CD320, the
            transcobalamin receptor
  JOURNAL   Exp Cell Res 396 (1), 112256 (2020)
   PUBMED   32898552
  REMARK    GeneRIF: Cellular uptake of vitamin B12: Role and fate of
            TCblR/CD320, the transcobalamin receptor.
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   7  (residues 1 to 240)
  AUTHORS   Zhang,X., Li,L., Jung,J., Xiang,S., Hollmann,C. and Choi,Y.S.
  TITLE     The distinct roles of T cell-derived cytokines and a novel
            follicular dendritic cell-signaling molecule 8D6 in germinal
            center-B cell differentiation
  JOURNAL   J Immunol 167 (1), 49-56 (2001)
   PUBMED   11418631
REFERENCE   8  (residues 1 to 240)
  AUTHORS   Acierno,J.S. Jr., Kennedy,J.C., Falardeau,J.L., Leyne,M.,
            Bromley,M.C., Colman,M.W., Sun,M., Bove,C., Ashworth,L.K.,
            Chadwick,L.H., Schiripo,T., Ma,S., Goldin,E., Schiffmann,R. and
            Slaugenhaupt,S.A.
  TITLE     A physical and transcript map of the MCOLN1 gene region on human
            chromosome 19p13.3-p13.2
  JOURNAL   Genomics 73 (2), 203-210 (2001)
   PUBMED   11318610
REFERENCE   9  (residues 1 to 240)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 240)
  AUTHORS   Li,L., Zhang,X., Kovacic,S., Long,A.J., Bourque,K., Wood,C.R. and
            Choi,Y.S.
  TITLE     Identification of a human follicular dendritic cell molecule that
            stimulates germinal center B cell growth
  JOURNAL   J Exp Med 191 (6), 1077-1084 (2000)
   PUBMED   10727470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010323.8.
            
            Summary: This gene encodes the transcobalamin receptor that is
            expressed at the cell surface. It mediates the cellular uptake of
            transcobalamin bound cobalamin (vitamin B12), and is involved in
            B-cell proliferation and immunoglobulin secretion. Mutations in
            this gene are associated with methylmalonic aciduria. Alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene.[provided by RefSeq, Jan 2011].
            
            Transcript Variant: This variant (2) lacks an in-frame coding exon
            compared to variant 1, resulting in a shorter isoform (2) missing
            an internal protein segment compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK058014.1, BX333939.2 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..240
                     /product="CD320 antigen isoform 2 precursor"
                     /note="8D6 antigen; CD320 antigen; FDC-SM-8D6;
                     transcobalamin receptor; FDC-signaling molecule 8D6;
                     transcobalamin 2 receptor; soluble CD320"
                     /calculated_mol_wt=20950
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3439
     mat_peptide     31..240
                     /product="CD320 antigen isoform 2"
                     /calculated_mol_wt=21405
     Region          90..125
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(95,104,115..116)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(108,111,115,121..122)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            118..122
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     CDS             1..240
                     /gene="CD320"
                     /gene_synonym="8D6; 8D6A; sCD320; TCBLR; TCII-R; TCN2R"
                     /coded_by="NM_001165895.2:69..791"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS54210.1"
                     /db_xref="GeneID:51293"
                     /db_xref="HGNC:HGNC:16692"
                     /db_xref="MIM:606475"
ORIGIN      
        1 msggwmaqvg awrtgalgla lllllglglg leaaasplst ptsaqaagie pctqkgqcpp
       61 ppglpcpctg vsdcsggtdk klrncsrlac lagelrctls ddcipltwrc dghpdcpdss
      121 delgcgtnei lpegdattmg ppvtlesvts lrnattmgpp vtlesvpsvg natsssagdq
      181 sgsptaygvi aaaavlsasl vtatllllsw lraqerlrpl gllvamkesl llseqktslp
//
LOCUS       NP_476528                186 aa            linear   PRI 21-NOV-2025
DEFINITION  vacuolar protein sorting-associated protein 29 isoform 2 [Homo
            sapiens].
ACCESSION   NP_476528
VERSION     NP_476528.1
DBSOURCE    REFSEQ: accession NM_057180.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Yao,Y.Q. and Lv,J.L.
  TITLE     Potential functions and causal associations of VPS29 in
            hepatocellular carcinoma: a bioinformatic and Mendelian
            randomization study
  JOURNAL   Eur Rev Med Pharmacol Sci 27 (20), 9586-9600 (2023)
   PUBMED   37916325
  REMARK    GeneRIF: Potential functions and causal associations of VPS29 in
            hepatocellular carcinoma: a bioinformatic and Mendelian
            randomization study.
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Laulumaa,S. and Varjosalo,M.
  TITLE     Commander Complex-A Multifaceted Operator in Intracellular
            Signaling and Cargo
  JOURNAL   Cells 10 (12), 3447 (2021)
   PUBMED   34943955
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 186)
  AUTHORS   Verges,M., Luton,F., Gruber,C., Tiemann,F., Reinders,L.G.,
            Huang,L., Burlingame,A.L., Haft,C.R. and Mostov,K.E.
  TITLE     The mammalian retromer regulates transcytosis of the polymeric
            immunoglobulin receptor
  JOURNAL   Nat Cell Biol 6 (8), 763-769 (2004)
   PUBMED   15247922
REFERENCE   7  (residues 1 to 186)
  AUTHORS   Haft,C.R., de la Luz Sierra,M., Bafford,R., Lesniak,M.A., Barr,V.A.
            and Taylor,S.I.
  TITLE     Human orthologs of yeast vacuolar protein sorting proteins Vps26,
            29, and 35: assembly into multimeric complexes
  JOURNAL   Mol Biol Cell 11 (12), 4105-4116 (2000)
   PUBMED   11102511
REFERENCE   8  (residues 1 to 186)
  AUTHORS   Edgar,A.J. and Polak,J.M.
  TITLE     Human homologues of yeast vacuolar protein sorting 29 and 35
  JOURNAL   Biochem Biophys Res Commun 277 (3), 622-630 (2000)
   PUBMED   11062004
REFERENCE   9  (residues 1 to 186)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 186)
  AUTHORS   Seaman,M.N., McCaffery,J.M. and Emr,S.D.
  TITLE     A membrane coat complex essential for endosome-to-Golgi retrograde
            transport in yeast
  JOURNAL   J Cell Biol 142 (3), 665-681 (1998)
   PUBMED   9700157
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB578892.1, AF168716.1,
            AL832866.1 and AC002350.1.
            
            Summary: This gene belongs to a group of vacuolar protein sorting
            (VPS) genes that, when functionally impaired, disrupt the efficient
            delivery of vacuolar hydrolases. The protein encoded by this gene
            is a component of a large multimeric complex, termed the retromer
            complex, which is involved in retrograde transport of proteins from
            endosomes to the trans-Golgi network. This VPS protein may be
            involved in the formation of the inner shell of the retromer coat
            for retrograde vesicles leaving the prevacuolar compartment.
            Alternative splice variants encoding different isoforms and
            representing non-protein coding transcripts have been found for
            this gene. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (2) lacks an alternate exon
            compared to variant 3. The resulting isoform (2) has a shorter and
            distinct N-terminus compared to isoform 3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG615560.1, GQ891479.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..186
                     /product="vacuolar protein sorting-associated protein 29
                     isoform 2"
                     /EC_number="3.1.3.3"
                     /note="vacuolar sorting protein VPS29/PEP11; retromer
                     protein; x 007 protein; vacuolar protein
                     sorting-associated protein 29; hVPS29; PEP11 homolog;
                     vesicle protein sorting 29; vacuolar protein sorting 29
                     homolog; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=20796
     Region          6..183
                     /region_name="MPP_Vps29"
                     /note="Homo sapiens Vps29 and related proteins,
                     metallophosphatase domain; cd07394"
                     /db_xref="CDD:163637"
     Site            order(12,14,43,66,90,119,121)
                     /site_type="active"
                     /db_xref="CDD:163637"
     Site            order(12,14,43,66,90,119,121)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:163637"
     Site            order(12,14,18,43,66..67,90,95,119)
                     /site_type="other"
                     /note="Vps29:Vps35 subcomplex [polypeptide binding]"
                     /db_xref="CDD:163637"
     CDS             1..186
                     /gene="VPS29"
                     /gene_synonym="DC15; DC7; PEP11"
                     /coded_by="NM_057180.3:61..621"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS53832.1"
                     /db_xref="GeneID:51699"
                     /db_xref="HGNC:HGNC:14340"
                     /db_xref="MIM:606932"
ORIGIN      
        1 maghrlvlvl gdlhiphrcn slpakfkkll vpgkiqhilc tgnlctkesy dylktlagdv
       61 hivrgdfden lnypeqkvvt vgqfkiglih ghqvipwgdm aslallqrqf dvdilisght
      121 hkfeafehen kfyinpgsat gaynaletni ipsfvlmdiq astvvtyvyq ligddvkver
      181 ieykkp
//
LOCUS       NP_001374885            1077 aa            linear   PRI 21-NOV-2025
DEFINITION  large proline-rich protein BAG6 isoform 4 [Homo sapiens].
ACCESSION   NP_001374885
VERSION     NP_001374885.1
DBSOURCE    REFSEQ: accession NM_001387956.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1077)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 1077)
  AUTHORS   Alashkar Alhamwe,B., Ponath,V., Alhamdan,F., Dorsam,B.,
            Landwehr,C., Linder,M., Pauck,K., Miethe,S., Garn,H.,
            Finkernagel,F., Brichkina,A., Lauth,M., Tiwari,D.K., Buchholz,M.,
            Bachurski,D., Elmshauser,S., Nist,A., Stiewe,T., Pogge von
            Strandmann,L., Szymanski,W., Beutgen,V., Graumann,J.,
            Teply-Szymanski,J., Keber,C., Denkert,C., Jacob,R., Preusser,C. and
            Pogge von Strandmann,E.
  TITLE     BAG6 restricts pancreatic cancer progression by suppressing the
            release of IL33-presenting extracellular vesicles and the
            activation of mast cells
  JOURNAL   Cell Mol Immunol 21 (8), 918-931 (2024)
   PUBMED   38942797
  REMARK    GeneRIF: BAG6 restricts pancreatic cancer progression by
            suppressing the release of IL33-presenting extracellular vesicles
            and the activation of mast cells.
REFERENCE   3  (residues 1 to 1077)
  AUTHORS   Liu,L., Wu,J., Yan,Y., Cheng,S., Yu,S. and Wang,Y.
  TITLE     DERL2 (derlin 2) stabilizes BAG6 (BAG cochaperone 6) in
            chemotherapy resistance of cholangiocarcinoma
  JOURNAL   J Physiol Biochem 80 (1), 81-97 (2024)
   PUBMED   37815698
  REMARK    GeneRIF: DERL2 (derlin 2) stabilizes BAG6 (BAG cochaperone 6) in
            chemotherapy resistance of cholangiocarcinoma.
REFERENCE   4  (residues 1 to 1077)
  AUTHORS   Roboti,P., Lawless,C. and High,S.
  TITLE     Mitochondrial antiviral-signalling protein is a client of the BAG6
            protein quality control complex
  JOURNAL   J Cell Sci 135 (9) (2022)
   PUBMED   35543156
  REMARK    GeneRIF: Mitochondrial antiviral-signalling protein is a client of
            the BAG6 protein quality control complex.
REFERENCE   5  (residues 1 to 1077)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1077)
  AUTHORS   Ozaki,T., Hanaoka,E., Naka,M., Nakagawara,A. and Sakiyama,S.
  TITLE     Cloning and characterization of rat BAT3 cDNA
  JOURNAL   DNA Cell Biol 18 (6), 503-512 (1999)
   PUBMED   10390159
REFERENCE   7  (residues 1 to 1077)
  AUTHORS   Cross,S.J., Tonks,S., Trowsdale,J. and Campbell,R.D.
  TITLE     Novel detection of restriction fragment length polymorphisms in the
            human major histocompatibility complex
  JOURNAL   Immunogenetics 34 (6), 376-384 (1991)
   PUBMED   1684176
REFERENCE   8  (residues 1 to 1077)
  AUTHORS   Banerji,J., Sands,J., Strominger,J.L. and Spies,T.
  TITLE     A gene pair from the human major histocompatibility complex encodes
            large proline-rich proteins with multiple repeated motifs and a
            single ubiquitin-like domain
  JOURNAL   Proc Natl Acad Sci U S A 87 (6), 2374-2378 (1990)
   PUBMED   2156268
REFERENCE   9  (residues 1 to 1077)
  AUTHORS   Spies,T., Bresnahan,M. and Strominger,J.L.
  TITLE     Human major histocompatibility complex contains a minimum of 19
            genes between the complement cluster and HLA-B
  JOURNAL   Proc Natl Acad Sci U S A 86 (22), 8955-8958 (1989)
   PUBMED   2813433
REFERENCE   10 (residues 1 to 1077)
  AUTHORS   Spies,T., Blanck,G., Bresnahan,M., Sands,J. and Strominger,J.L.
  TITLE     A new cluster of genes within the human major histocompatibility
            complex
  JOURNAL   Science 243 (4888), 214-217 (1989)
   PUBMED   2911734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL662801.7.
            
            Summary: This gene was first characterized as part of a cluster of
            genes located within the human major histocompatibility complex
            class III region. This gene encodes a nuclear protein that is
            cleaved by caspase 3 and is implicated in the control of apoptosis.
            In addition, the protein forms a complex with E1A binding protein
            p300 and is required for the acetylation of p53 in response to DNA
            damage. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.741283.1,
                                           SRR11853559.27606.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1077
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..1077
                     /product="large proline-rich protein BAG6 isoform 4"
                     /note="scythe; large proline-rich protein BAT3; large
                     proline-rich protein BAG6; protein G3; HLA-B-associated
                     transcript 3; protein Scythe; BAG family molecular
                     chaperone regulator 6; BCL2 associated athanogene 6"
                     /calculated_mol_wt=113325
     Region          17..87
                     /region_name="Ubl_BAG6"
                     /note="ubiquitin-like (Ubl) domain found in
                     BCL2-associated athanogene 6 (BAG6) and similar proteins;
                     cd01809"
                     /db_xref="CDD:340507"
     Site            order(22..25,58,60,62..65,83..87)
                     /site_type="other"
                     /note="ZF interaction site [polypeptide binding]"
                     /db_xref="CDD:340507"
     Region          270..386
                     /region_name="BAG6"
                     /note="BCL2-associated athanogene 6; pfam12057"
                     /db_xref="CDD:463449"
     Region          <899..1077
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     CDS             1..1077
                     /gene="BAG6"
                     /gene_synonym="BAG-6; BAT3; D6S52E; G3"
                     /coded_by="NM_001387956.1:276..3509"
                     /note="isoform 4 is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS56415.1"
                     /db_xref="GeneID:7917"
                     /db_xref="HGNC:HGNC:13919"
                     /db_xref="MIM:142590"
ORIGIN      
        1 mepndststa veepdslevl vktldsqtrt fivgaqmnvk efkehiaasv sipsekqrli
       61 yqgrvlqddk klqeynvggk vihlverapp qthlpsgass gtgsasathg ggsppgtrgp
      121 gasvhdrnan syvmvgtfnl psdgsavdvh inmeqapiqs eprvrlvmaq hmirdiqtll
      181 srmecrggpq pqhsqpppqp pavtpepval ssqtsepves eapprepmea eeveerapaq
      241 npeltpgpap agptpapetn apnhpspaey vevlqelqrl esrlqpflqr yyevlgaaat
      301 tdynnnhegr eedqrlinlv geslrllgnt fvalsdlrcn lactpprhlh vvrpmshytt
      361 pmvlqqaaip iqinvgttvt mtgngtrppp tpnaeapppg pgqassvaps stnvessaeg
      421 apppgpappp atshprviri shqsvepvvm mhmniqdsgt qpggvpsapt gplgppghgq
      481 tlgqqvpgfp taptrvviar ptppqarpsh pggppvsgtl qgaglgtnas laqmvsglvg
      541 qllmqpvlva qgtpgmappp apatasasag ttntattagp apggpaqppp tpqpsmadlq
      601 fsqllgnllg pagpgaggsg vasptitvam pgvpaflqgm tdflqatqta pppppppppp
      661 ppapeqqtmp ppgspsggag spgglglesl spefftsvvq gvlssllgsl garagssesi
      721 aafiqrlsgs snifepgadg algffgalls llcqnfsmvd vvmllhghfq plqrlqpqlr
      781 sffhqhylgg qeptpsnirm athtlitgle eyvresfslv qvqpgvdiir tnleflqeqf
      841 nsiaahvlhc tdsgfgarll elcnqglfec lalnlhclgg qqmelaavin grirrmsrgv
      901 npslvswltt mmglrlqvvl ehmpvgpdai lryvrrvgdp pqplpeepme vqgaeraspe
      961 pqrenaspap gttaeeamsr gpppapeggs rdeqdgasae tepwaaavpp ewvpiiqqdi
     1021 qsqrkvkpqp plsdaylsgm pakrrklrsd iqkrlqedpn yspqrfpnaq rafaddp
//
LOCUS       NP_001129607             169 aa            linear   PRI 21-NOV-2025
DEFINITION  large ribosomal subunit protein eL28 isoform 3 [Homo sapiens].
ACCESSION   NP_001129607
VERSION     NP_001129607.1
DBSOURCE    REFSEQ: accession NM_001136135.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 169)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 169)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   7  (residues 1 to 169)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   8  (residues 1 to 169)
  AUTHORS   Frigerio,J.M., Dagorn,J.C. and Iovanna,J.L.
  TITLE     Cloning, sequencing and expression of the L5, L21, L27a, L28, S5,
            S9, S10 and S29 human ribosomal protein mRNAs
  JOURNAL   Biochim Biophys Acta 1262 (1), 64-68 (1995)
   PUBMED   7772601
REFERENCE   9  (residues 1 to 169)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   10 (residues 1 to 169)
  AUTHORS   Brown,J.R., Daar,I.O., Krug,J.R. and Maquat,L.E.
  TITLE     Characterization of the functional gene and several processed
            pseudogenes in the human triosephosphate isomerase gene family
  JOURNAL   Mol Cell Biol 5 (7), 1694-1706 (1985)
   PUBMED   4022011
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP227047.1, AC020922.9 and
            BC011582.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L28E family of ribosomal proteins. It is located in the
            cytoplasm. Variable expression of this gene in colorectal cancers
            compared to adjacent normal tissues has been observed, although no
            correlation between the level of expression and the severity of the
            disease has been found. As is typical for genes encoding ribosomal
            proteins, there are multiple processed pseudogenes of this gene
            dispersed through the genome. Alternative splicing results in
            multiple transcript variants encoding distinct isoforms.[provided
            by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (3) lacks a stop-codon-containing
            segment in the 3' coding region, compared to variant 1. The encoded
            protein (isoform 3) has a distinct and longer C-terminus when
            compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic and transcript sequence to make the sequence consistent
            with the reference genome assembly. The extent of this transcript
            is supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.574282.1,
                                           SRR7346977.208999.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..169
                     /product="large ribosomal subunit protein eL28 isoform 3"
                     /EC_number="3.6.5.3"
                     /note="60S ribosomal protein L28; large ribosomal subunit
                     protein eL28"
                     /calculated_mol_wt=19017
     Region          5..112
                     /region_name="Ribosomal_L28e"
                     /note="Ribosomal L28e protein family; pfam01778"
                     /db_xref="CDD:460323"
     CDS             1..169
                     /gene="RPL28"
                     /gene_synonym="eL28; L28"
                     /coded_by="NM_001136135.2:43..552"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS46189.1"
                     /db_xref="GeneID:6158"
                     /db_xref="HGNC:HGNC:10330"
                     /db_xref="MIM:603638"
ORIGIN      
        1 msahlqwmvv rncssflikr nkqtystepn nlkarnsfry nglihrktvg vepaadgkgv
       61 vvvikrrsgq rkpatsyvrt tinknaratl ssirhmirkn kyrpdlrmdm lastgsglcc
      121 svavqpwass stslclrtli cnmrvdrpyy sglmrrlnvq nlldcahks
//
LOCUS       NP_775289                184 aa            linear   PRI 21-NOV-2025
DEFINITION  A-type potassium channel modulatory protein KCNIP2 isoform 7 [Homo
            sapiens].
ACCESSION   NP_775289
VERSION     NP_775289.1
DBSOURCE    REFSEQ: accession NM_173197.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Murthy,A., Workman,S.W., Jiang,M., Hu,J., Sifa,I., Bernas,T.,
            Tang,W., Deschenes,I. and Tseng,G.N.
  TITLE     Dynamic palmitoylation regulates trafficking of K channel
            interacting protein 2 (KChIP2) across multiple subcellular
            compartments in cardiac myocytes
  JOURNAL   J Mol Cell Cardiol 135, 1-9 (2019)
   PUBMED   31362018
  REMARK    GeneRIF: The palmitoylation status of KChIP2 determines its
            subcellular distribution in cardiac myocytes. Stress promotes
            nuclear entry of KChIP2, diverting it from ion channel modulation
            at the plasma membrane to other functions in the nuclear
            compartment.
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Murphy,J.G. and Hoffman,D.A.
  TITLE     A polybasic motif in alternatively spliced KChIP2 isoforms prevents
            Ca2+ regulation of Kv4 channels
  JOURNAL   J Biol Chem 294 (10), 3683-3695 (2019)
   PUBMED   30622142
  REMARK    GeneRIF: polybasic motif in alternatively spliced KChIP2 isoforms
            prevents Ca(2+) regulation of Kv4 channels
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Bahring,R., Dannenberg,J., Peters,H.C., Leicher,T., Pongs,O. and
            Isbrandt,D.
  TITLE     Conserved Kv4 N-terminal domain critical for effects of Kv
            channel-interacting protein 2.2 on channel expression and gating
  JOURNAL   J Biol Chem 276 (26), 23888-23894 (2001)
   PUBMED   11287421
REFERENCE   7  (residues 1 to 184)
  AUTHORS   Rosati,B., Pan,Z., Lypen,S., Wang,H.S., Cohen,I., Dixon,J.E. and
            McKinnon,D.
  TITLE     Regulation of KChIP2 potassium channel beta subunit gene expression
            underlies the gradient of transient outward current in canine and
            human ventricle
  JOURNAL   J Physiol 533 (Pt 1), 119-125 (2001)
   PUBMED   11351020
REFERENCE   8  (residues 1 to 184)
  AUTHORS   Ohya,S., Morohashi,Y., Muraki,K., Tomita,T., Watanabe,M.,
            Iwatsubo,T. and Imaizumi,Y.
  TITLE     Molecular cloning and expression of the novel splice variants of
            K(+) channel-interacting protein 2
  JOURNAL   Biochem Biophys Res Commun 282 (1), 96-102 (2001)
   PUBMED   11263977
REFERENCE   9  (residues 1 to 184)
  AUTHORS   An,W.F., Bowlby,M.R., Betty,M., Cao,J., Ling,H.P., Mendoza,G.,
            Hinson,J.W., Mattsson,K.I., Strassle,B.W., Trimmer,J.S. and
            Rhodes,K.J.
  TITLE     Modulation of A-type potassium channels by a family of calcium
            sensors
  JOURNAL   Nature 403 (6769), 553-556 (2000)
   PUBMED   10676964
REFERENCE   10 (residues 1 to 184)
  AUTHORS   Zhu,X.R., Wulf,A., Schwarz,M., Isbrandt,D. and Pongs,O.
  TITLE     Characterization of human Kv4.2 mediating a rapidly-inactivating
            transient voltage-sensitive K+ current
  JOURNAL   Recept Channels 6 (5), 387-400 (1999)
   PUBMED   10551270
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK094668.1, BC034685.1 and
            AF367019.1.
            
            Summary: This gene encodes a member of the family of voltage-gated
            potassium (Kv) channel-interacting proteins (KCNIPs), which belongs
            to the recoverin branch of the EF-hand superfamily. Members of the
            KCNIP family are small calcium binding proteins. They all have
            EF-hand-like domains, and differ from each other in the N-terminus.
            They are integral subunit components of native Kv4 channel
            complexes. They may regulate A-type currents, and hence neuronal
            excitability, in response to changes in intracellular calcium.
            Multiple alternatively spliced transcript variants encoding
            distinct isoforms have been identified from this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (7), also known as KChIP2.5, lacks
            four coding segments: two consecutive in the 5' region, one in the
            middle, and one at the 3' end, but has an alternate segment at the
            3' end, as compared to variant 1. The alternate segment contains
            the stop codon. Therefore, isoform 7 has a distinct C-terminus and
            is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF367019.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2159607
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..184
                     /product="A-type potassium channel modulatory protein
                     KCNIP2 isoform 7"
                     /note="A-type potassium channel modulatory protein 2;
                     potassium channel-interacting protein 2; cardiac
                     voltage-gated potassium channel modulatory subunit; Kv
                     channel interacting protein 2; A-type potassium channel
                     modulatory protein KCNIP2"
                     /calculated_mol_wt=21270
     Region          94..165
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cd00051"
                     /db_xref="CDD:238008"
     Site            order(103,105,107,114,151,153,155,162)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238008"
     CDS             1..184
                     /gene="KCNIP2"
                     /gene_synonym="KCHIP2"
                     /coded_by="NM_173197.3:233..787"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS7526.1"
                     /db_xref="GeneID:30819"
                     /db_xref="HGNC:HGNC:15522"
                     /db_xref="MIM:604661"
ORIGIN      
        1 mrgqgrkesl sdsrdldgsy dqltdsvdde felstvchrp egleqlqeqt kftrkelqvl
       61 yrgfknecps givneenfkq iysqffpqgd sstyatflfn afdtnhdgsv sfeemldimk
      121 siydmmgkyt ypalreeapr ehvesffqkm drnkdgvvti eefiescqkv qlpalyitlt
      181 wtqa
//
LOCUS       NP_665910                 96 aa            linear   PRI 21-NOV-2025
DEFINITION  high mobility group protein HMG-I/HMG-Y isoform b [Homo sapiens].
ACCESSION   NP_665910
VERSION     NP_665910.1
DBSOURCE    REFSEQ: accession NM_145903.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Olan,I., Ando-Kuri,M., Parry,A.J., Handa,T., Schoenfelder,S.,
            Fraser,P., Ohkawa,Y., Kimura,H., Narita,M. and Narita,M.
  TITLE     HMGA1 orchestrates chromatin compartmentalization and sequesters
            genes into 3D networks coordinating senescence heterogeneity
  JOURNAL   Nat Commun 15 (1), 6891 (2024)
   PUBMED   39134516
  REMARK    GeneRIF: HMGA1 orchestrates chromatin compartmentalization and
            sequesters genes into 3D networks coordinating senescence
            heterogeneity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 96)
  AUTHORS   Li,K.J., Hong,Y., Yu,Y.Z., Xie,Z., Lv,D.J., Wang,C., Xie,T.,
            Chen,H., Chen,Z.S., Zeng,J. and Zhao,S.C.
  TITLE     NAT10 Promotes Prostate Cancer Growth and Metastasis by Acetylating
            mRNAs of HMGA1 and KRT8
  JOURNAL   Adv Sci (Weinh) 11 (32), e2310131 (2024)
   PUBMED   38922788
  REMARK    GeneRIF: NAT10 Promotes Prostate Cancer Growth and Metastasis by
            Acetylating mRNAs of HMGA1 and KRT8.
REFERENCE   4  (residues 1 to 96)
  AUTHORS   Wang,L., Zhang,J., Xia,M., Liu,C., Zu,X. and Zhong,J.
  TITLE     High Mobility Group A1 (HMGA1): Structure, Biological Function, and
            Therapeutic Potential
  JOURNAL   Int J Biol Sci 18 (11), 4414-4431 (2022)
   PUBMED   35864955
  REMARK    GeneRIF: High Mobility Group A1 (HMGA1): Structure, Biological
            Function, and Therapeutic Potential.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 96)
  AUTHORS   Sumter,T.F., Xian,L., Huso,T., Koo,M., Chang,Y.T., Almasri,T.N.,
            Chia,L., Inglis,C., Reid,D. and Resar,L.M.
  TITLE     The High Mobility Group A1 (HMGA1) Transcriptome in Cancer and
            Development
  JOURNAL   Curr Mol Med 16 (4), 353-393 (2016)
   PUBMED   26980699
  REMARK    Review article
REFERENCE   6  (residues 1 to 96)
  AUTHORS   Friedmann,M., Holth,L.T., Zoghbi,H.Y. and Reeves,R.
  TITLE     Organization, inducible-expression and chromosome localization of
            the human HMG-I(Y) nonhistone protein gene
  JOURNAL   Nucleic Acids Res 21 (18), 4259-4267 (1993)
   PUBMED   8414980
REFERENCE   7  (residues 1 to 96)
  AUTHORS   Nissen,M.S., Langan,T.A. and Reeves,R.
  TITLE     Phosphorylation by cdc2 kinase modulates DNA binding activity of
            high mobility group I nonhistone chromatin protein
  JOURNAL   J Biol Chem 266 (30), 19945-19952 (1991)
   PUBMED   1939057
REFERENCE   8  (residues 1 to 96)
  AUTHORS   Reeves,R. and Nissen,M.S.
  TITLE     The A.T-DNA-binding domain of mammalian high mobility group I
            chromosomal proteins. A novel peptide motif for recognizing DNA
            structure
  JOURNAL   J Biol Chem 265 (15), 8573-8582 (1990)
   PUBMED   1692833
REFERENCE   9  (residues 1 to 96)
  AUTHORS   Eckner,R. and Birnstiel,M.L.
  TITLE     Cloning of cDNAs coding for human HMG I and HMG Y proteins: both
            are capable of binding to the octamer sequence motif
  JOURNAL   Nucleic Acids Res 17 (15), 5947-5959 (1989)
   PUBMED   2505228
REFERENCE   10 (residues 1 to 96)
  AUTHORS   Johnson,K.R., Lehn,D.A. and Reeves,R.
  TITLE     Alternative processing of mRNAs encoding mammalian chromosomal
            high-mobility-group proteins HMG-I and HMG-Y
  JOURNAL   Mol Cell Biol 9 (5), 2114-2123 (1989)
   PUBMED   2701943
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC338100.1, M23617.1,
            AL354740.29 and BC008832.2.
            
            Summary: This gene encodes a chromatin-associated protein involved
            in the regulation of gene transcription, integration of
            retroviruses into chromosomes, and the metastatic progression of
            cancer cells. The encoded protein preferentially binds to the minor
            groove of AT-rich regions in double-stranded DNA. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. Pseudogenes of this gene have been identified on
            multiple chromosomes. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (5) lacks an exon in the 5' UTR
            and uses an alternate in-frame splice site compared to variant 1.
            It encodes isoform b (also called HMG-Y), which is shorter than
            isoform a. Variants 2, 4, 5, 7, and 8 encode the same isoform (b).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.493594.1, M23617.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..96
                     /product="high mobility group protein HMG-I/HMG-Y isoform
                     b"
                     /note="nonhistone chromosomal high-mobility group protein
                     HMG-I/HMG-Y; high mobility group protein HMG-I/HMG-Y; high
                     mobility group protein R; high mobility group protein A1"
                     /calculated_mol_wt=10548
     CDS             1..96
                     /gene="HMGA1"
                     /gene_synonym="HMG-R; HMGA1A; HMGIY"
                     /coded_by="NM_145903.3:136..426"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS4788.1"
                     /db_xref="GeneID:3159"
                     /db_xref="HGNC:HGNC:5010"
                     /db_xref="MIM:600701"
ORIGIN      
        1 msessskssq plaskqekdg tekrgrgrpr kqppkepsev ptpkrprgrp kgsknkgaak
       61 trkttttpgr kprgrpkkle keeeegisqe sseeeq
//
LOCUS       NP_001273134             395 aa            linear   PRI 21-NOV-2025
DEFINITION  dynein regulatory complex subunit 4 isoform b [Homo sapiens].
ACCESSION   NP_001273134 XP_005256363
VERSION     NP_001273134.1
DBSOURCE    REFSEQ: accession NM_001286205.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Walton,T., Gui,M., Velkova,S., Fassad,M.R., Hirst,R.A., Haarman,E.,
            O'Callaghan,C., Bottier,M., Burgoyne,T., Mitchison,H.M. and
            Brown,A.
  TITLE     Axonemal structures reveal mechanoregulatory and disease mechanisms
  JOURNAL   Nature 618 (7965), 625-633 (2023)
   PUBMED   37258679
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Zhang,J., He,X., Wu,H., Zhang,X., Yang,S., Liu,C., Liu,S., Hua,R.,
            Zhou,S., Zhao,S., Hu,F., Zhang,J., Liu,W., Cheng,H., Gao,Y.,
            Zhang,F., Cao,Y. and Liu,M.
  TITLE     Loss of DRC1 function leads to multiple morphological abnormalities
            of the sperm flagella and male infertility in human and mouse
  JOURNAL   Hum Mol Genet 30 (21), 1996-2011 (2021)
   PUBMED   34169321
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Wu,X., Jiang,T., Huang,R. and Xiao,X.
  TITLE     LncRNA GAS8-AS1 downregulates lncRNA NEAT1 to inhibit glioblastoma
            cell proliferation
  JOURNAL   Brain Behav 11 (6), e02128 (2021)
   PUBMED   33942556
  REMARK    GeneRIF: LncRNA GAS8-AS1 downregulates lncRNA NEAT1 to inhibit
            glioblastoma cell proliferation.
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Ralston,K.S. and Hill,K.L.
  TITLE     Trypanin, a component of the flagellar Dynein regulatory complex,
            is essential in bloodstream form African trypanosomes
  JOURNAL   PLoS Pathog 2 (9), e101 (2006)
   PUBMED   17009870
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Colantonio,J.R., Bekker,J.M., Kim,S.J., Morrissey,K.M.,
            Crosbie,R.H. and Hill,K.L.
  TITLE     Expanding the role of the dynein regulatory complex to non-axonemal
            functions: association of GAS11 with the Golgi apparatus
  JOURNAL   Traffic 7 (5), 538-548 (2006)
   PUBMED   16643277
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Yeh,S.D., Chen,Y.J., Chang,A.C., Ray,R., She,B.R., Lee,W.S.,
            Chiang,H.S., Cohen,S.N. and Lin-Chao,S.
  TITLE     Isolation and properties of Gas8, a growth arrest-specific gene
            regulated during male gametogenesis to produce a protein associated
            with the sperm motility apparatus
  JOURNAL   J Biol Chem 277 (8), 6311-6317 (2002)
   PUBMED   11751847
REFERENCE   8  (residues 1 to 395)
  AUTHORS   Hill,K.L., Hutchings,N.R., Grandgenett,P.M. and Donelson,J.E.
  TITLE     T lymphocyte-triggering factor of african trypanosomes is
            associated with the flagellar fraction of the cytoskeleton and
            represents a new family of proteins that are present in several
            divergent eukaryotes
  JOURNAL   J Biol Chem 275 (50), 39369-39378 (2000)
   PUBMED   10969087
REFERENCE   9  (residues 1 to 395)
  AUTHORS   Whitmore,S.A., Settasatian,C., Crawford,J., Lower,K.M.,
            McCallum,B., Seshadri,R., Cornelisse,C.J., Moerland,E.W.,
            Cleton-Jansen,A.M., Tipping,A.J., Mathew,C.G., Savnio,M.,
            Savoia,A., Verlander,P., Auerbach,A.D., Van Berkel,C., Pronk,J.C.,
            Doggett,N.A. and Callen,D.F.
  TITLE     Characterization and screening for mutations of the growth
            arrest-specific 11 (GAS11) and C16orf3 genes at 16q24.3 in breast
            cancer
  JOURNAL   Genomics 52 (3), 325-331 (1998)
   PUBMED   9790751
REFERENCE   10 (residues 1 to 395)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC104785.1, AK293958.1,
            AF050079.1 and BX647947.1.
            
            On Oct 31, 2013 this sequence version replaced XP_005256363.1.
            
            Summary: This gene includes 11 exons spanning 25 kb and maps to a
            region of chromosome 16 that is sometimes deleted in breast and
            prostrate cancer. The second intron contains an apparently
            intronless gene, C16orf3, that is transcribed in the opposite
            orientation. This gene is a putative tumor suppressor gene. Several
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Oct 2013].
            
            Transcript Variant: This variant (3) uses an alternate splice site
            at the 5' end of an exon compared to variant 1. The resulting
            isoform (b) is shorter at the N-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853562.14137.1, AK293958.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..395
                     /product="dynein regulatory complex subunit 4 isoform b"
                     /note="growth arrest-specific protein 8; GAS-11; growth
                     arrest-specific protein 11; epididymis secretory sperm
                     binding protein; growth arrest specific 8"
                     /calculated_mol_wt=46222
     Region          <42..>127
                     /region_name="Mitofilin"
                     /note="Mitochondrial inner membrane protein; pfam09731"
                     /db_xref="CDD:430783"
     Region          138..337
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     CDS             1..395
                     /gene="DRC4"
                     /gene_synonym="CILD33; GAS11; GAS8"
                     /coded_by="NM_001286205.2:415..1602"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS73932.1"
                     /db_xref="GeneID:2622"
                     /db_xref="HGNC:HGNC:4166"
                     /db_xref="MIM:605178"
ORIGIN      
        1 meeaeerhqv eikvykqkvk hllyehqnnl temkaegtvv mklaqkehri qesvlrkdmr
       61 alkvelkeqe lasevvvknl rlkhteeitr mrndferqvr eieakydkkm kmlrdeldlr
      121 rktelhevee rkngqihtlm qrheeaftdi knyynditln nlalinslke qmedmrkked
      181 hleremaevs gqnkrladpl qkareemsem qkqlanyerd kqillctkar lkvrekelkd
      241 lqwehevleq rftkvqqerd elyrkftaai qevqqktgfk nlvlerklqa lsaavekkev
      301 qfnevlaasn ldpaaltlvs rkledvlesk nstikdlqye laqvckahnd llrtyeakll
      361 afgipldnvg fkpletavig qtlgqgpagl vgtpt
//
LOCUS       NP_001306011             107 aa            linear   PRI 21-NOV-2025
DEFINITION  high mobility group protein HMG-I/HMG-Y isoform a [Homo sapiens].
ACCESSION   NP_001306011
VERSION     NP_001306011.1
DBSOURCE    REFSEQ: accession NM_001319082.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Olan,I., Ando-Kuri,M., Parry,A.J., Handa,T., Schoenfelder,S.,
            Fraser,P., Ohkawa,Y., Kimura,H., Narita,M. and Narita,M.
  TITLE     HMGA1 orchestrates chromatin compartmentalization and sequesters
            genes into 3D networks coordinating senescence heterogeneity
  JOURNAL   Nat Commun 15 (1), 6891 (2024)
   PUBMED   39134516
  REMARK    GeneRIF: HMGA1 orchestrates chromatin compartmentalization and
            sequesters genes into 3D networks coordinating senescence
            heterogeneity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Li,K.J., Hong,Y., Yu,Y.Z., Xie,Z., Lv,D.J., Wang,C., Xie,T.,
            Chen,H., Chen,Z.S., Zeng,J. and Zhao,S.C.
  TITLE     NAT10 Promotes Prostate Cancer Growth and Metastasis by Acetylating
            mRNAs of HMGA1 and KRT8
  JOURNAL   Adv Sci (Weinh) 11 (32), e2310131 (2024)
   PUBMED   38922788
  REMARK    GeneRIF: NAT10 Promotes Prostate Cancer Growth and Metastasis by
            Acetylating mRNAs of HMGA1 and KRT8.
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Wang,L., Zhang,J., Xia,M., Liu,C., Zu,X. and Zhong,J.
  TITLE     High Mobility Group A1 (HMGA1): Structure, Biological Function, and
            Therapeutic Potential
  JOURNAL   Int J Biol Sci 18 (11), 4414-4431 (2022)
   PUBMED   35864955
  REMARK    GeneRIF: High Mobility Group A1 (HMGA1): Structure, Biological
            Function, and Therapeutic Potential.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 107)
  AUTHORS   Sumter,T.F., Xian,L., Huso,T., Koo,M., Chang,Y.T., Almasri,T.N.,
            Chia,L., Inglis,C., Reid,D. and Resar,L.M.
  TITLE     The High Mobility Group A1 (HMGA1) Transcriptome in Cancer and
            Development
  JOURNAL   Curr Mol Med 16 (4), 353-393 (2016)
   PUBMED   26980699
  REMARK    Review article
REFERENCE   6  (residues 1 to 107)
  AUTHORS   Friedmann,M., Holth,L.T., Zoghbi,H.Y. and Reeves,R.
  TITLE     Organization, inducible-expression and chromosome localization of
            the human HMG-I(Y) nonhistone protein gene
  JOURNAL   Nucleic Acids Res 21 (18), 4259-4267 (1993)
   PUBMED   8414980
REFERENCE   7  (residues 1 to 107)
  AUTHORS   Nissen,M.S., Langan,T.A. and Reeves,R.
  TITLE     Phosphorylation by cdc2 kinase modulates DNA binding activity of
            high mobility group I nonhistone chromatin protein
  JOURNAL   J Biol Chem 266 (30), 19945-19952 (1991)
   PUBMED   1939057
REFERENCE   8  (residues 1 to 107)
  AUTHORS   Reeves,R. and Nissen,M.S.
  TITLE     The A.T-DNA-binding domain of mammalian high mobility group I
            chromosomal proteins. A novel peptide motif for recognizing DNA
            structure
  JOURNAL   J Biol Chem 265 (15), 8573-8582 (1990)
   PUBMED   1692833
REFERENCE   9  (residues 1 to 107)
  AUTHORS   Eckner,R. and Birnstiel,M.L.
  TITLE     Cloning of cDNAs coding for human HMG I and HMG Y proteins: both
            are capable of binding to the octamer sequence motif
  JOURNAL   Nucleic Acids Res 17 (15), 5947-5959 (1989)
   PUBMED   2505228
REFERENCE   10 (residues 1 to 107)
  AUTHORS   Johnson,K.R., Lehn,D.A. and Reeves,R.
  TITLE     Alternative processing of mRNAs encoding mammalian chromosomal
            high-mobility-group proteins HMG-I and HMG-Y
  JOURNAL   Mol Cell Biol 9 (5), 2114-2123 (1989)
   PUBMED   2701943
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB029421.1, BE269847.1,
            AL354740.29 and BC008832.2.
            
            Summary: This gene encodes a chromatin-associated protein involved
            in the regulation of gene transcription, integration of
            retroviruses into chromosomes, and the metastatic progression of
            cancer cells. The encoded protein preferentially binds to the minor
            groove of AT-rich regions in double-stranded DNA. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. Pseudogenes of this gene have been identified on
            multiple chromosomes. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (12) uses an alternate splice site
            in the 5' UTR compared to variant 1. Variants 1, 3, 9, 10, 12, and
            13 encode isoform (a, also called HMG-I).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB029421.1, BE396787.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154529, SAMEA2155751
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..107
                     /product="high mobility group protein HMG-I/HMG-Y isoform
                     a"
                     /note="nonhistone chromosomal high-mobility group protein
                     HMG-I/HMG-Y; high mobility group protein HMG-I/HMG-Y; high
                     mobility group protein R; high mobility group protein A1"
                     /calculated_mol_wt=11545
     Region          1..107
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17096.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P17095; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            7
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P17095; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            15
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            26
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:12653562,
                     ECO:0000269|PubMed:15835918; Omega-N-methylarginine,
                     alternate. /evidence=ECO:0000269|PubMed:12653562,
                     ECO:0000269|PubMed:15835918; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by HIPK2 and CDC2.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P17096.3)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17960875,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P17096.3)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P17096.3)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Region          53..77
                     /region_name="Interaction with HIPK2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P17096.3)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by HIPK2 and CDC2.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P17096.3)"
     Site            58
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6, alternate.
                     /evidence=ECO:0000269|PubMed:16159886;
                     Omega-N-methylarginine, by PRMT6, alternate.
                     /evidence=ECO:0000269|PubMed:16159886; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            60
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6, alternate.
                     /evidence=ECO:0000269|PubMed:16159886;
                     Omega-N-methylarginine, by PRMT6, alternate.
                     /evidence=ECO:0000269|PubMed:16159886; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17960875; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by HIPK2 and CDC2.
                     /evidence=ECO:0000269|PubMed:12653562; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15835918,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P17096.3)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK.
                     /evidence=ECO:0000269|PubMed:15835918,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P17096.3)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK.
                     /evidence=ECO:0000269|PubMed:15835918,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P17096.3)"
     CDS             1..107
                     /gene="HMGA1"
                     /gene_synonym="HMG-R; HMGA1A; HMGIY"
                     /coded_by="NM_001319082.2:270..593"
                     /note="isoform a is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS4789.1"
                     /db_xref="GeneID:3159"
                     /db_xref="HGNC:HGNC:5010"
                     /db_xref="MIM:600701"
ORIGIN      
        1 msessskssq plaskqekdg tekrgrgrpr kqppvspgta lvgsqkepse vptpkrprgr
       61 pkgsknkgaa ktrkttttpg rkprgrpkkl ekeeeegisq esseeeq
//
LOCUS       NP_001317096             532 aa            linear   PRI 21-NOV-2025
DEFINITION  rab11 family-interacting protein 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001317096 XP_005269686
VERSION     NP_001317096.1
DBSOURCE    REFSEQ: accession NM_001330167.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 532)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 532)
  AUTHORS   Cullis,D.N., Philip,B., Baleja,J.D. and Feig,L.A.
  TITLE     Rab11-FIP2, an adaptor protein connecting cellular components
            involved in internalization and recycling of epidermal growth
            factor receptors
  JOURNAL   J Biol Chem 277 (51), 49158-49166 (2002)
   PUBMED   12364336
REFERENCE   7  (residues 1 to 532)
  AUTHORS   Lindsay,A.J. and McCaffrey,M.W.
  TITLE     Rab11-FIP2 functions in transferrin recycling and associates with
            endosomal membranes via its COOH-terminal domain
  JOURNAL   J Biol Chem 277 (30), 27193-27199 (2002)
   PUBMED   11994279
  REMARK    GeneRIF: Rab11-FIP2 functions downstream of Rab11 in endosomal
            trafficking.
REFERENCE   8  (residues 1 to 532)
  AUTHORS   Wallace,D.M., Lindsay,A.J., Hendrick,A.G. and McCaffrey,M.W.
  TITLE     The novel Rab11-FIP/Rip/RCP family of proteins displays extensive
            homo- and hetero-interacting abilities
  JOURNAL   Biochem Biophys Res Commun 292 (4), 909-915 (2002)
   PUBMED   11944901
REFERENCE   9  (residues 1 to 532)
  AUTHORS   Hales,C.M., Griner,R., Hobdy-Henderson,K.C., Dorn,M.C., Hardy,D.,
            Kumar,R., Navarre,J., Chan,E.K., Lapierre,L.A. and Goldenring,J.R.
  TITLE     Identification and characterization of a family of
            Rab11-interacting proteins
  JOURNAL   J Biol Chem 276 (42), 39067-39075 (2001)
   PUBMED   11495908
REFERENCE   10 (residues 1 to 532)
  AUTHORS   Prekeris,R., Davies,J.M. and Scheller,R.H.
  TITLE     Identification of a novel Rab11/25 binding domain present in Eferin
            and Rip proteins
  JOURNAL   J Biol Chem 276 (42), 38966-38970 (2001)
   PUBMED   11481332
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC022395.4, DQ013303.1 and R52658.1.
            
            On Aug 18, 2016 this sequence version replaced XP_005269686.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2405215.1,
                                           SRR14038193.90873.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267760 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.11"
     Protein         1..532
                     /product="rab11 family-interacting protein 2 isoform 2"
                     /note="rab11 family-interacting protein 2; RAB11 family
                     interacting protein 2 (class I)"
                     /calculated_mol_wt=60483
     Region          15..141
                     /region_name="C2_Rab11-FIP_classI"
                     /note="C2 domain found in Rab11-family interacting
                     proteins (FIP) class I; cd08682"
                     /db_xref="CDD:176064"
     Region          472..519
                     /region_name="RBD-FIP"
                     /note="FIP domain; pfam09457"
                     /db_xref="CDD:462805"
     CDS             1..532
                     /gene="RAB11FIP2"
                     /gene_synonym="nRip11; Rab11-FIP2"
                     /coded_by="NM_001330167.2:779..2377"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS81512.1"
                     /db_xref="GeneID:22841"
                     /db_xref="HGNC:HGNC:29152"
                     /db_xref="MIM:608599"
ORIGIN      
        1 mmlseqaqkw fpthvqvtvl qakdlkpkgk sgtndtytii qlgkekysts vaektlepvw
       61 keeasfelpg lliqgspeky ilflivmhrs lvgldkflgq vainlndife dkqrrktewf
      121 rleskqgkri knrgeikvni qfmrnnmtas mfdlsmkdkt rspfaklkdk mkgrkndgtf
      181 sdtssaiips thmpdansef ssgeiqmksk pkkpfllgpq rlssahsmsd lsgshmssek
      241 lkagtigqth llghqldsfg tvpesgslks phrrtlsfdt skmnqpdsiv degelcfgrq
      301 ndpftnvtas lpqkfatlpr kknpfeesse twdssmnlfs kpieirkenk rekrekvslf
      361 ervtgkkdsr rsdklnnggs dspcdlkspn afsenrqdyf dyestnpfta kfrasnimps
      421 srntlltpav aewrgslrwa elfhmsptsn edlrkipdsn pfdatagyrs ltyeevlqel
      481 vkhkellrrk dthireledy idnllvrvme etpsilrvpy epsrkagkfs ns
//
LOCUS       NP_001161880             817 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 1 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001161880
VERSION     NP_001161880.1
DBSOURCE    REFSEQ: accession NM_001168408.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 817)
  AUTHORS   Ruhle,F., Witten,A., Barysenka,A., Huge,A., Arning,A., Heller,C.,
            Krumpel,A., Mesters,R., Franke,A., Lieb,W., Riemenschneider,M.,
            Hiersche,M., Limperger,V., Nowak-Gottl,U. and Stoll,M.
  TITLE     Rare genetic variants in SMAP1, B3GAT2, and RIMS1 contribute to
            pediatric venous thromboembolism
  JOURNAL   Blood 129 (6), 783-790 (2017)
   PUBMED   28011674
  REMARK    GeneRIF: The study identified a region on chromosome 6 comprising
            the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus
            for pediatric venous thromboembolism.
REFERENCE   6  (residues 1 to 817)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 817)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
REFERENCE   8  (residues 1 to 817)
  AUTHORS   Schoch,S., Castillo,P.E., Jo,T., Mukherjee,K., Geppert,M., Wang,Y.,
            Schmitz,F., Malenka,R.C. and Sudhof,T.C.
  TITLE     RIM1alpha forms a protein scaffold for regulating neurotransmitter
            release at the active zone
  JOURNAL   Nature 415 (6869), 321-326 (2002)
   PUBMED   11797009
REFERENCE   9  (residues 1 to 817)
  AUTHORS   Coppola,T., Magnin-Luthi,S., Perret-Menoud,V., Gattesco,S.,
            Schiavo,G. and Regazzi,R.
  TITLE     Direct interaction of the Rab3 effector RIM with Ca2+ channels,
            SNAP-25, and synaptotagmin
  JOURNAL   J Biol Chem 276 (35), 32756-32762 (2001)
   PUBMED   11438518
REFERENCE   10 (residues 1 to 817)
  AUTHORS   Betz,A., Thakur,P., Junge,H.J., Ashery,U., Rhee,J.S., Scheuss,V.,
            Rosenmund,C., Rettig,J. and Brose,N.
  TITLE     Functional interaction of the active zone proteins Munc13-1 and
            RIM1 in synaptic vesicle priming
  JOURNAL   Neuron 30 (1), 183-196 (2001)
   PUBMED   11343654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK295001.1, AL035633.18 and
            BC036608.1.
            
            Summary: The protein encoded by this gene is a RAS gene superfamily
            member that regulates synaptic vesicle exocytosis. This gene also
            plays a role in the regulation of voltage-gated calcium channels
            during neurotransmitter and insulin release. Mutations have
            suggested a role cognition and have been identified as the cause of
            cone-rod dystrophy type 7. Multiple transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Mar 2012].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and has
            multiple coding region differences, compared to variant 1. The
            resulting isoform (3) has a shorter and distinct N-terminus and
            internal differences, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.152086.1,
                                           SRR1803612.190572.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..817
                     /product="regulating synaptic membrane exocytosis protein
                     1 isoform 3"
                     /note="RAB3-interacting protein 2; rab3-interacting
                     molecule 1; rab-3-interacting protein 2"
                     /calculated_mol_wt=91400
     Region          68..164
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(89..95,110,113,143,147,150..151)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          216..342
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(247,253,308,310,318)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          648..793
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(705,709..710,712,715,743,745,747,791..792)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..817
                     /gene="RIMS1"
                     /gene_synonym="CORD7; RAB3IP2; RIM; RIM1"
                     /coded_by="NM_001168408.2:231..2684"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55029.1"
                     /db_xref="GeneID:22999"
                     /db_xref="HGNC:HGNC:17282"
                     /db_xref="MIM:606629"
ORIGIN      
        1 mcapgihvss egweevrsvd seegtiearr avagdldyyw ldpatwhsre tspisshpvt
       61 wqpskegdrl igrvilnkrt tmpkdsgall glkvvggkmt dlgrlgafit kvkkgsladv
      121 vghlragdev lewngkplpg atneevynii lesksepqve iivsrpigdi pripesshpp
      181 lesssssfes qkmerpsisv isptspgalk dapqvlpgql svklwydkvg hqlivnvlqa
      241 tdlparvdgr prnpyvkmyf lpdrsdkskr rtktvkkile pkwnqtfvys hvhrrdfrer
      301 mleitvwdqp rvqeeesefl geilieleta llddephwyk lqthdesslp lpqpspfmpr
      361 rhihgesssk klqrsqrisd sdisdyevdd gigvvppvgy rssareskst tltvpeqqrt
      421 thhrsrsvsp hrgndqgkpr srlpnvplqr sldeihptrr srsptrhhda srspvdhrtr
      481 dvdsqylseq dsellmlpra krgrsaeclh ttselqpfld rarsastncl rpdtslhspe
      541 rermhrqrsp tqsppadtsf ssrrgrqlpq vpvrsgsieq esghkklkst iqrstetgma
      601 aemrkmvrqp srestdgsin syssegnlif pgvrlgadsq fsdfldglgp aqlvgrqtla
      661 tpamgdiqig medkkgqlev evirarsltq kpgskstpap yvkvylleng aciakkktri
      721 arktldplyq qslvfdespq gkvlqvivwg dygrmdhkcf mgvaqillee ldlssmvigw
      781 yklfppsslv dptltpltrr asqsslesst gppcirs
//
LOCUS       NP_001014834             438 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase PAK 4 isoform 2 [Homo sapiens].
ACCESSION   NP_001014834
VERSION     NP_001014834.1
DBSOURCE    REFSEQ: accession NM_001014834.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Zhang,J., Song,Y., Ahn,A.R., Park,H.S., Park,S.H., Moon,Y.J.,
            Kim,K.M. and Jang,K.Y.
  TITLE     PAK4 Is Involved in the Stabilization of PD-L1 and the Resistance
            to Doxorubicin in Osteosarcoma and Predicts the Survival of
            Diagnosed Patients
  JOURNAL   Cells 13 (17), 1444 (2024)
   PUBMED   39273017
  REMARK    GeneRIF: PAK4 Is Involved in the Stabilization of PD-L1 and the
            Resistance to Doxorubicin in Osteosarcoma and Predicts the Survival
            of Diagnosed Patients.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Wu,D., Yu,H.C., Cha,H.N., Park,S., Lee,Y., Yoon,S.J., Park,S.Y.,
            Park,B.H. and Bae,E.J.
  TITLE     PAK4 phosphorylates and inhibits AMPKalpha to control glucose
            uptake
  JOURNAL   Nat Commun 15 (1), 6858 (2024)
   PUBMED   39127697
  REMARK    GeneRIF: PAK4 phosphorylates and inhibits AMPKalpha to control
            glucose uptake.
            Erratum:[Nat Commun. 2025 Oct 13;16(1):9055. doi:
            10.1038/s41467-025-64713-3. PMID: 41083498]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Chi,X.J., Song,Y.B., Zhang,H., Wei,L.Q., Gao,Y., Miao,X.J.,
            Yang,S.T., Lin,C.Y., Lan,D. and Zhang,X.
  TITLE     TBC1D10B promotes tumor progression in colon cancer via
            PAK4-mediated promotion of the PI3K/AKT/mTOR pathway
  JOURNAL   Apoptosis 29 (7-8), 1185-1197 (2024)
   PUBMED   38824479
  REMARK    GeneRIF: TBC1D10B promotes tumor progression in colon cancer via
            PAK4-mediated promotion of the PI3K/AKT/mTOR pathway.
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Tang,L., Ye,H., Chen,L., Dong,W., Hu,X. and Yu,L.
  TITLE     Tumorigenic role of Pak4 in ovarian cancer and its correlation with
            immune infiltration
  JOURNAL   BMC Med Genomics 17 (1), 148 (2024)
   PUBMED   38807162
  REMARK    GeneRIF: Tumorigenic role of Pak4 in ovarian cancer and its
            correlation with immune infiltration.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 438)
  AUTHORS   Lu,Y., Pan,Z.Z., Devaux,Y. and Ray,P.
  TITLE     p21-activated protein kinase 4 (PAK4) interacts with the
            keratinocyte growth factor receptor and participates in
            keratinocyte growth factor-mediated inhibition of oxidant-induced
            cell death
  JOURNAL   J Biol Chem 278 (12), 10374-10380 (2003)
   PUBMED   12529371
  REMARK    GeneRIF: PAK4 interacts with KGF receptor and mediate
            anti-apoptosis effects of KGF on epithelial cells.
REFERENCE   7  (residues 1 to 438)
  AUTHORS   Zhang,H., Li,Z., Viklund,E.K. and Stromblad,S.
  TITLE     P21-activated kinase 4 interacts with integrin alpha v beta 5 and
            regulates alpha v beta 5-mediated cell migration
  JOURNAL   J Cell Biol 158 (7), 1287-1297 (2002)
   PUBMED   12356872
REFERENCE   8  (residues 1 to 438)
  AUTHORS   Dan,C., Kelly,A., Bernard,O. and Minden,A.
  TITLE     Cytoskeletal changes regulated by the PAK4 serine/threonine kinase
            are mediated by LIM kinase 1 and cofilin
  JOURNAL   J Biol Chem 276 (34), 32115-32121 (2001)
   PUBMED   11413130
REFERENCE   9  (residues 1 to 438)
  AUTHORS   Bagrodia,S. and Cerione,R.A.
  TITLE     Pak to the future
  JOURNAL   Trends Cell Biol 9 (9), 350-355 (1999)
   PUBMED   10461188
  REMARK    Review article
REFERENCE   10 (residues 1 to 438)
  AUTHORS   Abo,A., Qu,J., Cammarano,M.S., Dan,C., Fritsch,A., Baud,V.,
            Belisle,B. and Minden,A.
  TITLE     PAK4, a novel effector for Cdc42Hs, is implicated in the
            reorganization of the actin cytoskeleton and in the formation of
            filopodia
  JOURNAL   EMBO J 17 (22), 6527-6540 (1998)
   PUBMED   9822598
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG773480.1, AL834236.1,
            AB032968.1 and AC011443.6.
            
            Summary: PAK proteins, a family of serine/threonine p21-activating
            kinases, include PAK1, PAK2, PAK3 and PAK4. PAK proteins are
            critical effectors that link Rho GTPases to cytoskeleton
            reorganization and nuclear signaling. They serve as targets for the
            small GTP binding proteins Cdc42 and Rac and have been implicated
            in a wide range of biological activities. PAK4 interacts
            specifically with the GTP-bound form of Cdc42Hs and weakly
            activates the JNK family of MAP kinases. PAK4 is a mediator of
            filopodia formation and may play a role in the reorganization of
            the actin cytoskeleton. Multiple alternatively spliced transcript
            variants encoding distinct isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (5) lacks an exon in the 5' UTR
            and an in-frame exon in the coding region, as compared to variant
            1. The encoded isoform (2) thus lacks an internal segment, as
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL834236.1, AK294586.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..438
                     /product="serine/threonine-protein kinase PAK 4 isoform 2"
                     /EC_number="2.7.11.1"
                     /note="protein kinase related to S. cerevisiae STE20,
                     effector for Cdc42Hs; p21(CDKN1A)-activated kinase 4;
                     serine/threonine-protein kinase PAK 4; p21 protein
                     (Cdc42/Rac)-activated kinase 4"
                     /calculated_mol_wt=48137
     Region          10..55
                     /region_name="CRIB_PAK_like"
                     /note="PAK (p21 activated kinase) Binding Domain (PBD),
                     binds Cdc42p- and/or Rho-like small GTPases; also known as
                     the Cdc42/Rac interactive binding (CRIB) motif; has been
                     shown to inhibit transcriptional activation and cell
                     transformation mediated by the...; cd01093"
                     /db_xref="CDD:238526"
     Site            order(11,14,17,19,22,39,43)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238526"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O96013.1)"
     Region          147..438
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(174..177,180,182,195,197,226,242..245,287,291..292,
                     294,304..305)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..438
                     /gene="PAK4"
                     /coded_by="NM_001014834.3:157..1473"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS33019.1"
                     /db_xref="GeneID:10298"
                     /db_xref="HGNC:HGNC:16059"
                     /db_xref="MIM:605451"
ORIGIN      
        1 mfgkrkkrve isapsnfehr vhtgfdqheq kftglprqwq slieesarrp kplvdpacit
       61 siqpgapkge phdvapngps agglaipqss ssssrpptra rgapspgvlg phasepqlap
      121 pactpaapav pgppgprspq repqrvsheq fraalqlvvd pgdprsyldn fikigegstg
      181 ivciatvrss gklvavkkmd lrkqqrrell fnevvimrdy qhenvvemyn sylvgdelwv
      241 vmefleggal tdivthtrmn eeqiaavcla vlqalsvlha qgvihrdiks dsillthdgr
      301 vklsdfgfca qvskevprrk slvgtpywma pelisrlpyg pevdiwslgi mviemvdgep
      361 pyfnepplka mkmirdnlpp rlknlhkvsp slkgfldrll vrdpaqrata aellkhpfla
      421 kagppasivp lmrqnrtr
//
LOCUS       NP_620708                382 aa            linear   PRI 21-NOV-2025
DEFINITION  mitogen-activated protein kinase 9 isoform beta1 [Homo sapiens].
ACCESSION   NP_620708
VERSION     NP_620708.1
DBSOURCE    REFSEQ: accession NM_139069.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Ishibashi,R., Itani,M., Kawashima,A., Arakawa,Y. and Aoki,T.
  TITLE     JNK2-MMP-9 axis facilitates the progression of intracranial
            aneurysms
  JOURNAL   Sci Rep 14 (1), 19458 (2024)
   PUBMED   39169203
  REMARK    GeneRIF: JNK2-MMP-9 axis facilitates the progression of
            intracranial aneurysms.
            Erratum:[Sci Rep. 2025 Sep 18;15(1):32593. doi:
            10.1038/s41598-025-17846-w. PMID: 40968147]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Yang,F., Zhuang,Z., Liu,C., Li,F. and Zhou,J.
  TITLE     Overexpression of circZNF720 Inhibits Hepatocellular Carcinoma
            Progression by Regulating miR-421/MAPK9
  JOURNAL   Mol Biotechnol 66 (5), 1165-1173 (2024)
   PUBMED   38159171
  REMARK    GeneRIF: Overexpression of circZNF720 Inhibits Hepatocellular
            Carcinoma Progression by Regulating miR-421/MAPK9.
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Wang,K., Lu,Q., Luo,Y., Yu,G., Wang,Z., Lin,J., Tan,Z., Lao,Y.,
            Liu,S. and Yang,H.
  TITLE     Circ_MAPK9 promotes STAT3 and LDHA expression by silencing
            miR-642b-3p and affects the progression of hepatocellular carcinoma
  JOURNAL   Biol Direct 19 (1), 4 (2024)
   PUBMED   38163874
  REMARK    GeneRIF: Circ_MAPK9 promotes STAT3 and LDHA expression by silencing
            miR-642b-3p and affects the progression of hepatocellular
            carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Wang,L., Guo,M., Gao,L., Liu,K., Bai,J. and Liu,Z.
  TITLE     JNK2 Promotes Progression of Esophageal Squamous Cell Carcinoma via
            Inhibiting Axin2
  JOURNAL   Curr Pharm Des 29 (37), 2977-2987 (2023)
   PUBMED   37957865
  REMARK    GeneRIF: JNK2 Promotes Progression of Esophageal Squamous Cell
            Carcinoma via Inhibiting Axin2.
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Livingstone,C., Patel,G. and Jones,N.
  TITLE     ATF-2 contains a phosphorylation-dependent transcriptional
            activation domain
  JOURNAL   EMBO J 14 (8), 1785-1797 (1995)
   PUBMED   7737129
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Kallunki,T., Su,B., Tsigelny,I., Sluss,H.K., Derijard,B., Moore,G.,
            Davis,R. and Karin,M.
  TITLE     JNK2 contains a specificity-determining region responsible for
            efficient c-Jun binding and phosphorylation
  JOURNAL   Genes Dev 8 (24), 2996-3007 (1994)
   PUBMED   8001819
REFERENCE   8  (residues 1 to 382)
  AUTHORS   Sluss,H.K., Barrett,T., Derijard,B. and Davis,R.J.
  TITLE     Signal transduction by tumor necrosis factor mediated by JNK
            protein kinases
  JOURNAL   Mol Cell Biol 14 (12), 8376-8384 (1994)
   PUBMED   7969172
REFERENCE   9  (residues 1 to 382)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   10 (residues 1 to 382)
  AUTHORS   Denys,H., Desmet,R., Stragier,M., Vergison,R. and Lemahieu,S.F.
  TITLE     Cystitis emphysematosa
  JOURNAL   Acta Urol Belg 45 (4), 327-331 (1977)
   PUBMED   602896
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008610.7, DB451562.1,
            AK289638.1, U35002.1 and AC104115.3.
            
            Summary: The protein encoded by this gene is a member of the MAP
            kinase family. MAP kinases act as an integration point for multiple
            biochemical signals, and are involved in a wide variety of cellular
            processes such as proliferation, differentiation, transcription
            regulation and development. This kinase targets specific
            transcription factors, and thus mediates immediate-early gene
            expression in response to various cell stimuli. It is most closely
            related to MAPK8, both of which are involved in UV radiation
            induced apoptosis, thought to be related to the cytochrome
            c-mediated cell death pathway. This gene and MAPK8 are also known
            as c-Jun N-terminal kinases. This kinase blocks the ubiquitination
            of tumor suppressor p53, and thus it increases the stability of p53
            in nonstressed cells. Studies of this gene's mouse counterpart
            suggest a key role in T-cell differentiation. Several alternatively
            spliced transcript variants encoding distinct isoforms have been
            reported. [provided by RefSeq, Sep 2008].
            
            Transcript Variant: This variant (JNK2-b1) uses a different
            acceptor splice site in the last coding exon compared to transcript
            variant JNK2-b2, resulting in a frameshift and a shorter isoform
            (JNK2 beta1) with a different C-terminus, compared to isoform JNK2
            beta2. The JNK2-b1 variant differs from the JNK2-a1 variant in the
            use of an alternate internal coding exon of the same length. Thus,
            JNK2 beta1 isoform is the same length as JNK2 alpha1 isoform, with
            a few aa differences in an internal protein segment.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.194750.1,
                                           SRR1803611.261889.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..382
                     /product="mitogen-activated protein kinase 9 isoform
                     beta1"
                     /EC_number="2.7.11.24"
                     /note="c-Jun N-terminal kinase 2; stress-activated protein
                     kinase JNK2; MAP kinase 9; c-Jun kinase 2; MAPK 9;
                     stress-activated protein kinase 1a"
                     /calculated_mol_wt=44092
     Region          25..360
                     /region_name="STKc_JNK"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     c-Jun N-terminal Kinase; cd07850"
                     /db_xref="CDD:270840"
     Site            order(32..38,40,53,55,72,86,108..114,116..117,151,153,
                     155..156,158,168..169,172,183,185..188,190,227)
                     /site_type="active"
                     /db_xref="CDD:270840"
     Site            order(32..38,40,53,55,86,108..114,158,168)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270840"
     Site            order(72,116,151,153,172,183,185..188,190,227)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270840"
     Site            order(112,118,127,130,159..163,323..324,326,329)
                     /site_type="other"
                     /note="KIM docking site [polypeptide binding]"
                     /db_xref="CDD:270840"
     Site            order(168..178,182..190)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270840"
     CDS             1..382
                     /gene="MAPK9"
                     /gene_synonym="JNK-55; JNK2; JNK2A; JNK2ALPHA; JNK2B;
                     JNK2BETA; p54a; p54aSAPK; PRKM9; SAPK; SAPK1a"
                     /coded_by="NM_139069.3:284..1432"
                     /note="isoform beta1 is encoded by transcript variant
                     JNK2-b1"
                     /db_xref="CCDS:CCDS43410.1"
                     /db_xref="GeneID:5601"
                     /db_xref="HGNC:HGNC:6886"
                     /db_xref="MIM:602896"
ORIGIN      
        1 msdskcdsqf ysvqvadstf tvlkryqqlk pigsgaqgiv caafdtvlgi nvavkklsrp
       61 fqnqthakra yrelvllkcv nhkniislln vftpqktlee fqdvylvmel mdanlcqvih
      121 meldhermsy llyqmlcgik hlhsagiihr dlkpsnivvk sdctlkildf glartactnf
      181 mmtpyvvtry yrapevilgm gykenvdiws vgcimaemvl hkvlfpgrdy idqwnkvieq
      241 lgtpsaefmk klqptvrnyv enrpkypgik feelfpdwif pseserdkik tsqardllsk
      301 mlvidpdkri svdealrhpy itvwydpaea eapppqiyda qleerehaie ewkeliykev
      361 mdweerskng vvkdqpsaqm qq
//
LOCUS       NP_001273048             156 aa            linear   PRI 21-NOV-2025
DEFINITION  coiled-coil domain-containing protein 90B, mitochondrial isoform d
            [Homo sapiens].
ACCESSION   NP_001273048
VERSION     NP_001273048.1
DBSOURCE    REFSEQ: accession NM_001286119.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 156)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 156)
  AUTHORS   Adlakha,J., Karamichali,I., Sangwallek,J., Deiss,S., Bar,K.,
            Coles,M., Hartmann,M.D., Lupas,A.N. and Hernandez Alvarez,B.
  TITLE     Characterization of MCU-Binding Proteins MCUR1 and CCDC90B -
            Representatives of a Protein Family Conserved in Prokaryotes and
            Eukaryotic Organelles
  JOURNAL   Structure 27 (3), 464-475 (2019)
   PUBMED   30612859
  REMARK    GeneRIF: Using MCUR1, the functionally characterized paralog of
            study the role of individual domains, results find that the
            conserved head domain in CCDC90B interacts directly with
            mitochondrial calcium uniporter and is destabilized upon Ca(2+)
            binding.
REFERENCE   7  (residues 1 to 156)
  AUTHORS   Tomar,D., Dong,Z., Shanmughapriya,S., Koch,D.A., Thomas,T.,
            Hoffman,N.E., Timbalia,S.A., Goldman,S.J., Breves,S.L.,
            Corbally,D.P., Nemani,N., Fairweather,J.P., Cutri,A.R., Zhang,X.,
            Song,J., Jana,F., Huang,J., Barrero,C., Rabinowitz,J.E.,
            Luongo,T.S., Schumacher,S.M., Rockman,M.E., Dietrich,A., Merali,S.,
            Caplan,J., Stathopulos,P., Ahima,R.S., Cheung,J.Y., Houser,S.R.,
            Koch,W.J., Patel,V., Gohil,V.M., Elrod,J.W., Rajan,S. and Madesh,M.
  TITLE     MCUR1 Is a Scaffold Factor for the MCU Complex Function and
            Promotes Mitochondrial Bioenergetics
  JOURNAL   Cell Rep 15 (8), 1673-1685 (2016)
   PUBMED   27184846
REFERENCE   8  (residues 1 to 156)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 156)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP000873.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.296555.1,
                                           SRR14372079.3288520.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.1"
     Protein         1..156
                     /product="coiled-coil domain-containing protein 90B,
                     mitochondrial isoform d"
                     /note="coiled-coil domain-containing protein 90B,
                     mitochondrial"
                     /calculated_mol_wt=18311
     Region          <10..155
                     /region_name="CCDC90-like"
                     /note="Coiled-coil domain-containing protein 90-like;
                     pfam07798"
                     /db_xref="CDD:462268"
     CDS             1..156
                     /gene="CCDC90B"
                     /gene_synonym="MDS011; MDS025"
                     /coded_by="NM_001286119.3:282..752"
                     /note="isoform d is encoded by transcript variant 5"
                     /db_xref="GeneID:60492"
                     /db_xref="HGNC:HGNC:28108"
                     /db_xref="MIM:620753"
ORIGIN      
        1 mhwfrtwklm eitvqqlmah ldairkdmvi leksefanlr aenekmkiel dqvkqqlmhe
       61 tsriradnkl dinlersrvt dmftdqekql mettteftkk dtqtksiise tsnkidaeia
      121 slktlmesnk letirylaas vftclaialg fyrfwk
//
LOCUS       NP_001121599             553 aa            linear   PRI 21-NOV-2025
DEFINITION  glycerol kinase isoform c [Homo sapiens].
ACCESSION   NP_001121599
VERSION     NP_001121599.1
DBSOURCE    REFSEQ: accession NM_001128127.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Ying,F., Chen,X. and Lv,L.
  TITLE     Glycerol kinase enzyme is a prognostic predictor in esophageal
            carcinoma and is associated with immune cell infiltration
  JOURNAL   Sci Rep 14 (1), 3922 (2024)
   PUBMED   38365953
  REMARK    GeneRIF: Glycerol kinase enzyme is a prognostic predictor in
            esophageal carcinoma and is associated with immune cell
            infiltration.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Rani,R.M., Syngkli,S., Nongkhlaw,J. and Das,B.
  TITLE     Expression and characterisation of human glycerol kinase: the role
            of solubilising agents and molecular chaperones
  JOURNAL   Biosci Rep 43 (4) (2023)
   PUBMED   37021775
  REMARK    GeneRIF: Expression and characterisation of human glycerol kinase:
            the role of solubilising agents and molecular chaperones.
            Erratum:[Biosci Rep. 2023 Oct 31;43(10):BSR-2022-2258_COR. doi:
            10.1042/BSR-2022-2258_COR. PMID: 37860917]
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 553)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 553)
  AUTHORS   Sargent,C.A., Young,C., Marsh,S., Ferguson-Smith,M.A. and
            Affara,N.A.
  TITLE     The glycerol kinase gene family: structure of the Xp gene, and
            related intronless retroposons
  JOURNAL   Hum Mol Genet 3 (8), 1317-1324 (1994)
   PUBMED   7987308
REFERENCE   7  (residues 1 to 553)
  AUTHORS   Achermann,J.C. and Vilain,E.J.
  TITLE     NR0B1-Related Adrenal Hypoplasia Congenita
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301604
REFERENCE   8  (residues 1 to 553)
  AUTHORS   Love,D.R., Bloomfield,J.F., Kenwrick,S.J., Yates,J.R. and
            Davies,K.E.
  TITLE     Physical mapping distal to the DMD locus
  JOURNAL   Genomics 8 (1), 106-112 (1990)
   PUBMED   2081587
REFERENCE   9  (residues 1 to 553)
  AUTHORS   Pillers,D.A., Weleber,R.G., Powell,B.R., Hanna,C.E., Magenis,R.E.
            and Buist,N.R.
  TITLE     Aland Island eye disease (Forsius-Eriksson ocular albinism) and an
            Xp21 deletion in a patient with Duchenne muscular dystrophy,
            glycerol kinase deficiency, and congenital adrenal hypoplasia
  JOURNAL   Am J Med Genet 36 (1), 23-28 (1990)
   PUBMED   2159212
REFERENCE   10 (residues 1 to 553)
  AUTHORS   Kaneko,M., Kurokawa,M. and Ishibashi,S.
  TITLE     Binding and function of mitochondrial glycerol kinase in comparison
            with those of mitochondrial hexokinase
  JOURNAL   Arch Biochem Biophys 237 (1), 135-141 (1985)
   PUBMED   2982325
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC042421.1, AK313215.1,
            AK294938.1, AA689298.1, AC112496.2 and AW300142.1.
            
            Summary: The protein encoded by this gene belongs to the FGGY
            kinase family. This protein is a key enzyme in the regulation of
            glycerol uptake and metabolism. It catalyzes the phosphorylation of
            glycerol by ATP, yielding ADP and glycerol-3-phosphate. Mutations
            in this gene are associated with glycerol kinase deficiency (GKD).
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Mar
            2011].
            
            Transcript Variant: This variant (3) lacks an in-frame coding exon
            in the mid-region, and contains an additional in-frame coding exon
            at the 3' end compared to variant 1. This results in a longer
            isoform (c) compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4275568.1,
                                           SRR18074969.3030619.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp21.2"
     Protein         1..553
                     /product="glycerol kinase isoform c"
                     /EC_number="2.7.1.30"
                     /note="ATP:glycerol 3-phosphotransferase; glycerokinase"
                     /calculated_mol_wt=60462
     Region          11..510
                     /region_name="ASKHA_NBD_FGGY_GK1-3-like"
                     /note="nucleotide-binding domain (NBD) of metazoan
                     glycerol kinase 1-3 (GK1-3) and similar proteins; cd07792"
                     /db_xref="CDD:466802"
     Site            526..546
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32189.3)"
     CDS             1..553
                     /gene="GK"
                     /gene_synonym="GK1; GKD"
                     /coded_by="NM_001128127.3:116..1777"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS48090.1"
                     /db_xref="GeneID:2710"
                     /db_xref="HGNC:HGNC:4289"
                     /db_xref="MIM:300474"
ORIGIN      
        1 maaskkavlg plvgavdqgt sstrflvfns ktaellshhq veikqefpre gwveqdpkei
       61 lhsvyeciek tceklgqlni disnikaigv snqrettvvw dkitgeplyn avvwldlrtq
      121 stveslskri pgnnnfvksk tglplstyfs avklrwlldn vrkvqkavee kralfgtids
      181 wliwsltggv nggvhctdvt nasrtmlfni hslewdkqlc effgipmeil pnvrssseiy
      241 glmkagaleg vpisgclgdq saalvgqmcf qigqakntyg tgcfllcntg hkcvfsdhgl
      301 lttvayklgr dkpvyyaleg svaiagavir wlrdnlgiik tseeieklak evgtsygcyf
      361 vpafsglyap ywepsargii cgltqftnkc hiafaaleav cfqtreilda mnrdcgipls
      421 hlqvdggmts nkilmqlqad ilyipvvkps mpettalgaa maagaaegvg vwslepedls
      481 avtmerfepq inaeeseiry stwkkavmks mgwvttqspe sgdpsifcsl plgffivssm
      541 vmligaryis gip
//
LOCUS       NP_001381361             717 aa            linear   PRI 21-NOV-2025
DEFINITION  SUN domain-containing protein 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001381361
VERSION     NP_001381361.1
DBSOURCE    REFSEQ: accession NM_001394432.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Zhang,Y., Kong,Y., Guo,H., Liu,Y., Zang,Y. and Li,J.
  TITLE     Inner nuclear membrane protein TMEM201 maintains endothelial cell
            migration and angiogenesis by interacting with the LINC complex
  JOURNAL   J Mol Cell Biol 14 (3) (2022)
   PUBMED   35311970
REFERENCE   4  (residues 1 to 717)
  AUTHORS   Cruz-Palomar,K., Hawkins,J., Vandal,C., Quenneville,J., Gagnon,E.
            and Lippe,R.
  TITLE     SUN2 Modulates the Propagation of HSV-1
  JOURNAL   J Virol 96 (9), e0045322 (2022)
   PUBMED   35435724
  REMARK    GeneRIF: SUN2 Modulates the Propagation of HSV-1.
REFERENCE   5  (residues 1 to 717)
  AUTHORS   Ji,J., Shen,J., Xu,Y., Xie,M., Qian,Q., Qiu,T., Shi,W., Ren,D.,
            Ma,J., Liu,W. and Liu,B.
  TITLE     FBXO2 targets glycosylated SUN2 for ubiquitination and degradation
            to promote ovarian cancer development
  JOURNAL   Cell Death Dis 13 (5), 442 (2022)
   PUBMED   35525855
  REMARK    GeneRIF: FBXO2 targets glycosylated SUN2 for ubiquitination and
            degradation to promote ovarian cancer development.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 717)
  AUTHORS   Hoffenberg,S., Liu,X., Nikolova,L., Hall,H.S., Dai,W., Baughn,R.E.,
            Dickey,B.F., Barbieri,M.A., Aballay,A., Stahl,P.D. and Knoll,B.J.
  TITLE     A novel membrane-anchored Rab5 interacting protein required for
            homotypic endosome fusion
  JOURNAL   J Biol Chem 275 (32), 24661-24669 (2000)
   PUBMED   10818110
REFERENCE   7  (residues 1 to 717)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   8  (residues 1 to 717)
  AUTHORS   Raff,J.W.
  TITLE     The missing (L) UNC?
  JOURNAL   Curr Biol 9 (18), R708-R710 (1999)
   PUBMED   10508607
  REMARK    Review article
REFERENCE   9  (residues 1 to 717)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
REFERENCE   10 (residues 1 to 717)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL021707.2.
            
            Summary: SUN1 (MIM 607723) and SUN2 are inner nuclear membrane
            (INM) proteins that play a major role in nuclear-cytoplasmic
            connection by formation of a 'bridge' across the nuclear envelope,
            known as the LINC complex, via interaction with the conserved
            luminal KASH domain of nesprins (e.g., SYNE1; MIM 608441) located
            in the outer nuclear membrane (ONM). The LINC complex provides a
            direct connection between the nuclear lamina and the cytoskeleton,
            which contributes to nuclear positioning and cellular rigidity
            (summary by Haque et al., 2010 [PubMed 19933576]).[supplied by
            OMIM, Nov 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2434520.1,
                                           SRR18074967.2110465.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..717
                     /product="SUN domain-containing protein 2 isoform 2"
                     /note="Sad1 unc-84 domain protein 2; protein unc-84
                     homolog B; SUN domain-containing protein 2; nuclear
                     envelope protein; rab5-interacting protein; sad1/unc-84
                     protein-like 2"
                     /calculated_mol_wt=80180
     Region          1..139
                     /region_name="LMNA-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH99.3)"
     Region          1..66
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH99.3)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12239280; propagated from
                     UniProtKB/Swiss-Prot (Q9UH99.3)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UH99.3)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12239280,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UH99.3)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BJS4; propagated from
                     UniProtKB/Swiss-Prot (Q9UH99.3)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BJS4; propagated from
                     UniProtKB/Swiss-Prot (Q9UH99.3)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BJS4; propagated from
                     UniProtKB/Swiss-Prot (Q9UH99.3)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12239280; propagated from
                     UniProtKB/Swiss-Prot (Q9UH99.3)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BJS4; propagated from
                     UniProtKB/Swiss-Prot (Q9UH99.3)"
     Site            213..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH99.3)"
     Region          <278..>517
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          400..454
                     /region_name="SUN2_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 2 and similar proteins; cd21438"
                     /db_xref="CDD:410604"
     Site            order(400,403..404,407,410..411,414..415,417..418,
                     421..422,424..425,428..429,431..432,435,438..439,442,
                     445..446,449..450,452..454)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:410604"
     Region          481..538
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          507..717
                     /region_name="Sufficient for interaction with SYNE1 and
                     SYNE2. /evidence=ECO:0000269|PubMed:22632968"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH99.3)"
     Region          581..715
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     Site            636
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q9UH99.3)"
     CDS             1..717
                     /gene="SUN2"
                     /gene_synonym="rab5IP; UNC84B"
                     /coded_by="NM_001394432.1:172..2325"
                     /note="isoform 2 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS13978.1"
                     /db_xref="GeneID:25777"
                     /db_xref="HGNC:HGNC:14210"
                     /db_xref="MIM:613569"
ORIGIN      
        1 msrrsqrltr ysqgdddgss ssggssvags qstlfkdspl rtlkrkssnm krlspapqlg
       61 pssdahtsyy seslvheswf pprssleelh gdanwgedlr vrrrrgtggs essrasglvg
      121 rkatedflgs ssgysseddy vgysdvdqqs sssrlrsavs ragsllwmva tspgrlfrll
      181 ywwagttwyr lttaaslldv fvltrrfssl ktflwfllpl llltcltyga wyfypyglqt
      241 fhpalvswwa akdsrrpdeg weardssphf qaeqrvmsrv hslerrleal aaefssnwqk
      301 eamrlerlel rqgapgqggg gglshedtla lleglvsrre aalkedfrre taariqeels
      361 alraehqqds edlfkkivra sqeseariqq lksewqsmtq esfqessvke lrrledqlag
      421 lqqelaalal kqssvaeevg llpqqiqavr ddvesqfpaw isqflarggg grvgllqree
      481 mqaqlreles kilthvaemq gksareaaas lsltlqkegv igvteeqvhh ivkqalqrys
      541 edrigladya lesggasvis trcsetyetk tallslfgip lwyhsqsprv ilqpdvhpgn
      601 cwafqgpqgf avvrlsarir ptavtlehvp kalspnstis sapkdfaifg fdedlqqegt
      661 llgkftydqd gepiqtfhfq aptmatyqvv elriltnwgh peytciyrfr vhgepah
//
LOCUS       NP_065790                757 aa            linear   PRI 21-NOV-2025
DEFINITION  cell cycle progression protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_065790
VERSION     NP_065790.2
DBSOURCE    REFSEQ: accession NM_020739.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Wang,G., Liu,Z., Wang,Q., Liu,B. and Li,J.
  TITLE     Clinical and prognostic significance of CCPG1 in hepatocellular
            carcinoma
  JOURNAL   Gen Physiol Biophys 42 (5), 431-442 (2023)
   PUBMED   37702448
  REMARK    GeneRIF: Clinical and prognostic significance of CCPG1 in
            hepatocellular carcinoma.
REFERENCE   2  (residues 1 to 757)
  AUTHORS   Chino,H., Hatta,T., Natsume,T. and Mizushima,N.
  TITLE     Intrinsically Disordered Protein TEX264 Mediates ER-phagy
  JOURNAL   Mol Cell 74 (5), 909-921 (2019)
   PUBMED   31006538
REFERENCE   3  (residues 1 to 757)
  AUTHORS   Smith,M.D., Harley,M.E., Kemp,A.J., Wills,J., Lee,M., Arends,M.,
            von Kriegsheim,A., Behrends,C. and Wilkinson,S.
  TITLE     CCPG1 Is a Non-canonical Autophagy Cargo Receptor Essential for
            ER-Phagy and Pancreatic ER Proteostasis
  JOURNAL   Dev Cell 44 (2), 217-232 (2018)
   PUBMED   29290589
  REMARK    GeneRIF: identification of cell-cycle progression gene 1 (CCPG1),
            an ER-resident protein, as a non-canonical cargo receptor that
            directly binds to core autophagy proteins via an LIR motif to
            mammalian ATG8 proteins and, independently and via a discrete
            motif, to FIP200.
REFERENCE   4  (residues 1 to 757)
  AUTHORS   Dunlop,E.A., Seifan,S., Claessens,T., Behrends,C., Kamps,M.A.,
            Rozycka,E., Kemp,A.J., Nookala,R.K., Blenis,J., Coull,B.J.,
            Murray,J.T., van Steensel,M.A., Wilkinson,S. and Tee,A.R.
  TITLE     FLCN, a novel autophagy component, interacts with GABARAP and is
            regulated by ULK1 phosphorylation
  JOURNAL   Autophagy 10 (10), 1749-1760 (2014)
   PUBMED   25126726
REFERENCE   5  (residues 1 to 757)
  AUTHORS   Faghihi,M.A., Kocerha,J., Modarresi,F., Engstrom,P.G., Chalk,A.M.,
            Brothers,S.P., Koesema,E., St Laurent,G. and Wahlestedt,C.
  TITLE     RNAi screen indicates widespread biological function for human
            natural antisense transcripts
  JOURNAL   PLoS One 5 (10), e13177 (2010)
   PUBMED   20957177
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 757)
  AUTHORS   Myslinski,E., Gerard,M.A., Krol,A. and Carbon,P.
  TITLE     A genome scale location analysis of human Staf/ZNF143-binding sites
            suggests a widespread role for human Staf/ZNF143 in mammalian
            promoters
  JOURNAL   J Biol Chem 281 (52), 39953-39962 (2006)
   PUBMED   17092945
REFERENCE   7  (residues 1 to 757)
  AUTHORS   Edwards,M.C., Liegeois,N., Horecka,J., DePinho,R.A., Sprague,G.F.
            Jr., Tyers,M. and Elledge,S.J.
  TITLE     Human CPR (cell cycle progression restoration) genes impart a Far-
            phenotype on yeast cells
  JOURNAL   Genetics 147 (3), 1063-1076 (1997)
   PUBMED   9383053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB084778.1, BC039871.1, AC018926.10 and AA740595.1.
            
            On Sep 15, 2005 this sequence version replaced NP_065790.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB033080.2, SRR11853567.10185.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.3"
     Protein         1..757
                     /product="cell cycle progression protein 1 isoform 1"
                     /note="cell cycle progression restoration protein 8"
                     /calculated_mol_wt=87210
     Region          1..308
                     /region_name="Interaction with MCF2L and SRC.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULG6.3)"
     Region          84..>231
                     /region_name="PLN02328"
                     /note="lysine-specific histone demethylase 1 homolog"
                     /db_xref="CDD:215187"
     Region          152..207
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULG6.3)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9ULG6.3)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULG6.3)"
     Region          306..>459
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          458..483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULG6.3)"
     Region          <488..546
                     /region_name="GvpP"
                     /note="Gas vesicle protein YhaH [General function
                     prediction only]; COG4980"
                     /db_xref="CDD:444004"
     CDS             1..757
                     /gene="CCPG1"
                     /gene_synonym="CPR8"
                     /coded_by="NM_020739.5:149..2422"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42039.1"
                     /db_xref="GeneID:9236"
                     /db_xref="HGNC:HGNC:24227"
                     /db_xref="MIM:611326"
ORIGIN      
        1 msenssdsds scgwtvishe gsdiemlnsv tptdscepap ecssleqeel qalqieqges
       61 sqngtvlmee taypaleets stieaeeqki pedsiyigta sddsdivtle ppkleeignq
      121 evviveeaqs sedfnmgsss ssqytfcqpe tvfssqpsdd esssdetsnq pspafrrrra
      181 rkktvsases edrlvaeqet epskelskrq fssglnkcvi lalviaismg fghfygtiqi
      241 qkrqqlvrki hedelndmkd ylsqcqqeqe sfidykslke nlarcwtlte aekmsfetqk
      301 tnlatenqyl rvslekeeka lsslqeelnk lreqiriled kgtstelvke nqklkqhlee
      361 ekqkkhsfls qretllteak mlkrelerer lvttalrgel qqlsgsqlhg ksdspnvyte
      421 kkeiailrer ltelerkltf eqqrsdlwer lyveakdqng kqgtdgkkkg grgshraknk
      481 sketflgsvk etfdamknst kefvrhhkek ikqakeavke nlkkfsdsvk stfrhfkdtt
      541 knifdekgnk rfgatkeaae kprtvfsdyl hpqykapten hhnrgptmqn dgrkekpvhf
      601 kefrkntnsk kcspghdcre nshsfrkacs gvfdcaqqes mslfntvvnp irmdefrqii
      661 qrymlkeldt fchwneldqf inkfflngvf ihdqklftdf vndvkdylrn mkeyevdndg
      721 vfekldeyiy rhffghtfsp pygprsvyik pchyssl
//
LOCUS       NP_001317044             423 aa            linear   PRI 21-NOV-2025
DEFINITION  voltage-dependent L-type calcium channel subunit beta-4 isoform h
            [Homo sapiens].
ACCESSION   NP_001317044 XP_016860370
VERSION     NP_001317044.1
DBSOURCE    REFSEQ: accession NM_001330115.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Westhoff,M. and Dixon,R.E.
  TITLE     Mechanisms and Regulation of Cardiac CaV1.2 Trafficking
  JOURNAL   Int J Mol Sci 22 (11), 5927 (2021)
   PUBMED   34072954
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Coste de Bagneaux,P., von Elsner,L., Bierhals,T., Campiglio,M.,
            Johannsen,J., Obermair,G.J., Hempel,M., Flucher,B.E. and Kutsche,K.
  TITLE     A homozygous missense variant in CACNB4 encoding the auxiliary
            calcium channel beta4 subunit causes a severe neurodevelopmental
            disorder and impairs channel and non-channel functions
  JOURNAL   PLoS Genet 16 (3), e1008625 (2020)
   PUBMED   32176688
  REMARK    GeneRIF: The homozygous CACNB4 p.(Leu126Pro) variant underlies the
            severe neurological phenotype in the two siblings.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Vendel,A.C., Terry,M.D., Striegel,A.R., Iverson,N.M.,
            Leuranguer,V., Rithner,C.D., Lyons,B.A., Pickard,G.E., Tobet,S.A.
            and Horne,W.A.
  TITLE     Alternative splicing of the voltage-gated Ca2+ channel beta4
            subunit creates a uniquely folded N-terminal protein binding domain
            with cell-specific expression in the cerebellar cortex
  JOURNAL   J Neurosci 26 (10), 2635-2644 (2006)
   PUBMED   16525042
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Helton,T.D. and Horne,W.A.
  TITLE     Alternative splicing of the beta 4 subunit has alpha1 subunit
            subtype-specific effects on Ca2+ channel gating
  JOURNAL   J Neurosci 22 (5), 1573-1582 (2002)
   PUBMED   11880487
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Escayg,A., Jones,J.M., Kearney,J.A., Hitchcock,P.F. and
            Meisler,M.H.
  TITLE     Calcium channel beta 4 (CACNB4): human ortholog of the mouse
            epilepsy gene lethargic
  JOURNAL   Genomics 50 (1), 14-22 (1998)
   PUBMED   9628818
REFERENCE   7  (residues 1 to 423)
  AUTHORS   Burgess,D.L., Jones,J.M., Meisler,M.H. and Noebels,J.L.
  TITLE     Mutation of the Ca2+ channel beta subunit gene Cchb4 is associated
            with ataxia and seizures in the lethargic (lh) mouse
  JOURNAL   Cell 88 (3), 385-392 (1997)
   PUBMED   9039265
REFERENCE   8  (residues 1 to 423)
  AUTHORS   Diriong,S., Lory,P., Williams,M.E., Ellis,S.B., Harpold,M.M. and
            Taviaux,S.
  TITLE     Chromosomal localization of the human genes for alpha 1A, alpha 1B,
            and alpha 1E voltage-dependent Ca2+ channel subunits
  JOURNAL   Genomics 30 (3), 605-609 (1995)
   PUBMED   8825650
REFERENCE   9  (residues 1 to 423)
  AUTHORS   Spacey,S.
  TITLE     Episodic Ataxia Type 2 - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301674
REFERENCE   10 (residues 1 to 423)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068547.7 and AC097448.2.
            
            On Aug 17, 2016 this sequence version replaced XP_016860370.1.
            
            Summary: This gene encodes a member of the beta subunit family of
            voltage-dependent calcium channel complex proteins. Calcium
            channels mediate the influx of calcium ions into the cell upon
            membrane polarization and consist of a complex of alpha-1,
            alpha-2/delta, beta, and gamma subunits in a 1:1:1:1 ratio. Various
            versions of each of these subunits exist, either expressed from
            similar genes or the result of alternative splicing. The protein
            encoded by this locus plays an important role in calcium channel
            function by modulating G protein inhibition, increasing peak
            calcium current, controlling the alpha-1 subunit membrane targeting
            and shifting the voltage dependence of activation and inactivation.
            Certain mutations in this gene have been associated with idiopathic
            generalized epilepsy (IGE), juvenile myoclonic epilepsy (JME), and
            episodic ataxia, type 5. [provided by RefSeq, Aug 2016].
            
            Transcript Variant: This variant (8) represents use of an alternate
            promoter compared to variant 2. The encoded isoform (h) has an
            a-type N-terminus.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.267516.1,
                                           SRR1803617.248342.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q23.3"
     Protein         1..423
                     /product="voltage-dependent L-type calcium channel subunit
                     beta-4 isoform h"
                     /note="dihydropyridine-sensitive L-type, calcium channel
                     beta-4 subunit; voltage-dependent L-type calcium channel
                     subunit beta-4; calcium channel voltage-dependent subunit
                     beta 4"
                     /calculated_mol_wt=47101
     Region          16..57
                     /region_name="VGCC_beta4Aa_N"
                     /note="Voltage gated calcium channel subunit beta domain
                     4Aa N terminal; pfam12052"
                     /db_xref="CDD:463445"
     Region          57..124
                     /region_name="SH3_CACNB4"
                     /note="Src Homology 3 domain of Voltage-dependent L-type
                     calcium channel subunit beta4; cd12043"
                     /db_xref="CDD:212976"
     Site            order(67,69,72,83,101..102,118,120..121)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212976"
     Region          <185..301
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..423
                     /gene="CACNB4"
                     /gene_synonym="CAB4; CACNLB4; EA5; EIG9; EJM; EJM4; EJM6"
                     /coded_by="NM_001330115.2:266..1537"
                     /note="isoform h is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS82523.1"
                     /db_xref="GeneID:785"
                     /db_xref="HGNC:HGNC:1404"
                     /db_xref="MIM:601949"
ORIGIN      
        1 mydnlylhgi edseagsads ytsrpsdsdv sleedreair qereqqaaiq lerakskpva
       61 favktnvsyc galdedvpvp staisfdakd flhikekynn dwwigrlvke gceigfipsp
      121 lrleniriqq eqkrgrfhgg kssgnssssl gemvsgtfra tptstdgahs slrcctvnas
      181 ggvsgavter lraevqseie rifelarslq lvvldadtin hpaqliktsl apiivhvkvs
      241 spkvlqrlik srgksqskhl nvqlvaadkl aqcppemfdv ildenqleda cehlgeylea
      301 ywrathttss tpmtpllgrn lgstalspyp taisglqsqr mrhsnhsten spierrslmt
      361 sdenyhnera rksrnrlsss sqhsrdhypl veedypdsyq dtykphrnrg spggyshdsr
      421 hrl
//
LOCUS       NP_001340590             438 aa            linear   PRI 21-NOV-2025
DEFINITION  WD repeat-containing protein 20 isoform 17 [Homo sapiens].
ACCESSION   NP_001340590
VERSION     NP_001340590.1
DBSOURCE    REFSEQ: accession NM_001353661.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Jiang,L., Qi,X., Lai,M., Zhou,J., Yuan,M., You,J., Liu,Q., Pan,J.,
            Zhao,L., Ying,M., Ji,J., Li,K., Zhang,Y., Pan,W., He,Q., Yang,B.
            and Cao,J.
  TITLE     WDR20 prevents hepatocellular carcinoma senescence by orchestrating
            the simultaneous USP12/46-mediated deubiquitination of c-Myc
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2407904121 (2024)
   PUBMED   39432777
  REMARK    GeneRIF: WDR20 prevents hepatocellular carcinoma senescence by
            orchestrating the simultaneous USP12/46-mediated deubiquitination
            of c-Myc.
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Ng,V.H., Spencer,Z., Neitzel,L.R., Nayak,A., Loberg,M.A., Shen,C.,
            Kassel,S.N., Kroh,H.K., An,Z., Anthony,C.C., Bryant,J.M.,
            Lawson,A., Goldsmith,L., Benchabane,H., Hansen,A.G., Li,J.,
            D'Souza,S., Lebensohn,A.M., Rohatgi,R., Weiss,W.A., Weiss,V.L.,
            Williams,C., Hong,C.C., Robbins,D.J., Ahmed,Y. and Lee,E.
  TITLE     The USP46 complex deubiquitylates LRP6 to promote Wnt/beta-catenin
            signaling
  JOURNAL   Nat Commun 14 (1), 6173 (2023)
   PUBMED   37798301
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Olazabal-Herrero,A., Bilbao-Arribas,M., Carlevaris,O., Sendino,M.,
            Varela-Martinez,E., Jugo,B.M., Berra,E. and Rodriguez,J.A.
  TITLE     The dystrophia myotonica WD repeat-containing protein DMWD and
            WDR20 differentially regulate USP12 deubiquitinase
  JOURNAL   FEBS J 288 (20), 5943-5963 (2021)
   PUBMED   33844468
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 438)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 438)
  AUTHORS   Dahlberg,C.L. and Juo,P.
  TITLE     The WD40-repeat proteins WDR-20 and WDR-48 bind and activate the
            deubiquitinating enzyme USP-46 to promote the abundance of the
            glutamate receptor GLR-1 in the ventral nerve cord of
            Caenorhabditis elegans
  JOURNAL   J Biol Chem 289 (6), 3444-3456 (2014)
   PUBMED   24356955
REFERENCE   8  (residues 1 to 438)
  AUTHORS   Kee,Y., Yang,K., Cohn,M.A., Haas,W., Gygi,S.P. and D'Andrea,A.D.
  TITLE     WDR20 regulates activity of the USP12 x UAF1 deubiquitinating
            enzyme complex
  JOURNAL   J Biol Chem 285 (15), 11252-11257 (2010)
   PUBMED   20147737
  REMARK    GeneRIF: WDR20 serves as a stimulatory subunit for preserving and
            regulating the activity of the subset of the UAF1 x USP12 complexes
REFERENCE   9  (residues 1 to 438)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   10 (residues 1 to 438)
  AUTHORS   Smith,T.F.
  TITLE     Diversity of WD-repeat proteins
  JOURNAL   Subcell Biochem 48, 20-30 (2008)
   PUBMED   18925368
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133223.5 and AL359402.3.
            
            Summary: This gene encodes a WD repeat-containing protein that
            functions to preserve and regulate the activity of the USP12-UAF1
            deubiquitinating enzyme complex. Multiple alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Jun 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.161535.1,
                                           SRR1803611.183310.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.31"
     Protein         1..438
                     /product="WD repeat-containing protein 20 isoform 17"
                     /note="WD repeat-containing protein 20"
                     /calculated_mol_wt=48094
     Region          22..87
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <77..183
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          92..128
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          135..168
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..438
                     /gene="WDR20"
                     /gene_synonym="Bun107; DMR"
                     /coded_by="NM_001353661.2:452..1768"
                     /note="isoform 17 is encoded by transcript variant 17"
                     /db_xref="GeneID:91833"
                     /db_xref="HGNC:HGNC:19667"
                     /db_xref="MIM:617741"
ORIGIN      
        1 mrnmtflpsg kdkrlidksr vtcvkwvpgs eslflvahss gnmylynveh tcgttaphyq
       61 llkqgesfav htckskstrn pllkwtvgeg alnefafspd gkflacvsqd gflrvfnfds
      121 velhgtmksy fggllcvcws pdgkyivtgg eddlvtvwsf vdcrviargh ghkswvsvva
      181 fdpyttsvee gdpmefsgsd edfqdllhfg rdranstqsr lskrnstdsr pvsvtyrfgs
      241 vgqdtqlclw dltedilfph qplsrartht nvmnatsppa gsngnsvttp gnsvppplpr
      301 snslphsavs nagskssvmd gaiasgvskf atlslhdrke rhhekdhkrn hsmghissks
      361 sdklnlvtkt ktdpaktlgt plcprmedvp lleplickki aherltvlif ledcivtacq
      421 egfictwgrp gkvvsfnp
//
LOCUS       NP_001306086             121 aa            linear   PRI 21-NOV-2025
DEFINITION  dynein light chain roadblock-type 1 isoform d [Homo sapiens].
ACCESSION   NP_001306086 XP_005260625
VERSION     NP_001306086.1
DBSOURCE    REFSEQ: accession NM_001319157.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Canty,J.T., Tan,R., Kusakci,E., Fernandes,J. and Yildiz,A.
  TITLE     Structure and Mechanics of Dynein Motors
  JOURNAL   Annu Rev Biophys 50, 549-574 (2021)
   PUBMED   33957056
  REMARK    Review article
REFERENCE   4  (residues 1 to 121)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 121)
  AUTHORS   Vuolo,L., Stevenson,N.L., Mukhopadhyay,A.G., Roberts,A.J. and
            Stephens,D.J.
  TITLE     Cytoplasmic dynein-2 at a glance
  JOURNAL   J Cell Sci 133 (6) (2020)
   PUBMED   32229580
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 121)
  AUTHORS   Pfister,K.K., Fisher,E.M., Gibbons,I.R., Hays,T.S., Holzbaur,E.L.,
            McIntosh,J.R., Porter,M.E., Schroer,T.A., Vaughan,K.T.,
            Witman,G.B., King,S.M. and Vallee,R.B.
  TITLE     Cytoplasmic dynein nomenclature
  JOURNAL   J Cell Biol 171 (3), 411-413 (2005)
   PUBMED   16260502
REFERENCE   7  (residues 1 to 121)
  AUTHORS   Tang,Q., Staub,C.M., Gao,G., Jin,Q., Wang,Z., Ding,W.,
            Aurigemma,R.E. and Mulder,K.M.
  TITLE     A novel transforming growth factor-beta receptor-interacting
            protein that is also a light chain of the motor protein dynein
  JOURNAL   Mol Biol Cell 13 (12), 4484-4496 (2002)
   PUBMED   12475967
REFERENCE   8  (residues 1 to 121)
  AUTHORS   Susalka,S.J., Nikulina,K., Salata,M.W., Vaughan,P.S., King,S.M.,
            Vaughan,K.T. and Pfister,K.K.
  TITLE     The roadblock light chain binds a novel region of the cytoplasmic
            Dynein intermediate chain
  JOURNAL   J Biol Chem 277 (36), 32939-32946 (2002)
   PUBMED   12077152
REFERENCE   9  (residues 1 to 121)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Ray,S., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human retina for the NEIBank
            Project: retbindin, an abundant, novel retinal cDNA and alternative
            splicing of other retina-preferred gene transcripts
  JOURNAL   Mol Vis 8, 196-204 (2002)
   PUBMED   12107411
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 121)
  AUTHORS   Jiang,J., Yu,L., Huang,X., Chen,X., Li,D., Zhang,Y., Tang,L. and
            Zhao,S.
  TITLE     Identification of two novel human dynein light chain genes, DNLC2A
            and DNLC2B, and their expression changes in hepatocellular
            carcinoma tissues from 68 Chinese patients
  JOURNAL   Gene 281 (1-2), 103-113 (2001)
   PUBMED   11750132
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109923.29 and AL136173.24.
            
            On Jan 27, 2016 this sequence version replaced XP_005260625.1.
            
            Summary: This gene is a member of the roadblock dynein light chain
            family. The encoded cytoplasmic protein is capable of binding
            intermediate chain proteins, interacts with transforming growth
            factor-beta, and has been implicated in the regulation of actin
            modulating proteins. Upregulation of this gene has been associated
            with hepatocellular carcinomas, suggesting that this gene may be
            involved in tumor progression. Alternative splicing results in
            multiple transcript variants. Pseudogenes of this gene have been
            defined on chromosomes 12 and 18. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (7) lacks an exon and its 3'
            terminal exon extends past a splice site that is used in variant 1.
            This results in a novel 3' coding region and 3' UTR, compared to
            variant 1. The encoded isoform (d) is longer and has a distinct
            C-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK294214.1, DC384128.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..121
                     /product="dynein light chain roadblock-type 1 isoform d"
                     /note="dynein, cytoplasmic, light polypeptide 2A;
                     bithoraxoid-like protein; dynein-associated protein Km23;
                     ROBL/LC7-like 1; roadblock domain-containing protein 1"
                     /calculated_mol_wt=13231
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P62628; propagated from
                     UniProtKB/Swiss-Prot (Q9NP97.3)"
     Region          3..82
                     /region_name="Robl_LC7"
                     /note="Roadblock/LC7 domain; pfam03259"
                     /db_xref="CDD:397386"
     CDS             1..121
                     /gene="DYNLRB1"
                     /gene_synonym="BITH; BLP; DNCL2A; DNLC2A; ROBLD1"
                     /coded_by="NM_001319157.2:38..403"
                     /note="isoform d is encoded by transcript variant 7"
                     /db_xref="GeneID:83658"
                     /db_xref="HGNC:HGNC:15468"
                     /db_xref="MIM:607167"
ORIGIN      
        1 maeveetlkr lqsqkgvqgi ivvntegipi kstmdnpttt qyaslmhsfi lkarstvrdi
       61 dpqndltflr irskkneimv apgkgsstsp crnrphgtfs vahqeswhsg vsrgskqgpr
      121 s
//
LOCUS       NP_001338455             519 aa            linear   PRI 21-NOV-2025
DEFINITION  regulator of G-protein signaling 3 isoform 2 [Homo sapiens].
ACCESSION   NP_001338455 XP_011517199
VERSION     NP_001338455.1
DBSOURCE    REFSEQ: accession NM_001351526.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Kanwal,A., Pardo,J.V. and Naz,S.
  TITLE     RGS3 and IL1RAPL1 missense variants implicate defective
            neurotransmission in early-onset inherited schizophrenias
  JOURNAL   J Psychiatry Neurosci 47 (6), E379-E390 (2022)
   PUBMED   36318984
  REMARK    GeneRIF: RGS3 and IL1RAPL1 missense variants implicate defective
            neurotransmission in early-onset inherited schizophrenias.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Hao,F., Wang,N., Gui,H., Zhang,Y., Wu,Z. and Wang,J.
  TITLE     Pseudogene UBE2MP1 derived transcript enhances in vitro cell
            proliferation and apoptosis resistance of hepatocellular carcinoma
            cells through miR-145-5p/RGS3 axis
  JOURNAL   Aging (Albany NY) 14 (19), 7906-7925 (2022)
   PUBMED   36214767
  REMARK    GeneRIF: Pseudogene UBE2MP1 derived transcript enhances in vitro
            cell proliferation and apoptosis resistance of hepatocellular
            carcinoma cells through miR-145-5p/RGS3 axis.
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Kehrl,J.H., Srikumar,D., Harrison,K., Wilson,G.L. and Shi,C.S.
  TITLE     Additional 5' exons in the RGS3 locus generate multiple mRNA
            transcripts, one of which accounts for the origin of human PDZ-RGS3
  JOURNAL   Genomics 79 (6), 860-868 (2002)
   PUBMED   12036301
REFERENCE   5  (residues 1 to 519)
  AUTHORS   Mittmann,C., Schuler,C., Chung,C.H., Hoppner,G., Nose,M.,
            Kehrl,J.H. and Wieland,T.
  TITLE     Evidence for a short form of RGS3 preferentially expressed in the
            human heart
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 363 (4), 456-463 (2001)
   PUBMED   11330340
REFERENCE   6  (residues 1 to 519)
  AUTHORS   Dulin,N.O., Pratt,P., Tiruppathi,C., Niu,J., Voyno-Yasenetskaya,T.
            and Dunn,M.J.
  TITLE     Regulator of G protein signaling RGS3T is localized to the nucleus
            and induces apoptosis
  JOURNAL   J Biol Chem 275 (28), 21317-21323 (2000)
   PUBMED   10749886
REFERENCE   7  (residues 1 to 519)
  AUTHORS   Dulin,N.O., Sorokin,A., Reed,E., Elliott,S., Kehrl,J.H. and
            Dunn,M.J.
  TITLE     RGS3 inhibits G protein-mediated signaling via translocation to the
            membrane and binding to Galpha11
  JOURNAL   Mol Cell Biol 19 (1), 714-723 (1999)
   PUBMED   9858594
REFERENCE   8  (residues 1 to 519)
  AUTHORS   Chatterjee,T.K., Eapen,A., Kanis,A.B. and Fisher,R.A.
  TITLE     Genomic organization, 5'-flanking region, and chromosomal
            localization of the human RGS3 gene
  JOURNAL   Genomics 45 (2), 429-433 (1997)
   PUBMED   9344672
REFERENCE   9  (residues 1 to 519)
  AUTHORS   Chatterjee,T.K., Eapen,A.K. and Fisher,R.A.
  TITLE     A truncated form of RGS3 negatively regulates G protein-coupled
            receptor stimulation of adenylyl cyclase and phosphoinositide
            phospholipase C
  JOURNAL   J Biol Chem 272 (24), 15481-15487 (1997)
   PUBMED   9182581
REFERENCE   10 (residues 1 to 519)
  AUTHORS   Druey,K.M., Blumer,K.J., Kang,V.H. and Kehrl,J.H.
  TITLE     Inhibition of G-protein-mediated MAP kinase activation by a new
            mammalian gene family
  JOURNAL   Nature 379 (6567), 742-746 (1996)
   PUBMED   8602223
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP257809.1, DA575364.1,
            AL162727.20, AY585192.1, BQ953216.1, BE385269.1 and AF463495.1.
            
            On May 12, 2017 this sequence version replaced XP_011517199.1.
            
            Summary: This gene encodes a member of the regulator of G-protein
            signaling (RGS) family. This protein is a GTPase-activating protein
            that inhibits G-protein-mediated signal transduction. Alternative
            splicing and the use of alternative promoters results in multiple
            transcript variants encoding different isoforms. Long isoforms are
            largely cytosolic and plasma membrane-associated with a function in
            Wnt signaling and in the epithelial mesenchymal transition, while
            shorter N-terminally-truncated isoforms can be nuclear. [provided
            by RefSeq, Jan 2013].
            
            Transcript Variant: This variant (13) lacks several 5' exons but
            includes several alternate exons in the 5' region, and it thus
            differs in the 5' UTR, lacks a large portion of the 5' coding
            region, and uses a downstream in-frame start codon, compared to
            variant 6. The encoded isoform (2) is significantly shorter at the
            N-terminus, compared to isoform 6. Variants 2, 7 and 13 encode the
            same isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3710413.1,
                                           SRR14038196.2548929.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..519
                     /product="regulator of G-protein signaling 3 isoform 2"
                     /note="regulator of G-protein signalling 3"
                     /calculated_mol_wt=56471
     Region          <20..180
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          395..508
                     /region_name="RGS_RGS3"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the RGS3 protein; cd08713"
                     /db_xref="CDD:188668"
     CDS             1..519
                     /gene="RGS3"
                     /gene_synonym="C2PA; RGP3"
                     /coded_by="NM_001351526.2:689..2248"
                     /note="isoform 2 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS6798.1"
                     /db_xref="GeneID:5998"
                     /db_xref="HGNC:HGNC:9999"
                     /db_xref="MIM:602189"
ORIGIN      
        1 mfeteadekr emaleegkgp gaedsppske pspgqelppg qdlppnkdsp sgqepapsqe
       61 plsskdsats egsppgpdap pskdvppcqe pppaqdlspc qdlpagqepl phqdplltkd
      121 lpaiqesptr dlppcqdlpp sqvslpakal tedtmssgdl laatgdppaa prpafvipev
      181 rldstysqka gaeqgcsgde edaeeaeeve egeegeeded edtsddnyge rseakrssmi
      241 etgqgaeggl slrvqnslrr rthsegsllq eprgpcfasd ttlhcsdgeg aastwgmpsp
      301 stlkkelgrn ggsmhhlslf ftghrkmsga dtvgdddeas rkrksknlak dmknklgifr
      361 rrnespgapp agkadkmmks fkptseealk wgeslekllv hkyglavfqa flrtefseen
      421 lefwlacedf kkvksqskma skakkifaey iaiqackevn ldsytrehtk dnlqsvtrgc
      481 fdlaqkrifg lmekdsyprf lrsdlyldli nqkkmsppl
//
LOCUS       NP_001242945             138 aa            linear   PRI 21-NOV-2025
DEFINITION  homologous-pairing protein 2 homolog isoform 4 [Homo sapiens].
ACCESSION   NP_001242945
VERSION     NP_001242945.1
DBSOURCE    REFSEQ: accession NM_001256016.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Mei,L., Huang,L., Huang,Y., Wu,X., He,H., He,X., Su,Z. and Li,P.
  TITLE     Two novel biallelic mutations in PSMC3IP in a patient affected by
            premature ovarian insufficiency
  JOURNAL   Mol Med Rep 25 (2) (2022)
   PUBMED   34878148
  REMARK    GeneRIF: Two novel biallelic mutations in PSMC3IP in a patient
            affected by premature ovarian insufficiency.
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Nathansen,J., Lukiyanchuk,V., Hein,L., Stolte,M.I., Borgmann,K.,
            Lock,S., Kurth,I., Baumann,M., Krause,M., Linge,A. and Dubrovska,A.
  TITLE     Oct4 confers stemness and radioresistance to head and neck squamous
            cell carcinoma by regulating the homologous recombination factors
            PSMC3IP and RAD54L
  JOURNAL   Oncogene 40 (24), 4214-4228 (2021)
   PUBMED   34079088
  REMARK    GeneRIF: Oct4 confers stemness and radioresistance to head and neck
            squamous cell carcinoma by regulating the homologous recombination
            factors PSMC3IP and RAD54L.
REFERENCE   5  (residues 1 to 138)
  AUTHORS   Zangen,D., Kaufman,Y., Zeligson,S., Perlberg,S., Fridman,H.,
            Kanaan,M., Abdulhadi-Atwan,M., Abu Libdeh,A., Gussow,A.,
            Kisslov,I., Carmel,L., Renbaum,P. and Levy-Lahad,E.
  TITLE     XX ovarian dysgenesis is caused by a PSMC3IP/HOP2 mutation that
            abolishes coactivation of estrogen-driven transcription
  JOURNAL   Am J Hum Genet 89 (4), 572-579 (2011)
   PUBMED   21963259
  REMARK    GeneRIF: a PSMC3IP/HOP2 mutation may cause XX ovarian dysgenesis
            through abolishing coactivation of estrogen-driven transcription
REFERENCE   6  (residues 1 to 138)
  AUTHORS   Enomoto,R., Kinebuchi,T., Sato,M., Yagi,H., Kurumizaka,H. and
            Yokoyama,S.
  TITLE     Stimulation of DNA strand exchange by the human TBPIP/Hop2-Mnd1
            complex
  JOURNAL   J Biol Chem 281 (9), 5575-5581 (2006)
   PUBMED   16407260
  REMARK    GeneRIF: Data suggest that the human TBPIP/Hop2-Mnd1 complex may
            ensure proper pairing between homologous chromosomes through its
            stimulation of strand exchange during meiosis.
REFERENCE   7  (residues 1 to 138)
  AUTHORS   Ko,L., Cardona,G.R., Henrion-Caude,A. and Chin,W.W.
  TITLE     Identification and characterization of a tissue-specific
            coactivator, GT198, that interacts with the DNA-binding domains of
            nuclear receptors
  JOURNAL   Mol Cell Biol 22 (1), 357-369 (2002)
   PUBMED   11739747
  REMARK    GeneRIF: Identification of GT198 (TBPIP/Hop2) as a nuclear receptor
            coactivator. GT198 is phosphorylation regulated. GT198 interacts
            with nuclear receptors.
REFERENCE   8  (residues 1 to 138)
  AUTHORS   Ijichi,H., Tanaka,T., Nakamura,T., Yagi,H., Hakuba,A. and Sato,M.
  TITLE     Molecular cloning and characterization of a human homologue of
            TBPIP, a BRCA1 locus-related gene
  JOURNAL   Gene 248 (1-2), 99-107 (2000)
   PUBMED   10806355
REFERENCE   9  (residues 1 to 138)
  AUTHORS   Tanaka,T., Nakamura,T., Takagi,H. and Sato,M.
  TITLE     Molecular cloning and characterization of a novel TBP-1 interacting
            protein (TBPIP):enhancement of TBP-1 action on Tat by TBPIP
  JOURNAL   Biochem Biophys Res Commun 239 (1), 176-181 (1997)
   PUBMED   9345291
REFERENCE   10 (residues 1 to 138)
  AUTHORS   Rommens,J.M., Durocher,F., McArthur,J., Tonin,P., LeBlanc,J.F.,
            Allen,T., Samson,C., Ferri,L., Narod,S., Morgan,K. et al.
  TITLE     Generation of a transcription map at the HSD17B locus centromeric
            to BRCA1 at 17q21
  JOURNAL   Genomics 28 (3), 530-542 (1995)
   PUBMED   7490091
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC067852.23.
            
            Summary: This gene encodes a protein that functions in meiotic
            recombination. It is a subunit of the PSMC3IP/MND1 complex, which
            interacts with PSMC3/TBP1 to stimulate DMC1- and RAD51-mediated
            strand exchange during meiosis. The protein encoded by this gene
            can also co-activate ligand-driven transcription mediated by
            estrogen, androgen, glucocorticoid, progesterone, and thyroid
            nuclear receptors. Mutations in this gene cause XX female gonadal
            dysgenesis. Alternative splicing of this gene results in multiple
            transcript variants. [provided by RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI115923.1, SRR12921934.1448047.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2151119,
                                           SAMEA2161674 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..138
                     /product="homologous-pairing protein 2 homolog isoform 4"
                     /note="homologous-pairing protein 2 homolog;
                     DBD-interacting; nuclear receptor coactivator GT198;
                     TBP-1-interacting protein; tat-binding protein
                     1-interacting protein; proteasome 26S ATPase subunit
                     3-interacting protein"
                     /calculated_mol_wt=15932
     Region          <5..>129
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          75..131
                     /region_name="LZ3wCH"
                     /note="Leucine zipper with capping helix domain;
                     pfam18517"
                     /db_xref="CDD:465789"
     CDS             1..138
                     /gene="PSMC3IP"
                     /gene_synonym="GT198; HOP2; HUMGT198A; ODG3; TBPIP"
                     /coded_by="NM_001256016.2:300..716"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:29893"
                     /db_xref="HGNC:HGNC:17928"
                     /db_xref="MIM:608665"
ORIGIN      
        1 mvsdadlqvl dgkivaltak vqslqqscry meaelkelss alttpemqke iqelkkecag
       61 yrerlknika atnhvtpeek eqvyrerqky ckewrkrkrm atelsdaile gypkskkqff
      121 eevgietded ynvtlpdp
//
LOCUS       NP_001371276             424 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial ribosome-associated GTPase 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001371276
VERSION     NP_001371276.1
DBSOURCE    REFSEQ: accession NM_001384347.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Nguyen,T.G., Ritter,C. and Kummer,E.
  TITLE     Structural insights into the role of GTPBP10 in the RNA maturation
            of the mitoribosome
  JOURNAL   Nat Commun 14 (1), 7991 (2023)
   PUBMED   38042949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Hillen,H.S., Lavdovskaia,E., Nadler,F., Hanitsch,E., Linden,A.,
            Bohnsack,K.E., Urlaub,H. and Richter-Dennerlein,R.
  TITLE     Structural basis of GTPase-mediated mitochondrial ribosome
            biogenesis and recycling
  JOURNAL   Nat Commun 12 (1), 3672 (2021)
   PUBMED   34135319
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Cipullo,M., Gese,G.V., Khawaja,A., Hallberg,B.M. and Rorbach,J.
  TITLE     Structural basis for late maturation steps of the human
            mitoribosomal large subunit
  JOURNAL   Nat Commun 12 (1), 3673 (2021)
   PUBMED   34135318
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Cipullo,M., Pearce,S.F., Lopez Sanchez,I.G., Gopalakrishna,S.,
            Kruger,A., Schober,F., Busch,J.D., Li,X., Wredenberg,A.,
            Atanassov,I. and Rorbach,J.
  TITLE     Human GTPBP5 is involved in the late stage of mitoribosome large
            subunit assembly
  JOURNAL   Nucleic Acids Res 49 (1), 354-370 (2021)
   PUBMED   33283228
  REMARK    GeneRIF: Human GTPBP5 is involved in the late stage of mitoribosome
            large subunit assembly.
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Solomon,B.D., Pineda-Alvarez,D.E., Hadley,D.W., Keaton,A.A.,
            Agochukwu,N.B., Raam,M.S., Carlson-Donohoe,H.E., Kamat,A. and
            Chandrasekharappa,S.C.
  TITLE     De novo deletion of chromosome 20q13.33 in a patient with
            tracheo-esophageal fistula, cardiac defects and genitourinary
            anomalies implicates GTPBP5 as a candidate gene
  JOURNAL   Birth Defects Res A Clin Mol Teratol 91 (9), 862-865 (2011)
   PUBMED   21608104
  REMARK    GeneRIF: GTPBP5 bears further study as a cause of TEF/EA
            accompanied by other malformations.
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 424)
  AUTHORS   Hirano,Y., Ohniwa,R.L., Wada,C., Yoshimura,S.H. and Takeyasu,K.
  TITLE     Human small G proteins, ObgH1, and ObgH2, participate in the
            maintenance of mitochondria and nucleolar architectures
  JOURNAL   Genes Cells 11 (11), 1295-1304 (2006)
   PUBMED   17054726
  REMARK    GeneRIF: Knock-down of ObgH1 by RNAi induced mitochondria
            elongation, whereas knock-down of ObgH2 resulted in the
            disorganization of the nucleolar architecture.
REFERENCE   9  (residues 1 to 424)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL078633.32.
            
            Summary: Small G proteins, such as GTPBP5, act as molecular
            switches that play crucial roles in the regulation of fundamental
            cellular processes such as protein synthesis, nuclear transport,
            membrane trafficking, and signal transduction (Hirano et al., 2006
            [PubMed 17054726]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2154361,
                              SAMEA2155590 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..424
                     /product="mitochondrial ribosome-associated GTPase 2
                     isoform 1"
                     /note="protein obg homolog 1; GTP binding protein 5
                     (putative); GTP-binding protein 5"
                     /calculated_mol_wt=46038
     Region          90..403
                     /region_name="Obg_CgtA"
                     /note="Obg family GTPase CgtA; TIGR02729"
                     /db_xref="CDD:274271"
     CDS             1..424
                     /gene="MTG2"
                     /gene_synonym="dJ1005F21.2; GTPBP5; ObgH1"
                     /coded_by="NM_001384347.1:36..1310"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:26164"
                     /db_xref="HGNC:HGNC:16239"
                     /db_xref="MIM:610919"
ORIGIN      
        1 maparcfsar lrtvfqgvgh walstwaglk psrllpqras prllsvgrad lakhqelpgk
       61 kllsekklvr lleleqlacl llrrhrkryf vdyrrvlvcg gnggagascf hseprkefgg
      121 pdggdggngg hvilrvdqqv kslssvlsry qgfsgedggs kncfgrsgav lyirvpvgtl
      181 vkeggrvvad lscvgdeyia alggaggkgn rfflannnra pvtctpgqpg qqrvlhlelk
      241 tvahagmvgf pnagkssllr aisnarpava sypfttlkph vgivhyeghl qiavadipgi
      301 irgahqnrgl gsaflrhier crfllfvvdl sqpepwtqvd dlkyelemye kglsarphai
      361 vankidlpea qanlsqlrdh lgqevivlsa ltgenleqll lhlkvlyday aeaelgqgrq
      421 plrw
//
LOCUS       NP_001341222             497 aa            linear   PRI 21-NOV-2025
DEFINITION  GTPase-activating protein and VPS9 domain-containing protein 1
            isoform 7 [Homo sapiens].
ACCESSION   NP_001341222
VERSION     NP_001341222.1
DBSOURCE    REFSEQ: accession NM_001354293.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Khademi,B., Khorrami,M., Ayromlou,H., Rikhtegar,R., Moghadam,E.A.,
            Tahmasebivand,M., Mousavi,S.R., Kheirollahi,M., Fakhr,F.,
            Alizadeh-Ghodsi,M. and Emamalizadeh,B.
  TITLE     An interdependence between GAPVD1 gene polymorphism, expression
            level and response to interferon beta in patients with multiple
            sclerosis
  JOURNAL   J Neuroimmunol 353, 577507 (2021)
   PUBMED   33548618
  REMARK    GeneRIF: An interdependence between GAPVD1 gene polymorphism,
            expression level and response to interferon beta in patients with
            multiple sclerosis.
REFERENCE   5  (residues 1 to 497)
  AUTHORS   Ibrahim,H., Reus,P., Mundorf,A.K., Grothoff,A.L., Rudenko,V.,
            Buschhaus,C., Stefanski,A., Berleth,N., Stork,B., Stuhler,K.,
            Kalfalah,F. and Reinke,H.
  TITLE     Phosphorylation of GAPVD1 Is Regulated by the PER Complex and
            Linked to GAPVD1 Degradation
  JOURNAL   Int J Mol Sci 22 (7), 3787 (2021)
   PUBMED   33917494
  REMARK    GeneRIF: Phosphorylation of GAPVD1 Is Regulated by the PER Complex
            and Linked to GAPVD1 Degradation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 497)
  AUTHORS   Kim,H., Oh,H., Oh,Y.S., Bae,J., Hong,N.H., Park,S.J., Ahn,S.,
            Lee,M., Rhee,S., Lee,S.H., Jun,Y., Kim,S.H., Huh,Y.H. and Song,W.K.
  TITLE     SPIN90, an adaptor protein, alters the proximity between Rab5 and
            Gapex5 and facilitates Rab5 activation during EGF endocytosis
  JOURNAL   Exp Mol Med 51 (7), 1-14 (2019)
   PUBMED   31358736
  REMARK    GeneRIF: The findings suggest that SPIN90, as an adaptor protein,
            simultaneously binds inactive Rab5 and Gapex5, thereby altering
            their spatial proximity and facilitating Rab5 activation.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 497)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 497)
  AUTHORS   Su,X., Kong,C. and Stahl,P.D.
  TITLE     GAPex-5 mediates ubiquitination, trafficking, and degradation of
            epidermal growth factor receptor
  JOURNAL   J Biol Chem 282 (29), 21278-21284 (2007)
   PUBMED   17545148
  REMARK    GeneRIF: EGF-stimulated receptor ubiquitination and trafficking are
            mediated via GAPex-5: GAPex-5-mediated EGFR ubiquitination is
            independent of Rab5 activation
REFERENCE   9  (residues 1 to 497)
  AUTHORS   Hunker,C.M., Galvis,A., Kruk,I., Giambini,H., Veisaga,M.L. and
            Barbieri,M.A.
  TITLE     Rab5-activating protein 6, a novel endosomal protein with a role in
            endocytosis
  JOURNAL   Biochem Biophys Res Commun 340 (3), 967-975 (2006)
   PUBMED   16410077
REFERENCE   10 (residues 1 to 497)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL354710.17, BC110990.1 and AA683411.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110990.1, SRR14038191.1913708.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..497
                     /product="GTPase-activating protein and VPS9
                     domain-containing protein 1 isoform 7"
                     /note="GTPase-activating protein and VPS9
                     domain-containing protein 1; Rab5-activating protein 6;
                     Rab5 exchange factor"
                     /calculated_mol_wt=56331
     Region          84..449
                     /region_name="RasGAP_RAP6"
                     /note="Ras-GTPase Activating Domain of Rab5-activating
                     protein 6; cd05129"
                     /db_xref="CDD:213331"
     Site            order(129,168,170,172..173,179,182,186,304,312..313,
                     316..317,320,342,345..346,349,353,355,359..360)
                     /site_type="other"
                     /note="putative Rab5 interface [polypeptide binding]"
                     /db_xref="CDD:213331"
     CDS             1..497
                     /gene="GAPVD1"
                     /gene_synonym="GAPex-5; GAPEX5; RAP6"
                     /coded_by="NM_001354293.2:333..1826"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS87689.1"
                     /db_xref="GeneID:26130"
                     /db_xref="HGNC:HGNC:23375"
                     /db_xref="MIM:611714"
ORIGIN      
        1 mvkldihtla hhlkqerlyv nsekqliqrl nadvlktaek lyrtawiakq qrinldrlii
       61 tsaeaspaec cqhakiledt qfvdgykqlg fqetaygefl srlrenprli asslvagekl
      121 nqentqsviy tvftslygnc imqedesyll qvlryliefe lkesdnprrl lrrgtcafsi
      181 lfklfseglf saklfltatl hepimqllve dedhletdpn klierfspsq qeklfgekgs
      241 drfrqkvqem vesneaklva lvnkfigylk qntycfphsl rwivsqmykt lscvdrlevg
      301 evramctdll lacficpavv npeqygiisd apinevarfn lmqvgrllqq lamtgseegd
      361 prtksslgkf dkscvaafld vviggravet pplssvnlle glsrtvvyit ysqlitlvnf
      421 mksvmsgdql redrmaldnl lanlppakpg kssslemtpy ntpqlspatt pankknrlpi
      481 gkenfsywsf llnlifh
//
LOCUS       NP_060682                570 aa            linear   PRI 21-NOV-2025
DEFINITION  protein enabled homolog isoform b [Homo sapiens].
ACCESSION   NP_060682 NP_660283 XP_351324
VERSION     NP_060682.2
DBSOURCE    REFSEQ: accession NM_018212.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Yin,X., Wang,J., Shen,Z., Jia,Q., Bian,Y., Yang,Z., Liu,Y., Li,Y.
            and Zhang,H.
  TITLE     ENAH transcriptionally activated by YY1 promotes growth and
            invasion of laryngocarcinoma cells through PI3K/AKT signaling
  JOURNAL   Eur J Pharmacol 983, 176991 (2024)
   PUBMED   39265883
  REMARK    GeneRIF: ENAH transcriptionally activated by YY1 promotes growth
            and invasion of laryngocarcinoma cells through PI3K/AKT signaling.
REFERENCE   3  (residues 1 to 570)
  AUTHORS   Cui,H., Liang,X., Zhu,Y., Elayah,S.A., Qi,H., Xie,L., Guo,Z.,
            Siya,F., Ming,Y., Yuxin,G., Tu,J. and Na,S.
  TITLE     Mena as a key enhancer factor of EMT to promote metastasis of human
            tongue squamous cell carcinoma
  JOURNAL   Oral Dis 30 (4), 2084-2096 (2024)
   PUBMED   37203597
  REMARK    GeneRIF: Mena as a key enhancer factor of EMT to promote metastasis
            of human tongue squamous cell carcinoma.
REFERENCE   4  (residues 1 to 570)
  AUTHORS   He,L., She,C., Jiang,S., Qi,Z., Deng,Z., Ji,L., Cui,Y. and Wu,J.
  TITLE     Mammalian enabled protein enhances tamoxifen sensitivity of the
            hormone receptor-positive breast cancer patients by suppressing the
            AKT signaling pathway
  JOURNAL   Biol Direct 19 (1), 21 (2024)
   PUBMED   38459605
  REMARK    GeneRIF: Mammalian enabled protein enhances tamoxifen sensitivity
            of the hormone receptor-positive breast cancer patients by
            suppressing the AKT signaling pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 570)
  AUTHORS   Liu,R., Miao,K., Gao,L. and He,L.
  TITLE     TRIM67 interacts with ENAH to regulate the apoptosis and autophagy
            of lung cancer cells
  JOURNAL   Gen Physiol Biophys 43 (2), 163-173 (2024)
   PUBMED   38477606
  REMARK    GeneRIF: TRIM67 interacts with ENAH to regulate the apoptosis and
            autophagy of lung cancer cells.
REFERENCE   6  (residues 1 to 570)
  AUTHORS   Urbanelli,L., Massini,C., Emiliani,C., Orlacchio,A., Bernardi,G.
            and Orlacchio,A.
  TITLE     Characterization of human Enah gene
  JOURNAL   Biochim Biophys Acta 1759 (1-2), 99-107 (2006)
   PUBMED   16494957
REFERENCE   7  (residues 1 to 570)
  AUTHORS   Mammoto,A., Sasaki,T., Asakura,T., Hotta,I., Imamura,H.,
            Takahashi,K., Matsuura,Y., Shirao,T. and Takai,Y.
  TITLE     Interactions of drebrin and gephyrin with profilin
  JOURNAL   Biochem Biophys Res Commun 243 (1), 86-89 (1998)
   PUBMED   9473484
REFERENCE   8  (residues 1 to 570)
  AUTHORS   Ermekova,K.S., Zambrano,N., Linn,H., Minopoli,G., Gertler,F.,
            Russo,T. and Sudol,M.
  TITLE     The WW domain of neural protein FE65 interacts with proline-rich
            motifs in Mena, the mammalian homolog of Drosophila enabled
  JOURNAL   J Biol Chem 272 (52), 32869-32877 (1997)
   PUBMED   9407065
REFERENCE   9  (residues 1 to 570)
  AUTHORS   Niebuhr,K., Ebel,F., Frank,R., Reinhard,M., Domann,E., Carl,U.D.,
            Walter,U., Gertler,F.B., Wehland,J. and Chakraborty,T.
  TITLE     A novel proline-rich motif present in ActA of Listeria
            monocytogenes and cytoskeletal proteins is the ligand for the EVH1
            domain, a protein module present in the Ena/VASP family
  JOURNAL   EMBO J 16 (17), 5433-5444 (1997)
   PUBMED   9312002
REFERENCE   10 (residues 1 to 570)
  AUTHORS   Sazuka,T., Tomooka,Y., Kathju,S., Ikawa,Y., Noda,M. and Kumar,S.
  TITLE     Identification of a developmentally regulated gene in the mouse
            central nervous system which encodes a novel proline rich protein
  JOURNAL   Biochim Biophys Acta 1132 (3), 240-248 (1992)
   PUBMED   1420303
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB961874.1, AY345143.1,
            AK096246.1, AC092811.2 and BU675547.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Jan 1, 2004 this sequence version replaced
            XP_351324.1, NP_060682.1.
            
            Summary: This gene encodes a member of the enabled/
            vasodilator-stimulated phosphoprotein. Members of this gene family
            are involved in actin-based motility. This protein is involved in
            regulating the assembly of actin filaments and modulates cell
            adhesion and motility. Alternate splice variants of this gene have
            been correlated with tumor invasiveness in certain tissues and
            these variants may serve as prognostic markers. A pseudogene of
            this gene is found on chromosome 3. [provided by RefSeq, Sep 2016].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (b) has the same
            N- and C-termini but is shorter compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1944490.1, AY345143.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366843.7/ ENSP00000355808.2
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.12"
     Protein         1..570
                     /product="protein enabled homolog isoform b"
                     /note="protein enabled homolog; Mena delta 11a"
                     /calculated_mol_wt=63794
     Region          5..112
                     /region_name="EVH1_Ena_VASP-like"
                     /note="Enabled/VASP family EVH1 domain; cd01207"
                     /db_xref="CDD:269918"
     Site            order(16,23,69,71,77,79,81)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269918"
     Region          385..411
                     /region_name="WH2_hVASP-like"
                     /note="Wiskott-Aldrich syndrome protein (WASP)-homology
                     domain 2 (WH2) of human Vasodilator-stimulated
                     phosphoprotein and related proteins; cd22185"
                     /db_xref="CDD:409225"
     Site            order(392..393,395..396,399,401..405)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409225"
     Region          401..404
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409225"
     Region          532..566
                     /region_name="VASP_tetra"
                     /note="VASP tetramerization domain; pfam08776"
                     /db_xref="CDD:462599"
     CDS             1..570
                     /gene="ENAH"
                     /gene_synonym="ENA; MENA; NDPP1"
                     /coded_by="NM_018212.6:434..2146"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS31040.1"
                     /db_xref="GeneID:55740"
                     /db_xref="HGNC:HGNC:18271"
                     /db_xref="MIM:609061"
ORIGIN      
        1 mseqsicqar aavmvyddan kkwvpaggst gfsrvhiyhh tgnntfrvvg rkiqdhqvvi
       61 ncaipkglky nqatqtfhqw rdarqvygln fgskedanvf asammhalev lnsqetgptl
      121 prqnsqlpaq vqngpsqeel eiqrrqlqeq qrqkelerer lerermerer lererlerer
      181 lererleqeq lererqerer qerlerqerl erqerlerqe rldrerqerq ererlerler
      241 erqererqeq lereqlewer errissaaap asvetplnsv lgdssasepg lqaasqpaet
      301 psqqgivlgp lapppppplp pgpaqasval ppppgppppp plpstgpppp ppppplpnqv
      361 ppppppppap plpasgffla smsednrplt glaaaiagak lrkvsrmedt sfpsggnaig
      421 vnsassktdt grgngplplg gsglmeemsa llarrrriae kgstieteqk edkgedsepv
      481 tskasststp eptrkpwert ntmngskspv isrpkstpls qpsangvqte gldydrlkqd
      541 ildemrkelt klkeelidai rqelsksnta
//
LOCUS       NP_001357903             595 aa            linear   PRI 21-NOV-2025
DEFINITION  la-related protein 7 isoform 3 [Homo sapiens].
ACCESSION   NP_001357903 XP_024309848
VERSION     NP_001357903.1
DBSOURCE    REFSEQ: accession NM_001370974.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 595)
  AUTHORS   Kao,T.L., Huang,Y.C., Chen,Y.H., Baumann,P. and Tseng,C.K.
  TITLE     LARP3, LARP7, and MePCE are involved in the early stage of human
            telomerase RNA biogenesis
  JOURNAL   Nat Commun 15 (1), 5955 (2024)
   PUBMED   39009594
  REMARK    GeneRIF: LARP3, LARP7, and MePCE are involved in the early stage of
            human telomerase RNA biogenesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 595)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 595)
  AUTHORS   Yan,P., Li,Z., Xiong,J., Geng,Z., Wei,W., Zhang,Y., Wu,G.,
            Zhuang,T., Tian,X., Liu,Z., Liu,J., Sun,K., Chen,F., Zhang,Y.,
            Zeng,C., Huang,Y. and Zhang,B.
  TITLE     LARP7 ameliorates cellular senescence and aging by allosterically
            enhancing SIRT1 deacetylase activity
  JOURNAL   Cell Rep 37 (8), 110038 (2021)
   PUBMED   34818543
  REMARK    GeneRIF: LARP7 ameliorates cellular senescence and aging by
            allosterically enhancing SIRT1 deacetylase activity.
REFERENCE   6  (residues 1 to 595)
  AUTHORS   Xue,Y., Yang,Z., Chen,R. and Zhou,Q.
  TITLE     A capping-independent function of MePCE in stabilizing 7SK snRNA
            and facilitating the assembly of 7SK snRNP
  JOURNAL   Nucleic Acids Res 38 (2), 360-369 (2010)
   PUBMED   19906723
REFERENCE   7  (residues 1 to 595)
  AUTHORS   Markert,A., Grimm,M., Martinez,J., Wiesner,J., Meyerhans,A.,
            Meyuhas,O., Sickmann,A. and Fischer,U.
  TITLE     The La-related protein LARP7 is a component of the 7SK
            ribonucleoprotein and affects transcription of cellular and viral
            polymerase II genes
  JOURNAL   EMBO Rep 9 (6), 569-575 (2008)
   PUBMED   18483487
  REMARK    GeneRIF: Results suggest that LARP7 is a negative transcriptional
            regulator of polymerase II genes, acting by means of the 7SK RNP
            system.
REFERENCE   8  (residues 1 to 595)
  AUTHORS   Krueger,B.J., Jeronimo,C., Roy,B.B., Bouchard,A., Barrandon,C.,
            Byers,S.A., Searcey,C.E., Cooper,J.J., Bensaude,O., Cohen,E.A.,
            Coulombe,B. and Price,D.H.
  TITLE     LARP7 is a stable component of the 7SK snRNP while P-TEFb, HEXIM1
            and hnRNP A1 are reversibly associated
  JOURNAL   Nucleic Acids Res 36 (7), 2219-2229 (2008)
   PUBMED   18281698
  REMARK    GeneRIF: Results indicate LARP7 is a 7SK-binding protein.
REFERENCE   9  (residues 1 to 595)
  AUTHORS   He,N., Jahchan,N.S., Hong,E., Li,Q., Bayfield,M.A., Maraia,R.J.,
            Luo,K. and Zhou,Q.
  TITLE     A La-related protein modulates 7SK snRNP integrity to suppress
            P-TEFb-dependent transcriptional elongation and tumorigenesis
  JOURNAL   Mol Cell 29 (5), 588-599 (2008)
   PUBMED   18249148
  REMARK    GeneRIF: Results identify PIP7S as a La-related protein stably
            associated with and required for 7SK snRNP integrity.
REFERENCE   10 (residues 1 to 595)
  AUTHORS   Biewenga,P., Buist,M.R., Moerland,P.D., Ver Loren van Themaat,E.,
            van Kampen,A.H., ten Kate,F.J. and Baas,F.
  TITLE     Gene expression in early stage cervical cancer
  JOURNAL   Gynecol Oncol 108 (3), 520-526 (2008)
   PUBMED   18191186
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106864.5.
            
            On Jun 19, 2019 this sequence version replaced XP_024309848.1.
            
            Summary: This gene encodes a protein which is found in the 7SK
            snRNP (small nuclear ribonucleoprotein). This snRNP complex
            inhibits a cyclin-dependent kinase, positive transcription
            elongation factor b, which is required for paused RNA polymerase II
            at a promoter to begin transcription elongation. A pseudogene of
            this gene is located on chromosome 3. Alternative splicing results
            in multiple transcript variants. [provided by RefSeq, May 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3744169.1,
                                           SRR14038192.1604929.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..595
                     /product="la-related protein 7 isoform 3"
                     /note="P-TEFb-interaction protein for 7SK stability;
                     La-related protein 7; La ribonucleoprotein domain family
                     member 7"
                     /calculated_mol_wt=68265
     Region          30..111
                     /region_name="LARP_7"
                     /note="La RNA-binding domain of La-related protein 7;
                     cd08032"
                     /db_xref="CDD:153401"
     Site            order(41,44..45,50,53..54,56,77..79)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153401"
     Region          126..205
                     /region_name="RRM1_LARP7"
                     /note="RNA recognition motif 1 (RRM1) found in La-related
                     protein 7 (LARP7) and similar proteins; cd12290"
                     /db_xref="CDD:409732"
     Region          467..548
                     /region_name="RRM2_LARP7"
                     /note="RNA recognition motif 2 in La-related protein 7
                     (LARP7) and similar proteins; cd12542"
                     /db_xref="CDD:409958"
     CDS             1..595
                     /gene="LARP7"
                     /gene_synonym="ALAZS; HDCMA18P; hLARP7; PIP7S"
                     /coded_by="NM_001370974.1:100..1887"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS93568.1"
                     /db_xref="GeneID:51574"
                     /db_xref="HGNC:HGNC:24912"
                     /db_xref="MIM:612026"
ORIGIN      
        1 metesgnqek vmeeestekk kevekkkrsr vkqvladiak qvdfwfgdan lhkdrflreq
       61 ieksrdgyvd isllvsfnkm kklttdgkli aralrssavv eldlegtrir rkkplgerpk
      121 dedertvyve llpknvnhsw iervfgkcgn vvyisiphyk stgdpkgfaf vefetkeqaa
      181 kaieflnnpp eeaprkpgif pktvknkpip alrvveekkk kkkkkgrmkk edniqakeen
      241 mdtsntsisk mkrsrptseg sdiestepqk qcskkkkkrd rveasslpev rtgkrkrsss
      301 edaeslaprs kvkkiiqkdi ikeaseaske nrapclngel fylfqdieis teeekdtgdl
      361 kdssllktkr khkkkhkerh kmgeeviplr vlsksewmdl kkeylalqka smaslkktis
      421 qiksesemet dsgvpqntgm knektanree crtqekvnat gpqfvsgviv kiisteplpg
      481 rkqvrdtlaa isevlyvdll egdtecharf ktpedaqavi nayteinkkh cwkleilsgd
      541 heqrywqkil vdrqaklnqp rekkrgtekl itkaekirla ktqqaskhir fseyd
//
LOCUS       NP_001185845             980 aa            linear   PRI 21-NOV-2025
DEFINITION  liprin-beta-1 isoform 4 [Homo sapiens].
ACCESSION   NP_001185845 XP_005253574
VERSION     NP_001185845.2
DBSOURCE    REFSEQ: accession NM_001198916.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Waqas,A., Liaqat,R., Shaheen,S., Khan,A.Z., Mujahid, Habib,A.H.,
            Binothman,N., Aljadani,M., Zehri,Z., Shaheen,S., Alkathiri,A.,
            Naz,R., Umair,M. and Abbas,S.
  TITLE     A novel homozygous truncating variant in PPFIBP1 further delineates
            PPFIBP1-associated neurodevelopmental disorder
  JOURNAL   Int J Dev Neurosci 83 (2), 191-200 (2023)
   PUBMED   36527195
  REMARK    GeneRIF: A novel homozygous truncating variant in PPFIBP1 further
            delineates PPFIBP1-associated neurodevelopmental disorder.
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 980)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   5  (residues 1 to 980)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 980)
  AUTHORS   Benzinger,A., Muster,N., Koch,H.B., Yates,J.R. 3rd and Hermeking,H.
  TITLE     Targeted proteomic analysis of 14-3-3 sigma, a p53 effector
            commonly silenced in cancer
  JOURNAL   Mol Cell Proteomics 4 (6), 785-795 (2005)
   PUBMED   15778465
REFERENCE   7  (residues 1 to 980)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   8  (residues 1 to 980)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   9  (residues 1 to 980)
  AUTHORS   Kriajevska,M., Fischer-Larsen,M., Moertz,E., Vorm,O.,
            Tulchinsky,E., Grigorian,M., Ambartsumian,N. and Lukanidin,E.
  TITLE     Liprin beta 1, a member of the family of LAR transmembrane tyrosine
            phosphatase-interacting proteins, is a new target for the
            metastasis-associated protein S100A4 (Mts1)
  JOURNAL   J Biol Chem 277 (7), 5229-5235 (2002)
   PUBMED   11836260
  REMARK    GeneRIF: new molecular target of the S100A4 protein, liprin beta1
REFERENCE   10 (residues 1 to 980)
  AUTHORS   Serra-Pages,C., Medley,Q.G., Tang,M., Hart,A. and Streuli,M.
  TITLE     Liprins, a family of LAR transmembrane protein-tyrosine
            phosphatase-interacting proteins
  JOURNAL   J Biol Chem 273 (25), 15611-15620 (1998)
   PUBMED   9624153
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068794.25, AC087257.13 and
            AC009509.7.
            
            On Jun 1, 2019 this sequence version replaced NP_001185845.1.
            
            Summary: The protein encoded by this gene is a member of the LAR
            protein-tyrosine phosphatase-interacting protein (liprin) family.
            Liprins interact with members of LAR family of transmembrane
            protein tyrosine phosphatases, which are known to be important for
            axon guidance and mammary gland development. It has been proposed
            that liprins are multivalent proteins that form complex structures
            and act as scaffolds for the recruitment and anchoring of LAR
            family of tyrosine phosphatases. This protein was found to interact
            with S100A4, a calcium-binding protein related to tumor
            invasiveness and metastasis. In vitro experiment demonstrated that
            the interaction inhibited the phosphorylation of this protein by
            protein kinase C and protein kinase CK2. Alternatively spliced
            transcript variants encoding distinct isoforms have been reported.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon compared to variant 2. The resulting isoform (4) has the same
            N- and C-termini but is shorter compared to isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.5144.1,
                                           SRR1660805.246296.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p11.23-p11.22"
     Protein         1..980
                     /product="liprin-beta-1 isoform 4"
                     /note="liprin related protein; liprin-beta-1;
                     liprin-beta1; PPFIA binding protein 1; protein-tyrosine
                     phosphatase receptor-type f polypeptide-interacting
                     protein-binding protein 1; PTPRF-interacting
                     protein-binding protein 1; PTPRF interacting protein,
                     binding protein 1 (liprin beta 1)"
                     /calculated_mol_wt=110166
     Region          <54..>321
                     /region_name="SCP-1"
                     /note="Synaptonemal complex protein 1 (SCP-1); pfam05483"
                     /db_xref="CDD:114219"
     Region          613..676
                     /region_name="SAM_liprin-beta1,2_repeat1"
                     /note="SAM domain of liprin-beta1,2 proteins repeat 1;
                     cd09563"
                     /db_xref="CDD:188962"
     Region          687..749
                     /region_name="SAM_liprin-beta1,2_repeat2"
                     /note="SAM domain of liprin-beta1,2 proteins repeat 2;
                     cd09566"
                     /db_xref="CDD:188965"
     Region          772..843
                     /region_name="SAM_liprin-beta1,2_repeat3"
                     /note="SAM domain of liprin-beta proteins repeat 3;
                     cd09569"
                     /db_xref="CDD:188968"
     CDS             1..980
                     /gene="PPFIBP1"
                     /gene_synonym="hSGT2; hSgt2p; L2; NEDSMBA; SGT2"
                     /coded_by="NM_001198916.2:284..3226"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS55813.1"
                     /db_xref="GeneID:8496"
                     /db_xref="HGNC:HGNC:9249"
                     /db_xref="MIM:603141"
ORIGIN      
        1 mmsdasdmla aaleqmdgii agskaleysn gifdcqspts pfmgslralh lvedlrglle
       61 mmetdekegl rcqipdstae tlvewlqsqm tnghlpgngd vyqerlarle ndkeslvlqv
      121 svltdqveaq gekirdlefc leehrekvna teemlqqell srtsletqkl dlmaeisnlk
      181 lkltavekdr ldyedkfrdt egliqeindl rlkvsemdse rlqyekklks tkdelaslke
      241 qleekesevk rlqeklvckm kgegveivdr dievqkmkka veslmaanee kdrkiedlrq
      301 clnrykkmqd tvvlaqgkdg eyeellnsss isslldaqgf sdlekspspt pvmgspscdp
      361 fntsvpeefh ttilqvsips llpatvsmet sekskltpkp etsfeendgn iilgatvdtq
      421 lcdklltssl qkssslgnlk ketsdgeket iqktsedrap aesrpfgtlp prppgqdtsm
      481 ddnpfgtrkv rssfgrgffk iksnkrtasa pnlaeteket aehldlagas srpkdsqrns
      541 pfqipppspd skkksrgimk lfgklrrsqs ttfnpddmse pefkrggtra tagprlgwsr
      601 dlgqsnsdld mpfakwtkeq vcnwlmeqgl gsylnsgkhw iasgqtllqa sqqdlekelg
      661 ikhslhrkkl qlalqalgse eetnhgkldf nwvtrwlddi glpqyktqfd egrvdgrmlh
      721 ymtvddllsl kvvsvlhhls ikraiqvlri nnfepnclrr rpsdentiap sevqkwtnhr
      781 vmewlrsvdl aeyapnlrgs gvhgglmvle prfnvetmaq llnippnktl lrrhlathfn
      841 lligaeaqhq krdamelpdy vlltatakvk pkklafsnfg nlrkkkqedg eeyvcpmelg
      901 qasgsaskkg fkpgldmrly eeddldrleq medsegtvrq igafseginn lthmlkeddm
      961 fkdfaarsps asitdedsnv
//
LOCUS       NP_001371782            1057 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 85 [Homo sapiens].
ACCESSION   NP_001371782
VERSION     NP_001371782.1
DBSOURCE    REFSEQ: accession NM_001384853.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1057)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1057)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1057)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1057)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1057)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1057)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1057)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1057
                     /product="microtubule-associated protein 4 isoform 85"
                     /note="MAP-4"
                     /calculated_mol_wt=111234
     Region          <534..878
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          898..927
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          929..958
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          960..990
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1057
                     /gene="MAP4"
                     /coded_by="NM_001384853.1:96..3269"
                     /note="isoform 85 is encoded by transcript variant 104"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgsp tefleekmay qeypnsqnwp
      121 edtnfcfqpe qvvdpiqtdp fkmyhdddla dlvfpssata dtsifagqnd plkdsyvple
      181 lakeiemase erppaqalei mmglkttdma psketemala kdmalatkte valakdmesp
      241 tkldvtlakd mqpsmesdma lvkdmelpte kevalvkdvr wptetdvssa knvvlptete
      301 vapakdvtll keteraspik mdlapskdmg ppkenkkete raspikmdla pskdmgppke
      361 nkivpakdlv llseievaqa ndiissteis saekvalsse tevalardmt lppetnvilt
      421 kdkalpleae vapvkdmaql peteiapakd vapstvkevg llkdmsplse temalgkdvt
      481 pppetevvli knvclppeme valtedqvpa lkteaplakd gvltlannvt pakdvpplse
      541 teatpvpikd meiaqtqkgi sedshleslq dvgqsaaptf mispetvtgt gkkcslpaee
      601 dsvleklger kpcnsqpsel ssetsgiarp eegrpvvsgt gndittppnk elppspekkt
      661 kplattqpak tstskaktqp tslpkqpapt tigglnkkpm slasglvpaa ppkrpavasa
      721 rpsilpskdv kpkpiadaka pekraspskp asapasrsgs kstqtvaktt taaavastgp
      781 ssrspstllp kkptaikteg kpaevkkmta ksvpadlsrp kststssmkk tttlsgtapa
      841 agvvpsrvka tpmpsrpstt pfidkkptsa kpssttprls rlatntsapd lknvrskvqi
      901 vskkvsyshi qskcgskdni khvpgggnvq iqnkkvdisk vsskcgskan ikhkpgggdv
      961 kiesqklnfk ekaqakvgsl dnvghlpagg avktegggse aplcpgppag eepaiseaap
     1021 eagaptsasg lnghptlsgg gdqreaqtld sqiqetn
//
LOCUS       NP_001333532             451 aa            linear   PRI 21-NOV-2025
DEFINITION  RAD50-interacting protein 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001333532 XP_016867987
VERSION     NP_001333532.1
DBSOURCE    REFSEQ: accession NM_001346603.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Arnold,F., Gout,J., Wiese,H., Weissinger,S.E., Roger,E.,
            Perkhofer,L., Walter,K., Scheible,J., Prelli Bozzo,C., Lechel,A.,
            Ettrich,T.J., Azoitei,N., Hao,L., Furstberger,A., Kaminska,E.K.,
            Sparrer,K.M.J., Rasche,V., Wiese,S., Kestler,H.A., Moller,P.,
            Seufferlein,T., Frappart,P.O. and Kleger,A.
  TITLE     RINT1 Regulates SUMOylation and the DNA Damage Response to Preserve
            Cellular Homeostasis in Pancreatic Cancer
  JOURNAL   Cancer Res 81 (7), 1758-1774 (2021)
   PUBMED   33531371
  REMARK    GeneRIF: RINT1 Regulates SUMOylation and the DNA Damage Response to
            Preserve Cellular Homeostasis in Pancreatic Cancer.
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Arasaki,K., Taniguchi,M., Tani,K. and Tagaya,M.
  TITLE     RINT-1 regulates the localization and entry of ZW10 to the syntaxin
            18 complex
  JOURNAL   Mol Biol Cell 17 (6), 2780-2788 (2006)
   PUBMED   16571679
  REMARK    GeneRIF: RINT-1 coordinates the localization and function of ZW10
            by serving as a link between ZW10 and the SNARE complex comprising
            syntaxin 18.
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Kops,G.J., Kim,Y., Weaver,B.A., Mao,Y., McLeod,I., Yates,J.R. 3rd,
            Tagaya,M. and Cleveland,D.W.
  TITLE     ZW10 links mitotic checkpoint signaling to the structural
            kinetochore
  JOURNAL   J Cell Biol 169 (1), 49-60 (2005)
   PUBMED   15824131
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Nakajima,K., Hirose,H., Taniguchi,M., Kurashina,H., Arasaki,K.,
            Nagahama,M., Tani,K., Yamamoto,A. and Tagaya,M.
  TITLE     Involvement of BNIP1 in apoptosis and endoplasmic reticulum
            membrane fusion
  JOURNAL   EMBO J 23 (16), 3216-3226 (2004)
   PUBMED   15272311
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Hirose,H., Arasaki,K., Dohmae,N., Takio,K., Hatsuzawa,K.,
            Nagahama,M., Tani,K., Yamamoto,A., Tohyama,M. and Tagaya,M.
  TITLE     Implication of ZW10 in membrane trafficking between the endoplasmic
            reticulum and Golgi
  JOURNAL   EMBO J 23 (6), 1267-1278 (2004)
   PUBMED   15029241
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Xiao,J., Liu,C.C., Chen,P.L. and Lee,W.H.
  TITLE     RINT-1, a novel Rad50-interacting protein, participates in
            radiation-induced G(2)/M checkpoint control
  JOURNAL   J Biol Chem 276 (9), 6105-6111 (2001)
   PUBMED   11096100
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073073.2 and AA281630.1.
            
            On Oct 21, 2016 this sequence version replaced XP_016867987.1.
            
            Summary: This gene encodes a protein first identified for its
            ability to interact with the RAD50 double strand break repair
            protein, with the resulting interaction implicated in the
            regulation of cell cycle progression and telomere length. The
            encoded protein may also play a role in trafficking of cellular
            cargo from the endosome to the trans-Golgi network. Mutations in
            this gene may be associated with breast cancer in human patients.
            [provided by RefSeq, Oct 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1148965.1,
                                           SRR1660809.243000.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.3"
     Protein         1..451
                     /product="RAD50-interacting protein 1 isoform 3"
                     /note="Rad50-interacting protein 1"
                     /calculated_mol_wt=51843
     Region          1..443
                     /region_name="RINT1_TIP1"
                     /note="RINT-1 / TIP-1 family; pfam04437"
                     /db_xref="CDD:461309"
     CDS             1..451
                     /gene="RINT1"
                     /gene_synonym="ILFS3; RINT-1"
                     /coded_by="NM_001346603.2:658..2013"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="GeneID:60561"
                     /db_xref="HGNC:HGNC:21876"
                     /db_xref="MIM:610089"
ORIGIN      
        1 mwignhtefl dekiqpildk vgslvnarle fsrglmmlvl eklatdipcl lyddnlfchl
       61 vdevllfere lhsvhgypgt fascmhilse etcfqrwltv erkfalqkmd smlsseaawv
      121 sqykditdvd emkvpdcaet fmtlllvitd ryknlptasr klqflelqkd lvddfrirlt
      181 qvmkeetras lgfrycailn avnyistvla dwadnvfflq lqqaalevfa enntlsklql
      241 gqlasmessv fddminller lkhdmltrqv dhvfrevkda aklykkerwl slpsqseqav
      301 mslsssacpl lltlrdhllq leqqlcfslf kifwqmlvek ldvyiyqeii lanhfnegga
      361 aqlqfdmtrn lfplfshyck rpenyfkhik eacivlnlnv gsalllkdvl qsasgqlpat
      421 aalnevgiyk laqqdveill nlrtnwpntg k
//
LOCUS       NP_001135756             131 aa            linear   PRI 21-NOV-2025
DEFINITION  small ribosomal subunit protein eS24 isoform b [Homo sapiens].
ACCESSION   NP_001135756
VERSION     NP_001135756.1
DBSOURCE    REFSEQ: accession NM_001142284.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Park,J., Nam,D.H., Kim,D. and Chung,Y.J.
  TITLE     RPS24 alternative splicing is a marker of cancer progression and
            epithelial-mesenchymal transition
  JOURNAL   Sci Rep 14 (1), 13246 (2024)
   PUBMED   38853173
  REMARK    GeneRIF: RPS24 alternative splicing is a marker of cancer
            progression and epithelial-mesenchymal transition.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Kerry,J., Specker,E.J., Mizzoni,M., Brumwell,A., Fell,L.,
            Goodbrand,J., Rosen,M.N. and Uniacke,J.
  TITLE     Autophagy-dependent alternative splicing of ribosomal protein S24
            produces a more stable isoform that aids in hypoxic cell survival
  JOURNAL   FEBS Lett 598 (5), 503-520 (2024)
   PUBMED   38281767
  REMARK    GeneRIF: Autophagy-dependent alternative splicing of ribosomal
            protein S24 produces a more stable isoform that aids in hypoxic
            cell survival.
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Wang,S., Xia,L., Zhang,B., Zhang,H. and Lan,F.
  TITLE     Downregulated long intergenic non-coding RNA 00,174 represses
            malignant biological behaviors of lung cancer cells by regulating
            microRNA-584-3p/ribosomal protein S24 axis
  JOURNAL   Funct Integr Genomics 22 (4), 643-653 (2022)
   PUBMED   35451652
  REMARK    GeneRIF: Downregulated long intergenic non-coding RNA 00,174
            represses malignant biological behaviors of lung cancer cells by
            regulating microRNA-584-3p/ribosomal protein S24 axis.
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   5  (residues 1 to 131)
  AUTHORS   Kennedy,S.A., Jarboui,M.A., Srihari,S., Raso,C., Bryan,K.,
            Dernayka,L., Charitou,T., Bernal-Llinares,M., Herrera-Montavez,C.,
            Krstic,A., Matallanas,D., Kotlyar,M., Jurisica,I., Curak,J.,
            Wong,V., Stagljar,I., LeBihan,T., Imrie,L., Pillai,P., Lynn,M.A.,
            Fasterius,E., Al-Khalili Szigyarto,C., Breen,J., Kiel,C.,
            Serrano,L., Rauch,N., Rukhlenko,O., Kholodenko,B.N.,
            Iglesias-Martinez,L.F., Ryan,C.J., Pilkington,R., Cammareri,P.,
            Sansom,O., Shave,S., Auer,M., Horn,N., Klose,F., Ueffing,M.,
            Boldt,K., Lynn,D.J. and Kolch,W.
  TITLE     Extensive rewiring of the EGFR network in colorectal cancer cells
            expressing transforming levels of KRASG13D
  JOURNAL   Nat Commun 11 (1), 499 (2020)
   PUBMED   31980649
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 131)
  AUTHORS   Xu,W.B. and Roufa,D.J.
  TITLE     The gene encoding human ribosomal protein S24 and tissue-specific
            expression of differentially spliced mRNAs
  JOURNAL   Gene 169 (2), 257-262 (1996)
   PUBMED   8647458
REFERENCE   7  (residues 1 to 131)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   8  (residues 1 to 131)
  AUTHORS   Sieff,C.
  TITLE     DBA Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301769
REFERENCE   9  (residues 1 to 131)
  AUTHORS   Huang,R.T., Li,D.R., Wei,J., Huang,X.R., Yuan,X.T. and Tian,X.
  TITLE     Isolation and identification of hepatitis E virus in Xinjiang,
            China
  JOURNAL   J Gen Virol 73 (Pt 5), 1143-1148 (1992)
   PUBMED   1588318
REFERENCE   10 (residues 1 to 131)
  AUTHORS   Brown,S.J., Jewell,A., Maki,C.G. and Roufa,D.J.
  TITLE     A cDNA encoding human ribosomal protein S24
  JOURNAL   Gene 91 (2), 293-296 (1990)
   PUBMED   2210388
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG944046.1 and CD677556.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 40S subunit. The protein belongs
            to the S24E family of ribosomal proteins. It is located in the
            cytoplasm. Multiple transcript variants encoding different isoforms
            have been found for this gene. As is typical for genes encoding
            ribosomal proteins, there are multiple processed pseudogenes of
            this gene dispersed through the genome. Mutations in this gene
            result in Diamond-Blackfan anemia. [provided by RefSeq, Nov 2008].
            
            Transcript Variant: This variant (b) uses an alternate splice
            pattern in the 3' coding region, compared to variant d. The
            resulting protein (isoform b) has a shorter and distinct
            C-terminus, compared to isoform d. Variants b and f both encode the
            same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA776798.1, CD173411.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.3"
     Protein         1..131
                     /product="small ribosomal subunit protein eS24 isoform b"
                     /note="40S ribosomal protein S24; small ribosomal subunit
                     protein eS24"
                     /calculated_mol_wt=15066
     Region          1..130
                     /region_name="PTZ00071"
                     /note="40S ribosomal protein S24; Provisional"
                     /db_xref="CDD:240256"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P62847.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P62847.1)"
     CDS             1..131
                     /gene="RPS24"
                     /gene_synonym="DBA3; eS24; S24"
                     /coded_by="NM_001142284.2:40..435"
                     /note="isoform b is encoded by transcript variant b"
                     /db_xref="CCDS:CCDS86124.1"
                     /db_xref="GeneID:6229"
                     /db_xref="HGNC:HGNC:10411"
                     /db_xref="MIM:602412"
ORIGIN      
        1 mndtvtirtr kfmtnrllqr kqmvidvlhp gkatvpktei reklakmykt tpdvifvfgf
       61 rthfgggktt gfgmiydsld yakknepkhr larhglyekk ktsrkqrker knrmkkvrgt
      121 akanvgagkk k
//
LOCUS       NP_001091065              69 aa            linear   PRI 21-NOV-2025
DEFINITION  X antigen family member 1 isoform d [Homo sapiens].
ACCESSION   NP_001091065
VERSION     NP_001091065.1
DBSOURCE    REFSEQ: accession NM_001097596.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Skou,A.S., Juul-Dam,K.L., Hansen,M., Lausen,B., Stratmann,S.,
            Holmfeldt,L., Aggerholm,A., Nyvold,C.G., Ommen,H.B. and Hasle,H.
  TITLE     Measurable Residual Disease Monitoring of SPAG6, ST18, PRAME, and
            XAGE1A Expression in Peripheral Blood May Detect Imminent Relapse
            in Childhood Acute Myeloid Leukemia
  JOURNAL   J Mol Diagn 23 (12), 1787-1799 (2021)
   PUBMED   34600138
  REMARK    GeneRIF: Measurable Residual Disease Monitoring of SPAG6, ST18,
            PRAME, and XAGE1A Expression in Peripheral Blood May Detect
            Imminent Relapse in Childhood Acute Myeloid Leukemia.
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 69)
  AUTHORS   Sato,S., Noguchi,Y., Ohara,N., Uenaka,A., Shimono,M., Nakagawa,K.,
            Koizumi,F., Ishida,T., Yoshino,T., Shiratori,Y. and Nakayama,E.
  TITLE     Identification of XAGE-1 isoforms: predominant expression of
            XAGE-1b in testis and tumors
  JOURNAL   Cancer Immun 7, 5 (2007)
   PUBMED   17335148
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 69)
  AUTHORS   Nakagawa,K., Noguchi,Y., Uenaka,A., Sato,S., Okumura,H., Tanaka,M.,
            Shimono,M., Ali Eldib,A.M., Ono,T., Ohara,N., Yoshino,T.,
            Yamashita,K., Tsunoda,T., Aoe,M., Shimizu,N. and Nakayama,E.
  TITLE     XAGE-1 expression in non-small cell lung cancer and antibody
            response in patients
  JOURNAL   Clin Cancer Res 11 (15), 5496-5503 (2005)
   PUBMED   16061866
REFERENCE   6  (residues 1 to 69)
  AUTHORS   Zendman,A.J., Van Kraats,A.A., Weidle,U.H., Ruiter,D.J. and Van
            Muijen,G.N.
  TITLE     The XAGE family of cancer/testis-associated genes: alignment and
            expression profile in normal tissues, melanoma lesions and Ewing's
            sarcoma
  JOURNAL   Int J Cancer 99 (3), 361-369 (2002)
   PUBMED   11992404
REFERENCE   7  (residues 1 to 69)
  AUTHORS   Egland,K.A., Kumar,V., Duray,P. and Pastan,I.
  TITLE     Characterization of overlapping XAGE-1 transcripts encoding a
            cancer testis antigen expressed in lung, breast, and other types of
            cancers
  JOURNAL   Mol Cancer Ther 1 (7), 441-450 (2002)
   PUBMED   12479262
REFERENCE   8  (residues 1 to 69)
  AUTHORS   Zendman,A.J., van Kraats,A.A., den Hollander,A.I., Weidle,U.H.,
            Ruiter,D.J. and van Muijen,G.N.
  TITLE     Characterization of XAGE-1b, a short major transcript of
            cancer/testis-associated gene XAGE-1, induced in melanoma
            metastasis
  JOURNAL   Int J Cancer 97 (2), 195-204 (2002)
   PUBMED   11774264
REFERENCE   9  (residues 1 to 69)
  AUTHORS   Liu,X.F., Helman,L.J., Yeung,C., Bera,T.K., Lee,B. and Pastan,I.
  TITLE     XAGE-1, a new gene that is frequently expressed in Ewing's sarcoma
  JOURNAL   Cancer Res 60 (17), 4752-4755 (2000)
   PUBMED   10987281
REFERENCE   10 (residues 1 to 69)
  AUTHORS   Brinkmann,U., Vasmatzis,G., Lee,B. and Pastan,I.
  TITLE     Novel genes in the PAGE and GAGE family of tumor antigens found by
            homology walking in the dbEST database
  JOURNAL   Cancer Res 59 (7), 1445-1448 (1999)
   PUBMED   10197611
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX510359.5.
            
            Summary: This gene is a member of the XAGE subfamily, which belongs
            to the GAGE family. The GAGE genes are expressed in a variety of
            tumors and in some fetal and reproductive tissues. This gene is
            strongly expressed in Ewing's sarcoma, alveolar rhabdomyosarcoma
            and normal testis. The protein encoded by this gene contains a
            nuclear localization signal and shares a sequence similarity with
            other GAGE/PAGE proteins. Because of the expression pattern and the
            sequence similarity, this protein also belongs to a family of CT
            (cancer-testis) antigens. Alternative splicing of this gene, in
            addition to alternative transcription start sites, results in
            multiple transcript variants. [provided by RefSeq, Jan 2010].
            
            Transcript Variant: This variant (d, also known as XAGE-1d) starts
            at a downstream transcription start site, and uses an alternate
            splice site in an internal exon that causes a frameshift in the 3'
            coding region, compared to variant a. The encoded isoform (d) has a
            distinct and shorter C-terminus, compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138512.420946.1,
                                           DRR138512.23742.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..69
                     /product="X antigen family member 1 isoform d"
                     /note="cancer/testis antigen family 12, member 1b;
                     cancer/testis associated protein; G antigen family D
                     member 2; protein XAGE-1; cancer/testis antigen 12.1; X
                     antigen family member 1; X antigen family member 1B; G
                     antigen, family D, 2; cancer/testis antigen family 12,
                     member 1a"
                     /calculated_mol_wt=7834
     CDS             1..69
                     /gene="XAGE1A"
                     /gene_synonym="CT12.1; CT12.1A; CT12.1B; CTP9; GAGED2;
                     XAGE-1; XAGE1; XAGE1B"
                     /coded_by="NM_001097596.3:149..358"
                     /note="isoform d is encoded by transcript variant d"
                     /db_xref="CCDS:CCDS75983.1"
                     /db_xref="GeneID:653220"
                     /db_xref="HGNC:HGNC:4111"
                     /db_xref="MIM:300742"
ORIGIN      
        1 mespkkknqq lkvgilhlgs rqkkiriqlr sqvlgremrd megdlqelhq sntgdksgfg
       61 frrqgednt
//
LOCUS       NP_001161431             115 aa            linear   PRI 21-NOV-2025
DEFINITION  transmembrane protein 178A isoform 2 [Homo sapiens].
ACCESSION   NP_001161431
VERSION     NP_001161431.1
DBSOURCE    REFSEQ: accession NM_001167959.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Decker,C.E., Yang,Z., Rimer,R., Park-Min,K.H., Macaubas,C.,
            Mellins,E.D., Novack,D.V. and Faccio,R.
  TITLE     Tmem178 acts in a novel negative feedback loop targeting NFATc1 to
            regulate bone mass
  JOURNAL   Proc Natl Acad Sci U S A 112 (51), 15654-15659 (2015)
   PUBMED   26644563
  REMARK    GeneRIF: Tmem178 localizes to the ER membrane and regulates
            RANKL-induced Ca(2+) fluxes, thus controlling NFATc1 induction
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007246.3, BI757636.1 and BC029530.1.
            
            Transcript Variant: This variant (2) contains a distinct 5' UTR and
            lacks an in-frame portion of the 5' coding region, compared to
            variant 1. The resulting isoform (2) has a shorter N-terminus,
            compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI757636.1, SRR5189655.94955.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155550, SAMN02400288
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.1"
     Protein         1..115
                     /product="transmembrane protein 178A isoform 2"
                     /note="transmembrane protein 178"
                     /calculated_mol_wt=12369
     Region          <2..92
                     /region_name="PMP22_Claudin"
                     /note="PMP-22/EMP/MP20/Claudin family; cl21598"
                     /db_xref="CDD:473919"
     CDS             1..115
                     /gene="TMEM178A"
                     /gene_synonym="TMEM178"
                     /coded_by="NM_001167959.2:305..652"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:130733"
                     /db_xref="HGNC:HGNC:28517"
ORIGIN      
        1 mavavllcgc ivatvsffwe esltqhvagl lflmtgifct islctyaasi sydlnrlpkl
       61 iyslpadveh gyswsifcaw cslgfivaag glciaypfis rtkiaqlksg rdstv
//
LOCUS       NP_001374810             733 aa            linear   PRI 21-NOV-2025
DEFINITION  protein mono-ADP-ribosyltransferase PARP9 isoform g [Homo sapiens].
ACCESSION   NP_001374810
VERSION     NP_001374810.1
DBSOURCE    REFSEQ: accession NM_001387881.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 733)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 733)
  AUTHORS   Pandi,K., Angabo,S., Makkawi,H., Benyamini,H., Elgavish,S. and
            Nussbaum,G.
  TITLE     P. gingivalis-Induced TLR2 Interactome Analysis Reveals Association
            with PARP9
  JOURNAL   J Dent Res 103 (3), 329-338 (2024)
   PUBMED   38344758
  REMARK    GeneRIF: P. gingivalis-Induced TLR2 Interactome Analysis Reveals
            Association with PARP9.
REFERENCE   3  (residues 1 to 733)
  AUTHORS   Thirunavukkarasu,S., Ahmed,M., Rosa,B.A., Boothby,M., Cho,S.H.,
            Rangel-Moreno,J., Mbandi,S.K., Schreiber,V., Gupta,A., Zuniga,J.,
            Mitreva,M., Kaushal,D., Scriba,T.J. and Khader,S.A.
  TITLE     Poly(ADP-ribose) polymerase 9 mediates early protection against
            Mycobacterium tuberculosis infection by regulating type I IFN
            production
  JOURNAL   J Clin Invest 133 (12), e158630 (2023)
   PUBMED   37200107
  REMARK    GeneRIF: Poly(ADP-ribose) polymerase 9 mediates early protection
            against Mycobacterium tuberculosis infection by regulating type I
            IFN production.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 733)
  AUTHORS   Russo,L.C., Tomasin,R., Matos,I.A., Manucci,A.C., Sowa,S.T.,
            Dale,K., Caldecott,K.W., Lehtio,L., Schechtman,D., Meotti,F.C.,
            Bruni-Cardoso,A. and Hoch,N.C.
  TITLE     The SARS-CoV-2 Nsp3 macrodomain reverses PARP9/DTX3L-dependent
            ADP-ribosylation induced by interferon signaling
  JOURNAL   J Biol Chem 297 (3), 101041 (2021)
   PUBMED   34358560
  REMARK    GeneRIF: The SARS-CoV-2 Nsp3 macrodomain reverses
            PARP9/DTX3L-dependent ADP-ribosylation induced by interferon
            signaling.
REFERENCE   5  (residues 1 to 733)
  AUTHORS   Xing,J., Zhang,A., Du,Y., Fang,M., Minze,L.J., Liu,Y.J., Li,X.C.
            and Zhang,Z.
  TITLE     Identification of poly(ADP-ribose) polymerase 9 (PARP9) as a
            noncanonical sensor for RNA virus in dendritic cells
  JOURNAL   Nat Commun 12 (1), 2681 (2021)
   PUBMED   33976210
  REMARK    GeneRIF: Identification of poly(ADP-ribose) polymerase 9 (PARP9) as
            a noncanonical sensor for RNA virus in dendritic cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 733)
  AUTHORS   Jha,R., Agarwal,A., Mahfouz,R., Paasch,U., Grunewald,S.,
            Sabanegh,E., Yadav,S.P. and Sharma,R.
  TITLE     Determination of Poly (ADP-ribose) polymerase (PARP) homologues in
            human ejaculated sperm and its correlation with sperm maturation
  JOURNAL   Fertil Steril 91 (3), 782-790 (2009)
   PUBMED   18339380
  REMARK    GeneRIF: Determination of Poly (ADP-ribose) polymerase (PARP)
            homologues in human ejaculated sperm and its correlation with sperm
            maturation.
REFERENCE   7  (residues 1 to 733)
  AUTHORS   Juszczynski,P., Kutok,J.L., Li,C., Mitra,J., Aguiar,R.C. and
            Shipp,M.A.
  TITLE     BAL1 and BBAP are regulated by a gamma interferon-responsive
            bidirectional promoter and are overexpressed in diffuse large
            B-cell lymphomas with a prominent inflammatory infiltrate
  JOURNAL   Mol Cell Biol 26 (14), 5348-5359 (2006)
   PUBMED   16809771
  REMARK    GeneRIF: BAL1 and BBAP are located on chromosome 3q21 in a
            head-to-head orientation and are regulated by a
            IFN-gamma-responsive bidirectional promoter.
REFERENCE   8  (residues 1 to 733)
  AUTHORS   Aguiar,R.C., Takeyama,K., He,C., Kreinbrink,K. and Shipp,M.A.
  TITLE     B-aggressive lymphoma family proteins have unique domains that
            modulate transcription and exhibit poly(ADP-ribose) polymerase
            activity
  JOURNAL   J Biol Chem 280 (40), 33756-33765 (2005)
   PUBMED   16061477
REFERENCE   9  (residues 1 to 733)
  AUTHORS   Takeyama,K., Aguiar,R.C., Gu,L., He,C., Freeman,G.J., Kutok,J.L.,
            Aster,J.C. and Shipp,M.A.
  TITLE     The BAL-binding protein BBAP and related Deltex family members
            exhibit ubiquitin-protein isopeptide ligase activity
  JOURNAL   J Biol Chem 278 (24), 21930-21937 (2003)
   PUBMED   12670957
REFERENCE   10 (residues 1 to 733)
  AUTHORS   Aguiar,R.C., Yakushijin,Y., Kharbanda,S., Salgia,R., Fletcher,J.A.
            and Shipp,M.A.
  TITLE     BAL is a novel risk-related gene in diffuse large B-cell lymphomas
            that enhances cellular migration
  JOURNAL   Blood 96 (13), 4328-4334 (2000)
   PUBMED   11110709
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092908.9 and AC096861.5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.509048.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.1"
     Protein         1..733
                     /product="protein mono-ADP-ribosyltransferase PARP9
                     isoform g"
                     /EC_number="2.4.2.30"
                     /note="poly [ADP-ribose] polymerase 9; poly (ADP-ribose)
                     polymerase 9; PARP-9; b aggressive lymphoma protein;
                     ADP-ribosyltransferase diphtheria toxin-like 9; protein
                     mono-ADP-ribosyltransferase PARP9"
                     /calculated_mol_wt=82470
     Region          82..242
                     /region_name="Macro_Af1521_BAL-like"
                     /note="macrodomain, Af1521-like family; cd02907"
                     /db_xref="CDD:394877"
     Site            order(90..92,103..105,109..115,117,203..209)
                     /site_type="other"
                     /note="ADP-ribose binding site [chemical binding]"
                     /db_xref="CDD:394877"
     Region          275..451
                     /region_name="Macro_BAL-like"
                     /note="macrodomain, B-aggressive lymphoma (BAL)-like
                     family; cd02903"
                     /db_xref="CDD:394874"
     Site            order(290..292,302..304,310..313,316,394..400,434,440)
                     /site_type="other"
                     /note="ADP-ribose binding site [chemical binding]"
                     /db_xref="CDD:394874"
     Region          667..>694
                     /region_name="ADP_ribosyl"
                     /note="ADP_ribosylating enzymes catalyze the transfer of
                     ADP_ribose from NAD+ to substrates. Bacterial toxins are
                     cytoplasmic and catalyze the transfer of a single
                     ADP_ribose unit to eukaryotic elongation factor 2, halting
                     protein synthesis and killing the cell; cl00283"
                     /db_xref="CDD:444809"
     CDS             1..733
                     /gene="PARP9"
                     /gene_synonym="ARTD9; BAL; BAL1; MGC:7868"
                     /coded_by="NM_001387881.1:277..2478"
                     /note="isoform g is encoded by transcript variant 20"
                     /db_xref="GeneID:83666"
                     /db_xref="HGNC:HGNC:24118"
                     /db_xref="MIM:612065"
ORIGIN      
        1 mdfsmvagaa ayneksetga lgenyswqip inhndfkilk nnerqlcevl qnkfgcistl
       61 vspvqegnsk slqvfrkmlt prielsvwkd dltthavdav vnaanedllh ggglalalvk
      121 aggfeiqees kqfvarygkv sageiavtga grlpckqiih avgprwmewd kqgctgklqr
      181 aivsilnyvi yknthiktva ipalssgifq fplnlctkti vetirvslqg kpmmsnlkei
      241 hlvsnedptv aafkaasefi lgkselgqet tpsfnamvvn nltlqivqgh iewqtadviv
      301 nsvnphditv gpvaksilqq agvemksefl atkakqfqrs qlvlvtkgfn lfckyiyhvl
      361 whsefpkpqi lkhamkecle kcieqnitsi sfpalgtgnm eikketaaei lfdevltfak
      421 dhvkhqltvk fvifptdlei ykafssemak rskmlslnny svpqstreek renglearsp
      481 ainlmgfnve emyeahawiq rilslqnhhi iennhilylg rkehdilsql qktssvsite
      541 iispgrtele iegaradlie vvmniedmlc kvqeemarkk erglwrslgq wtiqqqktqd
      601 emkeniiflk cpvpptqell dqkkqfekcg lqvlkvekid nevlmaafqr kkkmmeeklh
      661 rqpvshrlfq qvpyqfcnvv crvgfqrmys tpceigshcv aqaslkllts tnppalasqs
      721 agitdmshsa wkf
//
LOCUS       NP_001372236             802 aa            linear   PRI 21-NOV-2025
DEFINITION  receptor-type tyrosine-protein phosphatase alpha isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_001372236
VERSION     NP_001372236.1
DBSOURCE    REFSEQ: accession NM_001385307.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 802)
  AUTHORS   Fang,J., Zhang,Y., Huang,C., Lu,R., Yu,J., Chen,R., Wang,Y.,
            Zhao,X., Yu,J. and Huang,J.
  TITLE     Glucose-mediated N-glycosylation of RPTPalpha affects its
            subcellular localization and Src activation
  JOURNAL   Oncogene 42 (14), 1058-1071 (2023)
   PUBMED   36765146
  REMARK    GeneRIF: Glucose-mediated N-glycosylation of RPTPalpha affects its
            subcellular localization and Src activation.
REFERENCE   3  (residues 1 to 802)
  AUTHORS   Hill,M.A., Bentley,S.R., Walker,T.L., Mellick,G.D., Wood,S.A. and
            Sykes,A.M.
  TITLE     Does a rare mutation in PTPRA contribute to the development of
            Parkinson's disease in an Australian multi-incident family?
  JOURNAL   PLoS One 17 (7), e0271499 (2022)
   PUBMED   35900966
  REMARK    GeneRIF: Does a rare mutation in PTPRA contribute to the
            development of Parkinson's disease in an Australian multi-incident
            family?
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 802)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 802)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 802)
  AUTHORS   Zheng,X.M., Wang,Y. and Pallen,C.J.
  TITLE     Cell transformation and activation of pp60c-src by overexpression
            of a protein tyrosine phosphatase
  JOURNAL   Nature 359 (6393), 336-339 (1992)
   PUBMED   1383828
REFERENCE   7  (residues 1 to 802)
  AUTHORS   Rao,V.V., Loffler,C., Sap,J., Schlessinger,J. and Hansmann,I.
  TITLE     The gene for receptor-linked protein-tyrosine-phosphatase (PTPA) is
            assigned to human chromosome 20p12-pter by in situ hybridization
            (ISH and FISH)
  JOURNAL   Genomics 13 (3), 906-907 (1992)
   PUBMED   1639427
REFERENCE   8  (residues 1 to 802)
  AUTHORS   Jirik,F.R., Anderson,L.L. and Duncan,A.M.
  TITLE     The human protein-tyrosine phosphatase PTP alpha/LRP gene (PTPA) is
            assigned to chromosome 20p13
  JOURNAL   Cytogenet Cell Genet 60 (2), 117-118 (1992)
   PUBMED   1611910
REFERENCE   9  (residues 1 to 802)
  AUTHORS   Kaplan,R., Morse,B., Huebner,K., Croce,C., Howk,R., Ravera,M.,
            Ricca,G., Jaye,M. and Schlessinger,J.
  TITLE     Cloning of three human tyrosine phosphatases reveals a multigene
            family of receptor-linked protein-tyrosine-phosphatases expressed
            in brain
  JOURNAL   Proc Natl Acad Sci U S A 87 (18), 7000-7004 (1990)
   PUBMED   2169617
REFERENCE   10 (residues 1 to 802)
  AUTHORS   Sap,J., D'Eustachio,P., Givol,D. and Schlessinger,J.
  TITLE     Cloning and expression of a widely expressed receptor tyrosine
            phosphatase
  JOURNAL   Proc Natl Acad Sci U S A 87 (16), 6112-6116 (1990)
   PUBMED   2166945
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL161656.20 and AL121905.23.
            
            Summary: The protein encoded by this gene is a member of the
            protein tyrosine phosphatase (PTP) family. PTPs are known to be
            signaling molecules that regulate a variety of cellular processes
            including cell growth, differentiation, mitotic cycle, and
            oncogenic transformation. This PTP contains an extracellular
            domain, a single transmembrane segment and two tandem
            intracytoplasmic catalytic domains, and thus represents a
            receptor-type PTP. This PTP has been shown to dephosphorylate and
            activate Src family tyrosine kinases, and is implicated in the
            regulation of integrin signaling, cell adhesion and proliferation.
            Three alternatively spliced variants of this gene, which encode two
            distinct isoforms, have been reported. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1799922.1,
                                           SRR14038193.1991774.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151358 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..802
                     /product="receptor-type tyrosine-protein phosphatase alpha
                     isoform 1 precursor"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase, receptor type, alpha
                     polypeptide; PTPase-alpha; Leukocyte common
                     antigen-related peptide (protein tyrosine phosphate);
                     tyrosine phosphatase alpha; PTPLCA-related phosphatase;
                     receptor-type tyrosine-protein phosphatase alpha;
                     protein-tyrosine phosphatase alpha"
                     /calculated_mol_wt=88713
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2024
     mat_peptide     20..802
                     /product="Receptor-type tyrosine-protein phosphatase
                     alpha. /id=PRO_0000025433"
                     /note="propagated from UniProtKB/Swiss-Prot (P18433.3)"
                     /calculated_mol_wt=88713
     Site            21
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Site            36
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Region          39..59
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18433.3)"
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Region          79..146
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18433.3)"
     Site            80
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Site            86
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Site            124
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Site            152..174
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18433.3)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P18052; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P18052; propagated from
                     UniProtKB/Swiss-Prot (P18433.3)"
     Region          214..509
                     /region_name="R-PTPc-A-1"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase A, repeat 1; cd14621"
                     /db_xref="CDD:350469"
     Region          563..790
                     /region_name="R-PTPc-A-2"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase A, repeat 2; cd14623"
                     /db_xref="CDD:350471"
     Site            798
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:22801373,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P18433.3)"
     CDS             1..802
                     /gene="PTPRA"
                     /gene_synonym="HEPTP; HLPR; HPTPA; HPTPalpha; LRP; PTPA;
                     PTPRL2; R-PTP-alpha; RPTPA"
                     /coded_by="NM_001385307.1:330..2738"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 9"
                     /db_xref="CCDS:CCDS13038.1"
                     /db_xref="GeneID:5786"
                     /db_xref="HGNC:HGNC:9664"
                     /db_xref="MIM:176884"
ORIGIN      
        1 mdswfilvll gsglicvsan nattvapsvg itrlinssta epvkeeakts nptssltsls
       61 vaptfspnit lgptylttvn ssdsdngttr tastnsigit ispngtwlpd nqftdartep
      121 wegnsstaat tpetfppsgn sdskdrrdet piiavmvals sllvivfiii vlymlrfkky
      181 kqagshsnsf rlsngrtedv epqsvpllar spstnrkypp lpvdkleeei nrrmaddnkl
      241 freefnalpa cpiqatceaa skeenkeknr yvnilpydhs rvhltpvegv pdsdyinasf
      301 ingyqeknkf iaaqgpkeet vndfwrmiwe qntativmvt nlkerkeckc aqywpdqgcw
      361 tygnirvsve dvtvlvdytv rkfciqqvgd mtnrkpqrli tqfhftswpd fgvpftpigm
      421 lkflkkvkac npqyagaivv hcsagvgrtg tfvvidamld mmhterkvdv ygfvsriraq
      481 rcqmvqtdmq yvfiyqalle hylygdtele vtslethlqk iynkipgtsn ngleeefkkl
      541 tsikiqndkm rtgnlpanmk knrvlqiipy efnrviipvk rgeentdyvn asfidgyrqk
      601 dsyiasqgpl lhtiedfwrm iwewkscsiv mlteleergq ekcaqywpsd glvsygditv
      661 elkkeeeces ytvrdllvtn trenksrqir qfhfhgwpev gipsdgkgmi siiaavqkqq
      721 qqsgnhpitv hcsagagrtg tfcalstvle rvkaegildv fqtvkslrlq rphmvqtleq
      781 yefcykvvqe yidafsdyan fk
//
LOCUS       NP_001358899             996 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase I subunit RPA2 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001358899
VERSION     NP_001358899.1
DBSOURCE    REFSEQ: accession NM_001371970.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Ford,B.L., Wei,T., Liu,H., Scull,C.E., Najmi,S.M., Pitts,S.,
            Fan,W., Schneider,D.A. and Laiho,M.
  TITLE     Expression of RNA polymerase I catalytic core is influenced by
            RPA12
  JOURNAL   PLoS One 18 (5), e0285660 (2023)
   PUBMED   37167337
  REMARK    GeneRIF: Expression of RNA polymerase I catalytic core is
            influenced by RPA12.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 996)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   5  (residues 1 to 996)
  AUTHORS   Zhao,D., Liu,W., Chen,K., Wu,Z., Yang,H. and Xu,Y.
  TITLE     Structure of the human RNA polymerase I elongation complex
  JOURNAL   Cell Discov 7 (1), 97 (2021)
   PUBMED   34671025
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 996)
  AUTHORS   Miller,G., Panov,K.I., Friedrich,J.K., Trinkle-Mulcahy,L.,
            Lamond,A.I. and Zomerdijk,J.C.
  TITLE     hRRN3 is essential in the SL1-mediated recruitment of RNA
            Polymerase I to rRNA gene promoters
  JOURNAL   EMBO J 20 (6), 1373-1382 (2001)
   PUBMED   11250903
REFERENCE   7  (residues 1 to 996)
  AUTHORS   Jansa,P., Mason,S.W., Hoffmann-Rohrer,U. and Grummt,I.
  TITLE     Cloning and functional characterization of PTRF, a novel protein
            which induces dissociation of paused ternary transcription
            complexes
  JOURNAL   EMBO J 17 (10), 2855-2864 (1998)
   PUBMED   9582279
REFERENCE   8  (residues 1 to 996)
  AUTHORS   Seither,P., Zatsepina,O., Hoffmann,M. and Grummt,I.
  TITLE     Constitutive and strong association of PAF53 with RNA polymerase I
  JOURNAL   Chromosoma 106 (4), 216-225 (1997)
   PUBMED   9254723
REFERENCE   9  (residues 1 to 996)
  AUTHORS   Seither,P. and Grummt,I.
  TITLE     Molecular cloning of RPA2, the gene encoding the second largest
            subunit of mouse RNA polymerase I
  JOURNAL   Genomics 37 (1), 135-139 (1996)
   PUBMED   8921381
REFERENCE   10 (residues 1 to 996)
  AUTHORS   Barbosa,M., Jabs,E.W. and Huston,S.
  TITLE     Treacher Collins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301704
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012442.7.
            
            Summary: Eukaryotic RNA polymerase I (pol I) is responsible for the
            transcription of ribosomal RNA (rRNA) genes and production of rRNA,
            the primary component of ribosomes. Pol I is a multisubunit enzyme
            composed of 6 to 14 polypeptides, depending on the species. Most of
            the mass of the pol I complex derives from the 2 largest subunits,
            Rpa1 and Rpa2 in yeast. POLR1B is homologous to Rpa2 (Seither and
            Grummt, 1996 [PubMed 8921381]).[supplied by OMIM, Mar 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.93936.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.1"
     Protein         1..996
                     /product="DNA-directed RNA polymerase I subunit RPA2
                     isoform 6"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerase I subunit RPA2;
                     DNA-directed RNA polymerase I 135kDa polypeptide; RNA
                     polymerase I subunit 2; DNA-directed RNA polymerase I 135
                     kDa polypeptide; polymerase (RNA) I polypeptide B, 128kDa;
                     polymerase (RNA) I subunit B"
                     /calculated_mol_wt=112721
     Region          1..994
                     /region_name="RNA_pol_B_RPB2"
                     /note="RNA polymerase beta subunit. RNA polymerases
                     catalyse the DNA dependent polymerization of RNA.
                     Prokaryotes contain a single RNA polymerase compared to
                     three in eukaryotes (not including mitochondrial. and
                     chloroplast polymerases). Each RNA polymerase...; cd00653"
                     /db_xref="CDD:238353"
     Region          47..236
                     /region_name="RNA_pol_Rpb2_2"
                     /note="RNA polymerase Rpb2, domain 2; pfam04561"
                     /db_xref="CDD:398318"
     Site            order(346,348..350,352,355,360,521,539..541,543,606..609,
                     612,614..616,751,753,755,777,779,782,785,790,794,811,842,
                     850..852,854,867,870..872,874..875,896..898,902,904..905,
                     907,909..914,916..921,925,974,978,980,982..983,985,
                     987..990,992,994)
                     /site_type="other"
                     /note="RPB1 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     Region          424..482
                     /region_name="RNA_pol_Rpa2_4"
                     /note="RNA polymerase I, Rpa2 specific domain; pfam06883"
                     /db_xref="CDD:462028"
     Site            order(579..580,601,603,624,627,760,773,800..801,803,838,
                     855)
                     /site_type="other"
                     /note="RPB10 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     Site            order(612,626,759,844)
                     /site_type="other"
                     /note="RPB11 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     Site            order(626..627,631,733,735,760..762,765,767..768,843..850,
                     852)
                     /site_type="other"
                     /note="RPB3 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     Site            order(631,669,671,675..677,679)
                     /site_type="other"
                     /note="RPB12 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     CDS             1..996
                     /gene="POLR1B"
                     /gene_synonym="A135; RPA135; RPA2; Rpo1-2; TCS4"
                     /coded_by="NM_001371970.1:706..3696"
                     /note="isoform 6 is encoded by transcript variant 9"
                     /db_xref="GeneID:84172"
                     /db_xref="HGNC:HGNC:20454"
                     /db_xref="MIM:602000"
ORIGIN      
        1 mvksklcnlr nlppqalieh heeaeemggy fiingiekvi rmlimprrnf piamirpkwk
       61 trgpgytqyg vsmhcvreeh savnmnlhyl engtvmlnfi yrkelfflpl gfalkalvsf
      121 sdyqifqeli kgkeddsflr nsvsqmlriv meegcstqkq vlnylgecfr vklnvpdwyp
      181 neqaaeflfn qcicihlksn tekfymlclm trklfalakg ecmednpdsl vnqevltpgq
      241 lflmflkekl egwlvsikia fdkkaqktsv smntdnlmri ftmgidltkp feylfatgnl
      301 rsktglgllq dsglcvvadk lnfirylshf rcvhrgadfa kmrtttvrrl lpeswgflcp
      361 vhtpdgepcg lmnhltavce vvtqfvytas ipallcnlgv tpidgaphrs ysecypvlld
      421 gvmvgwvdkd lapgiadslr hfkvlrekri ppwmevvlip mtgkpslypg lflfttpcrl
      481 vrpvqnlalg keeligtmeq ifmnvaifed evfagvtthq elfphsllsv ianfipfsdh
      541 nqsprnmyqc qmgkqtmgfp lltyqdrsdn klyrlqtpqs plvrpsmydy ydmdnypigt
      601 naivavisyt gydmedamiv nkaswergfa hgsvyksefi dlsekikqgd sslvfgikpg
      661 dprvlqkldd dglpfigakl qygdpyysyl nlntgesfvm yykskencvv dnikvcsndt
      721 gsgkfkcvci tmrvprnpti gdkfasrhgq kgilsrlwpa edmpftesgm vpdilfnphg
      781 fpsrmtigml iesmagksaa lhglchdatp fifseensal eyfgemlkaa gynfygterl
      841 ysgisglele adifigvvyy qrlrhmvsdk fqvrttgard rvtnqpiggr nvqggirfge
      901 merdallahg tsfllhdrlf ncsdrsvahv cvkcgsllsp llekpppsws amrnrkynct
      961 lcsrsdtidt vsvpyvfryf vaelaamnik vkldvv
//
LOCUS       NP_001378823            1585 aa            linear   PRI 21-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4 gamma 3 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001378823
VERSION     NP_001378823.1
DBSOURCE    REFSEQ: accession NM_001391894.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1585)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1585)
  AUTHORS   Kang,J.Y., Wen,Z., Pan,D., Zhang,Y., Li,Q., Zhong,A., Yu,X.,
            Wu,Y.C., Chen,Y., Zhang,X., Kou,P.C., Geng,J., Wang,Y.Y., Hua,M.M.,
            Zong,R., Li,B., Shi,H.J., Li,D., Fu,X.D., Li,J., Nelson,D.L.,
            Guo,X., Zhou,Y., Gou,L.T., Huang,Y. and Liu,M.F.
  TITLE     LLPS of FXR1 drives spermiogenesis by activating translation of
            stored mRNAs
  JOURNAL   Science 377 (6607), eabj6647 (2022)
   PUBMED   35951695
REFERENCE   3  (residues 1 to 1585)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1585)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 1585)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1585)
  AUTHORS   Waskiewicz,A.J., Johnson,J.C., Penn,B., Mahalingam,M., Kimball,S.R.
            and Cooper,J.A.
  TITLE     Phosphorylation of the cap-binding protein eukaryotic translation
            initiation factor 4E by protein kinase Mnk1 in vivo
  JOURNAL   Mol Cell Biol 19 (3), 1871-1880 (1999)
   PUBMED   10022874
REFERENCE   7  (residues 1 to 1585)
  AUTHORS   Pyronnet,S., Imataka,H., Gingras,A.C., Fukunaga,R., Hunter,T. and
            Sonenberg,N.
  TITLE     Human eukaryotic translation initiation factor 4G (eIF4G) recruits
            mnk1 to phosphorylate eIF4E
  JOURNAL   EMBO J 18 (1), 270-279 (1999)
   PUBMED   9878069
REFERENCE   8  (residues 1 to 1585)
  AUTHORS   Gingras,A.C., Raught,B. and Sonenberg,N.
  TITLE     eIF4 initiation factors: effectors of mRNA recruitment to ribosomes
            and regulators of translation
  JOURNAL   Annu Rev Biochem 68, 913-963 (1999)
   PUBMED   10872469
  REMARK    Review article
REFERENCE   9  (residues 1 to 1585)
  AUTHORS   Imataka,H., Gradi,A. and Sonenberg,N.
  TITLE     A newly identified N-terminal amino acid sequence of human eIF4G
            binds poly(A)-binding protein and functions in poly(A)-dependent
            translation
  JOURNAL   EMBO J 17 (24), 7480-7489 (1998)
   PUBMED   9857202
REFERENCE   10 (residues 1 to 1585)
  AUTHORS   Gradi,A., Imataka,H., Svitkin,Y.V., Rom,E., Raught,B., Morino,S.
            and Sonenberg,N.
  TITLE     A novel functional human eukaryotic translation initiation factor
            4G
  JOURNAL   Mol Cell Biol 18 (1), 334-342 (1998)
   PUBMED   9418880
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031005.2, AL627311.16,
            AL358392.19 and AL606477.11.
            
            Summary: The protein encoded by this gene is thought to be part of
            the eIF4F protein complex, which is involved in mRNA cap
            recognition and transport of mRNAs to the ribosome. Interestingly,
            a microRNA (miR-520c-3p) has been found that negatively regulates
            synthesis of the encoded protein, and this leads to a global
            decrease in protein translation and cell proliferation. Therefore,
            this protein is a key component of the anti-tumor activity of
            miR-520c-3p. [provided by RefSeq, May 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4105339.1,
                                           SRR18074967.2670588.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1585
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     Protein         1..1585
                     /product="eukaryotic translation initiation factor 4 gamma
                     3 isoform 3"
                     /note="eIF-4-gamma 3; eIF-4-gamma II"
                     /calculated_mol_wt=176522
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          <10..>296
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     Region          128..190
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          134..162
                     /region_name="PABPC1-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q80XI3; propagated from
                     UniProtKB/Swiss-Prot (O43432.2)"
     Region          208..232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43432.2)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43432.2)"
     Region          305..332
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XI3; propagated from
                     UniProtKB/Swiss-Prot (O43432.2)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          567..620
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          619..630
                     /region_name="EIF4E-binding.
                     /evidence=ECO:0000250|UniProtKB:Q04637"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          686..711
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          699..1019
                     /region_name="eIF3/EIF4A-binding.
                     /evidence=ECO:0000250|UniProtKB:Q04637"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Site            699..700
                     /site_type="cleavage"
                     /note="Cleavage, by enterovirus/rhinovirus protease 2A;
                     propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Site            700..701
                     /site_type="cleavage"
                     /note="Cleavage, by foot-and-mouth disease virus leader
                     protease; propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          729..749
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          755..983
                     /region_name="MIF4G"
                     /note="MIF4G domain; pfam02854"
                     /db_xref="CDD:397130"
     Region          860..880
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          1017..1042
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          1072..1219
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Site            1156
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK1.
                     /evidence=ECO:0000269|PubMed:14507913; propagated from
                     UniProtKB/Swiss-Prot (O43432.2)"
     Site            1218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43432.2)"
     Region          1222..1334
                     /region_name="MA3"
                     /note="MA3 domain; pfam02847"
                     /db_xref="CDD:397128"
     Site            1409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43432.2)"
     Region          1428..1556
                     /region_name="W2_eIF4G1_like"
                     /note="C-terminal W2 domain of eukaryotic translation
                     initiation factor 4 gamma 1 and similar proteins; cd11559"
                     /db_xref="CDD:211397"
     Region          1433..1585
                     /region_name="EIF4A-binding.
                     /evidence=ECO:0000250|UniProtKB:Q04637"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          <1535..1581
                     /region_name="W2"
                     /note="C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon;
                     cl17013"
                     /db_xref="CDD:473053"
     Region          1571..1585
                     /region_name="Necessary but not sufficient for
                     MKNK1-binding. /evidence=ECO:0000250|UniProtKB:Q04637"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     CDS             1..1585
                     /gene="EIF4G3"
                     /gene_synonym="eIF-4G 3; eIF4G 3; eIF4GII"
                     /coded_by="NM_001391894.1:509..5266"
                     /note="isoform 3 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS214.1"
                     /db_xref="GeneID:8672"
                     /db_xref="HGNC:HGNC:3298"
                     /db_xref="MIM:603929"
ORIGIN      
        1 mnsqpqtrsp ffqrpqiqpp ratipnssps irpgaqtpta vyqanqhimm vnhlpmpypv
       61 pqgpqycipq yrhsgppyvg ppqqypvqpp gpgpfypgpg pgdfpnaygt pfypsqpvyq
      121 sapiivptqq qpppakrekk tirirdpnqg gkditeeims gggsrnptpp igrptstptp
      181 pqqlpsqvpe hspvvygtve sahlaastpv taasdqkqee kpkpdpvlks pspvlrlvls
      241 gekkeqegqt settaivsia elplppsptt vssvarstia aptssalssq pifttaiddr
      301 celsspredt ipipsltsct etsdplptne ndddickkpc svapndiplv sstnlinein
      361 gvseklsate siveivkqev lpltleleil enppeemkle cipapitpst vpsfpptppt
      421 ppaspphtpv ivpaaattvs spsaaitvqr vleedesirt clsedakeiq nkieveadgq
      481 teeildsqnl nsrrspvpaq iaitvpktwk kpkdrtrtte emleaelelk aeeelsidkv
      541 leseqdkmsq gfhperdpsd lkkvkaveen geeaepvrng aesvsegegi dansgstdss
      601 gdgvtfpfkp eswkptdteg kkqydrefll dfqfmpaciq kpeglppisd vvldkinqpk
      661 lpmrtldpri lprgpdftpa fadfgrqtpg grgvpllnvg srrsqpgqrr eprkiitvsv
      721 kedvhlkkae nawkpsqkrd sqaddpenik tqelfrkvrs ilnkltpqmf nqlmkqvsgl
      781 tvdteerlkg vidlvfekai depsfsvaya nmcrclvtlk vpmadkpgnt vnfrklllnr
      841 cqkefekdka dddvfekkqk eleaasapee rtrlhdelee akdkarrrsi gnikfigelf
      901 klkmlteaim hdcvvkllkn hdeesleclc rllttigkdl dfekakprmd qyfnqmekiv
      961 kerktssrir fmlqdvidlr lcnwvsrrad qgpktieqih keakieeqee qrkvqqlmtk
     1021 ekrrpgvqrv deggwntvqg aknsrvldps kflkitkpti dekiqlvpka qlgswgkgss
     1081 ggakasetda lrssasslnr fsalqppaps gstpstpvef dsrrtltsrg smgrekndkp
     1141 lpsatarpnt fmrggsskdl ldnqsqeeqr remletvkql tggvdverns teaernktre
     1201 sakpeisams ahdkaalsee elerksksii deflhindfk eamqcveeln aqgllhvfvr
     1261 vgvestlers qitrdhmgql lyqlvqsekl skqdffkgfs etleladdma idiphiwlyl
     1321 aelvtpmlke ggismrelti efskpllpvg ragvllseil hllckqmshk kvgalwread
     1381 lswkdflpeg edvhnflleq kldfiesdsp cssealskke lsaeelykrl ekliiedkan
     1441 deqifdwvea nldeiqmssp tflralmtav ckaaiiadss tfrvdtavik qrvpillkyl
     1501 dsdtekelqa lyalqasivk ldqpanllrm ffdclydeev isedafykwe sskdpaeqng
     1561 kgvalksvta fftwlreaee esedn
//
LOCUS       NP_001300953              79 aa            linear   PRI 21-NOV-2025
DEFINITION  endoribonuclease YbeY isoform 5 [Homo sapiens].
ACCESSION   NP_001300953
VERSION     NP_001300953.1
DBSOURCE    REFSEQ: accession NM_001314024.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 79)
  AUTHORS   D'Souza,A.R., Van Haute,L., Powell,C.A., Mutti,C.D., Palenikova,P.,
            Rebelo-Guiomar,P., Rorbach,J. and Minczuk,M.
  TITLE     YbeY is required for ribosome small subunit assembly and tRNA
            processing in human mitochondria
  JOURNAL   Nucleic Acids Res 49 (10), 5798-5812 (2021)
   PUBMED   34037799
  REMARK    GeneRIF: YbeY is required for ribosome small subunit assembly and
            tRNA processing in human mitochondria.
REFERENCE   4  (residues 1 to 79)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 79)
  AUTHORS   Liao,Z., Schelcher,C. and Smirnov,A.
  TITLE     YbeY, eminence grise of ribosome biogenesis
  JOURNAL   Biochem Soc Trans 49 (2), 727-745 (2021)
   PUBMED   33929506
  REMARK    GeneRIF: YbeY, eminence grise of ribosome biogenesis.
            Review article
REFERENCE   6  (residues 1 to 79)
  AUTHORS   Ghosal,A., Kohrer,C., Babu,V.M.P., Yamanaka,K., Davies,B.W.,
            Jacob,A.I., Ferullo,D.J., Gruber,C.C., Vercruysse,M. and
            Walker,G.C.
  TITLE     C21orf57 is a human homologue of bacterial YbeY proteins
  JOURNAL   Biochem Biophys Res Commun 484 (3), 612-617 (2017)
   PUBMED   28153719
  REMARK    GeneRIF: This observation suggests that the function of HuYbeY in
            human cells is likely regulated through specific interactions with
            partner proteins similarly to the way YbeY is regulated in
            bacteria.
REFERENCE   7  (residues 1 to 79)
  AUTHORS   Uhlen,M., Oksvold,P., Algenas,C., Hamsten,C., Fagerberg,L.,
            Klevebring,D., Lundberg,E., Odeberg,J., Ponten,F., Kondo,T. and
            Sivertsson,A.
  TITLE     Antibody-based protein profiling of the human chromosome 21
  JOURNAL   Mol Cell Proteomics 11 (3), M111.013458 (2012)
   PUBMED   22042635
REFERENCE   8  (residues 1 to 79)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 79)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 79)
  AUTHORS   Reymond,A., Friedli,M., Henrichsen,C.N., Chapot,F., Deutsch,S.,
            Ucla,C., Rossier,C., Lyle,R., Guipponi,M. and Antonarakis,S.E.
  TITLE     From PREDs and open reading frames to cDNA isolation: revisiting
            the human chromosome 21 transcription map
  JOURNAL   Genomics 78 (1-2), 46-54 (2001)
   PUBMED   11707072
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC384882.1, AY040876.1 and
            AP000471.2.
            
            Summary: This gene encodes a highly conserved metalloprotein. A
            similar protein in bacteria acts as an endoribonuclease, and is
            thought to function in ribosomal RNA maturation and ribosome
            assembly. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (5) differs in the 5' UTR, uses an
            alternate in-frame splice site, and lacks an alternate in-frame
            exon in the coding region, compared to variant 1. The encoded
            isoform (5) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY040876.1, BF510872.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..79
                     /product="endoribonuclease YbeY isoform 5"
                     /note="putative metalloprotease C21orf57; rRNA maturation
                     factor homolog; putative ribonuclease; endoribonuclease
                     YbeY; ybeY metallopeptidase (putative)"
                     /calculated_mol_wt=8805
     Region          <27..61
                     /region_name="PRK13963"
                     /note="rRNA maturation RNase YbeY; cl46897"
                     /db_xref="CDD:481237"
     CDS             1..79
                     /gene="YBEY"
                     /gene_synonym="C21orf57"
                     /coded_by="NM_001314024.2:119..358"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS82686.1"
                     /db_xref="GeneID:54059"
                     /db_xref="HGNC:HGNC:1299"
                     /db_xref="MIM:617461"
ORIGIN      
        1 mslvirnlqr vipirraplr skieivtath glchllgfth gteaewqqmf qkekavldel
       61 grrtgtrlqp ltrglfggs
//
LOCUS       NP_001369696             272 aa            linear   PRI 21-NOV-2025
DEFINITION  procathepsin L isoform 4 precursor [Homo sapiens].
ACCESSION   NP_001369696 XP_011516565
VERSION     NP_001369696.1
DBSOURCE    REFSEQ: accession NM_001382767.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Bestle,D., Bittel,L., Werner,A.D., Kamper,L., Dolnik,O.,
            Krahling,V., Steinmetzer,T. and Bottcher-Friebertshauser,E.
  TITLE     Novel proteolytic activation of Ebolavirus glycoprotein GP by
            TMPRSS2 and cathepsin L at an uncharted position can compensate for
            furin cleavage
  JOURNAL   Virus Res 347, 199430 (2024)
   PUBMED   38964470
  REMARK    GeneRIF: Novel proteolytic activation of Ebolavirus glycoprotein GP
            by TMPRSS2 and cathepsin L at an uncharted position can compensate
            for furin cleavage.
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Wu,Y., Jiang,D., Liu,Q., Yan,S., Liu,X., Wu,T., Sun,W. and Li,G.
  TITLE     Cathepsin L induces cellular senescence by upregulating CUX1 and
            p16INK4a
  JOURNAL   Aging (Albany NY) 16 (13), 10749-10764 (2024)
   PUBMED   38944813
  REMARK    GeneRIF: Cathepsin L induces cellular senescence by upregulating
            CUX1 and p16[INK4a].
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Xu,J., Xu,W., Choi,J., Brhane,Y., Christiani,D.C., Kothari,J.,
            McKay,J., Field,J.K., Davies,M.P.A., Liu,G., Amos,C.I., Hung,R.J.
            and Briollais,L.
  TITLE     Large-scale whole exome sequencing studies identify two genes,CTSL
            and APOE, associated with lung cancer
  JOURNAL   PLoS Genet 19 (9), e1010902 (2023)
   PUBMED   37738239
  REMARK    GeneRIF: Large-scale whole exome sequencing studies identify two
            genes,CTSL and APOE, associated with lung cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Liu,P., Ju,M., Zheng,X., Jiang,Y., Yu,X., Pan,B., Luo,R., Jia,W.
            and Zheng,M.
  TITLE     Methyltransferase-like 3 promotes cervical cancer metastasis by
            enhancing cathepsin L mRNA stability in an
            N6-methyladenosine-dependent manner
  JOURNAL   Cancer Sci 114 (3), 837-854 (2023)
   PUBMED   36382580
  REMARK    GeneRIF: Methyltransferase-like 3 promotes cervical cancer
            metastasis by enhancing cathepsin L mRNA stability in an
            N6-methyladenosine-dependent manner.
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Goretzki,L., Schmitt,M., Mann,K., Calvete,J., Chucholowski,N.,
            Kramer,M., Gunzler,W.A., Janicke,F. and Graeff,H.
  TITLE     Effective activation of the proenzyme form of the urokinase-type
            plasminogen activator (pro-uPA) by the cysteine protease cathepsin
            L
  JOURNAL   FEBS Lett 297 (1-2), 112-118 (1992)
   PUBMED   1551416
REFERENCE   7  (residues 1 to 272)
  AUTHORS   Cataldo,A.M., Paskevich,P.A., Kominami,E. and Nixon,R.A.
  TITLE     Lysosomal hydrolases of different classes are abnormally
            distributed in brains of patients with Alzheimer disease
  JOURNAL   Proc Natl Acad Sci U S A 88 (24), 10998-11002 (1991)
   PUBMED   1837142
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1992 Mar 15;89(6):2509]
REFERENCE   8  (residues 1 to 272)
  AUTHORS   Dunn,A.D., Crutchfield,H.E. and Dunn,J.T.
  TITLE     Thyroglobulin processing by thyroidal proteases. Major sites of
            cleavage by cathepsins B, D, and L
  JOURNAL   J Biol Chem 266 (30), 20198-20204 (1991)
   PUBMED   1939080
REFERENCE   9  (residues 1 to 272)
  AUTHORS   Stearns,N.A., Dong,J.M., Pan,J.X., Brenner,D.A. and Sahagian,G.G.
  TITLE     Comparison of cathepsin L synthesized by normal and transformed
            cells at the gene, message, protein, and oligosaccharide levels
  JOURNAL   Arch Biochem Biophys 283 (2), 447-457 (1990)
   PUBMED   2275556
REFERENCE   10 (residues 1 to 272)
  AUTHORS   Smith,C.G., Smith,M.T., Besch,N.F., Smith,R.G. and Asch,R.H.
  TITLE     Effect of delta 9-tetrahydrocannabinol (THC) on female reproductive
            function
  JOURNAL   Adv Biosci 22-23, 449-467 (1978)
   PUBMED   116880
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160279.21.
            
            On May 20, 2020 this sequence version replaced XP_011516565.1.
            
            Summary: The protein encoded by this gene is a lysosomal cysteine
            proteinase that plays a major role in intracellular protein
            catabolism. Its substrates include collagen and elastin, as well as
            alpha-1 protease inhibitor, a major controlling element of
            neutrophil elastase activity. The encoded protein has been
            implicated in several pathologic processes, including myofibril
            necrosis in myopathies and in myocardial ischemia, and in the renal
            tubular response to proteinuria. This protein, which is a member of
            the peptidase C1 family, is a dimer composed of disulfide-linked
            heavy and light chains, both produced from a single protein
            precursor. Additionally, this protein cleaves the S1 subunit of the
            SARS-CoV-2 spike protein, which is necessary for entry of the virus
            into the cell. [provided by RefSeq, Aug 2020].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.63778.1,
                                           SRR14038194.2647667.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in SARS-CoV-2 infection
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.33"
     Protein         1..272
                     /product="procathepsin L isoform 4 precursor"
                     /EC_number="3.4.22.15"
                     /note="major excreted protein; cathepsin L1; procathepsin
                     L"
                     /calculated_mol_wt=28906
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1706
     Region          29..87
                     /region_name="Inhibitor_I29"
                     /note="Cathepsin propeptide inhibitor domain (I29);
                     smart00848"
                     /db_xref="CDD:214853"
     Site            106..107
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:9468501; propagated from
                     UniProtKB/Swiss-Prot (P07711.2)"
     Site            107..108
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:9468501; propagated from
                     UniProtKB/Swiss-Prot (P07711.2)"
     Site            112..113
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:9468501; propagated from
                     UniProtKB/Swiss-Prot (P07711.2)"
     Site            113..114
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:9468501; propagated from
                     UniProtKB/Swiss-Prot (P07711.2)"
     Region          114..>260
                     /region_name="Peptidase_C1"
                     /note="Papain family cysteine protease; pfam00112"
                     /db_xref="CDD:425470"
     Site            221
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218;
                     propagated from UniProtKB/Swiss-Prot (P07711.2)"
     CDS             1..272
                     /gene="CTSL"
                     /gene_synonym="CATL; CTSL1; MEP"
                     /coded_by="NM_001382767.1:291..1109"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 9"
                     /db_xref="CCDS:CCDS94432.1"
                     /db_xref="GeneID:1514"
                     /db_xref="HGNC:HGNC:2537"
                     /db_xref="MIM:116880"
ORIGIN      
        1 mnptlilaaf clgiasatlt fdhsleaqwt kwkamhnrly gmneegwrra vweknmkmie
       61 lhnqeyregk hsftmamnaf gdmtseefrq vmngfqnrkp rkgkvfqepl fyeaprsvdw
      121 rekgyvtpvk nqgqcgscwa fsatgalegq mfrktgrlis lseqnlvdcs gpqgnegcng
      181 glmdyafqyv qdnggldsee sypyeatees ckynpkysva ndtgfvdipk qekalmkava
      241 tvgpisvaid aghesflfyk eagvkngawv at
//
LOCUS       NP_001369491             861 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 4 regulatory subunit 1 isoform
            c [Homo sapiens].
ACCESSION   NP_001369491 XP_016881595
VERSION     NP_001369491.1
DBSOURCE    REFSEQ: accession NM_001382562.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 861)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 861)
  AUTHORS   Xu,W., Hua,Z., Wang,Y., Tang,W., Ou,W., Liu,F., Yang,Y., Ding,W.,
            Wang,Z., Cui,L., Ge,W., Gu,Y., Wang,X., Chen,Y., Liu,C.Y. and Du,P.
  TITLE     AMBRA1 promotes intestinal inflammation by antagonizing PP4R1/PP4c
            mediated IKK dephosphorylation in an autophagy-independent manner
  JOURNAL   Cell Death Differ 31 (5), 618-634 (2024)
   PUBMED   38424148
  REMARK    GeneRIF: AMBRA1 promotes intestinal inflammation by antagonizing
            PP4R1/PP4c mediated IKK dephosphorylation in an
            autophagy-independent manner.
REFERENCE   3  (residues 1 to 861)
  AUTHORS   He,Z., Zhong,Y., Lv,T., Wang,J., Jin,Y., Li,F. and Hu,H.
  TITLE     PP4R1 promotes glycolysis and gallbladder cancer progression
            through facilitating ERK1/2 mediated PKM2 nuclear translocation
  JOURNAL   Cancer Lett 586, 216677 (2024)
   PUBMED   38301910
  REMARK    GeneRIF: PP4R1 promotes glycolysis and gallbladder cancer
            progression through facilitating ERK1/2 mediated PKM2 nuclear
            translocation.
REFERENCE   4  (residues 1 to 861)
  AUTHORS   Zhu,X., Chen,X., Shen,X., Liu,Y., Fu,W., Wang,B., Zhao,L., Yang,F.,
            Mo,N., Zhong,G., Jiang,S. and Yang,Z.
  TITLE     PP4R1 accelerates the malignant progression of NSCLC via
            up-regulating HSPA6 expression and HSPA6-mediated ER stress
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (1), 119588 (2024)
   PUBMED   37739270
  REMARK    GeneRIF: PP4R1 accelerates the malignant progression of NSCLC via
            up-regulating HSPA6 expression and HSPA6-mediated ER stress.
REFERENCE   5  (residues 1 to 861)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 861)
  AUTHORS   Toyo-oka,K., Mori,D., Yano,Y., Shiota,M., Iwao,H., Goto,H.,
            Inagaki,M., Hiraiwa,N., Muramatsu,M., Wynshaw-Boris,A., Yoshiki,A.
            and Hirotsune,S.
  TITLE     Protein phosphatase 4 catalytic subunit regulates Cdk1 activity and
            microtubule organization via NDEL1 dephosphorylation
  JOURNAL   J Cell Biol 180 (6), 1133-1147 (2008)
   PUBMED   18347064
REFERENCE   7  (residues 1 to 861)
  AUTHORS   Gingras,A.C., Caballero,M., Zarske,M., Sanchez,A., Hazbun,T.R.,
            Fields,S., Sonenberg,N., Hafen,E., Raught,B. and Aebersold,R.
  TITLE     A novel, evolutionarily conserved protein phosphatase complex
            involved in cisplatin sensitivity
  JOURNAL   Mol Cell Proteomics 4 (11), 1725-1740 (2005)
   PUBMED   16085932
REFERENCE   8  (residues 1 to 861)
  AUTHORS   Zhang,X., Ozawa,Y., Lee,H., Wen,Y.D., Tan,T.H., Wadzinski,B.E. and
            Seto,E.
  TITLE     Histone deacetylase 3 (HDAC3) activity is regulated by interaction
            with protein serine/threonine phosphatase 4
  JOURNAL   Genes Dev 19 (7), 827-839 (2005)
   PUBMED   15805470
REFERENCE   9  (residues 1 to 861)
  AUTHORS   Wada,T., Miyata,T., Inagi,R., Nangaku,M., Wagatsuma,M., Suzuki,D.,
            Wadzinski,B.E., Okubo,K. and Kurokawa,K.
  TITLE     Cloning and characterization of a novel subunit of protein
            serine/threonine phosphatase 4 from mesangial cells
  JOURNAL   J Am Soc Nephrol 12 (12), 2601-2608 (2001)
   PUBMED   11729228
REFERENCE   10 (residues 1 to 861)
  AUTHORS   Kloeker,S. and Wadzinski,B.E.
  TITLE     Purification and identification of a novel subunit of protein
            serine/threonine phosphatase 4
  JOURNAL   J Biol Chem 274 (9), 5339-5347 (1999)
   PUBMED   10026142
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000902.5 and AP001381.5.
            
            On May 14, 2020 this sequence version replaced XP_016881595.1.
            
            Summary: This gene encodes one of several alternate regulatory
            subunits of serine/threonine protein phosphatase 4 (PP4). The
            protein features multiple HEAT repeats. This protein forms a
            complex with PP4RC. This complex may have a distinct role from
            other PP4 complexes, including regulation of HDAC3 (Zhang et al.,
            PMID: 15805470). There is also a transcribed pseudogene on
            chromosome 20. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jun 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1935358.1,
                                           SRR14038193.4333771.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..861
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.22"
     Protein         1..861
                     /product="serine/threonine-protein phosphatase 4
                     regulatory subunit 1 isoform c"
                     /note="serine/threonine phosphatase 4;
                     serine/threonine-protein phosphatase 4 regulatory subunit
                     1"
                     /calculated_mol_wt=97024
     Region          44..68
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(60..61,64,67..68,102..103,106,109..110,113,142..143,
                     146,149..150,153,181..182,185,188..189,220..221,224,227)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          84..113
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          123..154
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          163..189
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          200..227
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          364..>382
                     /region_name="WRNPLPNID"
                     /note="Putative WW-binding domain and destruction box;
                     pfam15017"
                     /db_xref="CDD:464448"
     Site            order(554..555,558,561..562,592..593,596,599..600,603,
                     630..631,634,637..638,641,671..672,675,678..679,710..711,
                     714,717..718)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          575..603
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          613..642
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          651..679
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          690..719
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          774..800
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..861
                     /gene="PPP4R1"
                     /gene_synonym="MEG1; PP4(Rmeg); PP4R1"
                     /coded_by="NM_001382562.1:185..2770"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="GeneID:9989"
                     /db_xref="HGNC:HGNC:9320"
                     /db_xref="MIM:604908"
ORIGIN      
        1 mlqvrtylte ptvraelmeq vphialfcqe nrpsipyafs kfllpivvry ladqnnqvrk
       61 tsqaallall eqelierfdv etkvcpvlie ltapdsnddv kteavaimck mapmvgkdit
      121 erlilprfce mccdcrmfhv rkvcaanfgd icsvvgqqat eemllprffq lcsdnvwgvr
      181 kacaecfmav scatcqeirr tklsalfinl isdpsrwvrq aafqslgpfi stfanpsssg
      241 qyfkeeskss eemsvenknr trdqeapedv qvrpedtpsd lsvsnssvil entmedhaae
      301 asgkplgeis vpldssllct lsseshqeaa snendkkpgn yksmlrpevg ttsqdsalld
      361 qelynsfhfw rtplpeidld ieleqnsggk pspegpeees egpvpsspni tmatrkelee
      421 mienlephid dpdvkaqvev lsaalrassl daheetisie krsdlqdeld inelpnckin
      481 qedsvplisd avenmdstlh yihsdsdlsn nssfspdeer rtkvqdvvpq alldqylsmt
      541 dpsraqtvdt eiakhcaysl pgvaltlgrq nwhclretye tlasdmqwkv rrtlafsihe
      601 lavilgdqlt aadlvpifng flkdldevri gvlkhlhdfl kllhidkrre ylyqlqeflv
      661 tdnsrnwrfr aelaeqlill lelysprdvy dylrpialnl cadkvssvrw isyklvsemv
      721 kklhaatppt fgvdlinelv enfgrcpkws grqafvfvcq tvieddclpm dqfavhlmph
      781 lltlandrvp nvrvllaktl rqtllekdyf lasaschqea veqtimalqm drdsdvkyfa
      841 sihpastkis edamstasst y
//
LOCUS       NP_001381703             464 aa            linear   PRI 21-NOV-2025
DEFINITION  COP9 signalosome complex subunit 1 isoform 18 [Homo sapiens].
ACCESSION   NP_001381703
VERSION     NP_001381703.1
DBSOURCE    REFSEQ: accession NM_001394774.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Wei,H., Niu,Z., Ji,R., Jiang,W., Tang,J., Meng,Z., Cao,X., Zhang,X.
            and Liu,X.
  TITLE     Bioinformatics analysis of GPS1 expression and biological function
            in breast cancer
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 52 (2024)
   PUBMED   38289496
  REMARK    GeneRIF: Bioinformatics analysis of GPS1 expression and biological
            function in breast cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Fu,H., Zhang,Y., Chen,Y., Chen,J. and Chen,P.
  TITLE     CSN1 facilitates proliferation and migration of hepatocellular
            carcinoma cells by upregulating cyclin A2 expression
  JOURNAL   Mol Med Rep 23 (1) (2021)
   PUBMED   33200803
  REMARK    GeneRIF: CSN1 facilitates proliferation and migration of
            hepatocellular carcinoma cells by upregulating cyclin A2
            expression.
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Lyapina,S., Cope,G., Shevchenko,A., Serino,G., Tsuge,T., Zhou,C.,
            Wolf,D.A., Wei,N., Shevchenko,A. and Deshaies,R.J.
  TITLE     Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome
  JOURNAL   Science 292 (5520), 1382-1385 (2001)
   PUBMED   11337588
REFERENCE   7  (residues 1 to 464)
  AUTHORS   Bech-Otschir,D., Kraft,R., Huang,X., Henklein,P., Kapelari,B.,
            Pollmann,C. and Dubiel,W.
  TITLE     COP9 signalosome-specific phosphorylation targets p53 to
            degradation by the ubiquitin system
  JOURNAL   EMBO J 20 (7), 1630-1639 (2001)
   PUBMED   11285227
REFERENCE   8  (residues 1 to 464)
  AUTHORS   Tsuge,T., Matsui,M. and Wei,N.
  TITLE     The subunit 1 of the COP9 signalosome suppresses gene expression
            through its N-terminal domain and incorporates into the complex
            through the PCI domain
  JOURNAL   J Mol Biol 305 (1), 1-9 (2001)
   PUBMED   11114242
  REMARK    GeneRIF: The N-terminal half of CSN1/GPS1 is required to repress
            c-fos expression and to inhibit AP-1 and SRE transactivation, while
            the C-terminal half allows integration of the protein into the COP9
            signalosome.
REFERENCE   9  (residues 1 to 464)
  AUTHORS   Seeger,M., Kraft,R., Ferrell,K., Bech-Otschir,D., Dumdey,R.,
            Schade,R., Gordon,C., Naumann,M. and Dubiel,W.
  TITLE     A novel protein complex involved in signal transduction possessing
            similarities to 26S proteasome subunits
  JOURNAL   FASEB J 12 (6), 469-478 (1998)
   PUBMED   9535219
REFERENCE   10 (residues 1 to 464)
  AUTHORS   Spain,B.H., Bowdish,K.S., Pacal,A.R., Staub,S.F., Koo,D.,
            Chang,C.Y., Xie,W. and Colicelli,J.
  TITLE     Two human cDNAs, including a homolog of Arabidopsis FUS6 (COP11),
            suppress G-protein- and mitogen-activated protein kinase-mediated
            signal transduction in yeast and mammalian cells
  JOURNAL   Mol Cell Biol 16 (12), 6698-6706 (1996)
   PUBMED   8943324
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC135056.4.
            
            Summary: This gene is known to suppress G-protein and
            mitogen-activated signal transduction in mammalian cells. The
            encoded protein shares significant similarity with Arabidopsis
            FUS6, which is a regulator of light-mediated signal transduction in
            plant cells. [provided by RefSeq, Mar 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1691682.1,
                                           ERR4368410.312331.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2145122
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..464
                     /product="COP9 signalosome complex subunit 1 isoform 18"
                     /note="COP9 signalosome complex subunit 1; JAB1-containing
                     signalosome subunit 1"
                     /calculated_mol_wt=52182
     Region          127..309
                     /region_name="RPN7"
                     /note="26S proteasome subunit RPN7; pfam10602"
                     /db_xref="CDD:431387"
     Region          348..416
                     /region_name="PINT"
                     /note="motif in proteasome subunits, Int-6, Nip-1 and
                     TRIP-15; smart00088"
                     /db_xref="CDD:214509"
     CDS             1..464
                     /gene="GPS1"
                     /gene_synonym="COPS1; CSN1; SGN1"
                     /coded_by="NM_001394774.1:35..1429"
                     /note="isoform 18 is encoded by transcript variant 25"
                     /db_xref="GeneID:2873"
                     /db_xref="HGNC:HGNC:4549"
                     /db_xref="MIM:601934"
ORIGIN      
        1 mplpvqvfnl qgavepmqid vdpqedpqna pdvnyvvenp sldleqyaas ysglmrierl
       61 qfiadhcptl rvealkmals fvqrtfnvdm yeeihrklse atrsslrelq napdaipesg
      121 veppaldtaw veatrkkall klekldtdlk nykgnsikes irrghddlgd hyldcgdlsn
      181 alkcysrard yctsakhvin mclnvikvsv ylqnwshvls yvskaestpe iaeqrgerds
      241 qtqailtklk caaglaelaa rkykqaakcl llasfdhcdf pellspsnva iygglcalat
      301 fdrqelqrnv issssfklfl elepqvrdii fkfyeskyas clkmldemky fspyvsadmh
      361 rmaaafnttv aaledeltql ileglisarv dshskilyar dvdqrsttfe ksllmgkefq
      421 rrakammlra avlrnqihvk sppregsqge ltpansqsrm stnm
//
LOCUS       NP_001364079             451 aa            linear   PRI 21-NOV-2025
DEFINITION  gamma-aminobutyric acid receptor subunit alpha-2 isoform a
            precursor [Homo sapiens].
ACCESSION   NP_001364079 XP_024309738
VERSION     NP_001364079.1
DBSOURCE    REFSEQ: accession NM_001377150.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Zhou,J., Noviello,C.M., Teng,J., Moore,H., Lega,B. and Hibbs,R.E.
  TITLE     Resolving native GABAA receptor structures from the human brain
  JOURNAL   Nature 638 (8050), 562-568 (2025)
   PUBMED   39843743
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Chakraborty,A., Dey,S., Kumar,K., Dixit,A.B., Tripathi,M.,
            Sharma,M.C., Chandra,P.S. and Banerjee,J.
  TITLE     Novel variants in GABAA receptor subunits: A possible association
            with benzodiazepine resistance in patients with drug-resistant
            epilepsy
  JOURNAL   Epilepsy Res 189, 107056 (2023)
   PUBMED   36469977
  REMARK    GeneRIF: Novel variants in GABAA receptor subunits: A possible
            association with benzodiazepine resistance in patients with
            drug-resistant epilepsy.
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Preuss,U.W., Koller,G. and Zill,P.
  TITLE     Prospective DNA Methylation Analysis of the CpG GABRA2 Receptor
            Subunit in Alcohol Dependence during Detoxification
  JOURNAL   Medicina (Kaunas) 58 (11), 1653 (2022)
   PUBMED   36422192
  REMARK    GeneRIF: Prospective DNA Methylation Analysis of the CpG GABRA2
            Receptor Subunit in Alcohol Dependence during Detoxification.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Hawkins,N.A., Nomura,T., Duarte,S., Barse,L., Williams,R.W.,
            Homanics,G.E., Mulligan,M.K., Contractor,A. and Kearney,J.A.
  TITLE     Gabra2 is a genetic modifier of Dravet syndrome in mice
  JOURNAL   Mamm Genome 32 (5), 350-363 (2021)
   PUBMED   34086081
  REMARK    GeneRIF: Gabra2 is a genetic modifier of Dravet syndrome in mice.
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Bonnert,T.P., McKernan,R.M., Farrar,S., le Bourdelles,B.,
            Heavens,R.P., Smith,D.W., Hewson,L., Rigby,M.R.,
            Sirinathsinghji,D.J., Brown,N., Wafford,K.A. and Whiting,P.J.
  TITLE     theta, a novel gamma-aminobutyric acid type A receptor subunit
  JOURNAL   Proc Natl Acad Sci U S A 96 (17), 9891-9896 (1999)
   PUBMED   10449790
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Russek,S.J.
  TITLE     Evolution of GABA(A) receptor diversity in the human genome
  JOURNAL   Gene 227 (2), 213-222 (1999)
   PUBMED   10023064
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Davies,P.A., Hanna,M.C., Hales,T.G. and Kirkness,E.F.
  TITLE     Insensitivity to anaesthetic agents conferred by a class of GABA(A)
            receptor subunit
  JOURNAL   Nature 385 (6619), 820-823 (1997)
   PUBMED   9039914
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Togel,M., Mossier,B., Fuchs,K. and Sieghart,W.
  TITLE     gamma-Aminobutyric acidA receptors displaying association of gamma
            3-subunits with beta 2/3 and different alpha-subunits exhibit
            unique pharmacological properties
  JOURNAL   J Biol Chem 269 (17), 12993-12998 (1994)
   PUBMED   8175718
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Hadingham,K.L., Wingrove,P., Le Bourdelles,B., Palmer,K.J.,
            Ragan,C.I. and Whiting,P.J.
  TITLE     Cloning of cDNA sequences encoding human alpha 2 and alpha 3
            gamma-aminobutyric acidA receptor subunits and characterization of
            the benzodiazepine pharmacology of recombinant alpha 1-, alpha 2-,
            alpha 3-, and alpha 5-containing human gamma-aminobutyric acidA
            receptors
  JOURNAL   Mol Pharmacol 43 (6), 970-975 (1993)
   PUBMED   8391122
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC095060.3, AC093745.3 and
            AC104072.3.
            
            On Dec 17, 2019 this sequence version replaced XP_024309738.1.
            
            Summary: GABA is the major inhibitory neurotransmitter in the
            mammalian brain where it acts at GABA-A receptors, which are
            ligand-gated chloride channels. Chloride conductance of these
            channels can be modulated by agents such as benzodiazepines that
            bind to the GABA-A receptor. At least 16 distinct subunits of
            GABA-A receptors have been identified. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Nov 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.214976.1,
                                           SRR1803613.33370.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p12"
     Protein         1..451
                     /product="gamma-aminobutyric acid receptor subunit alpha-2
                     isoform a precursor"
                     /note="GABA(A) receptor subunit alpha-2;
                     gamma-aminobutyric acid type A receptor alpha2 subunit;
                     GABAAR subunit alpha-2"
                     /calculated_mol_wt=47959
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3385
     Region          25..440
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     mat_peptide     29..451
                     /product="Gamma-aminobutyric acid receptor subunit
                     alpha-2. /id=PRO_0000000433"
                     /note="propagated from UniProtKB/Swiss-Prot (P47869.2)"
                     /calculated_mol_wt=47959
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47869.2)"
     Region          47..249
                     /region_name="LGIC_ECD_GABAAR_A2"
                     /note="extracellular domain of gamma-aminobutyric acid
                     receptor subunit alpha-2 (GABAAR-A2 or GABRA2); cd19035"
                     /db_xref="CDD:349836"
     Site            order(64,92)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:349836"
     Site            order(76,78..79,84..85,92,94..95,112,114..115,124..129,
                     132,134,136..137,143..145,147,157..159,187,249)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349836"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47869.2)"
     Region          166..180
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349836"
     Site            250..270
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47869.2)"
     Site            281..300
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47869.2)"
     Site            312..332
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47869.2)"
     Site            421..441
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47869.2)"
     CDS             1..451
                     /gene="GABRA2"
                     /gene_synonym="DEE78; EIEE78"
                     /coded_by="NM_001377150.1:110..1465"
                     /note="isoform a precursor is encoded by transcript
                     variant 11"
                     /db_xref="CCDS:CCDS3471.1"
                     /db_xref="GeneID:2555"
                     /db_xref="HGNC:HGNC:4076"
                     /db_xref="MIM:137140"
ORIGIN      
        1 mktklniynm qfllfvflvw dparlvlani qedeaknnit iftrildrll dgydnrlrpg
       61 lgdsitevft niyvtsfgpv sdtdmeytid vffrqkwkde rlkfkgpmni lrlnnlmask
      121 iwtpdtffhn gkksvahnmt mpnkllriqd dgtllytmrl tvqaecpmhl edfpmdahsc
      181 plkfgsyayt tsevtyiwty nasdsvqvap dgsrlnqydl lgqsigketi ksstgeytvm
      241 tahfhlkrki gyfviqtylp cimtvilsqv sfwlnresvp artvfgvttv ltmttlsisa
      301 rnslpkvaya tamdwfiavc yafvfsalie fatvnyftkr gwawdgksvv ndkkkekasv
      361 miqnnayava vanyapnlsk dpvlstisks attpepnkkp enkpaeakkt fnsvskidrm
      421 srivfpvlfg tfnlvywaty lnrepvlgvs p
//
LOCUS       NP_001380831              65 aa            linear   PRI 21-NOV-2025
DEFINITION  26S proteasome complex subunit SEM1 isoform e [Homo sapiens].
ACCESSION   NP_001380831
VERSION     NP_001380831.1
DBSOURCE    REFSEQ: accession NM_001393902.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Huang,Y., Li,W., Foo,T., Ji,J.H., Wu,B., Tomimatsu,N., Fang,Q.,
            Gao,B., Long,M., Xu,J., Maqbool,R., Mukherjee,B., Ni,T., Alejo,S.,
            He,Y., Burma,S., Lan,L., Xia,B. and Zhao,W.
  TITLE     DSS1 restrains BRCA2's engagement with dsDNA for homologous
            recombination, replication fork protection, and R-loop homeostasis
  JOURNAL   Nat Commun 15 (1), 7081 (2024)
   PUBMED   39152168
  REMARK    GeneRIF: DSS1 restrains BRCA2's engagement with dsDNA for
            homologous recombination, replication fork protection, and R-loop
            homeostasis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Li,C., Chen,B., Zhang,J., Yang,J., Guo,M., Ren,Y., Zhou,Z.,
            Fung,K.M., Li,M., Zhang,L. and Liu,Z.
  TITLE     SEM1 promotes tumor progression of glioblastoma via activating the
            akt signaling pathway
  JOURNAL   Cancer Lett 577, 216368 (2023)
   PUBMED   37652287
  REMARK    GeneRIF: SEM1 promotes tumor progression of glioblastoma via
            activating the akt signaling pathway.
REFERENCE   3  (residues 1 to 65)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   4  (residues 1 to 65)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   5  (residues 1 to 65)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 65)
  AUTHORS   Marston,N.J., Richards,W.J., Hughes,D., Bertwistle,D.,
            Marshall,C.J. and Ashworth,A.
  TITLE     Interaction between the product of the breast cancer susceptibility
            gene BRCA2 and DSS1, a protein functionally conserved from yeast to
            mammals
  JOURNAL   Mol Cell Biol 19 (7), 4633-4642 (1999)
   PUBMED   10373512
REFERENCE   7  (residues 1 to 65)
  AUTHORS   Jantti,J., Lahdenranta,J., Olkkonen,V.M., Soderlund,H. and
            Keranen,S.
  TITLE     SEM1, a homologue of the split hand/split foot malformation
            candidate gene Dss1, regulates exocytosis and pseudohyphal
            differentiation in yeast
  JOURNAL   Proc Natl Acad Sci U S A 96 (3), 909-914 (1999)
   PUBMED   9927667
REFERENCE   8  (residues 1 to 65)
  AUTHORS   Crackower,M.A., Scherer,S.W., Rommens,J.M., Hui,C.C., Poorkaj,P.,
            Soder,S., Cobben,J.M., Hudgins,L., Evans,J.P. and Tsui,L.C.
  TITLE     Characterization of the split hand/split foot malformation locus
            SHFM1 at 7q21.3-q22.1 and analysis of a candidate gene for its
            expression during limb development
  JOURNAL   Hum Mol Genet 5 (5), 571-579 (1996)
   PUBMED   8733122
REFERENCE   9  (residues 1 to 65)
  AUTHORS   Roberts,S.H., Hughes,H.E., Davies,S.J. and Meredith,A.L.
  TITLE     Bilateral split hand and split foot malformation in a boy with a de
            novo interstitial deletion of 7q21.3
  JOURNAL   J Med Genet 28 (7), 479-481 (1991)
   PUBMED   1895319
REFERENCE   10 (residues 1 to 65)
  AUTHORS   Sharland,M., Patton,M.A. and Hill,L.
  TITLE     Ectrodactyly of hands and feet in a child with a complex
            translocation including 7q21.2
  JOURNAL   Am J Med Genet 39 (4), 413-414 (1991)
   PUBMED   1877619
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073230.8.
            
            Summary: The product of this gene has been localized within the
            split hand/split foot malformation locus SHFM1 at chromosome 7. It
            has been proposed to be a candidate gene for the autosomal dominant
            form of the heterogeneous limb developmental disorder split
            hand/split foot malformation type 1. In addition, it has been shown
            to directly interact with BRCA2. It also may play a role in the
            completion of the cell cycle. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279827.7313.1,
                                           SRR14243140.10840136.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.3"
     Protein         1..65
                     /product="26S proteasome complex subunit SEM1 isoform e"
                     /note="deleted in split-hand/split-foot 1; SEM1 26S
                     proteasome complex subunit; 26S proteasome complex subunit
                     DSS1; split hand/foot malformation (ectrodactyly) type 1;
                     split hand/foot deleted protein 1; deleted in split
                     hand/split foot protein 1; split hand/foot malformation
                     type 1 protein; 26S proteasome complex subunit SEM1"
                     /calculated_mol_wt=7521
     Region          <23..58
                     /region_name="DSS1_SEM1"
                     /note="DSS1/SEM1 family; pfam05160"
                     /db_xref="CDD:461563"
     CDS             1..65
                     /gene="SEM1"
                     /gene_synonym="C7orf76; DSS1; ECD; PSMD15; SHFD1; Shfdg1;
                     SHFM1; SHSF1"
                     /coded_by="NM_001393902.1:84..281"
                     /note="isoform e is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS94146.1"
                     /db_xref="GeneID:7979"
                     /db_xref="HGNC:HGNC:10845"
                     /db_xref="MIM:601285"
ORIGIN      
        1 msekkqpvdl glleeddefe efpaedwagl dededahvwe dnwdddnved dfsnqlragy
       61 selee
//
LOCUS       NP_001128649             571 aa            linear   PRI 21-NOV-2025
DEFINITION  protein NEDD1 isoform c [Homo sapiens].
ACCESSION   NP_001128649
VERSION     NP_001128649.1
DBSOURCE    REFSEQ: accession NM_001135177.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Timon Perez,K., Scrofani,J. and Vernos,I.
  TITLE     NEDD1-S411 phosphorylation plays a critical function in the
            coordination of microtubule nucleation during mitosis
  JOURNAL   Biol Open 11 (11) (2022)
   PUBMED   36318115
  REMARK    GeneRIF: NEDD1-S411 phosphorylation plays a critical function in
            the coordination of microtubule nucleation during mitosis.
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Chi,W., Wang,G., Xin,G., Jiang,Q. and Zhang,C.
  TITLE     PLK4-phosphorylated NEDD1 facilitates cartwheel assembly and
            centriole biogenesis initiations
  JOURNAL   J Cell Biol 220 (1) (2021)
   PUBMED   33351100
  REMARK    GeneRIF: PLK4-phosphorylated NEDD1 facilitates cartwheel assembly
            and centriole biogenesis initiations.
REFERENCE   4  (residues 1 to 571)
  AUTHORS   Courtheoux,T., Reboutier,D., Vazeille,T., Cremet,J.Y., Benaud,C.,
            Vernos,I. and Prigent,C.
  TITLE     Microtubule nucleation during central spindle assembly requires
            NEDD1 phosphorylation on serine 405 by Aurora A
  JOURNAL   J Cell Sci 132 (10) (2019)
   PUBMED   31028180
  REMARK    GeneRIF: Authors show here that the expression of a NEDD1 isoform
            mimicking phosphorylation by Aurora A is sufficient to restore
            microtubule nucleation in the midzone under conditions of Aurora A
            inhibition.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 571)
  AUTHORS   Fang,C.T., Kuo,H.H., Pan,T.S., Yu,F.C. and Yih,L.H.
  TITLE     HSP70 regulates the function of mitotic centrosomes
  JOURNAL   Cell Mol Life Sci 73 (20), 3949-3960 (2016)
   PUBMED   27137183
REFERENCE   6  (residues 1 to 571)
  AUTHORS   Haren,L. and Merdes,A.
  TITLE     Direct binding of NuMA to tubulin is mediated by a novel sequence
            motif in the tail domain that bundles and stabilizes microtubules
  JOURNAL   J Cell Sci 115 (Pt 9), 1815-1824 (2002)
   PUBMED   11956313
REFERENCE   7  (residues 1 to 571)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   8  (residues 1 to 571)
  AUTHORS   Hsu,H.L. and Yeh,N.H.
  TITLE     Dynamic changes of NuMA during the cell cycle and possible
            appearance of a truncated form of NuMA during apoptosis
  JOURNAL   J Cell Sci 109 (Pt 2), 277-288 (1996)
   PUBMED   8838651
REFERENCE   9  (residues 1 to 571)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   10 (residues 1 to 571)
  AUTHORS   Takai,S., Yoshida,Y., Noda,M., Yamada,K. and Kumar,S.
  TITLE     Assignment of the developmentally regulated gene NEDD1 to human
            chromosome 12q22 by fluorescence in situ hybridization
  JOURNAL   Hum Genet 95 (1), 96-98 (1995)
   PUBMED   7814034
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK303656.1, AK290058.1, AL832466.1, AA236927.1 and AC013417.4.
            
            Transcript Variant: This variant (4) differs in the 5' UTR and uses
            a downstream translation initiation codon, compared to variant 1,
            resulting in an isoform (c) that has a shorter N-terminus, compared
            to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303656.1, SRR1803615.173908.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.1"
     Protein         1..571
                     /product="protein NEDD1 isoform c"
                     /note="protein NEDD1; NEDD-1; neural precursor cell
                     expressed developmentally down-regulated protein 1;
                     tubulin gamma complex associated protein 7; neural
                     precursor cell expressed, developmentally down-regulated
                     1"
                     /calculated_mol_wt=62248
     Region          <2..210
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Region          34..71
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          76..113
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          121..157
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          162..199
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..571
                     /gene="NEDD1"
                     /gene_synonym="GCP-WD; TUBGCP7"
                     /coded_by="NM_001135177.2:334..2049"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS44956.1"
                     /db_xref="GeneID:121441"
                     /db_xref="HGNC:HGNC:7723"
                     /db_xref="MIM:600372"
ORIGIN      
        1 mylvsgglnn tvniwdlksk rvhrslkdhk dqvtcvtynw ndcyiasgsl sgeiilhsvt
       61 tnlsstpfgh gsnqsvrhlk yslfkksllg svsdngivtl wdvnsqspyh nfdsvhkapa
      121 sgicfspvne llfvtigldk riilydtssk klvktlvadt pltavdfmpd gatlaigssr
      181 gkiyqydlrm lkspvktisa hktsvqciaf qystvltkss lnkgcsnkpt tvnkrsvnvn
      241 aasggvqnsg ivreapatsi atvlpqpmts amgkgtvavq ekaglprsin tdtlsketds
      301 gknqdfssfd dtgksslgdm fspirddavv nkgsdesigk gdgfdflpql nsvfpprknp
      361 vtsstsvlhs splnvfmgsp gkeenenrdl taeskkiymg kqeskdsfkq laklvtsgae
      421 sgnlntspss nqtrnsekfe kpeneieaql iceppingss tpnpkiassv tagvasslse
      481 kiadsignnr qnapltsiqi rfiqnmiqet lddfreachr divnlqvemi kqfhmqlnem
      541 hsllerysvn eglvaeierl reenkrlrah f
//
LOCUS       NP_001338270             336 aa            linear   PRI 21-NOV-2025
DEFINITION  interleukin-1 receptor-associated kinase 4 isoform b [Homo
            sapiens].
ACCESSION   NP_001338270 XP_016874880
VERSION     NP_001338270.1
DBSOURCE    REFSEQ: accession NM_001351341.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Fisch,D., Zhang,T., Sun,H., Ma,W., Tan,Y., Gygi,S.P., Higgins,D.E.
            and Kagan,J.C.
  TITLE     Molecular definition of the endogenous Toll-like receptor
            signalling pathways
  JOURNAL   Nature 631 (8021), 635-644 (2024)
   PUBMED   38961291
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Liu,Y., Yuan,J., Zhang,Y., Qin,F., Bai,X., Sun,W., Chen,T., Liu,F.,
            Zheng,Y., Qi,X., Zhao,W., Liu,B. and Gao,C.
  TITLE     OTUD5 promotes the inflammatory immune response by enhancing MyD88
            oligomerization and Myddosome formation
  JOURNAL   Cell Death Differ 31 (6), 753-767 (2024)
   PUBMED   38605168
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Peterson,J., Balogh Sivars,K., Bianco,A. and Roper,K.
  TITLE     Toll-like receptor signalling via IRAK4 affects epithelial
            integrity and tightness through regulation of junctional tension
  JOURNAL   Development 150 (24) (2023)
   PUBMED   37997696
  REMARK    GeneRIF: Toll-like receptor signalling via IRAK4 affects epithelial
            integrity and tightness through regulation of junctional tension.
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Cooray,S., Price-Kuehne,F., Hong,Y., Omoyinmi,E., Burleigh,A.,
            Gilmour,K.C., Ahmad,B., Choi,S., Bahar,M.W., Torpiano,P.,
            Gagunashvili,A., Jensen,B., Bellos,E., Sancho-Shimizu,V.,
            Herberg,J.A., Mankad,K., Kumar,A., Kaliakatsos,M., Worth,A.J.J.,
            Eleftheriou,D., Whittaker,E. and Brogan,P.A.
  TITLE     Neuroinflammation, autoinflammation, splenomegaly and anemia caused
            by bi-allelic mutations in IRAK4
  JOURNAL   Front Immunol 14, 1231749 (2023)
   PUBMED   37744344
  REMARK    GeneRIF: Neuroinflammation, autoinflammation, splenomegaly and
            anemia caused by bi-allelic mutations in IRAK4.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Wang,Z., Liu,J., Sudom,A., Ayres,M., Li,S., Wesche,H., Powers,J.P.
            and Walker,N.P.
  TITLE     Crystal structures of IRAK-4 kinase in complex with inhibitors: a
            serine/threonine kinase with tyrosine as a gatekeeper
  JOURNAL   Structure 14 (12), 1835-1844 (2006)
   PUBMED   17161373
  REMARK    GeneRIF: crystallographic analysis of IRAK-4 kinase in complex with
            inhibitors
REFERENCE   6  (residues 1 to 336)
  AUTHORS   Suzuki,N. and Saito,T.
  TITLE     IRAK-4--a shared NF-kappaB activator in innate and acquired
            immunity
  JOURNAL   Trends Immunol 27 (12), 566-572 (2006)
   PUBMED   17046325
  REMARK    GeneRIF: Although each system seems to possess distinct activation
            mechanisms, interleukin-1 receptor-associated kinase (IRAK)-4 is
            essential for NF-kappaB activation in Toll-like receptor (TLR) and
            T-cell receptor (TCR) signaling pathways.
            Review article
REFERENCE   7  (residues 1 to 336)
  AUTHORS   Burns,K., Clatworthy,J., Martin,L., Martinon,F., Plumpton,C.,
            Maschera,B., Lewis,A., Ray,K., Tschopp,J. and Volpe,F.
  TITLE     Tollip, a new component of the IL-1RI pathway, links IRAK to the
            IL-1 receptor
  JOURNAL   Nat Cell Biol 2 (6), 346-351 (2000)
   PUBMED   10854325
REFERENCE   8  (residues 1 to 336)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   9  (residues 1 to 336)
  AUTHORS   Scherer,D.C., Brockman,J.A., Chen,Z., Maniatis,T. and Ballard,D.W.
  TITLE     Signal-induced degradation of I kappa B alpha requires
            site-specific ubiquitination
  JOURNAL   Proc Natl Acad Sci U S A 92 (24), 11259-11263 (1995)
   PUBMED   7479976
REFERENCE   10 (residues 1 to 336)
  AUTHORS   Siu,G., Strauss,E.C., Lai,E. and Hood,L.E.
  TITLE     Analysis of a human V beta gene subfamily
  JOURNAL   J Exp Med 164 (5), 1600-1614 (1986)
   PUBMED   3772297
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093012.9.
            
            On May 6, 2017 this sequence version replaced XP_016874880.1.
            
            Summary: This gene encodes a kinase that activates NF-kappaB in
            both the Toll-like receptor (TLR) and T-cell receptor (TCR)
            signaling pathways. The protein is essential for most innate immune
            responses. Mutations in this gene result in IRAK4 deficiency and
            recurrent invasive pneumococcal disease. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (9), as well as variants 3-8 and
            10, encodes isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.197389.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..336
                     /product="interleukin-1 receptor-associated kinase 4
                     isoform b"
                     /EC_number="2.7.11.1"
                     /note="renal carcinoma antigen NY-REN-64"
                     /calculated_mol_wt=37543
     Region          46..333
                     /region_name="STKc_IRAK4"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Interleukin-1 Receptor Associated Kinase 4; cd14158"
                     /db_xref="CDD:271060"
     Site            order(68..72,76,87,89,122,138..141,145,147,187,189,
                     191..192,194,205,208,226..229)
                     /site_type="active"
                     /db_xref="CDD:271060"
     Site            order(68..72,76,87,89,122,138..141,145,187,189,191..192,
                     194,205)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271060"
     Site            order(72,145,147,187,189,191,208,226..229)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271060"
     Site            order(204..216,218..229)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271060"
     CDS             1..336
                     /gene="IRAK4"
                     /gene_synonym="IMD67; IPD1; IRAK-4; NY-REN-64; REN64"
                     /coded_by="NM_001351341.2:699..1709"
                     /note="isoform b is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS44862.1"
                     /db_xref="GeneID:51135"
                     /db_xref="HGNC:HGNC:17967"
                     /db_xref="MIM:606883"
ORIGIN      
        1 mpfcdkdrtl mtpvqnleqs ymppdssspe nkslevsdtr fhsfsfyelk nvtnnfderp
       61 isvggnkmge ggfgvvykgy vnnttvavkk laamvditte elkqqfdqei kvmakcqhen
      121 lvellgfssd gddlclvyvy mpngslldrl scldgtppls whmrckiaqg aanginflhe
      181 nhhihrdiks anilldeaft akisdfglar asekfaqtvm tsrivgttay mapealrgei
      241 tpksdiysfg vvlleiitgl pavdehrepq llldikeeie deektiedyi dkkmndadst
      301 sveamysvas qclhekknkr pdikkvqqll qemtas
//
LOCUS       NP_001317342             950 aa            linear   PRI 21-NOV-2025
DEFINITION  BCAS3 microtubule associated cell migration factor isoform 4 [Homo
            sapiens].
ACCESSION   NP_001317342 XP_005257529
VERSION     NP_001317342.1
DBSOURCE    REFSEQ: accession NM_001330413.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 950)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 950)
  AUTHORS   Wang,Y., Li,Y., Sun,Q., Yuan,F., Xu,Y., Tong,S., Li,Y., Yi,S.,
            Yan,T., Chen,Q. and Liu,B.
  TITLE     BCAS3 accelerates glioblastoma tumorigenesis by restraining the
            P53/GADD45alpha signaling pathway
  JOURNAL   Exp Cell Res 417 (2), 113231 (2022)
   PUBMED   35659972
  REMARK    GeneRIF: BCAS3 accelerates glioblastoma tumorigenesis by
            restraining the P53/GADD45alpha signaling pathway.
REFERENCE   3  (residues 1 to 950)
  AUTHORS   Zhou,Z., Qiu,R., Liu,W., Yang,T., Li,G., Huang,W., Teng,X.,
            Yang,Y., Yu,H., Yang,Y. and Wang,Y.
  TITLE     BCAS3 exhibits oncogenic properties by promoting CRL4A-mediated
            ubiquitination of p53 in breast cancer
  JOURNAL   Cell Prolif 54 (8), e13088 (2021)
   PUBMED   34240781
  REMARK    GeneRIF: BCAS3 exhibits oncogenic properties by promoting
            CRL4A-mediated ubiquitination of p53 in breast cancer.
REFERENCE   4  (residues 1 to 950)
  AUTHORS   Hengel,H., Hannan,S.B., Dyack,S., MacKay,S.B., Schatz,U.,
            Fleger,M., Kurringer,A., Balousha,G., Ghanim,Z., Alkuraya,F.S.,
            Alzaidan,H., Alsaif,H.S., Mitani,T., Bozdogan,S., Pehlivan,D.,
            Lupski,J.R., Gleeson,J.J., Dehghani,M., Mehrjardi,M.Y.V.,
            Sherr,E.H., Parks,K.C., Argilli,E., Begtrup,A., Galehdari,H.,
            Balousha,O., Shariati,G., Mazaheri,N., Malamiri,R.A.,
            Pagnamenta,A.T., Kingston,H., Banka,S., Jackson,A., Osmond,M.,
            Riess,A., Haack,T.B., Nagele,T., Schuster,S., Hauser,S., Admard,J.,
            Casadei,N., Velic,A., Macek,B., Ossowski,S., Houlden,H.,
            Maroofian,R. and Schols,L.
  CONSRTM   Care4Rare Canada Consortium; Genomics England Research Consortium
  TITLE     Bi-allelic loss-of-function variants in BCAS3 cause a syndromic
            neurodevelopmental disorder
  JOURNAL   Am J Hum Genet 108 (6), 1069-1082 (2021)
   PUBMED   34022130
  REMARK    GeneRIF: Bi-allelic loss-of-function variants in BCAS3 cause a
            syndromic neurodevelopmental disorder.
REFERENCE   5  (residues 1 to 950)
  AUTHORS   Salamon,S., Bevc,S., Ekart,R., Hojs,R. and Potocnik,U.
  TITLE     Polymorphism in the GATM Locus Associated with Dialysis-Independent
            Chronic Kidney Disease but Not Dialysis-Dependent Kidney Failure
  JOURNAL   Genes (Basel) 12 (6), 834 (2021)
   PUBMED   34071541
  REMARK    GeneRIF: Polymorphism in the GATM Locus Associated with
            Dialysis-Independent Chronic Kidney Disease but Not
            Dialysis-Dependent Kidney Failure.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 950)
  AUTHORS   Siva,K., Venu,P., Mahadevan,A., S,K. S and Inamdar,M.S.
  TITLE     Human BCAS3 expression in embryonic stem cells and vascular
            precursors suggests a role in human embryogenesis and tumor
            angiogenesis
  JOURNAL   PLoS One 2 (11), e1202 (2007)
   PUBMED   18030336
  REMARK    GeneRIF: BCAS3 is mis-expressed in brain tumors and could serve as
            a human ES cell and tumor marker
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 950)
  AUTHORS   Gururaj,A.E., Peng,S., Vadlamudi,R.K. and Kumar,R.
  TITLE     Estrogen induces expression of BCAS3, a novel estrogen
            receptor-alpha coactivator, through proline-, glutamic acid-, and
            leucine-rich protein-1 (PELP1)
  JOURNAL   Mol Endocrinol 21 (8), 1847-1860 (2007)
   PUBMED   17505058
  REMARK    GeneRIF: Physically associated with histone H3 and histone
            acetyltransferase complex protein P/CAF (p300/CBP-associated
            factor) and possesses histone acetyltransferase activity.
            Erratum:[Mol Endocrinol. 2013 May;27(5):862]
REFERENCE   8  (residues 1 to 950)
  AUTHORS   Gururaj,A.E., Holm,C., Landberg,G. and Kumar,R.
  TITLE     Breast cancer-amplified sequence 3, a target of
            metastasis-associated protein 1, contributes to tamoxifen
            resistance in premenopausal patients with breast cancer
  JOURNAL   Cell Cycle 5 (13), 1407-1410 (2006)
   PUBMED   16855396
  REMARK    GeneRIF: BCAS3 overexpression in hormone receptor-positive
            premenopausal breast cancer seemed to be associated with impaired
            responses to tamoxifen
REFERENCE   9  (residues 1 to 950)
  AUTHORS   Gururaj,A.E., Singh,R.R., Rayala,S.K., Holm,C., den Hollander,P.,
            Zhang,H., Balasenthil,S., Talukder,A.H., Landberg,G. and Kumar,R.
  TITLE     MTA1, a transcriptional activator of breast cancer amplified
            sequence 3
  JOURNAL   Proc Natl Acad Sci U S A 103 (17), 6670-6675 (2006)
   PUBMED   16617102
  REMARK    GeneRIF: role for MTA1-BCAS3 pathway in promoting cancerous
            phenotypes in breast tumor cells
            Erratum:[Proc Natl Acad Sci U S A. 2013 Mar 5;110(10):4147-8]
REFERENCE   10 (residues 1 to 950)
  AUTHORS   Barlund,M., Monni,O., Weaver,J.D., Kauraniemi,P., Sauter,G.,
            Heiskanen,M., Kallioniemi,O.P. and Kallioniemi,A.
  TITLE     Cloning of BCAS3 (17q23) and BCAS4 (20q13) genes that undergo
            amplification, overexpression, and fusion in breast cancer
  JOURNAL   Genes Chromosomes Cancer 35 (4), 311-317 (2002)
   PUBMED   12378525
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC110602.8, AC079005.9, AC015876.10, AC005884.1 and AC005746.1.
            
            On Aug 29, 2016 this sequence version replaced XP_005257529.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2398873.1,
                                           SRR1660805.247959.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..950
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.2"
     Protein         1..950
                     /product="BCAS3 microtubule associated cell migration
                     factor isoform 4"
                     /note="breast carcinoma-amplified sequence 3; metastasis
                     associated antigen of breast cancer; BCAS4/BCAS3 fusion;
                     breast carcinoma amplified sequence 4/3 fusion protein;
                     protein Maab1; Rudhira; phagophore assembly factor 2"
                     /calculated_mol_wt=103532
     Region          581..753
                     /region_name="BCAS3"
                     /note="Breast carcinoma amplified sequence 3; pfam12490"
                     /db_xref="CDD:463605"
     CDS             1..950
                     /gene="BCAS3"
                     /gene_synonym="GAOB1; HEMARS; MAAB; PHAF2"
                     /coded_by="NM_001330413.2:70..2922"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS82176.1"
                     /db_xref="GeneID:54828"
                     /db_xref="HGNC:HGNC:14347"
                     /db_xref="MIM:607470"
ORIGIN      
        1 mneamatdsp rrpsrctggv vvrpqavteq symesvvtfl qdvvpqaysg tplteekeki
       61 vwvrfenadl ndtsrnlefh eihstgnepp llimigysdg mqvwsipisg eaqelfsvrh
      121 gpiraarilp apqfgaqkcd nfaekrpllg vcksigssgt sppyccvdly slrtgemvks
      181 iqfktpiydl hcnkrilvvv lqekiaafds ctftkkffvt scypcpgpnm npialgsrwl
      241 ayaenklirc hqsrggacgd niqsytatvi saaktlksgl tmvgkvvtql tgtlpsgvte
      301 ddvaihsnsr rsplvpgiit vidtetvgeg qvlvsedsds dgivahfpah ekpvccmafn
      361 tsgmllvttd tlghdfhvfq ilthpwsssq cavhhlytlh rgeteakvqd icfshdcrwv
      421 vvstlrgtsh vfpinpyggq pcvrthmspr vvnrmsrfqk sagleeieqe ltskqggrcs
      481 pvpglsssps gsplhgklns qdsynnftnn npgnprlspl pslmvvmpla qikqpmtlgt
      541 itkrtgpylf gagcfsikap ckvkpppqis psksmggefc vaaifgtsrs wfannaglkr
      601 ekdqskqvvv eslyiiscyg tlvehmmepr plstapkisd dtplemmtsp raswtlvrtp
      661 qwnelqppfn anhplllaad avqyyqflla glvppgspgp itrhgsydsl asdhsgqede
      721 ewlsqveivt htgphrrlwm gpqfqfktih psgqttviss sssvlqshgp sdtpqplldf
      781 dtddldlnsl riqpvrsdpv smpgssrpvs drrgvstvid aasgtfdrsv tllevcgswp
      841 egfglrhmss mehteeglre rladamaesp srdvvgsgtd taldvavktf pperhvavkc
      901 felqregsie tlsnssgsts gsiprnfdgy rsplptnesq plslfptgfp
//
LOCUS       NP_001287722             918 aa            linear   PRI 21-NOV-2025
DEFINITION  echinoderm microtubule-associated protein-like 3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001287722 XP_005273933 XP_005273934
VERSION     NP_001287722.1
DBSOURCE    REFSEQ: accession NM_001300793.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 918)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 918)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 918)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   4  (residues 1 to 918)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 918)
  AUTHORS   Luo,J., Yang,B., Xin,G., Sun,M., Zhang,B., Guo,X., Jiang,Q. and
            Zhang,C.
  TITLE     The microtubule-associated protein EML3 regulates mitotic spindle
            assembly by recruiting the Augmin complex to spindle microtubules
  JOURNAL   J Biol Chem 294 (14), 5643-5656 (2019)
   PUBMED   30723163
  REMARK    GeneRIF: results indicate that EML3 regulates mitotic spindle
            assembly and the kinetochore-MT connection by regulating MT-based
            MT nucleation and recruiting Augmin/gamma-TuRC to MTs.
REFERENCE   6  (residues 1 to 918)
  AUTHORS   Richards,M.W., O'Regan,L., Roth,D., Montgomery,J.M., Straube,A.,
            Fry,A.M. and Bayliss,R.
  TITLE     Microtubule association of EML proteins and the EML4-ALK variant 3
            oncoprotein require an N-terminal trimerization domain
  JOURNAL   Biochem J 467 (3), 529-536 (2015)
   PUBMED   25740311
REFERENCE   7  (residues 1 to 918)
  AUTHORS   Tegha-Dunghu,J., Neumann,B., Reber,S., Krause,R., Erfle,H.,
            Walter,T., Held,M., Rogers,P., Hupfeld,K., Ruppert,T., Ellenberg,J.
            and Gruss,O.J.
  TITLE     EML3 is a nuclear microtubule-binding protein required for the
            correct alignment of chromosomes in metaphase
  JOURNAL   J Cell Sci 121 (Pt 10), 1718-1726 (2008)
   PUBMED   18445686
  REMARK    GeneRIF: Functional analysis of EML3 demonstrates an important role
            for EML3 in correct metaphase chromosome alignment.
REFERENCE   8  (residues 1 to 918)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   9  (residues 1 to 918)
  AUTHORS   O'Connor,V., Houtman,S.H., De Zeeuw,C.I., Bliss,T.V. and
            French,P.J.
  TITLE     Eml5, a novel WD40 domain protein expressed in rat brain
  JOURNAL   Gene 336 (1), 127-137 (2004)
   PUBMED   15225882
REFERENCE   10 (residues 1 to 918)
  AUTHORS   Pozuelo Rubio,M., Geraghty,K.M., Wong,B.H., Wood,N.T.,
            Campbell,D.G., Morrice,N. and Mackintosh,C.
  TITLE     14-3-3-affinity purification of over 200 human phosphoproteins
            reveals new links to regulation of cellular metabolism,
            proliferation and trafficking
  JOURNAL   Biochem J 379 (Pt 2), 395-408 (2004)
   PUBMED   14744259
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001458.6, CN386216.1, AK093146.1 and BC050467.1.
            
            On Jul 12, 2014 this sequence version replaced XP_005273933.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853561.5108.1,
                                           SRR14038193.28540.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..918
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..918
                     /product="echinoderm microtubule-associated protein-like 3
                     isoform 1"
                     /note="EMAP-3; echinoderm microtubule associated protein
                     like 3"
                     /calculated_mol_wt=97944
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          6..>37
                     /region_name="TD_EMAP-like"
                     /note="trimerization domain of the echinoderm
                     microtubule-associated protein-like family; cl41737"
                     /db_xref="CDD:425368"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q32P44.1)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q32P44.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          218..286
                     /region_name="HELP"
                     /note="HELP motif; pfam03451"
                     /db_xref="CDD:460922"
     Region          235..287
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          296..345
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          309..356
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          312..758
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          351..393
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          364..403
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          399..435
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          409..449
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          449..488
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          464..513
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          505..544
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          518..556
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          550..585
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          562..596
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          590..627
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          630..668
                     /region_name="WD 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          634..678
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          675..710
                     /region_name="WD 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          684..724
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          717..756
                     /region_name="WD 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          730..756
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..918
                     /gene="EML3"
                     /gene_synonym="ELP95; EMAP3; EMAP95"
                     /coded_by="NM_001300793.2:319..3075"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:256364"
                     /db_xref="HGNC:HGNC:26666"
                     /db_xref="MIM:618118"
ORIGIN      
        1 mdgaagpgdg parealqsls qrlrvqeqem elvkaalaea lrllrlqvpp sslqgsgtpa
       61 ppgdsslaap pglpptctps lvsrgtqtet evelksspgp pglsngppap qgaseepsgt
      121 qsegggssss gagspgppgi lrplqppqra dtprrnssss sspserprqk lsrkaissan
      181 llvrsgstes rggkdplssp ggpgsrrsny nlegisvkmf lrgrpitmyi psgirsleel
      241 psgpppetls ldwvygyrgr dsrsnlfvlr sgevvyfiac vvvlyrpggg pggpggggqr
      301 hyrghtdcvr clavhpdgvr vasgqtagvd kdgkplqpvv hiwdsetllk lqeiglgafe
      361 rgvgalafsa adqgaflcvv ddsnehmlsv wdcsrgmkla eikstndsvl avgfnprdss
      421 civtsgkshv hfwnwsggvg vpgngtltrk qgvfgkykkp kfipcfvflp dgdiltgdse
      481 gniltwgrsp sdsktpgrgg aketygivaq ahahegsifa lclrrdgtvl sgggrdrrlv
      541 qwgpglvalq eaeipehfga vraiaeglgs ellvgttkna llrgdlaqgf spviqghtde
      601 lwglcthpsq nrfltcghdr qlclwdgesh alawsidlke tglcadfhps gavvavglnt
      661 grwlvldtet reivsdvidg neqlsvvrys pdglylaigs hdnviyiysv ssdgakssrf
      721 grcmghssfi thldwskdgn fimsnsgdye ilywdvaggc kqlknryesr drewatytcv
      781 lgfhvyvpvr scqgaephvr gprqprdqrp iharrlaprl agrqgrqhlp vasagrwgrg
      841 agarhalsnp lpvprllprr liaawrdrla rrrgpappcp slaqspttrg rlfpgltsrh
      901 srsriflega ngapahtv
//
LOCUS       NP_001333147            2685 aa            linear   PRI 21-NOV-2025
DEFINITION  protein unc-79 homolog isoform 1 [Homo sapiens].
ACCESSION   NP_001333147 XP_016877001
VERSION     NP_001333147.1
DBSOURCE    REFSEQ: accession NM_001346218.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2685)
  AUTHORS   Bayat,A., Liu,Z., Luo,S., Fenger,C.D., Hojte,A.F., Isidor,B.,
            Cogne,B., Larson,A., Zanus,C., Faletra,F., Keren,B., Musante,L.,
            Gourfinkel-An,I., Perrine,C., Demily,C., Lesca,G., Liao,W. and
            Ren,D.
  TITLE     A new neurodevelopmental disorder linked to heterozygous variants
            in UNC79
  JOURNAL   Genet Med 25 (9), 100894 (2023)
   PUBMED   37183800
  REMARK    GeneRIF: A new neurodevelopmental disorder linked to heterozygous
            variants in UNC79.
REFERENCE   2  (residues 1 to 2685)
  AUTHORS   Kschonsak,M., Chua,H.C., Weidling,C., Chakouri,N., Noland,C.L.,
            Schott,K., Chang,T., Tam,C., Patel,N., Arthur,C.P., Leitner,A.,
            Ben-Johny,M., Ciferri,C., Pless,S.A. and Payandeh,J.
  TITLE     Structural architecture of the human NALCN channelosome
  JOURNAL   Nature 603 (7899), 180-186 (2022)
   PUBMED   34929720
REFERENCE   3  (residues 1 to 2685)
  AUTHORS   Chua,H.C., Wulf,M., Weidling,C., Rasmussen,L.P. and Pless,S.A.
  TITLE     The NALCN channel complex is voltage sensitive and directly
            modulated by extracellular calcium
  JOURNAL   Sci Adv 6 (17), eaaz3154 (2020)
   PUBMED   32494638
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2685)
  AUTHORS   Bramswig,N.C., Bertoli-Avella,A.M., Albrecht,B., Al Aqeel,A.I.,
            Alhashem,A., Al-Sannaa,N., Bah,M., Brohl,K., Depienne,C.,
            Dorison,N., Doummar,D., Ehmke,N., Elbendary,H.M., Gorokhova,S.,
            Heron,D., Horn,D., James,K., Keren,B., Kuechler,A., Ismail,S.,
            Issa,M.Y., Marey,I., Mayer,M., McEvoy-Venneri,J., Megarbane,A.,
            Mignot,C., Mohamed,S., Nava,C., Philip,N., Ravix,C., Rolfs,A.,
            Sadek,A.A., Segebrecht,L., Stanley,V., Trautman,C., Valence,S.,
            Villard,L., Wieland,T., Engels,H., Strom,T.M., Zaki,M.S.,
            Gleeson,J.G., Ludecke,H.J., Bauer,P. and Wieczorek,D.
  TITLE     Genetic variants in components of the NALCN-UNC80-UNC79 ion channel
            complex cause a broad clinical phenotype (NALCN channelopathies)
  JOURNAL   Hum Genet 137 (9), 753-768 (2018)
   PUBMED   30167850
  REMARK    GeneRIF: UNC79 variant is associated with neurodevelopmental
            diseases.
REFERENCE   5  (residues 1 to 2685)
  AUTHORS   Shamseldin,H.E., Faqeih,E., Alasmari,A., Zaki,M.S., Gleeson,J.G.
            and Alkuraya,F.S.
  TITLE     Mutations in UNC80, Encoding Part of the UNC79-UNC80-NALCN Channel
            Complex, Cause Autosomal-Recessive Severe Infantile Encephalopathy
  JOURNAL   Am J Hum Genet 98 (1), 210-215 (2016)
   PUBMED   26708753
  REMARK    GeneRIF: UNC80 encodes a large protein that is necessary for the
            stability and function of NALCN and for bridging NALCN to UNC79 to
            form a functional complex
REFERENCE   6  (residues 1 to 2685)
  AUTHORS   Lu,B., Zhang,Q., Wang,H., Wang,Y., Nakayama,M. and Ren,D.
  TITLE     Extracellular calcium controls background current and neuronal
            excitability via an UNC79-UNC80-NALCN cation channel complex
  JOURNAL   Neuron 68 (3), 488-499 (2010)
   PUBMED   21040849
REFERENCE   7  (residues 1 to 2685)
  AUTHORS   Speca,D.J., Chihara,D., Ashique,A.M., Bowers,M.S.,
            Pierce-Shimomura,J.T., Lee,J., Rabbee,N., Speed,T.P., Gularte,R.J.,
            Chitwood,J., Medrano,J.F., Liao,M., Sonner,J.M., Eger,E.I. 2nd,
            Peterson,A.S. and McIntire,S.L.
  TITLE     Conserved role of unc-79 in ethanol responses in lightweight mutant
            mice
  JOURNAL   PLoS Genet 6 (8), e1001057 (2010)
   PUBMED   20714347
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 2685)
  AUTHORS   Lind,P.A., Macgregor,S., Vink,J.M., Pergadia,M.L., Hansell,N.K., de
            Moor,M.H., Smit,A.B., Hottenga,J.J., Richter,M.M., Heath,A.C.,
            Martin,N.G., Willemsen,G., de Geus,E.J., Vogelzangs,N.,
            Penninx,B.W., Whitfield,J.B., Montgomery,G.W., Boomsma,D.I. and
            Madden,P.A.
  TITLE     A genomewide association study of nicotine and alcohol dependence
            in Australian and Dutch populations
  JOURNAL   Twin Res Hum Genet 13 (1), 10-29 (2010)
   PUBMED   20158304
  REMARK    GeneRIF: In the Australian GWAS, one SNP achieved genomewide
            significance for comorbid AD/ND, rs12882384 in KIAA1409 on
            chromosome 14 (p = 4.86 x 10(-8))).
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL122023.3, AL136338.4 and
            AL157858.5.
            
            On Oct 1, 2016 this sequence version replaced XP_016877001.1.
            
            Summary: The NALCN channel is responsible for Na(+) leak currents.
            The protein encoded by this gene, along with UNC80, is an accessory
            subunit of the NALCN channel that contributes to the Ca(2+)
            sensitivity of the channel. [provided by RefSeq, Sep 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.281008.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2685
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.12"
     Protein         1..2685
                     /product="protein unc-79 homolog isoform 1"
                     /note="protein unc-79 homolog; unc-79 homolog, NALCN
                     channel complex subunit"
                     /calculated_mol_wt=300955
     Region          114..645
                     /region_name="UNC-79"
                     /note="Cation-channel complex subunit UNC-79; pfam14776"
                     /db_xref="CDD:434201"
     Site            754
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q0KK59; propagated from
                     UniProtKB/Swiss-Prot (Q9P2D8.4)"
     Site            758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q0KK59; propagated from
                     UniProtKB/Swiss-Prot (Q9P2D8.4)"
     Region          907..929
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2D8.4)"
     Region          1588..1625
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2D8.4)"
     Region          1657..1728
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2D8.4)"
     Region          1743..1882
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2D8.4)"
     Region          1913..1959
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2D8.4)"
     Region          1979..2000
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2D8.4)"
     Site            2273..2293
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2D8.4)"
     Site            2516..2536
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2D8.4)"
     CDS             1..2685
                     /gene="UNC79"
                     /gene_synonym="KIAA1409"
                     /coded_by="NM_001346218.2:92..8149"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS91921.1"
                     /db_xref="GeneID:57578"
                     /db_xref="HGNC:HGNC:19966"
                     /db_xref="MIM:616884"
ORIGIN      
        1 mstkaeqfas kirylqeyhn rvlhniypvp sgtdiantlk yfsqtllsil srtgkkenqd
       61 asnltvpmtm clfpvpfplt pslrpqvssi nptvtrslly svlrdapser gpqsrdaqls
      121 dypsldyqgl yvtlvtlldl vpllqhgqhd lgqsifyttt cllpflnddi lstlpytmis
      181 tlatfppflh kdiieylsts flpmailgss rregvpahvn lsassmlmia mqytsnpvyh
      241 cqlleclmky kqevwkdlly viaygpsqvk ppavqmlfhy wpnlkppgai seyrglqyta
      301 wnpihcqhie chnainkpav kmcidpslsv algdkppply lceecseria gdhsewlidv
      361 llpqaeisai cqkkncsshv rravvtcfsa gccgrhgnrp vryckrchsn hhsnevgaaa
      421 ethlyqtspp pintrecgae elvcaveavi sllkeaefha eqrehelnrr rqlglssshh
      481 sldnadfdnk dddkhdqrll sqfgiwflvs lctpsentpt eslarlvamv fqwfhstaym
      541 mddevgslve klkpqfvtkw lktvcdvrfd vmvmcllpkp mefarvggyw dkscstvtql
      601 keglnrilcl ipynvinqsv wecimpewle airtevpdnq lkefrevlsk mfdielcplp
      661 fsmeemfgfi scrftgypss vqeqallwlh vlseldimvp lqllismfsd gvnsvkelan
      721 qrksrvsela gnlasrrvsv asdpgrrvqh nmlspfhspf qspfrsplrs pfrspfknfg
      781 hpggrtidfd ceddemnlnc filmfdlllk qmelqddgit mglehslskd iisiinnvfq
      841 apwggshtcq kdekaiecnl cqssilcyql acellerlap keesrlvept dsledsllss
      901 rpefiigpeg eeeenpaskh genpgnctep vehaavkndt erkfcyqqlp vtlrliytif
      961 qemakfeepd ilfnmlnclk ilclhgecly iarkdhpqfl ayiqdhmlia slwrvvksef
     1021 sqlsslavpl llhalslphg adifwtiing nfnskdwkmr feavekvavi crfldihsvt
     1081 knhllkysla hafccfltav edvnpavatr agllldtikr palqglclcl dfqfdtvvkd
     1141 rptilsklll lhflkqdipa lsweffvnrf etlsleaqlh ldcnkefpfp ttitavrtnv
     1201 anlsdaalwk ikrarfarnr qksvrslrds vkgpveskra lslpetltsk irqqspendn
     1261 tikdllpeda gidhqtvhql itvlmkfmak dessaesdis sakafntvkr hlyvllgydq
     1321 qegcfmiapq kmrlstcfna fiagiaqvmd yninlgkhll plvvqvlkyc scpqlrhyfq
     1381 qpprcslwsl kphirqmwlk allvilykyp yrdcdiskil lhlihitvnt lnaqyhsckp
     1441 hatagplysd nsnisrysek ekeedsvfde sdihdtptgp cnkesqtffa rlkriggskm
     1501 vkyqpvemnv qrseielaey retgalqdsl lhcvreesip kkklrsfkqk sldignadsl
     1561 lftldehrrk scidrcdiek pptqaayiaq rpndpgrsrq nsatrpdnse ipenpamegf
     1621 pdarrpvipe vrlncmetfe vkvdspvkpa pkedldlidl ssdstsgpek hsilstsdsd
     1681 slvfeplppl rivesdeeee tmnqgddgps gknaasspsv pshpsvlsls taplvqvsve
     1741 dcskdfsskd sgnnqsagnt dsalitledp mdaegsskpe elpefscgsp ltlkqkrdll
     1801 qksfalpems lddhpdpgte gekpgelmps sgaktvllkv pedaenptes ekpdtsaesd
     1861 teqnperkve edgaeesefk iqivprqrkq rkiavsaiqr eyldisfnil dklgeqkdpd
     1921 pstkglstle mpresssapt ldagvpetss hssistqyrq mkrgslgvlt msqlmkrqle
     1981 hqssaphnis nwdteqiqpg krqcnvptcl npdlegqplr mrgatkssll sapsivsmfv
     2041 papeeftdeq ptvmtdkchd cgaileeyde etlglaivvl stfihlspdl aapllldimq
     2101 svgrlasstt fsnqaesmmv pgnaagvakq flrcifhqla pngifpqlfq stikdgtflr
     2161 tlasslmdfn elssiaalsq lleglnnkkn lpaggamirc leniatfmea lpmdspsslw
     2221 ttisnqfqtf faklpcvlpl kcsldsslri micllkipst natrsllepf skllsfviqn
     2281 avftlaylve lcglcyraft kerdkfylsr svvlellqal klksplpdtn llllvqfica
     2341 dagtklaest ilskqmiasv pgcgtaamec vrqyinevld fmadmhtltk lkshmktcsq
     2401 plhedtfggh lkvglaqiaa mdisrgnhrd nkavirylpw lyhppsamqq gpkefiecvs
     2461 hirllswlll gslthnavcp nasspclpip ldagshvadh liviligfpe qsktsvlhmc
     2521 slfhafifaq lwtvyceqsa vatnlqnqne fsftailtal efwsrvtpsi lqlmahnkvm
     2581 vemvclhvis lmealqecns tifvklipmw lpmiqsnikh lsaglqlrlq aiqnhvnhhs
     2641 lrtlpgsgqs saglaalrkw lqctqfkmaq veiqsseaas qfypl
//
LOCUS       NP_001371711            1114 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 41 [Homo sapiens].
ACCESSION   NP_001371711
VERSION     NP_001371711.1
DBSOURCE    REFSEQ: accession NM_001384782.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1114)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1114)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1114)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1114)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1114)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1114)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1114)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.496949.1,
                                           SRR14038196.1802205.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1114
                     /product="microtubule-associated protein 4 isoform 41"
                     /note="MAP-4"
                     /calculated_mol_wt=117132
     Region          <552..896
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          954..983
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          985..1014
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          1016..1046
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1114
                     /gene="MAP4"
                     /coded_by="NM_001384782.1:96..3440"
                     /note="isoform 41 is encoded by transcript variant 43"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiegsptef leekmayqey pnsqnwpedt nfcfqpeqvv dpiqtdpfkm
      121 yhdddladlv fpssatadts ifagqndplk dsygmspcnt avvpqgwsve alnsphsesf
      181 vspeavaepp qptavplela keiemaseer ppaqaleimm glkttdmaps ketemalakd
      241 malatkteva lakdmesptk ldvtlakdmq psmesdmalv kdmelpteke valvkdvrwp
      301 tetdvssakn vvlpteteva pakdvtllke teraspikmd lapskdmgpp kenkketera
      361 spikmdlaps kdmgppkenk ivpakdlvll seievaqand iissteissa ekvalssete
      421 valardmtlp petnviltkd kalpleaeva pvkdmaqlpe teiapakdva pstvkevgll
      481 kdmsplsete malgkdvtpp petevvlikn vclppemeva ltedqvpalk teaplakdgv
      541 ltlannvtpa kdvpplsete atpvpikdme iaqtqkgise dshleslqdv gqsaaptfmi
      601 spetvtgtgk kcslpaeeds vleklgerkp cnsqpselss etsgiarpee grpvvsgtgn
      661 dittppnkel ppspekktkp lattqpakts tskaktqpts lpkqpaptti gglnkkpmsl
      721 asglvpaapp krpavasarp silpskdvkp kpiadakape kraspskpas apasrsgsks
      781 tqtvakttta aavastgpss rspstllpkk ptaiktegkp aevkkmtaks vpadlsrpks
      841 tstssmkktt tlsgtapaag vvpsrvkatp mpsrpsttpf idkkptsakp ssttprlsrl
      901 atntsapdlk nvrskakvek kteaaattrk pesnavtkta gpiasaqkqp agkvqivskk
      961 vsyshiqskc gskdnikhvp gggnvqiqnk kvdiskvssk cgskanikhk pgggdvkies
     1021 qklnfkekaq akvgsldnvg hlpaggavkt egggseaplc pgppageepa iseaapeaga
     1081 ptsasglngh ptlsgggdqr eaqtldsqiq etsi
//
LOCUS       NP_001287724             118 aa            linear   PRI 21-NOV-2025
DEFINITION  ubiquitin-conjugating enzyme E2 D3 isoform 4 [Homo sapiens].
ACCESSION   NP_001287724 XP_006714364
VERSION     NP_001287724.1
DBSOURCE    REFSEQ: accession NM_001300795.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Yalcin,Z., Koot,D., Bezstarosti,K., Salas-Lloret,D.,
            Bleijerveld,O.B., Boersma,V., Falcone,M., Gonzalez-Prieto,R.,
            Altelaar,M., Demmers,J.A.A. and Jacobs,J.J.L.
  TITLE     Ubiquitinome Profiling Reveals in Vivo UBE2D3 Targets and
            Implicates UBE2D3 in Protein Quality Control
  JOURNAL   Mol Cell Proteomics 22 (6), 100548 (2023)
   PUBMED   37059365
  REMARK    GeneRIF: Ubiquitinome Profiling Reveals in Vivo UBE2D3 Targets and
            Implicates UBE2D3 in Protein Quality Control.
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Jiang,C., Dai,X., He,S., Zhou,H., Fang,L., Guo,J., Liu,S.,
            Zhang,T., Pan,W., Yu,H., Fu,T., Li,D., Inuzuka,H., Wang,P., Xiao,J.
            and Wei,W.
  TITLE     Ring domains are essential for GATOR2-dependent mTORC1 activation
  JOURNAL   Mol Cell 83 (1), 74-89 (2023)
   PUBMED   36528027
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Ray,P., Nancarrow,D.J., Ferrer-Torres,D., Wang,Z., San Martinho,M.,
            Hinton,T., Wu,J.H., Wu,A., Turgeon,D.K., Hammer,M.A., Dame,M.K.,
            Lawrence,T.S., O'Brien,P.J., Spence,J.R., Beer,D.G. and Ray,D.
  TITLE     UBCH5 Family Members Differentially Impact Stabilization of Mutant
            p53 via RNF128 Iso1 During Barrett's Progression to Esophageal
            Adenocarcinoma
  JOURNAL   Cell Mol Gastroenterol Hepatol 13 (1), 129-149 (2022)
   PUBMED   34416429
  REMARK    GeneRIF: UBCH5 Family Members Differentially Impact Stabilization
            of Mutant p53 via RNF128 Iso1 During Barrett's Progression to
            Esophageal Adenocarcinoma.
REFERENCE   5  (residues 1 to 118)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 118)
  AUTHORS   Ohta,T., Michel,J.J., Schottelius,A.J. and Xiong,Y.
  TITLE     ROC1, a homolog of APC11, represents a family of cullin partners
            with an associated ubiquitin ligase activity
  JOURNAL   Mol Cell 3 (4), 535-541 (1999)
   PUBMED   10230407
REFERENCE   7  (residues 1 to 118)
  AUTHORS   Anan,T., Nagata,Y., Koga,H., Honda,Y., Yabuki,N., Miyamoto,C.,
            Kuwano,A., Matsuda,I., Endo,F., Saya,H. and Nakao,M.
  TITLE     Human ubiquitin-protein ligase Nedd4: expression, subcellular
            localization and selective interaction with ubiquitin-conjugating
            enzymes
  JOURNAL   Genes Cells 3 (11), 751-763 (1998)
   PUBMED   9990509
REFERENCE   8  (residues 1 to 118)
  AUTHORS   Rogakou,E.P., Pilch,D.R., Orr,A.H., Ivanova,V.S. and Bonner,W.M.
  TITLE     DNA double-stranded breaks induce histone H2AX phosphorylation on
            serine 139
  JOURNAL   J Biol Chem 273 (10), 5858-5868 (1998)
   PUBMED   9488723
REFERENCE   9  (residues 1 to 118)
  AUTHORS   Jensen,J.P., Bates,P.W., Yang,M., Vierstra,R.D. and Weissman,A.M.
  TITLE     Identification of a family of closely related human ubiquitin
            conjugating enzymes
  JOURNAL   J Biol Chem 270 (51), 30408-30414 (1995)
   PUBMED   8530467
REFERENCE   10 (residues 1 to 118)
  AUTHORS   Scheffner,M., Huibregtse,J.M. and Howley,P.M.
  TITLE     Identification of a human ubiquitin-conjugating enzyme that
            mediates the E6-AP-dependent ubiquitination of p53
  JOURNAL   Proc Natl Acad Sci U S A 91 (19), 8797-8801 (1994)
   PUBMED   8090726
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018797.4, DB234695.1,
            DA550074.1, AK127304.1, AI651378.1, CD242548.1, BQ719030.1 and
            BU677139.1.
            
            On Jul 12, 2014 this sequence version replaced XP_006714364.1.
            
            Summary: The modification of proteins with ubiquitin is an
            important cellular mechanism for targeting abnormal or short-lived
            proteins for degradation. Ubiquitination involves at least three
            classes of enzymes: ubiquitin-activating enzymes, or E1s,
            ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein
            ligases, or E3s. This gene encodes a member of the E2
            ubiquitin-conjugating enzyme family. This enzyme functions in the
            ubiquitination of the tumor-suppressor protein p53, which is
            induced by an E3 ubiquitin-protein ligase. [provided by RefSeq, Jan
            2017].
            
            Transcript Variant: This variant (10) differs in its 5' UTR and
            uses a downstream start codon, compared to variant 1. The encoded
            isoform (4) has a shorter N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1292646.1,
                                           SRR1660809.254929.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..118
                     /product="ubiquitin-conjugating enzyme E2 D3 isoform 4"
                     /EC_number="2.3.2.23"
                     /EC_number="2.3.2.24"
                     /note="ubiquitin-conjugating enzyme E2D 3 (UBC4/5 homolog,
                     yeast); ubiquitin-conjugating enzyme E2-17 kDa 3;
                     ubiquitin-protein ligase D3; ubiquitin carrier protein D3;
                     ubiquitin-conjugating enzyme E2(17)KB 3; ubiquitin
                     conjugating enzyme E2D 3; E2 ubiquitin-conjugating enzyme
                     D3; (E3-independent) E2 ubiquitin-conjugating enzyme D3;
                     ubiquitin-conjugating enzyme E2D 3 (homologous to yeast
                     UBC4/5)"
                     /calculated_mol_wt=13506
     Region          1..116
                     /region_name="UBCc_UEV"
                     /note="Ubiquitin-conjugating enzyme E2, catalytic (UBCc)
                     domain/ubiquitin E2 variant (UEV) domain; cl49610"
                     /db_xref="CDD:483950"
     CDS             1..118
                     /gene="UBE2D3"
                     /gene_synonym="E2(17)KB3; UBC4/5; UBCH5C"
                     /coded_by="NM_001300795.2:268..624"
                     /note="isoform 4 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS75172.1"
                     /db_xref="GeneID:7323"
                     /db_xref="HGNC:HGNC:12476"
                     /db_xref="MIM:602963"
ORIGIN      
        1 mfhwqatimg pndspyqggv ffltihfptd ypfkppkvaf ttriyhpnin sngsicldil
       61 rsqwspalti skvllsicsl lcdpnpddpl vpeiariykt drdkynrisr ewtqkyam
//
LOCUS       NP_002910                707 aa            linear   PRI 21-NOV-2025
DEFINITION  transcription factor RFX3 isoform a [Homo sapiens].
ACCESSION   NP_002910
VERSION     NP_002910.1
DBSOURCE    REFSEQ: accession NM_002919.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Qian,Y., Cheng,B., Luo,J., Hu,Y., Gao,L. and Cheng,H.
  TITLE     CircRFX3 Up-regulates Its Host Gene RFX3 to Facilitate
            Tumorigenesis and Progression of Glioma
  JOURNAL   J Mol Neurosci 72 (6), 1195-1207 (2022)
   PUBMED   35416616
  REMARK    GeneRIF: CircRFX3 Up-regulates Its Host Gene RFX3 to Facilitate
            Tumorigenesis and Progression of Glioma.
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 707)
  AUTHORS   Nakayama,A., Murakami,H., Maeyama,N., Yamashiro,N., Sakakibara,A.,
            Mori,N. and Takahashi,M.
  TITLE     Role for RFX transcription factors in non-neuronal cell-specific
            inactivation of the microtubule-associated protein MAP1A promoter
  JOURNAL   J Biol Chem 278 (1), 233-240 (2003)
   PUBMED   12411430
  REMARK    GeneRIF: Data show that two regulatory factor for X box (RFX1 and
            3) binding sites in exon1 of both the mouse and human
            microtubule-associated protein (MAP1A) gene are important for
            effective transcriptional repression in non-neuronal cells.
REFERENCE   7  (residues 1 to 707)
  AUTHORS   Morotomi-Yano,K., Yano,K., Saito,H., Sun,Z., Iwama,A. and Miki,Y.
  TITLE     Human regulatory factor X 4 (RFX4) is a testis-specific dimeric
            DNA-binding protein that cooperates with other human RFX members
  JOURNAL   J Biol Chem 277 (1), 836-842 (2002)
   PUBMED   11682486
REFERENCE   8  (residues 1 to 707)
  AUTHORS   Iwama,A., Pan,J., Zhang,P., Reith,W., Mach,B., Tenen,D.G. and
            Sun,Z.
  TITLE     Dimeric RFX proteins contribute to the activity and lineage
            specificity of the interleukin-5 receptor alpha promoter through
            activation and repression domains
  JOURNAL   Mol Cell Biol 19 (6), 3940-3950 (1999)
   PUBMED   10330134
REFERENCE   9  (residues 1 to 707)
  AUTHORS   Emery,P., Durand,B., Mach,B. and Reith,W.
  TITLE     RFX proteins, a novel family of DNA binding proteins conserved in
            the eukaryotic kingdom
  JOURNAL   Nucleic Acids Res 24 (5), 803-807 (1996)
   PUBMED   8600444
REFERENCE   10 (residues 1 to 707)
  AUTHORS   Reith,W., Ucla,C., Barras,E., Gaud,A., Durand,B.,
            Herrero-Sanchez,C., Kobr,M. and Mach,B.
  TITLE     RFX1, a transactivator of hepatitis B virus enhancer I, belongs to
            a novel family of homodimeric and heterodimeric DNA-binding
            proteins
  JOURNAL   Mol Cell Biol 14 (2), 1230-1244 (1994)
   PUBMED   8289803
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL365202.19, AL354941.10 and
            AL133549.11.
            
            Summary: This gene is a member of the regulatory factor X gene
            family, which encodes transcription factors that contain a
            highly-conserved winged helix DNA binding domain. The protein
            encoded by this gene is structurally related to regulatory factors
            X1, X2, X4, and X5. It is a transcriptional activator that can bind
            DNA as a monomer or as a heterodimer with other RFX family members.
            Multiple transcript variants encoding different isoforms have been
            described for this gene. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.197058.1,
                                           SRR1803613.108933.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.2"
     Protein         1..707
                     /product="transcription factor RFX3 isoform a"
                     /note="DNA binding protein RFX3; transcription factor
                     RFX3; regulatory factor X, 3 (influences HLA class II
                     expression)"
                     /calculated_mol_wt=79226
     Region          <51..138
                     /region_name="RFX1_trans_act"
                     /note="RFX1 transcription activation region; pfam04589"
                     /db_xref="CDD:461362"
     Region          184..258
                     /region_name="RFX_DNA_binding"
                     /note="RFX DNA-binding domain; pfam02257"
                     /db_xref="CDD:460512"
     CDS             1..707
                     /gene="RFX3"
                     /coded_by="NM_002919.4:264..2387"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6450.1"
                     /db_xref="GeneID:5991"
                     /db_xref="HGNC:HGNC:9984"
                     /db_xref="MIM:601337"
ORIGIN      
        1 mqtsetgsdt gstvtlqtsv asqaavptqv vqqvpvqqqv qqvqtvqqvq hvypaqvqyv
       61 egsdtvytng airtttypyt etqmysqntg gnyfdtqgss aqvttvvssh smvgtggiqm
      121 gvtggqliss sggtyligns mensghsvth ttraspatie maietlqksd glsthrssll
      181 nshlqwlldn yetaegvslp rstlynhylr hcqehkldpv naasfgklir sifmglrtrr
      241 lgtrgnskyh yygirvkpds plnrlqedmq ymamrqqpmq qkqrykpmqk vdgvadgftg
      301 sgqqtgtsve qtviaqsqhh qqfldasral pefgeveiss lpdgttfedi kslqslyreh
      361 ceaildvvvn lqfslieklw qtfwryspst ptdgttites snlseiesrl pkaklitlck
      421 hesilkwmcn cdhgmyqalv eilipdvlrp ipsaltqair nfakslegwl snamnnipqr
      481 miqtkvaavs afaqtlrryt slnhlaqaar avlqntsqin qmlsdlnrvd fanvqeqasw
      541 vcqcddnmvq rletdfkmtl qqqstleqwa awldnvmmqa lkpyegrpsf pkaarqfllk
      601 wsfyssmvir dltlrsaasf gsfhlirlly deymfylveh rvaqatgetp iavmgevrea
      661 eravthwvik nkpelhfsln tlliktmvpn qvslrarrdc gviarvp
//
LOCUS       NP_001340979             705 aa            linear   PRI 21-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 7 isoform k [Homo sapiens].
ACCESSION   NP_001340979
VERSION     NP_001340979.1
DBSOURCE    REFSEQ: accession NM_001354050.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 705)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 705)
  AUTHORS   Kawase,N., Sugihara,A., Kajiwara,K., Hiroshima,M., Akamatsu,K.,
            Nada,S., Matsumoto,K., Ueda,M. and Okada,M.
  TITLE     SRC kinase activator CDCP1 promotes hepatocyte growth
            factor-induced cell migration/invasion of a subset of breast cancer
            cells
  JOURNAL   J Biol Chem 298 (3), 101630 (2022)
   PUBMED   35085554
  REMARK    GeneRIF: SRC kinase activator CDCP1 promotes hepatocyte growth
            factor-induced cell migration/invasion of a subset of breast cancer
            cells.
REFERENCE   4  (residues 1 to 705)
  AUTHORS   Keum,S., Yang,S.J., Park,E., Kang,T., Choi,J.H., Jeong,J.,
            Hwang,Y.E., Kim,J.W., Park,D. and Rhee,S.
  TITLE     Beta-Pix-dynamin 2 complex promotes colorectal cancer progression
            by facilitating membrane dynamics
  JOURNAL   Cell Oncol (Dordr) 44 (6), 1287-1305 (2021)
   PUBMED   34582006
  REMARK    GeneRIF: Beta-Pix-dynamin 2 complex promotes colorectal cancer
            progression by facilitating membrane dynamics.
REFERENCE   5  (residues 1 to 705)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 705)
  AUTHORS   Turner,C.E., Brown,M.C., Perrotta,J.A., Riedy,M.C.,
            Nikolopoulos,S.N., McDonald,A.R., Bagrodia,S., Thomas,S. and
            Leventhal,P.S.
  TITLE     Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin
            repeat, ARF-GAP protein: A role in cytoskeletal remodeling
  JOURNAL   J Cell Biol 145 (4), 851-863 (1999)
   PUBMED   10330411
REFERENCE   7  (residues 1 to 705)
  AUTHORS   Aghazadeh,B., Zhu,K., Kubiseski,T.J., Liu,G.A., Pawson,T., Zheng,Y.
            and Rosen,M.K.
  TITLE     Structure and mutagenesis of the Dbl homology domain
  JOURNAL   Nat Struct Biol 5 (12), 1098-1107 (1998)
   PUBMED   9846881
REFERENCE   8  (residues 1 to 705)
  AUTHORS   Bagrodia,S., Taylor,S.J., Jordon,K.A., Van Aelst,L. and
            Cerione,R.A.
  TITLE     A novel regulator of p21-activated kinases
  JOURNAL   J Biol Chem 273 (37), 23633-23636 (1998)
   PUBMED   9726964
REFERENCE   9  (residues 1 to 705)
  AUTHORS   Manser,E., Loo,T.H., Koh,C.G., Zhao,Z.S., Chen,X.Q., Tan,L.,
            Tan,I., Leung,T. and Lim,L.
  TITLE     PAK kinases are directly coupled to the PIX family of nucleotide
            exchange factors
  JOURNAL   Mol Cell 1 (2), 183-192 (1998)
   PUBMED   9659915
REFERENCE   10 (residues 1 to 705)
  AUTHORS   Oh,W.K., Yoo,J.C., Jo,D., Song,Y.H., Kim,M.G. and Park,D.
  TITLE     Cloning of a SH3 domain-containing proline-rich protein, p85SPR,
            and its localization in focal adhesion
  JOURNAL   Biochem Biophys Res Commun 235 (3), 794-798 (1997)
   PUBMED   9207241
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL353704.10, AL390754.18 and
            AL139086.12.
            
            Summary: This gene encodes a protein that belongs to a family of
            cytoplasmic proteins that activate the Ras-like family of Rho
            proteins by exchanging bound GDP for GTP. It forms a complex with
            the small GTP binding protein Rac1 and recruits Rac1 to membrane
            ruffles and to focal adhesions. Multiple alternatively spliced
            transcript variants encoding different isoforms have been observed
            for this gene. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (16), as well as variants 14, 15,
            and 17, encodes isoform k.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.117757.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..705
                     /product="rho guanine nucleotide exchange factor 7 isoform
                     k"
                     /note="SH3 domain-containing proline-rich protein;
                     PAK-interacting exchange factor beta; Rho guanine
                     nucleotide exchange factor (GEF) 7"
                     /calculated_mol_wt=79702
     Region          10..63
                     /region_name="SH3_betaPIX"
                     /note="Src Homology 3 domain of beta-Pak Interactive
                     eXchange factor; cd12061"
                     /db_xref="CDD:212994"
     Site            order(15,17,20,23..24,39,41..43,54,56,58..59)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212994"
     Region          94..271
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(100,104,198,222..223,226..227,229..230,233..234,
                     237..238,241,267,271)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          302..400
                     /region_name="PH_Cool_Pix"
                     /note="Cloned out of library/PAK-interactive exchange
                     factor pleckstrin homology (PH) domain; cd01225"
                     /db_xref="CDD:269932"
     Region          460..550
                     /region_name="RhoGEF67_u2"
                     /note="Unstructured region two on RhoGEF 6 and 7;
                     pfam16614"
                     /db_xref="CDD:465200"
     Region          620..704
                     /region_name="betaPIX_CC"
                     /note="betaPIX coiled coil; pfam16523"
                     /db_xref="CDD:465158"
     CDS             1..705
                     /gene="ARHGEF7"
                     /gene_synonym="BETA-PIX; COOL-1; COOL1; Nbla10314; P50;
                     P50BP; P85; P85COOL1; P85SPR; PAK3; PIXB"
                     /coded_by="NM_001354050.2:278..2395"
                     /note="isoform k is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS86361.1"
                     /db_xref="GeneID:8874"
                     /db_xref="HGNC:HGNC:15607"
                     /db_xref="MIM:605477"
ORIGIN      
        1 mtdnsnnqlv vrakfnfqqt nedelsfskg dvihvtrvee ggwwegtlng rtgwfpsnyv
       61 revkasekpv spksgtlksp pkgfdttain ksyynvvlqn ileteneysk elqtvlstyl
      121 rplqtsekls sanisylmgn leeicsfqqm lvqsleectk lpeaqqrvgg cflnlmpqmk
      181 tlyltycanh psavnvlteh seelgefmet kgasspgilv lttglskpfm rldkyptllk
      241 elerhmedyh tdrqdiqksm aafknlsaqc qevrkrkele lqilteairn wegddiktlg
      301 nvtymsqvli qcagseekne rylllfpnvl lmlsasprms gfiyqgklpt tgmtitkled
      361 senhrnafei sgsmierilv scnnqqdlqe wvehlqkqtk vtsvgnptik phsvpshtlp
      421 shpvtpsskh adskpapltp ayhtlphpsh hgtphttinw gpleppktpk pwslsclrpa
      481 pplrpsaalc ykedlskspk tmkkllpkrk perkpsdeef asrkstaale edaqilkvie
      541 ayctsaktrq tlnstwqgtd lmhnhvladd dqpsldslgr rsslsrleps dlsedsdyds
      601 iwtahsyrmg stsrsrkesa pqvllpeeek iiveetksng qtvieekslv dtvyalkdev
      661 qelrqdnkkm kksleeeqra rkdleklvrk vlknmndpaw detnl
//
LOCUS       NP_001371790             996 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 115 [Homo sapiens].
ACCESSION   NP_001371790
VERSION     NP_001371790.1
DBSOURCE    REFSEQ: accession NM_001384861.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 996)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 996)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 996)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 996)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 996)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 996)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 996)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..996
                     /product="microtubule-associated protein 4 isoform 115"
                     /note="MAP-4"
                     /calculated_mol_wt=104942
     Region          <665..980
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          867..896
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          898..928
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..996
                     /gene="MAP4"
                     /coded_by="NM_001384861.1:96..3086"
                     /note="isoform 115 is encoded by transcript variant 108"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgsp tefleekmay qeypnsqnwp
      121 edtnfcfqpe qvvdpiqtdp fkmyhdddla dlvfpssata dtsifagqnd plkdsygmsp
      181 cntavvpqgw svealnsphs esfvspeava eppqptavpl elakeiemas eerppaqale
      241 immglkttdm apsketemal akdmalatkt evalakdmes ptkldvtlak dmqpsmesdm
      301 alvkdmelpt ekevalvkdv rwptetdvss aknvvlptet evapakdvtl lketeraspi
      361 kmdlapskdm gppkenkket eraspikmdl apskdmgppk enkivpakdl vllseievaq
      421 andiisstei ssaekvalss etevalardm tlppetnvil tkdkalplea evapvkdmaq
      481 lpeteiapak dvapstvkev gllkdmspls etemalgkdv tpppetevvl iknvclppem
      541 evaltedqvp alkteaplak dgvltlannv tpakdvppls eteatpvpik dmeiaqtqkg
      601 isedshlesl qdvgqsaapt fmispetvtg tgkkcslpae edsvleklge rkpcnsqpse
      661 lssetsgiar peegrpvvsg tgndittppn kelppspekk tkpiadakap ekraspskpa
      721 sapasrsgsk stqtvakttt aaavastgps srspstllpk kptaiktegk paevkkmtak
      781 svpadlsrpk ststssmkkt ttlsgtapaa gvvpsrvkat pmpsrpsttp fidkkptsak
      841 pssttprlsr latntsapdl knvrskvqiq nkkvdiskvs skcgskanik hkpgggdvki
      901 esqklnfkek aqakvgsldn vghlpaggav ktegggseap lcpgppagee paiseaapea
      961 gaptsasgln ghptlsgggd qreaqtldsq iqetsi
//
LOCUS       NP_001316833             231 aa            linear   PRI 21-NOV-2025
DEFINITION  pigment epithelium-derived factor isoform 2 [Homo sapiens].
ACCESSION   NP_001316833
VERSION     NP_001316833.1
DBSOURCE    REFSEQ: accession NM_001329904.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Tarabeih,R., Nemerovsky,L., Bar-Joseph,H., Eldar-Boock,A.,
            Elmechaly,C.L., Ben-Ami,I. and Shalgi,R.
  TITLE     Pigment epithelium-derived factor expression and role in follicular
            development
  JOURNAL   Reprod Biomed Online 49 (2), 103981 (2024)
   PUBMED   38870625
  REMARK    GeneRIF: Pigment epithelium-derived factor expression and role in
            follicular development.
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Li,R., Weng,X., Hu,X., Wang,J. and Zheng,L.
  TITLE     Pigment epithelium-derived factor inhibits proliferation, invasion
            and angiogenesis, and induces ferroptosis of extravillous
            trophoblasts by targeting Wnt-beta-catenin/VEGF signaling in
            placenta accreta spectrum
  JOURNAL   Mol Med Rep 29 (5) (2024)
   PUBMED   38488028
  REMARK    GeneRIF: Pigment epithelium-derived factor inhibits proliferation,
            invasion and angiogenesis, and induces ferroptosis of extravillous
            trophoblasts by targeting Wnt-beta-catenin/VEGF signaling in
            placenta accreta spectrum.
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Nampei,M., Suzuki,Y., Nakajima,H., Oinaka,H., Kawakita,F.,
            Suzuki,H. and pSEED,Group.
  TITLE     Acute-Phase Plasma Pigment Epithelium-Derived Factor Predicting
            Outcomes after Aneurysmal Subarachnoid Hemorrhage in the Elderly
  JOURNAL   Int J Mol Sci 25 (3), 1701 (2024)
   PUBMED   38338974
  REMARK    GeneRIF: Acute-Phase Plasma Pigment Epithelium-Derived Factor
            Predicting Outcomes after Aneurysmal Subarachnoid Hemorrhage in the
            Elderly.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 231)
  AUTHORS   Ziff,J.L., Crompton,M., Powell,H.R., Lavy,J.A., Aldren,C.P.,
            Steel,K.P., Saeed,S.R. and Dawson,S.J.
  TITLE     Mutations and altered expression of SERPINF1 in patients with
            familial otosclerosis
  JOURNAL   Hum Mol Genet 25 (12), 2393-2403 (2016)
   PUBMED   27056980
  REMARK    GeneRIF: Six rare heterozygous SERPINF1 variants were found in
            seven patients in our familial otosclerosis cohort; three are
            missense mutations predicted to be deleterious to protein function
REFERENCE   6  (residues 1 to 231)
  AUTHORS   Shaheen,R., Alazami,A.M., Alshammari,M.J., Faqeih,E., Alhashmi,N.,
            Mousa,N., Alsinani,A., Ansari,S., Alzahrani,F., Al-Owain,M.,
            Alzayed,Z.S. and Alkuraya,F.S.
  TITLE     Study of autosomal recessive osteogenesis imperfecta in Arabia
            reveals a novel locus defined by TMEM38B mutation
  JOURNAL   J Med Genet 49 (10), 630-635 (2012)
   PUBMED   23054245
REFERENCE   7  (residues 1 to 231)
  AUTHORS   Becerra,S.P., Sagasti,A., Spinella,P. and Notario,V.
  TITLE     Pigment epithelium-derived factor behaves like a noninhibitory
            serpin. Neurotrophic activity does not require the serpin reactive
            loop
  JOURNAL   J Biol Chem 270 (43), 25992-25999 (1995)
   PUBMED   7592790
REFERENCE   8  (residues 1 to 231)
  AUTHORS   Tombran-Tink,J., Pawar,H., Swaroop,A., Rodriguez,I. and Chader,G.J.
  TITLE     Localization of the gene for pigment epithelium-derived factor
            (PEDF) to chromosome 17p13.1 and expression in cultured human
            retinoblastoma cells
  JOURNAL   Genomics 19 (2), 266-272 (1994)
   PUBMED   8188257
REFERENCE   9  (residues 1 to 231)
  AUTHORS   Becerra,S.P., Palmer,I., Kumar,A., Steele,F., Shiloach,J.,
            Notario,V. and Chader,G.J.
  TITLE     Overexpression of fetal human pigment epithelium-derived factor in
            Escherichia coli. A functionally active neurotrophic factor
  JOURNAL   J Biol Chem 268 (31), 23148-23156 (1993)
   PUBMED   8226833
REFERENCE   10 (residues 1 to 231)
  AUTHORS   Steele,F.R., Chader,G.J., Johnson,L.V. and Tombran-Tink,J.
  TITLE     Pigment epithelium-derived factor: neurotrophic activity and
            identification as a member of the serine protease inhibitor gene
            family
  JOURNAL   Proc Natl Acad Sci U S A 90 (4), 1526-1530 (1993)
   PUBMED   8434014
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC130343.7 and AC130689.8.
            
            Summary: This gene encodes a member of the serpin family that does
            not display the serine protease inhibitory activity shown by many
            of the other serpin proteins. The encoded protein is secreted and
            strongly inhibits angiogenesis. In addition, this protein is a
            neurotrophic factor involved in neuronal differentiation in
            retinoblastoma cells. Mutations in this gene were found in
            individuals with osteogenesis imperfecta, type VI. [provided by
            RefSeq, Aug 2016].
            
            Transcript Variant: This variant (3) lacks a portion of the 5' UTR
            and 5' coding region, compared to variant 1, and initiates
            translation at a downstream start codon. The encoded isoform (2)
            has a shorter N-terminus than isoform 1. Variants 3 and 4 encode
            the same isoform (2).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2233790.1,
                                           SRR14038196.3408814.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.3"
     Protein         1..231
                     /product="pigment epithelium-derived factor isoform 2"
                     /note="pigment epithelium-derived factor; serine (or
                     cysteine) proteinase inhibitor, clade F (alpha-2
                     antiplasmin, pigment epithelium derived factor), member 1;
                     serpin peptidase inhibitor, clade F (alpha-2 antiplasmin,
                     pigment epithelium derived factor), member 1; testis
                     tissue sperm-binding protein Li 70n; cell
                     proliferation-inducing gene 35 protein"
                     /calculated_mol_wt=25847
     Region          <1..226
                     /region_name="serpin"
                     /note="SERine Proteinase INhibitors (serpin) family;
                     cl38926"
                     /db_xref="CDD:476815"
     Site            order(181..191,206)
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381000"
     CDS             1..231
                     /gene="SERPINF1"
                     /gene_synonym="EPC-1; OI12; OI6; PEDF; PIG35"
                     /coded_by="NM_001329904.2:532..1227"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:5176"
                     /db_xref="HGNC:HGNC:8824"
                     /db_xref="MIM:172860"
ORIGIN      
        1 mkgklarstk eipdeisill lgvahfkgqw vtkfdsrkts ledfyldeer tvrvpmmsdp
       61 kavlryglds dlsckiaqlp ltgsmsiiff lplkvtqnlt lieesltsef ihdidrelkt
      121 vqavltvpkl klsyegevtk slqemklqsl fdspdfskit gkpikltqve hragfewned
      181 gagttpspgl qpahltfpld yhlnqpfifv lrdtdtgall figkildprg p
//
LOCUS       NP_001380296             732 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 10 isoform 5 [Homo sapiens].
ACCESSION   NP_001380296 XP_016861599
VERSION     NP_001380296.1
DBSOURCE    REFSEQ: accession NM_001393367.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 732)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   3  (residues 1 to 732)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 732)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 732)
  AUTHORS   Raisch,T., Chang,C.T., Levdansky,Y., Muthukumar,S., Raunser,S. and
            Valkov,E.
  TITLE     Reconstitution of recombinant human CCR4-NOT reveals molecular
            insights into regulated deadenylation
  JOURNAL   Nat Commun 10 (1), 3173 (2019)
   PUBMED   31320642
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 732)
  AUTHORS   Miyasaka,T., Morita,M., Ito,K., Suzuki,T., Fukuda,H., Takeda,S.,
            Inoue,J., Semba,K. and Yamamoto,T.
  TITLE     Interaction of antiproliferative protein Tob with the CCR4-NOT
            deadenylase complex
  JOURNAL   Cancer Sci 99 (4), 755-761 (2008)
   PUBMED   18377426
REFERENCE   7  (residues 1 to 732)
  AUTHORS   Morita,M., Suzuki,T., Nakamura,T., Yokoyama,K., Miyasaka,T. and
            Yamamoto,T.
  TITLE     Depletion of mammalian CCR4b deadenylase triggers elevation of the
            p27Kip1 mRNA level and impairs cell growth
  JOURNAL   Mol Cell Biol 27 (13), 4980-4990 (2007)
   PUBMED   17452450
REFERENCE   8  (residues 1 to 732)
  AUTHORS   Tsang,H.T., Connell,J.W., Brown,S.E., Thompson,A., Reid,E. and
            Sanderson,C.M.
  TITLE     A systematic analysis of human CHMP protein interactions:
            additional MIT domain-containing proteins bind to multiple
            components of the human ESCRT III complex
  JOURNAL   Genomics 88 (3), 333-346 (2006)
   PUBMED   16730941
REFERENCE   9  (residues 1 to 732)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 732)
  AUTHORS   Weng,N.P., Snyder,J.G., Yu-Lee,L.Y. and Marcus,D.M.
  TITLE     Polymorphism of human immunoglobulin VH4 germ-line genes
  JOURNAL   Eur J Immunol 22 (4), 1075-1082 (1992)
   PUBMED   1348029
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC138972.8 and AC139452.4.
            
            On Feb 5, 2021 this sequence version replaced XP_016861599.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2691530.1,
                                           SRR14038191.2962085.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.3"
     Protein         1..732
                     /product="CCR4-NOT transcription complex subunit 10
                     isoform 5"
                     /calculated_mol_wt=80928
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9A5.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9H9A5.1)"
     Region          183..204
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9A5.1)"
     Region          248..>404
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          296..321
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(297..298,301..302,304,356,359..360,363..364,
                     366..367,390,393..394,397..398,401)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          354..384
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          477..521
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9A5.1)"
     CDS             1..732
                     /gene="CNOT10"
                     /coded_by="NM_001393367.1:274..2472"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:25904"
                     /db_xref="HGNC:HGNC:23817"
                     /db_xref="MIM:620508"
ORIGIN      
        1 maadkpadqg aekhegtgqs sgitdqekel stnafqafts gnydaclqhl aclqdinkdd
       61 ykiilntava effksnqttt dnlrqtlnql knqvhsavee mdglddvens mlyynqavil
      121 yhlrqyteai svgeklyqfi epfeekfaqa vcfllvdlyi ltyqaekalh llavlekmis
      181 qgnnnkngkn etgnnnnkdg snhkaesgal ieaakskihq ykvrayiqmk slkackreik
      241 svmntagnsa pslflksnfe ylrgnyrkav kllnssniae hpgfmktgec lrcmfwnnlg
      301 cihfamskhn lgifyfkkal qendnvcaql sagstdpgkk fsgrpmctll tnkryellyn
      361 cgiqllhigr plaafeclie avqvyhanpr lwlrlaecci aankgtseqe tkglpskkgi
      421 vqsivgqgyh rkivlasqsi qntvyndgqs saipvasmef aaiclrnall llpeeqqdpk
      481 qengaknsnq lggntesses setcsskshd gdkfipapps splrkqelen lkcsilacsa
      541 yvalalgdnl malnhadkll qqpklsgslk flghlyaaea lisldrisda ithlnpenvt
      601 dvslgissne qdqagkrapq cypssvnsar tvmlfnlgsa yclrseydka rkclhqaasm
      661 ihpkevppea illavylelq ngntqlalqi ikrnqllpav kthsevrkkp vfqpvhpiqp
      721 iqmpafttvq rk
//
LOCUS       NP_003556               1050 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase ULK1 [Homo sapiens].
ACCESSION   NP_003556 XP_947218
VERSION     NP_003556.2
DBSOURCE    REFSEQ: accession NM_003565.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1050)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 1050)
  AUTHORS   Zhang,Z., Liu,X., Chu,C., Zhang,Y., Li,W., Yu,X., Han,Q., Sun,H.,
            Zhang,Y., Zhu,X., Chen,L., Wei,R., Fan,N., Zhou,M. and Li,X.
  TITLE     MIR937 amplification potentiates ovarian cancer progression by
            attenuating FBXO16 inhibition on ULK1-mediated autophagy
  JOURNAL   Cell Death Dis 15 (10), 735 (2024)
   PUBMED   39384743
  REMARK    GeneRIF: MIR937 amplification potentiates ovarian cancer
            progression by attenuating FBXO16 inhibition on ULK1-mediated
            autophagy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1050)
  AUTHORS   Sankar,D.S., Kaeser-Pebernard,S., Vionnet,C., Favre,S., de Oliveira
            Marchioro,L., Pillet,B., Zhou,J., Stumpe,M., Kovacs,W.J.,
            Kressler,D., Antonioli,M., Fimia,G.M. and Dengjel,J.
  TITLE     The ULK1 effector BAG2 regulates autophagy initiation by modulating
            AMBRA1 localization
  JOURNAL   Cell Rep 43 (9), 114689 (2024)
   PUBMED   39207901
  REMARK    GeneRIF: The ULK1 effector BAG2 regulates autophagy initiation by
            modulating AMBRA1 localization.
REFERENCE   4  (residues 1 to 1050)
  AUTHORS   Yong,M., Zeng,Y., Yao,Y., Yang,M., Tang,F., Zhu,H. and Hu,J.
  TITLE     CircFAM188A Regulates Autophagy via miR-670-3p and ULK1 in
            Epithelial Ovarian Carcinoma
  JOURNAL   Cancer Rep (Hoboken) 7 (9), e2128 (2024)
   PUBMED   39229655
  REMARK    GeneRIF: CircFAM188A Regulates Autophagy via miR-670-3p and ULK1 in
            Epithelial Ovarian Carcinoma.
REFERENCE   5  (residues 1 to 1050)
  AUTHORS   Ghazi,P.C., O'Toole,K.T., Srinivas Boggaram,S., Scherzer,M.T.,
            Silvis,M.R., Zhang,Y., Bogdan,M., Smith,B.D., Lozano,G.,
            Flynn,D.L., Snyder,E.L., Kinsey,C.G. and McMahon,M.
  TITLE     Inhibition of ULK1/2 and KRASG12C controls tumor growth in
            preclinical models of lung cancer
  JOURNAL   Elife 13, 96992 (2024)
   PUBMED   39213022
  REMARK    GeneRIF: Inhibition of ULK1/2 and KRAS[G12C] controls tumor growth
            in preclinical models of lung cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1050)
  AUTHORS   Young,A.R., Chan,E.Y., Hu,X.W., Kochl,R., Crawshaw,S.G., High,S.,
            Hailey,D.W., Lippincott-Schwartz,J. and Tooze,S.A.
  TITLE     Starvation and ULK1-dependent cycling of mammalian Atg9 between the
            TGN and endosomes
  JOURNAL   J Cell Sci 119 (Pt 18), 3888-3900 (2006)
   PUBMED   16940348
  REMARK    GeneRIF: Starvation-induced autophagy, which requires mAtg9, may
            rely on an alteration of the steady-state trafficking of mAtg9, in
            a Atg1-dependent manner.
REFERENCE   7  (residues 1 to 1050)
  AUTHORS   Zhang,D.D., Lo,S.C., Cross,J.V., Templeton,D.J. and Hannink,M.
  TITLE     Keap1 is a redox-regulated substrate adaptor protein for a
            Cul3-dependent ubiquitin ligase complex
  JOURNAL   Mol Cell Biol 24 (24), 10941-10953 (2004)
   PUBMED   15572695
REFERENCE   8  (residues 1 to 1050)
  AUTHORS   Tomoda,T., Kim,J.H., Zhan,C. and Hatten,M.E.
  TITLE     Role of Unc51.1 and its binding partners in CNS axon outgrowth
  JOURNAL   Genes Dev 18 (5), 541-558 (2004)
   PUBMED   15014045
REFERENCE   9  (residues 1 to 1050)
  AUTHORS   Okazaki,N., Yan,J., Yuasa,S., Ueno,T., Kominami,E., Masuho,Y.,
            Koga,H. and Muramatsu,M.
  TITLE     Interaction of the Unc-51-like kinase and microtubule-associated
            protein light chain 3 related proteins in the brain: possible role
            of vesicular transport in axonal elongation
  JOURNAL   Brain Res Mol Brain Res 85 (1-2), 1-12 (2000)
   PUBMED   11146101
REFERENCE   10 (residues 1 to 1050)
  AUTHORS   Kuroyanagi,H., Yan,J., Seki,N., Yamanouchi,Y., Suzuki,Y.,
            Takano,T., Muramatsu,M. and Shirasawa,T.
  TITLE     Human ULK1, a novel serine/threonine kinase related to UNC-51
            kinase of Caenorhabditis elegans: cDNA cloning, expression, and
            chromosomal assignment
  JOURNAL   Genomics 51 (1), 76-85 (1998)
   PUBMED   9693035
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131009.7.
            
            On Sep 5, 2019 this sequence version replaced NP_003556.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF045458.1, AB018265.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321867.6/ ENSP00000324560.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1050
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.33"
     Protein         1..1050
                     /product="serine/threonine-protein kinase ULK1"
                     /EC_number="2.7.11.1"
                     /note="ATG1 autophagy related 1 homolog; autophagy-related
                     protein 1 homolog"
                     /calculated_mol_wt=112501
     Region          13..279
                     /region_name="STKc_ULK1"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Unc-51-like kinase 1; cd14202"
                     /db_xref="CDD:271104"
     Site            order(22..26,30,44,46,76,92..95,99,101,138,140,142..143,
                     145,165,168,183..186)
                     /site_type="active"
                     /db_xref="CDD:271104"
     Site            order(22..26,30,44,46,76,92..95,99,138,140,142..143,145,
                     165)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271104"
     Site            order(26,99,101,138,140,142,168,183..186)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271104"
     Site            162
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70405; propagated from
                     UniProtKB/Swiss-Prot (O75385.2)"
     Site            164..186
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271104"
     Region          283..358
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75385.2)"
     Region          287..416
                     /region_name="Interaction with GABARAP and GABARAPL2.
                     /evidence=ECO:0000269|PubMed:11146101"
                     /note="propagated from UniProtKB/Swiss-Prot (O75385.2)"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:25891078; propagated from
                     UniProtKB/Swiss-Prot (O75385.2)"
     Region          393..608
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75385.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75385.2)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75385.2)"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O75385.2)"
     Site            467
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75385.2)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75385.2)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75385.2)"
     Site            479
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75385.2)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70405; propagated from
                     UniProtKB/Swiss-Prot (O75385.2)"
     Site            556
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:24767988,
                     ECO:0000269|PubMed:25891078, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75385.2)"
     Site            575
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O70405; propagated from
                     UniProtKB/Swiss-Prot (O75385.2)"
     Site            607
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70405; propagated from
                     UniProtKB/Swiss-Prot (O75385.2)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O70405; propagated from
                     UniProtKB/Swiss-Prot (O75385.2)"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75385.2)"
     Site            639
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70405; propagated from
                     UniProtKB/Swiss-Prot (O75385.2)"
     Region          728..791
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75385.2)"
     Site            758
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000305|PubMed:21205641,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75385.2)"
     Site            775
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75385.2)"
     Region          828..1050
                     /region_name="C-terminal domain, mediates interaction with
                     SESN2. /evidence=ECO:0000269|PubMed:25040165"
                     /note="propagated from UniProtKB/Swiss-Prot (O75385.2)"
     Region          837..1044
                     /region_name="DUF3543"
                     /note="Domain of unknown function (DUF3543); pfam12063"
                     /db_xref="CDD:463451"
     CDS             1..1050
                     /gene="ULK1"
                     /gene_synonym="ATG1; ATG1A; hATG1; UNC51; Unc51.1"
                     /coded_by="NM_003565.4:381..3533"
                     /db_xref="CCDS:CCDS9274.1"
                     /db_xref="GeneID:8408"
                     /db_xref="HGNC:HGNC:12558"
                     /db_xref="MIM:603168"
ORIGIN      
        1 mepgrggtet vgkfefsrkd lighgafavv fkgrhrekhd levavkcink knlaksqtll
       61 gkeikilkel khenivalyd fqemansvyl vmeycnggdl adylhamrtl sedtirlflq
      121 qiagamrllh skgiihrdlk pqnillsnpa grranpnsir vkiadfgfar ylqsnmmaat
      181 lcgspmymap evimsqhydg kadlwsigti vyqcltgkap fqasspqdlr lfyeknktlv
      241 ptipretsap lrqlllallq rnhkdrmdfd effhhpflda spsvrksppv pvpsypssgs
      301 gsssssssts hlasppslge mqqlqktlas padtagflhs srdsggskds scdtddfvmv
      361 paqfpgdlva eapsakpppd slmcsgsslv asagleshgr tpspsppcss spspsgragp
      421 fsssrcgasv pipvptqvqn yqriernlqs ptqfqtprss airrsgstsp lgfaraspsp
      481 pahaehggvl arkmslgggr pytpspqvgt iperpgwsgt pspqgaemrg grsprpgssa
      541 pehsprtsgl gcrlhsapnl sdlhvvrpkl pkpptdplga vfsppqaspp qpshglqscr
      601 nlrgspklpd flqrnplppi lgsptkavps fdfpktpssq nllallarqg vvmtpprnrt
      661 lpdlsevgpf hgqplgpglr pgedpkgpfg rsfstsrltd lllkaafgtq apdpgstesl
      721 qekpmeiaps agfggslhpg araggtssps pvvftvgspp sgstppqgpr trmfsagptg
      781 sasssarhlv pgpcseapap elpapghgcs fadpitanle gavtfeapdl peetlmeqeh
      841 teilrglrft llfvqhvlei aalkgsasea aggpeyqlqe svvadqisll srewgfaeql
      901 vlylkvaell ssglqsaidq iragklclss tvkqvvrrln elykasvvsc qglslrlqrf
      961 fldkqrlldr ihsitaerli fshavqmvqs aaldemfqhr egcvpryhka lllleglqhm
     1021 lsdqadienv tkcklcierr lsalltgica
//
LOCUS       NP_001363714             513 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 44 [Homo sapiens].
ACCESSION   NP_001363714
VERSION     NP_001363714.1
DBSOURCE    REFSEQ: accession NM_001376785.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Muckenfuss,L.M., Migenda Herranz,A.C., Boneberg,F.M., Clerici,M.
            and Jinek,M.
  TITLE     Fip1 is a multivalent interaction scaffold for processing factors
            in human mRNA 3' end biogenesis
  JOURNAL   Elife 11, e80332 (2022)
   PUBMED   36073787
  REMARK    GeneRIF: Fip1 is a multivalent interaction scaffold for processing
            factors in human mRNA 3' end biogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Tennenbaum,J., Groh,M., Venditti,L., Campos-Gazeau,F., Chalayer,E.,
            De Broucker,T., Hamidou,M., Hunault,M., Lyoubi,A., Meunier,R.,
            Muron,T., Sene,D., Slama,B., Guidoux,C., Lefevre,G., Kahn,J.E.,
            Denier,C. and Rohmer,J.
  TITLE     FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a Treatable
            Cause of Watershed Infarction
  JOURNAL   Stroke 52 (10), e605-e609 (2021)
   PUBMED   34304603
  REMARK    GeneRIF: FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a
            Treatable Cause of Watershed Infarction.
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Helbig,G., Lewandowski,K., Swiderska,A., Rodzaj,M., Seferynska,I.
            and Gajkowska-Kulik,J.
  TITLE     Exquisite response to imatinib mesylate in FIP1L1-PDGFRA-mutated
            hypereosinophilic syndrome: a 12-year experience of the Polish
            Hypereosinophilic Syndrome Study Group
  JOURNAL   Pol Arch Intern Med 130 (3), 255-257 (2020)
   PUBMED   32125294
  REMARK    GeneRIF: Exquisite response to imatinib mesylate in
            FIP1L1-PDGFRA-mutated hypereosinophilic syndrome: a 12-year
            experience of the Polish Hypereosinophilic Syndrome Study Group.
REFERENCE   6  (residues 1 to 513)
  AUTHORS   Cools,J., Quentmeier,H., Huntly,B.J., Marynen,P., Griffin,J.D.,
            Drexler,H.G. and Gilliland,D.G.
  TITLE     The EOL-1 cell line as an in vitro model for the study of
            FIP1L1-PDGFRA-positive chronic eosinophilic leukemia
  JOURNAL   Blood 103 (7), 2802-2805 (2004)
   PUBMED   14630792
  REMARK    GeneRIF: results indicate that the fusion of FIP1L1 to PDGFRA
            occurs rarely in leukemia cell lines
REFERENCE   7  (residues 1 to 513)
  AUTHORS   Kaufmann,I., Martin,G., Friedlein,A., Langen,H. and Keller,W.
  TITLE     Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements
            and stimulates poly(A) polymerase
  JOURNAL   EMBO J 23 (3), 616-626 (2004)
   PUBMED   14749727
REFERENCE   8  (residues 1 to 513)
  AUTHORS   Pardanani,A., Ketterling,R.P., Brockman,S.R., Flynn,H.C.,
            Paternoster,S.F., Shearer,B.M., Reeder,T.L., Li,C.Y., Cross,N.C.,
            Cools,J., Gilliland,D.G., Dewald,G.W. and Tefferi,A.
  TITLE     CHIC2 deletion, a surrogate for FIP1L1-PDGFRA fusion, occurs in
            systemic mastocytosis associated with eosinophilia and predicts
            response to imatinib mesylate therapy
  JOURNAL   Blood 102 (9), 3093-3096 (2003)
   PUBMED   12842979
  REMARK    GeneRIF: observations suggest that the FIP1L1-PDGFRA rearrangement
            occurs in an early hematopoietic progenitor and suggests that the
            molecular pathogenesis for a subset of SMCD patients is similar to
            that of HES
REFERENCE   9  (residues 1 to 513)
  AUTHORS   Griffin,J.H., Leung,J., Bruner,R.J., Caligiuri,M.A. and
            Briesewitz,R.
  TITLE     Discovery of a fusion kinase in EOL-1 cells and idiopathic
            hypereosinophilic syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (13), 7830-7835 (2003)
   PUBMED   12808148
REFERENCE   10 (residues 1 to 513)
  AUTHORS   Cools,J., DeAngelo,D.J., Gotlib,J., Stover,E.H., Legare,R.D.,
            Cortes,J., Kutok,J., Clark,J., Galinsky,I., Griffin,J.D.,
            Cross,N.C., Tefferi,A., Malone,J., Alam,R., Schrier,S.L.,
            Schmid,J., Rose,M., Vandenberghe,P., Verhoef,G., Boogaerts,M.,
            Wlodarska,I., Kantarjian,H., Marynen,P., Coutre,S.E., Stone,R. and
            Gilliland,D.G.
  TITLE     A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes
            as a therapeutic target of imatinib in idiopathic hypereosinophilic
            syndrome
  JOURNAL   N Engl J Med 348 (13), 1201-1214 (2003)
   PUBMED   12660384
  REMARK    GeneRIF: The hypereosinophilic syndrome may result from a novel
            fusion tyrosine kinase - FIP1L1-PDGFRalpha - that is a consequence
            of an interstitial chromosomal deletion.
            GeneRIF: Describes the fusion gene Fip1-like-1-PDGFRalpha in
            patients with idiopathic hypereosinophilic syndrome, mostly
            responsive to imatinib therapy.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098821.3 and AC058822.6.
            
            Summary: This gene encodes a subunit of the CPSF (cleavage and
            polyadenylation specificity factor) complex that polyadenylates the
            3' end of mRNA precursors. This gene, the homolog of yeast Fip1
            (factor interacting with PAP), binds to U-rich sequences of
            pre-mRNA and stimulates poly(A) polymerase activity. Its N-terminus
            contains a PAP-binding site and its C-terminus an RNA-binding
            domain. An interstitial chromosomal deletion on 4q12 creates an
            in-frame fusion of human genes FIP1L1 and PDGFRA (platelet-derived
            growth factor receptor, alpha). The FIP1L1-PDGFRA fusion gene
            encodes a constitutively activated tyrosine kinase that joins the
            first 233 amino acids of FIP1L1 to the last 523 amino acids of
            PDGFRA. This gene fusion and chromosomal deletion is the cause of
            some forms of idiopathic hypereosinophilic syndrome (HES). This
            syndrome, recently reclassified as chronic eosinophilic leukemia
            (CEL), is responsive to treatment with tyrosine kinase inhibitors.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2155974,
                              SAMEA2163623 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..513
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     44"
                     /note="rearranged in hypereosinophilia; pre-mRNA
                     3'-end-processing factor FIP1; FIP1-like 1 protein; factor
                     interacting with PAP; FIP1 like 1; FIP1L1 cleavage and
                     polyadenylation specific factor subunit"
                     /calculated_mol_wt=57041
     CDS             1..513
                     /gene="FIP1L1"
                     /gene_synonym="FIP1; hFip1; Rhe"
                     /coded_by="NM_001376785.1:199..1740"
                     /note="isoform 44 is encoded by transcript variant 44"
                     /db_xref="GeneID:81608"
                     /db_xref="HGNC:HGNC:19124"
                     /db_xref="MIM:607686"
ORIGIN      
        1 msageverlv selsggtggd eeeewlyggp wdvhvhsdla kdldenever peeenasanp
       61 psgiedetae ngvpkpkvte teddsdsdsd ddeddvhvti gdiktgapqy gsygtapvnl
      121 niktggrvyg ttgtkvkgvd ldapgsingv pllevqqgrt gnseketalp stkaeftspp
      181 slfktglpps rnstssqsqt stasrkanss vgkwqdrygr aespdlrrlp gaidvigqti
      241 tisrvegrrr anensniqvl sersatevdn nfskpppffp pgappthlpp ppflpppptv
      301 stapplippp gfppppgapp psliptiesg hssgydsrsa rafpygnvaf phlpgsapsw
      361 pslvdtskqw dyyarrekdr drerdrdrer drdrdrerer trerererdh sptpsvfnsd
      421 eeryryreya ergyerhras rekeerhrer rhrekeetrh kssrsnsrrr heseegdshr
      481 rhkhkkskrs kegkeagsep apeqesteat pae
//
LOCUS       NP_789765                170 aa            linear   PRI 21-NOV-2025
DEFINITION  GTPase HRas isoform 2 [Homo sapiens].
ACCESSION   NP_789765
VERSION     NP_789765.1
DBSOURCE    REFSEQ: accession NM_176795.5
KEYWORDS    RefSeq; MANE Plus Clinical.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Ling,C., Liu,S.S., Wang,Y.Y., Huo,G.T., Yang,Y.W., Xu,N., Wang,H.,
            Wu,Y., Miao,Y.F., Fu,R., Zhao,Y.W. and Fan,C.F.
  TITLE     Overexpression of wild-type HRAS drives non-alcoholic
            steatohepatitis to hepatocellular carcinoma in mice
  JOURNAL   Zool Res 45 (3), 551-566 (2024)
   PUBMED   38757223
  REMARK    GeneRIF: Overexpression of wild-type HRAS drives non-alcoholic
            steatohepatitis to hepatocellular carcinoma in mice.
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Devi,P., Dwivedi,R., Sankar,R., Jain,A., Gupta,S. and Gupta,S.
  TITLE     Unraveling the Genetic Web: H-Ras Expression and Mutation in Oral
            Squamous Cell Carcinoma-A Systematic Review
  JOURNAL   Head Neck Pathol 18 (1), 21 (2024)
   PUBMED   38502412
  REMARK    GeneRIF: Unraveling the Genetic Web: H-Ras Expression and Mutation
            in Oral Squamous Cell Carcinoma-A Systematic Review.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Zhang,Q., Zheng,L., Bai,Y., Su,C., Che,Y., Xu,J., Sun,K., Ni,J.,
            Huang,L., Shen,Y., Jia,L., Xu,L., Yin,R., Li,M. and Hu,J.
  TITLE     ITPR1-AS1 promotes small cell lung cancer metastasis by
            facilitating P21HRAS splicing and stabilizing DDX3X to activate the
            cRaf-MEK-ERK cascade
  JOURNAL   Cancer Lett 577, 216426 (2023)
   PUBMED   37820992
  REMARK    GeneRIF: ITPR1-AS1 promotes small cell lung cancer metastasis by
            facilitating P21[HRAS] splicing and stabilizing DDX3X to activate
            the cRaf-MEK-ERK cascade.
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Wang,J., Al-Majid,D., Brenner,J.C. and Smith,J.D.
  TITLE     Mutant HRas Signaling and Rationale for Use of Farnesyltransferase
            Inhibitors in Head and Neck Squamous Cell Carcinoma
  JOURNAL   Target Oncol 18 (5), 643-655 (2023)
   PUBMED   37665491
  REMARK    GeneRIF: Mutant HRas Signaling and Rationale for Use of
            Farnesyltransferase Inhibitors in Head and Neck Squamous Cell
            Carcinoma.
            Review article
REFERENCE   6  (residues 1 to 170)
  AUTHORS   Gripp,K.W. and Weaver,K.N.
  TITLE     HRAS-Related Costello Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301680
REFERENCE   7  (residues 1 to 170)
  AUTHORS   Sakai,E., Rikimaru,K., Ueda,M., Matsumoto,Y., Ishii,N., Enomoto,S.,
            Yamamoto,H. and Tsuchida,N.
  TITLE     The p53 tumor-suppressor gene and ras oncogene mutations in oral
            squamous-cell carcinoma
  JOURNAL   Int J Cancer 52 (6), 867-872 (1992)
   PUBMED   1459726
REFERENCE   8  (residues 1 to 170)
  AUTHORS   Tanci,P., Genuardi,M., Santini,S.A. and Neri,G.
  TITLE     PCR detection of an insertion/deletion polymorphism in intron 1 of
            the HRAS1 locus
  JOURNAL   Nucleic Acids Res 20 (5), 1157 (1992)
   PUBMED   1549493
REFERENCE   9  (residues 1 to 170)
  AUTHORS   Kinsella,B.T., Erdman,R.A. and Maltese,W.A.
  TITLE     Posttranslational modification of Ha-ras p21 by farnesyl versus
            geranylgeranyl isoprenoids is determined by the COOH-terminal amino
            acid
  JOURNAL   Proc Natl Acad Sci U S A 88 (20), 8934-8938 (1991)
   PUBMED   1924354
REFERENCE   10 (residues 1 to 170)
  AUTHORS   Tong,L.A., de Vos,A.M., Milburn,M.V. and Kim,S.H.
  TITLE     Crystal structures at 2.2 A resolution of the catalytic domains of
            normal ras protein and an oncogenic mutant complexed with GDP
  JOURNAL   J Mol Biol 217 (3), 503-516 (1991)
   PUBMED   1899707
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC137894.5, BM808879.1,
            BQ674260.1 and BQ574535.1.
            
            Summary: This gene belongs to the Ras oncogene family, whose
            members are related to the transforming genes of mammalian sarcoma
            retroviruses. The products encoded by these genes function in
            signal transduction pathways. These proteins can bind GTP and GDP,
            and they have intrinsic GTPase activity. This protein undergoes a
            continuous cycle of de- and re-palmitoylation, which regulates its
            rapid exchange between the plasma membrane and the Golgi apparatus.
            Mutations in this gene cause Costello syndrome, a disease
            characterized by increased growth at the prenatal stage, growth
            deficiency at the postnatal stage, predisposition to tumor
            formation, cognitive disability, skin and musculoskeletal
            abnormalities, distinctive facial appearance and cardiovascular
            abnormalities. Defects in this gene are implicated in a variety of
            cancers, including bladder cancer, follicular thyroid cancer, and
            oral squamous cell carcinoma. Multiple transcript variants, which
            encode different isoforms, have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) includes an alternate exon
            resulting in a frameshift and an early stop codon compared to
            variant 1. The encoded isoform (2) has a shorter and distinct
            C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BQ674260.1, BQ672126.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match :: ENST00000417302.7/ ENSP00000388246.1
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..170
                     /product="GTPase HRas isoform 2"
                     /EC_number="3.6.5.2"
                     /note="Ha-Ras1 proto-oncoprotein; Ras family small GTP
                     binding protein H-Ras; Harvey rat sarcoma viral oncogene
                     homolog; p19 H-RasIDX protein; transforming protein p21;
                     GTPase HRas; GTP- and GDP-binding peptide B;
                     transformation gene: oncogene HAMSV; c-has/bas p21
                     protein; v-Ha-ras Harvey rat sarcoma viral oncogene
                     homolog; Harvey rat sarcoma viral oncoprotein"
                     /calculated_mol_wt=18739
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine, in GTPase HRas, alternate.
                     /evidence=ECO:0000269|Ref.12; propagated from
                     UniProtKB/Swiss-Prot (P01112.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in GTPase HRas, N-terminally
                     processed. /evidence=ECO:0000269|Ref.12; propagated from
                     UniProtKB/Swiss-Prot (P01112.1)"
     Region          3..150
                     /region_name="H_N_K_Ras_like"
                     /note="Ras GTPase family containing H-Ras,N-Ras and
                     K-Ras4A/4B; cd04138"
                     /db_xref="CDD:133338"
     Site            10..17
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133338"
     Site            order(11..12,59..60)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133338"
     Site            order(12..18,28..30,32,35,60,116..117,119..120,145..146)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133338"
     Site            order(17..18,30..32,34,37,40..41,54..55,57,59..61,63..65,
                     67,69..71,73,102..103,147)
                     /site_type="other"
                     /note="GEF interaction site [polypeptide binding]"
                     /db_xref="CDD:133338"
     Site            order(25,37..41)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:133338"
     Region          32..40
                     /region_name="Effector region"
                     /note="propagated from UniProtKB/Swiss-Prot (P01112.1)"
     Site            33..40
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133338"
     Site            35
                     /site_type="glycosylation"
                     /note="(Microbial infection) O-linked (Glc) threonine, by
                     P.sordellii toxin TcsL.
                     /evidence=ECO:0000269|PubMed:19744486,
                     ECO:0000269|PubMed:8626575, ECO:0000269|PubMed:8626586,
                     ECO:0000269|PubMed:9632667; propagated from
                     UniProtKB/Swiss-Prot (P01112.1)"
     Site            35
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133338"
     Site            57..60
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133338"
     Site            59..77
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133338"
     Site            116..119
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133338"
     Site            145..147
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133338"
     CDS             1..170
                     /gene="HRAS"
                     /gene_synonym="C-BAS/HAS; C-H-RAS; C-HA-RAS1; CTLO;
                     H-RASIDX; HAMSV; HRAS1; p21ras; RASH1"
                     /coded_by="NM_176795.5:215..727"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS7699.1"
                     /db_xref="GeneID:3265"
                     /db_xref="HGNC:HGNC:5173"
                     /db_xref="MIM:190020"
ORIGIN      
        1 mteyklvvvg aggvgksalt iqliqnhfvd eydptiedsy rkqvvidget clldildtag
       61 qeeysamrdq ymrtgegflc vfainntksf edihqyreqi krvkdsddvp mvlvgnkcdl
      121 aartvesrqa qdlarsygip yietsaktrq gsrsgsssss gtlwdppgpm
//
LOCUS       NP_000098                427 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA damage-binding protein 2 isoform WT [Homo sapiens].
ACCESSION   NP_000098
VERSION     NP_000098.1
DBSOURCE    REFSEQ: accession NM_000107.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Zhang,C., Li,W., Liu,L., Li,M., Sun,H., Zhang,C., Zhong,L.,
            Huang,J. and Li,T.
  TITLE     DDB2 promotes melanoma cell growth by transcriptionally regulating
            the expression of KMT2A and predicts a poor prognosis
  JOURNAL   FASEB J 38 (12), e23735 (2024)
   PUBMED   38860936
  REMARK    GeneRIF: DDB2 promotes melanoma cell growth by transcriptionally
            regulating the expression of KMT2A and predicts a poor prognosis.
REFERENCE   3  (residues 1 to 427)
  AUTHORS   de Souza Timoteo,A.R., Pinheiro de Almeida,I.C., Yurchenko,A.A., de
            Miranda Henriques,S.R., de Souza Segundo,P., Rajabi,F., Nikolaev,S.
            and Petta,T.B.
  TITLE     Brazilian XP-E siblings carrying a novel DDB2 variant developed
            early-onset melanoma: a case report
  JOURNAL   BMC Med Genomics 16 (1), 186 (2023)
   PUBMED   37573316
  REMARK    GeneRIF: Brazilian XP-E siblings carrying a novel DDB2 variant
            developed early-onset melanoma: a case report.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Schule,S., Bristy,E.A., Muhtadi,R., Kaletka,G., Stewart,S.,
            Ostheim,P., Hermann,C., Asang,C., Pleimes,D., Port,M. and Abend,M.
  TITLE     Four Genes Predictive for the Severity of Hematological Damage
            Reveal a Similar Response after X Irradiation and Chemotherapy
  JOURNAL   Radiat Res 199 (2), 115-123 (2023)
   PUBMED   36480042
  REMARK    GeneRIF: Four Genes Predictive for the Severity of Hematological
            Damage Reveal a Similar Response after X Irradiation and
            Chemotherapy.
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Wang,X., Huang,Z., Li,L., Yang,Y., Zhang,J., Wang,L., Yuan,J. and
            Li,Y.
  TITLE     The Role of Alternative Splicing Factors, DDB2-Related Ageing and
            DNA Damage Repair in the Progression and Prognosis of Stomach
            Adenocarcinoma Patients
  JOURNAL   Genes (Basel) 14 (1), 39 (2022)
   PUBMED   36672781
  REMARK    GeneRIF: The Role of Alternative Splicing Factors, DDB2-Related
            Ageing and DNA Damage Repair in the Progression and Prognosis of
            Stomach Adenocarcinoma Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Hayes,S., Shiyanov,P., Chen,X. and Raychaudhuri,P.
  TITLE     DDB, a putative DNA repair protein, can function as a
            transcriptional partner of E2F1
  JOURNAL   Mol Cell Biol 18 (1), 240-249 (1998)
   PUBMED   9418871
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Nichols,A.F., Ong,P. and Linn,S.
  TITLE     Mutations specific to the xeroderma pigmentosum group E Ddb-
            phenotype
  JOURNAL   J Biol Chem 271 (40), 24317-24320 (1996)
   PUBMED   8798680
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Dualan,R., Brody,T., Keeney,S., Nichols,A.F., Admon,A. and Linn,S.
  TITLE     Chromosomal localization and cDNA cloning of the genes (DDB1 and
            DDB2) for the p127 and p48 subunits of a human damage-specific DNA
            binding protein
  JOURNAL   Genomics 29 (1), 62-69 (1995)
   PUBMED   8530102
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Keeney,S., Chang,G.J. and Linn,S.
  TITLE     Characterization of a human DNA damage binding protein implicated
            in xeroderma pigmentosum E
  JOURNAL   J Biol Chem 268 (28), 21293-21300 (1993)
   PUBMED   8407967
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U18300.1 and AA278953.1.
            
            Summary: This gene encodes a protein that is necessary for the
            repair of ultraviolet light-damaged DNA. This protein is the
            smaller subunit of a heterodimeric protein complex that
            participates in nucleotide excision repair, and this complex
            mediates the ubiquitylation of histones H3 and H4, which
            facilitates the cellular response to DNA damage. This subunit
            appears to be required for DNA binding. Mutations in this gene
            cause xeroderma pigmentosum complementation group E, a recessive
            disease that is characterized by an increased sensitivity to UV
            light and a high predisposition for skin cancer development, in
            some cases accompanied by neurological abnormalities. Two
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (WT) represents the longer
            transcript and encodes the longer isoform (WT).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000093.2, U18300.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256996.9/ ENSP00000256996.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..427
                     /product="DNA damage-binding protein 2 isoform WT"
                     /note="xeroderma pigmentosum group E protein; UV-damaged
                     DNA-binding protein 2; DDB p48 subunit; DNA damage-binding
                     protein 2; damage-specific DNA binding protein 2, 48kDa"
                     /calculated_mol_wt=47733
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92466.1)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Site            35
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32789493; propagated from
                     UniProtKB/Swiss-Prot (Q92466.1)"
     Region          68..79
                     /region_name="Required for interaction with DDB1.
                     /evidence=ECO:0000269|PubMed:9632823"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Site            77
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32789493; propagated from
                     UniProtKB/Swiss-Prot (Q92466.1)"
     Region          87..98
                     /region_name="Required for interaction with DDB1.
                     /evidence=ECO:0000269|PubMed:9632823"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Region          115..419
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          115..154
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          116..151
                     /region_name="WD 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:19109893"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Site            order(129,133,139..140,152,155,174,178,184..185,196,198,
                     217,222,228..229,241,259,264,270..271,286..287,305,309,
                     315..316,328..329,352,358,375..376,388..389,409,418..419)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          159..194
                     /region_name="WD 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:19109893"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Region          160..195
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          200..239
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          203..238
                     /region_name="WD 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:19109893"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Region          244..287
                     /region_name="WD 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:19109893"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Region          246..284
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          256..274
                     /region_name="DWD box.
                     /evidence=ECO:0000269|PubMed:17079684"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Region          290..329
                     /region_name="WD 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:19109893"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Region          291..328
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          334..336
                     /region_name="Photolesion recognition"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Region          343..386
                     /region_name="WD 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:19109893"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Region          396..420
                     /region_name="WD 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:19109893"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     CDS             1..427
                     /gene="DDB2"
                     /gene_synonym="DDBB; UV-DDB2; XPE"
                     /coded_by="NM_000107.3:164..1447"
                     /note="isoform WT is encoded by transcript variant WT"
                     /db_xref="CCDS:CCDS7927.1"
                     /db_xref="GeneID:1643"
                     /db_xref="HGNC:HGNC:2718"
                     /db_xref="MIM:600811"
ORIGIN      
        1 mapkkrpetq ktseivlrpr nkrsrsplel epeakklcak gsgpsrrcds dclwvglagp
       61 qilppcrsiv rtlhqhklgr aswpsvqqgl qqsflhtlds yrilqkaapf drratslawh
      121 pthpstvavg skggdimlwn fgikdkptfi kgigaggsit glkfnplntn qfyassmegt
      181 trlqdfkgni lrvfassdti niwfcsldvs assrmvvtgd nvgnvillnm dgkelwnlrm
      241 hkkkvthval npccdwflat asvdqtvkiw dlrqvrgkas flyslphrhp vnaacfspdg
      301 arllttdqks eirvysasqw dcplgliphp hrhfqhltpi kaawhprynl ivvgrypdpn
      361 fksctpyelr tidvfdgnsg kmmcqlydpe ssgisslnef npmgdtlasa mgyhiliwsq
      421 eeartrk
//
LOCUS       NP_001035737             115 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase III subunit RPC9 isoform b [Homo
            sapiens].
ACCESSION   NP_001035737
VERSION     NP_001035737.1
DBSOURCE    REFSEQ: accession NM_001040647.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Nelson-Maney,N.P., Balint,L., Beeson,A.L., Serafin,D.S.,
            Kistner,B.M., Douglas,E.S., Siddiqui,A.H., Tauro,A.M. and
            Caron,K.M.
  TITLE     Meningeal lymphatic CGRP signaling governs pain via cerebrospinal
            fluid efflux and neuroinflammation in migraine models
  JOURNAL   J Clin Invest 134 (15), e175616 (2024)
   PUBMED   38743922
  REMARK    GeneRIF: Meningeal lymphatic CGRP signaling governs pain via
            cerebrospinal fluid efflux and neuroinflammation in migraine
            models.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Ramsay,E.P., Abascal-Palacios,G., Daiss,J.L., King,H., Gouge,J.,
            Pilsl,M., Beuron,F., Morris,E., Gunkel,P., Engel,C. and Vannini,A.
  TITLE     Structure of human RNA polymerase III
  JOURNAL   Nat Commun 11 (1), 6409 (2020)
   PUBMED   33335104
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Moreno,M.J., Terron,J.A., Stanimirovic,D.B., Doods,H. and Hamel,E.
  TITLE     Characterization of calcitonin gene-related peptide (CGRP)
            receptors and their receptor-activity-modifying proteins (RAMPs) in
            human brain microvascular and astroglial cells in culture
  JOURNAL   Neuropharmacology 42 (2), 270-280 (2002)
   PUBMED   11804624
REFERENCE   7  (residues 1 to 115)
  AUTHORS   Prado,M.A., Evans-Bain,B., Oliver,K.R. and Dickerson,I.M.
  TITLE     The role of the CGRP-receptor component protein (RCP) in
            adrenomedullin receptor signal transduction
  JOURNAL   Peptides 22 (11), 1773-1781 (2001)
   PUBMED   11754963
REFERENCE   8  (residues 1 to 115)
  AUTHORS   Evans,B.N., Rosenblatt,M.I., Mnayer,L.O., Oliver,K.R. and
            Dickerson,I.M.
  TITLE     CGRP-RCP, a novel protein required for signal transduction at
            calcitonin gene-related peptide and adrenomedullin receptors
  JOURNAL   J Biol Chem 275 (40), 31438-31443 (2000)
   PUBMED   10903324
REFERENCE   9  (residues 1 to 115)
  AUTHORS   Balkan,W., Oates,E.L., Howard,G.A. and Roos,B.A.
  TITLE     Testes exhibit elevated expression of calcitonin gene-related
            peptide receptor component protein
  JOURNAL   Endocrinology 140 (3), 1459-1469 (1999)
   PUBMED   10067875
REFERENCE   10 (residues 1 to 115)
  AUTHORS   Luebke,A.E., Dahl,G.P., Roos,B.A. and Dickerson,I.M.
  TITLE     Identification of a protein that confers calcitonin gene-related
            peptide responsiveness to oocytes by using a cystic fibrosis
            transmembrane conductance regulator assay
  JOURNAL   Proc Natl Acad Sci U S A 93 (8), 3455-3460 (1996)
   PUBMED   8622957
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI600330.1, BC040107.1,
            AC068533.7 and BC052570.1.
            
            Summary: This gene encodes a membrane protein that functions as
            part of a receptor complex for a small neuropeptide that increases
            intracellular cAMP levels. Alternate transcriptional splice
            variants, encoding different isoforms, have been characterized.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon, compared to variant 1, resulting in a shorter protein
            (isoform b), compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.2966692.1,
                                           SRR14038193.402161.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..115
                     /product="DNA-directed RNA polymerase III subunit RPC9
                     isoform b"
                     /note="calcitonin gene-related peptide-receptor component
                     protein; DNA-directed RNA polymerase III subunit RPC9; RNA
                     polymerase III subunit C9; CGRP-receptor component
                     protein"
                     /calculated_mol_wt=12923
     Region          <14..94
                     /region_name="RPOL4c"
                     /note="DNA-directed RNA-polymerase II subunit; cl00638"
                     /db_xref="CDD:469853"
     CDS             1..115
                     /gene="CRCP"
                     /gene_synonym="C17; CGRP-RCP; CGRPRCP; POLR3I; POLR3J;
                     RCP; RCP9; RPC9"
                     /coded_by="NM_001040647.2:117..464"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47599.1"
                     /db_xref="GeneID:27297"
                     /db_xref="HGNC:HGNC:17888"
                     /db_xref="MIM:606121"
ORIGIN      
        1 mevkdansal lsnyetlkyi sktpcrhqsp eivrefltal kshkltkaek lqllnhrpvt
       61 aveiqlmvee seerlteeqi eallhtvtsi lpaepeaeqk kntnsnvamd eedpa
//
LOCUS       NP_001315575             824 aa            linear   PRI 21-NOV-2025
DEFINITION  transforming growth factor-beta receptor-associated protein 1
            isoform 2 [Homo sapiens].
ACCESSION   NP_001315575 XP_011510495
VERSION     NP_001315575.1
DBSOURCE    REFSEQ: accession NM_001328646.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 824)
  AUTHORS   van der Beek,J., Jonker,C., van der Welle,R., Liv,N. and
            Klumperman,J.
  TITLE     CORVET, CHEVI and HOPS - multisubunit tethers of the endo-lysosomal
            system in health and disease
  JOURNAL   J Cell Sci 132 (10) (2019)
   PUBMED   31092635
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 824)
  AUTHORS   Yang,S., Chen,X., Yang,M., Zhao,X., Chen,Y., Zhao,H., Liu,C. and
            Shen,C.
  TITLE     The variant at TGFBRAP1 is significantly associated with type 2
            diabetes mellitus and affects diabetes-related miRNA expression
  JOURNAL   J Cell Mol Med 23 (1), 83-92 (2019)
   PUBMED   30461200
  REMARK    GeneRIF: Findings suggest that genetic polymorphisms of TGF-beta1
            receptor-associated protein 1 (TGFBRAP1) may contribute to the
            genetic susceptibility of type 2 diabetes mellitus (T2DM) by
            mediating diabetes-related miRNA expression.
REFERENCE   6  (residues 1 to 824)
  AUTHORS   Le Clerc,S., Limou,S., Coulonges,C., Carpentier,W., Dina,C.,
            Taing,L., Delaneau,O., Labib,T., Sladek,R., Deveau,C.,
            Guillemain,H., Ratsimandresy,R., Montes,M., Spadoni,J.L.,
            Therwath,A., Schachter,F., Matsuda,F., Gut,I., Lelievre,J.D.,
            Levy,Y., Froguel,P., Delfraissy,J.F., Hercberg,S. and Zagury,J.F.
  CONSRTM   ANRS Genomic Group
  TITLE     Genomewide association study of a rapid progression cohort
            identifies new susceptibility alleles for AIDS (ANRS Genomewide
            Association Study 03)
  JOURNAL   J Infect Dis 200 (8), 1194-1201 (2009)
   PUBMED   19754311
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   7  (residues 1 to 824)
  AUTHORS   Hwang,Y., Chen,E.Y., Gu,Z.J., Chuang,W.L., Yu,M.L., Lai,M.Y.,
            Chao,Y.C., Lee,C.M., Wang,J.H., Dai,C.Y., Shian-Jy Bey,M.,
            Liao,Y.T., Chen,P.J. and Chen,D.S.
  TITLE     Genetic predisposition of responsiveness to therapy for chronic
            hepatitis C
  JOURNAL   Pharmacogenomics 7 (5), 697-709 (2006)
   PUBMED   16886895
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   8  (residues 1 to 824)
  AUTHORS   Wurthner,J.U., Frank,D.B., Felici,A., Green,H.M., Cao,Z.,
            Schneider,M.D., McNally,J.G., Lechleider,R.J. and Roberts,A.B.
  TITLE     Transforming growth factor-beta receptor-associated protein 1 is a
            Smad4 chaperone
  JOURNAL   J Biol Chem 276 (22), 19495-19502 (2001)
   PUBMED   11278302
REFERENCE   9  (residues 1 to 824)
  AUTHORS   Provost,P., Samuelsson,B. and Radmark,O.
  TITLE     Interaction of 5-lipoxygenase with cellular proteins
  JOURNAL   Proc Natl Acad Sci U S A 96 (5), 1881-1885 (1999)
   PUBMED   10051563
REFERENCE   10 (residues 1 to 824)
  AUTHORS   Charng,M.J., Zhang,D., Kinnunen,P. and Schneider,M.D.
  TITLE     A novel protein distinguishes between quiescent and activated forms
            of the type I transforming growth factor beta receptor
  JOURNAL   J Biol Chem 273 (16), 9365-9368 (1998)
   PUBMED   9545258
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012360.7.
            
            On Jun 24, 2016 this sequence version replaced XP_011510495.1.
            
            Summary: This gene encodes a protein that binds to transforming
            growth factor-beta (TGF-beta) receptors and plays a role in
            TGF-beta signaling. The encoded protein acts as a chaprone in
            signaling downstream of TGF-beta. It is involved in
            signal-dependent association with SMAD4. The protein is also a
            component of mammalian CORVET, a multisubunit tethering protein
            complex that is involved in fusion of early endosomes. [provided by
            RefSeq, Jun 2016].
            
            Transcript Variant: This variant (3) contains an alternate 3'
            terminal exon, resulting in novel 3' coding region and 3' UTR. It
            encodes isoform 2, which has a shorter and distinct C-terminus,
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2020075.1,
                                           SRR1803615.186541.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q12.1-q12.2"
     Protein         1..824
                     /product="transforming growth factor-beta
                     receptor-associated protein 1 isoform 2"
                     /note="TGF-beta receptor-associated protein 1; VPS3 CORVET
                     complex subunit"
                     /calculated_mol_wt=92817
     Region          34..283
                     /region_name="CNH"
                     /note="CNH domain; cl02434"
                     /db_xref="CDD:470577"
     Region          448..550
                     /region_name="Vps39_1"
                     /note="Vacuolar sorting protein 39 domain 1; pfam10366"
                     /db_xref="CDD:371008"
     Region          564..728
                     /region_name="CHCR"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUH2.1)"
     Region          571..699
                     /region_name="Clathrin"
                     /note="Region in Clathrin and VPS; pfam00637"
                     /db_xref="CDD:459884"
     Region          738..>804
                     /region_name="Vps39_2"
                     /note="Vacuolar sorting protein 39 domain 2; pfam10367"
                     /db_xref="CDD:402126"
     CDS             1..824
                     /gene="TGFBRAP1"
                     /gene_synonym="TRAP-1; TRAP1; VPS3"
                     /coded_by="NM_001328646.3:129..2603"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:9392"
                     /db_xref="HGNC:HGNC:16836"
                     /db_xref="MIM:606237"
ORIGIN      
        1 mmsikaftlv saverellmg dkervniecv eccgrdlyvg tndcfvyhfl leerpvpagp
       61 atftatkqlq rhlgfkkpvn elraasalnr llvlcdnsis lvnmlnlepv psgarikgaa
      121 tfalnenpvs gdpfcvevci isvkrrtiqm flvyedrvqi vkevstaeqp lavavdghfl
      181 clalttqyii hnystgvsqd lfpycseerp pivkrigrqe fllagpgglg mfatvagisq
      241 rapvhwsenv igaavsfpyv ialddefitv hsmldqqqkq tlpfkeghil qdfegrviva
      301 tskgvyilvp lplekqiqdl lasrrveeal vlakgarrni pkekfqvmyr rilqqagfiq
      361 faqlqfleak elfrsgqldv relislypfl lptsssftrs hpplheyadl nqltqgdqek
      421 makckrflms ylnevrstev angykedidt allklyaead hdslldllvt enfclltdsa
      481 awlekhkkyf algllyhynn qdaaavqlwv nivngdvqds trsdlyeyiv dfltycldee
      541 lvwayadwvl qkseevgvqv ftkrpldeqq knsfnpddii nclkkypkal vkylehlvid
      601 krlqkeeyht hlavlyleev llqrasasgk gaeatetqak lrrllqksdl yrvhfllerl
      661 qgaglpmesa ilhgklgehe kalhilvhel qdfaaaedyc lwcsegrdpp hrqqlfhtll
      721 aiylhagpta helavaavdl lnrhatefda aqvlqmlpdt wsvqllcpfl mgamrdsiha
      781 rrtmqvalgl arsenliyty dktgiagrgt adargssren gdgt
//
LOCUS       NP_001243307             640 aa            linear   PRI 21-NOV-2025
DEFINITION  mini-chromosome maintenance complex-binding protein isoform 2 [Homo
            sapiens].
ACCESSION   NP_001243307
VERSION     NP_001243307.1
DBSOURCE    REFSEQ: accession NM_001256378.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Saito,Y., Santosa,V., Ishiguro,K.I. and Kanemaki,M.T.
  TITLE     MCMBP promotes the assembly of the MCM2-7 hetero-hexamer to ensure
            robust DNA replication in human cells
  JOURNAL   Elife 11, e77393 (2022)
   PUBMED   35438632
  REMARK    GeneRIF: MCMBP promotes the assembly of the MCM2-7 hetero-hexamer
            to ensure robust DNA replication in human cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 640)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 640)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 640)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 640)
  AUTHORS   Nishiyama,A., Frappier,L. and Mechali,M.
  TITLE     MCM-BP regulates unloading of the MCM2-7 helicase in late S phase
  JOURNAL   Genes Dev 25 (2), 165-175 (2011)
   PUBMED   21196493
  REMARK    GeneRIF: MCM-BP silencing in human cells also delays MCM
            dissociation in late S phase
REFERENCE   7  (residues 1 to 640)
  AUTHORS   Takahashi,N., Quimbaya,M., Schubert,V., Lammens,T., Vandepoele,K.,
            Schubert,I., Matsui,M., Inze,D., Berx,G. and De Veylder,L.
  TITLE     The MCM-binding protein ETG1 aids sister chromatid cohesion
            required for postreplicative homologous recombination repair
  JOURNAL   PLoS Genet 6 (1), e1000817 (2010)
   PUBMED   20090939
  REMARK    GeneRIF: Knockdown of the human ETG1 results in defective chromatid
            cohesion.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 640)
  AUTHORS   Sakwe,A.M., Nguyen,T., Athanasopoulos,V., Shire,K. and Frappier,L.
  TITLE     Identification and characterization of a novel component of the
            human minichromosome maintenance complex
  JOURNAL   Mol Cell Biol 27 (8), 3044-3055 (2007)
   PUBMED   17296731
  REMARK    GeneRIF: MCM-BP is conserved in multicellular eukaryotes and shares
            limited homology with MCM proteins. MCM-BP formed a complex with
            MCM3 to MCM7, which excluded MCM2.
REFERENCE   9  (residues 1 to 640)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   10 (residues 1 to 640)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC004183.2 and AC027672.12.
            
            Summary: This gene encodes a protein which is a component of the
            hexameric minichromosome maintenance (MCM) complex which regulates
            initiation and elongation of DNA. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2012].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region compared to variant 1. The
            resulting protein (isoform 2) is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.856279.1,
                                           SRR14038194.939795.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369077.4/ ENSP00000358073.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.11"
     Protein         1..640
                     /product="mini-chromosome maintenance complex-binding
                     protein isoform 2"
                     /note="MCM-binding protein; mini-chromosome maintenance
                     complex-binding protein"
                     /calculated_mol_wt=72618
     Region          36..626
                     /region_name="MCM_bind"
                     /note="Mini-chromosome maintenance replisome factor;
                     pfam09739"
                     /db_xref="CDD:462870"
     Region          151..197
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTE3.2)"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9BTE3.2)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BTE3.2)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BTE3.2)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BTE3.2)"
     CDS             1..640
                     /gene="MCMBP"
                     /gene_synonym="C10orf119; MCM-BP"
                     /coded_by="NM_001256378.2:260..2182"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58099.1"
                     /db_xref="GeneID:79892"
                     /db_xref="HGNC:HGNC:25782"
                     /db_xref="MIM:610909"
ORIGIN      
        1 mpcgedwlsh plgivqgffa qngvnpdwek kvieyfkekl kennapkwvp slnevplhyl
       61 kpnsfvkfrc miqdmfdpef ymgvyetvnq ntkahvlhfg kyrdvaecgp qqeldlnspr
      121 nttlerqtfy cvpvpgestw vkeayvnanq arvspstsyt psrhkrsyed dddmdlqpnk
      181 qkdqhagarq agsvgglqwc gepkrletea stgqqlnsln lsspfdlnfp lpgekgpacl
      241 vkvyedwdcf kvndilelyg ilsvdpvlsi lnnderdasa lldpmectdt aeeqrvhspp
      301 aslvprihvi laqklqhinp llpaclnkee sktfvssfms elspvraell gflthallgd
      361 slaaeylilh listvytrrd vlplgkftvn lsgcprnstf tehlyriiqh lvpasfrlqm
      421 tienmnhlkf iphkdytanr lvsgllqlps ntslvidetl leqgqldtpg vhnvtalsnl
      481 itwqkvdydf syhqmefpcn invfitsegr sllpadcqih lqpqlippnm eeymnsllsa
      541 vlpsvlnkfr iyltllrfle ysisdeitka veddfvemrk ndpqsitadd lhqllvvarc
      601 lslsagqttl srerwlrakq leslrrtrlq qqkcvngnel
//
LOCUS       NP_001034180             321 aa            linear   PRI 21-NOV-2025
DEFINITION  ribose-phosphate pyrophosphokinase 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001034180
VERSION     NP_001034180.1
DBSOURCE    REFSEQ: accession NM_001039091.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Luo,Y., Yuan,J., Huang,J., Yang,T., Zhou,J., Tang,J., Liu,M.,
            Chen,J., Chen,C., Huang,W. and Zhang,H.
  TITLE     Role of PRPS2 as a prognostic and therapeutic target in
            osteosarcoma
  JOURNAL   J Clin Pathol 74 (5), 321-326 (2021)
   PUBMED   33589531
  REMARK    GeneRIF: Role of PRPS2 as a prognostic and therapeutic target in
            osteosarcoma.
            Erratum:[J Clin Pathol. 2021 Aug;74(8):e12. doi:
            10.1136/jclinpath-2020-206505corr1. PMID: 34282027]
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Yang,Y., Song,L., Huang,X., Feng,Y., Zhang,Y., Liu,Y., Li,S.,
            Zhan,Z., Zheng,L., Feng,H. and Li,Y.
  TITLE     PRPS1-mediated purine biosynthesis is critical for pluripotent stem
            cell survival and stemness
  JOURNAL   Aging (Albany NY) 13 (3), 4063-4078 (2021)
   PUBMED   33493137
  REMARK    GeneRIF: PRPS1-mediated purine biosynthesis is critical for
            pluripotent stem cell survival and stemness.
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Lei,B., Zhang,S.B., Xie,L.X. and Mao,X.M.
  TITLE     [Expression of phosphoribosyl pyrophosphate synthase 2 in human
            testis tissue]
  JOURNAL   Zhonghua Nan Ke Xue 26 (2), 128-133 (2020)
   PUBMED   33346415
  REMARK    GeneRIF: [Expression of phosphoribosyl pyrophosphate synthase 2 in
            human testis tissue].
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Ishizuka,T., Iizasa,T., Taira,M., Ishijima,S., Sonoda,T.,
            Shimada,H., Nagatake,N. and Tatibana,M.
  TITLE     Promoter regions of the human X-linked housekeeping genes PRPS1 and
            PRPS2 encoding phosphoribosylpyrophosphate synthetase subunit I and
            II isoforms
  JOURNAL   Biochim Biophys Acta 1130 (2), 139-148 (1992)
   PUBMED   1314091
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Becker,M.A., Heidler,S.A., Bell,G.I., Seino,S., Le Beau,M.M.,
            Westbrook,C.A., Neuman,W., Shapiro,L.J., Mohandas,T.K.,
            Roessler,B.J. et al.
  TITLE     Cloning of cDNAs for human phosphoribosylpyrophosphate synthetases
            1 and 2 and X chromosome localization of PRPS1 and PRPS2 genes
  JOURNAL   Genomics 8 (3), 555-561 (1990)
   PUBMED   1962753
REFERENCE   9  (residues 1 to 321)
  AUTHORS   Taira,M., Iizasa,T., Yamada,K., Shimada,H. and Tatibana,M.
  TITLE     Tissue-differential expression of two distinct genes for
            phosphoribosyl pyrophosphate synthetase and existence of the
            testis-specific transcript
  JOURNAL   Biochim Biophys Acta 1007 (2), 203-208 (1989)
   PUBMED   2537655
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Taira,M., Kudoh,J., Minoshima,S., Iizasa,T., Shimada,H.,
            Shimizu,Y., Tatibana,M. and Shimizu,N.
  TITLE     Localization of human phosphoribosylpyrophosphate synthetase
            subunit I and II genes (PRPS1 and PRPS2) to different regions of
            the X chromosome and assignment of two PRPS1-related genes to
            autosomes
  JOURNAL   Somat Cell Mol Genet 15 (1), 29-37 (1989)
   PUBMED   2536962
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA478574.1, BC119662.1,
            BC110875.1 and BU675363.1.
            
            Summary: This gene encodes a phosphoribosyl pyrophosphate
            synthetase that plays a central role in the synthesis of purines
            and pyrimidines. The encoded protein catalyzes the synthesis of
            5-phosphoribosyl 1-pyrophosphate from ATP and D-ribose 5-phosphate.
            Alternate splicing results in multiple transcript variants.
            [provided by RefSeq, Mar 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005581.1, SRR14038191.4037913.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..321
                     /product="ribose-phosphate pyrophosphokinase 2 isoform 1"
                     /EC_number="2.7.6.1"
                     /note="ribose-phosphate diphosphokinase 2;
                     ribose-phosphate pyrophosphokinase 2; PPRibP synthetase;
                     PRS-II; phosphoribosyl pyrophosphate synthase II;
                     testicular secretory protein Li 41"
                     /calculated_mol_wt=34923
     Region          1..317
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
     Region          215..230
                     /region_name="Binding of phosphoribosylpyrophosphate.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P11908.2)"
     CDS             1..321
                     /gene="PRPS2"
                     /gene_synonym="PRSII"
                     /coded_by="NM_001039091.3:87..1052"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43918.1"
                     /db_xref="GeneID:5634"
                     /db_xref="HGNC:HGNC:9465"
                     /db_xref="MIM:311860"
ORIGIN      
        1 mpnivlfsgs shqdlsqrva drlglelgkv vtkkfsnqet sveigesvrg edvyiiqsgc
       61 geindnlmel liminackia sssrvtavip cfpyarqdkk dkvgesrapi saklvanmls
      121 vagadhiitm dlhasqiqgf fdipvdnlya epavlqwire niaewkncii vspdaggakr
      181 vtsiadrlnv efalihkerk kanevdrmvl vgdvkdrvai lvddmadtcg tichaadkll
      241 sagatkvyai lthgifsgpa isrinnaafe avvvtntipq edkmkhctki qvidismila
      301 eairrthnge svsylfshvp l
//
LOCUS       NP_001379000             782 aa            linear   PRI 21-NOV-2025
DEFINITION  cysteine-rich protein 2-binding protein isoform 1 [Homo sapiens].
ACCESSION   NP_001379000
VERSION     NP_001379000.1
DBSOURCE    REFSEQ: accession NM_001392071.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Gong,Y., Liu,M., Zhang,Q., Li,J., Cai,H., Ran,J., Ma,L., Ma,Y. and
            Quan,S.
  TITLE     Lysine acetyltransferase 14 mediates TGF-beta-induced fibrosis in
            ovarian endometrioma via co-operation with serum response factor
  JOURNAL   J Transl Med 22 (1), 561 (2024)
   PUBMED   38867256
  REMARK    GeneRIF: Lysine acetyltransferase 14 mediates TGF-beta-induced
            fibrosis in ovarian endometrioma via co-operation with serum
            response factor.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 782)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 782)
  AUTHORS   Viita,T., Kyheroinen,S., Prajapati,B., Virtanen,J., Frilander,M.J.,
            Varjosalo,M. and Vartiainen,M.K.
  TITLE     Nuclear actin interactome analysis links actin to KAT14 histone
            acetyl transferase and mRNA splicing
  JOURNAL   J Cell Sci 132 (8) (2019)
   PUBMED   30890647
  REMARK    GeneRIF: Actin binds directly to the hATAC subunit KAT14, and
            modulates its histone acetyl transferase activity in vitro and in
            cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 782)
  AUTHORS   Orpinell,M., Fournier,M., Riss,A., Nagy,Z., Krebs,A.R., Frontini,M.
            and Tora,L.
  TITLE     The ATAC acetyl transferase complex controls mitotic progression by
            targeting non-histone substrates
  JOURNAL   EMBO J 29 (14), 2381-2394 (2010)
   PUBMED   20562830
REFERENCE   7  (residues 1 to 782)
  AUTHORS   Nagy,Z., Riss,A., Fujiyama,S., Krebs,A., Orpinell,M., Jansen,P.,
            Cohen,A., Stunnenberg,H.G., Kato,S. and Tora,L.
  TITLE     The metazoan ATAC and SAGA coactivator HAT complexes regulate
            different sets of inducible target genes
  JOURNAL   Cell Mol Life Sci 67 (4), 611-628 (2010)
   PUBMED   19936620
REFERENCE   8  (residues 1 to 782)
  AUTHORS   Guelman,S., Kozuka,K., Mao,Y., Pham,V., Solloway,M.J., Wang,J.,
            Wu,J., Lill,J.R. and Zha,J.
  TITLE     The double-histone-acetyltransferase complex ATAC is essential for
            mammalian development
  JOURNAL   Mol Cell Biol 29 (5), 1176-1188 (2009)
   PUBMED   19103755
REFERENCE   9  (residues 1 to 782)
  AUTHORS   Wang,Y.L., Faiola,F., Xu,M., Pan,S. and Martinez,E.
  TITLE     Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel
            NC2-like histone fold module that interacts with the TATA-binding
            protein
  JOURNAL   J Biol Chem 283 (49), 33808-33815 (2008)
   PUBMED   18838386
REFERENCE   10 (residues 1 to 782)
  AUTHORS   Weiskirchen,R. and Gressner,A.M.
  TITLE     The cysteine- and glycine-rich LIM domain protein CRP2 specifically
            interacts with a novel human protein (CRP2BP)
  JOURNAL   Biochem Biophys Res Commun 274 (3), 655-663 (2000)
   PUBMED   10924333
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL050321.11 and KF459584.1.
            
            Summary: CSRP2 is a protein containing two LIM domains, which are
            double zinc finger motifs found in proteins of diverse function.
            CSRP2 and some related proteins are thought to act as protein
            adapters, bridging two or more proteins to form a larger protein
            complex. The protein encoded by this gene binds to one of the LIM
            domains of CSRP2 and contains an acetyltransferase domain. Although
            the encoded protein has been detected in the cytoplasm, it is
            predominantly a nuclear protein. Alternatively spliced transcript
            variants have been described. [provided by RefSeq, Jun 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.133322.1,
                                           SRR1803612.136115.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.23"
     Protein         1..782
                     /product="cysteine-rich protein 2-binding protein isoform
                     1"
                     /note="CRP2 binding protein; ATAC component 2 homolog;
                     CRP2 binding partner; cysteine-rich protein 2-binding
                     protein; CSRP2-binding protein; ADA2A-containing complex
                     subunit 2"
                     /calculated_mol_wt=88713
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Region          13..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Site            231
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8CID0; propagated from
                     UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Region          251..282
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Site            292
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Region          315..346
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Region          400..460
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Region          686..761
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
     CDS             1..782
                     /gene="KAT14"
                     /gene_synonym="ATAC2; CRP2BP; CSRP2BP; dJ717M23.1;
                     PRO1194"
                     /coded_by="NM_001392071.1:512..2860"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS13133.1"
                     /db_xref="GeneID:57325"
                     /db_xref="HGNC:HGNC:15904"
                     /db_xref="MIM:617501"
ORIGIN      
        1 mdssihlssl isrhddeatr tstsegleeg evegetlliv esedqasvdl shdqsgdsln
       61 sdegdvswme eqlsyfcdkc qkwipasqlr eqlsylkgdn ffrftcsdcs adgkeqyerl
      121 kltwqqvvml amynlslegs grqgyfrwke dicafiekhw tfllgnrkkt stwwstvagc
      181 lsvgspmyfr sgaqefgepg wwklvhnkpp tmkpegekls astlkikaas kptldpiitv
      241 eglrkrasrn pvesamelke krsrtqeakd irraqkeaag fldrstsstp vkfisrgrrp
      301 dvilekgevi dfsslsssdr tpltspspsp sldfsapgtp ashsatpsll seadlipdvm
      361 ppqalfhddd emegdgvidp gmeyvpppag svasgpvvgv rkkvrgpeqi kqeveseeek
      421 pdrmdidsed tdsntslqtr arekrkpqle kdtkpkepry tpvsiyeekl llkrleacpg
      481 avamtpearr lkrklivrqa krdrglplfd ldqvvnaall lvdgiygake ggisrlpagq
      541 atyrttcqdf rildryqtsl psrkgfrhqt tkflyrlvgs edmavdqsiv spytsrilkp
      601 yirrdyetkp pklqllsqir shlhrsdphw tpepdapldy cyvrpnhipt insmcqeffw
      661 pgidlseclq ypdfsvvvly kkviiafgfm vpdvkyneay isflfvhpew rragiatfmi
      721 yhliqtcmgk dvtlhvsasn pamllyqkfg fkteeyvldf ydkyyplest eckhafflrl
      781 rr
//
LOCUS       NP_001135903             288 aa            linear   PRI 21-NOV-2025
DEFINITION  mortality factor 4-like protein 2 [Homo sapiens].
ACCESSION   NP_001135903
VERSION     NP_001135903.1
DBSOURCE    REFSEQ: accession NM_001142431.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Kooblall,K.G., Stokes,V.J., Shariq,O.A., English,K.A.,
            Stevenson,M., Broxholme,J., Wright,B., Lockstone,H.E., Buck,D.,
            Grozinsky-Glasberg,S., Yates,C.J., Thakker,R.V. and Lines,K.E.
  TITLE     miR-3156-5p is downregulated in serum of MEN1 patients and
            regulates expression of MORF4L2
  JOURNAL   Endocr Relat Cancer 29 (10), 557-568 (2022)
   PUBMED   35900839
  REMARK    GeneRIF: miR-3156-5p is downregulated in serum of MEN1 patients and
            regulates expression of MORF4L2.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Zheng,X., Sun,Z., Yu,L., Shi,D., Zhu,M., Yao,H. and Li,L.
  TITLE     Interactome Analysis of the Nucleocapsid Protein of SARS-CoV-2
            Virus
  JOURNAL   Pathogens 10 (9), 1155 (2021)
   PUBMED   34578187
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Cai,Y., Jin,J., Tomomori-Sato,C., Sato,S., Sorokina,I.,
            Parmely,T.J., Conaway,R.C. and Conaway,J.W.
  TITLE     Identification of new subunits of the multiprotein mammalian
            TRRAP/TIP60-containing histone acetyltransferase complex
  JOURNAL   J Biol Chem 278 (44), 42733-42736 (2003)
   PUBMED   12963728
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Yochum,G.S. and Ayer,D.E.
  TITLE     Role for the mortality factors MORF4, MRGX, and MRG15 in
            transcriptional repression via associations with Pf1, mSin3A, and
            Transducin-Like Enhancer of Split
  JOURNAL   Mol Cell Biol 22 (22), 7868-7876 (2002)
   PUBMED   12391155
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Sakai,K., Shirakawa,T., Li,Y., Kitagawa,Y. and Hirose,G.
  TITLE     Interaction of a paraneoplastic cerebellar degeneration-associated
            neuronal protein with the nuclear helix-loop-helix leucine zipper
            protein MRG X
  JOURNAL   Mol Cell Neurosci 19 (4), 477-484 (2002)
   PUBMED   11988016
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Hoja,M.R., Wahlestedt,C. and Hoog,C.
  TITLE     A visual intracellular classification strategy for uncharacterized
            human proteins
  JOURNAL   Exp Cell Res 259 (1), 239-246 (2000)
   PUBMED   10942595
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Bertram,M.J., Berube,N.G., Hang-Swanson,X., Ran,Q., Leung,J.K.,
            Bryce,S., Spurgers,K., Bick,R.J., Baldini,A., Ning,Y., Clark,L.J.,
            Parkinson,E.K., Barrett,J.C., Smith,J.R. and Pereira-Smith,O.M.
  TITLE     Identification of a gene that reverses the immortal phenotype of a
            subset of cells and is a member of a novel family of transcription
            factor-like genes
  JOURNAL   Mol Cell Biol 19 (2), 1479-1485 (1999)
   PUBMED   9891081
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA268606.1, DC366195.1 and BC093013.1.
            
            Transcript Variant: This variant (15) differs in the 5' UTR,
            compared to variant 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.689380.1,
                                           SRR1803615.6636.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.2"
     Protein         1..288
                     /product="mortality factor 4-like protein 2"
                     /note="MSL3-2 protein; protein MSL3-2; MORF-related gene X
                     protein; transcription factor-like protein MRGX"
                     /calculated_mol_wt=32177
     Region          1..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15014.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15014.1)"
     Region          102..276
                     /region_name="MRG"
                     /note="pfam05712"
                     /db_xref="CDD:461721"
     CDS             1..288
                     /gene="MORF4L2"
                     /gene_synonym="MORFL2; MRGX"
                     /coded_by="NM_001142431.2:223..1089"
                     /db_xref="CCDS:CCDS14512.1"
                     /db_xref="GeneID:9643"
                     /db_xref="HGNC:HGNC:16849"
                     /db_xref="MIM:300409"
ORIGIN      
        1 mssrkqgsqp rgqqsaeeen fkkptrsnmq rskmrgassg kktagpqqkn lepalpgrwg
       61 grsaenppsg svrktrknkq ktpgngdggs tseapqpprk kraradptve seeafknrme
      121 vkvkipeelk pwlvedwdlv trqkqlfqlp akknvdaile eyanckksqg nvdnkeyavn
      181 evvagikeyf nvmlgtqlly kferpqyaei llahpdapms qvygaphllr lfvrigamla
      241 ytpldeksla lllgylhdfl kylaknsasl ftasdykvas aeyhrkal
//
LOCUS       NP_001336297             206 aa            linear   PRI 21-NOV-2025
DEFINITION  centromere protein K isoform 4 [Homo sapiens].
ACCESSION   NP_001336297 XP_016865187
VERSION     NP_001336297.1
DBSOURCE    REFSEQ: accession NM_001349368.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Li,G., Shen,J., Cheng,W., Wang,X., Wang,D., Song,Y., Chen,Y.,
            Li,X., Zhang,M., Ding,Y., Ma,X., Qian,Q., Zhang,G., Ji,J. and
            Liu,B.
  TITLE     CENPK orchestrates ovarian cancer progression via GOLPH3-Mediated
            activation of mTOR signaling
  JOURNAL   Mol Cell Endocrinol 589, 112253 (2024)
   PUBMED   38670220
  REMARK    GeneRIF: CENPK orchestrates ovarian cancer progression via
            GOLPH3-Mediated activation of mTOR signaling.
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Li,X., Han,Y.R., Xuefeng,X., Ma,Y.X., Xing,G.S., Yang,Z.W.,
            Zhang,Z., Shi,L. and Wu,X.L.
  TITLE     Lentivirus-mediated short hairpin RNA interference of CENPK
            inhibits growth of colorectal cancer cells with overexpression of
            Cullin 4A
  JOURNAL   World J Gastroenterol 28 (37), 5420-5443 (2022)
   PUBMED   36312839
  REMARK    GeneRIF: Lentivirus-mediated short hairpin RNA interference of
            CENPK inhibits growth of colorectal cancer cells with
            overexpression of Cullin 4A.
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Tian,T., Chen,L., Dou,Z., Yang,Z., Gao,X., Yuan,X., Wang,C.,
            Liu,R., Shen,Z., Gui,P., Teng,M., Meng,X., Hill,D.L., Li,L.,
            Zhang,X., Liu,X., Sun,L., Zang,J. and Yao,X.
  TITLE     Structural insights into human CCAN complex assembled onto DNA
  JOURNAL   Cell Discov 8 (1), 90 (2022)
   PUBMED   36085283
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Tian,H., Wang,F., Deng,Y., Ying,L., Fang,W., Chen,D., Miao,C.,
            Li,H., Sun,S., Ma,Y., Cai,H. and Guo,T.
  TITLE     Centromeric protein K (CENPK) promotes gastric cancer proliferation
            and migration via interacting with XRCC5
  JOURNAL   Gastric Cancer 25 (5), 879-895 (2022)
   PUBMED   35715658
  REMARK    GeneRIF: Centromeric protein K (CENPK) promotes gastric cancer
            proliferation and migration via interacting with XRCC5.
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Okada,M., Cheeseman,I.M., Hori,T., Okawa,K., McLeod,I.X.,
            Yates,J.R. 3rd, Desai,A. and Fukagawa,T.
  TITLE     The CENP-H-I complex is required for the efficient incorporation of
            newly synthesized CENP-A into centromeres
  JOURNAL   Nat Cell Biol 8 (5), 446-457 (2006)
   PUBMED   16622420
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Foltz,D.R., Jansen,L.E., Black,B.E., Bailey,A.O., Yates,J.R. 3rd
            and Cleveland,D.W.
  TITLE     The human CENP-A centromeric nucleosome-associated complex
  JOURNAL   Nat Cell Biol 8 (5), 458-469 (2006)
   PUBMED   16622419
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Obuse,C., Yang,H., Nozaki,N., Goto,S., Okazaki,T. and Yoda,K.
  TITLE     Proteomics analysis of the centromere complex from HeLa interphase
            cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of
            the CEN-complex, while BMI-1 is transiently co-localized with the
            centromeric region in interphase
  JOURNAL   Genes Cells 9 (2), 105-120 (2004)
   PUBMED   15009096
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Yamashita,A., Ito,M., Takamatsu,N. and Shiba,T.
  TITLE     Characterization of Solt, a novel SoxLZ/Sox6 binding protein
            expressed in adult mouse testis
  JOURNAL   FEBS Lett 481 (2), 147-151 (2000)
   PUBMED   10996314
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Taki,T., Hayashi,Y., Taniwaki,M., Seto,M., Ueda,R., Hanada,R.,
            Suzukawa,K., Yokota,J. and Morishita,K.
  TITLE     Fusion of the MLL gene with two different genes, AF-6 and
            AF-5alpha, by a complex translocation involving chromosomes 5, 6, 8
            and 11 in infant leukemia
  JOURNAL   Oncogene 13 (10), 2121-2130 (1996)
   PUBMED   8950979
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG502832.1, BG505115.1, BF211376.1, BC005400.1 and BC008504.1.
            
            On Mar 15, 2017 this sequence version replaced XP_016865187.1.
            
            Summary: CENPK is a subunit of a CENPH (MIM 605607)-CENPI (MIM
            300065)-associated centromeric complex that targets CENPA (MIM
            117139) to centromeres and is required for proper kinetochore
            function and mitotic progression (Okada et al., 2006 [PubMed
            16622420]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (4) differs in the 5' UTR, lacks a
            portion of the 5' coding region, initiates translation at a
            downstream start codon, and lacks an alternate in-frame exon in its
            central coding region, compared to variant 1. The encoded isoform
            (4) has a shorter N-terminus and lacks an internal segment compared
            to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.665842.1,
                                           SRR14243140.10948083.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..206
                     /product="centromere protein K isoform 4"
                     /note="leucine zipper protein FKSG14; SoxLZ/Sox6-binding
                     protein Solt; protein AF-5alpha; interphase centromere
                     complex protein 37"
                     /calculated_mol_wt=24100
     Region          1..206
                     /region_name="CENP-K"
                     /note="Centromere-associated protein K; pfam11802"
                     /db_xref="CDD:463355"
     CDS             1..206
                     /gene="CENPK"
                     /gene_synonym="AF5alpha; CENP-K; FKSG14; P33; Solt"
                     /coded_by="NM_001349368.2:255..875"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS87299.1"
                     /db_xref="GeneID:64105"
                     /db_xref="HGNC:HGNC:29479"
                     /db_xref="MIM:611502"
ORIGIN      
        1 mwkdmeecqn klsligtetl tdsnaqlsll imqvkcltae lsqwqkktpe tipltedvli
       61 tlgkeefqkl rqdlemvlst keskneklke dlerifnelk tkmlnikeyk ekllstlgef
      121 ledhfplpdr svkkkkkniq essvnlitlh emleilinrl fdvphdpyvk isdsfwppyv
      181 elllrngial rhpedptrir leafhq
//
LOCUS       NP_001372593            2219 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 9 [Homo sapiens].
ACCESSION   NP_001372593
VERSION     NP_001372593.1
DBSOURCE    REFSEQ: accession NM_001385664.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2219)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 2219)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2219)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2219)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2219)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 2219)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 2219)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 2219)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 2219)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 2219)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2219
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..2219
                     /product="microtubule-associated protein 4 isoform 9"
                     /note="MAP-4"
                     /calculated_mol_wt=237410
     Region          <1775..2024
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <2036..2057
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          2059..2088
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          2090..2119
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          2121..2151
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..2219
                     /gene="MAP4"
                     /coded_by="NM_001385664.1:103..6762"
                     /note="isoform 9 is encoded by transcript variant 128"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiegsptef leekmayqey pnsqnwpedt nfcfqpeqvv dpiqtdpfkm
      121 yhdddladlv fpssatadts ifagqndplk dsygmspcnt avvpqgwsve alnsphsesf
      181 vspeavaepp qptavplela keiemaseer ppaqaleimm glkttdmaps ketemalakd
      241 malatkteva lakdmesptk ldvtlakdmq psmesdmalv kdmelpteke valvkdvrwp
      301 tetdvssakn vvlpteteva pakdvtllke teraspikmd lapskdmgpp kenkketera
      361 spikmdlaps kdmgppkenk ivpakdlvll seievaqand iissteissa ekvalssete
      421 valardmtlp petnviltkd kalpleaeva pvkdmaqlpe teiapakdva pstvkevgll
      481 kdmsplsete malgkdvtpp petevvlikn vclppemeva ltedqvpalk teaplakdgv
      541 ltlannvtpa kdvpplsete atpvpikdme iaqtqkgise dshleslqdv gqsaaptfmi
      601 spetvtgtgk kcslpaeeds vleklgerkp cnsqpselss etsanfmycg tpptqakqvc
      661 rpsdrrstrp kparvppell ggsppwktld hrlghcslse sgwvsgsssc ggpgnqrksi
      721 hvdslepqrd lgreawdies tpimmkkkkk kpkqkrysqp raggpsdddn adkpkghpfa
      781 adtqksgvlp sqpttmgtey glvsgenlkr eclvnssaar lvaenfvses lriplypsee
      841 apktaissqs klrveeesks nksvlqnqdk kllkqheykp qpaphlktpv dksqsvgpln
      901 lkgplaevsa ynvetpldir lkegcspfld qevmgvvskp taakeipnlv ptliasnple
      961 cnlkegnnes kmtklqnvkl kefpegaeed kelkkeafpn erqeisifts eqlqgqvlvq
     1021 vpgvenepfk rmagdgksrk grgssgkmrt dsgkvkakse lpflldsqkd gravlipsep
     1081 vsktegmttq dkseelglns skqpgtkadl teavvmgepk emtqpkvagt mqaliplesg
     1141 sgmtqtsgvs tetgdvvkdm gvnnqskegr cpwkdheaap wisekpkkrg negkskkfkn
     1201 nystqparme rkeeilnppf egkdgdtgsi phkskeigft fpkmhdssfs htpdtptvea
     1261 vdrkggnfqv nfvelgtlge nkistvkast vteppakvtd vscqeqiqga gfvpsvvsee
     1321 nktdaanryt avadkpskrs ndgkskkvkn sspekhilen kidatkihvp mettgdqgie
     1381 gmaymdenrn itftcprtps elinkssple vlesaacekl ptptpqvvke gdsfpdtlak
     1441 ngqeiapaqi skslmvdnyt kdgvpgqerp kgpsavvpst stggvalpit taietvnihg
     1501 dhslknkael adsmkneagi deghvigese svhsgaskhs vekvtelakg hllpgvpved
     1561 qslpgearal egyadrgnfp ahpvneeket kegsvavqip dlledkaqkl sfcedqnaqd
     1621 rnskgsdsln kkvdltllsp ksendklkei slackitele svslptpeiq sdflhskvea
     1681 ppsevadtlv imtaskgvrl pepkdkilet pqkmtekses ktpgegkked ksrmaepmkg
     1741 ymrptksrgl tpllpkstiq eqerhkqlks agiarpeegr pvvsgtgndi ttppnkelpp
     1801 spekktkpla ttqpaktsts kaktqptslp kqpapttigg lnkkpmslas glvpaappkr
     1861 pavasarpsi lpskdvkpkp iadakapekr aspskpasap asrsgskstq tvaktttaaa
     1921 vastgpssrs pstllpkkpt aiktegkpae vkkmtaksvp adlsrpksts tssmkktttl
     1981 sgtapaagvv psrvkatpmp srpsttpfid kkptsakpss ttprlsrlat ntsapdlknv
     2041 rskvgsteni khqpgggrvq ivskkvsysh iqskcgskdn ikhvpgggnv qiqnkkvdis
     2101 kvsskcgska nikhkpgggd vkiesqklnf kekaqakvgs ldnvghlpag gavktegggs
     2161 eaplcpgppa geepaiseaa peagaptsas glnghptlsg ggdqreaqtl dsqiqetsi
//
LOCUS       NP_001166290             365 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphoglucomutase-1 isoform 3 [Homo sapiens].
ACCESSION   NP_001166290
VERSION     NP_001166290.1
DBSOURCE    REFSEQ: accession NM_001172819.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Liu,S., Deng,Y., Yu,Y. and Xia,X.
  TITLE     Knock-down of PGM1 inhibits cell viability, glycolysis, and
            oxidative phosphorylation in glioma under low glucose condition via
            the Myc signaling pathway
  JOURNAL   Biochem Biophys Res Commun 656, 38-45 (2023)
   PUBMED   36947965
  REMARK    GeneRIF: Knock-down of PGM1 inhibits cell viability, glycolysis,
            and oxidative phosphorylation in glioma under low glucose condition
            via the Myc signaling pathway.
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Stiers,K.M., Owuocha,L.F. and Beamer,L.J.
  TITLE     Effects of the T337M and G391V disease-related variants on human
            phosphoglucomutase 1: structural disruptions large and small
  JOURNAL   Acta Crystallogr F Struct Biol Commun 78 (Pt 5), 200-209 (2022)
   PUBMED   35506765
  REMARK    GeneRIF: Effects of the T337M and G391V disease-related variants on
            human phosphoglucomutase 1: structural disruptions large and small.
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Beamer,L.J.
  TITLE     Enzyme dysfunction at atomic resolution: Disease-associated
            variants of human phosphoglucomutase-1
  JOURNAL   Biochimie 183, 44-48 (2021)
   PUBMED   32898648
  REMARK    GeneRIF: Enzyme dysfunction at atomic resolution:
            Disease-associated variants of human phosphoglucomutase-1.
            Review article
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Conte,F., Morava,E., Bakar,N.A., Wortmann,S.B., Poerink,A.J.,
            Grunewald,S., Crushell,E., Al-Gazali,L., de Vries,M.C., Morkrid,L.,
            Hertecant,J., Brocke Holmefjord,K.S., Kronn,D., Feigenbaum,A.,
            Fingerhut,R., Wong,S.Y., van Scherpenzeel,M., Voermans,N.C. and
            Lefeber,D.J.
  TITLE     Phosphoglucomutase-1 deficiency: Early presentation, metabolic
            management and detection in neonatal blood spots
  JOURNAL   Mol Genet Metab 131 (1-2), 135-146 (2020)
   PUBMED   33342467
  REMARK    GeneRIF: Phosphoglucomutase-1 deficiency: Early presentation,
            metabolic management and detection in neonatal blood spots.
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Backe,P.H., Laerdahl,J.K., Kittelsen,L.S., Dalhus,B., Morkrid,L.
            and Bjoras,M.
  TITLE     Structural basis for substrate and product recognition in human
            phosphoglucomutase-1 (PGM1) isoform 2, a member of the
            alpha-D-phosphohexomutase superfamily
  JOURNAL   Sci Rep 10 (1), 5656 (2020)
   PUBMED   32221390
  REMARK    GeneRIF: Structural basis for substrate and product recognition in
            human phosphoglucomutase-1 (PGM1) isoform 2, a member of the
            alpha-D-phosphohexomutase superfamily.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 365)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
REFERENCE   7  (residues 1 to 365)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   8  (residues 1 to 365)
  AUTHORS   Whitehouse,D.B., Putt,W., Lovegrove,J.U., Morrison,K.,
            Hollyoake,M., Fox,M.F., Hopkinson,D.A. and Edwards,Y.H.
  TITLE     Phosphoglucomutase 1: complete human and rabbit mRNA sequences and
            direct mapping of this highly polymorphic marker on human
            chromosome 1
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 411-415 (1992)
   PUBMED   1530890
REFERENCE   9  (residues 1 to 365)
  AUTHORS   Drago,G.A., Hopkinson,D.A., Westwood,S.A. and Whitehouse,D.B.
  TITLE     Antigenic analysis of the major human phosphoglucomutase isozymes:
            PGM1, PGM2, PGM3 and PGM4
  JOURNAL   Ann Hum Genet 55 (4), 263-271 (1991)
   PUBMED   1840235
REFERENCE   10 (residues 1 to 365)
  AUTHORS   Herbich,J., Szilvassy,J. and Schnedl,W.
  TITLE     Gene localisation of the PGM1 enzyme system and the Duffy blood
            groups on chromosome No. 1 by means of a new fragile site at 1p31
  JOURNAL   Hum Genet 70 (2), 178-180 (1985)
   PUBMED   3159642
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK293298.1 and BC019920.1.
            
            Summary: The protein encoded by this gene is an isozyme of
            phosphoglucomutase (PGM) and belongs to the phosphohexose mutase
            family. There are several PGM isozymes, which are encoded by
            different genes and catalyze the transfer of phosphate between the
            1 and 6 positions of glucose. In most cell types, this PGM isozyme
            is predominant, representing about 90% of total PGM activity. In
            red cells, PGM2 is a major isozyme. This gene is highly
            polymorphic. Mutations in this gene cause glycogen storage disease
            type 14. Alternativley spliced transcript variants encoding
            different isoforms have been identified in this gene.[provided by
            RefSeq, Mar 2010].
            
            Transcript Variant: This variant (3) has an alternate 5' exon,
            which results in a downstream AUG start codon, as compared to
            variant 1. The resulting isoform (3) is shorter at the N-terminus,
            as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293298.1, AK298505.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145240, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..365
                     /product="phosphoglucomutase-1 isoform 3"
                     /EC_number="5.4.2.2"
                     /note="PGM 1; glucose phosphomutase 1"
                     /calculated_mol_wt=40152
     Region          <1..365
                     /region_name="phosphohexomutase"
                     /note="The alpha-D-phosphohexomutase superfamily includes
                     several related enzymes that catalyze a reversible
                     intramolecular phosphoryl transfer on their sugar
                     substrates. Members of this family include the
                     phosphoglucomutases (PGM1 and PGM2),
                     phosphoglucosamine...; cl38939"
                     /db_xref="CDD:476822"
     Site            order(96,139,160,162,179,181,183,306,308..310,318)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100087"
     CDS             1..365
                     /gene="PGM1"
                     /gene_synonym="CDG1T; GSD14"
                     /coded_by="NM_001172819.2:682..1779"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS53324.1"
                     /db_xref="GeneID:5236"
                     /db_xref="HGNC:HGNC:8905"
                     /db_xref="MIM:171900"
ORIGIN      
        1 mlrsifdfsa lkellsgpnr lkiridamhg vvgpyvkkil ceelgapans avncvpledf
       61 gghhpdpnlt yaadlvetmk sgehdfgaaf dgdgdrnmil gkhgffvnps dsvaviaani
      121 fsipyfqqtg vrgfarsmpt sgaldrvasa tkialyetpt gwkffgnlmd asklslcgee
      181 sfgtgsdhir ekdglwavla wlsilatrkq svedilkdhw qkygrnfftr ydyeeveaeg
      241 ankmmkdlea lmfdrsfvgk qfsandkvyt vekadnfeys dpvdgsisrn qglrliftdg
      301 srivfrlsgt gsagatirly idsyekdvak inqdpqvmla plisialkvs qlqertgrta
      361 ptvit
//
LOCUS       NP_001335413            1607 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 2 isoform e [Homo
            sapiens].
ACCESSION   NP_001335413 XP_016869502
VERSION     NP_001335413.1
DBSOURCE    REFSEQ: accession NM_001348484.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1607)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1607)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   3  (residues 1 to 1607)
  AUTHORS   Mechaussier,S., Almoallem,B., Zeitz,C., Van Schil,K., Jeddawi,L.,
            Van Dorpe,J., Duenas Rey,A., Condroyer,C., Pelle,O., Polak,M.,
            Boddaert,N., Bahi-Buisson,N., Cavallin,M., Bacquet,J.L.,
            Mouallem-Beziere,A., Zambrowski,O., Sahel,J.A., Audo,I., Kaplan,J.,
            Rozet,J.M., De Baere,E. and Perrault,I.
  TITLE     Loss of Function of RIMS2 Causes a Syndromic Congenital Cone-Rod
            Synaptic Disease with Neurodevelopmental and Pancreatic Involvement
  JOURNAL   Am J Hum Genet 106 (6), 859-871 (2020)
   PUBMED   32470375
  REMARK    GeneRIF: Loss of Function of RIMS2 Causes a Syndromic Congenital
            Cone-Rod Synaptic Disease with Neurodevelopmental and Pancreatic
            Involvement.
            Erratum:[Am J Hum Genet. 2020 Sep 3;107(3):580. doi:
            10.1016/j.ajhg.2020.08.004. PMID: 32888510]
REFERENCE   4  (residues 1 to 1607)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 1607)
  AUTHORS   Kim,K.T., Lee,J.S., Lee,B.W., Seok,H., Jeon,H.S., Kim,J.H. and
            Chung,J.H.
  TITLE     Association between regulating synaptic membrane exocytosis 2 gene
            polymorphisms and degenerative lumbar scoliosis
  JOURNAL   Biomed Rep 1 (4), 619-623 (2013)
   PUBMED   24648997
REFERENCE   6  (residues 1 to 1607)
  AUTHORS   Sun,L., Bittner,M.A. and Holz,R.W.
  TITLE     Rim, a component of the presynaptic active zone and modulator of
            exocytosis, binds 14-3-3 through its N terminus
  JOURNAL   J Biol Chem 278 (40), 38301-38309 (2003)
   PUBMED   12871946
REFERENCE   7  (residues 1 to 1607)
  AUTHORS   Fukuda,M.
  TITLE     Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and
            Noc2. Identification of a critical determinant of Rab3A/Rab27A
            recognition by Rim2
  JOURNAL   J Biol Chem 278 (17), 15373-15380 (2003)
   PUBMED   12578829
REFERENCE   8  (residues 1 to 1607)
  AUTHORS   Wang,Y. and Sudhof,T.C.
  TITLE     Genomic definition of RIM proteins: evolutionary amplification of a
            family of synaptic regulatory proteins
  JOURNAL   Genomics 81 (2), 126-137 (2003)
   PUBMED   12620390
REFERENCE   9  (residues 1 to 1607)
  AUTHORS   Kashima,Y., Miki,T., Shibasaki,T., Ozaki,N., Miyazaki,M., Yano,H.
            and Seino,S.
  TITLE     Critical role of cAMP-GEFII--Rim2 complex in incretin-potentiated
            insulin secretion
  JOURNAL   J Biol Chem 276 (49), 46046-46053 (2001)
   PUBMED   11598134
REFERENCE   10 (residues 1 to 1607)
  AUTHORS   Fenster,S.D., Chung,W.J., Zhai,R., Cases-Langhoff,C., Voss,B.,
            Garner,A.M., Kaempf,U., Kindler,S., Gundelfinger,E.D. and
            Garner,C.C.
  TITLE     Piccolo, a presynaptic zinc finger protein structurally related to
            bassoon
  JOURNAL   Neuron 25 (1), 203-214 (2000)
   PUBMED   10707984
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012213.8, AC007751.3,
            AC090686.4, AP001572.3, AC107933.6 and AP002849.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 6, 2017 this sequence version replaced XP_016869502.1.
            
            Summary: The protein encoded by this gene is a presynaptic protein
            that interacts with RAB3, a protein important for normal
            neurotransmitter release. The encoded protein can also bind several
            other synaptic proteins, including UNC-13 homolog B,
            ELKS/Rab6-interacting/CAST family member 1, and synaptotagmin 1.
            This protein is involved in synaptic membrane exocytosis.
            Polymorphisms in this gene have been associated with degenerative
            lumbar scoliosis. [provided by RefSeq, Feb 2017].
            
            Transcript Variant: This variant (5) encodes the longest isoform
            (e).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2157437,
                              SAMN03267754 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000696799.1/ ENSP00000512879.1
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1607
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..1607
                     /product="regulating synaptic membrane exocytosis protein
                     2 isoform e"
                     /note="RAB3 interacting protein 3; regulating synaptic
                     membrane exocytosis protein 2; nuclear protein; non-small
                     cell lung cancer RimL3a protein; non-small cell lung
                     cancer RimL3c protein; rab3-interacting molecule 2;
                     rab-3-interacting protein 3; rab-3-interacting molecule 2;
                     Rab3-interacting protein"
                     /calculated_mol_wt=181782
     Region          30..198
                     /region_name="PHD_SF"
                     /note="PHD finger superfamily; cl22851"
                     /db_xref="CDD:473978"
     Region          667..766
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(691..697,712,715,745,749,752..753)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          818..944
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(849,855,910,912,920)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          1438..1583
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(1495,1499..1500,1502,1505,1533,1535,1537,1581..1582)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..1607
                     /gene="RIMS2"
                     /gene_synonym="CRSDS; OBOE; RAB3IP3; RIM2"
                     /coded_by="NM_001348484.3:278..5101"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS94327.1"
                     /db_xref="GeneID:9699"
                     /db_xref="HGNC:HGNC:17283"
                     /db_xref="MIM:606630"
ORIGIN      
        1 msapvgprgr lapipaasqp plqpempdls hlteeerkii lavmdrqkke eekeqsvlkv
       61 keehkpqltq wfpfsgitel vnnvlqpqqk qqnekepqtk lhqqfemyke qvkkmgeesq
      121 qqqeqkgdap tcgichktkf adgcghncsy cqtkfcarcg grvslrsnke dkvvmwvcnl
      181 crkqqeiltk sgawfynsgs ntpqqpdqkv lrglrneeap qekkpklheq tqfqgpsgdl
      241 svpaveksrs hgltrqhsik ngsgvkhhia sdiasdrkrs psvsrdqnrr ydqreereey
      301 sqyatsdtam prspsdyadr rsqhepqfye dsdhlsyrds nrrshrhske yivddedves
      361 rdeyerqrre eeyqsryrsd pnlarypvkp qpyeeqmrih aevsrarher rhsdvslana
      421 dledsrisml rmdrpsrqrs iserraamen qrsysmertr eaqgpssyaq rttnhspptp
      481 rrsplpidrp dlrrtdslrk qhhldpssav rktkrekmet mlrndslssd qsesvrpppp
      541 kphkskkggk mrqislssse eelastpeyt scddveiese svsekgdsqk gkrktseqav
      601 lsdsntrser qkemmyfggh sleedlewse pqikdsgvdt cssttlneeh shsdkhpvtw
      661 qpskdgdrli grillnkrlk dgsvprdsga mlglkvvggk mtesgrlcaf itkvkkgsla
      721 dtvghlrpgd evlewngrll qgatfeevyn iileskpepq velvvsrpig dipripdsth
      781 aqlesssssf esqkmdrpsi svtspmspgm lrdvpqflsg qlsiklwfdk vghqlivtil
      841 gakdlpsred grprnpyvki yflpdrsdkn krrtktvkkt lepkwnqtfi yspvhrrefr
      901 ermleitlwd qarvreeese flgeiliele tallddephw yklqthdvss lplphpspym
      961 prrqlhgesp trrlqrskri sdsevsdydc ddgigvvsdy rhdgrdlqss tlsvpeqvms
     1021 snhcspsgsp hrvdvigrtr swspsvpppq srnveqglrg trtmtghynt isrmdrhrvm
     1081 ddhyspdrdr dceaadrqpy hrsrsteqrp llertttrsr sterpdtnlm rsmpslmtgr
     1141 sappspalsr shprtgsvqt spsstpvagr rgrqlpqlpp kgtldrkeld strrryagtm
     1201 dieernrqmk inkykqvags dprleqdyhs kyrsgwdphr gadnvstkss dsdvsdisav
     1261 srtssasrfs stsymsvqse rpggnkkisv ftskmqsrqm gisgknmtks tsisgdmcsl
     1321 ekndgsqsdt avgtlgtsgk krrsslgakm vaivglsrks rsasqlsqte aggkklrstv
     1381 qrstetglav emrnwmtrqa srestdgsmn syssegnlif pgvrlasdsq fsdfldglgp
     1441 aqlvgrqtla tpamgdiqvg mmdkkgqlev eiirarglvv kpgsktlpap yvkvylldng
     1501 vciakkktkv arktleplyq qllsfeespq gkvlqiivwg dygrmdhksf mgvaqillde
     1561 lelsnmvigw fklfppsslv dptlapltrr asqsslesst gpsysrs
//
LOCUS       NP_001350027             560 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger protein 250 isoform a [Homo sapiens].
ACCESSION   NP_001350027 XP_006716676
VERSION     NP_001350027.1
DBSOURCE    REFSEQ: accession NM_001363098.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   3  (residues 1 to 560)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 560)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 560)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   6  (residues 1 to 560)
  AUTHORS   Lorenz,P., Dietmann,S., Wilhelm,T., Koczan,D., Autran,S., Gad,S.,
            Wen,G., Ding,G., Li,Y., Rousseau-Merck,M.F. and Thiesen,H.J.
  TITLE     The ancient mammalian KRAB zinc finger gene cluster on human
            chromosome 8q24.3 illustrates principles of C2H2 zinc finger
            evolution associated with unique expression profiles in human
            tissues
  JOURNAL   BMC Genomics 11, 206 (2010)
   PUBMED   20346131
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 560)
  AUTHORS   Rual,J.F., Hirozane-Kishikawa,T., Hao,T., Bertin,N., Li,S.,
            Dricot,A., Li,N., Rosenberg,J., Lamesch,P., Vidalain,P.O.,
            Clingingsmith,T.R., Hartley,J.L., Esposito,D., Cheo,D., Moore,T.,
            Simmons,B., Sequerra,R., Bosak,S., Doucette-Stamm,L., Le Peuch,C.,
            Vandenhaute,J., Cusick,M.E., Albala,J.S., Hill,D.E. and Vidal,M.
  TITLE     Human ORFeome version 1.1: a platform for reverse proteomics
  JOURNAL   Genome Res 14 (10B), 2128-2135 (2004)
   PUBMED   15489335
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF235103.5, DA496584.1, BC017091.1, DB272357.1 and CA422363.1.
            
            On May 8, 2018 this sequence version replaced XP_006716676.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3127389.1,
                                           SRR1803615.40653.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..560
                     /product="zinc finger protein 250 isoform a"
                     /note="zinc finger protein 647; zinc finger protein (clone
                     647)"
                     /calculated_mol_wt=63337
     Region          22..82
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          178..537
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          201..221
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(206,208,210,212..213,216..217,220,234,236,240..241,
                     244..245,248,262,264,266,268..269,272..273,276)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          229..249
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          257..277
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          285..305
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          313..333
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          341..361
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          369..389
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          397..417
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          425..445
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          453..473
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          481..501
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(486,488,490,492..493,496..497,500,514,516,520..521,
                     524..525,528,542,544,546,548..549,552..553,556)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          509..529
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          537..557
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..560
                     /gene="ZNF250"
                     /gene_synonym="ZFP647; ZNF647"
                     /coded_by="NM_001363098.2:172..1854"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS34972.1"
                     /db_xref="GeneID:58500"
                     /db_xref="HGNC:HGNC:13044"
ORIGIN      
        1 maaarllpvp agpqplsfqa kltfedvavl lsqdewdrlc paqrglyrnv mmetygnvvs
       61 lglpgskpdi isqlergedp wvldrkgakk sqglwsdysd nlkydhttac tqqdslscpw
      121 ecetkgesqn tdlspkplis eqtvilgktp lgridqenne tkqsfclspn svdhrevqvl
      181 sqsmpltphq avpsgerpym cvecgkcfgr sshllqhqri htgekpyvcs vcgkafsqss
      241 vlskhrriht gekpyecnec gkafrvssdl aqhhkihtge kpheclecrk aftqlshliq
      301 hqrihtgerp yvcplcgkaf nhstvlrshq rvhtgekphr cnecgktfsv krtllqhqri
      361 htgekpytcs ecgkafsdrs vliqhhnvht gekpyecsec gktfshrstl mnherihtee
      421 kpyacyecgk afvqhshliq hqrvhtgekp yvcgecghaf sarrsliqhe rihtgekpfq
      481 ctecgkafsl katlivhlrt htgekpyecn scgkafsqys vliqhqriht gekpyecgec
      541 grafnqhghl iqhqkvhrkl
//
LOCUS       NP_001036216            1231 aa            linear   PRI 21-NOV-2025
DEFINITION  cohesin subunit SA-2 isoform b [Homo sapiens].
ACCESSION   NP_001036216
VERSION     NP_001036216.1
DBSOURCE    REFSEQ: accession NM_001042751.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1231)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1231)
  AUTHORS   Fischer,A., Hernandez-Rodriguez,B., Mulet-Lazaro,R., Nuetzel,M.,
            Holzl,F., van Herk,S., Kavelaars,F.G., Stanewsky,H., Ackermann,U.,
            Niang,A.H., Diaz,N., Reuschel,E., Strieder,N., Hernandez-Lopez,I.,
            Valk,P.J.M., Vaquerizas,J.M., Rehli,M., Delwel,R. and Gebhard,C.
  TITLE     STAG2 mutations reshape the cohesin-structured spatial chromatin
            architecture to drive gene regulation in acute myeloid leukemia
  JOURNAL   Cell Rep 43 (8), 114498 (2024)
   PUBMED   39084219
  REMARK    GeneRIF: STAG2 mutations reshape the cohesin-structured spatial
            chromatin architecture to drive gene regulation in acute myeloid
            leukemia.
REFERENCE   3  (residues 1 to 1231)
  AUTHORS   Huber,J., Tanasie,N.L., Zernia,S. and Stigler,J.
  TITLE     Single-molecule imaging reveals a direct role of CTCF's zinc
            fingers in SA interaction and cluster-dependent RNA recruitment
  JOURNAL   Nucleic Acids Res 52 (11), 6490-6506 (2024)
   PUBMED   38742641
  REMARK    GeneRIF: Single-molecule imaging reveals a direct role of CTCF's
            zinc fingers in SA interaction and cluster-dependent RNA
            recruitment.
REFERENCE   4  (residues 1 to 1231)
  AUTHORS   Xu,W., Kim,J.S., Yang,T., Ya,A., Sadzewicz,L., Tallon,L.,
            Harris,B.T., Sarkaria,J., Jin,F. and Waldman,T.
  TITLE     STAG2 mutations regulate 3D genome organization, chromatin loops,
            and Polycomb signaling in glioblastoma multiforme
  JOURNAL   J Biol Chem 300 (6), 107341 (2024)
   PUBMED   38705393
  REMARK    GeneRIF: STAG2 mutations regulate 3D genome organization, chromatin
            loops, and Polycomb signaling in glioblastoma multiforme.
REFERENCE   5  (residues 1 to 1231)
  AUTHORS   Ros-Pardo,D., Gomez-Puertas,P. and Marcos-Alcalde,I.
  TITLE     STAG2: Computational Analysis of Missense Variants Involved in
            Disease
  JOURNAL   Int J Mol Sci 25 (2), 1280 (2024)
   PUBMED   38279279
  REMARK    GeneRIF: STAG2: Computational Analysis of Missense Variants
            Involved in Disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1231)
  AUTHORS   Gregson,H.C., Schmiesing,J.A., Kim,J.S., Kobayashi,T., Zhou,S. and
            Yokomori,K.
  TITLE     A potential role for human cohesin in mitotic spindle aster
            assembly
  JOURNAL   J Biol Chem 276 (50), 47575-47582 (2001)
   PUBMED   11590136
REFERENCE   7  (residues 1 to 1231)
  AUTHORS   Sumara,I., Vorlaufer,E., Gieffers,C., Peters,B.H. and Peters,J.M.
  TITLE     Characterization of vertebrate cohesin complexes and their
            regulation in prophase
  JOURNAL   J Cell Biol 151 (4), 749-762 (2000)
   PUBMED   11076961
REFERENCE   8  (residues 1 to 1231)
  AUTHORS   Carramolino,L., Lee,B.C., Zaballos,A., Peled,A., Barthelemy,I.,
            Shav-Tal,Y., Prieto,I., Carmi,P., Gothelf,Y., Gonzalez de
            Buitrago,G., Aracil,M., Marquez,G., Barbero,J.L. and Zipori,D.
  TITLE     SA-1, a nuclear protein encoded by one member of a novel gene
            family: molecular cloning and detection in hemopoietic organs
  JOURNAL   Gene 195 (2), 151-159 (1997)
   PUBMED   9305759
  REMARK    Erratum:[Gene 1998 Jan 12;206(2):283]
REFERENCE   9  (residues 1 to 1231)
  AUTHORS   Wu,C., Friedlander,P., Lamoureux,C., Zannis-Hadjopoulos,M. and
            Price,G.B.
  TITLE     cDNA clones contain autonomous replication activity
  JOURNAL   Biochim Biophys Acta 1174 (3), 241-257 (1993)
   PUBMED   7690594
REFERENCE   10 (residues 1 to 1231)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA214149.1, BX641003.1,
            BC001765.1, CB250478.1, BC017095.1 and AA428995.1.
            
            Summary: The protein encoded by this gene is a subunit of the
            cohesin complex, which regulates the separation of sister
            chromatids during cell division. Targeted inactivation of this gene
            results in chromatid cohesion defects and aneuploidy, suggesting
            that genetic disruption of cohesin is a cause of aneuploidy in
            human cancer. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2013].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            lacks an in-frame coding exon compared to variant 1. The resulting
            isoform (b) is shorter, lacking an internal protein segment,
            compared to isoform a. Variants 3, 4 and 5 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX641003.1, SRR11853567.32276.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1231
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..1231
                     /product="cohesin subunit SA-2 isoform b"
                     /note="SCC3 homolog 2; cohesin subunit SA-2; SA2
                     stromalin; sister chromatid cohesion 3 homolog B; stromal
                     antigen 2"
                     /calculated_mol_wt=141196
     Region          1..75
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Region          102..>395
                     /region_name="IRR1"
                     /note="Cohesin [Cell division and chromosome
                     partitioning]; COG5537"
                     /db_xref="CDD:227824"
     Region          157..270
                     /region_name="STAG"
                     /note="STAG domain; pfam08514"
                     /db_xref="CDD:462502"
     Site            607
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1058
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1061
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Region          1064..1083
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1064
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35638; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1065
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35638; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1112
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     CDS             1..1231
                     /gene="STAG2"
                     /gene_synonym="bA517O1.1; HPE13; MKMS; NEDXCF; SA-2; SA2;
                     SCC3B"
                     /coded_by="NM_001042751.2:314..4009"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS14607.1"
                     /db_xref="GeneID:10735"
                     /db_xref="HGNC:HGNC:11355"
                     /db_xref="MIM:300826"
ORIGIN      
        1 miaapeiptd fnllqeseth fssdtdfedi egknqkqgkg ktckkgkkgp aekgkggngg
       61 gkppsgpnrm nghhqqngve nmmlfevvkm gksamqsvvd dwiesykhdr dialldlinf
      121 fiqcsgckgv vtaemfrhmq nseiirkmte efdedsgdyp ltmagpqwkk fkssfcefig
      181 vlvrqcqysi iydeymmdtv islltglsds qvrafrhtst laamklmtal vnvalnlsin
      241 mdntqrqyea ernkmigkra nerlelllqk rkelqenqde ienmmnaifk gvfvhryrda
      301 iaeiraicie eigiwmkmys daflndsylk yvgwtmhdkq gevrlkclta lqglyynkel
      361 nsklelftsr fkdrivsmtl dkeydvavqa iklltlvlqs seevltaedc envyhlvysa
      421 hrpvavaage flykklfsrr dpeedgmmkr rgrqgpnanl vktlvfffle selhehaayl
      481 vdsmwdcate llkdwecmns llleeplsge ealtdrqesa lieimlctir qaaechppvg
      541 rgtgkrvlta kekktqlddr tkitelfava lpqllakysv daekvtnllq lpqyfdleiy
      601 ttgrlekhld allrqirniv ekhtdtdvle acsktyhalc neeftifnrv disrsqlide
      661 ladkfnrlle dflqegeepd eddayqvlst lkritafhna hdlskwdlfa cnykllktgi
      721 engdmpeqiv ihalqcthyv ilwqlakite ssstkedllr lkkqmrvfcq icqhyltnvn
      781 ttvkeqafti lcdilmifsh qimsggrdml eplvytpdss lqsellsfil dhvfieqddd
      841 nnsadgqqed easkiealhk rrnllaafck livytvvemn taadifkqym kyyndygdii
      901 ketmsktrqi dkiqcaktli lslqqlfnem iqengynfdr ssstfsgike larrfaltfg
      961 ldqlktreai amlhkdgief afkepnpqge shpplnlafl dilsefsskl lrqdkrtvyv
     1021 ylekfmtfqm slrredvwlp lmsyrnslla ggdddtmsvi sgissrgstv rskkskpstg
     1081 krkvvegmql slteessssd smwlsreqtl htpvmmqtpq ltstimrepk rlrpedsfms
     1141 vypmqtehhq tpldynrrgt slmeddeepi vedvmmsseg riedlnegmd fdtmdidlpp
     1201 sknrrertel kpdffdpasi mdesvlgvsm f
//
LOCUS       NP_003176               1085 aa            linear   PRI 21-NOV-2025
DEFINITION  transcription initiation factor TFIID subunit 4 [Homo sapiens].
ACCESSION   NP_003176
VERSION     NP_003176.2
DBSOURCE    REFSEQ: accession NM_003185.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1085)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1085)
  AUTHORS   Janssen,B.D.E., van den Boogaard,M.H., Lichtenbelt,K., Seaby,E.G.,
            Stals,K., Ellard,S., Newbury-Ecob,R., Dixit,A., Roht,L.,
            Pajusalu,S., Ounap,K., Firth,H.V., Buckley,M., Wilson,M.,
            Roscioli,T., Tidwell,T., Mao,R., Ennis,S., Holwerda,S.J., van
            Gassen,K. and van Jaarsveld,R.H.
  TITLE     De novo putative loss-of-function variants in TAF4 are associated
            with a neuro-developmental disorder
  JOURNAL   Hum Mutat 43 (12), 1844-1851 (2022)
   PUBMED   35904126
  REMARK    GeneRIF: De novo putative loss-of-function variants in TAF4 are
            associated with a neuro-developmental disorder.
REFERENCE   3  (residues 1 to 1085)
  AUTHORS   Friis Theisen,F., Salladini,E., Davidsen,R., Jo Rasmussen,C.,
            Staby,L., Kragelund,B.B. and Skriver,K.
  TITLE     alphaalpha-hub coregulator structure and flexibility determine
            transcription factor binding and selection in regulatory
            interactomes
  JOURNAL   J Biol Chem 298 (6), 101963 (2022)
   PUBMED   35452682
  REMARK    GeneRIF: alphaalpha-hub coregulator structure and flexibility
            determine transcription factor binding and selection in regulatory
            interactomes.
REFERENCE   4  (residues 1 to 1085)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 1085)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1085)
  AUTHORS   Mengus,G., May,M., Jacq,X., Staub,A., Tora,L., Chambon,P. and
            Davidson,I.
  TITLE     Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28:
            three subunits of the human transcription factor TFIID
  JOURNAL   EMBO J 14 (7), 1520-1531 (1995)
   PUBMED   7729427
REFERENCE   7  (residues 1 to 1085)
  AUTHORS   Parada,C.A., Yoon,J.B. and Roeder,R.G.
  TITLE     A novel LBP-1-mediated restriction of HIV-1 transcription at the
            level of elongation in vitro
  JOURNAL   J Biol Chem 270 (5), 2274-2283 (1995)
   PUBMED   7836461
REFERENCE   8  (residues 1 to 1085)
  AUTHORS   Zhou,Q. and Sharp,P.A.
  TITLE     Novel mechanism and factor for regulation by HIV-1 Tat
  JOURNAL   EMBO J 14 (2), 321-328 (1995)
   PUBMED   7835343
REFERENCE   9  (residues 1 to 1085)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   10 (residues 1 to 1085)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL137077.31 and AL109911.47.
            
            On Jul 28, 2006 this sequence version replaced NP_003176.1.
            
            Summary: Initiation of transcription by RNA polymerase II requires
            the activities of more than 70 polypeptides. The protein that
            coordinates these activities is transcription factor IID (TFIID),
            which binds to the core promoter to position the polymerase
            properly, serves as the scaffold for assembly of the remainder of
            the transcription complex, and acts as a channel for regulatory
            signals. TFIID is composed of the TATA-binding protein (TBP) and a
            group of evolutionarily conserved proteins known as TBP-associated
            factors or TAFs. TAFs may participate in basal transcription, serve
            as coactivators, function in promoter recognition or modify general
            transcription factors (GTFs) to facilitate complex assembly and
            transcription initiation. This gene encodes one of the larger
            subunits of TFIID that has been shown to potentiate transcriptional
            activation by retinoic acid, thyroid hormone and vitamin D3
            receptors. In addition, this subunit interacts with the
            transcription factor CREB, which has a glutamine-rich activation
            domain, and binds to other proteins containing glutamine-rich
            regions. Aberrant binding to this subunit by proteins with expanded
            polyglutamine regions has been suggested as one of the pathogenetic
            mechanisms underlying a group of neurodegenerative disorders
            referred to as polyglutamine diseases. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y11354.1, SRR18074969.1800770.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000252996.9/ ENSP00000252996.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1085
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..1085
                     /product="transcription initiation factor TFIID subunit 4"
                     /note="TATA box binding protein (TBP)-associated factor,
                     RNA polymerase II, C1, 130kD; TAF4A RNA polymerase II,
                     TATA box binding protein (TBP)-associated factor, 135 kD;
                     transcription initiation factor TFIID 135 kD subunit;
                     TBP-associated factor 4; RNA polymerase II TBP-associated
                     factor subunit C; transcription initiation factor TFIID
                     135 kDa subunit; transcription initiation factor TFIID 130
                     kDa subunit; TAF4 RNA polymerase II, TATA box binding
                     protein (TBP)-associated factor, 135kDa"
                     /calculated_mol_wt=109984
     Region          66..204
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00268.2)"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00268.2)"
     Region          243..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00268.2)"
     Region          383..425
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00268.2)"
     Site            424
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (O00268.2)"
     Site            435
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (O00268.2)"
     Region          479..499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00268.2)"
     Region          566..586
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00268.2)"
     Region          592..675
                     /region_name="TAFH"
                     /note="NHR1 homology to TAF; pfam07531"
                     /db_xref="CDD:462195"
     Site            594
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0007744|PDB:2P6V; propagated from
                     UniProtKB/Swiss-Prot (O00268.2)"
     Site            595
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0007744|PDB:2P6V; propagated from
                     UniProtKB/Swiss-Prot (O00268.2)"
     Site            597
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0007744|PDB:2P6V; propagated from
                     UniProtKB/Swiss-Prot (O00268.2)"
     Site            605
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0007744|PDB:2P6V; propagated from
                     UniProtKB/Swiss-Prot (O00268.2)"
     Site            611
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0007744|PDB:2P6V; propagated from
                     UniProtKB/Swiss-Prot (O00268.2)"
     Site            621
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0007744|PDB:2P6V; propagated from
                     UniProtKB/Swiss-Prot (O00268.2)"
     Site            631
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0007744|PDB:2P6V; propagated from
                     UniProtKB/Swiss-Prot (O00268.2)"
     Site            658
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0007744|PDB:2P6V; propagated from
                     UniProtKB/Swiss-Prot (O00268.2)"
     Region          834..1082
                     /region_name="TAF4"
                     /note="Transcription initiation factor TFIID component
                     TAF4 family; pfam05236"
                     /db_xref="CDD:461598"
     Region          870..913
                     /region_name="Minimal region required to interact with
                     TAF12. /evidence=ECO:0000269|PubMed:10594036"
                     /note="propagated from UniProtKB/Swiss-Prot (O00268.2)"
     Region          1015..1049
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00268.2)"
     CDS             1..1085
                     /gene="TAF4"
                     /gene_synonym="MRD73; TAF(II)130; TAF(II)135; TAF2C;
                     TAF2C1; TAF4A; TAFII-130; TAFII-135; TAFII130; TAFII135"
                     /coded_by="NM_003185.4:72..3329"
                     /db_xref="CCDS:CCDS33500.1"
                     /db_xref="GeneID:6874"
                     /db_xref="HGNC:HGNC:11537"
                     /db_xref="MIM:601796"
ORIGIN      
        1 maagsdllde vffnsevdek vvsdlvgsle sqlaasaahh hhlaprtpev raaaagalgn
       61 hvvsgspaga agagpaapae gapgaapepp pagrarpggg gpqrpgppsp rrplvpagpa
      121 ppaaklrppp egsagscapv paaaavaagp epapagpakp agpaalaara gpgpgpgpgp
      181 gpgpgpgkpa gpgaaqtlng saallnshha aapavslvnn gpaallplpk paapgtviqt
      241 ppfvgaaapp apaapsppaa papaapaaap pppppapatl arppghpagp ptaapavppp
      301 aaaqnggsag aapapapaag gpagvsgqpg pgaaaaapap gvkaespkrv vqaappaaqt
      361 laasgpasta asmvigptmq galpspaavp ppapgtptgl pkgaagavtq slsrtptatt
      421 sgiratltpt vlaprlpqpp qnptniqnfq lppgmvlvrs engqllmipq qalaqmqaqa
      481 haqpqttmap rpatptsapp vqistvqapg tpiiarqvtp ttiikqvsqa qttvqpsatl
      541 qrspgvqpql vlggaaqtas lgtatavqtg tpqrtvpgat ttssaatetm envkkcknfl
      601 stliklassg kqstetaanv kelvqnlldg kieaedftsr lyrelnsspq pylvpflkrs
      661 lpalrqltpd saafiqqsqq qpppptsqat taltavvlss svqrtagkta atvtsalqpp
      721 vlsltqptqv gvgkqgqptp lviqqppkpg alirppqvtl tqtpmvalrq phnrimlttp
      781 qqiqlnplqp vpvvkpavlp gtkalsavsa qaaaaqknkl kepgggsfrd dddindvasm
      841 agvnlseesa rilatnselv gtltrsckde tfllqaplqr rileigkkhg itelhpdvvs
      901 yvshatqqrl qnlvekiset aqqknfsykd ddryeqasdv raqlkffeql dqiekqrkde
      961 qereilmraa ksrsrqedpe qlrlkqkake mqqqelaqmr qrdanltala aigprkkrkv
     1021 dcpgpgsgae gsgpgsvvpg ssgvgtprqf trqritrvnl rdlifclene retshsllly
     1081 kaflk
//
LOCUS       NP_001363271             810 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger CCCH domain-containing protein 11A isoform 1 [Homo
            sapiens].
ACCESSION   NP_001363271 XP_011508501
VERSION     NP_001363271.1
DBSOURCE    REFSEQ: accession NM_001376342.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Kases,K., Schubert,E., Hajikhezri,Z., Larsson,M., Devi,P.,
            Darweesh,M., Andersson,L., Akusjarvi,G., Punga,T. and Younis,S.
  TITLE     The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts
  JOURNAL   J Biol Chem 299 (8), 104959 (2023)
   PUBMED   37356722
  REMARK    GeneRIF: The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts.
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 810)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 810)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114402.2.
            
            On Nov 14, 2019 this sequence version replaced XP_011508501.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR627439.1, SRR7346977.2704948.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367210.3/ ENSP00000356179.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..810
                     /product="zinc finger CCCH domain-containing protein 11A
                     isoform 1"
                     /note="zinc finger CCCH-type domain containing 11A; zinc
                     finger CCCH domain-containing protein 11A"
                     /calculated_mol_wt=89000
     Region          1..110
                     /region_name="zf-CCCH_3"
                     /note="Zinc-finger containing family; pfam15663"
                     /db_xref="CDD:464787"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          139..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          223..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          285..351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          367..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          482..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          715..768
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     CDS             1..810
                     /gene="ZC3H11A"
                     /gene_synonym="ZC3HDC11A"
                     /coded_by="NM_001376342.1:1760..4192"
                     /note="isoform 1 is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS30978.1"
                     /db_xref="GeneID:9877"
                     /db_xref="HGNC:HGNC:29093"
                     /db_xref="MIM:613513"
ORIGIN      
        1 mpnqgedcyf ffystctkgd scpfrhceaa ignetvctlw qegrcfrqvc rfrhmeidkk
       61 rseipcywen qptgcqklnc afhhnrgryv dglflppskt vlptvpespe eevkasqlsv
      121 qqnklsvqsn pspqlrsvmk vessenvpsp thppvvinaa dddeddddqf seegdetktp
      181 tlqptpevhn glrvtsvrkp avnikqgecl nfgiktleei kskkmkeksk kqgegssgvs
      241 slllhpepvp gpekenvrtv vrtvtlstkq geeplvrlsl terlgkrkfs aggdsdpplk
      301 rslaqrlgkk veapetnidk tpkkaqvsks lkerlgmsad pdnedatdkv nkvgeihvkt
      361 leeilleras qkrgelqtkl ktegpsktdd stsgarssst iriktfsevl aekkhrqqea
      421 erqkskkdtt ciklkidsei kktvvlppiv asrgqseepa gktksmqevh iktleeikle
      481 kalrvqqsse sstsspsqhe atpgarrllr itkrtgmkee knlqegnevd sqssirteak
      541 easgettgvd itkiqvkrce tmrekhmqkq qereksvltp lrgdvascnt qvaekpvlta
      601 vpgitrhltk rlptkssqkv evetsgigds llnvkcaaqt lekrgkakpk vnvkpsvvkv
      661 vsspklapkr kavemhaavi aavkplssss vlqeppakka avavvplvse dksvtvpeae
      721 nprdslvlpp tqsssdsspp evsgpsssqm smktrrlssa stgkpplsve ddfekliwei
      781 sggkleaeid ldpgkdeddl llelsemids
//
LOCUS       NP_006295                 70 aa            linear   PRI 21-NOV-2025
DEFINITION  26S proteasome complex subunit SEM1 isoform c [Homo sapiens].
ACCESSION   NP_006295
VERSION     NP_006295.1
DBSOURCE    REFSEQ: accession NM_006304.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 70)
  AUTHORS   Huang,Y., Li,W., Foo,T., Ji,J.H., Wu,B., Tomimatsu,N., Fang,Q.,
            Gao,B., Long,M., Xu,J., Maqbool,R., Mukherjee,B., Ni,T., Alejo,S.,
            He,Y., Burma,S., Lan,L., Xia,B. and Zhao,W.
  TITLE     DSS1 restrains BRCA2's engagement with dsDNA for homologous
            recombination, replication fork protection, and R-loop homeostasis
  JOURNAL   Nat Commun 15 (1), 7081 (2024)
   PUBMED   39152168
  REMARK    GeneRIF: DSS1 restrains BRCA2's engagement with dsDNA for
            homologous recombination, replication fork protection, and R-loop
            homeostasis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 70)
  AUTHORS   Li,C., Chen,B., Zhang,J., Yang,J., Guo,M., Ren,Y., Zhou,Z.,
            Fung,K.M., Li,M., Zhang,L. and Liu,Z.
  TITLE     SEM1 promotes tumor progression of glioblastoma via activating the
            akt signaling pathway
  JOURNAL   Cancer Lett 577, 216368 (2023)
   PUBMED   37652287
  REMARK    GeneRIF: SEM1 promotes tumor progression of glioblastoma via
            activating the akt signaling pathway.
REFERENCE   3  (residues 1 to 70)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   4  (residues 1 to 70)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   5  (residues 1 to 70)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 70)
  AUTHORS   Marston,N.J., Richards,W.J., Hughes,D., Bertwistle,D.,
            Marshall,C.J. and Ashworth,A.
  TITLE     Interaction between the product of the breast cancer susceptibility
            gene BRCA2 and DSS1, a protein functionally conserved from yeast to
            mammals
  JOURNAL   Mol Cell Biol 19 (7), 4633-4642 (1999)
   PUBMED   10373512
REFERENCE   7  (residues 1 to 70)
  AUTHORS   Jantti,J., Lahdenranta,J., Olkkonen,V.M., Soderlund,H. and
            Keranen,S.
  TITLE     SEM1, a homologue of the split hand/split foot malformation
            candidate gene Dss1, regulates exocytosis and pseudohyphal
            differentiation in yeast
  JOURNAL   Proc Natl Acad Sci U S A 96 (3), 909-914 (1999)
   PUBMED   9927667
REFERENCE   8  (residues 1 to 70)
  AUTHORS   Crackower,M.A., Scherer,S.W., Rommens,J.M., Hui,C.C., Poorkaj,P.,
            Soder,S., Cobben,J.M., Hudgins,L., Evans,J.P. and Tsui,L.C.
  TITLE     Characterization of the split hand/split foot malformation locus
            SHFM1 at 7q21.3-q22.1 and analysis of a candidate gene for its
            expression during limb development
  JOURNAL   Hum Mol Genet 5 (5), 571-579 (1996)
   PUBMED   8733122
REFERENCE   9  (residues 1 to 70)
  AUTHORS   Roberts,S.H., Hughes,H.E., Davies,S.J. and Meredith,A.L.
  TITLE     Bilateral split hand and split foot malformation in a boy with a de
            novo interstitial deletion of 7q21.3
  JOURNAL   J Med Genet 28 (7), 479-481 (1991)
   PUBMED   1895319
REFERENCE   10 (residues 1 to 70)
  AUTHORS   Sharland,M., Patton,M.A. and Hill,L.
  TITLE     Ectrodactyly of hands and feet in a child with a complex
            translocation including 7q21.2
  JOURNAL   Am J Med Genet 39 (4), 413-414 (1991)
   PUBMED   1877619
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U41515.1 and AC073230.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The product of this gene has been localized within the
            split hand/split foot malformation locus SHFM1 at chromosome 7. It
            has been proposed to be a candidate gene for the autosomal dominant
            form of the heterogeneous limb developmental disorder split
            hand/split foot malformation type 1. In addition, it has been shown
            to directly interact with BRCA2. It also may play a role in the
            completion of the cell cycle. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HY170996.1, CB110705.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2154405
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000248566.4/ ENSP00000248566.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.3"
     Protein         1..70
                     /product="26S proteasome complex subunit SEM1 isoform c"
                     /note="deleted in split-hand/split-foot 1; SEM1 26S
                     proteasome complex subunit; 26S proteasome complex subunit
                     DSS1; split hand/foot malformation (ectrodactyly) type 1;
                     split hand/foot deleted protein 1; deleted in split
                     hand/split foot protein 1; split hand/foot malformation
                     type 1 protein; 26S proteasome complex subunit SEM1"
                     /calculated_mol_wt=8146
     Region          <23..62
                     /region_name="DSS1_SEM1"
                     /note="DSS1/SEM1 family; pfam05160"
                     /db_xref="CDD:461563"
     CDS             1..70
                     /gene="SEM1"
                     /gene_synonym="C7orf76; DSS1; ECD; PSMD15; SHFD1; Shfdg1;
                     SHFM1; SHSF1"
                     /coded_by="NM_006304.2:84..296"
                     /note="isoform c is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS5646.1"
                     /db_xref="GeneID:7979"
                     /db_xref="HGNC:HGNC:10845"
                     /db_xref="MIM:601285"
ORIGIN      
        1 msekkqpvdl glleeddefe efpaedwagl dededahvwe dnwdddnved dfsnqlrael
       61 ekhgykmets
//
LOCUS       NP_004371               2442 aa            linear   PRI 21-NOV-2025
DEFINITION  CREB-binding protein isoform a [Homo sapiens].
ACCESSION   NP_004371
VERSION     NP_004371.2
DBSOURCE    REFSEQ: accession NM_004380.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2442)
  AUTHORS   Shahib,A.K., Rastegar,M., van Wijnen,A.J. and Davie,J.R.
  TITLE     Neurodevelopmental functions and activities of the KAT3 class of
            lysine acetyltransferases
  JOURNAL   Biochem Cell Biol 102 (6), 430-447 (2024)
   PUBMED   39293094
  REMARK    Review article
REFERENCE   2  (residues 1 to 2442)
  AUTHORS   Sardar,S., McNair,C.M., Ravindranath,L., Chand,S.N., Yuan,W.,
            Bogdan,D., Welti,J., Sharp,A., Ryan,N.K., Knudsen,L.A.,
            Schiewer,M.J., DeArment,E.G., Janas,T., Su,X.A., Butler,L.M., de
            Bono,J.S., Frese,K., Brooks,N., Pegg,N., Knudsen,K.E. and
            Shafi,A.A.
  TITLE     AR coactivators, CBP/p300, are critical mediators of DNA repair in
            prostate cancer
  JOURNAL   Oncogene 43 (43), 3197-3213 (2024)
   PUBMED   39266679
  REMARK    GeneRIF: AR coactivators, CBP/p300, are critical mediators of DNA
            repair in prostate cancer.
REFERENCE   3  (residues 1 to 2442)
  AUTHORS   Yuan,X., Hao,X., Chan,H.L., Zhao,N., Pedroza,D.A., Liu,F., Le,K.,
            Smith,A.J., Calderon,S.J., Lieu,N., Soth,M.J., Jones,P., Zhang,X.H.
            and Rosen,J.M.
  TITLE     CREB-binding protein/P300 bromodomain inhibition reduces neutrophil
            accumulation and activates antitumor immunity in triple-negative
            breast cancer
  JOURNAL   JCI Insight 9 (20), e182621 (2024)
   PUBMED   39287984
  REMARK    GeneRIF: CREB-binding protein/P300 bromodomain inhibition reduces
            neutrophil accumulation and activates antitumor immunity in
            triple-negative breast cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2442)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   5  (residues 1 to 2442)
  AUTHORS   Ebrahimi,A., Waha,A., Schittenhelm,J., Gohla,G., Schuhmann,M.U. and
            Pietsch,T.
  TITLE     BCOR::CREBBP fusion in malignant neuroepithelial tumor of CNS
            expands the spectrum of methylation class CNS tumor with
            BCOR/BCOR(L1)-fusion
  JOURNAL   Acta Neuropathol Commun 12 (1), 60 (2024)
   PUBMED   38637838
  REMARK    GeneRIF: BCOR::CREBBP fusion in malignant neuroepithelial tumor of
            CNS expands the spectrum of methylation class CNS tumor with
            BCOR/BCOR(L1)-fusion.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2442)
  AUTHORS   Petrij,F., Giles,R.H., Dauwerse,H.G., Saris,J.J., Hennekam,R.C.,
            Masuno,M., Tommerup,N., van Ommen,G.J., Goodman,R.H., Peters,D.J.
            et al.
  TITLE     Rubinstein-Taybi syndrome caused by mutations in the
            transcriptional co-activator CBP
  JOURNAL   Nature 376 (6538), 348-351 (1995)
   PUBMED   7630403
REFERENCE   7  (residues 1 to 2442)
  AUTHORS   Chen,X.N. and Korenberg,J.R.
  TITLE     Localization of human CREBBP (CREB binding protein) to 16p13.3 by
            fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 71 (1), 56-57 (1995)
   PUBMED   7606928
REFERENCE   8  (residues 1 to 2442)
  AUTHORS   Stevens,C.A.
  TITLE     Rubinstein-Taybi Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301699
REFERENCE   9  (residues 1 to 2442)
  AUTHORS   Lacombe,D., Saura,R., Taine,L. and Battin,J.
  TITLE     Confirmation of assignment of a locus for Rubinstein-Taybi syndrome
            gene to 16p13.3
  JOURNAL   Am J Med Genet 44 (1), 126-128 (1992)
   PUBMED   1519642
REFERENCE   10 (residues 1 to 2442)
  AUTHORS   Benbrook,D.M. and Jones,N.C.
  TITLE     Heterodimer formation between CREB and JUN proteins
  JOURNAL   Oncogene 5 (3), 295-302 (1990)
   PUBMED   2138276
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U85962.3, AB210043.1 and
            AC006111.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 25, 2006 this sequence version replaced NP_004371.1.
            
            Summary: This gene is ubiquitously expressed and is involved in the
            transcriptional coactivation of many different transcription
            factors. First isolated as a nuclear protein that binds to
            cAMP-response element binding protein (CREB), this gene is now
            known to play critical roles in embryonic development, growth
            control, and homeostasis by coupling chromatin remodeling to
            transcription factor recognition. The protein encoded by this gene
            has intrinsic histone acetyltransferase activity and also acts as a
            scaffold to stabilize additional protein interactions with the
            transcription complex. This protein acetylates both histone and
            non-histone proteins. This protein shares regions of very high
            sequence similarity with protein p300 in its bromodomain,
            cysteine-histidine-rich regions, and histone acetyltransferase
            domain. Mutations in this gene cause Rubinstein-Taybi syndrome
            (RTS). Chromosomal translocations involving this gene have been
            associated with acute myeloid leukemia. Alternative splicing
            results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Feb 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer protein (isoform a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U85962.3, SRR14038196.3158172.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262367.10/ ENSP00000262367.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2442
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..2442
                     /product="CREB-binding protein isoform a"
                     /EC_number="2.3.1.48"
                     /note="histone lysine acetyltransferase CREBBP;
                     protein-lysine acetyltransferase CREBBP; protein
                     lactyltransferas CREBBP; CREB-binding protein"
                     /calculated_mol_wt=265221
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Site            29..30
                     /site_type="other"
                     /note="Breakpoint for translocation to form KAT6B-CREBBP;
                     propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Region          74..179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000269|PubMed:38128537; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Site            220
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Region          227..410
                     /region_name="Interaction with SRCAP.
                     /evidence=ECO:0000269|PubMed:10347196"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Region          266..290
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Site            266..267
                     /site_type="other"
                     /note="Breakpoint for translocation to form KAT6A-CREBBP;
                     propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Region          363..430
                     /region_name="zf-TAZ"
                     /note="TAZ zinc finger; pfam02135"
                     /db_xref="CDD:460457"
     Region          587..667
                     /region_name="KIX"
                     /note="KIX domain; pfam02172"
                     /db_xref="CDD:366953"
     Site            601
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P45481; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Site            625
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P45481; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Site            657
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P45481; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Region          <683..1025
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          794..1083
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Site            1014
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Site            1030
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Site            1076
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Region          1087..1194
                     /region_name="Bromo_cbp_like"
                     /note="Bromodomain, cbp_like subfamily. Cbp (CREB binding
                     protein or CREBBP) is an acetyltransferase acting on
                     histone, which gives a specific tag for transcriptional
                     activation and also acetylates non-histone proteins.
                     CREBBP binds specifically to...; cd05495"
                     /db_xref="CDD:99927"
     Site            order(1115,1122,1125,1164,1168,1174)
                     /site_type="active"
                     /note="acetyllysine binding site [active]"
                     /db_xref="CDD:99927"
     Region          1124..1170
                     /region_name="Interaction with histone.
                     /evidence=ECO:0000269|PubMed:24361270"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Region          1162..1180
                     /region_name="Interaction with ASF1A.
                     /evidence=ECO:0000269|PubMed:24616510"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Region          1206..1278
                     /region_name="RING_CBP-p300"
                     /note="atypical RING domain found in CREB-binding protein
                     and p300 histone acetyltransferases; cd15802"
                     /db_xref="CDD:276805"
     Site            order(1206,1209..1210,1276,1278)
                     /site_type="other"
                     /note="HAT interface [polypeptide binding]"
                     /db_xref="CDD:276805"
     Site            1216
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Region          1280..1311
                     /region_name="PHD_CBP_p300"
                     /note="PHD finger found in CREB-binding protein (CBP) and
                     histone acetyltransferase p300; cd15557"
                     /db_xref="CDD:277032"
     Site            order(1280..1283,1287,1306)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277032"
     Region          1342..1649
                     /region_name="HAT_KAT11"
                     /note="Histone acetylation protein; pfam08214"
                     /db_xref="CDD:400497"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKA.
                     /evidence=ECO:0000269|PubMed:17434128; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Site            1386
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKA.
                     /evidence=ECO:0000269|PubMed:17434128; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Region          1433..1435
                     /region_name="Interaction with histone.
                     /evidence=ECO:0000250|UniProtKB:Q09472"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Region          1460..1891
                     /region_name="Interaction with TRERF1.
                     /evidence=ECO:0000269|PubMed:11349124"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Region          1556..1615
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Site            1583
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Site            1591
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Site            1592
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Site            1595
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Site            1597
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Region          1705..1745
                     /region_name="ZZ_CBP"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     CBP/p300 and related proteins. The ZZ motif coordinates
                     two zinc ions and most likely participates in ligand
                     binding or molecular scaffolding. CREB-binding protein
                     (CBP) is a large multidomain protein that...; cd02337"
                     /db_xref="CDD:239077"
     Site            order(1707,1710,1720,1723,1729,1732,1738,1740)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239077"
     Site            order(1707,1710,1729,1732)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239077"
     Site            order(1708,1717,1719,1725,1727)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239077"
     Site            order(1718,1733,1742,1745)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239077"
     Site            order(1720,1723,1738,1740)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239077"
     Site            1741
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Site            1744
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Site            1763
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Region          1772..1840
                     /region_name="zf-TAZ"
                     /note="TAZ zinc finger; pfam02135"
                     /db_xref="CDD:460457"
     Region          1874..1959
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Region          1960..>2423
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          1977..2028
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Region          2013..2114
                     /region_name="Creb_binding"
                     /note="Creb binding; pfam09030"
                     /db_xref="CDD:462659"
     Site            2063
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Site            2076
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Site            2079
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     Region          2112..2263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Region          2294..2433
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92793.3)"
     Site            2351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P45481; propagated from
                     UniProtKB/Swiss-Prot (Q92793.3)"
     CDS             1..2442
                     /gene="CREBBP"
                     /gene_synonym="CBP; KAT3A; MKHK1; RSTS; RSTS1"
                     /coded_by="NM_004380.3:798..8126"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10509.1"
                     /db_xref="GeneID:1387"
                     /db_xref="HGNC:HGNC:2348"
                     /db_xref="MIM:600140"
ORIGIN      
        1 maenlldgpp npkraklssp gfsandstdf gslfdlendl pdelipngge lgllnsgnlv
       61 pdaaskhkql sellrggsgs sinpgignvs asspvqqglg gqaqgqpnsa nmaslsamgk
      121 splsqgdssa pslpkqaast sgptpaasqa lnpqaqkqvg latsspatsq tgpgicmnan
      181 fnqthpglln snsghslinq asqgqaqvmn gslgaagrgr gagmpyptpa mqgasssvla
      241 etltqvspqm tghaglntaq aggmakmgit gntspfgqpf sqaggqpmga tgvnpqlask
      301 qsmvnslptf ptdikntsvt nvpnmsqmqt svgivptqai atgptadpek rkliqqqlvl
      361 llhahkcqrr eqangevrac slphcrtmkn vlnhmthcqa gkacqvahca ssrqiishwk
      421 nctrhdcpvc lplknasdkr nqqtilgspa sgiqntigsv gtgqqnatsl snpnpidpss
      481 mqrayaalgl pymnqpqtql qpqvpgqqpa qpqthqqmrt lnplgnnpmn ipaggittdq
      541 qppnlisesa lptslgatnp lmndgsnsgn igtlstipta appsstgvrk gwhehvtqdl
      601 rshlvhklvq aifptpdpaa lkdrrmenlv ayakkvegdm yesansrdey yhllaekiyk
      661 iqkeleekrr srlhkqgilg nqpalpapga qppvipqaqp vrppngplsl pvnrmqvsqg
      721 mnsfnpmslg nvqlpqapmg praaspmnhs vqmnsmgsvp gmaispsrmp qppnmmgaht
      781 nnmmaqapaq sqflpqnqfp sssgamsvgm gqppaqtgvs qgqvpgaalp nplnmlgpqa
      841 sqlpcppvtq splhptpppa staagmpslq httppgmtpp qpaaptqpst pvsssgqtpt
      901 ptpgsvpsat qtqstptvqa aaqaqvtpqp qtpvqppsva tpqssqqqpt pvhaqppgtp
      961 lsqaaasidn rvptpssvas aetnsqqpgp dvpvlemkte tqaedtepdp geskgeprse
     1021 mmeedlqgas qvkeetdiae qksepmevde kkpevkvevk eeeesssngt asqstspsqp
     1081 rkkifkpeel rqalmptlea lyrqdpeslp frqpvdpqll gipdyfdivk npmdlstikr
     1141 kldtgqyqep wqyvddvwlm fnnawlynrk tsrvykfcsk laevfeqeid pvmqslgycc
     1201 grkyefspqt lccygkqlct iprdaayysy qnryhfcekc fteiqgenvt lgddpsqpqt
     1261 tiskdqfekk kndtldpepf vdckecgrkm hqicvlhydi iwpsgfvcdn clkktgrprk
     1321 enkfsakrlq ttrlgnhled rvnkflrrqn hpeagevfvr vvassdktve vkpgmksrfv
     1381 dsgemsesfp yrtkalfafe eidgvdvcff gmhvqeygsd cpppntrrvy isyldsihff
     1441 rprclrtavy heiligyley vkklgyvtgh iwacppsegd dyifhchppd qkipkpkrlq
     1501 ewykkmldka faeriihdyk difkqatedr ltsakelpyf egdfwpnvle esikeleqee
     1561 eerkkeesta asettegsqg dsknakkknn kktnknkssi srankkkpsm pnvsndlsqk
     1621 lyatmekhke vffvihlhag pvintlppiv dpdpllscdl mdgrdafltl ardkhwefss
     1681 lrrskwstlc mlvelhtqgq drfvytcnec khhvetrwhc tvcedydlci ncyntkshah
     1741 kmvkwglgld degssqgepq skspqesrrl siqrciqslv hacqcrnanc slpscqkmkr
     1801 vvqhtkgckr ktnggcpvck qlialccyha khcqenkcpv pfclnikhkl rqqqiqhrlq
     1861 qaqlmrrrma tmntrnvpqq slpsptsapp gtptqqpstp qtpqppaqpq pspvsmspag
     1921 fpsvartqpp ttvstgkpts qvpappppaq pppaaveaar qiereaqqqq hlyrvninns
     1981 mppgrtgmgt pgsqmapvsl nvprpnqvsg pvmpsmppgq wqqaplpqqq pmpglprpvi
     2041 smqaqaavag prmpsvqppr sispsalqdl lrtlkspssp qqqqqvlnil ksnpqlmaaf
     2101 ikqrtakyva nqpgmqpqpg lqsqpgmqpq pgmhqqpslq nlnamqagvp rpgvppqqqa
     2161 mgglnpqgqa lnimnpghnp nmasmnpqyr emlrrqllqq qqqqqqqqqq qqqqqqgsag
     2221 maggmaghgq fqqpqgpggy ppamqqqqrm qqhlplqgss mgqmaaqmgq lgqmgqpglg
     2281 adstpniqqa lqqrilqqqq mkqqigspgq pnpmspqqhm lsgqpqashl pgqqiatsls
     2341 nqvrspapvq sprpqsqpph sspspriqpq psphhvspqt gsphpglavt massidqghl
     2401 gnpeqsamlp qlntpsrsal sselslvgdt tgdtlekfve gl
//
LOCUS       NP_001387139            1179 aa            linear   PRI 21-NOV-2025
DEFINITION  protein transport protein Sec31A isoform 23 [Homo sapiens].
ACCESSION   NP_001387139
VERSION     NP_001387139.1
DBSOURCE    REFSEQ: accession NM_001400210.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1179)
  AUTHORS   Tobias,E.S., Lucas-Herald,A.K., Sagar,D., Montezano,A.C.,
            Rios,F.J., De Lucca Camargo,L., Hamilton,G., Gazdagh,G.,
            Diver,L.A., Williams,N., Herzyk,P., Touyz,R.M., Greenfield,A.,
            McGowan,R. and Ahmed,S.F.
  TITLE     SEC31A may be associated with pituitary hormone deficiency and
            gonadal dysgenesis
  JOURNAL   Endocrine 84 (2), 345-349 (2024)
   PUBMED   38400880
  REMARK    GeneRIF: SEC31A may be associated with pituitary hormone deficiency
            and gonadal dysgenesis.
REFERENCE   2  (residues 1 to 1179)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1179)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1179)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1179)
  AUTHORS   Jin,L., Pahuja,K.B., Wickliffe,K.E., Gorur,A., Baumgartel,C.,
            Schekman,R. and Rape,M.
  TITLE     Ubiquitin-dependent regulation of COPII coat size and function
  JOURNAL   Nature 482 (7386), 495-500 (2012)
   PUBMED   22358839
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1179)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1179)
  AUTHORS   Kim,J.H., Hong,J.A., Pih,K.T. and Hwang,I.
  TITLE     Identification and isolation of differentially expressed genes in
            osmotically stressed human oral keratinocytes
  JOURNAL   Arch Oral Biol 46 (4), 335-341 (2001)
   PUBMED   11269867
REFERENCE   8  (residues 1 to 1179)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 1179)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   10 (residues 1 to 1179)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021105.13 and AC108469.5.
            
            Summary: The protein encoded by this gene shares similarity with
            the yeast Sec31 protein, and is a component of the outer layer of
            the coat protein complex II (COPII). The encoded protein is
            involved in vesicle budding from the endoplasmic reticulum (ER) and
            contains multiple WD repeats near the N-terminus and a proline-rich
            region in the C-terminal half. It associates with the protein
            encoded by the SEC13 homolog, nuclear pore and COPII coat complex
            component (SEC13), and is required for ER-Golgi transport.
            Monoubiquitylation of this protein by CUL3-KLHL12 was found to
            regulate the size of COPII coats to accommodate unusually shaped
            cargo. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1792447.1,
                                           SRR14038193.849021.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1179
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..1179
                     /product="protein transport protein Sec31A isoform 23"
                     /note="yeast Sec31p homolog; protein transport protein
                     Sec31A; web1-like protein; SEC31 homolog A, COPII coat
                     complex component; SEC31-related protein A; SEC31-like
                     protein 1; SEC31 homolog A, COPII coating complex
                     component"
                     /calculated_mol_wt=128705
     Region          13..332
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(26,40,46..47,52..53,91,95,101..102,117,121,139,144,
                     150..151,164,185,190,196..197,209..210,231,235,244..245,
                     258..259,277,282,288..289,301..302,320,325,331..332)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          70..119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          125..162
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          172..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          263..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          306..331
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <547..>670
                     /region_name="ACE1-Sec16-like"
                     /note="Ancestral coatomer element 1 (ACE1) of COPII coat
                     complex assembly protein Sec16; cl14807"
                     /db_xref="CDD:449359"
     Site            order(548..552,554,556,567,569,570..571,573..574,578,584,
                     592,604,607,632..633)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187750"
     Region          724..>1114
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          888..>1075
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     CDS             1..1179
                     /gene="SEC31A"
                     /gene_synonym="ABP125; ABP130; HPBKS; HSPC275; HSPC334;
                     NEDSOSB; SEC31L1"
                     /coded_by="NM_001400210.1:68..3607"
                     /note="isoform 23 is encoded by transcript variant 44"
                     /db_xref="GeneID:22872"
                     /db_xref="HGNC:HGNC:17052"
                     /db_xref="MIM:610257"
ORIGIN      
        1 mklkevdrta mqawspaqnh piylatgtsa qqldatfstn asleifeldl sdpsldmksc
       61 atfssshryh kliwgpykmd skgdvsgvli aggengniil ydpskiiagd kevviaqndk
      121 htgpvraldv nifqtnlvas ganeseiyiw dlnnfatpmt pgaktqpped isciawnrqv
      181 qhilasasps gratvwdlrk nepiikvsdh snrmhcsgla whpdvatqmv laseddrlpv
      241 iqmwdlrfas splrvlenha rgilaiawsm adpelllscg kdakilcsnp ntgevlyelp
      301 tntqwcfdiq wcprnpavls aasfdgrisv ysimggstdg lrqkqvdkls ssfgnldpfg
      361 tgqplpplqi pqqtaqhsiv lplkkppkwi rrpvgasfsf ggklvtfenv rmpshqgaeq
      421 qqqqhhvfis qvvtekefls rsdqlqqavq sqgfinycqk kidasqtefe knvwsflkvn
      481 feddsrgkyl ellgyrkedl gkkialalnk vdganvhike ekeeseflps sggtfnisvs
      541 gdidglitqa lltgnfesav dlclhdnrma daiilaiagg qellartqkk yfaksqskit
      601 rlitavvmkn wkeivescdl knwrealaav ltyakpdefs alcdllgtrl enegdsllqt
      661 qaclcyicag nveklvacwt kaqdgshpls lqdliekvvi lrkavqltqa mdtstvgvll
      721 aakmsqyanl laaqgsiaaa laflpdntnq pnimqlrdrl craqgepvag hespkipyek
      781 qqlpkgrpgp vaghhqmprv qtqqyyphge nppppgfimh gnvnpnaagq lptspghmht
      841 qvppypqpqp yqpaqpypfg tggsamyrpq qpvapptsna ypntpyissa ssytgqsqly
      901 aaqhqasspt sspatsfppp pssgasfqhg gpgappsssa yalppgttgp qngwndppal
      961 nrvpkkkkmp enfmppvpit spimnplgdp qsqmlqqqps apvplssqss fpqphlpggq
     1021 pfhgvqqplg qtgmppsfsk pniegapgap igntfqhvqs lptkkitkkp ipdehlilkt
     1081 tfedliqrcl ssatdpqtkr klddaskrle flydklreqt lsptitsglh niarsietrn
     1141 ysegltmhth ivstsnfset safmpvlkvv ltqanklgv
//
LOCUS       NP_001361613            1100 aa            linear   PRI 21-NOV-2025
DEFINITION  trafficking protein particle complex subunit 9 isoform f [Homo
            sapiens].
ACCESSION   NP_001361613
VERSION     NP_001361613.1
DBSOURCE    REFSEQ: accession NM_001374684.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1100)
  AUTHORS   Kharrat,M., Triki,C., Ben Isaa,A., Bouchaala,W., Alila,O.,
            Chouchen,J., Ghouliya,Y., Kamoun,F., Tlili,A. and Fakhfakh,F.
  TITLE     Expanding the genetic and phenotypic spectrum of TRAPPC9 and
            MID2-related neurodevelopmental disabilities: report of two novel
            mutations, 3D-modelling, and molecular docking studies
  JOURNAL   J Hum Genet 69 (7), 291-299 (2024)
   PUBMED   38467738
  REMARK    GeneRIF: Expanding the genetic and phenotypic spectrum of TRAPPC9
            and MID2-related neurodevelopmental disabilities: report of two
            novel mutations, 3D-modelling, and molecular docking studies.
REFERENCE   2  (residues 1 to 1100)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1100)
  AUTHORS   Lorente-Pozo,S., Boronat,N., Parra-Llorca,A., Lara-Canton,I.,
            Solaz-Garcia,A., Oltra Soler,J.V., Buso,E.J., Casabo-Valles,G.,
            Garcia-Gimenez,J.L., Pallardo,F.V. and Vento,M.
  TITLE     Neurodevelopmental Outcome and Epigenetic Changes at 2 Years
            Associated with the Oxygen Load Received upon Postnatal
            Stabilization: A Pilot Study
  JOURNAL   Neonatology 119 (5), 575-584 (2022)
   PUBMED   35760056
  REMARK    GeneRIF: Neurodevelopmental Outcome and Epigenetic Changes at 2
            Years Associated with the Oxygen Load Received upon Postnatal
            Stabilization: A Pilot Study.
REFERENCE   4  (residues 1 to 1100)
  AUTHORS   Ben Ayed,I., Bouchaala,W., Bouzid,A., Feki,W., Souissi,A., Ben
            Nsir,S., Ben Said,M., Sammouda,T., Majdoub,F., Kharrat,I.,
            Kamoun,F., Elloumi,I., Kamoun,H., Tlili,A., Masmoudi,S. and
            Triki,C.
  TITLE     Further insights into the spectrum phenotype of TRAPPC9 and
            CDK5RAP2 genes, segregating independently in a large Tunisian
            family with intellectual disability and microcephaly
  JOURNAL   Eur J Med Genet 64 (12), 104373 (2021)
   PUBMED   34737153
  REMARK    GeneRIF: Further insights into the spectrum phenotype of TRAPPC9
            and CDK5RAP2 genes, segregating independently in a large Tunisian
            family with intellectual disability and microcephaly.
REFERENCE   5  (residues 1 to 1100)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1100)
  AUTHORS   Kent,J.W. Jr., Peterson,C.P., Dyer,T.D., Almasy,L. and Blangero,J.
  TITLE     Genome-wide discovery of maternal effect variants
  JOURNAL   BMC Proc 3 Suppl 7 (Suppl 7), S19 (2009)
   PUBMED   20018008
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1100)
  AUTHORS   Mir,A., Kaufman,L., Noor,A., Motazacker,M.M., Jamil,T., Azam,M.,
            Kahrizi,K., Rafiq,M.A., Weksberg,R., Nasr,T., Naeem,F.,
            Tzschach,A., Kuss,A.W., Ishak,G.E., Doherty,D., Ropers,H.H.,
            Barkovich,A.J., Najmabadi,H., Ayub,M. and Vincent,J.B.
  TITLE     Identification of mutations in TRAPPC9, which encodes the NIK- and
            IKK-beta-binding protein, in nonsyndromic autosomal-recessive
            mental retardation
  JOURNAL   Am J Hum Genet 85 (6), 909-915 (2009)
   PUBMED   20004765
  REMARK    GeneRIF: TRAPPC9, encodes the NIK- and IKK-beta-binding protein,
            has a role in nonsyndromic autosomal-recessive mental retardation
REFERENCE   8  (residues 1 to 1100)
  AUTHORS   Philippe,O., Rio,M., Carioux,A., Plaza,J.M., Guigue,P.,
            Molinari,F., Boddaert,N., Bole-Feysot,C., Nitschke,P., Smahi,A.,
            Munnich,A. and Colleaux,L.
  TITLE     Combination of linkage mapping and microarray-expression analysis
            identifies NF-kappaB signaling defect as a cause of
            autosomal-recessive mental retardation
  JOURNAL   Am J Hum Genet 85 (6), 903-908 (2009)
   PUBMED   20004764
REFERENCE   9  (residues 1 to 1100)
  AUTHORS   Mochida,G.H., Mahajnah,M., Hill,A.D., Basel-Vanagaite,L.,
            Gleason,D., Hill,R.S., Bodell,A., Crosier,M., Straussberg,R. and
            Walsh,C.A.
  TITLE     A truncating mutation of TRAPPC9 is associated with
            autosomal-recessive intellectual disability and postnatal
            microcephaly
  JOURNAL   Am J Hum Genet 85 (6), 897-902 (2009)
   PUBMED   20004763
  REMARK    GeneRIF: TRAPPC9 has a role in brain development, possibly through
            its effect on NF-kappaB activation and protein trafficking in the
            postmitotic neurons of the cerebral cortex
REFERENCE   10 (residues 1 to 1100)
  AUTHORS   Hu,W.H., Pendergast,J.S., Mo,X.M., Brambilla,R., Bracchi-Ricard,V.,
            Li,F., Walters,W.M., Blits,B., He,L., Schaal,S.M. and Bethea,J.R.
  TITLE     NIBP, a novel NIK and IKK(beta)-binding protein that enhances
            NF-(kappa)B activation
  JOURNAL   J Biol Chem 280 (32), 29233-29241 (2005)
   PUBMED   15951441
  REMARK    GeneRIF: NIBP is a NIK and IKK(beta)-binding protein that enhances
            NF-(kappa)B activation
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091022.4, AC104244.9,
            AC040978.8, AC021744.14 and AC007869.2.
            
            Summary: This gene encodes a protein that likely plays a role in
            NF-kappa-B signaling. Mutations in this gene have been associated
            with autosomal-recessive cognitive disability. Alternatively
            spliced transcript variants have been described.[provided by
            RefSeq, Feb 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1133509.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1100
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..1100
                     /product="trafficking protein particle complex subunit 9
                     isoform f"
                     /note="IKK2 binding protein; TRAPP 120 kDa subunit; NIK-
                     and IKBKB-binding protein; NIK and IKK-beta binding
                     protein; tularik gene 1 protein; trafficking protein
                     particle complex 9"
                     /calculated_mol_wt=122893
     Region          14..1052
                     /region_name="TRAPPC9-Trs120"
                     /note="Transport protein Trs120 or TRAPPC9, TRAPP II
                     complex subunit; pfam08626"
                     /db_xref="CDD:430114"
     CDS             1..1100
                     /gene="TRAPPC9"
                     /gene_synonym="IBP; IKBKBBP; MRT13; NIBP; T1; TRS120"
                     /coded_by="NM_001374684.1:117..3419"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="GeneID:83696"
                     /db_xref="HGNC:HGNC:30832"
                     /db_xref="MIM:611966"
ORIGIN      
        1 msvpdymqca edhqtllvvv qpvgivseen ffriykrics vsqisvrdsq rvlyiryrhh
       61 yppennewgd fqthrkvvgl ititdcfsak dwpqtfekfh vqkeiygstl ydsrlfvfgl
      121 qgeiveqprt dvafypnyed cqtvekried fieslfivle skrldratdk sgdkipllcv
      181 pfekkdfvgl dtdsrhykkr cqgrmrkhvg dlclqagmlq dslvhyhmsv ellrsvndfl
      241 wlgaaleglc sasviyhypg gtggksgarr fqgstlpaea anrhrpgaqe vlidpgaltt
      301 nginpdtste igraknclsp ediidkykea isyyskykna gvieleacik avrvlaiqkr
      361 smeaseflqn avyinlrqls eeekiqrysi lselyeligf hrksaffkrv aamqcvapsi
      421 aepgwracyk llletlpgys lsldpkdfsr ekkdvaqsle nytskcpgtm epialpgglt
      481 lppvpftklp ivrhvkllnl paslrphkmk sllgqnvstk spfiyspiia hnrgeernkk
      541 idfqwvqgdv cevqlmvynp mpfelrvenm glltsgvefe slpaalslpa esglypvtlv
      601 gvpqttgtit vngyhttvfg vfsdclldnl pgiktsgstv evipalprlq istslprsah
      661 slqpssgdei stnvsvqlyn gesqqliikl enigmeplek levtskvltt keklygdfls
      721 wkleetlaqf plqpgkvatf tinikvkldf scqenllqdl sddgisvsgf plsspfrqvv
      781 rprvegkpvn ppesnkagdy shvktleavl nfkysggpgh tegyyrnlsl glhvevepsv
      841 fftrvstlpa tstrqchlll dvfnstehel tvstrsseal ilhagecqrm aiqvdkfnfe
      901 sfpespgekg qfanpkqlee errearglei hsklgicwri pslkrsgeas vegllnqlvl
      961 ehlqlaplqw dvlvdgqpcd reavaacqvg dpvrlevrlt nrsprsvgpf altvvpfqdh
     1021 qngvhnydlh dtvsfvgsst fyldavqpsg qsaclgallf lytgdfflhi rfhedstske
     1081 lppswfclps vhvcaleaqa
//
LOCUS       NP_065869               2458 aa            linear   PRI 21-NOV-2025
DEFINITION  protein unc-79 homolog isoform 2 [Homo sapiens].
ACCESSION   NP_065869 XP_350940
VERSION     NP_065869.3
DBSOURCE    REFSEQ: accession NM_020818.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2458)
  AUTHORS   Bayat,A., Liu,Z., Luo,S., Fenger,C.D., Hojte,A.F., Isidor,B.,
            Cogne,B., Larson,A., Zanus,C., Faletra,F., Keren,B., Musante,L.,
            Gourfinkel-An,I., Perrine,C., Demily,C., Lesca,G., Liao,W. and
            Ren,D.
  TITLE     A new neurodevelopmental disorder linked to heterozygous variants
            in UNC79
  JOURNAL   Genet Med 25 (9), 100894 (2023)
   PUBMED   37183800
  REMARK    GeneRIF: A new neurodevelopmental disorder linked to heterozygous
            variants in UNC79.
REFERENCE   2  (residues 1 to 2458)
  AUTHORS   Kschonsak,M., Chua,H.C., Weidling,C., Chakouri,N., Noland,C.L.,
            Schott,K., Chang,T., Tam,C., Patel,N., Arthur,C.P., Leitner,A.,
            Ben-Johny,M., Ciferri,C., Pless,S.A. and Payandeh,J.
  TITLE     Structural architecture of the human NALCN channelosome
  JOURNAL   Nature 603 (7899), 180-186 (2022)
   PUBMED   34929720
REFERENCE   3  (residues 1 to 2458)
  AUTHORS   Chua,H.C., Wulf,M., Weidling,C., Rasmussen,L.P. and Pless,S.A.
  TITLE     The NALCN channel complex is voltage sensitive and directly
            modulated by extracellular calcium
  JOURNAL   Sci Adv 6 (17), eaaz3154 (2020)
   PUBMED   32494638
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2458)
  AUTHORS   Bramswig,N.C., Bertoli-Avella,A.M., Albrecht,B., Al Aqeel,A.I.,
            Alhashem,A., Al-Sannaa,N., Bah,M., Brohl,K., Depienne,C.,
            Dorison,N., Doummar,D., Ehmke,N., Elbendary,H.M., Gorokhova,S.,
            Heron,D., Horn,D., James,K., Keren,B., Kuechler,A., Ismail,S.,
            Issa,M.Y., Marey,I., Mayer,M., McEvoy-Venneri,J., Megarbane,A.,
            Mignot,C., Mohamed,S., Nava,C., Philip,N., Ravix,C., Rolfs,A.,
            Sadek,A.A., Segebrecht,L., Stanley,V., Trautman,C., Valence,S.,
            Villard,L., Wieland,T., Engels,H., Strom,T.M., Zaki,M.S.,
            Gleeson,J.G., Ludecke,H.J., Bauer,P. and Wieczorek,D.
  TITLE     Genetic variants in components of the NALCN-UNC80-UNC79 ion channel
            complex cause a broad clinical phenotype (NALCN channelopathies)
  JOURNAL   Hum Genet 137 (9), 753-768 (2018)
   PUBMED   30167850
  REMARK    GeneRIF: UNC79 variant is associated with neurodevelopmental
            diseases.
REFERENCE   5  (residues 1 to 2458)
  AUTHORS   Shamseldin,H.E., Faqeih,E., Alasmari,A., Zaki,M.S., Gleeson,J.G.
            and Alkuraya,F.S.
  TITLE     Mutations in UNC80, Encoding Part of the UNC79-UNC80-NALCN Channel
            Complex, Cause Autosomal-Recessive Severe Infantile Encephalopathy
  JOURNAL   Am J Hum Genet 98 (1), 210-215 (2016)
   PUBMED   26708753
  REMARK    GeneRIF: UNC80 encodes a large protein that is necessary for the
            stability and function of NALCN and for bridging NALCN to UNC79 to
            form a functional complex
REFERENCE   6  (residues 1 to 2458)
  AUTHORS   Lu,B., Zhang,Q., Wang,H., Wang,Y., Nakayama,M. and Ren,D.
  TITLE     Extracellular calcium controls background current and neuronal
            excitability via an UNC79-UNC80-NALCN cation channel complex
  JOURNAL   Neuron 68 (3), 488-499 (2010)
   PUBMED   21040849
REFERENCE   7  (residues 1 to 2458)
  AUTHORS   Speca,D.J., Chihara,D., Ashique,A.M., Bowers,M.S.,
            Pierce-Shimomura,J.T., Lee,J., Rabbee,N., Speed,T.P., Gularte,R.J.,
            Chitwood,J., Medrano,J.F., Liao,M., Sonner,J.M., Eger,E.I. 2nd,
            Peterson,A.S. and McIntire,S.L.
  TITLE     Conserved role of unc-79 in ethanol responses in lightweight mutant
            mice
  JOURNAL   PLoS Genet 6 (8), e1001057 (2010)
   PUBMED   20714347
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 2458)
  AUTHORS   Lind,P.A., Macgregor,S., Vink,J.M., Pergadia,M.L., Hansell,N.K., de
            Moor,M.H., Smit,A.B., Hottenga,J.J., Richter,M.M., Heath,A.C.,
            Martin,N.G., Willemsen,G., de Geus,E.J., Vogelzangs,N.,
            Penninx,B.W., Whitfield,J.B., Montgomery,G.W., Boomsma,D.I. and
            Madden,P.A.
  TITLE     A genomewide association study of nicotine and alcohol dependence
            in Australian and Dutch populations
  JOURNAL   Twin Res Hum Genet 13 (1), 10-29 (2010)
   PUBMED   20158304
  REMARK    GeneRIF: In the Australian GWAS, one SNP achieved genomewide
            significance for comorbid AD/ND, rs12882384 in KIAA1409 on
            chromosome 14 (p = 4.86 x 10(-8))).
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL122023.3, AL136338.4 and
            AL157858.5.
            
            On Jul 4, 2007 this sequence version replaced NP_065869.2.
            
            Summary: The NALCN channel is responsible for Na(+) leak currents.
            The protein encoded by this gene, along with UNC80, is an accessory
            subunit of the NALCN channel that contributes to the Ca(2+)
            sensitivity of the channel. [provided by RefSeq, Sep 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence and lacks an alternate in-frame exon compared to
            variant 1. The resulting isoform (2) is shorter at the N-terminus
            and lacks an alternate internal segment compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2161674
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2458
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.12"
     Protein         1..2458
                     /product="protein unc-79 homolog isoform 2"
                     /note="protein unc-79 homolog; unc-79 homolog, NALCN
                     channel complex subunit"
                     /calculated_mol_wt=275304
     Region          3..468
                     /region_name="UNC-79"
                     /note="Cation-channel complex subunit UNC-79; pfam14776"
                     /db_xref="CDD:434201"
     CDS             1..2458
                     /gene="UNC79"
                     /gene_synonym="KIAA1409"
                     /coded_by="NM_020818.5:693..8069"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9911.2"
                     /db_xref="GeneID:57578"
                     /db_xref="HGNC:HGNC:19966"
                     /db_xref="MIM:616884"
ORIGIN      
        1 mistlatfpp flhkdiieyl stsflpmail gssrregvpa hvnlsassml miamqytsnp
       61 vyhcqllecl mkykqevwkd llyviaygps qvkppavqml fhywpnlkpp gaiseyrglq
      121 ytawnpihcq hiechnaink pavkmcidps lsvalgdkpp plylceecse riagdhsewl
      181 idvllpqaei saicqkkncs shvrravvtc fsagccgrhg nrpvryckrc hsnhhsnevg
      241 aaaethlyqt spppintrec gaeelvcave avisllkeae fhaeqrehel nrrrqlglss
      301 shhsldnadf dnkdddkhdq rllsqfgiwf lvslctpsen tpteslarlv amvfqwfhst
      361 aymmddevgs lveklkpqfv tkwlktvcdv rfdvmvmcll pkpmefarvg gywdkscstv
      421 tqlkeglnri lclipynvin qsvwecimpe wleairtevp dnqlkefrev lskmfdielc
      481 plpfsmeemf gfiscrftgy pssvqeqall wlhvlseldi mvplqllism fsdgvnsvke
      541 lanqrksrvs elagnlasrr vsvasdpgrr vqhnmlspfh spfqspfrsp lrspfrspfk
      601 nfghpggrti dfdceddemn lncfilmfdl llkqmelqdd gitmglehsl skdiisiinn
      661 vfqapwggsh tcqkdekaie cnlcqssilc yqlaceller lapkeesrlv eptdsledsl
      721 lssrpefiig pegeeeenpa skhgenpgnc tepvehaavk ndterkfcyq qlpvtlrliy
      781 tifqemakfe epdilfnmln clkilclhge clyiarkdhp qflayiqdhm liaslwrvvk
      841 sefsqlssla vplllhalsl phgadifwti ingnfnskdw kmrfeavekv avicrfldih
      901 svtknhllky slahafccfl tavedvnpav atragllldt ikrpalqglc lcldfqfdtv
      961 vkdrptilsk llllhflkqd ipalsweffv nrfetlslea qlhldcnkef pfpttitavr
     1021 tnvanlsdaa lwkikrarfa rnrqksvrsl rdsvkgpves kralslpetl tskirqqspe
     1081 ndntikdllp edagidhqtv hqlitvlmkf makdessaes dissakafnt vkrhlyvllg
     1141 ydqqegcfmi apqkmrlstc fnafiagiaq vmdyninlgk hllplvvqvl kycscpqlrh
     1201 yfqqpprcsl wslkphirqm wlkallvily kypyrdcdis killhlihit vntlnaqyhs
     1261 ckphatagpl ysdnsnisry sekekgeiel aeyretgalq dsllhcvree sipkkklrsf
     1321 kqksldigna dsllftldeh rrkscidrcd iekpptqaay iaqrpndpgr srqnsatrpd
     1381 nseipenpam egfpdarrpv ipevrlncme tfevkvdspv kpapkedldl idlssdstsg
     1441 pekhsilsts dsdslvfepl pplrivesde eeetmnqgdd gpsgknaass psvpshpsvl
     1501 slstaplvqv svedcskdfs skdsgnnqsa gntdsalitl edpmdaegss kpeelpefsc
     1561 gspltlkqkr dllqksfalp emslddhpdp gtegekpgel mpssgaktvl lkvpedaenp
     1621 tesekpdtsa esdteqnper kveedgaees efkiqivprq rkqrkiavsa iqreyldisf
     1681 nildklgeqk dpdpstkgls tlempresss aptldagvpe tsshssistq yrqmkrgslg
     1741 vltmsqlmkr qlehqssaph nisnwdteqi qpgkrqcnvp tclnpdlegq plrmrgatks
     1801 sllsapsivs mfvpapeeft deqptvmtdk chdcgailee ydeetlglai vvlstfihls
     1861 pdlaapllld imqsvgrlas sttfsnqaes mmvpgnaagv akqflrcifh qlapngifpq
     1921 lfqstikdgt flrtlasslm dfnelssiaa lsqlleglnn kknlpaggam ircleniatf
     1981 mealpmdsps slwttisnqf qtffaklpcv lplkcsldss lrimicllki pstnatrsll
     2041 epfskllsfv iqnavftlay lvelcglcyr aftkerdkfy lsrsvvlell qalklksplp
     2101 dtnllllvqf icadagtkla estilskqmi asvpgcgtaa mecvrqyine vldfmadmht
     2161 ltklkshmkt csqplhedtf gghlkvglaq iaamdisrgn hrdnkaviry lpwlyhppsa
     2221 mqqgpkefie cvshirllsw lllgslthna vcpnasspcl pipldagshv adhlivilig
     2281 fpeqsktsvl hmcslfhafi faqlwtvyce qsavatnlqn qnefsftail talefwsrvt
     2341 psilqlmahn kvmvemvclh vislmealqe cnstifvkli pmwlpmiqsn ikhlsaglql
     2401 rlqaiqnhvn hhslrtlpgs gqssaglaal rkwlqctqfk maqveiqsse aasqfypl
//
LOCUS       NP_001335098             695 aa            linear   PRI 21-NOV-2025
DEFINITION  hepatoma-derived growth factor-related protein 2 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001335098 XP_011526677
VERSION     NP_001335098.1
DBSOURCE    REFSEQ: accession NM_001348169.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Wang,J., Zhu,X., Dang,L., Jiang,H., Xie,Y., Li,X., Guo,J., Wang,Y.,
            Peng,Z., Wang,M., Wang,J., Wang,S., Li,Q., Wang,Y., Wang,Q., Ye,L.,
            Zhang,L. and Liu,Z.
  TITLE     Epigenomic reprogramming via HRP2-MINA dictates response to
            proteasome inhibitors in multiple myeloma with t(4;14)
            translocation
  JOURNAL   J Clin Invest 132 (4) (2022)
   PUBMED   35166240
  REMARK    GeneRIF: Epigenomic reprogramming via HRP2-MINA dictates response
            to proteasome inhibitors in multiple myeloma with t(4;14)
            translocation.
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Van Belle,S., El Ashkar,S., Cermakova,K., Matthijssens,F.,
            Goossens,S., Canella,A., Hodges,C.H., Christ,F., De Rijck,J., Van
            Vlierberghe,P., Veverka,V. and Debyser,Z.
  TITLE     Unlike Its Paralog LEDGF/p75, HRP-2 Is Dispensable for MLL-R
            Leukemogenesis but Important for Leukemic Cell Survival
  JOURNAL   Cells 10 (1), 192 (2021)
   PUBMED   33477970
  REMARK    GeneRIF: Unlike Its Paralog LEDGF/p75, HRP-2 Is Dispensable for
            MLL-R Leukemogenesis but Important for Leukemic Cell Survival.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Zhu,X., Lan,B., Yi,X., He,C., Dang,L., Zhou,X., Lu,Y., Sun,Y.,
            Liu,Z., Bai,X., Zhang,K., Li,B., Li,M.J., Chen,Y. and Zhang,L.
  TITLE     HRP2-DPF3a-BAF complex coordinates histone modification and
            chromatin remodeling to regulate myogenic gene transcription
  JOURNAL   Nucleic Acids Res 48 (12), 6563-6582 (2020)
   PUBMED   32459350
REFERENCE   5  (residues 1 to 695)
  AUTHORS   LeRoy,G., Oksuz,O., Descostes,N., Aoi,Y., Ganai,R.A., Kara,H.O.,
            Yu,J.R., Lee,C.H., Stafford,J., Shilatifard,A. and Reinberg,D.
  TITLE     LEDGF and HDGF2 relieve the nucleosome-induced barrier to
            transcription in differentiated cells
  JOURNAL   Sci Adv 5 (10), eaay3068 (2019)
   PUBMED   31616795
  REMARK    GeneRIF: LEDGF and HDGF2 colocalize with Histone H3 lysine 36
            methylation 2/3 at genomic regions containing active genes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 695)
  AUTHORS   Schrijvers,R., Vets,S., De Rijck,J., Malani,N., Bushman,F.D.,
            Debyser,Z. and Gijsbers,R.
  TITLE     HRP-2 determines HIV-1 integration site selection in LEDGF/p75
            depleted cells
  JOURNAL   Retrovirology 9, 84 (2012)
   PUBMED   23046603
  REMARK    GeneRIF: Authors show that HRP-2 functions as a co-factor of HIV-1
            IN in LEDGF/p75-depleted cells.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 695)
  AUTHORS   Xiao,K., McClatchy,D.B., Shukla,A.K., Zhao,Y., Chen,M.,
            Shenoy,S.K., Yates,J.R. 3rd and Lefkowitz,R.J.
  TITLE     Functional specialization of beta-arrestin interactions revealed by
            proteomic analysis
  JOURNAL   Proc Natl Acad Sci U S A 104 (29), 12011-12016 (2007)
   PUBMED   17620599
REFERENCE   8  (residues 1 to 695)
  AUTHORS   Vandegraaff,N., Devroe,E., Turlure,F., Silver,P.A. and Engelman,A.
  TITLE     Biochemical and genetic analyses of integrase-interacting proteins
            lens epithelium-derived growth factor (LEDGF)/p75 and
            hepatoma-derived growth factor related protein 2 (HRP2) in
            preintegration complex function and HIV-1 replication
  JOURNAL   Virology 346 (2), 415-426 (2006)
   PUBMED   16337983
  REMARK    GeneRIF: Here, we show that recombinant HDGF2 host cell factor
            efficiently reconstitutes the in vitro activity of HIV-1
            preintegration complexes.
REFERENCE   9  (residues 1 to 695)
  AUTHORS   Cherepanov,P., Devroe,E., Silver,P.A. and Engelman,A.
  TITLE     Identification of an evolutionarily conserved domain in human lens
            epithelium-derived growth factor/transcriptional co-activator p75
            (LEDGF/p75) that binds HIV-1 integrase
  JOURNAL   J Biol Chem 279 (47), 48883-48892 (2004)
   PUBMED   15371438
REFERENCE   10 (residues 1 to 695)
  AUTHORS   Izumoto,Y., Kuroda,T., Harada,H., Kishimoto,T. and Nakamura,H.
  TITLE     Hepatoma-derived growth factor belongs to a gene family in mice
            showing significant homology in the amino terminus
  JOURNAL   Biochem Biophys Res Commun 238 (1), 26-32 (1997)
   PUBMED   9299445
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011498.7, KF573697.1 and
            BU738961.1.
            
            On Jan 13, 2017 this sequence version replaced XP_011526677.1.
            
            Summary: This gene encodes a member of the hepatoma-derived growth
            factor (HDGF) family. The protein includes an N-terminal PWWP
            domain that binds to methyl-lysine-containing histones, with
            specific binding of this protein to tri-methylated lysines 36 and
            79 of histone H3, and di- and tri-methylated lysine 20 of histone
            H4. The protein functions in LEDGF/p75-independent HIV-1
            replication by determining HIV-1 integration site selection.
            Alternative splicing of this gene results in multiple transcript
            variants. [provided by RefSeq, Apr 2014].
            
            Transcript Variant: This variant (3) contains an alternate 5' exon
            resulting in a novel 5' UTR and 5' coding region compared to
            variant 1. The encoded isoform (3) has a longer and distinct
            N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.92640.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..695
                     /product="hepatoma-derived growth factor-related protein 2
                     isoform 3"
                     /note="hepatoma-derived growth factor-related protein 2;
                     HDGF-related protein 2"
                     /calculated_mol_wt=76642
     Region          <49..112
                     /region_name="PWWP"
                     /note="PWWP (Pro-Trp-Trp-Pro) domain; cl02554"
                     /db_xref="CDD:470613"
     Region          <232..651
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          496..593
                     /region_name="LEDGF"
                     /note="Lens epithelium-derived growth factor (LEDGF);
                     pfam11467"
                     /db_xref="CDD:463284"
     CDS             1..695
                     /gene="HDGFL2"
                     /gene_synonym="HDGF-2; HDGF2; HDGFRP2; HRP-2; HRP2"
                     /coded_by="NM_001348169.2:392..2479"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:84717"
                     /db_xref="HGNC:HGNC:14680"
                     /db_xref="MIM:617884"
ORIGIN      
        1 mpgwssggln lgcfwrerda gpggpwpspg ardsdkvalr rpkregswid diadgavkpp
       61 pnkypifffg thetaflgpk dlfpydkckd kygkpnkrkg fneglweiqn nphasysapp
      121 pvsssdseap eanpadgsda deddedrgvm avtavtataa sdrmesdsds dkssdnsglk
      181 rktpalkmsv skrarkassd ldqasvspse eensessses ektsdqdftp ekkaavrapr
      241 rgplggrkkk kapsasdsds kadsdgakpe pvamarsass ssssssssds dvsvkkpprg
      301 rkpaekplpk prgrkpkper ppsssssdsd sdevdrisew krrdearrre learrrreqe
      361 eelrrlreqe keekerrrer adrgeaergs ggssgdelre ddepvkkrgr kgrgrgppss
      421 sdsepeaele reakksakkp qssstepark pgqkekrvrp eekqqakpvk vertrkrseg
      481 fsmdrkvekk kepsveeklq klhseikfal kvdspdvkrc lnaleelgtl qvtsqilqkn
      541 tdvvatlkki rrykankdvm ekaaevytrl ksrvlgpkie avqkvnkagm ekekaeekla
      601 geelageeap qekaedkpst dlsapvngea tsqkgesaed keheegrdse egprcgssed
      661 lhdsvregpd ldrpgsdrqe rerargdsea ldees
//
LOCUS       NP_001340197             324 aa            linear   PRI 21-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 1 [Homo sapiens].
ACCESSION   NP_001340197 XP_011515415
VERSION     NP_001340197.1
DBSOURCE    REFSEQ: accession NM_001353268.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC022973.5.
            
            On Jul 1, 2017 this sequence version replaced XP_011515415.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3222240.1,
                                           SRR1803613.238255.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 1"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=36617
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353268.2:424..1398"
                     /note="isoform 1 is encoded by transcript variant 30"
                     /db_xref="CCDS:CCDS6361.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mgnllkvltc tdleqgpnff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqik smlq
//
LOCUS       NP_001263690             354 aa            linear   PRI 21-NOV-2025
DEFINITION  cellular tumor antigen p53 isoform g [Homo sapiens].
ACCESSION   NP_001263690
VERSION     NP_001263690.1
DBSOURCE    REFSEQ: accession NM_001276761.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Mirgayazova,R., Khadiullina,R., Chasov,V., Mingaleeva,R.,
            Miftakhova,R., Rizvanov,A. and Bulatov,E.
  TITLE     Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an Option?
  JOURNAL   Genes (Basel) 11 (6), 704 (2020)
   PUBMED   32630614
  REMARK    GeneRIF: Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an
            Option?
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Flynt,E., Bisht,K., Sridharan,V., Ortiz,M., Towfic,F. and
            Thakurta,A.
  TITLE     Prognosis, Biology, and Targeting of TP53 Dysregulation in Multiple
            Myeloma
  JOURNAL   Cells 9 (2), 287 (2020)
   PUBMED   31991614
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Barnoud,T., Parris,J.L.D. and Murphy,M.E.
  TITLE     Common genetic variants in the TP53 pathway and their impact on
            cancer
  JOURNAL   J Mol Cell Biol 11 (7), 578-585 (2019)
   PUBMED   31152665
  REMARK    GeneRIF: Common genetic variants in the TP53 pathway and their
            impact on cancer.
            Review article
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Hu,W., Chen,S., Thorne,R.F. and Wu,M.
  TITLE     TP53, TP53 Target Genes (DRAM, TIGAR), and Autophagy
  JOURNAL   Adv Exp Med Biol 1206, 127-149 (2019)
   PUBMED   31776983
  REMARK    Review article
REFERENCE   5  (residues 1 to 354)
  AUTHORS   Baugh,E.H., Ke,H., Levine,A.J., Bonneau,R.A. and Chan,C.S.
  TITLE     Why are there hotspot mutations in the TP53 gene in human cancers?
  JOURNAL   Cell Death Differ 25 (1), 154-160 (2018)
   PUBMED   29099487
  REMARK    GeneRIF: TP53 missense mutant alleles that occur in human cancers
            are discussed in the context of high resolution models of these p53
            mutant protein structures to determine the structural features of
            mutations (review).
            Review article
REFERENCE   6  (residues 1 to 354)
  AUTHORS   Aubrey,B.J., Strasser,A. and Kelly,G.L.
  TITLE     Tumor-Suppressor Functions of the TP53 Pathway
  JOURNAL   Cold Spring Harb Perspect Med 6 (5), a026062 (2016)
   PUBMED   27141080
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 354)
  AUTHORS   Soussi,T. and Wiman,K.G.
  TITLE     TP53: an oncogene in disguise
  JOURNAL   Cell Death Differ 22 (8), 1239-1249 (2015)
   PUBMED   26024390
  REMARK    Review article
REFERENCE   8  (residues 1 to 354)
  AUTHORS   Soussi,T.
  TITLE     The TP53 gene network in a postgenomic era
  JOURNAL   Hum Mutat 35 (6), 641-642 (2014)
   PUBMED   24753184
  REMARK    GeneRIF: Recommendations and guidelines for reporting and
            annotating TP53 variants are also provided, to help researchers
            generate standardized data that are easy to understand, analyze,
            and exchange across various cancer variant databases
            Review article
REFERENCE   9  (residues 1 to 354)
  AUTHORS   Anczukow,O., Ware,M.D., Buisson,M., Zetoune,A.B.,
            Stoppa-Lyonnet,D., Sinilnikova,O.M. and Mazoyer,S.
  TITLE     Does the nonsense-mediated mRNA decay mechanism prevent the
            synthesis of truncated BRCA1, CHK2, and p53 proteins?
  JOURNAL   Hum Mutat 29 (1), 65-73 (2008)
   PUBMED   17694537
  REMARK    GeneRIF: the p53 protein encoded by the 770delT allele is as
            abundant as the wild-type protein, as removal of the C-terminal p53
            domain leads to a stabilized mutant protein, whose abundance is
            markedly increased when NMD is inhibited.
REFERENCE   10 (residues 1 to 354)
  AUTHORS   Bourdon,J.C.
  TITLE     p53 Family isoforms
  JOURNAL   Curr Pharm Biotechnol 8 (6), 332-336 (2007)
   PUBMED   18289041
  REMARK    Review article
REFERENCE   11 (residues 1 to 354)
  AUTHORS   Candeias,M.M., Powell,D.J., Roubalova,E., Apcher,S., Bourougaa,K.,
            Vojtesek,B., Bruzzoni-Giovanelli,H. and Fahraeus,R.
  TITLE     Expression of p53 and p53/47 are controlled by alternative
            mechanisms of messenger RNA translation initiation
  JOURNAL   Oncogene 25 (52), 6936-6947 (2006)
   PUBMED   16983332
  REMARK    GeneRIF: harbouring alternative translation initiation sites, the
            p53 mRNA gives rise to different levels of the p53 isoforms which
            help to orchestrate the cell biological outcome of p53 activation
REFERENCE   12 (residues 1 to 354)
  AUTHORS   Murray-Zmijewski,F., Lane,D.P. and Bourdon,J.C.
  TITLE     p53/p63/p73 isoforms: an orchestra of isoforms to harmonise cell
            differentiation and response to stress
  JOURNAL   Cell Death Differ 13 (6), 962-972 (2006)
   PUBMED   16601753
  REMARK    Review article
REFERENCE   13 (residues 1 to 354)
  AUTHORS   Bourdon,J.C., Fernandes,K., Murray-Zmijewski,F., Liu,G., Diot,A.,
            Xirodimas,D.P., Saville,M.K. and Lane,D.P.
  TITLE     p53 isoforms can regulate p53 transcriptional activity
  JOURNAL   Genes Dev 19 (18), 2122-2137 (2005)
   PUBMED   16131611
  REMARK    GeneRIF: p53 isoforms can regulate p53 transcriptional activity.
REFERENCE   14 (residues 1 to 354)
  AUTHORS   Ghosh,A., Stewart,D. and Matlashewski,G.
  TITLE     Regulation of human p53 activity and cell localization by
            alternative splicing
  JOURNAL   Mol Cell Biol 24 (18), 7987-7997 (2004)
   PUBMED   15340061
  REMARK    GeneRIF: mechanism of p53 regulation originating through
            alternative splicing of the human p53 gene resulting in the
            expression of a novel p53 mRNA
REFERENCE   15 (residues 1 to 354)
  AUTHORS   Flaman,J.M., Waridel,F., Estreicher,A., Vannier,A., Limacher,J.M.,
            Gilbert,D., Iggo,R. and Frebourg,T.
  TITLE     The human tumour suppressor gene p53 is alternatively spliced in
            normal cells
  JOURNAL   Oncogene 12 (4), 813-818 (1996)
   PUBMED   8632903
REFERENCE   16 (residues 1 to 354)
  AUTHORS   Schneider,K., Zelley,K., Nichols,K.E., Schwartz Levine,A. and
            Garber,J.
  TITLE     Li-Fraumeni Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301488
REFERENCE   17 (residues 1 to 354)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   18 (residues 1 to 354)
  AUTHORS   Lamb,P. and Crawford,L.
  TITLE     Characterization of the human p53 gene
  JOURNAL   Mol Cell Biol 6 (5), 1379-1385 (1986)
   PUBMED   2946935
REFERENCE   19 (residues 1 to 354)
  AUTHORS   Isobe,M., Emanuel,B.S., Givol,D., Oren,M. and Croce,C.M.
  TITLE     Localization of gene for human p53 tumour antigen to band 17p13
  JOURNAL   Nature 320 (6057), 84-85 (1986)
   PUBMED   3456488
REFERENCE   20 (residues 1 to 354)
  AUTHORS   Benchimol,S., Lamb,P., Crawford,L.V., Sheer,D., Shows,T.B.,
            Bruns,G.A. and Peacock,J.
  TITLE     Transformation associated p53 protein is encoded by a gene on human
            chromosome 17
  JOURNAL   Somat Cell Mol Genet 11 (5), 505-510 (1985)
   PUBMED   2994241
REFERENCE   21 (residues 1 to 354)
  AUTHORS   Harlow,E., Williamson,N.M., Ralston,R., Helfman,D.M. and Adams,T.E.
  TITLE     Molecular cloning and in vitro expression of a cDNA clone for human
            cellular tumor antigen p53
  JOURNAL   Mol Cell Biol 5 (7), 1601-1610 (1985)
   PUBMED   3894933
REFERENCE   22 (residues 1 to 354)
  AUTHORS   Zakut-Houri,R., Bienz-Tadmor,B., Givol,D. and Oren,M.
  TITLE     Human p53 cellular tumor antigen: cDNA sequence and expression in
            COS cells
  JOURNAL   EMBO J 4 (5), 1251-1255 (1985)
   PUBMED   4006916
REFERENCE   23 (residues 1 to 354)
  AUTHORS   Matlashewski,G., Lamb,P., Pim,D., Peacock,J., Crawford,L. and
            Benchimol,S.
  TITLE     Isolation and characterization of a human p53 cDNA clone:
            expression of the human p53 gene
  JOURNAL   EMBO J 3 (13), 3257-3262 (1984)
   PUBMED   6396087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA453049.1, AB082923.1,
            X02469.1 and AK223026.1.
            
            Summary: This gene encodes a tumor suppressor protein containing
            transcriptional activation, DNA binding, and oligomerization
            domains. The encoded protein responds to diverse cellular stresses
            to regulate expression of target genes, thereby inducing cell cycle
            arrest, apoptosis, senescence, DNA repair, or changes in
            metabolism. Mutations in this gene are associated with a variety of
            human cancers, including hereditary cancers such as Li-Fraumeni
            syndrome. Alternative splicing of this gene and the use of
            alternate promoters result in multiple transcript variants and
            isoforms. Additional isoforms have also been shown to result from
            the use of alternate translation initiation codons from identical
            transcript variants (PMIDs: 12032546, 20937277). [provided by
            RefSeq, Dec 2016].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 5' UTR, compared to variant 1. This variant can initiate
            translation from two in-frame AUG start codons. The isoform
            represented in this variant (g, also known as delta40p53alpha or
            deltaNp53) results from translation initiation at the downstream
            start codon. It has a shorter N-terminus, compared to isoform a.
            Variants 1, 2, and 8 encode isoform g.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB082923.1, SRR14038194.3914132.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:12032546)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..354
                     /product="cellular tumor antigen p53 isoform g"
                     /note="tumor protein 53; mutant tumor protein 53; cellular
                     tumor antigen p53; phosphoprotein p53;
                     transformation-related protein 53; antigen NY-CO-13; tumor
                     supressor p53"
                     /calculated_mol_wt=39189
     Region          1..20
                     /region_name="TAD2"
                     /note="Transactivation domain 2; pfam18521"
                     /db_xref="CDD:375947"
     Region          70..249
                     /region_name="P53"
                     /note="P53 DNA-binding domain; cd08367"
                     /db_xref="CDD:176262"
     Site            order(137,140,199,203)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:176262"
     Site            order(138..140,142)
                     /site_type="other"
                     /note="dimerization site [polypeptide binding]"
                     /db_xref="CDD:176262"
     Site            order(200,202,209,234,236..238,241)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176262"
     Region          280..319
                     /region_name="P53_tetramer"
                     /note="P53 tetramerization motif; pfam07710"
                     /db_xref="CDD:462238"
     CDS             1..354
                     /gene="TP53"
                     /gene_synonym="BCC7; BMFS5; LFS1; P53; TRP53"
                     /coded_by="NM_001276761.3:257..1321"
                     /note="isoform g is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS73969.1"
                     /db_xref="GeneID:7157"
                     /db_xref="HGNC:HGNC:11998"
                     /db_xref="MIM:191170"
ORIGIN      
        1 mddlmlspdd ieqwftedpg pdeaprmpea appvapapaa ptpaapapap swplsssvps
       61 qktyqgsygf rlgflhsgta ksvtctyspa lnkmfcqlak tcpvqlwvds tpppgtrvra
      121 maiykqsqhm tevvrrcphh ercsdsdgla ppqhlirveg nlrveylddr ntfrhsvvvp
      181 yeppevgsdc ttihynymcn sscmggmnrr piltiitled ssgnllgrns fevrvcacpg
      241 rdrrteeenl rkkgephhel ppgstkralp nntssspqpk kkpldgeyft lqirgrerfe
      301 mfrelneale lkdaqagkep ggsrahsshl kskkgqstsr hkklmfkteg pdsd
//
LOCUS       NP_001271210             594 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 4 regulatory subunit 3A
            isoform 3 [Homo sapiens].
ACCESSION   NP_001271210 XP_005267900
VERSION     NP_001271210.1
DBSOURCE    REFSEQ: accession NM_001284281.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Qadri,O., Bashir,S., Banday,M., Hilal,N., Majeed,Y., Fatima,N.I.,
            Pal,D. and Fazili,K.M.
  TITLE     Tumour suppressor protein sMEK1 links to IRE1 signalling pathway to
            modulate its activity during ER stress
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (7), 119774 (2024)
   PUBMED   38838857
  REMARK    GeneRIF: Tumour suppressor protein sMEK1 links to IRE1 signalling
            pathway to modulate its activity during ER stress.
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Kavousi,N., Tonge,D.P. and Mourtada-Maarabouni,M.
  TITLE     New insights into the functional role of protein phosphatase 4
            regulatory subunit PP4R3A/SMEK1 in the regulation of leukemic cell
            fate
  JOURNAL   Int J Biol Macromol 233, 123467 (2023)
   PUBMED   36731689
  REMARK    GeneRIF: New insights into the functional role of protein
            phosphatase 4 regulatory subunit PP4R3A/SMEK1 in the regulation of
            leukemic cell fate.
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 594)
  AUTHORS   Christopher,L., Napolioni,V., Khan,R.R., Han,S.S. and Greicius,M.D.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative
  TITLE     A variant in PPP4R3A protects against alzheimer-related metabolic
            decline
  JOURNAL   Ann Neurol 82 (6), 900-911 (2017)
   PUBMED   29130521
  REMARK    GeneRIF: A variant in PPP4R3A was associated with reduced metabolic
            decline in Alzheimer's disease patients.
REFERENCE   6  (residues 1 to 594)
  AUTHORS   Chen,G.I., Tisayakorn,S., Jorgensen,C., D'Ambrosio,L.M.,
            Goudreault,M. and Gingras,A.C.
  TITLE     PP4R4/KIAA1622 forms a novel stable cytosolic complex with
            phosphoprotein phosphatase 4
  JOURNAL   J Biol Chem 283 (43), 29273-29284 (2008)
   PUBMED   18715871
REFERENCE   7  (residues 1 to 594)
  AUTHORS   Chowdhury,D., Xu,X., Zhong,X., Ahmed,F., Zhong,J., Liao,J.,
            Dykxhoorn,D.M., Weinstock,D.M., Pfeifer,G.P. and Lieberman,J.
  TITLE     A PP4-phosphatase complex dephosphorylates gamma-H2AX generated
            during DNA replication
  JOURNAL   Mol Cell 31 (1), 33-46 (2008)
   PUBMED   18614045
REFERENCE   8  (residues 1 to 594)
  AUTHORS   Martin-Granados,C., Philp,A., Oxenham,S.K., Prescott,A.R. and
            Cohen,P.T.
  TITLE     Depletion of protein phosphatase 4 in human cells reveals essential
            roles in centrosome maturation, cell migration and the regulation
            of Rho GTPases
  JOURNAL   Int J Biochem Cell Biol 40 (10), 2315-2332 (2008)
   PUBMED   18487071
REFERENCE   9  (residues 1 to 594)
  AUTHORS   Gingras,A.C., Caballero,M., Zarske,M., Sanchez,A., Hazbun,T.R.,
            Fields,S., Sonenberg,N., Hafen,E., Raught,B. and Aebersold,R.
  TITLE     A novel, evolutionarily conserved protein phosphatase complex
            involved in cisplatin sensitivity
  JOURNAL   Mol Cell Proteomics 4 (11), 1725-1740 (2005)
   PUBMED   16085932
REFERENCE   10 (residues 1 to 594)
  AUTHORS   Mendoza,M.C., Du,F., Iranfar,N., Tang,N., Ma,H., Loomis,W.F. and
            Firtel,R.A.
  TITLE     Loss of SMEK, a novel, conserved protein, suppresses MEK1 null cell
            polarity, chemotaxis, and gene expression defects
  JOURNAL   Mol Cell Biol 25 (17), 7839-7853 (2005)
   PUBMED   16107728
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC038932.1, BC028088.1 and AI608781.1.
            
            On Sep 27, 2013 this sequence version replaced XP_005267900.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC038932.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2467147
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.12"
     Protein         1..594
                     /product="serine/threonine-protein phosphatase 4
                     regulatory subunit 3A isoform 3"
                     /note="serine/threonine-protein phosphatase 4 regulatory
                     subunit 3A; SMEK homolog 1, suppressor of mek1"
                     /calculated_mol_wt=67681
     Region          7..98
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          <66..118
                     /region_name="PP4R3"
                     /note="Phosphatase 4 regulatory subunit 3; pfam04802"
                     /db_xref="CDD:461435"
     Region          <86..163
                     /region_name="LPD_N"
                     /note="Lipoprotein N-terminal Domain; smart00638"
                     /db_xref="CDD:214755"
     CDS             1..594
                     /gene="PPP4R3A"
                     /gene_synonym="FLFL1; KIAA2010; MSTP033; PP4R3; PP4R3A;
                     SMEK1; smk-1; smk1"
                     /coded_by="NM_001284281.2:664..2448"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS61532.1"
                     /db_xref="GeneID:55671"
                     /db_xref="HGNC:HGNC:20219"
                     /db_xref="MIM:610351"
ORIGIN      
        1 mtdtrrrvkv ytlnedrqwd drgtghvssg yverlkgmsl lvraesdgsl lleskinpnt
       61 ayqkqqedek fltdlfaqlt deatdeekrq elvnflkefc afsqtlqpqn rdaffktlsn
      121 mgilpalevi lgmddtqvrs aatdifsylv eynpsmvref vmqeaqqndd vskklteqki
      181 tskdillinl iiehmicdtd pelggavqlm gllrtlvdpe nmlatankte kteflgffyk
      241 hcmhvltapl lanttedkps kddfqtaqll alvlelltfc vehhtyhikn yiinkdilrr
      301 vlvlmaskha flalcalrfk rkiiglkdef ynryimksfl fepvvkafln ngsrynlmns
      361 aiiemfefir vediksltah vienywkale dvdyvqtfkg lklrfeqqre rqdnpkldsm
      421 rsilrnhryr rdartledee emwfntdedd medgeavvsp sdktkndddi mdpiskfmer
      481 kklkeseeke vllktnlsgr qspsfklsls sgtktnltsq ssttnlpgsp gspgspgspg
      541 spgsvpknts qtaaittkgg lvglvdypdd dedddededk edtlplskka kfds
//
LOCUS       NP_001371736            1004 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 111 [Homo sapiens].
ACCESSION   NP_001371736
VERSION     NP_001371736.1
DBSOURCE    REFSEQ: accession NM_001384807.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1004)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1004)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1004)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1004)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1004)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1004)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1004)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1965299, SAMEA1966682
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1004
                     /product="microtubule-associated protein 4 isoform 111"
                     /note="MAP-4"
                     /calculated_mol_wt=104738
     Region          <496..840
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <852..873
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          875..904
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          906..936
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1004
                     /gene="MAP4"
                     /coded_by="NM_001384807.1:96..3110"
                     /note="isoform 111 is encoded by transcript variant 66"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgms pcntavvpqg wsvealnsph
      121 sesfvspeav aeppqptavp lelakeiema seerppaqal eimmglkttd mapsketema
      181 lakdmalatk tevalakdme sptkldvtla kdmqpsmesd malvkdmelp tekevalvkd
      241 vrwptetdvs saknvvlpte tevapakdvt llketerasp ikmdlapskd mgppkenkke
      301 teraspikmd lapskdmgpp kenkivpakd lvllseieva qandiisste issaekvals
      361 setevalard mtlppetnvi ltkdkalple aevapvkdma qlpeteiapa kdvapstvke
      421 vgllkdmspl setemalgkd vtpppetevv liknvclppe mevaltedqv palkteapla
      481 kdgvltlann vtpakdvppl seteatpvpi kdmeiaqtqk gisedshles lqdvgqsaap
      541 tfmispetvt gtgkkcslpa eedsvleklg erkpcnsqps elssetsgia rpeegrpvvs
      601 gtgndittpp nkelppspek ktkplattqp aktstskakt qptslpkqpa pttigglnkk
      661 pmslasglvp aappkrpava sarpsilpsk dvkpkpiada kapekrasps kpasapasrs
      721 gskstqtvak tttaaavast gpssrspstl lpkkptaikt egkpaevkkm taksvpadls
      781 rpkststssm kktttlsgta paagvvpsrv katpmpsrps ttpfidkkpt sakpssttpr
      841 lsrlatntsa pdlknvrskv gstenikhqp gggrvqiqnk kvdiskvssk cgskanikhk
      901 pgggdvkies qklnfkekaq akvgsldnvg hlpaggavkt egggseaplc pgppageepa
      961 iseaapeaga ptsasglngh ptlsgggdqr eaqtldsqiq etsi
//
LOCUS       NP_116162                712 aa            linear   PRI 21-NOV-2025
DEFINITION  DISP complex protein LRCH3 isoform 2 [Homo sapiens].
ACCESSION   NP_116162 XP_001127761
VERSION     NP_116162.1
DBSOURCE    REFSEQ: accession NM_032773.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 712)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 712)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 712)
  AUTHORS   O'Loughlin,T., Masters,T.A. and Buss,F.
  TITLE     The MYO6 interactome reveals adaptor complexes coordinating early
            endosome and cytoskeletal dynamics
  JOURNAL   EMBO Rep 19 (4) (2018)
   PUBMED   29467281
REFERENCE   6  (residues 1 to 712)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 712)
  AUTHORS   Foussard,H., Ferrer,P., Valenti,P., Polesello,C., Carreno,S. and
            Payre,F.
  TITLE     LRCH proteins: a novel family of cytoskeletal regulators
  JOURNAL   PLoS One 5 (8), e12257 (2010)
   PUBMED   20805893
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 712)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB454969.1, BC007504.2 and AK300466.1.
            
            On Mar 29, 2007 this sequence version replaced XP_001127761.1.
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            coding sequence compared to variant 1. The resulting isoform (2)
            has a shorter and distinct C-terminus compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC007504.2, SRR14038191.220684.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..712
                     /product="DISP complex protein LRCH3 isoform 2"
                     /note="leucine-rich repeat and calponin homology
                     domain-containing protein 3; leucine-rich repeats and
                     calponin homology (CH) domain containing 3; DISP complex
                     protein LRCH3"
                     /calculated_mol_wt=78671
     Region          56..290
                     /region_name="Mediates interaction with DOCK7.
                     /evidence=ECO:0000269|PubMed:29467281"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96II8.2)"
     Region          61..83
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <80..>286
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          84..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..145
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          152..174
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          175..197
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          198..218
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          220..242
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          243..261
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96II8.2)"
     Region          382..648
                     /region_name="Mediates direct interaction with MYO6.
                     /evidence=ECO:0000269|PubMed:29467281"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96II8.2)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19367720,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96II8.2)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96II8.2)"
     Region          568..590
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96II8.2)"
     Site            611
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96II8.2)"
     Region          621..653
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96II8.2)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96II8.2)"
     Region          657..>710
                     /region_name="CH_SF"
                     /note="calponin homology (CH) domain superfamily; cl00030"
                     /db_xref="CDD:469584"
     CDS             1..712
                     /gene="LRCH3"
                     /coded_by="NM_032773.4:26..2164"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3330.1"
                     /db_xref="GeneID:84859"
                     /db_xref="HGNC:HGNC:28637"
ORIGIN      
        1 maaaglvava aaaeysgtva sggnlpgvhc gpssgagpgf gpgswsrsld raleeaavtg
       61 vlslsgrklr efprgaanhd ltdttradls rnrlseipie achfvslenl nlyqnciryi
      121 peailnlqal tflnisrnql stlpvhlcnl plkvliasnn klvslpeeig hlrhlmeldv
      181 scneiqtips qignlealrd lnvrrnhlvh lpeelaelpl irldfscnki ttipvcyrnl
      241 rhlqtitldn nplqsppaqi cikgkvhifk ylniqackia pdlpdydrrp lgfgscheel
      301 yssrpygald sgfnsvdsgd krwsgneptd efsdlplrva eitkeqrlrr esqyqenrgs
      361 lvvtnggveh dldqidyids ctaeeeeaev rqpkgpdpds lssqfmayie qrrishegsp
      421 vkpvairefq ktedmrrylh qnrvpaepss llslsashnq lshtdlelhq rreqlvertr
      481 reaqlaalqy eeekirtkqi qrdavldfvk qkasqspqkq hplldgvdge cpfpsrrsqh
      541 tddsalcmsl sglnqvgcaa tlphssaftp lksddrpnal lsspatetvh hspaysfpaa
      601 iqrnqpqrpe sflfragvra etnkghaspl ppsaapttds tdsitgqnsr qreeelelid
      661 qlrkhieyrl kvslpcdlga altdgvvlch lanhvrprsv psihvpspav vs
//
LOCUS       NP_001139583             470 aa            linear   PRI 21-NOV-2025
DEFINITION  mesoderm induction early response protein 1 isoform g [Homo
            sapiens].
ACCESSION   NP_001139583
VERSION     NP_001139583.1
DBSOURCE    REFSEQ: accession NM_001146111.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Wang,S., Fairall,L., Pham,T.K., Ragan,T.J., Vashi,D., Collins,M.O.,
            Dominguez,C. and Schwabe,J.W.R.
  TITLE     A potential histone-chaperone activity for the MIER1 histone
            deacetylase complex
  JOURNAL   Nucleic Acids Res 51 (12), 6006-6019 (2023)
   PUBMED   37099381
  REMARK    GeneRIF: A potential histone-chaperone activity for the MIER1
            histone deacetylase complex.
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 470)
  AUTHORS   McCarthy,P.L., Mercer,F.C., Savicky,M.W., Carter,B.A., Paterno,G.D.
            and Gillespie,L.L.
  TITLE     Changes in subcellular localisation of MI-ER1 alpha, a novel
            oestrogen receptor-alpha interacting protein, is associated with
            breast cancer progression
  JOURNAL   Br J Cancer 99 (4), 639-646 (2008)
   PUBMED   18665173
  REMARK    GeneRIF: Loss of nuclear MI-ER1 alpha might contribute to the
            development of invasive breast carcinoma
REFERENCE   6  (residues 1 to 470)
  AUTHORS   Wang,L., Charroux,B., Kerridge,S. and Tsai,C.C.
  TITLE     Atrophin recruits HDAC1/2 and G9a to modify histone H3K9 and to
            determine cell fates
  JOURNAL   EMBO Rep 9 (6), 555-562 (2008)
   PUBMED   18451879
REFERENCE   7  (residues 1 to 470)
  AUTHORS   Ding,Z., Gillespie,L.L., Mercer,F.C. and Paterno,G.D.
  TITLE     The SANT domain of human MI-ER1 interacts with Sp1 to interfere
            with GC box recognition and repress transcription from its own
            promoter
  JOURNAL   J Biol Chem 279 (27), 28009-28016 (2004)
   PUBMED   15117948
  REMARK    GeneRIF: the association of hMI-ER1 with Sp1 represents a novel
            mechanism for the negative regulation of Sp1 target promoters
REFERENCE   8  (residues 1 to 470)
  AUTHORS   Ding,Z., Gillespie,L.L. and Paterno,G.D.
  TITLE     Human MI-ER1 alpha and beta function as transcriptional repressors
            by recruitment of histone deacetylase 1 to their conserved ELM2
            domain
  JOURNAL   Mol Cell Biol 23 (1), 250-258 (2003)
   PUBMED   12482978
  REMARK    GeneRIF: we investigated the role of hMI-ER1alpha and hMI-ER1beta
            in the regulation of transcription.We demonstrate that this
            repressor activity is due to interaction and recruitment of a
            trichostatin A-sensitive histone deacetylase 1 (HDAC1).
REFERENCE   9  (residues 1 to 470)
  AUTHORS   Paterno,G.D., Ding,Z., Lew,Y.Y., Nash,G.W., Mercer,F.C. and
            Gillespie,L.L.
  TITLE     Genomic organization of the human mi-er1 gene and characterization
            of alternatively spliced isoforms: regulated use of a facultative
            intron determines subcellular localization
  JOURNAL   Gene 295 (1), 79-88 (2002)
   PUBMED   12242014
  REMARK    GeneRIF: Results demonstrate that alternate use of a facultative
            intron regulates the subcellular localization of hMI-ER1 proteins
            and this may have important implications for hMI-ER1 function.
REFERENCE   10 (residues 1 to 470)
  AUTHORS   Paterno,G.D., Mercer,F.C., Chayter,J.J., Yang,X., Robb,J.D. and
            Gillespie,L.L.
  TITLE     Molecular cloning of human er1 cDNA and its differential expression
            in breast tumours and tumour-derived cell lines
  JOURNAL   Gene 222 (1), 77-82 (1998)
   PUBMED   9813250
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK302061.1, BC108726.1,
            AL500525.4 and BM987758.1.
            
            Summary: This gene encodes a protein that was first identified in
            Xenopus laevis by its role in a mesoderm induction early response
            (MIER). The encoded protein functions as a transcriptional
            regulator. Alternatively spliced transcript variants encode
            multiple isoforms, some of which lack a C-terminal nuclear
            localization signal. [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (7) lacks an alternate segment in
            the 3' coding region, compared to variant 1. The resulting isoform
            (g) has a shorter and distinct C-terminus, compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC108726.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..470
                     /product="mesoderm induction early response protein 1
                     isoform g"
                     /note="mesoderm induction early response protein 1;
                     mesoderm induction early response 1 homolog; mesoderm
                     induction early response 1, transcriptional regulator"
                     /calculated_mol_wt=53384
     Region          199..248
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          305..349
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(305,335..336,338..339,341..343,345..347)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          359..>436
                     /region_name="MIER1_3_C"
                     /note="Mesoderm induction early response protein 1/3
                     C-terminal; pfam19426"
                     /db_xref="CDD:437258"
     CDS             1..470
                     /gene="MIER1"
                     /gene_synonym="ER1; MI-ER1"
                     /coded_by="NM_001146111.2:222..1634"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS53328.1"
                     /db_xref="GeneID:57708"
                     /db_xref="HGNC:HGNC:29657"
                     /db_xref="MIM:616848"
ORIGIN      
        1 mfmfnwftdc lwtlflsnyq psvessspgg satsddhefd psadmlvhdf ddertleeee
       61 mmegetnfss eiedlaregd mpihellsly gygstvrlpe edeeeeeeee egeddedadn
      121 ddnsgcsgen keenikdssg qedetqssnd dpsqsvasqd aqeiirprrc kyfdtnseve
      181 eeseededyi psedwkkeim vgsmfqaeip vgicrykene kvyenddqll wdpeylpedk
      241 viiflkdasr rtgdekgvea ipegshikdn eqalyelvkc nfdteealrr lrfnvkaare
      301 elsvwteeec rnfeqglkay gkdfhliqan kvrtrsvgec vafyymwkks erydffaqqt
      361 rfgkkkynlh pgvtdymdrl ldesesaass rapsppptas nssnsqseke dgtvstanqn
      421 gvssngpgei lnkeevkveg lhingptgil qmllpvhfsa issranaflk
//
LOCUS       NP_001123561             625 aa            linear   PRI 21-NOV-2025
DEFINITION  lysine--tRNA ligase isoform 1 [Homo sapiens].
ACCESSION   NP_001123561
VERSION     NP_001123561.1
DBSOURCE    REFSEQ: accession NM_001130089.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Liu,Y., Luo,Z., Chen,X., Yang,X., Qi,Q., Alifu,M., Tao,C., Cui,W.,
            Liu,M. and Wang,W.
  TITLE     Determinants of the interaction between the 5'-leader of HIV-1
            genome and human lysyl-tRNA synthetase in reverse transcription
            primer release process
  JOURNAL   Biochem Biophys Res Commun 725, 150252 (2024)
   PUBMED   38878758
  REMARK    GeneRIF: Determinants of the interaction between the 5'-leader of
            HIV-1 genome and human lysyl-tRNA synthetase in reverse
            transcription primer release process.
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Tang,Y., Behrens,R.T., St Gelais,C., Wu,S., Vivekanandan,S.,
            Razin,E., Fang,P., Wu,L., Sherer,N. and Musier-Forsyth,K.
  TITLE     Human lysyl-tRNA synthetase phosphorylation promotes HIV-1 proviral
            DNA transcription
  JOURNAL   Nucleic Acids Res 51 (22), 12111-12123 (2023)
   PUBMED   37933844
  REMARK    GeneRIF: Human lysyl-tRNA synthetase phosphorylation promotes HIV-1
            proviral DNA transcription.
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Saettini,F., Guerra,F., Fazio,G., Bugarin,C., McMillan,H.J.,
            Ohtake,A., Ardissone,A., Itoh,M., Giglio,S., Cappuccio,G.,
            Giardino,G., Romano,R., Quadri,M., Gasperini,S., Moratto,D.,
            Chiarini,M., Akira,I., Fukuhara,Y., Hayakawa,I., Okazaki,Y.,
            Mauri,M., Piazza,R., Cazzaniga,G. and Biondi,A.
  TITLE     Antibody Deficiency in Patients with Biallelic KARS1 Mutations
  JOURNAL   J Clin Immunol 43 (8), 2115-2125 (2023)
   PUBMED   37770806
  REMARK    GeneRIF: Antibody Deficiency in Patients with Biallelic KARS1
            Mutations.
            Erratum:[J Clin Immunol. 2023 Nov;43(8):2126. doi:
            10.1007/s10875-023-01600-w. PMID: 37921915]
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Lee,D.H., Paik,E.S., Cho,Y.J., Lee,Y.Y., Lee,B., Lee,E.J.,
            Choi,J.J., Choi,C.H., Lee,S., Choi,J.W. and Lee,J.W.
  TITLE     Changes in subcellular localization of Lysyl-tRNA synthetase and
            the 67-kDa laminin receptor in epithelial ovarian cancer metastases
  JOURNAL   Cancer Biomark 35 (1), 99-109 (2022)
   PUBMED   35912727
  REMARK    GeneRIF: Changes in subcellular localization of Lysyl-tRNA
            synthetase and the 67-kDa laminin receptor in epithelial ovarian
            cancer metastases.
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Lamour,V., Quevillon,S., Diriong,S., N'Guyen,V.C., Lipinski,M. and
            Mirande,M.
  TITLE     Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme
            as a case of horizontal gene transfer
  JOURNAL   Proc Natl Acad Sci U S A 91 (18), 8670-8674 (1994)
   PUBMED   8078941
REFERENCE   7  (residues 1 to 625)
  AUTHORS   Shiba,K., Suzuki,N., Shigesada,K., Namba,Y., Schimmel,P. and
            Noda,T.
  TITLE     Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence
            of the anticodon-binding domain and acquisition of a new structural
            unit
  JOURNAL   Proc Natl Acad Sci U S A 91 (16), 7435-7439 (1994)
   PUBMED   8052601
REFERENCE   8  (residues 1 to 625)
  AUTHORS   Kaiser,E., Hu,B., Becher,S., Eberhard,D., Schray,B., Baack,M.,
            Hameister,H. and Knippers,R.
  TITLE     The human EPRS locus (formerly the QARS locus): a gene encoding a
            class I and a class II aminoacyl-tRNA synthetase
  JOURNAL   Genomics 19 (2), 280-290 (1994)
   PUBMED   8188258
REFERENCE   9  (residues 1 to 625)
  AUTHORS   Escalante,C. and Yang,D.C.
  TITLE     Expression of human aspartyl-tRNA synthetase in Escherichia coli.
            Functional analysis of the N-terminal putative amphiphilic helix
  JOURNAL   J Biol Chem 268 (8), 6014-6023 (1993)
   PUBMED   8449960
REFERENCE   10 (residues 1 to 625)
  AUTHORS   Norcum,M.T.
  TITLE     Structural analysis of the high molecular mass aminoacyl-tRNA
            synthetase complex. Effects of neutral salts and detergents
  JOURNAL   J Biol Chem 266 (23), 15398-15405 (1991)
   PUBMED   1651330
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC025287.8.
            
            Summary: Aminoacyl-tRNA synthetases are a class of enzymes that
            charge tRNAs with their cognate amino acids. Lysyl-tRNA synthetase
            is a homodimer localized to the cytoplasm which belongs to the
            class II family of tRNA synthetases. It has been shown to be a
            target of autoantibodies in the human autoimmune diseases,
            polymyositis or dermatomyositis. Alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF285758.1, SRR5189658.121957.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1"
     Protein         1..625
                     /product="lysine--tRNA ligase isoform 1"
                     /EC_number="6.1.1.6"
                     /note="lysine tRNA ligase; lysRS"
                     /calculated_mol_wt=71366
     Region          48..605
                     /region_name="PLN02502"
                     /note="lysyl-tRNA synthetase"
                     /db_xref="CDD:215278"
     Site            297..301
                     /site_type="other"
                     /note="motif 1"
                     /db_xref="CDD:238398"
     Site            order(329,351,353,359,363,515,522,525,529,581)
                     /site_type="active"
                     /db_xref="CDD:238398"
     Site            350..353
                     /site_type="other"
                     /note="motif 2"
                     /db_xref="CDD:238398"
     Site            578..581
                     /site_type="other"
                     /note="motif 3"
                     /db_xref="CDD:238398"
     CDS             1..625
                     /gene="KARS1"
                     /gene_synonym="CMTRIB; DEAPLE; DFNB89; KARS; KARS2; KRS;
                     LEPID"
                     /coded_by="NM_001130089.2:123..2000"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45532.1"
                     /db_xref="GeneID:3735"
                     /db_xref="HGNC:HGNC:6215"
                     /db_xref="MIM:601421"
ORIGIN      
        1 mltqaavrlv rgslrktswa ewghrelrlg qlapftaphk dksfsdqrse lkrrlkaekk
       61 vaekeakqke lsekqlsqat aaatnhttdn gvgpeeesvd pnqyykirsq aihqlkvnge
      121 dpyphkfhvd isltdfiqky shlqpgdhlt ditlkvagri hakrasggkl ifydlrgegv
      181 klqvmansrn ykseeefihi nnklrrgdii gvqgnpgktk kgelsiipye itllspclhm
      241 lphlhfglkd ketryrqryl dlilndfvrq kfiirskiit yirsfldelg fleietpmmn
      301 iipggavakp fityhneldm nlymriapel yhkmlvvggi drvyeigrqf rnegidlthn
      361 pefttcefym ayadyhdlme itekmvsgmv khitgsykvt yhpdgpegqa ydvdftppfr
      421 rinmveelek algmklpetn lfeteetrki lddicvakav ecppprttar lldklvgefl
      481 evtcinptfi cdhpqimspl akwhrskegl terfelfvmk keicnaytel ndpmrqrqlf
      541 eeqakakaag ddeamfiden fctaleyglp ptagwgmgid rvamfltdsn nikevllfpa
      601 mkpedkkenv attdtlestt vgtsv
//
LOCUS       NP_001362272             507 aa            linear   PRI 21-NOV-2025
DEFINITION  gamma-aminobutyric acid receptor subunit gamma-2 isoform 8
            precursor [Homo sapiens].
ACCESSION   NP_001362272
VERSION     NP_001362272.1
DBSOURCE    REFSEQ: accession NM_001375343.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Zhou,J., Noviello,C.M., Teng,J., Moore,H., Lega,B. and Hibbs,R.E.
  TITLE     Resolving native GABAA receptor structures from the human brain
  JOURNAL   Nature 638 (8050), 562-568 (2025)
   PUBMED   39843743
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Sui,J., Zhan,L., Ji,S., Wu,W., Chen,Y., Yun,F., Liang,W., Wang,J.,
            Cao,M., Shen,D. and Zhang,Q.
  TITLE     Differential inflammation responses determine the variable
            phenotypes of epilepsy induced by GABRG2 mutations
  JOURNAL   CNS Neurosci Ther 30 (2), e14583 (2024)
   PUBMED   38357846
  REMARK    GeneRIF: Differential inflammation responses determine the variable
            phenotypes of epilepsy induced by GABRG2 mutations.
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Zhang,Q., Forster-Gibson,C., Bercovici,E., Bernardo,A., Ding,F.,
            Shen,W., Langer,K., Rex,T. and Kang,J.Q.
  TITLE     Epilepsy plus blindness in microdeletion of GABRA1 and GABRG2 in
            mouse and human
  JOURNAL   Exp Neurol 369, 114537 (2023)
   PUBMED   37703949
  REMARK    GeneRIF: Epilepsy plus blindness in microdeletion of GABRA1 and
            GABRG2 in mouse and human.
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Ma,M., Zhao,J., Xie,D. and Chen,J.
  TITLE     Association between GABRG2 Gene Single Nucleotide Polymorphisms and
            Susceptibility to Ischemic Stroke in a Chinese Population
  JOURNAL   J Integr Neurosci 22 (6), 151 (2023)
   PUBMED   38176934
  REMARK    GeneRIF: Association between GABRG2 Gene Single Nucleotide
            Polymorphisms and Susceptibility to Ischemic Stroke in a Chinese
            Population.
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Bengtsson,S.K.S., Sjostedt,J., Malinina,E., Das,R., Doverskog,M.,
            Johansson,M., Haage,D. and Backstrom,T.
  TITLE     Extra-Synaptic GABAA Receptor Potentiation and Neurosteroid-Induced
            Learning Deficits Are Inhibited by GR3027, a GABAA Modulating
            Steroid Antagonist
  JOURNAL   Biomolecules 13 (10), 1496 (2023)
   PUBMED   37892178
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 507)
  AUTHORS   Kostrzewa,M., Kohler,A., Eppelt,K., Hellam,L., Fairweather,N.D.,
            Levy,E.R., Monaco,A.P. and Muller,U.
  TITLE     Assignment of genes encoding GABAA receptor subunits alpha 1, alpha
            6, beta 2, and gamma 2 to a YAC contig of 5q33
  JOURNAL   Eur J Hum Genet 4 (4), 199-204 (1996)
   PUBMED   8875185
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Russek,S.J. and Farb,D.H.
  TITLE     Mapping of the beta 2 subunit gene (GABRB2) to microdissected human
            chromosome 5q34-q35 defines a gene cluster for the most abundant
            GABAA receptor isoform
  JOURNAL   Genomics 23 (3), 528-533 (1994)
   PUBMED   7851879
REFERENCE   8  (residues 1 to 507)
  AUTHORS   Moss,S.J., Doherty,C.A. and Huganir,R.L.
  TITLE     Identification of the cAMP-dependent protein kinase and protein
            kinase C phosphorylation sites within the major intracellular
            domains of the beta 1, gamma 2S, and gamma 2L subunits of the
            gamma-aminobutyric acid type A receptor
  JOURNAL   J Biol Chem 267 (20), 14470-14476 (1992)
   PUBMED   1321150
REFERENCE   9  (residues 1 to 507)
  AUTHORS   Wilcox,A.S., Warrington,J.A., Gardiner,K., Berger,R., Whiting,P.,
            Altherr,M.R., Wasmuth,J.J., Patterson,D. and Sikela,J.M.
  TITLE     Human chromosomal localization of genes encoding the gamma 1 and
            gamma 2 subunits of the gamma-aminobutyric acid receptor indicates
            that members of this gene family are often clustered in the genome
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5857-5861 (1992)
   PUBMED   1321425
REFERENCE   10 (residues 1 to 507)
  AUTHORS   Pritchett,D.B., Sontheimer,H., Shivers,B.D., Ymer,S.,
            Kettenmann,H., Schofield,P.R. and Seeburg,P.H.
  TITLE     Importance of a novel GABAA receptor subunit for benzodiazepine
            pharmacology
  JOURNAL   Nature 338 (6216), 582-585 (1989)
   PUBMED   2538761
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008611.6, AC091926.4 and
            AC091984.3.
            
            Summary: This gene encodes a gamma-aminobutyric acid (GABA)
            receptor. GABA is the major inhibitory neurotransmitter in the
            mammlian brain, where it acts at GABA-A receptors, which are
            ligand-gated chloride channels. GABA-A receptors are pentameric,
            consisting of proteins from several subunit classes: alpha, beta,
            gamma, delta and rho. Mutations in this gene have been associated
            with epilepsy and febrile seizures. Multiple transcript variants
            encoding different isoforms have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD014120.1, SRR1660807.93334.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..507
                     /product="gamma-aminobutyric acid receptor subunit gamma-2
                     isoform 8 precursor"
                     /note="gamma-aminobutyric acid receptor subunit gamma-2;
                     GABA(A) receptor subunit gamma-2; GABA(A) receptor, gamma
                     2; gamma-aminobutyric acid (GABA) A receptor, gamma 2;
                     gamma-aminobutyric acid type A receptor gamma2 subunit;
                     GABAAR subunit gamma-2"
                     /calculated_mol_wt=53884
     sig_peptide     1..40
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4455
     Region          69..504
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     Region          90..311
                     /region_name="LGIC_ECD_GABAAR_G"
                     /note="extracellular domain of gamma-aminobutyric acid
                     receptor subunit gamma; cd19000"
                     /db_xref="CDD:349801"
     Site            order(97,116)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:349801"
     Site            order(100,102..103,108..109,116,118..119,136,138..139,
                     148..153,156,158,160..161,167..169,171,181..183,211,311)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349801"
     Region          190..204
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349801"
     CDS             1..507
                     /gene="GABRG2"
                     /gene_synonym="CAE2; DEE74; ECA2; EIEE74; FEB8; GEFSP3"
                     /coded_by="NM_001375343.1:536..2059"
                     /note="isoform 8 precursor is encoded by transcript
                     variant 8"
                     /db_xref="CCDS:CCDS93813.1"
                     /db_xref="GeneID:2566"
                     /db_xref="HGNC:HGNC:4087"
                     /db_xref="MIM:137164"
ORIGIN      
        1 msspniwstg ssvystpvfs qkmtvwilll lslypgftsq ksdddyedya snktwvltpk
       61 vpegdvtvil nnllegydnk lrpdigvkpt lihtdmyvns igpvnainme ytidiffaqt
      121 wydrrlkfns tikvlrlnsn mvgkiwipdt ffrnskkada hwittpnrml riwndgrvly
      181 tlrltidaec qlqlhnfpmd ehscplefss wsrsiaqagm csgvisahys lrfwgstdpp
      241 tlasrvagis dgypreeivy qwkrssvevg dtrswrlyqf sfvglrntte vvkttsgdyv
      301 vmsvyfdlsr rmgyftiqty ipctlivvls wvsfwinkda vpartslgit tvltmttlst
      361 iarkslpkvs yvtamdlfvs vcfifvfsal veygtlhyfv snrkpskdkd kkkknpapti
      421 dirprsatiq mnnathlqer deeygyecld gkdcasffcc fedcrtgawr hgrihiriak
      481 mdsyariffp tafclfnlvy wvsylyl
//
LOCUS       NP_001317964             576 aa            linear   PRI 21-NOV-2025
DEFINITION  complement factor I isoform 3 preproprotein [Homo sapiens].
ACCESSION   NP_001317964 XP_005263033
VERSION     NP_001317964.1
DBSOURCE    REFSEQ: accession NM_001331035.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Moreno,R. and Broderick,L.
  TITLE     Complement factor I deficiency: Diverse phenotypes
  JOURNAL   J Allergy Clin Immunol 156 (2), 305-307 (2025)
   PUBMED   40127737
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Schwotzer,N., Fakhouri,F., Martins,P.V., Delmas,Y., Caillard,S.,
            Zuber,J., Moranne,O., Mesnard,L., Fremeaux-Bacchi,V. and
            El-Sissy,C.
  TITLE     Hot Spot of Complement Factor I Rare Variant p.Ile357Met in
            Patients With Hemolytic Uremic Syndrome
  JOURNAL   Am J Kidney Dis 84 (2), 244-249 (2024)
   PUBMED   38423159
  REMARK    GeneRIF: Hot Spot of Complement Factor I Rare Variant p.Ile357Met
            in Patients With Hemolytic Uremic Syndrome.
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Felberg,A., Bienkowski,M., Stokowy,T., Myszczynski,K.,
            Polakiewicz,Z., Kitowska,K., Sadej,R., Mohlin,F., Kuzniewska,A.,
            Kowalska,D., Stasilojc,G., Jongerius,I., Spaapen,R.,
            Mesa-Guzman,M., Montuenga,L.M., Blom,A.M., Pio,R. and Okroj,M.
  TITLE     Elevated expression of complement factor I in lung cancer cells
            associates with shorter survival-Potentially via non-canonical
            mechanism
  JOURNAL   Transl Res 269, 1-13 (2024)
   PUBMED   38395390
  REMARK    GeneRIF: Elevated expression of complement factor I in lung cancer
            cells associates with shorter survival-Potentially via
            non-canonical mechanism.
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Massey,V., Nguyen,C.E., Francois,T., De Bruycker,J.J., Bonnefoy,A.,
            Lapeyraque,A.L. and Decaluwe,H.
  TITLE     CNS Inflammation as the First Sign of Complement Factor I
            Deficiency: A Severe Myelitis Treated With Intense Immunotherapy
            and Eculizumab
  JOURNAL   Neurol Neuroimmunol Neuroinflamm 11 (2), e200191 (2024)
   PUBMED   38134378
  REMARK    GeneRIF: CNS Inflammation as the First Sign of Complement Factor I
            Deficiency.
REFERENCE   5  (residues 1 to 576)
  AUTHORS   van de Ven,J.P., Nilsson,S.C., Tan,P.L., Buitendijk,G.H.,
            Ristau,T., Mohlin,F.C., Nabuurs,S.B., Schoenmaker-Koller,F.E.,
            Smailhodzic,D., Campochiaro,P.A., Zack,D.J., Duvvari,M.R.,
            Bakker,B., Paun,C.C., Boon,C.J., Uitterlinden,A.G., Liakopoulos,S.,
            Klevering,B.J., Fauser,S., Daha,M.R., Katsanis,N., Klaver,C.C.,
            Blom,A.M., Hoyng,C.B. and den Hollander,A.I.
  TITLE     A functional variant in the CFI gene confers a high risk of
            age-related macular degeneration
  JOURNAL   Nat Genet 45 (7), 813-817 (2013)
   PUBMED   23685748
  REMARK    GeneRIF: these findings demonstrate that rare, highly penetrant
            mutations in CFI contribute to the genetic burden of age-related
            macular degeneration.
REFERENCE   6  (residues 1 to 576)
  AUTHORS   Martin,B. and Smith,R.J.H.
  TITLE     C3 Glomerulopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301598
REFERENCE   7  (residues 1 to 576)
  AUTHORS   Noris,M., Bresin,E., Mele,C. and Remuzzi,G.
  TITLE     Genetic Atypical Hemolytic-Uremic Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301541
REFERENCE   8  (residues 1 to 576)
  AUTHORS   DiScipio,R.G.
  TITLE     Ultrastructures and interactions of complement factors H and I
  JOURNAL   J Immunol 149 (8), 2592-2599 (1992)
   PUBMED   1401896
REFERENCE   9  (residues 1 to 576)
  AUTHORS   Shiang,R., Murray,J.C., Morton,C.C., Buetow,K.H., Wasmuth,J.J.,
            Olney,A.H., Sanger,W.G. and Goldberger,G.
  TITLE     Mapping of the human complement factor I gene to 4q25
  JOURNAL   Genomics 4 (1), 82-86 (1989)
   PUBMED   2563353
REFERENCE   10 (residues 1 to 576)
  AUTHORS   Catterall,C.F., Lyons,A., Sim,R.B., Day,A.J. and Harris,T.J.
  TITLE     Characterization of primary amino acid sequence of human complement
            control protein factor I from an analysis of cDNA clones
  JOURNAL   Biochem J 242 (3), 849-856 (1987)
   PUBMED   2954545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC392360.1, J02770.1,
            BX453590.1, AK290625.1, N63668.1 and BM955734.1.
            
            On Sep 3, 2016 this sequence version replaced XP_005263033.1.
            
            Summary: This gene encodes a serine proteinase that is essential
            for regulating the complement cascade. The encoded preproprotein is
            cleaved to produce both heavy and light chains, which are linked by
            disulfide bonds to form a heterodimeric glycoprotein. This
            heterodimer can cleave and inactivate the complement components C4b
            and C3b, and it prevents the assembly of the C3 and C5 convertase
            enzymes. Defects in this gene cause complement factor I deficiency,
            an autosomal recessive disease associated with a susceptibility to
            pyogenic infections. Mutations in this gene have been associated
            with a predisposition to atypical hemolytic uremic syndrome, a
            disease characterized by acute renal failure, microangiopathic
            hemolytic anemia and thrombocytopenia. Primary glomerulonephritis
            with immune deposits and age-related macular degeneration are other
            conditions associated with mutations of this gene. [provided by
            RefSeq, Dec 2015].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon in the central coding region compared to variant 2. The
            encoded isoform (3) lacks a portion of the heavy chain compared to
            isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.170721.1,
                                           SRR1660803.237646.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..576
                     /product="complement factor I isoform 3 preproprotein"
                     /EC_number="3.4.21.45"
                     /note="C3b-inactivator; Konglutinogen-activating factor;
                     complement factor I heavy chain; complement component I;
                     C3B/C4B inactivator; complement control protein factor I;
                     light chain of factor I"
                     /calculated_mol_wt=62797
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2281
     mat_peptide     19..328
                     /product="Complement factor I heavy chain"
                     /inference="EXISTENCE: similar to protein (same species):
                     RefSeq:NP_000195.2"
                     /calculated_mol_wt=34626
     Region          43..108
                     /region_name="FIMAC"
                     /note="factor I membrane attack complex; smart00057"
                     /db_xref="CDD:214493"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Region          114..215
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     Region          224..256
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(227,235,246..247)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(239,242,246,252..253)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            249..253
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          257..293
                     /region_name="Ldl_recept_a"
                     /note="Low-density lipoprotein receptor domain class A;
                     pfam00057"
                     /db_xref="CDD:395011"
     Site            order(264,272,283..284)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(276,279,283,289..290)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            286..290
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     mat_peptide     333..576
                     /product="Complement factor I light chain.
                     /id=PRO_0000027570"
                     /note="propagated from UniProtKB/Swiss-Prot (P05156.2)"
                     /calculated_mol_wt=27593
     Region          333..565
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            333
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(373,422,518)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            457
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Site            487
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Site            order(512,538,540)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     Site            529
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     CDS             1..576
                     /gene="CFI"
                     /gene_synonym="AHUS3; ARMD13; C3b-INA; C3BINA; FI; IF;
                     KAF"
                     /coded_by="NM_001331035.2:29..1759"
                     /note="isoform 3 preproprotein is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS82945.1"
                     /db_xref="GeneID:3426"
                     /db_xref="HGNC:HGNC:5394"
                     /db_xref="MIM:217030"
ORIGIN      
        1 mkllhvfllf lcfhlrfckv tytsqedlve kkclakkyth lscdkvfcqp wqrciegtcv
       61 cklpyqcpkn gtavcatnrr sfptycqqks leclhpgtkf lnngtctaeg kfsvslkhgn
      121 tdsegivevk lvdqdktmfi cksswsmrea nvacldlgfq qgadtqrrfk lsdlsinste
      181 clhvhcrgle tslaectftk rrtmgyqdfa dvvcytqkad spmddffqcv ngkyisqmka
      241 cdgindcgdq sdelcckacq gkgfhcksgv cipsqyqcng evdcitgede vgcaeeteil
      301 tadmdaerrr iksllpklsc gvknrmhirr krivggkraq lgdlpwqvai kdasgitcgg
      361 iyiggcwilt aahclraskt hryqiwttvv dwihpdlkri vieyvdriif henynagtyq
      421 ndialiemkk dgnkkdcelp rsipacvpws pylfqpndtc ivsgwgrekd nervfslqwg
      481 evklisncsk fygnrfyeke mecagtydgs idackgdsgg plvcmdannv tyvwgvvswg
      541 encgkpefpg vytkvanyfd wisyhvgrpf isqynv
//
LOCUS       NP_001386807             363 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA damage-binding protein 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001386807
VERSION     NP_001386807.1
DBSOURCE    REFSEQ: accession NM_001399878.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Zhang,C., Li,W., Liu,L., Li,M., Sun,H., Zhang,C., Zhong,L.,
            Huang,J. and Li,T.
  TITLE     DDB2 promotes melanoma cell growth by transcriptionally regulating
            the expression of KMT2A and predicts a poor prognosis
  JOURNAL   FASEB J 38 (12), e23735 (2024)
   PUBMED   38860936
  REMARK    GeneRIF: DDB2 promotes melanoma cell growth by transcriptionally
            regulating the expression of KMT2A and predicts a poor prognosis.
REFERENCE   3  (residues 1 to 363)
  AUTHORS   de Souza Timoteo,A.R., Pinheiro de Almeida,I.C., Yurchenko,A.A., de
            Miranda Henriques,S.R., de Souza Segundo,P., Rajabi,F., Nikolaev,S.
            and Petta,T.B.
  TITLE     Brazilian XP-E siblings carrying a novel DDB2 variant developed
            early-onset melanoma: a case report
  JOURNAL   BMC Med Genomics 16 (1), 186 (2023)
   PUBMED   37573316
  REMARK    GeneRIF: Brazilian XP-E siblings carrying a novel DDB2 variant
            developed early-onset melanoma: a case report.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Schule,S., Bristy,E.A., Muhtadi,R., Kaletka,G., Stewart,S.,
            Ostheim,P., Hermann,C., Asang,C., Pleimes,D., Port,M. and Abend,M.
  TITLE     Four Genes Predictive for the Severity of Hematological Damage
            Reveal a Similar Response after X Irradiation and Chemotherapy
  JOURNAL   Radiat Res 199 (2), 115-123 (2023)
   PUBMED   36480042
  REMARK    GeneRIF: Four Genes Predictive for the Severity of Hematological
            Damage Reveal a Similar Response after X Irradiation and
            Chemotherapy.
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Wang,X., Huang,Z., Li,L., Yang,Y., Zhang,J., Wang,L., Yuan,J. and
            Li,Y.
  TITLE     The Role of Alternative Splicing Factors, DDB2-Related Ageing and
            DNA Damage Repair in the Progression and Prognosis of Stomach
            Adenocarcinoma Patients
  JOURNAL   Genes (Basel) 14 (1), 39 (2022)
   PUBMED   36672781
  REMARK    GeneRIF: The Role of Alternative Splicing Factors, DDB2-Related
            Ageing and DNA Damage Repair in the Progression and Prognosis of
            Stomach Adenocarcinoma Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 363)
  AUTHORS   Hayes,S., Shiyanov,P., Chen,X. and Raychaudhuri,P.
  TITLE     DDB, a putative DNA repair protein, can function as a
            transcriptional partner of E2F1
  JOURNAL   Mol Cell Biol 18 (1), 240-249 (1998)
   PUBMED   9418871
REFERENCE   7  (residues 1 to 363)
  AUTHORS   Nichols,A.F., Ong,P. and Linn,S.
  TITLE     Mutations specific to the xeroderma pigmentosum group E Ddb-
            phenotype
  JOURNAL   J Biol Chem 271 (40), 24317-24320 (1996)
   PUBMED   8798680
REFERENCE   8  (residues 1 to 363)
  AUTHORS   Dualan,R., Brody,T., Keeney,S., Nichols,A.F., Admon,A. and Linn,S.
  TITLE     Chromosomal localization and cDNA cloning of the genes (DDB1 and
            DDB2) for the p127 and p48 subunits of a human damage-specific DNA
            binding protein
  JOURNAL   Genomics 29 (1), 62-69 (1995)
   PUBMED   8530102
REFERENCE   9  (residues 1 to 363)
  AUTHORS   Keeney,S., Chang,G.J. and Linn,S.
  TITLE     Characterization of a human DNA damage binding protein implicated
            in xeroderma pigmentosum E
  JOURNAL   J Biol Chem 268 (28), 21293-21300 (1993)
   PUBMED   8407967
REFERENCE   10 (residues 1 to 363)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC090589.9 and AC018410.24.
            
            Summary: This gene encodes a protein that is necessary for the
            repair of ultraviolet light-damaged DNA. This protein is the
            smaller subunit of a heterodimeric protein complex that
            participates in nucleotide excision repair, and this complex
            mediates the ubiquitylation of histones H3 and H4, which
            facilitates the cellular response to DNA damage. This subunit
            appears to be required for DNA binding. Mutations in this gene
            cause xeroderma pigmentosum complementation group E, a recessive
            disease that is characterized by an increased sensitivity to UV
            light and a high predisposition for skin cancer development, in
            some cases accompanied by neurological abnormalities. Two
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB107039.1, SRR18074969.3470352.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..363
                     /product="DNA damage-binding protein 2 isoform 3"
                     /note="xeroderma pigmentosum group E protein; UV-damaged
                     DNA-binding protein 2; DDB p48 subunit; DNA damage-binding
                     protein 2; damage-specific DNA binding protein 2, 48kDa"
                     /calculated_mol_wt=40641
     Region          87..355
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(90..91,110,114,120..121,132,134,153,158,164..165,
                     177,195,200,206..207,222..223,241,245,251..252,264..265,
                     288,294,311..312,324..325,345,354..355)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          96..131
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          141..176
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          182..222
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          227..263
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          276..323
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..363
                     /gene="DDB2"
                     /gene_synonym="DDBB; UV-DDB2; XPE"
                     /coded_by="NM_001399878.1:164..1255"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS91469.1"
                     /db_xref="GeneID:1643"
                     /db_xref="HGNC:HGNC:2718"
                     /db_xref="MIM:600811"
ORIGIN      
        1 mapkkrpetq ktseivlrpr nkrsrsplel epeakklcak gsgpsrrcds dclwvglagp
       61 qilppcrsiv rtlhqhklgr aswpsvqqig aggsitglkf nplntnqfya ssmegttrlq
      121 dfkgnilrvf assdtiniwf csldvsassr mvvtgdnvgn villnmdgke lwnlrmhkkk
      181 vthvalnpcc dwflatasvd qtvkiwdlrq vrgkasflys lphrhpvnaa cfspdgarll
      241 ttdqkseirv ysasqwdcpl gliphphrhf qhltpikaaw hprynlivvg rypdpnfksc
      301 tpyelrtidv fdgnsgkmmc qlydpessgi sslnefnpmg dtlasamgyh iliwsqeear
      361 trk
//
LOCUS       NP_001130038             556 aa            linear   PRI 21-NOV-2025
DEFINITION  double-strand-break repair protein rad21-like protein 1 isoform 1
            [Homo sapiens].
ACCESSION   NP_001130038 XP_001717813
VERSION     NP_001130038.2
DBSOURCE    REFSEQ: accession NM_001136566.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Shi,Z., Gao,H., Bai,X.C. and Yu,H.
  TITLE     Cryo-EM structure of the human cohesin-NIPBL-DNA complex
  JOURNAL   Science 368 (6498), 1454-1459 (2020)
   PUBMED   32409525
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Minase,G., Miyamoto,T., Miyagawa,Y., Iijima,M., Ueda,H., Saijo,Y.,
            Namiki,M. and Sengoku,K.
  TITLE     Single-nucleotide polymorphisms in the human RAD21L gene may be a
            genetic risk factor for Japanese patients with azoospermia caused
            by meiotic arrest and Sertoli cell-only syndrome
  JOURNAL   Hum Fertil (Camb) 20 (3), 217-220 (2017)
   PUBMED   28635411
  REMARK    GeneRIF: The association of three single-nucleotide polymorphisms
            with azoospermia, especially Sertoli cell-only syndrome, was
            studied in Japanese men.
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Li,L., Fridley,B.L., Kalari,K., Niu,N., Jenkins,G., Batzler,A.,
            Abo,R.P., Schaid,D. and Wang,L.
  TITLE     Discovery of genetic biomarkers contributing to variation in drug
            response of cytidine analogues using human lymphoblastoid cell
            lines
  JOURNAL   BMC Genomics 15, 93 (2014)
   PUBMED   24483146
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 556)
  AUTHORS   Gutierrez-Caballero,C., Herran,Y., Sanchez-Martin,M., Suja,J.A.,
            Barbero,J.L., Llano,E. and Pendas,A.M.
  TITLE     Identification and molecular characterization of the mammalian
            alpha-kleisin RAD21L
  JOURNAL   Cell Cycle 10 (9), 1477-1487 (2011)
   PUBMED   21527826
  REMARK    GeneRIF: RAD21L is identified as a novel cohesin complex subunit
            homologous to mammalian RAD21/REC8/alpha-kleisin subfamily.
REFERENCE   5  (residues 1 to 556)
  AUTHORS   Baranzini,S.E., Wang,J., Gibson,R.A., Galwey,N., Naegelin,Y.,
            Barkhof,F., Radue,E.W., Lindberg,R.L., Uitdehaag,B.M.,
            Johnson,M.R., Angelakopoulou,A., Hall,L., Richardson,J.C.,
            Prinjha,R.K., Gass,A., Geurts,J.J., Kragt,J., Sombekke,M.,
            Vrenken,H., Qualley,P., Lincoln,R.R., Gomez,R., Caillier,S.J.,
            George,M.F., Mousavi,H., Guerrero,R., Okuda,D.T., Cree,B.A.,
            Green,A.J., Waubant,E., Goodin,D.S., Pelletier,D., Matthews,P.M.,
            Hauser,S.L., Kappos,L., Polman,C.H. and Oksenberg,J.R.
  TITLE     Genome-wide association analysis of susceptibility and clinical
            phenotype in multiple sclerosis
  JOURNAL   Hum Mol Genet 18 (4), 767-778 (2009)
   PUBMED   19010793
REFERENCE   6  (residues 1 to 556)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL031665.19.
            
            On Jan 29, 2009 this sequence version replaced NP_001130038.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC157891.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2161674 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..556
                     /product="double-strand-break repair protein rad21-like
                     protein 1 isoform 1"
                     /note="double-strand-break repair protein rad21-like
                     protein 1; RAD21-like 1"
                     /calculated_mol_wt=63193
     Region          1..100
                     /region_name="Rad21_Rec8_N"
                     /note="N terminus of Rad21 / Rec8 like protein; pfam04825"
                     /db_xref="CDD:461446"
     Region          290..370
                     /region_name="Rad21_Rec8_M_NXP1-like"
                     /note="Middle HEAT-repeat binding domain found in Homo
                     sapiens nuclear matrix protein 1 (NXP-1) and similar
                     proteins; cd21792"
                     /db_xref="CDD:439294"
     Site            order(296..298,301..308,311,314..315,317..318,320..327,
                     329..335,337..339,342..343,346..356,358..359,362..363,
                     365..370)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:439294"
     Region          502..553
                     /region_name="Rad21_Rec8"
                     /note="Conserved region of Rad21 / Rec8 like protein;
                     pfam04824"
                     /db_xref="CDD:335912"
     CDS             1..556
                     /gene="RAD21L1"
                     /gene_synonym="dJ545L17.2; RAD21L"
                     /coded_by="NM_001136566.3:170..1840"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46568.1"
                     /db_xref="GeneID:642636"
                     /db_xref="HGNC:HGNC:16271"
                     /db_xref="MIM:619533"
ORIGIN      
        1 mfythvlmsk rgplakiwla ahwekkltka hvfecnleit iekilspkvk ialrtsghll
       61 lgvvriynrk akylladcse aflkmkmtfc pglvdlpken feasynaitl peefhdfdtq
      121 nmnaidvseh ftqnqsrpee itlrenfdnd lifqaesfge eseilrrhsf fddnillnss
      181 gpliehssgs ltgerslfyd sgdgfgdega agemidnllq ddqnilledm hlnreislps
      241 eppnslavep dnsecicvpe nekmnetill steeegftld pidisdiaek rkgkkrrlli
      301 dpikelsskv ihkqltsfad tlmvlelapp tqrlmmwkkr ggvhtllsta aqdlihaelk
      361 mlftkcflss gfklgrkmiq kesvreevgn qnivetsmmq epnyqqelsk pqtwkdvigg
      421 sqhsshedtn kninseqdiv emvslaaees slmndlfaqe ieyspveles lsneeniete
      481 rwngrilqml nrlresnkmg mqsfslmklc rnsdrkqaaa kfysflvlkk qlaielsqsa
      541 pyadiiatmg pmfyni
//
LOCUS       NP_001340172             324 aa            linear   PRI 21-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 1 [Homo sapiens].
ACCESSION   NP_001340172
VERSION     NP_001340172.1
DBSOURCE    REFSEQ: accession NM_001353243.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            Transcript Variant: This variant (5) lacks two exons and includes
            three alternate exons in the 5' region, compared to variant 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC016345.1, SRR14038196.2616909.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 1"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=36617
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353243.2:477..1451"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS6361.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mgnllkvltc tdleqgpnff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqik smlq
//
LOCUS       NP_001263625             302 aa            linear   PRI 21-NOV-2025
DEFINITION  cellular tumor antigen p53 isoform i [Homo sapiens].
ACCESSION   NP_001263625
VERSION     NP_001263625.1
DBSOURCE    REFSEQ: accession NM_001276696.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Mirgayazova,R., Khadiullina,R., Chasov,V., Mingaleeva,R.,
            Miftakhova,R., Rizvanov,A. and Bulatov,E.
  TITLE     Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an Option?
  JOURNAL   Genes (Basel) 11 (6), 704 (2020)
   PUBMED   32630614
  REMARK    GeneRIF: Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an
            Option?
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Flynt,E., Bisht,K., Sridharan,V., Ortiz,M., Towfic,F. and
            Thakurta,A.
  TITLE     Prognosis, Biology, and Targeting of TP53 Dysregulation in Multiple
            Myeloma
  JOURNAL   Cells 9 (2), 287 (2020)
   PUBMED   31991614
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Barnoud,T., Parris,J.L.D. and Murphy,M.E.
  TITLE     Common genetic variants in the TP53 pathway and their impact on
            cancer
  JOURNAL   J Mol Cell Biol 11 (7), 578-585 (2019)
   PUBMED   31152665
  REMARK    GeneRIF: Common genetic variants in the TP53 pathway and their
            impact on cancer.
            Review article
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Hu,W., Chen,S., Thorne,R.F. and Wu,M.
  TITLE     TP53, TP53 Target Genes (DRAM, TIGAR), and Autophagy
  JOURNAL   Adv Exp Med Biol 1206, 127-149 (2019)
   PUBMED   31776983
  REMARK    Review article
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Baugh,E.H., Ke,H., Levine,A.J., Bonneau,R.A. and Chan,C.S.
  TITLE     Why are there hotspot mutations in the TP53 gene in human cancers?
  JOURNAL   Cell Death Differ 25 (1), 154-160 (2018)
   PUBMED   29099487
  REMARK    GeneRIF: TP53 missense mutant alleles that occur in human cancers
            are discussed in the context of high resolution models of these p53
            mutant protein structures to determine the structural features of
            mutations (review).
            Review article
REFERENCE   6  (residues 1 to 302)
  AUTHORS   Aubrey,B.J., Strasser,A. and Kelly,G.L.
  TITLE     Tumor-Suppressor Functions of the TP53 Pathway
  JOURNAL   Cold Spring Harb Perspect Med 6 (5), a026062 (2016)
   PUBMED   27141080
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 302)
  AUTHORS   Soussi,T. and Wiman,K.G.
  TITLE     TP53: an oncogene in disguise
  JOURNAL   Cell Death Differ 22 (8), 1239-1249 (2015)
   PUBMED   26024390
  REMARK    Review article
REFERENCE   8  (residues 1 to 302)
  AUTHORS   Soussi,T.
  TITLE     The TP53 gene network in a postgenomic era
  JOURNAL   Hum Mutat 35 (6), 641-642 (2014)
   PUBMED   24753184
  REMARK    GeneRIF: Recommendations and guidelines for reporting and
            annotating TP53 variants are also provided, to help researchers
            generate standardized data that are easy to understand, analyze,
            and exchange across various cancer variant databases
            Review article
REFERENCE   9  (residues 1 to 302)
  AUTHORS   Anczukow,O., Ware,M.D., Buisson,M., Zetoune,A.B.,
            Stoppa-Lyonnet,D., Sinilnikova,O.M. and Mazoyer,S.
  TITLE     Does the nonsense-mediated mRNA decay mechanism prevent the
            synthesis of truncated BRCA1, CHK2, and p53 proteins?
  JOURNAL   Hum Mutat 29 (1), 65-73 (2008)
   PUBMED   17694537
  REMARK    GeneRIF: the p53 protein encoded by the 770delT allele is as
            abundant as the wild-type protein, as removal of the C-terminal p53
            domain leads to a stabilized mutant protein, whose abundance is
            markedly increased when NMD is inhibited.
REFERENCE   10 (residues 1 to 302)
  AUTHORS   Bourdon,J.C.
  TITLE     p53 Family isoforms
  JOURNAL   Curr Pharm Biotechnol 8 (6), 332-336 (2007)
   PUBMED   18289041
  REMARK    Review article
REFERENCE   11 (residues 1 to 302)
  AUTHORS   Candeias,M.M., Powell,D.J., Roubalova,E., Apcher,S., Bourougaa,K.,
            Vojtesek,B., Bruzzoni-Giovanelli,H. and Fahraeus,R.
  TITLE     Expression of p53 and p53/47 are controlled by alternative
            mechanisms of messenger RNA translation initiation
  JOURNAL   Oncogene 25 (52), 6936-6947 (2006)
   PUBMED   16983332
  REMARK    GeneRIF: harbouring alternative translation initiation sites, the
            p53 mRNA gives rise to different levels of the p53 isoforms which
            help to orchestrate the cell biological outcome of p53 activation
REFERENCE   12 (residues 1 to 302)
  AUTHORS   Murray-Zmijewski,F., Lane,D.P. and Bourdon,J.C.
  TITLE     p53/p63/p73 isoforms: an orchestra of isoforms to harmonise cell
            differentiation and response to stress
  JOURNAL   Cell Death Differ 13 (6), 962-972 (2006)
   PUBMED   16601753
  REMARK    Review article
REFERENCE   13 (residues 1 to 302)
  AUTHORS   Bourdon,J.C., Fernandes,K., Murray-Zmijewski,F., Liu,G., Diot,A.,
            Xirodimas,D.P., Saville,M.K. and Lane,D.P.
  TITLE     p53 isoforms can regulate p53 transcriptional activity
  JOURNAL   Genes Dev 19 (18), 2122-2137 (2005)
   PUBMED   16131611
  REMARK    GeneRIF: p53 isoforms can regulate p53 transcriptional activity.
REFERENCE   14 (residues 1 to 302)
  AUTHORS   Ghosh,A., Stewart,D. and Matlashewski,G.
  TITLE     Regulation of human p53 activity and cell localization by
            alternative splicing
  JOURNAL   Mol Cell Biol 24 (18), 7987-7997 (2004)
   PUBMED   15340061
  REMARK    GeneRIF: mechanism of p53 regulation originating through
            alternative splicing of the human p53 gene resulting in the
            expression of a novel p53 mRNA
REFERENCE   15 (residues 1 to 302)
  AUTHORS   Flaman,J.M., Waridel,F., Estreicher,A., Vannier,A., Limacher,J.M.,
            Gilbert,D., Iggo,R. and Frebourg,T.
  TITLE     The human tumour suppressor gene p53 is alternatively spliced in
            normal cells
  JOURNAL   Oncogene 12 (4), 813-818 (1996)
   PUBMED   8632903
REFERENCE   16 (residues 1 to 302)
  AUTHORS   Schneider,K., Zelley,K., Nichols,K.E., Schwartz Levine,A. and
            Garber,J.
  TITLE     Li-Fraumeni Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301488
REFERENCE   17 (residues 1 to 302)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   18 (residues 1 to 302)
  AUTHORS   Lamb,P. and Crawford,L.
  TITLE     Characterization of the human p53 gene
  JOURNAL   Mol Cell Biol 6 (5), 1379-1385 (1986)
   PUBMED   2946935
REFERENCE   19 (residues 1 to 302)
  AUTHORS   Isobe,M., Emanuel,B.S., Givol,D., Oren,M. and Croce,C.M.
  TITLE     Localization of gene for human p53 tumour antigen to band 17p13
  JOURNAL   Nature 320 (6057), 84-85 (1986)
   PUBMED   3456488
REFERENCE   20 (residues 1 to 302)
  AUTHORS   Benchimol,S., Lamb,P., Crawford,L.V., Sheer,D., Shows,T.B.,
            Bruns,G.A. and Peacock,J.
  TITLE     Transformation associated p53 protein is encoded by a gene on human
            chromosome 17
  JOURNAL   Somat Cell Mol Genet 11 (5), 505-510 (1985)
   PUBMED   2994241
REFERENCE   21 (residues 1 to 302)
  AUTHORS   Harlow,E., Williamson,N.M., Ralston,R., Helfman,D.M. and Adams,T.E.
  TITLE     Molecular cloning and in vitro expression of a cDNA clone for human
            cellular tumor antigen p53
  JOURNAL   Mol Cell Biol 5 (7), 1601-1610 (1985)
   PUBMED   3894933
REFERENCE   22 (residues 1 to 302)
  AUTHORS   Zakut-Houri,R., Bienz-Tadmor,B., Givol,D. and Oren,M.
  TITLE     Human p53 cellular tumor antigen: cDNA sequence and expression in
            COS cells
  JOURNAL   EMBO J 4 (5), 1251-1255 (1985)
   PUBMED   4006916
REFERENCE   23 (residues 1 to 302)
  AUTHORS   Matlashewski,G., Lamb,P., Pim,D., Peacock,J., Crawford,L. and
            Benchimol,S.
  TITLE     Isolation and characterization of a human p53 cDNA clone:
            expression of the human p53 gene
  JOURNAL   EMBO J 3 (13), 3257-3262 (1984)
   PUBMED   6396087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA453049.1, DQ186648.1,
            DQ186649.1 and AK223026.1.
            
            Summary: This gene encodes a tumor suppressor protein containing
            transcriptional activation, DNA binding, and oligomerization
            domains. The encoded protein responds to diverse cellular stresses
            to regulate expression of target genes, thereby inducing cell cycle
            arrest, apoptosis, senescence, DNA repair, or changes in
            metabolism. Mutations in this gene are associated with a variety of
            human cancers, including hereditary cancers such as Li-Fraumeni
            syndrome. Alternative splicing of this gene and the use of
            alternate promoters result in multiple transcript variants and
            isoforms. Additional isoforms have also been shown to result from
            the use of alternate translation initiation codons from identical
            transcript variants (PMIDs: 12032546, 20937277). [provided by
            RefSeq, Dec 2016].
            
            Transcript Variant: This variant (3) contains an additional exon in
            the 3' region, resulting in an alternate 3' coding region and 3'
            UTR, compared to variant 1. This variant can initiate translation
            from two in-frame AUG start codons. The isoform represented in this
            variant (i, also known as delta40p53beta) results from translation
            initiation at the downstream start codon. It has a shorter
            N-terminus and a distinct C-terminus, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ186648.1, SRR14038196.3383531.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:12032546)
            NMD candidate                    :: translation inferred
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..302
                     /product="cellular tumor antigen p53 isoform i"
                     /note="tumor protein 53; mutant tumor protein 53; cellular
                     tumor antigen p53; phosphoprotein p53;
                     transformation-related protein 53; antigen NY-CO-13; tumor
                     supressor p53"
                     /calculated_mol_wt=33362
     Region          1..20
                     /region_name="TAD2"
                     /note="Transactivation domain 2; pfam18521"
                     /db_xref="CDD:375947"
     Region          70..249
                     /region_name="P53"
                     /note="P53 DNA-binding domain; cd08367"
                     /db_xref="CDD:176262"
     Site            order(137,140,199,203)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:176262"
     Site            order(138..140,142)
                     /site_type="other"
                     /note="dimerization site [polypeptide binding]"
                     /db_xref="CDD:176262"
     Site            order(200,202,209,234,236..238,241)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176262"
     CDS             1..302
                     /gene="TP53"
                     /gene_synonym="BCC7; BMFS5; LFS1; P53; TRP53"
                     /coded_by="NM_001276696.3:260..1168"
                     /note="isoform i is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS73971.1"
                     /db_xref="GeneID:7157"
                     /db_xref="HGNC:HGNC:11998"
                     /db_xref="MIM:191170"
ORIGIN      
        1 mddlmlspdd ieqwftedpg pdeaprmpea appvapapaa ptpaapapap swplsssvps
       61 qktyqgsygf rlgflhsgta ksvtctyspa lnkmfcqlak tcpvqlwvds tpppgtrvra
      121 maiykqsqhm tevvrrcphh ercsdsdgla ppqhlirveg nlrveylddr ntfrhsvvvp
      181 yeppevgsdc ttihynymcn sscmggmnrr piltiitled ssgnllgrns fevrvcacpg
      241 rdrrteeenl rkkgephhel ppgstkralp nntssspqpk kkpldgeyft lqdqtsfqke
      301 nc
//
LOCUS       NP_002292                332 aa            linear   PRI 21-NOV-2025
DEFINITION  L-lactate dehydrogenase C chain [Homo sapiens].
ACCESSION   NP_002292
VERSION     NP_002292.1
DBSOURCE    REFSEQ: accession NM_002301.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Naik,A. and Decock,J.
  TITLE     Targeting of lactate dehydrogenase C dysregulates the cell cycle
            and sensitizes breast cancer cells to DNA damage response targeted
            therapy
  JOURNAL   Mol Oncol 16 (4), 885-903 (2022)
   PUBMED   34050611
  REMARK    GeneRIF: Targeting of lactate dehydrogenase C dysregulates the cell
            cycle and sensitizes breast cancer cells to DNA damage response
            targeted therapy.
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Xiao,Z., Gong,R., Chen,X., Xiao,D., Luo,S. and Ji,Y.
  TITLE     Association between serum lactate dehydrogenase and 60-day
            mortality in Chinese Hakka patients with acute myeloid leukemia: A
            cohort study
  JOURNAL   J Clin Lab Anal 35 (12), e24049 (2021)
   PUBMED   34708888
  REMARK    GeneRIF: Association between serum lactate dehydrogenase and 60-day
            mortality in Chinese Hakka patients with acute myeloid leukemia: A
            cohort study.
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 332)
  AUTHORS   LeVan,K.M. and Goldberg,E.
  TITLE     Properties of human testis-specific lactate dehydrogenase expressed
            from Escherichia coli
  JOURNAL   Biochem J 273 (Pt 3) (Pt 3), 587-592 (1991)
   PUBMED   1996957
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Edwards,Y., West,L., Van Heyningen,V., Cowell,J. and Goldberg,E.
  TITLE     Regional localization of the sperm-specific lactate dehydrogenase,
            LDHC, gene on human chromosome 11
  JOURNAL   Ann Hum Genet 53 (3), 215-219 (1989)
   PUBMED   2596827
REFERENCE   8  (residues 1 to 332)
  AUTHORS   Takano,T. and Li,S.S.
  TITLE     Human testicular lactate dehydrogenase-C gene is interrupted by six
            introns at positions homologous to those of LDH-A (muscle) and
            LDH-B (heart) genes
  JOURNAL   Biochem Biophys Res Commun 159 (2), 579-583 (1989)
   PUBMED   2930531
REFERENCE   9  (residues 1 to 332)
  AUTHORS   Millan,J.L., Driscoll,C.E., LeVan,K.M. and Goldberg,E.
  TITLE     Epitopes of human testis-specific lactate dehydrogenase deduced
            from a cDNA sequence
  JOURNAL   Proc Natl Acad Sci U S A 84 (15), 5311-5315 (1987)
   PUBMED   2440048
REFERENCE   10 (residues 1 to 332)
  AUTHORS   Edwards,Y.H., Povey,S., LeVan,K.M., Driscoll,C.E., Millan,J.L. and
            Goldberg,E.
  TITLE     Locus determining the human sperm-specific lactate dehydrogenase,
            LDHC, is syntenic with LDHA
  JOURNAL   Dev Genet 8 (4), 219-232 (1987)
   PUBMED   2844458
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC084117.6 and AC027544.11.
            
            Summary:  Lactate dehydrogenase C catalyzes the conversion of
            L-lactate and NAD to pyruvate and NADH in the final step of
            anaerobic glycolysis.  LDHC is testis-specific and belongs to the
            lactate dehydrogenase family.  Two transcript variants have been
            detected which differ in the 5' untranslated region. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005647.1, BC064388.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.1"
     Protein         1..332
                     /product="L-lactate dehydrogenase C chain"
                     /EC_number="1.1.1.27"
                     /note="cancer/testis antigen 32; lactate dehydrogenase C4;
                     LDH-C; LDH-X; LDH testis subunit; testis secretory
                     sperm-binding protein Li 234P"
                     /calculated_mol_wt=36180
     Region          18..329
                     /region_name="LDH_1"
                     /note="A subgroup of L-lactate dehydrogenases; cd05293"
                     /db_xref="CDD:133429"
     Site            order(18,20,181,184,186,203,208,265..267,270,297..298,301,
                     303..305)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:133429"
     Site            order(29..31,52,54,57,95..99,136,138,161,165,193,248,252)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133429"
     Site            order(33,38,60..61,64,66..67,169,171..172,178,244..245,
                     248..251)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133429"
     Site            order(100,106,138,169,193,238,248)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133429"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P07864.4)"
     CDS             1..332
                     /gene="LDHC"
                     /gene_synonym="CT32; LDH3; LDHX"
                     /coded_by="NM_002301.5:155..1153"
                     /db_xref="CCDS:CCDS7840.1"
                     /db_xref="GeneID:3948"
                     /db_xref="HGNC:HGNC:6544"
                     /db_xref="MIM:150150"
ORIGIN      
        1 mstvkeqlie klieddensq ckitivgtga vgmacaisil lkdladelal vdvaldklkg
       61 emmdlqhgsl ffstskitsg kdysvsansr ivivtagarq qegetrlalv qrnvaimksi
      121 ipaivhyspd ckilvvsnpv diltyivwki sglpvtrvig sgcnldsarf ryligeklgv
      181 hptschgwii gehgdssvpl wsgvnvagva lktldpklgt dsdkehwkni hkqviqsaye
      241 iiklkgytsw aiglsvmdlv gsilknlrrv hpvstmvkgl ygikeelfls ipcvlgrngv
      301 sdvvkinlns eeealfkksa etlwniqkdl if
//
LOCUS       NP_001319                440 aa            linear   PRI 21-NOV-2025
DEFINITION  C-terminal-binding protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001319
VERSION     NP_001319.1
DBSOURCE    REFSEQ: accession NM_001328.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Kong,Y., Yang,G., Feng,X., Ji,Z., Wang,X., Shao,Y., Meng,J.,
            Yao,G., Ren,C. and Yang,G.
  TITLE     CTBP1 links metabolic syndrome to polycystic ovary syndrome through
            interruption of aromatase and SREBP1
  JOURNAL   Commun Biol 7 (1), 1174 (2024)
   PUBMED   39294274
  REMARK    GeneRIF: CTBP1 links metabolic syndrome to polycystic ovary
            syndrome through interruption of aromatase and SREBP1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Zhou,J., Yan,X., Liu,Y. and Yang,J.
  TITLE     Succinylation of CTBP1 mediated by KAT2A suppresses its inhibitory
            activity on the transcription of CDH1 to promote the progression of
            prostate cancer
  JOURNAL   Biochem Biophys Res Commun 650, 9-16 (2023)
   PUBMED   36764210
  REMARK    GeneRIF: Succinylation of CTBP1 mediated by KAT2A suppresses its
            inhibitory activity on the transcription of CDH1 to promote the
            progression of prostate cancer.
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Lou,L.Q., Zhou,W.Q., Song,X. and Chen,Z.
  TITLE     Elevation of hsa-miR-7-5p level mediated by CtBP1-p300-AP1 complex
            targets ATXN1 to trigger NF-kappaB-dependent inflammation response
  JOURNAL   J Mol Med (Berl) 101 (3), 223-235 (2023)
   PUBMED   36629882
  REMARK    GeneRIF: Elevation of hsa-miR-7-5p level mediated by CtBP1-p300-AP1
            complex targets ATXN1 to trigger NF-kappaB-dependent inflammation
            response.
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Tseng,C., Han,Y., Lv,Z., Song,Q., Wang,K., Shen,H. and Chen,Z.
  TITLE     The CRL4DCAF6 E3 ligase ubiquitinates CtBP1/2 to induce apoptotic
            signalling and promote intervertebral disc degeneration
  JOURNAL   J Mol Med (Berl) 101 (1-2), 171-181 (2023)
   PUBMED   36688959
  REMARK    GeneRIF: The CRL4[DCAF6] E3 ligase ubiquitinates CtBP1/2 to induce
            apoptotic signalling and promote intervertebral disc degeneration.
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Schaeper,U., Subramanian,T., Lim,L., Boyd,J.M. and Chinnadurai,G.
  TITLE     Interaction between a cellular protein that binds to the C-terminal
            region of adenovirus E1A (CtBP) and a novel cellular protein is
            disrupted by E1A through a conserved PLDLS motif
  JOURNAL   J Biol Chem 273 (15), 8549-8552 (1998)
   PUBMED   9535825
REFERENCE   7  (residues 1 to 440)
  AUTHORS   Katsanis,N. and Fisher,E.M.
  TITLE     A novel C-terminal binding protein (CTBP2) is closely related to
            CTBP1, an adenovirus E1A-binding protein, and maps to human
            chromosome 21q21.3
  JOURNAL   Genomics 47 (2), 294-299 (1998)
   PUBMED   9479502
REFERENCE   8  (residues 1 to 440)
  AUTHORS   Schaeper,U., Boyd,J.M., Verma,S., Uhlmann,E., Subramanian,T. and
            Chinnadurai,G.
  TITLE     Molecular cloning and characterization of a cellular phosphoprotein
            that interacts with a conserved C-terminal domain of adenovirus E1A
            involved in negative modulation of oncogenic transformation
  JOURNAL   Proc Natl Acad Sci U S A 92 (23), 10467-10471 (1995)
   PUBMED   7479821
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1998 Nov 24;95(24):14584]
REFERENCE   9  (residues 1 to 440)
  AUTHORS   Boyd,J.M., Subramanian,T., Schaeper,U., La Regina,M., Bayley,S. and
            Chinnadurai,G.
  TITLE     A region in the C-terminus of adenovirus 2/5 E1a protein is
            required for association with a cellular phosphoprotein and
            important for the negative modulation of T24-ras mediated
            transformation, tumorigenesis and metastasis
  JOURNAL   EMBO J 12 (2), 469-478 (1993)
   PUBMED   8440238
REFERENCE   10 (residues 1 to 440)
  AUTHORS   Battaglia,A., Carey,J.C. and South,S.T.
  TITLE     Wolf-Hirschhorn Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301362
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092535.4, BU553431.1,
            U37408.1, BC011655.2 and BM989059.1.
            
            Summary: This gene encodes a protein that binds to the C-terminus
            of adenovirus E1A proteins. This phosphoprotein is a
            transcriptional repressor and may play a role during cellular
            proliferation. This protein and the product of a second closely
            related gene, CTBP2, can dimerize. Both proteins can also interact
            with a polycomb group protein complex which participates in
            regulation of gene expression during development. Alternative
            splicing of transcripts from this gene results in multiple
            transcript variants. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098400.1, SRR1163658.170666.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245, SAMEA2146411
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..440
                     /product="C-terminal-binding protein 1 isoform 1"
                     /note="brefeldin A-ribosylated substrate"
                     /calculated_mol_wt=47404
     Region          1..70
                     /region_name="Interaction with GLIS2 1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13363.2)"
     Region          28..346
                     /region_name="CtBP_dh"
                     /note="C-terminal binding protein (CtBP),
                     D-isomer-specific 2-hydroxyacid dehydrogenases related
                     repressor; cd05299"
                     /db_xref="CDD:240624"
     Site            order(97,100..101,266,315,318)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240624"
     Site            order(100,128,180..181,183..185,203..207,236..238,240,243,
                     264..266,290..291,315,317..318)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240624"
     Region          288..360
                     /region_name="Interaction with GLIS2 2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13363.2)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13363.2)"
     Site            375..376
                     /site_type="cleavage"
                     /note="Cleavage, by CAPN1.
                     /evidence=ECO:0000269|PubMed:23707407; propagated from
                     UniProtKB/Swiss-Prot (Q13363.2)"
     Site            387..388
                     /site_type="cleavage"
                     /note="Cleavage, by CAPN1.
                     /evidence=ECO:0000269|PubMed:23707407; propagated from
                     UniProtKB/Swiss-Prot (Q13363.2)"
     Region          408..440
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13363.2)"
     Site            409..410
                     /site_type="cleavage"
                     /note="Cleavage, by CAPN1 and CAPN3.
                     /evidence=ECO:0000269|PubMed:23707407; propagated from
                     UniProtKB/Swiss-Prot (Q13363.2)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by HIPK2.
                     /evidence=ECO:0000269|PubMed:14567915; propagated from
                     UniProtKB/Swiss-Prot (Q13363.2)"
     CDS             1..440
                     /gene="CTBP1"
                     /gene_synonym="BARS; HADDTS"
                     /coded_by="NM_001328.3:176..1498"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3348.1"
                     /db_xref="GeneID:1487"
                     /db_xref="HGNC:HGNC:2494"
                     /db_xref="MIM:602618"
ORIGIN      
        1 mgsshllnkg lplgvrppim ngplhprplv alldgrdctv empilkdvat vafcdaqstq
       61 eihekvlnea vgalmyhtit ltredlekfk alriivrigs gfdnidiksa gdlgiavcnv
      121 paasveetad stlchilnly rratwlhqal regtrvqsve qirevasgaa rirgetlgii
      181 glgrvgqava lrakafgfnv lfydpylsdg veralglqrv stlqdllfhs dcvtlhcgln
      241 ehnhhlindf tvkqmrqgaf lvntargglv dekalaqalk egrirgaald vhesepfsfs
      301 qgplkdapnl ictphaawys eqasiemree aareirrait gripdslknc vnkdhltaat
      361 hwasmdpavv hpelngaayr yppgvvgvap tgipaavegi vpsamslshg lppvahppha
      421 pspgqtvkpe adrdhasdql
//
LOCUS       NP_001182472             221 aa            linear   PRI 21-NOV-2025
DEFINITION  transmembrane protein 225B [Homo sapiens].
ACCESSION   NP_001182472
VERSION     NP_001182472.1
DBSOURCE    REFSEQ: accession NM_001195543.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Polasek,O., Marusic,A., Rotim,K., Hayward,C., Vitart,V.,
            Huffman,J., Campbell,S., Jankovic,S., Boban,M., Biloglav,Z.,
            Kolcic,I., Krzelj,V., Terzic,J., Matec,L., Tometic,G., Nonkovic,D.,
            Nincevic,J., Pehlic,M., Zedelj,J., Velagic,V., Juricic,D.,
            Kirac,I., Belak Kovacevic,S., Wright,A.F., Campbell,H. and Rudan,I.
  TITLE     Genome-wide association study of anthropometric traits in Korcula
            Island, Croatia
  JOURNAL   Croat Med J 50 (1), 7-16 (2009)
   PUBMED   19260139
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB477974.1, BI559535.1, AA781117.1, AI028251.1 and HY200726.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. Variants 1-3 all encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.65351.1,
                                           SRR5189667.68640.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..221
                     /product="transmembrane protein 225B"
                     /note="transmembrane protein 225-like"
                     /calculated_mol_wt=24896
     Site            14..34
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DP42.1)"
     Site            77..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DP42.1)"
     Site            109..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DP42.1)"
     Site            147..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DP42.1)"
     CDS             1..221
                     /gene="TMEM225B"
                     /gene_synonym="GS1-259H13.2"
                     /coded_by="NM_001195543.3:191..856"
                     /db_xref="CCDS:CCDS87525.1"
                     /db_xref="GeneID:100289187"
                     /db_xref="HGNC:HGNC:53075"
ORIGIN      
        1 mltledkdmk gfswaivpal tslgyliilv vsifpfwvrl tneeshevff sglfencfna
       61 kcwkprplsi yiilgrvfll savflafvtt fimmpfasef fprtwkqnfv lacisfftga
      121 caflalvlha leikalrmkl gplqfsvlwp yyvlgfgifl fivagticli qemvcpcwhl
      181 lstsqsmeed hgslyldnle slggepssvq ketqvtaetv i
//
LOCUS       NP_001373393             422 aa            linear   PRI 21-NOV-2025
DEFINITION  plasminogen activator inhibitor 1 isoform 10 precursor [Homo
            sapiens].
ACCESSION   NP_001373393
VERSION     NP_001373393.1
DBSOURCE    REFSEQ: accession NM_001386464.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Doelker,T., Gallwas,J. and Grundker,C.
  TITLE     Suppressing Expression of SERPINE1/PAI1 Through Activation of GPER1
            Reduces Progression of Vulvar Carcinoma
  JOURNAL   Cancer Genomics Proteomics 21 (6), 566-579 (2024)
   PUBMED   39467628
  REMARK    GeneRIF: Suppressing Expression of SERPINE1/PAI1 Through Activation
            of GPER1 Reduces Progression of Vulvar Carcinoma.
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Khoukaz,H.B., Vadali,M., Schoenherr,A., Ramirez-Perez,F.I.,
            Morales-Quinones,M., Sun,Z., Fujie,S., Foote,C.A., Lyu,Z., Zeng,S.,
            Augenreich,M.A., Cai,D., Chen,S.Y., Joshi,T., Ji,Y., Hill,M.A.,
            Martinez-Lemus,L.A. and Fay,W.P.
  TITLE     PAI-1 Regulates the Cytoskeleton and Intrinsic Stiffness of
            Vascular Smooth Muscle Cells
  JOURNAL   Arterioscler Thromb Vasc Biol 44 (10), 2191-2203 (2024)
   PUBMED   38868940
  REMARK    GeneRIF: PAI-1 Regulates the Cytoskeleton and Intrinsic Stiffness
            of Vascular Smooth Muscle Cells.
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Guo,X., Zhou,H., Liu,Y., Xu,W., Kanwore,K. and Zhang,L.
  TITLE     Glial-Cell-Line-Derived Neurotrophic Factor Promotes Glioblastoma
            Cell Migration and Invasion via the SMAD2/3-SERPINE1-Signaling Axis
  JOURNAL   Int J Mol Sci 25 (18), 10229 (2024)
   PUBMED   39337713
  REMARK    GeneRIF: Glial-Cell-Line-Derived Neurotrophic Factor Promotes
            Glioblastoma Cell Migration and Invasion via the
            SMAD2/3-SERPINE1-Signaling Axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Yatsenko,T., Rios,R., Nogueira,T., Salama,Y., Takahashi,S.,
            Adachi,E., Tabe,Y., Hattori,N., Osada,T., Naito,T., Takahashi,K.,
            Hattori,K. and Heissig,B.
  TITLE     The influence of 4G/5G polymorphism in the
            plasminogen-activator-inhibitor-1 promoter on COVID-19 severity and
            endothelial dysfunction
  JOURNAL   Front Immunol 15, 1445294 (2024)
   PUBMED   39281671
  REMARK    GeneRIF: The influence of 4G/5G polymorphism in the
            plasminogen-activator-inhibitor-1 promoter on COVID-19 severity and
            endothelial dysfunction.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Heiman,M., Gupta,S., Lewandowska,M. and Shapiro,A.D.
  TITLE     Complete Plasminogen Activator Inhibitor 1 Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   28771291
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Fay,W.P., Shapiro,A.D., Shih,J.L., Schleef,R.R. and Ginsburg,D.
  TITLE     Brief report: complete deficiency of plasminogen-activator
            inhibitor type 1 due to a frame-shift mutation
  JOURNAL   N Engl J Med 327 (24), 1729-1733 (1992)
   PUBMED   1435917
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Koh,S.C., Wong,P.C., Yuen,R., Chua,S.E., Ng,B.L. and Ratnam,S.S.
  TITLE     Concentration of plasminogen activators and inhibitor in the human
            endometrium at different phases of the menstrual cycle
  JOURNAL   J Reprod Fertil 96 (2), 407-413 (1992)
   PUBMED   1339823
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Hagege,J., Peraldi,M.N., Rondeau,E., Adida,C., Delarue,F.,
            Medcalf,R., Schleuning,W.D. and Sraer,J.D.
  TITLE     Plasminogen activator inhibitor-1 deposition in the extracellular
            matrix of cultured human mesangial cells
  JOURNAL   Am J Pathol 141 (1), 117-128 (1992)
   PUBMED   1632457
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Ehrlich,H.J., Gebbink,R.K., Keijer,J., Linders,M., Preissner,K.T.
            and Pannekoek,H.
  TITLE     Alteration of serpin specificity by a protein cofactor. Vitronectin
            endows plasminogen activator inhibitor 1 with thrombin inhibitory
            properties
  JOURNAL   J Biol Chem 265 (22), 13029-13035 (1990)
   PUBMED   1695900
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004876.2.
            
            Summary: This gene encodes a member of the serine proteinase
            inhibitor (serpin) superfamily. This member is the principal
            inhibitor of tissue plasminogen activator (tPA) and urokinase
            (uPA), and hence is an inhibitor of fibrinolysis. The protein also
            functions as a component of innate antiviral immunity. Defects in
            this gene are the cause of plasminogen activator inhibitor-1
            deficiency (PAI-1 deficiency), and high concentrations of the gene
            product are associated with thrombophilia. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2280488.1,
                                           SRR14038195.463905.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..422
                     /product="plasminogen activator inhibitor 1 isoform 10
                     precursor"
                     /note="serine (or cysteine) proteinase inhibitor, clade E
                     (nexin, plasminogen activator inhibitor type 1), member 1;
                     endothelial plasminogen activator inhibitor; serpin E1;
                     serpin peptidase inhibitor, clade E (nexin, plasminogen
                     activator inhibitor type 1), member 1"
                     /calculated_mol_wt=44853
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2309
     Region          29..390
                     /region_name="serpinE1_PAI-1"
                     /note="serpin family E member 1, plasminogen activator
                     inhibitor-1; cd02051"
                     /db_xref="CDD:381007"
     Site            order(124,133..134,137,143,145..148,154,158,161..162)
                     /site_type="other"
                     /note="vitronectin binding site [polypeptide binding]"
                     /db_xref="CDD:381007"
     Site            order(172..173,346,348)
                     /site_type="other"
                     /note="putative Cl binding site [ion binding]"
                     /db_xref="CDD:381007"
     Site            order(228,230,233,235,245,264,292..295,361..362,364..373)
                     /site_type="other"
                     /note="plasminogen activator binding site [polypeptide
                     binding]"
                     /db_xref="CDD:381007"
     Site            232
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05121.1)"
     Site            288
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05121.1)"
     Site            352
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P05121.1)"
     Site            355..380
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381007"
     Site            369..370
                     /site_type="other"
                     /note="Reactive bond; propagated from UniProtKB/Swiss-Prot
                     (P05121.1)"
     CDS             1..422
                     /gene="SERPINE1"
                     /gene_synonym="PAI; PAI-1; PAI1; PLANH1"
                     /coded_by="NM_001386464.1:143..1411"
                     /note="isoform 10 precursor is encoded by transcript
                     variant 10"
                     /db_xref="GeneID:5054"
                     /db_xref="HGNC:HGNC:8583"
                     /db_xref="MIM:173360"
ORIGIN      
        1 mqmspaltcl vlglalvfge gsavhhppsy vahlasdfgv rvfqqvaqas kdrnvvfspy
       61 gvasvlamlq lttggetqqq iqaamgfkid dkgmapalrh lykelmgpwn kdeisttdai
      121 fvqrdlklvq gfmphffrlf rstvkqvdfs everarfiin dwvkthtkgm isnllgkgav
      181 dqltrlvlvn alyfngqwkt pfpdssthrr lfhksdgstv svpmmaqtnk fnytefttpd
      241 ghyydilelp yhgdtlsmfi aapyekevpl saltnilsaq lishwkgnmt rlprllvlpk
      301 fsletevdlr kplenlgmtd mfrqfqadft slsdqeplhv aqalqkvkie vnesgtvass
      361 stavivsarm apeeiimdrp flfvvrhnpt dsagsplcds gscdsrqlth lprsqsfhph
      421 pa
//
LOCUS       NP_112225                358 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase RNF146 isoform a [Homo sapiens].
ACCESSION   NP_112225
VERSION     NP_112225.2
DBSOURCE    REFSEQ: accession NM_030963.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Li,W., Han,Q., Zhu,Y., Zhou,Y., Zhang,J., Wu,W., Li,Y., Liu,L.,
            Qiu,Y., Hu,K. and Yin,D.
  TITLE     SUMOylation of RNF146 results in Axin degradation and activation of
            Wnt/beta-catenin signaling to promote the progression of
            hepatocellular carcinoma
  JOURNAL   Oncogene 42 (21), 1728-1740 (2023)
   PUBMED   37029301
  REMARK    GeneRIF: SUMOylation of RNF146 results in Axin degradation and
            activation of Wnt/beta-catenin signaling to promote the progression
            of hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Xu,Y.R., Shi,M.L., Zhang,Y., Kong,N., Wang,C., Xiao,Y.F., Du,S.S.,
            Zhu,Q.Y. and Lei,C.Q.
  TITLE     Tankyrases inhibit innate antiviral response by PARylating
            VISA/MAVS and priming it for RNF146-mediated ubiquitination and
            degradation
  JOURNAL   Proc Natl Acad Sci U S A 119 (26), e2122805119 (2022)
   PUBMED   35733260
  REMARK    GeneRIF: Tankyrases inhibit innate antiviral response by PARylating
            VISA/MAVS and priming it for RNF146-mediated ubiquitination and
            degradation.
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Zhang,Y., Liu,S., Mickanin,C., Feng,Y., Charlat,O., Michaud,G.A.,
            Schirle,M., Shi,X., Hild,M., Bauer,A., Myer,V.E., Finan,P.M.,
            Porter,J.A., Huang,S.M. and Cong,F.
  TITLE     RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin
            degradation and Wnt signalling
  JOURNAL   Nat Cell Biol 13 (5), 623-629 (2011)
   PUBMED   21478859
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Menachem,T.D., Laitman,Y., Kaufman,B. and Friedman,E.
  TITLE     The RNF146 and ECHDC1 genes as candidates for inherited breast and
            ovarian cancer in Jewish Ashkenazi women
  JOURNAL   Fam Cancer 8 (4), 399-402 (2009)
   PUBMED   19517271
  REMARK    GeneRIF: Mutations in the coding regions of the RNF146 and ECHDC1
            genes do not contribute to the burden of inherited predisposition
            of breast cancer in Ashkenazi high risk women.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 358)
  AUTHORS   Gold,B., Kirchhoff,T., Stefanov,S., Lautenberger,J., Viale,A.,
            Garber,J., Friedman,E., Narod,S., Olshen,A.B., Gregersen,P.,
            Kosarin,K., Olsh,A., Bergeron,J., Ellis,N.A., Klein,R.J.,
            Clark,A.G., Norton,L., Dean,M., Boyd,J. and Offit,K.
  TITLE     Genome-wide association study provides evidence for a breast cancer
            risk locus at 6q22.33
  JOURNAL   Proc Natl Acad Sci U S A 105 (11), 4340-4345 (2008)
   PUBMED   18326623
  REMARK    GeneRIF: Genome-wide association study of gene-disease association.
            (HuGE Navigator)
REFERENCE   9  (residues 1 to 358)
  AUTHORS   von Rotz,R.C., Kins,S., Hipfel,R., von der Kammer,H. and
            Nitsch,R.M.
  TITLE     The novel cytosolic RING finger protein dactylidin is up-regulated
            in brains of patients with Alzheimer's disease
  JOURNAL   Eur J Neurosci 21 (5), 1289-1298 (2005)
   PUBMED   15813938
  REMARK    GeneRIF: Dactylidin may function early in the progression of
            Alzheimer's disease.
REFERENCE   10 (residues 1 to 358)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB267873.1, AL136829.1 and AJ420549.1.
            
            On Aug 14, 2003 this sequence version replaced NP_112225.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1-7 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL136829.1, SRR1803612.178155.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.33"
     Protein         1..358
                     /product="E3 ubiquitin-protein ligase RNF146 isoform a"
                     /EC_number="2.3.2.27"
                     /note="dactylidin; RING-type E3 ubiquitin transferase
                     RNF146; E3 ubiquitin-protein ligase RNF146; iduna"
                     /calculated_mol_wt=38688
     Region          34..83
                     /region_name="RING-HC_RNF146"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 146 (RNF146) and similar proteins; cd16546"
                     /db_xref="CDD:438208"
     Site            order(37..38,40,69,71..72)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438208"
     Region          103..175
                     /region_name="WWE"
                     /note="Domain in Deltex and TRIP12 homologues. Possibly
                     involved in regulation of ubiquitin-mediated proteolysis;
                     smart00678"
                     /db_xref="CDD:128922"
     CDS             1..358
                     /gene="RNF146"
                     /coded_by="NM_030963.4:411..1487"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS5136.1"
                     /db_xref="GeneID:81847"
                     /db_xref="HGNC:HGNC:21336"
                     /db_xref="MIM:612137"
ORIGIN      
        1 magcgeidhs inmlptnrka nescsntaps ltvpecaicl qtcvhpvslp ckhvfcylcv
       61 kgaswlgkrc alcrqeiped fldkptllsp eelkaasrgn geyawyyegr ngwwqydert
      121 sreledafsk gkkntemlia gflyvadlen mvqyrrnehg rrrkikrdii dipkkgvagl
      181 rldcdantvn laressadga dsvsaqsgas vqplvssvrp ltsvdgqlts patpspdast
      241 sledsfahlq lsgdntaers hrgegeedhe spssgrvpap dtsieetesd assdsedvsa
      301 vvaqhsltqq rllvsnanqt vpdrsdrsgt drsvagggtv svsvrsrrpd gqctvtev
//
LOCUS       NP_001371710            1121 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 36 [Homo sapiens].
ACCESSION   NP_001371710
VERSION     NP_001371710.1
DBSOURCE    REFSEQ: accession NM_001384781.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1121)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1121)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1121)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1121)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1121)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1121)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1121)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1121)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1121)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1121)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3569580.1,
                                           SRR14038195.2603460.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1121
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1121
                     /product="microtubule-associated protein 4 isoform 36"
                     /note="MAP-4"
                     /calculated_mol_wt=117597
     Region          <575..919
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <931..952
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          992..1021
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          1023..1053
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1121
                     /gene="MAP4"
                     /coded_by="NM_001384781.1:96..3461"
                     /note="isoform 36 is encoded by transcript variant 42"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgsp tefleekmay qeypnsqnwp
      121 edtnfcfqpe qvvdpiqtdp fkmyhdddla dlvfpssata dtsifagqnd plkdsygmsp
      181 cntavvpqgw svealnsphs esfvspeava eppqptavpl elakeiemas eerppaqale
      241 immglkttdm apsketemal akdmalatkt evalakdmes ptkldvtlak dmqpsmesdm
      301 alvkdmelpt ekevalvkdv rwptetdvss aknvvlptet evapakdvtl lketeraspi
      361 kmdlapskdm gppkenkket eraspikmdl apskdmgppk enkivpakdl vllseievaq
      421 andiisstei ssaekvalss etevalardm tlppetnvil tkdkalplea evapvkdmaq
      481 lpeteiapak dvapstvkev gllkdmspls etemalgkdv tpppetevvl iknvclppem
      541 evaltedqvp alkteaplak dgvltlannv tpakdvppls eteatpvpik dmeiaqtqkg
      601 isedshlesl qdvgqsaapt fmispetvtg tgkkcslpae edsvleklge rkpcnsqpse
      661 lssetsgiar peegrpvvsg tgndittppn kelppspekk tkplattqpa ktstskaktq
      721 ptslpkqpap ttigglnkkp mslasglvpa appkrpavas arpsilpskd vkpkpiadak
      781 apekraspsk pasapasrsg skstqtvakt ttaaavastg pssrspstll pkkptaikte
      841 gkpaevkkmt aksvpadlsr pkststssmk ktttlsgtap aagvvpsrvk atpmpsrpst
      901 tpfidkkpts akpssttprl srlatntsap dlknvrskvg stenikhqpg ggrakvekkt
      961 eaaattrkpe snavtktagp iasaqkqpag kvqiqnkkvd iskvsskcgs kanikhkpgg
     1021 gdvkiesqkl nfkekaqakv gsldnvghlp aggavktegg gseaplcpgp pageepaise
     1081 aapeagapts asglnghptl sgggdqreaq tldsqiqets i
//
LOCUS       NP_001161096            2173 aa            linear   PRI 21-NOV-2025
DEFINITION  voltage-dependent L-type calcium channel subunit alpha-1C isoform
            22 [Homo sapiens].
ACCESSION   NP_001161096
VERSION     NP_001161096.2
DBSOURCE    REFSEQ: accession NM_001167624.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2173)
  AUTHORS   Zhang,X., Liang,X., Cheng,X., Chen,J., Deng,W., Zhang,Y., Cui,L.,
            Cheng,X., Li,X., Yang,C., Ye,B. and Cao,L.
  TITLE     [CACNA1C rs58619945 genotype influences the cortical thickness of
            attention network among patients with Bipolar disorder]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 41 (9), 1045-1052 (2024)
   PUBMED   39217481
  REMARK    GeneRIF: [CACNA1C rs58619945 genotype influences the cortical
            thickness of attention network among patients with Bipolar
            disorder].
REFERENCE   2  (residues 1 to 2173)
  AUTHORS   Yang,Y., Zhu,Z., Hui,L. and Sun,P.
  TITLE     Effects of CACNA1C and ANK3 on cognitive function in patients with
            bipolar disorder
  JOURNAL   Prog Neuropsychopharmacol Biol Psychiatry 133, 111016 (2024)
   PUBMED   38657895
  REMARK    GeneRIF: Effects of CACNA1C and ANK3 on cognitive function in
            patients with bipolar disorder.
REFERENCE   3  (residues 1 to 2173)
  AUTHORS   Almodovar-Paya,C., Guardiola-Ripoll,M., Giralt-Lopez,M.,
            Oscoz-Irurozqui,M., Canales-Rodriguez,E.J., Madre,M.,
            Soler-Vidal,J., Ramiro,N., Callado,L.F., Arias,B., Gallego,C.,
            Pomarol-Clotet,E. and Fatjo-Vilas,M.
  TITLE     NRN1 epistasis with BDNF and CACNA1C: mediation effects on symptom
            severity through neuroanatomical changes in schizophrenia
  JOURNAL   Brain Struct Funct 229 (5), 1299-1315 (2024)
   PUBMED   38720004
  REMARK    GeneRIF: NRN1 epistasis with BDNF and CACNA1C: mediation effects on
            symptom severity through neuroanatomical changes in schizophrenia.
REFERENCE   4  (residues 1 to 2173)
  AUTHORS   Gao,S., Yao,X., Chen,J., Huang,G., Fan,X., Xue,L., Li,Z., Wu,T.,
            Zheng,Y., Huang,J., Jin,X., Wang,Y., Wang,Z., Yu,Y., Liu,L.,
            Pan,X., Song,C. and Yan,N.
  TITLE     Structural basis for human Cav1.2 inhibition by multiple drugs and
            the neurotoxin calciseptine
  JOURNAL   Cell 186 (24), 5363-5374 (2023)
   PUBMED   37972591
  REMARK    GeneRIF: Structural basis for human Cav1.2 inhibition by multiple
            drugs and the neurotoxin calciseptine.
REFERENCE   5  (residues 1 to 2173)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   6  (residues 1 to 2173)
  AUTHORS   Napolitano,C. and Priori,S.G.
  TITLE     CACNA1C-Related Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301577
REFERENCE   7  (residues 1 to 2173)
  AUTHORS   Groffen,A.J., Bikker,H. and Christiaans,I.
  TITLE     Long QT Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301308
REFERENCE   8  (residues 1 to 2173)
  AUTHORS   Sun,W., McPherson,J.D., Hoang,D.Q., Wasmuth,J.J., Evans,G.A. and
            Montal,M.
  TITLE     Mapping of a human brain voltage-gated calcium channel to human
            chromosome 12p13-pter
  JOURNAL   Genomics 14 (4), 1092-1094 (1992)
   PUBMED   1335957
REFERENCE   9  (residues 1 to 2173)
  AUTHORS   Powers,P.A., Gregg,R.G. and Hogan,K.
  TITLE     Linkage mapping of the human gene for the alpha 1 subunit of the
            cardiac DHP-sensitive Ca2+ channel (CACNL1A1) to chromosome
            12p13.2-pter using a dinucleotide repeat
  JOURNAL   Genomics 14 (1), 206-207 (1992)
   PUBMED   1330882
REFERENCE   10 (residues 1 to 2173)
  AUTHORS   Soldatov,N.M.
  TITLE     Molecular diversity of L-type Ca2+ channel transcripts in human
            fibroblasts
  JOURNAL   Proc Natl Acad Sci U S A 89 (10), 4628-4632 (1992)
   PUBMED   1316612
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005342.1, AK309111.1,
            AF465484.1, L29534.1, Z34816.1, KF455578.2 and AC007618.21.
            
            On Mar 28, 2014 this sequence version replaced NP_001161096.1.
            
            Summary: This gene encodes an alpha-1 subunit of a
            voltage-dependent calcium channel. Calcium channels mediate the
            influx of calcium ions into the cell upon membrane polarization.
            The alpha-1 subunit consists of 24 transmembrane segments and forms
            the pore through which ions pass into the cell. The calcium channel
            consists of a complex of alpha-1, alpha-2/delta, beta, and gamma
            subunits in a 1:1:1:1 ratio. There are multiple isoforms of each of
            these proteins, either encoded by different genes or the result of
            alternative splicing of transcripts. The protein encoded by this
            gene binds to and is inhibited by dihydropyridine. Alternative
            splicing results in many transcript variants encoding different
            proteins. Some of the predicted proteins may not produce functional
            ion channel subunits. [provided by RefSeq, Oct 2012].
            
            Transcript Variant: This variant (22) lacks two alternate in-frame
            exons and contains another alternate in-frame exon compared to
            variant 1, resulting in a shorter protein (isoform 22), compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2155550 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2173
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..2173
                     /product="voltage-dependent L-type calcium channel subunit
                     alpha-1C isoform 22"
                     /note="calcium channel, cardic dihydropyridine-sensitive,
                     alpha-1 subunit; DHPR, alpha-1 subunit; voltage-dependent
                     L-type Ca2+ channel alpha 1 subunit; calcium channel,
                     voltage-dependent, L type, alpha 1C subunit; CACNA1C
                     intronic transcript 2; CACNA1C intronic transcript 2
                     (non-protein coding)"
                     /calculated_mol_wt=243532
     Region          123..416
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          523..764
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          899..1176
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          1218..1487
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          1496..1549
                     /region_name="GPHH"
                     /note="Voltage-dependent L-type calcium channel,
                     IQ-associated; pfam16905"
                     /db_xref="CDD:465306"
     Region          1559..1633
                     /region_name="Ca_chan_IQ"
                     /note="Voltage gated calcium channel IQ domain; pfam08763"
                     /db_xref="CDD:462591"
     Region          1653..2123
                     /region_name="CAC1F_C"
                     /note="Voltage-gated calcium channel subunit alpha,
                     C-term; pfam16885"
                     /db_xref="CDD:465298"
     CDS             1..2173
                     /gene="CACNA1C"
                     /gene_synonym="CACH2; CACN2; CACNA1C-IT2; CACNL1A1;
                     CaV1.2; CCHL1A1; LQT8; NEDHLSS; TS; TS. LQT8"
                     /coded_by="NM_001167624.3:577..7098"
                     /note="isoform 22 is encoded by transcript variant 22"
                     /db_xref="CCDS:CCDS53733.1"
                     /db_xref="GeneID:775"
                     /db_xref="HGNC:HGNC:1390"
                     /db_xref="MIM:114205"
ORIGIN      
        1 mvnentrmyi peenhqgsny gsprpahanm nanaaaglap ehiptpgaal swqaaidaar
       61 qaklmgsagn atistvsstq rkrqqygkpk kqgsttatrp prallcltlk npirracisi
      121 vewkpfeiii lltifancva laiyipfped dsnatnsnle rveylfliif tveaflkvia
      181 ygllfhpnay lrngwnlldf iivvvglfsa ileqatkadg analggkgag fdvkalrafr
      241 vlrplrlvsg vpslqvvlns iikamvpllh iallvlfvii iyaiiglelf mgkmhktcyn
      301 qegiadvpae ddpspcalet ghgrqcqngt vckpgwdgpk hgitnfdnfa famltvfqci
      361 tmegwtdvly wmqdamgyel pwvyfvslvi fgsffvlnlv lgvlsgefsk erekakargd
      421 fqklrekqql eedlkgyldw itqaedidpe nedegmdeek prnmsmptse tesvntenva
      481 ggdiegencg arlahrisks kfsrywrrwn rfcrrkcraa vksnvfywlv iflvflntlt
      541 iasehynqpn wltevqdtan kallalftae mllkmyslgl qayfvslfnr fdcfvvcggi
      601 letilvetki msplgisvlr cvrllrifki trywnslsnl vasllnsvrs iaslllllfl
      661 fiiifsllgm qlfggkfnfd emqtrrstfd nfpqslltvf qiltgedwns vmydgimayg
      721 gpsfpgmlvc iyfiilficg nyillnvfla iavdnladae sltsaqkeee eekerkklar
      781 taspekkqel vekpavgesk eekielksit adgesppatk inmddlqpne nedkspypnp
      841 ettgeedeee pempvgprpr plselhlkek avpmpeasaf fifssnnrfr lqchrivndt
      901 iftnlilffi llssislaae dpvqhtsfrn hilfyfdivf ttiftieial kmtaygaflh
      961 kgsfcrnyfn ildllvvsvs lisfgiqssa invvkilrvl rvlrplrain rakglkhvvq
     1021 cvfvairtig nivivttllq fmfacigvql fkgklytcsd sskqteaeck gnyitykdge
     1081 vdhpiiqprs wenskfdfdn vlaammalft vstfegwpel lyrsidshte dkgpiynyrv
     1141 eisiffiiyi iiiaffmmni fvgfvivtfq eqgeqeyknc eldknqrqcv eyalkarplr
     1201 ryipknqhqy kvwyvvnsty feylmfvlil lnticlamqh ygqsclfkia mnilnmlftg
     1261 lftvemilkl iafkpkgyfs dpwnvfdfli vigsiidvil setnpaehtq cspsmnaeen
     1321 srisitffrl frvmrlvkll srgegirtll wtfiksfqal pyvallivml ffiyavigmq
     1381 vfgkialndt teinrnnnfq tfpqavlllf rcatgeawqd imlacmpgkk capesepsns
     1441 tegetpcgss favfyfisfy mlcafliinl fvavimdnfd yltrdwsilg phhldefkri
     1501 waeydpeakg rikhldvvtl lrriqpplgf gklcphrvac krlvsmnmpl nsdgtvmfna
     1561 tlfalvrtal riktegnleq aneelraiik kiwkrtsmkl ldqvvppagd devtvgkfya
     1621 tfliqeyfrk fkkrkeqglv gkpsqrnals lqaglrtlhd igpeirrais gdltaeeeld
     1681 kamkeavsaa seddifrrag glfgnhvsyy qsdgrsafpq tfttqrplhi nkagssqgdt
     1741 espsheklvd stftpssyss tgsnaninna nntalgrlpr pagypstvst veghgpplsp
     1801 airvqevawk lssnrerhvp mcedlelrrd sgsagtqahc lllrranpsr chsresqaam
     1861 agqeetsqde tyevkmnhdt eacsepslls temlsyqdde nrqltlpeed krdirqspkr
     1921 gflrsaslgr rasfhleclk rqkdrggdis qktvlplhlv hhqalavagl spllqrshsp
     1981 asfprpfatp patpgsrgwp pqpvptlrle gvesseklns sfpsihcgsw aettpggggs
     2041 saarrvrpvs lmvpsqagap grqfhgsass lveavliseg lgqfaqdpkf ievttqelad
     2101 acdmtieeme saadnilsgg apqspngall pfvncrdagq draggeedag cvrargrpse
     2161 eelqdsrvyv ssl
//
LOCUS       NP_001381090             646 aa            linear   PRI 21-NOV-2025
DEFINITION  regulator of G-protein signaling 12 isoform 7 [Homo sapiens].
ACCESSION   NP_001381090 XP_006713970
VERSION     NP_001381090.1
DBSOURCE    REFSEQ: accession NM_001394161.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Sneddon,W.B., Ramineni,S., Van Doorn,G.E., Hepler,J.R. and
            Friedman,P.A.
  TITLE     Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport
  JOURNAL   Biochem Biophys Res Commun 733, 150700 (2024)
   PUBMED   39293332
  REMARK    GeneRIF: Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport.
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Yuan,G., Yang,S. and Yang,S.
  TITLE     RGS12 represses oral squamous cell carcinoma by driving M1
            polarization of tumor-associated macrophages via controlling
            ciliary MYCBP2/KIF2A signaling
  JOURNAL   Int J Oral Sci 15 (1), 11 (2023)
   PUBMED   36797232
  REMARK    GeneRIF: RGS12 represses oral squamous cell carcinoma by driving M1
            polarization of tumor-associated macrophages via controlling
            ciliary MYCBP2/KIF2A signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Yuan,G., Fu,C., Yang,S.T., Yuh,D.Y., Hajishengallis,G. and Yang,S.
  TITLE     RGS12 Drives Macrophage Activation and Osteoclastogenesis in
            Periodontitis
  JOURNAL   J Dent Res 101 (4), 448-457 (2022)
   PUBMED   34796776
  REMARK    GeneRIF: RGS12 Drives Macrophage Activation and Osteoclastogenesis
            in Periodontitis.
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Yuan,G., Huang,Y., Yang,S.T., Ng,A. and Yang,S.
  TITLE     RGS12 inhibits the progression and metastasis of multiple myeloma
            by driving M1 macrophage polarization and activation in the bone
            marrow microenvironment
  JOURNAL   Cancer Commun (Lond) 42 (1), 60-64 (2022)
   PUBMED   34931491
  REMARK    GeneRIF: RGS12 inhibits the progression and metastasis of multiple
            myeloma by driving M1 macrophage polarization and activation in the
            bone marrow microenvironment.
REFERENCE   6  (residues 1 to 646)
  AUTHORS   Schiff,M.L., Siderovski,D.P., Jordan,J.D., Brothers,G., Snow,B., De
            Vries,L., Ortiz,D.F. and Diverse-Pierluissi,M.
  TITLE     Tyrosine-kinase-dependent recruitment of RGS12 to the N-type
            calcium channel
  JOURNAL   Nature 408 (6813), 723-727 (2000)
   PUBMED   11130074
REFERENCE   7  (residues 1 to 646)
  AUTHORS   Chatterjee,T.K. and Fisher,R.A.
  TITLE     Novel alternative splicing and nuclear localization of human RGS12
            gene products
  JOURNAL   J Biol Chem 275 (38), 29660-29671 (2000)
   PUBMED   10869340
REFERENCE   8  (residues 1 to 646)
  AUTHORS   Frohme,M., Scharm,B., Delius,H., Knecht,R. and Hoheisel,J.D.
  TITLE     Use of representational difference analysis and cDNA arrays for
            transcriptional profiling of tumor tissue
  JOURNAL   Ann N Y Acad Sci 910, 85-104 (2000)
   PUBMED   10911908
  REMARK    Review article
REFERENCE   9  (residues 1 to 646)
  AUTHORS   Snow,B.E., Hall,R.A., Krumins,A.M., Brothers,G.M., Bouchard,D.,
            Brothers,C.A., Chung,S., Mangion,J., Gilman,A.G., Lefkowitz,R.J.
            and Siderovski,D.P.
  TITLE     GTPase activating specificity of RGS12 and binding specificity of
            an alternatively spliced PDZ (PSD-95/Dlg/ZO-1) domain
  JOURNAL   J Biol Chem 273 (28), 17749-17755 (1998)
   PUBMED   9651375
REFERENCE   10 (residues 1 to 646)
  AUTHORS   Snow,B.E., Antonio,L., Suggs,S., Gutstein,H.B. and Siderovski,D.P.
  TITLE     Molecular cloning and expression analysis of rat Rgs12 and Rgs14
  JOURNAL   Biochem Biophys Res Commun 233 (3), 770-777 (1997)
   PUBMED   9168931
  REMARK    GeneRIF: shows chromosomal mapping information for human locus.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645949.16 and AL590235.23.
            
            On Apr 5, 2021 this sequence version replaced XP_006713970.1.
            
            Summary: This gene encodes a member of the 'regulator of G protein
            signaling' (RGS) gene family. The encoded protein may function as a
            guanosine triphosphatase (GTPase)-activating protein as well as a
            transcriptional repressor. This protein may play a role in
            tumorigenesis. Multiple transcript variants encoding distinct
            isoforms have been identified for this gene. Other alternative
            splice variants have been described but their biological nature has
            not been determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR7346977.1091290.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2145743, SAMEA2146982 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..646
                     /product="regulator of G-protein signaling 12 isoform 7"
                     /note="regulator of G-protein signalling 12"
                     /calculated_mol_wt=68527
     Region          <1..29
                     /region_name="RGS"
                     /note="Regulator of G protein signaling (RGS) domain
                     superfamily; cl02565"
                     /db_xref="CDD:470619"
     Region          35..150
                     /region_name="RGS12_us1"
                     /note="Unstructured region of RGS12; pfam16613"
                     /db_xref="CDD:465199"
     Region          161..230
                     /region_name="RBD1_RGS12"
                     /note="Ras-binding domain (RBD) 1 of regulator of G
                     protein signaling 12 (RGS12); cd17136"
                     /db_xref="CDD:340656"
     Site            order(166,187,189,210)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340656"
     Region          231..303
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     Region          305..379
                     /region_name="RGS12_us2"
                     /note="Unstructured region between RBD and GoLoco;
                     pfam16611"
                     /db_xref="CDD:435461"
     Region          387..408
                     /region_name="GoLoco"
                     /note="LGN motif, putative GEFs specific for G-alpha
                     GTPases; smart00390"
                     /db_xref="CDD:214645"
     Region          438..575
                     /region_name="RGS12_usC"
                     /note="C-terminal unstructured region of RGS12; pfam16612"
                     /db_xref="CDD:465198"
     CDS             1..646
                     /gene="RGS12"
                     /coded_by="NM_001394161.1:675..2615"
                     /note="isoform 7 is encoded by transcript variant 10"
                     /db_xref="GeneID:6002"
                     /db_xref="HGNC:HGNC:9994"
                     /db_xref="MIM:602512"
ORIGIN      
        1 mfkeqqlqif nlmkfdsytr flksplyqec ilaevegral pdsqqvpssp askhslgsdh
       61 ssvstpkkls gksksgrsln eelgdedsek krkgaffsws rtrstgrsqk krehgdhadd
      121 alhangglcr resqgsvssa gsldlseacr tlapekdkat khccihlpdg tscvvavkag
      181 fsikdilsgl cerhgingaa adlflvggdk plvlhqdssi lesrdlrlek rtlfrldlvp
      241 inrsvglkak ptkpvtevlr pvvarygldl sgllvrlsge kepldlgapi ssldgqrvvl
      301 eekdpsrgka sadkqkgvpv kqntavnsss rnhsatgeer tlgksnsiki kgengknard
      361 prlskreesi akigkkkyqk inldeaeeff eliskaqsnr addqrgllrk edlvlpeflr
      421 lppgsteltl ptpaavakgf skrsatgngr esasqpgeqw epvqessdsp stspgsassp
      481 pgppgttppg qkspsgpfct pqspvslaqe gtaqiwkrqs qeveaggiqt vedehvaelt
      541 lmgegdissp nstllpppst pqevpgpsrp gsgthgsrdl pvnriidvdl vtgsapgrdg
      601 giagaqagpg rsqasggppt sdlpglgpvp gepakpktsa hhatfv
//
LOCUS       NP_001317015            1504 aa            linear   PRI 21-NOV-2025
DEFINITION  neurexin-1 isoform alpha9 precursor [Homo sapiens].
ACCESSION   NP_001317015 XP_016860802
VERSION     NP_001317015.1
DBSOURCE    REFSEQ: accession NM_001330086.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1504)
  AUTHORS   Sebastian,R., Jin,K., Pavon,N., Bansal,R., Potter,A., Song,Y.,
            Babu,J., Gabriel,R., Sun,Y., Aronow,B. and Pak,C.
  TITLE     Schizophrenia-associated NRXN1 deletions induce
            developmental-timing- and cell-type-specific vulnerabilities in
            human brain organoids
  JOURNAL   Nat Commun 14 (1), 3770 (2023)
   PUBMED   37355690
  REMARK    GeneRIF: Schizophrenia-associated NRXN1 deletions induce
            developmental-timing- and cell-type-specific vulnerabilities in
            human brain organoids.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1504)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1504)
  AUTHORS   Rhoades,R., Henry,B., Prichett,D., Fang,Y. and Teng,S.
  TITLE     Computational Saturation Mutagenesis to Investigate the Effects of
            Neurexin-1 Mutations on AlphaFold Structure
  JOURNAL   Genes (Basel) 13 (5), 789 (2022)
   PUBMED   35627176
  REMARK    GeneRIF: Computational Saturation Mutagenesis to Investigate the
            Effects of Neurexin-1 Mutations on AlphaFold Structure.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1504)
  AUTHORS   Aksu Uzunhan,T. and Ayaz,A.
  TITLE     Homozygous exonic and intragenic NRXN1 deletion presenting as
            either West syndrome or autism spectrum disorder in two siblings
  JOURNAL   Clin Neurol Neurosurg 214, 107141 (2022)
   PUBMED   35101781
  REMARK    GeneRIF: Homozygous exonic and intragenic NRXN1 deletion presenting
            as either West syndrome or autism spectrum disorder in two
            siblings.
REFERENCE   5  (residues 1 to 1504)
  AUTHORS   Yan,Q., Weyn-Vanhentenryck,S.M., Wu,J., Sloan,S.A., Zhang,Y.,
            Chen,K., Wu,J.Q., Barres,B.A. and Zhang,C.
  TITLE     Systematic discovery of regulated and conserved alternative exons
            in the mammalian brain reveals NMD modulating chromatin regulators
  JOURNAL   Proc Natl Acad Sci U S A 112 (11), 3445-3450 (2015)
   PUBMED   25737549
REFERENCE   6  (residues 1 to 1504)
  AUTHORS   Tabuchi,K. and Sudhof,T.C.
  TITLE     Structure and evolution of neurexin genes: insight into the
            mechanism of alternative splicing
  JOURNAL   Genomics 79 (6), 849-859 (2002)
   PUBMED   12036300
REFERENCE   7  (residues 1 to 1504)
  AUTHORS   Rowen,L., Young,J., Birditt,B., Kaur,A., Madan,A., Philipps,D.L.,
            Qin,S., Minx,P., Wilson,R.K., Hood,L. and Graveley,B.R.
  TITLE     Analysis of the human neurexin genes: alternative splicing and the
            generation of protein diversity
  JOURNAL   Genomics 79 (4), 587-597 (2002)
   PUBMED   11944992
REFERENCE   8  (residues 1 to 1504)
  AUTHORS   Ichtchenko,K., Hata,Y., Nguyen,T., Ullrich,B., Missler,M.,
            Moomaw,C. and Sudhof,T.C.
  TITLE     Neuroligin 1: a splice site-specific ligand for beta-neurexins
  JOURNAL   Cell 81 (3), 435-443 (1995)
   PUBMED   7736595
REFERENCE   9  (residues 1 to 1504)
  AUTHORS   Ullrich,B., Ushkaryov,Y.A. and Sudhof,T.C.
  TITLE     Cartography of neurexins: more than 1000 isoforms generated by
            alternative splicing and expressed in distinct subsets of neurons
  JOURNAL   Neuron 14 (3), 497-507 (1995)
   PUBMED   7695896
REFERENCE   10 (residues 1 to 1504)
  AUTHORS   Ushkaryov,Y.A., Petrenko,A.G., Geppert,M. and Sudhof,T.C.
  TITLE     Neurexins: synaptic cell surface proteins related to the
            alpha-latrotoxin receptor and laminin
  JOURNAL   Science 257 (5066), 50-56 (1992)
   PUBMED   1621094
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007682.3, AC009234.3,
            AC007462.3, AC068725.5, AC069550.4 and AC078994.3.
            
            On Aug 16, 2016 this sequence version replaced XP_016860802.1.
            
            Summary: This gene encodes a single-pass type I membrane protein
            that belongs to the neurexin family. Neurexins are cell-surface
            receptors that bind neuroligins to form Ca(2+)-dependent
            neurexin/neuroligin complexes at synapses in the central nervous
            system. This complex is required for efficient neurotransmission
            and is involved in the formation of synaptic contacts. Three
            members of this gene family have been studied in detail and are
            estimated to generate over 3,000 variants through the use of two
            alternative promoters (alpha and beta) and extensive alternative
            splicing in each family member. Recently, a third promoter (gamma)
            was identified for this gene in the 3' region. Mutations in this
            gene are associated with Pitt-Hopkins-like syndrome-2 and may
            contribute to susceptibility to schizophrenia. [provided by RefSeq,
            Aug 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1966682, SAMEA1968189
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1504
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.3"
     Protein         1..1504
                     /product="neurexin-1 isoform alpha9 precursor"
                     /note="neurexin I"
                     /calculated_mol_wt=162141
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3097
     Region          30..190
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Region          307..446
                     /region_name="LamG"
                     /note="Laminin G domain; smart00282"
                     /db_xref="CDD:214598"
     Region          503..652
                     /region_name="LamG"
                     /note="Laminin G domain; smart00282"
                     /db_xref="CDD:214598"
     Region          680..713
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          746..876
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          933..1061
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          1156..1304
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          1449..1467
                     /region_name="4.1m"
                     /note="putative band 4.1 homologues' binding motif;
                     smart00294"
                     /db_xref="CDD:128590"
     CDS             1..1504
                     /gene="NRXN1"
                     /gene_synonym="Hs.22998; PTHSL2; SCZD17"
                     /coded_by="NM_001330086.2:1074..5588"
                     /note="isoform alpha9 precursor is encoded by transcript
                     variant alpha9"
                     /db_xref="GeneID:9378"
                     /db_xref="HGNC:HGNC:8008"
                     /db_xref="MIM:600565"
ORIGIN      
        1 mgtallqrgg cfllclslll lgcwaelgsg lefpgaegqw trfpkwnacc esemsfqlkt
       61 rsarglvlyf ddegfcdfle liltrggrlq lsfsifcaep atlladtpvn dgawhsvrir
      121 rqfrnttlfi dqveakwvev kskrrdmtvf sglfvgglpp elraaalklt lasvrerepf
      181 kgwirdvrvn ssqvlpvdsg evklddeppn sgggspceag eegeggvcln ggvcsvvddq
      241 avcdcsrtgf rgkdcsqedn nveglahlmm gdqgkskgke eyiatfkgse yfcydlsqnp
      301 iqsssdeitl sfktlqrngl mlhtgksady vnlalkngav slvinlgsga fealvepvng
      361 kfndnawhdv kvtrnlrqhs gighamvtis vdgiltttgy tqedytmlgs ddffyvggsp
      421 stadlpgspv snnfmgclke vvyknndvrl elsrlakqgd pkmkihgvva fkcenvatld
      481 pitfetpesf islpkwnakk tgsisfdfrt tepnglilfs hgkprhqkda khpqmikvdf
      541 faiemldghl yllldmgsgt ikikallkkv ndgewyhvdf qrdgrsgtis vntlrtpyta
      601 pgeseildld delylgglpe nkaglvfpte vwtallnygy vgcirdlfid gqskdirqma
      661 evqstagvkp scsketakpc lsnpcknngm crdgwnryvc dcsgtgylgr scereatvls
      721 ydgsmfmkiq lpvvmhteae dvslrfrsqr aygilmatts rdsadtlrle ldagrvkltv
      781 nldcirincn sskgpetlfa gynlndnewh tvrvvrrgks lkltvddqqa mtgqmagdht
      841 rlefhnietg iiterrylss vpsnfighlq sltfngmayi dlckngdidy celnarfgfr
      901 niiadpvtfk tkssyvalat lqaytsmhlf fqfkttsldg lilynsgdgn dfivvelvkg
      961 ylhyvfdlgn ganlikgssn kplndnqwhn vmisrdtsnl htvkidtkit tqitagarnl
     1021 dlksdlyigg vaketykslp klvhakegfq gclasvdlng rlpdlisdal fcngqiergc
     1081 egpsttcqed scsnqgvclq qwdgfscdcs mtsfsgplcn dpgttyifsk gggqitykwp
     1141 pndrpstrad rlaigfstvq keavlvrvds ssglgdylel hihqgkigvk fnvgtddiai
     1201 eesnaiindg kyhvvrftrs ggnatlqvds wpvierypag nndnerlaia rqripyrlgr
     1261 vvdewlldkg rqltifnsqa tiiiggkeqg qpfqgqlsgl yynglkvlnm aaendaniai
     1321 vgnvrlvgev pssmttesta tamqsemsts imettttlat starrgkppt kepisqttdd
     1381 ilvasaecps ddedidpcep ssanptragg repypgsaev iresssttgm vvgivaaaal
     1441 cilillyamy kyrnrdegsy hvdesrnyis nsaqsngavv kekqpssaks snknkknkdk
     1501 eyyv
//
LOCUS       NP_001339527             911 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA ligase 4 isoform 1 [Homo sapiens].
ACCESSION   NP_001339527 XP_006720015
VERSION     NP_001339527.1
DBSOURCE    REFSEQ: accession NM_001352598.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Bayat,L., Abbasi,S., Balasuriya,N. and Schild-Poulter,C.
  TITLE     Critical residues in the Ku70 von Willebrand A domain mediate Ku
            interaction with the LigIV-XRCC4 complex in non-homologous
            end-joining
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (7), 119815 (2024)
   PUBMED   39151475
  REMARK    GeneRIF: Critical residues in the Ku70 von Willebrand A domain
            mediate Ku interaction with the LigIV-XRCC4 complex in
            non-homologous end-joining.
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Nicolle,R., Boutaud,L., Loeuillet,L., Talhi,N., Grotto,S.,
            Bourgon,N., Feresin,A., Coussement,A., Barrois,M., Beaujard,M.P.,
            Rambaud,T., Razavi,F. and Attie-Bitach,T.
  TITLE     Expanding the phenotypic spectrum of LIG4 pathogenic variations:
            neuro-histopathological description of 4 fetuses with stenosis of
            the aqueduct
  JOURNAL   Eur J Hum Genet 32 (5), 545-549 (2024)
   PUBMED   38351293
  REMARK    GeneRIF: Expanding the phenotypic spectrum of LIG4 pathogenic
            variations: neuro-histopathological description of 4 fetuses with
            stenosis of the aqueduct.
REFERENCE   4  (residues 1 to 911)
  AUTHORS   Deng,Y., Ke,T.W., Yueh,T.C., Chin,Y.T., Wang,Y.C., Hung,Y.C.,
            Mong,M.C., Yang,Y.C., Wu,W.T., Chang,W.S., Gu,J., Bau,D.T. and
            Tsai,C.W.
  TITLE     The Contribution of DNA Ligase 4 Polymorphisms to Colorectal Cancer
  JOURNAL   In Vivo 38 (1), 127-133 (2024)
   PUBMED   38148049
  REMARK    GeneRIF: The Contribution of DNA Ligase 4 Polymorphisms to
            Colorectal Cancer.
REFERENCE   5  (residues 1 to 911)
  AUTHORS   Kumari,N., Antil,H., Kumari,S. and Raghavan,S.C.
  TITLE     Deficiency of ligase IV leads to reduced NHEJ, accumulation of DNA
            damage, and can sensitize cells to cancer therapeutics
  JOURNAL   Genomics 115 (6), 110731 (2023)
   PUBMED   37871849
  REMARK    GeneRIF: Deficiency of ligase IV leads to reduced NHEJ,
            accumulation of DNA damage, and can sensitize cells to cancer
            therapeutics.
REFERENCE   6  (residues 1 to 911)
  AUTHORS   Leon,D.A., Chenet,L., Shkolnikov,V.M., Zakharov,S., Shapiro,J.,
            Rakhmanova,G., Vassin,S. and McKee,M.
  TITLE     Huge variation in Russian mortality rates 1984-94: artefact,
            alcohol, or what?
  JOURNAL   Lancet 350 (9075), 383-388 (1997)
   PUBMED   9259651
REFERENCE   7  (residues 1 to 911)
  AUTHORS   Critchlow,S.E., Bowater,R.P. and Jackson,S.P.
  TITLE     Mammalian DNA double-strand break repair protein XRCC4 interacts
            with DNA ligase IV
  JOURNAL   Curr Biol 7 (8), 588-598 (1997)
   PUBMED   9259561
REFERENCE   8  (residues 1 to 911)
  AUTHORS   Grawunder,U., Wilm,M., Wu,X., Kulesza,P., Wilson,T.E., Mann,M. and
            Lieber,M.R.
  TITLE     Activity of DNA ligase IV stimulated by complex formation with
            XRCC4 protein in mammalian cells
  JOURNAL   Nature 388 (6641), 492-495 (1997)
   PUBMED   9242410
REFERENCE   9  (residues 1 to 911)
  AUTHORS   Robins,P. and Lindahl,T.
  TITLE     DNA ligase IV from HeLa cell nuclei
  JOURNAL   J Biol Chem 271 (39), 24257-24261 (1996)
   PUBMED   8798671
REFERENCE   10 (residues 1 to 911)
  AUTHORS   Wei,Y.F., Robins,P., Carter,K., Caldecott,K., Pappin,D.J., Yu,G.L.,
            Wang,R.P., Shell,B.K., Nash,R.A., Schar,P. et al.
  TITLE     Molecular cloning and expression of human cDNAs encoding a novel
            DNA ligase IV and DNA ligase III, an enzyme active in DNA repair
            and recombination
  JOURNAL   Mol Cell Biol 15 (6), 3206-3216 (1995)
   PUBMED   7760816
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157762.13.
            
            On Jun 18, 2017 this sequence version replaced XP_006720015.1.
            
            Summary: The protein encoded by this gene is a DNA ligase that
            joins single-strand breaks in a double-stranded polydeoxynucleotide
            in an ATP-dependent reaction. This protein is essential for V(D)J
            recombination and DNA double-strand break (DSB) repair through
            nonhomologous end joining (NHEJ). This protein forms a complex with
            the X-ray repair cross complementing protein 4 (XRCC4), and further
            interacts with the DNA-dependent protein kinase (DNA-PK). Both
            XRCC4 and DNA-PK are known to be required for NHEJ. The crystal
            structure of the complex formed by this protein and XRCC4 has been
            resolved. Defects in this gene are the cause of LIG4 syndrome.
            Alternatively spliced transcript variants encoding the same protein
            have been observed. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (5), as well as variants 1-3 and
            6-10, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1744883.1,
                                           SRR1660803.41068.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465413, SAMN03465421
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q33.3"
     Protein         1..911
                     /product="DNA ligase 4 isoform 1"
                     /EC_number="6.5.1.1"
                     /note="polynucleotide ligase; ligase IV, DNA,
                     ATP-dependent; DNA repair enzyme; DNA joinase;
                     polydeoxyribonucleotide synthase [ATP] 4; sealase; DNA
                     ligase IV"
                     /calculated_mol_wt=103840
     Region          81..602
                     /region_name="dnl1"
                     /note="DNA ligase I, ATP-dependent (dnl1); TIGR00574"
                     /db_xref="CDD:273147"
     Region          610..620
                     /region_name="Required for catalytic activity.
                     /evidence=ECO:0000269|PubMed:23523427"
                     /note="propagated from UniProtKB/Swiss-Prot (P49917.2)"
     Region          658..745
                     /region_name="BRCT_DNA_ligase_IV_rpt1"
                     /note="first BRCT domain of DNA ligase 4 (LIG4) and
                     similar proteins; cd17722"
                     /db_xref="CDD:349354"
     Region          750..783
                     /region_name="DNA_ligase_IV"
                     /note="DNA ligase IV; pfam11411"
                     /db_xref="CDD:463272"
     Region          813..900
                     /region_name="BRCT_DNA_ligase_IV_rpt2"
                     /note="second BRCT domain of DNA ligase 4 (LIG4) and
                     similar proteins; cd17717"
                     /db_xref="CDD:349349"
     Site            order(814,835..837,839..840,843..844,846..847,895,
                     898..899)
                     /site_type="other"
                     /note="XRCC4 interaction site [polypeptide binding]"
                     /db_xref="CDD:349349"
     CDS             1..911
                     /gene="LIG4"
                     /gene_synonym="LIG4S"
                     /coded_by="NM_001352598.2:634..3369"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS9508.1"
                     /db_xref="GeneID:3981"
                     /db_xref="HGNC:HGNC:6601"
                     /db_xref="MIM:601837"
ORIGIN      
        1 maasqtsqtv ashvpfadlc stleriqksk graekirhfr efldswrkfh dalhknhkdv
       61 tdsfypamrl ilpqlererm aygiketmla klyiellnlp rdgkdalkll nyrtptgthg
      121 dagdfamiay fvlkprclqk gsltiqqvnd lldsiasnns akrkdlikks llqlitqssa
      181 leqkwlirmi ikdlklgvsq qtifsvfhnd aaelhnvttd lekvcrqlhd psvglsdisi
      241 tlfsafkpml aaiadiehie kdmkhqsfyi etkldgermq mhkdgdvyky fsrngynytd
      301 qfgasptegs ltpfihnafk adiqicildg emmaynpntq tfmqkgtkfd ikrmvedsdl
      361 qtcycvfdvl mvnnkklghe tlrkryeils siftpipgri eivqktqaht knevidalne
      421 aidkreegim vkqplsiykp dkrgegwlki kpeyvsglmd eldilivggy wgkgsrggmm
      481 shflcavaek pppgekpsvf htlsrvgsgc tmkelydlgl klakywkpfh rkappssilc
      541 gtekpevyie pcnsvivqik aaeivpsdmy ktgctlrfpr iekirddkew hecmtlddle
      601 qlrgkasgkl askhlyiggd depqekkrka apkmkkvigi iehlkapnlt nvnkisnife
      661 dvefcvmsgt dsqpkpdlen riaefggyiv qnpgpdtycv iagsenirvk niilsnkhdv
      721 vkpawllecf ktksfvpwqp rfmihmcpst kehfareydc ygdsyfidtd lnqlkevfsg
      781 iknsneqtpe emasliadle yryswdcspl smfrrhtvyl dsyavindls tknegtrlai
      841 kalelrfhga kvvsclaegv shviigedhs rvadfkafrr tfkrkfkilk eswvtdsidk
      901 celqeenqyl i
//
LOCUS       NP_001362958             908 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA-splicing factor CWC22 homolog isoform a [Homo sapiens].
ACCESSION   NP_001362958 XP_005246783
VERSION     NP_001362958.1
DBSOURCE    REFSEQ: accession NM_001376029.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 908)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 908)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 908)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   4  (residues 1 to 908)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   5  (residues 1 to 908)
  AUTHORS   Han,S.W., Ahn,J.Y., Lee,S., Noh,Y.S., Jung,H.C., Lee,M.H.,
            Park,H.J., Chun,H.J., Choi,S.J., Kim,E.S. and Lee,J.Y.
  TITLE     Gene expression network analysis of lymph node involvement in colon
            cancer identifies AHSA2, CDK10, and CWC22 as possible prognostic
            markers
  JOURNAL   Sci Rep 10 (1), 7170 (2020)
   PUBMED   32345988
  REMARK    GeneRIF: Gene expression network analysis of lymph node involvement
            in colon cancer identifies AHSA2, CDK10, and CWC22 as possible
            prognostic markers.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 908)
  AUTHORS   Tao,S., Wang,Z., Feng,J., Hsu,F.C., Jin,G., Kim,S.T., Zhang,Z.,
            Gronberg,H., Zheng,L.S., Isaacs,W.B., Xu,J. and Sun,J.
  TITLE     A genome-wide search for loci interacting with known prostate
            cancer risk-associated genetic variants
  JOURNAL   Carcinogenesis 33 (3), 598-603 (2012)
   PUBMED   22219177
REFERENCE   7  (residues 1 to 908)
  AUTHORS   Hegele,A., Kamburov,A., Grossmann,A., Sourlis,C., Wowro,S.,
            Weimann,M., Will,C.L., Pena,V., Luhrmann,R. and Stelzl,U.
  TITLE     Dynamic protein-protein interaction wiring of the human spliceosome
  JOURNAL   Mol Cell 45 (4), 567-580 (2012)
   PUBMED   22365833
REFERENCE   8  (residues 1 to 908)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   9  (residues 1 to 908)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   10 (residues 1 to 908)
  AUTHORS   Kelly,W.G., Xu,S., Montgomery,M.K. and Fire,A.
  TITLE     Distinct requirements for somatic and germline expression of a
            generally expressed Caernorhabditis elegans gene
  JOURNAL   Genetics 146 (1), 227-238 (1997)
   PUBMED   9136012
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC068194.6 and AC096587.1.
            
            On Nov 7, 2019 this sequence version replaced XP_005246783.1.
            
            Transcript Variant: This variant (2), as well as variants 1 and 3,
            encodes isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC057826.1, AK025635.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..908
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.3"
     Protein         1..908
                     /product="pre-mRNA-splicing factor CWC22 homolog isoform
                     a"
                     /note="functional spliceosome-associated protein b;
                     pre-mRNA-splicing factor CWC22 homolog; nucampholin
                     homolog; CWC22 homolog, spliceosome-associated protein;
                     CWC22 spliceosome associated protein homolog"
                     /calculated_mol_wt=105336
     Region          1..129
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCG8.3)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCG8.3)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9HCG8.3)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C5N3; propagated from
                     UniProtKB/Swiss-Prot (Q9HCG8.3)"
     Region          164..345
                     /region_name="MIF4G"
                     /note="Middle domain of eukaryotic initiation factor 4G
                     (eIF4G); smart00543"
                     /db_xref="CDD:214713"
     Region          404..443
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCG8.3)"
     Region          455..561
                     /region_name="MA3"
                     /note="MA3 domain; pfam02847"
                     /db_xref="CDD:397128"
     Region          654..908
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCG8.3)"
     Region          743..>874
                     /region_name="U2AF_lg"
                     /note="U2 snRNP auxilliary factor, large subunit, splicing
                     factor; TIGR01642"
                     /db_xref="CDD:273727"
     Site            786
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCG8.3)"
     Region          821..>902
                     /region_name="SF-CC1"
                     /note="splicing factor, CC1-like family; TIGR01622"
                     /db_xref="CDD:273721"
     Site            829
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9HCG8.3)"
     CDS             1..908
                     /gene="CWC22"
                     /gene_synonym="EIF4GL; fSAPb; NCM"
                     /coded_by="NM_001376029.1:151..2877"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS46465.1"
                     /db_xref="GeneID:57703"
                     /db_xref="HGNC:HGNC:29322"
                     /db_xref="MIM:615186"
ORIGIN      
        1 mkssvaqikp ssghdrrenl nsyqrnsspe dryeeqersp rdrdyfdysr sdyehsrrgr
       61 sydssmesrn rdrekrrere rdtdrkrsrk spspgrrnpe tsvtqsssaq depatkkkkd
      121 eldplltrtg gayippaklr mmqeqitdkn slayqrmswe alkksingli nkvnisnisi
      181 iiqellqeni vrgrgllsrs vlqaqsaspi fthvyaalva iinskfpqig elilkrliln
      241 frkgyrrndk qlcltaskfv ahlinqnvah evlclemltl llerptddsv evaigflkec
      301 glkltqvspr ginaiferlr nilheseidk rvqymievmf avrkdgfkdh piilegldlv
      361 eeddqfthml pleddynped vlnvfkmdpn fmeneekyka ikkeildegd tdsntdqdag
      421 sseedeeeee eegeedeegq kvtihdktei nlvsfrrtiy laiqssldfe ecahkllkme
      481 fpesqtkelc nmildccaqq rtyekffgll agrfcmlkke ymesfegifk eqydtihrle
      541 tnklrnvakm fahllytdsl pwsvlecikl seetttsssr ifvkiffqel ceymglpkln
      601 arlkdetlqp ffegllprdn prntrfainf ftsiglgglt delrehlknt pkvivaqkpd
      661 veqnksspss sssasssses dssdsdsdss dsssesssee sdsssisshs sasandvrkk
      721 ghgktrskev dklirnqqtn drkqkerrqe hghqetrter errsekhrdq nssgsnwrdp
      781 itkytsdkdv psernnysrv andrdqemhi dlenkhgdpk kkrgerrnsf senekhthri
      841 kdsenfrrkd rskskemnrk hsgsrsdedr yqngaerrwe kssryseqsr eskknqdrrr
      901 ekspakqk
//
LOCUS       NP_001120712             261 aa            linear   PRI 21-NOV-2025
DEFINITION  bcl-2-binding component 3 isoform 1 [Homo sapiens].
ACCESSION   NP_001120712
VERSION     NP_001120712.1
DBSOURCE    REFSEQ: accession NM_001127240.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Hao,S., Tong,J., Jha,A., Risnik,D., Lizardo,D., Lu,X., Goel,A.,
            Opresko,P.L., Yu,J. and Zhang,L.
  TITLE     Synthetical lethality of Werner helicase and mismatch repair
            deficiency is mediated by p53 and PUMA in colon cancer
  JOURNAL   Proc Natl Acad Sci U S A 119 (51), e2211775119 (2022)
   PUBMED   36508676
  REMARK    GeneRIF: Synthetical lethality of Werner helicase and mismatch
            repair deficiency is mediated by p53 and PUMA in colon cancer.
            Erratum:[Proc Natl Acad Sci U S A. 2025 Nov 25;122(47):e2529649122.
            doi: 10.1073/pnas.2529649122. PMID: 41259151]
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Chen,Y., Li,N., Yang,J., Li,K., Tang,M., Zhao,X., Guo,W., Tong,A.,
            Nie,C., Peng,Y. and Yuan,Z.
  TITLE     PUMA overexpression dissociates thioredoxin from ASK1 to activate
            the JNK/BCL-2/BCL-XL pathway augmenting apoptosis in ovarian cancer
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1868 (12), 166553 (2022)
   PUBMED   36122664
  REMARK    GeneRIF: PUMA overexpression dissociates thioredoxin from ASK1 to
            activate the JNK/BCL-2/BCL-XL pathway augmenting apoptosis in
            ovarian cancer.
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Chipuk,J.E. and Green,D.R.
  TITLE     PUMA cooperates with direct activator proteins to promote
            mitochondrial outer membrane permeabilization and apoptosis
  JOURNAL   Cell Cycle 8 (17), 2692-2696 (2009)
   PUBMED   19652530
  REMARK    Review article
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Yu,J. and Zhang,L.
  TITLE     PUMA, a potent killer with or without p53
  JOURNAL   Oncogene 27 Suppl 1 (Suppl 1), S71-S83 (2008)
   PUBMED   19641508
  REMARK    GeneRIF: PUMA is a critical mediator of p53-dependent &
            -independent apoptosis induced by a wide variety of stimuli.It
            directly binds and antagonizes all known antiapoptotic Bcl-2 family
            members to induce mitochondrial dysfunction & caspase activation.
            Review.
            Review article
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Hoque,M.O., Begum,S., Sommer,M., Lee,T., Trink,B., Ratovitski,E.
            and Sidransky,D.
  TITLE     PUMA in head and neck cancer
  JOURNAL   Cancer Lett 199 (1), 75-81 (2003)
   PUBMED   12963126
  REMARK    GeneRIF: PUMA suppresses tumor cell growth in head/neck cancer, but
            it does not appear to be a direct target of inactivation in head
            and neck tumorigenesis.
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Yu,J., Wang,Z., Kinzler,K.W., Vogelstein,B. and Zhang,L.
  TITLE     PUMA mediates the apoptotic response to p53 in colorectal cancer
            cells
  JOURNAL   Proc Natl Acad Sci U S A 100 (4), 1931-1936 (2003)
   PUBMED   12574499
  REMARK    GeneRIF: role in mediating the apoptotic response to p53 in
            colorectal cancer cells
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Han,J., Flemington,C., Houghton,A.B., Gu,Z., Zambetti,G.P.,
            Lutz,R.J., Zhu,L. and Chittenden,T.
  TITLE     Expression of bbc3, a pro-apoptotic BH3-only gene, is regulated by
            diverse cell death and survival signals
  JOURNAL   Proc Natl Acad Sci U S A 98 (20), 11318-11323 (2001)
   PUBMED   11572983
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Nakano,K. and Vousden,K.H.
  TITLE     PUMA, a novel proapoptotic gene, is induced by p53
  JOURNAL   Mol Cell 7 (3), 683-694 (2001)
   PUBMED   11463392
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Yu,J., Zhang,L., Hwang,P.M., Kinzler,K.W. and Vogelstein,B.
  TITLE     PUMA induces the rapid apoptosis of colorectal cancer cells
  JOURNAL   Mol Cell 7 (3), 673-682 (2001)
   PUBMED   11463391
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008532.7.
            
            Summary: This gene encodes a member of the BCL-2 family of
            proteins. This family member belongs to the BH3-only pro-apoptotic
            subclass. The protein cooperates with direct activator proteins to
            induce mitochondrial outer membrane permeabilization and apoptosis.
            It can bind to anti-apoptotic Bcl-2 family members to induce
            mitochondrial dysfunction and caspase activation. Because of its
            pro-apoptotic role, this gene is a potential drug target for cancer
            therapy and for tissue injury. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (1) includes an alternate exon in
            the 5' coding region, resulting in a frameshift for the remainder
            of the CDS, compared to variant 2. The encoded isoform (1, also
            known as PUMA-gamma) has the same N-terminus but is otherwise
            distinct and longer, compared to isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF354654.1, ERR279827.7607.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN02400288, SAMN02400289
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 11463392
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..261
                     /product="bcl-2-binding component 3 isoform 1"
                     /note="p53 up-regulated modulator of apoptosis;
                     p53-upregulated modulator of apoptosis"
                     /calculated_mol_wt=26367
     Region          27..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PG8.2)"
     CDS             1..261
                     /gene="BBC3"
                     /gene_synonym="JFY-1; JFY1; PUMA"
                     /coded_by="NM_001127240.3:66..851"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46129.1"
                     /db_xref="GeneID:27113"
                     /db_xref="HGNC:HGNC:17868"
                     /db_xref="MIM:605854"
ORIGIN      
        1 mkfgmgsaqa cpcqvpraas ttwvpcqicg prerhgprtp ggqlpgarrg pgprrpaplp
       61 arppgalgsv lrplrarpgc rprrphpaar clplrphrpt rrhrrpggfp lawgspqpap
      121 rpapgrssal alaggaapgv araqrpggsg grshpggpgs prgggtvgpg drgpaaadgg
      181 rpqrtvraae trgaaaappl tlegpvqshh gtpaltqgpq sprdgaqlga ctrpvdvrds
      241 ggrplpppdt lasagdflct m
//
LOCUS       NP_001387091            1223 aa            linear   PRI 21-NOV-2025
DEFINITION  protein transport protein Sec31A isoform 12 [Homo sapiens].
ACCESSION   NP_001387091
VERSION     NP_001387091.1
DBSOURCE    REFSEQ: accession NM_001400162.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1223)
  AUTHORS   Tobias,E.S., Lucas-Herald,A.K., Sagar,D., Montezano,A.C.,
            Rios,F.J., De Lucca Camargo,L., Hamilton,G., Gazdagh,G.,
            Diver,L.A., Williams,N., Herzyk,P., Touyz,R.M., Greenfield,A.,
            McGowan,R. and Ahmed,S.F.
  TITLE     SEC31A may be associated with pituitary hormone deficiency and
            gonadal dysgenesis
  JOURNAL   Endocrine 84 (2), 345-349 (2024)
   PUBMED   38400880
  REMARK    GeneRIF: SEC31A may be associated with pituitary hormone deficiency
            and gonadal dysgenesis.
REFERENCE   2  (residues 1 to 1223)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1223)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1223)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1223)
  AUTHORS   Jin,L., Pahuja,K.B., Wickliffe,K.E., Gorur,A., Baumgartel,C.,
            Schekman,R. and Rape,M.
  TITLE     Ubiquitin-dependent regulation of COPII coat size and function
  JOURNAL   Nature 482 (7386), 495-500 (2012)
   PUBMED   22358839
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1223)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1223)
  AUTHORS   Kim,J.H., Hong,J.A., Pih,K.T. and Hwang,I.
  TITLE     Identification and isolation of differentially expressed genes in
            osmotically stressed human oral keratinocytes
  JOURNAL   Arch Oral Biol 46 (4), 335-341 (2001)
   PUBMED   11269867
REFERENCE   8  (residues 1 to 1223)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 1223)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   10 (residues 1 to 1223)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021105.13 and AC108469.5.
            
            Summary: The protein encoded by this gene shares similarity with
            the yeast Sec31 protein, and is a component of the outer layer of
            the coat protein complex II (COPII). The encoded protein is
            involved in vesicle budding from the endoplasmic reticulum (ER) and
            contains multiple WD repeats near the N-terminus and a proline-rich
            region in the C-terminal half. It associates with the protein
            encoded by the SEC13 homolog, nuclear pore and COPII coat complex
            component (SEC13), and is required for ER-Golgi transport.
            Monoubiquitylation of this protein by CUL3-KLHL12 was found to
            regulate the size of COPII coats to accommodate unusually shaped
            cargo. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1223
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..1223
                     /product="protein transport protein Sec31A isoform 12"
                     /note="yeast Sec31p homolog; protein transport protein
                     Sec31A; web1-like protein; SEC31 homolog A, COPII coat
                     complex component; SEC31-related protein A; SEC31-like
                     protein 1; SEC31 homolog A, COPII coating complex
                     component"
                     /calculated_mol_wt=133336
     Region          13..332
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(26,40,46..47,52..53,91,95,101..102,117,121,139,144,
                     150..151,164,185,190,196..197,209..210,231,235,244..245,
                     258..259,277,282,288..289,301..302,320,325,331..332)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          70..119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          125..162
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          172..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          263..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          306..331
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <560..>683
                     /region_name="ACE1-Sec16-like"
                     /note="Ancestral coatomer element 1 (ACE1) of COPII coat
                     complex assembly protein Sec16; cl14807"
                     /db_xref="CDD:449359"
     Site            order(561..565,567,569,580,582,583..584,586..587,591,597,
                     605,617,620,645..646)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187750"
     Region          763..>1101
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          <1022..>1188
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     CDS             1..1223
                     /gene="SEC31A"
                     /gene_synonym="ABP125; ABP130; HPBKS; HSPC275; HSPC334;
                     NEDSOSB; SEC31L1"
                     /coded_by="NM_001400162.1:71..3742"
                     /note="isoform 12 is encoded by transcript variant 19"
                     /db_xref="GeneID:22872"
                     /db_xref="HGNC:HGNC:17052"
                     /db_xref="MIM:610257"
ORIGIN      
        1 mklkevdrta mqawspaqnh piylatgtsa qqldatfstn asleifeldl sdpsldmksc
       61 atfssshryh kliwgpykmd skgdvsgvli aggengniil ydpskiiagd kevviaqndk
      121 htgpvraldv nifqtnlvas ganeseiyiw dlnnfatpmt pgaktqpped isciawnrqv
      181 qhilasasps gratvwdlrk nepiikvsdh snrmhcsgla whpdvatqmv laseddrlpv
      241 iqmwdlrfas splrvlenha rgilaiawsm adpelllscg kdakilcsnp ntgevlyelp
      301 tntqwcfdiq wcprnpavls aasfdgrisv ysimggstdg lrqkqvdkls ssfgnldpfg
      361 tgqplpplqi pqqtaqhsiv lplkkppkwi rrpvgasfsf ggklvtfenv rmpshqgaeq
      421 qqqqhhvfis qvvtekefls rsdqlqqavq sqgfinycqk kidasqtefe knvwsflkvn
      481 feddsrgkyl ellgyrkedl gkkalkdsdq vaqsdgeesp aaeeqllgeh ikeekeesef
      541 lpssggtfni svsgdidgli tqalltgnfe savdlclhdn rmadaiilai aggqellart
      601 qkkyfaksqs kitrlitavv mknwkeives cdlknwreal aavltyakpd efsalcdllg
      661 trlenegdsl lqtqaclcyi cagnveklva cwtkaqdgsh plslqdliek vvilrkavql
      721 tqamdtstvg vllaakmsqy anllaaqgsi aaalaflpdn tnqpnimqlr drlcraqgep
      781 vaghespkip yekqqlpkgr pgpvaghhqm prvqtqqyyp hvriaptvtt wsnktptalp
      841 shppaaspsd tqgenppppg fimhgnvnpn aagqlptspg hmhtqvppyp qpqpyqpaqp
      901 ypfgtggsam yrpqqpvapp tsnaypntpy issassytgq sqlyaaqhqa ssptsspats
      961 fppppssgas fqhggpgapp sssayalppg ttgpqngwnd ppalnrvpkk kkmpenfmpp
     1021 vpitspimnp lgdpqsqmlq qqpsapvpls sqssfpqphl pggqpfhgvq qplgqtgmpp
     1081 sfskpniega pgapigntfq hvqslptkki tkkpipdehl ilkttfedli qrclssatdp
     1141 qtkrklddas krleflydkl reqtlsptit sglhniarsi etrnyseglt mhthivstsn
     1201 fsetsafmpv lkvvltqank lgv
//
LOCUS       NP_004402                645 aa            linear   PRI 21-NOV-2025
DEFINITION  cytoplasmic dynein 1 intermediate chain 1 isoform a [Homo sapiens].
ACCESSION   NP_004402
VERSION     NP_004402.1
DBSOURCE    REFSEQ: accession NM_004411.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 645)
  AUTHORS   Ananya,R.G., Pandi,C., Kannan,B., Pandi,A., Prasad,P.,
            Jayaseelan,V.P. and Arumugam,P.
  TITLE     DYNC1I1 acts as a promising prognostic biomarker and is correlated
            with immune infiltration in head and neck squamous cell carcinoma
  JOURNAL   J Stomatol Oral Maxillofac Surg 125 (4), 101734 (2024)
   PUBMED   38072235
  REMARK    GeneRIF: DYNC1I1 acts as a promising prognostic biomarker and is
            correlated with immune infiltration in head and neck squamous cell
            carcinoma.
REFERENCE   3  (residues 1 to 645)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 645)
  AUTHORS   Zhou,J., Zhu,Y., Ma,S., Li,Y., Liu,K., Xu,S., Li,X., Li,L., Hu,J.
            and Liu,Y.
  TITLE     Bioinformatics analysis identifies DYNC1I1 as prognosis marker in
            male patients with liver hepatocellular carcinoma
  JOURNAL   PLoS One 16 (10), e0258797 (2021)
   PUBMED   34679093
  REMARK    GeneRIF: Bioinformatics analysis identifies DYNC1I1 as prognosis
            marker in male patients with liver hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 645)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 645)
  AUTHORS   Ligon,L.A., Tokito,M., Finklestein,J.M., Grossman,F.E. and
            Holzbaur,E.L.
  TITLE     A direct interaction between cytoplasmic dynein and kinesin I may
            coordinate motor activity
  JOURNAL   J Biol Chem 279 (18), 19201-19208 (2004)
   PUBMED   14985359
REFERENCE   7  (residues 1 to 645)
  AUTHORS   Lo,K.W., Naisbitt,S., Fan,J.S., Sheng,M. and Zhang,M.
  TITLE     The 8-kDa dynein light chain binds to its targets via a conserved
            (K/R)XTQT motif
  JOURNAL   J Biol Chem 276 (17), 14059-14066 (2001)
   PUBMED   11148209
REFERENCE   8  (residues 1 to 645)
  AUTHORS   Horikawa,I., Parker,E.S., Solomon,G.G. and Barrett,J.C.
  TITLE     Upregulation of the gene encoding a cytoplasmic dynein intermediate
            chain in senescent human cells
  JOURNAL   J Cell Biochem 82 (3), 415-421 (2001)
   PUBMED   11500918
REFERENCE   9  (residues 1 to 645)
  AUTHORS   Crackower,M.A., Sinasac,D.S., Xia,J., Motoyama,J., Prochazka,M.,
            Rommens,J.M., Scherer,S.W. and Tsui,L.C.
  TITLE     Cloning and characterization of two cytoplasmic dynein intermediate
            chain genes in mouse and human
  JOURNAL   Genomics 55 (3), 257-267 (1999)
   PUBMED   10049579
REFERENCE   10 (residues 1 to 645)
  AUTHORS   King,S.M., Dillman,J.F. 3rd, Benashski,S.E., Lye,R.J.,
            Patel-King,R.S. and Pfister,K.K.
  TITLE     The mouse t-complex-encoded protein Tctex-1 is a light chain of
            brain cytoplasmic dynein
  JOURNAL   J Biol Chem 271 (50), 32281-32287 (1996)
   PUBMED   8943288
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA491512.1, AK313148.1, BP307571.1, DB343806.1 and BC032945.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF063228.1, AK313148.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.3"
     Protein         1..645
                     /product="cytoplasmic dynein 1 intermediate chain 1
                     isoform a"
                     /note="dynein, cytoplasmic, intermediate polypeptide 1;
                     cytoplasmic dynein 1 intermediate chain 1; DH IC-1; dynein
                     intermediate chain 1, cytosolic; cytoplasmic dynein
                     intermediate chain 1"
                     /calculated_mol_wt=72825
     Region          1..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14576.2)"
     Region          2..123
                     /region_name="Interaction with DCTN1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O14576.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q13409; propagated from
                     UniProtKB/Swiss-Prot (O14576.2)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88485; propagated from
                     UniProtKB/Swiss-Prot (O14576.2)"
     Region          96..125
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14576.2)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62871; propagated from
                     UniProtKB/Swiss-Prot (O14576.2)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q13409; propagated from
                     UniProtKB/Swiss-Prot (O14576.2)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13409; propagated from
                     UniProtKB/Swiss-Prot (O14576.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88485; propagated from
                     UniProtKB/Swiss-Prot (O14576.2)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88485; propagated from
                     UniProtKB/Swiss-Prot (O14576.2)"
     Region          143..173
                     /region_name="Dynein_IC2"
                     /note="Cytoplasmic dynein 1 intermediate chain 2;
                     pfam11540"
                     /db_xref="CDD:463291"
     Region          147..163
                     /region_name="Interaction with DYNLT1.
                     /evidence=ECO:0000269|PubMed:27502274"
                     /note="propagated from UniProtKB/Swiss-Prot (O14576.2)"
     Region          169..221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14576.2)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88485; propagated from
                     UniProtKB/Swiss-Prot (O14576.2)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88485; propagated from
                     UniProtKB/Swiss-Prot (O14576.2)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88485; propagated from
                     UniProtKB/Swiss-Prot (O14576.2)"
     Region          285..334
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14576.2)"
     Region          291..337
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <318..607
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          338..378
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14576.2)"
     Region          346..385
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          387..428
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14576.2)"
     Region          393..434
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          437..477
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14576.2)"
     Region          442..481
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          482..527
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14576.2)"
     Region          488..529
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          530..570
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O14576.2)"
     Region          535..573
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          576..615
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14576.2)"
     Region          581..607
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O14576.2)"
     CDS             1..645
                     /gene="DYNC1I1"
                     /gene_synonym="DNCI1; DNCIC1"
                     /coded_by="NM_004411.5:230..2167"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5644.1"
                     /db_xref="GeneID:1780"
                     /db_xref="HGNC:HGNC:2963"
                     /db_xref="MIM:603772"
ORIGIN      
        1 msdksdlkae lerkkqrlaq ireekkrkee erkkkeadmq qkkepvqdds dldrkrrete
       61 allqsigisp epplvqplhf ltwdtcyfhy lvptpmspss ksvstpseag sqdsgdlgpl
      121 trtlqwdtdp svlqlqsdse lgrrlhklgv skvtqvdflp revvsysket qtplathqse
      181 edeedeemve skvgqdsele nqdkkqevke apprelteee kqqilhseef liffdrtirv
      241 ieralaedsd iffdysgrel eekdgdvqag anlsfnrqfy dehwskhrvv tcmdwslqyp
      301 elmvasynnn edaphepdgv alvwnmkfkk ttpeyvfhcq ssvmsvcfar fhpnlvvggt
      361 ysgqivlwdn rshrrtpvqr tplsaaahth pvycvnvvgt qnahnlitvs tdgkmcswsl
      421 dmlstpqesm elvynkskpv avtgmafptg dvnnfvvgse egtvytacrh gskagigevf
      481 eghqgpvtgi nchmavgpid fshlfvtssf dwtvklwttk hnkplysfed nadyvydvmw
      541 spvhpalfac vdgmgrldlw nlnndtevpt asvaiegasa lnrvrwaqag kevavgdseg
      601 riwvydvgel avphndewtr fartlveira nradseeegt velsa
//
LOCUS       NP_001363210             545 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase PAK 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001363210
VERSION     NP_001363210.1
DBSOURCE    REFSEQ: accession NM_001376281.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Kervarrec,T., Westphal,D., Pissaloux,D., Legrand,M., Tirode,F.,
            Neuhart,A., Drouot,F., Becker,J.C., Macagno,N., Seris,A.,
            Jouary,T., Beltzung,F., Jullie,M.L., Harms,P.W., Cribier,B.,
            Mourah,S., Jouenne,F., Fromont,G., Louveau,B., Mancini,M.,
            Kazakov,D.V., de la Fouchardiere,A. and Battistella,M.
  TITLE     Porocarcinomas with PAK1/2/3 fusions: a series of 12 cases
  JOURNAL   Histopathology 85 (4), 566-578 (2024)
   PUBMED   38785043
  REMARK    GeneRIF: Porocarcinomas with PAK1/2/3 fusions: a series of 12
            cases.
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Zhao,P., Zhang,J., Song,W., Qi,D., Huang,Y., Su,Y., Wu,R., Zhang,L.
            and Zhang,S.
  TITLE     Incarvine C and its analogues inhibit the formation of cell
            cytoskeleton by targeting Rac1
  JOURNAL   Bioorg Chem 149, 107512 (2024)
   PUBMED   38833990
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Xu,M.H., Zheng,Y.M., Liang,B.G., Xu,W.X., Cao,J., Wang,P.,
            Dong,Z.Y., Zhou,C.H., Sun,H.C., Ren,N., Ke,A.W. and Shen,Y.H.
  TITLE     Deubiquitination of CIB1 by USP14 promotes lenvatinib resistance
            via the PAK1-ERK1/2 axis in hepatocellular carcinoma
  JOURNAL   Int J Biol Sci 20 (9), 3269-3284 (2024)
   PUBMED   38993552
  REMARK    GeneRIF: Deubiquitination of CIB1 by USP14 promotes lenvatinib
            resistance via the PAK1-ERK1/2 axis in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Luo,Q., Raulston,E.G., Prado,M.A., Wu,X., Gritsman,K., Whalen,K.S.,
            Yan,K., Booth,C.A.G., Xu,R., van Galen,P., Doench,J.G., Shimony,S.,
            Long,H.W., Neuberg,D.S., Paulo,J.A. and Lane,A.A.
  TITLE     Targetable leukaemia dependency on noncanonical PI3Kgamma
            signalling
  JOURNAL   Nature 630 (8015), 198-205 (2024)
   PUBMED   38720074
  REMARK    GeneRIF: Targetable leukaemia dependency on noncanonical PI3Kgamma
            signalling.
REFERENCE   6  (residues 1 to 545)
  AUTHORS   Manser,E., Huang,H.Y., Loo,T.H., Chen,X.Q., Dong,J.M., Leung,T. and
            Lim,L.
  TITLE     Expression of constitutively active alpha-PAK reveals effects of
            the kinase on actin and focal complexes
  JOURNAL   Mol Cell Biol 17 (3), 1129-1143 (1997)
   PUBMED   9032240
REFERENCE   7  (residues 1 to 545)
  AUTHORS   Bokoch,G.M., Wang,Y., Bohl,B.P., Sells,M.A., Quilliam,L.A. and
            Knaus,U.G.
  TITLE     Interaction of the Nck adapter protein with p21-activated kinase
            (PAK1)
  JOURNAL   J Biol Chem 271 (42), 25746-25749 (1996)
   PUBMED   8824201
REFERENCE   8  (residues 1 to 545)
  AUTHORS   Brown,J.L., Stowers,L., Baer,M., Trejo,J., Coughlin,S. and Chant,J.
  TITLE     Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase
            pathway
  JOURNAL   Curr Biol 6 (5), 598-605 (1996)
   PUBMED   8805275
REFERENCE   9  (residues 1 to 545)
  AUTHORS   Martin,G.A., Bollag,G., McCormick,F. and Abo,A.
  TITLE     A novel serine kinase activated by rac1/CDC42Hs-dependent
            autophosphorylation is related to PAK65 and STE20
  JOURNAL   EMBO J 14 (9), 1970-1978 (1995)
   PUBMED   7744004
  REMARK    Erratum:[EMBO J. 1995 Sep 1;14(17):4385. doi:
            10.1002/j.1460-2075.1995.tb00113.x. PMID: 7556080]
REFERENCE   10 (residues 1 to 545)
  AUTHORS   Manser,E., Leung,T., Salihuddin,H., Zhao,Z.S. and Lim,L.
  TITLE     A brain serine/threonine protein kinase activated by Cdc42 and Rac1
  JOURNAL   Nature 367 (6458), 40-46 (1994)
   PUBMED   8107774
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003680.2 and AP000486.6.
            
            Summary: This gene encodes a family member of serine/threonine
            p21-activating kinases, known as PAK proteins. These proteins are
            critical effectors that link RhoGTPases to cytoskeleton
            reorganization and nuclear signaling, and they serve as targets for
            the small GTP binding proteins Cdc42 and Rac. This specific family
            member regulates cell motility and morphology. Mutations in this
            gene have been associated with macrocephaly, seizures, and speech
            delay. Overexpression of this gene is also reported in many cancer
            types, and particularly in breast cancer. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1115507.1,
                                           SRR14038196.1453739.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.5-q14.1"
     Protein         1..545
                     /product="serine/threonine-protein kinase PAK 1 isoform 2"
                     /EC_number="2.7.11.1"
                     /note="p21/Cdc42/Rac1-activated kinase 1 (yeast
                     Ste20-related); p21/Cdc42/Rac1-activated kinase 1 (STE20
                     homolog, yeast); serine/threonine-protein kinase PAK 1;
                     p21 protein (Cdc42/Rac)-activated kinase 1"
                     /calculated_mol_wt=60516
     Region          1..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB and autocatalysis.
                     /evidence=ECO:0000269|PubMed:14585966,
                     ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          70..140
                     /region_name="Autoregulatory region.
                     /evidence=ECO:0000269|PubMed:22153498"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Region          74..132
                     /region_name="PBD"
                     /note="P21-Rho-binding domain; pfam00786"
                     /db_xref="CDD:395634"
     Site            order(75,78,81,83,86,103,107)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238526"
     Region          75..105
                     /region_name="GTPase-binding.
                     /evidence=ECO:0000269|PubMed:22153498"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by OXSR1.
                     /evidence=ECO:0000250|UniProtKB:P35465; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20417602,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000269|PubMed:17726028,
                     ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          159..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17989089,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20417602; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000269|PubMed:17726028; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          211..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17989089,
                     ECO:0000269|PubMed:23260667, ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88643; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88643; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          249..544
                     /region_name="STKc_PAK1"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     p21-activated kinase 1; cd06654"
                     /db_xref="CDD:270820"
     Site            order(276..280,284,297,299,328,344..348,350..351,354,389,
                     391..394,396,406..407,410,423..427,429,456,465..467)
                     /site_type="active"
                     /db_xref="CDD:270820"
     Site            order(276..280,284,297,299,328,344..348,350..351,354,
                     393..394,396,406..407)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270820"
     Site            order(279..280,389,391..393,410,423..427,429,456,465..467)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270820"
     Site            order(281,315,384,386..389,407..408,435..436,438,443,468,
                     471,474)
                     /site_type="other"
                     /note="AID interaction site [polypeptide binding]"
                     /db_xref="CDD:270820"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000269|PubMed:17726028,
                     ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            406..429
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270820"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis, BRSK2 and
                     PDPK1. /evidence=ECO:0000269|PubMed:10551809,
                     ECO:0000269|PubMed:10995762, ECO:0000269|PubMed:22153498,
                     ECO:0000269|PubMed:22669945; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     CDS             1..545
                     /gene="PAK1"
                     /gene_synonym="alpha-PAK; IDDMSSD; p65-PAK; PAKalpha"
                     /coded_by="NM_001376281.1:632..2269"
                     /note="isoform 2 is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS8250.1"
                     /db_xref="GeneID:5058"
                     /db_xref="HGNC:HGNC:8590"
                     /db_xref="MIM:602590"
ORIGIN      
        1 msnngldiqd kppappmrnt stmigagskd agtlnhgskp lppnpeekkk kdrfyrsilp
       61 gdktnkkkek erpeislpsd fehtihvgfd avtgeftgmp eqwarllqts nitkseqkkn
      121 pqavldvlef ynskktsnsq kymsftdksa edynssnaln vkavsetpav ppvsededdd
      181 dddatpppvi aprpehtksv ytrsvieplp vtptrdvats pisptenntt ppdaltrnte
      241 kqkkkpkmsd eeileklrsi vsvgdpkkky trfekigqga sgtvytamdv atgqevaikq
      301 mnlqqqpkke liineilvmr enknpnivny ldsylvgdel wvvmeylagg sltdvvtetc
      361 mdegqiaavc reclqalefl hsnqvihrdi ksdnillgmd gsvkltdfgf caqitpeqsk
      421 rstmvgtpyw mapevvtrka ygpkvdiwsl gimaiemieg eppylnenpl ralyliatng
      481 tpelqnpekl saifrdflnr clemdvekrg sakellqhqf lkiakplssl tpliaaakea
      541 tknnh
//
LOCUS       NP_001135890             288 aa            linear   PRI 21-NOV-2025
DEFINITION  mortality factor 4-like protein 2 [Homo sapiens].
ACCESSION   NP_001135890
VERSION     NP_001135890.1
DBSOURCE    REFSEQ: accession NM_001142418.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Kooblall,K.G., Stokes,V.J., Shariq,O.A., English,K.A.,
            Stevenson,M., Broxholme,J., Wright,B., Lockstone,H.E., Buck,D.,
            Grozinsky-Glasberg,S., Yates,C.J., Thakker,R.V. and Lines,K.E.
  TITLE     miR-3156-5p is downregulated in serum of MEN1 patients and
            regulates expression of MORF4L2
  JOURNAL   Endocr Relat Cancer 29 (10), 557-568 (2022)
   PUBMED   35900839
  REMARK    GeneRIF: miR-3156-5p is downregulated in serum of MEN1 patients and
            regulates expression of MORF4L2.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Zheng,X., Sun,Z., Yu,L., Shi,D., Zhu,M., Yao,H. and Li,L.
  TITLE     Interactome Analysis of the Nucleocapsid Protein of SARS-CoV-2
            Virus
  JOURNAL   Pathogens 10 (9), 1155 (2021)
   PUBMED   34578187
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Cai,Y., Jin,J., Tomomori-Sato,C., Sato,S., Sorokina,I.,
            Parmely,T.J., Conaway,R.C. and Conaway,J.W.
  TITLE     Identification of new subunits of the multiprotein mammalian
            TRRAP/TIP60-containing histone acetyltransferase complex
  JOURNAL   J Biol Chem 278 (44), 42733-42736 (2003)
   PUBMED   12963728
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Yochum,G.S. and Ayer,D.E.
  TITLE     Role for the mortality factors MORF4, MRGX, and MRG15 in
            transcriptional repression via associations with Pf1, mSin3A, and
            Transducin-Like Enhancer of Split
  JOURNAL   Mol Cell Biol 22 (22), 7868-7876 (2002)
   PUBMED   12391155
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Sakai,K., Shirakawa,T., Li,Y., Kitagawa,Y. and Hirose,G.
  TITLE     Interaction of a paraneoplastic cerebellar degeneration-associated
            neuronal protein with the nuclear helix-loop-helix leucine zipper
            protein MRG X
  JOURNAL   Mol Cell Neurosci 19 (4), 477-484 (2002)
   PUBMED   11988016
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Hoja,M.R., Wahlestedt,C. and Hoog,C.
  TITLE     A visual intracellular classification strategy for uncharacterized
            human proteins
  JOURNAL   Exp Cell Res 259 (1), 239-246 (2000)
   PUBMED   10942595
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Bertram,M.J., Berube,N.G., Hang-Swanson,X., Ran,Q., Leung,J.K.,
            Bryce,S., Spurgers,K., Bick,R.J., Baldini,A., Ning,Y., Clark,L.J.,
            Parkinson,E.K., Barrett,J.C., Smith,J.R. and Pereira-Smith,O.M.
  TITLE     Identification of a gene that reverses the immortal phenotype of a
            subset of cells and is a member of a novel family of transcription
            factor-like genes
  JOURNAL   Mol Cell Biol 19 (2), 1479-1485 (1999)
   PUBMED   9891081
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC419967.1 and BC093013.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.137326.1,
                                           SRR14038191.4351965.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2149876
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.2"
     Protein         1..288
                     /product="mortality factor 4-like protein 2"
                     /note="MSL3-2 protein; protein MSL3-2; MORF-related gene X
                     protein; transcription factor-like protein MRGX"
                     /calculated_mol_wt=32177
     Region          1..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15014.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15014.1)"
     Region          102..276
                     /region_name="MRG"
                     /note="pfam05712"
                     /db_xref="CDD:461721"
     CDS             1..288
                     /gene="MORF4L2"
                     /gene_synonym="MORFL2; MRGX"
                     /coded_by="NM_001142418.2:386..1252"
                     /db_xref="CCDS:CCDS14512.1"
                     /db_xref="GeneID:9643"
                     /db_xref="HGNC:HGNC:16849"
                     /db_xref="MIM:300409"
ORIGIN      
        1 mssrkqgsqp rgqqsaeeen fkkptrsnmq rskmrgassg kktagpqqkn lepalpgrwg
       61 grsaenppsg svrktrknkq ktpgngdggs tseapqpprk kraradptve seeafknrme
      121 vkvkipeelk pwlvedwdlv trqkqlfqlp akknvdaile eyanckksqg nvdnkeyavn
      181 evvagikeyf nvmlgtqlly kferpqyaei llahpdapms qvygaphllr lfvrigamla
      241 ytpldeksla lllgylhdfl kylaknsasl ftasdykvas aeyhrkal
//
LOCUS       NP_001333254             517 aa            linear   PRI 21-NOV-2025
DEFINITION  autophagy-related protein 13 isoform c [Homo sapiens].
ACCESSION   NP_001333254 XP_011518803
VERSION     NP_001333254.1
DBSOURCE    REFSEQ: accession NM_001346325.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Patel,A. and Faesen,A.C.
  TITLE     Metamorphosis by ATG13 and ATG101 in human autophagy initiation
  JOURNAL   Autophagy 20 (4), 968-969 (2024)
   PUBMED   37394799
  REMARK    GeneRIF: Metamorphosis by ATG13 and ATG101 in human autophagy
            initiation.
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Nguyen,A. and Faesen,A.C.
  TITLE     The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis
  JOURNAL   FEBS Lett 598 (1), 114-126 (2024)
   PUBMED   37567770
  REMARK    GeneRIF: The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis.
            Review article
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Karabi,Z., Moradian,F. and Kheirabadi,M.
  TITLE     The effect of lactoferrin on ULK1 and ATG13 genes expression in
            breast cancer cell line MCF7 and bioinformatics studies of protein
            interaction between lactoferrin and the autophagy initiation
            complex
  JOURNAL   Cell Biochem Biophys 80 (4), 795-806 (2022)
   PUBMED   36169801
  REMARK    GeneRIF: The effect of lactoferrin on ULK1 and ATG13 genes
            expression in breast cancer cell line MCF7 and bioinformatics
            studies of protein interaction between lactoferrin and the
            autophagy initiation complex.
REFERENCE   5  (residues 1 to 517)
  AUTHORS   Gottschalk,G., Peterson,D., Knox,K., Maynard,M., Whelan,R.J. and
            Roy,A.
  TITLE     Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE)
  JOURNAL   Mol Cell Neurosci 120, 103731 (2022)
   PUBMED   35487443
  REMARK    GeneRIF: Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE).
REFERENCE   6  (residues 1 to 517)
  AUTHORS   Jung,C.H., Jun,C.B., Ro,S.H., Kim,Y.M., Otto,N.M., Cao,J., Kundu,M.
            and Kim,D.H.
  TITLE     ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy
            machinery
  JOURNAL   Mol Biol Cell 20 (7), 1992-2003 (2009)
   PUBMED   19225151
  REMARK    GeneRIF: The ULK-Atg13-FIP200 complexes are direct targets of mTOR
            and important regulators of autophagy in response to mTOR
            signaling.
REFERENCE   7  (residues 1 to 517)
  AUTHORS   Hosokawa,N., Hara,T., Kaizuka,T., Kishi,C., Takamura,A., Miura,Y.,
            Iemura,S., Natsume,T., Takehana,K., Yamada,N., Guan,J.L., Oshiro,N.
            and Mizushima,N.
  TITLE     Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200
            complex required for autophagy
  JOURNAL   Mol Biol Cell 20 (7), 1981-1991 (2009)
   PUBMED   19211835
  REMARK    GeneRIF: mTORC1 suppresses autophagy through direct regulation of
            the approximately 3-MDa ULK1-Atg13-FIP200 complex.
REFERENCE   8  (residues 1 to 517)
  AUTHORS   Chan,E.Y., Longatti,A., McKnight,N.C. and Tooze,S.A.
  TITLE     Kinase-inactivated ULK proteins inhibit autophagy via their
            conserved C-terminal domains using an Atg13-independent mechanism
  JOURNAL   Mol Cell Biol 29 (1), 157-171 (2009)
   PUBMED   18936157
  REMARK    GeneRIF: The functions of ULK1 and ULK2 are controlled by
            autophosphorylation and conformational changes involving exposure
            of the C-terminal domain and interaction with the putative human
            homologue of Atg13.
            GeneRIF: The gene product is the functional homologue of yeast
            Atg13, and required for autophagy in mammalian cells.
REFERENCE   9  (residues 1 to 517)
  AUTHORS   Meijer,W.H., van der Klei,I.J., Veenhuis,M. and Kiel,J.A.
  TITLE     ATG genes involved in non-selective autophagy are conserved from
            yeast to man, but the selective Cvt and pexophagy pathways also
            require organism-specific genes
  JOURNAL   Autophagy 3 (2), 106-116 (2007)
   PUBMED   17204848
REFERENCE   10 (residues 1 to 517)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC127035.6 and AC115088.6.
            
            On Oct 9, 2016 this sequence version replaced XP_011518803.1.
            
            Summary: The protein encoded by this gene is an autophagy factor
            and a target of the TOR kinase signaling pathway. The encoded
            protein is essential for autophagosome formation and mitophagy.
            [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (21), as well as variants 1, 4,
            15-20, and 22-28, encodes isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.117747.1,
                                           SRR1803611.273014.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..517
                     /product="autophagy-related protein 13 isoform c"
                     /note="autophagy-related protein 13; ATG13 autophagy
                     related 13 homolog"
                     /calculated_mol_wt=56441
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O75143.1)"
     Region          19..192
                     /region_name="ATG13"
                     /note="Autophagy-related protein 13; pfam10033"
                     /db_xref="CDD:431003"
     Region          127..134
                     /region_name="Important for interaction with ATG101.
                     /evidence=ECO:0000269|PubMed:26299944"
                     /note="propagated from UniProtKB/Swiss-Prot (O75143.1)"
     Region          305..324
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75143.1)"
     Region          332..361
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75143.1)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ULK1.
                     /evidence=ECO:0000269|PubMed:21855797,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75143.1)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75143.1)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75143.1)"
     Region          405..439
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75143.1)"
     Region          444..447
                     /region_name="LIR. /evidence=ECO:0000305|PubMed:24290141"
                     /note="propagated from UniProtKB/Swiss-Prot (O75143.1)"
     CDS             1..517
                     /gene="ATG13"
                     /gene_synonym="KIAA0652; PARATARG8"
                     /coded_by="NM_001346325.2:524..2077"
                     /note="isoform c is encoded by transcript variant 21"
                     /db_xref="CCDS:CCDS44582.1"
                     /db_xref="GeneID:9776"
                     /db_xref="HGNC:HGNC:29091"
                     /db_xref="MIM:615088"
ORIGIN      
        1 metdlnsqdr kdldkfikff alktvqvivq arlgekictr ssssptgsdw fnlaikdipe
       61 vtheakkala gqlpavgrsm cveislktse gdsmeleiwc lemnekcdke ikvsytvynr
      121 lslllkslla itrvtpayrl srkqgheyvi lyriyfgevq lsglgegfqt vrvgtvgtpv
      181 gtitlscayr inlafmstrq fertppimgi iidhfvdrpy pssspmhpcn yrtagedtgv
      241 iypsvedsqe vcttsfstsp psqlsssrls yqpaalgvgs adlaypvvfa aglnathphq
      301 lmvpgkeggv plapnqpvhg tqadqerlat ctpsdrthca atpsssedte tvsnssegra
      361 sphdvletif vrkvgafvnk pinqvtltsl dipfamfapk nleledtdpm vnppdspete
      421 splqgslhsd gssggssgnt hddfvmidfk pafskddilp mdlgtfyref qnppqlssls
      481 idigaqsmae dldslpekla vheknvrefd afvetlq
//
LOCUS       NP_001027539             513 aa            linear   PRI 21-NOV-2025
DEFINITION  kunitz-type protease inhibitor 1 isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_001027539
VERSION     NP_001027539.1
DBSOURCE    REFSEQ: accession NM_001032367.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Lu,D.D., Huang,N., Li,S.A., Fang,J.R., Lai,C.H., Wang,J.K.,
            Chan,K.S., Johnson,M.D. and Lin,C.Y.
  TITLE     HAI-1 is required for the novel role of FGFBP1 in maintenance of
            cell morphology and F-actin rearrangement in human keratinocytes
  JOURNAL   Hum Cell 36 (4), 1403-1415 (2023)
   PUBMED   37076641
  REMARK    GeneRIF: HAI-1 is required for the novel role of FGFBP1 in
            maintenance of cell morphology and F-actin rearrangement in human
            keratinocytes.
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Izumi,A., Yamamoto,K., Kawaguchi,M., Yamashita,F., Fukushima,T.,
            Kiwaki,T., Tanaka,H., Yamashita,Y. and Kataoka,H.
  TITLE     Insufficiency of hepatocyte growth factor activator inhibitor-1
            confers lymphatic invasion of tongue carcinoma cells
  JOURNAL   Cancer Sci 113 (6), 2179-2193 (2022)
   PUBMED   35332604
  REMARK    GeneRIF: Insufficiency of hepatocyte growth factor activator
            inhibitor-1 confers lymphatic invasion of tongue carcinoma cells.
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Yamashita,F., Kaieda,T., Shimomura,T., Kawaguchi,M., Lin,C.Y.,
            Johnson,M.D., Tanaka,H., Kiwaki,T., Fukushima,T. and Kataoka,H.
  TITLE     Role of the polycystic kidney disease domain in matriptase
            chaperone activity and localization of hepatocyte growth factor
            activator inhibitor-1
  JOURNAL   FEBS J 289 (12), 3422-3439 (2022)
   PUBMED   35020274
  REMARK    GeneRIF: Role of the polycystic kidney disease domain in matriptase
            chaperone activity and localization of hepatocyte growth factor
            activator inhibitor-1.
            Review article
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Wu,Q., Yin,G., Luo,J., Zhang,Y., Ai,T., Tian,J., Jin,Y., Lei,J. and
            Liu,S.
  TITLE     Comprehensive Analysis of the Expression and Prognostic Value of
            SPINT1/2 in Breast Carcinoma
  JOURNAL   Front Endocrinol (Lausanne) 12, 665666 (2021)
   PUBMED   34381422
  REMARK    GeneRIF: Comprehensive Analysis of the Expression and Prognostic
            Value of SPINT1/2 in Breast Carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 513)
  AUTHORS   Shimomura,T., Denda,K., Kawaguchi,T., Matsumoto,K., Miyazawa,K. and
            Kitamura,N.
  TITLE     Multiple sites of proteolytic cleavage to release soluble forms of
            hepatocyte growth factor activator inhibitor type 1 from a
            transmembrane form
  JOURNAL   J Biochem 126 (5), 821-828 (1999)
   PUBMED   10544273
REFERENCE   7  (residues 1 to 513)
  AUTHORS   Lin,C.Y., Anders,J., Johnson,M. and Dickson,R.B.
  TITLE     Purification and characterization of a complex containing
            matriptase and a Kunitz-type serine protease inhibitor from human
            milk
  JOURNAL   J Biol Chem 274 (26), 18237-18242 (1999)
   PUBMED   10373425
REFERENCE   8  (residues 1 to 513)
  AUTHORS   Kataoka,H., Suganuma,T., Shimomura,T., Itoh,H., Kitamura,N.,
            Nabeshima,K. and Koono,M.
  TITLE     Distribution of hepatocyte growth factor activator inhibitor type 1
            (HAI-1) in human tissues. Cellular surface localization of HAI-1 in
            simple columnar epithelium and its modulated expression in injured
            and regenerative tissues
  JOURNAL   J Histochem Cytochem 47 (5), 673-682 (1999)
   PUBMED   10219059
REFERENCE   9  (residues 1 to 513)
  AUTHORS   Yamada,T., Tsujioka,Y., Taguchi,J., Takahashi,M., Tsuboi,Y. and
            Shimomura,T.
  TITLE     White matter astrocytes produce hepatocyte growth factor activator
            inhibitor in human brain tissues
  JOURNAL   Exp Neurol 153 (1), 60-64 (1998)
   PUBMED   9743567
REFERENCE   10 (residues 1 to 513)
  AUTHORS   Shimomura,T., Denda,K., Kitamura,A., Kawaguchi,T., Kito,M.,
            Kondo,J., Kagaya,S., Qin,L., Takata,H., Miyazawa,K. and Kitamura,N.
  TITLE     Hepatocyte growth factor activator inhibitor, a novel Kunitz-type
            serine protease inhibitor
  JOURNAL   J Biol Chem 272 (10), 6370-6376 (1997)
   PUBMED   9045658
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012476.8 and AI684245.1.
            
            Summary: The protein encoded by this gene is a member of the Kunitz
            family of serine protease inhibitors. The protein is a potent
            inhibitor specific for HGF activator and is thought to be involved
            in the regulation of the proteolytic activation of HGF in injured
            tissues. Alternative splicing results in multiple variants encoding
            different isoforms. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) has multiple differences in
            the 5' UTR and uses an alternate in-frame splice site in the 3'
            coding region, compared to variant 1, resulting in a shorter
            protein (isoform 2), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1097828.1,
                                           SRR7346977.954714.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.1"
     Protein         1..513
                     /product="kunitz-type protease inhibitor 1 isoform 2
                     precursor"
                     /note="serine protease inhibitor, Kunitz type 1;
                     Kunitz-type protease inhibitor 1; HAI-1; hepatocyte growth
                     factor activator inhibitor type 1"
                     /calculated_mol_wt=53312
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3591
     mat_peptide     36..513
                     /product="kunitz-type protease inhibitor 1 isoform 2"
                     /calculated_mol_wt=53312
     Region          50..139
                     /region_name="MANEC"
                     /note="MANEC domain; pfam07502"
                     /db_xref="CDD:462186"
     Region          245..303
                     /region_name="Kunitz_HAI1_1-like"
                     /note="Kunitz domain 1 of hepatocyte growth factor
                     activator inhibitor-1 (HAI-1); cd22623"
                     /db_xref="CDD:438666"
     Site            order(256..265,279,281,283..284,286,289,291)
                     /site_type="other"
                     /note="serine protease binding site [polypeptide binding]"
                     /db_xref="CDD:438666"
     Region          318..350
                     /region_name="LDLa"
                     /note="Low-density lipoprotein receptor domain class A;
                     smart00192"
                     /db_xref="CDD:197566"
     Site            order(324,332,343..344)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(336,339,343,349..350)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            346..350
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          374..434
                     /region_name="Kunitz_HAI1_2-like"
                     /note="Kunitz domain 2 of hepatocyte growth factor
                     activator inhibitor-1 (HAI1); cd22624"
                     /db_xref="CDD:438667"
     Site            order(381..385,387..389,404,408)
                     /site_type="other"
                     /note="putative serine protease binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438667"
     CDS             1..513
                     /gene="SPINT1"
                     /gene_synonym="HAI; HAI1; MANSC2"
                     /coded_by="NM_001032367.2:79..1620"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS45231.1"
                     /db_xref="GeneID:6692"
                     /db_xref="HGNC:HGNC:11246"
                     /db_xref="MIM:605123"
ORIGIN      
        1 mapartmara rlapagipav alwllctlgl qgtqagpppa ppglpagadc lnsftagvpg
       61 fvldtnasvs ngatflespt vrrgwdcvra ccttqncnla lvelqpdrge daiaacflin
      121 clyeqnfvck fapregfiny ltrevyrsyr qlrtqgfggs gipkawagid lkvqpqeplv
      181 lkdventdwr llrgdtdvrv erkdpnqvel wglkegtylf qltvtssdhp edtanvtvtv
      241 lstkqtedyc lasnkvgrcr gsfprwyydp teqicksfvy ggclgnknny lreeecilac
      301 rgvqgpsmer rhpvcsgtcq ptqfrcsngc cidsflecdd tpncpdasde aacekytsgf
      361 delqrihfps dkghcvdlpd tglckesipr wyynpfsehc arftyggcyg nknnfeeeqq
      421 clescrgisk kdvfglrrei pipstgsvem avavflvici vvvvailgyc ffknqrkdfh
      481 ghhhhppptp asstvstted tehlvynhtt rpl
//
LOCUS       NP_001381510             753 aa            linear   PRI 21-NOV-2025
DEFINITION  dynein axonemal heavy chain 3 isoform 3 [Homo sapiens].
ACCESSION   NP_001381510
VERSION     NP_001381510.1
DBSOURCE    REFSEQ: accession NM_001394581.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Wang,X., Shen,G., Yang,Y., Jiang,C., Ruan,T., Yang,X., Zhuo,L.,
            Zhang,Y., Ou,Y., Zhao,X., Long,S., Tang,X., Lin,T. and Shen,Y.
  TITLE     DNAH3 deficiency causes flagellar inner dynein arm loss and male
            infertility in humans and mice
  JOURNAL   Elife 13, 96755 (2024)
   PUBMED   39503742
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Li,S., Zhang,Z., Xie,L., Zhao,Y., Chen,H., Zhang,S., Cai,Y.,
            Ren,B., Liu,W., Tang,S. and Sha,Y.
  TITLE     Novel bi-allelic DNAH3 variants cause oligoasthenoteratozoospermia
  JOURNAL   Front Endocrinol (Lausanne) 15, 1462509 (2024)
   PUBMED   39588341
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Meng,G.Q., Wang,Y., Luo,C., Tan,Y.M., Li,Y., Tan,C., Tu,C.,
            Zhang,Q.J., Hu,L., Zhang,H., Meng,L.L., Liu,C.Y., Deng,L., Lu,G.X.,
            Lin,G., Du,J., Tan,Y.Q., Sha,Y., Wang,L. and He,W.B.
  TITLE     Bi-allelic variants in DNAH3 cause male infertility with
            asthenoteratozoospermia in humans and mice
  JOURNAL   Hum Reprod Open 2024 (1), hoae003 (2024)
   PUBMED   38312775
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Kennedy,R.B., Ovsyannikova,I.G., Pankratz,V.S., Haralambieva,I.H.,
            Vierkant,R.A. and Poland,G.A.
  TITLE     Genome-wide analysis of polymorphisms associated with cytokine
            responses in smallpox vaccine recipients
  JOURNAL   Hum Genet 131 (9), 1403-1421 (2012)
   PUBMED   22610502
REFERENCE   5  (residues 1 to 753)
  AUTHORS   Maiti,A.K., Mattei,M.G., Jorissen,M., Volz,A., Zeigler,A. and
            Bouvagnet,P.
  TITLE     Identification, tissue specific expression, and chromosomal
            localisation of several human dynein heavy chain genes
  JOURNAL   Eur J Hum Genet 8 (12), 923-932 (2000)
   PUBMED   11175280
REFERENCE   6  (residues 1 to 753)
  AUTHORS   Loftus,B.J., Kim,U.J., Sneddon,V.P., Kalush,F., Brandon,R.,
            Fuhrmann,J., Mason,T., Crosby,M.L., Barnstead,M., Cronin,L.,
            Deslattes Mays,A., Cao,Y., Xu,R.X., Kang,H.L., Mitchell,S.,
            Eichler,E.E., Harris,P.C., Venter,J.C. and Adams,M.D.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
   PUBMED   10493829
REFERENCE   7  (residues 1 to 753)
  AUTHORS   Milisav,I.
  TITLE     Dynein and dynein-related genes
  JOURNAL   Cell Motil Cytoskeleton 39 (4), 261-272 (1998)
   PUBMED   9556328
  REMARK    Review article
REFERENCE   8  (residues 1 to 753)
  AUTHORS   Neesen,J., Koehler,M.R., Kirschner,R., Steinlein,C.,
            Kreutzberger,J., Engel,W. and Schmid,M.
  TITLE     Identification of dynein heavy chain genes expressed in human and
            mouse testis: chromosomal localization of an axonemal dynein gene
  JOURNAL   Gene 200 (1-2), 193-202 (1997)
   PUBMED   9373155
REFERENCE   9  (residues 1 to 753)
  AUTHORS   Chapelin,C., Duriez,B., Magnino,F., Goossens,M., Escudier,E. and
            Amselem,S.
  TITLE     Isolation of several human axonemal dynein heavy chain genes:
            genomic structure of the catalytic site, phylogenetic analysis and
            chromosomal assignment
  JOURNAL   FEBS Lett 412 (2), 325-330 (1997)
   PUBMED   9256245
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008551.5.
            
            Summary: This gene belongs to the dynein family, whose members
            encode large proteins that are constituents of the
            microtubule-associated motor protein complex. This complex is
            composed of dynein heavy, intermediate and light chains, which can
            be axonemal or cytoplasmic. This protein is an axonemal dynein
            heavy chain. It is involved in producing force for ciliary beating
            by using energy from ATP hydrolysis. Alternative splicing results
            in multiple transcript variants encoding distinct isoforms.
            [provided by RefSeq, Dec 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056509.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.3"
     Protein         1..753
                     /product="dynein axonemal heavy chain 3 isoform 3"
                     /note="dynein, axonemal, heavy polypeptide 3; dynein heavy
                     chain 3, axonemal; axonemal dynein, heavy chain; ciliary
                     dynein heavy chain 3; axonemal beta dynein heavy chain 3;
                     epididymis luminal protein 36"
                     /calculated_mol_wt=87370
     CDS             1..753
                     /gene="DNAH3"
                     /gene_synonym="DNAHC3-B; DNAHC3B; HDHC8; HEL-36; HSADHC3"
                     /coded_by="NM_001394581.1:312..2573"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:55567"
                     /db_xref="HGNC:HGNC:2949"
                     /db_xref="MIM:603334"
ORIGIN      
        1 mgdmdcssqk iaksdsihhm shsqgqpelp plpasaneep sglyqtvmsh sfypplmqrt
       61 swtlaapfke qhhhrgpsds iannyslmaq dlklkdllkv yqpatisvpr drtgqglpss
      121 gnrsssepmr kktkfssrnk edstriklaf ktsifspmkk evktsltfpg srpmspeqql
      181 dvmlqqemem eskekkpses dleryyyylt ngirkdmiap eegevmvris klisntllts
      241 pfleplmvvl vqekendyyc slmksivdyi lmdpmerkrl fiesiprlfp qrvirapvpw
      301 hsvyrsakkw neehlhtvnp mmlrlkelwf aefrdlrfvr taeilagklp lqpqefwdvi
      361 qkhcleahqt llnkwiptca qlftsrkehw ihfapksnyd ssrnieeyfa svasfmslql
      421 relviksled lvslfmihkd gndfkepyqe mkffipqlim iklevsepii vfnpsfdgcw
      481 elirdsflei iknsngipkv esvlfpelkg ynlllgtvna eeklvsdfli qtfkvfqknq
      541 vgpckylnvy kkyvdlldnt aeqniaaflk enhdiddfvt kinaikkrrn eiasmnitvp
      601 lamfcldata lnhdlceraq nlkdhliqfq vdvnrdtnts icnqyshiad kvsevpantk
      661 elvslieflk kssavtvfkl rrqlrdaser leflmdyadl pyediklnst lflwpdqied
      721 ifdnsrnlll hkrdqaemdl ikryreslgl swk
//
LOCUS       NP_001337376             961 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 1 isoform 43 [Homo
            sapiens].
ACCESSION   NP_001337376
VERSION     NP_001337376.1
DBSOURCE    REFSEQ: accession NM_001350447.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 961)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 961)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 961)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 961)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 961)
  AUTHORS   Ruhle,F., Witten,A., Barysenka,A., Huge,A., Arning,A., Heller,C.,
            Krumpel,A., Mesters,R., Franke,A., Lieb,W., Riemenschneider,M.,
            Hiersche,M., Limperger,V., Nowak-Gottl,U. and Stoll,M.
  TITLE     Rare genetic variants in SMAP1, B3GAT2, and RIMS1 contribute to
            pediatric venous thromboembolism
  JOURNAL   Blood 129 (6), 783-790 (2017)
   PUBMED   28011674
  REMARK    GeneRIF: The study identified a region on chromosome 6 comprising
            the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus
            for pediatric venous thromboembolism.
REFERENCE   6  (residues 1 to 961)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 961)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
REFERENCE   8  (residues 1 to 961)
  AUTHORS   Schoch,S., Castillo,P.E., Jo,T., Mukherjee,K., Geppert,M., Wang,Y.,
            Schmitz,F., Malenka,R.C. and Sudhof,T.C.
  TITLE     RIM1alpha forms a protein scaffold for regulating neurotransmitter
            release at the active zone
  JOURNAL   Nature 415 (6869), 321-326 (2002)
   PUBMED   11797009
REFERENCE   9  (residues 1 to 961)
  AUTHORS   Coppola,T., Magnin-Luthi,S., Perret-Menoud,V., Gattesco,S.,
            Schiavo,G. and Regazzi,R.
  TITLE     Direct interaction of the Rab3 effector RIM with Ca2+ channels,
            SNAP-25, and synaptotagmin
  JOURNAL   J Biol Chem 276 (35), 32756-32762 (2001)
   PUBMED   11438518
REFERENCE   10 (residues 1 to 961)
  AUTHORS   Betz,A., Thakur,P., Junge,H.J., Ashery,U., Rhee,J.S., Scheuss,V.,
            Rosenmund,C., Rettig,J. and Brose,N.
  TITLE     Functional interaction of the active zone proteins Munc13-1 and
            RIM1 in synaptic vesicle priming
  JOURNAL   Neuron 30 (1), 183-196 (2001)
   PUBMED   11343654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590011.5, AL445256.18 and
            AL035633.18.
            
            Summary: The protein encoded by this gene is a RAS gene superfamily
            member that regulates synaptic vesicle exocytosis. This gene also
            plays a role in the regulation of voltage-gated calcium channels
            during neurotransmitter and insulin release. Mutations have
            suggested a role cognition and have been identified as the cause of
            cone-rod dystrophy type 7. Multiple transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Mar 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.252359.1,
                                           SRR1803615.81125.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..961
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..961
                     /product="regulating synaptic membrane exocytosis protein
                     1 isoform 43"
                     /note="RAB3-interacting protein 2; rab3-interacting
                     molecule 1; rab-3-interacting protein 2"
                     /calculated_mol_wt=107110
     Region          68..164
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(89..95,110,113,143,147,150..151)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          216..342
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(247,253,308,310,318)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          345..>580
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          792..937
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(849,853..854,856,859,887,889,891,935..936)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..961
                     /gene="RIMS1"
                     /gene_synonym="CORD7; RAB3IP2; RIM; RIM1"
                     /coded_by="NM_001350447.2:231..3116"
                     /note="isoform 43 is encoded by transcript variant 43"
                     /db_xref="GeneID:22999"
                     /db_xref="HGNC:HGNC:17282"
                     /db_xref="MIM:606629"
ORIGIN      
        1 mcapgihvss egweevrsvd seegtiearr avagdldyyw ldpatwhsre tspisshpvt
       61 wqpskegdrl igrvilnkrt tmpkdsgall glkvvggkmt dlgrlgafit kvkkgsladv
      121 vghlragdev lewngkplpg atneevynii lesksepqve iivsrpigdi pripesshpp
      181 lesssssfes qkmerpsisv isptspgalk dapqvlpgql svklwydkvg hqlivnvlqa
      241 tdlparvdgr prnpyvkmyf lpdrsdkskr rtktvkkile pkwnqtfvys hvhrrdfrer
      301 mleitvwdqp rvqeeesefl geilieleta llddephwyk lqthdesslp lpqpspfmpr
      361 rhihgesssk klqrsqrisd sdisdyevdd gigvvppgyr ssareskstt ltvpeqqrtt
      421 hhrsrsvsph rgndqgkprs rlpnvplqrs ldeihptrrs rsptrhhdas rspvdhrtrd
      481 vdsqylseqd rhsrkserss iqkqtrkgta sdaermhrqr sptqsppadt sfssrrgrql
      541 pqvpvrsgsi eqaslvveer trqmkmkvhr fkqttgsgss qeldreqysk ynihkdqyrs
      601 cdnvsakssd sdvsdvsais rtssasrlss tsfmseqser prgrissftp kmqgrrmgts
      661 grsimkstsv sgemytlehn dgsqsdtavg tvgaggkkrr sslsakvvai vsrrsrstsq
      721 lsqtesghkk lkstiqrste tgmaaemrkm vrqpsrestd gsinsysseg nlifpgvrlg
      781 adsqfsdfld glgpaqlvgr qtlatpamgd iqigmedkkg qlevevirar sltqkpgsks
      841 tpapyvkvyl lengaciakk ktriarktld plyqqslvfd espqgkvlqv ivwgdygrmd
      901 hkcfmgvaqi lleeldlssm vigwyklfpp sslvdptltp ltrrasqssl esstgppcir
      961 s
//
LOCUS       NP_001034786             411 aa            linear   PRI 21-NOV-2025
DEFINITION  snRNA-activating protein complex subunit 3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001034786
VERSION     NP_001034786.1
DBSOURCE    REFSEQ: accession NM_001039697.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Sun,J., Li,X., Hou,X., Cao,S., Cao,W., Zhang,Y., Song,J., Wang,M.,
            Wang,H., Yan,X., Li,Z., Roeder,R.G. and Wang,W.
  TITLE     Structural basis of human SNAPc recognizing proximal sequence
            element of snRNA promoter
  JOURNAL   Nat Commun 13 (1), 6871 (2022)
   PUBMED   36369505
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Henry,R.W., Mittal,V., Ma,B., Kobayashi,R. and Hernandez,N.
  TITLE     SNAP19 mediates the assembly of a functional core promoter complex
            (SNAPc) shared by RNA polymerases II and III
  JOURNAL   Genes Dev 12 (17), 2664-2672 (1998)
   PUBMED   9732265
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Henry,R.W., Ma,B., Sadowski,C.L., Kobayashi,R. and Hernandez,N.
  TITLE     Cloning and characterization of SNAP50, a subunit of the
            snRNA-activating protein complex SNAPc
  JOURNAL   EMBO J 15 (24), 7129-7136 (1996)
   PUBMED   9003788
REFERENCE   8  (residues 1 to 411)
  AUTHORS   Bai,L., Wang,Z., Yoon,J.B. and Roeder,R.G.
  TITLE     Cloning and characterization of the beta subunit of human proximal
            sequence element-binding transcription factor and its involvement
            in transcription of small nuclear RNA genes by RNA polymerases II
            and III
  JOURNAL   Mol Cell Biol 16 (10), 5419-5426 (1996)
   PUBMED   8816454
REFERENCE   9  (residues 1 to 411)
  AUTHORS   Henry,R.W., Sadowski,C.L., Kobayashi,R. and Hernandez,N.
  TITLE     A TBP-TAF complex required for transcription of human snRNA genes
            by RNA polymerase II and III
  JOURNAL   Nature 374 (6523), 653-656 (1995)
   PUBMED   7715707
REFERENCE   10 (residues 1 to 411)
  AUTHORS   Bagramian,E.R., Bogdanova,E.A., Krymskaia,M.L. and Sokovykh,S.I.
  TITLE     [Diagnostic importance of determining 17-ketosteroids in
            gynecology]
  JOURNAL   Akush Ginekol (Mosk) (2), 65-67 (1977)
   PUBMED   900378
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL441925.16.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.832476.1, BC108743.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380821.8/ ENSP00000370200.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p22.3"
     Protein         1..411
                     /product="snRNA-activating protein complex subunit 3
                     isoform 1"
                     /note="snRNA-activating protein complex subunit 3; SNAPc
                     subunit 3; PTF subunit beta; SNAPc 50 kDa subunit;
                     PSE-binding factor subunit beta; snRNA-activating protein
                     complex 50 kDa subunit; proximal sequence element-binding
                     transcription factor subunit beta; small nuclear RNA
                     activating complex, polypeptide 3, 50kD; small nuclear RNA
                     activating complex, polypeptide 3, 50kDa"
                     /calculated_mol_wt=46622
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92966.1)"
     Region          63..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92966.1)"
     Region          202..405
                     /region_name="SNAPC3"
                     /note="snRNA-activating protein complex (SNAPc), subunit
                     3; pfam12251"
                     /db_xref="CDD:463506"
     CDS             1..411
                     /gene="SNAPC3"
                     /gene_synonym="PTFbeta; SNAP50"
                     /coded_by="NM_001039697.2:5..1240"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6478.1"
                     /db_xref="GeneID:6619"
                     /db_xref="HGNC:HGNC:11136"
                     /db_xref="MIM:602348"
ORIGIN      
        1 maegsrggpt csgvggrqdp vsgsggcnfp eyelpelntr afhvgafgel wrgrlrgagd
       61 lslreppasa lpgsqaadsd redaavardl dcsleaaael ravcgldklk cledgedpev
      121 ipentdlvtl gvrkrflehr eetitidrac rqetfvyeme shaigkkpen sadmieegel
      181 ilsvnilypv ifhkhkehkp yqtmlvlgsq kltqlrdsir cvsdlqigge fsntpdqape
      241 hiskdlyksa ffyfegtfyn dkrypecrdl srtiiewses hdrgygkfqt armedftfnd
      301 lciklgfpyl ychqgdcehv ivitdirlvh hddcldrtly pllikkhwlw trkcfvckmy
      361 tarwvtnnds fapedpcffc dvcfrmlhyd segnklgefl aypyvdpgtf n
//
LOCUS       NP_001305742             171 aa            linear   PRI 21-NOV-2025
DEFINITION  tetratricopeptide repeat protein 9C isoform a [Homo sapiens].
ACCESSION   NP_001305742 XP_005273987
VERSION     NP_001305742.1
DBSOURCE    REFSEQ: accession NM_001318813.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 171)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   5  (residues 1 to 171)
  AUTHORS   Martins-de-Souza,D., Gattaz,W.F., Schmitt,A., Rewerts,C.,
            Maccarrone,G., Dias-Neto,E. and Turck,C.W.
  TITLE     Prefrontal cortex shotgun proteome analysis reveals altered calcium
            homeostasis and immune system imbalance in schizophrenia
  JOURNAL   Eur Arch Psychiatry Clin Neurosci 259 (3), 151-163 (2009)
   PUBMED   19165527
  REMARK    GeneRIF: Using shotgun mass spectrometry, we found this protein
            differentially expressed in the dorsolateral prefrontal cortex from
            patients with schizophrenia.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC032123.2 and BQ050575.1.
            
            On Jan 14, 2016 this sequence version replaced XP_005273987.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, and 3 all encode the same isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053665.1, SRR18074967.2057262.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..171
                     /product="tetratricopeptide repeat protein 9C isoform a"
                     /note="tetratricopeptide repeat protein 9C; TPR repeat
                     protein 9C"
                     /calculated_mol_wt=19882
     Region          2..>148
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          8..41
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5M4.1)"
     Region          8..36
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(9,12..13,16..17,19,73,76..77,80..81,83..84,109,
                     112..113,116..117,120)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          45..103
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          72..107
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5M4.1)"
     Region          108..141
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5M4.1)"
     Region          108..135
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          142..165
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..171
                     /gene="TTC9C"
                     /coded_by="NM_001318813.2:278..793"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS8033.1"
                     /db_xref="GeneID:283237"
                     /db_xref="HGNC:HGNC:28432"
ORIGIN      
        1 mekrlqeaql ykeegnqryr egkyrdavsr yhrallqlrg ldpslpsplp nlgpqgpalt
       61 peqenilhtt qtdcynnlaa cllqmepvny ervreysqkv lerqpdnaka lyragvaffh
      121 lqdydqarhy llaavnrqpk danvrrylql tqselssyhr kekqlylgmf g
//
LOCUS       NP_001364070            1859 aa            linear   PRI 21-NOV-2025
DEFINITION  Golgi-specific brefeldin A-resistance guanine nucleotide exchange
            factor 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001364070
VERSION     NP_001364070.1
DBSOURCE    REFSEQ: accession NM_001377141.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1859)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1859)
  AUTHORS   Hirano,J., Hayashi,T., Kitamura,K., Nishimura,Y., Shimizu,H.,
            Okamoto,T., Okada,K., Uemura,K., Yeh,M.T., Ono,C., Taguwa,S.,
            Muramatsu,M. and Matsuura,Y.
  TITLE     Enterovirus 3A protein disrupts endoplasmic reticulum homeostasis
            through interaction with GBF1
  JOURNAL   J Virol 98 (7), e0081324 (2024)
   PUBMED   38904364
  REMARK    GeneRIF: Enterovirus 3A protein disrupts endoplasmic reticulum
            homeostasis through interaction with GBF1.
REFERENCE   3  (residues 1 to 1859)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1859)
  AUTHORS   Navare,A.T., Mast,F.D., Olivier,J.P., Bertomeu,T., Neal,M.L.,
            Carpp,L.N., Kaushansky,A., Coulombe-Huntington,J., Tyers,M. and
            Aitchison,J.D.
  TITLE     Viral protein engagement of GBF1 induces host cell vulnerability
            through synthetic lethality
  JOURNAL   J Cell Biol 221 (11) (2022)
   PUBMED   36305789
  REMARK    GeneRIF: Viral protein engagement of GBF1 induces host cell
            vulnerability through synthetic lethality.
REFERENCE   5  (residues 1 to 1859)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1859)
  AUTHORS   Garcia-Mata,R. and Sztul,E.
  TITLE     The membrane-tethering protein p115 interacts with GBF1, an ARF
            guanine-nucleotide-exchange factor
  JOURNAL   EMBO Rep 4 (3), 320-325 (2003)
   PUBMED   12634853
  REMARK    GeneRIF: novel interaction between p115 and Golgi-specific
            brefeldin-A-resistant factor 1 (GBF1)
REFERENCE   7  (residues 1 to 1859)
  AUTHORS   Kawamoto,K., Yoshida,Y., Tamaki,H., Torii,S., Shinotsuka,C.,
            Yamashina,S. and Nakayama,K.
  TITLE     GBF1, a guanine nucleotide exchange factor for ADP-ribosylation
            factors, is localized to the cis-Golgi and involved in membrane
            association of the COPI coat
  JOURNAL   Traffic 3 (7), 483-495 (2002)
   PUBMED   12047556
  REMARK    GeneRIF: detailed subcellular localization to the cis-Golgi
REFERENCE   8  (residues 1 to 1859)
  AUTHORS   Verhoeven,K., Villanova,M., Rossi,A., Malandrini,A., De Jonghe,P.
            and Timmerman,V.
  TITLE     Localization of the gene for the intermediate form of
            Charcot-Marie-Tooth to chromosome 10q24.1-q25.1
  JOURNAL   Am J Hum Genet 69 (4), 889-894 (2001)
   PUBMED   11533914
REFERENCE   9  (residues 1 to 1859)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   10 (residues 1 to 1859)
  AUTHORS   Mansour,S.J., Herbrick,J.A., Scherer,S.W. and Melancon,P.
  TITLE     Human GBF1 is a ubiquitously expressed gene of the sec7 domain
            family mapping to 10q24
  JOURNAL   Genomics 54 (2), 323-327 (1998)
   PUBMED   9828135
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160011.35, AL356420.14 and
            AL121928.13.
            
            Summary: This gene encodes a member of the Sec7 domain family. The
            encoded protein is a guanine nucleotide exchange factor that
            regulates the recruitment of proteins to membranes by mediating GDP
            to GTP exchange. The encoded protein is localized to the Golgi
            apparatus and plays a role in vesicular trafficking by activating
            ADP ribosylation factor 1. The encoded protein has also been
            identified as an important host factor for viral replication.
            Multiple transcript variants have been observed for this gene.
            [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (8), as well as variant 1, encodes
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3098773.1,
                                           SRR1660805.183024.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149178, SAMEA2153733
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1859
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..1859
                     /product="Golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1 isoform 1"
                     /note="golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1; BFA-resistant GEF 1"
                     /calculated_mol_wt=206316
     Region          1..211
                     /region_name="DCB, DCB:DCB domain and DCB:HUS domain
                     interaction. /evidence=ECO:0000250|UniProtKB:Q9R1D7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          215..266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          <429..>1178
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          530..550
                     /region_name="HUS, DCB:HUS domain interaction.
                     /evidence=ECO:0000250|UniProtKB:Q9R1D7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          619..665
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          699..884
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          886..1370
                     /region_name="Phosphatidylinositol-phosphate binding,
                     required for translocation to the leading edge and for
                     ARF1 activation upon GPCR signaling.
                     /evidence=ECO:0000269|PubMed:22573891"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1284..1335
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1316
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1337
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AMPK.
                     /evidence=ECO:0000269|PubMed:18063581; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1350..1370
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1430..1483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1725..1808
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1773
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1784
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          <1794..1857
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1859
                     /gene="GBF1"
                     /gene_synonym="ARF1GEF; CMT2GG; CMTDI2; CMTDIA"
                     /coded_by="NM_001377141.1:360..5939"
                     /note="isoform 1 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS7533.1"
                     /db_xref="GeneID:8729"
                     /db_xref="HGNC:HGNC:4181"
                     /db_xref="MIM:603698"
ORIGIN      
        1 mvdkniyiiq geinivvgai krnarwstht pldeerdpll hsfghlkevl nsitelseie
       61 pnvflrpfle virsedttgp itglaltsvn kflsyalidp thegtaegme nmadavthar
      121 fvgtdpasde vvlmkilqvl rtllltpvga hltnesvcei mqscfricfe mrlsellrks
      181 aehtlvdmvq llftrlpqfk eepknyvgtn mkklkmragg msdsskwkkq krsprpprhm
      241 tkvtpgselp tpngttlssn ltggmpfidv ptpissasse aasavvspst dsglefssqt
      301 tskedltdle qpgspgysta tepgsselgv peqpdlqegt hveksqsasv esipevleec
      361 tspadhsdsa svhdmdyvnp rgvrftqssq kegtalvpyg lpcirelfrf lisltnphdr
      421 hnsevmihmg lhlltvales apvaqcqtll glikdemcrh lfqllsierl nlyaaslrvc
      481 fllfesmreh lkfqmemyik klmeiitven pkmpyemkem aleaivqlwr ipsfvtelyi
      541 nydcdyycsn lfeeltklls knafpvsgql ytthllslda lltvidstea hcqakvlnsl
      601 tqqekketar psceivdgtr easntertas dgkavgmasd ipglhlpggg rlppehgksg
      661 csdleeavds gadkkfarkp prfscllpdp relieiknkk kllitgteqf nqkpkkgiqf
      721 lqekglltip mdntevaqwl renprldkkm igefvsdrkn idllesfvst fsfqglrlde
      781 alrlyleafr lpgeapviqr lleafterwm ncngspfans dacfslayav imlntdqhnh
      841 nvrkqnapmt leefrknlkg vnggkdfeqd iledmyhaik neeivmpeeq tglvrenyvw
      901 nvllhrgatp egiflrvpta sydldlftmt wgptiaalsy vfdksleeti iqkaisgfrk
      961 camisahygl sdvfdnliis lckftalsse sienlpsvfg snpkahiaak tvfhlahrhg
     1021 dilregwkni meamlqlfra qllpkamiev edfvdpngki slqreetpsn rgestvlsfv
     1081 swltlsgpeq ssvrgpsten qeakrvalec ikqcdpekmi teskflqles lqelmkalvs
     1141 vtpdeetyde edaafcleml lrivlenrdr vgcvwqtvrd hlyhlcvqaq dfcflverav
     1201 vgllrlairl lrreeisaqv llslrilllm kpsvlsrvsh qvayglhell ktnaanihsg
     1261 ddwatlftll ecigsgvkpp aalqatarad apdagaqsds elpsyhqndv sldrgytsds
     1321 evytdhgrpg kihrsatdad vvnsgwlvvg kddvdnskpg psrpgpspli nqysltvgld
     1381 lgphdtksll kcveslsfiv rdaahitpdn felcvktlri fveaslnggc ksqekrgksh
     1441 kydskgnrfk kkskegsmlr rprtssqhas rggqsddded egvpasyhtv slqvsqdlld
     1501 lmhtlhtraa siysswaeeq rhletggqki eadsrtlwah cwcpllqgia clccdarrqv
     1561 rmqaltylqr allvhdlqkl dalewescfn kvlfplltkl lenispadvg gmeetrmras
     1621 tllskvflqh lspllslstf aalwltildf mdkymhagss dllseaipes lknmllvmdt
     1681 aeifhsadar gggpsalwei tweridcflp hlrdelfkqt viqdpmpmep qgqkplasah
     1741 ltsaagdtrt pghppppeip selgacdfek pespraasss spgspvassp srlsptpdgp
     1801 pplaqpplil qplasplqvg vppmtlpiil npalieatsp vpllatprpt dpiptsevn
//
LOCUS       NP_001273055             780 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase MARK1 isoform 3 [Homo sapiens].
ACCESSION   NP_001273055 XP_005273192
VERSION     NP_001273055.1
DBSOURCE    REFSEQ: accession NM_001286126.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 780)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 780)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 780)
  AUTHORS   Tang,X., Yang,M., Wang,Z., Wu,X. and Wang,D.
  TITLE     MicroRNA-23a promotes colorectal cancer cell migration and
            proliferation by targeting at MARK1
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 51 (7), 661-668 (2019)
   PUBMED   31281935
  REMARK    GeneRIF: Microtubule affinity regulating kinase 1 (MARK1) is a
            direct target of miR-23a in colorectal cancer (CRC) cells.
REFERENCE   6  (residues 1 to 780)
  AUTHORS   Drewes,G., Ebneth,A., Preuss,U., Mandelkow,E.M. and Mandelkow,E.
  TITLE     MARK, a novel family of protein kinases that phosphorylate
            microtubule-associated proteins and trigger microtubule disruption
  JOURNAL   Cell 89 (2), 297-308 (1997)
   PUBMED   9108484
REFERENCE   7  (residues 1 to 780)
  AUTHORS   Paudel,H.K.
  TITLE     The regulatory Ser262 of microtubule-associated protein tau is
            phosphorylated by phosphorylase kinase
  JOURNAL   J Biol Chem 272 (3), 1777-1785 (1997)
   PUBMED   8999860
REFERENCE   8  (residues 1 to 780)
  AUTHORS   Illenberger,S., Drewes,G., Trinczek,B., Biernat,J., Meyer,H.E.,
            Olmsted,J.B., Mandelkow,E.M. and Mandelkow,E.
  TITLE     Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by
            the protein kinase p110mark. Phosphorylation sites and regulation
            of microtubule dynamics
  JOURNAL   J Biol Chem 271 (18), 10834-10843 (1996)
   PUBMED   8631898
REFERENCE   9  (residues 1 to 780)
  AUTHORS   Drewes,G., Trinczek,B., Illenberger,S., Biernat,J.,
            Schmitt-Ulms,G., Meyer,H.E., Mandelkow,E.M. and Mandelkow,E.
  TITLE     Microtubule-associated protein/microtubule affinity-regulating
            kinase (p110mark). A novel protein kinase that regulates
            tau-microtubule interactions and dynamic instability by
            phosphorylation at the Alzheimer-specific site serine 262
  JOURNAL   J Biol Chem 270 (13), 7679-7688 (1995)
   PUBMED   7706316
REFERENCE   10 (residues 1 to 780)
  AUTHORS   Yang,S.D., Yu,J.S., Shiah,S.G. and Huang,J.J.
  TITLE     Protein kinase FA/glycogen synthase kinase-3 alpha after heparin
            potentiation phosphorylates tau on sites abnormally phosphorylated
            in Alzheimer's disease brain
  JOURNAL   J Neurochem 63 (4), 1416-1425 (1994)
   PUBMED   7931292
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC096640.2, BC068608.1, AK295506.1, AL592406.4 and CA412112.1.
            
            On Oct 30, 2013 this sequence version replaced XP_005273192.1.
            
            Transcript Variant: This variant (3) uses an alternate splice site
            and lacks an exon in the 3' coding region but maintains the reading
            frame, compared to variant 1. This results in a shorter protein
            (isoform 3), compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295506.1, KJ534881.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..780
                     /product="serine/threonine-protein kinase MARK1 isoform 3"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.11.26"
                     /note="serine/threonine-protein kinase MARK1; PAR1 homolog
                     c; MAP/microtubule affinity-regulating kinase 1"
                     /calculated_mol_wt=87325
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0L2.2)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9P0L2.2)"
     Region          59..311
                     /region_name="STKc_MARK"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     MAP/microtubule affinity-regulating kinases; cd14072"
                     /db_xref="CDD:270974"
     Site            order(66..70,74,87,89,120,136..139,143,145..146,148,
                     181..182,184,186..187,189,199..200,203,216..221,223,
                     253..256,258)
                     /site_type="active"
                     /db_xref="CDD:270974"
     Site            order(66..69,74,87,89,120,136..139,143,186..187,189,
                     199..200)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270974"
     Site            order(70,143,145,181..182,184,186,203,217..221,223)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270974"
     Site            199..221
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270974"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17573348; propagated from
                     UniProtKB/Swiss-Prot (Q9P0L2.2)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by LKB1 and TAOK1.
                     /evidence=ECO:0000269|PubMed:14976552; propagated from
                     UniProtKB/Swiss-Prot (Q9P0L2.2)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta.
                     /evidence=ECO:0000250|UniProtKB:O08678; propagated from
                     UniProtKB/Swiss-Prot (Q9P0L2.2)"
     Region          331..371
                     /region_name="UBA_MARK1"
                     /note="UBA domain found in serine/threonine-protein kinase
                     MARK1 and similar proteins; cd14405"
                     /db_xref="CDD:270588"
     Region          377..495
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0L2.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VHJ5; propagated from
                     UniProtKB/Swiss-Prot (Q9P0L2.2)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VHJ5; propagated from
                     UniProtKB/Swiss-Prot (Q9P0L2.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VHJ5; propagated from
                     UniProtKB/Swiss-Prot (Q9P0L2.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9P0L2.2)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VHJ5; propagated from
                     UniProtKB/Swiss-Prot (Q9P0L2.2)"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08678; propagated from
                     UniProtKB/Swiss-Prot (Q9P0L2.2)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VHJ5; propagated from
                     UniProtKB/Swiss-Prot (Q9P0L2.2)"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P0L2.2)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC/PRKCZ.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9P0L2.2)"
     Region          681..778
                     /region_name="MARK1-3_C"
                     /note="C-terminal, kinase associated domain 1 (KA1), a
                     phospholipid binding domain, of microtubule
                     affinity-regulating kinases 1-3; cd12196"
                     /db_xref="CDD:213381"
     Site            order(683,686,756,758..759)
                     /site_type="other"
                     /note="putative phospholipid binding site [chemical
                     binding]"
                     /db_xref="CDD:213381"
     CDS             1..780
                     /gene="MARK1"
                     /gene_synonym="MARK; Par-1c; Par1c"
                     /coded_by="NM_001286126.2:688..3030"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS73034.1"
                     /db_xref="GeneID:4139"
                     /db_xref="HGNC:HGNC:6896"
                     /db_xref="MIM:606511"
ORIGIN      
        1 msartplptv nerdtenhts vdgytephiq ptksssrqni prcrnsitsa tdeqphigny
       61 rlqktigkgn fakvklarhv ltgrevavki idktqlnpts lqklfrevri mkilnhpniv
      121 klfevietek tlylvmeyas ggevfdylva hgrmkekear akfrqivsav qychqkyivh
      181 rdlkaenlll dgdmnikiad fgfsneftvg nkldtfcgsp pyaapelfqg kkydgpevdv
      241 wslgvilytl vsgslpfdgq nlkelrervl rgkyripfym stdcenllkk llvlnpikrg
      301 sleqimkdrw mnvgheeeel kpytepdpdf ndtkridimv tmgfardein dalinqkyde
      361 vmatyillgr kppefegges lssgnlcqrs rpssdlnnst lqspahlkvq rsisanqkqr
      421 rfsdhagpsi ppavsytkrp qansveseqk eewdkdvark lgsttvgsks emtasplvgp
      481 erkksstips nnvysggsma rrntyvcert tdryvalqng kdssltemsv ssissagssv
      541 asavpsarpr hqksmstsgh pikvtlptik dgseayrpgt tqrvpaasps ahsistatpd
      601 rtrfprgsss rstfhgeqlr errsvayngp paspshetga faharrgtst giiskitskf
      661 vrrstsgepk erdkeegkds kprslrftws mkttssmdpn dmmreirkvl danncdyeqk
      721 erfllfcvhg darqdslvqw emevcklprl slngvrfkri sgtsiafkni askianelkl
//
LOCUS       NP_001248347             401 aa            linear   PRI 21-NOV-2025
DEFINITION  translation initiation factor eIF2B subunit gamma isoform 3 [Homo
            sapiens].
ACCESSION   NP_001248347
VERSION     NP_001248347.1
DBSOURCE    REFSEQ: accession NM_001261418.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Lee,Y.R., Kim,S.H., Ben-Mahmoud,A., Kim,O.H., Choi,T.I., Lee,K.H.,
            Ku,B., Eum,J., Kee,Y., Lee,S., Cha,J., Won,D., Lee,S.T., Choi,J.R.,
            Lee,J.S., Kim,H.D., Kim,H.G., Bonkowsky,J.L., Kang,H.C. and
            Kim,C.H.
  TITLE     Eif2b3 mutants recapitulate phenotypes of vanishing white matter
            disease and validate novel disease alleles in zebrafish
  JOURNAL   Hum Mol Genet 30 (5), 331-342 (2021)
   PUBMED   33517449
  REMARK    GeneRIF: Eif2b3 mutants recapitulate phenotypes of vanishing white
            matter disease and validate novel disease alleles in zebrafish.
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Zyryanova,A.F., Weis,F., Faille,A., Alard,A.A.,
            Crespillo-Casado,A., Sekine,Y., Harding,H.P., Allen,F., Parts,L.,
            Fromont,C., Fischer,P.M., Warren,A.J. and Ron,D.
  TITLE     Binding of ISRIB reveals a regulatory site in the nucleotide
            exchange factor eIF2B
  JOURNAL   Science 359 (6383), 1533-1536 (2018)
   PUBMED   29599245
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Tsai,J.C., Miller-Vedam,L.E., Anand,A.A., Jaishankar,P.,
            Nguyen,H.C., Renslo,A.R., Frost,A. and Walter,P.
  TITLE     Structure of the nucleotide exchange factor eIF2B reveals mechanism
            of memory-enhancing molecule
  JOURNAL   Science 359 (6383) (2018)
   PUBMED   29599213
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Kruger,M., Beger,C., Li,Q.X., Welch,P.J., Tritz,R., Leavitt,M.,
            Barber,J.R. and Wong-Staal,F.
  TITLE     Identification of eIF2Bgamma and eIF2gamma as cofactors of
            hepatitis C virus internal ribosome entry site-mediated translation
            using a functional genomics approach
  JOURNAL   Proc Natl Acad Sci U S A 97 (15), 8566-8571 (2000)
   PUBMED   10900014
REFERENCE   6  (residues 1 to 401)
  AUTHORS   Anthony,T.G., Fabian,J.R., Kimball,S.R. and Jefferson,L.S.
  TITLE     Identification of domains within the epsilon-subunit of the
            translation initiation factor eIF2B that are necessary for guanine
            nucleotide exchange activity and eIF2B holoprotein formation
  JOURNAL   Biochim Biophys Acta 1492 (1), 56-62 (2000)
   PUBMED   10858531
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Gomez,E. and Pavitt,G.D.
  TITLE     Identification of domains and residues within the epsilon subunit
            of eukaryotic translation initiation factor 2B (eIF2Bepsilon)
            required for guanine nucleotide exchange reveals a novel activation
            function promoted by eIF2B complex formation
  JOURNAL   Mol Cell Biol 20 (11), 3965-3976 (2000)
   PUBMED   10805739
REFERENCE   8  (residues 1 to 401)
  AUTHORS   Welsh,G.I., Miyamoto,S., Price,N.T., Safer,B. and Proud,C.G.
  TITLE     T-cell activation leads to rapid stimulation of translation
            initiation factor eIF2B and inactivation of glycogen synthase
            kinase-3
  JOURNAL   J Biol Chem 271 (19), 11410-11413 (1996)
   PUBMED   8626696
REFERENCE   9  (residues 1 to 401)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   10 (residues 1 to 401)
  AUTHORS   van der Knaap,M.S., Fogli,A., Boespflug-Tanguy,O., Abbink,T.E.M.
            and Schiffmann,R.
  TITLE     Childhood Ataxia with Central Nervous System Hypomyelination /
            Vanishing White Matter
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301435
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136380.22 and BC018728.1.
            
            Summary: The protein encoded by this gene is one of the subunits of
            initiation factor eIF2B, which catalyzes the exchange of eukaryotic
            initiation factor 2-bound GDP for GTP. It has also been found to
            function as a cofactor of hepatitis C virus internal ribosome entry
            site-mediated translation. Mutations in this gene have been
            associated with leukodystrophy with vanishing white matter.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Oct
            2009].
            
            Transcript Variant: This variant (3) lacks the penultimate exon
            compared to variant 1. The resulting protein (isoform 3) is shorter
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC018728.1, SRR14038193.712718.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..401
                     /product="translation initiation factor eIF2B subunit
                     gamma isoform 3"
                     /note="translation initiation factor eIF-2B subunit gamma;
                     eIF-2B GDP-GTP exchange factor subunit gamma; eukaryotic
                     translation initiation factor 2B, subunit 3 gamma, 58kDa;
                     eIF2B GDP-GTP exchange factor subunit gamma; translation
                     initiation factor eIF2B subunit gamma"
                     /calculated_mol_wt=44672
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.7,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9NR50.1)"
     Region          3..212
                     /region_name="eIF-2B_gamma_N"
                     /note="The N-terminal domain of gamma subunit of the
                     eIF-2B is a subfamily of glycosyltransferase 2; cd04198"
                     /db_xref="CDD:133041"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NR50.1)"
     Region          357..>401
                     /region_name="LbetaH"
                     /note="Left-handed parallel beta-Helix (LbetaH or LbH)
                     domain: The alignment contains 5 turns, each containing
                     three imperfect tandem repeats of a hexapeptide repeat
                     motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing
                     hexapeptide repeats are often enzymes...; cl00160"
                     /db_xref="CDD:469633"
     CDS             1..401
                     /gene="EIF2B3"
                     /gene_synonym="EIF-2B; EIF2Bgamma; VWM3"
                     /coded_by="NM_001261418.2:113..1318"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS72775.1"
                     /db_xref="GeneID:8891"
                     /db_xref="HGNC:HGNC:3259"
                     /db_xref="MIM:606273"
ORIGIN      
        1 mefqavvmav gggsrmtdlt ssipkpllpv gnkpliwypl nllervgfee vivvttrdvq
       61 kalcaefkmk mkpdivcipd dadmgtadsl ryiypklktd vlvlscdlit dvalhevvdl
      121 fraydaslam lmrkgqdsie pvpgqkgkkk aveqrdfigv dstgkrllfm aneadldeel
      181 vikgsilqkh prirfhtglv dahlyclkky ivdflmengs itsirselip ylvrkqfssa
      241 ssqqgqeeke edlkkkelks ldiysfikea ntlnlapyda cwnacrgdrw edlsrsqvrc
      301 yvhimkeglc srvstlglym eanrqvpkll salcpeeppv hssaqivskh lvgvdsligp
      361 etqigekssi krsvigsscl ikdrvtitnc llmnsvtvee g
//
LOCUS       NP_001229558             148 aa            linear   PRI 21-NOV-2025
DEFINITION  glucose-fructose oxidoreductase domain-containing protein 1 isoform
            3 precursor [Homo sapiens].
ACCESSION   NP_001229558
VERSION     NP_001229558.1
DBSOURCE    REFSEQ: accession NM_001242629.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Shi,J., Guo,X., Liu,C., Wang,Y., Chen,X., Wu,G., Ding,J. and
            Zhang,T.
  TITLE     Molecular insight into the potential functional role of
            pseudoenzyme GFOD1 via interaction with NKIRAS2
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 56 (9), 1256-1266 (2024)
   PUBMED   38946427
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 148)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 148)
  AUTHORS   Liu,Z., Ma,C., Gu,J. and Yu,M.
  TITLE     Potential biomarkers of acute myocardial infarction based on
            weighted gene co-expression network analysis
  JOURNAL   Biomed Eng Online 18 (1), 9 (2019)
   PUBMED   30683112
  REMARK    GeneRIF: three overlapping genes (FGFBP2, GFOD1 and MLC1) between
            two modules could potentially have a role in acute myocardial
            infarction and have diagnostic potential
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 148)
  AUTHORS   Wu,X.R., Chen,Y.H., Chen,W., Kong,W., Huang,J.W., Zhang,J., Xue,W.,
            Liu,D.M. and Huang,Y.R.
  TITLE     GFOD1 and peejar are promising markers for clear-cell renal cell
            carcinoma disease progression
  JOURNAL   Oncotarget 7 (25), 38004-38009 (2016)
   PUBMED   27191742
  REMARK    GeneRIF: Authors found the expression of peejar was positively
            correlated with the expression of GFOD1 in ccRCC tissue, with
            Pearson correlation coefficiency reaching 0.939 (p < 0.001). GFOD1
            and peejar were novel genes correlated with ccRCC disease
            progression and patients' poor prognosis.
REFERENCE   8  (residues 1 to 148)
  AUTHORS   Lasky-Su,J., Neale,B.M., Franke,B., Anney,R.J., Zhou,K.,
            Maller,J.B., Vasquez,A.A., Chen,W., Asherson,P., Buitelaar,J.,
            Banaschewski,T., Ebstein,R., Gill,M., Miranda,A., Mulas,F.,
            Oades,R.D., Roeyers,H., Rothenberger,A., Sergeant,J.,
            Sonuga-Barke,E., Steinhausen,H.C., Taylor,E., Daly,M., Laird,N.,
            Lange,C. and Faraone,S.V.
  TITLE     Genome-wide association scan of quantitative traits for attention
            deficit hyperactivity disorder identifies novel associations and
            confirms candidate gene associations
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 147B (8), 1345-1354 (2008)
   PUBMED   18821565
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL583828.4.
            
            Transcript Variant: This variant (4) has an alternate 3' exon,
            compared to variant 1. The resulting isoform (3) has a shorter and
            distinct C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.656714.1,
                                           SRR1660805.78396.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.1-p23"
     Protein         1..148
                     /product="glucose-fructose oxidoreductase
                     domain-containing protein 1 isoform 3 precursor"
                     /note="glucose-fructose oxidoreductase domain-containing
                     protein 1; glucose-fructose oxidoreductase domain
                     containing 1; gfo/Idh/MocA-like oxidoreductase
                     domain-containing protein 1"
                     /calculated_mol_wt=14197
     sig_peptide     1..21
                     /calculated_mol_wt=2155
     Region          4..>85
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
     mat_peptide     22..148
                     /product="glucose-fructose oxidoreductase
                     domain-containing protein 1 isoform 3"
                     /calculated_mol_wt=14197
     CDS             1..148
                     /gene="GFOD1"
                     /gene_synonym="ADG-90; C6orf114"
                     /coded_by="NM_001242629.2:711..1157"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS64351.1"
                     /db_xref="GeneID:54438"
                     /db_xref="HGNC:HGNC:21096"
                     /db_xref="MIM:619932"
ORIGIN      
        1 mlpgvgvfgt sltarviipl lkdegfavka lwgrtqeeae elakemsvpf ytsridevll
       61 hqdvdlvcin lpppltrqia vktlepghqr kkisrqkntg ekkmprgsvq lsfcslqhph
      121 mghlftphda algesqgtgf kplgmqpv
//
LOCUS       NP_001336008             795 aa            linear   PRI 21-NOV-2025
DEFINITION  TBC1 domain family member 5 isoform b [Homo sapiens].
ACCESSION   NP_001336008 XP_016863048
VERSION     NP_001336008.1
DBSOURCE    REFSEQ: accession NM_001349079.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   3  (residues 1 to 795)
  AUTHORS   Tu,Y.X.I., Sydor,A.M., Coyaud,E., Laurent,E.M.N., Dyer,D.,
            Mellouk,N., St-Germain,J., Vernon,R.M., Forman-Kay,J.D., Li,T.,
            Hua,R., Zhao,K., Ridgway,N.D., Kim,P.K., Raught,B. and Brumell,J.H.
  TITLE     Global Proximity Interactome of the Human Macroautophagy Pathway
  JOURNAL   Autophagy 18 (5), 1174-1186 (2022)
   PUBMED   34524948
REFERENCE   4  (residues 1 to 795)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 795)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 795)
  AUTHORS   Seaman,M.N., Harbour,M.E., Tattersall,D., Read,E. and Bright,N.
  TITLE     Membrane recruitment of the cargo-selective retromer subcomplex is
            catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP
            TBC1D5
  JOURNAL   J Cell Sci 122 (Pt 14), 2371-2382 (2009)
   PUBMED   19531583
  REMARK    GeneRIF: Membrane recruitment of the cargo-selective retromer
            subcomplex VPS35/29/26 is catalysed by the small GTPase Rab7 and
            inhibited by the Rab-GAP TBC1D5.
REFERENCE   7  (residues 1 to 795)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
REFERENCE   8  (residues 1 to 795)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   9  (residues 1 to 795)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 795)
  AUTHORS   Brill,L.M., Salomon,A.R., Ficarro,S.B., Mukherji,M.,
            Stettler-Gill,M. and Peters,E.C.
  TITLE     Robust phosphoproteomic profiling of tyrosine phosphorylation sites
            from human T cells using immobilized metal affinity chromatography
            and tandem mass spectrometry
  JOURNAL   Anal Chem 76 (10), 2763-2772 (2004)
   PUBMED   15144186
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104451.2, AC144531.2, AC090960.3 and AC090644.2.
            
            On Mar 3, 2017 this sequence version replaced XP_016863048.1.
            
            Transcript Variant: This variant (9), as well as variants 2, 6, 7,
            8, and 10, encodes isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3009163.1,
                                           SRR18074969.417600.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..795
                     /product="TBC1 domain family member 5 isoform b"
                     /calculated_mol_wt=88874
     Region          1..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92609.1)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Region          56..64
                     /region_name="Required for interaction with retromer,
                     involved in interaction with ATG8 family proteins.
                     /evidence=ECO:0000269|PubMed:22354992"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92609.1)"
     Region          57..62
                     /region_name="LIR 1.
                     /evidence=ECO:0000305|PubMed:22354992,
                     ECO:0000305|PubMed:23908376"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92609.1)"
     Region          79..381
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Site            169
                     /site_type="other"
                     /note="Arginine finger.
                     /evidence=ECO:0000250|UniProtKB:Q96BZ9; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            204
                     /site_type="other"
                     /note="Glutamine finger.
                     /evidence=ECO:0000250|UniProtKB:Q96BZ9; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Region          475..564
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92609.1)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q92609.1)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XQ2; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Region          674..795
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92609.1)"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Region          785..789
                     /region_name="LIR 2.
                     /evidence=ECO:0000305|PubMed:22354992,
                     ECO:0000305|PubMed:23908376"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92609.1)"
     Region          786..791
                     /region_name="Required for interaction with ATG8 family
                     proteins. /evidence=ECO:0000269|PubMed:22354992"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92609.1)"
     Site            791
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     CDS             1..795
                     /gene="TBC1D5"
                     /coded_by="NM_001349079.2:457..2844"
                     /note="isoform b is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS33714.1"
                     /db_xref="GeneID:9779"
                     /db_xref="HGNC:HGNC:19166"
                     /db_xref="MIM:615740"
ORIGIN      
        1 myhslsetrh plqpeeqevg idplssysnk sggdsnkngr rtsstldseg tfnsyrkewe
       61 elfvnnnyla tirqkgingq lrssrfrsic wklflcvlpq dksqwisrie elrawysnik
      121 eihitnprkv vgqqdlminn plsqdegslw nkffqdkelr smieqdvkrt fpemqffqqe
      181 nvrkiltdvl fcyareneql lykqgmhell apivfvlhcd hqaflhases aqpseemktv
      241 lnpeylehda yavfsqlmet aepwfstfeh dgqkgketlm tpipfarpqd lgptiaivtk
      301 vnqiqdhllk khdielymhl nrleiapqiy glrwvrllfg refplqdllv vwdalfadgl
      361 slglvdyifv amllyirdal issnyqtclg llmhypfigd vhslilkalf lrdpkrnprp
      421 vtyqfhpnld yykargadlm nksrtnakga plninkvsns linfgrklis pamapgsagg
      481 pvpggnssss ssvviptrts aeapshhlqq qqqqqrlmks esmpvqlnkg lssknisssp
      541 sveslpggre ftgsppssat kkdsffsnis rsrshsktmg rkeseeelea qisflqgqln
      601 dldamckyca kvmdthlvni qdvilqenle kedqilvsla glkqikdilk gslrfnqsql
      661 eaeeneqiti adnhycssgq gqgrgqgqsv qmsgaikqas setpgctdrg nsddfilisk
      721 dddgssargs fsgqaqplrt lrstsgksqa pvcsplvfsd plmgpasass snpssspddd
      781 sskdsgftiv spldi
//
LOCUS       NP_001382240            2256 aa            linear   PRI 21-NOV-2025
DEFINITION  myomegalin isoform 30 [Homo sapiens].
ACCESSION   NP_001382240
VERSION     NP_001382240.1
DBSOURCE    REFSEQ: accession NM_001395311.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2256)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2256)
  AUTHORS   Pan,R., Dai,J., Liang,W., Wang,H., Ye,L., Ye,S., Lin,Z., Huang,S.,
            Xiong,Y., Zhang,L., Lu,L., Wang,O., Shen,X., Liao,W. and Lu,X.
  TITLE     PDE4DIP contributes to colorectal cancer growth and chemoresistance
            through modulation of the NF1/RAS signaling axis
  JOURNAL   Cell Death Dis 14 (6), 373 (2023)
   PUBMED   37355626
  REMARK    GeneRIF: PDE4DIP contributes to colorectal cancer growth and
            chemoresistance through modulation of the NF1/RAS signaling axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2256)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   4  (residues 1 to 2256)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 2256)
  AUTHORS   Abou Ziki,M.D., Bhat,N., Neogi,A., Driscoll,T.P., Ugwu,N., Liu,Y.,
            Smith,E., Abboud,J.M., Chouairi,S., Schwartz,M.A., Akar,J.G. and
            Mani,A.
  TITLE     Epistatic interaction of PDE4DIP and DES mutations in familial
            atrial fibrillation with slow conduction
  JOURNAL   Hum Mutat 42 (10), 1279-1293 (2021)
   PUBMED   34289528
  REMARK    GeneRIF: Epistatic interaction of PDE4DIP and DES mutations in
            familial atrial fibrillation with slow conduction.
REFERENCE   6  (residues 1 to 2256)
  AUTHORS   Shimada,H., Kuboshima,M., Shiratori,T., Nabeya,Y., Takeuchi,A.,
            Takagi,H., Nomura,F., Takiguchi,M., Ochiai,T. and Hiwasa,T.
  TITLE     Serum anti-myomegalin antibodies in patients with esophageal
            squamous cell carcinoma
  JOURNAL   Int J Oncol 30 (1), 97-103 (2007)
   PUBMED   17143517
  REMARK    GeneRIF: MMGL-antibody is significantly with a favorable prognosis.
            Consequently, MMGL-anatibodies may be a useful tumor marker to
            diagnose and establish a prognosis in patients with esophageal
            squamous cell carcinoma.
REFERENCE   7  (residues 1 to 2256)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 2256)
  AUTHORS   Soejima,H., Kawamoto,S., Akai,J., Miyoshi,O., Arai,Y., Morohka,T.,
            Matsuo,S., Niikawa,N., Kimura,A., Okubo,K. and Mukai,T.
  TITLE     Isolation of novel heart-specific genes using the BodyMap database
  JOURNAL   Genomics 74 (1), 115-120 (2001)
   PUBMED   11374908
REFERENCE   9  (residues 1 to 2256)
  AUTHORS   Verde,I., Pahlke,G., Salanova,M., Zhang,G., Wang,S., Coletti,D.,
            Onuffer,J., Jin,S.L. and Conti,M.
  TITLE     Myomegalin is a novel protein of the golgi/centrosome that
            interacts with a cyclic nucleotide phosphodiesterase
  JOURNAL   J Biol Chem 276 (14), 11189-11198 (2001)
   PUBMED   11134006
REFERENCE   10 (residues 1 to 2256)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC245389.1, AC239802.3 and
            AC239804.2.
            
            Summary: The protein encoded by this gene serves to anchor
            phosphodiesterase 4D to the Golgi/centrosome region of the cell.
            Defects in this gene may be a cause of myeloproliferative disorder
            (MBD) associated with eosinophilia. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..2256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     Protein         1..2256
                     /product="myomegalin isoform 30"
                     /note="myomegalin; cardiomyopathy-associated protein 2"
                     /calculated_mol_wt=256036
     Region          69..745
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          72..139
                     /region_name="Cnn_1N"
                     /note="Centrosomin N-terminal motif 1; pfam07989"
                     /db_xref="CDD:462333"
     Region          419..1232
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1508..1577
                     /region_name="Olduvai"
                     /note="Olduvai domain; pfam06758"
                     /db_xref="CDD:429104"
     Region          <1735..>1912
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..2256
                     /gene="PDE4DIP"
                     /gene_synonym="CMYA2; MMGL"
                     /coded_by="NM_001395311.1:267..7037"
                     /note="isoform 30 is encoded by transcript variant 30"
                     /db_xref="GeneID:9659"
                     /db_xref="HGNC:HGNC:15580"
                     /db_xref="MIM:608117"
ORIGIN      
        1 meqtwtrdyf aeddgemvpr tshtaaflsd tkdrgppvqs qiwrsgekvp fvqtyslraf
       61 ekppqvqtqa lrdfekhlnd lkkenfslkl riyfleermq qkyeasredi ykrnielkve
      121 veslkrelqd kkqhldktwa dvenlnsqne aelrrqfeer qqetehvyel lenkiqllqe
      181 esrlakneaa rmaalveaek ecnlelsekl kgvtknwedv pgdqvkpdqy tealaqrdkr
      241 ieelnqslaa qerlveqlsr ekqqllhlle eptsmevqpm teellkqqkl nshettitqq
      301 svsdshlael qekiqqteat nkilqeklne msyelkcaqe ssqkqdgtiq nlketlksre
      361 reteelyqvi egqndtmakl remlhqsqlg qlhssegtsp aqqqvalldl qsalfcsqle
      421 iqklqrvvrq kerqladakq cvqfveaaah eseqqkeasw khnqelrkal qqlqeelqnk
      481 sqqlraweae kyneirtqeq niqhlnhsls hkeqllqefr ellqyrdnsd ktleanemll
      541 eklrqrihdk avaleraide kfsaleekek elrqlrlavr erdhdlerlr dvlssneatm
      601 qsmesllrak gleveqlstt cqnlqwlkee metkfsrwqk eqesiiqqlq tslhdrnkev
      661 edlsatllck lgpgqseiae elcqrlqrke rmlqdllsdr nkqvleheme iqgllqsvst
      721 reqesqaaae klvqalmern selqalrqyl ggrdslmsqa pisnqqaevt ptgrlgkqtd
      781 qgsmqipsrd dstsltaked vsiprstlgd ldtvagleke lsnakeelel makkeresqm
      841 elsalqsmma vqeeelqvqa admesltrni qikedlikdl qmqlvdpedi pamerltqev
      901 lllrekvasv esqgqeisgn rrqqlllmle glvdersrln ealqaerqly sslvkfhahp
      961 esserdrtlq velegaqvlr srleevlgrs lerlnrletl aaiggaaagd dtedtsteft
     1021 dsieeeaahh shqqlvkval ekslatvetq npsfsppspm ggdsnrclqe emlhlraefh
     1081 qhleekrkae eelkelkaqi eeagfssvsh irntmlslcl enaelkeqmg eamsdgweie
     1141 edkekgeldn qsqprdpgpq safslpgstq hlrsqlsqck qryqdlqekl llseatvfaq
     1201 anelekyrvm ltgeslvkqd skqiqvdlqd lgyetcgrse neaereetts peceehnslk
     1261 emvlmeglcs eqgrrgstla ssserkplen qlgkqeefrv ygksenilvl rkdikdlkaq
     1321 lqnankviqn lksrvrslsv tsdysssler prklravgtl egssphsvpd edegwlsdgt
     1381 gafyspglqa kkdlesliqr vsqleaqlpk ngleeklaee lrsaswpgky dsliqdqare
     1441 lsylrqkire grgicylitr hakdtvksfe dllrsndidy ylgqsfreql aqgsqlterl
     1501 tsklstkdhk sekdqaglep lalrlsrelq ekekvievlq akldarsltp ssshalsdsh
     1561 rspsstsfls deleacsdmd ivseythyee kkaspshsds ihhsshsavl sskpsstsas
     1621 qgakaesnsn pislptpqnt pkeanqahsg astvppasta tllsndlead ssyylnsaqp
     1681 hspprgtiel grilepgylg ssgkwdvmrp qkgsvsgdls sgssvyqlns kptgadllee
     1741 hlgeirnlrq rleesicind rlreqlehrl tstargrgst snfysqgles ipqlcnenrv
     1801 lrednrrlqa qlshvsrehs qeteslreal lssrshlqel ekelehqkve rqqlledlre
     1861 kqqevlhfre erlslqends rlqhklvllq qqceekqqlf eslqselqiy ealygnskkg
     1921 lkaysldach qiplssdlsh lvaevralrg qleqsiqgnn clrlqlqqql esgagkasls
     1981 pssinqnfpa stdpgnkqll lqdsavsppv rdvgmnspal vfpssasstp gsetpiinra
     2041 nglgldtspv mktppklegd atdgsfankh grhvighidd ysalrqqiae gkllvkkivs
     2101 lvrsacsfpg leaqgtevlg skgihelrss tsalhhalee saslltmfwr aalpsthipv
     2161 lpgkvgeste rellelrtkv skqerllqst tehlknanqq kesmeqfivs qltrthdvlk
     2221 kartnleepc kkrshqkslk qqerwacppf vqlpic
//
LOCUS       NP_001362819             486 aa            linear   PRI 21-NOV-2025
DEFINITION  F-box/WD repeat-containing protein 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001362819 XP_011516820
VERSION     NP_001362819.1
DBSOURCE    REFSEQ: accession NM_001375890.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Barik,G.K., Sahay,O., Mukhopadhyay,A., Manne,R.K., Islam,S.,
            Roy,A., Nath,S. and Santra,M.K.
  TITLE     FBXW2 suppresses breast tumorigenesis by targeting AKT-Moesin-SKP2
            axis
  JOURNAL   Cell Death Dis 14 (9), 623 (2023)
   PUBMED   37736741
  REMARK    GeneRIF: FBXW2 suppresses breast tumorigenesis by targeting
            AKT-Moesin-SKP2 axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Zhou,T., Chen,T., Lai,B., Zhang,W., Luo,X., Xia,D., Fu,W. and Xu,J.
  TITLE     FBXW2 inhibits prostate cancer proliferation and metastasis via
            promoting EGFR ubiquitylation and degradation
  JOURNAL   Cell Mol Life Sci 79 (5), 268 (2022)
   PUBMED   35499593
  REMARK    GeneRIF: FBXW2 inhibits prostate cancer proliferation and
            metastasis via promoting EGFR ubiquitylation and degradation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Han,S., Wang,R., Zhang,Y., Li,X., Gan,Y., Gao,F., Rong,P., Wang,W.
            and Li,W.
  TITLE     The role of ubiquitination and deubiquitination in tumor invasion
            and metastasis
  JOURNAL   Int J Biol Sci 18 (6), 2292-2303 (2022)
   PUBMED   35414786
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 486)
  AUTHORS   Chiaur,D.S., Murthy,S., Cenciarelli,C., Parks,W., Loda,M.,
            Inghirami,G., Demetrick,D. and Pagano,M.
  TITLE     Five human genes encoding F-box proteins: chromosome mapping and
            analysis in human tumors
  JOURNAL   Cytogenet Cell Genet 88 (3-4), 255-258 (2000)
   PUBMED   10828603
REFERENCE   7  (residues 1 to 486)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   8  (residues 1 to 486)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
REFERENCE   9  (residues 1 to 486)
  AUTHORS   Patton,E.E., Willems,A.R. and Tyers,M.
  TITLE     Combinatorial control in ubiquitin-dependent proteolysis: don't Skp
            the F-box hypothesis
  JOURNAL   Trends Genet 14 (6), 236-243 (1998)
   PUBMED   9635407
  REMARK    Review article
REFERENCE   10 (residues 1 to 486)
  AUTHORS   Schoenmakers,E.F., Wanschura,S., Mols,R., Bullerdiek,J., Van den
            Berghe,H. and Van de Ven,W.J.
  TITLE     Recurrent rearrangements in the high mobility group protein gene,
            HMGI-C, in benign mesenchymal tumours
  JOURNAL   Nat Genet 10 (4), 436-444 (1995)
   PUBMED   7670494
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL161911.17 and AL138836.15.
            
            On Nov 5, 2019 this sequence version replaced XP_011516820.1.
            
            Summary: F-box proteins are an expanding family of eukaryotic
            proteins characterized by an approximately 40 amino acid motif, the
            F box. Some F-box proteins have been shown to be critical for the
            ubiquitin-mediated degradation of cellular regulatory proteins. In
            fact, F-box proteins are one of the four subunits of ubiquitin
            protein ligases, called SCFs. SCF ligases bring ubiquitin
            conjugating enzymes to substrates that are specifically recruited
            by the different F-box proteins. Mammalian F-box proteins are
            classified into three groups based on the presence of either WD-40
            repeats, leucine-rich repeats, or the presence or absence of other
            protein-protein interacting domains. This gene encodes the second
            identified member of the F-box gene family and contains multiple
            WD-40 repeats. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2057664.1,
                                           SRR14038192.2189131.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.2"
     Protein         1..486
                     /product="F-box/WD repeat-containing protein 2 isoform 3"
                     /note="F-box and WD-40 domain protein 2; F-box/WD
                     repeat-containing protein 2; F-box and WD-40
                     domain-containing protein 2"
                     /calculated_mol_wt=55097
     Region          87..126
                     /region_name="F-box_FBXW2"
                     /note="F-box domain found in F-box/WD repeat-containing
                     protein 2 (FBXW2) and similar proteins; cd22131"
                     /db_xref="CDD:438903"
     Site            order(92,96,99..100,103..104,108,110..111,115..117,119)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438903"
     Region          172..479
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Site            order(179,195,199,205..206,218..219,233,237,243..244,
                     256..257,274,279,285..286,299,326,329,336..337,352..353,
                     372,376,382..383,394,411,416,422..423,450..451,469,474)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          183..217
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          220..255
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          261..297
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          313..351
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          359..394
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          409..449
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          455..477
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..486
                     /gene="FBXW2"
                     /gene_synonym="FBW2; Fwd2; Md6"
                     /coded_by="NM_001375890.1:359..1819"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:26190"
                     /db_xref="HGNC:HGNC:13608"
                     /db_xref="MIM:609071"
ORIGIN      
        1 mkcdevvyev qsailrhncg yamktgkffh nlmerkdfet wldnisvtfl sltdlqknet
       61 ldhlislsga vqlrhlsnnl etllkrdflk llplelsfyl lkwldpqtll tcclvskqwn
      121 kvisactevw qtacknlgwq iddsvqdalh wkkvylkail rmkqledhea fetsslighs
      181 arvyalyykd gllctgsddl saklwdvstg qcvygiqtht caavkfdeqk lvtgsfdntv
      241 acwewssgar tqhfrghtga vfsvdyndel dilvsgsadf tvkvwalsag tclntltght
      301 ewvtkvvlqk ckvksllhsp gdyillsadk yeikiwpigr einckclktl svsedrsicl
      361 qprlhfdgky ivcssalgly qwdfasydil rviktpeian lallgfgdif allfdnryly
      421 imdlrtesli srwplpeyrk skrgssflag easwlngldg hndtglvfat smpdhsihlv
      481 lwkehg
//
LOCUS       NP_055970                738 aa            linear   PRI 21-NOV-2025
DEFINITION  la-related protein 4B isoform 1 [Homo sapiens].
ACCESSION   NP_055970 XP_005252491 XP_040265
VERSION     NP_055970.1
DBSOURCE    REFSEQ: accession NM_015155.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 738)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   4  (residues 1 to 738)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 738)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 738)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 738)
  AUTHORS   Schaffler,K., Schulz,K., Hirmer,A., Wiesner,J., Grimm,M.,
            Sickmann,A. and Fischer,U.
  TITLE     A stimulatory role for the La-related protein 4B in translation
  JOURNAL   RNA 16 (8), 1488-1499 (2010)
   PUBMED   20573744
REFERENCE   8  (residues 1 to 738)
  AUTHORS   Bayfield,M.A., Yang,R. and Maraia,R.J.
  TITLE     Conserved and divergent features of the structure and function of
            La and La-related proteins (LARPs)
  JOURNAL   Biochim Biophys Acta 1799 (5-6), 365-378 (2010)
   PUBMED   20138158
  REMARK    Review article
REFERENCE   9  (residues 1 to 738)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   10 (residues 1 to 738)
  AUTHORS   Bousquet-Antonelli,C. and Deragon,J.M.
  TITLE     A comprehensive analysis of the La-motif protein superfamily
  JOURNAL   RNA 15 (5), 750-764 (2009)
   PUBMED   19299548
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359878.13 and AL157709.17.
            
            On or before Aug 31, 2013 this sequence version replaced
            XP_005252491.1, XP_040265.6.
            
            Summary: This gene encodes a member of an evolutionarily conserved
            protein family implicated in RNA metabolism and translation.
            Members of this family are characterized by the presence of an La
            motif, which is often located adjacent to one or more RNA
            recognition motifs (RRM). Together, the two motifs constitute the
            functional region of the protein and enable its interaction with
            the RNA substrate. This protein family is divided into five
            sub-families: the genuine La proteins and four La-related protein
            (LARP) sub-families. The protein encoded by this gene belongs to
            LARP sub-family 4. It is a cytoplasmic protein that may play a
            stimulatory role in translation. [provided by RefSeq, Oct 2012].
            
            Transcript Variant: This variant (1) encodes the shorter isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.518925.1,
                                           SRR1163658.241754.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316157.8/ ENSP00000326128.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p15.3"
     Protein         1..738
                     /product="la-related protein 4B isoform 1"
                     /note="La ribonucleoprotein domain family, member 5;
                     la-related protein 4B; la-related protein 5; La
                     ribonucleoprotein domain family member 4B"
                     /calculated_mol_wt=80421
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92615.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Region          90..157
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92615.3)"
     Region          157..231
                     /region_name="LARP_5"
                     /note="La RNA-binding domain of La-related protein 5;
                     cd08036"
                     /db_xref="CDD:153405"
     Site            order(163,166..167,172,175..176,178,197..199)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153405"
     Region          236..312
                     /region_name="RRM_LARP5"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     La-related protein 5 (LARP5 or LARP4B); cd12706"
                     /db_xref="CDD:410105"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6A0A2; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Region          399..420
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92615.3)"
     Site            404
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Site            419
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Region          449..540
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92615.3)"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Site            493
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6A0A2; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Site            498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6A0A2; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q92615.3)"
     Site            556
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Region          591..738
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92615.3)"
     Site            601
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Site            724
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Site            727
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Site            732
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6A0A2; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     Site            736
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92615.3)"
     CDS             1..738
                     /gene="LARP4B"
                     /gene_synonym="KIAA0217; LARP5"
                     /coded_by="NM_015155.3:318..2534"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31131.1"
                     /db_xref="GeneID:23185"
                     /db_xref="HGNC:HGNC:28987"
                     /db_xref="MIM:616513"
ORIGIN      
        1 mtsdqdakvv aepqtqrvqe gkdsahlmng pisqttsqts sipplsqvpa tkvselnpna
       61 evwgapvlhl eassaadgvs aaweevaghh adrgpqgsda ngdgdqghen aalpdpqesd
      121 padmnalalg pseydslpen setggnesqp dsqedprevl kktlefclsr enlasdmyli
      181 sqmdsdqyvp ittvanldhi kklstdvdli vevlrslplv qvdekgekvr pnqnrcivil
      241 reisestpve evealfkgdn lpkfincefa yndnwfitfe teadaqqayk ylreevktfq
      301 gkpikarika kaiaintflp kngfrpldvs lyaqqryats fyfppmyspq qqfplyslit
      361 pqtwsathsy ldpplvtpfp ntgfingfts pafkpaaspl tslrqypprs rnpskshlrh
      421 aipsaergpg llespsifnf tadrlingvr spqtrqagqt rtriqnpsay akreagpgrv
      481 epgslesspg lgrgrknsfg yrkkreekft ssqtqsptpp kppspsfelg lssfpplpga
      541 agnlktedlf enrlssliig pskertlsad asvntlpvvv srepsvpasc avsatyersp
      601 spahlpddpk vaekqreths vdrlpsalta tacksvqvng aatelrkpsy aeicqrtske
      661 ppssplqpqk eqkpntvgcg keekklaepa eryreppalk stpgaprdqr rpaggrpsps
      721 amgkrlsreq stppkspq
//
LOCUS       NP_001350442             482 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 4 [Homo sapiens].
ACCESSION   NP_001350442 XP_005269440
VERSION     NP_001350442.1
DBSOURCE    REFSEQ: accession NM_001363513.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 482)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 482)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 482)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 482)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            On May 24, 2018 this sequence version replaced XP_005269440.1.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..482
                     /product="calcium uptake protein 1, mitochondrial isoform
                     4"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=51392
     transit_peptide 1..33
                     /note="Mitochondrion. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:26387864; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
                     /calculated_mol_wt=3784
     Region          68..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          99..110
                     /region_name="Polybasic region.
                     /evidence=ECO:0000269|PubMed:27099988"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCX5; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          126..129
                     /region_name="K/R-ring.
                     /evidence=ECO:0000269|PubMed:32494073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          228..447
                     /region_name="EFh_MICU1"
                     /note="EF-hand, calcium binding motif, found in calcium
                     uptake protein 1, mitochondrial (MICU1) and similar
                     proteins; cd16173"
                     /db_xref="CDD:320081"
     Region          228..257
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Site            order(230,382,385,388..389,391,409)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:320081"
     Site            order(237,239,241,248,427,429,431,438)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320081"
     Region          265..269
                     /region_name="K/R-ring.
                     /evidence=ECO:0000269|PubMed:32494073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          283..313
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          381..410
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          418..447
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          461..471
                     /region_name="C-helix region.
                     /evidence=ECO:0000269|PubMed:24514027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Site            461
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:27642082; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
     CDS             1..482
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001363513.2:72..1520"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS86101.1"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mfrlnslsal aelavgsrwy hggsqpiqir rrlmmvaflg asavtastgl lwkrahaesp
       61 pcvdnlksdi gdkgknkdeg dvcnhekkta dlaphpeekk kkrsgfrdrk vmeyenrira
      121 ystpdkifry fatlkvisep geaevfmtpe dfvrsitpne kqpehlgldq yiikrfdgkd
      181 fwqtekisqe rekfadegsi fytlgecgli sfsdyifltt vlstpqrnfe iafkmfdlng
      241 dgevdmeefe qvqsiirsqt smgmrhrdrp ttgntlksgl csalttyffg adlkgkltik
      301 nflefqrklq hdvlklefer hdpvdgrite rqfggmllay sgvqskklta mqrqlkkhfk
      361 egkgltfqev enfftflkni ndvdtalsfy hmagasldkv tmqqvartva kvelsdhvcd
      421 vvfalfdcdg ngelsnkefv simkqrlmrg lekpkdmgft rlmqamwkca qetawdfalp
      481 kq
//
LOCUS       NP_001229323             610 aa            linear   PRI 21-NOV-2025
DEFINITION  synaptotagmin-like protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_001229323
VERSION     NP_001229323.1
DBSOURCE    REFSEQ: accession NM_001242394.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Dong,X., Yang,L., Liu,K., Ji,X., Tang,C., Li,W., Ma,L., Mei,Y.,
            Peng,T., Feng,B., Wu,Z., Tang,Q., Gao,Y., Yan,K., Zhou,W. and
            Xiong,M.
  TITLE     Transcriptional networks identify synaptotagmin-like 3 as a
            regulator of cortical neuronal migration during early
            neurodevelopment
  JOURNAL   Cell Rep 34 (9), 108802 (2021)
   PUBMED   33657377
  REMARK    GeneRIF: Transcriptional networks identify synaptotagmin-like 3 as
            a regulator of cortical neuronal migration during early
            neurodevelopment.
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 610)
  AUTHORS   Kurowska,M., Goudin,N., Nehme,N.T., Court,M., Garin,J., Fischer,A.,
            de Saint Basile,G. and Menasche,G.
  TITLE     Terminal transport of lytic granules to the immune synapse is
            mediated by the kinesin-1/Slp3/Rab27a complex
  JOURNAL   Blood 119 (17), 3879-3889 (2012)
   PUBMED   22308290
  REMARK    Erratum:[Blood. 2014 Feb 27;123(9):1432]
REFERENCE   6  (residues 1 to 610)
  AUTHORS   Fukuda,M.
  TITLE     Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through
            interaction with the GDP-bound form of Rab27A in PC12 cells
  JOURNAL   J Biol Chem 278 (17), 15390-15396 (2003)
   PUBMED   12590134
REFERENCE   7  (residues 1 to 610)
  AUTHORS   Fukuda,M.
  TITLE     The C2A domain of synaptotagmin-like protein 3 (Slp3) is an
            atypical calcium-dependent phospholipid-binding machine: comparison
            with the C2A domain of synaptotagmin I
  JOURNAL   Biochem J 366 (Pt 2), 681-687 (2002)
   PUBMED   12049610
REFERENCE   8  (residues 1 to 610)
  AUTHORS   Kuroda,T.S., Fukuda,M., Ariga,H. and Mikoshiba,K.
  TITLE     The Slp homology domain of synaptotagmin-like proteins 1-4 and
            Slac2 functions as a novel Rab27A binding domain
  JOURNAL   J Biol Chem 277 (11), 9212-9218 (2002)
   PUBMED   11773082
  REMARK    GeneRIF: Synaptotagmin-like protein 3-a (Slp3-a) contains an
            N-terminal Slp homology domain (SHD) (PMID: 11327731). The SHD of
            Slp3-a specifically and directly binds the GTP-bound form of
            Rab27A.
REFERENCE   9  (residues 1 to 610)
  AUTHORS   Fukuda,M., Saegusa,C. and Mikoshiba,K.
  TITLE     Novel splicing isoforms of synaptotagmin-like proteins 2 and 3:
            identification of the Slp homology domain
  JOURNAL   Biochem Biophys Res Commun 283 (2), 513-519 (2001)
   PUBMED   11327731
REFERENCE   10 (residues 1 to 610)
  AUTHORS   Fukuda,M. and Mikoshiba,K.
  TITLE     Synaptotagmin-like protein 1-3: a novel family of C-terminal-type
            tandem C2 proteins
  JOURNAL   Biochem Biophys Res Commun 281 (5), 1226-1233 (2001)
   PUBMED   11243866
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC394549.1, BC100829.1,
            AK304191.1, AL567177.3 and AI674404.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to a family of
            peripheral membrane proteins that play a role in vesicular
            trafficking. This protein binds phospholipids in the presence of
            calcium ions. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) contains an alternate segment
            in the 5' UTR compared to variant 1. Variants 1 and 2 encode the
            same isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2485883.1,
                                           SRR14038192.1645379.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000611299.5/ ENSP00000483936.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..610
                     /product="synaptotagmin-like protein 3 isoform 1"
                     /note="exophilin-6; synaptotagmin-like protein 3"
                     /calculated_mol_wt=68429
     Region          8..123
                     /region_name="PHD_SF"
                     /note="PHD finger superfamily; cl22851"
                     /db_xref="CDD:473978"
     Region          60..108
                     /region_name="FYVE_Slp3"
                     /note="FYVE-related domain found in synaptotagmin-like
                     protein 3 (Slp3) and similar proteins; cd15765"
                     /db_xref="CDD:277304"
     Region          219..239
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VX76.3)"
     Region          307..434
                     /region_name="C2A_SLP-3"
                     /note="C2 domain first repeat present in
                     Synaptotagmin-like protein 3; cd08392"
                     /db_xref="CDD:176038"
     Region          448..610
                     /region_name="C2B_SLP_1-2-3-4"
                     /note="C2 domain second repeat present in
                     Synaptotagmin-like proteins 1-4; cd04020"
                     /db_xref="CDD:175987"
     CDS             1..610
                     /gene="SYTL3"
                     /gene_synonym="SLP3"
                     /coded_by="NM_001242394.2:752..2584"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS56458.1"
                     /db_xref="GeneID:94120"
                     /db_xref="HGNC:HGNC:15587"
                     /db_xref="MIM:620973"
ORIGIN      
        1 maqeidlsal kelereailq vlyrdqavqn teeertrklk thlqhlrwkg akntdwehke
       61 kccarcqqvl gfllhrgavc rgcshrvcaq crvflrgtha wkctvcfedr nvkiktgewf
      121 yeerakkfpt ggkhetvggq llqsyqklsk isvvpptppp vsesqcsrsp grlqefgqfr
      181 gfnksvenlf lslathvkkl sksqndmtse khllatgprq cvgqterrsq sdtavnvttr
      241 kvsapdilkp lnqedpkcst npilkqqnlp sspapstifs ggfrhgslis idstctemgn
      301 fdnanvtgei efaihycfkt hsleicikac knlaygeekk kkcnpyvkty llpdrssqgk
      361 rktgvqrntv dptfqetlky qvapaqlvtr qlqvsvwhlg tlarrvflge viiplatwdf
      421 edsttqsfrw hplrakaeky edsvpqsnge ltvraklvlp srprklqeaq egtdqpslhg
      481 qlclvvlgak nlpvrpdgtl nsfvkgcltl pdqqklrlks pvlrkqacpq wkhsfvfsgv
      541 tpaqlrqssl eltvwdqalf gmndrllggt rlgskgdtav ggdacslskl qwqkvlsspn
      601 lwtdmtlvlh
//
LOCUS       NP_001230228             761 aa            linear   PRI 21-NOV-2025
DEFINITION  amyloid beta precursor like protein 2 isoform 5 [Homo sapiens].
ACCESSION   NP_001230228
VERSION     NP_001230228.1
DBSOURCE    REFSEQ: accession NM_001243299.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Tao,Z., Huang,J. and Li,J.
  TITLE     Comprehensive intratumoral heterogeneity landscaping of liver
            hepatocellular carcinoma and discerning of APLP2 in cancer
            progression
  JOURNAL   Environ Toxicol 39 (2), 612-625 (2024)
   PUBMED   37515494
  REMARK    GeneRIF: Comprehensive intratumoral heterogeneity landscaping of
            liver hepatocellular carcinoma and discerning of APLP2 in cancer
            progression.
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Huang,X., Yang,J., Xi,H., Zhang,M., Oh,Y., Jin,Z. and Zheng,Z.
  TITLE     Implication of Amyloid Precursor-like Protein 2 Expression in
            Cutaneous Squamous Cell Carcinoma Pathogenesis
  JOURNAL   In Vivo 38 (1), 399-408 (2024)
   PUBMED   38148084
  REMARK    GeneRIF: Implication of Amyloid Precursor-like Protein 2 Expression
            in Cutaneous Squamous Cell Carcinoma Pathogenesis.
REFERENCE   4  (residues 1 to 761)
  AUTHORS   Chen,J., Tang,F., Li,H., Wu,X., Yang,Y., Liu,Z., Huang,X., Wang,J.,
            Zheng,R., Wang,L., Liu,H., Xu,J., Wang,P. and Liu,F.
  TITLE     Mycobacterium tuberculosis suppresses APLP2 expression to enhance
            its survival in macrophage
  JOURNAL   Int Immunopharmacol 124 (Pt B), 111058 (2023)
   PUBMED   37844466
  REMARK    GeneRIF: Mycobacterium tuberculosis suppresses APLP2 expression to
            enhance its survival in macrophage.
REFERENCE   5  (residues 1 to 761)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 761)
  AUTHORS   Blangy,A., Vidal,F., Cuzin,F., Yang,Y.H., Boulukos,K. and
            Rassoulzadegan,M.
  TITLE     CDEBP, a site-specific DNA-binding protein of the 'APP-like'
            family, is required during the early development of the mouse
  JOURNAL   J Cell Sci 108 (Pt 2), 675-683 (1995)
   PUBMED   7539437
REFERENCE   7  (residues 1 to 761)
  AUTHORS   von der Kammer,H., Hanes,J., Klaudiny,J. and Scheit,K.H.
  TITLE     A human amyloid precursor-like protein is highly homologous to a
            mouse sequence-specific DNA-binding protein
  JOURNAL   DNA Cell Biol 13 (11), 1137-1143 (1994)
   PUBMED   7702756
REFERENCE   8  (residues 1 to 761)
  AUTHORS   Bush,A.I., Pettingell,W.H. Jr., de Paradis,M., Tanzi,R.E. and
            Wasco,W.
  TITLE     The amyloid beta-protein precursor and its mammalian homologues.
            Evidence for a zinc-modulated heparin-binding superfamily
  JOURNAL   J Biol Chem 269 (43), 26618-26621 (1994)
   PUBMED   7929392
REFERENCE   9  (residues 1 to 761)
  AUTHORS   von der Kammer,H., Loffler,C., Hanes,J., Klaudiny,J., Scheit,K.H.
            and Hansmann,I.
  TITLE     The gene for the amyloid precursor-like protein APLP2 is assigned
            to human chromosome 11q23-q25
  JOURNAL   Genomics 20 (2), 308-311 (1994)
   PUBMED   8020984
REFERENCE   10 (residues 1 to 761)
  AUTHORS   Wasco,W., Gurubhagavatula,S., Paradis,M.D., Romano,D.M.,
            Sisodia,S.S., Hyman,B.T., Neve,R.L. and Tanzi,R.E.
  TITLE     Isolation and characterization of APLP2 encoding a homologue of the
            Alzheimer's associated amyloid beta protein precursor
  JOURNAL   Nat Genet 5 (1), 95-100 (1993)
   PUBMED   8220435
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK128162.1, BC000373.2,
            AK056883.1 and BM992563.1.
            
            Summary: This gene encodes amyloid precursor- like protein 2
            (APLP2), which is a member of the APP (amyloid precursor protein)
            family including APP, APLP1 and APLP2. This protein is ubiquitously
            expressed. It contains heparin-, copper- and zinc- binding domains
            at the N-terminus, BPTI/Kunitz inhibitor and E2 domains in the
            middle region, and transmembrane and intracellular domains at the
            C-terminus. This protein interacts with major histocompatibility
            complex (MHC) class I molecules. The synergy of this protein and
            the APP is required to mediate neuromuscular transmission, spatial
            learning and synaptic plasticity. This protein has been implicated
            in the pathogenesis of Alzheimer's disease. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            identified. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (7) differs in the 5' exon and
            also lacks an in-frame exon in the 3' coding region, compared to
            variant 1. It encodes isoform 5 which has a different N-terminus
            and lacks an internal segment in the C-terminal region, compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK128162.1, SRR7346977.1473311.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.3"
     Protein         1..761
                     /product="amyloid beta precursor like protein 2 isoform 5"
                     /note="amyloid precursor protein homolog HSD-2; CDEI
                     box-binding protein; amyloid beta (A4) precursor-like
                     protein 2; testicular tissue protein Li 23; sperm membrane
                     protein YWK-II"
                     /calculated_mol_wt=87084
     Region          52..214
                     /region_name="A4_EXTRA"
                     /note="amyloid A4; smart00006"
                     /db_xref="CDD:128326"
     Region          319..370
                     /region_name="Kunitz_ABPP-like"
                     /note="Kunitz domain found in the amyloid-beta precursor
                     protein (ABPP) subfamily; cd22607"
                     /db_xref="CDD:438650"
     Site            order(326..334,349,351,353)
                     /site_type="other"
                     /note="serine protease binding site [polypeptide binding]"
                     /db_xref="CDD:438650"
     Region          375..557
                     /region_name="APP_E2"
                     /note="E2 domain of amyloid precursor protein; pfam12925"
                     /db_xref="CDD:463752"
     Region          678..758
                     /region_name="JMTM_APLP2"
                     /note="juxtamembrane and transmembrane (JMTM) domain found
                     in amyloid-like protein 2 (APLP-2) and similar proteins;
                     cd21709"
                     /db_xref="CDD:411992"
     Site            order(678..679,693,696..697,700..701,703..704,707..708,
                     711,714)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:411992"
     Site            order(679..681,697..698,700..701,703..708,711..716)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:411992"
     CDS             1..761
                     /gene="APLP2"
                     /gene_synonym="APLP-2; APPH; APPL2; CDEBP"
                     /coded_by="NM_001243299.2:46..2331"
                     /note="isoform 5 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS58196.1"
                     /db_xref="GeneID:334"
                     /db_xref="HGNC:HGNC:598"
                     /db_xref="MIM:104776"
ORIGIN      
        1 mlrapgelpr qaarcslcrl gpgrgraffk wrclpasvdr gnplwalaan agtgfavaep
       61 qiamfcgkln mhvniqtgkw epdptgtksc fetkeevlqy cqemypelqi tnvmeanqrv
      121 sidnwcrrdk kqcksrfvtp fkclvgefvs dvllvpekcq ffhkermevc enhqhwhtvv
      181 keacltqgmt lysygmllpc gvdqfhgtey vccpqtkiig svskeeeeed eeeeeeedee
      241 edydvyksef pteadledft eaavdedded eeegeevved rdyyydtfkg ddyneenpte
      301 pgsdgtmsdk eithdvkavc sqeamtgpcr avmprwyfdl skgkcvrfiy ggcggnrnnf
      361 esedycmavc kamipptplp tndvdvyfet saddneharf qkakeqleir hrnrmdrvkk
      421 eweeaelqak nlpkaerqtl iqhfqamvka lekeaasekq qlvethlarv eamlndrrrm
      481 alenylaalq sdpprphril qalrryvrae nkdrlhtirh yqhvlavdpe kaaqmksqvm
      541 thlhvieerr nqslsllykv pyvaqeiqee idellqeqra dmdqftasis etpvdvrvss
      601 eeseeippfh pfhpfpalpe negsgvgeqd ggligaeekv insknkvden mvidetldvk
      661 emifnaervg gleeeresvg plredfslss saligllvia vaiatvivis lvmlrkrqyg
      721 tishgivevd pmltpeerhl nkmqnhgyen ptykyleqmq i
//
LOCUS       NP_001164263             410 aa            linear   PRI 21-NOV-2025
DEFINITION  regulator of microtubule dynamics protein 2 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001164263
VERSION     NP_001164263.1
DBSOURCE    REFSEQ: accession NM_001170792.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Nho,K., Risacher,S.L., Apostolova,L.G., Bice,P.J., Brosch,J.R.,
            Deardorff,R., Faber,K., Farlow,M.R., Foroud,T., Gao,S.,
            Rosewood,T., Kim,J.P., Nudelman,K., Yu,M., Aisen,P., Sperling,R.,
            Hooli,B., Shcherbinin,S., Svaldi,D., Jack,C.R. Jr., Jagust,W.J.,
            Landau,S., Vasanthakumar,A., Waring,J.F., Dore,V., Laws,S.M.,
            Masters,C.L., Porter,T., Rowe,C.C., Villemagne,V.L., Dumitrescu,L.,
            Hohman,T.J., Libby,J.B., Mormino,E., Buckley,R.F., Johnson,K.,
            Yang,H.S., Petersen,R.C., Ramanan,V.K., Ertekin-Taner,N.,
            Vemuri,P., Cohen,A.D., Fan,K.H., Kamboh,M.I., Lopez,O.L.,
            Bennett,D.A., Ali,M., Benzinger,T., Cruchaga,C., Hobbs,D., De
            Jager,P.L., Fujita,M., Jadhav,V., Lamb,B.T., Tsai,A.P.,
            Castanho,I., Mill,J., Weiner,M.W. and Saykin,A.J.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative (ADNI); Department of
            Defense Alzheimer's Disease Neuroimaging Initiative (DoD-ADNI);
            Anti-Amyloid Treatment in Asymptomatic Alzheimer's Study (A4 Study)
            and Longitudinal Evaluation of Amyloid Risk and Neurodegeneration
            (LEARN); Australian Imaging, Biomarker & Lifestyle Study (AIBL)
  TITLE     CYP1B1-RMDN2 Alzheimer's disease endophenotype locus identified for
            cerebral tau PET
  JOURNAL   Nat Commun 15 (1), 8251 (2024)
   PUBMED   39304655
  REMARK    GeneRIF: CYP1B1-RMDN2 Alzheimer's disease endophenotype locus
            identified for cerebral tau PET.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Di Mattia,T., Martinet,A., Ikhlef,S., McEwen,A.G., Nomine,Y.,
            Wendling,C., Poussin-Courmontagne,P., Voilquin,L., Eberling,P.,
            Ruffenach,F., Cavarelli,J., Slee,J., Levine,T.P., Drin,G.,
            Tomasetto,C. and Alpy,F.
  TITLE     FFAT motif phosphorylation controls formation and lipid transfer
            function of inter-organelle contacts
  JOURNAL   EMBO J 39 (23), e104369 (2020)
   PUBMED   33124732
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Oishi,K., Okano,H. and Sawa,H.
  TITLE     RMD-1, a novel microtubule-associated protein, functions in
            chromosome segregation in Caenorhabditis elegans
  JOURNAL   J Cell Biol 179 (6), 1149-1162 (2007)
   PUBMED   18070910
  REMARK    Erratum:[J Cell Biol. 2009 Aug 24;186(4):629]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC024243.2 and BQ017142.1.
            
            Transcript Variant: This variant (3) differs in both UTRs and in
            the 5' and 3' coding regions, compared to variant 1. The encoded
            isoform (2) has distinct N- and C-termini and is shorter than
            isoform 1. Both variants 2 and 3 encode the same isoform (2).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BR000689.1, BC024243.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119, SAMEA2155550
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.2"
     Protein         1..410
                     /product="regulator of microtubule dynamics protein 2
                     isoform 2"
                     /note="family with sequence similarity 82, member A;
                     regulator of microtubule dynamics protein 2;
                     microtubule-associated protein; family with sequence
                     similarity 82, member A1"
                     /calculated_mol_wt=47268
     Site            9..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LZ7.2)"
     Region          <24..108
                     /region_name="RMtype1_S_TRD-CR_like"
                     /note="Type I restriction-modification system specificity
                     (S) subunit Target Recognition Domain-ConseRved domain
                     (TRD-CR) and similar domains; cl38903"
                     /db_xref="CDD:365779"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BSE0; propagated from
                     UniProtKB/Swiss-Prot (Q96LZ7.2)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q498D5; propagated from
                     UniProtKB/Swiss-Prot (Q96LZ7.2)"
     Region          122..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LZ7.2)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96LZ7.2)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96LZ7.2)"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96LZ7.2)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96LZ7.2)"
     Region          302..352
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          357..385
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..410
                     /gene="RMDN2"
                     /gene_synonym="BLOCK18; FAM82A; FAM82A1; PRO34163;
                     PYST9371; RMD-2; RMD2; RMD4"
                     /coded_by="NM_001170792.3:195..1427"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS54351.1"
                     /db_xref="GeneID:151393"
                     /db_xref="HGNC:HGNC:26567"
                     /db_xref="MIM:611872"
ORIGIN      
        1 mpystnkeli lgimvgtagi sllllwyhkv rkpgiamklp eflslgntfn sitlqdeihd
       61 dqgttvifqe rqlqilekln elltnmeelk eeirflkeai pkleeyiqde lggkitvhki
      121 spqhrarkrr lptiqssats nsseeaeseg gyitantdte eqsfpvpkaf ntrveelnld
      181 vllqkvdhlr msesgksesf ellrdhkekf rdeiefmwrf araygdmyel stntqekkhy
      241 anigktlser ainrapmngh chlwyavlcg yvsefeglqn kinyghlfke hldiaikllp
      301 eepflyylkg rycytvskls wiekkmaatl fgkipsstvq ealhnflkae elcpgysnpn
      361 ymylakcytd leenqnalkf cnlalllptv tkedkeaqke mqkimtslkr
//
LOCUS       NP_002432                834 aa            linear   PRI 21-NOV-2025
DEFINITION  mutS protein homolog 5 isoform c [Homo sapiens].
ACCESSION   NP_002432 XP_941243
VERSION     NP_002432.1
DBSOURCE    REFSEQ: accession NM_002441.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Chen,L. and Weir,J.R.
  TITLE     The molecular machinery of meiotic recombination
  JOURNAL   Biochem Soc Trans 52 (1), 379-393 (2024)
   PUBMED   38348856
  REMARK    Review article
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Gong,C., Abbas,T., Muhammad,Z., Zhou,J., Khan,R., Ma,H., Zhang,H.,
            Shi,Q. and Shi,B.
  TITLE     A Homozygous Loss-of-Function Mutation in MSH5 Abolishes MutSgamma
            Axial Loading and Causes Meiotic Arrest in NOA-Affected Individuals
  JOURNAL   Int J Mol Sci 23 (12), 6522 (2022)
   PUBMED   35742973
  REMARK    GeneRIF: A Homozygous Loss-of-Function Mutation in MSH5 Abolishes
            MutSgamma Axial Loading and Causes Meiotic Arrest in NOA-Affected
            Individuals.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 834)
  AUTHORS   Snowden,T., Shim,K.S., Schmutte,C., Acharya,S. and Fishel,R.
  TITLE     hMSH4-hMSH5 adenosine nucleotide processing and interactions with
            homologous recombination machinery
  JOURNAL   J Biol Chem 283 (1), 145-154 (2008)
   PUBMED   17977839
  REMARK    GeneRIF: Data have identified the interaction region between the
            individual subunits of hMSH4-hMSH5 that are likely involved in
            clamp formation and show that each subunit of the heterodimer binds
            ATP.
REFERENCE   4  (residues 1 to 834)
  AUTHORS   Sekine,H., Ferreira,R.C., Pan-Hammarstrom,Q., Graham,R.R.,
            Ziemba,B., de Vries,S.S., Liu,J., Hippen,K., Koeuth,T., Ortmann,W.,
            Iwahori,A., Elliott,M.K., Offer,S., Skon,C., Du,L., Novitzke,J.,
            Lee,A.T., Zhao,N., Tompkins,J.D., Altshuler,D., Gregersen,P.K.,
            Cunningham-Rundles,C., Harris,R.S., Her,C., Nelson,D.L.,
            Hammarstrom,L., Gilkeson,G.S. and Behrens,T.W.
  TITLE     Role for Msh5 in the regulation of Ig class switch recombination
  JOURNAL   Proc Natl Acad Sci U S A 104 (17), 7193-7198 (2007)
   PUBMED   17409188
  REMARK    GeneRIF: These findings suggest that Msh4/5 heterodimers contribute
            to class switch recombination.
REFERENCE   5  (residues 1 to 834)
  AUTHORS   Yi,W., Wu,X., Lee,T.H., Doggett,N.A. and Her,C.
  TITLE     Two variants of MutS homolog hMSH5: prevalence in humans and
            effects on protein interaction
  JOURNAL   Biochem Biophys Res Commun 332 (2), 524-532 (2005)
   PUBMED   15907804
  REMARK    GeneRIF: The different properties associated with these two hMSH5
            variants underscore the potential functional diversity of the human
            hMSH5 gene.
            Erratum:[Biochem Biophys Res Commun. 2006 Feb 17;340(3):1018]
REFERENCE   6  (residues 1 to 834)
  AUTHORS   Bocker,T., Barusevicius,A., Snowden,T., Rasio,D., Guerrette,S.,
            Robbins,D., Schmidt,C., Burczak,J., Croce,C.M., Copeland,T.,
            Kovatich,A.J. and Fishel,R.
  TITLE     hMSH5: a human MutS homologue that forms a novel heterodimer with
            hMSH4 and is expressed during spermatogenesis
  JOURNAL   Cancer Res 59 (4), 816-822 (1999)
   PUBMED   10029069
REFERENCE   7  (residues 1 to 834)
  AUTHORS   Winand,N.J., Panzer,J.A. and Kolodner,R.D.
  TITLE     Cloning and characterization of the human and Caenorhabditis
            elegans homologs of the Saccharomyces cerevisiae MSH5 gene
  JOURNAL   Genomics 53 (1), 69-80 (1998)
   PUBMED   9787078
REFERENCE   8  (residues 1 to 834)
  AUTHORS   Her,C. and Doggett,N.A.
  TITLE     Cloning, structural characterization, and chromosomal localization
            of the human orthologue of Saccharomyces cerevisiae MSH5 gene
  JOURNAL   Genomics 52 (1), 50-61 (1998)
   PUBMED   9740671
REFERENCE   9  (residues 1 to 834)
  AUTHORS   Albertella,M.R., Jones,H., Thomson,W., Olavesen,M.G. and
            Campbell,R.D.
  TITLE     Localization of eight additional genes in the human major
            histocompatibility complex, including the gene encoding the casein
            kinase II beta subunit (CSNK2B)
  JOURNAL   Genomics 36 (2), 240-251 (1996)
   PUBMED   8812450
REFERENCE   10 (residues 1 to 834)
  AUTHORS   Sargent,C.A., Dunham,I. and Campbell,R.D.
  TITLE     Identification of multiple HTF-island associated genes in the human
            major histocompatibility complex class III region
  JOURNAL   EMBO J 8 (8), 2305-2312 (1989)
   PUBMED   2477242
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB448226.1, AF048986.1 and
            AL662899.5.
            
            On Mar 4, 2006 this sequence version replaced XP_941243.1.
            
            Summary: This gene encodes a member of the mutS family of proteins
            that are involved in DNA mismatch repair and meiotic recombination.
            This protein is similar to a Saccharomyces cerevisiae protein that
            participates in segregation fidelity and crossing-over events
            during meiosis. This protein plays a role in promoting ionizing
            radiation-induced apoptosis. This protein forms hetero-oligomers
            with another member of this family, mutS homolog 4. Polymorphisms
            in this gene have been linked to various human diseases, including
            IgA deficiency, common variable immunodeficiency, and premature
            ovarian failure. Alternative splicing results multiple transcript
            variants. Read-through transcription also exists between this gene
            and the downstream chromosome 6 open reading frame 26 (C6orf26)
            gene. [provided by RefSeq, Feb 2011].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and uses
            alternate in-frame splice sites in both the central and 3' coding
            regions, compared to variant 1, resulting in an isoform (c) that is
            longer than isoform a. Both variants 3 and 4 encode the same
            isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF048986.1, AF070071.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..834
                     /product="mutS protein homolog 5 isoform c"
                     /note="mutS protein homolog 5"
                     /calculated_mol_wt=92745
     Region          1..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43196.1)"
     Region          <245..773
                     /region_name="mutS1"
                     /note="DNA mismatch repair protein MutS; TIGR01070"
                     /db_xref="CDD:273427"
     Region          557..763
                     /region_name="ABC_MSH5_euk"
                     /note="ATP-binding cassette domain of eukaryotic MutS5
                     homolog; cd03281"
                     /db_xref="CDD:213248"
     Site            592..599
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213248"
     Site            order(595..596,598..600,636,671..672,708)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:213248"
     Site            633..636
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213248"
     Site            641..654
                     /site_type="other"
                     /note="ABC transporter signature motif"
                     /db_xref="CDD:213248"
     Site            667..672
                     /site_type="other"
                     /note="Walker B"
                     /db_xref="CDD:213248"
     Site            675..678
                     /site_type="other"
                     /note="D-loop"
                     /db_xref="CDD:213248"
     Site            704..710
                     /site_type="other"
                     /note="H-loop/switch region"
                     /db_xref="CDD:213248"
     CDS             1..834
                     /gene="MSH5"
                     /gene_synonym="G7; MUTSH5; NG23; POF13; SPGF74"
                     /coded_by="NM_002441.5:230..2734"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS4720.1"
                     /db_xref="GeneID:4439"
                     /db_xref="HGNC:HGNC:7328"
                     /db_xref="MIM:603382"
ORIGIN      
        1 maslganprr tpqgprpgaa ssgfpspapv pgpreaeeee veeeeelaei hlcvlwnsgy
       61 lgiayydtsd stihfmpdap dheslkllqr vldeinpqsv vtsakqdenm trflgklasq
      121 ehrepkrpei iflpsvdfgl eiskqrllsg nysfipdamt atekilflss iipfdclltv
      181 ralggllkfl grrrigvele dynvsvpilg fkkfmlthlv nidqdtysvl qifkseshps
      241 vykvasglke glslfgilnr chckwgekll rlwftrpthd lgelssrldv iqffllpqnl
      301 dmaqmlhrll ghiknvplil krmklshtkv sdwqvlyktv ysalglrdac rslpqsiqlf
      361 rdiaqefsdd lhhiasligk vvdfegslae nrftvlpnid peidekkrrl mglpsfltev
      421 arkelenlds ripscsviyi pligfllsip rlpsmveasd feingldfmf lseeklhyrs
      481 artkeldall gdlhceirdq etllmyqlqc qvlaraavlt rvldlasrld vllalasaar
      541 dygysrprys pqvlgvriqn grhplmelca rtfvpnstec ggdkgrvkvi tgpnssgksi
      601 ylkqvglitf malvgsfvpa eeaeigavda iftrihsces islglstfmi dlnqvakavn
      661 nataqslvli defgkgtntv dglallaavl rhwlargptc phifvatnfl slvqlqllpq
      721 gplvqyltme tcedgndlvf fyqvcegvak ashashtaaq aglpdklvar gkevsdlirs
      781 gkpikpvkdl lkknqmencq tlvdkfmkld ledpnldlnv fmsqevlpaa tsil
//
LOCUS       NP_001371767            1143 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 20 [Homo sapiens].
ACCESSION   NP_001371767
VERSION     NP_001371767.1
DBSOURCE    REFSEQ: accession NM_001384838.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1143)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1143)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1143)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1143)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1143)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1143)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1143)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1143)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1143)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1143)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.130400.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1143
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1143
                     /product="microtubule-associated protein 4 isoform 20"
                     /note="MAP-4"
                     /calculated_mol_wt=119966
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          50..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          248..545
                     /region_name="17 X 14 AA tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          362..401
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          <575..910
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            580
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            696
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10791892,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            704
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            714
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            778
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10791892,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            788
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            794
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            816
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            818
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            844
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            919
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          <922..943
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            932
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            933
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          983..1013
                     /region_name="Tau/MAP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          983..1012
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            991
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          1014..1044
                     /region_name="Tau/MAP 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1014..1043
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          1045..1076
                     /region_name="Tau/MAP 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1045..1075
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            1064
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1065..1143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            1136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            1142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     CDS             1..1143
                     /gene="MAP4"
                     /coded_by="NM_001384838.1:96..3527"
                     /note="isoform 20 is encoded by transcript variant 90"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgsp tefleekmay qeypnsqnwp
      121 edtnfcfqpe qvvdpiqtdp fkmyhdddla dlvfpssata dtsifagqnd plkdsygmsp
      181 cntavvpqgw svealnsphs esfvspeava eppqptavpl elakeiemas eerppaqale
      241 immglkttdm apsketemal akdmalatkt evalakdmes ptkldvtlak dmqpsmesdm
      301 alvkdmelpt ekevalvkdv rwptetdvss aknvvlptet evapakdvtl lketeraspi
      361 kmdlapskdm gppkenkket eraspikmdl apskdmgppk enkivpakdl vllseievaq
      421 andiisstei ssaekvalss etevalardm tlppetnvil tkdkalplea evapvkdmaq
      481 lpeteiapak dvapstvkev gllkdmspls etemalgkdv tpppetevvl iknvclppem
      541 evaltedqvp alkteaplak dgvltlannv tpakdvppls eteatpvpik dmeiaqtqkg
      601 isedshlesl qdvgqsaapt fmispetvtg tgkkcslpae edsvleklge rkpcnsqpse
      661 lssetsgiar peegrpvvsg tgndittppn kelppspekk tktstskakt qptslpkqpa
      721 pttigglnkk pmslasglvp aappkrpava sarpsilpsk dvkpkpiada kapekrasps
      781 kpasapasrs gskstqtvak tttaaavast gpssrspstl lpkkptaikt egkpaevkkm
      841 taksvpadls rpkststssm kktttlsgta paagvvpsrv katpmpsrps ttpfidkkpt
      901 sakpssttpr lsrlatntsa pdlknvrskv gstenikhqp gggrakvekk teaaattrkp
      961 esnavtktag piasaqkqpa gkvqivskkv syshiqskcg skdnikhvpg ggnvqiqnkk
     1021 vdiskvsskc gskanikhkp gggdvkiesq klnfkekaqa kvgsldnvgh lpaggavkte
     1081 gggseaplcp gppageepai seaapeagap tsasglnghp tlsgggdqre aqtldsqiqe
     1141 tsi
//
LOCUS       NP_001074930             414 aa            linear   PRI 21-NOV-2025
DEFINITION  bifunctional arginine demethylase and lysyl-hydroxylase JMJD6
            isoform 1 [Homo sapiens].
ACCESSION   NP_001074930
VERSION     NP_001074930.1
DBSOURCE    REFSEQ: accession NM_001081461.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Pei,R., Zhao,L., Ding,Y., Su,Z., Li,D., Zhu,S., Xu,L., Zhao,W. and
            Zhou,W.
  TITLE     JMJD6-BRD4 complex stimulates lncRNA HOTAIR transcription by
            binding to the promoter region of HOTAIR and induces
            radioresistance in liver cancer stem cells
  JOURNAL   J Transl Med 21 (1), 752 (2023)
   PUBMED   37880710
  REMARK    GeneRIF: JMJD6-BRD4 complex stimulates lncRNA HOTAIR transcription
            by binding to the promoter region of HOTAIR and induces
            radioresistance in liver cancer stem cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Chen,S., Wang,M., Lu,T., Liu,Y., Hong,W., He,X., Cheng,Y., Liu,J.,
            Wei,Y. and Wei,X.
  TITLE     JMJD6 in tumor-associated macrophage regulates macrophage
            polarization and cancer progression via STAT3/IL-10 axis
  JOURNAL   Oncogene 42 (37), 2737-2750 (2023)
   PUBMED   37567973
  REMARK    GeneRIF: JMJD6 in tumor-associated macrophage regulates macrophage
            polarization and cancer progression via STAT3/IL-10 axis.
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Merchant,J.P., Zhu,K., Henrion,M.Y.R., Zaidi,S.S.A., Lau,B.,
            Moein,S., Alamprese,M.L., Pearse,R.V. 2nd, Bennett,D.A.,
            Ertekin-Taner,N., Young-Pearse,T.L. and Chang,R.
  TITLE     Predictive network analysis identifies JMJD6 and other potential
            key drivers in Alzheimer's disease
  JOURNAL   Commun Biol 6 (1), 503 (2023)
   PUBMED   37188718
  REMARK    GeneRIF: Predictive network analysis identifies JMJD6 and other
            potential key drivers in Alzheimer's disease.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Klose,R.J., Kallin,E.M. and Zhang,Y.
  TITLE     JmjC-domain-containing proteins and histone demethylation
  JOURNAL   Nat Rev Genet 7 (9), 715-727 (2006)
   PUBMED   16983801
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Williamson,P. and Schlegel,R.A.
  TITLE     Hide and seek: the secret identity of the phosphatidylserine
            receptor
  JOURNAL   J Biol 3 (4), 14 (2004)
   PUBMED   15453906
  REMARK    Review article
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Chan,A., Seguin,R., Magnus,T., Papadimitriou,C., Toyka,K.V.,
            Antel,J.P. and Gold,R.
  TITLE     Phagocytosis of apoptotic inflammatory cells by microglia and its
            therapeutic implications: termination of CNS autoimmune
            inflammation and modulation by interferon-beta
  JOURNAL   Glia 43 (3), 231-242 (2003)
   PUBMED   12898702
REFERENCE   8  (residues 1 to 414)
  AUTHORS   Ajmone-Cat,M.A., De Simone,R., Nicolini,A. and Minghetti,L.
  TITLE     Effects of phosphatidylserine on p38 mitogen activated protein
            kinase, cyclic AMP responding element binding protein and nuclear
            factor-kappaB activation in resting and activated microglial cells
  JOURNAL   J Neurochem 84 (2), 413-416 (2003)
   PUBMED   12559004
REFERENCE   9  (residues 1 to 414)
  AUTHORS   Vandivier,R.W., Fadok,V.A., Hoffmann,P.R., Bratton,D.L.,
            Penvari,C., Brown,K.K., Brain,J.D., Accurso,F.J. and Henson,P.M.
  TITLE     Elastase-mediated phosphatidylserine receptor cleavage impairs
            apoptotic cell clearance in cystic fibrosis and bronchiectasis
  JOURNAL   J Clin Invest 109 (5), 661-670 (2002)
   PUBMED   11877474
  REMARK    GeneRIF: Elastase-mediated phosphatidylserine receptor cleavage
            impairs apoptotic cell clearance in cystic fibrosis and
            bronchiectasis.
REFERENCE   10 (residues 1 to 414)
  AUTHORS   Fadok,V.A., Bratton,D.L., Rose,D.M., Pearson,A., Ezekewitz,R.A. and
            Henson,P.M.
  TITLE     A receptor for phosphatidylserine-specific clearance of apoptotic
            cells
  JOURNAL   Nature 405 (6782), 85-90 (2000)
   PUBMED   10811223
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB451815.1, AB011157.1,
            AC005837.1 and AA775442.1.
            
            Summary: This gene encodes a nuclear protein with a JmjC domain.
            JmjC domain-containing proteins are predicted to function as
            protein hydroxylases or histone demethylases. This protein was
            first identified as a putative phosphatidylserine receptor involved
            in phagocytosis of apoptotic cells; however, subsequent studies
            have indicated that it does not directly function in the clearance
            of apoptotic cells, and questioned whether it is a true
            phosphatidylserine receptor. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.252826.1,
                                           SRR1803614.164979.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151358, SAMEA2161674
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..414
                     /product="bifunctional arginine demethylase and
                     lysyl-hydroxylase JMJD6 isoform 1"
                     /EC_number="1.14.11.-"
                     /note="bifunctional arginine demethylase and
                     lysyl-hydroxylase JMJD6; jmjC domain-containing protein 6;
                     histone arginine demethylase JMJD6; peptide-lysine
                     5-dioxygenase JMJD6; jumonji domain-containing protein 6;
                     arginine demethylase and lysine hydroxylase;
                     phosphatidylserine receptor"
                     /calculated_mol_wt=47495
     Region          6..10
                     /region_name="Nuclear localization signal 1.
                     /evidence=ECO:0000269|PubMed:14729065"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NYC1.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NYC1.1)"
     Region          57..284
                     /region_name="Cupin_8"
                     /note="Cupin-like domain; pfam13621"
                     /db_xref="CDD:463936"
     Region          91..95
                     /region_name="Nuclear localization signal 2.
                     /evidence=ECO:0000269|PubMed:14729065"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NYC1.1)"
     Region          141..145
                     /region_name="Nuclear localization signal 3.
                     /evidence=ECO:0000269|PubMed:14729065"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NYC1.1)"
     Region          167..170
                     /region_name="Nuclear localization signal 4.
                     /evidence=ECO:0000269|PubMed:14729065"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NYC1.1)"
     Region          174..288
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     Region          336..403
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NYC1.1)"
     Region          373..378
                     /region_name="Nuclear localization signal 5.
                     /evidence=ECO:0000269|PubMed:14729065"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NYC1.1)"
     CDS             1..414
                     /gene="JMJD6"
                     /gene_synonym="PSR; PTDSR; PTDSR1"
                     /coded_by="NM_001081461.2:132..1376"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42383.1"
                     /db_xref="GeneID:23210"
                     /db_xref="HGNC:HGNC:19355"
                     /db_xref="MIM:604914"
ORIGIN      
        1 mnhkskkrir eakrsarpel kdsldwtrhn yyesfslspa avadnverad alqlsveefv
       61 eryerpykpv vllnaqegws aqekwtlerl krkyrnqkfk cgedndgysv kmkmkyyiey
      121 mestrddspl yifdssygeh pkrrklledy kvpkfftddl fqyagekrrp pyrwfvmgpp
      181 rsgtgihidp lgtsawnalv qghkrwclfp tstprelikv trdeggnqqd eaitwfnviy
      241 prtqlptwpp efkpleilqk pgetvfvpgg wwhvvlnldt tiaitqnfas stnfpvvwhk
      301 tvrgrpklsr kwyrilkqeh pelavladsv dlqestgias dsssdsssss sssssdsdse
      361 cesgsegdgt vhrrkkrrtc smvgngdtts qddcvskers ssrirdtcgg rahp
//
LOCUS       NP_001128409             588 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 2 [Homo sapiens].
ACCESSION   NP_001128409
VERSION     NP_001128409.1
DBSOURCE    REFSEQ: accession NM_001134937.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Muckenfuss,L.M., Migenda Herranz,A.C., Boneberg,F.M., Clerici,M.
            and Jinek,M.
  TITLE     Fip1 is a multivalent interaction scaffold for processing factors
            in human mRNA 3' end biogenesis
  JOURNAL   Elife 11, e80332 (2022)
   PUBMED   36073787
  REMARK    GeneRIF: Fip1 is a multivalent interaction scaffold for processing
            factors in human mRNA 3' end biogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   3  (residues 1 to 588)
  AUTHORS   Tennenbaum,J., Groh,M., Venditti,L., Campos-Gazeau,F., Chalayer,E.,
            De Broucker,T., Hamidou,M., Hunault,M., Lyoubi,A., Meunier,R.,
            Muron,T., Sene,D., Slama,B., Guidoux,C., Lefevre,G., Kahn,J.E.,
            Denier,C. and Rohmer,J.
  TITLE     FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a Treatable
            Cause of Watershed Infarction
  JOURNAL   Stroke 52 (10), e605-e609 (2021)
   PUBMED   34304603
  REMARK    GeneRIF: FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a
            Treatable Cause of Watershed Infarction.
REFERENCE   4  (residues 1 to 588)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 588)
  AUTHORS   Helbig,G., Lewandowski,K., Swiderska,A., Rodzaj,M., Seferynska,I.
            and Gajkowska-Kulik,J.
  TITLE     Exquisite response to imatinib mesylate in FIP1L1-PDGFRA-mutated
            hypereosinophilic syndrome: a 12-year experience of the Polish
            Hypereosinophilic Syndrome Study Group
  JOURNAL   Pol Arch Intern Med 130 (3), 255-257 (2020)
   PUBMED   32125294
  REMARK    GeneRIF: Exquisite response to imatinib mesylate in
            FIP1L1-PDGFRA-mutated hypereosinophilic syndrome: a 12-year
            experience of the Polish Hypereosinophilic Syndrome Study Group.
REFERENCE   6  (residues 1 to 588)
  AUTHORS   Cools,J., Quentmeier,H., Huntly,B.J., Marynen,P., Griffin,J.D.,
            Drexler,H.G. and Gilliland,D.G.
  TITLE     The EOL-1 cell line as an in vitro model for the study of
            FIP1L1-PDGFRA-positive chronic eosinophilic leukemia
  JOURNAL   Blood 103 (7), 2802-2805 (2004)
   PUBMED   14630792
  REMARK    GeneRIF: results indicate that the fusion of FIP1L1 to PDGFRA
            occurs rarely in leukemia cell lines
REFERENCE   7  (residues 1 to 588)
  AUTHORS   Kaufmann,I., Martin,G., Friedlein,A., Langen,H. and Keller,W.
  TITLE     Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements
            and stimulates poly(A) polymerase
  JOURNAL   EMBO J 23 (3), 616-626 (2004)
   PUBMED   14749727
REFERENCE   8  (residues 1 to 588)
  AUTHORS   Pardanani,A., Ketterling,R.P., Brockman,S.R., Flynn,H.C.,
            Paternoster,S.F., Shearer,B.M., Reeder,T.L., Li,C.Y., Cross,N.C.,
            Cools,J., Gilliland,D.G., Dewald,G.W. and Tefferi,A.
  TITLE     CHIC2 deletion, a surrogate for FIP1L1-PDGFRA fusion, occurs in
            systemic mastocytosis associated with eosinophilia and predicts
            response to imatinib mesylate therapy
  JOURNAL   Blood 102 (9), 3093-3096 (2003)
   PUBMED   12842979
  REMARK    GeneRIF: observations suggest that the FIP1L1-PDGFRA rearrangement
            occurs in an early hematopoietic progenitor and suggests that the
            molecular pathogenesis for a subset of SMCD patients is similar to
            that of HES
REFERENCE   9  (residues 1 to 588)
  AUTHORS   Griffin,J.H., Leung,J., Bruner,R.J., Caligiuri,M.A. and
            Briesewitz,R.
  TITLE     Discovery of a fusion kinase in EOL-1 cells and idiopathic
            hypereosinophilic syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (13), 7830-7835 (2003)
   PUBMED   12808148
REFERENCE   10 (residues 1 to 588)
  AUTHORS   Cools,J., DeAngelo,D.J., Gotlib,J., Stover,E.H., Legare,R.D.,
            Cortes,J., Kutok,J., Clark,J., Galinsky,I., Griffin,J.D.,
            Cross,N.C., Tefferi,A., Malone,J., Alam,R., Schrier,S.L.,
            Schmid,J., Rose,M., Vandenberghe,P., Verhoef,G., Boogaerts,M.,
            Wlodarska,I., Kantarjian,H., Marynen,P., Coutre,S.E., Stone,R. and
            Gilliland,D.G.
  TITLE     A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes
            as a therapeutic target of imatinib in idiopathic hypereosinophilic
            syndrome
  JOURNAL   N Engl J Med 348 (13), 1201-1214 (2003)
   PUBMED   12660384
  REMARK    GeneRIF: The hypereosinophilic syndrome may result from a novel
            fusion tyrosine kinase - FIP1L1-PDGFRalpha - that is a consequence
            of an interstitial chromosomal deletion.
            GeneRIF: Describes the fusion gene Fip1-like-1-PDGFRalpha in
            patients with idiopathic hypereosinophilic syndrome, mostly
            responsive to imatinib therapy.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098821.3 and AC058822.6.
            
            Summary: This gene encodes a subunit of the CPSF (cleavage and
            polyadenylation specificity factor) complex that polyadenylates the
            3' end of mRNA precursors. This gene, the homolog of yeast Fip1
            (factor interacting with PAP), binds to U-rich sequences of
            pre-mRNA and stimulates poly(A) polymerase activity. Its N-terminus
            contains a PAP-binding site and its C-terminus an RNA-binding
            domain. An interstitial chromosomal deletion on 4q12 creates an
            in-frame fusion of human genes FIP1L1 and PDGFRA (platelet-derived
            growth factor receptor, alpha). The FIP1L1-PDGFRA fusion gene
            encodes a constitutively activated tyrosine kinase that joins the
            first 233 amino acids of FIP1L1 to the last 523 amino acids of
            PDGFRA. This gene fusion and chromosomal deletion is the cause of
            some forms of idiopathic hypereosinophilic syndrome (HES). This
            syndrome, recently reclassified as chronic eosinophilic leukemia
            (CEL), is responsive to treatment with tyrosine kinase inhibitors.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295737.1, SRR1660805.253177.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..588
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     2"
                     /note="rearranged in hypereosinophilia; pre-mRNA
                     3'-end-processing factor FIP1; FIP1-like 1 protein; factor
                     interacting with PAP; FIP1 like 1; FIP1L1 cleavage and
                     polyadenylation specific factor subunit"
                     /calculated_mol_wt=65597
     Region          139..181
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     CDS             1..588
                     /gene="FIP1L1"
                     /gene_synonym="FIP1; hFip1; Rhe"
                     /coded_by="NM_001134937.2:199..1965"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47055.1"
                     /db_xref="GeneID:81608"
                     /db_xref="HGNC:HGNC:19124"
                     /db_xref="MIM:607686"
ORIGIN      
        1 msageverlv selsggtggd eeeewlygde neverpeeen asanppsgie detaengvpk
       61 pkvtetedds dsdsdddedd vhvtigdikt gapqygsygt apvnlniktg grvygttgtk
      121 vkgvdldapg singvpllev dldsfedkpw rkpgadlsdy fnygfnedtw kaycekqkri
      181 rmglevipvt sttnkitaed ctmevtpgae iqdgrfnlfk vqqgrtgnse ketalpstka
      241 eftsppslfk tglppsrnst ssqsqtstas rkanssvgkw qdrygraesp dlrrlpgaid
      301 vigqtitisr vegrrranen sniqvlsers atevdnnfsk pppffppgap pthlppppfl
      361 pppptvstap plipppgipi tvpppgfppp pgapppslip tiesghssgy dsrsarafpy
      421 gnvafphlpg sapswpslvd tskqwdyyar rekdrdrerd rdrerdrdrd rerertrere
      481 rerdhsptps vfnsdeeryr yreyaergye rhrasrekee rhrerrhrek eetrhkssrs
      541 nsrrrhesee gdshrrhkhk kskrskegke agsepapeqe steatpae
//
LOCUS       NP_055595               1698 aa            linear   PRI 21-NOV-2025
DEFINITION  cullin-7 isoform 2 [Homo sapiens].
ACCESSION   NP_055595
VERSION     NP_055595.2
DBSOURCE    REFSEQ: accession NM_014780.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1698)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1698)
  AUTHORS   Zhou,H.L., Grimmett,Z.W., Venetos,N.M., Stomberski,C.T., Qian,Z.,
            McLaughlin,P.J., Bansal,P.K., Zhang,R., Reynolds,J.D., Premont,R.T.
            and Stamler,J.S.
  TITLE     An enzyme that selectively S-nitrosylates proteins to regulate
            insulin signaling
  JOURNAL   Cell 186 (26), 5812-5825 (2023)
   PUBMED   38056462
REFERENCE   3  (residues 1 to 1698)
  AUTHORS   Wang,C., Zhao,Z., Zhang,Y., Liang,W., Zhou,C., Lin,W., He,Y.,
            Wu,M., Meng,Z., Liao,Y., Li,M., El Akkawi,M., Zhao,J. and He,Y.
  TITLE     Identification and verification of the prognostic value of CUL7 in
            colon adenocarcinoma
  JOURNAL   Front Immunol 13, 1043512 (2022)
   PUBMED   36304472
  REMARK    GeneRIF: Identification and verification of the prognostic value of
            CUL7 in colon adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1698)
  AUTHORS   Hopf,L.V.M., Baek,K., Klugel,M., von Gronau,S., Xiong,Y. and
            Schulman,B.A.
  TITLE     Structure of CRL7FBXW8 reveals coupling with CUL1-RBX1/ROC1 for
            multi-cullin-RING E3-catalyzed ubiquitin ligation
  JOURNAL   Nat Struct Mol Biol 29 (9), 854-862 (2022)
   PUBMED   35982156
REFERENCE   5  (residues 1 to 1698)
  AUTHORS   Goos,H., Kinnunen,M., Salokas,K., Tan,Z., Liu,X., Yadav,L.,
            Zhang,Q., Wei,G.H. and Varjosalo,M.
  TITLE     Human transcription factor protein interaction networks
  JOURNAL   Nat Commun 13 (1), 766 (2022)
   PUBMED   35140242
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1698)
  AUTHORS   Arai,T., Kasper,J.S., Skaar,J.R., Ali,S.H., Takahashi,C. and
            DeCaprio,J.A.
  TITLE     Targeted disruption of p185/Cul7 gene results in abnormal vascular
            morphogenesis
  JOURNAL   Proc Natl Acad Sci U S A 100 (17), 9855-9860 (2003)
   PUBMED   12904573
REFERENCE   7  (residues 1 to 1698)
  AUTHORS   Dias,D.C., Dolios,G., Wang,R. and Pan,Z.Q.
  TITLE     CUL7: A DOC domain-containing cullin selectively binds Skp1.Fbx29
            to form an SCF-like complex
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16601-16606 (2002)
   PUBMED   12481031
REFERENCE   8  (residues 1 to 1698)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   9  (residues 1 to 1698)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   10 (residues 1 to 1698)
  AUTHORS   Akilapa,R., Irving,M. and Holder-Espinasse,M.
  TITLE     3-M Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355385.15 and AL136304.10.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 3, 2004 this sequence version replaced NP_055595.1.
            
            Summary: The protein encoded by this gene is a component of an E3
            ubiquitin-protein ligase complex. The encoded protein interacts
            with TP53, CUL9, and FBXW8 proteins. Defects in this gene are a
            cause of 3M syndrome type 1 (3M1). Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Dec 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033647.1, SRR11853561.24882.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265348.9/ ENSP00000265348.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1698
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..1698
                     /product="cullin-7 isoform 2"
                     /calculated_mol_wt=191030
     Region          315..357
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14999.2)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14999.2)"
     Region          362..434
                     /region_name="Cul7"
                     /note="Mouse development and cellular proliferation
                     protein Cullin-7; pfam11515"
                     /db_xref="CDD:463286"
     Region          601..623
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14999.2)"
     Region          838..968
                     /region_name="APC10-CUL7"
                     /note="APC10-like DOC1 domain of CUL7, subunit of the
                     SCF-ROC1-like E3 ubiquitin ligase complex that mediates
                     substrate ubiquitination; cd08665"
                     /db_xref="CDD:176486"
     Site            order(864,892,898,900,960)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:176486"
     Region          <1217..1506
                     /region_name="Cullin"
                     /note="Cullin family; pfam00888"
                     /db_xref="CDD:459983"
     Region          1345..1370
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14999.2)"
     Region          1561..1639
                     /region_name="Cullin_Nedd8"
                     /note="Cullin protein neddylation domain; smart00884"
                     /db_xref="CDD:214883"
     CDS             1..1698
                     /gene="CUL7"
                     /gene_synonym="3M1; CUL-7; dJ20C7.5; KIAA0076"
                     /coded_by="NM_014780.5:239..5335"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4881.1"
                     /db_xref="GeneID:9820"
                     /db_xref="HGNC:HGNC:21024"
                     /db_xref="MIM:609577"
ORIGIN      
        1 mvgelryref rvplgpglha ypdelirqrv ghdghpeyqi rwlilrrgde gdggsgqvdc
       61 kaehillwms kdeiyanchk mlgedgqvig psqesagevg aldksvleem etdvksliqr
      121 alrqleecvg tippapllht vhvlsayasi epltgvfkdp rvldllmhml sspdyqirws
      181 agrmiqalss hdagtrtqil lslsqqeaie khldfdsrca llalfaqatl sehpmsfegi
      241 qlpqvpgrvl fslvkrylhv tslldqlnds aaepgaqnts apeelsgerg qlelefsmam
      301 gtliselvqa mrwdqasdrp rssarspgsi fqpqladvsp glpaaqaqps frrsrrfrpr
      361 sefasgntya lyvrdtlqpg mrvrmlddye eisagdegef rqsnngvppv qvfwestgrt
      421 ywvhwhmlei lgfeediedm veadeyqgav asrvlgralp awrwrpmtel yavpyvlped
      481 edteecehlt laewwellff ikkldgpdhq evlqilqenl dgeilddeil aelavpiela
      541 qdllltlpqr lndsalrdli nchvykkygp ealagnqayp slleaqedvl lldaqaqakd
      601 sedaakveak eppsqspntp lqrlvegygp agkilldleq alssegtqen kvkplllqlq
      661 rqpqpflalm qsldtpetnr tlhltvlril kqlvdfpeal llpwheavda cmaclrspnt
      721 drevlqelif flhrltsvsr dyavvlnqlg ardaiskale khlgklelaq elrdmvfkce
      781 khahlyrkli tnilggciqm vlgqiedhrr thqpinipff dvflrylcqg ssvevkedkc
      841 wekvevssnp hraskltdhn pktywesngs agshyitlhm rrgilirqlt llvasedssy
      901 mparvvvcgg dstsslhtel nsvnvmpsas rvillenltr fwpiiqirik rcqqggidtr
      961 irgleilgpk ptfwpvfreq lcrhtrlfym vraqawsqdm aedrrsllhl ssrlngalrq
     1021 eqnfadrflp ddeaaqalgk tcwealvspv vqnitspded gisplgwlld qylecqeavf
     1081 npqsrgpaff srvrrlthll vhvepceapp pvvatprpkg rnrshdwssl atrglpssim
     1141 rnltrcwrav vekqvnnflt sswrdddfvp rycehfnilq nssselfgpr aafllalqng
     1201 cagallklpf lkaahvseqf arhidqqiqg sriggaqeme rlaqlqqclq avlifsglei
     1261 attfehyyqh ymadrllgvv sswlegavle qigpcfpnrl pqqmlqslst skelqrqfhv
     1321 yqlqqldqel lkledtekki qvglgasgke hksekeeeag aaavvdvaeg eeeeeenedl
     1381 yyegampevs vlvlsrhswp vasichtlnp rtclpsylrg tlnrysnfyn ksqshpaler
     1441 gsqrrlqwtw lgwaelqfgn qtlhvstvqm wlllylndlk avsvesllaf sglsadmlnq
     1501 aigpltssrg pldlheqkdi pggvlkirdg skeprsrwdi vrlippqtyl qaegedgqnl
     1561 ekrrnllncl ivrilkahgd eglhidqlvc lvleawqkgp cpprglvssl gkgsacsstd
     1621 vlscilhllg kgtlrrhddr pqvlsyavpv tvmephtesl npgssgpnpp ltfhtlqirs
     1681 rgvpyascta tqsfstfr
//
LOCUS       NP_001381591             306 aa            linear   PRI 21-NOV-2025
DEFINITION  low-density lipoprotein receptor class A domain-containing protein
            4 isoform alpha 1 [Homo sapiens].
ACCESSION   NP_001381591 XP_024307017
VERSION     NP_001381591.1
DBSOURCE    REFSEQ: accession NM_001394662.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Xie,W., Xiao,H., Luo,J., Zhao,L., Jin,F., Ma,J., Li,J., Xiong,K.,
            Chen,C. and Wang,G.
  TITLE     Identification of low-density lipoprotein receptor class A domain
            containing 4 (LDLRAD4) as a prognostic indicator in primary
            gastrointestinal stromal tumors
  JOURNAL   Curr Probl Cancer 44 (6), 100593 (2020)
   PUBMED   32507364
  REMARK    GeneRIF: Identification of low-density lipoprotein receptor class A
            domain containing 4 (LDLRAD4) as a prognostic indicator in primary
            gastrointestinal stromal tumors.
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 306)
  AUTHORS   Meerabux,J.M., Ohba,H., Iwayama,Y., Maekawa,M.,
            Detera-Wadleigh,S.D., DeLisi,L.E. and Yoshikawa,T.
  TITLE     Analysis of a t(18;21)(p11.1;p11.1) translocation in a family with
            schizophrenia
  JOURNAL   J Hum Genet 54 (7), 386-391 (2009)
   PUBMED   19461657
REFERENCE   7  (residues 1 to 306)
  AUTHORS   Kikuchi,M., Yamada,K., Toyota,T. and Yoshikawa,T.
  TITLE     C18orf1 located on chromosome 18p11.2 may confer susceptibility to
            schizophrenia
  JOURNAL   J Med Dent Sci 50 (3), 225-229 (2003)
   PUBMED   15074360
REFERENCE   8  (residues 1 to 306)
  AUTHORS   Yoshikawa,T., Sanders,A.R., Esterling,L.E. and Detera-Wadleigh,S.D.
  TITLE     Multiple transcriptional variants and RNA editing in C18orf1, a
            novel gene with LDLRA and transmembrane domains on 18p11.2
  JOURNAL   Genomics 47 (2), 246-257 (1998)
   PUBMED   9479497
REFERENCE   9  (residues 1 to 306)
  AUTHORS   Esterling,L.E., Cox Matise,T., Sanders,A.R., Yoshikawa,T.,
            Overhauser,J., Gershon,E.S., Moskowitz,M.T. and
            Detera-Wadleigh,S.D.
  TITLE     An integrated physical map of 18p11.2: a susceptibility region for
            bipolar disorder
  JOURNAL   Mol Psychiatry 2 (6), 501-504 (1997)
   PUBMED   9399696
REFERENCE   10 (residues 1 to 306)
  AUTHORS   Yoshikawa,T., Sanders,A.R., Esterling,L.E., Overhauser,J.,
            Garnes,J.A., Lennon,G., Grewal,R. and Detera-Wadleigh,S.D.
  TITLE     Isolation of chromosome 18-specific brain transcripts as positional
            candidates for bipolar disorder
  JOURNAL   Am J Med Genet 74 (2), 140-149 (1997)
   PUBMED   9129712
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP002505.3, AP002439.3 and AP001010.4.
            
            On Apr 28, 2021 this sequence version replaced XP_024307017.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2144487.1,
                                           SRR14038192.3498576.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.21"
     Protein         1..306
                     /product="low-density lipoprotein receptor class A
                     domain-containing protein 4 isoform alpha 1"
                     /note="clone 22; low-density lipoprotein receptor class A
                     domain-containing protein 4"
                     /calculated_mol_wt=33769
     Region          16..47
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(17,25,37..38)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(30,33,37,43..44)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            40..44
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            65..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15165.1)"
     Region          180..183
                     /region_name="PPxY motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O15165.1)"
     Region          208..211
                     /region_name="SMAD interaction motif (SIM)"
                     /note="propagated from UniProtKB/Swiss-Prot (O15165.1)"
     Region          252..255
                     /region_name="PPxY motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O15165.1)"
     Region          286..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15165.1)"
     CDS             1..306
                     /gene="LDLRAD4"
                     /gene_synonym="C18orf1"
                     /coded_by="NM_001394662.1:590..1510"
                     /note="isoform alpha 1 is encoded by transcript variant
                     11"
                     /db_xref="CCDS:CCDS32793.1"
                     /db_xref="GeneID:753"
                     /db_xref="HGNC:HGNC:1224"
                     /db_xref="MIM:606571"
ORIGIN      
        1 mpeagfqatn afteckftct sgkclylgsl vcnqqndcgd nsdeencllv tehpppgifn
       61 selefaqiii ivvvvtvmvv vivcllnhyk vstrsfinrp nqsrrredgl pqegclwpsd
      121 saaprlgase imhaprsrdr ftapsfiqrd rfsrfqptyp yvqheidlpp tislsdgeep
      181 ppyqgpctlq lrdpeqqmel nresvrappn rtifdsdlid iamysggpcp pssnsgisas
      241 tcssngrmeg ppptysevmg hhpgasflhh qrsnahrgsr lqfqqnnaes tivpikgkdr
      301 kpgnlv
//
LOCUS       NP_001363218             507 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase PAK 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001363218
VERSION     NP_001363218.1
DBSOURCE    REFSEQ: accession NM_001376289.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Kervarrec,T., Westphal,D., Pissaloux,D., Legrand,M., Tirode,F.,
            Neuhart,A., Drouot,F., Becker,J.C., Macagno,N., Seris,A.,
            Jouary,T., Beltzung,F., Jullie,M.L., Harms,P.W., Cribier,B.,
            Mourah,S., Jouenne,F., Fromont,G., Louveau,B., Mancini,M.,
            Kazakov,D.V., de la Fouchardiere,A. and Battistella,M.
  TITLE     Porocarcinomas with PAK1/2/3 fusions: a series of 12 cases
  JOURNAL   Histopathology 85 (4), 566-578 (2024)
   PUBMED   38785043
  REMARK    GeneRIF: Porocarcinomas with PAK1/2/3 fusions: a series of 12
            cases.
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Zhao,P., Zhang,J., Song,W., Qi,D., Huang,Y., Su,Y., Wu,R., Zhang,L.
            and Zhang,S.
  TITLE     Incarvine C and its analogues inhibit the formation of cell
            cytoskeleton by targeting Rac1
  JOURNAL   Bioorg Chem 149, 107512 (2024)
   PUBMED   38833990
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Xu,M.H., Zheng,Y.M., Liang,B.G., Xu,W.X., Cao,J., Wang,P.,
            Dong,Z.Y., Zhou,C.H., Sun,H.C., Ren,N., Ke,A.W. and Shen,Y.H.
  TITLE     Deubiquitination of CIB1 by USP14 promotes lenvatinib resistance
            via the PAK1-ERK1/2 axis in hepatocellular carcinoma
  JOURNAL   Int J Biol Sci 20 (9), 3269-3284 (2024)
   PUBMED   38993552
  REMARK    GeneRIF: Deubiquitination of CIB1 by USP14 promotes lenvatinib
            resistance via the PAK1-ERK1/2 axis in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Luo,Q., Raulston,E.G., Prado,M.A., Wu,X., Gritsman,K., Whalen,K.S.,
            Yan,K., Booth,C.A.G., Xu,R., van Galen,P., Doench,J.G., Shimony,S.,
            Long,H.W., Neuberg,D.S., Paulo,J.A. and Lane,A.A.
  TITLE     Targetable leukaemia dependency on noncanonical PI3Kgamma
            signalling
  JOURNAL   Nature 630 (8015), 198-205 (2024)
   PUBMED   38720074
  REMARK    GeneRIF: Targetable leukaemia dependency on noncanonical PI3Kgamma
            signalling.
REFERENCE   6  (residues 1 to 507)
  AUTHORS   Manser,E., Huang,H.Y., Loo,T.H., Chen,X.Q., Dong,J.M., Leung,T. and
            Lim,L.
  TITLE     Expression of constitutively active alpha-PAK reveals effects of
            the kinase on actin and focal complexes
  JOURNAL   Mol Cell Biol 17 (3), 1129-1143 (1997)
   PUBMED   9032240
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Bokoch,G.M., Wang,Y., Bohl,B.P., Sells,M.A., Quilliam,L.A. and
            Knaus,U.G.
  TITLE     Interaction of the Nck adapter protein with p21-activated kinase
            (PAK1)
  JOURNAL   J Biol Chem 271 (42), 25746-25749 (1996)
   PUBMED   8824201
REFERENCE   8  (residues 1 to 507)
  AUTHORS   Brown,J.L., Stowers,L., Baer,M., Trejo,J., Coughlin,S. and Chant,J.
  TITLE     Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase
            pathway
  JOURNAL   Curr Biol 6 (5), 598-605 (1996)
   PUBMED   8805275
REFERENCE   9  (residues 1 to 507)
  AUTHORS   Martin,G.A., Bollag,G., McCormick,F. and Abo,A.
  TITLE     A novel serine kinase activated by rac1/CDC42Hs-dependent
            autophosphorylation is related to PAK65 and STE20
  JOURNAL   EMBO J 14 (9), 1970-1978 (1995)
   PUBMED   7744004
  REMARK    Erratum:[EMBO J. 1995 Sep 1;14(17):4385. doi:
            10.1002/j.1460-2075.1995.tb00113.x. PMID: 7556080]
REFERENCE   10 (residues 1 to 507)
  AUTHORS   Manser,E., Leung,T., Salihuddin,H., Zhao,Z.S. and Lim,L.
  TITLE     A brain serine/threonine protein kinase activated by Cdc42 and Rac1
  JOURNAL   Nature 367 (6458), 40-46 (1994)
   PUBMED   8107774
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000486.6.
            
            Summary: This gene encodes a family member of serine/threonine
            p21-activating kinases, known as PAK proteins. These proteins are
            critical effectors that link RhoGTPases to cytoskeleton
            reorganization and nuclear signaling, and they serve as targets for
            the small GTP binding proteins Cdc42 and Rac. This specific family
            member regulates cell motility and morphology. Mutations in this
            gene have been associated with macrocephaly, seizures, and speech
            delay. Overexpression of this gene is also reported in many cancer
            types, and particularly in breast cancer. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.94914.1,
                                           SRR14038194.1997701.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.5-q14.1"
     Protein         1..507
                     /product="serine/threonine-protein kinase PAK 1 isoform 5"
                     /EC_number="2.7.11.1"
                     /note="p21/Cdc42/Rac1-activated kinase 1 (yeast
                     Ste20-related); p21/Cdc42/Rac1-activated kinase 1 (STE20
                     homolog, yeast); serine/threonine-protein kinase PAK 1;
                     p21 protein (Cdc42/Rac)-activated kinase 1"
                     /calculated_mol_wt=56282
     Region          1..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB and autocatalysis.
                     /evidence=ECO:0000269|PubMed:14585966,
                     ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          70..140
                     /region_name="Autoregulatory region.
                     /evidence=ECO:0000269|PubMed:22153498"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Region          74..132
                     /region_name="PBD"
                     /note="P21-Rho-binding domain; pfam00786"
                     /db_xref="CDD:395634"
     Site            order(75,78,81,83,86,103,107)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238526"
     Region          75..105
                     /region_name="GTPase-binding.
                     /evidence=ECO:0000269|PubMed:22153498"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by OXSR1.
                     /evidence=ECO:0000250|UniProtKB:P35465; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20417602,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000269|PubMed:17726028,
                     ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          159..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17989089,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20417602; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000269|PubMed:17726028; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          211..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17989089,
                     ECO:0000269|PubMed:23260667, ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88643; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88643; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          262..471
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(276..279,282,284,297,299,328,344..347,389,393..394,
                     396,406..407)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000269|PubMed:17726028,
                     ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis, BRSK2 and
                     PDPK1. /evidence=ECO:0000269|PubMed:10551809,
                     ECO:0000269|PubMed:10995762, ECO:0000269|PubMed:22153498,
                     ECO:0000269|PubMed:22669945; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     CDS             1..507
                     /gene="PAK1"
                     /gene_synonym="alpha-PAK; IDDMSSD; p65-PAK; PAKalpha"
                     /coded_by="NM_001376289.1:220..1743"
                     /note="isoform 5 is encoded by transcript variant 24"
                     /db_xref="GeneID:5058"
                     /db_xref="HGNC:HGNC:8590"
                     /db_xref="MIM:602590"
ORIGIN      
        1 msnngldiqd kppappmrnt stmigagskd agtlnhgskp lppnpeekkk kdrfyrsilp
       61 gdktnkkkek erpeislpsd fehtihvgfd avtgeftgmp eqwarllqts nitkseqkkn
      121 pqavldvlef ynskktsnsq kymsftdksa edynssnaln vkavsetpav ppvsededdd
      181 dddatpppvi aprpehtksv ytrsvieplp vtptrdvats pisptenntt ppdaltrnte
      241 kqkkkpkmsd eeileklrsi vsvgdpkkky trfekigqga sgtvytamdv atgqevaikq
      301 mnlqqqpkke liineilvmr enknpnivny ldsylvgdel wvvmeylagg sltdvvtetc
      361 mdegqiaavc reclqalefl hsnqvihrdi ksdnillgmd gsvkltdfgf caqitpeqsk
      421 rstmvgtpyw mapevvtrka ygpkvdiwsl gimaiemieg eppylnenpl rvrklrfqvf
      481 snfsmiaasi pedcqaplqp hstdccs
//
LOCUS       NP_078865                287 aa            linear   PRI 21-NOV-2025
DEFINITION  protein rogdi homolog [Homo sapiens].
ACCESSION   NP_078865
VERSION     NP_078865.1
DBSOURCE    REFSEQ: accession NM_024589.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Gowda,V.K., Bylappa,A.Y., Srinivasan,V.M., Manohar,V. and Pandey,H.
  TITLE     Kohlschutter-Tonz syndrome (amelo-cerebro-hypohidrotic syndrome) in
            an Indian family with a novel ROGD1 mutation
  JOURNAL   Clin Dysmorphol 32 (4), 168-171 (2023)
   PUBMED   37646740
  REMARK    GeneRIF: Kohlschutter-Tonz syndrome (amelo-cerebro-hypohidrotic
            syndrome) in an Indian family with a novel ROGD1 mutation.
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Jaskolka,M.C., Winkley,S.R. and Kane,P.M.
  TITLE     RAVE and Rabconnectin-3 Complexes as Signal Dependent Regulators of
            Organelle Acidification
  JOURNAL   Front Cell Dev Biol 9, 698190 (2021)
   PUBMED   34249946
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Sugis,E., Dauvillier,J., Leontjeva,A., Adler,P., Hindie,V.,
            Moncion,T., Collura,V., Daudin,R., Loe-Mie,Y., Herault,Y.,
            Lambert,J.C., Hermjakob,H., Pupko,T., Rain,J.C., Xenarios,I.,
            Vilo,J., Simonneau,M. and Peterson,H.
  TITLE     HENA, heterogeneous network-based data set for Alzheimer's disease
  JOURNAL   Sci Data 6 (1), 151 (2019)
   PUBMED   31413325
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Tucci,A., Kara,E., Schossig,A., Wolf,N.I., Plagnol,V., Fawcett,K.,
            Paisan-Ruiz,C., Moore,M., Hernandez,D., Musumeci,S., Tennison,M.,
            Hennekam,R., Palmeri,S., Malandrini,A., Raskin,S., Donnai,D.,
            Hennig,C., Tzschach,A., Hordijk,R., Bast,T., Wimmer,K., Lo,C.N.,
            Shorvon,S., Mefford,H., Eichler,E.E., Hall,R., Hayes,I., Hardy,J.,
            Singleton,A., Zschocke,J. and Houlden,H.
  TITLE     Kohlschutter-Tonz syndrome: mutations in ROGDI and evidence of
            genetic heterogeneity
  JOURNAL   Hum Mutat 34 (2), 296-300 (2013)
   PUBMED   23086778
  REMARK    GeneRIF: We identify novel compound heterozygous ROGDI mutations in
            five typical Kohlschutter-Tonz syndrome families. Other families
            were negative for ROGDI mutations, suggesting genetic heterogeneity
            of atypical forms of the disease.
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Mory,A., Dagan,E., Illi,B., Duquesnoy,P., Mordechai,S., Shahor,I.,
            Romani,S., Hawash-Moustafa,N., Mandel,H., Valente,E.M., Amselem,S.
            and Gershoni-Baruch,R.
  TITLE     A nonsense mutation in the human homolog of Drosophila rogdi causes
            Kohlschutter-Tonz syndrome
  JOURNAL   Am J Hum Genet 90 (4), 708-714 (2012)
   PUBMED   22482807
  REMARK    GeneRIF: Homozygosity mapping localized the gene linked to
            Kohlschutter-Tonz syndrome to a 586,513 bp region (with a LOD score
            of 6.4) in chromosomal region 16p13.3. The nonsense mutation was
            homozygous in all affected individuals.
REFERENCE   8  (residues 1 to 287)
  AUTHORS   Schossig,A., Wolf,N.I., Fischer,C., Fischer,M., Stocker,G.,
            Pabinger,S., Dander,A., Steiner,B., Tonz,O., Kotzot,D.,
            Haberlandt,E., Amberger,A., Burwinkel,B., Wimmer,K., Fauth,C.,
            Grond-Ginsbach,C., Koch,M.J., Deichmann,A., von Kalle,C.,
            Bartram,C.R., Kohlschutter,A., Trajanoski,Z. and Zschocke,J.
  TITLE     Mutations in ROGDI Cause Kohlschutter-Tonz Syndrome
  JOURNAL   Am J Hum Genet 90 (4), 701-707 (2012)
   PUBMED   22424600
  REMARK    GeneRIF: The finding that ROGDI mutations cause Kohlschutter-Tonz
            Syndrome indicates that the protein product of this gene plays an
            important role in neuronal development as well as amelogenesis.
REFERENCE   9  (residues 1 to 287)
  AUTHORS   Camargo,L.M., Collura,V., Rain,J.C., Mizuguchi,K., Hermjakob,H.,
            Kerrien,S., Bonnert,T.P., Whiting,P.J. and Brandon,N.J.
  TITLE     Disrupted in Schizophrenia 1 Interactome: evidence for the close
            connectivity of risk genes and a potential synaptic basis for
            schizophrenia
  JOURNAL   Mol Psychiatry 12 (1), 74-86 (2007)
   PUBMED   17043677
REFERENCE   10 (residues 1 to 287)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020663.1, BC012901.2 and
            AA740842.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the functional protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026039.1, AL136675.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322048.12/ ENSP00000322832.6
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..287
                     /product="protein rogdi homolog"
                     /note="leucine zipper domain protein; rogdi homolog"
                     /calculated_mol_wt=32123
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9GZN7.1)"
     Region          18..276
                     /region_name="Rogdi_lz"
                     /note="Rogdi leucine zipper containing protein; pfam10259"
                     /db_xref="CDD:463031"
     CDS             1..287
                     /gene="ROGDI"
                     /gene_synonym="KTZS; RAV2; ROGD1"
                     /coded_by="NM_024589.3:63..926"
                     /db_xref="CCDS:CCDS10523.1"
                     /db_xref="GeneID:79641"
                     /db_xref="HGNC:HGNC:29478"
                     /db_xref="MIM:614574"
ORIGIN      
        1 matvmaataa eravleeefr wllhdevhav lkqlqdilke aslrftlpgs gtegpakqen
       61 filgscgtdq vkgvltlqgd alsqadvnlk mprnnqllhf afredkqwkl qqiqdarnhv
      121 sqaiylltsr dqsyqfktga evlklmdavm lqltrarnrl ttpatltlpe iaasgltrmf
      181 apalpsdllv nvyinlnklc ltvyqlhalq pnstknfrpa ggavlhspga mfewgsqrle
      241 vshvhkvecv ipwlndalvy ftvslqlcqq lkdkisvfss ywsyrpf
//
LOCUS       NP_001185951            1012 aa            linear   PRI 21-NOV-2025
DEFINITION  centriolar coiled-coil protein of 110 kDa isoform 1 [Homo sapiens].
ACCESSION   NP_001185951
VERSION     NP_001185951.2
DBSOURCE    REFSEQ: accession NM_001199022.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Iyer,S.S., Chen,F., Ogunmolu,F.E., Moradi,S., Volkov,V.A., van
            Grinsven,E.J., van Hoorn,C., Wu,J., Andrea,N., Hua,S., Jiang,K.,
            Vakonakis,I., Potocnjak,M., Herzog,F., Gigant,B., Gudimchuk,N.,
            Stecker,K.E., Dogterom,M., Steinmetz,M.O. and Akhmanova,A.
  TITLE     Centriolar cap proteins CP110 and CPAP control slow elongation of
            microtubule plus ends
  JOURNAL   J Cell Biol 224 (3) (2025)
   PUBMED   39847124
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Xie,S., Naslavsky,N. and Caplan,S.
  TITLE     Emerging insights into CP110 removal during early steps of
            ciliogenesis
  JOURNAL   J Cell Sci 137 (4) (2024)
   PUBMED   38415788
  REMARK    GeneRIF: Emerging insights into CP110 removal during early steps of
            ciliogenesis.
            Review article
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Xie,S., Naslavsky,N. and Caplan,S.
  TITLE     EHD1 promotes CP110 ubiquitination by centriolar satellite delivery
            of HERC2 to the mother centriole
  JOURNAL   EMBO Rep 24 (6), e56317 (2023)
   PUBMED   37074924
  REMARK    GeneRIF: EHD1 promotes CP110 ubiquitination by centriolar satellite
            delivery of HERC2 to the mother centriole.
REFERENCE   4  (residues 1 to 1012)
  AUTHORS   Wang,Y., Zhang,Y., Guo,X., Zheng,Y., Zhang,X., Feng,S. and Wu,H.Y.
  TITLE     CCP5 and CCP6 retain CP110 and negatively regulate ciliogenesis
  JOURNAL   BMC Biol 21 (1), 124 (2023)
   PUBMED   37226238
  REMARK    GeneRIF: CCP5 and CCP6 retain CP110 and negatively regulate
            ciliogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1012)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   6  (residues 1 to 1012)
  AUTHORS   Casenghi,M., Meraldi,P., Weinhart,U., Duncan,P.I., Korner,R. and
            Nigg,E.A.
  TITLE     Polo-like kinase 1 regulates Nlp, a centrosome protein involved in
            microtubule nucleation
  JOURNAL   Dev Cell 5 (1), 113-125 (2003)
   PUBMED   12852856
REFERENCE   7  (residues 1 to 1012)
  AUTHORS   Chen,Z., Indjeian,V.B., McManus,M., Wang,L. and Dynlacht,B.D.
  TITLE     CP110, a cell cycle-dependent CDK substrate, regulates centrosome
            duplication in human cells
  JOURNAL   Dev Cell 3 (3), 339-350 (2002)
   PUBMED   12361598
  REMARK    GeneRIF: CP110, a cell cycle-dependent CDK substrate, regulates
            centrosome duplication (CP110)
REFERENCE   8  (residues 1 to 1012)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   9  (residues 1 to 1012)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   10 (residues 1 to 1012)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY798911.2, CR749255.1, AC012621.8, CN307903.1, CN307908.1,
            DA250590.1, BQ632514.1 and BC036654.2.
            
            On Apr 22, 2016 this sequence version replaced NP_001185951.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749255.1, SRR1803614.205351.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.3"
     Protein         1..1012
                     /product="centriolar coiled-coil protein of 110 kDa
                     isoform 1"
                     /note="centrosomal protein CP110; centrosomal protein of
                     110 kDa; centriolar coiled-coil protein of 110 kDa;
                     centriolar coiled-coil protein 110kDa"
                     /calculated_mol_wt=113293
     Region          1..223
                     /region_name="CEP97 binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Region          29..106
                     /region_name="CaM_bind"
                     /note="Calcium-dependent calmodulin binding; pfam16025"
                     /db_xref="CDD:464981"
     Region          64..82
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Region          67..82
                     /region_name="Required for interaction with CEP290.
                     /evidence=ECO:0000269|PubMed:18694559"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:26304236; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000305|PubMed:26304236; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Region          350..565
                     /region_name="Interaction with CEP76.
                     /evidence=ECO:0000269|PubMed:19460342"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSH4; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSH4; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Region          611..633
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Region          <638..>704
                     /region_name="Stathmin"
                     /note="Stathmin family; pfam00836"
                     /db_xref="CDD:459956"
     Region          <639..>808
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          781..821
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Region          909..924
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Region          949..992
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     CDS             1..1012
                     /gene="CCP110"
                     /gene_synonym="Cep110; CP110"
                     /coded_by="NM_001199022.3:163..3201"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS55992.1"
                     /db_xref="GeneID:9738"
                     /db_xref="HGNC:HGNC:24342"
                     /db_xref="MIM:609544"
ORIGIN      
        1 meeyekfcek slariqeasl stesflpaqs esislirfhg vailspllni ekrkemqqek
       61 qkaldveark qvnrkkallt rvqeildnvq vrkapnasdf dqwemetvys nsevrnlnvp
      121 atfpnsfpsh tehstaakld kiagilpldn edqcktdgid lardsegfns pkqcdssnis
      181 hveneafpkt ssatpqetli sdgpfsvneq qdlpllaevi pdpyvmslqn lmkkskeyie
      241 reqsrrslrg sinrivnesh ldkehdavev adcvkekgql tgkhcvsvip dkpslnksnv
      301 llqgastqas smsmpvlasf skvdipirtg hptvlesnsd fkviptfvte nnviksltgs
      361 yaklpspeps mspkmhrrrs rtssachili nnpinacels pkgkeqamdl iiqdtdentn
      421 vpeimpklpt dlagvcsskv yvgkntsevk edvvlgksnq vcqssgnhle nkvthglvtv
      481 egqltsderg ahimnstcaa mpklhepyas sqciaspnfg tvsglkpasm lekncslqte
      541 lnksydvknp spllmqnqnt rqqmdtpmvs cgneqfldns fekvkrrldl didglqkenc
      601 pyvitsgite qerqhlpekr ypkgsgfvnk nkmlgtsske seellkskml afeemrkrle
      661 eqhaqqlsll iaeqereqer lqkeieeqek mlkekkamta easeldinna velewrkisd
      721 sslletmlsq adslhtsnsn ssgftnsamq ysfvsaneap fylwgsstsg ltklsvtrpf
      781 graktrwsqv fsleiqakfn kitavakgfl trrlmqtdkl kqlrqtvkdt mefirsfqse
      841 aplkrgivsa qdaslqervl aqlraalygi hdiffvmdaa ermsilhhdr evrkekmlrq
      901 mdkmksprva lsaatqksld rkkymkaaem gmpnkkflvk qnpsetrvlq pnqgqnapvh
      961 rllsrqgtpk tsvkgvvqnr qkpsqsrvpn rvpvsgvyag kiqrkrpnva ti
//
LOCUS       NP_001277152            1886 aa            linear   PRI 21-NOV-2025
DEFINITION  dedicator of cytokinesis protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001277152 XP_006717744
VERSION     NP_001277152.2
DBSOURCE    REFSEQ: accession NM_001290223.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1886)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1886)
  AUTHORS   Najafi,S., Hashemi-Gorji,F., Roudgari,H., Goudarzi,M.,
            Jafarzadegan,A.M. and Sheykhbahaei,N.
  TITLE     Genetic change investigation in DOCK1 gene in an Iranian family
            with sign and symptoms of temporomandibular joint disorder (TMD)
  JOURNAL   Clin Oral Investig 28 (8), 432 (2024)
   PUBMED   39020145
  REMARK    GeneRIF: Genetic change investigation in DOCK1 gene in an Iranian
            family with sign and symptoms of temporomandibular joint disorder
            (TMD).
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1886)
  AUTHORS   Liu,D., Dredge,B.K., Bert,A.G., Pillman,K.A., Toubia,J., Guo,W.,
            Dyakov,B.J.A., Migault,M.M., Conn,V.M., Conn,S.J., Gregory,P.A.,
            Gingras,A.C., Patel,D., Wu,B. and Goodall,G.J.
  TITLE     ESRP1 controls biogenesis and function of a large abundant
            multiexon circRNA
  JOURNAL   Nucleic Acids Res 52 (3), 1387-1403 (2024)
   PUBMED   38015468
  REMARK    GeneRIF: ESRP1 controls biogenesis and function of a large abundant
            multiexon circRNA.
REFERENCE   4  (residues 1 to 1886)
  AUTHORS   Xu,Y., Liu,X., Zeng,W., Zhu,Y., Dong,J., Wu,F., Chen,C., Sharma,S.
            and Lin,Y.
  TITLE     DOCK1 insufficiency disrupts trophoblast function and pregnancy
            outcomes via DUSP4-ERK pathway
  JOURNAL   Life Sci Alliance 7 (2), e202302247 (2023)
   PUBMED   37967942
  REMARK    GeneRIF: DOCK1 insufficiency disrupts trophoblast function and
            pregnancy outcomes via DUSP4-ERK pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1886)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 1886)
  AUTHORS   Wu,Y.C. and Horvitz,H.R.
  TITLE     C. elegans phagocytosis and cell-migration protein CED-5 is similar
            to human DOCK180
  JOURNAL   Nature 392 (6675), 501-504 (1998)
   PUBMED   9548255
REFERENCE   7  (residues 1 to 1886)
  AUTHORS   Savill,J.
  TITLE     Apoptosis. Phagocytic docking without shocking
  JOURNAL   Nature 392 (6675), 442-443 (1998)
   PUBMED   9548247
REFERENCE   8  (residues 1 to 1886)
  AUTHORS   Takai,S., Hasegawa,H., Kiyokawa,E., Yamada,K., Kurata,T. and
            Matsuda,M.
  TITLE     Chromosomal mapping of the gene encoding DOCK180, a major
            Crk-binding protein, to 10q26.13-q26.3 by fluorescence in situ
            hybridization
  JOURNAL   Genomics 35 (2), 403-404 (1996)
   PUBMED   8661160
REFERENCE   9  (residues 1 to 1886)
  AUTHORS   Matsuda,M., Ota,S., Tanimura,R., Nakamura,H., Matuoka,K.,
            Takenawa,T., Nagashima,K. and Kurata,T.
  TITLE     Interaction between the amino-terminal SH3 domain of CRK and its
            natural target proteins
  JOURNAL   J Biol Chem 271 (24), 14468-14472 (1996)
   PUBMED   8662907
REFERENCE   10 (residues 1 to 1886)
  AUTHORS   Hasegawa,H., Kiyokawa,E., Tanaka,S., Nagashima,K., Gotoh,N.,
            Shibuya,M., Kurata,T. and Matsuda,M.
  TITLE     DOCK180, a major CRK-binding protein, alters cell morphology upon
            translocation to the cell membrane
  JOURNAL   Mol Cell Biol 16 (4), 1770-1776 (1996)
   PUBMED   8657152
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607029.17, BX470155.5,
            BX470201.4, AL359094.14, AL390920.22, AL157711.12 and AL355316.12.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 21, 2020 this sequence version replaced NP_001277152.1.
            
            Summary: This gene encodes a member of the dedicator of cytokinesis
            protein family. Dedicator of cytokinesis proteins act as guanine
            nucleotide exchange factors for small Rho family G proteins. The
            encoded protein regulates the small GTPase Rac, thereby influencing
            several biological processes, including phagocytosis and cell
            migration. Overexpression of this gene has also been associated
            with certain cancers. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Mar 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC144632.1, SRR11853567.4596.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000623213.2/ ENSP00000485033.1
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1886
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.2"
     Protein         1..1886
                     /product="dedicator of cytokinesis protein 1 isoform 1"
                     /note="DOwnstream of CrK; 180 kDa protein downstream of
                     CRK"
                     /calculated_mol_wt=217623
     Region          13..68
                     /region_name="SH3_DOCK1_5_A"
                     /note="Src Homology 3 domain of Class A Dedicator of
                     Cytokinesis proteins 1 and 5; cd12051"
                     /db_xref="CDD:212984"
     Site            order(15..19,26,31..33,35,39..40,44..45,47,55,57,59,61,
                     63..64,66,68)
                     /site_type="other"
                     /note="ELMO interaction site [polypeptide binding]"
                     /db_xref="CDD:212984"
     Site            order(18,20,23,27,44..45,61,63..64)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212984"
     Region          76..437
                     /region_name="DOCK_N"
                     /note="DOCK N-terminus; pfam16172"
                     /db_xref="CDD:465040"
     Region          445..640
                     /region_name="C2_Dock-A"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class A proteins; cd08694"
                     /db_xref="CDD:176076"
     Region          1235..1633
                     /region_name="DHR2_DOCK1"
                     /note="Dock Homology Region 2, a GEF domain, of Class A
                     Dedicator of Cytokinesis 1; cd11707"
                     /db_xref="CDD:212580"
     Site            order(1319,1326..1328,1330,1332..1333,1335..1336,
                     1339..1340,1342..1343,1346..1347,1350,1437,1440..1443,
                     1446)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:212580"
     Site            order(1385,1387..1390,1406..1408,1425..1427,1460..1463,
                     1474..1475,1478,1517,1521,1541..1542,1544..1545,
                     1549..1550,1553..1559,1562,1592,1608,1610..1611,1614,1617)
                     /site_type="other"
                     /note="Rac binding site [polypeptide binding]"
                     /db_xref="CDD:212580"
     Site            1553..1558
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212580"
     Region          1640..1737
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14185.2)"
     Site            1702
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14185.2)"
     Region          1708..1716
                     /region_name="Phosphoinositide-binding.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14185.2)"
     Region          1753..1886
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14185.2)"
     Site            1764
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q14185.2)"
     Site            1772
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14185.2)"
     Site            1777
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q14185.2)"
     Site            1782
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q14185.2)"
     Site            1785
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q14185.2)"
     Site            1788
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q14185.2)"
     Site            1793
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q14185.2)"
     Region          1814..1840
                     /region_name="Interaction with NCK2 second and third SH3
                     domain (minor)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14185.2)"
     Region          1820..1826
                     /region_name="SH3-binding, interaction with CRK.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14185.2)"
     Region          1841..1857
                     /region_name="Interaction with NCK2 third SH3 domain
                     (major)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14185.2)"
     Region          1858..1873
                     /region_name="Interaction with NCK2 (minor)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14185.2)"
     Region          1859..1864
                     /region_name="SH3-binding, interaction with CRK.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14185.2)"
     Site            1879
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BUR4; propagated from
                     UniProtKB/Swiss-Prot (Q14185.2)"
     CDS             1..1886
                     /gene="DOCK1"
                     /gene_synonym="ced5; DOCK180"
                     /coded_by="NM_001290223.2:91..5751"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS76359.1"
                     /db_xref="GeneID:1793"
                     /db_xref="HGNC:HGNC:2987"
                     /db_xref="MIM:601403"
ORIGIN      
        1 mtrwvptkre ekygvafyny dargadelsl qigdtvhile tyegwyrgyt lrkkskkgif
       61 pasyihlkea ivegkgqhet vipgdlpliq evtttlrews tiwrqlyvqd nremfrsvrh
      121 miydliewrs qilsgtlpqd elkelkkkvt akidygnril dldlvvrded gnildpelts
      181 tislfrahei askqveerlq eeksqkqnid inrqakfaat pslalfvnlk nvvckigeda
      241 evlmslydpv eskfisenyl vrwsssglpk didrlhnlra vftdlgskdl krekisfvcq
      301 ivrvgrmelr dnntrkltsg lrrpfgvavm dvtdiingkv ddedkqhfip fqplalddai
      361 rhkplnmssr fsprvagend flqtvinkvi aakevnhkgq glwvtlkllp gdihqirkef
      421 phlvdrttav arktgfpeii mpgdvrndiy vtlvqgdfdk gskttaknve vtvsvydedg
      481 krlehvifpg agdeaiseyk sviyyqvkqp rwfetvkvai piedvnrshl rftfrhrssq
      541 dskdksekif alafvklmry dgttlrdgeh dlivykaeak kledaatyls lpstkaelee
      601 kghsatgksm qslgsctisk dsfqistlvc stkltqnvdl lgllkwrsnt sllqqnlrql
      661 mkvdggevvk flqdtldalf nimmensese tfdtlvfdal vfiigliadr kfqhfnpvle
      721 tyikkhfsat laytkltkvl knyvdgaekp gvneqlykam kalesifkfi vrsrilfnql
      781 yenkgeadfv esllqlfrsi ndmmssmsdq tvrvkgaalk ylptivndvk lvfdpkelsk
      841 mftefilnvp mglltiqkly clieivhsdl ftqhdcreil lpmmtdqlky hlerqedlea
      901 ccqllshile vlyrkdvgpt qrhvqiimek llrtvnrtvi smgrdselig nfvacmtail
      961 rqmedyhyah liktfgkmrt dvvdflmetf imfknligkn vypfdwvimn mvqnkvflra
     1021 inqyadmlnk kfldqanfel qlwnnyfhla vafltqeslq lenfssakra kilnkygdmr
     1081 rqigfeirdm wynlgqhkik fipemvgpil emtlipetel rkatipiffd mmqcefhstr
     1141 sfqmfeneii tkldhevegg rgdeqykvlf dkillehcrk hkylaktget fvklvvrlme
     1201 rlldyrtimh denkenrmsc tvnvlnfyke iereemyiry lyklcdlhke cdnyteaayt
     1261 lllhakllkw sedvcvahlt qrdgyqattq gqlkeqlyqe iihyfdkgkm weeaialgke
     1321 laeqyenemf dyeqlsellk kqaqfyeniv kvirpkpdyf avgyygqgfp tflrgkvfiy
     1381 rgkeyerred fearlltqfp naekmkttsp pgddiknspg qyiqcftvkp kldlppkfhr
     1441 pvseqivsfy rvnevqrfey srpirkgekn pdnefanmwi ertiyttayk lpgilrwfev
     1501 ksvfmveisp lenaietmql tndkinsmvq qhlddpslpi nplsmllngi vdpavmggfa
     1561 nyekafftdr ylqehpeahe kieklkdlia wqipflaegi rihgdkvtea lrpfhermea
     1621 cfkqlkekve keygvrimps slddrrgsrp rsmvrsftmp sssrplsvas vsslssdstp
     1681 srpgsdgfal epllpkkmhs rsqdkldkdd lekekkdkkk ekrnskhqei fekefkptdi
     1741 slqqseavil setisplrpq rpksqvmnvi gserrfsvsp sspssqqtpp pvtpraklsf
     1801 smqsslelng mtgadvadvp pplplkgsva dygnlmenqd llgsptpppp pphqrhlppp
     1861 lpsktppppp pkttrkqasv dsgivq
//
LOCUS       NP_000961                288 aa            linear   PRI 21-NOV-2025
DEFINITION  large ribosomal subunit protein eL6 isoform 1 [Homo sapiens].
ACCESSION   NP_000961
VERSION     NP_000961.2
DBSOURCE    REFSEQ: accession NM_000970.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Kennedy,S.A., Jarboui,M.A., Srihari,S., Raso,C., Bryan,K.,
            Dernayka,L., Charitou,T., Bernal-Llinares,M., Herrera-Montavez,C.,
            Krstic,A., Matallanas,D., Kotlyar,M., Jurisica,I., Curak,J.,
            Wong,V., Stagljar,I., LeBihan,T., Imrie,L., Pillai,P., Lynn,M.A.,
            Fasterius,E., Al-Khalili Szigyarto,C., Breen,J., Kiel,C.,
            Serrano,L., Rauch,N., Rukhlenko,O., Kholodenko,B.N.,
            Iglesias-Martinez,L.F., Ryan,C.J., Pilkington,R., Cammareri,P.,
            Sansom,O., Shave,S., Auer,M., Horn,N., Klose,F., Ueffing,M.,
            Boldt,K., Lynn,D.J. and Kolch,W.
  TITLE     Extensive rewiring of the EGFR network in colorectal cancer cells
            expressing transforming levels of KRASG13D
  JOURNAL   Nat Commun 11 (1), 499 (2020)
   PUBMED   31980649
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Wei,J., Kishton,R.J., Angel,M., Conn,C.S., Dalla-Venezia,N.,
            Marcel,V., Vincent,A., Catez,F., Ferre,S., Ayadi,L., Marchand,V.,
            Dersh,D., Gibbs,J.S., Ivanov,I.P., Fridlyand,N., Coute,Y.,
            Diaz,J.J., Qian,S.B., Staudt,L.M., Restifo,N.P. and Yewdell,J.W.
  TITLE     Ribosomal Proteins Regulate MHC Class I Peptide Generation for
            Immunosurveillance
  JOURNAL   Mol Cell 73 (6), 1162-1173 (2019)
   PUBMED   30712990
  REMARK    GeneRIF: 60S ribosomal proteins L6 (RPL6) and RPL28, which are
            adjacent on the ribosome, play opposite roles in generating an
            influenza A virus-encoded peptide. Depleting RPL6 decreases
            ubiquitin-dependent peptide presentation, whereas depleting RPL28
            increases ubiquitin-dependent and -independent peptide
            presentation.
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Ohta,K., Endo,T., Gunji,K. and Onaya,T.
  TITLE     Isolation of a cDNA whose expression is markedly increased in
            malignantly transformed FRTL cells and neoplastic human thyroid
            tissues
  JOURNAL   J Mol Endocrinol 12 (1), 85-92 (1994)
   PUBMED   8185817
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Zaman,G.J.
  TITLE     Sequence of a cDNA encoding human ribosomal protein L26 and of a
            cDNA probably encoding human ribosomal protein L6
  JOURNAL   Nucleic Acids Res 21 (7), 1673 (1993)
   PUBMED   8479925
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Morita,T., Sato,T., Nyunoya,H., Tsujimoto,A., Takahara,J., Irino,S.
            and Shimotohno,K.
  TITLE     Isolation of a cDNA clone encoding DNA-binding protein (TAXREB107)
            that binds specifically to domain C of the tax-responsive enhancer
            element in the long terminal repeat of human T-cell leukemia virus
            type I
  JOURNAL   AIDS Res Hum Retroviruses 9 (2), 115-121 (1993)
   PUBMED   8457378
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Nika,H. and Hultin,T.
  TITLE     Location of the sulfhydryl groups involved in disulfide interaction
            between the neighboring proteins L6 and L29 in mammalian ribosomes.
            S-cleavage of the cyanylated proteins in polyacrylamide gels after
            separation by dodecylsulfate gel electrophoresis
  JOURNAL   Eur J Biochem 142 (3), 521-526 (1984)
   PUBMED   6468376
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Todokoro,K., Ulbrich,N., Chan,Y.L. and Wool,I.G.
  TITLE     Characterization of the binding of rat liver ribosomal proteins L6,
            L8, L19, S9, and S13 to 5.8 S ribosomal ribonucleic acid
  JOURNAL   J Biol Chem 256 (14), 7207-7212 (1981)
   PUBMED   7251593
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BC004138.2 and AI583261.1.
            
            On Nov 6, 2001 this sequence version replaced NP_000961.1.
            
            Summary: This gene encodes a protein component of the 60S ribosomal
            subunit. This protein can bind specifically to domain C of the
            tax-responsive enhancer element of human T-cell leukemia virus type
            1, and may participate in tax-mediated transactivation of
            transcription. As is typical for genes encoding ribosomal proteins,
            there are multiple processed pseudogenes of this gene dispersed
            throughout the genome. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (2) is the predominant variant.
            Variants 1, 2, 3, 4, 5, 6, and 7 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC020679.1, AK311863.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155974 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000202773.14/ ENSP00000202773.9
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.13"
     Protein         1..288
                     /product="large ribosomal subunit protein eL6 isoform 1"
                     /note="60S ribosomal protein L6; tax-responsive enhancer
                     element-binding protein 107; DNA-binding protein
                     TAXREB107; neoplasm-related protein C140; large ribosomal
                     subunit protein eL6"
                     /calculated_mol_wt=32597
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02878.3)"
     Region          36..95
                     /region_name="Ribosomal_L6e_N"
                     /note="Ribosomal protein L6, N-terminal domain; pfam03868"
                     /db_xref="CDD:427554"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679; propagated from
                     UniProtKB/Swiss-Prot (Q02878.3)"
     Region          136..288
                     /region_name="KOW_RPL6"
                     /note="KOW motif of Ribosomal Protein L6; cd13156"
                     /db_xref="CDD:240520"
     Site            order(136,138,154..158,160,171..172,179..183,185,187..190,
                     192..193,219,243,246..247,269,272..274,278..279)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:240520"
     Site            239
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q02878.3)"
     CDS             1..288
                     /gene="RPL6"
                     /gene_synonym="eL6; L6; SHUJUN-2; TAXREB107; TXREB1"
                     /coded_by="NM_000970.6:20..886"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9162.1"
                     /db_xref="GeneID:6128"
                     /db_xref="HGNC:HGNC:10362"
                     /db_xref="MIM:603703"
ORIGIN      
        1 magekvekpd tkekkpeakk vdaggkvkkg nlkakkpkkg kphcsrnpvl vrgigrysrs
       61 amysrkamyk rkysaakskv ekkkkekvla tvtkpvggdk nggtrvvklr kmpryypted
      121 vprkllshgk kpfsqhvrkl rasitpgtil iiltgrhrgk rvvflkqlas glllvtgplv
      181 lnrvplrrth qkfviatstk idisnvkipk hltdayfkkk klrkprhqeg eifdtekeky
      241 eiteqrkidq kavdsqilpk ikaipqlqgy lrsvfaltng iyphklvf
//
LOCUS       NP_001365544            1620 aa            linear   PRI 21-NOV-2025
DEFINITION  coiled-coil and C2 domain-containing protein 2A isoform a [Homo
            sapiens].
ACCESSION   NP_001365544 XP_005248234
VERSION     NP_001365544.1
DBSOURCE    REFSEQ: accession NM_001378615.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1620)
  AUTHORS   Harion,M., Qebibo,L., Riquet,A., Rougeot,C., Afenjar,A., Garel,C.,
            Louha,M., Lacaze,E., Audic-Gerard,F., Barth,M., Berquin,P.,
            Bonneau,D., Bourdain,F., Busa,T., Colin,E., Cuisset,J.M., Des
            Portes,V., Dorison,N., Francannet,C., Heron,B., Laroche,C.,
            Lebrun,M., Metreau,J., Odent,S., Pasquier,L., Trujillo,Y.P.,
            Perrin,L., Pinson,L., Rivier,F., Sigaudy,S., Thauvin-Robinet,C.,
            Louvier,U.W., Labayle,O., Rodriguez,D., Valence,S. and Burglen,L.
  TITLE     New insights into CC2D2A-related Joubert syndrome
  JOURNAL   J Med Genet 60 (6), 578-586 (2023)
   PUBMED   36319078
  REMARK    GeneRIF: New insights into CC2D2A-related Joubert syndrome.
REFERENCE   2  (residues 1 to 1620)
  AUTHORS   Cabrita Pinto,R.L., Viaggi,S., Canale,E., Martinez Popple,M.,
            Capra,V., Conteduca,G., Testa,B., Coviello,D. and Covone,A.E.
  TITLE     Exome Analysis Reveals Novel Missense and Deletion Variants in the
            CC2D2A Gene as Causative of Joubert Syndrome
  JOURNAL   Genes (Basel) 14 (4), 810 (2023)
   PUBMED   37107568
  REMARK    GeneRIF: Exome Analysis Reveals Novel Missense and Deletion
            Variants in the CC2D2A Gene as Causative of Joubert Syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1620)
  AUTHORS   Barroso-Gil,M., Olinger,E., Ramsbottom,S.A., Molinari,E.,
            Miles,C.G. and Sayer,J.A.
  TITLE     Update of genetic variants in CEP120 and CC2D2A-With an emphasis on
            genotype-phenotype correlations, tissue specific transcripts and
            exploring mutation specific exon skipping therapies
  JOURNAL   Mol Genet Genomic Med 9 (12), e1603 (2021)
   PUBMED   33486889
  REMARK    GeneRIF: Update of genetic variants in CEP120 and CC2D2A-With an
            emphasis on genotype-phenotype correlations, tissue specific
            transcripts and exploring mutation specific exon skipping
            therapies.
REFERENCE   4  (residues 1 to 1620)
  AUTHORS   Khan,M.I., Latif,M., Saif,M., Ahmad,H., Khan,A.U., Naseer,M.I.,
            Hussain,H.M.J. and Jelani,M.
  TITLE     Whole exome sequencing identified a novel missense alteration in
            CC2D2A causing Joubert syndrome 9 in a Pakhtun family
  JOURNAL   J Gene Med 23 (1), e3279 (2021)
   PUBMED   32989887
  REMARK    GeneRIF: Whole exome sequencing identified a novel missense
            alteration in CC2D2A causing Joubert syndrome 9 in a Pakhtun
            family.
REFERENCE   5  (residues 1 to 1620)
  AUTHORS   Noor,A., Windpassinger,C., Patel,M., Stachowiak,B., Mikhailov,A.,
            Azam,M., Irfan,M., Paterson,A.D., Lutufullah,M., Doherty,D.,
            Vincent,J.B. and Ayub,M.
  TITLE     Addendum. CC2D2A, encoding a coiled-coil and C2 domain protein,
            causes autosomal-recessive mental retardation with retinitis
            pigmentosa
  JOURNAL   Am J Hum Genet 83 (5), 656 (2008)
   PUBMED   19068953
  REMARK    GeneRIF: CC2D2A causes autosomal-recessive mental retardation with
            retinitis pigmentosa.
REFERENCE   6  (residues 1 to 1620)
  AUTHORS   Gorden,N.T., Arts,H.H., Parisi,M.A., Coene,K.L., Letteboer,S.J.,
            van Beersum,S.E., Mans,D.A., Hikida,A., Eckert,M., Knutzen,D.,
            Alswaid,A.F., Ozyurek,H., Dibooglu,S., Otto,E.A., Liu,Y.,
            Davis,E.E., Hutter,C.M., Bammler,T.K., Farin,F.M., Dorschner,M.,
            Topcu,M., Zackai,E.H., Rosenthal,P., Owens,K.N., Katsanis,N.,
            Vincent,J.B., Hildebrandt,F., Rubel,E.W., Raible,D.W., Knoers,N.V.,
            Chance,P.F., Roepman,R., Moens,C.B., Glass,I.A. and Doherty,D.
  TITLE     CC2D2A is mutated in Joubert syndrome and interacts with the
            ciliopathy-associated basal body protein CEP290
  JOURNAL   Am J Hum Genet 83 (5), 559-571 (2008)
   PUBMED   18950740
  REMARK    GeneRIF: CC2D2A is mutated in Joubert syndrome and interacts with
            the ciliopathy-associated basal body protein CEP290.
REFERENCE   7  (residues 1 to 1620)
  AUTHORS   Tallila,J., Jakkula,E., Peltonen,L., Salonen,R. and Kestila,M.
  TITLE     Identification of CC2D2A as a Meckel syndrome gene adds an
            important piece to the ciliopathy puzzle
  JOURNAL   Am J Hum Genet 82 (6), 1361-1367 (2008)
   PUBMED   18513680
  REMARK    GeneRIF: CC2D2A appears to have at least two cilia-related
            functions: the molecule seems to be a part of the basal body
            complex where the cilium is assembled from and also seems to act as
            a sensor for the intracellular calcium.
REFERENCE   8  (residues 1 to 1620)
  AUTHORS   Noor,A., Windpassinger,C., Patel,M., Stachowiak,B., Mikhailov,A.,
            Azam,M., Irfan,M., Siddiqui,Z.K., Naeem,F., Paterson,A.D.,
            Lutfullah,M., Vincent,J.B. and Ayub,M.
  TITLE     CC2D2A, encoding a coiled-coil and C2 domain protein, causes
            autosomal-recessive mental retardation with retinitis pigmentosa
  JOURNAL   Am J Hum Genet 82 (4), 1011-1018 (2008)
   PUBMED   18387594
  REMARK    GeneRIF: A homozygous splice-site mutation segregating in the
            family with autosomal-recessive mental retardation, within a
            coiled-coil and C2 domain-containing gene, CC2D2A was identified.
REFERENCE   9  (residues 1 to 1620)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 1620)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007016.5 and AC116651.6.
            
            On Feb 26, 2020 this sequence version replaced XP_005248234.1.
            
            Summary: This gene encodes a coiled-coil and calcium binding domain
            protein that appears to play a critical role in cilia formation.
            Mutations in this gene cause Meckel syndrome type 6, as well as
            Joubert syndrome type 9. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853566.20960.1,
                                           SRR11853561.22027.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000424120.6/ ENSP00000403465.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1620
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.32"
     Protein         1..1620
                     /product="coiled-coil and C2 domain-containing protein 2A
                     isoform a"
                     /note="coiled-coil and C2 domain-containing protein 2A"
                     /calculated_mol_wt=186055
     Region          1..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2K1.3)"
     Region          131..383
                     /region_name="DUF5523"
                     /note="Family of unknown function (DUF5523); pfam17661"
                     /db_xref="CDD:465443"
     Region          592..628
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2K1.3)"
     Region          645..819
                     /region_name="CC2D2AN-C2"
                     /note="CC2D2A N-terminal C2 domain; pfam15625"
                     /db_xref="CDD:464780"
     Region          1062..1087
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2K1.3)"
     Region          1066..>1099
                     /region_name="DDA1"
                     /note="Det1 complexing ubiquitin ligase; pfam10172"
                     /db_xref="CDD:401980"
     Region          <1097..>1135
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     CDS             1..1620
                     /gene="CC2D2A"
                     /gene_synonym="COACH2; JBTS9; MKS6; RP93"
                     /coded_by="NM_001378615.1:195..5057"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS47026.1"
                     /db_xref="GeneID:57545"
                     /db_xref="HGNC:HGNC:29253"
                     /db_xref="MIM:612013"
ORIGIN      
        1 mnpreekvki iteefiende dadmgrqnkn skvrrqprkk qpptavpkem vsekshlgnp
       61 qepvqeepkt rllsmtvrrg prslppipst srtgfaefsm rgrmreklqa arskaesall
      121 qeiptprprr lrspskkele tefgtepgke vertqqevds qsysrvkfhd sarkikpkpq
      181 vppgfpsaee aynfftfnfd pepegseekp karhragtnq eeeegeeeep paqgggkemd
      241 eeellngdda edfllgldhv addfvavrpa dyesihdrlq meremlfips rqtvptykkl
      301 penvqprfle deglytgvrp evartnqnim enrllmqdpe rrwfgddgri lalpnpikpf
      361 psrppvltqe qsikaeletl ykkavkyvhs sqhvirsgdp pgnfqldidi sglifthhpc
      421 fsrehvlaak laqlydqyla rhqrnkakfl tdklqalrna vqtgldpekp hqsldtiqkt
      481 ineykseirq trkfrdaeqe kdrtllktii kvwkemkslr efqrftntpl klvlrkekad
      541 qkadeeayea eiqaeisell eehteeyaqk meeyrtslqq wkawrkvqra kkkkrkqaae
      601 ehpgdeiaep ypeedlvkps ppeptdravi eqevreraaq srrrpweptl vpelslagsv
      661 tpndqcprae vsrredvkkr svylkvlfnn kevsrtvsrp lgadfrvhfg qifnlqivnw
      721 pesltlqvye tvghssptll aevflpipet tvvtgrapte evefssnqhv tldhegvgsg
      781 vpfsfeadgs nqltlmtsgk vshsvawaig engiplippl sqqnigfrsa lkkadaissi
      841 gtsgltdmkk lakwaaeskl dpndpnnapl mqlisvatsg esyvpdffrl eqlqqefnfv
      901 sdqelnrskr frllhlrsqe vpefrnykqv pvydreimek vfqdyekrlr drnvietkeh
      961 idthraivak ylqqvresvi nrfliakqyf lladmiveee vpnisilgls lfklaeqkrp
     1021 lrprrkgrkk vtaqnlsdgd ikllvnivra ydipvrkpav skfqqpsrss rmfsekhaas
     1081 pstyspthna dyplgqvlvr pfvevsfqrt vchtttaegp npswneelel pfrapngdys
     1141 taslqsvkdv vfinifdevl hdvleddrer gsgihtrier hwlgcvkmpf stiyfqarid
     1201 gtfkidippv llgyskernm ilergfdsvr slsegsyitl fitiepqlvp gesirekfes
     1261 qedekllqat ekfqaecalk fpnrqclttv idisgktvfi trylkplnpp qellnvypnn
     1321 lqataelvar yvslipflpd tvsfggicdl wstsdqfldl lagdeeehav llcnyflslg
     1381 kkawllmgna ipegptayvl tweqgryliw npcsghfygq fdtfcplknv gcligpdniw
     1441 fniqryespl rinfdvtrpk lwksffsrsl pypglssvqp eeliyqrsdk aaaaelqdri
     1501 ekilkekimd wrprhltrwn ryctstlrhf lplleksqge dveddhrael lkqlgdyrfs
     1561 gfplhmpyse vkplidavys tgvhnidvpn vefalavyih pypknvlsvw iyvaslirnr
//
LOCUS       NP_001317017            1447 aa            linear   PRI 21-NOV-2025
DEFINITION  neurexin-1 isoform alpha11 precursor [Homo sapiens].
ACCESSION   NP_001317017 XP_016860820
VERSION     NP_001317017.1
DBSOURCE    REFSEQ: accession NM_001330088.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1447)
  AUTHORS   Sebastian,R., Jin,K., Pavon,N., Bansal,R., Potter,A., Song,Y.,
            Babu,J., Gabriel,R., Sun,Y., Aronow,B. and Pak,C.
  TITLE     Schizophrenia-associated NRXN1 deletions induce
            developmental-timing- and cell-type-specific vulnerabilities in
            human brain organoids
  JOURNAL   Nat Commun 14 (1), 3770 (2023)
   PUBMED   37355690
  REMARK    GeneRIF: Schizophrenia-associated NRXN1 deletions induce
            developmental-timing- and cell-type-specific vulnerabilities in
            human brain organoids.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1447)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1447)
  AUTHORS   Rhoades,R., Henry,B., Prichett,D., Fang,Y. and Teng,S.
  TITLE     Computational Saturation Mutagenesis to Investigate the Effects of
            Neurexin-1 Mutations on AlphaFold Structure
  JOURNAL   Genes (Basel) 13 (5), 789 (2022)
   PUBMED   35627176
  REMARK    GeneRIF: Computational Saturation Mutagenesis to Investigate the
            Effects of Neurexin-1 Mutations on AlphaFold Structure.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1447)
  AUTHORS   Aksu Uzunhan,T. and Ayaz,A.
  TITLE     Homozygous exonic and intragenic NRXN1 deletion presenting as
            either West syndrome or autism spectrum disorder in two siblings
  JOURNAL   Clin Neurol Neurosurg 214, 107141 (2022)
   PUBMED   35101781
  REMARK    GeneRIF: Homozygous exonic and intragenic NRXN1 deletion presenting
            as either West syndrome or autism spectrum disorder in two
            siblings.
REFERENCE   5  (residues 1 to 1447)
  AUTHORS   Yan,Q., Weyn-Vanhentenryck,S.M., Wu,J., Sloan,S.A., Zhang,Y.,
            Chen,K., Wu,J.Q., Barres,B.A. and Zhang,C.
  TITLE     Systematic discovery of regulated and conserved alternative exons
            in the mammalian brain reveals NMD modulating chromatin regulators
  JOURNAL   Proc Natl Acad Sci U S A 112 (11), 3445-3450 (2015)
   PUBMED   25737549
REFERENCE   6  (residues 1 to 1447)
  AUTHORS   Tabuchi,K. and Sudhof,T.C.
  TITLE     Structure and evolution of neurexin genes: insight into the
            mechanism of alternative splicing
  JOURNAL   Genomics 79 (6), 849-859 (2002)
   PUBMED   12036300
REFERENCE   7  (residues 1 to 1447)
  AUTHORS   Rowen,L., Young,J., Birditt,B., Kaur,A., Madan,A., Philipps,D.L.,
            Qin,S., Minx,P., Wilson,R.K., Hood,L. and Graveley,B.R.
  TITLE     Analysis of the human neurexin genes: alternative splicing and the
            generation of protein diversity
  JOURNAL   Genomics 79 (4), 587-597 (2002)
   PUBMED   11944992
REFERENCE   8  (residues 1 to 1447)
  AUTHORS   Ichtchenko,K., Hata,Y., Nguyen,T., Ullrich,B., Missler,M.,
            Moomaw,C. and Sudhof,T.C.
  TITLE     Neuroligin 1: a splice site-specific ligand for beta-neurexins
  JOURNAL   Cell 81 (3), 435-443 (1995)
   PUBMED   7736595
REFERENCE   9  (residues 1 to 1447)
  AUTHORS   Ullrich,B., Ushkaryov,Y.A. and Sudhof,T.C.
  TITLE     Cartography of neurexins: more than 1000 isoforms generated by
            alternative splicing and expressed in distinct subsets of neurons
  JOURNAL   Neuron 14 (3), 497-507 (1995)
   PUBMED   7695896
REFERENCE   10 (residues 1 to 1447)
  AUTHORS   Ushkaryov,Y.A., Petrenko,A.G., Geppert,M. and Sudhof,T.C.
  TITLE     Neurexins: synaptic cell surface proteins related to the
            alpha-latrotoxin receptor and laminin
  JOURNAL   Science 257 (5066), 50-56 (1992)
   PUBMED   1621094
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007682.3, AC009234.3,
            AC007462.3, AC068725.5, AC069550.4 and AC078994.3.
            
            On Aug 16, 2016 this sequence version replaced XP_016860820.1.
            
            Summary: This gene encodes a single-pass type I membrane protein
            that belongs to the neurexin family. Neurexins are cell-surface
            receptors that bind neuroligins to form Ca(2+)-dependent
            neurexin/neuroligin complexes at synapses in the central nervous
            system. This complex is required for efficient neurotransmission
            and is involved in the formation of synaptic contacts. Three
            members of this gene family have been studied in detail and are
            estimated to generate over 3,000 variants through the use of two
            alternative promoters (alpha and beta) and extensive alternative
            splicing in each family member. Recently, a third promoter (gamma)
            was identified for this gene in the 3' region. Mutations in this
            gene are associated with Pitt-Hopkins-like syndrome-2 and may
            contribute to susceptibility to schizophrenia. [provided by RefSeq,
            Aug 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1660803.3385.1, SRR7410570.155826.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1966682,
                                    SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1447
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.3"
     Protein         1..1447
                     /product="neurexin-1 isoform alpha11 precursor"
                     /note="neurexin I"
                     /calculated_mol_wt=155637
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3097
     Region          30..190
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Region          297..428
                     /region_name="LamG"
                     /note="Laminin G domain; smart00282"
                     /db_xref="CDD:214598"
     Region          485..634
                     /region_name="LamG"
                     /note="Laminin G domain; smart00282"
                     /db_xref="CDD:214598"
     Region          662..695
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          728..849
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          906..1034
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          1129..1247
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          1392..1410
                     /region_name="4.1m"
                     /note="putative band 4.1 homologues' binding motif;
                     smart00294"
                     /db_xref="CDD:128590"
     CDS             1..1447
                     /gene="NRXN1"
                     /gene_synonym="Hs.22998; PTHSL2; SCZD17"
                     /coded_by="NM_001330088.2:1074..5417"
                     /note="isoform alpha11 precursor is encoded by transcript
                     variant alpha11"
                     /db_xref="GeneID:9378"
                     /db_xref="HGNC:HGNC:8008"
                     /db_xref="MIM:600565"
ORIGIN      
        1 mgtallqrgg cfllclslll lgcwaelgsg lefpgaegqw trfpkwnacc esemsfqlkt
       61 rsarglvlyf ddegfcdfle liltrggrlq lsfsifcaep atlladtpvn dgawhsvrir
      121 rqfrnttlfi dqveakwvev kskrrdmtvf sglfvgglpp elraaalklt lasvrerepf
      181 kgwirdvrvn ssqvlpvdsg evklddeppn sgggspceag eegeggvcln ggvcsvvddq
      241 avcdcsrtgf rgkdcsqgla hlmmgdqgke eyiatfkgse yfcydlsqnp iqsssdeitl
      301 sfktlqrngl mlhtgksady vnlalkngav slvinlgsga fealvepvng kfndnawhdv
      361 kvtrnlrqvt isvdgilttt gytqedytml gsddffyvgg spstadlpgs pvsnnfmgcl
      421 kevvyknndv rlelsrlakq gdpkmkihgv vafkcenvat ldpitfetpe sfislpkwna
      481 kktgsisfdf rttepnglil fshgkprhqk dakhpqmikv dffaiemldg hlyllldmgs
      541 gtikikallk kvndgewyhv dfqrdgrsgt isvntlrtpy tapgeseild lddelylggl
      601 penkaglvfp tevwtallny gyvgcirdlf idgqskdirq maevqstagv kpscsketak
      661 pclsnpcknn gmcrdgwnry vcdcsgtgyl grscereatv lsydgsmfmk iqlpvvmhte
      721 aedvslrfrs qraygilmat tsrdsadtlr leldagrvkl tvnlgkgpet lfagynlndn
      781 ewhtvrvvrr gkslkltvdd qqamtgqmag dhtrlefhni etgiiterry lssvpsnfig
      841 hlqsltfngm ayidlckngd idycelnarf gfrniiadpv tfktkssyva latlqaytsm
      901 hlffqfktts ldglilynsg dgndfivvel vkgylhyvfd lgnganlikg ssnkplndnq
      961 whnvmisrdt snlhtvkidt kittqitaga rnldlksdly iggvaketyk slpklvhake
     1021 gfqgclasvd lngrlpdlis dalfcngqie rgcegpsttc qedscsnqgv clqqwdgfsc
     1081 dcsmtsfsgp lcndpgttyi fskgggqity kwppndrpst radrlaigfs tvqkeavlvr
     1141 vdsssglgdy lelhihqgki gvkfnvgtdd iaieesnaii ndgkyhvvrf trsggnatlq
     1201 vdswpviery pagrqltifn sqatiiiggk eqgqpfqgql sglyynglkv lnmaaendan
     1261 iaivgnvrlv gevpssmtte statamqsem stsimetttt latstarrgk pptkepisqt
     1321 tddilvasae cpsddedidp cepssanptr aggrepypgs aeviressst tgmvvgivaa
     1381 aalcililly amykyrnrde gsyhvdesrn yisnsaqsng avvkekqpss akssnknkkn
     1441 kdkeyyv
//
LOCUS       NP_001182606              99 aa            linear   PRI 21-NOV-2025
DEFINITION  vesicle-associated membrane protein-associated protein B/C isoform
            2 [Homo sapiens].
ACCESSION   NP_001182606
VERSION     NP_001182606.1
DBSOURCE    REFSEQ: accession NM_001195677.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 99)
  AUTHORS   James,C., Moller,U., Spillner,C., Konig,S., Dybkov,O., Urlaub,H.,
            Lenz,C. and Kehlenbach,R.H.
  TITLE     Phosphorylation of ELYS promotes its interaction with VAPB at
            decondensing chromosomes during mitosis
  JOURNAL   EMBO Rep 25 (5), 2391-2417 (2024)
   PUBMED   38605278
  REMARK    GeneRIF: Phosphorylation of ELYS promotes its interaction with VAPB
            at decondensing chromosomes during mitosis.
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Markovinovic,A., Martin-Guerrero,S.M., Morotz,G.M., Salam,S.,
            Gomez-Suaga,P., Paillusson,S., Greig,J., Lee,Y., Mitchell,J.C.,
            Noble,W. and Miller,C.C.J.
  TITLE     Stimulating VAPB-PTPIP51 ER-mitochondria tethering corrects FTD/ALS
            mutant TDP43 linked Ca2+ and synaptic defects
  JOURNAL   Acta Neuropathol Commun 12 (1), 32 (2024)
   PUBMED   38395965
  REMARK    GeneRIF: Stimulating VAPB-PTPIP51 ER-mitochondria tethering
            corrects FTD/ALS mutant TDP43 linked Ca[2+] and synaptic defects.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Obara,C.J., Nixon-Abell,J., Moore,A.S., Riccio,F., Hoffman,D.P.,
            Shtengel,G., Xu,C.S., Schaefer,K., Pasolli,H.A., Masson,J.B.,
            Hess,H.F., Calderon,C.P., Blackstone,C. and Lippincott-Schwartz,J.
  TITLE     Motion of VAPB molecules reveals ER-mitochondria contact site
            subdomains
  JOURNAL   Nature 626 (7997), 169-176 (2024)
   PUBMED   38267577
  REMARK    GeneRIF: Motion of VAPB molecules reveals ER-mitochondria contact
            site subdomains.
REFERENCE   5  (residues 1 to 99)
  AUTHORS   Nachreiner,T., Esser,M., Tenten,V., Troost,D., Weis,J. and
            Kruttgen,A.
  TITLE     Novel splice variants of the amyotrophic lateral
            sclerosis-associated gene VAPB expressed in human tissues
  JOURNAL   Biochem Biophys Res Commun 394 (3), 703-708 (2010)
   PUBMED   20227395
  REMARK    GeneRIF: under conditions of proteasomal inhibition, as encountered
            in many neurodegenerative diseases including ALS, variant VAPB
            proteins might accumulate in affected cells and contribute to ALS
            pathogenesis.
REFERENCE   6  (residues 1 to 99)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
REFERENCE   7  (residues 1 to 99)
  AUTHORS   Paumet,F., Le Mao,J., Martin,S., Galli,T., David,B., Blank,U. and
            Roa,M.
  TITLE     Soluble NSF attachment protein receptors (SNAREs) in RBL-2H3 mast
            cells: functional role of syntaxin 4 in exocytosis and
            identification of a vesicle-associated membrane protein
            8-containing secretory compartment
  JOURNAL   J Immunol 164 (11), 5850-5857 (2000)
   PUBMED   10820264
REFERENCE   8  (residues 1 to 99)
  AUTHORS   Bastepe,M., Pincus,J.E. and Juppner,H.
  TITLE     Two frequent tetra-nucleotide repeat polymorphisms between VAPB and
            STX16 on chromosome 20q13
  JOURNAL   Mol Cell Probes 13 (6), 449-451 (1999)
   PUBMED   10657150
REFERENCE   9  (residues 1 to 99)
  AUTHORS   Nishimura,Y., Hayashi,M., Inada,H. and Tanaka,T.
  TITLE     Molecular cloning and characterization of mammalian homologues of
            vesicle-associated membrane protein-associated (VAMP-associated)
            proteins
  JOURNAL   Biochem Biophys Res Commun 254 (1), 21-26 (1999)
   PUBMED   9920726
REFERENCE   10 (residues 1 to 99)
  AUTHORS   Siddique,N. and Siddique,T.
  TITLE     Amyotrophic Lateral Sclerosis Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA450527.1, AF086629.1,
            AL035455.30, AK124571.1 and BM968517.1.
            
            Summary: The protein encoded by this gene is a type IV membrane
            protein found in plasma and intracellular vesicle membranes. The
            encoded protein is found as a homodimer and as a heterodimer with
            VAPA. This protein also can interact with VAMP1 and VAMP2 and may
            be involved in vesicle trafficking. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2, also known as VAPC and VAMPC)
            lacks three exons in the coding region, which results in a
            frameshift and an early stop codon, compared to variant 1. The
            encoded isoform (2, also known as VAPC and VAMPC) is shorter and
            has a distinct C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF086629.1, SRR1803616.41985.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.32"
     Protein         1..99
                     /product="vesicle-associated membrane protein-associated
                     protein B/C isoform 2"
                     /note="VAMP-associated 33 kDa protein; vesicle-associated
                     membrane protein-associated protein B/C; VAMP
                     (vesicle-associated membrane protein)-associated protein B
                     and C"
                     /calculated_mol_wt=11020
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (O95292.3)"
     Region          8..>90
                     /region_name="Motile_Sperm"
                     /note="MSP (Major sperm protein) domain; pfam00635"
                     /db_xref="CDD:459882"
     Site            43
                     /site_type="other"
                     /note="Involved in binding the phosphorylated serine of
                     the phospho-FFAT motif.
                     /evidence=ECO:0000269|PubMed:33124732; propagated from
                     UniProtKB/Swiss-Prot (O95292.3)"
     CDS             1..99
                     /gene="VAPB"
                     /gene_synonym="ALS8; VAMP-B; VAP-B"
                     /coded_by="NM_001195677.2:232..531"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS56198.1"
                     /db_xref="GeneID:9217"
                     /db_xref="HGNC:HGNC:12649"
                     /db_xref="MIM:605704"
ORIGIN      
        1 makveqvlsl epqhelkfrg pftdvvttnl klgnptdrnv cfkvkttapr rycvrpnsgi
       61 idagasinvs grrwtadeed saeqqphfsi spnwegrrp
//
LOCUS       NP_001381336             483 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/arginine-rich splicing factor 11 isoform 2 [Homo sapiens].
ACCESSION   NP_001381336
VERSION     NP_001381336.1
DBSOURCE    REFSEQ: accession NM_001394407.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Oh,J., Oh,J.M. and Cho,S.Y.
  TITLE     METTL3-mediated downregulation of splicing factor SRSF11 is
            associated with carcinogenesis and poor survival of cancer patients
  JOURNAL   Eur Rev Med Pharmacol Sci 27 (6), 2561-2570 (2023)
   PUBMED   37013774
  REMARK    GeneRIF: METTL3-mediated downregulation of splicing factor SRSF11
            is associated with carcinogenesis and poor survival of cancer
            patients.
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Pan,Y.J., Huo,F.C., Kang,M.J., Liu,B.W., Wu,M.D. and Pei,D.S.
  TITLE     Alternative splicing of HSPA12A pre-RNA by SRSF11 contributes to
            metastasis potential of colorectal cancer
  JOURNAL   Clin Transl Med 12 (11), e1113 (2022)
   PUBMED   36394206
  REMARK    GeneRIF: Alternative splicing of HSPA12A pre-RNA by SRSF11
            contributes to metastasis potential of colorectal cancer.
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Manley,J.L. and Krainer,A.R.
  TITLE     A rational nomenclature for serine/arginine-rich protein splicing
            factors (SR proteins)
  JOURNAL   Genes Dev 24 (11), 1073-1074 (2010)
   PUBMED   20516191
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Page-McCaw,P.S., Amonlirdviman,K. and Sharp,P.A.
  TITLE     PUF60: a novel U2AF65-related splicing activity
  JOURNAL   RNA 5 (12), 1548-1560 (1999)
   PUBMED   10606266
REFERENCE   8  (residues 1 to 483)
  AUTHORS   Straub,T., Grue,P., Uhse,A., Lisby,M., Knudsen,B.R., Tange,T.O.,
            Westergaard,O. and Boege,F.
  TITLE     The RNA-splicing factor PSF/p54 controls DNA-topoisomerase I
            activity by a direct interaction
  JOURNAL   J Biol Chem 273 (41), 26261-26264 (1998)
   PUBMED   9756848
REFERENCE   9  (residues 1 to 483)
  AUTHORS   Zhang,W.J. and Wu,J.Y.
  TITLE     Functional properties of p54, a novel SR protein active in
            constitutive and alternative splicing
  JOURNAL   Mol Cell Biol 16 (10), 5400-5408 (1996)
   PUBMED   8816452
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Chaudhary,N., McMahon,C. and Blobel,G.
  TITLE     Primary structure of a human arginine-rich nuclear protein that
            colocalizes with spliceosome components
  JOURNAL   Proc Natl Acad Sci U S A 88 (18), 8189-8193 (1991)
   PUBMED   1896467
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL353771.8.
            
            Summary: This gene encodes 54-kD nuclear protein that contains an
            arginine/serine-rich region similar to segments found in pre-mRNA
            splicing factors. Although the function of this protein is not yet
            known, structure and immunolocalization data suggest that it may
            play a role in pre-mRNA processing. Alternative splicing results in
            multiple transcript variants encoding different proteins. In
            addition, a pseudogene of this gene has been found on chromosome
            12.[provided by RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2363366.1,
                                           SRR14038194.2331933.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.1"
     Protein         1..483
                     /product="serine/arginine-rich splicing factor 11 isoform
                     2"
                     /note="splicing factor, arginine/serine-rich 11; SR
                     splicing factor 11; arginine-rich 54 kDa nuclear protein;
                     splicing factor p54; serine/arginine-rich splicing factor
                     11"
                     /calculated_mol_wt=53283
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05519.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q05519.1)"
     Region          34..113
                     /region_name="RRM_SRSF11"
                     /note="RNA recognition motif (RRM) found in
                     serine/arginine-rich splicing factor 11 (SRSF11) and
                     similar proteins; cd12518"
                     /db_xref="CDD:409940"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q05519.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q05519.1)"
     Region          247..353
                     /region_name="10 X 8 AA approximate repeats of
                     R-R-S-R-S-R-S-R"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05519.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q05519.1)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q05519.1)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q05519.1)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q05519.1)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q05519.1)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q05519.1)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q05519.1)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q05519.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q05519.1)"
     CDS             1..483
                     /gene="SRSF11"
                     /gene_synonym="dJ677H15.2; NET2; p54; SFRS11"
                     /coded_by="NM_001394407.1:44..1495"
                     /note="isoform 2 is encoded by transcript variant 21"
                     /db_xref="CCDS:CCDS53332.1"
                     /db_xref="GeneID:9295"
                     /db_xref="HGNC:HGNC:10782"
                     /db_xref="MIM:602010"
ORIGIN      
        1 msnttvvpst agpgpsggpg gggggggggg gteviqvtnv spsasseqmr tlfgflgkid
       61 elrlfppdds plpvssrvcf vkfhdpdsav vaqhltntvf vdralivvpy aegvipdeak
      121 alsllapana vagllpgggl lptpnpltqi gavplaalga ptldpalaal glpganlnsq
      181 slaadqllkl mstvdpklnh vaaglvspsl ksdtsskeie eamkrvreaq slisaaiepd
      241 kkeekrrhsr srsrsrrrrt psssrhrrsr srsrrrshsk srsrrrsksp rrrrshsrer
      301 grrsrstskt rdkkkedkek krsktppksy starrsrsas rerrrrrsrs gtrspkkprs
      361 pkrklsrsps prrhkkekkk dkdkersrde rerstskkkk skdkekdrer ksesdkdvkv
      421 trdydeeeqg ydsekekkee kkpietgspk tkecsvekgt gdslreskvn gddhheedmd
      481 msd
//
LOCUS       NP_001364184             345 aa            linear   PRI 21-NOV-2025
DEFINITION  pleckstrin homology domain-containing family A member 1 isoform 11
            [Homo sapiens].
ACCESSION   NP_001364184
VERSION     NP_001364184.1
DBSOURCE    REFSEQ: accession NM_001377255.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Huang,Q. and Xiang,Y.
  TITLE     Polymorphisms in Selected Genes and Their Association with
            Age-Related Macular Degeneration in a Chinese Population
  JOURNAL   Med Sci Monit 24, 1693-1700 (2018)
   PUBMED   29565837
  REMARK    GeneRIF: investigated the association of PLEKHA1 958A/G,
            polymorphisms with Age-Related Macular Degeneration (AMD) risk.
            PLEKHA1 958A/G polymorphism was associated with a decreased AMD
            risk (additive model: aOR=0.722, 95% CI=0.450-0.979, P=0.019;
            allele model: aOR=0.883, 95% CI=0.736-0.992, P=0.014)
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Kortvely,E. and Ueffing,M.
  TITLE     Gene Structure of the 10q26 Locus: A Clue to Cracking the
            ARMS2/HTRA1 Riddle?
  JOURNAL   Adv Exp Med Biol 854, 23-29 (2016)
   PUBMED   26427389
  REMARK    GeneRIF: Studies indicate that the high-risk allele of the 10q26
            locus encompasses three genes, PLEKHA1, ARMS2, and HTRA1 with high
            linkage disequilibrium.
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Gupta,D., Gupta,V., Singh,V., Chawla,S., Parveen,F., Agrawal,S. and
            Phadke,S.R.
  TITLE     Study of Polymorphisms in CX3CR1, PLEKHA1 and VEGF genes as risk
            factors for age-related macular degeneration in Indian patients
  JOURNAL   Arch Med Res 45 (6), 489-494 (2014)
   PUBMED   25050486
  REMARK    GeneRIF: CX3CR1 (T280M and V249I) and PLEKHA1 (A320T) polymorphisms
            were not found to be associated with age-related macular
            degeneration in an Indian population.
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Hogan,A., Yakubchyk,Y., Chabot,J., Obagi,C., Daher,E., Maekawa,K.
            and Gee,S.H.
  TITLE     The phosphoinositol 3,4-bisphosphate-binding protein TAPP1
            interacts with syntrophins and regulates actin cytoskeletal
            organization
  JOURNAL   J Biol Chem 279 (51), 53717-53724 (2004)
   PUBMED   15485858
  REMARK    GeneRIF: syntrophins regulate the localization of TAPP1, which may
            be important for remodeling the actin cytoskeleton in response to
            growth factor stimulation
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Kimber,W.A., Deak,M., Prescott,A.R. and Alessi,D.R.
  TITLE     Interaction of the protein tyrosine phosphatase PTPL1 with the
            PtdIns(3,4)P2-binding adaptor protein TAPP1
  JOURNAL   Biochem J 376 (Pt 2), 525-535 (2003)
   PUBMED   14516276
  REMARK    GeneRIF: TAPP1 binds to protein tyrosine phosphatase PTPL1.
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Marshall,A.J., Krahn,A.K., Ma,K., Duronio,V. and Hou,S.
  TITLE     TAPP1 and TAPP2 are targets of phosphatidylinositol 3-kinase
            signaling in B cells: sustained plasma membrane recruitment
            triggered by the B-cell antigen receptor
  JOURNAL   Mol Cell Biol 22 (15), 5479-5491 (2002)
   PUBMED   12101241
REFERENCE   8  (residues 1 to 345)
  AUTHORS   Kimber,W.A., Trinkle-Mulcahy,L., Cheung,P.C., Deak,M.,
            Marsden,L.J., Kieloch,A., Watt,S., Javier,R.T., Gray,A.,
            Downes,C.P., Lucocq,J.M. and Alessi,D.R.
  TITLE     Evidence that the tandem-pleckstrin-homology-domain-containing
            protein TAPP1 interacts with Ptd(3,4)P2 and the
            multi-PDZ-domain-containing protein MUPP1 in vivo
  JOURNAL   Biochem J 361 (Pt 3), 525-536 (2002)
   PUBMED   11802782
REFERENCE   9  (residues 1 to 345)
  AUTHORS   Thomas,C.C., Dowler,S., Deak,M., Alessi,D.R. and van Aalten,D.M.
  TITLE     Crystal structure of the phosphatidylinositol
            3,4-bisphosphate-binding pleckstrin homology (PH) domain of tandem
            PH-domain-containing protein 1 (TAPP1): molecular basis of lipid
            specificity
  JOURNAL   Biochem J 358 (Pt 2), 287-294 (2001)
   PUBMED   11513726
REFERENCE   10 (residues 1 to 345)
  AUTHORS   Dowler,S., Currie,R.A., Campbell,D.G., Deak,M., Kular,G.,
            Downes,C.P. and Alessi,D.R.
  TITLE     Identification of pleckstrin-homology-domain-containing proteins
            with novel phosphoinositide-binding specificities
  JOURNAL   Biochem J 351 (Pt 1), 19-31 (2000)
   PUBMED   11001876
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX664700.3 and BX842242.1.
            
            Summary: This gene encodes a pleckstrin homology domain-containing
            adapter protein. The encoded protein is localized to the plasma
            membrane where it specifically binds phosphatidylinositol
            3,4-bisphosphate. This protein may be involved in the formation of
            signaling complexes in the plasma membrane. Polymorphisms in this
            gene are associated with age-related macular degeneration.
            Alternate splicing results in multiple transcript variants. A
            pseudogene of this gene is found on chromosome 5.[provided by
            RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.83358.1,
                                           SRR14038192.4110707.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..345
                     /product="pleckstrin homology domain-containing family A
                     member 1 isoform 11"
                     /note="tandem PH domain-containing protein 1; pleckstrin
                     homology domain containing, family A (phosphoinositide
                     binding specific) member 1"
                     /calculated_mol_wt=39069
     Region          1..>75
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          137..250
                     /region_name="PH2_TAPP1_2"
                     /note="Tandem PH-domain-containing proteins 1 and 2
                     Pleckstrin homology (PH) domain, C-terminal repeat;
                     cd13271"
                     /db_xref="CDD:270090"
     Site            order(152,154..155,163,174,184..185,217)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270090"
     CDS             1..345
                     /gene="PLEKHA1"
                     /gene_synonym="TAPP1"
                     /coded_by="NM_001377255.1:190..1227"
                     /note="isoform 11 is encoded by transcript variant 27"
                     /db_xref="GeneID:59338"
                     /db_xref="HGNC:HGNC:14335"
                     /db_xref="MIM:607772"
ORIGIN      
        1 mpyvdrqnri cgfldieene nsgkflrryf ildtredsfv wymdnpqnlp sgssrvgaik
       61 ltyiskvpkq sdsqpnsdnl srhgecgkkq vsyrtdivgg vpiitptqke evnecgesid
      121 rnnlkrsqsh lpyftpkppq dsavikagyc vkqgavmknw krryfqlden tigyfksele
      181 keplrviplk evhkvqeckq sdimmrdnlf eivttsrtfy vqadspeemh swikavsgai
      241 vaqrgpgrsa ssmrqarrls npciqrytsr agecstsipp vlqnpntlsv lptqpppphi
      301 pqplaatlws qplpwrsedf tsllprssqg tsrsrlslqe nqlpk
//
LOCUS       NP_002803                350 aa            linear   PRI 21-NOV-2025
DEFINITION  26S proteasome non-ATPase regulatory subunit 8 [Homo sapiens].
ACCESSION   NP_002803
VERSION     NP_002803.2
DBSOURCE    REFSEQ: accession NM_002812.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Li,X., Li,X., Hu,Y., Liu,O., Wang,Y., Li,S., Yang,Q. and Lin,B.
  TITLE     PSMD8 can serve as potential biomarker and therapeutic target of
            the PSMD family in ovarian cancer: based on bioinformatics analysis
            and in vitro validation
  JOURNAL   BMC Cancer 23 (1), 573 (2023)
   PUBMED   37349676
  REMARK    GeneRIF: PSMD8 can serve as potential biomarker and therapeutic
            target of the PSMD family in ovarian cancer: based on
            bioinformatics analysis and in vitro validation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Sahu,I. and Glickman,M.H.
  TITLE     Proteasome in action: substrate degradation by the 26S proteasome
  JOURNAL   Biochem Soc Trans 49 (2), 629-644 (2021)
   PUBMED   33729481
  REMARK    Review article
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Simon,J.H., Gaddis,N.C., Fouchier,R.A. and Malim,M.H.
  TITLE     Evidence for a newly discovered cellular anti-HIV-1 phenotype
  JOURNAL   Nat Med 4 (12), 1397-1400 (1998)
   PUBMED   9846577
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Madani,N. and Kabat,D.
  TITLE     An endogenous inhibitor of human immunodeficiency virus in human
            lymphocytes is overcome by the viral Vif protein
  JOURNAL   J Virol 72 (12), 10251-10255 (1998)
   PUBMED   9811770
REFERENCE   8  (residues 1 to 350)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   9  (residues 1 to 350)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   10 (residues 1 to 350)
  AUTHORS   Kominami,K., DeMartino,G.N., Moomaw,C.R., Slaughter,C.A.,
            Shimbara,N., Fujimuro,M., Yokosawa,H., Hisamatsu,H., Tanahashi,N.,
            Shimizu,Y. et al.
  TITLE     Nin1p, a regulatory subunit of the 26S proteasome, is necessary for
            activation of Cdc28p kinase of Saccharomyces cerevisiae
  JOURNAL   EMBO J 14 (13), 3105-3115 (1995)
   PUBMED   7621825
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005789.1.
            
            On Aug 31, 2007 this sequence version replaced NP_002803.1.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway.  An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            non-ATPase subunit of the 19S regulator. A pseudogene has been
            identified on chromosome 1. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU668354.1, BC001164.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000215071.9/ ENSP00000215071.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..350
                     /product="26S proteasome non-ATPase regulatory subunit 8"
                     /note="26S proteasome regulatory subunit p31; epididymis
                     secretory sperm binding protein Li 91n; 26S proteasome
                     regulatory subunit S14; 26S proteasome regulatory subunit
                     RPN12; proteasome (prosome, macropain) 26S subunit,
                     non-ATPase, 8"
                     /calculated_mol_wt=39481
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48556.2)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P48556.2)"
     Region          201..315
                     /region_name="CSN8_PSD8_EIF3K"
                     /note="CSN8/PSMD8/EIF3K family; pfam10075"
                     /db_xref="CDD:462954"
     CDS             1..350
                     /gene="PSMD8"
                     /gene_synonym="HEL-S-91n; HIP6; HYPF; Nin1p; p31; Rpn12;
                     S14"
                     /coded_by="NM_002812.5:32..1084"
                     /db_xref="CCDS:CCDS12515.2"
                     /db_xref="GeneID:5714"
                     /db_xref="HGNC:HGNC:9566"
                     /db_xref="MIM:617844"
ORIGIN      
        1 mfikgrapra pprerrratr gglrqvvapp ralgstsrph frrasvcrrr crksggllaa
       61 srkmaaaavn gaagfsssgp aatsgavlqa atgmyeqlkg ewnrkspnls kcgeelgrlk
      121 lvllelnflp ttgtkltkqq lilardilei gaqwsilrkd ipsferymaq lkcyyfdyke
      181 qlpesaymhq llglnllfll sqnrvaefht elerlpakdi qtnvyikhpv sleqylmegs
      241 ynkvflakgn ipaesytffi dilldtirde iagciekaye kilfteatri lffntpkkmt
      301 dyakkrgwvl gpnnyysfas qqqkpedtti pstelakqvi eyarqlemiv
//
LOCUS       NP_001381439             911 aa            linear   PRI 21-NOV-2025
DEFINITION  general transcription factor 3C polypeptide 2 isoform b [Homo
            sapiens].
ACCESSION   NP_001381439
VERSION     NP_001381439.1
DBSOURCE    REFSEQ: accession NM_001394510.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Peng,F., Zhou,Y., Wang,J., Guo,B., Wei,Y., Deng,H., Wu,Z.,
            Zhang,C., Shi,K., Li,Y., Wang,X., Shore,P., Zhao,S. and Deng,W.
  TITLE     The transcription factor Sp1 modulates RNA polymerase III gene
            transcription by controlling BRF1 and GTF3C2 expression in human
            cells
  JOURNAL   J Biol Chem 295 (14), 4617-4630 (2020)
   PUBMED   32115405
  REMARK    GeneRIF: The transcription factor Sp1 modulates RNA polymerase III
            gene transcription by controlling BRF1 and GTF3C2 expression in
            human cells.
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 911)
  AUTHORS   Kantidakis,T., Ramsbottom,B.A., Birch,J.L., Dowding,S.N. and
            White,R.J.
  TITLE     mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes,
            and targets their repressor Maf1
  JOURNAL   Proc Natl Acad Sci U S A 107 (26), 11823-11828 (2010)
   PUBMED   20543138
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11465]
REFERENCE   5  (residues 1 to 911)
  AUTHORS   Hirschowitz,E.A., Hiestand,D.M. and Yannelli,J.R.
  TITLE     Vaccines for lung cancer
  JOURNAL   J Thorac Oncol 1 (1), 93-104 (2006)
   PUBMED   17409835
  REMARK    Review article
REFERENCE   6  (residues 1 to 911)
  AUTHORS   Wang,Z. and Roeder,R.G.
  TITLE     DNA topoisomerase I and PC4 can interact with human TFIIIC to
            promote both accurate termination and transcription reinitiation by
            RNA polymerase III
  JOURNAL   Mol Cell 1 (5), 749-757 (1998)
   PUBMED   9660958
REFERENCE   7  (residues 1 to 911)
  AUTHORS   Oettel,S., Hartel,F., Kober,I., Iben,S. and Seifart,K.H.
  TITLE     Human transcription factors IIIC2, IIIC1 and a novel component
            IIIC0 fulfil different aspects of DNA binding to various pol III
            genes
  JOURNAL   Nucleic Acids Res 25 (12), 2440-2447 (1997)
   PUBMED   9171097
REFERENCE   8  (residues 1 to 911)
  AUTHORS   Chu,W.M., Wang,Z., Roeder,R.G. and Schmid,C.W.
  TITLE     RNA polymerase III transcription repressed by Rb through its
            interactions with TFIIIB and TFIIIC2
  JOURNAL   J Biol Chem 272 (23), 14755-14761 (1997)
   PUBMED   9169441
REFERENCE   9  (residues 1 to 911)
  AUTHORS   Sinn,E., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     Cloning and characterization of a TFIIIC2 subunit (TFIIIC beta)
            whose presence correlates with activation of RNA polymerase
            III-mediated transcription by adenovirus E1A expression and serum
            factors
  JOURNAL   Genes Dev 9 (6), 675-685 (1995)
   PUBMED   7729686
REFERENCE   10 (residues 1 to 911)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC074117.7, AC109828.4 and AC013413.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1197338.1,
                                           SRR14038197.2536826.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..911
                     /product="general transcription factor 3C polypeptide 2
                     isoform b"
                     /note="general transcription factor 3C polypeptide 2;
                     TFIIIC 110 kDa subunit; transcription factor IIIC subunit
                     beta; transcription factor IIIC 110 kDa subunit; general
                     transcription factor IIIC, polypeptide 2, beta 110kDa"
                     /calculated_mol_wt=100549
     Region          24..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          <62..255
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          205..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          366..426
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          427..483
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          470..543
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          484..535
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          536..603
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          558..595
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <559..644
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          604..654
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          616..656
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          655..690
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          765..785
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            871
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          889..911
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            892
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            893
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            895
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            901
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     CDS             1..911
                     /gene="GTF3C2"
                     /gene_synonym="TF3C-beta; TFIIIC-BETA; TFIIIC110"
                     /coded_by="NM_001394510.1:789..3524"
                     /note="isoform b is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS1749.1"
                     /db_xref="GeneID:2976"
                     /db_xref="HGNC:HGNC:4665"
                     /db_xref="MIM:604883"
ORIGIN      
        1 mdtcgvgyva lgeagpvgnm tvvdspgqev lnqldvktss emtsaeasve mslptplpgf
       61 edspdqrrlp peqeslsrle qpdlssemsk vskpraskpg rkrggrtrkg pkrpqqpnpp
      121 saplvpglld qsnplstpmp kkrgrkskae llllklskdl drpesqspkr ppedfetpsg
      181 erprrraaqv allylqelae elstalpapv scpegpkvss ptkpkkirqp aacpggeevd
      241 gaprdedffl qveaedvees egpsesssep epvvprstpr gstsgkqkph crgmapnglp
      301 nhimapvwkc lhltkdfreq khsywefaew iplawkwhll seleaapylp qeeksplfsv
      361 qreglpedgt lyrinrfssi tahperwdvs fftggplwal dwcpvpegag asqyvalfss
      421 pdmnethpls qlhsgpgllq lwglgtlqqe scpgnrahfv ygiacdngci wdlkfcpsga
      481 welpgtprka pllprlglla lacsdgkvll fslphpeall aqqppdavkp aiykvqcvat
      541 lqvgsmqatd psecgqclsl awmptrphqh laagyyngmv vfwnlptnsp lqrirlsdgs
      601 lklypfqcfl ahdqavrtlq wckanshflv sagsdrkikf wdlrrpyepi nsikrflste
      661 lawllpyngv tvaqdncyas yglcgihyid agylgfkayf taprkgtvws lsgsdwlgti
      721 aagdisgeli aailpdmaln pinvkrpver rfpiykadli pyqdspegpd hssassgvpn
      781 ppkartytet vnhhyllfqd tdlgsfhdll rrepmlrmqe geghsqlcld rlqleaihkv
      841 rfspnldsyg wlvsggqsgl vrihfvrgla splghrmqle srahfnamfq pssptrrpgf
      901 sptshrllpt p
//
LOCUS       NP_001365513            1217 aa            linear   PRI 21-NOV-2025
DEFINITION  isoleucine--tRNA ligase, cytoplasmic isoform 10 [Homo sapiens].
ACCESSION   NP_001365513
VERSION     NP_001365513.1
DBSOURCE    REFSEQ: accession NM_001378584.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1217)
  AUTHORS   Li,Y., Zhang,Y., Lu,X., Li,R., Peng,J. and Xu,Y.
  TITLE     Circular RNA IARS modulates the progression and ferroptosis of
            osteosarcoma via sponging miR-188-5p from RAB14
  JOURNAL   Neoplasma 71 (3), 279-288 (2024)
   PUBMED   38958715
  REMARK    GeneRIF: Circular RNA IARS modulates the progression and
            ferroptosis of osteosarcoma via sponging miR-188-5p from RAB14.
REFERENCE   2  (residues 1 to 1217)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1217)
  AUTHORS   Khan,K., Baleanu-Gogonea,C., Willard,B., Gogonea,V. and Fox,P.L.
  TITLE     3-Dimensional architecture of the human multi-tRNA synthetase
            complex
  JOURNAL   Nucleic Acids Res 48 (15), 8740-8754 (2020)
   PUBMED   32644155
REFERENCE   4  (residues 1 to 1217)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   5  (residues 1 to 1217)
  AUTHORS   Smigiel,R., Biela,M., Biernacka,A., Stembalska,A., Sasiadek,M.,
            Kosinska,J., Rydzanicz,M. and Ploski,R.
  TITLE     New evidence for association of recessive IARS gene mutations with
            hepatopathy, hypotonia, intellectual disability and growth
            retardation
  JOURNAL   Clin Genet 92 (6), 671-673 (2017)
   PUBMED   29052218
  REMARK    GeneRIF: Our report presents new evidence that recessive mutations
            inIARSgene are associated with characteristic clinical phenotype
            suchas infantile hepatopathy, growth retardation, facial
            dysmorphism,hypotonia, intellectual disability with no speech .
REFERENCE   6  (residues 1 to 1217)
  AUTHORS   Nichols,R.C., Raben,N., Boerkoel,C.F. and Plotz,P.H.
  TITLE     Human isoleucyl-tRNA synthetase: sequence of the cDNA, alternative
            mRNA splicing, and the characteristics of an unusually long
            C-terminal extension
  JOURNAL   Gene 155 (2), 299-304 (1995)
   PUBMED   7721108
REFERENCE   7  (residues 1 to 1217)
  AUTHORS   Lamour,V., Quevillon,S., Diriong,S., N'Guyen,V.C., Lipinski,M. and
            Mirande,M.
  TITLE     Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme
            as a case of horizontal gene transfer
  JOURNAL   Proc Natl Acad Sci U S A 91 (18), 8670-8674 (1994)
   PUBMED   8078941
REFERENCE   8  (residues 1 to 1217)
  AUTHORS   Shiba,K., Suzuki,N., Shigesada,K., Namba,Y., Schimmel,P. and
            Noda,T.
  TITLE     Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence
            of the anticodon-binding domain and acquisition of a new structural
            unit
  JOURNAL   Proc Natl Acad Sci U S A 91 (16), 7435-7439 (1994)
   PUBMED   8052601
REFERENCE   9  (residues 1 to 1217)
  AUTHORS   Kaiser,E., Hu,B., Becher,S., Eberhard,D., Schray,B., Baack,M.,
            Hameister,H. and Knippers,R.
  TITLE     The human EPRS locus (formerly the QARS locus): a gene encoding a
            class I and a class II aminoacyl-tRNA synthetase
  JOURNAL   Genomics 19 (2), 280-290 (1994)
   PUBMED   8188258
REFERENCE   10 (residues 1 to 1217)
  AUTHORS   Norcum,M.T.
  TITLE     Structural analysis of the high molecular mass aminoacyl-tRNA
            synthetase complex. Effects of neutral salts and detergents
  JOURNAL   J Biol Chem 266 (23), 15398-15405 (1991)
   PUBMED   1651330
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136097.10.
            
            Summary: Aminoacyl-tRNA synthetases catalyze the aminoacylation of
            tRNA by their cognate amino acid. Because of their central role in
            linking amino acids with nucleotide triplets contained in tRNAS,
            aminoacyl-tRNA synthetases are thought to be among the first
            proteins that appeared in evolution. Isoleucine-tRNA synthetase
            belongs to the class-I aminoacyl-tRNA synthetase family and has
            been identified as a target of autoantibodies in the autoimmune
            disease polymyositis/dermatomyositis. Alternatively spliced
            transcript variants have been found. [provided by RefSeq, Nov
            2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853564.27451.1,
                                           SRR14372080.2643725.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1217
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.31"
     Protein         1..1217
                     /product="isoleucine--tRNA ligase, cytoplasmic isoform 10"
                     /EC_number="6.1.1.5"
                     /note="isoleucine tRNA ligase 1, cytoplasmic;
                     isoleucine--tRNA ligase, cytoplasmic"
                     /calculated_mol_wt=139389
     Region          6..1046
                     /region_name="PLN02882"
                     /note="aminoacyl-tRNA ligase"
                     /db_xref="CDD:215477"
     CDS             1..1217
                     /gene="IARS1"
                     /gene_synonym="GRIDHH; IARS; ILERS; ILRS; IRS; PRO0785"
                     /coded_by="NM_001378584.1:95..3748"
                     /note="isoform 10 is encoded by transcript variant 20"
                     /db_xref="GeneID:3376"
                     /db_xref="HGNC:HGNC:5330"
                     /db_xref="MIM:600709"
ORIGIN      
        1 mlqqvpenin fpaeeekile fwtefncfqe clkqskhkpk ftfydgppfa tglphyghil
       61 agtikdivtr yahqsgfhvd rrfgwdchgl pveyeidktl girgpedvak mgiteynnqc
      121 raivmrysae wkstvsrlgr widfdndykt lypqfmesvw wvfkqlydkg lvyrgvkvmp
      181 fstacntpls nfeshqnykd vqdpsvfvtf pleedetvsl vawtttpwtl psnlavcvnp
      241 emqyvkikdv argrllilme arlsalykle sdyeilerfp gaylkgkkyr plfdyflkck
      301 engaftvlvd nyvkeeegtg vvhqapyfga edyrvcmdfn iirkdslpvc pvdasgcftt
      361 evtdfagqyv kdadksiirt lkeqgrllva ttfthsypfc wrsdtpliyk avpswfvrve
      421 nmvdqllrnn dlcywvpelv rekrfgnwlk dardwtisrn rywgtpiplw vsddfeevvc
      481 igsvaeleel sgakisdlhr esvdhltips rcgkgslhri sevfdcwfes gsmpyaqvhy
      541 pfenkrefed afpadfiaeg idqtrgwfyt llvlatalfg qppfknvivn glvlasdgqk
      601 mskrkknypd pvsiiqkyga dalrlylins pvvraenlrf keegvrdvlk dvllpwynay
      661 rfliqnvlrl qkeeeiefly nentvrespn itdrwilsfm qsligffete maayrlytvv
      721 prlvkfvdil tnwyvrmnrr rlkgengmed cvmaletlfs vllslcrlmd kdtlsihylm
      781 lprvreelid kktesavsqm qsvielgrvi rdrktipiky plkeivvihq dpealkdiks
      841 lekyiieeln vrkvtlstdk nkygirlrae pdhmvlgkrl kgafkavmts ikqlsseele
      901 qfqktgtivv eghelhdedi rlmytfdqat ggtaqfeahs daqalvlldv tpdqsmvdeg
      961 marevinriq klrkkcnlvp tdeitvyyka ksegtylnsv ieshtefift tikaplkpyp
     1021 vspsdkvliq ektqlkgsel eitltrgssl pgpacayvnl nicangseqg gvlllenpkg
     1081 dnrldllklk svvtsifgvk ntelavfhde tgsapslins sstllcqyin lqllnakpqe
     1141 clmgtvgtll lenplgqngl thqgllyeaa kvfglrsrkl klflnetqtq eitedipvkt
     1201 lnmktvyvsv lpttadf
//
LOCUS       NP_001381603             261 aa            linear   PRI 21-NOV-2025
DEFINITION  ER membrane protein complex subunit 3 [Homo sapiens].
ACCESSION   NP_001381603
VERSION     NP_001381603.1
DBSOURCE    REFSEQ: accession NM_001394674.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Pleiner,T., Tomaleri,G.P., Januszyk,K., Inglis,A.J., Hazu,M. and
            Voorhees,R.M.
  TITLE     Structural basis for membrane insertion by the human ER membrane
            protein complex
  JOURNAL   Science 369 (6502), 433-436 (2020)
   PUBMED   32439656
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Christianson,J.C., Olzmann,J.A., Shaler,T.A., Sowa,M.E.,
            Bennett,E.J., Richter,C.M., Tyler,R.E., Greenblatt,E.J.,
            Harper,J.W. and Kopito,R.R.
  TITLE     Defining human ERAD networks through an integrative mapping
            strategy
  JOURNAL   Nat Cell Biol 14 (1), 93-105 (2011)
   PUBMED   22119785
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Nayak,R.R., Kearns,M., Spielman,R.S. and Cheung,V.G.
  TITLE     Coexpression network based on natural variation in human gene
            expression reveals gene interactions and functions
  JOURNAL   Genome Res 19 (11), 1953-1962 (2009)
   PUBMED   19797678
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC022007.5 and AC018809.5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3704919.1,
                                           SRR14243140.5453352.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000245046.7/ ENSP00000245046.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3"
     Protein         1..261
                     /product="ER membrane protein complex subunit 3"
                     /note="30 kDa protein; partial optokinetic response b;
                     transmembrane protein 111"
                     /calculated_mol_wt=29821
     Region          5..190
                     /region_name="EMC3_TMCO1"
                     /note="Integral membrane protein EMC3/TMCO1-like;
                     pfam01956"
                     /db_xref="CDD:396507"
     Site            15..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0I2.3)"
     Site            115..130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0I2.3)"
     Site            169..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0I2.3)"
     CDS             1..261
                     /gene="EMC3"
                     /gene_synonym="POB; TMEM111"
                     /coded_by="NM_001394674.1:181..966"
                     /db_xref="CCDS:CCDS2594.1"
                     /db_xref="GeneID:55831"
                     /db_xref="HGNC:HGNC:23999"
                     /db_xref="MIM:620273"
ORIGIN      
        1 magpelllds nirlwvvlpi viitffvgmi rhyvsillqs dkkltqeqvs dsqvlirsrv
       61 lrengkyipk qsfltrkyyf nnpedgffkk tkrkvvppsp mtdptmltdm mkgnvtnvlp
      121 miliggwinm tfsgfvttkv pfpltlrfkp mlqqgiellt ldaswvssas wyflnvfglr
      181 siyslilgqd naadqsrmmq eqmtgaamam padtnkafkt ewealeltdh qwalddveee
      241 lmakdlhfeg mfkkelqtsi f
//
LOCUS       NP_001317543            2131 aa            linear   PRI 21-NOV-2025
DEFINITION  dedicator of cytokinesis protein 7 isoform 6 [Homo sapiens].
ACCESSION   NP_001317543 XP_005271349
VERSION     NP_001317543.1
DBSOURCE    REFSEQ: accession NM_001330614.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2131)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2131)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2131)
  AUTHORS   Chen,W., Zhou,M., Guan,B., Xie,B., Liu,Y., He,J., Zhao,J., Zhao,Q.
            and Yan,D.
  TITLE     Tumour-associated macrophage-derived DOCK7-enriched extracellular
            vesicles drive tumour metastasis in colorectal cancer via the
            RAC1/ABCA1 axis
  JOURNAL   Clin Transl Med 14 (2), e1591 (2024)
   PUBMED   38385857
  REMARK    GeneRIF: Tumour-associated macrophage-derived DOCK7-enriched
            extracellular vesicles drive tumour metastasis in colorectal cancer
            via the RAC1/ABCA1 axis.
REFERENCE   4  (residues 1 to 2131)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 2131)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 2131)
  AUTHORS   Nellist,M., Burgers,P.C., van den Ouweland,A.M., Halley,D.J. and
            Luider,T.M.
  TITLE     Phosphorylation and binding partner analysis of the TSC1-TSC2
            complex
  JOURNAL   Biochem Biophys Res Commun 333 (3), 818-826 (2005)
   PUBMED   15963462
REFERENCE   7  (residues 1 to 2131)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   8  (residues 1 to 2131)
  AUTHORS   Brajenovic,M., Joberty,G., Kuster,B., Bouwmeester,T. and Drewes,G.
  TITLE     Comprehensive proteomic analysis of human Par protein complexes
            reveals an interconnected protein network
  JOURNAL   J Biol Chem 279 (13), 12804-12811 (2004)
   PUBMED   14676191
REFERENCE   9  (residues 1 to 2131)
  AUTHORS   Cote,J.F. and Vuori,K.
  TITLE     Identification of an evolutionarily conserved superfamily of
            DOCK180-related proteins with guanine nucleotide exchange activity
  JOURNAL   J Cell Sci 115 (Pt 24), 4901-4913 (2002)
   PUBMED   12432077
REFERENCE   10 (residues 1 to 2131)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC103923.2, AL138847.14,
            AL451044.7 and AC096946.2.
            
            On Aug 30, 2016 this sequence version replaced XP_005271349.1.
            
            Summary: The protein encoded by this gene is a guanine nucleotide
            exchange factor (GEF) that plays a role in axon formation and
            neuronal polarization. The encoded protein displays GEF activity
            toward RAC1 and RAC3 Rho small GTPases but not toward CDC42.
            Several transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Dec 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2131
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..2131
                     /product="dedicator of cytokinesis protein 7 isoform 6"
                     /note="dedicator of cytokinesis protein 7"
                     /calculated_mol_wt=241543
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Region          52..161
                     /region_name="DOCK_C-D_N"
                     /note="Dedicator of cytokinesis C/D, N terminal;
                     pfam11878"
                     /db_xref="CDD:463380"
     Region          138..183
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            381
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1A4; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Region          560..737
                     /region_name="C2_Dock-C"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class C proteins; cd08696"
                     /db_xref="CDD:176078"
     Site            862
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1A4; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            864
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1A4; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            882
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Region          888..971
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            888
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            896
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            900
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            905
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            907
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            909
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            910
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            929
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            964
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1A4; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Region          1635..2109
                     /region_name="DHR2_DOCK7"
                     /note="Dock Homology Region 2, a GEF domain, of Class C
                     Dedicator of Cytokinesis 7; cd11703"
                     /db_xref="CDD:212576"
     Site            order(1790,1800,1802..1803,1805..1806,1809..1810,
                     1812..1813,1816..1817)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:212576"
     Site            order(1832,1834,1857,1860..1863,1865..1866,1885..1887,
                     1904..1906,1934..1937,1947..1948,1951,1953,1990..1991,
                     1994,2010..2011,2013..2014,2017..2019,2022..2024,
                     2027..2028,2031,2059,2081,2084)
                     /site_type="other"
                     /note="Rac/Cdc42 binding site [polypeptide binding]"
                     /db_xref="CDD:212576"
     Site            1953
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            2022..2027
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212576"
     Site            2120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     CDS             1..2131
                     /gene="DOCK7"
                     /gene_synonym="DEE23; EIEE23; ZIR2"
                     /coded_by="NM_001330614.2:123..6518"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS81338.1"
                     /db_xref="GeneID:85440"
                     /db_xref="HGNC:HGNC:19190"
                     /db_xref="MIM:615730"
ORIGIN      
        1 maerrafaqk isrtvaaevr kqisgqysgs pqllknlniv gnishhttvp lteavdpvdl
       61 edylithpla vdsgplrdli efppddievv ysprdcrtlv savpeesemd phvrdcirsy
      121 tedwaivirk yhklgtgfnp ntldkqkerq kglpkqvfes deapdgnsyq ddqddlkrrs
      181 msiddtprgs wacsifdlkn slpdallpnl ldrtpneeid rqnddqrksn rhkelfalhp
      241 spdeeepier lsvpdipkeh fgqrllvkcl slkfeieiep ifaslalydv kekkkisenf
      301 yfdlnseqmk gllrphvppa aittlarsai fsitypsqdv flviklekvl qqgdigecae
      361 pymifkeada tknkeklekl ksqadqfcqr lgkyrmpfaw taihlmnivs sagslerdst
      421 eveistgerk gswserrnss ivgrrslert tsgddacnlt sfrpatltvt nffkqegdrl
      481 sdedlykfla dmrrpssvlr rlrpitaqlk idispapenp hycltpellq vklypdsrvr
      541 ptreilefpa rdvyvpntty rnllyiypqs lnfanrqgsa rnitvkvqfm ygedpsnamp
      601 vifgksscse fskeaytavv yhnrspdfhe eikvklpatl tdhhhllftf yhvscqqkqn
      661 tpletpvgyt wipmlqngrl ktgqfclpvs lekppqaysv lspevplpgm kwvdnhkgvf
      721 nvevvavssi htqdpyldkf falvnaldeh lfpvrigdmr imennlenel kssisalnss
      781 qlepvvrflh llldklillv irppviagqi vnlgqasfea masiinrlhk nlegnhdqhg
      841 rnsllasyih yvfrlpntyp nssspgpggl ggsvhyatma rsavrpasln lnrsrslsns
      901 npdisgtpts pddevrsiig skgldrsnsw vntggpkaap wgsnpspsae stqamdrscn
      961 rmsshtetss flqtltgrlp tkklfheela lqwvvcsgsv resalqqawf ffelmvksmv
     1021 hhlyfndkle aprksrfper fmddiaalvs tiasdivsrf qkdtemverl ntslafflnd
     1081 llsvmdrgfv fslikscykq vssklyslpn psvlvslrld flriicsheh yvtlnlpcsl
     1141 ltppaspsps vssatsqssg fstnvqdqki anmfelsvpf rqqhylaglv ltelavildp
     1201 daeglfglhk kvinmvhnll sshdsdprys dpqikarvam lylpligiim etvpqlydft
     1261 ethnqrgrpi ciatddyese sgsmisqtva maiagtsvpq ltrpgsfllt stsgrqhttf
     1321 saessrslli cllwvlknad etvlqkwftd lsvlqlnrll dllylcvscf eykgkkvfer
     1381 mnsltfkksk dmrakleeai lgsigarqem vrrsrgqler spsgsafgsq enlrwrkdmt
     1441 hwrqntekld ksraeiehea lidgnlatea nliildtlei vvqtvsvtes kesilggvlk
     1501 vllhsmacnq savylqhcfa tqralvskfp ellfeeeteq cadlclrllr hcsssigtir
     1561 shasaslyll mrqnfeignn farvkmqvtm slsslvgtsq nfneeflrrs lktiltyaee
     1621 dlelrettfp dqvqdlvfnl hmilsdtvkm kehqedpeml idlmyriakg yqtspdlrlt
     1681 wlqnmagkhs ersnhaeaaq clvhsaalva eylsmledrk ylpvgcvtfq nissnvlees
     1741 avsddvvspd eegicsgkyf tesglvglle qaaasfsmag myeavnevyk vlipiheanr
     1801 dakklstihg klqeafskiv hqstgwermf gtyfrvgfyg tkfgdldeqe fvykepaitk
     1861 laeishrleg fygerfgedv vevikdsnpv dkckldpnka yiqityvepy fdtyemkdri
     1921 tyfdknynlr rfmyctpftl dgrahgelhe qfkrktiltt shafpyiktr vnvthkeeii
     1981 ltpievaied mqkktqelaf athqdpadpk mlqmvlqgsv gttvnqgple vaqvflseip
     2041 sdpklfrhhn klrlcfkdft krcedalrkn ksligpdqke yqrelernyh rlkealqpli
     2101 nrkipqlyka vlpvtchrds fsrmslrkmd l
//
LOCUS       NP_001128529             587 aa            linear   PRI 21-NOV-2025
DEFINITION  leucine-rich repeat-containing protein 15 isoform a precursor [Homo
            sapiens].
ACCESSION   NP_001128529
VERSION     NP_001128529.2
DBSOURCE    REFSEQ: accession NM_001135057.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Gong,S., Xiang,K., Chen,L., Zhuang,H., Song,Y. and Chen,J.
  TITLE     Integrated bioinformatics analysis identified leucine rich repeat
            containing 15 and secreted phosphoprotein 1 as hub genes for
            calcific aortic valve disease and osteoarthritis
  JOURNAL   IET Syst Biol 18 (3), 77-91 (2024)
   PUBMED   38566328
  REMARK    GeneRIF: Integrated bioinformatics analysis identified leucine rich
            repeat containing 15 and secreted phosphoprotein 1 as hub genes for
            calcific aortic valve disease and osteoarthritis.
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Wang,Q.W., Jia,Y.L., Li,P. and Yu,G.Y.
  TITLE     Effect of LRRC15 on autophagy in A549 cells
  JOURNAL   Yi Chuan 46 (5), 398-407 (2024)
   PUBMED   38763774
  REMARK    GeneRIF: Effect of LRRC15 on autophagy in A549 cells.
REFERENCE   4  (residues 1 to 587)
  AUTHORS   Kim,H.J., Kim,D.J., Kim,S.M. and Jang,Y.J.
  TITLE     Leucine-Rich Repeat Containing 15-Mediated Cell Adhesion Is
            Essential for Integrin Signaling in TGF-beta1-Induced PDL
            Fibroblastic Differentiation
  JOURNAL   Stem Cells 42 (3), 251-265 (2024)
   PUBMED   38051601
  REMARK    GeneRIF: Leucine-Rich Repeat Containing 15-Mediated Cell Adhesion
            Is Essential for Integrin Signaling in TGF-beta1-Induced PDL
            Fibroblastic Differentiation.
REFERENCE   5  (residues 1 to 587)
  AUTHORS   Loo,L., Waller,M.A., Moreno,C.L., Cole,A.J., Stella,A.O., Pop,O.T.,
            Jochum,A.K., Ali,O.H., Denes,C.E., Hamoudi,Z., Chung,F.,
            Aggarwal,A., Low,J.K.K., Patel,K., Siddiquee,R., Kang,T.,
            Mathivanan,S., Mackay,J.P., Jochum,W., Flatz,L., Hesselson,D.,
            Turville,S. and Neely,G.G.
  TITLE     Fibroblast-expressed LRRC15 is a receptor for SARS-CoV-2 spike and
            controls antiviral and antifibrotic transcriptional programs
  JOURNAL   PLoS Biol 21 (2), e3001967 (2023)
   PUBMED   36757924
  REMARK    GeneRIF: Fibroblast-expressed LRRC15 is a receptor for SARS-CoV-2
            spike and controls antiviral and antifibrotic transcriptional
            programs.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 587)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   7  (residues 1 to 587)
  AUTHORS   O'Prey,J., Wilkinson,S. and Ryan,K.M.
  TITLE     Tumor antigen LRRC15 impedes adenoviral infection: implications for
            virus-based cancer therapy
  JOURNAL   J Virol 82 (12), 5933-5939 (2008)
   PUBMED   18385238
  REMARK    GeneRIF: Tumor antigen LRRC15 impedes adenoviral infection:
            implications for virus-based cancer therapy are presented.
REFERENCE   8  (residues 1 to 587)
  AUTHORS   Satoh,K., Hata,M., Shimizu,T., Yokota,H., Akatsu,H., Yamamoto,T.,
            Kosaka,K. and Yamada,T.
  TITLE     Lib, transcriptionally induced in senile plaque-associated
            astrocytes, promotes glial migration through extracellular matrix
  JOURNAL   Biochem Biophys Res Commun 335 (2), 631-636 (2005)
   PUBMED   16098915
  REMARK    GeneRIF: Lib may contribute to regulation of cell-matrix adhesion
            interactions with respect to astrocyte recruitment around senile
            plaques in Alzheimer's disease brain
REFERENCE   9  (residues 1 to 587)
  AUTHORS   Reynolds,P.A., Smolen,G.A., Palmer,R.E., Sgroi,D., Yajnik,V.,
            Gerald,W.L. and Haber,D.A.
  TITLE     Identification of a DNA-binding site and transcriptional target for
            the EWS-WT1(+KTS) oncoprotein
  JOURNAL   Genes Dev 17 (17), 2094-2107 (2003)
   PUBMED   12923058
  REMARK    GeneRIF: LRRC15 is induced by EWS-WT1(+KTS) in the tumor DSRCT and
            may play a role in cellular invasion.
REFERENCE   10 (residues 1 to 587)
  AUTHORS   Satoh,K., Hata,M. and Yokota,H.
  TITLE     A novel member of the leucine-rich repeat superfamily induced in
            rat astrocytes by beta-amyloid
  JOURNAL   Biochem Biophys Res Commun 290 (2), 756-762 (2002)
   PUBMED   11785964
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BK001325.1, BC101064.1 and AC174158.3.
            
            On Feb 5, 2010 this sequence version replaced NP_001128529.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK001325.1, BC101064.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2146982
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..587
                     /product="leucine-rich repeat-containing protein 15
                     isoform a precursor"
                     /note="leucine-rich repeat protein induced by beta
                     amyloid; leucine-rich repeat-containing protein 15; hLib;
                     leucine-rich repeat protein induced by beta-amyloid
                     homolog"
                     /calculated_mol_wt=62314
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2726
     Region          50..449
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          88..108
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          109..156
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          157..180
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          181..204
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          205..228
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          229..252
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          253..276
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          277..300
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          301..324
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          325..348
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          349..370
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          373..393
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          397..418
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..587
                     /gene="LRRC15"
                     /gene_synonym="LIB"
                     /coded_by="NM_001135057.3:126..1889"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS46984.1"
                     /db_xref="GeneID:131578"
                     /db_xref="HGNC:HGNC:20818"
                     /db_xref="MIM:619327"
ORIGIN      
        1 mpldkamplk hyllllvgcq awgaglayhg cpsectcsra sqvectgari vavptplpwn
       61 amslqilnth itelnespfl nisalialri eknelsritp gafrnlgslr ylslannklq
      121 vlpiglfqgl dsleslllss nqllqiqpah fsqcsnlkel qlhgnhleyi pdgafdhlvg
      181 ltklnlgkns lthisprvfq hlgnlqvlrl yenrltdipm gtfdglvnlq elalqqnqig
      241 llspglfhnn hnlqrlylsn nhisqlppsv fmqlpqlnrl tlfgnslkel spgifgpmpn
      301 lrelwlydnh isslpdnvfs nlrqlqvlil srnqisfisp gafngltelr elslhtnalq
      361 dldgnvfrml anlqnislqn nrlrqlpgni fanvnglmai qlqnnqlenl plgifdhlgk
      421 lcelrlydnp wrcdsdilpl rnwlllnqpr lgtdtvpvcf spanvrgqsl iiinvnvavp
      481 svhvpevpsy petpwypdtp sypdttsvss tteltspved ytdlttiqvt ddrsvwgmtq
      541 aqsglaiaai vigivalacs laacvgcccc kkrsqavlmq mkapnec
//
LOCUS       NP_001382411             860 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA-processing factor 40 homolog A isoform 16 [Homo sapiens].
ACCESSION   NP_001382411 XP_016859947
VERSION     NP_001382411.1
DBSOURCE    REFSEQ: accession NM_001395482.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 860)
  AUTHORS   Choudhary,B. and Norris,A.
  TITLE     Conserved role for spliceosomal component PRPF40A in microexon
            splicing
  JOURNAL   RNA 31 (1), 43-50 (2024)
   PUBMED   39389624
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 860)
  AUTHORS   Martinez-Lumbreras,S., Trager,L.K., Mulorz,M.M., Payr,M.,
            Dikaya,V., Hipp,C., Konig,J. and Sattler,M.
  TITLE     Intramolecular autoinhibition regulates the selectivity of PRPF40A
            tandem WW domains for proline-rich motifs
  JOURNAL   Nat Commun 15 (1), 3888 (2024)
   PUBMED   38719828
  REMARK    GeneRIF: Intramolecular autoinhibition regulates the selectivity of
            PRPF40A tandem WW domains for proline-rich motifs.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 860)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 860)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 860)
  AUTHORS   Allen,M., Friedler,A., Schon,O. and Bycroft,M.
  TITLE     The structure of an FF domain from human HYPA/FBP11
  JOURNAL   J Mol Biol 323 (3), 411-416 (2002)
   PUBMED   12381297
  REMARK    GeneRIF: Data describe the structure of an FF domain from
            HYPA/FBP11, which differs from those of other
            phosphopeptide-binding domains and represents a novel
            phosphopeptide-binding fold.
REFERENCE   7  (residues 1 to 860)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   8  (residues 1 to 860)
  AUTHORS   Bedford,M.T., Reed,R. and Leder,P.
  TITLE     WW domain-mediated interactions reveal a spliceosome-associated
            protein that binds a third class of proline-rich motif: the proline
            glycine and methionine-rich motif
  JOURNAL   Proc Natl Acad Sci U S A 95 (18), 10602-10607 (1998)
   PUBMED   9724750
REFERENCE   9  (residues 1 to 860)
  AUTHORS   Faber,P.W., Barnes,G.T., Srinidhi,J., Chen,J., Gusella,J.F. and
            MacDonald,M.E.
  TITLE     Huntingtin interacts with a family of WW domain proteins
  JOURNAL   Hum Mol Genet 7 (9), 1463-1474 (1998)
   PUBMED   9700202
REFERENCE   10 (residues 1 to 860)
  AUTHORS   Chan,D.C., Bedford,M.T. and Leder,P.
  TITLE     Formin binding proteins bear WWP/WW domains that bind proline-rich
            peptides and functionally resemble SH3 domains
  JOURNAL   EMBO J 15 (5), 1045-1054 (1996)
   PUBMED   8605874
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079344.5 and AC012443.8.
            
            On Jul 8, 2021 this sequence version replaced XP_016859947.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q23.3"
     Protein         1..860
                     /product="pre-mRNA-processing factor 40 homolog A isoform
                     16"
                     /note="formin binding protein 3; Huntingtin-interacting
                     protein A; NY-REN-6 antigen; Fas-ligand associated factor
                     1; formin-binding protein 11; huntingtin yeast partner A;
                     fas ligand-associated factor 1; pre-mRNA processing factor
                     40 homolog A; renal carcinoma antigen NY-REN-6;
                     huntingtin-interacting protein 10; PRP40 pre-mRNA
                     processing factor 40 homolog A"
                     /calculated_mol_wt=98401
     Region          54..699
                     /region_name="PRP40"
                     /note="Splicing factor [RNA processing and modification];
                     COG5104"
                     /db_xref="CDD:227435"
     CDS             1..860
                     /gene="PRPF40A"
                     /gene_synonym="FBP-11; FBP11; FLAF1; FNBP3; HIP-10; HIP10;
                     HYPA; NY-REN-6; Prp40"
                     /coded_by="NM_001395482.1:397..2979"
                     /note="isoform 16 is encoded by transcript variant 23"
                     /db_xref="GeneID:55660"
                     /db_xref="HGNC:HGNC:16463"
                     /db_xref="MIM:612941"
ORIGIN      
        1 mllsflgpsv sigpikmpgm mssvmpgmmm shmsqasmqp alppgvnsmd vaagtasgak
       61 smwtehkspd grtyyyntet kqstwekpdd lktpaeqlls kcpwkeyksd sgkpyyynsq
      121 tkesrwakpk eledleamik aeesskqeec tttstapvpt teipttmstm aaaeaaaavv
      181 aaaaaaaaaa aaananasts asntvsgtvp vvpepevtsi vatvvdnent vtisteeqaq
      241 ltstpaiqdq svevssntge etskqetvad ftpkkeeees qpakktytwn tkeeakqafk
      301 ellkekrvps nasweqamkm iindprysal aklsekkqaf naykvqteke ekeearskyk
      361 eakesfqrfl enhekmtstt rykkaeqmfg emevwnaise rdrleiyedv lfflskkeke
      421 qakqlrkrnw ealknildnm anvtysttws eaqqylmdnp tfaedeelqn mdkedalicf
      481 eehiraleke eeeekqksll rerrrqrknr esfqifldel hehgqlhsms swmelyptis
      541 sdirftnmlg qpvfslgsta ldlfkfyved lkaryhdekk iikdilkdkg fvvevnttfe
      601 dfvaiisstk rsttldagni klafnsllek aearererek eearkmkrke safksmlkqa
      661 appieldavw edirerfvke pafeditles erkrifkdfm hvlehecqhh hsknkkhskk
      721 skkhhrkrsr srsgsdsddd dshskkkrqr sesrsasehs ssaesersyk kskkhkkksk
      781 krrhksdspe sdaerekdkk ekdresekdr trqrseskhk spkkktgkds gnwdtsgsel
      841 segelekrrr tlleqldddq
//
LOCUS       NP_001035847             950 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 4 regulatory subunit 1 isoform
            a [Homo sapiens].
ACCESSION   NP_001035847
VERSION     NP_001035847.1
DBSOURCE    REFSEQ: accession NM_001042388.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 950)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 950)
  AUTHORS   Xu,W., Hua,Z., Wang,Y., Tang,W., Ou,W., Liu,F., Yang,Y., Ding,W.,
            Wang,Z., Cui,L., Ge,W., Gu,Y., Wang,X., Chen,Y., Liu,C.Y. and Du,P.
  TITLE     AMBRA1 promotes intestinal inflammation by antagonizing PP4R1/PP4c
            mediated IKK dephosphorylation in an autophagy-independent manner
  JOURNAL   Cell Death Differ 31 (5), 618-634 (2024)
   PUBMED   38424148
  REMARK    GeneRIF: AMBRA1 promotes intestinal inflammation by antagonizing
            PP4R1/PP4c mediated IKK dephosphorylation in an
            autophagy-independent manner.
REFERENCE   3  (residues 1 to 950)
  AUTHORS   He,Z., Zhong,Y., Lv,T., Wang,J., Jin,Y., Li,F. and Hu,H.
  TITLE     PP4R1 promotes glycolysis and gallbladder cancer progression
            through facilitating ERK1/2 mediated PKM2 nuclear translocation
  JOURNAL   Cancer Lett 586, 216677 (2024)
   PUBMED   38301910
  REMARK    GeneRIF: PP4R1 promotes glycolysis and gallbladder cancer
            progression through facilitating ERK1/2 mediated PKM2 nuclear
            translocation.
REFERENCE   4  (residues 1 to 950)
  AUTHORS   Zhu,X., Chen,X., Shen,X., Liu,Y., Fu,W., Wang,B., Zhao,L., Yang,F.,
            Mo,N., Zhong,G., Jiang,S. and Yang,Z.
  TITLE     PP4R1 accelerates the malignant progression of NSCLC via
            up-regulating HSPA6 expression and HSPA6-mediated ER stress
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (1), 119588 (2024)
   PUBMED   37739270
  REMARK    GeneRIF: PP4R1 accelerates the malignant progression of NSCLC via
            up-regulating HSPA6 expression and HSPA6-mediated ER stress.
REFERENCE   5  (residues 1 to 950)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 950)
  AUTHORS   Toyo-oka,K., Mori,D., Yano,Y., Shiota,M., Iwao,H., Goto,H.,
            Inagaki,M., Hiraiwa,N., Muramatsu,M., Wynshaw-Boris,A., Yoshiki,A.
            and Hirotsune,S.
  TITLE     Protein phosphatase 4 catalytic subunit regulates Cdk1 activity and
            microtubule organization via NDEL1 dephosphorylation
  JOURNAL   J Cell Biol 180 (6), 1133-1147 (2008)
   PUBMED   18347064
REFERENCE   7  (residues 1 to 950)
  AUTHORS   Gingras,A.C., Caballero,M., Zarske,M., Sanchez,A., Hazbun,T.R.,
            Fields,S., Sonenberg,N., Hafen,E., Raught,B. and Aebersold,R.
  TITLE     A novel, evolutionarily conserved protein phosphatase complex
            involved in cisplatin sensitivity
  JOURNAL   Mol Cell Proteomics 4 (11), 1725-1740 (2005)
   PUBMED   16085932
REFERENCE   8  (residues 1 to 950)
  AUTHORS   Zhang,X., Ozawa,Y., Lee,H., Wen,Y.D., Tan,T.H., Wadzinski,B.E. and
            Seto,E.
  TITLE     Histone deacetylase 3 (HDAC3) activity is regulated by interaction
            with protein serine/threonine phosphatase 4
  JOURNAL   Genes Dev 19 (7), 827-839 (2005)
   PUBMED   15805470
REFERENCE   9  (residues 1 to 950)
  AUTHORS   Wada,T., Miyata,T., Inagi,R., Nangaku,M., Wagatsuma,M., Suzuki,D.,
            Wadzinski,B.E., Okubo,K. and Kurokawa,K.
  TITLE     Cloning and characterization of a novel subunit of protein
            serine/threonine phosphatase 4 from mesangial cells
  JOURNAL   J Am Soc Nephrol 12 (12), 2601-2608 (2001)
   PUBMED   11729228
REFERENCE   10 (residues 1 to 950)
  AUTHORS   Kloeker,S. and Wadzinski,B.E.
  TITLE     Purification and identification of a novel subunit of protein
            serine/threonine phosphatase 4
  JOURNAL   J Biol Chem 274 (9), 5339-5347 (1999)
   PUBMED   10026142
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DR006046.1, AK027064.1,
            BC060829.1 and AF100744.1.
            
            Summary: This gene encodes one of several alternate regulatory
            subunits of serine/threonine protein phosphatase 4 (PP4). The
            protein features multiple HEAT repeats. This protein forms a
            complex with PP4RC. This complex may have a distinct role from
            other PP4 complexes, including regulation of HDAC3 (Zhang et al.,
            PMID: 15805470). There is also a transcribed pseudogene on
            chromosome 20. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer protein (isoform a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK027064.1, AF200478.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000400556.8/ ENSP00000383402.3
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..950
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.22"
     Protein         1..950
                     /product="serine/threonine-protein phosphatase 4
                     regulatory subunit 1 isoform a"
                     /note="serine/threonine phosphatase 4;
                     serine/threonine-protein phosphatase 4 regulatory subunit
                     1"
                     /calculated_mol_wt=106873
     Region          1..25
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          26..63
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          65..81
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          82..119
                     /region_name="HEAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          127..164
                     /region_name="HEAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          133..157
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(149..150,153,156..157,191..192,195,198..199,202,
                     231..232,235,238..239,242,270..271,274,277..278,309..310,
                     313,316)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          168..206
                     /region_name="HEAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          173..202
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          208..246
                     /region_name="HEAT 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          212..243
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          248..285
                     /region_name="HEAT 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          252..278
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          287..324
                     /region_name="HEAT 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          289..316
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          326..374
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          413..438
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          453..>471
                     /region_name="WRNPLPNID"
                     /note="Putative WW-binding domain and destruction box;
                     pfam15017"
                     /db_xref="CDD:464448"
     Region          473..499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          505..542
                     /region_name="HEAT 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          568..606
                     /region_name="HEAT 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Site            order(643..644,647,650..651,681..682,685,688..689,692,
                     719..720,723,726..727,730,760..761,764,767..768,799..800,
                     803,806..807)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          664..692
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          698..734
                     /region_name="HEAT 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          702..731
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          740..768
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          779..808
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          799..837
                     /region_name="HEAT 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          861..898
                     /region_name="HEAT 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          863..889
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            935
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TF05.1)"
     CDS             1..950
                     /gene="PPP4R1"
                     /gene_synonym="MEG1; PP4(Rmeg); PP4R1"
                     /coded_by="NM_001042388.3:76..2928"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42412.1"
                     /db_xref="GeneID:9989"
                     /db_xref="HGNC:HGNC:9320"
                     /db_xref="MIM:604908"
ORIGIN      
        1 madlsllqed lqedadgfgv ddyssesdvi iipsaldfvs qdemltplgr ldkyaaseni
       61 fnrqmvarsl ldtlrevcdd erdciavler isrladdsep tvraelmeqv phialfcqen
      121 rpsipyafsk fllpivvryl adqnnqvrkt sqaallalle qelierfdve tkvcpvliel
      181 tapdsnddvk teavaimckm apmvgkdite rlilprfcem ccdcrmfhvr kvcaanfgdi
      241 csvvgqqate emllprffql csdnvwgvrk acaecfmavs catcqeirrt klsalfinli
      301 sdpsrwvrqa afqslgpfis tfanpsssgq yfkeesksse emsvenknrt rdqeapedvq
      361 vrpedtpsdl svsnssvile ntmedhaaea sgkplgeisv pldssllctl sseshqeaas
      421 nendkkpgny ksmlrpevgt tsqdsalldq elynsfhfwr tplpeidldi eleqnsggkp
      481 spegpeeese gpvpsspnit matrkeleem ienlephidd pdvkaqvevl saalrassld
      541 aheetisiek rsdlqdeldi nelpnckinq edsvplisda venmdstlhy ihsdsdlsnn
      601 ssfspdeerr tkvqdvvpqa lldqylsmtd psraqtvdte iakhcayslp gvaltlgrqn
      661 whclretyet lasdmqwkvr rtlafsihel avilgdqlta adlvpifngf lkdldevrig
      721 vlkhlhdflk llhidkrrey lyqlqeflvt dnsrnwrfra elaeqlilll elysprdvyd
      781 ylrpialnlc adkvssvrwi syklvsemvk klhaatpptf gvdlinelve nfgrcpkwsg
      841 rqafvfvcqt vieddclpmd qfavhlmphl ltlandrvpn vrvllaktlr qtllekdyfl
      901 asaschqeav eqtimalqmd rdsdvkyfas ihpastkise damstassty
//
LOCUS       NP_003028                335 aa            linear   PRI 21-NOV-2025
DEFINITION  signaling lymphocytic activation molecule isoform b precursor [Homo
            sapiens].
ACCESSION   NP_003028
VERSION     NP_003028.1
DBSOURCE    REFSEQ: accession NM_003037.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Liu,M., Jiang,Z., Liu,M., Ni,H., Li,Y., Fang,J., Du,Q. and Dong,Y.
  TITLE     SLAMF1 as a novel molecule mediating the causal association between
            rheumatoid arthritis and interstitial lung disease: A Mendelian
            randomization study combined with transcriptomics and in vivo
            validation
  JOURNAL   Int Immunopharmacol 142 (Pt A), 113082 (2024)
   PUBMED   39260308
  REMARK    GeneRIF: SLAMF1 as a novel molecule mediating the causal
            association between rheumatoid arthritis and interstitial lung
            disease: A Mendelian randomization study combined with
            transcriptomics and in vivo validation.
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Gomez-Torres,O., Amatya,S., Kamberov,L., Dhaibar,H.A., Khanna,P.,
            Rom,O., Yurdagul,A. Jr., Orr,A.W., Nunez,K., Thevenot,P., Cohen,A.,
            Samant,H., Alexander,J.S., Burgos-Ramos,E., Chapa-Rodriguez,A. and
            Cruz-Topete,D.
  TITLE     SLAMF1 is expressed and secreted by hepatocytes and the liver in
            nonalcoholic fatty liver disease
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 323 (3), G177-G187 (2022)
   PUBMED   35853010
  REMARK    GeneRIF: SLAMF1 is expressed and secreted by hepatocytes and the
            liver in nonalcoholic fatty liver disease.
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Li,A., Zhang,Z., Ru,X., Yi,Y., Li,X., Qian,J., Wang,J., Yang,X. and
            Yao,Y.
  TITLE     Identification of SLAMF1 as an immune-related key gene associated
            with rheumatoid arthritis and verified in mice collagen-induced
            arthritis model
  JOURNAL   Front Immunol 13, 961129 (2022)
   PUBMED   36110846
  REMARK    GeneRIF: Identification of SLAMF1 as an immune-related key gene
            associated with rheumatoid arthritis and verified in mice
            collagen-induced arthritis model.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Gordiienko,I.M., Lykhova,O.O., Shcherbina,V.M. and Shlapatska,L.M.
  TITLE     SLAMF1/CD150 expression and topology in prostate and breast cancer
            cell lines
  JOURNAL   Exp Oncol 43 (4), 312-316 (2021)
   PUBMED   34967540
  REMARK    GeneRIF: SLAMF1/CD150 expression and topology in prostate and
            breast cancer cell lines.
REFERENCE   6  (residues 1 to 335)
  AUTHORS   Putlyaeva,L.V., Schwartz,A.M., Korneev,K.V., Covic,M.,
            Uroshlev,L.A., Makeev,V.Y., Dmitriev,S.E. and Kuprash,D.V.
  TITLE     Upstream open reading frames regulate translation of the long
            isoform of SLAMF1 mRNA that encodes costimulatory receptor CD150
  JOURNAL   Biochemistry (Mosc) 79 (12), 1405-1411 (2014)
   PUBMED   25716736
  REMARK    GeneRIF: Upstream open reading frames regulate translation of the
            long isoform of SLAMF1 mRNA that encodes costimulatory receptor
            CD150
REFERENCE   7  (residues 1 to 335)
  AUTHORS   Sayos,J., Wu,C., Morra,M., Wang,N., Zhang,X., Allen,D., van
            Schaik,S., Notarangelo,L., Geha,R., Roncarolo,M.G., Oettgen,H., De
            Vries,J.E., Aversa,G. and Terhorst,C.
  TITLE     The X-linked lymphoproliferative-disease gene product SAP regulates
            signals induced through the co-receptor SLAM
  JOURNAL   Nature 395 (6701), 462-469 (1998)
   PUBMED   9774102
REFERENCE   8  (residues 1 to 335)
  AUTHORS   Punnonen,J., Cocks,B.G., Carballido,J.M., Bennett,B., Peterson,D.,
            Aversa,G. and de Vries,J.E.
  TITLE     Soluble and membrane-bound forms of signaling lymphocytic
            activation molecule (SLAM) induce proliferation and Ig synthesis by
            activated human B lymphocytes
  JOURNAL   J Exp Med 185 (6), 993-1004 (1997)
   PUBMED   9091591
REFERENCE   9  (residues 1 to 335)
  AUTHORS   Cocks,B.G., Chang,C.C., Carballido,J.M., Yssel,H., de Vries,J.E.
            and Aversa,G.
  TITLE     A novel receptor involved in T-cell activation
  JOURNAL   Nature 376 (6537), 260-263 (1995)
   PUBMED   7617038
REFERENCE   10 (residues 1 to 335)
  AUTHORS   Sidorenko,S.P. and Clark,E.A.
  TITLE     Characterization of a cell surface glycoprotein IPO-3, expressed on
            activated human B and T lymphocytes
  JOURNAL   J Immunol 151 (9), 4614-4624 (1993)
   PUBMED   8409422
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL121985.13 and AL138930.15.
            
            Transcript Variant: This variant (1) lacks an alternate coding exon
            compared to variant 5. The resulting isoform (b) has a shorter and
            distinct C-terminus compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302035.11/ ENSP00000306190.6
            RefSeq Select criteria :: based on conservation, expression
            regulatory uORF        :: PMID: 25716736
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..335
                     /product="signaling lymphocytic activation molecule
                     isoform b precursor"
                     /note="IPO-3; SLAM family member 1"
                     /calculated_mol_wt=35079
     Region          1..125
                     /region_name="SLAM"
                     /note="Signaling lymphocytic activation molecule (SLAM)
                     protein; pfam06214"
                     /db_xref="CDD:461853"
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2170
     CDS             1..335
                     /gene="SLAMF1"
                     /gene_synonym="CD150; CDw150; IPO3; SLAM"
                     /coded_by="NM_003037.5:100..1107"
                     /note="isoform b precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS1207.1"
                     /db_xref="GeneID:6504"
                     /db_xref="HGNC:HGNC:10903"
                     /db_xref="MIM:603492"
ORIGIN      
        1 mdpkgllslt fvlflslafg asygtggrmm ncpkilrqlg skvllpltye rinksmnksi
       61 hivvtmaksl ensvenkivs ldpseagppr ylgdrykfyl enltlgires rkedegwylm
      121 tleknvsvqr fclqlrlyeq vstpeikvln ktqengtctl ilgctvekgd hvayswseka
      181 gthplnpans shllsltlgp qhadniyict vsnpisnnsq tfspwpgcrt dpsetkpwav
      241 yagllggvim ilimvvilql rrrgktnhyq ttvekkslti yaqvqkpgpl qkkldsfpaq
      301 dpcttiyvaa tepvpesvqe tnsitvyasv tlpes
//
LOCUS       NP_001385212             301 aa            linear   PRI 21-NOV-2025
DEFINITION  TIMELESS-interacting protein isoform 1 [Homo sapiens].
ACCESSION   NP_001385212 XP_024305740
VERSION     NP_001385212.1
DBSOURCE    REFSEQ: accession NM_001398283.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Arai,H., Xiao,Y., Millstein,J., Wang,J., Battaglin,F.,
            Kawanishi,N., Jayachandran,P., Soni,S., Zhang,W., Mancao,C.,
            Salhia,B., Mumenthaler,S.M., Parikh,A.R. and Lenz,H.J.
  TITLE     Germline polymorphisms in genes maintaining the replication fork
            predict the efficacy of oxaliplatin and irinotecan in patients with
            metastatic colorectal cancer
  JOURNAL   Br J Cancer 126 (1), 72-78 (2022)
   PUBMED   34689170
  REMARK    GeneRIF: Germline polymorphisms in genes maintaining the
            replication fork predict the efficacy of oxaliplatin and irinotecan
            in patients with metastatic colorectal cancer.
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Grabarczyk,D.B.
  TITLE     The Fork Protection Complex: A Regulatory Hub at the Head of the
            Replisome
  JOURNAL   Subcell Biochem 99, 83-107 (2022)
   PUBMED   36151374
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Lerner,L.K., Holzer,S., Kilkenny,M.L., Svikovic,S., Murat,P.,
            Schiavone,D., Eldridge,C.B., Bittleston,A., Maman,J.D., Branzei,D.,
            Stott,K., Pellegrini,L. and Sale,J.E.
  TITLE     Timeless couples G-quadruplex detection with processing by DDX11
            helicase during DNA replication
  JOURNAL   EMBO J 39 (18), e104185 (2020)
   PUBMED   32705708
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Gotter,A.L., Suppa,C. and Emanuel,B.S.
  TITLE     Mammalian TIMELESS and Tipin are evolutionarily conserved
            replication fork-associated factors
  JOURNAL   J Mol Biol 366 (1), 36-52 (2007)
   PUBMED   17141802
  REMARK    GeneRIF: TIM and Tipin are functional orthologs of their
            replisome-associated yeast counterparts capable of coordinating
            replication with genotoxic stress responses, and distinguishes
            mammalian TIM from the circadian-specific paralogs.
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Yoshizawa-Sugata,N. and Masai,H.
  TITLE     Human Tim/Timeless-interacting protein, Tipin, is required for
            efficient progression of S phase and DNA replication checkpoint
  JOURNAL   J Biol Chem 282 (4), 2729-2740 (2007)
   PUBMED   17102137
  REMARK    GeneRIF: Tipin is a checkpoint mediator that cooperates with Tim
            and may regulate the nuclear relocation of Claspin in response to
            replication checkpoint
REFERENCE   8  (residues 1 to 301)
  AUTHORS   Chou,D.M. and Elledge,S.J.
  TITLE     Tipin and Timeless form a mutually protective complex required for
            genotoxic stress resistance and checkpoint function
  JOURNAL   Proc Natl Acad Sci U S A 103 (48), 18143-18147 (2006)
   PUBMED   17116885
  REMARK    GeneRIF: observation explains the similar checkpoint phenotypes
            observed in both Tipin- and Timeless-depleted cells
REFERENCE   9  (residues 1 to 301)
  AUTHORS   Gotter,A.L.
  TITLE     Tipin, a novel timeless-interacting protein, is developmentally
            co-expressed with timeless and disrupts its self-association
  JOURNAL   J Mol Biol 331 (1), 167-176 (2003)
   PUBMED   12875843
REFERENCE   10 (residues 1 to 301)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            
            On Dec 14, 2021 this sequence version replaced XP_024305740.1.
            
            Summary: The protein encoded by this gene is part of the replisome
            complex, a group of proteins that support DNA replication. It binds
            TIM, which is involved in circadian rhythm regulation, and aids in
            protecting cells against DNA damage and stress. Two pseudogenes and
            two transcript variants encoding different isoforms have been found
            for this gene. [provided by RefSeq, Jul 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3903197.1, BI825670.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..301
                     /product="TIMELESS-interacting protein isoform 1"
                     /note="timeless-interacting protein; CSM3 homolog"
                     /calculated_mol_wt=34424
     Region          1..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Region          66..148
                     /region_name="Swi3"
                     /note="Replication Fork Protection Component Swi3;
                     pfam07962"
                     /db_xref="CDD:462324"
     Region          67..143
                     /region_name="Interaction with TIMELESS.
                     /evidence=ECO:0000269|PubMed:23359676"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Region          240..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BVW5.2)"
     CDS             1..301
                     /gene="TIPIN"
                     /coded_by="NM_001398283.1:120..1025"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS10215.1"
                     /db_xref="GeneID:54962"
                     /db_xref="HGNC:HGNC:30750"
                     /db_xref="MIM:610716"
ORIGIN      
        1 mlepqengvi dlpdyehved etfppfpppa sperqdgegt epdeesgnga pvrvppkrtv
       61 krnipkldaq rliserglpa lrhvfdkakf kgkgheaedl kmlirhmehw ahrlfpklqf
      121 edfidrveyl gskkevqtcl krirldlpil hedfvsnnde vaennehdvt steldpfltn
      181 lsesemfase lsrslteeqq qriernkqla lerrqaklls nsqtlgndml mntprahtve
      241 evntdedqke esnglnedil dnpcndaian tlneeetlld qsfknvqqql datsrnitea
      301 r
//
LOCUS       NP_001349882             756 aa            linear   PRI 21-NOV-2025
DEFINITION  xylosyl- and glucuronyltransferase LARGE1 isoform 1 [Homo sapiens].
ACCESSION   NP_001349882
VERSION     NP_001349882.1
DBSOURCE    REFSEQ: accession NM_001362953.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Botti-Lodovico,Y., Nair,P., Nosamiefan,D., Stremlau,M.,
            Schaffner,S., Agignoae,S.V., Aiyepada,J.O., Ajogbasile,F.V.,
            Akpede,G.O., Alhasan,F., Andersen,K.G., Asogun,D.A., Ayodeji,O.O.,
            Badiane,A.S., Barnes,K., Bauer,M.R., Bell-Kareem,A., Benard,M.E.,
            Benevolence,E.O., Blessing,O., Boehm,C.K., Boisen,M.L., Bond,N.G.,
            Branco,L.M., Butts,M.J., Carter,A., Colubri,A., Deme,A.B.,
            DeRuff,K.C., Diedhiou,Y., Edamhande,A.P., Elhamoumi,S., Engel,E.J.,
            Eromon,P., Fallah,M., Folarin,O.A., Fry,B., Garry,R., Gaye,A.,
            Gbakie,M., Gevao,S.M., Gionet,G., Gladden-Young,A., Goba,A.,
            Gomis,J.F., Happi,A.N., Houghton,M., Ihekwuazu,C., Iruolagbe,C.O.,
            Jackson,J., Jalloh,S., Johnson,J., Kanneh,L., Kayode,A.,
            Kemball,M., Kingsley,O.C., Koroma,V., Kotliar,D., Mehta,S.,
            Metsky,H.C., Michael,A., Mirhashemi,M.E., Modjarrad,K., Momoh,M.,
            Myhrvold,C.A., Naregose,O.G., Ndiaye,T., Ndiaye,M., Ndiaye,A.,
            Normandin,E., Odia,I., Oguzie,J.U., Okogbenin,S.A., Okokhere,P.O.,
            Okolie,J., Olawoye,I.B., Olumade,T.J., Oluniyi,P.E., Omoregie,O.,
            Park,D.J., Paye,M.F., Petros,B., Philippakis,A.A., Priscilla,A.,
            Ricks,A., Rimoin,A., Sandi,J.D., Schieffelin,J.S., Schreiber,M.,
            Seck,M.C., Siddiqui,S., Siddle,K., Smither,A.R., Sy,M., Sy,N.,
            Tomkins-Tinch,C.H., Tomori,O., Ugwu,C., Uwanibe,J.N., Uyigue,E.A.,
            Victoria,D.I., Vinze,A., Vodzak,M.E., Welch,N., Wurie,H.I.,
            Zoumarou,D., Grant,D.S., Ndiaye,D., MacInnis,B., Sabeti,P.C. and
            Happi,C.
  TITLE     The Origins and Future of Sentinel: An Early-Warning System for
            Pandemic Preemption and Response
  JOURNAL   Viruses 13 (8), 1605 (2021)
   PUBMED   34452470
  REMARK    GeneRIF: The Origins and Future of Sentinel: An Early-Warning
            System for Pandemic Preemption and Response.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Wang,M., Tao,H. and Huang,P.
  TITLE     Clinical significance of LARGE1 in progression of liver cancer and
            the underlying mechanism
  JOURNAL   Gene 779, 145493 (2021)
   PUBMED   33588034
  REMARK    GeneRIF: Clinical significance of LARGE1 in progression of liver
            cancer and the underlying mechanism.
REFERENCE   3  (residues 1 to 756)
  AUTHORS   Walimbe,A.S., Okuma,H., Joseph,S., Yang,T., Yonekawa,T., Hord,J.M.,
            Venzke,D., Anderson,M.E., Torelli,S., Manzur,A., Devereaux,M.,
            Cuellar,M., Prouty,S., Ocampo Landa,S., Yu,L., Xiao,J., Dixon,J.E.,
            Muntoni,F. and Campbell,K.P.
  TITLE     POMK regulates dystroglycan function via LARGE1-mediated elongation
            of matriglycan
  JOURNAL   Elife 9, e61388 (2020)
   PUBMED   32975514
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 756)
  AUTHORS   Beltran,D., Anderson,M.E., Bharathy,N., Settelmeyer,T.P.,
            Svalina,M.N., Bajwa,Z., Shern,J.F., Gultekin,S.H., Cuellar,M.A.,
            Yonekawa,T., Keller,C. and Campbell,K.P.
  TITLE     Exogenous expression of the glycosyltransferase LARGE1 restores
            alpha-dystroglycan matriglycan and laminin binding in
            rhabdomyosarcoma
  JOURNAL   Skelet Muscle 9 (1), 11 (2019)
   PUBMED   31054580
  REMARK    GeneRIF: findings demonstrate that a lack of matriglycan on
            alpha-dystroglycan is a common feature in rhabdomyosarcoma due to
            the downregulation of LARGE1, and that ectopic expression of LARGE1
            can restore matriglycan modifications and the ability of
            alpha-dystroglycan to function as an extracellular matrix receptor
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 756)
  AUTHORS   Gao,G., Johnson,S.H., Vasmatzis,G., Pauley,C.E., Tombers,N.M.,
            Kasperbauer,J.L. and Smith,D.I.
  TITLE     Common fragile sites (CFS) and extremely large CFS genes are
            targets for human papillomavirus integrations and chromosome
            rearrangements in oropharyngeal squamous cell carcinoma
  JOURNAL   Genes Chromosomes Cancer 56 (1), 59-74 (2017)
   PUBMED   27636103
  REMARK    GeneRIF: Large1 gene is a target for human papillomavirus
            integrations and chromosome rearrangements in oropharyngeal
            squamous cell carcinoma.
REFERENCE   6  (residues 1 to 756)
  AUTHORS   Michele,D.E., Barresi,R., Kanagawa,M., Saito,F., Cohn,R.D.,
            Satz,J.S., Dollar,J., Nishino,I., Kelley,R.I., Somer,H., Straub,V.,
            Mathews,K.D., Moore,S.A. and Campbell,K.P.
  TITLE     Post-translational disruption of dystroglycan-ligand interactions
            in congenital muscular dystrophies
  JOURNAL   Nature 418 (6896), 417-422 (2002)
   PUBMED   12140558
REFERENCE   7  (residues 1 to 756)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   8  (residues 1 to 756)
  AUTHORS   Peyrard,M., Seroussi,E., Sandberg-Nordqvist,A.C., Xie,Y.G.,
            Han,F.Y., Fransson,I., Collins,J., Dunham,I., Kost-Alimova,M.,
            Imreh,S. and Dumanski,J.P.
  TITLE     The human LARGE gene from 22q12.3-q13.1 is a new, distinct member
            of the glycosyltransferase gene family
  JOURNAL   Proc Natl Acad Sci U S A 96 (2), 598-603 (1999)
   PUBMED   9892679
REFERENCE   9  (residues 1 to 756)
  AUTHORS   Montanaro,F., Gee,S.H., Jacobson,C., Lindenbaum,M.H., Froehner,S.C.
            and Carbonetto,S.
  TITLE     Laminin and alpha-dystroglycan mediate acetylcholine receptor
            aggregation via a MuSK-independent pathway
  JOURNAL   J Neurosci 18 (4), 1250-1260 (1998)
   PUBMED   9454835
REFERENCE   10 (residues 1 to 756)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z73429.1, AL096754.1, Z68287.1,
            Z69042.1, Z70288.1, Z69943.3, AL008715.1, Z82173.2 and AL008630.1.
            
            Summary: This gene encodes a member of the
            N-acetylglucosaminyltransferase gene family. It encodes a
            glycosyltransferase which participates in glycosylation of
            alpha-dystroglycan, and may carry out the synthesis of glycoprotein
            and glycosphingolipid sugar chains. It may also be involved in the
            addition of a repeated disaccharide unit. The protein encoded by
            this gene is the glycotransferase that adds the final xylose and
            glucuronic acid to alpha-dystroglycan and thereby allows
            alpha-dystroglycan to bind ligands including laminin 211 and
            neurexin. Mutations in this gene cause several forms of congenital
            muscular dystrophy characterized by cognitive disability and
            abnormal glycosylation of alpha-dystroglycan. Alternative splicing
            of this gene results in multiple transcript variants that encode
            the same protein. [provided by RefSeq, May 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.88548.1,
                                           SRR1803612.130343.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..756
                     /product="xylosyl- and glucuronyltransferase LARGE1
                     isoform 1"
                     /note="acetylglucosaminyltransferase-like protein;
                     glycosyltransferase-like protein LARGE1;
                     acetylglucosaminyltransferase-like 1A; xylosyl- and
                     glucuronyltransferase LARGE1"
                     /calculated_mol_wt=87935
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95461.1)"
     Region          43..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95461.1)"
     Region          81..109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95461.1)"
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95461.1)"
     Site            122
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95461.1)"
     Region          138..417
                     /region_name="GT8_LARGE_C"
                     /note="LARGE catalytic domain has closest homology to GT8
                     glycosyltransferase involved in lipooligosaccharide
                     synthesis; cd06431"
                     /db_xref="CDD:133053"
     Region          138..413
                     /region_name="Xylosyltransferase activity.
                     /evidence=ECO:0000305|PubMed:22223806"
                     /note="propagated from UniProtKB/Swiss-Prot (O95461.1)"
     Site            order(143..145,148..149,224,240,242..244,272,296..298,
                     334..335,360..361,380,382..383,386)
                     /site_type="active"
                     /note="putative ligand binding site [active]"
                     /db_xref="CDD:133053"
     Site            148
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95461.1)"
     Site            order(242,244,380)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:133053"
     Site            272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95461.1)"
     Region          414..756
                     /region_name="Glucuronyltransferase activity.
                     /evidence=ECO:0000305|PubMed:22223806"
                     /note="propagated from UniProtKB/Swiss-Prot (O95461.1)"
     Region          473..743
                     /region_name="Glyco_transf_49"
                     /note="Glycosyl-transferase for dystroglycan; pfam13896"
                     /db_xref="CDD:464027"
     CDS             1..756
                     /gene="LARGE1"
                     /gene_synonym="LARGE; MDC1D; MDDGA6; MDDGB6"
                     /coded_by="NM_001362953.2:287..2557"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS13912.1"
                     /db_xref="GeneID:9215"
                     /db_xref="HGNC:HGNC:6511"
                     /db_xref="MIM:603590"
ORIGIN      
        1 mlgicrgrrk flaaslsllc ipaitwiylf sgsfedgkpv slsplesqah sprytassqr
       61 ereslevrmr eveeenralr rqlslaqgra pshrrgnhsk tysmeegtgd senlragiva
      121 gnssecgqqp vvekcetihv aivcagynas rdvvtlvksv lfhrrnplhf hliadsiaeq
      181 ilatlfqtwm vpavrvdfyn adelksevsw ipnkhysgiy glmklvltkt lpanlerviv
      241 ldtditfatd iaelwavfhk fkgqqvlglv enqsdwylgn lwknhrpwpa lgrgyntgvi
      301 lllldklrkm kweqmwrlta erelmgmlst sladqdifna vikqnpflvy qlpcfwnvql
      361 sdhtrseqcy rdvsdlkvih wnspkklrvk nkhveffrnl yltfleydgn llrrelfgcp
      421 seadvnsenl qkqlselded dlcyefrrer ftvhrthlyf lhyeyepaad stdvtlvaql
      481 smdrlqmlea ickhwegpis lalylsdaea qqflryaqgs evlmsrhnvg yhivykegqf
      541 ypvnllrnva mkhistpymf lsdidflpmy glyeylrksv iqldlantkk amivpafetl
      601 ryrlsfpksk aellsmldmg tlftfryhvw tkghaptnfa kwrtattpyr veweadfepy
      661 vvvrrdcpey drrfvgfgwn kvahimeldv qeyefivlpn aymihmphap sfditkfrsn
      721 kqyriclktl keefqqdmsr rygfaalkyl taenns
//
LOCUS       NP_006087                394 aa            linear   PRI 21-NOV-2025
DEFINITION  protein NDRG1 isoform 1 [Homo sapiens].
ACCESSION   NP_006087
VERSION     NP_006087.2
DBSOURCE    REFSEQ: accession NM_006096.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Atkinson,D., Chamova,T., Candayan,A., Kastreva,K., Asenov,O.,
            Litvinenko,I., Estrada-Cuzcano,A., De Vriendt,E., Kukushev,G.,
            Tournev,I. and Jordanova,A.
  TITLE     Identification and Characterization of Novel Founder Mutations in
            NDRG1: Refining the Genetic Landscape of Charcot-Marie-Tooth
            Disease Type 4D in Bulgaria
  JOURNAL   Int J Mol Sci 25 (16), 9047 (2024)
   PUBMED   39201732
  REMARK    GeneRIF: Identification and Characterization of Novel Founder
            Mutations in NDRG1: Refining the Genetic Landscape of
            Charcot-Marie-Tooth Disease Type 4D in Bulgaria.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Gholam Azad,M., Hussaini,M., Russell,T.M., Richardson,V., Kaya,B.,
            Dharmasivam,M. and Richardson,D.R.
  TITLE     Multi-modal mechanisms of the metastasis suppressor, NDRG1:
            Inhibition of WNT/beta-catenin signaling by stabilization of
            protein kinase Calpha
  JOURNAL   J Biol Chem 300 (7), 107417 (2024)
   PUBMED   38815861
  REMARK    GeneRIF: Multi-modal mechanisms of the metastasis suppressor,
            NDRG1: Inhibition of WNT/beta-catenin signaling by stabilization of
            protein kinase Calpha.
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Lian,Z., Tian,P., Ma,S., Chang,T., Liu,R., Feng,Q. and Li,J.
  TITLE     Long noncoding RNA MEG3 regulates cell proliferation and apoptosis
            by disrupting microRNA-9-5p-mediated inhibition of NDRG1 in
            prostate cancer
  JOURNAL   Aging (Albany NY) 16 (2), 1938-1951 (2024)
   PUBMED   38271137
  REMARK    GeneRIF: Long noncoding RNA MEG3 regulates cell proliferation and
            apoptosis by disrupting microRNA-9-5p-mediated inhibition of NDRG1
            in prostate cancer.
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Soror,A.A., Eshagh,R., Fahim,M.R., Jamshidian,A. and Monfared,G.H.
  TITLE     Prostate cancer invasion is promoted by the miR-96-5p-induced NDRG1
            deficiency through NF-kappaB regulation
  JOURNAL   Klin Onkol 38 (2), 95-101 (2024)
   PUBMED   38697817
  REMARK    GeneRIF: Prostate cancer invasion is promoted by the
            miR-96-5p-induced NDRG1 deficiency through NF-kappaB regulation.
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Hunter,M., Bernard,R., Freitas,E., Boyer,A., Morar,B.,
            Martins,I.J., Tournev,I., Jordanova,A., Guergelcheva,V.,
            Ishpekova,B., Kremensky,I., Nicholson,G., Schlotter,B.,
            Lochmuller,H., Voit,T., Colomer,J., Thomas,P.K., Levy,N. and
            Kalaydjieva,L.
  TITLE     Mutation screening of the N-myc downstream-regulated gene 1 (NDRG1)
            in patients with Charcot-Marie-Tooth Disease
  JOURNAL   Hum Mutat 22 (2), 129-135 (2003)
   PUBMED   12872253
  REMARK    GeneRIF: Two disease causing mutations in NDRG1 in
            Charcot-Marie-Tooth Disease patients.
            GeneRIF: Observational study of genotype prevalence. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 394)
  AUTHORS   van Belzen,N., Dinjens,W.N., Diesveld,M.P., Groen,N.A., van der
            Made,A.C., Nozawa,Y., Vlietstra,R., Trapman,J. and Bosman,F.T.
  TITLE     A novel gene which is up-regulated during colon epithelial cell
            differentiation and down-regulated in colorectal neoplasms
  JOURNAL   Lab Invest 77 (1), 85-92 (1997)
   PUBMED   9251681
  REMARK    GeneRIF: NDRG1 up-regulation during colon epithelial cell
            differentiation. First publication on tissue and subcellular
            expression of NDRG1.
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Kokame,K., Kato,H. and Miyata,T.
  TITLE     Homocysteine-respondent genes in vascular endothelial cells
            identified by differential display analysis. GRP78/BiP and novel
            genes
  JOURNAL   J Biol Chem 271 (47), 29659-29665 (1996)
   PUBMED   8939898
REFERENCE   8  (residues 1 to 394)
  AUTHORS   Kalaydjieva,L., Hallmayer,J., Chandler,D., Savov,A., Nikolova,A.,
            Angelicheva,D., King,R.H., Ishpekova,B., Honeyman,K., Calafell,F.,
            Shmarov,A., Petrova,J., Turnev,I., Hristova,A., Moskov,M.,
            Stancheva,S., Petkova,I., Bittles,A.H., Georgieva,V., Middleton,L.
            and Thomas,P.K.
  TITLE     Gene mapping in Gypsies identifies a novel demyelinating neuropathy
            on chromosome 8q24
  JOURNAL   Nat Genet 14 (2), 214-217 (1996)
   PUBMED   8841199
REFERENCE   9  (residues 1 to 394)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 4 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301641
REFERENCE   10 (residues 1 to 394)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC353531.1, BC003175.1,
            AF004162.1 and D87953.1.
            
            On Oct 14, 2003 this sequence version replaced NP_006087.1.
            
            Summary: This gene is a member of the N-myc downregulated gene
            family which belongs to the alpha/beta hydrolase superfamily. The
            protein encoded by this gene is a cytoplasmic protein involved in
            stress responses, hormone responses, cell growth, and
            differentiation. The encoded protein is necessary for p53-mediated
            caspase activation and apoptosis. Mutations in this gene are a
            cause of Charcot-Marie-Tooth disease type 4D, and expression of
            this gene may be a prognostic indicator for several types of
            cancer. Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene. [provided by RefSeq, May
            2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC003175.1, AF004162.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323851.13/ ENSP00000319977.8
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.22"
     Protein         1..394
                     /product="protein NDRG1 isoform 1"
                     /note="differentiation-related gene 1 protein;
                     nickel-specific induction protein Cap43; reducing agents
                     and tunicamycin-responsive protein; protein regulated by
                     oxygen-1; protein NDRG1; N-myc downstream-regulated gene 1
                     protein"
                     /calculated_mol_wt=42705
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q92597.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92597.1)"
     Region          34..316
                     /region_name="Ndr"
                     /note="Ndr family; pfam03096"
                     /db_xref="CDD:397285"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62433; propagated from
                     UniProtKB/Swiss-Prot (Q92597.1)"
     Region          325..394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92597.1)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92597.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by SGK1.
                     /evidence=ECO:0000269|PubMed:15461589,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92597.1)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by SGK1.
                     /evidence=ECO:0000269|PubMed:15461589,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q92597.1)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by SGK1.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92597.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q92597.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q62433; propagated from
                     UniProtKB/Swiss-Prot (Q92597.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92597.1)"
     Region          339..368
                     /region_name="3 X 10 AA tandem repeats of
                     G-T-R-S-R-S-H-T-S-E"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92597.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q62433; propagated from
                     UniProtKB/Swiss-Prot (Q92597.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62433; propagated from
                     UniProtKB/Swiss-Prot (Q92597.1)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by SGK1.
                     /evidence=ECO:0000269|PubMed:15461589,
                     ECO:0000269|PubMed:18787837; propagated from
                     UniProtKB/Swiss-Prot (Q92597.1)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6JE36; propagated from
                     UniProtKB/Swiss-Prot (Q92597.1)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by SGK1.
                     /evidence=ECO:0000269|PubMed:15461589,
                     ECO:0000269|PubMed:18787837; propagated from
                     UniProtKB/Swiss-Prot (Q92597.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6JE36; propagated from
                     UniProtKB/Swiss-Prot (Q92597.1)"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by SGK1.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92597.1)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by SGK1.
                     /evidence=ECO:0000269|PubMed:15461589,
                     ECO:0000269|PubMed:18787837, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q92597.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92597.1)"
     CDS             1..394
                     /gene="NDRG1"
                     /gene_synonym="CAP43; CMT4D; DRG-1; DRG1; GC4; HMSNL;
                     NDR1; NMSL; PROXY1; RIT42; RTP; TARG1; TDD5"
                     /coded_by="NM_006096.4:138..1322"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS34945.1"
                     /db_xref="GeneID:10397"
                     /db_xref="HGNC:HGNC:7679"
                     /db_xref="MIM:605262"
ORIGIN      
        1 msremqdvdl aevkplvekg etitgllqef dvqeqdietl hgsvhvtlcg tpkgnrpvil
       61 tyhdigmnhk tcynplfnye dmqeitqhfa vchvdapgqq dgaasfpagy mypsmdqlae
      121 mlpgvlqqfg lksiigmgtg agayiltrfa lnnpemvegl vlinvnpcae gwmdwaaski
      181 sgwtqalpdm vvshlfgkee mqsnvevvht yrqhivndmn pgnlhlfina ynsrrdleie
      241 rpmpgthtvt lqcpallvvg dsspavdavv ecnskldptk ttllkmadcg glpqisqpak
      301 laeafkyfvq gmgympsasm trlmrsrtas gssvtsldgt rsrshtsegt rsrshtsegt
      361 rsrshtsega hlditpnsga agnsagpksm evsc
//
LOCUS       NP_001290370             286 aa            linear   PRI 21-NOV-2025
DEFINITION  protein HEXIM2 isoform 1 [Homo sapiens].
ACCESSION   NP_001290370
VERSION     NP_001290370.1
DBSOURCE    REFSEQ: accession NM_001303441.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Walker,F.M., Sobral,L.M., Danis,E., Sanford,B., Donthula,S.,
            Balakrishnan,I., Wang,D., Pierce,A., Karam,S.D., Kargar,S.,
            Serkova,N.J., Foreman,N.K., Venkataraman,S., Dowell,R., Vibhakar,R.
            and Dahl,N.A.
  TITLE     Rapid P-TEFb-dependent transcriptional reorganization underpins the
            glioma adaptive response to radiotherapy
  JOURNAL   Nat Commun 15 (1), 4616 (2024)
   PUBMED   38816355
  REMARK    GeneRIF: Rapid P-TEFb-dependent transcriptional reorganization
            underpins the glioma adaptive response to radiotherapy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Li,Q., Price,J.P., Byers,S.A., Cheng,D., Peng,J. and Price,D.H.
  TITLE     Analysis of the large inactive P-TEFb complex indicates that it
            contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two
            P-TEFb molecules containing Cdk9 phosphorylated at threonine 186
  JOURNAL   J Biol Chem 280 (31), 28819-28826 (2005)
   PUBMED   15965233
  REMARK    GeneRIF: Positive transcription elongation factor b regulates
            eukaryotic gene expression at the level of elongation and is
            controlled by the reversible association with HEXIM2.
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Fraldi,A., Varrone,F., Napolitano,G., Michels,A.A., Majello,B.,
            Bensaude,O. and Lania,L.
  TITLE     Inhibition of Tat activity by the HEXIM1 protein
  JOURNAL   Retrovirology 2, 42 (2005)
   PUBMED   15992410
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 286)
  AUTHORS   Byers,S.A., Price,J.P., Cooper,J.J., Li,Q. and Price,D.H.
  TITLE     HEXIM2, a HEXIM1-related protein, regulates positive transcription
            elongation factor b through association with 7SK
  JOURNAL   J Biol Chem 280 (16), 16360-16367 (2005)
   PUBMED   15713662
  REMARK    GeneRIF: utilization of HEXIM1 or HEXIM2 to bind and inhibit P-TEFb
            can be differentially regulated in vivo.
REFERENCE   9  (residues 1 to 286)
  AUTHORS   Yik,J.H., Chen,R., Pezda,A.C. and Zhou,Q.
  TITLE     Compensatory contributions of HEXIM1 and HEXIM2 in maintaining the
            balance of active and inactive positive transcription elongation
            factor b complexes for control of transcription
  JOURNAL   J Biol Chem 280 (16), 16368-16376 (2005)
   PUBMED   15713661
  REMARK    GeneRIF: HEXIM2 can functionally and quantitatively compensate for
            the loss of HEXIM1
REFERENCE   10 (residues 1 to 286)
  AUTHORS   Michels,A.A., Nguyen,V.T., Fraldi,A., Labas,V., Edwards,M.,
            Bonnet,F., Lania,L. and Bensaude,O.
  TITLE     MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a
            transcription-dependent manner
  JOURNAL   Mol Cell Biol 23 (14), 4859-4869 (2003)
   PUBMED   12832472
  REMARK    Erratum:[Mol Cell Biol. 2003 Dec;23(24):9405]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI829844.1, AA223138.1 and
            AK056946.1.
            
            Summary: This gene encodes a member of the HEXIM family of
            proteins. This protein is a component of the 7SK small nuclear
            ribonucleoprotein. This protein has been found to negatively
            regulate the kinase activity of the cyclin-dependent kinase P-TEFb,
            which phosphorylates multiple target proteins to promote
            transcriptional elongation. This gene is located approximately 7 kb
            downstream from related family member HEXIM1 on chromosome 17.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2015].
            
            Transcript Variant: This variant (7) differs in the 5' UTR compared
            to variant 1. Variants 1-9 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3268247.1,
                                           SRR14038193.376715.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000589230.6/ ENSP00000466200.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..286
                     /product="protein HEXIM2 isoform 1"
                     /note="hexamethylene-bis-acetamide-inducible transcript 2;
                     hexamethylene bis-acetamide inducible 2; MAQ1 paralog;
                     protein HEXIM2; hexamethylene bis-acetamide-inducible
                     protein 2; hexamethylene bisacetamide inducible 2"
                     /calculated_mol_wt=32287
     Region          1..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Region          102..227
                     /region_name="HEXIM"
                     /note="Hexamethylene bis-acetamide-inducible protein;
                     pfam15313"
                     /db_xref="CDD:464638"
     Region          140..143
                     /region_name="Interaction with P-TEFb"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Region          216..>271
                     /region_name="YabA"
                     /note="Regulator of replication initiation timing YabA
                     [Replication, recombination and repair]; COG4467"
                     /db_xref="CDD:443564"
     Region          226..286
                     /region_name="Interaction with CCNT1, HEXIM1 and HEXIM2.
                     /evidence=ECO:0000269|PubMed:15713661,
                     ECO:0000269|PubMed:15994294"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     CDS             1..286
                     /gene="HEXIM2"
                     /gene_synonym="L3"
                     /coded_by="NM_001303441.2:350..1210"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS11496.1"
                     /db_xref="GeneID:124790"
                     /db_xref="HGNC:HGNC:28591"
                     /db_xref="MIM:615695"
ORIGIN      
        1 mmatpnqtac naespvalee aktsgapgsp qtpperhdsg gslpltprme shsededlag
       61 avgglgwnsr sprtqspggc saeavlarkk hrrrpskrkr hwrpylelsw aekqqrderq
      121 sqrasrvree mfakgqpvap ynttqflmnd rdpeepnldv phgishpgss geseagdsdg
      181 rgrahgefqr kdfsetyerf hteslqgrsk qelvrdylel ekrlsqaeee trrlqqlqac
      241 tgqqscrqve elaaevqrlr tenqrlrqen qmwnregcrc deepgt
//
LOCUS       NP_001364387             551 aa            linear   PRI 21-NOV-2025
DEFINITION  chloride channel CLIC-like protein 1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001364387
VERSION     NP_001364387.1
DBSOURCE    REFSEQ: accession NM_001377458.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 551)
  AUTHORS   D'Atri,I., Martin,E.R., Yang,L., Sears,E., Baple,E., Crosby,A.H.,
            Chilton,J.K. and Oguro-Ando,A.
  TITLE     Unraveling the CLCC1 interactome: Impact of the Asp25Glu variant
            and its interaction with SigmaR1 at the Mitochondrial-Associated ER
            Membrane (MAM)
  JOURNAL   Neurosci Lett 830, 137778 (2024)
   PUBMED   38621504
  REMARK    GeneRIF: Unraveling the CLCC1 interactome: Impact of the Asp25Glu
            variant and its interaction with SigmaR1 at the
            Mitochondrial-Associated ER Membrane (MAM).
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Tang,L., Tang,X., Zhao,Q., Li,Y., Bu,Y., Liu,Z., Li,J., Guo,J.,
            Shen,L., Jiang,H., Tang,B., Xu,R., Cao,W., Yuan,Y. and Wang,J.
  TITLE     Mutation and clinical analysis of the CLCC1 gene in amyotrophic
            lateral sclerosis patients from Central South China
  JOURNAL   Ann Clin Transl Neurol 11 (1), 79-88 (2024)
   PUBMED   37916886
  REMARK    GeneRIF: Mutation and clinical analysis of the CLCC1 gene in
            amyotrophic lateral sclerosis patients from Central South China.
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Guo,L., Mao,Q., He,J., Liu,X., Piao,X., Luo,L., Hao,X., Yu,H.,
            Song,Q., Xiao,B., Fan,D., Gao,Z. and Jia,Y.
  TITLE     Disruption of ER ion homeostasis maintained by an ER anion channel
            CLCC1 contributes to ALS-like pathologies
  JOURNAL   Cell Res 33 (7), 497-515 (2023)
   PUBMED   37142673
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Irvin,M.R., Shrestha,S., Chen,Y.D., Wiener,H.W., Haritunians,T.,
            Vaughan,L.K., Tiwari,H.K., Taylor,K.D., Scherzer,R., Saag,M.S.,
            Grunfeld,C., Rotter,J.I. and Arnett,D.K.
  TITLE     Genes linked to energy metabolism and immunoregulatory mechanisms
            are associated with subcutaneous adipose tissue distribution in
            HIV-infected men
  JOURNAL   Pharmacogenet Genomics 21 (12), 798-807 (2011)
   PUBMED   21897333
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Zhang,Q., Zulfiqar,F., Xiao,X., Riazuddin,S.A., Ayyagari,R.,
            Sabar,F., Caruso,R., Sieving,P.A., Riazuddin,S. and Hejtmancik,J.F.
  TITLE     Severe autosomal recessive retinitis pigmentosa maps to chromosome
            1p13.3-p21.2 between D1S2896 and D1S457 but outside ABCA4
  JOURNAL   Hum Genet 118 (3-4), 356-365 (2005)
   PUBMED   16189710
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Li,X. and Weinman,S.A.
  TITLE     Chloride channels and hepatocellular function: prospects for
            molecular identification
  JOURNAL   Annu Rev Physiol 64, 609-633 (2002)
   PUBMED   11826282
  REMARK    Review article
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Nagasawa,M., Kanzaki,M., Iino,Y., Morishita,Y. and Kojima,I.
  TITLE     Identification of a novel chloride channel expressed in the
            endoplasmic reticulum, golgi apparatus, and nucleus
  JOURNAL   J Biol Chem 276 (23), 20413-20418 (2001)
   PUBMED   11279057
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL449266.17.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853564.1486.1,
                                           SRR1803612.111590.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369969.7/ ENSP00000358986.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..551
                     /product="chloride channel CLIC-like protein 1 isoform 1
                     precursor"
                     /note="chloride channel CLIC-like protein 1; Mid-1-related
                     chloride channel protein 1; retinitis pigmentosa 32
                     (autosomal recessive); ER anion channel 1"
                     /calculated_mol_wt=60112
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1928
     Region          14..551
                     /region_name="MCLC"
                     /note="Mid-1-related chloride channel (MCLC); pfam05934"
                     /db_xref="CDD:461783"
     mat_peptide     19..551
                     /product="Chloride channel CLIC-like protein 1.
                     /id=PRO_0000297682"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
                     /calculated_mol_wt=60112
     Site            25
                     /site_type="other"
                     /note="Ca(2+)-mediated inhibition of channel activity.
                     /evidence=ECO:0000269|PubMed:37142673; propagated from
                     UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            181
                     /site_type="other"
                     /note="Ca(2+)-mediated inhibition of channel activity.
                     /evidence=ECO:0000269|PubMed:37142673; propagated from
                     UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            217..237
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            330..350
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Region          363..415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Region          447..551
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     CDS             1..551
                     /gene="CLCC1"
                     /gene_synonym="ERAC1; MCLC; RP32"
                     /coded_by="NM_001377458.1:297..1952"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 5"
                     /db_xref="CCDS:CCDS41362.1"
                     /db_xref="GeneID:23155"
                     /db_xref="HGNC:HGNC:29675"
                     /db_xref="MIM:617539"
ORIGIN      
        1 mlcslllcec lllvagyahd ddwidptdml nydaasgtmr ksqakygisg ekdvspdlsc
       61 adeisecyhk ldsltykide cekkkredye sqsnpvfrry lnkilieagk lglpdenkgd
      121 mhydaeiilk retlleiqkf lngedwkpga lddalsdili nfkfhdfetw kwrfedsfgv
      181 dpynvlmvll cllcivvlva telwtyvrwy tqlrrvliis flfslgwnwm ylyklafaqh
      241 qaevakmepl nnvcakkmdw tgsiwewfrs swtykddpcq kyyelllvnp iwlvpptkal
      301 avtfttfvte plkhigkgtg efikalmkei pallhlpvli imalailsfc ygagksvhvl
      361 rhiggpesep pqalrprdrr rqeeidyrpd ggagdadfhy rgqmgpteqg pyaktyegrr
      421 eilrerdvdl rfqtgnkspe vlrafdvpda earehptvvp shkspvldtk pketggilge
      481 gtpkesstes sqsakpvsgq dtsgntegsp aaekaqlkse aagspdqgst yspargvagp
      541 rgqdpvsspc g
//
LOCUS       NP_001292486             134 aa            linear   PRI 21-NOV-2025
DEFINITION  thioredoxin-like protein 4A isoform 3 [Homo sapiens].
ACCESSION   NP_001292486
VERSION     NP_001292486.1
DBSOURCE    REFSEQ: accession NM_001305557.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 134)
  AUTHORS   Wood,K.A., Ellingford,J.M., Thomas,H.B., Douzgou,S., Beaman,G.M.,
            Hobson,E., Prescott,K., O'Keefe,R.T. and Newman,W.G.
  CONSRTM   Genomics UK Research Consortium
  TITLE     Expanding the genotypic spectrum of TXNL4A variants in Burn-McKeown
            syndrome
  JOURNAL   Clin Genet 101 (2), 255-259 (2022)
   PUBMED   34713892
  REMARK    GeneRIF: Expanding the genotypic spectrum of TXNL4A variants in
            Burn-McKeown syndrome.
REFERENCE   5  (residues 1 to 134)
  AUTHORS   Wieczorek,D., Newman,W.G., Wieland,T., Berulava,T., Kaffe,M.,
            Falkenstein,D., Beetz,C., Graf,E., Schwarzmayr,T., Douzgou,S.,
            Clayton-Smith,J., Daly,S.B., Williams,S.G., Bhaskar,S.S.,
            Urquhart,J.E., Anderson,B., O'Sullivan,J., Boute,O., Gundlach,J.,
            Czeschik,J.C., van Essen,A.J., Hazan,F., Park,S., Hing,A.,
            Kuechler,A., Lohmann,D.R., Ludwig,K.U., Mangold,E., Steenpass,L.,
            Zeschnigk,M., Lemke,J.R., Lourenco,C.M., Hehr,U., Prott,E.C.,
            Waldenberger,M., Bohmer,A.C., Horsthemke,B., O'Keefe,R.T.,
            Meitinger,T., Burn,J., Ludecke,H.J. and Strom,T.M.
  TITLE     Compound heterozygosity of low-frequency promoter deletions and
            rare loss-of-function mutations in TXNL4A causes Burn-McKeown
            syndrome
  JOURNAL   Am J Hum Genet 95 (6), 698-707 (2014)
   PUBMED   25434003
  REMARK    GeneRIF: Reporter gene and in vivo assays showed that the promoter
            deletions led to reduced expression of TXNL4A. Depletion of TXNL4A
            (Dib1) in yeast demonstrated reduced assembly of the tri-snRNP
            complex.
REFERENCE   6  (residues 1 to 134)
  AUTHORS   Zhou,Z., Licklider,L.J., Gygi,S.P. and Reed,R.
  TITLE     Comprehensive proteomic analysis of the human spliceosome
  JOURNAL   Nature 419 (6903), 182-185 (2002)
   PUBMED   12226669
REFERENCE   7  (residues 1 to 134)
  AUTHORS   Zhang,Y., Lindblom,T., Chang,A., Sudol,M., Sluder,A.E. and
            Golemis,E.A.
  TITLE     Evidence that dim1 associates with proteins involved in pre-mRNA
            splicing, and delineation of residues essential for dim1
            interactions with hnRNP F and Npw38/PQBP-1
  JOURNAL   Gene 257 (1), 33-43 (2000)
   PUBMED   11054566
REFERENCE   8  (residues 1 to 134)
  AUTHORS   Reuter,K., Nottrott,S., Fabrizio,P., Luhrmann,R. and Ficner,R.
  TITLE     Identification, characterization and crystal structure analysis of
            the human spliceosomal U5 snRNP-specific 15 kD protein
  JOURNAL   J Mol Biol 294 (2), 515-525 (1999)
   PUBMED   10610776
REFERENCE   9  (residues 1 to 134)
  AUTHORS   Zhang,Y.Z., Gould,K.L., Dunbrack,R.L. Jr., Cheng,H., Roder,H. and
            Golemis,E.A.
  TITLE     The evolutionarily conserved Dim1 protein defines a novel branch of
            the thioredoxin fold superfamily
  JOURNAL   Physiol Genomics 1 (3), 109-118 (1999)
   PUBMED   11015569
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 134)
  AUTHORS   Ludecke,H.J. and Wieczorek,D.
  TITLE     TXNL4A-Related Craniofacial Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27413799
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF972457.1, BE385528.1,
            BM922767.1, BC001046.2 and AC090360.9.
            
            Summary: The protein encoded by this gene is a member of the U5
            small ribonucleoprotein particle (snRNP), and is involved in
            pre-mRNA splicing. This protein contains a thioredoxin-like fold
            and it is expected to interact with multiple proteins.
            Protein-protein interactions have been observed with the
            polyglutamine tract-binding protein 1 (PQBP1). Mutations in both
            the coding region and promoter region of this gene have been
            associated with Burn-McKeown syndrome, which is a rare disorder
            characterized by craniofacial dysmorphisms, cardiac defects,
            hearing loss, and bilateral choanal atresia. A pseudogene of this
            gene is found on chromosome 2. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Mar 2015].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice site in the 5' coding region, compared to variant 1. The
            encoded isoform (3) is shorter than isoform 1, but has the same N-
            and C-termini.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM922767.1, SRR9304715.367330.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q23"
     Protein         1..134
                     /product="thioredoxin-like protein 4A isoform 3"
                     /note="thioredoxin-like 4; DIM1 protein homolog;
                     thioredoxin-like U5 snRNP protein U5-15kD; spliceosomal U5
                     snRNP-specific 15 kDa protein"
                     /calculated_mol_wt=15751
     Region          1..134
                     /region_name="PLN00410"
                     /note="U5 snRNP protein, DIM1 family; Provisional"
                     /db_xref="CDD:215109"
     Site            order(21,23..24,78..80)
                     /site_type="active"
                     /note="first critical site [active]"
                     /db_xref="CDD:239252"
     Site            40..43
                     /site_type="active"
                     /note="second critical site [active]"
                     /db_xref="CDD:239252"
     CDS             1..134
                     /gene="TXNL4A"
                     /gene_synonym="BMKS; DIB1; DIM1; SNRNP15; TXNL4; U5-15kD"
                     /coded_by="NM_001305557.2:172..576"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:10907"
                     /db_xref="HGNC:HGNC:30551"
                     /db_xref="MIM:611595"
ORIGIN      
        1 msymlphlhn gwqvdqails eedrvvvirf ghdwdptcmk mdevknfavi ylvditevpd
       61 fnkmyelydp ctvmfffrnk himidlgtgn nnkinwamed kqemvdiiet vyrgarkgrg
      121 lvvspkdyst kyry
//
LOCUS       NP_001336002             817 aa            linear   PRI 21-NOV-2025
DEFINITION  TBC1 domain family member 5 isoform a [Homo sapiens].
ACCESSION   NP_001336002 XP_005265669
VERSION     NP_001336002.1
DBSOURCE    REFSEQ: accession NM_001349073.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Tu,Y.X.I., Sydor,A.M., Coyaud,E., Laurent,E.M.N., Dyer,D.,
            Mellouk,N., St-Germain,J., Vernon,R.M., Forman-Kay,J.D., Li,T.,
            Hua,R., Zhao,K., Ridgway,N.D., Kim,P.K., Raught,B. and Brumell,J.H.
  TITLE     Global Proximity Interactome of the Human Macroautophagy Pathway
  JOURNAL   Autophagy 18 (5), 1174-1186 (2022)
   PUBMED   34524948
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 817)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 817)
  AUTHORS   Seaman,M.N., Harbour,M.E., Tattersall,D., Read,E. and Bright,N.
  TITLE     Membrane recruitment of the cargo-selective retromer subcomplex is
            catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP
            TBC1D5
  JOURNAL   J Cell Sci 122 (Pt 14), 2371-2382 (2009)
   PUBMED   19531583
  REMARK    GeneRIF: Membrane recruitment of the cargo-selective retromer
            subcomplex VPS35/29/26 is catalysed by the small GTPase Rab7 and
            inhibited by the Rab-GAP TBC1D5.
REFERENCE   7  (residues 1 to 817)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
REFERENCE   8  (residues 1 to 817)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   9  (residues 1 to 817)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 817)
  AUTHORS   Brill,L.M., Salomon,A.R., Ficarro,S.B., Mukherji,M.,
            Stettler-Gill,M. and Peters,E.C.
  TITLE     Robust phosphoproteomic profiling of tyrosine phosphorylation sites
            from human T cells using immobilized metal affinity chromatography
            and tandem mass spectrometry
  JOURNAL   Anal Chem 76 (10), 2763-2772 (2004)
   PUBMED   15144186
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104451.2, AC144531.2, AC090960.3 and AC090644.2.
            
            On Mar 3, 2017 this sequence version replaced XP_005265669.1.
            
            Transcript Variant: This variant (3), as well as variants 1, 4, and
            5, encodes isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2972454.1,
                                           SRR14038191.485674.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..817
                     /product="TBC1 domain family member 5 isoform a"
                     /calculated_mol_wt=91085
     Region          79..381
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     CDS             1..817
                     /gene="TBC1D5"
                     /coded_by="NM_001349073.2:187..2640"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS46770.1"
                     /db_xref="GeneID:9779"
                     /db_xref="HGNC:HGNC:19166"
                     /db_xref="MIM:615740"
ORIGIN      
        1 myhslsetrh plqpeeqevg idplssysnk sggdsnkngr rtsstldseg tfnsyrkewe
       61 elfvnnnyla tirqkgingq lrssrfrsic wklflcvlpq dksqwisrie elrawysnik
      121 eihitnprkv vgqqdlminn plsqdegslw nkffqdkelr smieqdvkrt fpemqffqqe
      181 nvrkiltdvl fcyareneql lykqgmhell apivfvlhcd hqaflhases aqpseemktv
      241 lnpeylehda yavfsqlmet aepwfstfeh dgqkgketlm tpipfarpqd lgptiaivtk
      301 vnqiqdhllk khdielymhl nrleiapqiy glrwvrllfg refplqdllv vwdalfadgl
      361 slglvdyifv amllyirdal issnyqtclg llmhypfigd vhslilkalf lrdpkrnprp
      421 vtyqfhpnld yykargadlm nksrtnakga plninkvsns linfgrklis pamapgsagg
      481 pvpggnssss ssvviptrts aeapshhlqq qqqqqrlmks esmpvqlnkg dvvtgsdaqv
      541 svpvqtltdl qglsskniss spsveslpgg reftgsppss atkkdsffsn isrsrshskt
      601 mgrkeseeel eaqisflqgq lndldamcky cakvmdthlv niqdvilqen lekedqilvs
      661 laglkqikdi lkgslrfnqs qleaeeneqi tiadnhycss gqgqgrgqgq svqmsgaikq
      721 assetpgctd rgnsddfili skdddgssar gsfsgqaqpl rtlrstsgks qapvcsplvf
      781 sdplmgpasa sssnpssspd ddsskdsgft ivspldi
//
LOCUS       NP_001374883            1113 aa            linear   PRI 21-NOV-2025
DEFINITION  large proline-rich protein BAG6 isoform 12 [Homo sapiens].
ACCESSION   NP_001374883
VERSION     NP_001374883.1
DBSOURCE    REFSEQ: accession NM_001387954.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Alashkar Alhamwe,B., Ponath,V., Alhamdan,F., Dorsam,B.,
            Landwehr,C., Linder,M., Pauck,K., Miethe,S., Garn,H.,
            Finkernagel,F., Brichkina,A., Lauth,M., Tiwari,D.K., Buchholz,M.,
            Bachurski,D., Elmshauser,S., Nist,A., Stiewe,T., Pogge von
            Strandmann,L., Szymanski,W., Beutgen,V., Graumann,J.,
            Teply-Szymanski,J., Keber,C., Denkert,C., Jacob,R., Preusser,C. and
            Pogge von Strandmann,E.
  TITLE     BAG6 restricts pancreatic cancer progression by suppressing the
            release of IL33-presenting extracellular vesicles and the
            activation of mast cells
  JOURNAL   Cell Mol Immunol 21 (8), 918-931 (2024)
   PUBMED   38942797
  REMARK    GeneRIF: BAG6 restricts pancreatic cancer progression by
            suppressing the release of IL33-presenting extracellular vesicles
            and the activation of mast cells.
REFERENCE   3  (residues 1 to 1113)
  AUTHORS   Liu,L., Wu,J., Yan,Y., Cheng,S., Yu,S. and Wang,Y.
  TITLE     DERL2 (derlin 2) stabilizes BAG6 (BAG cochaperone 6) in
            chemotherapy resistance of cholangiocarcinoma
  JOURNAL   J Physiol Biochem 80 (1), 81-97 (2024)
   PUBMED   37815698
  REMARK    GeneRIF: DERL2 (derlin 2) stabilizes BAG6 (BAG cochaperone 6) in
            chemotherapy resistance of cholangiocarcinoma.
REFERENCE   4  (residues 1 to 1113)
  AUTHORS   Roboti,P., Lawless,C. and High,S.
  TITLE     Mitochondrial antiviral-signalling protein is a client of the BAG6
            protein quality control complex
  JOURNAL   J Cell Sci 135 (9) (2022)
   PUBMED   35543156
  REMARK    GeneRIF: Mitochondrial antiviral-signalling protein is a client of
            the BAG6 protein quality control complex.
REFERENCE   5  (residues 1 to 1113)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1113)
  AUTHORS   Ozaki,T., Hanaoka,E., Naka,M., Nakagawara,A. and Sakiyama,S.
  TITLE     Cloning and characterization of rat BAT3 cDNA
  JOURNAL   DNA Cell Biol 18 (6), 503-512 (1999)
   PUBMED   10390159
REFERENCE   7  (residues 1 to 1113)
  AUTHORS   Cross,S.J., Tonks,S., Trowsdale,J. and Campbell,R.D.
  TITLE     Novel detection of restriction fragment length polymorphisms in the
            human major histocompatibility complex
  JOURNAL   Immunogenetics 34 (6), 376-384 (1991)
   PUBMED   1684176
REFERENCE   8  (residues 1 to 1113)
  AUTHORS   Banerji,J., Sands,J., Strominger,J.L. and Spies,T.
  TITLE     A gene pair from the human major histocompatibility complex encodes
            large proline-rich proteins with multiple repeated motifs and a
            single ubiquitin-like domain
  JOURNAL   Proc Natl Acad Sci U S A 87 (6), 2374-2378 (1990)
   PUBMED   2156268
REFERENCE   9  (residues 1 to 1113)
  AUTHORS   Spies,T., Bresnahan,M. and Strominger,J.L.
  TITLE     Human major histocompatibility complex contains a minimum of 19
            genes between the complement cluster and HLA-B
  JOURNAL   Proc Natl Acad Sci U S A 86 (22), 8955-8958 (1989)
   PUBMED   2813433
REFERENCE   10 (residues 1 to 1113)
  AUTHORS   Spies,T., Blanck,G., Bresnahan,M., Sands,J. and Strominger,J.L.
  TITLE     A new cluster of genes within the human major histocompatibility
            complex
  JOURNAL   Science 243 (4888), 214-217 (1989)
   PUBMED   2911734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL662801.7.
            
            Summary: This gene was first characterized as part of a cluster of
            genes located within the human major histocompatibility complex
            class III region. This gene encodes a nuclear protein that is
            cleaved by caspase 3 and is implicated in the control of apoptosis.
            In addition, the protein forms a complex with E1A binding protein
            p300 and is required for the acetylation of p53 in response to DNA
            damage. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.434448.1,
                                           SRR11853560.24470.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..1113
                     /product="large proline-rich protein BAG6 isoform 12"
                     /note="scythe; large proline-rich protein BAT3; large
                     proline-rich protein BAG6; protein G3; HLA-B-associated
                     transcript 3; protein Scythe; BAG family molecular
                     chaperone regulator 6; BCL2 associated athanogene 6"
                     /calculated_mol_wt=116975
     Region          17..87
                     /region_name="Ubl_BAG6"
                     /note="ubiquitin-like (Ubl) domain found in
                     BCL2-associated athanogene 6 (BAG6) and similar proteins;
                     cd01809"
                     /db_xref="CDD:340507"
     Site            order(22..25,58,60,62..65,83..87)
                     /site_type="other"
                     /note="ZF interaction site [polypeptide binding]"
                     /db_xref="CDD:340507"
     Region          270..386
                     /region_name="BAG6"
                     /note="BCL2-associated athanogene 6; pfam12057"
                     /db_xref="CDD:463449"
     Region          <935..1113
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     CDS             1..1113
                     /gene="BAG6"
                     /gene_synonym="BAG-6; BAT3; D6S52E; G3"
                     /coded_by="NM_001387954.1:163..3504"
                     /note="isoform 12 is encoded by transcript variant 14"
                     /db_xref="GeneID:7917"
                     /db_xref="HGNC:HGNC:13919"
                     /db_xref="MIM:142590"
ORIGIN      
        1 mepndststa veepdslevl vktldsqtrt fivgaqmnvk efkehiaasv sipsekqrli
       61 yqgrvlqddk klqeynvggk vihlverapp qthlpsgass gtgsasathg ggsppgtrgp
      121 gasvhdrnan syvmvgtfnl psdgsavdvh inmeqapiqs eprvrlvmaq hmirdiqtll
      181 srmecrggpq pqhsqpppqp pavtpepval ssqtsepves eapprepmea eeveerapaq
      241 npeltpgpap agptpapetn apnhpspaey vevlqelqrl esrlqpflqr yyevlgaaat
      301 tdynnnhegr eedqrlinlv geslrllgnt fvalsdlrcn lactpprhlh vvrpmshytt
      361 pmvlqqaaip iqinvgttvt mtgngtrppp tpnaeapppg pgqassvaps stnvessaeg
      421 apppgpappp atshprviri shqsvepvvm mhmniqdsgt qpggvpsapt gplgppghgq
      481 tlgstliqlp slppefmhav ahqithqamv aavasaaagq qvpgfptapt rvviarptpp
      541 qarpshpggp pvsgtlqgag lgtnaslaqm vsglvgqllm qpvlvaqgtp gmapppapat
      601 asasagttnt attagpapgg paqppptpqp smadlqfsql lgnllgpagp gaggsgvasp
      661 titvampgvp aflqgmtdfl qatqtapppp ppppppppap eqqtmpppgs psggagspgg
      721 lgleslspef ftsvvqgvls sllgslgara gssesiaafi qrlsgssnif epgadgalgf
      781 fgallsllcq nfsmvdvvml lhghfqplqr lqpqlrsffh qhylggqept psnirmatht
      841 litgleeyvr esfslvqvqp gvdiirtnle flqeqfnsia ahvlhctdsg fgarllelcn
      901 qglfeclaln lhclggqqme laavingrir rmsrgvnpsl vswlttmmgl rlqvvlehmp
      961 vgpdailryv rrvgdppqpl peepmevqga eraspepqre naspapgtta eeamsrgppp
     1021 apeggsrdeq dgasaetepw aaavppewvp iiqqdiqsqr kvkpqpplsd aylsgmpakr
     1081 rklrsdiqkr lqedpnyspq rfpnaqrafa ddp
//
LOCUS       NP_001274687            1707 aa            linear   PRI 21-NOV-2025
DEFINITION  collagen alpha-6(IV) chain isoform 3 precursor [Homo sapiens].
ACCESSION   NP_001274687 XP_005262130
VERSION     NP_001274687.1
DBSOURCE    REFSEQ: accession NM_001287758.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1707)
  AUTHORS   O'Brien,A., Aw,W.Y., Tee,H.Y., Naegeli,K.M., Bademci,G., Tekin,M.,
            Arnos,K. and Pandya,A.
  TITLE     Confirmation of COL4A6 variants in X-linked nonsyndromic hearing
            loss and its clinical implications
  JOURNAL   Eur J Hum Genet 30 (1), 7-12 (2022)
   PUBMED   33840813
  REMARK    GeneRIF: Confirmation of COL4A6 variants in X-linked nonsyndromic
            hearing loss and its clinical implications.
REFERENCE   2  (residues 1 to 1707)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 1707)
  AUTHORS   Komori,T., Ono,M., Hara,E.S., Ueda,J., Nguyen,H.T.T., Nguyen,H.T.,
            Yonezawa,T., Maeba,T., Kimura-Ono,A., Takarada,T., Momota,R.,
            Maekawa,K., Kuboki,T. and Oohashi,T.
  TITLE     Type IV collagen alpha6 chain is a regulator of keratin 10 in
            keratinization of oral mucosal epithelium
  JOURNAL   Sci Rep 8 (1), 2612 (2018)
   PUBMED   29422532
  REMARK    GeneRIF: These findings indicate that alpha112:alpha556 (IV)
            network, which is the only network that includes the alpha6(IV)
            chain, is one regulator of KRT10 expression in keratinization of
            oral mucosal epithelium.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1707)
  AUTHORS   Holmes,D.F., Lu,Y., Starborg,T. and Kadler,K.E.
  TITLE     Collagen Fibril Assembly and Function
  JOURNAL   Curr Top Dev Biol 130, 107-142 (2018)
   PUBMED   29853175
  REMARK    Review article
REFERENCE   5  (residues 1 to 1707)
  AUTHORS   Naba,A., Pearce,O.M.T., Del Rosario,A., Ma,D., Ding,H., Rajeeve,V.,
            Cutillas,P.R., Balkwill,F.R. and Hynes,R.O.
  TITLE     Characterization of the Extracellular Matrix of Normal and Diseased
            Tissues Using Proteomics
  JOURNAL   J Proteome Res 16 (8), 3083-3091 (2017)
   PUBMED   28675934
REFERENCE   6  (residues 1 to 1707)
  AUTHORS   Ghebrehiwet,B., Peerschke,E.I., Hong,Y., Munoz,P. and Gorevic,P.D.
  TITLE     Short amino acid sequences derived from C1q receptor (C1q-R) show
            homology with the alpha chains of fibronectin and vitronectin
            receptors and collagen type IV
  JOURNAL   J Leukoc Biol 51 (6), 546-556 (1992)
   PUBMED   1377218
REFERENCE   7  (residues 1 to 1707)
  AUTHORS   Gupta,S., Batchu,R.B. and Datta,K.
  TITLE     Purification, partial characterization of rat kidney hyaluronic
            acid binding protein and its localization on the cell surface
  JOURNAL   Eur J Cell Biol 56 (1), 58-67 (1991)
   PUBMED   1724753
REFERENCE   8  (residues 1 to 1707)
  AUTHORS   Hernandez,M.R., Igoe,F. and Neufeld,A.H.
  TITLE     Extracellular matrix of the human optic nerve head
  JOURNAL   Am J Ophthalmol 102 (2), 139-148 (1986)
   PUBMED   2426947
REFERENCE   9  (residues 1 to 1707)
  AUTHORS   Glant,T.T., Hadhazy,C., Mikecz,K. and Sipos,A.
  TITLE     Appearance and persistence of fibronectin in cartilage. Specific
            interaction of fibronectin with collagen type II
  JOURNAL   Histochemistry 82 (2), 149-158 (1985)
   PUBMED   3997552
REFERENCE   10 (residues 1 to 1707)
  AUTHORS   Matsubara,T., Trueb,B., Fehr,K., Ruttner,J.R. and Odermatt,B.F.
  TITLE     The localization and secretion of type IV collagen in synovial
            capillaries by immunohistochemistry using a monoclonal antibody
            against human type IV collagen
  JOURNAL   Exp Cell Biol 52 (3), 159-169 (1984)
   PUBMED   6386565
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN313347.1, AW082083.1,
            AL136080.6, CN313341.1, CN313332.1, CN313351.1, CA396616.1,
            CA489342.1, CN313343.1, CX872164.1, DA748513.1, BG680578.1,
            AL031177.1 and CB050016.1.
            
            On Dec 19, 2013 this sequence version replaced XP_005262130.1.
            
            Summary: This gene encodes one of the six subunits of type IV
            collagen, the major structural component of basement membranes.
            Like the other members of the type IV collagen gene family, this
            gene is organized in a head-to-head conformation with another type
            IV collagen gene, alpha 5 type IV collagen, so that the gene pair
            shares a common promoter. Deletions in the alpha 5 gene that extend
            into the alpha 6 gene result in diffuse leiomyomatosis accompanying
            the X-linked Alport syndrome caused by the deletion in the alpha 5
            gene. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2013].
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longest protein (isoform 3).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2146982
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1707
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.3"
     Protein         1..1707
                     /product="collagen alpha-6(IV) chain isoform 3 precursor"
                     /note="collagen of basement membrane, alpha-6; collagen
                     IV, alpha-6 polypeptide; collagen alpha-6(IV) chain;
                     dJ889N15.4 (Collagen Alpha 6(IV)); collagen, type IV,
                     alpha 6"
                     /calculated_mol_wt=163192
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2295
     mat_peptide     22..1707
                     /product="collagen alpha-6(IV) chain isoform 3"
                     /calculated_mol_wt=163192
     Region          <44..374
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <456..>757
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <677..>888
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          908..963
                     /region_name="Collagen"
                     /note="Collagen triple helix repeat (20 copies);
                     pfam01391"
                     /db_xref="CDD:460189"
     Region          <943..>1181
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <1239..>1478
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          1484..1589
                     /region_name="C4"
                     /note="C-terminal tandem repeated domain in type 4
                     procollagen; pfam01413"
                     /db_xref="CDD:460201"
     Region          1592..1705
                     /region_name="C4"
                     /note="C-terminal tandem repeated domain in type 4
                     procollagen; pfam01413"
                     /db_xref="CDD:460201"
     CDS             1..1707
                     /gene="COL4A6"
                     /gene_synonym="CXDELq22.3; DELXq22.3; DFNX6"
                     /coded_by="NM_001287758.2:227..5350"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS76010.1"
                     /db_xref="GeneID:1288"
                     /db_xref="HGNC:HGNC:2208"
                     /db_xref="MIM:303631"
ORIGIN      
        1 mhpglwlllv tlclteelaa ageksygkpc ggqdcsgscq cfpekgargr pgpigiqgpt
       61 gpqgftgstg lsglkgergf pgllgpygpk gdkgpmgvpg flgingipgh pgqpgprgpp
      121 gldgcngtqg avgfpgpdgy pgllgppglp gqkgskgdpv lapgsfkgmk gdpglpgldg
      181 itgpqgapgf pgavgpagpp glqgppgppg plgpdgnmgl gfqgekgvkg dvglpgpagp
      241 ppstgelefm gfpkgkkgsk gepgpkgfpg isgppgfpgl gttgekgekg ekgipglpgp
      301 rgpmgsegvq gppgqqgkkg tlgfpglngf qgiegqkgdi glpgpdvfid idgavisgnp
      361 gdpgvpglpg lkgdegiqgl rgpsgvpglp alsgvpgalg pqgfpglkgd qgnpgrttig
      421 aaglpgrdgl pgppgppgpp spefetetlh nkesgfpglr geqgpkgnlg lkgikgdsgf
      481 cacdggvpnt gppgepgppg pwgliglpgl kgargdrgsg gaqgpagapg lvgplgpsgp
      541 kgkkgepils tiqgmpgdrg dsgsqgfrgv igepgkdgvp glpglpglpg dggqgfpgek
      601 glpglpgekg hpgppglpgn glpglpgprg lpgdkgkdgl pgqqglpgsk gdcccrevgk
      661 gdldtergit lpciipgsyg psgfpgtpgf pgpkgsrglp gtpgqpgssg skgepgspgl
      721 vhlpelpgfp gprgekglpg fpglpgkdgl pgmigspglp gskgatgdif gaengapgeq
      781 glqgltghkg flgdsglpgl kgvhgkpgll gpkgergspg tpgqvgqpgt pgssgpygik
      841 gksglpgapg fpgisghpgk kgtrgkkgpp gsivkkglpg lkglpgnpgl vglkgspgsp
      901 gvaglpalsg pkgekgsvgf vgfpgipglp gipgtrglkg ipgstgkmgp sgragtpgek
      961 gdrgnpgpvg ipsprrpmsn lwlkgdkgsq gsagsngfpg prgdkgeagr pgppglpgap
     1021 glpgiikgvs gkpgppgfmg irglpglkgs sgitgfpgmp gesgsqgirg spglpgasgl
     1081 pglkgdngqt veisgspgpk gqpgesgfkg tkgrdglign igfpgnkged gkvgvsgdvg
     1141 lpgapgfpgv agmrgepglp gssghqgaig plgspgligp kgfpgfpglh glnglpgtkg
     1201 thgtpgpsit gvpgpaglpg pkgekgypgi gigapgkpgl rgqkgdrgfp glqgpaglpg
     1261 apgislpsli agqpgdpgrp gldgergrpg pagppgppgp ssnqgdtgdp gfpgipgpkg
     1321 pkgdqgipgf sglpgelglk gmrgepgfmg tpgkvgppgd pgfpgmkgka gprgssglqg
     1381 dpgqtptaea vqvppgplgl pgidgipglt gdpgaqgpvg lqgskglpgi pgkdgpsglp
     1441 gppgalgdpg lpglqgppgf egapgqqgpf gmpgmpgqsm rvgytlvkhs qseqvppcpi
     1501 gmsqlwvgys llfvegqeka hnqdlgfags clprfstmpf iycninevch yarrndksyw
     1561 lsttapipmm pvsqtqipqy isrcsvceap sqaiavhsqd itipqcplgw rslwigysfl
     1621 mhtaagaegg gqslvspgsc ledfratpfi ecsgargtch yfankysfwl ttveerqqfg
     1681 elpvsetlka gqlhtrvsrc qvcmksl
//
LOCUS       NP_001316597             181 aa            linear   PRI 21-NOV-2025
DEFINITION  COMM domain-containing protein 8 isoform 2 [Homo sapiens].
ACCESSION   NP_001316597
VERSION     NP_001316597.1
DBSOURCE    REFSEQ: accession NM_001329668.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Singla,A., Rogers,C., Touma,M.J., El-Najjar,Y., Colley,A.,
            Boesch,D.J., Billadeau,D.D., Gecz,J., Chen,B. and Burstein,E.
  TITLE     CCDC22 mutations that impair COMMD binding cause attenuated
            3C/Ritscher-Schinzel syndrome
  JOURNAL   BMC Med Genomics 18 (1), 98 (2025)
   PUBMED   40448120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Laulumaa,S. and Varjosalo,M.
  TITLE     Commander Complex-A Multifaceted Operator in Intracellular
            Signaling and Cargo
  JOURNAL   Cells 10 (12), 3447 (2021)
   PUBMED   34943955
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 181)
  AUTHORS   Starokadomskyy,P., Gluck,N., Li,H., Chen,B., Wallis,M., Maine,G.N.,
            Mao,X., Zaidi,I.W., Hein,M.Y., McDonald,F.J., Lenzner,S., Zecha,A.,
            Ropers,H.H., Kuss,A.W., McGaughran,J., Gecz,J. and Burstein,E.
  TITLE     CCDC22 deficiency in humans blunts activation of proinflammatory
            NF-kappaB signaling
  JOURNAL   J Clin Invest 123 (5), 2244-2256 (2013)
   PUBMED   23563313
REFERENCE   8  (residues 1 to 181)
  AUTHORS   Mao,X., Gluck,N., Chen,B., Starokadomskyy,P., Li,H., Maine,G.N. and
            Burstein,E.
  TITLE     COMMD1 (copper metabolism MURR1 domain-containing protein 1)
            regulates Cullin RING ligases by preventing CAND1
            (Cullin-associated Nedd8-dissociated protein 1) binding
  JOURNAL   J Biol Chem 286 (37), 32355-32365 (2011)
   PUBMED   21778237
REFERENCE   9  (residues 1 to 181)
  AUTHORS   Vinayagam,A., Stelzl,U., Foulle,R., Plassmann,S., Zenkner,M.,
            Timm,J., Assmus,H.E., Andrade-Navarro,M.A. and Wanker,E.E.
  TITLE     A directed protein interaction network for investigating
            intracellular signal transduction
  JOURNAL   Sci Signal 4 (189), rs8 (2011)
   PUBMED   21900206
REFERENCE   10 (residues 1 to 181)
  AUTHORS   Burstein,E., Hoberg,J.E., Wilkinson,A.S., Rumble,J.M., Csomos,R.A.,
            Komarck,C.M., Maine,G.N., Wilkinson,J.C., Mayo,M.W. and
            Duckett,C.S.
  TITLE     COMMD proteins, a novel family of structural and functional
            homologs of MURR1
  JOURNAL   J Biol Chem 280 (23), 22222-22232 (2005)
   PUBMED   15799966
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107398.4.
            
            Summary: The protein encoded by this gene binds coiled-coil
            domain-containing protein 22 (CCDC22), and this complex can
            regulate the turnover of I-kappa-B and the activation of
            NF-kappa-B. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice junction compared to variant 1. The resulting isoform (2)
            has the same N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1547613.1,
                                           SRR18074968.2589480.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p12"
     Protein         1..181
                     /product="COMM domain-containing protein 8 isoform 2"
                     /note="COMM domain-containing protein 8"
                     /calculated_mol_wt=20732
     Region          7..180
                     /region_name="Commd8"
                     /note="COMM_Domain containing protein 8. The COMM Domain
                     is found at the C-terminus of a variety of proteins;
                     presumably all COMM_Domain containing proteins are located
                     in the nucleus and the COMM domain plays a role in
                     protein-protein interactions. Several...; cd04756"
                     /db_xref="CDD:240104"
     CDS             1..181
                     /gene="COMMD8"
                     /coded_by="NM_001329668.2:52..597"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:54951"
                     /db_xref="HGNC:HGNC:26036"
                     /db_xref="MIM:616656"
ORIGIN      
        1 mepeegtplw rlqklpaelg pqllhkiidg icgraypvyq dyhtvwesee wmhvlediak
       61 ffkaivgknl pdeeifqqln qlnslhqeti mkcvksrkde ikqalsreiv aissaqlqdf
      121 dwqlalssdk iaalrmplls lhldvkenge vkpysiemsr eelqnliqsl eaankvvlql
      181 k
//
LOCUS       NP_001365078             429 aa            linear   PRI 21-NOV-2025
DEFINITION  BEN domain-containing protein 7 isoform 5 [Homo sapiens].
ACCESSION   NP_001365078
VERSION     NP_001365078.1
DBSOURCE    REFSEQ: accession NM_001378149.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Hernandez-Pacheco,N., Flores,C., Alonso,S., Eng,C., Mak,A.C.,
            Hunstman,S., Hu,D., White,M.J., Oh,S.S., Meade,K., Farber,H.J.,
            Avila,P.C., Serebrisky,D., Thyne,S.M., Brigino-Buenaventura,E.,
            Rodriguez-Cintron,W., Sen,S., Kumar,R., Lenoir,M.,
            Rodriguez-Santana,J.R., Burchard,E.G. and Pino-Yanes,M.
  TITLE     Identification of a novel locus associated with skin colour in
            African-admixed populations
  JOURNAL   Sci Rep 7, 44548 (2017)
   PUBMED   28300201
  REMARK    GeneRIF: These results validated the association of two previously
            known skin pigmentation genes, SLC24A5 (minimum p = 2.62 x 10(-14),
            rs1426654) and SLC45A2 (minimum p = 9.71 x 10(-10), rs16891982),
            and revealed the intergenic region of BEND7 and PRPF18 as a novel
            locus associated with this trait (minimum p = 4.58 x 10(-9),
            rs6602666).
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Lauc,G., Huffman,J.E., Pucic,M., Zgaga,L., Adamczyk,B., Muzinic,A.,
            Novokmet,M., Polasek,O., Gornik,O., Kristic,J., Keser,T.,
            Vitart,V., Scheijen,B., Uh,H.W., Molokhia,M., Patrick,A.L.,
            McKeigue,P., Kolcic,I., Lukic,I.K., Swann,O., van Leeuwen,F.N.,
            Ruhaak,L.R., Houwing-Duistermaat,J.J., Slagboom,P.E., Beekman,M.,
            de Craen,A.J., Deelder,A.M., Zeng,Q., Wang,W., Hastie,N.D.,
            Gyllensten,U., Wilson,J.F., Wuhrer,M., Wright,A.F., Rudd,P.M.,
            Hayward,C., Aulchenko,Y., Campbell,H. and Rudan,I.
  TITLE     Loci associated with N-glycosylation of human immunoglobulin G show
            pleiotropy with autoimmune diseases and haematological cancers
  JOURNAL   PLoS Genet 9 (1), e1003225 (2013)
   PUBMED   23382691
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 429)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL590677.7 and AL359172.19.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p13"
     Protein         1..429
                     /product="BEN domain-containing protein 7 isoform 5"
                     /note="BEN domain-containing protein 7"
                     /calculated_mol_wt=47917
     Region          78..153
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7W2.3)"
     Region          208..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7W2.3)"
     Region          310..389
                     /region_name="BEN"
                     /note="BEN domain; pfam10523"
                     /db_xref="CDD:463133"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N7W2.3)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N7W2.3)"
     CDS             1..429
                     /gene="BEND7"
                     /gene_synonym="C10orf30"
                     /coded_by="NM_001378149.1:482..1771"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:222389"
                     /db_xref="HGNC:HGNC:23514"
ORIGIN      
        1 mefserkrsr ksqsfklvsr dyhhevykip efsndvngea ketqpiflgd esmeikkqit
       61 gmrrllndst griyqrvgke geklkeepqd ldlvwpprln ssaeapqslh pssrgvwnel
      121 ppqsgqfsgq ygtrsrtfqs qphpttssng elpvvnssag sncctcncqs tlqailqelk
      181 tmrklmqiqa vgtqnrqqpp islicsqrta vsrkrnkkkk vppktveplt vkqkpsgsem
      241 ekksvvasel salqaaehts peesrvlgfg ivlespssdp evqlaegfdv fmpksqldsi
      301 lsnytrsgsl lfrklvcaff ddktlanslp ngkrkrglnd nrkgldqniv gaikvfteky
      361 ctanhvdklp gprdwvqilq dqiklarrrl krgseiadsd erldgialpp tgklsfrpfs
      421 mtgqyvdil
//
LOCUS       NP_001358901             195 aa            linear   PRI 21-NOV-2025
DEFINITION  ADP-ribosylation factor-like protein 6-interacting protein 6
            isoform c [Homo sapiens].
ACCESSION   NP_001358901
VERSION     NP_001358901.1
DBSOURCE    REFSEQ: accession NM_001371972.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Abumansour,I.S., Hijazi,H., Alazmi,A., Alzahrani,F., Bashiri,F.A.,
            Hassan,H., Alhaddab,M. and Alkuraya,F.S.
  TITLE     ARL6IP6, a susceptibility locus for ischemic stroke, is mutated in
            a patient with syndromic Cutis Marmorata Telangiectatica Congenita
  JOURNAL   Hum Genet 134 (8), 815-822 (2015)
   PUBMED   25957586
  REMARK    GeneRIF: ARL6IP6 as a novel candidate gene for a syndromic form of
            CMTC.
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Ingley,E., Williams,J.H., Walker,C.E., Tsai,S., Colley,S.,
            Sayer,M.S., Tilbrook,P.A., Sarna,M., Beaumont,J.G. and Klinken,S.P.
  TITLE     A novel ADP-ribosylation like factor (ARL-6), interacts with the
            protein-conducting channel SEC61beta subunit
  JOURNAL   FEBS Lett 459 (1), 69-74 (1999)
   PUBMED   10508919
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079344.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1190090.1,
                                           SRR14038194.2227594.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145774, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q23.3"
     Protein         1..195
                     /product="ADP-ribosylation factor-like protein
                     6-interacting protein 6 isoform c"
                     /note="ADP-ribosylation factor-like protein 6-interacting
                     protein 6; regulated by phosphonoformate; phosphonoformate
                     immuno-associated protein 1; ARL-6-interacting protein 6;
                     ADP-ribosylation-like factor 6 interacting protein 6;
                     ADP-ribosylation factor GTPase 6 interacting protein 6;
                     ADP-ribosylation factor-like 6 interacting protein 6; ADP
                     ribosylation factor like GTPase 6 interacting protein 6"
                     /calculated_mol_wt=21036
     Region          <147..183
                     /region_name="ARL6IP6"
                     /note="Haemopoietic lineage transmembrane helix;
                     pfam15062"
                     /db_xref="CDD:405709"
     CDS             1..195
                     /gene="ARL6IP6"
                     /gene_synonym="AIP-6; AIP6; PFAAP1"
                     /coded_by="NM_001371972.1:6..593"
                     /note="isoform c is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS92880.1"
                     /db_xref="GeneID:151188"
                     /db_xref="HGNC:HGNC:24048"
                     /db_xref="MIM:616495"
ORIGIN      
        1 msfaesgwrs alrrrgpgtp gpvarpsyss ftqgdswgeg evdeeegcdq vardlraefs
       61 agawseprkr svlppdgngs pvlpdkrngi fpaaagsraq prrwpvqvls ilcsllfail
      121 lafllaiayl ivkelhaenl kneddvdtgl lgmfpptpls parfkkltgh sfhmgysmai
      181 lngivaaltv awclm
//
LOCUS       NP_001382621            1715 aa            linear   PRI 21-NOV-2025
DEFINITION  endoribonuclease Dicer isoform 7 [Homo sapiens].
ACCESSION   NP_001382621
VERSION     NP_001382621.1
DBSOURCE    REFSEQ: accession NM_001395692.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1715)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1715)
  AUTHORS   Rojo-Pardillo,M., Godefroid,L., Dom,G., Lefort,A., Libert,F.,
            Robaye,B. and Maenhaut,C.
  TITLE     Understanding the Dosage-Dependent Role of Dicer1 in Thyroid
            Tumorigenesis
  JOURNAL   Int J Mol Sci 25 (19), 10701 (2024)
   PUBMED   39409030
  REMARK    GeneRIF: Understanding the Dosage-Dependent Role of Dicer1 in
            Thyroid Tumorigenesis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1715)
  AUTHORS   Mastnikova,K., Bulanova Pekova,B., Kuklikova,V., Vaclavikova,E.,
            Carkova,J., Katra,R., Fialova,L., Vlcek,P., Kodetova,D.,
            Chovanec,M., Drozenova,J., Matej,R., Pacesova,P., Novak,Z.,
            Procykova,K., Vcelak,J. and Bendlova,B.
  TITLE     DICER1 Variants in Pediatric and Young Adult Thyroid Nodules
  JOURNAL   Thyroid 34 (10), 1225-1233 (2024)
   PUBMED   39283830
  REMARK    GeneRIF: DICER1 Variants in Pediatric and Young Adult Thyroid
            Nodules.
REFERENCE   4  (residues 1 to 1715)
  AUTHORS   Dashti,N.K., Swanson,A.A., Bentz,J., Xing,D., Chrisinger,J.S.A.,
            Balzer,B., Guo,R., Schoolmeester,J.K. and Maluf,H.
  TITLE     DICER1-sarcomas of GYN tract: Expanding on an emerging entity
  JOURNAL   Hum Pathol 152, 105636 (2024)
   PUBMED   39127354
  REMARK    GeneRIF: DICER1-sarcomas of GYN tract: Expanding on an emerging
            entity.
REFERENCE   5  (residues 1 to 1715)
  AUTHORS   Irvin-Wilson,C.V. and Chaudhuri,G.
  TITLE     Alternative initiation and splicing in dicer gene expression in
            human breast cells
  JOURNAL   Breast Cancer Res 7 (4), R563-R569 (2005)
   PUBMED   15987463
REFERENCE   6  (residues 1 to 1715)
  AUTHORS   Bignell,G.R., Canzian,F., Shayeghi,M., Stark,M., Shugart,Y.Y.,
            Biggs,P., Mangion,J., Hamoudi,R., Rosenblatt,J., Buu,P., Sun,S.,
            Stoffer,S.S., Goldgar,D.E., Romeo,G., Houlston,R.S., Narod,S.A.,
            Stratton,M.R. and Foulkes,W.D.
  TITLE     Familial nontoxic multinodular thyroid goiter locus maps to
            chromosome 14q but does not account for familial nonmedullary
            thyroid cancer
  JOURNAL   Am J Hum Genet 61 (5), 1123-1130 (1997)
   PUBMED   9345104
REFERENCE   7  (residues 1 to 1715)
  AUTHORS   Schultz,K.A.P., Stewart,D.R., Kamihara,J., Bauer,A.J.,
            Merideth,M.A., Stratton,P., Huryn,L.A., Harris,A.K., Doros,L.,
            Field,A., Carr,A.G., Dehner,L.P., Messinger,Y. and Hill,D.A.
  TITLE     DICER1 Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24761742
REFERENCE   8  (residues 1 to 1715)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   9  (residues 1 to 1715)
  AUTHORS   Couch,R.M., Hughes,I.A., DeSa,D.J., Schiffrin,A., Guyda,H. and
            Winter,J.S.
  TITLE     An autosomal dominant form of adolescent multinodular goiter
  JOURNAL   Am J Hum Genet 39 (6), 811-816 (1986)
   PUBMED   3799599
REFERENCE   10 (residues 1 to 1715)
  AUTHORS   Murray,I.P., Thomson,J.A., McGirr,E.M., Macdonald,E.M.,
            Kennedy,J.S. and McLennan,I.
  TITLE     Unusual familial goiter associated with intrathyroidal
            calcification
  JOURNAL   J Clin Endocrinol Metab 26 (10), 1039-1049 (1966)
   PUBMED   4162574
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL356017.3 and AL390254.6.
            
            Summary: This gene encodes a protein possessing an RNA helicase
            motif containing a DEXH box in its amino terminus and an RNA motif
            in the carboxy terminus. The encoded protein functions as a
            ribonuclease and is required by the RNA interference and small
            temporal RNA (stRNA) pathways to produce the active small RNA
            component that represses gene expression. This protein also acts as
            a strong antiviral agent with activity against RNA viruses,
            including the Zika and SARS-CoV-2 viruses. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jul
            2021].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.103054.1,
                                           SRR18074969.1607426.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1715
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.13"
     Protein         1..1715
                     /product="endoribonuclease Dicer isoform 7"
                     /EC_number="3.1.26.3"
                     /note="dicer 1, double-stranded RNA-specific
                     endoribonuclease; helicase with RNAse motif;
                     endoribonuclease Dicer; helicase MOI; Dicer1, Dcr-1
                     homolog; dicer 1, ribonuclease type III"
                     /calculated_mol_wt=194958
     Region          42..239
                     /region_name="DEXHc_dicer"
                     /note="DEXH-box helicase domain of endoribonuclease Dicer;
                     cd18034"
                     /db_xref="CDD:350792"
     Site            order(42..45,48,65..72,113,176,207)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350792"
     Site            order(101..102,125..126,151,153..154,157,182..184)
                     /site_type="other"
                     /note="nucleic acid binding site [nucleotide binding]"
                     /db_xref="CDD:350792"
     Region          175..178
                     /region_name="DECH box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Region          256..595
                     /region_name="Required for interaction with PRKRA and
                     TARBP2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Region          271..365
                     /region_name="Dicer_PBD"
                     /note="Partner-binding domain of the endoribonuclease
                     Dicer; cd15903"
                     /db_xref="CDD:277191"
     Site            order(276..277,280,282..283,342..343,346..347,350,
                     353..354,357)
                     /site_type="other"
                     /note="Trbp binding interface [polypeptide binding]"
                     /db_xref="CDD:277191"
     Region          372..564
                     /region_name="SF2_C_dicer"
                     /note="C-terminal helicase domain of the endoribonuclease
                     Dicer; cd18802"
                     /db_xref="CDD:350189"
     Region          409..433
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            order(449..451,521,540,542)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350189"
     Site            order(525,527,552,554)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350189"
     Region          630..718
                     /region_name="Dicer_dimer"
                     /note="Dicer dimerization domain; pfam03368"
                     /db_xref="CDD:460900"
     Region          886..1008
                     /region_name="PAZ_dicer_like"
                     /note="PAZ domain, dicer_like subfamily. Dicer is an RNAse
                     involved in cleaving dsRNA in the RNA interference
                     pathway. It generates dsRNAs which are approximately 20 bp
                     long (siRNAs), which in turn target hydrolysis of
                     homologous RNAs. PAZ domains are named...; cd02843"
                     /db_xref="CDD:239209"
     Site            order(949,962,968,972,990,998,1000)
                     /site_type="other"
                     /note="nucleic acid-binding interface [nucleotide
                     binding]"
                     /db_xref="CDD:239209"
     Site            1016
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            1160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Region          1296..>1387
                     /region_name="RIBOc"
                     /note="Ribonuclease III family; smart00535"
                     /db_xref="CDD:197778"
     Site            order(1313..1314,1317..1318,1321,1324..1325,1328..1329,
                     1331..1333,1343)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238333"
     Site            1460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            1468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R418; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Site            1470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY3.3)"
     Region          1669..>1708
                     /region_name="RIBOc"
                     /note="Ribonuclease III C terminal domain. This group
                     consists of eukaryotic, bacterial and archeal ribonuclease
                     III (RNAse III) proteins. RNAse III is a double stranded
                     RNA-specific endonuclease. Prokaryotic RNAse III is
                     important in post-transcriptional...; cl00258"
                     /db_xref="CDD:469693"
     CDS             1..1715
                     /gene="DICER1"
                     /gene_synonym="aviD; DCR1; Dicer; Dicer1e; GLOW; HERNA;
                     K12H4.8-LIKE; MNG1; RMSE2"
                     /coded_by="NM_001395692.1:513..5660"
                     /note="isoform 7 is encoded by transcript variant 21"
                     /db_xref="CCDS:CCDS91926.1"
                     /db_xref="GeneID:23405"
                     /db_xref="HGNC:HGNC:17098"
                     /db_xref="MIM:606241"
ORIGIN      
        1 mkspalqpls maglqlmtpa sspmgpffgl pwqqeaihdn iytprkyqve lleaaldhnt
       61 ivclntgsgk tfiavlltke lsyqirgdfs rngkrtvflv nsanqvaqqv savrthsdlk
      121 vgeysnlevn aswtkerwnq eftkhqvlim tcyvalnvlk ngylslsdin llvfdechla
      181 ildhpyreim klcencpscp rilgltasil ngkcdpeele ekiqklekil ksnaetatdl
      241 vvldrytsqp ceivvdcgpf tdrsglyerl lmeleealnf indcnisvhs kerdstlisk
      301 qilsdcravl vvlgpwcadk vagmmvrelq kyikheqeel hrkfllftdt flrkihalce
      361 ehfspasldl kfvtpkvikl leilrkykpy erqqfesvew ynnrnqdnyv swsdseddde
      421 deeieekekp etnfpspftn ilcgiifver rytavvlnrl ikeagkqdpe layissnfit
      481 ghgigknqpr nkqmeaefrk qeevlrkfra hetnlliats iveegvdipk cnlvvrfdlp
      541 teyrsyvqsk grarapisny imladtdkik sfeedlktyk aiekilrnkc sksvdtgetd
      601 idpvmddddv fppyvlrpdd ggprvtinta ighinrycar lpsdpfthla pkcrtrelpd
      661 gtfystlylp insplrasiv gppmscvrla ervvalicce klhkigeldd hlmpvgketv
      721 kyeeeldlhd eeetsvpgrp gstkrrqcyp kaipeclrds yprpdqpcyl yvigmvlttp
      781 lpdelnfrrr klyppedttr cfgiltakpi pqiphfpvyt rsgevtisie lkksgfmlsl
      841 qmlelitrlh qyifshilrl ekpalefkpt dadsaycvlp lnvvndsstl didfkfmedi
      901 eksearigip stkytketpf vfkledyqda viipryrnfd qphrfyvadv ytdltplskf
      961 pspeyetfae yyktkynldl tnlnqplldv dhtssrlnll tprhlnqkgk alplssaekr
     1021 kakweslqnk qilvpelcai hpipaslwrk avclpsilyr lhclltaeel raqtasdagv
     1081 gvrslpadfr ypnldfgwkk sidsksfisi snsssaendn yckhstivpe naahqganrt
     1141 sslenhdqms vncrtllses pgklhvevsa dltainglsy nqnlangsyd lanrdfcqgn
     1201 qlnyykqeip vqpttsysiq nlysyenqpq psdectllsn kyldgnanks tsdgspvmav
     1261 mpgttdtiqv lkgrmdseqs psigyssrtl gpnpglilqa ltlsnasdgf nlerlemlgd
     1321 sflkhaitty lfctypdahe grlsymrskk vsncnlyrlg kkkglpsrmv vsifdppvnw
     1381 lppgyvvnqd ksntdkwekd emtkdcmlan gkldedyeee deeeeslmwr apkeeadyed
     1441 dfleydqehi rfidnmlmgs gafvkkisls pfsttdsaye wkmpkksslg smpfssdfed
     1501 fdysswdamc yldpskavee ddfvvgfwnp seencgvdtg kqsisydlht eqciadksia
     1561 dcveallgcy ltscgeraaq lflcslglkv lpvikrtdre kalcptrenf nsqqknlsvs
     1621 caaasvassr ssvlkdseyg clkipprcmf dhpdadktln hlisgfenfe kkinyrfknk
     1681 ayllqaftha syhyntitgk epttrlhfwe netlc
//
LOCUS       NP_001378835            1641 aa            linear   PRI 21-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4 gamma 3 isoform 14 [Homo
            sapiens].
ACCESSION   NP_001378835 XP_016858167
VERSION     NP_001378835.1
DBSOURCE    REFSEQ: accession NM_001391906.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1641)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1641)
  AUTHORS   Kang,J.Y., Wen,Z., Pan,D., Zhang,Y., Li,Q., Zhong,A., Yu,X.,
            Wu,Y.C., Chen,Y., Zhang,X., Kou,P.C., Geng,J., Wang,Y.Y., Hua,M.M.,
            Zong,R., Li,B., Shi,H.J., Li,D., Fu,X.D., Li,J., Nelson,D.L.,
            Guo,X., Zhou,Y., Gou,L.T., Huang,Y. and Liu,M.F.
  TITLE     LLPS of FXR1 drives spermiogenesis by activating translation of
            stored mRNAs
  JOURNAL   Science 377 (6607), eabj6647 (2022)
   PUBMED   35951695
REFERENCE   3  (residues 1 to 1641)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1641)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 1641)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1641)
  AUTHORS   Waskiewicz,A.J., Johnson,J.C., Penn,B., Mahalingam,M., Kimball,S.R.
            and Cooper,J.A.
  TITLE     Phosphorylation of the cap-binding protein eukaryotic translation
            initiation factor 4E by protein kinase Mnk1 in vivo
  JOURNAL   Mol Cell Biol 19 (3), 1871-1880 (1999)
   PUBMED   10022874
REFERENCE   7  (residues 1 to 1641)
  AUTHORS   Pyronnet,S., Imataka,H., Gingras,A.C., Fukunaga,R., Hunter,T. and
            Sonenberg,N.
  TITLE     Human eukaryotic translation initiation factor 4G (eIF4G) recruits
            mnk1 to phosphorylate eIF4E
  JOURNAL   EMBO J 18 (1), 270-279 (1999)
   PUBMED   9878069
REFERENCE   8  (residues 1 to 1641)
  AUTHORS   Gingras,A.C., Raught,B. and Sonenberg,N.
  TITLE     eIF4 initiation factors: effectors of mRNA recruitment to ribosomes
            and regulators of translation
  JOURNAL   Annu Rev Biochem 68, 913-963 (1999)
   PUBMED   10872469
  REMARK    Review article
REFERENCE   9  (residues 1 to 1641)
  AUTHORS   Imataka,H., Gradi,A. and Sonenberg,N.
  TITLE     A newly identified N-terminal amino acid sequence of human eIF4G
            binds poly(A)-binding protein and functions in poly(A)-dependent
            translation
  JOURNAL   EMBO J 17 (24), 7480-7489 (1998)
   PUBMED   9857202
REFERENCE   10 (residues 1 to 1641)
  AUTHORS   Gradi,A., Imataka,H., Svitkin,Y.V., Rom,E., Raught,B., Morino,S.
            and Sonenberg,N.
  TITLE     A novel functional human eukaryotic translation initiation factor
            4G
  JOURNAL   Mol Cell Biol 18 (1), 334-342 (1998)
   PUBMED   9418880
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031005.2, AL627311.16,
            AL358392.19 and AL606477.11.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 14, 2021 this sequence version replaced XP_016858167.1.
            
            Summary: The protein encoded by this gene is thought to be part of
            the eIF4F protein complex, which is involved in mRNA cap
            recognition and transport of mRNAs to the ribosome. Interestingly,
            a microRNA (miR-520c-3p) has been found that negatively regulates
            synthesis of the encoded protein, and this leads to a global
            decrease in protein translation and cell proliferation. Therefore,
            this protein is a key component of the anti-tumor activity of
            miR-520c-3p. [provided by RefSeq, May 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000602326.6/ ENSP00000473510.2
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1641
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     Protein         1..1641
                     /product="eukaryotic translation initiation factor 4 gamma
                     3 isoform 14"
                     /note="eIF-4-gamma 3; eIF-4-gamma II"
                     /calculated_mol_wt=182985
     Region          <52..383
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          811..1039
                     /region_name="MIF4G"
                     /note="MIF4G domain; pfam02854"
                     /db_xref="CDD:397130"
     Region          1278..1390
                     /region_name="MA3"
                     /note="MA3 domain; pfam02847"
                     /db_xref="CDD:397128"
     Region          1484..1612
                     /region_name="W2_eIF4G1_like"
                     /note="C-terminal W2 domain of eukaryotic translation
                     initiation factor 4 gamma 1 and similar proteins; cd11559"
                     /db_xref="CDD:211397"
     Region          <1591..1637
                     /region_name="W2"
                     /note="C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon;
                     cl17013"
                     /db_xref="CDD:473053"
     CDS             1..1641
                     /gene="EIF4G3"
                     /gene_synonym="eIF-4G 3; eIF4G 3; eIF4GII"
                     /coded_by="NM_001391906.1:632..5557"
                     /note="isoform 14 is encoded by transcript variant 19"
                     /db_xref="CCDS:CCDS90876.1"
                     /db_xref="GeneID:8672"
                     /db_xref="HGNC:HGNC:3298"
                     /db_xref="MIM:603929"
ORIGIN      
        1 mnsqpqtrsp psrtvpihct dnwkrrkvle qtpvyrslag rgwikycifa agprpphhqg
       61 gfrpiqffqr pqiqpprati pnsspsirpg aqtptavyqa nqhimmvnhl pmpypvpqgp
      121 qycipqyrhs gppyvgppqq ypvqppgpgp fypgpgpgdf pnaygtpfyp sqpvyqsapi
      181 ivptqqqppp akrekktiri rdpnqggkdi teeimsgggs rnptppigrp tstptppqql
      241 psqvpehspv vygtvesahl aastpvtaas dqkqeekpkp dpvlkspspv lrlvlsgekk
      301 eqegqtsett aivsiaelpl ppspttvssv arstiaapts salssqpift taiddrcels
      361 spredtipip sltsctetsd plptnenddd ickkpcsvap ndiplvsstn lineingvse
      421 klsatesive ivkqevlplt leleilenpp eemklecipa pitpstvpsf pptpptppas
      481 pphtpvivpa aattvsspsa aitvqrvlee desirtclse dakeiqnkie veadgqteei
      541 ldsqnlnsrr spvpaqiait vpktwkkpkd rtrtteemle aelelkaeee lsidkvlese
      601 qdkmsqgfhp erdpsdlkkv kaveengeea epvrngaesv segegidans gstdssgdgv
      661 tfpfkpeswk ptdtegkkqy dreflldfqf mpaciqkpeg lppisdvvld kinqpklpmr
      721 tldprilprg pdftpafadf grqtpggrgv pllnvgsrrs qpgqrreprk iitvsvkedv
      781 hlkkaenawk psqkrdsqad dpeniktqel frkvrsilnk ltpqmfnqlm kqvsgltvdt
      841 eerlkgvidl vfekaideps fsvayanmcr clvtlkvpma dkpgntvnfr klllnrcqke
      901 fekdkadddv fekkqkelea asapeertrl hdeleeakdk arrrsignik figelfklkm
      961 lteaimhdcv vkllknhdee sleclcrllt tigkdldfek akprmdqyfn qmekivkerk
     1021 tssrirfmlq dvidlrlcnw vsrradqgpk tieqihkeak ieeqeeqrkv qqlmtkekrr
     1081 pgvqrvdegg wntvqgakns rvldpskflk itkptideki qlvpkaqlgs wgkgssggak
     1141 asetdalrss asslnrfsal qppapsgstp stpvefdsrr tltsrgsmgr ekndkplpsa
     1201 tarpntfmrg gsskdlldnq sqeeqrreml etvkqltggv dvernsteae rnktresakp
     1261 eisamsahdk aalseeeler ksksiidefl hindfkeamq cveelnaqgl lhvfvrvgve
     1321 stlersqitr dhmgqllyql vqseklskqd ffkgfsetle laddmaidip hiwlylaelv
     1381 tpmlkeggis mreltiefsk pllpvgragv llseilhllc kqmshkkvga lwreadlswk
     1441 dflpegedvh nflleqkldf iesdspcsse alskkelsae elykrlekli iedkandeqi
     1501 fdwveanlde iqmssptflr almtavckaa iiadsstfrv dtavikqrvp illkyldsdt
     1561 ekelqalyal qasivkldqp anllrmffdc lydeevised afykwesskd paeqngkgva
     1621 lksvtafftw lreaeeesed n
//
LOCUS       NP_001371802            1126 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 33 [Homo sapiens].
ACCESSION   NP_001371802
VERSION     NP_001371802.1
DBSOURCE    REFSEQ: accession NM_001384873.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1126)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1126)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1126)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1126)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1126)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1126)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1126)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1126)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1126)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1126)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1126
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1126
                     /product="microtubule-associated protein 4 isoform 33"
                     /note="MAP-4"
                     /calculated_mol_wt=117776
     Region          <549..893
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <905..926
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          966..995
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          997..1026
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          1028..1058
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1126
                     /gene="MAP4"
                     /coded_by="NM_001384873.1:96..3476"
                     /note="isoform 33 is encoded by transcript variant 119"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttges kslgmasgsg sptefleekm
      121 ayqeypnsqn wpedtnfcfq peqvvdpiqt gmspcntavv pqgwsvealn sphsesfvsp
      181 eavaeppqpt avplelakei emaseerppa qaleimmglk ttdmapsket emalakdmal
      241 atktevalak dmesptkldv tlakdmqpsm esdmalvkdm elptekeval vkdvrwptet
      301 dvssaknvvl ptetevapak dvtllketer aspikmdlap skdmgppken kketeraspi
      361 kmdlapskdm gppkenkivp akdlvllsei evaqandiis steissaekv alsseteval
      421 ardmtlppet nviltkdkal pleaevapvk dmaqlpetei apakdvapst vkevgllkdm
      481 splsetemal gkdvtpppet evvliknvcl ppemevalte dqvpalktea plakdgvltl
      541 annvtpakdv pplseteatp vpikdmeiaq tqkgisedsh leslqdvgqs aaptfmispe
      601 tvtgtgkkcs lpaeedsvle klgerkpcns qpselssets giarpeegrp vvsgtgndit
      661 tppnkelpps pekktkplat tqpaktstsk aktqptslpk qpapttiggl nkkpmslasg
      721 lvpaappkrp avasarpsil pskdvkpkpi adakapekra spskpasapa srsgskstqt
      781 vaktttaaav astgpssrsp stllpkkpta iktegkpaev kkmtaksvpa dlsrpkstst
      841 ssmkktttls gtapaagvvp srvkatpmps rpsttpfidk kptsakpsst tprlsrlatn
      901 tsapdlknvr skvgstenik hqpgggrakv ekkteaaatt rkpesnavtk tagpiasaqk
      961 qpagkvqivs kkvsyshiqs kcgskdnikh vpgggnvqiq nkkvdiskvs skcgskanik
     1021 hkpgggdvki esqklnfkek aqakvgsldn vghlpaggav ktegggseap lcpgppagee
     1081 paiseaapea gaptsasgln ghptlsgggd qreaqtldsq iqetsi
//
LOCUS       NP_004121                350 aa            linear   PRI 21-NOV-2025
DEFINITION  glycogenin-1 isoform 1 [Homo sapiens].
ACCESSION   NP_004121
VERSION     NP_004121.2
DBSOURCE    REFSEQ: accession NM_004130.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Fastman,N.M., Liu,Y., Ramanan,V., Merritt,H., Ambing,E.,
            DePaoli-Roach,A.A., Roach,P.J., Hurley,T.D., Mellem,K.T.,
            Ullman,J.C., Green,E., Morgans,D. Jr. and Tzitzilonis,C.
  TITLE     The structural mechanism of human glycogen synthesis by the
            GYS1-GYG1 complex
  JOURNAL   Cell Rep 40 (1), 111041 (2022)
   PUBMED   35793618
  REMARK    GeneRIF: The structural mechanism of human glycogen synthesis by
            the GYS1-GYG1 complex.
REFERENCE   2  (residues 1 to 350)
  AUTHORS   McCorvie,T.J., Loria,P.M., Tu,M., Han,S., Shrestha,L., Froese,D.S.,
            Ferreira,I.M., Berg,A.P. and Yue,W.W.
  TITLE     Molecular basis for the regulation of human glycogen synthase by
            phosphorylation and glucose-6-phosphate
  JOURNAL   Nat Struct Mol Biol 29 (7), 628-638 (2022)
   PUBMED   35835870
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Munoz Sosa,C.J., Issoglio,F.M. and Carrizo,M.E.
  TITLE     Crystal structure and mutational analysis of the human TRIM7 B30.2
            domain provide insights into the molecular basis of its binding to
            glycogenin-1
  JOURNAL   J Biol Chem 296, 100772 (2021)
   PUBMED   33989636
  REMARK    GeneRIF: Crystal structure and mutational analysis of the human
            TRIM7 B30.2 domain provide insights into the molecular basis of its
            binding to glycogenin-1.
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Lomako,J., Mazuruk,K., Lomako,W.M., Alonso,M.D., Whelan,W.J. and
            Rodriguez,I.R.
  TITLE     The human intron-containing gene for glycogenin maps to chromosome
            3, band q24
  JOURNAL   Genomics 33 (3), 519-522 (1996)
   PUBMED   8661012
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Barbetti,F., Rocchi,M., Bossolasco,M., Cordera,R., Sbraccia,P.,
            Finelli,P. and Consalez,G.G.
  TITLE     The human skeletal muscle glycogenin gene: cDNA, tissue expression
            and chromosomal localization
  JOURNAL   Biochem Biophys Res Commun 220 (1), 72-77 (1996)
   PUBMED   8602861
REFERENCE   8  (residues 1 to 350)
  AUTHORS   Cao,Y., Mahrenholz,A.M., DePaoli-Roach,A.A. and Roach,P.J.
  TITLE     Characterization of rabbit skeletal muscle glycogenin. Tyrosine 194
            is essential for function
  JOURNAL   J Biol Chem 268 (20), 14687-14693 (1993)
   PUBMED   8325847
REFERENCE   9  (residues 1 to 350)
  AUTHORS   Viskupic,E., Cao,Y., Zhang,W., Cheng,C., DePaoli-Roach,A.A. and
            Roach,P.J.
  TITLE     Rabbit skeletal muscle glycogenin. Molecular cloning and production
            of fully functional protein in Escherichia coli
  JOURNAL   J Biol Chem 267 (36), 25759-25763 (1992)
   PUBMED   1281472
REFERENCE   10 (residues 1 to 350)
  AUTHORS   Browner,M.F., Nakano,K., Bang,A.G. and Fletterick,R.J.
  TITLE     Human muscle glycogen synthase cDNA sequence: a negatively charged
            protein with an asymmetric charge distribution
  JOURNAL   Proc Natl Acad Sci U S A 86 (5), 1443-1447 (1989)
   PUBMED   2493642
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG702275.1, AF087942.1,
            AA191440.1 and AC021059.25.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 10, 2002 this sequence version replaced NP_004121.1.
            
            Summary: This gene encodes a member of the glycogenin family.
            Glycogenin is a glycosyltransferase that catalyzes the formation of
            a short glucose polymer from uridine diphosphate glucose in an
            autoglucosylation reaction. This reaction is followed by elongation
            and branching of the polymer, catalyzed by glycogen synthase and
            branching enzyme, to form glycogen. This gene is expressed in
            muscle and other tissues. Mutations in this gene result in glycogen
            storage disease XV. This gene has pseudogenes on chromosomes 1, 8
            and 13 respectively. Alternatively spliced transcript variants
            encoding different isoforms have been identified.[provided by
            RefSeq, Sep 2010].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF087942.1, AK312283.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000345003.9/ ENSP00000340736.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q24"
     Protein         1..350
                     /product="glycogenin-1 isoform 1"
                     /EC_number="2.4.1.186"
                     /note="GN-1; glycogenin glucosyltransferase"
                     /calculated_mol_wt=39253
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P46976.4)"
     Region          4..254
                     /region_name="GT8_Glycogenin"
                     /note="Glycogenin belongs the GT 8 family and initiates
                     the biosynthesis of glycogen; cd02537"
                     /db_xref="CDD:133018"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13280; propagated from
                     UniProtKB/Swiss-Prot (P46976.4)"
     Site            order(82..83,86,100,102..104,125,133..135,163..164,
                     191..192,212,214..215,218)
                     /site_type="active"
                     /note="substrate binding site [active]"
                     /db_xref="CDD:133018"
     Site            86
                     /site_type="other"
                     /note="Important for catalytic activity.
                     /evidence=ECO:0000250|UniProtKB:P13280; propagated from
                     UniProtKB/Swiss-Prot (P46976.4)"
     Site            order(102,104,212)
                     /site_type="active"
                     /note="Manganese binding site [active]"
                     /db_xref="CDD:133018"
     Site            order(124..125,164,182,184..185,189,193)
                     /site_type="active"
                     /note="dimer interface [active]"
                     /db_xref="CDD:133018"
     Site            195
                     /site_type="glycosylation"
                     /note="O-linked (Glc...) tyrosine.
                     /evidence=ECO:0000269|PubMed:22160680,
                     ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3U2U,
                     ECO:0007744|PDB:3U2V; propagated from UniProtKB/Swiss-Prot
                     (P46976.4)"
     Region          301..333
                     /region_name="Interaction with GYS1.
                     /evidence=ECO:0000269|PubMed:17055998"
                     /note="propagated from UniProtKB/Swiss-Prot (P46976.4)"
     CDS             1..350
                     /gene="GYG1"
                     /gene_synonym="GSD15; GYG"
                     /coded_by="NM_004130.4:102..1154"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3139.1"
                     /db_xref="GeneID:2992"
                     /db_xref="HGNC:HGNC:4699"
                     /db_xref="MIM:603942"
ORIGIN      
        1 mtdqafvtlt tndayakgal vlgsslkqhr ttrrlvvlat pqvsdsmrkv letvfdevim
       61 vdvldsgdsa hltlmkrpel gvtltklhcw sltqyskcvf mdadtlvlan iddlfdreel
      121 saapdpgwpd cfnsgvfvyq psvetynqll hlaseqgsfd ggdqgilntf fsswattdir
      181 khlpfiynls sisiysylpa fkvfgasakv vhflgrvkpw nytydpktks vkseahdpnm
      241 thpeflilww nifttnvlpl lqqfglvkdt csyvnvlsdl vytlafscgf crkedvsgai
      301 shlslgeipa maqpfvssee rkerweqgqa dymgadsfdn ikrkldtylq
//
LOCUS       NP_001337386             992 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 1 isoform 51 [Homo
            sapiens].
ACCESSION   NP_001337386
VERSION     NP_001337386.1
DBSOURCE    REFSEQ: accession NM_001350457.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 992)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 992)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 992)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 992)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 992)
  AUTHORS   Ruhle,F., Witten,A., Barysenka,A., Huge,A., Arning,A., Heller,C.,
            Krumpel,A., Mesters,R., Franke,A., Lieb,W., Riemenschneider,M.,
            Hiersche,M., Limperger,V., Nowak-Gottl,U. and Stoll,M.
  TITLE     Rare genetic variants in SMAP1, B3GAT2, and RIMS1 contribute to
            pediatric venous thromboembolism
  JOURNAL   Blood 129 (6), 783-790 (2017)
   PUBMED   28011674
  REMARK    GeneRIF: The study identified a region on chromosome 6 comprising
            the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus
            for pediatric venous thromboembolism.
REFERENCE   6  (residues 1 to 992)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 992)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
REFERENCE   8  (residues 1 to 992)
  AUTHORS   Schoch,S., Castillo,P.E., Jo,T., Mukherjee,K., Geppert,M., Wang,Y.,
            Schmitz,F., Malenka,R.C. and Sudhof,T.C.
  TITLE     RIM1alpha forms a protein scaffold for regulating neurotransmitter
            release at the active zone
  JOURNAL   Nature 415 (6869), 321-326 (2002)
   PUBMED   11797009
REFERENCE   9  (residues 1 to 992)
  AUTHORS   Coppola,T., Magnin-Luthi,S., Perret-Menoud,V., Gattesco,S.,
            Schiavo,G. and Regazzi,R.
  TITLE     Direct interaction of the Rab3 effector RIM with Ca2+ channels,
            SNAP-25, and synaptotagmin
  JOURNAL   J Biol Chem 276 (35), 32756-32762 (2001)
   PUBMED   11438518
REFERENCE   10 (residues 1 to 992)
  AUTHORS   Betz,A., Thakur,P., Junge,H.J., Ashery,U., Rhee,J.S., Scheuss,V.,
            Rosenmund,C., Rettig,J. and Brose,N.
  TITLE     Functional interaction of the active zone proteins Munc13-1 and
            RIM1 in synaptic vesicle priming
  JOURNAL   Neuron 30 (1), 183-196 (2001)
   PUBMED   11343654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590011.5, AL445256.18 and
            AL035633.18.
            
            Summary: The protein encoded by this gene is a RAS gene superfamily
            member that regulates synaptic vesicle exocytosis. This gene also
            plays a role in the regulation of voltage-gated calcium channels
            during neurotransmitter and insulin release. Mutations have
            suggested a role cognition and have been identified as the cause of
            cone-rod dystrophy type 7. Multiple transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Mar 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.24937.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..992
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..992
                     /product="regulating synaptic membrane exocytosis protein
                     1 isoform 51"
                     /note="RAB3-interacting protein 2; rab3-interacting
                     molecule 1; rab-3-interacting protein 2"
                     /calculated_mol_wt=110605
     Region          68..164
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(89..95,110,113,143,147,150..151)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          216..342
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(247,253,308,310,318)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          823..968
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(880,884..885,887,890,918,920,922,966..967)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..992
                     /gene="RIMS1"
                     /gene_synonym="CORD7; RAB3IP2; RIM; RIM1"
                     /coded_by="NM_001350457.2:231..3209"
                     /note="isoform 51 is encoded by transcript variant 51"
                     /db_xref="GeneID:22999"
                     /db_xref="HGNC:HGNC:17282"
                     /db_xref="MIM:606629"
ORIGIN      
        1 mcapgihvss egweevrsvd seegtiearr avagdldyyw ldpatwhsre tspisshpvt
       61 wqpskegdrl igrvilnkrt tmpkdsgall glkvvggkmt dlgrlgafit kvkkgsladv
      121 vghlragdev lewngkplpg atneevynii lesksepqve iivsrpigdi pripesshpp
      181 lesssssfes qkmerpsisv isptspgalk dapqvlpgql svklwydkvg hqlivnvlqa
      241 tdlparvdgr prnpyvkmyf lpdrsdkskr rtktvkkile pkwnqtfvys hvhrrdfrer
      301 mleitvwdqp rvqeeesefl geilieleta llddephwyk lqthdesslp lpqpspfmpr
      361 rhihgesssk klqrsqrisd sdisdyevdd gigvvppvgy rssareskst tltvpeqqrt
      421 thhrsrsvsp hrgndqgkpr srlpnvplqr sldeihptrr srsptrhhda srspvdhrtr
      481 dvdsqylseq dselqpfldr arsastnclr pdtslhsper erhsrksers siqkqtrkgt
      541 asdaermhrq rsptqsppad tsfssrrgrq lpqvpvrsgs ieqaslvvee rtrqmkmkvh
      601 rfkqttgsgs sqeldreqys kynihkdqyr scdnvsakss dsdvsdvsai srtssasrls
      661 stsfmseqse rprgrissft pkmqgrrmgt sgrsimksts vsgemytleh ndgsqsdtav
      721 gtvgaggkkr rsslsakvva ivsrrsrsts qlsqtesghk klkstiqrst etgmaaemrk
      781 mvrqpsrest dgsinsysse gnlifpgvrl gadsqfsdfl dglgpaqlvg rqtlatpamg
      841 diqigmedkk gqlevevira rsltqkpgsk stpapyvkvy llengaciak kktriarktl
      901 dplyqqslvf despqgkvlq vivwgdygrm dhkcfmgvaq illeeldlss mvigwyklfp
      961 psslvdptlt pltrrasqss lesstgppci rs
//
LOCUS       NP_001381772             616 aa            linear   PRI 21-NOV-2025
DEFINITION  kinesin light chain 1 isoform 15 [Homo sapiens].
ACCESSION   NP_001381772
VERSION     NP_001381772.1
DBSOURCE    REFSEQ: accession NM_001394843.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Kikuchi,M., Viet,J., Nagata,K., Sato,M., David,G., Audic,Y.,
            Silverman,M.A., Yamamoto,M., Akatsu,H., Hashizume,Y., Takeda,S.,
            Akamine,S., Miyamoto,T., Uozumi,R., Gotoh,S., Mori,K., Ikeda,M.,
            Paillard,L. and Morihara,T.
  TITLE     Gene-gene functional relationships in Alzheimer's disease: CELF1
            regulates KLC1 alternative splicing
  JOURNAL   Biochem Biophys Res Commun 721, 150025 (2024)
   PUBMED   38768546
  REMARK    GeneRIF: Gene-gene functional relationships in Alzheimer's disease:
            CELF1 regulates KLC1 alternative splicing.
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   6  (residues 1 to 616)
  AUTHORS   Gyoeva,F.K., Bybikova,E.M. and Minin,A.A.
  TITLE     An isoform of kinesin light chain specific for the Golgi complex
  JOURNAL   J Cell Sci 113 (Pt 11), 2047-2054 (2000)
   PUBMED   10806115
REFERENCE   7  (residues 1 to 616)
  AUTHORS   Khodjakov,A., Lizunova,E.M., Minin,A.A., Koonce,M.P. and
            Gyoeva,F.K.
  TITLE     A specific light chain of kinesin associates with mitochondria in
            cultured cells
  JOURNAL   Mol Biol Cell 9 (2), 333-343 (1998)
   PUBMED   9450959
REFERENCE   8  (residues 1 to 616)
  AUTHORS   Chernajovsky,Y., Brown,A. and Clark,J.
  TITLE     Human kinesin light (beta) chain gene: DNA sequence and functional
            characterization of its promoter and first exon
  JOURNAL   DNA Cell Biol 15 (11), 965-974 (1996)
   PUBMED   8945637
REFERENCE   9  (residues 1 to 616)
  AUTHORS   Goedert,M., Marsh,S. and Carter,N.
  TITLE     Localization of the human kinesin light chain gene (KNS2) to
            chromosome 14q32.3 by fluorescence in situ hybridization
  JOURNAL   Genomics 32 (1), 173-175 (1996)
   PUBMED   8786116
REFERENCE   10 (residues 1 to 616)
  AUTHORS   Cabeza-Arvelaiz,Y., Shih,L.C., Hardman,N., Asselbergs,F., Bilbe,G.,
            Schmitz,A., White,B., Siciliano,M.J. and Lachman,L.B.
  TITLE     Cloning and genetic characterization of the human kinesin
            light-chain (KLC) gene
  JOURNAL   DNA Cell Biol 12 (10), 881-892 (1993)
   PUBMED   8274221
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139300.6 and AL049840.8.
            
            Summary: Conventional kinesin is a tetrameric molecule composed of
            two heavy chains and two light chains, and transports various
            cargos along microtubules toward their plus ends. The heavy chains
            provide the motor activity, while the light chains bind to various
            cargos. This gene encodes a member of the kinesin light chain
            family. It associates with kinesin heavy chain through an
            N-terminal domain, and six tetratricopeptide repeat (TPR) motifs
            are thought to be involved in binding of cargos such as vesicles,
            mitochondria, and the Golgi complex. Thus, kinesin light chains
            function as adapter molecules and not motors per se. Although
            previously named 'kinesin 2', this gene is not a member of the
            kinesin-2 / kinesin heavy chain subfamily of kinesin motor
            proteins. Extensive alternative splicing produces isoforms with
            different C-termini that are proposed to bind to different cargos;
            however, the full-length nature and/or biological validity of most
            of these variants have not been determined. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA2142853 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..616
                     /product="kinesin light chain 1 isoform 15"
                     /EC_number="2.7.1.21"
                     /note="kinesin 2 60/70kDa; medulloblastoma antigen
                     MU-MB-2.50"
                     /calculated_mol_wt=69315
     Region          35..>149
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          210..433
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          214..241
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          295..323
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(296,299..300,303..304,306,338,341..342,345..346,
                     348..349,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          336..366
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          379..406
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..616
                     /gene="KLC1"
                     /gene_synonym="KLC; KNS2; KNS2A"
                     /coded_by="NM_001394843.1:286..2136"
                     /note="isoform 15 is encoded by transcript variant 15"
                     /db_xref="GeneID:3831"
                     /db_xref="HGNC:HGNC:6387"
                     /db_xref="MIM:600025"
ORIGIN      
        1 mydnmstmvy ikedkleklt qdeiisktkq viqglealkn ehnsilqsll etlkclkkdd
       61 esnlveeksn mirkslemle lglseaqvmm alsnhlnave sekqklraqv rrlcqenqwl
      121 rdelantqqk lqkseqsvaq leeekkhlef mnqlkkyddd ispsedkdtd stkeplddlf
      181 pndeddpgqg iqqqhssaaa aaqqggyeip arlrtlhnlv iqyasqgrye vavplckqal
      241 edlektsghd hpdvatmlni lalvdqnkyk daanllndal airektlgkd hpavaatlnn
      301 lavlygkrgk ykeaeplckr aleirekvlg kdhpdvakql nnlallcqnq gkyeeveyyy
      361 qraleiyqtk lgpddpnvak tknnlascyl kqgkfkqaet lykeiltrah erefgsvdde
      421 nkpiwmhaee reeckgkqkd gtsfgeyggw ykackvdspt vtttlknlga lyrrqgkfea
      481 aetleeaamr srkqgldnvh kqrvaevlnd penmekrrsr eslnvdvvky esgpdggeev
      541 smsvewngdg tgslkrsgsf sklrasirrs seklvrklkg gssresepkn pgaslaeplf
      601 vendssssgl edatan
//
LOCUS       NP_056496                204 aa            linear   PRI 21-NOV-2025
DEFINITION  B9 domain-containing protein 1 isoform b [Homo sapiens].
ACCESSION   NP_056496
VERSION     NP_056496.1
DBSOURCE    REFSEQ: accession NM_015681.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Okazaki,M., Kobayashi,T., Chiba,S., Takei,R., Liang,L., Nakayama,K.
            and Katoh,Y.
  TITLE     Formation of the B9-domain protein complex MKS1-B9D2-B9D1 is
            essential as a diffusion barrier for ciliary membrane proteins
  JOURNAL   Mol Biol Cell 31 (20), 2259-2268 (2020)
   PUBMED   32726168
  REMARK    GeneRIF: Formation of the B9-domain protein complex MKS1-B9D2-B9D1
            is essential as a diffusion barrier for ciliary membrane proteins.
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Hopp,K., Heyer,C.M., Hommerding,C.J., Henke,S.A., Sundsbak,J.L.,
            Patel,S., Patel,P., Consugar,M.B., Czarnecki,P.G., Gliem,T.J.,
            Torres,V.E., Rossetti,S. and Harris,P.C.
  TITLE     B9D1 is revealed as a novel Meckel syndrome (MKS) gene by targeted
            exon-enriched next-generation sequencing and deletion analysis
  JOURNAL   Hum Mol Genet 20 (13), 2524-2534 (2011)
   PUBMED   21493627
  REMARK    GeneRIF: B9D1 is a novel Meckel syndrome gene
REFERENCE   6  (residues 1 to 204)
  AUTHORS   Bialas,N.J., Inglis,P.N., Li,C., Robinson,J.F., Parker,J.D.,
            Healey,M.P., Davis,E.E., Inglis,C.D., Toivonen,T., Cottell,D.C.,
            Blacque,O.E., Quarmby,L.M., Katsanis,N. and Leroux,M.R.
  TITLE     Functional interactions between the ciliopathy-associated Meckel
            syndrome 1 (MKS1) protein and two novel MKS1-related (MKSR)
            proteins
  JOURNAL   J Cell Sci 122 (Pt 5), 611-624 (2009)
   PUBMED   19208769
  REMARK    GeneRIF: MKS-1 and MKS-1-related proteins 1 and 2 (MKSR-1/EPPB9,
            MKSR-2/B9D2), localize to transition zones/basal bodies of sensory
            cilia; subcellular localization is largely co-dependent, pointing
            to a functional relationship between the proteins
REFERENCE   7  (residues 1 to 204)
  AUTHORS   Williams,C.L., Winkelbauer,M.E., Schafer,J.C., Michaud,E.J. and
            Yoder,B.K.
  TITLE     Functional redundancy of the B9 proteins and nephrocystins in
            Caenorhabditis elegans ciliogenesis
  JOURNAL   Mol Biol Cell 19 (5), 2154-2168 (2008)
   PUBMED   18337471
  REMARK    GeneRIF: Ciliary transition zone localization.  Functions in a
            module with related proteins (MKS1 and B9D1) that cooperates with
            nephrocystins in ciliogenesis.
REFERENCE   8  (residues 1 to 204)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   9  (residues 1 to 204)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 204)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124066.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a B9 domain-containing protein, one of
            several that are involved in ciliogenesis. Alterations in
            expression of this gene have been found in a family with Meckel
            syndrome. Meckel syndrome has been associated with at least six
            different genes. This gene is located within the Smith-Magenis
            syndrome region on chromosome 17. [provided by RefSeq, Mar 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853559.13590.1,
                                           SRR14038192.3898986.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261499.11/ ENSP00000261499.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..204
                     /product="B9 domain-containing protein 1 isoform b"
                     /note="endothelial precursor protein B9; B9
                     domain-containing protein 1; MKS1-related protein 1; B9
                     protein domain 1"
                     /calculated_mol_wt=22644
     Region          11..174
                     /region_name="B9-C2"
                     /note="Ciliary basal body-associated, B9 protein;
                     pfam07162"
                     /db_xref="CDD:462108"
     Region          182..204
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPM9.1)"
     CDS             1..204
                     /gene="B9D1"
                     /gene_synonym="B9; EPPB9; JBTS27; MKS9; MKSR-1; MKSR1"
                     /coded_by="NM_015681.6:155..769"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS11205.1"
                     /db_xref="GeneID:27077"
                     /db_xref="HGNC:HGNC:24123"
                     /db_xref="MIM:614144"
ORIGIN      
        1 mataspsvfl lmvngqvesa qfpeyddlyc kycfvygqdw aptagleegi sqitsksqdv
       61 rqalvwnfpi dvtfkstnpy gwpqivlsvy gpdvfgndvv rgygavhvpf spgrhkrtip
      121 mfvpestskl qkftswfmgr rpeytdpkvv aqgegrevtr vrsqgfvtll fnvvtkdmrk
      181 lgydtgpsdt qgvlgpsppq sfpq
//
LOCUS       NP_001376605             315 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal-specific septin-3 isoform L [Homo sapiens].
ACCESSION   NP_001376605
VERSION     NP_001376605.1
DBSOURCE    REFSEQ: accession NM_001389676.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Toth,V., Vadaszi,H., Ravasz,L., Mittli,D., Matyas,D., Molnar,T.,
            Micsonai,A., Szaniszlo,T., Lorincz,P., Kovacs,R.A., Juhasz,T.,
            Beke-Somfai,T., Juhasz,G., Gyorffy,B.A., Kekesi,K.A. and Kardos,J.
  TITLE     Neuronal-specific septin-3 binds Atg8/LC3B, accumulates and
            localizes to autophagosomes during induced autophagy
  JOURNAL   Cell Mol Life Sci 79 (9), 471 (2022)
   PUBMED   35932293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Fischer,M., Frank,D., Rosler,R., Johnsson,N. and Gronemeyer,T.
  TITLE     Biochemical Characterization of a Human Septin Octamer
  JOURNAL   Front Cell Dev Biol 10, 771388 (2022)
   PUBMED   35309913
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 315)
  AUTHORS   Xue,J., Milburn,P.J., Hanna,B.T., Graham,M.E., Rostas,J.A. and
            Robinson,P.J.
  TITLE     Phosphorylation of septin 3 on Ser-91 by cGMP-dependent protein
            kinase-I in nerve terminals
  JOURNAL   Biochem J 381 (Pt 3), 753-760 (2004)
   PUBMED   15107017
REFERENCE   7  (residues 1 to 315)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   8  (residues 1 to 315)
  AUTHORS   Takehashi,M., Alioto,T., Stedeford,T., Persad,A.S., Banasik,M.,
            Masliah,E., Tanaka,S. and Ueda,K.
  TITLE     Septin 3 gene polymorphism in Alzheimer's disease
  JOURNAL   Gene Expr 11 (5-6), 263-270 (2004)
   PUBMED   15200238
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 315)
  AUTHORS   Methner,A., Leypoldt,F., Joost,P. and Lewerenz,J.
  TITLE     Human septin 3 on chromosome 22q13.2 is upregulated by neuronal
            differentiation
  JOURNAL   Biochem Biophys Res Commun 283 (1), 48-56 (2001)
   PUBMED   11322766
REFERENCE   10 (residues 1 to 315)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z99716.4.
            
            Summary: This gene belongs to the septin family of GTPases. Members
            of this family are required for cytokinesis. Expression is
            upregulated by retinoic acid in a human teratocarcinoma cell line.
            The specific function of this gene has not been determined.
            Alternative splicing of this gene results in several transcript
            variants encoding different isoforms. [provided by RefSeq, May
            2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.34703.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..315
                     /product="neuronal-specific septin-3 isoform L"
                     /note="neuronal-specific septin-3"
                     /calculated_mol_wt=35880
     Region          67..290
                     /region_name="CDC_Septin"
                     /note="CDC/Septin GTPase family; cd01850"
                     /db_xref="CDD:206649"
     Site            82..85
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            84..130
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Site            164..167
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            222..224
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     CDS             1..315
                     /gene="SEPTIN3"
                     /gene_synonym="bK250D10.3; SEP3; SEPT3"
                     /coded_by="NM_001389676.1:288..1235"
                     /note="isoform L is encoded by transcript variant L"
                     /db_xref="GeneID:55964"
                     /db_xref="HGNC:HGNC:10750"
                     /db_xref="MIM:608314"
ORIGIN      
        1 mskglpetrt daamselvpe prpkpavpmk pmsinsnllg yigidtiieq mrkktmktgf
       61 dfnimvvvie eggvkmkltv idtpgfgdqi nnencwepie kyineqyekf lkeevniark
      121 kripdtrvhc clyfisptgh slrpldlefm khlskvvnii pviakadtmt leeksefkqr
      181 vrkelevngi efypqkefde dledktendk irqesmpfav vgsdkeyqvn gkrvlgrktp
      241 wgiievenln hcefallrdf virthlqdlk evthnihyet yrakrlndng glppgegllg
      301 tvlppvpatp cptae
//
LOCUS       NP_001376514             114 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerases I, II, and III subunit RPABC3 isoform
            3 [Homo sapiens].
ACCESSION   NP_001376514
VERSION     NP_001376514.1
DBSOURCE    REFSEQ: accession NM_001389585.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Zhao,D., Liu,W., Chen,K., Wu,Z., Yang,H. and Xu,Y.
  TITLE     Structure of the human RNA polymerase I elongation complex
  JOURNAL   Cell Discov 7 (1), 97 (2021)
   PUBMED   34671025
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   6  (residues 1 to 114)
  AUTHORS   Kato,H., Sumimoto,H., Pognonec,P., Chen,C.H., Rosen,C.A. and
            Roeder,R.G.
  TITLE     HIV-1 Tat acts as a processivity factor in vitro in conjunction
            with cellular elongation factors
  JOURNAL   Genes Dev 6 (4), 655-666 (1992)
   PUBMED   1559613
REFERENCE   7  (residues 1 to 114)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
REFERENCE   8  (residues 1 to 114)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 114)
  AUTHORS   Southgate,C., Zapp,M.L. and Green,M.R.
  TITLE     Activation of transcription by HIV-1 Tat protein tethered to
            nascent RNA through another protein
  JOURNAL   Nature 345 (6276), 640-642 (1990)
   PUBMED   2190099
REFERENCE   10 (residues 1 to 114)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078797.20.
            
            Summary: The three eukaryotic RNA polymerases are complex
            multisubunit enzymes that play a central role in the transcription
            of nuclear genes. This gene encodes an essential and highly
            conserved subunit of RNA polymerase II that is shared by the other
            two eukaryotic DNA-directed RNA polymerases, I and III. Alternative
            splicing results in multiple transcript variants of this gene.
            [provided by RefSeq, Jul 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1597689.1,
                                           DRR138512.661409.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..114
                     /product="DNA-directed RNA polymerases I, II, and III
                     subunit RPABC3 isoform 3"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerases I, II, and III subunit
                     RPABC3; RPB8 homolog; DNA-directed RNA polymerase II
                     subunit H; DNA-directed RNA polymerases I, II, and III
                     17.1 kDa polypeptide; polymerase (RNA) II (DNA directed)
                     polypeptide H; polymerase (RNA) II subunit H"
                     /calculated_mol_wt=12827
     Region          <1..111
                     /region_name="RPOL8c"
                     /note="RNA polymerase subunit 8; smart00658"
                     /db_xref="CDD:197821"
     CDS             1..114
                     /gene="POLR2H"
                     /gene_synonym="RPABC3; RPB17; RPB8"
                     /coded_by="NM_001389585.1:932..1276"
                     /note="isoform 3 is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS63861.1"
                     /db_xref="GeneID:5437"
                     /db_xref="HGNC:HGNC:9195"
                     /db_xref="MIM:606023"
ORIGIN      
        1 mdlildvniq iypvdlgdkf rlviastlye dgtlddgeyn ptddrpsrad qfeyvmygkv
       61 yriegdetst eaatrlsayv syggllmrlq gdannlhgfe vdsrvyllmk klaf
//
LOCUS       NP_001381367             687 aa            linear   PRI 21-NOV-2025
DEFINITION  SUN domain-containing protein 2 isoform 7 [Homo sapiens].
ACCESSION   NP_001381367
VERSION     NP_001381367.1
DBSOURCE    REFSEQ: accession NM_001394438.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 687)
  AUTHORS   Zhang,Y., Kong,Y., Guo,H., Liu,Y., Zang,Y. and Li,J.
  TITLE     Inner nuclear membrane protein TMEM201 maintains endothelial cell
            migration and angiogenesis by interacting with the LINC complex
  JOURNAL   J Mol Cell Biol 14 (3) (2022)
   PUBMED   35311970
REFERENCE   4  (residues 1 to 687)
  AUTHORS   Cruz-Palomar,K., Hawkins,J., Vandal,C., Quenneville,J., Gagnon,E.
            and Lippe,R.
  TITLE     SUN2 Modulates the Propagation of HSV-1
  JOURNAL   J Virol 96 (9), e0045322 (2022)
   PUBMED   35435724
  REMARK    GeneRIF: SUN2 Modulates the Propagation of HSV-1.
REFERENCE   5  (residues 1 to 687)
  AUTHORS   Ji,J., Shen,J., Xu,Y., Xie,M., Qian,Q., Qiu,T., Shi,W., Ren,D.,
            Ma,J., Liu,W. and Liu,B.
  TITLE     FBXO2 targets glycosylated SUN2 for ubiquitination and degradation
            to promote ovarian cancer development
  JOURNAL   Cell Death Dis 13 (5), 442 (2022)
   PUBMED   35525855
  REMARK    GeneRIF: FBXO2 targets glycosylated SUN2 for ubiquitination and
            degradation to promote ovarian cancer development.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 687)
  AUTHORS   Hoffenberg,S., Liu,X., Nikolova,L., Hall,H.S., Dai,W., Baughn,R.E.,
            Dickey,B.F., Barbieri,M.A., Aballay,A., Stahl,P.D. and Knoll,B.J.
  TITLE     A novel membrane-anchored Rab5 interacting protein required for
            homotypic endosome fusion
  JOURNAL   J Biol Chem 275 (32), 24661-24669 (2000)
   PUBMED   10818110
REFERENCE   7  (residues 1 to 687)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   8  (residues 1 to 687)
  AUTHORS   Raff,J.W.
  TITLE     The missing (L) UNC?
  JOURNAL   Curr Biol 9 (18), R708-R710 (1999)
   PUBMED   10508607
  REMARK    Review article
REFERENCE   9  (residues 1 to 687)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
REFERENCE   10 (residues 1 to 687)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL021707.2.
            
            Summary: SUN1 (MIM 607723) and SUN2 are inner nuclear membrane
            (INM) proteins that play a major role in nuclear-cytoplasmic
            connection by formation of a 'bridge' across the nuclear envelope,
            known as the LINC complex, via interaction with the conserved
            luminal KASH domain of nesprins (e.g., SYNE1; MIM 608441) located
            in the outer nuclear membrane (ONM). The LINC complex provides a
            direct connection between the nuclear lamina and the cytoskeleton,
            which contributes to nuclear positioning and cellular rigidity
            (summary by Haque et al., 2010 [PubMed 19933576]).[supplied by
            OMIM, Nov 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2499139.1,
                                           SRR14038194.3220681.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..687
                     /product="SUN domain-containing protein 2 isoform 7"
                     /note="Sad1 unc-84 domain protein 2; protein unc-84
                     homolog B; SUN domain-containing protein 2; nuclear
                     envelope protein; rab5-interacting protein; sad1/unc-84
                     protein-like 2"
                     /calculated_mol_wt=76820
     Region          <248..>487
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          370..424
                     /region_name="SUN2_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 2 and similar proteins; cd21438"
                     /db_xref="CDD:410604"
     Site            order(370,373..374,377,380..381,384..385,387..388,
                     391..392,394..395,398..399,401..402,405,408..409,412,
                     415..416,419..420,422..424)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:410604"
     Region          451..508
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          551..685
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..687
                     /gene="SUN2"
                     /gene_synonym="rab5IP; UNC84B"
                     /coded_by="NM_001394438.1:274..2337"
                     /note="isoform 7 is encoded by transcript variant 15"
                     /db_xref="GeneID:25777"
                     /db_xref="HGNC:HGNC:14210"
                     /db_xref="MIM:613569"
ORIGIN      
        1 msrrsqrltr ysqgdddgss ssggssvags qstlfkdspl seslvheswf pprssleelh
       61 gdanwgedlr vrrrrgtggs essrasglvg rkatedflgs ssgysseddy vgysdvdqqs
      121 sssrlrsavs ragsllwmva tspgrlfrll ywwagttwyr lttaaslldv fvltrrfssl
      181 ktflwfllpl llltcltyga wyfypyglqt fhpalvswwa akdsrrpdeg weardssphf
      241 qaeqrvmsrv hslerrleal aaefssnwqk eamrlerlel rqgapgqggg gglshedtla
      301 lleglvsrre aalkedfrre taariqeels alraehqqds edlfkkivra sqeseariqq
      361 lksewqsmtq esfqessvke lrrledqlag lqqelaalal kqssvaeevg llpqqiqavr
      421 ddvesqfpaw isqflarggg grvgllqree mqaqlreles kilthvaemq gksareaaas
      481 lsltlqkegv igvteeqvhh ivkqalqrys edrigladya lesggasvis trcsetyetk
      541 tallslfgip lwyhsqsprv ilqpdvhpgn cwafqgpqgf avvrlsarir ptavtlehvp
      601 kalspnstis sapkdfaifg fdedlqqegt llgkftydqd gepiqtfhfq aptmatyqvv
      661 elriltnwgh peytciyrfr vhgepah
//
LOCUS       NP_001380835              28 aa            linear   PRI 21-NOV-2025
DEFINITION  26S proteasome complex subunit SEM1 isoform i [Homo sapiens].
ACCESSION   NP_001380835
VERSION     NP_001380835.1
DBSOURCE    REFSEQ: accession NM_001393906.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 28)
  AUTHORS   Huang,Y., Li,W., Foo,T., Ji,J.H., Wu,B., Tomimatsu,N., Fang,Q.,
            Gao,B., Long,M., Xu,J., Maqbool,R., Mukherjee,B., Ni,T., Alejo,S.,
            He,Y., Burma,S., Lan,L., Xia,B. and Zhao,W.
  TITLE     DSS1 restrains BRCA2's engagement with dsDNA for homologous
            recombination, replication fork protection, and R-loop homeostasis
  JOURNAL   Nat Commun 15 (1), 7081 (2024)
   PUBMED   39152168
  REMARK    GeneRIF: DSS1 restrains BRCA2's engagement with dsDNA for
            homologous recombination, replication fork protection, and R-loop
            homeostasis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 28)
  AUTHORS   Li,C., Chen,B., Zhang,J., Yang,J., Guo,M., Ren,Y., Zhou,Z.,
            Fung,K.M., Li,M., Zhang,L. and Liu,Z.
  TITLE     SEM1 promotes tumor progression of glioblastoma via activating the
            akt signaling pathway
  JOURNAL   Cancer Lett 577, 216368 (2023)
   PUBMED   37652287
  REMARK    GeneRIF: SEM1 promotes tumor progression of glioblastoma via
            activating the akt signaling pathway.
REFERENCE   3  (residues 1 to 28)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   4  (residues 1 to 28)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   5  (residues 1 to 28)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 28)
  AUTHORS   Marston,N.J., Richards,W.J., Hughes,D., Bertwistle,D.,
            Marshall,C.J. and Ashworth,A.
  TITLE     Interaction between the product of the breast cancer susceptibility
            gene BRCA2 and DSS1, a protein functionally conserved from yeast to
            mammals
  JOURNAL   Mol Cell Biol 19 (7), 4633-4642 (1999)
   PUBMED   10373512
REFERENCE   7  (residues 1 to 28)
  AUTHORS   Jantti,J., Lahdenranta,J., Olkkonen,V.M., Soderlund,H. and
            Keranen,S.
  TITLE     SEM1, a homologue of the split hand/split foot malformation
            candidate gene Dss1, regulates exocytosis and pseudohyphal
            differentiation in yeast
  JOURNAL   Proc Natl Acad Sci U S A 96 (3), 909-914 (1999)
   PUBMED   9927667
REFERENCE   8  (residues 1 to 28)
  AUTHORS   Crackower,M.A., Scherer,S.W., Rommens,J.M., Hui,C.C., Poorkaj,P.,
            Soder,S., Cobben,J.M., Hudgins,L., Evans,J.P. and Tsui,L.C.
  TITLE     Characterization of the split hand/split foot malformation locus
            SHFM1 at 7q21.3-q22.1 and analysis of a candidate gene for its
            expression during limb development
  JOURNAL   Hum Mol Genet 5 (5), 571-579 (1996)
   PUBMED   8733122
REFERENCE   9  (residues 1 to 28)
  AUTHORS   Roberts,S.H., Hughes,H.E., Davies,S.J. and Meredith,A.L.
  TITLE     Bilateral split hand and split foot malformation in a boy with a de
            novo interstitial deletion of 7q21.3
  JOURNAL   J Med Genet 28 (7), 479-481 (1991)
   PUBMED   1895319
REFERENCE   10 (residues 1 to 28)
  AUTHORS   Sharland,M., Patton,M.A. and Hill,L.
  TITLE     Ectrodactyly of hands and feet in a child with a complex
            translocation including 7q21.2
  JOURNAL   Am J Med Genet 39 (4), 413-414 (1991)
   PUBMED   1877619
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073230.8.
            
            Summary: The product of this gene has been localized within the
            split hand/split foot malformation locus SHFM1 at chromosome 7. It
            has been proposed to be a candidate gene for the autosomal dominant
            form of the heterogeneous limb developmental disorder split
            hand/split foot malformation type 1. In addition, it has been shown
            to directly interact with BRCA2. It also may play a role in the
            completion of the cell cycle. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14243140.8891661.1,
                                           DRR138523.586014.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..28
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.3"
     Protein         1..28
                     /product="26S proteasome complex subunit SEM1 isoform i"
                     /note="deleted in split-hand/split-foot 1; SEM1 26S
                     proteasome complex subunit; 26S proteasome complex subunit
                     DSS1; split hand/foot malformation (ectrodactyly) type 1;
                     split hand/foot deleted protein 1; deleted in split
                     hand/split foot protein 1; split hand/foot malformation
                     type 1 protein; 26S proteasome complex subunit SEM1"
                     /calculated_mol_wt=3150
     CDS             1..28
                     /gene="SEM1"
                     /gene_synonym="C7orf76; DSS1; ECD; PSMD15; SHFD1; Shfdg1;
                     SHFM1; SHSF1"
                     /coded_by="NM_001393906.1:84..170"
                     /note="isoform i is encoded by transcript variant 17"
                     /db_xref="GeneID:7979"
                     /db_xref="HGNC:HGNC:10845"
                     /db_xref="MIM:601285"
ORIGIN      
        1 msekkqpvdl glleeddefe efpaeeln
//
LOCUS       NP_647477                653 aa            linear   PRI 21-NOV-2025
DEFINITION  amphiphysin isoform 2 [Homo sapiens].
ACCESSION   NP_647477
VERSION     NP_647477.1
DBSOURCE    REFSEQ: accession NM_139316.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 653)
  AUTHORS   Yao,X., Zhang,C., Zhang,Y., Geng,J., Bai,S., Hao,Y. and Guan,Y.
  TITLE     Amphiphysin-IgG autoimmune sciatic neuropathy and facial neuropathy
            related to primary central nervous system lymphoma: A case report
  JOURNAL   J Neuroimmunol 382, 578156 (2023)
   PUBMED   37556888
  REMARK    GeneRIF: Amphiphysin-IgG autoimmune sciatic neuropathy and facial
            neuropathy related to primary central nervous system lymphoma: A
            case report.
REFERENCE   3  (residues 1 to 653)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 653)
  AUTHORS   Zhang,X., Zou,L., Meng,L., Xiong,M., Pan,L., Chen,G., Zheng,Y.,
            Xiong,J., Wang,Z., Duong,D.M., Zhang,Z., Cao,X., Wang,T., Tang,L.,
            Ye,K. and Zhang,Z.
  TITLE     Amphiphysin I cleavage by asparagine endopeptidase leads to tau
            hyperphosphorylation and synaptic dysfunction
  JOURNAL   Elife 10, e65301 (2021)
   PUBMED   34018922
  REMARK    GeneRIF: Amphiphysin I cleavage by asparagine endopeptidase leads
            to tau hyperphosphorylation and synaptic dysfunction.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 653)
  AUTHORS   David,C., McPherson,P.S., Mundigl,O. and de Camilli,P.
  TITLE     A role of amphiphysin in synaptic vesicle endocytosis suggested by
            its binding to dynamin in nerve terminals
  JOURNAL   Proc Natl Acad Sci U S A 93 (1), 331-335 (1996)
   PUBMED   8552632
REFERENCE   6  (residues 1 to 653)
  AUTHORS   Auffray,C., Behar,G., Bois,F., Bouchier,C., Da Silva,C.,
            Devignes,M.D., Duprat,S., Houlgatte,R., Jumeau,M.N., Lamy,B. et al.
  TITLE     [IMAGE: molecular integration of the analysis of the human genome
            and its expression]
  JOURNAL   C R Acad Sci III 318 (2), 263-272 (1995)
   PUBMED   7757816
REFERENCE   7  (residues 1 to 653)
  AUTHORS   Yamamoto,R., Li,X., Winter,S., Francke,U. and Kilimann,M.W.
  TITLE     Primary structure of human amphiphysin, the dominant autoantigen of
            paraneoplastic stiff-man syndrome, and mapping of its gene (AMPH)
            to chromosome 7p13-p14
  JOURNAL   Hum Mol Genet 4 (2), 265-268 (1995)
   PUBMED   7757077
REFERENCE   8  (residues 1 to 653)
  AUTHORS   David,C., Solimena,M. and De Camilli,P.
  TITLE     Autoimmunity in stiff-Man syndrome with breast cancer is targeted
            to the C-terminal region of human amphiphysin, a protein similar to
            the yeast proteins, Rvs167 and Rvs161
  JOURNAL   FEBS Lett 351 (1), 73-79 (1994)
   PUBMED   8076697
REFERENCE   9  (residues 1 to 653)
  AUTHORS   De Camilli,P., Thomas,A., Cofiell,R., Folli,F., Lichte,B.,
            Piccolo,G., Meinck,H.M., Austoni,M., Fassetta,G., Bottazzo,G.,
            Bates,D., Cartlidge,N., Solimena,M., Kilimann,M.W. et al.
  TITLE     The synaptic vesicle-associated protein amphiphysin is the 128-kD
            autoantigen of Stiff-Man syndrome with breast cancer
  JOURNAL   J Exp Med 178 (6), 2219-2223 (1993)
   PUBMED   8245793
REFERENCE   10 (residues 1 to 653)
  AUTHORS   Lichte,B., Veh,R.W., Meyer,H.E. and Kilimann,M.W.
  TITLE     Amphiphysin, a novel protein associated with synaptic vesicles
  JOURNAL   EMBO J 11 (7), 2521-2530 (1992)
   PUBMED   1628617
  REMARK    Erratum:[EMBO J 1992 Oct;11(10):3809]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF034996.1.
            
            Summary: This gene encodes a protein associated with the
            cytoplasmic surface of synaptic vesicles. A subset of patients with
            stiff-man syndrome who were also affected by breast cancer are
            positive for autoantibodies against this protein. Alternate
            splicing of this gene results in two transcript variants encoding
            different isoforms. Additional splice variants have been described,
            but their full length sequences have not been determined. A
            pseudogene of this gene is found on chromosome 11.[provided by
            RefSeq, Nov 2010].
            
            Transcript Variant: This variant (2) lacks an in-frame exon within
            the coding region compared to variant 1, resulting in a shorter
            protein (isoform 2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF034996.1, SRR14038191.377725.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.1"
     Protein         1..653
                     /product="amphiphysin isoform 2"
                     /note="amphiphysin (Stiff-Mann syndrome with breast cancer
                     128kD autoantigen); amphiphysin I"
                     /calculated_mol_wt=71798
     Region          26..236
                     /region_name="BAR_Amphiphysin_I_II"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin
                     I and II; cd07611"
                     /db_xref="CDD:153295"
     Site            order(45,48..49,53,56,59..60,63,73..74,76..77,80..81,
                     83..84,87,95,192,195..196,198,203..204,206..207,210..211,
                     213..214,217..218,220..221,225,228)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153295"
     Site            order(68,75,134,137,140..141,165)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153295"
     Region          <404..584
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
     Region          581..652
                     /region_name="SH3_Amphiphysin_I"
                     /note="Src Homology 3 domain of Amphiphysin I; cd12140"
                     /db_xref="CDD:213016"
     Site            order(592..598,617,619..622,645,647..648)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213016"
     CDS             1..653
                     /gene="AMPH"
                     /gene_synonym="AMPH1"
                     /coded_by="NM_139316.3:23..1984"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47574.1"
                     /db_xref="GeneID:273"
                     /db_xref="HGNC:HGNC:471"
                     /db_xref="MIM:600418"
ORIGIN      
        1 madiktgifa knvqkrlnra qekvlqklgk adetkdeqfe eyvqnfkrqe aegtrlqrel
       61 rgylaaikgm qeasmkltes lhevyepdwy gredvkmvge kcdvlwedfh qklvdgsllt
      121 ldtylgqfpd iknriakrsr klvdydsarh hlealqsskr kdesriskae eefqkaqkvf
      181 eefnvdlqee lpslwsrrvg fyvntfknvs sleakfhkei avlchklyev mtklgdqhad
      241 kaftiqgaps dsgplriakt psppeepspl psptaspnht lapaspapar prspsqtrkg
      301 ppvpplpkvt ptkelqqeni isffednfvp eisvttpsqn evpevkkeet lldldfdpfk
      361 pevtpagsag vthspmsqtl pwdlwttstd lvqpasggsf ngftqpqdts lftmqtdqsm
      421 icnliipgad adaavgtlvs aaegapgeea eaekatvpag egvsleeaki gtettegaes
      481 aqpeaeelea tvpqekvips vviepasnhe eegeneitig aepketteda appgptsetp
      541 elateqkpiq dpqptpsapa mgaadqlasa reasqelppg flykvetlhd feaansdelt
      601 lqrgdvvlvv psdseadqda gwlvgvkesd wlqyrdlaty kglfpenftr rld
//
LOCUS       NP_001372126            1150 aa            linear   PRI 21-NOV-2025
DEFINITION  non-receptor tyrosine-protein kinase TYK2 isoform 3 [Homo sapiens].
ACCESSION   NP_001372126
VERSION     NP_001372126.1
DBSOURCE    REFSEQ: accession NM_001385197.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1150)
  AUTHORS   Chen,H., Ge,X., Li,C., Zeng,J. and Wang,X.
  TITLE     Structure and assembly of the human IL-12 signaling complex
  JOURNAL   Structure 32 (10), 1640-1651 (2024)
   PUBMED   39111304
REFERENCE   2  (residues 1 to 1150)
  AUTHORS   Lesgidou,N. and Vlassi,M.
  TITLE     Community analysis of large-scale molecular dynamics simulations
            elucidated dynamics-driven allostery in tyrosine kinase 2
  JOURNAL   Proteins 92 (4), 474-498 (2024)
   PUBMED   37950407
  REMARK    GeneRIF: Community analysis of large-scale molecular dynamics
            simulations elucidated dynamics-driven allostery in tyrosine kinase
            2.
REFERENCE   3  (residues 1 to 1150)
  AUTHORS   Zhang,M., Liu,Z., Zhu,Y., Wu,K., Zhou,L., Peng,Y., Pan,J., Chen,B.,
            Wang,X. and Chen,S.
  TITLE     Associations of genetic variants within TYK2 with pulmonary
            tuberculosis among Chinese population
  JOURNAL   Mol Genet Genomic Med 12 (2), e2386 (2024)
   PUBMED   38337161
  REMARK    GeneRIF: Associations of genetic variants within TYK2 with
            pulmonary tuberculosis among Chinese population.
REFERENCE   4  (residues 1 to 1150)
  AUTHORS   Benmansour,R., Tagajdid,M.R., El Hamzaoui,H., Fjouji,S., Doghmi,N.,
            Houba,A., Belbacha,I., Elkochri,S., Aabi,R., Elannaz,H.,
            Laraqui,A., El Mchichi,B., Chmitah,T., Touil,N., Ennibi,K.,
            Eljaoudi,R., Elmir,E., Amine Lahlou,I. and Oumzil,H.
  TITLE     TYK2, IFITM3, IFNAR2 and OAS3 single-nucleotide polymorphisms among
            severe COVID-19 ICU patients in Morocco
  JOURNAL   Int J Immunopathol Pharmacol 38, 3946320241257241 (2024)
   PUBMED   38760017
  REMARK    GeneRIF: TYK2, IFITM3, IFNAR2 and OAS3 single-nucleotide
            polymorphisms among severe COVID-19 ICU patients in Morocco.
REFERENCE   5  (residues 1 to 1150)
  AUTHORS   Yang,Z., Xiang,Q. and Nicholas,J.
  TITLE     Direct and biologically significant interactions of human
            herpesvirus 8 interferon regulatory factor 1 with STAT3 and Janus
            kinase TYK2
  JOURNAL   PLoS Pathog 19 (11), e1011806 (2023)
   PUBMED   37983265
  REMARK    GeneRIF: Direct and biologically significant interactions of human
            herpesvirus 8 interferon regulatory factor 1 with STAT3 and Janus
            kinase TYK2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1150)
  AUTHORS   Tavernier,J., Tuypens,T., Plaetinck,G., Verhee,A., Fiers,W. and
            Devos,R.
  TITLE     Molecular basis of the membrane-anchored and two soluble isoforms
            of the human interleukin 5 receptor alpha subunit
  JOURNAL   Proc Natl Acad Sci U S A 89 (15), 7041-7045 (1992)
   PUBMED   1495999
REFERENCE   7  (residues 1 to 1150)
  AUTHORS   Velazquez,L., Fellous,M., Stark,G.R. and Pellegrini,S.
  TITLE     A protein tyrosine kinase in the interferon alpha/beta signaling
            pathway
  JOURNAL   Cell 70 (2), 313-322 (1992)
   PUBMED   1386289
REFERENCE   8  (residues 1 to 1150)
  AUTHORS   Partanen,J., Makela,T.P., Alitalo,R., Lehvaslaiho,H. and Alitalo,K.
  TITLE     Putative tyrosine kinases expressed in K-562 human leukemia cells
  JOURNAL   Proc Natl Acad Sci U S A 87 (22), 8913-8917 (1990)
   PUBMED   2247464
REFERENCE   9  (residues 1 to 1150)
  AUTHORS   Firmbach-Kraft,I., Byers,M., Shows,T., Dalla-Favera,R. and
            Krolewski,J.J.
  TITLE     tyk2, prototype of a novel class of non-receptor tyrosine kinase
            genes
  JOURNAL   Oncogene 5 (9), 1329-1336 (1990)
   PUBMED   2216457
REFERENCE   10 (residues 1 to 1150)
  AUTHORS   Krolewski,J.J., Lee,R., Eddy,R., Shows,T.B. and Dalla-Favera,R.
  TITLE     Identification and chromosomal mapping of new human tyrosine kinase
            genes
  JOURNAL   Oncogene 5 (3), 277-282 (1990)
   PUBMED   2156206
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011557.7.
            
            Summary: This gene encodes a member of the tyrosine kinase and,
            more specifically, the Janus kinases (JAKs) protein families. This
            protein associates with the cytoplasmic domain of type I and type
            II cytokine receptors and promulgate cytokine signals by
            phosphorylating receptor subunits. It is also a component of both
            the type I and type III interferon signaling pathways. As such, it
            may play a role in anti-viral immunity. A mutation in this gene has
            been associated with Immunodeficiency 35. [provided by RefSeq, Sep
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.16410.1,
                                           SRR11853559.16343.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1150
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..1150
                     /product="non-receptor tyrosine-protein kinase TYK2
                     isoform 3"
                     /EC_number="2.7.10.2"
                     /note="non-receptor tyrosine-protein kinase TYK2"
                     /calculated_mol_wt=129283
     Region          28..125
                     /region_name="FERM_F1"
                     /note="FERM F1 ubiquitin-like domain; pfam18379"
                     /db_xref="CDD:465733"
     Region          143..266
                     /region_name="FERM_F2"
                     /note="FERM F2 acyl-CoA binding protein-like domain;
                     pfam18377"
                     /db_xref="CDD:436450"
     Region          285..432
                     /region_name="Jak1_Phl"
                     /note="Jak1 pleckstrin homology-like domain; pfam17887"
                     /db_xref="CDD:465552"
     Region          437..534
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(457,474,504,506)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198244"
     Site            order(505,532)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198244"
     Region          589..867
                     /region_name="PTK_Tyk2_rpt1"
                     /note="Pseudokinase (repeat 1) domain of the Protein
                     Tyrosine Kinase, Tyrosine kinase 2; cd05076"
                     /db_xref="CDD:270661"
     Region          892..1137
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(903..906,909,911,928,930,960,978..981,1023,
                     1027..1028,1030,1040..1041)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..1150
                     /gene="TYK2"
                     /gene_synonym="IMD35; JTK1"
                     /coded_by="NM_001385197.1:379..3831"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92513.1"
                     /db_xref="GeneID:7297"
                     /db_xref="HGNC:HGNC:12440"
                     /db_xref="MIM:176941"
ORIGIN      
        1 mplrhwgmar gskpvgdgaq pmaamgglkv llhwagpggg epwvtfsess ltaeevcihi
       61 ahkvgitppc fnlfalfdaq aqvwlppnhi leiprdaslm lyfrirfyfr nwhgmnprep
      121 avyrcgppgt eassdqtaqg mqlldpasfe ylfeqgkhef vndvaslwel steeeihhfk
      181 neslgmaflh lchlalrhgi pleevakkts fkdciprsfr rhirqhsalt rlrlrnvfrr
      241 flrdfqpgrl sqqmvmvkyl atlerlaprf gtervpvchl rllaqaegep cyirdsgvap
      301 tdpgpesaag ppthevlvtg tggiqwwpve eevnkeegss gssgrnpqas lfgkkakahk
      361 avgqpadrpr eplwayfcdf rdithvvlke hcvsihrqdn kclelslpsr aaalsfvslv
      421 dgyfrltads shylchevap prlvmsirdg ihgpllepfv qaklrpedgl ylihwstshp
      481 yrliltvaqr sqapdgmqsl rlrkfpieqq dgafvlegwg rsfpsvrelg aalqgcllra
      541 gddcfslrrc clpqpgetsn liimrgaras prtlnlsqls fhrvdqkeit qlshlgqgtr
      601 tnvyegrlrv egsgdpeegk mddedplvpg rdrgqelrvv lkvldpshhd ialafyetas
      661 lmsqvshthl afvhgvcvrg penimvteyv ehgpldvwlr rerghvpmaw kmvvaqqlas
      721 alsylenknl vhgnvcgrni llarlglaeg tspfiklsdp gvglgalsre erveripwla
      781 peclpggans lstamdkwgf gatlleicfd geaplqsrsp sekehfyqrq hrlpepscpq
      841 latltsqclt yeptqrpsfr tilrdltrlq phnladvltv npdspasdpt vfhkrylkki
      901 rdlgeghfgk vslycydptn dgtgemvavk alkadcgpqh rsgwkqeidi lrtlyhehii
      961 kykgccedqg ekslqlvmey vplgslrdyl prhsiglaql llfaqqiceg maylhaqhyi
     1021 hrdlaarnvl ldndrlvkig dfglakavpe gheyyrvred gdspvfwyap eclkeykfyy
     1081 asdvwsfgvt lyellthcds sqspptvyhl mkncweteas frptfenlip ilktvhekyq
     1141 gqapsvfsvc
//
LOCUS       NP_071374                111 aa            linear   PRI 21-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 3 isoform b [Homo
            sapiens].
ACCESSION   NP_071374
VERSION     NP_071374.1
DBSOURCE    REFSEQ: accession NM_022091.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Makhlouf,L., Peter,J.J., Magnussen,H.M., Thakur,R., Millrine,D.,
            Minshull,T.C., Harrison,G., Varghese,J., Lamoliatte,F.,
            Foglizzo,M., Macartney,T., Calabrese,A.N., Zeqiraj,E. and
            Kulathu,Y.
  TITLE     The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER
            translocons
  JOURNAL   Nature 627 (8003), 437-444 (2024)
   PUBMED   38383789
REFERENCE   3  (residues 1 to 111)
  AUTHORS   DaRosa,P.A., Penchev,I., Gumbin,S.C., Scavone,F., Wachalska,M.,
            Paulo,J.A., Ordureau,A., Peter,J.J., Kulathu,Y., Harper,J.W.,
            Becker,T., Beckmann,R. and Kopito,R.R.
  TITLE     UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from
            the ER
  JOURNAL   Nature 627 (8003), 445-452 (2024)
   PUBMED   38383785
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Ao,Y.Q., Gao,J., Jin,C., Wang,S., Zhang,L.C., Deng,J., Chen,Z.W.,
            Wang,H.K., Jiang,J.H. and Ding,J.Y.
  TITLE     ASCC3 promotes the immunosuppression and progression of non-small
            cell lung cancer by impairing the type I interferon response via
            CAND1-mediated ubiquitination inhibition of STAT3
  JOURNAL   J Immunother Cancer 11 (12), e007766 (2023)
   PUBMED   38148115
  REMARK    GeneRIF: ASCC3 promotes the immunosuppression and progression of
            non-small cell lung cancer by impairing the type I interferon
            response via CAND1-mediated ubiquitination inhibition of STAT3.
            Erratum:[J Immunother Cancer. 2024 Jul 10;12(7):e007766corr1. doi:
            10.1136/jitc-2023-007766corr1. PMID: 38986545]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 111)
  AUTHORS   Li,J., Ding,S.C., Cho,H., Chung,B.C., Gale,M. Jr., Chanda,S.K. and
            Diamond,M.S.
  TITLE     A short hairpin RNA screen of interferon-stimulated genes
            identifies a novel negative regulator of the cellular antiviral
            response
  JOURNAL   mBio 4 (3), e00385-e00313 (2013)
   PUBMED   23781071
  REMARK    GeneRIF: Silencing of ASCC3 resulted in upregulation of multiple
            antiviral interferon-stimulated genes, which correlated with
            inhibition of infection of several positive-strand RNA viruses.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 111)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 111)
  AUTHORS   Dango,S., Mosammaparast,N., Sowa,M.E., Xiong,L.J., Wu,F., Park,K.,
            Rubin,M., Gygi,S., Harper,J.W. and Shi,Y.
  TITLE     DNA unwinding by ASCC3 helicase is coupled to ALKBH3-dependent DNA
            alkylation repair and cancer cell proliferation
  JOURNAL   Mol Cell 44 (3), 373-384 (2011)
   PUBMED   22055184
  REMARK    GeneRIF: DNA unwinding by ASCC3 helicase is coupled to
            ALKBH3-dependent DNA alkylation repair and cancer cell
            proliferation.
REFERENCE   8  (residues 1 to 111)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   9  (residues 1 to 111)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
REFERENCE   10 (residues 1 to 111)
  AUTHORS   Coulie,P.G., Ikeda,H., Baurain,J.F. and Chiari,R.
  TITLE     Antitumor immunity at work in a melanoma patient
  JOURNAL   Adv Cancer Res 76, 213-242 (1999)
   PUBMED   10218103
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK299117.1, AL133338.8,
            BC050681.1, BC130038.1 and BU686034.1.
            
            Summary: This gene encodes a protein that belongs to a family of
            helicases that are involved in the ATP-dependent unwinding of
            nucleic acid duplexes. The encoded protein is the largest subunit
            of the activating signal cointegrator 1 complex that is involved in
            DNA repair and resistance to alkylation damage. Alternate splicing
            results in multiple transcript variants. [provided by RefSeq, Sep
            2013].
            
            Transcript Variant: This variant (2) lacks several exons in the 3'
            coding region and includes an alternate 3' terminal exon compared
            to variant 1. The encoded protein (isoform b) has a distinct
            C-terminus and is shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC130038.1, SRR11853559.28405.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2151358,
                                           SAMEA2153031 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q16.3"
     Protein         1..111
                     /product="activating signal cointegrator 1 complex subunit
                     3 isoform b"
                     /EC_number="5.6.2.4"
                     /note="RNA helicase family; ASC-1 complex subunit P200;
                     helicase, ATP binding 1; trip4 complex subunit p200"
                     /calculated_mol_wt=12883
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3C0.3)"
     CDS             1..111
                     /gene="ASCC3"
                     /gene_synonym="ASC1p200; HELIC1; MRT81; RNAH"
                     /coded_by="NM_022091.5:311..646"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS5047.1"
                     /db_xref="GeneID:10973"
                     /db_xref="HGNC:HGNC:18697"
                     /db_xref="MIM:614217"
ORIGIN      
        1 malprltgal rsfsnvtkqd nyneevadlk ikrsklheqv ldlgltwkki ikflneklek
       61 skmqsinedl kdilhaakqi evncpfqkrr ldgkeedekm srasdrfrgl r
//
LOCUS       NP_001291278             427 aa            linear   PRI 21-NOV-2025
DEFINITION  cAMP-dependent protein kinase catalytic subunit alpha isoform 3
            [Homo sapiens].
ACCESSION   NP_001291278 XP_005260041
VERSION     NP_001291278.1
DBSOURCE    REFSEQ: accession NM_001304349.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Shirani,M., Levin,S., Shebl,B., Requena,D., Finkelstein,T.M.,
            Johnson,D.S., Ng,D., Lalazar,G., Heissel,S., Hojrup,P., Molina,H.,
            de Jong,Y.P., Rice,C.M., Singhi,A.D., Torbenson,M.S., Coffino,P.,
            Lyons,B. and Simon,S.M.
  TITLE     Increased Protein Kinase A Activity Induces Fibrolamellar
            Hepatocellular Carcinoma Features Independent of DNAJB1
  JOURNAL   Cancer Res 84 (16), 2626-2644 (2024)
   PUBMED   38888469
  REMARK    GeneRIF: Increased Protein Kinase A Activity Induces Fibrolamellar
            Hepatocellular Carcinoma Features Independent of DNAJB1.
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Beuschlein,F., Fassnacht,M., Assie,G., Calebiro,D., Stratakis,C.A.,
            Osswald,A., Ronchi,C.L., Wieland,T., Sbiera,S., Faucz,F.R.,
            Schaak,K., Schmittfull,A., Schwarzmayr,T., Barreau,O., Vezzosi,D.,
            Rizk-Rabin,M., Zabel,U., Szarek,E., Salpea,P., Forlino,A.,
            Vetro,A., Zuffardi,O., Kisker,C., Diener,S., Meitinger,T.,
            Lohse,M.J., Reincke,M., Bertherat,J., Strom,T.M. and Allolio,B.
  TITLE     Constitutive activation of PKA catalytic subunit in adrenal
            Cushing's syndrome
  JOURNAL   N Engl J Med 370 (11), 1019-1028 (2014)
   PUBMED   24571724
  REMARK    GeneRIF: Genetic alterations of the catalytic subunit of PKA were
            found to be associated with bilateral adrenal hyperplasias and
            unilateral cortisol-producing adrenal adenomas.
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Agustin,J.T., Wilkerson,C.G. and Witman,G.B.
  TITLE     The unique catalytic subunit of sperm cAMP-dependent protein kinase
            is the product of an alternative Calpha mRNA expressed specifically
            in spermatogenic cells
  JOURNAL   Mol Biol Cell 11 (9), 3031-3044 (2000)
   PUBMED   10982398
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Reinton,N., Orstavik,S., Haugen,T.B., Jahnsen,T., Tasken,K. and
            Skalhegg,B.S.
  TITLE     A novel isoform of human cyclic 3',5'-adenosine
            monophosphate-dependent protein kinase, c alpha-s, localizes to
            sperm midpiece
  JOURNAL   Biol Reprod 63 (2), 607-611 (2000)
   PUBMED   10906071
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Desseyn,J.L., Burton,K.A. and McKnight,G.S.
  TITLE     Expression of a nonmyristylated variant of the catalytic subunit of
            protein kinase A during male germ-cell development
  JOURNAL   Proc Natl Acad Sci U S A 97 (12), 6433-6438 (2000)
   PUBMED   10841548
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Da Silva,J.D., Tkachenko,N. and Soares,A.R.
  TITLE     Ellis-van Creveld Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37903214
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Maldonado,F. and Hanks,S.K.
  TITLE     A cDNA clone encoding human cAMP-dependent protein kinase catalytic
            subunit C alpha
  JOURNAL   Nucleic Acids Res 16 (16), 8189-8190 (1988)
   PUBMED   2843813
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Shoji,S., Titani,K., Demaille,J.G. and Fischer,E.H.
  TITLE     Sequence of two phosphorylated sites in the catalytic subunit of
            bovine cardiac muscle adenosine 3':5'-monophosphate-dependent
            protein kinase
  JOURNAL   J Biol Chem 254 (14), 6211-6214 (1979)
   PUBMED   221492
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Joh,T.H., Park,D.H. and Reis,D.J.
  TITLE     Direct phosphorylation of brain tyrosine hydroxylase by cyclic
            AMP-dependent protein kinase: mechanism of enzyme activation
  JOURNAL   Proc Natl Acad Sci U S A 75 (10), 4744-4748 (1978)
   PUBMED   33381
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK131561.1, BC108259.1 and
            BC039846.1.
            
            On Jan 17, 2015 this sequence version replaced XP_005260041.1.
            
            Summary: This gene encodes one of the catalytic subunits of protein
            kinase A, which exists as a tetrameric holoenzyme with two
            regulatory subunits and two catalytic subunits, in its inactive
            form. cAMP causes the dissociation of the inactive holoenzyme into
            a dimer of regulatory subunits bound to four cAMP and two free
            monomeric catalytic subunits. Four different regulatory subunits
            and three catalytic subunits have been identified in humans.
            cAMP-dependent phosphorylation of proteins by protein kinase A is
            important to many cellular processes, including differentiation,
            proliferation, and apoptosis. Constitutive activation of this gene
            caused either by somatic mutations, or genomic duplications of
            regions that include this gene, have been associated with
            hyperplasias and adenomas of the adrenal cortex and are linked to
            corticotropin-independent Cushing's syndrome. Alternative splicing
            results in multiple transcript variants encoding different
            isoforms. Tissue-specific isoforms that differ at the N-terminus
            have been described, and these isoforms may differ in the
            post-translational modifications that occur at the N-terminus of
            some isoforms. [provided by RefSeq, Jan 2015].
            
            Transcript Variant: This variant (3) contains an alternate 5'
            terminal exon and initiates translation at an alternate start
            codon, compared to variant 1. It encodes isoform 3 which has a
            longer and distinct N-terminus, compared to Calpha1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK131561.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159607 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..427
                     /product="cAMP-dependent protein kinase catalytic subunit
                     alpha isoform 3"
                     /EC_number="2.7.11.11"
                     /note="protein kinase A catalytic subunit; PKA C-alpha;
                     protein kinase, cAMP-dependent, catalytic, alpha; protein
                     kinase, cAMP-dependent, alpha catalytic subunit"
                     /calculated_mol_wt=49003
     Region          118..407
                     /region_name="STKc_PKA"
                     /note="Catalytic subunit of the Serine/Threonine Kinase,
                     cAMP-dependent protein kinase; cd14209"
                     /db_xref="CDD:271111"
     Site            order(126..132,134,147,149,181,197..200,204,243,245,
                     247..248,250,260..261,404)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271111"
     Site            order(127..132,134,147,149,159,181,197..198,200,204,206,
                     210,243,245..248,250,260..261,264,275,277..280,307,
                     311..313,316..318,320,323,404,407)
                     /site_type="active"
                     /db_xref="CDD:271111"
     Site            order(128,130..131,159..161,204,206,210,243,245..247,264,
                     275..280,307,311..313,316..318,320,323..324,407)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271111"
     Site            order(130,160..161,163..164,204,206,210,245..247,264,271,
                     273..278,281,288..290,307,320..321,324..325,328,407)
                     /site_type="other"
                     /note="regulatory subunit interface [polypeptide binding]"
                     /db_xref="CDD:271111"
     Site            260..280
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271111"
     CDS             1..427
                     /gene="PRKACA"
                     /gene_synonym="CAFD1; PKACA; PPNAD4"
                     /coded_by="NM_001304349.2:407..1690"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92541.1"
                     /db_xref="GeneID:5566"
                     /db_xref="HGNC:HGNC:9380"
                     /db_xref="MIM:601639"
ORIGIN      
        1 mftlgyhgae ewasgetsle paleqcpcdc hgeeqgqlga kvtaeppkgt cypsprglhp
       61 rpglpregar gtaksqgyky lgwrrpwpwn vvkeflakak edflkkwesp aqntahldqf
      121 eriktlgtgs fgrvmlvkhk etgnhyamki ldkqkvvklk qiehtlnekr ilqavnfpfl
      181 vklefsfkdn snlymvmeyv pggemfshlr rigrfsepha rfyaaqivlt feylhsldli
      241 yrdlkpenll idqqgyiqvt dfgfakrvkg rtwtlcgtpe ylapeiilsk gynkavdwwa
      301 lgvliyemaa gyppffadqp iqiyekivsg kvrfpshfss dlkdllrnll qvdltkrfgn
      361 lkngvndikn hkwfattdwi aiyqrkveap fipkfkgpgd tsnfddyeee eirvsinekc
      421 gkefsef
//
LOCUS       NP_005424                543 aa            linear   PRI 21-NOV-2025
DEFINITION  tyrosine-protein kinase Yes [Homo sapiens].
ACCESSION   NP_005424
VERSION     NP_005424.1
DBSOURCE    REFSEQ: accession NM_005433.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Barros,P., Matos,A.M., Matos,P. and Jordan,P.
  TITLE     YES1 Kinase Mediates the Membrane Removal of Rescued F508del-CFTR
            in Airway Cells by Promoting MAPK Pathway Activation via SHC1
  JOURNAL   Biomolecules 13 (6), 949 (2023)
   PUBMED   37371529
  REMARK    GeneRIF: YES1 Kinase Mediates the Membrane Removal of Rescued
            F508del-CFTR in Airway Cells by Promoting MAPK Pathway Activation
            via SHC1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Jin,M., Wang,Y., Zhou,D., Liu,W., Han,R. and Chi,Y.
  TITLE     Downregulation of circ-YES1 suppresses NSCLC migration and
            proliferation through the miR-142-3p-HMGB1 axis
  JOURNAL   Respir Res 24 (1), 100 (2023)
   PUBMED   37009887
  REMARK    GeneRIF: Downregulation of circ-YES1 suppresses NSCLC migration and
            proliferation through the miR-142-3p-HMGB1 axis.
            Erratum:[Respir Res. 2023 Jul 10;24(1):181. doi:
            10.1186/s12931-023-02468-5. PMID: 37424028]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Redin,E., Garrido-Martin,E.M., Valencia,K., Redrado,M.,
            Solorzano,J.L., Carias,R., Echepare,M., Exposito,F., Serrano,D.,
            Ferrer,I., Nunez-Buiza,A., Garmendia,I., Garcia-Pedrero,J.M.,
            Gurpide,A., Paz-Ares,L., Politi,K., Montuenga,L.M. and Calvo,A.
  TITLE     YES1 Is a Druggable Oncogenic Target in SCLC
  JOURNAL   J Thorac Oncol 17 (12), 1387-1403 (2022)
   PUBMED   35988891
  REMARK    GeneRIF: YES1 Is a Druggable Oncogenic Target in SCLC.
REFERENCE   5  (residues 1 to 543)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 543)
  AUTHORS   Alai,M., Mui,A.L., Cutler,R.L., Bustelo,X.R., Barbacid,M. and
            Krystal,G.
  TITLE     Steel factor stimulates the tyrosine phosphorylation of the
            proto-oncogene product, p95vav, in human hemopoietic cells
  JOURNAL   J Biol Chem 267 (25), 18021-18025 (1992)
   PUBMED   1381360
REFERENCE   7  (residues 1 to 543)
  AUTHORS   Cichowski,K., McCormick,F. and Brugge,J.S.
  TITLE     p21rasGAP association with Fyn, Lyn, and Yes in thrombin-activated
            platelets
  JOURNAL   J Biol Chem 267 (8), 5025-5028 (1992)
   PUBMED   1544885
REFERENCE   8  (residues 1 to 543)
  AUTHORS   Brickell,P.M.
  TITLE     The p60c-src family of protein-tyrosine kinases: structure,
            regulation, and function
  JOURNAL   Crit Rev Oncog 3 (4), 401-446 (1992)
   PUBMED   1384720
  REMARK    Review article
REFERENCE   9  (residues 1 to 543)
  AUTHORS   Holtrich,U., Brauninger,A., Strebhardt,K. and Rubsamen-Waigmann,H.
  TITLE     Two additional protein-tyrosine kinases expressed in human lung:
            fourth member of the fibroblast growth factor receptor family and
            an intracellular protein-tyrosine kinase
  JOURNAL   Proc Natl Acad Sci U S A 88 (23), 10411-10415 (1991)
   PUBMED   1720539
REFERENCE   10 (residues 1 to 543)
  AUTHORS   Huang,M.M., Bolen,J.B., Barnwell,J.W., Shattil,S.J. and Brugge,J.S.
  TITLE     Membrane glycoprotein IV (CD36) is physically associated with the
            Fyn, Lyn, and Yes protein-tyrosine kinases in human platelets
  JOURNAL   Proc Natl Acad Sci U S A 88 (17), 7844-7848 (1991)
   PUBMED   1715582
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000894.6, AP001020.4 and
            AP001178.4.
            
            Summary: This gene is the cellular homolog of the Yamaguchi sarcoma
            virus oncogene. The encoded protein has tyrosine kinase activity
            and belongs to the src family of proteins. This gene lies in close
            proximity to thymidylate synthase gene on chromosome 18, and a
            corresponding pseudogene has been found on chromosome 22. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.64204.1, BC048960.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000314574.5/ ENSP00000324740.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.32"
     Protein         1..543
                     /product="tyrosine-protein kinase Yes"
                     /EC_number="2.7.10.2"
                     /note="Yamaguchi sarcoma oncogene; cellular yes-1 protein;
                     proto-oncogene tyrosine-protein kinase YES; proto-oncogene
                     c-Yes; v-yes-1 Yamaguchi sarcoma viral oncogene homolog 1;
                     YES1 proto-oncogene, Src family tyrosine kinase"
                     /calculated_mol_wt=60670
     Region          1..45
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07947.3)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P07947.3)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q04736; propagated from
                     UniProtKB/Swiss-Prot (P07947.3)"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P07947.3)"
     Region          94..151
                     /region_name="SH3_Yes"
                     /note="Src homology 3 domain of Yes Protein Tyrosine
                     Kinase; cd12007"
                     /db_xref="CDD:212940"
     Site            order(100,102,105..106,109,126..128,141,143,145..146)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212940"
     Region          154..253
                     /region_name="SH2_Src_family"
                     /note="Src homology 2 (SH2) domain found in the Src family
                     of non-receptor tyrosine kinases; cd09933"
                     /db_xref="CDD:199827"
     Site            order(165,185,187..190,195,211,213,246)
                     /site_type="other"
                     /note="autoinhibitory site [polypeptide binding]"
                     /db_xref="CDD:199827"
     Site            order(165,185,187..189,195,211..213)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:199827"
     Site            order(224,240,245..247)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:199827"
     Region          264..542
                     /region_name="PTKc_Yes"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Yes; cd05069"
                     /db_xref="CDD:270654"
     Site            order(283,285..287,291,303,305,348..351,355,396,400..401,
                     403,414,431..435,444,478)
                     /site_type="active"
                     /db_xref="CDD:270654"
     Site            order(283,286,291,303,305,348..351,355,396,398,401,403,
                     414)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270654"
     Site            order(297,299,331,334,336,349,375,379,407,527)
                     /site_type="other"
                     /note="SH3/SH2 domain interface [polypeptide binding]"
                     /db_xref="CDD:270654"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P07947.3)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P07947.3)"
     Site            order(385,388..389,452,514..516,518,520..521,524,528,
                     531..532,536)
                     /site_type="other"
                     /note="CSK binding interface [polypeptide binding]"
                     /db_xref="CDD:270654"
     Site            order(396,400,431..435,444,478)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270654"
     Site            413..437
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270654"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:9794236; propagated from
                     UniProtKB/Swiss-Prot (P07947.3)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine. /evidence=ECO:0000305; propagated
                     from UniProtKB/Swiss-Prot (P07947.3)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by CSK.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P07947.3)"
     CDS             1..543
                     /gene="YES1"
                     /gene_synonym="c-yes; HsT441; P61-YES; Yes"
                     /coded_by="NM_005433.4:138..1769"
                     /db_xref="CCDS:CCDS11824.1"
                     /db_xref="GeneID:7525"
                     /db_xref="HGNC:HGNC:12841"
                     /db_xref="MIM:164880"
ORIGIN      
        1 mgcikskenk spaikyrpen tpepvstsvs hygaepttvs pcpsssakgt avnfsslsmt
       61 pfggssgvtp fggasssfsv vpssypaglt ggvtifvaly dyearttedl sfkkgerfqi
      121 inntegdwwe arsiatgkng yipsnyvapa dsiqaeewyf gkmgrkdaer lllnpgnqrg
      181 iflvresett kgayslsird wdeirgdnvk hykirkldng gyyittraqf dtlqklvkhy
      241 tehadglchk lttvcptvkp qtqglakdaw eipreslrle vklgqgcfge vwmgtwngtt
      301 kvaiktlkpg tmmpeaflqe aqimkklrhd klvplyavvs eepiyivtef mskgslldfl
      361 kegdgkylkl pqlvdmaaqi adgmayierm nyihrdlraa nilvgenlvc kiadfglarl
      421 iedneytarq gakfpikwta peaalygrft iksdvwsfgi lqtelvtkgr vpypgmvnre
      481 vleqvergyr mpcpqgcpes lhelmnlcwk kdpderptfe yiqsfledyf tatepqyqpg
      541 enl
//
LOCUS       NP_001135753             423 aa            linear   PRI 21-NOV-2025
DEFINITION  coatomer subunit delta isoform 2 [Homo sapiens].
ACCESSION   NP_001135753
VERSION     NP_001135753.1
DBSOURCE    REFSEQ: accession NM_001142281.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   O'Donoghue,L., Comer,S.P., Hiebner,D.W., Schoen,I., von
            Kriegsheim,A. and Smolenski,A.
  TITLE     RhoGAP6 interacts with COPI to regulate protein transport
  JOURNAL   Biochem J 480 (14), 1109-1127 (2023)
   PUBMED   37409526
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Li,W., Liang,J., Outeda,P., Turner,S., Wakimoto,B.T. and Watnick,T.
  TITLE     A genetic screen in Drosophila reveals an unexpected role for the
            KIP1 ubiquitination-promoting complex in male fertility
  JOURNAL   PLoS Genet 16 (12), e1009217 (2020)
   PUBMED   33378371
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Tidwell,T., Deshotel,M., Palumbos,J., Miller,C., Bayrak-Toydemir,P.
            and Carey,J.C.
  TITLE     Novel de novo ARCN1 intronic variant causes rhizomelic short
            stature with microretrognathia and developmental delay
  JOURNAL   Cold Spring Harb Mol Case Stud 6 (6), a005728 (2020)
   PUBMED   33154040
  REMARK    GeneRIF: Novel de novo ARCN1 intronic variant causes rhizomelic
            short stature with microretrognathia and developmental delay.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Schekman,R. and Orci,L.
  TITLE     Coat proteins and vesicle budding
  JOURNAL   Science 271 (5255), 1526-1533 (1996)
   PUBMED   8599108
  REMARK    Review article
REFERENCE   7  (residues 1 to 423)
  AUTHORS   Cukierman,E., Huber,I., Rotman,M. and Cassel,D.
  TITLE     The ARF1 GTPase-activating protein: zinc finger motif and Golgi
            complex localization
  JOURNAL   Science 270 (5244), 1999-2002 (1995)
   PUBMED   8533093
REFERENCE   8  (residues 1 to 423)
  AUTHORS   Radice,P., Pensotti,V., Jones,C., Perry,H., Pierotti,M.A. and
            Tunnacliffe,A.
  TITLE     The human archain gene, ARCN1, has highly conserved homologs in
            rice and Drosophila
  JOURNAL   Genomics 26 (1), 101-106 (1995)
   PUBMED   7782067
REFERENCE   9  (residues 1 to 423)
  AUTHORS   Orcl,L., Palmer,D.J., Amherdt,M. and Rothman,J.E.
  TITLE     Coated vesicle assembly in the Golgi requires only coatomer and ARF
            proteins from the cytosol
  JOURNAL   Nature 364 (6439), 732-734 (1993)
   PUBMED   8355790
REFERENCE   10 (residues 1 to 423)
  AUTHORS   Waters,M.G., Serafini,T. and Rothman,J.E.
  TITLE     'Coatomer': a cytosolic protein complex containing subunits of
            non-clathrin-coated Golgi transport vesicles
  JOURNAL   Nature 349 (6306), 248-251 (1991)
   PUBMED   1898986
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK304019.1, BC093636.1,
            CR988766.1, AU125652.1, BC080638.1 and AA856562.1.
            
            Summary: This gene maps in a region, which include the mixed
            lineage leukemia and Friend leukemia virus integration 1 genes,
            where multiple disease-associated chromosome translocations occur.
            It is an intracellular protein. Archain sequences are well
            conserved among eukaryotes and this protein may play a fundamental
            role in eukaryotic cell biology. It has similarities to heat shock
            proteins and clathrin-associated proteins, and may be involved in
            vesicle structure or trafficking. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            5' coding region, compared to variant 1, and encodes a protein
            (isoform 2) with a shorter N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853561.5909.1,
                                           SRR14038196.2314541.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..423
                     /product="coatomer subunit delta isoform 2"
                     /note="coatomer protein delta-COP; coatomer protein
                     complex, subunit delta; archain vesicle transport protein
                     1; coatomer delta subunit; delta-coat protein; COPI coat
                     complex subunit delta"
                     /calculated_mol_wt=47074
     Region          <2..45
                     /region_name="longin-like"
                     /note="Longin-like domains; cl38905"
                     /db_xref="CDD:365781"
     Region          184..420
                     /region_name="AP_delta-COPI_MHD"
                     /note="Mu homology domain (MHD) of adaptor protein (AP)
                     coat protein I (COPI) delta subunit; cd09254"
                     /db_xref="CDD:271162"
     CDS             1..423
                     /gene="ARCN1"
                     /gene_synonym="COPD; SRMMD; SSMG"
                     /coded_by="NM_001142281.2:140..1411"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44749.1"
                     /db_xref="GeneID:372"
                     /db_xref="HGNC:HGNC:649"
                     /db_xref="MIM:600820"
ORIGIN      
        1 mipeycrale eneisehcfd lifafdeiva lgyrenvnla qirtftemds heekvfravr
       61 etqereakae mrrkakelqq arrdaerqgk kapgfggfgs savsggstaa mitetiietd
      121 kpkvapapar psgpskalkl gakgkevdnf vdklkseget imsssmgkrt seatkmhapp
      181 inmesvhmki eekitltcgr dgglqnmelh gmimlrisdd kygrirlhve nedkkgvqlq
      241 thpnvdkklf taesliglkn peksfpvnsd vgvlkwrlqt teesfiplti ncwpsesgng
      301 cdvnieyelq ednlelndvv itiplpsgvg apvigeidge yrhdsrrntl ewclpvidak
      361 nksgslefsi agqpndffpv qvsfvskkny cniqvtkvtq vdgnspvrfs tettflvdky
      421 eil
//
LOCUS       NP_001310501             991 aa            linear   PRI 21-NOV-2025
DEFINITION  centriolar coiled-coil protein of 110 kDa isoform 2 [Homo sapiens].
ACCESSION   NP_001310501
VERSION     NP_001310501.1
DBSOURCE    REFSEQ: accession NM_001323572.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Iyer,S.S., Chen,F., Ogunmolu,F.E., Moradi,S., Volkov,V.A., van
            Grinsven,E.J., van Hoorn,C., Wu,J., Andrea,N., Hua,S., Jiang,K.,
            Vakonakis,I., Potocnjak,M., Herzog,F., Gigant,B., Gudimchuk,N.,
            Stecker,K.E., Dogterom,M., Steinmetz,M.O. and Akhmanova,A.
  TITLE     Centriolar cap proteins CP110 and CPAP control slow elongation of
            microtubule plus ends
  JOURNAL   J Cell Biol 224 (3) (2025)
   PUBMED   39847124
REFERENCE   2  (residues 1 to 991)
  AUTHORS   Xie,S., Naslavsky,N. and Caplan,S.
  TITLE     Emerging insights into CP110 removal during early steps of
            ciliogenesis
  JOURNAL   J Cell Sci 137 (4) (2024)
   PUBMED   38415788
  REMARK    GeneRIF: Emerging insights into CP110 removal during early steps of
            ciliogenesis.
            Review article
REFERENCE   3  (residues 1 to 991)
  AUTHORS   Xie,S., Naslavsky,N. and Caplan,S.
  TITLE     EHD1 promotes CP110 ubiquitination by centriolar satellite delivery
            of HERC2 to the mother centriole
  JOURNAL   EMBO Rep 24 (6), e56317 (2023)
   PUBMED   37074924
  REMARK    GeneRIF: EHD1 promotes CP110 ubiquitination by centriolar satellite
            delivery of HERC2 to the mother centriole.
REFERENCE   4  (residues 1 to 991)
  AUTHORS   Wang,Y., Zhang,Y., Guo,X., Zheng,Y., Zhang,X., Feng,S. and Wu,H.Y.
  TITLE     CCP5 and CCP6 retain CP110 and negatively regulate ciliogenesis
  JOURNAL   BMC Biol 21 (1), 124 (2023)
   PUBMED   37226238
  REMARK    GeneRIF: CCP5 and CCP6 retain CP110 and negatively regulate
            ciliogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 991)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   6  (residues 1 to 991)
  AUTHORS   Casenghi,M., Meraldi,P., Weinhart,U., Duncan,P.I., Korner,R. and
            Nigg,E.A.
  TITLE     Polo-like kinase 1 regulates Nlp, a centrosome protein involved in
            microtubule nucleation
  JOURNAL   Dev Cell 5 (1), 113-125 (2003)
   PUBMED   12852856
REFERENCE   7  (residues 1 to 991)
  AUTHORS   Chen,Z., Indjeian,V.B., McManus,M., Wang,L. and Dynlacht,B.D.
  TITLE     CP110, a cell cycle-dependent CDK substrate, regulates centrosome
            duplication in human cells
  JOURNAL   Dev Cell 3 (3), 339-350 (2002)
   PUBMED   12361598
  REMARK    GeneRIF: CP110, a cell cycle-dependent CDK substrate, regulates
            centrosome duplication (CP110)
REFERENCE   8  (residues 1 to 991)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   9  (residues 1 to 991)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   10 (residues 1 to 991)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012621.8.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.206050.1,
                                           SRR1660805.187880.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000694978.1/ ENSP00000511625.1
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.3"
     Protein         1..991
                     /product="centriolar coiled-coil protein of 110 kDa
                     isoform 2"
                     /note="centrosomal protein CP110; centrosomal protein of
                     110 kDa; centriolar coiled-coil protein of 110 kDa;
                     centriolar coiled-coil protein 110kDa"
                     /calculated_mol_wt=111093
     Region          1..223
                     /region_name="CEP97 binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Region          29..106
                     /region_name="CaM_bind"
                     /note="Calcium-dependent calmodulin binding; pfam16025"
                     /db_xref="CDD:464981"
     Region          64..82
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Region          67..82
                     /region_name="Required for interaction with CEP290.
                     /evidence=ECO:0000269|PubMed:18694559"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:26304236; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000305|PubMed:26304236; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Region          350..565
                     /region_name="Interaction with CEP76.
                     /evidence=ECO:0000269|PubMed:19460342"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSH4; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSH4; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Region          611..633
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Region          <638..>704
                     /region_name="Stathmin"
                     /note="Stathmin family; pfam00836"
                     /db_xref="CDD:459956"
     Region          <639..>808
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          781..821
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Region          909..924
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     CDS             1..991
                     /gene="CCP110"
                     /gene_synonym="Cep110; CP110"
                     /coded_by="NM_001323572.2:163..3138"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS10579.1"
                     /db_xref="GeneID:9738"
                     /db_xref="HGNC:HGNC:24342"
                     /db_xref="MIM:609544"
ORIGIN      
        1 meeyekfcek slariqeasl stesflpaqs esislirfhg vailspllni ekrkemqqek
       61 qkaldveark qvnrkkallt rvqeildnvq vrkapnasdf dqwemetvys nsevrnlnvp
      121 atfpnsfpsh tehstaakld kiagilpldn edqcktdgid lardsegfns pkqcdssnis
      181 hveneafpkt ssatpqetli sdgpfsvneq qdlpllaevi pdpyvmslqn lmkkskeyie
      241 reqsrrslrg sinrivnesh ldkehdavev adcvkekgql tgkhcvsvip dkpslnksnv
      301 llqgastqas smsmpvlasf skvdipirtg hptvlesnsd fkviptfvte nnviksltgs
      361 yaklpspeps mspkmhrrrs rtssachili nnpinacels pkgkeqamdl iiqdtdentn
      421 vpeimpklpt dlagvcsskv yvgkntsevk edvvlgksnq vcqssgnhle nkvthglvtv
      481 egqltsderg ahimnstcaa mpklhepyas sqciaspnfg tvsglkpasm lekncslqte
      541 lnksydvknp spllmqnqnt rqqmdtpmvs cgneqfldns fekvkrrldl didglqkenc
      601 pyvitsgite qerqhlpekr ypkgsgfvnk nkmlgtsske seellkskml afeemrkrle
      661 eqhaqqlsll iaeqereqer lqkeieeqek mlkekkamta easeldinna velewrkisd
      721 sslletmlsq adslhtsnsn ssgftnsamq ysfvsaneap fylwgsstsg ltklsvtrpf
      781 graktrwsqv fsleiqakfn kitavakgfl trrlmqtdkl kqlrqtvkdt mefirsfqse
      841 aplkrgivsa qdaslqervl aqlraalygi hdiffvmdaa ermsilhhdr evrkekmlrq
      901 mdkmksprva lsaatqksld rkkymkaaem gmpnkkflvk qnpsetrvlq pnqgqnapvh
      961 rllsrqgsic rknpkkaakc cdnlrrqhsl g
//
LOCUS       NP_001349722             542 aa            linear   PRI 21-NOV-2025
DEFINITION  eukaryotic translation initiation factor 3 subunit B isoform 2
            [Homo sapiens].
ACCESSION   NP_001349722
VERSION     NP_001349722.1
DBSOURCE    REFSEQ: accession NM_001362793.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Huang,R., Nie,W., Mi,L., Yao,C. and Zhu,H.
  TITLE     EIF3B stabilizes PCNA by counteracting SYVN1-mediated
            ubiquitination to serve as a promotor in cholangiocarcinoma
  JOURNAL   Aging (Albany NY) 16 (8), 7311-7330 (2024)
   PUBMED   38687509
  REMARK    GeneRIF: EIF3B stabilizes PCNA by counteracting SYVN1-mediated
            ubiquitination to serve as a promotor in cholangiocarcinoma.
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Fang,P., Han,Y., Qu,Y., Wang,X., Zhang,Y., Zhang,W., Zhang,N.,
            Li,G. and Ma,W.
  TITLE     EIF3B stabilizes PTGS2 expression by counteracting MDM2-mediated
            ubiquitination to promote the development and progression of
            malignant melanoma
  JOURNAL   Cancer Sci 113 (12), 4181-4192 (2022)
   PUBMED   36050601
  REMARK    GeneRIF: EIF3B stabilizes PTGS2 expression by counteracting
            MDM2-mediated ubiquitination to promote the development and
            progression of malignant melanoma.
REFERENCE   5  (residues 1 to 542)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 542)
  AUTHORS   Sizova,D.V., Kolupaeva,V.G., Pestova,T.V., Shatsky,I.N. and
            Hellen,C.U.
  TITLE     Specific interaction of eukaryotic translation initiation factor 3
            with the 5' nontranslated regions of hepatitis C virus and
            classical swine fever virus RNAs
  JOURNAL   J Virol 72 (6), 4775-4782 (1998)
   PUBMED   9573242
REFERENCE   7  (residues 1 to 542)
  AUTHORS   Chaudhuri,J., Chakrabarti,A. and Maitra,U.
  TITLE     Biochemical characterization of mammalian translation initiation
            factor 3 (eIF3). Molecular cloning reveals that p110 subunit is the
            mammalian homologue of Saccharomyces cerevisiae protein Prt1
  JOURNAL   J Biol Chem 272 (49), 30975-30983 (1997)
   PUBMED   9388245
REFERENCE   8  (residues 1 to 542)
  AUTHORS   Methot,N., Rom,E., Olsen,H. and Sonenberg,N.
  TITLE     The human homologue of the yeast Prt1 protein is an integral part
            of the eukaryotic initiation factor 3 complex and interacts with
            p170
  JOURNAL   J Biol Chem 272 (2), 1110-1116 (1997)
   PUBMED   8995410
REFERENCE   9  (residues 1 to 542)
  AUTHORS   Asano,K., Kinzy,T.G., Merrick,W.C. and Hershey,J.W.
  TITLE     Conservation and diversity of eukaryotic translation initiation
            factor eIF3
  JOURNAL   J Biol Chem 272 (2), 1101-1109 (1997)
   PUBMED   8995409
REFERENCE   10 (residues 1 to 542)
  AUTHORS   Kirken,R.A., Rui,H., Evans,G.A. and Farrar,W.L.
  TITLE     Characterization of an interleukin-2 (IL-2)-induced tyrosine
            phosphorylated 116-kDa protein associated with the IL-2 receptor
            beta-subunit
  JOURNAL   J Biol Chem 268 (30), 22765-22770 (1993)
   PUBMED   7693677
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA781713.1, AC004971.3, AC004840.4 and BQ045103.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.269912.1,
                                           SRR1803613.73684.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..542
                     /product="eukaryotic translation initiation factor 3
                     subunit B isoform 2"
                     /note="eukaryotic translation initiation factor 3, subunit
                     9 (eta, 116kD); eukaryotic translation initiation factor
                     3, subunit 9 eta, 116kDa; prt1 homolog; eukaryotic
                     translation initiation factor 3 subunit 9; protein
                     synthesis 1"
                     /calculated_mol_wt=63559
     Region          33..533
                     /region_name="COG5354"
                     /note="Uncharacterized protein, contains Trp-Asp (WD)
                     repeat [General function prediction only]"
                     /db_xref="CDD:227657"
     Region          66..99
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          104..151
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          157..191
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          195..234
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          242..273
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          284..332
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          340..375
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          382..412
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..542
                     /gene="EIF3B"
                     /gene_synonym="EIF3-ETA; EIF3-P110; EIF3-P116; EIF3S9;
                     PRT1"
                     /coded_by="NM_001362793.2:615..2243"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:8662"
                     /db_xref="HGNC:HGNC:3280"
                     /db_xref="MIM:603917"
ORIGIN      
        1 mtisdewdip ekqpfkdlgn lrywleeaec rdqysvifes gdrtsifwnd vkdpvsieer
       61 arwtetyvrw spkgtylatf hqrgialwgg ekfkqiqrfs hqgvqlidfs pcerylvtfs
      121 plmdtqddpq aiiiwdiltg hkkrgfhces sahwpifkws hdgkffarmt ldtlsiyetp
      181 smglldkksl kisgikdfsw spggniiafw vpedkdipar vtlmqlptrq eirvrnlfnv
      241 vdcklhwqkn gdylcvkvdr tpkgtqgvvt nfeifrmrek qvpvdvvemk etiiafawep
      301 ngskfavlhg eaprisvsfy hvknngkiel ikmfdkqqan tifwspqgqf vvlaglrsmn
      361 galafvdtsd ctvmniaehy masdvewdpt gryvvtsvsw wshkvdnayw lwtfqgrllq
      421 knnkdrfcql lwrprpptll sqeqikqikk dlkkyskife qkdrlsqska skelverrrt
      481 mmedfrkyrk maqelymeqk nerlelrggv dtdeldsnvd dweeetieff vteeiiplgn
      541 qe
//
LOCUS       NP_001007234             338 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA excision repair protein ERCC-8 isoform 2 [Homo sapiens].
ACCESSION   NP_001007234
VERSION     NP_001007234.1
DBSOURCE    REFSEQ: accession NM_001007233.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Yang,D., Lai,A., Davies,A., Janssen,A.F., Ellis,M.O. and Larrieu,D.
  TITLE     A novel role for CSA in the regulation of nuclear envelope
            integrity: uncovering a non-canonical function
  JOURNAL   Life Sci Alliance 7 (11), e202402745 (2024)
   PUBMED   39209536
  REMARK    GeneRIF: A novel role for CSA in the regulation of nuclear envelope
            integrity: uncovering a non-canonical function.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   van Sluis,M., Yu,Q., van der Woude,M., Gonzalo-Hansen,C.,
            Dealy,S.C., Janssens,R.C., Somsen,H.B., Ramadhin,A.R.,
            Dekkers,D.H.W., Wienecke,H.L., Demmers,J.J.P.G., Raams,A.,
            Davo-Martinez,C., Llerena Schiffmacher,D.A., van Toorn,M.,
            Hackes,D., Thijssen,K.L., Zhou,D., Lammers,J.G., Pines,A.,
            Vermeulen,W., Pothof,J., Demmers,J.A.A., van den Berg,D.L.C.,
            Lans,H. and Marteijn,J.A.
  TITLE     Transcription-coupled DNA-protein crosslink repair by CSB and
            CRL4CSA-mediated degradation
  JOURNAL   Nat Cell Biol 26 (5), 770-783 (2024)
   PUBMED   38600236
  REMARK    GeneRIF: Transcription-coupled DNA-protein crosslink repair by CSB
            and CRL4[CSA]-mediated degradation.
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Carnie,C.J., Acampora,A.C., Bader,A.S., Erdenebat,C., Zhao,S.,
            Bitensky,E., van den Heuvel,D., Parnas,A., Gupta,V.,
            D'Alessandro,G., Sczaniecka-Clift,M., Weickert,P., Aygenli,F.,
            Gotz,M.J., Cordes,J., Esain-Garcia,I., Melidis,L., Wondergem,A.P.,
            Lam,S., Robles,M.S., Balasubramanian,S., Adar,S.,
            Luijsterburg,M.S., Jackson,S.P. and Stingele,J.
  TITLE     Transcription-coupled repair of DNA-protein cross-links depends on
            CSA and CSB
  JOURNAL   Nat Cell Biol 26 (5), 797-810 (2024)
   PUBMED   38600235
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Kokic,G., Yakoub,G., van den Heuvel,D., Wondergem,A.P., van der
            Meer,P.J., van der Weegen,Y., Chernev,A., Fianu,I., Fokkens,T.J.,
            Lorenz,S., Urlaub,H., Cramer,P. and Luijsterburg,M.S.
  TITLE     Structural basis for RNA polymerase II ubiquitylation and
            inactivation in transcription-coupled repair
  JOURNAL   Nat Struct Mol Biol 31 (3), 536-547 (2024)
   PUBMED   38316879
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Liu,M.W., Hu,C.F., Jin,J.Y., Xiang,R., Fan,L.L., Li,Y.L. and Zhu,L.
  TITLE     A compound heterozygous mutation of ERCC8 is responsible for a
            family with Cockayne syndrome
  JOURNAL   Mol Biol Rep 51 (1), 371 (2024)
   PUBMED   38411728
  REMARK    GeneRIF: A compound heterozygous mutation of ERCC8 is responsible
            for a family with Cockayne syndrome.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Selby,C.P. and Sancar,A.
  TITLE     Human transcription-repair coupling factor CSB/ERCC6 is a
            DNA-stimulated ATPase but is not a helicase and does not disrupt
            the ternary transcription complex of stalled RNA polymerase II
  JOURNAL   J Biol Chem 272 (3), 1885-1890 (1997)
   PUBMED   8999876
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Bregman,D.B., Halaban,R., van Gool,A.J., Henning,K.A.,
            Friedberg,E.C. and Warren,S.L.
  TITLE     UV-induced ubiquitination of RNA polymerase II: a novel
            modification deficient in Cockayne syndrome cells
  JOURNAL   Proc Natl Acad Sci U S A 93 (21), 11586-11590 (1996)
   PUBMED   8876179
REFERENCE   8  (residues 1 to 338)
  AUTHORS   Itoh,T., Shiomi,T., Shiomi,N., Harada,Y., Wakasugi,M.,
            Matsunaga,T., Nikaido,O., Friedberg,E.C. and Yamaizumi,M.
  TITLE     Rodent complementation group 8 (ERCC8) corresponds to Cockayne
            syndrome complementation group A
  JOURNAL   Mutat Res 362 (2), 167-174 (1996)
   PUBMED   8596535
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Henning,K.A., Li,L., Iyer,N., McDaniel,L.D., Reagan,M.S.,
            Legerski,R., Schultz,R.A., Stefanini,M., Lehmann,A.R., Mayne,L.V.
            and Friedberg,E.C.
  TITLE     The Cockayne syndrome group A gene encodes a WD repeat protein that
            interacts with CSB protein and a subunit of RNA polymerase II TFIIH
  JOURNAL   Cell 82 (4), 555-564 (1995)
   PUBMED   7664335
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Laugel,V.
  TITLE     Cockayne Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301516
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA169067.1, AK056931.1 and
            AC104113.3.
            
            Summary: This gene encodes a WD repeat protein, which interacts
            with Cockayne syndrome type B (CSB) protein and with p44 protein, a
            subunit of the RNA polymerase II transcription factor IIH.
            Mutations in this gene have been identified in patients with
            hereditary disease Cockayne syndrome (CS). CS cells are abnormally
            sensitive to ultraviolet radiation and are defective in the repair
            of transcriptionally active genes. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Mar 2014].
            
            Transcript Variant: This variant (2) has an additional exon in the
            5' region and uses a downstream AUG start codon compared to variant
            1. The resulting isoform (2) is shorter at the N-terminus compared
            to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056931.1, SRR18074969.2631445.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.1"
     Protein         1..338
                     /product="DNA excision repair protein ERCC-8 isoform 2"
                     /note="Cockayne syndrome WD-repeat protein CSA; DNA
                     excision repair protein ERCC-8; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 8; cockayne syndrome WD repeat
                     protein CSA; excision repair cross-complementation group
                     8"
                     /calculated_mol_wt=37352
     Region          <2..303
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          44..83
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          87..125
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          131..169
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..338
                     /gene="ERCC8"
                     /gene_synonym="CKN1; CSA; UVSS2"
                     /coded_by="NM_001007233.3:455..1471"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:1161"
                     /db_xref="HGNC:HGNC:3439"
                     /db_xref="MIM:609412"
ORIGIN      
        1 mlsggsdgvi vlydlenssr qsyytckavc sigrdhpdvh rysvetvqwy phdtgmftss
       61 sfdktlkvwd tntlqtadvf nfeetvyshh mspvstkhcl vavgtrgpkv qlcdlksgsc
      121 shilqghrqe ilavswspry dyilatasad srvklwdvrr asgclitldq hngkksqave
      181 santahngkv nglcftsdgl hlltvgtdnr mrlwnssnge ntlvnygkvc nnskkglkft
      241 vscgcssefv fvpygstiav ytvysgeqit mlkghyktvd ccvfqsnfqe lysgsrdcni
      301 lawvpslyep vpdddetttk sqlnpafeda wsssdeeg
//
LOCUS       NP_085076                401 aa            linear   PRI 21-NOV-2025
DEFINITION  beta-1,4-galactosyltransferase 2 isoform a [Homo sapiens].
ACCESSION   NP_085076
VERSION     NP_085076.2
DBSOURCE    REFSEQ: accession NM_030587.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Pallet,N., Belleville-Rolland,T., Savalle,A., Lejeune,M., Mauge,L.,
            Bertil,S., Loriot,M.A. and Gaussem,P.
  TITLE     Beta-1,4-galactosyltransferase 2 c.909C>T gene variant is
            predictive of on-clopidogrel platelet reactivity
  JOURNAL   Pharmacogenomics 19 (12), 937-945 (2018)
   PUBMED   30020015
  REMARK    GeneRIF: In individuals under dual antiplatelet therapy, B4GALT2
            c.909C>T is an independent genetic predictor of on-treatment
            platelet reactivity.
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Dekkers,G., Plomp,R., Koeleman,C.A., Visser,R., von Horsten,H.H.,
            Sandig,V., Rispens,T., Wuhrer,M. and Vidarsson,G.
  TITLE     Multi-level glyco-engineering techniques to generate IgG with
            defined Fc-glycans
  JOURNAL   Sci Rep 6, 36964 (2016)
   PUBMED   27872474
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Venkitachalam,S., Revoredo,L., Varadan,V., Fecteau,R.E., Ravi,L.,
            Lutterbaugh,J., Markowitz,S.D., Willis,J.E., Gerken,T.A. and
            Guda,K.
  TITLE     Biochemical and functional characterization of
            glycosylation-associated mutational landscapes in colon cancer
  JOURNAL   Sci Rep 6, 23642 (2016)
   PUBMED   27004849
  REMARK    GeneRIF: Study provides evidence that mutations in B3GNT2, B4GALT2,
            and ST6GALNAC2 underlie aberrant glycosylation, and contribute to
            the pathogenesis of molecular subsets of colon and other
            gastrointestinal malignancies.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Brockhausen,I., Dowler,T. and Paulsen,H.
  TITLE     Site directed processing: role of amino acid sequences and
            glycosylation of acceptor glycopeptides in the assembly of extended
            mucin type O-glycan core 2
  JOURNAL   Biochim Biophys Acta 1790 (10), 1244-1257 (2009)
   PUBMED   19524017
  REMARK    GeneRIF: Data show that Beta4-Gal-transferase (beta4GalT) extends
            core 2 and forms the backbone structure for biologically important
            epitopes.
REFERENCE   6  (residues 1 to 401)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Guo,S., Sato,T., Shirane,K. and Furukawa,K.
  TITLE     Galactosylation of N-linked oligosaccharides by human
            beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed
            in Sf-9 cells
  JOURNAL   Glycobiology 11 (10), 813-820 (2001)
   PUBMED   11588157
REFERENCE   8  (residues 1 to 401)
  AUTHORS   Amado,M., Almeida,R., Schwientek,T. and Clausen,H.
  TITLE     Identification and characterization of large galactosyltransferase
            gene families: galactosyltransferases for all functions
  JOURNAL   Biochim Biophys Acta 1473 (1), 35-53 (1999)
   PUBMED   10580128
  REMARK    Review article
REFERENCE   9  (residues 1 to 401)
  AUTHORS   Lo,N.W., Shaper,J.H., Pevsner,J. and Shaper,N.L.
  TITLE     The expanding beta 4-galactosyltransferase gene family: messages
            from the databanks
  JOURNAL   Glycobiology 8 (5), 517-526 (1998)
   PUBMED   9597550
REFERENCE   10 (residues 1 to 401)
  AUTHORS   Almeida,R., Amado,M., David,L., Levery,S.B., Holmes,E.H., Merkx,G.,
            van Kessel,A.G., Rygaard,E., Hassan,H., Bennett,E. and Clausen,H.
  TITLE     A family of human beta4-galactosyltransferases. Cloning and
            expression of two novel UDP-galactose:beta-n-acetylglucosamine
            beta1, 4-galactosyltransferases, beta4Gal-T2 and beta4Gal-T3
  JOURNAL   J Biol Chem 272 (51), 31979-31991 (1997)
   PUBMED   9405390
  REMARK    Erratum:[J Biol Chem 1998 Jul 17;273(29):18674]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC386748.1, AK293418.1 and
            BC096821.1.
            
            On Jul 2, 2011 this sequence version replaced NP_085076.1.
            
            Summary: This gene is one of seven beta-1,4-galactosyltransferase
            (beta4GalT) genes. They encode type II membrane-bound glycoproteins
            that appear to have exclusive specificity for the donor substrate
            UDP-galactose; all transfer galactose in a beta1,4 linkage to
            similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a
            distinct function in the biosynthesis of different glycoconjugates
            and saccharide structures. As type II membrane proteins, they have
            an N-terminal hydrophobic signal sequence that directs the protein
            to the Golgi apparatus and which then remains uncleaved to function
            as a transmembrane anchor. By sequence similarity, the beta4GalTs
            form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and
            beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. The enzyme
            encoded by this gene synthesizes N-acetyllactosamine in glycolipids
            and glycoproteins. Its substrate specificity is affected by
            alpha-lactalbumin but it is not expressed in lactating mammary
            tissue. Three transcript variants encoding two different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2011].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.725062.1, AK293418.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..401
                     /product="beta-1,4-galactosyltransferase 2 isoform a"
                     /EC_number="2.4.1.22"
                     /EC_number="2.4.1.90"
                     /EC_number="2.4.1.38"
                     /note="beta-4-GalT2; beta-N-acetylglucosaminyl-glycolipid
                     beta-1,4-galactosyltransferase 2; UDP-Gal:betaGlcNAc beta
                     1,4- galactosyltransferase 2; UDP-Gal:betaGlcNAc beta
                     1,4-galactosyltransferase, polypeptide 2; beta-1,4-GalTase
                     2; UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2;
                     UDP-galactose:beta-N-acetylglucosamine
                     beta-1,4-galactosyltransferase 2; nal synthase; lactose
                     synthase A protein; N-acetyllactosamine synthase;
                     beta-N-acetylglucosaminylglycopeptide
                     beta-1,4-galactosyltransferase"
                     /calculated_mol_wt=44633
     Region          174..390
                     /region_name="b4GalT"
                     /note="Beta-4-Galactosyltransferase is involved in the
                     formation of the poly-N-acetyllactosamine core structures
                     present in glycoproteins and glycosphingolipids; cd00899"
                     /db_xref="CDD:132999"
     Site            order(179,181,183,218,245..247)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:132999"
     Site            order(245,247,340)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:132999"
     CDS             1..401
                     /gene="B4GALT2"
                     /gene_synonym="B4Gal-T2; B4Gal-T3; beta4Gal-T2"
                     /coded_by="NM_030587.3:76..1281"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS55596.1"
                     /db_xref="GeneID:8704"
                     /db_xref="HGNC:HGNC:925"
                     /db_xref="MIM:604013"
ORIGIN      
        1 mavevqeqwp clpaagcpgp lggpvaacgm srllggtler vckavlllcl lhflvavily
       61 fdvyaqhlaf fsrfsargpa halhpaasss ssssncsrpn atasssglpe vpsalpgpta
      121 ptlppcpdsp pglvgrllie ftspmplerv qrenpgvlmg grytppdctp aqtvaviipf
      181 rhrehhlryw lhylhpilrr qrlrygvyvi nqhgedtfnr akllnvgfle alkedaaydc
      241 fifsdvdlvp mddrnlyrcg dqprhfaiam dkfgfrlpya gyfggvsgls kaqflringf
      301 pneywgwgge dddifnrisl tgmkisrpdi rigryrmikh drdkhnepnp qrftkiqntk
      361 ltmkrdgigs vryqvlevsr qplftnitvd igrppswppr g
//
LOCUS       NP_001372957             462 aa            linear   PRI 21-NOV-2025
DEFINITION  seipin isoform 1 [Homo sapiens].
ACCESSION   NP_001372957
VERSION     NP_001372957.1
DBSOURCE    REFSEQ: accession NM_001386028.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Guo,D., Hu,L., Xie,P., Sun,P. and Yu,W.
  TITLE     Seipin is involved in oxygen-glucose deprivation/reoxygenation
            induced neuroinflammation by regulating the TLR3/TRAF3/NF-kappaB
            pathway
  JOURNAL   Int Immunopharmacol 134, 112182 (2024)
   PUBMED   38703568
  REMARK    GeneRIF: Seipin is involved in oxygen-glucose
            deprivation/reoxygenation induced neuroinflammation by regulating
            the TLR3/TRAF3/NF-kappaB pathway.
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Zhu,X., An,X., Chen,M., Guo,D., Xie,P., Wang,B., Huang,Z. and Yu,W.
  TITLE     Seipin overexpression attenuates cerebral ischemia-reperfusion
            injury via preventing apoptosis and autophagy
  JOURNAL   Brain Behav 13 (12), e3195 (2023)
   PUBMED   37897134
  REMARK    GeneRIF: Seipin overexpression attenuates cerebral
            ischemia-reperfusion injury via preventing apoptosis and autophagy.
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Weterman,M.A.J., Bronk,M., Jongejan,A., Hoogendijk,J.E., Krudde,J.,
            Karjosukarso,D., Goebel,H.H., Aronica,E., Jobsis,G.J., van
            Ruissen,F., van Spaendonck-Zwarts,K.Y., de Visser,M. and Baas,F.
  TITLE     Pathogenic variants in three families with distal muscle
            involvement
  JOURNAL   Neuromuscul Disord 33 (1), 58-64 (2023)
   PUBMED   36539320
  REMARK    GeneRIF: Pathogenic variants in three families with distal muscle
            involvement.
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Windpassinger,C., Auer-Grumbach,M., Irobi,J., Patel,H., Petek,E.,
            Horl,G., Malli,R., Reed,J.A., Dierick,I., Verpoorten,N.,
            Warner,T.T., Proukakis,C., Van den Bergh,P., Verellen,C., Van
            Maldergem,L., Merlini,L., De Jonghe,P., Timmerman,V., Crosby,A.H.
            and Wagner,K.
  TITLE     Heterozygous missense mutations in BSCL2 are associated with distal
            hereditary motor neuropathy and Silver syndrome
  JOURNAL   Nat Genet 36 (3), 271-276 (2004)
   PUBMED   14981520
  REMARK    GeneRIF: Heterozygous missense mutations in BSCL2 are associated
            with distal hereditary motor neuropathy and Silver syndrome.
            GeneRIF: seipin is an integral membrane protein of the endoplasmic
            reticulum (ER)
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Simha,V. and Garg,A.
  TITLE     Phenotypic heterogeneity in body fat distribution in patients with
            congenital generalized lipodystrophy caused by mutations in the
            AGPAT2 or seipin genes
  JOURNAL   J Clin Endocrinol Metab 88 (11), 5433-5437 (2003)
   PUBMED   14602785
  REMARK    GeneRIF: Congenital lipodystrophy patients with Seipin mutations
            have a more severe lack of body fat, which affects both
            metabolically active and mechanical adipose tissue, compared with
            patients with mutations in the AGPAT2 gene.
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Magre,J., Delepine,M., Khallouf,E., Gedde-Dahl,T. Jr., Van
            Maldergem,L., Sobel,E., Papp,J., Meier,M., Megarbane,A., Bachy,A.,
            Verloes,A., d'Abronzo,F.H., Seemanova,E., Assan,R., Baudic,N.,
            Bourut,C., Czernichow,P., Huet,F., Grigorescu,F., de Kerdanet,M.,
            Lacombe,D., Labrune,P., Lanza,M., Loret,H., Matsuda,F., Navarro,J.,
            Nivelon-Chevalier,A., Polak,M., Robert,J.J., Tric,P.,
            Tubiana-Rufi,N., Vigouroux,C., Weissenbach,J., Savasta,S.,
            Maassen,J.A., Trygstad,O., Bogalho,P., Freitas,P., Medina,J.L.,
            Bonnicci,F., Joffe,B.I., Loyson,G., Panz,V.R., Raal,F.J.,
            O'Rahilly,S., Stephenson,T., Kahn,C.R., Lathrop,M. and Capeau,J.
  CONSRTM   BSCL Working Group
  TITLE     Identification of the gene altered in Berardinelli-Seip congenital
            lipodystrophy on chromosome 11q13
  JOURNAL   Nat Genet 28 (4), 365-370 (2001)
   PUBMED   11479539
  REMARK    GeneRIF: Alterations in BSCL2 (seipin gene) are responsible for
            BSCL (OMIM :606158).Predicted human seipin protein sequence.
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Patel,H., Hart,P.E., Warner,T.T., Houlston,R.S., Patton,M.A.,
            Jeffery,S. and Crosby,A.H.
  TITLE     The Silver syndrome variant of hereditary spastic paraplegia maps
            to chromosome 11q12-q14, with evidence for genetic heterogeneity
            within this subtype
  JOURNAL   Am J Hum Genet 69 (1), 209-215 (2001)
   PUBMED   11389484
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Ito,D.
  TITLE     BSCL2-Related Neurologic Disorders / Seipinopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301484
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Van Maldergem,L.
  TITLE     Berardinelli-Seip Congenital Lipodystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301391
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001458.6.
            
            Summary: This gene encodes the multi-pass transmembrane protein
            seipin. This protein localizes to the endoplasmic reticulum and may
            be important for lipid droplet morphology. Mutations in this gene
            have been associated with congenital generalized lipodystrophy type
            2 or Berardinelli-Seip syndrome, a rare autosomal recessive disease
            characterized by a near absence of adipose tissue and severe
            insulin resistance. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            Naturally occurring read-through transcription occurs between this
            locus and the neighboring locus HNRNPUL2 (heterogeneous nuclear
            ribonucleoprotein U-like 2).[provided by RefSeq, Jul 2024].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK315423.1, SRR14038193.1470674.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..462
                     /product="seipin isoform 1"
                     /note="Bernardinelli-Seip congenital lipodystrophy type 2
                     protein; Berardinelli-Seip congenital lipodystrophy 2
                     (seipin); BSCL2, seipin lipid droplet biogenesis
                     associated"
                     /calculated_mol_wt=51028
     Region          122..286
                     /region_name="Seipin"
                     /note="Seipin and similar proteins; cd23993"
                     /db_xref="CDD:467827"
     Region          <357..>412
                     /region_name="PHA03169"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:223003"
     CDS             1..462
                     /gene="BSCL2"
                     /gene_synonym="GNG3LG; HMN5; HMN5C; HMND13; PELD; SPG17"
                     /coded_by="NM_001386028.1:521..1909"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS44627.1"
                     /db_xref="GeneID:26580"
                     /db_xref="HGNC:HGNC:15832"
                     /db_xref="MIM:606158"
ORIGIN      
        1 mstekvdqke eagekevcgd qikgpdkeee ppaaashgqg wrpggraarn arpepgarhp
       61 alpamvndpp vpallwaqev gqvlagrarr lllqfgvlfc tillllwvsv flygsfyysy
      121 mptvshlspv hfyyrtdcds sttslcsfpv anvsltkggr drvlmygqpy rvtlelelpe
      181 spvnqdlgmf lvtiscytrg griistssrs vmlhyrsdll qmldtlvfss lllfgfaeqk
      241 qllevelyad yrensyvptt gaiieihskr iqlygaylri hahftglryl lynfpmtcaf
      301 igvasnftfl svivlfsymq wvwggiwprh rfslqvnirk rdnsrkevqr risahqpgpe
      361 gqeestpqsd vtedgesped psgtegqlse eekpdqqpls geeelepeas dgsgswedaa
      421 llteanlpap apasasapvl etlgssepag galrqrptcs ss
//
LOCUS       NP_973730                323 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA excision repair protein ERCC-1 isoform 1 [Homo sapiens].
ACCESSION   NP_973730
VERSION     NP_973730.1
DBSOURCE    REFSEQ: accession NM_202001.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Khalouei,A., Masoumi-Ardakani,Y., Jafarzaheh,A., Kalantari
            Khandani,B., Sedghy,F., Khosravi Mashizi,A., Yaghoobi,M.M.,
            Zangouey,M. and Shahouzehi,B.
  TITLE     Association of ERCC1 Gene Polymorphisms (rs3212986 and rs11615)
            With the Risk of Lung Cancer in a Population From Southeast Iran
  JOURNAL   J Res Health Sci 24 (4), e00631 (2024)
   PUBMED   39431656
  REMARK    GeneRIF: Association of ERCC1 Gene Polymorphisms (rs3212986 and
            rs11615) With the Risk of Lung Cancer in a Population From
            Southeast Iran.
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Imani,M.M., Akbari,S., Shalchi,M., Sadeghi,E. and Sadeghi,M.
  TITLE     Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis
  JOURNAL   Arch Oral Biol 162, 105955 (2024)
   PUBMED   38479279
  REMARK    GeneRIF: Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis.
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Jamai,D., Gargouri,R., Selmi,B. and Khabir,A.
  TITLE     ERCC1 and MGMT Methylation as a Predictive Marker of Relapse and
            FOLFOX Response in Colorectal Cancer Patients from South Tunisia
  JOURNAL   Genes (Basel) 14 (7), 1467 (2023)
   PUBMED   37510370
  REMARK    GeneRIF: ERCC1 and MGMT Methylation as a Predictive Marker of
            Relapse and FOLFOX Response in Colorectal Cancer Patients from
            South Tunisia.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Liu,P., Perryman,M.B., Liao,W. and Siciliano,M.J.
  TITLE     Efficiency and limitations of the hn-cDNA library approach for the
            isolation of human transcribed genes from hybrid cells
  JOURNAL   Somat Cell Mol Genet 18 (1), 7-18 (1992)
   PUBMED   1372133
REFERENCE   7  (residues 1 to 323)
  AUTHORS   van Duin,M., van Den Tol,J., Hoeijmakers,J.H., Bootsma,D.,
            Rupp,I.P., Reynolds,P., Prakash,L. and Prakash,S.
  TITLE     Conserved pattern of antisense overlapping transcription in the
            homologous human ERCC-1 and yeast RAD10 DNA repair gene regions
  JOURNAL   Mol Cell Biol 9 (4), 1794-1798 (1989)
   PUBMED   2471070
REFERENCE   8  (residues 1 to 323)
  AUTHORS   Hoeijmakers,J.H.
  TITLE     Characterization of genes and proteins involved in excision repair
            of human cells
  JOURNAL   J Cell Sci Suppl 6, 111-125 (1987)
   PUBMED   2821019
REFERENCE   9  (residues 1 to 323)
  AUTHORS   van Duin,M., de Wit,J., Odijk,H., Westerveld,A., Yasui,A.,
            Koken,M.H., Hoeijmakers,J.H. and Bootsma,D.
  TITLE     Molecular characterization of the human excision repair gene
            ERCC-1: cDNA cloning and amino acid homology with the yeast DNA
            repair gene RAD10
  JOURNAL   Cell 44 (6), 913-923 (1986)
   PUBMED   2420469
REFERENCE   10 (residues 1 to 323)
  AUTHORS   Westerveld,A., Hoeijmakers,J.H., van Duin,M., de Wit,J., Odijk,H.,
            Pastink,A., Wood,R.D. and Bootsma,D.
  TITLE     Molecular cloning of a human DNA repair gene
  JOURNAL   Nature 310 (5976), 425-429 (1984)
   PUBMED   6462228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB468563.1, BC052813.1,
            AK314884.1, BU627436.1 and AC139353.3.
            
            Summary: The product of this gene functions in the nucleotide
            excision repair pathway, and is required for the repair of DNA
            lesions such as those induced by UV light or formed by
            electrophilic compounds including cisplatin. The encoded protein
            forms a heterodimer with the XPF endonuclease (also known as
            ERCC4), and the heterodimeric endonuclease catalyzes the 5'
            incision in the process of excising the DNA lesion. The
            heterodimeric endonuclease is also involved in recombinational DNA
            repair and in the repair of inter-strand crosslinks. Mutations in
            this gene result in cerebrooculofacioskeletal syndrome, and
            polymorphisms that alter expression of this gene may play a role in
            carcinogenesis. Multiple transcript variants encoding different
            isoforms have been found for this gene. The last exon of this gene
            overlaps with the CD3e molecule, epsilon associated protein gene on
            the opposite strand. [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) represents use of an alternate
            promoter and 5' UTR and uses a distinct splice pattern in the 3'
            coding region and 3' UTR, compared to variant 2. The resulting
            isoform (1) has a longer and distinct C-terminus, compared to
            isoform 2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC052813.1, BM556010.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..323
                     /product="DNA excision repair protein ERCC-1 isoform 1"
                     /note="DNA excision repair protein ERCC-1; excision repair
                     cross-complementation group 1; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 1 (includes overlapping antisense
                     sequence)"
                     /calculated_mol_wt=35432
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07992.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P07992.1)"
     Region          17..23
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P07992.1)"
     Region          99..226
                     /region_name="ERCC1_C-like"
                     /note="Central domain of ERCC1; cd22325"
                     /db_xref="CDD:411729"
     Site            order(117..119,166,179,183,186,189..190,193..198,200,204,
                     207..208,210..212,214..216,218..219,221..222)
                     /site_type="other"
                     /note="XPF interaction interface [polypeptide binding]"
                     /db_xref="CDD:411729"
     Region          <250..>281
                     /region_name="PRK00024"
                     /note="DNA repair protein RadC"
                     /db_xref="CDD:178801"
     CDS             1..323
                     /gene="ERCC1"
                     /gene_synonym="COFS4; RAD10; UV20"
                     /coded_by="NM_202001.3:155..1126"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12663.1"
                     /db_xref="GeneID:2067"
                     /db_xref="HGNC:HGNC:3433"
                     /db_xref="MIM:126380"
ORIGIN      
        1 mdpgkdkegv pqpsgppark kfvipldede vppgvakplf rstqslptvd tsaqaapqty
       61 aeyaisqple gagatcptgs eplagetpnq alkpgaksns iivsprqrgn pvlkfvrnvp
      121 wefgdvipdy vlgqstcalf lslryhnlhp dyihgrlqsl gknfalrvll vqvdvkdpqq
      181 alkelakmci ladctlilaw speeagryle tykayeqkpa dllmekleqd fvsrvteclt
      241 tvksvnktds qtllttfgsl eqliaasred lalcpglgpq kvralgknpr swgkerapnk
      301 hnlrpqsfkv kkepktrhsg frl
//
LOCUS       NP_001308145             153 aa            linear   PRI 21-NOV-2025
DEFINITION  B9 domain-containing protein 1 isoform f [Homo sapiens].
ACCESSION   NP_001308145 XP_005256666
VERSION     NP_001308145.1
DBSOURCE    REFSEQ: accession NM_001321216.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Okazaki,M., Kobayashi,T., Chiba,S., Takei,R., Liang,L., Nakayama,K.
            and Katoh,Y.
  TITLE     Formation of the B9-domain protein complex MKS1-B9D2-B9D1 is
            essential as a diffusion barrier for ciliary membrane proteins
  JOURNAL   Mol Biol Cell 31 (20), 2259-2268 (2020)
   PUBMED   32726168
  REMARK    GeneRIF: Formation of the B9-domain protein complex MKS1-B9D2-B9D1
            is essential as a diffusion barrier for ciliary membrane proteins.
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Hopp,K., Heyer,C.M., Hommerding,C.J., Henke,S.A., Sundsbak,J.L.,
            Patel,S., Patel,P., Consugar,M.B., Czarnecki,P.G., Gliem,T.J.,
            Torres,V.E., Rossetti,S. and Harris,P.C.
  TITLE     B9D1 is revealed as a novel Meckel syndrome (MKS) gene by targeted
            exon-enriched next-generation sequencing and deletion analysis
  JOURNAL   Hum Mol Genet 20 (13), 2524-2534 (2011)
   PUBMED   21493627
  REMARK    GeneRIF: B9D1 is a novel Meckel syndrome gene
REFERENCE   6  (residues 1 to 153)
  AUTHORS   Bialas,N.J., Inglis,P.N., Li,C., Robinson,J.F., Parker,J.D.,
            Healey,M.P., Davis,E.E., Inglis,C.D., Toivonen,T., Cottell,D.C.,
            Blacque,O.E., Quarmby,L.M., Katsanis,N. and Leroux,M.R.
  TITLE     Functional interactions between the ciliopathy-associated Meckel
            syndrome 1 (MKS1) protein and two novel MKS1-related (MKSR)
            proteins
  JOURNAL   J Cell Sci 122 (Pt 5), 611-624 (2009)
   PUBMED   19208769
  REMARK    GeneRIF: MKS-1 and MKS-1-related proteins 1 and 2 (MKSR-1/EPPB9,
            MKSR-2/B9D2), localize to transition zones/basal bodies of sensory
            cilia; subcellular localization is largely co-dependent, pointing
            to a functional relationship between the proteins
REFERENCE   7  (residues 1 to 153)
  AUTHORS   Williams,C.L., Winkelbauer,M.E., Schafer,J.C., Michaud,E.J. and
            Yoder,B.K.
  TITLE     Functional redundancy of the B9 proteins and nephrocystins in
            Caenorhabditis elegans ciliogenesis
  JOURNAL   Mol Biol Cell 19 (5), 2154-2168 (2008)
   PUBMED   18337471
  REMARK    GeneRIF: Ciliary transition zone localization.  Functions in a
            module with related proteins (MKS1 and B9D1) that cooperates with
            nephrocystins in ciliogenesis.
REFERENCE   8  (residues 1 to 153)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   9  (residues 1 to 153)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 153)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY047032.1 and BC002944.2.
            
            On Mar 18, 2016 this sequence version replaced XP_005256666.1.
            
            Summary: This gene encodes a B9 domain-containing protein, one of
            several that are involved in ciliogenesis. Alterations in
            expression of this gene have been found in a family with Meckel
            syndrome. Meckel syndrome has been associated with at least six
            different genes. This gene is located within the Smith-Magenis
            syndrome region on chromosome 17. [provided by RefSeq, Mar 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC002944.2, SRR5189661.46287.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119, SAMEA2161674
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..153
                     /product="B9 domain-containing protein 1 isoform f"
                     /note="endothelial precursor protein B9; B9
                     domain-containing protein 1; MKS1-related protein 1; B9
                     protein domain 1"
                     /calculated_mol_wt=16788
     Region          11..>135
                     /region_name="B9-C2"
                     /note="Ciliary basal body-associated, B9 protein;
                     pfam07162"
                     /db_xref="CDD:462108"
     CDS             1..153
                     /gene="B9D1"
                     /gene_synonym="B9; EPPB9; JBTS27; MKS9; MKSR-1; MKSR1"
                     /coded_by="NM_001321216.2:155..616"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS82089.1"
                     /db_xref="GeneID:27077"
                     /db_xref="HGNC:HGNC:24123"
                     /db_xref="MIM:614144"
ORIGIN      
        1 mataspsvfl lmvngqvesa qfpeyddlyc kycfvygqdw aptagleegi sqitsksqdv
       61 rqalvwnfpi dvtfkstnpy gwpqivlsvy gpdvfgndvv rgygavhvpf spgrhkrtip
      121 mfvpestskl qkftslclva ssdlqaappt edk
//
LOCUS       NP_001381784             551 aa            linear   PRI 21-NOV-2025
DEFINITION  kinesin light chain 1 isoform 27 [Homo sapiens].
ACCESSION   NP_001381784
VERSION     NP_001381784.1
DBSOURCE    REFSEQ: accession NM_001394855.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Kikuchi,M., Viet,J., Nagata,K., Sato,M., David,G., Audic,Y.,
            Silverman,M.A., Yamamoto,M., Akatsu,H., Hashizume,Y., Takeda,S.,
            Akamine,S., Miyamoto,T., Uozumi,R., Gotoh,S., Mori,K., Ikeda,M.,
            Paillard,L. and Morihara,T.
  TITLE     Gene-gene functional relationships in Alzheimer's disease: CELF1
            regulates KLC1 alternative splicing
  JOURNAL   Biochem Biophys Res Commun 721, 150025 (2024)
   PUBMED   38768546
  REMARK    GeneRIF: Gene-gene functional relationships in Alzheimer's disease:
            CELF1 regulates KLC1 alternative splicing.
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Gyoeva,F.K., Bybikova,E.M. and Minin,A.A.
  TITLE     An isoform of kinesin light chain specific for the Golgi complex
  JOURNAL   J Cell Sci 113 (Pt 11), 2047-2054 (2000)
   PUBMED   10806115
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Khodjakov,A., Lizunova,E.M., Minin,A.A., Koonce,M.P. and
            Gyoeva,F.K.
  TITLE     A specific light chain of kinesin associates with mitochondria in
            cultured cells
  JOURNAL   Mol Biol Cell 9 (2), 333-343 (1998)
   PUBMED   9450959
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Chernajovsky,Y., Brown,A. and Clark,J.
  TITLE     Human kinesin light (beta) chain gene: DNA sequence and functional
            characterization of its promoter and first exon
  JOURNAL   DNA Cell Biol 15 (11), 965-974 (1996)
   PUBMED   8945637
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Goedert,M., Marsh,S. and Carter,N.
  TITLE     Localization of the human kinesin light chain gene (KNS2) to
            chromosome 14q32.3 by fluorescence in situ hybridization
  JOURNAL   Genomics 32 (1), 173-175 (1996)
   PUBMED   8786116
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Cabeza-Arvelaiz,Y., Shih,L.C., Hardman,N., Asselbergs,F., Bilbe,G.,
            Schmitz,A., White,B., Siciliano,M.J. and Lachman,L.B.
  TITLE     Cloning and genetic characterization of the human kinesin
            light-chain (KLC) gene
  JOURNAL   DNA Cell Biol 12 (10), 881-892 (1993)
   PUBMED   8274221
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139300.6 and AL049840.8.
            
            Summary: Conventional kinesin is a tetrameric molecule composed of
            two heavy chains and two light chains, and transports various
            cargos along microtubules toward their plus ends. The heavy chains
            provide the motor activity, while the light chains bind to various
            cargos. This gene encodes a member of the kinesin light chain
            family. It associates with kinesin heavy chain through an
            N-terminal domain, and six tetratricopeptide repeat (TPR) motifs
            are thought to be involved in binding of cargos such as vesicles,
            mitochondria, and the Golgi complex. Thus, kinesin light chains
            function as adapter molecules and not motors per se. Although
            previously named 'kinesin 2', this gene is not a member of the
            kinesin-2 / kinesin heavy chain subfamily of kinesin motor
            proteins. Extensive alternative splicing produces isoforms with
            different C-termini that are proposed to bind to different cargos;
            however, the full-length nature and/or biological validity of most
            of these variants have not been determined. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK001165.2, BK001166.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..551
                     /product="kinesin light chain 1 isoform 27"
                     /EC_number="2.7.1.21"
                     /note="kinesin 2 60/70kDa; medulloblastoma antigen
                     MU-MB-2.50"
                     /calculated_mol_wt=62695
     Region          35..>149
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          155..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P37285; propagated from
                     UniProtKB/Swiss-Prot (Q07866.2)"
     Region          210..435
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          213..246
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Region          214..241
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          255..288
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Region          255..283
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          297..330
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Region          297..325
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(298,301..302,305..306,308,340,343..344,347..348,
                     350..351,382,385..386,389..390,393)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          338..368
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          339..372
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Region          381..414
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Region          381..408
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O88447; propagated from
                     UniProtKB/Swiss-Prot (Q07866.2)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:21385839; propagated from
                     UniProtKB/Swiss-Prot (Q07866.2)"
     Region          464..497
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:20074060; propagated from
                     UniProtKB/Swiss-Prot (Q07866.2)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:20074060; propagated from
                     UniProtKB/Swiss-Prot (Q07866.2)"
     CDS             1..551
                     /gene="KLC1"
                     /gene_synonym="KLC; KNS2; KNS2A"
                     /coded_by="NM_001394855.1:286..1941"
                     /note="isoform 27 is encoded by transcript variant 27"
                     /db_xref="GeneID:3831"
                     /db_xref="HGNC:HGNC:6387"
                     /db_xref="MIM:600025"
ORIGIN      
        1 mydnmstmvy ikedkleklt qdeiisktkq viqglealkn ehnsilqsll etlkclkkdd
       61 esnlveeksn mirkslemle lglseaqvmm alsnhlnave sekqklraqv rrlcqenqwl
      121 rdelantqqk lqkseqsvaq leeekkhlef mnqlkkyddd ispsedkdtd stkeplddlf
      181 pndeddpgqg iqqqhssaaa aaqqggyeip arlrtlhnlv iqyasqgrye vavplckqal
      241 edlektsghd hpdvatmlni lalvyrdqnk ykdaanllnd alairektlg kdhpavaatl
      301 nnlavlygkr gkykeaeplc kraleirekv lgkdhpdvak qlnnlallcq nqgkyeevey
      361 yyqraleiyq tklgpddpnv aktknnlasc ylkqgkfkqa etlykeiltr aherefgsvd
      421 denkpiwmha eereeckgkq kdgtsfgeyg gwykackvds ptvtttlknl galyrrqgkf
      481 eaaetleeaa mrsrkqgldn vhkqrvaevl ndpenmekrr sreslnvdvv kyesgpdgge
      541 emrkmklglv n
//
LOCUS       NP_001239607             347 aa            linear   PRI 21-NOV-2025
DEFINITION  BBSome complex member BBS4 isoform 2 [Homo sapiens].
ACCESSION   NP_001239607
VERSION     NP_001239607.1
DBSOURCE    REFSEQ: accession NM_001252678.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Zacchia,M., Blanco,F.D.V., Trepiccione,F., Blasio,G., Torella,A.,
            Melluso,A., Capolongo,G., Pollastro,R.M., Piluso,G., Di Iorio,V.,
            Simonelli,F., Viggiano,D., Perna,A., Nigro,V. and Capasso,G.
  TITLE     Nephroplex: a kidney-focused NGS panel highlights the challenges of
            PKD1 sequencing and identifies a founder BBS4 mutation
  JOURNAL   J Nephrol 34 (6), 1855-1874 (2021)
   PUBMED   33964006
  REMARK    GeneRIF: Nephroplex: a kidney-focused NGS panel highlights the
            challenges of PKD1 sequencing and identifies a founder BBS4
            mutation.
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Riise,R., Tornqvist,K., Wright,A.F., Mykytyn,K. and Sheffield,V.C.
  TITLE     The phenotype in Norwegian patients with Bardet-Biedl syndrome with
            mutations in the BBS4 gene
  JOURNAL   Arch Ophthalmol 120 (10), 1364-1367 (2002)
   PUBMED   12365916
  REMARK    GeneRIF: The phenotype of patients with BBS4 mutations consists of
            severe retinitis pigmentosa, variable obesity, brachydactyly with
            variable polydactyly, small or missing teeth, genital hypoplasia,
            and cardiovascular disease.
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Katsanis,N., Eichers,E.R., Ansley,S.J., Lewis,R.A., Kayserili,H.,
            Hoskins,B.E., Scambler,P.J., Beales,P.L. and Lupski,J.R.
  TITLE     BBS4 is a minor contributor to Bardet-Biedl syndrome and may also
            participate in triallelic inheritance
  JOURNAL   Am J Hum Genet 71 (1), 22-29 (2002)
   PUBMED   12016587
  REMARK    GeneRIF: BBS4 is a minor contributor to Bardet-Biedl syndrome and
            may also participate in triallelic inheritance. Evaluated the
            spectrum of mutations in the recently identified BBS4 gene with a
            combination of haplotype analysis and mutation screening.
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Mykytyn,K., Braun,T., Carmi,R., Haider,N.B., Searby,C.C.,
            Shastri,M., Beck,G., Wright,A.F., Iannaccone,A., Elbedour,K.,
            Riise,R., Baldi,A., Raas-Rothschild,A., Gorman,S.W., Duhl,D.M.,
            Jacobson,S.G., Casavant,T., Stone,E.M. and Sheffield,V.C.
  TITLE     Identification of the gene that, when mutated, causes the human
            obesity syndrome BBS4
  JOURNAL   Nat Genet 28 (2), 188-191 (2001)
   PUBMED   11381270
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Bruford,E.A., Riise,R., Teague,P.W., Porter,K., Thomson,K.L.,
            Moore,A.T., Jay,M., Warburg,M., Schinzel,A., Tommerup,N.,
            Tornqvist,K., Rosenberg,T., Patton,M., Mansfield,D.C. and
            Wright,A.F.
  TITLE     Linkage mapping in 29 Bardet-Biedl syndrome families confirms loci
            in chromosomal regions 11q13, 15q22.3-q23, and 16q21
  JOURNAL   Genomics 41 (1), 93-99 (1997)
   PUBMED   9126487
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Carmi,R., Rokhlina,T., Kwitek-Black,A.E., Elbedour,K.,
            Nishimura,D., Stone,E.M. and Sheffield,V.C.
  TITLE     Use of a DNA pooling strategy to identify a human obesity syndrome
            locus on chromosome 15
  JOURNAL   Hum Mol Genet 4 (1), 9-13 (1995)
   PUBMED   7711739
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009712.22.
            
            Summary: This gene is a member of the Bardet-Biedl syndrome (BBS)
            gene family. Bardet-Biedl syndrome is an autosomal recessive
            disorder characterized by severe pigmentary retinopathy, obesity,
            polydactyly, renal malformation and cognitive disability. The
            proteins encoded by BBS gene family members are structurally
            diverse. The similar phenotypes exhibited by mutations in BBS gene
            family members are likely due to the protein's shared roles in
            cilia formation and function. Many BBS proteins localize to the
            basal bodies, ciliary axonemes, and pericentriolar regions of
            cells. BBS proteins may also be involved in intracellular
            trafficking via microtubule-related transport. The protein encoded
            by this gene has sequence similarity to O-linked
            N-acetylglucosamine (O-GlcNAc) transferases in plants and
            archaebacteria and in human forms a multi-protein 'BBSome' complex
            with seven other BBS proteins. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (2) lacks an internal exon and
            initiates translation at a downstream, in-frame start codon,
            compared to variant 1. The encoded isoform (2) has a shorter
            N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647855.1, AK303706.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..347
                     /product="BBSome complex member BBS4 isoform 2"
                     /note="bardet-Biedl syndrome 4 protein; BBSome complex
                     member BBS4"
                     /calculated_mol_wt=38151
     Region          1..258
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          64..92
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          98..126
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(99,102..103,106..107,109,133,136..137,140..141,
                     143..144,167,170..171,174..175,178)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          131..161
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          166..193
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          200..225
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..347
                     /gene="BBS4"
                     /coded_by="NM_001252678.2:491..1534"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58377.1"
                     /db_xref="GeneID:585"
                     /db_xref="HGNC:HGNC:969"
                     /db_xref="MIM:600374"
ORIGIN      
        1 mlgkihlleg dldkaievyk kavefspent ellttlglly lqlgiyqkaf ehlgnaltyd
       61 ptnykailaa gsmmqthgdf dvaltkyrvv acavpesppl wnnigmcffg kkkyvaaisc
      121 lkranylapf dwkilynlgl vhltmqqyas afhflsaain fqpkmgelym llavaltnle
      181 dienakraya eavhldkcnp lvnlnyavll ynqgekknal aqyqemekkv sllkdnssle
      241 fdsemvemaq klgaalqvge alvwtkpvkd pkskhqttst skpasfqqpl gsnqalgqam
      301 ssaaayrtlp sgaggtsqft kppslplepe pavessptet seqirek
//
LOCUS       NP_001338557             148 aa            linear   PRI 21-NOV-2025
DEFINITION  dynein light chain Tctex-type protein 2B isoform 1 [Homo sapiens].
ACCESSION   NP_001338557
VERSION     NP_001338557.1
DBSOURCE    REFSEQ: accession NM_001351628.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 148)
  AUTHORS   Vuolo,L., Stevenson,N.L., Mukhopadhyay,A.G., Roberts,A.J. and
            Stephens,D.J.
  TITLE     Cytoplasmic dynein-2 at a glance
  JOURNAL   J Cell Sci 133 (6) (2020)
   PUBMED   32229580
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 148)
  AUTHORS   Schmidts,M., Hou,Y., Cortes,C.R., Mans,D.A., Huber,C., Boldt,K.,
            Patel,M., van Reeuwijk,J., Plaza,J.M., van Beersum,S.E., Yap,Z.M.,
            Letteboer,S.J., Taylor,S.P., Herridge,W., Johnson,C.A.,
            Scambler,P.J., Ueffing,M., Kayserili,H., Krakow,D., King,S.M.,
            Beales,P.L., Al-Gazali,L., Wicking,C., Cormier-Daire,V.,
            Roepman,R., Mitchison,H.M. and Witman,G.B.
  CONSRTM   UK10K
  TITLE     TCTEX1D2 mutations underlie Jeune asphyxiating thoracic dystrophy
            with impaired retrograde intraflagellar transport
  JOURNAL   Nat Commun 6, 7074 (2015)
   PUBMED   26044572
  REMARK    GeneRIF: integral component of the evolutionarily conserved
            retrograde intraflagellar transport machinery
            Erratum:[Nat Commun. 2016 Mar 29;7:11270. doi: 10.1038/ncomms11270.
            PMID: 27021811]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 148)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   8  (residues 1 to 148)
  AUTHORS   Gholkar,A.A., Senese,S., Lo,Y.C., Capri,J., Deardorff,W.J.,
            Dharmarajan,H., Contreras,E., Hodara,E., Whitelegge,J.P.,
            Jackson,P.K. and Torres,J.Z.
  TITLE     Tctex1d2 associates with short-rib polydactyly syndrome proteins
            and is required for ciliogenesis
  JOURNAL   Cell Cycle 14 (7), 1116-1125 (2015)
   PUBMED   25830415
  REMARK    GeneRIF: Tctex1d2 is a novel dynein light chain important for
            trafficking to the cilium and potentially retrograde intraflagellar
            transport.
REFERENCE   9  (residues 1 to 148)
  AUTHORS   Asante,D., Stevenson,N.L. and Stephens,D.J.
  TITLE     Subunit composition of the human cytoplasmic dynein-2 complex
  JOURNAL   J Cell Sci 127 (Pt 21), 4774-4787 (2014)
   PUBMED   25205765
REFERENCE   10 (residues 1 to 148)
  AUTHORS   Miyamoto-Sato,E., Fujimori,S., Ishizaka,M., Hirai,N., Masuoka,K.,
            Saito,R., Ozawa,Y., Hino,K., Washio,T., Tomita,M., Yamashita,T.,
            Oshikubo,T., Akasaka,H., Sugiyama,J., Matsumoto,Y. and Yanagawa,H.
  TITLE     A comprehensive resource of interacting protein regions for
            refining human transcription factor networks
  JOURNAL   PLoS One 5 (2), e9289 (2010)
   PUBMED   20195357
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC069257.28.
            
            Summary: Dyneins are a group of microtubule-activated ATPases that
            function as molecular motors. They are divided into two subgroups
            of axonemal and cytoplasmic dyneins. The cytoplasmic dyneins
            function in intracellular motility, including retrograde axonal
            transport, protein sorting, organelle movement, and spindle
            dynamics. Molecules of conventional cytoplasmic dynein are
            comprised of 2 heavy chain polypeptides and a number of
            intermediate and light chains. This gene encodes a subunit of the
            human cytoplasmic dynein-2 complex. Mutations in this gene are
            associated with short-rib thoracic dysplasia 17 with or without
            polydactyly. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, May 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HY357702.1, HY160739.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..148
                     /product="dynein light chain Tctex-type protein 2B isoform
                     1"
                     /note="tctex1 domain-containing protein 2; Tctex1 domain
                     containing 2; dynein light chain Tctex-type protein 2B"
                     /calculated_mol_wt=16855
     Region          38..127
                     /region_name="DLC-like_TCTEX1D2"
                     /note="dynein light chain (DLC)-like domain found in
                     Tctex1 domain-containing protein 2 (TCTEX1D2) and similar
                     proteins; cd21459"
                     /db_xref="CDD:412007"
     CDS             1..148
                     /gene="DYNLT2B"
                     /gene_synonym="SRTD17; TCTEX1D2"
                     /coded_by="NM_001351628.2:89..535"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:255758"
                     /db_xref="HGNC:HGNC:28482"
                     /db_xref="MIM:617353"
ORIGIN      
        1 matsigvsfs vgdgvpeaek nagepentyi lrpvfqqrfr psvvkdciha vlkeelanae
       61 yspeempqlt khlsenikdk lkemgfdryk mvvqvvigeq rgegvfmasr cfwdadtdny
      121 thdvfmnfil rcssiwlfll lneslksw
//
LOCUS       NP_001264103             392 aa            linear   PRI 21-NOV-2025
DEFINITION  embryonal Fyn-associated substrate isoform 3 [Homo sapiens].
ACCESSION   NP_001264103
VERSION     NP_001264103.1
DBSOURCE    REFSEQ: accession NM_001277174.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Pavon,M.A., Arroyo-Solera,I., Leon,X., Tellez-Gabriel,M., Viros,D.,
            Gallardo,A., Cespedes,M.V., Casanova,I., Lopez-Pousa,A.,
            Barnadas,A., Quer,M. and Mangues,R.
  TITLE     The combined use of EFS, GPX2, and SPRR1A expression could
            distinguish favorable from poor clinical outcome among
            epithelial-like head and neck carcinoma subtypes
  JOURNAL   Head Neck 41 (6), 1830-1845 (2019)
   PUBMED   30652380
  REMARK    GeneRIF: The combined use of EFS, GPX2, and SPRR1A expression could
            distinguish favorable from poor clinical outcome among
            epithelial-like head and neck carcinoma subtypes.
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Wu,C., Ma,M.H., Brown,K.R., Geisler,M., Li,L., Tzeng,E., Jia,C.Y.,
            Jurisica,I. and Li,S.S.
  TITLE     Systematic identification of SH3 domain-mediated human
            protein-protein interactions by peptide array target screening
  JOURNAL   Proteomics 7 (11), 1775-1785 (2007)
   PUBMED   17474147
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Tchernev,V.T., Mansfield,T.A., Giot,L., Kumar,A.M., Nandabalan,K.,
            Li,Y., Mishra,V.S., Detter,J.C., Rothberg,J.M., Wallace,M.R.,
            Southwick,F.S. and Kingsmore,S.F.
  TITLE     The Chediak-Higashi protein interacts with SNARE complex and signal
            transduction proteins
  JOURNAL   Mol Med 8 (1), 56-64 (2002)
   PUBMED   11984006
REFERENCE   8  (residues 1 to 392)
  AUTHORS   Cote,J.F., Charest,A., Wagner,J. and Tremblay,M.L.
  TITLE     Combination of gene targeting and substrate trapping to identify
            substrates of protein tyrosine phosphatases using PTP-PEST as a
            model
  JOURNAL   Biochemistry 37 (38), 13128-13137 (1998)
   PUBMED   9748319
REFERENCE   9  (residues 1 to 392)
  AUTHORS   Ohba,T., Ishino,M., Aoto,H. and Sasaki,T.
  TITLE     Dot far-western blot analysis of relative binding affinities of the
            Src homology 3 domains of Efs and its related proteins
  JOURNAL   Anal Biochem 262 (2), 185-192 (1998)
   PUBMED   9750131
REFERENCE   10 (residues 1 to 392)
  AUTHORS   Ishino,M., Ohba,T., Inazawa,J., Sasaki,H., Ariyama,Y. and Sasaki,T.
  TITLE     Identification of an Efs isoform that lacks the SH3 domain and
            chromosomal mapping of human Efs
  JOURNAL   Oncogene 15 (14), 1741-1745 (1997)
   PUBMED   9349509
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049829.4.
            
            Summary: The protein encoded by this gene is a member of the CAS
            (CRK-associated substrate) family of adaptor proteins which
            typically serve as scaffolds for the assembly of larger signaling
            complexes. These complexes form at the cell surface where integrin
            binding leads to the subsequent phosphorylation of a CAS protein.
            Additional binding of SRC family kinases leads to CAS
            hyperphosphorylation and the creation of binding sites for CRK and
            other proteins that cause actin cytoskeleton reorganization. This
            gene plays a role in integrin-mediated cell attachment, spreading,
            and migration and also plays a role in both normal and malignant
            cellular transformation. This broadly expressed gene has been shown
            to play a role in neurite outgrowth and its expression in the
            thymus and lymphocytes is important for T cell maturation and the
            development of immunological self-tolerance. Alternative splicing
            of this gene results in multiple transcript variants encoding
            distinct isoforms. [provided by RefSeq, Jul 2020].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon and an alternate in-frame segment compared to variant 1. The
            resulting isoform (3) has the same N- and C-termini but is shorter
            compared to isoform 1. This isoform lacks the N-terminal SH3 domain
            found in isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295933.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465403 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..392
                     /product="embryonal Fyn-associated substrate isoform 3"
                     /note="Cas scaffolding protein family member 3; signal
                     transduction protein (SH3 containing)"
                     /calculated_mol_wt=40826
     Region          202..387
                     /region_name="CAS_C"
                     /note="Crk-Associated Substrate C-terminal domain;
                     pfam12026"
                     /db_xref="CDD:463437"
     CDS             1..392
                     /gene="EFS"
                     /gene_synonym="CAS3; CASS3; EFS1; EFS2; HEFS; SIN"
                     /coded_by="NM_001277174.2:148..1326"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS61404.1"
                     /db_xref="GeneID:10278"
                     /db_xref="HGNC:HGNC:16898"
                     /db_xref="MIM:609906"
ORIGIN      
        1 maiatsvyvv ppparpcpts gppagpcpps pdliykipra sgtqlaaprd alevydvppt
       61 alrvpssgpy dcpasfshpl trvapqppge ddappspepp galashdqdt laqllarspp
      121 pphrprlpsa eslsrrplpa lpvpeapsps pvpspapgrk gsiqdrplpp ppprlpgygg
      181 pkvegdpegr emeddpaghh neyegipmae eydyvhlkgm dkaqgsrppd qactgdpelp
      241 ergmpapqea lspgeplvvs tgdlqllyfy agqcqshysa lqaavaalms stqanqpprl
      301 fvphskrvvv aahrlvfvgd tlgrlaasap lraqvraagt algqalratv lavkgaalgy
      361 psspaiqemv qcvtelagqa lqfttlltsl ap
//
LOCUS       NP_001135755             132 aa            linear   PRI 21-NOV-2025
DEFINITION  small ribosomal subunit protein eS24 isoform e [Homo sapiens].
ACCESSION   NP_001135755
VERSION     NP_001135755.1
DBSOURCE    REFSEQ: accession NM_001142283.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Park,J., Nam,D.H., Kim,D. and Chung,Y.J.
  TITLE     RPS24 alternative splicing is a marker of cancer progression and
            epithelial-mesenchymal transition
  JOURNAL   Sci Rep 14 (1), 13246 (2024)
   PUBMED   38853173
  REMARK    GeneRIF: RPS24 alternative splicing is a marker of cancer
            progression and epithelial-mesenchymal transition.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Kerry,J., Specker,E.J., Mizzoni,M., Brumwell,A., Fell,L.,
            Goodbrand,J., Rosen,M.N. and Uniacke,J.
  TITLE     Autophagy-dependent alternative splicing of ribosomal protein S24
            produces a more stable isoform that aids in hypoxic cell survival
  JOURNAL   FEBS Lett 598 (5), 503-520 (2024)
   PUBMED   38281767
  REMARK    GeneRIF: Autophagy-dependent alternative splicing of ribosomal
            protein S24 produces a more stable isoform that aids in hypoxic
            cell survival.
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Wang,S., Xia,L., Zhang,B., Zhang,H. and Lan,F.
  TITLE     Downregulated long intergenic non-coding RNA 00,174 represses
            malignant biological behaviors of lung cancer cells by regulating
            microRNA-584-3p/ribosomal protein S24 axis
  JOURNAL   Funct Integr Genomics 22 (4), 643-653 (2022)
   PUBMED   35451652
  REMARK    GeneRIF: Downregulated long intergenic non-coding RNA 00,174
            represses malignant biological behaviors of lung cancer cells by
            regulating microRNA-584-3p/ribosomal protein S24 axis.
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   5  (residues 1 to 132)
  AUTHORS   Kennedy,S.A., Jarboui,M.A., Srihari,S., Raso,C., Bryan,K.,
            Dernayka,L., Charitou,T., Bernal-Llinares,M., Herrera-Montavez,C.,
            Krstic,A., Matallanas,D., Kotlyar,M., Jurisica,I., Curak,J.,
            Wong,V., Stagljar,I., LeBihan,T., Imrie,L., Pillai,P., Lynn,M.A.,
            Fasterius,E., Al-Khalili Szigyarto,C., Breen,J., Kiel,C.,
            Serrano,L., Rauch,N., Rukhlenko,O., Kholodenko,B.N.,
            Iglesias-Martinez,L.F., Ryan,C.J., Pilkington,R., Cammareri,P.,
            Sansom,O., Shave,S., Auer,M., Horn,N., Klose,F., Ueffing,M.,
            Boldt,K., Lynn,D.J. and Kolch,W.
  TITLE     Extensive rewiring of the EGFR network in colorectal cancer cells
            expressing transforming levels of KRASG13D
  JOURNAL   Nat Commun 11 (1), 499 (2020)
   PUBMED   31980649
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 132)
  AUTHORS   Xu,W.B. and Roufa,D.J.
  TITLE     The gene encoding human ribosomal protein S24 and tissue-specific
            expression of differentially spliced mRNAs
  JOURNAL   Gene 169 (2), 257-262 (1996)
   PUBMED   8647458
REFERENCE   7  (residues 1 to 132)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   8  (residues 1 to 132)
  AUTHORS   Sieff,C.
  TITLE     DBA Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301769
REFERENCE   9  (residues 1 to 132)
  AUTHORS   Huang,R.T., Li,D.R., Wei,J., Huang,X.R., Yuan,X.T. and Tian,X.
  TITLE     Isolation and identification of hepatitis E virus in Xinjiang,
            China
  JOURNAL   J Gen Virol 73 (Pt 5), 1143-1148 (1992)
   PUBMED   1588318
REFERENCE   10 (residues 1 to 132)
  AUTHORS   Brown,S.J., Jewell,A., Maki,C.G. and Roufa,D.J.
  TITLE     A cDNA encoding human ribosomal protein S24
  JOURNAL   Gene 91 (2), 293-296 (1990)
   PUBMED   2210388
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG944046.1, BX537975.1 and
            AL512628.12.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 40S subunit. The protein belongs
            to the S24E family of ribosomal proteins. It is located in the
            cytoplasm. Multiple transcript variants encoding different isoforms
            have been found for this gene. As is typical for genes encoding
            ribosomal proteins, there are multiple processed pseudogenes of
            this gene dispersed through the genome. Mutations in this gene
            result in Diamond-Blackfan anemia. [provided by RefSeq, Nov 2008].
            
            Transcript Variant: This variant (e) uses an alternate splice
            pattern in the 3' coding region, compared to variant d. The
            resulting protein (isoform e) has a shorter and distinct
            C-terminus, compared to isoform d.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD177602.1, CD176310.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.3"
     Protein         1..132
                     /product="small ribosomal subunit protein eS24 isoform e"
                     /note="40S ribosomal protein S24; small ribosomal subunit
                     protein eS24"
                     /calculated_mol_wt=15194
     Region          1..130
                     /region_name="PTZ00071"
                     /note="40S ribosomal protein S24; Provisional"
                     /db_xref="CDD:240256"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P62847.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P62847.1)"
     CDS             1..132
                     /gene="RPS24"
                     /gene_synonym="DBA3; eS24; S24"
                     /coded_by="NM_001142283.2:40..438"
                     /note="isoform e is encoded by transcript variant e"
                     /db_xref="CCDS:CCDS86122.1"
                     /db_xref="GeneID:6229"
                     /db_xref="HGNC:HGNC:10411"
                     /db_xref="MIM:602412"
ORIGIN      
        1 mndtvtirtr kfmtnrllqr kqmvidvlhp gkatvpktei reklakmykt tpdvifvfgf
       61 rthfgggktt gfgmiydsld yakknepkhr larhglyekk ktsrkqrker knrmkkvrgt
      121 akanvgagkk kk
//
LOCUS       NP_001093861             304 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 1 [Homo sapiens].
ACCESSION   NP_001093861
VERSION     NP_001093861.1
DBSOURCE    REFSEQ: accession NM_001100391.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC031090.1, SRR18074967.2989337.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..304
                     /product="RNA-binding Raly-like protein isoform 1"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=33780
     Region          28..110
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          212..>257
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     CDS             1..304
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001100391.3:329..1243"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS55252.1"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mskrrrlkqg epimtgktqt snvtnkndpk sinsrvfign lntaivkkvd ieaifskygk
       61 ivgcsvhkgy afvqymserh araavagena rviagqpldi nmagepkpyr pkpgnkrpls
      121 alyrleskep flsvggyvfd ydyyrddfyn rlfdyhgrvp pppraviplk rprvavtttr
      181 rgkgvfsmkg gsrstasgst gsklksdelq tikkeltqik tkidsllgrl ekiekqqkae
      241 aeaqkkqlee slvliqeecv seiadhstee paeggpdadg eemtdgieed fdedgghelf
      301 lqik
//
LOCUS       NP_001363674             603 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 5 [Homo sapiens].
ACCESSION   NP_001363674 XP_005265826
VERSION     NP_001363674.1
DBSOURCE    REFSEQ: accession NM_001376745.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Muckenfuss,L.M., Migenda Herranz,A.C., Boneberg,F.M., Clerici,M.
            and Jinek,M.
  TITLE     Fip1 is a multivalent interaction scaffold for processing factors
            in human mRNA 3' end biogenesis
  JOURNAL   Elife 11, e80332 (2022)
   PUBMED   36073787
  REMARK    GeneRIF: Fip1 is a multivalent interaction scaffold for processing
            factors in human mRNA 3' end biogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Tennenbaum,J., Groh,M., Venditti,L., Campos-Gazeau,F., Chalayer,E.,
            De Broucker,T., Hamidou,M., Hunault,M., Lyoubi,A., Meunier,R.,
            Muron,T., Sene,D., Slama,B., Guidoux,C., Lefevre,G., Kahn,J.E.,
            Denier,C. and Rohmer,J.
  TITLE     FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a Treatable
            Cause of Watershed Infarction
  JOURNAL   Stroke 52 (10), e605-e609 (2021)
   PUBMED   34304603
  REMARK    GeneRIF: FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a
            Treatable Cause of Watershed Infarction.
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 603)
  AUTHORS   Helbig,G., Lewandowski,K., Swiderska,A., Rodzaj,M., Seferynska,I.
            and Gajkowska-Kulik,J.
  TITLE     Exquisite response to imatinib mesylate in FIP1L1-PDGFRA-mutated
            hypereosinophilic syndrome: a 12-year experience of the Polish
            Hypereosinophilic Syndrome Study Group
  JOURNAL   Pol Arch Intern Med 130 (3), 255-257 (2020)
   PUBMED   32125294
  REMARK    GeneRIF: Exquisite response to imatinib mesylate in
            FIP1L1-PDGFRA-mutated hypereosinophilic syndrome: a 12-year
            experience of the Polish Hypereosinophilic Syndrome Study Group.
REFERENCE   6  (residues 1 to 603)
  AUTHORS   Cools,J., Quentmeier,H., Huntly,B.J., Marynen,P., Griffin,J.D.,
            Drexler,H.G. and Gilliland,D.G.
  TITLE     The EOL-1 cell line as an in vitro model for the study of
            FIP1L1-PDGFRA-positive chronic eosinophilic leukemia
  JOURNAL   Blood 103 (7), 2802-2805 (2004)
   PUBMED   14630792
  REMARK    GeneRIF: results indicate that the fusion of FIP1L1 to PDGFRA
            occurs rarely in leukemia cell lines
REFERENCE   7  (residues 1 to 603)
  AUTHORS   Kaufmann,I., Martin,G., Friedlein,A., Langen,H. and Keller,W.
  TITLE     Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements
            and stimulates poly(A) polymerase
  JOURNAL   EMBO J 23 (3), 616-626 (2004)
   PUBMED   14749727
REFERENCE   8  (residues 1 to 603)
  AUTHORS   Pardanani,A., Ketterling,R.P., Brockman,S.R., Flynn,H.C.,
            Paternoster,S.F., Shearer,B.M., Reeder,T.L., Li,C.Y., Cross,N.C.,
            Cools,J., Gilliland,D.G., Dewald,G.W. and Tefferi,A.
  TITLE     CHIC2 deletion, a surrogate for FIP1L1-PDGFRA fusion, occurs in
            systemic mastocytosis associated with eosinophilia and predicts
            response to imatinib mesylate therapy
  JOURNAL   Blood 102 (9), 3093-3096 (2003)
   PUBMED   12842979
  REMARK    GeneRIF: observations suggest that the FIP1L1-PDGFRA rearrangement
            occurs in an early hematopoietic progenitor and suggests that the
            molecular pathogenesis for a subset of SMCD patients is similar to
            that of HES
REFERENCE   9  (residues 1 to 603)
  AUTHORS   Griffin,J.H., Leung,J., Bruner,R.J., Caligiuri,M.A. and
            Briesewitz,R.
  TITLE     Discovery of a fusion kinase in EOL-1 cells and idiopathic
            hypereosinophilic syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (13), 7830-7835 (2003)
   PUBMED   12808148
REFERENCE   10 (residues 1 to 603)
  AUTHORS   Cools,J., DeAngelo,D.J., Gotlib,J., Stover,E.H., Legare,R.D.,
            Cortes,J., Kutok,J., Clark,J., Galinsky,I., Griffin,J.D.,
            Cross,N.C., Tefferi,A., Malone,J., Alam,R., Schrier,S.L.,
            Schmid,J., Rose,M., Vandenberghe,P., Verhoef,G., Boogaerts,M.,
            Wlodarska,I., Kantarjian,H., Marynen,P., Coutre,S.E., Stone,R. and
            Gilliland,D.G.
  TITLE     A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes
            as a therapeutic target of imatinib in idiopathic hypereosinophilic
            syndrome
  JOURNAL   N Engl J Med 348 (13), 1201-1214 (2003)
   PUBMED   12660384
  REMARK    GeneRIF: The hypereosinophilic syndrome may result from a novel
            fusion tyrosine kinase - FIP1L1-PDGFRalpha - that is a consequence
            of an interstitial chromosomal deletion.
            GeneRIF: Describes the fusion gene Fip1-like-1-PDGFRalpha in
            patients with idiopathic hypereosinophilic syndrome, mostly
            responsive to imatinib therapy.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098821.3 and AC058822.6.
            
            On Nov 20, 2019 this sequence version replaced XP_005265826.1.
            
            Summary: This gene encodes a subunit of the CPSF (cleavage and
            polyadenylation specificity factor) complex that polyadenylates the
            3' end of mRNA precursors. This gene, the homolog of yeast Fip1
            (factor interacting with PAP), binds to U-rich sequences of
            pre-mRNA and stimulates poly(A) polymerase activity. Its N-terminus
            contains a PAP-binding site and its C-terminus an RNA-binding
            domain. An interstitial chromosomal deletion on 4q12 creates an
            in-frame fusion of human genes FIP1L1 and PDGFRA (platelet-derived
            growth factor receptor, alpha). The FIP1L1-PDGFRA fusion gene
            encodes a constitutively activated tyrosine kinase that joins the
            first 233 amino acids of FIP1L1 to the last 523 amino acids of
            PDGFRA. This gene fusion and chromosomal deletion is the cause of
            some forms of idiopathic hypereosinophilic syndrome (HES). This
            syndrome, recently reclassified as chronic eosinophilic leukemia
            (CEL), is responsive to treatment with tyrosine kinase inhibitors.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.209632.1,
                                           SRR14038195.1210300.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..603
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     5"
                     /note="rearranged in hypereosinophilia; pre-mRNA
                     3'-end-processing factor FIP1; FIP1-like 1 protein; factor
                     interacting with PAP; FIP1 like 1; FIP1L1 cleavage and
                     polyadenylation specific factor subunit"
                     /calculated_mol_wt=67268
     Region          1..356
                     /region_name="Necessary for stimulating PAPOLA activity"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UN15.1)"
     Region          1..111
                     /region_name="Sufficient for interaction with PAPOLA"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UN15.1)"
     Region          1..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UN15.1)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D824; propagated from
                     UniProtKB/Swiss-Prot (Q6UN15.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D824; propagated from
                     UniProtKB/Swiss-Prot (Q6UN15.1)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D824; propagated from
                     UniProtKB/Swiss-Prot (Q6UN15.1)"
     Region          137..243
                     /region_name="Sufficient for interaction with CPSF4.
                     /evidence=ECO:0000269|PubMed:14749727"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UN15.1)"
     Region          154..196
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     Region          238..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UN15.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D824; propagated from
                     UniProtKB/Swiss-Prot (Q6UN15.1)"
     Site            339..340
                     /site_type="other"
                     /note="Breakpoint for interstitial deletion to form the
                     FIP1L1-PDGFRA fusion protein; propagated from
                     UniProtKB/Swiss-Prot (Q6UN15.1)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q6UN15.1)"
     Region          452..603
                     /region_name="Sufficient for interaction with CPSF1 and
                     CSTF3. /evidence=ECO:0000269|PubMed:14749727"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UN15.1)"
     Region          466..499
                     /region_name="Arg/Asp/Glu-rich domain.
                     /evidence=ECO:0000269|PubMed:29276085"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UN15.1)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6UN15.1)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q6UN15.1)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q6UN15.1)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q6UN15.1)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q6UN15.1)"
     CDS             1..603
                     /gene="FIP1L1"
                     /gene_synonym="FIP1; hFip1; Rhe"
                     /coded_by="NM_001376745.1:199..2010"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS93495.1"
                     /db_xref="GeneID:81608"
                     /db_xref="HGNC:HGNC:19124"
                     /db_xref="MIM:607686"
ORIGIN      
        1 msageverlv selsggtggd eeeewlyggp wdvhvhsdla kdldenever peeenasanp
       61 psgiedetae ngvpkpkvte teddsdsdsd ddeddvhvti gdiktgapqy gsygtapvnl
      121 niktggrvyg ttgtkvkgvd ldapgsingv pllevdldsf edkpwrkpga dlsdyfnygf
      181 nedtwkayce kqkrirmgle vipvtsttnk itaedctmev tpgaeiqdgr fnlfkvqqgr
      241 tgnseketal pstkaeftsp pslfktglpp srnstssqsq tstasrkans svgkwqdryg
      301 raespdlrrl pgaidvigqt itisrvegrr ranensniqv lsersatevd nnfskpppff
      361 ppgappthlp pppflppppt vstapplipp pgipitvppp gfppppgapp psliptiesg
      421 hssgydsrsa rafpygnvaf phlpgsapsw pslvdtskqw dyyarrekdr drerdrdrer
      481 drdrdrerer trerererdh sptpsvfnsd eeryryreya ergyerhras rekeerhrer
      541 rhrekeetrh kssrsnsrrr heseegdshr rhkhkkskrs kegkeagsep apeqesteat
      601 pae
//
LOCUS       NP_001364472            1919 aa            linear   PRI 21-NOV-2025
DEFINITION  dedicator of cytokinesis protein 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001364472
VERSION     NP_001364472.1
DBSOURCE    REFSEQ: accession NM_001377543.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1919)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1919)
  AUTHORS   Najafi,S., Hashemi-Gorji,F., Roudgari,H., Goudarzi,M.,
            Jafarzadegan,A.M. and Sheykhbahaei,N.
  TITLE     Genetic change investigation in DOCK1 gene in an Iranian family
            with sign and symptoms of temporomandibular joint disorder (TMD)
  JOURNAL   Clin Oral Investig 28 (8), 432 (2024)
   PUBMED   39020145
  REMARK    GeneRIF: Genetic change investigation in DOCK1 gene in an Iranian
            family with sign and symptoms of temporomandibular joint disorder
            (TMD).
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1919)
  AUTHORS   Liu,D., Dredge,B.K., Bert,A.G., Pillman,K.A., Toubia,J., Guo,W.,
            Dyakov,B.J.A., Migault,M.M., Conn,V.M., Conn,S.J., Gregory,P.A.,
            Gingras,A.C., Patel,D., Wu,B. and Goodall,G.J.
  TITLE     ESRP1 controls biogenesis and function of a large abundant
            multiexon circRNA
  JOURNAL   Nucleic Acids Res 52 (3), 1387-1403 (2024)
   PUBMED   38015468
  REMARK    GeneRIF: ESRP1 controls biogenesis and function of a large abundant
            multiexon circRNA.
REFERENCE   4  (residues 1 to 1919)
  AUTHORS   Xu,Y., Liu,X., Zeng,W., Zhu,Y., Dong,J., Wu,F., Chen,C., Sharma,S.
            and Lin,Y.
  TITLE     DOCK1 insufficiency disrupts trophoblast function and pregnancy
            outcomes via DUSP4-ERK pathway
  JOURNAL   Life Sci Alliance 7 (2), e202302247 (2023)
   PUBMED   37967942
  REMARK    GeneRIF: DOCK1 insufficiency disrupts trophoblast function and
            pregnancy outcomes via DUSP4-ERK pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1919)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 1919)
  AUTHORS   Wu,Y.C. and Horvitz,H.R.
  TITLE     C. elegans phagocytosis and cell-migration protein CED-5 is similar
            to human DOCK180
  JOURNAL   Nature 392 (6675), 501-504 (1998)
   PUBMED   9548255
REFERENCE   7  (residues 1 to 1919)
  AUTHORS   Savill,J.
  TITLE     Apoptosis. Phagocytic docking without shocking
  JOURNAL   Nature 392 (6675), 442-443 (1998)
   PUBMED   9548247
REFERENCE   8  (residues 1 to 1919)
  AUTHORS   Takai,S., Hasegawa,H., Kiyokawa,E., Yamada,K., Kurata,T. and
            Matsuda,M.
  TITLE     Chromosomal mapping of the gene encoding DOCK180, a major
            Crk-binding protein, to 10q26.13-q26.3 by fluorescence in situ
            hybridization
  JOURNAL   Genomics 35 (2), 403-404 (1996)
   PUBMED   8661160
REFERENCE   9  (residues 1 to 1919)
  AUTHORS   Matsuda,M., Ota,S., Tanimura,R., Nakamura,H., Matuoka,K.,
            Takenawa,T., Nagashima,K. and Kurata,T.
  TITLE     Interaction between the amino-terminal SH3 domain of CRK and its
            natural target proteins
  JOURNAL   J Biol Chem 271 (24), 14468-14472 (1996)
   PUBMED   8662907
REFERENCE   10 (residues 1 to 1919)
  AUTHORS   Hasegawa,H., Kiyokawa,E., Tanaka,S., Nagashima,K., Gotoh,N.,
            Shibuya,M., Kurata,T. and Matsuda,M.
  TITLE     DOCK180, a major CRK-binding protein, alters cell morphology upon
            translocation to the cell membrane
  JOURNAL   Mol Cell Biol 16 (4), 1770-1776 (1996)
   PUBMED   8657152
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607029.17, BX470155.5,
            BX470201.4, AL359094.14, AL390920.22, AL157711.12 and AL355316.12.
            
            Summary: This gene encodes a member of the dedicator of cytokinesis
            protein family. Dedicator of cytokinesis proteins act as guanine
            nucleotide exchange factors for small Rho family G proteins. The
            encoded protein regulates the small GTPase Rac, thereby influencing
            several biological processes, including phagocytosis and cell
            migration. Overexpression of this gene has also been associated
            with certain cancers. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Mar 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3050710.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1919
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.2"
     Protein         1..1919
                     /product="dedicator of cytokinesis protein 1 isoform 3"
                     /note="DOwnstream of CrK; 180 kDa protein downstream of
                     CRK"
                     /calculated_mol_wt=221055
     Region          13..68
                     /region_name="SH3_DOCK1_5_A"
                     /note="Src Homology 3 domain of Class A Dedicator of
                     Cytokinesis proteins 1 and 5; cd12051"
                     /db_xref="CDD:212984"
     Site            order(15..19,26,31..33,35,39..40,44..45,47,55,57,59,61,
                     63..64,66,68)
                     /site_type="other"
                     /note="ELMO interaction site [polypeptide binding]"
                     /db_xref="CDD:212984"
     Site            order(18,20,23,27,44..45,61,63..64)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212984"
     Region          76..416
                     /region_name="DOCK_N"
                     /note="DOCK N-terminus; pfam16172"
                     /db_xref="CDD:465040"
     Region          424..619
                     /region_name="C2_Dock-A"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class A proteins; cd08694"
                     /db_xref="CDD:176076"
     Region          1214..1666
                     /region_name="DHR2_DOCK"
                     /note="Dock Homology Region 2, a GEF domain, of Dedicator
                     of Cytokinesis proteins; cl06123"
                     /db_xref="CDD:471388"
     Site            order(1298,1309,1311..1312,1314..1315,1318..1319,
                     1321..1322,1325..1326)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:212566"
     Site            order(1337,1339,1363,1366..1369,1371..1372,1385..1387,
                     1404..1406,1493..1496,1507..1508,1511,1513,1550..1551,
                     1554,1574..1575,1577..1578,1581..1583,1586..1588,
                     1591..1592,1595,1625,1646..1647,1650)
                     /site_type="other"
                     /note="Rac/Cdc42 binding site [polypeptide binding]"
                     /db_xref="CDD:212566"
     Site            order(1586..1588,1591)
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212566"
     CDS             1..1919
                     /gene="DOCK1"
                     /gene_synonym="ced5; DOCK180"
                     /coded_by="NM_001377543.1:91..5850"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:1793"
                     /db_xref="HGNC:HGNC:2987"
                     /db_xref="MIM:601403"
ORIGIN      
        1 mtrwvptkre ekygvafyny dargadelsl qigdtvhile tyegwyrgyt lrkkskkgif
       61 pasyihlkea ivegkgqhet vipgdlpliq evtttlrews tiwrqlyvqd nremfrsvrh
      121 miydliewrs qilsgtlpqd elkelkkkvt akidygnril dldlvvrded gnildpelts
      181 tislfrahei askqveerlq eeksqkqnid inrqakfaat pslalfvnlk nvvckigeda
      241 evlmslydpv eskfisenyl vrwsssglpk didrlhnlra vftdlgskdl krekisfvcq
      301 ivrvgrmelr dnntrkltsg lrrpfgvavm dvtdiingkv ddedkqhfip fqpvagendf
      361 lqtvinkvia akevnhkgqg lwvtlkllpg dihqirkefp hlvdrttava rktgfpeiim
      421 pgdvrndiyv tlvqgdfdkg skttaknvev tvsvydedgk rlehvifpga gdeaiseyks
      481 viyyqvkqpr wfetvkvaip iedvnrshlr ftfrhrssqd skdksekifa lafvklmryd
      541 gttlrdgehd livykaeakk ledaatylsl pstkaeleek ghsatgksmq slgsctiskd
      601 sfqistlvcs tkltqnvdll gllkwrsnts llqqnlrqlm kvdggevvkf lqdtldalfn
      661 immenseset fdtlvfdalv fiigliadrk fqhfnpvlet yikkhfsatl aytkltkvlk
      721 nyvdgaekpg vneqlykamk alesifkfiv rsrilfnqly enkgeadfve sllqlfrsin
      781 dmmssmsdqt vrvkgaalky lptivndvkl vfdpkelskm ftefilnvpm glltiqklyc
      841 lieivhsdlf tqhdcreill pmmtdqlkyh lerqedleac cqllshilev lyrkdvgptq
      901 rhvqiimekl lrtvnrtvis mgrdselign fvacmtailr qmedyhyahl iktfgkmrtd
      961 vvdflmetfi mfknligknv ypfdwvimnm vqnkvflrai nqyadmlnkk fldqanfelq
     1021 lwnnyfhlav afltqeslql enfssakrak ilnkygdmrr qigfeirdmw ynlgqhkikf
     1081 ipemvgpile mtlipetelr katipiffdm mqcefhstrs fqmfeneiit kldheveggr
     1141 gdeqykvlfd killehcrkh kylaktgetf vklvvrlmer lldyrtimhd enkenrmsct
     1201 vnvlnfykei ereemyiryl yklcdlhkec dnyteaaytl llhakllkws edvcvahltq
     1261 rdgyqattqg qlkeqlyqei ihyfdkgkmw eeaialgkel aeqyenemfd yeqlsellkk
     1321 qaqfyenivk virpkpdyfa vgyygqgfpt flrgkvfiyr gkeyerredf earlltqfpn
     1381 aekmkttspp gddiknspgq yiqcftvkpk ldlppkfhrp vseqivrglk qivtlrafsd
     1441 avvsfaveac lhfsageksv svsprpalcm rkaclvprpr sfyrvnevqr feysrpirkg
     1501 eknpdnefan mwiertiytt ayklpgilrw fevksvfmve isplenaiet mqltndkins
     1561 mvqqhlddps lpinplsmll ngivdpavmg gfanyekaff tdrylqehpe ahekieklkd
     1621 liawqipfla egirihgdkv tealrpfher meacfkqlke kvekeygvri mpsslddrrg
     1681 srprsmvrsf tmpsssrpls vasvsslssd stpsrpgsdg falepllpkk mhsrsqdkld
     1741 kddlekekkd kkkekrnskh qeifekefkp tdislqqsea vilsetispl rpqrpksqvm
     1801 nvigserrfs vspsspssqq tpppvtprak lsfsmqssle lngmtgadva dvppplplkg
     1861 svadygnlme nqdllgsptp ppppphqrhl ppplpsktpp ppppkttrkq asvdsgivq
//
LOCUS       NP_001371754            1045 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 88 [Homo sapiens].
ACCESSION   NP_001371754
VERSION     NP_001371754.1
DBSOURCE    REFSEQ: accession NM_001384825.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1045)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1045)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1045)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1045)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1045)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1045)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1045)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1045)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1045)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1045)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2662726.1,
                                           SRR18074967.2309081.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1045
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1045
                     /product="microtubule-associated protein 4 isoform 88"
                     /note="MAP-4"
                     /calculated_mol_wt=109559
     Region          <537..881
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <893..914
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          916..945
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          947..977
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1045
                     /gene="MAP4"
                     /coded_by="NM_001384825.1:96..3233"
                     /note="isoform 88 is encoded by transcript variant 80"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgsp tefleekmay qeypnsqnwp
      121 edtnfcfqpe qvvdpiqtgm spcntavvpq gwsvealnsp hsesfvspea vaeppqptav
      181 plelakeiem aseerppaqa leimmglktt dmapsketem alakdmalat ktevalakdm
      241 esptkldvtl akdmqpsmes dmalvkdmel ptekevalvk dvrwptetdv ssaknvvlpt
      301 etevapakdv tllketeras pikmdlapsk dmgppkenkk eteraspikm dlapskdmgp
      361 pkenkivpak dlvllseiev aqandiisst eissaekval ssetevalar dmtlppetnv
      421 iltkdkalpl eaevapvkdm aqlpeteiap akdvapstvk evgllkdmsp lsetemalgk
      481 dvtpppetev vliknvclpp emevaltedq vpalkteapl akdgvltlan nvtpakdvpp
      541 lseteatpvp ikdmeiaqtq kgisedshle slqdvgqsaa ptfmispetv tgtgkkcslp
      601 aeedsvlekl gerkpcnsqp selssetsgi arpeegrpvv sgtgndittp pnkelppspe
      661 kktkplattq paktstskak tqptslpkqp apttigglnk kpmslasglv paappkrpav
      721 asarpsilps kdvkpkpiad akapekrasp skpasapasr sgskstqtva ktttaaavas
      781 tgpssrspst llpkkptaik tegkpaevkk mtaksvpadl srpkststss mkktttlsgt
      841 apaagvvpsr vkatpmpsrp sttpfidkkp tsakpssttp rlsrlatnts apdlknvrsk
      901 vgstenikhq pgggrvqiqn kkvdiskvss kcgskanikh kpgggdvkie sqklnfkeka
      961 qakvgsldnv ghlpaggavk tegggseapl cpgppageep aiseaapeag aptsasglng
     1021 hptlsgggdq reaqtldsqi qetsi
//
LOCUS       NP_001387096            1212 aa            linear   PRI 21-NOV-2025
DEFINITION  protein transport protein Sec31A isoform 15 [Homo sapiens].
ACCESSION   NP_001387096
VERSION     NP_001387096.1
DBSOURCE    REFSEQ: accession NM_001400167.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1212)
  AUTHORS   Tobias,E.S., Lucas-Herald,A.K., Sagar,D., Montezano,A.C.,
            Rios,F.J., De Lucca Camargo,L., Hamilton,G., Gazdagh,G.,
            Diver,L.A., Williams,N., Herzyk,P., Touyz,R.M., Greenfield,A.,
            McGowan,R. and Ahmed,S.F.
  TITLE     SEC31A may be associated with pituitary hormone deficiency and
            gonadal dysgenesis
  JOURNAL   Endocrine 84 (2), 345-349 (2024)
   PUBMED   38400880
  REMARK    GeneRIF: SEC31A may be associated with pituitary hormone deficiency
            and gonadal dysgenesis.
REFERENCE   2  (residues 1 to 1212)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1212)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1212)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1212)
  AUTHORS   Jin,L., Pahuja,K.B., Wickliffe,K.E., Gorur,A., Baumgartel,C.,
            Schekman,R. and Rape,M.
  TITLE     Ubiquitin-dependent regulation of COPII coat size and function
  JOURNAL   Nature 482 (7386), 495-500 (2012)
   PUBMED   22358839
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1212)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1212)
  AUTHORS   Kim,J.H., Hong,J.A., Pih,K.T. and Hwang,I.
  TITLE     Identification and isolation of differentially expressed genes in
            osmotically stressed human oral keratinocytes
  JOURNAL   Arch Oral Biol 46 (4), 335-341 (2001)
   PUBMED   11269867
REFERENCE   8  (residues 1 to 1212)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 1212)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   10 (residues 1 to 1212)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021105.13 and AC108469.5.
            
            Summary: The protein encoded by this gene shares similarity with
            the yeast Sec31 protein, and is a component of the outer layer of
            the coat protein complex II (COPII). The encoded protein is
            involved in vesicle budding from the endoplasmic reticulum (ER) and
            contains multiple WD repeats near the N-terminus and a proline-rich
            region in the C-terminal half. It associates with the protein
            encoded by the SEC13 homolog, nuclear pore and COPII coat complex
            component (SEC13), and is required for ER-Golgi transport.
            Monoubiquitylation of this protein by CUL3-KLHL12 was found to
            regulate the size of COPII coats to accommodate unusually shaped
            cargo. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.716319.1,
                                           SRR18074967.3712452.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1212
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..1212
                     /product="protein transport protein Sec31A isoform 15"
                     /note="yeast Sec31p homolog; protein transport protein
                     Sec31A; web1-like protein; SEC31 homolog A, COPII coat
                     complex component; SEC31-related protein A; SEC31-like
                     protein 1; SEC31 homolog A, COPII coating complex
                     component"
                     /calculated_mol_wt=132117
     Region          13..332
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(26,40,46..47,52..53,91,95,101..102,117,121,139,144,
                     150..151,164,185,190,196..197,209..210,231,235,244..245,
                     258..259,277,282,288..289,301..302,320,325,331..332)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          70..119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          125..162
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          172..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          263..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          306..331
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <534..>657
                     /region_name="ACE1-Sec16-like"
                     /note="Ancestral coatomer element 1 (ACE1) of COPII coat
                     complex assembly protein Sec16; cl14807"
                     /db_xref="CDD:449359"
     Site            order(535..539,541,543,554,556,557..558,560..561,565,571,
                     579,591,594,619..620)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187750"
     Region          737..>1090
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     CDS             1..1212
                     /gene="SEC31A"
                     /gene_synonym="ABP125; ABP130; HPBKS; HSPC275; HSPC334;
                     NEDSOSB; SEC31L1"
                     /coded_by="NM_001400167.1:71..3709"
                     /note="isoform 15 is encoded by transcript variant 23"
                     /db_xref="GeneID:22872"
                     /db_xref="HGNC:HGNC:17052"
                     /db_xref="MIM:610257"
ORIGIN      
        1 mklkevdrta mqawspaqnh piylatgtsa qqldatfstn asleifeldl sdpsldmksc
       61 atfssshryh kliwgpykmd skgdvsgvli aggengniil ydpskiiagd kevviaqndk
      121 htgpvraldv nifqtnlvas ganeseiyiw dlnnfatpmt pgaktqpped isciawnrqv
      181 qhilasasps gratvwdlrk nepiikvsdh snrmhcsgla whpdvatqmv laseddrlpv
      241 iqmwdlrfas splrvlenha rgilaiawsm adpelllscg kdakilcsnp ntgevlyelp
      301 tntqwcfdiq wcprnpavls aasfdgrisv ysimggstdg lrqkqvdkls ssfgnldpfg
      361 tgqplpplqi pqqtaqhsiv lplkkppkwi rrpvgasfsf ggklvtfenv rmpshqgaeq
      421 qqqqhhvfis qvvtekefls rsdqlqqavq sqgfinycqk kidasqtefe knvwsflkvn
      481 feddsrgkyl ellgyrkedl gkkhikeeke eseflpssgg tfnisvsgdi dglitqallt
      541 gnfesavdlc lhdnrmadai ilaiaggqel lartqkkyfa ksqskitrli tavvmknwke
      601 ivescdlknw realaavlty akpdefsalc dllgtrlene gdsllqtqac lcyicagnve
      661 klvacwtkaq dgshplslqd liekvvilrk avqltqamdt stvgvllaak msqyanllaa
      721 qgsiaaalaf lpdntnqpni mqlrdrlcra qgepvaghes pkipyekqql pkgrpgpvag
      781 hhqmprvqtq qyyphvriap tvttwsnktp talpshppaa spsdtqgenp pppgfimhgn
      841 vnpnaagqlp tspghmhtqv ppypqpqpyq paqpypfgtg gsamyrpqqp vapptsnayp
      901 ntpyissass ytgqsqlyaa qhqassptss patsfpppps sgasfqhggp gappsssaya
      961 lppgttgtlp aaselpasqr tgpqngwndp palnrvpkkk kmpenfmppv pitspimnpl
     1021 gdpqsqmlqq qpsapvplss qssfpqphlp ggqpfhgvqq plgqtgmpps fskpniegap
     1081 gapigntfqh vqslptkkit kkpipdehli lkttfedliq rclssatdpq tkrklddask
     1141 rleflydklr eqtlsptits glhniarsie trnysegltm hthivstsnf setsafmpvl
     1201 kvvltqankl gv
//
LOCUS       NP_000864                275 aa            linear   PRI 21-NOV-2025
DEFINITION  intercellular adhesion molecule 2 precursor [Homo sapiens].
ACCESSION   NP_000864
VERSION     NP_000864.2
DBSOURCE    REFSEQ: accession NM_000873.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Tang,X., Huang,J., Jiang,Y., Qiu,J., Li,T., Li,W., Chen,Z.,
            Huang,Z., Yu,X., Yang,T., Ji,X., Tan,R., Lv,L., Yang,Z. and Chen,H.
  TITLE     Intercellular adhesion molecule 2 as a novel prospective tumor
            suppressor induced by ERG promotes ubiquitination-mediated radixin
            degradation to inhibit gastric cancer tumorigenicity and metastasis
  JOURNAL   J Transl Med 21 (1), 670 (2023)
   PUBMED   37759298
  REMARK    GeneRIF: Intercellular adhesion molecule 2 as a novel prospective
            tumor suppressor induced by ERG promotes ubiquitination-mediated
            radixin degradation to inhibit gastric cancer tumorigenicity and
            metastasis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Chong,D.L.W., Rebeyrol,C., Jose,R.J., Williams,A.E., Brown,J.S.,
            Scotton,C.J. and Porter,J.C.
  TITLE     ICAM-1 and ICAM-2 Are Differentially Expressed and Up-Regulated on
            Inflamed Pulmonary Epithelium, but Neither ICAM-2 nor LFA-1: ICAM-1
            Are Required for Neutrophil Migration Into the Airways In Vivo
  JOURNAL   Front Immunol 12, 691957 (2021)
   PUBMED   34484188
  REMARK    GeneRIF: ICAM-1 and ICAM-2 Are Differentially Expressed and
            Up-Regulated on Inflamed Pulmonary Epithelium, but Neither ICAM-2
            nor LFA-1: ICAM-1 Are Required for Neutrophil Migration Into the
            Airways In Vivo.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Jin,X., Bu,Q., Zou,Y., Feng,Y. and Wei,M.
  TITLE     Lewis-antigen-containing ICAM-2/3 on Jurkat leukemia cells interact
            with DC-SIGN to regulate DC functions
  JOURNAL   Glycoconj J 35 (3), 287-297 (2018)
   PUBMED   29671117
  REMARK    GeneRIF: Lewis-antigen-containing ICAM-2/3 on Jurkat leukemia cells
            interact with DC-SIGN to regulate DC functions.
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Zuo,Y., Cui,Y., Di Poto,C., Varghese,R.S., Yu,G., Li,R. and
            Ressom,H.W.
  TITLE     INDEED: Integrated differential expression and differential network
            analysis of omic data for biomarker discovery
  JOURNAL   Methods 111, 12-20 (2016)
   PUBMED   27592383
  REMARK    GeneRIF: INDEED also identified some candidates previously reported
            to be relevant to HCC, such as intercellular adhesion molecule 2
            (ICAM2) and c4b-binding protein alpha chain (C4BPA), which were
            missed by both Differential expression and differential network
            analyses
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Sasaki,Y., Tamura,M., Takeda,K., Ogi,K., Nakagaki,T., Koyama,R.,
            Idogawa,M., Hiratsuka,H. and Tokino,T.
  TITLE     Identification and characterization of the intercellular adhesion
            molecule-2 gene as a novel p53 target
  JOURNAL   Oncotarget 7 (38), 61426-61437 (2016)
   PUBMED   27556181
  REMARK    GeneRIF: ICAM2 induction by p53 has a key role in inhibiting cancer
            cell migration and invasion.ICAM2 acts at least in part through the
            suppression of the MEK-ERK signaling pathway.
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Fawcett,J., Holness,C.L., Needham,L.A., Turley,H., Gatter,K.C.,
            Mason,D.Y. and Simmons,D.L.
  TITLE     Molecular cloning of ICAM-3, a third ligand for LFA-1,
            constitutively expressed on resting leukocytes
  JOURNAL   Nature 360 (6403), 481-484 (1992)
   PUBMED   1448173
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Sansom,D., Borrow,J., Solomon,E. and Trowsdale,J.
  TITLE     The human ICAM2 gene maps to 17q23-25
  JOURNAL   Genomics 11 (2), 462-464 (1991)
   PUBMED   1769660
REFERENCE   8  (residues 1 to 275)
  AUTHORS   de Fougerolles,A.R., Stacker,S.A., Schwarting,R. and Springer,T.A.
  TITLE     Characterization of ICAM-2 and evidence for a third
            counter-receptor for LFA-1
  JOURNAL   J Exp Med 174 (1), 253-267 (1991)
   PUBMED   1676048
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Staunton,D.E., Dustin,M.L. and Springer,T.A.
  TITLE     Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1
            homologous to ICAM-1
  JOURNAL   Nature 339 (6219), 61-64 (1989)
   PUBMED   2497351
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Dustin,M.L., Garcia-Aguilar,J., Hibbs,M.L., Larson,R.S.,
            Stacker,S.A., Staunton,D.E., Wardlaw,A.J. and Springer,T.A.
  TITLE     Structure and regulation of the leukocyte adhesion receptor LFA-1
            and its counterreceptors, ICAM-1 and ICAM-2
  JOURNAL   Cold Spring Harb Symp Quant Biol 54 Pt 2, 753-765 (1989)
   PUBMED   2577025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK223219.1.
            
            On Jul 24, 2007 this sequence version replaced NP_000864.1.
            
            Summary: The protein encoded by this gene is a member of the
            intercellular adhesion molecule (ICAM) family. All ICAM proteins
            are type I transmembrane glycoproteins, contain 2-9
            immunoglobulin-like C2-type domains, and bind to the leukocyte
            adhesion LFA-1 protein. This protein may play a role in lymphocyte
            recirculation by blocking LFA-1-dependent cell adhesion. It
            mediates adhesive interactions important for antigen-specific
            immune response, NK-cell mediated clearance, lymphocyte
            recirculation, and other cellular interactions important for immune
            response and surveillance. Several transcript variants encoding the
            same protein have been found for this gene. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (5) differs in the 5' UTR compared
            to variant 1. All 5 variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK223219.1, BC003097.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2150385
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.3"
     Protein         1..275
                     /product="intercellular adhesion molecule 2 precursor"
                     /note="ICAM-2"
                     /calculated_mol_wt=28392
     sig_peptide     1..21
                     /calculated_mol_wt=2281
     mat_peptide     22..275
                     /product="intercellular adhesion molecule 2"
                     /calculated_mol_wt=28392
     Region          27..109
                     /region_name="IgI_N_ICAM-2"
                     /note="N-terminal immunoglobulin domain of the
                     intercellular adhesion molecules ICAM-2 (Cluster of
                     Differentiation 102 or CD102); member of the I-set of IgSF
                     domains; cd20995"
                     /db_xref="CDD:409587"
     Region          29..32
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409587"
     Region          35..38
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409587"
     Region          43..49
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409587"
     Site            47
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:9153399,
                     ECO:0007744|PDB:1ZXQ; propagated from UniProtKB/Swiss-Prot
                     (P13598.2)"
     Region          56..61
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409587"
     Region          63..64
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409587"
     Region          66..72
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409587"
     Region          75..80
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409587"
     Site            82
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973,
                     ECO:0000269|PubMed:9153399, ECO:0007744|PDB:1ZXQ;
                     propagated from UniProtKB/Swiss-Prot (P13598.2)"
     Region          86..94
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409587"
     Region          98..108
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409587"
     Site            105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:9153399,
                     ECO:0007744|PDB:1ZXQ; propagated from UniProtKB/Swiss-Prot
                     (P13598.2)"
     Region          111..211
                     /region_name="IgC2_2_ICAM-1_like"
                     /note="Second immunoglobulin (Ig)-like C2-set domain of
                     intercellular cell adhesion molecule 1 (ICAM-1), and
                     similar domains; cd05755"
                     /db_xref="CDD:409413"
     Region          111..118
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409413"
     Region          129..138
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409413"
     Region          145..151
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409413"
     Region          153..156
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409413"
     Site            153
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973,
                     ECO:0000269|PubMed:9153399, ECO:0007744|PDB:1ZXQ;
                     propagated from UniProtKB/Swiss-Prot (P13598.2)"
     Region          171..178
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409413"
     Site            176
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P13598.2)"
     Region          186..193
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409413"
     Site            187
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:9153399,
                     ECO:0007744|PDB:1ZXQ; propagated from UniProtKB/Swiss-Prot
                     (P13598.2)"
     Region          202..209
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409413"
     Site            224..248
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13598.2)"
     Region          251..275
                     /region_name="Required for interaction with EZR, MSN and
                     RDX and co-localization to microvilli.
                     /evidence=ECO:0000250|UniProtKB:P35330"
                     /note="propagated from UniProtKB/Swiss-Prot (P13598.2)"
     CDS             1..275
                     /gene="ICAM2"
                     /gene_synonym="CD102"
                     /coded_by="NM_000873.4:72..899"
                     /db_xref="CCDS:CCDS11657.1"
                     /db_xref="GeneID:3384"
                     /db_xref="HGNC:HGNC:5345"
                     /db_xref="MIM:146630"
ORIGIN      
        1 mssfgyrtlt valftliccp gsdekvfevh vrpkklavep kgslevncst tcnqpevggl
       61 etsldkilld eqaqwkhylv snishdtvlq chftcsgkqe smnsnvsvyq pprqviltlq
      121 ptlvavgksf tiecrvptve pldsltlflf rgnetlhyet fgkaapapqe atatfnstad
      181 redghrnfsc lavldlmsrg gnifhkhsap kmleiyepvs dsqmviivtv vsvllslfvt
      241 svllcfifgq hlrqqrmgty gvraawrrlp qafrp
//
LOCUS       NP_001366484             851 aa            linear   PRI 21-NOV-2025
DEFINITION  KN motif and ankyrin repeat domain-containing protein 2 isoform 2
            [Homo sapiens].
ACCESSION   NP_001366484
VERSION     NP_001366484.1
DBSOURCE    REFSEQ: accession NM_001379555.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 851)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 851)
  AUTHORS   Loncaric,M., Stojanovic,N., Rac-Justament,A., Coopmans,K.,
            Majhen,D., Humphries,J.D., Humphries,M.J. and Ambriovic-Ristov,A.
  TITLE     Talin2 and KANK2 functionally interact to regulate microtubule
            dynamics, paclitaxel sensitivity and cell migration in the
            MDA-MB-435S melanoma cell line
  JOURNAL   Cell Mol Biol Lett 28 (1), 56 (2023)
   PUBMED   37460977
  REMARK    GeneRIF: Talin2 and KANK2 functionally interact to regulate
            microtubule dynamics, paclitaxel sensitivity and cell migration in
            the MDA-MB-435S melanoma cell line.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 851)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 851)
  AUTHORS   Xu,Y., Guo,C., Pan,W., Zhao,C., Ding,Y., Xie,X., Wei,Z., Sun,Y. and
            Yu,C.
  TITLE     Nephrotic-syndrome-associated mutation of KANK2 induces pathologic
            binding competition with physiological interactor KIF21A
  JOURNAL   J Biol Chem 297 (2), 100958 (2021)
   PUBMED   34274317
  REMARK    GeneRIF: Nephrotic-syndrome-associated mutation of KANK2 induces
            pathologic binding competition with physiological interactor
            KIF21A.
REFERENCE   5  (residues 1 to 851)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 851)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   7  (residues 1 to 851)
  AUTHORS   Kakinuma,N., Zhu,Y., Wang,Y., Roy,B.C. and Kiyama,R.
  TITLE     Kank proteins: structure, functions and diseases
  JOURNAL   Cell Mol Life Sci 66 (16), 2651-2659 (2009)
   PUBMED   19554261
  REMARK    Review article
REFERENCE   8  (residues 1 to 851)
  AUTHORS   Zhu,Y., Kakinuma,N., Wang,Y. and Kiyama,R.
  TITLE     Kank proteins: a new family of ankyrin-repeat domain-containing
            proteins
  JOURNAL   Biochim Biophys Acta 1780 (2), 128-133 (2008)
   PUBMED   17996375
REFERENCE   9  (residues 1 to 851)
  AUTHORS   Zhang,Y., Zhang,H., Liang,J., Yu,W. and Shang,Y.
  TITLE     SIP, a novel ankyrin repeat containing protein, sequesters steroid
            receptor coactivators in the cytoplasm
  JOURNAL   EMBO J 26 (11), 2645-2657 (2007)
   PUBMED   17476305
  REMARK    GeneRIF: SIP, a novel ankyrin repeat containing protein, sequesters
            steroid receptor coactivators in the cytoplasm.
REFERENCE   10 (residues 1 to 851)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009000.6 and AC011485.6.
            
            Summary: This gene encodes a member of the KN motif and ankyrin
            repeat domains (KANK) family of proteins, which play a role in
            cytoskeletal formation by regulating actin polymerization. The
            encoded protein functions in the sequestration of steroid receptor
            coactivators and possibly other proteins. Mutations in this gene
            are associated with impaired kidney podocyte function and nephrotic
            syndrome, and keratoderma and woolly hair. [provided by RefSeq, Jul
            2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AB040951.2, SRR14038197.839862.1
                                    [ECO:0000331]
            RNAseq introns       :: partial sample support SAMEA1968189
                                    [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..851
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..851
                     /product="KN motif and ankyrin repeat domain-containing
                     protein 2 isoform 2"
                     /note="KN motif and ankyrin repeat domain-containing
                     protein 2; kidney ankyrin repeat-containing protein 2;
                     SRC1-interacting protein; matrix-remodeling-associated
                     protein 3; ankyrin repeat domain-containing protein 25;
                     SRC-interacting protein; steroid receptor coactivator
                     interacting protein"
                     /calculated_mol_wt=91044
     Region          1..72
                     /region_name="Interaction with AIFM1.
                     /evidence=ECO:0000269|PubMed:22371500"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          31..69
                     /region_name="KN_motif"
                     /note="KN motif; pfam12075"
                     /db_xref="CDD:432311"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BX02; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BX02; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BX02; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            105
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          139..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BX02; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          304..325
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          416..584
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            472
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Site            552
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          614..651
                     /region_name="ANK 0, degenerate.
                     /evidence=ECO:0000269|PubMed:29183992"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          628..664
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <650..825
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          666..698
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          666..696
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          669..835
                     /region_name="Interaction with NCOA1.
                     /evidence=ECO:0000269|PubMed:17476305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q63ZY3.1)"
     Region          700..735
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          739..769
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(740,744..745,748..750,752..753,757,760,769,771,773,
                     777..778,781..783,785..786,790,793,803,805,807,811..812,
                     815..817,819..820,824,827)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          771..803
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..851
                     /gene="KANK2"
                     /gene_synonym="ANKRD25; MXRA3; NPHS16; PPKWH; SIP"
                     /coded_by="NM_001379555.1:461..3016"
                     /note="isoform 2 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS12255.1"
                     /db_xref="GeneID:25959"
                     /db_xref="HGNC:HGNC:29300"
                     /db_xref="MIM:614610"
ORIGIN      
        1 maqvlhvpap fpgtpgpasp pafpakdpdp pysvetpygy rldldflkyv ddiekghtlr
       61 rvavqrrprl sslprgpgsw wtsteslcsn asgdsrhsay sycgrgfypq ygaletrggf
      121 nprvertlld arrrledqaa tptglgsltp saagstaslv gvglppptpr ssglstpvpp
      181 saghlahvre qmagalrklr qleeqvklip vlqvklsvlq eekrqltvql ksqkflghpt
      241 agrgrselcl dlpdppedpv aletrsvgtw vrerdlgmpd geaalaakva vletqlkkal
      301 qelqaaqarq adpqpqawpp pdspvrvdtv rvvegpreve vvastaagap aqraqslepy
      361 gtglralamp grpesppvfr sqevvetmcp vpaaatsnvh mvkkisiter scdgaaglpe
      421 vpaesssspp gsevasltqp ekstgrvptq epthreptrq aasqeseeag gtggppagvr
      481 simkrkeeva dptahrrslq fvgvnggyes ssedsstaen isdndstene apeprervps
      541 vaeapqlrpa gtaaaktsrq ecqlsresqh iptaegasgs nteeeirmel spdlisacla
      601 lekyldnpna lterelkvay ttvlqewlrl acrsdahpel vrrhlvtfra msarlldyvv
      661 niadsngnta lhysvshanf pvvqqlldsg vckvdkqnra gyspimltal atlktqddie
      721 tvlqlfrlgn inakasqagq talmlavshg rvdvvkalla ceadvnvqdd dgstalmcac
      781 ehghkeiagl llavpscdis ltdrdgstal mvaldagqse iasmlysrmn ikcsfapmsd
      841 desptsssae e
//
LOCUS       NP_940992                176 aa            linear   PRI 21-NOV-2025
DEFINITION  basigin isoform 3 [Homo sapiens].
ACCESSION   NP_940992
VERSION     NP_940992.1
DBSOURCE    REFSEQ: accession NM_198590.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Dai,P., Ma,C., Jiang,T., Shi,J., Liu,S., Zheng,M., Zhou,Y., Li,X.,
            Liu,Y. and Chen,H.
  TITLE     CD147 mediates S protein pseudovirus of SARS-CoV-2 infection and
            its induction of spermatogonia apoptosis
  JOURNAL   Endocrine 85 (3), 1435-1445 (2024)
   PUBMED   38824220
  REMARK    GeneRIF: CD147 mediates S protein pseudovirus of SARS-CoV-2
            infection and its induction of spermatogonia apoptosis.
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Mygind,K.J., Nikodemus,D., Gnosa,S., Kweder,R., Albrechtsen,N.J.W.,
            Kveiborg,M., Erler,J.T. and Albrechtsen,R.
  TITLE     ADAM12-Generated Basigin Ectodomain Binds beta1 Integrin and
            Enhances the Expression of Cancer-Related Extracellular Matrix
            Proteins
  JOURNAL   Int J Mol Sci 25 (11), 5871 (2024)
   PUBMED   38892056
  REMARK    GeneRIF: ADAM12-Generated Basigin Ectodomain Binds beta1 Integrin
            and Enhances the Expression of Cancer-Related Extracellular Matrix
            Proteins.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Meng,S., Sorensen,E.E., Ponniah,M., Thorlacius-Ussing,J.,
            Crouigneau,R., Larsen,T., Borre,M.T., Willumsen,N., Flinck,M. and
            Pedersen,S.F.
  TITLE     MCT4 and CD147 colocalize with MMP14 in invadopodia and support
            matrix degradation and invasion by breast cancer cells
  JOURNAL   J Cell Sci 137 (8) (2024)
   PUBMED   38661040
  REMARK    GeneRIF: MCT4 and CD147 colocalize with MMP14 in invadopodia and
            support matrix degradation and invasion by breast cancer cells.
REFERENCE   5  (residues 1 to 176)
  AUTHORS   Liu,P., Xie,L., Wu,Q., Huang,L., Liu,X., Li,W., Cai,J., Wang,Z.,
            Yang,P. and Cai,L.
  TITLE     TIE1 promotes cervical cancer progression via Basigin-matrix
            metalloproteinase axis
  JOURNAL   Int J Biol Sci 20 (6), 2297-2309 (2024)
   PUBMED   38617545
  REMARK    GeneRIF: TIE1 promotes cervical cancer progression via
            Basigin-matrix metalloproteinase axis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 176)
  AUTHORS   Spring,F.A., Holmes,C.H., Simpson,K.L., Mawby,W.J., Mattes,M.J.,
            Okubo,Y. and Parsons,S.F.
  TITLE     The Oka blood group antigen is a marker for the M6 leukocyte
            activation antigen, the human homolog of OX-47 antigen, basigin and
            neurothelin, an immunoglobulin superfamily molecule that is widely
            expressed in human cells and tissues
  JOURNAL   Eur J Immunol 27 (4), 891-897 (1997)
   PUBMED   9130641
REFERENCE   7  (residues 1 to 176)
  AUTHORS   Kasinrerk,W., Fiebiger,E., Stefanova,I., Baumruker,T., Knapp,W. and
            Stockinger,H.
  TITLE     Human leukocyte activation antigen M6, a member of the Ig
            superfamily, is the species homologue of rat OX-47, mouse basigin,
            and chicken HT7 molecule
  JOURNAL   J Immunol 149 (3), 847-854 (1992)
   PUBMED   1634773
REFERENCE   8  (residues 1 to 176)
  AUTHORS   Miyauchi,T., Masuzawa,Y. and Muramatsu,T.
  TITLE     The basigin group of the immunoglobulin superfamily: complete
            conservation of a segment in and around transmembrane domains of
            human and mouse basigin and chicken HT7 antigen
  JOURNAL   J Biochem 110 (5), 770-774 (1991)
   PUBMED   1783610
REFERENCE   9  (residues 1 to 176)
  AUTHORS   Nabeshima,K., Lane,W.S. and Biswas,C.
  TITLE     Partial sequencing and characterization of the tumor cell-derived
            collagenase stimulatory factor
  JOURNAL   Arch Biochem Biophys 285 (1), 90-96 (1991)
   PUBMED   1846736
REFERENCE   10 (residues 1 to 176)
  AUTHORS   Kanekura,T., Miyauchi,T., Tashiro,M. and Muramatsu,T.
  TITLE     Basigin, a new member of the immunoglobulin superfamily: genes in
            different mammalian species, glycosylation changes in the molecule
            from adult organs and possible variation in the N-terminal
            sequences
  JOURNAL   Cell Struct Funct 16 (1), 23-30 (1991)
   PUBMED   2032306
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA007913.1 and GU557064.1.
            
            Summary: The protein encoded by this gene, basigin, is a plasma
            membrane protein that is important in spermatogenesis, embryo
            implantation, neural network formation, and tumor progression.
            Basigin is also a member of the immunoglobulin superfamily,
            ubiquitously expressed in various tissues. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, May 2020].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (3) is
            shorter at the N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: GU557064.1, DRR138512.231140.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..176
                     /product="basigin isoform 3"
                     /note="collagenase stimulatory factor; extracellular
                     matrix metalloproteinase inducer; OK blood group antigen;
                     leukocyte activation antigen M6; tumor cell-derived
                     collagenase stimulatory factor; hepatoma-associated
                     antigen"
                     /calculated_mol_wt=19307
     Region          19..109
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          29..33
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          74..78
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          89..94
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          102..105
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..176
                     /gene="BSG"
                     /gene_synonym="5F7; CD147; EMMPRIN; EMPRIN; HAb18G; OK;
                     TCSF"
                     /coded_by="NM_198590.3:510..1040"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58635.1"
                     /db_xref="GeneID:682"
                     /db_xref="HGNC:HGNC:1116"
                     /db_xref="MIM:109480"
ORIGIN      
        1 mgtaniqlhg pprvkavkss ehinegetam lvcksesvpp vtdwawykit dsedkalmng
       61 sesrffvsss qgrselhien lnmeadpgqy rcngtsskgs dqaiitlrvr shlaalwpfl
      121 givaevlvlv tiifiyekrr kpedvldddd agsaplkssg qhqndkgknv rqrnss
//
LOCUS       NP_001129242             392 aa            linear   PRI 21-NOV-2025
DEFINITION  poliovirus receptor isoform delta precursor [Homo sapiens].
ACCESSION   NP_001129242
VERSION     NP_001129242.2
DBSOURCE    REFSEQ: accession NM_001135770.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Sun,T., Yang,N., Li,L., Zhang,X., Liu,H., Kusuman,N., Chu,J.,
            Lu,G., Aji,T., Bi,X. and Lin,R.
  TITLE     sCD155 as a potential marker for diagnosing the vascular invasion
            in hepatic alveolar echinococcosis
  JOURNAL   Acta Trop 255, 107203 (2024)
   PUBMED   38604326
  REMARK    GeneRIF: sCD155 as a potential marker for diagnosing the vascular
            invasion in hepatic alveolar echinococcosis.
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Baker,F.L., Smith,K.A., Mylabathula,P.L., Zuniga,T.M., Diak,D.M.,
            Batatinha,H., Niemiro,G.M., Seckeler,M.D., Pedlar,C.R.,
            O'Connor,D.P., Colombo,J., Katsanis,E. and Simpson,R.J.
  TITLE     Exercise-induced beta2-adrenergic Receptor Activation Enhances the
            Antileukemic Activity of Expanded gammadelta T-Cells via DNAM-1
            Upregulation and PVR/Nectin-2 Recognition
  JOURNAL   Cancer Res Commun 4 (5), 1253-1267 (2024)
   PUBMED   38592213
  REMARK    GeneRIF: Exercise-induced beta2-adrenergic Receptor Activation
            Enhances the Antileukemic Activity of Expanded gammadelta T-Cells
            via DNAM-1 Upregulation and PVR/Nectin-2 Recognition.
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Tahara,S., Okumura,G., Matsuo,T., Shibuya,A. and Shibuya,K.
  TITLE     Essential role of CD155 glycosylation in functional binding to
            DNAM-1 on natural killer cells
  JOURNAL   Int Immunol 36 (6), 317-325 (2024)
   PUBMED   38289706
  REMARK    GeneRIF: Essential role of CD155 glycosylation in functional
            binding to DNAM-1 on natural killer cells.
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Liang,J., Liao,L., Xie,L., Tang,W., Yu,X., Lu,Y., Chen,H., Xu,J.,
            Sun,L., Wu,H., Cui,C. and Tan,Y.
  TITLE     PITPNC1 Suppress CD8+ T cell immune function and promote
            radioresistance in rectal cancer by modulating FASN/CD155
  JOURNAL   J Transl Med 22 (1), 117 (2024)
   PUBMED   38291470
  REMARK    GeneRIF: PITPNC1 Suppress CD8[+] T cell immune function and promote
            radioresistance in rectal cancer by modulating FASN/CD155.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Zibert,A. and Wimmer,E.
  TITLE     N glycosylation of the virus binding domain is not essential for
            function of the human poliovirus receptor
  JOURNAL   J Virol 66 (12), 7368-7373 (1992)
   PUBMED   1331527
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Koike,S., Ise,I. and Nomoto,A.
  TITLE     Functional domains of the poliovirus receptor
  JOURNAL   Proc Natl Acad Sci U S A 88 (10), 4104-4108 (1991)
   PUBMED   1851992
REFERENCE   8  (residues 1 to 392)
  AUTHORS   Koike,S., Horie,H., Ise,I., Okitsu,A., Yoshida,M., Iizuka,N.,
            Takeuchi,K., Takegami,T. and Nomoto,A.
  TITLE     The poliovirus receptor protein is produced both as membrane-bound
            and secreted forms
  JOURNAL   EMBO J 9 (10), 3217-3224 (1990)
   PUBMED   2170108
REFERENCE   9  (residues 1 to 392)
  AUTHORS   Schonk,D., van Dijk,P., Riegmann,P., Trapman,J., Holm,C.,
            Willcocks,T.C., Sillekens,P., van Venrooij,W., Wimmer,E., Geurts
            van Kessel,A. et al.
  TITLE     Assignment of seven genes to distinct intervals on the midportion
            of human chromosome 19q surrounding the myotonic dystrophy gene
            region
  JOURNAL   Cytogenet Cell Genet 54 (1-2), 15-19 (1990)
   PUBMED   1701111
REFERENCE   10 (residues 1 to 392)
  AUTHORS   Mendelsohn,C.L., Wimmer,E. and Racaniello,V.R.
  TITLE     Cellular receptor for poliovirus: molecular cloning, nucleotide
            sequence, and expression of a new member of the immunoglobulin
            superfamily
  JOURNAL   Cell 56 (5), 855-865 (1989)
   PUBMED   2538245
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC400059.1, AC243964.3 and
            M24406.1.
            
            On Apr 11, 2014 this sequence version replaced NP_001129242.1.
            
            Summary: The protein encoded by this gene is a transmembrane
            glycoprotein belonging to the immunoglobulin superfamily. The
            external domain mediates cell attachment to the extracellular
            matrix molecule vitronectin, while its intracellular domain
            interacts with the dynein light chain Tctex-1/DYNLT1. The gene is
            specific to the primate lineage, and serves as a cellular receptor
            for poliovirus in the first step of poliovirus replication.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (4) has an alternate 3' coding
            region and 3' UTR, compared to variant 1. The encoded isoform
            (delta), also known as H20B, has a shorter and distinct C-terminus,
            compared to isoform alpha.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M24406.1, SRR14038194.4462536.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..392
                     /product="poliovirus receptor isoform delta precursor"
                     /note="nectin-like protein 5; poliovirus receptor"
                     /calculated_mol_wt=40097
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2803
     Region          29..141
                     /region_name="IgV_1_Nectin-2_NecL-5_like_CD112_CD155"
                     /note="First immunoglobulin variable (IgV) domain of
                     nectin-2, nectin-like protein 5, and similar domains;
                     cd20989"
                     /db_xref="CDD:409581"
     Region          29..52
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409581"
     Region          29..33
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409581"
     Region          35..39
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409581"
     Region          44..52
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409581"
     Region          53..61
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409581"
     Region          62..68
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409581"
     Region          63..68
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409581"
     Region          69..86
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409581"
     Region          76..81
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409581"
     Region          83..86
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409581"
     Region          87..127
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409581"
     Region          91..97
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409581"
     Region          105..112
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409581"
     Site            105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P15151.2)"
     Region          119..127
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409581"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:22171320; propagated from
                     UniProtKB/Swiss-Prot (P15151.2)"
     Region          128..131
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409581"
     Region          131..141
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409581"
     Region          132..141
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409581"
     Region          145..241
                     /region_name="IgC1_2_Nectin-2_Necl-5_like"
                     /note="Second immunoglobulin (Ig) domain of Nectin-2 and
                     Nectin-like protein 5, and similar domains; member of the
                     C1-set of the Ig superfamily (IgSF) domains; cd07703"
                     /db_xref="CDD:409500"
     Region          145..151
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409500"
     Region          162..169
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409500"
     Region          174..180
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409500"
     Region          182..184
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409500"
     Region          187..195
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409500"
     Site            188
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15151.2)"
     Region          200..208
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409500"
     Region          218..225
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409500"
     Site            218
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15151.2)"
     Region          231..237
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409500"
     Site            237
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15151.2)"
     Region          244..329
                     /region_name="Ig3_Nectin-5_like"
                     /note="Third immunoglobulin domain of Nectin-like
                     Protein-5, and similar domains; cd20930"
                     /db_xref="CDD:409524"
     Region          244..250
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409524"
     Region          262..266
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409524"
     Region          276..281
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409524"
     Site            278
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P15151.2)"
     Region          283..286
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409524"
     Region          289..294
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409524"
     Region          295..301
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409524"
     Region          306..316
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409524"
     Site            307
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P15151.2)"
     Site            313
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15151.2)"
     Region          319..329
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409524"
     Site            344..367
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P15151.2)"
     Site            352
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P15151.2)"
     Site            360
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P15151.2)"
     Region          368..372
                     /region_name="DYNLT1 binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P15151.2)"
     CDS             1..392
                     /gene="PVR"
                     /gene_synonym="CD155; HVED; Necl-5; NECL5; PVS; TAGE4"
                     /coded_by="NM_001135770.4:188..1366"
                     /note="isoform delta precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS46107.1"
                     /db_xref="GeneID:5817"
                     /db_xref="HGNC:HGNC:9705"
                     /db_xref="MIM:173850"
ORIGIN      
        1 maramaaawp lllvallvls wpppgtgdvv vqaptqvpgf lgdsvtlpcy lqvpnmevth
       61 vsqltwarhg esgsmavfhq tqgpsysesk rlefvaarlg aelrnaslrm fglrvedegn
      121 ytclfvtfpq gsrsvdiwlr vlakpqntae vqkvqltgep vpmarcvstg grppaqitwh
      181 sdlggmpnts qvpgflsgtv tvtslwilvp ssqvdgknvt ckvehesfek pqlltvnltv
      241 yyppevsisg ydnnwylgqn eatltcdars npeptgynws ttmgplppfa vaqgaqllir
      301 pvdkpinttl icnvtnalga rqaeltvqvk egppsehsgm srnaiiflvl gilvflillg
      361 igiyfywskc srevlwhchl cpssehhqsc rn
//
LOCUS       NP_001073852             396 aa            linear   PRI 21-NOV-2025
DEFINITION  gap junction gamma-1 protein [Homo sapiens].
ACCESSION   NP_001073852
VERSION     NP_001073852.1
DBSOURCE    REFSEQ: accession NM_001080383.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Maciunas,K., Snipas,M., Kraujalis,T., Kraujaliene,L. and
            Panfilov,A.V.
  TITLE     The role of the Cx43/Cx45 gap junction voltage gating on wave
            propagation and arrhythmogenic activity in cardiac tissue
  JOURNAL   Sci Rep 13 (1), 14863 (2023)
   PUBMED   37684404
  REMARK    GeneRIF: The role of the Cx43/Cx45 gap junction voltage gating on
            wave propagation and arrhythmogenic activity in cardiac tissue.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Li,R.G., Xu,Y.J., Ye,W.G., Li,Y.J., Chen,H., Qiu,X.B., Yang,Y.Q.
            and Bai,D.
  TITLE     Connexin45 (GJC1) loss-of-function mutation contributes to familial
            atrial fibrillation and conduction disease
  JOURNAL   Heart Rhythm 18 (5), 684-693 (2021)
   PUBMED   33429106
  REMARK    GeneRIF: Connexin45 (GJC1) loss-of-function mutation contributes to
            familial atrial fibrillation and conduction disease.
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Choi,E.J., Palacios-Prado,N., Saez,J.C. and Lee,J.
  TITLE     Identification of Cx45 as a Major Component of GJs in HeLa Cells
  JOURNAL   Biomolecules 10 (10), 1389 (2020)
   PUBMED   33003547
  REMARK    GeneRIF: Identification of Cx45 as a Major Component of GJs in HeLa
            Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
REFERENCE   7  (residues 1 to 396)
  AUTHORS   Chanson,M., Scerri,I. and Suter,S.
  TITLE     Defective regulation of gap junctional coupling in cystic fibrosis
            pancreatic duct cells
  JOURNAL   J Clin Invest 103 (12), 1677-1684 (1999)
   PUBMED   10377174
REFERENCE   8  (residues 1 to 396)
  AUTHORS   Vozzi,C., Dupont,E., Coppen,S.R., Yeh,H.I. and Severs,N.J.
  TITLE     Chamber-related differences in connexin expression in the human
            heart
  JOURNAL   J Mol Cell Cardiol 31 (5), 991-1003 (1999)
   PUBMED   10336839
REFERENCE   9  (residues 1 to 396)
  AUTHORS   Kilarski,W.M., Dupont,E., Coppen,S., Yeh,H.I., Vozzi,C.,
            Gourdie,R.G., Rezapour,M., Ulmsten,U., Roomans,G.M. and Severs,N.J.
  TITLE     Identification of two further gap-junctional proteins, connexin40
            and connexin45, in human myometrial smooth muscle cells at term
  JOURNAL   Eur J Cell Biol 75 (1), 1-8 (1998)
   PUBMED   9523149
REFERENCE   10 (residues 1 to 396)
  AUTHORS   Kanter,H.L., Saffitz,J.E. and Beyer,E.C.
  TITLE     Molecular cloning of two human cardiac gap junction proteins,
            connexin40 and connexin45
  JOURNAL   J Mol Cell Cardiol 26 (7), 861-868 (1994)
   PUBMED   7966354
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005180.3, DA845933.1 and
            BC096216.3.
            
            Summary: This gene is a member of the connexin gene family. The
            encoded protein is a component of gap junctions, which are composed
            of arrays of intercellular channels that provide a route for the
            diffusion of low molecular weight materials from cell to cell.
            Alternatively spliced transcript variants encoding the same isoform
            have been described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1223507.1,
                                           SRR18074967.3216009.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..396
                     /product="gap junction gamma-1 protein"
                     /note="connexin-45; gap junction alpha-7 protein;
                     CTC-296K1.4; gap junction protein, gamma 1, 45kDa"
                     /calculated_mol_wt=45339
     Region          2..255
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            23..45
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P36383.2)"
     Site            76..95
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P36383.2)"
     Region          145..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P36383.2)"
     Site            176..198
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P36383.2)"
     Site            229..248
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P36383.2)"
     Region          353..396
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P36383.2)"
     CDS             1..396
                     /gene="GJC1"
                     /gene_synonym="CX45; GJA7"
                     /coded_by="NM_001080383.2:294..1484"
                     /db_xref="CCDS:CCDS11487.1"
                     /db_xref="GeneID:10052"
                     /db_xref="HGNC:HGNC:4280"
                     /db_xref="MIM:608655"
ORIGIN      
        1 mswsfltrll eeihnhstfv gkiwltvliv frivltavgg esiyydeqsk fvcnteqpgc
       61 envcydafap lshvrfwvfq iilvatpsvm ylgyaihkia kmehgeadkk aarskpyamr
      121 wkqhraleet eedneedpmm ypemelesdk enkeqsqpkp khdgrrrire dglmkiyvlq
      181 llartvfevg fligqyflyg fqvhpfyvcs rlpcphkidc fisrptekti fllimygvtg
      241 lclllniwem lhlgfgtird slnskrrele dpgaynypft wntpsappgy niavkpdqiq
      301 ytelsnakia ykqnkantaq eqqygsheen lpadlealqr eirmaqerld lavqayshqn
      361 nphgprekka kvgskagsnk stassksgdg ktsvwi
//
LOCUS       NP_001278951             547 aa            linear   PRI 21-NOV-2025
DEFINITION  antigen peptide transporter 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001278951
VERSION     NP_001278951.1
DBSOURCE    REFSEQ: accession NM_001292022.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Lee,J., Oldham,M.L., Manon,V. and Chen,J.
  TITLE     Principles of peptide selection by the transporter associated with
            antigen processing
  JOURNAL   Proc Natl Acad Sci U S A 121 (23), e2320879121 (2024)
   PUBMED   38805290
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Zhu,R., Chen,Y.T., Wang,B.W., You,Y.Y., Wang,X.H., Xie,H.T.,
            Jiang,F.G. and Zhang,M.C.
  TITLE     TAP1, a potential immune-related prognosis biomarker with
            functional significance in uveal melanoma
  JOURNAL   BMC Cancer 23 (1), 146 (2023)
   PUBMED   36774490
  REMARK    GeneRIF: TAP1, a potential immune-related prognosis biomarker with
            functional significance in uveal melanoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Tu,Z., Li,K., Ji,Q., Huang,Y., Lv,S., Li,J., Wu,L., Huang,K. and
            Zhu,X.
  TITLE     Pan-cancer analysis: predictive role of TAP1 in cancer prognosis
            and response to immunotherapy
  JOURNAL   BMC Cancer 23 (1), 133 (2023)
   PUBMED   36759763
  REMARK    GeneRIF: Pan-cancer analysis: predictive role of TAP1 in cancer
            prognosis and response to immunotherapy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 547)
  AUTHORS   Muller,I.K., Winter,C., Thomas,C., Spaapen,R.M., Trowitzsch,S. and
            Tampe,R.
  TITLE     Structure of an MHC I-tapasin-ERp57 editing complex defines
            chaperone promiscuity
  JOURNAL   Nat Commun 13 (1), 5383 (2022)
   PUBMED   36104323
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 547)
  AUTHORS   Li,B., Feng,Y., Hou,Q., Fu,Y. and Luo,Y.
  TITLE     Antigen Peptide Transporter 1 (TAP1) Promotes Resistance to MEK
            Inhibitors in Pancreatic Cancers
  JOURNAL   Int J Mol Sci 23 (13), 7168 (2022)
   PUBMED   35806187
  REMARK    GeneRIF: Antigen Peptide Transporter 1 (TAP1) Promotes Resistance
            to MEK Inhibitors in Pancreatic Cancers.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 547)
  AUTHORS   Beck,S., Kelly,A., Radley,E., Khurshid,F., Alderton,R.P. and
            Trowsdale,J.
  TITLE     DNA sequence analysis of 66 kb of the human MHC class II region
            encoding a cluster of genes for antigen processing
  JOURNAL   J Mol Biol 228 (2), 433-441 (1992)
   PUBMED   1453454
REFERENCE   7  (residues 1 to 547)
  AUTHORS   Colonna,M., Bresnahan,M., Bahram,S., Strominger,J.L. and Spies,T.
  TITLE     Allelic variants of the human putative peptide transporter involved
            in antigen processing
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3932-3936 (1992)
   PUBMED   1570316
REFERENCE   8  (residues 1 to 547)
  AUTHORS   Bodmer,J.G., Marsh,S.G., Albert,E.D., Bodmer,W.F., Dupont,B.,
            Erlich,H.A., Mach,B., Mayr,W.R., Parham,P., Sasazuki,T. et al.
  TITLE     Nomenclature for factors of the HLA system, 1991. WHO Nomenclature
            Committee for factors of the HLA system
  JOURNAL   Tissue Antigens 39 (4), 161-173 (1992)
   PUBMED   1529427
  REMARK    Erratum:[Tissue Antigens. 1992 Nov;40(5):229-43. doi:
            10.1111/j.1399-0039.1992.tb02050.x. PMID: 1362295]
REFERENCE   9  (residues 1 to 547)
  AUTHORS   Kelly,A., Powis,S.H., Kerr,L.A., Mockridge,I., Elliott,T.,
            Bastin,J., Uchanska-Ziegler,B., Ziegler,A., Trowsdale,J. and
            Townsend,A.
  TITLE     Assembly and function of the two ABC transporter proteins encoded
            in the human major histocompatibility complex
  JOURNAL   Nature 355 (6361), 641-644 (1992)
   PUBMED   1538751
REFERENCE   10 (residues 1 to 547)
  AUTHORS   Bahram,S., Arnold,D., Bresnahan,M., Strominger,J.L. and Spies,T.
  TITLE     Two putative subunits of a peptide pump encoded in the human major
            histocompatibility complex class II region
  JOURNAL   Proc Natl Acad Sci U S A 88 (22), 10094-10098 (1991)
   PUBMED   1946428
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC354917.1, AK302340.1 and
            BC014081.2.
            
            Summary: The membrane-associated protein encoded by this gene is a
            member of the superfamily of ATP-binding cassette (ABC)
            transporters. ABC proteins transport various molecules across
            extra- and intra-cellular membranes. ABC genes are divided into
            seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20,
            White). This protein is a member of the MDR/TAP subfamily. Members
            of the MDR/TAP subfamily are involved in multidrug resistance. The
            protein encoded by this gene is involved in the pumping of degraded
            cytosolic peptides across the endoplasmic reticulum into the
            membrane-bound compartment where class I molecules assemble.
            Mutations in this gene may be associated with ankylosing
            spondylitis, insulin-dependent diabetes mellitus, and celiac
            disease. Two transcript variants encoding different isoforms have
            been found for this gene. [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (2) is
            shorter at the N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302340.1, SRR14038193.1834091.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.32"
     Protein         1..547
                     /product="antigen peptide transporter 1 isoform 2"
                     /EC_number="7.4.2.14"
                     /note="antigen peptide transporter 1; transporter,
                     ATP-binding cassette, major histocompatibility complex, 1;
                     ABC transporter, MHC 1; peptide supply factor 1;
                     ATP-binding cassette, sub-family B (MDR/TAP), member 2;
                     transporter 1, ATP-binding cassette, sub-family B
                     (MDR/TAP); transporter associated with antigen processing;
                     peptide transporter PSF1; peptide transporter TAP1; really
                     interesting new gene 4 protein; ATP-binding cassette
                     sub-family B member 2; peptide transporter involved in
                     antigen processing 1; transporter 1 ATP-binding cassette
                     sub-family B"
                     /calculated_mol_wt=59869
     Region          <1..539
                     /region_name="3a01208"
                     /note="Conjugate Transporter-2 (CT2) Family protein;
                     TIGR00958"
                     /db_xref="CDD:273363"
     CDS             1..547
                     /gene="TAP1"
                     /gene_synonym="ABC17; ABCB2; APT1; D6S114E; MHC1D1; PSF-1;
                     PSF1; RING4; TAP1*0102N; TAP1N"
                     /coded_by="NM_001292022.2:173..1816"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:6890"
                     /db_xref="HGNC:HGNC:43"
                     /db_xref="MIM:170260"
ORIGIN      
        1 maipfftgrl tdwilqdgsa dtftrnltlm siltiasavl efvgdgiynn tmghvhshlq
       61 gevfgavlrq eteffqqnqt gnimsrvted tstlsdslse nlslflwylv rglcllgiml
      121 wgsvsltmvt litlpllfll pkkvgkwyql levqvresla kssqvaieal samptvrsfa
      181 neegeaqkfr eklqeiktln qkeavayavn swttsisgml lkvgilyigg qlvtsgavss
      241 gnlvtfvlyq mqftqavevl lsiyprvqka vgssekifey ldrtprcpps glltplhleg
      301 lvqfqdvsfa ypnrpdvlvl qgltftlrpg evtalvgpng sgkstvaall qnlyqptggq
      361 llldgkplpq yehrylhrqv aavgqepqvf grslqeniay gltqkptmee itaaavksga
      421 hsfisglpqg ydtevdeags qlsggqrqav alaralirkp cvlilddats aldansqlqv
      481 eqllyesper ysrsvllitq hlslveqadh ilfleggair eggthqqlme kkgcywamvq
      541 apadape
//
LOCUS       NP_001020092             192 aa            linear   PRI 21-NOV-2025
DEFINITION  large ribosomal subunit protein uL6 [Homo sapiens].
ACCESSION   NP_001020092 XP_005262718
VERSION     NP_001020092.1
DBSOURCE    REFSEQ: accession NM_001024921.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Li,A., Xie,J., Lv,L., Zheng,Z., Yang,W., Zhuo,W., Yang,S., Cai,D.,
            Duan,J., Liu,P., Min,J. and Wei,J.
  TITLE     RPL9 acts as an oncogene by shuttling miRNAs through exosomes in
            human hepatocellular carcinoma cells
  JOURNAL   Int J Oncol 64 (6) (2024)
   PUBMED   38639179
  REMARK    GeneRIF: RPL9 acts as an oncogene by shuttling miRNAs through
            exosomes in human hepatocellular carcinoma cells.
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Tsioras,K., Smith,K.C., Edassery,S.L., Garjani,M., Li,Y.,
            Williams,C., McKenna,E.D., Guo,W., Wilen,A.P., Hark,T.J.,
            Marklund,S.L., Ostrow,L.W., Gilthorpe,J.D., Ichida,J.K., Kalb,R.G.,
            Savas,J.N. and Kiskinis,E.
  TITLE     Analysis of proteome-wide degradation dynamics in ALS SOD1
            iPSC-derived patient neurons reveals disrupted VCP homeostasis
  JOURNAL   Cell Rep 42 (10), 113160 (2023)
   PUBMED   37776851
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Hassan,F.M., Alsultan,A., Alzehrani,F., Albuali,W., Bubshait,D.,
            Abass,E., Elbasheer,M. and Alkhanbashi,A.
  TITLE     Genetic Variants of RPL5 and RPL9 Genes among Saudi Patients
            Diagnosed with Thrombosis
  JOURNAL   Med Arch 75 (3), 188-193 (2021)
   PUBMED   34483448
  REMARK    GeneRIF: Genetic Variants of RPL5 and RPL9 Genes among Saudi
            Patients Diagnosed with Thrombosis.
REFERENCE   6  (residues 1 to 192)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   7  (residues 1 to 192)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   8  (residues 1 to 192)
  AUTHORS   Mazuruk,K., Schoen,T.J., Chader,G.J., Iwata,T. and Rodriguez,I.R.
  TITLE     Structural organization and chromosomal localization of the human
            ribosomal protein L9 gene
  JOURNAL   Biochim Biophys Acta 1305 (3), 151-162 (1996)
   PUBMED   8597601
REFERENCE   9  (residues 1 to 192)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 192)
  AUTHORS   Hori,N., Murakawa,K., Matoba,R., Fukushima,A., Okubo,K. and
            Matsubara,K.
  TITLE     A new human ribosomal protein sequence, homologue of rat L9
  JOURNAL   Nucleic Acids Res 21 (18), 4395 (1993)
   PUBMED   8415001
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL039355.2, AY376242.1 and
            BC031906.1.
            
            On Feb 3, 2016 this sequence version replaced XP_005262718.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L6P family of ribosomal proteins. It is located in the
            cytoplasm. As is typical for genes encoding ribosomal proteins,
            there are multiple processed pseudogenes of this gene dispersed
            through the genome. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (2) uses an alternative splice
            site in its 5' UTR, compared to variant 1. Variants 1 and 2 encode
            the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD050008.1, CD248858.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14"
     Protein         1..192
                     /product="large ribosomal subunit protein uL6"
                     /note="60S ribosomal protein L9"
                     /calculated_mol_wt=21732
     Region          1..191
                     /region_name="PTZ00027"
                     /note="60S ribosomal protein L6; Provisional"
                     /db_xref="CDD:240234"
     Site            121
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P32969.1)"
     CDS             1..192
                     /gene="RPL9"
                     /gene_synonym="L9; NPC-A-16; uL6"
                     /coded_by="NM_001024921.4:192..770"
                     /db_xref="CCDS:CCDS3452.1"
                     /db_xref="GeneID:6133"
                     /db_xref="HGNC:HGNC:10369"
                     /db_xref="MIM:603686"
ORIGIN      
        1 mktilsnqtv dipenvditl kgrtvivkgp rgtlrrdfnh invelsllgk kkkrlrvdkw
       61 wgnrkelatv rticshvqnm ikgvtlgfry kmrsvyahfp invviqengs lveirnflge
      121 kyirrvrmrp gvacsvsqaq kdelilegnd ielvsnsaal iqqattvknk dirkfldgiy
      181 vsekgtvqqa de
//
LOCUS       NP_001273561             983 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding protein 26 isoform 2 [Homo sapiens].
ACCESSION   NP_001273561 XP_005266557
VERSION     NP_001273561.1
DBSOURCE    REFSEQ: accession NM_001286632.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 983)
  AUTHORS   Gockert,M., Schmid,M., Jakobsen,L., Jens,M., Andersen,J.S. and
            Jensen,T.H.
  TITLE     Rapid factor depletion highlights intricacies of nucleoplasmic RNA
            degradation
  JOURNAL   Nucleic Acids Res 50 (3), 1583-1600 (2022)
   PUBMED   35048984
REFERENCE   2  (residues 1 to 983)
  AUTHORS   Silla,T., Schmid,M., Dou,Y., Garland,W., Milek,M., Imami,K.,
            Johnsen,D., Polak,P., Andersen,J.S., Selbach,M., Landthaler,M. and
            Jensen,T.H.
  TITLE     The human ZC3H3 and RBM26/27 proteins are critical for
            PAXT-mediated nuclear RNA decay
  JOURNAL   Nucleic Acids Res 48 (5), 2518-2530 (2020)
   PUBMED   31950173
  REMARK    GeneRIF: three additional proteins required for Poly(A) Tail
            eXosome Targeting (PAXT) function: ZC3H3, RBM26 and RBM27 along
            with the known PAXT-associated protein, PABPN1, were identified.
REFERENCE   3  (residues 1 to 983)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 983)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 983)
  AUTHORS   Dubinsky,M.C., Mei,L., Friedman,M., Dhere,T., Haritunians,T.,
            Hakonarson,H., Kim,C., Glessner,J., Targan,S.R., McGovern,D.P.,
            Taylor,K.D. and Rotter,J.I.
  TITLE     Genome wide association (GWA) predictors of anti-TNFalpha
            therapeutic responsiveness in pediatric inflammatory bowel disease
  JOURNAL   Inflamm Bowel Dis 16 (8), 1357-1366 (2010)
   PUBMED   20014019
REFERENCE   6  (residues 1 to 983)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   7  (residues 1 to 983)
  AUTHORS   Miele,A., Medina,R., van Wijnen,A.J., Stein,G.S. and Stein,J.L.
  TITLE     The interactome of the histone gene regulatory factor HiNF-P
            suggests novel cell cycle related roles in transcriptional control
            and RNA processing
  JOURNAL   J Cell Biochem 102 (1), 136-148 (2007)
   PUBMED   17577209
REFERENCE   8  (residues 1 to 983)
  AUTHORS   Kavanagh,S.J., Schulz,T.C., Davey,P., Claudianos,C., Russell,C. and
            Rathjen,P.D.
  TITLE     A family of RS domain proteins with novel subcellular localization
            and trafficking
  JOURNAL   Nucleic Acids Res 33 (4), 1309-1322 (2005)
   PUBMED   15741184
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL139006.13, CF994811.1, AK302871.1 and AL159974.21.
            
            On Nov 8, 2013 this sequence version replaced XP_005266557.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon and uses two alternate in-frame splice sites, compared to
            variant 1. The encoded isoform (2) is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302871.1, BC111697.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q31.1"
     Protein         1..983
                     /product="RNA-binding protein 26 isoform 2"
                     /note="acidic rich RS domain containing 2; RNA-binding
                     protein 26; cutaneous T-cell lymphoma tumor antigen
                     se70-2; CTCL tumor antigen se70-2; protein phosphatase 1,
                     regulatory 132"
                     /calculated_mol_wt=110894
     Region          11..76
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <294..314
                     /region_name="ZnF_C3H1"
                     /note="zinc finger; smart00356"
                     /db_xref="CDD:214632"
     Region          531..606
                     /region_name="RRM1_RBM26"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     RNA-binding protein 26 (RBM26); cd12516"
                     /db_xref="CDD:409938"
     Region          678..>770
                     /region_name="DR0291"
                     /note="Predicted nucleic acid-binding protein DR0291,
                     contains C4-type Zn-ribbon domain [General function
                     prediction only]; COG1579"
                     /db_xref="CDD:441187"
     Region          862..933
                     /region_name="RRM2_RBM26_like"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     RNA-binding protein 26 (RBM26) and similar proteins;
                     cd12258"
                     /db_xref="CDD:409703"
     CDS             1..983
                     /gene="RBM26"
                     /gene_synonym="ARRS2; C13orf10; PPP1R132; PRO1777; SE70-2;
                     ZC3H17"
                     /coded_by="NM_001286632.2:482..3433"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS66566.1"
                     /db_xref="GeneID:64062"
                     /db_xref="HGNC:HGNC:20327"
                     /db_xref="MIM:620081"
ORIGIN      
        1 mvskmiienf ealkswlskt lepicdadps alakyvlalv kkdksekelk alcidqldvf
       61 lqketqifve klfdavntks ylpppeqpss gslkveffph qekdikkeei tkeeerekkf
      121 srrlnhsppq sssryrenrs rderkkddrs rkrdydrnpp rrdsyrdryn rrrgrsrsys
      181 rsrsrswske rlrerdrdrs rtrsrsrtrs rerdlvkpky dldrtdplen nytpvssvps
      241 issghypvpt lsstitviap thhgnnttes wsefhedqvd hnsyvrppmp kkrcrdydek
      301 gfcmrgdmcp fdhgsdpvvv edvnlpgmlp fpaqppvveg ppppglpppp piltpppvnl
      361 rppvpppgpl ppslppvtgp ppplpplqps gmdappnsat ssvptvvttg ihhqpppapp
      421 slftadtydt dgynpeapsi tntsrpmyrh rvhaqrpnli gltsgdmdlp prekppnkss
      481 mrivvdsesr krtigsgepg vptkktwfdk pnfnrtnspg fqkkvqfgne ntklelrkvp
      541 pelnniskln ehfsrfgtlv nlqvayngdp egaliqfaty eeakkaisst eavlnnrfik
      601 vywhregstq qlqttspkvm qplvqqpilp vvkqsvkerl gpvpsstiep aeaqsassdl
      661 pqvlststgl tktvynpaal kaaqktllvs tsavdnneaq kkkqealklq qdvrkrkqei
      721 lekhietqkm liskleknkt mksedkaeim ktlevltkni tklkdevkaa spgrclpksi
      781 ktktqmqkel ldteldlykk mqageevtel rrkytelqle aakrgilssg rgrgihsrgr
      841 gavhgrgrgr grgrgvpgha vvdhrprale isaftesdre dllphfaqyg eiedcqidds
      901 slhavitfkt raeaeaaavh garfkgqdlk lawnkpvtni saveteevep deeefqeesl
      961 vddsllqddd eeeednesrs wrr
//
LOCUS       NP_001337358             938 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 1 isoform 25 [Homo
            sapiens].
ACCESSION   NP_001337358 XP_016866037
VERSION     NP_001337358.1
DBSOURCE    REFSEQ: accession NM_001350429.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 938)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 938)
  AUTHORS   Ruhle,F., Witten,A., Barysenka,A., Huge,A., Arning,A., Heller,C.,
            Krumpel,A., Mesters,R., Franke,A., Lieb,W., Riemenschneider,M.,
            Hiersche,M., Limperger,V., Nowak-Gottl,U. and Stoll,M.
  TITLE     Rare genetic variants in SMAP1, B3GAT2, and RIMS1 contribute to
            pediatric venous thromboembolism
  JOURNAL   Blood 129 (6), 783-790 (2017)
   PUBMED   28011674
  REMARK    GeneRIF: The study identified a region on chromosome 6 comprising
            the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus
            for pediatric venous thromboembolism.
REFERENCE   6  (residues 1 to 938)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 938)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
REFERENCE   8  (residues 1 to 938)
  AUTHORS   Schoch,S., Castillo,P.E., Jo,T., Mukherjee,K., Geppert,M., Wang,Y.,
            Schmitz,F., Malenka,R.C. and Sudhof,T.C.
  TITLE     RIM1alpha forms a protein scaffold for regulating neurotransmitter
            release at the active zone
  JOURNAL   Nature 415 (6869), 321-326 (2002)
   PUBMED   11797009
REFERENCE   9  (residues 1 to 938)
  AUTHORS   Coppola,T., Magnin-Luthi,S., Perret-Menoud,V., Gattesco,S.,
            Schiavo,G. and Regazzi,R.
  TITLE     Direct interaction of the Rab3 effector RIM with Ca2+ channels,
            SNAP-25, and synaptotagmin
  JOURNAL   J Biol Chem 276 (35), 32756-32762 (2001)
   PUBMED   11438518
REFERENCE   10 (residues 1 to 938)
  AUTHORS   Betz,A., Thakur,P., Junge,H.J., Ashery,U., Rhee,J.S., Scheuss,V.,
            Rosenmund,C., Rettig,J. and Brose,N.
  TITLE     Functional interaction of the active zone proteins Munc13-1 and
            RIM1 in synaptic vesicle priming
  JOURNAL   Neuron 30 (1), 183-196 (2001)
   PUBMED   11343654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590011.5, AL445256.18 and
            AL035633.18.
            
            On Apr 14, 2017 this sequence version replaced XP_016866037.1.
            
            Summary: The protein encoded by this gene is a RAS gene superfamily
            member that regulates synaptic vesicle exocytosis. This gene also
            plays a role in the regulation of voltage-gated calcium channels
            during neurotransmitter and insulin release. Mutations have
            suggested a role cognition and have been identified as the cause of
            cone-rod dystrophy type 7. Multiple transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Mar 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.220270.1,
                                           SRR1660805.228658.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..938
                     /product="regulating synaptic membrane exocytosis protein
                     1 isoform 25"
                     /note="RAB3-interacting protein 2; rab3-interacting
                     molecule 1; rab-3-interacting protein 2"
                     /calculated_mol_wt=104483
     Region          68..164
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(89..95,110,113,143,147,150..151)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          216..342
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(247,253,308,310,318)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          769..914
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(826,830..831,833,836,864,866,868,912..913)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..938
                     /gene="RIMS1"
                     /gene_synonym="CORD7; RAB3IP2; RIM; RIM1"
                     /coded_by="NM_001350429.2:231..3047"
                     /note="isoform 25 is encoded by transcript variant 25"
                     /db_xref="GeneID:22999"
                     /db_xref="HGNC:HGNC:17282"
                     /db_xref="MIM:606629"
ORIGIN      
        1 mcapgihvss egweevrsvd seegtiearr avagdldyyw ldpatwhsre tspisshpvt
       61 wqpskegdrl igrvilnkrt tmpkdsgall glkvvggkmt dlgrlgafit kvkkgsladv
      121 vghlragdev lewngkplpg atneevynii lesksepqve iivsrpigdi pripesshpp
      181 lesssssfes qkmerpsisv isptspgalk dapqvlpgql svklwydkvg hqlivnvlqa
      241 tdlparvdgr prnpyvkmyf lpdrsdkskr rtktvkkile pkwnqtfvys hvhrrdfrer
      301 mleitvwdqp rvqeeesefl geilieleta llddephwyk lqthdesslp lpqpspfmpr
      361 rhihgesssk klqrsqrisd sdisdyevdd gigvvppvgy rssareskst tltvpeqqrt
      421 thhrsrsvsp hrgndqgkpr srlpnvplqr sldeihptrr srsptrhhda srspvdhrtr
      481 dvdsqylseq drmhrqrspt qsppadtsfs srrgrqlpqv pvrsgsieqa slvveertrq
      541 mkmkvhrfkq ttgsgssqel dreqyskyni hkdqyrscdn vsakssdsdv sdvsaisrts
      601 sasrlsstsf mseqserprg rissftpkmq grrmgtsgrs imkstsvsge mytlehndgs
      661 qsdtavgtvg aggkkrrssl sakvvaivsr rsrstsqlsq tesghkklks tiqrstetgm
      721 aaemrkmvrq psrestdgsi nsyssegnli fpgvrlgads qfsdfldglg paqlvgrqtl
      781 atpamgdiqi gmedkkgqle vevirarslt qkpgskstpa pyvkvyllen gaciakkktr
      841 iarktldply qqslvfdesp qgkvlqvivw gdygrmdhkc fmgvaqille eldlssmvig
      901 wyklfppssl vdptltpltr rasqssless tgppcirs
//
LOCUS       NP_001374212            1679 aa            linear   PRI 21-NOV-2025
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily A member 4 isoform A [Homo sapiens].
ACCESSION   NP_001374212 XP_006722908
VERSION     NP_001374212.1
DBSOURCE    REFSEQ: accession NM_001387283.1
KEYWORDS    RefSeq; MANE Plus Clinical.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1679)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1679)
  AUTHORS   Schneppenheim,R., Fruhwald,M.C., Gesk,S., Hasselblatt,M.,
            Jeibmann,A., Kordes,U., Kreuz,M., Leuschner,I., Martin Subero,J.I.,
            Obser,T., Oyen,F., Vater,I. and Siebert,R.
  TITLE     Germline nonsense mutation and somatic inactivation of SMARCA4/BRG1
            in a family with rhabdoid tumor predisposition syndrome
  JOURNAL   Am J Hum Genet 86 (2), 279-284 (2010)
   PUBMED   20137775
  REMARK    GeneRIF: SMARCA4 is involved in cancer predisposition
REFERENCE   3  (residues 1 to 1679)
  AUTHORS   Wong,A.K., Shanahan,F., Chen,Y., Lian,L., Ha,P., Hendricks,K.,
            Ghaffari,S., Iliev,D., Penn,B., Woodland,A.M., Smith,R., Salada,G.,
            Carillo,A., Laity,K., Gupte,J., Swedlund,B., Tavtigian,S.V.,
            Teng,D.H. and Lees,E.
  TITLE     BRG1, a component of the SWI-SNF complex, is mutated in multiple
            human tumor cell lines
  JOURNAL   Cancer Res 60 (21), 6171-6177 (2000)
   PUBMED   11085541
REFERENCE   4  (residues 1 to 1679)
  AUTHORS   Muchardt,C., Reyes,J.C., Bourachot,B., Leguoy,E. and Yaniv,M.
  TITLE     The hbrm and BRG-1 proteins, components of the human SNF/SWI
            complex, are phosphorylated and excluded from the condensed
            chromosomes during mitosis
  JOURNAL   EMBO J 15 (13), 3394-3402 (1996)
   PUBMED   8670841
REFERENCE   5  (residues 1 to 1679)
  AUTHORS   Muchardt,C., Sardet,C., Bourachot,B., Onufryk,C. and Yaniv,M.
  TITLE     A human protein with homology to Saccharomyces cerevisiae SNF5
            interacts with the potential helicase hbrm
  JOURNAL   Nucleic Acids Res 23 (7), 1127-1132 (1995)
   PUBMED   7739891
REFERENCE   6  (residues 1 to 1679)
  AUTHORS   Chiba,H., Muramatsu,M., Nomoto,A. and Kato,H.
  TITLE     Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and
            Drosophila brahma are transcriptional coactivators cooperating with
            the estrogen receptor and the retinoic acid receptor
  JOURNAL   Nucleic Acids Res 22 (10), 1815-1820 (1994)
   PUBMED   8208605
REFERENCE   7  (residues 1 to 1679)
  AUTHORS   Khavari,P.A., Peterson,C.L., Tamkun,J.W., Mendel,D.B. and
            Crabtree,G.R.
  TITLE     BRG1 contains a conserved domain of the SWI2/SNF2 family necessary
            for normal mitotic growth and transcription
  JOURNAL   Nature 366 (6451), 170-174 (1993)
   PUBMED   8232556
REFERENCE   8  (residues 1 to 1679)
  AUTHORS   Nemes,K., Bens,S., Bourdeaut,F., Johann,P., Kordes,U., Siebert,R.
            and Fruhwald,M.C.
  TITLE     Rhabdoid Tumor Predisposition Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29215836
REFERENCE   9  (residues 1 to 1679)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
REFERENCE   10 (residues 1 to 1679)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011442.5, AC006127.1 and
            AC011485.6.
            
            On Sep 29, 2020 this sequence version replaced XP_006722908.1.
            
            Summary: The protein encoded by this gene is a member of the
            SWI/SNF family of proteins and is similar to the brahma protein of
            Drosophila. Members of this family have helicase and ATPase
            activities and are thought to regulate transcription of certain
            genes by altering the chromatin structure around those genes. The
            encoded protein is part of the large ATP-dependent chromatin
            remodeling complex SNF/SWI, which is required for transcriptional
            activation of genes normally repressed by chromatin. In addition,
            this protein can bind BRCA1, as well as regulate the expression of
            the tumorigenic protein CD44. Mutations in this gene cause rhabdoid
            tumor predisposition syndrome type 2. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, May 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1970526 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000646693.2/ ENSP00000495368.1
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1679
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..1679
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily A member
                     4 isoform A"
                     /note="sucrose nonfermenting-like 4; mitotic growth and
                     transcription activator; BRM/SWI2-related gene 1; homeotic
                     gene regulator; nuclear protein GRB1; brahma protein-like
                     1; SNF2-like 4; global transcription activator homologous
                     sequence; transcription activator BRG1; ATP-dependent
                     helicase SMARCA4; protein BRG-1; protein brahma homolog 1;
                     BRG1-associated factor 190A; SWI/SNF related, matrix
                     associated, actin dependent regulator of chromatin,
                     subfamily a, member 4"
                     /calculated_mol_wt=188018
     Region          1..282
                     /region_name="Necessary for interaction with SS18L1/CREST.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Region          1..177
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (P51532.2)"
     Region          42..>222
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          171..205
                     /region_name="QLQ"
                     /note="pfam08880"
                     /db_xref="CDD:462622"
     Site            188
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51532.2)"
     Region          198..352
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P51532.2)"
     Region          <364..>570
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          460..532
                     /region_name="HSA"
                     /note="domain in helicases and associated with SANT
                     domains; smart00573"
                     /db_xref="CDD:214727"
     Region          462..728
                     /region_name="RNA-binding region which is sufficient for
                     binding to lncRNA Evf2.
                     /evidence=ECO:0000250|UniProtKB:Q3TKT4"
                     /note="propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Region          577..610
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Site            609
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P51532.2)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P51532.2)"
     Region          612..656
                     /region_name="BRK"
                     /note="domain in transcription and CHROMO domain
                     helicases; smart00592"
                     /db_xref="CDD:197800"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51532.2)"
     Site            626
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6DIC0; propagated from
                     UniProtKB/Swiss-Prot (P51532.2)"
     Region          647..699
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51532.2)"
     Site            699
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Region          731..981
                     /region_name="DEXHc_SMARCA4"
                     /note="DEXH-box helicase domain of SMARCA4; cd18062"
                     /db_xref="CDD:350820"
     Region          750..>1232
                     /region_name="PLN03142"
                     /note="Probable chromatin-remodeling complex ATPase chain;
                     Provisional"
                     /db_xref="CDD:215601"
     Site            order(781..787,821,881..882)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350820"
     Region          837..916
                     /region_name="Sufficient for interaction with DLX1.
                     /evidence=ECO:0000250|UniProtKB:Q3TKT4"
                     /note="propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Region          881..884
                     /region_name="DEGH box"
                     /note="propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Region          1254..1299
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Region          1322..1389
                     /region_name="SnAC"
                     /note="Snf2-ATP coupling, chromatin remodelling complex;
                     pfam14619"
                     /db_xref="CDD:464219"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P51532.2)"
     Region          1432..1492
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Site            1455
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3TKT4; propagated from
                     UniProtKB/Swiss-Prot (P51532.2)"
     Site            1484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Region          1490..1596
                     /region_name="Bromo_SNF2L2"
                     /note="Bromodomain, SNF2L2-like subfamily, specific to
                     animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related
                     matrix-associated actin-dependent regulator of chromatin
                     subfamily A member 2 is a global transcriptional
                     activator, which cooperates with nuclear hormone...;
                     cd05516"
                     /db_xref="CDD:99947"
     Site            order(1521,1526,1529,1568,1572,1578)
                     /site_type="active"
                     /note="acetyllysine binding site [active]"
                     /db_xref="CDD:99947"
     Site            1571..1572
                     /site_type="other"
                     /note="Required for binding to 'Lys-15'-acetylated histone
                     3; propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Region          1596..1679
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Site            1602
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Site            1607
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Site            1618
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P51532.2)"
     Region          1628..1631
                     /region_name="KIKL. /evidence=ECO:0000269|PubMed:29567837"
                     /note="propagated from UniProtKB/Swiss-Prot (P51532.2)"
     Site            1659
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P51532.2)"
     Site            1663
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51532.2)"
     CDS             1..1679
                     /gene="SMARCA4"
                     /gene_synonym="BAF190; BAF190A; BRG1; CSS4; hSNF2b; MRD16;
                     OTSC12; RTPS2; SNF2; SNF2-beta; SNF2L4; SNF2LB; SWI2"
                     /coded_by="NM_001387283.1:174..5213"
                     /note="isoform A is encoded by transcript variant 10"
                     /db_xref="GeneID:6597"
                     /db_xref="HGNC:HGNC:11100"
                     /db_xref="MIM:603254"
ORIGIN      
        1 mstpdpplgg tprpgpspgp gpspgamlgp spgpspgsah smmgpspgpp saghpiptqg
       61 pggypqdnmh qmhkpmesmh ekgmsddpry nqmkgmgmrs gghagmgppp spmdqhsqgy
      121 psplggseha sspvpasgps sgpqmssgpg gapldgadpq algqqnrgpt pfnqnqlhql
      181 raqimaykml argqplpdhl qmavqgkrpm pgmqqqmptl pppsvsatgp gpgpgpgpgp
      241 gpgpappnys rphgmggpnm pppgpsgvpp gmpgqppggp pkpwpegpma naaaptstpq
      301 klippqptgr pspappavpp aaspvmppqt qspgqpaqpa pmvplhqkqs ritpiqkprg
      361 ldpveilqer eyrlqariah riqelenlpg slagdlrtka tielkalrll nfqrqlrqev
      421 vvcmrrdtal etalnakayk rskrqslrea riteklekqq kieqerkrrq khqeylnsil
      481 qhakdfkeyh rsvtgkiqkl tkavatyhan tereqkkene riekermrrl maedeegyrk
      541 lidqkkdkrl ayllqqtdey vanltelvrq hkaaqvakek kkkkkkkkae naegqtpaig
      601 pdgepldets qmsdlpvkvi hvesgkiltg tdapkagqle awlemnpgye vaprsdsees
      661 gseeeeeeee eeqpqaaqpp tlpveekkki pdpdsddvse vdarhiiena kqdvddeygv
      721 sqalarglqs yyavahavte rvdkqsalmv ngvlkqyqik glewlvslyn nnlngilade
      781 mglgktiqti alitylmehk ringpfliiv plstlsnway efdkwapsvv kvsykgspaa
      841 rrafvpqlrs gkfnvlltty eyiikdkhil akirwkymiv deghrmknhh ckltqvlnth
      901 yvaprrlllt gtplqnklpe lwallnfllp tifkscstfe qwfnapfamt gekvdlneee
      961 tiliirrlhk vlrpfllrrl kkeveaqlpe kveyvikcdm salqrvlyrh mqakgvlltd
     1021 gsekdkkgkg gtktlmntim qlrkicnhpy mfqhieesfs ehlgftggiv qgldlyrasg
     1081 kfelldrilp klratnhkvl lfcqmtslmt imedyfayrg fkylrldgtt kaedrgmllk
     1141 tfnepgseyf ifllstragg lglnlqsadt viifdsdwnp hqdlqaqdra hrigqqnevr
     1201 vlrlctvnsv eekilaaaky klnvdqkviq agmfdqksss herraflqai leheeqdesr
     1261 hcstgsgsas fahtapppag vnpdleeppl keedevpdde tvnqmiarhe eefdlfmrmd
     1321 ldrrreearn pkrkprlmee delpswiikd daeverltce eeeekmfgrg srhrkevdys
     1381 dsltekqwlk kitgkdihdt assvarglqf qrglqfctra skaieegtle eieeevrqkk
     1441 ssrkrkrdsd agsstpttst rsrdkddesk kqkkrgrppa eklspnppnl tkkmkkivda
     1501 vikykdsssg rqlsevfiql psrkelpeyy elirkpvdfk kikerirnhk yrslndlekd
     1561 vmllcqnaqt fnlegsliye dsivlqsvft svrqkieked dsegeeseee eegeeegses
     1621 esrsvkvkik lgrkekaqdr lkggrrrpsr gsrakpvvsd ddseeeqeed rsgsgseed
//
LOCUS       NP_001333243             550 aa            linear   PRI 21-NOV-2025
DEFINITION  autophagy-related protein 13 isoform a [Homo sapiens].
ACCESSION   NP_001333243 XP_006718457
VERSION     NP_001333243.1
DBSOURCE    REFSEQ: accession NM_001346314.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Patel,A. and Faesen,A.C.
  TITLE     Metamorphosis by ATG13 and ATG101 in human autophagy initiation
  JOURNAL   Autophagy 20 (4), 968-969 (2024)
   PUBMED   37394799
  REMARK    GeneRIF: Metamorphosis by ATG13 and ATG101 in human autophagy
            initiation.
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Nguyen,A. and Faesen,A.C.
  TITLE     The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis
  JOURNAL   FEBS Lett 598 (1), 114-126 (2024)
   PUBMED   37567770
  REMARK    GeneRIF: The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis.
            Review article
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Karabi,Z., Moradian,F. and Kheirabadi,M.
  TITLE     The effect of lactoferrin on ULK1 and ATG13 genes expression in
            breast cancer cell line MCF7 and bioinformatics studies of protein
            interaction between lactoferrin and the autophagy initiation
            complex
  JOURNAL   Cell Biochem Biophys 80 (4), 795-806 (2022)
   PUBMED   36169801
  REMARK    GeneRIF: The effect of lactoferrin on ULK1 and ATG13 genes
            expression in breast cancer cell line MCF7 and bioinformatics
            studies of protein interaction between lactoferrin and the
            autophagy initiation complex.
REFERENCE   5  (residues 1 to 550)
  AUTHORS   Gottschalk,G., Peterson,D., Knox,K., Maynard,M., Whelan,R.J. and
            Roy,A.
  TITLE     Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE)
  JOURNAL   Mol Cell Neurosci 120, 103731 (2022)
   PUBMED   35487443
  REMARK    GeneRIF: Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE).
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Jung,C.H., Jun,C.B., Ro,S.H., Kim,Y.M., Otto,N.M., Cao,J., Kundu,M.
            and Kim,D.H.
  TITLE     ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy
            machinery
  JOURNAL   Mol Biol Cell 20 (7), 1992-2003 (2009)
   PUBMED   19225151
  REMARK    GeneRIF: The ULK-Atg13-FIP200 complexes are direct targets of mTOR
            and important regulators of autophagy in response to mTOR
            signaling.
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Hosokawa,N., Hara,T., Kaizuka,T., Kishi,C., Takamura,A., Miura,Y.,
            Iemura,S., Natsume,T., Takehana,K., Yamada,N., Guan,J.L., Oshiro,N.
            and Mizushima,N.
  TITLE     Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200
            complex required for autophagy
  JOURNAL   Mol Biol Cell 20 (7), 1981-1991 (2009)
   PUBMED   19211835
  REMARK    GeneRIF: mTORC1 suppresses autophagy through direct regulation of
            the approximately 3-MDa ULK1-Atg13-FIP200 complex.
REFERENCE   8  (residues 1 to 550)
  AUTHORS   Chan,E.Y., Longatti,A., McKnight,N.C. and Tooze,S.A.
  TITLE     Kinase-inactivated ULK proteins inhibit autophagy via their
            conserved C-terminal domains using an Atg13-independent mechanism
  JOURNAL   Mol Cell Biol 29 (1), 157-171 (2009)
   PUBMED   18936157
  REMARK    GeneRIF: The functions of ULK1 and ULK2 are controlled by
            autophosphorylation and conformational changes involving exposure
            of the C-terminal domain and interaction with the putative human
            homologue of Atg13.
            GeneRIF: The gene product is the functional homologue of yeast
            Atg13, and required for autophagy in mammalian cells.
REFERENCE   9  (residues 1 to 550)
  AUTHORS   Meijer,W.H., van der Klei,I.J., Veenhuis,M. and Kiel,J.A.
  TITLE     ATG genes involved in non-selective autophagy are conserved from
            yeast to man, but the selective Cvt and pexophagy pathways also
            require organism-specific genes
  JOURNAL   Autophagy 3 (2), 106-116 (2007)
   PUBMED   17204848
REFERENCE   10 (residues 1 to 550)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC127035.6 and AC115088.6.
            
            On Oct 9, 2016 this sequence version replaced XP_006718457.1.
            
            Summary: The protein encoded by this gene is an autophagy factor
            and a target of the TOR kinase signaling pathway. The encoded
            protein is essential for autophagosome formation and mitophagy.
            [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (10), as well as variants 3, 7-9,
            and 11-12, encodes isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.856495.1,
                                           SRR1803616.175392.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..550
                     /product="autophagy-related protein 13 isoform a"
                     /note="autophagy-related protein 13; ATG13 autophagy
                     related 13 homolog"
                     /calculated_mol_wt=60024
     Region          19..192
                     /region_name="ATG13"
                     /note="Autophagy-related protein 13; pfam10033"
                     /db_xref="CDD:431003"
     CDS             1..550
                     /gene="ATG13"
                     /gene_synonym="KIAA0652; PARATARG8"
                     /coded_by="NM_001346314.2:524..2176"
                     /note="isoform a is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS55760.1"
                     /db_xref="GeneID:9776"
                     /db_xref="HGNC:HGNC:29091"
                     /db_xref="MIM:615088"
ORIGIN      
        1 metdlnsqdr kdldkfikff alktvqvivq arlgekictr ssssptgsdw fnlaikdipe
       61 vtheakkala gqlpavgrsm cveislktse gdsmeleiwc lemnekcdke ikvsytvynr
      121 lslllkslla itrvtpayrl srkqgheyvi lyriyfgevq lsglgegfqt vrvgtvgtpv
      181 gtitlscayr inlafmstrq fertppimgi iidhfvdrpy pssspmhpcn yrtagedtgv
      241 iypsvedsqe vcttsfstsp psqcvftvtk ahfqtptpvv tdtlrvpmag lafshqlsss
      301 rlsyqpaalg vgsadlaypv vfaaglnath phqlmvpgke ggvplapnqp vhgtqadqer
      361 latctpsdrt hcaatpssse dtetvsnsse grasphdvle tifvrkvgaf vnkpinqvtl
      421 tsldipfamf apknleledt dpmvnppdsp etesplqgsl hsdgssggss gnthddfvmi
      481 dfkpafskdd ilpmdlgtfy refqnppqls slsidigaqs maedldslpe klavheknvr
      541 efdafvetlq
//
LOCUS       NP_001361612            1111 aa            linear   PRI 21-NOV-2025
DEFINITION  trafficking protein particle complex subunit 9 isoform e [Homo
            sapiens].
ACCESSION   NP_001361612
VERSION     NP_001361612.1
DBSOURCE    REFSEQ: accession NM_001374683.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1111)
  AUTHORS   Kharrat,M., Triki,C., Ben Isaa,A., Bouchaala,W., Alila,O.,
            Chouchen,J., Ghouliya,Y., Kamoun,F., Tlili,A. and Fakhfakh,F.
  TITLE     Expanding the genetic and phenotypic spectrum of TRAPPC9 and
            MID2-related neurodevelopmental disabilities: report of two novel
            mutations, 3D-modelling, and molecular docking studies
  JOURNAL   J Hum Genet 69 (7), 291-299 (2024)
   PUBMED   38467738
  REMARK    GeneRIF: Expanding the genetic and phenotypic spectrum of TRAPPC9
            and MID2-related neurodevelopmental disabilities: report of two
            novel mutations, 3D-modelling, and molecular docking studies.
REFERENCE   2  (residues 1 to 1111)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1111)
  AUTHORS   Lorente-Pozo,S., Boronat,N., Parra-Llorca,A., Lara-Canton,I.,
            Solaz-Garcia,A., Oltra Soler,J.V., Buso,E.J., Casabo-Valles,G.,
            Garcia-Gimenez,J.L., Pallardo,F.V. and Vento,M.
  TITLE     Neurodevelopmental Outcome and Epigenetic Changes at 2 Years
            Associated with the Oxygen Load Received upon Postnatal
            Stabilization: A Pilot Study
  JOURNAL   Neonatology 119 (5), 575-584 (2022)
   PUBMED   35760056
  REMARK    GeneRIF: Neurodevelopmental Outcome and Epigenetic Changes at 2
            Years Associated with the Oxygen Load Received upon Postnatal
            Stabilization: A Pilot Study.
REFERENCE   4  (residues 1 to 1111)
  AUTHORS   Ben Ayed,I., Bouchaala,W., Bouzid,A., Feki,W., Souissi,A., Ben
            Nsir,S., Ben Said,M., Sammouda,T., Majdoub,F., Kharrat,I.,
            Kamoun,F., Elloumi,I., Kamoun,H., Tlili,A., Masmoudi,S. and
            Triki,C.
  TITLE     Further insights into the spectrum phenotype of TRAPPC9 and
            CDK5RAP2 genes, segregating independently in a large Tunisian
            family with intellectual disability and microcephaly
  JOURNAL   Eur J Med Genet 64 (12), 104373 (2021)
   PUBMED   34737153
  REMARK    GeneRIF: Further insights into the spectrum phenotype of TRAPPC9
            and CDK5RAP2 genes, segregating independently in a large Tunisian
            family with intellectual disability and microcephaly.
REFERENCE   5  (residues 1 to 1111)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1111)
  AUTHORS   Kent,J.W. Jr., Peterson,C.P., Dyer,T.D., Almasy,L. and Blangero,J.
  TITLE     Genome-wide discovery of maternal effect variants
  JOURNAL   BMC Proc 3 Suppl 7 (Suppl 7), S19 (2009)
   PUBMED   20018008
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1111)
  AUTHORS   Mir,A., Kaufman,L., Noor,A., Motazacker,M.M., Jamil,T., Azam,M.,
            Kahrizi,K., Rafiq,M.A., Weksberg,R., Nasr,T., Naeem,F.,
            Tzschach,A., Kuss,A.W., Ishak,G.E., Doherty,D., Ropers,H.H.,
            Barkovich,A.J., Najmabadi,H., Ayub,M. and Vincent,J.B.
  TITLE     Identification of mutations in TRAPPC9, which encodes the NIK- and
            IKK-beta-binding protein, in nonsyndromic autosomal-recessive
            mental retardation
  JOURNAL   Am J Hum Genet 85 (6), 909-915 (2009)
   PUBMED   20004765
  REMARK    GeneRIF: TRAPPC9, encodes the NIK- and IKK-beta-binding protein,
            has a role in nonsyndromic autosomal-recessive mental retardation
REFERENCE   8  (residues 1 to 1111)
  AUTHORS   Philippe,O., Rio,M., Carioux,A., Plaza,J.M., Guigue,P.,
            Molinari,F., Boddaert,N., Bole-Feysot,C., Nitschke,P., Smahi,A.,
            Munnich,A. and Colleaux,L.
  TITLE     Combination of linkage mapping and microarray-expression analysis
            identifies NF-kappaB signaling defect as a cause of
            autosomal-recessive mental retardation
  JOURNAL   Am J Hum Genet 85 (6), 903-908 (2009)
   PUBMED   20004764
REFERENCE   9  (residues 1 to 1111)
  AUTHORS   Mochida,G.H., Mahajnah,M., Hill,A.D., Basel-Vanagaite,L.,
            Gleason,D., Hill,R.S., Bodell,A., Crosier,M., Straussberg,R. and
            Walsh,C.A.
  TITLE     A truncating mutation of TRAPPC9 is associated with
            autosomal-recessive intellectual disability and postnatal
            microcephaly
  JOURNAL   Am J Hum Genet 85 (6), 897-902 (2009)
   PUBMED   20004763
  REMARK    GeneRIF: TRAPPC9 has a role in brain development, possibly through
            its effect on NF-kappaB activation and protein trafficking in the
            postmitotic neurons of the cerebral cortex
REFERENCE   10 (residues 1 to 1111)
  AUTHORS   Hu,W.H., Pendergast,J.S., Mo,X.M., Brambilla,R., Bracchi-Ricard,V.,
            Li,F., Walters,W.M., Blits,B., He,L., Schaal,S.M. and Bethea,J.R.
  TITLE     NIBP, a novel NIK and IKK(beta)-binding protein that enhances
            NF-(kappa)B activation
  JOURNAL   J Biol Chem 280 (32), 29233-29241 (2005)
   PUBMED   15951441
  REMARK    GeneRIF: NIBP is a NIK and IKK(beta)-binding protein that enhances
            NF-(kappa)B activation
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091022.4, AC104244.9,
            AC040978.8, AC021744.14 and AC007869.2.
            
            Summary: This gene encodes a protein that likely plays a role in
            NF-kappa-B signaling. Mutations in this gene have been associated
            with autosomal-recessive cognitive disability. Alternatively
            spliced transcript variants have been described.[provided by
            RefSeq, Feb 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2324800.1,
                                           SRR14038194.1185141.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1111
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..1111
                     /product="trafficking protein particle complex subunit 9
                     isoform e"
                     /note="IKK2 binding protein; TRAPP 120 kDa subunit; NIK-
                     and IKBKB-binding protein; NIK and IKK-beta binding
                     protein; tularik gene 1 protein; trafficking protein
                     particle complex 9"
                     /calculated_mol_wt=124291
     Region          14..1063
                     /region_name="TRAPPC9-Trs120"
                     /note="Transport protein Trs120 or TRAPPC9, TRAPP II
                     complex subunit; pfam08626"
                     /db_xref="CDD:430114"
     CDS             1..1111
                     /gene="TRAPPC9"
                     /gene_synonym="IBP; IKBKBBP; MRT13; NIBP; T1; TRS120"
                     /coded_by="NM_001374683.1:117..3452"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="GeneID:83696"
                     /db_xref="HGNC:HGNC:30832"
                     /db_xref="MIM:611966"
ORIGIN      
        1 msvpdymqca edhqtllvvv qpvgivseen ffriykrics vsqisvrdsq rvlyiryrhh
       61 yppennewgd fqthrkvvgl ititdcfsak dwpqtfekfh vqkeiygstl ydsrlfvfgl
      121 qgeiveqprt dvafypnyed cqtvekried fieslfivle skrldratdk sgdkipllcv
      181 pfekkdfvgl dtdsrhykkr cqgrmrkhvg dlclqagmlq dslvhyhmsv ellrsvndfl
      241 wlgaaleglc sasviyhypg gtggksgarr fqgstlpaea anrhrpgaqe vlidpgaltt
      301 nginpdtste igraknclsp ediidkykea isyyskykna gvieleacik avrvlaiqkr
      361 smeaseflqn avyinlrqls eeekiqrysi lselyeligf hrksaffkrv aamqcvapsi
      421 aepgwracyk llletlpgys lsldpkdfsr gthrgwaavq mrllhelvya srrmgnpals
      481 vrhlsfllqt mldflsdqek kdvaqsleny tskcpgtmep ialpggltlp pvpftklpiv
      541 rhvkllnlpa slrphkmksl lgqnvstksp fiyspiiahn rgeernkkid fqwvqgdvce
      601 vqlmvynpmp felrvenmgl ltsgvefesl paalslpaes glypvtlvgv pqttgtitvn
      661 gyhttvfgvf sdclldnlpg iktsgstvev ipalprlqis tslprsahsl qpssgdeist
      721 nvsvqlynge sqqliiklen igmeplekle vtskvlttke klygdflswk leetlaqfpl
      781 qpgkvatfti nikvkldfsc qenllqdlsd dgisvsgfpl sspfrqvvrp rvegkpvnpp
      841 esnkagdysh vktleavlnf kysggpghte gyyrnlslgl hvevepsvff trvstlpatr
      901 maiqvdkfnf esfpespgek gqfanpkqle eerreargle ihsklgicwr ipslkrsgea
      961 svegllnqlv lehlqlaplq wdvlvdgqpc dreavaacqv gdpvrlevrl tnrsprsvgp
     1021 faltvvpfqd hqngvhnydl hdtvsfvgss tfyldavqps gqsaclgall flytgdfflh
     1081 irfhedstsk elppswfclp svhvcaleaq a
//
LOCUS       NP_001158219             419 aa            linear   PRI 21-NOV-2025
DEFINITION  ras association domain-containing protein 8 isoform a [Homo
            sapiens].
ACCESSION   NP_001158219
VERSION     NP_001158219.1
DBSOURCE    REFSEQ: accession NM_001164747.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Lin,Y., Guo,R., R,G. and Xu,B.
  TITLE     Tailored modulation of S100A1 and RASSF8 expression by
            butanediamide augments healing of rotator cuff tears
  JOURNAL   PeerJ 11, e15791 (2023)
   PUBMED   37601265
  REMARK    GeneRIF: Tailored modulation of S100A1 and RASSF8 expression by
            butanediamide augments healing of rotator cuff tears.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Li,X., Jiang,X., Lu,J., Lin,Y., Jiang,L., Li,Y., Wan,F. and Wang,C.
  TITLE     CircCERS6 Suppresses the Development of Epithelial Ovarian Cancer
            Through Mediating miR-630/RASSF8
  JOURNAL   Biochem Genet 60 (6), 2611-2629 (2022)
   PUBMED   35676548
  REMARK    GeneRIF: CircCERS6 Suppresses the Development of Epithelial Ovarian
            Cancer Through Mediating miR-630/RASSF8.
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Zhang,X., Sun,P., Yang,W., Li,S., Jia,H., Wang,W., Jiang,S.,
            Wang,L., Liu,X., Liang,L. and Zi,W.
  TITLE     RASSF8-AS1 displays low expression in colorectal cancer and
            up-regulates RASSF8 to suppress cell invasion and migration
  JOURNAL   Pathol Res Pract 237, 153996 (2022)
   PUBMED   35839610
  REMARK    GeneRIF: RASSF8-AS1 displays low expression in colorectal cancer
            and up-regulates RASSF8 to suppress cell invasion and migration.
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Falvella,F.S., Manenti,G., Spinola,M., Pignatiello,C., Conti,B.,
            Pastorino,U. and Dragani,T.A.
  TITLE     Identification of RASSF8 as a candidate lung tumor suppressor gene
  JOURNAL   Oncogene 25 (28), 3934-3938 (2006)
   PUBMED   16462760
  REMARK    GeneRIF: Expression of RASSF8 protein by transfected lung cancer
            cells led to inhibition of anchorage-independent growth in soft
            agar in A549 cells and reduction of clonogenic activity in NCI-H520
            cells
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   8  (residues 1 to 419)
  AUTHORS   Debeer,P., Schoenmakers,E.F., Twal,W.O., Argraves,W.S., De Smet,L.,
            Fryns,J.P. and Van De Ven,W.J.
  TITLE     The fibulin-1 gene (FBLN1) is disrupted in a t(12;22) associated
            with a complex type of synpolydactyly
  JOURNAL   J Med Genet 39 (2), 98-104 (2002)
   PUBMED   11836357
REFERENCE   9  (residues 1 to 419)
  AUTHORS   Gonzalez,P., Epstein,D.L. and Borras,T.
  TITLE     Characterization of gene expression in human trabecular meshwork
            using single-pass sequencing of 1060 clones
  JOURNAL   Invest Ophthalmol Vis Sci 41 (12), 3678-3693 (2000)
   PUBMED   11053263
REFERENCE   10 (residues 1 to 419)
  AUTHORS   Debeer,P., Schoenmakers,E.F., Thoelen,R., Holvoet,M., Kuittinen,T.,
            Fabry,G., Fryns,J.P., Goodman,F.R. and Van de Ven,W.J.
  TITLE     Physical map of a 1.5 mb region on 12p11.2 harbouring a
            synpolydactyly associated chromosomal breakpoint
  JOURNAL   Eur J Hum Genet 8 (8), 561-570 (2000)
   PUBMED   10951517
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290055.1, AY665468.1,
            AC055707.33 and BE440096.1.
            
            Summary: This gene encodes a member of the Ras-assocation domain
            family (RASSF) of tumor suppressor proteins. This gene is essential
            for maintaining adherens junction function in epithelial cells and
            has a role in epithelial cell migration. It is a lung tumor
            suppressor gene candidate. A chromosomal translocation
            t(12;22)(p11.2;q13.3) leading to the fusion of this gene and the
            FBLN1 gene is found in a complex type of synpolydactyly. Multiple
            alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, May
            2011].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290055.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465420 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..419
                     /product="ras association domain-containing protein 8
                     isoform a"
                     /note="ras association domain-containing protein 8; Ras
                     association (RalGDS/AF-6) domain family (N-terminal)
                     member 8; carcinoma-associated protein HOJ-1"
                     /calculated_mol_wt=48196
     Region          2..83
                     /region_name="RA_RASSF8"
                     /note="Ras-associating (RA) domain found in N-terminal
                     Ras-association domain family 8 (RASSF8); cd16134"
                     /db_xref="CDD:340551"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8NHQ8.2)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NHQ8.2)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NHQ8.2)"
     Region          <164..>384
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NHQ8.2)"
     CDS             1..419
                     /gene="RASSF8"
                     /gene_synonym="C12orf2; HOJ1"
                     /coded_by="NM_001164747.2:293..1552"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS53765.1"
                     /db_xref="GeneID:11228"
                     /db_xref="HGNC:HGNC:13232"
                     /db_xref="MIM:608231"
ORIGIN      
        1 melkvwvdgv qrivcgvtev ttcqevvial aqaigrtgry tliekwrdte rhlaphenpi
       61 islnkwgqya sdvqlilrrt gpslserpts dsvaripert lyrqslppla klrpqidksi
      121 krrepkrksl tftggakglm difgkgkete fkqkvlnnck ttadelkkli rlqteklqsi
      181 ekqlesneie irfweqkyns nleeeivrle qkikrndvei eeeefwenel qieqenekql
      241 kdqlqeirqk itecenklkd ylaqirtmes gleaeklqre vqeaqvneee vkgkigkvkg
      301 eidiqgqqsl rlengikave rslgqatkrl qdkeqeleql tkelrqvnlq qfiqqtgtkv
      361 tvlpaepiei eashadiere apfqsgslkr pgssrqlpsn lrilqnpiss gfnpegiyv
//
LOCUS       NP_001186270             184 aa            linear   PRI 21-NOV-2025
DEFINITION  large ribosomal subunit protein uL22 isoform a [Homo sapiens].
ACCESSION   NP_001186270 NP_001356488
VERSION     NP_001186270.1
DBSOURCE    REFSEQ: accession NM_001199341.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Fellmann,F., Saunders,C., O'Donohue,M.F., Reid,D.W., McFadden,K.A.,
            Montel-Lehry,N., Yu,C., Fang,M., Zhang,J., Royer-Bertrand,B.,
            Farinelli,P., Karboul,N., Willer,J.R., Fievet,L., Bhuiyan,Z.A.,
            Kleinhenz,A.L., Jadeau,J., Fulbright,J., Rivolta,C., Renella,R.,
            Katsanis,N., Beckmann,J.S., Nicchitta,C.V., Da Costa,L., Davis,E.E.
            and Gleizes,P.E.
  TITLE     An atypical form of 60S ribosomal subunit in Diamond-Blackfan
            anemia linked to RPL17 variants
  JOURNAL   JCI Insight 9 (17), e172475 (2024)
   PUBMED   39088281
  REMARK    GeneRIF: An atypical form of 60S ribosomal subunit in
            Diamond-Blackfan anemia linked to RPL17 variants.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Hori,H., Nakamura,S., Yoshida,F., Teraishi,T., Sasayama,D., Ota,M.,
            Hattori,K., Kim,Y., Higuchi,T. and Kunugi,H.
  TITLE     Integrated profiling of phenotype and blood transcriptome for
            stress vulnerability and depression
  JOURNAL   J Psychiatr Res 104, 202-210 (2018)
   PUBMED   30103068
  REMARK    GeneRIF: The present study combines an individual-based phenotypic
            profiling with a transdiagnostic approach and shows that several
            ribosomal genes including RPL17 is involved in stress vulnerability
            across nonclinical and clinical conditions.
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   7  (residues 1 to 184)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   8  (residues 1 to 184)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 184)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 184)
  AUTHORS   Mager,D.L. and Freeman,J.D.
  TITLE     A human gene related to the ribosomal protein L23 gene of
            Halobacterium marismortui
  JOURNAL   Nucleic Acids Res 18 (17), 5301 (1990)
   PUBMED   2402465
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC100778.5.
            
            On May 20, 2019 this sequence version replaced NP_001356488.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L22P family of ribosomal proteins. It is located in the
            cytoplasm. This gene has been referred to as rpL23 because the
            encoded protein shares amino acid identity with ribosomal protein
            L23 from Halobacterium marismortui; however, its official symbol is
            RPL17. As is typical for genes encoding ribosomal proteins, there
            are multiple processed pseudogenes of this gene dispersed through
            the genome. Alternative splicing results in multiple transcript
            variants. Read-through transcription also exists between this gene
            and the neighboring downstream C18orf32 (chromosome 18 open reading
            frame 32) gene. [provided by RefSeq, Dec 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BF026501.1, CD385689.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..184
                     /product="large ribosomal subunit protein uL22 isoform a"
                     /note="60S ribosomal protein L17; large ribosomal subunit
                     protein uL22; gene encoding putative NFkB activating
                     protein; 60S ribosomal protein L23"
                     /calculated_mol_wt=21266
     Region          1..165
                     /region_name="PTZ00178"
                     /note="60S ribosomal protein L17; Provisional"
                     /db_xref="CDD:240306"
     Site            order(15..16,38..40,42..43,45..46,99..104,112..117,
                     149..150)
                     /site_type="active"
                     /note="putative translocon binding site [active]"
                     /db_xref="CDD:238205"
     Site            order(18,20,23,25..27,30,34,37,97,101,104,116,118..120,
                     122,125,137..142)
                     /site_type="other"
                     /note="protein-rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238205"
     Region          160..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18621.3)"
     CDS             1..184
                     /gene="RPL17"
                     /gene_synonym="DBA22; L17; PD-1; RPL23; uL22"
                     /coded_by="NM_001199341.3:222..776"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS45865.1"
                     /db_xref="GeneID:6139"
                     /db_xref="HGNC:HGNC:10307"
                     /db_xref="MIM:603661"
ORIGIN      
        1 mvrysldpen ptkscksrgs nlrvhfkntr etaqaikgmh irkatkylkd vtlqkqcvpf
       61 rrynggvgrc aqakqwgwtq grwpkksaef llhmlknaes naelkgldvd slviehiqvn
      121 kapkmrrrty rahgrinpym sspchiemil tekeqivpkp eeevaqkkki sqkklkkqkl
      181 mare
//
LOCUS       NP_001317700             819 aa            linear   PRI 21-NOV-2025
DEFINITION  connector enhancer of kinase suppressor of ras 2 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001317700
VERSION     NP_001317700.1
DBSOURCE    REFSEQ: accession NM_001330771.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Ito,H. and Nagata,K.I.
  TITLE     Functions of CNKSR2 and Its Association with Neurodevelopmental
            Disorders
  JOURNAL   Cells 11 (2), 303 (2022)
   PUBMED   35053419
  REMARK    GeneRIF: Functions of CNKSR2 and Its Association with
            Neurodevelopmental Disorders.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Toraman,B., Bilginer,S.C., Hesapcioglu,S.T., Goker,Z., Soykam,H.O.,
            Erguner,B., Dincer,T., Yildiz,G., Unsal,S., Kasap,B.K., Kandil,S.
            and Kalay,E.
  TITLE     Finding underlying genetic mechanisms of two patients with autism
            spectrum disorder carrying familial apparently balanced chromosomal
            translocations
  JOURNAL   J Gene Med 23 (4), e3322 (2021)
   PUBMED   33591602
  REMARK    GeneRIF: Finding underlying genetic mechanisms of two patients with
            autism spectrum disorder carrying familial apparently balanced
            chromosomal translocations.
REFERENCE   4  (residues 1 to 819)
  AUTHORS   Zhang,Y., Yu,T., Li,N., Wang,J., Wang,J., Ge,Y. and Yao,R.
  TITLE     Psychomotor development and attention problems caused by a splicing
            variant of CNKSR2
  JOURNAL   BMC Med Genomics 13 (1), 182 (2020)
   PUBMED   33298018
  REMARK    GeneRIF: Psychomotor development and attention problems caused by a
            splicing variant of CNKSR2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 819)
  AUTHORS   Daoqi,M., Guohong,C., Yuan,W., Zhixiao,Y., Kaili,X. and Shiyue,M.
  TITLE     Exons deletion of CNKSR2 gene identified in X-linked syndromic
            intellectual disability
  JOURNAL   BMC Med Genet 21 (1), 69 (2020)
   PUBMED   32245427
  REMARK    GeneRIF: This study enhances our knowledge of the CNKSR2 gene
            mutation spectrum and provides further information about the
            phenotypic characteristics of X-linked syndromic intellectual
            disability.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 819)
  AUTHORS   Wang,X., Patel,R. and Studzinski,G.P.
  TITLE     hKSR-2, a vitamin D-regulated gene, inhibits apoptosis in
            arabinocytosine-treated HL60 leukemia cells
  JOURNAL   Mol Cancer Ther 7 (9), 2798-2806 (2008)
   PUBMED   18790760
REFERENCE   7  (residues 1 to 819)
  AUTHORS   Rajakulendran,T., Sahmi,M., Kurinov,I., Tyers,M., Therrien,M. and
            Sicheri,F.
  TITLE     CNK and HYP form a discrete dimer by their SAM domains to mediate
            RAF kinase signaling
  JOURNAL   Proc Natl Acad Sci U S A 105 (8), 2836-2841 (2008)
   PUBMED   18287031
  REMARK    GeneRIF: CNK and HYP form a discrete dimer by their SAM domains to
            mediate RAF kinase signaling.
REFERENCE   8  (residues 1 to 819)
  AUTHORS   Bumeister,R., Rosse,C., Anselmo,A., Camonis,J. and White,M.A.
  TITLE     CNK2 couples NGF signal propagation to multiple regulatory cascades
            driving cell differentiation
  JOURNAL   Curr Biol 14 (5), 439-445 (2004)
   PUBMED   15028221
REFERENCE   9  (residues 1 to 819)
  AUTHORS   Lanigan,T.M., Liu,A., Huang,Y.Z., Mei,L., Margolis,B. and Guan,K.L.
  TITLE     Human homologue of Drosophila CNK interacts with Ras effector
            proteins Raf and Rlf
  JOURNAL   FASEB J 17 (14), 2048-2060 (2003)
   PUBMED   14597674
  REMARK    GeneRIF: CNK2 through interaction with Raf and Rlf may function as
            a regulator of Ras signaling.
REFERENCE   10 (residues 1 to 819)
  AUTHORS   Ohtakara,K., Nishizawa,M., Izawa,I., Hata,Y., Matsushima,S.,
            Taki,W., Inada,H., Takai,Y. and Inagaki,M.
  TITLE     Densin-180, a synaptic protein, links to PSD-95 through its direct
            interaction with MAGUIN-1
  JOURNAL   Genes Cells 7 (11), 1149-1160 (2002)
   PUBMED   12390249
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL807781.6, AL928874.3 and
            AL772392.4.
            
            Summary: This gene encodes a multidomain protein that functions as
            a scaffold protein to mediate the mitogen-activated protein kinase
            pathways downstream from Ras. This gene product is induced by
            vitamin D and inhibits apoptosis in certain cancer cells. It may
            also play a role in ternary complex assembly of synaptic proteins
            at the postsynaptic membrane and coupling of signal transduction to
            membrane/cytoskeletal remodeling. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Dec 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.18081.1,
                                           SRR1803613.197637.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA2144333 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.12"
     Protein         1..819
                     /product="connector enhancer of kinase suppressor of ras 2
                     isoform 6"
                     /note="connector enhancer of KSR2; membrane-associated
                     guanylate kinase-interacting protein; CNK homolog protein
                     2"
                     /calculated_mol_wt=92615
     Region          8..76
                     /region_name="SAM_CNK1,2,3-suppressor"
                     /note="SAM domain of CNK1,2,3-suppressor subfamily;
                     cd09511"
                     /db_xref="CDD:188910"
     Site            order(24,49,53,58..65,67..68,71)
                     /site_type="other"
                     /note="heterodimer interface EH [polypeptide binding]"
                     /db_xref="CDD:188910"
     Region          84..176
                     /region_name="CRIC_ras_sig"
                     /note="Connector enhancer of kinase suppressor of ras;
                     pfam10534"
                     /db_xref="CDD:463138"
     Region          214..294
                     /region_name="PDZ_CNK1_2_3-like"
                     /note="PDZ domain of connector enhancer of kinase
                     suppressor of ras 1 (CNK1), CNK2, CNK3, and related
                     domains; cd06748"
                     /db_xref="CDD:467230"
     Site            order(226..232,242,245,275,279,282..283)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467230"
     Region          290..>408
                     /region_name="CNK2_3_dom"
                     /note="Connector enhancer of kinase suppressor of ras 2/3
                     domain; pfam06663"
                     /db_xref="CDD:461979"
     Region          480..593
                     /region_name="PH_CNK_mammalian-like"
                     /note="Connector enhancer of KSR (Kinase suppressor of
                     ras) (CNK) pleckstrin homology (PH) domain; cd01260"
                     /db_xref="CDD:269962"
     CDS             1..819
                     /gene="CNKSR2"
                     /gene_synonym="CNK2; KSR2; MAGUIN; MRXSHG"
                     /coded_by="NM_001330771.2:481..2940"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS87730.1"
                     /db_xref="GeneID:22866"
                     /db_xref="HGNC:HGNC:19701"
                     /db_xref="MIM:300724"
ORIGIN      
        1 malimepvsk wspsqvvdwm kglddclqqy iknferekis gdqllrithq eledlgvsri
       61 ghqelileav dllcalnygl etenlktlsh klnasaknlq nfitgrrrsg hydgrtsrkl
      121 pndfltsvvd ligaakslla wldrspfaav tdysvtrnnv iqlcleltti vqqdctvyet
      181 enkilhvckt lsgvcdhiis lssdplvsqs ahleviqlan ikpseglgmy ikstydglhv
      241 itgttenspa drckkihagd eviqvnhqtv pliprsptss vatpsstist ptkrdssalq
      301 dlyippppae pyiprdekgn lpcedlrghm vgkpvhkgse spnsfldqey rkrfniveed
      361 tvlycyeyek grsssqgrre stptyensll rymsnekiaq eeymfqrnsk kdtgkkskkk
      421 gdksnspthy sllpslqmda lrqdimgtpv pettlyhtfq qsslqhkskk knkgpiagks
      481 krrisckdlg rgdcegwlwk kkdaksyfsq kwkkywfvlk daslywyine edekaegfis
      541 lpefkidras ecrkkyafka chpkiksfyf aaehlddmnr wlnrinmlta gyaererikq
      601 eqdywsesdk eeadtpstpk qdsppppydt yprppsmsca spyveakhsr lsstetsqsq
      661 ssheefrqev tgssavspir ktasqrrswq dlietpltss glhylqtlpl edsvfsdsaa
      721 ispehrrqst lptqkchlqd hygpyplaes ermqvlngng gkprsftlpr dsgfnhccln
      781 apvsacdpqd dvqppeveee eeeeeeegea agenigeks
//
LOCUS       NP_060252               2430 aa            linear   PRI 21-NOV-2025
DEFINITION  protein TASOR 2 isoform 1 [Homo sapiens].
ACCESSION   NP_060252 XP_374765 XP_943063
VERSION     NP_060252.5
DBSOURCE    REFSEQ: accession NM_017782.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2430)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2430)
  AUTHORS   Jensvold,Z.D., Flood,J.R., Christenson,A.E. and Lewis,P.W.
  TITLE     Interplay between Two Paralogous Human Silencing Hub (HuSH)
            Complexes in Regulating LINE-1 Element Silencing
  JOURNAL   Nat Commun 15 (1), 9492 (2024)
   PUBMED   39489739
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2430)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   4  (residues 1 to 2430)
  AUTHORS   Krishnamoorthy,V., Foglizzo,M., Dilley,R.L., Wu,A., Datta,A.,
            Dutta,P., Campbell,L.J., Degtjarik,O., Musgrove,L.J.,
            Calabrese,A.N., Zeqiraj,E. and Greenberg,R.A.
  TITLE     The SPATA5-SPATA5L1 ATPase complex directs replisome proteostasis
            to ensure genome integrity
  JOURNAL   Cell 187 (9), 2250-2268 (2024)
   PUBMED   38554706
REFERENCE   5  (residues 1 to 2430)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 2430)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   7  (residues 1 to 2430)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   8  (residues 1 to 2430)
  AUTHORS   Savage,S.A., Mirabello,L., Wang,Z., Gastier-Foster,J.M.,
            Gorlick,R., Khanna,C., Flanagan,A.M., Tirabosco,R., Andrulis,I.L.,
            Wunder,J.S., Gokgoz,N., Patino-Garcia,A., Sierrasesumaga,L.,
            Lecanda,F., Kurucu,N., Ilhan,I.E., Sari,N., Serra,M., Hattinger,C.,
            Picci,P., Spector,L.G., Barkauskas,D.A., Marina,N., de Toledo,S.R.,
            Petrilli,A.S., Amary,M.F., Halai,D., Thomas,D.M., Douglass,C.,
            Meltzer,P.S., Jacobs,K., Chung,C.C., Berndt,S.I., Purdue,M.P.,
            Caporaso,N.E., Tucker,M., Rothman,N., Landi,M.T., Silverman,D.T.,
            Kraft,P., Hunter,D.J., Malats,N., Kogevinas,M., Wacholder,S.,
            Troisi,R., Helman,L., Fraumeni,J.F. Jr., Yeager,M., Hoover,R.N. and
            Chanock,S.J.
  TITLE     Genome-wide association study identifies two susceptibility loci
            for osteosarcoma
  JOURNAL   Nat Genet 45 (7), 799-803 (2013)
   PUBMED   23727862
REFERENCE   9  (residues 1 to 2430)
  AUTHORS   Oshikawa,M., Tsutsui,C., Ikegami,T., Fuchida,Y., Matsubara,M.,
            Toyama,S., Usami,R., Ohtoko,K. and Kato,S.
  TITLE     Full-length transcriptome analysis of human retina-derived cell
            lines ARPE-19 and Y79 using the vector-capping method
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6662-6670 (2011)
   PUBMED   21697133
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 2430)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL365356.13 and AL596094.2.
            
            On Aug 13, 2020 this sequence version replaced NP_060252.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR936780.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2430
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p15.1"
     Protein         1..2430
                     /product="protein TASOR 2 isoform 1"
                     /note="protein FAM208B; family with sequence similarity
                     208 member B; protein TASOR 2"
                     /calculated_mol_wt=268713
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Region          94..167
                     /region_name="DUF3699"
                     /note="Protein of unknown function (DUF3699); pfam12480"
                     /db_xref="CDD:463601"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Region          416..488
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Region          552..701
                     /region_name="DUF3715"
                     /note="Protein of unknown function (DUF3715); pfam12509"
                     /db_xref="CDD:463613"
     Region          577..648
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Site            685
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Region          704..727
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Site            1025
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Site            1087
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Site            1172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Region          1331..1360
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Site            1541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Region          1700..1727
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Site            1848
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Site            2009
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Site            2037
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Region          2046..2069
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Site            2062
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5DTT3; propagated from
                     UniProtKB/Swiss-Prot (Q5VWN6.1)"
     Site            2066
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VWN6.1)"
     CDS             1..2430
                     /gene="TASOR2"
                     /gene_synonym="bA318E3.2; C10orf18; FAM208B"
                     /coded_by="NM_017782.5:626..7918"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41485.1"
                     /db_xref="GeneID:54906"
                     /db_xref="HGNC:HGNC:23484"
                     /db_xref="MIM:621243"
ORIGIN      
        1 mappahksil ersenvlmsp wkgklivqdr mlcdialwst ygamiptqlp qeldfkyvmk
       61 vsslkkrlpe aafrkqnyle ekvcfqdlcf nlyevelsnr qgenidklte ciknkqlaii
      121 kcledrgffi lltssallse pdfggkqmgl hglhlfrspl stgvkdlkve ddismkvipi
      181 lstlncalle tkkslpeeri hpntlvkrhf qelykadrsp slsvapqdrm kdptflgklp
      241 sgfdlippae kcpsesltql nsyfsdpsay ilevstaldl laehpqspcv sdgicdagfs
      301 lvmtpdpefl vseaevrket etkkdseeml kakkrvfpls pasnlrvqpk rkasmphmvq
      361 skkvnlcrpf pkrtasradn ssdspttlkl vkgqfpqkrk rgaevltaqf vqktkldrkn
      421 qeapiskdvp vptnakrark qekspvktvp rakppvkksp qkqrvnivkg nenprnrkql
      481 qpvkgetask lqseisrgcq edgisinsvq penttaahnd lpensivnyd sqalnmladl
      541 alssatsstp vsearnlhcs selpqndvll skenslrgts dheyhrgvkt qkgellpnps
      601 sdrksnsgsd ltvsqdeesl vpcsqapaka qsalteemle ssdasqsssv svehsyalll
      661 tehskkhlqe reilsplfpr ngtkspeaat pvgkvmpfrh qpglllqqkp pddpvvkpkd
      721 rppsarvkks scsrivlscd dsvkitfkce teyafsldsk ytnnplektv vralhgpwnt
      781 dlpdnveevk lllhmwvalf ysnqnkiirs srkvvehsnp akyvsinstl escelreiee
      841 slglekcsad slletneisr ahaaevsfrd pncllpfikt pltqglelcv qneqkktfar
      901 ecdpdtqedq nficsynnev tgeeakqesl etsnlvlsgi gstqtngpsv pseeeivqpl
      961 dstrvasysg tvtqatftrt ydgpgsqpvi cqssvygtle nkvdildaav qtktgtlqdl
     1021 iqhgspinne chpslerkdd nmgcavinpe pitltfekna hvpiqtegvn taderttfkk
     1081 elikqvspaa slrhpvstse nartqglrdi pslvvagqkg tkylcassvg getldkavcs
     1141 lqketplpvs lpsdktmvme alslaksssh lspseevrct qdflsqtqsl lglsseglle
     1201 ltqvevdsss asttlgrqcs lncissgcht sgdslelrkn hkngpntenm nleafdsvfi
     1261 kqtslsvsre vslelseeds didlaltisp ptspreempa geieqfeeap fsnlelqdva
     1321 eeigepeeva ltesrevssa dnvsvypsvs eepvenkerk gdnlqpvtli lskenctlei
     1381 aeeinvtsdf pfdsvieevs passpeppvp vketrpyqav tpcilklhgt qceksnqisq
     1441 cesedlgite kenvfvgpth pvgqdnftqv qqmqvsaemp liltdhpgrt grptlpgkvt
     1501 eeivssehde glsfsgkvqc ygrelnqpas aakctgdfsp speklvksgn plqpvsienr
     1561 nldlkhlvle sseppfgprn vienkslsdt lvsttapsgi vnvsvkqqts pkssqnhlfp
     1621 gdlktdegiy lqvksltaas vdgaystqgc mcsvvptlcs ssdnatlthy vrpinaepvf
     1681 qaqeipagrm asllkngepe aelhkettgp gtagpqsntt sslkgerkai htlqdvstce
     1741 tkellnvgvs slcagpyqnt adtkenlske plasfvsesf dtsvcgiate hveiensgeg
     1801 lraeagsetl grdgevgvns dmhyelsgds dldllgdcrn prldledsyt lrgsytrkkd
     1861 vptdgyessl nfhnnnqedw gcsswvpgme tslppghwta avkkeekcvp pyvqirdlhg
     1921 ilrtyanfsi tkelkdtmrt shglrrhpsf sancglpssw tstwqvaddl tqntldleyl
     1981 rfahklkqti kngdsqhsas sanvfpkesp tqisigafps tkiseapflh paprsrspll
     2041 vtvvesdprp qgqprrgyta ssldsssswr ercshnrdlr nsqrnhtvsf hlnklkynst
     2101 vkesrndisl ilneyaefnk vmknsnqfif qdkelndvsg eataqemylp fpgrsasyed
     2161 iiidvctnlh vklrsvvkea ckstflfylv etedksffvr tknllrkggh teiepqhfcq
     2221 afhrendtli iiirnediss hlhqipsllk lkhfpsvifa gvdspgdvld htyqelfrag
     2281 gfvisddkil eavtlvqlke iikileklng ngrwkwllhy renkklkede rvdstahkkn
     2341 imlksfqsan iiellhyhqc dsrsstkaei lkcllnlqiq hidarfavll tdkptiprev
     2401 fensgilvtd vnnfieniek iaapfrssyw
//
LOCUS       NP_006306                242 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb group RING finger protein 3 isoform a [Homo sapiens].
ACCESSION   NP_006306 NP_694982
VERSION     NP_006306.2
DBSOURCE    REFSEQ: accession NM_006315.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Hu,Y., Cheng,Y., Jiang,X., Zhang,Y., Wang,H., Ren,H., Xu,Y.,
            Jiang,J., Wang,Q., Su,H., Zhang,B. and Qiu,X.
  TITLE     PCGF3 promotes the proliferation and migration of non-small cell
            lung cancer cells via the PI3K/AKT signaling pathway
  JOURNAL   Exp Cell Res 400 (2), 112496 (2021)
   PUBMED   33485844
  REMARK    GeneRIF: PCGF3 promotes the proliferation and migration of
            non-small cell lung cancer cells via the PI3K/AKT signaling
            pathway.
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Mu,G., Xiang,Q., Zhang,Z., Liu,C., Zhang,H., Liu,Z., Pang,X.,
            Jiang,J., Xie,Q., Zhou,S., Wang,Z., Hu,K., Wang,Z., Jiang,S.,
            Qin,X. and Cui,Y.
  TITLE     PNPT1 and PCGF3 variants associated with angiotensin-converting
            enzyme inhibitor-induced cough: a nested case-control genome-wide
            study
  JOURNAL   Pharmacogenomics 21 (9), 601-614 (2020)
   PUBMED   32397904
  REMARK    GeneRIF: PNPT1 and PCGF3 variants associated with
            angiotensin-converting enzyme inhibitor-induced cough: a nested
            case-control genome-wide study.
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Purohit,G., Mukherjee,A.K., Sharma,S. and Chowdhury,S.
  TITLE     Extratelomeric Binding of the Telomere Binding Protein TRF2 at the
            PCGF3 Promoter Is G-Quadruplex Motif-Dependent
  JOURNAL   Biochemistry 57 (16), 2317-2324 (2018)
   PUBMED   29589913
  REMARK    GeneRIF: We demonstrate that promoter binding by TRF2 mediates
            PCGF3 promoter activity, and both the N-terminal and C-terminal
            domains of TRF2 are necessary for promoter activity.
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Marcon,E., Ni,Z., Pu,S., Turinsky,A.L., Trimble,S.S., Olsen,J.B.,
            Silverman-Gavrila,R., Silverman-Gavrila,L., Phanse,S., Guo,H.,
            Zhong,G., Guo,X., Young,P., Bailey,S., Roudeva,D., Zhao,D.,
            Hewel,J., Li,J., Graslund,S., Paduch,M., Kossiakoff,A.A.,
            Lupien,M., Emili,A., Wodak,S.J. and Greenblatt,J.
  TITLE     Human-chromatin-related protein interactions identify a demethylase
            complex required for chromosome segregation
  JOURNAL   Cell Rep 8 (1), 297-310 (2014)
   PUBMED   24981860
REFERENCE   7  (residues 1 to 242)
  AUTHORS   Woodsmith,J., Jenn,R.C. and Sanderson,C.M.
  TITLE     Systematic analysis of dimeric E3-RING interactions reveals
            increased combinatorial complexity in human ubiquitination networks
  JOURNAL   Mol Cell Proteomics 11 (7), M111.016162 (2012)
   PUBMED   22493164
REFERENCE   8  (residues 1 to 242)
  AUTHORS   Oudot-Mellakh,T., Cohen,W., Germain,M., Saut,N., Kallel,C.,
            Zelenika,D., Lathrop,M., Tregouet,D.A. and Morange,P.E.
  TITLE     Genome wide association study for plasma levels of natural
            anticoagulant inhibitors and protein C anticoagulant pathway: the
            MARTHA project
  JOURNAL   Br J Haematol 157 (2), 230-239 (2012)
   PUBMED   22443383
REFERENCE   9  (residues 1 to 242)
  AUTHORS   Gao,Z., Zhang,J., Bonasio,R., Strino,F., Sawai,A., Parisi,F.,
            Kluger,Y. and Reinberg,D.
  TITLE     PCGF homologs, CBX proteins, and RYBP define functionally distinct
            PRC1 family complexes
  JOURNAL   Mol Cell 45 (3), 344-356 (2012)
   PUBMED   22325352
REFERENCE   10 (residues 1 to 242)
  AUTHORS   Vandamme,J., Volkel,P., Rosnoblet,C., Le Faou,P. and Angrand,P.O.
  TITLE     Interaction proteomics analysis of polycomb proteins defines
            distinct PRC1 complexes in mammalian cells
  JOURNAL   Mol Cell Proteomics 10 (4), M110.002642 (2011)
   PUBMED   21282530
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107464.5 and AC139887.3.
            
            On or before Aug 27, 2003 this sequence version replaced
            NP_694982.2, NP_006306.1.
            
            Summary: The protein encoded by this gene contains a C3HC4 type
            RING finger, which is a motif known to be involved in
            protein-protein interactions. The specific function of this protein
            has not yet been determined. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an alternate exon in the
            5' UTR compared to variant 1. Variants 1-7 all encode the same
            isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.533208.1,
                                           SRR14038196.3559349.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000362003.10/ ENSP00000354724.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..242
                     /product="polycomb group RING finger protein 3 isoform a"
                     /note="ring finger protein 3; polycomb group RING finger
                     protein 3; RING finger protein 3A"
                     /calculated_mol_wt=27984
     Region          4..69
                     /region_name="RING-HC_PCGF3"
                     /note="RING finger found in polycomb group RING finger
                     protein 3 (PCGF3) and similar proteins; cd16735"
                     /db_xref="CDD:438393"
     Site            order(16,20,22..23,26,28..29,31..35,38..41,43..44)
                     /site_type="other"
                     /note="putative heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:438393"
     Region          115..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KNV8.1)"
     Region          132..242
                     /region_name="Interaction with BCORL1.
                     /evidence=ECO:0000269|PubMed:27568929"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KNV8.1)"
     Region          154..236
                     /region_name="RAWUL_PCGF3"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in polycomb group RING finger protein
                     3 (PCGF3) and similar proteins; cd17083"
                     /db_xref="CDD:340603"
     CDS             1..242
                     /gene="PCGF3"
                     /gene_synonym="DONG1; RNF3; RNF3A"
                     /coded_by="NM_006315.7:329..1057"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3339.2"
                     /db_xref="GeneID:10336"
                     /db_xref="HGNC:HGNC:10066"
                     /db_xref="MIM:617543"
ORIGIN      
        1 mltrkiklwd inahitcrlc sgylidattv teclhtfcrs clvkyleenn tcptcrivih
       61 qshplqyigh drtmqdivyk lvpglqeaem rkqrefyhkl gmevpgdikg etcsakqhld
      121 shrngetkad dssnkeaaee kpeedndyhr sdeqvsicle cnssklrglk rkwircsaqa
      181 tvlhlkkfia kklnlssfne ldilcneeil gkdhtlkfvv vtrwrfkkap lllhyrpkmd
      241 ll
//
LOCUS       NP_001303285             356 aa            linear   PRI 21-NOV-2025
DEFINITION  COP9 signalosome complex subunit 3 isoform 5 [Homo sapiens].
ACCESSION   NP_001303285 XP_005256896
VERSION     NP_001303285.1
DBSOURCE    REFSEQ: accession NM_001316356.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Niu,J., Yan,T., Guo,W., Wang,W., Ren,T., Huang,Y., Zhao,Z., Yu,Y.,
            Chen,C., Huang,Q., Lou,J. and Guo,L.
  TITLE     The COPS3-FOXO3 positive feedback loop regulates autophagy to
            promote cisplatin resistance in osteosarcoma
  JOURNAL   Autophagy 19 (6), 1693-1710 (2023)
   PUBMED   36451342
  REMARK    GeneRIF: The COPS3-FOXO3 positive feedback loop regulates autophagy
            to promote cisplatin resistance in osteosarcoma.
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Liu,W., Nichols,A.F., Graham,J.A., Dualan,R., Abbas,A. and Linn,S.
  TITLE     Nuclear transport of human DDB protein induced by ultraviolet light
  JOURNAL   J Biol Chem 275 (28), 21429-21434 (2000)
   PUBMED   10777491
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Bianchi,E., Denti,S., Granata,A., Bossi,G., Geginat,J., Villa,A.,
            Rogge,L. and Pardi,R.
  TITLE     Integrin LFA-1 interacts with the transcriptional co-activator JAB1
            to modulate AP-1 activity
  JOURNAL   Nature 404 (6778), 617-621 (2000)
   PUBMED   10766246
REFERENCE   8  (residues 1 to 356)
  AUTHORS   Potocki,L., Chen,K.S. and Lupski,J.R.
  TITLE     Subunit 3 of the COP9 signal transduction complex is conserved from
            plants to humans and maps within the smith-magenis syndrome
            critical region in 17p11.2
  JOURNAL   Genomics 57 (1), 180-182 (1999)
   PUBMED   10191102
REFERENCE   9  (residues 1 to 356)
  AUTHORS   Wei,N., Tsuge,T., Serino,G., Dohmae,N., Takio,K., Matsui,M. and
            Deng,X.W.
  TITLE     The COP9 complex is conserved between plants and mammals and is
            related to the 26S proteasome regulatory complex
  JOURNAL   Curr Biol 8 (16), 919-922 (1998)
   PUBMED   9707402
REFERENCE   10 (residues 1 to 356)
  AUTHORS   Seeger,M., Kraft,R., Ferrell,K., Bech-Otschir,D., Dumdey,R.,
            Schade,R., Gordon,C., Naumann,M. and Dubiel,W.
  TITLE     A novel protein complex involved in signal transduction possessing
            similarities to 26S proteasome subunits
  JOURNAL   FASEB J 12 (6), 469-478 (1998)
   PUBMED   9535219
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP260214.1, DB493356.1,
            BU171304.1, AF031647.1, BC001891.1, BU952436.1 and AC055811.20.
            
            On Oct 17, 2015 this sequence version replaced XP_005256896.1.
            
            Summary: The protein encoded by this gene possesses kinase activity
            that phosphorylates regulators involved in signal transduction. It
            phosphorylates I kappa-Balpha, p105, and c-Jun. It acts as a
            docking site for complex-mediated phosphorylation. The gene is
            located within the Smith-Magenis syndrome region on chromosome 17.
            Several transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (5) lacks a 5' exon compared to
            variant 1. This difference causes translation initiation at a
            downstream AUG and results in an isoform (5) with a shorter
            N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2338851.1,
                                           SRR14038196.236012.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..356
                     /product="COP9 signalosome complex subunit 3 isoform 5"
                     /note="COP9 complex subunit 3; JAB1-containing signalosome
                     subunit 3; COP9 signalosome complex subunit 3; COP9
                     constitutive photomorphogenic homolog subunit 3"
                     /calculated_mol_wt=40518
     Region          192..295
                     /region_name="PCI"
                     /note="PCI domain; pfam01399"
                     /db_xref="CDD:460195"
     CDS             1..356
                     /gene="COPS3"
                     /gene_synonym="CSN3; SGN3"
                     /coded_by="NM_001316356.2:132..1202"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:8533"
                     /db_xref="HGNC:HGNC:2239"
                     /db_xref="MIM:604665"
ORIGIN      
        1 mpsvpdfetl fsqvqlfist cngehiryat dtfaglchql tnalverkqp lrgigilkqa
       61 idkmqmntnq ltsihadlcq lcllakcfkp alpyldvdmm dickengayd akhflcyyyy
      121 ggmiytglkn feralyfyeq aittpamavs himlesykky ilvslillgk vqqlpkytsq
      181 ivgrfikpls nayhelaqvy stnnpselrn lvnkhsetft rdnnmglvkq clsslykkni
      241 qrltktfltl slqdmasrvq lsgpqeaeky vlhmiedgei fasinqkdgm vsfhdnpeky
      301 nnpamlhnid qemlkcield erlkamdqei tvnpqfvqks mgsqeddsgn kpssys
//
LOCUS       NP_001374942            1010 aa            linear   PRI 21-NOV-2025
DEFINITION  large proline-rich protein BAG6 isoform 24 [Homo sapiens].
ACCESSION   NP_001374942
VERSION     NP_001374942.1
DBSOURCE    REFSEQ: accession NM_001388013.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Alashkar Alhamwe,B., Ponath,V., Alhamdan,F., Dorsam,B.,
            Landwehr,C., Linder,M., Pauck,K., Miethe,S., Garn,H.,
            Finkernagel,F., Brichkina,A., Lauth,M., Tiwari,D.K., Buchholz,M.,
            Bachurski,D., Elmshauser,S., Nist,A., Stiewe,T., Pogge von
            Strandmann,L., Szymanski,W., Beutgen,V., Graumann,J.,
            Teply-Szymanski,J., Keber,C., Denkert,C., Jacob,R., Preusser,C. and
            Pogge von Strandmann,E.
  TITLE     BAG6 restricts pancreatic cancer progression by suppressing the
            release of IL33-presenting extracellular vesicles and the
            activation of mast cells
  JOURNAL   Cell Mol Immunol 21 (8), 918-931 (2024)
   PUBMED   38942797
  REMARK    GeneRIF: BAG6 restricts pancreatic cancer progression by
            suppressing the release of IL33-presenting extracellular vesicles
            and the activation of mast cells.
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Liu,L., Wu,J., Yan,Y., Cheng,S., Yu,S. and Wang,Y.
  TITLE     DERL2 (derlin 2) stabilizes BAG6 (BAG cochaperone 6) in
            chemotherapy resistance of cholangiocarcinoma
  JOURNAL   J Physiol Biochem 80 (1), 81-97 (2024)
   PUBMED   37815698
  REMARK    GeneRIF: DERL2 (derlin 2) stabilizes BAG6 (BAG cochaperone 6) in
            chemotherapy resistance of cholangiocarcinoma.
REFERENCE   4  (residues 1 to 1010)
  AUTHORS   Roboti,P., Lawless,C. and High,S.
  TITLE     Mitochondrial antiviral-signalling protein is a client of the BAG6
            protein quality control complex
  JOURNAL   J Cell Sci 135 (9) (2022)
   PUBMED   35543156
  REMARK    GeneRIF: Mitochondrial antiviral-signalling protein is a client of
            the BAG6 protein quality control complex.
REFERENCE   5  (residues 1 to 1010)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1010)
  AUTHORS   Ozaki,T., Hanaoka,E., Naka,M., Nakagawara,A. and Sakiyama,S.
  TITLE     Cloning and characterization of rat BAT3 cDNA
  JOURNAL   DNA Cell Biol 18 (6), 503-512 (1999)
   PUBMED   10390159
REFERENCE   7  (residues 1 to 1010)
  AUTHORS   Cross,S.J., Tonks,S., Trowsdale,J. and Campbell,R.D.
  TITLE     Novel detection of restriction fragment length polymorphisms in the
            human major histocompatibility complex
  JOURNAL   Immunogenetics 34 (6), 376-384 (1991)
   PUBMED   1684176
REFERENCE   8  (residues 1 to 1010)
  AUTHORS   Banerji,J., Sands,J., Strominger,J.L. and Spies,T.
  TITLE     A gene pair from the human major histocompatibility complex encodes
            large proline-rich proteins with multiple repeated motifs and a
            single ubiquitin-like domain
  JOURNAL   Proc Natl Acad Sci U S A 87 (6), 2374-2378 (1990)
   PUBMED   2156268
REFERENCE   9  (residues 1 to 1010)
  AUTHORS   Spies,T., Bresnahan,M. and Strominger,J.L.
  TITLE     Human major histocompatibility complex contains a minimum of 19
            genes between the complement cluster and HLA-B
  JOURNAL   Proc Natl Acad Sci U S A 86 (22), 8955-8958 (1989)
   PUBMED   2813433
REFERENCE   10 (residues 1 to 1010)
  AUTHORS   Spies,T., Blanck,G., Bresnahan,M., Sands,J. and Strominger,J.L.
  TITLE     A new cluster of genes within the human major histocompatibility
            complex
  JOURNAL   Science 243 (4888), 214-217 (1989)
   PUBMED   2911734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL662801.7.
            
            Summary: This gene was first characterized as part of a cluster of
            genes located within the human major histocompatibility complex
            class III region. This gene encodes a nuclear protein that is
            cleaved by caspase 3 and is implicated in the control of apoptosis.
            In addition, the protein forms a complex with E1A binding protein
            p300 and is required for the acetylation of p53 in response to DNA
            damage. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..1010
                     /product="large proline-rich protein BAG6 isoform 24"
                     /note="scythe; large proline-rich protein BAT3; large
                     proline-rich protein BAG6; protein G3; HLA-B-associated
                     transcript 3; protein Scythe; BAG family molecular
                     chaperone regulator 6; BCL2 associated athanogene 6"
                     /calculated_mol_wt=106521
     Region          17..87
                     /region_name="Ubl_BAG6"
                     /note="ubiquitin-like (Ubl) domain found in
                     BCL2-associated athanogene 6 (BAG6) and similar proteins;
                     cd01809"
                     /db_xref="CDD:340507"
     Site            order(22..25,58,60,62..65,83..87)
                     /site_type="other"
                     /note="ZF interaction site [polypeptide binding]"
                     /db_xref="CDD:340507"
     Region          252..368
                     /region_name="BAG6"
                     /note="BCL2-associated athanogene 6; pfam12057"
                     /db_xref="CDD:463449"
     CDS             1..1010
                     /gene="BAG6"
                     /gene_synonym="BAG-6; BAT3; D6S52E; G3"
                     /coded_by="NM_001388013.1:284..3316"
                     /note="isoform 24 is encoded by transcript variant 53"
                     /db_xref="GeneID:7917"
                     /db_xref="HGNC:HGNC:13919"
                     /db_xref="MIM:142590"
ORIGIN      
        1 mepndststa veepdslevl vktldsqtrt fivgaqmnvk efkehiaasv sipsekqrli
       61 yqgrvlqddk klqeynvggk vihlverapp qthlpsgass gtgsasathg ggsppgtrgp
      121 gasvhdrnan syvmvgtfnl pseprvrlvm aqhmirdiqt llsrmecrgg pqpqhsqppp
      181 qppavtpepv alssqtsepv eseapprepm eaeeveerap aqnpeltpgp apagptpape
      241 tnapnhpspa eyvevlqelq rlesrlqpfl qryyevlgaa attdynnnhe greedqrlin
      301 lvgeslrllg ntfvalsdlr cnlactpprh lhvvrpmshy ttpmvlqqaa ipiqinvgtt
      361 vtmtgngtrp pptpnaeapp pgpgqassva psstnvessa egapppgpap ppatshprvi
      421 rishqsvepv vmmhmniqds gtqpggvpsa ptgplgppgh gqtlgqqvpg fptaptrvvi
      481 arptppqarp shpggppvsg tlgaglgtna slaqmvsglv gqllmqpvlv aqgtpgmapp
      541 papatasasa gttntattag papggpaqpp ptpqpsmadl qfsqllgnll gpagpgaggs
      601 gvasptitva mpgvpaflqg mtdflqatqt appppppppp pppapeqqtm pppgspsgga
      661 gspgglgles lspefftsvv qgvlssllgs lgaragsses iaafiqrlsg ssnifepgad
      721 galgffgall sllcqnfsmv dvvmllhghf qplqrlqpql rsffhqhylg gqeptpsnir
      781 mathtlitgl eeyvresfsl vqvqpgvdii rtnleflqeq fnsiaahvlh ctdsgfgarl
      841 lelcnqglfe clalnlhclg gqqmelaavi ngrirrmsrg vnpslvswlt tmmglrlqvv
      901 lehmpvgpda ilryvrrvgd ppqplpeepm evqgaerasp epqewvpiiq qdiqsqrkvk
      961 pqpplsdayl sgmpakrrkl rsdiqkrlqe dpnyspqrfp naqrafaddp
//
LOCUS       NP_001369296              89 aa            linear   PRI 21-NOV-2025
DEFINITION  dynein light chain roadblock-type 1 isoform f [Homo sapiens].
ACCESSION   NP_001369296
VERSION     NP_001369296.1
DBSOURCE    REFSEQ: accession NM_001382367.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Canty,J.T., Tan,R., Kusakci,E., Fernandes,J. and Yildiz,A.
  TITLE     Structure and Mechanics of Dynein Motors
  JOURNAL   Annu Rev Biophys 50, 549-574 (2021)
   PUBMED   33957056
  REMARK    Review article
REFERENCE   4  (residues 1 to 89)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 89)
  AUTHORS   Vuolo,L., Stevenson,N.L., Mukhopadhyay,A.G., Roberts,A.J. and
            Stephens,D.J.
  TITLE     Cytoplasmic dynein-2 at a glance
  JOURNAL   J Cell Sci 133 (6) (2020)
   PUBMED   32229580
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 89)
  AUTHORS   Pfister,K.K., Fisher,E.M., Gibbons,I.R., Hays,T.S., Holzbaur,E.L.,
            McIntosh,J.R., Porter,M.E., Schroer,T.A., Vaughan,K.T.,
            Witman,G.B., King,S.M. and Vallee,R.B.
  TITLE     Cytoplasmic dynein nomenclature
  JOURNAL   J Cell Biol 171 (3), 411-413 (2005)
   PUBMED   16260502
REFERENCE   7  (residues 1 to 89)
  AUTHORS   Tang,Q., Staub,C.M., Gao,G., Jin,Q., Wang,Z., Ding,W.,
            Aurigemma,R.E. and Mulder,K.M.
  TITLE     A novel transforming growth factor-beta receptor-interacting
            protein that is also a light chain of the motor protein dynein
  JOURNAL   Mol Biol Cell 13 (12), 4484-4496 (2002)
   PUBMED   12475967
REFERENCE   8  (residues 1 to 89)
  AUTHORS   Susalka,S.J., Nikulina,K., Salata,M.W., Vaughan,P.S., King,S.M.,
            Vaughan,K.T. and Pfister,K.K.
  TITLE     The roadblock light chain binds a novel region of the cytoplasmic
            Dynein intermediate chain
  JOURNAL   J Biol Chem 277 (36), 32939-32946 (2002)
   PUBMED   12077152
REFERENCE   9  (residues 1 to 89)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Ray,S., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human retina for the NEIBank
            Project: retbindin, an abundant, novel retinal cDNA and alternative
            splicing of other retina-preferred gene transcripts
  JOURNAL   Mol Vis 8, 196-204 (2002)
   PUBMED   12107411
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 89)
  AUTHORS   Jiang,J., Yu,L., Huang,X., Chen,X., Li,D., Zhang,Y., Tang,L. and
            Zhao,S.
  TITLE     Identification of two novel human dynein light chain genes, DNLC2A
            and DNLC2B, and their expression changes in hepatocellular
            carcinoma tissues from 68 Chinese patients
  JOURNAL   Gene 281 (1-2), 103-113 (2001)
   PUBMED   11750132
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109923.29 and AL136173.24.
            
            Summary: This gene is a member of the roadblock dynein light chain
            family. The encoded cytoplasmic protein is capable of binding
            intermediate chain proteins, interacts with transforming growth
            factor-beta, and has been implicated in the regulation of actin
            modulating proteins. Upregulation of this gene has been associated
            with hepatocellular carcinomas, suggesting that this gene may be
            involved in tumor progression. Alternative splicing results in
            multiple transcript variants. Pseudogenes of this gene have been
            defined on chromosomes 12 and 18. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.4030681.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146236, SAMEA2151741
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..89
                     /product="dynein light chain roadblock-type 1 isoform f"
                     /note="dynein, cytoplasmic, light polypeptide 2A;
                     bithoraxoid-like protein; dynein-associated protein Km23;
                     ROBL/LC7-like 1; roadblock domain-containing protein 1"
                     /calculated_mol_wt=9860
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P62628; propagated from
                     UniProtKB/Swiss-Prot (Q9NP97.3)"
     Region          3..83
                     /region_name="Robl_LC7"
                     /note="Roadblock/LC7 domain; pfam03259"
                     /db_xref="CDD:397386"
     CDS             1..89
                     /gene="DYNLRB1"
                     /gene_synonym="BITH; BLP; DNCL2A; DNLC2A; ROBLD1"
                     /coded_by="NM_001382367.1:38..307"
                     /note="isoform f is encoded by transcript variant 10"
                     /db_xref="GeneID:83658"
                     /db_xref="HGNC:HGNC:15468"
                     /db_xref="MIM:607167"
ORIGIN      
        1 maeveetlkr lqsqkgvqgi ivvntegipi kstmdnpttt qyaslmhsfi lkarstvrdi
       61 dpqndltflr irskkneimv apafgdaer
//
LOCUS       NP_001247432             288 aa            linear   PRI 21-NOV-2025
DEFINITION  signal recognition particle subunit SRP68 isoform 3 [Homo sapiens].
ACCESSION   NP_001247432
VERSION     NP_001247432.1
DBSOURCE    REFSEQ: accession NM_001260503.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Lim,S.H., Snider,J., Birimberg-Schwartz,L., Ip,W., Serralha,J.C.,
            Botelho,H.M., Lopes-Pacheco,M., Pinto,M.C., Moutaoufik,M.T.,
            Zilocchi,M., Laselva,O., Esmaeili,M., Kotlyar,M., Lyakisheva,A.,
            Tang,P., Lopez Vazquez,L., Akula,I., Aboualizadeh,F., Wong,V.,
            Grozavu,I., Opacak-Bernardi,T., Yao,Z., Mendoza,M., Babu,M.,
            Jurisica,I., Gonska,T., Bear,C.E., Amaral,M.D. and Stagljar,I.
  TITLE     CFTR interactome mapping using the mammalian membrane two-hybrid
            high-throughput screening system
  JOURNAL   Mol Syst Biol 18 (2), e10629 (2022)
   PUBMED   35156780
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Kellogg,M.K., Miller,S.C., Tikhonova,E.B. and Karamyshev,A.L.
  TITLE     SRPassing Co-translational Targeting: The Role of the Signal
            Recognition Particle in Protein Targeting and mRNA Protection
  JOURNAL   Int J Mol Sci 22 (12), 6284 (2021)
   PUBMED   34208095
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Menichelli,E., Isel,C., Oubridge,C. and Nagai,K.
  TITLE     Protein-induced conformational changes of RNA during the assembly
            of human signal recognition particle
  JOURNAL   J Mol Biol 367 (1), 187-203 (2007)
   PUBMED   17254600
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Iakhiaeva,E., Bhuiyan,S.H., Yin,J. and Zwieb,C.
  TITLE     Protein SRP68 of human signal recognition particle: identification
            of the RNA and SRP72 binding domains
  JOURNAL   Protein Sci 15 (6), 1290-1302 (2006)
   PUBMED   16672232
  REMARK    GeneRIF: The RNA binding domain of SRP68 included residues from
            positions 52 to 252. Ninety-four amino acids near the C terminus of
            SRP68 mediated the binding to SRP72
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Harada,H., Nagai,H., Mine,N., Terada,Y., Fujiwara,H., Mikami,I.,
            Tsuneizumi,M., Yabe,A., Miyazaki,K., Yokota,T., Imoto,I.,
            Inazawa,J. and Emi,M.
  TITLE     Molecular cloning, tissue expression, and chromosomal assignment of
            a novel gene encoding a subunit of the human signal-recognition
            particle
  JOURNAL   J Hum Genet 46 (2), 70-75 (2001)
   PUBMED   11281415
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Politz,J.C., Yarovoi,S., Kilroy,S.M., Gowda,K., Zwieb,C. and
            Pederson,T.
  TITLE     Signal recognition particle components in the nucleolus
  JOURNAL   Proc Natl Acad Sci U S A 97 (1), 55-60 (2000)
   PUBMED   10618370
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Larsen,N., Samuelsson,T. and Zwieb,C.
  TITLE     The Signal Recognition Particle Database (SRPDB)
  JOURNAL   Nucleic Acids Res 26 (1), 177-178 (1998)
   PUBMED   9399828
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Lutcke,H., Prehn,S., Ashford,A.J., Remus,M., Frank,R. and
            Dobberstein,B.
  TITLE     Assembly of the 68- and 72-kD proteins of signal recognition
            particle with 7S RNA
  JOURNAL   J Cell Biol 121 (5), 977-985 (1993)
   PUBMED   8388879
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK097962.1, DQ786315.1 and
            DB315535.1.
            
            Summary: This gene encodes a subunit of the signal recognition
            particle (SRP). The SRP is a ribonucleoprotein complex that
            transports secreted and membrane proteins to the endoplasmic
            reticulum for processing. The complex includes a 7S RNA and six
            protein subunits. The encoded protein is the 68kDa component of the
            SRP, and forms a heterodimer with the 72kDa subunit that is
            required for SRP function. Alternatively spliced transcript
            variants encoding multiple isoforms have been observed for this
            gene, and three pseudogenes of this gene are located within the
            Smith-Magenis syndrome region on chromosome 17. [provided by
            RefSeq, May 2012].
            
            Transcript Variant: This variant (3) lacks a large portion of the
            5' coding region, uses an alternate 5'-most exon and initiates
            translation at a downstream, in-frame start codon, compared to
            variant 1. The encoded isoform (3) has a shorter N-terminus
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK097962.1, SRR11853563.14945.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..288
                     /product="signal recognition particle subunit SRP68
                     isoform 3"
                     /note="signal recognition particle 68 kDa protein; signal
                     recognition particle 68kDa; signal recognition particle
                     subunit SRP68"
                     /calculated_mol_wt=32720
     Region          <1..259
                     /region_name="SRP68-RBD"
                     /note="RNA-binding domain of signal recognition particle
                     subunit 68; cl22422"
                     /db_xref="CDD:473954"
     CDS             1..288
                     /gene="SRP68"
                     /gene_synonym="SCN10"
                     /coded_by="NM_001260503.2:248..1114"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58600.1"
                     /db_xref="GeneID:6730"
                     /db_xref="HGNC:HGNC:11302"
                     /db_xref="MIM:604858"
ORIGIN      
        1 mlsecrdaiq vvreelkpdq kqrdyilege pgkvsnlqyl hsyltyikls taikrnenma
       61 kglqrallqq qpeddskrsp rpqdlirlyd iilqnlvell qlpgleedka fqkeiglktl
      121 vfkayrcffi aqsyvlvkkw sealvlydrv lkyanevnsd agafknslkd lpdvqelitq
      181 vrsekcslqa aaildandah qtetsssqvk dnkplverfe tfcldpslvt kqanlvhfpp
      241 gfqpipckpl ffdlalnhva fppledkleq ktksgltgyi kgifgfrs
//
LOCUS       NP_001317018             284 aa            linear   PRI 21-NOV-2025
DEFINITION  neurexin-1 isoform 8 precursor [Homo sapiens].
ACCESSION   NP_001317018
VERSION     NP_001317018.1
DBSOURCE    REFSEQ: accession NM_001330089.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Sebastian,R., Jin,K., Pavon,N., Bansal,R., Potter,A., Song,Y.,
            Babu,J., Gabriel,R., Sun,Y., Aronow,B. and Pak,C.
  TITLE     Schizophrenia-associated NRXN1 deletions induce
            developmental-timing- and cell-type-specific vulnerabilities in
            human brain organoids
  JOURNAL   Nat Commun 14 (1), 3770 (2023)
   PUBMED   37355690
  REMARK    GeneRIF: Schizophrenia-associated NRXN1 deletions induce
            developmental-timing- and cell-type-specific vulnerabilities in
            human brain organoids.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Rhoades,R., Henry,B., Prichett,D., Fang,Y. and Teng,S.
  TITLE     Computational Saturation Mutagenesis to Investigate the Effects of
            Neurexin-1 Mutations on AlphaFold Structure
  JOURNAL   Genes (Basel) 13 (5), 789 (2022)
   PUBMED   35627176
  REMARK    GeneRIF: Computational Saturation Mutagenesis to Investigate the
            Effects of Neurexin-1 Mutations on AlphaFold Structure.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Aksu Uzunhan,T. and Ayaz,A.
  TITLE     Homozygous exonic and intragenic NRXN1 deletion presenting as
            either West syndrome or autism spectrum disorder in two siblings
  JOURNAL   Clin Neurol Neurosurg 214, 107141 (2022)
   PUBMED   35101781
  REMARK    GeneRIF: Homozygous exonic and intragenic NRXN1 deletion presenting
            as either West syndrome or autism spectrum disorder in two
            siblings.
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Yan,Q., Weyn-Vanhentenryck,S.M., Wu,J., Sloan,S.A., Zhang,Y.,
            Chen,K., Wu,J.Q., Barres,B.A. and Zhang,C.
  TITLE     Systematic discovery of regulated and conserved alternative exons
            in the mammalian brain reveals NMD modulating chromatin regulators
  JOURNAL   Proc Natl Acad Sci U S A 112 (11), 3445-3450 (2015)
   PUBMED   25737549
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Tabuchi,K. and Sudhof,T.C.
  TITLE     Structure and evolution of neurexin genes: insight into the
            mechanism of alternative splicing
  JOURNAL   Genomics 79 (6), 849-859 (2002)
   PUBMED   12036300
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Rowen,L., Young,J., Birditt,B., Kaur,A., Madan,A., Philipps,D.L.,
            Qin,S., Minx,P., Wilson,R.K., Hood,L. and Graveley,B.R.
  TITLE     Analysis of the human neurexin genes: alternative splicing and the
            generation of protein diversity
  JOURNAL   Genomics 79 (4), 587-597 (2002)
   PUBMED   11944992
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Ichtchenko,K., Hata,Y., Nguyen,T., Ullrich,B., Missler,M.,
            Moomaw,C. and Sudhof,T.C.
  TITLE     Neuroligin 1: a splice site-specific ligand for beta-neurexins
  JOURNAL   Cell 81 (3), 435-443 (1995)
   PUBMED   7736595
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Ullrich,B., Ushkaryov,Y.A. and Sudhof,T.C.
  TITLE     Cartography of neurexins: more than 1000 isoforms generated by
            alternative splicing and expressed in distinct subsets of neurons
  JOURNAL   Neuron 14 (3), 497-507 (1995)
   PUBMED   7695896
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Ushkaryov,Y.A., Petrenko,A.G., Geppert,M. and Sudhof,T.C.
  TITLE     Neurexins: synaptic cell surface proteins related to the
            alpha-latrotoxin receptor and laminin
  JOURNAL   Science 257 (5066), 50-56 (1992)
   PUBMED   1621094
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007682.3 and BX113737.1.
            
            Summary: This gene encodes a single-pass type I membrane protein
            that belongs to the neurexin family. Neurexins are cell-surface
            receptors that bind neuroligins to form Ca(2+)-dependent
            neurexin/neuroligin complexes at synapses in the central nervous
            system. This complex is required for efficient neurotransmission
            and is involved in the formation of synaptic contacts. Three
            members of this gene family have been studied in detail and are
            estimated to generate over 3,000 variants through the use of two
            alternative promoters (alpha and beta) and extensive alternative
            splicing in each family member. Recently, a third promoter (gamma)
            was identified for this gene in the 3' region. Mutations in this
            gene are associated with Pitt-Hopkins-like syndrome-2 and may
            contribute to susceptibility to schizophrenia. [provided by RefSeq,
            Aug 2016].
            
            Transcript Variant: This variant (8) lacks multiple 3' coding exons
            and contains an alternate 3' exon structure compared to variant
            alpha2. The encoded isoform (8) is much shorter than isoform alpha2
            and has a distinct C-terminus.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.201117.1,
                                           SRR3476690.371137.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.3"
     Protein         1..284
                     /product="neurexin-1 isoform 8 precursor"
                     /note="neurexin I"
                     /calculated_mol_wt=27916
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3097
     Region          30..190
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     CDS             1..284
                     /gene="NRXN1"
                     /gene_synonym="Hs.22998; PTHSL2; SCZD17"
                     /coded_by="NM_001330089.2:1074..1928"
                     /note="isoform 8 precursor is encoded by transcript
                     variant 8"
                     /db_xref="GeneID:9378"
                     /db_xref="HGNC:HGNC:8008"
                     /db_xref="MIM:600565"
ORIGIN      
        1 mgtallqrgg cfllclslll lgcwaelgsg lefpgaegqw trfpkwnacc esemsfqlkt
       61 rsarglvlyf ddegfcdfle liltrggrlq lsfsifcaep atlladtpvn dgawhsvrir
      121 rqfrnttlfi dqveakwvev kskrrdmtvf sglfvgglpp elraaalklt lasvrerepf
      181 kgwirdvrvn ssqvlpvdsg evklddeppn sgggspceag eegeggvcln ggvcsvvddq
      241 avcdcsrtgf rgkdcsqgla hlmmgdqgmg svpfplcfqc flvl
//
LOCUS       NP_001167618             402 aa            linear   PRI 21-NOV-2025
DEFINITION  LIM homeobox transcription factor 1-beta isoform 2 [Homo sapiens].
ACCESSION   NP_001167618
VERSION     NP_001167618.1
DBSOURCE    REFSEQ: accession NM_001174147.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Chen,C., Kong,D., Wang,P., Li,M. and Gui,R.
  TITLE     Genetic polymorphisms of LMX1B and MLXIP are associated with hip
            osteoarthritis in the Chinese population
  JOURNAL   Biomark Med 18 (15-16), 695-702 (2024)
   PUBMED   39263770
  REMARK    GeneRIF: Genetic polymorphisms of LMX1B and MLXIP are associated
            with hip osteoarthritis in the Chinese population.
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Francis,D., Lall,P., Ayres,S., Van Bergen,N.J., Christodoulou,J.,
            Brown,N.J. and Kalitsis,P.
  TITLE     De novo enhancer deletion of LMX1B produces a mild nail-patella
            clinical phenotype
  JOURNAL   Clin Genet 105 (2), 214-219 (2024)
   PUBMED   37899549
  REMARK    GeneRIF: De novo enhancer deletion of LMX1B produces a mild
            nail-patella clinical phenotype.
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Jimenez-Moreno,N., Kollareddy,M., Stathakos,P., Moss,J.J.,
            Anton,Z., Shoemark,D.K., Sessions,R.B., Witzgall,R., Caldwell,M.
            and Lane,J.D.
  TITLE     ATG8-dependent LMX1B-autophagy crosstalk shapes human midbrain
            dopaminergic neuronal resilience
  JOURNAL   J Cell Biol 222 (5) (2023)
   PUBMED   37014324
  REMARK    GeneRIF: ATG8-dependent LMX1B-autophagy crosstalk shapes human
            midbrain dopaminergic neuronal resilience.
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Dunston,J.A., Hamlington,J.D., Zaveri,J., Sweeney,E., Sibbring,J.,
            Tran,C., Malbroux,M., O'Neill,J.P., Mountford,R. and McIntosh,I.
  TITLE     The human LMX1B gene: transcription unit, promoter, and pathogenic
            mutations
  JOURNAL   Genomics 84 (3), 565-576 (2004)
   PUBMED   15498463
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Chen,H., Lun,Y., Ovchinnikov,D., Kokubo,H., Oberg,K.C.,
            Pepicelli,C.V., Gan,L., Lee,B. and Johnson,R.L.
  TITLE     Limb and kidney defects in Lmx1b mutant mice suggest an involvement
            of LMX1B in human nail patella syndrome
  JOURNAL   Nat Genet 19 (1), 51-55 (1998)
   PUBMED   9590288
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Dreyer,S.D., Zhou,G., Baldini,A., Winterpacht,A., Zabel,B.,
            Cole,W., Johnson,R.L. and Lee,B.
  TITLE     Mutations in LMX1B cause abnormal skeletal patterning and renal
            dysplasia in nail patella syndrome
  JOURNAL   Nat Genet 19 (1), 47-50 (1998)
   PUBMED   9590287
REFERENCE   8  (residues 1 to 402)
  AUTHORS   Iannotti,C.A., Inoue,H., Bernal,E., Aoki,M., Liu,L.,
            Donis-Keller,H., German,M.S. and Permutt,M.A.
  TITLE     Identification of a human LMX1 (LMX1.1)-related gene, LMX1.2:
            tissue-specific expression and linkage mapping on chromosome 9
  JOURNAL   Genomics 46 (3), 520-524 (1997)
   PUBMED   9441763
REFERENCE   9  (residues 1 to 402)
  AUTHORS   Johnson,J.D., Zhang,W., Rudnick,A., Rutter,W.J. and German,M.S.
  TITLE     Transcriptional synergy between LIM-homeodomain proteins and basic
            helix-loop-helix proteins: the LIM2 domain determines specificity
  JOURNAL   Mol Cell Biol 17 (7), 3488-3496 (1997)
   PUBMED   9199284
REFERENCE   10 (residues 1 to 402)
  AUTHORS   Sweeney,E., Hoover-Fong,J.E. and McIntosh,I.
  TITLE     Nail-Patella Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301311
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL161908.13, BC113491.1,
            BC069588.1, AL161731.20 and EL952935.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of LIM-homeodomain family of
            proteins containing two N-terminal zinc-binding LIM domains, 1
            homeodomain, and a C-terminal glutamine-rich domain. It functions
            as a transcription factor, and is essential for the normal
            development of dorsal limb structures, the glomerular basement
            membrane, the anterior segment of the eye, and dopaminergic and
            serotonergic neurons. Mutations in this gene are associated with
            nail-patella syndrome. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Mar 2010].
            
            Transcript Variant: This variant (2) uses an alternate donor splice
            site at the penultimate coding exon compared to variant 1,
            resulting in a longer isoform (2) containing an additional 7 aa
            protein segment compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3310587.1,
                                           SRR14038194.804166.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373474.9/ ENSP00000362573.3
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..402
                     /product="LIM homeobox transcription factor 1-beta isoform
                     2"
                     /note="LMX-1.2; LIM/homeobox protein 1.2"
                     /calculated_mol_wt=44786
     Region          56..108
                     /region_name="LIM1_Lmx1b"
                     /note="The first LIM domain of Lmx1b; cd09371"
                     /db_xref="CDD:188757"
     Site            order(56,59,77,80,83,86,103,106)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188757"
     Region          115..169
                     /region_name="LIM2_Lmx1a_Lmx1b"
                     /note="The second LIM domain of Lmx1a and Lmx1b; cd09378"
                     /db_xref="CDD:188764"
     Site            order(115,118,137,140,143,146,165,168)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188764"
     Region          176..229
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60663.3)"
     Region          220..276
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          326..346
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60663.3)"
     CDS             1..402
                     /gene="LMX1B"
                     /gene_synonym="FSGS10; LMX1.2; NPS1"
                     /coded_by="NM_001174147.2:523..1731"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55342.1"
                     /db_xref="GeneID:4010"
                     /db_xref="HGNC:HGNC:6654"
                     /db_xref="MIM:602575"
ORIGIN      
        1 mdiatgpesl ercfprgqtd cakmldgikm eehalrpgpa tlgvllgsdc phpavcegcq
       61 rpisdrflmr vnesswheec lqcaacqqal ttscyfrdrk lyckqdyqql faakcsgcme
      121 kiaptefvmr alecvyhlgc fcccvcerql rkgdefvlke gqllckgdye kekdllssvs
      181 pdesdsvkse dedgdmkpak gqgsqskgsg ddgkdprrpk rprtilttqq rrafkasfev
      241 sskpcrkvre tlaaetglsv rvvqvwfqnq rakmkklarr hqqqqeqqns qrlgqevlss
      301 rmegmmasyt plappqqqiv ameqspygss dpfqqgltpp qmpgdhmnpy gndsifhdid
      361 sdtsltslsd cflgssdvgs lqarvgnpid rlysmqssyf as
//
LOCUS       NP_001306168             810 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger CCCH domain-containing protein 11A isoform 1 [Homo
            sapiens].
ACCESSION   NP_001306168
VERSION     NP_001306168.1
DBSOURCE    REFSEQ: accession NM_001319239.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Kases,K., Schubert,E., Hajikhezri,Z., Larsson,M., Devi,P.,
            Darweesh,M., Andersson,L., Akusjarvi,G., Punga,T. and Younis,S.
  TITLE     The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts
  JOURNAL   J Biol Chem 299 (8), 104959 (2023)
   PUBMED   37356722
  REMARK    GeneRIF: The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts.
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 810)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 810)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114402.2.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1-7 encode the same protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC038513.2, SRR1660803.122512.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..810
                     /product="zinc finger CCCH domain-containing protein 11A
                     isoform 1"
                     /note="zinc finger CCCH-type domain containing 11A; zinc
                     finger CCCH domain-containing protein 11A"
                     /calculated_mol_wt=89000
     Region          1..110
                     /region_name="zf-CCCH_3"
                     /note="Zinc-finger containing family; pfam15663"
                     /db_xref="CDD:464787"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          139..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          223..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          285..351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          367..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          482..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          715..768
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     CDS             1..810
                     /gene="ZC3H11A"
                     /gene_synonym="ZC3HDC11A"
                     /coded_by="NM_001319239.2:941..3373"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS30978.1"
                     /db_xref="GeneID:9877"
                     /db_xref="HGNC:HGNC:29093"
                     /db_xref="MIM:613513"
ORIGIN      
        1 mpnqgedcyf ffystctkgd scpfrhceaa ignetvctlw qegrcfrqvc rfrhmeidkk
       61 rseipcywen qptgcqklnc afhhnrgryv dglflppskt vlptvpespe eevkasqlsv
      121 qqnklsvqsn pspqlrsvmk vessenvpsp thppvvinaa dddeddddqf seegdetktp
      181 tlqptpevhn glrvtsvrkp avnikqgecl nfgiktleei kskkmkeksk kqgegssgvs
      241 slllhpepvp gpekenvrtv vrtvtlstkq geeplvrlsl terlgkrkfs aggdsdpplk
      301 rslaqrlgkk veapetnidk tpkkaqvsks lkerlgmsad pdnedatdkv nkvgeihvkt
      361 leeilleras qkrgelqtkl ktegpsktdd stsgarssst iriktfsevl aekkhrqqea
      421 erqkskkdtt ciklkidsei kktvvlppiv asrgqseepa gktksmqevh iktleeikle
      481 kalrvqqsse sstsspsqhe atpgarrllr itkrtgmkee knlqegnevd sqssirteak
      541 easgettgvd itkiqvkrce tmrekhmqkq qereksvltp lrgdvascnt qvaekpvlta
      601 vpgitrhltk rlptkssqkv evetsgigds llnvkcaaqt lekrgkakpk vnvkpsvvkv
      661 vsspklapkr kavemhaavi aavkplssss vlqeppakka avavvplvse dksvtvpeae
      721 nprdslvlpp tqsssdsspp evsgpsssqm smktrrlssa stgkpplsve ddfekliwei
      781 sggkleaeid ldpgkdeddl llelsemids
//
LOCUS       NP_958923                374 aa            linear   PRI 21-NOV-2025
DEFINITION  periphilin-1 isoform 2 [Homo sapiens].
ACCESSION   NP_958923
VERSION     NP_958923.1
DBSOURCE    REFSEQ: accession NM_201515.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Bloor,S., Wit,N. and Lehner,P.J.
  TITLE     RNA binding by Periphilin plays an essential role in initiating
            silencing by the HUSH complex
  JOURNAL   Nucleic Acids Res 53 (2) (2025)
   PUBMED   39658355
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Jensvold,Z.D., Flood,J.R., Christenson,A.E. and Lewis,P.W.
  TITLE     Interplay between Two Paralogous Human Silencing Hub (HuSH)
            Complexes in Regulating LINE-1 Element Silencing
  JOURNAL   Nat Commun 15 (1), 9492 (2024)
   PUBMED   39489739
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Tunbak,H., Enriquez-Gasca,R., Tie,C.H.C., Gould,P.A., Mlcochova,P.,
            Gupta,R.K., Fernandes,L., Holt,J., van der Veen,A.G.,
            Giampazolias,E., Burns,K.H., Maillard,P.V. and Rowe,H.M.
  TITLE     The HUSH complex is a gatekeeper of type I interferon through
            epigenetic regulation of LINE-1s
  JOURNAL   Nat Commun 11 (1), 5387 (2020)
   PUBMED   33144593
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Prigozhin,D.M., Douse,C.H., Farleigh,L.E., Albecka,A.,
            Tchasovnikarova,I.A., Timms,R.T., Oda,S.I., Adolf,F.,
            Freund,S.M.V., Maslen,S., Lehner,P.J. and Modis,Y.
  TITLE     Periphilin self-association underpins epigenetic silencing by the
            HUSH complex
  JOURNAL   Nucleic Acids Res 48 (18), 10313-10328 (2020)
   PUBMED   32976585
  REMARK    GeneRIF: Periphilin self-association underpins epigenetic silencing
            by the HUSH complex.
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Kurita,M., Suzuki,H., Masai,H., Mizumoto,K., Ogata,E.,
            Nishimoto,I., Aiso,S. and Matsuoka,M.
  TITLE     Overexpression of CR/periphilin downregulates Cdc7 expression and
            induces S-phase arrest
  JOURNAL   Biochem Biophys Res Commun 324 (2), 554-561 (2004)
   PUBMED   15474462
  REMARK    GeneRIF: CR (periphilin) retards S-phase progression by modifying
            expression of Cdc7 and other genes involved in progression of DNA
            replication
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Goehler,H., Lalowski,M., Stelzl,U., Waelter,S., Stroedicke,M.,
            Worm,U., Droege,A., Lindenberg,K.S., Knoblich,M., Haenig,C.,
            Herbst,M., Suopanki,J., Scherzinger,E., Abraham,C., Bauer,B.,
            Hasenbank,R., Fritzsche,A., Ludewig,A.H., Bussow,K., Coleman,S.H.,
            Gutekunst,C.A., Landwehrmeyer,B.G., Lehrach,H. and Wanker,E.E.
  TITLE     A protein interaction network links GIT1, an enhancer of huntingtin
            aggregation, to Huntington's disease
  JOURNAL   Mol Cell 15 (6), 853-865 (2004)
   PUBMED   15383276
  REMARK    Erratum:[Mol Cell. 2005 Jul 22;19(2):287. Buessow, Konrad
            [corrected to Bussow, Konrad]]
REFERENCE   8  (residues 1 to 374)
  AUTHORS   Kazerounian,S. and Aho,S.
  TITLE     Characterization of periphilin, a widespread, highly insoluble
            nuclear protein and potential constituent of the keratinocyte
            cornified envelope
  JOURNAL   J Biol Chem 278 (38), 36707-36717 (2003)
   PUBMED   12853457
  REMARK    GeneRIF: periphilin is potentially involved in epithelial
            differentiation and contributes to epidermal integrity and barrier
            formation
REFERENCE   9  (residues 1 to 374)
  AUTHORS   Kazerounian,S., Uitto,J. and Aho,S.
  TITLE     Unique role for the periplakin tail in intermediate filament
            association: specific binding to keratin 8 and vimentin
  JOURNAL   Exp Dermatol 11 (5), 428-438 (2002)
   PUBMED   12366696
REFERENCE   10 (residues 1 to 374)
  AUTHORS   Line,A., Stengrevics,A., Slucka,Z., Li,G., Jankevics,E. and
            Rees,R.C.
  TITLE     Serological identification and expression analysis of gastric
            cancer-associated genes
  JOURNAL   Br J Cancer 86 (11), 1824-1830 (2002)
   PUBMED   12087473
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK129910.1, CA444170.1 and
            AC079601.25.
            
            Summary: The protein encoded by this gene is one of the several
            proteins that become sequentially incorporated into the cornified
            cell envelope during the terminal differentiation of keratinocyte
            at the outer layers of epidermis. This protein interacts with
            periplakin, which is known as a precursor of the cornified cell
            envelope. The cellular localization pattern and insolubility of
            this protein suggest that it may play a role in epithelial
            differentiation and contribute to epidermal integrity and barrier
            formation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (2) has an additional exon in the
            5' region and has multiple differences in the 3' region when
            compared to variant 1. The resulting isoform (2) has a longer
            N-terminus and a distinct and shorter C-terminus, as compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY157850.1, AK129910.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..374
                     /product="periphilin-1 isoform 2"
                     /note="gastric cancer antigen Ga50; CDC7 expression
                     repressor"
                     /calculated_mol_wt=43266
     Region          292..364
                     /region_name="periphilin-like"
                     /note="Vertebrate periphilin-1 and similar proteins;
                     cd22896"
                     /db_xref="CDD:439377"
     Site            order(297,301..302,305,308..309,312..313,316..317,320,338,
                     341..342,345..346,349..350,352..353,356..357,360)
                     /site_type="other"
                     /note="heterotrimer interface [polypeptide binding]"
                     /db_xref="CDD:439377"
     CDS             1..374
                     /gene="PPHLN1"
                     /gene_synonym="CR; HSPC206; HSPC232"
                     /coded_by="NM_201515.2:106..1230"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS41773.1"
                     /db_xref="GeneID:51535"
                     /db_xref="HGNC:HGNC:19369"
                     /db_xref="MIM:608150"
ORIGIN      
        1 mayrrdemws egryeyerip rerapprshp sdgynrlvni vpkkpplldr pgegsynryy
       61 shvdyrdyde grsfshdrrs gpphrgdesg yrwtrddhsa srqpeyrdmr dgfrrksfys
      121 shyarerspy krdntffres pvgrkdsphs rsgssvssrs yspersksys fhqsqhrksv
      181 rpgasykrqn egnperdker pvqslktsrd tspssgsavs sskvldkpsr ltekelaeaa
      241 skwaaeklek sdesnlpeis eyeagstapl ftdqpeepes ntthgielfe dsqlttrska
      301 iasktkeieq vyrqdcetfg mvvkmliekd psleksiqfa lrqnlheige rcveelkhfi
      361 aeydtstqdf gepf
//
LOCUS       NP_000651                390 aa            linear   PRI 21-NOV-2025
DEFINITION  transforming growth factor beta-1 proprotein preproprotein [Homo
            sapiens].
ACCESSION   NP_000651
VERSION     NP_000651.3
DBSOURCE    REFSEQ: accession NM_000660.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Fu,Y., Sun,X., He,Q., Gu,Z., Jia,X. and Zhuang,Z.
  TITLE     Connexin 43 controls metastatic behavior in triple negative breast
            cancer through TGFbeta1-Smad3-intergin alphaV signaling axis Based
            on optical image diagnosis
  JOURNAL   SLAS Technol 29 (5), 100190 (2024)
   PUBMED   39299505
  REMARK    GeneRIF: Connexin 43 controls metastatic behavior in triple
            negative breast cancer through TGFbeta1-Smad3-intergin alphaV
            signaling axis Based on optical image diagnosis.
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Dubois,C.M., Laprise,M.H., Blanchette,F., Gentry,L.E. and Leduc,R.
  TITLE     Processing of transforming growth factor beta 1 precursor by human
            furin convertase
  JOURNAL   J Biol Chem 270 (18), 10618-10624 (1995)
   PUBMED   7737999
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Wallace,S.E. and Wilcox,W.R.
  TITLE     Camurati-Engelmann Disease
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301335
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Zauli,G., Davis,B.R., Re,M.C., Visani,G., Furlini,G. and La
            Placa,M.
  TITLE     tat protein stimulates production of transforming growth
            factor-beta 1 by marrow macrophages: a potential mechanism for
            human immunodeficiency virus-1-induced hematopoietic suppression
  JOURNAL   Blood 80 (12), 3036-3043 (1992)
   PUBMED   1281686
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Cheifetz,S., Bellon,T., Cales,C., Vera,S., Bernabeu,C., Massague,J.
            and Letarte,M.
  TITLE     Endoglin is a component of the transforming growth factor-beta
            receptor system in human endothelial cells
  JOURNAL   J Biol Chem 267 (27), 19027-19030 (1992)
   PUBMED   1326540
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Kim,S.J., Glick,A., Sporn,M.B. and Roberts,A.B.
  TITLE     Characterization of the promoter region of the human transforming
            growth factor-beta 1 gene
  JOURNAL   J Biol Chem 264 (1), 402-408 (1989)
   PUBMED   2909528
REFERENCE   8  (residues 1 to 390)
  AUTHORS   Miyazono,K., Hellman,U., Wernstedt,C. and Heldin,C.H.
  TITLE     Latent high molecular weight complex of transforming growth factor
            beta 1. Purification from human platelets and structural
            characterization
  JOURNAL   J Biol Chem 263 (13), 6407-6415 (1988)
   PUBMED   3162913
REFERENCE   9  (residues 1 to 390)
  AUTHORS   Derynck,R., Rhee,L., Chen,E.Y. and Van Tilburg,A.
  TITLE     Intron-exon structure of the human transforming growth factor-beta
            precursor gene
  JOURNAL   Nucleic Acids Res 15 (7), 3188-3189 (1987)
   PUBMED   3470709
REFERENCE   10 (residues 1 to 390)
  AUTHORS   Derynck,R., Jarrett,J.A., Chen,E.Y., Eaton,D.H., Bell,J.R.,
            Assoian,R.K., Roberts,A.B., Sporn,M.B. and Goeddel,D.V.
  TITLE     Human transforming growth factor-beta complementary DNA sequence
            and expression in normal and transformed cells
  JOURNAL   Nature 316 (6030), 701-705 (1985)
   PUBMED   3861940
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011462.4, X02812.1,
            BC000125.1 and BM692012.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 4, 2005 this sequence version replaced NP_000651.2.
            
            Summary: This gene encodes a secreted ligand of the TGF-beta
            (transforming growth factor-beta) superfamily of proteins. Ligands
            of this family bind various TGF-beta receptors leading to
            recruitment and activation of SMAD family transcription factors
            that regulate gene expression. The encoded preproprotein is
            proteolytically processed to generate a latency-associated peptide
            (LAP) and a mature peptide, and is found in either a latent form
            composed of a mature peptide homodimer, a LAP homodimer, and a
            latent TGF-beta binding protein, or in an active form consisting
            solely of the mature peptide homodimer. The mature peptide may also
            form heterodimers with other TGFB family members. This encoded
            protein regulates cell proliferation, differentiation and growth,
            and can modulate expression and activation of other growth factors
            including interferon gamma and tumor necrosis factor alpha. This
            gene is frequently upregulated in tumor cells, and mutations in
            this gene result in Camurati-Engelmann disease. [provided by
            RefSeq, Aug 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X02812.1, SRR3476690.819241.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221930.6/ ENSP00000221930.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..390
                     /product="transforming growth factor beta-1 proprotein
                     preproprotein"
                     /note="prepro-transforming growth factor beta-1;
                     latency-associated peptide; TGF-beta-1; transforming
                     growth factor beta-1 proprotein; transforming growth
                     factor beta1"
                     /calculated_mol_wt=41267
     sig_peptide     1..29
                     /note="/evidence=ECO:0000269|PubMed:3162913; propagated
                     from UniProtKB/Swiss-Prot (P01137.3)"
                     /calculated_mol_wt=3076
     mat_peptide     30..278
                     /product="Latency-associated peptide.
                     /evidence=ECO:0000305|PubMed:2982829,
                     ECO:0000305|PubMed:3162913, ECO:0000305|PubMed:7737999,
                     ECO:0000305|PubMed:8471846. /id=PRO_0000033762"
                     /note="propagated from UniProtKB/Swiss-Prot (P01137.3)"
                     /calculated_mol_wt=28491
     Region          30..261
                     /region_name="TGFb_propeptide"
                     /note="TGF-beta propeptide; pfam00688"
                     /db_xref="CDD:459906"
     Region          30..74
                     /region_name="Straightjacket domain.
                     /evidence=ECO:0000250|UniProtKB:P07200"
                     /note="propagated from UniProtKB/Swiss-Prot (P01137.3)"
     Region          75..271
                     /region_name="Arm domain.
                     /evidence=ECO:0000250|UniProtKB:P07200"
                     /note="propagated from UniProtKB/Swiss-Prot (P01137.3)"
     Site            82
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16263699,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:28117447,
                     ECO:0007744|PDB:5FFO; propagated from UniProtKB/Swiss-Prot
                     (P01137.3)"
     Site            136
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P01137.3)"
     Site            176
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P01137.3)"
     Region          226..252
                     /region_name="Bowtie tail.
                     /evidence=ECO:0000269|PubMed:28117447"
                     /note="propagated from UniProtKB/Swiss-Prot (P01137.3)"
     Region          244..246
                     /region_name="Cell attachment site.
                     /evidence=ECO:0000269|PubMed:28117447"
                     /note="propagated from UniProtKB/Swiss-Prot (P01137.3)"
     Site            278..279
                     /site_type="cleavage"
                     /experiment="EXISTENCE:Western blot evidence
                     [ECO:0000112][PMID:7737999]"
                     /note="cleavage by furin"
     mat_peptide     279..390
                     /product="Transforming growth factor beta-1.
                     /evidence=ECO:0000305|PubMed:2982829,
                     ECO:0000305|PubMed:3162913, ECO:0000305|PubMed:7737999,
                     ECO:0000305|PubMed:8471846. /id=PRO_0000033763"
                     /note="propagated from UniProtKB/Swiss-Prot (P01137.3)"
                     /calculated_mol_wt=12795
     Region          292..390
                     /region_name="TGF_beta_TGFB1"
                     /note="transforming growth factor beta (TGF-beta) like
                     domain found in transforming growth factor beta-1
                     (TGF-beta-1) and similar proteins; cd19384"
                     /db_xref="CDD:381654"
     Site            order(298..300,302,304..306,308,317,319..323,334..336,
                     338..340,342..343,346..347,351..353,355..358,361,379..384,
                     390)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381654"
     CDS             1..390
                     /gene="TGFB1"
                     /gene_synonym="CAEND1; CED; DPD1; IBDIMDE; LAP; TGF-beta1;
                     TGFB; TGFbeta"
                     /coded_by="NM_000660.7:879..2051"
                     /db_xref="CCDS:CCDS33031.1"
                     /db_xref="GeneID:7040"
                     /db_xref="HGNC:HGNC:11766"
                     /db_xref="MIM:190180"
ORIGIN      
        1 mppsglrllp lllpllwllv ltpgrpaagl stcktidmel vkrkrieair gqilsklrla
       61 sppsqgevpp gplpeavlal ynstrdrvag esaepepepe adyyakevtr vlmvethnei
      121 ydkfkqsths iymffntsel reavpepvll sraelrllrl klkveqhvel yqkysnnswr
      181 ylsnrllaps dspewlsfdv tgvvrqwlsr ggeiegfrls ahcscdsrdn tlqvdingft
      241 tgrrgdlati hgmnrpflll matpleraqh lqssrhrral dtnycfsste knccvrqlyi
      301 dfrkdlgwkw ihepkgyhan fclgpcpyiw sldtqyskvl alynqhnpga saapccvpqa
      361 leplpivyyv grkpkveqls nmivrsckcs
//
LOCUS       NP_001378855            1844 aa            linear   PRI 21-NOV-2025
DEFINITION  Golgi-specific brefeldin A-resistance guanine nucleotide exchange
            factor 1 isoform 10 [Homo sapiens].
ACCESSION   NP_001378855
VERSION     NP_001378855.1
DBSOURCE    REFSEQ: accession NM_001391926.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1844)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1844)
  AUTHORS   Hirano,J., Hayashi,T., Kitamura,K., Nishimura,Y., Shimizu,H.,
            Okamoto,T., Okada,K., Uemura,K., Yeh,M.T., Ono,C., Taguwa,S.,
            Muramatsu,M. and Matsuura,Y.
  TITLE     Enterovirus 3A protein disrupts endoplasmic reticulum homeostasis
            through interaction with GBF1
  JOURNAL   J Virol 98 (7), e0081324 (2024)
   PUBMED   38904364
  REMARK    GeneRIF: Enterovirus 3A protein disrupts endoplasmic reticulum
            homeostasis through interaction with GBF1.
REFERENCE   3  (residues 1 to 1844)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1844)
  AUTHORS   Navare,A.T., Mast,F.D., Olivier,J.P., Bertomeu,T., Neal,M.L.,
            Carpp,L.N., Kaushansky,A., Coulombe-Huntington,J., Tyers,M. and
            Aitchison,J.D.
  TITLE     Viral protein engagement of GBF1 induces host cell vulnerability
            through synthetic lethality
  JOURNAL   J Cell Biol 221 (11) (2022)
   PUBMED   36305789
  REMARK    GeneRIF: Viral protein engagement of GBF1 induces host cell
            vulnerability through synthetic lethality.
REFERENCE   5  (residues 1 to 1844)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1844)
  AUTHORS   Garcia-Mata,R. and Sztul,E.
  TITLE     The membrane-tethering protein p115 interacts with GBF1, an ARF
            guanine-nucleotide-exchange factor
  JOURNAL   EMBO Rep 4 (3), 320-325 (2003)
   PUBMED   12634853
  REMARK    GeneRIF: novel interaction between p115 and Golgi-specific
            brefeldin-A-resistant factor 1 (GBF1)
REFERENCE   7  (residues 1 to 1844)
  AUTHORS   Kawamoto,K., Yoshida,Y., Tamaki,H., Torii,S., Shinotsuka,C.,
            Yamashina,S. and Nakayama,K.
  TITLE     GBF1, a guanine nucleotide exchange factor for ADP-ribosylation
            factors, is localized to the cis-Golgi and involved in membrane
            association of the COPI coat
  JOURNAL   Traffic 3 (7), 483-495 (2002)
   PUBMED   12047556
  REMARK    GeneRIF: detailed subcellular localization to the cis-Golgi
REFERENCE   8  (residues 1 to 1844)
  AUTHORS   Verhoeven,K., Villanova,M., Rossi,A., Malandrini,A., De Jonghe,P.
            and Timmerman,V.
  TITLE     Localization of the gene for the intermediate form of
            Charcot-Marie-Tooth to chromosome 10q24.1-q25.1
  JOURNAL   Am J Hum Genet 69 (4), 889-894 (2001)
   PUBMED   11533914
REFERENCE   9  (residues 1 to 1844)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   10 (residues 1 to 1844)
  AUTHORS   Mansour,S.J., Herbrick,J.A., Scherer,S.W. and Melancon,P.
  TITLE     Human GBF1 is a ubiquitously expressed gene of the sec7 domain
            family mapping to 10q24
  JOURNAL   Genomics 54 (2), 323-327 (1998)
   PUBMED   9828135
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160011.35, AL356420.14 and
            AL121928.13.
            
            Summary: This gene encodes a member of the Sec7 domain family. The
            encoded protein is a guanine nucleotide exchange factor that
            regulates the recruitment of proteins to membranes by mediating GDP
            to GTP exchange. The encoded protein is localized to the Golgi
            apparatus and plays a role in vesicular trafficking by activating
            ADP ribosylation factor 1. The encoded protein has also been
            identified as an important host factor for viral replication.
            Multiple transcript variants have been observed for this gene.
            [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3041382.1,
                                           SRR14038191.2086303.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1844
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..1844
                     /product="Golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1 isoform 10"
                     /note="golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1; BFA-resistant GEF 1"
                     /calculated_mol_wt=204725
     Region          1..381
                     /region_name="Interaction with RAB1B.
                     /evidence=ECO:0000269|PubMed:17429068"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1..211
                     /region_name="DCB, DCB:DCB domain and DCB:HUS domain
                     interaction. /evidence=ECO:0000250|UniProtKB:Q9R1D7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          215..266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          281..372
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          <430..>1167
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          531..551
                     /region_name="HUS, DCB:HUS domain interaction.
                     /evidence=ECO:0000250|UniProtKB:Q9R1D7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            651
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          688..873
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          875..1359
                     /region_name="Phosphatidylinositol-phosphate binding,
                     required for translocation to the leading edge and for
                     ARF1 activation upon GPCR signaling.
                     /evidence=ECO:0000269|PubMed:22573891"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1273..1324
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1305
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1326
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AMPK.
                     /evidence=ECO:0000269|PubMed:18063581; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1339..1359
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1419..1472
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1710..1793
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1769
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          <1779..1842
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1844
                     /gene="GBF1"
                     /gene_synonym="ARF1GEF; CMT2GG; CMTDI2; CMTDIA"
                     /coded_by="NM_001391926.1:261..5795"
                     /note="isoform 10 is encoded by transcript variant 18"
                     /db_xref="GeneID:8729"
                     /db_xref="HGNC:HGNC:4181"
                     /db_xref="MIM:603698"
ORIGIN      
        1 mvdkniyiiq geinivvgai krnarwstht pldeerdpll hsfghlkevl nsitelseie
       61 pnvflrpfle virsedttgp itglaltsvn kflsyalidp thegtaegme nmadavthar
      121 fvgtdpasde vvlmkilqvl rtllltpvga hltnesvcei mqscfricfe mrlsellrks
      181 aehtlvdmvq llftrlpqfk eepknyvgtn mkklkmragg msdsskwkkq krsprpprhm
      241 tkvtpgselp tpngttlssn ltggmpfidv ptpissasse aasavvspst dsglefssqt
      301 tskedltdle qpgspgysta tepgsselgv peqpdlqqeg thveksqsas vesipevlee
      361 ctspadhsds asvhdmdyvn prgvrftqss qkegtalvpy glpcirelfr flisltnphd
      421 rhnsevmihm glhlltvale sapvaqcqtl lglikdemcr hlfqllsier lnlyaaslrv
      481 cfllfesmre hlkfqmemyi kklmeiitve npkmpyemke maleaivqlw ripsfvtely
      541 inydcdyycs nlfeeltkll sknafpvsgq lytthllsld alltvidste ahcqakvlns
      601 ltqqekketa rpssertasd gkavgmasdi pglhlpgggr lppehgksgc sdleeavdsg
      661 adkkfarkpp rfscllpdpr elieiknkkk llitgteqfn qkpkkgiqfl qekglltipm
      721 dntevaqwlr enprldkkmi gefvsdrkni dllesfvstf sfqglrldea lrlyleafrl
      781 pgeapviqrl leafterwmn cngspfansd acfslayavi mlntdqhnhn vrkqnapmtl
      841 eefrknlkgv nggkdfeqdi ledmyhaikn eeivmpeeqt glvrenyvwn vllhrgatpe
      901 giflrvptas ydldlftmtw gptiaalsyv fdksleetii qkaisgfrkc amisahygls
      961 dvfdnliisl ckftalsses ienlpsvfgs npkahiaakt vfhlahrhgd ilregwknim
     1021 eamlqlfraq llpkamieve dfvdpngkis lqreetpsnr gestvlsfvs wltlsgpeqs
     1081 svrgpstenq eakrvaleci kqcdpekmit eskflqlesl qelmkalvsv tpdeetydee
     1141 daafclemll rivlenrdrv gcvwqtvrdh lyhlcvqaqd fcflveravv gllrlairll
     1201 rreeisaqvl lslrilllmk psvlsrvshq vayglhellk tnaanihsgd dwatlftlle
     1261 cigsgvkppa alqatarada pdagaqsdse lpsyhqndvs ldrgytsdse vytdhgrpgk
     1321 ihrsatdadv vnsgwlvvgk ddvdnskpgp srpgpsplin qysltvgldl gphdtksllk
     1381 cveslsfivr daahitpdnf elcvktlrif veaslnggck sqekrgkshk ydskgnrfkk
     1441 kskegsmlrr prtssqhasr ggqsdddede gvpasyhtvs lqlldlmhtl htraasiyss
     1501 waeeqrhlet ggqkieadsr tlwahcwcpl lqgiaclccd arrqvrmqal tylqrallvh
     1561 dlqkldalew escfnkvlfp lltkllenis padvggmeet rmrastllsk vflqhlspll
     1621 slstfaalwl tildfmdkym hagssdllse aipeslknml lvmdtaeifh sadargggps
     1681 alweitweri dcflphlrde lfkqtviqdp mpmepqgqkp lasahltsaa gdtrtpghpp
     1741 ppeipselga cdfekpespr aasssspgsp vasspsrlsp tpdgppplaq pplilqplas
     1801 plqvgvppmt lpiilnpali eatspvplla tprptdpipt sevn
//
LOCUS       NP_002664               2135 aa            linear   PRI 21-NOV-2025
DEFINITION  plexin-B1 precursor [Homo sapiens].
ACCESSION   NP_002664
VERSION     NP_002664.2
DBSOURCE    REFSEQ: accession NM_002673.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2135)
  AUTHORS   Xuan,Z., Zhang,Y., Li,D., Wang,K., Huang,P. and Shi,J.
  TITLE     PLXNB1/SEMA4D signals mediate interactions between malignant
            epithelial and immune cells to promote colorectal cancer liver
            metastasis
  JOURNAL   J Cell Mol Med 28 (20), e70142 (2024)
   PUBMED   39443302
  REMARK    GeneRIF: PLXNB1/SEMA4D signals mediate interactions between
            malignant epithelial and immune cells to promote colorectal cancer
            liver metastasis.
REFERENCE   2  (residues 1 to 2135)
  AUTHORS   Wei,X., Liu,Z., Shen,Y., Dong,H., Chen,K., Shi,X., Chen,Y., Wang,B.
            and Dong,S.
  TITLE     Semaphorin4A promotes lung cancer by activation of NF-kappaB
            pathway mediated by PlexinB1
  JOURNAL   PeerJ 11, e16292 (2023)
   PUBMED   37901456
  REMARK    GeneRIF: Semaphorin4A promotes lung cancer by activation of
            NF-kappaB pathway mediated by PlexinB1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2135)
  AUTHORS   Yang,G., Ullah,H.M.A., Parker,E., Gorsi,B., Libowitz,M.,
            Maguire,C., King,J.B., Coon,H., Lopez-Larson,M., Anderson,J.S.,
            Yandell,M. and Shcheglovitov,A.
  TITLE     Neurite outgrowth deficits caused by rare PLXNB1 mutation in
            pediatric bipolar disorder
  JOURNAL   Mol Psychiatry 28 (6), 2525-2539 (2023)
   PUBMED   37032361
  REMARK    GeneRIF: Neurite outgrowth deficits caused by rare PLXNB1 mutation
            in pediatric bipolar disorder.
REFERENCE   4  (residues 1 to 2135)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2135)
  AUTHORS   Welch,B.A., Cho,H.J., Ucakturk,S.A., Farmer,S.M., Cetinkaya,S.,
            Abaci,A., Akkus,G., Simsek,E., Kotan,L.D., Turan,I., Gurbuz,F.,
            Yuksel,B., Wray,S. and Topaloglu,A.K.
  TITLE     PLXNB1 mutations in the etiology of idiopathic hypogonadotropic
            hypogonadism
  JOURNAL   J Neuroendocrinol 34 (4), e13103 (2022)
   PUBMED   35170806
  REMARK    GeneRIF: PLXNB1 mutations in the etiology of idiopathic
            hypogonadotropic hypogonadism.
REFERENCE   6  (residues 1 to 2135)
  AUTHORS   Swiercz,J.M., Kuner,R., Behrens,J. and Offermanns,S.
  TITLE     Plexin-B1 directly interacts with PDZ-RhoGEF/LARG to regulate RhoA
            and growth cone morphology
  JOURNAL   Neuron 35 (1), 51-63 (2002)
   PUBMED   12123608
REFERENCE   7  (residues 1 to 2135)
  AUTHORS   Vikis,H.G., Li,W. and Guan,K.L.
  TITLE     The plexin-B1/Rac interaction inhibits PAK activation and enhances
            Sema4D ligand binding
  JOURNAL   Genes Dev 16 (7), 836-845 (2002)
   PUBMED   11937491
  REMARK    GeneRIF: The plexin-B1/Rac interaction inhibits PAK activation and
            enhances Sema4D ligand binding
REFERENCE   8  (residues 1 to 2135)
  AUTHORS   Vikis,H.G., Li,W., He,Z. and Guan,K.L.
  TITLE     The semaphorin receptor plexin-B1 specifically interacts with
            active Rac in a ligand-dependent manner
  JOURNAL   Proc Natl Acad Sci U S A 97 (23), 12457-12462 (2000)
   PUBMED   11035813
REFERENCE   9  (residues 1 to 2135)
  AUTHORS   Tamagnone,L., Artigiani,S., Chen,H., He,Z., Ming,G.I., Song,H.,
            Chedotal,A., Winberg,M.L., Goodman,C.S., Poo,M., Tessier-Lavigne,M.
            and Comoglio,P.M.
  TITLE     Plexins are a large family of receptors for transmembrane,
            secreted, and GPI-anchored semaphorins in vertebrates
  JOURNAL   Cell 99 (1), 71-80 (1999)
   PUBMED   10520995
  REMARK    Erratum:[Cell 2001 Jan 26;104(2):following 320]
REFERENCE   10 (residues 1 to 2135)
  AUTHORS   Maestrini,E., Tamagnone,L., Longati,P., Cremona,O., Gulisano,M.,
            Bione,S., Tamanini,F., Neel,B.G., Toniolo,D. and Comoglio,P.M.
  TITLE     A family of transmembrane proteins with homology to the
            MET-hepatocyte growth factor receptor
  JOURNAL   Proc Natl Acad Sci U S A 93 (2), 674-678 (1996)
   PUBMED   8570614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB007867.1, AC134772.2 and BC066773.1.
            
            On Dec 20, 2003 this sequence version replaced NP_002664.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 both encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB007867.1, BC146793.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2135
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..2135
                     /product="plexin-B1 precursor"
                     /note="plexin 5; semaphorin receptor SEP"
                     /calculated_mol_wt=230308
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43157.3)"
                     /calculated_mol_wt=2008
     mat_peptide     20..2135
                     /product="Plexin-B1. /id=PRO_0000024671"
                     /note="propagated from UniProtKB/Swiss-Prot (O43157.3)"
                     /calculated_mol_wt=230308
     Region          28..480
                     /region_name="Sema_plexin_B1"
                     /note="The Sema domain, a protein interacting module, of
                     Plexin B1; cd11275"
                     /db_xref="CDD:200536"
     Site            31
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43157.3)"
     Site            order(80..82,136,138..140,178,202,207,209..210,212..213,
                     235,242,361..362,367..368,375,380..382)
                     /site_type="other"
                     /note="Semaphorin binding site [polypeptide binding]"
                     /db_xref="CDD:200536"
     Site            334
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43157.3)"
     Region          481..527
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          541..627
                     /region_name="TIG_plexin"
                     /note="TIG domain; pfam17960"
                     /db_xref="CDD:465588"
     Site            543
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43157.3)"
     Region          641..677
                     /region_name="PSI"
                     /note="domain found in Plexins, Semaphorins and Integrins;
                     smart00423"
                     /db_xref="CDD:214655"
     Region          671..829
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43157.3)"
     Region          <681..839
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          849..884
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43157.3)"
     Region          921..1020
                     /region_name="TIG_2"
                     /note="TIG domain found in plexin; pfam18020"
                     /db_xref="CDD:465619"
     Region          1021..>1061
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          1070..1161
                     /region_name="IPT_plexin_repeat1"
                     /note="First repeat of the IPT domain of Plexins and Cell
                     Surface Receptors (PCSR) . Plexins are involved in the
                     regulation of cell proliferation and of cellular adhesion
                     and repulsion receptors. In general, there are three
                     copies of the IPT domain present...; cd01180"
                     /db_xref="CDD:238585"
     Region          1162..1249
                     /region_name="IPT_plexin_repeat2"
                     /note="Second repeat of the IPT domain of Plexins and Cell
                     Surface Receptors (PCSR) . Plexins are involved in the
                     regulation of cell proliferation and of cellular adhesion
                     and repulsion receptors. In general, there are three
                     copies of the IPT domain present...; cd01179"
                     /db_xref="CDD:238584"
     Site            1183
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43157.3)"
     Region          1252..1376
                     /region_name="IPT_plexin_repeat3"
                     /note="Third repeat of the IPT domain of Plexins and Cell
                     Surface Receptors (PCSR) . Plexins are involved in the
                     regulation of cell proliferation and of cellular adhesion
                     and repulsion receptors. In general, there are three
                     copies of the IPT domain present...; cd01181"
                     /db_xref="CDD:238586"
     Site            1253
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973;
                     propagated from UniProtKB/Swiss-Prot (O43157.3)"
     Site            1305..1306
                     /site_type="cleavage"
                     /note="Cleavage, by proprotein convertases; propagated
                     from UniProtKB/Swiss-Prot (O43157.3)"
     Site            1330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (O43157.3)"
     Site            1491..1511
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43157.3)"
     Region          1562..2097
                     /region_name="Plexin_cytopl"
                     /note="Plexin cytoplasmic RasGAP domain; pfam08337"
                     /db_xref="CDD:462434"
     Site            1815
                     /site_type="other"
                     /note="Important for interaction with RAC1 and RND1;
                     propagated from UniProtKB/Swiss-Prot (O43157.3)"
     Region          1883..1908
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43157.3)"
     CDS             1..2135
                     /gene="PLXNB1"
                     /gene_synonym="PLEXIN-B1; PLXN5; SEP"
                     /coded_by="NM_002673.6:152..6559"
                     /db_xref="CCDS:CCDS2765.1"
                     /db_xref="GeneID:5364"
                     /db_xref="HGNC:HGNC:9103"
                     /db_xref="MIM:601053"
ORIGIN      
        1 mpalgpallq alwagwvltl qplpptaftp ngtylqhlar dptsgtlylg atnflfqlsp
       61 glqleatvst gpvldsrdcl ppvmpdecpq aqptnnpnql llvspgalvv cgsvhqgvce
      121 qrrlgqleql llrperpgdt qyvaandpav stvglvaqgl agepllfvgr gytsrgvggg
      181 ippittralw ppdpqaafsy eetaklavgr lseyshhfvs afargasayf lflrrdlqaq
      241 srafrayvsr vclrdqhyys yvelplaceg grygliqaaa vatsrevahg evlfaafssa
      301 apptvgrpps aaagasgasa lcafpldevd rlanrtrdac ytregraedg tevayieydv
      361 nsdcaqlpvd tldaypcgsd htpspmasrv pleatpilew pgiqltavav tmedghtiaf
      421 lgdsqgqlhr vylgpgsdgh pystqsiqqg savsrdltfd gtfehlyvmt qstllkvpva
      481 scaqhldcas clahrdpycg wcvllgrcsr rsecsrgqgp eqwlwsfqpe lgclqvaams
      541 panisreetr evflsvpdlp plwpgesysc hfgehqspal ltgsgvmcps pdpseapvlp
      601 rgadyvsvsv elrfgavvia ktslsfydcv avtelrpsaq cqacvssrwg cnwcvwqhlc
      661 thkascdagp mvashqsplv spdpparggp spspptapka latpapdtlp vepgapstat
      721 asdispgasp sllspwgpwa gsgsisspgs tgsplheeps ppspqngpgt avpaptdfrp
      781 satpedllas plspsevaav ppadpgpeal hptvpldlpp atvpattfpg amgsvkpald
      841 wltreggelp eadewtggda pafststlls gdgdsaeleg ppaplilpss ldyqydtpgl
      901 weleeatlga sscpcvesvq gstlmpvhve reirllgrnl hlfqdgpgdn ecvmelegle
      961 vvvearvece pppdtqchvt cqqhqlsyea lqpelrvglf lrragrlrvd saeglhvvly
     1021 dcsvghgdcs rcqtampqyg cvwcegerpr cvtreacgea eavatqcpap lihsvepltg
     1081 pvdggtrvti rgsnlgqhvq dvlgmvtvag vpcavdaqey evssslvcit gasgeevaga
     1141 tavevpgrgr gvsehdfayq dpkvhsifpa rgpraggtrl tlngsklltg rledirvvvg
     1201 dqpchllpeq qseqlrcets prptpatlpv avwfgaterr lqrgqfkytl dpnitsagpt
     1261 ksflsggrei cvrgqnldvv qtprirvtvv srmlqpsqgl grrrrvvpet acslgpscss
     1321 qqfeepchvn ssqlitcrtp alpglpedpw vrvefildnl vfdfatlnpt pfsyeadptl
     1381 qplnpedptm pfrhkpgsvf svegenldla mskeevvami gdgpcvvktl trhhlycepp
     1441 veqplprhha lreapdslpe ftvqmgnlrf slghvqydge spgafpvaaq vglgvgtsll
     1501 algviiivlm yrrkskqalr dykkvqiqle nlessvrdrc kkeftdlmte mtdltsdllg
     1561 sgipfldykv yaeriffpgh resplhrdlg vpesrrptve qglgqlsnll nsklfltkfi
     1621 htlesqrtfs ardrayvasl ltvalhgkle yftdilrtll sdlvaqyvak npklmlrrte
     1681 tvveklltnw msiclytfvr dsvgeplyml frgikhqvdk gpvdsvtgka kytlndnrll
     1741 redveyrplt lnallavgpg ageaqgvpvk vldcdtisqa kekmldqlyk gvpltqrpdp
     1801 rtldvewrsg vaghlilsde dvtsevqglw rrlntlqhyk vpdgatvalv pcltkhvlre
     1861 nqdyvpgert pmledvdegg irpwhlvkps depepprprr gslrggerer akaipeiylt
     1921 rllsmkgtlq kfvddlfqvi lstsrpvpla vkyffdllde qaqqhgisdq dtihiwktns
     1981 lplrfwinii knpqfvfdvq tsdnmdavll viaqtfmdac tladhklgrd spinkllyar
     2041 diprykrmve ryyadirqtv pasdqemnsv laelswnysg dlgarvalhe lykyinkyyd
     2101 qiitaleedg taqkmqlgyr lqqiaaaven kvtdl
//
LOCUS       NP_067612                188 aa            linear   PRI 21-NOV-2025
DEFINITION  B-cell antigen receptor complex-associated protein alpha chain
            isoform 2 precursor [Homo sapiens].
ACCESSION   NP_067612
VERSION     NP_067612.1
DBSOURCE    REFSEQ: accession NM_021601.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Alhalwani,A.Y., Abudawood,K., Qadizadah,A.B.E.A., Jambi,S. and
            Sannan,N.S.
  TITLE     Immunoglobulin A levels and its correlation with
            neutrophil-to-lymphocyte ratio as inflammatory biomarkers for dry
            eye disease in type 2 diabetes: a retrospective study
  JOURNAL   Front Immunol 14, 1184862 (2023)
   PUBMED   37520541
  REMARK    GeneRIF: Immunoglobulin A levels and its correlation with
            neutrophil-to-lymphocyte ratio as inflammatory biomarkers for dry
            eye disease in type 2 diabetes: a retrospective study.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Leung,I., Templeton,M.L., Lo,Y., Rajan,A., Stull,S.M.,
            Garrison,S.M., Salter,A.I., Smythe,K.S., Correnti,C.E.,
            Srivastava,S., Yeung,C.C.S. and Riddell,S.R.
  TITLE     Compromised antigen binding and signaling interfere with bispecific
            CD19 and CD79a chimeric antigen receptor function
  JOURNAL   Blood Adv 7 (12), 2718-2730 (2023)
   PUBMED   36469024
  REMARK    GeneRIF: Compromised antigen binding and signaling interfere with
            bispecific CD19 and CD79a chimeric antigen receptor function.
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Li,Y., Shen,H., Zhang,R., Ji,C., Wang,Y., Su,C. and Xiao,J.
  TITLE     Immunoglobulin M perception by FcmuR
  JOURNAL   Nature 615 (7954), 907-912 (2023)
   PUBMED   36949194
REFERENCE   5  (residues 1 to 188)
  AUTHORS   Huse,K., Bai,B., Hilden,V.I., Bollum,L.K., Vatsveen,T.K.,
            Munthe,L.A., Smeland,E.B., Irish,J.M., Walchli,S. and
            Myklebust,J.H.
  TITLE     Mechanism of CD79A and CD79B Support for IgM+ B Cell Fitness
            through B Cell Receptor Surface Expression
  JOURNAL   J Immunol 209 (10), 2042-2053 (2022)
   PUBMED   36426942
  REMARK    GeneRIF: Mechanism of CD79A and CD79B Support for IgM+ B Cell
            Fitness through B Cell Receptor Surface Expression.
REFERENCE   6  (residues 1 to 188)
  AUTHORS   Leduc,I., Preud'homme,J.L. and Cogne,M.
  TITLE     Structure and expression of the mb-1 transcript in human lymphoid
            cells
  JOURNAL   Clin Exp Immunol 90 (1), 141-146 (1992)
   PUBMED   1395095
REFERENCE   7  (residues 1 to 188)
  AUTHORS   Muller,B., Cooper,L. and Terhorst,C.
  TITLE     Cloning and sequencing of the cDNA encoding the human homologue of
            the murine immunoglobulin-associated protein B29
  JOURNAL   Eur J Immunol 22 (6), 1621-1625 (1992)
   PUBMED   1534761
REFERENCE   8  (residues 1 to 188)
  AUTHORS   Hutchcroft,J.E., Harrison,M.L. and Geahlen,R.L.
  TITLE     Association of the 72-kDa protein-tyrosine kinase PTK72 with the B
            cell antigen receptor
  JOURNAL   J Biol Chem 267 (12), 8613-8619 (1992)
   PUBMED   1569106
REFERENCE   9  (residues 1 to 188)
  AUTHORS   Ha,H.J., Kubagawa,H. and Burrows,P.D.
  TITLE     Molecular cloning and expression pattern of a human gene homologous
            to the murine mb-1 gene
  JOURNAL   J Immunol 148 (5), 1526-1531 (1992)
   PUBMED   1538135
REFERENCE   10 (residues 1 to 188)
  AUTHORS   Reth,M.
  TITLE     Antigen receptors on B lymphocytes
  JOURNAL   Annu Rev Immunol 10, 97-121 (1992)
   PUBMED   1591006
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC243967.3 and X83540.1.
            
            Summary: The B lymphocyte antigen receptor is a multimeric complex
            that includes the antigen-specific component, surface
            immunoglobulin (Ig). Surface Ig non-covalently associates with two
            other proteins, Ig-alpha and Ig-beta, which are necessary for
            expression and function of the B-cell antigen receptor. This gene
            encodes the Ig-alpha protein of the B-cell antigen component.
            Alternatively spliced transcript variants encoding different
            isoforms have been described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site compared to variant 1. The resulting isoform (2) has
            the same N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.136145.1,
                                           SRR1163657.245347.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..188
                     /product="B-cell antigen receptor complex-associated
                     protein alpha chain isoform 2 precursor"
                     /note="MB-1 membrane glycoprotein; CD79a antigen
                     (immunoglobulin-associated alpha); B-cell antigen receptor
                     complex-associated protein alpha chain; surface
                     IgM-associated protein; ig-alpha; membrane-bound
                     immunoglobulin-associated protein; CD79a molecule,
                     immunoglobulin-associated alpha"
                     /calculated_mol_wt=17588
     sig_peptide     1..32
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3216
     mat_peptide     33..188
                     /product="B-cell antigen receptor complex-associated
                     protein alpha chain isoform 2"
                     /calculated_mol_wt=17588
     Region          147..167
                     /region_name="ITAM"
                     /note="Immunoreceptor tyrosine-based activation motif;
                     smart00077"
                     /db_xref="CDD:128390"
     CDS             1..188
                     /gene="CD79A"
                     /gene_synonym="IGA; IGAlpha; MB-1; MB1"
                     /coded_by="NM_021601.4:27..593"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS46088.1"
                     /db_xref="GeneID:973"
                     /db_xref="HGNC:HGNC:1698"
                     /db_xref="MIM:112205"
ORIGIN      
        1 mpggpgvlqa lpatifllfl lsavylgpgc qalwmhkvpa slmvslgeda hfqcphnssn
       61 nanvtwwrvl hgnytwppef lgpgedpnep pprpfldmge gtknriitae giillfcavv
      121 pgtlllfrkr wqneklglda gdeyedenly eglnlddcsm yedisrglqg tyqdvgslni
      181 gdvqlekp
//
LOCUS       NP_001371813             671 aa            linear   PRI 21-NOV-2025
DEFINITION  signal transducer and activator of transcription 1-alpha/beta
            isoform 5 [Homo sapiens].
ACCESSION   NP_001371813
VERSION     NP_001371813.1
DBSOURCE    REFSEQ: accession NM_001384884.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Wang,Y., Song,Q., Huang,W., Lin,Y., Wang,X., Wang,C., Willard,B.,
            Zhao,C., Nan,J., Holvey-Bates,E., Wang,Z., Taylor,D., Yang,J. and
            Stark,G.R.
  TITLE     A virus-induced conformational switch of STAT1-STAT2 dimers boosts
            antiviral defenses
  JOURNAL   Cell Res 31 (2), 206-218 (2021)
   PUBMED   32759968
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Decker,T. and Kovarik,P.
  TITLE     Serine phosphorylation of STATs
  JOURNAL   Oncogene 19 (21), 2628-2637 (2000)
   PUBMED   10851062
  REMARK    Review article
REFERENCE   4  (residues 1 to 671)
  AUTHORS   Bowman,T., Garcia,R., Turkson,J. and Jove,R.
  TITLE     STATs in oncogenesis
  JOURNAL   Oncogene 19 (21), 2474-2488 (2000)
   PUBMED   10851046
  REMARK    Review article
REFERENCE   5  (residues 1 to 671)
  AUTHORS   Haddad,B., Pabon-Pena,C.R., Young,H. and Sun,W.H.
  TITLE     Assignment1 of STAT1 to human chromosome 2q32 by FISH and radiation
            hybrids
  JOURNAL   Cytogenet Cell Genet 83 (1-2), 58-59 (1998)
   PUBMED   9925928
REFERENCE   6  (residues 1 to 671)
  AUTHORS   Yan,R., Qureshi,S., Zhong,Z., Wen,Z. and Darnell,J.E. Jr.
  TITLE     The genomic structure of the STAT genes: multiple exons in
            coincident sites in Stat1 and Stat2
  JOURNAL   Nucleic Acids Res 23 (3), 459-463 (1995)
   PUBMED   7885841
REFERENCE   7  (residues 1 to 671)
  AUTHORS   Igarashi,K., Garotta,G., Ozmen,L., Ziemiecki,A., Wilks,A.F.,
            Harpur,A.G., Larner,A.C. and Finbloom,D.S.
  TITLE     Interferon-gamma induces tyrosine phosphorylation of
            interferon-gamma receptor and regulated association of protein
            tyrosine kinases, Jak1 and Jak2, with its receptor
  JOURNAL   J Biol Chem 269 (20), 14333-14336 (1994)
   PUBMED   7514165
REFERENCE   8  (residues 1 to 671)
  AUTHORS   Shuai,K., Horvath,C.M., Huang,L.H., Qureshi,S.A., Cowburn,D. and
            Darnell,J.E. Jr.
  TITLE     Interferon activation of the transcription factor Stat91 involves
            dimerization through SH2-phosphotyrosyl peptide interactions
  JOURNAL   Cell 76 (5), 821-828 (1994)
   PUBMED   7510216
REFERENCE   9  (residues 1 to 671)
  AUTHORS   Schindler,C., Fu,X.Y., Improta,T., Aebersold,R. and Darnell,J.E.
            Jr.
  TITLE     Proteins of transcription factor ISGF-3: one gene encodes the
            91-and 84-kDa ISGF-3 proteins that are activated by interferon
            alpha
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7836-7839 (1992)
   PUBMED   1502203
REFERENCE   10 (residues 1 to 671)
  AUTHORS   Schindler,C., Shuai,K., Prezioso,V.R. and Darnell,J.E. Jr.
  TITLE     Interferon-dependent tyrosine phosphorylation of a latent
            cytoplasmic transcription factor
  JOURNAL   Science 257 (5071), 809-813 (1992)
   PUBMED   1496401
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC067945.4.
            
            Summary: The protein encoded by this gene is a member of the STAT
            protein family. In response to cytokines and growth factors, STAT
            family members are phosphorylated by the receptor associated
            kinases, and then form homo- or heterodimers that translocate to
            the cell nucleus where they act as transcription activators. The
            protein encoded by this gene can be activated by various ligands
            including interferon-alpha, interferon-gamma, EGF, PDGF and IL6.
            This protein mediates the expression of a variety of genes, which
            is thought to be important for cell viability in response to
            different cell stimuli and pathogens. The protein plays an
            important role in immune responses to viral, fungal and
            mycobacterial pathogens. Mutations in this gene are associated with
            Immunodeficiency 31B, 31A, and 31C. [provided by RefSeq, Jun 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1966682, SAMEA2145743
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.2"
     Protein         1..671
                     /product="signal transducer and activator of transcription
                     1-alpha/beta isoform 5"
                     /note="transcription factor ISGF-3 components p91/p84;
                     signal transducer and activator of transcription
                     1-alpha/beta; signal transducer and activator of
                     transcription 1, 91kD; signal transducer and activator of
                     transcription 1, 91kDa"
                     /calculated_mol_wt=78345
     Region          4..123
                     /region_name="STAT_int"
                     /note="STAT protein, protein interaction domain;
                     smart00964"
                     /db_xref="CDD:214942"
     Region          140..315
                     /region_name="STAT1_CCD"
                     /note="Coiled-coil domain of Signal Transducer and
                     Activator of Transcription 1 (STAT1); cd16851"
                     /db_xref="CDD:341076"
     Site            order(166..167,170..171,174,177..178,181,234,238,241..243,
                     245..246,258..259,261..262,265..266,269,273,276,308,
                     311..313)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:341076"
     Site            order(241..243,245..246,258..259,262,265..266,269,273,276,
                     304,308,311..312)
                     /site_type="other"
                     /note="CCD-DBD interface [polypeptide binding]"
                     /db_xref="CDD:341076"
     Region          319..479
                     /region_name="STAT1_DBD"
                     /note="DNA-binding domain of Signal Transducer and
                     Activator of Transcription 1 (STAT1); cd16845"
                     /db_xref="CDD:341083"
     Site            order(338,342,380,413,415,428..429,461..462,465)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:341083"
     Region          559..>655
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(586,604,632,634)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198173"
     Site            order(633,649)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198173"
     CDS             1..671
                     /gene="STAT1"
                     /gene_synonym="CANDF7; IMD31A; IMD31B; IMD31C; ISGF-3;
                     STAT91"
                     /coded_by="NM_001384884.1:387..2402"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:6772"
                     /db_xref="HGNC:HGNC:11362"
                     /db_xref="MIM:600555"
ORIGIN      
        1 mwmsqwyelq qldskfleqv hqlyddsfpm eirqylaqwl ekqdwehaan dvsfatirfh
       61 dllsqlddqy srfslennfl lqhnirkskr nlqdnfqedp iqmsmiiysc lkeerkilen
      121 aqrfnqaqsg niqstvmldk qkeldskvrn vkdkvmcieh eiksledlqd eydfkcktlq
      181 nrehetngva ksdqkqeqll lkkmylmldn krkevvhkii ellnvteltq nalindelve
      241 wkrrqqsaci ggppnacldq lqnwftivae slqqvrqqlk kleeleqkyt yehdpitknk
      301 qvlwdrtfsl fqqliqssfv verqpcmpth pqrplvlktg vqftvklrll vklqelnynl
      361 kvkvlfdkdv nerntvkgfr kfnilgthtk vmnmeestng slaaefrhlq lkeqknagtr
      421 tnegplivte elhslsfetq lcqpglvidl ettslpvvvi snvsqlpsgw asilwynmlv
      481 aeprnlsffl tppcarwaql sevlswqfss vtkrglnvdq lnmlgekllg pnaspdglip
      541 wtrfckenin dknfpfwlwi esilelikkh llplwndgci mgfiskerer allkdqqpgt
      601 fllrfsessr egaitftwve rsqnggepdf havepytkke lsavtfpdii rnykvsrivg
      661 svefdsmmnt v
//
LOCUS       NP_001180444             432 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc transporter 6 isoform 4 [Homo sapiens].
ACCESSION   NP_001180444
VERSION     NP_001180444.1
DBSOURCE    REFSEQ: accession NM_001193515.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Song,C.C., Liu,T., Hogstrand,C., Zhong,C.C., Zheng,H., Sun,L.H. and
            Luo,Z.
  TITLE     SENP1 mediates zinc-induced ZnT6 deSUMOylation at Lys-409 involved
            in the regulation of zinc metabolism in Golgi apparatus
  JOURNAL   Cell Mol Life Sci 81 (1), 422 (2024)
   PUBMED   39367979
  REMARK    GeneRIF: SENP1 mediates zinc-induced ZnT6 deSUMOylation at Lys-409
            involved in the regulation of zinc metabolism in Golgi apparatus.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Aktay,I., Billur,D., Tuncay,E. and Turan,B.
  TITLE     An Overexpression of SLC30A6 Gene Contributes to Cardiomyocyte
            Dysfunction via Affecting Mitochondria and Inducing Activations in
            K-Acetylation and Epigenetic Proteins
  JOURNAL   Biochem Genet 62 (4), 3198-3214 (2024)
   PUBMED   38091184
  REMARK    GeneRIF: An Overexpression of SLC30A6 Gene Contributes to
            Cardiomyocyte Dysfunction via Affecting Mitochondria and Inducing
            Activations in K-Acetylation and Epigenetic Proteins.
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Zhu,B., Huo,R., Zhi,Q., Zhan,M., Chen,X. and Hua,Z.C.
  TITLE     Increased expression of zinc transporter ZIP4, ZIP11, ZnT1, and
            ZnT6 predicts poor prognosis in pancreatic cancer
  JOURNAL   J Trace Elem Med Biol 65, 126734 (2021)
   PUBMED   33631610
  REMARK    GeneRIF: Increased expression of zinc transporter ZIP4, ZIP11,
            ZnT1, and ZnT6 predicts poor prognosis in pancreatic cancer.
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Falcon-Perez,J.M. and Dell'Angelica,E.C.
  TITLE     Zinc transporter 2 (SLC30A2) can suppress the vesicular zinc defect
            of adaptor protein 3-depleted fibroblasts by promoting zinc
            accumulation in lysosomes
  JOURNAL   Exp Cell Res 313 (7), 1473-1483 (2007)
   PUBMED   17349999
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Smith,J.L., Xiong,S., Markesbery,W.R. and Lovell,M.A.
  TITLE     Altered expression of zinc transporters-4 and -6 in mild cognitive
            impairment, early and late Alzheimer's disease brain
  JOURNAL   Neuroscience 140 (3), 879-888 (2006)
   PUBMED   16580781
  REMARK    GeneRIF: Our results show that Zn transporter-4 and Zn
            transporter-6 are significantly (P<0.05) increased in
            hippocampus/parahippocampal gyrus of early Alzheimer's disease and
            Alzheimer's disease subjects.
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Suzuki,T., Ishihara,K., Migaki,H., Ishihara,K., Nagao,M.,
            Yamaguchi-Iwai,Y. and Kambe,T.
  TITLE     Two different zinc transport complexes of cation diffusion
            facilitator proteins localized in the secretory pathway operate to
            activate alkaline phosphatases in vertebrate cells
  JOURNAL   J Biol Chem 280 (35), 30956-30962 (2005)
   PUBMED   15994300
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Seve,M., Chimienti,F., Devergnas,S. and Favier,A.
  TITLE     In silico identification and expression of SLC30 family genes: an
            expressed sequence tag data mining strategy for the
            characterization of zinc transporters' tissue expression
  JOURNAL   BMC Genomics 5 (1), 32 (2004)
   PUBMED   15154973
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 432)
  AUTHORS   Huang,L., Kirschke,C.P. and Gitschier,J.
  TITLE     Functional characterization of a novel mammalian zinc transporter,
            ZnT6
  JOURNAL   J Biol Chem 277 (29), 26389-26395 (2002)
   PUBMED   11997387
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK304225.1, AL121653.2 and
            AA594503.1.
            
            Summary: This gene encodes a member of a family of proteins that
            function as zinc transporters. This protein can regulate
            subcellular levels of zinc in the Golgi and vesicles. Expression of
            this gene is altered in the Alzheimer's disease brain plaques.
            [provided by RefSeq, Aug 2016].
            
            Transcript Variant: This variant (4) lacks two alternate in-frame
            exons compared to variant 1. The resulting protein (isoform 4) is
            shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2385447.1, AK304225.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.3"
     Protein         1..432
                     /product="zinc transporter 6 isoform 4"
                     /note="zinc transporter 6; solute carrier family 30 (zinc
                     transporter), member 6"
                     /calculated_mol_wt=47487
     Region          14..226
                     /region_name="Cation_efflux"
                     /note="Cation efflux family; pfam01545"
                     /db_xref="CDD:426316"
     CDS             1..432
                     /gene="SLC30A6"
                     /gene_synonym="MST103; MSTP103; ZNT6"
                     /coded_by="NM_001193515.3:38..1336"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS54343.1"
                     /db_xref="GeneID:55676"
                     /db_xref="HGNC:HGNC:19305"
                     /db_xref="MIM:611148"
ORIGIN      
        1 mswkillfgv inlictgfll mwcsstnsia ltaytyltif dlfslmtcli sywvtlrkps
       61 pvysfgferl evlavfastv laqlgalfil kesaerfleq peihtgrllv gtfvalcfnl
      121 ftmlsirnkp fayvseaast swlqehvadl srslcgiipg lssiflprmn pfvlidlaga
      181 falcitymli einnyfavdt asaiaialmt fgtmypmsvy sgkvllqttp phvigqldkl
      241 irevstldgv levrnehfwt lgfgslagsv hvrirrdane qmvlahvtnr lytlvstltv
      301 qifkddwirp allsgpvaan vlnfsdhhvi pmpllkgtdd lnpvtstpak psspppefsf
      361 ntpgknvnpv illntqtrpy gfglnhghtp yssmlnqglg vpgigatqgl rtgftnipsr
      421 ygtnnrigqp rp
//
LOCUS       NP_001336018             659 aa            linear   PRI 21-NOV-2025
DEFINITION  TBC1 domain family member 5 isoform e [Homo sapiens].
ACCESSION   NP_001336018 XP_016863052
VERSION     NP_001336018.1
DBSOURCE    REFSEQ: accession NM_001349089.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Tu,Y.X.I., Sydor,A.M., Coyaud,E., Laurent,E.M.N., Dyer,D.,
            Mellouk,N., St-Germain,J., Vernon,R.M., Forman-Kay,J.D., Li,T.,
            Hua,R., Zhao,K., Ridgway,N.D., Kim,P.K., Raught,B. and Brumell,J.H.
  TITLE     Global Proximity Interactome of the Human Macroautophagy Pathway
  JOURNAL   Autophagy 18 (5), 1174-1186 (2022)
   PUBMED   34524948
REFERENCE   4  (residues 1 to 659)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 659)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 659)
  AUTHORS   Seaman,M.N., Harbour,M.E., Tattersall,D., Read,E. and Bright,N.
  TITLE     Membrane recruitment of the cargo-selective retromer subcomplex is
            catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP
            TBC1D5
  JOURNAL   J Cell Sci 122 (Pt 14), 2371-2382 (2009)
   PUBMED   19531583
  REMARK    GeneRIF: Membrane recruitment of the cargo-selective retromer
            subcomplex VPS35/29/26 is catalysed by the small GTPase Rab7 and
            inhibited by the Rab-GAP TBC1D5.
REFERENCE   7  (residues 1 to 659)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
REFERENCE   8  (residues 1 to 659)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   9  (residues 1 to 659)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 659)
  AUTHORS   Brill,L.M., Salomon,A.R., Ficarro,S.B., Mukherji,M.,
            Stettler-Gill,M. and Peters,E.C.
  TITLE     Robust phosphoproteomic profiling of tyrosine phosphorylation sites
            from human T cells using immobilized metal affinity chromatography
            and tandem mass spectrometry
  JOURNAL   Anal Chem 76 (10), 2763-2772 (2004)
   PUBMED   15144186
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104451.2, AC144531.2, AC090960.3 and AC090644.2.
            
            On Mar 3, 2017 this sequence version replaced XP_016863052.1.
            
            Transcript Variant: This variant (19), as well as variants 17, 18,
            20, and 21, encodes isoform e.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2530214.1,
                                           SRR14038192.2201602.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..659
                     /product="TBC1 domain family member 5 isoform e"
                     /calculated_mol_wt=73027
     Region          19..245
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     CDS             1..659
                     /gene="TBC1D5"
                     /coded_by="NM_001349089.2:649..2628"
                     /note="isoform e is encoded by transcript variant 19"
                     /db_xref="GeneID:9779"
                     /db_xref="HGNC:HGNC:19166"
                     /db_xref="MIM:615740"
ORIGIN      
        1 minnplsqde gslwnkffqd kelrsmieqd vkrtfpemqf fqqenvrkil tdvlfcyare
       61 neqllykqgm hellapivfv lhcdhqaflh asesaqpsee mktvlnpeyl ehdayavfsq
      121 lmetaepwfs tfehdgqkgk etlmtpipfa rpqdlgptia ivtkvnqiqd hllkkhdiel
      181 ymhlnrleia pqiyglrwvr llfgrefplq dllvvwdalf adglslglvd yifvamllyi
      241 rdalissnyq tclgllmhyp figdvhslil kalflrdpkr nprpvtyqfh pnldyykarg
      301 adlmnksrtn akgaplnink vsnslinfgr klispamapg saggpvpggn ssssssvvip
      361 trtsaeapsh hlqqqqqqqr lmksesmpvq lnkglsskni ssspsveslp ggreftgspp
      421 ssatkkdsff snisrsrshs ktmgrkesee eleaqisflq gqlndldamc kycakvmdth
      481 lvniqdvilq enlekedqil vslaglkqik dilkgslrfn qsqleaeene qitiadnhyc
      541 ssgqgqgrgq gqsvqmsgai kqassetpgc tdrgnsddfi liskdddgss argsfsgqaq
      601 plrtlrstsg ksqapvcspl vfsdplmgpa sasssnpsss pdddsskdsg ftivspldi
//
LOCUS       NP_001333278             480 aa            linear   PRI 21-NOV-2025
DEFINITION  autophagy-related protein 13 isoform f [Homo sapiens].
ACCESSION   NP_001333278
VERSION     NP_001333278.1
DBSOURCE    REFSEQ: accession NM_001346349.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Patel,A. and Faesen,A.C.
  TITLE     Metamorphosis by ATG13 and ATG101 in human autophagy initiation
  JOURNAL   Autophagy 20 (4), 968-969 (2024)
   PUBMED   37394799
  REMARK    GeneRIF: Metamorphosis by ATG13 and ATG101 in human autophagy
            initiation.
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Nguyen,A. and Faesen,A.C.
  TITLE     The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis
  JOURNAL   FEBS Lett 598 (1), 114-126 (2024)
   PUBMED   37567770
  REMARK    GeneRIF: The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis.
            Review article
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Karabi,Z., Moradian,F. and Kheirabadi,M.
  TITLE     The effect of lactoferrin on ULK1 and ATG13 genes expression in
            breast cancer cell line MCF7 and bioinformatics studies of protein
            interaction between lactoferrin and the autophagy initiation
            complex
  JOURNAL   Cell Biochem Biophys 80 (4), 795-806 (2022)
   PUBMED   36169801
  REMARK    GeneRIF: The effect of lactoferrin on ULK1 and ATG13 genes
            expression in breast cancer cell line MCF7 and bioinformatics
            studies of protein interaction between lactoferrin and the
            autophagy initiation complex.
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Gottschalk,G., Peterson,D., Knox,K., Maynard,M., Whelan,R.J. and
            Roy,A.
  TITLE     Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE)
  JOURNAL   Mol Cell Neurosci 120, 103731 (2022)
   PUBMED   35487443
  REMARK    GeneRIF: Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE).
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Jung,C.H., Jun,C.B., Ro,S.H., Kim,Y.M., Otto,N.M., Cao,J., Kundu,M.
            and Kim,D.H.
  TITLE     ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy
            machinery
  JOURNAL   Mol Biol Cell 20 (7), 1992-2003 (2009)
   PUBMED   19225151
  REMARK    GeneRIF: The ULK-Atg13-FIP200 complexes are direct targets of mTOR
            and important regulators of autophagy in response to mTOR
            signaling.
REFERENCE   7  (residues 1 to 480)
  AUTHORS   Hosokawa,N., Hara,T., Kaizuka,T., Kishi,C., Takamura,A., Miura,Y.,
            Iemura,S., Natsume,T., Takehana,K., Yamada,N., Guan,J.L., Oshiro,N.
            and Mizushima,N.
  TITLE     Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200
            complex required for autophagy
  JOURNAL   Mol Biol Cell 20 (7), 1981-1991 (2009)
   PUBMED   19211835
  REMARK    GeneRIF: mTORC1 suppresses autophagy through direct regulation of
            the approximately 3-MDa ULK1-Atg13-FIP200 complex.
REFERENCE   8  (residues 1 to 480)
  AUTHORS   Chan,E.Y., Longatti,A., McKnight,N.C. and Tooze,S.A.
  TITLE     Kinase-inactivated ULK proteins inhibit autophagy via their
            conserved C-terminal domains using an Atg13-independent mechanism
  JOURNAL   Mol Cell Biol 29 (1), 157-171 (2009)
   PUBMED   18936157
  REMARK    GeneRIF: The functions of ULK1 and ULK2 are controlled by
            autophosphorylation and conformational changes involving exposure
            of the C-terminal domain and interaction with the putative human
            homologue of Atg13.
            GeneRIF: The gene product is the functional homologue of yeast
            Atg13, and required for autophagy in mammalian cells.
REFERENCE   9  (residues 1 to 480)
  AUTHORS   Meijer,W.H., van der Klei,I.J., Veenhuis,M. and Kiel,J.A.
  TITLE     ATG genes involved in non-selective autophagy are conserved from
            yeast to man, but the selective Cvt and pexophagy pathways also
            require organism-specific genes
  JOURNAL   Autophagy 3 (2), 106-116 (2007)
   PUBMED   17204848
REFERENCE   10 (residues 1 to 480)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC127035.6 and AC115088.6.
            
            Summary: The protein encoded by this gene is an autophagy factor
            and a target of the TOR kinase signaling pathway. The encoded
            protein is essential for autophagosome formation and mitophagy.
            [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (40), as well as variants 2, 5,
            36-39, and 41-45, encodes isoform f.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2976876.1,
                                           SRR1803613.99748.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145313, SAMEA2153031
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..480
                     /product="autophagy-related protein 13 isoform f"
                     /note="autophagy-related protein 13; ATG13 autophagy
                     related 13 homolog"
                     /calculated_mol_wt=52692
     Region          19..192
                     /region_name="ATG13"
                     /note="Autophagy-related protein 13; pfam10033"
                     /db_xref="CDD:431003"
     CDS             1..480
                     /gene="ATG13"
                     /gene_synonym="KIAA0652; PARATARG8"
                     /coded_by="NM_001346349.2:519..1961"
                     /note="isoform f is encoded by transcript variant 40"
                     /db_xref="CCDS:CCDS7921.1"
                     /db_xref="GeneID:9776"
                     /db_xref="HGNC:HGNC:29091"
                     /db_xref="MIM:615088"
ORIGIN      
        1 metdlnsqdr kdldkfikff alktvqvivq arlgekictr ssssptgsdw fnlaikdipe
       61 vtheakkala gqlpavgrsm cveislktse gdsmeleiwc lemnekcdke ikvsytvynr
      121 lslllkslla itrvtpayrl srkqgheyvi lyriyfgevq lsglgegfqt vrvgtvgtpv
      181 gtitlscayr inlafmstrq fertppimgi iidhfvdrpy pssspmhpcn yrtagedtgv
      241 iypsvedsqe vcttsfstsp psqlmvpgke ggvplapnqp vhgtqadqer latctpsdrt
      301 hcaatpssse dtetvsnsse grasphdvle tifvrkvgaf vnkpinqvtl tsldipfamf
      361 apknleledt dpmvnppdsp etesplqgsl hsdgssggss gnthddfvmi dfkpafskdd
      421 ilpmdlgtfy refqnppqls slsidigaqs maedldslpe klavheknvr efdafvetlq
//
LOCUS       NP_001362504             260 aa            linear   PRI 21-NOV-2025
DEFINITION  cAMP-dependent protein kinase catalytic subunit beta isoform 24
            [Homo sapiens].
ACCESSION   NP_001362504 XP_016857201
VERSION     NP_001362504.1
DBSOURCE    REFSEQ: accession NM_001375575.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Tanaka,M., Takeshita,K., Kunita,A., Hasegawa,K. and Ushiku,T.
  TITLE     PRKACA/PRKACB Fusions in Pancreatobiliary Intraductal Oncocytic
            Papillary Neoplasms Including Those With Atypical Morphology: An
            Analysis of 22 Cases Expanding Morphologic Spectrum
  JOURNAL   Am J Surg Pathol 48 (8), 1032-1040 (2024)
   PUBMED   38841868
  REMARK    GeneRIF: PRKACA/PRKACB Fusions in Pancreatobiliary Intraductal
            Oncocytic Papillary Neoplasms Including Those With Atypical
            Morphology: An Analysis of 22 Cases Expanding Morphologic Spectrum.
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Pei,W., Yin,W., Yu,T., Zhang,X., Zhang,Q., Yang,X., Shi,C., Shen,W.
            and Liu,G.
  TITLE     Dual-Specificity Phosphatase 4 Promotes Malignant Features in
            Colorectal Cancer Through Cyclic-AMP Response Element Binding
            Protein/Protein Kinase CAMP-Activated Catalytic Subunit Beta
            Activation
  JOURNAL   Dig Dis Sci 69 (8), 2856-2874 (2024)
   PUBMED   38824257
  REMARK    GeneRIF: Dual-Specificity Phosphatase 4 Promotes Malignant Features
            in Colorectal Cancer Through Cyclic-AMP Response Element Binding
            Protein/Protein Kinase CAMP-Activated Catalytic Subunit Beta
            Activation.
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Itoh,T., Omori,Y., Seino,M., Hirose,K., Date,F., Ono,Y.,
            Mizukami,Y., Aoki,S., Ishida,M., Mizuma,M., Morikawa,T.,
            Higuchi,R., Honda,G., Okamura,Y., Kinoshita,K., Unno,M. and
            Furukawa,T.
  TITLE     Gene Rearrangement and Expression of PRKACA and PRKACB Govern
            Morphobiology of Pancreatobiliary Oncocytic Neoplasms
  JOURNAL   Mod Pathol 37 (1), 100358 (2024)
   PUBMED   37871652
  REMARK    GeneRIF: Gene Rearrangement and Expression of PRKACA and PRKACB
            Govern Morphobiology of Pancreatobiliary Oncocytic Neoplasms.
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Maimaitiaili,Y., Fukumura,Y., Hirabayashi,K., Kinowaki,Y.,
            Naito,Y., Saito,A., Rong,L., Nakahodo,J. and Yao,T.
  TITLE     Investigation of -PRKACA/-PRKACB fusion genes in oncocytic tumors
            of the pancreatobiliary and other systems
  JOURNAL   Virchows Arch 481 (6), 865-876 (2022)
   PUBMED   36152045
  REMARK    GeneRIF: Investigation of -PRKACA/-PRKACB fusion genes in oncocytic
            tumors of the pancreatobiliary and other systems.
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Orstavik,S., Reinton,N., Frengen,E., Langeland,B.T., Jahnsen,T. and
            Skalhegg,B.S.
  TITLE     Identification of novel splice variants of the human catalytic
            subunit Cbeta of cAMP-dependent protein kinase
  JOURNAL   Eur J Biochem 268 (19), 5066-5073 (2001)
   PUBMED   11589697
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Scarpetta,M.A. and Uhler,M.D.
  TITLE     Evidence for two additional isoforms of the endogenous protein
            kinase inhibitor of cAMP-dependent protein kinase in mouse
  JOURNAL   J Biol Chem 268 (15), 10927-10931 (1993)
   PUBMED   7684369
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Da Silva,J.D., Tkachenko,N. and Soares,A.R.
  TITLE     Ellis-van Creveld Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37903214
REFERENCE   8  (residues 1 to 260)
  AUTHORS   Simard,J., Berube,D., Sandberg,M., Grzeschik,K.H., Gagne,R.,
            Hansson,V. and Jahnsen,T.
  TITLE     Assignment of the gene encoding the catalytic subunit C beta of
            cAMP-dependent protein kinase to the p36 band on chromosome 1
  JOURNAL   Hum Genet 88 (6), 653-657 (1992)
   PUBMED   1551670
REFERENCE   9  (residues 1 to 260)
  AUTHORS   Beebe,S.J., Oyen,O., Sandberg,M., Froysa,A., Hansson,V. and
            Jahnsen,T.
  TITLE     Molecular cloning of a tissue-specific protein kinase (C gamma)
            from human testis--representing a third isoform for the catalytic
            subunit of cAMP-dependent protein kinase
  JOURNAL   Mol Endocrinol 4 (3), 465-475 (1990)
   PUBMED   2342480
REFERENCE   10 (residues 1 to 260)
  AUTHORS   Taylor,S.S., Buechler,J.A. and Yonemoto,W.
  TITLE     cAMP-dependent protein kinase: framework for a diverse family of
            regulatory enzymes
  JOURNAL   Annu Rev Biochem 59, 971-1005 (1990)
   PUBMED   2165385
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL450063.14.
            
            On Oct 29, 2019 this sequence version replaced XP_016857201.1.
            
            Summary: The protein encoded by this gene is a member of the
            serine/threonine protein kinase family. The encoded protein is a
            catalytic subunit of cAMP (cyclic AMP)-dependent protein kinase,
            which mediates signalling though cAMP. cAMP signaling is important
            to a number of processes, including cell proliferaton and
            differentiation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.728943.1,
                                           SRR1803617.385022.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.1"
     Protein         1..260
                     /product="cAMP-dependent protein kinase catalytic subunit
                     beta isoform 24"
                     /EC_number="2.7.11.11"
                     /note="protein kinase A catalytic subunit beta; protein
                     kinase, cAMP-dependent, catalytic, beta; protein kinase,
                     cAMP-dependent, beta catalytic subunit"
                     /calculated_mol_wt=29890
     Region          45..>258
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(53..56,59,61,74,76,108,124..127,170,174..175,177,
                     187..188)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..260
                     /gene="PRKACB"
                     /gene_synonym="CAFD2; PKA C-beta; PKACB"
                     /coded_by="NM_001375575.1:314..1096"
                     /note="isoform 24 is encoded by transcript variant 24"
                     /db_xref="GeneID:5567"
                     /db_xref="HGNC:HGNC:9381"
                     /db_xref="MIM:176892"
ORIGIN      
        1 msarkssdas acssseisvk eflakakedf lkkwenptqn nagledferk ktlgtgsfgr
       61 vmlvkhkate qyyamkildk qkvvklkqie htlnekrilq avnfpflvrl eyafkdnsnl
      121 ymvmeyvpgg emfshlrrig rfsepharfy aaqivltfey lhsldliyrd lkpenllidh
      181 qgyiqvtdfg fakrvkgrtw tlcgtpeyla peiilskgyn kavdwwalgv liyemaagyp
      241 pffadqpiqi yekivsgknf
//
LOCUS       NP_001373883             514 aa            linear   PRI 21-NOV-2025
DEFINITION  solute carrier organic anion transporter family member 1A2 isoform
            13 [Homo sapiens].
ACCESSION   NP_001373883
VERSION     NP_001373883.1
DBSOURCE    REFSEQ: accession NM_001386954.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Flogel,S., Tust,M., Boussettaoui,S., Fischer,D. and Grundemann,D.
  TITLE     Enhancing transporter activity in heterologous expression systems
            with SAHA: a 2500-times more potent and odorless alternative to
            butyrate
  JOURNAL   FEBS Open Bio 15 (6), 906-913 (2025)
   PUBMED   40052353
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Kataoka,H., Akiyoshi,T., Uchida,Y., Imaoka,A., Terasaki,T. and
            Ohtani,H.
  TITLE     The Effects of N-Glycosylation on the Expression and Transport
            Activity of OATP1A2 and OATP2B1
  JOURNAL   J Pharm Sci 113 (5), 1376-1384 (2024)
   PUBMED   38432624
  REMARK    GeneRIF: The Effects of N-Glycosylation on the Expression and
            Transport Activity of OATP1A2 and OATP2B1.
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Han,H., Akiyoshi,T., Morita,T., Kataoka,H., Katayama,K., Yajima,K.,
            Imaoka,A. and Ohtani,H.
  TITLE     Comparison of the transport kinetics of fexofenadine and its pH
            dependency among OATP1A2 genetic variants
  JOURNAL   Drug Metab Pharmacokinet 47, 100470 (2022)
   PUBMED   36116173
  REMARK    GeneRIF: Comparison of the transport kinetics of fexofenadine and
            its pH dependency among OATP1A2 genetic variants.
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Hau,R.K., Klein,R.R., Wright,S.H. and Cherrington,N.J.
  TITLE     Localization of Xenobiotic Transporters Expressed at the Human
            Blood-Testis Barrier
  JOURNAL   Drug Metab Dispos 50 (6), 770-780 (2022)
   PUBMED   35307651
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Kullak-Ublick,G.A., Fisch,T., Oswald,M., Hagenbuch,B., Meier,P.J.,
            Beuers,U. and Paumgartner,G.
  TITLE     Dehydroepiandrosterone sulfate (DHEAS): identification of a carrier
            protein in human liver and brain
  JOURNAL   FEBS Lett 424 (3), 173-176 (1998)
   PUBMED   9539145
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Meier,P.J., Eckhardt,U., Schroeder,A., Hagenbuch,B. and Stieger,B.
  TITLE     Substrate specificity of sinusoidal bile acid and organic anion
            uptake systems in rat and human liver
  JOURNAL   Hepatology 26 (6), 1667-1677 (1997)
   PUBMED   9398014
  REMARK    Review article
REFERENCE   8  (residues 1 to 514)
  AUTHORS   Kullak-Ublick,G.A., Beuers,U., Fahney,C., Hagenbuch,B., Meier,P.J.
            and Paumgartner,G.
  TITLE     Identification and functional characterization of the promoter
            region of the human organic anion transporting polypeptide gene
  JOURNAL   Hepatology 26 (4), 991-997 (1997)
   PUBMED   9328325
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Kullak-Ublick,G.A., Beuers,U., Meier,P.J., Domdey,H. and
            Paumgartner,G.
  TITLE     Assignment of the human organic anion transporting polypeptide
            (OATP) gene to chromosome 12p12 by fluorescence in situ
            hybridization
  JOURNAL   J Hepatol 25 (6), 985-987 (1996)
   PUBMED   9007731
REFERENCE   10 (residues 1 to 514)
  AUTHORS   Kullak-Ublick,G.A., Hagenbuch,B., Stieger,B., Schteingart,C.D.,
            Hofmann,A.F., Wolkoff,A.W. and Meier,P.J.
  TITLE     Molecular and functional characterization of an organic anion
            transporting polypeptide cloned from human liver
  JOURNAL   Gastroenterology 109 (4), 1274-1282 (1995)
   PUBMED   7557095
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022224.22.
            
            Summary: This gene encodes a sodium-independent transporter which
            mediates cellular uptake of organic ions in the liver. Its
            substrates include bile acids, bromosulphophthalein, and some
            steroidal compounds. The protein is a member of the SLC21A family
            of solute carriers. Alternative splicing of this gene results in
            multiple transcript variants. [provided by RefSeq, Dec 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.204323.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2142363,
                                           SAMEA2144333 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..514
                     /product="solute carrier organic anion transporter family
                     member 1A2 isoform 13"
                     /note="organic anion transporting polypeptide A; solute
                     carrier family 21 (organic anion transporter), member 3;
                     sodium-independent organic anion transporter; OATP-1;
                     solute carrier family 21 member 3; organic
                     anion-transporting polypeptide 1"
                     /calculated_mol_wt=56569
     Region          <1..469
                     /region_name="oat"
                     /note="sodium-independent organic anion transporter;
                     TIGR00805"
                     /db_xref="CDD:273279"
     CDS             1..514
                     /gene="SLCO1A2"
                     /gene_synonym="OATP; OATP-A; OATP1A2; SLC21A3"
                     /coded_by="NM_001386954.1:193..1737"
                     /note="isoform 13 is encoded by transcript variant 33"
                     /db_xref="GeneID:6579"
                     /db_xref="HGNC:HGNC:10956"
                     /db_xref="MIM:602883"
ORIGIN      
        1 mwvyvlvgni vrgmgetpil plgisyiedf akfensplyi glvetgaiig pliglllasf
       61 canvyvdtgf vntddliitp tdtrwvgaww fgflicagvn vltaipfffl pntlpkegle
      121 tnadiiknen edkqkeevkk ekygitkdfl pfmkslscnp iymlfilvsv iqfnafvnmi
      181 sfmpkyleqq ygisssdaif lmgiynlppi cigyiiggli mkkfkitvkq aahigcwlsl
      241 leyllyflsf lmtcenssvv gintsyegip qdlyvendif adcnvdcncp skiwdpvcgn
      301 nglsylsacl agcetsigtg inmvfqncsc iqtsgnssav lglcdkgpdc slmlqyflil
      361 samssfiysl aaipgymvll rcmkseeksl gvglhtfctr vfagipapiy fgalmdstcl
      421 hwgtlkcges gacriydstt fryiylglpa alrgssfvpa liilillrkc hlpgenassg
      481 telietkvkg keneckdiyq kstvlkddel ktkl
//
LOCUS       NP_001288115             614 aa            linear   PRI 21-NOV-2025
DEFINITION  leucine-rich repeat and immunoglobulin-like domain-containing nogo
            receptor-interacting protein 1 isoform b precursor [Homo sapiens].
ACCESSION   NP_001288115
VERSION     NP_001288115.1
DBSOURCE    REFSEQ: accession NM_001301186.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Andrews,J.L., Zalesky,A., Nair,S., Sullivan,R.P., Green,M.J.,
            Pantelis,C., Newell,K.A. and Fernandez,F.
  TITLE     Genetic and Epigenetic Regulation in Lingo-1: Effects on Cognitive
            Function and White Matter Microstructure in a Case-Control Study
            for Schizophrenia
  JOURNAL   Int J Mol Sci 24 (21), 15624 (2023)
   PUBMED   37958608
  REMARK    GeneRIF: Genetic and Epigenetic Regulation in Lingo-1: Effects on
            Cognitive Function and White Matter Microstructure in a
            Case-Control Study for Schizophrenia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 614)
  AUTHORS   Kalafatakis,I., Papagianni,F., Theodorakis,K. and Karagogeos,D.
  TITLE     Nogo-A and LINGO-1: Two Important Targets for Remyelination and
            Regeneration
  JOURNAL   Int J Mol Sci 24 (5), 4479 (2023)
   PUBMED   36901909
  REMARK    GeneRIF: Nogo-A and LINGO-1: Two Important Targets for
            Remyelination and Regeneration.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 614)
  AUTHORS   Zhu,J., Zhu,Z., Ren,Y., Dong,Y., Li,Y. and Yang,X.
  TITLE     LINGO-1 shRNA protects the brain against ischemia/reperfusion
            injury by inhibiting the activation of NF-kappaB and JAK2/STAT3
  JOURNAL   Hum Cell 34 (4), 1114-1122 (2021)
   PUBMED   33830473
  REMARK    GeneRIF: LINGO-1 shRNA protects the brain against
            ischemia/reperfusion injury by inhibiting the activation of
            NF-kappaB and JAK2/STAT3.
REFERENCE   5  (residues 1 to 614)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 614)
  AUTHORS   Satoh,J., Tabunoki,H., Yamamura,T., Arima,K. and Konno,H.
  TITLE     TROY and LINGO-1 expression in astrocytes and macrophages/microglia
            in multiple sclerosis lesions
  JOURNAL   Neuropathol Appl Neurobiol 33 (1), 99-107 (2007)
   PUBMED   17239012
  REMARK    GeneRIF: the ternary complex of NgR/TROY/LINGO-1 expressed on
            astrocytes, macrophages/microglia and neurones, by interacting with
            Nogo-A on oligodendrocytes, might modulate glial-neuronal
            interactions in demyelinating lesions of multiple sclerosis
REFERENCE   7  (residues 1 to 614)
  AUTHORS   Mosyak,L., Wood,A., Dwyer,B., Buddha,M., Johnson,M., Aulabaugh,A.,
            Zhong,X., Presman,E., Benard,S., Kelleher,K., Wilhelm,J.,
            Stahl,M.L., Kriz,R., Gao,Y., Cao,Z., Ling,H.P., Pangalos,M.N.,
            Walsh,F.S. and Somers,W.S.
  TITLE     The structure of the Lingo-1 ectodomain, a module implicated in
            central nervous system repair inhibition
  JOURNAL   J Biol Chem 281 (47), 36378-36390 (2006)
   PUBMED   17005555
  REMARK    GeneRIF: the Lingo-1 ectodomain is a module implicated in central
            nervous system repair inhibition
REFERENCE   8  (residues 1 to 614)
  AUTHORS   Mi,S., Lee,X., Shao,Z., Thill,G., Ji,B., Relton,J., Levesque,M.,
            Allaire,N., Perrin,S., Sands,B., Crowell,T., Cate,R.L., McCoy,J.M.
            and Pepinsky,R.B.
  TITLE     LINGO-1 is a component of the Nogo-66 receptor/p75 signaling
            complex
  JOURNAL   Nat Neurosci 7 (3), 221-228 (2004)
   PUBMED   14966521
REFERENCE   9  (residues 1 to 614)
  AUTHORS   Carim-Todd,L., Escarceller,M., Estivill,X. and Sumoy,L.
  TITLE     LRRN6A/LERN1 (leucine-rich repeat neuronal protein 1), a novel gene
            with enriched expression in limbic system and neocortex
  JOURNAL   Eur J Neurosci 18 (12), 3167-3182 (2003)
   PUBMED   14686891
  REMARK    GeneRIF: The LERN1 expression pattern is specific to the central
            nervous system, highly and broadly expressed during early stages of
            development and gradually restricted to forebrain structures as
            development proceeds(LERN1)
REFERENCE   10 (residues 1 to 614)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA150164.1, DA232085.1, BC011057.1 and AK027500.1.
            
            Transcript Variant: This variant (2) contains alternate 5' exon
            structure and thus differs in the 5' UTR, lacks a portion of the 5'
            coding region, and initiates translation at a downstream in-frame
            start codon, compared to variant 1. The encoded isoform (b) is
            shorter at the N-terminus, compared to isoform a. Variants 2
            through 12 all encode isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA150164.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2145743,
                                           SAMEA2148093 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.3"
     Protein         1..614
                     /product="leucine-rich repeat and immunoglobulin-like
                     domain-containing nogo receptor-interacting protein 1
                     isoform b precursor"
                     /note="leucine-rich repeat neuronal protein 1; leucine
                     rich repeat neuronal 6A; leucine-rich repeat and
                     immunoglobulin-like domain-containing nogo
                     receptor-interacting protein 1; leucine-rich repeat and
                     immunoglobulin domain-containing protein 1"
                     /calculated_mol_wt=65668
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3496
     Region          35..69
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; smart00013"
                     /db_xref="CDD:214470"
     Region          65..>365
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          67..90
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          91..114
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          115..138
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          139..186
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          187..210
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          211..258
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          259..282
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          283..306
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          307..330
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          331..351
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          335..>415
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Region          417..508
                     /region_name="IgI_Lingo-1"
                     /note="Immunoglobulin I-set domain of the Leucine-rich
                     repeat and immunoglobin-like domain-containing protein 1
                     (Lingo-1); cd20969"
                     /db_xref="CDD:409561"
     Region          417..420
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409561"
     Region          425..429
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409561"
     Region          435..444
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409561"
     Region          449..454
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409561"
     Region          457..459
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409561"
     Region          468..471
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409561"
     Region          474..481
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409561"
     Region          487..495
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409561"
     Region          498..508
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409561"
     CDS             1..614
                     /gene="LINGO1"
                     /gene_synonym="LERN1; LRRN6A; MRT64; UNQ201"
                     /coded_by="NM_001301186.2:516..2360"
                     /note="isoform b precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS73766.1"
                     /db_xref="GeneID:84894"
                     /db_xref="HGNC:HGNC:21205"
                     /db_xref="MIM:609791"
ORIGIN      
        1 mlaggvrsmp spllacwqpi lllvlgsvls gsatgcpprc ecsaqdravl chrkrfvavp
       61 egiptetrll dlgknriktl nqdefasfph leelelneni vsavepgafn nlfnlrtlgl
      121 rsnrlklipl gvftglsnlt kldisenkiv illdymfqdl ynlkslevgd ndlvyishra
      181 fsglnsleql tlekcnltsi ptealshlhg livlrlrhln inairdysfk rlyrlkvlei
      241 shwpyldtmt pnclyglnlt slsithcnlt avpylavrhl vylrflnlsy npistiegsm
      301 lhellrlqei qlvggqlavv epyafrglny lrvlnvsgnq lttleesvfh svgnletlil
      361 dsnplacdcr llwvfrrrwr lnfnrqqptc atpefvqgke fkdfpdvllp nyftcrrari
      421 rdrkaqqvfv deghtvqfvc radgdpppai lwlsprkhlv saksngrltv fpdgtlevry
      481 aqvqdngtyl ciaanaggnd smpahlhvrs yspdwphqpn ktfafisnqp gegeanstra
      541 tvpfpfdikt liiattmgfi sflgvvlfcl vllflwsrgk gntkhnieie yvprksdagi
      601 ssadaprkfn mkmi
//
LOCUS       NP_001129028             628 aa            linear   PRI 21-NOV-2025
DEFINITION  cytoplasmic dynein 1 intermediate chain 1 isoform b [Homo sapiens].
ACCESSION   NP_001129028
VERSION     NP_001129028.1
DBSOURCE    REFSEQ: accession NM_001135556.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Ananya,R.G., Pandi,C., Kannan,B., Pandi,A., Prasad,P.,
            Jayaseelan,V.P. and Arumugam,P.
  TITLE     DYNC1I1 acts as a promising prognostic biomarker and is correlated
            with immune infiltration in head and neck squamous cell carcinoma
  JOURNAL   J Stomatol Oral Maxillofac Surg 125 (4), 101734 (2024)
   PUBMED   38072235
  REMARK    GeneRIF: DYNC1I1 acts as a promising prognostic biomarker and is
            correlated with immune infiltration in head and neck squamous cell
            carcinoma.
REFERENCE   3  (residues 1 to 628)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 628)
  AUTHORS   Zhou,J., Zhu,Y., Ma,S., Li,Y., Liu,K., Xu,S., Li,X., Li,L., Hu,J.
            and Liu,Y.
  TITLE     Bioinformatics analysis identifies DYNC1I1 as prognosis marker in
            male patients with liver hepatocellular carcinoma
  JOURNAL   PLoS One 16 (10), e0258797 (2021)
   PUBMED   34679093
  REMARK    GeneRIF: Bioinformatics analysis identifies DYNC1I1 as prognosis
            marker in male patients with liver hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 628)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 628)
  AUTHORS   Ligon,L.A., Tokito,M., Finklestein,J.M., Grossman,F.E. and
            Holzbaur,E.L.
  TITLE     A direct interaction between cytoplasmic dynein and kinesin I may
            coordinate motor activity
  JOURNAL   J Biol Chem 279 (18), 19201-19208 (2004)
   PUBMED   14985359
REFERENCE   7  (residues 1 to 628)
  AUTHORS   Lo,K.W., Naisbitt,S., Fan,J.S., Sheng,M. and Zhang,M.
  TITLE     The 8-kDa dynein light chain binds to its targets via a conserved
            (K/R)XTQT motif
  JOURNAL   J Biol Chem 276 (17), 14059-14066 (2001)
   PUBMED   11148209
REFERENCE   8  (residues 1 to 628)
  AUTHORS   Horikawa,I., Parker,E.S., Solomon,G.G. and Barrett,J.C.
  TITLE     Upregulation of the gene encoding a cytoplasmic dynein intermediate
            chain in senescent human cells
  JOURNAL   J Cell Biochem 82 (3), 415-421 (2001)
   PUBMED   11500918
REFERENCE   9  (residues 1 to 628)
  AUTHORS   Crackower,M.A., Sinasac,D.S., Xia,J., Motoyama,J., Prochazka,M.,
            Rommens,J.M., Scherer,S.W. and Tsui,L.C.
  TITLE     Cloning and characterization of two cytoplasmic dynein intermediate
            chain genes in mouse and human
  JOURNAL   Genomics 55 (3), 257-267 (1999)
   PUBMED   10049579
REFERENCE   10 (residues 1 to 628)
  AUTHORS   King,S.M., Dillman,J.F. 3rd, Benashski,S.E., Lye,R.J.,
            Patel-King,R.S. and Pfister,K.K.
  TITLE     The mouse t-complex-encoded protein Tctex-1 is a light chain of
            brain cytoplasmic dynein
  JOURNAL   J Biol Chem 271 (50), 32281-32287 (1996)
   PUBMED   8943288
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA491512.1, AK313148.1, AF123074.1, BC032945.2 and DB343806.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice junction compared to variant 1. The resulting isoform (b)
            has the same N- and C-termini but is shorter compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032945.2, SRR1660807.171288.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000447467.6/ ENSP00000392337.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.3"
     Protein         1..628
                     /product="cytoplasmic dynein 1 intermediate chain 1
                     isoform b"
                     /note="dynein, cytoplasmic, intermediate polypeptide 1;
                     cytoplasmic dynein 1 intermediate chain 1; DH IC-1; dynein
                     intermediate chain 1, cytosolic; cytoplasmic dynein
                     intermediate chain 1"
                     /calculated_mol_wt=70659
     Region          126..156
                     /region_name="Dynein_IC2"
                     /note="Cytoplasmic dynein 1 intermediate chain 2;
                     pfam11540"
                     /db_xref="CDD:463291"
     Region          274..320
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <301..590
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          329..368
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          376..417
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          425..464
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          471..512
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          518..556
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          564..590
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..628
                     /gene="DYNC1I1"
                     /gene_synonym="DNCI1; DNCIC1"
                     /coded_by="NM_001135556.2:230..2116"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47645.1"
                     /db_xref="GeneID:1780"
                     /db_xref="HGNC:HGNC:2963"
                     /db_xref="MIM:603772"
ORIGIN      
        1 msdksdlkae lerkkqrlaq ireekkrkee erkkkeadmq qkkepvqdds dldrkrrete
       61 allqsigisp epplvptpms pssksvstps eagsqdsgdl gpltrtlqwd tdpsvlqlqs
      121 dselgrrlhk lgvskvtqvd flprevvsys ketqtplath qseedeedee mveskvgqds
      181 elenqdkkqe vkeapprelt eeekqqilhs eefliffdrt irvieralae dsdiffdysg
      241 releekdgdv qaganlsfnr qfydehwskh rvvtcmdwsl qypelmvasy nnnedaphep
      301 dgvalvwnmk fkkttpeyvf hcqssvmsvc farfhpnlvv ggtysgqivl wdnrshrrtp
      361 vqrtplsaaa hthpvycvnv vgtqnahnli tvstdgkmcs wsldmlstpq esmelvynks
      421 kpvavtgmaf ptgdvnnfvv gseegtvyta crhgskagig evfeghqgpv tginchmavg
      481 pidfshlfvt ssfdwtvklw ttkhnkplys fednadyvyd vmwspvhpal facvdgmgrl
      541 dlwnlnndte vptasvaieg asalnrvrwa qagkevavgd segriwvydv gelavphnde
      601 wtrfartlve iranradsee egtvelsa
//
LOCUS       NP_001364905             363 aa            linear   PRI 21-NOV-2025
DEFINITION  disks large homolog 2 isoform 19 [Homo sapiens].
ACCESSION   NP_001364905 XP_016872780
VERSION     NP_001364905.1
DBSOURCE    REFSEQ: accession NM_001377976.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Li,H., Zhu,J., Liu,X., Liu,L., Huang,S., Wu,A., Xu,Z., Zhang,X.,
            Li,Z., Ni,F., Liu,L. and Dong,J.
  TITLE     Glioma stem cell-derived exosomes induce the transformation of
            astrocytes via the miR-3065-5p/DLG2 signaling axis
  JOURNAL   Glia 72 (5), 857-871 (2024)
   PUBMED   38234042
  REMARK    GeneRIF: Glioma stem cell-derived exosomes induce the
            transformation of astrocytes via the miR-3065-5p/DLG2 signaling
            axis.
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Chen,Y., Karaca,E., Robin,N.H., Goodloe,D., Al-Beshri,A.,
            Dean,S.J., Hurst,A.C.E., Carroll,A.J. and Mikhail,F.M.
  TITLE     DLG2 intragenic exonic deletions reinforce the link to
            neurodevelopmental disorders and suggest a potential association
            with congenital anomalies and dysmorphism
  JOURNAL   Genet Med 26 (1), 101010 (2024)
   PUBMED   37860969
  REMARK    GeneRIF: DLG2 intragenic exonic deletions reinforce the link to
            neurodevelopmental disorders and suggest a potential association
            with congenital anomalies and dysmorphism.
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Stathakis,D.G., Lee,D. and Bryant,P.J.
  TITLE     Fine-scale physical map of the 11q21 region surrounding the human
            DLG2 locus, the gene encoding Chapsyn-110
  JOURNAL   Genomics 54 (1), 186-188 (1998)
   PUBMED   9806853
REFERENCE   6  (residues 1 to 363)
  AUTHORS   Irie,M., Hata,Y., Takeuchi,M., Ichtchenko,K., Toyoda,A., Hirao,K.,
            Takai,Y., Rosahl,T.W. and Sudhof,T.C.
  TITLE     Binding of neuroligins to PSD-95
  JOURNAL   Science 277 (5331), 1511-1515 (1997)
   PUBMED   9278515
REFERENCE   7  (residues 1 to 363)
  AUTHORS   Hsueh,Y.P., Kim,E. and Sheng,M.
  TITLE     Disulfide-linked head-to-head multimerization in the mechanism of
            ion channel clustering by PSD-95
  JOURNAL   Neuron 18 (5), 803-814 (1997)
   PUBMED   9182804
REFERENCE   8  (residues 1 to 363)
  AUTHORS   Kim,E., Cho,K.O., Rothschild,A. and Sheng,M.
  TITLE     Heteromultimerization and NMDA receptor-clustering activity of
            Chapsyn-110, a member of the PSD-95 family of proteins
  JOURNAL   Neuron 17 (1), 103-113 (1996)
   PUBMED   8755482
REFERENCE   9  (residues 1 to 363)
  AUTHORS   Brenman,J.E., Chao,D.S., Gee,S.H., McGee,A.W., Craven,S.E.,
            Santillano,D.R., Wu,Z., Huang,F., Xia,H., Peters,M.F.,
            Froehner,S.C. and Bredt,D.S.
  TITLE     Interaction of nitric oxide synthase with the postsynaptic density
            protein PSD-95 and alpha1-syntrophin mediated by PDZ domains
  JOURNAL   Cell 84 (5), 757-767 (1996)
   PUBMED   8625413
REFERENCE   10 (residues 1 to 363)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002370.5, AP000773.4 and
            AP003026.2.
            
            On Jan 23, 2020 this sequence version replaced XP_016872780.1.
            
            Summary: This gene encodes a member of the membrane-associated
            guanylate kinase (MAGUK) family. The encoded protein forms a
            heterodimer with a related family member that may interact at
            postsynaptic sites to form a multimeric scaffold for the clustering
            of receptors, ion channels, and associated signaling proteins.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. Additional transcript variants have been
            described, but their full-length nature is not known. [provided by
            RefSeq, Dec 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.32525.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.1"
     Protein         1..363
                     /product="disks large homolog 2 isoform 19"
                     /note="channel-associated protein of synapses, 110kDa;
                     postsynaptic density protein PSD-93; channel-associated
                     protein of synapse-110; discs, large homolog 2,
                     chapsyn-110; protein phosphatase 1, regulatory subunit 58;
                     disks large homolog 2"
                     /calculated_mol_wt=41729
     Region          45..118
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(56,58,61,70,88..89,108,110..111)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          172..350
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..363
                     /gene="DLG2"
                     /gene_synonym="chapsyn-110; PPP1R58; PSD-93; PSD93"
                     /coded_by="NM_001377976.1:181..1272"
                     /note="isoform 19 is encoded by transcript variant 19"
                     /db_xref="GeneID:1740"
                     /db_xref="HGNC:HGNC:2901"
                     /db_xref="MIM:603583"
ORIGIN      
        1 msfdsqcdlr ssepdyarfe akihdlreqm mnhsmssgsg slrtnqkrsl yvramfdydk
       61 skdsglpsqg lsfkygdilh vinasddeww qarrvmlegd seemgvipsk rrverkerar
      121 lktvkfnakp gvidskgdip glgddgygtk tlrgqedlil syepvtrqei nytrpviilg
      181 pmkdrinddl isefpdkfgs cvphttrpkr dyevdgrdyh fvisreqmek diqehkfiea
      241 gqyndnlygt svqsvrfvae rgkhcildvs gnaikrlqva qlypiaifik prsleplmem
      301 nkrlteeqak ktydraikle qefgeyftai vqgdtlediy nqcklvieeq sgpfiwipsk
      361 ekl
//
LOCUS       NP_758871                355 aa            linear   PRI 21-NOV-2025
DEFINITION  membrane cofactor protein isoform 12 precursor [Homo sapiens].
ACCESSION   NP_758871
VERSION     NP_758871.1
DBSOURCE    REFSEQ: accession NM_172361.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Grodstein,F., Lemos,B., Yang,J., de Paiva Lopes,K., Vialle,R.A.,
            Seyfried,N., Wang,Y., Shireby,G., Hannon,E., Thomas,A., Brookes,K.,
            Mill,J., De Jager,P.L. and Bennett,D.A.
  TITLE     Genetic architecture of epigenetic cortical clock age in brain
            tissue from older individuals: alterations in CD46 and other loci
  JOURNAL   Epigenetics 19 (1), 2392050 (2024)
   PUBMED   39169872
  REMARK    GeneRIF: Genetic architecture of epigenetic cortical clock age in
            brain tissue from older individuals: alterations in CD46 and other
            loci.
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Thi,T.N., Thanh,H.D., Nguyen,V.T., Kwon,S.Y., Moon,C., Hwang,E.C.
            and Jung,C.
  TITLE     Complement regulatory protein CD46 promotes bladder cancer
            metastasis through activation of MMP9
  JOURNAL   Int J Oncol 65 (1) (2024)
   PUBMED   38847230
  REMARK    GeneRIF: Complement regulatory protein CD46 promotes bladder cancer
            metastasis through activation of MMP9.
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Vassiliev,P., Gusev,E., Komelkova,M., Kochetkov,A., Dobrynina,M.
            and Sarapultsev,A.
  TITLE     Computational Analysis of CD46 Protein Interaction with SARS-CoV-2
            Structural Proteins: Elucidating a Putative Viral Entry Mechanism
            into Human Cells
  JOURNAL   Viruses 15 (12), 2297 (2023)
   PUBMED   38140538
  REMARK    GeneRIF: Computational Analysis of CD46 Protein Interaction with
            SARS-CoV-2 Structural Proteins: Elucidating a Putative Viral Entry
            Mechanism into Human Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Richards,A., Kemp,E.J., Liszewski,M.K., Goodship,J.A., Lampe,A.K.,
            Decorte,R., Muslumanoglu,M.H., Kavukcu,S., Filler,G., Pirson,Y.,
            Wen,L.S., Atkinson,J.P. and Goodship,T.H.
  TITLE     Mutations in human complement regulator, membrane cofactor protein
            (CD46), predispose to development of familial hemolytic uremic
            syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (22), 12966-12971 (2003)
   PUBMED   14566051
  REMARK    GeneRIF: Mutations predispose to development of familial hemolytic
            uremic syndrome.
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Martin,B. and Smith,R.J.H.
  TITLE     C3 Glomerulopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301598
REFERENCE   6  (residues 1 to 355)
  AUTHORS   Noris,M., Bresin,E., Mele,C. and Remuzzi,G.
  TITLE     Genetic Atypical Hemolytic-Uremic Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301541
REFERENCE   7  (residues 1 to 355)
  AUTHORS   Russell,S.M., Sparrow,R.L., McKenzie,I.F. and Purcell,D.F.
  TITLE     Tissue-specific and allelic expression of the complement regulator
            CD46 is controlled by alternative splicing
  JOURNAL   Eur J Immunol 22 (6), 1513-1518 (1992)
   PUBMED   1601037
REFERENCE   8  (residues 1 to 355)
  AUTHORS   Adams,E.M., Brown,M.C., Nunge,M., Krych,M. and Atkinson,J.P.
  TITLE     Contribution of the repeating domains of membrane cofactor protein
            (CD46) of the complement system to ligand binding and cofactor
            activity
  JOURNAL   J Immunol 147 (9), 3005-3011 (1991)
   PUBMED   1717583
REFERENCE   9  (residues 1 to 355)
  AUTHORS   Post,T.W., Liszewski,M.K., Adams,E.M., Tedja,I., Miller,E.A. and
            Atkinson,J.P.
  TITLE     Membrane cofactor protein of the complement system: alternative
            splicing of serine/threonine/proline-rich exons and cytoplasmic
            tails produces multiple isoforms that correlate with protein
            phenotype
  JOURNAL   J Exp Med 174 (1), 93-102 (1991)
   PUBMED   1711570
REFERENCE   10 (residues 1 to 355)
  AUTHORS   Lublin,D.M., Liszewski,M.K., Post,T.W., Arce,M.A., Le Beau,M.M.,
            Rebentisch,M.B., Lemons,L.S., Seya,T. and Atkinson,J.P.
  TITLE     Molecular cloning and chromosomal localization of human membrane
            cofactor protein (MCP). Evidence for inclusion in the multigene
            family of complement-regulatory proteins
  JOURNAL   J Exp Med 168 (1), 181-194 (1988)
   PUBMED   3260937
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB078198.1, EF076057.1 and
            BC030594.2.
            
            Summary: The protein encoded by this gene is a type I membrane
            protein and is a regulatory part of the complement system. The
            encoded protein has cofactor activity for inactivation of
            complement components C3b and C4b by serum factor I, which protects
            the host cell from damage by complement. In addition, the encoded
            protein can act as a receptor for the Edmonston strain of measles
            virus, human herpesvirus-6, and type IV pili of pathogenic
            Neisseria. Finally, the protein encoded by this gene may be
            involved in the fusion of the spermatozoa with the oocyte during
            fertilization. Mutations at this locus have been associated with
            susceptibility to hemolytic uremic syndrome. Alternatively spliced
            transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (l) lacks an alternate in-frame
            segment and an exon containing the stop codon as compared to
            variant a. The resulting isoform (12) is shorter and has a distinct
            C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1795621.1,
                                           SRR14038197.2637676.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.2"
     Protein         1..355
                     /product="membrane cofactor protein isoform 12 precursor"
                     /note="CD46 antigen, complement regulatory protein;
                     membrane cofactor protein (CD46, trophoblast-lymphocyte
                     cross-reactive antigen); complement membrane cofactor
                     protein; measles virus receptor; trophoblast leucocyte
                     common antigen; antigen identified by monoclonal antibody
                     TRA-2-10; trophoblast leukocyte common antigen; CD46
                     molecule, complement regulatory protein"
                     /calculated_mol_wt=35953
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3869
     mat_peptide     35..355
                     /product="membrane cofactor protein isoform 12"
                     /calculated_mol_wt=35953
     Region          54..285
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     CDS             1..355
                     /gene="CD46"
                     /gene_synonym="AHUS2; MCP; MIC10; TLX; TRA2.10"
                     /coded_by="NM_172361.3:160..1227"
                     /note="isoform 12 precursor is encoded by transcript
                     variant l"
                     /db_xref="CCDS:CCDS1484.1"
                     /db_xref="GeneID:4179"
                     /db_xref="HGNC:HGNC:6953"
                     /db_xref="MIM:120920"
ORIGIN      
        1 meppgrrecp fpswrfpgll laamvlllys fsdaceeppt feameligkp kpyyeigerv
       61 dykckkgyfy ipplathtic drnhtwlpvs ddacyretcp yirdplngqa vpangtyefg
      121 yqmhficneg yyligeeily celkgsvaiw sgkppicekv lctpppkikn gkhtfsevev
      181 feyldavtys cdpapgpdpf sligestiyc gdnsvwsraa peckvvkcrf pvvengkqis
      241 gfgkkfyyka tvmfecdkgf yldgsdtivc dsnstwdppv pkclkgypkp eegildsldv
      301 wviaviviai vvgvavicvv pyrylqrrkk kgkadggaey atyqtksttp aeqrg
//
LOCUS       NP_001180262             461 aa            linear   PRI 21-NOV-2025
DEFINITION  coronin-1A [Homo sapiens].
ACCESSION   NP_001180262 XP_005255109
VERSION     NP_001180262.1
DBSOURCE    REFSEQ: accession NM_001193333.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Wang,Y., Ma,L., Jia,S., Liu,D., Gu,H., Wei,X., Ma,W., Luo,W.,
            Bai,Y., Wang,W. and Yuan,Z.
  TITLE     Serum exosomal coronin 1A and dynamin 2 as neural tube defect
            biomarkers
  JOURNAL   J Mol Med (Berl) 100 (9), 1307-1319 (2022)
   PUBMED   35915349
  REMARK    GeneRIF: Serum exosomal coronin 1A and dynamin 2 as neural tube
            defect biomarkers.
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Min,F., Fan,C., Zeng,Y., He,N., Zeng,T., Qin,B. and Shi,Y.
  TITLE     Carbamazepine-modified HLA-A*24:02-bound peptidome: Implication of
            CORO1A in skin rash
  JOURNAL   Int Immunopharmacol 109, 108804 (2022)
   PUBMED   35526384
  REMARK    GeneRIF: Carbamazepine-modified HLA-A*24:02-bound peptidome:
            Implication of CORO1A in skin rash.
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Vanguri,V.K., Wang,S., Godyna,S., Ranganathan,S. and Liau,G.
  TITLE     Thrombospondin-1 binds to polyhistidine with high affinity and
            specificity
  JOURNAL   Biochem J 347 (Pt 2), 469-473 (2000)
   PUBMED   10749676
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Ferrari,G., Langen,H., Naito,M. and Pieters,J.
  TITLE     A coat protein on phagosomes involved in the intracellular survival
            of mycobacteria
  JOURNAL   Cell 97 (4), 435-447 (1999)
   PUBMED   10338208
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Okumura,M., Kung,C., Wong,S., Rodgers,M. and Thomas,M.L.
  TITLE     Definition of family of coronin-related proteins conserved between
            humans and mice: close genetic linkage between coronin-2 and
            CD45-associated protein
  JOURNAL   DNA Cell Biol 17 (9), 779-787 (1998)
   PUBMED   9778037
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Grogan,A., Reeves,E., Keep,N., Wientjes,F., Totty,N.F.,
            Burlingame,A.L., Hsuan,J.J. and Segal,A.W.
  TITLE     Cytosolic phox proteins interact with and regulate the assembly of
            coronin in neutrophils
  JOURNAL   J Cell Sci 110 (Pt 24), 3071-3081 (1997)
   PUBMED   9365277
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Suzuki,K., Nishihata,J., Arai,Y., Honma,N., Yamamoto,K., Irimura,T.
            and Toyoshima,S.
  TITLE     Molecular cloning of a novel actin-binding protein, p57, with a WD
            repeat and a leucine zipper motif
  JOURNAL   FEBS Lett 364 (3), 283-288 (1995)
   PUBMED   7758584
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA256300.1, AK314714.1,
            U34690.1 and BC110374.1.
            
            On Aug 31, 2013 this sequence version replaced XP_005255109.1.
            
            Summary: This gene encodes a member of the WD repeat protein
            family. WD repeats are minimally conserved regions of approximately
            40 amino acids typically bracketed by gly-his and trp-asp (GH-WD),
            which may facilitate formation of heterotrimeric or multiprotein
            complexes. Members of this family are involved in a variety of
            cellular processes, including cell cycle progression, signal
            transduction, apoptosis, and gene regulation. Alternative splicing
            results in multiple transcript variants. A related pseudogene has
            been defined on chromosome 16. [provided by RefSeq, Sep 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314714.1, SRR18074968.547675.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..461
                     /product="coronin-1A"
                     /note="coronin-1; clipin-A; coronin, actin binding
                     protein, 1A; coronin-like protein A; coronin-like protein
                     p57; tryptophan aspartate-containing coat protein"
                     /calculated_mol_wt=50895
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.8;
                     propagated from UniProtKB/Swiss-Prot (P31146.4)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000269|PubMed:23100250; propagated from
                     UniProtKB/Swiss-Prot (P31146.4)"
     Region          9..461
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..63
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P31146.4)"
     Region          37..79
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          73..110
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P31146.4)"
     Region          85..129
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          123..160
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P31146.4)"
     Region          134..171
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          164..204
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P31146.4)"
     Region          180..215
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          207..251
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P31146.4)"
     Region          224..263
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          258..296
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P31146.4)"
     Region          270..311
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          302..349
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P31146.4)"
     Region          403..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P31146.4)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC.
                     /evidence=ECO:0000269|PubMed:23100250; propagated from
                     UniProtKB/Swiss-Prot (P31146.4)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O89053; propagated from
                     UniProtKB/Swiss-Prot (P31146.4)"
     Site            449
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P31146.4)"
     CDS             1..461
                     /gene="CORO1A"
                     /gene_synonym="CLABP; CLIPINA; HCORO1; IMD8; p57; TACO"
                     /coded_by="NM_001193333.3:244..1629"
                     /db_xref="CCDS:CCDS10673.1"
                     /db_xref="GeneID:11151"
                     /db_xref="HGNC:HGNC:2252"
                     /db_xref="MIM:605000"
ORIGIN      
        1 msrqvvrssk frhvfgqpak adqcyedvrv sqttwdsgfc avnpkfvali ceasgggafl
       61 vlplgktgrv dknaptvcgh tapvldiawc phndnviasg sedctvmvwe ipdgglmlpl
      121 repvvtlegh tkrvgivawh ttaqnvllsa gcdnvimvwd vgtgaamltl gpevhpdtiy
      181 svdwsrdggl ictscrdkrv riieprkgtv vaekdrpheg trpvravfvs egkilttgfs
      241 rmserqvalw dtkhleepls lqeldtssgv llpffdpdtn ivylcgkgds siryfeitse
      301 apflhylsmf sskesqrgmg ympkrglevn kceiarfykl herrcepiam tvprksdlfq
      361 edlypptagp dpaltaeewl ggrdagplli slkdgyvppk srelrvnrgl dtgrrraape
      421 asgtpssdav srleeemrkl qatvqelqkr ldrleetvqa k
//
LOCUS       NP_001338205             871 aa            linear   PRI 21-NOV-2025
DEFINITION  disks large homolog 2 isoform 9 [Homo sapiens].
ACCESSION   NP_001338205 XP_016872761
VERSION     NP_001338205.1
DBSOURCE    REFSEQ: accession NM_001351276.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Li,H., Zhu,J., Liu,X., Liu,L., Huang,S., Wu,A., Xu,Z., Zhang,X.,
            Li,Z., Ni,F., Liu,L. and Dong,J.
  TITLE     Glioma stem cell-derived exosomes induce the transformation of
            astrocytes via the miR-3065-5p/DLG2 signaling axis
  JOURNAL   Glia 72 (5), 857-871 (2024)
   PUBMED   38234042
  REMARK    GeneRIF: Glioma stem cell-derived exosomes induce the
            transformation of astrocytes via the miR-3065-5p/DLG2 signaling
            axis.
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Chen,Y., Karaca,E., Robin,N.H., Goodloe,D., Al-Beshri,A.,
            Dean,S.J., Hurst,A.C.E., Carroll,A.J. and Mikhail,F.M.
  TITLE     DLG2 intragenic exonic deletions reinforce the link to
            neurodevelopmental disorders and suggest a potential association
            with congenital anomalies and dysmorphism
  JOURNAL   Genet Med 26 (1), 101010 (2024)
   PUBMED   37860969
  REMARK    GeneRIF: DLG2 intragenic exonic deletions reinforce the link to
            neurodevelopmental disorders and suggest a potential association
            with congenital anomalies and dysmorphism.
REFERENCE   3  (residues 1 to 871)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 871)
  AUTHORS   Stathakis,D.G., Lee,D. and Bryant,P.J.
  TITLE     Fine-scale physical map of the 11q21 region surrounding the human
            DLG2 locus, the gene encoding Chapsyn-110
  JOURNAL   Genomics 54 (1), 186-188 (1998)
   PUBMED   9806853
REFERENCE   6  (residues 1 to 871)
  AUTHORS   Irie,M., Hata,Y., Takeuchi,M., Ichtchenko,K., Toyoda,A., Hirao,K.,
            Takai,Y., Rosahl,T.W. and Sudhof,T.C.
  TITLE     Binding of neuroligins to PSD-95
  JOURNAL   Science 277 (5331), 1511-1515 (1997)
   PUBMED   9278515
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Hsueh,Y.P., Kim,E. and Sheng,M.
  TITLE     Disulfide-linked head-to-head multimerization in the mechanism of
            ion channel clustering by PSD-95
  JOURNAL   Neuron 18 (5), 803-814 (1997)
   PUBMED   9182804
REFERENCE   8  (residues 1 to 871)
  AUTHORS   Kim,E., Cho,K.O., Rothschild,A. and Sheng,M.
  TITLE     Heteromultimerization and NMDA receptor-clustering activity of
            Chapsyn-110, a member of the PSD-95 family of proteins
  JOURNAL   Neuron 17 (1), 103-113 (1996)
   PUBMED   8755482
REFERENCE   9  (residues 1 to 871)
  AUTHORS   Brenman,J.E., Chao,D.S., Gee,S.H., McGee,A.W., Craven,S.E.,
            Santillano,D.R., Wu,Z., Huang,F., Xia,H., Peters,M.F.,
            Froehner,S.C. and Bredt,D.S.
  TITLE     Interaction of nitric oxide synthase with the postsynaptic density
            protein PSD-95 and alpha1-syntrophin mediated by PDZ domains
  JOURNAL   Cell 84 (5), 757-767 (1996)
   PUBMED   8625413
REFERENCE   10 (residues 1 to 871)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001825.4, AP001791.4,
            AP003305.2, AP002797.3, AC023118.4, AP002751.3, AP002370.5,
            AP000773.4 and AP003026.2.
            
            On May 5, 2017 this sequence version replaced XP_016872761.1.
            
            Summary: This gene encodes a member of the membrane-associated
            guanylate kinase (MAGUK) family. The encoded protein forms a
            heterodimer with a related family member that may interact at
            postsynaptic sites to form a multimeric scaffold for the clustering
            of receptors, ion channels, and associated signaling proteins.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. Additional transcript variants have been
            described, but their full-length nature is not known. [provided by
            RefSeq, Dec 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.234514.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.1"
     Protein         1..871
                     /product="disks large homolog 2 isoform 9"
                     /note="channel-associated protein of synapses, 110kDa;
                     postsynaptic density protein PSD-93; channel-associated
                     protein of synapse-110; discs, large homolog 2,
                     chapsyn-110; protein phosphatase 1, regulatory subunit 58;
                     disks large homolog 2"
                     /calculated_mol_wt=96810
     Region          34..116
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          115..203
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(126..132,149,152,182,186,189..190)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          212..296
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(221..227,244,247,277,281,284..285)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          297..364
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          437..527
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(449..455,466,469,499,503,506..507)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          553..626
                     /region_name="SH3_DLG2"
                     /note="Src Homology 3 domain of Disks Large homolog 2;
                     cd12032"
                     /db_xref="CDD:212965"
     Site            order(561,583..584)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212965"
     Site            order(564,566,569,578,596..597,616,618..619)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212965"
     Region          680..858
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..871
                     /gene="DLG2"
                     /gene_synonym="chapsyn-110; PPP1R58; PSD-93; PSD93"
                     /coded_by="NM_001351276.2:546..3161"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:1740"
                     /db_xref="HGNC:HGNC:2901"
                     /db_xref="MIM:603583"
ORIGIN      
        1 mspvvkdpdc ftpmichckv actnntlslm fgckyryqde daphdhslpr lthevrgpel
       61 vhvseknlsq ienvhgyvlq shisplkasp apiivntdtl dtipyvngte ieyefeeitl
      121 ergnsglgfs iaggtdnphi gddpgifitk iipggaaaed grlrvndcil rvnevdvsev
      181 shskavealk eagsivrlyv rrrrpiletv veiklfkgpk glgfsiaggv gnqhipgdns
      241 iyvtkiidgg aaqkdgrlqv gdrllmvnny sleevtheea vailkntsev vylkvgkptt
      301 iymtdpygpp dithsysppm enhllsgnng tleyktslpp ispgryspip khmlvdddyt
      361 rppepvystv nklcdkpasp rhyspvecdk sfllsapysh yhlgllpdse mtshsqhsta
      421 trqpsmtlqr avslegeprk vvlhkgstgl gfnivggedg egifvsfila ggpadlsgel
      481 qrgdqilsvn gidlrgashe qaaaalkgag qtvtiiaqyq pedyarfeak ihdlreqmmn
      541 hsmssgsgsl rtnqkrslyv ramfdydksk dsglpsqgls fkygdilhvi nasddewwqa
      601 rrvmlegdse emgvipskrr verkerarlk tvkfnakpgv idskgdipgl gddgygtktl
      661 rgqedlilsy epvtrqeiny trpviilgpm kdrinddlis efpdkfgscv phttrpkrdy
      721 evdgrdyhfv isreqmekdi qehkfieagq yndnlygtsv qsvrfvaerg khcildvsgn
      781 aikrlqvaql ypiaifikpr sleplmemnk rlteeqakkt ydraikleqe fgeyftaivq
      841 gdtlediynq cklvieeqsg pfiwipskek l
//
LOCUS       NP_004399                864 aa            linear   PRI 21-NOV-2025
DEFINITION  dynamin-1 isoform 1 [Homo sapiens].
ACCESSION   NP_004399
VERSION     NP_004399.2
DBSOURCE    REFSEQ: accession NM_004408.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 864)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 864)
  AUTHORS   Pierga,A., Matusiak,R., Cauhape,M., Branchu,J., Danglot,L.,
            Boutry,M. and Darios,F.
  TITLE     Spatacsin regulates directionality of lysosome trafficking by
            promoting the degradation of its partner AP5Z1
  JOURNAL   PLoS Biol 21 (10), e3002337 (2023)
   PUBMED   37871017
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 864)
  AUTHORS   Parthasarathy,S., Ruggiero,S.M., Gelot,A., Soardi,F.C.,
            Ribeiro,B.F.R., Pires,D.E.V., Ascher,D.B., Schmitt,A., Rambaud,C.,
            Represa,A., Xie,H.M., Lusk,L., Wilmarth,O., McDonnell,P.P.,
            Juarez,O.A., Grace,A.N., Buratti,J., Mignot,C., Gras,D., Nava,C.,
            Pierce,S.R., Keren,B., Kennedy,B.C., Pena,S.D.J., Helbig,I. and
            Cuddapah,V.A.
  TITLE     A recurrent de novo splice site variant involving DNM1 exon 10a
            causes developmental and epileptic encephalopathy through a
            dominant-negative mechanism
  JOURNAL   Am J Hum Genet 109 (12), 2253-2269 (2022)
   PUBMED   36413998
  REMARK    GeneRIF: A recurrent de novo splice site variant involving DNM1
            exon 10a causes developmental and epileptic encephalopathy through
            a dominant-negative mechanism.
REFERENCE   4  (residues 1 to 864)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 864)
  AUTHORS   Liu,J., Alvarez,F.J.D., Clare,D.K., Noel,J.K. and Zhang,P.
  TITLE     CryoEM structure of the super-constricted two-start dynamin 1
            filament
  JOURNAL   Nat Commun 12 (1), 5393 (2021)
   PUBMED   34518553
  REMARK    GeneRIF: CryoEM structure of the super-constricted two-start
            dynamin 1 filament.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 864)
  AUTHORS   Timm,D., Salim,K., Gout,I., Guruprasad,L., Waterfield,M. and
            Blundell,T.
  TITLE     Crystal structure of the pleckstrin homology domain from dynamin
  JOURNAL   Nat Struct Biol 1 (11), 782-788 (1994)
   PUBMED   7634088
REFERENCE   7  (residues 1 to 864)
  AUTHORS   Ferguson,K.M., Lemmon,M.A., Schlessinger,J. and Sigler,P.B.
  TITLE     Crystal structure at 2.2 A resolution of the pleckstrin homology
            domain from human dynamin
  JOURNAL   Cell 79 (2), 199-209 (1994)
   PUBMED   7954789
REFERENCE   8  (residues 1 to 864)
  AUTHORS   Downing,A.K., Driscoll,P.C., Gout,I., Salim,K., Zvelebil,M.J. and
            Waterfield,M.D.
  TITLE     Three-dimensional solution structure of the pleckstrin homology
            domain from dynamin
  JOURNAL   Curr Biol 4 (10), 884-891 (1994)
   PUBMED   7850421
REFERENCE   9  (residues 1 to 864)
  AUTHORS   van der Bliek,A.M., Redelmeier,T.E., Damke,H., Tisdale,E.J.,
            Meyerowitz,E.M. and Schmid,S.L.
  TITLE     Mutations in human dynamin block an intermediate stage in coated
            vesicle formation
  JOURNAL   J Cell Biol 122 (3), 553-563 (1993)
   PUBMED   8101525
REFERENCE   10 (residues 1 to 864)
  AUTHORS   Obar,R.A., Collins,C.A., Hammarback,J.A., Shpetner,H.S. and
            Vallee,R.B.
  TITLE     Molecular cloning of the microtubule-associated mechanochemical
            enzyme dynamin reveals homology with a new family of GTP-binding
            proteins
  JOURNAL   Nature 347 (6290), 256-261 (1990)
   PUBMED   2144893
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA221568.1, BC050279.1,
            BC063850.1 and AI660320.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 15, 2005 this sequence version replaced NP_004399.1.
            
            Summary: This gene encodes a member of the dynamin subfamily of
            GTP-binding proteins. The encoded protein possesses unique
            mechanochemical properties used to tubulate and sever membranes,
            and is involved in clathrin-mediated endocytosis and other
            vesicular trafficking processes. Actin and other cytoskeletal
            proteins act as binding partners for the encoded protein, which can
            also self-assemble leading to stimulation of GTPase activity. More
            than sixty highly conserved copies of the 3' region of this gene
            are found elsewhere in the genome, particularly on chromosomes Y
            and 15. Alternatively spliced transcript variants encoding
            different isoforms have been described. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1). Isoform 1 has been referred to as internal form 1 and the long
            C-terminal form.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L07807.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154125
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372923.8/ ENSP00000362014.4
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..864
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..864
                     /product="dynamin-1 isoform 1"
                     /EC_number="3.6.5.5"
                     /note="dynamin I"
                     /calculated_mol_wt=97278
     Region          6..245
                     /region_name="DYNc"
                     /note="Dynamin, GTPase; smart00053"
                     /db_xref="CDD:197491"
     Region          38..45
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05193.2)"
     Site            38..45
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(39,41..46,59..60,65,136,206,208..209,235..239,242)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(40..41,140,153,178,180,182..185,187..188,209,
                     211..214,238..240)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Region          64..66
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05193.2)"
     Site            65
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            69..71
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39053; propagated from
                     UniProtKB/Swiss-Prot (Q05193.2)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P39053; propagated from
                     UniProtKB/Swiss-Prot (Q05193.2)"
     Region          136..139
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05193.2)"
     Site            136..139
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(138..139,169..170)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Region          205..208
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05193.2)"
     Site            205..208
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          215..502
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Region          235..238
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05193.2)"
     Site            235..237
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39053; propagated from
                     UniProtKB/Swiss-Prot (Q05193.2)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21575; propagated from
                     UniProtKB/Swiss-Prot (Q05193.2)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39053; propagated from
                     UniProtKB/Swiss-Prot (Q05193.2)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P39053; propagated from
                     UniProtKB/Swiss-Prot (Q05193.2)"
     Region          520..629
                     /region_name="PH_dynamin"
                     /note="Dynamin pleckstrin homology (PH) domain; cd01256"
                     /db_xref="CDD:269958"
     Site            order(520,522..523,525,542,611..612,615,618..619,622)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:269958"
     Region          655..745
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     Region          <747..844
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          767..864
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05193.2)"
     Site            774
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta.
                     /evidence=ECO:0000269|PubMed:29668686; propagated from
                     UniProtKB/Swiss-Prot (Q05193.2)"
     Site            778
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21575; propagated from
                     UniProtKB/Swiss-Prot (Q05193.2)"
     Site            796
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P39053; propagated from
                     UniProtKB/Swiss-Prot (Q05193.2)"
     Site            822
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21575; propagated from
                     UniProtKB/Swiss-Prot (Q05193.2)"
     Site            851
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21575; propagated from
                     UniProtKB/Swiss-Prot (Q05193.2)"
     Site            857
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21575; propagated from
                     UniProtKB/Swiss-Prot (Q05193.2)"
     CDS             1..864
                     /gene="DNM1"
                     /gene_synonym="DEE31; DEE31A; DEE31B; DNM; EIEE31"
                     /coded_by="NM_004408.4:93..2687"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6895.1"
                     /db_xref="GeneID:1759"
                     /db_xref="HGNC:HGNC:2972"
                     /db_xref="MIM:602377"
ORIGIN      
        1 mgnrgmedli plvnrlqdaf saigqnadld lpqiavvggq sagkssvlen fvgrdflprg
       61 sgivtrrplv lqlvnattey aeflhckgkk ftdfeevrle ieaetdrvtg tnkgispvpi
      121 nlrvysphvl nltlvdlpgm tkvpvgdqpp diefqirdml mqfvtkencl ilavspansd
      181 lansdalkva kevdpqgqrt igvitkldlm degtdardvl enkllplrrg yigvvnrsqk
      241 didgkkdita alaaerkffl shpsyrhlad rmgtpylqkv lnqqltnhir dtlpglrnkl
      301 qsqllsieke veeyknfrpd dparktkall qmvqqfavdf ekriegsgdq idtyelsgga
      361 rinrifherf pfelvkmefd ekelrreisy aiknihgirt glftpdmafe tivkkqvkki
      421 repclkcvdm viselistvr qctkklqqyp rlreemeriv tthireregr tkeqvmllid
      481 ielaymntnh edfigfanaq qrsnqmnkkk tsgnqdeilv irkgwltinn igimkggske
      541 ywfvltaenl swykddeeke kkymlsvdnl klrdvekgfm sskhifalfn teqrnvykdy
      601 rqlelacetq eevdswkasf lragvyperv gdkekasete engsdsfmhs mdpqlerqve
      661 tirnlvdsym aivnktvrdl mpktimhlmi nntkefifse llanlyscgd qntlmeesae
      721 qaqrrdemlr myhalkeals iigdintttv stpmpppvdd swlqvqsvpa grrsptsspt
      781 pqrrapavpp arpgsrgpap gpppagsalg gappvpsrpg aspdpfgppp qvpsrpnrap
      841 pgvpsrsgqa spsrpesprp pfdl
//
LOCUS       NP_001362208             593 aa            linear   PRI 21-NOV-2025
DEFINITION  complement factor I isoform 5 preproprotein [Homo sapiens].
ACCESSION   NP_001362208
VERSION     NP_001362208.1
DBSOURCE    REFSEQ: accession NM_001375279.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Moreno,R. and Broderick,L.
  TITLE     Complement factor I deficiency: Diverse phenotypes
  JOURNAL   J Allergy Clin Immunol 156 (2), 305-307 (2025)
   PUBMED   40127737
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Schwotzer,N., Fakhouri,F., Martins,P.V., Delmas,Y., Caillard,S.,
            Zuber,J., Moranne,O., Mesnard,L., Fremeaux-Bacchi,V. and
            El-Sissy,C.
  TITLE     Hot Spot of Complement Factor I Rare Variant p.Ile357Met in
            Patients With Hemolytic Uremic Syndrome
  JOURNAL   Am J Kidney Dis 84 (2), 244-249 (2024)
   PUBMED   38423159
  REMARK    GeneRIF: Hot Spot of Complement Factor I Rare Variant p.Ile357Met
            in Patients With Hemolytic Uremic Syndrome.
REFERENCE   3  (residues 1 to 593)
  AUTHORS   Felberg,A., Bienkowski,M., Stokowy,T., Myszczynski,K.,
            Polakiewicz,Z., Kitowska,K., Sadej,R., Mohlin,F., Kuzniewska,A.,
            Kowalska,D., Stasilojc,G., Jongerius,I., Spaapen,R.,
            Mesa-Guzman,M., Montuenga,L.M., Blom,A.M., Pio,R. and Okroj,M.
  TITLE     Elevated expression of complement factor I in lung cancer cells
            associates with shorter survival-Potentially via non-canonical
            mechanism
  JOURNAL   Transl Res 269, 1-13 (2024)
   PUBMED   38395390
  REMARK    GeneRIF: Elevated expression of complement factor I in lung cancer
            cells associates with shorter survival-Potentially via
            non-canonical mechanism.
REFERENCE   4  (residues 1 to 593)
  AUTHORS   Massey,V., Nguyen,C.E., Francois,T., De Bruycker,J.J., Bonnefoy,A.,
            Lapeyraque,A.L. and Decaluwe,H.
  TITLE     CNS Inflammation as the First Sign of Complement Factor I
            Deficiency: A Severe Myelitis Treated With Intense Immunotherapy
            and Eculizumab
  JOURNAL   Neurol Neuroimmunol Neuroinflamm 11 (2), e200191 (2024)
   PUBMED   38134378
  REMARK    GeneRIF: CNS Inflammation as the First Sign of Complement Factor I
            Deficiency.
REFERENCE   5  (residues 1 to 593)
  AUTHORS   van de Ven,J.P., Nilsson,S.C., Tan,P.L., Buitendijk,G.H.,
            Ristau,T., Mohlin,F.C., Nabuurs,S.B., Schoenmaker-Koller,F.E.,
            Smailhodzic,D., Campochiaro,P.A., Zack,D.J., Duvvari,M.R.,
            Bakker,B., Paun,C.C., Boon,C.J., Uitterlinden,A.G., Liakopoulos,S.,
            Klevering,B.J., Fauser,S., Daha,M.R., Katsanis,N., Klaver,C.C.,
            Blom,A.M., Hoyng,C.B. and den Hollander,A.I.
  TITLE     A functional variant in the CFI gene confers a high risk of
            age-related macular degeneration
  JOURNAL   Nat Genet 45 (7), 813-817 (2013)
   PUBMED   23685748
  REMARK    GeneRIF: these findings demonstrate that rare, highly penetrant
            mutations in CFI contribute to the genetic burden of age-related
            macular degeneration.
REFERENCE   6  (residues 1 to 593)
  AUTHORS   Martin,B. and Smith,R.J.H.
  TITLE     C3 Glomerulopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301598
REFERENCE   7  (residues 1 to 593)
  AUTHORS   Noris,M., Bresin,E., Mele,C. and Remuzzi,G.
  TITLE     Genetic Atypical Hemolytic-Uremic Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301541
REFERENCE   8  (residues 1 to 593)
  AUTHORS   DiScipio,R.G.
  TITLE     Ultrastructures and interactions of complement factors H and I
  JOURNAL   J Immunol 149 (8), 2592-2599 (1992)
   PUBMED   1401896
REFERENCE   9  (residues 1 to 593)
  AUTHORS   Shiang,R., Murray,J.C., Morton,C.C., Buetow,K.H., Wasmuth,J.J.,
            Olney,A.H., Sanger,W.G. and Goldberger,G.
  TITLE     Mapping of the human complement factor I gene to 4q25
  JOURNAL   Genomics 4 (1), 82-86 (1989)
   PUBMED   2563353
REFERENCE   10 (residues 1 to 593)
  AUTHORS   Catterall,C.F., Lyons,A., Sim,R.B., Day,A.J. and Harris,T.J.
  TITLE     Characterization of primary amino acid sequence of human complement
            control protein factor I from an analysis of cDNA clones
  JOURNAL   Biochem J 242 (3), 849-856 (1987)
   PUBMED   2954545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC126283.3 and AC004067.1.
            
            Summary: This gene encodes a serine proteinase that is essential
            for regulating the complement cascade. The encoded preproprotein is
            cleaved to produce both heavy and light chains, which are linked by
            disulfide bonds to form a heterodimeric glycoprotein. This
            heterodimer can cleave and inactivate the complement components C4b
            and C3b, and it prevents the assembly of the C3 and C5 convertase
            enzymes. Defects in this gene cause complement factor I deficiency,
            an autosomal recessive disease associated with a susceptibility to
            pyogenic infections. Mutations in this gene have been associated
            with a predisposition to atypical hemolytic uremic syndrome, a
            disease characterized by acute renal failure, microangiopathic
            hemolytic anemia and thrombocytopenia. Primary glomerulonephritis
            with immune deposits and age-related macular degeneration are other
            conditions associated with mutations of this gene. [provided by
            RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..593
                     /product="complement factor I isoform 5 preproprotein"
                     /EC_number="3.4.21.45"
                     /note="C3b-inactivator; Konglutinogen-activating factor;
                     complement factor I heavy chain; complement component I;
                     C3B/C4B inactivator; complement control protein factor I;
                     light chain of factor I"
                     /calculated_mol_wt=64770
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2281
     Region          43..108
                     /region_name="FIMAC"
                     /note="factor I membrane attack complex; smart00057"
                     /db_xref="CDD:214493"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Region          114..215
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     Region          224..256
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(227,235,246..247)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(239,242,246,252..253)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            249..253
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          257..293
                     /region_name="Ldl_recept_a"
                     /note="Low-density lipoprotein receptor domain class A;
                     pfam00057"
                     /db_xref="CDD:395011"
     Site            order(264,272,283..284)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(276,279,283,289..290)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            286..290
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          340..>511
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            340
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            464
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Site            494
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     CDS             1..593
                     /gene="CFI"
                     /gene_synonym="AHUS3; ARMD13; C3b-INA; C3BINA; FI; IF;
                     KAF"
                     /coded_by="NM_001375279.1:29..1810"
                     /note="isoform 5 preproprotein is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:3426"
                     /db_xref="HGNC:HGNC:5394"
                     /db_xref="MIM:217030"
ORIGIN      
        1 mkllhvfllf lcfhlrfckv tytsqedlve kkclakkyth lscdkvfcqp wqrciegtcv
       61 cklpyqcpkn gtavcatnrr sfptycqqks leclhpgtkf lnngtctaeg kfsvslkhgn
      121 tdsegivevk lvdqdktmfi cksswsmrea nvacldlgfq qgadtqrrfk lsdlsinste
      181 clhvhcrgle tslaectftk rrtmgyqdfa dvvcytqkad spmddffqcv ngkyisqmka
      241 cdgindcgdq sdelcckacq gkgfhcksgv cipsqyqcng evdcitgede vgcagfasvt
      301 qeeteiltad mdaerrriks llpklscgvk nrmhirrkri vggkraqlgd lpwqvaikda
      361 sgitcggiyi ggcwiltaah clraskthry qiwttvvdwi hpdlkrivie yvdriifhen
      421 ynagtyqndi aliemkkdgn kkdcelprsi pacvpwspyl fqpndtcivs gwgrekdner
      481 vfslqwgevk lisncskfyg nrfyekemec adccsvaqag vqwhdlsslq pppprfkqfs
      541 clslpsswdy rhlpprpesr svpqagvqwc nlsslqhpst swvqvillpp ppe
//
LOCUS       NP_001387285             309 aa            linear   PRI 21-NOV-2025
DEFINITION  single-stranded DNA-binding protein 2 isoform 24 [Homo sapiens].
ACCESSION   NP_001387285
VERSION     NP_001387285.1
DBSOURCE    REFSEQ: accession NM_001400356.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Schwab,C., Roberts,K., Boer,J.M., Gohring,G., Steinemann,D.,
            Vora,A., Macartney,C., Hough,R., Thorn,Z., Dillon,R., Escherich,G.,
            Cazzaniga,G., Schlegelberger,B., Loh,M., den Boer,M.L.,
            Moorman,A.V. and Harrison,C.J.
  TITLE     SSBP2-CSF1R is a recurrent fusion in B-lineage acute lymphoblastic
            leukemia with diverse genetic presentation and variable outcome
  JOURNAL   Blood 137 (13), 1835-1838 (2021)
   PUBMED   33197935
  REMARK    GeneRIF: SSBP2-CSF1R is a recurrent fusion in B-lineage acute
            lymphoblastic leukemia with diverse genetic presentation and
            variable outcome.
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Wang,H., Kim,J., Wang,Z., Yan,X.X., Dean,A. and Xu,W.
  TITLE     Crystal structure of human LDB1 in complex with SSBP2
  JOURNAL   Proc Natl Acad Sci U S A 117 (2), 1042-1048 (2020)
   PUBMED   31892537
  REMARK    GeneRIF: Single-stranded DNA binding proteins (SSBPs) interact
            specifically with the LDB/Chip conserved domain (LCCD) of LDB
            proteins and stabilize LDBs by preventing their proteasomal
            degradation, thus promoting their functions in gene regulation.
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Kim,H., Kim,Y., Bang,S., Park,S., Jee,S., Sim,J., Shin,S.J.,
            Paik,S.S. and Jang,K.
  TITLE     Low Expression of Single-stranded DNA Binding Protein 2 (SSBP2)
            Predicts Unfavourable Postoperative Outcomes in Patients With Clear
            Cell Renal Cell Carcinoma
  JOURNAL   In Vivo 34 (1), 101-107 (2020)
   PUBMED   31882468
  REMARK    GeneRIF: CcRCC with low SSBP2 expression was associated with
            adverse clinicopathological characteristics and poor patient
            outcomes.
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Fleisig,H.B., Orazio,N.I., Liang,H., Tyler,A.F., Adams,H.P.,
            Weitzman,M.D. and Nagarajan,L.
  TITLE     Adenoviral E1B55K oncoprotein sequesters candidate leukemia
            suppressor sequence-specific single-stranded DNA-binding protein 2
            into aggresomes
  JOURNAL   Oncogene 26 (33), 4797-4805 (2007)
   PUBMED   17311003
  REMARK    GeneRIF: Results suggest that subverting SSBP2 function by
            oncoprotein E1B55K may contribute to cell transformation by viral
            oncoproteins.
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Liang,H., Samanta,S. and Nagarajan,L.
  TITLE     SSBP2, a candidate tumor suppressor gene, induces growth arrest and
            differentiation of myeloid leukemia cells
  JOURNAL   Oncogene 24 (16), 2625-2634 (2005)
   PUBMED   15782145
  REMARK    GeneRIF: Our findings are consistent with human SSBP2 being a novel
            regulator of hematopoietic growth and differentiation, whose loss
            confers a block in differentiation advantage to myeloid leukemic
            cells.
REFERENCE   8  (residues 1 to 309)
  AUTHORS   Castro,P., Liang,H., Liang,J.C. and Nagarajan,L.
  TITLE     A novel, evolutionarily conserved gene family with putative
            sequence-specific single-stranded DNA-binding activity
  JOURNAL   Genomics 80 (1), 78-85 (2002)
   PUBMED   12079286
  REMARK    GeneRIF: Member of a closely related, evolutionarily conserved, and
            ubiquitously expressed gene family, potential tumor suppressor
REFERENCE   9  (residues 1 to 309)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 309)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016562.7, AC093250.3,
            AC026419.5 and AC010623.10.
            
            Summary: This gene encodes a subunit of a protein complex that
            interacts with single-stranded DNA and is involved in the DNA
            damage response and maintenance of genome stability. The encoded
            protein may also play a role in telomere repair. A variant of this
            gene may be associated with survival in human glioblastoma
            patients. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.86799.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.1"
     Protein         1..309
                     /product="single-stranded DNA-binding protein 2 isoform
                     24"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein 2"
                     /calculated_mol_wt=31552
     Region          32..286
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     CDS             1..309
                     /gene="SSBP2"
                     /gene_synonym="HSPC116; SOSS-B2"
                     /coded_by="NM_001400356.1:330..1259"
                     /note="isoform 24 is encoded by transcript variant 27"
                     /db_xref="GeneID:23635"
                     /db_xref="HGNC:HGNC:15831"
                     /db_xref="MIM:607389"
ORIGIN      
        1 mitrdgvssc ypgwsrspdl vihlprppev lglqsaaaap spvlgnippg dgmpvgpvpp
       61 gffqpfmspr ypggprpplr ipnqalggvp gsqpllpsgm dptrqqghpn mggpmqrmtp
      121 prgmvplgpq sdpwlslqny ggamrpplna lggpgmpgmn mgpgggrpwp nptnansipy
      181 ssaspgnyvg ppggggppgt pimpspadst nsgdnmytlm navppgpnrp nfpmgpgsdg
      241 pmgglggmes hhmngslgsg dmdsisknsp nnmslsnqpg tprddgemgg nflnpfqses
      301 yspsmtmsv
//
LOCUS       NP_001265720             253 aa            linear   PRI 21-NOV-2025
DEFINITION  replication factor C subunit 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001265720
VERSION     NP_001265720.1
DBSOURCE    REFSEQ: accession NM_001278791.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Wang,F., He,Q., Yao,N.Y., O'Donnell,M.E. and Li,H.
  TITLE     The human ATAD5 has evolved unique structural elements to function
            exclusively as a PCNA unloader
  JOURNAL   Nat Struct Mol Biol 31 (11), 1680-1691 (2024)
   PUBMED   38871854
REFERENCE   3  (residues 1 to 253)
  AUTHORS   He,Q., Wang,F., O'Donnell,M.E. and Li,H.
  TITLE     Cryo-EM reveals a nearly complete PCNA loading process and unique
            features of the human alternative clamp loader CTF18-RFC
  JOURNAL   Proc Natl Acad Sci U S A 121 (18), e2319727121 (2024)
   PUBMED   38669181
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Lou,F. and Zhang,M.
  TITLE     RFC2 promotes aerobic glycolysis and progression of colorectal
            cancer
  JOURNAL   BMC Gastroenterol 23 (1), 353 (2023)
   PUBMED   37821801
  REMARK    GeneRIF: RFC2 promotes aerobic glycolysis and progression of
            colorectal cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Li,H., Chai,L., Ding,Z. and He,H.
  TITLE     CircCOL1A2 Sponges MiR-1286 to Promote Cell Invasion and Migration
            of Gastric Cancer by Elevating Expression of USP10 to Downregulate
            RFC2 Ubiquitination Level
  JOURNAL   J Microbiol Biotechnol 32 (7), 938-948 (2022)
   PUBMED   35791074
  REMARK    GeneRIF: CircCOL1A2 Sponges MiR-1286 to Promote Cell Invasion and
            Migration of Gastric Cancer by Elevating Expression of USP10 to
            Downregulate RFC2 Ubiquitination Level.
REFERENCE   6  (residues 1 to 253)
  AUTHORS   Uhlmann,F., Cai,J., Flores-Rozas,H., Dean,F.B., Finkelstein,J.,
            O'Donnell,M. and Hurwitz,J.
  TITLE     In vitro reconstitution of human replication factor C from its five
            subunits
  JOURNAL   Proc Natl Acad Sci U S A 93 (13), 6521-6526 (1996)
   PUBMED   8692848
REFERENCE   7  (residues 1 to 253)
  AUTHORS   Peoples,R., Perez-Jurado,L., Wang,Y.K., Kaplan,P. and Francke,U.
  TITLE     The gene for replication factor C subunit 2 (RFC2) is within the
            7q11.23 Williams syndrome deletion
  JOURNAL   Am J Hum Genet 58 (6), 1370-1373 (1996)
   PUBMED   8651315
REFERENCE   8  (residues 1 to 253)
  AUTHORS   Okumura,K., Nogami,M., Taguchi,H., Dean,F.B., Chen,M., Pan,Z.Q.,
            Hurwitz,J., Shiratori,A., Murakami,Y., Ozawa,K. et al.
  TITLE     Assignment of the 36.5-kDa (RFC5), 37-kDa (RFC4), 38-kDa (RFC3),
            and 40-kDa (RFC2) subunit genes of human replication factor C to
            chromosome bands 12q24.2-q24.3, 3q27, 13q12.3-q13, and 7q11.23
  JOURNAL   Genomics 25 (1), 274-278 (1995)
   PUBMED   7774928
REFERENCE   9  (residues 1 to 253)
  AUTHORS   Pan,Z.Q., Chen,M. and Hurwitz,J.
  TITLE     The subunits of activator 1 (replication factor C) carry out
            multiple functions essential for proliferating-cell nuclear
            antigen-dependent DNA synthesis
  JOURNAL   Proc Natl Acad Sci U S A 90 (1), 6-10 (1993)
   PUBMED   8093561
REFERENCE   10 (residues 1 to 253)
  AUTHORS   Chen,M., Pan,Z.Q. and Hurwitz,J.
  TITLE     Sequence and expression in Escherichia coli of the 40-kDa subunit
            of activator 1 (replication factor C) of HeLa cells
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 2516-2520 (1992)
   PUBMED   1313560
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY046046.1, HY056452.1,
            BM563468.1, BC002813.1 and AW450467.1.
            
            Summary: This gene encodes a member of the activator 1 small
            subunits family. The elongation of primed DNA templates by DNA
            polymerase delta and epsilon requires the action of the accessory
            proteins, proliferating cell nuclear antigen (PCNA) and replication
            factor C (RFC). Replication factor C, also called activator 1, is a
            protein complex consisting of five distinct subunits. This gene
            encodes the 40 kD subunit, which has been shown to be responsible
            for binding ATP and may help promote cell survival. Disruption of
            this gene is associated with Williams syndrome. Alternatively
            spliced transcript variants encoding distinct isoforms have been
            described. A pseudogene of this gene has been defined on chromosome
            2. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (3) uses an alternate splice site
            in its 5' UTR, and initiates translation at a downstream start
            codon, compared to variant 1. The encoded isoform (3) has a shorter
            N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1917214.1,
                                           SRR14038192.4037610.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..253
                     /product="replication factor C subunit 2 isoform 3"
                     /note="A1 40 kDa subunit; RF-C 40 kDa subunit; activator 1
                     subunit 2; replication factor C (activator 1) 2, 40kDa"
                     /calculated_mol_wt=28514
     Region          <2..247
                     /region_name="PLN03025"
                     /note="replication factor C subunit; Provisional"
                     /db_xref="CDD:178596"
     CDS             1..253
                     /gene="RFC2"
                     /gene_synonym="RFC40"
                     /coded_by="NM_001278791.2:422..1183"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:5982"
                     /db_xref="HGNC:HGNC:9970"
                     /db_xref="MIM:600404"
ORIGIN      
        1 mlelnasndr gidvvrnkik mfaqqkvtlp kgrhkiiild eadsmtdgaq qalrrtmeiy
       61 skttrfalac nasdkiiepi qsrcavlryt kltdaqiltr lmnviekerv pytddgleai
      121 iftaqgdmrq alnnlqstfs gfgfinsenv fkvcdephpl lvkemiqhcv nanideayki
      181 lahlwhlgys pediignifr vcktfqmaey lklefikeig ythmkiaegv nsllqmagll
      241 arlcqktmap vas
//
LOCUS       NP_001381901            1099 aa            linear   PRI 21-NOV-2025
DEFINITION  mitotic deacetylase-associated SANT domain protein isoform 2 [Homo
            sapiens].
ACCESSION   NP_001381901 XP_005268262
VERSION     NP_001381901.1
DBSOURCE    REFSEQ: accession NM_001394972.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Lu,Y.A., Sun,J., Wang,L., Wang,M., Wu,Y., Getachew,A.,
            Matthews,R.C., Li,H., Peng,W.G., Zhang,J., Lu,R. and Zhou,Y.
  TITLE     ELM2-SANT Domain-Containing Scaffolding Protein 1 Regulates
            Differentiation and Maturation of Cardiomyocytes Derived From
            Human-Induced Pluripotent Stem Cells
  JOURNAL   J Am Heart Assoc 13 (13), e034816 (2024)
   PUBMED   38904247
  REMARK    GeneRIF: ELM2-SANT Domain-Containing Scaffolding Protein 1
            Regulates Differentiation and Maturation of Cardiomyocytes Derived
            From Human-Induced Pluripotent Stem Cells.
REFERENCE   3  (residues 1 to 1099)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1099)
  AUTHORS   Turnbull,R.E., Fairall,L., Saleh,A., Kelsall,E., Morris,K.L.,
            Ragan,T.J., Savva,C.G., Chandru,A., Millard,C.J., Makarova,O.V.,
            Smith,C.J., Roseman,A.M., Fry,A.M., Cowley,S.M. and Schwabe,J.W.R.
  TITLE     The MiDAC histone deacetylase complex is essential for embryonic
            development and has a unique multivalent structure
  JOURNAL   Nat Commun 11 (1), 3252 (2020)
   PUBMED   32591534
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1099)
  AUTHORS   Itoh,T., Fairall,L., Muskett,F.W., Milano,C.P., Watson,P.J.,
            Arnaudo,N., Saleh,A., Millard,C.J., El-Mezgueldi,M., Martino,F. and
            Schwabe,J.W.
  TITLE     Structural and functional characterization of a cell cycle
            associated HDAC1/2 complex reveals the structural basis for complex
            assembly and nucleosome targeting
  JOURNAL   Nucleic Acids Res 43 (4), 2033-2044 (2015)
   PUBMED   25653165
REFERENCE   6  (residues 1 to 1099)
  AUTHORS   Bantscheff,M., Hopf,C., Savitski,M.M., Dittmann,A., Grandi,P.,
            Michon,A.M., Schlegl,J., Abraham,Y., Becher,I., Bergamini,G.,
            Boesche,M., Delling,M., Dumpelfeld,B., Eberhard,D., Huthmacher,C.,
            Mathieson,T., Poeckel,D., Reader,V., Strunk,K., Sweetman,G.,
            Kruse,U., Neubauer,G., Ramsden,N.G. and Drewes,G.
  TITLE     Chemoproteomics profiling of HDAC inhibitors reveals selective
            targeting of HDAC complexes
  JOURNAL   Nat Biotechnol 29 (3), 255-265 (2011)
   PUBMED   21258344
  REMARK    GeneRIF: C14ORF43 (MIDEAS) is part of a mitotic deacetylase complex
            (MIDAC) formed in cell division with HDAC1/HDAC2 and DNTTIP1.
REFERENCE   7  (residues 1 to 1099)
  AUTHORS   Bandyopadhyay,S., Chiang,C.Y., Srivastava,J., Gersten,M., White,S.,
            Bell,R., Kurschner,C., Martin,C., Smoot,M., Sahasrabudhe,S.,
            Barber,D.L., Chanda,S.K. and Ideker,T.
  TITLE     A human MAP kinase interactome
  JOURNAL   Nat Methods 7 (10), 801-805 (2010)
   PUBMED   20936779
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005520.2 and AC006146.2.
            
            On May 13, 2021 this sequence version replaced XP_005268262.1.
            
            Transcript Variant: This variant (4), as well as variant 3, encodes
            the longer isoform (2).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.448205.1,
                                           SRR18074969.2463589.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..1099
                     /product="mitotic deacetylase-associated SANT domain
                     protein isoform 2"
                     /note="ELM2 and SANT domain-containing protein 1; ELM2 and
                     Myb/SANT-like domain containing 1; ELM2 and Myb/SANT
                     domain containing 1"
                     /calculated_mol_wt=120603
     mat_peptide     1..1045
                     /product="Mitotic deacetylase-associated SANT domain
                     protein. /id=PRO_0000259764"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG2.2)"
                     /calculated_mol_wt=114989
     Region          1..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Region          99..159
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Site            193
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Region          228..264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Region          276..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Region          330..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Region          378..397
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Region          410..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Site            447
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Region          543..563
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Site            704
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Site            709
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Site            715
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Region          723..778
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          832..876
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cl21498"
                     /db_xref="CDD:473887"
     Site            order(833,862..863,865..866,868..870,872..874)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          887..1045
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG2.2)"
     Site            923
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG2.2)"
     CDS             1..1099
                     /gene="MIDEAS"
                     /gene_synonym="C14orf117; C14orf43; c14_5541; ELMSAN1;
                     LSR68"
                     /coded_by="NM_001394972.1:355..3654"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS91901.1"
                     /db_xref="GeneID:91748"
                     /db_xref="HGNC:HGNC:19853"
                     /db_xref="MIM:621074"
ORIGIN      
        1 mnlqaqpkaq nkrkrclfgg qepapkeqpp plqppqqsir vkeeqylghe gpggavstsq
       61 pvelpppssl allnsvvygp ertsaamlsq qvasvkwpns vmapgrgper gggggvsdss
      121 wqqqpgqppp hstwnchsls lysatkgsph pgvgvptyyn hpealkreka ggpqldryvr
      181 pmmpqkvqle vgrpqaplns fhaakkppnq slplqpfqla fghqvnrqvf rqgppppnpv
      241 aafppqkqqq qqqpqqqqqq qqaalpqmpl fenfysmpqq psqqpqdfgl qpagplgqsh
      301 lahhsmapyp fppnpdmnpe lrkallqdsa pqpalpqvqi pfprrsrrls kegilppsal
      361 dgagtqpgqe atgnlflhhw plqqpppgsl gqphpealgf plelresqll pdgerlapng
      421 rereapamgs eegmravstg dcgqvlrggv iqstrrrrra sqeanlltla qkavelaslq
      481 nakdgsgsee krksvlastt kcgvefseps latkrareds gmvpliipvs vpvrtvdpte
      541 aaqagglded gkgpeqnpae hkpsvivtrr rstripgtda qaqaedmnvk legepsvrkp
      601 kqrprpepli iptkagtfia ppvysnitpy qshlrspvrl adhpsersfe lppytpppil
      661 spvregsgly fnaiiststi papppitpks ahrtllrtns aevtppvlsv mgeatpvsie
      721 prinvgsrfq aeiplmrdra laaadphkad lvwqpwedle ssrekqrqve dlltaacssi
      781 fpgagtnqel alhclhesrg diletlnkll lkkplrphnh platyhytgs dqwkmaerkl
      841 fnkgiaiykk dfflvqkliq tktvaqcvef yytykkqvki grngtltfgd vdtsdeksaq
      901 eevevdikts qkfprvplpr respseerle pkrevkeprk egeeevpeiq ekeeqeegre
      961 rsrraaavka tqtlqanesa sdililrshe snapgsaggq asekpregtg ksrralpfse
     1021 kkkktetfsk tqnqentfpc kkcgrvfykv ksrsahmksh aeqekkaaal rlkekeaaaa
     1081 aaaahqqalr eesgagdkg
//
LOCUS       NP_001364438             312 aa            linear   PRI 21-NOV-2025
DEFINITION  UDP-glucuronic acid decarboxylase 1 isoform 9 [Homo sapiens].
ACCESSION   NP_001364438 XP_016860502
VERSION     NP_001364438.1
DBSOURCE    REFSEQ: accession NM_001377509.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Jacobs,J., Lyubenova,H., Potelle,S., Kopp,J., Gerin,I., Chan,W.L.,
            Rodriguez de Los Santos,M., Hulsemann,W., Mensah,M.A.,
            Cormier-Daire,V., Joosten,M., Bruggenwirth,H.T., Stuurman,K.E.,
            Miranda,V., Campeau,P.M., Wittler,L., Graff,J., Mundlos,S.,
            Ibrahim,D.M., Van Schaftingen,E., Fischer-Zirnsak,B., Kornak,U.,
            Ehmke,N. and Bommer,G.T.
  TITLE     A missing enzyme-rescue metabolite as cause of a rare skeletal
            dysplasia
  JOURNAL   Nature 646 (8083), 218-226 (2025)
   PUBMED   40836090
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Brewer,G.
  TITLE     UXS1: a sweet spot for cell death
  JOURNAL   Nat Rev Cancer 24 (1), 3 (2024)
   PUBMED   38030856
  REMARK    GeneRIF: UXS1: a sweet spot for cell death.
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Walsh,R.M. Jr., Polizzi,S.J., Kadirvelraj,R., Howard,W.W. and
            Wood,Z.A.
  TITLE     Man o' war mutation in UDP-alpha-D-xylose synthase favors the
            abortive catalytic cycle and uncovers a latent potential for
            hexamer formation
  JOURNAL   Biochemistry 54 (3), 807-819 (2015)
   PUBMED   25521717
  REMARK    GeneRIF: The persistence of a latent hexamer-building interface in
            the human enzyme suggests that the ancestral UXS may have been a
            hexamer.
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Polizzi,S.J., Walsh,R.M. Jr., Le Magueres,P., Criswell,A.R. and
            Wood,Z.A.
  TITLE     Human UDP-alpha-d-xylose synthase forms a catalytically important
            tetramer that has not been observed in crystal structures
  JOURNAL   Biochemistry 52 (22), 3888-3898 (2013)
   PUBMED   23656592
  REMARK    GeneRIF: hUXS forms a tetramer in solution that is important for
            activity. The higher activity of the tetramer coupled with the
            relative instability of the dimeric complex suggests that an
            association-dissociation mechanism may regulate hUXS activity.
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Polizzi,S.J., Walsh,R.M. Jr., Peeples,W.B., Lim,J.M., Wells,L. and
            Wood,Z.A.
  TITLE     Human UDP-alpha-D-xylose synthase and Escherichia coli ArnA
            conserve a conformational shunt that controls whether xylose or
            4-keto-xylose is produced
  JOURNAL   Biochemistry 51 (44), 8844-8855 (2012)
   PUBMED   23072385
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Gonzalez-Begne,M., Lu,B., Han,X., Hagen,F.K., Hand,A.R.,
            Melvin,J.E. and Yates,J.R.
  TITLE     Proteomic analysis of human parotid gland exosomes by
            multidimensional protein identification technology (MudPIT)
  JOURNAL   J Proteome Res 8 (3), 1304-1314 (2009)
   PUBMED   19199708
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Bakker,H., Oka,T., Ashikov,A., Yadav,A., Berger,M., Rana,N.A.,
            Bai,X., Jigami,Y., Haltiwanger,R.S., Esko,J.D. and
            Gerardy-Schahn,R.
  TITLE     Functional UDP-xylose transport across the endoplasmic
            reticulum/Golgi membrane in a Chinese hamster ovary cell mutant
            defective in UDP-xylose Synthase
  JOURNAL   J Biol Chem 284 (4), 2576-2583 (2009)
   PUBMED   19028698
  REMARK    GeneRIF: Complementation was achieved by expression of a
            cytoplasmic variant of UDP-xylose Synthase, which proves the
            existence of a functional Golgi UDP-xylose transporter[UDP-xylose
            Synthase]
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Hwang,H.Y. and Horvitz,H.R.
  TITLE     The SQV-1 UDP-glucuronic acid decarboxylase and the SQV-7
            nucleotide-sugar transporter may act in the Golgi apparatus to
            affect Caenorhabditis elegans vulval morphogenesis and embryonic
            development
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14218-14223 (2002)
   PUBMED   12391314
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Moriarity,J.L., Hurt,K.J., Resnick,A.C., Storm,P.B., Laroy,W.,
            Schnaar,R.L. and Snyder,S.H.
  TITLE     UDP-glucuronate decarboxylase, a key enzyme in proteoglycan
            synthesis: cloning, characterization, and localization
  JOURNAL   J Biol Chem 277 (19), 16968-16975 (2002)
   PUBMED   11877387
  REMARK    GeneRIF: UDP-glucuronate decarboxylase, a key enzyme in
            proteoglycan synthesis: cloning, characterization, and
            localization.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC018878.8.
            
            On Jan 16, 2020 this sequence version replaced XP_016860502.1.
            
            Summary: This gene encodes an enzyme found in the perinuclear Golgi
            which catalyzes the synthesis of UDP-xylose used in
            glycosaminoglycan (GAG) synthesis on proteoglycans. The GAG chains
            are covalently attached to proteoglycans which participate in
            signaling pathways during development. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Dec 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.99528.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q12.2"
     Protein         1..312
                     /product="UDP-glucuronic acid decarboxylase 1 isoform 9"
                     /EC_number="4.1.1.35"
                     /note="short chain dehydrogenase/reductase family 6E,
                     member 12; UDP-glucuronic acid decarboxylase 1; UXS-1"
                     /calculated_mol_wt=35148
     Region          1..284
                     /region_name="UGD_SDR_e"
                     /note="UDP-glucuronate decarboxylase (UGD) and related
                     proteins, extended (e) SDRs; cd05230"
                     /db_xref="CDD:187541"
     Site            order(11..16,35..37,51..55,70,92..94,123,127,150..153,164)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:187541"
     Site            order(40..41,76..77,80..81,83..84,137)
                     /site_type="other"
                     /note="putative substrate binding site 2 [chemical
                     binding]"
                     /db_xref="CDD:187541"
     Site            order(57,120,152,163..165,168..169,180..182,187,189,223,
                     249,253)
                     /site_type="other"
                     /note="putative substrate binding site 1 [chemical
                     binding]"
                     /db_xref="CDD:187541"
     Site            order(71,94,123,127)
                     /site_type="active"
                     /db_xref="CDD:187541"
     CDS             1..312
                     /gene="UXS1"
                     /gene_synonym="hUXS; hUXS1; SDR6E1; UGD"
                     /coded_by="NM_001377509.1:983..1921"
                     /note="isoform 9 is encoded by transcript variant 10"
                     /db_xref="GeneID:80146"
                     /db_xref="HGNC:HGNC:17729"
                     /db_xref="MIM:609749"
ORIGIN      
        1 mmdghevtvv dnfftgrkrn vehwighenf elinhdvvep lyievdqiyh laspasppny
       61 mynpiktlkt ntigtlnmlg lakrvgarll lastsevygd pevhpqsedy wghvnpigpr
      121 acydegkrva etmcyaymkq egvevrvari fntfgprmhm ndgrvvsnfi lqalqgeplt
      181 vygsgsqtra fqyvsdlvng lvalmnsnvs spvnlgnpee htilefaqli knlvgsgsei
      241 qflseaqddp qkrkpdikka klmlgwepvv pleeglnkai hyfrkeleyq annqyipkpk
      301 parikkgrtr hs
//
LOCUS       NP_001340060             347 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-B-cell leukemia transcription factor 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001340060 XP_016856885
VERSION     NP_001340060.1
DBSOURCE    REFSEQ: accession NM_001353131.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Huang,N., Zhang,H., Huang,Z., Wu,X., Zhang,N., Jiang,Y., Chen,C.
            and Zhuang,J.
  TITLE     Whole Exome Sequencing Revealing a Novel PBX1 Gene Variant in a
            Chinese Family Causing Recurrent Neonatal Death
  JOURNAL   Birth Defects Res 116 (8), e2396 (2024)
   PUBMED   39189629
  REMARK    GeneRIF: Whole Exome Sequencing Revealing a Novel PBX1 Gene Variant
            in a Chinese Family Causing Recurrent Neonatal Death.
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Choi,S.C., Park,Y.P., Roach,T., Jimenez,D., Fisher,A., Zadeh,M.,
            Ma,L., Sobel,E.S., Ge,Y., Mohamadzadeh,M. and Morel,L.
  TITLE     Lupus susceptibility gene Pbx1 controls the development, stability,
            and function of regulatory T cells via Rtkn2 expression
  JOURNAL   Sci Adv 10 (13), eadi4310 (2024)
   PUBMED   38536923
  REMARK    GeneRIF: Lupus susceptibility gene Pbx1 controls the development,
            stability, and function of regulatory T cells via Rtkn2 expression.
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Kao,T.W., Chen,H.H., Lin,J., Wang,T.L. and Shen,Y.A.
  TITLE     PBX1 as a novel master regulator in cancer: Its regulation,
            molecular biology, and therapeutic applications
  JOURNAL   Biochim Biophys Acta Rev Cancer 1879 (2), 189085 (2024)
   PUBMED   38341110
  REMARK    GeneRIF: PBX1 as a novel master regulator in cancer: Its
            regulation, molecular biology, and therapeutic applications.
            Review article
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Zhang,L., Guo,H., Zhang,X., Wang,L., Wei,F., Zhao,Y., Wang,B.,
            Meng,Y. and Li,Y.
  TITLE     Small nucleolar RNA Snora73 promotes psoriasis progression by
            sponging miR-3074-5p and regulating PBX1 expression
  JOURNAL   Funct Integr Genomics 24 (1), 15 (2024)
   PUBMED   38240925
  REMARK    GeneRIF: Small nucleolar RNA Snora73 promotes psoriasis progression
            by sponging miR-3074-5p and regulating PBX1 expression.
            Erratum:[Funct Integr Genomics. 2024 Jan 30;24(1):21. doi:
            10.1007/s10142-024-01306-1. PMID: 38286903]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Lu,Q., Knoepfler,P.S., Scheele,J., Wright,D.D. and Kamps,M.P.
  TITLE     Both Pbx1 and E2A-Pbx1 bind the DNA motif ATCAATCAA cooperatively
            with the products of multiple murine Hox genes, some of which are
            themselves oncogenes
  JOURNAL   Mol Cell Biol 15 (7), 3786-3795 (1995)
   PUBMED   7791786
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Monica,K., Galili,N., Nourse,J., Saltman,D. and Cleary,M.L.
  TITLE     PBX2 and PBX3, new homeobox genes with extensive homology to the
            human proto-oncogene PBX1
  JOURNAL   Mol Cell Biol 11 (12), 6149-6157 (1991)
   PUBMED   1682799
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Hunger,S.P., Galili,N., Carroll,A.J., Crist,W.M., Link,M.P. and
            Cleary,M.L.
  TITLE     The t(1;19)(q23;p13) results in consistent fusion of E2A and PBX1
            coding sequences in acute lymphoblastic leukemias
  JOURNAL   Blood 77 (4), 687-693 (1991)
   PUBMED   1671560
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Kamps,M.P., Murre,C., Sun,X.H. and Baltimore,D.
  TITLE     A new homeobox gene contributes the DNA binding domain of the
            t(1;19) translocation protein in pre-B ALL
  JOURNAL   Cell 60 (4), 547-555 (1990)
   PUBMED   1967983
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Nourse,J., Mellentin,J.D., Galili,N., Wilkinson,J., Stanbridge,E.,
            Smith,S.D. and Cleary,M.L.
  TITLE     Chromosomal translocation t(1;19) results in synthesis of a
            homeobox fusion mRNA that codes for a potential chimeric
            transcription factor
  JOURNAL   Cell 60 (4), 535-545 (1990)
   PUBMED   1967982
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359255.12, AL357568.14 and
            AL390119.25.
            
            On Jun 28, 2017 this sequence version replaced XP_016856885.1.
            
            Summary: This gene encodes a nuclear protein that belongs to the
            PBX homeobox family of transcriptional factors. Studies in mice
            suggest that this gene may be involved in the regulation of
            osteogenesis and required for skeletal patterning and programming.
            A chromosomal translocation, t(1;19) involving this gene and
            TCF3/E2A gene, is associated with pre-B-cell acute lymphoblastic
            leukemia. The resulting fusion protein, in which the DNA binding
            domain of E2A is replaced by the DNA binding domain of this
            protein, transforms cells by constitutively activating
            transcription of genes regulated by the PBX protein family.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jun
            2017].
            
            Transcript Variant: This variant (5) uses an alternate 3' terminal
            exon and lacks an exon in the 3' coding region, compared to variant
            1. This results in a frame-shift and a shorter isoform (2, also
            known as isoform PBX1b) with a distinct C-terminus compared to
            isoform 1. Variants 2 and 5 encode the same isoform.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BT006705.1 [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..347
                     /product="pre-B-cell leukemia transcription factor 1
                     isoform 2"
                     /note="pre-B-cell leukemia transcription factor 1;
                     homeobox protein PRL; homeobox protein PBX1; pre-B-cell
                     leukemia homeobox 1"
                     /calculated_mol_wt=38296
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P40424.1)"
     Region          42..232
                     /region_name="PBC"
                     /note="PBC domain; pfam03792"
                     /db_xref="CDD:461052"
     Region          45..124
                     /region_name="PBC-A.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01322"
                     /note="propagated from UniProtKB/Swiss-Prot (P40424.1)"
     Site            88..89
                     /site_type="other"
                     /note="Breakpoint for translocation to form TCF3-PBX1
                     oncogene; propagated from UniProtKB/Swiss-Prot (P40424.1)"
     Region          127..232
                     /region_name="PBC-B.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01322"
                     /note="propagated from UniProtKB/Swiss-Prot (P40424.1)"
     Region          234..294
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(234..238,240,260,266,279,281..282,285..286,288..290,
                     292..293)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(236,239,282,285..286,289)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            286
                     /site_type="other"
                     /note="Required for binding to the NFIL3 promoter.
                     /evidence=ECO:0000250|UniProtKB:P41778; propagated from
                     UniProtKB/Swiss-Prot (P40424.1)"
     CDS             1..347
                     /gene="PBX1"
                     /gene_synonym="CAKUHED"
                     /coded_by="NM_001353131.2:640..1683"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS55654.1"
                     /db_xref="GeneID:5087"
                     /db_xref="HGNC:HGNC:8632"
                     /db_xref="MIM:176310"
ORIGIN      
        1 mdeqprlmhs hagvgmaghp glsqhlqdga ggtegeggrk qdigdilqqi mtitdqslde
       61 aqarkhalnc hrmkpalfnv lceikektvl sirgaqeeep tdpqlmrldn mllaegvagp
      121 ekgggsaaaa aaaaasggag sdnsvehsdy raklsqirqi yhtelekyeq acneftthvm
      181 nllreqsrtr pispkeierm vsiihrkfss iqmqlkqstc eavmilrsrf ldarrkrrnf
      241 nkqateilne yfyshlsnpy pseeakeela kkcgitvsqv snwfgnkrir ykknigkfqe
      301 eaniyaakta vtatnvsahg sqanspstpn saggypspcy qpdrriq
//
LOCUS       NP_001382177             242 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb group RING finger protein 3 isoform a [Homo sapiens].
ACCESSION   NP_001382177
VERSION     NP_001382177.1
DBSOURCE    REFSEQ: accession NM_001395248.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Hu,Y., Cheng,Y., Jiang,X., Zhang,Y., Wang,H., Ren,H., Xu,Y.,
            Jiang,J., Wang,Q., Su,H., Zhang,B. and Qiu,X.
  TITLE     PCGF3 promotes the proliferation and migration of non-small cell
            lung cancer cells via the PI3K/AKT signaling pathway
  JOURNAL   Exp Cell Res 400 (2), 112496 (2021)
   PUBMED   33485844
  REMARK    GeneRIF: PCGF3 promotes the proliferation and migration of
            non-small cell lung cancer cells via the PI3K/AKT signaling
            pathway.
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Mu,G., Xiang,Q., Zhang,Z., Liu,C., Zhang,H., Liu,Z., Pang,X.,
            Jiang,J., Xie,Q., Zhou,S., Wang,Z., Hu,K., Wang,Z., Jiang,S.,
            Qin,X. and Cui,Y.
  TITLE     PNPT1 and PCGF3 variants associated with angiotensin-converting
            enzyme inhibitor-induced cough: a nested case-control genome-wide
            study
  JOURNAL   Pharmacogenomics 21 (9), 601-614 (2020)
   PUBMED   32397904
  REMARK    GeneRIF: PNPT1 and PCGF3 variants associated with
            angiotensin-converting enzyme inhibitor-induced cough: a nested
            case-control genome-wide study.
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Purohit,G., Mukherjee,A.K., Sharma,S. and Chowdhury,S.
  TITLE     Extratelomeric Binding of the Telomere Binding Protein TRF2 at the
            PCGF3 Promoter Is G-Quadruplex Motif-Dependent
  JOURNAL   Biochemistry 57 (16), 2317-2324 (2018)
   PUBMED   29589913
  REMARK    GeneRIF: We demonstrate that promoter binding by TRF2 mediates
            PCGF3 promoter activity, and both the N-terminal and C-terminal
            domains of TRF2 are necessary for promoter activity.
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Marcon,E., Ni,Z., Pu,S., Turinsky,A.L., Trimble,S.S., Olsen,J.B.,
            Silverman-Gavrila,R., Silverman-Gavrila,L., Phanse,S., Guo,H.,
            Zhong,G., Guo,X., Young,P., Bailey,S., Roudeva,D., Zhao,D.,
            Hewel,J., Li,J., Graslund,S., Paduch,M., Kossiakoff,A.A.,
            Lupien,M., Emili,A., Wodak,S.J. and Greenblatt,J.
  TITLE     Human-chromatin-related protein interactions identify a demethylase
            complex required for chromosome segregation
  JOURNAL   Cell Rep 8 (1), 297-310 (2014)
   PUBMED   24981860
REFERENCE   7  (residues 1 to 242)
  AUTHORS   Woodsmith,J., Jenn,R.C. and Sanderson,C.M.
  TITLE     Systematic analysis of dimeric E3-RING interactions reveals
            increased combinatorial complexity in human ubiquitination networks
  JOURNAL   Mol Cell Proteomics 11 (7), M111.016162 (2012)
   PUBMED   22493164
REFERENCE   8  (residues 1 to 242)
  AUTHORS   Oudot-Mellakh,T., Cohen,W., Germain,M., Saut,N., Kallel,C.,
            Zelenika,D., Lathrop,M., Tregouet,D.A. and Morange,P.E.
  TITLE     Genome wide association study for plasma levels of natural
            anticoagulant inhibitors and protein C anticoagulant pathway: the
            MARTHA project
  JOURNAL   Br J Haematol 157 (2), 230-239 (2012)
   PUBMED   22443383
REFERENCE   9  (residues 1 to 242)
  AUTHORS   Gao,Z., Zhang,J., Bonasio,R., Strino,F., Sawai,A., Parisi,F.,
            Kluger,Y. and Reinberg,D.
  TITLE     PCGF homologs, CBX proteins, and RYBP define functionally distinct
            PRC1 family complexes
  JOURNAL   Mol Cell 45 (3), 344-356 (2012)
   PUBMED   22325352
REFERENCE   10 (residues 1 to 242)
  AUTHORS   Vandamme,J., Volkel,P., Rosnoblet,C., Le Faou,P. and Angrand,P.O.
  TITLE     Interaction proteomics analysis of polycomb proteins defines
            distinct PRC1 complexes in mammalian cells
  JOURNAL   Mol Cell Proteomics 10 (4), M110.002642 (2011)
   PUBMED   21282530
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107464.5 and AC139887.3.
            
            Summary: The protein encoded by this gene contains a C3HC4 type
            RING finger, which is a motif known to be involved in
            protein-protein interactions. The specific function of this protein
            has not yet been determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.352.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..242
                     /product="polycomb group RING finger protein 3 isoform a"
                     /note="ring finger protein 3; polycomb group RING finger
                     protein 3; RING finger protein 3A"
                     /calculated_mol_wt=27984
     Region          4..69
                     /region_name="RING-HC_PCGF3"
                     /note="RING finger found in polycomb group RING finger
                     protein 3 (PCGF3) and similar proteins; cd16735"
                     /db_xref="CDD:438393"
     Site            order(16,20,22..23,26,28..29,31..35,38..41,43..44)
                     /site_type="other"
                     /note="putative heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:438393"
     Region          115..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KNV8.1)"
     Region          132..242
                     /region_name="Interaction with BCORL1.
                     /evidence=ECO:0000269|PubMed:27568929"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KNV8.1)"
     Region          154..236
                     /region_name="RAWUL_PCGF3"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in polycomb group RING finger protein
                     3 (PCGF3) and similar proteins; cd17083"
                     /db_xref="CDD:340603"
     CDS             1..242
                     /gene="PCGF3"
                     /gene_synonym="DONG1; RNF3; RNF3A"
                     /coded_by="NM_001395248.1:319..1047"
                     /note="isoform a is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS3339.2"
                     /db_xref="GeneID:10336"
                     /db_xref="HGNC:HGNC:10066"
                     /db_xref="MIM:617543"
ORIGIN      
        1 mltrkiklwd inahitcrlc sgylidattv teclhtfcrs clvkyleenn tcptcrivih
       61 qshplqyigh drtmqdivyk lvpglqeaem rkqrefyhkl gmevpgdikg etcsakqhld
      121 shrngetkad dssnkeaaee kpeedndyhr sdeqvsicle cnssklrglk rkwircsaqa
      181 tvlhlkkfia kklnlssfne ldilcneeil gkdhtlkfvv vtrwrfkkap lllhyrpkmd
      241 ll
//
LOCUS       NP_001363788             371 aa            linear   PRI 21-NOV-2025
DEFINITION  alpha-taxilin isoform 2 [Homo sapiens].
ACCESSION   NP_001363788 XP_016856053
VERSION     NP_001363788.1
DBSOURCE    REFSEQ: accession NM_001376859.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Ma,D., Wang,F., Wang,R., Hu,Y., Chen,Z., Huang,N., Tian,Y., Xia,Y.,
            Teng,J. and Chen,J.
  TITLE     alpha-/gamma-Taxilin are required for centriolar subdistal
            appendage assembly and microtubule organization
  JOURNAL   Elife 11, e73252 (2022)
   PUBMED   35119360
  REMARK    GeneRIF: alpha-/gamma-Taxilin are required for centriolar subdistal
            appendage assembly and microtubule organization.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Nogami,S., Satoh,S., Nakano,M., Terano,A. and Shirataki,H.
  TITLE     Interaction of taxilin with syntaxin which does not form the SNARE
            complex
  JOURNAL   Biochem Biophys Res Commun 311 (4), 797-802 (2003)
   PUBMED   14623251
REFERENCE   7  (residues 1 to 371)
  AUTHORS   Nogami,S., Satoh,S., Nakano,M., Shimizu,H., Fukushima,H.,
            Maruyama,A., Terano,A. and Shirataki,H.
  TITLE     Taxilin; a novel syntaxin-binding protein that is involved in
            Ca2+-dependent exocytosis in neuroendocrine cells
  JOURNAL   Genes Cells 8 (1), 17-28 (2003)
   PUBMED   12558796
REFERENCE   8  (residues 1 to 371)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 371)
  AUTHORS   Ambrus,J.L. Jr., Pippin,J., Joseph,A., Xu,C., Blumenthal,D.,
            Tamayo,A., Claypool,K., McCourt,D., Srikiatchatochorn,A. and
            Ford,R.
  TITLE     Identification of a cDNA for a human high molecular-weight B-cell
            growth factor
  JOURNAL   Proc Natl Acad Sci U S A 93 (15), 8154 (1996)
   PUBMED   8755619
  REMARK    Correction to:[Proc Natl Acad Sci U S A. 1993 Jul 1;90(13):6330-4.
            doi: 10.1073/pnas.90.13.6330. PMID: 8327514]
REFERENCE   10 (residues 1 to 371)
  AUTHORS   Ambrus,J.L. Jr., Pippin,J., Joseph,A., Xu,C., Blumenthal,D.,
            Tamayo,A., Claypool,K., McCourt,D., Srikiatchatochorn,A. and
            Ford,R.J.
  TITLE     Identification of a cDNA for a human high-molecular-weight B-cell
            growth factor
  JOURNAL   Proc Natl Acad Sci U S A 90 (13), 6330-6334 (1993)
   PUBMED   8327514
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1996 Jul 23;93(15):8154. doi:
            10.1073/pnas.93.15.8154-b. PMID: 8755619]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL049795.21.
            
            On Nov 20, 2019 this sequence version replaced XP_016856053.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1971797.1,
                                           SRR18074969.511928.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.2"
     Protein         1..371
                     /product="alpha-taxilin isoform 2"
                     /note="alpha-taxilin; interleukin 14"
                     /calculated_mol_wt=43175
     Region          1..302
                     /region_name="Taxilin"
                     /note="Myosin-like coiled-coil protein; pfam09728"
                     /db_xref="CDD:462861"
     CDS             1..371
                     /gene="TXLNA"
                     /gene_synonym="IL-14; IL14; TXLN"
                     /coded_by="NM_001376859.1:459..1574"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:200081"
                     /db_xref="HGNC:HGNC:30685"
                     /db_xref="MIM:608676"
ORIGIN      
        1 mqtlntlstp eeklaalckk yaelleehrn sqkqmkllqk kqsqlvqekd hlrgehskav
       61 larskleslc relqrhnrsl keegvqrare eeekrkevts hfqvtlndiq lqmeqhnern
      121 sklrqenmel aerlkklieq yelreehidk vfkhkdlqqq lvdaklqqaq emlkeaeerh
      181 qrekdfllke avesqrmcel mkqqethlkq qlalytekfe efqntlskss evfttfkqem
      241 ekmtkkikkl ekettmyrsr wessnkalle maeektvrdk eleglqvkiq rleklcralq
      301 terndlnkrv qdlsaggqgs ltdsgperrp egpgaqapss prvteapcyp gapsteasgq
      361 tgpqeptsar a
//
LOCUS       NP_001374925            1162 aa            linear   PRI 21-NOV-2025
DEFINITION  large proline-rich protein BAG6 isoform 5 [Homo sapiens].
ACCESSION   NP_001374925
VERSION     NP_001374925.1
DBSOURCE    REFSEQ: accession NM_001387996.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1162)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 1162)
  AUTHORS   Alashkar Alhamwe,B., Ponath,V., Alhamdan,F., Dorsam,B.,
            Landwehr,C., Linder,M., Pauck,K., Miethe,S., Garn,H.,
            Finkernagel,F., Brichkina,A., Lauth,M., Tiwari,D.K., Buchholz,M.,
            Bachurski,D., Elmshauser,S., Nist,A., Stiewe,T., Pogge von
            Strandmann,L., Szymanski,W., Beutgen,V., Graumann,J.,
            Teply-Szymanski,J., Keber,C., Denkert,C., Jacob,R., Preusser,C. and
            Pogge von Strandmann,E.
  TITLE     BAG6 restricts pancreatic cancer progression by suppressing the
            release of IL33-presenting extracellular vesicles and the
            activation of mast cells
  JOURNAL   Cell Mol Immunol 21 (8), 918-931 (2024)
   PUBMED   38942797
  REMARK    GeneRIF: BAG6 restricts pancreatic cancer progression by
            suppressing the release of IL33-presenting extracellular vesicles
            and the activation of mast cells.
REFERENCE   3  (residues 1 to 1162)
  AUTHORS   Liu,L., Wu,J., Yan,Y., Cheng,S., Yu,S. and Wang,Y.
  TITLE     DERL2 (derlin 2) stabilizes BAG6 (BAG cochaperone 6) in
            chemotherapy resistance of cholangiocarcinoma
  JOURNAL   J Physiol Biochem 80 (1), 81-97 (2024)
   PUBMED   37815698
  REMARK    GeneRIF: DERL2 (derlin 2) stabilizes BAG6 (BAG cochaperone 6) in
            chemotherapy resistance of cholangiocarcinoma.
REFERENCE   4  (residues 1 to 1162)
  AUTHORS   Roboti,P., Lawless,C. and High,S.
  TITLE     Mitochondrial antiviral-signalling protein is a client of the BAG6
            protein quality control complex
  JOURNAL   J Cell Sci 135 (9) (2022)
   PUBMED   35543156
  REMARK    GeneRIF: Mitochondrial antiviral-signalling protein is a client of
            the BAG6 protein quality control complex.
REFERENCE   5  (residues 1 to 1162)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1162)
  AUTHORS   Ozaki,T., Hanaoka,E., Naka,M., Nakagawara,A. and Sakiyama,S.
  TITLE     Cloning and characterization of rat BAT3 cDNA
  JOURNAL   DNA Cell Biol 18 (6), 503-512 (1999)
   PUBMED   10390159
REFERENCE   7  (residues 1 to 1162)
  AUTHORS   Cross,S.J., Tonks,S., Trowsdale,J. and Campbell,R.D.
  TITLE     Novel detection of restriction fragment length polymorphisms in the
            human major histocompatibility complex
  JOURNAL   Immunogenetics 34 (6), 376-384 (1991)
   PUBMED   1684176
REFERENCE   8  (residues 1 to 1162)
  AUTHORS   Banerji,J., Sands,J., Strominger,J.L. and Spies,T.
  TITLE     A gene pair from the human major histocompatibility complex encodes
            large proline-rich proteins with multiple repeated motifs and a
            single ubiquitin-like domain
  JOURNAL   Proc Natl Acad Sci U S A 87 (6), 2374-2378 (1990)
   PUBMED   2156268
REFERENCE   9  (residues 1 to 1162)
  AUTHORS   Spies,T., Bresnahan,M. and Strominger,J.L.
  TITLE     Human major histocompatibility complex contains a minimum of 19
            genes between the complement cluster and HLA-B
  JOURNAL   Proc Natl Acad Sci U S A 86 (22), 8955-8958 (1989)
   PUBMED   2813433
REFERENCE   10 (residues 1 to 1162)
  AUTHORS   Spies,T., Blanck,G., Bresnahan,M., Sands,J. and Strominger,J.L.
  TITLE     A new cluster of genes within the human major histocompatibility
            complex
  JOURNAL   Science 243 (4888), 214-217 (1989)
   PUBMED   2911734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL662801.7.
            
            Summary: This gene was first characterized as part of a cluster of
            genes located within the human major histocompatibility complex
            class III region. This gene encodes a nuclear protein that is
            cleaved by caspase 3 and is implicated in the control of apoptosis.
            In addition, the protein forms a complex with E1A binding protein
            p300 and is required for the acetylation of p53 in response to DNA
            damage. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853565.24587.1,
                                           SRR14038197.1018946.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1162
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..1162
                     /product="large proline-rich protein BAG6 isoform 5"
                     /note="scythe; large proline-rich protein BAT3; large
                     proline-rich protein BAG6; protein G3; HLA-B-associated
                     transcript 3; protein Scythe; BAG family molecular
                     chaperone regulator 6; BCL2 associated athanogene 6"
                     /calculated_mol_wt=122212
     Region          17..87
                     /region_name="Ubl_BAG6"
                     /note="ubiquitin-like (Ubl) domain found in
                     BCL2-associated athanogene 6 (BAG6) and similar proteins;
                     cd01809"
                     /db_xref="CDD:340507"
     Site            order(22..25,58,60,62..65,83..87)
                     /site_type="other"
                     /note="ZF interaction site [polypeptide binding]"
                     /db_xref="CDD:340507"
     Region          270..386
                     /region_name="BAG6"
                     /note="BCL2-associated athanogene 6; pfam12057"
                     /db_xref="CDD:463449"
     Region          <935..1126
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     CDS             1..1162
                     /gene="BAG6"
                     /gene_synonym="BAG-6; BAT3; D6S52E; G3"
                     /coded_by="NM_001387996.1:276..3764"
                     /note="isoform 5 is encoded by transcript variant 36"
                     /db_xref="CCDS:CCDS93882.1"
                     /db_xref="GeneID:7917"
                     /db_xref="HGNC:HGNC:13919"
                     /db_xref="MIM:142590"
ORIGIN      
        1 mepndststa veepdslevl vktldsqtrt fivgaqmnvk efkehiaasv sipsekqrli
       61 yqgrvlqddk klqeynvggk vihlverapp qthlpsgass gtgsasathg ggsppgtrgp
      121 gasvhdrnan syvmvgtfnl psdgsavdvh inmeqapiqs eprvrlvmaq hmirdiqtll
      181 srmecrggpq pqhsqpppqp pavtpepval ssqtsepves eapprepmea eeveerapaq
      241 npeltpgpap agptpapetn apnhpspaey vevlqelqrl esrlqpflqr yyevlgaaat
      301 tdynnnhegr eedqrlinlv geslrllgnt fvalsdlrcn lactpprhlh vvrpmshytt
      361 pmvlqqaaip iqinvgttvt mtgngtrppp tpnaeapppg pgqassvaps stnvessaeg
      421 apppgpappp atshprviri shqsvepvvm mhmniqdsgt qpggvpsapt gplgppghgq
      481 tlgstliqlp slppefmhav ahqithqamv aavasaaagq qvpgfptapt rvviarptpp
      541 qarpshpggp pvsgtlqgag lgtnaslaqm vsglvgqllm qpvlvaqgtp gmapppapat
      601 asasagttnt attagpapgg paqppptpqp smadlqfsql lgnllgpagp gaggsgvasp
      661 titvampgvp aflqgmtdfl qatqtapppp ppppppppap eqqtmpppgs psggagspgg
      721 lgleslspef ftsvvqgvls sllgslgara gssesiaafi qrlsgssnif epgadgalgf
      781 fgallsllcq nfsmvdvvml lhghfqplqr lqpqlrsffh qhylggqept psnirmatht
      841 litgleeyvr esfslvqvqp gvdiirtnle flqeqfnsia ahvlhctdsg fgarllelcn
      901 qglfeclaln lhclggqqme laavingrir rmsrgvnpsl vswlttmmgl rlqvvlehmp
      961 vgpdailryv rrvgdppqpl peepmevqga eraspepqre naspapgtta eeamsrgppp
     1021 apeggsrdeq dgasaetepw aaavppewvp iiqqdiqsqr kvkpqpplsd aylsgmpakr
     1081 rktmqgegpq lllseavsra akaagarplt speslsrdle apevqesyrq qlrsdiqkrl
     1141 qedpnyspqr fpnaqrafad dp
//
LOCUS       NP_001676                108 aa            linear   PRI 21-NOV-2025
DEFINITION  ATP synthase peripheral stalk subunit F6, mitochondrial isoform a
            precursor [Homo sapiens].
ACCESSION   NP_001676
VERSION     NP_001676.2
DBSOURCE    REFSEQ: accession NM_001685.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Hochstrasser,D.F., Frutiger,S., Paquet,N., Bairoch,A., Ravier,F.,
            Pasquali,C., Sanchez,J.C., Tissot,J.D., Bjellqvist,B., Vargas,R. et
            al.
  TITLE     Human liver protein map: a reference database established by
            microsequencing and gel comparison
  JOURNAL   Electrophoresis 13 (12), 992-1001 (1992)
   PUBMED   1286669
REFERENCE   8  (residues 1 to 108)
  AUTHORS   Higuti,T., Tsurumi,C., Kawamura,Y., Tsujita,H., Osaka,F.,
            Yoshihara,Y., Tani,I., Tanaka,K. and Ichihara,A.
  TITLE     Molecular cloning of cDNA for the import precursor of human
            coupling factor 6 of H(+)-ATP synthase in mitochondria
  JOURNAL   Biochem Biophys Res Commun 178 (2), 793-799 (1991)
   PUBMED   1830479
REFERENCE   9  (residues 1 to 108)
  AUTHORS   Javed,A.A., Ogata,K. and Sanadi,D.R.
  TITLE     Human mitochondrial ATP synthase: cloning cDNA for the
            nuclear-encoded precursor of coupling factor 6
  JOURNAL   Gene 97 (2), 307-310 (1991)
   PUBMED   1825642
REFERENCE   10 (residues 1 to 108)
  AUTHORS   Boyer,P.D., Cross,R.L. and Momsen,W.
  TITLE     A new concept for energy coupling in oxidative phosphorylation
            based on a molecular explanation of the oxygen exchange reactions
  JOURNAL   Proc Natl Acad Sci U S A 70 (10), 2837-2839 (1973)
   PUBMED   4517936
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC001178.1, BC066310.1 and
            AI085837.1.
            
            On Feb 11, 2002 this sequence version replaced NP_001676.1.
            
            Summary: Mitochondrial ATP synthase catalyzes ATP synthesis,
            utilizing an electrochemical gradient of protons across the inner
            membrane during oxidative phosphorylation. It is composed of two
            linked multi-subunit complexes: the soluble catalytic core, F1, and
            the membrane-spanning component, Fo, which comprises the proton
            channel. The F1 complex consists of 5 different subunits (alpha,
            beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3
            beta, and a single representative of the other 3. The Fo complex
            has nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene
            encodes the F6 subunit of the Fo complex. The F6 subunit is
            required for F1 and Fo interactions. Alternatively spliced
            transcript variants encoding different isoforms have been
            identified for this gene. This gene has 1 or more pseudogenes.
            [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1, 2, 3, 4, 6 and 7 encode the same
            isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD370588.1, BM272692.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03568911, SAMN03568912
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..108
                     /product="ATP synthase peripheral stalk subunit F6,
                     mitochondrial isoform a precursor"
                     /EC_number="3.6.1.14"
                     /note="ATP synthase, H+ transporting, mitochondrial F0
                     complex, subunit F6; coupling factor 6; mitochondrial ATP
                     synthase, subunit F6; mitochondrial ATPase coupling factor
                     6; mitochondrial ATP synthase, coupling factor 6; ATP
                     synthase-coupling factor 6, mitochondrial;
                     proliferation-inducing protein 36; ATPase subunit F6; ATP
                     synthase, H+ transporting, mitochondrial Fo complex
                     subunit F6; ATP synthase subunit h; ATP synthase
                     peripheral stalk subunit F6, mitochondrial"
                     /calculated_mol_wt=8960
     Region          1..96
                     /region_name="ATP-synt_F6"
                     /note="Mitochondrial ATP synthase coupling factor 6;
                     pfam05511"
                     /db_xref="CDD:461669"
     transit_peptide 1..32
                     /calculated_mol_wt=3645
     mat_peptide     33..108
                     /product="ATP synthase peripheral stalk subunit F6,
                     mitochondrial isoform a"
                     /calculated_mol_wt=8960
     Site            41
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P18859.1)"
     Site            46
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P18859.1)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P18859.1)"
     Site            79
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P97450; propagated from
                     UniProtKB/Swiss-Prot (P18859.1)"
     Site            94
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P97450; propagated from
                     UniProtKB/Swiss-Prot (P18859.1)"
     Site            99
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P18859.1)"
     Site            105
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P18859.1)"
     CDS             1..108
                     /gene="ATP5PF"
                     /gene_synonym="ATP5; ATP5A; ATP5J; ATPM; CF6; F6"
                     /coded_by="NM_001685.5:74..400"
                     /note="isoform a precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS13574.1"
                     /db_xref="GeneID:522"
                     /db_xref="HGNC:HGNC:847"
                     /db_xref="MIM:603152"
ORIGIN      
        1 milqrlfrfs svirsavsvh lrrnigvtav afnkeldpiq klfvdkirey kskrqtsggp
       61 vdasseyqqe lerelfklkq mfgnadmntf ptfkfedpkf eviekpqa
//
LOCUS       NP_001333529             451 aa            linear   PRI 21-NOV-2025
DEFINITION  RAD50-interacting protein 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001333529 XP_016867986
VERSION     NP_001333529.1
DBSOURCE    REFSEQ: accession NM_001346600.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Arnold,F., Gout,J., Wiese,H., Weissinger,S.E., Roger,E.,
            Perkhofer,L., Walter,K., Scheible,J., Prelli Bozzo,C., Lechel,A.,
            Ettrich,T.J., Azoitei,N., Hao,L., Furstberger,A., Kaminska,E.K.,
            Sparrer,K.M.J., Rasche,V., Wiese,S., Kestler,H.A., Moller,P.,
            Seufferlein,T., Frappart,P.O. and Kleger,A.
  TITLE     RINT1 Regulates SUMOylation and the DNA Damage Response to Preserve
            Cellular Homeostasis in Pancreatic Cancer
  JOURNAL   Cancer Res 81 (7), 1758-1774 (2021)
   PUBMED   33531371
  REMARK    GeneRIF: RINT1 Regulates SUMOylation and the DNA Damage Response to
            Preserve Cellular Homeostasis in Pancreatic Cancer.
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Arasaki,K., Taniguchi,M., Tani,K. and Tagaya,M.
  TITLE     RINT-1 regulates the localization and entry of ZW10 to the syntaxin
            18 complex
  JOURNAL   Mol Biol Cell 17 (6), 2780-2788 (2006)
   PUBMED   16571679
  REMARK    GeneRIF: RINT-1 coordinates the localization and function of ZW10
            by serving as a link between ZW10 and the SNARE complex comprising
            syntaxin 18.
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Kops,G.J., Kim,Y., Weaver,B.A., Mao,Y., McLeod,I., Yates,J.R. 3rd,
            Tagaya,M. and Cleveland,D.W.
  TITLE     ZW10 links mitotic checkpoint signaling to the structural
            kinetochore
  JOURNAL   J Cell Biol 169 (1), 49-60 (2005)
   PUBMED   15824131
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Nakajima,K., Hirose,H., Taniguchi,M., Kurashina,H., Arasaki,K.,
            Nagahama,M., Tani,K., Yamamoto,A. and Tagaya,M.
  TITLE     Involvement of BNIP1 in apoptosis and endoplasmic reticulum
            membrane fusion
  JOURNAL   EMBO J 23 (16), 3216-3226 (2004)
   PUBMED   15272311
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Hirose,H., Arasaki,K., Dohmae,N., Takio,K., Hatsuzawa,K.,
            Nagahama,M., Tani,K., Yamamoto,A., Tohyama,M. and Tagaya,M.
  TITLE     Implication of ZW10 in membrane trafficking between the endoplasmic
            reticulum and Golgi
  JOURNAL   EMBO J 23 (6), 1267-1278 (2004)
   PUBMED   15029241
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Xiao,J., Liu,C.C., Chen,P.L. and Lee,W.H.
  TITLE     RINT-1, a novel Rad50-interacting protein, participates in
            radiation-induced G(2)/M checkpoint control
  JOURNAL   J Biol Chem 276 (9), 6105-6111 (2001)
   PUBMED   11096100
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073073.2 and AA281630.1.
            
            On Oct 21, 2016 this sequence version replaced XP_016867986.1.
            
            Summary: This gene encodes a protein first identified for its
            ability to interact with the RAD50 double strand break repair
            protein, with the resulting interaction implicated in the
            regulation of cell cycle progression and telomere length. The
            encoded protein may also play a role in trafficking of cellular
            cargo from the endosome to the trans-Golgi network. Mutations in
            this gene may be associated with breast cancer in human patients.
            [provided by RefSeq, Oct 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2505347.1,
                                           SRR14038192.788423.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.3"
     Protein         1..451
                     /product="RAD50-interacting protein 1 isoform 3"
                     /note="Rad50-interacting protein 1"
                     /calculated_mol_wt=51843
     Region          1..443
                     /region_name="RINT1_TIP1"
                     /note="RINT-1 / TIP-1 family; pfam04437"
                     /db_xref="CDD:461309"
     CDS             1..451
                     /gene="RINT1"
                     /gene_synonym="ILFS3; RINT-1"
                     /coded_by="NM_001346600.2:1135..2490"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:60561"
                     /db_xref="HGNC:HGNC:21876"
                     /db_xref="MIM:610089"
ORIGIN      
        1 mwignhtefl dekiqpildk vgslvnarle fsrglmmlvl eklatdipcl lyddnlfchl
       61 vdevllfere lhsvhgypgt fascmhilse etcfqrwltv erkfalqkmd smlsseaawv
      121 sqykditdvd emkvpdcaet fmtlllvitd ryknlptasr klqflelqkd lvddfrirlt
      181 qvmkeetras lgfrycailn avnyistvla dwadnvfflq lqqaalevfa enntlsklql
      241 gqlasmessv fddminller lkhdmltrqv dhvfrevkda aklykkerwl slpsqseqav
      301 mslsssacpl lltlrdhllq leqqlcfslf kifwqmlvek ldvyiyqeii lanhfnegga
      361 aqlqfdmtrn lfplfshyck rpenyfkhik eacivlnlnv gsalllkdvl qsasgqlpat
      421 aalnevgiyk laqqdveill nlrtnwpntg k
//
LOCUS       NP_001372232             813 aa            linear   PRI 21-NOV-2025
DEFINITION  receptor-type tyrosine-protein phosphatase alpha isoform 3
            precursor [Homo sapiens].
ACCESSION   NP_001372232
VERSION     NP_001372232.1
DBSOURCE    REFSEQ: accession NM_001385303.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Fang,J., Zhang,Y., Huang,C., Lu,R., Yu,J., Chen,R., Wang,Y.,
            Zhao,X., Yu,J. and Huang,J.
  TITLE     Glucose-mediated N-glycosylation of RPTPalpha affects its
            subcellular localization and Src activation
  JOURNAL   Oncogene 42 (14), 1058-1071 (2023)
   PUBMED   36765146
  REMARK    GeneRIF: Glucose-mediated N-glycosylation of RPTPalpha affects its
            subcellular localization and Src activation.
REFERENCE   3  (residues 1 to 813)
  AUTHORS   Hill,M.A., Bentley,S.R., Walker,T.L., Mellick,G.D., Wood,S.A. and
            Sykes,A.M.
  TITLE     Does a rare mutation in PTPRA contribute to the development of
            Parkinson's disease in an Australian multi-incident family?
  JOURNAL   PLoS One 17 (7), e0271499 (2022)
   PUBMED   35900966
  REMARK    GeneRIF: Does a rare mutation in PTPRA contribute to the
            development of Parkinson's disease in an Australian multi-incident
            family?
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 813)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 813)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 813)
  AUTHORS   Zheng,X.M., Wang,Y. and Pallen,C.J.
  TITLE     Cell transformation and activation of pp60c-src by overexpression
            of a protein tyrosine phosphatase
  JOURNAL   Nature 359 (6393), 336-339 (1992)
   PUBMED   1383828
REFERENCE   7  (residues 1 to 813)
  AUTHORS   Rao,V.V., Loffler,C., Sap,J., Schlessinger,J. and Hansmann,I.
  TITLE     The gene for receptor-linked protein-tyrosine-phosphatase (PTPA) is
            assigned to human chromosome 20p12-pter by in situ hybridization
            (ISH and FISH)
  JOURNAL   Genomics 13 (3), 906-907 (1992)
   PUBMED   1639427
REFERENCE   8  (residues 1 to 813)
  AUTHORS   Jirik,F.R., Anderson,L.L. and Duncan,A.M.
  TITLE     The human protein-tyrosine phosphatase PTP alpha/LRP gene (PTPA) is
            assigned to chromosome 20p13
  JOURNAL   Cytogenet Cell Genet 60 (2), 117-118 (1992)
   PUBMED   1611910
REFERENCE   9  (residues 1 to 813)
  AUTHORS   Kaplan,R., Morse,B., Huebner,K., Croce,C., Howk,R., Ravera,M.,
            Ricca,G., Jaye,M. and Schlessinger,J.
  TITLE     Cloning of three human tyrosine phosphatases reveals a multigene
            family of receptor-linked protein-tyrosine-phosphatases expressed
            in brain
  JOURNAL   Proc Natl Acad Sci U S A 87 (18), 7000-7004 (1990)
   PUBMED   2169617
REFERENCE   10 (residues 1 to 813)
  AUTHORS   Sap,J., D'Eustachio,P., Givol,D. and Schlessinger,J.
  TITLE     Cloning and expression of a widely expressed receptor tyrosine
            phosphatase
  JOURNAL   Proc Natl Acad Sci U S A 87 (16), 6112-6116 (1990)
   PUBMED   2166945
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL161656.20 and AL121905.23.
            
            Summary: The protein encoded by this gene is a member of the
            protein tyrosine phosphatase (PTP) family. PTPs are known to be
            signaling molecules that regulate a variety of cellular processes
            including cell growth, differentiation, mitotic cycle, and
            oncogenic transformation. This PTP contains an extracellular
            domain, a single transmembrane segment and two tandem
            intracytoplasmic catalytic domains, and thus represents a
            receptor-type PTP. This PTP has been shown to dephosphorylate and
            activate Src family tyrosine kinases, and is implicated in the
            regulation of integrin signaling, cell adhesion and proliferation.
            Three alternatively spliced variants of this gene, which encode two
            distinct isoforms, have been reported. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK294499.1, SRR14038196.1198137.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..813
                     /product="receptor-type tyrosine-protein phosphatase alpha
                     isoform 3 precursor"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase, receptor type, alpha
                     polypeptide; PTPase-alpha; Leukocyte common
                     antigen-related peptide (protein tyrosine phosphate);
                     tyrosine phosphatase alpha; PTPLCA-related phosphatase;
                     receptor-type tyrosine-protein phosphatase alpha;
                     protein-tyrosine phosphatase alpha"
                     /calculated_mol_wt=88713
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3227
     Region          225..520
                     /region_name="R-PTPc-A-1"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase A, repeat 1; cd14621"
                     /db_xref="CDD:350469"
     Region          574..801
                     /region_name="R-PTPc-A-2"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase A, repeat 2; cd14623"
                     /db_xref="CDD:350471"
     CDS             1..813
                     /gene="PTPRA"
                     /gene_synonym="HEPTP; HLPR; HPTPA; HPTPalpha; LRP; PTPA;
                     PTPRL2; R-PTP-alpha; RPTPA"
                     /coded_by="NM_001385303.1:333..2774"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:5786"
                     /db_xref="HGNC:HGNC:9664"
                     /db_xref="MIM:176884"
ORIGIN      
        1 mddavqitki smdswfilvl lgsglicvsa nnattvapsv gitrlinsst aepvkeeakt
       61 snptssltsl svaptfspni tlgptylttv nssdsdngtt rtastnsigi tispngtwlp
      121 dnqftdarte pwegnsstaa ttpetfppsg nsdskdrrde tpiiavmval ssllvivfii
      181 ivlymlrfkk ykqagshsns frlsngrted vepqsvplla rspstnrkyp plpvdkleee
      241 inrrmaddnk lfreefnalp acpiqatcea askeenkekn ryvnilpydh srvhltpveg
      301 vpdsdyinas fingyqeknk fiaaqgpkee tvndfwrmiw eqntativmv tnlkerkeck
      361 caqywpdqgc wtygnirvsv edvtvlvdyt vrkfciqqvg dmtnrkpqrl itqfhftswp
      421 dfgvpftpig mlkflkkvka cnpqyagaiv vhcsagvgrt gtfvvidaml dmmhterkvd
      481 vygfvsrira qrcqmvqtdm qyvfiyqall ehylygdtel evtslethlq kiynkipgts
      541 nngleeefkk ltsikiqndk mrtgnlpanm kknrvlqiip yefnrviipv krgeentdyv
      601 nasfidgyrq kdsyiasqgp llhtiedfwr miwewkscsi vmlteleerg qekcaqywps
      661 dglvsygdit velkkeeece sytvrdllvt ntrenksrqi rqfhfhgwpe vgipsdgkgm
      721 isiiaavqkq qqqsgnhpit vhcsagagrt gtfcalstvl ervkaegild vfqtvkslrl
      781 qrphmvqtle qyefcykvvq eyidafsdya nfk
//
LOCUS       NP_001362763             503 aa            linear   PRI 21-NOV-2025
DEFINITION  WAS/WASL-interacting protein family member 1 isoform a [Homo
            sapiens].
ACCESSION   NP_001362763 XP_011510082
VERSION     NP_001362763.1
DBSOURCE    REFSEQ: accession NM_001375834.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Dong,Y., Jin,Q., Sun,M., Qi,D., Qu,H., Wang,X. and Quan,C.
  TITLE     CLDN6 inhibits breast cancer metastasis through WIP-dependent actin
            cytoskeleton-mediated autophagy
  JOURNAL   J Exp Clin Cancer Res 42 (1), 68 (2023)
   PUBMED   36935496
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 503)
  AUTHORS   Sokolik,C.G., Qassem,N. and Chill,J.H.
  TITLE     The Disordered Cellular Multi-Tasker WIP and Its Protein-Protein
            Interactions: A Structural View
  JOURNAL   Biomolecules 10 (7), 1084 (2020)
   PUBMED   32708183
  REMARK    GeneRIF: The Disordered Cellular Multi-Tasker WIP and Its
            Protein-Protein Interactions: A Structural View.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 503)
  AUTHORS   Vaduva,G., Martinez-Quiles,N., Anton,I.M., Martin,N.C., Geha,R.S.,
            Hopper,A.K. and Ramesh,N.
  TITLE     The human WASP-interacting protein, WIP, activates the cell
            polarity pathway in yeast
  JOURNAL   J Biol Chem 274 (24), 17103-17108 (1999)
   PUBMED   10358064
REFERENCE   7  (residues 1 to 503)
  AUTHORS   Stewart,D.M., Tian,L. and Nelson,D.L.
  TITLE     Mutations that cause the Wiskott-Aldrich syndrome impair the
            interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP
            interacting protein
  JOURNAL   J Immunol 162 (8), 5019-5024 (1999)
   PUBMED   10202051
REFERENCE   8  (residues 1 to 503)
  AUTHORS   Ramesh,N., Anton,I.M., Martinez-Quiles,N. and Geha,R.S.
  TITLE     Waltzing with WASP
  JOURNAL   Trends Cell Biol 9 (1), 15-19 (1999)
   PUBMED   10087612
  REMARK    Review article
REFERENCE   9  (residues 1 to 503)
  AUTHORS   Anton,I.M., Lu,W., Mayer,B.J., Ramesh,N. and Geha,R.S.
  TITLE     The Wiskott-Aldrich syndrome protein-interacting protein (WIP)
            binds to the adaptor protein Nck
  JOURNAL   J Biol Chem 273 (33), 20992-20995 (1998)
   PUBMED   9694849
REFERENCE   10 (residues 1 to 503)
  AUTHORS   Ramesh,N., Anton,I.M., Hartwig,J.H. and Geha,R.S.
  TITLE     WIP, a protein associated with wiskott-aldrich syndrome protein,
            induces actin polymerization and redistribution in lymphoid cells
  JOURNAL   Proc Natl Acad Sci U S A 94 (26), 14671-14676 (1997)
   PUBMED   9405671
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010894.10.
            
            On Nov 5, 2019 this sequence version replaced XP_011510082.1.
            
            Summary: This gene encodes a protein that plays an important role
            in the organization of the actin cytoskeleton. The encoded protein
            binds to a region of Wiskott-Aldrich syndrome protein that is
            frequently mutated in Wiskott-Aldrich syndrome, an X-linked
            recessive disorder. Impairment of the interaction between these two
            proteins may contribute to the disease. Two transcript variants
            encoding the same protein have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (5), as well as variants 1-4,
            encodes isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.810258.1,
                                           SRR14038197.1513463.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000679041.1/ ENSP00000503603.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..503
                     /product="WAS/WASL-interacting protein family member 1
                     isoform a"
                     /note="Wiskott-Aldrich syndrome protein interacting
                     protein; protein PRPL-2; WASP-interacting protein;
                     testicular tissue protein Li 226"
                     /calculated_mol_wt=51128
     Region          1..503
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43516.3)"
     Region          29..60
                     /region_name="WH2_WAS_WASL-1"
                     /note="Wiskott Aldrich syndrome homology region 2 (WH2
                     motif) in WAS/WASL-interacting protein family member 1;
                     cd22076"
                     /db_xref="CDD:409219"
     Site            order(29..33,35..37,39..41,44,46..60)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409219"
     Site            33
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8K1I7; propagated from
                     UniProtKB/Swiss-Prot (O43516.3)"
     Region          45..48
                     /region_name="Binds actin"
                     /note="propagated from UniProtKB/Swiss-Prot (O43516.3)"
     Region          46..49
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409219"
     Site            125
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8K1I7; propagated from
                     UniProtKB/Swiss-Prot (O43516.3)"
     Site            134
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8K1I7; propagated from
                     UniProtKB/Swiss-Prot (O43516.3)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K1I7; propagated from
                     UniProtKB/Swiss-Prot (O43516.3)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43516.3)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O43516.3)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43516.3)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43516.3)"
     CDS             1..503
                     /gene="WIPF1"
                     /gene_synonym="PRPL-2; WAS2; WASPIP; WIP"
                     /coded_by="NM_001375834.1:243..1754"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS2260.1"
                     /db_xref="GeneID:7456"
                     /db_xref="HGNC:HGNC:12736"
                     /db_xref="MIM:602357"
ORIGIN      
        1 mpvppppapp ppptfalant ekptlnkteq agrnallsdi skgkklkktv tndrsapild
       61 kpkgagaggg gggfgggggf gggggggggg sfggggppgl gglfqagmpk lrstanrdnd
      121 sggsrppllp pggrstsakp fsppsgpgrf pvpspghrsg ppepqrnrmp pprpdvgskp
      181 dsipppvpst prpiqssphn rgsppvpggp rqpspgptpp pfpgnrgtal gggsirqspl
      241 sssspfsnrp plpptpsral ddkppppppp vgnrpsihre avpppppqnn kppvpstprp
      301 sassqapppp pppsrpgppp lppsssgnde tprlpqrnls lssstpplps pgrsgplppp
      361 pserppppvr dppgrsgplp ppppvsrngs tsralpatpq lpsrsgvdsp rsgprpplpp
      421 drpsagappp pppstsirng fqdspcedew esrfyfhpis dlpppepyvq ttksypskla
      481 rnesrsgsnr rergapplpp ipr
//
LOCUS       NP_001350028             560 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger protein 250 isoform a [Homo sapiens].
ACCESSION   NP_001350028 XP_006716675
VERSION     NP_001350028.1
DBSOURCE    REFSEQ: accession NM_001363099.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 560)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 560)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   3  (residues 1 to 560)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 560)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 560)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   6  (residues 1 to 560)
  AUTHORS   Lorenz,P., Dietmann,S., Wilhelm,T., Koczan,D., Autran,S., Gad,S.,
            Wen,G., Ding,G., Li,Y., Rousseau-Merck,M.F. and Thiesen,H.J.
  TITLE     The ancient mammalian KRAB zinc finger gene cluster on human
            chromosome 8q24.3 illustrates principles of C2H2 zinc finger
            evolution associated with unique expression profiles in human
            tissues
  JOURNAL   BMC Genomics 11, 206 (2010)
   PUBMED   20346131
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 560)
  AUTHORS   Rual,J.F., Hirozane-Kishikawa,T., Hao,T., Bertin,N., Li,S.,
            Dricot,A., Li,N., Rosenberg,J., Lamesch,P., Vidalain,P.O.,
            Clingingsmith,T.R., Hartley,J.L., Esposito,D., Cheo,D., Moore,T.,
            Simmons,B., Sequerra,R., Bosak,S., Doucette-Stamm,L., Le Peuch,C.,
            Vandenhaute,J., Cusick,M.E., Albala,J.S., Hill,D.E. and Vidal,M.
  TITLE     Human ORFeome version 1.1: a platform for reverse proteomics
  JOURNAL   Genome Res 14 (10B), 2128-2135 (2004)
   PUBMED   15489335
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF235103.5, BI820228.1, BC017091.1, DB272357.1 and CA422363.1.
            
            On May 8, 2018 this sequence version replaced XP_006716675.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1922577.1,
                                           SRR14038195.299964.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..560
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..560
                     /product="zinc finger protein 250 isoform a"
                     /note="zinc finger protein 647; zinc finger protein (clone
                     647)"
                     /calculated_mol_wt=63337
     Region          22..82
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          178..537
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          201..221
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(206,208,210,212..213,216..217,220,234,236,240..241,
                     244..245,248,262,264,266,268..269,272..273,276)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          229..249
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          257..277
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          285..305
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          313..333
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          341..361
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          369..389
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          397..417
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          425..445
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          453..473
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          481..501
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(486,488,490,492..493,496..497,500,514,516,520..521,
                     524..525,528,542,544,546,548..549,552..553,556)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          509..529
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          537..557
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..560
                     /gene="ZNF250"
                     /gene_synonym="ZFP647; ZNF647"
                     /coded_by="NM_001363099.2:484..2166"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS34972.1"
                     /db_xref="GeneID:58500"
                     /db_xref="HGNC:HGNC:13044"
ORIGIN      
        1 maaarllpvp agpqplsfqa kltfedvavl lsqdewdrlc paqrglyrnv mmetygnvvs
       61 lglpgskpdi isqlergedp wvldrkgakk sqglwsdysd nlkydhttac tqqdslscpw
      121 ecetkgesqn tdlspkplis eqtvilgktp lgridqenne tkqsfclspn svdhrevqvl
      181 sqsmpltphq avpsgerpym cvecgkcfgr sshllqhqri htgekpyvcs vcgkafsqss
      241 vlskhrriht gekpyecnec gkafrvssdl aqhhkihtge kpheclecrk aftqlshliq
      301 hqrihtgerp yvcplcgkaf nhstvlrshq rvhtgekphr cnecgktfsv krtllqhqri
      361 htgekpytcs ecgkafsdrs vliqhhnvht gekpyecsec gktfshrstl mnherihtee
      421 kpyacyecgk afvqhshliq hqrvhtgekp yvcgecghaf sarrsliqhe rihtgekpfq
      481 ctecgkafsl katlivhlrt htgekpyecn scgkafsqys vliqhqriht gekpyecgec
      541 grafnqhghl iqhqkvhrkl
//
LOCUS       NP_001337354             998 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 1 isoform 21 [Homo
            sapiens].
ACCESSION   NP_001337354 XP_016866030
VERSION     NP_001337354.1
DBSOURCE    REFSEQ: accession NM_001350425.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 998)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 998)
  AUTHORS   Ruhle,F., Witten,A., Barysenka,A., Huge,A., Arning,A., Heller,C.,
            Krumpel,A., Mesters,R., Franke,A., Lieb,W., Riemenschneider,M.,
            Hiersche,M., Limperger,V., Nowak-Gottl,U. and Stoll,M.
  TITLE     Rare genetic variants in SMAP1, B3GAT2, and RIMS1 contribute to
            pediatric venous thromboembolism
  JOURNAL   Blood 129 (6), 783-790 (2017)
   PUBMED   28011674
  REMARK    GeneRIF: The study identified a region on chromosome 6 comprising
            the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus
            for pediatric venous thromboembolism.
REFERENCE   6  (residues 1 to 998)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 998)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
REFERENCE   8  (residues 1 to 998)
  AUTHORS   Schoch,S., Castillo,P.E., Jo,T., Mukherjee,K., Geppert,M., Wang,Y.,
            Schmitz,F., Malenka,R.C. and Sudhof,T.C.
  TITLE     RIM1alpha forms a protein scaffold for regulating neurotransmitter
            release at the active zone
  JOURNAL   Nature 415 (6869), 321-326 (2002)
   PUBMED   11797009
REFERENCE   9  (residues 1 to 998)
  AUTHORS   Coppola,T., Magnin-Luthi,S., Perret-Menoud,V., Gattesco,S.,
            Schiavo,G. and Regazzi,R.
  TITLE     Direct interaction of the Rab3 effector RIM with Ca2+ channels,
            SNAP-25, and synaptotagmin
  JOURNAL   J Biol Chem 276 (35), 32756-32762 (2001)
   PUBMED   11438518
REFERENCE   10 (residues 1 to 998)
  AUTHORS   Betz,A., Thakur,P., Junge,H.J., Ashery,U., Rhee,J.S., Scheuss,V.,
            Rosenmund,C., Rettig,J. and Brose,N.
  TITLE     Functional interaction of the active zone proteins Munc13-1 and
            RIM1 in synaptic vesicle priming
  JOURNAL   Neuron 30 (1), 183-196 (2001)
   PUBMED   11343654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590011.5, AL445256.18 and
            AL035633.18.
            
            On Apr 14, 2017 this sequence version replaced XP_016866030.1.
            
            Summary: The protein encoded by this gene is a RAS gene superfamily
            member that regulates synaptic vesicle exocytosis. This gene also
            plays a role in the regulation of voltage-gated calcium channels
            during neurotransmitter and insulin release. Mutations have
            suggested a role cognition and have been identified as the cause of
            cone-rod dystrophy type 7. Multiple transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Mar 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.118977.1,
                                           SRR1803611.123230.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..998
                     /product="regulating synaptic membrane exocytosis protein
                     1 isoform 21"
                     /note="RAB3-interacting protein 2; rab3-interacting
                     molecule 1; rab-3-interacting protein 2"
                     /calculated_mol_wt=111327
     Region          68..164
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(89..95,110,113,143,147,150..151)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          216..342
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(247,253,308,310,318)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          829..974
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(886,890..891,893,896,924,926,928,972..973)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..998
                     /gene="RIMS1"
                     /gene_synonym="CORD7; RAB3IP2; RIM; RIM1"
                     /coded_by="NM_001350425.2:231..3227"
                     /note="isoform 21 is encoded by transcript variant 21"
                     /db_xref="GeneID:22999"
                     /db_xref="HGNC:HGNC:17282"
                     /db_xref="MIM:606629"
ORIGIN      
        1 mcapgihvss egweevrsvd seegtiearr avagdldyyw ldpatwhsre tspisshpvt
       61 wqpskegdrl igrvilnkrt tmpkdsgall glkvvggkmt dlgrlgafit kvkkgsladv
      121 vghlragdev lewngkplpg atneevynii lesksepqve iivsrpigdi pripesshpp
      181 lesssssfes qkmerpsisv isptspgalk dapqvlpgql svklwydkvg hqlivnvlqa
      241 tdlparvdgr prnpyvkmyf lpdrsdkskr rtktvkkile pkwnqtfvys hvhrrdfrer
      301 mleitvwdqp rvqeeesefl geilieleta llddephwyk lqthdesslp lpqpspfmpr
      361 rhihgesssk klqrsqrisd sdisdyevdd gigvvppgyr ssareskstt ltvpeqqrtt
      421 hhrsrsvsph rgndqgkprs rlpnvplqrs ldeihptrrs rsptrhhdas rspvdhrtrd
      481 vdsqylseqd sellmlprak rgrsaeclht tselqpfldr arsastnclr pdtslhsper
      541 ermhrqrspt qsppadtsfs srrgrqlpqv pvrsgsieqe qekynsstka slvveertrq
      601 mkmkvhrfkq ttgsgssqel dreqyskyni hkdqyrscdn vsakssdsdv sdvsaisrts
      661 sasrlsstsf mseqserprg rissftpkmq grrmgtsgrs imkstsvsge mytlehndgs
      721 qsdtavgtvg aggkkrrssl sakvvaivsr rsrstsqlsq tesghkklks tiqrstetgm
      781 aaemrkmvrq psrestdgsi nsyssegnli fpgvrlgads qfsdfldglg paqlvgrqtl
      841 atpamgdiqi gmedkkgqle vevirarslt qkpgskstpa pyvkvyllen gaciakkktr
      901 iarktldply qqslvfdesp qgkvlqvivw gdygrmdhkc fmgvaqille eldlssmvig
      961 wyklfppssl vdptltpltr rasqssless tgppcirs
//
LOCUS       NP_001304162             155 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial carrier homolog 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001304162
VERSION     NP_001304162.1
DBSOURCE    REFSEQ: accession NM_001317233.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Ulupinar,P., Caglayan,E., Rayaman,E., Nagata,K. and Turan,K.
  TITLE     The mitochondrial carrier homolog 2 is involved in down-regulation
            of influenza A virus replication
  JOURNAL   Mol Biol Rep 51 (1), 642 (2024)
   PUBMED   38727866
  REMARK    GeneRIF: The mitochondrial carrier homolog 2 is involved in
            down-regulation of influenza A virus replication.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Zheng,X. and Chu,B.
  TITLE     The biology of mitochondrial carrier homolog 2
  JOURNAL   Mitochondrion 75, 101837 (2024)
   PUBMED   38158152
  REMARK    GeneRIF: The biology of mitochondrial carrier homolog 2.
            Review article
REFERENCE   4  (residues 1 to 155)
  AUTHORS   Goldman,A., Mullokandov,M., Zaltsman,Y., Regev,L., Levin-Zaidman,S.
            and Gross,A.
  TITLE     MTCH2 cooperates with MFN2 and lysophosphatidic acid synthesis to
            sustain mitochondrial fusion
  JOURNAL   EMBO Rep 25 (1), 45-67 (2024)
   PUBMED   38177900
  REMARK    GeneRIF: MTCH2 cooperates with MFN2 and lysophosphatidic acid
            synthesis to sustain mitochondrial fusion.
REFERENCE   5  (residues 1 to 155)
  AUTHORS   Eswarappa,S.M., Potdar,A.A., Koch,W.J., Fan,Y., Vasu,K.,
            Lindner,D., Willard,B., Graham,L.M., DiCorleto,P.E. and Fox,P.L.
  TITLE     Programmed translational readthrough generates antiangiogenic
            VEGF-Ax
  JOURNAL   Cell 157 (7), 1605-1618 (2014)
   PUBMED   24949972
REFERENCE   6  (residues 1 to 155)
  AUTHORS   Renstrom,F., Payne,F., Nordstrom,A., Brito,E.C., Rolandsson,O.,
            Hallmans,G., Barroso,I., Nordstrom,P. and Franks,P.W.
  CONSRTM   GIANT Consortium
  TITLE     Replication and extension of genome-wide association study results
            for obesity in 4923 adults from northern Sweden
  JOURNAL   Hum Mol Genet 18 (8), 1489-1496 (2009)
   PUBMED   19164386
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 155)
  AUTHORS   Willer,C.J., Speliotes,E.K., Loos,R.J., Li,S., Lindgren,C.M.,
            Heid,I.M., Berndt,S.I., Elliott,A.L., Jackson,A.U., Lamina,C.,
            Lettre,G., Lim,N., Lyon,H.N., McCarroll,S.A., Papadakis,K., Qi,L.,
            Randall,J.C., Roccasecca,R.M., Sanna,S., Scheet,P., Weedon,M.N.,
            Wheeler,E., Zhao,J.H., Jacobs,L.C., Prokopenko,I., Soranzo,N.,
            Tanaka,T., Timpson,N.J., Almgren,P., Bennett,A., Bergman,R.N.,
            Bingham,S.A., Bonnycastle,L.L., Brown,M., Burtt,N.P., Chines,P.,
            Coin,L., Collins,F.S., Connell,J.M., Cooper,C., Smith,G.D.,
            Dennison,E.M., Deodhar,P., Elliott,P., Erdos,M.R., Estrada,K.,
            Evans,D.M., Gianniny,L., Gieger,C., Gillson,C.J., Guiducci,C.,
            Hackett,R., Hadley,D., Hall,A.S., Havulinna,A.S., Hebebrand,J.,
            Hofman,A., Isomaa,B., Jacobs,K.B., Johnson,T., Jousilahti,P.,
            Jovanovic,Z., Khaw,K.T., Kraft,P., Kuokkanen,M., Kuusisto,J.,
            Laitinen,J., Lakatta,E.G., Luan,J., Luben,R.N., Mangino,M.,
            McArdle,W.L., Meitinger,T., Mulas,A., Munroe,P.B., Narisu,N.,
            Ness,A.R., Northstone,K., O'Rahilly,S., Purmann,C., Rees,M.G.,
            Ridderstrale,M., Ring,S.M., Rivadeneira,F., Ruokonen,A.,
            Sandhu,M.S., Saramies,J., Scott,L.J., Scuteri,A., Silander,K.,
            Sims,M.A., Song,K., Stephens,J., Stevens,S., Stringham,H.M.,
            Tung,Y.C., Valle,T.T., Van Duijn,C.M., Vimaleswaran,K.S.,
            Vollenweider,P., Waeber,G., Wallace,C., Watanabe,R.M.,
            Waterworth,D.M., Watkins,N., Witteman,J.C., Zeggini,E., Zhai,G.,
            Zillikens,M.C., Altshuler,D., Caulfield,M.J., Chanock,S.J.,
            Farooqi,I.S., Ferrucci,L., Guralnik,J.M., Hattersley,A.T., Hu,F.B.,
            Jarvelin,M.R., Laakso,M., Mooser,V., Ong,K.K., Ouwehand,W.H.,
            Salomaa,V., Samani,N.J., Spector,T.D., Tuomi,T., Tuomilehto,J.,
            Uda,M., Uitterlinden,A.G., Wareham,N.J., Deloukas,P.,
            Frayling,T.M., Groop,L.C., Hayes,R.B., Hunter,D.J., Mohlke,K.L.,
            Peltonen,L., Schlessinger,D., Strachan,D.P., Wichmann,H.E.,
            McCarthy,M.I., Boehnke,M., Barroso,I., Abecasis,G.R. and
            Hirschhorn,J.N.
  CONSRTM   Wellcome Trust Case Control Consortium; Genetic Investigation of
            ANthropometric Traits Consortium
  TITLE     Six new loci associated with body mass index highlight a neuronal
            influence on body weight regulation
  JOURNAL   Nat Genet 41 (1), 25-34 (2009)
   PUBMED   19079261
  REMARK    GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 155)
  AUTHORS   Grinberg,M., Schwarz,M., Zaltsman,Y., Eini,T., Niv,H.,
            Pietrokovski,S. and Gross,A.
  TITLE     Mitochondrial carrier homolog 2 is a target of tBID in cells
            signaled to die by tumor necrosis factor alpha
  JOURNAL   Mol Cell Biol 25 (11), 4579-4590 (2005)
   PUBMED   15899861
  REMARK    GeneRIF: Mtch2 is a mitochondrial target of tBID and possibly
            participates in the mitochondrial apoptotic program.
REFERENCE   9  (residues 1 to 155)
  AUTHORS   Yerushalmi,G.M., Leibowitz-Amit,R., Shaharabany,M. and Tsarfaty,I.
  TITLE     Met-HGF/SF signal transduction induces mimp, a novel mitochondrial
            carrier homologue, which leads to mitochondrial depolarization
  JOURNAL   Neoplasia 4 (6), 510-522 (2002)
   PUBMED   12407445
REFERENCE   10 (residues 1 to 155)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK313032.1, AK295218.1,
            AY380792.1 and AC104942.5.
            
            Summary: This gene encodes a member of the SLC25 family of
            nuclear-encoded transporters that are localized in the inner
            mitochondrial membrane. Members of this superfamily are involved in
            many metabolic pathways and cell functions. Genome-wide association
            studies in human have identified single-nucleotide polymorphisms in
            several loci associated with obesity. This gene is one such locus,
            which is highly expressed in white adipose tissue and adipocytes,
            and thought to play a regulatory role in adipocyte differentiation
            and biology. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. A recent study
            showed this gene to be an authentic stop codon readthrough target
            that can produce two isoforms from the same mRNA by use of
            alternative in-frame translation termination codons. [provided by
            RefSeq, Dec 2017].
            
            Transcript Variant: This variant (3) lacks an exon in the 5'
            region, which results in translation initiation from an in-frame,
            downstream start codon compared to variant 1. The encoded isoform
            (3) has a shorter N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.61828.1, AK295218.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..155
                     /product="mitochondrial carrier homolog 2 isoform 3"
                     /note="met-induced mitochondrial protein; mitochondrial
                     carrier homolog 2; solute carrier family 25, member 50"
                     /calculated_mol_wt=17151
     Region          <1..>44
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     CDS             1..155
                     /gene="MTCH2"
                     /gene_synonym="HSPC032; MIMP; SLC25A50"
                     /coded_by="NM_001317233.2:481..948"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:23788"
                     /db_xref="HGNC:HGNC:17587"
                     /db_xref="MIM:613221"
ORIGIN      
        1 mvqfigresk ycglcdsiit iyreegilgf faglvprllg dilslwlcns laylvntyal
       61 dsgvstmnem ksysqavtgf fasmltypfv lvsnlmavnn cglaggcppy spiytswidc
      121 wcmlqkegnm srgnslffrk vpfgktyccd lkmli
//
LOCUS       NP_060450                365 aa            linear   PRI 21-NOV-2025
DEFINITION  LIM and senescent cell antigen-like-containing domain protein 2
            isoform 2 [Homo sapiens].
ACCESSION   NP_060450
VERSION     NP_060450.2
DBSOURCE    REFSEQ: accession NM_017980.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Gorska,A. and Mazur,A.J.
  TITLE     Integrin-linked kinase (ILK): the known vs. the unknown and
            perspectives
  JOURNAL   Cell Mol Life Sci 79 (2), 100 (2022)
   PUBMED   35089438
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Wang,J. and Zhang,S.
  TITLE     Fluid shear stress modulates endothelial inflammation by targeting
            LIMS2
  JOURNAL   Exp Biol Med (Maywood) 245 (18), 1656-1663 (2020)
   PUBMED   32752897
  REMARK    GeneRIF: Fluid shear stress modulates endothelial inflammation by
            targeting LIMS2.
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Xu,H., Cao,H. and Xiao,G.
  TITLE     Signaling via PINCH: Functions, binding partners and implications
            in human diseases
  JOURNAL   Gene 594 (1), 10-15 (2016)
   PUBMED   27590440
  REMARK    GeneRIF: Mammalian cells have two functional PINCH proteins, PINCH1
            and PINCH2. PINCH not only binds to Nck2 and engages in the
            signaling of growth factor receptors, but also forms a ternary
            complex with ILK and parvin (IPP complex).
            Review article
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Chardon,J.W., Smith,A.C., Woulfe,J., Pena,E., Rakhra,K., Dennie,C.,
            Beaulieu,C., Huang,L., Schwartzentruber,J., Hawkins,C., Harms,M.B.,
            Dojeiji,S., Zhang,M., Majewski,J., Bulman,D.E., Boycott,K.M. and
            Dyment,D.A.
  CONSRTM   FORGE Canada Consortium
  TITLE     LIMS2 mutations are associated with a novel muscular dystrophy,
            severe cardiomyopathy and triangular tongues
  JOURNAL   Clin Genet 88 (6), 558-564 (2015)
   PUBMED   25589244
  REMARK    GeneRIF: Data indicate compound heterozygous missense mutations
            that are predicted to be pathogenic in LIM and senescent cell
            antigen-like domains 2 protein (LIMS2).
REFERENCE   6  (residues 1 to 365)
  AUTHORS   Shi,X., Qu,H., Kretzler,M. and Wu,C.
  TITLE     Roles of PINCH-2 in regulation of glomerular cell shape change and
            fibronectin matrix deposition
  JOURNAL   Am J Physiol Renal Physiol 295 (1), F253-F263 (2008)
   PUBMED   18480182
REFERENCE   7  (residues 1 to 365)
  AUTHORS   Liu,Y., Liu,J., Chen,J., Cheng,L., Cao,Q., Zhu,L., Sun,Y., Liu,Q.
            and Li,J.
  TITLE     Molecular cloning and characterization of a novel splice variant of
            the LIM domain family gene, PINCH 2, in human testis
  JOURNAL   Mol Biotechnol 35 (2), 109-118 (2007)
   PUBMED   17435276
REFERENCE   8  (residues 1 to 365)
  AUTHORS   Kim,S.K., Jang,H.R., Kim,J.H., Noh,S.M., Song,K.S., Kim,M.R.,
            Kim,S.Y., Yeom,Y.I., Kim,N.S., Yoo,H.S. and Kim,Y.S.
  TITLE     The epigenetic silencing of LIMS2 in gastric cancer and its
            inhibitory effect on cell migration
  JOURNAL   Biochem Biophys Res Commun 349 (3), 1032-1040 (2006)
   PUBMED   16959213
  REMARK    GeneRIF: LIMS2 may be useful as a molecular biomarker and a
            therapeutic target by increasing its expression and activity in
            gastric cancer
REFERENCE   9  (residues 1 to 365)
  AUTHORS   Zhang,Y., Chen,K., Guo,L. and Wu,C.
  TITLE     Characterization of PINCH-2, a new focal adhesion protein that
            regulates the PINCH-1-ILK interaction, cell spreading, and
            migration
  JOURNAL   J Biol Chem 277 (41), 38328-38338 (2002)
   PUBMED   12167643
  REMARK    GeneRIF: These results identify a novel nuclear and focal adhesion
            protein that associates with ILK and reveals an important role of
            PINCH-2 in the regulation of the PINCH-1-ILK interaction, cell
            shape change, and migration.
REFERENCE   10 (residues 1 to 365)
  AUTHORS   Tu,Y., Huang,Y., Zhang,Y., Hua,Y. and Wu,C.
  TITLE     A new focal adhesion protein that interacts with integrin-linked
            kinase and regulates cell adhesion and spreading
  JOURNAL   J Cell Biol 153 (3), 585-598 (2001)
   PUBMED   11331308
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC074114.6, BP221000.1,
            AF527764.1 and AF527765.1.
            
            On Jan 13, 2004 this sequence version replaced NP_060450.1.
            
            Summary: This gene encodes a member of a small family of focal
            adhesion proteins which interacts with ILK (integrin-linked
            kinase), a protein which effects protein-protein interactions with
            the extraceullar matrix. The encoded protein has five LIM domains,
            each domain forming two zinc fingers, which permit interactions
            which regulate cell shape and migration. A pseudogene of this gene
            is located on chromosome 4. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (2) has a distinct N-terminus and is longer than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF527764.1, SRR18074967.1992036.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..365
                     /product="LIM and senescent cell antigen-like-containing
                     domain protein 2 isoform 2"
                     /note="LIM and senescent cell antigen-like-containing
                     domain protein 2; LIM and senescent cell antigen-like
                     domains 2; LIM-type zinc finger domains 2; ILK-binding
                     protein; particularly interesting new Cys-His protein 2"
                     /calculated_mol_wt=41381
     Region          39..97
                     /region_name="LIM1_PINCH"
                     /note="The first LIM domain of protein PINCH; cd09331"
                     /db_xref="CDD:188717"
     Site            order(39,42,61,64,67,70,88,91)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188717"
     Site            order(41..42,44,66,68..72,82..83,85,90..91,93..97)
                     /site_type="other"
                     /note="ILK binding interface"
                     /db_xref="CDD:188717"
     Region          100..151
                     /region_name="LIM2_PINCH"
                     /note="The second LIM domain of protein PINCH; cd09332"
                     /db_xref="CDD:188718"
     Site            order(100,103,120,123,126,129,147,150)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188718"
     Region          164..214
                     /region_name="LIM3_PINCH"
                     /note="The third LIM domain of protein PINCH; cd09333"
                     /db_xref="CDD:188719"
     Site            order(164,167,184,187,190,193,210,213)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188719"
     Region          220..273
                     /region_name="LIM4_PINCH"
                     /note="The fourth LIM domain of protein PINCH; cd09334"
                     /db_xref="CDD:188720"
     Site            order(221,225..228)
                     /site_type="other"
                     /note="N(i)ck binding interface"
                     /db_xref="CDD:188720"
     Site            order(222,225,242,245,248,251,269,272)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188720"
     Region          281..334
                     /region_name="LIM5_PINCH"
                     /note="The fifth LIM domain of protein PINCH; cd09335"
                     /db_xref="CDD:188721"
     Site            order(281,284,301,304,307,310,329,332)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188721"
     CDS             1..365
                     /gene="LIMS2"
                     /gene_synonym="LGMD2W; MDRCMTT; PINCH-2; PINCH2"
                     /coded_by="NM_017980.5:206..1303"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS2147.1"
                     /db_xref="GeneID:55679"
                     /db_xref="HGNC:HGNC:16084"
                     /db_xref="MIM:607908"
ORIGIN      
        1 maarlgalaa sglyrrrqhr qspppatgnm sdalanavcq rcqarfspae rivnsngely
       61 hehcfvcaqc frpfpeglfy efegrkyceh dfqmlfapcc gscgefiigr vikamnnnwh
      121 pgcfrcelcd veladlgfvk nagrhlcrpc hnrekakglg kyicqrchlv ideqplmfrs
      181 dayhpdhfnc thcgkeltae arelkgelyc lpchdkmgvp icgacrrpie grvvnalgkq
      241 whvehfvcak cekpflghrh yekkglayce thynqlfgdv cyncshvieg dvvsalnkaw
      301 cvscfscstc nskltlknkf vefdmkpvck rcyekfplel kkrlkklsel tsrkaqpkat
      361 dlnsa
//
LOCUS       NP_001382249            1019 aa            linear   PRI 21-NOV-2025
DEFINITION  myomegalin isoform 39 [Homo sapiens].
ACCESSION   NP_001382249
VERSION     NP_001382249.1
DBSOURCE    REFSEQ: accession NM_001395320.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Pan,R., Dai,J., Liang,W., Wang,H., Ye,L., Ye,S., Lin,Z., Huang,S.,
            Xiong,Y., Zhang,L., Lu,L., Wang,O., Shen,X., Liao,W. and Lu,X.
  TITLE     PDE4DIP contributes to colorectal cancer growth and chemoresistance
            through modulation of the NF1/RAS signaling axis
  JOURNAL   Cell Death Dis 14 (6), 373 (2023)
   PUBMED   37355626
  REMARK    GeneRIF: PDE4DIP contributes to colorectal cancer growth and
            chemoresistance through modulation of the NF1/RAS signaling axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   4  (residues 1 to 1019)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 1019)
  AUTHORS   Abou Ziki,M.D., Bhat,N., Neogi,A., Driscoll,T.P., Ugwu,N., Liu,Y.,
            Smith,E., Abboud,J.M., Chouairi,S., Schwartz,M.A., Akar,J.G. and
            Mani,A.
  TITLE     Epistatic interaction of PDE4DIP and DES mutations in familial
            atrial fibrillation with slow conduction
  JOURNAL   Hum Mutat 42 (10), 1279-1293 (2021)
   PUBMED   34289528
  REMARK    GeneRIF: Epistatic interaction of PDE4DIP and DES mutations in
            familial atrial fibrillation with slow conduction.
REFERENCE   6  (residues 1 to 1019)
  AUTHORS   Shimada,H., Kuboshima,M., Shiratori,T., Nabeya,Y., Takeuchi,A.,
            Takagi,H., Nomura,F., Takiguchi,M., Ochiai,T. and Hiwasa,T.
  TITLE     Serum anti-myomegalin antibodies in patients with esophageal
            squamous cell carcinoma
  JOURNAL   Int J Oncol 30 (1), 97-103 (2007)
   PUBMED   17143517
  REMARK    GeneRIF: MMGL-antibody is significantly with a favorable prognosis.
            Consequently, MMGL-anatibodies may be a useful tumor marker to
            diagnose and establish a prognosis in patients with esophageal
            squamous cell carcinoma.
REFERENCE   7  (residues 1 to 1019)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 1019)
  AUTHORS   Soejima,H., Kawamoto,S., Akai,J., Miyoshi,O., Arai,Y., Morohka,T.,
            Matsuo,S., Niikawa,N., Kimura,A., Okubo,K. and Mukai,T.
  TITLE     Isolation of novel heart-specific genes using the BodyMap database
  JOURNAL   Genomics 74 (1), 115-120 (2001)
   PUBMED   11374908
REFERENCE   9  (residues 1 to 1019)
  AUTHORS   Verde,I., Pahlke,G., Salanova,M., Zhang,G., Wang,S., Coletti,D.,
            Onuffer,J., Jin,S.L. and Conti,M.
  TITLE     Myomegalin is a novel protein of the golgi/centrosome that
            interacts with a cyclic nucleotide phosphodiesterase
  JOURNAL   J Biol Chem 276 (14), 11189-11198 (2001)
   PUBMED   11134006
REFERENCE   10 (residues 1 to 1019)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC245389.1 and AC239802.3.
            
            Summary: The protein encoded by this gene serves to anchor
            phosphodiesterase 4D to the Golgi/centrosome region of the cell.
            Defects in this gene may be a cause of myeloproliferative disorder
            (MBD) associated with eosinophilia. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.180983.1,
                                           SRR1803614.185852.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     Protein         1..1019
                     /product="myomegalin isoform 39"
                     /note="myomegalin; cardiomyopathy-associated protein 2"
                     /calculated_mol_wt=118295
     Region          69..745
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          72..139
                     /region_name="Cnn_1N"
                     /note="Centrosomin N-terminal motif 1; pfam07989"
                     /db_xref="CDD:462333"
     CDS             1..1019
                     /gene="PDE4DIP"
                     /gene_synonym="CMYA2; MMGL"
                     /coded_by="NM_001395320.1:267..3326"
                     /note="isoform 39 is encoded by transcript variant 39"
                     /db_xref="GeneID:9659"
                     /db_xref="HGNC:HGNC:15580"
                     /db_xref="MIM:608117"
ORIGIN      
        1 meqtwtrdyf aeddgemvpr tshtaaflsd tkdrgppvqs qiwrsgekvp fvqtyslraf
       61 ekppqvqtqa lrdfekhlnd lkkenfslkl riyfleermq qkyeasredi ykrnielkve
      121 veslkrelqd kkqhldktwa dvenlnsqne aelrrqfeer qqetehvyel lenkiqllqe
      181 esrlakneaa rmaalveaek ecnlelsekl kgvtknwedv pgdqvkpdqy tealaqrdkr
      241 ieelnqslaa qerlveqlsr ekqqllhlle eptsmevqpm teellkqqkl nshettitqq
      301 svsdshlael qekiqqteat nkilqeklne msyelkcaqe ssqkqdgtiq nlketlksre
      361 reteelyqvi egqndtmakl remlhqsqlg qlhssegtsp aqqqvalldl qsalfcsqle
      421 iqklqrvvrq kerqladakq cvqfveaaah eseqqkeasw khnqelrkal qqlqeelqnk
      481 sqqlraweae kyneirtqeq niqhlnhsls hkeqllqefr ellqyrdnsd ktleanemll
      541 eklrqrihdk avaleraide kfsaleekek elrqlrlavr erdhdlerlr dvlssneatm
      601 qsmesllrak gleveqlstt cqnlqwlkee metkfsrwqk eqesiiqqlq tslhdrnkev
      661 edlsatllck lgpgqseiae elcqrlqrke rmlqdllsdr nkqvleheme iqgllqsvst
      721 reqesqaaae klvqalmern selqalrqyl ggrdslmsqa pisnqqaevt ptgrlgkqtd
      781 qgsmqipsrd dstsltaked vsiprstlgd ldtvagleke lsnakeelel makkeresqm
      841 elsalqsmma vqeeelqvqa admesltrni qikedlikdl qmqlvdpedi pamerltqev
      901 lllrekvasv esqgqeisgn rrqqlllmle glvdersrln ealqaerqly sslvkfhahp
      961 esserdrtlq velegaqvlr srleevlgrs lerlnrletl aaigggeles vrihhkhay
//
LOCUS       NP_001356579             356 aa            linear   PRI 21-NOV-2025
DEFINITION  snRNA-activating protein complex subunit 3 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001356579
VERSION     NP_001356579.1
DBSOURCE    REFSEQ: accession NM_001369650.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Sun,J., Li,X., Hou,X., Cao,S., Cao,W., Zhang,Y., Song,J., Wang,M.,
            Wang,H., Yan,X., Li,Z., Roeder,R.G. and Wang,W.
  TITLE     Structural basis of human SNAPc recognizing proximal sequence
            element of snRNA promoter
  JOURNAL   Nat Commun 13 (1), 6871 (2022)
   PUBMED   36369505
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Henry,R.W., Mittal,V., Ma,B., Kobayashi,R. and Hernandez,N.
  TITLE     SNAP19 mediates the assembly of a functional core promoter complex
            (SNAPc) shared by RNA polymerases II and III
  JOURNAL   Genes Dev 12 (17), 2664-2672 (1998)
   PUBMED   9732265
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Henry,R.W., Ma,B., Sadowski,C.L., Kobayashi,R. and Hernandez,N.
  TITLE     Cloning and characterization of SNAP50, a subunit of the
            snRNA-activating protein complex SNAPc
  JOURNAL   EMBO J 15 (24), 7129-7136 (1996)
   PUBMED   9003788
REFERENCE   8  (residues 1 to 356)
  AUTHORS   Bai,L., Wang,Z., Yoon,J.B. and Roeder,R.G.
  TITLE     Cloning and characterization of the beta subunit of human proximal
            sequence element-binding transcription factor and its involvement
            in transcription of small nuclear RNA genes by RNA polymerases II
            and III
  JOURNAL   Mol Cell Biol 16 (10), 5419-5426 (1996)
   PUBMED   8816454
REFERENCE   9  (residues 1 to 356)
  AUTHORS   Henry,R.W., Sadowski,C.L., Kobayashi,R. and Hernandez,N.
  TITLE     A TBP-TAF complex required for transcription of human snRNA genes
            by RNA polymerase II and III
  JOURNAL   Nature 374 (6523), 653-656 (1995)
   PUBMED   7715707
REFERENCE   10 (residues 1 to 356)
  AUTHORS   Bagramian,E.R., Bogdanova,E.A., Krymskaia,M.L. and Sokovykh,S.I.
  TITLE     [Diagnostic importance of determining 17-ketosteroids in
            gynecology]
  JOURNAL   Akush Ginekol (Mosk) (2), 65-67 (1977)
   PUBMED   900378
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL441925.16.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1194743.1,
                                           SRR18074967.129400.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p22.3"
     Protein         1..356
                     /product="snRNA-activating protein complex subunit 3
                     isoform 5"
                     /note="snRNA-activating protein complex subunit 3; SNAPc
                     subunit 3; PTF subunit beta; SNAPc 50 kDa subunit;
                     PSE-binding factor subunit beta; snRNA-activating protein
                     complex 50 kDa subunit; proximal sequence element-binding
                     transcription factor subunit beta; small nuclear RNA
                     activating complex, polypeptide 3, 50kD; small nuclear RNA
                     activating complex, polypeptide 3, 50kDa"
                     /calculated_mol_wt=40126
     Region          202..350
                     /region_name="SNAPC3"
                     /note="snRNA-activating protein complex (SNAPc), subunit
                     3; pfam12251"
                     /db_xref="CDD:463506"
     CDS             1..356
                     /gene="SNAPC3"
                     /gene_synonym="PTFbeta; SNAP50"
                     /coded_by="NM_001369650.3:5..1075"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:6619"
                     /db_xref="HGNC:HGNC:11136"
                     /db_xref="MIM:602348"
ORIGIN      
        1 maegsrggpt csgvggrqdp vsgsggcnfp eyelpelntr afhvgafgel wrgrlrgagd
       61 lslreppasa lpgsqaadsd redaavardl dcsleaaael ravcgldklk cledgedpev
      121 ipentdlvtl gvrkrflehr eetitidrac rqetfvyeme shaigkkpen sadmieegel
      181 ilsvnilypv ifhkhkehkp yqtmlvlgsq kltqlrdsir cvsdlqigge fsntpdqape
      241 hiskdlyksa ffyfegtfyn dkrypecrdl srlvhhddcl drtlypllik khwlwtrkcf
      301 vckmytarwv tnndsfaped pcffcdvcfr mlhydsegnk lgeflaypyv dpgtfn
//
LOCUS       NP_001035719             193 aa            linear   PRI 21-NOV-2025
DEFINITION  neurocalcin-delta [Homo sapiens].
ACCESSION   NP_001035719
VERSION     NP_001035719.1
DBSOURCE    REFSEQ: accession NM_001040629.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Feng,L.Y. and Li,L.
  TITLE     Low expression of NCALD is associated with chemotherapy resistance
            and poor prognosis in epithelial ovarian cancer
  JOURNAL   J Ovarian Res 13 (1), 35 (2020)
   PUBMED   32228639
  REMARK    GeneRIF: Low expression of NCALD is associated with chemotherapy
            resistance and poor prognosis in epithelial ovarian cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 193)
  AUTHORS   O'Callaghan,D.W., Ivings,L., Weiss,J.L., Ashby,M.C., Tepikin,A.V.
            and Burgoyne,R.D.
  TITLE     Differential use of myristoyl groups on neuronal calcium sensor
            proteins as a determinant of spatio-temporal aspects of Ca2+ signal
            transduction
  JOURNAL   J Biol Chem 277 (16), 14227-14237 (2002)
   PUBMED   11836243
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Wang,W., Zhou,Z., Zhao,W., Huang,Y., Tang,R., Ying,K., Xie,Y. and
            Mao,Y.
  TITLE     Molecular cloning, mapping and characterization of the human
            neurocalcin delta gene (NCALD)
  JOURNAL   Biochim Biophys Acta 1518 (1-2), 162-167 (2001)
   PUBMED   11267673
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Burgoyne,R.D. and Weiss,J.L.
  TITLE     The neuronal calcium sensor family of Ca2+-binding proteins
  JOURNAL   Biochem J 353 (Pt 1), 1-12 (2001)
   PUBMED   11115393
  REMARK    Review article
            Erratum:[Biochem J 2001 Mar 15;354(Pt 3):727]
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Ladant,D.
  TITLE     Calcium and membrane binding properties of bovine neurocalcin delta
            expressed in Escherichia coli
  JOURNAL   J Biol Chem 270 (7), 3179-3185 (1995)
   PUBMED   7852401
  REMARK    GeneRIF: The author characterizes the biochemical properties of
            recombinant bovine neurocalcin delta, whose protein sequence is
            identical to the human ortholog
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA417037.1, DA779293.1,
            BC063428.1, AP000426.3 and BM681731.1.
            
            Summary: This gene encodes a member of the neuronal calcium sensor
            (NCS) family of calcium-binding proteins. The protein contains an
            N-terminal myristoylation signal and four EF-hand calcium binding
            loops. The protein is cytosolic at resting calcium levels; however,
            elevated intracellular calcium levels induce a conformational
            change that exposes the myristoyl group, resulting in protein
            association with membranes and partial co-localization with the
            perinuclear trans-golgi network. The protein is thought to be a
            regulator of G protein-coupled receptor signal transduction.
            Several alternatively spliced variants of this gene have been
            determined, all of which encode the same protein; additional
            variants may exist but their biological validity has not been
            determined. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (6) differs in the 5' UTR compared
            to variant 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1058360.1,
                                           SRR11853561.27579.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2150585
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..193
                     /product="neurocalcin-delta"
                     /calculated_mol_wt=22114
     Region          21..175
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..193
                     /gene="NCALD"
                     /coded_by="NM_001040629.2:204..785"
                     /db_xref="CCDS:CCDS6292.1"
                     /db_xref="GeneID:83988"
                     /db_xref="HGNC:HGNC:7655"
                     /db_xref="MIM:606722"
ORIGIN      
        1 mgkqnsklrp evmqdllest dfteheiqew ykgflrdcps ghlsmeefkk iygnffpygd
       61 askfaehvfr tfdangdgti dfrefiials vtsrgkleqk lkwafsmydl dgngyiskae
      121 mleivqaiyk mvssvmkmpe destpekrte kifrqmdtnr dgklsleefi rgaksdpsiv
      181 rllqcdpssa gqf
//
LOCUS       NP_001362678             367 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform aaaa [Homo sapiens].
ACCESSION   NP_001362678
VERSION     NP_001362678.1
DBSOURCE    REFSEQ: accession NM_001375749.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 367)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 367)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 367)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 367)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 367)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.257610.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..367
                     /product="abl interactor 2 isoform aaaa"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=39970
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62484; propagated from
                     UniProtKB/Swiss-Prot (Q9NYB9.1)"
     Region          306..366
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(314,316,319,323,341..342,355,357..358)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..367
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375749.1:122..1225"
                     /note="isoform aaaa is encoded by transcript variant 84"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqs adkqraleet kayttqslas
       61 vaylintlan nvlqmldiqa sqlrrmessi nhisqvstqn mkmgglprtt pptqkppspp
      121 msgkgtlgss gssggshpss rsssrensgs gsvgvpiavp tpsppsvfpg hpvqfysmnr
      181 pasrhtppti ggslpyrrpp sitsqtslqn qmnggpfysq npvslapppp silqvtpqlp
      241 lmgfvarvqe nisdtppppp pveepvfdes pppppppedy eeeeaavvey sdpyaeedpp
      301 waprsylekv vaiydytkdk edelsfqega iiyvikkndd gwyegvmngv tglfpgnyve
      361 simhyse
//
LOCUS       NP_001288007             156 aa            linear   PRI 21-NOV-2025
DEFINITION  AP-2 complex subunit sigma isoform 4 [Homo sapiens].
ACCESSION   NP_001288007 XP_005258557
VERSION     NP_001288007.1
DBSOURCE    REFSEQ: accession NM_001301078.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Wen,Q.X., Luo,B., Xie,X.Y., Zhou,G.F., Chen,J., Song,L., Liu,Y.,
            Xie,S.Q., Chen,L., Li,K.Y., Xiang,X.J. and Chen,G.J.
  TITLE     AP2S1 regulates APP degradation through late endosome-lysosome
            fusion in cells and APP/PS1 mice
  JOURNAL   Traffic 24 (1), 20-33 (2023)
   PUBMED   36412210
  REMARK    GeneRIF: AP2S1 regulates APP degradation through late
            endosome-lysosome fusion in cells and APP/PS1 mice.
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Perez Verdaguer,M., Zhang,T., Paulo,J.A., Gygi,S., Watkins,S.C.,
            Sakurai,H. and Sorkin,A.
  TITLE     Mechanism of p38 MAPK-induced EGFR endocytosis and its crosstalk
            with ligand-induced pathways
  JOURNAL   J Cell Biol 220 (7) (2021)
   PUBMED   34032851
  REMARK    GeneRIF: Mechanism of p38 MAPK-induced EGFR endocytosis and its
            crosstalk with ligand-induced pathways.
REFERENCE   5  (residues 1 to 156)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 156)
  AUTHORS   Winterpacht,A., Endele,S., Enklaar,T., Fuhry,M. and Zabel,B.
  TITLE     Human CLAPS2 encoding AP17, a small chain of the
            clathrin-associated protein complex: cDNA cloning and chromosomal
            assignment to 19q13.2-->q13.3
  JOURNAL   Cytogenet Cell Genet 75 (2-3), 132-135 (1996)
   PUBMED   9040778
REFERENCE   7  (residues 1 to 156)
  AUTHORS   Page,L.J. and Robinson,M.S.
  TITLE     Targeting signals and subunit interactions in coated vesicle
            adaptor complexes
  JOURNAL   J Cell Biol 131 (3), 619-630 (1995)
   PUBMED   7593184
REFERENCE   8  (residues 1 to 156)
  AUTHORS   Kirchhausen,T., Davis,A.C., Frucht,S., Greco,B.O., Payne,G.S. and
            Tubb,B.
  TITLE     AP17 and AP19, the mammalian small chains of the
            clathrin-associated protein complexes show homology to Yap17p,
            their putative homolog in yeast
  JOURNAL   J Biol Chem 266 (17), 11153-11157 (1991)
   PUBMED   2040623
REFERENCE   9  (residues 1 to 156)
  AUTHORS   Garcia,J.V. and Miller,A.D.
  TITLE     Serine phosphorylation-independent downregulation of cell-surface
            CD4 by nef
  JOURNAL   Nature 350 (6318), 508-511 (1991)
   PUBMED   2014052
REFERENCE   10 (residues 1 to 156)
  AUTHORS   Kirchhausen,T., Nathanson,K.L., Matsui,W., Vaisberg,A., Chow,E.P.,
            Burne,C., Keen,J.H. and Davis,A.E.
  TITLE     Structural and functional division into two domains of the large
            (100- to 115-kDa) chains of the clathrin-associated protein complex
            AP-2
  JOURNAL   Proc Natl Acad Sci U S A 86 (8), 2612-2616 (1989)
   PUBMED   2495531
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB472500.1, BG282225.1,
            CB108423.1, BC006337.2 and AI139089.1.
            
            On Jul 29, 2014 this sequence version replaced XP_005258557.1.
            
            Summary: One of two major clathrin-associated adaptor complexes,
            AP-2, is a heterotetramer which is associated with the plasma
            membrane. This complex is composed of two large chains, a medium
            chain, and a small chain. This gene encodes the small chain of this
            complex. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (4) contains an alternate 5'
            terminal exon, initiates translation at an alternate start codon
            and uses an alternate in-frame splice site in the 5' coding region,
            compared to variant 3. It encodes isoform 4, which is shorter and
            has a distinct N-terminus, compared to isoform 3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG333638.1, SRR14038192.1965090.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..156
                     /product="AP-2 complex subunit sigma isoform 4"
                     /note="clathrin-associated/assembly/adaptor protein, small
                     2 (17kD); sigma2-adaptin; HA2 17 kDa subunit; clathrin
                     coat assembly protein AP17; clathrin coat-associated
                     protein AP17; sigma-2; adaptor protein complex AP-2
                     subunit sigma; plasma membrane adaptor AP-2 17 kDa
                     protein; clathrin assembly protein 2 sigma small chain;
                     adaptor related protein complex 2 sigma 1 subunit"
                     /calculated_mol_wt=18283
     Region          1..155
                     /region_name="AP2_sigma"
                     /note="AP-2 complex subunit sigma; cd14833"
                     /db_xref="CDD:341437"
     Site            order(1,18,20,45..49,74,88..93,95..97,99..100,103,115,
                     118..119,121..122,125..126,129,133..134,136..144,151..152,
                     155)
                     /site_type="other"
                     /note="AP-2 alpha interface [polypeptide binding]"
                     /db_xref="CDD:341437"
     Site            order(3,21,23,26..27,30..31,51,67..68)
                     /site_type="other"
                     /note="AP-2 mu interface [polypeptide binding]"
                     /db_xref="CDD:341437"
     Site            order(9..10,15,76..79,102..103,106,111..115)
                     /site_type="other"
                     /note="dileucine motif interface [polypeptide binding]"
                     /db_xref="CDD:341437"
     CDS             1..156
                     /gene="AP2S1"
                     /gene_synonym="AP17; CLAPS2; FBH3; FBHOk; HHC3"
                     /coded_by="NM_001301078.3:81..551"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS77323.1"
                     /db_xref="GeneID:1175"
                     /db_xref="HGNC:HGNC:565"
                     /db_xref="MIM:602242"
ORIGIN      
        1 mirfiliqnr agktrlakwy mqfdddekqk lieevhavvt vrdakhtnfv evlaisvads
       61 lsvlqfrnfk iiyrryagly fcicvdvndn nlayleaihn fvevlneyfh nvceldlvfn
      121 fykvytvvde mflageiret sqtkvlkqll mlqsle
//
LOCUS       NP_001364397             551 aa            linear   PRI 21-NOV-2025
DEFINITION  chloride channel CLIC-like protein 1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001364397
VERSION     NP_001364397.1
DBSOURCE    REFSEQ: accession NM_001377468.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 551)
  AUTHORS   D'Atri,I., Martin,E.R., Yang,L., Sears,E., Baple,E., Crosby,A.H.,
            Chilton,J.K. and Oguro-Ando,A.
  TITLE     Unraveling the CLCC1 interactome: Impact of the Asp25Glu variant
            and its interaction with SigmaR1 at the Mitochondrial-Associated ER
            Membrane (MAM)
  JOURNAL   Neurosci Lett 830, 137778 (2024)
   PUBMED   38621504
  REMARK    GeneRIF: Unraveling the CLCC1 interactome: Impact of the Asp25Glu
            variant and its interaction with SigmaR1 at the
            Mitochondrial-Associated ER Membrane (MAM).
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Tang,L., Tang,X., Zhao,Q., Li,Y., Bu,Y., Liu,Z., Li,J., Guo,J.,
            Shen,L., Jiang,H., Tang,B., Xu,R., Cao,W., Yuan,Y. and Wang,J.
  TITLE     Mutation and clinical analysis of the CLCC1 gene in amyotrophic
            lateral sclerosis patients from Central South China
  JOURNAL   Ann Clin Transl Neurol 11 (1), 79-88 (2024)
   PUBMED   37916886
  REMARK    GeneRIF: Mutation and clinical analysis of the CLCC1 gene in
            amyotrophic lateral sclerosis patients from Central South China.
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Guo,L., Mao,Q., He,J., Liu,X., Piao,X., Luo,L., Hao,X., Yu,H.,
            Song,Q., Xiao,B., Fan,D., Gao,Z. and Jia,Y.
  TITLE     Disruption of ER ion homeostasis maintained by an ER anion channel
            CLCC1 contributes to ALS-like pathologies
  JOURNAL   Cell Res 33 (7), 497-515 (2023)
   PUBMED   37142673
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Irvin,M.R., Shrestha,S., Chen,Y.D., Wiener,H.W., Haritunians,T.,
            Vaughan,L.K., Tiwari,H.K., Taylor,K.D., Scherzer,R., Saag,M.S.,
            Grunfeld,C., Rotter,J.I. and Arnett,D.K.
  TITLE     Genes linked to energy metabolism and immunoregulatory mechanisms
            are associated with subcutaneous adipose tissue distribution in
            HIV-infected men
  JOURNAL   Pharmacogenet Genomics 21 (12), 798-807 (2011)
   PUBMED   21897333
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Zhang,Q., Zulfiqar,F., Xiao,X., Riazuddin,S.A., Ayyagari,R.,
            Sabar,F., Caruso,R., Sieving,P.A., Riazuddin,S. and Hejtmancik,J.F.
  TITLE     Severe autosomal recessive retinitis pigmentosa maps to chromosome
            1p13.3-p21.2 between D1S2896 and D1S457 but outside ABCA4
  JOURNAL   Hum Genet 118 (3-4), 356-365 (2005)
   PUBMED   16189710
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Li,X. and Weinman,S.A.
  TITLE     Chloride channels and hepatocellular function: prospects for
            molecular identification
  JOURNAL   Annu Rev Physiol 64, 609-633 (2002)
   PUBMED   11826282
  REMARK    Review article
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Nagasawa,M., Kanzaki,M., Iino,Y., Morishita,Y. and Kojima,I.
  TITLE     Identification of a novel chloride channel expressed in the
            endoplasmic reticulum, golgi apparatus, and nucleus
  JOURNAL   J Biol Chem 276 (23), 20413-20418 (2001)
   PUBMED   11279057
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL449266.17.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.194845.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..551
                     /product="chloride channel CLIC-like protein 1 isoform 1
                     precursor"
                     /note="chloride channel CLIC-like protein 1; Mid-1-related
                     chloride channel protein 1; retinitis pigmentosa 32
                     (autosomal recessive); ER anion channel 1"
                     /calculated_mol_wt=60112
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1928
     Region          14..551
                     /region_name="MCLC"
                     /note="Mid-1-related chloride channel (MCLC); pfam05934"
                     /db_xref="CDD:461783"
     mat_peptide     19..551
                     /product="Chloride channel CLIC-like protein 1.
                     /id=PRO_0000297682"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
                     /calculated_mol_wt=60112
     Site            25
                     /site_type="other"
                     /note="Ca(2+)-mediated inhibition of channel activity.
                     /evidence=ECO:0000269|PubMed:37142673; propagated from
                     UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            181
                     /site_type="other"
                     /note="Ca(2+)-mediated inhibition of channel activity.
                     /evidence=ECO:0000269|PubMed:37142673; propagated from
                     UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            217..237
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            330..350
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Region          363..415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Region          447..551
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     CDS             1..551
                     /gene="CLCC1"
                     /gene_synonym="ERAC1; MCLC; RP32"
                     /coded_by="NM_001377468.1:281..1936"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 15"
                     /db_xref="CCDS:CCDS41362.1"
                     /db_xref="GeneID:23155"
                     /db_xref="HGNC:HGNC:29675"
                     /db_xref="MIM:617539"
ORIGIN      
        1 mlcslllcec lllvagyahd ddwidptdml nydaasgtmr ksqakygisg ekdvspdlsc
       61 adeisecyhk ldsltykide cekkkredye sqsnpvfrry lnkilieagk lglpdenkgd
      121 mhydaeiilk retlleiqkf lngedwkpga lddalsdili nfkfhdfetw kwrfedsfgv
      181 dpynvlmvll cllcivvlva telwtyvrwy tqlrrvliis flfslgwnwm ylyklafaqh
      241 qaevakmepl nnvcakkmdw tgsiwewfrs swtykddpcq kyyelllvnp iwlvpptkal
      301 avtfttfvte plkhigkgtg efikalmkei pallhlpvli imalailsfc ygagksvhvl
      361 rhiggpesep pqalrprdrr rqeeidyrpd ggagdadfhy rgqmgpteqg pyaktyegrr
      421 eilrerdvdl rfqtgnkspe vlrafdvpda earehptvvp shkspvldtk pketggilge
      481 gtpkesstes sqsakpvsgq dtsgntegsp aaekaqlkse aagspdqgst yspargvagp
      541 rgqdpvsspc g
//
LOCUS       NP_001340195             324 aa            linear   PRI 21-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 1 [Homo sapiens].
ACCESSION   NP_001340195
VERSION     NP_001340195.1
DBSOURCE    REFSEQ: accession NM_001353266.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.78117.1,
                                           SRR1803616.236354.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 1"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=36617
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353266.2:215..1189"
                     /note="isoform 1 is encoded by transcript variant 28"
                     /db_xref="CCDS:CCDS6361.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mgnllkvltc tdleqgpnff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqik smlq
//
LOCUS       NP_001371779            1086 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 61 [Homo sapiens].
ACCESSION   NP_001371779
VERSION     NP_001371779.1
DBSOURCE    REFSEQ: accession NM_001384850.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1086)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1086)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1086)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1086)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1086)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1086)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1086)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1123969.1,
                                           SRR14038192.1877965.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1086
                     /product="microtubule-associated protein 4 isoform 61"
                     /note="MAP-4"
                     /calculated_mol_wt=114093
     Region          <534..852
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <865..886
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          926..955
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          957..986
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          988..1018
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1086
                     /gene="MAP4"
                     /coded_by="NM_001384850.1:96..3356"
                     /note="isoform 61 is encoded by transcript variant 102"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgsp tefleekmay qeypnsqnwp
      121 edtnfcfqpe qvvdpiqtdp fkmyhdddla dlvfpssata dtsifagqnd plkdsyvple
      181 lakeiemase erppaqalei mmglkttdma psketemala kdmalatkte valakdmesp
      241 tkldvtlakd mqpsmesdma lvkdmelpte kevalvkdvr wptetdvssa knvvlptete
      301 vapakdvtll keteraspik mdlapskdmg ppkenkkete raspikmdla pskdmgppke
      361 nkivpakdlv llseievaqa ndiissteis saekvalsse tevalardmt lppetnvilt
      421 kdkalpleae vapvkdmaql peteiapakd vapstvkevg llkdmsplse temalgkdvt
      481 pppetevvli knvclppeme valtedqvpa lkteaplakd gvltlannvt pakdvpplse
      541 teatpvpikd meiaqtqkgi sedshleslq dvgqsaaptf mispetvtgt gkkcslpaee
      601 dsvleklger kpcnsqpsel ssetsgiarp eegrpvvsgt gndittppnk elppspekkt
      661 kpapttiggl nkkpmslasg lvpaappkrp avasarpsil pskdvkpkpi adakapekra
      721 spskpasapa srsgskstqt vaktttaaav astgpssrsp stllpkkpta iktegkpaev
      781 kkmtaksvpa dlsrpkstst ssmkktttls gtapaagvvp srvkatpmps rpsttpfidk
      841 kptsakpsst tprlsrlatn tsapdlknvr skvgstenik hqpgggrakv ekkteaaatt
      901 rkpesnavtk tagpiasaqk qpagkvqivs kkvsyshiqs kcgskdnikh vpgggnvqiq
      961 nkkvdiskvs skcgskanik hkpgggdvki esqklnfkek aqakvgsldn vghlpaggav
     1021 ktegggseap lcpgppagee paiseaapea gaptsasgln ghptlsgggd qreaqtldsq
     1081 iqetsi
//
LOCUS       NP_001363291             810 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger CCCH domain-containing protein 11A isoform 1 [Homo
            sapiens].
ACCESSION   NP_001363291
VERSION     NP_001363291.1
DBSOURCE    REFSEQ: accession NM_001376362.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Kases,K., Schubert,E., Hajikhezri,Z., Larsson,M., Devi,P.,
            Darweesh,M., Andersson,L., Akusjarvi,G., Punga,T. and Younis,S.
  TITLE     The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts
  JOURNAL   J Biol Chem 299 (8), 104959 (2023)
   PUBMED   37356722
  REMARK    GeneRIF: The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts.
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 810)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 810)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114402.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.119560.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..810
                     /product="zinc finger CCCH domain-containing protein 11A
                     isoform 1"
                     /note="zinc finger CCCH-type domain containing 11A; zinc
                     finger CCCH domain-containing protein 11A"
                     /calculated_mol_wt=89000
     Region          1..110
                     /region_name="zf-CCCH_3"
                     /note="Zinc-finger containing family; pfam15663"
                     /db_xref="CDD:464787"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          139..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          223..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          285..351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          367..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          482..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          715..768
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     CDS             1..810
                     /gene="ZC3H11A"
                     /gene_synonym="ZC3HDC11A"
                     /coded_by="NM_001376362.1:617..3049"
                     /note="isoform 1 is encoded by transcript variant 38"
                     /db_xref="CCDS:CCDS30978.1"
                     /db_xref="GeneID:9877"
                     /db_xref="HGNC:HGNC:29093"
                     /db_xref="MIM:613513"
ORIGIN      
        1 mpnqgedcyf ffystctkgd scpfrhceaa ignetvctlw qegrcfrqvc rfrhmeidkk
       61 rseipcywen qptgcqklnc afhhnrgryv dglflppskt vlptvpespe eevkasqlsv
      121 qqnklsvqsn pspqlrsvmk vessenvpsp thppvvinaa dddeddddqf seegdetktp
      181 tlqptpevhn glrvtsvrkp avnikqgecl nfgiktleei kskkmkeksk kqgegssgvs
      241 slllhpepvp gpekenvrtv vrtvtlstkq geeplvrlsl terlgkrkfs aggdsdpplk
      301 rslaqrlgkk veapetnidk tpkkaqvsks lkerlgmsad pdnedatdkv nkvgeihvkt
      361 leeilleras qkrgelqtkl ktegpsktdd stsgarssst iriktfsevl aekkhrqqea
      421 erqkskkdtt ciklkidsei kktvvlppiv asrgqseepa gktksmqevh iktleeikle
      481 kalrvqqsse sstsspsqhe atpgarrllr itkrtgmkee knlqegnevd sqssirteak
      541 easgettgvd itkiqvkrce tmrekhmqkq qereksvltp lrgdvascnt qvaekpvlta
      601 vpgitrhltk rlptkssqkv evetsgigds llnvkcaaqt lekrgkakpk vnvkpsvvkv
      661 vsspklapkr kavemhaavi aavkplssss vlqeppakka avavvplvse dksvtvpeae
      721 nprdslvlpp tqsssdsspp evsgpsssqm smktrrlssa stgkpplsve ddfekliwei
      781 sggkleaeid ldpgkdeddl llelsemids
//
LOCUS       NP_003759                130 aa            linear   PRI 21-NOV-2025
DEFINITION  astrocytic phosphoprotein PEA-15 isoform b [Homo sapiens].
ACCESSION   NP_003759 NP_037419
VERSION     NP_003759.1
DBSOURCE    REFSEQ: accession NM_003768.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Li,L., Wang,N., Xiong,Y., Guo,G., Zhu,M. and Gu,Y.
  TITLE     Transcription Factor FOSL1 Enhances Drug Resistance of Breast
            Cancer through DUSP7-Mediated Dephosphorylation of PEA15
  JOURNAL   Mol Cancer Res 20 (4), 515-526 (2022)
   PUBMED   34907034
  REMARK    GeneRIF: Transcription Factor FOSL1 Enhances Drug Resistance of
            Breast Cancer through DUSP7-Mediated Dephosphorylation of PEA15.
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Ikedife,J., He,J. and Wei,Y.
  TITLE     PEA-15 engages in allosteric interactions using a common scaffold
            in a phosphorylation-dependent manner
  JOURNAL   Sci Rep 12 (1), 116 (2022)
   PUBMED   34997083
  REMARK    GeneRIF: PEA-15 engages in allosteric interactions using a common
            scaffold in a phosphorylation-dependent manner.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Fiory,F., Formisano,P., Perruolo,G. and Beguinot,F.
  TITLE     Frontiers: PED/PEA-15, a multifunctional protein controlling cell
            survival and glucose metabolism
  JOURNAL   Am J Physiol Endocrinol Metab 297 (3), E592-E601 (2009)
   PUBMED   19531639
  REMARK    GeneRIF: Strategies are being devised to target key signaling
            events in PED/PEA-15 action aimed at improving glucose tolerance
            and at facilitating cancer cell death.
            Review article
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Wolford,J.K., Bogardus,C., Ossowski,V. and Prochazka,M.
  TITLE     Molecular characterization of the human PEA15 gene on 1q21-q22 and
            association with type 2 diabetes mellitus in Pima Indians
  JOURNAL   Gene 241 (1), 143-148 (2000)
   PUBMED   10607908
REFERENCE   6  (residues 1 to 130)
  AUTHORS   Condorelli,G., Vigliotta,G., Iavarone,C., Caruso,M.,
            Tocchetti,C.G., Andreozzi,F., Cafieri,A., Tecce,M.F., Formisano,P.,
            Beguinot,L. and Beguinot,F.
  TITLE     PED/PEA-15 gene controls glucose transport and is overexpressed in
            type 2 diabetes mellitus
  JOURNAL   EMBO J 17 (14), 3858-3866 (1998)
   PUBMED   9670003
REFERENCE   7  (residues 1 to 130)
  AUTHORS   Hwang,S., Kuo,W.L., Cochran,J.F., Guzman,R.C., Tsukamoto,T.,
            Bandyopadhyay,G., Myambo,K. and Collins,C.C.
  TITLE     Assignment of HMAT1, the human homolog of the murine mammary
            transforming gene (MAT1) associated with tumorigenesis, to 1q21.1,
            a region frequently gained in human breast cancers
  JOURNAL   Genomics 42 (3), 540-542 (1997)
   PUBMED   9205133
REFERENCE   8  (residues 1 to 130)
  AUTHORS   Estelles,A., Yokoyama,M., Nothias,F., Vincent,J.D., Glowinski,J.,
            Vernier,P. and Chneiweiss,H.
  TITLE     The major astrocytic phosphoprotein PEA-15 is encoded by two mRNAs
            conserved on their full length in mouse and human
  JOURNAL   J Biol Chem 271 (25), 14800-14806 (1996)
   PUBMED   8662970
REFERENCE   9  (residues 1 to 130)
  AUTHORS   Danziger,N., Yokoyama,M., Jay,T., Cordier,J., Glowinski,J. and
            Chneiweiss,H.
  TITLE     Cellular expression, developmental regulation, and phylogenic
            conservation of PEA-15, the astrocytic major phosphoprotein and
            protein kinase C substrate
  JOURNAL   J Neurochem 64 (3), 1016-1025 (1995)
   PUBMED   7861130
REFERENCE   10 (residues 1 to 130)
  AUTHORS   Araujo,H., Danziger,N., Cordier,J., Glowinski,J. and Chneiweiss,H.
  TITLE     Characterization of PEA-15, a major substrate for protein kinase C
            in astrocytes
  JOURNAL   J Biol Chem 268 (8), 5911-5920 (1993)
   PUBMED   8449955
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA131259.1, BC002426.2,
            BC022554.1 and BC010469.1.
            
            On Nov 4, 2002 this sequence version replaced NP_037419.1.
            
            Summary: This gene encodes a death effector domain-containing
            protein that functions as a negative regulator of apoptosis. The
            encoded protein is an endogenous substrate for protein kinase C.
            This protein is also overexpressed in type 2 diabetes mellitus,
            where it may contribute to insulin resistance in glucose uptake.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (2) lacks two alternate exons in
            the 5' region and initiates translation at a downstream in-frame
            start codon, compared to variant 1. The encoded isoform (b) has a
            shorter N-terminus than isoform a. Variants 2 and 3 encode the same
            isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC022554.1, Y13736.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360472.9/ ENSP00000353660.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.2"
     Protein         1..130
                     /product="astrocytic phosphoprotein PEA-15 isoform b"
                     /note="homolog of mouse MAT-1 oncogene; astrocytic
                     phosphoprotein PEA-15; phosphoprotein enriched in
                     diabetes; 15 kDa phosphoprotein enriched in astrocytes;
                     mammary transforming gene 1, mouse, homolog of;
                     phosphoprotein enriched in astrocytes 15; proliferation
                     and apoptosis adaptor 15"
                     /calculated_mol_wt=14909
     Region          2..85
                     /region_name="DED_PEA15"
                     /note="Death Effector Domain of Astrocyte phosphoprotein
                     PEA-15; cd08338"
                     /db_xref="CDD:260045"
     Site            order(14,19,68..69,71..74,76..77,80)
                     /site_type="other"
                     /note="ERK2 interaction site [polypeptide binding]"
                     /db_xref="CDD:260045"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15121.2)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62048; propagated from
                     UniProtKB/Swiss-Prot (Q15121.2)"
     Region          98..107
                     /region_name="Microtubule-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15121.2)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15121.2)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15121.2)"
     Region          122..129
                     /region_name="Microtubule-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15121.2)"
     CDS             1..130
                     /gene="PEA15"
                     /gene_synonym="HMAT1; HUMMAT1H; MAT1; MAT1H; PEA-15; PED;
                     PED-PEA15; PED/PEA15"
                     /coded_by="NM_003768.5:142..534"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1199.1"
                     /db_xref="GeneID:8682"
                     /db_xref="HGNC:HGNC:8822"
                     /db_xref="MIM:603434"
ORIGIN      
        1 maeygtllqd ltnnitledl eqlksacked ipsekseeit tgsawfsfle shnkldkdnl
       61 syiehifeis rrpdlltmvv dyrtrvlkis eedeldtklt ripsakkykd iirqpseeei
      121 iklapppkka
//
LOCUS       NP_000206               1124 aa            linear   PRI 21-NOV-2025
DEFINITION  tyrosine-protein kinase JAK3 [Homo sapiens].
ACCESSION   NP_000206
VERSION     NP_000206.2
DBSOURCE    REFSEQ: accession NM_000215.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1124)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1124)
  AUTHORS   Tsilifis,C., Spegarova,J.S., Good,R., Griffin,H., Engelhardt,K.R.,
            Graham,S., Hughes,S., Arkwright,P.D., Hambleton,S. and Gennery,A.R.
  TITLE     Omenn Syndrome in Two Infants with Different Hypomorphic Variants
            in Janus Kinase 3
  JOURNAL   J Clin Immunol 44 (4), 98 (2024)
   PUBMED   38598033
  REMARK    GeneRIF: Omenn Syndrome in Two Infants with Different Hypomorphic
            Variants in Janus Kinase 3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1124)
  AUTHORS   Liongue,C., Ratnayake,T., Basheer,F. and Ward,A.C.
  TITLE     Janus Kinase 3 (JAK3): A Critical Conserved Node in Immunity
            Disrupted in Immune Cell Cancer and Immunodeficiency
  JOURNAL   Int J Mol Sci 25 (5), 2977 (2024)
   PUBMED   38474223
  REMARK    GeneRIF: Janus Kinase 3 (JAK3): A Critical Conserved Node in
            Immunity Disrupted in Immune Cell Cancer and Immunodeficiency.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1124)
  AUTHORS   Le,K., Vollenweider,J., Han,J., Staudinger,N., Stenson,M.,
            Bayraktar,L., Wellik,L.E., Maurer,M.J., McPhail,E.D., Witzig,T.E.
            and Gupta,M.
  TITLE     Dependence of peripheral T-cell lymphoma on constitutively
            activated JAK3: Implication for JAK3 inhibition as a therapeutic
            approach
  JOURNAL   Hematol Oncol 42 (1), e3233 (2024)
   PUBMED   37876297
  REMARK    GeneRIF: Dependence of peripheral T-cell lymphoma on constitutively
            activated JAK3: Implication for JAK3 inhibition as a therapeutic
            approach.
REFERENCE   5  (residues 1 to 1124)
  AUTHORS   Zhao,Y., Mu,Y., Zou,Y., He,Z., Lu,T., Wang,X., Li,W. and Gao,B.
  TITLE     Conjoint research of WGCNA, single-cell transcriptome and
            structural biology reveals the potential targets of IDD development
            and treatment and JAK3 involvement
  JOURNAL   Aging (Albany NY) 15 (24), 14764-14790 (2023)
   PUBMED   38095643
  REMARK    GeneRIF: Conjoint research of WGCNA, single-cell transcriptome and
            structural biology reveals the potential targets of IDD development
            and treatment and JAK3 involvement.
REFERENCE   6  (residues 1 to 1124)
  AUTHORS   Johnston,J.A., Wang,L.M., Hanson,E.P., Sun,X.J., White,M.F.,
            Oakes,S.A., Pierce,J.H. and O'Shea,J.J.
  TITLE     Interleukins 2, 4, 7, and 15 stimulate tyrosine phosphorylation of
            insulin receptor substrates 1 and 2 in T cells. Potential role of
            JAK kinases
  JOURNAL   J Biol Chem 270 (48), 28527-28530 (1995)
   PUBMED   7499365
REFERENCE   7  (residues 1 to 1124)
  AUTHORS   Russell,S.M., Tayebi,N., Nakajima,H., Riedy,M.C., Roberts,J.L.,
            Aman,M.J., Migone,T.S., Noguchi,M., Markert,M.L., Buckley,R.H.,
            O'Shea,J.J. and Leonard,W.J.
  TITLE     Mutation of Jak3 in a patient with SCID: essential role of Jak3 in
            lymphoid development
  JOURNAL   Science 270 (5237), 797-800 (1995)
   PUBMED   7481768
REFERENCE   8  (residues 1 to 1124)
  AUTHORS   Lai,K.S., Jin,Y., Graham,D.K., Witthuhn,B.A., Ihle,J.N. and
            Liu,E.T.
  TITLE     A kinase-deficient splice variant of the human JAK3 is expressed in
            hematopoietic and epithelial cancer cells
  JOURNAL   J Biol Chem 270 (42), 25028-25036 (1995)
   PUBMED   7559633
REFERENCE   9  (residues 1 to 1124)
  AUTHORS   Rolling,C., Treton,D., Beckmann,P., Galanaud,P. and Richard,Y.
  TITLE     JAK3 associates with the human interleukin 4 receptor and is
            tyrosine phosphorylated following receptor triggering
  JOURNAL   Oncogene 10 (9), 1757-1761 (1995)
   PUBMED   7538655
REFERENCE   10 (residues 1 to 1124)
  AUTHORS   Musso,T., Johnston,J.A., Linnekin,D., Varesio,L., Rowe,T.K.,
            O'Shea,J.J. and McVicar,D.W.
  TITLE     Regulation of JAK3 expression in human monocytes: phosphorylation
            in response to interleukins 2, 4, and 7
  JOURNAL   J Exp Med 181 (4), 1425-1431 (1995)
   PUBMED   7535338
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA405504.1, U31601.1, U09607.1,
            AC007201.1 and BF512748.1.
            
            On May 13, 2004 this sequence version replaced NP_000206.1.
            
            Summary: The protein encoded by this gene is a member of the Janus
            kinase (JAK) family of tyrosine kinases involved in cytokine
            receptor-mediated intracellular signal transduction. It is
            predominantly expressed in immune cells and transduces a signal in
            response to its activation via tyrosine phosphorylation by
            interleukin receptors. Mutations in this gene are associated with
            autosomal SCID (severe combined immunodeficiency disease).
            [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3434126.1,
                                           SRR14038194.3063212.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000458235.7/ ENSP00000391676.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..1124
                     /product="tyrosine-protein kinase JAK3"
                     /EC_number="2.7.10.2"
                     /note="Janus kinase 3 (a protein tyrosine kinase,
                     leukocyte); leukocyte Janus kinase"
                     /calculated_mol_wt=124968
     Region          1..223
                     /region_name="Interaction with cytokine/interferon/growth
                     hormone receptors. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P52333.2)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62137; propagated from
                     UniProtKB/Swiss-Prot (P52333.2)"
     Region          26..112
                     /region_name="FERM_F1"
                     /note="FERM F1 ubiquitin-like domain; pfam18379"
                     /db_xref="CDD:465733"
     Region          126..245
                     /region_name="FERM_B-lobe"
                     /note="FERM domain B-lobe; cl46853"
                     /db_xref="CDD:481193"
     Region          250..362
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          362..458
                     /region_name="SH2_Jak3"
                     /note="Src homology 2 (SH2) domain in the Janus kinase 3
                     (Jak3) proteins; cd10380"
                     /db_xref="CDD:198243"
     Site            order(382,402,427,429)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198243"
     Site            order(428,457)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198243"
     Region          521..778
                     /region_name="PTK_Jak3_rpt1"
                     /note="Pseudokinase (repeat 1) domain of the Protein
                     Tyrosine Kinase, Janus kinase 3; cd14208"
                     /db_xref="CDD:271110"
     Site            592
                     /site_type="other"
                     /note="V617F mutation site"
                     /db_xref="CDD:271110"
     Site            785
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15121872; propagated from
                     UniProtKB/Swiss-Prot (P52333.2)"
     Region          817..1099
                     /region_name="PTKc_Jak3_rpt2"
                     /note="Catalytic (repeat 2) domain of the Protein Tyrosine
                     Kinase, Janus kinase 3; cd05081"
                     /db_xref="CDD:270665"
     Site            order(828..829,836,853,855,884,902..905,909,911,949,
                     953..954,956,966..967,986..990,999,1047)
                     /site_type="active"
                     /db_xref="CDD:270665"
     Site            order(828..829,836,853,855,884,902..905,909,911,953..954,
                     956,966..967)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270665"
     Site            904
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:18250158; propagated from
                     UniProtKB/Swiss-Prot (P52333.2)"
     Site            939
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:18250158; propagated from
                     UniProtKB/Swiss-Prot (P52333.2)"
     Site            order(949,953,986..990,999,1047)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270665"
     Site            966..992
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270665"
     Site            980
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15831699; propagated from
                     UniProtKB/Swiss-Prot (P52333.2)"
     Site            981
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15831699; propagated from
                     UniProtKB/Swiss-Prot (P52333.2)"
     CDS             1..1124
                     /gene="JAK3"
                     /gene_synonym="JAK-3; JAK3_HUMAN; JAKL; L-JAK; LJAK"
                     /coded_by="NM_000215.4:51..3425"
                     /db_xref="CCDS:CCDS12366.1"
                     /db_xref="GeneID:3718"
                     /db_xref="HGNC:HGNC:6193"
                     /db_xref="MIM:600173"
ORIGIN      
        1 mappseetpl ipqrscslls teagalhvll pargpgppqr lsfsfgdhla edlcvqaaka
       61 sgilpvyhsl falatedlsc wfppshifsv edastqvlly rirfyfpnwf glekchrfgl
      121 rkdlasaild lpvlehlfaq hrsdlvsgrl pvglslkeqg eclslavldl armareqaqr
      181 pgellktvsy kaclppslrd liqglsfvtr rrirrtvrra lrrvaacqad rhslmakyim
      241 dlerldpaga aetfhvglpg algghdglgl lrvagdggia wtqgeqevlq pfcdfpeivd
      301 isikqaprvg pagehrlvtv trtdnqilea efpglpeals fvalvdgyfr lttdsqhffc
      361 kevapprlle evaeqchgpi tldfainklk tggsrpgsyv lrrspqdfds flltvcvqnp
      421 lgpdykgcli rrsptgtfll vglsrphssl rellatcwdg glhvdgvavt ltscciprpk
      481 eksnlivvqr ghspptsslv qpqsqyqlsq mtfhkipads lewhenlghg sftkiyrgcr
      541 hevvdgeark tevllkvmda khkncmesfl eaaslmsqvs yrhlvllhgv cmagdstmvq
      601 efvhlgaidm ylrkrghlvp aswklqvvkq layalnyled kglphgnvsa rkvllarega
      661 dgsppfikls dpgvspavls lemltdripw vapeclreaq tlsleadkwg fgatvwevfs
      721 gvtmpisald pakklqfyed rqqlpapkwt elalliqqcm ayepvqrpsf ravirdlnsl
      781 issdyellsd ptpgalaprd glwngaqlya cqdptifeer hlkyisqlgk gnfgsvelcr
      841 ydplgdntga lvavkqlqhs gpdqqrdfqr eiqilkalhs dfivkyrgvs ygpgrqslrl
      901 vmeylpsgcl rdflqrhrar ldasrlllys sqickgmeyl gsrrcvhrdl aarnilvese
      961 ahvkiadfgl akllpldkdy yvvrepgqsp ifwyapesls dnifsrqsdv wsfgvvlyel
     1021 ftycdkscsp saeflrmmgc erdvpalcrl lelleegqrl pappacpaev helmklcwap
     1081 spqdrpsfsa lgpqldmlws gsrgcethaf tahpegkhhs lsfs
//
LOCUS       NP_001263180             208 aa            linear   PRI 21-NOV-2025
DEFINITION  low-density lipoprotein receptor class A domain-containing protein
            4 isoform epsilon 1 [Homo sapiens].
ACCESSION   NP_001263180
VERSION     NP_001263180.1
DBSOURCE    REFSEQ: accession NM_001276251.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Xie,W., Xiao,H., Luo,J., Zhao,L., Jin,F., Ma,J., Li,J., Xiong,K.,
            Chen,C. and Wang,G.
  TITLE     Identification of low-density lipoprotein receptor class A domain
            containing 4 (LDLRAD4) as a prognostic indicator in primary
            gastrointestinal stromal tumors
  JOURNAL   Curr Probl Cancer 44 (6), 100593 (2020)
   PUBMED   32507364
  REMARK    GeneRIF: Identification of low-density lipoprotein receptor class A
            domain containing 4 (LDLRAD4) as a prognostic indicator in primary
            gastrointestinal stromal tumors.
REFERENCE   5  (residues 1 to 208)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 208)
  AUTHORS   Meerabux,J.M., Ohba,H., Iwayama,Y., Maekawa,M.,
            Detera-Wadleigh,S.D., DeLisi,L.E. and Yoshikawa,T.
  TITLE     Analysis of a t(18;21)(p11.1;p11.1) translocation in a family with
            schizophrenia
  JOURNAL   J Hum Genet 54 (7), 386-391 (2009)
   PUBMED   19461657
REFERENCE   7  (residues 1 to 208)
  AUTHORS   Kikuchi,M., Yamada,K., Toyota,T. and Yoshikawa,T.
  TITLE     C18orf1 located on chromosome 18p11.2 may confer susceptibility to
            schizophrenia
  JOURNAL   J Med Dent Sci 50 (3), 225-229 (2003)
   PUBMED   15074360
REFERENCE   8  (residues 1 to 208)
  AUTHORS   Yoshikawa,T., Sanders,A.R., Esterling,L.E. and Detera-Wadleigh,S.D.
  TITLE     Multiple transcriptional variants and RNA editing in C18orf1, a
            novel gene with LDLRA and transmembrane domains on 18p11.2
  JOURNAL   Genomics 47 (2), 246-257 (1998)
   PUBMED   9479497
REFERENCE   9  (residues 1 to 208)
  AUTHORS   Esterling,L.E., Cox Matise,T., Sanders,A.R., Yoshikawa,T.,
            Overhauser,J., Gershon,E.S., Moskowitz,M.T. and
            Detera-Wadleigh,S.D.
  TITLE     An integrated physical map of 18p11.2: a susceptibility region for
            bipolar disorder
  JOURNAL   Mol Psychiatry 2 (6), 501-504 (1997)
   PUBMED   9399696
REFERENCE   10 (residues 1 to 208)
  AUTHORS   Yoshikawa,T., Sanders,A.R., Esterling,L.E., Overhauser,J.,
            Garnes,J.A., Lennon,G., Grewal,R. and Detera-Wadleigh,S.D.
  TITLE     Isolation of chromosome 18-specific brain transcripts as positional
            candidates for bipolar disorder
  JOURNAL   Am J Med Genet 74 (2), 140-149 (1997)
   PUBMED   9129712
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC029958.1, AP001010.4, AI878844.1, N63974.1, HY309264.1,
            BC066971.1 and AF009424.1.
            
            Transcript Variant: This variant (6) contains an alternate 5'
            terminal exon, differs in its 5' UTR, lacks a portion of the 5'
            coding region, and initiates translation at an alternate start
            codon, compared to variant a1. The encoded isoform (epsilon 1) is
            shorter and has a distinct N-terminus, compared to isoform alpha 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC029958.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158188 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.21"
     Protein         1..208
                     /product="low-density lipoprotein receptor class A
                     domain-containing protein 4 isoform epsilon 1"
                     /note="clone 22; low-density lipoprotein receptor class A
                     domain-containing protein 4"
                     /calculated_mol_wt=22922
     CDS             1..208
                     /gene="LDLRAD4"
                     /gene_synonym="C18orf1"
                     /coded_by="NM_001276251.2:959..1585"
                     /note="isoform epsilon 1 is encoded by transcript variant
                     6"
                     /db_xref="GeneID:753"
                     /db_xref="HGNC:HGNC:1224"
                     /db_xref="MIM:606571"
ORIGIN      
        1 mrldshleci sstqegclwp sdsaaprlga seimhaprsr drftapsfiq rdrfsrfqpt
       61 ypyvqheidl pptislsdge epppyqgpct lqlrdpeqqm elnresvrap pnrtifdsdl
      121 idiamysggp cppssnsgis astcssngrm egppptysev mghhpgasfl hhqrsnahrg
      181 srlqfqqnna estivpikgk drkpgnlv
//
LOCUS       NP_001369555             969 aa            linear   PRI 21-NOV-2025
DEFINITION  nuclear factor NF-kappa-B p105 subunit isoform 1 [Homo sapiens].
ACCESSION   NP_001369555
VERSION     NP_001369555.1
DBSOURCE    REFSEQ: accession NM_001382626.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 969)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 969)
  AUTHORS   Vazquez-Coto,D., Perez-Oliveira,S., Menendez-Gonzalez,M., Coto,E.
            and Alvarez,V.
  TITLE     Assessing the association between common functional Nuclear Factor
            Kappa-b gene polymorphisms (NFKB1, NFKBIZ, NFKBIA) and Alzheimer s
            disease
  JOURNAL   Behav Brain Res 476, 115264 (2025)
   PUBMED   39322062
  REMARK    GeneRIF: Assessing the association between common functional
            Nuclear Factor Kappa-b gene polymorphisms (NFKB1, NFKBIZ, NFKBIA)
            and Alzheimer s disease.
REFERENCE   3  (residues 1 to 969)
  AUTHORS   Al-Salihy,S.R., Al-Shawk,R.S., Al-Waysi,S.A. and Rasheed,M.N.
  TITLE     Association of nuclear factor-kappa B1 (NF-kappaB1) Ins/Del gene
            polymorphism with Hepatitis C virus outcomes
  JOURNAL   J Pak Med Assoc 74 (10 (Supple-8)), S34-S38 (2024)
   PUBMED   39434268
  REMARK    GeneRIF: Association of nuclear factor-kappa B1 (NF-kappaB1)
            Ins/Del gene polymorphism with Hepatitis C virus outcomes.
REFERENCE   4  (residues 1 to 969)
  AUTHORS   Eluard,B., Thieblemont,C. and Baud,V.
  TITLE     NF-kappaB in the New Era of Cancer Therapy
  JOURNAL   Trends Cancer 6 (8), 677-687 (2020)
   PUBMED   32409139
  REMARK    Review article
REFERENCE   5  (residues 1 to 969)
  AUTHORS   Lin,L. and Ghosh,S.
  TITLE     A glycine-rich region in NF-kappaB p105 functions as a processing
            signal for the generation of the p50 subunit
  JOURNAL   Mol Cell Biol 16 (5), 2248-2254 (1996)
   PUBMED   8628291
REFERENCE   6  (residues 1 to 969)
  AUTHORS   Muller,C.W., Rey,F.A., Sodeoka,M., Verdine,G.L. and Harrison,S.C.
  TITLE     Structure of the NF-kappa B p50 homodimer bound to DNA
  JOURNAL   Nature 373 (6512), 311-317 (1995)
   PUBMED   7830764
REFERENCE   7  (residues 1 to 969)
  AUTHORS   Rice,N.R., MacKichan,M.L. and Israel,A.
  TITLE     The precursor of NF-kappa B p50 has I kappa B-like functions
  JOURNAL   Cell 71 (2), 243-253 (1992)
   PUBMED   1423592
REFERENCE   8  (residues 1 to 969)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
REFERENCE   9  (residues 1 to 969)
  AUTHORS   Urban,M.B., Schreck,R. and Baeuerle,P.A.
  TITLE     NF-kappa B contacts DNA by a heterodimer of the p50 and p65 subunit
  JOURNAL   EMBO J 10 (7), 1817-1825 (1991)
   PUBMED   2050119
REFERENCE   10 (residues 1 to 969)
  AUTHORS   Bours,V., Villalobos,J., Burd,P.R., Kelly,K. and Siebenlist,U.
  TITLE     Cloning of a mitogen-inducible gene encoding a kappa B DNA-binding
            protein with homology to the rel oncogene and to cell-cycle motifs
  JOURNAL   Nature 348 (6296), 76-80 (1990)
   PUBMED   2234062
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF213884.2.
            
            Summary: This gene encodes a 105 kD protein which can undergo
            cotranslational processing by the 26S proteasome to produce a 50 kD
            protein. The 105 kD protein is a Rel protein-specific transcription
            inhibitor and the 50 kD protein is a DNA binding subunit of the
            NF-kappa-B (NFKB) protein complex. NFKB is a transcription
            regulator that is activated by various intra- and extra-cellular
            stimuli such as cytokines, oxidant-free radicals, ultraviolet
            irradiation, and bacterial or viral products. Activated NFKB
            translocates into the nucleus and stimulates the expression of
            genes involved in a wide variety of biological functions.
            Inappropriate activation of NFKB has been associated with a number
            of inflammatory diseases while persistent inhibition of NFKB leads
            to inappropriate immune cell development or delayed cell growth.
            NFKB is a critical regulator of the immediate-early response to
            viral infection. Alternative splicing results in multiple
            transcript variants encoding different isoforms, at least one of
            which is proteolytically processed. [provided by RefSeq, Aug 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1395601.1,
                                           SRR14038196.2117568.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            coronavirus related              :: involved in immune response or
                                                antiviral activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..969
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..969
                     /product="nuclear factor NF-kappa-B p105 subunit isoform
                     1"
                     /note="nuclear factor kappa-B DNA binding subunit; nuclear
                     factor NF-kappa-B p50 subunit; nuclear factor NF-kappa-B
                     p105 subunit; DNA-binding factor KBF1; nuclear factor of
                     kappa light polypeptide gene enhancer in B-cells 1"
                     /calculated_mol_wt=105296
     Region          43..244
                     /region_name="RHD-n_NFkB1"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor of kappa B1 (NF-kappa B1);
                     cd07935"
                     /db_xref="CDD:143651"
     Site            order(57,59..60,62..63,66..69,144,146..147,244)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143651"
     Region          251..352
                     /region_name="IPT_NFkappaB"
                     /note="IPT domain of the transcription factor NFkappaB and
                     related transcription factors. NFkappaB is considered a
                     central regulator of stress responses, activated by
                     different stressful conditions, including physical stress,
                     oxidative stress, and exposure to...; cd01177"
                     /db_xref="CDD:238582"
     Site            order(252,254..256,258..260,300..302,315,327,346,349,351)
                     /site_type="other"
                     /note="ankyrin protein binding site [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(254..255,257,270,272,274,307..308,311,313)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(275,277,308..309)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238582"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Region          361..366
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Region          373..395
                     /region_name="GRR. /evidence=ECO:0000269|PubMed:8628291"
                     /note="propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Region          426..454
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Site            432
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000305|PubMed:11739381; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            434..435
                     /site_type="cleavage"
                     /note="Cleavage (when cotranslationally processed).
                     /evidence=ECO:0000269|PubMed:9529257; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Region          436..969
                     /region_name="Interaction with CFLAR.
                     /evidence=ECO:0000269|PubMed:13679070"
                     /note="propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Site            441
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000305|PubMed:11739381; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            442
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000305|PubMed:11739381; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25799; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Region          499..759
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(543,545,549..550,553..555,557..558,562,565,580,582,
                     584,588..589,592..594,596..597,601,604,613,615,617,
                     621..622,625..627,629..630,634,637)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          543..580
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          582..613
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          651..685
                     /region_name="Essential for interaction with HIF1AN.
                     /evidence=ECO:0000269|PubMed:17003112"
                     /note="propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Region          651..681
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            679
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyasparagine, by HIF1AN, partial.
                     /evidence=ECO:0000269|PubMed:17003112; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Region          685..717
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            760
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63369; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Region          816..891
                     /region_name="Death_NFkB1_p105"
                     /note="Death domain of the Nuclear Factor-KappaB1
                     precursor protein p105; cd08797"
                     /db_xref="CDD:260063"
     Site            893
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            904
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta, in vitro.
                     /evidence=ECO:0000269|PubMed:12871932,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            908
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta, in vitro.
                     /evidence=ECO:0000269|PubMed:12871932,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            924
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11158290; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            928
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKB.
                     /evidence=ECO:0000269|PubMed:11158290,
                     ECO:0000269|PubMed:11297557, ECO:0000269|PubMed:12482991,
                     ECO:0000269|PubMed:25860612; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            933
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKB.
                     /evidence=ECO:0000269|PubMed:12482991; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            938
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            944
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P25799; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     CDS             1..969
                     /gene="NFKB1"
                     /gene_synonym="CVID12; EBP-1; KBF1; NF-kappa-B1;
                     NF-kappaB; NF-kappabeta; NF-kB; NF-kB1; NFkappaB;
                     NFKB-p105; NFKB-p50"
                     /coded_by="NM_001382626.1:508..3417"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS3657.1"
                     /db_xref="GeneID:4790"
                     /db_xref="HGNC:HGNC:7794"
                     /db_xref="MIM:164011"
ORIGIN      
        1 maeddpylgr peqmfhldps lthtifnpev fqpqmalpta dgpylqileq pkqrgfrfry
       61 vcegpshggl pgasseknkk sypqvkicny vgpakvivql vtngknihlh ahslvgkhce
      121 dgictvtagp kdmvvgfanl gilhvtkkkv fetlearmte acirgynpgl lvhpdlaylq
      181 aegggdrqlg drekelirqa alqqtkemdl svvrlmftaf lpdstgsftr rlepvvsdai
      241 ydskapnasn lkivrmdrta gcvtggeeiy llcdkvqkdd iqirfyeeee nggvwegfgd
      301 fsptdvhrqf aivfktpkyk dinitkpasv fvqlrrksdl etsepkpfly ypeikdkeev
      361 qrkrqklmpn fsdsfgggsg agaggggmfg sggggggtgs tgpgysfphy gfptyggitf
      421 hpgttksnag mkhgtmdtes kkdpegcdks ddkntvnlfg kvietteqdq epseatvgng
      481 evtltyatgt keesagvqdn lflekamqla krhanalfdy avtgdvkmll avqrhltavq
      541 dengdsvlhl aiihlhsqlv rdllevtsgl isddiinmrn dlyqtplhla vitkqedvve
      601 dllragadls lldrlgnsvl hlaakeghdk vlsillkhkk aallldhpng dglnaihlam
      661 msnslpclll lvaagadvna qeqksgrtal hlavehdnis lagclllegd ahvdsttydg
      721 ttplhiaagr gstrlaallk aagadplven feplydldds wenagedegv vpgttpldma
      781 tswqvfdiln gkpyepefts ddllaqgdmk qlaedvklql yklleipdpd knwatlaqkl
      841 glgilnnafr lspapsktlm dnyevsggtv relvealrqm gyteaieviq aasspvktts
      901 qahslplspa strqqidelr dsdsvcdsgv etsfrklsft esltsgasll tlnkmphdyg
      961 qegplegki
//
LOCUS       NP_001070957             379 aa            linear   PRI 21-NOV-2025
DEFINITION  protein GNAS isoform g [Homo sapiens].
ACCESSION   NP_001070957
VERSION     NP_001070957.1
DBSOURCE    REFSEQ: accession NM_001077489.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Lin,J., Nie,Q., Cheng,J., Zhong,Y.N., Zhang,T., Zhang,X., Ge,X.,
            Ding,Y., Niu,C., Gao,Y., Wang,K., Gao,M., Wang,X., Chen,W., Yun,C.,
            Ye,C., Xu,J., Shaoyong,W., Zhang,L., Shang,P., Luo,X., Zhang,Z.,
            Zheng,X., Sha,X., Zhang,J., Nie,S., Zhang,X., Ren,F., Liu,H.,
            Dong,E., Yu,X., Ji,L., Pang,Y., Sun,J.P. and Jiang,C.
  TITLE     A microbial amino-acid-conjugated bile acid, tryptophan-cholic
            acid, improves glucose homeostasis via the orphan receptor MRGPRE
  JOURNAL   Cell 188 (17), 4530-4548 (2025)
   PUBMED   40446798
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Crane,J.L., Shamblott,M.J., Axelman,J., Hsu,S., Levine,M.A. and
            Germain-Lee,E.L.
  TITLE     Imprinting status of Galpha(s), NESP55, and XLalphas in cell
            cultures derived from human embryonic germ cells: GNAS imprinting
            in human embryonic germ cells
  JOURNAL   Clin Transl Sci 2 (5), 355-360 (2009)
   PUBMED   20443919
  REMARK    GeneRIF: analysis of the imprinting Status of Galpha(s), NESP55,
            and XLalphas in cell cultures derived from human embryonic germ
            cells
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Bastepe,M.
  TITLE     The GNAS Locus: Quintessential Complex Gene Encoding Gsalpha,
            XLalphas, and other Imprinted Transcripts
  JOURNAL   Curr Genomics 8 (6), 398-414 (2007)
   PUBMED   19412439
  REMARK    GeneRIF: GNAS locus has a highly complex imprinted expression
            pattern, giving rise to transcripts (including non-coding) that are
            maternally, paternally, or biallelically expressed.
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Jakobsen,A.M., Ahlman,H., Kolby,L., Abrahamsson,J.,
            Fischer-Colbrie,R. and Nilsson,O.
  TITLE     NESP55, a novel chromogranin-like peptide, is expressed in
            endocrine tumours of the pancreas and adrenal medulla but not in
            ileal carcinoids
  JOURNAL   Br J Cancer 88 (11), 1746-1754 (2003)
   PUBMED   12771991
  REMARK    GeneRIF: Neuroendocrine secretory protein 55 is found in a subset
            of neuroendocrine tumours showing differentiation towards adrenal
            chromaffin cells and pancreatic islets cells and not in ileal
            carcinoids
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Freson,K., Jaeken,J., Van Helvoirt,M., de Zegher,F.,
            Wittevrongel,C., Thys,C., Hoylaerts,M.F., Vermylen,J. and Van
            Geet,C.
  TITLE     Functional polymorphisms in the paternally expressed XLalphas and
            its cofactor ALEX decrease their mutual interaction and enhance
            receptor-mediated cAMP formation
  JOURNAL   Hum Mol Genet 12 (10), 1121-1130 (2003)
   PUBMED   12719376
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Weiss,U., Ischia,R., Eder,S., Lovisetti-Scamihorn,P., Bauer,R. and
            Fischer-Colbrie,R.
  TITLE     Neuroendocrine secretory protein 55 (NESP55): alternative splicing
            onto transcripts of the GNAS gene and posttranslational processing
            of a maternally expressed protein
  JOURNAL   Neuroendocrinology 71 (3), 177-186 (2000)
   PUBMED   10729789
REFERENCE   7  (residues 1 to 379)
  AUTHORS   Ischia,R., Lovisetti-Scamihorn,P., Hogue-Angeletti,R.,
            Wolkersdorfer,M., Winkler,H. and Fischer-Colbrie,R.
  TITLE     Molecular cloning and characterization of NESP55, a novel
            chromogranin-like precursor of a peptide with 5-HT1B receptor
            antagonist activity
  JOURNAL   J Biol Chem 272 (17), 11657-11662 (1997)
   PUBMED   9111083
REFERENCE   8  (residues 1 to 379)
  AUTHORS   Haldeman-Englert,C.R., Hurst,A.C.E. and Levine,M.A.
  TITLE     Disorders of GNAS Inactivation
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29072892
REFERENCE   9  (residues 1 to 379)
  AUTHORS   Szymczuk,V., Florenzano,P., de Castro,L.F., Collins,M.T. and
            Boyce,A.M.
  TITLE     Fibrous Dysplasia / McCune-Albright Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719192
REFERENCE   10 (residues 1 to 379)
  AUTHORS   Weinstein,L.S., Gejman,P.V., de Mazancourt,P., American,N. and
            Spiegel,A.M.
  TITLE     A heterozygous 4-bp deletion mutation in the Gs alpha gene (GNAS1)
            in a patient with Albright hereditary osteodystrophy
  JOURNAL   Genomics 13 (4), 1319-1321 (1992)
   PUBMED   1505964
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC089157.1, BC066923.1,
            AF493897.1 and AF105253.1.
            
            Summary: This locus has a highly complex imprinted expression
            pattern. It gives rise to maternally, paternally, and biallelically
            expressed transcripts that are derived from four alternative
            promoters and 5' exons. Some transcripts contain a differentially
            methylated region (DMR) at their 5' exons, and this DMR is commonly
            found in imprinted genes and correlates with transcript expression.
            An antisense transcript is produced from an overlapping locus on
            the opposite strand. One of the transcripts produced from this
            locus, and the antisense transcript, are paternally expressed
            noncoding RNAs, and may regulate imprinting in this region. In
            addition, one of the transcripts contains a second overlapping ORF,
            which encodes a structurally unrelated protein - Alex. Alternative
            splicing of downstream exons is also observed, which results in
            different forms of the stimulatory G-protein alpha subunit, a key
            element of the classical signal transduction pathway linking
            receptor-ligand interactions with the activation of adenylyl
            cyclase and a variety of cellular reponses. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            Mutations in this gene result in pseudohypoparathyroidism type 1a,
            pseudohypoparathyroidism type 1b, Albright hereditary
            osteodystrophy, pseudopseudohypoparathyroidism, McCune-Albright
            syndrome, progressive osseus heteroplasia, polyostotic fibrous
            dysplasia of bone, and some pituitary tumors. [provided by RefSeq,
            Aug 2012].
            
            Transcript Variant: This variant (7) is biallelically expressed and
            lacks an alternate in-frame coding exon, compared to variant 1. It
            encodes isoform g, which lacks an internal segment, compared to
            isoform GNASL.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.532414.1, BC066923.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 19412439
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.32"
     Protein         1..379
                     /product="protein GNAS isoform g"
                     /note="secretogranin VI; G protein subunit alpha S;
                     guanine nucleotide binding protein (G protein), alpha
                     stimulating activity polypeptide 1; guanine nucleotide
                     regulatory protein; adenylate cyclase-stimulating G alpha
                     protein; protein ALEX; extra large alphas protein;
                     alternative gene product encoded by XL-exon"
                     /calculated_mol_wt=44048
     Region          41..373
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Site            order(47,52..54,189,208,211,277..278,280,350..351)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206639"
     Site            47..54
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206639"
     Site            order(48..50,78,82,86,89,92..93,113,116,157,186,211,219,
                     223)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Site            184..192
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            189
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(190,192,194,205,207,211..213,215,218..219,221..224)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(192,217,220..221,224)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            208..211
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            209..225
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Site            277..280
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(342..353,355..358)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Site            350..352
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..379
                     /gene="GNAS"
                     /gene_synonym="AHO; AIMAH1; C20orf45; GNAS1; GPSA; GSA;
                     GSP; NESP; PITA3; POH; SCG6; SgVI"
                     /coded_by="NM_001077489.4:307..1446"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS42892.1"
                     /db_xref="GeneID:2778"
                     /db_xref="HGNC:HGNC:4392"
                     /db_xref="MIM:139320"
ORIGIN      
        1 mgclgnskte dqrneekaqr eankkiekql qkdkqvyrat hrllllgage sgkstivkqm
       61 rilhvngfng dekatkvqdi knnlkeaiet ivaamsnlvp pvelanpenq frvdyilsvm
      121 nvpdfdfppe fyehakalwe degvracyer sneyqlidca qyfldkidvi kqadyvpsdq
      181 dllrcrvlts gifetkfqvd kvnfhmfdvg gqrderrkwi qcfndvtaii fvvasssynm
      241 virednqtnr lqealnlfks iwnnrwlrti svilflnkqd llaekvlagk skiedyfpef
      301 aryttpedat pepgedprvt rakyfirdef lristasgdg rhycyphftc avdtenirrv
      361 fndcrdiiqr mhlrqyell
//
LOCUS       NP_001291900             913 aa            linear   PRI 21-NOV-2025
DEFINITION  plakophilin-4 isoform e [Homo sapiens].
ACCESSION   NP_001291900
VERSION     NP_001291900.1
DBSOURCE    REFSEQ: accession NM_001304971.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 913)
  AUTHORS   Park,S.S., Ponce-Balbuena,D., Kuick,R., Guerrero-Serna,G., Yoon,J.,
            Mellacheruvu,D., Conlon,K.P., Basrur,V., Nesvizhskii,A.I.,
            Jalife,J. and Rual,J.F.
  TITLE     Kir2.1 Interactome Mapping Uncovers PKP4 as a Modulator of the
            Kir2.1-Regulated Inward Rectifier Potassium Currents
  JOURNAL   Mol Cell Proteomics 19 (9), 1436-1449 (2020)
   PUBMED   32541000
  REMARK    GeneRIF: Kir2.1 Interactome Mapping Uncovers PKP4 as a Modulator of
            the Kir2.1-Regulated Inward Rectifier Potassium Currents.
REFERENCE   5  (residues 1 to 913)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 913)
  AUTHORS   Stahl,B., Diehlmann,A. and Sudhof,T.C.
  TITLE     Direct interaction of Alzheimer's disease-related presenilin 1 with
            armadillo protein p0071
  JOURNAL   J Biol Chem 274 (14), 9141-9148 (1999)
   PUBMED   10092585
REFERENCE   7  (residues 1 to 913)
  AUTHORS   Levesque,G., Yu,G., Nishimura,M., Zhang,D.M., Levesque,L., Yu,H.,
            Xu,D., Liang,Y., Rogaeva,E., Ikeda,M., Duthie,M., Murgolo,N.,
            Wang,L., VanderVere,P., Bayne,M.L., Strader,C.D., Rommens,J.M.,
            Fraser,P.E. and St George-Hyslop,P.
  TITLE     Presenilins interact with armadillo proteins including
            neural-specific plakophilin-related protein and beta-catenin
  JOURNAL   J Neurochem 72 (3), 999-1008 (1999)
   PUBMED   10037471
REFERENCE   8  (residues 1 to 913)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   9  (residues 1 to 913)
  AUTHORS   Paffenholz,R. and Franke,W.W.
  TITLE     Identification and localization of a neurally expressed member of
            the plakoglobin/armadillo multigene family
  JOURNAL   Differentiation 61 (5), 293-304 (1997)
   PUBMED   9342840
REFERENCE   10 (residues 1 to 913)
  AUTHORS   Hatzfeld,M. and Nachtsheim,C.
  TITLE     Cloning and characterization of a new armadillo family member,
            p0071, associated with the junctional plaque: evidence for a
            subfamily of closely related proteins
  JOURNAL   J Cell Sci 109 (Pt 11), 2767-2778 (1996)
   PUBMED   8937994
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008070.4 and AC005042.2.
            
            Summary: Armadillo-like proteins are characterized by a series of
            armadillo repeats, first defined in the Drosophila 'armadillo' gene
            product, that are typically 42 to 45 amino acids in length. These
            proteins can be divided into subfamilies based on their number of
            repeats, their overall sequence similarity, and the dispersion of
            the repeats throughout their sequences. Members of the
            p120(ctn)/plakophilin subfamily of Armadillo-like proteins,
            including CTNND1, CTNND2, PKP1, PKP2, PKP4, and ARVCF. PKP4 may be
            a component of desmosomal plaque and other adhesion plaques and is
            thought to be involved in regulating junctional plaque organization
            and cadherin function. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Feb 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034473.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.1"
     Protein         1..913
                     /product="plakophilin-4 isoform e"
                     /note="catenin 4"
                     /calculated_mol_wt=100235
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          73..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Region          <232..347
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            254
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            270
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Region          290..310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Region          323..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Region          415..455
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Region          518..557
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          530..555
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(546,550,554,588,592,596,633,637,641)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          559..598
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          560..599
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          563..599
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          603..644
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          604..644
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          607..642
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          649..700
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          660..702
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          706..751
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          708..749
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          773..810
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            776
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          815..855
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          825..855
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          862..901
                     /region_name="ARM 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          865..900
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          865..899
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     CDS             1..913
                     /gene="PKP4"
                     /gene_synonym="p0071"
                     /coded_by="NM_001304971.2:273..3014"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="GeneID:8502"
                     /db_xref="HGNC:HGNC:9026"
                     /db_xref="MIM:604276"
ORIGIN      
        1 mpapeqaslv eegqpqtrqe aastgpgmep ettattilas vkeqelqfqr ltreleverq
       61 ivasqlercr lgaespsias tssteksfpw rstdvpntgv skprvsdavq pnnylirtep
      121 eqgtlyspeq tslhesegsl gnsrsstqmn sysdsgyqea gsfhnsqnvs kadnrqqhsf
      181 igstnnhvvr nsraegqtlv qpsvanramr rvssvpsraq spsyvistgv spsrgslrts
      241 lgsgfgspsv tdprplnpsa yssttlpaar aaspysqrpa sptairrigs vtsrqtsnpn
      301 gptpqyqtta rvgspltltd aqtrvaspsq gqvgssspkr sgmtavpqhl gpslqrtvhd
      361 meqfgqqqyd iyermvpprp dsltglrssy asqhsqlgqd lrsavspdlh itpiyegrty
      421 yspvyrspnh gtvelqgsqt alyrtgsvgi gnlqrtssqr stltyqrnny alnttatyae
      481 pyrpiqyrvq ecnynrlqha vpaddgttrs psidsiqkdp refawrdpel pevihmlqhq
      541 fpsvqanaaa ylqhlcfgdn kvkmevcrlg gikhlvdlld hrvlevqkna cgalrnlvfg
      601 kstdenkiam knvggipall rllrksidae vrelvtgvlw nlsscdavkm tiirdalstl
      661 tntvivphsg wnnssfdddh kikfqtslvl rnttgclrnl ssageearkq mrsceglvds
      721 llyvihtcvn tsdydsktve ncvctlrnls yrlelevpqa rllglneldd llgkespskd
      781 sepscwgkkk kkkkrtpqed qwdgvgpipg lskspkgvem lwhpsvvkpy ltllaessnp
      841 atlegsagsl qnlsagnwkf aayiraavrk ekglpilvel lrmdndrvvs svatalrnma
      901 ldvrnkelig mfw
//
LOCUS       NP_001306120             345 aa            linear   PRI 21-NOV-2025
DEFINITION  urokinase-type plasminogen activator isoform 3 [Homo sapiens].
ACCESSION   NP_001306120 XP_011538169
VERSION     NP_001306120.2
DBSOURCE    REFSEQ: accession NM_001319191.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Li,D., Ding,C., Huang,F., Chang,M., Lu,Z., Li,G., Li,Y., Gao,H. and
            Sun,F.
  TITLE     Bioinformatics Analysis of the Expression and Prognostic Value of
            PLAU Gene in Wilms' Tumor
  JOURNAL   Anticancer Res 44 (9), 3829-3842 (2024)
   PUBMED   39197889
  REMARK    GeneRIF: Bioinformatics Analysis of the Expression and Prognostic
            Value of PLAU Gene in Wilms' Tumor.
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Guo,J., Wang,H., Huang,C., Lai,C., Shang,W., Luo,S. and Chen,L.
  TITLE     PLAU, transcriptionally negatively regulated by GATA6, promotes
            lung squamous carcinoma cell proliferation and migration
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (5), 119744 (2024)
   PUBMED   38702016
  REMARK    GeneRIF: PLAU, transcriptionally negatively regulated by GATA6,
            promotes lung squamous carcinoma cell proliferation and migration.
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Cui,X., Sun,H., Liu,X., Bai,Y., Bai,Y., Cui,Y., Wang,B., Zhang,S.
            and Li,X.
  TITLE     PLAU promotes cell proliferation and migration of head and neck
            cancer via STAT3 signaling pathway
  JOURNAL   Exp Cell Res 438 (2), 114056 (2024)
   PUBMED   38663475
  REMARK    GeneRIF: PLAU promotes cell proliferation and migration of head and
            neck cancer via STAT3 signaling pathway.
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Cetinsoy,O., Anyanwu,I., Krishnanand,H., Natarajan,G.,
            Ramachandran,N., Thomas,A. and Brookes,K.J.
  TITLE     Gene Association Study of the Urokinase Plasminogen Activator and
            Its Receptor Gene in Alzheimer's Disease
  JOURNAL   J Alzheimers Dis 99 (1), 241-250 (2024)
   PUBMED   38669542
  REMARK    GeneRIF: Gene Association Study of the Urokinase Plasminogen
            Activator and Its Receptor Gene in Alzheimer's Disease.
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Mekkawy,A.H., Pourgholami,M.H. and Morris,D.L.
  TITLE     Involvement of urokinase-type plasminogen activator system in
            cancer: an overview
  JOURNAL   Med Res Rev 34 (5), 918-956 (2014)
   PUBMED   24549574
  REMARK    Review article
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Naldini,L., Tamagnone,L., Vigna,E., Sachs,M., Hartmann,G.,
            Birchmeier,W., Daikuhara,Y., Tsubouchi,H., Blasi,F. and
            Comoglio,P.M.
  TITLE     Extracellular proteolytic cleavage by urokinase is required for
            activation of hepatocyte growth factor/scatter factor
  JOURNAL   EMBO J 11 (13), 4825-4833 (1992)
   PUBMED   1334458
REFERENCE   8  (residues 1 to 345)
  AUTHORS   Li,X., Smith,R.A. and Dobson,C.M.
  TITLE     Sequential 1H NMR assignments and secondary structure of the
            kringle domain from urokinase
  JOURNAL   Biochemistry 31 (40), 9562-9571 (1992)
   PUBMED   1327118
REFERENCE   9  (residues 1 to 345)
  AUTHORS   Stephens,R.W., Aumailley,M., Timpl,R., Reisberg,T., Tapiovaara,H.,
            Myohanen,H., Murphy-Ullrich,J. and Vaheri,A.
  TITLE     Urokinase binding to laminin-nidogen. Structural requirements and
            interactions with heparin
  JOURNAL   Eur J Biochem 207 (3), 937-942 (1992)
   PUBMED   1499567
REFERENCE   10 (residues 1 to 345)
  AUTHORS   Moroi,M. and Aoki,N.
  TITLE     Isolation and characterization of alpha2-plasmin inhibitor from
            human plasma. A novel proteinase inhibitor which inhibits
            activator-induced clot lysis
  JOURNAL   J Biol Chem 251 (19), 5956-5965 (1976)
   PUBMED   134998
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK297940.1, AL596247.22,
            BC013575.2 and AB208961.1.
            
            On Jan 1, 2020 this sequence version replaced NP_001306120.1.
            
            Summary: This gene encodes a secreted serine protease that converts
            plasminogen to plasmin. The encoded preproprotein is
            proteolytically processed to generate A and B polypeptide chains.
            These chains associate via a single disulfide bond to form the
            catalytically inactive high molecular weight urokinase-type
            plasminogen activator (HMW-uPA). HMW-uPA can be further processed
            into the catalytically active low molecular weight urokinase-type
            plasminogen activator (LMW-uPA). This low molecular weight form
            does not bind to the urokinase-type plasminogen activator receptor.
            Mutations in this gene may be associated with Quebec platelet
            disorder and late-onset Alzheimer's disease. Alternative splicing
            results in multiple transcript variants, at least one of which
            encodes an isoform that is proteolytically processed. [provided by
            RefSeq, Jan 2016].
            
            Transcript Variant: This variant (3) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at a
            downstream start site compared to variant 1. The encoded isoform
            (3) has a shorter N-terminus and lacks a predicted signal peptide
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297940.1, SRR11853566.3554.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..345
                     /product="urokinase-type plasminogen activator isoform 3"
                     /EC_number="3.4.21.73"
                     /note="plasminogen activator, urinary; U-plasminogen
                     activator; urokinase-type plasminogen activator"
                     /calculated_mol_wt=38910
     Region          <1..66
                     /region_name="KR"
                     /note="Kringle domain; Kringle domains are believed to
                     play a role in binding mediators, such as peptides, other
                     proteins, membranes, or phospholipids. They are autonomous
                     structural domains, found in a varying number of copies,
                     in blood clotting and...; cd00108"
                     /db_xref="CDD:238056"
     Site            order(8,18,46,48,57)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Region          93..336
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            93
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(138,189,290)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            order(284,309,311)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..345
                     /gene="PLAU"
                     /gene_synonym="ATF; BDPLT5; QPD; u-PA; UPA; URK"
                     /coded_by="NM_001319191.2:349..1386"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:5328"
                     /db_xref="HGNC:HGNC:9052"
                     /db_xref="MIM:191840"
ORIGIN      
        1 mgrpclpwns atvlqqtyha hrsdalqlgl gkhnycrnpd nrrrpwcyvq vglkllvqec
       61 mvhdcadgkk pssppeelkf qcgqktlrpr fkiiggeftt ienqpwfaai yrrhrggsvt
      121 yvcggslisp cwvisathcf idypkkedyi vylgrsrlns ntqgemkfev enlilhkdys
      181 adtlahhndi allkirskeg rcaqpsrtiq ticlpsmynd pqfgtsceit gfgkenstdy
      241 lypeqlkmtv vklishrecq qphyygsevt tkmlcaadpq wktdscqgds ggplvcslqg
      301 rmtltgivsw grgcalkdkp gvytrvshfl pwirshtkee nglal
//
LOCUS       NP_524147                151 aa            linear   PRI 21-NOV-2025
DEFINITION  myosin light polypeptide 6 isoform 2 [Homo sapiens].
ACCESSION   NP_524147
VERSION     NP_524147.2
DBSOURCE    REFSEQ: accession NM_079423.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 151)
  AUTHORS   Zanivan,S., Maione,F., Hein,M.Y., Hernandez-Fernaud,J.R.,
            Ostasiewicz,P., Giraudo,E. and Mann,M.
  TITLE     SILAC-based proteomics of human primary endothelial cell
            morphogenesis unveils tumor angiogenic markers
  JOURNAL   Mol Cell Proteomics 12 (12), 3599-3611 (2013)
   PUBMED   23979707
REFERENCE   6  (residues 1 to 151)
  AUTHORS   Watanabe,M., Kohri,M., Takaishi,M., Horie,R. and Higashihara,M.
  TITLE     Molecular cloning and sequencing of myosin light chains in human
            megakaryoblastic leukemia cells
  JOURNAL   J Smooth Muscle Res 37 (1), 25-38 (2001)
   PUBMED   11436981
REFERENCE   7  (residues 1 to 151)
  AUTHORS   Komiyama,M., Soldati,T., von Arx,P. and Perriard,J.C.
  TITLE     The intracompartmental sorting of myosin alkali light chain
            isoproteins reflects the sequence of developmental expression as
            determined by double epitope-tagging competition
  JOURNAL   J Cell Sci 109 (Pt 8), 2089-2099 (1996)
   PUBMED   8856505
REFERENCE   8  (residues 1 to 151)
  AUTHORS   Bora,P.S., Bora,N.S., Wu,X., Kaplan,H.J. and Lange,L.G.
  TITLE     Molecular cloning, sequencing, and characterization of smooth
            muscle myosin alkali light chain from human eye cDNA: homology with
            myocardial fatty acid ethyl ester synthase-III cDNA
  JOURNAL   Genomics 19 (1), 186-188 (1994)
   PUBMED   8188229
REFERENCE   9  (residues 1 to 151)
  AUTHORS   Hailstones,D.L. and Gunning,P.W.
  TITLE     Characterization of human myosin light chains 1sa and 3nm:
            implications for isoform evolution and function
  JOURNAL   Mol Cell Biol 10 (3), 1095-1104 (1990)
   PUBMED   2304459
REFERENCE   10 (residues 1 to 151)
  AUTHORS   Lenz,S., Lohse,P., Seidel,U. and Arnold,H.H.
  TITLE     The alkali light chains of human smooth and nonmuscle myosins are
            encoded by a single gene. Tissue-specific expression by alternative
            splicing pathways
  JOURNAL   J Biol Chem 264 (15), 9009-9015 (1989)
   PUBMED   2722814
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG283793.1, BC093066.1 and
            CA427580.1.
            
            On Feb 28, 2006 this sequence version replaced NP_524147.1.
            
            Summary: Myosin is a hexameric ATPase cellular motor protein. It is
            composed of two heavy chains, two nonphosphorylatable alkali light
            chains, and two phosphorylatable regulatory light chains. This gene
            encodes a myosin alkali light chain that is expressed in smooth
            muscle and non-muscle tissues. Genomic sequences representing
            several pseudogenes have been described and two transcript variants
            encoding different isoforms have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an alternate coding exon
            compared to variant 1, that causes a frameshift. The resulting
            isoform (2) is the same length as isoform 1, but the proteins
            differ in their C-terminal sequences.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.196378.1,
                                           SRR5189658.146856.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.2"
     Protein         1..151
                     /product="myosin light polypeptide 6 isoform 2"
                     /note="myosin, light polypeptide 6, alkali, smooth muscle
                     and non-muscle; myosin light chain alkali 3; myosin light
                     chain A3; 17 kDa myosin light chain; myosin, light chain
                     6, alkali, smooth muscle and non-muscle"
                     /calculated_mol_wt=16830
     Region          5..149
                     /region_name="PTZ00184"
                     /note="calmodulin; Provisional"
                     /db_xref="CDD:185504"
     CDS             1..151
                     /gene="MYL6"
                     /gene_synonym="ESMLC; LC17; LC17-GI; LC17-NM; LC17A;
                     LC17B; MLC-3; MLC1SM; MLC3NM; MLC3SM"
                     /coded_by="NM_079423.4:44..499"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS31834.1"
                     /db_xref="GeneID:4637"
                     /db_xref="HGNC:HGNC:7587"
                     /db_xref="MIM:609931"
ORIGIN      
        1 mcdftedqta efkeafqlfd rtgdgkilys qcgdvmralg qnptnaevlk vlgnpksdem
       61 nvkvldfehf lpmlqtvakn kdqgtyedyv eglrvfdkeg ngtvmgaeir hvlvtlgekm
      121 teeevemlva ghedsngcin yeelvrmvln g
//
LOCUS       NP_001387119            1205 aa            linear   PRI 21-NOV-2025
DEFINITION  protein transport protein Sec31A isoform 3 [Homo sapiens].
ACCESSION   NP_001387119
VERSION     NP_001387119.1
DBSOURCE    REFSEQ: accession NM_001400190.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1205)
  AUTHORS   Tobias,E.S., Lucas-Herald,A.K., Sagar,D., Montezano,A.C.,
            Rios,F.J., De Lucca Camargo,L., Hamilton,G., Gazdagh,G.,
            Diver,L.A., Williams,N., Herzyk,P., Touyz,R.M., Greenfield,A.,
            McGowan,R. and Ahmed,S.F.
  TITLE     SEC31A may be associated with pituitary hormone deficiency and
            gonadal dysgenesis
  JOURNAL   Endocrine 84 (2), 345-349 (2024)
   PUBMED   38400880
  REMARK    GeneRIF: SEC31A may be associated with pituitary hormone deficiency
            and gonadal dysgenesis.
REFERENCE   2  (residues 1 to 1205)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1205)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1205)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1205)
  AUTHORS   Jin,L., Pahuja,K.B., Wickliffe,K.E., Gorur,A., Baumgartel,C.,
            Schekman,R. and Rape,M.
  TITLE     Ubiquitin-dependent regulation of COPII coat size and function
  JOURNAL   Nature 482 (7386), 495-500 (2012)
   PUBMED   22358839
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1205)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1205)
  AUTHORS   Kim,J.H., Hong,J.A., Pih,K.T. and Hwang,I.
  TITLE     Identification and isolation of differentially expressed genes in
            osmotically stressed human oral keratinocytes
  JOURNAL   Arch Oral Biol 46 (4), 335-341 (2001)
   PUBMED   11269867
REFERENCE   8  (residues 1 to 1205)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 1205)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   10 (residues 1 to 1205)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021105.13 and AC108469.5.
            
            Summary: The protein encoded by this gene shares similarity with
            the yeast Sec31 protein, and is a component of the outer layer of
            the coat protein complex II (COPII). The encoded protein is
            involved in vesicle budding from the endoplasmic reticulum (ER) and
            contains multiple WD repeats near the N-terminus and a proline-rich
            region in the C-terminal half. It associates with the protein
            encoded by the SEC13 homolog, nuclear pore and COPII coat complex
            component (SEC13), and is required for ER-Golgi transport.
            Monoubiquitylation of this protein by CUL3-KLHL12 was found to
            regulate the size of COPII coats to accommodate unusually shaped
            cargo. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1090680.1,
                                           SRR14038196.2833175.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..1205
                     /product="protein transport protein Sec31A isoform 3"
                     /note="yeast Sec31p homolog; protein transport protein
                     Sec31A; web1-like protein; SEC31 homolog A, COPII coat
                     complex component; SEC31-related protein A; SEC31-like
                     protein 1; SEC31 homolog A, COPII coating complex
                     component"
                     /calculated_mol_wt=131404
     Region          4..47
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          13..332
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(26,40,46..47,52..53,91,95,101..102,117,121,139,144,
                     150..151,164,185,190,196..197,209..210,231,235,244..245,
                     258..259,277,282,288..289,301..302,320,325,331..332)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          68..111
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          70..119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          120..160
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          125..162
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          161..471
                     /region_name="Interaction with SEC13.
                     /evidence=ECO:0000269|PubMed:16957052"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          172..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          263..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          306..331
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94979.3)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (O94979.3)"
     Region          <573..>696
                     /region_name="ACE1-Sec16-like"
                     /note="Ancestral coatomer element 1 (ACE1) of COPII coat
                     complex assembly protein Sec16; cl14807"
                     /db_xref="CDD:449359"
     Site            order(574..578,580,582,593,595,596..597,599..600,604,610,
                     618,630,633,658..659)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187750"
     Region          791..908
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          <793..>1088
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Site            799
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          842..848
                     /region_name="ALG-2-binding site motif-2 (ABS-2)"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Site            1146
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94979.3)"
     Site            1148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O94979.3)"
     CDS             1..1205
                     /gene="SEC31A"
                     /gene_synonym="ABP125; ABP130; HPBKS; HSPC275; HSPC334;
                     NEDSOSB; SEC31L1"
                     /coded_by="NM_001400190.1:376..3993"
                     /note="isoform 3 is encoded by transcript variant 29"
                     /db_xref="CCDS:CCDS47088.1"
                     /db_xref="GeneID:22872"
                     /db_xref="HGNC:HGNC:17052"
                     /db_xref="MIM:610257"
ORIGIN      
        1 mklkevdrta mqawspaqnh piylatgtsa qqldatfstn asleifeldl sdpsldmksc
       61 atfssshryh kliwgpykmd skgdvsgvli aggengniil ydpskiiagd kevviaqndk
      121 htgpvraldv nifqtnlvas ganeseiyiw dlnnfatpmt pgaktqpped isciawnrqv
      181 qhilasasps gratvwdlrk nepiikvsdh snrmhcsgla whpdvatqmv laseddrlpv
      241 iqmwdlrfas splrvlenha rgilaiawsm adpelllscg kdakilcsnp ntgevlyelp
      301 tntqwcfdiq wcprnpavls aasfdgrisv ysimggstdg lrqkqvdkls ssfgnldpfg
      361 tgqplpplqi pqqtaqhsiv lplkkppkwi rrpvgasfsf ggklvtfenv rmpshqgaeq
      421 qqqqhhvfis qvvtekefls rsdqlqqavq sqgfinycqk kidasqtefe knvwsflkvn
      481 feddsrgkyl ellgyrkedl gkkialalnk vdganvalkd sdqvaqsdge espaaeeqll
      541 gehikeekee seflpssggt fnisvsgdid glitqalltg nfesavdlcl hdnrmadaii
      601 laiaggqell artqkkyfak sqskitrlit avvmknwkei vescdlknwr ealaavltya
      661 kpdefsalcd llgtrleneg dsllqtqacl cyicagnvek lvacwtkaqd gshplslqdl
      721 iekvvilrka vqltqamdts tvgvllaakm sqyanllaaq gsiaaalafl pdntnqpnim
      781 qlrdrlcraq gepvaghesp kipyekqqlp kgrpgpvagh hqmprvqtqq yyphgenppp
      841 pgfimhgnvn pnaagqlpts pghmhtqvpp ypqpqpyqpa qpypfgtggs amyrpqqpva
      901 pptsnaypnt pyissassyt gqsqlyaaqh qassptsspa tsfppppssg asfqhggpga
      961 ppsssayalp pgttgpqngw ndppalnrvp kkkkmpenfm ppvpitspim nplgdpqsqm
     1021 lqqqpsapvp lssqssfpqp hlpggqpfhg vqqplgqtgm ppsfskpnie gapgapignt
     1081 fqhvqslptk kitkkpipde hlilkttfed liqrclssat dpqtkrkldd askrleflyd
     1141 klreqtlspt itsglhniar sietrnyseg ltmhthivst snfsetsafm pvlkvvltqa
     1201 nklgv
//
LOCUS       NP_001336252             318 aa            linear   PRI 21-NOV-2025
DEFINITION  F-box/LRR-repeat protein 2 isoform 6 [Homo sapiens].
ACCESSION   NP_001336252
VERSION     NP_001336252.1
DBSOURCE    REFSEQ: accession NM_001349323.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Li,F., Niu,M., Qin,K., Guo,R., Yi,Y., Xu,J., Li,L., Xie,S., Fu,M.,
            Wen,N., Liao,W. and Xiao,Z.J.
  TITLE     FBXL2 promotes E47 protein instability to inhibit breast cancer
            stemness and paclitaxel resistance
  JOURNAL   Oncogene 42 (5), 339-350 (2023)
   PUBMED   36460773
  REMARK    GeneRIF: FBXL2 promotes E47 protein instability to inhibit breast
            cancer stemness and paclitaxel resistance.
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Niu,M., Xu,J., Liu,Y., Li,Y., He,T., Ding,L., He,Y., Yi,Y., Li,F.,
            Guo,R., Gao,Y., Li,R., Li,L., Fu,M., Hu,Q., Luo,Y., Zhang,C.,
            Qin,K., Yi,J., Yu,S., Yang,J., Chen,H., Wang,L., Li,Z., Dong,B.,
            Qi,S., Ouyang,L., Zhang,Y., Cao,Y. and Xiao,Z.J.
  TITLE     FBXL2 counteracts Grp94 to destabilize EGFR and inhibit EGFR-driven
            NSCLC growth
  JOURNAL   Nat Commun 12 (1), 5919 (2021)
   PUBMED   34635651
  REMARK    GeneRIF: FBXL2 counteracts Grp94 to destabilize EGFR and inhibit
            EGFR-driven NSCLC growth.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Wang,C., Gale,M. Jr., Keller,B.C., Huang,H., Brown,M.S.,
            Goldstein,J.L. and Ye,J.
  TITLE     Identification of FBL2 as a geranylgeranylated cellular protein
            required for hepatitis C virus RNA replication
  JOURNAL   Mol Cell 18 (4), 425-434 (2005)
   PUBMED   15893726
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Ilyin,G.P., Rialland,M., Pigeon,C. and Guguen-Guillouzo,C.
  TITLE     cDNA cloning and expression analysis of new members of the
            mammalian F-box protein family
  JOURNAL   Genomics 67 (1), 40-47 (2000)
   PUBMED   10945468
REFERENCE   8  (residues 1 to 318)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   9  (residues 1 to 318)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
REFERENCE   10 (residues 1 to 318)
  AUTHORS   Ilyin,G.P., Rialland,M., Glaise,D. and Guguen-Guillouzo,C.
  TITLE     Identification of a novel Skp2-like mammalian protein containing
            F-box and leucine-rich repeats
  JOURNAL   FEBS Lett 459 (1), 75-79 (1999)
   PUBMED   10508920
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC123900.2 and AC122176.2.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box),
            which function in phosphorylation-dependent ubiquitination. The
            F-box proteins are divided into 3 classes: Fbws containing WD-40
            domains, Fbls containing leucine-rich repeats, and Fbxs containing
            either different protein-protein interaction modules or no
            recognizable motifs. The protein encoded by this gene belongs to
            the Fbls class and, in addition to an F-box, contains 12 tandem
            leucine-rich repeats. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2010].
            
            Transcript Variant: This variant (8), as well as variants 9, 10,
            and 11, encodes isoform 6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.133704.1,
                                           SRR1660807.119526.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155371 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.3"
     Protein         1..318
                     /product="F-box/LRR-repeat protein 2 isoform 6"
                     /note="F-box protein containing leucine-rich repeats;
                     F-box/LRR-repeat protein 2; F-box protein FBL2/FBL3"
                     /calculated_mol_wt=35164
     Region          27..52
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          53..78
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          63..262
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          79..104
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          105..130
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          131..156
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          157..182
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          183..208
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          209..228
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          238..257
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..318
                     /gene="FBXL2"
                     /gene_synonym="FBL2; FBL3"
                     /coded_by="NM_001349323.2:404..1360"
                     /note="isoform 6 is encoded by transcript variant 8"
                     /db_xref="GeneID:25827"
                     /db_xref="HGNC:HGNC:13598"
                     /db_xref="MIM:605652"
ORIGIN      
        1 mdaqksltvr llffstcysl srfcsklkhl dltscvsitn sslkgisegc rnleylnlsw
       61 cdqitkdgie alvrgcrglk alllrgctql edealkhiqn ychelvslnl qscsritdeg
      121 vvqicrgchr lqalclsgcs nltdasltal glncprlqil eaarcshltd agftllarnc
      181 helekmdlee cilitdstli qlsihcpklq alslshceli tddgilhlsn stcgherlrv
      241 leldncllit dvalehlenc rglerlelyd cqqvtragik rmraqlphvk vhayfapvtp
      301 ptavagsgqr lcrccvil
//
LOCUS       NP_001289963             244 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal acetylcholine receptor subunit alpha-10 isoform b [Homo
            sapiens].
ACCESSION   NP_001289963
VERSION     NP_001289963.1
DBSOURCE    REFSEQ: accession NM_001303034.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Gu,S., Knowland,D., Matta,J.A., O'Carroll,M.L., Davini,W.B.,
            Dhara,M., Kweon,H.J. and Bredt,D.S.
  TITLE     Hair cell alpha9alpha10 nicotinic acetylcholine receptor functional
            expression regulated by ligand binding and deafness gene products
  JOURNAL   Proc Natl Acad Sci U S A 117 (39), 24534-24544 (2020)
   PUBMED   32929005
  REMARK    GeneRIF: Hair cell alpha9alpha10 nicotinic acetylcholine receptor
            functional expression regulated by ligand binding and deafness gene
            products.
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Zouridakis,M., Giastas,P., Zarkadas,E., Chroni-Tzartou,D.,
            Bregestovski,P. and Tzartos,S.J.
  TITLE     Crystal structures of free and antagonist-bound states of human
            alpha9 nicotinic receptor extracellular domain
  JOURNAL   Nat Struct Mol Biol 21 (11), 976-980 (2014)
   PUBMED   25282151
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Azam,L. and McIntosh,J.M.
  TITLE     Molecular basis for the differential sensitivity of rat and human
            alpha9alpha10 nAChRs to alpha-conotoxin RgIA
  JOURNAL   J Neurochem 122 (6), 1137-1144 (2012)
   PUBMED   22774872
  REMARK    GeneRIF: A two order of magnitude species difference is reported in
            potency of alpha-conotoxin RgIA for rat versus human alpha9alpha10
            nAChR.
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Rigbi,A., Yakir,A., Sarner-Kanyas,K., Pollak,Y. and Lerer,B.
  TITLE     Why do young women smoke? VI. A controlled study of nicotine
            effects on attention: pharmacogenetic interactions
  JOURNAL   Pharmacogenomics J 11 (1), 45-52 (2011)
   PUBMED   20231857
  REMARK    GeneRIF: Clinical trial of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Saccone,N.L., Schwantes-An,T.H., Wang,J.C., Grucza,R.A.,
            Breslau,N., Hatsukami,D., Johnson,E.O., Rice,J.P., Goate,A.M. and
            Bierut,L.J.
  TITLE     Multiple cholinergic nicotinic receptor genes affect nicotine
            dependence risk in African and European Americans
  JOURNAL   Genes Brain Behav 9 (7), 741-750 (2010)
   PUBMED   20584212
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 244)
  AUTHORS   Rigbi,A., Kanyas,K., Yakir,A., Greenbaum,L., Pollak,Y.,
            Ben-Asher,E., Lancet,D., Kertzman,S. and Lerer,B.
  TITLE     Why do young women smoke? V. Role of direct and interactive effects
            of nicotinic cholinergic receptor gene variation on neurocognitive
            function
  JOURNAL   Genes Brain Behav 7 (2), 164-172 (2008)
   PUBMED   17559419
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   7  (residues 1 to 244)
  AUTHORS   Shi,J., Hattori,E., Zou,H., Badner,J.A., Christian,S.L.,
            Gershon,E.S. and Liu,C.
  TITLE     No evidence for association between 19 cholinergic genes and
            bipolar disorder
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 144B (6), 715-723 (2007)
   PUBMED   17373692
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 244)
  AUTHORS   Peng,H., Ferris,R.L., Matthews,T., Hiel,H., Lopez-Albaitero,A. and
            Lustig,L.R.
  TITLE     Characterization of the human nicotinic acetylcholine receptor
            subunit alpha (alpha) 9 (CHRNA9) and alpha (alpha) 10 (CHRNA10) in
            lymphocytes
  JOURNAL   Life Sci 76 (3), 263-280 (2004)
   PUBMED   15531379
REFERENCE   9  (residues 1 to 244)
  AUTHORS   Sgard,F., Charpantier,E., Bertrand,S., Walker,N., Caput,D.,
            Graham,D., Bertrand,D. and Besnard,F.
  TITLE     A novel human nicotinic receptor subunit, alpha10, that confers
            functionality to the alpha9-subunit
  JOURNAL   Mol Pharmacol 61 (1), 150-159 (2002)
   PUBMED   11752216
REFERENCE   10 (residues 1 to 244)
  AUTHORS   Lustig,L.R., Peng,H., Hiel,H., Yamamoto,T. and Fuchs,P.A.
  TITLE     Molecular cloning and mapping of the human nicotinic acetylcholine
            receptor alpha10 (CHRNA10)
  JOURNAL   Genomics 73 (3), 272-283 (2001)
   PUBMED   11350119
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF199235.2, BC143303.1 and AC060812.15.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            at an internal exon compared to variant 1. This difference results
            in translation initiation at a downstream in-frame start site
            through ribosomal re-initiation or leaky scanning. The encoded
            isoform (b) is shorter at the N-terminus compared to isoform a.
            Variants 2 and 3 both encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143303.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158188, SAMN04284274
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..244
                     /product="neuronal acetylcholine receptor subunit alpha-10
                     isoform b"
                     /note="cholinergic receptor, nicotinic, alpha polypeptide
                     10; neuronal acetylcholine receptor subunit alpha-10;
                     NACHR alpha-10; nicotinic acetylcholine receptor subunit
                     alpha-10; acetylcholine receptor, nicotinic, alpha 10
                     (neuronal); cholinergic receptor, nicotinic, alpha 10
                     (neuronal); cholinergic receptor, nicotinic alpha 10"
                     /calculated_mol_wt=26669
     Region          <1..29
                     /region_name="LGIC_ECD"
                     /note="extracellular domain (ECD) of Cys-loop
                     neurotransmitter-gated ion channels (also known as
                     ligand-gated ion channel (LGIC)); cl28912"
                     /db_xref="CDD:475126"
     Region          33..>118
                     /region_name="LGIC_TM_cation"
                     /note="transmembrane domain of Cys-loop
                     neurotransmitter-gated ion channels, includes 5HT3, nAChR,
                     and ZAC; cd19051"
                     /db_xref="CDD:349853"
     Region          33..55
                     /region_name="TM1 helix"
                     /note="TM1 helix [structural motif]"
                     /db_xref="CDD:349853"
     Region          37..228
                     /region_name="Neur_chan_memb"
                     /note="Neurotransmitter-gated ion-channel transmembrane
                     region; pfam02932"
                     /db_xref="CDD:460753"
     Region          63..84
                     /region_name="TM2 helix"
                     /note="TM2 helix [structural motif]"
                     /db_xref="CDD:349853"
     Region          94..116
                     /region_name="TM3 helix"
                     /note="TM3 helix [structural motif]"
                     /db_xref="CDD:349853"
     CDS             1..244
                     /gene="CHRNA10"
                     /coded_by="NM_001303034.2:753..1487"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:57053"
                     /db_xref="HGNC:HGNC:13800"
                     /db_xref="MIM:606372"
ORIGIN      
        1 mparrrvlty gccsepypdv tftlllrrra aayvcnlllp cvlisllapl afhlpadsge
       61 kvslgvtvll altvfqllla esmppaesvp ligkyymatm tmvtfstalt ilimnlhycg
      121 psvrpvpawa ralllghlar glcvrergep cgqsrppels pspqspegga gppagpchep
      181 rclcrqeall hhvatiantf rshraaqrch edwkrlarvm drfflaiffs malvmsllvl
      241 vqal
//
LOCUS       NP_001229773             358 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase RNF146 isoform a [Homo sapiens].
ACCESSION   NP_001229773
VERSION     NP_001229773.1
DBSOURCE    REFSEQ: accession NM_001242844.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Li,W., Han,Q., Zhu,Y., Zhou,Y., Zhang,J., Wu,W., Li,Y., Liu,L.,
            Qiu,Y., Hu,K. and Yin,D.
  TITLE     SUMOylation of RNF146 results in Axin degradation and activation of
            Wnt/beta-catenin signaling to promote the progression of
            hepatocellular carcinoma
  JOURNAL   Oncogene 42 (21), 1728-1740 (2023)
   PUBMED   37029301
  REMARK    GeneRIF: SUMOylation of RNF146 results in Axin degradation and
            activation of Wnt/beta-catenin signaling to promote the progression
            of hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Xu,Y.R., Shi,M.L., Zhang,Y., Kong,N., Wang,C., Xiao,Y.F., Du,S.S.,
            Zhu,Q.Y. and Lei,C.Q.
  TITLE     Tankyrases inhibit innate antiviral response by PARylating
            VISA/MAVS and priming it for RNF146-mediated ubiquitination and
            degradation
  JOURNAL   Proc Natl Acad Sci U S A 119 (26), e2122805119 (2022)
   PUBMED   35733260
  REMARK    GeneRIF: Tankyrases inhibit innate antiviral response by PARylating
            VISA/MAVS and priming it for RNF146-mediated ubiquitination and
            degradation.
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Zhang,Y., Liu,S., Mickanin,C., Feng,Y., Charlat,O., Michaud,G.A.,
            Schirle,M., Shi,X., Hild,M., Bauer,A., Myer,V.E., Finan,P.M.,
            Porter,J.A., Huang,S.M. and Cong,F.
  TITLE     RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin
            degradation and Wnt signalling
  JOURNAL   Nat Cell Biol 13 (5), 623-629 (2011)
   PUBMED   21478859
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Menachem,T.D., Laitman,Y., Kaufman,B. and Friedman,E.
  TITLE     The RNF146 and ECHDC1 genes as candidates for inherited breast and
            ovarian cancer in Jewish Ashkenazi women
  JOURNAL   Fam Cancer 8 (4), 399-402 (2009)
   PUBMED   19517271
  REMARK    GeneRIF: Mutations in the coding regions of the RNF146 and ECHDC1
            genes do not contribute to the burden of inherited predisposition
            of breast cancer in Ashkenazi high risk women.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 358)
  AUTHORS   Gold,B., Kirchhoff,T., Stefanov,S., Lautenberger,J., Viale,A.,
            Garber,J., Friedman,E., Narod,S., Olshen,A.B., Gregersen,P.,
            Kosarin,K., Olsh,A., Bergeron,J., Ellis,N.A., Klein,R.J.,
            Clark,A.G., Norton,L., Dean,M., Boyd,J. and Offit,K.
  TITLE     Genome-wide association study provides evidence for a breast cancer
            risk locus at 6q22.33
  JOURNAL   Proc Natl Acad Sci U S A 105 (11), 4340-4345 (2008)
   PUBMED   18326623
  REMARK    GeneRIF: Genome-wide association study of gene-disease association.
            (HuGE Navigator)
REFERENCE   9  (residues 1 to 358)
  AUTHORS   von Rotz,R.C., Kins,S., Hipfel,R., von der Kammer,H. and
            Nitsch,R.M.
  TITLE     The novel cytosolic RING finger protein dactylidin is up-regulated
            in brains of patients with Alzheimer's disease
  JOURNAL   Eur J Neurosci 21 (5), 1289-1298 (2005)
   PUBMED   15813938
  REMARK    GeneRIF: Dactylidin may function early in the progression of
            Alzheimer's disease.
REFERENCE   10 (residues 1 to 358)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA639989.1 and AJ420549.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the shorter isoform (a). Variants 1-7 encode
            the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3613276.1,
                                           SRR14038192.3595620.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.33"
     Protein         1..358
                     /product="E3 ubiquitin-protein ligase RNF146 isoform a"
                     /EC_number="2.3.2.27"
                     /note="dactylidin; RING-type E3 ubiquitin transferase
                     RNF146; E3 ubiquitin-protein ligase RNF146; iduna"
                     /calculated_mol_wt=38688
     Region          34..83
                     /region_name="RING-HC_RNF146"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 146 (RNF146) and similar proteins; cd16546"
                     /db_xref="CDD:438208"
     Site            order(37..38,40,69,71..72)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438208"
     Region          103..175
                     /region_name="WWE"
                     /note="Domain in Deltex and TRIP12 homologues. Possibly
                     involved in regulation of ubiquitin-mediated proteolysis;
                     smart00678"
                     /db_xref="CDD:128922"
     CDS             1..358
                     /gene="RNF146"
                     /coded_by="NM_001242844.2:581..1657"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5136.1"
                     /db_xref="GeneID:81847"
                     /db_xref="HGNC:HGNC:21336"
                     /db_xref="MIM:612137"
ORIGIN      
        1 magcgeidhs inmlptnrka nescsntaps ltvpecaicl qtcvhpvslp ckhvfcylcv
       61 kgaswlgkrc alcrqeiped fldkptllsp eelkaasrgn geyawyyegr ngwwqydert
      121 sreledafsk gkkntemlia gflyvadlen mvqyrrnehg rrrkikrdii dipkkgvagl
      181 rldcdantvn laressadga dsvsaqsgas vqplvssvrp ltsvdgqlts patpspdast
      241 sledsfahlq lsgdntaers hrgegeedhe spssgrvpap dtsieetesd assdsedvsa
      301 vvaqhsltqq rllvsnanqt vpdrsdrsgt drsvagggtv svsvrsrrpd gqctvtev
//
LOCUS       NP_001381437             911 aa            linear   PRI 21-NOV-2025
DEFINITION  general transcription factor 3C polypeptide 2 isoform b [Homo
            sapiens].
ACCESSION   NP_001381437
VERSION     NP_001381437.1
DBSOURCE    REFSEQ: accession NM_001394508.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Peng,F., Zhou,Y., Wang,J., Guo,B., Wei,Y., Deng,H., Wu,Z.,
            Zhang,C., Shi,K., Li,Y., Wang,X., Shore,P., Zhao,S. and Deng,W.
  TITLE     The transcription factor Sp1 modulates RNA polymerase III gene
            transcription by controlling BRF1 and GTF3C2 expression in human
            cells
  JOURNAL   J Biol Chem 295 (14), 4617-4630 (2020)
   PUBMED   32115405
  REMARK    GeneRIF: The transcription factor Sp1 modulates RNA polymerase III
            gene transcription by controlling BRF1 and GTF3C2 expression in
            human cells.
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 911)
  AUTHORS   Kantidakis,T., Ramsbottom,B.A., Birch,J.L., Dowding,S.N. and
            White,R.J.
  TITLE     mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes,
            and targets their repressor Maf1
  JOURNAL   Proc Natl Acad Sci U S A 107 (26), 11823-11828 (2010)
   PUBMED   20543138
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11465]
REFERENCE   5  (residues 1 to 911)
  AUTHORS   Hirschowitz,E.A., Hiestand,D.M. and Yannelli,J.R.
  TITLE     Vaccines for lung cancer
  JOURNAL   J Thorac Oncol 1 (1), 93-104 (2006)
   PUBMED   17409835
  REMARK    Review article
REFERENCE   6  (residues 1 to 911)
  AUTHORS   Wang,Z. and Roeder,R.G.
  TITLE     DNA topoisomerase I and PC4 can interact with human TFIIIC to
            promote both accurate termination and transcription reinitiation by
            RNA polymerase III
  JOURNAL   Mol Cell 1 (5), 749-757 (1998)
   PUBMED   9660958
REFERENCE   7  (residues 1 to 911)
  AUTHORS   Oettel,S., Hartel,F., Kober,I., Iben,S. and Seifart,K.H.
  TITLE     Human transcription factors IIIC2, IIIC1 and a novel component
            IIIC0 fulfil different aspects of DNA binding to various pol III
            genes
  JOURNAL   Nucleic Acids Res 25 (12), 2440-2447 (1997)
   PUBMED   9171097
REFERENCE   8  (residues 1 to 911)
  AUTHORS   Chu,W.M., Wang,Z., Roeder,R.G. and Schmid,C.W.
  TITLE     RNA polymerase III transcription repressed by Rb through its
            interactions with TFIIIB and TFIIIC2
  JOURNAL   J Biol Chem 272 (23), 14755-14761 (1997)
   PUBMED   9169441
REFERENCE   9  (residues 1 to 911)
  AUTHORS   Sinn,E., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     Cloning and characterization of a TFIIIC2 subunit (TFIIIC beta)
            whose presence correlates with activation of RNA polymerase
            III-mediated transcription by adenovirus E1A expression and serum
            factors
  JOURNAL   Genes Dev 9 (6), 675-685 (1995)
   PUBMED   7729686
REFERENCE   10 (residues 1 to 911)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC074117.7, AC109828.4 and AC013413.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.859249.1,
                                           SRR14038196.1505882.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..911
                     /product="general transcription factor 3C polypeptide 2
                     isoform b"
                     /note="general transcription factor 3C polypeptide 2;
                     TFIIIC 110 kDa subunit; transcription factor IIIC subunit
                     beta; transcription factor IIIC 110 kDa subunit; general
                     transcription factor IIIC, polypeptide 2, beta 110kDa"
                     /calculated_mol_wt=100549
     Region          24..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          <62..255
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          205..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          366..426
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          427..483
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          470..543
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          484..535
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          536..603
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          558..595
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <559..644
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          604..654
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          616..656
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          655..690
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          765..785
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            871
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          889..911
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            892
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            893
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            895
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            901
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     CDS             1..911
                     /gene="GTF3C2"
                     /gene_synonym="TF3C-beta; TFIIIC-BETA; TFIIIC110"
                     /coded_by="NM_001394508.1:455..3190"
                     /note="isoform b is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS1749.1"
                     /db_xref="GeneID:2976"
                     /db_xref="HGNC:HGNC:4665"
                     /db_xref="MIM:604883"
ORIGIN      
        1 mdtcgvgyva lgeagpvgnm tvvdspgqev lnqldvktss emtsaeasve mslptplpgf
       61 edspdqrrlp peqeslsrle qpdlssemsk vskpraskpg rkrggrtrkg pkrpqqpnpp
      121 saplvpglld qsnplstpmp kkrgrkskae llllklskdl drpesqspkr ppedfetpsg
      181 erprrraaqv allylqelae elstalpapv scpegpkvss ptkpkkirqp aacpggeevd
      241 gaprdedffl qveaedvees egpsesssep epvvprstpr gstsgkqkph crgmapnglp
      301 nhimapvwkc lhltkdfreq khsywefaew iplawkwhll seleaapylp qeeksplfsv
      361 qreglpedgt lyrinrfssi tahperwdvs fftggplwal dwcpvpegag asqyvalfss
      421 pdmnethpls qlhsgpgllq lwglgtlqqe scpgnrahfv ygiacdngci wdlkfcpsga
      481 welpgtprka pllprlglla lacsdgkvll fslphpeall aqqppdavkp aiykvqcvat
      541 lqvgsmqatd psecgqclsl awmptrphqh laagyyngmv vfwnlptnsp lqrirlsdgs
      601 lklypfqcfl ahdqavrtlq wckanshflv sagsdrkikf wdlrrpyepi nsikrflste
      661 lawllpyngv tvaqdncyas yglcgihyid agylgfkayf taprkgtvws lsgsdwlgti
      721 aagdisgeli aailpdmaln pinvkrpver rfpiykadli pyqdspegpd hssassgvpn
      781 ppkartytet vnhhyllfqd tdlgsfhdll rrepmlrmqe geghsqlcld rlqleaihkv
      841 rfspnldsyg wlvsggqsgl vrihfvrgla splghrmqle srahfnamfq pssptrrpgf
      901 sptshrllpt p
//
LOCUS       NP_001271242             327 aa            linear   PRI 21-NOV-2025
DEFINITION  drebrin-like protein isoform d [Homo sapiens].
ACCESSION   NP_001271242 XP_005249779
VERSION     NP_001271242.1
DBSOURCE    REFSEQ: accession NM_001284313.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Ghosh,A., Enderlein,J. and Butkevich,E.
  TITLE     Dimerization of Human Drebrin-like Protein Governs Its Biological
            Activity
  JOURNAL   Biochemistry 59 (16), 1553-1558 (2020)
   PUBMED   32282191
  REMARK    GeneRIF: Dimerization of Human Drebrin-like Protein Governs Its
            Biological Activity.
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Yamazaki,H., Takahashi,H., Aoki,T. and Shirao,T.
  TITLE     Molecular cloning and dendritic localization of rat SH3P7
  JOURNAL   Eur J Neurosci 14 (6), 998-1008 (2001)
   PUBMED   11595038
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Ensenat,D., Yao,Z., Wang,X.S., Kori,R., Zhou,G., Lee,S.C. and
            Tan,T.H.
  TITLE     A novel src homology 3 domain-containing adaptor protein, HIP-55,
            that interacts with hematopoietic progenitor kinase 1
  JOURNAL   J Biol Chem 274 (48), 33945-33950 (1999)
   PUBMED   10567356
  REMARK    Erratum:[J Biol Chem 2000 May 5;275(18):14004]
REFERENCE   8  (residues 1 to 327)
  AUTHORS   Lee,C.G., Morse,H.C. 3rd, Kay,B.K. and Kozak,C.A.
  TITLE     Genetic mapping of eight SH3 domain genes on seven mouse
            chromosomes
  JOURNAL   Mamm Genome 10 (4), 402-404 (1999)
   PUBMED   10087302
REFERENCE   9  (residues 1 to 327)
  AUTHORS   Larbolette,O., Wollscheid,B., Schweikert,J., Nielsen,P.J. and
            Wienands,J.
  TITLE     SH3P7 is a cytoskeleton adapter protein and is coupled to signal
            transduction from lymphocyte antigen receptors
  JOURNAL   Mol Cell Biol 19 (2), 1539-1546 (1999)
   PUBMED   9891087
REFERENCE   10 (residues 1 to 327)
  AUTHORS   Gipson,I.K., Spurr-Michaud,S., Moccia,R., Zhan,Q., Toribara,N.,
            Ho,S.B., Gargiulo,A.R. and Hill,J.A. 3rd.
  TITLE     MUC4 and MUC5B transcripts are the prevalent mucin messenger
            ribonucleic acids of the human endocervix
  JOURNAL   Biol Reprod 60 (1), 58-64 (1999)
   PUBMED   9858486
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK293698.1, AF218020.3 and AC017116.7.
            
            On Sep 27, 2013 this sequence version replaced XP_005249779.1.
            
            Transcript Variant: This variant (4) lacks two exons, uses an
            alternate in-frame splice site and initiates translation at a
            downstream start codon compared to variant 1. The encoded isoform
            (d) has a shorter N-terminus compared to isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293698.1, SRR14038194.2305623.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2144835
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..327
                     /product="drebrin-like protein isoform d"
                     /note="src homology 3 domain-containing protein HIP-55;
                     drebrin-like protein; drebrin-F; cervical SH3P7; SH3
                     domain-containing protein 7; cervical mucin-associated
                     protein; HPK1-interacting protein of 55 kDa; actin-binding
                     protein 1"
                     /calculated_mol_wt=36970
     Region          <1..35
                     /region_name="ADF_gelsolin"
                     /note="Actin depolymerization factor/cofilin- and
                     gelsolin-like domains; cl15697"
                     /db_xref="CDD:472830"
     Region          272..325
                     /region_name="SH3_Abp1_eu"
                     /note="Src homology 3 domain of eumetazoan Actin-binding
                     protein 1; cd11960"
                     /db_xref="CDD:212893"
     Site            order(277,279,282,285..286,304..305,317,319,321..322)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212893"
     CDS             1..327
                     /gene="DBNL"
                     /gene_synonym="ABP1; HIP-55; HIP55; SH3P7"
                     /coded_by="NM_001284313.2:177..1160"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS64634.1"
                     /db_xref="GeneID:28988"
                     /db_xref="HGNC:HGNC:2696"
                     /db_xref="MIM:610106"
ORIGIN      
        1 masflkgahv tinaraeedv epecimekva kasganysfh kesgrfqdvg pqapvgsvyq
       61 ktnavseikr vgkdsfwaka ekeeenrrle ekrraeeaqr qleqerrere lreaarreqr
      121 yqeqggeasp qrtweqqqev vsrnrneqes avhpreifkq keramsttsi sspqpgklrs
      181 pflqkqltqp ethfgrepaa aisrpradlp aeepapstpp clvqaeeeav yeeppeqetf
      241 yeqpplvqqq gagsehidhh iqgqglsgqg lcaralydyq aaddteisfd penlitgiev
      301 idegwwrgyg pdghfgmfpa nyvelie
//
LOCUS       NP_001978                452 aa            linear   PRI 21-NOV-2025
DEFINITION  transcription factor ETV6 isoform 1 [Homo sapiens].
ACCESSION   NP_001978
VERSION     NP_001978.1
DBSOURCE    REFSEQ: accession NM_001987.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Xu,W., Tian,F., Tai,X., Song,G., Liu,Y., Fan,L., Weng,X., Yang,E.,
            Wang,M., Bornhauser,M., Zhang,C., Lock,R.B., Wong,J.W.H., Wang,J.,
            Jing,D. and Mi,J.Q.
  TITLE     ETV6::ACSL6 translocation-driven super-enhancer activation leads to
            eosinophilia in acute lymphoblastic leukemia through IL-3
            overexpression
  JOURNAL   Haematologica 109 (8), 2445-2458 (2024)
   PUBMED   38356460
  REMARK    GeneRIF: ETV6::ACSL6 translocation-driven super-enhancer activation
            leads to eosinophilia in acute lymphoblastic leukemia through IL-3
            overexpression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Xue,S., Sun,H.P., Huang,X.B., Chen,X., Wang,T., Ma,W., Tian,Y.,
            Pan,Z.L., Li,L.H., Zhang,L., Liu,H.X. and Cao,X.Y.
  TITLE     Characteristics and literature review of ETV6::ABL1 fusion
            gene-positive acute myeloid leukemia
  JOURNAL   Int J Hematol 119 (5), 564-572 (2024)
   PUBMED   38441775
  REMARK    GeneRIF: Characteristics and literature review of ETV6::ABL1 fusion
            gene-positive acute myeloid leukemia.
            Review article
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Mueller,S.B., Pikman,Y., Tasian,S.K., Silverman,L.B., Harris,M.H.
            and Tsai,H.K.
  TITLE     ETV6 fusions from insertions of exons 3-5 in pediatric hematologic
            malignancies
  JOURNAL   Haematologica 108 (12), 3471-3476 (2023)
   PUBMED   37381775
  REMARK    GeneRIF: ETV6 fusions from insertions of exons 3-5 in pediatric
            hematologic malignancies.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 452)
  AUTHORS   Klubickova,N., Mosaieby,E., Ptakova,N., Trinquet,A., Lae,M.,
            Costes-Martineau,V. and Skalova,A.
  TITLE     High-grade non-intestinal type sinonasal adenocarcinoma with
            ETV6::NTRK3 fusion, distinct from secretory carcinoma by
            immunoprofile and morphology
  JOURNAL   Virchows Arch 483 (2), 187-195 (2023)
   PUBMED   37415052
  REMARK    GeneRIF: High-grade non-intestinal type sinonasal adenocarcinoma
            with ETV6::NTRK3 fusion, distinct from secretory carcinoma by
            immunoprofile and morphology.
REFERENCE   6  (residues 1 to 452)
  AUTHORS   Romana,S.P., Mauchauffe,M., Le Coniat,M., Chumakov,I., Le
            Paslier,D., Berger,R. and Bernard,O.A.
  TITLE     The t(12;21) of acute lymphoblastic leukemia results in a tel-AML1
            gene fusion
  JOURNAL   Blood 85 (12), 3662-3670 (1995)
   PUBMED   7780150
REFERENCE   7  (residues 1 to 452)
  AUTHORS   Golub,T.R., Barker,G.F., Bohlander,S.K., Hiebert,S.W., Ward,D.C.,
            Bray-Ward,P., Morgan,E., Raimondi,S.C., Rowley,J.D. and
            Gilliland,D.G.
  TITLE     Fusion of the TEL gene on 12p13 to the AML1 gene on 21q22 in acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 92 (11), 4917-4921 (1995)
   PUBMED   7761424
REFERENCE   8  (residues 1 to 452)
  AUTHORS   Buijs,A., Sherr,S., van Baal,S., van Bezouw,S., van der Plas,D.,
            Geurts van Kessel,A., Riegman,P., Lekanne Deprez,R., Zwarthoff,E.,
            Hagemeijer,A. et al.
  TITLE     Translocation (12;22) (p13;q11) in myeloproliferative disorders
            results in fusion of the ETS-like TEL gene on 12p13 to the MN1 gene
            on 22q11
  JOURNAL   Oncogene 10 (8), 1511-1519 (1995)
   PUBMED   7731705
  REMARK    Erratum:[Oncogene 1995 Aug 17;11(4):809]
REFERENCE   9  (residues 1 to 452)
  AUTHORS   Pencheva,B., Di Paola,J. and Porter,C.C.
  TITLE     ETV6-Related Thrombocytopenia and Predisposition to Leukemia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   33226740
REFERENCE   10 (residues 1 to 452)
  AUTHORS   Fainstein,E., Einat,M., Gokkel,E., Marcelle,C., Croce,C.M.,
            Gale,R.P. and Canaani,E.
  TITLE     Nucleotide sequence analysis of human abl and bcr-abl cDNAs
  JOURNAL   Oncogene 4 (12), 1477-1481 (1989)
   PUBMED   2687768
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007450.1, BC043399.1,
            T79261.1 and AC084358.19.
            
            Summary: This gene encodes an ETS family transcription factor. The
            product of this gene contains two functional domains: a N-terminal
            pointed (PNT) domain that is involved in protein-protein
            interactions with itself and other proteins, and a C-terminal
            DNA-binding domain. Gene knockout studies in mice suggest that it
            is required for hematopoiesis and maintenance of the developing
            vascular network. This gene is known to be involved in a large
            number of chromosomal rearrangements associated with leukemia and
            congenital fibrosarcoma. [provided by RefSeq, Sep 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.6560.1, BC043399.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396373.9/ ENSP00000379658.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..452
                     /product="transcription factor ETV6 isoform 1"
                     /note="ets variant gene 6 (TEL oncogene); TEL1 oncogene;
                     transcription factor ETV6; ETS-related protein Tel1;
                     ETV6-RUNX1 fusion protein"
                     /calculated_mol_wt=52869
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            11..12
                     /site_type="other"
                     /note="Breakpoint for translocation to form CHIC2-ETV6 in
                     AML; propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12435397,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            54..55
                     /site_type="other"
                     /note="Breakpoint for translocation to form ETV6-MDS2 in
                     MDS; propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            55..56
                     /site_type="other"
                     /note="Breakpoint for translocation to form PAX5-ETV6;
                     propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Region          56..123
                     /region_name="SAM_PNT-Tel_Yan"
                     /note="Sterile alpha motif (SAM)/Pointed domain of Tel/Yan
                     protein; cd08535"
                     /db_xref="CDD:176085"
     Site            order(63,85,88..90,92..93,96,98,100..101,104..105)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:176085"
     Site            order(75..80,107..109,111..112,115..116)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:176085"
     Region          158..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97360; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14.
                     /evidence=ECO:0000269|PubMed:12435397; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            302
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97360; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            336..337
                     /site_type="other"
                     /note="Breakpoint for translocation to form ETV6-AML1 in
                     ALL; propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Region          338..424
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..452
                     /gene="ETV6"
                     /gene_synonym="TEL; TEL/ABL; THC5"
                     /coded_by="NM_001987.5:455..1813"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8643.1"
                     /db_xref="GeneID:2120"
                     /db_xref="HGNC:HGNC:3495"
                     /db_xref="MIM:600618"
ORIGIN      
        1 msetpaqcsi kqerisytpp espvpsyass tplhvpvpra lrmeedsirl pahlrlqpiy
       61 wsrddvaqwl kwaenefslr pidsntfemn gkalllltke dfryrsphsg dvlyellqhi
      121 lkqrkprilf spffhpgnsi htqpevilhq nheedncvqr tprpsvdnvh hnpptiellh
      181 rsrspittnh rpspdpeqrp lrspldnmir rlspaeraqg prphqennhq esyplsvspm
      241 ennhcpasse shpkpssprq estrviqlmp spimhpliln prhsvdfkqs rlsedglhre
      301 gkpinlshre dlaymnhimv svsppeeham pigriadcrl lwdyvyqlls dsryenfirw
      361 edkeskifri vdpnglarlw gnhknrtnmt yekmsralrh yyklniirke pgqrllfrfm
      421 ktpdeimsgr tdrlehlesq eldeqiyqed ec
//
LOCUS       NP_001362886             764 aa            linear   PRI 21-NOV-2025
DEFINITION  protein zer-1 homolog isoform 2 [Homo sapiens].
ACCESSION   NP_001362886 XP_005251703
VERSION     NP_001362886.1
DBSOURCE    REFSEQ: accession NM_001375957.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Yan,X., Li,Y., Wang,G., Zhou,Z., Song,G., Feng,Q., Zhao,Y., Mi,W.,
            Ma,Z. and Dong,C.
  TITLE     Molecular basis for recognition of Gly/N-degrons by CRL2ZYG11B and
            CRL2ZER1
  JOURNAL   Mol Cell 81 (16), 3262-3274 (2021)
   PUBMED   34214466
  REMARK    GeneRIF: Molecular basis for recognition of Gly/N-degrons by
            CRL2(ZYG11B) and CRL2(ZER1).
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Timms,R.T., Zhang,Z., Rhee,D.Y., Harper,J.W., Koren,I. and
            Elledge,S.J.
  TITLE     A glycine-specific N-degron pathway mediates the quality control of
            protein N-myristoylation
  JOURNAL   Science 365 (6448) (2019)
   PUBMED   31273098
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Wade,T.D., Gordon,S., Medland,S., Bulik,C.M., Heath,A.C.,
            Montgomery,G.W. and Martin,N.G.
  TITLE     Genetic variants associated with disordered eating
  JOURNAL   Int J Eat Disord 46 (6), 594-608 (2013)
   PUBMED   23568457
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Cheng,C.Y., Schache,M., Ikram,M.K., Young,T.L., Guggenheim,J.A.,
            Vitart,V., MacGregor,S., Verhoeven,V.J., Barathi,V.A., Liao,J.,
            Hysi,P.G., Bailey-Wilson,J.E., St Pourcain,B., Kemp,J.P.,
            McMahon,G., Timpson,N.J., Evans,D.M., Montgomery,G.W., Mishra,A.,
            Wang,Y.X., Wang,J.J., Rochtchina,E., Polasek,O., Wright,A.F.,
            Amin,N., van Leeuwen,E.M., Wilson,J.F., Pennell,C.E., van
            Duijn,C.M., de Jong,P.T., Vingerling,J.R., Zhou,X., Chen,P., Li,R.,
            Tay,W.T., Zheng,Y., Chew,M., Burdon,K.P., Craig,J.E., Iyengar,S.K.,
            Igo,R.P. Jr., Lass,J.H. Jr., Chew,E.Y., Haller,T., Mihailov,E.,
            Metspalu,A., Wedenoja,J., Simpson,C.L., Wojciechowski,R., Hohn,R.,
            Mirshahi,A., Zeller,T., Pfeiffer,N., Lackner,K.J., Bettecken,T.,
            Meitinger,T., Oexle,K., Pirastu,M., Portas,L., Nag,A.,
            Williams,K.M., Yonova-Doing,E., Klein,R., Klein,B.E.,
            Hosseini,S.M., Paterson,A.D., Makela,K.M., Lehtimaki,T.,
            Kahonen,M., Raitakari,O., Yoshimura,N., Matsuda,F., Chen,L.J.,
            Pang,C.P., Yip,S.P., Yap,M.K., Meguro,A., Mizuki,N., Inoko,H.,
            Foster,P.J., Zhao,J.H., Vithana,E., Tai,E.S., Fan,Q., Xu,L.,
            Campbell,H., Fleck,B., Rudan,I., Aung,T., Hofman,A.,
            Uitterlinden,A.G., Bencic,G., Khor,C.C., Forward,H., Parssinen,O.,
            Mitchell,P., Rivadeneira,F., Hewitt,A.W., Williams,C., Oostra,B.A.,
            Teo,Y.Y., Hammond,C.J., Stambolian,D., Mackey,D.A., Klaver,C.C.,
            Wong,T.Y., Saw,S.M. and Baird,P.N.
  CONSRTM   Consortium for Refractive Error and Myopia; Fuchs' Genetics
            Multi-Center Study Group; Wellcome Trust Case Control Consortium 2;
            Diabetes Control and Complications Trial/Epidemiology of Diabetes
            Interventions, and Complications Research Group
  TITLE     Nine loci for ocular axial length identified through genome-wide
            association studies, including shared loci with refractive error
  JOURNAL   Am J Hum Genet 93 (2), 264-277 (2013)
   PUBMED   24144296
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Okumura,F., Matsuzaki,M., Nakatsukasa,K. and Kamura,T.
  TITLE     The Role of Elongin BC-Containing Ubiquitin Ligases
  JOURNAL   Front Oncol 2, 10 (2012)
   PUBMED   22649776
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 764)
  AUTHORS   Vasudevan,S., Starostina,N.G. and Kipreos,E.T.
  TITLE     The Caenorhabditis elegans cell-cycle regulator ZYG-11 defines a
            conserved family of CUL-2 complex components
  JOURNAL   EMBO Rep 8 (3), 279-286 (2007)
   PUBMED   17304241
REFERENCE   8  (residues 1 to 764)
  AUTHORS   Feral,C., Wu,Y.Q., Pawlak,A. and Guellaen,G.
  TITLE     Meiotic human sperm cells express a leucine-rich homologue of
            Caenorhabditis elegans early embryogenesis gene, Zyg-11
  JOURNAL   Mol Hum Reprod 7 (12), 1115-1122 (2001)
   PUBMED   11719588
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL441992.17.
            
            On Nov 7, 2019 this sequence version replaced XP_005251703.1.
            
            Summary: This gene encodes a subunit of an E3 ubiquitin ligase
            complex that may be involved in meiosis. The encoded protein
            contains three leucine-rich repeat motifs. [provided by RefSeq, Nov
            2012].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14478891.252713.1,
                                           SRR11853559.32691.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..764
                     /product="protein zer-1 homolog isoform 2"
                     /note="ZYG homolog; protein zer-1 homolog; zyg-11 homolog
                     B-like protein; zyg11b-like protein"
                     /calculated_mol_wt=87839
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          82..104
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          105..130
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          131..176
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          177..200
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          201..223
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          224..247
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          226..245
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          246..268
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          278..302
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          281..324
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          509..554
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Site            order(543,547,551,587,591,595,628,634,638)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          556..598
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          560..598
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          600..641
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     Region          603..639
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          712..754
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7L7.1)"
     CDS             1..764
                     /gene="ZER1"
                     /gene_synonym="C9orf60; ZYG; ZYG11BL"
                     /coded_by="NM_001375957.1:442..2736"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:10444"
                     /db_xref="HGNC:HGNC:30960"
                     /db_xref="MIM:617764"
ORIGIN      
        1 masdtpeslm alctdfclrn ldgtlgylld ketlrlhpdi flpseicdrl vneyvelvna
       61 acnfephesf fslfsdprst rltrihlred lvqdqdleai rkqdlvelyl tnceklsaks
      121 lqtlrsfsht lvslslfgct nifyeeenpg gcedeylvnp tcqvlvkdft fegfsrlrfl
      181 nlgrmidwvp vesllrplns laaldlsgiq tsdaafltqw kdslvslvly nmdlsddhir
      241 vivqlhklrh ldisrdrlss yykfkltrev lslfvqklgn lmsldisghm ilencsiskm
      301 eeeagqtsie pskssiipfr alkrplqflg lfenslcrlt hipaykvsgd kneeqvlnai
      361 eaytehrpei tsrainllfd iariercnql lralklvita lkchkydrni qvtgsaalfy
      421 ltnseyrseq svklrrqviq vvlngmesyq evqrnccltl cnfsipeele fqyrrvnell
      481 lsilnptrqd esiqriavhl cnalvcqvdn dhkeavgkmg fvvtmlkliq kklldktcdq
      541 vmefswsalw nitdetpdnc emflnfngmk lfldclkefp ekqelhrnml gllgnvaevk
      601 elrpqlmtsq fisvfsnlle skadgievsy nacgvlshim fdgpeawgvc epqreeveer
      661 mwaaiqswdi nsrrninyrs fepilrllpq gispvsqhwa twalynlvsv ypdkycplli
      721 keggmpllrd iikmatarqe tkemarkvie hcsnfkeenm dtsr
//
LOCUS       NP_665799                427 aa            linear   PRI 21-NOV-2025
DEFINITION  septin-6 isoform A [Homo sapiens].
ACCESSION   NP_665799
VERSION     NP_665799.1
DBSOURCE    REFSEQ: accession NM_145800.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Fischer,M., Frank,D., Rosler,R., Johnsson,N. and Gronemeyer,T.
  TITLE     Biochemical Characterization of a Human Septin Octamer
  JOURNAL   Front Cell Dev Biol 10, 771388 (2022)
   PUBMED   35309913
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Mendonca,D.C., Guimaraes,S.L., Pereira,H.D., Pinto,A.A., de
            Farias,M.A., de Godoy,A.S., Araujo,A.P.U., van Heel,M.,
            Portugal,R.V. and Garratt,R.C.
  TITLE     An atomic model for the human septin hexamer by cryo-EM
  JOURNAL   J Mol Biol 433 (15), 167096 (2021)
   PUBMED   34116125
  REMARK    GeneRIF: An atomic model for the human septin hexamer by cryo-EM.
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Sheffield,P.J., Oliver,C.J., Kremer,B.E., Sheng,S., Shao,Z. and
            Macara,I.G.
  TITLE     Borg/septin interactions and the assembly of mammalian septin
            heterodimers, trimers, and filaments
  JOURNAL   J Biol Chem 278 (5), 3483-3488 (2003)
   PUBMED   12446710
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Surka,M.C., Tsang,C.W. and Trimble,W.S.
  TITLE     The mammalian septin MSF localizes with microtubules and is
            required for completion of cytokinesis
  JOURNAL   Mol Biol Cell 13 (10), 3532-3545 (2002)
   PUBMED   12388755
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Slater,D.J., Hilgenfeld,E., Rappaport,E.F., Shah,N., Meek,R.G.,
            Williams,W.R., Lovett,B.D., Osheroff,N., Autar,R.S., Ried,T. and
            Felix,C.A.
  TITLE     MLL-SEPTIN6 fusion recurs in novel translocation of chromosomes 3,
            X, and 11 in infant acute myelomonocytic leukaemia and in t(X;11)
            in infant acute myeloid leukaemia, and MLL genomic breakpoint in
            complex MLL-SEPTIN6 rearrangement is a DNA topoisomerase II
            cleavage site
  JOURNAL   Oncogene 21 (30), 4706-4714 (2002)
   PUBMED   12096348
  REMARK    GeneRIF: MLL-SEPTIN6 fusion recurs in novel translocation of
            chromosomes 3, X, and 11 in infant acute myelomonocytic leukaemia
            and in t(X;11) in infant acute myeloid leukaemia
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Ono,R., Taki,T., Taketani,T., Kawaguchi,H., Taniwaki,M.,
            Okamura,T., Kawa,K., Hanada,R., Kobayashi,M. and Hayashi,Y.
  TITLE     SEPTIN6, a human homologue to mouse Septin6, is fused to MLL in
            infant acute myeloid leukemia with complex chromosomal
            abnormalities involving 11q23 and Xq24
  JOURNAL   Cancer Res 62 (2), 333-337 (2002)
   PUBMED   11809673
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Kinoshita,A., Noda,M. and Kinoshita,M.
  TITLE     Differential localization of septins in the mouse brain
  JOURNAL   J Comp Neurol 428 (2), 223-239 (2000)
   PUBMED   11064363
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005052.2, AL355348.28 and
            AC004913.2.
            
            Summary: This gene is a member of the septin family of GTPases.
            Members of this family are required for cytokinesis. One version of
            pediatric acute myeloid leukemia is the result of a reciprocal
            translocation between chromosomes 11 and X, with the breakpoint
            associated with the genes encoding the mixed-lineage leukemia and
            septin 2 proteins. This gene encodes four transcript variants
            encoding three distinct isoforms. An additional transcript variant
            has been identified, but its biological validity has not been
            determined. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (III) contains an alternate 3'
            sequence, as compared to variant II. The resulting isoform (A) is
            truncated at the C-terminus, as compared to isoform B.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026589.1, SRR14038191.2739344.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq24"
     Protein         1..427
                     /product="septin-6 isoform A"
                     /note="septin 2"
                     /calculated_mol_wt=48742
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:12665801,
                     ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q14141.4)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14141.4)"
     Region          39..307
                     /region_name="CDC_Septin"
                     /note="CDC/Septin GTPase family; cd01850"
                     /db_xref="CDD:206649"
     Region          49..56
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14141.4)"
     Site            49..56
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206649"
     Site            order(51..57,101,104,184..185,187,239..240)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206649"
     Site            76..84
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206649"
     Site            78
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206649"
     Region          101..104
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14141.4)"
     Site            101..104
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            order(103..139,141..150)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Region          184..187
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14141.4)"
     Site            184..187
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            239..241
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     Site            367
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14141.4)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14141.4)"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14141.4)"
     CDS             1..427
                     /gene="SEPTIN6"
                     /gene_synonym="SEP2; SEPT2; SEPT6; Septin-6"
                     /coded_by="NM_145800.4:64..1347"
                     /note="isoform A is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS14585.1"
                     /db_xref="GeneID:23157"
                     /db_xref="HGNC:HGNC:15848"
                     /db_xref="MIM:300683"
ORIGIN      
        1 maatdiarqv gegcrtvpla ghvgfdslpd qlvnksvsqg fcfnilcvge tglgkstlmd
       61 tlfntkfege pathtqpgvq lqsntydlqe snvrlkltiv stvgfgdqin kedsykpive
      121 fidaqfeayl qeelkirrvl htyhdsrihv clyfiaptgh slksldlvtm kkldskvnii
      181 piiakadais kseltkfkik itselvsngv qiyqfptdde svaeingtmn ahlpfavigs
      241 teelkignkm mrarqypwgt vqveneahcd fvklremlir vnmedlreqt htrhyelyrr
      301 ckleemgfkd tdpdskpfsl qetyeakrne flgelqkkee emrqmfvqrv kekeaelkea
      361 ekelhekfdr lkklhqdekk kledkkksld devnafkqrk taaellqsqg sqaggsqtlk
      421 rdkekkn
//
LOCUS       NP_001303250             751 aa            linear   PRI 21-NOV-2025
DEFINITION  coiled-coil domain-containing protein 57 isoform 2 [Homo sapiens].
ACCESSION   NP_001303250 XP_005256402
VERSION     NP_001303250.1
DBSOURCE    REFSEQ: accession NM_001316321.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   2  (residues 1 to 751)
  AUTHORS   Gurkaslar,H.K., Culfa,E., Arslanhan,M.D., Lince-Faria,M. and
            Firat-Karalar,E.N.
  TITLE     CCDC57 Cooperates with Microtubules and Microcephaly Protein CEP63
            and Regulates Centriole Duplication and Mitotic Progression
  JOURNAL   Cell Rep 31 (6), 107630 (2020)
   PUBMED   32402286
  REMARK    GeneRIF: CCDC57 Cooperates with Microtubules and Microcephaly
            Protein CEP63 and Regulates Centriole Duplication and Mitotic
            Progression.
REFERENCE   3  (residues 1 to 751)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 751)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 751)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 751)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 751)
  AUTHORS   Shin,S.Y., Fauman,E.B., Petersen,A.K., Krumsiek,J., Santos,R.,
            Huang,J., Arnold,M., Erte,I., Forgetta,V., Yang,T.P., Walter,K.,
            Menni,C., Chen,L., Vasquez,L., Valdes,A.M., Hyde,C.L., Wang,V.,
            Ziemek,D., Roberts,P., Xi,L., Grundberg,E., Waldenberger,M.,
            Richards,J.B., Mohney,R.P., Milburn,M.V., John,S.L., Trimmer,J.,
            Theis,F.J., Overington,J.P., Suhre,K., Brosnan,M.J., Gieger,C.,
            Kastenmuller,G., Spector,T.D. and Soranzo,N.
  CONSRTM   Multiple Tissue Human Expression Resource (MuTHER) Consortium
  TITLE     An atlas of genetic influences on human blood metabolites
  JOURNAL   Nat Genet 46 (6), 543-550 (2014)
   PUBMED   24816252
REFERENCE   8  (residues 1 to 751)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   9  (residues 1 to 751)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 751)
  AUTHORS   Ozyildirim,A.M., Wistow,G.J., Gao,J., Wang,J., Dickinson,D.P.,
            Frierson,H.F. Jr. and Laurie,G.W.
  TITLE     The lacrimal gland transcriptome is an unusually rich source of
            rare and poorly characterized gene transcripts
  JOURNAL   Invest Ophthalmol Vis Sci 46 (5), 1572-1580 (2005)
   PUBMED   15851553
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC132872.17, HY095706.1, BC040264.1, AC129510.15 and AF007146.1.
            
            On Oct 14, 2015 this sequence version replaced XP_005256402.1.
            
            Transcript Variant: This variant (2) uses an alternate exon in the
            5' UTR, lacks several 3' exons and has a 3' end that extends into
            an intron compared to variant 1. The resulting isoform (3) has a
            shorter and distinct C-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC040264.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..751
                     /product="coiled-coil domain-containing protein 57 isoform
                     2"
                     /EC_number="4.2.1.59"
                     /note="coiled-coil domain-containing protein 57"
                     /calculated_mol_wt=85334
     Region          1..502
                     /region_name="Centrosomal targeting domain.
                     /evidence=ECO:0000269|PubMed:32402286"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAC2.3)"
     Region          <12..>558
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          555..574
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAC2.3)"
     Region          606..653
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAC2.3)"
     CDS             1..751
                     /gene="CCDC57"
                     /coded_by="NM_001316321.3:385..2640"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS11803.1"
                     /db_xref="GeneID:284001"
                     /db_xref="HGNC:HGNC:27564"
ORIGIN      
        1 mlplgsepal nelllrkeee wralqahrtq lqeaalqdtr sqleeaqgkl rclqedfvyn
       61 lqvleerdle lerydaafaq areweearra evselkieaa klrqalarea rkveelqqqq
      121 qlafqehrle lervhsdkng eidhhreqye nlkwtlerkl eeldgelalq rqelllefes
      181 kmrkrehefr lqadnmsnta lsrelkvkll hkelealkea gakaaeslqr aeatnaeler
      241 klqsragelq dleamsrarv kdledklhsv qltrkkeeet fkrkheeldr larekdavlv
      301 avkgahveql qelqtrvlel qahcetleaq lrraewrqad takekdaaid qlredastvk
      361 sawdaqiaql skemvsrdlq iqtlqeeevk lkaqvarsqq dierykqqls laverersle
      421 rdqvqlgldw qrrcddierd qiqksealiq glsmaksqva aklqeteqal qeqevvlkav
      481 tlerdqavqa lrmhglprpg aqmllrqhee eiskdfpsse iqrlreqnts lrnaiaqmrk
      541 emealshqip ppiqtaaest danqpdpeag gdaatpdyvl aleaeirtlk hkfktlekhl
      601 edvldplkms sphaesqpsv rtstettggs aqagqaggsv qagqaggsvq agpvssglal
      661 rklgdrvqll nllvtrlrqk vlreplepaa lqrelprevd qvhlevlelr kqvaelgkhl
      721 riaqhggaep sgrkqppasd avalgrevga r
//
LOCUS       NP_919436                736 aa            linear   PRI 21-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_919436
VERSION     NP_919436.1
DBSOURCE    REFSEQ: accession NM_194454.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (3) lacks 2 exons but has an
            alternate exon in the 5' UTR, as compared to variant 1. Variants
            1-4 encode the same isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3293575.1, AF310133.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394505.7/ ENSP00000378013.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..736
                     /product="krev interaction trapped protein 1 isoform 1"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=84217
     Region          1..170
                     /region_name="N-terminal domain similar to Nudix hydrolase
                     domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          172..195
                     /region_name="Interaction with ITGB1BP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          287..316
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          <291..>414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          291..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293..294,297..299,301..302,306,309,318,320,322,
                     326..327,330..332,334..335,339,342,352,354,356,360..361,
                     364..366,368..369,373,376)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          320..352
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          320..350
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          354..383
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          388..419
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          421..640
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          430..452
                     /region_name="Interaction with RAP1B.
                     /evidence=ECO:0000269|PubMed:22577140"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          636..735
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(650,669,671,677)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(681,686..689,723,727,730..731)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            723..734
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..736
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_194454.3:546..2756"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS5624.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkerqwvddf plhrsacegd
      301 sellsrllse rfsvnqldsd hwapihyacw ygkveatril lekgkcnpnl lngqlssplh
      361 faaggghaei vqillnhpet drhitdqqgr splniceenk qnnweeaakl lkeainkpye
      421 kvriyrmdgs yrsvelkhgn nttvqqimeg mrlsqetqqy ftiwicsenl slqlkpyhkp
      481 lqhvrdwpei laeltnldpq retpqlflrr dvrlplevek qiedplaili lfdearynll
      541 kgfytapdak litlaslllq ivygnyeskk hkqgflneen lksivpvtkl kskaphwtnr
      601 ilheyknlst segvskemhh lqrmflqncw eiptygaaff tgqiftkasp snhkvipvyv
      661 gvnikglhll nmetkallis lkygcfmwql gdtdtcfqih smenkmsfiv htkqaglvvk
      721 llmklngqlm pterns
//
LOCUS       NP_001128634             271 aa            linear   PRI 21-NOV-2025
DEFINITION  catechol O-methyltransferase isoform MB-COMT [Homo sapiens].
ACCESSION   NP_001128634
VERSION     NP_001128634.1
DBSOURCE    REFSEQ: accession NM_001135162.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Clelland,J.D., Hesson,H., Ramiah,K., Anderson,J., Thengampallil,A.,
            Girgis,R.R. and Clelland,C.L.
  TITLE     The relationship between COMT, proline, and negative symptoms in
            clinical high risk and recent psychosis onset
  JOURNAL   Transl Psychiatry 14 (1), 409 (2024)
   PUBMED   39358340
  REMARK    GeneRIF: The relationship between COMT, proline, and negative
            symptoms in clinical high risk and recent psychosis onset.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Happer,J.P., Beaton,L.E., Wagner,L.C., Hodgkinson,C.A., Goldman,D.
            and Marinkovic,K.
  TITLE     Neural indices of heritable impulsivity: Impact of the COMT
            Val158Met polymorphism on frontal beta power during early motor
            preparation
  JOURNAL   Biol Psychol 191, 108826 (2024)
   PUBMED   38862067
  REMARK    GeneRIF: Neural indices of heritable impulsivity: Impact of the
            COMT Val158Met polymorphism on frontal beta power during early
            motor preparation.
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Yousuf,F., Fatima,T., Rehman,R., Azam,I., Khan,S., Anis,M.,
            Mansha,R. and Khan,S.
  TITLE     Association of catechol-o-methyltransferase gene polymorphism with
            preeclampsia and biomarkers of oxidative stress: Study protocol for
            a prospective case-control study in Pakistan
  JOURNAL   PLoS One 19 (6), e0304314 (2024)
   PUBMED   38861573
  REMARK    GeneRIF: Association of catechol-o-methyltransferase gene
            polymorphism with preeclampsia and biomarkers of oxidative stress:
            Study protocol for a prospective case-control study in Pakistan.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Marjani,A., Poursharifi,N., Sajedi,A. and Tatari,M.
  TITLE     Age and Sex-related Chromogranin A Gene Polymorphisms and its
            Association with Metabolic Syndrome Components
  JOURNAL   J ASEAN Fed Endocr Soc 39 (1), 45-52 (2024)
   PUBMED   38863909
  REMARK    GeneRIF: Age and Sex-related Chromogranin A Gene Polymorphisms and
            its Association with Metabolic Syndrome Components.
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Grossman,M.H., Emanuel,B.S. and Budarf,M.L.
  TITLE     Chromosomal mapping of the human catechol-O-methyltransferase gene
            to 22q11.1----q11.2
  JOURNAL   Genomics 12 (4), 822-825 (1992)
   PUBMED   1572656
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Ulmanen,I. and Lundstrom,K.
  TITLE     Cell-free synthesis of rat and human catechol O-methyltransferase.
            Insertion of the membrane-bound form into microsomal membranes in
            vitro
  JOURNAL   Eur J Biochem 202 (3), 1013-1020 (1991)
   PUBMED   1765063
REFERENCE   8  (residues 1 to 271)
  AUTHORS   Lundstrom,K., Salminen,M., Jalanko,A., Savolainen,R. and Ulmanen,I.
  TITLE     Cloning and characterization of human placental
            catechol-O-methyltransferase cDNA
  JOURNAL   DNA Cell Biol 10 (3), 181-189 (1991)
   PUBMED   1707278
REFERENCE   9  (residues 1 to 271)
  AUTHORS   Bertocci,B., Miggiano,V., Da Prada,M., Dembic,Z., Lahm,H.W. and
            Malherbe,P.
  TITLE     Human catechol-O-methyltransferase: cloning and expression of the
            membrane-associated form
  JOURNAL   Proc Natl Acad Sci U S A 88 (4), 1416-1420 (1991)
   PUBMED   1847521
REFERENCE   10 (residues 1 to 271)
  AUTHORS   Schultz,E.
  TITLE     Catechol-O-methyltransferase and aromatic L-amino acid
            decarboxylase activities in human gastrointestinal tissues
  JOURNAL   Life Sci 49 (10), 721-725 (1991)
   PUBMED   1875781
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005663.2, BE728779.1 and
            AK290440.1.
            
            Summary: Catechol-O-methyltransferase catalyzes the transfer of a
            methyl group from S-adenosylmethionine to catecholamines, including
            the neurotransmitters dopamine, epinephrine, and norepinephrine.
            This O-methylation results in one of the major degradative pathways
            of the catecholamine transmitters. In addition to its role in the
            metabolism of endogenous substances, COMT is important in the
            metabolism of catechol drugs used in the treatment of hypertension,
            asthma, and Parkinson disease. COMT is found in two forms in
            tissues, a soluble form (S-COMT) and a membrane-bound form
            (MB-COMT). The differences between S-COMT and MB-COMT reside within
            the N-termini. Several transcript variants are formed through the
            use of alternative translation initiation sites and promoters.
            [provided by RefSeq, Sep 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, 3, and 5 all encode isoform MB-COMT
            and may also make the shorter isoform S-COMT at a low level.
            MB-COMT is a membrane-bound protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC100018.2, SRR5189652.6618.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..271
                     /product="catechol O-methyltransferase isoform MB-COMT"
                     /EC_number="2.1.1.6"
                     /note="epididymis secretory sperm binding protein Li 98n;
                     testicular tissue protein Li 42"
                     /calculated_mol_wt=29906
     Site            7..26
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21964.2)"
     Region          104..242
                     /region_name="TrmR"
                     /note="tRNA 5-hydroxyU34 O-methylase TrmR/YrrM
                     [Translation, ribosomal structure and biogenesis];
                     COG4122"
                     /db_xref="CDD:443298"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P22734; propagated from
                     UniProtKB/Swiss-Prot (P21964.2)"
     CDS             1..271
                     /gene="COMT"
                     /gene_synonym="HEL-S-98n"
                     /coded_by="NM_001135162.2:229..1044"
                     /note="isoform MB-COMT is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS13770.1"
                     /db_xref="GeneID:1312"
                     /db_xref="HGNC:HGNC:2228"
                     /db_xref="MIM:116790"
ORIGIN      
        1 mpeappllla avllglvllv vlllllrhwg wglcligwne filqpihnll mgdtkeqril
       61 nhvlqhaepg naqsvleaid tyceqkewam nvgdkkgkiv daviqehqps vllelgaycg
      121 ysavrmarll spgarlitie inpdcaaitq rmvdfagvkd kvtlvvgasq diipqlkkky
      181 dvdtldmvfl dhwkdrylpd tllleecgll rkgtvlladn vicpgapdfl ahvrgsscfe
      241 cthyqsfley revvdgleka iykgpgseag p
//
LOCUS       NP_001387152            1067 aa            linear   PRI 21-NOV-2025
DEFINITION  protein transport protein Sec31A isoform 6 [Homo sapiens].
ACCESSION   NP_001387152
VERSION     NP_001387152.1
DBSOURCE    REFSEQ: accession NM_001400223.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1067)
  AUTHORS   Tobias,E.S., Lucas-Herald,A.K., Sagar,D., Montezano,A.C.,
            Rios,F.J., De Lucca Camargo,L., Hamilton,G., Gazdagh,G.,
            Diver,L.A., Williams,N., Herzyk,P., Touyz,R.M., Greenfield,A.,
            McGowan,R. and Ahmed,S.F.
  TITLE     SEC31A may be associated with pituitary hormone deficiency and
            gonadal dysgenesis
  JOURNAL   Endocrine 84 (2), 345-349 (2024)
   PUBMED   38400880
  REMARK    GeneRIF: SEC31A may be associated with pituitary hormone deficiency
            and gonadal dysgenesis.
REFERENCE   2  (residues 1 to 1067)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1067)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1067)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1067)
  AUTHORS   Jin,L., Pahuja,K.B., Wickliffe,K.E., Gorur,A., Baumgartel,C.,
            Schekman,R. and Rape,M.
  TITLE     Ubiquitin-dependent regulation of COPII coat size and function
  JOURNAL   Nature 482 (7386), 495-500 (2012)
   PUBMED   22358839
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1067)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1067)
  AUTHORS   Kim,J.H., Hong,J.A., Pih,K.T. and Hwang,I.
  TITLE     Identification and isolation of differentially expressed genes in
            osmotically stressed human oral keratinocytes
  JOURNAL   Arch Oral Biol 46 (4), 335-341 (2001)
   PUBMED   11269867
REFERENCE   8  (residues 1 to 1067)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 1067)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   10 (residues 1 to 1067)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021105.13 and AC108469.5.
            
            Summary: The protein encoded by this gene shares similarity with
            the yeast Sec31 protein, and is a component of the outer layer of
            the coat protein complex II (COPII). The encoded protein is
            involved in vesicle budding from the endoplasmic reticulum (ER) and
            contains multiple WD repeats near the N-terminus and a proline-rich
            region in the C-terminal half. It associates with the protein
            encoded by the SEC13 homolog, nuclear pore and COPII coat complex
            component (SEC13), and is required for ER-Golgi transport.
            Monoubiquitylation of this protein by CUL3-KLHL12 was found to
            regulate the size of COPII coats to accommodate unusually shaped
            cargo. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853564.21135.1,
                                           SRR14038191.1643492.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1067
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..1067
                     /product="protein transport protein Sec31A isoform 6"
                     /note="yeast Sec31p homolog; protein transport protein
                     Sec31A; web1-like protein; SEC31 homolog A, COPII coat
                     complex component; SEC31-related protein A; SEC31-like
                     protein 1; SEC31 homolog A, COPII coating complex
                     component"
                     /calculated_mol_wt=117543
     Region          13..332
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(26,40,46..47,52..53,91,95,101..102,117,121,139,144,
                     150..151,164,185,190,196..197,209..210,231,235,244..245,
                     258..259,277,282,288..289,301..302,320,325,331..332)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          70..119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          125..162
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          172..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          263..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          306..331
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <534..>657
                     /region_name="ACE1-Sec16-like"
                     /note="Ancestral coatomer element 1 (ACE1) of COPII coat
                     complex assembly protein Sec16; cl14807"
                     /db_xref="CDD:449359"
     Site            order(535..539,541,543,554,556,557..558,560..561,565,571,
                     579,591,594,619..620)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187750"
     Region          <749..>962
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     CDS             1..1067
                     /gene="SEC31A"
                     /gene_synonym="ABP125; ABP130; HPBKS; HSPC275; HSPC334;
                     NEDSOSB; SEC31L1"
                     /coded_by="NM_001400223.1:68..3271"
                     /note="isoform 6 is encoded by transcript variant 57"
                     /db_xref="CCDS:CCDS75155.1"
                     /db_xref="GeneID:22872"
                     /db_xref="HGNC:HGNC:17052"
                     /db_xref="MIM:610257"
ORIGIN      
        1 mklkevdrta mqawspaqnh piylatgtsa qqldatfstn asleifeldl sdpsldmksc
       61 atfssshryh kliwgpykmd skgdvsgvli aggengniil ydpskiiagd kevviaqndk
      121 htgpvraldv nifqtnlvas ganeseiyiw dlnnfatpmt pgaktqpped isciawnrqv
      181 qhilasasps gratvwdlrk nepiikvsdh snrmhcsgla whpdvatqmv laseddrlpv
      241 iqmwdlrfas splrvlenha rgilaiawsm adpelllscg kdakilcsnp ntgevlyelp
      301 tntqwcfdiq wcprnpavls aasfdgrisv ysimggstdg lrqkqvdkls ssfgnldpfg
      361 tgqplpplqi pqqtaqhsiv lplkkppkwi rrpvgasfsf ggklvtfenv rmpshqgaeq
      421 qqqqhhvfis qvvtekefls rsdqlqqavq sqgfinycqk kidasqtefe knvwsflkvn
      481 feddsrgkyl ellgyrkedl gkkhikeeke eseflpssgg tfnisvsgdi dglitqallt
      541 gnfesavdlc lhdnrmadai ilaiaggqel lartqkkyfa ksqskitrli tavvmknwke
      601 ivescdlknw realaavlty akpdefsalc dllgtrlene gdsllqtqac lcyicagnve
      661 klvacwtkaq dgshplslqd liekvvilrk avqltqamdt stvgvllaak msqyanllaa
      721 qgsiaaalaf lpdntnqpni mqlrdrlcra qgepvaghes pkipyekqql pkgrpgpvag
      781 hhqmprvqtq qyyphgenpp ppgfimhgnv npnaagqlpt spghmhtqvp pypqpqrpqn
      841 gwndppalnr vpkkkkmpen fmppvpitsp imnplgdpqs qmlqqqpsap vplssqssfp
      901 qphlpggqpf hgvqqplgqt gmppsfskpn iegapgapig ntfqhvqslp tkkitkkpip
      961 dehlilkttf edliqrclss atdpqtkrkl ddaskrlefl ydklreqtls ptitsglhni
     1021 arsietrnys egltmhthiv stsnfsetsa fmpvlkvvlt qanklgv
//
LOCUS       NP_001128143             231 aa            linear   PRI 21-NOV-2025
DEFINITION  derlin-1 isoform b [Homo sapiens].
ACCESSION   NP_001128143
VERSION     NP_001128143.1
DBSOURCE    REFSEQ: accession NM_001134671.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Wang,T., Wang,D., Kuang,G., Gong,X., Zhang,L., Wan,J. and Li,K.
  TITLE     Derlin-1 promotes diet-induced non-alcoholic fatty liver disease
            via increasing RIPK3-mediated necroptosis
  JOURNAL   Free Radic Biol Med 217, 29-47 (2024)
   PUBMED   38522486
  REMARK    GeneRIF: Derlin-1 promotes diet-induced non-alcoholic fatty liver
            disease via increasing RIPK3-mediated necroptosis.
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Rao,B., Wang,Q., Yao,D., Xia,Y., Li,W., Xie,Y., Li,S., Cao,M.,
            Shen,Y., Qin,A., Zhao,J. and Cao,Y.
  TITLE     The cryo-EM structure of the human ERAD retrotranslocation complex
  JOURNAL   Sci Adv 9 (41), eadi5656 (2023)
   PUBMED   37831771
REFERENCE   3  (residues 1 to 231)
  AUTHORS   You,H., Wen,X., Wang,X., Zhu,C., Chen,H., Bu,L., Zhang,J. and Qu,S.
  TITLE     Derlin-1 ameliorates nonalcoholic hepatic steatosis by promoting
            ubiquitylation and degradation of FABP1
  JOURNAL   Free Radic Biol Med 207, 260-271 (2023)
   PUBMED   37499886
  REMARK    GeneRIF: Derlin-1 ameliorates nonalcoholic hepatic steatosis by
            promoting ubiquitylation and degradation of FABP1.
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Miyano,K., Okamoto,S., Kajikawa,M., Kiyohara,T., Kawai,C.,
            Yamauchi,A. and Kuribayashi,F.
  TITLE     Regulation of Derlin-1-mediated degradation of NADPH oxidase
            partner p22phox by thiol modification
  JOURNAL   Redox Biol 56, 102479 (2022)
   PUBMED   36122532
  REMARK    GeneRIF: Regulation of Derlin-1-mediated degradation of NADPH
            oxidase partner p22(phox) by thiol modification.
REFERENCE   5  (residues 1 to 231)
  AUTHORS   Schulze,A., Standera,S., Buerger,E., Kikkert,M., van Voorden,S.,
            Wiertz,E., Koning,F., Kloetzel,P.M. and Seeger,M.
  TITLE     The ubiquitin-domain protein HERP forms a complex with components
            of the endoplasmic reticulum associated degradation pathway
  JOURNAL   J Mol Biol 354 (5), 1021-1027 (2005)
   PUBMED   16289116
REFERENCE   6  (residues 1 to 231)
  AUTHORS   Ye,Y., Shibata,Y., Kikkert,M., van Voorden,S., Wiertz,E. and
            Rapoport,T.A.
  TITLE     Recruitment of the p97 ATPase and ubiquitin ligases to the site of
            retrotranslocation at the endoplasmic reticulum membrane
  JOURNAL   Proc Natl Acad Sci U S A 102 (40), 14132-14138 (2005)
   PUBMED   16186510
  REMARK    GeneRIF: Derlin-1 is part of a retrotranslocation channel that is
            associated with both the polyubiquitination and p97-ATPase
            machineries at the endoplasmic reticulum membrane.
REFERENCE   7  (residues 1 to 231)
  AUTHORS   Lilley,B.N. and Ploegh,H.L.
  TITLE     Multiprotein complexes that link dislocation, ubiquitination, and
            extraction of misfolded proteins from the endoplasmic reticulum
            membrane
  JOURNAL   Proc Natl Acad Sci U S A 102 (40), 14296-14301 (2005)
   PUBMED   16186509
REFERENCE   8  (residues 1 to 231)
  AUTHORS   Katiyar,S., Joshi,S. and Lennarz,W.J.
  TITLE     The retrotranslocation protein Derlin-1 binds peptide:N-glycanase
            to the endoplasmic reticulum
  JOURNAL   Mol Biol Cell 16 (10), 4584-4594 (2005)
   PUBMED   16055502
  REMARK    GeneRIF: Derlin-1 interacts with the N-terminal domain of PNGase
            via its cytosolic C-terminus. PNGase distributed in two
            populations; ER-associated and free in the cytosol, which suggests
            the deglycosylation process can proceed at either site
REFERENCE   9  (residues 1 to 231)
  AUTHORS   Ye,Y., Shibata,Y., Yun,C., Ron,D. and Rapoport,T.A.
  TITLE     A membrane protein complex mediates retro-translocation from the ER
            lumen into the cytosol
  JOURNAL   Nature 429 (6994), 841-847 (2004)
   PUBMED   15215856
  REMARK    GeneRIF: Derlin-1 interacts with US11, a virally encoded ER protein
            that specifically targets MHC class I heavy chains for export from
            the ER, as well as with VIMP, a novel membrane protein that
            recruits the p97 ATPase and its cofactor
REFERENCE   10 (residues 1 to 231)
  AUTHORS   Lilley,B.N. and Ploegh,H.L.
  TITLE     A membrane protein required for dislocation of misfolded proteins
            from the ER
  JOURNAL   Nature 429 (6994), 834-840 (2004)
   PUBMED   15215855
  REMARK    GeneRIF: Derlin-1 is an important factor for the extraction of
            certain aberrantly folded proteins from the mammalian ER
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA800358.1, DA906855.1,
            AK124086.1, AY358818.1, AK023846.1, AF131854.1 and AA976062.1.
            
            Summary: The protein encoded by this gene is a member of the derlin
            family. Members of this family participate in the ER-associated
            degradation response and retrotranslocate misfolded or unfolded
            proteins from the ER lumen to the cytosol for proteasomal
            degradation. This protein recognizes substrate in the ER and works
            in a complex to retrotranslocate it across the ER membrane into the
            cytosol. This protein may select cystic fibrosis transmembrane
            conductance regulator protein (CFTR) for degradation as well as
            unfolded proteins in Alzheimer's disease. Alternative splicing
            results in multiple transcript variants that encode different
            protein isoforms. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.193719.1, AK124086.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..231
                     /product="derlin-1 isoform b"
                     /note="DERtrin-1; degradation in endoplasmic reticulum
                     protein 1; Der1-like domain family, member 1"
                     /calculated_mol_wt=26292
     Region          11..184
                     /region_name="DER1"
                     /note="Der1-like family; pfam04511"
                     /db_xref="CDD:427988"
     CDS             1..231
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /coded_by="NM_001134671.3:181..876"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47915.1"
                     /db_xref="GeneID:79139"
                     /db_xref="HGNC:HGNC:28454"
                     /db_xref="MIM:608813"
ORIGIN      
        1 msdigdwfrs ipaitrywfa atvavplvgk lglispaylf lwpeaflyrf qiwrpitatf
       61 yfpvgpgtgf lylvnlyfly qystrletga fdgrpadylf mllfnwiciv itglamdmql
      121 lmiplimsvl yvwaqlnrdm ivsfwfgtrf kacylpwvil gfnyiiggsy pmdlggrnfl
      181 stpqflyrwl psrrggvsgf gvppasmrra adqnggggrh nwgqgfrlgd q
//
LOCUS       NP_001259034             341 aa            linear   PRI 21-NOV-2025
DEFINITION  membrane progestin receptor delta isoform 3 [Homo sapiens].
ACCESSION   NP_001259034
VERSION     NP_001259034.1
DBSOURCE    REFSEQ: accession NM_001272105.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Yang,M., Li,J.C., Tao,C., Wu,S., Liu,B., Shu,Q., Li,B. and Zhu,R.
  TITLE     PAQR6 Upregulation Is Associated with AR Signaling and Unfavorite
            Prognosis in Prostate Cancers
  JOURNAL   Biomolecules 11 (9), 1383 (2021)
   PUBMED   34572596
  REMARK    GeneRIF: PAQR6 Upregulation Is Associated with AR Signaling and
            Unfavorite Prognosis in Prostate Cancers.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Huang,X., Dai,F.F., Gaisano,G., Giglou,K., Han,J., Zhang,M.,
            Kittanakom,S., Wong,V., Wei,L., Showalter,A.D., Sloop,K.W.,
            Stagljar,I. and Wheeler,M.B.
  TITLE     The identification of novel proteins that interact with the GLP-1
            receptor and restrain its activity
  JOURNAL   Mol Endocrinol 27 (9), 1550-1563 (2013)
   PUBMED   23864651
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Pang,Y., Dong,J. and Thomas,P.
  TITLE     Characterization, neurosteroid binding and brain distribution of
            human membrane progesterone receptors delta and {epsilon} (mPRdelta
            and mPR{epsilon}) and mPRdelta involvement in neurosteroid
            inhibition of apoptosis
  JOURNAL   Endocrinology 154 (1), 283-295 (2013)
   PUBMED   23161870
  REMARK    GeneRIF: The results suggest that PAQR6 and PAQR9 (mPRdelta and
            mPRepsilon) function as mPRs coupled to G proteins and are
            potential intermediaries of nonclassical antiapoptotic actions of
            neurosteroids in the central nervous system.
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Kamatani,Y., Matsuda,K., Okada,Y., Kubo,M., Hosono,N., Daigo,Y.,
            Nakamura,Y. and Kamatani,N.
  TITLE     Genome-wide association study of hematological and biochemical
            traits in a Japanese population
  JOURNAL   Nat Genet 42 (3), 210-215 (2010)
   PUBMED   20139978
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Smith,J.L., Kupchak,B.R., Garitaonandia,I., Hoang,L.K., Maina,A.S.,
            Regalla,L.M. and Lyons,T.J.
  TITLE     Heterologous expression of human mPRalpha, mPRbeta and mPRgamma in
            yeast confirms their ability to function as membrane progesterone
            receptors
  JOURNAL   Steroids 73 (11), 1160-1173 (2008)
   PUBMED   18603275
  REMARK    GeneRIF: PAQR6 is a previously uncharacterized PAQR which is also
            capable of responding to progesterone.
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Tang,Y.T., Hu,T., Arterburn,M., Boyle,B., Bright,J.M., Emtage,P.C.
            and Funk,W.D.
  TITLE     PAQR proteins: a novel membrane receptor family defined by an
            ancient 7-transmembrane pass motif
  JOURNAL   J Mol Evol 61 (3), 372-380 (2005)
   PUBMED   16044242
REFERENCE   9  (residues 1 to 341)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK316034.1, DT218672.1, AF455047.1, AA310453.1 and AL135927.14.
            
            Transcript Variant: This variant (4) differs in the 5' UTR, uses
            alternate splice sites in the coding region and initiates
            translation at an alternate start codon, compared to variant 1. The
            resulting isoform (3) has distinct N- and C-termini and is shorter,
            compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK316034.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..341
                     /product="membrane progestin receptor delta isoform 3"
                     /note="mPR delta; membrane progesterone receptor delta;
                     progestin and adipoQ receptor family member VI; membrane
                     progesterone P4 receptor delta; progesterone and adipoQ
                     receptor family member 6; membrane progestin receptor
                     delta"
                     /calculated_mol_wt=37506
     Region          40..269
                     /region_name="HlyIII"
                     /note="Haemolysin-III related; pfam03006"
                     /db_xref="CDD:427098"
     Site            49..69
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TCH4.2)"
     Site            81..101
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TCH4.2)"
     Site            111..131
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TCH4.2)"
     Site            145..165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TCH4.2)"
     Site            215..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TCH4.2)"
     Site            256..276
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TCH4.2)"
     Site            290..310
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TCH4.2)"
     CDS             1..341
                     /gene="PAQR6"
                     /gene_synonym="PRdelta"
                     /coded_by="NM_001272105.2:249..1274"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS60301.1"
                     /db_xref="GeneID:79957"
                     /db_xref="HGNC:HGNC:30132"
                     /db_xref="MIM:614579"
ORIGIN      
        1 mlslklpqll qvhqvfwedg imsgyrrpts saldcvlssf qmtnetvniw thflptwyfl
       61 wrllalaggp gfraepyhwp llvfllpacl ypfasccaht fssmsprmrh icyfldygal
      121 slyslgcafp yaaysmpasw lhghlhqffv paaalnsflc tglscysrfl elespglskv
      181 lrtgafaypf lfdnlplfyr lglcwgrghg cgqealstsh gyhlfcallt gflfashlpe
      241 rlapgrfdyi ghshqlfhic avlgthfqle avladmgsrr awlatqepal glagtvatlv
      301 laaagnllii aaftatllra pstcpllqgg pleggtqakq q
//
LOCUS       NP_001276898             410 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2B catalytic subunit beta
            isoform isoform e [Homo sapiens].
ACCESSION   NP_001276898
VERSION     NP_001276898.1
DBSOURCE    REFSEQ: accession NM_001289969.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Gazzeri,S., Zubchuk,N., Montaudon,E., Nemati,F., Huot-Marchand,S.,
            Berardi,G., Pucciarelli,A., Dib,Y., Nerini,D., Oddou,C., Pezet,M.,
            David-Boudet,L., Ardin,C., de Fraipont,F., Maraver,A., Girard,N.,
            Decaudin,D., Toffart,A.C. and Eymin,B.
  TITLE     PPP3CB overexpression mediates EGFR TKI resistance in lung tumors
            via calcineurin/MEK/ERK signaling
  JOURNAL   Life Sci Alliance 7 (12), e202402873 (2024)
   PUBMED   39353739
  REMARK    GeneRIF: PPP3CB overexpression mediates EGFR TKI resistance in lung
            tumors via calcineurin/MEK/ERK signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Zhang,Z., Chen,C., Yang,F., Zeng,Y.X., Sun,P., Liu,P. and Li,X.
  TITLE     Itaconate is a lysosomal inducer that promotes antibacterial innate
            immunity
  JOURNAL   Mol Cell 82 (15), 2844-2857 (2022)
   PUBMED   35662396
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Miyata,H., Oura,S., Morohoshi,A., Shimada,K., Mashiko,D., Oyama,Y.,
            Kaneda,Y., Matsumura,T., Abbasi,F. and Ikawa,M.
  TITLE     SPATA33 localizes calcineurin to the mitochondria and regulates
            sperm motility in mice
  JOURNAL   Proc Natl Acad Sci U S A 118 (35) (2021)
   PUBMED   34446558
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Chen,M.X., Chen,Y.H. and Cohen,P.T.
  TITLE     Polymerase chain reactions using Saccharomyces, Drosophila and
            human DNA predict a large family of protein serine/threonine
            phosphatases
  JOURNAL   FEBS Lett 306 (1), 54-58 (1992)
   PUBMED   1321058
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Giri,P.R., Higuchi,S. and Kincaid,R.L.
  TITLE     Chromosomal mapping of the human genes for the calmodulin-dependent
            protein phosphatase (calcineurin) catalytic subunit
  JOURNAL   Biochem Biophys Res Commun 181 (1), 252-258 (1991)
   PUBMED   1659808
REFERENCE   8  (residues 1 to 410)
  AUTHORS   McPartlin,A.E., Barker,H.M. and Cohen,P.T.
  TITLE     Identification of a third alternatively spliced cDNA encoding the
            catalytic subunit of protein phosphatase 2B beta
  JOURNAL   Biochim Biophys Acta 1088 (2), 308-310 (1991)
   PUBMED   1848109
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Guerini,D. and Klee,C.B.
  TITLE     Cloning of human calcineurin A: evidence for two isozymes and
            identification of a polyproline structural domain
  JOURNAL   Proc Natl Acad Sci U S A 86 (23), 9183-9187 (1989)
   PUBMED   2556704
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Guerini,D., Krinks,M.H., Sikela,J.M., Hahn,W.E. and Klee,C.B.
  TITLE     Isolation and sequence of a cDNA clone for human calcineurin B, the
            Ca2+-binding subunit of the Ca2+/calmodulin-stimulated protein
            phosphatase
  JOURNAL   DNA 8 (9), 675-682 (1989)
   PUBMED   2558868
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB479220.1, AK301582.1, AL359074.12, M29550.1 and CA429703.1.
            
            Transcript Variant: This variant (5) has multiple differences in
            the coding region, one of which results in a frameshift and early
            stop codon, compared to variant 1. The resulting protein (isoform
            e) has a distinct C-terminus and is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038193.3514217.1,
                                    SRR14038194.2171653.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..410
                     /product="serine/threonine-protein phosphatase 2B
                     catalytic subunit beta isoform isoform e"
                     /EC_number="3.1.3.16"
                     /note="calcineurin A beta; CAM-PRP catalytic subunit;
                     calcineurin A2; protein phosphatase 3, catalytic subunit,
                     beta isozyme; protein phosphatase from PCR fragment H32;
                     CNA beta"
                     /calculated_mol_wt=46567
     Region          1..268
                     /region_name="MPP_PP2B"
                     /note="PP2B, metallophosphatase domain; cd07416"
                     /db_xref="CDD:277361"
     Site            order(13,15,41,73,82,122,204,237,264)
                     /site_type="other"
                     /note="CN-CyPA-CsA complex [polypeptide binding]"
                     /db_xref="CDD:277361"
     Site            order(13,15,41,45,73..74,122,155,177,204,206)
                     /site_type="active"
                     /db_xref="CDD:277361"
     Site            order(13,15,41,73,122,204)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277361"
     CDS             1..410
                     /gene="PPP3CB"
                     /gene_synonym="CALNA2; CALNB; CNA2; PP2Bbeta"
                     /coded_by="NM_001289969.2:513..1745"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="GeneID:5532"
                     /db_xref="HGNC:HGNC:9315"
                     /db_xref="MIM:114106"
ORIGIN      
        1 mieveapitv cgdihgqffd lmklfevggs pantrylflg dyvdrgyfsi ecvlylwvlk
       61 ilypstlfll rgnhecrhlt eyftfkqeck ikyservyea cmeafdslpl aallnqqflc
      121 vhgglspeih tlddirrldr fkeppafgpm cdllwsdpse dfgneksqeh fshntvrgcs
      181 yfynypavce flqnnnllsi iraheaqdag yrmyrksqtt gfpslitifs apnyldvynn
      241 kaavlkyenn vmnirqfncs phpywlpnfm dvftwslpfv gekvtemlvn vlsicsddel
      301 mtegedqfdg saaarkeiir nkiraigkma rvfsvlrees esvltlkglt ptgmlpsgvl
      361 aggrqtlqsg ndvmqlavpq mdwgtphsfa nnshnacref llffssclss
//
LOCUS       NP_001364901             819 aa            linear   PRI 21-NOV-2025
DEFINITION  disks large homolog 2 isoform 15 [Homo sapiens].
ACCESSION   NP_001364901 XP_005273868
VERSION     NP_001364901.1
DBSOURCE    REFSEQ: accession NM_001377972.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Li,H., Zhu,J., Liu,X., Liu,L., Huang,S., Wu,A., Xu,Z., Zhang,X.,
            Li,Z., Ni,F., Liu,L. and Dong,J.
  TITLE     Glioma stem cell-derived exosomes induce the transformation of
            astrocytes via the miR-3065-5p/DLG2 signaling axis
  JOURNAL   Glia 72 (5), 857-871 (2024)
   PUBMED   38234042
  REMARK    GeneRIF: Glioma stem cell-derived exosomes induce the
            transformation of astrocytes via the miR-3065-5p/DLG2 signaling
            axis.
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Chen,Y., Karaca,E., Robin,N.H., Goodloe,D., Al-Beshri,A.,
            Dean,S.J., Hurst,A.C.E., Carroll,A.J. and Mikhail,F.M.
  TITLE     DLG2 intragenic exonic deletions reinforce the link to
            neurodevelopmental disorders and suggest a potential association
            with congenital anomalies and dysmorphism
  JOURNAL   Genet Med 26 (1), 101010 (2024)
   PUBMED   37860969
  REMARK    GeneRIF: DLG2 intragenic exonic deletions reinforce the link to
            neurodevelopmental disorders and suggest a potential association
            with congenital anomalies and dysmorphism.
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 819)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 819)
  AUTHORS   Stathakis,D.G., Lee,D. and Bryant,P.J.
  TITLE     Fine-scale physical map of the 11q21 region surrounding the human
            DLG2 locus, the gene encoding Chapsyn-110
  JOURNAL   Genomics 54 (1), 186-188 (1998)
   PUBMED   9806853
REFERENCE   6  (residues 1 to 819)
  AUTHORS   Irie,M., Hata,Y., Takeuchi,M., Ichtchenko,K., Toyoda,A., Hirao,K.,
            Takai,Y., Rosahl,T.W. and Sudhof,T.C.
  TITLE     Binding of neuroligins to PSD-95
  JOURNAL   Science 277 (5331), 1511-1515 (1997)
   PUBMED   9278515
REFERENCE   7  (residues 1 to 819)
  AUTHORS   Hsueh,Y.P., Kim,E. and Sheng,M.
  TITLE     Disulfide-linked head-to-head multimerization in the mechanism of
            ion channel clustering by PSD-95
  JOURNAL   Neuron 18 (5), 803-814 (1997)
   PUBMED   9182804
REFERENCE   8  (residues 1 to 819)
  AUTHORS   Kim,E., Cho,K.O., Rothschild,A. and Sheng,M.
  TITLE     Heteromultimerization and NMDA receptor-clustering activity of
            Chapsyn-110, a member of the PSD-95 family of proteins
  JOURNAL   Neuron 17 (1), 103-113 (1996)
   PUBMED   8755482
REFERENCE   9  (residues 1 to 819)
  AUTHORS   Brenman,J.E., Chao,D.S., Gee,S.H., McGee,A.W., Craven,S.E.,
            Santillano,D.R., Wu,Z., Huang,F., Xia,H., Peters,M.F.,
            Froehner,S.C. and Bredt,D.S.
  TITLE     Interaction of nitric oxide synthase with the postsynaptic density
            protein PSD-95 and alpha1-syntrophin mediated by PDZ domains
  JOURNAL   Cell 84 (5), 757-767 (1996)
   PUBMED   8625413
REFERENCE   10 (residues 1 to 819)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003305.2, AP002797.3,
            AC023118.4, AP002751.3, AP002370.5, AP000773.4 and AP003026.2.
            
            On Jan 23, 2020 this sequence version replaced XP_005273868.1.
            
            Summary: This gene encodes a member of the membrane-associated
            guanylate kinase (MAGUK) family. The encoded protein forms a
            heterodimer with a related family member that may interact at
            postsynaptic sites to form a multimeric scaffold for the clustering
            of receptors, ion channels, and associated signaling proteins.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. Additional transcript variants have been
            described, but their full-length nature is not known. [provided by
            RefSeq, Dec 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.265170.1, AK294375.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.1"
     Protein         1..819
                     /product="disks large homolog 2 isoform 15"
                     /note="channel-associated protein of synapses, 110kDa;
                     postsynaptic density protein PSD-93; channel-associated
                     protein of synapse-110; discs, large homolog 2,
                     chapsyn-110; protein phosphatase 1, regulatory subunit 58;
                     disks large homolog 2"
                     /calculated_mol_wt=91014
     Region          <35..64
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          63..151
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(74..80,97,100,130,134,137..138)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          160..244
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(169..175,192,195,225,229,232..233)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          245..312
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          385..475
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(397..403,414,417,447,451,454..455)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          501..574
                     /region_name="SH3_DLG2"
                     /note="Src Homology 3 domain of Disks Large homolog 2;
                     cd12032"
                     /db_xref="CDD:212965"
     Site            order(509,531..532)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212965"
     Site            order(512,514,517,526,544..545,564,566..567)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212965"
     Region          628..806
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..819
                     /gene="DLG2"
                     /gene_synonym="chapsyn-110; PPP1R58; PSD-93; PSD93"
                     /coded_by="NM_001377972.1:26..2485"
                     /note="isoform 15 is encoded by transcript variant 15"
                     /db_xref="GeneID:1740"
                     /db_xref="HGNC:HGNC:2901"
                     /db_xref="MIM:603583"
ORIGIN      
        1 mqrpsvsrae nyqllwdtia slkqceqamq hafipaspap iivntdtldt ipyvngteie
       61 yefeeitler gnsglgfsia ggtdnphigd dpgifitkii pggaaaedgr lrvndcilrv
      121 nevdvsevsh skavealkea gsivrlyvrr rrpiletvve iklfkgpkgl gfsiaggvgn
      181 qhipgdnsiy vtkiidggaa qkdgrlqvgd rllmvnnysl eevtheeava ilkntsevvy
      241 lkvgkpttiy mtdpygppdi thsysppmen hllsgnngtl eyktslppis pgryspipkh
      301 mlvdddytrp pepvystvnk lcdkpasprh yspvecdksf llsapyshyh lgllpdsemt
      361 shsqhstatr qpsmtlqrav slegeprkvv lhkgstglgf nivggedgeg ifvsfilagg
      421 padlsgelqr gdqilsvngi dlrgasheqa aaalkgagqt vtiiaqyqpe dyarfeakih
      481 dlreqmmnhs mssgsgslrt nqkrslyvra mfdydkskds glpsqglsfk ygdilhvina
      541 sddewwqarr vmlegdseem gvipskrrve rkerarlktv kfnakpgvid skgdipglgd
      601 dgygtktlrg qedlilsyep vtrqeinytr pviilgpmkd rinddlisef pdkfgscvph
      661 ttrpkrdyev dgrdyhfvis reqmekdiqe hkfieagqyn dnlygtsvqs vrfvaergkh
      721 cildvsgnai krlqvaqlyp iaifikprsl eplmemnkrl teeqakktyd raikleqefg
      781 eyftaivqgd tlediynqck lvieeqsgpf iwipskekl
//
LOCUS       NP_001127836            1135 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 4 [Homo sapiens].
ACCESSION   NP_001127836
VERSION     NP_001127836.1
DBSOURCE    REFSEQ: accession NM_001134364.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1135)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1135)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1135)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1135)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1135)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1135)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1135)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1135)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1135)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1135)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA114613.1, AB209377.1 and
            AA904866.1.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Transcript Variant: This variant (4) lacks an alternate exon and
            uses an alternate splice site in the 3' coding region, compared to
            variant 1. The resulting protein (isoform 4) has a shorter and
            distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB209377.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1135
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1135
                     /product="microtubule-associated protein 4 isoform 4"
                     /note="MAP-4"
                     /calculated_mol_wt=119828
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          50..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          248..545
                     /region_name="17 X 14 AA tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          362..401
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          <575..919
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            580
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          641..991
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            696
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10791892,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            723
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            787
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10791892,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            797
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            803
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            825
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            853
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            928
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          <931..952
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            941
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            942
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          992..1022
                     /region_name="Tau/MAP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          992..1021
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            1000
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          1023..1053
                     /region_name="Tau/MAP 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1023..1052
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          1054..1085
                     /region_name="Tau/MAP 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1054..1084
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            1073
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     CDS             1..1135
                     /gene="MAP4"
                     /coded_by="NM_001134364.2:96..3503"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS46818.1"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgsp tefleekmay qeypnsqnwp
      121 edtnfcfqpe qvvdpiqtdp fkmyhdddla dlvfpssata dtsifagqnd plkdsygmsp
      181 cntavvpqgw svealnsphs esfvspeava eppqptavpl elakeiemas eerppaqale
      241 immglkttdm apsketemal akdmalatkt evalakdmes ptkldvtlak dmqpsmesdm
      301 alvkdmelpt ekevalvkdv rwptetdvss aknvvlptet evapakdvtl lketeraspi
      361 kmdlapskdm gppkenkket eraspikmdl apskdmgppk enkivpakdl vllseievaq
      421 andiisstei ssaekvalss etevalardm tlppetnvil tkdkalplea evapvkdmaq
      481 lpeteiapak dvapstvkev gllkdmspls etemalgkdv tpppetevvl iknvclppem
      541 evaltedqvp alkteaplak dgvltlannv tpakdvppls eteatpvpik dmeiaqtqkg
      601 isedshlesl qdvgqsaapt fmispetvtg tgkkcslpae edsvleklge rkpcnsqpse
      661 lssetsgiar peegrpvvsg tgndittppn kelppspekk tkplattqpa ktstskaktq
      721 ptslpkqpap ttigglnkkp mslasglvpa appkrpavas arpsilpskd vkpkpiadak
      781 apekraspsk pasapasrsg skstqtvakt ttaaavastg pssrspstll pkkptaikte
      841 gkpaevkkmt aksvpadlsr pkststssmk ktttlsgtap aagvvpsrvk atpmpsrpst
      901 tpfidkkpts akpssttprl srlatntsap dlknvrskvg stenikhqpg ggrakvekkt
      961 eaaattrkpe snavtktagp iasaqkqpag kvqivskkvs yshiqskcgs kdnikhvpgg
     1021 gnvqiqnkkv diskvsskcg skanikhkpg ggdvkiesqk lnfkekaqak vgsldnvghl
     1081 paggavkiet yrltfranar artdhgadiv srpphfpggp nsgsrvlgpl sravh
//
LOCUS       NP_001362510             265 aa            linear   PRI 21-NOV-2025
DEFINITION  cAMP-dependent protein kinase catalytic subunit beta isoform 19
            [Homo sapiens].
ACCESSION   NP_001362510 XP_016857195
VERSION     NP_001362510.1
DBSOURCE    REFSEQ: accession NM_001375581.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Tanaka,M., Takeshita,K., Kunita,A., Hasegawa,K. and Ushiku,T.
  TITLE     PRKACA/PRKACB Fusions in Pancreatobiliary Intraductal Oncocytic
            Papillary Neoplasms Including Those With Atypical Morphology: An
            Analysis of 22 Cases Expanding Morphologic Spectrum
  JOURNAL   Am J Surg Pathol 48 (8), 1032-1040 (2024)
   PUBMED   38841868
  REMARK    GeneRIF: PRKACA/PRKACB Fusions in Pancreatobiliary Intraductal
            Oncocytic Papillary Neoplasms Including Those With Atypical
            Morphology: An Analysis of 22 Cases Expanding Morphologic Spectrum.
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Pei,W., Yin,W., Yu,T., Zhang,X., Zhang,Q., Yang,X., Shi,C., Shen,W.
            and Liu,G.
  TITLE     Dual-Specificity Phosphatase 4 Promotes Malignant Features in
            Colorectal Cancer Through Cyclic-AMP Response Element Binding
            Protein/Protein Kinase CAMP-Activated Catalytic Subunit Beta
            Activation
  JOURNAL   Dig Dis Sci 69 (8), 2856-2874 (2024)
   PUBMED   38824257
  REMARK    GeneRIF: Dual-Specificity Phosphatase 4 Promotes Malignant Features
            in Colorectal Cancer Through Cyclic-AMP Response Element Binding
            Protein/Protein Kinase CAMP-Activated Catalytic Subunit Beta
            Activation.
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Itoh,T., Omori,Y., Seino,M., Hirose,K., Date,F., Ono,Y.,
            Mizukami,Y., Aoki,S., Ishida,M., Mizuma,M., Morikawa,T.,
            Higuchi,R., Honda,G., Okamura,Y., Kinoshita,K., Unno,M. and
            Furukawa,T.
  TITLE     Gene Rearrangement and Expression of PRKACA and PRKACB Govern
            Morphobiology of Pancreatobiliary Oncocytic Neoplasms
  JOURNAL   Mod Pathol 37 (1), 100358 (2024)
   PUBMED   37871652
  REMARK    GeneRIF: Gene Rearrangement and Expression of PRKACA and PRKACB
            Govern Morphobiology of Pancreatobiliary Oncocytic Neoplasms.
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Maimaitiaili,Y., Fukumura,Y., Hirabayashi,K., Kinowaki,Y.,
            Naito,Y., Saito,A., Rong,L., Nakahodo,J. and Yao,T.
  TITLE     Investigation of -PRKACA/-PRKACB fusion genes in oncocytic tumors
            of the pancreatobiliary and other systems
  JOURNAL   Virchows Arch 481 (6), 865-876 (2022)
   PUBMED   36152045
  REMARK    GeneRIF: Investigation of -PRKACA/-PRKACB fusion genes in oncocytic
            tumors of the pancreatobiliary and other systems.
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Orstavik,S., Reinton,N., Frengen,E., Langeland,B.T., Jahnsen,T. and
            Skalhegg,B.S.
  TITLE     Identification of novel splice variants of the human catalytic
            subunit Cbeta of cAMP-dependent protein kinase
  JOURNAL   Eur J Biochem 268 (19), 5066-5073 (2001)
   PUBMED   11589697
REFERENCE   6  (residues 1 to 265)
  AUTHORS   Scarpetta,M.A. and Uhler,M.D.
  TITLE     Evidence for two additional isoforms of the endogenous protein
            kinase inhibitor of cAMP-dependent protein kinase in mouse
  JOURNAL   J Biol Chem 268 (15), 10927-10931 (1993)
   PUBMED   7684369
REFERENCE   7  (residues 1 to 265)
  AUTHORS   Da Silva,J.D., Tkachenko,N. and Soares,A.R.
  TITLE     Ellis-van Creveld Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37903214
REFERENCE   8  (residues 1 to 265)
  AUTHORS   Simard,J., Berube,D., Sandberg,M., Grzeschik,K.H., Gagne,R.,
            Hansson,V. and Jahnsen,T.
  TITLE     Assignment of the gene encoding the catalytic subunit C beta of
            cAMP-dependent protein kinase to the p36 band on chromosome 1
  JOURNAL   Hum Genet 88 (6), 653-657 (1992)
   PUBMED   1551670
REFERENCE   9  (residues 1 to 265)
  AUTHORS   Beebe,S.J., Oyen,O., Sandberg,M., Froysa,A., Hansson,V. and
            Jahnsen,T.
  TITLE     Molecular cloning of a tissue-specific protein kinase (C gamma)
            from human testis--representing a third isoform for the catalytic
            subunit of cAMP-dependent protein kinase
  JOURNAL   Mol Endocrinol 4 (3), 465-475 (1990)
   PUBMED   2342480
REFERENCE   10 (residues 1 to 265)
  AUTHORS   Taylor,S.S., Buechler,J.A. and Yonemoto,W.
  TITLE     cAMP-dependent protein kinase: framework for a diverse family of
            regulatory enzymes
  JOURNAL   Annu Rev Biochem 59, 971-1005 (1990)
   PUBMED   2165385
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL450063.14.
            
            On Oct 29, 2019 this sequence version replaced XP_016857195.1.
            
            Summary: The protein encoded by this gene is a member of the
            serine/threonine protein kinase family. The encoded protein is a
            catalytic subunit of cAMP (cyclic AMP)-dependent protein kinase,
            which mediates signalling though cAMP. cAMP signaling is important
            to a number of processes, including cell proliferaton and
            differentiation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA2145544 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.1"
     Protein         1..265
                     /product="cAMP-dependent protein kinase catalytic subunit
                     beta isoform 19"
                     /EC_number="2.7.11.11"
                     /note="protein kinase A catalytic subunit beta; protein
                     kinase, cAMP-dependent, catalytic, beta; protein kinase,
                     cAMP-dependent, beta catalytic subunit"
                     /calculated_mol_wt=30466
     Region          49..>265
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(57..60,63,65,78,80,112,128..131,174,178..179,181,
                     191..192)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..265
                     /gene="PRKACB"
                     /gene_synonym="CAFD2; PKA C-beta; PKACB"
                     /coded_by="NM_001375581.1:109..906"
                     /note="isoform 19 is encoded by transcript variant 19"
                     /db_xref="GeneID:5567"
                     /db_xref="HGNC:HGNC:9381"
                     /db_xref="MIM:176892"
ORIGIN      
        1 mglsrkssda sacssseisd sfvkeflaka kedflkkwen ptqnnagled ferkktlgtg
       61 sfgrvmlvkh kateqyyamk ildkqkvvkl kqiehtlnek rilqavnfpf lvrleyafkd
      121 nsnlymvmey vpggemfshl rrigrfseph arfyaaqivl tfeylhsldl iyrdlkpenl
      181 lidhqgyiqv tdfgfakrvk grtwtlcgtp eylapeiils kgynkavdww algvliyema
      241 agyppffadq piqiyekivs gkqnf
//
LOCUS       NP_001135896             288 aa            linear   PRI 21-NOV-2025
DEFINITION  mortality factor 4-like protein 2 [Homo sapiens].
ACCESSION   NP_001135896
VERSION     NP_001135896.1
DBSOURCE    REFSEQ: accession NM_001142424.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Kooblall,K.G., Stokes,V.J., Shariq,O.A., English,K.A.,
            Stevenson,M., Broxholme,J., Wright,B., Lockstone,H.E., Buck,D.,
            Grozinsky-Glasberg,S., Yates,C.J., Thakker,R.V. and Lines,K.E.
  TITLE     miR-3156-5p is downregulated in serum of MEN1 patients and
            regulates expression of MORF4L2
  JOURNAL   Endocr Relat Cancer 29 (10), 557-568 (2022)
   PUBMED   35900839
  REMARK    GeneRIF: miR-3156-5p is downregulated in serum of MEN1 patients and
            regulates expression of MORF4L2.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Zheng,X., Sun,Z., Yu,L., Shi,D., Zhu,M., Yao,H. and Li,L.
  TITLE     Interactome Analysis of the Nucleocapsid Protein of SARS-CoV-2
            Virus
  JOURNAL   Pathogens 10 (9), 1155 (2021)
   PUBMED   34578187
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Cai,Y., Jin,J., Tomomori-Sato,C., Sato,S., Sorokina,I.,
            Parmely,T.J., Conaway,R.C. and Conaway,J.W.
  TITLE     Identification of new subunits of the multiprotein mammalian
            TRRAP/TIP60-containing histone acetyltransferase complex
  JOURNAL   J Biol Chem 278 (44), 42733-42736 (2003)
   PUBMED   12963728
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Yochum,G.S. and Ayer,D.E.
  TITLE     Role for the mortality factors MORF4, MRGX, and MRG15 in
            transcriptional repression via associations with Pf1, mSin3A, and
            Transducin-Like Enhancer of Split
  JOURNAL   Mol Cell Biol 22 (22), 7868-7876 (2002)
   PUBMED   12391155
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Sakai,K., Shirakawa,T., Li,Y., Kitagawa,Y. and Hirose,G.
  TITLE     Interaction of a paraneoplastic cerebellar degeneration-associated
            neuronal protein with the nuclear helix-loop-helix leucine zipper
            protein MRG X
  JOURNAL   Mol Cell Neurosci 19 (4), 477-484 (2002)
   PUBMED   11988016
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Hoja,M.R., Wahlestedt,C. and Hoog,C.
  TITLE     A visual intracellular classification strategy for uncharacterized
            human proteins
  JOURNAL   Exp Cell Res 259 (1), 239-246 (2000)
   PUBMED   10942595
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Bertram,M.J., Berube,N.G., Hang-Swanson,X., Ran,Q., Leung,J.K.,
            Bryce,S., Spurgers,K., Bick,R.J., Baldini,A., Ning,Y., Clark,L.J.,
            Parkinson,E.K., Barrett,J.C., Smith,J.R. and Pereira-Smith,O.M.
  TITLE     Identification of a gene that reverses the immortal phenotype of a
            subset of cells and is a member of a novel family of transcription
            factor-like genes
  JOURNAL   Mol Cell Biol 19 (2), 1479-1485 (1999)
   PUBMED   9891081
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC093013.1.
            
            Transcript Variant: This variant (8) differs in the 5' UTR,
            compared to variant 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC093013.1, SRR7346977.377951.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.2"
     Protein         1..288
                     /product="mortality factor 4-like protein 2"
                     /note="MSL3-2 protein; protein MSL3-2; MORF-related gene X
                     protein; transcription factor-like protein MRGX"
                     /calculated_mol_wt=32177
     Region          1..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15014.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15014.1)"
     Region          102..276
                     /region_name="MRG"
                     /note="pfam05712"
                     /db_xref="CDD:461721"
     CDS             1..288
                     /gene="MORF4L2"
                     /gene_synonym="MORFL2; MRGX"
                     /coded_by="NM_001142424.2:335..1201"
                     /db_xref="CCDS:CCDS14512.1"
                     /db_xref="GeneID:9643"
                     /db_xref="HGNC:HGNC:16849"
                     /db_xref="MIM:300409"
ORIGIN      
        1 mssrkqgsqp rgqqsaeeen fkkptrsnmq rskmrgassg kktagpqqkn lepalpgrwg
       61 grsaenppsg svrktrknkq ktpgngdggs tseapqpprk kraradptve seeafknrme
      121 vkvkipeelk pwlvedwdlv trqkqlfqlp akknvdaile eyanckksqg nvdnkeyavn
      181 evvagikeyf nvmlgtqlly kferpqyaei llahpdapms qvygaphllr lfvrigamla
      241 ytpldeksla lllgylhdfl kylaknsasl ftasdykvas aeyhrkal
//
LOCUS       NP_001373100             373 aa            linear   PRI 21-NOV-2025
DEFINITION  tetratricopeptide repeat protein 23-like isoform 5 [Homo sapiens].
ACCESSION   NP_001373100
VERSION     NP_001373100.1
DBSOURCE    REFSEQ: accession NM_001386171.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Pan,T.L., Hsu,S.Y., Wang,P.W., Cheng,Y.T., Chang,Y.C., Saha,S.,
            Hu,J. and Ouyang,P.
  TITLE     FLJ25439, a novel cytokinesis-associated protein, induces
            tetraploidization and maintains chromosomal stability via enhancing
            expression of endoplasmic reticulum stress chaperones
  JOURNAL   Cell Cycle 14 (8), 1174-1187 (2015)
   PUBMED   25751302
  REMARK    GeneRIF: FLJ25439 is involved in pathways related to
            anti-apoptosis, protein folding, the cell cycle, and cytoskeleton
            regulation.
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Corominas,R., Yang,X., Lin,G.N., Kang,S., Shen,Y., Ghamsari,L.,
            Broly,M., Rodriguez,M., Tam,S., Wanamaker,S.A., Fan,C., Yi,S.,
            Tasan,M., Lemmens,I., Kuang,X., Zhao,N., Malhotra,D.,
            Michaelson,J.J., Vacic,V., Calderwood,M.A., Roth,F.P.,
            Tavernier,J., Horvath,S., Salehi-Ashtiani,K., Korkin,D., Sebat,J.,
            Hill,D.E., Hao,T., Vidal,M. and Iakoucheva,L.M.
  TITLE     Protein interaction network of alternatively spliced isoforms from
            brain links genetic risk factors for autism
  JOURNAL   Nat Commun 5, 3650 (2014)
   PUBMED   24722188
  REMARK    Erratum:[Nat Commun. 2023 Feb 2;14(1):569. doi:
            10.1038/s41467-023-36264-y. PMID: 36732511]
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC026801.7.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.84552.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968968,
                                           SAMEA2148874 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..373
                     /product="tetratricopeptide repeat protein 23-like isoform
                     5"
                     /note="tetratricopeptide repeat protein 23-like"
                     /calculated_mol_wt=41973
     Region          164..>331
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          262..341
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     CDS             1..373
                     /gene="TTC23L"
                     /gene_synonym="MC25-1"
                     /coded_by="NM_001386171.1:255..1376"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:153657"
                     /db_xref="HGNC:HGNC:26355"
                     /db_xref="MIM:616344"
ORIGIN      
        1 mdalepgkkm qaspiriptv sndidwdfcf hmsqqteipa hqqtdelypt ggcgeseeet
       61 kakekekaid cmshpkekla qsqkkvaqli kekmntqank elircvilsr iifgdhhwkc
      121 aralanlayg yltlrglpvq akkhatsakn tlltwkantt snkekeeile alvklyytlg
      181 vawllqnrgr eayfnlqkae rnmkelkely kggvcelqvs endltlalgr aslaihrlnl
      241 alayfekaig dviaakgdrt sdlislyeea aqieqlrrnh nqaiqylqqa hsvcvslfte
      301 vspktaemsa llakayamsg eaqhrdavei yfirsinayr atlgsedfet lstteefckw
      361 lvqngekqls nli
//
LOCUS       NP_001273448             299 aa            linear   PRI 21-NOV-2025
DEFINITION  adenosine 3'-phospho 5'-phosphosulfate transporter 1 isoform f
            [Homo sapiens].
ACCESSION   NP_001273448
VERSION     NP_001273448.1
DBSOURCE    REFSEQ: accession NM_001286519.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Guasto,A., Dubail,J., Aguilera-Albesa,S., Paganini,C., Vanhulle,C.,
            Haouari,W., Gorria-Redondo,N., Aznal-Sainz,E., Boddaert,N.,
            Planas-Serra,L., Schluter,A., Velez-Santamaria,V., Verdura,E.,
            Bruneel,A., Rossi,A., Huber,C., Pujol,A. and Cormier-Daire,V.
  TITLE     Biallelic variants in SLC35B2 cause a novel chondrodysplasia with
            hypomyelinating leukodystrophy
  JOURNAL   Brain 145 (10), 3711-3722 (2022)
   PUBMED   35325049
  REMARK    GeneRIF: Biallelic variants in SLC35B2 cause a novel
            chondrodysplasia with hypomyelinating leukodystrophy.
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Uezato,A., Jitoku,D., Shimazu,D., Yamamoto,N., Kurumaji,A.,
            Iwayama,Y., Toyota,T., Yoshikawa,T., Haroutunian,V., Bentea,E.,
            Meller,J., Sullivan,C.R., Meador-Woodruff,J.H., McCullumsmith,R.E.
            and Nishikawa,T.
  TITLE     Differential genetic associations and expression of PAPST1/SLC35B2
            in bipolar disorder and schizophrenia
  JOURNAL   J Neural Transm (Vienna) 129 (7), 913-924 (2022)
   PUBMED   35501530
  REMARK    GeneRIF: Differential genetic associations and expression of
            PAPST1/SLC35B2 in bipolar disorder and schizophrenia.
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Guo,D., Yu,X., Wang,D., Li,Z., Zhou,Y., Xu,G., Yuan,B., Qin,Y. and
            Chen,M.
  TITLE     SLC35B2 Acts in a Dual Role in the Host Sulfation Required for EV71
            Infection
  JOURNAL   J Virol 96 (9), e0204221 (2022)
   PUBMED   35420441
  REMARK    GeneRIF: SLC35B2 Acts in a Dual Role in the Host Sulfation Required
            for EV71 Infection.
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Guo,X.Y., Gao,X.D. and Fujita,M.
  TITLE     Sulfation of a FLAG tag mediated by SLC35B2 and TPST2 affects
            antibody recognition
  JOURNAL   PLoS One 16 (5), e0250805 (2021)
   PUBMED   33951064
  REMARK    GeneRIF: Sulfation of a FLAG tag mediated by SLC35B2 and TPST2
            affects antibody recognition.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Xu,Q.F., Pan,Y.W., Li,L.C., Zhou,Z., Huang,Q.L., Pang,J.C.,
            Zhu,X.P., Ren,Y., Yang,H., Ohgaki,H. and Lv,S.Q.
  TITLE     MiR-22 is frequently downregulated in medulloblastomas and inhibits
            cell proliferation via the novel target PAPST1
  JOURNAL   Brain Pathol 24 (6), 568-583 (2014)
   PUBMED   24576181
  REMARK    GeneRIF: Results suggest that frequently downregulated miR-22
            expression is associated with cell proliferation in
            medulloblastomas, and this may be at least in part via PAPST1,
            which is a novel target of miR-22
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Kamiyama,S., Ichimiya,T., Ikehara,Y., Takase,T., Fujimoto,I.,
            Suda,T., Nakamori,S., Nakamura,M., Nakayama,F., Irimura,T.,
            Nakanishi,H., Watanabe,M., Narimatsu,H. and Nishihara,S.
  TITLE     Expression and the role of 3'-phosphoadenosine 5'-phosphosulfate
            transporters in human colorectal carcinoma
  JOURNAL   Glycobiology 21 (2), 235-246 (2011)
   PUBMED   20978009
  REMARK    GeneRIF: PAPS transporters play a role in the proliferation of
            colorectal carcinoma cells themselves and take part in a
            desmoplastic reaction to support cancer growth by controlling their
            sulfation status.
REFERENCE   8  (residues 1 to 299)
  AUTHORS   Hosgood,H.D. 3rd, Zhang,L., Shen,M., Berndt,S.I., Vermeulen,R.,
            Li,G., Yin,S., Yeager,M., Yuenger,J., Rothman,N., Chanock,S.,
            Smith,M. and Lan,Q.
  TITLE     Association between genetic variants in VEGF, ERCC3 and
            occupational benzene haematotoxicity
  JOURNAL   Occup Environ Med 66 (12), 848-853 (2009)
   PUBMED   19773279
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 299)
  AUTHORS   Kamiyama,S., Suda,T., Ueda,R., Suzuki,M., Okubo,R., Kikuchi,N.,
            Chiba,Y., Goto,S., Toyoda,H., Saigo,K., Watanabe,M., Narimatsu,H.,
            Jigami,Y. and Nishihara,S.
  TITLE     Molecular cloning and identification of 3'-phosphoadenosine
            5'-phosphosulfate transporter
  JOURNAL   J Biol Chem 278 (28), 25958-25963 (2003)
   PUBMED   12716889
  REMARK    GeneRIF: PAPS1 has roles in PAPS transport and post-translational
            sulfation
REFERENCE   10 (residues 1 to 299)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY044970.1, AK293251.1, AK075456.1 and AK223028.1.
            
            Summary: Sulfotransferases (e.g., SULT4A1; MIM 608359) use an
            activated form of sulfate, 3-prime-phosphoadenosine
            5-prime-phosphosulfate (PAPS), as a common sulfate donor for
            sulfation of glycoproteins, proteoglycans, and glycolipids in the
            endoplasmic reticulum and Golgi apparatus. SLC35B2 is located in
            the microsomal membrane and transports PAPS from the cytosol, where
            it is synthesized, into the Golgi lumen (Kamiyama et al., 2003
            [PubMed 12716889]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (8) lacks two alternate exons,
            resulting in translation initiation at a downstream in-frame start
            codon, compared to variant 1. The encoded isoform (f) is shorter at
            the N-terminus, compared to isoform a. Both variants 8 and 9 encode
            isoform f.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293251.1, DA023482.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146982, SAMEA2155628
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..299
                     /product="adenosine 3'-phospho 5'-phosphosulfate
                     transporter 1 isoform f"
                     /note="3'-phosphoadenosine 5'-phosphosulfate transporter;
                     adenosine 3'-phospho 5'-phosphosulfate transporter 1; PAPS
                     transporter 1; putative MAPK-activating protein PM15;
                     putative NF-kappa-B-activating protein 48; solute carrier
                     family 35 (adenosine 3'-phospho 5'-phosphosulfate
                     transporter), member B2"
                     /calculated_mol_wt=32533
     Region          20..279
                     /region_name="UAA"
                     /note="UAA transporter family; pfam08449"
                     /db_xref="CDD:462479"
     CDS             1..299
                     /gene="SLC35B2"
                     /gene_synonym="HLD26; PAPST1; SLL; UGTrel4"
                     /coded_by="NM_001286519.2:169..1068"
                     /note="isoform f is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS75462.1"
                     /db_xref="GeneID:347734"
                     /db_xref="HGNC:HGNC:16872"
                     /db_xref="MIM:610788"
ORIGIN      
        1 mtrsygatat spgerftdsq flvlmnrvla livaglscvl ckqprhgapm yrysfaslsn
       61 vlsswcqyea lkfvsfptqv lakaskvipv mlmgklvsrr syehweylta tlisigvsmf
      121 llssgpeprs spattlsgli llagyiafds ftsnwqdalf aykmssvqmm fgvnffsclf
      181 tvgslleqga llegtrfmgr hsefaahall lsicsacgql fifytigqfg aavftiimtl
      241 rqafaillsc llyghtvtvv gglgvavvfa alllrvyarg rlkqrgkkav pvespvqkv
//
LOCUS       NP_001371820             762 aa            linear   PRI 21-NOV-2025
DEFINITION  signal transducer and activator of transcription 1-alpha/beta
            isoform 12 [Homo sapiens].
ACCESSION   NP_001371820
VERSION     NP_001371820.1
DBSOURCE    REFSEQ: accession NM_001384891.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 762)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 762)
  AUTHORS   Wang,Y., Song,Q., Huang,W., Lin,Y., Wang,X., Wang,C., Willard,B.,
            Zhao,C., Nan,J., Holvey-Bates,E., Wang,Z., Taylor,D., Yang,J. and
            Stark,G.R.
  TITLE     A virus-induced conformational switch of STAT1-STAT2 dimers boosts
            antiviral defenses
  JOURNAL   Cell Res 31 (2), 206-218 (2021)
   PUBMED   32759968
REFERENCE   3  (residues 1 to 762)
  AUTHORS   Decker,T. and Kovarik,P.
  TITLE     Serine phosphorylation of STATs
  JOURNAL   Oncogene 19 (21), 2628-2637 (2000)
   PUBMED   10851062
  REMARK    Review article
REFERENCE   4  (residues 1 to 762)
  AUTHORS   Bowman,T., Garcia,R., Turkson,J. and Jove,R.
  TITLE     STATs in oncogenesis
  JOURNAL   Oncogene 19 (21), 2474-2488 (2000)
   PUBMED   10851046
  REMARK    Review article
REFERENCE   5  (residues 1 to 762)
  AUTHORS   Haddad,B., Pabon-Pena,C.R., Young,H. and Sun,W.H.
  TITLE     Assignment1 of STAT1 to human chromosome 2q32 by FISH and radiation
            hybrids
  JOURNAL   Cytogenet Cell Genet 83 (1-2), 58-59 (1998)
   PUBMED   9925928
REFERENCE   6  (residues 1 to 762)
  AUTHORS   Yan,R., Qureshi,S., Zhong,Z., Wen,Z. and Darnell,J.E. Jr.
  TITLE     The genomic structure of the STAT genes: multiple exons in
            coincident sites in Stat1 and Stat2
  JOURNAL   Nucleic Acids Res 23 (3), 459-463 (1995)
   PUBMED   7885841
REFERENCE   7  (residues 1 to 762)
  AUTHORS   Igarashi,K., Garotta,G., Ozmen,L., Ziemiecki,A., Wilks,A.F.,
            Harpur,A.G., Larner,A.C. and Finbloom,D.S.
  TITLE     Interferon-gamma induces tyrosine phosphorylation of
            interferon-gamma receptor and regulated association of protein
            tyrosine kinases, Jak1 and Jak2, with its receptor
  JOURNAL   J Biol Chem 269 (20), 14333-14336 (1994)
   PUBMED   7514165
REFERENCE   8  (residues 1 to 762)
  AUTHORS   Shuai,K., Horvath,C.M., Huang,L.H., Qureshi,S.A., Cowburn,D. and
            Darnell,J.E. Jr.
  TITLE     Interferon activation of the transcription factor Stat91 involves
            dimerization through SH2-phosphotyrosyl peptide interactions
  JOURNAL   Cell 76 (5), 821-828 (1994)
   PUBMED   7510216
REFERENCE   9  (residues 1 to 762)
  AUTHORS   Schindler,C., Fu,X.Y., Improta,T., Aebersold,R. and Darnell,J.E.
            Jr.
  TITLE     Proteins of transcription factor ISGF-3: one gene encodes the
            91-and 84-kDa ISGF-3 proteins that are activated by interferon
            alpha
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7836-7839 (1992)
   PUBMED   1502203
REFERENCE   10 (residues 1 to 762)
  AUTHORS   Schindler,C., Shuai,K., Prezioso,V.R. and Darnell,J.E. Jr.
  TITLE     Interferon-dependent tyrosine phosphorylation of a latent
            cytoplasmic transcription factor
  JOURNAL   Science 257 (5071), 809-813 (1992)
   PUBMED   1496401
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC067945.4.
            
            Summary: The protein encoded by this gene is a member of the STAT
            protein family. In response to cytokines and growth factors, STAT
            family members are phosphorylated by the receptor associated
            kinases, and then form homo- or heterodimers that translocate to
            the cell nucleus where they act as transcription activators. The
            protein encoded by this gene can be activated by various ligands
            including interferon-alpha, interferon-gamma, EGF, PDGF and IL6.
            This protein mediates the expression of a variety of genes, which
            is thought to be important for cell viability in response to
            different cell stimuli and pathogens. The protein plays an
            important role in immune responses to viral, fungal and
            mycobacterial pathogens. Mutations in this gene are associated with
            Immunodeficiency 31B, 31A, and 31C. [provided by RefSeq, Jun 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1965299, SAMEA1966682
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.2"
     Protein         1..762
                     /product="signal transducer and activator of transcription
                     1-alpha/beta isoform 12"
                     /note="transcription factor ISGF-3 components p91/p84;
                     signal transducer and activator of transcription
                     1-alpha/beta; signal transducer and activator of
                     transcription 1, 91kD; signal transducer and activator of
                     transcription 1, 91kDa"
                     /calculated_mol_wt=88508
     Region          2..133
                     /region_name="STAT_int"
                     /note="STAT protein, protein interaction domain;
                     smart00964"
                     /db_xref="CDD:214942"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            126
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Region          150..325
                     /region_name="STAT1_CCD"
                     /note="Coiled-coil domain of Signal Transducer and
                     Activator of Transcription 1 (STAT1); cd16851"
                     /db_xref="CDD:341076"
     Site            order(176..177,180..181,184,187..188,191,244,248,251..253,
                     255..256,268..269,271..272,275..276,279,283,286,318,
                     321..323)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:341076"
     Site            187
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            order(251..253,255..256,268..269,272,275..276,279,283,286,
                     314,318,321..322)
                     /site_type="other"
                     /note="CCD-DBD interface [polypeptide binding]"
                     /db_xref="CDD:341076"
     Site            308
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Region          329..489
                     /region_name="STAT1_DBD"
                     /note="DNA-binding domain of Signal Transducer and
                     Activator of Transcription 1 (STAT1); cd16845"
                     /db_xref="CDD:341083"
     Site            order(348,352,390,423,425,438..439,471..472,475)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:341083"
     Site            378
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            537
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Region          569..719
                     /region_name="SH2_STAT1"
                     /note="Src homology 2 (SH2) domain found in signal
                     transducer and activator of transcription (STAT) 1
                     proteins; cd10372"
                     /db_xref="CDD:198235"
     Site            order(596,614,642,644)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198235"
     Site            order(643,659)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198235"
     Site            649
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            order(653..654,718)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:198235"
     Site            677
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK1, JAK2 or TYK2.
                     /evidence=ECO:0000269|PubMed:17561467,
                     ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:21135090,
                     ECO:0000269|PubMed:22065572, ECO:0000269|PubMed:26479788,
                     ECO:0000269|PubMed:27796300, ECO:0000269|PubMed:28753426,
                     ECO:0000269|PubMed:38621137, ECO:0000269|PubMed:7657660;
                     propagated from UniProtKB/Swiss-Prot (P42224.2)"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKE.
                     /evidence=ECO:0000269|PubMed:22065572; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Region          727..751
                     /region_name="STAT1_TAZ2bind"
                     /note="STAT1 TAZ2 binding domain; pfam12162"
                     /db_xref="CDD:432372"
     Site            736
                     /site_type="other"
                     /note="Required for recruitment of EP300/p300.
                     /evidence=ECO:0000269|PubMed:16257975; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            739
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CAMK2 and MAPK14.
                     /evidence=ECO:0000269|PubMed:11972023,
                     ECO:0000269|PubMed:15322115, ECO:0000269|PubMed:16257975,
                     ECO:0000269|PubMed:17897103, ECO:0000269|PubMed:21135090,
                     ECO:0000269|PubMed:22065572, ECO:0000269|PubMed:26479788,
                     ECO:0000269|PubMed:38621137, ECO:0000269|PubMed:7543024,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            757
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKE.
                     /evidence=ECO:0000250|UniProtKB:P42225; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            761
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by IKKB.
                     /evidence=ECO:0000269|PubMed:32209697,
                     ECO:0000269|PubMed:38621137; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     CDS             1..762
                     /gene="STAT1"
                     /gene_synonym="CANDF7; IMD31A; IMD31B; IMD31C; ISGF-3;
                     STAT91"
                     /coded_by="NM_001384891.1:310..2598"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="GeneID:6772"
                     /db_xref="HGNC:HGNC:11362"
                     /db_xref="MIM:600555"
ORIGIN      
        1 msqwyelqql dskfleqvhq lyddsfpmei rqylaqwlek qdcsrmkcvn vksprehaan
       61 dvsfatirfh dllsqlddqy srfslennfl lqhnirkskr nlqdnfqedp iqmsmiiysc
      121 lkeerkilen aqrfnqaqsg niqstvmldk qkeldskvrn vkdkvmcieh eiksledlqd
      181 eydfkcktlq nrehetngva ksdqkqeqll lkkmylmldn krkevvhkii ellnvteltq
      241 nalindelve wkrrqqsaci ggppnacldq lqnwftivae slqqvrqqlk kleeleqkyt
      301 yehdpitknk qvlwdrtfsl fqqliqssfv verqpcmpth pqrplvlktg vqftvklrll
      361 vklqelnynl kvkvlfdkdv nerntvkgfr kfnilgthtk vmnmeestng slaaefrhlq
      421 lkeqknagtr tnegplivte elhslsfetq lcqpglvidl ettslpvvvi snvsqlpsgw
      481 asilwynmlv aeprnlsffl tppcarwaql sevlswqfss vtkrglnvdq lnmlgekllg
      541 pnaspdglip wtrfckenin dknfpfwlwi esilelikkh llplwndgci mgfiskerer
      601 allkdqqpgt fllrfsessr egaitftwve rsqnggepdf havepytkke lsavtfpdii
      661 rnykvmaaen ipenplkyly pnidkdhafg kyysrpkeap epmeldgpkg tgyiktelis
      721 vsevhpsrlq ttdnllpmsp eefdevsriv gsvefdsmmn tv
//
LOCUS       NP_001308206             465 aa            linear   PRI 21-NOV-2025
DEFINITION  tRNA-splicing endonuclease subunit Sen2 isoform 1 [Homo sapiens].
ACCESSION   NP_001308206 XP_005265552
VERSION     NP_001308206.1
DBSOURCE    REFSEQ: accession NM_001321277.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Canpolat,N., Liu,D., Atayar,E., Saygili,S., Kara,N.S.,
            Westfall,T.A., Ding,Q., Brown,B.J., Braun,T.A., Slusarski,D., Karli
            Oguz,K., Ozluk,Y., Tuysuz,B., Tastemel Ozturk,T., Sever,L.,
            Sezerman,O.U., Topaloglu,R., Caliskan,S., Attanasio,M. and
            Ozaltin,F.
  TITLE     A splice site mutation in the TSEN2 causes a new syndrome with
            craniofacial and central nervous system malformations, and atypical
            hemolytic uremic syndrome
  JOURNAL   Clin Genet 101 (3), 346-358 (2022)
   PUBMED   34964109
  REMARK    GeneRIF: A splice site mutation in the TSEN2 causes a new syndrome
            with craniofacial and central nervous system malformations, and
            atypical hemolytic uremic syndrome.
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Sekulovski,S., Devant,P., Panizza,S., Gogakos,T., Pitiriciu,A.,
            Heitmeier,K., Ramsay,E.P., Barth,M., Schmidt,C., Tuschl,T.,
            Baas,F., Weitzer,S., Martinez,J. and Trowitzsch,S.
  TITLE     Assembly defects of human tRNA splicing endonuclease contribute to
            impaired pre-tRNA processing in pontocerebellar hypoplasia
  JOURNAL   Nat Commun 12 (1), 5610 (2021)
   PUBMED   34584079
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Weitzer,S. and Martinez,J.
  TITLE     The human RNA kinase hClp1 is active on 3' transfer RNA exons and
            short interfering RNAs
  JOURNAL   Nature 447 (7141), 222-226 (2007)
   PUBMED   17495927
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Paushkin,S.V., Patel,M., Furia,B.S., Peltz,S.W. and Trotta,C.R.
  TITLE     Identification of a human endonuclease complex reveals a link
            between tRNA splicing and pre-mRNA 3' end formation
  JOURNAL   Cell 117 (3), 311-321 (2004)
   PUBMED   15109492
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   10 (residues 1 to 465)
  AUTHORS   van Dijk,T. and Baas,F.
  TITLE     TSEN54 Pontocerebellar Hypoplasia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301773
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA614108.1, AK225875.1,
            BC004178.2, BM671402.1 and AC018500.4.
            
            On Mar 19, 2016 this sequence version replaced XP_005265552.1.
            
            Summary: This gene encodes one of the subunits of the tRNA splicing
            endonuclease. This endonuclease catalyzes the first step in RNA
            splicing which is the removal of introns. Mutations in this gene
            have been associated with pontocerebellar hypoplasia type 2. A
            pseudogene has been identified on chromosome 4. Multiple transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, Feb 2009].
            
            Transcript Variant: This variant (6) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 6 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1433201.1,
                                           SRR18074968.2149331.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.2"
     Protein         1..465
                     /product="tRNA-splicing endonuclease subunit Sen2 isoform
                     1"
                     /EC_number="4.6.1.16"
                     /note="tRNA-splicing endonuclease subunit Sen2; hsSen2;
                     tRNA-intron endonuclease Sen2; TSEN2 tRNA splicing
                     endonuclease subunit"
                     /calculated_mol_wt=53116
     Region          157..204
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCE0.2)"
     Region          <283..329
                     /region_name="tRNA_int_endo_N"
                     /note="tRNA intron endonuclease, N-terminal domain;
                     pfam02778"
                     /db_xref="CDD:397071"
     Region          339..430
                     /region_name="tRNA-intron_lyase_C"
                     /note="catalytic C-terminal domain of the tRNA-intron
                     lyase; cd22363"
                     /db_xref="CDD:411767"
     Site            order(369,377,416)
                     /site_type="active"
                     /db_xref="CDD:411767"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P7W5; propagated from
                     UniProtKB/Swiss-Prot (Q8NCE0.2)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P7W5; propagated from
                     UniProtKB/Swiss-Prot (Q8NCE0.2)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P7W5; propagated from
                     UniProtKB/Swiss-Prot (Q8NCE0.2)"
     CDS             1..465
                     /gene="TSEN2"
                     /gene_synonym="PCH2B; SEN2; SEN2L"
                     /coded_by="NM_001321277.2:56..1453"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS2611.1"
                     /db_xref="GeneID:80746"
                     /db_xref="HGNC:HGNC:28422"
                     /db_xref="MIM:608753"
ORIGIN      
        1 maeavfhapk rkrrvyetye splpipfgqd hgplkefkif raeminnnvi vrnaedieql
       61 ygkgyfgkgi lsrsrpsfti sdpklvakwk dmktnmpiit skryqhsvew aaelmrrqgq
      121 destvrrilk dytkplehpp vkrneeaqvh dklnsgmvsn megtaggerp svvngdsgks
      181 ggvgdprepl gclqegsgch pttesfeksv redasplphv ccckqdalil qrglhhedgs
      241 qhigllhpgd rgpdheyvlv eeaecamser eaapneelvq rnrlicrrnp yrifeylqls
      301 leeafflvya lgclsiyyek epltivklwk aftvvqptfr ttymayhyfr skgwvpkvgl
      361 kygtdlllyr kgppfyhasy sviielvddh fegslrrpls wkslaalsrv svnvskelml
      421 cylikpstmt dkemespecm krikvqevil srwvssrers dqddl
//
LOCUS       NP_001186195             934 aa            linear   PRI 21-NOV-2025
DEFINITION  diacylglycerol kinase zeta isoform 5 [Homo sapiens].
ACCESSION   NP_001186195
VERSION     NP_001186195.1
DBSOURCE    REFSEQ: accession NM_001199266.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 934)
  AUTHORS   Harris,R.A., Bush,A.H., Eagar,T.N., Qian,J., Greenwood,M.P.,
            Opekun,A.R., Baldassano,R., Guthery,S.L., Noe,J.D., Otley,A.,
            Rosh,J.R., Kugathasan,S. and Kellermayer,R.
  TITLE     Exome Sequencing Implicates DGKZ, ESRRA, and GXYLT1 for Modulating
            Granuloma Formation in Crohn Disease
  JOURNAL   J Pediatr Gastroenterol Nutr 77 (3), 354-357 (2023)
   PUBMED   37347142
  REMARK    GeneRIF: Exome Sequencing Implicates DGKZ , ESRRA , and GXYLT1 for
            Modulating Granuloma Formation in Crohn Disease.
REFERENCE   2  (residues 1 to 934)
  AUTHORS   Liu,X.F., Zhao,S.W., Cui,J.J., Gu,Y.W., Fan,J.W., Fu,Y.F.,
            Zhang,Y.H., Yin,H., Chen,K. and Cui,L.B.
  TITLE     Differential expression of diacylglycerol kinase zeta is involved
            in inferior parietal lobule-related dysfunction in schizophrenia
            with cognitive impairments
  JOURNAL   BMC Psychiatry 23 (1), 526 (2023)
   PUBMED   37479996
  REMARK    GeneRIF: Differential expression of diacylglycerol kinase zeta is
            involved in inferior parietal lobule-related dysfunction in
            schizophrenia with cognitive impairments.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 934)
  AUTHORS   Furuta,M., Murakami,C., Numagami,Y., Suzuki,R. and Sakane,F.
  TITLE     Diacylglycerol kinase zeta interacts with sphingomyelin synthase 1
            and sphingomyelin synthase-related protein via different regions
  JOURNAL   FEBS Open Bio 13 (7), 1333-1345 (2023)
   PUBMED   37166445
  REMARK    GeneRIF: Diacylglycerol kinase zeta interacts with sphingomyelin
            synthase 1 and sphingomyelin synthase-related protein via different
            regions.
REFERENCE   4  (residues 1 to 934)
  AUTHORS   Yamazaki,A., Kawashima,A., Honda,T., Kohama,T., Murakami,C.,
            Sakane,F., Murayama,T. and Nakamura,H.
  TITLE     Identification and characterization of diacylglycerol kinase zeta
            as a novel enzyme producing ceramide-1-phosphate
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1868 (6), 159307 (2023)
   PUBMED   36906254
  REMARK    GeneRIF: Identification and characterization of diacylglycerol
            kinase zeta as a novel enzyme producing ceramide-1-phosphate.
REFERENCE   5  (residues 1 to 934)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 934)
  AUTHORS   Topham,M.K. and Prescott,S.M.
  TITLE     Diacylglycerol kinase zeta regulates Ras activation by a novel
            mechanism
  JOURNAL   J Cell Biol 152 (6), 1135-1143 (2001)
   PUBMED   11257115
REFERENCE   7  (residues 1 to 934)
  AUTHORS   Liu,Z., Chang,G.Q. and Leibowitz,S.F.
  TITLE     Diacylglycerol kinase zeta in hypothalamus interacts with long form
            leptin receptor. Relation to dietary fat and body weight regulation
  JOURNAL   J Biol Chem 276 (8), 5900-5907 (2001)
   PUBMED   11078732
REFERENCE   8  (residues 1 to 934)
  AUTHORS   Topham,M.K., Bunting,M., Zimmerman,G.A., McIntyre,T.M.,
            Blackshear,P.J. and Prescott,S.M.
  TITLE     Protein kinase C regulates the nuclear localization of
            diacylglycerol kinase-zeta
  JOURNAL   Nature 394 (6694), 697-700 (1998)
   PUBMED   9716136
REFERENCE   9  (residues 1 to 934)
  AUTHORS   Ding,L., Bunting,M., Topham,M.K., McIntyre,T.M., Zimmerman,G.A. and
            Prescott,S.M.
  TITLE     Alternative splicing of the human diacylglycerol kinase zeta gene
            in muscle
  JOURNAL   Proc Natl Acad Sci U S A 94 (11), 5519-5524 (1997)
   PUBMED   9159104
REFERENCE   10 (residues 1 to 934)
  AUTHORS   Bunting,M., Tang,W., Zimmerman,G.A., McIntyre,T.M. and
            Prescott,S.M.
  TITLE     Molecular cloning and characterization of a novel human
            diacylglycerol kinase zeta
  JOURNAL   J Biol Chem 271 (17), 10230-10236 (1996)
   PUBMED   8626588
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB959911.1, AK225774.1 and
            U51477.1.
            
            Summary: The protein encoded by this gene belongs to the eukaryotic
            diacylglycerol kinase family. It may attenuate protein kinase C
            activity by regulating diacylglycerol levels in intracellular
            signaling cascade and signal transduction. Alternative splicing
            occurs at this locus and multiple transcript variants encoding
            distinct isoforms have been identified. [provided by RefSeq, Nov
            2010].
            
            Transcript Variant: This variant (5) has an alternate 5' sequence
            including the coding region and extra nts CAG and an extra segment
            at alternate splice sites, respectively, in the CDS, compared to
            variant 4. The resulting isoform (5) has a shorter and distinct
            N-terminus, and an internal additional aa and an additional
            segment, compared to isoform 4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225774.1, SRR14038193.3544196.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..934
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..934
                     /product="diacylglycerol kinase zeta isoform 5"
                     /EC_number="2.7.1.107"
                     /EC_number="2.7.1.93"
                     /note="diacylglycerol kinase, zeta 104kDa; DAG kinase
                     zeta; diglyceride kinase zeta"
                     /calculated_mol_wt=104450
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13574.4)"
     Region          59..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13574.4)"
     Region          88..161
                     /region_name="C1_DGKzeta_rpt1"
                     /note="first protein kinase C conserved region 1 (C1
                     domain) found in diacylglycerol kinase zeta (DAG kinase
                     zeta) and similar proteins; cd20849"
                     /db_xref="CDD:410399"
     Region          171..245
                     /region_name="C1_DGKzeta_rpt2"
                     /note="second protein kinase C conserved region 1 (C1
                     domain) found in diacylglycerol kinase zeta (DAG kinase
                     zeta) and similar proteins; cd20895"
                     /db_xref="CDD:410445"
     Region          252..281
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13574.4)"
     Region          260..274
                     /region_name="MARCKS homology"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13574.4)"
     Region          279..417
                     /region_name="Mediates interaction with RASGRP1.
                     /evidence=ECO:0000269|PubMed:11257115"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13574.4)"
     Region          298..419
                     /region_name="DAGKc"
                     /note="Diacylglycerol kinase catalytic domain (presumed);
                     smart00046"
                     /db_xref="CDD:214487"
     Region          362..370
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250|UniProtKB:Q80UP3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13574.4)"
     Region          447..604
                     /region_name="DAGKa"
                     /note="Diacylglycerol kinase accessory domain (presumed);
                     smart00045"
                     /db_xref="CDD:214486"
     Site            706
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13574.4)"
     Region          760..789
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13574.4)"
     Site            782
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13574.4)"
     Region          <795..>916
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          795..821
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(796..797,800..802,804..805,809,812,821,823,825,
                     829..830,833..835,837..838,842,845,853,863,865,869..870,
                     873..875,877..878,882,885)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          823..853
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          823..853
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13574.4)"
     Region          863..888
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          930..934
                     /region_name="PDZ-binding.
                     /evidence=ECO:0000269|PubMed:11352924,
                     ECO:0000269|PubMed:17351151"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13574.4)"
     CDS             1..934
                     /gene="DGKZ"
                     /gene_synonym="DAGK5; DAGK6; DGK-ZETA; hDGKzeta"
                     /coded_by="NM_001199266.2:198..3002"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS55757.1"
                     /db_xref="GeneID:8525"
                     /db_xref="HGNC:HGNC:2857"
                     /db_xref="MIM:601441"
ORIGIN      
        1 meprdgspea rssdsesasa sssgserdag pepdkaprrl nkrrfpglrl fghrkaitks
       61 glqhlapppp tpgapcsese rqirstvdws esatygehiw fetnvsgdfc yvgeqycvar
      121 mlqksvsrrk caackivvht pcieqlekin frckpsfres gsrnvreptf vrhhwvhrrr
      181 qdgkcrhcgk gfqqkftfhs keivaiscsw ckqayhskvs cfmlqqieep cslgvhaavv
      241 ipptwilrar rpqntlkask kkkrasfkrk sskkgpeegr wrpfiirptp splmkpllvf
      301 vnpksggnqg akiiqsflwy lnprqvfdls qggpkealem yrkvhnlril acggdgtvgw
      361 ilstldqlrl kppppvailp lgtgndlart lnwgggytde pvskilshve egnvvqldrw
      421 dlhaepnpea gpedrdegat drlpldvfnn yfslgfdahv tlefhesrea npekfnsrfr
      481 nkmfyagtaf sdflmgsskd lakhirvvcd gmdltpkiqd lkpqcvvfln iprycagtmp
      541 wghpgehhdf epqrhddgyl evigftmtsl aalqvgghge rltqcrevvl ttskaipvqv
      601 dgepcklaas ririalrnqa tmvqkakrrs aaplhsdqqp vpeqlriqvs rvsmhdyeal
      661 hydkeqlkea svplgtvvvp gdsdlelcra hierlqqepd gagaksptcq klspkwcfld
      721 attasrfyri draqehlnyv teiaqdeiyi ldpellgasa rpdlptptsp lptspcsptp
      781 rslqgdaapp qgeelieaak rndfcklqel hraggdlmhr deqsrtllhh avstgskdvv
      841 rylldhappe ildaveenpc spsgetclhq aaalgqrtic hyiveagasl mktdqqgdtp
      901 rqraekaqdt elaaylenrq hyqmiqredq etav
//
LOCUS       NP_001177906             138 aa            linear   PRI 21-NOV-2025
DEFINITION  YY1-associated factor 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001177906
VERSION     NP_001177906.1
DBSOURCE    REFSEQ: accession NM_001190977.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Zhang,S., Zhang,X., Guan,X., Ma,X., Chen,H., Huang,B. and Chen,D.
  TITLE     YAF2 exerts anti-apoptotic effect in human tumor cells in a FANK1-
            and phosphorylation-dependent manner
  JOURNAL   Biochem Biophys Res Commun 554, 99-106 (2021)
   PUBMED   33784512
  REMARK    GeneRIF: YAF2 exerts anti-apoptotic effect in human tumor cells in
            a FANK1- and phosphorylation-dependent manner.
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 138)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 138)
  AUTHORS   Madge,B., Geisen,C., Moroy,T. and Schwab,M.
  TITLE     Yaf2 inhibits Myc biological function
  JOURNAL   Cancer Lett 193 (2), 171-176 (2003)
   PUBMED   12706874
REFERENCE   7  (residues 1 to 138)
  AUTHORS   Sawa,C., Yoshikawa,T., Matsuda-Suzuki,F., Delehouzee,S., Goto,M.,
            Watanabe,H., Sawada,J., Kataoka,K. and Handa,H.
  TITLE     YEAF1/RYBP and YAF-2 are functionally distinct members of a
            cofactor family for the YY1 and E4TF1/hGABP transcription factors
  JOURNAL   J Biol Chem 277 (25), 22484-22490 (2002)
   PUBMED   11953439
  REMARK    GeneRIF: YEAF1/RYBP and YAF-2 are functionally distinct members of
            a cofactor family for the YY1 and E4TF1/hGABP transcription
            factors.
REFERENCE   8  (residues 1 to 138)
  AUTHORS   Ogawa,H., Ishiguro,K., Gaubatz,S., Livingston,D.M. and Nakatani,Y.
  TITLE     A complex with chromatin modifiers that occupies E2F- and
            Myc-responsive genes in G0 cells
  JOURNAL   Science 296 (5570), 1132-1136 (2002)
   PUBMED   12004135
REFERENCE   9  (residues 1 to 138)
  AUTHORS   Bannasch,D., Madge,B. and Schwab,M.
  TITLE     Functional interaction of Yaf2 with the central region of MycN
  JOURNAL   Oncogene 20 (41), 5913-5919 (2001)
   PUBMED   11593398
REFERENCE   10 (residues 1 to 138)
  AUTHORS   Kalenik,J.L., Chen,D., Bradley,M.E., Chen,S.J. and Lee,T.C.
  TITLE     Yeast two-hybrid cloning of a novel zinc finger protein that
            interacts with the multifunctional transcription factor YY1
  JOURNAL   Nucleic Acids Res 25 (4), 843-849 (1997)
   PUBMED   9016636
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK294260.1, BC037777.2 and
            AC020629.6.
            
            Summary: This gene encodes a zinc finger containing protein that
            functions in the regulation of transcription. This protein was
            identified as an interacting partner of transcriptional repressor
            protein Yy1, and also interacts with other transcriptional
            regulators, including Myc and Polycomb. This protein can promote
            proteolysis of Yy1. Multiple alternatively spliced transcript
            variants have been found. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (3) lacks two consecutive in-frame
            exons compared to variant 1. The resulting isoform (3) is shorter
            than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK294260.1, SRR14038197.2162492.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145122, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..138
                     /product="YY1-associated factor 2 isoform 3"
                     /calculated_mol_wt=14984
     Region          60..92
                     /region_name="YAF2_RYBP"
                     /note="Yaf2/RYBP C-terminal binding motif; pfam17219"
                     /db_xref="CDD:465386"
     CDS             1..138
                     /gene="YAF2"
                     /coded_by="NM_001190977.3:69..485"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS53778.1"
                     /db_xref="GeneID:10138"
                     /db_xref="HGNC:HGNC:17363"
                     /db_xref="MIM:607534"
ORIGIN      
        1 mgdkksptrk prpvsqlvaq qvtqqfvppt qskkekkdkv ekeksekett skknshkktr
       61 prlknvdrss aqhlevtvgd ltviitdfke ktksppassa asadqhsqsg sssdntergm
      121 srsssprgea sslngesh
//
LOCUS       NP_001276048             543 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger CCHC domain-containing protein 7 [Homo sapiens].
ACCESSION   NP_001276048 XP_005251663
VERSION     NP_001276048.1
DBSOURCE    REFSEQ: accession NM_001289119.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Sudo,H., Nozaki,A., Uno,H., Ishida,Y. and Nagahama,M.
  TITLE     Interaction properties of human TRAMP-like proteins and their role
            in pre-rRNA 5'ETS turnover
  JOURNAL   FEBS Lett 590 (17), 2963-2972 (2016)
   PUBMED   27434818
  REMARK    GeneRIF: We analyzed the interactions of the human TRAMP-like
            proteins, PAPD5, ZCCHC7, and MTR4, with the nuclear exosome. PAPD5
            and ZCCHC7 exhibited mutual interactions in presence of the exosome
            catalytic subunit RRP6, whereas MTR4 was dispensable for their
            assembly
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Kipper,S., Hamad,S., Caly,L., Avrahami,D., Bacharach,E., Jans,D.A.,
            Gerber,D. and Bajorek,M.
  TITLE     New host factors important for respiratory syncytial virus (RSV)
            replication revealed by a novel microfluidics screen for
            interactors of matrix (M) protein
  JOURNAL   Mol Cell Proteomics 14 (3), 532-543 (2015)
   PUBMED   25556234
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 543)
  AUTHORS   Lubas,M., Christensen,M.S., Kristiansen,M.S., Domanski,M.,
            Falkenby,L.G., Lykke-Andersen,S., Andersen,J.S., Dziembowski,A. and
            Jensen,T.H.
  TITLE     Interaction profiling identifies the human nuclear exosome
            targeting complex
  JOURNAL   Mol Cell 43 (4), 624-637 (2011)
   PUBMED   21855801
REFERENCE   6  (residues 1 to 543)
  AUTHORS   An,Q., Wright,S.L., Moorman,A.V., Parker,H., Griffiths,M.,
            Ross,F.M., Davies,T., Harrison,C.J. and Strefford,J.C.
  TITLE     Heterogeneous breakpoints in patients with acute lymphoblastic
            leukemia and the dic(9;20)(p11-13;q11) show recurrent involvement
            of genes at 20q11.21
  JOURNAL   Haematologica 94 (8), 1164-1169 (2009)
   PUBMED   19586940
  REMARK    GeneRIF: Data show that sequences 3' of PAX5 disrupting ASXL1, and
            ZCCHC7 disrupted by sequences 3' of FRG1B and LOC1499503.
REFERENCE   7  (residues 1 to 543)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   8  (residues 1 to 543)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC034022.1, BC005990.1 and BC036940.1.
            
            On Jan 15, 2014 this sequence version replaced XP_005251663.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. Variants 1, 2, 3, and 4 encode the same
            protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034022.1, SRR14038191.4174327.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.2"
     Protein         1..543
                     /product="zinc finger CCHC domain-containing protein 7"
                     /note="TRAMP-like complex RNA-binding factor ZCCHC7; zinc
                     finger, CCHC domain containing 7"
                     /calculated_mol_wt=62922
     Region          51..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3Z6.2)"
     Region          <238..379
                     /region_name="AIR1"
                     /note="Arginine methyltransferase-interacting protein,
                     contains RING Zn-finger [Posttranslational modification,
                     protein turnover, chaperones / Intracellular trafficking
                     and secretion]; COG5082"
                     /db_xref="CDD:227414"
     Region          414..543
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3Z6.2)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8N3Z6.2)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3Z6.2)"
     CDS             1..543
                     /gene="ZCCHC7"
                     /gene_synonym="AIR1; HSPC086"
                     /coded_by="NM_001289119.2:76..1707"
                     /db_xref="CCDS:CCDS6608.2"
                     /db_xref="GeneID:84186"
                     /db_xref="HGNC:HGNC:26209"
ORIGIN      
        1 mmfggyetie ayeddlyrde ssselsvdse vefqlysqih yaqdlddvir eeeheeknsg
       61 nsesssskpn qkklivlsds eviqlsdgse vitlsdedsi yrckgknvrv qaqenahgls
      121 sslqsnelvd kkcksdiekp kseersgvir evmiievsss eeeestiseg dnveswmllg
      181 cevddkdddi llnlvgcens vtegedginw sisdkdieaq iannrtpgrw tqryysankn
      241 iicrncdkrg hlskncplpr kvrrcflcsr rghllyscpa plceycpvpk mldhsclfrh
      301 swdkqcdrch mlghytdact eiwrqyhltt kpgppkkpkt psrpsalayc yhcaqkghyg
      361 hecperevyd pspvspficy yddkyeiqer ekrlkqkikv lkkngvipep sklpyikaan
      421 enphhdirkg raswksnrwp qenketqkem knknrnwekh rkadrhrevd edfprgpkty
      481 sspgsfktqk pskpfhrssh yhtsredksp kegkrgkqkk kercwedddn dnlflikqrk
      541 kks
//
LOCUS       NP_004626                382 aa            linear   PRI 21-NOV-2025
DEFINITION  MAP kinase-activated protein kinase 3 [Homo sapiens].
ACCESSION   NP_004626
VERSION     NP_004626.1
DBSOURCE    REFSEQ: accession NM_004635.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Ludwig,S., Engel,K., Hoffmeyer,A., Sithanandam,G., Neufeld,B.,
            Palm,D., Gaestel,M. and Rapp,U.R.
  TITLE     3pK, a novel mitogen-activated protein (MAP) kinase-activated
            protein kinase, is targeted by three MAP kinase pathways
  JOURNAL   Mol Cell Biol 16 (12), 6687-6697 (1996)
   PUBMED   8943323
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Clifton,A.D., Young,P.R. and Cohen,P.
  TITLE     A comparison of the substrate specificity of MAPKAP kinase-2 and
            MAPKAP kinase-3 and their activation by cytokines and cellular
            stress
  JOURNAL   FEBS Lett 392 (3), 209-214 (1996)
   PUBMED   8774846
REFERENCE   7  (residues 1 to 382)
  AUTHORS   McLaughlin,M.M., Kumar,S., McDonnell,P.C., Van Horn,S., Lee,J.C.,
            Livi,G.P. and Young,P.R.
  TITLE     Identification of mitogen-activated protein (MAP) kinase-activated
            protein kinase-3, a novel substrate of CSBP p38 MAP kinase
  JOURNAL   J Biol Chem 271 (14), 8488-8492 (1996)
   PUBMED   8626550
REFERENCE   8  (residues 1 to 382)
  AUTHORS   Sithanandam,G., Latif,F., Duh,F.M., Bernal,R., Smola,U., Li,H.,
            Kuzmin,I., Wixler,V., Geil,L. and Shrestha,S.
  TITLE     3pK, a new mitogen-activated protein kinase-activated protein
            kinase located in the small cell lung cancer tumor suppressor gene
            region
  JOURNAL   Mol Cell Biol 16 (3), 868-876 (1996)
   PUBMED   8622688
  REMARK    Erratum:[Mol Cell Biol 1996 Apr;16(4):1880]
REFERENCE   9  (residues 1 to 382)
  AUTHORS   Ben-Levy,R., Leighton,I.A., Doza,Y.N., Attwood,P., Morrice,N.,
            Marshall,C.J. and Cohen,P.
  TITLE     Identification of novel phosphorylation sites required for
            activation of MAPKAP kinase-2
  JOURNAL   EMBO J 14 (23), 5920-5930 (1995)
   PUBMED   8846784
REFERENCE   10 (residues 1 to 382)
  AUTHORS   Lavoie,J.N., Lambert,H., Hickey,E., Weber,L.A. and Landry,J.
  TITLE     Modulation of cellular thermoresistance and actin filament
            stability accompanies phosphorylation-induced changes in the
            oligomeric structure of heat shock protein 27
  JOURNAL   Mol Cell Biol 15 (1), 505-516 (1995)
   PUBMED   7799959
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM848086.1, BC001662.2,
            AC096920.2 and BE301676.1.
            
            Summary: This gene encodes a member of the Ser/Thr protein kinase
            family. This kinase functions as a mitogen-activated protein kinase
            (MAP kinase)- activated protein kinase. MAP kinases are also known
            as extracellular signal-regulated kinases (ERKs), act as an
            integration point for multiple biochemical signals. This kinase was
            shown to be activated by growth inducers and stress stimulation of
            cells. In vitro studies demonstrated that ERK, p38 MAP kinase and
            Jun N-terminal kinase were all able to phosphorylate and activate
            this kinase, which suggested the role of this kinase as an
            integrative element of signaling in both mitogen and stress
            responses. This kinase was reported to interact with, phosphorylate
            and repress the activity of E47, which is a basic helix-loop-helix
            transcription factor known to be involved in the regulation of
            tissue-specific gene expression and cell differentiation. Alternate
            splicing results in multiple transcript variants that encode the
            same protein. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001662.2, SRR11853567.21030.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.2"
     Protein         1..382
                     /product="MAP kinase-activated protein kinase 3"
                     /EC_number="2.7.11.1"
                     /note="MAPKAP kinase 3; chromosome 3p kinase;
                     mitogen-activated protein kinase-activated protein kinase
                     3"
                     /calculated_mol_wt=42856
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q16644.1)"
     Region          39..304
                     /region_name="STKc_MAPKAPK3"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Mitogen-activated protein kinase-activated protein kinase
                     3; cd14172"
                     /db_xref="CDD:271074"
     Site            order(50..55,58,71,73,98,118..121,125,127,165..166,168,
                     170..171,173,186..187,190,203..207,209)
                     /site_type="active"
                     /db_xref="CDD:271074"
     Site            order(50..55,58,71,73,98,118..121,171,173,186..187)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271074"
     Site            order(52..55,57,206..210,214,216,219,240,242..245,
                     259..260,262..263,287..288)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:271074"
     Site            order(54,125,127,165..166,168,170,190,203..207,209)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271074"
     Site            order(186..195,197..207)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271074"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK14.
                     /evidence=ECO:0000250|UniProtKB:Q3UMW7; propagated from
                     UniProtKB/Swiss-Prot (Q16644.1)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          307..343
                     /region_name="Autoinhibitory helix. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q16644.1)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK14. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          335..344
                     /region_name="Nuclear export signal (NES).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          345..369
                     /region_name="p38 MAPK-binding site.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          350..353
                     /region_name="Bipartite nuclear localization signal 1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          357..382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          364..368
                     /region_name="Bipartite nuclear localization signal 2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     CDS             1..382
                     /gene="MAPKAPK3"
                     /gene_synonym="3PK; MAPKAP-K3; MAPKAP3; MAPKAPK-3; MDPT3;
                     MK-3; MK3"
                     /coded_by="NM_004635.5:129..1277"
                     /db_xref="CCDS:CCDS2832.1"
                     /db_xref="GeneID:7867"
                     /db_xref="HGNC:HGNC:6888"
                     /db_xref="MIM:602130"
ORIGIN      
        1 mdgetaeeqg gpvpppvapg gpglggapgg rrepkkyavt ddyqlskqvl glgvngkvle
       61 cfhrrtgqkc alkllydspk arqevdhhwq asggphivci ldvyenmhhg krclliimec
      121 meggelfsri qergdqafte reaaeimrdi gtaiqflhsh niahrdvkpe nllytskekd
      181 avlkltdfgf akettqnalq tpcytpyyva pevlgpekyd kscdmwslgv imyillcgfp
      241 pfysntgqai spgmkrrirl gqygfpnpew sevsedakql irlllktdpt erltitqfmn
      301 hpwinqsmvv pqtplhtarv lqedkdhwde vkeemtsala tmrvdydqvk ikdlktsnnr
      361 llnkrrkkqa gsssasqgcn nq
//
LOCUS       NP_001230855             382 aa            linear   PRI 21-NOV-2025
DEFINITION  MAP kinase-activated protein kinase 3 [Homo sapiens].
ACCESSION   NP_001230855
VERSION     NP_001230855.1
DBSOURCE    REFSEQ: accession NM_001243926.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Ludwig,S., Engel,K., Hoffmeyer,A., Sithanandam,G., Neufeld,B.,
            Palm,D., Gaestel,M. and Rapp,U.R.
  TITLE     3pK, a novel mitogen-activated protein (MAP) kinase-activated
            protein kinase, is targeted by three MAP kinase pathways
  JOURNAL   Mol Cell Biol 16 (12), 6687-6697 (1996)
   PUBMED   8943323
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Clifton,A.D., Young,P.R. and Cohen,P.
  TITLE     A comparison of the substrate specificity of MAPKAP kinase-2 and
            MAPKAP kinase-3 and their activation by cytokines and cellular
            stress
  JOURNAL   FEBS Lett 392 (3), 209-214 (1996)
   PUBMED   8774846
REFERENCE   7  (residues 1 to 382)
  AUTHORS   McLaughlin,M.M., Kumar,S., McDonnell,P.C., Van Horn,S., Lee,J.C.,
            Livi,G.P. and Young,P.R.
  TITLE     Identification of mitogen-activated protein (MAP) kinase-activated
            protein kinase-3, a novel substrate of CSBP p38 MAP kinase
  JOURNAL   J Biol Chem 271 (14), 8488-8492 (1996)
   PUBMED   8626550
REFERENCE   8  (residues 1 to 382)
  AUTHORS   Sithanandam,G., Latif,F., Duh,F.M., Bernal,R., Smola,U., Li,H.,
            Kuzmin,I., Wixler,V., Geil,L. and Shrestha,S.
  TITLE     3pK, a new mitogen-activated protein kinase-activated protein
            kinase located in the small cell lung cancer tumor suppressor gene
            region
  JOURNAL   Mol Cell Biol 16 (3), 868-876 (1996)
   PUBMED   8622688
  REMARK    Erratum:[Mol Cell Biol 1996 Apr;16(4):1880]
REFERENCE   9  (residues 1 to 382)
  AUTHORS   Ben-Levy,R., Leighton,I.A., Doza,Y.N., Attwood,P., Morrice,N.,
            Marshall,C.J. and Cohen,P.
  TITLE     Identification of novel phosphorylation sites required for
            activation of MAPKAP kinase-2
  JOURNAL   EMBO J 14 (23), 5920-5930 (1995)
   PUBMED   8846784
REFERENCE   10 (residues 1 to 382)
  AUTHORS   Lavoie,J.N., Lambert,H., Hickey,E., Weber,L.A. and Landry,J.
  TITLE     Modulation of cellular thermoresistance and actin filament
            stability accompanies phosphorylation-induced changes in the
            oligomeric structure of heat shock protein 27
  JOURNAL   Mol Cell Biol 15 (1), 505-516 (1995)
   PUBMED   7799959
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB450001.1, AC096920.2,
            BC068497.1 and BE301676.1.
            
            Summary: This gene encodes a member of the Ser/Thr protein kinase
            family. This kinase functions as a mitogen-activated protein kinase
            (MAP kinase)- activated protein kinase. MAP kinases are also known
            as extracellular signal-regulated kinases (ERKs), act as an
            integration point for multiple biochemical signals. This kinase was
            shown to be activated by growth inducers and stress stimulation of
            cells. In vitro studies demonstrated that ERK, p38 MAP kinase and
            Jun N-terminal kinase were all able to phosphorylate and activate
            this kinase, which suggested the role of this kinase as an
            integrative element of signaling in both mitogen and stress
            responses. This kinase was reported to interact with, phosphorylate
            and repress the activity of E47, which is a basic helix-loop-helix
            transcription factor known to be involved in the regulation of
            tissue-specific gene expression and cell differentiation. Alternate
            splicing results in multiple transcript variants that encode the
            same protein. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC068497.1, SRR14038192.1931767.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.2"
     Protein         1..382
                     /product="MAP kinase-activated protein kinase 3"
                     /EC_number="2.7.11.1"
                     /note="MAPKAP kinase 3; chromosome 3p kinase;
                     mitogen-activated protein kinase-activated protein kinase
                     3"
                     /calculated_mol_wt=42856
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q16644.1)"
     Region          39..304
                     /region_name="STKc_MAPKAPK3"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Mitogen-activated protein kinase-activated protein kinase
                     3; cd14172"
                     /db_xref="CDD:271074"
     Site            order(50..55,58,71,73,98,118..121,125,127,165..166,168,
                     170..171,173,186..187,190,203..207,209)
                     /site_type="active"
                     /db_xref="CDD:271074"
     Site            order(50..55,58,71,73,98,118..121,171,173,186..187)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271074"
     Site            order(52..55,57,206..210,214,216,219,240,242..245,
                     259..260,262..263,287..288)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:271074"
     Site            order(54,125,127,165..166,168,170,190,203..207,209)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271074"
     Site            order(186..195,197..207)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271074"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK14.
                     /evidence=ECO:0000250|UniProtKB:Q3UMW7; propagated from
                     UniProtKB/Swiss-Prot (Q16644.1)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          307..343
                     /region_name="Autoinhibitory helix. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q16644.1)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK14. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          335..344
                     /region_name="Nuclear export signal (NES).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          345..369
                     /region_name="p38 MAPK-binding site.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          350..353
                     /region_name="Bipartite nuclear localization signal 1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          357..382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          364..368
                     /region_name="Bipartite nuclear localization signal 2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     CDS             1..382
                     /gene="MAPKAPK3"
                     /gene_synonym="3PK; MAPKAP-K3; MAPKAP3; MAPKAPK-3; MDPT3;
                     MK-3; MK3"
                     /coded_by="NM_001243926.2:628..1776"
                     /db_xref="CCDS:CCDS2832.1"
                     /db_xref="GeneID:7867"
                     /db_xref="HGNC:HGNC:6888"
                     /db_xref="MIM:602130"
ORIGIN      
        1 mdgetaeeqg gpvpppvapg gpglggapgg rrepkkyavt ddyqlskqvl glgvngkvle
       61 cfhrrtgqkc alkllydspk arqevdhhwq asggphivci ldvyenmhhg krclliimec
      121 meggelfsri qergdqafte reaaeimrdi gtaiqflhsh niahrdvkpe nllytskekd
      181 avlkltdfgf akettqnalq tpcytpyyva pevlgpekyd kscdmwslgv imyillcgfp
      241 pfysntgqai spgmkrrirl gqygfpnpew sevsedakql irlllktdpt erltitqfmn
      301 hpwinqsmvv pqtplhtarv lqedkdhwde vkeemtsala tmrvdydqvk ikdlktsnnr
      361 llnkrrkkqa gsssasqgcn nq
//
LOCUS       NP_001381785             567 aa            linear   PRI 21-NOV-2025
DEFINITION  kinesin light chain 1 isoform 28 [Homo sapiens].
ACCESSION   NP_001381785
VERSION     NP_001381785.1
DBSOURCE    REFSEQ: accession NM_001394856.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Kikuchi,M., Viet,J., Nagata,K., Sato,M., David,G., Audic,Y.,
            Silverman,M.A., Yamamoto,M., Akatsu,H., Hashizume,Y., Takeda,S.,
            Akamine,S., Miyamoto,T., Uozumi,R., Gotoh,S., Mori,K., Ikeda,M.,
            Paillard,L. and Morihara,T.
  TITLE     Gene-gene functional relationships in Alzheimer's disease: CELF1
            regulates KLC1 alternative splicing
  JOURNAL   Biochem Biophys Res Commun 721, 150025 (2024)
   PUBMED   38768546
  REMARK    GeneRIF: Gene-gene functional relationships in Alzheimer's disease:
            CELF1 regulates KLC1 alternative splicing.
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 567)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   6  (residues 1 to 567)
  AUTHORS   Gyoeva,F.K., Bybikova,E.M. and Minin,A.A.
  TITLE     An isoform of kinesin light chain specific for the Golgi complex
  JOURNAL   J Cell Sci 113 (Pt 11), 2047-2054 (2000)
   PUBMED   10806115
REFERENCE   7  (residues 1 to 567)
  AUTHORS   Khodjakov,A., Lizunova,E.M., Minin,A.A., Koonce,M.P. and
            Gyoeva,F.K.
  TITLE     A specific light chain of kinesin associates with mitochondria in
            cultured cells
  JOURNAL   Mol Biol Cell 9 (2), 333-343 (1998)
   PUBMED   9450959
REFERENCE   8  (residues 1 to 567)
  AUTHORS   Chernajovsky,Y., Brown,A. and Clark,J.
  TITLE     Human kinesin light (beta) chain gene: DNA sequence and functional
            characterization of its promoter and first exon
  JOURNAL   DNA Cell Biol 15 (11), 965-974 (1996)
   PUBMED   8945637
REFERENCE   9  (residues 1 to 567)
  AUTHORS   Goedert,M., Marsh,S. and Carter,N.
  TITLE     Localization of the human kinesin light chain gene (KNS2) to
            chromosome 14q32.3 by fluorescence in situ hybridization
  JOURNAL   Genomics 32 (1), 173-175 (1996)
   PUBMED   8786116
REFERENCE   10 (residues 1 to 567)
  AUTHORS   Cabeza-Arvelaiz,Y., Shih,L.C., Hardman,N., Asselbergs,F., Bilbe,G.,
            Schmitz,A., White,B., Siciliano,M.J. and Lachman,L.B.
  TITLE     Cloning and genetic characterization of the human kinesin
            light-chain (KLC) gene
  JOURNAL   DNA Cell Biol 12 (10), 881-892 (1993)
   PUBMED   8274221
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139300.6 and AL049840.8.
            
            Summary: Conventional kinesin is a tetrameric molecule composed of
            two heavy chains and two light chains, and transports various
            cargos along microtubules toward their plus ends. The heavy chains
            provide the motor activity, while the light chains bind to various
            cargos. This gene encodes a member of the kinesin light chain
            family. It associates with kinesin heavy chain through an
            N-terminal domain, and six tetratricopeptide repeat (TPR) motifs
            are thought to be involved in binding of cargos such as vesicles,
            mitochondria, and the Golgi complex. Thus, kinesin light chains
            function as adapter molecules and not motors per se. Although
            previously named 'kinesin 2', this gene is not a member of the
            kinesin-2 / kinesin heavy chain subfamily of kinesin motor
            proteins. Extensive alternative splicing produces isoforms with
            different C-termini that are proposed to bind to different cargos;
            however, the full-length nature and/or biological validity of most
            of these variants have not been determined. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.449993.1,
                                           SRR18074967.150152.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..567
                     /product="kinesin light chain 1 isoform 28"
                     /EC_number="2.7.1.21"
                     /note="kinesin 2 60/70kDa; medulloblastoma antigen
                     MU-MB-2.50"
                     /calculated_mol_wt=64255
     Region          35..>149
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          210..435
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          214..241
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          255..283
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          297..325
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(298,301..302,305..306,308,340,343..344,347..348,
                     350..351,382,385..386,389..390,393)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          338..368
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          381..408
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..567
                     /gene="KLC1"
                     /gene_synonym="KLC; KNS2; KNS2A"
                     /coded_by="NM_001394856.1:286..1989"
                     /note="isoform 28 is encoded by transcript variant 28"
                     /db_xref="GeneID:3831"
                     /db_xref="HGNC:HGNC:6387"
                     /db_xref="MIM:600025"
ORIGIN      
        1 mydnmstmvy ikedkleklt qdeiisktkq viqglealkn ehnsilqsll etlkclkkdd
       61 esnlveeksn mirkslemle lglseaqvmm alsnhlnave sekqklraqv rrlcqenqwl
      121 rdelantqqk lqkseqsvaq leeekkhlef mnqlkkyddd ispsedkdtd stkeplddlf
      181 pndeddpgqg iqqqhssaaa aaqqggyeip arlrtlhnlv iqyasqgrye vavplckqal
      241 edlektsghd hpdvatmlni lalvyrdqnk ykdaanllnd alairektlg kdhpavaatl
      301 nnlavlygkr gkykeaeplc kraleirekv lgkdhpdvak qlnnlallcq nqgkyeevey
      361 yyqraleiyq tklgpddpnv aktknnlasc ylkqgkfkqa etlykeiltr aherefgsvd
      421 denkpiwmha eereeckgkq kdgtsfgeyg gwykackvds ptvtttlknl galyrrqgkf
      481 eaaetleeaa mrsrkqrsis eipkkilsan gsnhfplpgs qgldnvhkqr vaevlndpen
      541 mekrrsresl nvdvvkyesg pdggeea
//
LOCUS       NP_001378920              71 aa            linear   PRI 21-NOV-2025
DEFINITION  oncomodulin-1 isoform b [Homo sapiens].
ACCESSION   NP_001378920
VERSION     NP_001378920.1
DBSOURCE    REFSEQ: accession NM_001391991.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Tong,B., Hornak,A.J., Maison,S.F., Ohlemiller,K.K., Liberman,M.C.
            and Simmons,D.D.
  TITLE     Oncomodulin, an EF-Hand Ca2+ Buffer, Is Critical for Maintaining
            Cochlear Function in Mice
  JOURNAL   J Neurosci 36 (5), 1631-1635 (2016)
   PUBMED   26843644
  REMARK    GeneRIF: Deletion of oncomodulin in outer hair cells, leads to a
            progressive hearing loss in transgenic mice.
REFERENCE   3  (residues 1 to 71)
  AUTHORS   Ali,G., Lee,K., Andrade,P.B., Basit,S., Santos-Cortez,R.L.,
            Chen,L., Jelani,M., Ansar,M., Ahmad,W. and Leal,S.M.
  TITLE     Novel autosomal recessive nonsyndromic hearing impairment locus
            DFNB90 maps to 7p22.1-p15.3
  JOURNAL   Hum Hered 71 (2), 106-112 (2011)
   PUBMED   21734401
  REMARK    GeneRIF: Data indicate taht candidate genes ACTB, BZW, OCM, MACC1,
            NXPH1, PRPS1L1, RAC1 and RPA3, which lie within the DFNB90 region,
            were sequenced and no potentially causal variants were identified.
REFERENCE   4  (residues 1 to 71)
  AUTHORS   Kurimoto,T., Yin,Y., Omura,K., Gilbert,H.Y., Kim,D., Cen,L.P.,
            Moko,L., Kugler,S. and Benowitz,L.I.
  TITLE     Long-distance axon regeneration in the mature optic nerve:
            contributions of oncomodulin, cAMP, and pten gene deletion
  JOURNAL   J Neurosci 30 (46), 15654-15663 (2010)
   PUBMED   21084621
  REMARK    GeneRIF: Ocm plays a central role in inflammation-induced
            regeneration in the optic nerve.
REFERENCE   5  (residues 1 to 71)
  AUTHORS   Babini,E., Bertini,I., Capozzi,F., Del Bianco,C., Hollender,D.,
            Kiss,T., Luchinat,C. and Quattrone,A.
  TITLE     Solution structure of human beta-parvalbumin and structural
            comparison with its paralog alpha-parvalbumin and with their rat
            orthologs
  JOURNAL   Biochemistry 43 (51), 16076-16085 (2004)
   PUBMED   15610002
REFERENCE   6  (residues 1 to 71)
  AUTHORS   Pauls,T.L., Cox,J.A. and Berchtold,M.W.
  TITLE     The Ca2+(-)binding proteins parvalbumin and oncomodulin and their
            genes: new structural and functional findings
  JOURNAL   Biochim Biophys Acta 1306 (1), 39-54 (1996)
   PUBMED   8611623
  REMARK    Review article
REFERENCE   7  (residues 1 to 71)
  AUTHORS   Fohr,U.G., Weber,B.R., Muntener,M., Staudenmann,W., Hughes,G.J.,
            Frutiger,S., Banville,D., Schafer,B.W. and Heizmann,C.W.
  TITLE     Human alpha and beta parvalbumins. Structure and tissue-specific
            expression
  JOURNAL   Eur J Biochem 215 (3), 719-727 (1993)
   PUBMED   8354278
REFERENCE   8  (residues 1 to 71)
  AUTHORS   Ritzler,J.M., Sawhney,R., Geurts van Kessel,A.H., Grzeschik,K.H.,
            Schinzel,A. and Berchtold,M.W.
  TITLE     The genes for the highly homologous Ca(2+)-binding proteins
            oncomodulin and parvalbumin are not linked in the human genome
  JOURNAL   Genomics 12 (3), 567-572 (1992)
   PUBMED   1559707
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004983.3.
            
            Summary: Oncomodulin is a high-affinity calcium ion-binding
            protein. It belongs to the superfamily of calmodulin proteins, also
            known as the EF-hand proteins. Oncomodulin is an oncodevelopmental
            protein found in early embryonic cells in the placenta and also in
            tumors. [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            CDS exon combination :: CB045979.1, DB339645.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2144335, SAMEA2155371 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.1"
     Protein         1..71
                     /product="oncomodulin-1 isoform b"
                     /note="oncomodulin-1; hCG18255; parvalbumin beta; beta
                     parvalbumin"
                     /calculated_mol_wt=7895
     Region          <1..71
                     /region_name="EFh_parvalbumin_like"
                     /note="EF-hand, calcium binding motif, found in
                     parvalbumin-like EF-hand family; cl25356"
                     /db_xref="CDD:330177"
     Region          5..34
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:319998"
     Site            order(14,16,18,22,25,53,55,57,64)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:319998"
     Region          44..71
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:319998"
     CDS             1..71
                     /gene="OCM"
                     /gene_synonym="OCM1; OM; ONCM"
                     /coded_by="NM_001391991.1:157..372"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:654231"
                     /db_xref="HGNC:HGNC:8105"
                     /db_xref="MIM:164795"
ORIGIN      
        1 msanqvkdvf rfidndqsgy ldeeelkffl qkfesgarel tesetkslma aadndgdgki
       61 gaeefqemvh s
//
LOCUS       NP_001335661            1752 aa            linear   PRI 21-NOV-2025
DEFINITION  kinase D-interacting substrate of 220 kDa isoform 4 [Homo sapiens].
ACCESSION   NP_001335661
VERSION     NP_001335661.1
DBSOURCE    REFSEQ: accession NM_001348732.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1752)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1752)
  AUTHORS   Zhang,J., Zhang,Y., Shang,Q., Cheng,Y., Su,Y., Zhang,J., Wang,T.,
            Ding,J., Li,Y., Xie,Y. and Xing,Q.
  TITLE     Gain-of-Function KIDINS220 Variants Disrupt Neuronal Development
            and Cause Cerebral Palsy
  JOURNAL   Mov Disord 39 (3), 498-509 (2024)
   PUBMED   38148610
  REMARK    GeneRIF: Gain-of-Function KIDINS220 Variants Disrupt Neuronal
            Development and Cause Cerebral Palsy.
REFERENCE   3  (residues 1 to 1752)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1752)
  AUTHORS   Bondeson,D.P., Paolella,B.R., Asfaw,A., Rothberg,M.V.,
            Skipper,T.A., Langan,C., Mesa,G., Gonzalez,A., Surface,L.E.,
            Ito,K., Kazachkova,M., Colgan,W.N., Warren,A., Dempster,J.M.,
            Krill-Burger,J.M., Ericsson,M., Tang,A.A., Fung,I., Chambers,E.S.,
            Abdusamad,M., Dumont,N., Doench,J.G., Piccioni,F., Root,D.E.,
            Boehm,J., Hahn,W.C., Mannstadt,M., McFarland,J.M., Vazquez,F. and
            Golub,T.R.
  TITLE     Phosphate dysregulation via the XPR1-KIDINS220 protein complex is a
            therapeutic vulnerability in ovarian cancer
  JOURNAL   Nat Cancer 3 (6), 681-695 (2022)
   PUBMED   35437317
  REMARK    GeneRIF: Phosphate dysregulation via the XPR1-KIDINS220 protein
            complex is a therapeutic vulnerability in ovarian cancer.
REFERENCE   5  (residues 1 to 1752)
  AUTHORS   Scholz-Starke,J. and Cesca,F.
  TITLE     Stepping Out of the Shade: Control of Neuronal Activity by the
            Scaffold Protein Kidins220/ARMS
  JOURNAL   Front Cell Neurosci 10, 68 (2016)
   PUBMED   27013979
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1752)
  AUTHORS   Arevalo,J.C., Yano,H., Teng,K.K. and Chao,M.V.
  TITLE     A unique pathway for sustained neurotrophin signaling through an
            ankyrin-rich membrane-spanning protein
  JOURNAL   EMBO J 23 (12), 2358-2368 (2004)
   PUBMED   15167895
REFERENCE   7  (residues 1 to 1752)
  AUTHORS   Riol-Blanco,L., Iglesias,T., Sanchez-Sanchez,N., de la Rosa,G.,
            Sanchez-Ruiloba,L., Cabrera-Poch,N., Torres,A., Longo,I.,
            Garcia-Bordas,J., Longo,N., Tejedor,A., Sanchez-Mateos,P. and
            Rodriguez-Fernandez,J.L.
  TITLE     The neuronal protein Kidins220 localizes in a raft compartment at
            the leading edge of motile immature dendritic cells
  JOURNAL   Eur J Immunol 34 (1), 108-118 (2004)
   PUBMED   14971036
REFERENCE   8  (residues 1 to 1752)
  AUTHORS   Kong,H., Boulter,J., Weber,J.L., Lai,C. and Chao,M.V.
  TITLE     An evolutionarily conserved transmembrane protein that is a novel
            downstream target of neurotrophin and ephrin receptors
  JOURNAL   J Neurosci 21 (1), 176-185 (2001)
   PUBMED   11150334
REFERENCE   9  (residues 1 to 1752)
  AUTHORS   Iglesias,T., Cabrera-Poch,N., Mitchell,M.P., Naven,T.J.,
            Rozengurt,E. and Schiavo,G.
  TITLE     Identification and cloning of Kidins220, a novel neuronal substrate
            of protein kinase D
  JOURNAL   J Biol Chem 275 (51), 40048-40056 (2000)
   PUBMED   10998417
REFERENCE   10 (residues 1 to 1752)
  AUTHORS   Kaplan,D.R. and Miller,F.D.
  TITLE     Signal transduction by the neurotrophin receptors
  JOURNAL   Curr Opin Cell Biol 9 (2), 213-221 (1997)
   PUBMED   9069267
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012495.9.
            
            Summary: This gene encodes a transmembrane protein that is
            preferentially expressed in the nervous system where it controls
            neuronal cell survival, differentiation into exons and dendrites,
            and synaptic plasticity. The encoded protein interacts with
            membrane receptors, cytosolic signaling components, and
            cytoskeletal proteins, serving as a scaffold that mediates
            crosstalk between the neurotrophin pathway and several other
            intracellular signaling pathways. Aberrant expression of this gene
            is associated with the onset of various neuropsychiatric disorders
            and neurodegenerative diseases, including Alzheimer's disease.
            Naturally occurring mutations in this gene are associated with a
            syndrome characterized by spastic paraplegia, intellectual
            disability, nystagmus and obesity. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Feb 2017].
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon in the 3' coding region, compared to variant 1. The encoded
            isoform (4) is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.36630.1,
                                           SRR1660807.117893.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1752
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.1"
     Protein         1..1752
                     /product="kinase D-interacting substrate of 220 kDa
                     isoform 4"
                     /note="ankyrin repeat-rich membrane-spanning protein;
                     kinase D-interacting substrate 220kDa"
                     /calculated_mol_wt=194439
     Region          4..33
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          18..306
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          37..66
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          38..68
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(39,43..44,47..49,51..52,56,59,68,70,72,76..77,
                     80..82,84..85,89,92,101,103,105,109..110,113..115,
                     117..118,122,125)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          70..101
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          70..99
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          103..132
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          103..132
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          136..165
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          169..198
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          169..197
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          202..231
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          235..266
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          235..264
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          268..298
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          268..297
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          273..365
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Region          301..365
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          301..330
                     /region_name="ANK 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          334..363
                     /region_name="ANK 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          <348..412
                     /region_name="PHA02736"
                     /note="Viral ankyrin protein; Provisional"
                     /db_xref="CDD:165103"
     Region          367..396
                     /region_name="ANK 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          440..953
                     /region_name="KAP_NTPase"
                     /note="KAP family P-loop domain; pfam07693"
                     /db_xref="CDD:462231"
     Site            500..520
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            525..545
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            660..680
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            686..706
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            882
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            885
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            914
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            918
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          1089..1092
                     /region_name="Mediates interaction with CRKL.
                     /evidence=ECO:0000250|UniProtKB:Q9EQG6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            1163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          1266..1291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            1277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          1325..1349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            1333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            1340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            1342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            1343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            1346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          1378..1545
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            1502
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            1507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            1536
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            1555
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          1559..1614
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            1604
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            1614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            1660
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            1662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            1665
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          1694..1752
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          1747..1752
                     /region_name="PDZ-binding.
                     /evidence=ECO:0000250|UniProtKB:Q9EQG6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     CDS             1..1752
                     /gene="KIDINS220"
                     /gene_synonym="ARMS; SINO; VENARG"
                     /coded_by="NM_001348732.2:171..5429"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS86818.1"
                     /db_xref="GeneID:57498"
                     /db_xref="HGNC:HGNC:29508"
                     /db_xref="MIM:615759"
ORIGIN      
        1 msvlisqsvi nyveeenipa lkallekckd vdernecgqt plmiaaeqgn leivkelikn
       61 gancnledld nwtalisask eghvhiveel lkcgvnlehr dmggwtalmw acykgrtdvv
      121 elllshganp svtglysvyp iiwaagrgha divhlllqng akvncsdkyg ttplvwaark
      181 ghlecvkhll amgadvdqeg ansmtaliva vkggytqsvk eilkrnpnvn ltdkdgntal
      241 miaskeghte ivqdlldagt yvnipdrsgd tvligavrgg hveivrallq kyadidirgq
      301 dnktalywav ekgnatmvrd ilqcnpdtei ctkdgetpli katkmrniev vellldkgak
      361 vsavdkkgdt plhiairgrs rklaelllrn pkdgrllyrp nkagetpyni dcshqksilt
      421 qifgarhlsp tetdgdmlgy dlyssaladi lseptmqppi cvglyaqwgs gksfllkkle
      481 demktfagqq ieplfqfswl ivfltlllcg glgllfaftv hpnlgiavsl sflallyiff
      541 iviyfggrre geswnwawvl strlarhigy lelllklmfv nppelpeqtt kalpvrflft
      601 dynrlssvgg etslaemiat lsdacerefg flatrlfrvf ktedtqgkkk wkktcclpsf
      661 viflfiigci isgitllaif rvdpkhltvn avlisiasvv glafvlncrt wwqvldslln
      721 sqrkrlhnaa sklhklkseg fmkvlkceve lmarmaktid sftqnqtrlv viidgldace
      781 qdkvlqmldt vrvlfskgpf iaifasdphi iikainqnln svlrdsning hdymrnivhl
      841 pvflnsrgls narkflvtsa tngdvpcsdt tgiqedadrr vsqnslgemt klgsktalnr
      901 rdtyrrrqmq rtitrqmsfd ltkllvtedw fsdispqtmr rllnivsvtg rllranqisf
      961 nwdrlaswin lteqwpyrts wlilyleete gipdqmtlkt iyerisknip ttkdveplle
     1021 idgdirnfev flssrtpvlv ardvkvflpc tvnldpklre iiadvraare qisigglayp
     1081 plplhegppr apsgysqpps vcsstsfngp faggvvspqp hssyysgmtg pqhpfynrpf
     1141 fapylytpry ypggsqhlis rpsvktslpr dqnnglgsgp apgpvvllns lnvdavcekl
     1201 kqiegldqsm lpqycttikk aningrvlaq cnidelkkem nmnfgdwhlf rstvlemrna
     1261 eshvvpedpr flsesssgpa phgeparras hnelphtels sqtpytlnfs feelntlgld
     1321 egaprhsnls wqsqtrrtps lsslnsqdss ieiskltdkv qaeyrdayre yiaqmsqleg
     1381 gpgsttisgr ssphstyymg qsssggsihs nleqekgkds epkpddgrks flmkrgdvid
     1441 ysssgvstnd aspldpitee deksdqsgsk llpgkksser sslfqtdlkl kgsglryqkl
     1501 psdedesgte esdntpllkd dkdrkaegkv ervpkspehs aepirtfika keylsdalld
     1561 kkdssdsgvr ssesspnhsl hnevaddsql ekanlieled dshsgkrgip hslsglqdpi
     1621 iarmsicsed kkspsecsli asspeenwpa cqkaynlnrt pstvtlnnns apanranqnf
     1681 demegirets qvilrpsssp npttiqnenl ksmthkrsqr ssytrlskdp pelhaaasse
     1741 stgfgeeres il
//
LOCUS       NP_001304897             442 aa            linear   PRI 21-NOV-2025
DEFINITION  arrestin domain-containing protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001304897 XP_005266178
VERSION     NP_001304897.1
DBSOURCE    REFSEQ: accession NM_001317968.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Lee,K.T., Pranoto,I.K.A., Kim,S.Y., Choi,H.J., To,N.B., Chae,H.,
            Lee,J.Y., Kim,J.E., Kwon,Y.V. and Nam,J.W.
  TITLE     Comparative interactome analysis of alpha-arrestin families in
            human and Drosophila
  JOURNAL   Elife 12, 88328 (2024)
   PUBMED   38270169
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Zhao,Q., Jiang,F., Zhuang,H., Chu,Y., Zhang,F. and Wang,C.
  TITLE     MicroRNA miR-124-3p suppresses proliferation and
            epithelial-mesenchymal transition of hepatocellular carcinoma via
            ARRDC1 (arrestin domain containing 1)
  JOURNAL   Bioengineered 13 (4), 8255-8265 (2022)
   PUBMED   35300565
  REMARK    GeneRIF: MicroRNA miR-124-3p suppresses proliferation and
            epithelial-mesenchymal transition of hepatocellular carcinoma via
            ARRDC1 (arrestin domain containing 1).
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Xu,H., Yu,X., Yang,Z., Song,Q., Cheng,S., He,Z. and Dai,L.
  TITLE     PAX5-activated lncRNA ARRDC1-AS1 accelerates the autophagy and
            progression of DLBCL through sponging miR-2355-5p to regulate ATG5
  JOURNAL   Life Sci 286, 119932 (2021)
   PUBMED   34499929
  REMARK    GeneRIF: PAX5-activated lncRNA ARRDC1-AS1 accelerates the autophagy
            and progression of DLBCL through sponging miR-2355-5p to regulate
            ATG5.
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Nabhan,J.F., Hu,R., Oh,R.S., Cohen,S.N. and Lu,Q.
  TITLE     Formation and release of arrestin domain-containing protein
            1-mediated microvesicles (ARMMs) at plasma membrane by recruitment
            of TSG101 protein
  JOURNAL   Proc Natl Acad Sci U S A 109 (11), 4146-4151 (2012)
   PUBMED   22315426
REFERENCE   7  (residues 1 to 442)
  AUTHORS   Shea,F.F., Rowell,J.L., Li,Y., Chang,T.H. and Alvarez,C.E.
  TITLE     Mammalian alpha arrestins link activated seven transmembrane
            receptors to Nedd4 family e3 ubiquitin ligases and interact with
            beta arrestins
  JOURNAL   PLoS One 7 (12), e50557 (2012)
   PUBMED   23236378
REFERENCE   8  (residues 1 to 442)
  AUTHORS   Rauch,S. and Martin-Serrano,J.
  TITLE     Multiple interactions between the ESCRT machinery and
            arrestin-related proteins: implications for PPXY-dependent budding
  JOURNAL   J Virol 85 (7), 3546-3556 (2011)
   PUBMED   21191027
  REMARK    GeneRIF: The authors show that WWP1 changes the ubiquitination
            status of ARRDC1, suggesting that the arrestins may provide a
            platform for ubiquitination in PPXY-dependent budding.
REFERENCE   9  (residues 1 to 442)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   10 (residues 1 to 442)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI906381.1, AK308376.1, AL365502.57, AK001822.1 and AA552336.1.
            
            On Dec 17, 2015 this sequence version replaced XP_005266178.1.
            
            Transcript Variant: This variant (2) retains an intron in the 3'
            coding region, compared to variant 1. The encoded protein (isoform
            2) is shorter and has a distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK308376.1, SRR18074969.142044.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..442
                     /product="arrestin domain-containing protein 1 isoform 2"
                     /note="arrestin domain-containing protein 1;
                     alpha-arrestin 1"
                     /calculated_mol_wt=46815
     Region          7..139
                     /region_name="Arrestin_N"
                     /note="Arrestin (or S-antigen), N-terminal domain;
                     cl22903"
                     /db_xref="CDD:451447"
     Region          162..284
                     /region_name="Arrestin_C"
                     /note="Arrestin (or S-antigen), C-terminal domain;
                     pfam02752"
                     /db_xref="CDD:460676"
     Region          296..322
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5I2.1)"
     Region          349..372
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5I2.1)"
     Region          402..405
                     /region_name="PPxY motif 1.
                     /evidence=ECO:0000269|PubMed:23886940"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5I2.1)"
     CDS             1..442
                     /gene="ARRDC1"
                     /coded_by="NM_001317968.2:33..1361"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:92714"
                     /db_xref="HGNC:HGNC:28633"
                     /db_xref="MIM:619768"
ORIGIN      
        1 mgrvqlfeis lshgrvvysp geplagtvrv rlgaplpfra irvtcigscg vsnkandtaw
       61 vveegyfnss lsladkgslp agehsfpfqf llpataptsf egpfgkivhq vraaihtprf
      121 skdhkcslvf yilsplnlns ipdieqpnva satkkfsykl vktgsvvlta stdlrgyvvg
      181 qalqlhadve nqsgkdtspv vasllqkvsy kakrwihdvr tiaevegagv kawrraqwhe
      241 qilvpalpqs alpgcslihi dyylqvslka peatvtlpvf igniavnhap vsprpglglp
      301 pgapplvvps appqeeaeae aaaggphfld pvflstkshs qrqpllatls svpgapepcp
      361 qdgspashpl hpplcistga tvpyfaegsg gpvpttstli lppeysswgy pygestaraw
      421 qggdaksptq tllssrrgpt vl
//
LOCUS       NP_001352566            1471 aa            linear   PRI 21-NOV-2025
DEFINITION  protein TASOR isoform f [Homo sapiens].
ACCESSION   NP_001352566 XP_016861519
VERSION     NP_001352566.1
DBSOURCE    REFSEQ: accession NM_001365637.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1471)
  AUTHORS   Jensvold,Z.D., Flood,J.R., Christenson,A.E. and Lewis,P.W.
  TITLE     Interplay between Two Paralogous Human Silencing Hub (HuSH)
            Complexes in Regulating LINE-1 Element Silencing
  JOURNAL   Nat Commun 15 (1), 9492 (2024)
   PUBMED   39489739
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1471)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   3  (residues 1 to 1471)
  AUTHORS   Vauthier,V., Lasserre,A., Morel,M., Versapuech,M.,
            Berlioz-Torrent,C., Zamborlini,A., Margottin-Goguet,F. and
            Matkovic,R.
  TITLE     HUSH-mediated HIV silencing is independent of TASOR phosphorylation
            on threonine 819
  JOURNAL   Retrovirology 19 (1), 23 (2022)
   PUBMED   36309692
  REMARK    GeneRIF: HUSH-mediated HIV silencing is independent of TASOR
            phosphorylation on threonine 819.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1471)
  AUTHORS   Matkovic,R., Morel,M., Lanciano,S., Larrous,P., Martin,B.,
            Bejjani,F., Vauthier,V., Hansen,M.M.K., Emiliani,S., Cristofari,G.,
            Gallois-Montbrun,S. and Margottin-Goguet,F.
  TITLE     TASOR epigenetic repressor cooperates with a CNOT1 RNA degradation
            pathway to repress HIV
  JOURNAL   Nat Commun 13 (1), 66 (2022)
   PUBMED   35013187
  REMARK    GeneRIF: TASOR epigenetic repressor cooperates with a CNOT1 RNA
            degradation pathway to repress HIV.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1471)
  AUTHORS   Douse,C.H., Tchasovnikarova,I.A., Timms,R.T., Protasio,A.V.,
            Seczynska,M., Prigozhin,D.M., Albecka,A., Wagstaff,J.,
            Williamson,J.C., Freund,S.M.V., Lehner,P.J. and Modis,Y.
  TITLE     TASOR is a pseudo-PARP that directs HUSH complex assembly and
            epigenetic transposon control
  JOURNAL   Nat Commun 11 (1), 4940 (2020)
   PUBMED   33009411
  REMARK    GeneRIF: TASOR is a pseudo-PARP that directs HUSH complex assembly
            and epigenetic transposon control.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1471)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   7  (residues 1 to 1471)
  AUTHORS   Lango Allen,H., Estrada,K., Lettre,G., Berndt,S.I., Weedon,M.N.,
            Rivadeneira,F., Willer,C.J., Jackson,A.U., Vedantam,S.,
            Raychaudhuri,S., Ferreira,T., Wood,A.R., Weyant,R.J., Segre,A.V.,
            Speliotes,E.K., Wheeler,E., Soranzo,N., Park,J.H., Yang,J.,
            Gudbjartsson,D., Heard-Costa,N.L., Randall,J.C., Qi,L., Vernon
            Smith,A., Magi,R., Pastinen,T., Liang,L., Heid,I.M., Luan,J.,
            Thorleifsson,G., Winkler,T.W., Goddard,M.E., Sin Lo,K., Palmer,C.,
            Workalemahu,T., Aulchenko,Y.S., Johansson,A., Zillikens,M.C.,
            Feitosa,M.F., Esko,T., Johnson,T., Ketkar,S., Kraft,P., Mangino,M.,
            Prokopenko,I., Absher,D., Albrecht,E., Ernst,F., Glazer,N.L.,
            Hayward,C., Hottenga,J.J., Jacobs,K.B., Knowles,J.W., Kutalik,Z.,
            Monda,K.L., Polasek,O., Preuss,M., Rayner,N.W., Robertson,N.R.,
            Steinthorsdottir,V., Tyrer,J.P., Voight,B.F., Wiklund,F., Xu,J.,
            Zhao,J.H., Nyholt,D.R., Pellikka,N., Perola,M., Perry,J.R.,
            Surakka,I., Tammesoo,M.L., Altmaier,E.L., Amin,N., Aspelund,T.,
            Bhangale,T., Boucher,G., Chasman,D.I., Chen,C., Coin,L.,
            Cooper,M.N., Dixon,A.L., Gibson,Q., Grundberg,E., Hao,K., Juhani
            Junttila,M., Kaplan,L.M., Kettunen,J., Konig,I.R., Kwan,T.,
            Lawrence,R.W., Levinson,D.F., Lorentzon,M., McKnight,B.,
            Morris,A.P., Muller,M., Suh Ngwa,J., Purcell,S., Rafelt,S.,
            Salem,R.M., Salvi,E., Sanna,S., Shi,J., Sovio,U., Thompson,J.R.,
            Turchin,M.C., Vandenput,L., Verlaan,D.J., Vitart,V., White,C.C.,
            Ziegler,A., Almgren,P., Balmforth,A.J., Campbell,H., Citterio,L.,
            De Grandi,A., Dominiczak,A., Duan,J., Elliott,P., Elosua,R.,
            Eriksson,J.G., Freimer,N.B., Geus,E.J., Glorioso,N., Haiqing,S.,
            Hartikainen,A.L., Havulinna,A.S., Hicks,A.A., Hui,J., Igl,W.,
            Illig,T., Jula,A., Kajantie,E., Kilpelainen,T.O., Koiranen,M.,
            Kolcic,I., Koskinen,S., Kovacs,P., Laitinen,J., Liu,J., Lokki,M.L.,
            Marusic,A., Maschio,A., Meitinger,T., Mulas,A., Pare,G.,
            Parker,A.N., Peden,J.F., Petersmann,A., Pichler,I.,
            Pietilainen,K.H., Pouta,A., Ridderstrale,M., Rotter,J.I.,
            Sambrook,J.G., Sanders,A.R., Schmidt,C.O., Sinisalo,J., Smit,J.H.,
            Stringham,H.M., Bragi Walters,G., Widen,E., Wild,S.H.,
            Willemsen,G., Zagato,L., Zgaga,L., Zitting,P., Alavere,H.,
            Farrall,M., McArdle,W.L., Nelis,M., Peters,M.J., Ripatti,S., van
            Meurs,J.B., Aben,K.K., Ardlie,K.G., Beckmann,J.S., Beilby,J.P.,
            Bergman,R.N., Bergmann,S., Collins,F.S., Cusi,D., den Heijer,M.,
            Eiriksdottir,G., Gejman,P.V., Hall,A.S., Hamsten,A., Huikuri,H.V.,
            Iribarren,C., Kahonen,M., Kaprio,J., Kathiresan,S., Kiemeney,L.,
            Kocher,T., Launer,L.J., Lehtimaki,T., Melander,O., Mosley,T.H. Jr.,
            Musk,A.W., Nieminen,M.S., O'Donnell,C.J., Ohlsson,C., Oostra,B.,
            Palmer,L.J., Raitakari,O., Ridker,P.M., Rioux,J.D., Rissanen,A.,
            Rivolta,C., Schunkert,H., Shuldiner,A.R., Siscovick,D.S.,
            Stumvoll,M., Tonjes,A., Tuomilehto,J., van Ommen,G.J., Viikari,J.,
            Heath,A.C., Martin,N.G., Montgomery,G.W., Province,M.A., Kayser,M.,
            Arnold,A.M., Atwood,L.D., Boerwinkle,E., Chanock,S.J., Deloukas,P.,
            Gieger,C., Gronberg,H., Hall,P., Hattersley,A.T., Hengstenberg,C.,
            Hoffman,W., Lathrop,G.M., Salomaa,V., Schreiber,S., Uda,M.,
            Waterworth,D., Wright,A.F., Assimes,T.L., Barroso,I., Hofman,A.,
            Mohlke,K.L., Boomsma,D.I., Caulfield,M.J., Cupples,L.A.,
            Erdmann,J., Fox,C.S., Gudnason,V., Gyllensten,U., Harris,T.B.,
            Hayes,R.B., Jarvelin,M.R., Mooser,V., Munroe,P.B., Ouwehand,W.H.,
            Penninx,B.W., Pramstaller,P.P., Quertermous,T., Rudan,I.,
            Samani,N.J., Spector,T.D., Volzke,H., Watkins,H., Wilson,J.F.,
            Groop,L.C., Haritunians,T., Hu,F.B., Kaplan,R.C., Metspalu,A.,
            North,K.E., Schlessinger,D., Wareham,N.J., Hunter,D.J.,
            O'Connell,J.R., Strachan,D.P., Wichmann,H.E., Borecki,I.B., van
            Duijn,C.M., Schadt,E.E., Thorsteinsdottir,U., Peltonen,L.,
            Uitterlinden,A.G., Visscher,P.M., Chatterjee,N., Loos,R.J.,
            Boehnke,M., McCarthy,M.I., Ingelsson,E., Lindgren,C.M.,
            Abecasis,G.R., Stefansson,K., Frayling,T.M. and Hirschhorn,J.N.
  TITLE     Hundreds of variants clustered in genomic loci and biological
            pathways affect human height
  JOURNAL   Nature 467 (7317), 832-838 (2010)
   PUBMED   20881960
REFERENCE   8  (residues 1 to 1471)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   9  (residues 1 to 1471)
  AUTHORS   Eichmuller,S., Usener,D., Dummer,R., Stein,A., Thiel,D. and
            Schadendorf,D.
  TITLE     Serological detection of cutaneous T-cell lymphoma-associated
            antigens
  JOURNAL   Proc Natl Acad Sci U S A 98 (2), 629-634 (2001)
   PUBMED   11149944
REFERENCE   10 (residues 1 to 1471)
  AUTHORS   Li,Q., Wen,H. and Ao,S.
  TITLE     Identification and cloning of the cDNA of a Rb-associated protein
            RAP140a
  JOURNAL   Sci China C Life Sci 43 (6), 637-647 (2000)
   PUBMED   18726359
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099781.2.
            
            On Sep 6, 2018 this sequence version replaced XP_016861519.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.154555.1,
                                           SRR1660809.203204.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1471
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.3"
     Protein         1..1471
                     /product="protein TASOR isoform f"
                     /note="retinoblastoma-associated protein 140; CTCL tumor
                     antigen se89-1; retinoblastoma-associated protein RAP140;
                     protein FAM208A; transgene activation suppressor protein;
                     protein TASOR; family with sequence similarity 208 member
                     A"
                     /calculated_mol_wt=166023
     Region          166..319
                     /region_name="DUF3715"
                     /note="Protein of unknown function (DUF3715); pfam12509"
                     /db_xref="CDD:463613"
     Region          973..1054
                     /region_name="TASOR_PBD"
                     /note="periphilin binding domain of protein TASOR and
                     similar proteins; cd22569"
                     /db_xref="CDD:439336"
     Site            order(973,975..977,979..980,983..984,987..988,990..991,
                     994..995,998..999,1002,1004..1011,1031,1033..1037,
                     1040..1041,1043..1044,1047..1048,1051..1052)
                     /site_type="other"
                     /note="periphilin binding site [polypeptide binding]"
                     /db_xref="CDD:439336"
     CDS             1..1471
                     /gene="TASOR"
                     /gene_synonym="C3orf63; FAM208A; RAP140; se89-1; TASOR1"
                     /coded_by="NM_001365637.2:260..4675"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="GeneID:23272"
                     /db_xref="HGNC:HGNC:30314"
                     /db_xref="MIM:616493"
ORIGIN      
        1 mataveteac qptdaswesg gggddemkqa lpelessqqn ggggglniae psggagreen
       61 agaeaaqsls heqpqdssea gaaalprgpe eperpvrrsf qiprksrekk alfqpltpgs
      121 refedvvnil hssyleptsv tnfnyrracl vhnellekef tekrrelkfd grldkelses
      181 yaflmvdryq vqticekglh vgqskitilg spsmgvylsr yadllqanpl dtgamgdvvi
      241 fkimkgkiks iydpmgvksl esmlnksald ptpkhechvs knanritsll ayrayeltqy
      301 yfyeygfdel rrrprhvcpy avvsftykdd iqtpkfvpss rsnsfntdrn idkynytlwk
      361 gqllnkgkll cyislrsatr aflpiklpek ldvetvmsid hlkqkippal fyketylgpn
      421 evlkngmycs lyevvektri gsnmesllqk ldreklvlvk plgdrgylfl lspyqmvppy
      481 eyqtaksrvl halflfqepr sivtsqkgst naapqerhes mpdvlkiaqf lqfsliqcrk
      541 efknisainf hsvvekyvse ffkrgfgsgk refimfpyds rlddkkflys aprnkshidt
      601 clhayifrpe vyqlpicklk elfeenrklq qfsplsdyeg qeeemngtkm kfgkrnnsrg
      661 eaiisgkqrs shsldydkdr vkelinliqc rkksvggdsd tedmrsktvl krkledlpen
      721 mrklaktsnl senchlyees pqpigslghd adlrrqqqdt cnsgiadihr lfnwlsetla
      781 narhsdaslt dtvnkalgls tddayeelrq kheyelnstp dkkdyeqptc akvenaqfkg
      841 tqslllevda tskysvaist sevgtdhklh lkedpnlisv nnfedcslcp svpiehgfrr
      901 qqsksnnvee teihwklipi tggnarsped qlgkhgekqt pdtlkgtted dvltgqveeq
      961 cvpaaeaepp avsettertv lgeynlfsrk ieeilkqknv syvstvstpi fstqekmkrl
     1021 sefiysktsk agvqefvdgl heklntiiik asakggnlpp vspndsgaki asnplerhvi
     1081 pvsssdfnnk hlleplcsdp lkdtnsdeqh stsaltevem nqpqhatelm vtsdhivpgd
     1141 marepveett kspsdvnisa qpalsnfisq lepevfnslv kimkdvqknt vkfyiheeee
     1201 svlckeikey liklgntech peqflerrsk ldklliiiqn ediagfihki pglvtlkklp
     1261 cvsfagvdsl ddvknhtyne lfvsggfivs desilnpevv tvenlknflt fleelstpeg
     1321 kwqwkvhckf qkklkelgrl nakalslltl lnvyqkkhlv eilsyhncds qtrnapeldc
     1381 lirlqaqniq qrhivfltek nikmlssytd ngivvataed fmqnfknlvg yhnsiteenl
     1441 pqlganenle sqsdavltlt plelgvgisq h
//
LOCUS       NP_068814                639 aa            linear   PRI 21-NOV-2025
DEFINITION  heat shock-related 70 kDa protein 2 [Homo sapiens].
ACCESSION   NP_068814
VERSION     NP_068814.2
DBSOURCE    REFSEQ: accession NM_021979.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 639)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 639)
  AUTHORS   Sojka,D.R., Gogler,A., Kania,D., Vydra,N., Wiecha,K.,
            Adamiec-Organisciok,M., Wilk,A., Chumak,V., Matysniak,D. and
            Scieglinska,D.
  TITLE     The human testis-enriched HSPA2 interacts with HIF-1alpha in
            epidermal keratinocytes, yet HIF-1alpha stability and
            HIF-1-dependent gene expression rely on the HSPA (HSP70) activity
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (5), 119735 (2024)
   PUBMED   38641179
  REMARK    GeneRIF: The human testis-enriched HSPA2 interacts with HIF-1alpha
            in epidermal keratinocytes, yet HIF-1alpha stability and
            HIF-1-dependent gene expression rely on the HSPA (HSP70) activity.
REFERENCE   3  (residues 1 to 639)
  AUTHORS   Dong,Y., Li,T., Ma,Z., Zhou,C., Wang,X. and Li,J.
  TITLE     HSPA1A, HSPA2, and HSPA8 Are Potential Molecular Biomarkers for
            Prognosis among HSP70 Family in Alzheimer's Disease
  JOURNAL   Dis Markers 2022, 9480398 (2022)
   PUBMED   36246562
  REMARK    GeneRIF: HSPA1A, HSPA2, and HSPA8 Are Potential Molecular
            Biomarkers for Prognosis among HSP70 Family in Alzheimer's Disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 639)
  AUTHORS   Zhai,L.L., Qiao,P.P., Sun,Y.S., Ju,T.F. and Tang,Z.G.
  TITLE     Tumorigenic and immunological roles of Heat shock protein A2 in
            pancreatic cancer: a bioinformatics analysis
  JOURNAL   Rev Assoc Med Bras (1992) 68 (4), 470-475 (2022)
   PUBMED   35649069
  REMARK    GeneRIF: Tumorigenic and immunological roles of Heat shock protein
            A2 in pancreatic cancer: a bioinformatics analysis.
REFERENCE   5  (residues 1 to 639)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 639)
  AUTHORS   Allen,J.W., Dix,D.J., Collins,B.W., Merrick,B.A., He,C.,
            Selkirk,J.K., Poorman-Allen,P., Dresser,M.E. and Eddy,E.M.
  TITLE     HSP70-2 is part of the synaptonemal complex in mouse and hamster
            spermatocytes
  JOURNAL   Chromosoma 104 (6), 414-421 (1996)
   PUBMED   8601336
REFERENCE   7  (residues 1 to 639)
  AUTHORS   Roux,A.F., Nguyen,V.T., Squire,J.A. and Cox,D.W.
  TITLE     A heat shock gene at 14q22: mapping and expression
  JOURNAL   Hum Mol Genet 3 (10), 1819-1822 (1994)
   PUBMED   7849706
REFERENCE   8  (residues 1 to 639)
  AUTHORS   Bonnycastle,L.L., Yu,C.E., Hunt,C.R., Trask,B.J., Clancy,K.P.,
            Weber,J.L., Patterson,D. and Schellenberg,G.D.
  TITLE     Cloning, sequencing, and mapping of the human chromosome 14 heat
            shock protein gene (HSPA2)
  JOURNAL   Genomics 23 (1), 85-93 (1994)
   PUBMED   7829106
REFERENCE   9  (residues 1 to 639)
  AUTHORS   Schwab,C.G., Bozak,C.K., Whitehouse,N.L. and Olson,V.M.
  TITLE     Amino acid limitation and flow to the duodenum at four stages of
            lactation. 2. Extent of lysine limitation
  JOURNAL   J Dairy Sci 75 (12), 3503-3518 (1992)
   PUBMED   1474216
REFERENCE   10 (residues 1 to 639)
  AUTHORS   Dworniczak,B. and Mirault,M.E.
  TITLE     Structure and expression of a human gene coding for a 71 kd heat
            shock 'cognate' protein
  JOURNAL   Nucleic Acids Res 15 (13), 5181-5197 (1987)
   PUBMED   3037489
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB042367.1, CN356507.1, CD300159.1, BC036107.1 and BC001752.1.
            
            On Apr 19, 2001 this sequence version replaced NP_068814.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: GQ891480.1, BC036107.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000247207.7/ ENSP00000247207.6
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..639
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..639
                     /product="heat shock-related 70 kDa protein 2"
                     /note="heat shock 70kD protein 2; heat shock 70kDa protein
                     2; epididymis secretory sperm binding protein; heat shock
                     protein family A member 2"
                     /calculated_mol_wt=69890
     Region          2..615
                     /region_name="PTZ00009"
                     /note="heat shock 70 kDa protein; Provisional"
                     /db_xref="CDD:240227"
     Region          2..389
                     /region_name="Nucleotide-binding domain (NBD).
                     /evidence=ECO:0000250|UniProtKB:P11142"
                     /note="propagated from UniProtKB/Swiss-Prot (P54652.1)"
     Region          397..512
                     /region_name="Substrate-binding domain (SBD).
                     /evidence=ECO:0000250|UniProtKB:P11142"
                     /note="propagated from UniProtKB/Swiss-Prot (P54652.1)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P14659; propagated from
                     UniProtKB/Swiss-Prot (P54652.1)"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P14659; propagated from
                     UniProtKB/Swiss-Prot (P54652.1)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P14659; propagated from
                     UniProtKB/Swiss-Prot (P54652.1)"
     Site            564
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, by METTL21A, in vitro.
                     /evidence=ECO:0000269|PubMed:23921388; propagated from
                     UniProtKB/Swiss-Prot (P54652.1)"
     Region          613..639
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54652.1)"
     CDS             1..639
                     /gene="HSPA2"
                     /gene_synonym="HSP70-2; HSP70-3"
                     /coded_by="NM_021979.4:110..2029"
                     /db_xref="CCDS:CCDS9766.1"
                     /db_xref="GeneID:3306"
                     /db_xref="HGNC:HGNC:5235"
                     /db_xref="MIM:140560"
ORIGIN      
        1 msargpaigi dlgttyscvg vfqhgkveii andqgnrttp syvaftdter ligdaaknqv
       61 amnptntifd akrligrkfe datvqsdmkh wpfrvvsegg kpkvqveykg etktffpeei
      121 ssmvltkmke iaeaylggkv hsavitvpay fndsqrqatk dagtitglnv lriineptaa
      181 aiaygldkkg caggeknvli fdlgggtfdv siltiedgif evkstagdth lggedfdnrm
      241 vshlaeefkr khkkdigpnk ravrrlrtac erakrtlsss tqasieidsl yegvdfytsi
      301 trarfeelna dlfrgtlepv ekalrdakld kgqiqeivlv ggstripkiq kllqdffngk
      361 elnksinpde avaygaavqa ailigdksen vqdlllldvt plslgietag gvmtplikrn
      421 ttiptkqtqt fttysdnqss vlvqvyeger amtkdnnllg kfdltgippa prgvpqievt
      481 fdidangiln vtaadkstgk enkititndk grlskddidr mvqeaeryks edeanrdrva
      541 aknalesyty nikqtvedek lrgkiseqdk nkildkcqev inwldrnqma ekdeyehkqk
      601 elervcnpii sklyqggpgg gsggggsgas ggptieevd
//
LOCUS       NP_001307976             932 aa            linear   PRI 21-NOV-2025
DEFINITION  PMS1 protein homolog 1 isoform a [Homo sapiens].
ACCESSION   NP_001307976 XP_011509655
VERSION     NP_001307976.1
DBSOURCE    REFSEQ: accession NM_001321047.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 932)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 932)
  AUTHORS   Landry,K.K., Seward,D.J., Dragon,J.A., Slavik,M., Xu,K.,
            McKinnon,W.C., Colello,L., Sweasy,J., Wallace,S.S., Cuke,M. and
            Wood,M.E.
  TITLE     Investigation of discordant sibling pairs from hereditary breast
            cancer families and analysis of a rare PMS1 variant
  JOURNAL   Cancer Genet 260-261, 30-36 (2022)
   PUBMED   34852986
  REMARK    GeneRIF: Investigation of discordant sibling pairs from hereditary
            breast cancer families and analysis of a rare PMS1 variant.
REFERENCE   3  (residues 1 to 932)
  AUTHORS   Graur,F., Puia,A., Mois,E., Pop,P., Berar,M., Elisei,R.,
            Zaharie,F., Nechita,V., Rusu,I., Buiga,R., Puia,C. and Al Hajjar,N.
  TITLE     Analysis of the MLH1, MLH2, MLH6, PMS2 genes and their correlations
            with clinical data in rectal mucinous adenocarcinoma
  JOURNAL   Ann Ital Chir 93, 188-194 (2022)
   PUBMED   34807001
  REMARK    GeneRIF: Analysis of the MLH1, MLH2, MLH6, PMS2 genes and their
            correlations with clinical data in rectal mucinous adenocarcinoma.
REFERENCE   4  (residues 1 to 932)
  AUTHORS   Kim,M., Park,J., Bouhaddou,M., Kim,K., Rojc,A., Modak,M.,
            Soucheray,M., McGregor,M.J., O'Leary,P., Wolf,D., Stevenson,E.,
            Foo,T.K., Mitchell,D., Herrington,K.A., Munoz,D.P., Tutuncuoglu,B.,
            Chen,K.H., Zheng,F., Kreisberg,J.F., Diolaiti,M.E., Gordan,J.D.,
            Coppe,J.P., Swaney,D.L., Xia,B., van 't Veer,L., Ashworth,A.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein interaction landscape of breast cancer
  JOURNAL   Science 374 (6563), eabf3066 (2021)
   PUBMED   34591612
REFERENCE   5  (residues 1 to 932)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 932)
  AUTHORS   Kolodner,R.
  TITLE     Biochemistry and genetics of eukaryotic mismatch repair
  JOURNAL   Genes Dev 10 (12), 1433-1442 (1996)
   PUBMED   8666228
  REMARK    Review article
REFERENCE   7  (residues 1 to 932)
  AUTHORS   Horii,A., Han,H.J., Sasaki,S., Shimada,M. and Nakamura,Y.
  TITLE     Cloning, characterization and chromosomal assignment of the human
            genes homologous to yeast PMS1, a member of mismatch repair genes
  JOURNAL   Biochem Biophys Res Commun 204 (3), 1257-1264 (1994)
   PUBMED   7980603
REFERENCE   8  (residues 1 to 932)
  AUTHORS   Nicolaides,N.C., Papadopoulos,N., Liu,B., Wei,Y.F., Carter,K.C.,
            Ruben,S.M., Rosen,C.A., Haseltine,W.A., Fleischmann,R.D.,
            Fraser,C.M. et al.
  TITLE     Mutations of two PMS homologues in hereditary nonpolyposis colon
            cancer
  JOURNAL   Nature 371 (6492), 75-80 (1994)
   PUBMED   8072530
REFERENCE   9  (residues 1 to 932)
  AUTHORS   Papadopoulos,N., Nicolaides,N.C., Wei,Y.F., Ruben,S.M.,
            Carter,K.C., Rosen,C.A., Haseltine,W.A., Fleischmann,R.D.,
            Fraser,C.M., Adams,M.D. et al.
  TITLE     Mutation of a mutL homolog in hereditary colon cancer
  JOURNAL   Science 263 (5153), 1625-1629 (1994)
   PUBMED   8128251
REFERENCE   10 (residues 1 to 932)
  AUTHORS   Idos,G. and Valle,L.
  TITLE     Lynch Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301390
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC347859.1, BG772717.1,
            AC013468.12, BC096332.1, AK316215.1 and BM677668.1.
            
            On Mar 12, 2016 this sequence version replaced XP_011509655.1.
            
            Summary: This gene encodes a protein belonging to the DNA mismatch
            repair mutL/hexB family. This protein is thought to be involved in
            the repair of DNA mismatches, and it can form heterodimers with
            MLH1, a known DNA mismatch repair protein. Mutations in this gene
            cause hereditary nonpolyposis colorectal cancer type 3 (HNPCC3)
            either alone or in combination with mutations in other genes
            involved in the HNPCC phenotype, which is also known as Lynch
            syndrome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.122237.1,
                                           SRR1803611.7784.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.2"
     Protein         1..932
                     /product="PMS1 protein homolog 1 isoform a"
                     /note="human homolog of yeast mutL; PMS1 postmeiotic
                     segregation increased 1; PMS1 protein homolog 1; mismatch
                     repair gene PMSL1; rhabdomyosarcoma antigen MU-RMS-40.10B;
                     rhabdomyosarcoma antigen MU-RMS-40.10E; DNA mismatch
                     repair protein PMS1"
                     /calculated_mol_wt=105700
     Region          1..318
                     /region_name="mutl"
                     /note="DNA mismatch repair protein MutL; TIGR00585"
                     /db_xref="CDD:273155"
     Region          465..493
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54277.1)"
     Region          571..642
                     /region_name="HMG-box_PMS1"
                     /note="high mobility group (HMG)-box found in PMS1 protein
                     homolog 1 (PMS1) and similar proteins; cd21985"
                     /db_xref="CDD:438801"
     Site            order(572..573,575..579,582..583,590,602..603,606,
                     609..610,617,621,624,628,631)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438801"
     CDS             1..932
                     /gene="PMS1"
                     /gene_synonym="HNPCC3; hPMS1; MLH2; PMSL1"
                     /coded_by="NM_001321047.2:342..3140"
                     /note="isoform a is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS2302.1"
                     /db_xref="GeneID:5378"
                     /db_xref="HGNC:HGNC:9121"
                     /db_xref="MIM:600258"
ORIGIN      
        1 mkqlpaatvr llsssqiits vvsvvkelie nsldagatsv dvklenygfd kievrdngeg
       61 ikavdapvma mkyytskins hedlenltty gfrgealgsi cciaevlitt rtaadnfstq
      121 yvldgsghil sqkpshlgqg ttvtalrlfk nlpvrkqfys takkckdeik kiqdllmsfg
      181 ilkpdlrivf vhnkaviwqk srvsdhkmal msvlgtavmn nmesfqyhse esqiylsgfl
      241 pkcdadhsft slstpersfi finsrpvhqk dilklirhhy nlkclkestr lypvfflkid
      301 vptadvdvnl tpdksqvllq nkesvliale nlmttcygpl pstnsyennk tdvsaadivl
      361 sktaetdvlf nkvessgkny snvdtsvipf qndmhndesg kntddclnhq isigdfgygh
      421 csseisnidk ntknafqdis msnvswensq teysktcfis svkhtqseng nkdhidesge
      481 neeeaglens seisadewsr gnilknsvge niepvkilvp ekslpckvsn nnypipeqmn
      541 lnedscnkks nvidnksgkv taydllsnrv ikkpmsasal fvqdhrpqfl ienpktsled
      601 atlqieelwk tlseeeklky eekatkdler ynsqmkraie qesqmslkdg rkkikptsaw
      661 nlaqkhklkt slsnqpklde llqsqiekrr sqnikmvqip fsmknlkinf kkqnkvdlee
      721 kdepclihnl rfpdawlmts ktevmllnpy rveeallfkr llenhklpae plekpimlte
      781 slfngshyld vlykmtaddq rysgstylsd prltangfki klipgvsite nyleiegman
      841 clpfygvadl keilnailnr nakevyecrp rkvisylege avrlsrqlpm ylskediqdi
      901 iyrmkhqfgn eikecvhgrp ffhhltylpe tt
//
LOCUS       NP_001229314             583 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase MAK isoform 2 [Homo sapiens].
ACCESSION   NP_001229314
VERSION     NP_001229314.1
DBSOURCE    REFSEQ: accession NM_001242385.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Gray,J.M., Orlans,H.O., Shanks,M., Clouston,P. and MacLaren,R.E.
  TITLE     Slowly progressive retinitis pigmentosa caused by two novel
            mutations in the MAK gene
  JOURNAL   Ophthalmic Genet 39 (4), 508-511 (2018)
   PUBMED   29781741
  REMARK    GeneRIF: The natural history of this individual's retinitis
            pigmentosa (RP) is consistent with previously described MAK
            mutations, being significantly milder than that associated with
            other photoreceptor ciliopathies. We suggest inclusion of MAK as
            part of wider genetic testing in all individuals presenting with
            RP.
REFERENCE   3  (residues 1 to 583)
  AUTHORS   Kimchi,A., Khateb,S., Wen,R., Guan,Z., Obolensky,A., Beryozkin,A.,
            Kurtzman,S., Blumenfeld,A., Pras,E., Jacobson,S.G., Ben-Yosef,T.,
            Newman,H., Sharon,D. and Banin,E.
  TITLE     Nonsyndromic Retinitis Pigmentosa in the Ashkenazi Jewish
            Population: Genetic and Clinical Aspects
  JOURNAL   Ophthalmology 125 (5), 725-734 (2018)
   PUBMED   29276052
  REMARK    GeneRIF: The clinical data show that in general, patients with
            biallelic MAK mutations had a later age of onset and a milder
            retinal phenotype compared with patients with biallelic DHDDS
            mutations.
            Erratum:[Ophthalmology. 2020 Jan;127(1):139. doi:
            10.1016/j.ophtha.2019.10.024. PMID: 31864473]
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Lai,Y.H., Capasso,J.E., Kaiser,R. and Levin,A.V.
  TITLE     Intraretinal cystoid spaces in a patient with retinitis pigmentosa
            due to mutation in the MAK gene
  JOURNAL   Ophthalmic Genet 37 (4), 424-426 (2016)
   PUBMED   26894652
  REMARK    GeneRIF: We report the first case of leaking intraretinal cystoid
            spaces due to mutation in MAK. Mak regulates microtubule stability
            via phosphorylating RP1. Abnormal Mak may impact retinal
            photoreceptor ciliary length and subcompartmentalization.
REFERENCE   5  (residues 1 to 583)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 583)
  AUTHORS   Xia,L., Robinson,D., Ma,A.H., Chen,H.C., Wu,F., Qiu,Y. and
            Kung,H.J.
  TITLE     Identification of human male germ cell-associated kinase, a kinase
            transcriptionally activated by androgen in prostate cancer cells
  JOURNAL   J Biol Chem 277 (38), 35422-35433 (2002)
   PUBMED   12084720
  REMARK    GeneRIF: identification and transcriptional activation by androgen
            in prostate cancer cells
REFERENCE   7  (residues 1 to 583)
  AUTHORS   Jinno,A., Tanaka,K., Matsushime,H., Haneji,T. and Shibuya,M.
  TITLE     Testis-specific mak protein kinase is expressed specifically in the
            meiotic phase in spermatogenesis and is associated with a
            210-kilodalton cellular phosphoprotein
  JOURNAL   Mol Cell Biol 13 (7), 4146-4156 (1993)
   PUBMED   8321219
REFERENCE   8  (residues 1 to 583)
  AUTHORS   Bladt,F. and Birchmeier,C.
  TITLE     Characterization and expression analysis of the murine rck gene: a
            protein kinase with a potential function in sensory cells
  JOURNAL   Differentiation 53 (2), 115-122 (1993)
   PUBMED   8359591
REFERENCE   9  (residues 1 to 583)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   10 (residues 1 to 583)
  AUTHORS   Matsushime,H., Jinno,A., Takagi,N. and Shibuya,M.
  TITLE     A novel mammalian protein kinase gene (mak) is highly expressed in
            testicular germ cells at and after meiosis
  JOURNAL   Mol Cell Biol 10 (5), 2261-2268 (1990)
   PUBMED   2183027
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP246863.1, AB593146.1 and
            BM704130.1.
            
            Summary: The product of this gene is a serine/threonine protein
            kinase related to kinases involved in cell cycle regulation.
            Studies of the mouse and rat homologs have localized the kinase to
            the chromosomes during meiosis in spermatogenesis, specifically to
            the synaptonemal complex that exists while homologous chromosomes
            are paired. Mutations in this gene have been associated with
            ciliary defects resulting in retinitis pigmentosa 62. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) represents a longer 5' UTR and
            lacks an alternate in-frame exon compared to variant 1. The
            resulting isoform (2) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB593146.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.2"
     Protein         1..583
                     /product="serine/threonine-protein kinase MAK isoform 2"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine protein kinase MAK; testicular
                     secretory protein Li 28"
                     /calculated_mol_wt=66214
     Region          4..284
                     /region_name="STKc_MAK_like"
                     /note="Catalytic domain of Male germ cell-Associated
                     Kinase-like Serine/Threonine Kinases; cd07830"
                     /db_xref="CDD:270824"
     Site            order(10..13,18,31,33,49,63,79..82,85,87..88,125,127,
                     129..130,132,143,146,157,159..162,164,202)
                     /site_type="active"
                     /db_xref="CDD:270824"
     Site            order(10..14,18,31,33,63,79..82,85,125,127,129..130,132,
                     143)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270824"
     Site            order(49,87,125,127,146,157,159..162,164,202)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270824"
     Site            order(142..152,155..164)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270824"
     CDS             1..583
                     /gene="MAK"
                     /gene_synonym="RP62"
                     /coded_by="NM_001242385.2:288..2039"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS75398.1"
                     /db_xref="GeneID:4117"
                     /db_xref="HGNC:HGNC:6816"
                     /db_xref="MIM:154235"
ORIGIN      
        1 mnryttmrql gdgtygsvlm gksnesgelv aikrmkrkfy swdecmnlre vkslkklnha
       61 nviklkevir endhlyfife ymkenlyqlm kdrnklfpes virnimyqil qglafihkhg
      121 ffhrdmkpen llcmgpelvk iadfglarel rsqppytdyv strwyrapev llrssvyssp
      181 idvwavgsim aelymlrplf pgtsevdeif kicqvlgtpk ksdwpegyql assmnfrfpq
      241 cvpinlktli pnasneaiql mtemlnwdpk krptasqalk hpyfqvgqvl gpssnhlesk
      301 qslnkqlqpl eskpslveve pkplpdiidq vvgqpqpkts qqplqpiqpp qnlsvqqppk
      361 qqsqekppqt lfpsivknmp tkpngtlshk sgrrrwgqti fksgdsweel edydfgashs
      421 kkpsmgvfke krkkdspfrl pepvpsgsnh stgenkslpa vtslksdsel staptskqyy
      481 lkqsrylpgv npkkvslias gkeinphtws nqlfpkslgp vgaelafkrs naeytwntkt
      541 grgqfsgrty nptaknlniv nraqpipsvh grtdwvakyg ghr
//
LOCUS       NP_001350596             673 aa            linear   PRI 21-NOV-2025
DEFINITION  kin of IRRE-like protein 2 isoform e precursor [Homo sapiens].
ACCESSION   NP_001350596 XP_016882837
VERSION     NP_001350596.1
DBSOURCE    REFSEQ: accession NM_001363667.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 673)
  AUTHORS   Voskarides,K., Stefanou,C., Pieri,M., Demosthenous,P., Felekkis,K.,
            Arsali,M., Athanasiou,Y., Xydakis,D., Stylianou,K., Daphnis,E.,
            Goulielmos,G., Loizou,P., Savige,J., Hohne,M., Volker,L.A.,
            Benzing,T., Maxwell,P.H., Gale,D.P., Gorski,M., Boger,C.,
            Kollerits,B., Kronenberg,F., Paulweber,B., Zavros,M., Pierides,A.
            and Deltas,C.
  TITLE     A functional variant in NEPH3 gene confers high risk of renal
            failure in primary hematuric glomerulopathies. Evidence for
            predisposition to microalbuminuria in the general population
  JOURNAL   PLoS One 12 (3), e0174274 (2017)
   PUBMED   28334007
  REMARK    GeneRIF: SNP V353M confers high risk of renal failure in primary
            hematuric glomerulopathies and predisposition to microalbuminuria
            in the general population
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 673)
  AUTHORS   Yesildag,B., Bock,T., Herrmanns,K., Wollscheid,B. and Stoffel,M.
  TITLE     Kin of IRRE-like Protein 2 Is a Phosphorylated Glycoprotein That
            Regulates Basal Insulin Secretion
  JOURNAL   J Biol Chem 290 (43), 25891-25906 (2015)
   PUBMED   26324709
REFERENCE   5  (residues 1 to 673)
  AUTHORS   Ristola,M. and Lehtonen,S.
  TITLE     Functions of the podocyte proteins nephrin and Neph3 and the
            transcriptional regulation of their genes
  JOURNAL   Clin Sci (Lond) 126 (5), 315-328 (2014)
   PUBMED   24219158
  REMARK    GeneRIF: summarize the current knowledge of the functions of
            nephrin and Neph-family proteins and transcription factors and
            agents that control nephrin and Neph3 gene expression.
            Review article
REFERENCE   6  (residues 1 to 673)
  AUTHORS   Ristola,M., Arpiainen,S., Saleem,M.A., Mathieson,P.W., Welsh,G.I.,
            Lehtonen,S. and Holthofer,H.
  TITLE     Regulation of Neph3 gene in podocytes--key roles of transcription
            factors NF-kappaB and Sp1
  JOURNAL   BMC Mol Biol 10, 83 (2009)
   PUBMED   19703278
  REMARK    GeneRIF: NF-kappaB and Sp1 response elements are essential for the
            basal transcriptional activity of the Neph3 promoter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 673)
  AUTHORS   Ihalmo,P., Schmid,H., Rastaldi,M.P., Mattinzoli,D., Langham,R.G.,
            Luimula,P., Kilpikari,R., Lassila,M., Gilbert,R.E., Kerjaschki,D.,
            Kretzler,M. and Holthofer,H.
  TITLE     Expression of filtrin in human glomerular diseases
  JOURNAL   Nephrol Dial Transplant 22 (7), 1903-1909 (2007)
   PUBMED   17442742
REFERENCE   8  (residues 1 to 673)
  AUTHORS   Rinta-Valkama,J., Aaltonen,P., Lassila,M., Palmen,T.,
            Tossavainen,P., Knip,M. and Holthofer,H.
  TITLE     Densin and filtrin in the pancreas and in the kidney, targets for
            humoral autoimmunity in patients with type 1 diabetes
  JOURNAL   Diabetes Metab Res Rev 23 (2), 119-126 (2007)
   PUBMED   16741999
  REMARK    GeneRIF: Filtrin can act as autoantigen, and autoantibodies against
            these can be detected in patients with type 1 diabetes.
REFERENCE   9  (residues 1 to 673)
  AUTHORS   Sun,C., Kilburn,D., Lukashin,A., Crowell,T., Gardner,H.,
            Brundiers,R., Diefenbach,B. and Carulli,J.P.
  TITLE     Kirrel2, a novel immunoglobulin superfamily gene expressed
            primarily in beta cells of the pancreatic islets
  JOURNAL   Genomics 82 (2), 130-142 (2003)
   PUBMED   12837264
  REMARK    GeneRIF: KIRREL2 protein is a beta-cell-expressed Ig domain protein
            and may be involved in pancreas development or beta cell function
REFERENCE   10 (residues 1 to 673)
  AUTHORS   Ihalmo,P., Palmen,T., Ahola,H., Valtonen,E. and Holthofer,H.
  TITLE     Filtrin is a novel member of nephrin-like proteins
  JOURNAL   Biochem Biophys Res Commun 300 (2), 364-370 (2003)
   PUBMED   12504092
  REMARK    GeneRIF: Identification of Filtrin as a member of nephrin-like
            proteins.
            GeneRIF: Filtrin is a novel protein with substantial homology to
            nephrin. It is a transmembrane protein of the immunoglobulin
            superfamily (apparent molecular weight 107 kDa) and most
            prominently expressed in the pancreas, lymph nodes as well as
            kidney glomerulus.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL529115.3, AB593116.1,
            AK307865.1 and BM693057.1.
            
            On May 25, 2018 this sequence version replaced XP_016882837.1.
            
            Summary: This gene encodes a type I transmembrane protein and
            member of the immunoglobulin superfamily of cell adhesion
            molecules. The encoded protein localizes to adherens junctions in
            pancreatic beta cells and regulates insulin secretion.
            Autoantibodies against the encoded protein have been detected in
            serum from patients with type 1 diabetes. This gene may also play a
            role in glomerular development and decreased expression of this
            gene has been observed in human glomerular diseases. This gene and
            the related opposite-strand gene nephrin (GeneID: 527362) are
            regulated by a bidirectional promoter. [provided by RefSeq, Jul
            2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK307865.1, SRR14038192.2078961.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151405, SAMEA2153347
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..673
                     /product="kin of IRRE-like protein 2 isoform e precursor"
                     /note="nephrin-like gene 1; nephrin-like protein 3; kin of
                     irregular chiasm-like protein 2; kin of IRRE like 2"
                     /calculated_mol_wt=69085
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2363
     Region          30..119
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          41..45
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          53..57
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          86..90
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          100..105
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          125..223
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          142..146
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          157..161
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          187..191
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          201..206
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          216..219
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          226..295
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          312..378
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          397..501
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          415..419
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:319310"
     Region          429..433
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:319310"
     Region          467..471
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:319310"
     Region          482..487
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:319310"
     Region          495..498
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:319310"
     CDS             1..673
                     /gene="KIRREL2"
                     /gene_synonym="FILTRIN; NEPH3; NLG1"
                     /coded_by="NM_001363667.2:210..2231"
                     /note="isoform e precursor is encoded by transcript
                     variant 5"
                     /db_xref="CCDS:CCDS86753.1"
                     /db_xref="GeneID:84063"
                     /db_xref="HGNC:HGNC:18816"
                     /db_xref="MIM:607762"
ORIGIN      
        1 mlrmrvpall vllfcfrgra gpsphflqqp edlvvllgee arlpcalgay wglvqwtksg
       61 lalggqrdlp gwsrywisgn aangqhdlhi rpveledeas yecqatqagl rsrpaqlhvl
      121 vppeapqvlg gpsvslvagv panltcrsrg darptpellw frdgvlldga tfhqtllkeg
      181 tpgsvestlt ltpfshddga tfvcrarsqa lptgrdtait lslqyppevt lsasphtvqe
      241 gekviflcqa taqppvtgyr wakggspvlg argprlevva dasfltepvs cevsnavgsa
      301 nrstaldvlf gpilqakpep vsvdvgedas fscawrgnpl prvtwtrrgg aqvlgsgatl
      361 rlpsvgpeda gdyvcraeag lsglrggaae arltvnappv vtalhsapaf lrgparlqcl
      421 vfaspapdav vwswdegfle agsqgrflve tfpapesrgg lgpglisvlh isgtqesdfs
      481 rsfncsarnr lgeggaqasl grrasasfse qknlmripgs sdgsssrgpe eeetgsredr
      541 gpivhtdhsd lvleeegtle tkdptngyyk vrgvsvslsl geapggglfl pppsplgppg
      601 tptfydfnph lgmvppcrly raragylttp hpraftsyik ptsfgppdla pgtppfpyaa
      661 fptpshprlq thv
//
LOCUS       NP_001357907             582 aa            linear   PRI 21-NOV-2025
DEFINITION  la-related protein 7 isoform 1 [Homo sapiens].
ACCESSION   NP_001357907 XP_024309853
VERSION     NP_001357907.1
DBSOURCE    REFSEQ: accession NM_001370978.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Kao,T.L., Huang,Y.C., Chen,Y.H., Baumann,P. and Tseng,C.K.
  TITLE     LARP3, LARP7, and MePCE are involved in the early stage of human
            telomerase RNA biogenesis
  JOURNAL   Nat Commun 15 (1), 5955 (2024)
   PUBMED   39009594
  REMARK    GeneRIF: LARP3, LARP7, and MePCE are involved in the early stage of
            human telomerase RNA biogenesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 582)
  AUTHORS   Yan,P., Li,Z., Xiong,J., Geng,Z., Wei,W., Zhang,Y., Wu,G.,
            Zhuang,T., Tian,X., Liu,Z., Liu,J., Sun,K., Chen,F., Zhang,Y.,
            Zeng,C., Huang,Y. and Zhang,B.
  TITLE     LARP7 ameliorates cellular senescence and aging by allosterically
            enhancing SIRT1 deacetylase activity
  JOURNAL   Cell Rep 37 (8), 110038 (2021)
   PUBMED   34818543
  REMARK    GeneRIF: LARP7 ameliorates cellular senescence and aging by
            allosterically enhancing SIRT1 deacetylase activity.
REFERENCE   6  (residues 1 to 582)
  AUTHORS   Xue,Y., Yang,Z., Chen,R. and Zhou,Q.
  TITLE     A capping-independent function of MePCE in stabilizing 7SK snRNA
            and facilitating the assembly of 7SK snRNP
  JOURNAL   Nucleic Acids Res 38 (2), 360-369 (2010)
   PUBMED   19906723
REFERENCE   7  (residues 1 to 582)
  AUTHORS   Markert,A., Grimm,M., Martinez,J., Wiesner,J., Meyerhans,A.,
            Meyuhas,O., Sickmann,A. and Fischer,U.
  TITLE     The La-related protein LARP7 is a component of the 7SK
            ribonucleoprotein and affects transcription of cellular and viral
            polymerase II genes
  JOURNAL   EMBO Rep 9 (6), 569-575 (2008)
   PUBMED   18483487
  REMARK    GeneRIF: Results suggest that LARP7 is a negative transcriptional
            regulator of polymerase II genes, acting by means of the 7SK RNP
            system.
REFERENCE   8  (residues 1 to 582)
  AUTHORS   Krueger,B.J., Jeronimo,C., Roy,B.B., Bouchard,A., Barrandon,C.,
            Byers,S.A., Searcey,C.E., Cooper,J.J., Bensaude,O., Cohen,E.A.,
            Coulombe,B. and Price,D.H.
  TITLE     LARP7 is a stable component of the 7SK snRNP while P-TEFb, HEXIM1
            and hnRNP A1 are reversibly associated
  JOURNAL   Nucleic Acids Res 36 (7), 2219-2229 (2008)
   PUBMED   18281698
  REMARK    GeneRIF: Results indicate LARP7 is a 7SK-binding protein.
REFERENCE   9  (residues 1 to 582)
  AUTHORS   He,N., Jahchan,N.S., Hong,E., Li,Q., Bayfield,M.A., Maraia,R.J.,
            Luo,K. and Zhou,Q.
  TITLE     A La-related protein modulates 7SK snRNP integrity to suppress
            P-TEFb-dependent transcriptional elongation and tumorigenesis
  JOURNAL   Mol Cell 29 (5), 588-599 (2008)
   PUBMED   18249148
  REMARK    GeneRIF: Results identify PIP7S as a La-related protein stably
            associated with and required for 7SK snRNP integrity.
REFERENCE   10 (residues 1 to 582)
  AUTHORS   Biewenga,P., Buist,M.R., Moerland,P.D., Ver Loren van Themaat,E.,
            van Kampen,A.H., ten Kate,F.J. and Baas,F.
  TITLE     Gene expression in early stage cervical cancer
  JOURNAL   Gynecol Oncol 108 (3), 520-526 (2008)
   PUBMED   18191186
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106864.5.
            
            On Jun 19, 2019 this sequence version replaced XP_024309853.1.
            
            Summary: This gene encodes a protein which is found in the 7SK
            snRNP (small nuclear ribonucleoprotein). This snRNP complex
            inhibits a cyclin-dependent kinase, positive transcription
            elongation factor b, which is required for paused RNA polymerase II
            at a promoter to begin transcription elongation. A pseudogene of
            this gene is located on chromosome 3. Alternative splicing results
            in multiple transcript variants. [provided by RefSeq, May 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.726558.1,
                                           SRR14038194.2148685.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..582
                     /product="la-related protein 7 isoform 1"
                     /note="P-TEFb-interaction protein for 7SK stability;
                     La-related protein 7; La ribonucleoprotein domain family
                     member 7"
                     /calculated_mol_wt=66768
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G0J3.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q4G0J3.1)"
     Region          30..111
                     /region_name="LARP_7"
                     /note="La RNA-binding domain of La-related protein 7;
                     cd08032"
                     /db_xref="CDD:153401"
     Site            order(41,44..45,50,53..54,56,77..79)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153401"
     Region          126..205
                     /region_name="RRM1_LARP7"
                     /note="RNA recognition motif 1 (RRM1) found in La-related
                     protein 7 (LARP7) and similar proteins; cd12290"
                     /db_xref="CDD:409732"
     Region          188..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G0J3.1)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q4G0J3.1)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q4G0J3.1)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q4G0J3.1)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q4G0J3.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q4G0J3.1)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q4G0J3.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q4G0J3.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q4G0J3.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q4G0J3.1)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q4G0J3.1)"
     Region          410..442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G0J3.1)"
     Region          454..535
                     /region_name="RRM2_LARP7"
                     /note="RNA recognition motif 2 in La-related protein 7
                     (LARP7) and similar proteins; cd12542"
                     /db_xref="CDD:409958"
     CDS             1..582
                     /gene="LARP7"
                     /gene_synonym="ALAZS; HDCMA18P; hLARP7; PIP7S"
                     /coded_by="NM_001370978.1:161..1909"
                     /note="isoform 1 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS3701.2"
                     /db_xref="GeneID:51574"
                     /db_xref="HGNC:HGNC:24912"
                     /db_xref="MIM:612026"
ORIGIN      
        1 metesgnqek vmeeestekk kevekkkrsr vkqvladiak qvdfwfgdan lhkdrflreq
       61 ieksrdgyvd isllvsfnkm kklttdgkli aralrssavv eldlegtrir rkkplgerpk
      121 dedertvyve llpknvnhsw iervfgkcgn vvyisiphyk stgdpkgfaf vefetkeqaa
      181 kaieflnnpp eeaprkpgif pktvknkpip alrvveekkk kkkkkgrmkk edniqakeen
      241 mdtsntsisk mkrsrptseg sdiestepqk qcskkkkkrd rveasslpev rtgkrkrsss
      301 edaeslaprs kvkkiiqkdi ikeaseaske nrdieistee ekdtgdlkds sllktkrkhk
      361 kkhkerhkmg eeviplrvls ksewmdlkke ylalqkasma slkktisqik sesemetdsg
      421 vpqntgmkne ktanreecrt qekvnatgpq fvsgvivkii steplpgrkq vrdtlaaise
      481 vlyvdllegd techarfktp edaqavinay teinkkhcwk leilsgdheq rywqkilvdr
      541 qaklnqprek krgteklitk aekirlaktq qaskhirfse yd
//
LOCUS       NP_001317263             361 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform d [Homo sapiens].
ACCESSION   NP_001317263 XP_005274430
VERSION     NP_001317263.1
DBSOURCE    REFSEQ: accession NM_001330334.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 361)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 361)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 361)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 361)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 361)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2 and AW263732.1.
            
            On Aug 23, 2016 this sequence version replaced XP_005274430.1.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) lacks three alternate in-frame
            exons in the 3' coding region compared to variant 3. It encodes
            isoform d, which is shorter than isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3853802.1,
                                           SRR14038197.554080.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..361
                     /product="polycomb protein EED isoform d"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=40504
     Region          96..140
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <109..>358
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          148..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          193..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          285..325
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          333..357
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..361
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001330334.2:478..1563"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS81612.1"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdendd avsiesgtnt erpdtptntp
       61 napgrkswgk gkwkskkcky sfkcvnslke dhnqplfgvq fnwhskegdp lvfatvgsnr
      121 vtlyechsqg eirllqsyvd adadenfytc awtydsntsh pllavagsrg iiriinpitm
      181 qcikhyvghg nainelkfhp rdpnlllsvs kdhalrlwni qtdtlvaifg gveghrdevl
      241 sascenaivc wkpgkmeddi dkikpsesnv tilgrfdysq cdiwymrfsm dfwqkmlalg
      301 nqvgklyvwd levedphkak cttlthhkcg aairqtsfsr dssiliavcd dasiwrwdrl
      361 r
//
LOCUS       NP_001338956             681 aa            linear   PRI 21-NOV-2025
DEFINITION  PHD finger protein 21A isoform c [Homo sapiens].
ACCESSION   NP_001338956 XP_011518475
VERSION     NP_001338956.1
DBSOURCE    REFSEQ: accession NM_001352027.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Mustafa,S., Abbas,S., Mahmood,A., Khan,A.Z., Zeb,S., Khan,A. and
            Umair,M.
  TITLE     A novel de novo variant in the PHF21A causes craniofacial
            abnormalities, intellectual disability and skeletal manifestations
  JOURNAL   Clin Genet 104 (1), 142-144 (2023)
   PUBMED   36843358
  REMARK    GeneRIF: A novel de novo variant in the PHF21A causes craniofacial
            abnormalities, intellectual disability and skeletal manifestations.
REFERENCE   3  (residues 1 to 681)
  AUTHORS   Huang,J.Q., Ji,L.C., Jing,Q.A., He,Y.C., Ma,Y.Y. and Tong,X.M.
  TITLE     PHF21A expression as a biomarker of hepatocellular carcinoma
            progression and prognosis
  JOURNAL   Neoplasma 69 (6), 1349-1358 (2022)
   PUBMED   36305691
  REMARK    GeneRIF: PHF21A expression as a biomarker of hepatocellular
            carcinoma progression and prognosis.
REFERENCE   4  (residues 1 to 681)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 681)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 681)
  AUTHORS   Hailesellasse Sene,K., Porter,C.J., Palidwor,G., Perez-Iratxeta,C.,
            Muro,E.M., Campbell,P.A., Rudnicki,M.A. and Andrade-Navarro,M.A.
  TITLE     Gene function in early mouse embryonic stem cell differentiation
  JOURNAL   BMC Genomics 8, 85 (2007)
   PUBMED   17394647
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 681)
  AUTHORS   Shi,Y.J., Matson,C., Lan,F., Iwase,S., Baba,T. and Shi,Y.
  TITLE     Regulation of LSD1 histone demethylase activity by its associated
            factors
  JOURNAL   Mol Cell 19 (6), 857-864 (2005)
   PUBMED   16140033
REFERENCE   8  (residues 1 to 681)
  AUTHORS   Iwase,S., Januma,A., Miyamoto,K., Shono,N., Honda,A., Yanagisawa,J.
            and Baba,T.
  TITLE     Characterization of BHC80 in BRAF-HDAC complex, involved in
            neuron-specific gene repression
  JOURNAL   Biochem Biophys Res Commun 322 (2), 601-608 (2004)
   PUBMED   15325272
  REMARK    GeneRIF: Presumably serves as a scaffold protein in BHC in neuronal
            as well as non-neuronal cells. Possible role in spermatogenesis.
REFERENCE   9  (residues 1 to 681)
  AUTHORS   Hakimi,M.A., Dong,Y., Lane,W.S., Speicher,D.W. and Shiekhattar,R.
  TITLE     A candidate X-linked mental retardation gene is a component of a
            new family of histone deacetylase-containing complexes
  JOURNAL   J Biol Chem 278 (9), 7234-7239 (2003)
   PUBMED   12493763
REFERENCE   10 (residues 1 to 681)
  AUTHORS   Hakimi,M.A., Bochar,D.A., Chenoweth,J., Lane,W.S., Mandel,G. and
            Shiekhattar,R.
  TITLE     A core-BRAF35 complex containing histone deacetylase mediates
            repression of neuronal-specific genes
  JOURNAL   Proc Natl Acad Sci U S A 99 (11), 7420-7425 (2002)
   PUBMED   12032298
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC024475.15 and AC068385.9.
            
            On Jun 3, 2017 this sequence version replaced XP_011518475.1.
            
            Summary: The PHF21A gene encodes BHC80, a component of a BRAF35
            (MIM 605535)/histone deacetylase (HDAC; see MIM 601241) complex
            (BHC) that mediates repression of neuron-specific genes through the
            cis-regulatory element known as repressor element-1 (RE1) or neural
            restrictive silencer (NRS) (Hakimi et al., 2002 [PubMed
            12032298]).[supplied by OMIM, Nov 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1461092.1,
                                           SRR14038191.2276146.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000676320.1/ ENSP00000502222.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..681
                     /product="PHD finger protein 21A isoform c"
                     /note="BRAF35/HDAC2 complex (80 kDa); BHC80a; BRAF35-HDAC
                     complex protein BHC80"
                     /calculated_mol_wt=74851
     Region          82..118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          319..364
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          <375..537
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          441..464
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96BD5.1)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          487..681
                     /region_name="Required for transcriptional repression"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          491..533
                     /region_name="PHD_PHF21A"
                     /note="PHD finger found in PHD finger protein 21A
                     (PHF21A); cd15523"
                     /db_xref="CDD:276998"
     Site            order(491,498..503,523..526,528)
                     /site_type="other"
                     /note="histone H3 binding site [polypeptide binding]"
                     /db_xref="CDD:276998"
     Region          640..681
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     CDS             1..681
                     /gene="PHF21A"
                     /gene_synonym="BHC80; BM-006; IDDBCS; NEDMS"
                     /coded_by="NM_001352027.3:757..2802"
                     /note="isoform c is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS91465.1"
                     /db_xref="GeneID:51317"
                     /db_xref="HGNC:HGNC:24156"
                     /db_xref="MIM:608325"
ORIGIN      
        1 melqtlqeal kveiqvhqkl vaqmkqdpqn adlkkqlhel qakitalsek qkrvveqlrk
       61 nlivkqeqpd kfqiqplpqs enklqtaqqq plqqlqqqqq yhhhhaqqsa aaspnltasq
      121 ktvttasmit tktlplvlka atatmpasvv gqrptiamvt ainsqkavls tdvqntpvnl
      181 qtsskvtgpg aeavqivakn tvtlqvqatp pqpikvpqfi ppprltprpn flpqvrpkpv
      241 aqnnipiapa pppmlaapql iqrpvmltkf tpttlptsqn sihpvrvvng qtatiaktfp
      301 maqltsivia tpgtrlagpq tvqlskpsle kqtvkshtet dekqtesrti tppaapkpkr
      361 eenpqklafm vslglvthdh leeiqskrqe rkrrttanpv ysgavfeper kksavtylns
      421 tmhpgtrkrg rppkynavlg fgaltptspq sshpdspene ktettftfpa pvqpvslpsp
      481 tstdgdihed fcsvcrksgq llmcdtcsrv yhldcldppl ktipkgmwic prcqdqmlkk
      541 eeaipwpgtl aivhsyiayk aakeeekqkl lkwssdlkqe reqleqkvkq lsnsiskcme
      601 mkntilarqk emhsslekvk qlirlihgid lskpvdseat vgaisngpdc tppanaatst
      661 papspssqsc tancnqgeet k
//
LOCUS       NP_001358080            1183 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal cell adhesion molecule isoform B precursor [Homo sapiens].
ACCESSION   NP_001358080
VERSION     NP_001358080.1
DBSOURCE    REFSEQ: accession NM_001371151.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1183)
  AUTHORS   Wang,C., Wang,Z., Fu,L., Du,J., Ji,F. and Qiu,X.
  TITLE     CircNRCAM up-regulates NRCAM to promote papillary thyroid carcinoma
            progression
  JOURNAL   J Endocrinol Invest 47 (5), 1215-1226 (2024)
   PUBMED   38485895
  REMARK    GeneRIF: CircNRCAM up-regulates NRCAM to promote papillary thyroid
            carcinoma progression.
REFERENCE   2  (residues 1 to 1183)
  AUTHORS   Zhou,L., He,L., Liu,C.H., Qiu,H., Zheng,L., Sample,K.M., Wu,Q.,
            Li,J., Xie,K., Ampuero,J., Li,Z., Lv,D., Liu,M., Romero-Gomez,M.,
            Hu,Y. and Tang,H.
  TITLE     Liver cancer stem cell dissemination and metastasis: uncovering the
            role of NRCAM in hepatocellular carcinoma
  JOURNAL   J Exp Clin Cancer Res 42 (1), 311 (2023)
   PUBMED   37993901
  REMARK    GeneRIF: Liver cancer stem cell dissemination and metastasis:
            uncovering the role of NRCAM in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1183)
  AUTHORS   Sannes,A.C., Christensen,J.O., Nielsen,M.B. and Gjerstad,J.
  TITLE     Stress-induced headache in the general working population is
            moderated by the NRCAM rs2300043 genotype
  JOURNAL   Scand J Pain 23 (2), 326-332 (2022)
   PUBMED   36181733
  REMARK    GeneRIF: Stress-induced headache in the general working population
            is moderated by the NRCAM rs2300043 genotype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1183)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 1183)
  AUTHORS   Bai,C. and Chen,D.G.
  TITLE     NRCAM acts as a prognostic biomarker and promotes the tumor
            progression in gastric cancer via EMT pathway
  JOURNAL   Tissue Cell 77, 101859 (2022)
   PUBMED   35763884
  REMARK    GeneRIF: NRCAM acts as a prognostic biomarker and promotes the
            tumor progression in gastric cancer via EMT pathway.
REFERENCE   6  (residues 1 to 1183)
  AUTHORS   Wang,B., Williams,H., Du,J.S., Terrett,J. and Kenwrick,S.
  TITLE     Alternative splicing of human NrCAM in neural and nonneural tissues
  JOURNAL   Mol Cell Neurosci 10 (5-6), 287-295 (1998)
   PUBMED   9604207
REFERENCE   7  (residues 1 to 1183)
  AUTHORS   Grumet,M.
  TITLE     Nr-CAM: a cell adhesion molecule with ligand and receptor functions
  JOURNAL   Cell Tissue Res 290 (2), 423-428 (1997)
   PUBMED   9321706
  REMARK    Review article
REFERENCE   8  (residues 1 to 1183)
  AUTHORS   Sakurai,T., Lustig,M., Nativ,M., Hemperly,J.J., Schlessinger,J.,
            Peles,E. and Grumet,M.
  TITLE     Induction of neurite outgrowth through contactin and Nr-CAM by
            extracellular regions of glial receptor tyrosine phosphatase beta
  JOURNAL   J Cell Biol 136 (4), 907-918 (1997)
   PUBMED   9049255
REFERENCE   9  (residues 1 to 1183)
  AUTHORS   Volkmer,H., Leuschner,R., Zacharias,U. and Rathjen,F.G.
  TITLE     Neurofascin induces neurites by heterophilic interactions with
            axonal NrCAM while NrCAM requires F11 on the axonal surface to
            extend neurites
  JOURNAL   J Cell Biol 135 (4), 1059-1069 (1996)
   PUBMED   8922386
REFERENCE   10 (residues 1 to 1183)
  AUTHORS   Lane,R.P., Chen,X.N., Yamakawa,K., Vielmetter,J., Korenberg,J.R.
            and Dreyer,W.J.
  TITLE     Characterization of a highly conserved human homolog to the chicken
            neural cell surface protein Bravo/Nr-CAM that maps to chromosome
            band 7q31
  JOURNAL   Genomics 35 (3), 456-465 (1996)
   PUBMED   8812479
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005058.1, AC007567.2 and
            AC005683.2.
            
            Summary: Cell adhesion molecules (CAMs) are members of the
            immunoglobulin superfamily. This gene encodes a neuronal cell
            adhesion molecule with multiple immunoglobulin-like C2-type domains
            and fibronectin type-III domains. This ankyrin-binding protein is
            involved in neuron-neuron adhesion and promotes directional
            signaling during axonal cone growth. This gene is also expressed in
            non-neural tissues and may play a general role in cell-cell
            communication via signaling from its intracellular domain to the
            actin cytoskeleton during directional cell migration. Allelic
            variants of this gene have been associated with autism and
            addiction vulnerability. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (9), as well as variants 2, 8, 10,
            and 11, encodes isoform B.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.226726.1,
                                           SRR14038194.3993869.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1183
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1183
                     /product="neuronal cell adhesion molecule isoform B
                     precursor"
                     /note="NgCAM-related cell adhesion molecule; neuronal
                     surface protein Bravo"
                     /calculated_mol_wt=127750
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3315
     Region          40..134
                     /region_name="IgI_NrCAM"
                     /note="Immunoglobulin (Ig)-like domain of NrCAM (Ng
                     (neuronglia) CAM-related cell adhesion molecule); member
                     of the I-set of Ig superfamily (IgSF) domains; cd05874"
                     /db_xref="CDD:409458"
     Region          40..44
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409458"
     Region          49..53
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409458"
     Region          58..65
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409458"
     Region          71..76
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409458"
     Site            77
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          79..81
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409458"
     Region          88..91
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409458"
     Region          96..100
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409458"
     Region          113..121
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409458"
     Region          124..134
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409458"
     Region          143..232
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          157..161
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          171..175
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          194..198
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          209..214
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            217
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          225..228
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            239
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            245
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            270
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          271..352
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          282..286
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          295..299
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            308
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          317..321
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          331..336
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          344..347
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          356..444
                     /region_name="Ig4_NrCAM"
                     /note="Fourth immunoglobulin (Ig)-like domain of NrCAM
                     (NgCAM-related cell adhesion molecule); cd05868"
                     /db_xref="CDD:409454"
     Region          372..376
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409454"
     Region          385..389
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409454"
     Region          409..413
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409454"
     Region          423..428
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409454"
     Site            427
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          436..439
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409454"
     Region          453..536
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          466..470
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          479..483
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            501
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          502..506
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          516..521
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          529..532
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          542..627
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          557..561
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          572..576
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          596..1036
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          607..612
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            613
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          620..623
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          631..721
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(631,697,712)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            700
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            order(713..714,716..717)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            786
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            842
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            order(936,1004,1019)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          937..1021
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            977
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            993
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1003
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            order(1020..1021,1023..1024)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1070..1159
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     CDS             1..1183
                     /gene="NRCAM"
                     /gene_synonym="NEDNMS"
                     /coded_by="NM_001371151.1:368..3919"
                     /note="isoform B precursor is encoded by transcript
                     variant 9"
                     /db_xref="CCDS:CCDS5751.1"
                     /db_xref="GeneID:4897"
                     /db_xref="HGNC:HGNC:7994"
                     /db_xref="MIM:601581"
ORIGIN      
        1 mqlkimpkkk rlsagrvpli lflcqmisal evpldlvqpp titqqspkdy iidprenivi
       61 qceakgkppp sfswtrngth fdidkdplvt mkpgtgtlii nimsegkaet yegvyqctar
      121 nergaavsnn ivvrpsrspl wtkeklepit lqsgqslvlp crppiglppp iifwmdnsfq
      181 rlpqservsq glngdlyfsn vlpedtredy icyarfnhtq tiqqkqpisv kvisvdelnd
      241 tiaanlsdte fygakssrer pptfltpegn asnkeelrgn vlsleciaeg lptpiiywak
      301 edgmlpknrt vyknfektlq iihvseadsg nyqciaknal gaihhtisvr vkaapywita
      361 pqnlvlspge dgtlicrang npkpriswlt ngvpieiapd dpsrkidgdt iifsnvqers
      421 savyqcnasn eygyllanaf vnvlaeppri ltpantlyqv ianrpalldc affgsplpti
      481 ewfkgakgsa lhediyvlhe ngtleipvaq kdstgtytcv arnklgmakn evhleikdpt
      541 wivkqpeyav vqrgsmvsfe ckvkhdhtls ltvlwlkdnr elpsderftv dkdhlvvadv
      601 sdddsgtytc vanttldsvs asavlsvvdv pnppfdlelt dqldksvqls wtpgddnnsp
      661 itkfiieyed amhkpglwhh qtevsgtqtt aqlklspyvn ysfrvmavns igkslpseas
      721 eqyltkasep dknptavegl gsepdnlvit wkplngfesn gpglqykvsw rqkdgddewt
      781 svvvanvsky ivsgtptfvp ylikvqalnd mgfapepavv mghsgedlpm vapgnvrvnv
      841 vnstlaevhw dpvplksirg hlqgyriyyw ktqssskrnr rhiekkiltf qgskthgmlp
      901 glepfshytl nvrvvngkge gpaspdrvfn tpegvpsaps slkivnptld sltlewdpps
      961 hpngilteyt lkyqpinsth elgplvdlki panktrwtlk nlnfstrykf yfyaqtsags
     1021 gsqiteeavt tvdeamasrq vdiatqgwfi glmcavalli lillivcfir rnkggkypvk
     1081 ekedahadpe iqpmkeddgt fgeysdaedh kplkkgsrtp sdrtvkkeds ddslvdygeg
     1141 vngqfnedgs figqysgkke kepaegness eapspvnamn sfv
//
LOCUS       NP_001308637            1057 aa            linear   PRI 21-NOV-2025
DEFINITION  diacylglycerol kinase iota isoform 2 [Homo sapiens].
ACCESSION   NP_001308637 XP_006716235
VERSION     NP_001308637.1
DBSOURCE    REFSEQ: accession NM_001321708.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1057)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1057)
  AUTHORS   Bai,M., Ke,S., Yu,H., Xu,Y., Yu,Y., Lu,S., Wang,C., Huang,J.,
            Ma,Y., Dai,W. and Wu,Y.
  TITLE     Key molecules associated with thyroid carcinoma prognosis: A study
            based on transcriptome sequencing and GEO datasets
  JOURNAL   Front Immunol 13, 964891 (2022)
   PUBMED   36059514
  REMARK    GeneRIF: Key molecules associated with thyroid carcinoma prognosis:
            A study based on transcriptome sequencing and GEO datasets.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1057)
  AUTHORS   Etcheverry,A., Aubry,M., Idbaih,A., Vauleon,E., Marie,Y., Menei,P.,
            Boniface,R., Figarella-Branger,D., Karayan-Tapon,L., Quillien,V.,
            Sanson,M., de Tayrac,M., Delattre,J.Y. and Mosser,J.
  TITLE     DGKI methylation status modulates the prognostic value of MGMT in
            glioblastoma patients treated with combined radio-chemotherapy with
            temozolomide
  JOURNAL   PLoS One 9 (9), e104455 (2014)
   PUBMED   25233099
  REMARK    GeneRIF: the DGKI methylation status identified 22% of poorly
            responding patients in the low-risk group
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1057)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   5  (residues 1 to 1057)
  AUTHORS   Zhang,C. and Pierce,B.L.
  TITLE     Genetic susceptibility to accelerated cognitive decline in the US
            Health and Retirement Study
  JOURNAL   Neurobiol Aging 35 (6), 1512 (2014)
   PUBMED   24468470
REFERENCE   6  (residues 1 to 1057)
  AUTHORS   Yang,J., Seo,J., Nair,R., Han,S., Jang,S., Kim,K., Han,K.,
            Paik,S.K., Choi,J., Lee,S., Bae,Y.C., Topham,M.K., Prescott,S.M.,
            Rhee,J.S., Choi,S.Y. and Kim,E.
  TITLE     DGKiota regulates presynaptic release during mGluR-dependent LTD
  JOURNAL   EMBO J 30 (1), 165-180 (2011)
   PUBMED   21119615
REFERENCE   7  (residues 1 to 1057)
  AUTHORS   Moskvina,V., Craddock,N., Holmans,P., Nikolov,I., Pahwa,J.S.,
            Green,E., Owen,M.J. and O'Donovan,M.C.
  CONSRTM   Wellcome Trust Case Control Consortium
  TITLE     Gene-wide analyses of genome-wide association data sets: evidence
            for multiple common risk alleles for schizophrenia and bipolar
            disorder and for overlap in genetic risk
  JOURNAL   Mol Psychiatry 14 (3), 252-260 (2009)
   PUBMED   19065143
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 1057)
  AUTHORS   Bex,C., Knauth,K., Dambacher,S. and Buchberger,A.
  TITLE     A yeast two-hybrid system reconstituting substrate recognition of
            the von Hippel-Lindau tumor suppressor protein
  JOURNAL   Nucleic Acids Res 35 (21), e142 (2007)
   PUBMED   17986458
REFERENCE   9  (residues 1 to 1057)
  AUTHORS   Bowne,S.J., Sullivan,L.S., Ding,L., Traer,E., Prescott,S.M.,
            Birch,D.G., Kennan,A., Humphries,P. and Daiger,S.P.
  TITLE     Evaluation of human diacylglycerol kinase(iota), DGKI, a homolog of
            Drosophila rdgA, in inherited retinopathy mapping to 7q
  JOURNAL   Mol Vis 6, 6-9 (2000)
   PUBMED   10706894
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1057)
  AUTHORS   Ding,L., Traer,E., McIntyre,T.M., Zimmerman,G.A. and Prescott,S.M.
  TITLE     The cloning and characterization of a novel human diacylglycerol
            kinase, DGKiota
  JOURNAL   J Biol Chem 273 (49), 32746-32752 (1998)
   PUBMED   9830018
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022173.7, AC009179.17,
            AC090498.4 and AC078842.2.
            
            On Mar 30, 2016 this sequence version replaced XP_006716235.2.
            
            Summary: This gene is a member of the type IV diacylglycerol kinase
            subfamily.  Diacylglycerol kinases regulate the intracellular
            concentration of diacylglycerol through its phosphorylation,
            producing phosphatidic acid.  The specific role of the enzyme
            encoded by this gene is undetermined, however, it may play a
            crucial role in the production of phosphatidic acid in the retina
            or in recessive forms of retinal degeneration. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.116607.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000614521.2/ ENSP00000479053.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1057
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..1057
                     /product="diacylglycerol kinase iota isoform 2"
                     /EC_number="2.7.1.107"
                     /note="DAG kinase iota; diglyceride kinase iota"
                     /calculated_mol_wt=116103
     Region          15..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75912.2)"
     Region          168..240
                     /region_name="C1_DGKiota_rpt1"
                     /note="first protein kinase C conserved region 1 (C1
                     domain) found in diacylglycerol kinase iota (DAG kinase
                     iota) and similar proteins; cd20850"
                     /db_xref="CDD:410400"
     Region          249..323
                     /region_name="C1_DGKiota_rpt2"
                     /note="second protein kinase C conserved region 1 (C1
                     domain) found in diacylglycerol kinase iota (DAG kinase
                     iota) and similar proteins; cd20896"
                     /db_xref="CDD:410446"
     Region          334..358
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75912.2)"
     Region          378..499
                     /region_name="DAGKc"
                     /note="Diacylglycerol kinase catalytic domain (presumed);
                     smart00046"
                     /db_xref="CDD:214487"
     Region          526..683
                     /region_name="DAGKa"
                     /note="Diacylglycerol kinase accessory domain (presumed);
                     smart00045"
                     /db_xref="CDD:214486"
     Region          917..948
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <921..1056
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(950,952,956..957,960..962,964..965,969,972,983,985,
                     988,992..993,996..998,1000..1001,1005,1008,1017,1019,1021,
                     1025..1026,1029..1031,1033..1034,1038)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          950..983
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          950..979
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75912.2)"
     Region          985..1017
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          986..1015
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75912.2)"
     Region          1014..1033
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75912.2)"
     Region          1055..1057
                     /region_name="PDZ-binding.
                     /evidence=ECO:0000250|UniProtKB:F1MAB7"
                     /note="propagated from UniProtKB/Swiss-Prot (O75912.2)"
     CDS             1..1057
                     /gene="DGKI"
                     /gene_synonym="DGK-IOTA"
                     /coded_by="NM_001321708.2:113..3286"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS94212.1"
                     /db_xref="GeneID:9162"
                     /db_xref="HGNC:HGNC:2855"
                     /db_xref="MIM:604072"
ORIGIN      
        1 mdaagrgchl lplpaargpa rapaaaaaaa asppgpcsga acapsaaaga gamnpsssag
       61 eekgatggss ssgsgagscc lgaeggadpr gagsaaaaga aaldepaaag qkekdealee
      121 klrnltfrkq vsyrkaisra glqhlapahp lslpvangpa kepratldws enavngehlw
      181 letnvsgdlc ylgeencqvr faksalrrkc avckivvhta cieqlekinf rckptfregg
      241 srsprenfvr hhwvhrrrqe gkckqcgkgf qqkfsfhske ivaiscswck qafhnkvtcf
      301 mlhhieepcs lgahaavivp ptwiikvkkp qnslkasnrk kkrtsfkrka skrgmeqenk
      361 grpfvikpis splmkpllvf vnpksggnqg tkvlqmfmwy lnprqvfdls qegpkdalel
      421 yrkvpnlril acggdgtvgw ilsildelql spqppvgvlp lgtgndlart lnwgggytde
      481 pvskilcqve dgtvvqldrw nlhvernpdl ppeeledgvc klplnvfnny fslgfdahvt
      541 lefhesrean pekfnsrfrn kmfyagaafs dflqrssrdl skhvkvvcdg tdltpkiqel
      601 kfqcivflni prycagtmpw gnpgdhhdfe pqrhddgyie vigftmasla alqvgghger
      661 lhqcrevmll tyksipmqvd gepcrlapam irislrnqan mvqkskrrts mpllndpqsv
      721 pdrlrirvnk islqdyegfh ydkeklreas iplgilvvrg dcdletcrmy idrlqedlqs
      781 vssgsqrvhy qdhetsfpra lsaqrlsprw cfldatsadr fyridrsqeh lhfvmeisqd
      841 eifildpdmv vsqpagtppg mpdlvveqas gisdwwnpal rkrmlsdsgl gmiapyyeds
      901 dlkdlshsrv lqspvssedh ailqaviagd lmkliesykn ggslliqgpd hcsllhyaak
      961 tgngeivkyi ldhgpselld madsetgeta lhkaacqrnr avcqllvdag aslrktdskg
     1021 ktpqeraqqa gdpdlaayle srqnykvigh edletav
//
LOCUS       NP_001381594             288 aa            linear   PRI 21-NOV-2025
DEFINITION  low-density lipoprotein receptor class A domain-containing protein
            4 isoform alpha 2 [Homo sapiens].
ACCESSION   NP_001381594
VERSION     NP_001381594.1
DBSOURCE    REFSEQ: accession NM_001394665.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Xie,W., Xiao,H., Luo,J., Zhao,L., Jin,F., Ma,J., Li,J., Xiong,K.,
            Chen,C. and Wang,G.
  TITLE     Identification of low-density lipoprotein receptor class A domain
            containing 4 (LDLRAD4) as a prognostic indicator in primary
            gastrointestinal stromal tumors
  JOURNAL   Curr Probl Cancer 44 (6), 100593 (2020)
   PUBMED   32507364
  REMARK    GeneRIF: Identification of low-density lipoprotein receptor class A
            domain containing 4 (LDLRAD4) as a prognostic indicator in primary
            gastrointestinal stromal tumors.
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Meerabux,J.M., Ohba,H., Iwayama,Y., Maekawa,M.,
            Detera-Wadleigh,S.D., DeLisi,L.E. and Yoshikawa,T.
  TITLE     Analysis of a t(18;21)(p11.1;p11.1) translocation in a family with
            schizophrenia
  JOURNAL   J Hum Genet 54 (7), 386-391 (2009)
   PUBMED   19461657
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Kikuchi,M., Yamada,K., Toyota,T. and Yoshikawa,T.
  TITLE     C18orf1 located on chromosome 18p11.2 may confer susceptibility to
            schizophrenia
  JOURNAL   J Med Dent Sci 50 (3), 225-229 (2003)
   PUBMED   15074360
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Yoshikawa,T., Sanders,A.R., Esterling,L.E. and Detera-Wadleigh,S.D.
  TITLE     Multiple transcriptional variants and RNA editing in C18orf1, a
            novel gene with LDLRA and transmembrane domains on 18p11.2
  JOURNAL   Genomics 47 (2), 246-257 (1998)
   PUBMED   9479497
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Esterling,L.E., Cox Matise,T., Sanders,A.R., Yoshikawa,T.,
            Overhauser,J., Gershon,E.S., Moskowitz,M.T. and
            Detera-Wadleigh,S.D.
  TITLE     An integrated physical map of 18p11.2: a susceptibility region for
            bipolar disorder
  JOURNAL   Mol Psychiatry 2 (6), 501-504 (1997)
   PUBMED   9399696
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Yoshikawa,T., Sanders,A.R., Esterling,L.E., Overhauser,J.,
            Garnes,J.A., Lennon,G., Grewal,R. and Detera-Wadleigh,S.D.
  TITLE     Isolation of chromosome 18-specific brain transcripts as positional
            candidates for bipolar disorder
  JOURNAL   Am J Med Genet 74 (2), 140-149 (1997)
   PUBMED   9129712
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP002505.3, AP002439.3 and AP001010.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1104591.1,
                                           SRR14038196.1060147.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.21"
     Protein         1..288
                     /product="low-density lipoprotein receptor class A
                     domain-containing protein 4 isoform alpha 2"
                     /note="clone 22; low-density lipoprotein receptor class A
                     domain-containing protein 4"
                     /calculated_mol_wt=31941
     Region          16..47
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(17,25,37..38)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(30,33,37,43..44)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            40..44
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     CDS             1..288
                     /gene="LDLRAD4"
                     /gene_synonym="C18orf1"
                     /coded_by="NM_001394665.1:524..1390"
                     /note="isoform alpha 2 is encoded by transcript variant
                     14"
                     /db_xref="CCDS:CCDS32794.1"
                     /db_xref="GeneID:753"
                     /db_xref="HGNC:HGNC:1224"
                     /db_xref="MIM:606571"
ORIGIN      
        1 mpeagfqatn afteckftct sgkclylgsl vcnqqndcgd nsdeencllv tehpppgifn
       61 selefaqiii ivvvvtvmvv vivcllnhyk vstrsfinrp nqsrrredgl pqimhaprsr
      121 drftapsfiq rdrfsrfqpt ypyvqheidl pptislsdge epppyqgpct lqlrdpeqqm
      181 elnresvrap pnrtifdsdl idiamysggp cppssnsgis astcssngrm egppptysev
      241 mghhpgasfl hhqrsnahrg srlqfqqnna estivpikgk drkpgnlv
//
LOCUS       NP_001258570             389 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial carrier homolog 1 isoform PSAP-LL [Homo sapiens].
ACCESSION   NP_001258570
VERSION     NP_001258570.1
DBSOURCE    REFSEQ: accession NM_001271641.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Xie,L., Shu,Y., Ye,M. and Li,Y.
  TITLE     Identification of MTCH1 as a novel prognostic indicator and
            therapeutic target in hepatocellular carcinoma
  JOURNAL   Pathol Res Pract 259, 155358 (2024)
   PUBMED   38820930
  REMARK    GeneRIF: Identification of MTCH1 as a novel prognostic indicator
            and therapeutic target in hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Wang,X., Ji,Y., Qi,J., Zhou,S., Wan,S., Fan,C., Gu,Z., An,P.,
            Luo,Y. and Luo,J.
  TITLE     Mitochondrial carrier 1 (MTCH1) governs ferroptosis by triggering
            the FoxO1-GPX4 axis-mediated retrograde signaling in cervical
            cancer cells
  JOURNAL   Cell Death Dis 14 (8), 508 (2023)
   PUBMED   37550282
  REMARK    GeneRIF: Mitochondrial carrier 1 (MTCH1) governs ferroptosis by
            triggering the FoxO1-GPX4 axis-mediated retrograde signaling in
            cervical cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Guna,A., Stevens,T.A., Inglis,A.J., Replogle,J.M., Esantsi,T.K.,
            Muthukumar,G., Shaffer,K.C.L., Wang,M.L., Pogson,A.N., Jones,J.J.,
            Lomenick,B., Chou,T.F., Weissman,J.S. and Voorhees,R.M.
  TITLE     MTCH2 is a mitochondrial outer membrane protein insertase
  JOURNAL   Science 378 (6617), 317-322 (2022)
   PUBMED   36264797
REFERENCE   5  (residues 1 to 389)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 389)
  AUTHORS   Lamarca,V., Marzo,I., Sanz-Clemente,A. and Carrodeguas,J.A.
  TITLE     Exposure of any of two proapoptotic domains of presenilin
            1-associated protein/mitochondrial carrier homolog 1 on the surface
            of mitochondria is sufficient for induction of apoptosis in a
            Bax/Bak-independent manner
  JOURNAL   Eur J Cell Biol 87 (5), 325-334 (2008)
   PUBMED   18375015
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Mao,G., Tan,J., Gao,W., Shi,Y., Cui,M.Z. and Xu,X.
  TITLE     Both the N-terminal fragment and the protein-protein interaction
            domain (PDZ domain) are required for the pro-apoptotic activity of
            presenilin-associated protein PSAP
  JOURNAL   Biochim Biophys Acta 1780 (4), 696-708 (2008)
   PUBMED   18291114
  REMARK    GeneRIF: Data show that all PSAP splicing isoforms are localized in
            the mitochondria and are pro-apoptotic.
REFERENCE   8  (residues 1 to 389)
  AUTHORS   Lamarca,V., Sanz-Clemente,A., Perez-Pe,R., Martinez-Lorenzo,M.J.,
            Halaihel,N., Muniesa,P. and Carrodeguas,J.A.
  TITLE     Two isoforms of PSAP/MTCH1 share two proapoptotic domains and
            multiple internal signals for import into the mitochondrial outer
            membrane
  JOURNAL   Am J Physiol Cell Physiol 293 (4), C1347-C1361 (2007)
   PUBMED   17670888
  REMARK    GeneRIF: PSAP has two proapoptotic isoforms generated by
            alternative splicing, and both proteins are imported into the
            mitochondrial outer membrane using multiple internal targeting
            signals, and both contain two proapoptotic domains.
REFERENCE   9  (residues 1 to 389)
  AUTHORS   Xu,X., Shi,Y.C., Gao,W., Mao,G., Zhao,G., Agrawal,S., Chisolm,G.M.,
            Sui,D. and Cui,M.Z.
  TITLE     The novel presenilin-1-associated protein is a proapoptotic
            mitochondrial protein
  JOURNAL   J Biol Chem 277 (50), 48913-48922 (2002)
   PUBMED   12377771
  REMARK    GeneRIF: mitochondrial localization and proapoptotic activity of
            PSAP suggest that it is an important regulator of apoptosis
REFERENCE   10 (residues 1 to 389)
  AUTHORS   Xu,X., Shi,Yc., Wu,X., Gambetti,P., Sui,D. and Cui,M.Z.
  TITLE     Identification of a novel PSD-95/Dlg/ZO-1 (PDZ)-like protein
            interacting with the C terminus of presenilin-1
  JOURNAL   J Biol Chem 274 (46), 32543-32546 (1999)
   PUBMED   10551805
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL122034.29.
            
            Summary: This gene encodes a member of the mitochondrial carrier
            family. The encoded protein is localized to the mitochondrion inner
            membrane and induces apoptosis independent of the proapoptotic
            proteins Bax and Bak. Pseudogenes on chromosomes 6 and 11 have been
            identified for this gene. Alternatively spliced transcript variants
            encoding multiple isoforms have been observed. [provided by RefSeq,
            Oct 2012].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the coding region, compared to variant 1. The encoded isoform
            (PSAP-LL, PMID:18291114) is longer compared to isoform PSAP-LS.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF192559.3, AF189289.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000373627.10/
                                                  ENSP00000362730.5
            RefSeq Select criteria             :: based on manual assertion,
                                                  conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..389
                     /product="mitochondrial carrier homolog 1 isoform PSAP-LL"
                     /note="presenilin-associated protein; cell
                     proliferation-inducing protein 60; mitochondrial carrier
                     homolog 1; solute carrier family 25, member 49"
                     /calculated_mol_wt=41413
     Region          1..76
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Region          19
                     /region_name="Alternative start codon encodes isoform
                     PSAP-L"
     Site            29
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Region          76..173
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Region          81..176
                     /region_name="Solcar 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Site            94..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Site            156..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Region          192..280
                     /region_name="Solcar 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Region          206..>264
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Site            210..229
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Site            255..279
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Site            323..342
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Site            372..389
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     CDS             1..389
                     /gene="MTCH1"
                     /gene_synonym="CGI-64; PIG60; PSAP; SLC25A49"
                     /coded_by="NM_001271641.2:24..1193"
                     /note="isoform PSAP-LL is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS64411.1"
                     /db_xref="GeneID:23787"
                     /db_xref="HGNC:HGNC:17586"
                     /db_xref="MIM:610449"
ORIGIN      
        1 mgasdpevap warggaagma gagagagarg gaaagveara rdpppahrah prhprpaaqp
       61 sarrmdggsg glgsgdnapt tealfvalga gvtalshpll yvklliqvgh epmpptlgtn
      121 vlgrkvlylp sfftyakyiv qvdgkiglfr glsprlmsna lstvtrgsmk kvfppdeieq
      181 vsnkddmkts lkkvvketsy emmmqcvsrm lahplhvism rcmvqfvgre akysgvlssi
      241 gkifkeegll gffvgliphl lgdvvflwgc nllahfinay lvddsvsdtp gglgndqnpg
      301 sqfsqalair sytkfvmgia vsmltypfll vgdlmavnnc glqaglppys pvfkswihcw
      361 kylsvqgqlf rgssllfrrv ssgscfale
//
LOCUS       NP_001077089             836 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001077089
VERSION     NP_001077089.2
DBSOURCE    REFSEQ: accession NM_001083620.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 836)
  AUTHORS   Coombs,I.D., Ziobro,J., Krotov,V., Surtees,T.L., Cull-Candy,S.G.
            and Farrant,M.
  TITLE     A gain-of-function GRIA2 variant associated with neurodevelopmental
            delay and seizures: Functional characterization and targeted
            treatment
  JOURNAL   Epilepsia 63 (12), e156-e163 (2022)
   PUBMED   36161652
REFERENCE   2  (residues 1 to 836)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 836)
  AUTHORS   La,T.M., Yamada,H., Seiriki,S., Li,S.A., Fujise,K., Katsumi,N.,
            Abe,T., Watanabe,M. and Takei,K.
  TITLE     Internalization of AMPA-type Glutamate Receptor in the MIN6
            Pancreatic beta-cell Line
  JOURNAL   Cell Struct Funct 45 (2), 121-130 (2020)
   PUBMED   32581155
  REMARK    GeneRIF: Internalization of AMPA-type Glutamate Receptor in the
            MIN6 Pancreatic beta-cell Line.
REFERENCE   4  (residues 1 to 836)
  AUTHORS   Qneibi,M., Hamed,O., Natsheh,A.R., Fares,O., Jaradat,N., Emwas,N.,
            AbuHasan,Q., Al-Kerm,R. and Al-Kerm,R.
  TITLE     Inhibition and assessment of the biophysical gating properties of
            GluA2 and GluA2/A3 AMPA receptors using curcumin derivatives
  JOURNAL   PLoS One 14 (8), e0221132 (2019)
   PUBMED   31454362
  REMARK    GeneRIF: he current study investigated novel curcumin derivatives
            on the biophysical properties of AMPA receptors, specifically on
            the homomeric GluA2 and the heteromeric GluA2/A3 subunits and
            assessed for inhibitory actions
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 836)
  AUTHORS   Higuchi,M., Single,F.N., Kohler,M., Sommer,B., Sprengel,R. and
            Seeburg,P.H.
  TITLE     RNA editing of AMPA receptor subunit GluR-B: a base-paired
            intron-exon structure determines position and efficiency
  JOURNAL   Cell 75 (7), 1361-1370 (1993)
   PUBMED   8269514
REFERENCE   6  (residues 1 to 836)
  AUTHORS   Efthymiou,S., Rumbos Siurana,E., Salpietro,V., Bayat,A. and
            Houlden,H.
  TITLE     GRIA2-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   38224558
REFERENCE   7  (residues 1 to 836)
  AUTHORS   McNamara,J.O., Eubanks,J.H., McPherson,J.D., Wasmuth,J.J.,
            Evans,G.A. and Heinemann,S.F.
  TITLE     Chromosomal localization of human glutamate receptor genes
  JOURNAL   J Neurosci 12 (7), 2555-2562 (1992)
   PUBMED   1319477
REFERENCE   8  (residues 1 to 836)
  AUTHORS   Sun,W., Ferrer-Montiel,A.V., Schinder,A.F., McPherson,J.P.,
            Evans,G.A. and Montal,M.
  TITLE     Molecular cloning, chromosomal mapping, and functional expression
            of human brain glutamate receptors
  JOURNAL   Proc Natl Acad Sci U S A 89 (4), 1443-1447 (1992)
   PUBMED   1311100
REFERENCE   9  (residues 1 to 836)
  AUTHORS   Sommer,B., Kohler,M., Sprengel,R. and Seeburg,P.H.
  TITLE     RNA editing in brain controls a determinant of ion flow in
            glutamate-gated channels
  JOURNAL   Cell 67 (1), 11-19 (1991)
   PUBMED   1717158
REFERENCE   10 (residues 1 to 836)
  AUTHORS   Sommer,B., Keinanen,K., Verdoorn,T.A., Wisden,W., Burnashev,N.,
            Herb,A., Kohler,M., Takagi,T., Sakmann,B. and Seeburg,P.H.
  TITLE     Flip and flop: a cell-specific functional switch in
            glutamate-operated channels of the CNS
  JOURNAL   Science 249 (4976), 1580-1585 (1990)
   PUBMED   1699275
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112240.4 and AC079233.4.
            
            On Mar 28, 2020 this sequence version replaced NP_001077089.1.
            
            Summary: Glutamate receptors are the predominant excitatory
            neurotransmitter receptors in the mammalian brain and are activated
            in a variety of normal neurophysiologic processes. This gene
            product belongs to a family of glutamate receptors that are
            sensitive to alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate
            (AMPA), and function as ligand-activated cation channels. These
            channels are assembled from 4 related subunits, GRIA1-4. The
            subunit encoded by this gene (GRIA2) is subject to RNA editing
            (CAG->CGG; Q->R) within the second transmembrane domain, which is
            thought to render the channel impermeable to Ca(2+). Human and
            animal studies suggest that pre-mRNA editing is essential for brain
            function, and defective GRIA2 RNA editing at the Q/R site may be
            relevant to amyotrophic lateral sclerosis (ALS) etiology.
            Alternative splicing, resulting in transcript variants encoding
            different isoforms, (including the flip and flop isoforms that vary
            in their signal transduction properties), has been noted for this
            gene. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028736.1, SRR1803613.167076.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267774, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            undergoes RNA editing :: PMID: 8269514, 15006707, 14985749
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..836
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q32.1"
     Protein         1..836
                     /product="glutamate receptor 2 isoform 3"
                     /note="glutamate receptor 2; AMPA-selective glutamate
                     receptor 2; AMPA receptor subunit GluA2; glutamate
                     receptor, ionotropic, AMPA 2"
                     /calculated_mol_wt=93645
     Region          1..351
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Region          366..747
                     /region_name="PBP2_iGluR_AMPA"
                     /note="The ligand-binding domain of the AMPA
                     (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic
                     acid) subtypes of ionotropic glutamate receptors, a member
                     of the type 2 periplasmic binding fold protein
                     superfamily; cd13715"
                     /db_xref="CDD:270433"
     Site            order(405,409,456..457,460,465..468,703,721..722,725..730,
                     732,735)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270433"
     Site            order(424,452..454,459,624,627..629,678..679,682,706)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270433"
     Site            order(467..471,725,728,733..734,737)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:270433"
     CDS             1..836
                     /gene="GRIA2"
                     /gene_synonym="GluA2; gluR-2; gluR-B; GluR-K2; GLUR2;
                     GLURB; HBGR2; NEDLIB"
                     /coded_by="NM_001083620.3:161..2671"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS43275.1"
                     /db_xref="GeneID:2891"
                     /db_xref="HGNC:HGNC:4572"
                     /db_xref="MIM:138247"
ORIGIN      
        1 mvqfstsefr ltphidnlev ansfavtnaf csqfsrgvya ifgfydkksv ntitsfcgtl
       61 hvsfitpsfp tdgthpfviq mrpdlkgall slieyyqwdk faylydsdrg lstlqavlds
      121 aaekkwqvta invgninndk kdemyrslfq dlelkkerrv ildcerdkvn divdqvitig
      181 khvkgyhyii anlgftdgdl lkiqfgganv sgfqivdydd slvskfierw stleekeypg
      241 ahtttikyts altydavqvm teafrnlrkq rieisrrgna gdclanpavp wgqgveiera
      301 lkqvqvegls gnikfdqngk rinytinime lktngprkig ywsevdkmvv tltelpsgnd
      361 tsglenktvv vttilespyv mmkknhemle gneryegycv dlaaeiakhc gfkykltivg
      421 dgkygardad tkiwngmvge lvygkadiai apltitlvre evidfskpfm slgisimikk
      481 pqkskpgvfs fldplayeiw mcivfayigv svvlflvsrf spyewhteef edgretqsse
      541 stnefgifns lwfslgafmq qgcdisprsl sgrivggvww fftliiissy tanlaafltv
      601 ermvspiesa edlskqteia ygtldsgstk effrrskiav fdkmwtymrs aepsvfvrtt
      661 aegvarvrks kgkyaylles tmneyieqrk pcdtmkvggn ldskgygiat pkgsslrtpv
      721 nlavlklseq gvldklknkw wydkgecgak dsgskektsa lslsnvagvf yilvgglgla
      781 mlvaliefcy ksraeakrmk vaknaqninp sssqnsqnfa tykegynvyg iesvki
//
LOCUS       NP_001186182             275 aa            linear   PRI 21-NOV-2025
DEFINITION  shugoshin 1 isoform 1CD [Homo sapiens].
ACCESSION   NP_001186182
VERSION     NP_001186182.1
DBSOURCE    REFSEQ: accession NM_001199253.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Yang,Z., Jiang,Y., Wang,L., Yu,B., Cai,H., Fan,J. and Zhang,M.
  TITLE     Prognosis and biological function of SGOL1 in clear cell renal cell
            carcinoma: a multiomics analysis
  JOURNAL   BMC Med Genomics 17 (1), 60 (2024)
   PUBMED   38383432
  REMARK    GeneRIF: Prognosis and biological function of SGOL1 in clear cell
            renal cell carcinoma: a multiomics analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Chetaille,P., Preuss,C., Burkhard,S., Cote,J.M., Houde,C.,
            Castilloux,J., Piche,J., Gosset,N., Leclerc,S., Wunnemann,F.,
            Thibeault,M., Gagnon,C., Galli,A., Tuck,E., Hickson,G.R., El
            Amine,N., Boufaied,I., Lemyre,E., de Santa Barbara,P., Faure,S.,
            Jonzon,A., Cameron,M., Dietz,H.C., Gallo-McFarlane,E., Benson,D.W.,
            Moreau,C., Labuda,D., Zhan,S.H., Shen,Y., Jomphe,M., Jones,S.J.,
            Bakkers,J. and Andelfinger,G.
  CONSRTM   FORGE Canada Consortium
  TITLE     Mutations in SGOL1 cause a novel cohesinopathy affecting heart and
            gut rhythm
  JOURNAL   Nat Genet 46 (11), 1245-1249 (2014)
   PUBMED   25282101
  REMARK    GeneRIF: Mutations in SGOL1 cause a novel cohesinopathy affecting
            heart and gut rhythm.
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Wang,X., Yang,Y., Duan,Q., Jiang,N., Huang,Y., Darzynkiewicz,Z. and
            Dai,W.
  TITLE     sSgo1, a major splice variant of Sgo1, functions in centriole
            cohesion where it is regulated by Plk1
  JOURNAL   Dev Cell 14 (3), 331-341 (2008)
   PUBMED   18331714
  REMARK    GeneRIF: Centriole splitting induced by Sgo1 depletion or
            expression of a dominant negative mutant is suppressed by ectopic
            expression of sSgo1 or by Plk1 knockdown.
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Kitajima,T.S., Sakuno,T., Ishiguro,K., Iemura,S., Natsume,T.,
            Kawashima,S.A. and Watanabe,Y.
  TITLE     Shugoshin collaborates with protein phosphatase 2A to protect
            cohesin
  JOURNAL   Nature 441 (7089), 46-52 (2006)
   PUBMED   16541025
  REMARK    GeneRIF: a specific subtype of serine/threonine protein phosphatase
            2A (PP2A) associates with human shugoshin
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Wang,X., Yang,Y. and Dai,W.
  TITLE     Differential subcellular localizations of two human Sgo1 isoforms:
            implications in regulation of sister chromatid cohesion and
            microtubule dynamics
  JOURNAL   Cell Cycle 5 (6), 635-640 (2006)
   PUBMED   16582621
REFERENCE   8  (residues 1 to 275)
  AUTHORS   McGuinness,B.E., Hirota,T., Kudo,N.R., Peters,J.M. and Nasmyth,K.
  TITLE     Shugoshin prevents dissociation of cohesin from centromeres during
            mitosis in vertebrate cells
  JOURNAL   PLoS Biol 3 (3), e86 (2005)
   PUBMED   15737064
  REMARK    GeneRIF: A shugoshin-like protein associates with centromeres
            during prophase and disappears at the onset of anaphase
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Tang,Z., Sun,Y., Harley,S.E., Zou,H. and Yu,H.
  TITLE     Human Bub1 protects centromeric sister-chromatid cohesion through
            Shugoshin during mitosis
  JOURNAL   Proc Natl Acad Sci U S A 101 (52), 18012-18017 (2004)
   PUBMED   15604152
  REMARK    GeneRIF: Bub1 protects centromeric cohesion through Shugoshin in
            mitosis
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Scanlan,M.J., Gout,I., Gordon,C.M., Williamson,B., Stockert,E.,
            Gure,A.O., Jager,D., Chen,Y.T., Mackay,A., O'Hare,M.J. and Old,L.J.
  TITLE     Humoral immunity to human breast cancer: antigen definition and
            quantitative analysis of mRNA expression
  JOURNAL   Cancer Immun 1, 4 (2001)
   PUBMED   12747765
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX494477.1, AB193059.1,
            AF308299.1, BC032696.1, BX648516.1 and AC099057.3.
            
            Summary: The protein encoded by this gene is a member of the
            shugoshin family of proteins. This protein is thought to protect
            centromeric cohesin from cleavage during mitotic prophase by
            preventing phosphorylation of a cohesin subunit. Reduced expression
            of this gene leads to the premature loss of centromeric cohesion,
            mis-segregation of sister chromatids, and mitotic arrest. Evidence
            suggests that this protein also protects a small subset of cohesin
            found along the length of the chromosome arms during mitotic
            prophase. An isoform lacking exon 6 has been shown to play a role
            in the cohesion of centrioles (PMID: 16582621 and PMID:18331714).
            Mutations in this gene have been associated with Chronic Atrial and
            Intestinal Dysrhythmia (CAID) syndrome, characterized by the
            co-occurrence of Sick Sinus Syndrome (SSS) and Chronic Intestinal
            Pseudo-obstruction (CIPO) within the first four decades of life
            (PMID:25282101). Fibroblast cells from CAID patients exhibited both
            increased cell proliferation and higher rates of senescence.
            Pseudogenes of this gene have been found on chromosomes 1 and 7.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Mar 2015].
            
            Transcript Variant: This variant (Sgo1D, PMID:15737064) uses an
            alternate in-frame splice site in its central coding region
            compared to variant 1. It encodes isoform 1CD which is shorter and
            has a distinct internal amino acid, compared to isoform 1. Both
            variants Sgo1C and Sgo1D encode the same isoform (1CD).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1560325.1,
                                           SRR14038193.3870051.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267758, SAMN03267770
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..275
                     /product="shugoshin 1 isoform 1CD"
                     /note="shugoshin 1AB protein; shugoshin 1CD protein;
                     shugoshin 1EF protein; shugoshin 1GH protein; shugoshin
                     1KL protein; serologically defined breast cancer antigen
                     NY-BR-85"
                     /calculated_mol_wt=31145
     Region          1..176
                     /region_name="Necessary for interaction with PPP2CA and
                     PPP2R1A. /evidence=ECO:0000269|PubMed:16580887"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NEK2.
                     /evidence=ECO:0000269|PubMed:17621308; propagated from
                     UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          22..66
                     /region_name="Shugoshin_N"
                     /note="Shugoshin N-terminal coiled-coil region; pfam07558"
                     /db_xref="CDD:462208"
     Region          222..243
                     /region_name="Shugoshin_C"
                     /note="Shugoshin C terminus; pfam07557"
                     /db_xref="CDD:462207"
     CDS             1..275
                     /gene="SGO1"
                     /gene_synonym="CAID; NY-BR-85; SGO; SGOL1"
                     /coded_by="NM_001199253.3:267..1094"
                     /note="isoform 1CD is encoded by transcript variant Sgo1D"
                     /db_xref="CCDS:CCDS46774.1"
                     /db_xref="GeneID:151648"
                     /db_xref="HGNC:HGNC:25088"
                     /db_xref="MIM:609168"
ORIGIN      
        1 makerclkks fqdsledikk rmkekrnknl aeigkrrsfi aapcqiitnt stllknyqdn
       61 nkmlvlalen ekskvkeaqd iilqlrkecy yltcqlyalk gkltsqqtve paqnqeicss
      121 gmdpnsddss rnlfvkdlpq ipleetelpg qgesfqiedq iptipqdtlg vdfdsatppe
      181 tqqsphlslk ditnvslypv vkirrlslsp kknkaspava lpkrrctasv nykeptlask
      241 lrrgdpftdl cflnspifkq kkdlrrskks mkqiq
//
LOCUS       NP_003865                328 aa            linear   PRI 21-NOV-2025
DEFINITION  SLAM family member 5 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_003865
VERSION     NP_003865.1
DBSOURCE    REFSEQ: accession NM_003874.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Kim,Y., Calderon,A.A., Favaro,P., Glass,D.R., Tsai,A.G., Ho,D.,
            Borges,L., Greenleaf,W.J. and Bendall,S.C.
  TITLE     Terminal deoxynucleotidyl transferase and CD84 identify human
            multi-potent lymphoid progenitors
  JOURNAL   Nat Commun 15 (1), 5910 (2024)
   PUBMED   39003273
  REMARK    GeneRIF: Terminal deoxynucleotidyl transferase and CD84 identify
            human multi-potent lymphoid progenitors.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Lewinsky,H., Gunes,E.G., David,K., Radomir,L., Kramer,M.P.,
            Pellegrino,B., Perpinial,M., Chen,J., He,T.F., Mansour,A.G.,
            Teng,K.Y., Bhattacharya,S., Caserta,E., Troadec,E., Lee,P.,
            Feng,M., Keats,J., Krishnan,A., Rosenzweig,M., Yu,J.,
            Caligiuri,M.A., Cohen,Y., Shevetz,O., Becker-Herman,S.,
            Pichiorri,F., Rosen,S. and Shachar,I.
  TITLE     CD84 is a regulator of the immunosuppressive microenvironment in
            multiple myeloma
  JOURNAL   JCI Insight 6 (4), 141683 (2021)
   PUBMED   33465053
  REMARK    GeneRIF: CD84 is a regulator of the immunosuppressive
            microenvironment in multiple myeloma.
            Erratum:[JCI Insight. 2023 Jul 24;8(14):e173312. doi:
            10.1172/jci.insight.173312. PMID: 37485873]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Barak,A.F., Lewinsky,H., Perpinial,M., Huber,V., Radomir,L.,
            Kramer,M.P., Sever,L., Wolf,Y., Shapiro,M., Herishanu,Y., Jung,S.,
            Becker-Herman,S. and Shachar,I.
  TITLE     Bone marrow dendritic cells support the survival of chronic
            lymphocytic leukemia cells in a CD84 dependent manner
  JOURNAL   Oncogene 39 (9), 1997-2008 (2020)
   PUBMED   31772329
  REMARK    GeneRIF: Bone marrow dendritic cells support the survival of
            chronic lymphocytic leukemia cells in a CD84 dependent manner.
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Vroegindewey,M.M., Oemrawsingh,R.M., Kardys,I., Asselbergs,F.W.,
            van der Harst,P., Oude Ophuis,A.J., Etienne Cramer,G., Maas,A.,
            Hong Kie The,S., Wardeh,A.J., Mouthaan,H., Boersma,E. and
            Akkerhuis,K.M.
  TITLE     The temporal pattern of immune and inflammatory proteins prior to a
            recurrent coronary event in post-acute coronary syndrome patients
  JOURNAL   Biomarkers 24 (2), 199-205 (2019)
   PUBMED   30514120
  REMARK    GeneRIF: Among 29 immune and inflammatory proteins, CXCL1, CD84 and
            TNFRSF10A were associated with early post-acute coronary syndrome
            (ACS) after initial ACS-admission
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Krause,S.W., Rehli,M., Heinz,S., Ebner,R. and Andreesen,R.
  TITLE     Characterization of MAX.3 antigen, a glycoprotein expressed on
            mature macrophages, dendritic cells and blood platelets: identity
            with CD84
  JOURNAL   Biochem J 346 Pt 3 (Pt 3), 729-736 (2000)
   PUBMED   10698700
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Palou,E., Pirotto,F., Sole,J., Freed,J.H., Peral,B., Vilardell,C.,
            Vilella,R., Vives,J. and Gaya,A.
  TITLE     Genomic characterization of CD84 reveals the existence of five
            isoforms differing in their cytoplasmic domains
  JOURNAL   Tissue Antigens 55 (2), 118-127 (2000)
   PUBMED   10746783
REFERENCE   8  (residues 1 to 328)
  AUTHORS   de la Fuente,M.A., Pizcueta,P., Nadal,M., Bosch,J. and Engel,P.
  TITLE     CD84 leukocyte antigen is a new member of the Ig superfamily
  JOURNAL   Blood 90 (6), 2398-2405 (1997)
   PUBMED   9310491
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Kingsmore,S.F., Souryal,C.A., Watson,M.L., Patel,D.D. and
            Seldin,M.F.
  TITLE     Physical and genetic linkage of the genes encoding Ly-9 and CD48 on
            mouse and human chromosomes 1
  JOURNAL   Immunogenetics 42 (1), 59-62 (1995)
   PUBMED   7797269
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Andreesen,R., Bross,K.J., Osterholz,J. and Emmrich,F.
  TITLE     Human macrophage maturation and heterogeneity: analysis with a
            newly generated set of monoclonal antibodies to differentiation
            antigens
  JOURNAL   Blood 67 (5), 1257-1264 (1986)
   PUBMED   3008886
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL138930.15, BC020063.1 and CA448708.1.
            
            Summary: This gene encodes a membrane glycoprotein that is a member
            of the signaling lymphocyte activation molecule (SLAM) family. This
            family forms a subset of the larger CD2 cell-surface receptor Ig
            superfamily. The encoded protein is a homophilic adhesion molecule
            that is expressed in numerous immune cells types and is involved in
            regulating receptor-mediated signaling in those cells. Alternate
            splicing results in multiple transcript variants. [provided by
            RefSeq, Oct 2011].
            
            Transcript Variant: This variant (2) lacks an alternate, in-frame
            segment, compared to variant 1. The resulting protein (isoform 2)
            is shorter when it is compared to isoform 1. This variant has also
            been called CD84c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC020063.1, AJ223324.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368054.8/ ENSP00000357033.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..328
                     /product="SLAM family member 5 isoform 2 precursor"
                     /note="CD84 antigen (leukocyte antigen); leukocyte antigen
                     CD84; SLAM family member 5; leukocyte differentiation
                     antigen CD84; leucocyte differentiation antigen CD84;
                     hly9-beta; cell surface antigen MAX.3; signaling
                     lymphocytic activation molecule 5"
                     /calculated_mol_wt=34457
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2432
     Region          27..129
                     /region_name="Ig_SLAM-like_N"
                     /note="N-terminal immunoglobulin (Ig)-like domain of the
                     signaling lymphocyte activation molecule (SLAM) family;
                     cd16842"
                     /db_xref="CDD:409517"
     Region          27..32
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409517"
     Region          35..41
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409517"
     Site            order(51,53,108,110,112)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409517"
     Region          59..64
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409517"
     Region          72..77
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409517"
     Region          84..89
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409517"
     Region          92..97
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409517"
     Region          105..112
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409517"
     Region          119..129
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409517"
     Region          150..207
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     CDS             1..328
                     /gene="CD84"
                     /gene_synonym="hCD84; LY9B; mCD84; SLAMF5"
                     /coded_by="NM_003874.4:60..1046"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS1206.1"
                     /db_xref="GeneID:8832"
                     /db_xref="HGNC:HGNC:1704"
                     /db_xref="MIM:604513"
ORIGIN      
        1 maqhhlwill lclqtwpeaa gkdseiftvn gilgesvtfp vniqeprqvk iiawtsktsv
       61 ayvtpgdset apvvtvthrn yyerihalgp nynlvisdlr medagdykad intqadpytt
      121 tkrynlqiyr rlgkpkitqs lmasvnstcn vtltcsveke eknvtynwsp lgeegnvlqi
      181 fqtpedqelt ytctaqnpvs nnsdsisarq lcadiamgfr thhtgllsvl amffllvlil
      241 ssvflfrlfk rrqdaaskkt iytyimasrn tqpaesriyd eilqskvlps keepvntvys
      301 evqfadkmgk astqdskppg tssyeivi
//
LOCUS       NP_598400                717 aa            linear   PRI 21-NOV-2025
DEFINITION  5-taurinomethyluridine-[tRNA] synthase subunit MTO1, mitochondrial
            isoform b [Homo sapiens].
ACCESSION   NP_598400
VERSION     NP_598400.1
DBSOURCE    REFSEQ: accession NM_133645.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Zhou,C., Wang,J., Zhang,Q., Yang,Q., Yi,S., Shen,Y., Luo,J. and
            Qin,Z.
  TITLE     Clinical and genetic analysis of combined oxidative phosphorylation
            defificiency-10 caused by MTO1 mutation
  JOURNAL   Clin Chim Acta 526, 74-80 (2022)
   PUBMED   34990597
  REMARK    GeneRIF: Clinical and genetic analysis of combined oxidative
            phosphorylation defificiency-10 caused by MTO1 mutation.
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Li,D., Zhang,J., Yang,J., Wang,J., Zhang,R., Li,J. and Zhang,R.
  TITLE     CircMTO1 suppresses hepatocellular carcinoma progression via the
            miR-541-5p/ZIC1 axis by regulating Wnt/beta-catenin signaling
            pathway and epithelial-to-mesenchymal transition
  JOURNAL   Cell Death Dis 13 (1), 12 (2021)
   PUBMED   34930906
  REMARK    GeneRIF: CircMTO1 suppresses hepatocellular carcinoma progression
            via the miR-541-5p/ZIC1 axis by regulating Wnt/beta-catenin
            signaling pathway and epithelial-to-mesenchymal transition.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 717)
  AUTHORS   Ji,N., Wang,Y., Gong,X., Ni,S. and Zhang,H.
  TITLE     CircMTO1 inhibits ox-LDL-stimulated vascular smooth muscle cell
            proliferation and migration via regulating the miR-182-5p/RASA1
            axis
  JOURNAL   Mol Med 27 (1), 73 (2021)
   PUBMED   34238206
  REMARK    GeneRIF: CircMTO1 inhibits ox-LDL-stimulated vascular smooth muscle
            cell proliferation and migration via regulating the
            miR-182-5p/RASA1 axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 717)
  AUTHORS   Peng,G.X., Zhang,Y., Wang,Q.Q., Li,Q.R., Xu,H., Wang,E.D. and
            Zhou,X.L.
  TITLE     The human tRNA taurine modification enzyme GTPBP3 is an active
            GTPase linked to mitochondrial diseases
  JOURNAL   Nucleic Acids Res 49 (5), 2816-2834 (2021)
   PUBMED   33619562
REFERENCE   6  (residues 1 to 717)
  AUTHORS   Umeda,N., Suzuki,T., Yukawa,M., Ohya,Y., Shindo,H., Watanabe,K. and
            Suzuki,T.
  TITLE     Mitochondria-specific RNA-modifying enzymes responsible for the
            biosynthesis of the wobble base in mitochondrial tRNAs.
            Implications for the molecular pathogenesis of human mitochondrial
            diseases
  JOURNAL   J Biol Chem 280 (2), 1613-1624 (2005)
   PUBMED   15509579
REFERENCE   7  (residues 1 to 717)
  AUTHORS   Bykhovskaya,Y., Mengesha,E., Wang,D., Yang,H., Estivill,X.,
            Shohat,M. and Fischel-Ghodsian,N.
  TITLE     Phenotype of non-syndromic deafness associated with the
            mitochondrial A1555G mutation is modulated by mitochondrial RNA
            modifying enzymes MTO1 and GTPBP3
  JOURNAL   Mol Genet Metab 83 (3), 199-206 (2004)
   PUBMED   15542390
  REMARK    GeneRIF: Phenotype of non-syndromic deafness associated with the
            mitochondrial A1555G mutation is modulated by mitochondrial RNA
            modifying enzymes MTO1 and GTPBP3.
REFERENCE   8  (residues 1 to 717)
  AUTHORS   Finnila,S. and Majamaa,K.
  TITLE     Lack of a modulative factor in locus 8p23 in a Finnish family with
            nonsyndromic sensorineural hearing loss associated with the 1555A>G
            mitochondrial DNA mutation
  JOURNAL   Eur J Hum Genet 11 (9), 652-658 (2003)
   PUBMED   12939650
REFERENCE   9  (residues 1 to 717)
  AUTHORS   Li,X., Li,R., Lin,X. and Guan,M.X.
  TITLE     Isolation and characterization of the putative nuclear modifier
            gene MTO1 involved in the pathogenesis of deafness-associated
            mitochondrial 12 S rRNA A1555G mutation
  JOURNAL   J Biol Chem 277 (30), 27256-27264 (2002)
   PUBMED   12011058
  REMARK    GeneRIF: identification of full-length cDNA and elucidation of
            genomic organization of the human MTO1 homolog
REFERENCE   10 (residues 1 to 717)
  AUTHORS   Rahman,S., Thorburn,D.R. and Ball,M.
  TITLE     Nuclear Gene-Encoded Leigh Syndrome Spectrum Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26425749
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DN993156.1, AK074625.1,
            AY078986.1, BE501391.1 and AL603910.6.
            
            Summary: This gene encodes a mitochondrial protein thought to be
            involved in mitochondrial tRNA modification. The encoded protein
            may also play a role in the expression of the non-syndromic and
            aminoglycoside-induced deafness phenotypes associated with a
            specific mutation in the mitochondrial 12S rRNA gene. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) includes an additional
            in-frame exon compared to variant 1; it encodes isoform b which is
            longer than isoform a. The additional protein-coding exon contains
            Alu Sine repeat sequence.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY078986.1, AY078985.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..717
                     /product="5-taurinomethyluridine-[tRNA] synthase subunit
                     MTO1, mitochondrial isoform b"
                     /note="homolog of yeast Mto1; protein MTO1 homolog,
                     mitochondrial; mitochondrial MTO1-3; mitochondrial
                     translation optimization 1 homolog;
                     5-taurinomethyluridine-[tRNA] synthase subunit MTO1,
                     mitochondrial"
                     /calculated_mol_wt=79833
     Region          36..695
                     /region_name="MnmG"
                     /note="tRNA U34 5-carboxymethylaminomethyl modifying
                     enzyme MnmG/GidA [Translation, ribosomal structure and
                     biogenesis]; COG0445"
                     /db_xref="CDD:440214"
     Site            533
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2Z2.2)"
     CDS             1..717
                     /gene="MTO1"
                     /gene_synonym="CGI-02; COXPD10"
                     /coded_by="NM_133645.3:119..2272"
                     /note="isoform b is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4979.1"
                     /db_xref="GeneID:25821"
                     /db_xref="HGNC:HGNC:19261"
                     /db_xref="MIM:614667"
ORIGIN      
        1 mfyfrgcgrw vavsftkqqf plarlssdsa aprtphfdvi viggghagte aataaarcgs
       61 rtlllthrvd tigqmscnps fggigkghlm revdaldglc sricdqsgvh ykvlnrrkgp
      121 avwglraqid rklykqnmqk eilntplltv qegavedlil tepepehtgk crvsgvvlvd
      181 gstvyaesvi lttgtflrgm iviglethpa grlgdqpsig laqtleklgf vvgrlktgtp
      241 priakesinf silnkhipdn psipfsftne tvwikpedql pcylthtnpr vdeivlknlh
      301 lnshvkettr gprycpsies kvlrfpnrlh qvwlepegmd sdliypqgls mtlpaelqek
      361 mitcirglek akviqpdgvl lllprmecng aisahhnlpl pgygvqydyl dprqitpsle
      421 thlvqrlffa gqingttgye eaaaqgviag inaslrvsrk ppfvvsrteg yigvliddlt
      481 tlgtsepyrm ftsrvefrls lrpdnadsrl tlrgykdagc vsqqryerac wmkssleegi
      541 svlksiefls skwkklipea sistsrslpv raldvlkyee vdmdslakav peplkkytkc
      601 relaerlkie atyesvlfhq lqeikgvqqd ealqlpkdld yltirdvsls hevreklhfs
      661 rpqtigaasr ipgvtpaaii nllrfvkttq rrqsamness ktdqylcdad rlqerel
//
LOCUS       NP_059107                294 aa            linear   PRI 21-NOV-2025
DEFINITION  survival motor neuron protein isoform d [Homo sapiens].
ACCESSION   NP_059107
VERSION     NP_059107.1
DBSOURCE    REFSEQ: accession NM_017411.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Ricci,M., Cicala,G., Capasso,A., Coratti,G., Fiori,S., Cutrona,C.,
            D'Amico,A., Sansone,V.A., Bruno,C., Messina,S., Mongini,T.,
            Coccia,M., Siciliano,G., Pegoraro,E., Masson,R., Filosto,M.,
            Comi,G.P., Corti,S., Ronchi,D., Maggi,L., D'Angelo,M.G.,
            Vacchiano,V., Ticci,C., Ruggiero,L., Verriello,L., Ricci,F.S.,
            Berardinelli,A.L., Maioli,M.A., Garibaldi,M., Nigro,V.,
            Previtali,S.C., Pera,M.C., Tizzano,E., Pane,M., Tiziano,F.D. and
            Mercuri,E.
  CONSRTM   ITASMAC Working Group
  TITLE     Clinical Phenotype of Pediatric and Adult Patients With Spinal
            Muscular Atrophy With Four SMN2 Copies: Are They Really All Stable?
  JOURNAL   Ann Neurol 94 (6), 1126-1135 (2023)
   PUBMED   37695206
  REMARK    GeneRIF: Clinical Phenotype of Pediatric and Adult Patients With
            Spinal Muscular Atrophy With Four SMN2 Copies: Are They Really All
            Stable?
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Kimizu,T., Ida,S., Oki,K., Shima,M., Nishimoto,S., Nakajima,K.,
            Ikeda,T., Mogami,Y., Yanagihara,K., Matsuda,K., Nishi,E.,
            Hasegawa,Y., Nozaki,M., Fujita,H., Irie,A., Katayama,T.,
            Okamoto,N., Imai,K., Nishio,H. and Suzuki,Y.
  TITLE     Newborn screening for spinal muscular atrophy in Osaka -challenges
            in a Japanese pilot study
  JOURNAL   Brain Dev 45 (7), 363-371 (2023)
   PUBMED   36973114
  REMARK    GeneRIF: Newborn screening for spinal muscular atrophy in Osaka
            -challenges in a Japanese pilot study.
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Davidson,J.E., Russell,J.S., Martinez,N.N., Mowat,D.R., Jones,K.J.,
            Kirk,E.P., Kariyawasam,D., Farrar,M. and D'Silva,A.
  TITLE     The Carrier Frequency of Two SMN1 Genes in Parents of Symptomatic
            Children with SMA and the Significance of SMN1 Exon 8 in Carriers
  JOURNAL   Genes (Basel) 14 (7), 1403 (2023)
   PUBMED   37510307
  REMARK    GeneRIF: The Carrier Frequency of Two SMN1 Genes in Parents of
            Symptomatic Children with SMA and the Significance of SMN1 Exon 8
            in Carriers.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Wang,L., Ji,Y., Chen,Y., Bai,J., Gao,P. and Feng,P.
  TITLE     A splicing silencer in SMN2 intron 6 is critical in spinal muscular
            atrophy
  JOURNAL   Hum Mol Genet 32 (6), 971-983 (2023)
   PUBMED   36255739
  REMARK    GeneRIF: A splicing silencer in SMN2 intron 6 is critical in spinal
            muscular atrophy.
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Liu,Q. and Dreyfuss,G.
  TITLE     A novel nuclear structure containing the survival of motor neurons
            protein
  JOURNAL   EMBO J 15 (14), 3555-3565 (1996)
   PUBMED   8670859
REFERENCE   7  (residues 1 to 294)
  AUTHORS   Gennarelli,M., Lucarelli,M., Capon,F., Pizzuti,A., Merlini,L.,
            Angelini,C., Novelli,G. and Dallapiccola,B.
  TITLE     Survival motor neuron gene transcript analysis in muscles from
            spinal muscular atrophy patients
  JOURNAL   Biochem Biophys Res Commun 213 (1), 342-348 (1995)
   PUBMED   7639755
REFERENCE   8  (residues 1 to 294)
  AUTHORS   Lefebvre,S., Burglen,L., Reboullet,S., Clermont,O., Burlet,P.,
            Viollet,L., Benichou,B., Cruaud,C., Millasseau,P., Zeviani,M. et
            al.
  TITLE     Identification and characterization of a spinal muscular
            atrophy-determining gene
  JOURNAL   Cell 80 (1), 155-165 (1995)
   PUBMED   7813012
REFERENCE   9  (residues 1 to 294)
  AUTHORS   van der Steege,G., Draaijers,T.G., Grootscholten,P.M., Osinga,J.,
            Anzevino,R., Velona,I., Den Dunnen,J.T., Scheffer,H., Brahe,C., van
            Ommen,G.J. et al.
  TITLE     A provisional transcript map of the spinal muscular atrophy (SMA)
            critical region
  JOURNAL   Eur J Hum Genet 3 (2), 87-95 (1995)
   PUBMED   7552146
REFERENCE   10 (residues 1 to 294)
  AUTHORS   Prior,T.W., Leach,M.E. and Finanger,E.L.
  TITLE     Spinal Muscular Atrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301526
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC015308.1, CN272420.1 and
            AI312583.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is part of a 500 kb inverted duplication on
            chromosome 5q13. This duplicated region contains at least four
            genes and repetitive elements which make it prone to rearrangements
            and deletions. The repetitiveness and complexity of the sequence
            have also caused difficulty in determining the organization of this
            genomic region. The telomeric and centromeric copies of this gene
            are nearly identical and encode the same protein. While mutations
            in the telomeric copy are associated with spinal muscular atrophy,
            mutations in this gene, the centromeric copy, do not lead to
            disease. This gene may be a modifier of disease caused by mutation
            in the telomeric copy. The critical sequence difference between the
            two genes is a single nucleotide in exon 7, which is thought to be
            an exon splice enhancer. Note that the nine exons of both the
            telomeric and centromeric copies are designated historically as
            exon 1, 2a, 2b, and 3-8. It is thought that gene conversion events
            may involve the two genes, leading to varying copy numbers of each
            gene. The full length protein encoded by this gene localizes to
            both the cytoplasm and the nucleus. Within the nucleus, the protein
            localizes to subnuclear bodies called gems which are found near
            coiled bodies containing high concentrations of small
            ribonucleoproteins (snRNPs). This protein forms heteromeric
            complexes with proteins such as SIP1 and GEMIN4, and also interacts
            with several proteins known to be involved in the biogenesis of
            snRNPs, such as hnRNP U protein and the small nucleolar RNA binding
            protein. Four transcript variants encoding distinct isoforms have
            been described. [provided by RefSeq, Sep 2008].
            
            Transcript Variant: This variant (d) represents the longest
            transcript and encodes the longest isoform (d).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410571.120678.1,
                                           SRR7410571.120550.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380743.9/ ENSP00000370119.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13.2"
     Protein         1..294
                     /product="survival motor neuron protein isoform d"
                     /note="survival motor neuron protein; gemin-1; component
                     of gems 1; tudor domain containing 16B"
                     /calculated_mol_wt=31718
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q16637.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:21609790,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:21609790,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q16637.1)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:21609790,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16637.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q16637.1)"
     Region          26..291
                     /region_name="SMN"
                     /note="Survival motor neuron protein (SMN); pfam06003"
                     /db_xref="CDD:428716"
     Region          26..51
                     /region_name="Interacts with GEMIN2.
                     /evidence=ECO:0000269|PubMed:21816274,
                     ECO:0000269|PubMed:22607171, ECO:0000269|PubMed:26092730"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Region          59..88
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16637.1)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA.
                     /evidence=ECO:0000269|PubMed:21609790; propagated from
                     UniProtKB/Swiss-Prot (Q16637.1)"
     Region          97..209
                     /region_name="Required for interaction with RPP20/POP7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Region          156..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:21609790; propagated from
                     UniProtKB/Swiss-Prot (Q16637.1)"
     Region          240..267
                     /region_name="P2 (binding site for SNRPB)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Region          252..280
                     /region_name="Involved in homooligomerization.
                     /evidence=ECO:0000269|PubMed:10500148,
                     ECO:0000269|PubMed:14715275, ECO:0000269|PubMed:17178713,
                     ECO:0000269|PubMed:21816274, ECO:0000269|PubMed:23022347,
                     ECO:0000269|PubMed:26092730"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Region          279..294
                     /region_name="Required for interaction with SYNCRIP.
                     /evidence=ECO:0000269|PubMed:11574476"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     CDS             1..294
                     /gene="SMN2"
                     /gene_synonym="BCD541; C-BCD541; GEMIN1; SMNC; TDRD16B"
                     /coded_by="NM_017411.4:18..902"
                     /note="isoform d is encoded by transcript variant d"
                     /db_xref="CCDS:CCDS4007.1"
                     /db_xref="GeneID:6607"
                     /db_xref="HGNC:HGNC:11118"
                     /db_xref="MIM:601627"
ORIGIN      
        1 mamssggsgg gvpeqedsvl frrgtgqsdd sdiwddtali kaydkavasf khalkngdic
       61 etsgkpkttp krkpakknks qkkntaaslq qwkvgdkcsa iwsedgciyp atiasidfkr
      121 etcvvvytgy gnreeqnlsd llspicevan nieqnaqene nesqvstdes ensrspgnks
      181 dnikpksapw nsflpppppm pgprlgpgkp glkfngpppp pppppphlls cwlppfpsgp
      241 piipppppic pdslddadal gsmliswyms gyhtgyymgf rqnqkegrcs hsln
//
LOCUS       NP_001337873             376 aa            linear   PRI 21-NOV-2025
DEFINITION  actin-related protein 3B isoform 4 [Homo sapiens].
ACCESSION   NP_001337873
VERSION     NP_001337873.1
DBSOURCE    REFSEQ: accession NM_001350944.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Abella,J.V., Galloni,C., Pernier,J., Barry,D.J., Kjaer,S.,
            Carlier,M.F. and Way,M.
  TITLE     Isoform diversity in the Arp2/3 complex determines actin filament
            dynamics
  JOURNAL   Nat Cell Biol 18 (1), 76-86 (2016)
   PUBMED   26655834
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Shin,J.H., Gulesserian,T., Weitzdoerfer,R., Fountoulakis,M. and
            Lubec,G.
  TITLE     Derangement of hypothetical proteins in fetal Down's syndrome brain
  JOURNAL   Neurochem Res 29 (6), 1307-1316 (2004)
   PUBMED   15176487
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Shindo-Okada,N. and Iigo,M.
  TITLE     Expression of the Arp11 gene suppresses the tumorigenicity of PC-14
            human lung adenocarcinoma cells
  JOURNAL   Biochem Biophys Res Commun 312 (4), 889-896 (2003)
   PUBMED   14651955
  REMARK    GeneRIF: Thus, overexpression of Arp11 may suppress tumorigenicity
            in nude mice.
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Eckley,D.M. and Schroer,T.A.
  TITLE     Interactions between the evolutionarily conserved, actin-related
            protein, Arp11, actin, and Arp1
  JOURNAL   Mol Biol Cell 14 (7), 2645-2654 (2003)
   PUBMED   12857853
REFERENCE   8  (residues 1 to 376)
  AUTHORS   Shindo-Okada,N. and Shimizu,K.
  TITLE     Isolation of a novel actin-related gene expressed in low-metastatic
            PC-14 human lung adenocarcinoma
  JOURNAL   Biochem Biophys Res Commun 280 (1), 61-67 (2001)
   PUBMED   11162478
REFERENCE   9  (residues 1 to 376)
  AUTHORS   Jay,P., Berge-Lefranc,J.L., Massacrier,A., Roessler,E., Wallis,D.,
            Muenke,M., Gastaldi,M., Taviaux,S., Cau,P. and Berta,P.
  TITLE     ARP3beta, the gene encoding a new human actin-related protein, is
            alternatively spliced and predominantly expressed in brain neuronal
            cells
  JOURNAL   Eur J Biochem 267 (10), 2921-2928 (2000)
   PUBMED   10806390
REFERENCE   10 (residues 1 to 376)
  AUTHORS   Machesky,L.M. and Gould,K.L.
  TITLE     The Arp2/3 complex: a multifunctional actin organizer
  JOURNAL   Curr Opin Cell Biol 11 (1), 117-121 (1999)
   PUBMED   10047519
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092180.5 and AC072057.8.
            
            Summary: This gene encodes a member of the actin-related proteins
            (ARP), which form multiprotein complexes and share 35-55% amino
            acid identity with conventional actin. The protein encoded by this
            gene may have a regulatory role in the actin cytoskeleton and
            induce cell-shape change and motility. Pseudogenes of this gene are
            located on chromosomes 2, 4, 10, 16, 22 and Y. Alternative splicing
            results in multiple transcript variants and protein isoforms.
            [provided by RefSeq, Jul 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.212690.1,
                                           SRR1660805.206084.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1-q36.2"
     Protein         1..376
                     /product="actin-related protein 3B isoform 4"
                     /note="actin-related protein 3-beta; actin-related protein
                     Arp11; ARP3-beta; actin-like protein 3B; actin-related
                     protein ARP4; ARP3 actin related protein 3 homolog B"
                     /calculated_mol_wt=42705
     Region          7..368
                     /region_name="ASKHA_NBD_Arp3-like"
                     /note="nucleotide-binding domain (NBD) of actin-related
                     protein3 (Arp3) and similar proteins; cd10221"
                     /db_xref="CDD:466822"
     CDS             1..376
                     /gene="ACTR3B"
                     /gene_synonym="ARP11; ARP3BETA"
                     /coded_by="NM_001350944.2:132..1262"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:57180"
                     /db_xref="HGNC:HGNC:17256"
ORIGIN      
        1 magslppcvv dcgtgytklg yagntepqfi ipsciaires akvvdqaqrr vlrgvddldf
       61 figdeaidkp tyatkwpirh giiedwdlme rfmeqvvfky lraepedhyf lmtepplntp
      121 enreylaeim fesfnvpgly iavqavlala aswtsrqvge rtltgivids gdgvthvipv
      181 aegyvigsci khipiagrdi tyfiqqllre revgippeqs letakaikek ycyicpdivk
      241 efakydvdpr kwikqytgin ainqkkfvid vgyerflgpe iffhpefanp dfmesisdvv
      301 deviqncpid vrrplykpkp vevqvvthhm qryavwfggs mlastpeffq vchtkkdyee
      361 ygpsicrhnp vfgvms
//
LOCUS       NP_001362611             491 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform v [Homo sapiens].
ACCESSION   NP_001362611 XP_016858611
VERSION     NP_001362611.1
DBSOURCE    REFSEQ: accession NM_001375682.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            On Oct 31, 2019 this sequence version replaced XP_016858611.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..491
                     /product="abl interactor 2 isoform v"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=52859
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62484; propagated from
                     UniProtKB/Swiss-Prot (Q9NYB9.1)"
     Region          93..156
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          <221..357
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          430..490
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(438,440,443,447,465..466,479,481..482)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..491
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375682.1:122..1597"
                     /note="isoform v is encoded by transcript variant 27"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqs adkqraleet kayttqslas
       61 vaylintlan nvlqmldiqa sqlrrmessi nhisqtvdih kekvarreig ilttnkntsr
      121 thkiiapanl erpvryirkp idytilddig hgvkwllrfk vstqnmkmgg lprttpptqk
      181 ppsppmsgkg tlgssgssgg shpssrsssr ensgsgsvgv piavptpspp svfpapagsa
      241 gtpplpatsa sapaplvpat vpsstapdaa aggaqtladg ftsptppvvs stpptghpvq
      301 fysmnrpasr htpptiggsl pyrrppsits qtslqnqmng gpfysqnpvs lappppsilq
      361 vtpqlplmgf varvqenntp pppppveepv fdespppppp pedyeeeeaa vveysdpyae
      421 edppwaprsy lekvvaiydy tkdkedelsf qegaiiyvik knddgwyegv mngvtglfpg
      481 nyvesimhys e
//
LOCUS       NP_861440                522 aa            linear   PRI 21-NOV-2025
DEFINITION  plexin-A4 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_861440
VERSION     NP_861440.2
DBSOURCE    REFSEQ: accession NM_181775.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Cho,H., Park,H.J. and Seo,Y.K.
  TITLE     Induction of PLXNA4 Gene during Neural Differentiation in Human
            Umbilical-Cord-Derived Mesenchymal Stem Cells by Low-Intensity
            Sub-Sonic Vibration
  JOURNAL   Int J Mol Sci 23 (3), 1522 (2022)
   PUBMED   35163445
  REMARK    GeneRIF: Induction of PLXNA4 Gene during Neural Differentiation in
            Human Umbilical-Cord-Derived Mesenchymal Stem Cells by
            Low-Intensity Sub-Sonic Vibration.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Razzaq,M., Iglesias,M.J., Ibrahim-Kosta,M., Goumidi,L.,
            Soukarieh,O., Proust,C., Roux,M., Suchon,P., Boland,A., Daiain,D.,
            Olaso,R., Havervall,S., Thalin,C., Butler,L., Deleuze,J.F.,
            Odeberg,J., Morange,P.E. and Tregouet,D.A.
  TITLE     An artificial neural network approach integrating plasma proteomics
            and genetic data identifies PLXNA4 as a new susceptibility locus
            for pulmonary embolism
  JOURNAL   Sci Rep 11 (1), 14015 (2021)
   PUBMED   34234248
  REMARK    GeneRIF: An artificial neural network approach integrating plasma
            proteomics and genetic data identifies PLXNA4 as a new
            susceptibility locus for pulmonary embolism.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 522)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 522)
  AUTHORS   Maestrini,E., Pagnamenta,A.T., Lamb,J.A., Bacchelli,E., Sykes,N.H.,
            Sousa,I., Toma,C., Barnby,G., Butler,H., Winchester,L.,
            Scerri,T.S., Minopoli,F., Reichert,J., Cai,G., Buxbaum,J.D.,
            Korvatska,O., Schellenberg,G.D., Dawson,G., de Bildt,A.,
            Minderaa,R.B., Mulder,E.J., Morris,A.P., Bailey,A.J. and
            Monaco,A.P.
  CONSRTM   IMGSAC
  TITLE     High-density SNP association study and copy number variation
            analysis of the AUTS1 and AUTS5 loci implicate the IMMP2L-DOCK4
            gene region in autism susceptibility
  JOURNAL   Mol Psychiatry 15 (9), 954-968 (2010)
   PUBMED   19401682
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 522)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   8  (residues 1 to 522)
  AUTHORS   Whitford,K.L. and Ghosh,A.
  TITLE     Plexin signaling via off-track and rho family GTPases
  JOURNAL   Neuron 32 (1), 1-3 (2001)
   PUBMED   11604131
  REMARK    Review article
REFERENCE   9  (residues 1 to 522)
  AUTHORS   Tamagnone,L., Artigiani,S., Chen,H., He,Z., Ming,G.I., Song,H.,
            Chedotal,A., Winberg,M.L., Goodman,C.S., Poo,M., Tessier-Lavigne,M.
            and Comoglio,P.M.
  TITLE     Plexins are a large family of receptors for transmembrane,
            secreted, and GPI-anchored semaphorins in vertebrates
  JOURNAL   Cell 99 (1), 71-80 (1999)
   PUBMED   10520995
  REMARK    Erratum:[Cell 2001 Jan 26;104(2):following 320]
REFERENCE   10 (residues 1 to 522)
  AUTHORS   Touchman,J.W., Bouffard,G.G., Weintraub,L.A., Idol,J.R., Wang,L.,
            Robbins,C.M., Nussbaum,J.C., Lovett,M. and Green,E.D.
  TITLE     2006 expressed-sequence tags derived from human chromosome
            7-enriched cDNA libraries
  JOURNAL   Genome Res 7 (3), 281-292 (1997)
   PUBMED   9074931
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC028744.2 and AL137352.1.
            
            On Sep 28, 2007 this sequence version replaced NP_861440.1.
            
            Transcript Variant: This variant (2) has different 5' and 3'
            terminal exons, and is missing many coding exons found in variant
            1. It thus encodes a shorter isoform (2) with the same N-terminus,
            but a different C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: GQ901020.1, BC028744.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q32.3"
     Protein         1..522
                     /product="plexin-A4 isoform 2 precursor"
                     /note="epididymis secretory sperm binding protein"
                     /calculated_mol_wt=55589
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2594
     Region          39..469
                     /region_name="Sema"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorins and plexins; cl15693"
                     /db_xref="CDD:472829"
     CDS             1..522
                     /gene="PLXNA4"
                     /gene_synonym="FAYV2820; PLEXA4; PLXNA4A; PLXNA4B;
                     PRO34003"
                     /coded_by="NM_181775.4:378..1946"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS5826.1"
                     /db_xref="GeneID:91584"
                     /db_xref="HGNC:HGNC:9102"
                     /db_xref="MIM:604280"
ORIGIN      
        1 mkampwnwtc llshllmvgm gsstlltrqp aplsqkqrsf vtfrgepaeg fnhlvvdert
       61 ghiylgavnr iyklssdlkv lvthetgpde dnpkcyppri vqtcnepltt tnnvnkmlli
      121 dykenrliac gslyqgickl lrledlfklg epyhkkehyl sgvnesgsvf gvivsysnld
      181 dklfiatavd gkpeyfptis srkltknsea dgmfayvfhd efvasmikip sdtftiipdf
      241 diyyvygfss gnfvyfltlq pemvsppgst tkeqvytskl vrlckedtaf nsyvevpigc
      301 ersgveyrll qaaylskaga vlgrtlgvhp dddllftvfs kgqkrkmksl desalcifil
      361 kqindriker lqscyrgegt ldlawlkvkd ipcssallti ddnfcgldmn aplgvsdmvr
      421 gipvftedrd rmtsviayvy knhslafvgt ksgklkksfg tgpqggitqe wigvegdppg
      481 aniasqeqml cvylqcsshk aisdqrvqpl lccflnvpgn ss
//
LOCUS       NP_001374648            1008 aa            linear   PRI 21-NOV-2025
DEFINITION  activated CDC42 kinase 1 isoform 13 [Homo sapiens].
ACCESSION   NP_001374648
VERSION     NP_001374648.1
DBSOURCE    REFSEQ: accession NM_001387719.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Zheng,D., Wei,Z., Zhang,C., Liu,W., Gong,C., Wu,F. and Guo,W.
  TITLE     ZNF692 promotes osteosarcoma cell proliferation, migration, and
            invasion through TNK2-mediated activation of the MEK/ERK pathway
  JOURNAL   Biol Direct 19 (1), 28 (2024)
   PUBMED   38650011
  REMARK    GeneRIF: ZNF692 promotes osteosarcoma cell proliferation,
            migration, and invasion through TNK2-mediated activation of the
            MEK/ERK pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Hodder,S., Fox,M., Binti Ahmad Mokhtar,A.M., Mott,H.R. and Owen,D.
  TITLE     ACKnowledging the role of the Activated-Cdc42 associated kinase
            (ACK) in regulating protein stability in cancer
  JOURNAL   Small GTPases 14 (1), 14-25 (2023)
   PUBMED   37194323
  REMARK    GeneRIF: ACKnowledging the role of the Activated-Cdc42 associated
            kinase (ACK) in regulating protein stability in cancer.
            Review article
REFERENCE   4  (residues 1 to 1008)
  AUTHORS   Zhou,A., Zhang,W. and Wang,B.
  TITLE     Host factor TNK2 is required for influenza virus infection
  JOURNAL   Genes Genomics 45 (6), 771-781 (2023)
   PUBMED   37133719
  REMARK    GeneRIF: Host factor TNK2 is required for influenza virus
            infection.
REFERENCE   5  (residues 1 to 1008)
  AUTHORS   Kan,Y., Paung,Y., Seeliger,M.A. and Miller,W.T.
  TITLE     Domain Architecture of the Nonreceptor Tyrosine Kinase Ack1
  JOURNAL   Cells 12 (6), 900 (2023)
   PUBMED   36980241
  REMARK    GeneRIF: Domain Architecture of the Nonreceptor Tyrosine Kinase
            Ack1.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1008)
  AUTHORS   Kato,J., Kaziro,Y. and Satoh,T.
  TITLE     Activation of the guanine nucleotide exchange factor Dbl following
            ACK1-dependent tyrosine phosphorylation
  JOURNAL   Biochem Biophys Res Commun 268 (1), 141-147 (2000)
   PUBMED   10652228
REFERENCE   7  (residues 1 to 1008)
  AUTHORS   Eisenmann,K.M., McCarthy,J.B., Simpson,M.A., Keely,P.J., Guan,J.L.,
            Tachibana,K., Lim,L., Manser,E., Furcht,L.T. and Iida,J.
  TITLE     Melanoma chondroitin sulphate proteoglycan regulates cell spreading
            through Cdc42, Ack-1 and p130cas
  JOURNAL   Nat Cell Biol 1 (8), 507-513 (1999)
   PUBMED   10587647
REFERENCE   8  (residues 1 to 1008)
  AUTHORS   Mott,H.R., Owen,D., Nietlispach,D., Lowe,P.N., Manser,E., Lim,L.
            and Laue,E.D.
  TITLE     Structure of the small G protein Cdc42 bound to the GTPase-binding
            domain of ACK
  JOURNAL   Nature 399 (6734), 384-388 (1999)
   PUBMED   10360579
REFERENCE   9  (residues 1 to 1008)
  AUTHORS   Satoh,T., Kato,J., Nishida,K. and Kaziro,Y.
  TITLE     Tyrosine phosphorylation of ACK in response to temperature
            shift-down, hyperosmotic shock, and epidermal growth factor
            stimulation
  JOURNAL   FEBS Lett 386 (2-3), 230-234 (1996)
   PUBMED   8647288
REFERENCE   10 (residues 1 to 1008)
  AUTHORS   Manser,E., Leung,T., Salihuddin,H., Tan,L. and Lim,L.
  TITLE     A non-receptor tyrosine kinase that inhibits the GTPase activity of
            p21cdc42
  JOURNAL   Nature 363 (6427), 364-367 (1993)
   PUBMED   8497321
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124944.8.
            
            Summary: This gene encodes a tyrosine kinase that binds Cdc42Hs in
            its GTP-bound form and inhibits both the intrinsic and
            GTPase-activating protein (GAP)-stimulated GTPase activity of
            Cdc42Hs. This binding is mediated by a unique sequence of 47 amino
            acids C-terminal to an SH3 domain. The protein may be involved in a
            regulatory mechanism that sustains the GTP-bound active form of
            Cdc42Hs and which is directly linked to a tyrosine phosphorylation
            signal transduction pathway. Several alternatively spliced
            transcript variants have been identified from this gene, but the
            full-length nature of only two transcript variants has been
            determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.879463.1,
                                           SRR18074969.3514972.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..1008
                     /product="activated CDC42 kinase 1 isoform 13"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="activated p21cdc42Hs kinase; activated
                     Cdc42-associated kinase 1; tyrosine kinase non-receptor
                     protein 2"
                     /calculated_mol_wt=111139
     Region          6..67
                     /region_name="SAM_TNK-like"
                     /note="SAM domain of TNK(ACK)-like non-receptor
                     tyrosine-protein kinases; cd09539"
                     /db_xref="CDD:188938"
     Region          130..387
                     /region_name="PTKc_Ack_like"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Activated Cdc42-associated kinase; cd05040"
                     /db_xref="CDD:270636"
     Site            order(132..134,140,156,158,205..208,212,252,256..257,259,
                     270,289..293,302,336)
                     /site_type="active"
                     /db_xref="CDD:270636"
     Site            order(132..134,140,156,158,205..208,212,252,256..257,259,
                     270)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270636"
     Site            order(252,256,289..293,302,336)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270636"
     Site            order(269..279,281..295)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270636"
     Region          395..444
                     /region_name="SH3_9"
                     /note="Variant SH3 domain; pfam14604"
                     /db_xref="CDD:434066"
     Site            order(397,399,404,422,424,439,441..442)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212754"
     Region          449..514
                     /region_name="GTPase_binding"
                     /note="GTPase binding; pfam09027"
                     /db_xref="CDD:430374"
     Region          <543..849
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          774..840
                     /region_name="Inhibitor_Mig-6"
                     /note="EGFR receptor inhibitor Mig-6; pfam11555"
                     /db_xref="CDD:463294"
     Region          959..998
                     /region_name="UBA_TNK1"
                     /note="UBA domain found in non-receptor tyrosine-protein
                     kinase TNK1 and similar proteins; cd14328"
                     /db_xref="CDD:270513"
     CDS             1..1008
                     /gene="TNK2"
                     /gene_synonym="ACK; ACK-1; ACK1; p21cdc42Hs"
                     /coded_by="NM_001387719.1:67..3093"
                     /note="isoform 13 is encoded by transcript variant 22"
                     /db_xref="CCDS:CCDS93440.1"
                     /db_xref="GeneID:10188"
                     /db_xref="HGNC:HGNC:19297"
                     /db_xref="MIM:606994"
ORIGIN      
        1 mqpeegtgwl lellsevqlq qyflrlrddl nvtrlshfey vknedlekig mgrpgqrrlw
       61 eavkrrkalc krkswmskvf sgkrleaefp phhsqstfrk tspapggpag egplqsltcl
      121 igekdlrlle klgdgsfgvv rrgewdapsg ktvsvavkcl kpdvlsqpea mddfirevna
      181 mhsldhrnli rlygvvltpp mkmvtelapl gslldrlrkh qghfllgtls ryavqvaegm
      241 gyleskrfih rdlaarnlll atrdlvkigd fglmralpqn ddhyvmqehr kvpfawcape
      301 slktrtfsha sdtwmfgvtl wemftygqep wiglngsqil hkidkegerl prpedcpqdi
      361 ynvmvqcwah kpedrptfva lrdflleaqp tdmralqdfe epdklhiqmn dvitviegra
      421 enywwrgqnt rtlcvgpfpr nvvtsvagls aqdisqplqn sfihtghgds dprhcwgfpd
      481 ridelylgnp mdppdllsve lstsrppqhl ggvkkptydp vsedqdplss dfkrlglrkp
      541 glprglwlak psarvpgtka srgsgaevtl idfgeepvvp alrpcapsla qlamdacsll
      601 detppqsptr alprplhptp vvdwdarplp pppayddvaq deddfeicsi nstlvgagvp
      661 agpsqgqtny afvpeqarpp pplednlflp pqgggkppss aqtaeifqal qqecmrqlqa
      721 pagspapsps pggddkpqvp prvpipprpt rphvqlspap pgeeetsqwp gpaspprvpp
      781 replspqgsr tpsplvppgs splpprlsss pgktmpttqs fasdpkyatp qviqapgpra
      841 gpcilpivrd gkkvssthyy llperpsyle ryqrflreaq speeptplpv plllpppstp
      901 apaaptatvr pmpqaaldpk anfstnnsnp garpppprat arlpqrgcpg dgpeagrpad
      961 kiqmveqlfg lglrprgech kvlemfdwnl eqagchllgs wgpahhkr
//
LOCUS       NP_001180538             398 aa            linear   PRI 21-NOV-2025
DEFINITION  tubulin delta chain isoform 2 [Homo sapiens].
ACCESSION   NP_001180538
VERSION     NP_001180538.1
DBSOURCE    REFSEQ: accession NM_001193609.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Pudlowski,R., Xu,L., Milenkovic,L., Kumar,C., Hemsworth,K.,
            Aqrabawi,Z., Stearns,T. and Wang,J.T.
  TITLE     A delta-tubulin/epsilon-tubulin/Ted protein complex is required for
            centriole architecture
  JOURNAL   Elife 13, 98704 (2025)
   PUBMED   40067174
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Wang,J.T., Kong,D., Hoerner,C.R., Loncarek,J. and Stearns,T.
  TITLE     Centriole triplet microtubules are required for stable centriole
            formation and inheritance in human cells
  JOURNAL   Elife 6, e29061 (2017)
   PUBMED   28906251
  REMARK    GeneRIF: Here, the authors report that centrioles in delta-tubulin
            and epsilon-tubulin null mutant human cells lack triplet
            microtubules and fail to undergo centriole maturation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Jostins,L., Ripke,S., Weersma,R.K., Duerr,R.H., McGovern,D.P.,
            Hui,K.Y., Lee,J.C., Schumm,L.P., Sharma,Y., Anderson,C.A.,
            Essers,J., Mitrovic,M., Ning,K., Cleynen,I., Theatre,E.,
            Spain,S.L., Raychaudhuri,S., Goyette,P., Wei,Z., Abraham,C.,
            Achkar,J.P., Ahmad,T., Amininejad,L., Ananthakrishnan,A.N.,
            Andersen,V., Andrews,J.M., Baidoo,L., Balschun,T., Bampton,P.A.,
            Bitton,A., Boucher,G., Brand,S., Buning,C., Cohain,A., Cichon,S.,
            D'Amato,M., De Jong,D., Devaney,K.L., Dubinsky,M., Edwards,C.,
            Ellinghaus,D., Ferguson,L.R., Franchimont,D., Fransen,K.,
            Gearry,R., Georges,M., Gieger,C., Glas,J., Haritunians,T., Hart,A.,
            Hawkey,C., Hedl,M., Hu,X., Karlsen,T.H., Kupcinskas,L.,
            Kugathasan,S., Latiano,A., Laukens,D., Lawrance,I.C., Lees,C.W.,
            Louis,E., Mahy,G., Mansfield,J., Morgan,A.R., Mowat,C., Newman,W.,
            Palmieri,O., Ponsioen,C.Y., Potocnik,U., Prescott,N.J.,
            Regueiro,M., Rotter,J.I., Russell,R.K., Sanderson,J.D., Sans,M.,
            Satsangi,J., Schreiber,S., Simms,L.A., Sventoraityte,J.,
            Targan,S.R., Taylor,K.D., Tremelling,M., Verspaget,H.W., De Vos,M.,
            Wijmenga,C., Wilson,D.C., Winkelmann,J., Xavier,R.J., Zeissig,S.,
            Zhang,B., Zhang,C.K., Zhao,H., Silverberg,M.S., Annese,V.,
            Hakonarson,H., Brant,S.R., Radford-Smith,G., Mathew,C.G.,
            Rioux,J.D., Schadt,E.E., Daly,M.J., Franke,A., Parkes,M.,
            Vermeire,S., Barrett,J.C. and Cho,J.H.
  CONSRTM   International IBD Genetics Consortium (IIBDGC)
  TITLE     Host-microbe interactions have shaped the genetic architecture of
            inflammatory bowel disease
  JOURNAL   Nature 491 (7422), 119-124 (2012)
   PUBMED   23128233
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Kato,A., Nagata,Y. and Todokoro,K.
  TITLE     Delta-tubulin is a component of intercellular bridges and both the
            early and mature perinuclear rings during spermatogenesis
  JOURNAL   Dev Biol 269 (1), 196-205 (2004)
   PUBMED   15081367
REFERENCE   8  (residues 1 to 398)
  AUTHORS   Sidjanin,D.J., Zangerl,B., Johnson,J.L., Xue,F., Mellersh,C.,
            Ostrander,E.A., Acland,G. and Aguirre,G.D.
  TITLE     Cloning of the canine delta tubulin cDNA (TUBD) and mapping to CFA9
  JOURNAL   Anim Genet 33 (2), 161-162 (2002)
   PUBMED   12047234
REFERENCE   9  (residues 1 to 398)
  AUTHORS   Smrzka,O.W., Delgehyr,N. and Bornens,M.
  TITLE     Tissue-specific expression and subcellular localisation of
            mammalian delta-tubulin
  JOURNAL   Curr Biol 10 (7), 413-416 (2000)
   PUBMED   10753753
REFERENCE   10 (residues 1 to 398)
  AUTHORS   Chang,P. and Stearns,T.
  TITLE     Delta-tubulin and epsilon-tubulin: two new human centrosomal
            tubulins reveal new aspects of centrosome structure and function
  JOURNAL   Nat Cell Biol 2 (1), 30-35 (2000)
   PUBMED   10620804
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG682935.1, BC000258.1, AK024741.1 and BX119803.1.
            
            Transcript Variant: This variant (2) lacks an alternate, in-frame,
            segment, compared to variant 1. The resulting protein (isoform 2)
            is shorter when it is compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4141261.1, BC000258.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.1"
     Protein         1..398
                     /product="tubulin delta chain isoform 2"
                     /note="delta-tubulin; tubulin delta chain"
                     /calculated_mol_wt=44527
     Region          2..397
                     /region_name="delta_zeta_tubulin-like"
                     /note="The delta- and zeta-tubulin families; cd02189"
                     /db_xref="CDD:276958"
     Site            order(9..11,14..15,67..69,72,100..102,141..147,172,
                     174..175,182..183,206,210,224,227..228,231)
                     /site_type="other"
                     /note="putative nucleotide binding site [chemical
                     binding]"
                     /db_xref="CDD:276958"
     CDS             1..398
                     /gene="TUBD1"
                     /gene_synonym="TUBD"
                     /coded_by="NM_001193609.2:287..1483"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54153.1"
                     /db_xref="GeneID:51174"
                     /db_xref="HGNC:HGNC:16811"
                     /db_xref="MIM:607344"
ORIGIN      
        1 msivtvqlgq cgnqigfevf dallsdshss qglcsmrene ayqasckerf fseeengvpi
       61 aravlvdmep kvinqmlska aqsgqwkygq hacfcqkqgs gnnwaygysv hgprheesim
      121 niirkevekc dsfsgffiim smaggtgsgl gafvtqnled qysnslkmnq iiwpygtgev
      181 ivqnynsilt lshlyrssda lllhendaih kicaklmnik qisfsdinqv lahqlgsvfq
      241 ptysaessfh yrrnplgidr hvwpplsglp plskmslnkd lhfntsianl vilrgkdvqs
      301 advegfkdpa lytswlkpvn afnvwktqra fskyeksavl vsnsqflvkp ldmivgkawn
      361 mfaskayihq ytkfgieeed fldsftsleq vvasycnl
//
LOCUS       NP_001334994             446 aa            linear   PRI 21-NOV-2025
DEFINITION  dynactin subunit 2 isoform 4 [Homo sapiens].
ACCESSION   NP_001334994
VERSION     NP_001334994.1
DBSOURCE    REFSEQ: accession NM_001348065.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Xu,S., Xing,J., Li,K., Qiao,L., Zhang,C., Ren,Y. and Liu,Y.
  TITLE     Pan-cancer analysis of DCTN2 and its tumour-promoting role in HCC
            by modulating the AKT pathway
  JOURNAL   J Cell Mol Med 28 (11), e18450 (2024)
   PUBMED   38842133
  REMARK    GeneRIF: Pan-cancer analysis of DCTN2 and its tumour-promoting role
            in HCC by modulating the AKT pathway.
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Li,Y.F., Shi,L.J., Wang,P., Wang,J.W., Shi,G.Y. and Lee,S.C.
  TITLE     Binding between ROCK1 and DCTN2 triggers diabetes-associated
            centrosome amplification in colon cancer cells
  JOURNAL   Oncol Rep 46 (1) (2021)
   PUBMED   34080666
  REMARK    GeneRIF: Binding between ROCK1 and DCTN2 triggers
            diabetesassociated centrosome amplification in colon cancer cells.
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Eckley,D.M., Gill,S.R., Melkonian,K.A., Bingham,J.B., Goodson,H.V.,
            Heuser,J.E. and Schroer,T.A.
  TITLE     Analysis of dynactin subcomplexes reveals a novel actin-related
            protein associated with the arp1 minifilament pointed end
  JOURNAL   J Cell Biol 147 (2), 307-320 (1999)
   PUBMED   10525537
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Berrueta,L., Tirnauer,J.S., Schuyler,S.C., Pellman,D. and
            Bierer,B.E.
  TITLE     The APC-associated protein EB1 associates with components of the
            dynactin complex and cytoplasmic dynein intermediate chain
  JOURNAL   Curr Biol 9 (8), 425-428 (1999)
   PUBMED   10226031
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Starr,D.A., Williams,B.C., Hays,T.S. and Goldberg,M.L.
  TITLE     ZW10 helps recruit dynactin and dynein to the kinetochore
  JOURNAL   J Cell Biol 142 (3), 763-774 (1998)
   PUBMED   9700164
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Echeverri,C.J., Paschal,B.M., Vaughan,K.T. and Vallee,R.B.
  TITLE     Molecular characterization of the 50-kD subunit of dynactin reveals
            function for the complex in chromosome alignment and spindle
            organization during mitosis
  JOURNAL   J Cell Biol 132 (4), 617-633 (1996)
   PUBMED   8647893
REFERENCE   10 (residues 1 to 446)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022506.38.
            
            Summary: This gene encodes a 50-kD subunit of dynactin, a
            macromolecular complex consisting of 10-11 subunits ranging in size
            from 22 to 150 kD. Dynactin binds to both microtubules and
            cytoplasmic dynein. It is involved in a diverse array of cellular
            functions, including ER-to-Golgi transport, the centripetal
            movement of lysosomes and endosomes, spindle formation, chromosome
            movement, nuclear positioning, and axonogenesis. This subunit is
            present in 4-5 copies per dynactin molecule. It contains three
            short alpha-helical coiled-coil domains that may mediate
            association with self or other dynactin subunits. It may interact
            directly with the largest subunit (p150) of dynactin and may affix
            p150 in place. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been found for this gene. [provided
            by RefSeq, May 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..446
                     /product="dynactin subunit 2 isoform 4"
                     /note="p50 dynamitin; dynactin complex 50 kDa subunit;
                     epididymis secretory protein Li 77; 50 kDa
                     dynein-associated polypeptide; dynactin 2 (p50);
                     epididymis secretory sperm binding protein"
                     /calculated_mol_wt=49250
     Region          59..444
                     /region_name="Dynamitin"
                     /note="pfam04912"
                     /db_xref="CDD:461477"
     CDS             1..446
                     /gene="DCTN2"
                     /gene_synonym="DCTN50; DYNAMITIN; HEL-S-77; RBP50"
                     /coded_by="NM_001348065.2:200..1540"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:10540"
                     /db_xref="HGNC:HGNC:2712"
                     /db_xref="MIM:607376"
ORIGIN      
        1 mafilprkrf chlaepscar wgalslrepm pspsphshdn pgvylpfvlp clllkarnep
       61 dvyetsdlpe ddqaefdael eeltstsveh iivnpnaayd kfkdkrvgtk gldfsdrigk
      121 tkrtgyesge yemlgeglgv ketpqqkyqr llhevqeltt evekikttvk esateekltp
      181 vllakqlaal kqqlvashle kllgpdaain ltdpdgalak rlllqleatk nskggsggkt
      241 tgtppdsslv tyelhsrpeq dkfsqaakva elekrltele tavrcdqdaq nplsaglqga
      301 clmetvellq akvsaldlav ldqvearlqs vlgkvneiak hkasvedadt qskvhqlyet
      361 iqrwspiast lpelvqrlvt ikqlheqamq fgqllthldt tqqmianslk dnttlltqvq
      421 ttmrenlatv egnfasider mkklgk
//
LOCUS       NP_001230903             521 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2B catalytic subunit gamma
            isoform isoform 1 [Homo sapiens].
ACCESSION   NP_001230903
VERSION     NP_001230903.1
DBSOURCE    REFSEQ: accession NM_001243974.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Li,D. and Hu,A.
  TITLE     LINC-PINT suppresses breast cancer cell proliferation and migration
            via MEIS2/PPP3CC/NF-kappaB pathway by sponging miR-576-5p
  JOURNAL   Am J Med Sci 367 (3), 201-211 (2024)
   PUBMED   37660994
  REMARK    GeneRIF: LINC-PINT suppresses breast cancer cell proliferation and
            migration via MEIS2/PPP3CC/NF-kappaB pathway by sponging
            miR-576-5p.
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Anastasiadou,E., Messina,E., Sanavia,T., Labruna,V., Ceccarelli,S.,
            Megiorni,F., Gerini,G., Pontecorvi,P., Camero,S., Perniola,G.,
            Venneri,M.A., Trivedi,P., Lenzi,A. and Marchese,C.
  TITLE     Calcineurin Gamma Catalytic Subunit PPP3CC Inhibition by
            miR-200c-3p Affects Apoptosis in Epithelial Ovarian Cancer
  JOURNAL   Genes (Basel) 12 (9), 1400 (2021)
   PUBMED   34573382
  REMARK    GeneRIF: Calcineurin Gamma Catalytic Subunit PPP3CC Inhibition by
            miR-200c-3p Affects Apoptosis in Epithelial Ovarian Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Miyata,H., Oura,S., Morohoshi,A., Shimada,K., Mashiko,D., Oyama,Y.,
            Kaneda,Y., Matsumura,T., Abbasi,F. and Ikawa,M.
  TITLE     SPATA33 localizes calcineurin to the mitochondria and regulates
            sperm motility in mice
  JOURNAL   Proc Natl Acad Sci U S A 118 (35) (2021)
   PUBMED   34446558
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Yang,S.A. and Klee,C.B.
  TITLE     Low affinity Ca2+-binding sites of calcineurin B mediate
            conformational changes in calcineurin A
  JOURNAL   Biochemistry 39 (51), 16147-16154 (2000)
   PUBMED   11123943
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Wang,H.G., Pathan,N., Ethell,I.M., Krajewski,S., Yamaguchi,Y.,
            Shibasaki,F., McKeon,F., Bobo,T., Franke,T.F. and Reed,J.C.
  TITLE     Ca2+-induced apoptosis through calcineurin dephosphorylation of BAD
  JOURNAL   Science 284 (5412), 339-343 (1999)
   PUBMED   10195903
REFERENCE   8  (residues 1 to 521)
  AUTHORS   Loh,C., Shaw,K.T., Carew,J., Viola,J.P., Luo,C., Perrino,B.A. and
            Rao,A.
  TITLE     Calcineurin binds the transcription factor NFAT1 and reversibly
            regulates its activity
  JOURNAL   J Biol Chem 271 (18), 10884-10891 (1996)
   PUBMED   8631904
REFERENCE   9  (residues 1 to 521)
  AUTHORS   Muramatsu,T. and Kincaid,R.L.
  TITLE     Molecular cloning and chromosomal mapping of the human gene for the
            testis-specific catalytic subunit of calmodulin-dependent protein
            phosphatase (calcineurin A)
  JOURNAL   Biochem Biophys Res Commun 188 (1), 265-271 (1992)
   PUBMED   1339277
REFERENCE   10 (residues 1 to 521)
  AUTHORS   King,M.M., Huang,C.Y., Chock,P.B., Nairn,A.C., Hemmings,H.C. Jr.,
            Chan,K.F. and Greengard,P.
  TITLE     Mammalian brain phosphoproteins as substrates for calcineurin
  JOURNAL   J Biol Chem 259 (13), 8080-8083 (1984)
   PUBMED   6330098
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK055013.1, AK299415.1,
            AC037459.16 and AY007249.1.
            
            Summary: Calcineurin is a calcium-dependent, calmodulin-stimulated
            protein phosphatase involved in the downstream regulation of
            dopaminergic signal transduction. Calcineurin is composed of a
            regulatory subunit and a catalytic subunit. The protein encoded by
            this gene represents one of the regulatory subunits that has been
            found for calcineurin. Three transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK299415.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151741, SAMEA2154361
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..521
                     /product="serine/threonine-protein phosphatase 2B
                     catalytic subunit gamma isoform isoform 1"
                     /EC_number="3.1.3.16"
                     /note="CAM-PRP catalytic subunit; calcineurin,
                     testis-specific catalytic subunit; protein phosphatase 3,
                     catalytic subunit, gamma isozyme"
                     /calculated_mol_wt=59131
     Region          37..341
                     /region_name="MPP_PP2B"
                     /note="PP2B, metallophosphatase domain; cd07416"
                     /db_xref="CDD:277361"
     Site            order(49,51,86,88,114,146,155,195,277,310,337)
                     /site_type="other"
                     /note="CN-CyPA-CsA complex [polypeptide binding]"
                     /db_xref="CDD:277361"
     Region          52..343
                     /region_name="Catalytic. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P48454.3)"
     Site            order(86,88,114,118,146..147,195,228,250,277,279)
                     /site_type="active"
                     /db_xref="CDD:277361"
     Site            order(86,88,114,146,195,277)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277361"
     Region          303..307
                     /region_name="SAPNY motif.
                     /evidence=ECO:0000250|UniProtKB:Q08209"
                     /note="propagated from UniProtKB/Swiss-Prot (P48454.3)"
     Region          344..366
                     /region_name="Calcineurin B binding.
                     /evidence=ECO:0000250|UniProtKB:P16298"
                     /note="propagated from UniProtKB/Swiss-Prot (P48454.3)"
     Region          395..409
                     /region_name="Calmodulin-binding.
                     /evidence=ECO:0000250|UniProtKB:P16298"
                     /note="propagated from UniProtKB/Swiss-Prot (P48454.3)"
     Region          410..417
                     /region_name="Autoinhibitory segment.
                     /evidence=ECO:0000250|UniProtKB:P16298"
                     /note="propagated from UniProtKB/Swiss-Prot (P48454.3)"
     Region          468..490
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000250|UniProtKB:P16298"
                     /note="propagated from UniProtKB/Swiss-Prot (P48454.3)"
     Region          480..521
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48454.3)"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P48454.3)"
     CDS             1..521
                     /gene="PPP3CC"
                     /gene_synonym="CALNA3; CNA3; PP2Bgamma"
                     /coded_by="NM_001243974.2:333..1898"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS59093.1"
                     /db_xref="GeneID:5533"
                     /db_xref="HGNC:HGNC:9316"
                     /db_xref="MIM:114107"
ORIGIN      
        1 msgrrfhlst tdrvikavpf pptqrltfke vfengkpkvd vlknhlvkeg rleeevalki
       61 indgaailrq ektmievdap itvcgdihgq ffdlmklfev ggspsntryl flgdyvdrgy
      121 fsiecvlylw slkinhpktl fllrgnhecr hltdyftfkq ecrikyseqv ydacmetfdc
      181 lplaallnqq flcvhggmsp eitslddirk ldrfteppaf gpvcdllwsd psedygnekt
      241 lehythntvr gcsyfysypa vceflqnnnl lsiiraheaq dagyrmyrks qatgfpslit
      301 ifsapnyldv ynnkaavlky ennvmnirqf ncsphpywlp nfmdvftwsl pfvgekvtem
      361 lvnvlnicsd delisddeae dhyipsyqkg sttvrkeiir nkiraigkma rvfsilrqes
      421 esvltlkglt ptgtlplgvl sggkqtieta tveavearea irgfslqhki rsfeeargld
      481 rinermpprk dsihaggpmk svtsahshaa hrsdqgkkah s
//
LOCUS       NP_001230159             664 aa            linear   PRI 21-NOV-2025
DEFINITION  transcription factor 4 isoform f [Homo sapiens].
ACCESSION   NP_001230159
VERSION     NP_001230159.1
DBSOURCE    REFSEQ: accession NM_001243230.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 664)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 664)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 664)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 664)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 664)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 664)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK122765.1, FR748216.1 and
            AC091103.4.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (6) differs in the 5' UTR and
            coding sequence and uses an alternate in-frame splice site at the
            3' end of an exon compared to variant 3. The resulting isoform (f,
            also known as TCF4-E-) has a shorter and distinct N-terminus and
            lacks an alternate internal segment compared to isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments. Sequence
            Note: This gene is distinct from TCF7L2 (alias TCF-4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FR748216.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..664
                     /product="transcription factor 4 isoform f"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=71096
     Region          555..639
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(563,567,569..571,573,578,599..600)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(576..577,580..581,583..584,587,591,601,604,608,611,
                     614..619)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..664
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001243230.2:83..2077"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS59321.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mqraktelfr lqivtddlrk nemfsppvss gkngptslas ghftgsnved rsssgswgng
       61 ghpspsrnyg dgtpydhmts rdlgshdnls ppfvnsriqs ktergsyssy gresnlqgch
      121 qqsllggdmd mgnpgtlspt kpgsqyyqys snnprrrplh ssamevqtkk vrkvppglps
      181 svyapsasta dynrdspgyp sskpatstfp ssffmqdghh ssdpwssssg mnqpgyagml
      241 gnsshipqss sycslhpher lsypshssad insslppmst fhrsgtnhys tssctppang
      301 tdsimanrgs gaagssqtgd algkalasiy spdhtnnsfs snpstpvgsp pslsgtavws
      361 rnggqasssp nyegplhslq sriedrlerl ddaihvlrnh avgpstampg ghgdmhgiig
      421 pshngamggl gsgygtglls anrhslmvgt hredgvalrg shsllpnqvp vpqlpvqsat
      481 spdlnppqdp yrgmppglqg qsvssgssei ksddegdenl qdtkssedkk ldddkkdiks
      541 itsnnddedl tpeqkaerek errmannare rlrvrdinea fkelgrmvql hlksdkpqtk
      601 llilhqavav ilsleqqvre rnlnpkaacl krreeekvss eppplslagp hpgmgdasnh
      661 mgqm
//
LOCUS       NP_001295126             198 aa            linear   PRI 21-NOV-2025
DEFINITION  translocon-associated protein subunit gamma isoform 1 [Homo
            sapiens].
ACCESSION   NP_001295126 XP_011511401
VERSION     NP_001295126.1
DBSOURCE    REFSEQ: accession NM_001308197.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Hu,Q., Wu,G., Ma,H., Zhang,J. and Yang,Z.
  TITLE     Signal sequence receptor subunit 3: A novel indicator of
            immunosuppressive tumor microenvironment and clinical benefits from
            immunotherapy
  JOURNAL   Cell Signal 111, 110871 (2023)
   PUBMED   37652395
  REMARK    GeneRIF: Signal sequence receptor subunit 3: A novel indicator of
            immunosuppressive tumor microenvironment and clinical benefits from
            immunotherapy.
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Gemmer,M., Chaillet,M.L., van Loenhout,J., Cuevas Arenas,R.,
            Vismpas,D., Grollers-Mulderij,M., Koh,F.A., Albanese,P.,
            Scheltema,R.A., Howes,S.C., Kotecha,A., Fedry,J. and Forster,F.
  TITLE     Visualization of translation and protein biogenesis at the ER
            membrane
  JOURNAL   Nature 614 (7946), 160-167 (2023)
   PUBMED   36697828
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Dmello,C., Sonabend,A., Arrieta,V.A., Zhang,D.Y., Kanojia,D.,
            Chen,L., Gould,A., Zhang,J., Kang,S.J., Winter,J., Horbinski,C.,
            Amidei,C., Gyorffy,B., Cordero,A., Chang,C.L., Castro,B., Hsu,P.,
            Ahmed,A.U., Lesniak,M.S., Stupp,R. and Sonabend,A.M.
  TITLE     Translocon-associated Protein Subunit SSR3 Determines and Predicts
            Susceptibility to Paclitaxel in Breast Cancer and Glioblastoma
  JOURNAL   Clin Cancer Res 28 (14), 3156-3169 (2022)
   PUBMED   35552677
  REMARK    GeneRIF: Translocon-associated Protein Subunit SSR3 Determines and
            Predicts Susceptibility to Paclitaxel in Breast Cancer and
            Glioblastoma.
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Xu,X., Huang,Y., Li,X., Arvan,P. and Liu,M.
  TITLE     The Role of TRAPgamma/SSR3 in Preproinsulin Translocation Into the
            Endoplasmic Reticulum
  JOURNAL   Diabetes 71 (3), 440-452 (2022)
   PUBMED   34857543
  REMARK    GeneRIF: The Role of TRAPgamma/SSR3 in Preproinsulin Translocation
            Into the Endoplasmic Reticulum.
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Dittner-Moormann,S., Lourenco,C.M., Reunert,J., Nishinakamura,R.,
            Tanaka,S.S., Werner,C., Debus,V., Zimmer,K.P., Wetzel,G.,
            Naim,H.Y., Wada,Y., Rust,S. and Marquardt,T.
  TITLE     TRAPgamma-CDG shows asymmetric glycosylation and an effect on
            processing of proteins required in higher organisms
  JOURNAL   J Med Genet 58 (3), 213-216 (2021)
   PUBMED   32332102
  REMARK    GeneRIF: TRAPgamma-CDG shows asymmetric glycosylation and an effect
            on processing of proteins required in higher organisms.
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Ng,B.G., Lourenco,C.M., Losfeld,M.E., Buckingham,K.J., Kircher,M.,
            Nickerson,D.A., Shendure,J., Bamshad,M.J. and Freeze,H.H.
  CONSRTM   University of Washington Center for Mendelian Genomics
  TITLE     Mutations in the translocon-associated protein complex subunit SSR3
            cause a novel congenital disorder of glycosylation
  JOURNAL   J Inherit Metab Dis 42 (5), 993-997 (2019)
   PUBMED   30945312
  REMARK    GeneRIF: Mutations in the translocon-associated protein complex
            subunit SSR3 cause a novel congenital disorder of glycosylation.
REFERENCE   7  (residues 1 to 198)
  AUTHORS   Huang,S., Zhong,W., Shi,Z., Wang,K., Jin,H., Zhang,Z., Wang,H.,
            Wei,Y., Chen,S., Zhou,Q. and He,X.
  TITLE     Overexpression of signal sequence receptor gamma predicts poor
            survival in patients with hepatocellular carcinoma
  JOURNAL   Hum Pathol 81, 47-54 (2018)
   PUBMED   29940286
  REMARK    GeneRIF: SSR3 acts as an oncogene in hepatocellular carcinoma with
            overexpression predicting poor survival.
REFERENCE   8  (residues 1 to 198)
  AUTHORS   Pfeffer,S., Dudek,J., Schaffer,M., Ng,B.G., Albert,S.,
            Plitzko,J.M., Baumeister,W., Zimmermann,R., Freeze,H.H., Engel,B.D.
            and Forster,F.
  TITLE     Dissecting the molecular organization of the translocon-associated
            protein complex
  JOURNAL   Nat Commun 8, 14516 (2017)
   PUBMED   28218252
  REMARK    GeneRIF: Data suggest that the mutation leads to complete absence
            of TRAP gamma (SSR3).
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 198)
  AUTHORS   Chen,H.Z., Wen,Q., Wang,W.J., He,J.P. and Wu,Q.
  TITLE     The orphan nuclear receptor TR3/Nur77 regulates ER stress and
            induces apoptosis via interaction with TRAPgamma
  JOURNAL   Int J Biochem Cell Biol 45 (8), 1600-1609 (2013)
   PUBMED   23660295
  REMARK    GeneRIF: translocon-associated protein subunit gamma (TRAPgamma)
            was identified as a novel TR3 binding partner.
REFERENCE   10 (residues 1 to 198)
  AUTHORS   Hartmann,E., Gorlich,D., Kostka,S., Otto,A., Kraft,R., Knespel,S.,
            Burger,E., Rapoport,T.A. and Prehn,S.
  TITLE     A tetrameric complex of membrane proteins in the endoplasmic
            reticulum
  JOURNAL   Eur J Biochem 214 (2), 375-381 (1993)
   PUBMED   7916687
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY035536.1, AK304364.1,
            AC092927.5 and AI225105.1.
            
            On Apr 28, 2015 this sequence version replaced XP_011511401.1.
            
            Summary: The signal sequence receptor (SSR) is a glycosylated
            endoplasmic reticulum (ER) membrane receptor associated with
            protein translocation across the ER membrane. The SSR is comprised
            of four membrane proteins/subunits: alpha, beta, gamma, and delta.
            The first two are glycosylated subunits and the latter two are
            non-glycosylated subunits. This gene encodes the gamma subunit,
            which is predicted to span the membrane four times. [provided by
            RefSeq, Aug 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14243140.10739317.1,
                                           SRR6380202.143674.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.31"
     Protein         1..198
                     /product="translocon-associated protein subunit gamma
                     isoform 1"
                     /note="translocon-associated protein gamma subunit;
                     TRAP-gamma; SSR gamma; translocon-associated protein
                     subunit gamma; TRAP-complex gamma subunit; signal sequence
                     receptor subunit gamma; signal sequence receptor, gamma
                     (translocon-associated protein gamma)"
                     /calculated_mol_wt=22479
     Region          12..196
                     /region_name="TRAP-gamma"
                     /note="Translocon-associated protein, gamma subunit
                     (TRAP-gamma); pfam07074"
                     /db_xref="CDD:399809"
     CDS             1..198
                     /gene="SSR3"
                     /gene_synonym="TRAPG"
                     /coded_by="NM_001308197.2:29..625"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS77846.1"
                     /db_xref="GeneID:6747"
                     /db_xref="HGNC:HGNC:11325"
                     /db_xref="MIM:606213"
ORIGIN      
        1 mapkgsskqq seedlllqdf srnlsakssa lffgnafivs aipiwlywri whmdliqsav
       61 lysvmtlvst ylvafayknv kfvlkhkvaq kredavskev trklseadnr kmsrkekder
      121 fdsclkyghh krgilwkkne vadyeattfs ifynntlflv vvivasffil knfnptvnyi
      181 lsisassgli allstgsk
//
LOCUS       NP_001035197            1453 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA mismatch repair protein Mlh3 isoform 1 [Homo sapiens].
ACCESSION   NP_001035197
VERSION     NP_001035197.1
DBSOURCE    REFSEQ: accession NM_001040108.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1453)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1453)
  AUTHORS   Khailany,R.A. and Ozaslan,M.
  TITLE     Exonic sequencing and MLH3 gene expression analysis of breast
            cancer patients
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 67 (3), 35-43 (2021)
   PUBMED   34933735
  REMARK    GeneRIF: Exonic sequencing and MLH3 gene expression analysis of
            breast cancer patients.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1453)
  AUTHORS   Nawaz,S., Ullah,M.I., Hamid,B.S., Nargis,J., Nawaz,M., Hussain,S.
            and Ahmad,W.
  TITLE     A loss-of-function variant in DNA mismatch repair gene MLH3
            underlies severe oligozoospermia
  JOURNAL   J Hum Genet 66 (7), 725-730 (2021)
   PUBMED   33517345
  REMARK    GeneRIF: A loss-of-function variant in DNA mismatch repair gene
            MLH3 underlies severe oligozoospermia.
REFERENCE   4  (residues 1 to 1453)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1453)
  AUTHORS   Rahman,M.M., Mohiuddin,M., Shamima Keka,I., Yamada,K., Tsuda,M.,
            Sasanuma,H., Andreani,J., Guerois,R., Borde,V., Charbonnier,J.B.
            and Takeda,S.
  TITLE     Genetic evidence for the involvement of mismatch repair proteins,
            PMS2 and MLH3, in a late step of homologous recombination
  JOURNAL   J Biol Chem 295 (51), 17460-17475 (2020)
   PUBMED   33453991
  REMARK    GeneRIF: Genetic evidence for the involvement of mismatch repair
            proteins, PMS2 and MLH3, in a late step of homologous
            recombination.
REFERENCE   6  (residues 1 to 1453)
  AUTHORS   Lipkin,S.M., Wang,V., Stoler,D.L., Anderson,G.R., Kirsch,I.,
            Hadley,D., Lynch,H.T. and Collins,F.S.
  TITLE     Germline and somatic mutation analyses in the DNA mismatch repair
            gene MLH3: Evidence for somatic mutation in colorectal cancers
  JOURNAL   Hum Mutat 17 (5), 389-396 (2001)
   PUBMED   11317354
REFERENCE   7  (residues 1 to 1453)
  AUTHORS   Kondo,E., Horii,A. and Fukushige,S.
  TITLE     The interacting domains of three MutL heterodimers in man: hMLH1
            interacts with 36 homologous amino acid residues within hMLH3,
            hPMS1 and hPMS2
  JOURNAL   Nucleic Acids Res 29 (8), 1695-1702 (2001)
   PUBMED   11292842
REFERENCE   8  (residues 1 to 1453)
  AUTHORS   Lipkin,S.M., Wang,V., Jacoby,R., Banerjee-Basu,S., Baxevanis,A.D.,
            Lynch,H.T., Elliott,R.M. and Collins,F.S.
  TITLE     MLH3: a DNA mismatch repair gene associated with mammalian
            microsatellite instability
  JOURNAL   Nat Genet 24 (1), 27-35 (2000)
   PUBMED   10615123
REFERENCE   9  (residues 1 to 1453)
  AUTHORS   Sherrington,R., Rogaev,E.I., Liang,Y., Rogaeva,E.A., Levesque,G.,
            Ikeda,M., Chi,H., Lin,C., Li,G., Holman,K., Tsuda,T., Mar,L.,
            Foncin,J.F., Bruni,A.C., Montesi,M.P., Sorbi,S., Rainero,I.,
            Pinessi,L., Nee,L., Chumakov,I., Pollen,D., Brookes,A., Sanseau,P.,
            Polinsky,R.J., Wasco,W., Da Silva,H.A., Haines,J.L.,
            Perkicak-Vance,M.A., Tanzi,R.E., Roses,A.D., Fraser,P.E.,
            Rommens,J.M. and St George-Hyslop,P.H.
  TITLE     Cloning of a gene bearing missense mutations in early-onset
            familial Alzheimer's disease
  JOURNAL   Nature 375 (6534), 754-760 (1995)
   PUBMED   7596406
REFERENCE   10 (residues 1 to 1453)
  AUTHORS   Idos,G. and Valle,L.
  TITLE     Lynch Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301390
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA805814.1, AB039667.1,
            AL049780.4 and BX090851.1.
            
            Summary: This gene is a member of the MutL-homolog (MLH) family of
            DNA mismatch repair (MMR) genes. MLH genes are implicated in
            maintaining genomic integrity during DNA replication and after
            meiotic recombination. The protein encoded by this gene functions
            as a heterodimer with other family members. Somatic mutations in
            this gene frequently occur in tumors exhibiting microsatellite
            instability, and germline mutations have been linked to hereditary
            nonpolyposis colorectal cancer type 7 (HNPCC7). Several
            alternatively spliced transcript variants have been identified, but
            the full-length nature of only two transcript variants has been
            determined. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2612854.1,
                                           SRR14038192.3759035.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355774.7/ ENSP00000348020.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1453
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..1453
                     /product="DNA mismatch repair protein Mlh3 isoform 1"
                     /note="DNA mismatch repair protein MLH3"
                     /calculated_mol_wt=163581
     Region          9..192
                     /region_name="HATPase_MutL-MLH-PMS-like"
                     /note="Histidine kinase-like ATPase domain of DNA mismatch
                     repair proteins Escherichia coli MutL, human MutL homologs
                     (MLH/ PMS), and related domains; cd16926"
                     /db_xref="CDD:340403"
     Site            order(28,32..33,35..36,54,56,58,60..61,69,74..77,94..97,
                     109,111,143..144,146)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:340403"
     Site            order(70,97)
                     /site_type="other"
                     /note="ATP-lid"
                     /db_xref="CDD:340403"
     Region          206..349
                     /region_name="MutL_Trans_MLH3"
                     /note="transducer domain, having a ribosomal S5 domain
                     2-like fold, found in proteins similar to yeast and human
                     MLH3 (MutL homologue 3). MLH3 belongs to the DNA mismatch
                     repair (MutL/MLH1/PMS2) family. This transducer domain is
                     homologous to the second domain...; cd03486"
                     /db_xref="CDD:239568"
     Site            325
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:239568"
     Region          624..650
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHC1.3)"
     Region          933..960
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHC1.3)"
     Region          <1194..1409
                     /region_name="MutL"
                     /note="DNA mismatch repair ATPase MutL [Replication,
                     recombination and repair]; COG0323"
                     /db_xref="CDD:440092"
     CDS             1..1453
                     /gene="MLH3"
                     /gene_synonym="HNPCC7"
                     /coded_by="NM_001040108.2:152..4513"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32123.1"
                     /db_xref="GeneID:27030"
                     /db_xref="HGNC:HGNC:7128"
                     /db_xref="MIM:604395"
ORIGIN      
        1 mikclsvevq aklrsglais slgqcveela lnsidaeakc vavrvnmetf qvqvidngfg
       61 mgsddvekvg nryftskchs vqdlenprfy gfrgealani admasaveis skknrtmktf
      121 vklfqsgkal kaceadvtra sagttvtvyn lfyqlpvrrk cmdprlefek vrqriealsl
      181 mhpsisfslr ndvsgsmvlq lpktkdvcsr fcqiyglgks qklreisfky kefelsgyis
      241 seahynknmq flfvnkrlvl rtklhklidf llrkesiick pkngptsrqm nsslrhrstp
      301 elygiyvinv qcqfceydvc mepaktlief qnwdtllfci qegvkmflkq eklfvelsge
      361 dikefsedng fslfdatlqk rvtsdersnf qeacnnilds yemfnlqska vkrkttaenv
      421 ntqssrdsea trkntndafl yiyesggpgh skmtepslqn kdsscseskm leqetivase
      481 agenekhkks flehsslenp cgtslemfls pfqtpchfee sgqdleiwke sttvngmaan
      541 ilknnriqnq pkrfkdatev gcqplpfatt lwgvhsaqte kekkkessnc grrnvfsygr
      601 vklcstgfit hvvqnektks tetehsfkny vrpgptraqe tfgnrtrhsv etpdikdlas
      661 tlskesgqlp nkkncrtnis ygleneptat ytmfsafqeg skksqtdcil sdtspsfpwy
      721 rhvsndsrkt dkligfskpi vrkklslssq lgslekfkrq ygkvenpldt eveesngvtt
      781 nlslqvepdi llkdknrlen sdvckittme hsdsdsscqp ashilnsekf pfskdedcle
      841 qqmpslresp mtlkelslfn rkpldlekss eslasklsrl kgseretqtm gmmsrfnelp
      901 nsdssrkdsk lcsvltqdfc mlfnnkhekt engviptsds atqdnsfnkn skthsnsntt
      961 encvisetpl vlpynnskvt gkdsdvlira seqqigslds psgmlmnpve datgdqngic
     1021 fqseeskara cseteesntc csdwqrhfdv algrmvyvnk mtglstfiap tediqaactk
     1081 dlttvavdvv lengsqyrcq pfrsdlvlpf lpraraertv mrqdnrdtvd dtvsseslqs
     1141 lfsewdnpvf arypevavdv ssgqaeslav kihnilypyr ftkgmihsmq vlqqvdnkfi
     1201 aclmstktee ngeaggnllv lvdqhaaher irleqliids yekqqaqgsg rkkllsstli
     1261 ppleitvtee qrrllwcyhk nledlglefv fpdtsdslvl vgkvplcfve reanelrrgr
     1321 stvtksivee fireqlellq ttggiqgtlp ltvqkvlasq achgaikfnd glslqescrl
     1381 iealsscqlp fqcahgrpsm lpladidhle qekqikpnlt klrkmaqawr lfgkaecdtr
     1441 qslqqsmppc epp
//
LOCUS       NP_001269046             413 aa            linear   PRI 21-NOV-2025
DEFINITION  transcription factor RFX3 isoform c [Homo sapiens].
ACCESSION   NP_001269046
VERSION     NP_001269046.1
DBSOURCE    REFSEQ: accession NM_001282117.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Qian,Y., Cheng,B., Luo,J., Hu,Y., Gao,L. and Cheng,H.
  TITLE     CircRFX3 Up-regulates Its Host Gene RFX3 to Facilitate
            Tumorigenesis and Progression of Glioma
  JOURNAL   J Mol Neurosci 72 (6), 1195-1207 (2022)
   PUBMED   35416616
  REMARK    GeneRIF: CircRFX3 Up-regulates Its Host Gene RFX3 to Facilitate
            Tumorigenesis and Progression of Glioma.
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 413)
  AUTHORS   Nakayama,A., Murakami,H., Maeyama,N., Yamashiro,N., Sakakibara,A.,
            Mori,N. and Takahashi,M.
  TITLE     Role for RFX transcription factors in non-neuronal cell-specific
            inactivation of the microtubule-associated protein MAP1A promoter
  JOURNAL   J Biol Chem 278 (1), 233-240 (2003)
   PUBMED   12411430
  REMARK    GeneRIF: Data show that two regulatory factor for X box (RFX1 and
            3) binding sites in exon1 of both the mouse and human
            microtubule-associated protein (MAP1A) gene are important for
            effective transcriptional repression in non-neuronal cells.
REFERENCE   7  (residues 1 to 413)
  AUTHORS   Morotomi-Yano,K., Yano,K., Saito,H., Sun,Z., Iwama,A. and Miki,Y.
  TITLE     Human regulatory factor X 4 (RFX4) is a testis-specific dimeric
            DNA-binding protein that cooperates with other human RFX members
  JOURNAL   J Biol Chem 277 (1), 836-842 (2002)
   PUBMED   11682486
REFERENCE   8  (residues 1 to 413)
  AUTHORS   Iwama,A., Pan,J., Zhang,P., Reith,W., Mach,B., Tenen,D.G. and
            Sun,Z.
  TITLE     Dimeric RFX proteins contribute to the activity and lineage
            specificity of the interleukin-5 receptor alpha promoter through
            activation and repression domains
  JOURNAL   Mol Cell Biol 19 (6), 3940-3950 (1999)
   PUBMED   10330134
REFERENCE   9  (residues 1 to 413)
  AUTHORS   Emery,P., Durand,B., Mach,B. and Reith,W.
  TITLE     RFX proteins, a novel family of DNA binding proteins conserved in
            the eukaryotic kingdom
  JOURNAL   Nucleic Acids Res 24 (5), 803-807 (1996)
   PUBMED   8600444
REFERENCE   10 (residues 1 to 413)
  AUTHORS   Reith,W., Ucla,C., Barras,E., Gaud,A., Durand,B.,
            Herrero-Sanchez,C., Kobr,M. and Mach,B.
  TITLE     RFX1, a transactivator of hepatitis B virus enhancer I, belongs to
            a novel family of homodimeric and heterodimeric DNA-binding
            proteins
  JOURNAL   Mol Cell Biol 14 (2), 1230-1244 (1994)
   PUBMED   8289803
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL365202.19, AL354941.10 and
            AL133549.11.
            
            Summary: This gene is a member of the regulatory factor X gene
            family, which encodes transcription factors that contain a
            highly-conserved winged helix DNA binding domain. The protein
            encoded by this gene is structurally related to regulatory factors
            X1, X2, X4, and X5. It is a transcriptional activator that can bind
            DNA as a monomer or as a heterodimer with other RFX family members.
            Multiple transcript variants encoding different isoforms have been
            described for this gene. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC067778.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.2"
     Protein         1..413
                     /product="transcription factor RFX3 isoform c"
                     /note="DNA binding protein RFX3; transcription factor
                     RFX3; regulatory factor X, 3 (influences HLA class II
                     expression)"
                     /calculated_mol_wt=45584
     Region          <51..138
                     /region_name="RFX1_trans_act"
                     /note="RFX1 transcription activation region; pfam04589"
                     /db_xref="CDD:461362"
     Region          184..258
                     /region_name="RFX_DNA_binding"
                     /note="RFX DNA-binding domain; pfam02257"
                     /db_xref="CDD:460512"
     CDS             1..413
                     /gene="RFX3"
                     /coded_by="NM_001282117.2:195..1436"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS75809.1"
                     /db_xref="GeneID:5991"
                     /db_xref="HGNC:HGNC:9984"
                     /db_xref="MIM:601337"
ORIGIN      
        1 mqtsetgsdt gstvtlqtsv asqaavptqv vqqvpvqqqv qqvqtvqqvq hvypaqvqyv
       61 egsdtvytng airtttypyt etqmysqntg gnyfdtqgss aqvttvvssh smvgtggiqm
      121 gvtggqliss sggtyligns mensghsvth ttraspatie maietlqksd glsthrssll
      181 nshlqwlldn yetaegvslp rstlynhylr hcqehkldpv naasfgklir sifmglrtrr
      241 lgtrgnskyh yygirvkpds plnrlqedmq ymamrqqpmq qkqrykpmqk vdgvadgftg
      301 sgqqtgtsve qtviaqsqhh qqfldasral pefgeveiss lpdgttfedi kslqslyreh
      361 ceaildvvvn lqfslieklw qtfwryspst ptdgttites rsestsfpih fhg
//
LOCUS       NP_001333277             480 aa            linear   PRI 21-NOV-2025
DEFINITION  autophagy-related protein 13 isoform f [Homo sapiens].
ACCESSION   NP_001333277 XP_016874101
VERSION     NP_001333277.1
DBSOURCE    REFSEQ: accession NM_001346348.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Patel,A. and Faesen,A.C.
  TITLE     Metamorphosis by ATG13 and ATG101 in human autophagy initiation
  JOURNAL   Autophagy 20 (4), 968-969 (2024)
   PUBMED   37394799
  REMARK    GeneRIF: Metamorphosis by ATG13 and ATG101 in human autophagy
            initiation.
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Nguyen,A. and Faesen,A.C.
  TITLE     The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis
  JOURNAL   FEBS Lett 598 (1), 114-126 (2024)
   PUBMED   37567770
  REMARK    GeneRIF: The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis.
            Review article
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Karabi,Z., Moradian,F. and Kheirabadi,M.
  TITLE     The effect of lactoferrin on ULK1 and ATG13 genes expression in
            breast cancer cell line MCF7 and bioinformatics studies of protein
            interaction between lactoferrin and the autophagy initiation
            complex
  JOURNAL   Cell Biochem Biophys 80 (4), 795-806 (2022)
   PUBMED   36169801
  REMARK    GeneRIF: The effect of lactoferrin on ULK1 and ATG13 genes
            expression in breast cancer cell line MCF7 and bioinformatics
            studies of protein interaction between lactoferrin and the
            autophagy initiation complex.
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Gottschalk,G., Peterson,D., Knox,K., Maynard,M., Whelan,R.J. and
            Roy,A.
  TITLE     Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE)
  JOURNAL   Mol Cell Neurosci 120, 103731 (2022)
   PUBMED   35487443
  REMARK    GeneRIF: Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE).
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Jung,C.H., Jun,C.B., Ro,S.H., Kim,Y.M., Otto,N.M., Cao,J., Kundu,M.
            and Kim,D.H.
  TITLE     ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy
            machinery
  JOURNAL   Mol Biol Cell 20 (7), 1992-2003 (2009)
   PUBMED   19225151
  REMARK    GeneRIF: The ULK-Atg13-FIP200 complexes are direct targets of mTOR
            and important regulators of autophagy in response to mTOR
            signaling.
REFERENCE   7  (residues 1 to 480)
  AUTHORS   Hosokawa,N., Hara,T., Kaizuka,T., Kishi,C., Takamura,A., Miura,Y.,
            Iemura,S., Natsume,T., Takehana,K., Yamada,N., Guan,J.L., Oshiro,N.
            and Mizushima,N.
  TITLE     Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200
            complex required for autophagy
  JOURNAL   Mol Biol Cell 20 (7), 1981-1991 (2009)
   PUBMED   19211835
  REMARK    GeneRIF: mTORC1 suppresses autophagy through direct regulation of
            the approximately 3-MDa ULK1-Atg13-FIP200 complex.
REFERENCE   8  (residues 1 to 480)
  AUTHORS   Chan,E.Y., Longatti,A., McKnight,N.C. and Tooze,S.A.
  TITLE     Kinase-inactivated ULK proteins inhibit autophagy via their
            conserved C-terminal domains using an Atg13-independent mechanism
  JOURNAL   Mol Cell Biol 29 (1), 157-171 (2009)
   PUBMED   18936157
  REMARK    GeneRIF: The functions of ULK1 and ULK2 are controlled by
            autophosphorylation and conformational changes involving exposure
            of the C-terminal domain and interaction with the putative human
            homologue of Atg13.
            GeneRIF: The gene product is the functional homologue of yeast
            Atg13, and required for autophagy in mammalian cells.
REFERENCE   9  (residues 1 to 480)
  AUTHORS   Meijer,W.H., van der Klei,I.J., Veenhuis,M. and Kiel,J.A.
  TITLE     ATG genes involved in non-selective autophagy are conserved from
            yeast to man, but the selective Cvt and pexophagy pathways also
            require organism-specific genes
  JOURNAL   Autophagy 3 (2), 106-116 (2007)
   PUBMED   17204848
REFERENCE   10 (residues 1 to 480)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC127035.6 and AC115088.6.
            
            On Oct 9, 2016 this sequence version replaced XP_016874101.1.
            
            Summary: The protein encoded by this gene is an autophagy factor
            and a target of the TOR kinase signaling pathway. The encoded
            protein is essential for autophagosome formation and mitophagy.
            [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (39), as well as variants 2, 5,
            36-38, and 40-45, encodes isoform f.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.1543229.1,
                                           SRR11853563.5301.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..480
                     /product="autophagy-related protein 13 isoform f"
                     /note="autophagy-related protein 13; ATG13 autophagy
                     related 13 homolog"
                     /calculated_mol_wt=52692
     Region          19..192
                     /region_name="ATG13"
                     /note="Autophagy-related protein 13; pfam10033"
                     /db_xref="CDD:431003"
     CDS             1..480
                     /gene="ATG13"
                     /gene_synonym="KIAA0652; PARATARG8"
                     /coded_by="NM_001346348.2:662..2104"
                     /note="isoform f is encoded by transcript variant 39"
                     /db_xref="CCDS:CCDS7921.1"
                     /db_xref="GeneID:9776"
                     /db_xref="HGNC:HGNC:29091"
                     /db_xref="MIM:615088"
ORIGIN      
        1 metdlnsqdr kdldkfikff alktvqvivq arlgekictr ssssptgsdw fnlaikdipe
       61 vtheakkala gqlpavgrsm cveislktse gdsmeleiwc lemnekcdke ikvsytvynr
      121 lslllkslla itrvtpayrl srkqgheyvi lyriyfgevq lsglgegfqt vrvgtvgtpv
      181 gtitlscayr inlafmstrq fertppimgi iidhfvdrpy pssspmhpcn yrtagedtgv
      241 iypsvedsqe vcttsfstsp psqlmvpgke ggvplapnqp vhgtqadqer latctpsdrt
      301 hcaatpssse dtetvsnsse grasphdvle tifvrkvgaf vnkpinqvtl tsldipfamf
      361 apknleledt dpmvnppdsp etesplqgsl hsdgssggss gnthddfvmi dfkpafskdd
      421 ilpmdlgtfy refqnppqls slsidigaqs maedldslpe klavheknvr efdafvetlq
//
LOCUS       NP_001265657             237 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-binding protein RFXANK isoform b [Homo sapiens].
ACCESSION   NP_001265657
VERSION     NP_001265657.1
DBSOURCE    REFSEQ: accession NM_001278728.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Mousavi Khorshidi,M.S., Seeleuthner,Y., Chavoshzadeh,Z., Behfar,M.,
            Hamidieh,A.A., Alimadadi,H., Sherkat,R., Momen,T., Behniafard,N.,
            Eskandarzadeh,S., Mansouri,M., Behnam,M., Mahdavi,M., Heydarazad
            Zadeh,M., Shokri,M., Alizadeh,F., Movahedi,M., Momenilandi,M.,
            Keramatipour,M., Casanova,J.L., Cobat,A., Abel,L., Shahrooei,M. and
            Parvaneh,N.
  TITLE     Clinical, Immunological, and Genetic Findings in Iranian Patients
            with MHC-II Deficiency: Confirmation of c.162delG RFXANK Founder
            Mutation in the Iranian Population
  JOURNAL   J Clin Immunol 43 (8), 1941-1952 (2023)
   PUBMED   37584719
  REMARK    GeneRIF: Clinical, Immunological, and Genetic Findings in Iranian
            Patients with MHC-II Deficiency: Confirmation of c.162delG RFXANK
            Founder Mutation in the Iranian Population.
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Gao,J. and Xu,C.
  TITLE     Structural basis for the recognition of RFX7 by ANKRA2 and RFXANK
  JOURNAL   Biochem Biophys Res Commun 523 (1), 263-266 (2020)
   PUBMED   31864703
  REMARK    GeneRIF: Structural basis for the recognition of RFX7 by ANKRA2 and
            RFXANK.
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Abolnezhadian,F., Saeedi-Boroujeni,A. and Iranparast,S.
  TITLE     MHC Class II Deficiency with Normal CD4+ T Cell Counts: A Case
            Report
  JOURNAL   Iran J Allergy Asthma Immunol 17 (6), 594-600 (2018)
   PUBMED   30644704
  REMARK    GeneRIF: this study reports an 8 month-old girl with MHC class II
            deficiency with a novel homozygous mutation in RFXANK gene and
            normal CD4+ T cell counts, diagnosed by whole exome sequencing and
            negative HLA-DR proteins on peripheral blood mononuclear cell in
            flow cytometry
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 237)
  AUTHORS   Nagarajan,U.M., Peijnenburg,A., Gobin,S.J., Boss,J.M. and van den
            elsen,P.J.
  TITLE     Novel mutations within the RFX-B gene and partial rescue of MHC and
            related genes through exogenous class II transactivator in
            RFX-B-deficient cells
  JOURNAL   J Immunol 164 (7), 3666-3674 (2000)
   PUBMED   10725724
REFERENCE   7  (residues 1 to 237)
  AUTHORS   Wiszniewski,W., Fondaneche,M.C., Lambert,N., Masternak,K.,
            Picard,C., Notarangelo,L., Schwartz,K., Bal,J., Reith,W.,
            Alcaide,C., de Saint Basile,G., Fischer,A. and
            Lisowska-Grospierre,B.
  TITLE     Founder effect for a 26-bp deletion in the RFXANK gene in North
            African major histocompatibility complex class II-deficient
            patients belonging to complementation group B
  JOURNAL   Immunogenetics 51 (4-5), 261-267 (2000)
   PUBMED   10803838
REFERENCE   8  (residues 1 to 237)
  AUTHORS   Lin,J.H., Makris,A., McMahon,C., Bear,S.E., Patriotis,C.,
            Prasad,V.R., Brent,R., Golemis,E.A. and Tsichlis,P.N.
  TITLE     The ankyrin repeat-containing adaptor protein Tvl-1 is a novel
            substrate and regulator of Raf-1
  JOURNAL   J Biol Chem 274 (21), 14706-14715 (1999)
   PUBMED   10329666
REFERENCE   9  (residues 1 to 237)
  AUTHORS   Nagarajan,U.M., Louis-Plence,P., DeSandro,A., Nilsen,R., Bushey,A.
            and Boss,J.M.
  TITLE     RFX-B is the gene responsible for the most common cause of the bare
            lymphocyte syndrome, an MHC class II immunodeficiency
  JOURNAL   Immunity 10 (2), 153-162 (1999)
   PUBMED   10072068
  REMARK    Erratum:[Immunity 1999 Mar;10(3):399]
REFERENCE   10 (residues 1 to 237)
  AUTHORS   Masternak,K., Barras,E., Zufferey,M., Conrad,B., Corthals,G.,
            Aebersold,R., Sanchez,J.C., Hochstrasser,D.F., Mach,B. and Reith,W.
  TITLE     A gene encoding a novel RFX-associated transactivator is mutated in
            the majority of MHC class II deficiency patients
  JOURNAL   Nat Genet 20 (3), 273-277 (1998)
   PUBMED   9806546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG740813.1, AF105428.1 and
            AW411190.1.
            
            Summary: Major histocompatibility (MHC) class II molecules are
            transmembrane proteins that have a central role in development and
            control of the immune system. The protein encoded by this gene,
            along with regulatory factor X-associated protein and regulatory
            factor-5, forms a complex that binds to the X box motif of certain
            MHC class II gene promoters and activates their transcription. Once
            bound to the promoter, this complex associates with the
            non-DNA-binding factor MHC class II transactivator, which controls
            the cell type specificity and inducibility of MHC class II gene
            expression. This protein contains ankyrin repeats involved in
            protein-protein interactions. Mutations in this gene have been
            linked to bare lymphocyte syndrome type II, complementation group
            B. Multiple alternatively spliced transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Jul 2013].
            
            Transcript Variant: This variant (4) differs in the 5' UTR, and has
            an alternate splice site and lacks an in-frame exon in the coding
            region, as compared to variant 1. The resulting isoform (b) lacks
            an internal single aa and an internal segment, as compared to
            isoform a. Variants 2 and 4 encode the same isoform c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF105428.1, BG740813.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..237
                     /product="DNA-binding protein RFXANK isoform b"
                     /note="ankyrin repeat-containing regulatory factor
                     X-associated protein; regulatory factor X subunit B;
                     RFX-Bdelta4; DNA-binding protein RFXANK; ankyrin repeat
                     family A protein 1"
                     /calculated_mol_wt=25449
     Region          <94..226
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(100,102,106..107,110..112,114..115,119,122,131,133,
                     135,139..140,143..145,147..148,152,155,164,166,168,
                     172..173,176..178,180..181,185,188)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          100..131
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          133..164
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          166..194
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..237
                     /gene="RFXANK"
                     /gene_synonym="ANKRA1; BLS; F14150_1; MHC2D2; RFX-B"
                     /coded_by="NM_001278728.2:175..888"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS12396.1"
                     /db_xref="GeneID:8625"
                     /db_xref="HGNC:HGNC:9987"
                     /db_xref="MIM:603200"
ORIGIN      
        1 meltqpaedl iqtqqtpase lgdpedpgee aadgsdtvvl slfpctpepv npepdasvss
       61 pqgsslkhst tltnrqrgne vsalpatldc dnlvnkpder gftpliwasa fgeietvrfl
      121 lewgadphil akeresalsl astggytdiv glllerdvdi niydwnggtp llyavrgnhv
      181 kcveallarg adltteadsg ytpmdlaval gyrkvqqvie nhilklfqsn lvpadpe
//
LOCUS       NP_055066                675 aa            linear   PRI 21-NOV-2025
DEFINITION  electrogenic aspartate/glutamate antiporter SLC25A13, mitochondrial
            isoform 2 [Homo sapiens].
ACCESSION   NP_055066
VERSION     NP_055066.1
DBSOURCE    REFSEQ: accession NM_014251.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 675)
  AUTHORS   Lin,J., Lin,W., Lin,Y., Peng,W. and Zheng,Z.
  TITLE     Clinical and genetic analysis of 26 Chinese patients with neonatal
            intrahepatic cholestasis due to citrin deficiency
  JOURNAL   Clin Chim Acta 552, 117617 (2024)
   PUBMED   37890575
  REMARK    GeneRIF: Clinical and genetic analysis of 26 Chinese patients with
            neonatal intrahepatic cholestasis due to citrin deficiency.
REFERENCE   3  (residues 1 to 675)
  AUTHORS   Jiang,M., Peng,M., Lu,Z., Shao,Y., Liu,Z., Li,X., Lin,Y., Liu,L.,
            Zhang,W. and Cai,Y.
  TITLE     Features of liver injury in 138 Chinese patients with NICCD
  JOURNAL   J Pediatr Endocrinol Metab 36 (12), 1154-1160 (2023)
   PUBMED   37939726
  REMARK    GeneRIF: Features of liver injury in 138 Chinese patients with
            NICCD.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 675)
  AUTHORS   Broeks,M.H., Meijer,N.W.F., Westland,D., Bosma,M., Gerrits,J.,
            German,H.M., Ciapaite,J., van Karnebeek,C.D.M., Wanders,R.J.A.,
            Zwartkruis,F.J.T., Verhoeven-Duif,N.M. and Jans,J.J.M.
  TITLE     The malate-aspartate shuttle is important for de novo serine
            biosynthesis
  JOURNAL   Cell Rep 42 (9), 113043 (2023)
   PUBMED   37647199
REFERENCE   5  (residues 1 to 675)
  AUTHORS   Yasuda,T., Yamaguchi,N., Kobayashi,K., Nishi,I., Horinouchi,H.,
            Jalil,M.A., Li,M.X., Ushikai,M., Iijima,M., Kondo,I. and Saheki,T.
  TITLE     Identification of two novel mutations in the SLC25A13 gene and
            detection of seven mutations in 102 patients with adult-onset type
            II citrullinemia
  JOURNAL   Hum Genet 107 (6), 537-545 (2000)
   PUBMED   11153906
  REMARK    GeneRIF: Observational study of genotype prevalence. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 675)
  AUTHORS   Del Arco,A., Agudo,M. and Satrustegui,J.
  TITLE     Characterization of a second member of the subfamily of
            calcium-binding mitochondrial carriers expressed in human
            non-excitable tissues
  JOURNAL   Biochem J 345 Pt 3 (Pt 3), 725-732 (2000)
   PUBMED   10642534
REFERENCE   7  (residues 1 to 675)
  AUTHORS   Sinasac,D.S., Crackower,M.A., Lee,J.R., Kobayashi,K., Saheki,T.,
            Scherer,S.W. and Tsui,L.C.
  TITLE     Genomic structure of the adult-onset type II citrullinemia gene,
            SLC25A13, and cloning and expression of its mouse homologue
  JOURNAL   Genomics 62 (2), 289-292 (1999)
   PUBMED   10610724
REFERENCE   8  (residues 1 to 675)
  AUTHORS   Kobayashi,K., Sinasac,D.S., Iijima,M., Boright,A.P., Begum,L.,
            Lee,J.R., Yasuda,T., Ikeda,S., Hirano,R., Terazono,H.,
            Crackower,M.A., Kondo,I., Tsui,L.C., Scherer,S.W. and Saheki,T.
  TITLE     The gene mutated in adult-onset type II citrullinaemia encodes a
            putative mitochondrial carrier protein
  JOURNAL   Nat Genet 22 (2), 159-163 (1999)
   PUBMED   10369257
REFERENCE   9  (residues 1 to 675)
  AUTHORS   Simpson,K.L., MacLeod,E.L., Kakajiwala,A., Gropman,A.L. and Ah
            Mew,N.
  TITLE     Urea Cycle Disorders Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301396
REFERENCE   10 (residues 1 to 675)
  AUTHORS   Song,Y.Z., Oishi,K. and Saheki,T.
  TITLE     Citrin Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA118296.1, AC004458.1 and
            BC006566.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the mitochondrial carrier family.
            The encoded protein contains four EF-hand Ca(2+) binding motifs in
            the N-terminal domain, and localizes to mitochondria. The protein
            catalyzes the exchange of aspartate for glutamate and a proton
            across the inner mitochondrial membrane, and is stimulated by
            calcium on the external side of the inner mitochondrial membrane.
            Mutations in this gene result in citrullinemia, type II. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, May 2009].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the central coding region, compared to variant 1.
            The resulting isoform (2) lacks one-aa, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF118838.1, BC006566.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000265631.10/
                                                  ENSP00000265631.6
            RefSeq Select criteria             :: based on manual assertion,
                                                  conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.3"
     Protein         1..675
                     /product="electrogenic aspartate/glutamate antiporter
                     SLC25A13, mitochondrial isoform 2"
                     /note="calcium-binding mitochondrial carrier protein
                     Aralar2; mitochondrial aspartate glutamate carrier 2;
                     solute carrier family 25 (aspartate/glutamate carrier),
                     member 13; citrullinemia type II; ARALAR-related gene 2;
                     electrogenic aspartate/glutamate antiporter SLC25A13,
                     mitochondrial"
                     /calculated_mol_wt=74045
     Region          2..295
                     /region_name="Regulatory N-terminal domain.
                     /evidence=ECO:0000303|PubMed:25410934"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJS0.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q9UJS0.2)"
     Region          16..81
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     Region          <56..183
                     /region_name="EFh_PEF"
                     /note="The penta-EF hand (PEF) family; cl25352"
                     /db_xref="CDD:355382"
     Region          57..83
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320060"
     Site            order(66,68,70,77,100,102,104,111)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320060"
     Region          84..126
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320060"
     Region          133..159
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320060"
     Region          296..311
                     /region_name="Linker loop domain.
                     /evidence=ECO:0000250|UniProtKB:O75746"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJS0.2)"
     Region          321..612
                     /region_name="Carrier domain.
                     /evidence=ECO:0000303|PubMed:25410934"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJS0.2)"
     Region          329..422
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Site            332..349
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJS0.2)"
     Site            353
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXX4; propagated from
                     UniProtKB/Swiss-Prot (Q9UJS0.2)"
     Site            372
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXX4; propagated from
                     UniProtKB/Swiss-Prot (Q9UJS0.2)"
     Site            393..412
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJS0.2)"
     Region          424..511
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Site            436..449
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJS0.2)"
     Site            453
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9UJS0.2)"
     Site            484
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9QXX4; propagated from
                     UniProtKB/Swiss-Prot (Q9UJS0.2)"
     Site            485..504
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJS0.2)"
     Region          516..611
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Site            524..541
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJS0.2)"
     Site            581..600
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJS0.2)"
     Region          613..675
                     /region_name="C-terminal domain.
                     /evidence=ECO:0000303|PubMed:25410934"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJS0.2)"
     Site            662
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXX4; propagated from
                     UniProtKB/Swiss-Prot (Q9UJS0.2)"
     Site            666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UJS0.2)"
     CDS             1..675
                     /gene="SLC25A13"
                     /gene_synonym="ARALAR2; CITRIN; CTLN2; NICCD"
                     /coded_by="NM_014251.3:143..2170"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS5645.1"
                     /db_xref="GeneID:10165"
                     /db_xref="HGNC:HGNC:10983"
                     /db_xref="MIM:603859"
ORIGIN      
        1 maaakvaltk radpaelrti flkyasiekn geffmspndf vtrylnifge sqpnpktvel
       61 lsgvvdqtkd glisfqefva fesvlcapda lfmvafqlfd kagkgevtfe dvkqvfgqtt
      121 ihqhipfnwd sefvqlhfgk erkrhltyae ftqflleiql ehakqafvqr dnartgrvta
      181 idfrdimvti rphvltpfve eclvaaaggt tshqvsfsyf ngfnsllnnm elirkiystl
      241 agtrkdvevt keefvlaaqk fgqvtpmevd ilfqladlye prgrmtladi eriapleegt
      301 lpfnlaeaqr qkasgdsarp vllqvaesay rfglgsvaga vgatavypid lvktrmqnqr
      361 stgsfvgelm yknsfdcfkk vlryegffgl yrgllpqllg vapekaiklt vndfvrdkfm
      421 hkdgsvplaa eilaggcagg sqviftnple ivkirlqvag eittgprvsa lsvvrdlgff
      481 giykgakacf lrdipfsaiy fpcyahvkas fanedgqvsp gslllagaia gmpaaslvtp
      541 adviktrlqv aaragqttys gvidcfrkil reegpkalwk gagarvfrss pqfgvtllty
      601 ellqrwfyid fggvkpmgse pvpksrinlp apnpdhvggy klavatfagi enkfglylpl
      661 fkpsvstska igggp
//
LOCUS       NP_001374195             361 aa            linear   PRI 21-NOV-2025
DEFINITION  5-cytosine rRNA methyltransferase NSUN4 isoform d [Homo sapiens].
ACCESSION   NP_001374195
VERSION     NP_001374195.1
DBSOURCE    REFSEQ: accession NM_001387266.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Zhao,Z., Zhou,Y., Lv,P., Zhou,T., Liu,H., Xie,Y., Wu,Z., Wang,X.,
            Zhao,H., Zheng,J. and Jiang,X.
  TITLE     NSUN4 mediated RNA 5-methylcytosine promotes the malignant
            progression of glioma through improving the CDC42 mRNA
            stabilization
  JOURNAL   Cancer Lett 597, 217059 (2024)
   PUBMED   38876383
  REMARK    GeneRIF: NSUN4 mediated RNA 5-methylcytosine promotes the malignant
            progression of glioma through improving the CDC42 mRNA
            stabilization.
            Erratum:[Cancer Lett. 2025 Feb 1;610:217351. doi:
            10.1016/j.canlet.2024.217351. PMID: 39616022]
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Kim,S., Tan,S., Ku,J., Widowati,T.A., Ku,D., Lee,K., You,K. and
            Kim,Y.
  TITLE     RNA 5-methylcytosine marks mitochondrial double-stranded RNAs for
            degradation and cytosolic release
  JOURNAL   Mol Cell 84 (15), 2935-2948 (2024)
   PUBMED   39019044
  REMARK    Erratum:[Mol Cell. 2025 Feb 20;85(4):857. doi:
            10.1016/j.molcel.2025.01.029. PMID: 39909040]
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Nguyen,T.G., Ritter,C. and Kummer,E.
  TITLE     Structural insights into the role of GTPBP10 in the RNA maturation
            of the mitoribosome
  JOURNAL   Nat Commun 14 (1), 7991 (2023)
   PUBMED   38042949
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Cui,M., Qu,F., Wang,L., Liu,X., Yu,J., Tang,Z. and Cheng,D.
  TITLE     m5C RNA methyltransferase-related gene NSUN4 stimulates malignant
            progression of hepatocellular carcinoma and can be a prognostic
            marker
  JOURNAL   Cancer Biomark 33 (3), 389-400 (2022)
   PUBMED   34744073
  REMARK    GeneRIF: m5C RNA methyltransferase-related gene NSUN4 stimulates
            malignant progression of hepatocellular carcinoma and can be a
            prognostic marker.
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 361)
  AUTHORS   Yakubovskaya,E., Guja,K.E., Mejia,E., Castano,S., Hambardjieva,E.,
            Choi,W.S. and Garcia-Diaz,M.
  TITLE     Structure of the essential MTERF4:NSUN4 protein complex reveals how
            an MTERF protein collaborates to facilitate rRNA modification
  JOURNAL   Structure 20 (11), 1940-1947 (2012)
   PUBMED   23022348
REFERENCE   7  (residues 1 to 361)
  AUTHORS   Spahr,H., Habermann,B., Gustafsson,C.M., Larsson,N.G. and
            Hallberg,B.M.
  TITLE     Structure of the human MTERF4-NSUN4 protein complex that regulates
            mitochondrial ribosome biogenesis
  JOURNAL   Proc Natl Acad Sci U S A 109 (38), 15253-15258 (2012)
   PUBMED   22949673
  REMARK    GeneRIF: analysis of the 3D crystal structure of the human
            MTERF4-NSUN4 complex
REFERENCE   8  (residues 1 to 361)
  AUTHORS   Camara,Y., Asin-Cayuela,J., Park,C.B., Metodiev,M.D., Shi,Y.,
            Ruzzenente,B., Kukat,C., Habermann,B., Wibom,R., Hultenby,K.,
            Franz,T., Erdjument-Bromage,H., Tempst,P., Hallberg,B.M.,
            Gustafsson,C.M. and Larsson,N.G.
  TITLE     MTERF4 regulates translation by targeting the methyltransferase
            NSUN4 to the mammalian mitochondrial ribosome
  JOURNAL   Cell Metab 13 (5), 527-539 (2011)
   PUBMED   21531335
REFERENCE   9  (residues 1 to 361)
  AUTHORS   Gratacos,M., Costas,J., de Cid,R., Bayes,M., Gonzalez,J.R.,
            Baca-Garcia,E., de Diego,Y., Fernandez-Aranda,F.,
            Fernandez-Piqueras,J., Guitart,M., Martin-Santos,R., Martorell,L.,
            Menchon,J.M., Roca,M., Saiz-Ruiz,J., Sanjuan,J., Torrens,M.,
            Urretavizcaya,M., Valero,J., Vilella,E., Estivill,X. and
            Carracedo,A.
  CONSRTM   Psychiatric Genetics Network Group
  TITLE     Identification of new putative susceptibility genes for several
            psychiatric disorders by association analysis of regulatory and
            non-synonymous SNPs of 306 genes involved in neurotransmission and
            neurodevelopment
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 150B (6), 808-816 (2009)
   PUBMED   19086053
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 361)
  AUTHORS   Wang,D.D., Shu,Z., Lieser,S.A., Chen,P.L. and Lee,W.H.
  TITLE     Human mitochondrial SUV3 and polynucleotide phosphorylase form a
            330-kDa heteropentamer to cooperatively degrade double-stranded RNA
            with a 3'-to-5' directionality
  JOURNAL   J Biol Chem 284 (31), 20812-20821 (2009)
   PUBMED   19509288
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL122001.32.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1317714.1,
                                           SRR14038194.2244427.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2159931
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p33"
     Protein         1..361
                     /product="5-cytosine rRNA methyltransferase NSUN4 isoform
                     d"
                     /note="putative methyltransferase NSUN4; NOL1/NOP2/Sun
                     domain family member 4; sperm head and tail associated
                     protein; 5-methylcytosine rRNA methyltransferase NSUN4;
                     NOP2/Sun RNA methyltransferase family member 4; NOP2/Sun
                     domain family, member 4; 5-methylcytosine tRNA
                     methyltransferase NSUN4; 5-cytosine tRNA methyltransferase
                     NSUN4; mRNA cytosine C(5)-methyltransferase NSUN4;
                     5-cytosine rRNA methyltransferase NSUN4"
                     /calculated_mol_wt=37079
     transit_peptide 1..25
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:22949673,
                     ECO:0000269|PubMed:23022348; propagated from
                     UniProtKB/Swiss-Prot (Q96CB9.2)"
                     /calculated_mol_wt=2872
     Region          <135..326
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96CB9.2)"
     CDS             1..361
                     /gene="NSUN4"
                     /gene_synonym="SHTAP"
                     /coded_by="NM_001387266.1:21..1106"
                     /note="isoform d is encoded by transcript variant 8"
                     /db_xref="GeneID:387338"
                     /db_xref="HGNC:HGNC:31802"
                     /db_xref="MIM:615394"
ORIGIN      
        1 maaltlrgvr ellkrvdlat vprrhrykkk waatepkfpa vrlalqnfdm tysvqfgdlw
       61 psirvsllse qkygalvnnf aawdhvsakl eqlsakdfvn eaishwelqs eggqsaapsp
      121 aswacspnlr cftfdrgdis rfpparpgsl gvmeyylmda asllpvlalg lqpgdivldl
      181 caapggktla llqtgccrnl aandlspsri arlqkilhsy vpeeirdgnq vrvtswdgrk
      241 wgelegdtyd rvlvdvpctt drhslheeen nifkrsrkke rqilpvlqvq llaagllatk
      301 pgghvvystc slshlqneyv vqgaiellan qysiqtgsgs hqggvpwcdl gslqpppprl
      361 k
//
LOCUS       NP_001372187             173 aa            linear   PRI 21-NOV-2025
DEFINITION  protein tyrosine phosphatase type IVA 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001372187
VERSION     NP_001372187.1
DBSOURCE    REFSEQ: accession NM_001385258.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Cho,M.J., Lee,D.G., Lee,J.W., Hwang,B., Yoon,S.J., Lee,S.J.,
            Park,Y.J., Park,S.H., Lee,H.G., Kim,Y.H., Lee,C.H., Lee,J.,
            Lee,N.K., Han,T.S., Cho,H.S., Moon,J.H., Lee,G.S., Bae,K.H.,
            Hwang,G.S., Lee,S.H., Chung,S.J., Shim,S., Cho,J., Oh,G.T.,
            Kwon,Y.G., Park,J.G. and Min,J.K.
  TITLE     Endothelial PTP4A1 mitigates vascular inflammation via USF1/A20
            axis-mediated NF-kappaB inactivation
  JOURNAL   Cardiovasc Res 119 (5), 1265-1278 (2023)
   PUBMED   36534975
  REMARK    GeneRIF: Endothelial PTP4A1 mitigates vascular inflammation via
            USF1/A20 axis-mediated NF-kappaB inactivation.
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Hu,H., Ye,L. and Liu,Z.
  TITLE     GINS2 regulates the proliferation and apoptosis of colon cancer
            cells through PTP4A1
  JOURNAL   Mol Med Rep 25 (4) (2022)
   PUBMED   35137928
  REMARK    GeneRIF: GINS2 regulates the proliferation and apoptosis of colon
            cancer cells through PTP4A1.
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 173)
  AUTHORS   Li,O., Jiang,B., Yi,W.M., Zhang,Y., Yang,P.Z., Guo,C., Sun,Z.P. and
            Peng,C.
  TITLE     LncRNA NEAT1 promotes cell proliferation, migration, and invasion
            via the miR-186-5p/PTP4A1 axis in cholangiocarcinoma
  JOURNAL   Kaohsiung J Med Sci 37 (5), 379-391 (2021)
   PUBMED   33502823
  REMARK    GeneRIF: LncRNA NEAT1 promotes cell proliferation, migration, and
            invasion via the miR-186-5p/PTP4A1 axis in cholangiocarcinoma.
REFERENCE   6  (residues 1 to 173)
  AUTHORS   Andreev,D.E., O'Connor,P.B., Fahey,C., Kenny,E.M., Terenin,I.M.,
            Dmitriev,S.E., Cormican,P., Morris,D.W., Shatsky,I.N. and
            Baranov,P.V.
  TITLE     Translation of 5' leaders is pervasive in genes resistant to eIF2
            repression
  JOURNAL   Elife 4, e03971 (2015)
   PUBMED   25621764
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 173)
  AUTHORS   Tsujimoto,H., Nishizuka,S., Redpath,J.L. and Stanbridge,E.J.
  TITLE     Differential gene expression in tumorigenic and nontumorigenic HeLa
            x normal human fibroblast hybrid cells
  JOURNAL   Mol Carcinog 26 (4), 298-304 (1999)
   PUBMED   10569806
REFERENCE   8  (residues 1 to 173)
  AUTHORS   Peng,Y., Genin,A., Spinner,N.B., Diamond,R.H. and Taub,R.
  TITLE     The gene encoding human nuclear protein tyrosine phosphatase,
            PRL-1. Cloning, chromosomal localization, and identification of an
            intron enhancer
  JOURNAL   J Biol Chem 273 (27), 17286-17295 (1998)
   PUBMED   9642300
REFERENCE   9  (residues 1 to 173)
  AUTHORS   Dayton,M.A. and Knobloch,T.J.
  TITLE     Multiple phosphotyrosine phosphatase mRNAs are expressed in the
            human lung fibroblast cell line WI-38
  JOURNAL   Recept Signal Transduct 7 (4), 241-256 (1997)
   PUBMED   9633825
REFERENCE   10 (residues 1 to 173)
  AUTHORS   Cates,C.A., Michael,R.L., Stayrook,K.R., Harvey,K.A., Burke,Y.D.,
            Randall,S.K., Crowell,P.L. and Crowell,D.N.
  TITLE     Prenylation of oncogenic human PTP(CAAX) protein tyrosine
            phosphatases
  JOURNAL   Cancer Lett 110 (1-2), 49-55 (1996)
   PUBMED   9018080
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL135905.6.
            
            Summary: This gene encodes a member of a small class of prenylated
            protein tyrosine phosphatases (PTPs), which contain a PTP domain
            and a characteristic C-terminal prenylation motif. The encoded
            protein is a cell signaling molecule that plays regulatory roles in
            a variety of cellular processes, including cell proliferation and
            migration. The protein may also be involved in cancer development
            and metastasis. This tyrosine phosphatase is a nuclear protein, but
            may associate with plasma membrane by means of its prenylation
            motif. Pseudogenes related to this gene are located on chromosomes
            1, 2, 5, 7, 11 and X. [provided by RefSeq, Jun 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1084937.1,
                                           SRR14038191.3147562.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465405, SAMN04284274
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q12"
     Protein         1..173
                     /product="protein tyrosine phosphatase type IVA 1 isoform
                     1"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase type IVA protein 1;
                     protein-tyrosine phosphatase of regenerating liver 1;
                     PVT1/PTP4A1 fusion; protein tyrosine phosphatase type IVA,
                     member 1"
                     /calculated_mol_wt=19684
     mat_peptide     1..170
                     /product="Protein tyrosine phosphatase type IVA 1.
                     /id=PRO_0000094780"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93096.2)"
                     /calculated_mol_wt=19471
     Region          1..167
                     /region_name="PTP-IVa1"
                     /note="protein tyrosine phosphatase type IVA 1; cd18537"
                     /db_xref="CDD:350513"
     Site            order(5,7,72..73,108..110,137..140,142,144)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:350513"
     Site            order(47,53..54,56,59,64..68)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:350513"
     Region          97..132
                     /region_name="Interaction with ATF5.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93096.2)"
     Site            170
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q93096.2)"
     CDS             1..173
                     /gene="PTP4A1"
                     /gene_synonym="HH72; PRL-1; PRL1; PTP(CAAX1); PTPCAAX1"
                     /coded_by="NM_001385258.1:1322..1843"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS4965.1"
                     /db_xref="GeneID:7803"
                     /db_xref="HGNC:HGNC:9634"
                     /db_xref="MIM:601585"
ORIGIN      
        1 marmnrpapv evtyknmrfl ithnptnatl nkfieelkky gvttivrvce atydttlvek
       61 egihvldwpf ddgappsnqi vddwlslvki kfreepgcci avhcvaglgr apvlvalali
      121 eggmkyedav qfirqkrrga fnskqllyle kyrpkmrlrf kdsnghrnnc ciq
//
LOCUS       NP_000542                213 aa            linear   PRI 21-NOV-2025
DEFINITION  von Hippel-Lindau disease tumor suppressor isoform 1 [Homo
            sapiens].
ACCESSION   NP_000542
VERSION     NP_000542.1
DBSOURCE    REFSEQ: accession NM_000551.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Dong,X., Zhang,D., Zhang,X., Liu,Y. and Liu,Y.
  TITLE     Network modeling links kidney developmental programs and the cancer
            type-specificity of VHL mutations
  JOURNAL   NPJ Syst Biol Appl 10 (1), 114 (2024)
   PUBMED   39362887
  REMARK    GeneRIF: Network modeling links kidney developmental programs and
            the cancer type-specificity of VHL mutations.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Mabry,A.R., Singh,A., Mulrooney,B., Gorman,J., Thielbar,A.R.,
            Wolf,E.R. and Mayo,L.D.
  TITLE     Induction of the Mdm2 gene and protein by kinase signaling pathways
            is repressed by the pVHL tumor suppressor
  JOURNAL   Proc Natl Acad Sci U S A 121 (31), e2400935121 (2024)
   PUBMED   39047034
  REMARK    GeneRIF: Induction of the Mdm2 gene and protein by kinase signaling
            pathways is repressed by the pVHL tumor suppressor.
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Mukhopadhyay,D., Chakraborty,B., Sarkar,S., Alam,N. and Panda,C.K.
  TITLE     Clinical implications of activation of the LIMD1-VHL-HIF1alpha
            pathway during head-&-neck squamous cell carcinoma development
  JOURNAL   Indian J Med Res 159 (5), 479-493 (2024)
   PUBMED   39382421
  REMARK    GeneRIF: Clinical implications of activation of the
            LIMD1-VHL-HIF1alpha pathway during head-&-neck squamous cell
            carcinoma development.
REFERENCE   5  (residues 1 to 213)
  AUTHORS   Neumann,H.P., Eng,C., Mulligan,L.M., Glavac,D., Zauner,I.,
            Ponder,B.A., Crossey,P.A., Maher,E.R. and Brauch,H.
  TITLE     Consequences of direct genetic testing for germline mutations in
            the clinical management of families with multiple endocrine
            neoplasia, type II
  JOURNAL   JAMA 274 (14), 1149-1151 (1995)
   PUBMED   7563486
REFERENCE   6  (residues 1 to 213)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   7  (residues 1 to 213)
  AUTHORS   Duan,D.R., Humphrey,J.S., Chen,D.Y., Weng,Y., Sukegawa,J., Lee,S.,
            Gnarra,J.R., Linehan,W.M. and Klausner,R.D.
  TITLE     Characterization of the VHL tumor suppressor gene product:
            localization, complex formation, and the effect of natural
            inactivating mutations
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6459-6463 (1995)
   PUBMED   7604013
REFERENCE   8  (residues 1 to 213)
  AUTHORS   Latif,F., Tory,K., Gnarra,J., Yao,M., Duh,F.M., Orcutt,M.L.,
            Stackhouse,T., Kuzmin,I., Modi,W., Geil,L. et al.
  TITLE     Identification of the von Hippel-Lindau disease tumor suppressor
            gene
  JOURNAL   Science 260 (5112), 1317-1320 (1993)
   PUBMED   8493574
REFERENCE   9  (residues 1 to 213)
  AUTHORS   van Leeuwaarde,R.S., Ahmad,S., van Nesselrooij,B., Zandee,W. and
            Giles,R.H.
  TITLE     Von Hippel-Lindau Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301636
REFERENCE   10 (residues 1 to 213)
  AUTHORS   Neumann,H.P. and Wiestler,O.D.
  TITLE     Clustering of features of von Hippel-Lindau syndrome: evidence for
            a complex genetic locus
  JOURNAL   Lancet 337 (8749), 1052-1054 (1991)
   PUBMED   1673491
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC034193.5.
            
            Summary: This gene encodes a component of a ubiquitination complex.
            The encoded protein is involved in the ubiquitination and
            degradation of hypoxia-inducible-factor (HIF), which is a
            transcription factor that plays a central role in the regulation of
            gene expression by oxygen. In addition to oxygen-related gene
            expression, this protein plays a role in many other cellular
            processes including cilia formation, cytokine signaling, regulation
            of senescence, and formation of the extracellular matrix. Variants
            of this gene are associated with von Hippel-Lindau syndrome,
            pheochromocytoma, erythrocytosis, renal cell carcinoma, and
            cerebellar hemangioblastoma. [provided by RefSeq, Jun 2022].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.971511.1, L15409.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256474.3/ ENSP00000256474.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3"
     Protein         1..213
                     /product="von Hippel-Lindau disease tumor suppressor
                     isoform 1"
                     /note="elongin binding protein; von Hippel-Lindau disease
                     tumor suppressor; protein G7; von Hippel-Lindau tumor
                     suppressor, E3 ubiquitin protein ligase"
                     /calculated_mol_wt=24022
     Region          1..65
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P40337.2)"
     Region          14..53
                     /region_name="8 X 5 AA tandem repeats of
                     G-[PAVG]-E-E-[DAYSLE]"
                     /note="propagated from UniProtKB/Swiss-Prot (P40337.2)"
     Region          54
                     /region_name="alternative start codon"
     Region          63..144
                     /region_name="VHL"
                     /note="VHL beta domain; pfam01847"
                     /db_xref="CDD:460360"
     Site            order(67,69,75,77..79,88,91,98..99,105..112,115,117)
                     /site_type="other"
                     /note="pVHL-HIF-1alpha interaction [polypeptide binding]"
                     /db_xref="CDD:176472"
     Site            order(79,153,159,161..163,165..166,174,177..178,184)
                     /site_type="other"
                     /note="pVHL-ElonginB-ElonginC (VBC) interface [polypeptide
                     binding]"
                     /db_xref="CDD:176472"
     Region          100..155
                     /region_name="Involved in binding to CCT complex"
                     /note="propagated from UniProtKB/Swiss-Prot (P40337.2)"
     Region          156..204
                     /region_name="VHL_C"
                     /note="VHL box domain; pfam17211"
                     /db_xref="CDD:407332"
     Region          157..166
                     /region_name="Interaction with Elongin BC complex"
                     /note="propagated from UniProtKB/Swiss-Prot (P40337.2)"
     CDS             1..213
                     /gene="VHL"
                     /gene_synonym="HRCA1; pVHL; RCA1; VHL1"
                     /coded_by="NM_000551.4:71..712"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2597.1"
                     /db_xref="GeneID:7428"
                     /db_xref="HGNC:HGNC:12687"
                     /db_xref="MIM:608537"
ORIGIN      
        1 mprraenwde aevgaeeagv eeygpeedgg eesgaeesgp eesgpeelga eeemeagrpr
       61 pvlrsvnsre psqvifcnrs prvvlpvwln fdgepqpypt lppgtgrrih syrghlwlfr
      121 dagthdgllv nqtelfvpsl nvdgqpifan itlpvytlke rclqvvrslv kpenyrrldi
      181 vrslyedled hpnvqkdler ltqeriahqr mgd
//
LOCUS       NP_001311127             862 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase Itchy homolog isoform 2 [Homo sapiens].
ACCESSION   NP_001311127
VERSION     NP_001311127.1
DBSOURCE    REFSEQ: accession NM_001324198.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Shen,S., Cai,D., Liang,H., Zeng,G., Liu,W., Yan,R., Yu,X.,
            Zhang,H., Liu,S., Li,W., Deng,R., Lu,X., Liu,Y., Sun,J. and Guo,H.
  TITLE     NEDD4 family ubiquitin ligase AIP4 interacts with Alix to enable
            HBV naked capsid egress in an Alix ubiquitination-independent
            manner
  JOURNAL   PLoS Pathog 20 (9), e1012485 (2024)
   PUBMED   39259704
  REMARK    GeneRIF: NEDD4 family ubiquitin ligase AIP4 interacts with Alix to
            enable HBV naked capsid egress in an Alix
            ubiquitination-independent manner.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 862)
  AUTHORS   Gahlot,P., Kravic,B., Rota,G., van den Boom,J., Levantovsky,S.,
            Schulze,N., Maspero,E., Polo,S., Behrends,C. and Meyer,H.
  TITLE     Lysosomal damage sensing and lysophagy initiation by SPG20-ITCH
  JOURNAL   Mol Cell 84 (8), 1556-1569 (2024)
   PUBMED   38503285
  REMARK    GeneRIF: Lysosomal damage sensing and lysophagy initiation by
            SPG20-ITCH.
REFERENCE   4  (residues 1 to 862)
  AUTHORS   Totland,M.Z., Knudsen,L.M., Rasmussen,N.L., Omori,Y., Sorensen,V.,
            Elster,V.C.W., Stenersen,J.M., Larsen,M., Jensen,C.L., Zickfeldt
            Lade,A.A., Bruusgaard,E., Basing,S., Kryeziu,K., Brech,A.,
            Aasen,T., Lothe,R.A. and Leithe,E.
  TITLE     The E3 ubiquitin ligase ITCH negatively regulates intercellular
            communication via gap junctions by targeting connexin43 for
            lysosomal degradation
  JOURNAL   Cell Mol Life Sci 81 (1), 171 (2024)
   PUBMED   38597989
  REMARK    GeneRIF: The E3 ubiquitin ligase ITCH negatively regulates
            intercellular communication via gap junctions by targeting
            connexin43 for lysosomal degradation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 862)
  AUTHORS   Lohr,N.J., Molleston,J.P., Strauss,K.A., Torres-Martinez,W.,
            Sherman,E.A., Squires,R.H., Rider,N.L., Chikwava,K.R.,
            Cummings,O.W., Morton,D.H. and Puffenberger,E.G.
  TITLE     Human ITCH E3 ubiquitin ligase deficiency causes syndromic
            multisystem autoimmune disease
  JOURNAL   Am J Hum Genet 86 (3), 447-453 (2010)
   PUBMED   20170897
  REMARK    GeneRIF: describe, in ten patients, identification of a mutation
            resulting in truncation of ITCH. These patients not only have
            multisystem autoimmune disease but also display morphologic and
            developmental abnormalities.
REFERENCE   6  (residues 1 to 862)
  AUTHORS   Chen,X., Wen,S., Fukuda,M.N., Gavva,N.R., Hsu,D., Akama,T.O.,
            Yang-Feng,T. and Shen,C.K.
  TITLE     Human ITCH is a coregulator of the hematopoietic transcription
            factor NF-E2
  JOURNAL   Genomics 73 (2), 238-241 (2001)
   PUBMED   11318614
  REMARK    GeneRIF: gene expression regulation; coregulates hematopoietic
            transcription factor NF-E2
REFERENCE   7  (residues 1 to 862)
  AUTHORS   Qiu,L., Joazeiro,C., Fang,N., Wang,H.Y., Elly,C., Altman,Y.,
            Fang,D., Hunter,T. and Liu,Y.C.
  TITLE     Recognition and ubiquitination of Notch by Itch, a hect-type E3
            ubiquitin ligase
  JOURNAL   J Biol Chem 275 (46), 35734-35737 (2000)
   PUBMED   10940313
REFERENCE   8  (residues 1 to 862)
  AUTHORS   Winberg,G., Matskova,L., Chen,F., Plant,P., Rotin,D., Gish,G.,
            Ingham,R., Ernberg,I. and Pawson,T.
  TITLE     Latent membrane protein 2A of Epstein-Barr virus binds WW domain E3
            protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases
  JOURNAL   Mol Cell Biol 20 (22), 8526-8535 (2000)
   PUBMED   11046148
REFERENCE   9  (residues 1 to 862)
  AUTHORS   Wood,J.D., Yuan,J., Margolis,R.L., Colomer,V., Duan,K., Kushi,J.,
            Kaminsky,Z., Kleiderlein,J.J., Sharp,A.H. and Ross,C.A.
  TITLE     Atrophin-1, the DRPLA gene product, interacts with two families of
            WW domain-containing proteins
  JOURNAL   Mol Cell Neurosci 11 (3), 149-160 (1998)
   PUBMED   9647693
REFERENCE   10 (residues 1 to 862)
  AUTHORS   Perry,W.L., Hustad,C.M., Swing,D.A., O'Sullivan,T.N., Jenkins,N.A.
            and Copeland,N.G.
  TITLE     The itchy locus encodes a novel ubiquitin protein ligase that is
            disrupted in a18H mice
  JOURNAL   Nat Genet 18 (2), 143-146 (1998)
   PUBMED   9462742
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL356299.16, AL109923.29 and
            BG928040.1.
            
            Summary: This gene encodes a member of the Nedd4 family of HECT
            domain E3 ubiquitin ligases. HECT domain E3 ubiquitin ligases
            transfer ubiquitin from E2 ubiquitin-conjugating enzymes to protein
            substrates, thus targeting specific proteins for lysosomal
            degradation. The encoded protein plays a role in multiple cellular
            processes including erythroid and lymphoid cell differentiation and
            the regulation of immune responses. Mutations in this gene are a
            cause of syndromic multisystem autoimmune disease. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed for this gene. [provided by RefSeq, Mar 2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.17759.1,
                                           SRR1660807.164506.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..862
                     /product="E3 ubiquitin-protein ligase Itchy homolog
                     isoform 2"
                     /EC_number="2.3.2.26"
                     /note="atrophin-1 interacting protein 4; NFE2-associated
                     polypeptide 1; itchy E3 ubiquitin protein ligase homolog;
                     HECT-type E3 ubiquitin transferase Itchy homolog"
                     /calculated_mol_wt=98545
     Region          17..140
                     /region_name="C2_E3_ubiquitin_ligase"
                     /note="C2 domain present in E3 ubiquitin ligase; cd04021"
                     /db_xref="CDD:175988"
     Region          287..316
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          <318..862
                     /region_name="HUL4"
                     /note="Ubiquitin-protein ligase [Posttranslational
                     modification, protein turnover, chaperones]; COG5021"
                     /db_xref="CDD:227354"
     CDS             1..862
                     /gene="ITCH"
                     /gene_synonym="ADMFD; AIF4; AIP4; NAPP1"
                     /coded_by="NM_001324198.2:197..2785"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS13234.1"
                     /db_xref="GeneID:83737"
                     /db_xref="HGNC:HGNC:13890"
                     /db_xref="MIM:606409"
ORIGIN      
        1 msdsgsqlgs mgsltmksql qitvisaklk enkknwfgps pyvevtvdgq skktekcnnt
       61 nspkwkqplt vivtpvsklh frvwshqtlk sdvllgtaal diyetlksnn mkleevvvtl
      121 qlggdkepte tigdlsicld glqlesevvt ngettcsesa sqnddgsrsk detrvstngs
      181 ddpedagage nrrvsgnnsp slsnggfkps rpprpsrppp ptprrpasvn gspsatsesd
      241 gsstgslppt ntntntsega tsgliiplti sggsgprpln pvtqaplppg weqrvdqhgr
      301 vyyvdhvekr ttwdrpeplp pgwerrvdnm griyyvdhft rtttwqrptl esvrnyeqwq
      361 lqrsqlqgam qqfnqrfiyg nqdlfatsqs kefdplgplp pgwekrtdsn grvyfvnhnt
      421 ritqwedprs qgqlnekplp egwemrftvd gipyfvdhnr rtttyidprt gksaldngpq
      481 iayvrdfkak vqyfrfwcqq lampqhikit vtrktlfeds fqqimsfspq dlrrrlwvif
      541 pgeegldygg varewfflls hevlnpmycl feyagkdnyc lqinpasyin pdhlkyfrfi
      601 grfiamalfh gkfidtgfsl pfykrilnkp vglkdlesid pefynsliwv kennieecdl
      661 emyfsvdkei lgeikshdlk pnggnilvte enkeeyirmv aewrlsrgve eqtqaffegf
      721 neilpqqylq yfdakelevl lcgmqeidln dwqrhaiyrh yartskqimw fwqfvkeidn
      781 ekrmrllqfv tgtcrlpvgg fadlmgsngp qkfciekvgk enwlprshtc fnrldlppyk
      841 syeqlkekll faieetegfg qe
//
LOCUS       NP_001373971             346 aa            linear   PRI 21-NOV-2025
DEFINITION  heparan sulfate glucosamine 3-O-sulfotransferase 5 [Homo sapiens].
ACCESSION   NP_001373971 XP_016865959
VERSION     NP_001373971.1
DBSOURCE    REFSEQ: accession NM_001387042.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wang,Q., Xiang,B., Deng,W., Wu,J., Li,M., Ma,X., Wang,Y., Jiang,L.,
            McAlonan,G., Chua,S.E., Sham,P.C., Hu,X. and Li,T.
  TITLE     Genome-wide association analysis with gray matter volume as a
            quantitative phenotype in first-episode treatment-naive patients
            with schizophrenia
  JOURNAL   PLoS One 8 (9), e75083 (2013)
   PUBMED   24086445
  REMARK    Erratum:[PLoS One. 2015 Apr 07;10(4):e0122945. doi:
            10.1371/journal.pone.0122945. PMID: 25848962]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Vieira,A.R., McHenry,T.G., Daack-Hirsch,S., Murray,J.C. and
            Marazita,M.L.
  TITLE     Candidate gene/loci studies in cleft lip/palate and dental
            anomalies finds novel susceptibility genes for clefts
  JOURNAL   Genet Med 10 (9), 668-674 (2008)
   PUBMED   18978678
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Chen,J. and Liu,J.
  TITLE     Characterization of the structure of antithrombin-binding heparan
            sulfate generated by heparan sulfate 3-O-sulfotransferase 5
  JOURNAL   Biochim Biophys Acta 1725 (2), 190-200 (2005)
   PUBMED   16099108
  REMARK    GeneRIF: Structural analysis of 3-OST-5 HS(act) revealed that the
            antithrombin-binding site of 3-OST-5 HS(act) is located within a
            domain clustered with N-sulfated glucosamine units.
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Duncan,M.B., Chen,J., Krise,J.P. and Liu,J.
  TITLE     The biosynthesis of anticoagulant heparan sulfate by the heparan
            sulfate 3-O-sulfotransferase isoform 5
  JOURNAL   Biochim Biophys Acta 1671 (1-3), 34-43 (2004)
   PUBMED   15026143
  REMARK    GeneRIF: Results demonstrate that the human 3-O-sulfotransferase
            isoform 5 gene is capable of synthesizing anticoagulant heparan
            sulfate (HS) in CHO cells and may contribute to the biosynthesis of
            HS in humans.
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Chen,J., Duncan,M.B., Carrick,K., Pope,R.M. and Liu,J.
  TITLE     Biosynthesis of 3-O-sulfated heparan sulfate: unique substrate
            specificity of heparan sulfate 3-O-sulfotransferase isoform 5
  JOURNAL   Glycobiology 13 (11), 785-794 (2003)
   PUBMED   12907690
REFERENCE   6  (residues 1 to 346)
  AUTHORS   Mochizuki,H., Yoshida,K., Gotoh,M., Sugioka,S., Kikuchi,N.,
            Kwon,Y.D., Tawada,A., Maeyama,K., Inaba,N., Hiruma,T., Kimata,K.
            and Narimatsu,H.
  TITLE     Characterization of a heparan sulfate 3-O-sulfotransferase-5, an
            enzyme synthesizing a tetrasulfated disaccharide
  JOURNAL   J Biol Chem 278 (29), 26780-26787 (2003)
   PUBMED   12740361
  REMARK    GeneRIF: Recombinant 3-OST-5 only exhibited sulfotransferase
            activity toward heparan sulfate and heparin. 3-OST-5 was highly
            expressed in fetal brain, followed by adult brain and spinal cord,
            and at very low or undetectable levels in other tissues.
REFERENCE   7  (residues 1 to 346)
  AUTHORS   Xia,G., Chen,J., Tiwari,V., Ju,W., Li,J.P., Malmstrom,A., Shukla,D.
            and Liu,J.
  TITLE     Heparan sulfate 3-O-sulfotransferase isoform 5 generates both an
            antithrombin-binding site and an entry receptor for herpes simplex
            virus, type 1
  JOURNAL   J Biol Chem 277 (40), 37912-37919 (2002)
   PUBMED   12138164
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136446.14, AL500524.10 and AL355498.10.
            
            On Sep 21, 2020 this sequence version replaced XP_016865959.1.
            
            Summary: HS3ST5 belongs to a group of heparan sulfate
            3-O-sulfotransferases (EC 2.8.2.23) that transfer sulfate from
            3-prime-phosphoadenosine 5-prime phosphosulfate (PAPS) to heparan
            sulfate and heparin (Mochizuki et al., 2003 [PubMed
            12740361]).[supplied by OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.3525830.1,
                                           SRR1803616.125222.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267774, SAMN03267781
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21-q22.1"
     Protein         1..346
                     /product="heparan sulfate glucosamine 3-O-sulfotransferase
                     5"
                     /EC_number="2.8.2.23"
                     /note="heparan sulfate 3-OST-5; h3-OST-5; heparan sulfate
                     3-O-sulfotransferase 5; heparan sulfate D-glucosaminyl
                     3-O-sulfotransferase 5; heparan sulfate (glucosamine)
                     3-O-sulfotransferase 5"
                     /calculated_mol_wt=40277
     Site            13..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZT8.1)"
     Region          90..330
                     /region_name="Sulfotransfer_1"
                     /note="Sulfotransferase domain; cl21551"
                     /db_xref="CDD:473908"
     Site            287
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZT8.1)"
     CDS             1..346
                     /gene="HS3ST5"
                     /gene_synonym="3-OST-5; 3OST5; HS3OST5; NBLA04021"
                     /coded_by="NM_001387042.1:1991..3031"
                     /db_xref="CCDS:CCDS34517.1"
                     /db_xref="GeneID:222537"
                     /db_xref="HGNC:HGNC:19419"
                     /db_xref="MIM:609407"
ORIGIN      
        1 mlfkqqawlr qkllvlgsla vgsllylvar vgsldrlqpi cpiegrlgga rtqaefplra
       61 lqfkrgllhe frkgnaskeq vrlhdlvqql pkaiiigvrk ggtralleml nlhpavvkas
      121 qeihffdnde nygkgiewyr kkmpfsypqq itiekspayf iteevperiy kmnssiklli
      181 ivrepttrai sdytqvlegk erknktyykf eklaidpntc evntkykavr tsiytkhler
      241 wlkyfpieqf hvvdgdrlit eplpelqlve kflnlppris qynlyfnatr gfyclrfnii
      301 fnkclagskg rihpevdpsv itklrkffhp fnqkfyqitg rtlnwp
//
LOCUS       NP_001363201             552 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase PAK 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001363201
VERSION     NP_001363201.1
DBSOURCE    REFSEQ: accession NM_001376272.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Kervarrec,T., Westphal,D., Pissaloux,D., Legrand,M., Tirode,F.,
            Neuhart,A., Drouot,F., Becker,J.C., Macagno,N., Seris,A.,
            Jouary,T., Beltzung,F., Jullie,M.L., Harms,P.W., Cribier,B.,
            Mourah,S., Jouenne,F., Fromont,G., Louveau,B., Mancini,M.,
            Kazakov,D.V., de la Fouchardiere,A. and Battistella,M.
  TITLE     Porocarcinomas with PAK1/2/3 fusions: a series of 12 cases
  JOURNAL   Histopathology 85 (4), 566-578 (2024)
   PUBMED   38785043
  REMARK    GeneRIF: Porocarcinomas with PAK1/2/3 fusions: a series of 12
            cases.
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Zhao,P., Zhang,J., Song,W., Qi,D., Huang,Y., Su,Y., Wu,R., Zhang,L.
            and Zhang,S.
  TITLE     Incarvine C and its analogues inhibit the formation of cell
            cytoskeleton by targeting Rac1
  JOURNAL   Bioorg Chem 149, 107512 (2024)
   PUBMED   38833990
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Xu,M.H., Zheng,Y.M., Liang,B.G., Xu,W.X., Cao,J., Wang,P.,
            Dong,Z.Y., Zhou,C.H., Sun,H.C., Ren,N., Ke,A.W. and Shen,Y.H.
  TITLE     Deubiquitination of CIB1 by USP14 promotes lenvatinib resistance
            via the PAK1-ERK1/2 axis in hepatocellular carcinoma
  JOURNAL   Int J Biol Sci 20 (9), 3269-3284 (2024)
   PUBMED   38993552
  REMARK    GeneRIF: Deubiquitination of CIB1 by USP14 promotes lenvatinib
            resistance via the PAK1-ERK1/2 axis in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 552)
  AUTHORS   Luo,Q., Raulston,E.G., Prado,M.A., Wu,X., Gritsman,K., Whalen,K.S.,
            Yan,K., Booth,C.A.G., Xu,R., van Galen,P., Doench,J.G., Shimony,S.,
            Long,H.W., Neuberg,D.S., Paulo,J.A. and Lane,A.A.
  TITLE     Targetable leukaemia dependency on noncanonical PI3Kgamma
            signalling
  JOURNAL   Nature 630 (8015), 198-205 (2024)
   PUBMED   38720074
  REMARK    GeneRIF: Targetable leukaemia dependency on noncanonical PI3Kgamma
            signalling.
REFERENCE   6  (residues 1 to 552)
  AUTHORS   Manser,E., Huang,H.Y., Loo,T.H., Chen,X.Q., Dong,J.M., Leung,T. and
            Lim,L.
  TITLE     Expression of constitutively active alpha-PAK reveals effects of
            the kinase on actin and focal complexes
  JOURNAL   Mol Cell Biol 17 (3), 1129-1143 (1997)
   PUBMED   9032240
REFERENCE   7  (residues 1 to 552)
  AUTHORS   Bokoch,G.M., Wang,Y., Bohl,B.P., Sells,M.A., Quilliam,L.A. and
            Knaus,U.G.
  TITLE     Interaction of the Nck adapter protein with p21-activated kinase
            (PAK1)
  JOURNAL   J Biol Chem 271 (42), 25746-25749 (1996)
   PUBMED   8824201
REFERENCE   8  (residues 1 to 552)
  AUTHORS   Brown,J.L., Stowers,L., Baer,M., Trejo,J., Coughlin,S. and Chant,J.
  TITLE     Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase
            pathway
  JOURNAL   Curr Biol 6 (5), 598-605 (1996)
   PUBMED   8805275
REFERENCE   9  (residues 1 to 552)
  AUTHORS   Martin,G.A., Bollag,G., McCormick,F. and Abo,A.
  TITLE     A novel serine kinase activated by rac1/CDC42Hs-dependent
            autophosphorylation is related to PAK65 and STE20
  JOURNAL   EMBO J 14 (9), 1970-1978 (1995)
   PUBMED   7744004
  REMARK    Erratum:[EMBO J. 1995 Sep 1;14(17):4385. doi:
            10.1002/j.1460-2075.1995.tb00113.x. PMID: 7556080]
REFERENCE   10 (residues 1 to 552)
  AUTHORS   Manser,E., Leung,T., Salihuddin,H., Zhao,Z.S. and Lim,L.
  TITLE     A brain serine/threonine protein kinase activated by Cdc42 and Rac1
  JOURNAL   Nature 367 (6458), 40-46 (1994)
   PUBMED   8107774
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000486.6.
            
            Summary: This gene encodes a family member of serine/threonine
            p21-activating kinases, known as PAK proteins. These proteins are
            critical effectors that link RhoGTPases to cytoskeleton
            reorganization and nuclear signaling, and they serve as targets for
            the small GTP binding proteins Cdc42 and Rac. This specific family
            member regulates cell motility and morphology. Mutations in this
            gene have been associated with macrocephaly, seizures, and speech
            delay. Overexpression of this gene is also reported in many cancer
            types, and particularly in breast cancer. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.164699.1,
                                           SRR18074969.2946872.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.5-q14.1"
     Protein         1..552
                     /product="serine/threonine-protein kinase PAK 1 isoform 3"
                     /EC_number="2.7.11.1"
                     /note="p21/Cdc42/Rac1-activated kinase 1 (yeast
                     Ste20-related); p21/Cdc42/Rac1-activated kinase 1 (STE20
                     homolog, yeast); serine/threonine-protein kinase PAK 1;
                     p21 protein (Cdc42/Rac)-activated kinase 1"
                     /calculated_mol_wt=61279
     Region          1..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB and autocatalysis.
                     /evidence=ECO:0000269|PubMed:14585966,
                     ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          74..139
                     /region_name="PBD"
                     /note="P21-Rho-binding domain; pfam00786"
                     /db_xref="CDD:395634"
     Site            order(75,78,81,83,86,110,114)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238526"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by OXSR1.
                     /evidence=ECO:0000250|UniProtKB:P35465; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20417602,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000269|PubMed:17726028,
                     ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          166..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17989089,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20417602; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000269|PubMed:17726028; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          218..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17989089,
                     ECO:0000269|PubMed:23260667, ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88643; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88643; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          256..551
                     /region_name="STKc_PAK1"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     p21-activated kinase 1; cd06654"
                     /db_xref="CDD:270820"
     Site            order(283..287,291,304,306,335,351..355,357..358,361,396,
                     398..401,403,413..414,417,430..434,436,463,472..474)
                     /site_type="active"
                     /db_xref="CDD:270820"
     Site            order(283..287,291,304,306,335,351..355,357..358,361,
                     400..401,403,413..414)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270820"
     Site            order(286..287,396,398..400,417,430..434,436,463,472..474)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270820"
     Site            order(288,322,391,393..396,414..415,442..443,445,450,475,
                     478,481)
                     /site_type="other"
                     /note="AID interaction site [polypeptide binding]"
                     /db_xref="CDD:270820"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000269|PubMed:17726028,
                     ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            413..436
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270820"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis, BRSK2 and
                     PDPK1. /evidence=ECO:0000269|PubMed:10551809,
                     ECO:0000269|PubMed:10995762, ECO:0000269|PubMed:22153498,
                     ECO:0000269|PubMed:22669945; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     CDS             1..552
                     /gene="PAK1"
                     /gene_synonym="alpha-PAK; IDDMSSD; p65-PAK; PAKalpha"
                     /coded_by="NM_001376272.1:220..1878"
                     /note="isoform 3 is encoded by transcript variant 7"
                     /db_xref="GeneID:5058"
                     /db_xref="HGNC:HGNC:8590"
                     /db_xref="MIM:602590"
ORIGIN      
        1 msnngldiqd kppappmrnt stmigagskd agtlnhgskp lppnpeekkk kdrfyrsilp
       61 gdktnkkkek erpeislpsd fehtihvgfd avtgeftscm sllqgmpeqw arllqtsnit
      121 kseqkknpqa vldvlefyns kktsnsqkym sftdksaedy nssnalnvka vsetpavppv
      181 sededddddd atpppviapr pehtksvytr svieplpvtp trdvatspis ptennttppd
      241 altrntekqk kkpkmsdeei leklrsivsv gdpkkkytrf ekigqgasgt vytamdvatg
      301 qevaikqmnl qqqpkkelii neilvmrenk npnivnylds ylvgdelwvv meylaggslt
      361 dvvtetcmde gqiaavcrec lqaleflhsn qvihrdiksd nillgmdgsv kltdfgfcaq
      421 itpeqskrst mvgtpywmap evvtrkaygp kvdiwslgim aiemiegepp ylnenplral
      481 yliatngtpe lqnpeklsai frdflnrcle mdvekrgsak ellqhqflki akplssltpl
      541 iaaakeatkn nh
//
LOCUS       NP_001308018             559 aa            linear   PRI 21-NOV-2025
DEFINITION  COP9 signalosome complex subunit 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001308018
VERSION     NP_001308018.1
DBSOURCE    REFSEQ: accession NM_001321089.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Wei,H., Niu,Z., Ji,R., Jiang,W., Tang,J., Meng,Z., Cao,X., Zhang,X.
            and Liu,X.
  TITLE     Bioinformatics analysis of GPS1 expression and biological function
            in breast cancer
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 52 (2024)
   PUBMED   38289496
  REMARK    GeneRIF: Bioinformatics analysis of GPS1 expression and biological
            function in breast cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 559)
  AUTHORS   Fu,H., Zhang,Y., Chen,Y., Chen,J. and Chen,P.
  TITLE     CSN1 facilitates proliferation and migration of hepatocellular
            carcinoma cells by upregulating cyclin A2 expression
  JOURNAL   Mol Med Rep 23 (1) (2021)
   PUBMED   33200803
  REMARK    GeneRIF: CSN1 facilitates proliferation and migration of
            hepatocellular carcinoma cells by upregulating cyclin A2
            expression.
REFERENCE   5  (residues 1 to 559)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 559)
  AUTHORS   Lyapina,S., Cope,G., Shevchenko,A., Serino,G., Tsuge,T., Zhou,C.,
            Wolf,D.A., Wei,N., Shevchenko,A. and Deshaies,R.J.
  TITLE     Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome
  JOURNAL   Science 292 (5520), 1382-1385 (2001)
   PUBMED   11337588
REFERENCE   7  (residues 1 to 559)
  AUTHORS   Bech-Otschir,D., Kraft,R., Huang,X., Henklein,P., Kapelari,B.,
            Pollmann,C. and Dubiel,W.
  TITLE     COP9 signalosome-specific phosphorylation targets p53 to
            degradation by the ubiquitin system
  JOURNAL   EMBO J 20 (7), 1630-1639 (2001)
   PUBMED   11285227
REFERENCE   8  (residues 1 to 559)
  AUTHORS   Tsuge,T., Matsui,M. and Wei,N.
  TITLE     The subunit 1 of the COP9 signalosome suppresses gene expression
            through its N-terminal domain and incorporates into the complex
            through the PCI domain
  JOURNAL   J Mol Biol 305 (1), 1-9 (2001)
   PUBMED   11114242
  REMARK    GeneRIF: The N-terminal half of CSN1/GPS1 is required to repress
            c-fos expression and to inhibit AP-1 and SRE transactivation, while
            the C-terminal half allows integration of the protein into the COP9
            signalosome.
REFERENCE   9  (residues 1 to 559)
  AUTHORS   Seeger,M., Kraft,R., Ferrell,K., Bech-Otschir,D., Dumdey,R.,
            Schade,R., Gordon,C., Naumann,M. and Dubiel,W.
  TITLE     A novel protein complex involved in signal transduction possessing
            similarities to 26S proteasome subunits
  JOURNAL   FASEB J 12 (6), 469-478 (1998)
   PUBMED   9535219
REFERENCE   10 (residues 1 to 559)
  AUTHORS   Spain,B.H., Bowdish,K.S., Pacal,A.R., Staub,S.F., Koo,D.,
            Chang,C.Y., Xie,W. and Colicelli,J.
  TITLE     Two human cDNAs, including a homolog of Arabidopsis FUS6 (COP11),
            suppress G-protein- and mitogen-activated protein kinase-mediated
            signal transduction in yeast and mammalian cells
  JOURNAL   Mol Cell Biol 16 (12), 6698-6706 (1996)
   PUBMED   8943324
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC135056.4.
            
            Summary: This gene is known to suppress G-protein and
            mitogen-activated signal transduction in mammalian cells. The
            encoded protein shares significant similarity with Arabidopsis
            FUS6, which is a regulator of light-mediated signal transduction in
            plant cells. [provided by RefSeq, Mar 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.2784167.1,
                                           SRR1803611.268288.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..559
                     /product="COP9 signalosome complex subunit 1 isoform 3"
                     /note="COP9 signalosome complex subunit 1; JAB1-containing
                     signalosome subunit 1"
                     /calculated_mol_wt=62232
     Region          195..377
                     /region_name="RPN7"
                     /note="26S proteasome subunit RPN7; pfam10602"
                     /db_xref="CDD:431387"
     Region          392..496
                     /region_name="PCI"
                     /note="PCI domain; pfam01399"
                     /db_xref="CDD:460195"
     CDS             1..559
                     /gene="GPS1"
                     /gene_synonym="COPS1; CSN1; SGN1"
                     /coded_by="NM_001321089.3:35..1714"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:2873"
                     /db_xref="HGNC:HGNC:4549"
                     /db_xref="MIM:601934"
ORIGIN      
        1 mplpvqvfnl qqpassvsgs ggaesqdrmr dssapssass svtdlyctph ssrsdlvlpg
       61 tagdfslsas lsactllyeg avepmqidvd pqedpqnapd vnyvvenpsl dleqyaasys
      121 glmrierlqf iadhcptlrv ealkmalsfv qrtfnvdmye eihrklseat rsslrelqna
      181 pdaipesgve ppaldtawve atrkkallkl ekldtdlkny kgnsikesir rghddlgdhy
      241 ldcgdlsnal kcysrardyc tsakhvinmc lnvikvsvyl qnwshvlsyv skaestpeia
      301 eqrgerdsqt qailtklkca aglaelaark ykqaakclll asfdhcdfpe llspsnvaiy
      361 gglcalatfd rqelqrnvis sssfklflel epqvrdiifk fyeskyascl kmldemkdnl
      421 lldmylaphv rtlytqirnr aliqyfspyv sadmhrmaaa fnttvaaled eltqlilegl
      481 isarvdshsk ilyardvdqr sttfeksllm gkefqrraka mmlraavlrn qihvksppre
      541 gsqgeltpan sqsrmstnm
//
LOCUS       NP_001098720             459 aa            linear   PRI 21-NOV-2025
DEFINITION  neurexin 3 isoform 3 precursor [Homo sapiens].
ACCESSION   NP_001098720
VERSION     NP_001098720.1
DBSOURCE    REFSEQ: accession NM_001105250.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Gulec,G., Cosan,D.T., Sahin,F.M., Calis,I.U., Sonkurt,M.D.,
            Kosger,F. and Essizoglu,A.
  TITLE     Association of Nicotine Use Disorder with Neurexin 3 Gene
            Polymorphisms
  JOURNAL   Turk Psikiyatri Derg 32 (3), 160-166 (2021)
   PUBMED   34647286
  REMARK    GeneRIF: Association of Nicotine Use Disorder with Neurexin 3 Gene
            Polymorphisms.', trans 'Nikotin Kullanim Bozuklugunun Neurexin 3
            Gen Polimorfizmi ile Iliskisi.
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Hishimoto,A., Liu,Q.R., Drgon,T., Pletnikova,O., Walther,D.,
            Zhu,X.G., Troncoso,J.C. and Uhl,G.R.
  TITLE     Neurexin 3 polymorphisms are associated with alcohol dependence and
            altered expression of specific isoforms
  JOURNAL   Hum Mol Genet 16 (23), 2880-2891 (2007)
   PUBMED   17804423
  REMARK    GeneRIF: details of NRXN3's gene structure and variants, and
            association of NRXN3 SNPs with alcohol dependence
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 459)
  AUTHORS   Occhi,G., Rampazzo,A., Beffagna,G. and Antonio Danieli,G.
  TITLE     Identification and characterization of heart-specific splicing of
            human neurexin 3 mRNA (NRXN3)
  JOURNAL   Biochem Biophys Res Commun 298 (1), 151-155 (2002)
   PUBMED   12379233
  REMARK    GeneRIF: Identification and characterization of heart-specific
            splicing of neurexin 3 mRNA
REFERENCE   5  (residues 1 to 459)
  AUTHORS   Tabuchi,K. and Sudhof,T.C.
  TITLE     Structure and evolution of neurexin genes: insight into the
            mechanism of alternative splicing
  JOURNAL   Genomics 79 (6), 849-859 (2002)
   PUBMED   12036300
REFERENCE   6  (residues 1 to 459)
  AUTHORS   Rowen,L., Young,J., Birditt,B., Kaur,A., Madan,A., Philipps,D.L.,
            Qin,S., Minx,P., Wilson,R.K., Hood,L. and Graveley,B.R.
  TITLE     Analysis of the human neurexin genes: alternative splicing and the
            generation of protein diversity
  JOURNAL   Genomics 79 (4), 587-597 (2002)
   PUBMED   11944992
REFERENCE   7  (residues 1 to 459)
  AUTHORS   Missler,M., Hammer,R.E. and Sudhof,T.C.
  TITLE     Neurexophilin binding to alpha-neurexins. A single LNS domain
            functions as an independently folding ligand-binding unit
  JOURNAL   J Biol Chem 273 (52), 34716-34723 (1998)
   PUBMED   9856994
  REMARK    GeneRIF: N-terminal sequencing of rat neurexin III alpha provides
            evidence for signal peptide
REFERENCE   8  (residues 1 to 459)
  AUTHORS   Missler,M. and Sudhof,T.C.
  TITLE     Neurexins: three genes and 1001 products
  JOURNAL   Trends Genet 14 (1), 20-26 (1998)
   PUBMED   9448462
  REMARK    Review article
REFERENCE   9  (residues 1 to 459)
  AUTHORS   Ichtchenko,K., Nguyen,T. and Sudhof,T.C.
  TITLE     Structures, alternative splicing, and neurexin binding of multiple
            neuroligins
  JOURNAL   J Biol Chem 271 (5), 2676-2682 (1996)
   PUBMED   8576240
REFERENCE   10 (residues 1 to 459)
  AUTHORS   Ushkaryov,Y.A., Hata,Y., Ichtchenko,K., Moomaw,C., Afendis,S.,
            Slaughter,C.A. and Sudhof,T.C.
  TITLE     Conserved domain structure of beta-neurexins. Unusual cleaved
            signal sequences in receptor-like neuronal cell-surface proteins
  JOURNAL   J Biol Chem 269 (16), 11987-11992 (1994)
   PUBMED   8163501
  REMARK    GeneRIF: N-terminal sequencing of cow neurexin III beta provides
            evidence for signal peptide
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA243312.1, BC150194.1 and
            AF123462.1.
            
            Summary: This gene encodes a member of a family of proteins that
            function in the nervous system as receptors and cell adhesion
            molecules. Extensive alternative splicing and the use of
            alternative promoters results in multiple transcript variants and
            protein isoforms for this gene, but the full-length nature of many
            of these variants has not been determined. Transcripts that
            initiate from an upstream promoter encode alpha isoforms, which
            contain epidermal growth factor-like (EGF-like) sequences and
            laminin G domains. Transcripts initiating from the downstream
            promoter encode beta isoforms, which lack EGF-like sequences.
            Genetic variation at this locus has been associated with a range of
            behavioral phenotypes, including alcohol dependence and autism
            spectrum disorder. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            contains multiple differences in the coding region, including the
            lack of multiple 5' exons, compared to variant 1. It initiates
            translation at an alternate start codon. The encoded isoform (3) is
            shorter and has a distinct N-terminus, compared to isoform 1. This
            variant encodes a beta isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.68915.1,
                                           SRR1803612.155445.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144835, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3-q31.1"
     Protein         1..459
                     /product="neurexin 3 isoform 3 precursor"
                     /note="neurexin III; neurexin-3-alpha"
                     /calculated_mol_wt=46502
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4221
     mat_peptide     36..459
                     /product="neurexin 3 isoform 3"
                     /calculated_mol_wt=46502
     Region          86..265
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Region          385..441
                     /region_name="Syndecan"
                     /note="Syndecan domain; pfam01034"
                     /db_xref="CDD:460035"
     CDS             1..459
                     /gene="NRXN3"
                     /gene_synonym="C14orf60"
                     /coded_by="NM_001105250.3:913..2292"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS45145.1"
                     /db_xref="GeneID:9369"
                     /db_xref="HGNC:HGNC:8010"
                     /db_xref="MIM:600567"
ORIGIN      
        1 mhlriharrs pprrpawtlg iwflfwgciv ssvwsssnva sssstssspg shsqhehhfh
       61 gskhhsvpis iyrspvslrg ghagatyifg ksgglilytw pandrpstrs drlavgfstt
      121 vkdgilvrid sapglgdflq lhieqgkigv vfnigtvdis ikeertpvnd gkyhvvrftr
      181 nggnatlqvd nwpvnehypt gntdnerfqm vkqkipfkyn rpveewlqek grqltifntq
      241 aqiaiggkdk grlfqgqlsg lyydglkvln maaennpnik ingsvrlvge vpsilgttqt
      301 tsmppemstt vmettttmat tttrknrsta siqptsddlv ssaecssdde dfvecepsta
      361 nptepgirrv pgasevires ssttgmvvgi vaaaalcili llyamykyrn rdegsyqvde
      421 trnyisnsaq sngtlmkekq qssksghkkq knkdreyyv
//
LOCUS       NP_001230154             583 aa            linear   PRI 21-NOV-2025
DEFINITION  pescadillo homolog isoform 2 [Homo sapiens].
ACCESSION   NP_001230154
VERSION     NP_001230154.1
DBSOURCE    REFSEQ: accession NM_001243225.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Zhou,J., Lu,Y., Lin,Y., Li,C., Liu,J., Jiang,Z. and Chen,K.
  TITLE     Overexpression of hepatic pescadillo 1 in obesity induces lipid
            dysregulation by inhibiting autophagy
  JOURNAL   Transl Res 258, 1-15 (2023)
   PUBMED   36775058
  REMARK    GeneRIF: Overexpression of hepatic pescadillo 1 in obesity induces
            lipid dysregulation by inhibiting autophagy.
REFERENCE   3  (residues 1 to 583)
  AUTHORS   He,Y., Xiang,J., Li,Y., Huang,W., Gu,F., Wang,Y. and Chen,R.
  TITLE     PES1 is a biomarker of head and neck squamous cell carcinoma and is
            associated with the tumor microenvironment
  JOURNAL   Cancer Med 12 (11), 12622-12638 (2023)
   PUBMED   37076985
  REMARK    GeneRIF: PES1 is a biomarker of head and neck squamous cell
            carcinoma and is associated with the tumor microenvironment.
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Li,D., Yao,C., Ding,Z., Liu,P., Chen,X., Liu,W., Yi,F., Jiang,C.,
            Li,H., Liu,Y. and Wu,J.
  TITLE     Pescadillo ribosomal biogenesis factor 1 reduction suppresses
            tumour growth and renders chemosensitivity of head and neck
            squamous cell carcinoma
  JOURNAL   Cancer Med 12 (5), 5703-5717 (2023)
   PUBMED   36217758
  REMARK    GeneRIF: Pescadillo ribosomal biogenesis factor 1 reduction
            suppresses tumour growth and renders chemosensitivity of head and
            neck squamous cell carcinoma.
REFERENCE   5  (residues 1 to 583)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 583)
  AUTHORS   Li,J., Yu,L., Zhang,H., Wu,J., Yuan,J., Li,X. and Li,M.
  TITLE     Down-regulation of pescadillo inhibits proliferation and
            tumorigenicity of breast cancer cells
  JOURNAL   Cancer Sci 100 (12), 2255-2260 (2009)
   PUBMED   19764998
  REMARK    GeneRIF: pescadillo might play a role in promoting the
            proliferation and carcinogenesis of human breast cancer, and
            thereby might be a potential target for human breast cancer
            treatment.
            Erratum:[Cancer Sci. 2021 Nov;112(11):4812. doi: 10.1111/cas.15148.
            PMID: 34766426]
REFERENCE   7  (residues 1 to 583)
  AUTHORS   Oeffinger,M., Leung,A., Lamond,A. and Tollervey,D.
  TITLE     Yeast Pescadillo is required for multiple activities during 60S
            ribosomal subunit synthesis
  JOURNAL   RNA 8 (5), 626-636 (2002)
   PUBMED   12022229
  REMARK    Erratum:[RNA 2002 Jun;8(6):851. Lueng Anthony [corrected to Leung
            Anthony]]
REFERENCE   8  (residues 1 to 583)
  AUTHORS   Suzuki,Y., Tsunoda,T., Sese,J., Taira,H., Mizushima-Sugano,J.,
            Hata,H., Ota,T., Isogai,T., Tanaka,T., Nakamura,Y., Suyama,A.,
            Sakaki,Y., Morishita,S., Okubo,K. and Sugano,S.
  TITLE     Identification and characterization of the potential promoter
            regions of 1031 kinds of human genes
  JOURNAL   Genome Res 11 (5), 677-684 (2001)
   PUBMED   11337467
REFERENCE   9  (residues 1 to 583)
  AUTHORS   Kinoshita,Y., Jarell,A.D., Flaman,J.M., Foltz,G., Schuster,J.,
            Sopher,B.L., Irvin,D.K., Kanning,K., Kornblum,H.I., Nelson,P.S.,
            Hieter,P. and Morrison,R.S.
  TITLE     Pescadillo, a novel cell cycle regulatory protein abnormally
            expressed in malignant cells
  JOURNAL   J Biol Chem 276 (9), 6656-6665 (2001)
   PUBMED   11071894
REFERENCE   10 (residues 1 to 583)
  AUTHORS   Allende,M.L., Amsterdam,A., Becker,T., Kawakami,K., Gaiano,N. and
            Hopkins,N.
  TITLE     Insertional mutagenesis in zebrafish identifies two novel genes,
            pescadillo and dead eye, essential for embryonic development
  JOURNAL   Genes Dev 10 (24), 3141-3155 (1996)
   PUBMED   8985183
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU098520.1, CR456539.1 and
            BQ576244.1.
            
            Summary: This gene encodes a nuclear protein that contains a breast
            cancer associated gene 1 (BRCA1) C-terminal interaction domain. The
            encoded protein interacts with BOP1 and WDR12 to form the PeBoW
            complex, which plays a critical role in cell proliferation via
            pre-rRNA processing and 60S ribosomal subunit maturation.
            Expression of this gene may play an important role in breast cancer
            proliferation and tumorigenicity. Alternatively spliced transcript
            variants encoding multiple isoforms have been observed for this
            gene. Pseudogenes of this gene are located on the long arm of
            chromosome 4 and the short arm of chromosome 9. [provided by
            RefSeq, Aug 2011].
            
            Transcript Variant: This variant (3) uses an alternate splice site
            in the coding region but maintains the reading frame, compared to
            variant 1. The encoded isoform (2) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR456539.1, SRR7346977.1143067.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..583
                     /product="pescadillo homolog isoform 2"
                     /note="pescadillo homolog 1, containing BRCT domain"
                     /calculated_mol_wt=67325
     Region          1..257
                     /region_name="Sufficient for nucleolar localization"
                     /note="propagated from UniProtKB/Swiss-Prot (O00541.1)"
     Region          1..54
                     /region_name="Required for 28S ribosomal RNA processing"
                     /note="propagated from UniProtKB/Swiss-Prot (O00541.1)"
     Region          6..579
                     /region_name="NOP7"
                     /note="Protein required for biogenesis of the 60S
                     ribosomal subunit [Translation, ribosomal structure and
                     biogenesis]; COG5163"
                     /db_xref="CDD:227492"
     Region          9..278
                     /region_name="Pescadillo_N"
                     /note="Pescadillo N-terminus; pfam06732"
                     /db_xref="CDD:461996"
     Site            98
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O00541.1)"
     Region          443..510
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00541.1)"
     Region          534..583
                     /region_name="Required for 28S ribosomal RNA processing"
                     /note="propagated from UniProtKB/Swiss-Prot (O00541.1)"
     Region          560..583
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00541.1)"
     CDS             1..583
                     /gene="PES1"
                     /gene_synonym="NOP7; PES"
                     /coded_by="NM_001243225.2:78..1829"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58802.1"
                     /db_xref="GeneID:23481"
                     /db_xref="HGNC:HGNC:8848"
                     /db_xref="MIM:605819"
ORIGIN      
        1 mgglekkkye rgsatnyitr nkarkklqls ladfrrlcil kgiyphepkh kkkvnkgsta
       61 artfylikdi rfllhepivn kfreykvfvr klrkaygkse wntverlkdn kpnykldhii
      121 keryptfida lrdlddalsm cflfstfprt gkchvqtiql crrltvefmh yiiaaralrk
      181 vflsikgiyy qaevlgqpiv witpyafshd hptdvdyrvm atftefyttl lgfvnfrlyq
      241 llnlhyppkl egqaqaeaka gegtyaldse scmeklaals aslarvvvpa teeeaevdef
      301 ptdgeedrrk eleaqekhkk lfeglkffln revprealaf iirsfggevs wdkslcigat
      361 ydvtdsrith qivdrpgqqt svigrcyvqp qwvfdsvnar lllpvaeyfs gvqlpphlsp
      421 fvtekegdyv ppeklkllal qrgedpgnln eseeeeeedd nnegdgdeeg eneeeeedae
      481 agsekeeear laaleeqrme gkkprvmagt lkledkqrla qeeeseakrl aimmmkkrek
      541 ylyqkimfgk rrkireankl aekrkahdea vrsekkakka rpe
//
LOCUS       NP_001365779             243 aa            linear   PRI 21-NOV-2025
DEFINITION  myeloid leukemia factor 1 isoform 10 [Homo sapiens].
ACCESSION   NP_001365779
VERSION     NP_001365779.1
DBSOURCE    REFSEQ: accession NM_001378850.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Tang,Z., Yang,Y., Chen,W. and Liang,T.
  TITLE     Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling
  JOURNAL   Hepatol Commun 7 (8), e0204 (2023)
   PUBMED   37486965
  REMARK    GeneRIF: Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Huang,D., Liu,C., Sun,X., Sun,X., Qu,Y., Tang,Y., Li,G. and Tong,T.
  TITLE     CRL4DCAF8 and USP11 oppositely regulate the stability of myeloid
            leukemia factors (MLFs)
  JOURNAL   Biochem Biophys Res Commun 529 (2), 127-132 (2020)
   PUBMED   32703400
  REMARK    GeneRIF: CRL4(DCAF8) and USP11 oppositely regulate the stability of
            myeloid leukemia factors (MLFs).
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Darracq,A., Pak,H., Bourgoin,V., Zmiri,F., Dellaire,G., Affar,E.B.
            and Milot,E.
  TITLE     NPM and NPM-MLF1 interact with chromatin remodeling complexes and
            influence their recruitment to specific genes
  JOURNAL   PLoS Genet 15 (11), e1008463 (2019)
   PUBMED   31675375
  REMARK    GeneRIF: the abnormal gene regulation imposed by NPM-MLF1 can be
            characterized by the enhanced recruitment of NuRD to gene
            regulatory regions. Thus, different mechanisms would orchestrate
            the dysregulation of NPM function in NPMc+- versus
            NPM1-MLF1-associated leukemia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Yoneda-Kato,N., Tomoda,K., Umehara,M., Arata,Y. and Kato,J.Y.
  TITLE     Myeloid leukemia factor 1 regulates p53 by suppressing COP1 via
            COP9 signalosome subunit 3
  JOURNAL   EMBO J 24 (9), 1739-1749 (2005)
   PUBMED   15861129
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Hanissian,S.H., Akbar,U., Teng,B., Janjetovic,Z., Hoffmann,A.,
            Hitzler,J.K., Iscove,N., Hamre,K., Du,X., Tong,Y., Mukatira,S.,
            Robertson,J.H. and Morris,S.W.
  TITLE     cDNA cloning and characterization of a novel gene encoding the
            MLF1-interacting protein MLF1IP
  JOURNAL   Oncogene 23 (20), 3700-3707 (2004)
   PUBMED   15116101
REFERENCE   8  (residues 1 to 243)
  AUTHORS   Arber,D.A., Chang,K.L., Lyda,M.H., Bedell,V., Spielberger,R. and
            Slovak,M.L.
  TITLE     Detection of NPM/MLF1 fusion in t(3;5)-positive acute myeloid
            leukemia and myelodysplasia
  JOURNAL   Hum Pathol 34 (8), 809-813 (2003)
   PUBMED   14506644
  REMARK    GeneRIF: These findings suggest that an NPM/MLF1 fusion is the
            primary molecular abnormality in t(3;5) MDS and AML with
            multilineage dysplasia, and that cases with NPM/MLF1 may be
            clinically distinct from other MDS-associated disease
REFERENCE   9  (residues 1 to 243)
  AUTHORS   Lim,R., Winteringham,L.N., Williams,J.H., McCulloch,R.K.,
            Ingley,E., Tiao,J.Y., Lalonde,J.P., Tsai,S., Tilbrook,P.A., Sun,Y.,
            Wu,X., Morris,S.W. and Klinken,S.P.
  TITLE     MADM, a novel adaptor protein that mediates phosphorylation of the
            14-3-3 binding site of myeloid leukemia factor 1
  JOURNAL   J Biol Chem 277 (43), 40997-41008 (2002)
   PUBMED   12176995
  REMARK    GeneRIF: phosphorylation of 14-3-3 binding site by MADM
REFERENCE   10 (residues 1 to 243)
  AUTHORS   Yoneda-Kato,N., Look,A.T., Kirstein,M.N., Valentine,M.B.,
            Raimondi,S.C., Cohen,K.J., Carroll,A.J. and Morris,S.W.
  TITLE     The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid
            leukemia produces a novel fusion gene, NPM-MLF1
  JOURNAL   Oncogene 12 (2), 265-275 (1996)
   PUBMED   8570204
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106707.9 and AC025033.20.
            
            Summary: This gene encodes an oncoprotein which is thought to play
            a role in the phenotypic determination of hemopoetic cells.
            Translocations between this gene and nucleophosmin have been
            associated with myelodysplastic syndrome and acute myeloid
            leukemia. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.307578.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMN03267757
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.32"
     Protein         1..243
                     /product="myeloid leukemia factor 1 isoform 10"
                     /note="myelodysplasia-myeloid leukemia factor 1; testis
                     tissue sperm-binding protein Li 49e"
                     /calculated_mol_wt=27524
     Region          1..177
                     /region_name="Mlf1IP"
                     /note="Myelodysplasia-myeloid leukemia factor
                     1-interacting protein; pfam10248"
                     /db_xref="CDD:463022"
     CDS             1..243
                     /gene="MLF1"
                     /coded_by="NM_001378850.1:108..839"
                     /note="isoform 10 is encoded by transcript variant 16"
                     /db_xref="GeneID:4291"
                     /db_xref="HGNC:HGNC:7125"
                     /db_xref="MIM:601402"
ORIGIN      
        1 mfrmlnssfe ddpffshtgg ltlqqlklkh kkplelssgh htdvssfqtm dqmvsnmrny
       61 mqklernfgq lsvdpnghsf csssvmtysk igdeppkvfq astqtrrapg giketrkamr
      121 dsdsglekma ighhihdrah vikksknkkt gdeevnqefi nmnesdahaf deewqsevlk
      181 ykpgrhnlgn trmrsvghen pgsrelkrre kpqqspaieh grrsnvlgdk lhikgssvks
      241 nkk
//
LOCUS       NP_001341216            1782 aa            linear   PRI 21-NOV-2025
DEFINITION  signal-induced proliferation-associated 1-like protein 1 isoform 3
            [Homo sapiens].
ACCESSION   NP_001341216 XP_016876681
VERSION     NP_001341216.1
DBSOURCE    REFSEQ: accession NM_001354287.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1782)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   2  (residues 1 to 1782)
  AUTHORS   Bentley,S.R., Guella,I., Sherman,H.E., Neuendorf,H.M., Sykes,A.M.,
            Fowdar,J.Y., Silburn,P.A., Wood,S.A., Farrer,M.J. and Mellick,G.D.
  TITLE     Hunting for Familial Parkinson's Disease Mutations in the Post
            Genome Era
  JOURNAL   Genes (Basel) 12 (3), 430 (2021)
   PUBMED   33802862
  REMARK    GeneRIF: Hunting for Familial Parkinson's Disease Mutations in the
            Post Genome Era.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1782)
  AUTHORS   Dolnik,A., Kanwal,N., Mackert,S., Halbedl,S., Proepper,C.,
            Bockmann,J., Schoen,M., Boeckers,T.M., Kuhl,S.J. and
            Schmeisser,M.J.
  TITLE     Sipa1l3/SPAR3 is targeted to postsynaptic specializations and
            interacts with the Fezzin ProSAPiP1/Lzts3
  JOURNAL   J Neurochem 136 (1), 28-35 (2016)
   PUBMED   26364583
  REMARK    GeneRIF: Sipa1L1 is conserved across species, has a distinct
            expression pattern in brain and is localized to excitatory
            postsynapses.
REFERENCE   4  (residues 1 to 1782)
  AUTHORS   Quillen,E.E., Chen,X.D., Almasy,L., Yang,F., He,H., Li,X.,
            Wang,X.Y., Liu,T.Q., Hao,W., Deng,H.W., Kranzler,H.R. and
            Gelernter,J.
  TITLE     ALDH2 is associated to alcohol dependence and is the major genetic
            determinant of 'daily maximum drinks' in a GWAS study of an
            isolated rural Chinese sample
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 165B (2), 103-110 (2014)
   PUBMED   24277619
REFERENCE   5  (residues 1 to 1782)
  AUTHORS   Neveu,G., Cassonnet,P., Vidalain,P.O., Rolloy,C., Mendoza,J.,
            Jones,L., Tangy,F., Muller,M., Demeret,C., Tafforeau,L.,
            Lotteau,V., Rabourdin-Combe,C., Trave,G., Dricot,A., Hill,D.E.,
            Vidal,M., Favre,M. and Jacob,Y.
  TITLE     Comparative analysis of virus-host interactomes with a mammalian
            high-throughput protein complementation assay based on Gaussia
            princeps luciferase
  JOURNAL   Methods 58 (4), 349-359 (2012)
   PUBMED   22898364
REFERENCE   6  (residues 1 to 1782)
  AUTHORS   Benzinger,A., Muster,N., Koch,H.B., Yates,J.R. 3rd and Hermeking,H.
  TITLE     Targeted proteomic analysis of 14-3-3 sigma, a p53 effector
            commonly silenced in cancer
  JOURNAL   Mol Cell Proteomics 4 (6), 785-795 (2005)
   PUBMED   15778465
REFERENCE   7  (residues 1 to 1782)
  AUTHORS   Chih,D.Y., Park,D.J., Gross,M., Idos,G., Vuong,P.T., Hirama,T.,
            Chumakov,A.M., Said,J. and Koeffler,H.P.
  TITLE     Protein partners of C/EBPepsilon
  JOURNAL   Exp Hematol 32 (12), 1173-1181 (2004)
   PUBMED   15588942
REFERENCE   8  (residues 1 to 1782)
  AUTHORS   Lu,Z., Hu,X., Li,Y., Zheng,L., Zhou,Y., Jiang,H., Ning,T.,
            Basang,Z., Zhang,C. and Ke,Y.
  TITLE     Human papillomavirus 16 E6 oncoprotein interferences with insulin
            signaling pathway by binding to tuberin
  JOURNAL   J Biol Chem 279 (34), 35664-35670 (2004)
   PUBMED   15175323
REFERENCE   9  (residues 1 to 1782)
  AUTHORS   Pak,D.T., Yang,S., Rudolph-Correia,S., Kim,E. and Sheng,M.
  TITLE     Regulation of dendritic spine morphology by SPAR, a
            PSD-95-associated RapGAP
  JOURNAL   Neuron 31 (2), 289-303 (2001)
   PUBMED   11502259
REFERENCE   10 (residues 1 to 1782)
  AUTHORS   Gao,Q., Srinivasan,S., Boyer,S.N., Wazer,D.E. and Band,V.
  TITLE     The E6 oncoproteins of high-risk papillomaviruses bind to a novel
            putative GAP protein, E6TP1, and target it for degradation
  JOURNAL   Mol Cell Biol 19 (1), 733-744 (1999)
   PUBMED   9858596
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005476.4, AC004968.1, DA330003.1, AK122930.1, AC004974.1,
            AF090989.1 and AC004900.2.
            
            On Aug 29, 2017 this sequence version replaced XP_016876681.1.
            
            Transcript Variant: This variant (7) differs in the 5' UTR, lacks
            an alternate in-frame exon, uses an alternate in-frame splice site,
            compared to variant 1. The encoded isoform (3) is shorter than
            isoform 1. Variants 3, 6, 7, and 8 encode the same isoform (3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803617.274247.1, SRR7346977.2550920.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968540, SAMEA1970526 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1782
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.2"
     Protein         1..1782
                     /product="signal-induced proliferation-associated 1-like
                     protein 1 isoform 3"
                     /note="signal-induced proliferation-associated 1-like
                     protein 1; SIPA1-like protein 1; high-risk human papilloma
                     viruses E6 oncoproteins targeted protein 1;
                     spine-associated RapGAP 1"
                     /calculated_mol_wt=197278
     Region          1..157
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Region          277..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Region          380..401
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Region          629..809
                     /region_name="Rap_GAP"
                     /note="Rap/ran-GAP; pfam02145"
                     /db_xref="CDD:460463"
     Region          953..1025
                     /region_name="PDZ_SIPA1-like"
                     /note="PDZ domain of signal-induced
                     proliferation-associated protein 1 (SIPA1), and related
                     domains; cd06745"
                     /db_xref="CDD:467227"
     Site            order(963..969,975,978,1007,1011,1014..1015)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467227"
     Region          1067..1128
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            1078
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1087
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Region          1144..1207
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            1149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1181
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Region          1247..1285
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            1249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1305
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:O35412; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Region          1306..1345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            1309
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:O35412; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1328
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5.
                     /evidence=ECO:0000250|UniProtKB:O35412; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Region          1358..1454
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            1369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Region          1483..1727
                     /region_name="SPAR_C"
                     /note="C-terminal domain of SPAR protein; pfam11881"
                     /db_xref="CDD:463383"
     Region          1484..1515
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            1507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            1530
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1533
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1564
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O43166.4)"
     Site            1567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1580
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1582
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1629
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1690
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1707
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0T5; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Site            1712
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43166.4)"
     Region          1715..1770
                     /region_name="ZapB"
                     /note="Cell division protein ZapB; pfam06005"
                     /db_xref="CDD:428718"
     CDS             1..1782
                     /gene="SIPA1L1"
                     /gene_synonym="E6TP1; SPAR1"
                     /coded_by="NM_001354287.2:553..5901"
                     /note="isoform 3 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS61491.1"
                     /db_xref="GeneID:26037"
                     /db_xref="HGNC:HGNC:20284"
                     /db_xref="MIM:617504"
ORIGIN      
        1 mtslkrsqte rplatdrasv vgtdgtpkvh tddfymrrfr sqngslgssv mapvgpprse
       61 gshhitstpg vpkmgvrari adwpprkeni kessrssqei etsscldsls sksspvsqgs
      121 svslnsndsa mlksiqntlk nktrpsenmd srflmpeayp ssprkalrri rqrsnsditi
      181 seldvdsfde cisptyktgp slhreygsts sidkqgtsge sffdllkgyk ddksdrgptp
      241 tklsdflitg ggkgsgfsld vidgpisqre nlrlfkerek plkrrskset gdssifrklr
      301 nakgeelgks sdlednrsed svrpwtcpkc fahydvqsil fdlneaimnr hnvikrrntt
      361 tgasaaavas lvsgplshsa sfsspmgste dlnskgslsm dqgddksnel vmscpyfrne
      421 iggegerkis lsksnsgsfs gcesasfest lsshctnagv avlevpkenl vlhldrvkry
      481 ivehvdlgay yyrkffyqke hwnyfgaden lgpvavsirr ekpdemkeng spynyriifr
      541 tselmtlrgs vledaipsta khstarglpl kevlehvvpe lnvqclrlaf ntpkvteqlm
      601 kldeqglnyq qkvgimycka gqsteeemyn nesagpafee flqllgervr lkgfekyraq
      661 ldtktdstgt hslyttykdy eimfhvstml pytpnnkqql lrkrhigndi vtivfqepga
      721 qpfspknirs hfqhvfvivr vhnpcsdsvc ysvavtrsrd vpsfgppipk gvtfpksnvf
      781 rdfllakvin aenaahksek framatrtrq eylkdlaekn vtntpidpsg kfpfislask
      841 kkekskpypg aelssmgaiv wavraedynk ameldcllgi snefivlieq etksvvfncs
      901 crdvigwtst dtslkifyer gecvsvgsfi nieeikeivk rlqfvskgce svemtlrrng
      961 lgqlgfhvny egivadvepy gyawqaglrq gsrlveickv avatlsheqm idllrtsvtv
     1021 kvviipphdd ctprrscset yrmpvmeykm negvsyefkf pfrnnnkwqr naskgphspq
     1081 vpsqvqspmt srlnagkgdg kmppperaan iprsissdgr plerrlspgs diyvtvssma
     1141 larsqcrnsp snlssssdtg svggtyrqks mpegfgvsrr spasidrqnt qsdiggsgks
     1201 tpswqrseds iadqmeptch lpavskvlpa frespsgrlm rqdpvvhlsp nkqghsdshy
     1261 sshsssntls snassahsde kwydgdrtes elnsynylqg tsadsgidtt sygpshgsta
     1321 slgaatsspr sgpgkekvap lwhsssevis madrtletes hgldrktess lsldihsksq
     1381 agstpltren stfsindaas htstmssrhs aspvvftsar sspkeelhpa apsqlapsfs
     1441 sssssssgpr sfyprqgats kyligwkkpe gtinsvgfmd trkrhqsdgn eiahtrlras
     1501 trdlraspkp tskstieedl kklidlespt pesqksfkfh alsspqspfp stptsrralh
     1561 rtlsdesiyn sqrehfftsr aslldqalpn dvlfsstyps lpkslplrrp sytlgmkslh
     1621 gefsasdssl tdiqetrrqp mpdpglmplp dtaadldwsn lvdaakayev qrasffaasd
     1681 enhrplsaas nsdqledqal aqmkpysskd ssptlaskvd qlegmlkmlr edlkkekedk
     1741 ahlqaevqhl rednlrlqee sqnasdklkk ftewvfntid ms
//
LOCUS       NP_938074                353 aa            linear   PRI 21-NOV-2025
DEFINITION  protein arginine N-methyltransferase 1 isoform 3 [Homo sapiens].
ACCESSION   NP_938074
VERSION     NP_938074.2
DBSOURCE    REFSEQ: accession NM_198318.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Walton,J., Ng,A.S.N., Arevalo,K., Apostoli,A., Meens,J.,
            Karamboulas,C., St-Germain,J., Prinos,P., Dmytryshyn,J., Chen,E.,
            Arrowsmith,C.H., Raught,B. and Ailles,L.
  TITLE     PRMT1 inhibition perturbs RNA metabolism and induces DNA damage in
            clear cell renal cell carcinoma
  JOURNAL   Nat Commun 15 (1), 8232 (2024)
   PUBMED   39300069
  REMARK    GeneRIF: PRMT1 inhibition perturbs RNA metabolism and induces DNA
            damage in clear cell renal cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Wang,H., Li,Y., Wu,N., Lv,C. and Wang,Y.
  TITLE     P4HB regulates the TGFbeta/SMAD3 signaling pathway through PRMT1 to
            participate in high glucose-induced epithelial-mesenchymal
            transition and fibrosis of renal tubular epithelial cells
  JOURNAL   BMC Nephrol 25 (1), 297 (2024)
   PUBMED   39251943
  REMARK    GeneRIF: P4HB regulates the TGFbeta/SMAD3 signaling pathway through
            PRMT1 to participate in high glucose-induced epithelial-mesenchymal
            transition and fibrosis of renal tubular epithelial cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Yoshimatsu,M., Toyokawa,G., Hayami,S., Unoki,M., Tsunoda,T.,
            Field,H.I., Kelly,J.D., Neal,D.E., Maehara,Y., Ponder,B.A.,
            Nakamura,Y. and Hamamoto,R.
  TITLE     Dysregulation of PRMT1 and PRMT6, Type I arginine
            methyltransferases, is involved in various types of human cancers
  JOURNAL   Int J Cancer 128 (3), 562-573 (2011)
   PUBMED   20473859
  REMARK    GeneRIF: PRMT1 may be involved in human carcinogenesis and may thus
            be a therapeutic target for various types of cancer.
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Scorilas,A., Black,M.H., Talieri,M. and Diamandis,E.P.
  TITLE     Genomic organization, physical mapping, and expression analysis of
            the human protein arginine methyltransferase 1 gene
  JOURNAL   Biochem Biophys Res Commun 278 (2), 349-359 (2000)
   PUBMED   11097842
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Abramovich,C., Yakobson,B., Chebath,J. and Revel,M.
  TITLE     A protein-arginine methyltransferase binds to the intracytoplasmic
            domain of the IFNAR1 chain in the type I interferon receptor
  JOURNAL   EMBO J 16 (2), 260-266 (1997)
   PUBMED   9029147
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Hoodless,P.A., Haerry,T., Abdollah,S., Stapleton,M., O'Connor,M.B.,
            Attisano,L. and Wrana,J.L.
  TITLE     MADR1, a MAD-related protein that functions in BMP2 signaling
            pathways
  JOURNAL   Cell 85 (4), 489-500 (1996)
   PUBMED   8653785
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Rajpurohit,R., Lee,S.O., Park,J.O., Paik,W.K. and Kim,S.
  TITLE     Enzymatic methylation of recombinant heterogeneous nuclear RNP
            protein A1. Dual substrate specificity for
            S-adenosylmethionine:histone-arginine N-methyltransferase
  JOURNAL   J Biol Chem 269 (2), 1075-1082 (1994)
   PUBMED   8288564
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Baldwin,G.S. and Carnegie,P.R.
  TITLE     Specific enzymic methylation of an arginine in the experimental
            allergic encephalomyelitis protein from human myelin
  JOURNAL   Science 171 (3971), 579-581 (1971)
   PUBMED   4924231
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC421815.1 and Y10807.1.
            
            On Jul 6, 2007 this sequence version replaced NP_938074.1.
            
            Summary: This gene encodes a member of the protein arginine
            N-methyltransferase (PRMT) family. Post-translational modification
            of target proteins by PRMTs plays an important regulatory role in
            many biological processes, whereby PRMTs methylate arginine
            residues by transferring methyl groups from S-adenosyl-L-methionine
            to terminal guanidino nitrogen atoms. The encoded protein is a type
            I PRMT and is responsible for the majority of cellular arginine
            methylation activity. Increased expression of this gene may play a
            role in many types of cancer. Alternatively spliced transcript
            variants encoding multiple isoforms have been observed for this
            gene, and a pseudogene of this gene is located on the long arm of
            chromosome 5. [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (3) lacks an exon in the coding
            region, but maintains the reading frame, compared to variant 1. The
            encoded isoform (3) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC019268.1, AK304660.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..353
                     /product="protein arginine N-methyltransferase 1 isoform
                     3"
                     /EC_number="2.1.1.319"
                     /note="HMT1 (hnRNP methyltransferase, S. cerevisiae)-like
                     2; protein arginine N-methyltransferase 1; interferon
                     receptor 1-bound protein 4; histone-arginine
                     N-methyltransferase PRMT1; heterogeneous nuclear
                     ribonucleoprotein methyltransferase 1-like 2; highly
                     conserved protein 1"
                     /calculated_mol_wt=40418
     Region          45..>218
                     /region_name="COG4076"
                     /note="Predicted RNA methylase [General function
                     prediction only]"
                     /db_xref="CDD:443253"
     CDS             1..353
                     /gene="PRMT1"
                     /gene_synonym="ANM1; HCP1; HRMT1L2; IR1B4"
                     /coded_by="NM_198318.5:11..1072"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS42592.1"
                     /db_xref="GeneID:3276"
                     /db_xref="HGNC:HGNC:5187"
                     /db_xref="MIM:602950"
ORIGIN      
        1 maaaeaanci mevscgqaes sekpnaedmt skdyyfdsya hfgiheemlk devrtltyrn
       61 smfhnrhlfk dkvvldvgsg tgilcmfaak agarkvigie cssisdyavk ivkankldhv
      121 vtiikgkvee velpvekvdi iisewmgycl fyesmlntvl yardkwlapd glifpdratl
      181 yvtaiedrqy kdykihwwen vygfdmscik dvaikeplvd vvdpkqlvtn aclikevdiy
      241 tvkvedltft spfclqvkrn dyvhalvayf nieftrchkr tgfstspesp ythwkqtvfy
      301 medyltvktg eeifgtigmr pnaknnrdld ftidldfkgq lcelscstdy rmr
//
LOCUS       NP_001186512             444 aa            linear   PRI 21-NOV-2025
DEFINITION  protein kinase C and casein kinase substrate in neurons protein 1
            [Homo sapiens].
ACCESSION   NP_001186512
VERSION     NP_001186512.1
DBSOURCE    REFSEQ: accession NM_001199583.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Liu,Z., Li,X., Muhammad,A., Sun,Q., Zhang,Q., Wang,Y., Wang,Y.,
            Ren,J. and Wang,D.
  TITLE     PACSIN1 promotes immunosuppression in gastric cancer by degrading
            MHC-I
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 56 (10), 1473-1482 (2024)
   PUBMED   38826133
  REMARK    GeneRIF: PACSIN1 promotes immunosuppression in gastric cancer by
            degrading MHC-I.
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Xie,C., Zhou,H., Athanasopoulos,V., Shen,Q., Zhang,Y., Meng,X.,
            Burgio,G., Arsov,T., Lungu,A.C., Zhang,P., Qin,Y., Ma,J., Wu,X.,
            Jiang,X., Ding,H., Meng,Y., Shen,N., He,Y. and Vinuesa,C.G.
  TITLE     De Novo PACSIN1 Gene Variant Found in Childhood Lupus and a Role
            for PACSIN1/TRAF4 Complex in Toll-like Receptor 7 Activation
  JOURNAL   Arthritis Rheumatol 75 (6), 1058-1071 (2023)
   PUBMED   36622335
  REMARK    GeneRIF: De Novo PACSIN1 Gene Variant Found in Childhood Lupus and
            a Role for PACSIN1/TRAF4 Complex in Toll-like Receptor 7
            Activation.
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Regan,P., Mitchell,S.J., Kim,S.C., Lee,Y., Yi,J.H., Barbati,S.A.,
            Shaw,C. and Cho,K.
  TITLE     Regulation of Synapse Weakening through Interactions of the
            Microtubule Associated Protein Tau with PACSIN1
  JOURNAL   J Neurosci 41 (34), 7162-7170 (2021)
   PUBMED   34290082
  REMARK    GeneRIF: Regulation of Synapse Weakening through Interactions of
            the Microtubule Associated Protein Tau with PACSIN1.
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Zucconi,A., Dente,L., Santonico,E., Castagnoli,L. and Cesareni,G.
  TITLE     Selection of ligands by panning of domain libraries displayed on
            phage lambda reveals new potential partners of synaptojanin 1
  JOURNAL   J Mol Biol 307 (5), 1329-1339 (2001)
   PUBMED   11292345
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Sumoy,L., Pluvinet,R., Andreu,N., Estivill,X. and Escarceller,M.
  TITLE     PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the
            pacsin-syndapin-FAP52 gene family
  JOURNAL   Gene 262 (1-2), 199-205 (2001)
   PUBMED   11179684
REFERENCE   8  (residues 1 to 444)
  AUTHORS   Modregger,J., Ritter,B., Witter,B., Paulsson,M. and Plomann,M.
  TITLE     All three PACSIN isoforms bind to endocytic proteins and inhibit
            endocytosis
  JOURNAL   J Cell Sci 113 Pt 24, 4511-4521 (2000)
   PUBMED   11082044
REFERENCE   9  (residues 1 to 444)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 444)
  AUTHORS   Qualmann,B., Roos,J., DiGregorio,P.J. and Kelly,R.B.
  TITLE     Syndapin I, a synaptic dynamin-binding protein that associates with
            the neural Wiskott-Aldrich syndrome protein
  JOURNAL   Mol Biol Cell 10 (2), 501-513 (1999)
   PUBMED   9950691
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP251080.1, BC040228.1 and AL157372.18.
            
            Transcript Variant: This variant (2) has an alternate 5' UTR exon
            and encodes the same protein as variant 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC040228.1, SRR14372080.3131079.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..444
                     /product="protein kinase C and casein kinase substrate in
                     neurons protein 1"
                     /note="syndapin I; syndapin-1"
                     /calculated_mol_wt=50835
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0W5; propagated from
                     UniProtKB/Swiss-Prot (Q9BY11.1)"
     Region          19..276
                     /region_name="F-BAR_PACSIN1"
                     /note="The F-BAR (FES-CIP4 Homology and
                     Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein
                     kinase Substrate in Neurons 1 (PACSIN1); cd07680"
                     /db_xref="CDD:153364"
     Site            order(19..21,27..28,31,34,37..38,41..42,44..45,48..49,
                     52..53,55..56,59..60,63,66..67,84,87,90,98,146,150,157,
                     160..161,164..165,209,213,224,228,231,235,238..239,
                     241..242,245..246,249..250,252..253,256..260,264..265,
                     268..269,271..272,275..276)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153364"
     Site            order(26,30,36,47,51,54,65..66,73,102,114,133,140..141,
                     148..149,151,158,204,208,211)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153364"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0W5; propagated from
                     UniProtKB/Swiss-Prot (Q9BY11.1)"
     Region          175..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BY11.1)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0W5; propagated from
                     UniProtKB/Swiss-Prot (Q9BY11.1)"
     Region          309..386
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BY11.1)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61644; propagated from
                     UniProtKB/Swiss-Prot (Q9BY11.1)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61644; propagated from
                     UniProtKB/Swiss-Prot (Q9BY11.1)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0W5; propagated from
                     UniProtKB/Swiss-Prot (Q9BY11.1)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61644; propagated from
                     UniProtKB/Swiss-Prot (Q9BY11.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0W5; propagated from
                     UniProtKB/Swiss-Prot (Q9BY11.1)"
     Region          388..443
                     /region_name="SH3_PACSIN1-2"
                     /note="Src homology 3 domain of Protein kinase C and
                     Casein kinase Substrate in Neurons 1 (PACSIN1) and PACSIN
                     2; cd11998"
                     /db_xref="CDD:212931"
     Site            order(394,396,399,403,422..423,437,439..440)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212931"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q61644; propagated from
                     UniProtKB/Swiss-Prot (Q9BY11.1)"
     Site            405
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61644; propagated from
                     UniProtKB/Swiss-Prot (Q9BY11.1)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61644; propagated from
                     UniProtKB/Swiss-Prot (Q9BY11.1)"
     CDS             1..444
                     /gene="PACSIN1"
                     /gene_synonym="SDPI"
                     /coded_by="NM_001199583.3:261..1595"
                     /db_xref="CCDS:CCDS4793.1"
                     /db_xref="GeneID:29993"
                     /db_xref="HGNC:HGNC:8570"
                     /db_xref="MIM:606512"
ORIGIN      
        1 msssydeasl apeettdsfw evgnykrtvk riddghrlcn dlmncvqera kiekaygqql
       61 tdwakrwrql iekgpqygsl erawgaimte adkvselhqe vknnllnedl ekvknwqkda
      121 yhkqimggfk etkeaedgfr kaqkpwakkm keleaakkay hlackeekla mtremnskte
      181 qsvtpeqqkk lqdkvdkckq dvqktqekye kvledvgktt pqymenmeqv feqcqqfeek
      241 rlvflkevll dikrhlnlae nssyihvyre leqairgada qedlrwfrst sgpgmpmnwp
      301 qfeewnpdlp htttkkekqp kkaegvaltn atgavestsq agdrgsvssy drgqpyatew
      361 sddesgnpfg gsetngganp feddskgvrv ralydydgqe qdelsfkagd eltklgeede
      421 qgwcrgrlds gqlglypany veai
//
LOCUS       NP_001353472             499 aa            linear   PRI 21-NOV-2025
DEFINITION  inositol 1,4,5-triphosphate receptor associated 2 isoform a [Homo
            sapiens].
ACCESSION   NP_001353472 XP_016874790
VERSION     NP_001353472.1
DBSOURCE    REFSEQ: accession NM_001366543.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Okumura,W., Tadahira,K., Kozono,T., Tamura-Nakano,M., Sato,H.,
            Matsui,H., Dohi,T., Rohrer,J., Tonozuka,T. and Nishikawa,A.
  TITLE     Jaw1/LRMP is associated with the maintenance of Golgi ribbon
            structure
  JOURNAL   J Biochem 173 (5), 383-392 (2023)
   PUBMED   36689741
  REMARK    GeneRIF: Jaw1/LRMP is associated with the maintenance of Golgi
            ribbon structure.
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Okumura,W., Kozono,T., Sato,H., Matsui,H., Takagi,T., Tonozuka,T.
            and Nishikawa,A.
  TITLE     Jaw1/LRMP increases Ca2+ influx upon GPCR stimulation with
            heterogeneous effect on the activity of each ITPR subtype
  JOURNAL   Sci Rep 12 (1), 9476 (2022)
   PUBMED   35676525
  REMARK    GeneRIF: Jaw1/LRMP increases Ca(2+) influx upon GPCR stimulation
            with heterogeneous effect on the activity of each ITPR subtype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Cruz,V.E., Esra Demircioglu,F. and Schwartz,T.U.
  TITLE     Structural Analysis of Different LINC Complexes Reveals Distinct
            Binding Modes
  JOURNAL   J Mol Biol 432 (23), 6028-6041 (2020)
   PUBMED   33058875
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Bataille,P., Michaud,V., Robert,M.P., Bekel,L., Leclerc-Mercier,S.,
            Harroche,A., Celerier,C., Lasseaux,E., Borgel,D.,
            Bremond-Gignac,D., Bodemer,C., Arveiler,B. and Hadj-Rabia,S.
  TITLE     Clinical variability and probable founder effect in oculocutaneous
            albinism type 7
  JOURNAL   Clin Genet 97 (3), 527-528 (2020)
   PUBMED   31694064
  REMARK    GeneRIF: Clinical variability and probable founder effect in
            oculocutaneous albinism type 7.
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Kohno,T., Kunitoh,H., Suzuki,K., Yamamoto,S., Kuchiba,A.,
            Matsuno,Y., Yanagitani,N. and Yokota,J.
  TITLE     Association of KRAS polymorphisms with risk for lung adenocarcinoma
            accompanied by atypical adenomatous hyperplasias
  JOURNAL   Carcinogenesis 29 (5), 957-963 (2008)
   PUBMED   18299280
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Manenti,G., Galbiati,F., Pettinicchio,A., Spinola,M., Piconese,S.,
            Leoni,V.P., Conti,B., Ravagnani,F., Incarbone,M., Pastorino,U. and
            Dragani,T.A.
  TITLE     A V141L polymorphism of the human LRMP gene is associated with
            survival of lung cancer patients
  JOURNAL   Carcinogenesis 27 (7), 1386-1390 (2006)
   PUBMED   16410263
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Snyder,H.L., Bacik,I., Bennink,J.R., Kearns,G., Behrens,T.W.,
            Bachi,T., Orlowski,M. and Yewdell,J.W.
  TITLE     Two novel routes of transporter associated with antigen processing
            (TAP)-independent major histocompatibility complex class I antigen
            processing
  JOURNAL   J Exp Med 186 (7), 1087-1098 (1997)
   PUBMED   9314557
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Behrens,T.W., Kearns,G.M., Rivard,J.J., Bernstein,H.D.,
            Yewdell,J.W. and Staudt,L.M.
  TITLE     Carboxyl-terminal targeting and novel post-translational processing
            of JAW1, a lymphoid protein of the endoplasmic reticulum
  JOURNAL   J Biol Chem 271 (38), 23528-23534 (1996)
   PUBMED   8798562
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Behrens,T.W., Jagadeesh,J., Scherle,P., Kearns,G., Yewdell,J. and
            Staudt,L.M.
  TITLE     Jaw1, A lymphoid-restricted membrane protein localized to the
            endoplasmic reticulum
  JOURNAL   J Immunol 153 (2), 682-690 (1994)
   PUBMED   8021504
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC023510.16.
            
            On Oct 11, 2018 this sequence version replaced XP_016874790.1.
            
            Summary: The protein encode dby this gene is expressed in a
            developmentally regulated manner in lymphoid cell lines and
            tissues. The protein is localized to the cytoplasmic face of the
            endoplasmic reticulum. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.4135296.1,
                                           SRR14038194.3033179.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..499
                     /product="inositol 1,4,5-triphosphate receptor associated
                     2 isoform a"
                     /note="protein Jaw1; lymphoid restricted membrane protein"
                     /calculated_mol_wt=56082
     Region          4..499
                     /region_name="MRVI1"
                     /note="MRVI1 protein; pfam05781"
                     /db_xref="CDD:461738"
     CDS             1..499
                     /gene="IRAG2"
                     /gene_synonym="JAW1; LRMP"
                     /coded_by="NM_001366543.2:488..1987"
                     /note="isoform a is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS8701.1"
                     /db_xref="GeneID:4033"
                     /db_xref="HGNC:HGNC:6690"
                     /db_xref="MIM:602003"
ORIGIN      
        1 mnddpsmeen gvervcpesl lqsreysslp lprhtsstdg titssdpgle ilnmascdld
       61 rnslckkeed trsasptiea qgtspahdni afqdstskdk tilnleakee petieehkke
      121 hasgdsvvsp lpvttvksvn lrqsentsan ekeveaeflr lslgfkcdwf tlekrvklee
      181 rsrdlaeenl kkeitnclkl lesltplced dnqaqeiikk leksikflsq caarvasrae
      241 mlgainqesr vskavevmiq hvenlkrmya kehaeleelk qvllqnersf npleddddcq
      301 ikkrsaslns kpsslrrvti aslprnigna gmvagmennd rfsrrssswr ilgskqsehr
      361 pslprfisty swadaeeekc elktkddsep sgeetvertr kpslsekknn pskwdvssvy
      421 dtiaswatnl kssirkanka lwlsiafivl faalmsfltg qlfqksvdaa ptqqedswts
      481 lehilwpftr lrhngpppv
//
LOCUS       NP_001180541             279 aa            linear   PRI 21-NOV-2025
DEFINITION  tubulin delta chain isoform 5 [Homo sapiens].
ACCESSION   NP_001180541
VERSION     NP_001180541.1
DBSOURCE    REFSEQ: accession NM_001193612.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Pudlowski,R., Xu,L., Milenkovic,L., Kumar,C., Hemsworth,K.,
            Aqrabawi,Z., Stearns,T. and Wang,J.T.
  TITLE     A delta-tubulin/epsilon-tubulin/Ted protein complex is required for
            centriole architecture
  JOURNAL   Elife 13, 98704 (2025)
   PUBMED   40067174
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Wang,J.T., Kong,D., Hoerner,C.R., Loncarek,J. and Stearns,T.
  TITLE     Centriole triplet microtubules are required for stable centriole
            formation and inheritance in human cells
  JOURNAL   Elife 6, e29061 (2017)
   PUBMED   28906251
  REMARK    GeneRIF: Here, the authors report that centrioles in delta-tubulin
            and epsilon-tubulin null mutant human cells lack triplet
            microtubules and fail to undergo centriole maturation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Jostins,L., Ripke,S., Weersma,R.K., Duerr,R.H., McGovern,D.P.,
            Hui,K.Y., Lee,J.C., Schumm,L.P., Sharma,Y., Anderson,C.A.,
            Essers,J., Mitrovic,M., Ning,K., Cleynen,I., Theatre,E.,
            Spain,S.L., Raychaudhuri,S., Goyette,P., Wei,Z., Abraham,C.,
            Achkar,J.P., Ahmad,T., Amininejad,L., Ananthakrishnan,A.N.,
            Andersen,V., Andrews,J.M., Baidoo,L., Balschun,T., Bampton,P.A.,
            Bitton,A., Boucher,G., Brand,S., Buning,C., Cohain,A., Cichon,S.,
            D'Amato,M., De Jong,D., Devaney,K.L., Dubinsky,M., Edwards,C.,
            Ellinghaus,D., Ferguson,L.R., Franchimont,D., Fransen,K.,
            Gearry,R., Georges,M., Gieger,C., Glas,J., Haritunians,T., Hart,A.,
            Hawkey,C., Hedl,M., Hu,X., Karlsen,T.H., Kupcinskas,L.,
            Kugathasan,S., Latiano,A., Laukens,D., Lawrance,I.C., Lees,C.W.,
            Louis,E., Mahy,G., Mansfield,J., Morgan,A.R., Mowat,C., Newman,W.,
            Palmieri,O., Ponsioen,C.Y., Potocnik,U., Prescott,N.J.,
            Regueiro,M., Rotter,J.I., Russell,R.K., Sanderson,J.D., Sans,M.,
            Satsangi,J., Schreiber,S., Simms,L.A., Sventoraityte,J.,
            Targan,S.R., Taylor,K.D., Tremelling,M., Verspaget,H.W., De Vos,M.,
            Wijmenga,C., Wilson,D.C., Winkelmann,J., Xavier,R.J., Zeissig,S.,
            Zhang,B., Zhang,C.K., Zhao,H., Silverberg,M.S., Annese,V.,
            Hakonarson,H., Brant,S.R., Radford-Smith,G., Mathew,C.G.,
            Rioux,J.D., Schadt,E.E., Daly,M.J., Franke,A., Parkes,M.,
            Vermeire,S., Barrett,J.C. and Cho,J.H.
  CONSRTM   International IBD Genetics Consortium (IIBDGC)
  TITLE     Host-microbe interactions have shaped the genetic architecture of
            inflammatory bowel disease
  JOURNAL   Nature 491 (7422), 119-124 (2012)
   PUBMED   23128233
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 279)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 279)
  AUTHORS   Kato,A., Nagata,Y. and Todokoro,K.
  TITLE     Delta-tubulin is a component of intercellular bridges and both the
            early and mature perinuclear rings during spermatogenesis
  JOURNAL   Dev Biol 269 (1), 196-205 (2004)
   PUBMED   15081367
REFERENCE   8  (residues 1 to 279)
  AUTHORS   Sidjanin,D.J., Zangerl,B., Johnson,J.L., Xue,F., Mellersh,C.,
            Ostrander,E.A., Acland,G. and Aguirre,G.D.
  TITLE     Cloning of the canine delta tubulin cDNA (TUBD) and mapping to CFA9
  JOURNAL   Anim Genet 33 (2), 161-162 (2002)
   PUBMED   12047234
REFERENCE   9  (residues 1 to 279)
  AUTHORS   Smrzka,O.W., Delgehyr,N. and Bornens,M.
  TITLE     Tissue-specific expression and subcellular localisation of
            mammalian delta-tubulin
  JOURNAL   Curr Biol 10 (7), 413-416 (2000)
   PUBMED   10753753
REFERENCE   10 (residues 1 to 279)
  AUTHORS   Chang,P. and Stearns,T.
  TITLE     Delta-tubulin and epsilon-tubulin: two new human centrosomal
            tubulins reveal new aspects of centrosome structure and function
  JOURNAL   Nat Cell Biol 2 (1), 30-35 (2000)
   PUBMED   10620804
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG682935.1, DA607129.1, AK315172.1, AB030837.1, AK024741.1 and
            BX119803.1.
            
            Transcript Variant: This variant (5) contains an alternate exon in
            the 5' end, which results in the use of a downstream start codon,
            and lacks an alternate, in-frame segment in the 3' coding region,
            compared to variant 1. The resulting protein (isoform 5) has a
            shorter N-terminus when it is compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK315172.1, SRR14038193.1226425.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.1"
     Protein         1..279
                     /product="tubulin delta chain isoform 5"
                     /note="delta-tubulin; tubulin delta chain"
                     /calculated_mol_wt=31351
     Region          <1..278
                     /region_name="delta_zeta_tubulin-like"
                     /note="The delta- and zeta-tubulin families; cd02189"
                     /db_xref="CDD:276958"
     CDS             1..279
                     /gene="TUBD1"
                     /gene_synonym="TUBD"
                     /coded_by="NM_001193612.2:740..1579"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:51174"
                     /db_xref="HGNC:HGNC:16811"
                     /db_xref="MIM:607344"
ORIGIN      
        1 mniirkevek cdsfsgffii msmaggtgsg lgafvtqnle dqysnslkmn qiiwpygtge
       61 vivqnynsil tlshlyrssd alllhendai hkicaklmni kqisfsdinq vlahqlgsvf
      121 qptysaessf hyrrnplgid rhvwpplsgl pplskmslnk dlhfntsian lvilrgkdvq
      181 sadvegfkdp alytswlkpv nafnvwktqr afskyeksav lvsnsqflvk pldmivgkaw
      241 nmfaskayih qytkfgieee dfldsftsle qvvasycnl
//
LOCUS       NP_001305445             213 aa            linear   PRI 21-NOV-2025
DEFINITION  toll-interacting protein isoform 4 [Homo sapiens].
ACCESSION   NP_001305445
VERSION     NP_001305445.1
DBSOURCE    REFSEQ: accession NM_001318516.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Nouri,H.R., Schaunaman,N., Kraft,M., Li,L., Numata,M. and Chu,H.W.
  TITLE     Tollip deficiency exaggerates airway type 2 inflammation in mice
            exposed to allergen and influenza A virus: role of the ATP/IL-33
            signaling axis
  JOURNAL   Front Immunol 14, 1304758 (2023)
   PUBMED   38124753
  REMARK    GeneRIF: Tollip deficiency exaggerates airway type 2 inflammation
            in mice exposed to allergen and influenza A virus: role of the
            ATP/IL-33 signaling axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Demir,A.B., Baris,E., Kaner,U.B., Alotaibi,H., Atabey,N. and Koc,A.
  TITLE     Toll-interacting protein may affect doxorubicin resistance in
            hepatocellular carcinoma cell lines
  JOURNAL   Mol Biol Rep 50 (10), 8551-8563 (2023)
   PUBMED   37644370
  REMARK    GeneRIF: Toll-interacting protein may affect doxorubicin resistance
            in hepatocellular carcinoma cell lines.
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Kowalewski,A., Jaworski,D., Borowczak,J., Maniewski,M.,
            Szczerbowski,K., Antosik,P., Durslewicz,J., Smolinska,M.,
            Ligmanowska,J., Grzanka,D. and Szylberg,L.
  TITLE     TOLLIP Protein Expression Predicts Unfavorable Outcome in Renal
            Cell Carcinoma
  JOURNAL   Int J Mol Sci 23 (23), 14702 (2022)
   PUBMED   36499030
  REMARK    GeneRIF: TOLLIP Protein Expression Predicts Unfavorable Outcome in
            Renal Cell Carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 213)
  AUTHORS   Venkatasubramanian,S., Pryor,R., Plumlee,C., Cohen,S.B.,
            Simmons,J.D., Warr,A.J., Graustein,A.D., Saha,A., Hawn,T.R.,
            Urdahl,K.B. and Shah,J.A.
  TITLE     TOLLIP Optimizes Dendritic Cell Maturation to Lipopolysaccharide
            and Mycobacterium tuberculosis
  JOURNAL   J Immunol 209 (3), 435-445 (2022)
   PUBMED   35803695
  REMARK    GeneRIF: TOLLIP Optimizes Dendritic Cell Maturation to
            Lipopolysaccharide and Mycobacterium tuberculosis.
REFERENCE   6  (residues 1 to 213)
  AUTHORS   Jensen,L.E. and Whitehead,A.S.
  TITLE     IRAK1b, a novel alternative splice variant of interleukin-1
            receptor-associated kinase (IRAK), mediates interleukin-1 signaling
            and has prolonged stability
  JOURNAL   J Biol Chem 276 (31), 29037-29044 (2001)
   PUBMED   11397809
REFERENCE   7  (residues 1 to 213)
  AUTHORS   Burns,K., Clatworthy,J., Martin,L., Martinon,F., Plumpton,C.,
            Maschera,B., Lewis,A., Ray,K., Tschopp,J. and Volpe,F.
  TITLE     Tollip, a new component of the IL-1RI pathway, links IRAK to the
            IL-1 receptor
  JOURNAL   Nat Cell Biol 2 (6), 346-351 (2000)
   PUBMED   10854325
REFERENCE   8  (residues 1 to 213)
  AUTHORS   Volpe,F., Clatworthy,J., Kaptein,A., Maschera,B., Griffin,A.M. and
            Ray,K.
  TITLE     The IL1 receptor accessory protein is responsible for the
            recruitment of the interleukin-1 receptor associated kinase to the
            IL1/IL1 receptor I complex
  JOURNAL   FEBS Lett 419 (1), 41-44 (1997)
   PUBMED   9426216
REFERENCE   9  (residues 1 to 213)
  AUTHORS   Cao,Z., Xiong,J., Takeuchi,M., Kurama,T. and Goeddel,D.V.
  TITLE     TRAF6 is a signal transducer for interleukin-1
  JOURNAL   Nature 383 (6599), 443-446 (1996)
   PUBMED   8837778
REFERENCE   10 (residues 1 to 213)
  AUTHORS   Nilsen,K.H.
  TITLE     Malignant lymphoma and rheumatic symptoms
  JOURNAL   N Z Med J 83 (563), 320-322 (1976)
   PUBMED   1085432
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY031351.1, AK096693.1,
            AC136297.6, AK090850.1 and AL136835.1.
            
            Summary: This gene encodes a ubiquitin-binding protein that
            interacts with several Toll-like receptor (TLR) signaling cascade
            components. The encoded protein regulates inflammatory signaling
            and is involved in interleukin-1 receptor trafficking and in the
            turnover of IL1R-associated kinase. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (4) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK096693.1, SRR1660803.85555.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158188, SAMN04284274
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..213
                     /product="toll-interacting protein isoform 4"
                     /note="Toll-interacting protein; adapter protein"
                     /calculated_mol_wt=23149
     Region          <61..111
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Region          169..209
                     /region_name="CUE_TOLIP"
                     /note="CUE domain found in the C-terminal of
                     toll-interacting protein (Tollip) and similar proteins;
                     cd14363"
                     /db_xref="CDD:270546"
     CDS             1..213
                     /gene="TOLLIP"
                     /gene_synonym="IL-1RAcPIP"
                     /coded_by="NM_001318516.2:135..776"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS81534.1"
                     /db_xref="GeneID:54472"
                     /db_xref="HGNC:HGNC:16476"
                     /db_xref="MIM:606277"
ORIGIN      
        1 mattvstqrg pvyigelpqd flritptqqq rqvqldaqaa qqlqyggavg tvgrlnitvv
       61 qrafsmddri awthitipes lrqgkvedkw yslsgrqgdd kegminlvms yallpaamvm
      121 ppqpvvlmpt vyqqgvgyvp itgmpavcsp gmvpvalppa avnaqprcse edlkaiqdmf
      181 pnmdqevirs vleaqrgnkd aainsllqmg eep
//
LOCUS       NP_001387289             257 aa            linear   PRI 21-NOV-2025
DEFINITION  single-stranded DNA-binding protein 2 isoform 29 [Homo sapiens].
ACCESSION   NP_001387289
VERSION     NP_001387289.1
DBSOURCE    REFSEQ: accession NM_001400360.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Schwab,C., Roberts,K., Boer,J.M., Gohring,G., Steinemann,D.,
            Vora,A., Macartney,C., Hough,R., Thorn,Z., Dillon,R., Escherich,G.,
            Cazzaniga,G., Schlegelberger,B., Loh,M., den Boer,M.L.,
            Moorman,A.V. and Harrison,C.J.
  TITLE     SSBP2-CSF1R is a recurrent fusion in B-lineage acute lymphoblastic
            leukemia with diverse genetic presentation and variable outcome
  JOURNAL   Blood 137 (13), 1835-1838 (2021)
   PUBMED   33197935
  REMARK    GeneRIF: SSBP2-CSF1R is a recurrent fusion in B-lineage acute
            lymphoblastic leukemia with diverse genetic presentation and
            variable outcome.
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Wang,H., Kim,J., Wang,Z., Yan,X.X., Dean,A. and Xu,W.
  TITLE     Crystal structure of human LDB1 in complex with SSBP2
  JOURNAL   Proc Natl Acad Sci U S A 117 (2), 1042-1048 (2020)
   PUBMED   31892537
  REMARK    GeneRIF: Single-stranded DNA binding proteins (SSBPs) interact
            specifically with the LDB/Chip conserved domain (LCCD) of LDB
            proteins and stabilize LDBs by preventing their proteasomal
            degradation, thus promoting their functions in gene regulation.
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Kim,H., Kim,Y., Bang,S., Park,S., Jee,S., Sim,J., Shin,S.J.,
            Paik,S.S. and Jang,K.
  TITLE     Low Expression of Single-stranded DNA Binding Protein 2 (SSBP2)
            Predicts Unfavourable Postoperative Outcomes in Patients With Clear
            Cell Renal Cell Carcinoma
  JOURNAL   In Vivo 34 (1), 101-107 (2020)
   PUBMED   31882468
  REMARK    GeneRIF: CcRCC with low SSBP2 expression was associated with
            adverse clinicopathological characteristics and poor patient
            outcomes.
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Fleisig,H.B., Orazio,N.I., Liang,H., Tyler,A.F., Adams,H.P.,
            Weitzman,M.D. and Nagarajan,L.
  TITLE     Adenoviral E1B55K oncoprotein sequesters candidate leukemia
            suppressor sequence-specific single-stranded DNA-binding protein 2
            into aggresomes
  JOURNAL   Oncogene 26 (33), 4797-4805 (2007)
   PUBMED   17311003
  REMARK    GeneRIF: Results suggest that subverting SSBP2 function by
            oncoprotein E1B55K may contribute to cell transformation by viral
            oncoproteins.
REFERENCE   7  (residues 1 to 257)
  AUTHORS   Liang,H., Samanta,S. and Nagarajan,L.
  TITLE     SSBP2, a candidate tumor suppressor gene, induces growth arrest and
            differentiation of myeloid leukemia cells
  JOURNAL   Oncogene 24 (16), 2625-2634 (2005)
   PUBMED   15782145
  REMARK    GeneRIF: Our findings are consistent with human SSBP2 being a novel
            regulator of hematopoietic growth and differentiation, whose loss
            confers a block in differentiation advantage to myeloid leukemic
            cells.
REFERENCE   8  (residues 1 to 257)
  AUTHORS   Castro,P., Liang,H., Liang,J.C. and Nagarajan,L.
  TITLE     A novel, evolutionarily conserved gene family with putative
            sequence-specific single-stranded DNA-binding activity
  JOURNAL   Genomics 80 (1), 78-85 (2002)
   PUBMED   12079286
  REMARK    GeneRIF: Member of a closely related, evolutionarily conserved, and
            ubiquitously expressed gene family, potential tumor suppressor
REFERENCE   9  (residues 1 to 257)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 257)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016562.7, AC093250.3,
            AC026419.5 and AC010623.10.
            
            Summary: This gene encodes a subunit of a protein complex that
            interacts with single-stranded DNA and is involved in the DNA
            damage response and maintenance of genome stability. The encoded
            protein may also play a role in telomere repair. A variant of this
            gene may be associated with survival in human glioblastoma
            patients. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1660803.128491.1, SRR3476690.1040243.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.1"
     Protein         1..257
                     /product="single-stranded DNA-binding protein 2 isoform
                     29"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein 2"
                     /calculated_mol_wt=26220
     Region          <12..234
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     CDS             1..257
                     /gene="SSBP2"
                     /gene_synonym="HSPC116; SOSS-B2"
                     /coded_by="NM_001400360.1:363..1136"
                     /note="isoform 29 is encoded by transcript variant 31"
                     /db_xref="GeneID:23635"
                     /db_xref="HGNC:HGNC:15831"
                     /db_xref="MIM:607389"
ORIGIN      
        1 mpvgpvppgf fqpfmspryp ggprpplrip nqalggvpgs qpllpsgmdp trqqghpnmg
       61 gpmqrmtppr gmvplgpqsd pwlslqnygg amrpplnalg gpgmpgmnmg pgggrpwpnp
      121 tnansipyss aspgnyvgpp ggggppgtpi mpspadstns gdnmytlmna vppgpnrpnf
      181 pmgpgsdgpm gglggmeshh mngslgsgdm dsisknspnn mslsnqpgtp rddgemggnf
      241 lnpfqsesys psmtmsv
//
LOCUS       NP_001309835             206 aa            linear   PRI 21-NOV-2025
DEFINITION  synaptosomal-associated protein 25 isoform SNAP25B [Homo sapiens].
ACCESSION   NP_001309835
VERSION     NP_001309835.1
DBSOURCE    REFSEQ: accession NM_001322906.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Wang,W., Gao,W., Gong,P., Song,W., Bu,X., Hou,J., Zhang,L. and
            Zhao,B.
  TITLE     Neuronal-specific TNFAIP1 ablation attenuates postoperative
            cognitive dysfunction via targeting SNAP25 for K48-linked
            ubiquitination
  JOURNAL   Cell Commun Signal 21 (1), 356 (2023)
   PUBMED   38102610
  REMARK    GeneRIF: Neuronal-specific TNFAIP1 ablation attenuates
            postoperative cognitive dysfunction via targeting SNAP25 for
            K48-linked ubiquitination.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Bolognesi,E., Guerini,F.R., Carta,A., Chiappedi,M., Sotgiu,S.,
            Mensi,M.M., Agliardi,C., Zanzottera,M. and Clerici,M.
  TITLE     The Role of SNAP-25 in Autism Spectrum Disorders Onset Patterns
  JOURNAL   Int J Mol Sci 24 (18), 14042 (2023)
   PUBMED   37762342
  REMARK    GeneRIF: The Role of SNAP-25 in Autism Spectrum Disorders Onset
            Patterns.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Yazar,V., Kuhlwein,J.K., Knehr,A., Grozdanov,V., Ekici,A.B.,
            Ludolph,A.C. and Danzer,K.M.
  TITLE     Impaired ATF3 signaling involves SNAP25 in SOD1 mutant ALS patients
  JOURNAL   Sci Rep 13 (1), 12019 (2023)
   PUBMED   37491426
  REMARK    GeneRIF: Impaired ATF3 signaling involves SNAP25 in SOD1 mutant ALS
            patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Zhang,J., Hou,S., Chi,X.Q., Shan,H.F., Li,X.W., Zhang,Q.J.,
            Wang,J.L. and Kang,C.B.
  TITLE     Role of SNAP25 on the occurrence and development of eosinophilic
            gastritis
  JOURNAL   Medicine (Baltimore) 102 (29), e34377 (2023)
   PUBMED   37478220
  REMARK    GeneRIF: Role of SNAP25 on the occurrence and development of
            eosinophilic gastritis.
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Hanson,P.I., Otto,H., Barton,N. and Jahn,R.
  TITLE     The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce
            a conformational change in syntaxin
  JOURNAL   J Biol Chem 270 (28), 16955-16961 (1995)
   PUBMED   7622514
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Hata,Y. and Sudhof,T.C.
  TITLE     A novel ubiquitous form of Munc-18 interacts with multiple
            syntaxins. Use of the yeast two-hybrid system to study interactions
            between proteins involved in membrane traffic
  JOURNAL   J Biol Chem 270 (22), 13022-13028 (1995)
   PUBMED   7768895
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Chapman,E.R., An,S., Barton,N. and Jahn,R.
  TITLE     SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin
            via domains that may form coiled coils
  JOURNAL   J Biol Chem 269 (44), 27427-27432 (1994)
   PUBMED   7961655
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Zhao,N., Hashida,H., Takahashi,N. and Sakaki,Y.
  TITLE     Cloning and sequence analysis of the human SNAP25 cDNA
  JOURNAL   Gene 145 (2), 313-314 (1994)
   PUBMED   8056350
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Abicht,A., Muller,J.S. and Lochmuller,H.
  TITLE     Congenital Myasthenic Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354824.8 and AL023913.6.
            
            Summary: Synaptic vesicle membrane docking and fusion is mediated
            by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment
            protein receptors) located on the vesicle membrane (v-SNAREs) and
            the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE
            complex consists of a bundle of four helices, one of which is
            supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on
            the plasma membrane, the protein syntaxin supplies one helix and
            the protein encoded by this gene contributes the other two.
            Therefore, this gene product is a presynaptic plasma membrane
            protein involved in the regulation of neurotransmitter release. Two
            alternative transcript variants encoding different protein isoforms
            have been described for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.249223.1,
                                           SRR1803614.1469.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.2"
     Protein         1..206
                     /product="synaptosomal-associated protein 25 isoform
                     SNAP25B"
                     /note="resistance to inhibitors of cholinesterase 4
                     homolog; synaptosome associated protein 25kDa;
                     synaptosomal-associated protein, 25kDa"
                     /calculated_mol_wt=23184
     Region          1..75
                     /region_name="Interaction with CENPF.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P60880.1)"
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60880.1)"
     Region          10..82
                     /region_name="SNARE_SNAP25N"
                     /note="N-terminal SNARE motif of SNAP25; cd15894"
                     /db_xref="CDD:277247"
     Site            order(24..25,28..29,31..33,35..40,42..44,46..47,49..50,
                     53..54,56..61,63..65,67..68,70..75,77..78)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277247"
     Site            53
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277247"
     Region          91..142
                     /region_name="SNAP-25"
                     /note="SNAP-25 family; pfam00835"
                     /db_xref="CDD:459955"
     Region          111..120
                     /region_name="Interaction with ZDHHC17.
                     /evidence=ECO:0000269|PubMed:28757145"
                     /note="propagated from UniProtKB/Swiss-Prot (P60880.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P60879; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     Region          143..201
                     /region_name="SNARE_SNAP25C"
                     /note="C-terminal SNARE motif of SNAP25; cd15885"
                     /db_xref="CDD:277238"
     Site            order(143,145..146,149..154,156..157,160..161,163..165,
                     167..168,171..172,174..175,177..182,184..185,188,191,195,
                     198,201)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277238"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P60879; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     Site            174
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277238"
     Site            180..181
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by C.botulinum
                     neurotoxin type E (BoNT/E).
                     /evidence=ECO:0000269|PubMed:9886085; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P60879; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     Site            197..198
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by C.botulinum
                     neurotoxin type A (BoNT/A, botA).
                     /evidence=ECO:0000269|PubMed:9886085,
                     ECO:0000305|PubMed:15592454; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     Site            198..199
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by C.botulinum
                     neurotoxin type C (BoNT/C).
                     /evidence=ECO:0000269|PubMed:9886085,
                     ECO:0000305|PubMed:15592454; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     CDS             1..206
                     /gene="SNAP25"
                     /gene_synonym="bA416N4.2; CMS18; DEE117; dJ1068F16.2;
                     RIC-4; RIC4; SEC9; SNAP; SNAP-25; SUP"
                     /coded_by="NM_001322906.2:266..886"
                     /note="isoform SNAP25B is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS13110.1"
                     /db_xref="GeneID:6616"
                     /db_xref="HGNC:HGNC:11132"
                     /db_xref="MIM:600322"
ORIGIN      
        1 maedadmrne leemqrradq ladeslestr rmlqlveesk dagirtlvml deqgeqleri
       61 eegmdqinkd mkeaeknltd lgkfcglcvc pcnklkssda ykkawgnnqd gvvasqparv
      121 vdereqmais ggfirrvtnd arenemdenl eqvsgiignl rhmaldmgne idtqnrqidr
      181 imekadsnkt rideanqrat kmlgsg
//
LOCUS       NP_001362638             444 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform qq [Homo sapiens].
ACCESSION   NP_001362638 XP_016858625
VERSION     NP_001362638.1
DBSOURCE    REFSEQ: accession NM_001375709.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 444)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 444)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 444)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            On Oct 31, 2019 this sequence version replaced XP_016858625.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2829014.1,
                                           SRR14038192.3717598.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..444
                     /product="abl interactor 2 isoform qq"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=48966
     Region          93..156
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          384..>418
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     CDS             1..444
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375709.1:122..1456"
                     /note="isoform qq is encoded by transcript variant 48"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqs adkqraleet kayttqslas
       61 vaylintlan nvlqmldiqa sqlrrmessi nhisqtvdih kekvarreig ilttnkntsr
      121 thkiiapanl erpvryirkp idytilddig hgvkvstqnm kmgglprttp ptqkppsppm
      181 sgkgtlgrhs pyrtlepvrp pvvpndyvps ptrnmapsqq spvrtasvnq rnrtyssgss
      241 ggshpssrss srensgsgsv gvpiavptps ppsvfpghpv qfysmnrpas rhtpptiggs
      301 lpyrrppsit sqtslqnqmn ggpfysqnpv sdtppppppv eepvfdespp pppppedyee
      361 eeaavveysd pyaeedppwa prsylekvva iydytkdked elsfqegaii yvikknddvl
      421 ktkqaeseqm dlsaiictml scld
//
LOCUS       NP_149159                597 aa            linear   PRI 21-NOV-2025
DEFINITION  dystrobrevin beta isoform 2 [Homo sapiens].
ACCESSION   NP_149159
VERSION     NP_149159.2
DBSOURCE    REFSEQ: accession NM_033147.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Prokopenko,D., Lee,S., Hecker,J., Mullin,K., Morgan,S.,
            Katsumata,Y., Weiner,M.W., Fardo,D.W., Laird,N., Bertram,L.,
            Hide,W., Lange,C. and Tanzi,R.E.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative (ADNI)
  TITLE     Region-based analysis of rare genomic variants in whole-genome
            sequencing datasets reveal two novel Alzheimer's disease-associated
            genes: DTNB and DLG2
  JOURNAL   Mol Psychiatry 27 (4), 1963-1969 (2022)
   PUBMED   35246634
  REMARK    GeneRIF: Region-based analysis of rare genomic variants in
            whole-genome sequencing datasets reveal two novel Alzheimer's
            disease-associated genes: DTNB and DLG2.
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 597)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 597)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 597)
  AUTHORS   Piluso,G., Mirabella,M., Ricci,E., Belsito,A., Abbondanza,C.,
            Servidei,S., Puca,A.A., Tonali,P., Puca,G.A. and Nigro,V.
  TITLE     Gamma1- and gamma2-syntrophins, two novel dystrophin-binding
            proteins localized in neuronal cells
  JOURNAL   J Biol Chem 275 (21), 15851-15860 (2000)
   PUBMED   10747910
REFERENCE   7  (residues 1 to 597)
  AUTHORS   Blake,D.J., Hawkes,R., Benson,M.A. and Beesley,P.W.
  TITLE     Different dystrophin-like complexes are expressed in neurons and
            glia
  JOURNAL   J Cell Biol 147 (3), 645-658 (1999)
   PUBMED   10545507
REFERENCE   8  (residues 1 to 597)
  AUTHORS   Puca,A.A., Nigro,V., Piluso,G., Belsito,A., Sampaolo,S.,
            Quaderi,N., Rossi,E., Di Iorio,G., Ballabio,A. and Franco,B.
  TITLE     Identification and characterization of a novel member of the
            dystrobrevin gene family
  JOURNAL   FEBS Lett 425 (1), 7-13 (1998)
   PUBMED   9540997
REFERENCE   9  (residues 1 to 597)
  AUTHORS   Peters,M.F., O'Brien,K.F., Sadoulet-Puccio,H.M., Kunkel,L.M.,
            Adams,M.E. and Froehner,S.C.
  TITLE     beta-dystrobrevin, a new member of the dystrophin family.
            Identification, cloning, and protein associations
  JOURNAL   J Biol Chem 272 (50), 31561-31569 (1997)
   PUBMED   9395493
REFERENCE   10 (residues 1 to 597)
  AUTHORS   Straub,V. and Campbell,K.P.
  TITLE     Muscular dystrophies and the dystrophin-glycoprotein complex
  JOURNAL   Curr Opin Neurol 10 (2), 168-175 (1997)
   PUBMED   9146999
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB460644.1, AF022728.1 and
            BC016655.1.
            
            On Oct 8, 2003 this sequence version replaced NP_149159.1.
            
            Summary: This gene encodes dystrobrevin beta, a component of the
            dystrophin-associated protein complex (DPC). The DPC consists of
            dystrophin and several integral and peripheral membrane proteins,
            including dystroglycans, sarcoglycans, syntrophins and dystrobrevin
            alpha and beta. The DPC localizes to the sarcolemma and its
            disruption is associated with various forms of muscular dystrophy.
            Dystrobrevin beta is thought to interact with syntrophin and the
            DP71 short form of dystrophin. [provided by RefSeq, Mar 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..597
                     /product="dystrobrevin beta isoform 2"
                     /note="DTN-B; beta-dystrobrevin"
                     /calculated_mol_wt=67930
     Region          54..214
                     /region_name="EFh_DTN"
                     /note="EF-hand-like motif found in dystrobrevins and
                     similar proteins; cd16244"
                     /db_xref="CDD:320002"
     Region          54..95
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320002"
     Region          104..138
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320002"
     Region          144..180
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320002"
     Region          191..214
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320002"
     Region          241..289
                     /region_name="ZZ_dystrophin"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     dystrophin and dystrobrevin. The ZZ motif coordinates two
                     zinc ions and most likely participates in ligand binding
                     or molecular scaffolding. Dystrophin attaches actin
                     filaments to an integral membrane...; cd02334"
                     /db_xref="CDD:239074"
     Site            order(243,246,258,261,267,270,280,284)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(243,246,267,270)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(244,255,257,263,265)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(256,271,286,289)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(258,261,280,284)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239074"
     Region          <400..>549
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     CDS             1..597
                     /gene="DTNB"
                     /coded_by="NM_033147.4:194..1987"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS46235.1"
                     /db_xref="GeneID:1838"
                     /db_xref="HGNC:HGNC:3058"
                     /db_xref="MIM:602415"
ORIGIN      
        1 mieesgnkrk tmaekrqlfi emraqnfdvi rlstyrtack lrfvqkrcnl hlvdiwnmie
       61 afrdnglntl dhtteisvsr letvissiyy qlnkrlpsth qisveqsisl llnfmiaayd
      121 segrgkltvf svkamlatmc ggkmldklry vfsqmsdsng lmifskfdqf lkevlklpta
      181 vfegpsfgyt ehsvrtcfpq qrkimlnmfl dtmmadpppq clvwlplmhr lahvenvfhp
      241 vecsycrces mmgfryrcqq chnyqlcqnc fwrghaggph snqhqmkehs swkspakkls
      301 haiskslgcv ptrepphpvf peqpekpldl ahivpprplt nmndtmvshm ssgvptptkr
      361 lqysqdipsh ladehalias yvarlqhcar vldspsrlde ehrliaryaa rlaaeagnvt
      421 rpptdlsfnf dankqqrqli aelenknrei lqeiqrlrle heqasqptpe kaqqnptlla
      481 elrllrqrkd eleqrmsalq esrrelmvql eelmkllkee eqkqaaqatg sphtspthgg
      541 grpmpmpvrs tsagstpthc pqdslsgvgg dvqeafaqae egaeeeeekm qngkdrg
//
LOCUS       NP_001269695             349 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase I subunit RPA49 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001269695 XP_005251605
VERSION     NP_001269695.1
DBSOURCE    REFSEQ: accession NM_001282766.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   McNamar,R., Freeman,E., Baylor,K.N., Fakhouri,A.M., Huang,S.,
            Knutson,B.A. and Rothblum,L.I.
  TITLE     PAF49: An RNA Polymerase I subunit essential for rDNA transcription
            and stabilization of PAF53
  JOURNAL   J Biol Chem 299 (8), 104951 (2023)
   PUBMED   37356716
  REMARK    GeneRIF: PAF49: An RNA Polymerase I subunit essential for rDNA
            transcription and stabilization of PAF53.
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Zhao,D., Liu,W., Chen,K., Wu,Z., Yang,H. and Xu,Y.
  TITLE     Structure of the human RNA polymerase I elongation complex
  JOURNAL   Cell Discov 7 (1), 97 (2021)
   PUBMED   34671025
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Bjerregaard,B., Wrenzycki,C., Strejcek,F., Laurincik,J., Holm,P.,
            Ochs,R.L., Rosenkranz,C., Callesen,H., Rath,D., Niemann,H. and
            Maddox-Hyttel,P.
  TITLE     Expression of nucleolar-related proteins in porcine preimplantation
            embryos produced in vivo and in vitro
  JOURNAL   Biol Reprod 70 (4), 867-876 (2004)
   PUBMED   14585813
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   8  (residues 1 to 349)
  AUTHORS   Voit,R. and Grummt,I.
  TITLE     Phosphorylation of UBF at serine 388 is required for interaction
            with RNA polymerase I and activation of rDNA transcription
  JOURNAL   Proc Natl Acad Sci U S A 98 (24), 13631-13636 (2001)
   PUBMED   11698641
REFERENCE   9  (residues 1 to 349)
  AUTHORS   Seither,P., Zatsepina,O., Hoffmann,M. and Grummt,I.
  TITLE     Constitutive and strong association of PAF53 with RNA polymerase I
  JOURNAL   Chromosoma 106 (4), 216-225 (1997)
   PUBMED   9254723
REFERENCE   10 (residues 1 to 349)
  AUTHORS   Hanada,K., Song,C.Z., Yamamoto,K., Yano,K., Maeda,Y., Yamaguchi,K.
            and Muramatsu,M.
  TITLE     RNA polymerase I associated factor 53 binds to the nucleolar
            transcription factor UBF and functions in specific rDNA
            transcription
  JOURNAL   EMBO J 15 (9), 2217-2226 (1996)
   PUBMED   8641287
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL158156.7.
            
            On Sep 19, 2013 this sequence version replaced XP_005251605.1.
            
            Transcript Variant: This variant (2) uses an alternate exon the
            coding region which results in the use of downstream start codon
            compared to variant 1. The encoded isoform (2) has a shorter and
            distinct N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303167.1, SRR14038197.287705.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.2"
     Protein         1..349
                     /product="DNA-directed RNA polymerase I subunit RPA49
                     isoform 2"
                     /note="polymerase (RNA) I associated factor 1; polymerase
                     (RNA) I subunit E; DNA-directed RNA polymerase I subunit
                     RPA49; RNA polymerase I subunit A49; RNA polymerase
                     I-associated factor 53; DNA-directed RNA polymerase I
                     subunit E; polymerase (RNA) I polypeptide E, 53kDa"
                     /calculated_mol_wt=39652
     Region          <47..334
                     /region_name="RNA_pol_I_A49"
                     /note="A49-like RNA polymerase I associated factor;
                     pfam06870"
                     /db_xref="CDD:462024"
     CDS             1..349
                     /gene="POLR1E"
                     /gene_synonym="A49; PAF53; PRAF1; RPA49"
                     /coded_by="NM_001282766.2:405..1454"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:64425"
                     /db_xref="HGNC:HGNC:17631"
                     /db_xref="MIM:621031"
ORIGIN      
        1 mmlncstcsh yfqvfhqesk iifwkeprtc flilslplpg eltwdvsves elalesqtkt
       61 yrekmdscie afgttkqkra lntrrmnrvg neslnravak aaetiidtkg vtalvsdaih
      121 ndlqddslyl ppcyddaakp edvykfedll spaeyealqs pseafrnvts eeilkmieen
      181 shctfvieal kslpsdvesr drqarciwfl dtlikfrahr vvkrksalgp gvphiintkl
      241 lkhftcltyn ngrlrnlisd smkakitayv iilalhihdf qidltvlqrd lklsekrmme
      301 iakamrlkis krrvsvaags eedhklgtls lplppaqtsd rlakrrkit
//
LOCUS       NP_001122317            1617 aa            linear   PRI 21-NOV-2025
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily A member 4 isoform C [Homo sapiens].
ACCESSION   NP_001122317
VERSION     NP_001122317.1
DBSOURCE    REFSEQ: accession NM_001128845.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1617)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1617)
  AUTHORS   Schneppenheim,R., Fruhwald,M.C., Gesk,S., Hasselblatt,M.,
            Jeibmann,A., Kordes,U., Kreuz,M., Leuschner,I., Martin Subero,J.I.,
            Obser,T., Oyen,F., Vater,I. and Siebert,R.
  TITLE     Germline nonsense mutation and somatic inactivation of SMARCA4/BRG1
            in a family with rhabdoid tumor predisposition syndrome
  JOURNAL   Am J Hum Genet 86 (2), 279-284 (2010)
   PUBMED   20137775
  REMARK    GeneRIF: SMARCA4 is involved in cancer predisposition
REFERENCE   3  (residues 1 to 1617)
  AUTHORS   Wong,A.K., Shanahan,F., Chen,Y., Lian,L., Ha,P., Hendricks,K.,
            Ghaffari,S., Iliev,D., Penn,B., Woodland,A.M., Smith,R., Salada,G.,
            Carillo,A., Laity,K., Gupte,J., Swedlund,B., Tavtigian,S.V.,
            Teng,D.H. and Lees,E.
  TITLE     BRG1, a component of the SWI-SNF complex, is mutated in multiple
            human tumor cell lines
  JOURNAL   Cancer Res 60 (21), 6171-6177 (2000)
   PUBMED   11085541
REFERENCE   4  (residues 1 to 1617)
  AUTHORS   Muchardt,C., Reyes,J.C., Bourachot,B., Leguoy,E. and Yaniv,M.
  TITLE     The hbrm and BRG-1 proteins, components of the human SNF/SWI
            complex, are phosphorylated and excluded from the condensed
            chromosomes during mitosis
  JOURNAL   EMBO J 15 (13), 3394-3402 (1996)
   PUBMED   8670841
REFERENCE   5  (residues 1 to 1617)
  AUTHORS   Muchardt,C., Sardet,C., Bourachot,B., Onufryk,C. and Yaniv,M.
  TITLE     A human protein with homology to Saccharomyces cerevisiae SNF5
            interacts with the potential helicase hbrm
  JOURNAL   Nucleic Acids Res 23 (7), 1127-1132 (1995)
   PUBMED   7739891
REFERENCE   6  (residues 1 to 1617)
  AUTHORS   Chiba,H., Muramatsu,M., Nomoto,A. and Kato,H.
  TITLE     Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and
            Drosophila brahma are transcriptional coactivators cooperating with
            the estrogen receptor and the retinoic acid receptor
  JOURNAL   Nucleic Acids Res 22 (10), 1815-1820 (1994)
   PUBMED   8208605
REFERENCE   7  (residues 1 to 1617)
  AUTHORS   Khavari,P.A., Peterson,C.L., Tamkun,J.W., Mendel,D.B. and
            Crabtree,G.R.
  TITLE     BRG1 contains a conserved domain of the SWI2/SNF2 family necessary
            for normal mitotic growth and transcription
  JOURNAL   Nature 366 (6451), 170-174 (1993)
   PUBMED   8232556
REFERENCE   8  (residues 1 to 1617)
  AUTHORS   Nemes,K., Bens,S., Bourdeaut,F., Johann,P., Kordes,U., Siebert,R.
            and Fruhwald,M.C.
  TITLE     Rhabdoid Tumor Predisposition Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29215836
REFERENCE   9  (residues 1 to 1617)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
REFERENCE   10 (residues 1 to 1617)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011442.5, AC006127.1 and
            AC011485.6.
            
            Summary: The protein encoded by this gene is a member of the
            SWI/SNF family of proteins and is similar to the brahma protein of
            Drosophila. Members of this family have helicase and ATPase
            activities and are thought to regulate transcription of certain
            genes by altering the chromatin structure around those genes. The
            encoded protein is part of the large ATP-dependent chromatin
            remodeling complex SNF/SWI, which is required for transcriptional
            activation of genes normally repressed by chromatin. In addition,
            this protein can bind BRCA1, as well as regulate the expression of
            the tumorigenic protein CD44. Mutations in this gene cause rhabdoid
            tumor predisposition syndrome type 2. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, May 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU430757.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1617
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..1617
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily A member
                     4 isoform C"
                     /note="sucrose nonfermenting-like 4; mitotic growth and
                     transcription activator; BRM/SWI2-related gene 1; homeotic
                     gene regulator; nuclear protein GRB1; brahma protein-like
                     1; SNF2-like 4; global transcription activator homologous
                     sequence; transcription activator BRG1; ATP-dependent
                     helicase SMARCA4; protein BRG-1; protein brahma homolog 1;
                     BRG1-associated factor 190A; SWI/SNF related, matrix
                     associated, actin dependent regulator of chromatin,
                     subfamily a, member 4"
                     /calculated_mol_wt=181560
     Region          42..>222
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          171..205
                     /region_name="QLQ"
                     /note="pfam08880"
                     /db_xref="CDD:462622"
     Region          <364..>570
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          460..532
                     /region_name="HSA"
                     /note="domain in helicases and associated with SANT
                     domains; smart00573"
                     /db_xref="CDD:214727"
     Region          612..656
                     /region_name="BRK"
                     /note="domain in transcription and CHROMO domain
                     helicases; smart00592"
                     /db_xref="CDD:197800"
     Region          731..981
                     /region_name="DEXHc_SMARCA4"
                     /note="DEXH-box helicase domain of SMARCA4; cd18062"
                     /db_xref="CDD:350820"
     Region          750..>1232
                     /region_name="PLN03142"
                     /note="Probable chromatin-remodeling complex ATPase chain;
                     Provisional"
                     /db_xref="CDD:215601"
     Site            order(781..787,821,881..882)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350820"
     Region          1289..1356
                     /region_name="SnAC"
                     /note="Snf2-ATP coupling, chromatin remodelling complex;
                     pfam14619"
                     /db_xref="CDD:464219"
     Region          1428..1534
                     /region_name="Bromo_SNF2L2"
                     /note="Bromodomain, SNF2L2-like subfamily, specific to
                     animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related
                     matrix-associated actin-dependent regulator of chromatin
                     subfamily A member 2 is a global transcriptional
                     activator, which cooperates with nuclear hormone...;
                     cd05516"
                     /db_xref="CDD:99947"
     Site            order(1459,1464,1467,1506,1510,1516)
                     /site_type="active"
                     /note="acetyllysine binding site [active]"
                     /db_xref="CDD:99947"
     CDS             1..1617
                     /gene="SMARCA4"
                     /gene_synonym="BAF190; BAF190A; BRG1; CSS4; hSNF2b; MRD16;
                     OTSC12; RTPS2; SNF2; SNF2-beta; SNF2L4; SNF2LB; SWI2"
                     /coded_by="NM_001128845.2:29..4882"
                     /note="isoform C is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS45972.1"
                     /db_xref="GeneID:6597"
                     /db_xref="HGNC:HGNC:11100"
                     /db_xref="MIM:603254"
ORIGIN      
        1 mstpdpplgg tprpgpspgp gpspgamlgp spgpspgsah smmgpspgpp saghpiptqg
       61 pggypqdnmh qmhkpmesmh ekgmsddpry nqmkgmgmrs gghagmgppp spmdqhsqgy
      121 psplggseha sspvpasgps sgpqmssgpg gapldgadpq algqqnrgpt pfnqnqlhql
      181 raqimaykml argqplpdhl qmavqgkrpm pgmqqqmptl pppsvsatgp gpgpgpgpgp
      241 gpgpappnys rphgmggpnm pppgpsgvpp gmpgqppggp pkpwpegpma naaaptstpq
      301 klippqptgr pspappavpp aaspvmppqt qspgqpaqpa pmvplhqkqs ritpiqkprg
      361 ldpveilqer eyrlqariah riqelenlpg slagdlrtka tielkalrll nfqrqlrqev
      421 vvcmrrdtal etalnakayk rskrqslrea riteklekqq kieqerkrrq khqeylnsil
      481 qhakdfkeyh rsvtgkiqkl tkavatyhan tereqkkene riekermrrl maedeegyrk
      541 lidqkkdkrl ayllqqtdey vanltelvrq hkaaqvakek kkkkkkkkae naegqtpaig
      601 pdgepldets qmsdlpvkvi hvesgkiltg tdapkagqle awlemnpgye vaprsdsees
      661 gseeeeeeee eeqpqaaqpp tlpveekkki pdpdsddvse vdarhiiena kqdvddeygv
      721 sqalarglqs yyavahavte rvdkqsalmv ngvlkqyqik glewlvslyn nnlngilade
      781 mglgktiqti alitylmehk ringpfliiv plstlsnway efdkwapsvv kvsykgspaa
      841 rrafvpqlrs gkfnvlltty eyiikdkhil akirwkymiv deghrmknhh ckltqvlnth
      901 yvaprrlllt gtplqnklpe lwallnfllp tifkscstfe qwfnapfamt gekvdlneee
      961 tiliirrlhk vlrpfllrrl kkeveaqlpe kveyvikcdm salqrvlyrh mqakgvlltd
     1021 gsekdkkgkg gtktlmntim qlrkicnhpy mfqhieesfs ehlgftggiv qgldlyrasg
     1081 kfelldrilp klratnhkvl lfcqmtslmt imedyfayrg fkylrldgtt kaedrgmllk
     1141 tfnepgseyf ifllstragg lglnlqsadt viifdsdwnp hqdlqaqdra hrigqqnevr
     1201 vlrlctvnsv eekilaaaky klnvdqkviq agmfdqksss herraflqai leheeqdeee
     1261 devpddetvn qmiarheeef dlfmrmdldr rreearnpkr kprlmeedel pswiikddae
     1321 verltceeee ekmfgrgsrh rkevdysdsl tekqwlktlk aieegtleei eeevrqkkss
     1381 rkrkrdsdag sstpttstrs rdkddeskkq kkrgrppaek lspnppnltk kmkkivdavi
     1441 kykdsssgrq lsevfiqlps rkelpeyyel irkpvdfkki kerirnhkyr slndlekdvm
     1501 llcqnaqtfn legsliyeds ivlqsvftsv rqkiekedds egeeseeeee geeegseses
     1561 rsvkvkiklg rkekaqdrlk ggrrrpsrgs rakpvvsddd seeeqeedrs gsgseed
//
LOCUS       NP_001382408             912 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA-processing factor 40 homolog A isoform 2 [Homo sapiens].
ACCESSION   NP_001382408
VERSION     NP_001382408.1
DBSOURCE    REFSEQ: accession NM_001395479.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 912)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 912)
  AUTHORS   Choudhary,B. and Norris,A.
  TITLE     Conserved role for spliceosomal component PRPF40A in microexon
            splicing
  JOURNAL   RNA 31 (1), 43-50 (2024)
   PUBMED   39389624
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 912)
  AUTHORS   Martinez-Lumbreras,S., Trager,L.K., Mulorz,M.M., Payr,M.,
            Dikaya,V., Hipp,C., Konig,J. and Sattler,M.
  TITLE     Intramolecular autoinhibition regulates the selectivity of PRPF40A
            tandem WW domains for proline-rich motifs
  JOURNAL   Nat Commun 15 (1), 3888 (2024)
   PUBMED   38719828
  REMARK    GeneRIF: Intramolecular autoinhibition regulates the selectivity of
            PRPF40A tandem WW domains for proline-rich motifs.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 912)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 912)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 912)
  AUTHORS   Allen,M., Friedler,A., Schon,O. and Bycroft,M.
  TITLE     The structure of an FF domain from human HYPA/FBP11
  JOURNAL   J Mol Biol 323 (3), 411-416 (2002)
   PUBMED   12381297
  REMARK    GeneRIF: Data describe the structure of an FF domain from
            HYPA/FBP11, which differs from those of other
            phosphopeptide-binding domains and represents a novel
            phosphopeptide-binding fold.
REFERENCE   7  (residues 1 to 912)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   8  (residues 1 to 912)
  AUTHORS   Bedford,M.T., Reed,R. and Leder,P.
  TITLE     WW domain-mediated interactions reveal a spliceosome-associated
            protein that binds a third class of proline-rich motif: the proline
            glycine and methionine-rich motif
  JOURNAL   Proc Natl Acad Sci U S A 95 (18), 10602-10607 (1998)
   PUBMED   9724750
REFERENCE   9  (residues 1 to 912)
  AUTHORS   Faber,P.W., Barnes,G.T., Srinidhi,J., Chen,J., Gusella,J.F. and
            MacDonald,M.E.
  TITLE     Huntingtin interacts with a family of WW domain proteins
  JOURNAL   Hum Mol Genet 7 (9), 1463-1474 (1998)
   PUBMED   9700202
REFERENCE   10 (residues 1 to 912)
  AUTHORS   Chan,D.C., Bedford,M.T. and Leder,P.
  TITLE     Formin binding proteins bear WWP/WW domains that bind proline-rich
            peptides and functionally resemble SH3 domains
  JOURNAL   EMBO J 15 (5), 1045-1054 (1996)
   PUBMED   8605874
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079344.5 and AC012443.8.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..912
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q23.3"
     Protein         1..912
                     /product="pre-mRNA-processing factor 40 homolog A isoform
                     2"
                     /note="formin binding protein 3; Huntingtin-interacting
                     protein A; NY-REN-6 antigen; Fas-ligand associated factor
                     1; formin-binding protein 11; huntingtin yeast partner A;
                     fas ligand-associated factor 1; pre-mRNA processing factor
                     40 homolog A; renal carcinoma antigen NY-REN-6;
                     huntingtin-interacting protein 10; PRP40 pre-mRNA
                     processing factor 40 homolog A"
                     /calculated_mol_wt=103898
     Region          110..751
                     /region_name="PRP40"
                     /note="Splicing factor [RNA processing and modification];
                     COG5104"
                     /db_xref="CDD:227435"
     CDS             1..912
                     /gene="PRPF40A"
                     /gene_synonym="FBP-11; FBP11; FLAF1; FNBP3; HIP-10; HIP10;
                     HYPA; NY-REN-6; Prp40"
                     /coded_by="NM_001395479.1:214..2952"
                     /note="isoform 2 is encoded by transcript variant 20"
                     /db_xref="GeneID:55660"
                     /db_xref="HGNC:HGNC:16463"
                     /db_xref="MIM:612941"
ORIGIN      
        1 mcsgsgrrrs slsptmrpgt gaergglmmg hpgmhyapmg mhpmgqranm ppvphgmmpq
       61 mmppmggppm gqmpgmmssv mpgmmmshms qasmqpalpp gvnsmdvaag tasgaksmwt
      121 ehkspdgrty yyntetkqst wekpddlktp aeqllskcpw keyksdsgkp yyynsqtkes
      181 rwakpkeled leamikaees skqeecttts tapvptteip ttmstmaaae aaaavvaaaa
      241 aaaaaaaaan anastsasnt vsgtvpvvpe pevtsivatv vdnentvtis teeqaqltst
      301 paiqdqsvev ssntgeetsk qetvadftpk keeeesqpak ktytwntkee akqafkellk
      361 ekrvpsnasw eqamkmiind prysalakls ekkqafnayk vqtekeekee arskykeake
      421 sfqrflenhe kmtsttrykk aeqmfgemev wnaiserdrl eiyedvlffl skkekeqakq
      481 lrkrnwealk nildnmanvt ysttwseaqq ylmdnptfae deelqnmdke dalicfeehi
      541 ralekeeeee kqksllrerr rqrknresfq ifldelhehg qlhsmsswme lyptissdir
      601 ftnmlgqpgs taldlfkfyv edlkaryhde kkiikdilkd kgfvvevntt fedfvaiiss
      661 tkrsttldag niklafnsll ekaearerer ekeearkmkr kesafksmlk qaappielda
      721 vwedirerfv kepafeditl eserkrifkd fmhvlehecq hhhsknkkhs kkskkhhrkr
      781 srsrsgsdsd dddshskkkr qrsesrsase hsssaesers ykkskkhkkk skkrrhksds
      841 pesdaerekd kkekdresek drtrqrsesk hkspkkktgk dsgnwdtsgs elsegelekr
      901 rrtlleqldd dq
//
LOCUS       NP_068711                512 aa            linear   PRI 21-NOV-2025
DEFINITION  gamma-aminobutyric acid receptor subunit beta-2 isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_068711 XP_005265924
VERSION     NP_068711.1
DBSOURCE    REFSEQ: accession NM_021911.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Zhou,J., Noviello,C.M., Teng,J., Moore,H., Lega,B. and Hibbs,R.E.
  TITLE     Resolving native GABAA receptor structures from the human brain
  JOURNAL   Nature 638 (8050), 562-568 (2025)
   PUBMED   39843743
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Li,P.P., Zhou,Y.Y., Gao,L., Lv,J.N., Xu,S.S., Zhao,Y.W., Xu,D.,
            Huang,R., Zhang,X., Li,P., Fu,X. and He,Z.
  TITLE     The de novo missense mutation F224S in GABRB2, identified in
            epileptic encephalopathy and developmental delay, impairs GABAAR
            function
  JOURNAL   Neuroscience 553, 172-184 (2024)
   PUBMED   38964454
  REMARK    GeneRIF: The de novo missense mutation F224S in GABRB2, identified
            in epileptic encephalopathy and developmental delay, impairs GABAAR
            function.
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Mohammadi,N.A., Ahring,P.K., Yu Liao,V.W., Chua,H.C., Ortiz de la
            Rosa,S., Johannesen,K.M., Michaeli-Yossef,Y., Vincent-Devulder,A.,
            Meridda,C., Bruel,A.L., Rossi,A., Patel,C., Klepper,J., Bonanni,P.,
            Minghetti,S., Trivisano,M., Specchio,N., Amor,D., Auvin,S.,
            Baer,S., Meyer,P., Milh,M., Salpietro,V., Maroofian,R., Lemke,J.R.,
            Weckhuysen,S., Christophersen,P., Rubboli,G., Chebib,M.,
            Jensen,A.A., Absalom,N.L. and Moller,R.S.
  TITLE     Distinct neurodevelopmental and epileptic phenotypes associated
            with gain- and loss-of-function GABRB2 variants
  JOURNAL   EBioMedicine 106, 105236 (2024)
   PUBMED   38996765
  REMARK    GeneRIF: Distinct neurodevelopmental and epileptic phenotypes
            associated with gain- and loss-of-function GABRB2 variants.
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Bengtsson,S.K.S., Sjostedt,J., Malinina,E., Das,R., Doverskog,M.,
            Johansson,M., Haage,D. and Backstrom,T.
  TITLE     Extra-Synaptic GABAA Receptor Potentiation and Neurosteroid-Induced
            Learning Deficits Are Inhibited by GR3027, a GABAA Modulating
            Steroid Antagonist
  JOURNAL   Biomolecules 13 (10), 1496 (2023)
   PUBMED   37892178
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Sente,A., Desai,R., Naydenova,K., Malinauskas,T., Jounaidi,Y.,
            Miehling,J., Zhou,X., Masiulis,S., Hardwick,S.W., Chirgadze,D.Y.,
            Miller,K.W. and Aricescu,A.R.
  TITLE     Differential assembly diversifies GABAA receptor structures and
            signalling
  JOURNAL   Nature 604 (7904), 190-194 (2022)
   PUBMED   35355020
REFERENCE   6  (residues 1 to 512)
  AUTHORS   McKinley,D.D., Lennon,D.J. and Carter,D.B.
  TITLE     Cloning, sequence analysis and expression of two forms of mRNA
            coding for the human beta 2 subunit of the GABAA receptor
  JOURNAL   Brain Res Mol Brain Res 28 (1), 175-179 (1995)
   PUBMED   7707873
REFERENCE   7  (residues 1 to 512)
  AUTHORS   Russek,S.J. and Farb,D.H.
  TITLE     Mapping of the beta 2 subunit gene (GABRB2) to microdissected human
            chromosome 5q34-q35 defines a gene cluster for the most abundant
            GABAA receptor isoform
  JOURNAL   Genomics 23 (3), 528-533 (1994)
   PUBMED   7851879
REFERENCE   8  (residues 1 to 512)
  AUTHORS   Togel,M., Mossier,B., Fuchs,K. and Sieghart,W.
  TITLE     gamma-Aminobutyric acidA receptors displaying association of gamma
            3-subunits with beta 2/3 and different alpha-subunits exhibit
            unique pharmacological properties
  JOURNAL   J Biol Chem 269 (17), 12993-12998 (1994)
   PUBMED   8175718
REFERENCE   9  (residues 1 to 512)
  AUTHORS   Kellenberger,S., Malherbe,P. and Sigel,E.
  TITLE     Function of the alpha 1 beta 2 gamma 2S gamma-aminobutyric acid
            type A receptor is modulated by protein kinase C via multiple
            phosphorylation sites
  JOURNAL   J Biol Chem 267 (36), 25660-25663 (1992)
   PUBMED   1334482
REFERENCE   10 (residues 1 to 512)
  AUTHORS   Moss,S.J., Doherty,C.A. and Huganir,R.L.
  TITLE     Identification of the cAMP-dependent protein kinase and protein
            kinase C phosphorylation sites within the major intracellular
            domains of the beta 1, gamma 2S, and gamma 2L subunits of the
            gamma-aminobutyric acid type A receptor
  JOURNAL   J Biol Chem 267 (20), 14470-14476 (1992)
   PUBMED   1321150
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091989.3, S77553.1 and
            AC022120.7.
            
            On Aug 31, 2013 this sequence version replaced XP_005265924.1.
            
            Summary: The gamma-aminobutyric acid (GABA) A receptor is a
            multisubunit chloride channel that mediates the fastest inhibitory
            synaptic transmission in the central nervous system. This gene
            encodes GABA A receptor, beta 2 subunit. It is mapped to chromosome
            5q34 in a cluster comprised of genes encoding alpha 1 and gamma 2
            subunits of the GABA A receptor. Alternative splicing of this gene
            generates 2 transcript variants, differing by a 114 bp insertion.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the full length
            isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.105987.1,
                                           SRR1803611.104577.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..512
                     /product="gamma-aminobutyric acid receptor subunit beta-2
                     isoform 1 precursor"
                     /note="gamma-aminobutyric acid A receptor beta 2; GABA(A)
                     receptor subunit beta-2; gamma-aminobutyric acid type A
                     receptor beta2 subunit; GABAAR subunit beta-2"
                     /calculated_mol_wt=56199
     sig_peptide     1..25
                     /note="/evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P47870.2)"
                     /calculated_mol_wt=2970
     Region          9..510
                     /region_name="LIC"
                     /note="Cation transporter family protein; TIGR00860"
                     /db_xref="CDD:273305"
     mat_peptide     26..512
                     /product="Gamma-aminobutyric acid receptor subunit beta-2.
                     /id=PRO_0000000459"
                     /note="propagated from UniProtKB/Swiss-Prot (P47870.2)"
                     /calculated_mol_wt=56199
     Site            32
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P47870.2)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29950725,
                     ECO:0007744|PDB:6D6T; propagated from UniProtKB/Swiss-Prot
                     (P47870.2)"
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29950725,
                     ECO:0007744|PDB:6D6T; propagated from UniProtKB/Swiss-Prot
                     (P47870.2)"
     Site            242..262
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47870.2)"
     Site            273..292
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47870.2)"
     Site            311..331
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47870.2)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P63137; propagated from
                     UniProtKB/Swiss-Prot (P47870.2)"
     Site            491..511
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P47870.2)"
     CDS             1..512
                     /gene="GABRB2"
                     /gene_synonym="DEE92; ICEE2"
                     /coded_by="NM_021911.3:499..2037"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4355.1"
                     /db_xref="GeneID:2561"
                     /db_xref="HGNC:HGNC:4082"
                     /db_xref="MIM:600232"
ORIGIN      
        1 mwrvrkrgyf giwsfpliia avcaqsvndp snmslvketv drllkgydir lrpdfggppv
       61 avgmnidias idmvsevnmd ytltmyfqqa wrdkrlsynv iplnltldnr vadqlwvpdt
      121 yflndkksfv hgvtvknrmi rlhpdgtvly glritttaac mmdlrrypld eqnctleies
      181 ygyttddief ywrgddnavt gvtkielpqf sivdyklitk kvvfstgsyp rlslsfklkr
      241 nigyfilqty mpsilitils wvsfwinyda saarvalgit tvltmttint hlretlpkip
      301 yvkaidmylm gcfvfvfmal leyalvnyif fgrgpqrqkk aaekaasann ekmrldvnki
      361 fykdikqngt qyrslwdptg nlsptrrttn ydfslytmdp henillstle iknematsea
      421 vmglgdprst mlaydassiq yrkaglprhs fgrnalerhv aqkksrlrrr asqlkitipd
      481 ltdvnaidrw sriffpvvfs ffnivywlyy vn
//
LOCUS       NP_001374805             819 aa            linear   PRI 21-NOV-2025
DEFINITION  protein mono-ADP-ribosyltransferase PARP9 isoform b [Homo sapiens].
ACCESSION   NP_001374805 XP_016862794
VERSION     NP_001374805.1
DBSOURCE    REFSEQ: accession NM_001387876.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Pandi,K., Angabo,S., Makkawi,H., Benyamini,H., Elgavish,S. and
            Nussbaum,G.
  TITLE     P. gingivalis-Induced TLR2 Interactome Analysis Reveals Association
            with PARP9
  JOURNAL   J Dent Res 103 (3), 329-338 (2024)
   PUBMED   38344758
  REMARK    GeneRIF: P. gingivalis-Induced TLR2 Interactome Analysis Reveals
            Association with PARP9.
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Thirunavukkarasu,S., Ahmed,M., Rosa,B.A., Boothby,M., Cho,S.H.,
            Rangel-Moreno,J., Mbandi,S.K., Schreiber,V., Gupta,A., Zuniga,J.,
            Mitreva,M., Kaushal,D., Scriba,T.J. and Khader,S.A.
  TITLE     Poly(ADP-ribose) polymerase 9 mediates early protection against
            Mycobacterium tuberculosis infection by regulating type I IFN
            production
  JOURNAL   J Clin Invest 133 (12), e158630 (2023)
   PUBMED   37200107
  REMARK    GeneRIF: Poly(ADP-ribose) polymerase 9 mediates early protection
            against Mycobacterium tuberculosis infection by regulating type I
            IFN production.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 819)
  AUTHORS   Russo,L.C., Tomasin,R., Matos,I.A., Manucci,A.C., Sowa,S.T.,
            Dale,K., Caldecott,K.W., Lehtio,L., Schechtman,D., Meotti,F.C.,
            Bruni-Cardoso,A. and Hoch,N.C.
  TITLE     The SARS-CoV-2 Nsp3 macrodomain reverses PARP9/DTX3L-dependent
            ADP-ribosylation induced by interferon signaling
  JOURNAL   J Biol Chem 297 (3), 101041 (2021)
   PUBMED   34358560
  REMARK    GeneRIF: The SARS-CoV-2 Nsp3 macrodomain reverses
            PARP9/DTX3L-dependent ADP-ribosylation induced by interferon
            signaling.
REFERENCE   5  (residues 1 to 819)
  AUTHORS   Xing,J., Zhang,A., Du,Y., Fang,M., Minze,L.J., Liu,Y.J., Li,X.C.
            and Zhang,Z.
  TITLE     Identification of poly(ADP-ribose) polymerase 9 (PARP9) as a
            noncanonical sensor for RNA virus in dendritic cells
  JOURNAL   Nat Commun 12 (1), 2681 (2021)
   PUBMED   33976210
  REMARK    GeneRIF: Identification of poly(ADP-ribose) polymerase 9 (PARP9) as
            a noncanonical sensor for RNA virus in dendritic cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 819)
  AUTHORS   Jha,R., Agarwal,A., Mahfouz,R., Paasch,U., Grunewald,S.,
            Sabanegh,E., Yadav,S.P. and Sharma,R.
  TITLE     Determination of Poly (ADP-ribose) polymerase (PARP) homologues in
            human ejaculated sperm and its correlation with sperm maturation
  JOURNAL   Fertil Steril 91 (3), 782-790 (2009)
   PUBMED   18339380
  REMARK    GeneRIF: Determination of Poly (ADP-ribose) polymerase (PARP)
            homologues in human ejaculated sperm and its correlation with sperm
            maturation.
REFERENCE   7  (residues 1 to 819)
  AUTHORS   Juszczynski,P., Kutok,J.L., Li,C., Mitra,J., Aguiar,R.C. and
            Shipp,M.A.
  TITLE     BAL1 and BBAP are regulated by a gamma interferon-responsive
            bidirectional promoter and are overexpressed in diffuse large
            B-cell lymphomas with a prominent inflammatory infiltrate
  JOURNAL   Mol Cell Biol 26 (14), 5348-5359 (2006)
   PUBMED   16809771
  REMARK    GeneRIF: BAL1 and BBAP are located on chromosome 3q21 in a
            head-to-head orientation and are regulated by a
            IFN-gamma-responsive bidirectional promoter.
REFERENCE   8  (residues 1 to 819)
  AUTHORS   Aguiar,R.C., Takeyama,K., He,C., Kreinbrink,K. and Shipp,M.A.
  TITLE     B-aggressive lymphoma family proteins have unique domains that
            modulate transcription and exhibit poly(ADP-ribose) polymerase
            activity
  JOURNAL   J Biol Chem 280 (40), 33756-33765 (2005)
   PUBMED   16061477
REFERENCE   9  (residues 1 to 819)
  AUTHORS   Takeyama,K., Aguiar,R.C., Gu,L., He,C., Freeman,G.J., Kutok,J.L.,
            Aster,J.C. and Shipp,M.A.
  TITLE     The BAL-binding protein BBAP and related Deltex family members
            exhibit ubiquitin-protein isopeptide ligase activity
  JOURNAL   J Biol Chem 278 (24), 21930-21937 (2003)
   PUBMED   12670957
REFERENCE   10 (residues 1 to 819)
  AUTHORS   Aguiar,R.C., Yakushijin,Y., Kharbanda,S., Salgia,R., Fletcher,J.A.
            and Shipp,M.A.
  TITLE     BAL is a novel risk-related gene in diffuse large B-cell lymphomas
            that enhances cellular migration
  JOURNAL   Blood 96 (13), 4328-4334 (2000)
   PUBMED   11110709
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092908.9 and AC096861.5.
            
            On Oct 14, 2020 this sequence version replaced XP_016862794.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.432446.1,
                                           SRR14038194.623359.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.1"
     Protein         1..819
                     /product="protein mono-ADP-ribosyltransferase PARP9
                     isoform b"
                     /EC_number="2.4.2.30"
                     /note="poly [ADP-ribose] polymerase 9; poly (ADP-ribose)
                     polymerase 9; PARP-9; b aggressive lymphoma protein;
                     ADP-ribosyltransferase diphtheria toxin-like 9; protein
                     mono-ADP-ribosyltransferase PARP9"
                     /calculated_mol_wt=92141
     Region          82..242
                     /region_name="Macro_Af1521_BAL-like"
                     /note="macrodomain, Af1521-like family; cd02907"
                     /db_xref="CDD:394877"
     Site            order(90..92,103..105,109..115,117,203..209)
                     /site_type="other"
                     /note="ADP-ribose binding site [chemical binding]"
                     /db_xref="CDD:394877"
     Region          275..451
                     /region_name="Macro_BAL-like"
                     /note="macrodomain, B-aggressive lymphoma (BAL)-like
                     family; cd02903"
                     /db_xref="CDD:394874"
     Site            order(290..292,302..304,310..313,316,394..400,434,440)
                     /site_type="other"
                     /note="ADP-ribose binding site [chemical binding]"
                     /db_xref="CDD:394874"
     Region          667..786
                     /region_name="TCCD_inducible_PARP_like"
                     /note="Poly(ADP-ribose) polymerases catalyse the covalent
                     attachment of ADP-ribose units from NAD+ to itself and to
                     a limited number of other DNA binding proteins, which
                     decreases their affinity for DNA. Poly(ADP-ribose)
                     polymerase is a regulatory component...; cd01439"
                     /db_xref="CDD:238719"
     Site            order(669..673,676,680,684..686,688,701..703,713,769)
                     /site_type="other"
                     /note="nad+ binding pocket [chemical binding]"
                     /db_xref="CDD:238719"
     CDS             1..819
                     /gene="PARP9"
                     /gene_synonym="ARTD9; BAL; BAL1; MGC:7868"
                     /coded_by="NM_001387876.1:143..2602"
                     /note="isoform b is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS54634.1"
                     /db_xref="GeneID:83666"
                     /db_xref="HGNC:HGNC:24118"
                     /db_xref="MIM:612065"
ORIGIN      
        1 mdfsmvagaa ayneksetga lgenyswqip inhndfkilk nnerqlcevl qnkfgcistl
       61 vspvqegnsk slqvfrkmlt prielsvwkd dltthavdav vnaanedllh ggglalalvk
      121 aggfeiqees kqfvarygkv sageiavtga grlpckqiih avgprwmewd kqgctgklqr
      181 aivsilnyvi yknthiktva ipalssgifq fplnlctkti vetirvslqg kpmmsnlkei
      241 hlvsnedptv aafkaasefi lgkselgqet tpsfnamvvn nltlqivqgh iewqtadviv
      301 nsvnphditv gpvaksilqq agvemksefl atkakqfqrs qlvlvtkgfn lfckyiyhvl
      361 whsefpkpqi lkhamkecle kcieqnitsi sfpalgtgnm eikketaaei lfdevltfak
      421 dhvkhqltvk fvifptdlei ykafssemak rskmlslnny svpqstreek renglearsp
      481 ainlmgfnve emyeahawiq rilslqnhhi iennhilylg rkehdilsql qktssvsite
      541 iispgrtele iegaradlie vvmniedmlc kvqeemarkk erglwrslgq wtiqqqktqd
      601 emkeniiflk cpvpptqell dqkkqfekcg lqvlkvekid nevlmaafqr kkkmmeeklh
      661 rqpvshrlfq qvpyqfcnvv crvgfqrmys tpcdpkygag iyftknlknl aekakkisaa
      721 dkliyvfeae vltgffcqgh plnivpppls pgaidghdsv vdnvsspetf vifsgmqaip
      781 qylwtctqey vqsqdyssgp mrpfaqhpwr gfasgspvd
//
LOCUS       NP_001383895             509 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 33 [Homo sapiens].
ACCESSION   NP_001383895 XP_011530592
VERSION     NP_001383895.1
DBSOURCE    REFSEQ: accession NM_001396966.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 509)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 509)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 509)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 509)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            On Oct 28, 2021 this sequence version replaced XP_011530592.1.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..509
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 33"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=57418
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          356..483
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..509
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001396966.1:671..2200"
                     /note="isoform 33 is encoded by transcript variant 36"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaksll kkpdgvkkrk ssssvqmmes tessnttied edvkarkqei
      361 ikvteqliea inngdfeayt kicdpgltaf epealgnlve gmdfhrfyfe nalsksnkpi
      421 htiilnphvh lvgddaacia yirltqymdg sgmpktmqse etrvwhrrdg kwqnvhfhrs
      481 gsptvpikpp cipngkenfs ggtslwqni
//
LOCUS       NP_001381450             488 aa            linear   PRI 21-NOV-2025
DEFINITION  protein THEMIS isoform 6 [Homo sapiens].
ACCESSION   NP_001381450
VERSION     NP_001381450.1
DBSOURCE    REFSEQ: accession NM_001394521.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Sun,C., Shou,P., Du,H., Hirabayashi,K., Chen,Y., Herring,L.E.,
            Ahn,S., Xu,Y., Suzuki,K., Li,G., Tsahouridis,O., Su,L., Savoldo,B.
            and Dotti,G.
  TITLE     THEMIS-SHP1 Recruitment by 4-1BB Tunes LCK-Mediated Priming of
            Chimeric Antigen Receptor-Redirected T Cells
  JOURNAL   Cancer Cell 37 (2), 216-225 (2020)
   PUBMED   32004441
  REMARK    GeneRIF: THEMIS-SHP1 Recruitment by 4-1BB Tunes LCK-Mediated
            Priming of Chimeric Antigen Receptor-Redirected T Cells
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Choi,S., Warzecha,C., Zvezdova,E., Lee,J., Argenty,J., Lesourne,R.,
            Aravind,L. and Love,P.E.
  TITLE     THEMIS enhances TCR signaling and enables positive selection by
            selective inhibition of the phosphatase SHP-1
  JOURNAL   Nat Immunol 18 (4), 433-441 (2017)
   PUBMED   28250424
  REMARK    GeneRIF: we found that THEMIS directly regulated the catalytic
            activity of the tyrosine phosphatase SHP-1.
            Erratum:[Nat Immunol. 2017 May 18;18(6):705. doi:
            10.1038/ni0617-705c. PMID: 28518157]
REFERENCE   5  (residues 1 to 488)
  AUTHORS   Kinosada,H., Yasunaga,J.I., Shimura,K., Miyazato,P., Onishi,C.,
            Iyoda,T., Inaba,K. and Matsuoka,M.
  TITLE     HTLV-1 bZIP Factor Enhances T-Cell Proliferation by Impeding the
            Suppressive Signaling of Co-inhibitory Receptors
  JOURNAL   PLoS Pathog 13 (1), e1006120 (2017)
   PUBMED   28046066
  REMARK    Erratum:[PLoS Pathog. 2017 Feb 23;13(2):e1006228. doi:
            10.1371/journal.ppat.1006228. PMID: 28231270]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 488)
  AUTHORS   Kakugawa,K., Yasuda,T., Miura,I., Kobayashi,A., Fukiage,H.,
            Satoh,R., Matsuda,M., Koseki,H., Wakana,S., Kawamoto,H. and
            Yoshida,H.
  TITLE     A novel gene essential for the development of single positive
            thymocytes
  JOURNAL   Mol Cell Biol 29 (18), 5128-5135 (2009)
   PUBMED   19620281
REFERENCE   7  (residues 1 to 488)
  AUTHORS   Allen,P.M.
  TITLE     Themis imposes new law and order on positive selection
  JOURNAL   Nat Immunol 10 (8), 805-806 (2009)
   PUBMED   19621038
REFERENCE   8  (residues 1 to 488)
  AUTHORS   Fu,G., Vallee,S., Rybakin,V., McGuire,M.V., Ampudia,J.,
            Brockmeyer,C., Salek,M., Fallen,P.R., Hoerter,J.A., Munshi,A.,
            Huang,Y.H., Hu,J., Fox,H.S., Sauer,K., Acuto,O. and Gascoigne,N.R.
  TITLE     Themis controls thymocyte selection through regulation of T cell
            antigen receptor-mediated signaling
  JOURNAL   Nat Immunol 10 (8), 848-856 (2009)
   PUBMED   19597499
  REMARK    GeneRIF: Functional analysis of the mouse gene by knockout, and
            comparison of the mouse and human proteins.
REFERENCE   9  (residues 1 to 488)
  AUTHORS   Lesourne,R., Uehara,S., Lee,J., Song,K.D., Li,L., Pinkhasov,J.,
            Zhang,Y., Weng,N.P., Wildt,K.F., Wang,L., Bosselut,R. and Love,P.E.
  TITLE     Themis, a T cell-specific protein important for late thymocyte
            development
  JOURNAL   Nat Immunol 10 (8), 840-847 (2009)
   PUBMED   19597498
  REMARK    GeneRIF: Functional characterization of the homologous mouse gene.
            Erratum:[Nat Immunol. 2010 Jan;11(1):97]
REFERENCE   10 (residues 1 to 488)
  AUTHORS   Johnson,A.L., Aravind,L., Shulzhenko,N., Morgun,A., Choi,S.Y.,
            Crockford,T.L., Lambe,T., Domaschenz,H., Kucharska,E.M., Zheng,L.,
            Vinuesa,C.G., Lenardo,M.J., Goodnow,C.C., Cornall,R.J. and
            Schwartz,R.H.
  TITLE     Themis is a member of a new metazoan gene family and is required
            for the completion of thymocyte positive selection
  JOURNAL   Nat Immunol 10 (8), 831-839 (2009)
   PUBMED   19597497
  REMARK    Erratum:[Nat Immunol. 2010 Jan;11(1):97]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL035470.10, AL365224.8 and
            AL356432.17.
            
            Summary: This gene encodes a protein that plays a regulatory role
            in both positive and negative T-cell selection during late
            thymocyte development. The protein functions through T-cell antigen
            receptor signaling, and is necessary for proper lineage commitment
            and maturation of T-cells. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA2149876 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.33"
     Protein         1..488
                     /product="protein THEMIS isoform 6"
                     /note="thymocyte selection pathway associated;
                     GRB2-associated protein; signaling phosphoprotein specific
                     for T cells; thymocyte-expressed molecule involved in
                     selection; protein THEMIS"
                     /calculated_mol_wt=55456
     Region          128..376
                     /region_name="CABIT"
                     /note="Cell-cycle sustaining, positive selection;
                     pfam12736"
                     /db_xref="CDD:463686"
     CDS             1..488
                     /gene="THEMIS"
                     /gene_synonym="C6orf190; C6orf207; GASP; SPOT; THEMIS1;
                     TSEPA"
                     /coded_by="NM_001394521.1:127..1593"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:387357"
                     /db_xref="HGNC:HGNC:21569"
                     /db_xref="MIM:613607"
ORIGIN      
        1 malsleefvh sldlrtlprv leiqagiyle gsiyemfgne ccfstgevik itglkvkkii
       61 aeiceqiegc eslqpfelpm nfpvrkdiir ilpsldvevk ditdsydanw flqllstedl
      121 femtskefpi vtevieapeg nhlpqsilqp gktivihkky qasrilasei rsnfpkrhfl
      181 iptsykgkfk rrprefptay dleiakseke plhvvatkaf hsphdklssv svgdqflvhq
      241 settevlceg ikkvvnvlac ekilkksyea allplymegg fvevihdkkq ypiselckqf
      301 rlpfnvkvsv rdlsieedvl aatpglqlee ditdsyllis dfanptecwe ipvgrlnmtv
      361 qlvsnfsrda epflvrtlve eiteeqyymm rryessashp pprppkhpsv eetkltlltl
      421 aeertvdlpk spkrhhvdit kklhpnqagl dskvligsqn dlvdeekers nrgataiaet
      481 fknekhqk
//
LOCUS       NP_001180231             629 aa            linear   PRI 21-NOV-2025
DEFINITION  semaphorin-4A isoform 2 [Homo sapiens].
ACCESSION   NP_001180231
VERSION     NP_001180231.1
DBSOURCE    REFSEQ: accession NM_001193302.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Hou,T., Zhang,P., Tian,H., Luo,Y., Li,J., Zhang,K. and Li,Y.
  TITLE     Semaphorin 4A Maintains Trophoblastic Function via Activating the
            STAT3 Pathway
  JOURNAL   Biomolecules 14 (7), 826 (2024)
   PUBMED   39062540
  REMARK    GeneRIF: Semaphorin 4A Maintains Trophoblastic Function via
            Activating the STAT3 Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Wei,X., Liu,Z., Shen,Y., Dong,H., Chen,K., Shi,X., Chen,Y., Wang,B.
            and Dong,S.
  TITLE     Semaphorin4A promotes lung cancer by activation of NF-kappaB
            pathway mediated by PlexinB1
  JOURNAL   PeerJ 11, e16292 (2023)
   PUBMED   37901456
  REMARK    GeneRIF: Semaphorin4A promotes lung cancer by activation of
            NF-kappaB pathway mediated by PlexinB1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Naito,Y., Koyama,S., Masuhiro,K., Hirai,T., Uenami,T., Inoue,T.,
            Osa,A., Machiyama,H., Watanabe,G., Sax,N., Villa,J.,
            Kinugasa-Katayama,Y., Nojima,S., Yaga,M., Hosono,Y., Okuzaki,D.,
            Satoh,S., Tsuda,T., Nakanishi,Y., Suga,Y., Morita,T., Fukushima,K.,
            Nishide,M., Shiroyama,T., Miyake,K., Iwahori,K., Hirata,H.,
            Nagatomo,I., Yano,Y., Tamiya,M., Kumagai,T., Takemoto,N.,
            Inohara,H., Yamasaki,S., Yamashita,K., Aoshi,T., Akbay,E.A.,
            Hosen,N., Shintani,Y., Takamatsu,H., Mori,M., Takeda,Y. and
            Kumanogoh,A.
  TITLE     Tumor-derived semaphorin 4A improves PD-1-blocking antibody
            efficacy by enhancing CD8+ T cell cytotoxicity and proliferation
  JOURNAL   Sci Adv 9 (20), eade0718 (2023)
   PUBMED   37205755
  REMARK    GeneRIF: Tumor-derived semaphorin 4A improves PD-1-blocking
            antibody efficacy by enhancing CD8[+] T cell cytotoxicity and
            proliferation.
REFERENCE   4  (residues 1 to 629)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 629)
  AUTHORS   Eiza,N., Garty,M., Staun-Ram,E., Miller,A. and Vadasz,Z.
  TITLE     The possible involvement of sema3A and sema4A in the pathogenesis
            of multiple sclerosis
  JOURNAL   Clin Immunol 238, 109017 (2022)
   PUBMED   35460904
  REMARK    GeneRIF: The possible involvement of sema3A and sema4A in the
            pathogenesis of multiple sclerosis.
REFERENCE   6  (residues 1 to 629)
  AUTHORS   Kumanogoh,A. and Kikutani,H.
  TITLE     Immune semaphorins: a new area of semaphorin research
  JOURNAL   J Cell Sci 116 (Pt 17), 3463-3470 (2003)
   PUBMED   12893810
  REMARK    Review article
REFERENCE   7  (residues 1 to 629)
  AUTHORS   Kikutani,H. and Kumanogoh,A.
  TITLE     Semaphorins in interactions between T cells and antigen-presenting
            cells
  JOURNAL   Nat Rev Immunol 3 (2), 159-167 (2003)
   PUBMED   12563299
  REMARK    Review article
REFERENCE   8  (residues 1 to 629)
  AUTHORS   Kumanogoh,A., Marukawa,S., Suzuki,K., Takegahara,N., Watanabe,C.,
            Ch'ng,E., Ishida,I., Fujimura,H., Sakoda,S., Yoshida,K. and
            Kikutani,H.
  TITLE     Class IV semaphorin Sema4A enhances T-cell activation and interacts
            with Tim-2
  JOURNAL   Nature 419 (6907), 629-633 (2002)
   PUBMED   12374982
REFERENCE   9  (residues 1 to 629)
  AUTHORS   Puschel,A.W., Adams,R.H. and Betz,H.
  TITLE     Murine semaphorin D/collapsin is a member of a diverse gene family
            and creates domains inhibitory for axonal extension
  JOURNAL   Neuron 14 (5), 941-948 (1995)
   PUBMED   7748561
REFERENCE   10 (residues 1 to 629)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK091127.1 and AY358531.1.
            
            Summary: This gene encodes a member of the semaphorin family of
            soluble and transmembrane proteins. Semaphorins are involved in
            numerous functions, including axon guidance, morphogenesis,
            carcinogenesis, and immunomodulation. The encoded protein is a
            single-pass type I membrane protein containing an
            immunoglobulin-like C2-type domain, a PSI domain and a sema domain.
            It inhibits axonal extension by providing local signals to specify
            territories inaccessible for growing axons. It is an activator of
            T-cell-mediated immunity and suppresses vascular endothelial growth
            factor (VEGF)-mediated endothelial cell migration and proliferation
            in vitro and angiogenesis in vivo. Mutations in this gene are
            associated with retinal degenerative diseases including retinitis
            pigmentosa type 35 (RP35) and cone-rod dystrophy type 10 (CORD10).
            Multiple alternatively spliced transcript variants encoding
            different isoforms have been identified.[provided by RefSeq, Sep
            2010].
            
            Transcript Variant: This variant (4) lacks two internal exons in 5'
            different regions respectively, resulting in a downstream AUG start
            codon, as compared to variant 1. The resulting isoform (2) is
            shorter at the N-terminus and lacks an internal segment, as
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK091127.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..629
                     /product="semaphorin-4A isoform 2"
                     /note="sema B; semaphorin-B; sema domain, immunoglobulin
                     domain (Ig), transmembrane domain (TM) and short
                     cytoplasmic domain, (semaphorin) 4A"
                     /calculated_mol_wt=68973
     Region          1..363
                     /region_name="Sema"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorins and plexins; cl15693"
                     /db_xref="CDD:472829"
     Region          364..408
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          434..506
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          444..448
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          456..460
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          475..479
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          489..494
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..629
                     /gene="SEMA4A"
                     /gene_synonym="CORD10; RP35; SEMAB; SEMB"
                     /coded_by="NM_001193302.2:339..2228"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS53378.1"
                     /db_xref="GeneID:64218"
                     /db_xref="HGNC:HGNC:10729"
                     /db_xref="MIM:607292"
ORIGIN      
        1 mipwpasdrk ksecafkkks neelqdsyll pisedkvmeg kgqspfdpah khtavlvdgm
       61 lysgtmnnfl gsepilmrtl gsqpvlktdn flrwlhhdas fvaaipstqv vyfffeetas
      121 efdfferlht srvarvcknd vggekllqkk wttflkaqll ctqpgqlpfn virhavllpa
      181 dsptaphiya vftsqwqvgg trssavcafs lldiervfkg kykelnkets rwttyrgpet
      241 nprpgscsvg pssdkaltfm kdhflmdeqv vgtpllvksg veytrlavet aqgldghshl
      301 vmylgtttgs lhkavvsgds sahlveeiql fpdpepvrnl qlaptqgavf vgfsggvwrv
      361 prancsvyes cvdcvlardp hcawdpesrt ccllsapnln swkqdmergn pewacasgpm
      421 srslrpqsrp qiikevlavp nsilelpcph lsalasyyws hgpaavpeas stvyngslll
      481 ivqdgvggly qcwatengfs ypvisywvds qdqtlaldpe lagiprehvk vpltrvsgga
      541 alaaqqsywp hfvtvtvlfa lvlsgaliil vasplralra rgkvqgcetl rpgekaplsr
      601 eqhlqspkec rtsasdvdad nnclgteva
//
LOCUS       NP_001335674            1031 aa            linear   PRI 21-NOV-2025
DEFINITION  kinase D-interacting substrate of 220 kDa isoform 11 [Homo
            sapiens].
ACCESSION   NP_001335674
VERSION     NP_001335674.1
DBSOURCE    REFSEQ: accession NM_001348745.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1031)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1031)
  AUTHORS   Zhang,J., Zhang,Y., Shang,Q., Cheng,Y., Su,Y., Zhang,J., Wang,T.,
            Ding,J., Li,Y., Xie,Y. and Xing,Q.
  TITLE     Gain-of-Function KIDINS220 Variants Disrupt Neuronal Development
            and Cause Cerebral Palsy
  JOURNAL   Mov Disord 39 (3), 498-509 (2024)
   PUBMED   38148610
  REMARK    GeneRIF: Gain-of-Function KIDINS220 Variants Disrupt Neuronal
            Development and Cause Cerebral Palsy.
REFERENCE   3  (residues 1 to 1031)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1031)
  AUTHORS   Bondeson,D.P., Paolella,B.R., Asfaw,A., Rothberg,M.V.,
            Skipper,T.A., Langan,C., Mesa,G., Gonzalez,A., Surface,L.E.,
            Ito,K., Kazachkova,M., Colgan,W.N., Warren,A., Dempster,J.M.,
            Krill-Burger,J.M., Ericsson,M., Tang,A.A., Fung,I., Chambers,E.S.,
            Abdusamad,M., Dumont,N., Doench,J.G., Piccioni,F., Root,D.E.,
            Boehm,J., Hahn,W.C., Mannstadt,M., McFarland,J.M., Vazquez,F. and
            Golub,T.R.
  TITLE     Phosphate dysregulation via the XPR1-KIDINS220 protein complex is a
            therapeutic vulnerability in ovarian cancer
  JOURNAL   Nat Cancer 3 (6), 681-695 (2022)
   PUBMED   35437317
  REMARK    GeneRIF: Phosphate dysregulation via the XPR1-KIDINS220 protein
            complex is a therapeutic vulnerability in ovarian cancer.
REFERENCE   5  (residues 1 to 1031)
  AUTHORS   Scholz-Starke,J. and Cesca,F.
  TITLE     Stepping Out of the Shade: Control of Neuronal Activity by the
            Scaffold Protein Kidins220/ARMS
  JOURNAL   Front Cell Neurosci 10, 68 (2016)
   PUBMED   27013979
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1031)
  AUTHORS   Arevalo,J.C., Yano,H., Teng,K.K. and Chao,M.V.
  TITLE     A unique pathway for sustained neurotrophin signaling through an
            ankyrin-rich membrane-spanning protein
  JOURNAL   EMBO J 23 (12), 2358-2368 (2004)
   PUBMED   15167895
REFERENCE   7  (residues 1 to 1031)
  AUTHORS   Riol-Blanco,L., Iglesias,T., Sanchez-Sanchez,N., de la Rosa,G.,
            Sanchez-Ruiloba,L., Cabrera-Poch,N., Torres,A., Longo,I.,
            Garcia-Bordas,J., Longo,N., Tejedor,A., Sanchez-Mateos,P. and
            Rodriguez-Fernandez,J.L.
  TITLE     The neuronal protein Kidins220 localizes in a raft compartment at
            the leading edge of motile immature dendritic cells
  JOURNAL   Eur J Immunol 34 (1), 108-118 (2004)
   PUBMED   14971036
REFERENCE   8  (residues 1 to 1031)
  AUTHORS   Kong,H., Boulter,J., Weber,J.L., Lai,C. and Chao,M.V.
  TITLE     An evolutionarily conserved transmembrane protein that is a novel
            downstream target of neurotrophin and ephrin receptors
  JOURNAL   J Neurosci 21 (1), 176-185 (2001)
   PUBMED   11150334
REFERENCE   9  (residues 1 to 1031)
  AUTHORS   Iglesias,T., Cabrera-Poch,N., Mitchell,M.P., Naven,T.J.,
            Rozengurt,E. and Schiavo,G.
  TITLE     Identification and cloning of Kidins220, a novel neuronal substrate
            of protein kinase D
  JOURNAL   J Biol Chem 275 (51), 40048-40056 (2000)
   PUBMED   10998417
REFERENCE   10 (residues 1 to 1031)
  AUTHORS   Kaplan,D.R. and Miller,F.D.
  TITLE     Signal transduction by the neurotrophin receptors
  JOURNAL   Curr Opin Cell Biol 9 (2), 213-221 (1997)
   PUBMED   9069267
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012495.9 and AL133620.1.
            
            Summary: This gene encodes a transmembrane protein that is
            preferentially expressed in the nervous system where it controls
            neuronal cell survival, differentiation into exons and dendrites,
            and synaptic plasticity. The encoded protein interacts with
            membrane receptors, cytosolic signaling components, and
            cytoskeletal proteins, serving as a scaffold that mediates
            crosstalk between the neurotrophin pathway and several other
            intracellular signaling pathways. Aberrant expression of this gene
            is associated with the onset of various neuropsychiatric disorders
            and neurodegenerative diseases, including Alzheimer's disease.
            Naturally occurring mutations in this gene are associated with a
            syndrome characterized by spastic paraplegia, intellectual
            disability, nystagmus and obesity. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Feb 2017].
            
            Transcript Variant: This variant (14) has multiple coding region
            differences and differs in the 3' UTR, compared to variant 1. The
            encoded isoform (11) is shorter and has a distinct C-terminus,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL133620.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1031
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.1"
     Protein         1..1031
                     /product="kinase D-interacting substrate of 220 kDa
                     isoform 11"
                     /note="ankyrin repeat-rich membrane-spanning protein;
                     kinase D-interacting substrate 220kDa"
                     /calculated_mol_wt=115181
     Region          4..33
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          18..307
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          37..66
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          38..68
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(39,43..44,47..49,51..52,56,59,68,70,72,76..77,
                     80..82,84..85,89,92,101,103,105,109..110,113..115,
                     117..118,122,125)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          70..101
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          70..99
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          103..132
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          103..132
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          137..166
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          170..199
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          170..198
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          203..232
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          236..267
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          236..265
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          269..299
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          269..298
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          274..366
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Region          302..332
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          302..331
                     /region_name="ANK 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          335..366
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          335..364
                     /region_name="ANK 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          <349..413
                     /region_name="PHA02736"
                     /note="Viral ankyrin protein; Provisional"
                     /db_xref="CDD:165103"
     Region          368..397
                     /region_name="ANK 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          441..954
                     /region_name="KAP_NTPase"
                     /note="KAP family P-loop domain; pfam07693"
                     /db_xref="CDD:462231"
     Site            501..521
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            526..546
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            661..681
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            687..707
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            883
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            915
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Site            919
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9ULH0.3)"
     Region          <1010..>1030
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     CDS             1..1031
                     /gene="KIDINS220"
                     /gene_synonym="ARMS; SINO; VENARG"
                     /coded_by="NM_001348745.2:171..3266"
                     /note="isoform 11 is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS86819.1"
                     /db_xref="GeneID:57498"
                     /db_xref="HGNC:HGNC:29508"
                     /db_xref="MIM:615759"
ORIGIN      
        1 msvlisqsvi nyveeenipa lkallekckd vdernecgqt plmiaaeqgn leivkelikn
       61 gancnledld nwtalisask eghvhiveel lkcgvnlehr dmggwtalmw acykgrtdvv
      121 elllshganp svtglqysvy piiwaagrgh adivhlllqn gakvncsdky gttplvwaar
      181 kghlecvkhl lamgadvdqe gansmtaliv avkggytqsv keilkrnpnv nltdkdgnta
      241 lmiaskeght eivqdlldag tyvnipdrsg dtvligavrg ghveivrall qkyadidirg
      301 qdnktalywa vekgnatmvr dilqcnpdte ictkdgetpl ikatkmrnie vvellldkga
      361 kvsavdkkgd tplhiairgr srklaelllr npkdgrllyr pnkagetpyn idcshqksil
      421 tqifgarhls ptetdgdmlg ydlyssalad ilseptmqpp icvglyaqwg sgksfllkkl
      481 edemktfagq qieplfqfsw livfltlllc gglgllfaft vhpnlgiavs lsflallyif
      541 fiviyfggrr egeswnwawv lstrlarhig ylelllklmf vnppelpeqt tkalpvrflf
      601 tdynrlssvg getslaemia tlsdaceref gflatrlfrv fktedtqgkk kwkktcclps
      661 fviflfiigc iisgitllai frvdpkhltv navlisiasv vglafvlncr twwqvldsll
      721 nsqrkrlhna asklhklkse gfmkvlkcev elmarmakti dsftqnqtrl vviidgldac
      781 eqdkvlqmld tvrvlfskgp fiaifasdph iiikainqnl nsvlrdsnin ghdymrnivh
      841 lpvflnsrgl snarkflvts atngdvpcsd ttgiqedadr rvsqnslgem tklgsktaln
      901 rrdtyrrrqm qrtitrqmsf dltkllvted wfsdispqtm rrllnivsvt grllranqis
      961 fnwdrlaswi nlteqwpyrt swlilyleet egipdqmtlk tiyerccgad scdrdrigis
     1021 ksvlvamlme s
//
LOCUS       NP_001307783             547 aa            linear   PRI 21-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 7 isoform g [Homo sapiens].
ACCESSION   NP_001307783
VERSION     NP_001307783.1
DBSOURCE    REFSEQ: accession NM_001320854.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Kawase,N., Sugihara,A., Kajiwara,K., Hiroshima,M., Akamatsu,K.,
            Nada,S., Matsumoto,K., Ueda,M. and Okada,M.
  TITLE     SRC kinase activator CDCP1 promotes hepatocyte growth
            factor-induced cell migration/invasion of a subset of breast cancer
            cells
  JOURNAL   J Biol Chem 298 (3), 101630 (2022)
   PUBMED   35085554
  REMARK    GeneRIF: SRC kinase activator CDCP1 promotes hepatocyte growth
            factor-induced cell migration/invasion of a subset of breast cancer
            cells.
REFERENCE   4  (residues 1 to 547)
  AUTHORS   Keum,S., Yang,S.J., Park,E., Kang,T., Choi,J.H., Jeong,J.,
            Hwang,Y.E., Kim,J.W., Park,D. and Rhee,S.
  TITLE     Beta-Pix-dynamin 2 complex promotes colorectal cancer progression
            by facilitating membrane dynamics
  JOURNAL   Cell Oncol (Dordr) 44 (6), 1287-1305 (2021)
   PUBMED   34582006
  REMARK    GeneRIF: Beta-Pix-dynamin 2 complex promotes colorectal cancer
            progression by facilitating membrane dynamics.
REFERENCE   5  (residues 1 to 547)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 547)
  AUTHORS   Turner,C.E., Brown,M.C., Perrotta,J.A., Riedy,M.C.,
            Nikolopoulos,S.N., McDonald,A.R., Bagrodia,S., Thomas,S. and
            Leventhal,P.S.
  TITLE     Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin
            repeat, ARF-GAP protein: A role in cytoskeletal remodeling
  JOURNAL   J Cell Biol 145 (4), 851-863 (1999)
   PUBMED   10330411
REFERENCE   7  (residues 1 to 547)
  AUTHORS   Aghazadeh,B., Zhu,K., Kubiseski,T.J., Liu,G.A., Pawson,T., Zheng,Y.
            and Rosen,M.K.
  TITLE     Structure and mutagenesis of the Dbl homology domain
  JOURNAL   Nat Struct Biol 5 (12), 1098-1107 (1998)
   PUBMED   9846881
REFERENCE   8  (residues 1 to 547)
  AUTHORS   Bagrodia,S., Taylor,S.J., Jordon,K.A., Van Aelst,L. and
            Cerione,R.A.
  TITLE     A novel regulator of p21-activated kinases
  JOURNAL   J Biol Chem 273 (37), 23633-23636 (1998)
   PUBMED   9726964
REFERENCE   9  (residues 1 to 547)
  AUTHORS   Manser,E., Loo,T.H., Koh,C.G., Zhao,Z.S., Chen,X.Q., Tan,L.,
            Tan,I., Leung,T. and Lim,L.
  TITLE     PAK kinases are directly coupled to the PIX family of nucleotide
            exchange factors
  JOURNAL   Mol Cell 1 (2), 183-192 (1998)
   PUBMED   9659915
REFERENCE   10 (residues 1 to 547)
  AUTHORS   Oh,W.K., Yoo,J.C., Jo,D., Song,Y.H., Kim,M.G. and Park,D.
  TITLE     Cloning of a SH3 domain-containing proline-rich protein, p85SPR,
            and its localization in focal adhesion
  JOURNAL   Biochem Biophys Res Commun 235 (3), 794-798 (1997)
   PUBMED   9207241
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK308897.1, AK295472.1,
            BC060776.1, BM677392.1, DB180957.1 and AK093326.1.
            
            Summary: This gene encodes a protein that belongs to a family of
            cytoplasmic proteins that activate the Ras-like family of Rho
            proteins by exchanging bound GDP for GTP. It forms a complex with
            the small GTP binding protein Rac1 and recruits Rac1 to membrane
            ruffles and to focal adhesions. Multiple alternatively spliced
            transcript variants encoding different isoforms have been observed
            for this gene. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (9) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at an
            alternate start codon compared to variant 1. The encoded isoform
            (g) has a distinct, shorter N-terminus, compared to isoform c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295472.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..547
                     /product="rho guanine nucleotide exchange factor 7 isoform
                     g"
                     /note="SH3 domain-containing proline-rich protein;
                     PAK-interacting exchange factor beta; Rho guanine
                     nucleotide exchange factor (GEF) 7"
                     /calculated_mol_wt=61499
     Region          16..193
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(22,26,120,144..145,148..149,151..152,155..156,
                     159..160,163,189,193)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          224..322
                     /region_name="PH_Cool_Pix"
                     /note="Cloned out of library/PAK-interactive exchange
                     factor pleckstrin homology (PH) domain; cd01225"
                     /db_xref="CDD:269932"
     Region          382..472
                     /region_name="RhoGEF67_u2"
                     /note="Unstructured region two on RhoGEF 6 and 7;
                     pfam16614"
                     /db_xref="CDD:465200"
     CDS             1..547
                     /gene="ARHGEF7"
                     /gene_synonym="BETA-PIX; COOL-1; COOL1; Nbla10314; P50;
                     P50BP; P85; P85COOL1; P85SPR; PAK3; PIXB"
                     /coded_by="NM_001320854.2:110..1753"
                     /note="isoform g is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS81781.1"
                     /db_xref="GeneID:8874"
                     /db_xref="HGNC:HGNC:15607"
                     /db_xref="MIM:605477"
ORIGIN      
        1 mgscssqsvq ktrrgrkvvl qnileteney skelqtvlst ylrplqtsek lssanisylm
       61 gnleeicsfq qmlvqsleec tklpeaqqrv ggcflnlmpq mktlyltyca nhpsavnvlt
      121 ehseelgefm etkgasspgi lvlttglskp fmrldkyptl lkelerhmed yhtdrqdiqk
      181 smaafknlsa qcqevrkrke lelqilteai rnwegddikt lgnvtymsqv liqcagseek
      241 nerylllfpn vllmlsaspr msgfiyqgkl pttgmtitkl edsenhrnaf eisgsmieri
      301 lvscnnqqdl qewvehlqkq tkvtsvgnpt ikphsvpsht lpshpvtpss khadskpapl
      361 tpayhtlphp shhgtphtti nwgpleppkt pkpwslsclr papplrpsaa lcykedlsks
      421 pktmkkllpk rkperkpsde efasrkstaa leedaqilkv ieayctsakt rqtlnstwqg
      481 tdlmhnhvla dddqpsldsl grrsslsrle psdlsedsdy dsiwtahsyr mgstsrkscc
      541 syishqn
//
LOCUS       NP_001276868             496 aa            linear   PRI 21-NOV-2025
DEFINITION  excitatory amino acid transporter 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001276868
VERSION     NP_001276868.1
DBSOURCE    REFSEQ: accession NM_001289939.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Albury,C.L., Sutherland,H.G., Lam,A.W.Y., Tran,N.K., Lea,R.A.,
            Haupt,L.M. and Griffiths,L.R.
  TITLE     Identification of Polymorphisms in EAAT1 Glutamate Transporter Gene
            SLC1A3 Associated with Reduced Migraine Risk
  JOURNAL   Genes (Basel) 15 (6), 797 (2024)
   PUBMED   38927733
  REMARK    GeneRIF: Identification of Polymorphisms in EAAT1 Glutamate
            Transporter Gene SLC1A3 Associated with Reduced Migraine Risk.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Welby,E. and Ebert,A.D.
  TITLE     Diminished motor neuron activity driven by abnormal astrocytic
            EAAT1 glutamate transporter activity in spinal muscular atrophy is
            not fully restored after lentiviral SMN delivery
  JOURNAL   Glia 71 (5), 1311-1332 (2023)
   PUBMED   36655314
  REMARK    GeneRIF: Diminished motor neuron activity driven by abnormal
            astrocytic EAAT1 glutamate transporter activity in spinal muscular
            atrophy is not fully restored after lentiviral SMN delivery.
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Pant,S., Wu,Q., Ryan,R. and Tajkhorshid,E.
  TITLE     Microscopic Characterization of the Chloride Permeation Pathway in
            the Human Excitatory Amino Acid Transporter 1 (EAAT1)
  JOURNAL   ACS Chem Neurosci 13 (6), 776-785 (2022)
   PUBMED   35192345
  REMARK    GeneRIF: Microscopic Characterization of the Chloride Permeation
            Pathway in the Human Excitatory Amino Acid Transporter 1 (EAAT1).
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Lee,A., Anderson,A.R., Beasley,S.J., Barnett,N.L., Poronnik,P. and
            Pow,D.V.
  TITLE     A new splice variant of the glutamate-aspartate transporter:
            cloning and immunolocalization of GLAST1c in rat, pig and human
            brains
  JOURNAL   J Chem Neuroanat 43 (1), 52-63 (2012)
   PUBMED   22026960
REFERENCE   6  (residues 1 to 496)
  AUTHORS   Vallejo-Illarramendi,A., Domercq,M. and Matute,C.
  TITLE     A novel alternative splicing form of excitatory amino acid
            transporter 1 is a negative regulator of glutamate uptake
  JOURNAL   J Neurochem 95 (2), 341-348 (2005)
   PUBMED   16042756
  REMARK    GeneRIF: EAAT1ex9skip splice variant is a negative regulator of
            full-length EAAT1 function in the human brain
REFERENCE   7  (residues 1 to 496)
  AUTHORS   Takai,S., Yamada,K., Kawakami,H., Tanaka,K. and Nakamura,S.
  TITLE     Localization of the gene (SLC1A3) encoding human glutamate
            transporter (GluT-1) to 5p13 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 209-210 (1995)
   PUBMED   7698014
REFERENCE   8  (residues 1 to 496)
  AUTHORS   Shashidharan,P., Huntley,G.W., Meyer,T., Morrison,J.H. and
            Plaitakis,A.
  TITLE     Neuron-specific human glutamate transporter: molecular cloning,
            characterization and expression in human brain
  JOURNAL   Brain Res 662 (1-2), 245-250 (1994)
   PUBMED   7859077
REFERENCE   9  (residues 1 to 496)
  AUTHORS   Arriza,J.L., Fairman,W.A., Wadiche,J.I., Murdoch,G.H.,
            Kavanaugh,M.P. and Amara,S.G.
  TITLE     Functional comparisons of three glutamate transporter subtypes
            cloned from human motor cortex
  JOURNAL   J Neurosci 14 (9), 5559-5569 (1994)
   PUBMED   7521911
REFERENCE   10 (residues 1 to 496)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC320625.1, BC022285.1,
            BC037310.2, AK293886.1, AK057823.1 and AF070609.1.
            
            Summary: This gene encodes a member of a member of a high affinity
            glutamate transporter family. This gene functions in the
            termination of excitatory neurotransmission in central nervous
            system. Mutations are associated with episodic ataxia, Type 6.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (GLAST1a) lacks an alternate
            in-frame exon in the 5' coding region, compared to variant GLAST.
            The encoded protein (isoform 4) is shorter, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2146982,
                              SAMEA2147975 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..496
                     /product="excitatory amino acid transporter 1 isoform 4"
                     /note="excitatory amino acid transporter 1; GLAST-1;
                     sodium-dependent glutamate/aspartate transporter 1; solute
                     carrier family 1 (glial high affinity glutamate
                     transporter), member 3"
                     /calculated_mol_wt=54077
     Region          53..450
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     CDS             1..496
                     /gene="SLC1A3"
                     /gene_synonym="EA6; EAAT1; GLAST; GLAST1"
                     /coded_by="NM_001289939.2:226..1716"
                     /note="isoform 4 is encoded by transcript variant GLAST1a"
                     /db_xref="CCDS:CCDS78004.1"
                     /db_xref="GeneID:6507"
                     /db_xref="HGNC:HGNC:10941"
                     /db_xref="MIM:600111"
ORIGIN      
        1 mtksngeepk mggrmerfqq gvrkrtllak kkvqnitked vksylfrnaf vlltvtaviv
       61 gmaaldskas gkmgmravvy ymtttiiavv igiiiviiih pgkgtkenmh regkivrvta
      121 adafldlirn mfppnlveac fkqfktnyek rsfkvpiqan etlvgavinn vseametltr
      181 iteelvpvpg svngvnalgl vvfsmcfgfv ignmkeqgqa lreffdslne aimrlvavim
      241 wyapvgilfl iagkivemed mgviggqlam ytvtvivgll ihavivlpll yflvtrknpw
      301 vfiggllqal italgtssss atlpitfkcl eenngvdkrv trfvlpvgat inmdgtalye
      361 alaaifiaqv nnfelnfgqi itisitataa sigaagipqa glvtmvivlt svglptddit
      421 liiavdwfld rlrtttnvlg dslgagiveh lsrhelknrd vemgnsviee nemkkpyqli
      481 aqdnetekpi dsetkm
//
LOCUS       NP_063916                216 aa            linear   PRI 21-NOV-2025
DEFINITION  coagulation factor VIII isoform b [Homo sapiens].
ACCESSION   NP_063916
VERSION     NP_063916.1
DBSOURCE    REFSEQ: accession NM_019863.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   de Vries,P.S., Reventun,P., Brown,M.R., Heath,A.S., Huffman,J.E.,
            Le,N.Q., Bebo,A., Brody,J.A., Temprano-Sagrera,G., Raffield,L.M.,
            Ozel,A.B., Thibord,F., Jain,D., Lewis,J.P., Rodriguez,B.A.T.,
            Pankratz,N., Taylor,K.D., Polasek,O., Chen,M.H., Yanek,L.R.,
            Carrasquilla,G.D., Marioni,R.E., Kleber,M.E., Tregouet,D.A.,
            Yao,J., Li-Gao,R., Joshi,P.K., Trompet,S., Martinez-Perez,A.,
            Ghanbari,M., Howard,T.E., Reiner,A.P., Arvanitis,M., Ryan,K.A.,
            Bartz,T.M., Rudan,I., Faraday,N., Linneberg,A., Ekunwe,L.,
            Davies,G., Delgado,G.E., Suchon,P., Guo,X., Rosendaal,F.R.,
            Klaric,L., Noordam,R., van Rooij,F., Curran,J.E., Wheeler,M.M.,
            Osburn,W.O., O'Connell,J.R., Boerwinkle,E., Beswick,A., Psaty,B.M.,
            Kolcic,I., Souto,J.C., Becker,L.C., Hansen,T., Doyle,M.F.,
            Harris,S.E., Moissl,A.P., Deleuze,J.F., Rich,S.S., van Hylckama
            Vlieg,A., Campbell,H., Stott,D.J., Soria,J.M., de Maat,M.P.M.,
            Almasy,L., Brody,L.C., Auer,P.L., Mitchell,B.D., Ben-Shlomo,Y.,
            Fornage,M., Hayward,C., Mathias,R.A., Kilpelainen,T.O., Lange,L.A.,
            Cox,S.R., Marz,W., Morange,P.E., Rotter,J.I., Mook-Kanamori,D.O.,
            Wilson,J.F., van der Harst,P., Jukema,J.W., Ikram,M.A.,
            Blangero,J., Kooperberg,C., Desch,K.C., Johnson,A.D.,
            Sabater-Lleal,M., Lowenstein,C.J., Smith,N.L. and Morrison,A.C.
  TITLE     A genetic association study of circulating coagulation factor VIII
            and von Willebrand factor levels
  JOURNAL   Blood 143 (18), 1845-1855 (2024)
   PUBMED   38320121
  REMARK    GeneRIF: A genetic association study of circulating coagulation
            factor VIII and von Willebrand factor levels.
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Hopp,M.T., Ugurlar,D., Pezeshkpoor,B., Biswas,A., Ramoji,A.,
            Neugebauer,U., Oldenburg,J. and Imhof,D.
  TITLE     In-depth structure-function profiling of the complex formation
            between clotting factor VIII and heme
  JOURNAL   Thromb Res 237, 184-195 (2024)
   PUBMED   38631156
  REMARK    GeneRIF: In-depth structure-function profiling of the complex
            formation between clotting factor VIII and heme.
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Symington,E., Rangarajan,S., Lester,W., Madan,B., Pierce,G.F.,
            Raheja,P., Robinson,T.M., Osmond,D., Russell,C.B., Vettermann,C.,
            Agarwal,S.K., Li,M., Wong,W.Y. and Laffan,M.
  TITLE     Long-term safety and efficacy outcomes of valoctocogene
            roxaparvovec gene transfer up to 6 years post-treatment
  JOURNAL   Haemophilia 30 (2), 320-330 (2024)
   PUBMED   38317480
  REMARK    GeneRIF: Long-term safety and efficacy outcomes of valoctocogene
            roxaparvovec gene transfer up to 6 years post-treatment.
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Tse,V., Chacaltana,G., Gutierrez,M., Forino,N.M., Jimenez,A.G.,
            Tao,H., Do,P.H., Oh,C., Chary,P., Quesada,I., Hamrick,A., Lee,S.,
            Stone,M.D. and Sanford,J.R.
  TITLE     An intronic RNA element modulates Factor VIII exon-16 splicing
  JOURNAL   Nucleic Acids Res 52 (1), 300-315 (2024)
   PUBMED   37962303
  REMARK    GeneRIF: An intronic RNA element modulates Factor VIII exon-16
            splicing.
REFERENCE   5  (residues 1 to 216)
  AUTHORS   Nakajima,Y. and Nogami,K.
  TITLE     The role of proteolytic cleavage at Arg336 and Arg372 of the A1
            domain in factor VIIa/tissue factor-catalyzed reactions of B
            domain-deleted factor VIII
  JOURNAL   Biochim Biophys Acta Gen Subj 1868 (1), 130501 (2024)
   PUBMED   37925034
  REMARK    GeneRIF: The role of proteolytic cleavage at Arg[336] and Arg[372]
            of the A1 domain in factor VIIa/tissue factor-catalyzed reactions
            of B domain-deleted factor VIII.
REFERENCE   6  (residues 1 to 216)
  AUTHORS   Konkle,B.A. and Nakaya Fletcher,S.
  TITLE     Hemophilia A
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301578
REFERENCE   7  (residues 1 to 216)
  AUTHORS   Jonsdottir,S., Diamond,C., Levinson,B., Magnusson,S., Jensson,O.
            and Gitschier,J.
  TITLE     Missense mutations causing mild hemophilia A in Iceland detected by
            denaturing gradient gel electrophoresis
  JOURNAL   Hum Mutat 1 (6), 506-508 (1992)
   PUBMED   1301960
REFERENCE   8  (residues 1 to 216)
  AUTHORS   Diamond,C., Kogan,S., Levinson,B. and Gitschier,J.
  TITLE     Amino acid substitutions in conserved domains of factor VIII and
            related proteins: study of patients with mild and moderately severe
            hemophilia A
  JOURNAL   Hum Mutat 1 (3), 248-257 (1992)
   PUBMED   1301932
REFERENCE   9  (residues 1 to 216)
  AUTHORS   Nafa,K., Baudis,M., Deburgrave,N., Bardin,J.M., Sultan,Y.,
            Kaplan,J.C. and Delpech,M.
  TITLE     A novel mutation (Arg-->Leu in exon 18) in factor VIII gene
            responsible for moderate hemophilia A
  JOURNAL   Hum Mutat 1 (1), 77-78 (1992)
   PUBMED   1301194
REFERENCE   10 (residues 1 to 216)
  AUTHORS   Zucker,M.B., Broekman,M.J. and Kaplan,K.L.
  TITLE     Factor VIII-related antigen in human blood platelets: localization
            and release by thrombin and collagen
  JOURNAL   J Lab Clin Med 94 (5), 675-682 (1979)
   PUBMED   501196
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX842559.3 and AC109993.4.
            
            Summary: This gene encodes coagulation factor VIII, which
            participates in the intrinsic pathway of blood coagulation; factor
            VIII is a cofactor for factor IXa which, in the presence of Ca+2
            and phospholipids, converts factor X to the activated form Xa.
            This gene produces two alternatively spliced transcripts.
            Transcript variant 1 encodes a large glycoprotein, isoform a, which
            circulates in plasma and associates with von Willebrand factor in a
            noncovalent complex. This protein undergoes multiple cleavage
            events. Transcript variant 2 encodes a putative small protein,
            isoform b, which consists primarily of the phospholipid binding
            domain of factor VIIIc. This binding domain is essential for
            coagulant activity. Defects in this gene results in hemophilia A, a
            common recessive X-linked coagulation disorder. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) contains an unique 5' exon
            located within intron 22 of transcript variant 1. This exon codes
            for eight amino acids and is spliced to exons 23-26 maintaining the
            reading frame. The resulting isoform (b) is considerably shorter
            compared to isoform a, and includes the phospholipid binding
            domain.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064380.1, M90707.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..216
                     /product="coagulation factor VIII isoform b"
                     /note="factor VIII F8B; coagulation factor VIIIc;
                     antihemophilic factor; coagulation factor VIII,
                     procoagulant component; coagulation factor VIII C2 domain;
                     coagulation factor VIII A1 domain"
                     /calculated_mol_wt=24510
     Region          1..8
                     /region_name="region encoded by the alternative exon"
     Region          <4..52
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cl25480"
                     /db_xref="CDD:330301"
     Region          57..216
                     /region_name="phospholipid binding domain"
     Region          60..209
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Site            order(104,132,139)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     CDS             1..216
                     /gene="F8"
                     /gene_synonym="AHF; DXS1253E; F8B; F8C; FVIII; HEMA;
                     THPH13"
                     /coded_by="NM_019863.3:161..811"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44026.1"
                     /db_xref="GeneID:2157"
                     /db_xref="HGNC:HGNC:3546"
                     /db_xref="MIM:300841"
ORIGIN      
        1 mriqdpgkvf fgnvdssgik hnifnppiia ryirlhpthy sirstlrmel mgcdlnscsm
       61 plgmeskais daqitassyf tnmfatwsps karlhlqgrs nawrpqvnnp kewlqvdfqk
      121 tmkvtgvttq gvkslltsmy vkeflisssq dghqwtlffq ngkvkvfqgn qdsftpvvns
      181 ldpplltryl rihpqswvhq ialrmevlgc eaqdly
//
LOCUS       NP_001167447             483 aa            linear   PRI 21-NOV-2025
DEFINITION  tectonic-1 isoform 5 precursor [Homo sapiens].
ACCESSION   NP_001167447 XP_005253990
VERSION     NP_001167447.1
DBSOURCE    REFSEQ: accession NM_001173976.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Xu,X., Gao,F., Wang,J., Long,C., Tao,L., Ding,L. and Ji,Y.
  TITLE     microRNA-216a-5p inhibits the development of gastric cancer through
            target combination with TCTN1
  JOURNAL   Minerva Med 114 (3), 323-331 (2023)
   PUBMED   32486612
  REMARK    GeneRIF: microRNA-216a-5p inhibits the development of gastric
            cancer through target combination with TCTN1.
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Bai,G., Wei,N., Li,F., Zhao,P., Meng,Z., Zou,B., Liu,Y., Xu,K.,
            Li,K., Yao,C. and Yang,P.
  TITLE     Function and transcriptional regulation of TCTN1 in oral squamous
            cell carcinoma
  JOURNAL   Oncol Rep 47 (2) (2022)
   PUBMED   34859261
  REMARK    GeneRIF: Function and transcriptional regulation of TCTN1 in oral
            squamous cell carcinoma.
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Wang,H., Jiang,W., Dai,M., Xiao,B., Xu,Y., Sun,Y., Liu,Y., Ying,X.,
            Sun,Y., Wei,W. and Ji,X.
  TITLE     [Diagnosis of two cases from one family with Joubert syndrome
            caused by novel mutations of TCTN1 gene by whole exome sequencing]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 36 (7), 686-689 (2019)
   PUBMED   31302911
  REMARK    GeneRIF: Two novel TCTN1 mutations were identified in a family with
            Joubert syndrome
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Alazami,A.M., Alshammari,M.J., Salih,M.A., Alzahrani,F., Hijazi,H.,
            Seidahmed,M.Z., Abu Safieh,L., Aldosary,M., Khan,A.O. and
            Alkuraya,F.S.
  TITLE     Molecular characterization of Joubert syndrome in Saudi Arabia
  JOURNAL   Hum Mutat 33 (10), 1423-1428 (2012)
   PUBMED   22693042
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Garcia-Gonzalo,F.R., Corbit,K.C., Sirerol-Piquer,M.S.,
            Ramaswami,G., Otto,E.A., Noriega,T.R., Seol,A.D., Robinson,J.F.,
            Bennett,C.L., Josifova,D.J., Garcia-Verdugo,J.M., Katsanis,N.,
            Hildebrandt,F. and Reiter,J.F.
  TITLE     A transition zone complex regulates mammalian ciliogenesis and
            ciliary membrane composition
  JOURNAL   Nat Genet 43 (8), 776-784 (2011)
   PUBMED   21725307
  REMARK    GeneRIF: Mutations in Tctn1 is associated with ciliopathies.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 483)
  AUTHORS   Reiter,J.F. and Skarnes,W.C.
  TITLE     Tectonic, a novel regulator of the Hedgehog pathway required for
            both activation and inhibition
  JOURNAL   Genes Dev 20 (1), 22-27 (2006)
   PUBMED   16357211
REFERENCE   9  (residues 1 to 483)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK024780.1, AC144522.12,
            AK055891.1 and CA419765.1.
            
            On Aug 31, 2013 this sequence version replaced XP_005253990.1.
            
            Summary: This gene encodes a member of a family of secreted and
            transmembrane proteins. The orthologous gene in mouse functions
            downstream of smoothened and rab23 to modulate hedgehog signal
            transduction. This protein is a component of the tectonic-like
            complex, which forms a barrier between the ciliary axoneme and the
            basal body. A mutation in this gene was found in a family with
            Joubert syndrome-13. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (5) includes an alternate exon in
            the 5' region, initiates translation at an alternate start codon,
            and lacks an in-frame exon and uses an alternate in-frame splice
            site in the 3' coding region, compared to variant 1. The resulting
            isoform (5) has a distinct N-terminus and is shorter than isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK024780.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2159368
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..483
                     /product="tectonic-1 isoform 5 precursor"
                     /calculated_mol_wt=50014
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2763
     Region          18..327
                     /region_name="TCTN_DUF1619"
                     /note="Tectonic domain DUF1619; pfam07773"
                     /db_xref="CDD:462260"
     CDS             1..483
                     /gene="TCTN1"
                     /gene_synonym="JBTS13; TECT1"
                     /coded_by="NM_001173976.2:311..1762"
                     /note="isoform 5 precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:79600"
                     /db_xref="HGNC:HGNC:26113"
                     /db_xref="MIM:609863"
ORIGIN      
        1 mitahcsldl lgsvavlcvc dlspaqcdin cccdpdcssv dfsvfsacsv pvvtgdsqfc
       61 sqkaviysln ftanppqrvf elvdqinpsi fcihitnykp alsfinpevp dennfdtlmk
      121 tsdgftlnae syvsfttkld iptaakyeyg vplqtsdsfl rfpssltssl ctdnnpaafl
      181 vnqavkctrk inleqceeie alsmafyssp eilrvpdsrk kvpitvqsiv iqslnktltr
      241 redtdvlqpt lvnaghfslc vnvvlevkys ltytdagevt kadlsfvlgt vssvvvplqq
      301 kfeihflqen tqpvplsgnp gyvvglplaa gfqphkggal pcqlvaqkvk sllwgqgfpd
      361 yvapfgnsqa qdmldwvpih fitqsfnrkh fvlqdscqlp galvievkwt kygsllnpqa
      421 kivnvtanli sssfpeansg nertilista vtfvdvsapa eagfrappai narlpfnfff
      481 pfv
//
LOCUS       NP_001385213             301 aa            linear   PRI 21-NOV-2025
DEFINITION  TIMELESS-interacting protein isoform 1 [Homo sapiens].
ACCESSION   NP_001385213
VERSION     NP_001385213.1
DBSOURCE    REFSEQ: accession NM_001398284.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Arai,H., Xiao,Y., Millstein,J., Wang,J., Battaglin,F.,
            Kawanishi,N., Jayachandran,P., Soni,S., Zhang,W., Mancao,C.,
            Salhia,B., Mumenthaler,S.M., Parikh,A.R. and Lenz,H.J.
  TITLE     Germline polymorphisms in genes maintaining the replication fork
            predict the efficacy of oxaliplatin and irinotecan in patients with
            metastatic colorectal cancer
  JOURNAL   Br J Cancer 126 (1), 72-78 (2022)
   PUBMED   34689170
  REMARK    GeneRIF: Germline polymorphisms in genes maintaining the
            replication fork predict the efficacy of oxaliplatin and irinotecan
            in patients with metastatic colorectal cancer.
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Grabarczyk,D.B.
  TITLE     The Fork Protection Complex: A Regulatory Hub at the Head of the
            Replisome
  JOURNAL   Subcell Biochem 99, 83-107 (2022)
   PUBMED   36151374
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Lerner,L.K., Holzer,S., Kilkenny,M.L., Svikovic,S., Murat,P.,
            Schiavone,D., Eldridge,C.B., Bittleston,A., Maman,J.D., Branzei,D.,
            Stott,K., Pellegrini,L. and Sale,J.E.
  TITLE     Timeless couples G-quadruplex detection with processing by DDX11
            helicase during DNA replication
  JOURNAL   EMBO J 39 (18), e104185 (2020)
   PUBMED   32705708
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Gotter,A.L., Suppa,C. and Emanuel,B.S.
  TITLE     Mammalian TIMELESS and Tipin are evolutionarily conserved
            replication fork-associated factors
  JOURNAL   J Mol Biol 366 (1), 36-52 (2007)
   PUBMED   17141802
  REMARK    GeneRIF: TIM and Tipin are functional orthologs of their
            replisome-associated yeast counterparts capable of coordinating
            replication with genotoxic stress responses, and distinguishes
            mammalian TIM from the circadian-specific paralogs.
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Yoshizawa-Sugata,N. and Masai,H.
  TITLE     Human Tim/Timeless-interacting protein, Tipin, is required for
            efficient progression of S phase and DNA replication checkpoint
  JOURNAL   J Biol Chem 282 (4), 2729-2740 (2007)
   PUBMED   17102137
  REMARK    GeneRIF: Tipin is a checkpoint mediator that cooperates with Tim
            and may regulate the nuclear relocation of Claspin in response to
            replication checkpoint
REFERENCE   8  (residues 1 to 301)
  AUTHORS   Chou,D.M. and Elledge,S.J.
  TITLE     Tipin and Timeless form a mutually protective complex required for
            genotoxic stress resistance and checkpoint function
  JOURNAL   Proc Natl Acad Sci U S A 103 (48), 18143-18147 (2006)
   PUBMED   17116885
  REMARK    GeneRIF: observation explains the similar checkpoint phenotypes
            observed in both Tipin- and Timeless-depleted cells
REFERENCE   9  (residues 1 to 301)
  AUTHORS   Gotter,A.L.
  TITLE     Tipin, a novel timeless-interacting protein, is developmentally
            co-expressed with timeless and disrupts its self-association
  JOURNAL   J Mol Biol 331 (1), 167-176 (2003)
   PUBMED   12875843
REFERENCE   10 (residues 1 to 301)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            
            Summary: The protein encoded by this gene is part of the replisome
            complex, a group of proteins that support DNA replication. It binds
            TIM, which is involved in circadian rhythm regulation, and aids in
            protecting cells against DNA damage and stress. Two pseudogenes and
            two transcript variants encoding different isoforms have been found
            for this gene. [provided by RefSeq, Jul 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.789455.1,
                                           SRR14372080.2186245.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..301
                     /product="TIMELESS-interacting protein isoform 1"
                     /note="timeless-interacting protein; CSM3 homolog"
                     /calculated_mol_wt=34424
     Region          1..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Region          66..148
                     /region_name="Swi3"
                     /note="Replication Fork Protection Component Swi3;
                     pfam07962"
                     /db_xref="CDD:462324"
     Region          67..143
                     /region_name="Interaction with TIMELESS.
                     /evidence=ECO:0000269|PubMed:23359676"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Region          240..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BVW5.2)"
     CDS             1..301
                     /gene="TIPIN"
                     /coded_by="NM_001398284.1:676..1581"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS10215.1"
                     /db_xref="GeneID:54962"
                     /db_xref="HGNC:HGNC:30750"
                     /db_xref="MIM:610716"
ORIGIN      
        1 mlepqengvi dlpdyehved etfppfpppa sperqdgegt epdeesgnga pvrvppkrtv
       61 krnipkldaq rliserglpa lrhvfdkakf kgkgheaedl kmlirhmehw ahrlfpklqf
      121 edfidrveyl gskkevqtcl krirldlpil hedfvsnnde vaennehdvt steldpfltn
      181 lsesemfase lsrslteeqq qriernkqla lerrqaklls nsqtlgndml mntprahtve
      241 evntdedqke esnglnedil dnpcndaian tlneeetlld qsfknvqqql datsrnitea
      301 r
//
LOCUS       NP_001014795             452 aa            linear   PRI 21-NOV-2025
DEFINITION  scaffold protein ILK isoform 1 [Homo sapiens].
ACCESSION   NP_001014795
VERSION     NP_001014795.1
DBSOURCE    REFSEQ: accession NM_001014795.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Bildyug,N.
  TITLE     Inhibition of Integrin-Associated Kinases FAK and ILK on the In
            Vitro Model of Skin Wound Healing
  JOURNAL   Appl Biochem Biotechnol 196 (8), 5604-5615 (2024)
   PUBMED   38165590
  REMARK    GeneRIF: Inhibition of Integrin-Associated Kinases FAK and ILK on
            the In Vitro Model of Skin Wound Healing.
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Campillo,S., Gutierrez-Calabres,E., Garcia-Miranda,S., Griera,M.,
            Fernandez Rodriguez,L., de Frutos,S., Rodriguez-Puyol,D. and
            Calleros,L.
  TITLE     Integrin-linked kinase mRNA expression in circulating mononuclear
            cells as a biomarker of kidney and vascular damage in experimental
            chronic kidney disease
  JOURNAL   Cell Commun Signal 22 (1), 264 (2024)
   PUBMED   38734696
  REMARK    GeneRIF: Integrin-linked kinase mRNA expression in circulating
            mononuclear cells as a biomarker of kidney and vascular damage in
            experimental chronic kidney disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Ahmed,A.U., Almasabi,S., Firestein,R. and Williams,B.R.G.
  TITLE     Integrin-linked kinase expression in myeloid cells promotes colon
            tumorigenesis
  JOURNAL   Front Immunol 14, 1270194 (2023)
   PUBMED   38077324
  REMARK    GeneRIF: Integrin-linked kinase expression in myeloid cells
            promotes colon tumorigenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 452)
  AUTHORS   Hannigan,G.E., McDonald,P.C., Walsh,M.P. and Dedhar,S.
  TITLE     Integrin-linked kinase: not so 'pseudo' after all
  JOURNAL   Oncogene 30 (43), 4375-4385 (2011)
   PUBMED   21602880
  REMARK    Review article
REFERENCE   6  (residues 1 to 452)
  AUTHORS   Melchior,C., Kreis,S., Janji,B. and Kieffer,N.
  TITLE     Promoter characterization and genomic organization of the gene
            encoding integrin-linked kinase 1
  JOURNAL   Biochim Biophys Acta 1575 (1-3), 117-122 (2002)
   PUBMED   12020826
REFERENCE   7  (residues 1 to 452)
  AUTHORS   Delcommenne,M., Tan,C., Gray,V., Rue,L., Woodgett,J. and Dedhar,S.
  TITLE     Phosphoinositide-3-OH kinase-dependent regulation of glycogen
            synthase kinase 3 and protein kinase B/AKT by the integrin-linked
            kinase
  JOURNAL   Proc Natl Acad Sci U S A 95 (19), 11211-11216 (1998)
   PUBMED   9736715
REFERENCE   8  (residues 1 to 452)
  AUTHORS   Li,F., Liu,J., Mayne,R. and Wu,C.
  TITLE     Identification and characterization of a mouse protein kinase that
            is highly homologous to human integrin-linked kinase
  JOURNAL   Biochim Biophys Acta 1358 (3), 215-220 (1997)
   PUBMED   9366252
REFERENCE   9  (residues 1 to 452)
  AUTHORS   Hannigan,G.E., Bayani,J., Weksberg,R., Beatty,B., Pandita,A.,
            Dedhar,S. and Squire,J.
  TITLE     Mapping of the gene encoding the integrin-linked kinase, ILK, to
            human chromosome 11p15.5-p15.4
  JOURNAL   Genomics 42 (1), 177-179 (1997)
   PUBMED   9177792
REFERENCE   10 (residues 1 to 452)
  AUTHORS   Hannigan,G.E., Leung-Hagesteijn,C., Fitz-Gibbon,L., Coppolino,M.G.,
            Radeva,G., Filmus,J., Bell,J.C. and Dedhar,S.
  TITLE     Regulation of cell adhesion and anchorage-dependent growth by a new
            beta 1-integrin-linked protein kinase
  JOURNAL   Nature 379 (6560), 91-96 (1996)
   PUBMED   8538749
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091564.12, DC379936.1,
            CR749220.1, U40282.1 and HY257434.1.
            
            Summary: This gene encodes a protein with a kinase-like domain and
            four ankyrin-like repeats. The encoded protein associates at the
            cell membrane with the cytoplasmic domain of beta integrins, where
            it regulates integrin-mediated signal transduction. Activity of
            this protein is important in the epithelial to mesenchymal
            transition, and over-expression of this gene is implicated in tumor
            growth and metastasis. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. Variants 1, 2, and 3 encode the same isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU794625.1, SRR1163658.315320.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..452
                     /product="scaffold protein ILK isoform 1"
                     /EC_number="2.7.11.1"
                     /note="integrin-linked kinase-2; 59 kDa
                     serine/threonine-protein kinase; integrin-linked protein
                     kinase; epididymis secretory protein Li 28;
                     beta-integrin-linked kinase; inactive integrin-linked
                     kinase; scaffold protein ILK"
                     /calculated_mol_wt=51288
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q13418.2)"
     Region          2..30
                     /region_name="ANK 1.
                     /evidence=ECO:0000269|PubMed:19074270"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13418.2)"
     Region          <8..162
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          31..63
                     /region_name="ANK 2.
                     /evidence=ECO:0000269|PubMed:19074270"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13418.2)"
     Region          33..139
                     /region_name="Interaction with LIMS1.
                     /evidence=ECO:0000269|PubMed:12167643"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13418.2)"
     Site            order(33,35,39..40,43..45,47..48,52,55,64,66,68,72..73,
                     76..78,80..81,85,88,97,99,101,105..106,109..111,113..114,
                     118,121,130)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          33..64
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          66..97
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          99..130
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          130..174
                     /region_name="ANK 5.
                     /evidence=ECO:0000269|PubMed:19074270"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13418.2)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PAK1.
                     /evidence=ECO:0000269|PubMed:17420447; propagated from
                     UniProtKB/Swiss-Prot (Q13418.2)"
     Region          180..212
                     /region_name="PH-like, mediates interaction with TGFB1I1.
                     /evidence=ECO:0000250|UniProtKB:O55222"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13418.2)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13418.2)"
     Region          197..449
                     /region_name="PK_ILK"
                     /note="Pseudokinase domain of Integrin Linked Kinase;
                     cd14057"
                     /db_xref="CDD:270959"
     Site            order(200,202..204,207,218,220,269..272,279,323,326,339,
                     341)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270959"
     Site            order(225,348..351,361..364,396..399,401..403,406)
                     /site_type="other"
                     /note="Parvin interface [polypeptide binding]"
                     /db_xref="CDD:270959"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PAK1.
                     /evidence=ECO:0000269|PubMed:17420447; propagated from
                     UniProtKB/Swiss-Prot (Q13418.2)"
     Region          363..371
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:17420447"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13418.2)"
     Site            426
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O55222; propagated from
                     UniProtKB/Swiss-Prot (Q13418.2)"
     CDS             1..452
                     /gene="ILK"
                     /gene_synonym="HEL-S-28; ILK-1; ILK-2; P59; p59ILK"
                     /coded_by="NM_001014795.3:499..1857"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS7768.1"
                     /db_xref="GeneID:3611"
                     /db_xref="HGNC:HGNC:6040"
                     /db_xref="MIM:602366"
ORIGIN      
        1 mddiftqcre gnavavrlwl dntendlnqg ddhgfsplhw acregrsavv emlimrgari
       61 nvmnrgddtp lhlaashghr divqkllqyk adinavnehg nvplhyacfw gqdqvaedlv
      121 angalvsicn kygempvdka kaplrellre raekmgqnln ripykdtfwk gttrtrprng
      181 tlnkhsgidf kqlnfltkln enhsgelwkg rwqgndivvk vlkvrdwstr ksrdfneecp
      241 rlrifshpnv lpvlgacqsp paphptlith wmpygslynv lhegtnfvvd qsqavkfald
      301 margmaflht lepliprhal nsrsvmided mtarismadv kfsfqcpgrm yapawvapea
      361 lqkkpedtnr rsadmwsfav llwelvtrev pfadlsnmei gmkvaleglr ptippgisph
      421 vcklmkicmn edpakrpkfd mivpilekmq dk
//
LOCUS       NP_001310260             427 aa            linear   PRI 21-NOV-2025
DEFINITION  mitogen-activated protein kinase 8 isoform alpha2 [Homo sapiens].
ACCESSION   NP_001310260
VERSION     NP_001310260.1
DBSOURCE    REFSEQ: accession NM_001323331.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Liu,X., Ye,Z., Rao,D., Chen,Q. and Zhang,Z.
  TITLE     DUSP4 maintains the survival and LSD1 protein stability in
            esophageal squamous cell carcinoma cells by inhibiting JNK
            signaling-dependent autophagy
  JOURNAL   In Vitro Cell Dev Biol Anim 60 (2), 115-122 (2024)
   PUBMED   38286920
  REMARK    GeneRIF: DUSP4 maintains the survival and LSD1 protein stability in
            esophageal squamous cell carcinoma cells by inhibiting JNK
            signaling-dependent autophagy.
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Louw-du Toit,R., Simons,M. and Africander,D.
  TITLE     Progestins and breast cancer hallmarks: The role of the ERK1/2 and
            JNK pathways in estrogen receptor positive breast cancer cells
  JOURNAL   J Steroid Biochem Mol Biol 237, 106440 (2024)
   PUBMED   38048919
  REMARK    GeneRIF: Progestins and breast cancer hallmarks: The role of the
            ERK1/2 and JNK pathways in estrogen receptor positive breast cancer
            cells.
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Chai,F., Peng,H., Qin,L., Liu,C., Zeng,Y., Wang,R., Xu,G., Wang,R.,
            Wei,G., Huang,H., Lan,Y., Chen,W. and Wang,C.
  TITLE     MicroRNA miR-181d-5p regulates the MAPK signaling pathway by
            targeting mitogen-activated protein kinase 8 (MAPK8) to improve
            lupus nephritis
  JOURNAL   Gene 893, 147961 (2024)
   PUBMED   37931853
  REMARK    GeneRIF: MicroRNA miR-181d-5p regulates the MAPK signaling pathway
            by targeting mitogen-activated protein kinase 8 (MAPK8) to improve
            lupus nephritis.
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Feng,Y., Cao,H., Wang,D., Chen,L., Gao,R. and Sun,P.
  TITLE     JNK promotes the progression of castration-resistant prostate
            cancer
  JOURNAL   Acta Biochim Pol 70 (4), 817-822 (2023)
   PUBMED   38099475
  REMARK    GeneRIF: JNK promotes the progression of castration-resistant
            prostate cancer.
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Kharbanda,S., Saleem,A., Shafman,T., Emoto,Y., Taneja,N., Rubin,E.,
            Weichselbaum,R., Woodgett,J., Avruch,J., Kyriakis,J. et al.
  TITLE     Ionizing radiation stimulates a Grb2-mediated association of the
            stress-activated protein kinase with phosphatidylinositol 3-kinase
  JOURNAL   J Biol Chem 270 (32), 18871-18874 (1995)
   PUBMED   7642542
REFERENCE   7  (residues 1 to 427)
  AUTHORS   van Dam,H., Wilhelm,D., Herr,I., Steffen,A., Herrlich,P. and
            Angel,P.
  TITLE     ATF-2 is preferentially activated by stress-activated protein
            kinases to mediate c-jun induction in response to genotoxic agents
  JOURNAL   EMBO J 14 (8), 1798-1811 (1995)
   PUBMED   7737130
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Livingstone,C., Patel,G. and Jones,N.
  TITLE     ATF-2 contains a phosphorylation-dependent transcriptional
            activation domain
  JOURNAL   EMBO J 14 (8), 1785-1797 (1995)
   PUBMED   7737129
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Derijard,B., Raingeaud,J., Barrett,T., Wu,I.H., Han,J.,
            Ulevitch,R.J. and Davis,R.J.
  TITLE     Independent human MAP-kinase signal transduction pathways defined
            by MEK and MKK isoforms
  JOURNAL   Science 267 (5198), 682-685 (1995)
   PUBMED   7839144
  REMARK    Erratum:[Science 1995 Jul 7;269(5220):17]
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Seth,A., Alvarez,E., Gupta,S. and Davis,R.J.
  TITLE     A phosphorylation site located in the NH2-terminal domain of c-Myc
            increases transactivation of gene expression
  JOURNAL   J Biol Chem 266 (35), 23521-23524 (1991)
   PUBMED   1748630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC074325.7 and AC016397.6.
            
            Summary: The protein encoded by this gene is a member of the MAP
            kinase family. MAP kinases act as an integration point for multiple
            biochemical signals, and are involved in a wide variety of cellular
            processes such as proliferation, differentiation, transcription
            regulation and development. This kinase is activated by various
            cell stimuli, and targets specific transcription factors, and thus
            mediates immediate-early gene expression in response to cell
            stimuli. The activation of this kinase by tumor-necrosis factor
            alpha (TNF-alpha) is found to be required for TNF-alpha induced
            apoptosis. This kinase is also involved in UV radiation induced
            apoptosis, which is thought to be related to cytochrom c-mediated
            cell death pathway. Studies of the mouse counterpart of this gene
            suggested that this kinase play a key role in T cell proliferation,
            apoptosis and differentiation. Several alternatively spliced
            transcript variants encoding distinct isoforms have been reported.
            [provided by RefSeq, Apr 2016].
            
            Transcript Variant: This variant (17), along with variants JNK1-a2,
            14, and 15, encodes isoform alpha2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.120767.1,
                                           SRR1803615.220510.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q11.22"
     Protein         1..427
                     /product="mitogen-activated protein kinase 8 isoform
                     alpha2"
                     /EC_number="2.7.11.24"
                     /note="JUN N-terminal kinase; c-Jun N-terminal kinase 1;
                     MAP kinase 8; stress-activated protein kinase 1;
                     stress-activated protein kinase 1c"
                     /calculated_mol_wt=48165
     Region          25..360
                     /region_name="STKc_JNK"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     c-Jun N-terminal Kinase; cd07850"
                     /db_xref="CDD:270840"
     Site            order(32..38,40,53,55,72,86,108..114,116..117,151,153,
                     155..156,158,168..169,172,183,185..188,190,227)
                     /site_type="active"
                     /db_xref="CDD:270840"
     Site            order(32..38,40,53,55,86,108..114,158,168)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270840"
     Site            order(72,116,151,153,172,183,185..188,190,227)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270840"
     Site            order(112,118,127,130,159..163,323..324,326,329)
                     /site_type="other"
                     /note="KIM docking site [polypeptide binding]"
                     /db_xref="CDD:270840"
     Site            order(168..178,182..190)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270840"
     Region          183..185
                     /region_name="TXY"
                     /note="propagated from UniProtKB/Swiss-Prot (P45983.2)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAP2K7.
                     /evidence=ECO:0000269|PubMed:11062067; propagated from
                     UniProtKB/Swiss-Prot (P45983.2)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by MAP2K4.
                     /evidence=ECO:0000269|PubMed:11062067; propagated from
                     UniProtKB/Swiss-Prot (P45983.2)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P45983.2)"
     Region          371..427
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P45983.2)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91Y86; Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P45983.2)"
     CDS             1..427
                     /gene="MAPK8"
                     /gene_synonym="JNK; JNK-46; JNK1; JNK1A2; JNK21B1/2;
                     PRKM8; SAPK1; SAPK1c"
                     /coded_by="NM_001323331.2:389..1672"
                     /note="isoform alpha2 is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS7224.1"
                     /db_xref="GeneID:5599"
                     /db_xref="HGNC:HGNC:6881"
                     /db_xref="MIM:601158"
ORIGIN      
        1 msrskrdnnf ysveigdstf tvlkryqnlk pigsgaqgiv caaydailer nvaikklsrp
       61 fqnqthakra yrelvlmkcv nhkniiglln vftpqkslee fqdvyivmel mdanlcqviq
      121 meldhermsy llyqmlcgik hlhsagiihr dlkpsnivvk sdctlkildf glartagtsf
      181 mmtpyvvtry yrapevilgm gykenvdlws vgcimgemvc hkilfpgrdy idqwnkvieq
      241 lgtpcpefmk klqptvrtyv enrpkyagys feklfpdvlf padsehnklk asqardllsk
      301 mlvidaskri svdealqhpy invwydpsea eapppkipdk qlderehtie ewkeliykev
      361 mdleertkng virgqpsplg aavingsqhp sssssvndvs smstdptlas dtdssleaaa
      421 gplgccr
//
LOCUS       NP_001269523             241 aa            linear   PRI 21-NOV-2025
DEFINITION  SLAM family member 7 isoform h precursor [Homo sapiens].
ACCESSION   NP_001269523 XP_005245444
VERSION     NP_001269523.1
DBSOURCE    REFSEQ: accession NM_001282594.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Chu,E., Wu,J., Kang,S.S. and Kang,Y.
  TITLE     SLAMF7 as a Promising Immunotherapeutic Target in Multiple Myeloma
            Treatments
  JOURNAL   Curr Oncol 30 (9), 7891-7903 (2023)
   PUBMED   37754488
  REMARK    GeneRIF: SLAMF7 as a Promising Immunotherapeutic Target in Multiple
            Myeloma Treatments.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Choe,U., Pham,Q., Kim,Y.S., Yu,L. and Wang,T.T.Y.
  TITLE     Identification and elucidation of cross talk between SLAM Family
            Member 7 (SLAMF7) and Toll-like receptor (TLR) pathways in
            monocytes and macrophages
  JOURNAL   Sci Rep 13 (1), 11007 (2023)
   PUBMED   37420084
  REMARK    GeneRIF: Identification and elucidation of cross talk between SLAM
            Family Member 7 (SLAMF7) and Toll-like receptor (TLR) pathways in
            monocytes and macrophages.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 241)
  AUTHORS   O'Connell,P., Blake,M.K., Godbehere,S., Amalfitano,A. and
            Aldhamen,Y.A.
  TITLE     SLAMF7 modulates B cells and adaptive immunity to regulate
            susceptibility to CNS autoimmunity
  JOURNAL   J Neuroinflammation 19 (1), 241 (2022)
   PUBMED   36199066
  REMARK    GeneRIF: SLAMF7 modulates B cells and adaptive immunity to regulate
            susceptibility to CNS autoimmunity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Simmons,D.P., Nguyen,H.N., Gomez-Rivas,E., Jeong,Y., Jonsson,A.H.,
            Chen,A.F., Lange,J.K., Dyer,G.S., Blazar,P., Earp,B.E.,
            Coblyn,J.S., Massarotti,E.M., Sparks,J.A., Todd,D.J., Rao,D.A.,
            Kim,E.Y. and Brenner,M.B.
  CONSRTM   Accelerating Medicines Partnership (AMP) RA/SLE Network
  TITLE     SLAMF7 engagement superactivates macrophages in acute and chronic
            inflammation
  JOURNAL   Sci Immunol 7 (68), eabf2846 (2022)
   PUBMED   35148199
  REMARK    GeneRIF: SLAMF7 engagement superactivates macrophages in acute and
            chronic inflammation.
REFERENCE   6  (residues 1 to 241)
  AUTHORS   Lee,J.K., Boles,K.S. and Mathew,P.A.
  TITLE     Molecular and functional characterization of a CS1 (CRACC) splice
            variant expressed in human NK cells that does not contain
            immunoreceptor tyrosine-based switch motifs
  JOURNAL   Eur J Immunol 34 (10), 2791-2799 (2004)
   PUBMED   15368295
  REMARK    GeneRIF: CS1-L and CS1-S may differentially regulate human NK cell
            functions
REFERENCE   7  (residues 1 to 241)
  AUTHORS   Tovar,V., del Valle,J., Zapater,N., Martin,M., Romero,X.,
            Pizcueta,P., Bosch,J., Terhorst,C. and Engel,P.
  TITLE     Mouse novel Ly9: a new member of the expanding CD150 (SLAM) family
            of leukocyte cell-surface receptors
  JOURNAL   Immunogenetics 54 (6), 394-402 (2002)
   PUBMED   12242590
REFERENCE   8  (residues 1 to 241)
  AUTHORS   Murphy,J.J., Hobby,P., Vilarino-Varela,J., Bishop,B.,
            Iordanidou,P., Sutton,B.J. and Norton,J.D.
  TITLE     A novel immunoglobulin superfamily receptor (19A) related to CD2 is
            expressed on activated lymphocytes and promotes homotypic B-cell
            adhesion
  JOURNAL   Biochem J 361 (Pt 3), 431-436 (2002)
   PUBMED   11802771
REFERENCE   9  (residues 1 to 241)
  AUTHORS   Bouchon,A., Cella,M., Grierson,H.L., Cohen,J.I. and Colonna,M.
  TITLE     Activation of NK cell-mediated cytotoxicity by a SAP-independent
            receptor of the CD2 family
  JOURNAL   J Immunol 167 (10), 5517-5521 (2001)
   PUBMED   11698418
REFERENCE   10 (residues 1 to 241)
  AUTHORS   Boles,K.S. and Mathew,P.A.
  TITLE     Molecular cloning of CS1, a novel human natural killer cell
            receptor belonging to the CD2 subset of the immunoglobulin
            superfamily
  JOURNAL   Immunogenetics 52 (3-4), 302-307 (2001)
   PUBMED   11220635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC388332.1, AK301432.1, AL121985.13 and BQ000581.1.
            
            On Sep 14, 2013 this sequence version replaced XP_005245444.1.
            
            Transcript Variant: This variant (8) lacks an alternate in-frame
            exon in the 5' coding region, and uses an alternate in-frame splice
            site in the central coding region, compared to variant 1. The
            encoded isoform (h) is shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301432.1, SRR1163657.447904.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..241
                     /product="SLAM family member 7 isoform h precursor"
                     /note="CD2-like receptor activating cytotoxic cells; 19A24
                     protein; novel LY9 (lymphocyte antigen 9) like protein;
                     protein 19A; CD2 subset 1; membrane protein FOAP-12"
                     /calculated_mol_wt=24122
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3176
     CDS             1..241
                     /gene="SLAMF7"
                     /gene_synonym="19A; CD319; CRACC; CS1"
                     /coded_by="NM_001282594.2:56..781"
                     /note="isoform h precursor is encoded by transcript
                     variant 8"
                     /db_xref="CCDS:CCDS72957.1"
                     /db_xref="GeneID:57823"
                     /db_xref="HGNC:HGNC:21394"
                     /db_xref="MIM:606625"
ORIGIN      
        1 magsptcltl iyilwqlteh lskpkvtmgl qsnkngtcvt nltccmehge edviytwkal
       61 gqaaneshng silpiswrwg esdmtficva rnpvsrnfss pilarklceg dclsplhrrl
      121 cpgaaddpds smvllclllv plllslfvlg lflwflkrer qeeyieekkr vdicretpni
      181 cphsgentey dtiphtnrti lkedpantvy stveipkkme nphslltmpd tprlfayenv
      241 i
//
LOCUS       NP_002939                204 aa            linear   PRI 21-NOV-2025
DEFINITION  large ribosomal subunit protein eL15 isoform 1 [Homo sapiens].
ACCESSION   NP_002939
VERSION     NP_002939.2
DBSOURCE    REFSEQ: accession NM_002948.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Wang,G., Qin,M., Zhang,B., Yan,Y., Yang,F., Chen,Q., Liu,Y.,
            Qiao,F. and Ni,Y.
  TITLE     Decreased expression of RPL15 and RPL18 exacerbated the
            calcification of valve interstitial cells during aortic valve
            calcification
  JOURNAL   Cell Biol Int 47 (10), 1749-1759 (2023)
   PUBMED   37431269
  REMARK    GeneRIF: Decreased expression of RPL15 and RPL18 exacerbated the
            calcification of valve interstitial cells during aortic valve
            calcification.
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Xu,C., He,X.Y., Ren,X.H., Han,D. and Cheng,S.X.
  TITLE     Detection of mRNAs of Ribosomal Protein L15 and E-Cadherin in
            Living Circulating Tumor Cells at Single Cell Resolution To Study
            Tumor Heterogeneity
  JOURNAL   Anal Chem 94 (30), 10610-10616 (2022)
   PUBMED   35856393
  REMARK    GeneRIF: Detection of mRNAs of Ribosomal Protein L15 and E-Cadherin
            in Living Circulating Tumor Cells at Single Cell Resolution To
            Study Tumor Heterogeneity.
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   6  (residues 1 to 204)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   7  (residues 1 to 204)
  AUTHORS   Wang,Q., Yang,C., Zhou,J., Wang,X., Wu,M. and Liu,Z.
  TITLE     Cloning and characterization of full-length human ribosomal protein
            L15 cDNA which was overexpressed in esophageal cancer
  JOURNAL   Gene 263 (1-2), 205-209 (2001)
   PUBMED   11223259
REFERENCE   8  (residues 1 to 204)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 204)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 204)
  AUTHORS   Sieff,C.
  TITLE     DBA Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AC124914.3.
            
            On Sep 5, 2001 this sequence version replaced NP_002939.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of four RNA species and approximately
            80 structurally distinct proteins. This gene encodes a member of
            the L15E family of ribosomal proteins and a component of the 60S
            subunit. This gene shares sequence similarity with the yeast
            ribosomal protein YL10 gene. Elevated expression of this gene has
            been observed in esophageal tumors and gastric cancer tissues, and
            deletion of this gene has been observed in a Diamond-Blackfan
            anemia (DBA) patient. As is typical for genes encoding ribosomal
            proteins, there are multiple processed pseudogenes of this gene
            dispersed through the genome. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1). Variants 1-5 encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014837.1, AF283772.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307839.10/ ENSP00000309334.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.2"
     Protein         1..204
                     /product="large ribosomal subunit protein eL15 isoform 1"
                     /note="60S ribosomal protein L15; large ribosomal subunit
                     protein eL15"
                     /calculated_mol_wt=24015
     Region          2..191
                     /region_name="Ribosomal_L15e"
                     /note="Ribosomal L15; pfam00827"
                     /db_xref="CDD:459950"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P61314; propagated from
                     UniProtKB/Swiss-Prot (P61313.2)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P61313.2)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P61313.2)"
     Region          165..186
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61313.2)"
     CDS             1..204
                     /gene="RPL15"
                     /gene_synonym="DBA12; EC45; eL15; L15; RPL10; RPLY10;
                     RPYL10"
                     /coded_by="NM_002948.5:53..667"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2640.1"
                     /db_xref="GeneID:6138"
                     /db_xref="HGNC:HGNC:10306"
                     /db_xref="MIM:604174"
ORIGIN      
        1 mgaykyiqel wrkkqsdvmr fllrvrcwqy rqlsalhrap rptrpdkarr lgykakqgyv
       61 iyrirvrrgg rkrpvpkgat ygkpvhhgvn qlkfarslqs vaeeragrhc galrvlnsyw
      121 vgedstykff evilidpfhk airrnpdtqw itkpvhkhre mrgltsagrk srglgkghkf
      181 hhtiggsrra awrrrntlql hryr
//
LOCUS       NP_001363203             545 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase PAK 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001363203 XP_016873336
VERSION     NP_001363203.1
DBSOURCE    REFSEQ: accession NM_001376274.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Kervarrec,T., Westphal,D., Pissaloux,D., Legrand,M., Tirode,F.,
            Neuhart,A., Drouot,F., Becker,J.C., Macagno,N., Seris,A.,
            Jouary,T., Beltzung,F., Jullie,M.L., Harms,P.W., Cribier,B.,
            Mourah,S., Jouenne,F., Fromont,G., Louveau,B., Mancini,M.,
            Kazakov,D.V., de la Fouchardiere,A. and Battistella,M.
  TITLE     Porocarcinomas with PAK1/2/3 fusions: a series of 12 cases
  JOURNAL   Histopathology 85 (4), 566-578 (2024)
   PUBMED   38785043
  REMARK    GeneRIF: Porocarcinomas with PAK1/2/3 fusions: a series of 12
            cases.
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Zhao,P., Zhang,J., Song,W., Qi,D., Huang,Y., Su,Y., Wu,R., Zhang,L.
            and Zhang,S.
  TITLE     Incarvine C and its analogues inhibit the formation of cell
            cytoskeleton by targeting Rac1
  JOURNAL   Bioorg Chem 149, 107512 (2024)
   PUBMED   38833990
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Xu,M.H., Zheng,Y.M., Liang,B.G., Xu,W.X., Cao,J., Wang,P.,
            Dong,Z.Y., Zhou,C.H., Sun,H.C., Ren,N., Ke,A.W. and Shen,Y.H.
  TITLE     Deubiquitination of CIB1 by USP14 promotes lenvatinib resistance
            via the PAK1-ERK1/2 axis in hepatocellular carcinoma
  JOURNAL   Int J Biol Sci 20 (9), 3269-3284 (2024)
   PUBMED   38993552
  REMARK    GeneRIF: Deubiquitination of CIB1 by USP14 promotes lenvatinib
            resistance via the PAK1-ERK1/2 axis in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Luo,Q., Raulston,E.G., Prado,M.A., Wu,X., Gritsman,K., Whalen,K.S.,
            Yan,K., Booth,C.A.G., Xu,R., van Galen,P., Doench,J.G., Shimony,S.,
            Long,H.W., Neuberg,D.S., Paulo,J.A. and Lane,A.A.
  TITLE     Targetable leukaemia dependency on noncanonical PI3Kgamma
            signalling
  JOURNAL   Nature 630 (8015), 198-205 (2024)
   PUBMED   38720074
  REMARK    GeneRIF: Targetable leukaemia dependency on noncanonical PI3Kgamma
            signalling.
REFERENCE   6  (residues 1 to 545)
  AUTHORS   Manser,E., Huang,H.Y., Loo,T.H., Chen,X.Q., Dong,J.M., Leung,T. and
            Lim,L.
  TITLE     Expression of constitutively active alpha-PAK reveals effects of
            the kinase on actin and focal complexes
  JOURNAL   Mol Cell Biol 17 (3), 1129-1143 (1997)
   PUBMED   9032240
REFERENCE   7  (residues 1 to 545)
  AUTHORS   Bokoch,G.M., Wang,Y., Bohl,B.P., Sells,M.A., Quilliam,L.A. and
            Knaus,U.G.
  TITLE     Interaction of the Nck adapter protein with p21-activated kinase
            (PAK1)
  JOURNAL   J Biol Chem 271 (42), 25746-25749 (1996)
   PUBMED   8824201
REFERENCE   8  (residues 1 to 545)
  AUTHORS   Brown,J.L., Stowers,L., Baer,M., Trejo,J., Coughlin,S. and Chant,J.
  TITLE     Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase
            pathway
  JOURNAL   Curr Biol 6 (5), 598-605 (1996)
   PUBMED   8805275
REFERENCE   9  (residues 1 to 545)
  AUTHORS   Martin,G.A., Bollag,G., McCormick,F. and Abo,A.
  TITLE     A novel serine kinase activated by rac1/CDC42Hs-dependent
            autophosphorylation is related to PAK65 and STE20
  JOURNAL   EMBO J 14 (9), 1970-1978 (1995)
   PUBMED   7744004
  REMARK    Erratum:[EMBO J. 1995 Sep 1;14(17):4385. doi:
            10.1002/j.1460-2075.1995.tb00113.x. PMID: 7556080]
REFERENCE   10 (residues 1 to 545)
  AUTHORS   Manser,E., Leung,T., Salihuddin,H., Zhao,Z.S. and Lim,L.
  TITLE     A brain serine/threonine protein kinase activated by Cdc42 and Rac1
  JOURNAL   Nature 367 (6458), 40-46 (1994)
   PUBMED   8107774
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000486.6.
            
            On Nov 13, 2019 this sequence version replaced XP_016873336.1.
            
            Summary: This gene encodes a family member of serine/threonine
            p21-activating kinases, known as PAK proteins. These proteins are
            critical effectors that link RhoGTPases to cytoskeleton
            reorganization and nuclear signaling, and they serve as targets for
            the small GTP binding proteins Cdc42 and Rac. This specific family
            member regulates cell motility and morphology. Mutations in this
            gene have been associated with macrocephaly, seizures, and speech
            delay. Overexpression of this gene is also reported in many cancer
            types, and particularly in breast cancer. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853564.5594.1,
                                           SRR11853565.5676.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.5-q14.1"
     Protein         1..545
                     /product="serine/threonine-protein kinase PAK 1 isoform 2"
                     /EC_number="2.7.11.1"
                     /note="p21/Cdc42/Rac1-activated kinase 1 (yeast
                     Ste20-related); p21/Cdc42/Rac1-activated kinase 1 (STE20
                     homolog, yeast); serine/threonine-protein kinase PAK 1;
                     p21 protein (Cdc42/Rac)-activated kinase 1"
                     /calculated_mol_wt=60516
     Region          1..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB and autocatalysis.
                     /evidence=ECO:0000269|PubMed:14585966,
                     ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          70..140
                     /region_name="Autoregulatory region.
                     /evidence=ECO:0000269|PubMed:22153498"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Region          74..132
                     /region_name="PBD"
                     /note="P21-Rho-binding domain; pfam00786"
                     /db_xref="CDD:395634"
     Site            order(75,78,81,83,86,103,107)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238526"
     Region          75..105
                     /region_name="GTPase-binding.
                     /evidence=ECO:0000269|PubMed:22153498"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by OXSR1.
                     /evidence=ECO:0000250|UniProtKB:P35465; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20417602,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000269|PubMed:17726028,
                     ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          159..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17989089,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20417602; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000269|PubMed:17726028; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          211..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13153.2)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17989089,
                     ECO:0000269|PubMed:23260667, ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88643; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O88643; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Region          249..544
                     /region_name="STKc_PAK1"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     p21-activated kinase 1; cd06654"
                     /db_xref="CDD:270820"
     Site            order(276..280,284,297,299,328,344..348,350..351,354,389,
                     391..394,396,406..407,410,423..427,429,456,465..467)
                     /site_type="active"
                     /db_xref="CDD:270820"
     Site            order(276..280,284,297,299,328,344..348,350..351,354,
                     393..394,396,406..407)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270820"
     Site            order(279..280,389,391..393,410,423..427,429,456,465..467)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270820"
     Site            order(281,315,384,386..389,407..408,435..436,438,443,468,
                     471,474)
                     /site_type="other"
                     /note="AID interaction site [polypeptide binding]"
                     /db_xref="CDD:270820"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK2.
                     /evidence=ECO:0000269|PubMed:17726028,
                     ECO:0000269|PubMed:17989089; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     Site            406..429
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270820"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis, BRSK2 and
                     PDPK1. /evidence=ECO:0000269|PubMed:10551809,
                     ECO:0000269|PubMed:10995762, ECO:0000269|PubMed:22153498,
                     ECO:0000269|PubMed:22669945; propagated from
                     UniProtKB/Swiss-Prot (Q13153.2)"
     CDS             1..545
                     /gene="PAK1"
                     /gene_synonym="alpha-PAK; IDDMSSD; p65-PAK; PAKalpha"
                     /coded_by="NM_001376274.1:220..1857"
                     /note="isoform 2 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS8250.1"
                     /db_xref="GeneID:5058"
                     /db_xref="HGNC:HGNC:8590"
                     /db_xref="MIM:602590"
ORIGIN      
        1 msnngldiqd kppappmrnt stmigagskd agtlnhgskp lppnpeekkk kdrfyrsilp
       61 gdktnkkkek erpeislpsd fehtihvgfd avtgeftgmp eqwarllqts nitkseqkkn
      121 pqavldvlef ynskktsnsq kymsftdksa edynssnaln vkavsetpav ppvsededdd
      181 dddatpppvi aprpehtksv ytrsvieplp vtptrdvats pisptenntt ppdaltrnte
      241 kqkkkpkmsd eeileklrsi vsvgdpkkky trfekigqga sgtvytamdv atgqevaikq
      301 mnlqqqpkke liineilvmr enknpnivny ldsylvgdel wvvmeylagg sltdvvtetc
      361 mdegqiaavc reclqalefl hsnqvihrdi ksdnillgmd gsvkltdfgf caqitpeqsk
      421 rstmvgtpyw mapevvtrka ygpkvdiwsl gimaiemieg eppylnenpl ralyliatng
      481 tpelqnpekl saifrdflnr clemdvekrg sakellqhqf lkiakplssl tpliaaakea
      541 tknnh
//
LOCUS       NP_001378857            1808 aa            linear   PRI 21-NOV-2025
DEFINITION  Golgi-specific brefeldin A-resistance guanine nucleotide exchange
            factor 1 isoform 12 [Homo sapiens].
ACCESSION   NP_001378857
VERSION     NP_001378857.1
DBSOURCE    REFSEQ: accession NM_001391928.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1808)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1808)
  AUTHORS   Hirano,J., Hayashi,T., Kitamura,K., Nishimura,Y., Shimizu,H.,
            Okamoto,T., Okada,K., Uemura,K., Yeh,M.T., Ono,C., Taguwa,S.,
            Muramatsu,M. and Matsuura,Y.
  TITLE     Enterovirus 3A protein disrupts endoplasmic reticulum homeostasis
            through interaction with GBF1
  JOURNAL   J Virol 98 (7), e0081324 (2024)
   PUBMED   38904364
  REMARK    GeneRIF: Enterovirus 3A protein disrupts endoplasmic reticulum
            homeostasis through interaction with GBF1.
REFERENCE   3  (residues 1 to 1808)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1808)
  AUTHORS   Navare,A.T., Mast,F.D., Olivier,J.P., Bertomeu,T., Neal,M.L.,
            Carpp,L.N., Kaushansky,A., Coulombe-Huntington,J., Tyers,M. and
            Aitchison,J.D.
  TITLE     Viral protein engagement of GBF1 induces host cell vulnerability
            through synthetic lethality
  JOURNAL   J Cell Biol 221 (11) (2022)
   PUBMED   36305789
  REMARK    GeneRIF: Viral protein engagement of GBF1 induces host cell
            vulnerability through synthetic lethality.
REFERENCE   5  (residues 1 to 1808)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1808)
  AUTHORS   Garcia-Mata,R. and Sztul,E.
  TITLE     The membrane-tethering protein p115 interacts with GBF1, an ARF
            guanine-nucleotide-exchange factor
  JOURNAL   EMBO Rep 4 (3), 320-325 (2003)
   PUBMED   12634853
  REMARK    GeneRIF: novel interaction between p115 and Golgi-specific
            brefeldin-A-resistant factor 1 (GBF1)
REFERENCE   7  (residues 1 to 1808)
  AUTHORS   Kawamoto,K., Yoshida,Y., Tamaki,H., Torii,S., Shinotsuka,C.,
            Yamashina,S. and Nakayama,K.
  TITLE     GBF1, a guanine nucleotide exchange factor for ADP-ribosylation
            factors, is localized to the cis-Golgi and involved in membrane
            association of the COPI coat
  JOURNAL   Traffic 3 (7), 483-495 (2002)
   PUBMED   12047556
  REMARK    GeneRIF: detailed subcellular localization to the cis-Golgi
REFERENCE   8  (residues 1 to 1808)
  AUTHORS   Verhoeven,K., Villanova,M., Rossi,A., Malandrini,A., De Jonghe,P.
            and Timmerman,V.
  TITLE     Localization of the gene for the intermediate form of
            Charcot-Marie-Tooth to chromosome 10q24.1-q25.1
  JOURNAL   Am J Hum Genet 69 (4), 889-894 (2001)
   PUBMED   11533914
REFERENCE   9  (residues 1 to 1808)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   10 (residues 1 to 1808)
  AUTHORS   Mansour,S.J., Herbrick,J.A., Scherer,S.W. and Melancon,P.
  TITLE     Human GBF1 is a ubiquitously expressed gene of the sec7 domain
            family mapping to 10q24
  JOURNAL   Genomics 54 (2), 323-327 (1998)
   PUBMED   9828135
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160011.35, AL356420.14 and
            AL121928.13.
            
            Summary: This gene encodes a member of the Sec7 domain family. The
            encoded protein is a guanine nucleotide exchange factor that
            regulates the recruitment of proteins to membranes by mediating GDP
            to GTP exchange. The encoded protein is localized to the Golgi
            apparatus and plays a role in vesicular trafficking by activating
            ADP ribosylation factor 1. The encoded protein has also been
            identified as an important host factor for viral replication.
            Multiple transcript variants have been observed for this gene.
            [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2607153.1,
                                           SRR14038197.2226348.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1808
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..1808
                     /product="Golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1 isoform 12"
                     /note="golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1; BFA-resistant GEF 1"
                     /calculated_mol_wt=201274
     Region          <429..>1131
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Region          652..837
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          <1743..1806
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1808
                     /gene="GBF1"
                     /gene_synonym="ARF1GEF; CMT2GG; CMTDI2; CMTDIA"
                     /coded_by="NM_001391928.1:261..5687"
                     /note="isoform 12 is encoded by transcript variant 20"
                     /db_xref="GeneID:8729"
                     /db_xref="HGNC:HGNC:4181"
                     /db_xref="MIM:603698"
ORIGIN      
        1 mvdkniyiiq geinivvgai krnarwstht pldeerdpll hsfghlkevl nsitelseie
       61 pnvflrpfle virsedttgp itglaltsvn kflsyalidp thegtaegme nmadavthar
      121 fvgtdpasde vvlmkilqvl rtllltpvga hltnesvcei mqscfricfe mrlsellrks
      181 aehtlvdmvq llftrlpqfk eepknyvgtn mkklkmragg msdsskwkkq krsprpprhm
      241 tkvtpgselp tpngttlssn ltggmpfidv ptpissasse aasavvspst dsglefssqt
      301 tskedltdle qpgspgysta tepgsselgv peqpdlqegt hveksqsasv esipevleec
      361 tspadhsdsa svhdmdyvnp rgvrftqssq kegtalvpyg lpcirelfrf lisltnphdr
      421 hnsevmihmg lhlltvales apvaqcqtll glikdemcrh lfqllsierl nlyaaslrvc
      481 fllfesmreh lkfqmemyik klmeiitven pkmpyemkem aleaivqlwr ipsfvtelyi
      541 nydcdyycsn lfeeltklls knafpvsgql ytthllslda lltvidstea hcqakvlnsl
      601 tqqekketar psceivdgtr easntdkkfa rkpprfscll pdprelieik nkkkllitgt
      661 eqfnqkpkkg iqflqekgll tipmdnteva qwlrenprld kkmigefvsd rknidllesf
      721 vstfsfqglr ldealrlyle afrlpgeapv iqrlleafte rwmncngspf ansdacfsla
      781 yavimlntdq hnhnvrkqna pmtleefrkn lkgvnggkdf eqdiledmyh aikneeivmp
      841 eeqtglvren yvwnvllhrg atpegiflrv ptasydldlf tmtwgptiaa lsyvfdksle
      901 etiiqkaisg frkcamisah yglsdvfdnl iislckftal ssesienlps vfgsnpkahi
      961 aaktvfhlah rhgdilregw knimeamlql fraqllpkam ievedfvdpn gkislqreet
     1021 psnrgestvl sfvswltlsg peqssvrgps tenqeakrva lecikqcdpe kmiteskflq
     1081 leslqelmka lvsvtpdeet ydeedaafcl emllrivlen rdrvgcvwqt vrdhlyhlcv
     1141 qaqdfcflve ravvgllrla irllrreeis aqvllslril llmkpsvlsr vshqvayglh
     1201 ellktnaani hsgddwatlf tllecigsgv kppaalqata radapdagaq sdselpsyhq
     1261 ndvsldrgyt sdsevytdhg rpgkihrsat dadvvnsgwl vvgkddvdns kpgpsrpgps
     1321 plinqysltv gldlgphdtk sllkcvesls fivrdaahit pdnfelcvkt lrifveasln
     1381 ggcksqekrg kshkydskgn rfkkkskegs mlrrprtssq hasrggqsdd dedegvpasy
     1441 htvslqlldl mhtlhtraas iysswaeeqr hletggqkie adsrtlwahc wcpllqgiac
     1501 lccdarrqvr mqaltylqra llvhdlqkld alewescfnk vlfplltkll enispadvgg
     1561 meetrmrast llskvflqhl spllslstfa alwltildfm dkymhagssd llseaipesl
     1621 knmllvmdta eifhsadarg ggpsalweit weridcflph lrdelfkqtv iqdpmpmepq
     1681 gqkplasahl tsaagdtrtp ghppppeips elgacdfekp espraassss pgspvassps
     1741 rlsptpdgpp plaqpplilq plasplqvgv ppmtlpiiln palieatspv pllatprptd
     1801 piptsevn
//
LOCUS       NP_002899                619 aa            linear   PRI 21-NOV-2025
DEFINITION  proto-oncogene c-Rel isoform 1 [Homo sapiens].
ACCESSION   NP_002899
VERSION     NP_002899.1
DBSOURCE    REFSEQ: accession NM_002908.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   4  (residues 1 to 619)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   5  (residues 1 to 619)
  AUTHORS   Neumann,M., Tsapos,K., Scheppler,J.A., Ross,J. and Franza,B.R. Jr.
  TITLE     Identification of complex formation between two intracellular
            tyrosine kinase substrates: human c-Rel and the p105 precursor of
            p50 NF-kappa B
  JOURNAL   Oncogene 7 (11), 2095-2104 (1992)
   PUBMED   1437141
REFERENCE   6  (residues 1 to 619)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
REFERENCE   7  (residues 1 to 619)
  AUTHORS   Ruben,S.M., Klement,J.F., Coleman,T.A., Maher,M., Chen,C.H. and
            Rosen,C.A.
  TITLE     I-Rel: a novel rel-related protein that inhibits NF-kappa B
            transcriptional activity
  JOURNAL   Genes Dev 6 (5), 745-760 (1992)
   PUBMED   1577270
REFERENCE   8  (residues 1 to 619)
  AUTHORS   Kochel,T. and Rice,N.R.
  TITLE     v-rel- and c-rel-protein complexes bind to the NF-kappa B site in
            vitro
  JOURNAL   Oncogene 7 (3), 567-572 (1992)
   PUBMED   1549370
REFERENCE   9  (residues 1 to 619)
  AUTHORS   Brownell,E., Mittereder,N. and Rice,N.R.
  TITLE     A human rel proto-oncogene cDNA containing an Alu fragment as a
            potential coding exon
  JOURNAL   Oncogene 4 (7), 935-942 (1989)
   PUBMED   2666912
REFERENCE   10 (residues 1 to 619)
  AUTHORS   Brownell,E., Kozak,C.A., Fowle,J.R. 3rd, Modi,W.S., Rice,N.R. and
            O'Brien,S.J.
  TITLE     Comparative genetic mapping of cellular rel sequences in man,
            mouse, and the domestic cat
  JOURNAL   Am J Hum Genet 39 (2), 194-202 (1986)
   PUBMED   3529946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY123671.1, X75042.1,
            AC010733.8 and BG036646.1.
            
            Summary: This gene encodes a protein that belongs to the Rel
            homology domain/immunoglobulin-like fold, plexin, transcription
            factor (RHD/IPT) family. Members of this family regulate genes
            involved in apoptosis, inflammation, the immune response, and
            oncogenic processes. This proto-oncogene plays a role in the
            survival and proliferation of B lymphocytes. Mutation or
            amplification of this gene is associated with B-cell lymphomas,
            including Hodgkin's lymphoma. Single nucleotide polymorphisms in
            this gene are associated with susceptibility to ulcerative colitis
            and rheumatoid arthritis. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Apr 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.61931.1, X75042.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.1"
     Protein         1..619
                     /product="proto-oncogene c-Rel isoform 1"
                     /note="proto-oncogene c-Rel; oncogene REL, avian
                     reticuloendotheliosis; v-rel avian reticuloendotheliosis
                     viral oncogene homolog"
                     /calculated_mol_wt=68389
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q04864.1)"
     Region          8..179
                     /region_name="RHD-n_c-Rel"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of c-Rel; cd07933"
                     /db_xref="CDD:143649"
     Site            order(22,24..25,27..28,31,111..112,179)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143649"
     Region          186..281
                     /region_name="IPT_NFkappaB"
                     /note="IPT domain of the transcription factor NFkappaB and
                     related transcription factors. NFkappaB is considered a
                     central regulator of stress responses, activated by
                     different stressful conditions, including physical stress,
                     oxidative stress, and exposure to...; cd01177"
                     /db_xref="CDD:238582"
     Site            order(187,189..191,193..195,230..232,245,256,275,278,280)
                     /site_type="other"
                     /note="ankyrin protein binding site [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(189..190,192,205,207,209,237..238,241,243)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(210,212,238..239)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238582"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q04864.1)"
     Region          290..295
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04864.1)"
     Region          399..437
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04864.1)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10823840; propagated from
                     UniProtKB/Swiss-Prot (Q04864.1)"
     Region          572..593
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04864.1)"
     CDS             1..619
                     /gene="REL"
                     /gene_synonym="C-Rel; HIVEN86A; IMD92"
                     /coded_by="NM_002908.4:268..2127"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1864.1"
                     /db_xref="GeneID:5966"
                     /db_xref="HGNC:HGNC:9954"
                     /db_xref="MIM:164910"
ORIGIN      
        1 masgaynpyi eiieqprqrg mrfrykcegr sagsipgehs tdnnrtypsi qimnyygkgk
       61 vritlvtknd pykphphdlv gkdcrdgyye aefgqerrpl ffqnlgircv kkkevkeaii
      121 trikaginpf nvpekqlndi edcdlnvvrl cfqvflpdeh gnlttalppv vsnpiydnra
      181 pntaelricr vnkncgsvrg gdeifllcdk vqkddievrf vlndweakgi fsqadvhrqv
      241 aivfktppyc kaitepvtvk mqlrrpsdqe vsesmdfryl pdekdtygnk akkqkttllf
      301 qklcqdhvet gfrhvdqdgl elltsgdppt lasqsagitv nfperprpgl lgsigegryf
      361 kkepnlfshd avvremptgv ssqaesyyps pgpissglsh hasmaplpss swssvahptp
      421 rsgntnplss fstrtlpsns qgippflrip vgndlnasna ciynnaddiv gmeassmpsa
      481 dlygisdpnm lsncsvnmmt tssdsmgetd nprllsmnle npscnsvldp rdlrqlhqms
      541 sssmsagans nttvfvsqsd afegsdfsca dnsminesgp snstnpnshg fvqdsqysgi
      601 gsmqneqlsd sfpyeffqv
//
LOCUS       NP_001363265             810 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger CCCH domain-containing protein 11A isoform 1 [Homo
            sapiens].
ACCESSION   NP_001363265
VERSION     NP_001363265.1
DBSOURCE    REFSEQ: accession NM_001376336.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Kases,K., Schubert,E., Hajikhezri,Z., Larsson,M., Devi,P.,
            Darweesh,M., Andersson,L., Akusjarvi,G., Punga,T. and Younis,S.
  TITLE     The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts
  JOURNAL   J Biol Chem 299 (8), 104959 (2023)
   PUBMED   37356722
  REMARK    GeneRIF: The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts.
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 810)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 810)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114402.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.97123.1,
                                           SRR1803612.29434.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..810
                     /product="zinc finger CCCH domain-containing protein 11A
                     isoform 1"
                     /note="zinc finger CCCH-type domain containing 11A; zinc
                     finger CCCH domain-containing protein 11A"
                     /calculated_mol_wt=89000
     Region          1..110
                     /region_name="zf-CCCH_3"
                     /note="Zinc-finger containing family; pfam15663"
                     /db_xref="CDD:464787"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          139..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          223..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          285..351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          367..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          482..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          715..768
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     CDS             1..810
                     /gene="ZC3H11A"
                     /gene_synonym="ZC3HDC11A"
                     /coded_by="NM_001376336.1:318..2750"
                     /note="isoform 1 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS30978.1"
                     /db_xref="GeneID:9877"
                     /db_xref="HGNC:HGNC:29093"
                     /db_xref="MIM:613513"
ORIGIN      
        1 mpnqgedcyf ffystctkgd scpfrhceaa ignetvctlw qegrcfrqvc rfrhmeidkk
       61 rseipcywen qptgcqklnc afhhnrgryv dglflppskt vlptvpespe eevkasqlsv
      121 qqnklsvqsn pspqlrsvmk vessenvpsp thppvvinaa dddeddddqf seegdetktp
      181 tlqptpevhn glrvtsvrkp avnikqgecl nfgiktleei kskkmkeksk kqgegssgvs
      241 slllhpepvp gpekenvrtv vrtvtlstkq geeplvrlsl terlgkrkfs aggdsdpplk
      301 rslaqrlgkk veapetnidk tpkkaqvsks lkerlgmsad pdnedatdkv nkvgeihvkt
      361 leeilleras qkrgelqtkl ktegpsktdd stsgarssst iriktfsevl aekkhrqqea
      421 erqkskkdtt ciklkidsei kktvvlppiv asrgqseepa gktksmqevh iktleeikle
      481 kalrvqqsse sstsspsqhe atpgarrllr itkrtgmkee knlqegnevd sqssirteak
      541 easgettgvd itkiqvkrce tmrekhmqkq qereksvltp lrgdvascnt qvaekpvlta
      601 vpgitrhltk rlptkssqkv evetsgigds llnvkcaaqt lekrgkakpk vnvkpsvvkv
      661 vsspklapkr kavemhaavi aavkplssss vlqeppakka avavvplvse dksvtvpeae
      721 nprdslvlpp tqsssdsspp evsgpsssqm smktrrlssa stgkpplsve ddfekliwei
      781 sggkleaeid ldpgkdeddl llelsemids
//
LOCUS       NP_001123359             568 aa            linear   PRI 21-NOV-2025
DEFINITION  dnaJ homolog subfamily C member 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001123359
VERSION     NP_001123359.1
DBSOURCE    REFSEQ: accession NM_001129887.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Yang,F., Hu,A., Guo,Y., Wang,J., Li,D., Wang,X., Jin,S., Yuan,B.,
            Cai,S., Zhou,Y., Li,Q., Chen,G., Gao,H., Zheng,L. and Tong,Q.
  TITLE     p113 isoform encoded by CUX1 circular RNA drives tumor progression
            via facilitating ZRF1/BRD4 transactivation
  JOURNAL   Mol Cancer 20 (1), 123 (2021)
   PUBMED   34579723
  REMARK    GeneRIF: p113 isoform encoded by CUX1 circular RNA drives tumor
            progression via facilitating ZRF1/BRD4 transactivation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 568)
  AUTHORS   Liu,H., Li,J., Zhao,H., Liu,X. and Ye,X.
  TITLE     DNAJC2 is reversely regulated by miR-627-3p, promoting the
            proliferation of colorectal cancer
  JOURNAL   Mol Med Rep 24 (2) (2021)
   PUBMED   34165158
  REMARK    GeneRIF: DNAJC2 is reversely regulated by miR6273p, promoting the
            proliferation of colorectal cancer.
REFERENCE   5  (residues 1 to 568)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 568)
  AUTHORS   Hundley,H.A., Walter,W., Bairstow,S. and Craig,E.A.
  TITLE     Human Mpp11 J protein: ribosome-tethered molecular chaperones are
            ubiquitous
  JOURNAL   Science 308 (5724), 1032-1034 (2005)
   PUBMED   15802566
  REMARK    GeneRIF: concluded that Mpp11, an ortholog of yeast Zuo, is a
            ribosome-associated J protein; proposed that in metazoans,
            ribosome-associated Zuo and Mpp11 orthologs recruit cytosolic Hsc70
            to short ribosome-bound nascent chains as they exit the ribosome
REFERENCE   7  (residues 1 to 568)
  AUTHORS   Greiner,J., Ringhoffer,M., Taniguchi,M., Li,L., Schmitt,A.,
            Shiku,H., Dohner,H. and Schmitt,M.
  TITLE     mRNA expression of leukemia-associated antigens in patients with
            acute myeloid leukemia for the development of specific
            immunotherapies
  JOURNAL   Int J Cancer 108 (5), 704-711 (2004)
   PUBMED   14696097
REFERENCE   8  (residues 1 to 568)
  AUTHORS   Greiner,J., Ringhoffer,M., Taniguchi,M., Hauser,T., Schmitt,A.,
            Dohner,H. and Schmitt,M.
  TITLE     Characterization of several leukemia-associated antigens inducing
            humoral immune responses in acute and chronic myeloid leukemia
  JOURNAL   Int J Cancer 106 (2), 224-231 (2003)
   PUBMED   12800198
REFERENCE   9  (residues 1 to 568)
  AUTHORS   Resto,V.A., Caballero,O.L., Buta,M.R., Westra,W.H., Wu,L.,
            Westendorf,J.M., Jen,J., Hieter,P. and Sidransky,D.
  TITLE     A putative oncogenic role for MPP11 in head and neck squamous cell
            cancer
  JOURNAL   Cancer Res 60 (19), 5529-5535 (2000)
   PUBMED   11034098
REFERENCE   10 (residues 1 to 568)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004668.1, X98260.1 and
            AI140595.1.
            
            Summary: This gene is a member of the M-phase phosphoprotein (MPP)
            family. The gene encodes a phosphoprotein with a J domain and a Myb
            DNA-binding domain which localizes to both the nucleus and the
            cytosol. The protein is capable of forming a heterodimeric complex
            that associates with ribosomes, acting as a molecular chaperone for
            nascent polypeptide chains as they exit the ribosome. This protein
            was identified as a leukemia-associated antigen and expression of
            the gene is upregulated in leukemic blasts. Also, chromosomal
            aberrations involving this gene are associated with primary head
            and neck squamous cell tumors. This gene has a pseudogene on
            chromosome 6. Alternatively spliced variants which encode different
            protein isoforms have been described. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (2) lacks two alternate in-frame
            exons, compared to variant 1, resulting in a shorter protein
            (isoform 2), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X98260.1, SRR14038192.1906402.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..568
                     /product="dnaJ homolog subfamily C member 2 isoform 2"
                     /note="M-phase phosphoprotein 11; dnaJ homolog subfamily C
                     member 2; zuotin-related factor 1; DnaJ (Hsp40) homolog,
                     subfamily C, member 2"
                     /calculated_mol_wt=65783
     Region          13..49
                     /region_name="zuotin_NTD"
                     /note="N-terminal domain of fungal ribosome associated
                     J-protein zuotin and similar proteins; cd23953"
                     /db_xref="CDD:467935"
     Region          75..361
                     /region_name="ZUO1"
                     /note="Ribosome-associated chaperone zuotin [Translation,
                     ribosomal structure and biogenesis / Posttranslational
                     modification, protein turnover, chaperones]; COG5269"
                     /db_xref="CDD:227594"
     Region          400..453
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cd00167"
                     /db_xref="CDD:238096"
     Site            order(401,441..442,444..445,447..449,451..453)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238096"
     Region          500..547
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cd00167"
                     /db_xref="CDD:238096"
     Site            order(501,534..535,537..538,540..542,544..546)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238096"
     CDS             1..568
                     /gene="DNAJC2"
                     /gene_synonym="MPHOSPH11; MPP11; ZRF1; ZUO1"
                     /coded_by="NM_001129887.3:146..1852"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47679.1"
                     /db_xref="GeneID:27000"
                     /db_xref="HGNC:HGNC:13192"
                     /db_xref="MIM:605502"
ORIGIN      
        1 mlllpsaadg rgtaithalt sastlcqvep vgrwfeafvk rrnrnasasf qeledkkels
       61 eesedeelql eefpmlktld pkdwknqdhy avlglghvry katqrqikaa hkamvlkhhp
      121 dkrkaagepi kegdndyftc itkayemlsd pvkrrafnsv dptfdnsvps kseakdnffe
      181 vftpvferns rwsnkknvpk lgdmnssfed vdifysfwyn fdswrefsyl deeekekaec
      241 rderrwiekq nratraqrkk eemnrirtlv dnayscdpri kkfkeeekak keaekkakae
      301 akrkeqeake kqrqaeleaa rlakekeeee vrqqallakk ekdiqkkaik kerqklrnsc
      361 kieeineqir kekeeaearm rqasknteks tggggngskn wseddlqlli kavnlfpagt
      421 nsrweviany mnihsssgvk rtakdvigka kslqkldphq kddinkkafd kfkkehgvvp
      481 qadnatpser fegpytdftp wtteeqklle qalktypvnt perwekiaea vpgrtkkdcm
      541 krykelvemv kakkaaqeqv lnasrakk
//
LOCUS       NP_001369467             655 aa            linear   PRI 21-NOV-2025
DEFINITION  amyloid beta precursor like protein 2 isoform 22 precursor [Homo
            sapiens].
ACCESSION   NP_001369467
VERSION     NP_001369467.1
DBSOURCE    REFSEQ: accession NM_001382538.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Tao,Z., Huang,J. and Li,J.
  TITLE     Comprehensive intratumoral heterogeneity landscaping of liver
            hepatocellular carcinoma and discerning of APLP2 in cancer
            progression
  JOURNAL   Environ Toxicol 39 (2), 612-625 (2024)
   PUBMED   37515494
  REMARK    GeneRIF: Comprehensive intratumoral heterogeneity landscaping of
            liver hepatocellular carcinoma and discerning of APLP2 in cancer
            progression.
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Huang,X., Yang,J., Xi,H., Zhang,M., Oh,Y., Jin,Z. and Zheng,Z.
  TITLE     Implication of Amyloid Precursor-like Protein 2 Expression in
            Cutaneous Squamous Cell Carcinoma Pathogenesis
  JOURNAL   In Vivo 38 (1), 399-408 (2024)
   PUBMED   38148084
  REMARK    GeneRIF: Implication of Amyloid Precursor-like Protein 2 Expression
            in Cutaneous Squamous Cell Carcinoma Pathogenesis.
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Chen,J., Tang,F., Li,H., Wu,X., Yang,Y., Liu,Z., Huang,X., Wang,J.,
            Zheng,R., Wang,L., Liu,H., Xu,J., Wang,P. and Liu,F.
  TITLE     Mycobacterium tuberculosis suppresses APLP2 expression to enhance
            its survival in macrophage
  JOURNAL   Int Immunopharmacol 124 (Pt B), 111058 (2023)
   PUBMED   37844466
  REMARK    GeneRIF: Mycobacterium tuberculosis suppresses APLP2 expression to
            enhance its survival in macrophage.
REFERENCE   5  (residues 1 to 655)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Blangy,A., Vidal,F., Cuzin,F., Yang,Y.H., Boulukos,K. and
            Rassoulzadegan,M.
  TITLE     CDEBP, a site-specific DNA-binding protein of the 'APP-like'
            family, is required during the early development of the mouse
  JOURNAL   J Cell Sci 108 (Pt 2), 675-683 (1995)
   PUBMED   7539437
REFERENCE   7  (residues 1 to 655)
  AUTHORS   von der Kammer,H., Hanes,J., Klaudiny,J. and Scheit,K.H.
  TITLE     A human amyloid precursor-like protein is highly homologous to a
            mouse sequence-specific DNA-binding protein
  JOURNAL   DNA Cell Biol 13 (11), 1137-1143 (1994)
   PUBMED   7702756
REFERENCE   8  (residues 1 to 655)
  AUTHORS   Bush,A.I., Pettingell,W.H. Jr., de Paradis,M., Tanzi,R.E. and
            Wasco,W.
  TITLE     The amyloid beta-protein precursor and its mammalian homologues.
            Evidence for a zinc-modulated heparin-binding superfamily
  JOURNAL   J Biol Chem 269 (43), 26618-26621 (1994)
   PUBMED   7929392
REFERENCE   9  (residues 1 to 655)
  AUTHORS   von der Kammer,H., Loffler,C., Hanes,J., Klaudiny,J., Scheit,K.H.
            and Hansmann,I.
  TITLE     The gene for the amyloid precursor-like protein APLP2 is assigned
            to human chromosome 11q23-q25
  JOURNAL   Genomics 20 (2), 308-311 (1994)
   PUBMED   8020984
REFERENCE   10 (residues 1 to 655)
  AUTHORS   Wasco,W., Gurubhagavatula,S., Paradis,M.D., Romano,D.M.,
            Sisodia,S.S., Hyman,B.T., Neve,R.L. and Tanzi,R.E.
  TITLE     Isolation and characterization of APLP2 encoding a homologue of the
            Alzheimer's associated amyloid beta protein precursor
  JOURNAL   Nat Genet 5 (1), 95-100 (1993)
   PUBMED   8220435
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003041.3 and AP001183.6.
            
            Summary: This gene encodes amyloid precursor- like protein 2
            (APLP2), which is a member of the APP (amyloid precursor protein)
            family including APP, APLP1 and APLP2. This protein is ubiquitously
            expressed. It contains heparin-, copper- and zinc- binding domains
            at the N-terminus, BPTI/Kunitz inhibitor and E2 domains in the
            middle region, and transmembrane and intracellular domains at the
            C-terminus. This protein interacts with major histocompatibility
            complex (MHC) class I molecules. The synergy of this protein and
            the APP is required to mediate neuromuscular transmission, spatial
            learning and synaptic plasticity. This protein has been implicated
            in the pathogenesis of Alzheimer's disease. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            identified. [provided by RefSeq, Aug 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1043903.1,
                                           SRR11853564.6107.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.3"
     Protein         1..655
                     /product="amyloid beta precursor like protein 2 isoform 22
                     precursor"
                     /note="amyloid precursor protein homolog HSD-2; CDEI
                     box-binding protein; amyloid beta (A4) precursor-like
                     protein 2; testicular tissue protein Li 23; sperm membrane
                     protein YWK-II"
                     /calculated_mol_wt=71398
     sig_peptide     1..31
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q06481.2)"
                     /calculated_mol_wt=2878
     Region          42..>112
                     /region_name="A4_EXTRA"
                     /note="amyloid A4; smart00006"
                     /db_xref="CDD:128326"
     Region          213..264
                     /region_name="Kunitz_ABPP-like"
                     /note="Kunitz domain found in the amyloid-beta precursor
                     protein (ABPP) subfamily; cd22607"
                     /db_xref="CDD:438650"
     Site            order(220..228,243,245,247)
                     /site_type="other"
                     /note="serine protease binding site [polypeptide binding]"
                     /db_xref="CDD:438650"
     Region          269..451
                     /region_name="APP_E2"
                     /note="E2 domain of amyloid precursor protein; pfam12925"
                     /db_xref="CDD:463752"
     Region          572..652
                     /region_name="JMTM_APLP2"
                     /note="juxtamembrane and transmembrane (JMTM) domain found
                     in amyloid-like protein 2 (APLP-2) and similar proteins;
                     cd21709"
                     /db_xref="CDD:411992"
     Site            order(572..573,587,590..591,594..595,597..598,601..602,
                     605,608)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:411992"
     Site            order(573..575,591..592,594..595,597..602,605..610)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:411992"
     CDS             1..655
                     /gene="APLP2"
                     /gene_synonym="APLP-2; APPH; APPL2; CDEBP"
                     /coded_by="NM_001382538.1:85..2052"
                     /note="isoform 22 precursor is encoded by transcript
                     variant 24"
                     /db_xref="GeneID:334"
                     /db_xref="HGNC:HGNC:598"
                     /db_xref="MIM:104776"
ORIGIN      
        1 maatgtaaaa atgrllllll vgltapalal agyiealaan agtgfavaep qiamfcgkln
       61 mhvniqtgkw epdptgtksc fetkeevlqy cqemypelqi tnvmeanqrt kiigsvskee
      121 eeedeeeeee edeeedydvy ksefpteadl edfteaavde ddedeeegee vvedrdyyyd
      181 tfkgddynee nptepgsdgt msdkeithdv kavcsqeamt gpcravmprw yfdlskgkcv
      241 rfiyggcggn rnnfesedyc mavckamipp tplptndvdv yfetsaddne harfqkakeq
      301 leirhrnrmd rvkkeweeae lqaknlpkae rqtliqhfqa mvkalekeaa sekqqlveth
      361 larveamlnd rrrmalenyl aalqsdpprp hrilqalrry vraenkdrlh tirhyqhvla
      421 vdpekaaqmk sqvmthlhvi eerrnqslsl lykvpyvaqe iqeeidellq eqradmdqft
      481 asisetpvdv rvsseeseei ppfhpfhpfp alpenegsgv geqdggliga eekvinsknk
      541 vdenmvidet ldvkemifna ervggleeer esvgplredf slsssaligl lviavaiatv
      601 ivislvmlrk rqygtishgi vevdpmltpe erhlnkmqnh gyenptykyl eqmqi
//
LOCUS       NP_001363396             614 aa            linear   PRI 21-NOV-2025
DEFINITION  ephrin type-A receptor 7 isoform 6 precursor [Homo sapiens].
ACCESSION   NP_001363396
VERSION     NP_001363396.1
DBSOURCE    REFSEQ: accession NM_001376467.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Wang,L., Zhao,Q.F., Yang,B.B., Liang,H.J., Zhang,X.E., Zhang,X.Y.,
            Yang,W.J., Guo,Z.Y., Xu,X., Tian,F. and Wu,Q.H.
  TITLE     STAT3-EphA7 axis contributes to the progression of esophageal
            squamous cell carcinoma
  JOURNAL   Acta Oncol 62 (12), 1757-1766 (2023)
   PUBMED   37738252
  REMARK    GeneRIF: STAT3-EphA7 axis contributes to the progression of
            esophageal squamous cell carcinoma.
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 614)
  AUTHORS   Zhang,W., Cao,H., Yang,J., Zhao,J., Liang,Z., Kang,X. and Wang,R.
  TITLE     The identification and validation of EphA7 hypermethylation, a
            novel biomarker, in cervical cancer
  JOURNAL   BMC Cancer 22 (1), 636 (2022)
   PUBMED   35681118
  REMARK    GeneRIF: The identification and validation of EphA7
            hypermethylation, a novel biomarker, in cervical cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 614)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   5  (residues 1 to 614)
  AUTHORS   Chakraborty,S. and Varma,A.K.
  TITLE     Crystal structure of clinically reported mutations Gly656Arg,
            Gly656Glu and Asp751His identified in the kinase domain of EphA7
  JOURNAL   Biochem Biophys Res Commun 568, 62-67 (2021)
   PUBMED   34186436
  REMARK    GeneRIF: Crystal structure of clinically reported mutations
            Gly656Arg, Gly656Glu and Asp751His identified in the kinase domain
            of EphA7.
REFERENCE   6  (residues 1 to 614)
  AUTHORS   Zhou,R.
  TITLE     The Eph family receptors and ligands
  JOURNAL   Pharmacol Ther 77 (3), 151-181 (1998)
   PUBMED   9576626
  REMARK    Review article
REFERENCE   7  (residues 1 to 614)
  AUTHORS   Flanagan,J.G. and Vanderhaeghen,P.
  TITLE     The ephrins and Eph receptors in neural development
  JOURNAL   Annu Rev Neurosci 21, 309-345 (1998)
   PUBMED   9530499
  REMARK    Review article
REFERENCE   8  (residues 1 to 614)
  AUTHORS   Ciossek,T. and Ullrich,A.
  TITLE     Identification of Elf-1 and B61 as high affinity ligands for the
            receptor tyrosine kinase MDK1
  JOURNAL   Oncogene 14 (1), 35-43 (1997)
   PUBMED   9010230
REFERENCE   9  (residues 1 to 614)
  AUTHORS   Gale,N.W., Holland,S.J., Valenzuela,D.M., Flenniken,A., Pan,L.,
            Ryan,T.E., Henkemeyer,M., Strebhardt,K., Hirai,H., Wilkinson,D.G.,
            Pawson,T., Davis,S. and Yancopoulos,G.D.
  TITLE     Eph receptors and ligands comprise two major specificity subclasses
            and are reciprocally compartmentalized during embryogenesis
  JOURNAL   Neuron 17 (1), 9-19 (1996)
   PUBMED   8755474
REFERENCE   10 (residues 1 to 614)
  AUTHORS   Fox,G.M., Holst,P.L., Chute,H.T., Lindberg,R.A., Janssen,A.M.,
            Basu,R. and Welcher,A.A.
  TITLE     cDNA cloning and tissue distribution of five human EPH-like
            receptor protein-tyrosine kinases
  JOURNAL   Oncogene 10 (5), 897-905 (1995)
   PUBMED   7898931
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121966.10, AL591036.8 and
            AL354857.13.
            
            Summary: This gene belongs to the ephrin receptor subfamily of the
            protein-tyrosine kinase family. EPH and EPH-related receptors have
            been implicated in mediating developmental events, particularly in
            the nervous system. Receptors in the EPH subfamily typically have a
            single kinase domain and an extracellular region containing a
            Cys-rich domain and 2 fibronectin type III repeats. The ephrin
            receptors are divided into 2 groups based on the similarity of
            their extracellular domain sequences and their affinities for
            binding ephrin-A and ephrin-B ligands. Increased expression of this
            gene is associated with multiple forms of carcinoma. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Dec 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.226267.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q16.1"
     Protein         1..614
                     /product="ephrin type-A receptor 7 isoform 6 precursor"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-A receptor 7; tyrosine-protein kinase
                     receptor EHK-3; Eph homology kinase-3; receptor
                     protein-tyrosine kinase HEK11; EPH-like kinase 11; EPH
                     homology kinase 3"
                     /calculated_mol_wt=65667
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3316
     Region          30..206
                     /region_name="EphR_LBD_A7"
                     /note="Ligand Binding Domain of Ephrin type-A Receptor 7;
                     cd10485"
                     /db_xref="CDD:198453"
     Site            order(56,58..62,69..70,72,74,105,107,112..113,155,
                     159..160,163..165,192..194,196)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198453"
     Region          275..312
                     /region_name="Ephrin_rec_like"
                     /note="Tyrosine-protein kinase ephrin type A/B
                     receptor-like; pfam07699"
                     /db_xref="CDD:429604"
     Region          <314..>539
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            343
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15375.3)"
     Site            410
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15375.3)"
     Region          443..534
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(443,507,522)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(523..524,526..527)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            556..576
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15375.3)"
     CDS             1..614
                     /gene="EPHA7"
                     /gene_synonym="EHK-3; EHK3; EK11; HEK11"
                     /coded_by="NM_001376467.1:219..2063"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:2045"
                     /db_xref="HGNC:HGNC:3390"
                     /db_xref="MIM:602190"
ORIGIN      
        1 mvfqtrypsw iilcyiwllr fahtgeaqaa kevllldska qqtelewiss ppngweeisg
       61 ldenytpirt yqvcqvmepn qnnwlrtnwi skgnaqrifv elkftlrdcn slpgvlgtck
      121 etfnlyyyet dydtgrnire nlyvkidtia adesftqgdl gerkmklnte vreigplskk
      181 gfylafqdvg acialvsvkv yykkcwsiie nlaifpdtvt gsefsslvev rgtcvssaee
      241 eaenaprmhc saegewlvpi gkcickagyq qkgdtcepcg rgfyksssqd lqcsrcpths
      301 fsdkegssrc ecedgyyrap sdppyvactr ppsapqnlif ninqttvsle wsppadnggr
      361 ndvtyrilck rcsweqgecv pcgsnigymp qqtglednyv tvmdllahan ytfeveavng
      421 vsdlsrsqrl faavsittgq aapsqvsgvm kervlqrsve lswqepehpn gviteyeiky
      481 yekdqrerty stvktkstsa sinnlkpgtv yvfqirafta agygnysprl dvatleeatg
      541 kmfeatavss eqnpviiiav vavagtiilv fmvfgfiigr rhcgyskadq egdeelyfhy
      601 syvnicedtv lyps
//
LOCUS       NP_001229427             263 aa            linear   PRI 21-NOV-2025
DEFINITION  MIF4G domain-containing protein isoform 1 [Homo sapiens].
ACCESSION   NP_001229427
VERSION     NP_001229427.1
DBSOURCE    REFSEQ: accession NM_001242498.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Cakmakci,N.G., Lerner,R.S., Wagner,E.J., Zheng,L. and Marzluff,W.F.
  TITLE     SLIP1, a factor required for activation of histone mRNA translation
            by the stem-loop binding protein
  JOURNAL   Mol Cell Biol 28 (3), 1182-1194 (2008)
   PUBMED   18025107
  REMARK    GeneRIF: downregulation of endogenous SLIP1 reduces the rate of
            translation of endogenous histone mRNA and also reduces cell
            viability.
REFERENCE   8  (residues 1 to 263)
  AUTHORS   Miele,A., Medina,R., van Wijnen,A.J., Stein,G.S. and Stein,J.L.
  TITLE     The interactome of the histone gene regulatory factor HiNF-P
            suggests novel cell cycle related roles in transcriptional control
            and RNA processing
  JOURNAL   J Cell Biochem 102 (1), 136-148 (2007)
   PUBMED   17577209
REFERENCE   9  (residues 1 to 263)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 263)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022211.5, BI752882.1,
            AK300711.1 and BC033759.1.
            
            Summary: This gene encodes a protein which interacts with the
            N-terminus of the stem-loop binding protein (SLBP) and the 3' end
            of histone mRNA. This interaction facilitates the activation of
            histone mRNA translation. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jun 2011].
            
            Transcript Variant: This variant (1), as well as variant 6, encodes
            the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.98392.1,
                                           SRR14038193.2449058.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..263
                     /product="MIF4G domain-containing protein isoform 1"
                     /note="SLBP (stem loop binding protein)-interacting
                     protein 1; MIF4G domain-containing protein;
                     SLBP-interacting protein 1"
                     /calculated_mol_wt=29960
     Region          75..220
                     /region_name="MIF4G"
                     /note="MIF4G domain; cl02652"
                     /db_xref="CDD:413423"
     CDS             1..263
                     /gene="MIF4GD"
                     /gene_synonym="AD023; MIFD; SLIP1"
                     /coded_by="NM_001242498.2:139..930"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS58598.1"
                     /db_xref="GeneID:57409"
                     /db_xref="HGNC:HGNC:24030"
                     /db_xref="MIM:612072"
ORIGIN      
        1 mgepsreeyk iqsfdaetqq llktalkaps lectvacfet edgeysvcqr sysncsrlmp
       61 srcntqyrdp gavdlekvan vivdhslqdc vfskeagrmc yaiiqaeskq agqsvfrrgl
      121 lnrlqqeyqa reqlrarslq gwvcyvtfic nifdylrvnn mpmmalvnpv ydclfrlaqp
      181 dslskeeevd clvlqlhrvg eqlekmngqr mdelfvlird gfllptglss laqlllleii
      241 efraagwktt paahkyyyse vsd
//
LOCUS       NP_001369416            1490 aa            linear   PRI 21-NOV-2025
DEFINITION  WD repeat-containing protein 7 isoform 1 [Homo sapiens].
ACCESSION   NP_001369416 XP_006722494
VERSION     NP_001369416.1
DBSOURCE    REFSEQ: accession NM_001382487.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1490)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 1490)
  AUTHORS   Jaskolka,M.C., Winkley,S.R. and Kane,P.M.
  TITLE     RAVE and Rabconnectin-3 Complexes as Signal Dependent Regulators of
            Organelle Acidification
  JOURNAL   Front Cell Dev Biol 9, 698190 (2021)
   PUBMED   34249946
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1490)
  AUTHORS   Course,M.M., Gudsnuk,K., Smukowski,S.N., Winston,K., Desai,N.,
            Ross,J.P., Sulovari,A., Bourassa,C.V., Spiegelman,D., Couthouis,J.,
            Yu,C.E., Tsuang,D.W., Jayadev,S., Kay,M.A., Gitler,A.D., Dupre,N.,
            Eichler,E.E., Dion,P.A., Rouleau,G.A. and Valdmanis,P.N.
  TITLE     Evolution of a Human-Specific Tandem Repeat Associated with ALS
  JOURNAL   Am J Hum Genet 107 (3), 445-460 (2020)
   PUBMED   32750315
  REMARK    GeneRIF: Evolution of a Human-Specific Tandem Repeat Associated
            with ALS.
REFERENCE   4  (residues 1 to 1490)
  AUTHORS   Yu,D., Mathews,C.A., Scharf,J.M., Neale,B.M., Davis,L.K.,
            Gamazon,E.R., Derks,E.M., Evans,P., Edlund,C.K., Crane,J.,
            Fagerness,J.A., Osiecki,L., Gallagher,P., Gerber,G., Haddad,S.,
            Illmann,C., McGrath,L.M., Mayerfeld,C., Arepalli,S., Barlassina,C.,
            Barr,C.L., Bellodi,L., Benarroch,F., Berrio,G.B., Bienvenu,O.J.,
            Black,D.W., Bloch,M.H., Brentani,H., Bruun,R.D., Budman,C.L.,
            Camarena,B., Campbell,D.D., Cappi,C., Silgado,J.C., Cavallini,M.C.,
            Chavira,D.A., Chouinard,S., Cook,E.H., Cookson,M.R., Coric,V.,
            Cullen,B., Cusi,D., Delorme,R., Denys,D., Dion,Y., Eapen,V.,
            Egberts,K., Falkai,P., Fernandez,T., Fournier,E., Garrido,H.,
            Geller,D., Gilbert,D.L., Girard,S.L., Grabe,H.J., Grados,M.A.,
            Greenberg,B.D., Gross-Tsur,V., Grunblatt,E., Hardy,J., Heiman,G.A.,
            Hemmings,S.M., Herrera,L.D., Hezel,D.M., Hoekstra,P.J.,
            Jankovic,J., Kennedy,J.L., King,R.A., Konkashbaev,A.I.,
            Kremeyer,B., Kurlan,R., Lanzagorta,N., Leboyer,M., Leckman,J.F.,
            Lennertz,L., Liu,C., Lochner,C., Lowe,T.L., Lupoli,S.,
            Macciardi,F., Maier,W., Manunta,P., Marconi,M., McCracken,J.T.,
            Mesa Restrepo,S.C., Moessner,R., Moorjani,P., Morgan,J., Muller,H.,
            Murphy,D.L., Naarden,A.L., Nurmi,E., Ochoa,W.C., Ophoff,R.A.,
            Pakstis,A.J., Pato,M.T., Pato,C.N., Piacentini,J., Pittenger,C.,
            Pollak,Y., Rauch,S.L., Renner,T., Reus,V.I., Richter,M.A.,
            Riddle,M.A., Robertson,M.M., Romero,R., Rosario,M.C., Rosenberg,D.,
            Ruhrmann,S., Sabatti,C., Salvi,E., Sampaio,A.S., Samuels,J.,
            Sandor,P., Service,S.K., Sheppard,B., Singer,H.S., Smit,J.H.,
            Stein,D.J., Strengman,E., Tischfield,J.A., Turiel,M., Valencia
            Duarte,A.V., Vallada,H., Veenstra-VanderWeele,J., Walitza,S.,
            Wang,Y., Weale,M., Weiss,R., Wendland,J.R., Westenberg,H.G.,
            Shugart,Y.Y., Hounie,A.G., Miguel,E.C., Nicolini,H., Wagner,M.,
            Ruiz-Linares,A., Cath,D.C., McMahon,W., Posthuma,D., Oostra,B.A.,
            Nestadt,G., Rouleau,G.A., Purcell,S., Jenike,M.A., Heutink,P.,
            Hanna,G.L., Conti,D.V., Arnold,P.D., Freimer,N.B., Stewart,S.E.,
            Knowles,J.A., Cox,N.J. and Pauls,D.L.
  TITLE     Cross-disorder genome-wide analyses suggest a complex genetic
            relationship between Tourette's syndrome and OCD
  JOURNAL   Am J Psychiatry 172 (1), 82-93 (2015)
   PUBMED   25158072
REFERENCE   5  (residues 1 to 1490)
  AUTHORS   Edwards,A.C., Aliev,F., Bierut,L.J., Bucholz,K.K., Edenberg,H.,
            Hesselbrock,V., Kramer,J., Kuperman,S., Nurnberger,J.I. Jr.,
            Schuckit,M.A., Porjesz,B. and Dick,D.M.
  TITLE     Genome-wide association study of comorbid depressive syndrome and
            alcohol dependence
  JOURNAL   Psychiatr Genet 22 (1), 31-41 (2012)
   PUBMED   22064162
REFERENCE   6  (residues 1 to 1490)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1490)
  AUTHORS   Baranzini,S.E., Wang,J., Gibson,R.A., Galwey,N., Naegelin,Y.,
            Barkhof,F., Radue,E.W., Lindberg,R.L., Uitdehaag,B.M.,
            Johnson,M.R., Angelakopoulou,A., Hall,L., Richardson,J.C.,
            Prinjha,R.K., Gass,A., Geurts,J.J., Kragt,J., Sombekke,M.,
            Vrenken,H., Qualley,P., Lincoln,R.R., Gomez,R., Caillier,S.J.,
            George,M.F., Mousavi,H., Guerrero,R., Okuda,D.T., Cree,B.A.,
            Green,A.J., Waubant,E., Goodin,D.S., Pelletier,D., Matthews,P.M.,
            Hauser,S.L., Kappos,L., Polman,C.H. and Oksenberg,J.R.
  TITLE     Genome-wide association analysis of susceptibility and clinical
            phenotype in multiple sclerosis
  JOURNAL   Hum Mol Genet 18 (4), 767-778 (2009)
   PUBMED   19010793
REFERENCE   8  (residues 1 to 1490)
  AUTHORS   Kawabe,H., Sakisaka,T., Yasumi,M., Shingai,T., Izumi,G., Nagano,F.,
            Deguchi-Tawarada,M., Takeuchi,M., Nakanishi,H. and Takai,Y.
  TITLE     A novel rabconnectin-3-binding protein that directly binds a
            GDP/GTP exchange protein for Rab3A small G protein implicated in
            Ca(2+)-dependent exocytosis of neurotransmitter
  JOURNAL   Genes Cells 8 (6), 537-546 (2003)
   PUBMED   12786944
REFERENCE   9  (residues 1 to 1490)
  AUTHORS   Sanders,S., Keck-Waggoner,C.L., Zimonjic,D.B., Popescu,N.C. and
            Thorgeirsson,S.S.
  TITLE     Assignment of WDR7 (alias TRAG, TGF-beta resistance associated
            gene) to orthologous regions of human chromosome 18q21.1-->q22 and
            mouse chromosome 18D.1-E.3 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 88 (3-4), 324-325 (2000)
   PUBMED   10828621
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007052.4, AC008006.10 and
            AC012301.5.
            
            On May 12, 2020 this sequence version replaced XP_006722494.1.
            
            Summary: This gene encodes a member of the WD repeat protein
            family. WD repeats are minimally conserved regions of approximately
            40 amino acids typically bracketed by gly-his and trp-asp (GH-WD)
            that may facilitate formation of heterotrimeric or multiprotein
            complexes. Members of this family are involved in a variety of
            cellular processes, including cell cycle progression, signal
            transduction, apoptosis, and gene regulation. The encoded protein
            forms the beta subunit of rabconnectin-3 and binds directly with
            Rab3A GDP/GTP exchange protein and indirectly with Rab3A GDP/GTP
            activating protein; these proteins are regulators of Rab3 small G
            protein family members involved in control of the calcium-dependant
            exocytosis of neurotransmitters. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.204130.1,
                                           SRR1803612.19810.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1490
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.31"
     Protein         1..1490
                     /product="WD repeat-containing protein 7 isoform 1"
                     /note="WD repeat-containing protein 7; TGF-beta resistance
                     associated; rabconnectin-3 beta; TGF-beta
                     resistance-associated protein TRAG"
                     /calculated_mol_wt=163680
     Region          17..56
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4E6.2)"
     Region          <22..>189
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          22..62
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          62..104
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4E6.2)"
     Region          68..109
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          114..153
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          156..199
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4E6.2)"
     Region          162..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          324..366
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4E6.2)"
     Region          404..443
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4E6.2)"
     Region          408..>598
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          409..461
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          462..507
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4E6.2)"
     Region          516..558
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          558..597
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4E6.2)"
     Region          563..589
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          761..783
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4E6.2)"
     Region          911..945
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4E6.2)"
     Site            935
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4E6.2)"
     Region          1351..1390
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4E6.2)"
     Region          1357..1391
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <1366..>1426
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          1392..1432
                     /region_name="WD 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4E6.2)"
     Site            1456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4E6.2)"
     CDS             1..1490
                     /gene="WDR7"
                     /gene_synonym="TRAG"
                     /coded_by="NM_001382487.1:122..4594"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS11962.1"
                     /db_xref="GeneID:23335"
                     /db_xref="HGNC:HGNC:13490"
                     /db_xref="MIM:613473"
ORIGIN      
        1 magnslvlpi vlwgrkapth cisavlltdd gativtgchd gqiclwdlsv elqinprall
       61 fghtasitcl skacassdkq yivsasesge mclwdvsdgr cieftklact htgiqfyqfs
      121 vgnqregrll chghypeilv vdatslevly slvskispdw issmsiirsh rtqedtvval
      181 svtgilkvwi vtseisdmqd tepifeeesk piycqncqsi sfcaftqrsl lvvcskywrv
      241 fdagdysllc sgpsengqtw tggdfvssdk viiwtengqs yiyklpascl pasdsfrsdv
      301 gkavenlipp vqhilldrkd kellicppvt rffygcreyf hklliqgdss grlniwnisd
      361 tadkqgseeg lamttsislq eafdklnpcp agiidqlsvi pnsneplkvt asvyipahgr
      421 lvcgredgsi vivpatqtai vqllqgehml rrgwpphrtl rghrnkvtcl lyphqvsary
      481 dqrylisggv dfsviiwdif sgemkhifcv hggeitqllv ppencsarvq hcicsvasdh
      541 svgllslrek kcimlasrhl fpiqvikwrp sddylvvgcs dgsvyvwqmd tgaldrcvmg
      601 itaveilnac deavpaavds lshpavnlkq amtrrslaal knmahhklqt latnllasea
      661 sdkgnlpkys hnslmvqaik tnltdpdihv lffdvealii qllteeasrp ntalispenl
      721 qkasgssdkg gsfltgkraa vlfqqvketi kenikehlld deeedeeimr qrreesdpey
      781 rsskskpltl leynltmdta klfmsclhaw glnevldevc ldrlgmlkph ctvsfgllsr
      841 gghmslmlpg ynqpacklsh gktevgrklp asegvgkgty gvsravttqh llsiislant
      901 lmsmtnatfi gdhmkkgptr pprpstpdls kargspptss nivqgqikqv aapvvsarsd
      961 adhsgsdpps apalhtcflv negwsqlaam hcvmlpdllg ldkfrpplle mlarrwqdrc
     1021 levreaaqal llaelrrieq agrkeaidaw apylpqyidh vispgvtsea aqtittapda
     1081 sgpeakvqee ehdlvdddit tgclssvpqm kkistsyeer rkqataivll gvigaefgae
     1141 ieppklltrp rsssqipegf gltsggsnys larhtckalt flllqppspk lpphstirrt
     1201 aidligrgft vwepymdvsa vlmgllelca daekqlanit mglplspaad sarsarhals
     1261 liatarppaf ittiakevhr htalaantqs qqnmhtttla rakgeilrvi eiliekmptd
     1321 vvdllvevmd iimyclegsl vkkkglqecf paicrfymvs yyernhriav garhgsvaly
     1381 dirtgkcqti hghkgpitav afapdgryla tysntdshis fwqmntsllg sigmlnsapq
     1441 lrciktyqvp pvqpaspgsh nalklarliw tsnrnvilma hdgkehrfmv
//
LOCUS       NP_001245262             449 aa            linear   PRI 21-NOV-2025
DEFINITION  histidine ammonia-lyase isoform 2 [Homo sapiens].
ACCESSION   NP_001245262
VERSION     NP_001245262.1
DBSOURCE    REFSEQ: accession NM_001258333.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Rivera-Paredez,B., Hidalgo-Bravo,A., Leon-Reyes,G.,
            Barajas-Olmos,F., Martinez-Hernandez,A., Orozco,L.,
            Denova-Gutierrez,E., Salmeron,J. and Velazquez-Cruz,R.
  TITLE     The role of single nucleotide variant rs3819817 of the Histidine
            Ammonia-Lyase gene and 25-Hydroxyvitamin D on bone mineral density,
            adiposity markers, and skin pigmentation, in Mexican population
  JOURNAL   J Endocrinol Invest 46 (9), 1911-1921 (2023)
   PUBMED   36862244
  REMARK    GeneRIF: The role of single nucleotide variant rs3819817 of the
            Histidine Ammonia-Lyase gene and 25-Hydroxyvitamin D on bone
            mineral density, adiposity markers, and skin pigmentation, in
            Mexican population.
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Chen,K., Liu,H., Liu,Z., Bloomer,W., Amos,C.I., Lee,J.E., Li,X.,
            Nan,H. and Wei,Q.
  TITLE     Genetic variants in glutamine metabolic pathway genes predict
            cutaneous melanoma-specific survival
  JOURNAL   Mol Carcinog 58 (11), 2091-2103 (2019)
   PUBMED   31435991
  REMARK    GeneRIF: In the analysis of the genotype tissue expression (GTEx)
            project datasets, HAL rs17676826 C and NOXRED1 rs8012548 G alleles
            were significantly associated with their mRNA expression levels in
            sun-exposed skin of the lower leg (P = 6.62 x 10(-6) and 1.37 x
            10(-7) , respectively) and in sun-not-exposed suprapubic skin (P <
            .001 and 1.43 x 10(-8) , respectively).
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Yu,B., Li,A.H., Muzny,D., Veeraraghavan,N., de Vries,P.S.,
            Bis,J.C., Musani,S.K., Alexander,D., Morrison,A.C., Franco,O.H.,
            Uitterlinden,A., Hofman,A., Dehghan,A., Wilson,J.G., Psaty,B.M.,
            Gibbs,R., Wei,P. and Boerwinkle,E.
  TITLE     Association of Rare Loss-Of-Function Alleles in HAL, Serum
            Histidine: Levels and Incident Coronary Heart Disease
  JOURNAL   Circ Cardiovasc Genet 8 (2), 351-355 (2015)
   PUBMED   25575548
  REMARK    GeneRIF: Three LoF mutations in HAL were associated with increased
            histidine levels, which in turn were shown to be inversely related
            to the risk of CHD among both African Americans and European
            Americans.
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Aleman,G., Ortiz,V., Langley,E., Tovar,A.R. and Torres,N.
  TITLE     Regulation by glucagon of the rat histidase gene promoter in
            cultured rat hepatocytes and human hepatoblastoma cells
  JOURNAL   Am J Physiol Endocrinol Metab 289 (1), E172-E179 (2005)
   PUBMED   15741241
  REMARK    GeneRIF: This evidence supports that the Hal gene is turned on by
            glucocorticoids and by glucagon either via PKC or PKA, but prefers
            the PKA pathway.
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Kawai,Y., Moriyama,A., Asai,K., Coleman-Campbell,C.M., Sumi,S.,
            Morishita,H. and Suchi,M.
  TITLE     Molecular characterization of histidinemia: identification of four
            missense mutations in the histidase gene
  JOURNAL   Hum Genet 116 (5), 340-346 (2005)
   PUBMED   15806399
  REMARK    GeneRIF: This report describes the first mutations occurring in the
            coding region of the histidase structural gene in patients with
            histidinemia.
            Erratum:[Hum Genet. 2005 Dec;118(3-4):531-2]
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Suchi,M., Sano,H., Mizuno,H. and Wada,Y.
  TITLE     Molecular cloning and structural characterization of the human
            histidase gene (HAL)
  JOURNAL   Genomics 29 (1), 98-104 (1995)
   PUBMED   8530107
REFERENCE   9  (residues 1 to 449)
  AUTHORS   Suchi,M., Harada,N., Wada,Y. and Takagi,Y.
  TITLE     Molecular cloning of a cDNA encoding human histidase
  JOURNAL   Biochim Biophys Acta 1216 (2), 293-295 (1993)
   PUBMED   7916645
REFERENCE   10 (residues 1 to 449)
  AUTHORS   Taylor,R.G., Garcia-Heras,J., Sadler,S.J., Lafreniere,R.G.,
            Willard,H.F., Ledbetter,D.H. and McInnes,R.R.
  TITLE     Localization of histidase to human chromosome region 12q22----q24.1
            and mouse chromosome region 10C2----D1
  JOURNAL   Cytogenet Cell Genet 56 (3-4), 178-181 (1991)
   PUBMED   2055114
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596896.1, AK303544.1,
            D16626.1, AC126174.9 and AI248003.1.
            
            Summary: Histidine ammonia-lyase is a cytosolic enzyme catalyzing
            the first reaction in histidine catabolism, the nonoxidative
            deamination of L-histidine to trans-urocanic acid. Histidine
            ammonia-lyase defects cause histidinemia which is characterized by
            increased histidine and histamine and decreased urocanic acid in
            body fluids. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Apr
            2012].
            
            Transcript Variant: This variant (2) lacks an alternate coding exon
            compared to variant 1, that causes a frameshift. The resulting
            isoform (2) is shorter at the N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303544.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.1"
     Protein         1..449
                     /product="histidine ammonia-lyase isoform 2"
                     /EC_number="4.3.1.3"
                     /note="histidase"
                     /calculated_mol_wt=48992
     Region          1..417
                     /region_name="hutH"
                     /note="histidine ammonia-lyase; TIGR01225"
                     /db_xref="CDD:200086"
     Site            order(12,40..41,54,57,143..144,147..148,150,153,184,
                     186..188,190..191,194..195,201..202,205,208..209,212..213,
                     216..217,222..224,229,231..237,239..240,243,247,254,257,
                     261,265,268,271,283..284,286..287,289..292,294,296..301,
                     303..306,317..323,326,332..333,336,339..340)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:176460"
     CDS             1..449
                     /gene="HAL"
                     /gene_synonym="HIS; HSTD"
                     /coded_by="NM_001258333.2:906..2255"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58264.1"
                     /db_xref="GeneID:3034"
                     /db_xref="HGNC:HGNC:4806"
                     /db_xref="MIM:609457"
ORIGIN      
        1 mllalrinvl akgysgisle tlkqviemfn asclpyvpek gtvgasgdla plshlalglv
       61 gegkmwspks gwadakyvle ahglkpvilk pkeglaling tqmitslgce averasaiar
      121 qadivaaltl evlkgttkaf dtdihalrph rgqievafrf rslldsdhhp seiaeshrfc
      181 drvqdaytlr ccpqvhgvvn dtiafvknii ttelnsatdn pmvfanrget vsggnfhgey
      241 pakaldylai gihelaaise rrierlcnps lselpaflva egglnsgfmi ahctaaalvs
      301 enkalchpss vdslstsaat edhvsmggwa arkalrvieh veqvlaiell aacqgieflr
      361 plktttplek vydlvrsvvr pwikdrfmap dieaahrlll eqkvwevaap yiekyrmehi
      421 pesrplspta fslqflhkks tkipesedl
//
LOCUS       NP_001340587             531 aa            linear   PRI 21-NOV-2025
DEFINITION  WD repeat-containing protein 20 isoform 14 [Homo sapiens].
ACCESSION   NP_001340587 XP_016877260
VERSION     NP_001340587.1
DBSOURCE    REFSEQ: accession NM_001353658.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Jiang,L., Qi,X., Lai,M., Zhou,J., Yuan,M., You,J., Liu,Q., Pan,J.,
            Zhao,L., Ying,M., Ji,J., Li,K., Zhang,Y., Pan,W., He,Q., Yang,B.
            and Cao,J.
  TITLE     WDR20 prevents hepatocellular carcinoma senescence by orchestrating
            the simultaneous USP12/46-mediated deubiquitination of c-Myc
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2407904121 (2024)
   PUBMED   39432777
  REMARK    GeneRIF: WDR20 prevents hepatocellular carcinoma senescence by
            orchestrating the simultaneous USP12/46-mediated deubiquitination
            of c-Myc.
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Ng,V.H., Spencer,Z., Neitzel,L.R., Nayak,A., Loberg,M.A., Shen,C.,
            Kassel,S.N., Kroh,H.K., An,Z., Anthony,C.C., Bryant,J.M.,
            Lawson,A., Goldsmith,L., Benchabane,H., Hansen,A.G., Li,J.,
            D'Souza,S., Lebensohn,A.M., Rohatgi,R., Weiss,W.A., Weiss,V.L.,
            Williams,C., Hong,C.C., Robbins,D.J., Ahmed,Y. and Lee,E.
  TITLE     The USP46 complex deubiquitylates LRP6 to promote Wnt/beta-catenin
            signaling
  JOURNAL   Nat Commun 14 (1), 6173 (2023)
   PUBMED   37798301
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Olazabal-Herrero,A., Bilbao-Arribas,M., Carlevaris,O., Sendino,M.,
            Varela-Martinez,E., Jugo,B.M., Berra,E. and Rodriguez,J.A.
  TITLE     The dystrophia myotonica WD repeat-containing protein DMWD and
            WDR20 differentially regulate USP12 deubiquitinase
  JOURNAL   FEBS J 288 (20), 5943-5963 (2021)
   PUBMED   33844468
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Dahlberg,C.L. and Juo,P.
  TITLE     The WD40-repeat proteins WDR-20 and WDR-48 bind and activate the
            deubiquitinating enzyme USP-46 to promote the abundance of the
            glutamate receptor GLR-1 in the ventral nerve cord of
            Caenorhabditis elegans
  JOURNAL   J Biol Chem 289 (6), 3444-3456 (2014)
   PUBMED   24356955
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Kee,Y., Yang,K., Cohn,M.A., Haas,W., Gygi,S.P. and D'Andrea,A.D.
  TITLE     WDR20 regulates activity of the USP12 x UAF1 deubiquitinating
            enzyme complex
  JOURNAL   J Biol Chem 285 (15), 11252-11257 (2010)
   PUBMED   20147737
  REMARK    GeneRIF: WDR20 serves as a stimulatory subunit for preserving and
            regulating the activity of the subset of the UAF1 x USP12 complexes
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Smith,T.F.
  TITLE     Diversity of WD-repeat proteins
  JOURNAL   Subcell Biochem 48, 20-30 (2008)
   PUBMED   18925368
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133223.5 and AL359402.3.
            
            On Jul 21, 2017 this sequence version replaced XP_016877260.1.
            
            Summary: This gene encodes a WD repeat-containing protein that
            functions to preserve and regulate the activity of the USP12-UAF1
            deubiquitinating enzyme complex. Multiple alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Jun 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.121069.1,
                                           SRR1803614.64060.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.31"
     Protein         1..531
                     /product="WD repeat-containing protein 20 isoform 14"
                     /note="WD repeat-containing protein 20"
                     /calculated_mol_wt=57772
     Region          103..168
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <158..264
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          173..209
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          216..249
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..531
                     /gene="WDR20"
                     /gene_synonym="Bun107; DMR"
                     /coded_by="NM_001353658.2:230..1825"
                     /note="isoform 14 is encoded by transcript variant 14"
                     /db_xref="GeneID:91833"
                     /db_xref="HGNC:HGNC:19667"
                     /db_xref="MIM:617741"
ORIGIN      
        1 mwagsctsis trgsarqshe vgrteilisv lteaadlskp idkriykgtq ptchdfnhlt
       61 ataesvsllv gfsagqvqli dpikketskl fneerlidks rvtcvkwvpg seslflvahs
      121 sgnmylynve htcgttaphy qllkqgesfa vhtckskstr npllkwtvge galnefafsp
      181 dgkflacvsq dgflrvfnfd svelhgtmks yfggllcvcw spdgkyivtg geddlvtvws
      241 fvdcrviarg hghkswvsvv afdpyttsve egdpmefsgs dedfqdllhf grdranstqs
      301 rlskrnstds rpvsvtyrfg svgqdtqlcl wdltedilfp hqplsrarth tnvmnatspp
      361 agsngnsvtt pgnsvppplp rsnslphsav snagskssvm dgaiasgvsk fatlslhdrk
      421 erhhekdhkr nhsmghissk ssdklnlvtk tktdpaktlg tplcprmedv plleplickk
      481 iaherltvli fledcivtac qegfictwgr pgkvgslssp sqasspggtv v
//
LOCUS       NP_001371774            1030 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 101 [Homo sapiens].
ACCESSION   NP_001371774
VERSION     NP_001371774.1
DBSOURCE    REFSEQ: accession NM_001384845.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1030)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1030)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1030)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1030)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1030)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1030)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1030)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2097028.1,
                                           SRR14038195.215306.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1030
                     /product="microtubule-associated protein 4 isoform 101"
                     /note="MAP-4"
                     /calculated_mol_wt=108014
     Region          <468..812
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          870..899
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          901..930
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          932..962
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1030
                     /gene="MAP4"
                     /coded_by="NM_001384845.1:175..3267"
                     /note="isoform 101 is encoded by transcript variant 97"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 mayqeypnsq nwpedtnfcf qpeqvvdpiq tdpfkmyhdd dladlvfpss atadtsifag
       61 qndplkdsyg mspcntavvp qgwsvealns phsesfvspe avaeppqpta vplelakeie
      121 maseerppaq aleimmglkt tdmapskete malakdmala tktevalakd mesptkldvt
      181 lakdmqpsme sdmalvkdme lptekevalv kdvrwptetd vssaknvvlp tetevapakd
      241 vtllketera spikmdlaps kdmgppkenk keteraspik mdlapskdmg ppkenkivpa
      301 kdlvllseie vaqandiiss teissaekva lssetevala rdmtlppetn viltkdkalp
      361 leaevapvkd maqlpeteia pakdvapstv kevgllkdms plsetemalg kdvtpppete
      421 vvliknvclp pemevalted qvpalkteap lakdgvltla nnvtpakdvp plseteatpv
      481 pikdmeiaqt qkgisedshl eslqdvgqsa aptfmispet vtgtgkkcsl paeedsvlek
      541 lgerkpcnsq pselssetsg iarpeegrpv vsgtgnditt ppnkelppsp ekktkplatt
      601 qpaktstska ktqptslpkq papttiggln kkpmslasgl vpaappkrpa vasarpsilp
      661 skdvkpkpia dakapekras pskpasapas rsgskstqtv aktttaaava stgpssrsps
      721 tllpkkptai ktegkpaevk kmtaksvpad lsrpkststs smkktttlsg tapaagvvps
      781 rvkatpmpsr psttpfidkk ptsakpsstt prlsrlatnt sapdlknvrs kakvekktea
      841 aattrkpesn avtktagpia saqkqpagkv qivskkvsys hiqskcgskd nikhvpgggn
      901 vqiqnkkvdi skvsskcgsk anikhkpggg dvkiesqkln fkekaqakvg sldnvghlpa
      961 ggavkteggg seaplcpgpp ageepaisea apeagaptsa sglnghptls gggdqreaqt
     1021 ldsqiqetsi
//
LOCUS       NP_001374918            1162 aa            linear   PRI 21-NOV-2025
DEFINITION  large proline-rich protein BAG6 isoform 5 [Homo sapiens].
ACCESSION   NP_001374918
VERSION     NP_001374918.1
DBSOURCE    REFSEQ: accession NM_001387989.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1162)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 1162)
  AUTHORS   Alashkar Alhamwe,B., Ponath,V., Alhamdan,F., Dorsam,B.,
            Landwehr,C., Linder,M., Pauck,K., Miethe,S., Garn,H.,
            Finkernagel,F., Brichkina,A., Lauth,M., Tiwari,D.K., Buchholz,M.,
            Bachurski,D., Elmshauser,S., Nist,A., Stiewe,T., Pogge von
            Strandmann,L., Szymanski,W., Beutgen,V., Graumann,J.,
            Teply-Szymanski,J., Keber,C., Denkert,C., Jacob,R., Preusser,C. and
            Pogge von Strandmann,E.
  TITLE     BAG6 restricts pancreatic cancer progression by suppressing the
            release of IL33-presenting extracellular vesicles and the
            activation of mast cells
  JOURNAL   Cell Mol Immunol 21 (8), 918-931 (2024)
   PUBMED   38942797
  REMARK    GeneRIF: BAG6 restricts pancreatic cancer progression by
            suppressing the release of IL33-presenting extracellular vesicles
            and the activation of mast cells.
REFERENCE   3  (residues 1 to 1162)
  AUTHORS   Liu,L., Wu,J., Yan,Y., Cheng,S., Yu,S. and Wang,Y.
  TITLE     DERL2 (derlin 2) stabilizes BAG6 (BAG cochaperone 6) in
            chemotherapy resistance of cholangiocarcinoma
  JOURNAL   J Physiol Biochem 80 (1), 81-97 (2024)
   PUBMED   37815698
  REMARK    GeneRIF: DERL2 (derlin 2) stabilizes BAG6 (BAG cochaperone 6) in
            chemotherapy resistance of cholangiocarcinoma.
REFERENCE   4  (residues 1 to 1162)
  AUTHORS   Roboti,P., Lawless,C. and High,S.
  TITLE     Mitochondrial antiviral-signalling protein is a client of the BAG6
            protein quality control complex
  JOURNAL   J Cell Sci 135 (9) (2022)
   PUBMED   35543156
  REMARK    GeneRIF: Mitochondrial antiviral-signalling protein is a client of
            the BAG6 protein quality control complex.
REFERENCE   5  (residues 1 to 1162)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1162)
  AUTHORS   Ozaki,T., Hanaoka,E., Naka,M., Nakagawara,A. and Sakiyama,S.
  TITLE     Cloning and characterization of rat BAT3 cDNA
  JOURNAL   DNA Cell Biol 18 (6), 503-512 (1999)
   PUBMED   10390159
REFERENCE   7  (residues 1 to 1162)
  AUTHORS   Cross,S.J., Tonks,S., Trowsdale,J. and Campbell,R.D.
  TITLE     Novel detection of restriction fragment length polymorphisms in the
            human major histocompatibility complex
  JOURNAL   Immunogenetics 34 (6), 376-384 (1991)
   PUBMED   1684176
REFERENCE   8  (residues 1 to 1162)
  AUTHORS   Banerji,J., Sands,J., Strominger,J.L. and Spies,T.
  TITLE     A gene pair from the human major histocompatibility complex encodes
            large proline-rich proteins with multiple repeated motifs and a
            single ubiquitin-like domain
  JOURNAL   Proc Natl Acad Sci U S A 87 (6), 2374-2378 (1990)
   PUBMED   2156268
REFERENCE   9  (residues 1 to 1162)
  AUTHORS   Spies,T., Bresnahan,M. and Strominger,J.L.
  TITLE     Human major histocompatibility complex contains a minimum of 19
            genes between the complement cluster and HLA-B
  JOURNAL   Proc Natl Acad Sci U S A 86 (22), 8955-8958 (1989)
   PUBMED   2813433
REFERENCE   10 (residues 1 to 1162)
  AUTHORS   Spies,T., Blanck,G., Bresnahan,M., Sands,J. and Strominger,J.L.
  TITLE     A new cluster of genes within the human major histocompatibility
            complex
  JOURNAL   Science 243 (4888), 214-217 (1989)
   PUBMED   2911734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL662801.7.
            
            Summary: This gene was first characterized as part of a cluster of
            genes located within the human major histocompatibility complex
            class III region. This gene encodes a nuclear protein that is
            cleaved by caspase 3 and is implicated in the control of apoptosis.
            In addition, the protein forms a complex with E1A binding protein
            p300 and is required for the acetylation of p53 in response to DNA
            damage. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853564.23232.1,
                                           SRR14038193.960583.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1162
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..1162
                     /product="large proline-rich protein BAG6 isoform 5"
                     /note="scythe; large proline-rich protein BAT3; large
                     proline-rich protein BAG6; protein G3; HLA-B-associated
                     transcript 3; protein Scythe; BAG family molecular
                     chaperone regulator 6; BCL2 associated athanogene 6"
                     /calculated_mol_wt=122212
     Region          17..87
                     /region_name="Ubl_BAG6"
                     /note="ubiquitin-like (Ubl) domain found in
                     BCL2-associated athanogene 6 (BAG6) and similar proteins;
                     cd01809"
                     /db_xref="CDD:340507"
     Site            order(22..25,58,60,62..65,83..87)
                     /site_type="other"
                     /note="ZF interaction site [polypeptide binding]"
                     /db_xref="CDD:340507"
     Region          270..386
                     /region_name="BAG6"
                     /note="BCL2-associated athanogene 6; pfam12057"
                     /db_xref="CDD:463449"
     Region          <935..1126
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     CDS             1..1162
                     /gene="BAG6"
                     /gene_synonym="BAG-6; BAT3; D6S52E; G3"
                     /coded_by="NM_001387989.1:163..3651"
                     /note="isoform 5 is encoded by transcript variant 29"
                     /db_xref="CCDS:CCDS93882.1"
                     /db_xref="GeneID:7917"
                     /db_xref="HGNC:HGNC:13919"
                     /db_xref="MIM:142590"
ORIGIN      
        1 mepndststa veepdslevl vktldsqtrt fivgaqmnvk efkehiaasv sipsekqrli
       61 yqgrvlqddk klqeynvggk vihlverapp qthlpsgass gtgsasathg ggsppgtrgp
      121 gasvhdrnan syvmvgtfnl psdgsavdvh inmeqapiqs eprvrlvmaq hmirdiqtll
      181 srmecrggpq pqhsqpppqp pavtpepval ssqtsepves eapprepmea eeveerapaq
      241 npeltpgpap agptpapetn apnhpspaey vevlqelqrl esrlqpflqr yyevlgaaat
      301 tdynnnhegr eedqrlinlv geslrllgnt fvalsdlrcn lactpprhlh vvrpmshytt
      361 pmvlqqaaip iqinvgttvt mtgngtrppp tpnaeapppg pgqassvaps stnvessaeg
      421 apppgpappp atshprviri shqsvepvvm mhmniqdsgt qpggvpsapt gplgppghgq
      481 tlgstliqlp slppefmhav ahqithqamv aavasaaagq qvpgfptapt rvviarptpp
      541 qarpshpggp pvsgtlqgag lgtnaslaqm vsglvgqllm qpvlvaqgtp gmapppapat
      601 asasagttnt attagpapgg paqppptpqp smadlqfsql lgnllgpagp gaggsgvasp
      661 titvampgvp aflqgmtdfl qatqtapppp ppppppppap eqqtmpppgs psggagspgg
      721 lgleslspef ftsvvqgvls sllgslgara gssesiaafi qrlsgssnif epgadgalgf
      781 fgallsllcq nfsmvdvvml lhghfqplqr lqpqlrsffh qhylggqept psnirmatht
      841 litgleeyvr esfslvqvqp gvdiirtnle flqeqfnsia ahvlhctdsg fgarllelcn
      901 qglfeclaln lhclggqqme laavingrir rmsrgvnpsl vswlttmmgl rlqvvlehmp
      961 vgpdailryv rrvgdppqpl peepmevqga eraspepqre naspapgtta eeamsrgppp
     1021 apeggsrdeq dgasaetepw aaavppewvp iiqqdiqsqr kvkpqpplsd aylsgmpakr
     1081 rktmqgegpq lllseavsra akaagarplt speslsrdle apevqesyrq qlrsdiqkrl
     1141 qedpnyspqr fpnaqrafad dp
//
LOCUS       NP_001374644            1032 aa            linear   PRI 21-NOV-2025
DEFINITION  activated CDC42 kinase 1 isoform 11 [Homo sapiens].
ACCESSION   NP_001374644
VERSION     NP_001374644.1
DBSOURCE    REFSEQ: accession NM_001387715.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Zheng,D., Wei,Z., Zhang,C., Liu,W., Gong,C., Wu,F. and Guo,W.
  TITLE     ZNF692 promotes osteosarcoma cell proliferation, migration, and
            invasion through TNK2-mediated activation of the MEK/ERK pathway
  JOURNAL   Biol Direct 19 (1), 28 (2024)
   PUBMED   38650011
  REMARK    GeneRIF: ZNF692 promotes osteosarcoma cell proliferation,
            migration, and invasion through TNK2-mediated activation of the
            MEK/ERK pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Hodder,S., Fox,M., Binti Ahmad Mokhtar,A.M., Mott,H.R. and Owen,D.
  TITLE     ACKnowledging the role of the Activated-Cdc42 associated kinase
            (ACK) in regulating protein stability in cancer
  JOURNAL   Small GTPases 14 (1), 14-25 (2023)
   PUBMED   37194323
  REMARK    GeneRIF: ACKnowledging the role of the Activated-Cdc42 associated
            kinase (ACK) in regulating protein stability in cancer.
            Review article
REFERENCE   4  (residues 1 to 1032)
  AUTHORS   Zhou,A., Zhang,W. and Wang,B.
  TITLE     Host factor TNK2 is required for influenza virus infection
  JOURNAL   Genes Genomics 45 (6), 771-781 (2023)
   PUBMED   37133719
  REMARK    GeneRIF: Host factor TNK2 is required for influenza virus
            infection.
REFERENCE   5  (residues 1 to 1032)
  AUTHORS   Kan,Y., Paung,Y., Seeliger,M.A. and Miller,W.T.
  TITLE     Domain Architecture of the Nonreceptor Tyrosine Kinase Ack1
  JOURNAL   Cells 12 (6), 900 (2023)
   PUBMED   36980241
  REMARK    GeneRIF: Domain Architecture of the Nonreceptor Tyrosine Kinase
            Ack1.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1032)
  AUTHORS   Kato,J., Kaziro,Y. and Satoh,T.
  TITLE     Activation of the guanine nucleotide exchange factor Dbl following
            ACK1-dependent tyrosine phosphorylation
  JOURNAL   Biochem Biophys Res Commun 268 (1), 141-147 (2000)
   PUBMED   10652228
REFERENCE   7  (residues 1 to 1032)
  AUTHORS   Eisenmann,K.M., McCarthy,J.B., Simpson,M.A., Keely,P.J., Guan,J.L.,
            Tachibana,K., Lim,L., Manser,E., Furcht,L.T. and Iida,J.
  TITLE     Melanoma chondroitin sulphate proteoglycan regulates cell spreading
            through Cdc42, Ack-1 and p130cas
  JOURNAL   Nat Cell Biol 1 (8), 507-513 (1999)
   PUBMED   10587647
REFERENCE   8  (residues 1 to 1032)
  AUTHORS   Mott,H.R., Owen,D., Nietlispach,D., Lowe,P.N., Manser,E., Lim,L.
            and Laue,E.D.
  TITLE     Structure of the small G protein Cdc42 bound to the GTPase-binding
            domain of ACK
  JOURNAL   Nature 399 (6734), 384-388 (1999)
   PUBMED   10360579
REFERENCE   9  (residues 1 to 1032)
  AUTHORS   Satoh,T., Kato,J., Nishida,K. and Kaziro,Y.
  TITLE     Tyrosine phosphorylation of ACK in response to temperature
            shift-down, hyperosmotic shock, and epidermal growth factor
            stimulation
  JOURNAL   FEBS Lett 386 (2-3), 230-234 (1996)
   PUBMED   8647288
REFERENCE   10 (residues 1 to 1032)
  AUTHORS   Manser,E., Leung,T., Salihuddin,H., Tan,L. and Lim,L.
  TITLE     A non-receptor tyrosine kinase that inhibits the GTPase activity of
            p21cdc42
  JOURNAL   Nature 363 (6427), 364-367 (1993)
   PUBMED   8497321
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124944.8.
            
            Summary: This gene encodes a tyrosine kinase that binds Cdc42Hs in
            its GTP-bound form and inhibits both the intrinsic and
            GTPase-activating protein (GAP)-stimulated GTPase activity of
            Cdc42Hs. This binding is mediated by a unique sequence of 47 amino
            acids C-terminal to an SH3 domain. The protein may be involved in a
            regulatory mechanism that sustains the GTP-bound active form of
            Cdc42Hs and which is directly linked to a tyrosine phosphorylation
            signal transduction pathway. Several alternatively spliced
            transcript variants have been identified from this gene, but the
            full-length nature of only two transcript variants has been
            determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.759975.1,
                                           SRR14038195.2773273.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..1032
                     /product="activated CDC42 kinase 1 isoform 11"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="activated p21cdc42Hs kinase; activated
                     Cdc42-associated kinase 1; tyrosine kinase non-receptor
                     protein 2"
                     /calculated_mol_wt=113654
     Region          30..91
                     /region_name="SAM_TNK-like"
                     /note="SAM domain of TNK(ACK)-like non-receptor
                     tyrosine-protein kinases; cd09539"
                     /db_xref="CDD:188938"
     Region          154..411
                     /region_name="PTKc_Ack_like"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Activated Cdc42-associated kinase; cd05040"
                     /db_xref="CDD:270636"
     Site            order(156..158,164,180,182,229..232,236,276,280..281,283,
                     294,313..317,326,360)
                     /site_type="active"
                     /db_xref="CDD:270636"
     Site            order(156..158,164,180,182,229..232,236,276,280..281,283,
                     294)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270636"
     Site            order(276,280,313..317,326,360)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270636"
     Site            order(293..303,305..319)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270636"
     Region          419..468
                     /region_name="SH3_9"
                     /note="Variant SH3 domain; pfam14604"
                     /db_xref="CDD:434066"
     Site            order(421,423,428,446,448,463,465..466)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          473..538
                     /region_name="GTPase_binding"
                     /note="GTPase binding; pfam09027"
                     /db_xref="CDD:430374"
     Region          <567..873
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          798..864
                     /region_name="Inhibitor_Mig-6"
                     /note="EGFR receptor inhibitor Mig-6; pfam11555"
                     /db_xref="CDD:463294"
     Region          983..1022
                     /region_name="UBA_TNK1"
                     /note="UBA domain found in non-receptor tyrosine-protein
                     kinase TNK1 and similar proteins; cd14328"
                     /db_xref="CDD:270513"
     CDS             1..1032
                     /gene="TNK2"
                     /gene_synonym="ACK; ACK-1; ACK1; p21cdc42Hs"
                     /coded_by="NM_001387715.1:50..3148"
                     /note="isoform 11 is encoded by transcript variant 18"
                     /db_xref="GeneID:10188"
                     /db_xref="HGNC:HGNC:19297"
                     /db_xref="MIM:606994"
ORIGIN      
        1 mgersayqrl aggeegpqrl gggrmqpeeg tgwllellse vqlqqyflrl rddlnvtrls
       61 hfeyvknedl ekigmgrpgq rrlweavkrr kalckrkswm skvfsgkrle aefpphhsqs
      121 tfrktspapg gpagegplqs ltcligekdl rlleklgdgs fgvvrrgewd apsgktvsva
      181 vkclkpdvls qpeamddfir evnamhsldh rnlirlygvv ltppmkmvte laplgslldr
      241 lrkhqghfll gtlsryavqv aegmgylesk rfihrdlaar nlllatrdlv kigdfglmra
      301 lpqnddhyvm qehrkvpfaw capeslktrt fshasdtwmf gvtlwemfty gqepwiglng
      361 sqilhkidke gerlprpedc pqdiynvmvq cwahkpedrp tfvalrdfll eaqptdmral
      421 qdfeepdklh iqmndvitvi egraenywwr gqntrtlcvg pfprnvvtsv aglsaqdisq
      481 plqnsfihtg hgdsdprhcw gfpdridely lgnpmdppdl lsvelstsrp pqhlggvkkp
      541 tydpvsedqd plssdfkrlg lrkpglprgl wlakpsarvp gtkasrgsga evtlidfgee
      601 pvvpalrpca pslaqlamda cslldetppq sptralprpl hptpvvdwda rplppppayd
      661 dvaqdeddfe icsinstlvg agvpagpsqg qtnyafvpeq arppppledn lflppqgggk
      721 ppssaqtaei fqalqqecmr qlqapagspa pspspggddk pqvpprvpip prptrphvql
      781 spappgeeet sqwpgpaspp rvppreplsp qgsrtpsplv ppgssplppr lssspgktmp
      841 ttqsfasdpk yatpqviqap gpragpcilp ivrdgkkvss thyyllperp syleryqrfl
      901 reaqspeept plpvplllpp pstpapaapt atvrpmpqaa ldpkanfstn nsnpgarppp
      961 pratarlpqr gcpgdgpeag rpadkiqmve qlfglglrpr gechkvlemf dwnleqagch
     1021 llgswgpahh kr
//
LOCUS       NP_001018008             245 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform Tpm1.12br [Homo sapiens].
ACCESSION   NP_001018008
VERSION     NP_001018008.1
DBSOURCE    REFSEQ: accession NM_001018008.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 245)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 245)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 245)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC053545.1, BC050473.1 and
            AC079328.11.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Transcript Variant: This variant (Tpm1.12, also known as variant 6)
            contains alternate in-frame exons in the 5' and 3' coding region,
            compared to variant Tpm1.1. It encodes isoform Tpm1.12br, also
            known as the TMBr-3 brain isoform, which has distinct N- and
            C-termini and is shorter than isoform Tpm1.1st.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.177480.1,
                                           SRR1660805.118885.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..245
                     /product="tropomyosin alpha-1 chain isoform Tpm1.12br"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=28254
     Region          12..244
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..245
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001018008.2:88..825"
                     /note="isoform Tpm1.12br is encoded by transcript variant
                     Tpm1.12"
                     /db_xref="CCDS:CCDS32264.1"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 magsssleav rrkirslqeq adaaeeragt lqreldherk lretaeadva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkviesraqk deekmeiqei qlkeakhiae
      121 dadrkyeeva rklviiesdl eraeeraels egkcaeleee lktvtnnlks leaqaekysq
      181 kedryeeeik vlsdklkeae traefaersv tkleksiddl edqlyqqleq nrrltnelkl
      241 alned
//
LOCUS       NP_001353471             499 aa            linear   PRI 21-NOV-2025
DEFINITION  inositol 1,4,5-triphosphate receptor associated 2 isoform a [Homo
            sapiens].
ACCESSION   NP_001353471 XP_016874789
VERSION     NP_001353471.1
DBSOURCE    REFSEQ: accession NM_001366542.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Okumura,W., Tadahira,K., Kozono,T., Tamura-Nakano,M., Sato,H.,
            Matsui,H., Dohi,T., Rohrer,J., Tonozuka,T. and Nishikawa,A.
  TITLE     Jaw1/LRMP is associated with the maintenance of Golgi ribbon
            structure
  JOURNAL   J Biochem 173 (5), 383-392 (2023)
   PUBMED   36689741
  REMARK    GeneRIF: Jaw1/LRMP is associated with the maintenance of Golgi
            ribbon structure.
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Okumura,W., Kozono,T., Sato,H., Matsui,H., Takagi,T., Tonozuka,T.
            and Nishikawa,A.
  TITLE     Jaw1/LRMP increases Ca2+ influx upon GPCR stimulation with
            heterogeneous effect on the activity of each ITPR subtype
  JOURNAL   Sci Rep 12 (1), 9476 (2022)
   PUBMED   35676525
  REMARK    GeneRIF: Jaw1/LRMP increases Ca(2+) influx upon GPCR stimulation
            with heterogeneous effect on the activity of each ITPR subtype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Cruz,V.E., Esra Demircioglu,F. and Schwartz,T.U.
  TITLE     Structural Analysis of Different LINC Complexes Reveals Distinct
            Binding Modes
  JOURNAL   J Mol Biol 432 (23), 6028-6041 (2020)
   PUBMED   33058875
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Bataille,P., Michaud,V., Robert,M.P., Bekel,L., Leclerc-Mercier,S.,
            Harroche,A., Celerier,C., Lasseaux,E., Borgel,D.,
            Bremond-Gignac,D., Bodemer,C., Arveiler,B. and Hadj-Rabia,S.
  TITLE     Clinical variability and probable founder effect in oculocutaneous
            albinism type 7
  JOURNAL   Clin Genet 97 (3), 527-528 (2020)
   PUBMED   31694064
  REMARK    GeneRIF: Clinical variability and probable founder effect in
            oculocutaneous albinism type 7.
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Kohno,T., Kunitoh,H., Suzuki,K., Yamamoto,S., Kuchiba,A.,
            Matsuno,Y., Yanagitani,N. and Yokota,J.
  TITLE     Association of KRAS polymorphisms with risk for lung adenocarcinoma
            accompanied by atypical adenomatous hyperplasias
  JOURNAL   Carcinogenesis 29 (5), 957-963 (2008)
   PUBMED   18299280
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Manenti,G., Galbiati,F., Pettinicchio,A., Spinola,M., Piconese,S.,
            Leoni,V.P., Conti,B., Ravagnani,F., Incarbone,M., Pastorino,U. and
            Dragani,T.A.
  TITLE     A V141L polymorphism of the human LRMP gene is associated with
            survival of lung cancer patients
  JOURNAL   Carcinogenesis 27 (7), 1386-1390 (2006)
   PUBMED   16410263
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Snyder,H.L., Bacik,I., Bennink,J.R., Kearns,G., Behrens,T.W.,
            Bachi,T., Orlowski,M. and Yewdell,J.W.
  TITLE     Two novel routes of transporter associated with antigen processing
            (TAP)-independent major histocompatibility complex class I antigen
            processing
  JOURNAL   J Exp Med 186 (7), 1087-1098 (1997)
   PUBMED   9314557
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Behrens,T.W., Kearns,G.M., Rivard,J.J., Bernstein,H.D.,
            Yewdell,J.W. and Staudt,L.M.
  TITLE     Carboxyl-terminal targeting and novel post-translational processing
            of JAW1, a lymphoid protein of the endoplasmic reticulum
  JOURNAL   J Biol Chem 271 (38), 23528-23534 (1996)
   PUBMED   8798562
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Behrens,T.W., Jagadeesh,J., Scherle,P., Kearns,G., Yewdell,J. and
            Staudt,L.M.
  TITLE     Jaw1, A lymphoid-restricted membrane protein localized to the
            endoplasmic reticulum
  JOURNAL   J Immunol 153 (2), 682-690 (1994)
   PUBMED   8021504
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC023510.16.
            
            On Oct 11, 2018 this sequence version replaced XP_016874789.1.
            
            Summary: The protein encode dby this gene is expressed in a
            developmentally regulated manner in lymphoid cell lines and
            tissues. The protein is localized to the cytoplasmic face of the
            endoplasmic reticulum. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3317885.1,
                                           SRR14038196.1718355.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..499
                     /product="inositol 1,4,5-triphosphate receptor associated
                     2 isoform a"
                     /note="protein Jaw1; lymphoid restricted membrane protein"
                     /calculated_mol_wt=56082
     Region          4..499
                     /region_name="MRVI1"
                     /note="MRVI1 protein; pfam05781"
                     /db_xref="CDD:461738"
     CDS             1..499
                     /gene="IRAG2"
                     /gene_synonym="JAW1; LRMP"
                     /coded_by="NM_001366542.2:633..2132"
                     /note="isoform a is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS8701.1"
                     /db_xref="GeneID:4033"
                     /db_xref="HGNC:HGNC:6690"
                     /db_xref="MIM:602003"
ORIGIN      
        1 mnddpsmeen gvervcpesl lqsreysslp lprhtsstdg titssdpgle ilnmascdld
       61 rnslckkeed trsasptiea qgtspahdni afqdstskdk tilnleakee petieehkke
      121 hasgdsvvsp lpvttvksvn lrqsentsan ekeveaeflr lslgfkcdwf tlekrvklee
      181 rsrdlaeenl kkeitnclkl lesltplced dnqaqeiikk leksikflsq caarvasrae
      241 mlgainqesr vskavevmiq hvenlkrmya kehaeleelk qvllqnersf npleddddcq
      301 ikkrsaslns kpsslrrvti aslprnigna gmvagmennd rfsrrssswr ilgskqsehr
      361 pslprfisty swadaeeekc elktkddsep sgeetvertr kpslsekknn pskwdvssvy
      421 dtiaswatnl kssirkanka lwlsiafivl faalmsfltg qlfqksvdaa ptqqedswts
      481 lehilwpftr lrhngpppv
//
LOCUS       NP_001018062             175 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase III subunit RPC8 isoform b [Homo
            sapiens].
ACCESSION   NP_001018062
VERSION     NP_001018062.1
DBSOURCE    REFSEQ: accession NM_001018052.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Ramsay,E.P., Abascal-Palacios,G., Daiss,J.L., King,H., Gouge,J.,
            Pilsl,M., Beuron,F., Morris,E., Gunkel,P., Engel,C. and Vannini,A.
  TITLE     Structure of human RNA polymerase III
  JOURNAL   Nat Commun 11 (1), 6409 (2020)
   PUBMED   33335104
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Franca,M.M., Han,X., Funari,M.F.A., Lerario,A.M., Nishi,M.Y.,
            Fontenele,E.G.P., Domenice,S., Jorge,A.A.L., Garcia-Galiano,D.,
            Elias,C.F. and Mendonca,B.B.
  TITLE     Exome Sequencing Reveals the POLR3H Gene as a Novel Cause of
            Primary Ovarian Insufficiency
  JOURNAL   J Clin Endocrinol Metab 104 (7), 2827-2841 (2019)
   PUBMED   30830215
  REMARK    GeneRIF: A pathogenic homozygous missense mutation (c.149A>G;
            p.Asp50Gly) in the POLR3H gene in two unrelated families with
            primary ovarian insufficiency was identified.
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Owen,T.J., O'Neil,J.D., Dawson,C.W., Hu,C., Chen,X., Yao,Y.,
            Wood,V.H., Mitchell,L.E., White,R.J., Young,L.S. and Arrand,J.R.
  TITLE     Epstein-Barr virus-encoded EBNA1 enhances RNA polymerase
            III-dependent EBER expression through induction of EBER-associated
            cellular transcription factors
  JOURNAL   Mol Cancer 9, 241 (2010)
   PUBMED   20843307
  REMARK    GeneRIF: Findings reveal that RNA polymerase III-dependent EBER
            expression through induction of cellular transcription factors and
            add to the repertoire of EBNA1's transcription-regulatory
            properties.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Greco-Stewart,V.S., Schissel,E. and Pelchat,M.
  TITLE     The hepatitis delta virus RNA genome interacts with the human RNA
            polymerases I and III
  JOURNAL   Virology 386 (1), 12-15 (2009)
   PUBMED   19246067
  REMARK    GeneRIF: The authors demonstrate the interaction of both RNA
            polymerase I and III with hepatitis delta virus RNA, both in vitro
            and in human cells.
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Hu,P., Wu,S., Sun,Y., Yuan,C.C., Kobayashi,R., Myers,M.P. and
            Hernandez,N.
  TITLE     Characterization of human RNA polymerase III identifies orthologues
            for Saccharomyces cerevisiae RNA polymerase III subunits
  JOURNAL   Mol Cell Biol 22 (22), 8044-8055 (2002)
   PUBMED   12391170
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA449644.1, DA238361.1, BC017248.2, AB051452.1, AK000365.1,
            AL023553.5 and BM701572.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            lacks an alternate in-frame exon, compared to variant 1. The
            encoded isoform (b) is shorter than isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853561.20040.1,
                                           SRR14038192.2517240.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..175
                     /product="DNA-directed RNA polymerase III subunit RPC8
                     isoform b"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerase III subunit RPC8;
                     polymerase (RNA) III subunit H; RNA nucleotidyltransferase
                     (DNA-directed); RNA polymerase III subunit C8;
                     DNA-directed RNA polymerase III subunit H; DNA-directed
                     RNA polymerase III subunit 22.9 kDa polypeptide;
                     polymerase (RNA) III (DNA directed) polypeptide H
                     (22.9kD)"
                     /calculated_mol_wt=19527
     Region          2..70
                     /region_name="RNAP_III_Rpc25_N"
                     /note="Rpc25, N-terminal ribonucleoprotein (RNP) domain.
                     Rpc25 is a subunit of eukaryotic RNA polymerase (RNAP) III
                     and is homologous to Rpa43 of eukaryotic RNAP I, Rpb7 of
                     eukaryotic RNAP II, and RpoE of archaeal RNAP. Rpc25 has
                     two domains, an N-terminal RNP...; cd04330"
                     /db_xref="CDD:239822"
     Site            order(2..6,8,28,31..32,46..49)
                     /site_type="other"
                     /note="Rpc17 interaction site [polypeptide binding]"
                     /db_xref="CDD:239822"
     Region          69..172
                     /region_name="RNA_pol_Rbc25"
                     /note="RNA polymerase III subunit Rpc25; pfam08292"
                     /db_xref="CDD:400543"
     CDS             1..175
                     /gene="POLR3H"
                     /gene_synonym="C25; RPC22.9; RPC8"
                     /coded_by="NM_001018052.4:370..897"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS33651.1"
                     /db_xref="GeneID:171568"
                     /db_xref="HGNC:HGNC:30349"
                     /db_xref="MIM:619801"
ORIGIN      
        1 mfvlvemvdt vrippwqfer klndsiaeel nkklankvvy nvglciclfd itkledayvf
       61 pgdgashtkv slgffddili ppeslqqpak fdeaeqvwvw eyeteegahd lymdtgeeir
      121 frvvdesfvd tsptgpssad attsseelpk keapytlvgs isepglglls wwtsn
//
LOCUS       NP_001092103             256 aa            linear   PRI 21-NOV-2025
DEFINITION  proline-rich AKT1 substrate 1 isoform b [Homo sapiens].
ACCESSION   NP_001092103
VERSION     NP_001092103.1
DBSOURCE    REFSEQ: accession NM_001098633.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Zhang,T., Wang,Y., Yu,H., Zhang,T., Guo,L., Xu,J., Wei,X., Wang,N.,
            Wu,Y., Wang,X. and Huang,L.
  TITLE     PGK1 represses autophagy-mediated cell death to promote the
            proliferation of liver cancer cells by phosphorylating PRAS40
  JOURNAL   Cell Death Dis 13 (1), 68 (2022)
   PUBMED   35058442
  REMARK    GeneRIF: PGK1 represses autophagy-mediated cell death to promote
            the proliferation of liver cancer cells by phosphorylating PRAS40.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Challa,S., Khulpateea,B.R., Nandu,T., Camacho,C.V., Ryu,K.W.,
            Chen,H., Peng,Y., Lea,J.S. and Kraus,W.L.
  TITLE     Ribosome ADP-ribosylation inhibits translation and maintains
            proteostasis in cancers
  JOURNAL   Cell 184 (17), 4531-4546 (2021)
   PUBMED   34314702
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Saito,A., Narasimhan,P., Hayashi,T., Okuno,S., Ferrand-Drake,M. and
            Chan,P.H.
  TITLE     Neuroprotective role of a proline-rich Akt substrate in apoptotic
            neuronal cell death after stroke: relationships with nerve growth
            factor
  JOURNAL   J Neurosci 24 (7), 1584-1593 (2004)
   PUBMED   14973226
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Kovacina,K.S., Park,G.Y., Bae,S.S., Guzzetta,A.W., Schaefer,E.,
            Birnbaum,M.J. and Roth,R.A.
  TITLE     Identification of a proline-rich Akt substrate as a 14-3-3 binding
            partner
  JOURNAL   J Biol Chem 278 (12), 10189-10194 (2003)
   PUBMED   12524439
REFERENCE   8  (residues 1 to 256)
  AUTHORS   Park,I.H., Bachmann,R., Shirazi,H. and Chen,J.
  TITLE     Regulation of ribosomal S6 kinase 2 by mammalian target of
            rapamycin
  JOURNAL   J Biol Chem 277 (35), 31423-31429 (2002)
   PUBMED   12087098
REFERENCE   9  (residues 1 to 256)
  AUTHORS   Vladimirov,S.N., Ivanov,A.V., Karpova,G.G., Musolyamov,A.K.,
            Egorov,T.A., Thiede,B., Wittmann-Liebold,B. and Otto,A.
  TITLE     Characterization of the human small-ribosomal-subunit proteins by
            N-terminal and internal sequencing, and mass spectrometry
  JOURNAL   Eur J Biochem 239 (1), 144-149 (1996)
   PUBMED   8706699
REFERENCE   10 (residues 1 to 256)
  AUTHORS   Grove,J.R., Banerjee,P., Balasubramanyam,A., Coffer,P.J.,
            Price,D.J., Avruch,J. and Woodgett,J.R.
  TITLE     Cloning and expression of two human p70 S6 kinase polypeptides
            differing only at their amino termini
  JOURNAL   Mol Cell Biol 11 (11), 5541-5550 (1991)
   PUBMED   1922062
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA848626.1 and BC051844.2.
            
            Summary: AKT1S1 is a proline-rich substrate of AKT (MIM 164730)
            that binds 14-3-3 protein (see YWHAH, MIM 113508) when
            phosphorylated (Kovacina et al., 2003 [PubMed 12524439]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (b) is
            shorter at the N-terminus compared to isoform a. Variants 2, 3, 4,
            and 5 encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2466897.1,
                                           SRR11853565.15684.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000344175.10/ ENSP00000341698.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..256
                     /product="proline-rich AKT1 substrate 1 isoform b"
                     /note="40 kDa proline-rich AKT substrate; AKT1 substrate 1
                     (proline rich)"
                     /calculated_mol_wt=27252
     Site            51
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Region          69..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D1F4; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Region          127..251
                     /region_name="PRAS"
                     /note="Proline-rich AKT1 substrate 1; pfam15798"
                     /db_xref="CDD:406279"
     Region          129..133
                     /region_name="TOS motif.
                     /evidence=ECO:0000269|PubMed:17510057"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000269|PubMed:17517883,
                     ECO:0000269|PubMed:18372248, ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Region          197..216
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000269|PubMed:18372248,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000269|PubMed:18372248; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Region          237..256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1 and DYRK3.
                     /evidence=ECO:0000269|PubMed:12524439,
                     ECO:0000269|PubMed:23415227, ECO:0000269|PubMed:29634919,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     CDS             1..256
                     /gene="AKT1S1"
                     /gene_synonym="Lobe; PRAS40"
                     /coded_by="NM_001098633.4:127..897"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS12784.1"
                     /db_xref="GeneID:84335"
                     /db_xref="HGNC:HGNC:28426"
                     /db_xref="MIM:610221"
ORIGIN      
        1 masgrpeelw eavvgaaerf rartgtelvl ltaapppppr pgpcayaahg rgalaeaarr
       61 clhdialahr aataarppap ppapqppspt pspprptlar edneededep tetetsgeql
      121 gisdngglfv mdedatlqdl ppfcesdpes tddgslseet pagpptcsvp pasalptqqy
      181 akslpvsvpv wgfkekrtea rssdeengpp sspdldriaa smralvlrea edtqvfgdlp
      241 rprlntsdfq klkrky
//
LOCUS       NP_000336                140 aa            linear   PRI 21-NOV-2025
DEFINITION  alpha-synuclein isoform NACP140 [Homo sapiens].
ACCESSION   NP_000336
VERSION     NP_000336.1
DBSOURCE    REFSEQ: accession NM_000345.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Aggarwal,L., Karmakar,S. and Biswas,P.
  TITLE     Differentially heterogeneous hydration environment of the familial
            mutants of alpha-synuclein
  JOURNAL   J Chem Phys 161 (15) (2024)
   PUBMED   39412059
  REMARK    GeneRIF: Differentially heterogeneous hydration environment of the
            familial mutants of alpha-synuclein.
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Kametani,F., Tahira,M., Takao,M., Matsubara,T., Hasegawa,K.,
            Yoshida,M., Saito,Y., Murayama,S. and Hasegawa,M.
  TITLE     Analysis and comparison of post-translational modifications of
            alpha-synuclein filaments in multiple system atrophy and dementia
            with Lewy bodies
  JOURNAL   Sci Rep 14 (1), 22892 (2024)
   PUBMED   39358446
  REMARK    GeneRIF: Analysis and comparison of post-translational
            modifications of alpha-synuclein filaments in multiple system
            atrophy and dementia with Lewy bodies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Xia,P., Cao,Y., Zhao,Q. and Li,H.
  TITLE     Energy gap of conformational transition related with temperature
            for the NACore of alpha-synuclein
  JOURNAL   Phys Chem Chem Phys 26 (35), 23062-23072 (2024)
   PUBMED   39175373
  REMARK    GeneRIF: Energy gap of conformational transition related with
            temperature for the NACore of alpha-synuclein.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Tripathi,A., Alnakhala,H., Brontesi,L., Selkoe,D. and Dettmer,U.
  TITLE     RXR nuclear receptor signaling modulates lipid metabolism and
            triggers lysosomal clearance of alpha-synuclein in neuronal models
            of synucleinopathy
  JOURNAL   Cell Mol Life Sci 81 (1), 362 (2024)
   PUBMED   39162859
  REMARK    GeneRIF: RXR nuclear receptor signaling modulates lipid metabolism
            and triggers lysosomal clearance of alpha-synuclein in neuronal
            models of synucleinopathy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Martins,G.F. and Galamba,N.
  TITLE     Wild-Type alpha-Synuclein Structure and Aggregation: A
            Comprehensive Coarse-Grained and All-Atom Molecular Dynamics Study
  JOURNAL   J Chem Inf Model 64 (15), 6115-6131 (2024)
   PUBMED   39046235
  REMARK    GeneRIF: Wild-Type alpha-Synuclein Structure and Aggregation: A
            Comprehensive Coarse-Grained and All-Atom Molecular Dynamics Study.
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Spillantini,M.G., Divane,A. and Goedert,M.
  TITLE     Assignment of human alpha-synuclein (SNCA) and beta-synuclein
            (SNCB) genes to chromosomes 4q21 and 5q35
  JOURNAL   Genomics 27 (2), 379-381 (1995)
   PUBMED   7558013
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Chen,X., de Silva,H.A., Pettenati,M.J., Rao,P.N., St
            George-Hyslop,P., Roses,A.D., Xia,Y., Horsburgh,K., Ueda,K. and
            Saitoh,T.
  TITLE     The human NACP/alpha-synuclein gene: chromosome assignment to
            4q21.3-q22 and TaqI RFLP analysis
  JOURNAL   Genomics 26 (2), 425-427 (1995)
   PUBMED   7601479
REFERENCE   8  (residues 1 to 140)
  AUTHORS   Campion,D., Martin,C., Heilig,R., Charbonnier,F., Moreau,V.,
            Flaman,J.M., Petit,J.L., Hannequin,D., Brice,A. and Frebourg,T.
  TITLE     The NACP/synuclein gene: chromosomal assignment and screening for
            alterations in Alzheimer disease
  JOURNAL   Genomics 26 (2), 254-257 (1995)
   PUBMED   7601450
REFERENCE   9  (residues 1 to 140)
  AUTHORS   Ueda,K., Saitoh,T. and Mori,H.
  TITLE     Tissue-dependent alternative splicing of mRNA for NACP, the
            precursor of non-A beta component of Alzheimer's disease amyloid
  JOURNAL   Biochem Biophys Res Commun 205 (2), 1366-1372 (1994)
   PUBMED   7802671
REFERENCE   10 (residues 1 to 140)
  AUTHORS   Morris,H. and Lim,S.Y.
  TITLE     Monogenic Parkinson Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301402
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AI815523.1, BC108275.1 and
            AC097478.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Alpha-synuclein is a member of the synuclein family, which
            also includes beta- and gamma-synuclein. Synucleins are abundantly
            expressed in the brain and alpha- and beta-synuclein inhibit
            phospholipase D2 selectively. SNCA may serve to integrate
            presynaptic signaling and membrane trafficking. Defects in SNCA
            have been implicated in the pathogenesis of Parkinson disease. SNCA
            peptides are a major component of amyloid plaques in the brains of
            patients with Alzheimer's disease. Alternatively spliced
            transcripts encoding different isoforms have been identified for
            this gene. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1, also known as NACP140) is the
            longest transcript and encodes the longer isoform (NACP140).
            Variants 1, 2, and 3 all encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.57584.1,
                                           SRR1803612.110177.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394991.8/ ENSP00000378442.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q22.1"
     Protein         1..140
                     /product="alpha-synuclein isoform NACP140"
                     /note="non A-beta component of AD amyloid; synuclein
                     alpha-140; synuclein, alpha (non A4 component of amyloid
                     precursor); I+/--synuclein"
                     /calculated_mol_wt=14329
     Region          1..131
                     /region_name="Synuclein"
                     /note="pfam01387"
                     /db_xref="CDD:460186"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:22407793; propagated from
                     UniProtKB/Swiss-Prot (P37840.1)"
     Region          20..67
                     /region_name="4 X 11 AA tandem repeats of
                     [EGS]-K-T-K-[EQ]-[GQ]-V-X(4)"
                     /note="propagated from UniProtKB/Swiss-Prot (P37840.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10617630; propagated from
                     UniProtKB/Swiss-Prot (P37840.1)"
     Region          100..140
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P37840.1)"
     Region          111..140
                     /region_name="Interaction with SERF1A.
                     /evidence=ECO:0000269|PubMed:22854022"
                     /note="propagated from UniProtKB/Swiss-Prot (P37840.1)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by FYN.
                     /evidence=ECO:0000269|PubMed:11162638,
                     ECO:0000269|PubMed:12893833; propagated from
                     UniProtKB/Swiss-Prot (P37840.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by BARK1, PLK2, CK2, CK1 and GRK5.
                     /evidence=ECO:0000269|PubMed:10617630,
                     ECO:0000269|PubMed:11813001, ECO:0000269|PubMed:24936070;
                     propagated from UniProtKB/Swiss-Prot (P37840.1)"
     CDS             1..140
                     /gene="SNCA"
                     /gene_synonym="NACP; PARK1; PARK4; PD1"
                     /coded_by="NM_000345.4:226..648"
                     /note="isoform NACP140 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3634.1"
                     /db_xref="GeneID:6622"
                     /db_xref="HGNC:HGNC:11138"
                     /db_xref="MIM:163890"
ORIGIN      
        1 mdvfmkglsk akegvvaaae ktkqgvaeaa gktkegvlyv gsktkegvvh gvatvaektk
       61 eqvtnvggav vtgvtavaqk tvegagsiaa atgfvkkdql gkneegapqe giledmpvdp
      121 dneayempse egyqdyepea
//
LOCUS       NP_001350466             282 aa            linear   PRI 21-NOV-2025
DEFINITION  cyclin-C isoform c [Homo sapiens].
ACCESSION   NP_001350466 XP_006715657
VERSION     NP_001350466.1
DBSOURCE    REFSEQ: accession NM_001363537.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Lloyd,R.L., Urban,V., Munoz-Martinez,F., Ayestaran,I., Thomas,J.C.,
            de Renty,C., O'Connor,M.J., Forment,J.V., Galanty,Y. and
            Jackson,S.P.
  TITLE     Loss of Cyclin C or CDK8 provides ATR inhibitor resistance by
            suppressing transcription-associated replication stress
  JOURNAL   Nucleic Acids Res 49 (15), 8665-8683 (2021)
   PUBMED   34329458
  REMARK    GeneRIF: Loss of Cyclin C or CDK8 provides ATR inhibitor resistance
            by suppressing transcription-associated replication stress.
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Tang,M., Pei,G., Su,D., Wang,C., Feng,X., Srivastava,M., Chen,Z.,
            Zhao,Z. and Chen,J.
  TITLE     Genome-wide CRISPR screens reveal cyclin C as synthetic survival
            target of BRCA2
  JOURNAL   Nucleic Acids Res 49 (13), 7476-7491 (2021)
   PUBMED   34197614
  REMARK    GeneRIF: Genome-wide CRISPR screens reveal cyclin C as synthetic
            survival target of BRCA2.
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Tassan,J.P., Jaquenoud,M., Leopold,P., Schultz,S.J. and Nigg,E.A.
  TITLE     Identification of human cyclin-dependent kinase 8, a putative
            protein kinase partner for cyclin C
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8871-8875 (1995)
   PUBMED   7568034
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Yoshizumi,M., Lee,W.S., Hsieh,C.M., Tsai,J.C., Li,J.,
            Perrella,M.A., Patterson,C., Endege,W.O., Schlegel,R. and Lee,M.E.
  TITLE     Disappearance of cyclin A correlates with permanent withdrawal of
            cardiomyocytes from the cell cycle in human and rat hearts
  JOURNAL   J Clin Invest 95 (5), 2275-2280 (1995)
   PUBMED   7738192
REFERENCE   8  (residues 1 to 282)
  AUTHORS   Demetrick,D.J., Matsumoto,S., Hannon,G.J., Okamoto,K., Xiong,Y.,
            Zhang,H. and Beach,D.H.
  TITLE     Chromosomal mapping of the genes for the human cell cycle proteins
            cyclin C (CCNC), cyclin E (CCNE), p21 (CDKN1) and KAP (CDKN3)
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 190-192 (1995)
   PUBMED   7698009
REFERENCE   9  (residues 1 to 282)
  AUTHORS   Lew,D.J., Dulic,V. and Reed,S.I.
  TITLE     Isolation of three novel human cyclins by rescue of G1 cyclin (Cln)
            function in yeast
  JOURNAL   Cell 66 (6), 1197-1206 (1991)
   PUBMED   1833066
REFERENCE   10 (residues 1 to 282)
  AUTHORS   Nozawa,T., Hatano,M., Yamamoto,H. and Kwan,T.
  TITLE     Magnetic circular dichroism on the reversible oxygenation of
            dimethylmesoporphyrin-IX-atopyridinecobalt (II)
  JOURNAL   Bioinorg Chem 5 (3), 267-273 (1976)
   PUBMED   1260071
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL137784.14.
            
            On May 24, 2018 this sequence version replaced XP_006715657.1.
            
            Summary: The protein encoded by this gene is a member of the cyclin
            family of proteins. The encoded protein interacts with
            cyclin-dependent kinase 8 and induces the phophorylation of the
            carboxy-terminal domain of the large subunit of RNA polymerase II.
            The level of mRNAs for this gene peaks in the G1 phase of the cell
            cycle. Two transcript variants encoding different isoforms have
            been found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) differs in the 3' UTR and
            coding sequence compared to variant 1. The resulting isoform (c)
            has a shorter and distinct C-terminus compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1183910.1,
                                           SRR11853565.25219.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q16.2"
     Protein         1..282
                     /product="cyclin-C isoform c"
                     /note="SRB11 homolog"
                     /calculated_mol_wt=33009
     Region          40..146
                     /region_name="CYCLIN_CCNC_rpt1"
                     /note="first cyclin box found in cyclin-C (CCNC) and
                     similar proteins; cd20513"
                     /db_xref="CDD:410217"
     Site            order(93,96..99,136..137,139..141,143..145)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410217"
     Region          154..245
                     /region_name="CYCLIN_CCNC_rpt2"
                     /note="second cyclin box found in cyclin-C (CCNC) and
                     similar proteins; cd20514"
                     /db_xref="CDD:410218"
     CDS             1..282
                     /gene="CCNC"
                     /gene_synonym="CycC; hSRB11; SRB11"
                     /coded_by="NM_001363537.2:134..982"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS87420.1"
                     /db_xref="GeneID:892"
                     /db_xref="HGNC:HGNC:1581"
                     /db_xref="MIM:123838"
ORIGIN      
        1 magnfwqssh ylqwildkqd llkerqkdlk flseeeywkl qifftnviqa lgehlklrqq
       61 viatatvyfk rfyaryslks idpvlmaptc vflaskveef gvvsntrlia aatsvlktrf
      121 syafpkefpy rmnhilecef yllelmdccl ivyhpyrpll qyvqdmgqed mllplawriv
      181 ndtyrtdlcl lyppfmiala clhvacvvqq kdarqwfael svdmekilei irvilklyeq
      241 wknfderkem atilskmpkp kpppnrnsls dsplvagpea ar
//
LOCUS       NP_001123532             462 aa            linear   PRI 21-NOV-2025
DEFINITION  cyclic AMP-dependent transcription factor ATF-7 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001123532
VERSION     NP_001123532.1
DBSOURCE    REFSEQ: accession NM_001130060.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Zhang,J., Liu,D., Deng,G., Wang,Q., Li,L., Zhang,J. and Wu,H.
  TITLE     lncRNA prostate cancer-associated transcript 18 upregulates
            activating transcription factor 7 to prevent metastasis of
            triple-negative breast cancer via sponging miR-103a-3p
  JOURNAL   Bioengineered 12 (2), 12070-12086 (2021)
   PUBMED   34787047
  REMARK    GeneRIF: lncRNA prostate cancer-associated transcript 18
            upregulates activating transcription factor 7 to prevent metastasis
            of triple-negative breast cancer via sponging miR-103a-3p.
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Newman,S.P., Bates,N.P., Vernimmen,D., Parker,M.G. and Hurst,H.C.
  TITLE     Cofactor competition between the ligand-bound oestrogen receptor
            and an intron 1 enhancer leads to oestrogen repression of ERBB2
            expression in breast cancer
  JOURNAL   Oncogene 19 (4), 490-497 (2000)
   PUBMED   10698518
REFERENCE   6  (residues 1 to 462)
  AUTHORS   De Graeve,F., Bahr,A., Sabapathy,K.T., Hauss,C., Wagner,E.F.,
            Kedinger,C. and Chatton,B.
  TITLE     Role of the ATFa/JNK2 complex in Jun activation
  JOURNAL   Oncogene 18 (23), 3491-3500 (1999)
   PUBMED   10376527
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Goetz,J., Chatton,B., Mattei,M.G. and Kedinger,C.
  TITLE     Structure and expression of the ATFa gene
  JOURNAL   J Biol Chem 271 (47), 29589-29598 (1996)
   PUBMED   8939888
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Bocco,J.L., Bahr,A., Goetz,J., Hauss,C., Kallunki,T., Kedinger,C.
            and Chatton,B.
  TITLE     In vivo association of ATFa with JNK/SAP kinase activities
  JOURNAL   Oncogene 12 (9), 1971-1980 (1996)
   PUBMED   8649858
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Pescini,R., Kaszubska,W., Whelan,J., DeLamarter,J.F. and Hooft van
            Huijsduijnen,R.
  TITLE     ATF-a0, a novel variant of the ATF/CREB transcription factor
            family, forms a dominant transcription inhibitor in ATF-a
            heterodimers
  JOURNAL   J Biol Chem 269 (2), 1159-1165 (1994)
   PUBMED   8288576
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Gaire,M., Chatton,B. and Kedinger,C.
  TITLE     Isolation and characterization of two novel, closely related ATF
            cDNA clones from HeLa cells
  JOURNAL   Nucleic Acids Res 18 (12), 3467-3473 (1990)
   PUBMED   1694576
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB047160.1, X52943.1, BP312300.1, BP279417.1, AC023509.42 and
            BQ184780.1.
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice site in an internal exon, compared to variant 2, resulting
            in a shorter isoform (3, also known as ATFa1 or ATF-a delta),
            compared to isoform 2. There are no publicly available transcripts
            representing this variant; it is supported by data in PMIDs 1694576
            and 8939888, and by alternative splicing annotation on accessions
            X52943.1 and X57197.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4480190.1,
                                           SRR18074967.344647.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..462
                     /product="cyclic AMP-dependent transcription factor ATF-7
                     isoform 3"
                     /note="cyclic AMP-dependent transcription factor ATF-7;
                     transcription factor ATF-A"
                     /calculated_mol_wt=49519
     Region          9..31
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          47..84
                     /region_name="GCN4_cent"
                     /note="GCN4 central activation domain-like acidic
                     activation domain; cd12192"
                     /db_xref="CDD:213399"
     Site            order(58..59,61..62,70..71,73..75,77..78,82..84)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:213399"
     Region          313..373
                     /region_name="bZIP_ATF2"
                     /note="Basic leucine zipper (bZIP) domain of Activating
                     Transcription Factor-2 (ATF-2) and similar proteins: a
                     DNA-binding and dimerization domain; cd14687"
                     /db_xref="CDD:269835"
     Region          313..373
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269835"
     Site            order(314,318,320..322,325,327..329,331..333)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269835"
     Site            order(332,339..340,342..343,346..347,350,353..354,357,
                     360..361,363..364,367..368,371..372)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269835"
     CDS             1..462
                     /gene="ATF7"
                     /gene_synonym="ATFA"
                     /coded_by="NM_001130060.2:126..1514"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:11016"
                     /db_xref="HGNC:HGNC:792"
                     /db_xref="MIM:606371"
ORIGIN      
        1 mgddrpfvcn apgcgqrftn edhlavhkhk hemtlkfgpa rtdsviiadq tptptrflkn
       61 ceevglfnel assfehefkk aadedekkaa agpldmslps tpdikikeee pveevtpkpv
      121 listptptiv rpgslplhlg ydplhptlps ptsvitqapp snrqmgsptg slplvmhlan
      181 gqtmpvlpgp pvqmpsvisl arpvsmvpni pgipgppvns sgsispsghp ipseakmrlk
      241 atlthqvssi nggcgmvvgt astmvtarpe qsqiliqhpd apspaqpqvs paqptpstgg
      301 rrrrtvdedp derrqrfler nraaasrcrq krklwvssle kkaeeltsqn iqlsnevtll
      361 rnevaqlkql llahkdcpvt alqkktqgyl espkessept gspapviqhs satapsngls
      421 vrsaaeavat svltqmasqr telsmpiqsh vimtpqsqsa gr
//
LOCUS       NP_001387148            1082 aa            linear   PRI 21-NOV-2025
DEFINITION  protein transport protein Sec31A isoform 29 [Homo sapiens].
ACCESSION   NP_001387148
VERSION     NP_001387148.1
DBSOURCE    REFSEQ: accession NM_001400219.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1082)
  AUTHORS   Tobias,E.S., Lucas-Herald,A.K., Sagar,D., Montezano,A.C.,
            Rios,F.J., De Lucca Camargo,L., Hamilton,G., Gazdagh,G.,
            Diver,L.A., Williams,N., Herzyk,P., Touyz,R.M., Greenfield,A.,
            McGowan,R. and Ahmed,S.F.
  TITLE     SEC31A may be associated with pituitary hormone deficiency and
            gonadal dysgenesis
  JOURNAL   Endocrine 84 (2), 345-349 (2024)
   PUBMED   38400880
  REMARK    GeneRIF: SEC31A may be associated with pituitary hormone deficiency
            and gonadal dysgenesis.
REFERENCE   2  (residues 1 to 1082)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1082)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1082)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1082)
  AUTHORS   Jin,L., Pahuja,K.B., Wickliffe,K.E., Gorur,A., Baumgartel,C.,
            Schekman,R. and Rape,M.
  TITLE     Ubiquitin-dependent regulation of COPII coat size and function
  JOURNAL   Nature 482 (7386), 495-500 (2012)
   PUBMED   22358839
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1082)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1082)
  AUTHORS   Kim,J.H., Hong,J.A., Pih,K.T. and Hwang,I.
  TITLE     Identification and isolation of differentially expressed genes in
            osmotically stressed human oral keratinocytes
  JOURNAL   Arch Oral Biol 46 (4), 335-341 (2001)
   PUBMED   11269867
REFERENCE   8  (residues 1 to 1082)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 1082)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   10 (residues 1 to 1082)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021105.13 and AC108469.5.
            
            Summary: The protein encoded by this gene shares similarity with
            the yeast Sec31 protein, and is a component of the outer layer of
            the coat protein complex II (COPII). The encoded protein is
            involved in vesicle budding from the endoplasmic reticulum (ER) and
            contains multiple WD repeats near the N-terminus and a proline-rich
            region in the C-terminal half. It associates with the protein
            encoded by the SEC13 homolog, nuclear pore and COPII coat complex
            component (SEC13), and is required for ER-Golgi transport.
            Monoubiquitylation of this protein by CUL3-KLHL12 was found to
            regulate the size of COPII coats to accommodate unusually shaped
            cargo. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1082
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..1082
                     /product="protein transport protein Sec31A isoform 29"
                     /note="yeast Sec31p homolog; protein transport protein
                     Sec31A; web1-like protein; SEC31 homolog A, COPII coat
                     complex component; SEC31-related protein A; SEC31-like
                     protein 1; SEC31 homolog A, COPII coating complex
                     component"
                     /calculated_mol_wt=118556
     Region          13..332
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(26,40,46..47,52..53,91,95,101..102,117,121,139,144,
                     150..151,164,185,190,196..197,209..210,231,235,244..245,
                     258..259,277,282,288..289,301..302,320,325,331..332)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          70..119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          125..162
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          172..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          263..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          306..331
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <573..>696
                     /region_name="ACE1-Sec16-like"
                     /note="Ancestral coatomer element 1 (ACE1) of COPII coat
                     complex assembly protein Sec16; cl14807"
                     /db_xref="CDD:449359"
     Site            order(574..578,580,582,593,595,596..597,599..600,604,610,
                     618,630,633,658..659)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187750"
     Region          <788..>1001
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     CDS             1..1082
                     /gene="SEC31A"
                     /gene_synonym="ABP125; ABP130; HPBKS; HSPC275; HSPC334;
                     NEDSOSB; SEC31L1"
                     /coded_by="NM_001400219.1:68..3316"
                     /note="isoform 29 is encoded by transcript variant 53"
                     /db_xref="GeneID:22872"
                     /db_xref="HGNC:HGNC:17052"
                     /db_xref="MIM:610257"
ORIGIN      
        1 mklkevdrta mqawspaqnh piylatgtsa qqldatfstn asleifeldl sdpsldmksc
       61 atfssshryh kliwgpykmd skgdvsgvli aggengniil ydpskiiagd kevviaqndk
      121 htgpvraldv nifqtnlvas ganeseiyiw dlnnfatpmt pgaktqpped isciawnrqv
      181 qhilasasps gratvwdlrk nepiikvsdh snrmhcsgla whpdvatqmv laseddrlpv
      241 iqmwdlrfas splrvlenha rgilaiawsm adpelllscg kdakilcsnp ntgevlyelp
      301 tntqwcfdiq wcprnpavls aasfdgrisv ysimggstdg lrqkqvdkls ssfgnldpfg
      361 tgqplpplqi pqqtaqhsiv lplkkppkwi rrpvgasfsf ggklvtfenv rmpshqgaeq
      421 qqqqhhvfis qvvtekefls rsdqlqqavq sqgfinycqk kidasqtefe knvwsflkvn
      481 feddsrgkyl ellgyrkedl gkkialalnk vdganvalkd sdqvaqsdge espaaeeqll
      541 gehikeekee seflpssggt fnisvsgdid glitqalltg nfesavdlcl hdnrmadaii
      601 laiaggqell artqkkyfak sqskitrlit avvmknwkei vescdlknwr ealaavltya
      661 kpdefsalcd llgtrleneg dsllqtqacl cyicagnvek lvacwtkaqd gshplslqdl
      721 iekvvilrka vqltqamdts tvgvllaakm sqyanllaaq gsiaaalafl pdntnqpnim
      781 qlrdrlcraq gepvaghesp kipyekqqlp kgrpgpvagh hqmprvqtqq yyphgenppp
      841 pgfimhgnvn pnaagqlpts pghmhtqvpp ypqpqrpqng wndppalnrv pkkkkmpenf
      901 mppvpitspi mnplgdpqsq mlqqqpsapv plssqssfpq phlpggqpfh gvqqplgqtg
      961 mppsfskpni egapgapign tfqhvqslpt kkitkkpipd ehlilkttfe dliqrclssa
     1021 tdplsptits glhniarsie trnysegltm hthivstsnf setsafmpvl kvvltqankl
     1081 gv
//
LOCUS       NP_001353465             447 aa            linear   PRI 21-NOV-2025
DEFINITION  tetratricopeptide repeat protein 8 isoform H [Homo sapiens].
ACCESSION   NP_001353465 XP_016876467
VERSION     NP_001353465.1
DBSOURCE    REFSEQ: accession NM_001366536.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Ullah,A., Umair,M., Yousaf,M., Khan,S.A., Nazim-Ud-Din,M., Shah,K.,
            Ahmad,F., Azeem,Z., Ali,G., Alhaddad,B., Rafique,A., Jan,A.,
            Haack,T.B., Strom,T.M., Meitinger,T., Ghous,T. and Ahmad,W.
  TITLE     Sequence variants in four genes underlying Bardet-Biedl syndrome in
            consanguineous families
  JOURNAL   Mol Vis 23, 482-494 (2017)
   PUBMED   28761321
  REMARK    GeneRIF: Two novel mutations and three previously reported
            variants, identified in the present study, further extend the body
            of evidence implicating BBS6, BBS7, BBS8, and BBS10 in causing
            Bardet-Biedl Syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Nachury,M.V., Loktev,A.V., Zhang,Q., Westlake,C.J., Peranen,J.,
            Merdes,A., Slusarski,D.C., Scheller,R.H., Bazan,J.F.,
            Sheffield,V.C. and Jackson,P.K.
  TITLE     A core complex of BBS proteins cooperates with the GTPase Rab8 to
            promote ciliary membrane biogenesis
  JOURNAL   Cell 129 (6), 1201-1213 (2007)
   PUBMED   17574030
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Badano,J.L., Leitch,C.C., Ansley,S.J., May-Simera,H., Lawson,S.,
            Lewis,R.A., Beales,P.L., Dietz,H.C., Fisher,S. and Katsanis,N.
  TITLE     Dissection of epistasis in oligogenic Bardet-Biedl syndrome
  JOURNAL   Nature 439 (7074), 326-330 (2006)
   PUBMED   16327777
REFERENCE   7  (residues 1 to 447)
  AUTHORS   Ansley,S.J., Badano,J.L., Blacque,O.E., Hill,J., Hoskins,B.E.,
            Leitch,C.C., Kim,J.C., Ross,A.J., Eichers,E.R., Teslovich,T.M.,
            Mah,A.K., Johnsen,R.C., Cavender,J.C., Lewis,R.A., Leroux,M.R.,
            Beales,P.L. and Katsanis,N.
  TITLE     Basal body dysfunction is a likely cause of pleiotropic
            Bardet-Biedl syndrome
  JOURNAL   Nature 425 (6958), 628-633 (2003)
   PUBMED   14520415
  REMARK    GeneRIF: A homozygous null BBS8 mutation leads to Bardet-Biedl
            syndrome with randomization of left-right body axis symmetry, a
            known defect of the nodal cilium
REFERENCE   8  (residues 1 to 447)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   9  (residues 1 to 447)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   10 (residues 1 to 447)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121768.4 and AL133238.3.
            
            On Oct 11, 2018 this sequence version replaced XP_016876467.1.
            
            Summary: This gene encodes a protein that has been directly linked
            to Bardet-Biedl syndrome. The primary features of this syndrome
            include retinal dystrophy, obesity, polydactyly, renal
            abnormalities and learning disabilities. Experimentation in
            non-human eukaryotes suggests that this gene is expressed in
            ciliated cells and that it is involved in the formation of cilia. A
            mutation in this gene has also been implicated in nonsyndromic
            retinitis pigmentosa. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jan 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.224115.1,
                                           SRR1803611.216957.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q31.3"
     Protein         1..447
                     /product="tetratricopeptide repeat protein 8 isoform H"
                     /note="Bardet-Biedl syndrome type 8; TPR repeat protein 8"
                     /calculated_mol_wt=50752
     Region          30..154
                     /region_name="TTC8_N"
                     /note="N-terminal domain of tetratricopeptide repeat
                     domain 8; cd21341"
                     /db_xref="CDD:411061"
     Site            order(190,193..194,196,219,222..223,226..227,229..230,253,
                     256..257,260..261,264)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          190..213
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          192..426
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          217..247
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          252..280
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          286..314
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(321,324..325,328..329,331,358,361..362,365..366,
                     368..369,392,395..396,399..400,403)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          321..348
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          353..386
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..447
                     /gene="TTC8"
                     /gene_synonym="BBS8; RP51"
                     /coded_by="NM_001366536.2:58..1401"
                     /note="isoform H is encoded by transcript variant 9"
                     /db_xref="GeneID:123016"
                     /db_xref="HGNC:HGNC:20087"
                     /db_xref="MIM:608132"
ORIGIN      
        1 mssemeplll awsyfrrrkf qlcadlctqm lekspydqaa wilkaralte mvyideidvd
       61 qegiaemmld enaiaqvprp gtslklpgtn qtggpsqavr pitqagrpit gflrpstqsg
      121 rpgtmeqair tprtaytarp itsssgrfvr lgtalfeyif hhendvktal dlaalstehs
      181 qykdwwwkvq igkcyyrlgm yreaekqfks alkqqemvdt flylakvyvs ldqpvtalnl
      241 fkqgldkfpg evtllcgiar iyeemnnmss aaeyykevlk qdnthveaia cigsnhfysd
      301 qpeialrfyr rllqmgiyng qlfnnlglcc fyaqqydmtl tsferalsla eneeeaadvw
      361 ynlghvavgi gdtnlahqcf rlalvnnnnh aeaynnlavl emrkghveqi gdlqrsyvaa
      421 qkseaafpdh vdtqhlikql rqhfaml
//
LOCUS       NP_001273638             345 aa            linear   PRI 21-NOV-2025
DEFINITION  general transcription factor 3C polypeptide 5 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001273638
VERSION     NP_001273638.1
DBSOURCE    REFSEQ: accession NM_001286709.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Iwata-Otsubo,A., Skraban,C.M., Yoshimura,A., Sakata,T.,
            Alves,C.A.P., Fiordaliso,S.K., Kuroda,Y., Vengoechea,J.,
            Grochowsky,A., Ernste,P., Lulis,L., Nesbitt,A., Tayoun,A.A.,
            Gray,C., Towne,M.C., Radtke,K., Normand,E.A., Rhodes,L., Seiler,C.,
            Shirahige,K. and Izumi,K.
  TITLE     Biallelic variants in GTF3C5, a regulator of RNA polymerase
            III-mediated transcription, cause a multisystem developmental
            disorder
  JOURNAL   Hum Genet 143 (3), 437-453 (2024)
   PUBMED   38520561
  REMARK    GeneRIF: Biallelic variants in GTF3C5, a regulator of RNA
            polymerase III-mediated transcription, cause a multisystem
            developmental disorder.
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Dumay-Odelot,H., Marck,C., Durrieu-Gaillard,S., Lefebvre,O.,
            Jourdain,S., Prochazkova,M., Pflieger,A. and Teichmann,M.
  TITLE     Identification, molecular cloning, and characterization of the
            sixth subunit of human transcription factor TFIIIC
  JOURNAL   J Biol Chem 282 (23), 17179-17189 (2007)
   PUBMED   17409385
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Hirschowitz,E.A., Hiestand,D.M. and Yannelli,J.R.
  TITLE     Vaccines for lung cancer
  JOURNAL   J Thorac Oncol 1 (1), 93-104 (2006)
   PUBMED   17409835
  REMARK    Review article
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Hsieh,Y.J., Kundu,T.K., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     The TFIIIC90 subunit of TFIIIC interacts with multiple components
            of the RNA polymerase III machinery and contains a histone-specific
            acetyltransferase activity
  JOURNAL   Mol Cell Biol 19 (11), 7697-7704 (1999)
   PUBMED   10523658
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Hsieh,Y.J., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     Cloning and characterization of two evolutionarily conserved
            subunits (TFIIIC102 and TFIIIC63) of human TFIIIC and their
            involvement in functional interactions with TFIIIB and RNA
            polymerase III
  JOURNAL   Mol Cell Biol 19 (7), 4944-4952 (1999)
   PUBMED   10373544
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB194811.1, BQ673969.1, AL162417.23 and BC017337.2.
            
            Transcript Variant: This variant (3) lacks two alternate exons in
            the 5' region, which results in translation initiation from an
            alternate start codon, and it lacks an alternate in-frame exon in
            the 3' coding region, compared to variant 1. The encoded isoform
            (3) has a distinct N-terminus and is shorter than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2663565.1,
                                           SRR14038192.2076625.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..345
                     /product="general transcription factor 3C polypeptide 5
                     isoform 3"
                     /note="transcription factor IIIC, 63 kD; general
                     transcription factor 3C polypeptide 5; TF3C-epsilon;
                     TFIIIC 63 kDa subunit; transcription factor IIIC subunit
                     epsilon; transcription factor IIIC 63 kDa subunit; general
                     transcription factor IIIC, polypeptide 5, 63kDa"
                     /calculated_mol_wt=39564
     Region          24..148
                     /region_name="Tau95"
                     /note="RNA polymerase III transcription factor (TF)IIIC
                     subunit HTH domain; pfam09734"
                     /db_xref="CDD:462865"
     CDS             1..345
                     /gene="GTF3C5"
                     /gene_synonym="TFiiiC2-63; TFIIIC63; TFIIICepsilon"
                     /coded_by="NM_001286709.2:119..1156"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS75927.1"
                     /db_xref="GeneID:9328"
                     /db_xref="HGNC:HGNC:4668"
                     /db_xref="MIM:604890"
ORIGIN      
        1 mwlrccrlwa arkaspgegy nnppisgenl iglsrarrph naifvnfede evpkqpleaa
       61 aqtwrrvctn pvdrkveeel rklfdirpiw srnavkanis vhpdklkvll pfiayymitg
      121 pwrslwirfg ydprknpdak iyqvldfrir cgmkhgyaps dlpvkakrst ynyslpitvk
      181 ktssqlvtmh dlkqglgpsg tsgarkpass kyklkdsvyi fregalppyr qmfyqlcdln
      241 veelqkiihr ndgaenscte rdgwclpkts delrdtmslm irqtirskrp alfsssakad
      301 ggkeqltyes gedeedeeee eeeeedfkps dgsenemete ildyv
//
LOCUS       NP_001337874             289 aa            linear   PRI 21-NOV-2025
DEFINITION  actin-related protein 3B isoform 5 [Homo sapiens].
ACCESSION   NP_001337874 XP_016867951
VERSION     NP_001337874.1
DBSOURCE    REFSEQ: accession NM_001350945.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Abella,J.V., Galloni,C., Pernier,J., Barry,D.J., Kjaer,S.,
            Carlier,M.F. and Way,M.
  TITLE     Isoform diversity in the Arp2/3 complex determines actin filament
            dynamics
  JOURNAL   Nat Cell Biol 18 (1), 76-86 (2016)
   PUBMED   26655834
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Shin,J.H., Gulesserian,T., Weitzdoerfer,R., Fountoulakis,M. and
            Lubec,G.
  TITLE     Derangement of hypothetical proteins in fetal Down's syndrome brain
  JOURNAL   Neurochem Res 29 (6), 1307-1316 (2004)
   PUBMED   15176487
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Shindo-Okada,N. and Iigo,M.
  TITLE     Expression of the Arp11 gene suppresses the tumorigenicity of PC-14
            human lung adenocarcinoma cells
  JOURNAL   Biochem Biophys Res Commun 312 (4), 889-896 (2003)
   PUBMED   14651955
  REMARK    GeneRIF: Thus, overexpression of Arp11 may suppress tumorigenicity
            in nude mice.
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Eckley,D.M. and Schroer,T.A.
  TITLE     Interactions between the evolutionarily conserved, actin-related
            protein, Arp11, actin, and Arp1
  JOURNAL   Mol Biol Cell 14 (7), 2645-2654 (2003)
   PUBMED   12857853
REFERENCE   8  (residues 1 to 289)
  AUTHORS   Shindo-Okada,N. and Shimizu,K.
  TITLE     Isolation of a novel actin-related gene expressed in low-metastatic
            PC-14 human lung adenocarcinoma
  JOURNAL   Biochem Biophys Res Commun 280 (1), 61-67 (2001)
   PUBMED   11162478
REFERENCE   9  (residues 1 to 289)
  AUTHORS   Jay,P., Berge-Lefranc,J.L., Massacrier,A., Roessler,E., Wallis,D.,
            Muenke,M., Gastaldi,M., Taviaux,S., Cau,P. and Berta,P.
  TITLE     ARP3beta, the gene encoding a new human actin-related protein, is
            alternatively spliced and predominantly expressed in brain neuronal
            cells
  JOURNAL   Eur J Biochem 267 (10), 2921-2928 (2000)
   PUBMED   10806390
REFERENCE   10 (residues 1 to 289)
  AUTHORS   Machesky,L.M. and Gould,K.L.
  TITLE     The Arp2/3 complex: a multifunctional actin organizer
  JOURNAL   Curr Opin Cell Biol 11 (1), 117-121 (1999)
   PUBMED   10047519
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092180.5 and AC072057.8.
            
            On Apr 27, 2017 this sequence version replaced XP_016867951.1.
            
            Summary: This gene encodes a member of the actin-related proteins
            (ARP), which form multiprotein complexes and share 35-55% amino
            acid identity with conventional actin. The protein encoded by this
            gene may have a regulatory role in the actin cytoskeleton and
            induce cell-shape change and motility. Pseudogenes of this gene are
            located on chromosomes 2, 4, 10, 16, 22 and Y. Alternative splicing
            results in multiple transcript variants and protein isoforms.
            [provided by RefSeq, Jul 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.85809.1,
                                           SRR14038195.2833964.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1-q36.2"
     Protein         1..289
                     /product="actin-related protein 3B isoform 5"
                     /note="actin-related protein 3-beta; actin-related protein
                     Arp11; ARP3-beta; actin-like protein 3B; actin-related
                     protein ARP4; ARP3 actin related protein 3 homolog B"
                     /calculated_mol_wt=32709
     Region          <1..281
                     /region_name="ASKHA_NBD_Arp3-like"
                     /note="nucleotide-binding domain (NBD) of actin-related
                     protein3 (Arp3) and similar proteins; cd10221"
                     /db_xref="CDD:466822"
     CDS             1..289
                     /gene="ACTR3B"
                     /gene_synonym="ARP11; ARP3BETA"
                     /coded_by="NM_001350945.2:500..1369"
                     /note="isoform 5 is encoded by transcript variant 8"
                     /db_xref="GeneID:57180"
                     /db_xref="HGNC:HGNC:17256"
ORIGIN      
        1 mfesfnvpgl yiavqavlal aaswtsrqvg ertltgivid sgdgvthvip vaegyvigsc
       61 ikhipiagrd ityfiqqllr erevgippeq sletakaike kycyicpdiv kefakydvdp
      121 rkwikqytgi nainqkkfvi dvgyerflgp eiffhpefan pdfmesisdv vdeviqncpi
      181 dvrrplyknv vlsggstmfr dfgrrlqrdl krvvdarlrl seelsggrik pkpvevqvvt
      241 hhmqryavwf ggsmlastpe ffqvchtkkd yeeygpsicr hnpvfgvms
//
LOCUS       NP_001274525             158 aa            linear   PRI 21-NOV-2025
DEFINITION  excitatory amino acid transporter 5 isoform 2 [Homo sapiens].
ACCESSION   NP_001274525
VERSION     NP_001274525.1
DBSOURCE    REFSEQ: accession NM_001287596.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Lee,A., Balcar,V.J., McCombe,P. and Pow,D.V.
  TITLE     Human brain neurons express a novel splice variant of excitatory
            amino acid transporter 5 (hEAAT5v)
  JOURNAL   J Comp Neurol 528 (17), 3134-3142 (2020)
   PUBMED   32173860
  REMARK    GeneRIF: Human brain neurons express a novel splice variant of
            excitatory amino acid transporter 5 (hEAAT5v).
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Melville,S.A., Buros,J., Parrado,A.R., Vardarajan,B., Logue,M.W.,
            Shen,L., Risacher,S.L., Kim,S., Jun,G., DeCarli,C., Lunetta,K.L.,
            Baldwin,C.T., Saykin,A.J. and Farrer,L.A.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative
  TITLE     Multiple loci influencing hippocampal degeneration identified by
            genome scan
  JOURNAL   Ann Neurol 72 (1), 65-75 (2012)
   PUBMED   22745009
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Oshikawa,M., Tsutsui,C., Ikegami,T., Fuchida,Y., Matsubara,M.,
            Toyama,S., Usami,R., Ohtoko,K. and Kato,S.
  TITLE     Full-length transcriptome analysis of human retina-derived cell
            lines ARPE-19 and Y79 using the vector-capping method
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6662-6670 (2011)
   PUBMED   21697133
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 158)
  AUTHORS   Chung,S.A., Taylor,K.E., Graham,R.R., Nititham,J., Lee,A.T.,
            Ortmann,W.A., Jacob,C.O., Alarcon-Riquelme,M.E., Tsao,B.P.,
            Harley,J.B., Gaffney,P.M., Moser,K.L., Petri,M., Demirci,F.Y.,
            Kamboh,M.I., Manzi,S., Gregersen,P.K., Langefeld,C.D., Behrens,T.W.
            and Criswell,L.A.
  CONSRTM   SLEGEN
  TITLE     Differential genetic associations for systemic lupus erythematosus
            based on anti-dsDNA autoantibody production
  JOURNAL   PLoS Genet 7 (3), e1001323 (2011)
   PUBMED   21408207
REFERENCE   6  (residues 1 to 158)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 158)
  AUTHORS   Gratacos,M., Costas,J., de Cid,R., Bayes,M., Gonzalez,J.R.,
            Baca-Garcia,E., de Diego,Y., Fernandez-Aranda,F.,
            Fernandez-Piqueras,J., Guitart,M., Martin-Santos,R., Martorell,L.,
            Menchon,J.M., Roca,M., Saiz-Ruiz,J., Sanjuan,J., Torrens,M.,
            Urretavizcaya,M., Valero,J., Vilella,E., Estivill,X. and
            Carracedo,A.
  CONSRTM   Psychiatric Genetics Network Group
  TITLE     Identification of new putative susceptibility genes for several
            psychiatric disorders by association analysis of regulatory and
            non-synonymous SNPs of 306 genes involved in neurotransmission and
            neurodevelopment
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 150B (6), 808-816 (2009)
   PUBMED   19086053
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 158)
  AUTHORS   Boehmer,C., Rajamanickam,J., Schniepp,R., Kohler,K., Wulff,P.,
            Kuhl,D., Palmada,M. and Lang,F.
  TITLE     Regulation of the excitatory amino acid transporter EAAT5 by the
            serum and glucocorticoid dependent kinases SGK1 and SGK3
  JOURNAL   Biochem Biophys Res Commun 329 (2), 738-742 (2005)
   PUBMED   15737648
  REMARK    GeneRIF: In conclusion, the kinases SGK1 and SGK3 increase EAAT5
            activity by increasing cell surface abundance of the carrier.
REFERENCE   9  (residues 1 to 158)
  AUTHORS   Wistow,G., Bernstein,S.L., Ray,S., Wyatt,M.K., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human iris for the NEIBank
            Project: steroid-response factors and similarities with retinal
            pigment epithelium
  JOURNAL   Mol Vis 8, 185-195 (2002)
   PUBMED   12107412
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 158)
  AUTHORS   Arriza,J.L., Eliasof,S., Kavanaugh,M.P. and Amara,S.G.
  TITLE     Excitatory amino acid transporter 5, a retinal glutamate
            transporter coupled to a chloride conductance
  JOURNAL   Proc Natl Acad Sci U S A 94 (8), 4155-4160 (1997)
   PUBMED   9108121
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445183.19, AB593060.1 and BC000651.2.
            
            Transcript Variant: This variant (2) lacks several exons and uses
            an alternate 3'-terminal exon, compared to variant 1. The encoded
            isoform (2) has a shorter and distinct C-terminus, compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000651.2, BG472897.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..158
                     /product="excitatory amino acid transporter 5 isoform 2"
                     /note="excitatory amino acid transporter 5 (retinal
                     glutamate transporter); solute carrier family 1 (glutamate
                     transporter), member 7"
                     /calculated_mol_wt=17252
     Site            17..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00341.2)"
     Region          19..>144
                     /region_name="SDF"
                     /note="Sodium:dicarboxylate symporter family; cl00573"
                     /db_xref="CDD:444986"
     Site            60..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00341.2)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00341.2)"
     CDS             1..158
                     /gene="SLC1A7"
                     /gene_synonym="AAAT; EAAT5"
                     /coded_by="NM_001287596.2:190..666"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS72798.1"
                     /db_xref="GeneID:6512"
                     /db_xref="HGNC:HGNC:10945"
                     /db_xref="MIM:604471"
ORIGIN      
        1 mvphailarg rdvcrrngll ilsvlsvivg cllgfflrtr rlspqeisyf qfpgellmrm
       61 lkmmilplvv sslmsglasl daktssrlgv ltvayylwtt fmavivgifm vsiihpgsaa
      121 qketteqsgk pimssadall dlirqkeesw rngpkgpg
//
LOCUS       NP_001308738             347 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA repair protein RAD51 homolog 2 isoform 4 [Homo sapiens].
ACCESSION   NP_001308738
VERSION     NP_001308738.1
DBSOURCE    REFSEQ: accession NM_001321809.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Slupianek,A., Jozwiakowski,S.K., Gurdek,E. and Skorski,T.
  TITLE     BCR/ABL kinase interacts with and phosphorylates the RAD51 paralog,
            RAD51B
  JOURNAL   Leukemia 23 (12), 2308-2310 (2009)
   PUBMED   19657362
  REMARK    GeneRIF: BCR/ABL fragments were used for identifying the sites of
            BCR/ABL interaction with RAD51B
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Thomas,G., Jacobs,K.B., Kraft,P., Yeager,M., Wacholder,S.,
            Cox,D.G., Hankinson,S.E., Hutchinson,A., Wang,Z., Yu,K.,
            Chatterjee,N., Garcia-Closas,M., Gonzalez-Bosquet,J.,
            Prokunina-Olsson,L., Orr,N., Willett,W.C., Colditz,G.A.,
            Ziegler,R.G., Berg,C.D., Buys,S.S., McCarty,C.A., Feigelson,H.S.,
            Calle,E.E., Thun,M.J., Diver,R., Prentice,R., Jackson,R.,
            Kooperberg,C., Chlebowski,R., Lissowska,J., Peplonska,B.,
            Brinton,L.A., Sigurdson,A., Doody,M., Bhatti,P., Alexander,B.H.,
            Buring,J., Lee,I.M., Vatten,L.J., Hveem,K., Kumle,M., Hayes,R.B.,
            Tucker,M., Gerhard,D.S., Fraumeni,J.F. Jr., Hoover,R.N.,
            Chanock,S.J. and Hunter,D.J.
  TITLE     A multistage genome-wide association study in breast cancer
            identifies two new risk alleles at 1p11.2 and 14q24.1 (RAD51L1)
  JOURNAL   Nat Genet 41 (5), 579-584 (2009)
   PUBMED   19330030
  REMARK    GeneRIF: A multistage genome-wide association study in breast
            cancer identifies two new risk alleles at 1p11.2 and 14q24.1
            (RAD51L1).
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Quade,B.J., Weremowicz,S., Neskey,D.M., Vanni,R., Ladd,C., Dal
            Cin,P. and Morton,C.C.
  TITLE     Fusion transcripts involving HMGA2 are not a common molecular
            mechanism in uterine leiomyomata with rearrangements in 12q15
  JOURNAL   Cancer Res 63 (6), 1351-1358 (2003)
   PUBMED   12649198
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Lio,Y.C., Mazin,A.V., Kowalczykowski,S.C. and Chen,D.J.
  TITLE     Complex formation by the human Rad51B and Rad51C DNA repair
            proteins and their activities in vitro
  JOURNAL   J Biol Chem 278 (4), 2469-2478 (2003)
   PUBMED   12427746
  REMARK    GeneRIF: Rad51B and Rad51C function through interactions with the
            human Rad51 recombinase and play a crucial role in the homologous
            recombinational repair pathway
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Masson,J.Y., Tarsounas,M.C., Stasiak,A.Z., Stasiak,A., Shah,R.,
            McIlwraith,M.J., Benson,F.E. and West,S.C.
  TITLE     Identification and purification of two distinct complexes
            containing the five RAD51 paralogs
  JOURNAL   Genes Dev 15 (24), 3296-3307 (2001)
   PUBMED   11751635
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Takata,M., Sasaki,M.S., Sonoda,E., Fukushima,T., Morrison,C.,
            Albala,J.S., Swagemakers,S.M., Kanaar,R., Thompson,L.H. and
            Takeda,S.
  TITLE     The Rad51 paralog Rad51B promotes homologous recombinational repair
  JOURNAL   Mol Cell Biol 20 (17), 6476-6482 (2000)
   PUBMED   10938124
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Cartwright,R., Dunn,A.M., Simpson,P.J., Tambini,C.E. and Thacker,J.
  TITLE     Isolation of novel human and mouse genes of the recA/RAD51
            recombination-repair gene family
  JOURNAL   Nucleic Acids Res 26 (7), 1653-1659 (1998)
   PUBMED   9512535
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Albala,J.S., Thelen,M.P., Prange,C., Fan,W., Christensen,M.,
            Thompson,L.H. and Lennon,G.G.
  TITLE     Identification of a novel human RAD51 homolog, RAD51B
  JOURNAL   Genomics 46 (3), 476-479 (1997)
   PUBMED   9441753
  REMARK    Erratum:[Genomics 1998 Aug 1;51(3):480]
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Rice,M.C., Smith,S.T., Bullrich,F., Havre,P. and Kmiec,E.B.
  TITLE     Isolation of human and mouse genes based on homology to REC2, a
            recombinational repair gene from the fungus Ustilago maydis
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7417-7422 (1997)
   PUBMED   9207106
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121595.5, AL122013.5,
            AL589168.3 and AL121820.4.
            
            Summary: The protein encoded by this gene is a member of the RAD51
            protein family. RAD51 family members are evolutionarily conserved
            proteins essential for DNA repair by homologous recombination. This
            protein has been shown to form a stable heterodimer with the family
            member RAD51C, which further interacts with the other family
            members, such as RAD51, XRCC2, and XRCC3. Overexpression of this
            gene was found to cause cell cycle G1 delay and cell apoptosis,
            which suggested a role of this protein in sensing DNA damage.
            Rearrangements between this locus and high mobility group AT-hook 2
            (HMGA2, GeneID 8091) have been observed in uterine leiomyomata.
            [provided by RefSeq, Mar 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.124038.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.1"
     Protein         1..347
                     /product="DNA repair protein RAD51 homolog 2 isoform 4"
                     /note="RecA-like protein; recombination repair protein;
                     DNA repair protein RAD51 homolog 2; RAD51 homolog B"
                     /calculated_mol_wt=37804
     Region          1..75
                     /region_name="Interaction with RAD51C"
                     /note="propagated from UniProtKB/Swiss-Prot (O15315.2)"
     Region          91..327
                     /region_name="Rad51B"
                     /note="RAD51B recombinase; cd19493"
                     /db_xref="CDD:410901"
     Site            order(111..116,144,210,258,312)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:410901"
     Site            252..253
                     /site_type="other"
                     /note="Breakpoint for translocation to form HMGA2-RAD51B;
                     propagated from UniProtKB/Swiss-Prot (O15315.2)"
     CDS             1..347
                     /gene="RAD51B"
                     /gene_synonym="R51H2; RAD51L1; REC2"
                     /coded_by="NM_001321809.2:78..1121"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:5890"
                     /db_xref="HGNC:HGNC:9822"
                     /db_xref="MIM:602948"
ORIGIN      
        1 mgskklkrvg lsqelcdrls rhqiltcqdf lclsplelmk vtglsyrgvh ellcmvsrac
       61 apkmqtaygi kaqrsadfsp aflsttlsal dealhggvac gslteitgpp gcgktqfcim
      121 msilatlptn mgglegavvy idtesafsae rlveiaesrf pryfnteekl lltsskvhly
      181 reltcdevlq riesleeeii skgiklvild svasvvrkef daqlqgnlke rnkflareas
      241 slkylaeefs ipviltnqit thlsgalasq adlvspaddl slsegtsgss cviaalgntw
      301 shsvntrlil qyldserrqi liaksplapf tsfvytikee glvlqgl
//
LOCUS       NP_001365386            3058 aa            linear   PRI 21-NOV-2025
DEFINITION  dmX-like protein 2 isoform 4 [Homo sapiens].
ACCESSION   NP_001365386 XP_005254312
VERSION     NP_001365386.1
DBSOURCE    REFSEQ: accession NM_001378457.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 3058)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 3058)
  AUTHORS   Wonkam-Tingang,E., Schrauwen,I., Esoh,K.K., Bharadwaj,T.,
            Nouel-Saied,L.M., Acharya,A., Nasir,A., Leal,S.M. and Wonkam,A.
  TITLE     A novel variant in DMXL2 gene is associated with autosomal dominant
            non-syndromic hearing impairment (DFNA71) in a Cameroonian family
  JOURNAL   Exp Biol Med (Maywood) 246 (13), 1524-1532 (2021)
   PUBMED   33715530
  REMARK    GeneRIF: A novel variant in DMXL2 gene is associated with autosomal
            dominant non-syndromic hearing impairment (DFNA71) in a Cameroonian
            family.
            Erratum:[Exp Biol Med (Maywood). 2021 Nov;246(21):NP5. doi:
            10.1177/15353702211040362. PMID: 34749523]
REFERENCE   3  (residues 1 to 3058)
  AUTHORS   Jaskolka,M.C., Winkley,S.R. and Kane,P.M.
  TITLE     RAVE and Rabconnectin-3 Complexes as Signal Dependent Regulators of
            Organelle Acidification
  JOURNAL   Front Cell Dev Biol 9, 698190 (2021)
   PUBMED   34249946
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 3058)
  AUTHORS   Esposito,A., Falace,A., Wagner,M., Gal,M., Mei,D., Conti,V.,
            Pisano,T., Aprile,D., Cerullo,M.S., De Fusco,A., Giovedi,S.,
            Seibt,A., Magen,D., Polster,T., Eran,A., Stenton,S.L., Fiorillo,C.,
            Ravid,S., Mayatepek,E., Hafner,H., Wortmann,S., Levanon,E.Y.,
            Marini,C., Mandel,H., Benfenati,F., Distelmaier,F., Fassio,A. and
            Guerrini,R.
  TITLE     Biallelic DMXL2 mutations impair autophagy and cause Ohtahara
            syndrome with progressive course
  JOURNAL   Brain 142 (12), 3876-3891 (2019)
   PUBMED   31688942
  REMARK    GeneRIF: Impaired lysosomal function and autophagy caused by
            biallelic DMXL2 mutations affect neuronal development and synapse
            formation and result in Ohtahara syndrome with profound
            developmental impairment and reduced life expectancy.
            Erratum:[Brain. 2020 Feb 1;143(2):e16. doi: 10.1093/brain/awz397.
            PMID: 31840736]
REFERENCE   5  (residues 1 to 3058)
  AUTHORS   Costain,G., Walker,S., Argiropoulos,B., Baribeau,D.A.,
            Bassett,A.S., Boot,E., Devriendt,K., Kellam,B., Marshall,C.R.,
            Prasad,A., Serrano,M.A., Stavropoulos,D.J., Twede,H.,
            Vermeesch,J.R., Vorstman,J.A.S. and Scherer,S.W.
  TITLE     Rare copy number variations affecting the synaptic gene DMXL2 in
            neurodevelopmental disorders
  JOURNAL   J Neurodev Disord 11 (1), 3 (2019)
   PUBMED   30732576
  REMARK    GeneRIF: Disruption of DMXL2 may predispose to NDDs including
            autism spectrum disorder.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 3058)
  AUTHORS   Tata,B., Huijbregts,L., Jacquier,S., Csaba,Z., Genin,E., Meyer,V.,
            Leka,S., Dupont,J., Charles,P., Chevenne,D., Carel,J.C., Leger,J.
            and de Roux,N.
  TITLE     Haploinsufficiency of Dmxl2, encoding a synaptic protein, causes
            infertility associated with a loss of GnRH neurons in mouse
  JOURNAL   PLoS Biol 12 (9), e1001952 (2014)
   PUBMED   25248098
  REMARK    GeneRIF: Haploinsufficiency of Dmxl2, encoding a synaptic protein,
            causes infertility associated with a loss of GnRH neurons in humans
            and mice.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 3058)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   8  (residues 1 to 3058)
  AUTHORS   Sethi,N., Yan,Y., Quek,D., Schupbach,T. and Kang,Y.
  TITLE     Rabconnectin-3 is a functional regulator of mammalian Notch
            signaling
  JOURNAL   J Biol Chem 285 (45), 34757-34764 (2010)
   PUBMED   20810660
  REMARK    GeneRIF: an important role for Rabconnectin-3 and V-ATPase activity
            in the Notch signaling pathway in mammalian cells.
REFERENCE   9  (residues 1 to 3058)
  AUTHORS   Luke,M.M., O'Meara,E.S., Rowland,C.M., Shiffman,D., Bare,L.A.,
            Arellano,A.R., Longstreth,W.T. Jr., Lumley,T., Rice,K., Tracy,R.P.,
            Devlin,J.J. and Psaty,B.M.
  TITLE     Gene variants associated with ischemic stroke: the cardiovascular
            health study
  JOURNAL   Stroke 40 (2), 363-368 (2009)
   PUBMED   19023099
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 3058)
  AUTHORS   Nagano,F., Kawabe,H., Nakanishi,H., Shinohara,M.,
            Deguchi-Tawarada,M., Takeuchi,M., Sasaki,T. and Takai,Y.
  TITLE     Rabconnectin-3, a novel protein that binds both GDP/GTP exchange
            protein and GTPase-activating protein for Rab3 small G protein
            family
  JOURNAL   J Biol Chem 277 (12), 9629-9632 (2002)
   PUBMED   11809763
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020892.7 and AC066613.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 14, 2020 this sequence version replaced XP_005254312.1.
            
            Summary: This gene encodes a protein with 12 WD domains. Proteins
            with WD domains are involved in many functions including
            participation in signal transduction pathways. Participation of the
            encoded protein in regulation of the Notch signaling pathway has
            been demonstrated in vitro using several human cell lines
            (PMID:20810660). A gene encoding a similar protein is located on
            chromosome 5. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Aug
            2011].
            
            Transcript Variant: This variant (4) represents the longest
            transcript and encodes the longest isoform (4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3077244.1,
                                           SRR14038192.2693553.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000560891.6/ ENSP00000453267.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..3058
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.2"
     Protein         1..3058
                     /product="dmX-like protein 2 isoform 4"
                     /note="rabconnectin-3; dmX-like protein 2"
                     /calculated_mol_wt=342020
     Region          <45..268
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          61..102
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          108..145
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          109..171
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          167..207
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          174..225
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          230..278
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          235..268
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BPN8; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          417..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          492..532
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BPN8; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          595..634
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          751..803
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          878..920
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          932..959
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            944
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            945
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          1000..1037
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            1140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            1143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            1151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          1163..1204
                     /region_name="WD 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          1171..1902
                     /region_name="Rav1p_C"
                     /note="RAVE protein 1 C terminal; pfam12234"
                     /db_xref="CDD:432413"
     Region          1244..1281
                     /region_name="WD 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            1287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BPN8; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            1400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            1417
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BPN8; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            1857
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          1927..1952
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            1984
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          1999..2033
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            2022
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BPN8; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            2400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            2641
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BPN8; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          2783..2822
                     /region_name="WD 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          2788..3040
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          2826..2865
                     /region_name="WD 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          2832..2872
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2872..2914
                     /region_name="WD 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          2877..2919
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2920..2959
                     /region_name="WD 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          2926..2961
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2962..3001
                     /region_name="WD 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          2967..3003
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          3014..3052
                     /region_name="WD 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     CDS             1..3058
                     /gene="DMXL2"
                     /gene_synonym="DEE81; DFNA71; EIEE81; PEPNS; RC3"
                     /coded_by="NM_001378457.1:227..9403"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS91998.1"
                     /db_xref="GeneID:23312"
                     /db_xref="HGNC:HGNC:2938"
                     /db_xref="MIM:612186"
ORIGIN      
        1 mhlhqvltga vnpgdncysv gsvgdvpfta ygsgcdivil andfecvqii pgakhgniqv
       61 scvecsnqqg riaasygnav cifeplgins hkrncqlkcq wlktgqffls svtynlawdp
      121 qdnrlltatd siqlwappgd dileeeeeid ntvppvlndw kcvwqcktsv svhlmewspd
      181 geyfatagkd dcllkvwypm tgwkssiipq dhhevkrrqs stqfsfvyla hpravtgfsw
      241 rktskymprg svcnvlltsc hdgvcrlwae tllpedcllg eqicetttss iasslshagr
      301 hkdriqhale tihhlknlrk gqrrssvlvt haelmpdqta mhevqrhish hanalchfhi
      361 aasinpatdi pnvlvgtafn vddgnggfvv hwlnnkefhf tsstevfmhq lrklsdkqvd
      421 henddadred eehsqedrer glhmkldhdl sldreseagt gssehedger egsprtysrl
      481 svpmplptvl ldrkietllt ewnknpdmlf tihpvdgtfl vwhvkyldey npgifrqvqv
      541 sfssripvaf psgdasslsk nimmyacina tkdshhtllh qegmsvgsph gsqphsrshs
      601 thmnilaptv mmiskhidgs lnqwavtfad ksafttvltv shkfrycghr fhlndlachs
      661 vlpllltssh hnalltpeld cqwdsdnkls rlmdpvkhik gsskqplrna atrtfhdpna
      721 iyselilwrv dpigplsytg gvselarins lhtsafsnva wlptlipsyc lgtycnsasa
      781 cfvasdgknl rlyqavvdar klldelsdpe sskligevfn ivsqqstarp gciieldait
      841 nqcgsntqll hvfqedfiig ykphkedmek keteiffqps qgyrpppfse kfflvviekd
      901 snnnsilhmw hlhlksvqac lakasegass esllsvpgqk nvdsspetsp svspmphsss
      961 ianlqtaskl ilssrlvysq pldlpesvev iratpsaghl ssssiypvcl apylvvttcs
     1021 dnkvrfwkcc meanpecnks dekeiyhwkr wplmndeged nsstvsivgr pvavscsytg
     1081 rlavaykqpi hhngfvskef smhvcifece stggsewvle qtihlddlvk vgsvldsrvs
     1141 vdsnlfvysk sdallskdry lipnikhlvh ldwvskedgs hiltvgvgan ifmygrlsgi
     1201 vteqtnskdg vavitlplgg sikqgvksrw vllrsidlvs svdgtpslpv slswvrdgil
     1261 vvgmdcemhv yaqwkhavkf gdteadssna eeaamqdhst fksnmlarks vvegtaisdd
     1321 vfcsptviqd gglfeaahvl sptlpqyhpt qllelmdlgk vrrakailsh lvkciageva
     1381 ivrdpdageg tkrhlsrtis vsgstaketv tvgkdgtrdy teidsipplp lyallaadqd
     1441 tsyriseest kipqsyedqt vsqpedqyse lfqiqdiptd didlepekre nkskvinlsq
     1501 ygpayfgqeh arvlsshlmh sslpgltrle qmflvaladt vattstelde srdkscsgrd
     1561 tldecglryl lamrlhtcll tslpplyrvq llhqgvstch fawafhseae eelinmipai
     1621 qrgdpqwsel ramgigwwvr nintlrrcie kvakasfqrn ndaldaalfy lsmkkkavvw
     1681 glfrsqhdek mttffshnfn edrwrkaalk nafsllgkqr feqsaaffll agslkdaiev
     1741 clekmediql amviarlyes efetsstyis ilnqkilgcq kdgsgfsckr lhpdpflrsl
     1801 aywvmkdytr aldtlleqtp keddehqvii kscnpvafsf ynylrthpll irrnlaspeg
     1861 tlatlglkte knfvdkinli erklffttan ahfkvgcpvl alevlskipk vtktsalsak
     1921 kdqpdfishr mddvpshska lsdgngssgi ewsnvtssqy dwsqpivkvd eeplnldwge
     1981 dhdsaldeee ddavglvmks tdarekdkqs dqkasdpnml ltpqeeddpe gdtevdviae
     2041 qlkfraclki lmtelrtlat gyevdggklr fqlynwleke iaalheicnh esvikeyssk
     2101 tyskvesdll dqeemvdkpd igsyerhqie rrrlqakreh aerrkswlqk nqdllrvfls
     2161 ycslhgaqgg glasvrmelk fllqesqqet tvkqlqsplp lpttlpllsa siastktvia
     2221 npvlylnnhi hdilytivqm ktpphpsied vkvhtlhsla aslsasiyqa lcdshsyssq
     2281 tegnqftgma yqglllsdrr rlrtesieeh atpnsspaqw pgvsslinll ssaqdedqpk
     2341 lnillceavv avylslliha latnssself rlaahplnnr mwaavfgggv klvvkprrqs
     2401 enisappvls edidkhrrrf nmrmlvpgrp vkdatpppvp aerpsykekf ippelsmwdy
     2461 fvakpflpls dsgviydsde sihsdeedda ffsdtqiqeh qdpnsyswal lhltmvklal
     2521 hnvknffpia glefselpvt splgiavikn lenweqilqe kmdqfegppp nyintyptdl
     2581 svgagpailr nkamlepent pfksrdssaf pvkrlwhflv kqevlqetfi ryiftkkrkq
     2641 sesieehveq vnqnciaedc hikveadlgy pggkakvihk esdmimafsv nkancneivl
     2701 asthdvqeld vtsllacqsy iwigeeydre skssddvdyr gstttlyqps atsysasqvh
     2761 ppsslpwlgt gqtstgasvl mkrnlhnvkr mtshpvhqyy ltgaqdgsvr mfewtrpqql
     2821 vcfrqagnar vtrlyfnsqg nkcgvadgeg flsiwqvnqt asnpkpymsw qchskatsdf
     2881 afitssslva tsghsndnrn vclwdtlisp gnslihgftc hdhgatvlqy apkqqllisg
     2941 grkghvcifd irqrqlihtf qahdsaikal aldpyeeyft tgsaegnikv wrltghglih
     3001 sfksehakqs ifrnigagvm qidiiqgnrl fscgadgtlk trvlpnafni pnrildil
//
LOCUS       NP_001278675             587 aa            linear   PRI 21-NOV-2025
DEFINITION  proto-oncogene c-Rel isoform 2 [Homo sapiens].
ACCESSION   NP_001278675 XP_005264527
VERSION     NP_001278675.1
DBSOURCE    REFSEQ: accession NM_001291746.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   4  (residues 1 to 587)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   5  (residues 1 to 587)
  AUTHORS   Neumann,M., Tsapos,K., Scheppler,J.A., Ross,J. and Franza,B.R. Jr.
  TITLE     Identification of complex formation between two intracellular
            tyrosine kinase substrates: human c-Rel and the p105 precursor of
            p50 NF-kappa B
  JOURNAL   Oncogene 7 (11), 2095-2104 (1992)
   PUBMED   1437141
REFERENCE   6  (residues 1 to 587)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
REFERENCE   7  (residues 1 to 587)
  AUTHORS   Ruben,S.M., Klement,J.F., Coleman,T.A., Maher,M., Chen,C.H. and
            Rosen,C.A.
  TITLE     I-Rel: a novel rel-related protein that inhibits NF-kappa B
            transcriptional activity
  JOURNAL   Genes Dev 6 (5), 745-760 (1992)
   PUBMED   1577270
REFERENCE   8  (residues 1 to 587)
  AUTHORS   Kochel,T. and Rice,N.R.
  TITLE     v-rel- and c-rel-protein complexes bind to the NF-kappa B site in
            vitro
  JOURNAL   Oncogene 7 (3), 567-572 (1992)
   PUBMED   1549370
REFERENCE   9  (residues 1 to 587)
  AUTHORS   Brownell,E., Mittereder,N. and Rice,N.R.
  TITLE     A human rel proto-oncogene cDNA containing an Alu fragment as a
            potential coding exon
  JOURNAL   Oncogene 4 (7), 935-942 (1989)
   PUBMED   2666912
REFERENCE   10 (residues 1 to 587)
  AUTHORS   Brownell,E., Kozak,C.A., Fowle,J.R. 3rd, Modi,W.S., Rice,N.R. and
            O'Brien,S.J.
  TITLE     Comparative genetic mapping of cellular rel sequences in man,
            mouse, and the domestic cat
  JOURNAL   Am J Hum Genet 39 (2), 194-202 (1986)
   PUBMED   3529946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY123671.1, BC143885.1,
            AC010733.8 and BG036646.1.
            
            On Apr 26, 2014 this sequence version replaced XP_005264527.1.
            
            Summary: This gene encodes a protein that belongs to the Rel
            homology domain/immunoglobulin-like fold, plexin, transcription
            factor (RHD/IPT) family. Members of this family regulate genes
            involved in apoptosis, inflammation, the immune response, and
            oncogenic processes. This proto-oncogene plays a role in the
            survival and proliferation of B lymphocytes. Mutation or
            amplification of this gene is associated with B-cell lymphomas,
            including Hodgkin's lymphoma. Single nucleotide polymorphisms in
            this gene are associated with susceptibility to ulcerative colitis
            and rheumatoid arthritis. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Apr 2014].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            central coding region compared to variant 1. The encoded isoform
            (2) is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303926.1, SRR1803616.262836.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394479.4/ ENSP00000377989.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.1"
     Protein         1..587
                     /product="proto-oncogene c-Rel isoform 2"
                     /note="proto-oncogene c-Rel; oncogene REL, avian
                     reticuloendotheliosis; v-rel avian reticuloendotheliosis
                     viral oncogene homolog"
                     /calculated_mol_wt=65094
     Region          8..179
                     /region_name="RHD-n_c-Rel"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of c-Rel; cd07933"
                     /db_xref="CDD:143649"
     Site            order(22,24..25,27..28,31,111..112,179)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143649"
     Region          186..281
                     /region_name="IPT_NFkappaB"
                     /note="IPT domain of the transcription factor NFkappaB and
                     related transcription factors. NFkappaB is considered a
                     central regulator of stress responses, activated by
                     different stressful conditions, including physical stress,
                     oxidative stress, and exposure to...; cd01177"
                     /db_xref="CDD:238582"
     Site            order(187,189..191,193..195,230..232,245,256,275,278,280)
                     /site_type="other"
                     /note="ankyrin protein binding site [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(189..190,192,205,207,209,237..238,241,243)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(210,212,238..239)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238582"
     CDS             1..587
                     /gene="REL"
                     /gene_synonym="C-Rel; HIVEN86A; IMD92"
                     /coded_by="NM_001291746.2:268..2031"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS74515.1"
                     /db_xref="GeneID:5966"
                     /db_xref="HGNC:HGNC:9954"
                     /db_xref="MIM:164910"
ORIGIN      
        1 masgaynpyi eiieqprqrg mrfrykcegr sagsipgehs tdnnrtypsi qimnyygkgk
       61 vritlvtknd pykphphdlv gkdcrdgyye aefgqerrpl ffqnlgircv kkkevkeaii
      121 trikaginpf nvpekqlndi edcdlnvvrl cfqvflpdeh gnlttalppv vsnpiydnra
      181 pntaelricr vnkncgsvrg gdeifllcdk vqkddievrf vlndweakgi fsqadvhrqv
      241 aivfktppyc kaitepvtvk mqlrrpsdqe vsesmdfryl pdekdtygnk akkqkttllf
      301 qklcqdhvnf perprpgllg sigegryfkk epnlfshdav vremptgvss qaesyypspg
      361 pissglshha smaplpsssw ssvahptprs gntnplssfs trtlpsnsqg ippflripvg
      421 ndlnasnaci ynnaddivgm eassmpsadl ygisdpnmls ncsvnmmtts sdsmgetdnp
      481 rllsmnlenp scnsvldprd lrqlhqmsss smsagansnt tvfvsqsdaf egsdfscadn
      541 sminesgpsn stnpnshgfv qdsqysgigs mqneqlsdsf pyeffqv
//
LOCUS       NP_001136068             516 aa            linear   PRI 21-NOV-2025
DEFINITION  prolyl 4-hydroxylase subunit alpha-1 isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_001136068
VERSION     NP_001136068.1
DBSOURCE    REFSEQ: accession NM_001142596.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Gou,W., Song,B. and Yang,Y.
  TITLE     P4HA1 expression and function in esophageal squamous cell carcinoma
  JOURNAL   Medicine (Baltimore) 102 (51), e36800 (2023)
   PUBMED   38134053
  REMARK    GeneRIF: P4HA1 expression and function in esophageal squamous cell
            carcinoma.
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Cao,J., Zhong,Q., Huang,Y., Zhu,M., Wang,Z. and Xiong,Z.
  TITLE     Identification and validation of INHBE and P4HA1 as hub genes in
            non-alcoholic fatty liver disease
  JOURNAL   Biochem Biophys Res Commun 686, 149180 (2023)
   PUBMED   37922570
  REMARK    GeneRIF: Identification and validation of INHBE and P4HA1 as hub
            genes in non-alcoholic fatty liver disease.
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Sato,K., Sano,D., Takahashi,H., Kuwahara,T., Aizawa,Y., Aoyama,J.,
            Nojima,Y., Hatano,T., Arai,Y., Nishimura,G., Hatakeyama,H. and
            Oridate,N.
  TITLE     P4HA1 Promotes Cell Migration and Colonization in Hypopharyngeal
            Squamous Cell Carcinoma
  JOURNAL   Anticancer Res 43 (6), 2571-2582 (2023)
   PUBMED   37247900
  REMARK    GeneRIF: P4HA1 Promotes Cell Migration and Colonization in
            Hypopharyngeal Squamous Cell Carcinoma.
REFERENCE   5  (residues 1 to 516)
  AUTHORS   Zhu,M., Yan,T., Zhu,S., Weng,F., Zhu,K., Wang,C. and Guo,C.
  TITLE     Identification and verification of FN1, P4HA1 and CREBBP as
            potential biomarkers in human atrial fibrillation
  JOURNAL   Math Biosci Eng 20 (4), 6947-6965 (2023)
   PUBMED   37161136
  REMARK    GeneRIF: Identification and verification of FN1, P4HA1 and CREBBP
            as potential biomarkers in human atrial fibrillation.
REFERENCE   6  (residues 1 to 516)
  AUTHORS   Horelli-Kuitunen,N., Kvist,A.P., Helaakoski,T., Kivirikko,K.,
            Pihlajaniemi,T. and Palotie,A.
  TITLE     The order and transcriptional orientation of the human COL13A1 and
            P4HA genes on chromosome 10 long arm determined by high-resolution
            FISH
  JOURNAL   Genomics 46 (2), 299-302 (1997)
   PUBMED   9417920
REFERENCE   7  (residues 1 to 516)
  AUTHORS   Annunen,P., Helaakoski,T., Myllyharju,J., Veijola,J.,
            Pihlajaniemi,T. and Kivirikko,K.I.
  TITLE     Cloning of the human prolyl 4-hydroxylase alpha subunit isoform
            alpha(II) and characterization of the type II enzyme tetramer. The
            alpha(I) and alpha(II) subunits do not form a mixed
            alpha(I)alpha(II)beta2 tetramer
  JOURNAL   J Biol Chem 272 (28), 17342-17348 (1997)
   PUBMED   9211872
REFERENCE   8  (residues 1 to 516)
  AUTHORS   Helaakoski,T., Veijola,J., Vuori,K., Rehn,M., Chow,L.T.,
            Taillon-Miller,P., Kivirikko,K.I. and Pihlajaniemi,T.
  TITLE     Structure and expression of the human gene for the alpha subunit of
            prolyl 4-hydroxylase. The two alternatively spliced types of mRNA
            correspond to two homologous exons the sequences of which are
            expressed in a variety of tissues
  JOURNAL   J Biol Chem 269 (45), 27847-27854 (1994)
   PUBMED   7961714
REFERENCE   9  (residues 1 to 516)
  AUTHORS   Pajunen,L., Jones,T.A., Helaakoski,T., Pihlajaniemi,T., Solomon,E.,
            Sheer,D. and Kivirikko,K.I.
  TITLE     Assignment of the gene coding for the alpha-subunit of prolyl
            4-hydroxylase to human chromosome region 10q21.3-23.1
  JOURNAL   Am J Hum Genet 45 (6), 829-834 (1989)
   PUBMED   2556027
REFERENCE   10 (residues 1 to 516)
  AUTHORS   Helaakoski,T., Vuori,K., Myllyla,R., Kivirikko,K.I. and
            Pihlajaniemi,T.
  TITLE     Molecular cloning of the alpha-subunit of human prolyl
            4-hydroxylase: the complete cDNA-derived amino acid sequence and
            evidence for alternative splicing of RNA transcripts
  JOURNAL   Proc Natl Acad Sci U S A 86 (12), 4392-4396 (1989)
   PUBMED   2543975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB030709.1, CD013929.1 and
            AI061083.1.
            
            Summary: This gene encodes a component of prolyl 4-hydroxylase, a
            key enzyme in collagen synthesis composed of two identical alpha
            subunits and two beta subunits. The encoded protein is one of
            several different types of alpha subunits and provides the major
            part of the catalytic site of the active enzyme. In collagen and
            related proteins, prolyl 4-hydroxylase catalyzes the formation of
            4-hydroxyproline that is essential to the proper three-dimensional
            folding of newly synthesized procollagen chains. Alternatively
            spliced transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (3) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD013929.1, SRR14038195.1796247.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..516
                     /product="prolyl 4-hydroxylase subunit alpha-1 isoform 3
                     precursor"
                     /EC_number="1.14.11.2"
                     /note="C-P4Halpha(I); collagen prolyl 4-hydroxylase
                     alpha(I); procollagen-proline, 2-oxoglutarate
                     4-dioxygenase (proline 4-hydroxylase), alpha polypeptide
                     I; procollagen-proline,2-oxoglutarate-4-dioxygenase
                     subunit alpha-1; prolyl 4-hydroxylase, alpha polypeptide
                     I"
                     /calculated_mol_wt=57019
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1958
     mat_peptide     18..516
                     /product="prolyl 4-hydroxylase subunit alpha-1 isoform 3"
                     /calculated_mol_wt=57019
     Region          24..155
                     /region_name="P4Ha_N"
                     /note="Prolyl 4-Hydroxylase alpha-subunit, N-terminal
                     region; pfam08336"
                     /db_xref="CDD:462433"
     Region          345..500
                     /region_name="P4Hc"
                     /note="Prolyl 4-hydroxylase alpha subunit homologues;
                     smart00702"
                     /db_xref="CDD:214780"
     CDS             1..516
                     /gene="P4HA1"
                     /gene_synonym="P4HA"
                     /coded_by="NM_001142596.2:134..1684"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS44432.1"
                     /db_xref="GeneID:5033"
                     /db_xref="HGNC:HGNC:8546"
                     /db_xref="MIM:176710"
ORIGIN      
        1 miwyiliigi llpqslahpg fftsigqmtd lihtekdlvt slkdyikaee dkleqikkwa
       61 ekldrltsta tkdpegfvgh pvnafklmkr lntewselen lvlkdmsdgf isnltiqrqy
      121 fpndedqvga akallrlqdt ynldtdtisk gnlpgvkhks fltaedcfel gkvayteady
      181 yhtelwmeqa lrqldegeis tidkvsvldy lsyavyqqgd ldkallltkk lleldpehqr
      241 angnlkyfey imakekdvnk sasddqsdqk ttpkkkgvav dylperqkye mlcrgegikm
      301 tprrqkklfc ryhdgnrnpk filapakqed ewdkpriirf hdiisdaeie ivkdlakprl
      361 sratvhdpet gklttaqyrv sksawlsgye npvvsrinmr iqdltgldvs taeelqkdep
      421 dafkelgtgn riatwlfyms dvsaggatvf pevgasvwpk kgtavfwynl fasgegdyst
      481 rhaacpvlvg nkwvsnkwlh ergqefrrpc tlsele
//
LOCUS       NP_258441                437 aa            linear   PRI 21-NOV-2025
DEFINITION  F-box only protein 9 isoform 2 [Homo sapiens].
ACCESSION   NP_258441
VERSION     NP_258441.1
DBSOURCE    REFSEQ: accession NM_033480.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Hussain,S., Dong,J., Ma,X., Li,J., Chen,S., Clement,A. and Liu,H.
  TITLE     F-box only protein 9 and its role in cancer
  JOURNAL   Mol Biol Rep 49 (2), 1537-1544 (2022)
   PUBMED   35025031
  REMARK    GeneRIF: F-box only protein 9 and its role in cancer.
            Review article
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Lai,Y., Li,X., Li,T., Nyunoya,T., Chen,K., Kitsios,G.D.,
            Nouraie,S.M., Zhang,Y., McVerry,B.J., Lee,J.S., Mallampalli,R.K.
            and Zou,C.
  TITLE     Endotoxin stabilizes protein arginine methyltransferase 4 (PRMT4)
            protein triggering death of lung epithelia
  JOURNAL   Cell Death Dis 12 (9), 828 (2021)
   PUBMED   34480022
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 437)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 437)
  AUTHORS   Yada,M., Hatakeyama,S., Kamura,T., Nishiyama,M., Tsunematsu,R.,
            Imaki,H., Ishida,N., Okumura,F., Nakayama,K. and Nakayama,K.I.
  TITLE     Phosphorylation-dependent degradation of c-Myc is mediated by the
            F-box protein Fbw7
  JOURNAL   EMBO J 23 (10), 2116-2125 (2004)
   PUBMED   15103331
REFERENCE   7  (residues 1 to 437)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   8  (residues 1 to 437)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   9  (residues 1 to 437)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   10 (residues 1 to 437)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031178.1 and AL137520.1.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            the ubiquitin protein ligase complex called SCFs
            (SKP1-cullin-F-box), which function in phosphorylation-dependent
            ubiquitination. The F-box proteins are divided into 3 classes: Fbws
            containing WD-40 domains, Fbls containing leucine-rich repeats, and
            Fbxs containing either different protein-protein interaction
            modules or no recognizable motifs. The protein encoded by this gene
            belongs to the Fbxs class. Alternative splicing of this gene
            generates at least 3 transcript variants diverging at the 5'
            terminus. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) contains a different segment
            for the 5' UTR and 5' coding region, compared to variant 1. It uses
            a different translation start codon and the encoded protein
            (isoform 2) has a shorter and distinct N-terminus when it is
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL137520.1, AY858798.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323557.12/ ENSP00000326968.7
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.1"
     Protein         1..437
                     /product="F-box only protein 9 isoform 2"
                     /note="F-box protein Fbx9; F-box only protein 9;
                     cross-immune reaction antigen 1; renal carcinoma antigen
                     NY-REN-57"
                     /calculated_mol_wt=51005
     Region          82..>113
                     /region_name="MIT"
                     /note="MIT (microtubule interacting and transport) domain;
                     pfam04212"
                     /db_xref="CDD:461228"
     Region          176..229
                     /region_name="F-box_FBXO9"
                     /note="F-box domain found in F-box only protein 9 (FBXO9)
                     and similar proteins; cd22089"
                     /db_xref="CDD:438861"
     Site            order(181,185,188..189,192..193,202,204..205,209..211,213)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438861"
     Region          243..>335
                     /region_name="FBO_C"
                     /note="F-box only protein C-terminal region; pfam19270"
                     /db_xref="CDD:466021"
     CDS             1..437
                     /gene="FBXO9"
                     /gene_synonym="dJ341E18.2; FBX9; NY-REN-57; VCIA1"
                     /coded_by="NM_033480.3:387..1700"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55022.1"
                     /db_xref="GeneID:26268"
                     /db_xref="HGNC:HGNC:13588"
                     /db_xref="MIM:609091"
ORIGIN      
        1 maeaeedchs dtvradddee nespaetdlq aqlqmfraqw mfelapgvss snlenrpcra
       61 argslqktsa dtkgkqeqak eekarelflk aveeeqngal yeaikfyrra mqlvpdiefk
      121 itytrspdgd gvgnsyiedn dddskmadll syfqqqltfq esvlklcqpe lessqihisv
      181 lpmevlmyif rwvvssdldl rsleqlslvc rgfyicardp eiwrlaclkv wgrsciklvp
      241 ytswremfle rprvrfdgvy iskttyirqg eqsldgfyra whqveyyryi rffpdghvmm
      301 lttpeepqsi vprlrtrntr tdaillghyr lsqdtdnqtk vfavitkkke ekpldykyry
      361 frrvpvqead qsfhvglqlc ssghqrfnkl iwihhschit ykstgetavs afeidkmytp
      421 lffarvrsyt afserpl
//
LOCUS       NP_001374257            2645 aa            linear   PRI 21-NOV-2025
DEFINITION  protein TASOR 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001374257
VERSION     NP_001374257.1
DBSOURCE    REFSEQ: accession NM_001387328.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2645)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2645)
  AUTHORS   Jensvold,Z.D., Flood,J.R., Christenson,A.E. and Lewis,P.W.
  TITLE     Interplay between Two Paralogous Human Silencing Hub (HuSH)
            Complexes in Regulating LINE-1 Element Silencing
  JOURNAL   Nat Commun 15 (1), 9492 (2024)
   PUBMED   39489739
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2645)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   4  (residues 1 to 2645)
  AUTHORS   Krishnamoorthy,V., Foglizzo,M., Dilley,R.L., Wu,A., Datta,A.,
            Dutta,P., Campbell,L.J., Degtjarik,O., Musgrove,L.J.,
            Calabrese,A.N., Zeqiraj,E. and Greenberg,R.A.
  TITLE     The SPATA5-SPATA5L1 ATPase complex directs replisome proteostasis
            to ensure genome integrity
  JOURNAL   Cell 187 (9), 2250-2268 (2024)
   PUBMED   38554706
REFERENCE   5  (residues 1 to 2645)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 2645)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   7  (residues 1 to 2645)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   8  (residues 1 to 2645)
  AUTHORS   Savage,S.A., Mirabello,L., Wang,Z., Gastier-Foster,J.M.,
            Gorlick,R., Khanna,C., Flanagan,A.M., Tirabosco,R., Andrulis,I.L.,
            Wunder,J.S., Gokgoz,N., Patino-Garcia,A., Sierrasesumaga,L.,
            Lecanda,F., Kurucu,N., Ilhan,I.E., Sari,N., Serra,M., Hattinger,C.,
            Picci,P., Spector,L.G., Barkauskas,D.A., Marina,N., de Toledo,S.R.,
            Petrilli,A.S., Amary,M.F., Halai,D., Thomas,D.M., Douglass,C.,
            Meltzer,P.S., Jacobs,K., Chung,C.C., Berndt,S.I., Purdue,M.P.,
            Caporaso,N.E., Tucker,M., Rothman,N., Landi,M.T., Silverman,D.T.,
            Kraft,P., Hunter,D.J., Malats,N., Kogevinas,M., Wacholder,S.,
            Troisi,R., Helman,L., Fraumeni,J.F. Jr., Yeager,M., Hoover,R.N. and
            Chanock,S.J.
  TITLE     Genome-wide association study identifies two susceptibility loci
            for osteosarcoma
  JOURNAL   Nat Genet 45 (7), 799-803 (2013)
   PUBMED   23727862
REFERENCE   9  (residues 1 to 2645)
  AUTHORS   Oshikawa,M., Tsutsui,C., Ikegami,T., Fuchida,Y., Matsubara,M.,
            Toyama,S., Usami,R., Ohtoko,K. and Kato,S.
  TITLE     Full-length transcriptome analysis of human retina-derived cell
            lines ARPE-19 and Y79 using the vector-capping method
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6662-6670 (2011)
   PUBMED   21697133
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 2645)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL365356.13 and AL596094.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2110756.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2645
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p15.1"
     Protein         1..2645
                     /product="protein TASOR 2 isoform 3"
                     /note="protein FAM208B; family with sequence similarity
                     208 member B; protein TASOR 2"
                     /calculated_mol_wt=293419
     Region          102..202
                     /region_name="DUF3715"
                     /note="Protein of unknown function (DUF3715); pfam12509"
                     /db_xref="CDD:463613"
     Region          309..382
                     /region_name="DUF3699"
                     /note="Protein of unknown function (DUF3699); pfam12480"
                     /db_xref="CDD:463601"
     Region          767..916
                     /region_name="DUF3715"
                     /note="Protein of unknown function (DUF3715); pfam12509"
                     /db_xref="CDD:463613"
     CDS             1..2645
                     /gene="TASOR2"
                     /gene_synonym="bA318E3.2; C10orf18; FAM208B"
                     /coded_by="NM_001387328.1:117..8054"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS91208.1"
                     /db_xref="GeneID:54906"
                     /db_xref="HGNC:HGNC:23484"
                     /db_xref="MIM:621243"
ORIGIN      
        1 msiydinreq dyvknsegil genelrppsq lhsllekiet gslsekifet vslssdslfq
       61 ravsllhtsy ldsssehgfq ysqvtlvknd iflneyktfy qqkkassytq eelqdtygfl
      121 lfdtekqakl vcqcglrvgs savttlgdpa kgvyiskysd clhsrpwyhg ksgyvvifni
      181 ikyyfyelsg ntvierprqi cpyvivafry resktmappa hksilersen vlmspwkgkl
      241 ivqdrmlcdi alwstygami ptqlpqeldf kyvmkvsslk krlpeaafrk qnyleekvcf
      301 qdlcfnlyev elsnrqgeni dklteciknk qlaiikcled rgffilltss allsepdfgg
      361 kqmglhglhl frsplstgvk dlkveddism kvipilstln calletkksl peerihpntl
      421 vkrhfqelyk adrspslsva pqdrmkdptf lgklpsgfdl ippaekcpse sltqlnsyfs
      481 dpsayilevs taldllaehp qspcvsdgic dagfslvmtp dpeflvseae vrketetkkd
      541 seemlkakkr vfplspasnl rvqpkrkasm phmvqskkvn lcrpfpkrta sradnssdsp
      601 ttlklvkgqf pqkrkrgaev ltaqfvqktk ldrknqeapi skdvpvptna krarkqeksp
      661 vktvprakpp vkkspqkqrv nivkgnenpr nrkqlqpvkg etasklqsei srgcqedgis
      721 insvqpentt aahndlpens ivnydsqaln mladlalssa tsstpvsear nlhcsselpq
      781 ndvllskens lrgtsdheyh rgvktqkgel lpnpssdrks nsgsdltvsq deeslvpcsq
      841 apakaqsalt eemlessdas qsssvsvehs yallltehsk khlqereils plfprngtks
      901 peaatpvgkv mpfrhqpgll lqqkppddpv vkpkdrppsa rvkksscsri vlscddsvki
      961 tfkceteyaf sldskytnnp lektvvralh gpwntdlpdn veevklllhm wvalfysnqn
     1021 kiirssrkvv ehsnpakyvs instlescel reieeslgle kcsadsllet neisrahaae
     1081 vsfrdpncll pfiktpltqg lelcvqneqk ktfarecdpd tqedqnfics ynnevtgeea
     1141 kqesletsnl vlsgigstqt ngpsvpseee ivqpldstrv asysgtvtqa tftrtydgpg
     1201 sqpvicqssv ygtlenkvdi ldaavqtktg tlqdliqhgs pinnechpsl erkddnmgca
     1261 vinpepitlt feknahvpiq tegvntader ttfkkelikq vspaaslrhp vstsenartq
     1321 glrdipslvv agqkgtkylc assvggetld kavcslqket plpvslpsdk tmvmealsla
     1381 kssshlspse evrctqdfls qtqsllglss eglleltqve vdsssasttl grqcslncis
     1441 sgchtsgdsl elrknhkngp ntenmnleaf dsvfikqtsl svsrevslel seedsdidla
     1501 ltispptspr eempageieq feeapfsnle lqdvaeeige peevaltesr evssadnvsv
     1561 ypsvseepve nkerkgdnlq pvtlilsken ctleiaeein vtsdfpfdsv ieevspassp
     1621 eppvpvketr pyqavtpcil klhgtqceks nqisqcesed lgitekenvf vgpthpvgqd
     1681 nftqvqqmqv saempliltd hpgrtgrptl pgkvteeivs sehdeglsfs gkvqcygrel
     1741 nqpasaakct gdfspspekl vksgnplqpv sienrnldlk hlvlessepp fgprnvienk
     1801 slsdtlvstt apsgivnvsv kqqtspkssq nhlfpgdlkt degiylqvks ltaasvdgay
     1861 stqgcmcsvv ptlcsssdna tlthyvrpin aepvfqaqei pagrmasllk ngepeaelhk
     1921 ettgpgtagp qsnttsslkg erkaihtlqd vstcetkell nvgvsslcag pyqntadtke
     1981 nlskeplasf vsesfdtsvc giatehveie nsgeglraea gsetlgrdge vgvnsdmhye
     2041 lsgdsdldll gdcrnprldl edsytlrgsy trkkdvptdg yesslnfhnn nqedwgcssw
     2101 vpgmetslpp ghwtaavkke ekcvppyvqi rdlhgilrty anfsitkelk dtmrtshglr
     2161 rhpsfsancg lpsswtstwq vaddltqntl dleylrfahk lkqtikngds qhsassanvf
     2221 pkesptqisi gafpstkise apflhpaprs rspllvtvve sdprpqgqpr rgytasslds
     2281 ssswrercsh nrdlrnsqrn htvsfhlnkl kynstvkesr ndislilney aefnkvmkns
     2341 nqfifqdkel ndvsgeataq emylpfpgrs asyediiidv ctnlhvklrs vvkeackstf
     2401 lfylvetedk sffvrtknll rkgghteiep qhfcqafhre ndtliiiirn edisshlhqi
     2461 psllklkhfp svifagvdsp gdvldhtyqe lfraggfvis ddkileavtl vqlkeiikil
     2521 eklngngrwk wllhyrenkk lkedervdst ahkknimlks fqsaniiell hyhqcdsrss
     2581 tkaeilkcll nlqiqhidar favlltdkpt iprevfensg ilvtdvnnfi eniekiaapf
     2641 rssyw
//
LOCUS       NP_001171504             176 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger C4H2 domain-containing protein isoform 3 [Homo
            sapiens].
ACCESSION   NP_001171504
VERSION     NP_001171504.1
DBSOURCE    REFSEQ: accession NM_001178033.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Wongkittichote,P., Choi,T.I., Kim,O.H., Riley,K., Koeberl,D.,
            Narayanan,V., Ramsey,K., Balak,C., Schwartz,C.E.,
            Cueto-Gonzalez,A.M., Casadesus,F.M., Kim,C.H. and Shinawi,M.S.
  TITLE     Expanding allelic and phenotypic spectrum of ZC4H2-related
            disorder: A novel hypomorphic variant and high prevalence of
            tethered cord
  JOURNAL   Clin Genet 103 (2), 167-178 (2023)
   PUBMED   36250278
  REMARK    GeneRIF: Expanding allelic and phenotypic spectrum of ZC4H2-related
            disorder: A novel hypomorphic variant and high prevalence of
            tethered cord.
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Li,Y., Yang,C., Wang,H., Zhao,L., Kong,Q., Cang,Y., Zhao,S., Lv,L.,
            Li,Y., Mao,B. and Ma,P.
  TITLE     Sequential stabilization of RNF220 by RLIM and ZC4H2 during
            cerebellum development and Shh-group medulloblastoma progression
  JOURNAL   J Mol Cell Biol 14 (1) (2022)
   PUBMED   35040952
  REMARK    GeneRIF: Sequential stabilization of RNF220 by RLIM and ZC4H2
            during cerebellum development and Shh-group medulloblastoma
            progression.
            Erratum:[J Mol Cell Biol. 2022 May 25;14(2):mjac030. doi:
            10.1093/jmcb/mjac030. PMID: 35639540]
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 176)
  AUTHORS   Lombard,Z., Park,C., Makova,K.D. and Ramsay,M.
  TITLE     A computational approach to candidate gene prioritization for
            X-linked mental retardation using annotation-based binary filtering
            and motif-based linear discriminatory analysis
  JOURNAL   Biol Direct 6, 30 (2011)
   PUBMED   21668950
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 176)
  AUTHORS   Kroncke,K.D. and Klotz,L.O.
  TITLE     Zinc fingers as biologic redox switches?
  JOURNAL   Antioxid Redox Signal 11 (5), 1015-1027 (2009)
   PUBMED   19132878
  REMARK    Review article
REFERENCE   7  (residues 1 to 176)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   8  (residues 1 to 176)
  AUTHORS   Wang,Y., Han,K.J., Pang,X.W., Vaughan,H.A., Qu,W., Dong,X.Y.,
            Peng,J.R., Zhao,H.T., Rui,J.A., Leng,X.S., Cebon,J., Burgess,A.W.
            and Chen,W.F.
  TITLE     Large scale identification of human hepatocellular
            carcinoma-associated antigens by autoantibodies
  JOURNAL   J Immunol 169 (2), 1102-1109 (2002)
   PUBMED   12097419
REFERENCE   9  (residues 1 to 176)
  AUTHORS   Mulley,J.C., Kerr,B., Stevenson,R. and Lubs,H.
  TITLE     Nomenclature guidelines for X-linked mental retardation
  JOURNAL   Am J Med Genet 43 (1-2), 383-391 (1992)
   PUBMED   1605216
  REMARK    Review article
REFERENCE   10 (residues 1 to 176)
  AUTHORS   Miles,J.H. and Carpenter,N.J.
  TITLE     Unique X-linked mental retardation syndrome with fingertip arches
            and contractures linked to Xq21.31
  JOURNAL   Am J Med Genet 38 (2-3), 215-223 (1991)
   PUBMED   2018061
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK293570.1 and AK001547.1.
            
            Summary: This gene encodes a member of the zinc finger
            domain-containing protein family. This family member has a
            C-terminal zinc finger domain that is characterized by four
            cysteine residues and two histidine residues, and it also includes
            a coiled-coil region. This protein has been detected as an
            autoantigen in hepatocellular carcinoma patients. This gene has
            been identified as a potential candidate for X-linked cognitive
            disability. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (3) lacks an alternate exon in the
            3' coding region that results in a frameshift, compared to variant
            1. The resulting isoform (3) has a distinct C-terminus and is
            shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293570.1, DC303870.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq11.2"
     Protein         1..176
                     /product="zinc finger C4H2 domain-containing protein
                     isoform 3"
                     /note="hepatocellular carcinoma-associated antigen 127;
                     zinc finger C4H2 domain-containing protein; zinc finger,
                     C4H2 domain containing"
                     /calculated_mol_wt=20512
     Region          13..>130
                     /region_name="zf-C4H2"
                     /note="Zinc finger-containing protein; pfam10146"
                     /db_xref="CDD:462963"
     CDS             1..176
                     /gene="ZC4H2"
                     /gene_synonym="HCA127; KIAA1166; MCS; MRXS4; WRWF; WRWFFR;
                     WWS"
                     /coded_by="NM_001178033.3:74..604"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55432.1"
                     /db_xref="GeneID:55906"
                     /db_xref="HGNC:HGNC:24931"
                     /db_xref="MIM:300897"
ORIGIN      
        1 madeqeimck lesikeirnk tlqmekikar lkaefeales eerhlkeykq emdlllqekm
       61 ahveelrlih adinvmenti kqsendlnkl lestrrlhde ykplkehvda lrmtlglqrl
      121 pdlceeeekl slepachvts kftgmhlyal farprvgpgt pksrngsrmn kerest
//
LOCUS       NP_148982                130 aa            linear   PRI 21-NOV-2025
DEFINITION  small ribosomal subunit protein eS24 isoform a [Homo sapiens].
ACCESSION   NP_148982
VERSION     NP_148982.1
DBSOURCE    REFSEQ: accession NM_033022.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Park,J., Nam,D.H., Kim,D. and Chung,Y.J.
  TITLE     RPS24 alternative splicing is a marker of cancer progression and
            epithelial-mesenchymal transition
  JOURNAL   Sci Rep 14 (1), 13246 (2024)
   PUBMED   38853173
  REMARK    GeneRIF: RPS24 alternative splicing is a marker of cancer
            progression and epithelial-mesenchymal transition.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Kerry,J., Specker,E.J., Mizzoni,M., Brumwell,A., Fell,L.,
            Goodbrand,J., Rosen,M.N. and Uniacke,J.
  TITLE     Autophagy-dependent alternative splicing of ribosomal protein S24
            produces a more stable isoform that aids in hypoxic cell survival
  JOURNAL   FEBS Lett 598 (5), 503-520 (2024)
   PUBMED   38281767
  REMARK    GeneRIF: Autophagy-dependent alternative splicing of ribosomal
            protein S24 produces a more stable isoform that aids in hypoxic
            cell survival.
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Wang,S., Xia,L., Zhang,B., Zhang,H. and Lan,F.
  TITLE     Downregulated long intergenic non-coding RNA 00,174 represses
            malignant biological behaviors of lung cancer cells by regulating
            microRNA-584-3p/ribosomal protein S24 axis
  JOURNAL   Funct Integr Genomics 22 (4), 643-653 (2022)
   PUBMED   35451652
  REMARK    GeneRIF: Downregulated long intergenic non-coding RNA 00,174
            represses malignant biological behaviors of lung cancer cells by
            regulating microRNA-584-3p/ribosomal protein S24 axis.
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Kennedy,S.A., Jarboui,M.A., Srihari,S., Raso,C., Bryan,K.,
            Dernayka,L., Charitou,T., Bernal-Llinares,M., Herrera-Montavez,C.,
            Krstic,A., Matallanas,D., Kotlyar,M., Jurisica,I., Curak,J.,
            Wong,V., Stagljar,I., LeBihan,T., Imrie,L., Pillai,P., Lynn,M.A.,
            Fasterius,E., Al-Khalili Szigyarto,C., Breen,J., Kiel,C.,
            Serrano,L., Rauch,N., Rukhlenko,O., Kholodenko,B.N.,
            Iglesias-Martinez,L.F., Ryan,C.J., Pilkington,R., Cammareri,P.,
            Sansom,O., Shave,S., Auer,M., Horn,N., Klose,F., Ueffing,M.,
            Boldt,K., Lynn,D.J. and Kolch,W.
  TITLE     Extensive rewiring of the EGFR network in colorectal cancer cells
            expressing transforming levels of KRASG13D
  JOURNAL   Nat Commun 11 (1), 499 (2020)
   PUBMED   31980649
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 130)
  AUTHORS   Xu,W.B. and Roufa,D.J.
  TITLE     The gene encoding human ribosomal protein S24 and tissue-specific
            expression of differentially spliced mRNAs
  JOURNAL   Gene 169 (2), 257-262 (1996)
   PUBMED   8647458
REFERENCE   7  (residues 1 to 130)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   8  (residues 1 to 130)
  AUTHORS   Sieff,C.
  TITLE     DBA Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301769
REFERENCE   9  (residues 1 to 130)
  AUTHORS   Huang,R.T., Li,D.R., Wei,J., Huang,X.R., Yuan,X.T. and Tian,X.
  TITLE     Isolation and identification of hepatitis E virus in Xinjiang,
            China
  JOURNAL   J Gen Virol 73 (Pt 5), 1143-1148 (1992)
   PUBMED   1588318
REFERENCE   10 (residues 1 to 130)
  AUTHORS   Brown,S.J., Jewell,A., Maki,C.G. and Roufa,D.J.
  TITLE     A cDNA encoding human ribosomal protein S24
  JOURNAL   Gene 91 (2), 293-296 (1990)
   PUBMED   2210388
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BG944046.1 and BC071926.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 40S subunit. The protein belongs
            to the S24E family of ribosomal proteins. It is located in the
            cytoplasm. Multiple transcript variants encoding different isoforms
            have been found for this gene. As is typical for genes encoding
            ribosomal proteins, there are multiple processed pseudogenes of
            this gene dispersed through the genome. Mutations in this gene
            result in Diamond-Blackfan anemia. [provided by RefSeq, Nov 2008].
            
            Transcript Variant: This variant (a) uses an alternate splice
            pattern in the 3' coding region, compared to variant d. The
            resulting protein (isoform a) has a shorter and distinct
            C-terminus, compared to isoform d.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB121452.1, DB075119.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372360.9/ ENSP00000361435.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.3"
     Protein         1..130
                     /product="small ribosomal subunit protein eS24 isoform a"
                     /note="40S ribosomal protein S24; small ribosomal subunit
                     protein eS24"
                     /calculated_mol_wt=14938
     Region          1..130
                     /region_name="PTZ00071"
                     /note="40S ribosomal protein S24; Provisional"
                     /db_xref="CDD:240256"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P62847.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P62847.1)"
     CDS             1..130
                     /gene="RPS24"
                     /gene_synonym="DBA3; eS24; S24"
                     /coded_by="NM_033022.4:40..432"
                     /note="isoform a is encoded by transcript variant a"
                     /db_xref="CCDS:CCDS7356.1"
                     /db_xref="GeneID:6229"
                     /db_xref="HGNC:HGNC:10411"
                     /db_xref="MIM:602412"
ORIGIN      
        1 mndtvtirtr kfmtnrllqr kqmvidvlhp gkatvpktei reklakmykt tpdvifvfgf
       61 rthfgggktt gfgmiydsld yakknepkhr larhglyekk ktsrkqrker knrmkkvrgt
      121 akanvgagkk
//
LOCUS       NP_001374643            1038 aa            linear   PRI 21-NOV-2025
DEFINITION  activated CDC42 kinase 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001374643
VERSION     NP_001374643.1
DBSOURCE    REFSEQ: accession NM_001387714.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1038)
  AUTHORS   Zheng,D., Wei,Z., Zhang,C., Liu,W., Gong,C., Wu,F. and Guo,W.
  TITLE     ZNF692 promotes osteosarcoma cell proliferation, migration, and
            invasion through TNK2-mediated activation of the MEK/ERK pathway
  JOURNAL   Biol Direct 19 (1), 28 (2024)
   PUBMED   38650011
  REMARK    GeneRIF: ZNF692 promotes osteosarcoma cell proliferation,
            migration, and invasion through TNK2-mediated activation of the
            MEK/ERK pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1038)
  AUTHORS   Hodder,S., Fox,M., Binti Ahmad Mokhtar,A.M., Mott,H.R. and Owen,D.
  TITLE     ACKnowledging the role of the Activated-Cdc42 associated kinase
            (ACK) in regulating protein stability in cancer
  JOURNAL   Small GTPases 14 (1), 14-25 (2023)
   PUBMED   37194323
  REMARK    GeneRIF: ACKnowledging the role of the Activated-Cdc42 associated
            kinase (ACK) in regulating protein stability in cancer.
            Review article
REFERENCE   4  (residues 1 to 1038)
  AUTHORS   Zhou,A., Zhang,W. and Wang,B.
  TITLE     Host factor TNK2 is required for influenza virus infection
  JOURNAL   Genes Genomics 45 (6), 771-781 (2023)
   PUBMED   37133719
  REMARK    GeneRIF: Host factor TNK2 is required for influenza virus
            infection.
REFERENCE   5  (residues 1 to 1038)
  AUTHORS   Kan,Y., Paung,Y., Seeliger,M.A. and Miller,W.T.
  TITLE     Domain Architecture of the Nonreceptor Tyrosine Kinase Ack1
  JOURNAL   Cells 12 (6), 900 (2023)
   PUBMED   36980241
  REMARK    GeneRIF: Domain Architecture of the Nonreceptor Tyrosine Kinase
            Ack1.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1038)
  AUTHORS   Kato,J., Kaziro,Y. and Satoh,T.
  TITLE     Activation of the guanine nucleotide exchange factor Dbl following
            ACK1-dependent tyrosine phosphorylation
  JOURNAL   Biochem Biophys Res Commun 268 (1), 141-147 (2000)
   PUBMED   10652228
REFERENCE   7  (residues 1 to 1038)
  AUTHORS   Eisenmann,K.M., McCarthy,J.B., Simpson,M.A., Keely,P.J., Guan,J.L.,
            Tachibana,K., Lim,L., Manser,E., Furcht,L.T. and Iida,J.
  TITLE     Melanoma chondroitin sulphate proteoglycan regulates cell spreading
            through Cdc42, Ack-1 and p130cas
  JOURNAL   Nat Cell Biol 1 (8), 507-513 (1999)
   PUBMED   10587647
REFERENCE   8  (residues 1 to 1038)
  AUTHORS   Mott,H.R., Owen,D., Nietlispach,D., Lowe,P.N., Manser,E., Lim,L.
            and Laue,E.D.
  TITLE     Structure of the small G protein Cdc42 bound to the GTPase-binding
            domain of ACK
  JOURNAL   Nature 399 (6734), 384-388 (1999)
   PUBMED   10360579
REFERENCE   9  (residues 1 to 1038)
  AUTHORS   Satoh,T., Kato,J., Nishida,K. and Kaziro,Y.
  TITLE     Tyrosine phosphorylation of ACK in response to temperature
            shift-down, hyperosmotic shock, and epidermal growth factor
            stimulation
  JOURNAL   FEBS Lett 386 (2-3), 230-234 (1996)
   PUBMED   8647288
REFERENCE   10 (residues 1 to 1038)
  AUTHORS   Manser,E., Leung,T., Salihuddin,H., Tan,L. and Lim,L.
  TITLE     A non-receptor tyrosine kinase that inhibits the GTPase activity of
            p21cdc42
  JOURNAL   Nature 363 (6427), 364-367 (1993)
   PUBMED   8497321
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124944.8.
            
            Summary: This gene encodes a tyrosine kinase that binds Cdc42Hs in
            its GTP-bound form and inhibits both the intrinsic and
            GTPase-activating protein (GAP)-stimulated GTPase activity of
            Cdc42Hs. This binding is mediated by a unique sequence of 47 amino
            acids C-terminal to an SH3 domain. The protein may be involved in a
            regulatory mechanism that sustains the GTP-bound active form of
            Cdc42Hs and which is directly linked to a tyrosine phosphorylation
            signal transduction pathway. Several alternatively spliced
            transcript variants have been identified from this gene, but the
            full-length nature of only two transcript variants has been
            determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14372080.2651624.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..1038
                     /product="activated CDC42 kinase 1 isoform 1"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="activated p21cdc42Hs kinase; activated
                     Cdc42-associated kinase 1; tyrosine kinase non-receptor
                     protein 2"
                     /calculated_mol_wt=114438
     Region          1..110
                     /region_name="SAM-like domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          6..67
                     /region_name="SAM_TNK-like"
                     /note="SAM domain of TNK(ACK)-like non-receptor
                     tyrosine-protein kinases; cd09539"
                     /db_xref="CDD:188938"
     Region          90..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          130..387
                     /region_name="PTKc_Ack_like"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Activated Cdc42-associated kinase; cd05040"
                     /db_xref="CDD:270636"
     Site            order(132..134,140,156,158,205..208,212,252,256..257,259,
                     270,289..293,302,336)
                     /site_type="active"
                     /db_xref="CDD:270636"
     Site            order(132..134,140,156,158,205..208,212,252,256..257,259,
                     270)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270636"
     Site            order(252,256,289..293,302,336)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270636"
     Site            order(269..279,281..295)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270636"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000269|PubMed:15308621,
                     ECO:0000269|PubMed:16472662, ECO:0000269|PubMed:20333297,
                     ECO:0000269|PubMed:20623637, ECO:0000269|PubMed:20979614,
                     ECO:0000269|PubMed:21169560, ECO:0000269|PubMed:21309750,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Region          395..444
                     /region_name="SH3_9"
                     /note="Variant SH3 domain; pfam14604"
                     /db_xref="CDD:434066"
     Site            order(397,399,404,422,424,439,441..442)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          449..514
                     /region_name="GTPase_binding"
                     /note="GTPase binding; pfam09027"
                     /db_xref="CDD:430374"
     Region          497..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:21169560; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Region          <543..849
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          623..652
                     /region_name="Required for interaction with SRC.
                     /evidence=ECO:0000269|PubMed:21309750"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          632..635
                     /region_name="Required for interaction with NEDD4.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          659..702
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          718..840
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Site            724
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Region          733..876
                     /region_name="EBD domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          774..840
                     /region_name="Inhibitor_Mig-6"
                     /note="EGFR receptor inhibitor Mig-6; pfam11555"
                     /db_xref="CDD:463294"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:21169560; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Site            839
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O54967; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Site            859
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:21169560; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Site            872
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:21169560; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Site            881
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Region          917..957
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          958..1002
                     /region_name="UBA_ACK1"
                     /note="UBA domain found in activated Cdc42 kinase 1 (ACK1)
                     and similar proteins; cd14274"
                     /db_xref="CDD:270460"
     Region          989..1028
                     /region_name="UBA_TNK1"
                     /note="UBA domain found in non-receptor tyrosine-protein
                     kinase TNK1 and similar proteins; cd14328"
                     /db_xref="CDD:270513"
     CDS             1..1038
                     /gene="TNK2"
                     /gene_synonym="ACK; ACK-1; ACK1; p21cdc42Hs"
                     /coded_by="NM_001387714.1:144..3260"
                     /note="isoform 1 is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS33928.1"
                     /db_xref="GeneID:10188"
                     /db_xref="HGNC:HGNC:19297"
                     /db_xref="MIM:606994"
ORIGIN      
        1 mqpeegtgwl lellsevqlq qyflrlrddl nvtrlshfey vknedlekig mgrpgqrrlw
       61 eavkrrkalc krkswmskvf sgkrleaefp phhsqstfrk tspapggpag egplqsltcl
      121 igekdlrlle klgdgsfgvv rrgewdapsg ktvsvavkcl kpdvlsqpea mddfirevna
      181 mhsldhrnli rlygvvltpp mkmvtelapl gslldrlrkh qghfllgtls ryavqvaegm
      241 gyleskrfih rdlaarnlll atrdlvkigd fglmralpqn ddhyvmqehr kvpfawcape
      301 slktrtfsha sdtwmfgvtl wemftygqep wiglngsqil hkidkegerl prpedcpqdi
      361 ynvmvqcwah kpedrptfva lrdflleaqp tdmralqdfe epdklhiqmn dvitviegra
      421 enywwrgqnt rtlcvgpfpr nvvtsvagls aqdisqplqn sfihtghgds dprhcwgfpd
      481 ridelylgnp mdppdllsve lstsrppqhl ggvkkptydp vsedqdplss dfkrlglrkp
      541 glprglwlak psarvpgtka srgsgaevtl idfgeepvvp alrpcapsla qlamdacsll
      601 detppqsptr alprplhptp vvdwdarplp pppayddvaq deddfeicsi nstlvgagvp
      661 agpsqgqtny afvpeqarpp pplednlflp pqgggkppss aqtaeifqal qqecmrqlqa
      721 pagspapsps pggddkpqvp prvpipprpt rphvqlspap pgeeetsqwp gpaspprvpp
      781 replspqgsr tpsplvppgs splpprlsss pgktmpttqs fasdpkyatp qviqapgpra
      841 gpcilpivrd gkkvssthyy llperpsyle ryqrflreaq speeptplpv plllpppstp
      901 apaaptatvr pmpqaaldpk anfstnnsnp garpppprat arlpqrgcpg dgpeagrpad
      961 kiqmamvhgv tteecqaalq chgwsvqraa qylkveqlfg lglrprgech kvlemfdwnl
     1021 eqagchllgs wgpahhkr
//
LOCUS       NP_001036041             977 aa            linear   PRI 21-NOV-2025
DEFINITION  ribosome-binding protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001036041
VERSION     NP_001036041.2
DBSOURCE    REFSEQ: accession NM_001042576.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Chiu,C.H., Hsuan,C.F., Lin,S.H., Hung,Y.J., Hwu,C.M., Hee,S.W.,
            Lin,S.W., Fong,S.W., Hsieh,P.C., Yang,W.S., Lin,W.C., Lee,H.L.,
            Hsieh,M.L., Li,W.Y., Lin,J.W., Hsu,C.N., Wu,V.C., Chuang,G.T.,
            Chang,Y.C. and Chuang,L.M.
  TITLE     ER ribosomal-binding protein 1 regulates blood pressure and
            potassium homeostasis by modulating intracellular renin trafficking
  JOURNAL   J Biomed Sci 30 (1), 13 (2023)
   PUBMED   36803854
  REMARK    GeneRIF: ER ribosomal-binding protein 1 regulates blood pressure
            and potassium homeostasis by modulating intracellular renin
            trafficking.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 977)
  AUTHORS   Luo,H.L., Liu,H.Y., Chang,Y.L., Sung,M.T., Chen,P.Y., Su,Y.L.,
            Huang,C.C. and Peng,J.M.
  TITLE     Hypomethylated RRBP1 Potentiates Tumor Malignancy and
            Chemoresistance in Upper Tract Urothelial Carcinoma
  JOURNAL   Int J Mol Sci 22 (16), 8761 (2021)
   PUBMED   34445467
  REMARK    GeneRIF: Hypomethylated RRBP1 Potentiates Tumor Malignancy and
            Chemoresistance in Upper Tract Urothelial Carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 977)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 977)
  AUTHORS   Foster,L.J., Zeemann,P.A., Li,C., Mann,M., Jensen,O.N. and
            Kassem,M.
  TITLE     Differential expression profiling of membrane proteins by
            quantitative proteomics in a human mesenchymal stem cell line
            undergoing osteoblast differentiation
  JOURNAL   Stem Cells 23 (9), 1367-1377 (2005)
   PUBMED   16210410
REFERENCE   7  (residues 1 to 977)
  AUTHORS   Diefenbach,R.J., Diefenbach,E., Douglas,M.W. and Cunningham,A.L.
  TITLE     The ribosome receptor, p180, interacts with kinesin heavy chain,
            KIF5B
  JOURNAL   Biochem Biophys Res Commun 319 (3), 987-992 (2004)
   PUBMED   15184079
  REMARK    GeneRIF: Results identify the ribosome receptor, p180, as a binding
            partner of the kinesin heavy chain isoform KIF5B.
REFERENCE   8  (residues 1 to 977)
  AUTHORS   Langley,R., Leung,E., Morris,C., Berg,R., McDonald,M., Weaver,A.,
            Parry,D.A., Ni,J., Su,J., Gentz,R., Spurr,N. and Krissansen,G.W.
  TITLE     Identification of multiple forms of 180-kDa ribosome receptor in
            human cells
  JOURNAL   DNA Cell Biol 17 (5), 449-460 (1998)
   PUBMED   9628588
REFERENCE   9  (residues 1 to 977)
  AUTHORS   Basson,C.T., MacRae,C.A., Schoenberg-Fejzo,M., Morton,C.C.,
            Spinner,N.B., Genin,A., Krug,E., Seidman,J.G. and Seidman,C.E.
  TITLE     Identification, characterization, and chromosomal localization of
            the human homolog (hES) of ES/130
  JOURNAL   Genomics 35 (3), 628-631 (1996)
   PUBMED   8812507
REFERENCE   10 (residues 1 to 977)
  AUTHORS   Savitz,A.J. and Meyer,D.I.
  TITLE     Identification of a ribosome receptor in the rough endoplasmic
            reticulum
  JOURNAL   Nature 346 (6284), 540-544 (1990)
   PUBMED   2165568
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL132765.38.
            
            On May 21, 2020 this sequence version replaced NP_001036041.1.
            
            Summary: This gene encodes a ribosome-binding protein of the
            endoplasmic reticulum (ER) membrane. Studies suggest that this gene
            plays a role in ER proliferation, secretory pathways and secretory
            cell differentiation, and mediation of ER-microtubule interactions.
            Alternative splicing has been observed and protein isoforms are
            characterized by regions of N-terminal decapeptide and C-terminal
            heptad repeats. Splicing of the tandem repeats results in
            variations in ribosome-binding affinity and secretory function. The
            full-length nature of variants which differ in repeat length has
            not been determined. Pseudogenes of this gene have been identified
            on chromosomes 3 and 7, and RRBP1 has been excluded as a candidate
            gene in the cause of Alagille syndrome, the result of a mutation in
            a nearby gene on chromosome 20p12. [provided by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.1"
     Protein         1..977
                     /product="ribosome-binding protein 1 isoform 2"
                     /note="ES/130-related protein; ribosome receptor protein;
                     180 kDa ribosome receptor homolog; ribosome binding
                     protein 1 homolog 180kDa (dog); ribosomal receptor-binding
                     protein 1; endoplasmic reticulum ribosome-binding protein
                     1"
                     /calculated_mol_wt=108501
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2E9.5)"
     Region          33..168
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          44..90
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2E9.5)"
     Region          129..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2E9.5)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99PL5; propagated from
                     UniProtKB/Swiss-Prot (Q9P2E9.5)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99PL5; propagated from
                     UniProtKB/Swiss-Prot (Q9P2E9.5)"
     Region          265..962
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..977
                     /gene="RRBP1"
                     /gene_synonym="ES/130; ES130; hES; p180; RRp"
                     /coded_by="NM_001042576.2:314..3247"
                     /note="isoform 2 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13128.1"
                     /db_xref="GeneID:6238"
                     /db_xref="HGNC:HGNC:10448"
                     /db_xref="MIM:601418"
ORIGIN      
        1 mdiydtqtlg vvvfggfmvv saigiflvst fsmketsyee alanqrkema kthhqkvekk
       61 kkektvekkg ktkkkeekpn gkipdhdpap nvtvllrepv rapavavapt pvqppiivap
      121 vatvpampqe klasspkdkk kkekkvakve pavssvvnsi qvltskaail etapkegrnt
      181 dvaqspeapk qeapakkksg skkkgppdad gplylpyktl vstvgsmvfn egeaqrliei
      241 lsekagiiqd twhkatqkgd pvailkrqle ekekllateq edaavakskl relnkemaae
      301 kakaaageak vkkqlvareq eitavqarmq asyrehvkev qqlqgkirtl qeqlengpnt
      361 qlarlqqens ilrdalnqat sqveskqnae laklrqelsk vskelvekse avrqdeqqrk
      421 aleakaaafe kqvlqlqash reseealqkr ldevsrelch tqsshaslra daekaqeqqq
      481 qmaelhsklq sseaevrskc eelsglhgql qearaensql terirsieal leagqardaq
      541 dvqasqaead qqqtrlkele sqvsglekea ielreaveqq kvknndlrek nwkamealat
      601 aeqackekll sltqakeese kqlclieaqt meallallpe lsvlaqqnyt ewlqdlkekg
      661 ptllkhppap aepssdlask lreaeetqst lqaecdqyrs ilaetegmlr dlqksveeee
      721 qvwrakvgaa eeelqksrvt vkhleeivek lkgelessdq vrehtshlea elekhmaaas
      781 aecqnyakev aglrqllles qsqldaakse aqkqsdelal vrqqlsemks hvedgdiaga
      841 passpeappa eqdpvqlktq lewteailed eqtqrqklta efeeaqtsac rlqeeleklr
      901 tagplesset eeasqlkerl ekekkltsdl graatrlqel lkttqeqlar ekdtvkklqe
      961 qlekaedgss skegtsv
//
LOCUS       NP_001244935             352 aa            linear   PRI 21-NOV-2025
DEFINITION  COP9 signalosome complex subunit 4 isoform 2 [Homo sapiens].
ACCESSION   NP_001244935
VERSION     NP_001244935.1
DBSOURCE    REFSEQ: accession NM_001258006.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Kim,M., Park,J., Bouhaddou,M., Kim,K., Rojc,A., Modak,M.,
            Soucheray,M., McGregor,M.J., O'Leary,P., Wolf,D., Stevenson,E.,
            Foo,T.K., Mitchell,D., Herrington,K.A., Munoz,D.P., Tutuncuoglu,B.,
            Chen,K.H., Zheng,F., Kreisberg,J.F., Diolaiti,M.E., Gordan,J.D.,
            Coppe,J.P., Swaney,D.L., Xia,B., van 't Veer,L., Ashworth,A.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein interaction landscape of breast cancer
  JOURNAL   Science 374 (6563), eabf3066 (2021)
   PUBMED   34591612
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Bech-Otschir,D., Kraft,R., Huang,X., Henklein,P., Kapelari,B.,
            Pollmann,C. and Dubiel,W.
  TITLE     COP9 signalosome-specific phosphorylation targets p53 to
            degradation by the ubiquitin system
  JOURNAL   EMBO J 20 (7), 1630-1639 (2001)
   PUBMED   11285227
REFERENCE   7  (residues 1 to 352)
  AUTHORS   Cohen,H., Azriel,A., Cohen,T., Meraro,D., Hashmueli,S.,
            Bech-Otschir,D., Kraft,R., Dubiel,W. and Levi,B.Z.
  TITLE     Interaction between interferon consensus sequence-binding protein
            and COP9/signalosome subunit CSN2 (Trip15). A possible link between
            interferon regulatory factor signaling and the COP9/signalosome
  JOURNAL   J Biol Chem 275 (50), 39081-39089 (2000)
   PUBMED   10991940
REFERENCE   8  (residues 1 to 352)
  AUTHORS   Naumann,M., Bech-Otschir,D., Huang,X., Ferrell,K. and Dubiel,W.
  TITLE     COP9 signalosome-directed c-Jun activation/stabilization is
            independent of JNK
  JOURNAL   J Biol Chem 274 (50), 35297-35300 (1999)
   PUBMED   10585392
REFERENCE   9  (residues 1 to 352)
  AUTHORS   Wei,N., Tsuge,T., Serino,G., Dohmae,N., Takio,K., Matsui,M. and
            Deng,X.W.
  TITLE     The COP9 complex is conserved between plants and mammals and is
            related to the 26S proteasome regulatory complex
  JOURNAL   Curr Biol 8 (16), 919-922 (1998)
   PUBMED   9707402
REFERENCE   10 (residues 1 to 352)
  AUTHORS   Seeger,M., Kraft,R., Ferrell,K., Bech-Otschir,D., Dumdey,R.,
            Schade,R., Gordon,C., Naumann,M. and Dubiel,W.
  TITLE     A novel protein complex involved in signal transduction possessing
            similarities to 26S proteasome subunits
  JOURNAL   FASEB J 12 (6), 469-478 (1998)
   PUBMED   9535219
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK094238.1 and BC009292.2.
            
            Summary: This gene encodes one of eight subunits composing COP9
            signalosome, a highly conserved protein complex that functions as
            an important regulator in multiple signaling pathways. The
            structure and function of COP9 signalosome is similar to that of
            the 19S regulatory particle of 26S proteasome. COP9 signalosome has
            been shown to interact with SCF-type E3 ubiquitin ligases and act
            as a positive regulator of E3 ubiquitin ligases. Two transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (2) lacks an alternate coding exon
            compared to variant 1, that causes a frameshift. The resulting
            isoform (2) has a shorter and distinct C-terminus compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK094238.1, SRR1803613.382316.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..352
                     /product="COP9 signalosome complex subunit 4 isoform 2"
                     /note="COP9 signalosome complex subunit 4; signalosome
                     subunit 4; JAB1-containing signalosome subunit 4; COP9
                     constitutive photomorphogenic homolog subunit 4; COP9
                     constitutive photomorphogenic-like protein subunit 4;
                     testis tissue sperm-binding protein Li 42a"
                     /calculated_mol_wt=40066
     Region          <71..337
                     /region_name="RPN5"
                     /note="26S proteasome regulatory complex component
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5071"
                     /db_xref="CDD:227403"
     CDS             1..352
                     /gene="COPS4"
                     /gene_synonym="CSN4; SGN4"
                     /coded_by="NM_001258006.2:43..1101"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58909.1"
                     /db_xref="GeneID:51138"
                     /db_xref="HGNC:HGNC:16702"
                     /db_xref="MIM:616008"
ORIGIN      
        1 maaavrqdla qlmnssgshk dlagkyrqil ekaiqlsgae qlealkafve amvnenvslv
       61 isrqlltdfc thlpnlpdst akeiyhftle kiqprvisfe eqvasirqhl asiyekeedw
      121 rnaaqvlvgi pletgqkqyn vdykletylk iarlyleddd pvqaeayinr asllqnestn
      181 eqlqihykvc yarvldyrrk fieaaqryne lsyktivhes erlealkhal hctilasagq
      241 qrsrmlatlf kdercqqlaa ygilekmyld riirgnqlqe faamlmphqk attadgssil
      301 draviehnll sasklynnit feelgallei paakhekpcq rgisrsnhfv sk
//
LOCUS       NP_001288784             342 aa            linear   PRI 21-NOV-2025
DEFINITION  SAP30-binding protein isoform 1 [Homo sapiens].
ACCESSION   NP_001288784
VERSION     NP_001288784.1
DBSOURCE    REFSEQ: accession NM_001301855.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Fukumura,K., Sperotto,L., Seuss,S., Kang,H.S., Yoshimoto,R.,
            Sattler,M. and Mayeda,A.
  TITLE     SAP30BP interacts with RBM17/SPF45 to promote splicing in a subset
            of human short introns
  JOURNAL   Cell Rep 42 (12), 113534 (2023)
   PUBMED   38065098
  REMARK    GeneRIF: SAP30BP interacts with RBM17/SPF45 to promote splicing in
            a subset of human short introns.
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Wang,C., Xu,L., Du,C., Yun,H., Wang,K., Liu,H., Ye,M., Fan,J.,
            Zhou,Y. and Cheng,H.
  TITLE     CDK11 requires a critical activator SAP30BP to regulate pre-mRNA
            splicing
  JOURNAL   EMBO J 42 (24), e114051 (2023)
   PUBMED   38059508
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Barros,R.S.M., Sant' Anna,C.C., Alcantara,D.D.F.A.,
            Pantoja,K.B.C.C., Fernandes,M.R., Bentes,L.G.B., Pimentel,A.L.J.C.,
            Lemos,R.S., Almeida,N.R.C., Fernandes,M.R.N., da Cruz,T.S.,
            Candido,A.A. and Burbano,R.M.R.
  TITLE     Association between the rs820218 Variant within the SAP30BP Gene
            and Rotator Cuff Rupture in an Amazonian Population
  JOURNAL   Genes (Basel) 14 (2), 367 (2023)
   PUBMED   36833294
  REMARK    GeneRIF: Association between the rs820218 Variant within the
            SAP30BP Gene and Rotator Cuff Rupture in an Amazonian Population.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 342)
  AUTHORS   Naukkarinen,J., Surakka,I., Pietilainen,K.H., Rissanen,A.,
            Salomaa,V., Ripatti,S., Yki-Jarvinen,H., van Duijn,C.M.,
            Wichmann,H.E., Kaprio,J., Taskinen,M.R. and Peltonen,L.
  CONSRTM   ENGAGE Consortium
  TITLE     Use of genome-wide expression data to mine the 'Gray Zone' of GWA
            studies leads to novel candidate obesity genes
  JOURNAL   PLoS Genet 6 (6), e1000976 (2010)
   PUBMED   20532202
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 342)
  AUTHORS   Gao,J., Li,W.X., Feng,S.Q., Yuan,Y.S., Wan,D.F., Han,W. and Yu,Y.
  TITLE     A protein-protein interaction network of transcription factors
            acting during liver cell proliferation
  JOURNAL   Genomics 91 (4), 347-355 (2008)
   PUBMED   18255255
REFERENCE   8  (residues 1 to 342)
  AUTHORS   Li,J.F., Liu,L.D., Ma,S.H., Che,Y.C., Wang,L.C., Dong,C.H.,
            Zhao,H.L., Liao,Y. and Li,Q.H.
  TITLE     HTRP--an immediate-early gene product induced by HSV1 infection in
            human embryo fibroblasts, is involved in cellular co-repressors
  JOURNAL   J Biochem 136 (2), 169-176 (2004)
   PUBMED   15496587
  REMARK    GeneRIF: HTRP is involved in cellular co-repressors
REFERENCE   9  (residues 1 to 342)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
REFERENCE   10 (residues 1 to 342)
  AUTHORS   Zhang,Y., Sun,Z.W., Iratni,R., Erdjument-Bromage,H., Tempst,P.,
            Hampsey,M. and Reinberg,D.
  TITLE     SAP30, a novel protein conserved between human and yeast, is a
            component of a histone deacetylase complex
  JOURNAL   Mol Cell 1 (7), 1021-1031 (1998)
   PUBMED   9651585
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF450482.1, BM807177.1 and BC011724.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.783387.1,
                                           SRR14038192.124640.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..342
                     /product="SAP30-binding protein isoform 1"
                     /note="HSV-1 binding; transcriptional regulator protein
                     HCNGP"
                     /calculated_mol_wt=37507
     Region          153..244
                     /region_name="HCNGP"
                     /note="HCNGP-like protein; pfam07818"
                     /db_xref="CDD:462281"
     CDS             1..342
                     /gene="SAP30BP"
                     /gene_synonym="HCNGP; HTRG; HTRP"
                     /coded_by="NM_001301855.2:36..1064"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:29115"
                     /db_xref="HGNC:HGNC:30785"
                     /db_xref="MIM:610218"
ORIGIN      
        1 magkknvlss lavyaedsep esdgeagiea vgsaaeekgg lvsdaygedd fsrlggdedg
       61 yeeeedensr qsedddsete kpeaddpkek lgtvteapra qqahgpacwt qraeeshskh
      121 dkdnteaekr dpqelvasfs ervrnmspde ikippeppgr csnhlqdkiq klyerkikeg
      181 mdmnyiiqrk kefrnpsiye kliqfcaide lgtnypkdmf dphgwsedsy yealakaqki
      241 emdklekakk ertkiefvtg tkkgtttnat stttttasta vadaqkrksk wdsaipvtti
      301 aqptilttta tlpavvtvtt sasgskttvi savgtivkka kq
//
LOCUS       NP_001315611             707 aa            linear   PRI 21-NOV-2025
DEFINITION  amyloid beta precursor like protein 2 isoform 6 precursor [Homo
            sapiens].
ACCESSION   NP_001315611
VERSION     NP_001315611.1
DBSOURCE    REFSEQ: accession NM_001328682.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Tao,Z., Huang,J. and Li,J.
  TITLE     Comprehensive intratumoral heterogeneity landscaping of liver
            hepatocellular carcinoma and discerning of APLP2 in cancer
            progression
  JOURNAL   Environ Toxicol 39 (2), 612-625 (2024)
   PUBMED   37515494
  REMARK    GeneRIF: Comprehensive intratumoral heterogeneity landscaping of
            liver hepatocellular carcinoma and discerning of APLP2 in cancer
            progression.
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Huang,X., Yang,J., Xi,H., Zhang,M., Oh,Y., Jin,Z. and Zheng,Z.
  TITLE     Implication of Amyloid Precursor-like Protein 2 Expression in
            Cutaneous Squamous Cell Carcinoma Pathogenesis
  JOURNAL   In Vivo 38 (1), 399-408 (2024)
   PUBMED   38148084
  REMARK    GeneRIF: Implication of Amyloid Precursor-like Protein 2 Expression
            in Cutaneous Squamous Cell Carcinoma Pathogenesis.
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Chen,J., Tang,F., Li,H., Wu,X., Yang,Y., Liu,Z., Huang,X., Wang,J.,
            Zheng,R., Wang,L., Liu,H., Xu,J., Wang,P. and Liu,F.
  TITLE     Mycobacterium tuberculosis suppresses APLP2 expression to enhance
            its survival in macrophage
  JOURNAL   Int Immunopharmacol 124 (Pt B), 111058 (2023)
   PUBMED   37844466
  REMARK    GeneRIF: Mycobacterium tuberculosis suppresses APLP2 expression to
            enhance its survival in macrophage.
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 707)
  AUTHORS   Blangy,A., Vidal,F., Cuzin,F., Yang,Y.H., Boulukos,K. and
            Rassoulzadegan,M.
  TITLE     CDEBP, a site-specific DNA-binding protein of the 'APP-like'
            family, is required during the early development of the mouse
  JOURNAL   J Cell Sci 108 (Pt 2), 675-683 (1995)
   PUBMED   7539437
REFERENCE   7  (residues 1 to 707)
  AUTHORS   von der Kammer,H., Hanes,J., Klaudiny,J. and Scheit,K.H.
  TITLE     A human amyloid precursor-like protein is highly homologous to a
            mouse sequence-specific DNA-binding protein
  JOURNAL   DNA Cell Biol 13 (11), 1137-1143 (1994)
   PUBMED   7702756
REFERENCE   8  (residues 1 to 707)
  AUTHORS   Bush,A.I., Pettingell,W.H. Jr., de Paradis,M., Tanzi,R.E. and
            Wasco,W.
  TITLE     The amyloid beta-protein precursor and its mammalian homologues.
            Evidence for a zinc-modulated heparin-binding superfamily
  JOURNAL   J Biol Chem 269 (43), 26618-26621 (1994)
   PUBMED   7929392
REFERENCE   9  (residues 1 to 707)
  AUTHORS   von der Kammer,H., Loffler,C., Hanes,J., Klaudiny,J., Scheit,K.H.
            and Hansmann,I.
  TITLE     The gene for the amyloid precursor-like protein APLP2 is assigned
            to human chromosome 11q23-q25
  JOURNAL   Genomics 20 (2), 308-311 (1994)
   PUBMED   8020984
REFERENCE   10 (residues 1 to 707)
  AUTHORS   Wasco,W., Gurubhagavatula,S., Paradis,M.D., Romano,D.M.,
            Sisodia,S.S., Hyman,B.T., Neve,R.L. and Tanzi,R.E.
  TITLE     Isolation and characterization of APLP2 encoding a homologue of the
            Alzheimer's associated amyloid beta protein precursor
  JOURNAL   Nat Genet 5 (1), 95-100 (1993)
   PUBMED   8220435
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003041.3, AP001183.6 and
            BM992563.1.
            
            Summary: This gene encodes amyloid precursor- like protein 2
            (APLP2), which is a member of the APP (amyloid precursor protein)
            family including APP, APLP1 and APLP2. This protein is ubiquitously
            expressed. It contains heparin-, copper- and zinc- binding domains
            at the N-terminus, BPTI/Kunitz inhibitor and E2 domains in the
            middle region, and transmembrane and intracellular domains at the
            C-terminus. This protein interacts with major histocompatibility
            complex (MHC) class I molecules. The synergy of this protein and
            the APP is required to mediate neuromuscular transmission, spatial
            learning and synaptic plasticity. This protein has been implicated
            in the pathogenesis of Alzheimer's disease. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            identified. [provided by RefSeq, Aug 2011].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1782323.1,
                                           SRR7346977.1906538.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.3"
     Protein         1..707
                     /product="amyloid beta precursor like protein 2 isoform 6
                     precursor"
                     /note="amyloid precursor protein homolog HSD-2; CDEI
                     box-binding protein; amyloid beta (A4) precursor-like
                     protein 2; testicular tissue protein Li 23; sperm membrane
                     protein YWK-II"
                     /calculated_mol_wt=77847
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2878
     Region          42..204
                     /region_name="A4_EXTRA"
                     /note="amyloid A4; smart00006"
                     /db_xref="CDD:128326"
     Region          309..491
                     /region_name="APP_E2"
                     /note="E2 domain of amyloid precursor protein; pfam12925"
                     /db_xref="CDD:463752"
     Region          624..704
                     /region_name="JMTM_APLP2"
                     /note="juxtamembrane and transmembrane (JMTM) domain found
                     in amyloid-like protein 2 (APLP-2) and similar proteins;
                     cd21709"
                     /db_xref="CDD:411992"
     Site            order(624..625,639,642..643,646..647,649..650,653..654,
                     657,660)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:411992"
     Site            order(625..627,643..644,646..647,649..654,657..662)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:411992"
     CDS             1..707
                     /gene="APLP2"
                     /gene_synonym="APLP-2; APPH; APPL2; CDEBP"
                     /coded_by="NM_001328682.2:85..2208"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 8"
                     /db_xref="GeneID:334"
                     /db_xref="HGNC:HGNC:598"
                     /db_xref="MIM:104776"
ORIGIN      
        1 maatgtaaaa atgrllllll vgltapalal agyiealaan agtgfavaep qiamfcgkln
       61 mhvniqtgkw epdptgtksc fetkeevlqy cqemypelqi tnvmeanqrv sidnwcrrdk
      121 kqcksrfvtp fkclvgefvs dvllvpekcq ffhkermevc enhqhwhtvv keacltqgmt
      181 lysygmllpc gvdqfhgtey vccpqtkiig svskeeeeed eeeeeeedee edydvyksef
      241 pteadledft eaavdedded eeegeevved rdyyydtfkg ddyneenpte pgsdgtmsdk
      301 eithdvkvpp tplptndvdv yfetsaddne harfqkakeq leirhrnrmd rvkkeweeae
      361 lqaknlpkae rqtliqhfqa mvkalekeaa sekqqlveth larveamlnd rrrmalenyl
      421 aalqsdpprp hrilqalrry vraenkdrlh tirhyqhvla vdpekaaqmk sqvmthlhvi
      481 eerrnqslsl lykvpyvaqe iqeeidellq eqradmdqft asisetpvdv rvsseeseei
      541 ppfhpfhpfp alpenedtqp elyhpmkkgs gvgeqdggli gaeekvinsk nkvdenmvid
      601 etldvkemif naervgglee eresvgplre dfslsssali gllviavaia tvivislvml
      661 rkrqygtish givevdpmlt peerhlnkmq nhgyenptyk yleqmqi
//
LOCUS       NP_001341244             280 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 3 [Homo sapiens].
ACCESSION   NP_001341244 XP_016868555
VERSION     NP_001341244.1
DBSOURCE    REFSEQ: accession NM_001354315.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 280)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 280)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 280)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            On Aug 29, 2017 this sequence version replaced XP_016868555.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.434909.1,
                                           SRR1660805.118579.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..280
                     /product="RNA-binding Raly-like protein isoform 3"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=30943
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          188..>233
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     CDS             1..280
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001354315.2:329..1171"
                     /note="isoform 3 is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS75760.1"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly sgyvfdydyy
      121 rddfynrlfd yhgrvppppr aviplkrprv avtttrrgkg vfsmkggsrs tasgstgskl
      181 ksdelqtikk eltqiktkid sllgrlekie kqqkaeaeaq kkqleeslvl iqeecvseia
      241 dhsteepaeg gpdadgeemt dgieedfded gghelflqik
//
LOCUS       NP_001383893             513 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 31 [Homo sapiens].
ACCESSION   NP_001383893 XP_016864161
VERSION     NP_001383893.1
DBSOURCE    REFSEQ: accession NM_001396964.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 513)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 513)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 513)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 513)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 513)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            On Oct 28, 2021 this sequence version replaced XP_016864161.1.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.146588.1,
                                           SRR1803613.275726.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..513
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 31"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=57771
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          360..487
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..513
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001396964.1:671..2212"
                     /note="isoform 31 is encoded by transcript variant 34"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkep qttvihnpdg nkestessnt tiededvkar
      361 kqeiikvteq lieainngdf eaytkicdpg ltafepealg nlvegmdfhr fyfenalsks
      421 nkpihtiiln phvhlvgdda aciayirltq ymdgsgmpkt mqseetrvwh rrdgkwqnvh
      481 fhrsgsptvp ikppcipngk enfsggtslw qni
//
LOCUS       NP_001364391             551 aa            linear   PRI 21-NOV-2025
DEFINITION  chloride channel CLIC-like protein 1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001364391
VERSION     NP_001364391.1
DBSOURCE    REFSEQ: accession NM_001377462.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 551)
  AUTHORS   D'Atri,I., Martin,E.R., Yang,L., Sears,E., Baple,E., Crosby,A.H.,
            Chilton,J.K. and Oguro-Ando,A.
  TITLE     Unraveling the CLCC1 interactome: Impact of the Asp25Glu variant
            and its interaction with SigmaR1 at the Mitochondrial-Associated ER
            Membrane (MAM)
  JOURNAL   Neurosci Lett 830, 137778 (2024)
   PUBMED   38621504
  REMARK    GeneRIF: Unraveling the CLCC1 interactome: Impact of the Asp25Glu
            variant and its interaction with SigmaR1 at the
            Mitochondrial-Associated ER Membrane (MAM).
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Tang,L., Tang,X., Zhao,Q., Li,Y., Bu,Y., Liu,Z., Li,J., Guo,J.,
            Shen,L., Jiang,H., Tang,B., Xu,R., Cao,W., Yuan,Y. and Wang,J.
  TITLE     Mutation and clinical analysis of the CLCC1 gene in amyotrophic
            lateral sclerosis patients from Central South China
  JOURNAL   Ann Clin Transl Neurol 11 (1), 79-88 (2024)
   PUBMED   37916886
  REMARK    GeneRIF: Mutation and clinical analysis of the CLCC1 gene in
            amyotrophic lateral sclerosis patients from Central South China.
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Guo,L., Mao,Q., He,J., Liu,X., Piao,X., Luo,L., Hao,X., Yu,H.,
            Song,Q., Xiao,B., Fan,D., Gao,Z. and Jia,Y.
  TITLE     Disruption of ER ion homeostasis maintained by an ER anion channel
            CLCC1 contributes to ALS-like pathologies
  JOURNAL   Cell Res 33 (7), 497-515 (2023)
   PUBMED   37142673
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Irvin,M.R., Shrestha,S., Chen,Y.D., Wiener,H.W., Haritunians,T.,
            Vaughan,L.K., Tiwari,H.K., Taylor,K.D., Scherzer,R., Saag,M.S.,
            Grunfeld,C., Rotter,J.I. and Arnett,D.K.
  TITLE     Genes linked to energy metabolism and immunoregulatory mechanisms
            are associated with subcutaneous adipose tissue distribution in
            HIV-infected men
  JOURNAL   Pharmacogenet Genomics 21 (12), 798-807 (2011)
   PUBMED   21897333
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Zhang,Q., Zulfiqar,F., Xiao,X., Riazuddin,S.A., Ayyagari,R.,
            Sabar,F., Caruso,R., Sieving,P.A., Riazuddin,S. and Hejtmancik,J.F.
  TITLE     Severe autosomal recessive retinitis pigmentosa maps to chromosome
            1p13.3-p21.2 between D1S2896 and D1S457 but outside ABCA4
  JOURNAL   Hum Genet 118 (3-4), 356-365 (2005)
   PUBMED   16189710
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Li,X. and Weinman,S.A.
  TITLE     Chloride channels and hepatocellular function: prospects for
            molecular identification
  JOURNAL   Annu Rev Physiol 64, 609-633 (2002)
   PUBMED   11826282
  REMARK    Review article
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Nagasawa,M., Kanzaki,M., Iino,Y., Morishita,Y. and Kojima,I.
  TITLE     Identification of a novel chloride channel expressed in the
            endoplasmic reticulum, golgi apparatus, and nucleus
  JOURNAL   J Biol Chem 276 (23), 20413-20418 (2001)
   PUBMED   11279057
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL449266.17.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1455922.1,
                                           SRR1660809.146717.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..551
                     /product="chloride channel CLIC-like protein 1 isoform 1
                     precursor"
                     /note="chloride channel CLIC-like protein 1; Mid-1-related
                     chloride channel protein 1; retinitis pigmentosa 32
                     (autosomal recessive); ER anion channel 1"
                     /calculated_mol_wt=60112
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1928
     Region          14..551
                     /region_name="MCLC"
                     /note="Mid-1-related chloride channel (MCLC); pfam05934"
                     /db_xref="CDD:461783"
     mat_peptide     19..551
                     /product="Chloride channel CLIC-like protein 1.
                     /id=PRO_0000297682"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
                     /calculated_mol_wt=60112
     Site            25
                     /site_type="other"
                     /note="Ca(2+)-mediated inhibition of channel activity.
                     /evidence=ECO:0000269|PubMed:37142673; propagated from
                     UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            181
                     /site_type="other"
                     /note="Ca(2+)-mediated inhibition of channel activity.
                     /evidence=ECO:0000269|PubMed:37142673; propagated from
                     UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            217..237
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            330..350
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Region          363..415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Region          447..551
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96S66.1)"
     CDS             1..551
                     /gene="CLCC1"
                     /gene_synonym="ERAC1; MCLC; RP32"
                     /coded_by="NM_001377462.1:96..1751"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 9"
                     /db_xref="CCDS:CCDS41362.1"
                     /db_xref="GeneID:23155"
                     /db_xref="HGNC:HGNC:29675"
                     /db_xref="MIM:617539"
ORIGIN      
        1 mlcslllcec lllvagyahd ddwidptdml nydaasgtmr ksqakygisg ekdvspdlsc
       61 adeisecyhk ldsltykide cekkkredye sqsnpvfrry lnkilieagk lglpdenkgd
      121 mhydaeiilk retlleiqkf lngedwkpga lddalsdili nfkfhdfetw kwrfedsfgv
      181 dpynvlmvll cllcivvlva telwtyvrwy tqlrrvliis flfslgwnwm ylyklafaqh
      241 qaevakmepl nnvcakkmdw tgsiwewfrs swtykddpcq kyyelllvnp iwlvpptkal
      301 avtfttfvte plkhigkgtg efikalmkei pallhlpvli imalailsfc ygagksvhvl
      361 rhiggpesep pqalrprdrr rqeeidyrpd ggagdadfhy rgqmgpteqg pyaktyegrr
      421 eilrerdvdl rfqtgnkspe vlrafdvpda earehptvvp shkspvldtk pketggilge
      481 gtpkesstes sqsakpvsgq dtsgntegsp aaekaqlkse aagspdqgst yspargvagp
      541 rgqdpvsspc g
//
LOCUS       NP_001317948             105 aa            linear   PRI 21-NOV-2025
DEFINITION  cell division cycle-associated protein 3 isoform 5 [Homo sapiens].
ACCESSION   NP_001317948
VERSION     NP_001317948.1
DBSOURCE    REFSEQ: accession NM_001331019.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Zhang,H., Zheng,Y., Yu,L., Liu,M. and Zhang,Y.
  TITLE     Identification of circ_0038632 as a Promoter of Breast Cancer
            through miR-520a-3p-Dependent Modulation of CDCA3
  JOURNAL   Ann Clin Lab Sci 53 (4), 562-572 (2023)
   PUBMED   37625824
  REMARK    GeneRIF: Identification of circ_0038632 as a Promoter of Breast
            Cancer through miR-520a-3p-Dependent Modulation of CDCA3.
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Gong,S., Bai,B., Sun,G., Jin,H. and Zhang,Z.
  TITLE     CDCA3 exhibits a role in promoting the progression of ovarian
            cancer
  JOURNAL   Tissue Cell 79, 101903 (2022)
   PUBMED   36081320
  REMARK    GeneRIF: CDCA3 exhibits a role in promoting the progression of
            ovarian cancer.
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Liu,W., Shen,D., Ju,L., Zhang,R., Du,W., Jin,W., Xiong,K., Wang,G.,
            Qian,K., Zhang,Y., Xiao,Y. and Wang,X.
  TITLE     MYBL2 promotes proliferation and metastasis of bladder cancer
            through transactivation of CDCA3
  JOURNAL   Oncogene 41 (41), 4606-4617 (2022)
   PUBMED   36071275
  REMARK    GeneRIF: MYBL2 promotes proliferation and metastasis of bladder
            cancer through transactivation of CDCA3.
REFERENCE   5  (residues 1 to 105)
  AUTHORS   Luo,J., Xia,L., Zhang,L., Zhao,K. and Li,C.
  TITLE     MiRNA-144-5p down-modulates CDCA3 to regulate proliferation and
            apoptosis of lung adenocarcinoma cells
  JOURNAL   Mutat Res 825, 111798 (2022)
   PUBMED   36087462
  REMARK    GeneRIF: MiRNA-144-5p down-modulates CDCA3 to regulate
            proliferation and apoptosis of lung adenocarcinoma cells.
REFERENCE   6  (residues 1 to 105)
  AUTHORS   Chen,J., Zhu,S., Jiang,N., Shang,Z., Quan,C. and Niu,Y.
  TITLE     HoxB3 promotes prostate cancer cell progression by transactivating
            CDCA3
  JOURNAL   Cancer Lett 330 (2), 217-224 (2013)
   PUBMED   23219899
  REMARK    GeneRIF: HoxB3 promote prostate cancer progression by upregulating
            CDCA3 expression.
REFERENCE   7  (residues 1 to 105)
  AUTHORS   Uchida,F., Uzawa,K., Kasamatsu,A., Takatori,H., Sakamoto,Y.,
            Ogawara,K., Shiiba,M., Tanzawa,H. and Bukawa,H.
  TITLE     Overexpression of cell cycle regulator CDCA3 promotes oral cancer
            progression by enhancing cell proliferation with prevention of G1
            phase arrest
  JOURNAL   BMC Cancer 12, 321 (2012)
   PUBMED   22839099
  REMARK    GeneRIF: overexpression of CDCA3 occurs frequently during oral
            carcinogenesis.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 105)
  AUTHORS   Yoshida,K.
  TITLE     Cell-cycle-dependent regulation of the human and mouse Tome-1
            promoters
  JOURNAL   FEBS Lett 579 (6), 1488-1492 (2005)
   PUBMED   15733861
  REMARK    GeneRIF: a repressor element (cell-cycle-dependent element/cell
            cycle gene homology region) in the vicinity of the transcription
            start site, and mutations within this element diminished the
            cell-cycle-dependent transcriptional regulation of Tome-1
REFERENCE   9  (residues 1 to 105)
  AUTHORS   Ayad,N.G., Rankin,S., Murakami,M., Jebanathirajah,J., Gygi,S. and
            Kirschner,M.W.
  TITLE     Tome-1, a trigger of mitotic entry, is degraded during G1 via the
            APC
  JOURNAL   Cell 113 (1), 101-113 (2003)
   PUBMED   12679038
REFERENCE   10 (residues 1 to 105)
  AUTHORS   Ansari-Lari,M.A., Muzny,D.M., Lu,J., Lu,F., Lilley,C.E., Spanos,S.,
            Malley,T. and Gibbs,R.A.
  TITLE     A gene-rich cluster between the CD4 and triosephosphate isomerase
            genes at human chromosome 12p13
  JOURNAL   Genome Res 6 (4), 314-326 (1996)
   PUBMED   8723724
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U47924.1, AV714087.1 and AK291421.1.
            
            Transcript Variant: This variant (6) differs in the both the 5' and
            3' coding regions and initiates translation at a downstream start
            codon compared to variant 1. The encoded isoform (5) has a shorter
            N-terminus and distict, shorter C-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AV714087.1, SRR14243140.3203590.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..105
                     /product="cell division cycle-associated protein 3 isoform
                     5"
                     /note="cell division cycle-associated protein 3; gene-rich
                     cluster protein C8; trigger of mitotic entry protein 1"
                     /calculated_mol_wt=11327
     CDS             1..105
                     /gene="CDCA3"
                     /gene_synonym="GRCC8; TOME-1; TOME1"
                     /coded_by="NM_001331019.2:177..494"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:83461"
                     /db_xref="HGNC:HGNC:14624"
                     /db_xref="MIM:607749"
ORIGIN      
        1 mktssgdpps plvkqlsevf etedsksnlp pepvlppeap lsseldlplg tqlsveeqmp
       61 pwnqtefpsk qvfskeearq ptetpvasqs sdkpsrdpet prssg
//
LOCUS       NP_001339843             545 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
            gamma isoform isoform h [Homo sapiens].
ACCESSION   NP_001339843 XP_005267880
VERSION     NP_001339843.1
DBSOURCE    REFSEQ: accession NM_001352914.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Li,B., Liu,S., Gao,Y., Zheng,L. and Lu,Y.
  TITLE     Combined detection of SDC2/ADHFE1/PPP2R5C methylation in stool DNA
            for colorectal cancer screening
  JOURNAL   J Cancer Res Clin Oncol 149 (12), 10241-10253 (2023)
   PUBMED   37270460
  REMARK    GeneRIF: Combined detection of SDC2/ADHFE1/PPP2R5C methylation in
            stool DNA for colorectal cancer screening.
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Ripamonti,M., Lamarca,A., Davey,N.E., Tonoli,D., Surini,S. and de
            Curtis,I.
  TITLE     A functional interaction between liprin-alpha1 and B56gamma
            regulatory subunit of protein phosphatase 2A supports tumor cell
            motility
  JOURNAL   Commun Biol 5 (1), 1025 (2022)
   PUBMED   36171301
  REMARK    GeneRIF: A functional interaction between liprin-alpha1 and
            B56gamma regulatory subunit of protein phosphatase 2A supports
            tumor cell motility.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 545)
  AUTHORS   McCright,B., Rivers,A.M., Audlin,S. and Virshup,D.M.
  TITLE     The B56 family of protein phosphatase 2A (PP2A) regulatory subunits
            encodes differentiation-induced phosphoproteins that target PP2A to
            both nucleus and cytoplasm
  JOURNAL   J Biol Chem 271 (36), 22081-22089 (1996)
   PUBMED   8703017
REFERENCE   5  (residues 1 to 545)
  AUTHORS   McCright,B., Brothman,A.R. and Virshup,D.M.
  TITLE     Assignment of human protein phosphatase 2A regulatory subunit genes
            b56alpha, b56beta, b56gamma, b56delta, and b56epsilon
            (PPP2R5A-PPP2R5E), highly expressed in muscle and brain, to
            chromosome regions 1q41, 11q12, 3p21, 6p21.1, and 7p11.2 --> p12
  JOURNAL   Genomics 36 (1), 168-170 (1996)
   PUBMED   8812429
REFERENCE   6  (residues 1 to 545)
  AUTHORS   Zolnierowicz,S., Van Hoof,C., Andjelkovic,N., Cron,P., Stevens,I.,
            Merlevede,W., Goris,J. and Hemmings,B.A.
  TITLE     The variable subunit associated with protein phosphatase 2A0
            defines a novel multimember family of regulatory subunits
  JOURNAL   Biochem J 317 (Pt 1) (Pt 1), 187-194 (1996)
   PUBMED   8694763
REFERENCE   7  (residues 1 to 545)
  AUTHORS   Tehrani,M.A., Mumby,M.C. and Kamibayashi,C.
  TITLE     Identification of a novel protein phosphatase 2A regulatory subunit
            highly expressed in muscle
  JOURNAL   J Biol Chem 271 (9), 5164-5170 (1996)
   PUBMED   8617797
REFERENCE   8  (residues 1 to 545)
  AUTHORS   McCright,B. and Virshup,D.M.
  TITLE     Identification of a new family of protein phosphatase 2A regulatory
            subunits
  JOURNAL   J Biol Chem 270 (44), 26123-26128 (1995)
   PUBMED   7592815
REFERENCE   9  (residues 1 to 545)
  AUTHORS   Akiyama,N., Shima,H., Hatano,Y., Osawa,Y., Sugimura,T. and Nagao,M.
  TITLE     cDNA cloning of BR gamma, a novel brain-specific isoform of the B
            regulatory subunit of type-2A protein phosphatase
  JOURNAL   Eur J Biochem 230 (2), 766-772 (1995)
   PUBMED   7607250
REFERENCE   10 (residues 1 to 545)
  AUTHORS   Ruediger,R., Roeckel,D., Fait,J., Bergqvist,A., Magnusson,G. and
            Walter,G.
  TITLE     Identification of binding sites on the regulatory A subunit of
            protein phosphatase 2A for the catalytic C subunit and for tumor
            antigens of simian virus 40 and polyomavirus
  JOURNAL   Mol Cell Biol 12 (11), 4872-4882 (1992)
   PUBMED   1328865
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL137779.6 and AL118558.6.
            
            On Jun 24, 2017 this sequence version replaced XP_005267880.1.
            
            Summary: The product of this gene belongs to the phosphatase 2A
            regulatory subunit B family. Protein phosphatase 2A is one of the
            four major Ser/Thr phosphatases, and it is implicated in the
            negative control of cell growth and division. It consists of a
            common heteromeric core enzyme, which is composed of a catalytic
            subunit and a constant regulatory subunit, that associates with a
            variety of regulatory subunits. The B regulatory subunit might
            modulate substrate selectivity and catalytic activity. This gene
            encodes a gamma isoform of the regulatory subunit B56 subfamily.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.140534.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.31"
     Protein         1..545
                     /product="serine/threonine-protein phosphatase 2A 56 kDa
                     regulatory subunit gamma isoform isoform h"
                     /note="B' alpha regulatory subunit; renal carcinoma
                     antigen NY-REN-29; protein phosphatase 2 regulatory
                     subunit B', gamma"
                     /calculated_mol_wt=63084
     Region          94..497
                     /region_name="B56"
                     /note="Protein phosphatase 2A regulatory B subunit (B56
                     family); pfam01603"
                     /db_xref="CDD:460264"
     CDS             1..545
                     /gene="PPP2R5C"
                     /gene_synonym="B56G; B56gamma; HJS4; PR61G"
                     /coded_by="NM_001352914.2:113..1750"
                     /note="isoform h is encoded by transcript variant 9"
                     /db_xref="GeneID:5527"
                     /db_xref="HGNC:HGNC:9311"
                     /db_xref="MIM:601645"
ORIGIN      
        1 mggtsreelr kaelespkag ksgksskegq dtveseqisv rknslvavps tvsakikvpv
       61 sqpivkkdkr qnssrfsasn nrelqklpsl kdvppadqek lfiqklrqcc vlfdfvsdpl
      121 sdlkwkevkr aalsemveyi thnrnvitep iypevvhmfa vnmfrtlpps snptgaefdp
      181 eedeptleaa wphlqlvyef flrflespdf qpniakkyid qkfvlqllel fdsedprerd
      241 flkttlhriy gkflglrayi rkqinnifyr fiyetehhng iaelleilgs iingfalplk
      301 eehkifllkv llplhkvksl svyhpqlayc vvqflekdst ltepvvmall kywpkthspk
      361 evmflnelee ildviepsef vkimeplfrq lakcvssphf qvaeralyyw nneyimslis
      421 dnaakilpim fpslyrnskt hwnktihgli ynalklfmem nqklfddctq qfkaeklkek
      481 lkmkereeaw vkienlakan pqaqkdpkkd rplarrksel pqdphtkkal eahcradela
      541 sqdgr
//
LOCUS       NP_001030178             184 aa            linear   PRI 21-NOV-2025
DEFINITION  large ribosomal subunit protein uL22 isoform a [Homo sapiens].
ACCESSION   NP_001030178 XP_001713705
VERSION     NP_001030178.1
DBSOURCE    REFSEQ: accession NM_001035006.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Fellmann,F., Saunders,C., O'Donohue,M.F., Reid,D.W., McFadden,K.A.,
            Montel-Lehry,N., Yu,C., Fang,M., Zhang,J., Royer-Bertrand,B.,
            Farinelli,P., Karboul,N., Willer,J.R., Fievet,L., Bhuiyan,Z.A.,
            Kleinhenz,A.L., Jadeau,J., Fulbright,J., Rivolta,C., Renella,R.,
            Katsanis,N., Beckmann,J.S., Nicchitta,C.V., Da Costa,L., Davis,E.E.
            and Gleizes,P.E.
  TITLE     An atypical form of 60S ribosomal subunit in Diamond-Blackfan
            anemia linked to RPL17 variants
  JOURNAL   JCI Insight 9 (17), e172475 (2024)
   PUBMED   39088281
  REMARK    GeneRIF: An atypical form of 60S ribosomal subunit in
            Diamond-Blackfan anemia linked to RPL17 variants.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Hori,H., Nakamura,S., Yoshida,F., Teraishi,T., Sasayama,D., Ota,M.,
            Hattori,K., Kim,Y., Higuchi,T. and Kunugi,H.
  TITLE     Integrated profiling of phenotype and blood transcriptome for
            stress vulnerability and depression
  JOURNAL   J Psychiatr Res 104, 202-210 (2018)
   PUBMED   30103068
  REMARK    GeneRIF: The present study combines an individual-based phenotypic
            profiling with a transdiagnostic approach and shows that several
            ribosomal genes including RPL17 is involved in stress vulnerability
            across nonclinical and clinical conditions.
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   7  (residues 1 to 184)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   8  (residues 1 to 184)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 184)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 184)
  AUTHORS   Mager,D.L. and Freeman,J.D.
  TITLE     A human gene related to the ribosomal protein L23 gene of
            Halobacterium marismortui
  JOURNAL   Nucleic Acids Res 18 (17), 5301 (1990)
   PUBMED   2402465
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AC100778.5.
            
            On Nov 19, 2008 this sequence version replaced XP_001713705.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L22P family of ribosomal proteins. It is located in the
            cytoplasm. This gene has been referred to as rpL23 because the
            encoded protein shares amino acid identity with ribosomal protein
            L23 from Halobacterium marismortui; however, its official symbol is
            RPL17. As is typical for genes encoding ribosomal proteins, there
            are multiple processed pseudogenes of this gene dispersed through
            the genome. Alternative splicing results in multiple transcript
            variants. Read-through transcription also exists between this gene
            and the neighboring downstream C18orf32 (chromosome 18 open reading
            frame 32) gene. [provided by RefSeq, Dec 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BQ949854.1, BU153842.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000580261.6/ ENSP00000462385.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..184
                     /product="large ribosomal subunit protein uL22 isoform a"
                     /note="60S ribosomal protein L17; large ribosomal subunit
                     protein uL22; gene encoding putative NFkB activating
                     protein; 60S ribosomal protein L23"
                     /calculated_mol_wt=21266
     Region          1..165
                     /region_name="PTZ00178"
                     /note="60S ribosomal protein L17; Provisional"
                     /db_xref="CDD:240306"
     Site            order(15..16,38..40,42..43,45..46,99..104,112..117,
                     149..150)
                     /site_type="active"
                     /note="putative translocon binding site [active]"
                     /db_xref="CDD:238205"
     Site            order(18,20,23,25..27,30,34,37,97,101,104,116,118..120,
                     122,125,137..142)
                     /site_type="other"
                     /note="protein-rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238205"
     Region          160..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18621.3)"
     CDS             1..184
                     /gene="RPL17"
                     /gene_synonym="DBA22; L17; PD-1; RPL23; uL22"
                     /coded_by="NM_001035006.5:22..576"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45865.1"
                     /db_xref="GeneID:6139"
                     /db_xref="HGNC:HGNC:10307"
                     /db_xref="MIM:603661"
ORIGIN      
        1 mvrysldpen ptkscksrgs nlrvhfkntr etaqaikgmh irkatkylkd vtlqkqcvpf
       61 rrynggvgrc aqakqwgwtq grwpkksaef llhmlknaes naelkgldvd slviehiqvn
      121 kapkmrrrty rahgrinpym sspchiemil tekeqivpkp eeevaqkkki sqkklkkqkl
      181 mare
//
LOCUS       NP_001337138             550 aa            linear   PRI 21-NOV-2025
DEFINITION  oxysterol-binding protein-related protein 9 isoform h [Homo
            sapiens].
ACCESSION   NP_001337138 XP_016855712
VERSION     NP_001337138.1
DBSOURCE    REFSEQ: accession NM_001350209.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Cabukusta,B., Borst Pauwels,S., Akkermans,J.J.L.L., Blomberg,N.,
            Mulder,A.A., Koning,R.I., Giera,M. and Neefjes,J.
  TITLE     The ORP9-ORP11 dimer promotes sphingomyelin synthesis
  JOURNAL   Elife 12, 91345 (2024)
   PUBMED   39106189
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 550)
  AUTHORS   He,R., Liu,F., Wang,H., Huang,S., Xu,K., Zhang,C., Liu,Y. and Yu,H.
  TITLE     ORP9 and ORP10 form a heterocomplex to transfer
            phosphatidylinositol 4-phosphate at ER-TGN contact sites
  JOURNAL   Cell Mol Life Sci 80 (3), 77 (2023)
   PUBMED   36853333
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Tan,J.X. and Finkel,T.
  TITLE     A phosphoinositide signalling pathway mediates rapid lysosomal
            repair
  JOURNAL   Nature 609 (7928), 815-821 (2022)
   PUBMED   36071159
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 550)
  AUTHORS   Hacker,B., Schultheiss,C., Doring,M. and Kurzik-Dumke,U.
  TITLE     Molecular partners of hNOT/ALG3, the human counterpart of the
            Drosophila NOT and yeast ALG3 gene, suggest its involvement in
            distinct cellular processes relevant to congenital disorders of
            glycosylation, cancer, neurodegeneration and a variety of further
            pathologies
  JOURNAL   Hum Mol Genet 27 (11), 1858-1878 (2018)
   PUBMED   29547901
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Gauci,S., Helbig,A.O., Slijper,M., Krijgsveld,J., Heck,A.J. and
            Mohammed,S.
  TITLE     Lys-N and trypsin cover complementary parts of the phosphoproteome
            in a refined SCX-based approach
  JOURNAL   Anal Chem 81 (11), 4493-4501 (2009)
   PUBMED   19413330
  REMARK    GeneRIF: Includes data showing N-alpha terminal acetylation of this
            protein (OSBL9_HUMAN), which begins with nASIMEGPLSK following
            cleavage of the initiating Met-1 residue.
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Lessmann,E., Ngo,M., Leitges,M., Minguet,S., Ridgway,N.D. and
            Huber,M.
  TITLE     Oxysterol-binding protein-related protein (ORP) 9 is a PDK-2
            substrate and regulates Akt phosphorylation
  JOURNAL   Cell Signal 19 (2), 384-392 (2007)
   PUBMED   16962287
  REMARK    GeneRIF: Furthermore, mammalian target of rapamycin was implicated
            in ORP9L phosphorylation in HEK293 cells. These studies identify
            ORP9 as a PDK-2 substrate and negative regulator of Akt
            phosphorylation at the PDK-2 site.
REFERENCE   8  (residues 1 to 550)
  AUTHORS   Wyles,J.P. and Ridgway,N.D.
  TITLE     VAMP-associated protein-A regulates partitioning of
            oxysterol-binding protein-related protein-9 between the endoplasmic
            reticulum and Golgi apparatus
  JOURNAL   Exp Cell Res 297 (2), 533-547 (2004)
   PUBMED   15212954
REFERENCE   9  (residues 1 to 550)
  AUTHORS   Jaworski,C.J., Moreira,E., Li,A., Lee,R. and Rodriguez,I.R.
  TITLE     A family of 12 human genes containing oxysterol-binding domains
  JOURNAL   Genomics 78 (3), 185-196 (2001)
   PUBMED   11735225
REFERENCE   10 (residues 1 to 550)
  AUTHORS   Lehto,M., Laitinen,S., Chinetti,G., Johansson,M., Ehnholm,C.,
            Staels,B., Ikonen,E. and Olkkonen,V.M.
  TITLE     The OSBP-related protein family in humans
  JOURNAL   J Lipid Res 42 (8), 1203-1213 (2001)
   PUBMED   11483621
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB254963.1, AF392445.1,
            DA754904.1, AL050343.17 and EL953716.1.
            
            On Apr 8, 2017 this sequence version replaced XP_016855712.1.
            
            Summary: This gene encodes a member of the oxysterol-binding
            protein (OSBP) family, a group of intracellular lipid receptors.
            Most members contain an N-terminal pleckstrin homology domain and a
            highly conserved C-terminal OSBP-like sterol-binding domain,
            although some members contain only the sterol-binding domain. This
            family member functions as a cholesterol transfer protein that
            regulates Golgi structure and function. Multiple transcript
            variants, most of which encode distinct isoforms, have been
            identified. Related pseudogenes have been identified on chromosomes
            3, 11 and 12. [provided by RefSeq, Jul 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.139251.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2151741
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..550
                     /product="oxysterol-binding protein-related protein 9
                     isoform h"
                     /note="oxysterol-binding protein-related protein 9;
                     OSBP-related protein 9"
                     /calculated_mol_wt=61433
     Region          191..537
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     CDS             1..550
                     /gene="OSBPL9"
                     /gene_synonym="ORP-9; ORP9"
                     /coded_by="NM_001350209.2:752..2404"
                     /note="isoform h is encoded by transcript variant 11"
                     /db_xref="GeneID:114883"
                     /db_xref="HGNC:HGNC:16386"
                     /db_xref="MIM:606737"
ORIGIN      
        1 msshslslst inpvdaiyqp splepvistm psqtvlppep vqlckseqrp sslpvgpvla
       61 tlghhqtptp nstgsghspp sssltspshv nlspntvpef sysssedefy dadefhqsgs
      121 spkrlidssg sasvlthsss gnslkrpdtt eslnsslsng tsdadlfdsh ddrdddaeag
      181 sveehksvim hllsqvrlgm dltkvvlptf ilerrsllem yadffahpdl fvsisdqkdp
      241 kdrmvqvvkw ylsafhagrk gsvakkpynp ilgeifqchw tlpndteent elvsegpvpw
      301 vsknsvtfva eqvshhppis afyaecfnkk iqfnahiwtk skflgmsigv hnigqgcvsc
      361 ldydehyilt fpngygrsil tvpwvelgge cnincsktgy saniifhtkp fyggkkhrit
      421 aeifspndkk sfcsiegewn gvmyakyatg entvfvdtkk lpiikkkvrk ledqneyesr
      481 slwkdvtfnl kirdidaate akhrleerqr aearerkeke iqwetrlfhe dgecwvydep
      541 llkrlgaakh
//
LOCUS       NP_964010                424 aa            linear   PRI 21-NOV-2025
DEFINITION  STAM-binding protein isoform 1 [Homo sapiens].
ACCESSION   NP_964010
VERSION     NP_964010.1
DBSOURCE    REFSEQ: accession NM_201647.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Zhang,W., Xu,Z., Du,Y., Liu,T., Xiong,Z., Hu,J., Chen,L., Peng,X.
            and Zhou,F.
  TITLE     Identification of STAM-binding protein as a target for the
            treatment of gemcitabine resistance pancreatic cancer in a
            nutrient-poor microenvironment
  JOURNAL   Cell Death Dis 15 (9), 657 (2024)
   PUBMED   39242557
  REMARK    GeneRIF: Identification of STAM-binding protein as a target for the
            treatment of gemcitabine resistance pancreatic cancer in a
            nutrient-poor microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Li,L., Yang,X., He,M., Xu,X., Xuan,X., Zhang,J., Zhang,L., Xu,H.
            and Li,D.
  TITLE     The expression and clinical significance of STAMBP in breast cancer
  JOURNAL   Mol Biol Rep 50 (1), 899-906 (2023)
   PUBMED   36309616
  REMARK    GeneRIF: The expression and clinical significance of STAMBP in
            breast cancer.
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Yang,Q., Yan,D., Zou,C., Xue,Q., Lin,S., Huang,Q., Li,X., Tang,D.,
            Chen,X. and Liu,J.
  TITLE     The deubiquitinating enzyme STAMBP is a newly discovered driver of
            triple-negative breast cancer progression that maintains RAI14
            protein stability
  JOURNAL   Exp Mol Med 54 (11), 2047-2059 (2022)
   PUBMED   36434041
  REMARK    GeneRIF: The deubiquitinating enzyme STAMBP is a newly discovered
            driver of triple-negative breast cancer progression that maintains
            RAI14 protein stability.
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Yu,S., E,C. and Yang,J.
  TITLE     STAM binding protein regulated by hsa_circ_0007334 exerts oncogenic
            potential in pancreatic cancer
  JOURNAL   Pancreatology 22 (7), 1003-1012 (2022)
   PUBMED   36089485
  REMARK    GeneRIF: STAM binding protein regulated by hsa_circ_0007334 exerts
            oncogenic potential in pancreatic cancer.
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Itoh,F., Asao,H., Sugamura,K., Heldin,C.H., ten Dijke,P. and
            Itoh,S.
  TITLE     Promoting bone morphogenetic protein signaling through negative
            regulation of inhibitory Smads
  JOURNAL   EMBO J 20 (15), 4132-4142 (2001)
   PUBMED   11483516
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Endo,K., Takeshita,T., Kasai,H., Sasaki,Y., Tanaka,N., Asao,H.,
            Kikuchi,K., Yamada,M., Chenb,M., O'Shea,J.J. and Sugamura,K.
  TITLE     STAM2, a new member of the STAM family, binding to the Janus
            kinases
  JOURNAL   FEBS Lett 477 (1-2), 55-61 (2000)
   PUBMED   10899310
REFERENCE   8  (residues 1 to 424)
  AUTHORS   Tanaka,N., Kaneko,K., Asao,H., Kasai,H., Endo,Y., Fujita,T.,
            Takeshita,T. and Sugamura,K.
  TITLE     Possible involvement of a novel STAM-associated molecule 'AMSH' in
            intracellular signal transduction mediated by cytokines
  JOURNAL   J Biol Chem 274 (27), 19129-19135 (1999)
   PUBMED   10383417
REFERENCE   9  (residues 1 to 424)
  AUTHORS   Asada,H., Ishii,N., Sasaki,Y., Endo,K., Kasai,H., Tanaka,N.,
            Takeshita,T., Tsuchiya,S., Konno,T. and Sugamura,K.
  TITLE     Grf40, A novel Grb2 family member, is involved in T cell signaling
            through interaction with SLP-76 and LAT
  JOURNAL   J Exp Med 189 (9), 1383-1390 (1999)
   PUBMED   10224278
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Carter,M.T., Mirzaa,G., McDonell,L.M. and Boycott,K.M.
  TITLE     Microcephaly-Capillary Malformation Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24354023
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DN919763.1, U73522.1 and
            AC073046.7.
            
            Summary: Cytokine-mediated signal transduction in the JAK-STAT
            cascade requires the involvement of adaptor molecules. One such
            signal-transducing adaptor molecule contains an SH3 domain that is
            required for induction of MYC and cell growth. The protein encoded
            by this gene binds to the SH3 domain of the signal-transducing
            adaptor molecule, and plays a critical role in cytokine-mediated
            signaling for MYC induction and cell cycle progression. Multiple
            alternatively spliced transcript variants encoding the same protein
            isoform have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1964169.1,
                                           SRR14038197.1180695.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..424
                     /product="STAM-binding protein isoform 1"
                     /EC_number="3.1.2.15"
                     /note="associated molecule with the SH3 domain of STAM;
                     endosome-associated ubiquitin isopeptidase; testicular
                     secretory protein Li 54"
                     /calculated_mol_wt=47946
     Region          1..127
                     /region_name="Interaction with CHMP3.
                     /evidence=ECO:0000269|PubMed:17146056"
                     /note="propagated from UniProtKB/Swiss-Prot (O95630.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          13..117
                     /region_name="USP8_dimer"
                     /note="USP8 dimerization domain; pfam08969"
                     /db_xref="CDD:462647"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          227..231
                     /region_name="Interaction with STAM.
                     /evidence=ECO:0000269|PubMed:10383417"
                     /note="propagated from UniProtKB/Swiss-Prot (O95630.1)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          254..424
                     /region_name="MPN_AMSH_like"
                     /note="Mov34/MPN/PAD-1 family; cd08066"
                     /db_xref="CDD:163697"
     Site            order(280,335,337,345,348)
                     /site_type="active"
                     /note="MPN+ (JAMM) motif [active]"
                     /db_xref="CDD:163697"
     Site            280
                     /site_type="other"
                     /note="Indirect zinc-binding.
                     /evidence=ECO:0000250|UniProtKB:Q96FJ0; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Site            order(282..284,309..313,316..317,320,323,329..330,333,335,
                     337,345,347..348,350..351,354..355,357..358,395)
                     /site_type="other"
                     /note="Distal ubiquitin recognition interface [polypeptide
                     binding]"
                     /db_xref="CDD:163697"
     Site            order(309,337,340..341,343,345..346,395..397)
                     /site_type="active"
                     /note="Proximal ubiquitin recognition interface [active]"
                     /db_xref="CDD:163697"
     Region          335..348
                     /region_name="JAMM motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01182"
                     /note="propagated from UniProtKB/Swiss-Prot (O95630.1)"
     Site            order(335,337,348)
                     /site_type="other"
                     /note="Zinc-binding site [ion binding]"
                     /db_xref="CDD:163697"
     CDS             1..424
                     /gene="STAMBP"
                     /gene_synonym="AMSH; MICCAP"
                     /coded_by="NM_201647.4:49..1323"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1929.1"
                     /db_xref="GeneID:10617"
                     /db_xref="HGNC:HGNC:16950"
                     /db_xref="MIM:606247"
ORIGIN      
        1 msdhgdvslp pedrvralsq lgsavevned ipprryfrsg veiirmasiy seegniehaf
       61 ilynkyitlf ieklpkhrdy ksavipekkd tvkklkeiaf pkaeelkael lkrytkeyte
      121 yneekkkeae elarnmaiqq elekekqrva qqkqqqleqe qfhafeemir nqelekerlk
      181 ivqefgkvdp glggplvpdl ekpsldvfpt ltvssiqpsd chttvrpakp pvvdrslkpg
      241 alsnsesipt idglrhvvvp grlcpqflql asantargve tcgilcgklm rneftithvl
      301 ipkqsagsdy cnteneeelf liqdqqglit lgwihthptq taflssvdlh thcsyqmmlp
      361 esvaivcspk fqetgffklt dhgleeissc rqkgfhphsk dpplfcscsh vtvvdravti
      421 tdlr
//
LOCUS       NP_001242944             138 aa            linear   PRI 21-NOV-2025
DEFINITION  homologous-pairing protein 2 homolog isoform 4 [Homo sapiens].
ACCESSION   NP_001242944
VERSION     NP_001242944.1
DBSOURCE    REFSEQ: accession NM_001256015.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Mei,L., Huang,L., Huang,Y., Wu,X., He,H., He,X., Su,Z. and Li,P.
  TITLE     Two novel biallelic mutations in PSMC3IP in a patient affected by
            premature ovarian insufficiency
  JOURNAL   Mol Med Rep 25 (2) (2022)
   PUBMED   34878148
  REMARK    GeneRIF: Two novel biallelic mutations in PSMC3IP in a patient
            affected by premature ovarian insufficiency.
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Nathansen,J., Lukiyanchuk,V., Hein,L., Stolte,M.I., Borgmann,K.,
            Lock,S., Kurth,I., Baumann,M., Krause,M., Linge,A. and Dubrovska,A.
  TITLE     Oct4 confers stemness and radioresistance to head and neck squamous
            cell carcinoma by regulating the homologous recombination factors
            PSMC3IP and RAD54L
  JOURNAL   Oncogene 40 (24), 4214-4228 (2021)
   PUBMED   34079088
  REMARK    GeneRIF: Oct4 confers stemness and radioresistance to head and neck
            squamous cell carcinoma by regulating the homologous recombination
            factors PSMC3IP and RAD54L.
REFERENCE   5  (residues 1 to 138)
  AUTHORS   Zangen,D., Kaufman,Y., Zeligson,S., Perlberg,S., Fridman,H.,
            Kanaan,M., Abdulhadi-Atwan,M., Abu Libdeh,A., Gussow,A.,
            Kisslov,I., Carmel,L., Renbaum,P. and Levy-Lahad,E.
  TITLE     XX ovarian dysgenesis is caused by a PSMC3IP/HOP2 mutation that
            abolishes coactivation of estrogen-driven transcription
  JOURNAL   Am J Hum Genet 89 (4), 572-579 (2011)
   PUBMED   21963259
  REMARK    GeneRIF: a PSMC3IP/HOP2 mutation may cause XX ovarian dysgenesis
            through abolishing coactivation of estrogen-driven transcription
REFERENCE   6  (residues 1 to 138)
  AUTHORS   Enomoto,R., Kinebuchi,T., Sato,M., Yagi,H., Kurumizaka,H. and
            Yokoyama,S.
  TITLE     Stimulation of DNA strand exchange by the human TBPIP/Hop2-Mnd1
            complex
  JOURNAL   J Biol Chem 281 (9), 5575-5581 (2006)
   PUBMED   16407260
  REMARK    GeneRIF: Data suggest that the human TBPIP/Hop2-Mnd1 complex may
            ensure proper pairing between homologous chromosomes through its
            stimulation of strand exchange during meiosis.
REFERENCE   7  (residues 1 to 138)
  AUTHORS   Ko,L., Cardona,G.R., Henrion-Caude,A. and Chin,W.W.
  TITLE     Identification and characterization of a tissue-specific
            coactivator, GT198, that interacts with the DNA-binding domains of
            nuclear receptors
  JOURNAL   Mol Cell Biol 22 (1), 357-369 (2002)
   PUBMED   11739747
  REMARK    GeneRIF: Identification of GT198 (TBPIP/Hop2) as a nuclear receptor
            coactivator. GT198 is phosphorylation regulated. GT198 interacts
            with nuclear receptors.
REFERENCE   8  (residues 1 to 138)
  AUTHORS   Ijichi,H., Tanaka,T., Nakamura,T., Yagi,H., Hakuba,A. and Sato,M.
  TITLE     Molecular cloning and characterization of a human homologue of
            TBPIP, a BRCA1 locus-related gene
  JOURNAL   Gene 248 (1-2), 99-107 (2000)
   PUBMED   10806355
REFERENCE   9  (residues 1 to 138)
  AUTHORS   Tanaka,T., Nakamura,T., Takagi,H. and Sato,M.
  TITLE     Molecular cloning and characterization of a novel TBP-1 interacting
            protein (TBPIP):enhancement of TBP-1 action on Tat by TBPIP
  JOURNAL   Biochem Biophys Res Commun 239 (1), 176-181 (1997)
   PUBMED   9345291
REFERENCE   10 (residues 1 to 138)
  AUTHORS   Rommens,J.M., Durocher,F., McArthur,J., Tonin,P., LeBlanc,J.F.,
            Allen,T., Samson,C., Ferri,L., Narod,S., Morgan,K. et al.
  TITLE     Generation of a transcription map at the HSD17B locus centromeric
            to BRCA1 at 17q21
  JOURNAL   Genomics 28 (3), 530-542 (1995)
   PUBMED   7490091
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC067852.23.
            
            Summary: This gene encodes a protein that functions in meiotic
            recombination. It is a subunit of the PSMC3IP/MND1 complex, which
            interacts with PSMC3/TBP1 to stimulate DMC1- and RAD51-mediated
            strand exchange during meiosis. The protein encoded by this gene
            can also co-activate ligand-driven transcription mediated by
            estrogen, androgen, glucocorticoid, progesterone, and thyroid
            nuclear receptors. Mutations in this gene cause XX female gonadal
            dysgenesis. Alternative splicing of this gene results in multiple
            transcript variants. [provided by RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ952182.1, SRR14038197.37522.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..138
                     /product="homologous-pairing protein 2 homolog isoform 4"
                     /note="homologous-pairing protein 2 homolog;
                     DBD-interacting; nuclear receptor coactivator GT198;
                     TBP-1-interacting protein; tat-binding protein
                     1-interacting protein; proteasome 26S ATPase subunit
                     3-interacting protein"
                     /calculated_mol_wt=15932
     Region          <5..>129
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          75..131
                     /region_name="LZ3wCH"
                     /note="Leucine zipper with capping helix domain;
                     pfam18517"
                     /db_xref="CDD:465789"
     CDS             1..138
                     /gene="PSMC3IP"
                     /gene_synonym="GT198; HOP2; HUMGT198A; ODG3; TBPIP"
                     /coded_by="NM_001256015.2:414..830"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:29893"
                     /db_xref="HGNC:HGNC:17928"
                     /db_xref="MIM:608665"
ORIGIN      
        1 mvsdadlqvl dgkivaltak vqslqqscry meaelkelss alttpemqke iqelkkecag
       61 yrerlknika atnhvtpeek eqvyrerqky ckewrkrkrm atelsdaile gypkskkqff
      121 eevgietded ynvtlpdp
//
LOCUS       NP_001363295             808 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger CCCH domain-containing protein 11A isoform 2 [Homo
            sapiens].
ACCESSION   NP_001363295 XP_016858450
VERSION     NP_001363295.1
DBSOURCE    REFSEQ: accession NM_001376366.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 808)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 808)
  AUTHORS   Kases,K., Schubert,E., Hajikhezri,Z., Larsson,M., Devi,P.,
            Darweesh,M., Andersson,L., Akusjarvi,G., Punga,T. and Younis,S.
  TITLE     The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts
  JOURNAL   J Biol Chem 299 (8), 104959 (2023)
   PUBMED   37356722
  REMARK    GeneRIF: The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts.
REFERENCE   3  (residues 1 to 808)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 808)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 808)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 808)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 808)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   8  (residues 1 to 808)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 808)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   10 (residues 1 to 808)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114402.2.
            
            On Nov 16, 2019 this sequence version replaced XP_016858450.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.37434.1,
                                           SRR7346977.2648868.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..808
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..808
                     /product="zinc finger CCCH domain-containing protein 11A
                     isoform 2"
                     /note="zinc finger CCCH-type domain containing 11A; zinc
                     finger CCCH domain-containing protein 11A"
                     /calculated_mol_wt=88815
     Region          1..110
                     /region_name="zf-CCCH_3"
                     /note="Zinc-finger containing family; pfam15663"
                     /db_xref="CDD:464787"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          139..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          223..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          285..351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          367..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          482..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          713..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     CDS             1..808
                     /gene="ZC3H11A"
                     /gene_synonym="ZC3HDC11A"
                     /coded_by="NM_001376366.1:1760..4186"
                     /note="isoform 2 is encoded by transcript variant 42"
                     /db_xref="GeneID:9877"
                     /db_xref="HGNC:HGNC:29093"
                     /db_xref="MIM:613513"
ORIGIN      
        1 mpnqgedcyf ffystctkgd scpfrhceaa ignetvctlw qegrcfrqvc rfrhmeidkk
       61 rseipcywen qptgcqklnc afhhnrgryv dglflppskt vlptvpespe eevkasqlsv
      121 qqnklsvqsn pspqlrsvmk vessenvpsp thppvvinaa dddeddddqf seegdetktp
      181 tlqptpevhn glrvtsvrkp avnikqgecl nfgiktleei kskkmkeksk kqgegssgvs
      241 slllhpepvp gpekenvrtv vrtvtlstkq geeplvrlsl terlgkrkfs aggdsdpplk
      301 rslaqrlgkk veapetnidk tpkkaqvsks lkerlgmsad pdnedatdkv nkvgeihvkt
      361 leeilleras qkrgelqtkl ktegpsktdd stsgarssst iriktfsevl aekkhrqqea
      421 erqkskkdtt ciklkidsei kktvvlppiv asrgqseepa gktksmqevh iktleeikle
      481 kalrvqqsse sstsspsqhe atpgarrllr itkrtgmkee knlqegnevd sqssirteak
      541 easgettgvd itkiqvkrce tmrekhmqkq qereksvltp lrgdvascnt qvaekpvlta
      601 vpgitrhltk rlptkssqkv evetsgigds llnvkcaaqt lekrakpkvn vkpsvvkvvs
      661 spklapkrka vemhaaviaa vkplssssvl qeppakkaav avvplvsedk svtvpeaenp
      721 rdslvlpptq sssdssppev sgpsssqmsm ktrrlssast gkpplsvedd fekliweisg
      781 gkleaeidld pgkdeddlll elsemids
//
LOCUS       NP_001373880             589 aa            linear   PRI 21-NOV-2025
DEFINITION  solute carrier organic anion transporter family member 1A2 isoform
            6 [Homo sapiens].
ACCESSION   NP_001373880
VERSION     NP_001373880.1
DBSOURCE    REFSEQ: accession NM_001386951.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Flogel,S., Tust,M., Boussettaoui,S., Fischer,D. and Grundemann,D.
  TITLE     Enhancing transporter activity in heterologous expression systems
            with SAHA: a 2500-times more potent and odorless alternative to
            butyrate
  JOURNAL   FEBS Open Bio 15 (6), 906-913 (2025)
   PUBMED   40052353
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Kataoka,H., Akiyoshi,T., Uchida,Y., Imaoka,A., Terasaki,T. and
            Ohtani,H.
  TITLE     The Effects of N-Glycosylation on the Expression and Transport
            Activity of OATP1A2 and OATP2B1
  JOURNAL   J Pharm Sci 113 (5), 1376-1384 (2024)
   PUBMED   38432624
  REMARK    GeneRIF: The Effects of N-Glycosylation on the Expression and
            Transport Activity of OATP1A2 and OATP2B1.
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Han,H., Akiyoshi,T., Morita,T., Kataoka,H., Katayama,K., Yajima,K.,
            Imaoka,A. and Ohtani,H.
  TITLE     Comparison of the transport kinetics of fexofenadine and its pH
            dependency among OATP1A2 genetic variants
  JOURNAL   Drug Metab Pharmacokinet 47, 100470 (2022)
   PUBMED   36116173
  REMARK    GeneRIF: Comparison of the transport kinetics of fexofenadine and
            its pH dependency among OATP1A2 genetic variants.
REFERENCE   4  (residues 1 to 589)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 589)
  AUTHORS   Hau,R.K., Klein,R.R., Wright,S.H. and Cherrington,N.J.
  TITLE     Localization of Xenobiotic Transporters Expressed at the Human
            Blood-Testis Barrier
  JOURNAL   Drug Metab Dispos 50 (6), 770-780 (2022)
   PUBMED   35307651
REFERENCE   6  (residues 1 to 589)
  AUTHORS   Kullak-Ublick,G.A., Fisch,T., Oswald,M., Hagenbuch,B., Meier,P.J.,
            Beuers,U. and Paumgartner,G.
  TITLE     Dehydroepiandrosterone sulfate (DHEAS): identification of a carrier
            protein in human liver and brain
  JOURNAL   FEBS Lett 424 (3), 173-176 (1998)
   PUBMED   9539145
REFERENCE   7  (residues 1 to 589)
  AUTHORS   Meier,P.J., Eckhardt,U., Schroeder,A., Hagenbuch,B. and Stieger,B.
  TITLE     Substrate specificity of sinusoidal bile acid and organic anion
            uptake systems in rat and human liver
  JOURNAL   Hepatology 26 (6), 1667-1677 (1997)
   PUBMED   9398014
  REMARK    Review article
REFERENCE   8  (residues 1 to 589)
  AUTHORS   Kullak-Ublick,G.A., Beuers,U., Fahney,C., Hagenbuch,B., Meier,P.J.
            and Paumgartner,G.
  TITLE     Identification and functional characterization of the promoter
            region of the human organic anion transporting polypeptide gene
  JOURNAL   Hepatology 26 (4), 991-997 (1997)
   PUBMED   9328325
REFERENCE   9  (residues 1 to 589)
  AUTHORS   Kullak-Ublick,G.A., Beuers,U., Meier,P.J., Domdey,H. and
            Paumgartner,G.
  TITLE     Assignment of the human organic anion transporting polypeptide
            (OATP) gene to chromosome 12p12 by fluorescence in situ
            hybridization
  JOURNAL   J Hepatol 25 (6), 985-987 (1996)
   PUBMED   9007731
REFERENCE   10 (residues 1 to 589)
  AUTHORS   Kullak-Ublick,G.A., Hagenbuch,B., Stieger,B., Schteingart,C.D.,
            Hofmann,A.F., Wolkoff,A.W. and Meier,P.J.
  TITLE     Molecular and functional characterization of an organic anion
            transporting polypeptide cloned from human liver
  JOURNAL   Gastroenterology 109 (4), 1274-1282 (1995)
   PUBMED   7557095
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022224.22.
            
            Summary: This gene encodes a sodium-independent transporter which
            mediates cellular uptake of organic ions in the liver. Its
            substrates include bile acids, bromosulphophthalein, and some
            steroidal compounds. The protein is a member of the SLC21A family
            of solute carriers. Alternative splicing of this gene results in
            multiple transcript variants. [provided by RefSeq, Dec 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.246085.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..589
                     /product="solute carrier organic anion transporter family
                     member 1A2 isoform 6"
                     /note="organic anion transporting polypeptide A; solute
                     carrier family 21 (organic anion transporter), member 3;
                     sodium-independent organic anion transporter; OATP-1;
                     solute carrier family 21 member 3; organic
                     anion-transporting polypeptide 1"
                     /calculated_mol_wt=64956
     Region          1..517
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            order(13..14,17..18,21,53,152..153,155..157,160,180,
                     183..184,187,305,308..309,312..314,317,346,350,391..392,
                     396,400,461,464..465,468..469,472)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341016"
     CDS             1..589
                     /gene="SLCO1A2"
                     /gene_synonym="OATP; OATP-A; OATP1A2; SLC21A3"
                     /coded_by="NM_001386951.1:167..1936"
                     /note="isoform 6 is encoded by transcript variant 30"
                     /db_xref="GeneID:6579"
                     /db_xref="HGNC:HGNC:10956"
                     /db_xref="MIM:602883"
ORIGIN      
        1 mfllaitcaf vsktlsgsym nsmltqierq fniptslvgf ingsfeignl lliifvsyfg
       61 tklhrpimig igcvvmglgc flkslphflm nqyeyestvs vsgnlssnsf lcmengtqil
      121 rptqdpsect kevkslmwvy vlvgnivrgm getpilplgi syiedfakfe nsplyiglve
      181 tgaiigplig lllasfcanv yvdtgfvntd dliitptdtr wvgawwfgfl icagvnvlta
      241 ipffflpntl pkegletnad iiknenedkq keevkkekyg itkdflpfmk slscnpiyml
      301 filvsviqfn afvnmisfmp kyleqqygis ssdaiflmgi ynlppicigy iigglimkkf
      361 kitvkqaahi gcwlslleyl lyflsflmtc enssvvgint syegipqdly vendifadcn
      421 vdcncpskiw dpvcgnngls ylsaclagce tsigtginmv fqncsciqts gnssavlglc
      481 dkgpdcslml qyflilsams sfiyslaaip gymvllryiy lglpaalrgs sfvpaliili
      541 llrkchlpge nassgtelie tkvkgkenec kdiyqkstvl kddelktkl
//
LOCUS       NP_001284478            1129 aa            linear   PRI 21-NOV-2025
DEFINITION  regulator of nonsense transcripts 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001284478 XP_005260072
VERSION     NP_001284478.1
DBSOURCE    REFSEQ: accession NM_001297549.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1129)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1129)
  AUTHORS   Langer,L.M., Kurscheidt,K., Basquin,J., Bonneau,F., Iermak,I.,
            Basquin,C. and Conti,E.
  TITLE     UPF1 helicase orchestrates mutually exclusive interactions with the
            SMG6 endonuclease and UPF2
  JOURNAL   Nucleic Acids Res 52 (10), 6036-6048 (2024)
   PUBMED   38709891
  REMARK    GeneRIF: UPF1 helicase orchestrates mutually exclusive interactions
            with the SMG6 endonuclease and UPF2.
REFERENCE   3  (residues 1 to 1129)
  AUTHORS   Chapman,J.H., Youle,A.M., Grimme,A.L., Neuman,K.C. and Hogg,J.R.
  TITLE     UPF1 ATPase autoinhibition and activation modulate RNA binding
            kinetics and NMD efficiency
  JOURNAL   Nucleic Acids Res 52 (9), 5376-5391 (2024)
   PUBMED   38412299
  REMARK    GeneRIF: UPF1 ATPase autoinhibition and activation modulate RNA
            binding kinetics and NMD efficiency.
REFERENCE   4  (residues 1 to 1129)
  AUTHORS   Musaev,D., Abdelmessih,M., Vejnar,C.E., Yartseva,V., Weiss,L.A.,
            Strayer,E.C., Takacs,C.M. and Giraldez,A.J.
  TITLE     UPF1 regulates mRNA stability by sensing poorly translated coding
            sequences
  JOURNAL   Cell Rep 43 (4), 114074 (2024)
   PUBMED   38625794
  REMARK    GeneRIF: UPF1 regulates mRNA stability by sensing poorly translated
            coding sequences.
REFERENCE   5  (residues 1 to 1129)
  AUTHORS   Machida,R., Ogawa,T., Min Soe,K. and Moriyama,K.
  TITLE     Nonsense-mediated mRNA decay affects hyperactive root formation in
            oculo-facio-cardio-dental syndrome via up-frameshift protein 1
  JOURNAL   J Oral Biosci 66 (1), 225-231 (2024)
   PUBMED   38244688
  REMARK    GeneRIF: Nonsense-mediated mRNA decay affects hyperactive root
            formation in oculo-facio-cardio-dental syndrome via up-frameshift
            protein 1.
            Erratum:[J Oral Biosci. 2024 Jun;66(2):483. doi:
            10.1016/j.job.2024.03.003. PMID: 38871435]
REFERENCE   6  (residues 1 to 1129)
  AUTHORS   Page,M.F., Carr,B., Anders,K.R., Grimson,A. and Anderson,P.
  TITLE     SMG-2 is a phosphorylated protein required for mRNA surveillance in
            Caenorhabditis elegans and related to Upf1p of yeast
  JOURNAL   Mol Cell Biol 19 (9), 5943-5951 (1999)
   PUBMED   10454541
REFERENCE   7  (residues 1 to 1129)
  AUTHORS   Czaplinski,K., Ruiz-Echevarria,M.J., Paushkin,S.V., Han,X.,
            Weng,Y., Perlick,H.A., Dietz,H.C., Ter-Avanesyan,M.D. and
            Peltz,S.W.
  TITLE     The surveillance complex interacts with the translation release
            factors to enhance termination and degrade aberrant mRNAs
  JOURNAL   Genes Dev 12 (11), 1665-1677 (1998)
   PUBMED   9620853
REFERENCE   8  (residues 1 to 1129)
  AUTHORS   Applequist,S.E., Selg,M., Raman,C. and Jack,H.M.
  TITLE     Cloning and characterization of HUPF1, a human homolog of the
            Saccharomyces cerevisiae nonsense mRNA-reducing UPF1 protein
  JOURNAL   Nucleic Acids Res 25 (4), 814-821 (1997)
   PUBMED   9064659
REFERENCE   9  (residues 1 to 1129)
  AUTHORS   Perlick,H.A., Medghalchi,S.M., Spencer,F.A., Kendzior,R.J. Jr. and
            Dietz,H.C.
  TITLE     Mammalian orthologues of a yeast regulator of nonsense transcript
            stability
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 10928-10932 (1996)
   PUBMED   8855285
REFERENCE   10 (residues 1 to 1129)
  AUTHORS   Horikoshi,M., Sekimizu,K. and Natori,S.
  TITLE     Analysis of the stimulatory factor of RNA polymerase II in the
            initiation and elongation complex
  JOURNAL   J Biol Chem 259 (1), 608-611 (1984)
   PUBMED   6200476
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BE243084.1, BX364728.2,
            U65533.1, D86988.1, AK128727.1 and BM969672.1.
            
            On Jul 3, 2014 this sequence version replaced XP_005260072.1.
            
            Summary: This gene encodes a protein that is part of a
            post-splicing multiprotein complex involved in both mRNA nuclear
            export and mRNA surveillance. mRNA surveillance detects exported
            mRNAs with truncated open reading frames and initiates
            nonsense-mediated mRNA decay (NMD). When translation ends upstream
            from the last exon-exon junction, this triggers NMD to degrade
            mRNAs containing premature stop codons. This protein is located
            only in the cytoplasm. When translation ends, it interacts with the
            protein that is a functional homolog of yeast Upf2p to trigger mRNA
            decapping. Use of multiple polyadenylation sites has been noted for
            this gene. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D86988.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1129
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..1129
                     /product="regulator of nonsense transcripts 1 isoform 1"
                     /EC_number="3.6.4.13"
                     /EC_number="3.6.4.12"
                     /note="delta helicase; smg-2 homolog, nonsense mediated
                     mRNA decay factor; regulator of nonsense transcripts 1;
                     nonsense mRNA reducing factor 1; yeast Upf1p homolog;
                     ATP-dependent helicase RENT1; up-frameshift suppressor 1
                     homolog; up-frameshift mutation 1 homolog; UPF1 regulator
                     of nonsense transcripts homolog"
                     /calculated_mol_wt=124215
     Region          1..415
                     /region_name="Sufficient for interaction with RENT2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92900.2)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92900.2)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92900.2)"
     Region          39..70
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92900.2)"
     Region          121..272
                     /region_name="UPF1_Zn_bind"
                     /note="RNA helicase (UPF2 interacting domain); pfam09416"
                     /db_xref="CDD:401391"
     Region          123..155
                     /region_name="C3H.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01341"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92900.2)"
     Region          137..165
                     /region_name="CC/SHH/C.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01341"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92900.2)"
     Region          183..213
                     /region_name="C4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01341"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92900.2)"
     Region          370..911
                     /region_name="TIGR00376"
                     /note="DNA helicase, putative"
                     /db_xref="CDD:273041"
     Region          481..714
                     /region_name="DEXXQc_UPF1"
                     /note="DEXXQ-box helicase domain of UPF1; cd18039"
                     /db_xref="CDD:350797"
     Site            order(481..483,486,505..511,676,713..714)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350797"
     Site            order(533..535,557..560,611,627,629,680,682)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:350797"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92900.2)"
     Site            956
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92900.2)"
     Region          1009..1058
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92900.2)"
     Site            1019
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q92900.2)"
     Region          1073..1096
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92900.2)"
     Region          1089..1090
                     /region_name="[ST]-Q motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92900.2)"
     Site            1089
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11544179,
                     ECO:0000269|PubMed:16452507; propagated from
                     UniProtKB/Swiss-Prot (Q92900.2)"
     Region          1107..1108
                     /region_name="[ST]-Q motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92900.2)"
     Site            1107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11544179,
                     ECO:0000269|PubMed:16452507, ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92900.2)"
     Region          1110..1129
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92900.2)"
     Site            1110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q92900.2)"
     Site            1127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q92900.2)"
     CDS             1..1129
                     /gene="UPF1"
                     /gene_synonym="HUPF1; NORF1; pNORF1; RENT1; smg-2; UTF"
                     /coded_by="NM_001297549.2:252..3641"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS74315.1"
                     /db_xref="GeneID:5976"
                     /db_xref="HGNC:HGNC:9962"
                     /db_xref="MIM:601430"
ORIGIN      
        1 msveaygpss qtltfldtee aellgadtqg sefeftdftl psqtqtppgg pggpggggag
       61 gpggagagaa agqldaqvgp egilqngavd dsvaktsqll aelnfeedee dtyytkdlpi
      121 hacsycgihd pacvvycnts kkwfcngrgn tsgshivnhl vrakckevtl hkdgplgetv
      181 lecyncgcrn vfllgfipak adsvvvllcr qpcasqsslk dinwdssqwq pliqdrcfls
      241 wlvkipseqe qlrarqitaq qinkleelwk enpsatledl ekpgvdeepq hvllryeday
      301 qyqnifgplv kleadydkkl kesqtqdnit vrwdlglnkk riayftlpkt dsgnedlvii
      361 wlrdmrlmqg deiclrykgd laplwkgigh vikvpdnygd eiaielrssv gapvevthnf
      421 qvdfvwksts fdrmqsalkt favdetsvsg yiyhkllghe vedviikcql pkrftaqglp
      481 dlnhsqvyav ktvlqrplsl iqgppgtgkt vtsativyhl arqgngpvlv capsniavdq
      541 ltekihqtgl kvvrlcaksr eaidspvsfl alhnqirnmd smpelqklqq lkdetgelss
      601 adekryralk rtaerellmn advicctcvg agdprlakmq frsilidest qatepecmvp
      661 vvlgakqlil vgdhcqlgpv vmckkaakag lsqslferlv vlgirpirlq vqyrmhpals
      721 afpsnifyeg slqngvtaad rvkkgfdfqw pqpdkpmffy vtqgqeeias sgtsylnrte
      781 aanvekittk llkagakpdq igiitpyegq rsylvqymqf sgslhtklyq eveiasvdaf
      841 qgrekdfiil scvranehqg igflndprrl nvaltraryg viivgnpkal skqplwnhll
      901 nyykeqkvlv egplnnlres lmqfskprkl vntinpgarf mttamydare aiipgsvydr
      961 ssqgrpssmy fqthdqigmi sagpshvaam nipipfnlvm ppmpppgyfg qangpaagrg
     1021 tpkgktgrgg rqknrfglpg psqtnlpnsq asqdvasqpf sqgaltqgyi smsqpsqmsq
     1081 pglsqpelsq dsylgdefks qidvalsqds tyqgerayqh ggvtglsqy
//
LOCUS       NP_001364927             370 aa            linear   PRI 21-NOV-2025
DEFINITION  protein FAM110B [Homo sapiens].
ACCESSION   NP_001364927 XP_005251382
VERSION     NP_001364927.1
DBSOURCE    REFSEQ: accession NM_001377998.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 370)
  AUTHORS   He,J., Kelly,T.N., Zhao,Q., Li,H., Huang,J., Wang,L., Jaquish,C.E.,
            Sung,Y.J., Shimmin,L.C., Lu,F., Mu,J., Hu,D., Ji,X., Shen,C.,
            Guo,D., Ma,J., Wang,R., Shen,J., Li,S., Chen,J., Mei,H., Chen,C.S.,
            Chen,S., Chen,J., Li,J., Cao,J., Lu,X., Wu,X., Rice,T.K., Gu,C.C.,
            Schwander,K., Hamm,L.L., Liu,D., Rao,D.C., Hixson,J.E. and Gu,D.
  TITLE     Genome-wide association study identifies 8 novel loci associated
            with blood pressure responses to interventions in Han Chinese
  JOURNAL   Circ Cardiovasc Genet 6 (6), 598-607 (2013)
   PUBMED   24165912
REFERENCE   7  (residues 1 to 370)
  AUTHORS   Vainio,P., Wolf,M., Edgren,H., He,T., Kohonen,P., Mpindi,J.P.,
            Smit,F., Verhaegh,G., Schalken,J., Perala,M., Iljin,K. and
            Kallioniemi,O.
  TITLE     Integrative genomic, transcriptomic, and RNAi analysis indicates a
            potential oncogenic role for FAM110B in castration-resistant
            prostate cancer
  JOURNAL   Prostate 72 (7), 789-802 (2012)
   PUBMED   21919029
  REMARK    GeneRIF: FAM110B was able to regulate androgen receptor signaling
            in prostate cancer cells and FAM110B itself was regulated by
            androgens. FAM110B siRNA inhibited the growth of prostate cancer
            cells in vitro.
REFERENCE   8  (residues 1 to 370)
  AUTHORS   Wang,K.S., Liu,X.F. and Aragam,N.
  TITLE     A genome-wide meta-analysis identifies novel loci associated with
            schizophrenia and bipolar disorder
  JOURNAL   Schizophr Res 124 (1-3), 192-199 (2010)
   PUBMED   20889312
REFERENCE   9  (residues 1 to 370)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 370)
  AUTHORS   Hauge,H., Patzke,S. and Aasheim,H.C.
  TITLE     Characterization of the FAM110 gene family
  JOURNAL   Genomics 90 (1), 14-27 (2007)
   PUBMED   17499476
  REMARK    GeneRIF: Localizes to centrosomes and accumulates at the
            microtubule organization center in interphase and at spindle poles
            in mitosis; ectopic expression impairs cell cycle progression in
            the G1 phase.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104350.6 and AC110013.5.
            
            On Jan 23, 2020 this sequence version replaced XP_005251382.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.2845111.1,
                                           SRR1803612.89733.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.1"
     Protein         1..370
                     /product="protein FAM110B"
                     /calculated_mol_wt=40597
     Region          13..118
                     /region_name="FAM110_N"
                     /note="Centrosome-associated N terminus; pfam14161"
                     /db_xref="CDD:464095"
     Region          127..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC76.1)"
     Region          237..256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC76.1)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C739; propagated from
                     UniProtKB/Swiss-Prot (Q8TC76.1)"
     Region          253..361
                     /region_name="FAM110_C"
                     /note="Centrosome-associated C terminus; pfam14160"
                     /db_xref="CDD:464094"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8TC76.1)"
     Region          317..337
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC76.1)"
     CDS             1..370
                     /gene="FAM110B"
                     /gene_synonym="C8orf72"
                     /coded_by="NM_001377998.1:569..1681"
                     /db_xref="CCDS:CCDS6170.1"
                     /db_xref="GeneID:90362"
                     /db_xref="HGNC:HGNC:28587"
                     /db_xref="MIM:611394"
ORIGIN      
        1 mptetlqtgs mvkpvspagt ftsavplril nkgpdyfrrq aepnpkrlsa verleadkak
       61 yvksqevina kqepvkpavl akppvcpaak ralgsptlkv fgnhaktesg vqrenlklei
      121 lkniinsseg sssgsghkhs srnwpphrse atdlhrhsfa eslkvyptqg rrspqeggsh
      181 vgrrlleqsa esflhvshss sdirkvtsvk plkaipcsss applppkpki aaiasmkspe
      241 adpvepacgv srrpslqrsk sdlsdryfrv dadverffny cgldpeelen lgmenfaran
      301 sdiislnfrs asmissdceq sqdsnsdlrn ddsandrvpy gisaiernar iikwlysikq
      361 aresqkvshv
//
LOCUS       NP_001365027             306 aa            linear   PRI 21-NOV-2025
DEFINITION  low-density lipoprotein receptor class A domain-containing protein
            4 isoform alpha 1 [Homo sapiens].
ACCESSION   NP_001365027 XP_024307025
VERSION     NP_001365027.1
DBSOURCE    REFSEQ: accession NM_001378098.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Xie,W., Xiao,H., Luo,J., Zhao,L., Jin,F., Ma,J., Li,J., Xiong,K.,
            Chen,C. and Wang,G.
  TITLE     Identification of low-density lipoprotein receptor class A domain
            containing 4 (LDLRAD4) as a prognostic indicator in primary
            gastrointestinal stromal tumors
  JOURNAL   Curr Probl Cancer 44 (6), 100593 (2020)
   PUBMED   32507364
  REMARK    GeneRIF: Identification of low-density lipoprotein receptor class A
            domain containing 4 (LDLRAD4) as a prognostic indicator in primary
            gastrointestinal stromal tumors.
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 306)
  AUTHORS   Meerabux,J.M., Ohba,H., Iwayama,Y., Maekawa,M.,
            Detera-Wadleigh,S.D., DeLisi,L.E. and Yoshikawa,T.
  TITLE     Analysis of a t(18;21)(p11.1;p11.1) translocation in a family with
            schizophrenia
  JOURNAL   J Hum Genet 54 (7), 386-391 (2009)
   PUBMED   19461657
REFERENCE   7  (residues 1 to 306)
  AUTHORS   Kikuchi,M., Yamada,K., Toyota,T. and Yoshikawa,T.
  TITLE     C18orf1 located on chromosome 18p11.2 may confer susceptibility to
            schizophrenia
  JOURNAL   J Med Dent Sci 50 (3), 225-229 (2003)
   PUBMED   15074360
REFERENCE   8  (residues 1 to 306)
  AUTHORS   Yoshikawa,T., Sanders,A.R., Esterling,L.E. and Detera-Wadleigh,S.D.
  TITLE     Multiple transcriptional variants and RNA editing in C18orf1, a
            novel gene with LDLRA and transmembrane domains on 18p11.2
  JOURNAL   Genomics 47 (2), 246-257 (1998)
   PUBMED   9479497
REFERENCE   9  (residues 1 to 306)
  AUTHORS   Esterling,L.E., Cox Matise,T., Sanders,A.R., Yoshikawa,T.,
            Overhauser,J., Gershon,E.S., Moskowitz,M.T. and
            Detera-Wadleigh,S.D.
  TITLE     An integrated physical map of 18p11.2: a susceptibility region for
            bipolar disorder
  JOURNAL   Mol Psychiatry 2 (6), 501-504 (1997)
   PUBMED   9399696
REFERENCE   10 (residues 1 to 306)
  AUTHORS   Yoshikawa,T., Sanders,A.R., Esterling,L.E., Overhauser,J.,
            Garnes,J.A., Lennon,G., Grewal,R. and Detera-Wadleigh,S.D.
  TITLE     Isolation of chromosome 18-specific brain transcripts as positional
            candidates for bipolar disorder
  JOURNAL   Am J Med Genet 74 (2), 140-149 (1997)
   PUBMED   9129712
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP002505.3, AP002439.3 and AP001010.4.
            
            On Jan 28, 2020 this sequence version replaced XP_024307025.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138515.60460.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145122, SAMEA2153733
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.21"
     Protein         1..306
                     /product="low-density lipoprotein receptor class A
                     domain-containing protein 4 isoform alpha 1"
                     /note="clone 22; low-density lipoprotein receptor class A
                     domain-containing protein 4"
                     /calculated_mol_wt=33769
     Region          16..47
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(17,25,37..38)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(30,33,37,43..44)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            40..44
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            65..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15165.1)"
     Region          180..183
                     /region_name="PPxY motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O15165.1)"
     Region          208..211
                     /region_name="SMAD interaction motif (SIM)"
                     /note="propagated from UniProtKB/Swiss-Prot (O15165.1)"
     Region          252..255
                     /region_name="PPxY motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O15165.1)"
     Region          286..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15165.1)"
     CDS             1..306
                     /gene="LDLRAD4"
                     /gene_synonym="C18orf1"
                     /coded_by="NM_001378098.1:672..1592"
                     /note="isoform alpha 1 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS32793.1"
                     /db_xref="GeneID:753"
                     /db_xref="HGNC:HGNC:1224"
                     /db_xref="MIM:606571"
ORIGIN      
        1 mpeagfqatn afteckftct sgkclylgsl vcnqqndcgd nsdeencllv tehpppgifn
       61 selefaqiii ivvvvtvmvv vivcllnhyk vstrsfinrp nqsrrredgl pqegclwpsd
      121 saaprlgase imhaprsrdr ftapsfiqrd rfsrfqptyp yvqheidlpp tislsdgeep
      181 ppyqgpctlq lrdpeqqmel nresvrappn rtifdsdlid iamysggpcp pssnsgisas
      241 tcssngrmeg ppptysevmg hhpgasflhh qrsnahrgsr lqfqqnnaes tivpikgkdr
      301 kpgnlv
//
LOCUS       NP_001030087             677 aa            linear   PRI 21-NOV-2025
DEFINITION  epithelial splicing regulatory protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001030087
VERSION     NP_001030087.2
DBSOURCE    REFSEQ: accession NM_001034915.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Wang,P., Gao,X., Zheng,W. and Zhang,J.
  TITLE     Potential impact of epithelial splicing regulatory protein 1
            (ESRP1) associated with tumor immunity in pancreatic adenocarcinoma
  JOURNAL   J Proteomics 308, 105277 (2024)
   PUBMED   39127164
  REMARK    GeneRIF: Potential impact of epithelial splicing regulatory protein
            1 (ESRP1) associated with tumor immunity in pancreatic
            adenocarcinoma.
REFERENCE   3  (residues 1 to 677)
  AUTHORS   Chen,S., Zong,Y., Hou,Z., Deng,Z. and Xia,Z.
  TITLE     Splicing factor ESRP1 derived circ_0068162 promotes the progression
            of oral squamous cell carcinoma via the miR-186/JAG axis
  JOURNAL   Carcinogenesis 45 (3), 107-118 (2024)
   PUBMED   37966490
  REMARK    GeneRIF: Splicing factor ESRP1 derived circ_0068162 promotes the
            progression of oral squamous cell carcinoma via the miR-186/JAG
            axis.
REFERENCE   4  (residues 1 to 677)
  AUTHORS   Liu,D., Dredge,B.K., Bert,A.G., Pillman,K.A., Toubia,J., Guo,W.,
            Dyakov,B.J.A., Migault,M.M., Conn,V.M., Conn,S.J., Gregory,P.A.,
            Gingras,A.C., Patel,D., Wu,B. and Goodall,G.J.
  TITLE     ESRP1 controls biogenesis and function of a large abundant
            multiexon circRNA
  JOURNAL   Nucleic Acids Res 52 (3), 1387-1403 (2024)
   PUBMED   38015468
  REMARK    GeneRIF: ESRP1 controls biogenesis and function of a large abundant
            multiexon circRNA.
REFERENCE   5  (residues 1 to 677)
  AUTHORS   Wang,W., Taufalele,P.V., Millet,M., Homsy,K., Smart,K.,
            Berestesky,E.D., Schunk,C.T., Rowe,M.M., Bordeleau,F. and
            Reinhart-King,C.A.
  TITLE     Matrix stiffness regulates tumor cell intravasation through
            expression and ESRP1-mediated alternative splicing of MENA
  JOURNAL   Cell Rep 42 (4), 112338 (2023)
   PUBMED   37027295
  REMARK    GeneRIF: Matrix stiffness regulates tumor cell intravasation
            through expression and ESRP1-mediated alternative splicing of MENA.
REFERENCE   6  (residues 1 to 677)
  AUTHORS   Warzecha,C.C., Shen,S., Xing,Y. and Carstens,R.P.
  TITLE     The epithelial splicing factors ESRP1 and ESRP2 positively and
            negatively regulate diverse types of alternative splicing events
  JOURNAL   RNA Biol 6 (5), 546-562 (2009)
   PUBMED   19829082
  REMARK    GeneRIF: results further establish ESRP1 and ESRP2 as global
            regulators of an epithelial splicing regulatory network.
REFERENCE   7  (residues 1 to 677)
  AUTHORS   Warzecha,C.C., Sato,T.K., Nabet,B., Hogenesch,J.B. and
            Carstens,R.P.
  TITLE     ESRP1 and ESRP2 are epithelial cell-type-specific regulators of
            FGFR2 splicing
  JOURNAL   Mol Cell 33 (5), 591-601 (2009)
   PUBMED   19285943
  REMARK    GeneRIF: ESRP1 and ESRP2 are epithelial cell-type-specific
            regulators of FGFR2 splicing.
REFERENCE   8  (residues 1 to 677)
  AUTHORS   Leontieva,O.V. and Ionov,Y.
  TITLE     RNA-binding motif protein 35A is a novel tumor suppressor for
            colorectal cancer
  JOURNAL   Cell Cycle 8 (3), 490-497 (2009)
   PUBMED   19177006
  REMARK    GeneRIF: Results demonstrate that RBM35A functions as a tumor
            suppressor in colon cancer cells, and suggest that RBM35A is
            involved in posttranscriptional regulation of a number of genes by
            exerting a differential effect on protein translation via 5'UTRs of
            mRNAs.
REFERENCE   9  (residues 1 to 677)
  AUTHORS   Rohan,S., Tu,J.J., Kao,J., Mukherjee,P., Campagne,F., Zhou,X.K.,
            Hyjek,E., Alonso,M.A. and Chen,Y.T.
  TITLE     Gene expression profiling separates chromophobe renal cell
            carcinoma from oncocytoma and identifies vesicular transport and
            cell junction proteins as differentially expressed genes
  JOURNAL   Clin Cancer Res 12 (23), 6937-6945 (2006)
   PUBMED   17145811
  REMARK    GeneRIF: The FLJ20171 gene was shown to effectively separate these
            two chromophobe renal cell carcinoma (RCC) and benign oncocytoma
            groups by quantitative reverse transcription-PCR using fresh tissue
            samples, with similar trends seen on formalin-fixed tissues.
REFERENCE   10 (residues 1 to 677)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC099916.1, BC052574.1, BX647570.1, BG212336.1, BG182742.1 and
            AI990751.1.
            
            On Mar 25, 2008 this sequence version replaced NP_001030087.1.
            
            Summary: ESPR1 is an epithelial cell-type-specific splicing
            regulator (Warzecha et al., 2009 [PubMed 19285943]).[supplied by
            OMIM, Aug 2009].
            
            Transcript Variant: This variant (2) lacks a segment in the 3'
            coding region, compared to variant 1, that results in a shorter
            protein (isoform 2) when compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC099916.1, SRR14038191.63460.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.1"
     Protein         1..677
                     /product="epithelial splicing regulatory protein 1 isoform
                     2"
                     /note="RNA-binding protein 35A; RNA-binding motif protein
                     35A"
                     /calculated_mol_wt=75013
     Region          29..168
                     /region_name="DnaQ_like_exo"
                     /note="DnaQ-like (or DEDD) 3'-5' exonuclease domain
                     superfamily; cl10012"
                     /db_xref="CDD:447876"
     Region          216..308
                     /region_name="RRM1_ESRP1"
                     /note="RNA recognition motif 1 (RRM1) found in epithelial
                     splicing regulatory protein 1 (ESRP1) and similar
                     proteins; cd12736"
                     /db_xref="CDD:410134"
     Region          310..419
                     /region_name="RRM2_ESRP1"
                     /note="RNA recognition motif 2 (RRM2) found in epithelial
                     splicing regulatory protein 1 (ESRP1) and similar
                     proteins; cd12739"
                     /db_xref="CDD:410136"
     Region          444..524
                     /region_name="RRM3_ESRP1_ESRP2"
                     /note="RNA recognition motif 3 (RRM3) found in epithelial
                     splicing regulatory protein ESRP1, ESRP2 and similar
                     proteins; cd12742"
                     /db_xref="CDD:410138"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6T0; propagated from
                     UniProtKB/Swiss-Prot (Q6NXG1.2)"
     Site            578
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q6NXG1.2)"
     Region          629..>668
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     CDS             1..677
                     /gene="ESRP1"
                     /gene_synonym="DFNB109; RBM35A; RMB35A"
                     /coded_by="NM_001034915.3:146..2179"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47898.1"
                     /db_xref="GeneID:54845"
                     /db_xref="HGNC:HGNC:25966"
                     /db_xref="MIM:612959"
ORIGIN      
        1 mtaspdylvv lfgitagatg aklgsdekel illfwkvvdl ankkvgqlhe vlvrpdqlel
       61 tedckeetki dveslssasq ldqalrqfnq svsnelnigv gtsfclctdg qlhvrqilhp
      121 easkknvllp ecfysffdlr kefkkccpgs pdidkldvat mteylnfeks ssvsrygasq
      181 vedmgniila misepynhrf sdpervnykf esgtcskmel iddntvvrar glpwqssdqd
      241 iarffkglni akggaalcln aqgrrngeal vrfvseehrd lalqrhkhhm gtryievyka
      301 tgedflkiag gtsnevaqfl skenqvivrm rglpftatae evvaffgqhc pitggkegil
      361 fvtypdgrpt gdafvlface eyaqnalrkh kdllgkryie lfrstaaevq qvlnrfssap
      421 liplptppii pvlpqqfvpp tnvrdcirlr glpyaatied ildflgefat dirthgvhmv
      481 lnhqgrpsgd afiqmksadr afmaaqkchk knmkdryvev fqcsaeemnf vlmggtlnrn
      541 glspppclsp psytfpapaa vipteaaiyq psvilnpral qpstayypag tqlfmnytay
      601 ypsppgspns lgyfptaanl sgvppqpgtv vrmqglaynt gvkeilnffq gyqyatedgl
      661 ihtndqartl pkewvci
//
LOCUS       NP_000483               1480 aa            linear   PRI 21-NOV-2025
DEFINITION  cystic fibrosis transmembrane conductance regulator [Homo sapiens].
ACCESSION   NP_000483
VERSION     NP_000483.3
DBSOURCE    REFSEQ: accession NM_000492.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1480)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   2  (residues 1 to 1480)
  AUTHORS   Hong,J.S., Tindall,J.M., Tindall,S.R. and Sorscher,E.J.
  TITLE     Mutation accumulation in H. sapiens F508del CFTR countermands dN/dS
            type genomic analysis
  JOURNAL   PLoS One 19 (7), e0305832 (2024)
   PUBMED   39024311
  REMARK    GeneRIF: Mutation accumulation in H. sapiens F508del CFTR
            countermands dN/dS type genomic analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1480)
  AUTHORS   Merigo,F., Lagni,A., Boschi,F., Bernardi,P., Conti,A., Plebani,R.,
            Romano,M., Sorio,C., Lotti,V. and Sbarbati,A.
  TITLE     Loss of CFTR Reverses Senescence Hallmarks in SARS-CoV-2 Infected
            Bronchial Epithelial Cells
  JOURNAL   Int J Mol Sci 25 (11), 6185 (2024)
   PUBMED   38892373
  REMARK    GeneRIF: Loss of CFTR Reverses Senescence Hallmarks in SARS-CoV-2
            Infected Bronchial Epithelial Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1480)
  AUTHORS   Al Abdulsalam,E.A.
  TITLE     Insights and considerations on CFTR variant reporting in a study of
            cystic fibrosis patients in Saudi Arabia CFTR 1548del G and 1549del
            G: Navigating the discovery of novel mutations
  JOURNAL   Saudi Med J 45 (5), 541 (2024)
   PUBMED   38734430
  REMARK    GeneRIF: Insights and considerations on CFTR variant reporting in a
            study of cystic fibrosis patients in Saudi Arabia CFTR 1548del G
            and 1549del G: Navigating the discovery of novel mutations.
REFERENCE   5  (residues 1 to 1480)
  AUTHORS   Shelton,C., LaRusch,J. and Whitcomb,D.C.
  TITLE     Pancreatitis Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24624459
REFERENCE   6  (residues 1 to 1480)
  AUTHORS   Savant,A., Lyman,B., Bojanowski,C. and Upadia,J.
  TITLE     Cystic Fibrosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301428
REFERENCE   7  (residues 1 to 1480)
  AUTHORS   Lissens,W., Bonduelle,M., Malfroot,A., Dab,I. and Liebaers,I.
  TITLE     A serine to proline substitution (S1255P) in the second nucleotide
            binding fold of the cystic fibrosis gene
  JOURNAL   Hum Mol Genet 1 (6), 441-442 (1992)
   PUBMED   1284530
REFERENCE   8  (residues 1 to 1480)
  AUTHORS   Shackleton,S., Beards,F. and Harris,A.
  TITLE     Detection of novel and rare mutations in exon 4 of the cystic
            fibrosis gene by SSCP
  JOURNAL   Hum Mol Genet 1 (6), 439-440 (1992)
   PUBMED   1284529
REFERENCE   9  (residues 1 to 1480)
  AUTHORS   Cheadle,J.P., Meredith,A.L. and al-Jader,L.N.
  TITLE     A new missense mutation (R1283M) in exon 20 of the cystic fibrosis
            transmembrane conductance regulator gene
  JOURNAL   Hum Mol Genet 1 (2), 123-125 (1992)
   PUBMED   1284468
REFERENCE   10 (residues 1 to 1480)
  AUTHORS   Jones,C.T., McIntosh,I., Keston,M., Ferguson,A. and Brock,D.J.
  TITLE     Three novel mutations in the cystic fibrosis gene detected by
            chemical cleavage: analysis of variant splicing and a nonsense
            mutation
  JOURNAL   Hum Mol Genet 1 (1), 11-17 (1992)
   PUBMED   1284466
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M28668.1, AC000111.1 and
            AC000061.1.
            
            On Mar 24, 2006 this sequence version replaced NP_000483.2.
            
            Summary: This gene encodes a member of the ATP-binding cassette
            (ABC) transporter superfamily. The encoded protein functions as a
            chloride channel, making it unique among members of this protein
            family, and controls ion and water secretion and absorption in
            epithelial tissues. Channel activation is mediated by cycles of
            regulatory domain phosphorylation, ATP-binding by the
            nucleotide-binding domains, and ATP hydrolysis. Mutations in this
            gene cause cystic fibrosis, the most common lethal genetic disorder
            in populations of Northern European descent. The most frequently
            occurring mutation in cystic fibrosis, DeltaF508, results in
            impaired folding and trafficking of the encoded protein. Multiple
            pseudogenes have been identified in the human genome. [provided by
            RefSeq, Aug 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M28668.1, SRR18074969.707190.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000003084.11/ ENSP00000003084.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1480
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.2"
     Protein         1..1480
                     /product="cystic fibrosis transmembrane conductance
                     regulator"
                     /EC_number="5.6.1.6"
                     /note="cAMP-dependent chloride channel; channel
                     conductance-controlling ATPase; cystic fibrosis
                     transmembrane conductance regulator (ATP-binding cassette
                     sub-family C, member 7); cystic fibrosis transmembrane
                     conductance regulating"
                     /calculated_mol_wt=168011
     Region          1..1480
                     /region_name="CFTR_protein"
                     /note="cystic fibrosis transmembrane conductor regulator
                     (CFTR); TIGR01271"
                     /db_xref="CDD:273530"
     Site            78..98
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            123..146
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            196..216
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            223..243
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            299..319
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            340..358
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            549
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P13569.3)"
     Region          654..831
                     /region_name="Disordered R region.
                     /evidence=ECO:0000269|PubMed:10792060"
                     /note="propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:1377674,
                     ECO:0000269|PubMed:22119790, ECO:0000269|PubMed:25330774,
                     ECO:0000269|PubMed:9385646; propagated from
                     UniProtKB/Swiss-Prot (P13569.3)"
     Site            670
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:25330774; propagated from
                     UniProtKB/Swiss-Prot (P13569.3)"
     Site            686
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000269|PubMed:1377674,
                     ECO:0000269|PubMed:22119790; propagated from
                     UniProtKB/Swiss-Prot (P13569.3)"
     Site            700
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:1377674,
                     ECO:0000269|PubMed:22119790, ECO:0000269|PubMed:25330774,
                     ECO:0000269|PubMed:9385646; propagated from
                     UniProtKB/Swiss-Prot (P13569.3)"
     Site            712
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:22119790,
                     ECO:0000269|PubMed:25330774, ECO:0000269|PubMed:9385646;
                     propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            717
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:22119790; propagated from
                     UniProtKB/Swiss-Prot (P13569.3)"
     Site            737
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:1377674,
                     ECO:0000269|PubMed:22119790, ECO:0000269|PubMed:25330774,
                     ECO:0000269|PubMed:9385646; propagated from
                     UniProtKB/Swiss-Prot (P13569.3)"
     Site            753
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:25330774,
                     ECO:0000269|PubMed:9385646; propagated from
                     UniProtKB/Swiss-Prot (P13569.3)"
     Site            768
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:1377674,
                     ECO:0000269|PubMed:25330774, ECO:0000269|PubMed:9385646;
                     propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            790
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000269|PubMed:1377674; propagated from
                     UniProtKB/Swiss-Prot (P13569.3)"
     Site            795
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:1377674,
                     ECO:0000269|PubMed:22119790, ECO:0000269|PubMed:25330774,
                     ECO:0000269|PubMed:9385646; propagated from
                     UniProtKB/Swiss-Prot (P13569.3)"
     Site            813
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:1377674,
                     ECO:0000269|PubMed:25330774, ECO:0000269|PubMed:9385646;
                     propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            859..879
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            894
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7518437,
                     ECO:0000305|PubMed:20008117; propagated from
                     UniProtKB/Swiss-Prot (P13569.3)"
     Site            900
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7518437,
                     ECO:0000305|PubMed:20008117; propagated from
                     UniProtKB/Swiss-Prot (P13569.3)"
     Site            919..939
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            991..1011
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            1014..1034
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            1096..1116
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            1131..1151
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Region          1386..1480
                     /region_name="Interaction with GORASP2.
                     /evidence=ECO:0000269|PubMed:21884936"
                     /note="propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            1444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22119790; propagated from
                     UniProtKB/Swiss-Prot (P13569.3)"
     Region          1452..1480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13569.3)"
     Site            1456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22119790; propagated from
                     UniProtKB/Swiss-Prot (P13569.3)"
     Region          1478..1480
                     /region_name="PDZ-binding.
                     /evidence=ECO:0000269|PubMed:11707463,
                     ECO:0000269|PubMed:16331976"
                     /note="propagated from UniProtKB/Swiss-Prot (P13569.3)"
     CDS             1..1480
                     /gene="CFTR"
                     /gene_synonym="ABC35; ABCC7; CF; CFTR/MRP; dJ760C5.1;
                     MRP7; TNR-CFTR"
                     /coded_by="NM_000492.4:71..4513"
                     /db_xref="CCDS:CCDS5773.1"
                     /db_xref="GeneID:1080"
                     /db_xref="HGNC:HGNC:1884"
                     /db_xref="MIM:602421"
ORIGIN      
        1 mqrsplekas vvsklffswt rpilrkgyrq rlelsdiyqi psvdsadnls eklerewdre
       61 laskknpkli nalrrcffwr fmfygiflyl gevtkavqpl llgriiasyd pdnkeersia
      121 iylgiglcll fivrtlllhp aifglhhigm qmriamfsli ykktlklssr vldkisigql
      181 vsllsnnlnk fdeglalahf vwiaplqval lmgliwellq asafcglgfl ivlalfqagl
      241 grmmmkyrdq ragkiserlv itsemieniq svkaycweea mekmienlrq telkltrkaa
      301 yvryfnssaf ffsgffvvfl svlpyalikg iilrkiftti sfcivlrmav trqfpwavqt
      361 wydslgaink iqdflqkqey ktleynlttt evvmenvtaf weegfgelfe kakqnnnnrk
      421 tsngddslff snfsllgtpv lkdinfkier gqllavagst gagktsllmv imgelepseg
      481 kikhsgrisf csqfswimpg tikeniifgv sydeyryrsv ikacqleedi skfaekdniv
      541 lgeggitlsg gqrarislar avykdadlyl ldspfgyldv ltekeifesc vcklmanktr
      601 ilvtskmehl kkadkililh egssyfygtf selqnlqpdf ssklmgcdsf dqfsaerrns
      661 iltetlhrfs legdapvswt etkkqsfkqt gefgekrkns ilnpinsirk fsivqktplq
      721 mngieedsde plerrlslvp dseqgeailp risvistgpt lqarrrqsvl nlmthsvnqg
      781 qnihrkttas trkvslapqa nlteldiysr rlsqetglei seeineedlk ecffddmesi
      841 pavttwntyl ryitvhksli fvliwclvif laevaaslvv lwllgntplq dkgnsthsrn
      901 nsyaviitst ssyyvfyiyv gvadtllamg ffrglplvht litvskilhh kmlhsvlqap
      961 mstlntlkag gilnrfskdi ailddllplt ifdfiqllli vigaiavvav lqpyifvatv
     1021 pvivafimlr ayflqtsqql kqlesegrsp ifthlvtslk glwtlrafgr qpyfetlfhk
     1081 alnlhtanwf lylstlrwfq mriemifvif fiavtfisil ttgegegrvg iiltlamnim
     1141 stlqwavnss idvdslmrsv srvfkfidmp tegkptkstk pykngqlskv miienshvkk
     1201 ddiwpsggqm tvkdltakyt eggnaileni sfsispgqrv gllgrtgsgk stllsaflrl
     1261 lntegeiqid gvswdsitlq qwrkafgvip qkvfifsgtf rknldpyeqw sdqeiwkvad
     1321 evglrsvieq fpgkldfvlv dggcvlshgh kqlmclarsv lskakillld epsahldpvt
     1381 yqiirrtlkq afadctvilc ehrieamlec qqflvieenk vrqydsiqkl lnerslfrqa
     1441 ispsdrvklf phrnsskcks kpqiaalkee teeevqdtrl
//
LOCUS       NP_001317254             561 aa            linear   PRI 21-NOV-2025
DEFINITION  non-homologous end joining factor IFFO1 isoform 8 [Homo sapiens].
ACCESSION   NP_001317254 XP_016874660
VERSION     NP_001317254.1
DBSOURCE    REFSEQ: accession NM_001330325.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Yu,H., Liu,P. and Chen,T.
  TITLE     CircIFFO1 suppresses tumor growth and metastasis of cutaneous
            squamous cell carcinoma by targeting the miR-424-5p/NFIB axis
  JOURNAL   Arch Dermatol Res 315 (9), 2585-2596 (2023)
   PUBMED   37405427
  REMARK    GeneRIF: CircIFFO1 suppresses tumor growth and metastasis of
            cutaneous squamous cell carcinoma by targeting the miR-424-5p/NFIB
            axis.
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Zhang,Y., Qiu,J.G., Jia,X.Y., Ke,Y., Zhang,M.K., Stieg,D.,
            Liu,W.J., Liu,L.Z., Wang,L. and Jiang,B.H.
  TITLE     METTL3-mediated N6-methyladenosine modification and HDAC5/YY1
            promote IFFO1 downregulation in tumor development and
            chemo-resistance
  JOURNAL   Cancer Lett 553, 215971 (2023)
   PUBMED   36257380
  REMARK    GeneRIF: METTL3-mediated N6-methyladenosine modification and
            HDAC5/YY1 promote IFFO1 downregulation in tumor development and
            chemo-resistance.
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 561)
  AUTHORS   Li,W., Bai,X., Li,J., Zhao,Y., Liu,J., Zhao,H., Liu,L., Ding,M.,
            Wang,Q., Shi,F.Y., Hou,M., Ji,J., Gao,G., Guo,R., Sun,Y., Liu,Y.
            and Xu,D.
  TITLE     The nucleoskeleton protein IFFO1 immobilizes broken DNA and
            suppresses chromosome translocation during tumorigenesis
  JOURNAL   Nat Cell Biol 21 (10), 1273-1285 (2019)
   PUBMED   31548606
  REMARK    GeneRIF: The lamin A/C-IFFO1-constituted nucleoskeleton prevents
            chromosome translocation by immobilizing broken DNA ends during
            tumorigenesis.
REFERENCE   6  (residues 1 to 561)
  AUTHORS   Tureci,O., Sahin,U., Koslowski,M., Buss,B., Bell,C., Ballweber,P.,
            Zwick,C., Eberle,T., Zuber,M., Villena-Heinsen,C., Seitz,G. and
            Pfreundschuh,M.
  TITLE     A novel tumour associated leucine zipper protein targeting to sites
            of gene transcription and splicing
  JOURNAL   Oncogene 21 (24), 3879-3888 (2002)
   PUBMED   12032826
REFERENCE   7  (residues 1 to 561)
  AUTHORS   Steinert,P.M. and Roop,D.R.
  TITLE     Molecular and cellular biology of intermediate filaments
  JOURNAL   Annu Rev Biochem 57, 593-625 (1988)
   PUBMED   3052284
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM147696.1, AL548672.3,
            AC006064.10, AF124432.1, BE410988.1, BC001790.1 and AA251428.1.
            
            On Aug 23, 2016 this sequence version replaced XP_016874660.1.
            
            Summary: This gene is a member of the intermediate filament family.
            Intermediate filaments are proteins which are primordial components
            of the cytoskeleton and nuclear envelope. The proteins encoded by
            the members of this gene family are evolutionarily and structurally
            related but have limited sequence homology, with the exception of
            the central rod domain. Multiple alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2010].
            
            Transcript Variant: This variant (9) uses an alternate in-frame
            splice site in the central coding region, compared to variant 2,
            resulting in an isoform (8) that is 1 aa shorter than isoform 2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..561
                     /product="non-homologous end joining factor IFFO1 isoform
                     8"
                     /note="intermediate filament-like MGC:2625; NHEJ factor
                     IFFO1; non-homologous end joining factor IFFO1"
                     /calculated_mol_wt=62089
     Region          21..57
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0D2I5.2)"
     Region          65..116
                     /region_name="LMNA binding.
                     /evidence=ECO:0000269|PubMed:31548606"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0D2I5.2)"
     Region          158..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0D2I5.2)"
     Region          230..520
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          362..396
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0D2I5.2)"
     Region          452..527
                     /region_name="XCCR4 binding. Required for localization to
                     the double-strand breaks (DSBs).
                     /evidence=ECO:0000269|PubMed:31548606"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0D2I5.2)"
     Region          522..561
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0D2I5.2)"
     CDS             1..561
                     /gene="IFFO1"
                     /gene_synonym="HOM-TES-103; IFFO"
                     /coded_by="NM_001330325.2:14..1699"
                     /note="isoform 8 is encoded by transcript variant 9"
                     /db_xref="GeneID:25900"
                     /db_xref="HGNC:HGNC:24970"
                     /db_xref="MIM:610495"
ORIGIN      
        1 mnplfgpnlf llqqeqqgla gplgdslggd hfagggdlpp aplspagpaa ysppgpgpap
       61 paamalrndl gsninvlktl nlrfrcflak vhelerrnrl lekqlqqale egkqgrrglg
      121 rrdqavqtgf vspirplglq lgarpaavcs psarvlgspa rspagplaps aaslssssts
      181 tsttysssar fmpgtiwsfs harrlgpgle ptlvqgpgls wvhpdgvgvq idtitpeira
      241 lynvlakvkr erdeykrrwe eeytvriqlq drvnelqeea qeadacqeel alkveqlkae
      301 lvvfkglmsn nlseldtkiq ekamkvdmdi crriditakl cdvaqqrnce dmiqmfqklv
      361 psmggrkrer kaaveedtsl sesegprqpd gdeeestals ineemqrmln qlreydfedd
      421 cdsltweete etlllwedfs gyamaaaeaq geqedslekv ikdteslfkt rekeyqetid
      481 qielelatak ndmnrhlhey memcsmkrgl dvqmetcrrl itqsgdrksp aftavplsdp
      541 ppppseaeds drdvssdssm r
//
LOCUS       NP_054902                 96 aa            linear   PRI 21-NOV-2025
DEFINITION  dynein light chain roadblock-type 1 isoform a [Homo sapiens].
ACCESSION   NP_054902
VERSION     NP_054902.1
DBSOURCE    REFSEQ: accession NM_014183.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 96)
  AUTHORS   Canty,J.T., Tan,R., Kusakci,E., Fernandes,J. and Yildiz,A.
  TITLE     Structure and Mechanics of Dynein Motors
  JOURNAL   Annu Rev Biophys 50, 549-574 (2021)
   PUBMED   33957056
  REMARK    Review article
REFERENCE   4  (residues 1 to 96)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 96)
  AUTHORS   Vuolo,L., Stevenson,N.L., Mukhopadhyay,A.G., Roberts,A.J. and
            Stephens,D.J.
  TITLE     Cytoplasmic dynein-2 at a glance
  JOURNAL   J Cell Sci 133 (6) (2020)
   PUBMED   32229580
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 96)
  AUTHORS   Pfister,K.K., Fisher,E.M., Gibbons,I.R., Hays,T.S., Holzbaur,E.L.,
            McIntosh,J.R., Porter,M.E., Schroer,T.A., Vaughan,K.T.,
            Witman,G.B., King,S.M. and Vallee,R.B.
  TITLE     Cytoplasmic dynein nomenclature
  JOURNAL   J Cell Biol 171 (3), 411-413 (2005)
   PUBMED   16260502
REFERENCE   7  (residues 1 to 96)
  AUTHORS   Tang,Q., Staub,C.M., Gao,G., Jin,Q., Wang,Z., Ding,W.,
            Aurigemma,R.E. and Mulder,K.M.
  TITLE     A novel transforming growth factor-beta receptor-interacting
            protein that is also a light chain of the motor protein dynein
  JOURNAL   Mol Biol Cell 13 (12), 4484-4496 (2002)
   PUBMED   12475967
REFERENCE   8  (residues 1 to 96)
  AUTHORS   Susalka,S.J., Nikulina,K., Salata,M.W., Vaughan,P.S., King,S.M.,
            Vaughan,K.T. and Pfister,K.K.
  TITLE     The roadblock light chain binds a novel region of the cytoplasmic
            Dynein intermediate chain
  JOURNAL   J Biol Chem 277 (36), 32939-32946 (2002)
   PUBMED   12077152
REFERENCE   9  (residues 1 to 96)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Ray,S., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human retina for the NEIBank
            Project: retbindin, an abundant, novel retinal cDNA and alternative
            splicing of other retina-preferred gene transcripts
  JOURNAL   Mol Vis 8, 196-204 (2002)
   PUBMED   12107411
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 96)
  AUTHORS   Jiang,J., Yu,L., Huang,X., Chen,X., Li,D., Zhang,Y., Tang,L. and
            Zhao,S.
  TITLE     Identification of two novel human dynein light chain genes, DNLC2A
            and DNLC2B, and their expression changes in hepatocellular
            carcinoma tissues from 68 Chinese patients
  JOURNAL   Gene 281 (1-2), 103-113 (2001)
   PUBMED   11750132
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109923.29 and AL136173.24.
            
            Summary: This gene is a member of the roadblock dynein light chain
            family. The encoded cytoplasmic protein is capable of binding
            intermediate chain proteins, interacts with transforming growth
            factor-beta, and has been implicated in the regulation of actin
            modulating proteins. Upregulation of this gene has been associated
            with hepatocellular carcinomas, suggesting that this gene may be
            involved in tumor progression. Alternative splicing results in
            multiple transcript variants. Pseudogenes of this gene have been
            defined on chromosomes 12 and 18. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (1), as well as variant 8, encodes
            isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA734845.1, BQ056781.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357156.7/ ENSP00000349679.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..96
                     /product="dynein light chain roadblock-type 1 isoform a"
                     /note="dynein, cytoplasmic, light polypeptide 2A;
                     bithoraxoid-like protein; dynein-associated protein Km23;
                     ROBL/LC7-like 1; roadblock domain-containing protein 1"
                     /calculated_mol_wt=10790
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P62628; propagated from
                     UniProtKB/Swiss-Prot (Q9NP97.3)"
     Region          3..93
                     /region_name="Robl_LC7"
                     /note="Roadblock/LC7 domain; pfam03259"
                     /db_xref="CDD:397386"
     CDS             1..96
                     /gene="DYNLRB1"
                     /gene_synonym="BITH; BLP; DNCL2A; DNLC2A; ROBLD1"
                     /coded_by="NM_014183.4:38..328"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13235.1"
                     /db_xref="GeneID:83658"
                     /db_xref="HGNC:HGNC:15468"
                     /db_xref="MIM:607167"
ORIGIN      
        1 maeveetlkr lqsqkgvqgi ivvntegipi kstmdnpttt qyaslmhsfi lkarstvrdi
       61 dpqndltflr irskkneimv apdkdyfliv iqnpte
//
LOCUS       NP_001371683            1120 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 38 [Homo sapiens].
ACCESSION   NP_001371683
VERSION     NP_001371683.1
DBSOURCE    REFSEQ: accession NM_001384754.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1120)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1120)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1120)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1120)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1120)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1120)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1120)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1120)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1120)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1120)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.875663.1,
                                           SRR18074969.1029755.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1120
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1120
                     /product="microtubule-associated protein 4 isoform 38"
                     /note="MAP-4"
                     /calculated_mol_wt=117510
     Region          <575..919
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <931..952
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          992..1021
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          1023..1053
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1120
                     /gene="MAP4"
                     /coded_by="NM_001384754.1:96..3458"
                     /note="isoform 38 is encoded by transcript variant 27"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgsp tefleekmay qeypnsqnwp
      121 edtnfcfqpe qvvdpiqtdp fkmyhdddla dlvfpssata dtsifagqnd plkdsygmsp
      181 cntavvpqgw svealnsphs esfvspeava eppqptavpl elakeiemas eerppaqale
      241 immglkttdm apsketemal akdmalatkt evalakdmes ptkldvtlak dmqpsmesdm
      301 alvkdmelpt ekevalvkdv rwptetdvss aknvvlptet evapakdvtl lketeraspi
      361 kmdlapskdm gppkenkket eraspikmdl apskdmgppk enkivpakdl vllseievaq
      421 andiisstei ssaekvalss etevalardm tlppetnvil tkdkalplea evapvkdmaq
      481 lpeteiapak dvapstvkev gllkdmspls etemalgkdv tpppetevvl iknvclppem
      541 evaltedqvp alkteaplak dgvltlannv tpakdvppls eteatpvpik dmeiaqtqkg
      601 isedshlesl qdvgqsaapt fmispetvtg tgkkcslpae edsvleklge rkpcnsqpse
      661 lssetsgiar peegrpvvsg tgndittppn kelppspekk tkplattqpa ktstskaktq
      721 ptslpkqpap ttigglnkkp mslasglvpa appkrpavas arpsilpskd vkpkpiadak
      781 apekraspsk pasapasrsg skstqtvakt ttaaavastg pssrspstll pkkptaikte
      841 gkpaevkkmt aksvpadlsr pkststssmk ktttlsgtap aagvvpsrvk atpmpsrpst
      901 tpfidkkpts akpssttprl srlatntsap dlknvrskvg stenikhqpg ggrakvekkt
      961 eaaattrkpe snavtktagp iasaqkqpag kvqiqnkkvd iskvsskcgs kanikhkpgg
     1021 gdvkiesqkl nfkekaqakv gsldnvghlp aggavktegg gseaplcpgp pageepaise
     1081 aapeagapts asglnghptl sgggdqreaq tldsqiqetn
//
LOCUS       NP_001340245             316 aa            linear   PRI 21-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 4 [Homo sapiens].
ACCESSION   NP_001340245
VERSION     NP_001340245.1
DBSOURCE    REFSEQ: accession NM_001353316.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 316)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 316)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 316)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 316)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 316)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.363171.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..316
                     /product="CYFIP-related Rac1 interactor B isoform 4"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=35665
     Region          17..312
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..316
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353316.2:341..1291"
                     /note="isoform 4 is encoded by transcript variant 78"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mmdslsfhch kacllgnaqp tesekeiynq vnvvlkdaeg iledlqsyrg agheireaiq
       61 hpadeklqek awgavvplvg klkkfyefsq rleaalrgll galtstpysp tqhlereqal
      121 akqfaeilhf tlrfdelkmt npaiqndfsy yrrtlsrmri nnvpaegene vnnelanrms
      181 lfyaeatpml ktlsdattkf vsenknlpie nttdclstma svcrvmletp eyrsrftnee
      241 tvsfclrvmv gviilydhvh pvgafaktsk idmkgcikvl kdqppnsveg llnalryttk
      301 hlndettskq iksmlq
//
LOCUS       NP_000964                257 aa            linear   PRI 21-NOV-2025
DEFINITION  large ribosomal subunit protein uL2 [Homo sapiens].
ACCESSION   NP_000964
VERSION     NP_000964.1
DBSOURCE    REFSEQ: accession NM_000973.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Sun,T., Zhu,W., Ru,Q. and Zheng,Y.
  TITLE     Silencing RPL8 inhibits the progression of hepatocellular carcinoma
            by down-regulating the mTORC1 signalling pathway
  JOURNAL   Hum Cell 36 (2), 725-737 (2023)
   PUBMED   36577883
  REMARK    GeneRIF: Silencing RPL8 inhibits the progression of hepatocellular
            carcinoma by down-regulating the mTORC1 signalling pathway.
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Fan,S., Zhang,S., Kong,D., Wang,H., Shi,Y., Wang,Z. and Zheng,H.
  TITLE     Integrative Multi-Omics Analysis of Identified Ferroptosis-Marker
            RPL8 as a Candidate Oncogene Correlates with Poor Prognosis and
            Immune Infiltration in Liver Cancer
  JOURNAL   Comb Chem High Throughput Screen 26 (7), 1298-1310 (2023)
   PUBMED   36017842
  REMARK    GeneRIF: Integrative Multi-Omics Analysis of Identified
            Ferroptosis-Marker RPL8 as a Candidate Oncogene Correlates with
            Poor Prognosis and Immune Infiltration in Liver Cancer.
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   7  (residues 1 to 257)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   8  (residues 1 to 257)
  AUTHORS   Uhlein,M., Weglohner,W., Urlaub,H. and Wittmann-Liebold,B.
  TITLE     Functional implications of ribosomal protein L2 in protein
            biosynthesis as shown by in vivo replacement studies
  JOURNAL   Biochem J 331 (Pt 2) (Pt 2), 423-430 (1998)
   PUBMED   9531480
REFERENCE   9  (residues 1 to 257)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 257)
  AUTHORS   Hanes,J., Klaudiny,J., von der Kammer,H. and Scheit,K.H.
  TITLE     Characterization by cDNA cloning of the mRNA of human ribosomal
            protein L8
  JOURNAL   Biochem Biophys Res Commun 197 (3), 1223-1228 (1993)
   PUBMED   7506540
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BC093064.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L2P family of ribosomal proteins. It is located in the
            cytoplasm. In rat, the protein associates with the 5.8S rRNA, very
            likely participates in the binding of aminoacyl-tRNA, and is a
            constituent of the elongation factor 2-binding site at the
            ribosomal subunit interface. Alternatively spliced transcript
            variants encoding the same protein exist. As is typical for genes
            encoding ribosomal proteins, there are multiple processed
            pseudogenes of this gene dispersed through the genome. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the shortest
            transcript. Variants 1-4 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD051211.1, BI553837.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..257
                     /product="large ribosomal subunit protein uL2"
                     /note="60S ribosomal protein L8"
                     /calculated_mol_wt=27894
     Region          1..254
                     /region_name="PTZ00180"
                     /note="60S ribosomal protein L8; Provisional"
                     /db_xref="CDD:173464"
     Region          207..232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62917.2)"
     Site            216
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyhistidine.
                     /evidence=ECO:0000269|PubMed:23103944; propagated from
                     UniProtKB/Swiss-Prot (P62917.2)"
     CDS             1..257
                     /gene="RPL8"
                     /gene_synonym="L8; uL2"
                     /coded_by="NM_000973.5:37..810"
                     /db_xref="CCDS:CCDS6433.1"
                     /db_xref="GeneID:6132"
                     /db_xref="HGNC:HGNC:10368"
                     /db_xref="MIM:604177"
ORIGIN      
        1 mgrvirgqrk gagsvfrahv khrkgaarlr avdfaerhgy ikgivkdiih dpgrgaplak
       61 vvfrdpyrfk krtelfiaae gihtgqfvyc gkkaqlnign vlpvgtmpeg tivccleekp
      121 gdrgklaras gnyatvishn petkktrvkl psgskkviss anravvgvva gggridkpil
      181 kagrayhkyk akrncwprvr gvamnpvehp fgggnhqhig kpstirrdap agrkvgliaa
      241 rrtgrlrgtk tvqeken
//
LOCUS       NP_001317602             174 aa            linear   PRI 21-NOV-2025
DEFINITION  proteasome subunit alpha type-4 isoform 3 [Homo sapiens].
ACCESSION   NP_001317602
VERSION     NP_001317602.1
DBSOURCE    REFSEQ: accession NM_001330673.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Bai,Y., Zheng,J., Cheng,L., Liu,Q., Zhao,G., Li,J., Gu,Y., Xu,W.,
            Wang,M., Wei,Q. and Zhang,R.
  TITLE     Potentially functional genetic variants of VAV2 and PSMA4 in the
            immune-activation pathway and non-small cell lung cancer survival
  JOURNAL   J Gene Med 24 (10), e3447 (2022)
   PUBMED   36039727
  REMARK    GeneRIF: Potentially functional genetic variants of VAV2 and PSMA4
            in the immune-activation pathway and non-small cell lung cancer
            survival.
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   6  (residues 1 to 174)
  AUTHORS   Palmer,A., Rivett,A.J., Thomson,S., Hendil,K.B., Butcher,G.W.,
            Fuertes,G. and Knecht,E.
  TITLE     Subpopulations of proteasomes in rat liver nuclei, microsomes and
            cytosol
  JOURNAL   Biochem J 316 (Pt 2) (Pt 2), 401-407 (1996)
   PUBMED   8687380
REFERENCE   7  (residues 1 to 174)
  AUTHORS   Castano,J.G., Mahillo,E., Arizti,P. and Arribas,J.
  TITLE     Phosphorylation of C8 and C9 subunits of the multicatalytic
            proteinase by casein kinase II and identification of the C8
            phosphorylation sites by direct mutagenesis
  JOURNAL   Biochemistry 35 (12), 3782-3789 (1996)
   PUBMED   8619999
REFERENCE   8  (residues 1 to 174)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   9  (residues 1 to 174)
  AUTHORS   Arribas,J., Arizti,P. and Castano,J.G.
  TITLE     Antibodies against the C2 COOH-terminal region discriminate the
            active and latent forms of the multicatalytic proteinase complex
  JOURNAL   J Biol Chem 269 (17), 12858-12864 (1994)
   PUBMED   8175701
REFERENCE   10 (residues 1 to 174)
  AUTHORS   Tamura,T., Lee,D.H., Osaka,F., Fujiwara,T., Shin,S., Chung,C.H.,
            Tanaka,K. and Ichihara,A.
  TITLE     Molecular cloning and sequence analysis of cDNAs for five major
            subunits of human proteasomes (multi-catalytic proteinase
            complexes)
  JOURNAL   Biochim Biophys Acta 1089 (1), 95-102 (1991)
   PUBMED   2025653
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU188756.1, BF589105.1,
            BG208993.1 and AC027228.16.
            
            Summary: This gene encodes a core alpha subunit of the 20S
            proteosome, which is a highly ordered ring-shaped structure
            composed of four rings of 28 non-identical subunits. Proteasomes
            cleave peptides in an ATP- and ubiquitin-dependent manner.
            [provided by RefSeq, Aug 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2962874.1,
                                           SRR18074967.2842740.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.1"
     Protein         1..174
                     /product="proteasome subunit alpha type-4 isoform 3"
                     /EC_number="3.4.25.1"
                     /note="proteasome component C9; proteasome subunit HC9;
                     proteasome subunit L; macropain subunit C9; alpha-3;
                     multicatalytic endopeptidase complex subunit C9;
                     proteasome subunit alpha type-4; proteasome (prosome,
                     macropain) subunit, alpha type, 4; proteasome subunit
                     alpha 4; proteasome subunit alpha3; proteasome subunit
                     alpha-3"
                     /calculated_mol_wt=19523
     Region          3..>169
                     /region_name="Ntn_hydrolase"
                     /note="The Ntn hydrolases (N-terminal nucleophile) are a
                     diverse superfamily of of enzymes that are activated
                     autocatalytically via an N-terminally lcated nucleophilic
                     amino acid. N-terminal nucleophile (NTN-) hydrolase
                     superfamily, which contains a...; cl00467"
                     /db_xref="CDD:469781"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P25789.1)"
     Site            order(32,48,50,64)
                     /site_type="active"
                     /db_xref="CDD:238884"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17323924; propagated from
                     UniProtKB/Swiss-Prot (P25789.1)"
     Site            127
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P25789.1)"
     CDS             1..174
                     /gene="PSMA4"
                     /gene_synonym="HC9; HsT17706; PSC9"
                     /coded_by="NM_001330673.2:120..644"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS86478.1"
                     /db_xref="GeneID:5685"
                     /db_xref="HGNC:HGNC:9533"
                     /db_xref="MIM:176846"
ORIGIN      
        1 msrrydsrtt ifspegrlyq veyameaigh agtclgilan dgvllaaerr nihklldevf
       61 fsekiyklne dmacsvagit sdanvltnel rliaqryllq yqepipceql vtalcdikqa
      121 ytqfggkrpf gvsllyigwd khygfqlyqs dpsgnyggwk atcignnsaw klqh
//
LOCUS       NP_001287663             238 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA damage-binding protein 2 isoform D1 [Homo sapiens].
ACCESSION   NP_001287663 XP_005252865
VERSION     NP_001287663.1
DBSOURCE    REFSEQ: accession NM_001300734.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Zhang,C., Li,W., Liu,L., Li,M., Sun,H., Zhang,C., Zhong,L.,
            Huang,J. and Li,T.
  TITLE     DDB2 promotes melanoma cell growth by transcriptionally regulating
            the expression of KMT2A and predicts a poor prognosis
  JOURNAL   FASEB J 38 (12), e23735 (2024)
   PUBMED   38860936
  REMARK    GeneRIF: DDB2 promotes melanoma cell growth by transcriptionally
            regulating the expression of KMT2A and predicts a poor prognosis.
REFERENCE   3  (residues 1 to 238)
  AUTHORS   de Souza Timoteo,A.R., Pinheiro de Almeida,I.C., Yurchenko,A.A., de
            Miranda Henriques,S.R., de Souza Segundo,P., Rajabi,F., Nikolaev,S.
            and Petta,T.B.
  TITLE     Brazilian XP-E siblings carrying a novel DDB2 variant developed
            early-onset melanoma: a case report
  JOURNAL   BMC Med Genomics 16 (1), 186 (2023)
   PUBMED   37573316
  REMARK    GeneRIF: Brazilian XP-E siblings carrying a novel DDB2 variant
            developed early-onset melanoma: a case report.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Schule,S., Bristy,E.A., Muhtadi,R., Kaletka,G., Stewart,S.,
            Ostheim,P., Hermann,C., Asang,C., Pleimes,D., Port,M. and Abend,M.
  TITLE     Four Genes Predictive for the Severity of Hematological Damage
            Reveal a Similar Response after X Irradiation and Chemotherapy
  JOURNAL   Radiat Res 199 (2), 115-123 (2023)
   PUBMED   36480042
  REMARK    GeneRIF: Four Genes Predictive for the Severity of Hematological
            Damage Reveal a Similar Response after X Irradiation and
            Chemotherapy.
REFERENCE   5  (residues 1 to 238)
  AUTHORS   Wang,X., Huang,Z., Li,L., Yang,Y., Zhang,J., Wang,L., Yuan,J. and
            Li,Y.
  TITLE     The Role of Alternative Splicing Factors, DDB2-Related Ageing and
            DNA Damage Repair in the Progression and Prognosis of Stomach
            Adenocarcinoma Patients
  JOURNAL   Genes (Basel) 14 (1), 39 (2022)
   PUBMED   36672781
  REMARK    GeneRIF: The Role of Alternative Splicing Factors, DDB2-Related
            Ageing and DNA Damage Repair in the Progression and Prognosis of
            Stomach Adenocarcinoma Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 238)
  AUTHORS   Hayes,S., Shiyanov,P., Chen,X. and Raychaudhuri,P.
  TITLE     DDB, a putative DNA repair protein, can function as a
            transcriptional partner of E2F1
  JOURNAL   Mol Cell Biol 18 (1), 240-249 (1998)
   PUBMED   9418871
REFERENCE   7  (residues 1 to 238)
  AUTHORS   Nichols,A.F., Ong,P. and Linn,S.
  TITLE     Mutations specific to the xeroderma pigmentosum group E Ddb-
            phenotype
  JOURNAL   J Biol Chem 271 (40), 24317-24320 (1996)
   PUBMED   8798680
REFERENCE   8  (residues 1 to 238)
  AUTHORS   Dualan,R., Brody,T., Keeney,S., Nichols,A.F., Admon,A. and Linn,S.
  TITLE     Chromosomal localization and cDNA cloning of the genes (DDB1 and
            DDB2) for the p127 and p48 subunits of a human damage-specific DNA
            binding protein
  JOURNAL   Genomics 29 (1), 62-69 (1995)
   PUBMED   8530102
REFERENCE   9  (residues 1 to 238)
  AUTHORS   Keeney,S., Chang,G.J. and Linn,S.
  TITLE     Characterization of a human DNA damage binding protein implicated
            in xeroderma pigmentosum E
  JOURNAL   J Biol Chem 268 (28), 21293-21300 (1993)
   PUBMED   8407967
REFERENCE   10 (residues 1 to 238)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB053816.1, AB107037.1 and
            AA278953.1.
            
            On Jul 11, 2014 this sequence version replaced XP_005252865.1.
            
            Summary: This gene encodes a protein that is necessary for the
            repair of ultraviolet light-damaged DNA. This protein is the
            smaller subunit of a heterodimeric protein complex that
            participates in nucleotide excision repair, and this complex
            mediates the ubiquitylation of histones H3 and H4, which
            facilitates the cellular response to DNA damage. This subunit
            appears to be required for DNA binding. Mutations in this gene
            cause xeroderma pigmentosum complementation group E, a recessive
            disease that is characterized by an increased sensitivity to UV
            light and a high predisposition for skin cancer development, in
            some cases accompanied by neurological abnormalities. Two
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (D1) lacks four consecutive
            alternate exons compared to variant WT, without a reading frame
            change. The resulting isoform (D1) has the same N- and C-termini
            but is shorter compared to isoform WT.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1993147.1, AB107037.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..238
                     /product="DNA damage-binding protein 2 isoform D1"
                     /note="xeroderma pigmentosum group E protein; UV-damaged
                     DNA-binding protein 2; DDB p48 subunit; DNA damage-binding
                     protein 2; damage-specific DNA binding protein 2, 48kDa"
                     /calculated_mol_wt=26613
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92466.1)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Site            35
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32789493; propagated from
                     UniProtKB/Swiss-Prot (Q92466.1)"
     Region          68..79
                     /region_name="Required for interaction with DDB1.
                     /evidence=ECO:0000269|PubMed:9632823"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Site            77
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:32789493; propagated from
                     UniProtKB/Swiss-Prot (Q92466.1)"
     Region          87..98
                     /region_name="Required for interaction with DDB1.
                     /evidence=ECO:0000269|PubMed:9632823"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Region          <95..221
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          114..151
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          116..151
                     /region_name="WD 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:19109893"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92466.1)"
     Region          153..198
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..238
                     /gene="DDB2"
                     /gene_synonym="DDBB; UV-DDB2; XPE"
                     /coded_by="NM_001300734.2:164..880"
                     /note="isoform D1 is encoded by transcript variant D1"
                     /db_xref="CCDS:CCDS73284.1"
                     /db_xref="GeneID:1643"
                     /db_xref="HGNC:HGNC:2718"
                     /db_xref="MIM:600811"
ORIGIN      
        1 mapkkrpetq ktseivlrpr nkrsrsplel epeakklcak gsgpsrrcds dclwvglagp
       61 qilppcrsiv rtlhqhklgr aswpsvqqgl qqsflhtlds yrilqkaapf drratslawh
      121 pthpstvavg skggdimlwn fgikdkptfi kgaawhpryn livvgrypdp nfksctpyel
      181 rtidvfdgns gkmmcqlydp essgisslne fnpmgdtlas amgyhiliws qeeartrk
//
LOCUS       NP_631895                798 aa            linear   PRI 21-NOV-2025
DEFINITION  AMP deaminase 2 isoform 2 [Homo sapiens].
ACCESSION   NP_631895
VERSION     NP_631895.1
DBSOURCE    REFSEQ: accession NM_139156.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Flores-Mendez,M., Ohl,L., Roule,T., Zhou,Y., Tintos-Hernandez,J.A.,
            Walsh,K., Ortiz-Gonzalez,X.R. and Akizu,N.
  TITLE     IMPDH2 filaments protect from neurodegeneration in AMPD2 deficiency
  JOURNAL   EMBO Rep 25 (9), 3990-4012 (2024)
   PUBMED   39075237
  REMARK    GeneRIF: IMPDH2 filaments protect from neurodegeneration in AMPD2
            deficiency.
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Gilboa,T., Elefant,N., Meiner,V. and Hacohen,N.
  TITLE     Delineating the phenotype and genetic basis of AMPD2-related
            pontocerebellar hypoplasia
  JOURNAL   Neurogenetics 24 (1), 61-66 (2023)
   PUBMED   36445597
  REMARK    GeneRIF: Delineating the phenotype and genetic basis of
            AMPD2-related pontocerebellar hypoplasia.
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Van den Bergh,F. and Sabina,R.L.
  TITLE     Characterization of human AMP deaminase 2 (AMPD2) gene expression
            reveals alternative transcripts encoding variable N-terminal
            extensions of isoform L
  JOURNAL   Biochem J 312 (Pt 2) (Pt 2), 401-410 (1995)
   PUBMED   8526848
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Bausch-Jurken,M.T., Mahnke-Zizelman,D.K., Morisaki,T. and
            Sabina,R.L.
  TITLE     Molecular cloning of AMP deaminase isoform L. Sequence and
            bacterial expression of human AMPD2 cDNA
  JOURNAL   J Biol Chem 267 (31), 22407-22413 (1992)
   PUBMED   1429593
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Mahnke-Zizelman,D.K. and Sabina,R.L.
  TITLE     Cloning of human AMP deaminase isoform E cDNAs. Evidence for a
            third AMPD gene exhibiting alternatively spliced 5'-exons
  JOURNAL   J Biol Chem 267 (29), 20866-20877 (1992)
   PUBMED   1400401
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Ashby,B. and Holmsen,H.
  TITLE     Platelet AMP deaminase. Purification and kinetic studies
  JOURNAL   J Biol Chem 256 (20), 10519-10523 (1981)
   PUBMED   7287721
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA558264.1 and BC007711.2.
            
            Summary: The protein encoded by this gene is important in purine
            metabolism by converting AMP to IMP. The encoded protein, which
            acts as a homotetramer, is one of three AMP deaminases found in
            mammals. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (2) lacks the exon containing the
            translational start site compared to variant 4. The resulting
            isoform (2) has a shorter and distinct N-terminus compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK025706.1, BC075844.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..798
                     /product="AMP deaminase 2 isoform 2"
                     /EC_number="3.5.4.6"
                     /note="adenosine monophosphate deaminase 2 (isoform L);
                     AMP deaminase 2"
                     /calculated_mol_wt=91940
     Region          136..779
                     /region_name="AMP_deaminase"
                     /note="AMP deaminase; pfam19326"
                     /db_xref="CDD:437158"
     CDS             1..798
                     /gene="AMPD2"
                     /gene_synonym="AMPD; PCH9; SPG63"
                     /coded_by="NM_139156.4:433..2829"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS804.1"
                     /db_xref="GeneID:271"
                     /db_xref="HGNC:HGNC:469"
                     /db_xref="MIM:102771"
ORIGIN      
        1 maseargglg applqsarsl pgpapclkhf pldlrtsmdg kckeiaeelf trslaeselr
       61 sapyefpees pieqleerrq rlerqisqdv klepdillra kqdflktdsd sdlqlykeqg
      121 egqgdrslre rdvlerefqr vtisgeekcg vpftdlldaa ksvvralfir ekymalslqs
      181 fcpttrrylq qlaekpletr tyeqgpdtpv sadapvhppa leqhpyehce pstmpgdlgl
      241 glrmvrgvvh vytrrepdeh csevelpypd lqefvadvnv lmaliingpi ksfcyrrlqy
      301 lsskfqmhvl lnemkelaaq kkvphrdfyn irkvdthiha sscmnqkhll rfikramkrh
      361 leeivhveqg reqtlrevfe smnltaydls vdtldvhadr ntfhrfdkfn akynpigesv
      421 lreifiktdn rvsgkyfahi ikevmsdlee skyqnaelrl siygrsrdew dklarwavmh
      481 rvhspnvrwl vqvprlfdvy rtkgqlanfq emleniflpl featvhpash pelhlflehv
      541 dgfdsvddes kpenhvfnle splpeawvee dnppyayyly ytfanmamln hlrrqrgfht
      601 fvlrphcgea gpihhlvsaf mlaenishgl llrkapvlqy lyylaqigia msplsnnslf
      661 lsyhrnplpe ylsrglmvsl stddplqfhf tkeplmeeys iatqvwklss cdmcelarns
      721 vlmsgfshkv kshwlgpnyt kegpegndir rtnvpdirvg yryetlcqel alitqavqse
      781 mletipeeag itmspgpq
//
LOCUS       NP_001257382             754 aa            linear   PRI 21-NOV-2025
DEFINITION  NEDD4-like E3 ubiquitin-protein ligase WWP2 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001257382
VERSION     NP_001257382.1
DBSOURCE    REFSEQ: accession NM_001270453.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Wang,H., Lian,X., Wang,K. and Wang,S.
  TITLE     WWP2 binds to NKRF, enhances the NF-kappaB signaling, and promotes
            malignant phenotypes of acute myeloid leukemia cells
  JOURNAL   Biochem Cell Biol 102 (1), 85-95 (2024)
   PUBMED   37921219
  REMARK    GeneRIF: WWP2 binds to NKRF, enhances the NF-kappaB signaling, and
            promotes malignant phenotypes of acute myeloid leukemia cells.
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Lee,K.T., Pranoto,I.K.A., Kim,S.Y., Choi,H.J., To,N.B., Chae,H.,
            Lee,J.Y., Kim,J.E., Kwon,Y.V. and Nam,J.W.
  TITLE     Comparative interactome analysis of alpha-arrestin families in
            human and Drosophila
  JOURNAL   Elife 12, 88328 (2024)
   PUBMED   38270169
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 754)
  AUTHORS   Chantry,A.
  TITLE     WWP2 ubiquitin ligase and its isoforms: new biological insight and
            promising disease targets
  JOURNAL   Cell Cycle 10 (15), 2437-2439 (2011)
   PUBMED   21750408
REFERENCE   5  (residues 1 to 754)
  AUTHORS   Soond,S.M. and Chantry,A.
  TITLE     Selective targeting of activating and inhibitory Smads by distinct
            WWP2 ubiquitin ligase isoforms differentially modulates TGFbeta
            signalling and EMT
  JOURNAL   Oncogene 30 (21), 2451-2462 (2011)
   PUBMED   21258410
  REMARK    GeneRIF: Data show that the WWP2-N isoform interacts with Smad2 and
            Smad3, whereas WWP2-C interacts only with Smad7.
REFERENCE   6  (residues 1 to 754)
  AUTHORS   McDonald,F.J., Western,A.H., McNeil,J.D., Thomas,B.C., Olson,D.R.
            and Snyder,P.M.
  TITLE     Ubiquitin-protein ligase WWP2 binds to and downregulates the
            epithelial Na(+) channel
  JOURNAL   Am J Physiol Renal Physiol 283 (3), F431-F436 (2002)
   PUBMED   12167593
  REMARK    GeneRIF: expression, binding, and functional data all suggest that
            WWP2 is a candidate to regulate ENaC-mediated Na(+) transport in
            epithelia
REFERENCE   7  (residues 1 to 754)
  AUTHORS   Harvey,K.F., Shearwin-Whyatt,L.M., Fotia,A., Parton,R.G. and
            Kumar,S.
  TITLE     N4WBP5, a potential target for ubiquitination by the Nedd4 family
            of proteins, is a novel Golgi-associated protein
  JOURNAL   J Biol Chem 277 (11), 9307-9317 (2002)
   PUBMED   11748237
REFERENCE   8  (residues 1 to 754)
  AUTHORS   Wood,J.D., Yuan,J., Margolis,R.L., Colomer,V., Duan,K., Kushi,J.,
            Kaminsky,Z., Kleiderlein,J.J., Sharp,A.H. and Ross,C.A.
  TITLE     Atrophin-1, the DRPLA gene product, interacts with two families of
            WW domain-containing proteins
  JOURNAL   Mol Cell Neurosci 11 (3), 149-160 (1998)
   PUBMED   9647693
REFERENCE   9  (residues 1 to 754)
  AUTHORS   Jonsson,A.B.
  TITLE     Identification of a human cDNA clone that mediates adherence of
            pathogenic Neisseria to non-binding cells
  JOURNAL   FEMS Microbiol Lett 162 (1), 25-30 (1998)
   PUBMED   9595660
REFERENCE   10 (residues 1 to 754)
  AUTHORS   Pirozzi,G., McConnell,S.J., Uveges,A.J., Carter,J.M., Sparks,A.B.,
            Kay,B.K. and Fowlkes,D.M.
  TITLE     Identification of novel human WW domain-containing proteins by
            cloning of ligand targets
  JOURNAL   J Biol Chem 272 (23), 14611-14616 (1997)
   PUBMED   9169421
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK300266.1, AK316097.1 and
            JN712744.1.
            
            Summary: This gene encodes a member of the Nedd4 family of E3
            ligases, which play an important role in protein ubiquitination.
            The encoded protein contains four WW domains and may play a role in
            multiple processes including chondrogenesis and the regulation of
            oncogenic signaling pathways via interactions with Smad proteins
            and the tumor suppressor PTEN. Alternatively spliced transcript
            variants encoding multiple isoforms have been observed for this
            gene, and a pseudogene of this gene is located on the long arm of
            chromosome 10. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (4) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream, in-frame start codon, compared to variant 1. The
            encoded isoform (4) has a shorter N-terminus, compared to isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK300266.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..754
                     /product="NEDD4-like E3 ubiquitin-protein ligase WWP2
                     isoform 4"
                     /EC_number="2.3.2.26"
                     /note="atrophin-1 interacting protein 2; NEDD4-like E3
                     ubiquitin-protein ligase WWP2; HECT-type E3 ubiquitin
                     transferase WWP2"
                     /calculated_mol_wt=86177
     Region          <1..26
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Region          <48..227
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          186..215
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          216..245
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          291..319
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          331..361
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(345,356)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          400..752
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(405,435,446,507,681,716..717,720..724,744,751)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(535,538..539,541..542,545,552,554,557..558,560,566,
                     571,588,592)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..754
                     /gene="WWP2"
                     /gene_synonym="AIP2; WWp2-like"
                     /coded_by="NM_001270453.2:162..2426"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS58476.1"
                     /db_xref="GeneID:11060"
                     /db_xref="HGNC:HGNC:16804"
                     /db_xref="MIM:602308"
ORIGIN      
        1 mqltlnlqte nkgsvvsgge ltifldgptv dlgnvpngsa ltdgsqlpsr dssgtavape
       61 nrhqppstnc fggrsrthrh sgasarttpa tgeqspgars rhrqpvknsg hsglangtvn
      121 depttatdpe epsvvgvtsp paaplsvtpn pnttslpapa tpaegeepst sgtqqlpaaa
      181 qapdalpagw eqrelpngrv yyvdhntktt twerplppgw ekrtdprgrf yyvdhntrtt
      241 twqrptaeyv rnyeqwqsqr nqlqgamqhf sqrflyqsss astdhdplgp lppgwekrqd
      301 ngrvyyvnhn trttqwedpr tqgmiqepal ppgwemkyts egvryfvdhn trtttfkdpr
      361 pgfesgtkqg spgaydrsfr wkyhqfrflc hsnalpshvk isvsrqtlfe dsfqqimnmk
      421 pydlrrrlyi imrgeegldy ggiarewffl lshevlnpmy clfeyagknn yclqinpass
      481 inpdhltyfr figrfiamal yhgkfidtgf tlpfykrmln krptlkdles idpefynsiv
      541 wikennleec glelyfiqdm eilgkvtthe lkeggesirv teenkeeyim lltdwrftrg
      601 veeqtkafld gfnevaplew lryfdekele lmlcgmqeid msdwqkstiy rhytknskqi
      661 qwfwqvvkem dnekrirllq fvtgtcrlpv ggfaeligsn gpqkfcidkv gketwlprsh
      721 tcfnrldlpp yksyeqlrek llyaieeteg fgqe
//
LOCUS       NP_001362667             397 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform ooo [Homo sapiens].
ACCESSION   NP_001362667 XP_006712249
VERSION     NP_001362667.1
DBSOURCE    REFSEQ: accession NM_001375738.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 397)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 397)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 397)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 397)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 397)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            On Oct 31, 2019 this sequence version replaced XP_006712249.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1207484.1,
                                           SRR18074967.556233.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..397
                     /product="abl interactor 2 isoform ooo"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=43632
     Region          93..156
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          336..396
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(344,346,349,353,371..372,385,387..388)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..397
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375738.1:122..1315"
                     /note="isoform ooo is encoded by transcript variant 72"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqs adkqraleet kayttqslas
       61 vaylintlan nvlqmldiqa sqlrrmessi nhisqtvdih kekvarreig ilttnkntsr
      121 thkiiapanl erpvryirkp idytilddig hgvkvstqnm kmgglprttp ptqkppsppm
      181 sgkgtlgssg ssggshpssr sssrensgsg svgvpiavpt psppsvfpgh pvqfysmnrp
      241 asrhtpptig gslpyrrpps itsqtslqnq mnggpfysqn pvsdtppppp pveepvfdes
      301 pppppppedy eeeeaavvey sdpyaeedpp waprsylekv vaiydytkdk edelsfqega
      361 iiyvikkndd gwyegvmngv tglfpgnyve simhyse
//
LOCUS       NP_001340448             507 aa            linear   PRI 21-NOV-2025
DEFINITION  integrator complex subunit 10 isoform n [Homo sapiens].
ACCESSION   NP_001340448
VERSION     NP_001340448.1
DBSOURCE    REFSEQ: accession NM_001353519.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Lin,M.H., Jensen,M.K., Elrod,N.D., Chu,H.F., Haseley,M., Beam,A.C.,
            Huang,K.L., Chiang,W., Russell,W.K., Williams,K., Proschel,C.,
            Wagner,E.J. and Tong,L.
  TITLE     Cytoplasmic binding partners of the Integrator endonuclease INTS11
            and its paralog CPSF73 are required for their nuclear function
  JOURNAL   Mol Cell 84 (15), 2900-2917 (2024)
   PUBMED   39032490
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Razew,M., Fraudeau,A., Pfleiderer,M.M., Linares,R. and Galej,W.P.
  TITLE     Structural basis of the Integrator complex assembly and association
            with transcription factors
  JOURNAL   Mol Cell 84 (13), 2542-2552 (2024)
   PUBMED   38823386
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Fianu,I., Ochmann,M., Walshe,J.L., Dybkov,O., Cruz,J.N., Urlaub,H.
            and Cramer,P.
  TITLE     Structural basis of Integrator-dependent RNA polymerase II
            termination
  JOURNAL   Nature 629 (8010), 219-227 (2024)
   PUBMED   38570683
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Offley,S.R., Pfleiderer,M.M., Zucco,A., Fraudeau,A., Welsh,S.A.,
            Razew,M., Galej,W.P. and Gardini,A.
  TITLE     A combinatorial approach to uncover an additional Integrator
            subunit
  JOURNAL   Cell Rep 42 (3), 112244 (2023)
   PUBMED   36920904
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Wu,Y., Lin,Z., Luo,M., Yu,X., Chen,S. and Liu,L.
  TITLE     Effects of genetic polymorphisms in INTS10 and their interaction
            with environmental factors on progression from persistent HBV
            infection to hepatocellular carcinoma
  JOURNAL   Mol Carcinog 60 (9), 620-626 (2021)
   PUBMED   34133796
  REMARK    GeneRIF: Effects of genetic polymorphisms in INTS10 and their
            interaction with environmental factors on progression from
            persistent HBV infection to hepatocellular carcinoma.
REFERENCE   6  (residues 1 to 507)
  AUTHORS   Weissglas-Volkov,D., Aguilar-Salinas,C.A., Nikkola,E., Deere,K.A.,
            Cruz-Bautista,I., Arellano-Campos,O., Munoz-Hernandez,L.L.,
            Gomez-Munguia,L., Ordonez-Sanchez,M.L., Reddy,P.M., Lusis,A.J.,
            Matikainen,N., Taskinen,M.R., Riba,L., Cantor,R.M.,
            Sinsheimer,J.S., Tusie-Luna,T. and Pajukanta,P.
  TITLE     Genomic study in Mexicans identifies a new locus for triglycerides
            and refines European lipid loci
  JOURNAL   J Med Genet 50 (5), 298-308 (2013)
   PUBMED   23505323
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Ellinghaus,E., Stanulla,M., Richter,G., Ellinghaus,D., te
            Kronnie,G., Cario,G., Cazzaniga,G., Horstmann,M., Panzer
            Grumayer,R., Cave,H., Trka,J., Cinek,O., Teigler-Schlegel,A.,
            ElSharawy,A., Hasler,R., Nebel,A., Meissner,B., Bartram,T.,
            Lescai,F., Franceschi,C., Giordan,M., Nurnberg,P., Heinzow,B.,
            Zimmermann,M., Schreiber,S., Schrappe,M. and Franke,A.
  TITLE     Identification of germline susceptibility loci in
            ETV6-RUNX1-rearranged childhood acute lymphoblastic leukemia
  JOURNAL   Leukemia 26 (5), 902-909 (2012)
   PUBMED   22076464
REFERENCE   8  (residues 1 to 507)
  AUTHORS   Kooner,J.S., Chambers,J.C., Aguilar-Salinas,C.A., Hinds,D.A.,
            Hyde,C.L., Warnes,G.R., Gomez Perez,F.J., Frazer,K.A., Elliott,P.,
            Scott,J., Milos,P.M., Cox,D.R. and Thompson,J.F.
  TITLE     Genome-wide scan identifies variation in MLXIPL associated with
            plasma triglycerides
  JOURNAL   Nat Genet 40 (2), 149-151 (2008)
   PUBMED   18193046
REFERENCE   9  (residues 1 to 507)
  AUTHORS   Baillat,D., Hakimi,M.A., Naar,A.M., Shilatifard,A., Cooch,N. and
            Shiekhattar,R.
  TITLE     Integrator, a multiprotein mediator of small nuclear RNA
            processing, associates with the C-terminal repeat of RNA polymerase
            II
  JOURNAL   Cell 123 (2), 265-276 (2005)
   PUBMED   16239144
REFERENCE   10 (residues 1 to 507)
  AUTHORS   Yuryev,A. and Wennogle,L.P.
  TITLE     Novel raf kinase protein-protein interactions found by an
            exhaustive yeast two-hybrid analysis
  JOURNAL   Genomics 81 (2), 112-125 (2003)
   PUBMED   12620389
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC107964.4.
            
            Summary: INTS10 is a subunit of the Integrator complex, which
            associates with the C-terminal domain of RNA polymerase II large
            subunit (POLR2A; MIM 180660) and mediates 3-prime end processing of
            small nuclear RNAs U1 (RNU1; MIM 180680) and U2 (RNU2; MIM 180690)
            (Baillat et al., 2005 [PubMed 16239144]).[supplied by OMIM, Mar
            2008].
            
            Transcript Variant: This variant (16), along with variants 14 and
            15, encodes isoform n.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1660805.126645.1, SRR1803614.141001.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2153307, SAMEA2154529 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..507
                     /product="integrator complex subunit 10 isoform n"
                     /calculated_mol_wt=58441
     CDS             1..507
                     /gene="INTS10"
                     /gene_synonym="C8orf35; INT10"
                     /coded_by="NM_001353519.2:751..2274"
                     /note="isoform n is encoded by transcript variant 16"
                     /db_xref="GeneID:55174"
                     /db_xref="HGNC:HGNC:25548"
                     /db_xref="MIM:611353"
ORIGIN      
        1 mspskrssqk yiieglteks sqivdpwerl fkilnvvgmr cewqmdkgrr sygdilhrmk
       61 dlcrymnnfd seahakyknq vvystmlvff knafqyvnsi qpslfqgpna psqvplvlle
      121 dvsnvygdve idrnkhihkk rklaegrekt mssddedcsa kgrnrhivvn kaelanstev
      181 lesfklares wellyslefl dkeftricla wktdtwlwlr ifltdmiiyq gqykkaiasl
      241 hhlaalqgsi sqpqitgqgt lehqraliql atchfalgey rmtcekvldl mcymvlpiqd
      301 ggksqeepsk vkpkfrkgsd lkllpctska impyclhlml acfklraftd nrddmalghv
      361 ivllqqewpr genlflkavn kicqqgnfqy enffnyvtni dmleefaylr tqeggkihle
      421 llpnqgmlik pssppmgllq qeflpvlqps iqtadrhhtv trgitkgvke dfrlamerqv
      481 srcgenlmvv lhrfcineki lllqtlt
//
LOCUS       NP_001381789             551 aa            linear   PRI 21-NOV-2025
DEFINITION  kinesin light chain 1 isoform 32 [Homo sapiens].
ACCESSION   NP_001381789
VERSION     NP_001381789.1
DBSOURCE    REFSEQ: accession NM_001394860.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Kikuchi,M., Viet,J., Nagata,K., Sato,M., David,G., Audic,Y.,
            Silverman,M.A., Yamamoto,M., Akatsu,H., Hashizume,Y., Takeda,S.,
            Akamine,S., Miyamoto,T., Uozumi,R., Gotoh,S., Mori,K., Ikeda,M.,
            Paillard,L. and Morihara,T.
  TITLE     Gene-gene functional relationships in Alzheimer's disease: CELF1
            regulates KLC1 alternative splicing
  JOURNAL   Biochem Biophys Res Commun 721, 150025 (2024)
   PUBMED   38768546
  REMARK    GeneRIF: Gene-gene functional relationships in Alzheimer's disease:
            CELF1 regulates KLC1 alternative splicing.
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Gyoeva,F.K., Bybikova,E.M. and Minin,A.A.
  TITLE     An isoform of kinesin light chain specific for the Golgi complex
  JOURNAL   J Cell Sci 113 (Pt 11), 2047-2054 (2000)
   PUBMED   10806115
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Khodjakov,A., Lizunova,E.M., Minin,A.A., Koonce,M.P. and
            Gyoeva,F.K.
  TITLE     A specific light chain of kinesin associates with mitochondria in
            cultured cells
  JOURNAL   Mol Biol Cell 9 (2), 333-343 (1998)
   PUBMED   9450959
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Chernajovsky,Y., Brown,A. and Clark,J.
  TITLE     Human kinesin light (beta) chain gene: DNA sequence and functional
            characterization of its promoter and first exon
  JOURNAL   DNA Cell Biol 15 (11), 965-974 (1996)
   PUBMED   8945637
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Goedert,M., Marsh,S. and Carter,N.
  TITLE     Localization of the human kinesin light chain gene (KNS2) to
            chromosome 14q32.3 by fluorescence in situ hybridization
  JOURNAL   Genomics 32 (1), 173-175 (1996)
   PUBMED   8786116
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Cabeza-Arvelaiz,Y., Shih,L.C., Hardman,N., Asselbergs,F., Bilbe,G.,
            Schmitz,A., White,B., Siciliano,M.J. and Lachman,L.B.
  TITLE     Cloning and genetic characterization of the human kinesin
            light-chain (KLC) gene
  JOURNAL   DNA Cell Biol 12 (10), 881-892 (1993)
   PUBMED   8274221
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139300.6 and AL049840.8.
            
            Summary: Conventional kinesin is a tetrameric molecule composed of
            two heavy chains and two light chains, and transports various
            cargos along microtubules toward their plus ends. The heavy chains
            provide the motor activity, while the light chains bind to various
            cargos. This gene encodes a member of the kinesin light chain
            family. It associates with kinesin heavy chain through an
            N-terminal domain, and six tetratricopeptide repeat (TPR) motifs
            are thought to be involved in binding of cargos such as vesicles,
            mitochondria, and the Golgi complex. Thus, kinesin light chains
            function as adapter molecules and not motors per se. Although
            previously named 'kinesin 2', this gene is not a member of the
            kinesin-2 / kinesin heavy chain subfamily of kinesin motor
            proteins. Extensive alternative splicing produces isoforms with
            different C-termini that are proposed to bind to different cargos;
            however, the full-length nature and/or biological validity of most
            of these variants have not been determined. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.325349.1,
                                           SRR18074969.1927049.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..551
                     /product="kinesin light chain 1 isoform 32"
                     /EC_number="2.7.1.21"
                     /note="kinesin 2 60/70kDa; medulloblastoma antigen
                     MU-MB-2.50"
                     /calculated_mol_wt=62585
     Region          35..>149
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          155..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P37285; propagated from
                     UniProtKB/Swiss-Prot (Q07866.2)"
     Region          210..435
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          213..246
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Region          214..241
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          255..288
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Region          255..283
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          297..330
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Region          297..325
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(298,301..302,305..306,308,340,343..344,347..348,
                     350..351,382,385..386,389..390,393)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          338..368
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          339..372
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Region          381..414
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Region          381..408
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O88447; propagated from
                     UniProtKB/Swiss-Prot (Q07866.2)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:21385839; propagated from
                     UniProtKB/Swiss-Prot (Q07866.2)"
     Region          464..497
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:20074060; propagated from
                     UniProtKB/Swiss-Prot (Q07866.2)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:20074060; propagated from
                     UniProtKB/Swiss-Prot (Q07866.2)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q07866.2)"
     CDS             1..551
                     /gene="KLC1"
                     /gene_synonym="KLC; KNS2; KNS2A"
                     /coded_by="NM_001394860.1:286..1941"
                     /note="isoform 32 is encoded by transcript variant 32"
                     /db_xref="CCDS:CCDS91951.1"
                     /db_xref="GeneID:3831"
                     /db_xref="HGNC:HGNC:6387"
                     /db_xref="MIM:600025"
ORIGIN      
        1 mydnmstmvy ikedkleklt qdeiisktkq viqglealkn ehnsilqsll etlkclkkdd
       61 esnlveeksn mirkslemle lglseaqvmm alsnhlnave sekqklraqv rrlcqenqwl
      121 rdelantqqk lqkseqsvaq leeekkhlef mnqlkkyddd ispsedkdtd stkeplddlf
      181 pndeddpgqg iqqqhssaaa aaqqggyeip arlrtlhnlv iqyasqgrye vavplckqal
      241 edlektsghd hpdvatmlni lalvyrdqnk ykdaanllnd alairektlg kdhpavaatl
      301 nnlavlygkr gkykeaeplc kraleirekv lgkdhpdvak qlnnlallcq nqgkyeevey
      361 yyqraleiyq tklgpddpnv aktknnlasc ylkqgkfkqa etlykeiltr aherefgsvd
      421 denkpiwmha eereeckgkq kdgtsfgeyg gwykackvds ptvtttlknl galyrrqgkf
      481 eaaetleeaa mrsrkqgldn vhkqrvaevl ndpenmekrr sreslnvdvv kyesgpdgge
      541 evsmsvewng a
//
LOCUS       NP_001294870             161 aa            linear   PRI 21-NOV-2025
DEFINITION  signal peptidase complex catalytic subunit SEC11C isoform 2 [Homo
            sapiens].
ACCESSION   NP_001294870 XP_005266836
VERSION     NP_001294870.1
DBSOURCE    REFSEQ: accession NM_001307941.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Zhang,N., Cao,S., Sun,R., Wang,Y., Liu,L., Wang,W. and Meng,X.
  TITLE     Signal peptidase 21 suppresses cell proliferation, migration, and
            invasion via the PTEN-PI3K/Akt signaling pathway in lung
            adenocarcinoma
  JOURNAL   PeerJ 10, e14206 (2022)
   PUBMED   36275477
  REMARK    GeneRIF: Signal peptidase 21 suppresses cell proliferation,
            migration, and invasion via the PTEN-PI3K/Akt signaling pathway in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Liaci,A.M., Steigenberger,B., Telles de Souza,P.C., Tamara,S.,
            Grollers-Mulderij,M., Ogrissek,P., Marrink,S.J., Scheltema,R.A. and
            Forster,F.
  TITLE     Structure of the human signal peptidase complex reveals the
            determinants for signal peptide cleavage
  JOURNAL   Mol Cell 81 (19), 3934-3948 (2021)
   PUBMED   34388369
  REMARK    GeneRIF: Structure of the human signal peptidase complex reveals
            the determinants for signal peptide cleavage.
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 161)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 161)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 161)
  AUTHORS   Oue,N., Naito,Y., Hayashi,T., Takigahira,M., Kawano-Nagatsuma,A.,
            Sentani,K., Sakamoto,N., Zarni Oo,H., Uraoka,N., Yanagihara,K.,
            Ochiai,A., Sasaki,H. and Yasui,W.
  TITLE     Signal peptidase complex 18, encoded by SEC11A, contributes to
            progression via TGF-alpha secretion in gastric cancer
  JOURNAL   Oncogene 33 (30), 3918-3926 (2014)
   PUBMED   23995782
  REMARK    Erratum:[Oncogene. 2019 Jul;38(28):5748. doi:
            10.1038/s41388-019-0837-z. PMID: 31175341]
REFERENCE   8  (residues 1 to 161)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   9  (residues 1 to 161)
  AUTHORS   Dodson,G. and Steiner,D.
  TITLE     The role of assembly in insulin's biosynthesis
  JOURNAL   Curr Opin Struct Biol 8 (2), 189-194 (1998)
   PUBMED   9631292
  REMARK    Review article
REFERENCE   10 (residues 1 to 161)
  AUTHORS   Shelness,G.S. and Blobel,G.
  TITLE     Two subunits of the canine signal peptidase complex are homologous
            to yeast SEC11 protein
  JOURNAL   J Biol Chem 265 (16), 9512-9519 (1990)
   PUBMED   2188978
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM789622.1, BQ417397.1 and BM760252.1.
            
            On Apr 17, 2015 this sequence version replaced XP_005266836.1.
            
            Transcript Variant: This variant (2) differs in the 3' UTR, and
            lacks an alternate exon in the 3' coding region resulting in a
            frameshift, compared to variant 1. The encoded isoform (2) has a
            distinct C-terminus and is shorter than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.499936.1,
                                           SRR1163658.529136.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.32"
     Protein         1..161
                     /product="signal peptidase complex catalytic subunit
                     SEC11C isoform 2"
                     /EC_number="3.4.21.89"
                     /note="signal peptidase complex catalytic subunit SEC11C;
                     SEC11-like protein 3; SPase 21 kDa subunit; microsomal
                     signal peptidase 21 kDa subunit; SEC11-like 3; signal
                     peptidase complex 21"
                     /calculated_mol_wt=17964
     Region          34..>134
                     /region_name="Peptidase_S24_S26"
                     /note="The S24, S26 LexA/signal peptidase superfamily
                     contains LexA-related and type I signal peptidase
                     families. The S24 LexA protein domains include: the lambda
                     repressor CI/C2 family and related bacterial prophage
                     repressor proteins; LexA (EC 3.4.21.88), the...; cl10465"
                     /db_xref="CDD:447902"
     Site            order(68,108)
                     /site_type="active"
                     /note="Catalytic site [active]"
                     /db_xref="CDD:119398"
     CDS             1..161
                     /gene="SEC11C"
                     /gene_synonym="SEC11L3; SPC21; SPCS4C"
                     /coded_by="NM_001307941.2:66..551"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS77193.1"
                     /db_xref="GeneID:90701"
                     /db_xref="HGNC:HGNC:23400"
ORIGIN      
        1 mvragavgah lpasgldifg dlkkmnkrql yyqvlnfami vssalmiwkg livltgsesp
       61 ivvvlsgsme pafhrgdllf ltnfredpir ageivvfkve grdipivhrv ikvhekdngd
      121 ikfltkgdnn evddrglyke gqnwlekkdv vgrargmlfw l
//
LOCUS       NP_001035241             215 aa            linear   PRI 21-NOV-2025
DEFINITION  sodium channel regulatory subunit beta-3 precursor [Homo sapiens].
ACCESSION   NP_001035241
VERSION     NP_001035241.1
DBSOURCE    REFSEQ: accession NM_001040151.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Noland,C.L., Chua,H.C., Kschonsak,M., Heusser,S.A., Braun,N.,
            Chang,T., Tam,C., Tang,J., Arthur,C.P., Ciferri,C., Pless,S.A. and
            Payandeh,J.
  TITLE     Structure-guided unlocking of NaX reveals a non-selective
            tetrodotoxin-sensitive cation channel
  JOURNAL   Nat Commun 13 (1), 1416 (2022)
   PUBMED   35301303
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Li,S., Han,J., Guo,G., Sun,Y., Zhang,T., Zhao,M., Xu,Y., Cui,Y.,
            Liu,Y. and Zhang,J.
  TITLE     Voltage-gated sodium channels beta3 subunit promotes tumorigenesis
            in hepatocellular carcinoma by facilitating p53 degradation
  JOURNAL   FEBS Lett 594 (3), 497-508 (2020)
   PUBMED   31626714
  REMARK    GeneRIF: Voltage-gated sodium channels beta3 subunit promotes
            tumorigenesis in hepatocellular carcinoma by facilitating p53
            degradation.
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Ratcliffe,C.F., Westenbroek,R.E., Curtis,R. and Catterall,W.A.
  TITLE     Sodium channel beta1 and beta3 subunits associate with neurofascin
            through their extracellular immunoglobulin-like domain
  JOURNAL   J Cell Biol 154 (2), 427-434 (2001)
   PUBMED   11470829
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Stevens,E.B., Cox,P.J., Shah,B.S., Dixon,A.K., Richardson,P.J.,
            Pinnock,R.D. and Lee,K.
  TITLE     Tissue distribution and functional expression of the human
            voltage-gated sodium channel beta3 subunit
  JOURNAL   Pflugers Arch 441 (4), 481-488 (2001)
   PUBMED   11212211
REFERENCE   8  (residues 1 to 215)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 215)
  AUTHORS   Morgan,K., Stevens,E.B., Shah,B., Cox,P.J., Dixon,A.K., Lee,K.,
            Pinnock,R.D., Hughes,J., Richardson,P.J., Mizuguchi,K. and
            Jackson,A.P.
  TITLE     beta 3: an additional auxiliary subunit of the voltage-sensitive
            sodium channel that modulates channel gating with distinct kinetics
  JOURNAL   Proc Natl Acad Sci U S A 97 (5), 2308-2313 (2000)
   PUBMED   10688874
REFERENCE   10 (residues 1 to 215)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002765.3.
            
            Summary: Voltage-gated sodium channels are transmembrane
            glycoprotein complexes composed of a large alpha subunit and one or
            more regulatory beta subunits. They are responsible for the
            generation and propagation of action potentials in neurons and
            muscle. This gene encodes one member of the sodium channel beta
            subunit gene family, and influences the inactivation kinetics of
            the sodium channel. Two alternatively spliced variants, encoding
            the same protein, have been identified. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same isoform.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB032984.1, SRR1660809.251090.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162841 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000299333.8/ ENSP00000299333.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.1"
     Protein         1..215
                     /product="sodium channel regulatory subunit beta-3
                     precursor"
                     /note="voltage-gated sodium channel beta-3 subunit; sodium
                     channel subunit beta-3; sodium channel, voltage-gated,
                     type III, beta subunit; sodium channel regulatory subunit
                     beta-3"
                     /calculated_mol_wt=22180
     sig_peptide     1..22
                     /calculated_mol_wt=2540
     mat_peptide     23..215
                     /product="sodium channel regulatory subunit beta-3"
                     /calculated_mol_wt=22180
     Region          28..140
                     /region_name="V-set"
                     /note="Immunoglobulin V-set domain; pfam07686"
                     /db_xref="CDD:462230"
     Site            95
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NY72.1)"
     Site            109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NY72.1)"
     Site            113
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NY72.1)"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NY72.1)"
     Site            157..178
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NY72.1)"
     CDS             1..215
                     /gene="SCN3B"
                     /gene_synonym="ATFB16; BRGDA7; HSA243396; SCNB3"
                     /coded_by="NM_001040151.2:425..1072"
                     /db_xref="CCDS:CCDS8442.1"
                     /db_xref="GeneID:55800"
                     /db_xref="HGNC:HGNC:20665"
                     /db_xref="MIM:608214"
ORIGIN      
        1 mpafnrlfpl aslvliywvs vcfpvcvevp seteavqgnp mklrciscmk reeveattvv
       61 ewfyrpeggk dfliyeyrng hqevespfqg rlqwngskdl qdvsitvlnv tlndsglytc
      121 nvsrefefea hrpfvkttrl iplrvteeag edftsvvsei mmyillvflt lwlliemiyc
      181 yrkvskaeea aqenasdyla ipsenkensa vpvee
//
LOCUS       NP_001268734             704 aa            linear   PRI 21-NOV-2025
DEFINITION  fibronectin type III and SPRY domain-containing protein 2 isoform b
            [Homo sapiens].
ACCESSION   NP_001268734 XP_005272485
VERSION     NP_001268734.1
DBSOURCE    REFSEQ: accession NM_001281805.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 704)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 704)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 704)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 704)
  AUTHORS   Benson,M.A., Tinsley,C.L., Waite,A.J., Carlisle,F.A., Sweet,S.M.M.,
            Ehler,E., George,C.H., Lai,F.A., Martin-Rendon,E. and Blake,D.J.
  TITLE     Ryanodine receptors are part of the myospryn complex in cardiac
            muscle
  JOURNAL   Sci Rep 7 (1), 6312 (2017)
   PUBMED   28740084
  REMARK    GeneRIF: Data identify a novel muscle-expressed TRIM-related
            protein minispryn, encoded by Fsd2, that has extensive sequence
            similarity with the C-terminus of Cmya5. They appear to have
            originated by a chromosomal duplication and are found within
            evolutionarily-conserved gene clusters on different chromosomes.
            Both proteins co-localize with RyR2 at the junctional sarcoplasmic
            reticulum of isolated cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 704)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 704)
  AUTHORS   Dong,C., Beecham,A., Slifer,S., Wang,L., Blanton,S.H., Wright,C.B.,
            Rundek,T. and Sacco,R.L.
  TITLE     Genomewide linkage and peakwide association analyses of carotid
            plaque in Caribbean Hispanics
  JOURNAL   Stroke 41 (12), 2750-2756 (2010)
   PUBMED   20966410
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA826684.1, BC144175.1,
            AC105339.9 and AL833295.1.
            
            On Aug 31, 2013 this sequence version replaced XP_005272485.1.
            
            Summary: This gene encodes a protein that belongs to the FN3/SPRY
            family of proteins. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (2) contains an alternate exon in
            the 5' UTR and lacks an alternate in-frame exon compared to variant
            1. The encoded isoform (b) is shorter than isoform a. Variants 2
            and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC144175.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA2144120 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2"
     Protein         1..704
                     /product="fibronectin type III and SPRY domain-containing
                     protein 2 isoform b"
                     /note="SPRY domain containing 1; fibronectin type III and
                     SPRY domain-containing protein 2; SPRY domain-containing
                     protein 1; minispryn"
                     /calculated_mol_wt=80160
     Region          188..>333
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     Region          424..516
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(424,489,504)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(505..506,508..509)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          520..695
                     /region_name="SPRY_PRY_TRIM76_like"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     protein 76 (TRIM76)-like; cd12899"
                     /db_xref="CDD:293956"
     CDS             1..704
                     /gene="FSD2"
                     /gene_synonym="SPRYD1"
                     /coded_by="NM_001281805.2:300..2414"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS61738.1"
                     /db_xref="GeneID:123722"
                     /db_xref="HGNC:HGNC:18024"
ORIGIN      
        1 meeesgeelg ldrstpkdfh fyhmdlydse drlhlfpeen trmrkvvqae manesrgagd
       61 gkaqrdlqee vdelvhlygl eddhelgdef vdeniprtgv seyppymmkr rdpareqrdw
      121 rlsgeaaeae dlgfggwgsa gqcqdlreay rythgrasee yecyvipeee deeeaadvfc
      181 vtcktpiraf qkvfdehkeh eviplneale sakdeihknm yklekqiiem enfanhleev
      241 fitveenfgk qeqnfeshyn eiletlaqky eekiqalgek kkeklealyg qlvscgenld
      301 tckelmetie emcheekvdf ikdavamadr lgkflktktd veisaqpefe dqtldfsdve
      361 qlmgsintip apsapvinpq vpnsatgssv rvcwslysdd tvesyqlsyr pvqdsspgtd
      421 qaapsppiik tkeirsceea vlicwesgnl npvdsytvel tqaespeasg vtesvvgipt
      481 cesvvqlqpg rsyiiyvral nmggpsvrse patvhtigsy frlnkdtchp wltisedglt
      541 avrserrtpa relspsdthf trcvavmgnl ipvrghhywe vevdehldyr vgvafadvrk
      601 qedlgancls wcmrhtfass rhkyeflhnr ttpdiritvp pkkigilldy ehsklsffnv
      661 dlsqhlytfs cqlhefvhpc fslekpgclk vhngismpkh vtfy
//
LOCUS       NP_001265371             318 aa            linear   PRI 21-NOV-2025
DEFINITION  scaffold protein ILK isoform 3 [Homo sapiens].
ACCESSION   NP_001265371
VERSION     NP_001265371.1
DBSOURCE    REFSEQ: accession NM_001278442.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Bildyug,N.
  TITLE     Inhibition of Integrin-Associated Kinases FAK and ILK on the In
            Vitro Model of Skin Wound Healing
  JOURNAL   Appl Biochem Biotechnol 196 (8), 5604-5615 (2024)
   PUBMED   38165590
  REMARK    GeneRIF: Inhibition of Integrin-Associated Kinases FAK and ILK on
            the In Vitro Model of Skin Wound Healing.
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Campillo,S., Gutierrez-Calabres,E., Garcia-Miranda,S., Griera,M.,
            Fernandez Rodriguez,L., de Frutos,S., Rodriguez-Puyol,D. and
            Calleros,L.
  TITLE     Integrin-linked kinase mRNA expression in circulating mononuclear
            cells as a biomarker of kidney and vascular damage in experimental
            chronic kidney disease
  JOURNAL   Cell Commun Signal 22 (1), 264 (2024)
   PUBMED   38734696
  REMARK    GeneRIF: Integrin-linked kinase mRNA expression in circulating
            mononuclear cells as a biomarker of kidney and vascular damage in
            experimental chronic kidney disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Ahmed,A.U., Almasabi,S., Firestein,R. and Williams,B.R.G.
  TITLE     Integrin-linked kinase expression in myeloid cells promotes colon
            tumorigenesis
  JOURNAL   Front Immunol 14, 1270194 (2023)
   PUBMED   38077324
  REMARK    GeneRIF: Integrin-linked kinase expression in myeloid cells
            promotes colon tumorigenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Hannigan,G.E., McDonald,P.C., Walsh,M.P. and Dedhar,S.
  TITLE     Integrin-linked kinase: not so 'pseudo' after all
  JOURNAL   Oncogene 30 (43), 4375-4385 (2011)
   PUBMED   21602880
  REMARK    Review article
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Melchior,C., Kreis,S., Janji,B. and Kieffer,N.
  TITLE     Promoter characterization and genomic organization of the gene
            encoding integrin-linked kinase 1
  JOURNAL   Biochim Biophys Acta 1575 (1-3), 117-122 (2002)
   PUBMED   12020826
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Delcommenne,M., Tan,C., Gray,V., Rue,L., Woodgett,J. and Dedhar,S.
  TITLE     Phosphoinositide-3-OH kinase-dependent regulation of glycogen
            synthase kinase 3 and protein kinase B/AKT by the integrin-linked
            kinase
  JOURNAL   Proc Natl Acad Sci U S A 95 (19), 11211-11216 (1998)
   PUBMED   9736715
REFERENCE   8  (residues 1 to 318)
  AUTHORS   Li,F., Liu,J., Mayne,R. and Wu,C.
  TITLE     Identification and characterization of a mouse protein kinase that
            is highly homologous to human integrin-linked kinase
  JOURNAL   Biochim Biophys Acta 1358 (3), 215-220 (1997)
   PUBMED   9366252
REFERENCE   9  (residues 1 to 318)
  AUTHORS   Hannigan,G.E., Bayani,J., Weksberg,R., Beatty,B., Pandita,A.,
            Dedhar,S. and Squire,J.
  TITLE     Mapping of the gene encoding the integrin-linked kinase, ILK, to
            human chromosome 11p15.5-p15.4
  JOURNAL   Genomics 42 (1), 177-179 (1997)
   PUBMED   9177792
REFERENCE   10 (residues 1 to 318)
  AUTHORS   Hannigan,G.E., Leung-Hagesteijn,C., Fitz-Gibbon,L., Coppolino,M.G.,
            Radeva,G., Filmus,J., Bell,J.C. and Dedhar,S.
  TITLE     Regulation of cell adhesion and anchorage-dependent growth by a new
            beta 1-integrin-linked protein kinase
  JOURNAL   Nature 379 (6560), 91-96 (1996)
   PUBMED   8538749
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK293474.1.
            
            Summary: This gene encodes a protein with a kinase-like domain and
            four ankyrin-like repeats. The encoded protein associates at the
            cell membrane with the cytoplasmic domain of beta integrins, where
            it regulates integrin-mediated signal transduction. Activity of
            this protein is important in the epithelial to mesenchymal
            transition, and over-expression of this gene is implicated in tumor
            growth and metastasis. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (5) uses an alternate splice site
            in the 5' UTR, lacks an exon in the 5' coding region, and initiates
            translation at a downstream in-frame start codon, compared to
            variant 1. The encoded isoform (3) has a shorter N-terminus,
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293474.1, SRR14038192.2205759.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..318
                     /product="scaffold protein ILK isoform 3"
                     /EC_number="2.7.11.1"
                     /note="integrin-linked kinase-2; 59 kDa
                     serine/threonine-protein kinase; integrin-linked protein
                     kinase; epididymis secretory protein Li 28;
                     beta-integrin-linked kinase; inactive integrin-linked
                     kinase; scaffold protein ILK"
                     /calculated_mol_wt=36336
     Region          63..315
                     /region_name="PK_ILK"
                     /note="Pseudokinase domain of Integrin Linked Kinase;
                     cd14057"
                     /db_xref="CDD:270959"
     Site            order(66,68..70,73,84,86,135..138,145,189,192,205,207)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270959"
     Site            order(91,214..217,227..230,262..265,267..269,272)
                     /site_type="other"
                     /note="Parvin interface [polypeptide binding]"
                     /db_xref="CDD:270959"
     CDS             1..318
                     /gene="ILK"
                     /gene_synonym="HEL-S-28; ILK-1; ILK-2; P59; p59ILK"
                     /coded_by="NM_001278442.2:332..1288"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS60713.1"
                     /db_xref="GeneID:3611"
                     /db_xref="HGNC:HGNC:6040"
                     /db_xref="MIM:602366"
ORIGIN      
        1 mpvdkakapl rellreraek mgqnlnripy kdtfwkgttr trprngtlnk hsgidfkqln
       61 fltklnenhs gelwkgrwqg ndivvkvlkv rdwstrksrd fneecprlri fshpnvlpvl
      121 gacqsppaph ptlithwmpy gslynvlheg tnfvvdqsqa vkfaldmarg maflhtlepl
      181 iprhalnsrs vmidedmtar ismadvkfsf qcpgrmyapa wvapealqkk pedtnrrsad
      241 mwsfavllwe lvtrevpfad lsnmeigmkv aleglrptip pgisphvckl mkicmnedpa
      301 krpkfdmivp ilekmqdk
//
LOCUS       NP_001362670             390 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform sss [Homo sapiens].
ACCESSION   NP_001362670
VERSION     NP_001362670.1
DBSOURCE    REFSEQ: accession NM_001375741.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 390)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 390)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 390)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.777948.1,
                                           SRR14038196.1915340.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..390
                     /product="abl interactor 2 isoform sss"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=42971
     Region          39..100
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          329..389
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(337,339,342,346,364..365,378,380..381)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..390
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375741.1:122..1294"
                     /note="isoform sss is encoded by transcript variant 76"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqt vdihkekvar reigilttnk
       61 ntsrthkiia panlerpvry irkpidytil ddighgvkvs tqnmkmgglp rttpptqkpp
      121 sppmsgkgtl grhspyrtle pvrppvvpnd yvpsptrnma psqqspvrta svnqrnrtys
      181 ssgssggshp ssrsssrens gsgsvgvpia vptpsppsvf pghpvqfysm nrpasrhtpp
      241 tiggslpyrr ppsitsqtsl qnqmnggpfy sqnpvsdtpp ppppveepvf desppppppp
      301 edyeeeeaav veysdpyaee dppwaprsyl ekvvaiydyt kdkedelsfq egaiiyvikk
      361 nddgwyegvm ngvtglfpgn yvesimhyse
//
LOCUS       NP_001371717            1168 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 13 [Homo sapiens].
ACCESSION   NP_001371717 XP_016861889
VERSION     NP_001371717.1
DBSOURCE    REFSEQ: accession NM_001384788.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1168)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1168)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1168)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1168)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1168)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1168)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1168)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1168)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1168)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1168)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            On Jun 26, 2020 this sequence version replaced XP_016861889.1.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.100674.1,
                                           SRR14372080.1886437.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1168
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1168
                     /product="microtubule-associated protein 4 isoform 13"
                     /note="MAP-4"
                     /calculated_mol_wt=122621
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          265..562
                     /region_name="17 X 14 AA tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          379..418
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            457
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            538
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          <592..936
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            602
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          658..1008
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            704
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10791892,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            804
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10791892,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            814
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            820
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            842
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            844
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            870
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            945
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          <948..969
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            958
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            959
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          1009..1039
                     /region_name="Tau/MAP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1009..1038
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            1017
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          1040..1070
                     /region_name="Tau/MAP 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1040..1069
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          1071..1102
                     /region_name="Tau/MAP 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1071..1101
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            1090
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            1168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     CDS             1..1168
                     /gene="MAP4"
                     /coded_by="NM_001384788.1:96..3602"
                     /note="isoform 13 is encoded by transcript variant 49"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedlplpp hpaslsfhlp ldtpsskptl langghgveg sdttgsptef
      121 leekmayqey pnsqnwpedt nfcfqpeqvv dpiqtdpfkm yhdddladlv fpssatadts
      181 ifagqndplk dsygmspcnt avvpqgwsve alnsphsesf vspeavaepp qptavplela
      241 keiemaseer ppaqaleimm glkttdmaps ketemalakd malatkteva lakdmesptk
      301 ldvtlakdmq psmesdmalv kdmelpteke valvkdvrwp tetdvssakn vvlpteteva
      361 pakdvtllke teraspikmd lapskdmgpp kenkketera spikmdlaps kdmgppkenk
      421 ivpakdlvll seievaqand iissteissa ekvalssete valardmtlp petnviltkd
      481 kalpleaeva pvkdmaqlpe teiapakdva pstvkevgll kdmsplsete malgkdvtpp
      541 petevvlikn vclppemeva ltedqvpalk teaplakdgv ltlannvtpa kdvpplsete
      601 atpvpikdme iaqtqkgise dshleslqdv gqsaaptfmi spetvtgtgk kcslpaeeds
      661 vleklgerkp cnsqpselss etsgiarpee grpvvsgtgn dittppnkel ppspekktkp
      721 lattqpakts tskaktqpts lpkqpaptti gglnkkpmsl asglvpaapp krpavasarp
      781 silpskdvkp kpiadakape kraspskpas apasrsgsks tqtvakttta aavastgpss
      841 rspstllpkk ptaiktegkp aevkkmtaks vpadlsrpks tstssmkktt tlsgtapaag
      901 vvpsrvkatp mpsrpsttpf idkkptsakp ssttprlsrl atntsapdlk nvrskvgste
      961 nikhqpgggr akvekkteaa attrkpesna vtktagpias aqkqpagkvq ivskkvsysh
     1021 iqskcgskdn ikhvpgggnv qiqnkkvdis kvsskcgska nikhkpgggd vkiesqklnf
     1081 kekaqakvgs ldnvghlpag gavktegggs eaplcpgppa geepaiseaa peagaptsas
     1141 glnghptlsg ggdqreaqtl dsqiqetn
//
LOCUS       NP_001309185            1467 aa            linear   PRI 21-NOV-2025
DEFINITION  helicase ARIP4 isoform a [Homo sapiens].
ACCESSION   NP_001309185 XP_006713124
VERSION     NP_001309185.1
DBSOURCE    REFSEQ: accession NM_001322256.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1467)
  AUTHORS   Ng,R.R., Lin,Z., Zhang,Y., Ti,S.C., Javed,A., Wong,J.W.H., Fang,Q.,
            Leung,J.W.C., Tang,A.H.N. and Huen,M.S.Y.
  TITLE     R-loop resolution by ARIP4 helicase promotes androgen-mediated
            transcription induction
  JOURNAL   Sci Adv 10 (29), eadm9577 (2024)
   PUBMED   39028815
REFERENCE   2  (residues 1 to 1467)
  AUTHORS   He,Q., Hao,Q., Wu,Y., Vadgama,J.V. and Jiang,Y.
  TITLE     CircRAD54L2 promotes triple-negative breast cancer progression by
            regulating the miR-888 family/PDK1 axis
  JOURNAL   Life Sci 312, 121128 (2023)
   PUBMED   36334805
  REMARK    GeneRIF: CircRAD54L2 promotes triple-negative breast cancer
            progression by regulating the miR-888 family/PDK1 axis.
REFERENCE   3  (residues 1 to 1467)
  AUTHORS   Geng,T., Li,M., Chen,R., Yang,S., Jin,G., Jin,T. and Chen,F.
  TITLE     Impact of GTF2H1 and RAD54L2 polymorphisms on the risk of lung
            cancer in the Chinese Han population
  JOURNAL   BMC Cancer 22 (1), 1181 (2022)
   PUBMED   36384536
  REMARK    GeneRIF: Impact of GTF2H1 and RAD54L2 polymorphisms on the risk of
            lung cancer in the Chinese Han population.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1467)
  AUTHORS   Muraszko,J., Kramarz,K., Argunhan,B., Ito,K., Baranowska,G.,
            Kurokawa,Y., Murayama,Y., Tsubouchi,H., Lambert,S., Iwasaki,H. and
            Dziadkowiec,D.
  TITLE     Rrp1 translocase and ubiquitin ligase activities restrict the
            genome destabilising effects of Rad51 in fission yeast
  JOURNAL   Nucleic Acids Res 49 (12), 6832-6848 (2021)
   PUBMED   34157114
REFERENCE   5  (residues 1 to 1467)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 1467)
  AUTHORS   Tsuchiya,M., Isogai,S., Taniguchi,H., Tochio,H., Shirakawa,M.,
            Morohashi,K.I., Hiraoka,Y., Haraguchi,T. and Ogawa,H.
  TITLE     Selective autophagic receptor p62 regulates the abundance of
            transcriptional coregulator ARIP4 during nutrient starvation
  JOURNAL   Sci Rep 5, 14498 (2015)
   PUBMED   26412716
  REMARK    GeneRIF: p62 is a novel binding partner for ARIP4, and that its
            binding regulates the cellular protein level of ARIP4 under
            conditions of metabolic stress.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1467)
  AUTHORS   Ogawa,H., Komatsu,T., Hiraoka,Y. and Morohashi,K.
  TITLE     Transcriptional Suppression by Transient Recruitment of ARIP4 to
            Sumoylated nuclear receptor Ad4BP/SF-1
  JOURNAL   Mol Biol Cell 20 (19), 4235-4245 (2009)
   PUBMED   19692572
  REMARK    GeneRIF: The ATPase activity of ARIP4 was stimulated in the
            presence of sumoylated Ad4BP/SF-1 and the Ad4BP/SF-1-binding site
            containing double-stranded DNA.
REFERENCE   8  (residues 1 to 1467)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   9  (residues 1 to 1467)
  AUTHORS   Janne,O.A., Moilanen,A.M., Poukka,H., Rouleau,N., Karvonen,U.,
            Kotaja,N., Hakli,M. and Palvimo,J.J.
  TITLE     Androgen-receptor-interacting nuclear proteins
  JOURNAL   Biochem Soc Trans 28 (4), 401-405 (2000)
   PUBMED   10961928
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092037.2, AC113933.2 and AC099050.2.
            
            On Apr 8, 2016 this sequence version replaced XP_006713124.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1966682,
                              SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1467
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.2"
     Protein         1..1467
                     /product="helicase ARIP4 isoform a"
                     /EC_number="3.6.4.12"
                     /note="helicase ARIP4; RAD54-like protein 2; androgen
                     receptor-interacting protein 4; AR interacting protein 4"
                     /calculated_mol_wt=162638
     Region          1..150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4B4.4)"
     Region          110..890
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
     Region          186..234
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4B4.4)"
     Region          271..547
                     /region_name="DEXHc_ARIP4"
                     /note="DEXH-box helicase domain of ARIP4; cd18069"
                     /db_xref="CDD:350827"
     Site            order(307..313,346,463..464)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350827"
     Region          463..466
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4B4.4)"
     Region          551..555
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4B4.4)"
     Region          649..673
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4B4.4)"
     Region          <1106..1414
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1120..1171
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4B4.4)"
     Site            1169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4B4.4)"
     Site            1172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4B4.4)"
     Region          1184..1221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4B4.4)"
     Region          1247..1284
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4B4.4)"
     Site            1260
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4B4.4)"
     Region          1329..1333
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4B4.4)"
     Region          1445..1467
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4B4.4)"
     CDS             1..1467
                     /gene="RAD54L2"
                     /gene_synonym="ARIP4; HSPC325; SRISNF2L"
                     /coded_by="NM_001322256.2:252..4655"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS33765.2"
                     /db_xref="GeneID:23132"
                     /db_xref="HGNC:HGNC:29123"
                     /db_xref="MIM:620006"
ORIGIN      
        1 msdesasgsd pdldpdvele daeeeeeeee vaveecdrdd eedllddpsl egmcgtehaq
       61 lgedgqqppr ctsttssqse pseqlrrhqg knlasedpkk kraqkpshmr rnirkllred
      121 qlepvtkaaq qeelerrkrl eqqrkdyaap iptvpleflp eeialrasdg pqlpprvlaq
      181 evicldsssg sedekssrde vielssgeed tlhivdsses vseddeeeek ggthvndvln
      241 qrdalgrvlv nlnhppeeen vflapqlara vkphqiggir flydnlvesl erfktssgfg
      301 cilahsmglg ktlqvisfid vlfrhtpakt vlaivpvntl qnwlaefnmw lpppealpad
      361 nkpeevqprf fkvhilndeh ktmasrakvm adwvseggvl lmgyemyrll tlkksfatgr
      421 pkktkkrshp viidldeedr qqefrrefek alcrpgpdvv icdeghrikn cqastsqalk
      481 nirsrrrvvl tgyplqnnli eywcmvdfvr pdflgtrqef snmferpiln gqcidstpqd
      541 vrlmryrshv lhsllegfvq rrghtvlkih lpakeenvil vrlskiqrdl ytqfmdrfrd
      601 cgssgwlgln plkafcvcck iwnhpdvlye alqkeslane qdldveelgs agtsarcppq
      661 gtkgkgedst lassmgeatn skflqgvgfn pfqergnniv tyewakdllt nyqtgvlens
      721 pkmvllfhli eesvklgdki lvfsqslstl alieeflgkr evpcppgteg qgaqkwvrni
      781 syfrldgstp afererlinq fndpsnlttw lfllstragc lgvnliganr vvvfdaswnp
      841 chdaqavcrv yrygqkkpcy iyrlvadytl ekkiydrqis kqgmsdrvvd dlnpmlnftr
      901 kevenllhfv ekepapqvsl nvkgikesvl qlaclkyphl itkepfehes lllnrkdhkl
      961 tkaekkaakk syeedkrtsv pytrpsyaqy ypasdqslts ipafsqrnwq ptlkgdekpv
     1021 asvrpvqstp ipmmprhvpl ggsvssasst npsmnfpiny lqragvlvqk vvtttdivip
     1081 glnsstdvqa rinagesihi irgtkgtyir tsdgrifavr atgkpkvped grmaasgsqg
     1141 pscestsngr hsasspkapd peglarpvsp dspeiiselq qyadvaaare srqsspstna
     1201 alpgppaqlm dssavpgtal gteprlgghc lnssllvtgq pcgdrhpvld lrghkrklat
     1261 ppaaqessrr rsrkghlpap vqpyehgypv sggfamppvs lnhnlttpft sqagenslfm
     1321 gstpsyyqls nlladarlvf pvttdplvpa gpvsssstat svtasnpsfm lnpsvpgilp
     1381 syslpfsqpl lseprmfapf pspvlpsnls rgmsiypgym sphagypagg llrsqvppfd
     1441 shevaevgfs snddedkddd vievtgk
//
LOCUS       NP_001362616             474 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform aa [Homo sapiens].
ACCESSION   NP_001362616 XP_016858614
VERSION     NP_001362616.1
DBSOURCE    REFSEQ: accession NM_001375687.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 474)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 474)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 474)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 474)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 474)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 474)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 474)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            On Oct 31, 2019 this sequence version replaced XP_016858614.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.104256.1,
                                           SRR18074967.370560.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..474
                     /product="abl interactor 2 isoform aa"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=52228
     Region          93..156
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          413..473
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(421,423,426,430,448..449,462,464..465)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..474
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375687.1:122..1546"
                     /note="isoform aa is encoded by transcript variant 32"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqs adkqraleet kayttqslas
       61 vaylintlan nvlqmldiqa sqlrrmessi nhisqtvdih kekvarreig ilttnkntsr
      121 thkiiapanl erpvryirkp idytilddig hgvkvstqnm kmgglprttp ptqkppsppm
      181 sgkgtlgrhs pyrtlepvrp pvvpndyvps ptrnmapsqq spvrtasvnq rnrtyssgss
      241 ggshpssrss srensgsgsv gvpiavptps ppsvfpghpv qfysmnrpas rhtpptiggs
      301 lpyrrppsit sqtslqnqmn ggpfysqnpv slappppsil qvtpqlplmg fvarvqenis
      361 dtppppppve epvfdesppp ppppedyeee eaavveysdp yaeedppwap rsylekvvai
      421 ydytkdkede lsfqegaiiy vikknddgwy egvmngvtgl fpgnyvesim hyse
//
LOCUS       NP_001349997             922 aa            linear   PRI 21-NOV-2025
DEFINITION  cell cycle and apoptosis regulator protein 2 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001349997 XP_016869206
VERSION     NP_001349997.1
DBSOURCE    REFSEQ: accession NM_001363068.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 922)
  AUTHORS   Wang,Y., Wang,J.M., Xiao,Y., Hu,X.B., Zheng,S.Y., Fu,J.L.,
            Zhang,L., Gan,Y.W., Liang,X.M. and Li,D.W.
  TITLE     SUMO1-regulated DBC1 promotes p53-dependent stress-induced
            apoptosis of lens epithelial cells
  JOURNAL   Aging (Albany NY) 15 (17), 8812-8832 (2023)
   PUBMED   37683133
  REMARK    GeneRIF: SUMO1-regulated DBC1 promotes p53-dependent stress-induced
            apoptosis of lens epithelial cells.
REFERENCE   3  (residues 1 to 922)
  AUTHORS   Kim,H.J., Moon,S.J. and Kim,J.H.
  TITLE     Mechanistic insights into the dual role of CCAR2/DBC1 in cancer
  JOURNAL   Exp Mol Med 55 (8), 1691-1701 (2023)
   PUBMED   37524873
  REMARK    GeneRIF: Mechanistic insights into the dual role of CCAR2/DBC1 in
            cancer.
            Review article
REFERENCE   4  (residues 1 to 922)
  AUTHORS   Sarwar,Z., Nabi,N., Bhat,S.A., Gillani,S.Q., Reshi,I., Un Nisa,M.,
            Adelmant,G., A Marto,J. and Andrabi,S.
  TITLE     Interaction of DBC1 with polyoma small T antigen promotes its
            degradation and negatively regulates tumorigenesis
  JOURNAL   J Biol Chem 298 (2), 101496 (2022)
   PUBMED   34921839
  REMARK    GeneRIF: Interaction of DBC1 with polyoma small T antigen promotes
            its degradation and negatively regulates tumorigenesis.
REFERENCE   5  (residues 1 to 922)
  AUTHORS   Chen,L., Zhou,S.J., Xu,Y., Liao,Q.M., Zou,Y.S. and Pei,H.
  TITLE     CCAR2 promotes a malignant phenotype of osteosarcoma through
            Wnt/beta-catenin-dependent transcriptional activation of SPARC
  JOURNAL   Biochem Biophys Res Commun 580, 67-73 (2021)
   PUBMED   34624572
  REMARK    GeneRIF: CCAR2 promotes a malignant phenotype of osteosarcoma
            through Wnt/beta-catenin-dependent transcriptional activation of
            SPARC.
REFERENCE   6  (residues 1 to 922)
  AUTHORS   Hafler,D.A., Compston,A., Sawcer,S., Lander,E.S., Daly,M.J., De
            Jager,P.L., de Bakker,P.I., Gabriel,S.B., Mirel,D.B., Ivinson,A.J.,
            Pericak-Vance,M.A., Gregory,S.G., Rioux,J.D., McCauley,J.L.,
            Haines,J.L., Barcellos,L.F., Cree,B., Oksenberg,J.R. and
            Hauser,S.L.
  CONSRTM   International Multiple Sclerosis Genetics Consortium
  TITLE     Risk alleles for multiple sclerosis identified by a genomewide
            study
  JOURNAL   N Engl J Med 357 (9), 851-862 (2007)
   PUBMED   17660530
REFERENCE   7  (residues 1 to 922)
  AUTHORS   Trauernicht,A.M., Kim,S.J., Kim,N.H. and Boyer,T.G.
  TITLE     Modulation of estrogen receptor alpha protein level and survival
            function by DBC-1
  JOURNAL   Mol Endocrinol 21 (7), 1526-1536 (2007)
   PUBMED   17473282
  REMARK    GeneRIF: biological function for DBC-1 in the modulation of ERalpha
            expression and hormone-independent breast cancer cell survival
            GeneRIF: DBC-1 functions to modulate ER alpha expression and
            hormone-independent breast cancer cell survival.
REFERENCE   8  (residues 1 to 922)
  AUTHORS   Koch,H.B., Zhang,R., Verdoodt,B., Bailey,A., Zhang,C.D., Yates,J.R.
            3rd, Menssen,A. and Hermeking,H.
  TITLE     Large-scale identification of c-MYC-associated proteins using a
            combined TAP/MudPIT approach
  JOURNAL   Cell Cycle 6 (2), 205-217 (2007)
   PUBMED   17314511
REFERENCE   9  (residues 1 to 922)
  AUTHORS   Sundararajan,R., Chen,G., Mukherjee,C. and White,E.
  TITLE     Caspase-dependent processing activates the proapoptotic activity of
            deleted in breast cancer-1 during tumor necrosis
            factor-alpha-mediated death signaling
  JOURNAL   Oncogene 24 (31), 4908-4920 (2005)
   PUBMED   15824730
  REMARK    GeneRIF: Caspase-dependent processing of DBC-1 may act as a
            feed-forward mechanism to promote apoptosis and possibly also tumor
            suppression.
REFERENCE   10 (residues 1 to 922)
  AUTHORS   Hamaguchi,M., Meth,J.L., von Klitzing,C., Wei,W., Esposito,D.,
            Rodgers,L., Walsh,T., Welcsh,P., King,M.C. and Wigler,M.H.
  TITLE     DBC2, a candidate for a tumor suppressor gene involved in breast
            cancer
  JOURNAL   Proc Natl Acad Sci U S A 99 (21), 13647-13652 (2002)
   PUBMED   12370419
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB240982.1, DA721640.1, BC065495.1, AL834351.1, AL137523.1 and
            AC037459.16.
            
            On May 5, 2018 this sequence version replaced XP_016869206.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.137705.1,
                                           SRR1803615.262685.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..922
                     /product="cell cycle and apoptosis regulator protein 2
                     isoform 2"
                     /note="deleted in breast cancer 1; cell division cycle and
                     apoptosis regulator protein 2; cell cycle and apoptosis
                     regulator protein 2"
                     /calculated_mol_wt=102700
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N163.2)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N163.2)"
     Region          55..112
                     /region_name="S1-like"
                     /note="pfam14444"
                     /db_xref="CDD:464176"
     Site            112
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by KAT8.
                     /evidence=ECO:0000269|PubMed:24126058; propagated from
                     UniProtKB/Swiss-Prot (Q8N163.2)"
     Site            123
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8N163.2)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N163.2)"
     Region          178..218
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N163.2)"
     Site            180
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8N163.2)"
     Site            215
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by KAT8.
                     /evidence=ECO:0000269|PubMed:24126058,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8N163.2)"
     Region          234..315
                     /region_name="BURAN"
                     /note="BURAN domain; pfam19257"
                     /db_xref="CDD:466013"
     Region          340..457
                     /region_name="DBC1"
                     /note="pfam14443"
                     /db_xref="CDD:464175"
     Region          446..510
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N163.2)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ATM, ATR and CK2.
                     /evidence=ECO:0000269|PubMed:22735644,
                     ECO:0000269|PubMed:24962073, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N163.2)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8N163.2)"
     Region          <512..560
                     /region_name="LAIKA"
                     /note="LAIKA domain; pfam19256"
                     /db_xref="CDD:466012"
     Region          568..643
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N163.2)"
     Site            569
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8N163.2)"
     Site            627
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8N163.2)"
     Site            674
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N163.2)"
     Site            677
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N163.2)"
     Site            680
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N163.2)"
     Site            686
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8N163.2)"
     Region          703..922
                     /region_name="Interaction with NR1D1.
                     /evidence=ECO:0000269|PubMed:23398316"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N163.2)"
     Site            807
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N163.2)"
     Site            896
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N163.2)"
     CDS             1..922
                     /gene="CCAR2"
                     /gene_synonym="DBC-1; DBC1; KIAA1967; NET35; p30 DBC;
                     p30DBC"
                     /coded_by="NM_001363068.2:416..3184"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:57805"
                     /db_xref="HGNC:HGNC:23360"
                     /db_xref="MIM:607359"
ORIGIN      
        1 msqfkrqrin plpggrnfsg tastsllgpp pglltppvat elsqnarhlq ggekqrvftg
       61 ivtslhdyfg vvdeevffql svvkgrlpql gekvlvkaay npgqavpwna vkvqtlsnqp
      121 llkspappll hvaalgqkqg ilgaqpqlif qphripplfp qkplslfqts htlhlshlnr
      181 fpargphgrl dqgrsddyds kkrkqragge pwgakkprhd lppyrvhltp ytvdspicdf
      241 lelqrryrsl lvpsdflsvh lswlsafpls qpfslhhpsr iqvssekeaa pdagaepita
      301 dsdpaysskv lllsspglee lyrccmlfvd dmaepretpe hplkqikfll grkeeeavlv
      361 ggewspsldg ldpqadpqvl vrtaircaqa qtgidlsgct kwwrfaefqy lqpgpprrlq
      421 tvvvylpdvw timptleewe alcqqkaaea apptqeaqge tepteqapda leqaadtsrr
      481 naetpeattq qetdtdlpea pppplepavi arpgcvnlsl hgivedrrpk erisfevmvl
      541 aelflemlqr dfgyrvykml lslpekvvsp pepekeeaak eeatkeeeai keevvkepkd
      601 eaqnegpate seaplkedgl lpkplssgge eeekprgeas edlcemaldp ellllrddge
      661 eefgakleds evrsvasnqs emefsslqdm pkeldpsavl pldcllafvf fdanwcgylh
      721 rrdlerillt lgirlsaeqa kqlvsrvvtq nicqyrslqy srqegldggl peevlfgnld
      781 llpppgkstk pgaaptehka lvshngslin vgsllqraeq qdsgrlylen kihtlelkle
      841 eshnrfsate vtnktlaaem qelrvrlaea eetartaerq ksqlqrllqe lrrrltplql
      901 eiqrvvekad swvekeepap sn
//
LOCUS       NP_001258907             426 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase 25 isoform 1 [Homo sapiens].
ACCESSION   NP_001258907
VERSION     NP_001258907.1
DBSOURCE    REFSEQ: accession NM_001271978.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Chen,K.Q., Lei,G.L., Ke,B.Y., Chen,L., Wang,Z.B. and Wang,S.Z.
  TITLE     STK25: a viable therapeutic target for cancer treatments?
  JOURNAL   Anticancer Drugs 34 (9), 995-1001 (2023)
   PUBMED   36728989
  REMARK    GeneRIF: STK25: a viable therapeutic target for cancer treatments?
            Review article
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Zhang,X., Wang,B.Z., Kim,M., Nash,T.R., Liu,B., Rao,J., Lock,R.,
            Tamargo,M., Soni,R.K., Belov,J., Li,E., Vunjak-Novakovic,G. and
            Fine,B.
  TITLE     STK25 inhibits PKA signaling by phosphorylating PRKAR1A
  JOURNAL   Cell Rep 40 (7), 111203 (2022)
   PUBMED   35977512
  REMARK    GeneRIF: STK25 inhibits PKA signaling by phosphorylating PRKAR1A.
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Chen,J., Gao,P., Peng,L., Liu,T., Wu,F., Xu,K., Chen,L., Tan,F.,
            Xing,P., Wang,Z., Di,J., Jiang,B. and Su,X.
  TITLE     Downregulation of STK25 promotes autophagy via the Janus kinase
            2/signal transducer and activator of transcription 3 pathway in
            colorectal cancer
  JOURNAL   Mol Carcinog 61 (6), 572-586 (2022)
   PUBMED   35349179
  REMARK    GeneRIF: Downregulation of STK25 promotes autophagy via the Janus
            kinase 2/signal transducer and activator of transcription 3 pathway
            in colorectal cancer.
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Voss,K., Stahl,S., Schleider,E., Ullrich,S., Nickel,J.,
            Mueller,T.D. and Felbor,U.
  TITLE     CCM3 interacts with CCM2 indicating common pathogenesis for
            cerebral cavernous malformations
  JOURNAL   Neurogenetics 8 (4), 249-256 (2007)
   PUBMED   17657516
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Findlay,G.M., Yan,L., Procter,J., Mieulet,V. and Lamb,R.F.
  TITLE     A MAP4 kinase related to Ste20 is a nutrient-sensitive regulator of
            mTOR signalling
  JOURNAL   Biochem J 403 (1), 13-20 (2007)
   PUBMED   17253963
  REMARK    GeneRIF: Ste20 family member (MAP4K3) that is required for maximal
            S6K (S6 kinase)/4E-BP1 [eIF4E (eukaryotic initiation factor 4E)
            that is required for maximal S6K (S6 kinase).
REFERENCE   8  (residues 1 to 426)
  AUTHORS   Preisinger,C., Short,B., De Corte,V., Bruyneel,E., Haas,A.,
            Kopajtich,R., Gettemans,J. and Barr,F.A.
  TITLE     YSK1 is activated by the Golgi matrix protein GM130 and plays a
            role in cell migration through its substrate 14-3-3zeta
  JOURNAL   J Cell Biol 164 (7), 1009-1020 (2004)
   PUBMED   15037601
  REMARK    GeneRIF: 14-3-3zeta is a specific substrate for YSK1 that localizes
            to the Golgi apparatus, and potentially links YSK1 signaling at the
            Golgi apparatus with protein transport.
REFERENCE   9  (residues 1 to 426)
  AUTHORS   Osada,S., Izawa,M., Saito,R., Mizuno,K., Suzuki,A., Hirai,S. and
            Ohno,S.
  TITLE     YSK1, a novel mammalian protein kinase structurally related to
            Ste20 and SPS1, but is not involved in the known MAPK pathways
  JOURNAL   Oncogene 14 (17), 2047-2057 (1997)
   PUBMED   9160885
REFERENCE   10 (residues 1 to 426)
  AUTHORS   Pombo,C.M., Bonventre,J.V., Molnar,A., Kyriakis,J. and Force,T.
  TITLE     Activation of a human Ste20-like kinase by oxidant stress defines a
            novel stress response pathway
  JOURNAL   EMBO J 15 (17), 4537-4546 (1996)
   PUBMED   8887545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU541010.1, BC015793.1,
            AC110299.3 and HY315908.1.
            
            Summary: This gene encodes a member of the germinal centre kinase
            III (GCK III) subfamily of the sterile 20 superfamily of kinases.
            The encoded enzyme plays a role in serine-threonine liver kinase B1
            (LKB1) signaling pathway to regulate neuronal polarization and
            morphology of the Golgi apparatus. The protein is translocated from
            the Golgi apparatus to the nucleus in response to chemical anoxia
            and plays a role in regulation of cell death. A pseudogene
            associated with this gene is located on chromosome 18. Multiple
            alternatively spliced transcript variants have been observed for
            this gene. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (5) differs in the 5' UTR compared
            to variant 1. Variants 1, 4 and 5 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC015793.1, X99325.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..426
                     /product="serine/threonine-protein kinase 25 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase 25; Ste20, yeast
                     homolog; ste20-like kinase; ste20/oxidant stress response
                     kinase 1; sterile 20/oxidant stress-response kinase 1"
                     /calculated_mol_wt=47981
     Region          15..291
                     /region_name="STKc_STK25"
                     /note="Catalytic domain of Serine/Threonine Kinase 25
                     (also called Yeast Sps1/Ste20-related kinase 1); cd06642"
                     /db_xref="CDD:270810"
     Site            order(26..30,34,47,49,79,95..98,101..102,105,140,142..145,
                     147,157..158,161,175..178,180,207,216)
                     /site_type="active"
                     /db_xref="CDD:270810"
     Site            order(26..30,34,47,49,66,79,95..98,101..102,105,144..145,
                     147,158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270810"
     Site            order(29..30,140,142..144,161,175..178,180,207,216)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270810"
     Site            157..180
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270810"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15037601; propagated from
                     UniProtKB/Swiss-Prot (O00506.1)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2W1; propagated from
                     UniProtKB/Swiss-Prot (O00506.1)"
     Region          291..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00506.1)"
     CDS             1..426
                     /gene="STK25"
                     /gene_synonym="SOK1; YSK1"
                     /coded_by="NM_001271978.2:311..1591"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS2549.1"
                     /db_xref="GeneID:10494"
                     /db_xref="HGNC:HGNC:11404"
                     /db_xref="MIM:602255"
ORIGIN      
        1 mahlrgfanq hsrvdpeelf tkldrigkgs fgevykgidn htkevvaiki idleeaedei
       61 ediqqeitvl sqcdspyitr yfgsylkstk lwiimeylgg gsaldllkpg pleetyiati
      121 lreilkgldy lhserkihrd ikaanvllse qgdvkladfg vagqltdtqi krntfvgtpf
      181 wmapevikqs aydfkadiws lgitaielak geppnsdlhp mrvlflipkn spptlegqhs
      241 kpfkefveac lnkdprfrpt akellkhkfi trytkktsfl telidrykrw kseghgeess
      301 sedsdidgea edgeqgpiwt fpptirpsph sklhkgtalh ssqkpaepvk rqprsqclst
      361 lvrpvfgelk ekhkqsggsv galeelenaf slaeescpgi sdklmvhlve rvqrfshnrn
      421 hltstr
//
LOCUS       NP_001307815             251 aa            linear   PRI 21-NOV-2025
DEFINITION  ATP synthase F(1) complex subunit gamma, mitochondrial isoform 3
            [Homo sapiens].
ACCESSION   NP_001307815 XP_011517792
VERSION     NP_001307815.1
DBSOURCE    REFSEQ: accession NM_001320886.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Pecina,P., Nuskova,H., Karbanova,V., Kaplanova,V., Mracek,T. and
            Houstek,J.
  TITLE     Role of the mitochondrial ATP synthase central stalk subunits gamma
            and delta in the activity and assembly of the mammalian enzyme
  JOURNAL   Biochim Biophys Acta Bioenerg 1859 (5), 374-381 (2018)
   PUBMED   29499186
  REMARK    GeneRIF: Both gamma and delta subunits silenced cells displayed
            decreased ATP synthase function - lowered rate of ADP-stimulated
            respiration, a two-fold increased sensitivity of respiration to
            inhibitor oligomycin, and impaired utilization of mitochondrial
            membrane potential for ADP phosphorylation.
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Elston,T., Wang,H. and Oster,G.
  TITLE     Energy transduction in ATP synthase
  JOURNAL   Nature 391 (6666), 510-513 (1998)
   PUBMED   9461222
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Abrahams,J.P., Leslie,A.G., Lutter,R. and Walker,J.E.
  TITLE     Structure at 2.8 A resolution of F1-ATPase from bovine heart
            mitochondria
  JOURNAL   Nature 370 (6491), 621-628 (1994)
   PUBMED   8065448
REFERENCE   8  (residues 1 to 251)
  AUTHORS   Jabs,E.W., Thomas,P.J., Bernstein,M., Coss,C., Ferreira,G.C. and
            Pedersen,P.L.
  TITLE     Chromosomal localization of genes required for the terminal steps
            of oxidative metabolism: alpha and gamma subunits of ATP synthase
            and the phosphate carrier
  JOURNAL   Hum Genet 93 (5), 600-602 (1994)
   PUBMED   8168843
REFERENCE   9  (residues 1 to 251)
  AUTHORS   Matsuda,C., Endo,H., Ohta,S. and Kagawa,Y.
  TITLE     Gene structure of human mitochondrial ATP synthase gamma-subunit.
            Tissue specificity produced by alternative RNA splicing
  JOURNAL   J Biol Chem 268 (33), 24950-24958 (1993)
   PUBMED   8227057
REFERENCE   10 (residues 1 to 251)
  AUTHORS   Boyer,P.D., Cross,R.L. and Momsen,W.
  TITLE     A new concept for energy coupling in oxidative phosphorylation
            based on a molecular explanation of the oxygen exchange reactions
  JOURNAL   Proc Natl Acad Sci U S A 70 (10), 2837-2839 (1973)
   PUBMED   4517936
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI603806.1 and BC026049.1.
            
            On Mar 9, 2016 this sequence version replaced XP_011517792.1.
            
            Summary: This gene encodes a subunit of mitochondrial ATP synthase.
            Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an
            electrochemical gradient of protons across the inner membrane
            during oxidative phosphorylation. ATP synthase is composed of two
            linked multi-subunit complexes: the soluble catalytic core, F1, and
            the membrane-spanning component, Fo, comprising the proton channel.
            The catalytic portion of mitochondrial ATP synthase consists of 5
            different subunits (alpha, beta, gamma, delta, and epsilon)
            assembled with a stoichiometry of 3 alpha, 3 beta, and a single
            representative of the other 3. The proton channel consists of three
            main subunits (a, b, c). This gene encodes the gamma subunit of the
            catalytic core. Alternatively spliced transcript variants encoding
            different isoforms have been identified. This gene also has a
            pseudogene on chromosome 14. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) encodes isoform 3, which lacks
            a mitochondrial transit peptide compared to isoforms L and H.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2065153.1,
                                           SRR14478891.2742607.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p14"
     Protein         1..251
                     /product="ATP synthase F(1) complex subunit gamma,
                     mitochondrial isoform 3"
                     /EC_number="3.6.1.14"
                     /note="mitochondrial ATP synthase, gamma subunit 1; ATP
                     synthase gamma chain, mitochondrial; ATP synthase subunit
                     gamma, mitochondrial; F-ATPase gamma subunit; ATP
                     synthase, H+ transporting, mitochondrial F1 complex, gamma
                     polypeptide 1; ATP synthase F(1) complex subunit gamma,
                     mitochondrial"
                     /calculated_mol_wt=27497
     Region          1..250
                     /region_name="ATPsyn_F1gamma"
                     /note="ATP synthase, F1 gamma subunit; TIGR01146"
                     /db_xref="CDD:273469"
     Site            order(1,3..4,7..8,53,55..58,88..89,92..93,96,213,216..217,
                     220,226,229..230,232..233,236..237,240,242..247)
                     /site_type="other"
                     /note="core domain interface [polypeptide binding]"
                     /db_xref="CDD:213394"
     Site            order(18..19,21..22,25,28..29,178,181..182,185)
                     /site_type="other"
                     /note="delta subunit interface [polypeptide binding]"
                     /db_xref="CDD:213394"
     Site            order(91,103..108,181,184..185)
                     /site_type="other"
                     /note="epsilon subunit interface [polypeptide binding]"
                     /db_xref="CDD:213394"
     CDS             1..251
                     /gene="ATP5F1C"
                     /gene_synonym="ATP5C; ATP5C1; ATP5CL1"
                     /coded_by="NM_001320886.2:138..893"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:509"
                     /db_xref="HGNC:HGNC:833"
                     /db_xref="MIM:108729"
ORIGIN      
        1 mkmvaaakya raerelkpar iyglgslaly ekadikgped kkkhlligvs sdrglcgaih
       61 ssiakqmkse vatltaagke vmlvgigdki rgilyrthsd qflvafkevg rkpptfgdas
      121 vialellnsg yefdegsiif nkfrsvisyk teekpifsln tvasadsmsi yddidadvlq
      181 nyqeynlani iyyslkestt seqsarmtam dnasknasem idkltltfnr trqavitkel
      241 ieiisgaaal d
//
LOCUS       NP_060362                930 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA-processing factor 40 homolog A isoform 1 [Homo sapiens].
ACCESSION   NP_060362 XP_371575 XP_943607
VERSION     NP_060362.3
DBSOURCE    REFSEQ: accession NM_017892.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 930)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 930)
  AUTHORS   Choudhary,B. and Norris,A.
  TITLE     Conserved role for spliceosomal component PRPF40A in microexon
            splicing
  JOURNAL   RNA 31 (1), 43-50 (2024)
   PUBMED   39389624
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 930)
  AUTHORS   Martinez-Lumbreras,S., Trager,L.K., Mulorz,M.M., Payr,M.,
            Dikaya,V., Hipp,C., Konig,J. and Sattler,M.
  TITLE     Intramolecular autoinhibition regulates the selectivity of PRPF40A
            tandem WW domains for proline-rich motifs
  JOURNAL   Nat Commun 15 (1), 3888 (2024)
   PUBMED   38719828
  REMARK    GeneRIF: Intramolecular autoinhibition regulates the selectivity of
            PRPF40A tandem WW domains for proline-rich motifs.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 930)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 930)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 930)
  AUTHORS   Allen,M., Friedler,A., Schon,O. and Bycroft,M.
  TITLE     The structure of an FF domain from human HYPA/FBP11
  JOURNAL   J Mol Biol 323 (3), 411-416 (2002)
   PUBMED   12381297
  REMARK    GeneRIF: Data describe the structure of an FF domain from
            HYPA/FBP11, which differs from those of other
            phosphopeptide-binding domains and represents a novel
            phosphopeptide-binding fold.
REFERENCE   7  (residues 1 to 930)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   8  (residues 1 to 930)
  AUTHORS   Bedford,M.T., Reed,R. and Leder,P.
  TITLE     WW domain-mediated interactions reveal a spliceosome-associated
            protein that binds a third class of proline-rich motif: the proline
            glycine and methionine-rich motif
  JOURNAL   Proc Natl Acad Sci U S A 95 (18), 10602-10607 (1998)
   PUBMED   9724750
REFERENCE   9  (residues 1 to 930)
  AUTHORS   Faber,P.W., Barnes,G.T., Srinidhi,J., Chen,J., Gusella,J.F. and
            MacDonald,M.E.
  TITLE     Huntingtin interacts with a family of WW domain proteins
  JOURNAL   Hum Mol Genet 7 (9), 1463-1474 (1998)
   PUBMED   9700202
REFERENCE   10 (residues 1 to 930)
  AUTHORS   Chan,D.C., Bedford,M.T. and Leder,P.
  TITLE     Formin binding proteins bear WWP/WW domains that bind proline-rich
            peptides and functionally resemble SH3 domains
  JOURNAL   EMBO J 15 (5), 1045-1054 (1996)
   PUBMED   8605874
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079344.5 and AC012443.8.
            
            On or before Jul 25, 2007 this sequence version replaced
            XP_371575.4, XP_943607.2, NP_060362.2.
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038192.4108841.1,
                                    SRR14372080.3712854.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..930
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q23.3"
     Protein         1..930
                     /product="pre-mRNA-processing factor 40 homolog A isoform
                     1"
                     /note="formin binding protein 3; Huntingtin-interacting
                     protein A; NY-REN-6 antigen; Fas-ligand associated factor
                     1; formin-binding protein 11; huntingtin yeast partner A;
                     fas ligand-associated factor 1; pre-mRNA processing factor
                     40 homolog A; renal carcinoma antigen NY-REN-6;
                     huntingtin-interacting protein 10; PRP40 pre-mRNA
                     processing factor 40 homolog A"
                     /calculated_mol_wt=105796
     Region          110..769
                     /region_name="PRP40"
                     /note="Splicing factor [RNA processing and modification];
                     COG5104"
                     /db_xref="CDD:227435"
     CDS             1..930
                     /gene="PRPF40A"
                     /gene_synonym="FBP-11; FBP11; FLAF1; FNBP3; HIP-10; HIP10;
                     HYPA; NY-REN-6; Prp40"
                     /coded_by="NM_017892.5:376..3168"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:55660"
                     /db_xref="HGNC:HGNC:16463"
                     /db_xref="MIM:612941"
ORIGIN      
        1 mcsgsgrrrs slsptmrpgt gaergglmmg hpgmhyapmg mhpmgqranm ppvphgmmpq
       61 mmppmggppm gqmpgmmssv mpgmmmshms qasmqpalpp gvnsmdvaag tasgaksmwt
      121 ehkspdgrty yyntetkqst wekpddlktp aeqllskcpw keyksdsgkp yyynsqtkes
      181 rwakpkeled legyqntiva gslitksnlh amikaeessk qeectttsta pvptteiptt
      241 mstmaaaeaa aavvaaaaaa aaaaaaanan astsasntvs gtvpvvpepe vtsivatvvd
      301 nentvtiste eqaqltstpa iqdqsvevss ntgeetskqe tvadftpkke eeesqpakkt
      361 ytwntkeeak qafkellkek rvpsnasweq amkmiindpr ysalaklsek kqafnaykvq
      421 tekeekeear skykeakesf qrflenhekm tsttrykkae qmfgemevwn aiserdrlei
      481 yedvlfflsk kekeqakqlr krnwealkni ldnmanvtys ttwseaqqyl mdnptfaede
      541 elqnmdkeda licfeehira lekeeeeekq ksllrerrrq rknresfqif ldelhehgql
      601 hsmsswmely ptissdirft nmlgqpgsta ldlfkfyved lkaryhdekk iikdilkdkg
      661 fvvevnttfe dfvaiisstk rsttldagni klafnsllek aearererek eearkmkrke
      721 safksmlkqa appieldavw edirerfvke pafeditles erkrifkdfm hvlehecqhh
      781 hsknkkhskk skkhhrkrsr srsgsdsddd dshskkkrqr sesrsasehs ssaesersyk
      841 kskkhkkksk krrhksdspe sdaerekdkk ekdresekdr trqrseskhk spkkktgkds
      901 gnwdtsgsel segelekrrr tlleqldddq
//
LOCUS       NP_660325                157 aa            linear   PRI 21-NOV-2025
DEFINITION  solute carrier family 25 member 48 isoform 2 [Homo sapiens].
ACCESSION   NP_660325
VERSION     NP_660325.4
DBSOURCE    REFSEQ: accession NM_145282.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Patil,S., Borisov,O., Scherer,N., Wirth,C., Schlosser,P.,
            Wuttke,M., Ehret,S., Hannibal,L., Eckardt,K.U., Hunte,C.,
            Neubauer,B., Kottgen,A. and Kottgen,M.
  TITLE     The membrane transporter SLC25A48 enables transport of choline into
            human mitochondria
  JOURNAL   Kidney Int 107 (2), 296-301 (2025)
   PUBMED   39084256
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Verkerke,A.R.P., Shi,X., Li,M., Higuchi,Y., Yamamuro,T., Katoh,D.,
            Nishida,H., Auger,C., Abe,I., Gerszten,R.E. and Kajimura,S.
  TITLE     SLC25A48 controls mitochondrial choline import and metabolism
  JOURNAL   Cell Metab 36 (9), 2156-2166 (2024)
   PUBMED   39111307
  REMARK    GeneRIF: SLC25A48 controls mitochondrial choline import and
            metabolism.
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Bernard,D.J., Pangilinan,F., Mendina,C., Desporte,T.,
            Wincovitch,S.M., Walsh,D.J., Porter,R.K., Molloy,A.M., Shane,B. and
            Brody,L.C.
  TITLE     SLC25A48 influences plasma levels of choline and localizes to the
            inner mitochondrial membrane
  JOURNAL   Mol Genet Metab 143 (1-2), 108518 (2024)
   PUBMED   39047301
  REMARK    GeneRIF: SLC25A48 influences plasma levels of choline and localizes
            to the inner mitochondrial membrane.
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Khan,A., Unlu,G., Lin,P., Liu,Y., Kilic,E., Kenny,T.C., Birsoy,K.
            and Gamazon,E.R.
  TITLE     Metabolic gene function discovery platform GeneMAP identifies
            SLC25A48 as necessary for mitochondrial choline import
  JOURNAL   Nat Genet 56 (8), 1614-1623 (2024)
   PUBMED   38977856
  REMARK    GeneRIF: Metabolic gene function discovery platform GeneMAP
            identifies SLC25A48 as necessary for mitochondrial choline import.
REFERENCE   5  (residues 1 to 157)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 157)
  AUTHORS   Palmieri,F.
  TITLE     The mitochondrial transporter family SLC25: identification,
            properties and physiopathology
  JOURNAL   Mol Aspects Med 34 (2-3), 465-484 (2013)
   PUBMED   23266187
  REMARK    GeneRIF: Compares and contrasts all the known human SLC25A* genes
            and includes functional information.
            Review article
REFERENCE   7  (residues 1 to 157)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   8  (residues 1 to 157)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 157)
  AUTHORS   Hosgood,H.D. 3rd, Zhang,L., Shen,M., Berndt,S.I., Vermeulen,R.,
            Li,G., Yin,S., Yeager,M., Yuenger,J., Rothman,N., Chanock,S.,
            Smith,M. and Lan,Q.
  TITLE     Association between genetic variants in VEGF, ERCC3 and
            occupational benzene haematotoxicity
  JOURNAL   Occup Environ Med 66 (12), 848-853 (2009)
   PUBMED   19773279
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011427.4, BC025747.1 and BG700532.1.
            
            On Feb 12, 2009 this sequence version replaced NP_660325.3.
            
            Transcript Variant: This variant (2) lacks several exons and
            includes an alternate 3' terminal exon, compared to variant 1. The
            encoded isoform (2) is shorter and has a distinct C-terminus,
            compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025747.1, BI758252.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2153932
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.1"
     Protein         1..157
                     /product="solute carrier family 25 member 48 isoform 2"
                     /note="CTC-321K16.1"
                     /calculated_mol_wt=16824
     Region          3..86
                     /region_name="Solcar 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZT89.2)"
     Region          6..91
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Site            9..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZT89.2)"
     Site            61..81
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZT89.2)"
     Region          107..>142
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Site            107..127
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZT89.2)"
     CDS             1..157
                     /gene="SLC25A48"
                     /coded_by="NM_145282.5:186..659"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43366.2"
                     /db_xref="GeneID:153328"
                     /db_xref="HGNC:HGNC:30451"
                     /db_xref="MIM:616150"
ORIGIN      
        1 mgsfqledfa agwiggaasv ivghpldtvk trlqagvgyg ntlscirvvy rresmfgffk
       61 gmsfplasia vynsvvfgvf sntqrflsqh rcgepeaspp rtlsdlllas mvagvvsvgl
      121 ggpvdlikir lqmqtqpfrd ggehrmttvf pgphlcm
//
LOCUS       NP_001291366             357 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase E3D isoform 2 [Homo sapiens].
ACCESSION   NP_001291366
VERSION     NP_001291366.1
DBSOURCE    REFSEQ: accession NM_001304437.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Lin,M.H., Jensen,M.K., Elrod,N.D., Chu,H.F., Haseley,M., Beam,A.C.,
            Huang,K.L., Chiang,W., Russell,W.K., Williams,K., Proschel,C.,
            Wagner,E.J. and Tong,L.
  TITLE     Cytoplasmic binding partners of the Integrator endonuclease INTS11
            and its paralog CPSF73 are required for their nuclear function
  JOURNAL   Mol Cell 84 (15), 2900-2917 (2024)
   PUBMED   39032490
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Offenbacher,S., Divaris,K., Barros,S.P., Moss,K.L., Marchesan,J.T.,
            Morelli,T., Zhang,S., Kim,S., Sun,L., Beck,J.D., Laudes,M.,
            Munz,M., Schaefer,A.S. and North,K.E.
  TITLE     Genome-wide association study of biologically informed periodontal
            complex traits offers novel insights into the genetic basis of
            periodontal disease
  JOURNAL   Hum Mol Genet 25 (10), 2113-2129 (2016)
   PUBMED   26962152
  REMARK    GeneRIF: With the exception of associations of BEGAIN with severe
            and UBE3D with moderate chronic periodontitis (CP) , no other loci
            were associated with CP in ARIC or aggressive periodontitis in the
            German sample.
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 357)
  AUTHORS   Huang,L.Z., Li,Y.J., Xie,X.F., Zhang,J.J., Cheng,C.Y.,
            Yamashiro,K., Chen,L.J., Ma,X.Y., Cheung,C.M., Wang,Y.S.,
            Zhang,C.F., Bai,Y.J., Hou,J., Chen,X.L., Qi,Y., Li,S.S., Sun,Y.Y.,
            Mei,J.P., Cheng,Y., Yu,W.Z., Hu,X.B., Zhuang,F.F., Fan,L., Lu,Y.,
            Sun,X.H., Zhu,X.J., Shen,D.F., Chan,C.C., Zhao,M.W., Yoshimura,N.,
            Pang,C.P., Wong,T.Y., Khor,C.C., Zhang,K., Zhou,P. and Li,X.X.
  TITLE     Whole-exome sequencing implicates UBE3D in age-related macular
            degeneration in East Asian populations
  JOURNAL   Nat Commun 6, 6687 (2015)
   PUBMED   25872646
  REMARK    GeneRIF: A novel missense SNV, rs7739323, is strongly associated
            with age-related macular degeneration in an East Asian population.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 357)
  AUTHORS   Kobirumaki,F., Miyauchi,Y., Fukami,K. and Tanaka,H.
  TITLE     A novel UbcH10-binding protein facilitates the ubiquitinylation of
            cyclin B in vitro
  JOURNAL   J Biochem 137 (2), 133-139 (2005)
   PUBMED   15749827
  REMARK    GeneRIF: The carboxyl terminal half of H10BH was able to bind
            cyclin B and ubiquitinylate cyclin B in vitro.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC057845.1, BC036049.1, BC071763.1 and AL034377.1.
            
            Transcript Variant: This variant (2) has an alternate splice site
            in the 5' region, which results in translation initiation at a
            downstream AUG start codon, compared to variant 1. The resulting
            isoform (2) is shorter at the N-terminus, compared to isoform 1.
            Variants 2 and 3 both encode the same isoform (2).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC057845.1, SRR14038195.1838941.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..357
                     /product="E3 ubiquitin-protein ligase E3D isoform 2"
                     /EC_number="2.3.2.26"
                     /note="UBCH10 binding protein with a hect-like domain;
                     ubiquitin-conjugating enzyme E2C-binding protein; E3
                     ubiquitin-protein ligase E3D; ubcH10-binding protein with
                     a HECT-like domain; HECT-type E3 ubiquitin transferase
                     E3D"
                     /calculated_mol_wt=40201
     Region          2..352
                     /region_name="HECT_2"
                     /note="HECT-like Ubiquitin-conjugating enzyme
                     (E2)-binding; pfam09814"
                     /db_xref="CDD:462911"
     CDS             1..357
                     /gene="UBE3D"
                     /gene_synonym="C6orf157; H10BH; UBE2CBP; YJR141W"
                     /coded_by="NM_001304437.2:182..1255"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:90025"
                     /db_xref="HGNC:HGNC:21381"
                     /db_xref="MIM:612495"
ORIGIN      
        1 mpmnisimps slqmktpegc teiqlpaevr lvpsscrglq fvvgdglhlr lqtqaklgtk
       61 lismfnqssq tqecctfycq scgeviikdr kllrvlplps enwgalvgew cchpdpfank
      121 slhpqendcf igdsfflvnl rtslwqqrpe lspvemccvs sdnhcklepk antkvickrc
      181 kvmlgetvss ettkfymtei iiqssersfp iiprswfvqs viaqclvqls sarstfrfti
      241 qgqddkvyil lwllnsdslv ieslrnskyi kkfpllentf kadsssawsa vkvlyqpcik
      301 srneklvslw esdisvhplt lpsatclell lilsksnanl psslrrvnsf qvaflkm
//
LOCUS       NP_001351057             913 aa            linear   PRI 21-NOV-2025
DEFINITION  catenin delta-2 isoform 6 [Homo sapiens].
ACCESSION   NP_001351057 XP_016864565
VERSION     NP_001351057.1
DBSOURCE    REFSEQ: accession NM_001364128.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Assendorp,N., Fossati,M., Libe-Philippot,B., Christopoulou,E.,
            Depp,M., Rapone,R., Dingli,F., Loew,D., Vanderhaeghen,P. and
            Charrier,C.
  TITLE     CTNND2 moderates the pace of synaptic maturation and links human
            evolution to synaptic neoteny
  JOURNAL   Cell Rep 43 (10), 114797 (2024)
   PUBMED   39352808
  REMARK    GeneRIF: CTNND2 moderates the pace of synaptic maturation and links
            human evolution to synaptic neoteny.
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Pauly,M., Krumbiegel,M., Trumpp,S., Braig,S., Rupprecht,T.,
            Kraus,C., Uebe,S., Reis,A. and Vasileiou,G.
  TITLE     Severe manifestation of Rauch-Azzarello syndrome associated with
            biallelic deletion of CTNND2
  JOURNAL   Clin Genet 106 (2), 180-186 (2024)
   PUBMED   38604781
  REMARK    GeneRIF: Severe manifestation of Rauch-Azzarello syndrome
            associated with biallelic deletion of CTNND2.
REFERENCE   4  (residues 1 to 913)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 913)
  AUTHORS   Li,M., Nopparat,J., Aguilar,B.J., Chen,Y.H., Zhang,J., Du,J.,
            Ai,X., Luo,Y., Jiang,Y., Boykin,C. and Lu,Q.
  TITLE     Intratumor delta-catenin heterogeneity driven by genomic
            rearrangement dictates growth factor dependent prostate cancer
            progression
  JOURNAL   Oncogene 39 (22), 4358-4374 (2020)
   PUBMED   32313227
  REMARK    GeneRIF: Intratumor delta-catenin heterogeneity driven by genomic
            rearrangement dictates growth factor dependent prostate cancer
            progression.
REFERENCE   6  (residues 1 to 913)
  AUTHORS   Lu,Q., Paredes,M., Medina,M., Zhou,J., Cavallo,R., Peifer,M.,
            Orecchio,L. and Kosik,K.S.
  TITLE     delta-catenin, an adhesive junction-associated protein which
            promotes cell scattering
  JOURNAL   J Cell Biol 144 (3), 519-532 (1999)
   PUBMED   9971746
REFERENCE   7  (residues 1 to 913)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   8  (residues 1 to 913)
  AUTHORS   Paffenholz,R. and Franke,W.W.
  TITLE     Identification and localization of a neurally expressed member of
            the plakoglobin/armadillo multigene family
  JOURNAL   Differentiation 61 (5), 293-304 (1997)
   PUBMED   9342840
REFERENCE   9  (residues 1 to 913)
  AUTHORS   Zhou,J., Liyanage,U., Medina,M., Ho,C., Simmons,A.D., Lovett,M. and
            Kosik,K.S.
  TITLE     Presenilin 1 interaction in the brain with a novel member of the
            Armadillo family
  JOURNAL   Neuroreport 8 (8), 2085-2090 (1997)
   PUBMED   9223106
REFERENCE   10 (residues 1 to 913)
  AUTHORS   Simmons,A.D., Overhauser,J. and Lovett,M.
  TITLE     Isolation of cDNAs from the Cri-du-chat critical region by direct
            screening of a chromosome 5-specific cDNA library
  JOURNAL   Genome Res 7 (2), 118-127 (1997)
   PUBMED   9049630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010433.9, AC003954.1,
            AC005367.1, AC004648.1, AC005610.1 and AC010626.6.
            
            On Jun 7, 2018 this sequence version replaced XP_016864565.1.
            
            Summary: This gene encodes an adhesive junction associated protein
            of the armadillo/beta-catenin superfamily and is implicated in
            brain and eye development and cancer formation. The protein encoded
            by this gene promotes the disruption of E-cadherin based adherens
            junction to favor cell spreading upon stimulation by hepatocyte
            growth factor. This gene is overexpressed in prostate
            adenocarcinomas and is associated with decreased expression of
            tumor suppressor E-cadherin in this tissue. This gene resides in a
            region of the short arm of chromosome 5 that is deleted in Cri du
            Chat syndrome. Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Dec
            2013].
            
            Transcript Variant: This variant (6) differs in the 5' UTR and
            coding sequence, lacks two alternate exons, and contains another
            alternate in-frame exon compared to variant 1. The resulting
            isoform (6) is shorter at the N-terminus, lacks an alternate
            internal segment, and contains another alternate segment compared
            to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.168784.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.2"
     Protein         1..913
                     /product="catenin delta-2 isoform 6"
                     /note="catenin (cadherin-associated protein), delta 2
                     (neural plakophilin-related arm-repeat protein); T-cell
                     delta-catenin; neurojungin"
                     /calculated_mol_wt=100434
     Region          213..>386
                     /region_name="PLN03200"
                     /note="cellulose synthase-interactive protein;
                     Provisional"
                     /db_xref="CDD:215629"
     Region          215..240
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(231,235,239,273,277,281,318,322,326)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          244..284
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          248..284
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          288..329
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          292..327
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          334..385
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          497..538
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          501..538
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          573..608
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          573..607
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          614..660
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          662..706
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          666..701
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     CDS             1..913
                     /gene="CTNND2"
                     /gene_synonym="GT24; NPRAP"
                     /coded_by="NM_001364128.2:432..3173"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS93685.1"
                     /db_xref="GeneID:1501"
                     /db_xref="HGNC:HGNC:2516"
                     /db_xref="MIM:604275"
ORIGIN      
        1 mssmssaeeq fqwqsqdgqk diedelttgl elvdscirsl qesgildpqd ystgetgsra
       61 syssqhghlg pelralqspe hhidpiyedr vyqkppmrsl sqsqgdplpp ahtgtyrtst
      121 apsspgvdsv plqrtgsqhg pqnaaaatfq rasyaagpas nyadpyrqlq ycpsvespys
      181 ksgpalppeg tlarspsids iqkdprefgw rdpelpeviq mlqhqfpsvq snaaaylqhl
      241 cfgdnkikae irrqggiqll vdlldhrmte vhrsacgalr nlvygkandd nkialkncgg
      301 ipalvrllrk ttdleirelv tgvlwnlssc dalkmpiiqd alavltnavi iphsgwensp
      361 lqddrkiqlh ssqvlrnatg clrnvssage earrrmrecd gltdallyvi qsalgsseid
      421 sktvencvci lrnlsyrlaa etsqgqhmgt deldgllcge angkdaessg cwgkkkkkkk
      481 sqdqwdgvgp lpdcaeppkg iqmlwhpsiv kpyltllsec snpdtlegaa galqnlaags
      541 wkgwaedvag mayalrslpe gapclpqwsv yiraavrkek glpilvellr idndrvvcav
      601 atalrnmald vrnkeligky amrdlvhrlp ggnnsnntas kamsddtvta vcctlhevit
      661 knmenakalr daggieklvg iskskgdkhs pkvvkaasqv lnsmwqyrdl rslykkdgws
      721 qyhfvassst ierdrqrpys ssrtpsispv rvspnnrsas apaspremis lkerktdyec
      781 tgsnatyhga kgehtsrkda mtaqntgist lyrnsygapa edikhnqvsa qpvpqepsrk
      841 dyetyqpfqn strnydesff edqvhhrppa seytmhlglk stgnyvdfys aarpyselny
      901 etshypaspd swv
//
LOCUS       NP_001230007             101 aa            linear   PRI 21-NOV-2025
DEFINITION  T-cell-specific surface glycoprotein CD28 isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_001230007
VERSION     NP_001230007.1
DBSOURCE    REFSEQ: accession NM_001243078.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Xiong,Y., Taleb,M., Misawa,K., Hou,Z., Banerjee,S.,
            Amador-Molina,A., Jones,D.R., Chintala,N.K. and Adusumilli,P.S.
  TITLE     c-Kit signaling potentiates CAR T cell efficacy in solid tumors by
            CD28- and IL-2-independent co-stimulation
  JOURNAL   Nat Cancer 4 (7), 1001-1015 (2023)
   PUBMED   37336986
  REMARK    GeneRIF: c-Kit signaling potentiates CAR T cell efficacy in solid
            tumors by CD28- and IL-2-independent co-stimulation.
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Pulanco,M.C., Madsen,A.T., Tanwar,A., Corrigan,D.T. and Zang,X.
  TITLE     Recent advancements in the B7/CD28 immune checkpoint families: new
            biology and clinical therapeutic strategies
  JOURNAL   Cell Mol Immunol 20 (7), 694-713 (2023)
   PUBMED   37069229
  REMARK    GeneRIF: Recent advancements in the B7/CD28 immune checkpoint
            families: new biology and clinical therapeutic strategies.
            Review article
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Mai,H.L., Degauque,N., Lorent,M., Rimbert,M., Renaudin,K.,
            Danger,R., Kerleau,C., Tilly,G., Vivet,A., Le Bot,S., Delbos,F.,
            Walencik,A., Giral,M. and Brouard,S.
  TITLE     Kidney allograft rejection is associated with an imbalance of B
            cells, regulatory T cells and differentiated CD28-CD8+ T cells:
            analysis of a cohort of 1095 graft biopsies
  JOURNAL   Front Immunol 14, 1151127 (2023)
   PUBMED   37168864
  REMARK    GeneRIF: Kidney allograft rejection is associated with an imbalance
            of B cells, regulatory T cells and differentiated CD28-CD8+ T
            cells: analysis of a cohort of 1095 graft biopsies.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Gelemanovic,A., Catipovic Ardalic,T., Pribisalic,A., Hayward,C.,
            Kolcic,I. and Polasek,O.
  TITLE     Genome-Wide Meta-Analysis Identifies Multiple Novel Rare Variants
            to Predict Common Human Infectious Diseases Risk
  JOURNAL   Int J Mol Sci 24 (8), 7006 (2023)
   PUBMED   37108169
  REMARK    GeneRIF: Genome-Wide Meta-Analysis Identifies Multiple Novel Rare
            Variants to Predict Common Human Infectious Diseases Risk.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 101)
  AUTHORS   Liu,T.H., Lei,J.Y., Mai,Y.G. and Fang,J.P.
  TITLE     [Clinical Analysis of Pediatric Acute Leukemia Complicated with
            Septic Shock]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 30 (6), 1708-1714 (2022)
   PUBMED   36476893
  REMARK    GeneRIF: [Clinical Analysis of Pediatric Acute Leukemia Complicated
            with Septic Shock].
REFERENCE   6  (residues 1 to 101)
  AUTHORS   Fraser,J.D., Newton,M.E. and Weiss,A.
  TITLE     CD28 and T cell antigen receptor signal transduction coordinately
            regulate interleukin 2 gene expression in response to superantigen
            stimulation
  JOURNAL   J Exp Med 175 (4), 1131-1134 (1992)
   PUBMED   1313075
REFERENCE   7  (residues 1 to 101)
  AUTHORS   Zocchi,M.R., Poggi,A., Crosti,F., Tongiani,S. and Rugarli,C.
  TITLE     Signalling in human tumour infiltrating lymphocytes: the CD28
            molecule is functional and is physically associated with the CD45R0
            molecule
  JOURNAL   Eur J Cancer 28A (4-5), 749-754 (1992)
   PUBMED   1355979
REFERENCE   8  (residues 1 to 101)
  AUTHORS   Gimmi,C.D., Freeman,G.J., Gribben,J.G., Sugita,K., Freedman,A.S.,
            Morimoto,C. and Nadler,L.M.
  TITLE     B-cell surface antigen B7 provides a costimulatory signal that
            induces T cells to proliferate and secrete interleukin 2
  JOURNAL   Proc Natl Acad Sci U S A 88 (15), 6575-6579 (1991)
   PUBMED   1650475
REFERENCE   9  (residues 1 to 101)
  AUTHORS   Linsley,P.S., Brady,W., Grosmaire,L., Aruffo,A., Damle,N.K. and
            Ledbetter,J.A.
  TITLE     Binding of the B cell activation antigen B7 to CD28 costimulates T
            cell proliferation and interleukin 2 mRNA accumulation
  JOURNAL   J Exp Med 173 (3), 721-730 (1991)
   PUBMED   1847722
REFERENCE   10 (residues 1 to 101)
  AUTHORS   Lafage-Pochitaloff,M., Costello,R., Couez,D., Simonetti,J.,
            Mannoni,P., Mawas,C. and Olive,D.
  TITLE     Human CD28 and CTLA-4 Ig superfamily genes are located on
            chromosome 2 at bands q33-q34
  JOURNAL   Immunogenetics 31 (3), 198-201 (1990)
   PUBMED   2156778
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC125238.5, AF222342.1,
            AK303421.1, J02988.1, DA939711.1, AW241446.1, AA311148.1 and
            BF509568.1.
            
            Summary: The protein encoded by this gene is essential for T-cell
            proliferation and survival, cytokine production, and T-helper
            type-2 development. Several alternatively spliced transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, Jul 2011].
            
            Transcript Variant: This variant (3) lacks an in-frame coding exon
            compared to variant 1. This results in a shorter isoform (3)
            missing an internal protein segment compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2812506.1,
                                           SRR14038195.1252044.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465410 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..101
                     /product="T-cell-specific surface glycoprotein CD28
                     isoform 3 precursor"
                     /calculated_mol_wt=11397
     mat_peptide     19..101
                     /product="T-cell-specific surface glycoprotein CD28
                     isoform 3"
                     /calculated_mol_wt=9546
     CDS             1..101
                     /gene="CD28"
                     /gene_synonym="IMD123; Tp44"
                     /coded_by="NM_001243078.2:59..364"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS58749.1"
                     /db_xref="GeneID:940"
                     /db_xref="HGNC:HGNC:1653"
                     /db_xref="MIM:186760"
ORIGIN      
        1 mlrlllalnl fpsiqvtgkh lcpsplfpgp skpfwvlvvv ggvlacysll vtvafiifwv
       61 rskrsrllhs dymnmtprrp gptrkhyqpy apprdfaayr s
//
LOCUS       NP_001371523             692 aa            linear   PRI 21-NOV-2025
DEFINITION  protein Smaug homolog 2 isoform c [Homo sapiens].
ACCESSION   NP_001371523
VERSION     NP_001371523.1
DBSOURCE    REFSEQ: accession NM_001384594.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 692)
  AUTHORS   Wu,C., Liu,X., Li,B., Sun,G., Peng,C. and Xiang,D.
  TITLE     miR-451 suppresses the malignant characteristics of colorectal
            cancer via targeting SAMD4B
  JOURNAL   Mol Med Rep 24 (2) (2021)
   PUBMED   34109425
  REMARK    GeneRIF: miR451 suppresses the malignant characteristics of
            colorectal cancer via targeting SAMD4B.
REFERENCE   6  (residues 1 to 692)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   7  (residues 1 to 692)
  AUTHORS   Baez,M.V. and Boccaccio,G.L.
  TITLE     Mammalian Smaug is a translational repressor that forms cytoplasmic
            foci similar to stress granules
  JOURNAL   J Biol Chem 280 (52), 43131-43140 (2005)
   PUBMED   16221671
REFERENCE   8  (residues 1 to 692)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   9  (residues 1 to 692)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 692)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011445.6 and AC005239.1.
            
            Transcript Variant: This variant (29) differs in the 5' UTR
            compared to variant 20. Variants 20-29 all encode the same isoform
            (c).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038195.2199635.1, SRR1660805.50936.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..692
                     /product="protein Smaug homolog 2 isoform c"
                     /note="smaug homolog B; protein Smaug homolog 2; smaug 2;
                     SAM domain-containing protein 4B; sterile alpha motif
                     domain-containing protein 4B"
                     /calculated_mol_wt=75262
     Region          158..301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XS6; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XS6; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XS6; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Region          296..358
                     /region_name="SAM_Smaug"
                     /note="SAM domain of Smaug subfamily; cd09557"
                     /db_xref="CDD:188956"
     Site            order(312,314..315,343,346..348,355,357)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:188956"
     Region          407..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            555
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            592
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            600
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            602
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Region          607..643
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     CDS             1..692
                     /gene="SAMD4B"
                     /gene_synonym="Smaug2; SMGB"
                     /coded_by="NM_001384594.1:598..2676"
                     /note="isoform c is encoded by transcript variant 29"
                     /db_xref="GeneID:55095"
                     /db_xref="HGNC:HGNC:25492"
                     /db_xref="MIM:619231"
ORIGIN      
        1 mmfrdqvgil agwfkgwnec eqtvallsll krvtrtqarf lqlclehsla dcndihlles
       61 eansaaivsq wqqeskekvv slllshlpll qpgnteakse ymrllqkvla ysiesnafie
      121 esrqllsyal ihpattledr nalalwlshl eerlasgfrs rpepsyhsrq gsdewggpae
      181 lgpgeagpgw qdkpprengh vpfhpsssvp painsigsna ntglpcqihp splkrsmsli
      241 ptspqvpgew pspeelgara afttpdhapl spqssvassg seqteeqgss rntfqedgsg
      301 mkdvpswlks lrlhkyaalf sqmsyeemmt lteqhlesqn vtkgarhkia lsiqklrerq
      361 svlkslekdv leggnlrnal qelqqiiitp ikaysvlqat vaaatttpta kdgapgeppl
      421 pgaepplahp gtdkgteakd ppavenyppp papaptdgse papapvadgd ipsqftrvmg
      481 kvctqllvsr pdeenitsyl qliekclthe aftetqkkrl lswkqqvlkl lrtfprkaal
      541 emqnyrqqkg wafgsnslpi agsvgmgvar rtqrqfpmpp ralppgrmgl lspsgiggvs
      601 prhaltspsl ggqgrqnlwf anpggsnsmp sqsrssvqrt hslpvhsspq ailmfppdcp
      661 vpgpdleinp tleslclsmt ehalggehfl fp
//
LOCUS       NP_001338788             810 aa            linear   PRI 21-NOV-2025
DEFINITION  liprin-beta-2 isoform 10 [Homo sapiens].
ACCESSION   NP_001338788 XP_016873933
VERSION     NP_001338788.2
DBSOURCE    REFSEQ: accession NM_001351859.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Wu,Y., Yu,H., Zheng,S.L., Feng,B., Kapron,A.L., Na,R., Boyle,J.L.,
            Shah,S., Shi,Z., Ewing,C.M., Wiley,K.E., Luo,J., Walsh,P.C.,
            Carter,H.B., Helfand,B.T., Cooney,K.A., Xu,J. and Isaacs,W.B.
  TITLE     Germline mutations in PPFIBP2 are associated with lethal prostate
            cancer
  JOURNAL   Prostate 78 (16), 1222-1228 (2018)
   PUBMED   30043417
  REMARK    GeneRIF: germline mutations in a novel gene, PPFIBP2,
            differentiated risk for lethal prostate cancer from low-risk cases
            and were associated with shorter survival times after diagnosis.
REFERENCE   6  (residues 1 to 810)
  AUTHORS   von Thun,A., Birtwistle,M., Kalna,G., Grindlay,J., Strachan,D.,
            Kolch,W., von Kriegsheim,A. and Norman,J.C.
  TITLE     ERK2 drives tumour cell migration in three-dimensional
            microenvironments by suppressing expression of Rab17 and
            liprin-beta2
  JOURNAL   J Cell Sci 125 (Pt 6), 1465-1477 (2012)
   PUBMED   22328529
  REMARK    GeneRIF: Knockdown of either Rab17 or liprin-beta2 restores
            invasiveness of ERK2-depleted cells, indicating that ERK2 drives
            invasion of MDA-MB-231 cells by suppressing expression of these
            genes.
REFERENCE   7  (residues 1 to 810)
  AUTHORS   Colas,E., Perez,C., Cabrera,S., Pedrola,N., Monge,M., Castellvi,J.,
            Eyzaguirre,F., Gregorio,J., Ruiz,A., Llaurado,M., Rigau,M.,
            Garcia,M., Ertekin,T., Montes,M., Lopez-Lopez,R., Carreras,R.,
            Xercavins,J., Ortega,A., Maes,T., Rosell,E., Doll,A., Abal,M.,
            Reventos,J. and Gil-Moreno,A.
  TITLE     Molecular markers of endometrial carcinoma detected in uterine
            aspirates
  JOURNAL   Int J Cancer 129 (10), 2435-2444 (2011)
   PUBMED   21207424
  REMARK    Erratum:[Int J Cancer. 2012 Jun 15;130(12):E4]
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Stafford,R.L., Tang,M.Y., Sawaya,M.R., Phillips,M.L. and Bowie,J.U.
  TITLE     Crystal structure of the central coiled-coil domain from human
            liprin-beta2
  JOURNAL   Biochemistry 50 (18), 3807-3815 (2011)
   PUBMED   21462929
  REMARK    GeneRIF: analysis of crystal structure of the central coiled-coil
            domain from human liprin-beta2
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Serra-Pages,C., Medley,Q.G., Tang,M., Hart,A. and Streuli,M.
  TITLE     Liprins, a family of LAR transmembrane protein-tyrosine
            phosphatase-interacting proteins
  JOURNAL   J Biol Chem 273 (25), 15611-15620 (1998)
   PUBMED   9624153
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107884.15 and AC104237.2.
            
            On May 21, 2020 this sequence version replaced NP_001338788.1.
            
            Summary: This gene encodes a member of the LAR protein-tyrosine
            phosphatase-interacting protein (liprin) family. The encoded
            protein is a beta liprin and plays a role in axon guidance and
            neuronal synapse development by recruiting LAR protein-tyrosine
            phosphatases to the plasma membrane. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene. [provided by RefSeq, Feb 2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.144974.1,
                                           SRR1803615.102866.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..810
                     /product="liprin-beta-2 isoform 10"
                     /note="protein tyrosine phosphatase receptor type f
                     polypeptide-interacting protein-binding protein 2; PTPRF
                     interacting protein, binding protein 2 (liprin beta 2);
                     PPFIA binding protein 2"
                     /calculated_mol_wt=91520
     Region          <14..>240
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          489..552
                     /region_name="SAM_liprin-beta1,2_repeat1"
                     /note="SAM domain of liprin-beta1,2 proteins repeat 1;
                     cd09563"
                     /db_xref="CDD:188962"
     Region          563..625
                     /region_name="SAM_liprin-beta1,2_repeat2"
                     /note="SAM domain of liprin-beta1,2 proteins repeat 2;
                     cd09566"
                     /db_xref="CDD:188965"
     Region          648..719
                     /region_name="SAM_liprin-beta1,2_repeat3"
                     /note="SAM domain of liprin-beta proteins repeat 3;
                     cd09569"
                     /db_xref="CDD:188968"
     CDS             1..810
                     /gene="PPFIBP2"
                     /gene_synonym="Cclp1"
                     /coded_by="NM_001351859.2:552..2984"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS91429.1"
                     /db_xref="GeneID:8495"
                     /db_xref="HGNC:HGNC:9250"
                     /db_xref="MIM:603142"
ORIGIN      
        1 mdgdidvykh fswlkrsqvn hhsaasnety qerlarlegd keslilqvsv ltdqveaqge
       61 kirdlevcle ghqvklnaae emlqqellsr tsletqkldl mtevselklk lvgmekeqre
      121 qeekqrkaee llqelrhlki kveelenern qyewklkatk aevaqlqeqv alkdaeierl
      181 hsqlsrtaal hseshterdq eiqrlkmgme tlllanedkd rrieeltgll nqyrkvkeiv
      241 mvtqgpsert lsineeepeg gfskwnatnk dpeelfkqem pprcssptvg ppplpqksle
      301 traqkklscs ledlrsesvd kcmdgnqpfp vlepkdspfl aehkyptlpg klsgatpnge
      361 aaksppticq pdatgssllr lnrgrsvsap vlgdtesgwd dtavvndlss tssgtesgpq
      421 spltpdgkrn pkgikkfwgk irrtqsgnfy tdtlgmaefr rgglratagp rlsrtrdskg
      481 qksdanapfa qwstervcaw ledfglaqyv ifarqwvssg htlltatpqd mekelgikhp
      541 lhrkklvlav kaintkqeek salldhiwvt rwlddiglpq ykdqfhesrv drrmlqyltv
      601 ndllflkvts qlhhlsikca ihvlhvnkfn phclhrrpad esnlspsevv qwsnhrvmew
      661 lrsvdlaeya pnlrgsgvhg gliileprft gdtlamllni ppqktllrrh lttkfnalig
      721 peaeqekrek maspaytplt ttakvrprkl gfshfgnirk kkfdestdyi cpmepsdgvs
      781 dshrvysgyr glspldapel dgldqvgqis
//
LOCUS       NP_001381084            1447 aa            linear   PRI 21-NOV-2025
DEFINITION  regulator of G-protein signaling 12 isoform 1 [Homo sapiens].
ACCESSION   NP_001381084
VERSION     NP_001381084.1
DBSOURCE    REFSEQ: accession NM_001394155.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1447)
  AUTHORS   Sneddon,W.B., Ramineni,S., Van Doorn,G.E., Hepler,J.R. and
            Friedman,P.A.
  TITLE     Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport
  JOURNAL   Biochem Biophys Res Commun 733, 150700 (2024)
   PUBMED   39293332
  REMARK    GeneRIF: Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport.
REFERENCE   2  (residues 1 to 1447)
  AUTHORS   Yuan,G., Yang,S. and Yang,S.
  TITLE     RGS12 represses oral squamous cell carcinoma by driving M1
            polarization of tumor-associated macrophages via controlling
            ciliary MYCBP2/KIF2A signaling
  JOURNAL   Int J Oral Sci 15 (1), 11 (2023)
   PUBMED   36797232
  REMARK    GeneRIF: RGS12 represses oral squamous cell carcinoma by driving M1
            polarization of tumor-associated macrophages via controlling
            ciliary MYCBP2/KIF2A signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1447)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1447)
  AUTHORS   Yuan,G., Fu,C., Yang,S.T., Yuh,D.Y., Hajishengallis,G. and Yang,S.
  TITLE     RGS12 Drives Macrophage Activation and Osteoclastogenesis in
            Periodontitis
  JOURNAL   J Dent Res 101 (4), 448-457 (2022)
   PUBMED   34796776
  REMARK    GeneRIF: RGS12 Drives Macrophage Activation and Osteoclastogenesis
            in Periodontitis.
REFERENCE   5  (residues 1 to 1447)
  AUTHORS   Yuan,G., Huang,Y., Yang,S.T., Ng,A. and Yang,S.
  TITLE     RGS12 inhibits the progression and metastasis of multiple myeloma
            by driving M1 macrophage polarization and activation in the bone
            marrow microenvironment
  JOURNAL   Cancer Commun (Lond) 42 (1), 60-64 (2022)
   PUBMED   34931491
  REMARK    GeneRIF: RGS12 inhibits the progression and metastasis of multiple
            myeloma by driving M1 macrophage polarization and activation in the
            bone marrow microenvironment.
REFERENCE   6  (residues 1 to 1447)
  AUTHORS   Schiff,M.L., Siderovski,D.P., Jordan,J.D., Brothers,G., Snow,B., De
            Vries,L., Ortiz,D.F. and Diverse-Pierluissi,M.
  TITLE     Tyrosine-kinase-dependent recruitment of RGS12 to the N-type
            calcium channel
  JOURNAL   Nature 408 (6813), 723-727 (2000)
   PUBMED   11130074
REFERENCE   7  (residues 1 to 1447)
  AUTHORS   Chatterjee,T.K. and Fisher,R.A.
  TITLE     Novel alternative splicing and nuclear localization of human RGS12
            gene products
  JOURNAL   J Biol Chem 275 (38), 29660-29671 (2000)
   PUBMED   10869340
REFERENCE   8  (residues 1 to 1447)
  AUTHORS   Frohme,M., Scharm,B., Delius,H., Knecht,R. and Hoheisel,J.D.
  TITLE     Use of representational difference analysis and cDNA arrays for
            transcriptional profiling of tumor tissue
  JOURNAL   Ann N Y Acad Sci 910, 85-104 (2000)
   PUBMED   10911908
  REMARK    Review article
REFERENCE   9  (residues 1 to 1447)
  AUTHORS   Snow,B.E., Hall,R.A., Krumins,A.M., Brothers,G.M., Bouchard,D.,
            Brothers,C.A., Chung,S., Mangion,J., Gilman,A.G., Lefkowitz,R.J.
            and Siderovski,D.P.
  TITLE     GTPase activating specificity of RGS12 and binding specificity of
            an alternatively spliced PDZ (PSD-95/Dlg/ZO-1) domain
  JOURNAL   J Biol Chem 273 (28), 17749-17755 (1998)
   PUBMED   9651375
REFERENCE   10 (residues 1 to 1447)
  AUTHORS   Snow,B.E., Antonio,L., Suggs,S., Gutstein,H.B. and Siderovski,D.P.
  TITLE     Molecular cloning and expression analysis of rat Rgs12 and Rgs14
  JOURNAL   Biochem Biophys Res Commun 233 (3), 770-777 (1997)
   PUBMED   9168931
  REMARK    GeneRIF: shows chromosomal mapping information for human locus.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645949.16 and AL590235.23.
            
            Summary: This gene encodes a member of the 'regulator of G protein
            signaling' (RGS) gene family. The encoded protein may function as a
            guanosine triphosphatase (GTPase)-activating protein as well as a
            transcriptional repressor. This protein may play a role in
            tumorigenesis. Multiple transcript variants encoding distinct
            isoforms have been identified for this gene. Other alternative
            splice variants have been described but their biological nature has
            not been determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038191.543146.1, SRR14038197.1027984.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMN03465403 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1447
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..1447
                     /product="regulator of G-protein signaling 12 isoform 1"
                     /note="regulator of G-protein signalling 12"
                     /calculated_mol_wt=156227
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14924.1)"
     Region          21..96
                     /region_name="PDZ_RGS12-like"
                     /note="PDZ domain of regulator of G-protein signaling 12
                     (RGS12), and related domains; cd06710"
                     /db_xref="CDD:467194"
     Site            order(31..37,45,48,77,81,84..85)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467194"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGE9; propagated from
                     UniProtKB/Swiss-Prot (O14924.1)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGE9; propagated from
                     UniProtKB/Swiss-Prot (O14924.1)"
     Region          228..359
                     /region_name="PTB_RGS12"
                     /note="Regulator of G-protein signaling 12
                     Phosphotyrosine-binding (PTB) PH-like fold; cd13162"
                     /db_xref="CDD:269984"
     Site            order(233,310,341)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269984"
     Site            order(299..304,317,352,356)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269984"
     Region          410..429
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14924.1)"
     Region          443..482
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14924.1)"
     Site            524
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (O14924.1)"
     Region          618..652
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14924.1)"
     Site            633
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGE9; propagated from
                     UniProtKB/Swiss-Prot (O14924.1)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGE9; propagated from
                     UniProtKB/Swiss-Prot (O14924.1)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGE9; propagated from
                     UniProtKB/Swiss-Prot (O14924.1)"
     Region          716..830
                     /region_name="RGS_RGS12"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the RGS12 protein; cd08742"
                     /db_xref="CDD:188696"
     Site            order(736..738,740..741,778..783,785..786,813,815..817,
                     821)
                     /site_type="other"
                     /note="G-alpha-3 interaction site [polypeptide binding]"
                     /db_xref="CDD:188696"
     Region          836..951
                     /region_name="RGS12_us1"
                     /note="Unstructured region of RGS12; pfam16613"
                     /db_xref="CDD:465199"
     Region          843..941
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14924.1)"
     Site            850
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGE9; propagated from
                     UniProtKB/Swiss-Prot (O14924.1)"
     Site            879
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGE9; propagated from
                     UniProtKB/Swiss-Prot (O14924.1)"
     Site            943
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGE9; propagated from
                     UniProtKB/Swiss-Prot (O14924.1)"
     Region          962..1031
                     /region_name="RBD1_RGS12"
                     /note="Ras-binding domain (RBD) 1 of regulator of G
                     protein signaling 12 (RGS12); cd17136"
                     /db_xref="CDD:340656"
     Site            order(967,988,990,1011)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340656"
     Region          1032..1104
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     Region          1103..1169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14924.1)"
     Region          1106..1180
                     /region_name="RGS12_us2"
                     /note="Unstructured region between RBD and GoLoco;
                     pfam16611"
                     /db_xref="CDD:435461"
     Region          1188..1209
                     /region_name="GoLoco"
                     /note="LGN motif, putative GEFs specific for G-alpha
                     GTPases; smart00390"
                     /db_xref="CDD:214645"
     Region          1239..1376
                     /region_name="RGS12_usC"
                     /note="C-terminal unstructured region of RGS12; pfam16612"
                     /db_xref="CDD:465198"
     Region          1240..1447
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14924.1)"
     CDS             1..1447
                     /gene="RGS12"
                     /coded_by="NM_001394155.1:287..4630"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS3366.1"
                     /db_xref="GeneID:6002"
                     /db_xref="HGNC:HGNC:9994"
                     /db_xref="MIM:602512"
ORIGIN      
        1 mfrageaskr plpgpspprv rsvevargra gygftlsgqa pcvlscvmrg spadfvglra
       61 gdqilavnei nvkkashedv vkligkcsgv lhmviaegvg rfescssdee gglyegkgwl
      121 kpkldskalg inraervvee mqsggifnmi fenpslcasn seplklkqrs lsesaatrfd
      181 vghesinnpn pnmlskeeis kvihddsvfs igleshddfa ldasilnvam ivgylgsiel
      241 pstssnlesd slqairgcmr rlraeqkihs lvtmkimhdc vqlstdkagv vaeypaekla
      301 fsavcpddrr ffglvtmqtn ddgslaqeee galrtschvf mvdpdlfnhk ihqgiarrfg
      361 fectadpdtn gclefpassl pvlqfisvly rdmgeliegm rarafldgda dahqnnstss
      421 nsdsgignfh qeeksnrvlv vdlggsssrh gpggsawdgv ggrgaqpwga pwtgpfcpdp
      481 egsppfeaah qtdrfwdlnk hlgpaspvev ppaslrssvp pskrgtvgag cgfnqrwlpv
      541 hvlrewqcgh tsdqdsytds tdgwssincg tlpppmskip adryrvegsf aqpplnapkr
      601 ewsrkafgmq sifgphrnvr ktkedkkgsk fgrgtgltqp sqrtsarrsf grskrfsitr
      661 slddlesatv sdgeltgadl kdcvsnnsls snaslpsvqs crrlrerrva swavsferll
      721 qdpvgvryfs dflrkefsee nilfwqacey fnhvpahdkk elsyrareif skflcskatt
      781 pvnidsqaql addvlraphp dmfkeqqlqi fnlmkfdsyt rflksplyqe cilaevegra
      841 lpdsqqvpss paskhslgsd hssvstpkkl sgksksgrsl neelgdedse kkrkgaffsw
      901 srtrstgrsq kkrehgdhad dalhangglc rresqgsvss agsldlseac rtlapekdka
      961 tkhccihlpd gtscvvavka gfsikdilsg lcerhginga aadlflvggd kplvlhqdss
     1021 ilesrdlrle krtlfrldlv pinrsvglka kptkpvtevl rpvvarygld lsgllvrlsg
     1081 ekepldlgap issldgqrvv leekdpsrgk asadkqkgvp vkqntavnss srnhsatgee
     1141 rtlgksnsik ikgengknar dprlskrees iakigkkkyq kinldeaeef feliskaqsn
     1201 raddqrgllr kedlvlpefl rlppgstelt lptpaavakg fskrsatgng resasqpgeq
     1261 wepvqessds pstspgsass ppgppgttpp gqkspsgpfc tpqspvslaq egtaqiwkrq
     1321 sqeveaggiq tvedehvael tlmgegdiss pnstllppps tpqevpgpsr pgsgthgsrd
     1381 lpvnriidvd lvtgsapgrd ggiagaqagp grsqasggpp tsdlpglgpv pgepakpkts
     1441 ahhatfv
//
LOCUS       NP_001192048             550 aa            linear   PRI 21-NOV-2025
DEFINITION  autophagy-related protein 13 isoform a [Homo sapiens].
ACCESSION   NP_001192048
VERSION     NP_001192048.1
DBSOURCE    REFSEQ: accession NM_001205119.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Patel,A. and Faesen,A.C.
  TITLE     Metamorphosis by ATG13 and ATG101 in human autophagy initiation
  JOURNAL   Autophagy 20 (4), 968-969 (2024)
   PUBMED   37394799
  REMARK    GeneRIF: Metamorphosis by ATG13 and ATG101 in human autophagy
            initiation.
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Nguyen,A. and Faesen,A.C.
  TITLE     The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis
  JOURNAL   FEBS Lett 598 (1), 114-126 (2024)
   PUBMED   37567770
  REMARK    GeneRIF: The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis.
            Review article
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Karabi,Z., Moradian,F. and Kheirabadi,M.
  TITLE     The effect of lactoferrin on ULK1 and ATG13 genes expression in
            breast cancer cell line MCF7 and bioinformatics studies of protein
            interaction between lactoferrin and the autophagy initiation
            complex
  JOURNAL   Cell Biochem Biophys 80 (4), 795-806 (2022)
   PUBMED   36169801
  REMARK    GeneRIF: The effect of lactoferrin on ULK1 and ATG13 genes
            expression in breast cancer cell line MCF7 and bioinformatics
            studies of protein interaction between lactoferrin and the
            autophagy initiation complex.
REFERENCE   5  (residues 1 to 550)
  AUTHORS   Gottschalk,G., Peterson,D., Knox,K., Maynard,M., Whelan,R.J. and
            Roy,A.
  TITLE     Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE)
  JOURNAL   Mol Cell Neurosci 120, 103731 (2022)
   PUBMED   35487443
  REMARK    GeneRIF: Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE).
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Jung,C.H., Jun,C.B., Ro,S.H., Kim,Y.M., Otto,N.M., Cao,J., Kundu,M.
            and Kim,D.H.
  TITLE     ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy
            machinery
  JOURNAL   Mol Biol Cell 20 (7), 1992-2003 (2009)
   PUBMED   19225151
  REMARK    GeneRIF: The ULK-Atg13-FIP200 complexes are direct targets of mTOR
            and important regulators of autophagy in response to mTOR
            signaling.
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Hosokawa,N., Hara,T., Kaizuka,T., Kishi,C., Takamura,A., Miura,Y.,
            Iemura,S., Natsume,T., Takehana,K., Yamada,N., Guan,J.L., Oshiro,N.
            and Mizushima,N.
  TITLE     Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200
            complex required for autophagy
  JOURNAL   Mol Biol Cell 20 (7), 1981-1991 (2009)
   PUBMED   19211835
  REMARK    GeneRIF: mTORC1 suppresses autophagy through direct regulation of
            the approximately 3-MDa ULK1-Atg13-FIP200 complex.
REFERENCE   8  (residues 1 to 550)
  AUTHORS   Chan,E.Y., Longatti,A., McKnight,N.C. and Tooze,S.A.
  TITLE     Kinase-inactivated ULK proteins inhibit autophagy via their
            conserved C-terminal domains using an Atg13-independent mechanism
  JOURNAL   Mol Cell Biol 29 (1), 157-171 (2009)
   PUBMED   18936157
  REMARK    GeneRIF: The functions of ULK1 and ULK2 are controlled by
            autophosphorylation and conformational changes involving exposure
            of the C-terminal domain and interaction with the putative human
            homologue of Atg13.
            GeneRIF: The gene product is the functional homologue of yeast
            Atg13, and required for autophagy in mammalian cells.
REFERENCE   9  (residues 1 to 550)
  AUTHORS   Meijer,W.H., van der Klei,I.J., Veenhuis,M. and Kiel,J.A.
  TITLE     ATG genes involved in non-selective autophagy are conserved from
            yeast to man, but the selective Cvt and pexophagy pathways also
            require organism-specific genes
  JOURNAL   Autophagy 3 (2), 106-116 (2007)
   PUBMED   17204848
REFERENCE   10 (residues 1 to 550)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA195671.1, AK223603.1 and
            BC002378.2.
            
            Summary: The protein encoded by this gene is an autophagy factor
            and a target of the TOR kinase signaling pathway. The encoded
            protein is essential for autophagosome formation and mitophagy.
            [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (3) encodes the longest isoform
            (a, also known as isoform 3). Variants 3 and 7-12 all encode the
            same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.37064.1,
                                           SRR1803615.152274.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..550
                     /product="autophagy-related protein 13 isoform a"
                     /note="autophagy-related protein 13; ATG13 autophagy
                     related 13 homolog"
                     /calculated_mol_wt=60024
     Region          19..192
                     /region_name="ATG13"
                     /note="Autophagy-related protein 13; pfam10033"
                     /db_xref="CDD:431003"
     CDS             1..550
                     /gene="ATG13"
                     /gene_synonym="KIAA0652; PARATARG8"
                     /coded_by="NM_001205119.2:352..2004"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55760.1"
                     /db_xref="GeneID:9776"
                     /db_xref="HGNC:HGNC:29091"
                     /db_xref="MIM:615088"
ORIGIN      
        1 metdlnsqdr kdldkfikff alktvqvivq arlgekictr ssssptgsdw fnlaikdipe
       61 vtheakkala gqlpavgrsm cveislktse gdsmeleiwc lemnekcdke ikvsytvynr
      121 lslllkslla itrvtpayrl srkqgheyvi lyriyfgevq lsglgegfqt vrvgtvgtpv
      181 gtitlscayr inlafmstrq fertppimgi iidhfvdrpy pssspmhpcn yrtagedtgv
      241 iypsvedsqe vcttsfstsp psqcvftvtk ahfqtptpvv tdtlrvpmag lafshqlsss
      301 rlsyqpaalg vgsadlaypv vfaaglnath phqlmvpgke ggvplapnqp vhgtqadqer
      361 latctpsdrt hcaatpssse dtetvsnsse grasphdvle tifvrkvgaf vnkpinqvtl
      421 tsldipfamf apknleledt dpmvnppdsp etesplqgsl hsdgssggss gnthddfvmi
      481 dfkpafskdd ilpmdlgtfy refqnppqls slsidigaqs maedldslpe klavheknvr
      541 efdafvetlq
//
LOCUS       NP_001381434             911 aa            linear   PRI 21-NOV-2025
DEFINITION  general transcription factor 3C polypeptide 2 isoform b [Homo
            sapiens].
ACCESSION   NP_001381434
VERSION     NP_001381434.1
DBSOURCE    REFSEQ: accession NM_001394505.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Peng,F., Zhou,Y., Wang,J., Guo,B., Wei,Y., Deng,H., Wu,Z.,
            Zhang,C., Shi,K., Li,Y., Wang,X., Shore,P., Zhao,S. and Deng,W.
  TITLE     The transcription factor Sp1 modulates RNA polymerase III gene
            transcription by controlling BRF1 and GTF3C2 expression in human
            cells
  JOURNAL   J Biol Chem 295 (14), 4617-4630 (2020)
   PUBMED   32115405
  REMARK    GeneRIF: The transcription factor Sp1 modulates RNA polymerase III
            gene transcription by controlling BRF1 and GTF3C2 expression in
            human cells.
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 911)
  AUTHORS   Kantidakis,T., Ramsbottom,B.A., Birch,J.L., Dowding,S.N. and
            White,R.J.
  TITLE     mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes,
            and targets their repressor Maf1
  JOURNAL   Proc Natl Acad Sci U S A 107 (26), 11823-11828 (2010)
   PUBMED   20543138
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11465]
REFERENCE   5  (residues 1 to 911)
  AUTHORS   Hirschowitz,E.A., Hiestand,D.M. and Yannelli,J.R.
  TITLE     Vaccines for lung cancer
  JOURNAL   J Thorac Oncol 1 (1), 93-104 (2006)
   PUBMED   17409835
  REMARK    Review article
REFERENCE   6  (residues 1 to 911)
  AUTHORS   Wang,Z. and Roeder,R.G.
  TITLE     DNA topoisomerase I and PC4 can interact with human TFIIIC to
            promote both accurate termination and transcription reinitiation by
            RNA polymerase III
  JOURNAL   Mol Cell 1 (5), 749-757 (1998)
   PUBMED   9660958
REFERENCE   7  (residues 1 to 911)
  AUTHORS   Oettel,S., Hartel,F., Kober,I., Iben,S. and Seifart,K.H.
  TITLE     Human transcription factors IIIC2, IIIC1 and a novel component
            IIIC0 fulfil different aspects of DNA binding to various pol III
            genes
  JOURNAL   Nucleic Acids Res 25 (12), 2440-2447 (1997)
   PUBMED   9171097
REFERENCE   8  (residues 1 to 911)
  AUTHORS   Chu,W.M., Wang,Z., Roeder,R.G. and Schmid,C.W.
  TITLE     RNA polymerase III transcription repressed by Rb through its
            interactions with TFIIIB and TFIIIC2
  JOURNAL   J Biol Chem 272 (23), 14755-14761 (1997)
   PUBMED   9169441
REFERENCE   9  (residues 1 to 911)
  AUTHORS   Sinn,E., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     Cloning and characterization of a TFIIIC2 subunit (TFIIIC beta)
            whose presence correlates with activation of RNA polymerase
            III-mediated transcription by adenovirus E1A expression and serum
            factors
  JOURNAL   Genes Dev 9 (6), 675-685 (1995)
   PUBMED   7729686
REFERENCE   10 (residues 1 to 911)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC074117.7, AC109828.4 and AC013413.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3134523.1,
                                           SRR14372079.1535745.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..911
                     /product="general transcription factor 3C polypeptide 2
                     isoform b"
                     /note="general transcription factor 3C polypeptide 2;
                     TFIIIC 110 kDa subunit; transcription factor IIIC subunit
                     beta; transcription factor IIIC 110 kDa subunit; general
                     transcription factor IIIC, polypeptide 2, beta 110kDa"
                     /calculated_mol_wt=100549
     Region          24..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          <62..255
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          205..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          366..426
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          427..483
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          470..543
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          484..535
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          536..603
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          558..595
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <559..644
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          604..654
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          616..656
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          655..690
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          765..785
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            871
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          889..911
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            892
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            893
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            895
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            901
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     CDS             1..911
                     /gene="GTF3C2"
                     /gene_synonym="TF3C-beta; TFIIIC-BETA; TFIIIC110"
                     /coded_by="NM_001394505.1:335..3070"
                     /note="isoform b is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS1749.1"
                     /db_xref="GeneID:2976"
                     /db_xref="HGNC:HGNC:4665"
                     /db_xref="MIM:604883"
ORIGIN      
        1 mdtcgvgyva lgeagpvgnm tvvdspgqev lnqldvktss emtsaeasve mslptplpgf
       61 edspdqrrlp peqeslsrle qpdlssemsk vskpraskpg rkrggrtrkg pkrpqqpnpp
      121 saplvpglld qsnplstpmp kkrgrkskae llllklskdl drpesqspkr ppedfetpsg
      181 erprrraaqv allylqelae elstalpapv scpegpkvss ptkpkkirqp aacpggeevd
      241 gaprdedffl qveaedvees egpsesssep epvvprstpr gstsgkqkph crgmapnglp
      301 nhimapvwkc lhltkdfreq khsywefaew iplawkwhll seleaapylp qeeksplfsv
      361 qreglpedgt lyrinrfssi tahperwdvs fftggplwal dwcpvpegag asqyvalfss
      421 pdmnethpls qlhsgpgllq lwglgtlqqe scpgnrahfv ygiacdngci wdlkfcpsga
      481 welpgtprka pllprlglla lacsdgkvll fslphpeall aqqppdavkp aiykvqcvat
      541 lqvgsmqatd psecgqclsl awmptrphqh laagyyngmv vfwnlptnsp lqrirlsdgs
      601 lklypfqcfl ahdqavrtlq wckanshflv sagsdrkikf wdlrrpyepi nsikrflste
      661 lawllpyngv tvaqdncyas yglcgihyid agylgfkayf taprkgtvws lsgsdwlgti
      721 aagdisgeli aailpdmaln pinvkrpver rfpiykadli pyqdspegpd hssassgvpn
      781 ppkartytet vnhhyllfqd tdlgsfhdll rrepmlrmqe geghsqlcld rlqleaihkv
      841 rfspnldsyg wlvsggqsgl vrihfvrgla splghrmqle srahfnamfq pssptrrpgf
      901 sptshrllpt p
//
LOCUS       NP_001364415             384 aa            linear   PRI 21-NOV-2025
DEFINITION  gigaxonin isoform 2 [Homo sapiens].
ACCESSION   NP_001364415 XP_016879223
VERSION     NP_001364415.1
DBSOURCE    REFSEQ: accession NM_001377486.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Renganathan,B., Zewe,J.P., Cheng,Y., Paumier,J.M., Kittisopikul,M.,
            Ridge,K.M., Opal,P. and Gelfand,V.I.
  TITLE     Gigaxonin is required for intermediate filament transport
  JOURNAL   FASEB J 37 (5), e22886 (2023)
   PUBMED   37043392
  REMARK    GeneRIF: Gigaxonin is required for intermediate filament transport.
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Zhang,X., Guo,Y. and Sun,W.
  TITLE     Two novel pathogenic mutations of GAN gene identified in a chinese
            family with giant axonal neuropathy: a case report
  JOURNAL   Mol Biol Rep 49 (9), 9107-9112 (2022)
   PUBMED   35764747
  REMARK    GeneRIF: Two novel pathogenic mutations of GAN gene identified in a
            chinese family with giant axonal neuropathy: a case report.
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Ding,J., Liu,J.J., Kowal,A.S., Nardine,T., Bhattacharya,P., Lee,A.
            and Yang,Y.
  TITLE     Microtubule-associated protein 1B: a neuronal binding partner for
            gigaxonin
  JOURNAL   J Cell Biol 158 (3), 427-433 (2002)
   PUBMED   12147674
  REMARK    Erratum:[J Cell Biol. 2003 Oct 13;163(1):189]
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Kuhlenbaumer,G., Young,P., Oberwittler,C., Hunermund,G.,
            Schirmacher,A., Domschke,K., Ringelstein,B. and Stogbauer,F.
  TITLE     Giant axonal neuropathy (GAN): case report and two novel mutations
            in the gigaxonin gene
  JOURNAL   Neurology 58 (8), 1273-1276 (2002)
   PUBMED   11971098
  REMARK    Erratum:[Neurology 2002 May 14;58(9):1444]
REFERENCE   8  (residues 1 to 384)
  AUTHORS   Bomont,P., Cavalier,L., Blondeau,F., Ben Hamida,C., Belal,S.,
            Tazir,M., Demir,E., Topaloglu,H., Korinthenberg,R., Tuysuz,B.,
            Landrieu,P., Hentati,F. and Koenig,M.
  TITLE     The gene encoding gigaxonin, a new member of the cytoskeletal
            BTB/kelch repeat family, is mutated in giant axonal neuropathy
  JOURNAL   Nat Genet 26 (3), 370-374 (2000)
   PUBMED   11062483
REFERENCE   9  (residues 1 to 384)
  AUTHORS   Flanigan,K.M., Crawford,T.O., Griffin,J.W., Goebel,H.H.,
            Kohlschutter,A., Ranells,J., Camfield,P.R. and Ptacek,L.J.
  TITLE     Localization of the giant axonal neuropathy gene to chromosome
            16q24
  JOURNAL   Ann Neurol 43 (1), 143-148 (1998)
   PUBMED   9450783
REFERENCE   10 (residues 1 to 384)
  AUTHORS   Opal,P.
  TITLE     GAN-Related Neurodegeneration
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301315
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009148.11 and AC092139.5.
            
            On Jan 16, 2020 this sequence version replaced XP_016879223.1.
            
            Summary: This gene encodes a member of the cytoskeletal BTB/kelch
            (Broad-Complex, Tramtrack and Bric a brac) repeat family. The
            encoded protein plays a role in neurofilament architecture and is
            involved in mediating the ubiquitination and degradation of some
            proteins. Defects in this gene are a cause of giant axonal
            neuropathy (GAN). [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2991409.1,
                                           SRR14038194.4184241.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145313, SAMEA2152798
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.2"
     Protein         1..384
                     /product="gigaxonin isoform 2"
                     /note="kelch-like protein 16; kelch-like family member 16;
                     epididymis secretory sperm binding protein"
                     /calculated_mol_wt=43230
     Region          85..262
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          103..147
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          151..195
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          198..243
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          245..298
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          301..348
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     CDS             1..384
                     /gene="GAN"
                     /gene_synonym="GAN1; GIG; KLHL16"
                     /coded_by="NM_001377486.1:677..1831"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:8139"
                     /db_xref="HGNC:HGNC:4137"
                     /db_xref="MIM:605379"
ORIGIN      
        1 mkdvmsalwv sgldssylre qmlneplvre ivkecsnipl sqpqqgeaml anfkprgyse
       61 civtvggeer vsrkptaamr cmcplydpnr qlwielapls mprinhgvls aegflfvfgg
      121 qdenkqtlss gekydpdant wtalppmnea rhnfgiveid gmlyilgged gekelismec
      181 ydiysktwtk qpdltmvrki gcyaamkkki yamgggsygk lfesvecydp rtqqwtaicp
      241 lkerrfgava cgvamelyvf ggvrsredaq gsemvtckse fyhdefkrwi ylndqnlcip
      301 asssfvygav pigasiyvig dldtgtnydy vrefkrstgt whhtkpllps dlrrtgcaal
      361 riancklfrl qlqqglfrir vhsp
//
LOCUS       NP_001363220             504 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase PAK 1 isoform 6 [Homo sapiens].
ACCESSION   NP_001363220
VERSION     NP_001363220.1
DBSOURCE    REFSEQ: accession NM_001376291.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Kervarrec,T., Westphal,D., Pissaloux,D., Legrand,M., Tirode,F.,
            Neuhart,A., Drouot,F., Becker,J.C., Macagno,N., Seris,A.,
            Jouary,T., Beltzung,F., Jullie,M.L., Harms,P.W., Cribier,B.,
            Mourah,S., Jouenne,F., Fromont,G., Louveau,B., Mancini,M.,
            Kazakov,D.V., de la Fouchardiere,A. and Battistella,M.
  TITLE     Porocarcinomas with PAK1/2/3 fusions: a series of 12 cases
  JOURNAL   Histopathology 85 (4), 566-578 (2024)
   PUBMED   38785043
  REMARK    GeneRIF: Porocarcinomas with PAK1/2/3 fusions: a series of 12
            cases.
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Zhao,P., Zhang,J., Song,W., Qi,D., Huang,Y., Su,Y., Wu,R., Zhang,L.
            and Zhang,S.
  TITLE     Incarvine C and its analogues inhibit the formation of cell
            cytoskeleton by targeting Rac1
  JOURNAL   Bioorg Chem 149, 107512 (2024)
   PUBMED   38833990
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Xu,M.H., Zheng,Y.M., Liang,B.G., Xu,W.X., Cao,J., Wang,P.,
            Dong,Z.Y., Zhou,C.H., Sun,H.C., Ren,N., Ke,A.W. and Shen,Y.H.
  TITLE     Deubiquitination of CIB1 by USP14 promotes lenvatinib resistance
            via the PAK1-ERK1/2 axis in hepatocellular carcinoma
  JOURNAL   Int J Biol Sci 20 (9), 3269-3284 (2024)
   PUBMED   38993552
  REMARK    GeneRIF: Deubiquitination of CIB1 by USP14 promotes lenvatinib
            resistance via the PAK1-ERK1/2 axis in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Luo,Q., Raulston,E.G., Prado,M.A., Wu,X., Gritsman,K., Whalen,K.S.,
            Yan,K., Booth,C.A.G., Xu,R., van Galen,P., Doench,J.G., Shimony,S.,
            Long,H.W., Neuberg,D.S., Paulo,J.A. and Lane,A.A.
  TITLE     Targetable leukaemia dependency on noncanonical PI3Kgamma
            signalling
  JOURNAL   Nature 630 (8015), 198-205 (2024)
   PUBMED   38720074
  REMARK    GeneRIF: Targetable leukaemia dependency on noncanonical PI3Kgamma
            signalling.
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Manser,E., Huang,H.Y., Loo,T.H., Chen,X.Q., Dong,J.M., Leung,T. and
            Lim,L.
  TITLE     Expression of constitutively active alpha-PAK reveals effects of
            the kinase on actin and focal complexes
  JOURNAL   Mol Cell Biol 17 (3), 1129-1143 (1997)
   PUBMED   9032240
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Bokoch,G.M., Wang,Y., Bohl,B.P., Sells,M.A., Quilliam,L.A. and
            Knaus,U.G.
  TITLE     Interaction of the Nck adapter protein with p21-activated kinase
            (PAK1)
  JOURNAL   J Biol Chem 271 (42), 25746-25749 (1996)
   PUBMED   8824201
REFERENCE   8  (residues 1 to 504)
  AUTHORS   Brown,J.L., Stowers,L., Baer,M., Trejo,J., Coughlin,S. and Chant,J.
  TITLE     Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase
            pathway
  JOURNAL   Curr Biol 6 (5), 598-605 (1996)
   PUBMED   8805275
REFERENCE   9  (residues 1 to 504)
  AUTHORS   Martin,G.A., Bollag,G., McCormick,F. and Abo,A.
  TITLE     A novel serine kinase activated by rac1/CDC42Hs-dependent
            autophosphorylation is related to PAK65 and STE20
  JOURNAL   EMBO J 14 (9), 1970-1978 (1995)
   PUBMED   7744004
  REMARK    Erratum:[EMBO J. 1995 Sep 1;14(17):4385. doi:
            10.1002/j.1460-2075.1995.tb00113.x. PMID: 7556080]
REFERENCE   10 (residues 1 to 504)
  AUTHORS   Manser,E., Leung,T., Salihuddin,H., Zhao,Z.S. and Lim,L.
  TITLE     A brain serine/threonine protein kinase activated by Cdc42 and Rac1
  JOURNAL   Nature 367 (6458), 40-46 (1994)
   PUBMED   8107774
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000486.6.
            
            Summary: This gene encodes a family member of serine/threonine
            p21-activating kinases, known as PAK proteins. These proteins are
            critical effectors that link RhoGTPases to cytoskeleton
            reorganization and nuclear signaling, and they serve as targets for
            the small GTP binding proteins Cdc42 and Rac. This specific family
            member regulates cell motility and morphology. Mutations in this
            gene have been associated with macrocephaly, seizures, and speech
            delay. Overexpression of this gene is also reported in many cancer
            types, and particularly in breast cancer. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2009249.1,
                                           SRR1803617.198786.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.5-q14.1"
     Protein         1..504
                     /product="serine/threonine-protein kinase PAK 1 isoform 6"
                     /EC_number="2.7.11.1"
                     /note="p21/Cdc42/Rac1-activated kinase 1 (yeast
                     Ste20-related); p21/Cdc42/Rac1-activated kinase 1 (STE20
                     homolog, yeast); serine/threonine-protein kinase PAK 1;
                     p21 protein (Cdc42/Rac)-activated kinase 1"
                     /calculated_mol_wt=55956
     Region          74..132
                     /region_name="PBD"
                     /note="P21-Rho-binding domain; pfam00786"
                     /db_xref="CDD:395634"
     Site            order(75,78,81,83,86,103,107)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238526"
     Region          249..503
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     CDS             1..504
                     /gene="PAK1"
                     /gene_synonym="alpha-PAK; IDDMSSD; p65-PAK; PAKalpha"
                     /coded_by="NM_001376291.1:220..1734"
                     /note="isoform 6 is encoded by transcript variant 26"
                     /db_xref="GeneID:5058"
                     /db_xref="HGNC:HGNC:8590"
                     /db_xref="MIM:602590"
ORIGIN      
        1 msnngldiqd kppappmrnt stmigagskd agtlnhgskp lppnpeekkk kdrfyrsilp
       61 gdktnkkkek erpeislpsd fehtihvgfd avtgeftgmp eqwarllqts nitkseqkkn
      121 pqavldvlef ynskktsnsq kymsftdksa edynssnaln vkavsetpav ppvsededdd
      181 dddatpppvi aprpehtksv ytrsvieplp vtptrdvats pisptenntt ppdaltrnte
      241 kqkkkpkmsd eeileklrsi vsvgdpkkky trfekigqga sgtvytamdv atgqevaikq
      301 mnlqqqpkke liineilvmr enknpnivny ldsylvgdel wvvmeylagg sltdvvtetc
      361 mdegqiaavc reitpeqskr stmvgtpywm apevvtrkay gpkvdiwslg imaiemiege
      421 ppylnenplr alyliatngt pelqnpekls aifrdflnrc lemdvekrgs akellqhqfl
      481 kiakplsslt pliaaakeat knnh
//
LOCUS       NP_001041686             161 aa            linear   PRI 21-NOV-2025
DEFINITION  dysbindin domain-containing protein 2 isoform a [Homo sapiens].
ACCESSION   NP_001041686
VERSION     NP_001041686.1
DBSOURCE    REFSEQ: accession NM_001048221.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Elsholz,L., Wasser,Y., Ziegler,P., Habib,P. and Voigt,A.
  TITLE     CK1BP Reduces alpha-Synuclein Oligomerization and Aggregation
            Independent of Serine 129 Phosphorylation
  JOURNAL   Cells 10 (11), 2830 (2021)
   PUBMED   34831053
  REMARK    GeneRIF: CK1BP Reduces alpha-Synuclein Oligomerization and
            Aggregation Independent of Serine 129 Phosphorylation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   5  (residues 1 to 161)
  AUTHORS   Yin,H., Laguna,K.A., Li,G. and Kuret,J.
  TITLE     Dysbindin structural homologue CK1BP is an isoform-selective
            binding partner of human casein kinase-1
  JOURNAL   Biochemistry 45 (16), 5297-5308 (2006)
   PUBMED   16618118
  REMARK    GeneRIF: CK1BP is an isoform-selective binding partner of human
            casein kinase-1
REFERENCE   6  (residues 1 to 161)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   7  (residues 1 to 161)
  AUTHORS   Lucas,T., Pratscher,B., Fink,D., Wolschek,M., Samorapoompichit,P.,
            Schofer,C., Pehamberger,H., Muller,M., Sorensen,P. and Jansen,B.
  TITLE     The human orthologue of a novel apoptosis response gene induced
            during rat myelomonocytic stem cell apoptosis maps to 20q13.12
  JOURNAL   Stem Cells Dev 14 (5), 556-563 (2005)
   PUBMED   16305340
REFERENCE   8  (residues 1 to 161)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP330715.1, AL021578.4 and AW516035.1.
            
            Transcript Variant: This variant (1) encodes isoform a. Variants 1,
            5, 7 and 8 all encode the same isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP368882.1, SRR3476690.989945.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..161
                     /product="dysbindin domain-containing protein 2 isoform a"
                     /note="SCF apoptosis response protein 1; casein kinase-1
                     binding protein; dysbindin (dystrobrevin binding protein
                     1) domain containing 2"
                     /calculated_mol_wt=17394
     Region          12..157
                     /region_name="Dysbindin"
                     /note="Dysbindin (Dystrobrevin binding protein 1);
                     pfam04440"
                     /db_xref="CDD:461312"
     CDS             1..161
                     /gene="DBNDD2"
                     /gene_synonym="C20orf35; CK1BP; HSMNP1"
                     /coded_by="NM_001048221.3:168..653"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42880.1"
                     /db_xref="GeneID:55861"
                     /db_xref="HGNC:HGNC:15881"
                     /db_xref="MIM:611453"
ORIGIN      
        1 mdpnpraale rqqlrlrerq kffedilqpe tefvfplshl hlesqrppig sissmevnvd
       61 tleqvelidl gdpdaadvfl pcedppptpq ssgmdnhlee lslpvptsdr ttsrtsssss
      121 sdsstnlhsp npsddgadtp laqsdeeeer gdggaepgac s
//
LOCUS       NP_001337400             959 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 1 isoform 65 [Homo
            sapiens].
ACCESSION   NP_001337400
VERSION     NP_001337400.1
DBSOURCE    REFSEQ: accession NM_001350471.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 959)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 959)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 959)
  AUTHORS   Ruhle,F., Witten,A., Barysenka,A., Huge,A., Arning,A., Heller,C.,
            Krumpel,A., Mesters,R., Franke,A., Lieb,W., Riemenschneider,M.,
            Hiersche,M., Limperger,V., Nowak-Gottl,U. and Stoll,M.
  TITLE     Rare genetic variants in SMAP1, B3GAT2, and RIMS1 contribute to
            pediatric venous thromboembolism
  JOURNAL   Blood 129 (6), 783-790 (2017)
   PUBMED   28011674
  REMARK    GeneRIF: The study identified a region on chromosome 6 comprising
            the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus
            for pediatric venous thromboembolism.
REFERENCE   6  (residues 1 to 959)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 959)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
REFERENCE   8  (residues 1 to 959)
  AUTHORS   Schoch,S., Castillo,P.E., Jo,T., Mukherjee,K., Geppert,M., Wang,Y.,
            Schmitz,F., Malenka,R.C. and Sudhof,T.C.
  TITLE     RIM1alpha forms a protein scaffold for regulating neurotransmitter
            release at the active zone
  JOURNAL   Nature 415 (6869), 321-326 (2002)
   PUBMED   11797009
REFERENCE   9  (residues 1 to 959)
  AUTHORS   Coppola,T., Magnin-Luthi,S., Perret-Menoud,V., Gattesco,S.,
            Schiavo,G. and Regazzi,R.
  TITLE     Direct interaction of the Rab3 effector RIM with Ca2+ channels,
            SNAP-25, and synaptotagmin
  JOURNAL   J Biol Chem 276 (35), 32756-32762 (2001)
   PUBMED   11438518
REFERENCE   10 (residues 1 to 959)
  AUTHORS   Betz,A., Thakur,P., Junge,H.J., Ashery,U., Rhee,J.S., Scheuss,V.,
            Rosenmund,C., Rettig,J. and Brose,N.
  TITLE     Functional interaction of the active zone proteins Munc13-1 and
            RIM1 in synaptic vesicle priming
  JOURNAL   Neuron 30 (1), 183-196 (2001)
   PUBMED   11343654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590011.5, AL445256.18 and
            AL035633.18.
            
            Summary: The protein encoded by this gene is a RAS gene superfamily
            member that regulates synaptic vesicle exocytosis. This gene also
            plays a role in the regulation of voltage-gated calcium channels
            during neurotransmitter and insulin release. Mutations have
            suggested a role cognition and have been identified as the cause of
            cone-rod dystrophy type 7. Multiple transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Mar 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.77084.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..959
                     /product="regulating synaptic membrane exocytosis protein
                     1 isoform 65"
                     /note="RAB3-interacting protein 2; rab3-interacting
                     molecule 1; rab-3-interacting protein 2"
                     /calculated_mol_wt=107160
     Region          45..141
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(66..72,87,90,120,124,127..128)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          193..319
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(224,230,285,287,295)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          790..935
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(847,851..852,854,857,885,887,889,933..934)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..959
                     /gene="RIMS1"
                     /gene_synonym="CORD7; RAB3IP2; RIM; RIM1"
                     /coded_by="NM_001350471.2:361..3240"
                     /note="isoform 65 is encoded by transcript variant 65"
                     /db_xref="GeneID:22999"
                     /db_xref="HGNC:HGNC:17282"
                     /db_xref="MIM:606629"
ORIGIN      
        1 meysvsmwkp gdldyywldp atwhsretsp isshpvtwqp skegdrligr vilnkrttmp
       61 kdsgallglk vvggkmtdlg rlgafitkvk kgsladvvgh lragdevlew ngkplpgatn
      121 eevyniiles ksepqveiiv srpigdipri pesshpples ssssfesqkm erpsisvisp
      181 tspgalkdap qvlpgqlsvk lwydkvghql ivnvlqatdl parvdgrprn pyvkmyflpd
      241 rsdkskrrtk tvkkilepkw nqtfvyshvh rrdfrermle itvwdqprvq eeeseflgei
      301 lieletalld dephwyklqt hdesslplpq pspfmprrhi hgessskklq rsqrisdsdi
      361 sdyevddgig vvppgyrssa resksttltv peqqrtthhr srsvsphrgn dqgkprsrlp
      421 nvplqrslde ihptrrsrsp trhhdasrsp vdhrtrdvds qylseqdsel lmlprakrgr
      481 saeclhttrh srkserssiq kqtrkgtasd aermhrqrsp tqsppadtsf ssrrgrqlpq
      541 vpvrsgsieq aslvveertr qmkmkvhrfk qttgsgssqe ldreqyskyn ihkdqyrscd
      601 nvsakssdsd vsdvsaisrt ssasrlssts fmseqserpr grissftpkm qgrrmgtsgr
      661 simkstsvsg emytlehndg sqsdtavgtv gaggkkrrss lsakvvaivs rrsrstsqls
      721 qtesghkklk stiqrstetg maaemrkmvr qpsrestdgs insyssegnl ifpgvrlgad
      781 sqfsdfldgl gpaqlvgrqt latpamgdiq igmedkkgql evevirarsl tqkpgskstp
      841 apyvkvylle ngaciakkkt riarktldpl yqqslvfdes pqgkvlqviv wgdygrmdhk
      901 cfmgvaqill eeldlssmvi gwyklfppss lvdptltplt rrasqssles stgppcirs
//
LOCUS       NP_001362659             418 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform ggg [Homo sapiens].
ACCESSION   NP_001362659
VERSION     NP_001362659.1
DBSOURCE    REFSEQ: accession NM_001375730.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 418)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 418)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 418)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.925300.1,
                                           SRR14038192.601408.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..418
                     /product="abl interactor 2 isoform ggg"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=45980
     Region          39..100
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          357..417
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(365,367,370,374,392..393,406,408..409)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..418
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375730.1:122..1378"
                     /note="isoform ggg is encoded by transcript variant 64"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqt vdihkekvar reigilttnk
       61 ntsrthkiia panlerpvry irkpidytil ddighgvkvs tqnmkmgglp rttpptqkpp
      121 sppmsgkgtl grhspyrtle pvrppvvpnd yvpsptrnma psqqspvrta svnqrnrtys
      181 sgssggshps srsssrensg sgsvgvpiav ptpsppsvfp ghpvqfysmn rpasrhtppt
      241 iggslpyrrp psitsqtslq nqmnggpfys qnpvslappp psilqvtpql plmgfvarvq
      301 enisdtpppp ppveepvfde sppppppped yeeeeaavve ysdpyaeedp pwaprsylek
      361 vvaiydytkd kedelsfqeg aiiyvikknd dgwyegvmng vtglfpgnyv esimhyse
//
LOCUS       NP_001341872             174 aa            linear   PRI 21-NOV-2025
DEFINITION  cullin-4A isoform 5 [Homo sapiens].
ACCESSION   NP_001341872
VERSION     NP_001341872.1
DBSOURCE    REFSEQ: accession NM_001354943.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Jia,Y., Huo,X., Wu,L., Zhang,H., Xu,W. and Leng,H.
  TITLE     circSNTB2 and CUL4A Induces Dysfunction of Nucleus Pulposus Cells
            by Competitively Binding miR-665
  JOURNAL   Biochem Genet 62 (2), 968-986 (2024)
   PUBMED   37507642
  REMARK    GeneRIF: circSNTB2 and CUL4A Induces Dysfunction of Nucleus
            Pulposus Cells by Competitively Binding miR-665.
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Tavlas,P., Nikou,S., Geramoutsou,C., Bosgana,P., Tsaniras,S.C.,
            Melachrinou,M., Maroulis,I. and Bravou,V.
  TITLE     CUL4A Ubiquitin Ligase Is an Independent Predictor of Overall
            Survival in Pancreatic Adenocarcinoma
  JOURNAL   Cancer Genomics Proteomics 21 (2), 166-177 (2024)
   PUBMED   38423594
  REMARK    GeneRIF: CUL4A Ubiquitin Ligase Is an Independent Predictor of
            Overall Survival in Pancreatic Adenocarcinoma.
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Hu,Y., Zhang,R., Lu,S., Zhang,W., Wang,D., Ge,Y., Jiang,F., Qin,X.
            and Liu,Y.
  TITLE     S100 Calcium Binding Protein A16 Promotes Cell Proliferation by
            triggering LATS1 ubiquitin degradation mediated by CUL4A ligase to
            inhibit Hippo pathway in Glioma development
  JOURNAL   Int J Biol Sci 19 (7), 2034-2052 (2023)
   PUBMED   37151881
  REMARK    GeneRIF: S100 Calcium Binding Protein A16 Promotes Cell
            Proliferation by triggering LATS1 ubiquitin degradation mediated by
            CUL4A ligase to inhibit Hippo pathway in Glioma development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Ito,T., Ando,H., Suzuki,T., Ogura,T., Hotta,K., Imamura,Y.,
            Yamaguchi,Y. and Handa,H.
  TITLE     Identification of a primary target of thalidomide teratogenicity
  JOURNAL   Science 327 (5971), 1345-1350 (2010)
   PUBMED   20223979
REFERENCE   6  (residues 1 to 174)
  AUTHORS   Angers,S., Li,T., Yi,X., MacCoss,M.J., Moon,R.T. and Zheng,N.
  TITLE     Molecular architecture and assembly of the DDB1-CUL4A ubiquitin
            ligase machinery
  JOURNAL   Nature 443 (7111), 590-593 (2006)
   PUBMED   16964240
  REMARK    GeneRIF: crystallographic analyses of the virally hijacked form of
            the human DDB1-CUL4A-ROC1 machinery
REFERENCE   7  (residues 1 to 174)
  AUTHORS   Ohta,T., Michel,J.J., Schottelius,A.J. and Xiong,Y.
  TITLE     ROC1, a homolog of APC11, represents a family of cullin partners
            with an associated ubiquitin ligase activity
  JOURNAL   Mol Cell 3 (4), 535-541 (1999)
   PUBMED   10230407
REFERENCE   8  (residues 1 to 174)
  AUTHORS   Chen,L.C., Manjeshwar,S., Lu,Y., Moore,D., Ljung,B.M., Kuo,W.L.,
            Dairkee,S.H., Wernick,M., Collins,C. and Smith,H.S.
  TITLE     The human homologue for the Caenorhabditis elegans cul-4 gene is
            amplified and overexpressed in primary breast cancers
  JOURNAL   Cancer Res 58 (16), 3677-3683 (1998)
   PUBMED   9721878
REFERENCE   9  (residues 1 to 174)
  AUTHORS   Osaka,F., Kawasaki,H., Aida,N., Saeki,M., Chiba,T., Kawashima,S.,
            Tanaka,K. and Kato,S.
  TITLE     A new NEDD8-ligating system for cullin-4A
  JOURNAL   Genes Dev 12 (15), 2263-2268 (1998)
   PUBMED   9694792
REFERENCE   10 (residues 1 to 174)
  AUTHORS   Kipreos,E.T., Lander,L.E., Wing,J.P., He,W.W. and Hedgecock,E.M.
  TITLE     cul-1 is required for cell cycle exit in C. elegans and identifies
            a novel gene family
  JOURNAL   Cell 85 (6), 829-839 (1996)
   PUBMED   8681378
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB455959.1, BC008308.1,
            BQ185339.1 and CK300635.1.
            
            Summary: CUL4A is the ubiquitin ligase component of a multimeric
            complex involved in the degradation of DNA damage-response proteins
            (Liu et al., 2009 [PubMed 19481525]).[supplied by OMIM, Oct 2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.278187.1, BX340651.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..174
                     /product="cullin-4A isoform 5"
                     /note="CUL-4A"
                     /calculated_mol_wt=19615
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13619.3)"
     Region          63..>170
                     /region_name="Cullin"
                     /note="Cullin family; pfam00888"
                     /db_xref="CDD:459983"
     CDS             1..174
                     /gene="CUL4A"
                     /coded_by="NM_001354943.2:16..540"
                     /note="isoform 5 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS86363.1"
                     /db_xref="GeneID:8451"
                     /db_xref="HGNC:HGNC:2554"
                     /db_xref="MIM:603137"
ORIGIN      
        1 madeaprkgs fsalvgrtng ltkpaalaaa pakpggaggs kklviknfrd rprlpdnytq
       61 dtwrklheav ravqsstsir ynleelyqav enlcshkvsp mlykqlrqac edhvqaqilp
      121 fredsldsvl flkkintcwq dhcrqmimir siflfldrty vlqnstlpsi cqnh
//
LOCUS       NP_001340426             643 aa            linear   PRI 21-NOV-2025
DEFINITION  asparagine synthetase domain-containing protein 1 [Homo sapiens].
ACCESSION   NP_001340426 NP_001340427
VERSION     NP_001340426.1
DBSOURCE    REFSEQ: accession NM_001353497.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Vogel,P., Ding,Z.M., Read,R., DaCosta,C.M., Hansard,M., Small,D.L.,
            Ye,G.L., Hansen,G., Brommage,R. and Powell,D.R.
  TITLE     Progressive Degenerative Myopathy and Myosteatosis in
            ASNSD1-Deficient Mice
  JOURNAL   Vet Pathol 57 (5), 723-735 (2020)
   PUBMED   32638637
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Li,J.W., Li,K., Jiang,J., Xu,X.L. and Huang,Z.Q.
  TITLE     Construction of eukaryotic expression plasmid containing HCV NS3
            segment and protein expression in human HL-7702 hepatocytes
  JOURNAL   World J Gastroenterol 12 (7), 1038-1042 (2006)
   PUBMED   16534843
  REMARK    GeneRIF: Normal human HL-7702 hepatocytes can efficiently express
            specific HCV NS3 protein in vitro.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012488.10.
            
            On Mar 23, 2018 this sequence version replaced NP_001340427.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.236452.1,
                                           SRR14038191.4426226.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.2"
     Protein         1..643
                     /product="asparagine synthetase domain-containing protein
                     1"
                     /note="HCV NS3-transactivated protein 1"
                     /calculated_mol_wt=71949
     Region          1..179
                     /region_name="Gn_AT_II_novel"
                     /note="This asparagine synthase-related domain is present
                     in eukaryotes but its function has not yet been
                     determined. The glutaminase domain catalyzes an amide
                     nitrogen transfer from glutamine to the appropriate
                     substrate. In this process, glutamine is...; cd03766"
                     /db_xref="CDD:239735"
     Site            order(2,54,76..78,91)
                     /site_type="active"
                     /db_xref="CDD:239735"
     Region          320..608
                     /region_name="Asn_synthase_B_C"
                     /note="C-terminal domain of asparagine synthase B;
                     cd01991"
                     /db_xref="CDD:467495"
     CDS             1..643
                     /gene="ASNSD1"
                     /gene_synonym="NBLA00058; NS3TP1"
                     /coded_by="NM_001353497.2:321..2252"
                     /db_xref="CCDS:CCDS2300.1"
                     /db_xref="GeneID:54529"
                     /db_xref="HGNC:HGNC:24910"
                     /db_xref="MIM:619739"
ORIGIN      
        1 mcgiccsvnf saehfsqdlk edllynlkqr gpnsskqllk sdvnyqclfs ahvlhlrgvl
       61 ttqpvederg nvflwngeif sgikveaeen dtqilfnyls sckneseils lfsevqgpws
      121 fiyyqasshy lwfgrdffgr rsllwhfsnl gksfclssvg tqtsglanqw qevpasglfr
      181 idlkstvisg ciilqlypwk yisreniiee nvnslsqisa dlpafvsvva neaklylekp
      241 vvplnmmlpq aalethcsni snvpptreil qvfltdvhmk eviqqfidvl svavkkrvlc
      301 lprdenltan evlktcdrka nvailfsggi dsmviatlad rhipldepid llnvafiaee
      361 ktmpttfnre gnkqknkcei pseefskdva aaaadspnkh vsvpdritgr aglkelqavs
      421 psriwnfvei nvsmeelqkl rrtrichlir pldtvlddsi gcavwfasrg igwlvaqegv
      481 ksyqsnakvv ltgigadeql agysrhrvrf qshgleglnk eimmelgris srnlgrddrv
      541 igdhgkearf pfldenvvsf lnslpiweka nltlprgige klllrlaave lgltasallp
      601 kramqfgsri akmekineka sdkcgrlqim slenlsieke tkl
//
LOCUS       NP_001362766             403 aa            linear   PRI 21-NOV-2025
DEFINITION  WAS/WASL-interacting protein family member 1 isoform c [Homo
            sapiens].
ACCESSION   NP_001362766
VERSION     NP_001362766.1
DBSOURCE    REFSEQ: accession NM_001375837.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Dong,Y., Jin,Q., Sun,M., Qi,D., Qu,H., Wang,X. and Quan,C.
  TITLE     CLDN6 inhibits breast cancer metastasis through WIP-dependent actin
            cytoskeleton-mediated autophagy
  JOURNAL   J Exp Clin Cancer Res 42 (1), 68 (2023)
   PUBMED   36935496
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Sokolik,C.G., Qassem,N. and Chill,J.H.
  TITLE     The Disordered Cellular Multi-Tasker WIP and Its Protein-Protein
            Interactions: A Structural View
  JOURNAL   Biomolecules 10 (7), 1084 (2020)
   PUBMED   32708183
  REMARK    GeneRIF: The Disordered Cellular Multi-Tasker WIP and Its
            Protein-Protein Interactions: A Structural View.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 403)
  AUTHORS   Vaduva,G., Martinez-Quiles,N., Anton,I.M., Martin,N.C., Geha,R.S.,
            Hopper,A.K. and Ramesh,N.
  TITLE     The human WASP-interacting protein, WIP, activates the cell
            polarity pathway in yeast
  JOURNAL   J Biol Chem 274 (24), 17103-17108 (1999)
   PUBMED   10358064
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Stewart,D.M., Tian,L. and Nelson,D.L.
  TITLE     Mutations that cause the Wiskott-Aldrich syndrome impair the
            interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP
            interacting protein
  JOURNAL   J Immunol 162 (8), 5019-5024 (1999)
   PUBMED   10202051
REFERENCE   8  (residues 1 to 403)
  AUTHORS   Ramesh,N., Anton,I.M., Martinez-Quiles,N. and Geha,R.S.
  TITLE     Waltzing with WASP
  JOURNAL   Trends Cell Biol 9 (1), 15-19 (1999)
   PUBMED   10087612
  REMARK    Review article
REFERENCE   9  (residues 1 to 403)
  AUTHORS   Anton,I.M., Lu,W., Mayer,B.J., Ramesh,N. and Geha,R.S.
  TITLE     The Wiskott-Aldrich syndrome protein-interacting protein (WIP)
            binds to the adaptor protein Nck
  JOURNAL   J Biol Chem 273 (33), 20992-20995 (1998)
   PUBMED   9694849
REFERENCE   10 (residues 1 to 403)
  AUTHORS   Ramesh,N., Anton,I.M., Hartwig,J.H. and Geha,R.S.
  TITLE     WIP, a protein associated with wiskott-aldrich syndrome protein,
            induces actin polymerization and redistribution in lymphoid cells
  JOURNAL   Proc Natl Acad Sci U S A 94 (26), 14671-14676 (1997)
   PUBMED   9405671
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010894.10.
            
            Summary: This gene encodes a protein that plays an important role
            in the organization of the actin cytoskeleton. The encoded protein
            binds to a region of Wiskott-Aldrich syndrome protein that is
            frequently mutated in Wiskott-Aldrich syndrome, an X-linked
            recessive disorder. Impairment of the interaction between these two
            proteins may contribute to the disease. Two transcript variants
            encoding the same protein have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (8), as well as variants 7 and 9,
            encodes isoform c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK304194.1, SRR14038193.3125456.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..403
                     /product="WAS/WASL-interacting protein family member 1
                     isoform c"
                     /note="Wiskott-Aldrich syndrome protein interacting
                     protein; protein PRPL-2; WASP-interacting protein;
                     testicular tissue protein Li 226"
                     /calculated_mol_wt=40332
     Region          29..60
                     /region_name="WH2_WAS_WASL-1"
                     /note="Wiskott Aldrich syndrome homology region 2 (WH2
                     motif) in WAS/WASL-interacting protein family member 1;
                     cd22076"
                     /db_xref="CDD:409219"
     Site            order(29..33,35..37,39..41,44,46..60)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409219"
     Region          46..49
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409219"
     CDS             1..403
                     /gene="WIPF1"
                     /gene_synonym="PRPL-2; WAS2; WASPIP; WIP"
                     /coded_by="NM_001375837.1:127..1338"
                     /note="isoform c is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS92900.1"
                     /db_xref="GeneID:7456"
                     /db_xref="HGNC:HGNC:12736"
                     /db_xref="MIM:602357"
ORIGIN      
        1 mpvppppapp ppptfalant ekptlnkteq agrnallsdi skgkklkktv tndrsapild
       61 kpkgagaggg gggfgggggf gggggggggg sfggggppgl gglfqagmpk lrstanrdnd
      121 sggsrppllp pggrstsakp fsppsgpgrf pvpspghrsg ppepqrnrmp pprpdvgskp
      181 dsipppvpst prpiqssphn rgsppvpggp rqpspgptpp pfpgnrgtal gggsirqspl
      241 sssspfsnrp plpptpsral ddkppppppp vgnrpsihre avpppppqnn kppvpstprp
      301 sassqapppp pppsrpgppp lppsssgnde tprlpqrnls lssstpplps pgrsgplppp
      361 pserppppvr dppgrsgmtr rgvscfqnpa cpnvpiilsv kiv
//
LOCUS       NP_001369222              91 aa            linear   PRI 21-NOV-2025
DEFINITION  ragulator complex protein LAMTOR5 isoform 2 [Homo sapiens].
ACCESSION   NP_001369222
VERSION     NP_001369222.1
DBSOURCE    REFSEQ: accession NM_001382293.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Zhang,W., Sha,Z., Tang,Y., Jin,C., Gao,W., Chen,C., Yu,L., Lv,N.,
            Liu,S., Xu,F., Wang,D. and Shi,L.
  TITLE     Defective Lamtor5 Leads to Autoimmunity by Deregulating v-ATPase
            and Lysosomal Acidification
  JOURNAL   Adv Sci (Weinh) 11 (22), e2400446 (2024)
   PUBMED   38639386
  REMARK    GeneRIF: Defective Lamtor5 Leads to Autoimmunity by Deregulating
            v-ATPase and Lysosomal Acidification.
REFERENCE   4  (residues 1 to 91)
  AUTHORS   Cheng,L., Guo,L., Zou,T., Yang,Y., Tao,R. and Liu,S.
  TITLE     Research progress on oncoprotein hepatitis B X-interacting protein
            (Review)
  JOURNAL   Mol Med Rep 29 (6) (2024)
   PUBMED   38577934
  REMARK    GeneRIF: Research progress on oncoprotein hepatitis B X-interacting
            protein (Review).
            Review article
REFERENCE   5  (residues 1 to 91)
  AUTHORS   Jansen,R.M., Peruzzo,R., Fromm,S.A., Yokom,A.L., Zoncu,R. and
            Hurley,J.H.
  TITLE     Structural basis for FLCN RagC GAP activation in MiT-TFE
            substrate-selective mTORC1 regulation
  JOURNAL   Sci Adv 8 (37), eadd2926 (2022)
   PUBMED   36103527
REFERENCE   6  (residues 1 to 91)
  AUTHORS   Lee,S.H., Park,S.G., Lim,S.O. and Jung,G.
  TITLE     The hepatitis B virus X protein up-regulates lymphotoxin alpha
            expression in hepatocytes
  JOURNAL   Biochim Biophys Acta 1741 (1-2), 75-84 (2005)
   PUBMED   15955450
  REMARK    GeneRIF: HBXIP up-regulates LTA expression in hepatocytes.
REFERENCE   7  (residues 1 to 91)
  AUTHORS   Marusawa,H., Matsuzawa,S., Welsh,K., Zou,H., Armstrong,R., Tamm,I.
            and Reed,J.C.
  TITLE     HBXIP functions as a cofactor of survivin in apoptosis suppression
  JOURNAL   EMBO J 22 (11), 2729-2740 (2003)
   PUBMED   12773388
  REMARK    GeneRIF: Survivin-HBXIP complexes, but neither survivin nor HBXIP
            individually, bind pro-caspase-9, preventing its recruitment to
            Apaf1, and thereby selectively suppressing apoptosis.
REFERENCE   8  (residues 1 to 91)
  AUTHORS   Li,Y. and Lu,Y.Y.
  TITLE     Applying a highly specific and reproducible cDNA RDA method to
            clone garlic up-regulated genes in human gastric cancer cells
  JOURNAL   World J Gastroenterol 8 (2), 213-216 (2002)
   PUBMED   11925594
  REMARK    GeneRIF: Elevated levels of GDN/PN1 and XIP mRNAs induced by
            Allitridi provide valuable molecular evidence for elucidating
            garlic's efficacies against neurodegenerative and inflammatory
            diseases.
REFERENCE   9  (residues 1 to 91)
  AUTHORS   Shamay,M., Barak,O., Doitsh,G., Ben-Dor,I. and Shaul,Y.
  TITLE     Hepatitis B virus pX interacts with HBXAP, a PHD finger protein to
            coactivate transcription
  JOURNAL   J Biol Chem 277 (12), 9982-9988 (2002)
   PUBMED   11788598
  REMARK    GeneRIF: Hepatitis B virus pX interacts with HBXAP
REFERENCE   10 (residues 1 to 91)
  AUTHORS   Melegari,M., Scaglioni,P.P. and Wands,J.R.
  TITLE     Cloning and characterization of a novel hepatitis B virus x binding
            protein that inhibits viral replication
  JOURNAL   J Virol 72 (3), 1737-1743 (1998)
   PUBMED   9499022
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390797.16.
            
            Summary: This gene encodes a protein that specifically complexes
            with the C-terminus of hepatitis B virus X protein (HBx). The
            function of this protein is to negatively regulate HBx activity and
            thus to alter the replication life cycle of the virus. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) uses a downstream
            transcription start site and a downstream in-frame translation
            start site, compared to variant 1. The encoded isoform (2) has a
            shorter N-terminus, compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC062619.1, BF791527.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000602318.6/ ENSP00000473439.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..91
                     /product="ragulator complex protein LAMTOR5 isoform 2"
                     /note="HBx-interacting protein; hepatitis B virus
                     x-interacting protein (9.6kD); HBV X-interacting protein;
                     hepatitis B virus x interacting protein; late
                     endosomal/lysosomal adaptor and MAPK and MTOR activator 5;
                     ragulator complex protein LAMTOR5"
                     /calculated_mol_wt=9483
     Region          1..88
                     /region_name="LAMTOR5"
                     /note="Ragulator complex protein LAMTOR5; pfam16672"
                     /db_xref="CDD:406957"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (O43504.1)"
     CDS             1..91
                     /gene="LAMTOR5"
                     /gene_synonym="HBXIP; XIP"
                     /coded_by="NM_001382293.1:75..350"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS91022.1"
                     /db_xref="GeneID:10542"
                     /db_xref="HGNC:HGNC:17955"
                     /db_xref="MIM:608521"
ORIGIN      
        1 meatleqhle dtmknpsivg vlctdsqgln lgcrgtlsde hagvisvlaq qaakltsdpt
       61 dipvvclesd ngnimiqkhd gitvavhkma s
//
LOCUS       NP_001363704             535 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 34 [Homo sapiens].
ACCESSION   NP_001363704 XP_005265839
VERSION     NP_001363704.1
DBSOURCE    REFSEQ: accession NM_001376775.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Muckenfuss,L.M., Migenda Herranz,A.C., Boneberg,F.M., Clerici,M.
            and Jinek,M.
  TITLE     Fip1 is a multivalent interaction scaffold for processing factors
            in human mRNA 3' end biogenesis
  JOURNAL   Elife 11, e80332 (2022)
   PUBMED   36073787
  REMARK    GeneRIF: Fip1 is a multivalent interaction scaffold for processing
            factors in human mRNA 3' end biogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Tennenbaum,J., Groh,M., Venditti,L., Campos-Gazeau,F., Chalayer,E.,
            De Broucker,T., Hamidou,M., Hunault,M., Lyoubi,A., Meunier,R.,
            Muron,T., Sene,D., Slama,B., Guidoux,C., Lefevre,G., Kahn,J.E.,
            Denier,C. and Rohmer,J.
  TITLE     FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a Treatable
            Cause of Watershed Infarction
  JOURNAL   Stroke 52 (10), e605-e609 (2021)
   PUBMED   34304603
  REMARK    GeneRIF: FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a
            Treatable Cause of Watershed Infarction.
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 535)
  AUTHORS   Helbig,G., Lewandowski,K., Swiderska,A., Rodzaj,M., Seferynska,I.
            and Gajkowska-Kulik,J.
  TITLE     Exquisite response to imatinib mesylate in FIP1L1-PDGFRA-mutated
            hypereosinophilic syndrome: a 12-year experience of the Polish
            Hypereosinophilic Syndrome Study Group
  JOURNAL   Pol Arch Intern Med 130 (3), 255-257 (2020)
   PUBMED   32125294
  REMARK    GeneRIF: Exquisite response to imatinib mesylate in
            FIP1L1-PDGFRA-mutated hypereosinophilic syndrome: a 12-year
            experience of the Polish Hypereosinophilic Syndrome Study Group.
REFERENCE   6  (residues 1 to 535)
  AUTHORS   Cools,J., Quentmeier,H., Huntly,B.J., Marynen,P., Griffin,J.D.,
            Drexler,H.G. and Gilliland,D.G.
  TITLE     The EOL-1 cell line as an in vitro model for the study of
            FIP1L1-PDGFRA-positive chronic eosinophilic leukemia
  JOURNAL   Blood 103 (7), 2802-2805 (2004)
   PUBMED   14630792
  REMARK    GeneRIF: results indicate that the fusion of FIP1L1 to PDGFRA
            occurs rarely in leukemia cell lines
REFERENCE   7  (residues 1 to 535)
  AUTHORS   Kaufmann,I., Martin,G., Friedlein,A., Langen,H. and Keller,W.
  TITLE     Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements
            and stimulates poly(A) polymerase
  JOURNAL   EMBO J 23 (3), 616-626 (2004)
   PUBMED   14749727
REFERENCE   8  (residues 1 to 535)
  AUTHORS   Pardanani,A., Ketterling,R.P., Brockman,S.R., Flynn,H.C.,
            Paternoster,S.F., Shearer,B.M., Reeder,T.L., Li,C.Y., Cross,N.C.,
            Cools,J., Gilliland,D.G., Dewald,G.W. and Tefferi,A.
  TITLE     CHIC2 deletion, a surrogate for FIP1L1-PDGFRA fusion, occurs in
            systemic mastocytosis associated with eosinophilia and predicts
            response to imatinib mesylate therapy
  JOURNAL   Blood 102 (9), 3093-3096 (2003)
   PUBMED   12842979
  REMARK    GeneRIF: observations suggest that the FIP1L1-PDGFRA rearrangement
            occurs in an early hematopoietic progenitor and suggests that the
            molecular pathogenesis for a subset of SMCD patients is similar to
            that of HES
REFERENCE   9  (residues 1 to 535)
  AUTHORS   Griffin,J.H., Leung,J., Bruner,R.J., Caligiuri,M.A. and
            Briesewitz,R.
  TITLE     Discovery of a fusion kinase in EOL-1 cells and idiopathic
            hypereosinophilic syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (13), 7830-7835 (2003)
   PUBMED   12808148
REFERENCE   10 (residues 1 to 535)
  AUTHORS   Cools,J., DeAngelo,D.J., Gotlib,J., Stover,E.H., Legare,R.D.,
            Cortes,J., Kutok,J., Clark,J., Galinsky,I., Griffin,J.D.,
            Cross,N.C., Tefferi,A., Malone,J., Alam,R., Schrier,S.L.,
            Schmid,J., Rose,M., Vandenberghe,P., Verhoef,G., Boogaerts,M.,
            Wlodarska,I., Kantarjian,H., Marynen,P., Coutre,S.E., Stone,R. and
            Gilliland,D.G.
  TITLE     A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes
            as a therapeutic target of imatinib in idiopathic hypereosinophilic
            syndrome
  JOURNAL   N Engl J Med 348 (13), 1201-1214 (2003)
   PUBMED   12660384
  REMARK    GeneRIF: The hypereosinophilic syndrome may result from a novel
            fusion tyrosine kinase - FIP1L1-PDGFRalpha - that is a consequence
            of an interstitial chromosomal deletion.
            GeneRIF: Describes the fusion gene Fip1-like-1-PDGFRalpha in
            patients with idiopathic hypereosinophilic syndrome, mostly
            responsive to imatinib therapy.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098821.3 and AC058822.6.
            
            On Nov 20, 2019 this sequence version replaced XP_005265839.1.
            
            Summary: This gene encodes a subunit of the CPSF (cleavage and
            polyadenylation specificity factor) complex that polyadenylates the
            3' end of mRNA precursors. This gene, the homolog of yeast Fip1
            (factor interacting with PAP), binds to U-rich sequences of
            pre-mRNA and stimulates poly(A) polymerase activity. Its N-terminus
            contains a PAP-binding site and its C-terminus an RNA-binding
            domain. An interstitial chromosomal deletion on 4q12 creates an
            in-frame fusion of human genes FIP1L1 and PDGFRA (platelet-derived
            growth factor receptor, alpha). The FIP1L1-PDGFRA fusion gene
            encodes a constitutively activated tyrosine kinase that joins the
            first 233 amino acids of FIP1L1 to the last 523 amino acids of
            PDGFRA. This gene fusion and chromosomal deletion is the cause of
            some forms of idiopathic hypereosinophilic syndrome (HES). This
            syndrome, recently reclassified as chronic eosinophilic leukemia
            (CEL), is responsive to treatment with tyrosine kinase inhibitors.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.838402.1,
                                           SRR11853561.22196.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..535
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     34"
                     /note="rearranged in hypereosinophilia; pre-mRNA
                     3'-end-processing factor FIP1; FIP1-like 1 protein; factor
                     interacting with PAP; FIP1 like 1; FIP1L1 cleavage and
                     polyadenylation specific factor subunit"
                     /calculated_mol_wt=59915
     Region          154..196
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     CDS             1..535
                     /gene="FIP1L1"
                     /gene_synonym="FIP1; hFip1; Rhe"
                     /coded_by="NM_001376775.1:199..1806"
                     /note="isoform 34 is encoded by transcript variant 34"
                     /db_xref="CCDS:CCDS93509.1"
                     /db_xref="GeneID:81608"
                     /db_xref="HGNC:HGNC:19124"
                     /db_xref="MIM:607686"
ORIGIN      
        1 msageverlv selsggtggd eeeewlyggp wdvhvhsdla kdldenever peeenasanp
       61 psgiedetae ngvpkpkvte teddsdsdsd ddeddvhvti gdiktgapqy gsygtapvnl
      121 niktggrvyg ttgtkvkgvd ldapgsingv pllevdldsf edkpwrkpga dlsdyfnygf
      181 nedtwkayce kqkrirmgle vipvtsttnk itvqqgrtgn seketalpst kaeftsppsl
      241 fktglppsrr lpgaidvigq titisrvegr rranensniq vlsersatev dnnfskpppf
      301 fppgappthl ppppflpppp tvstapplip ppgfppppga pppsliptie sghssgydsr
      361 sarafpygnv afphlpgsap swpslvdtsk qwdyyarrek drdrerdrdr erdrdrdrer
      421 ertrererer dhsptpsvfn sdeeryryre yaergyerhr asrekeerhr errhrekeet
      481 rhkssrsnsr rrheseegds hrrhkhkksk rskegkeags epapeqeste atpae
//
LOCUS       NP_001247431             589 aa            linear   PRI 21-NOV-2025
DEFINITION  signal recognition particle subunit SRP68 isoform 2 [Homo sapiens].
ACCESSION   NP_001247431
VERSION     NP_001247431.1
DBSOURCE    REFSEQ: accession NM_001260502.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Lim,S.H., Snider,J., Birimberg-Schwartz,L., Ip,W., Serralha,J.C.,
            Botelho,H.M., Lopes-Pacheco,M., Pinto,M.C., Moutaoufik,M.T.,
            Zilocchi,M., Laselva,O., Esmaeili,M., Kotlyar,M., Lyakisheva,A.,
            Tang,P., Lopez Vazquez,L., Akula,I., Aboualizadeh,F., Wong,V.,
            Grozavu,I., Opacak-Bernardi,T., Yao,Z., Mendoza,M., Babu,M.,
            Jurisica,I., Gonska,T., Bear,C.E., Amaral,M.D. and Stagljar,I.
  TITLE     CFTR interactome mapping using the mammalian membrane two-hybrid
            high-throughput screening system
  JOURNAL   Mol Syst Biol 18 (2), e10629 (2022)
   PUBMED   35156780
REFERENCE   4  (residues 1 to 589)
  AUTHORS   Kellogg,M.K., Miller,S.C., Tikhonova,E.B. and Karamyshev,A.L.
  TITLE     SRPassing Co-translational Targeting: The Role of the Signal
            Recognition Particle in Protein Targeting and mRNA Protection
  JOURNAL   Int J Mol Sci 22 (12), 6284 (2021)
   PUBMED   34208095
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 589)
  AUTHORS   Menichelli,E., Isel,C., Oubridge,C. and Nagai,K.
  TITLE     Protein-induced conformational changes of RNA during the assembly
            of human signal recognition particle
  JOURNAL   J Mol Biol 367 (1), 187-203 (2007)
   PUBMED   17254600
REFERENCE   6  (residues 1 to 589)
  AUTHORS   Iakhiaeva,E., Bhuiyan,S.H., Yin,J. and Zwieb,C.
  TITLE     Protein SRP68 of human signal recognition particle: identification
            of the RNA and SRP72 binding domains
  JOURNAL   Protein Sci 15 (6), 1290-1302 (2006)
   PUBMED   16672232
  REMARK    GeneRIF: The RNA binding domain of SRP68 included residues from
            positions 52 to 252. Ninety-four amino acids near the C terminus of
            SRP68 mediated the binding to SRP72
REFERENCE   7  (residues 1 to 589)
  AUTHORS   Harada,H., Nagai,H., Mine,N., Terada,Y., Fujiwara,H., Mikami,I.,
            Tsuneizumi,M., Yabe,A., Miyazaki,K., Yokota,T., Imoto,I.,
            Inazawa,J. and Emi,M.
  TITLE     Molecular cloning, tissue expression, and chromosomal assignment of
            a novel gene encoding a subunit of the human signal-recognition
            particle
  JOURNAL   J Hum Genet 46 (2), 70-75 (2001)
   PUBMED   11281415
REFERENCE   8  (residues 1 to 589)
  AUTHORS   Politz,J.C., Yarovoi,S., Kilroy,S.M., Gowda,K., Zwieb,C. and
            Pederson,T.
  TITLE     Signal recognition particle components in the nucleolus
  JOURNAL   Proc Natl Acad Sci U S A 97 (1), 55-60 (2000)
   PUBMED   10618370
REFERENCE   9  (residues 1 to 589)
  AUTHORS   Larsen,N., Samuelsson,T. and Zwieb,C.
  TITLE     The Signal Recognition Particle Database (SRPDB)
  JOURNAL   Nucleic Acids Res 26 (1), 177-178 (1998)
   PUBMED   9399828
REFERENCE   10 (residues 1 to 589)
  AUTHORS   Lutcke,H., Prehn,S., Ashford,A.J., Remus,M., Frank,R. and
            Dobberstein,B.
  TITLE     Assembly of the 68- and 72-kD proteins of signal recognition
            particle with 7S RNA
  JOURNAL   J Cell Biol 121 (5), 977-985 (1993)
   PUBMED   8388879
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU137443.1, AK126258.1,
            DQ786315.1 and DB315535.1.
            
            Summary: This gene encodes a subunit of the signal recognition
            particle (SRP). The SRP is a ribonucleoprotein complex that
            transports secreted and membrane proteins to the endoplasmic
            reticulum for processing. The complex includes a 7S RNA and six
            protein subunits. The encoded protein is the 68kDa component of the
            SRP, and forms a heterodimer with the 72kDa subunit that is
            required for SRP function. Alternatively spliced transcript
            variants encoding multiple isoforms have been observed for this
            gene, and three pseudogenes of this gene are located within the
            Smith-Magenis syndrome region on chromosome 17. [provided by
            RefSeq, May 2012].
            
            Transcript Variant: This variant (2) lacks an exon in the 5' coding
            region, but maintains the reading frame, compared to variant 1. The
            encoded isoform (2) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK126258.1, SRR14038197.1338822.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..589
                     /product="signal recognition particle subunit SRP68
                     isoform 2"
                     /note="signal recognition particle 68 kDa protein; signal
                     recognition particle 68kDa; signal recognition particle
                     subunit SRP68"
                     /calculated_mol_wt=65977
     Region          75..560
                     /region_name="SRP68"
                     /note="RNA-binding signal recognition particle 68;
                     pfam16969"
                     /db_xref="CDD:465323"
     CDS             1..589
                     /gene="SRP68"
                     /gene_synonym="SCN10"
                     /coded_by="NM_001260502.2:27..1796"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58601.1"
                     /db_xref="GeneID:6730"
                     /db_xref="HGNC:HGNC:11302"
                     /db_xref="MIM:604858"
ORIGIN      
        1 maaekqvpgg gggggsgggg gsggggsggg rgaggeenke nerpsagska nkefgdslsl
       61 eilqiikesq qqhglrhgdf qryrylllvl mdaerawsya mqlkqeante prkrfhllsr
      121 lrkavkhaee lerlcesnrv daktkleaqa ytaylsgmlr fehqewkaai eafnkcktiy
      181 eklasaftee qavlynqrve eispniryca ynigdqsain elmqmrlrsg gtegllaekl
      241 ealitqtrak qaatmsevew rgrtvpvkid kvrifllgla dneaaivqae seetkerlfe
      301 smlsecrdai qvvreelkpd qkqrdyileg epgkvsnlqy lhsyltyikl staikrnenm
      361 akglqrallq qqpeddskrs prpqdlirly diilqnlvel lqlpgleedk afqkeiglkt
      421 lvfkayrcff iaqsyvlvkk wsealvlydr vlkyanevns dagafknslk dlpdvqelit
      481 qvrsekcslq aaaildanda hqtetsssqv kdnkplverf etfcldpslv tkqanlvhfp
      541 pgfqpipckp lffdlalnhv afppledkle qktksgltgy ikgifgfrs
//
LOCUS       NP_001350388             427 aa            linear   PRI 21-NOV-2025
DEFINITION  cerebral cavernous malformations 2 protein isoform 6 [Homo
            sapiens].
ACCESSION   NP_001350388 XP_011513866
VERSION     NP_001350388.1
DBSOURCE    REFSEQ: accession NM_001363459.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Chaussenot,A., Ayrignac,X., Chatron,N., Granchon-Riolzir,T.,
            Labauge,P., Tournier-Lasserve,E. and Riant,F.
  TITLE     Loss of heterozygosity in CCM2 cDNA revealing a structural variant
            causing multiple cerebral cavernous malformations
  JOURNAL   Eur J Hum Genet 32 (7), 876-878 (2024)
   PUBMED   38755314
  REMARK    GeneRIF: Loss of heterozygosity in CCM2 cDNA revealing a structural
            variant causing multiple cerebral cavernous malformations.
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Gallione,C.J., Detter,M.R., Sheline,A., Christmas,H.M., Lee,C. and
            Marchuk,D.A.
  TITLE     Genetic genealogy uncovers a founder deletion mutation in the
            cerebral cavernous malformations 2 gene
  JOURNAL   Hum Genet 141 (11), 1761-1769 (2022)
   PUBMED   35488064
  REMARK    GeneRIF: Genetic genealogy uncovers a founder deletion mutation in
            the cerebral cavernous malformations 2 gene.
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Wan,D., Gong,Y., Qin,W., Zhang,P., Li,J., Wei,L., Zhou,X., Li,H.,
            Qiu,X., Zhong,F., He,L., Yu,J., Yao,G., Jiang,H., Qian,L., Yu,Y.,
            Shu,H., Chen,X., Xu,H., Guo,M., Pan,Z., Chen,Y., Ge,C., Yang,S. and
            Gu,J.
  TITLE     Large-scale cDNA transfection screening for genes related to cancer
            development and progression
  JOURNAL   Proc Natl Acad Sci U S A 101 (44), 15724-15729 (2004)
   PUBMED   15498874
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 Dec 14:101(50):17565]
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Denier,C., Goutagny,S., Labauge,P., Krivosic,V., Arnoult,M.,
            Cousin,A., Benabid,A.L., Comoy,J., Frerebeau,P., Gilbert,B.,
            Houtteville,J.P., Jan,M., Lapierre,F., Loiseau,H., Menei,P.,
            Mercier,P., Moreau,J.J., Nivelon-Chevallier,A., Parker,F.,
            Redondo,A.M., Scarabin,J.M., Tremoulet,M., Zerah,M., Maciazek,J.
            and Tournier-Lasserve,E.
  CONSRTM   Societe Francaise de Neurochirurgie
  TITLE     Mutations within the MGC4607 gene cause cerebral cavernous
            malformations
  JOURNAL   Am J Hum Genet 74 (2), 326-337 (2004)
   PUBMED   14740320
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Liquori,C.L., Berg,M.J., Siegel,A.M., Huang,E., Zawistowski,J.S.,
            Stoffer,T., Verlaan,D., Balogun,F., Hughes,L., Leedom,T.P.,
            Plummer,N.W., Cannella,M., Maglione,V., Squitieri,F., Johnson,E.W.,
            Rouleau,G.A., Ptacek,L. and Marchuk,D.A.
  TITLE     Mutations in a gene encoding a novel protein containing a
            phosphotyrosine-binding domain cause type 2 cerebral cavernous
            malformations
  JOURNAL   Am J Hum Genet 73 (6), 1459-1464 (2003)
   PUBMED   14624391
  REMARK    GeneRIF: MGC4607 encodes a protein with a phosphotyrosine-binding
            domain that may be part of the complex pathway of integrin
            signaling that, when perturbed, causes abnormal vascular
            morphogenesis in the brain, leading to CCM formation.
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Craig,H.D., Gunel,M., Cepeda,O., Johnson,E.W., Ptacek,L.,
            Steinberg,G.K., Ogilvy,C.S., Berg,M.J., Crawford,S.C., Scott,R.M.,
            Steichen-Gersdorf,E., Sabroe,R., Kennedy,C.T., Mettler,G.,
            Beis,M.J., Fryer,A., Awad,I.A. and Lifton,R.P.
  TITLE     Multilocus linkage identifies two new loci for a mendelian form of
            stroke, cerebral cavernous malformation, at 7p15-13 and 3q25.2-27
  JOURNAL   Hum Mol Genet 7 (12), 1851-1858 (1998)
   PUBMED   9811928
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF370392.1, CV571060.1,
            HY347636.1, AC013416.4, AK098005.1 and BC004903.2.
            
            On May 19, 2018 this sequence version replaced XP_011513866.1.
            
            Summary: This gene encodes a scaffold protein that functions in the
            stress-activated p38 Mitogen-activated protein kinase (MAPK)
            signaling cascade. The protein interacts with SMAD specific E3
            ubiquitin protein ligase 1 (also known as SMURF1) via a
            phosphotyrosine binding domain to promote RhoA degradation. The
            protein is required for normal cytoskeletal structure, cell-cell
            interactions, and lumen formation in endothelial cells. Mutations
            in this gene result in cerebral cavernous malformations. Multiple
            transcript variants encoding different isoforms have been found for
            this gene.[provided by RefSeq, Nov 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.508219.1,
                                           SRR3476690.228964.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..427
                     /product="cerebral cavernous malformations 2 protein
                     isoform 6"
                     /note="malcavernin; cerebral cavernous malformations 2
                     protein; cerebral cavernous malformation 2; osmosensing
                     scaffold for MEKK3; CCM2 scaffolding protein"
                     /calculated_mol_wt=46445
     Region          10..179
                     /region_name="PTB_CCM2"
                     /note="Cerebral cavernous malformation 2 FERM domain
                     C-lobe; cd13166"
                     /db_xref="CDD:269987"
     Site            order(57,64..67)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269987"
     Site            order(265..269,273..274,276,279..280,282..283,286,299,302,
                     305..307,309..310)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:259825"
     Region          270..364
                     /region_name="CCM2_C"
                     /note="Cerebral cavernous malformation protein,
                     harmonin-homology; pfam16545"
                     /db_xref="CDD:435415"
     CDS             1..427
                     /gene="CCM2"
                     /gene_synonym="C7orf22; OSM; PP10187"
                     /coded_by="NM_001363459.2:134..1417"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="GeneID:83605"
                     /db_xref="HGNC:HGNC:21708"
                     /db_xref="MIM:607929"
ORIGIN      
        1 meeegkkgkk ylgqltsipg ylnpssrtei lhfidnakra hqlpghltqe hdavlslsay
       61 nvklawrdge diilrvpihd iaavsyvrdd aahlvvlkta qdpgispsqs lcaessrgls
      121 agslsesavg pveacclvil aaeskvaaee lccllgqvfq vvytestidf ldraifdgas
      181 tpthhlslhs ashvtsstvt ssfdcqlplh frtlaitlsp pkfsrvislf qddsstkvdi
      241 ketyeveast fcfpesvdvg gasphsktis eselsasate llqdymltlr tklssqeiqq
      301 faallheyrn gasihefcin lrqlygdsrk flllglrpfi pekdsqhfen fletigvkdg
      361 rgiitdsfgr hrralsttss sttngnratg ssddrsapse gdewdrmisd issdiealgc
      421 smdqdsa
//
LOCUS       NP_001339322             514 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase 33 isoform a [Homo sapiens].
ACCESSION   NP_001339322 XP_011518596
VERSION     NP_001339322.1
DBSOURCE    REFSEQ: accession NM_001352393.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Yu,W., Li,Y., Chen,H., Cui,Y., Situ,C., Yao,L., Zhang,X., Lu,S.,
            Liu,L., Li,L., Ren,J., Guo,Y., Huo,Z., Chen,Y., Li,H., Jiang,T.,
            Gu,Y., Wang,C., Zhu,T., Li,Y., Hu,Z. and Guo,X.
  TITLE     STK33 Phosphorylates Fibrous Sheath Protein AKAP3/4 to Regulate
            Sperm Flagella Assembly in Spermiogenesis
  JOURNAL   Mol Cell Proteomics 22 (6), 100564 (2023)
   PUBMED   37146716
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Li,X., Lin,M., Liu,M., Ye,H. and Qin,S.
  TITLE     Interaction between STK33 and autophagy promoted renal cell
            carcinoma metastasis by regulating mTOR/ULK1 signaling pathway
  JOURNAL   Mol Biol Rep 50 (6), 5059-5067 (2023)
   PUBMED   37101009
  REMARK    GeneRIF: Interaction between STK33 and autophagy promoted renal
            cell carcinoma metastasis by regulating mTOR/ULK1 signaling
            pathway.
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Ma,H., Zhang,B., Khan,A., Zhao,D., Ma,A., Zhou,J., Khan,I.,
            Khan,K., Zhang,H., Zhang,Y., Jiang,X., Dil,S., Zeb,A., Rahim,F. and
            Shi,Q.
  TITLE     Novel frameshift mutation in STK33 is associated with
            asthenozoospermia and multiple morphological abnormalities of the
            flagella
  JOURNAL   Hum Mol Genet 30 (21), 1977-1984 (2021)
   PUBMED   34155512
  REMARK    GeneRIF: Novel frameshift mutation in STK33 is associated with
            asthenozoospermia and multiple morphological abnormalities of the
            flagella.
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Xie,Y., Lv,X., Ni,D., Liu,J., Hu,Y., Liu,Y., Liu,Y., Liu,R.,
            Zhao,H., Lu,Z. and Zhou,Q.
  TITLE     HPD degradation regulated by the TTC36-STK33-PELI1 signaling axis
            induces tyrosinemia and neurological damage
  JOURNAL   Nat Commun 10 (1), 4266 (2019)
   PUBMED   31537781
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Zhang,S., Wu,H., Wang,K. and Liu,M.
  TITLE     STK33/ERK2 signal pathway contribute the tumorigenesis of
            colorectal cancer HCT15 cells
  JOURNAL   Biosci Rep 39 (3) (2019)
   PUBMED   30760631
  REMARK    GeneRIF: Data show that serine/threonine kinase 33 (STK33) can bind
            with extracellular signal-regulated kinase 2 (ERK2) and take part
            in the regulation of ERKs signaling pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Melen,E., Himes,B.E., Brehm,J.M., Boutaoui,N., Klanderman,B.J.,
            Sylvia,J.S. and Lasky-Su,J.
  TITLE     Analyses of shared genetic factors between asthma and obesity in
            children
  JOURNAL   J Allergy Clin Immunol 126 (3), 631-7 (2010)
   PUBMED   20816195
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Willer,C.J., Speliotes,E.K., Loos,R.J., Li,S., Lindgren,C.M.,
            Heid,I.M., Berndt,S.I., Elliott,A.L., Jackson,A.U., Lamina,C.,
            Lettre,G., Lim,N., Lyon,H.N., McCarroll,S.A., Papadakis,K., Qi,L.,
            Randall,J.C., Roccasecca,R.M., Sanna,S., Scheet,P., Weedon,M.N.,
            Wheeler,E., Zhao,J.H., Jacobs,L.C., Prokopenko,I., Soranzo,N.,
            Tanaka,T., Timpson,N.J., Almgren,P., Bennett,A., Bergman,R.N.,
            Bingham,S.A., Bonnycastle,L.L., Brown,M., Burtt,N.P., Chines,P.,
            Coin,L., Collins,F.S., Connell,J.M., Cooper,C., Smith,G.D.,
            Dennison,E.M., Deodhar,P., Elliott,P., Erdos,M.R., Estrada,K.,
            Evans,D.M., Gianniny,L., Gieger,C., Gillson,C.J., Guiducci,C.,
            Hackett,R., Hadley,D., Hall,A.S., Havulinna,A.S., Hebebrand,J.,
            Hofman,A., Isomaa,B., Jacobs,K.B., Johnson,T., Jousilahti,P.,
            Jovanovic,Z., Khaw,K.T., Kraft,P., Kuokkanen,M., Kuusisto,J.,
            Laitinen,J., Lakatta,E.G., Luan,J., Luben,R.N., Mangino,M.,
            McArdle,W.L., Meitinger,T., Mulas,A., Munroe,P.B., Narisu,N.,
            Ness,A.R., Northstone,K., O'Rahilly,S., Purmann,C., Rees,M.G.,
            Ridderstrale,M., Ring,S.M., Rivadeneira,F., Ruokonen,A.,
            Sandhu,M.S., Saramies,J., Scott,L.J., Scuteri,A., Silander,K.,
            Sims,M.A., Song,K., Stephens,J., Stevens,S., Stringham,H.M.,
            Tung,Y.C., Valle,T.T., Van Duijn,C.M., Vimaleswaran,K.S.,
            Vollenweider,P., Waeber,G., Wallace,C., Watanabe,R.M.,
            Waterworth,D.M., Watkins,N., Witteman,J.C., Zeggini,E., Zhai,G.,
            Zillikens,M.C., Altshuler,D., Caulfield,M.J., Chanock,S.J.,
            Farooqi,I.S., Ferrucci,L., Guralnik,J.M., Hattersley,A.T., Hu,F.B.,
            Jarvelin,M.R., Laakso,M., Mooser,V., Ong,K.K., Ouwehand,W.H.,
            Salomaa,V., Samani,N.J., Spector,T.D., Tuomi,T., Tuomilehto,J.,
            Uda,M., Uitterlinden,A.G., Wareham,N.J., Deloukas,P.,
            Frayling,T.M., Groop,L.C., Hayes,R.B., Hunter,D.J., Mohlke,K.L.,
            Peltonen,L., Schlessinger,D., Strachan,D.P., Wichmann,H.E.,
            McCarthy,M.I., Boehnke,M., Barroso,I., Abecasis,G.R. and
            Hirschhorn,J.N.
  CONSRTM   Wellcome Trust Case Control Consortium; Genetic Investigation of
            ANthropometric Traits Consortium
  TITLE     Six new loci associated with body mass index highlight a neuronal
            influence on body weight regulation
  JOURNAL   Nat Genet 41 (1), 25-34 (2009)
   PUBMED   19079261
REFERENCE   8  (residues 1 to 514)
  AUTHORS   Mujica,A.O., Brauksiepe,B., Saaler-Reinhardt,S., Reuss,S. and
            Schmidt,E.R.
  TITLE     Differential expression pattern of the novel serine/threonine
            kinase, STK33, in mice and men
  JOURNAL   FEBS J 272 (19), 4884-4898 (2005)
   PUBMED   16176263
  REMARK    GeneRIF: STK33/Stk33 expression pattern resembles those of some
            related members of the calcium/calmodulin dependent kinase group
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Mujica,A.O., Hankeln,T. and Schmidt,E.R.
  TITLE     A novel serine/threonine kinase gene, STK33, on human chromosome
            11p15.3
  JOURNAL   Gene 280 (1-2), 175-181 (2001)
   PUBMED   11738831
REFERENCE   10 (residues 1 to 514)
  AUTHORS   Amid,C., Bahr,A., Mujica,A., Sampson,N., Bikar,S.E.,
            Winterpacht,A., Zabel,B., Hankeln,T. and Schmidt,E.R.
  TITLE     Comparative genomic sequencing reveals a strikingly similar
            architecture of a conserved syntenic region on human chromosome
            11p15.3 (including gene ST5) and mouse chromosome 7
  JOURNAL   Cytogenet Cell Genet 93 (3-4), 284-290 (2001)
   PUBMED   11528127
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104360.8 and AC105357.7.
            
            On Jun 13, 2017 this sequence version replaced XP_011518596.1.
            
            Transcript Variant: This variant (11), as well as variants 1 and
            4-10, encodes isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4643878.72872.1,
                                           ERR4643830.4689954.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..514
                     /product="serine/threonine-protein kinase 33 isoform a"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase 33"
                     /calculated_mol_wt=57700
     Region          65..91
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYT3.1)"
     Region          114..381
                     /region_name="STKc_STK33"
                     /note="Catalytic domain of Serine/Threonine Kinase 33;
                     cd14097"
                     /db_xref="CDD:270999"
     Site            order(122..126,130,143,145,176,192..195,199,201,237..238,
                     240,242..243,245,264..265,268,284..288,290)
                     /site_type="active"
                     /db_xref="CDD:270999"
     Site            order(122..125,130,143,145,176,192..195,199,242..243,245,
                     264..265)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270999"
     Site            order(126,199,201,237..238,240,242,268,284..288,290)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270999"
     Site            order(264..278,280..288)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270999"
     Region          402..468
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYT3.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q924X7; propagated from
                     UniProtKB/Swiss-Prot (Q9BYT3.1)"
     Region          485..514
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYT3.1)"
     CDS             1..514
                     /gene="STK33"
                     /gene_synonym="SPGF93"
                     /coded_by="NM_001352393.2:308..1852"
                     /note="isoform a is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS7789.1"
                     /db_xref="GeneID:65975"
                     /db_xref="HGNC:HGNC:14568"
                     /db_xref="MIM:607670"
ORIGIN      
        1 madsgldkks tkcpdcssas qkdvlcvcss ktrvppvlvv emsqtssigs aeslislerk
       61 kekninrdit srkdlpsrts nverkasqqq wgrgnftegk vphirienga aieeiytfgr
      121 ilgkgsfgiv ieatdketet kwaikkvnke kagssavkll erevnilksv khehiihleq
      181 vfetpkkmyl vmelcedgel keildrkghf senetrwiiq slasaiaylh nndivhrdlk
      241 lenimvkssl iddnneinln ikvtdfglav kkqsrseaml qatcgtpiym apevisahdy
      301 sqqcdiwsig vvmymllrge ppflasseek lfelirkgel hfenavwnsi sdcaksvlkq
      361 lmkvdpahri takelldnqw ltgnklssvr ptnvlemmke wknnpesvee ntteeknkps
      421 teeklksyqp wgnvpdanyt sdeeeekqst ayekqfpats kdnfdmcsss ftsskllpae
      481 ikgemektpv tpsqgtatky paksgalsrt kkkl
//
LOCUS       NP_004011               1115 aa            linear   PRI 21-NOV-2025
DEFINITION  dystrophin isoform Dp140c [Homo sapiens].
ACCESSION   NP_004011
VERSION     NP_004011.3
DBSOURCE    REFSEQ: accession NM_004020.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Chen,L., Luo,X., Wang,H., Tian,Y. and Liu,Y.
  TITLE     Identifying inversions with breakpoints in the Dystrophin gene
            through long-read sequencing: report of two cases
  JOURNAL   BMC Med Genomics 17 (1), 227 (2024)
   PUBMED   39251998
  REMARK    GeneRIF: Identifying inversions with breakpoints in the Dystrophin
            gene through long-read sequencing: report of two cases.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Davies,K.E. and Vogt,J.
  TITLE     Long-term clinical follow-up of a family with Becker muscular
            dystrophy associated with a large deletion in the DMD gene
  JOURNAL   Neuromuscul Disord 39, 5-9 (2024)
   PUBMED   38653179
  REMARK    GeneRIF: Long-term clinical follow-up of a family with Becker
            muscular dystrophy associated with a large deletion in the DMD
            gene.
            Erratum:[Neuromuscul Disord. 2024 Jun;39:54. doi:
            10.1016/j.nmd.2024.05.010. PMID: 38801812]
REFERENCE   4  (residues 1 to 1115)
  AUTHORS   Achermann,J.C. and Vilain,E.J.
  TITLE     NR0B1-Related Adrenal Hypoplasia Congenita
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301604
REFERENCE   5  (residues 1 to 1115)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   6  (residues 1 to 1115)
  AUTHORS   Darras,B.T., Urion,D.K. and Ghosh,P.S.
  TITLE     Dystrophinopathies
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301298
REFERENCE   7  (residues 1 to 1115)
  AUTHORS   Nigro,V., Politano,L., Nigro,G., Romano,S.C., Molinari,A.M. and
            Puca,G.A.
  TITLE     Detection of a nonsense mutation in the dystrophin gene by multiple
            SSCP
  JOURNAL   Hum Mol Genet 1 (7), 517-520 (1992)
   PUBMED   1307253
REFERENCE   8  (residues 1 to 1115)
  AUTHORS   Gorecki,D.C., Monaco,A.P., Derry,J.M., Walker,A.P., Barnard,E.A.
            and Barnard,P.J.
  TITLE     Expression of four alternative dystrophin transcripts in brain
            regions regulated by different promoters
  JOURNAL   Hum Mol Genet 1 (7), 505-510 (1992)
   PUBMED   1307251
REFERENCE   9  (residues 1 to 1115)
  AUTHORS   Lederfein,D., Levy,Z., Augier,N., Mornet,D., Morris,G., Fuchs,O.,
            Yaffe,D. and Nudel,U.
  TITLE     A 71-kilodalton protein is a major product of the Duchenne muscular
            dystrophy gene in brain and other nonmuscle tissues
  JOURNAL   Proc Natl Acad Sci U S A 89 (12), 5346-5350 (1992)
   PUBMED   1319059
REFERENCE   10 (residues 1 to 1115)
  AUTHORS   Koenig,M., Monaco,A.P. and Kunkel,L.M.
  TITLE     The complete sequence of dystrophin predicts a rod-shaped
            cytoskeletal protein
  JOURNAL   Cell 53 (2), 219-228 (1988)
   PUBMED   3282674
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078957.16, AC093193.11,
            AC079864.22, AC093167.11, AC079175.24, AC079177.21, AC090632.13,
            AC078958.30, AC079143.17 and AC006061.1.
            
            On Aug 14, 2020 this sequence version replaced NP_004011.2.
            
            Summary: This gene spans a genomic range of greater than 2 Mb and
            encodes a large protein containing an N-terminal actin-binding
            domain and multiple spectrin repeats. The encoded protein forms a
            component of the dystrophin-glycoprotein complex (DGC), which
            bridges the inner cytoskeleton and the extracellular matrix.
            Deletions, duplications, and point mutations at this gene locus may
            cause Duchenne muscular dystrophy (DMD), Becker muscular dystrophy
            (BMD), or cardiomyopathy. Alternative promoter usage and
            alternative splicing result in numerous distinct transcript
            variants and protein isoforms for this gene. [provided by RefSeq,
            Dec 2016].
            
            Transcript Variant: Dp140 transcripts use exons 45-79, starting at
            a promoter/exon 1 located in intron 44. Dp140 transcripts have a
            long (1 kb) 5' UTR since translation is initiated in exon 51
            (corresponding to aa 2461 of dystrophin). In addition to the
            alternative promoter and exon 1, differential splicing of exons
            71-74 and 78 produces at least five Dp140 isoforms. Of these, this
            transcript (Dp140c) lacks exons 71-74.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.194609.1,
                                           SRR1803612.148053.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp21.2-p21.1"
     Protein         1..1115
                     /product="dystrophin isoform Dp140c"
                     /note="mutant dystrophin"
                     /calculated_mol_wt=128847
     Region          <1..580
                     /region_name="central rod domain"
     Region          <1..10
                     /region_name="hinge region 3"
     Region          11..117
                     /region_name="repeat region 20"
     Region          12..228
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          118..226
                     /region_name="repeat region 21"
     Site            118..123
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          227..342
                     /region_name="repeat region 22"
     Region          230..473
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          343..471
                     /region_name="repeat region 23"
     Site            343..348
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          472..580
                     /region_name="repeat region 24"
     Region          474..580
                     /region_name="Spectrin"
                     /note="Spectrin repeat; pfam00435"
                     /db_xref="CDD:395348"
     Region          554..652
                     /region_name="hinge region 4"
     Site            581..585
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          596..632
                     /region_name="WW-domain"
     Region          599..628
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(612,623)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          640..840
                     /region_name="Cysteine-rich domain"
     Region          665..826
                     /region_name="EFh_DMD"
                     /note="EF-hand-like motif found in dystrophin; cd16246"
                     /db_xref="CDD:320004"
     Site            order(665..666,668..669,687,691,695,697..698,701,712..718,
                     720..721,724,730,743,784..785,787)
                     /site_type="other"
                     /note="Domain interface"
                     /db_xref="CDD:320004"
     Region          665..704
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          670..697
                     /region_name="EF-hand 1"
     Region          711..745
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          718..746
                     /region_name="EF-hand 2"
     Site            728..730
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:320004"
     Region          751..787
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          800..826
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          840..1115
                     /region_name="Carboxy-terminal region"
     Region          847..894
                     /region_name="ZZ-domain"
     Region          851..899
                     /region_name="ZZ_dystrophin"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     dystrophin and dystrobrevin. The ZZ motif coordinates two
                     zinc ions and most likely participates in ligand binding
                     or molecular scaffolding. Dystrophin attaches actin
                     filaments to an integral membrane...; cd02334"
                     /db_xref="CDD:239074"
     Site            order(853,856,868,871,877,880,890,894)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(853,856,877,880)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(854,865,867,873,875)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(866,881,896,899)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(868,871,890,894)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239074"
     Region          988..1023
                     /region_name="(Leu)6-heptad repeat"
     CDS             1..1115
                     /gene="DMD"
                     /gene_synonym="BMD; CMD3B; DXS142; DXS164; DXS206; DXS230;
                     DXS239; DXS268; DXS269; DXS270; DXS272; MRX85"
                     /coded_by="NM_004020.4:1042..4389"
                     /note="isoform Dp140c is encoded by transcript variant
                     Dp140c"
                     /db_xref="CCDS:CCDS55394.1"
                     /db_xref="GeneID:1756"
                     /db_xref="HGNC:HGNC:2928"
                     /db_xref="MIM:300377"
ORIGIN      
        1 mpsslmlevp aladfnrawt eltdwlslld qviksqrvmv gdledinemi ikqkatmqdl
       61 eqrrpqleel itaaqnlknk tsnqeartii tdrieriqnq wdevqehlqn rrqqlnemlk
      121 dstqwleake eaeqvlgqar akleswkegp ytvdaiqkki tetkqlakdl rqwqtnvdva
      181 ndlalkllrd ysaddtrkvh miteninasw rsihkrvser eaaleethrl lqqfpldlek
      241 flawlteaet tanvlqdatr kerlledskg vkelmkqwqd lqgeieahtd vyhnldensq
      301 kilrslegsd davllqrrld nmnfkwselr kkslnirshl eassdqwkrl hlslqellvw
      361 lqlkddelsr qapiggdfpa vqkqndvhra fkrelktkep vimstletvr iflteqpleg
      421 leklyqepre lppeeraqnv trllrkqaee vnteweklnl hsadwqrkid etlerlrelq
      481 eatdeldlkl rqaevikgsw qpvgdllids lqdhlekvka lrgeiaplke nvshvndlar
      541 qlttlgiqls pynlstledl ntrwkllqva vedrvrqlhe ahrdfgpasq hflstsvqgp
      601 weraispnkv pyyinhetqt tcwdhpkmte lyqsladlnn vrfsayrtam klrrlqkalc
      661 ldllslsaac daldqhnlkq ndqpmdilqi inclttiydr leqehnnlvn vplcvdmcln
      721 wllnvydtgr tgrirvlsfk tgiislckah ledkyrylfk qvasstgfcd qrrlglllhd
      781 siqiprqlge vasfggsnie psvrscfqfa nnkpeieaal fldwmrlepq smvwlpvlhr
      841 vaaaetakhq akcnickecp iigfryrslk hfnydicqsc ffsgrvakgh kmhypmveyc
      901 tpttsgedvr dfakvlknkf rtkryfakhp rmgylpvqtv legdnmetnl qaeydrlkqq
      961 hehkglsplp sppemmptsp qsprdaelia eakllrqhkg rlearmqile dhnkqlesql
     1021 hrlrqlleqp qaeakvngtt vsspstslqr sdssqpmllr vvgsqtsdsm geedllsppq
     1081 dtstgleevm eqlnnsfpss rgrntpgkpm redtm
//
LOCUS       NP_001307644             222 aa            linear   PRI 21-NOV-2025
DEFINITION  B-cell lymphoma/leukemia 10 isoform 2 [Homo sapiens].
ACCESSION   NP_001307644 XP_005271368
VERSION     NP_001307644.1
DBSOURCE    REFSEQ: accession NM_001320715.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Kowluru,A.
  TITLE     Regulatory roles of CARD9-BCL10-Rac1 (CBR) signalome in islet
            beta-cell function in health and metabolic stress: Is there room
            for MALT1?
  JOURNAL   Biochem Pharmacol 218, 115889 (2023)
   PUBMED   37991197
  REMARK    GeneRIF: Regulatory roles of CARD9-BCL10-Rac1 (CBR) signalome in
            islet beta-cell function in health and metabolic stress: Is there
            room for MALT1?
            Review article
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Plaisance,I., Chouvardas,P., Sun,Y., Nemir,M., Aghagolzadeh,P.,
            Aminfar,F., Shen,S., Shim,W.J., Rochais,F., Johnson,R., Palpant,N.
            and Pedrazzini,T.
  TITLE     A transposable element into the human long noncoding RNA CARMEN is
            a switch for cardiac precursor cell specification
  JOURNAL   Cardiovasc Res 119 (6), 1361-1376 (2023)
   PUBMED   36537036
  REMARK    GeneRIF: A transposable element into the human long noncoding RNA
            CARMEN is a switch for cardiac precursor cell specification.
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Al-Tamemi,S., Alhinai,Z., Al-Rahbi,N., Al-Abdawani,R.,
            Al-Yazidi,L., Al-Shekaili,J., Al-Kindi,M. and Al-Maawali,A.
  TITLE     BCL10 loss-of-function novel mutation leading to atypical severe
            combined immunodeficiency
  JOURNAL   Clin Immunol 241, 109067 (2022)
   PUBMED   35750252
  REMARK    GeneRIF: BCL10 loss-of-function novel mutation leading to atypical
            severe combined immunodeficiency.
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Rodriguez Gama,A., Miller,T., Lange,J.J., Unruh,J.R. and
            Halfmann,R.
  TITLE     A nucleation barrier spring-loads the CBM signalosome for binary
            activation
  JOURNAL   Elife 11, e79826 (2022)
   PUBMED   35727133
  REMARK    GeneRIF: A nucleation barrier spring-loads the CBM signalosome for
            binary activation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 222)
  AUTHORS   Yan,M., Lee,J., Schilbach,S., Goddard,A. and Dixit,V.
  TITLE     mE10, a novel caspase recruitment domain-containing proapoptotic
            molecule
  JOURNAL   J Biol Chem 274 (15), 10287-10292 (1999)
   PUBMED   10187815
REFERENCE   7  (residues 1 to 222)
  AUTHORS   Thome,M., Martinon,F., Hofmann,K., Rubio,V., Steiner,V.,
            Schneider,P., Mattmann,C. and Tschopp,J.
  TITLE     Equine herpesvirus-2 E10 gene product, but not its cellular
            homologue, activates NF-kappaB transcription factor and c-Jun
            N-terminal kinase
  JOURNAL   J Biol Chem 274 (15), 9962-9968 (1999)
   PUBMED   10187771
REFERENCE   8  (residues 1 to 222)
  AUTHORS   Koseki,T., Inohara,N., Chen,S., Carrio,R., Merino,J.,
            Hottiger,M.O., Nabel,G.J. and Nunez,G.
  TITLE     CIPER, a novel NF kappaB-activating protein containing a caspase
            recruitment domain with homology to Herpesvirus-2 protein E10
  JOURNAL   J Biol Chem 274 (15), 9955-9961 (1999)
   PUBMED   10187770
REFERENCE   9  (residues 1 to 222)
  AUTHORS   Willis,T.G., Jadayel,D.M., Du,M.Q., Peng,H., Perry,A.R.,
            Abdul-Rauf,M., Price,H., Karran,L., Majekodunmi,O., Wlodarska,I.,
            Pan,L., Crook,T., Hamoudi,R., Isaacson,P.G. and Dyer,M.J.
  TITLE     Bcl10 is involved in t(1;14)(p22;q32) of MALT B cell lymphoma and
            mutated in multiple tumor types
  JOURNAL   Cell 96 (1), 35-45 (1999)
   PUBMED   9989495
REFERENCE   10 (residues 1 to 222)
  AUTHORS   Lee,W.C., Balsara,B., Liu,Z., Jhanwar,S.C. and Testa,J.R.
  TITLE     Loss of heterozygosity analysis defines a critical region in
            chromosome 1p22 commonly deleted in human malignant mesothelioma
  JOURNAL   Cancer Res 56 (19), 4297-4301 (1996)
   PUBMED   8813110
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590113.8, EF189176.1 and
            CA420027.1.
            
            On Mar 3, 2016 this sequence version replaced XP_005271368.1.
            
            Summary: This gene was identified by its translocation in a case of
            mucosa-associated lymphoid tissue (MALT) lymphoma. The protein
            encoded by this gene contains a caspase recruitment domain (CARD),
            and has been shown to induce apoptosis and to activate NF-kappaB.
            This protein is reported to interact with other CARD domain
            containing proteins including CARD9, 10, 11 and 14, which are
            thought to function as upstream regulators in NF-kappaB signaling.
            This protein is found to form a complex with MALT1, a protein
            encoded by another gene known to be translocated in MALT lymphoma.
            MALT1 and this protein are thought to synergize in the activation
            of NF-kappaB, and the deregulation of either of them may contribute
            to the same pathogenetic process that leads to the malignancy.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region, compared to variant 1. This
            results in a shorter protein (isoform 2), compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR6380200.139358.9,
                                           SRR6380200.139358.19 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267760 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.3"
     Protein         1..222
                     /product="B-cell lymphoma/leukemia 10 isoform 2"
                     /note="CARD-containing apoptotic signaling protein; CARD
                     containing molecule enhancing NF-kB; caspase-recruiting
                     domain-containing protein; CARD-containing proapoptotic
                     protein; B-cell lymphoma/leukemia 10; hCLAP; cCARMEN;
                     cellular-E10; cellular homolog of vCARMEN; CARD-containing
                     molecule enhancing NF-kappa-B; mammalian CARD-containing
                     adapter molecule E10; CED-3/ICH-1 prodomain homologous
                     E10-like regulator; B cell CLL/lymphoma 10"
                     /calculated_mol_wt=24971
     Region          17..100
                     /region_name="CARD_BCL10"
                     /note="Caspase activation and recruitment domain of B-cell
                     lymphoma 10; cd08810"
                     /db_xref="CDD:260072"
     CDS             1..222
                     /gene="BCL10"
                     /gene_synonym="c-E10; CARMEN; CIPER; CLAP; IMD37; mE10"
                     /coded_by="NM_001320715.2:281..949"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS90994.1"
                     /db_xref="GeneID:8915"
                     /db_xref="HGNC:HGNC:989"
                     /db_xref="MIM:603517"
ORIGIN      
        1 meptapslte edltevkkda lenlrvylce kiiaerhfdh lrakkilsre dteeiscrts
       61 srkragklld ylqenpkgld tlvesirrek tqnfliqkit devlklrnik lehlkdgatn
      121 nlsrsnsdes nfseklrast vmyhpegess ttpffstnss lnlpvlevgr tentifsstt
      181 lprpgdpgap plppdlqlee egtcanssem flplrsrtvs rq
//
LOCUS       NP_001192051             401 aa            linear   PRI 21-NOV-2025
DEFINITION  autophagy-related protein 13 isoform h [Homo sapiens].
ACCESSION   NP_001192051
VERSION     NP_001192051.1
DBSOURCE    REFSEQ: accession NM_001205122.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Patel,A. and Faesen,A.C.
  TITLE     Metamorphosis by ATG13 and ATG101 in human autophagy initiation
  JOURNAL   Autophagy 20 (4), 968-969 (2024)
   PUBMED   37394799
  REMARK    GeneRIF: Metamorphosis by ATG13 and ATG101 in human autophagy
            initiation.
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Nguyen,A. and Faesen,A.C.
  TITLE     The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis
  JOURNAL   FEBS Lett 598 (1), 114-126 (2024)
   PUBMED   37567770
  REMARK    GeneRIF: The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis.
            Review article
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Karabi,Z., Moradian,F. and Kheirabadi,M.
  TITLE     The effect of lactoferrin on ULK1 and ATG13 genes expression in
            breast cancer cell line MCF7 and bioinformatics studies of protein
            interaction between lactoferrin and the autophagy initiation
            complex
  JOURNAL   Cell Biochem Biophys 80 (4), 795-806 (2022)
   PUBMED   36169801
  REMARK    GeneRIF: The effect of lactoferrin on ULK1 and ATG13 genes
            expression in breast cancer cell line MCF7 and bioinformatics
            studies of protein interaction between lactoferrin and the
            autophagy initiation complex.
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Gottschalk,G., Peterson,D., Knox,K., Maynard,M., Whelan,R.J. and
            Roy,A.
  TITLE     Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE)
  JOURNAL   Mol Cell Neurosci 120, 103731 (2022)
   PUBMED   35487443
  REMARK    GeneRIF: Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE).
REFERENCE   6  (residues 1 to 401)
  AUTHORS   Jung,C.H., Jun,C.B., Ro,S.H., Kim,Y.M., Otto,N.M., Cao,J., Kundu,M.
            and Kim,D.H.
  TITLE     ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy
            machinery
  JOURNAL   Mol Biol Cell 20 (7), 1992-2003 (2009)
   PUBMED   19225151
  REMARK    GeneRIF: The ULK-Atg13-FIP200 complexes are direct targets of mTOR
            and important regulators of autophagy in response to mTOR
            signaling.
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Hosokawa,N., Hara,T., Kaizuka,T., Kishi,C., Takamura,A., Miura,Y.,
            Iemura,S., Natsume,T., Takehana,K., Yamada,N., Guan,J.L., Oshiro,N.
            and Mizushima,N.
  TITLE     Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200
            complex required for autophagy
  JOURNAL   Mol Biol Cell 20 (7), 1981-1991 (2009)
   PUBMED   19211835
  REMARK    GeneRIF: mTORC1 suppresses autophagy through direct regulation of
            the approximately 3-MDa ULK1-Atg13-FIP200 complex.
REFERENCE   8  (residues 1 to 401)
  AUTHORS   Chan,E.Y., Longatti,A., McKnight,N.C. and Tooze,S.A.
  TITLE     Kinase-inactivated ULK proteins inhibit autophagy via their
            conserved C-terminal domains using an Atg13-independent mechanism
  JOURNAL   Mol Cell Biol 29 (1), 157-171 (2009)
   PUBMED   18936157
  REMARK    GeneRIF: The functions of ULK1 and ULK2 are controlled by
            autophosphorylation and conformational changes involving exposure
            of the C-terminal domain and interaction with the putative human
            homologue of Atg13.
            GeneRIF: The gene product is the functional homologue of yeast
            Atg13, and required for autophagy in mammalian cells.
REFERENCE   9  (residues 1 to 401)
  AUTHORS   Meijer,W.H., van der Klei,I.J., Veenhuis,M. and Kiel,J.A.
  TITLE     ATG genes involved in non-selective autophagy are conserved from
            yeast to man, but the selective Cvt and pexophagy pathways also
            require organism-specific genes
  JOURNAL   Autophagy 3 (2), 106-116 (2007)
   PUBMED   17204848
REFERENCE   10 (residues 1 to 401)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA195671.1, AK294110.1,
            AB014552.1 and AC115088.6.
            
            Summary: The protein encoded by this gene is an autophagy factor
            and a target of the TOR kinase signaling pathway. The encoded
            protein is essential for autophagosome formation and mitophagy.
            [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (6) has multiple differences
            compared to variant 3. These differences result in a distinct 5'
            UTR and cause translation initiation at a downstream start codon
            compared to variant 3. The encoded isoform (h, also known as
            isoform 4) has a distinct N-terminus and is shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK294110.1, SRR14038192.293832.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..401
                     /product="autophagy-related protein 13 isoform h"
                     /note="autophagy-related protein 13; ATG13 autophagy
                     related 13 homolog"
                     /calculated_mol_wt=43962
     CDS             1..401
                     /gene="ATG13"
                     /gene_synonym="KIAA0652; PARATARG8"
                     /coded_by="NM_001205122.2:507..1712"
                     /note="isoform h is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS55761.1"
                     /db_xref="GeneID:9776"
                     /db_xref="HGNC:HGNC:29091"
                     /db_xref="MIM:615088"
ORIGIN      
        1 mcveislkts egdsmeleiw clemnekcdk eikvsytvyn rlslllksll aitrvtpayr
       61 lsrkqgheyv ilyriyfgev qlsglgegfq tvrvgtvgtp vgtitlscay rinlafmstr
      121 qfertppimg iiidhfvdrp ypssspmhpc nyrtagedtg viypsvedsq evcttsfsts
      181 ppsqlmvpgk eggvplapnq pvhgtqadqe rlatctpsdr thcaatpsss edtetvsnss
      241 egrasphdvl etifvrkvga fvnkpinqvt ltsldipfam fapknleled tdpmvnppds
      301 petesplqgs lhsdgssggs sgnthddfvm idfkpafskd dilpmdlgtf yrefqnppql
      361 sslsidigaq smaedldslp eklavheknv refdafvetl q
//
LOCUS       NP_001364264            1606 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing
            subunit beta isoform 2 [Homo sapiens].
ACCESSION   NP_001364264
VERSION     NP_001364264.1
DBSOURCE    REFSEQ: accession NM_001377335.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1606)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1606)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 1606)
  AUTHORS   Gozzelino,L., Kochlamazashvili,G., Baldassari,S., Mackintosh,A.I.,
            Licchetta,L., Iovino,E., Liu,Y.C., Bennett,C.A., Bennett,M.F.,
            Damiano,J.A., Zsurka,G., Marconi,C., Giangregorio,T., Magini,P.,
            Kuijpers,M., Maritzen,T., Norata,G.D., Baulac,S., Canafoglia,L.,
            Seri,M., Tinuper,P., Scheffer,I.E., Bahlo,M., Berkovic,S.F.,
            Hildebrand,M.S., Kunz,W.S., Giordano,L., Bisulli,F., Martini,M.,
            Haucke,V., Hirsch,E. and Pippucci,T.
  TITLE     Defective lipid signalling caused by mutations in PIK3C2B underlies
            focal epilepsy
  JOURNAL   Brain 145 (7), 2313-2331 (2022)
   PUBMED   35786744
  REMARK    GeneRIF: Defective lipid signalling caused by mutations in PIK3C2B
            underlies focal epilepsy.
REFERENCE   4  (residues 1 to 1606)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   5  (residues 1 to 1606)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1606)
  AUTHORS   Ueno,H., Honda,H., Nakamoto,T., Yamagata,T., Sasaki,K.,
            Miyagawa,K., Mitani,K., Yazaki,Y. and Hirai,H.
  TITLE     The phosphatidylinositol 3' kinase pathway is required for the
            survival signal of leukocyte tyrosine kinase
  JOURNAL   Oncogene 14 (25), 3067-3072 (1997)
   PUBMED   9223670
REFERENCE   7  (residues 1 to 1606)
  AUTHORS   Brown,R.A., Ho,L.K., Weber-Hall,S.J., Shipley,J.M. and Fry,M.J.
  TITLE     Identification and cDNA cloning of a novel mammalian C2
            domain-containing phosphoinositide 3-kinase, HsC2-PI3K
  JOURNAL   Biochem Biophys Res Commun 233 (2), 537-544 (1997)
   PUBMED   9144573
REFERENCE   8  (residues 1 to 1606)
  AUTHORS   Milani,D., Mazzoni,M., Borgatti,P., Zauli,G., Cantley,L. and
            Capitani,S.
  TITLE     Extracellular human immunodeficiency virus type-1 Tat protein
            activates phosphatidylinositol 3-kinase in PC12 neuronal cells
  JOURNAL   J Biol Chem 271 (38), 22961-22964 (1996)
   PUBMED   8798481
REFERENCE   9  (residues 1 to 1606)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
REFERENCE   10 (residues 1 to 1606)
  AUTHORS   Kozutsumi,H., Toyoshima,H., Hagiwara,K., Yazaki,Y. and Hirai,H.
  TITLE     Human ltk receptor tyrosine kinase binds to PLC-gamma 1, PI3-K, GAP
            and Raf-1 in vivo
  JOURNAL   Oncogene 9 (10), 2991-2998 (1994)
   PUBMED   8084603
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL606489.26.
            
            Summary: The protein encoded by this gene belongs to the
            phosphoinositide 3-kinase (PI3K) family. PI3-kinases play roles in
            signaling pathways involved in cell proliferation, oncogenic
            transformation, cell survival, cell migration, and intracellular
            protein trafficking. This protein contains a lipid kinase catalytic
            domain as well as a C-terminal C2 domain, a characteristic of class
            II PI3-kinases. C2 domains act as calcium-dependent phospholipid
            binding motifs that mediate translocation of proteins to membranes,
            and may also mediate protein-protein interactions. The PI3-kinase
            activity of this protein is sensitive to low nanomolar levels of
            the inhibitor wortmanin. The C2 domain of this protein was shown to
            bind phospholipids but not Ca2+, which suggests that this enzyme
            may function in a calcium-independent manner. [provided by RefSeq,
            Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC144342.1 [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1606
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..1606
                     /product="phosphatidylinositol 4-phosphate 3-kinase C2
                     domain-containing subunit beta isoform 2"
                     /EC_number="2.7.1.137"
                     /EC_number="2.7.1.154"
                     /note="phosphatidylinositol 3-kinase C2 domain-containing
                     beta polypeptide; PTDINS-3-kinase C2 beta; PI3K-C2beta;
                     PI3K-C2-beta; ptdIns-3-kinase C2 subunit beta;
                     phosphoinositide 3-kinase-C2-beta; phosphatidylinositol
                     4-phosphate 3-kinase C2 domain-containing subunit beta;
                     phosphoinositide-3-kinase, class 2, beta polypeptide"
                     /calculated_mol_wt=181556
     Region          2..298
                     /region_name="Interaction with GRB2.
                     /evidence=ECO:0000269|PubMed:11533253"
                     /note="propagated from UniProtKB/Swiss-Prot (O00750.2)"
     Region          45..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00750.2)"
     Region          259..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00750.2)"
     Region          364..466
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, ras-binding domain; pfam00794"
                     /db_xref="CDD:395642"
     Region          622..794
                     /region_name="C2A_PI3K_class_II"
                     /note="C2 domain first repeat present in class II
                     phosphatidylinositol 3-kinases (PI3Ks); cd04012"
                     /db_xref="CDD:175979"
     Region          813..953
                     /region_name="PI3Ka"
                     /note="Phosphoinositide 3-kinase family, accessory domain
                     (PIK domain); PIK domain is conserved in PI3 and
                     PI4-kinases. Its role is unclear, but it has been
                     suggested to be involved in substrate presentation.
                     Phosphoinositide 3-kinases play an important role in...;
                     cl00271"
                     /db_xref="CDD:412275"
     Region          959..1312
                     /region_name="PI3Kc_C2_beta"
                     /note="Catalytic domain of Class II Phosphoinositide
                     3-kinase beta; cd00895"
                     /db_xref="CDD:119421"
     Region          1028..1034
                     /region_name="G-loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (O00750.2)"
     Site            order(1029,1031..1033,1035,1053,1055,1058,1089,1101..1104,
                     1109,1112,1172,1174,1184..1185)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:119421"
     Region          1164..1172
                     /region_name="Catalytic loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (O00750.2)"
     Site            1164..1172
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:119421"
     Region          1183..1209
                     /region_name="Activation loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (O00750.2)"
     Site            1185..1209
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:119421"
     Region          1341..1449
                     /region_name="PX_PI3K_C2_beta"
                     /note="The phosphoinositide binding Phox Homology Domain
                     of the Beta Isoform of Class II Phosphoinositide
                     3-Kinases; cd07290"
                     /db_xref="CDD:132823"
     Site            order(1377..1379,1403..1404,1418)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132823"
     Region          1477..1599
                     /region_name="C2B_PI3K_class_II"
                     /note="C2 domain second repeat present in class II
                     phosphatidylinositol 3-kinases (PI3Ks); cd08381"
                     /db_xref="CDD:176027"
     Site            1527..1537
                     /site_type="active"
                     /note="nuclear localization signal [active]"
                     /db_xref="CDD:176027"
     CDS             1..1606
                     /gene="PIK3C2B"
                     /gene_synonym="C2-PI3K"
                     /coded_by="NM_001377335.1:1334..6154"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS91148.1"
                     /db_xref="GeneID:5287"
                     /db_xref="HGNC:HGNC:8972"
                     /db_xref="MIM:602838"
ORIGIN      
        1 msstqgngeh wkslesvgis rkelamaeal qmeydalsrl rhdkeenrak qnadpslisw
       61 depgvdfysk pagrrtdlkl lrglsgsdpt lnynslspqe gppnhstsqg pqpgsdpwpk
      121 gslsgdylyi fdgsdggvss spgpgdiegs ckklsppplp prasiwdtpp lpprkgspss
      181 skisqpsdin tfslveqlpg kllehrilee eevlggggqg rllgsvdydg indaitrlnl
      241 kstydaemlr datrgwkegr gpldfskdts gkpvarsktm ppqvpprtya srygnrknat
      301 pgknrrisaa pvgsrphtva nghelfevse erdeevaafc hmldilrsgs diqdyfltgy
      361 vwsavtpspe hlgdevnlkv tvlcdrlqea ltftcncsst vdlliyqtlc ythddlrnvd
      421 vgdfvlkpcg leeflqnkha lgsheyiqyc rkfdidirlq lmeqkvvrsd lartvnddqs
      481 pstlnylvhl qerpvkqtis rqalsllfdt yhnevdafll adgdfplkad rvvqsvkaic
      541 nalaavetpe itsalnqlpp cpsrmqpkiq kdpsvlavre nrekvvealt aaildlvely
      601 cntfnadfqt avpgsrkhdl vqeachfars laftvyathr ipiiwatsye dfylscslsh
      661 ggkelcsplq trrahfskyl fhlivwdqqi cfpvqvnrlp retllcatly alpipppgss
      721 seankqrrvp ealgwvttpl fnfrqvltcg rkllglwpat qenpsarwsa pnfhqpdsvi
      781 lqidfptsaf dikftsppgd kfspryefgs lreedqrklk dimqkeslyw ltdadkkrlw
      841 ekryychsew thmnhqdalg llhatfpdqe vrrmavqwig slsdaelldy lpqlvqalky
      901 ecyldsplvr fllkravsdl rvthyffwll kdglkdsqfs iryqyllaal lcccgkglre
      961 efnrqcwlvn alaklaqqvr eaapsarqgi lrtgleevkq ffalngscrl plspsllvkg
     1021 ivprdcsyfn snavplklsf qnvdplgeni rvifkcgddl rqdmltlqmi rimskiwvqe
     1081 gldmrmvifr cfstgrgrgm vemipnaetl rkiqvehgvt gsfkdrplad wlqkhnpged
     1141 eyekavenfi yscagccvat yvlgicdrhn dnimlkttgh mfhidfgrfl ghaqmfgnik
     1201 rdrapfvfts dmayvinggd kpssrfhdfv dlccqaynli rkhthlflnl lglmlscgip
     1261 elsdledlky vydalrpqdt eanattyftr liesslgsva tklnffihnl aqmkftgsdd
     1321 rltlsfasrt htlkssgris dvflcrheki fhpnkgyiyv vkvmrenthe atyiqrtfee
     1381 fqelhnklrl lfpsshlpsf psrfvigrsr geavaerrre elngyiwhli happevaecd
     1441 lvytffhplp rdekamgtsp apkssdgtwa rpvgkvggev klsisyknnk lfimvmhirg
     1501 lqllqdgndp dpyvkiyllp dpqkttkrkt kvarktcnpt ynemlvydgi pkgdlqqrel
     1561 qlsvlseqgf wenvllgevn irlreldlaq ektgwfalgs rshgtl
//
LOCUS       NP_001365774             261 aa            linear   PRI 21-NOV-2025
DEFINITION  myeloid leukemia factor 1 isoform 9 [Homo sapiens].
ACCESSION   NP_001365774
VERSION     NP_001365774.1
DBSOURCE    REFSEQ: accession NM_001378845.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Tang,Z., Yang,Y., Chen,W. and Liang,T.
  TITLE     Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling
  JOURNAL   Hepatol Commun 7 (8), e0204 (2023)
   PUBMED   37486965
  REMARK    GeneRIF: Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Huang,D., Liu,C., Sun,X., Sun,X., Qu,Y., Tang,Y., Li,G. and Tong,T.
  TITLE     CRL4DCAF8 and USP11 oppositely regulate the stability of myeloid
            leukemia factors (MLFs)
  JOURNAL   Biochem Biophys Res Commun 529 (2), 127-132 (2020)
   PUBMED   32703400
  REMARK    GeneRIF: CRL4(DCAF8) and USP11 oppositely regulate the stability of
            myeloid leukemia factors (MLFs).
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Darracq,A., Pak,H., Bourgoin,V., Zmiri,F., Dellaire,G., Affar,E.B.
            and Milot,E.
  TITLE     NPM and NPM-MLF1 interact with chromatin remodeling complexes and
            influence their recruitment to specific genes
  JOURNAL   PLoS Genet 15 (11), e1008463 (2019)
   PUBMED   31675375
  REMARK    GeneRIF: the abnormal gene regulation imposed by NPM-MLF1 can be
            characterized by the enhanced recruitment of NuRD to gene
            regulatory regions. Thus, different mechanisms would orchestrate
            the dysregulation of NPM function in NPMc+- versus
            NPM1-MLF1-associated leukemia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Yoneda-Kato,N., Tomoda,K., Umehara,M., Arata,Y. and Kato,J.Y.
  TITLE     Myeloid leukemia factor 1 regulates p53 by suppressing COP1 via
            COP9 signalosome subunit 3
  JOURNAL   EMBO J 24 (9), 1739-1749 (2005)
   PUBMED   15861129
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Hanissian,S.H., Akbar,U., Teng,B., Janjetovic,Z., Hoffmann,A.,
            Hitzler,J.K., Iscove,N., Hamre,K., Du,X., Tong,Y., Mukatira,S.,
            Robertson,J.H. and Morris,S.W.
  TITLE     cDNA cloning and characterization of a novel gene encoding the
            MLF1-interacting protein MLF1IP
  JOURNAL   Oncogene 23 (20), 3700-3707 (2004)
   PUBMED   15116101
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Arber,D.A., Chang,K.L., Lyda,M.H., Bedell,V., Spielberger,R. and
            Slovak,M.L.
  TITLE     Detection of NPM/MLF1 fusion in t(3;5)-positive acute myeloid
            leukemia and myelodysplasia
  JOURNAL   Hum Pathol 34 (8), 809-813 (2003)
   PUBMED   14506644
  REMARK    GeneRIF: These findings suggest that an NPM/MLF1 fusion is the
            primary molecular abnormality in t(3;5) MDS and AML with
            multilineage dysplasia, and that cases with NPM/MLF1 may be
            clinically distinct from other MDS-associated disease
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Lim,R., Winteringham,L.N., Williams,J.H., McCulloch,R.K.,
            Ingley,E., Tiao,J.Y., Lalonde,J.P., Tsai,S., Tilbrook,P.A., Sun,Y.,
            Wu,X., Morris,S.W. and Klinken,S.P.
  TITLE     MADM, a novel adaptor protein that mediates phosphorylation of the
            14-3-3 binding site of myeloid leukemia factor 1
  JOURNAL   J Biol Chem 277 (43), 40997-41008 (2002)
   PUBMED   12176995
  REMARK    GeneRIF: phosphorylation of 14-3-3 binding site by MADM
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Yoneda-Kato,N., Look,A.T., Kirstein,M.N., Valentine,M.B.,
            Raimondi,S.C., Cohen,K.J., Carroll,A.J. and Morris,S.W.
  TITLE     The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid
            leukemia produces a novel fusion gene, NPM-MLF1
  JOURNAL   Oncogene 12 (2), 265-275 (1996)
   PUBMED   8570204
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106707.9 and AC025033.20.
            
            Summary: This gene encodes an oncoprotein which is thought to play
            a role in the phenotypic determination of hemopoetic cells.
            Translocations between this gene and nucleophosmin have been
            associated with myelodysplastic syndrome and acute myeloid
            leukemia. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138520.86415.1,
                                           SRR6380198.154677.45 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.32"
     Protein         1..261
                     /product="myeloid leukemia factor 1 isoform 9"
                     /note="myelodysplasia-myeloid leukemia factor 1; testis
                     tissue sperm-binding protein Li 49e"
                     /calculated_mol_wt=29803
     Region          26..202
                     /region_name="Mlf1IP"
                     /note="Myelodysplasia-myeloid leukemia factor
                     1-interacting protein; pfam10248"
                     /db_xref="CDD:463022"
     CDS             1..261
                     /gene="MLF1"
                     /coded_by="NM_001378845.1:108..893"
                     /note="isoform 9 is encoded by transcript variant 12"
                     /db_xref="GeneID:4291"
                     /db_xref="HGNC:HGNC:7125"
                     /db_xref="MIM:601402"
ORIGIN      
        1 mfrmlnssfe ddpffsesil ahrenmrqmi rsfsepfgrd llsisdgrgr ahnrrghndg
       61 edslthtdvs sfqtmdqmvs nmrnymqkle rnfgqlsvdp nghsfcsssv mtyskigdep
      121 pkvfqastqt rrapggiket rkamrdsdsg lekmaighhi hdrahvikks knkktgdeev
      181 nqefinmnes dahafdeewq sevlkykpgr hnlgntrmrs vghenpgsre lkrrnlnkvq
      241 plnmegdqmf wgtnstskah l
//
LOCUS       NP_001291949             190 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger protein 747 isoform 4 [Homo sapiens].
ACCESSION   NP_001291949
VERSION     NP_001291949.1
DBSOURCE    REFSEQ: accession NM_001305020.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 190)
  AUTHORS   Ravasi,T., Suzuki,H., Cannistraci,C.V., Katayama,S., Bajic,V.B.,
            Tan,K., Akalin,A., Schmeier,S., Kanamori-Katayama,M., Bertin,N.,
            Carninci,P., Daub,C.O., Forrest,A.R., Gough,J., Grimmond,S.,
            Han,J.H., Hashimoto,T., Hide,W., Hofmann,O., Kamburov,A., Kaur,M.,
            Kawaji,H., Kubosaki,A., Lassmann,T., van Nimwegen,E.,
            MacPherson,C.R., Ogawa,C., Radovanovic,A., Schwartz,A.,
            Teasdale,R.D., Tegner,J., Lenhard,B., Teichmann,S.A., Arakawa,T.,
            Ninomiya,N., Murakami,K., Tagami,M., Fukuda,S., Imamura,K., Kai,C.,
            Ishihara,R., Kitazume,Y., Kawai,J., Hume,D.A., Ideker,T. and
            Hayashizaki,Y.
  TITLE     An atlas of combinatorial transcriptional regulation in mouse and
            man
  JOURNAL   Cell 140 (5), 744-752 (2010)
   PUBMED   20211142
  REMARK    Erratum:[Cell. 2010 Apr 16;141(2):369. Kamburov, Atanas [added];
            Kaur, Mandeep [added]; MacPherson, Cameron Ross [added];
            Radovanovic, Aleksandar [added]; Schwartz, Ariel [added]]
REFERENCE   7  (residues 1 to 190)
  AUTHORS   Loftus,B.J., Kim,U.J., Sneddon,V.P., Kalush,F., Brandon,R.,
            Fuhrmann,J., Mason,T., Crosby,M.L., Barnstead,M., Cronin,L.,
            Deslattes Mays,A., Cao,Y., Xu,R.X., Kang,H.L., Mitchell,S.,
            Eichler,E.E., Harris,P.C., Venter,J.C. and Adams,M.D.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
   PUBMED   10493829
REFERENCE   8  (residues 1 to 190)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP359683.1, AB209546.1, BC001361.2, AA316824.1, BM461939.1,
            BE327668.1 and CA429734.1.
            
            Transcript Variant: This variant (4) includes an alternate segment
            in the 5' coding region and uses an alternate splice site in the 3'
            coding region, compared to variant 1. These differences result in a
            frameshift compared to variant 1. The encoded isoform (4) is
            shorter and has a distinct C-terminus compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK054567.1, SRR3476690.889183.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467143, SAMN03267765
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..190
                     /product="zinc finger protein 747 isoform 4"
                     /note="KRAB domain-containing protein ZNF747"
                     /calculated_mol_wt=20350
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BV97.2)"
     Region          37..>77
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     CDS             1..190
                     /gene="ZNF747"
                     /coded_by="NM_001305020.2:180..752"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS76855.1"
                     /db_xref="GeneID:65988"
                     /db_xref="HGNC:HGNC:28350"
ORIGIN      
        1 mtdpslgltv pmapplaplp prdpngagse wrkpgavsfa dvavyfsree wgclrpaqra
       61 lyrdvmrety ghlgalgesp tclpgpcast gpaaplgaac gvggpgagqa assqrgvcvl
      121 lpqeseaasr rsspgwrrrp ncgirlprir rwrsvrqkrt qipetrkrkd kgkgrepwrs
      181 ptlwppgllg
//
LOCUS       NP_001387095            1220 aa            linear   PRI 21-NOV-2025
DEFINITION  protein transport protein Sec31A isoform 1 [Homo sapiens].
ACCESSION   NP_001387095
VERSION     NP_001387095.1
DBSOURCE    REFSEQ: accession NM_001400166.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1220)
  AUTHORS   Tobias,E.S., Lucas-Herald,A.K., Sagar,D., Montezano,A.C.,
            Rios,F.J., De Lucca Camargo,L., Hamilton,G., Gazdagh,G.,
            Diver,L.A., Williams,N., Herzyk,P., Touyz,R.M., Greenfield,A.,
            McGowan,R. and Ahmed,S.F.
  TITLE     SEC31A may be associated with pituitary hormone deficiency and
            gonadal dysgenesis
  JOURNAL   Endocrine 84 (2), 345-349 (2024)
   PUBMED   38400880
  REMARK    GeneRIF: SEC31A may be associated with pituitary hormone deficiency
            and gonadal dysgenesis.
REFERENCE   2  (residues 1 to 1220)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1220)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1220)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1220)
  AUTHORS   Jin,L., Pahuja,K.B., Wickliffe,K.E., Gorur,A., Baumgartel,C.,
            Schekman,R. and Rape,M.
  TITLE     Ubiquitin-dependent regulation of COPII coat size and function
  JOURNAL   Nature 482 (7386), 495-500 (2012)
   PUBMED   22358839
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1220)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1220)
  AUTHORS   Kim,J.H., Hong,J.A., Pih,K.T. and Hwang,I.
  TITLE     Identification and isolation of differentially expressed genes in
            osmotically stressed human oral keratinocytes
  JOURNAL   Arch Oral Biol 46 (4), 335-341 (2001)
   PUBMED   11269867
REFERENCE   8  (residues 1 to 1220)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 1220)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   10 (residues 1 to 1220)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021105.13 and AC108469.5.
            
            Summary: The protein encoded by this gene shares similarity with
            the yeast Sec31 protein, and is a component of the outer layer of
            the coat protein complex II (COPII). The encoded protein is
            involved in vesicle budding from the endoplasmic reticulum (ER) and
            contains multiple WD repeats near the N-terminus and a proline-rich
            region in the C-terminal half. It associates with the protein
            encoded by the SEC13 homolog, nuclear pore and COPII coat complex
            component (SEC13), and is required for ER-Golgi transport.
            Monoubiquitylation of this protein by CUL3-KLHL12 was found to
            regulate the size of COPII coats to accommodate unusually shaped
            cargo. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1178011.1,
                                           SRR14038193.2817885.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1220
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..1220
                     /product="protein transport protein Sec31A isoform 1"
                     /note="yeast Sec31p homolog; protein transport protein
                     Sec31A; web1-like protein; SEC31 homolog A, COPII coat
                     complex component; SEC31-related protein A; SEC31-like
                     protein 1; SEC31 homolog A, COPII coating complex
                     component"
                     /calculated_mol_wt=132884
     Region          4..47
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          13..332
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(26,40,46..47,52..53,91,95,101..102,117,121,139,144,
                     150..151,164,185,190,196..197,209..210,231,235,244..245,
                     258..259,277,282,288..289,301..302,320,325,331..332)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          68..111
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          70..119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          120..160
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          125..162
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          161..471
                     /region_name="Interaction with SEC13.
                     /evidence=ECO:0000269|PubMed:16957052"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          172..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          263..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          306..331
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94979.3)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (O94979.3)"
     Region          <573..>696
                     /region_name="ACE1-Sec16-like"
                     /note="Ancestral coatomer element 1 (ACE1) of COPII coat
                     complex assembly protein Sec16; cl14807"
                     /db_xref="CDD:449359"
     Site            order(574..578,580,582,593,595,596..597,599..600,604,610,
                     618,630,633,658..659)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187736"
     Region          791..908
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Site            799
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          800..1113
                     /region_name="Interaction with PDCD6.
                     /evidence=ECO:0000269|PubMed:16957052"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          <800..>1098
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          842..848
                     /region_name="ALG-2-binding site motif-2 (ABS-2)"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          924..1096
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Site            1161
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94979.3)"
     Site            1163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O94979.3)"
     CDS             1..1220
                     /gene="SEC31A"
                     /gene_synonym="ABP125; ABP130; HPBKS; HSPC275; HSPC334;
                     NEDSOSB; SEC31L1"
                     /coded_by="NM_001400166.1:320..3982"
                     /note="isoform 1 is encoded by transcript variant 21"
                     /db_xref="CCDS:CCDS3596.1"
                     /db_xref="GeneID:22872"
                     /db_xref="HGNC:HGNC:17052"
                     /db_xref="MIM:610257"
ORIGIN      
        1 mklkevdrta mqawspaqnh piylatgtsa qqldatfstn asleifeldl sdpsldmksc
       61 atfssshryh kliwgpykmd skgdvsgvli aggengniil ydpskiiagd kevviaqndk
      121 htgpvraldv nifqtnlvas ganeseiyiw dlnnfatpmt pgaktqpped isciawnrqv
      181 qhilasasps gratvwdlrk nepiikvsdh snrmhcsgla whpdvatqmv laseddrlpv
      241 iqmwdlrfas splrvlenha rgilaiawsm adpelllscg kdakilcsnp ntgevlyelp
      301 tntqwcfdiq wcprnpavls aasfdgrisv ysimggstdg lrqkqvdkls ssfgnldpfg
      361 tgqplpplqi pqqtaqhsiv lplkkppkwi rrpvgasfsf ggklvtfenv rmpshqgaeq
      421 qqqqhhvfis qvvtekefls rsdqlqqavq sqgfinycqk kidasqtefe knvwsflkvn
      481 feddsrgkyl ellgyrkedl gkkialalnk vdganvalkd sdqvaqsdge espaaeeqll
      541 gehikeekee seflpssggt fnisvsgdid glitqalltg nfesavdlcl hdnrmadaii
      601 laiaggqell artqkkyfak sqskitrlit avvmknwkei vescdlknwr ealaavltya
      661 kpdefsalcd llgtrleneg dsllqtqacl cyicagnvek lvacwtkaqd gshplslqdl
      721 iekvvilrka vqltqamdts tvgvllaakm sqyanllaaq gsiaaalafl pdntnqpnim
      781 qlrdrlcraq gepvaghesp kipyekqqlp kgrpgpvagh hqmprvqtqq yyphgenppp
      841 pgfimhgnvn pnaagqlpts pghmhtqvpp ypqpqpyqpa qpypfgtggs amyrpqqpva
      901 pptsnaypnt pyissassyt gqsqlyaaqh qassptsspa tsfppppssg asfqhggpga
      961 ppsssayalp pgttgtlpaa selpasqrtg pqngwndppa lnrvpkkkkm penfmppvpi
     1021 tspimnplgd pqsqmlqqqp sapvplssqs sfpqphlpgg qpfhgvqqpl gqtgmppsfs
     1081 kpniegapga pigntfqhvq slptkkitkk pipdehlilk ttfedliqrc lssatdpqtk
     1141 rklddaskrl eflydklreq tlsptitsgl hniarsietr nysegltmht hivstsnfse
     1201 tsafmpvlkv vltqanklgv
//
LOCUS       NP_001308498             533 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 9 [Homo sapiens].
ACCESSION   NP_001308498 XP_005263308
VERSION     NP_001308498.1
DBSOURCE    REFSEQ: accession NM_001321569.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 533)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 533)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 533)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 533)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 533)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 533)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            On Mar 26, 2016 this sequence version replaced XP_005263308.1.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.28550.1,
                                           SRR1660809.181734.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..533
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 9"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=59873
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          380..507
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..533
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001321569.2:671..2272"
                     /note="isoform 9 is encoded by transcript variant 10"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkin nkanvvtspk eniptpalep qttvihnpdg
      361 nkestessnt tiededvkar kqeiikvteq lieainngdf eaytkicdpg ltafepealg
      421 nlvegmdfhr fyfenalsks nkpihtiiln phvhlvgdda aciayirltq ymdgsgmpkt
      481 mqseetrvwh rrdgkwqnvh fhrsgsptvp ikppcipngk enfsggtslw qni
//
LOCUS       NP_001264743             588 aa            linear   PRI 21-NOV-2025
DEFINITION  YTH domain-containing family protein 3 isoform b [Homo sapiens].
ACCESSION   NP_001264743
VERSION     NP_001264743.1
DBSOURCE    REFSEQ: accession NM_001277814.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Duan,J., Fan,D., Chen,P., Xiang,J., Xie,X., Peng,Y., Bai,J., Li,T.,
            Li,Y., Song,H., Fu,W., Zhang,T., Xiao,Y., Qi,X., Hong,W., Zhou,J.,
            He,Y., Wu,C., Zeng,H., Bai,H., Chen,T., Yu,W. and Zhang,Q.
  TITLE     YTHDF3 Regulates the Degradation and Stability of m6A-Enriched
            Transcripts to Facilitate the Progression of Castration-Resistant
            Prostate Cancer
  JOURNAL   J Pineal Res 76 (5), e13003 (2024)
   PUBMED   39143673
  REMARK    GeneRIF: YTHDF3 Regulates the Degradation and Stability of
            m6A-Enriched Transcripts to Facilitate the Progression of
            Castration-Resistant Prostate Cancer.
REFERENCE   3  (residues 1 to 588)
  AUTHORS   Qiu,D., Gao,L. and Yu,X.
  TITLE     Knockdown of YAP1 Reduces YTHDF3 to Stabilize SMAD7 and thus
            Inhibit Bladder Cancer Stem Cell Stemness
  JOURNAL   Discov Med 36 (186), 1486-1498 (2024)
   PUBMED   39054719
  REMARK    GeneRIF: Knockdown of YAP1 Reduces YTHDF3 to Stabilize SMAD7 and
            thus Inhibit Bladder Cancer Stem Cell Stemness.
REFERENCE   4  (residues 1 to 588)
  AUTHORS   Zhang,H., Sun,Y., Wang,Z., Huang,X., Tang,L., Jiang,K. and Jin,X.
  TITLE     ZDHHC20-mediated S-palmitoylation of YTHDF3 stabilizes MYC mRNA to
            promote pancreatic cancer progression
  JOURNAL   Nat Commun 15 (1), 4642 (2024)
   PUBMED   38821916
  REMARK    GeneRIF: ZDHHC20-mediated S-palmitoylation of YTHDF3 stabilizes MYC
            mRNA to promote pancreatic cancer progression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 588)
  AUTHORS   Zhong,S., Guo,Q., Chen,X., Luo,X., Long,Y., Chong,T., Ye,M., He,H.,
            Lu,A., Ao,K., Yin,M., Xu,A., Li,X., Hao,Y. and Guo,X.
  TITLE     The inhibition of YTHDF3/m6A/LRP6 reprograms fatty acid metabolism
            and suppresses lymph node metastasis in cervical cancer
  JOURNAL   Int J Biol Sci 20 (3), 916-936 (2024)
   PUBMED   38250152
  REMARK    GeneRIF: The inhibition of YTHDF3/m[6]A/LRP6 reprograms fatty acid
            metabolism and suppresses lymph node metastasis in cervical cancer.
            Erratum:[Int J Biol Sci. 2025 Jun 5;21(8):3825-3826. doi:
            10.7150/ijbs.115928. PMID: 40520018]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 588)
  AUTHORS   Varade,J., Comabella,M., Ortiz,M.A., Arroyo,R., Fernandez,O.,
            Pinto-Medel,M.J., Fedetz,M., Izquierdo,G., Lucas,M., Gomez,C.L.,
            Rabasa,A.C., Alcina,A., Matesanz,F., Alloza,I., Antiguedad,A.,
            Garcia-Barcina,M., Otaegui,D., Olascoaga,J., Saiz,A., Blanco,Y.,
            Montalban,X., Vandenbroeck,K. and Urcelay,E.
  TITLE     Replication study of 10 genes showing evidence for association with
            multiple sclerosis: validation of TMEM39A, IL12B and CBLB
            [correction of CLBL] genes
  JOURNAL   Mult Scler 18 (7), 959-965 (2012)
   PUBMED   22194214
REFERENCE   7  (residues 1 to 588)
  AUTHORS   Dominissini,D., Moshitch-Moshkovitz,S., Schwartz,S.,
            Salmon-Divon,M., Ungar,L., Osenberg,S., Cesarkas,K.,
            Jacob-Hirsch,J., Amariglio,N., Kupiec,M., Sorek,R. and Rechavi,G.
  TITLE     Topology of the human and mouse m6A RNA methylomes revealed by
            m6A-seq
  JOURNAL   Nature 485 (7397), 201-206 (2012)
   PUBMED   22575960
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 588)
  AUTHORS   Jager,S., Cimermancic,P., Gulbahce,N., Johnson,J.R., McGovern,K.E.,
            Clarke,S.C., Shales,M., Mercenne,G., Pache,L., Li,K., Hernandez,H.,
            Jang,G.M., Roth,S.L., Akiva,E., Marlett,J., Stephens,M., D'Orso,I.,
            Fernandes,J., Fahey,M., Mahon,C., O'Donoghue,A.J., Todorovic,A.,
            Morris,J.H., Maltby,D.A., Alber,T., Cagney,G., Bushman,F.D.,
            Young,J.A., Chanda,S.K., Sundquist,W.I., Kortemme,T.,
            Hernandez,R.D., Craik,C.S., Burlingame,A., Sali,A., Frankel,A.D.
            and Krogan,N.J.
  TITLE     Global landscape of HIV-human protein complexes
  JOURNAL   Nature 481 (7381), 365-370 (2011)
   PUBMED   22190034
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 588)
  AUTHORS   Sundstrom,G., Dreborg,S. and Larhammar,D.
  TITLE     Concomitant duplications of opioid peptide and receptor genes
            before the origin of jawed vertebrates
  JOURNAL   PLoS One 5 (5), e10512 (2010)
   PUBMED   20463905
  REMARK    GeneRIF: Includes a multi-species analysis of YTHDF family members.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 588)
  AUTHORS   Stoilov,P., Rafalska,I. and Stamm,S.
  TITLE     YTH: a new domain in nuclear proteins
  JOURNAL   Trends Biochem Sci 27 (10), 495-497 (2002)
   PUBMED   12368078
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK093081.1, AK298544.1,
            AK127574.1 and AL832335.1.
            
            Summary: This gene encodes a member of the YTH (YT521-B homology)
            domain protein family. The YTH domain is common in eukaryotes, is
            often found in the middle of the protein sequence, and may function
            in binding to RNA. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Apr 2013].
            
            Transcript Variant: This variant (3) differs in its 5' UTR and 5'
            coding region, and uses an alternate start codon, compared to
            variant 1. The encoded isoform (b) has a longer and distinct
            N-terminus, compared to isoform a. Both variants 2 and 3 encode the
            same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.2390801.1, AK298544.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.3"
     Protein         1..588
                     /product="YTH domain-containing family protein 3 isoform
                     b"
                     /note="YTH domain family protein 3; YTH
                     N(6)-methyladenosine RNA binding protein 3; YTH
                     domain-containing family protein 3; YTH domain family,
                     member 3; YTH N6-methyladenosine RNA binding protein 3"
                     /calculated_mol_wt=64363
     Region          420..553
                     /region_name="YTH"
                     /note="YT521-B-like domain; pfam04146"
                     /db_xref="CDD:461195"
     CDS             1..588
                     /gene="YTHDF3"
                     /gene_synonym="DF3"
                     /coded_by="NM_001277814.2:215..1981"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS75748.1"
                     /db_xref="GeneID:253943"
                     /db_xref="HGNC:HGNC:26465"
                     /db_xref="MIM:618669"
ORIGIN      
        1 mfyldltlfh raeetgeesf svqngsihqk davndddfep ylssqtnqsn syppmsdpym
       61 psyyapsigf pyslgeaaws tagdqpmpyl ttygqmsnge hhyipdgvfs qpgalgntpp
      121 flgqhgfnff pgnadfstwg tsgsqgqstq ssaysssygy ppsslgrait dgqagfgndt
      181 lskvpgissi eqgmtglkig gdltaavtkt vgtalsssgm tsiatnsvpp vssaapkpts
      241 waaiarkpak pqpklkpkgn vgiggsavpp ppikhnmnig twdekgsvvk apptqpvlpp
      301 qtiiqqpqpl iqppplvqsq lpqqqpqppq pqqqqgpqpq aqphqvqpqq qqlqnrwvap
      361 rnrgagfnqn ngagsenfgl gvvpvsasps svevhpvlek lkainnynpk dfdwnlkngr
      421 vfiiksysed dihrsikysi wcstehgnkr ldaayrslng kgplyllfsv ngsghfcgva
      481 emksvvdyna yagvwsqdkw kgkfevkwif vkdvpnnqlr hirlenndnk pvtnsrdtqe
      541 vplekakqvl kiiatfkhtt sifddfahye krqeeeeamr rernrnkq
//
LOCUS       NP_001258877             432 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B
            beta isoform isoform d [Homo sapiens].
ACCESSION   NP_001258877
VERSION     NP_001258877.1
DBSOURCE    REFSEQ: accession NM_001271948.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Shen,D. and Kang,S.
  TITLE     Comprehensive analysis of mitochondria-related genes indicates that
            PPP2R2B is a novel biomarker and promotes the progression of
            bladder cancer via Wnt signaling pathway
  JOURNAL   Biol Direct 19 (1), 17 (2024)
   PUBMED   38409085
  REMARK    GeneRIF: Comprehensive analysis of mitochondria-related genes
            indicates that PPP2R2B is a novel biomarker and promotes the
            progression of bladder cancer via Wnt signaling pathway.
            Erratum:[Biol Direct. 2024 Apr 18;19(1):27. doi:
            10.1186/s13062-024-00474-1. PMID: 38637864]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Zhou,C., Liu,H.B., Jahanbakhsh,F., Deng,L., Wu,B., Ying,M.,
            Margolis,R.L. and Li,P.P.
  TITLE     Bidirectional Transcription at the PPP2R2B Gene Locus in
            Spinocerebellar Ataxia Type 12
  JOURNAL   Mov Disord 38 (12), 2230-2240 (2023)
   PUBMED   37735923
  REMARK    GeneRIF: Bidirectional Transcription at the PPP2R2B Gene Locus in
            Spinocerebellar Ataxia Type 12.
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Ruediger,R., Brewis,N., Ohst,K. and Walter,G.
  TITLE     Increasing the ratio of PP2A core enzyme to holoenzyme inhibits
            Tat-stimulated HIV-1 transcription and virus production
  JOURNAL   Virology 238 (2), 432-443 (1997)
   PUBMED   9400615
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Tung,H.Y., De Rocquigny,H., Zhao,L.J., Cayla,X., Roques,B.P. and
            Ozon,R.
  TITLE     Direct activation of protein phosphatase-2A0 by HIV-1 encoded
            protein complex NCp7:vpr
  JOURNAL   FEBS Lett 401 (2-3), 197-201 (1997)
   PUBMED   9013886
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Schalling,M., Hudson,T.J., Buetow,K.H. and Housman,D.E.
  TITLE     Direct detection of novel expanded trinucleotide repeats in the
            human genome
  JOURNAL   Nat Genet 4 (2), 135-139 (1993)
   PUBMED   8348150
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Margolis,R.L., Holmes,S.E., Srivastava,A.K., Mukherji,M. and
            Sinha,K.K.
  TITLE     Spinocerebellar Ataxia Type 12 - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301381
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
REFERENCE   10 (residues 1 to 432)
  AUTHORS   Mayer,R.E., Hendrix,P., Cron,P., Matthies,R., Stone,S.R., Goris,J.,
            Merlevede,W., Hofsteenge,J. and Hemmings,B.A.
  TITLE     Structure of the 55-kDa regulatory subunit of protein phosphatase
            2A: evidence for a neuronal-specific isoform
  JOURNAL   Biochemistry 30 (15), 3589-3597 (1991)
   PUBMED   1849734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP195204.1, AK314810.1,
            BC031790.1, AI621232.1 and AC008728.7.
            
            Summary: The product of this gene belongs to the phosphatase 2
            regulatory subunit B family. Protein phosphatase 2 is one of the
            four major Ser/Thr phosphatases, and it is implicated in the
            negative control of cell growth and division. It consists of a
            common heteromeric core enzyme, which is composed of a catalytic
            subunit and a constant regulatory subunit, that associates with a
            variety of regulatory subunits. The B regulatory subunit might
            modulate substrate selectivity and catalytic activity. This gene
            encodes a beta isoform of the regulatory subunit B55 subfamily.
            Defects in this gene cause autosomal dominant spinocerebellar
            ataxia 12 (SCA12), a disease caused by degeneration of the
            cerebellum, sometimes involving the brainstem and spinal cord, and
            in resulting in poor coordination of speech and body movements.
            Multiple alternatively spliced variants, which encode different
            isoforms, have been identified for this gene. The 5' UTR of some of
            these variants includes a CAG trinucleotide repeat sequence (7-28
            copies) that can be expanded to 55-78 copies in cases of SCA12.
            [provided by RefSeq, Jul 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314810.1, SRR18074967.906137.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..432
                     /product="serine/threonine-protein phosphatase 2A 55 kDa
                     regulatory subunit B beta isoform isoform d"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase 2, regulatory subunit B, beta"
                     /calculated_mol_wt=50240
     Region          13..427
                     /region_name="CDC55"
                     /note="Serine/threonine protein phosphatase 2A, regulatory
                     subunit [Signal transduction mechanisms]; COG5170"
                     /db_xref="CDD:227498"
     Region          16..64
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          82..159
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          165..201
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          215..266
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          273..309
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          330..365
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          404..427
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..432
                     /gene="PPP2R2B"
                     /gene_synonym="B55BETA; PP2AB55BETA; PP2ABBETA; PP2APR55B;
                     PP2APR55BETA; PR2AB55BETA; PR2ABBETA; PR2APR55BETA; PR52B;
                     PR55-BETA; PR55BETA; SCA12"
                     /coded_by="NM_001271948.2:805..2103"
                     /note="isoform d is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS43380.1"
                     /db_xref="GeneID:5521"
                     /db_xref="HGNC:HGNC:9305"
                     /db_xref="MIM:604325"
ORIGIN      
        1 mnypdentyg nkadiistve fnhtgellat gdkggrvvif qreqesknqv hrrgeynvys
       61 tfqshepefd ylksleieek inkirwlpqq naayfllstn dktvklwkvs erdkrpegyn
      121 lkdeegrlrd patittlrvp vlrpmdlmve atprrvfana htyhinsisv nsdyetymsa
      181 ddlrinlwnf eitnqsfniv dikpanmeel tevitaaefh phhcntfvys sskgtirlcd
      241 mrasalcdrh tkffeepedp snrsffseii ssisdvkfsh sgryimtrdy ltvkvwdlnm
      301 enrpietyqv hdylrsklcs lyendcifdk fecvwngsds vimtgsynnf frmfdrntkr
      361 dvtleasren skprailkpr kvcvggkrrk deisvdsldf skkilhtawh pseniiavaa
      421 tnnlyifqdk vn
//
LOCUS       NP_065397                782 aa            linear   PRI 21-NOV-2025
DEFINITION  cysteine-rich protein 2-binding protein isoform 1 [Homo sapiens].
ACCESSION   NP_065397
VERSION     NP_065397.4
DBSOURCE    REFSEQ: accession NM_020536.7
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Gong,Y., Liu,M., Zhang,Q., Li,J., Cai,H., Ran,J., Ma,L., Ma,Y. and
            Quan,S.
  TITLE     Lysine acetyltransferase 14 mediates TGF-beta-induced fibrosis in
            ovarian endometrioma via co-operation with serum response factor
  JOURNAL   J Transl Med 22 (1), 561 (2024)
   PUBMED   38867256
  REMARK    GeneRIF: Lysine acetyltransferase 14 mediates TGF-beta-induced
            fibrosis in ovarian endometrioma via co-operation with serum
            response factor.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 782)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 782)
  AUTHORS   Viita,T., Kyheroinen,S., Prajapati,B., Virtanen,J., Frilander,M.J.,
            Varjosalo,M. and Vartiainen,M.K.
  TITLE     Nuclear actin interactome analysis links actin to KAT14 histone
            acetyl transferase and mRNA splicing
  JOURNAL   J Cell Sci 132 (8) (2019)
   PUBMED   30890647
  REMARK    GeneRIF: Actin binds directly to the hATAC subunit KAT14, and
            modulates its histone acetyl transferase activity in vitro and in
            cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 782)
  AUTHORS   Orpinell,M., Fournier,M., Riss,A., Nagy,Z., Krebs,A.R., Frontini,M.
            and Tora,L.
  TITLE     The ATAC acetyl transferase complex controls mitotic progression by
            targeting non-histone substrates
  JOURNAL   EMBO J 29 (14), 2381-2394 (2010)
   PUBMED   20562830
REFERENCE   7  (residues 1 to 782)
  AUTHORS   Nagy,Z., Riss,A., Fujiyama,S., Krebs,A., Orpinell,M., Jansen,P.,
            Cohen,A., Stunnenberg,H.G., Kato,S. and Tora,L.
  TITLE     The metazoan ATAC and SAGA coactivator HAT complexes regulate
            different sets of inducible target genes
  JOURNAL   Cell Mol Life Sci 67 (4), 611-628 (2010)
   PUBMED   19936620
REFERENCE   8  (residues 1 to 782)
  AUTHORS   Guelman,S., Kozuka,K., Mao,Y., Pham,V., Solloway,M.J., Wang,J.,
            Wu,J., Lill,J.R. and Zha,J.
  TITLE     The double-histone-acetyltransferase complex ATAC is essential for
            mammalian development
  JOURNAL   Mol Cell Biol 29 (5), 1176-1188 (2009)
   PUBMED   19103755
REFERENCE   9  (residues 1 to 782)
  AUTHORS   Wang,Y.L., Faiola,F., Xu,M., Pan,S. and Martinez,E.
  TITLE     Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel
            NC2-like histone fold module that interacts with the TATA-binding
            protein
  JOURNAL   J Biol Chem 283 (49), 33808-33815 (2008)
   PUBMED   18838386
REFERENCE   10 (residues 1 to 782)
  AUTHORS   Weiskirchen,R. and Gressner,A.M.
  TITLE     The cysteine- and glycine-rich LIM domain protein CRP2 specifically
            interacts with a novel human protein (CRP2BP)
  JOURNAL   Biochem Biophys Res Commun 274 (3), 655-663 (2000)
   PUBMED   10924333
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL050321.11 and KF459584.1.
            
            On Nov 18, 2020 this sequence version replaced NP_065397.3.
            
            Summary: CSRP2 is a protein containing two LIM domains, which are
            double zinc finger motifs found in proteins of diverse function.
            CSRP2 and some related proteins are thought to act as protein
            adapters, bridging two or more proteins to form a larger protein
            complex. The protein encoded by this gene binds to one of the LIM
            domains of CSRP2 and contains an acetyltransferase domain. Although
            the encoded protein has been detected in the cytoplasm, it is
            predominantly a nuclear protein. Alternatively spliced transcript
            variants have been described. [provided by RefSeq, Jun 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. This variant contains a uORF which represents a portion
            of the coding region for the PET117 protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.2191173.1,
                                           SRR11853564.17132.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.23"
     Protein         1..782
                     /product="cysteine-rich protein 2-binding protein isoform
                     1"
                     /note="CRP2 binding protein; ATAC component 2 homolog;
                     CRP2 binding partner; cysteine-rich protein 2-binding
                     protein; CSRP2-binding protein; ADA2A-containing complex
                     subunit 2"
                     /calculated_mol_wt=88713
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Region          13..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Site            231
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8CID0; propagated from
                     UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Region          251..282
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Site            292
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Region          315..346
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Region          400..460
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8E8.3)"
     Region          686..761
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
     CDS             1..782
                     /gene="KAT14"
                     /gene_synonym="ATAC2; CRP2BP; CSRP2BP; dJ717M23.1;
                     PRO1194"
                     /coded_by="NM_020536.7:828..3176"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13133.1"
                     /db_xref="GeneID:57325"
                     /db_xref="HGNC:HGNC:15904"
                     /db_xref="MIM:617501"
ORIGIN      
        1 mdssihlssl isrhddeatr tstsegleeg evegetlliv esedqasvdl shdqsgdsln
       61 sdegdvswme eqlsyfcdkc qkwipasqlr eqlsylkgdn ffrftcsdcs adgkeqyerl
      121 kltwqqvvml amynlslegs grqgyfrwke dicafiekhw tfllgnrkkt stwwstvagc
      181 lsvgspmyfr sgaqefgepg wwklvhnkpp tmkpegekls astlkikaas kptldpiitv
      241 eglrkrasrn pvesamelke krsrtqeakd irraqkeaag fldrstsstp vkfisrgrrp
      301 dvilekgevi dfsslsssdr tpltspspsp sldfsapgtp ashsatpsll seadlipdvm
      361 ppqalfhddd emegdgvidp gmeyvpppag svasgpvvgv rkkvrgpeqi kqeveseeek
      421 pdrmdidsed tdsntslqtr arekrkpqle kdtkpkepry tpvsiyeekl llkrleacpg
      481 avamtpearr lkrklivrqa krdrglplfd ldqvvnaall lvdgiygake ggisrlpagq
      541 atyrttcqdf rildryqtsl psrkgfrhqt tkflyrlvgs edmavdqsiv spytsrilkp
      601 yirrdyetkp pklqllsqir shlhrsdphw tpepdapldy cyvrpnhipt insmcqeffw
      661 pgidlseclq ypdfsvvvly kkviiafgfm vpdvkyneay isflfvhpew rragiatfmi
      721 yhliqtcmgk dvtlhvsasn pamllyqkfg fkteeyvldf ydkyyplest eckhafflrl
      781 rr
//
LOCUS       NP_001371279             142 aa            linear   PRI 21-NOV-2025
DEFINITION  alpha-lactalbumin precursor [Homo sapiens].
ACCESSION   NP_001371279
VERSION     NP_001371279.1
DBSOURCE    REFSEQ: accession NM_001384350.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Sadovnikova,A., Garcia,S.C. and Hovey,R.C.
  TITLE     A Comparative Review of the Cell Biology, Biochemistry, and
            Genetics of Lactose Synthesis
  JOURNAL   J Mammary Gland Biol Neoplasia 26 (2), 181-196 (2021)
   PUBMED   34125364
  REMARK    Review article
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Lebedev,D.V., Zabrodskaya,Y.A., Pipich,V., Kuklin,A.I., Ramsay,E.,
            Sokolov,A.V., Elizarova,A.Y., Shaldzhyan,A.A., Grudinina,N.A.,
            Pantina,R.A., Wu,B., Shtam,T.A., Volnitskiy,A.V., Schmidt,A.E.,
            Shvetsov,A.V., Vasilyev,V.B., Isaev-Ivanov,V.V. and Egorov,V.V.
  TITLE     Effect of alpha-lactalbumin and lactoferrin oleic acid complexes on
            chromatin structural organization
  JOURNAL   Biochem Biophys Res Commun 520 (1), 136-139 (2019)
   PUBMED   31582209
  REMARK    GeneRIF: human alpha-lactalbumin and human lactoferrin complexes
            appeared to interact with the chromatin of isolated nuclei
            affecting chromatin structural organization
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Permyakov,E.A., Permyakov,S.E., Breydo,L., Redwan,E.M.,
            Almehdar,H.A. and Uversky,V.N.
  TITLE     Disorder in Milk Proteins: alpha-Lactalbumin. Part C. Peculiarities
            of Metal Binding
  JOURNAL   Curr Protein Pept Sci 17 (8), 735-745 (2016)
   PUBMED   27238572
  REMARK    GeneRIF: Studies indicate that alpha-lactalbumin has two domains, a
            large alpha-helical domain and a small beta-sheet domain connected
            by a calcium binding loop.
            Review article
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Wu,Y., Gao,H., Li,H., Tabara,Y., Nakatochi,M., Chiu,Y.F.,
            Park,E.J., Wen,W., Adair,L.S., Borja,J.B., Cai,Q., Chang,Y.C.,
            Chen,P., Croteau-Chonka,D.C., Fogarty,M.P., Gan,W., He,C.T.,
            Hsiung,C.A., Hwu,C.M., Ichihara,S., Igase,M., Jo,J., Kato,N.,
            Kawamoto,R., Kuzawa,C.W., Lee,J.J., Liu,J., Lu,L., McDade,T.W.,
            Osawa,H., Sheu,W.H., Teo,Y., Vadlamudi,S., Van Dam,R.M., Wang,Y.,
            Xiang,Y.B., Yamamoto,K., Ye,X., Young,T.L., Zheng,W., Zhu,J.,
            Shu,X.O., Shin,C., Jee,S.H., Chuang,L.M., Miki,T., Yokota,M.,
            Lin,X., Mohlke,K.L. and Tai,E.S.
  TITLE     A meta-analysis of genome-wide association studies for adiponectin
            levels in East Asians identifies a novel locus near WDR11-FGFR2
  JOURNAL   Hum Mol Genet 23 (4), 1108-1119 (2014)
   PUBMED   24105470
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Kulig,M. and Ecroyd,H.
  TITLE     The small heat-shock protein alphaB-crystallin uses different
            mechanisms of chaperone action to prevent the amorphous versus
            fibrillar aggregation of alpha-lactalbumin
  JOURNAL   Biochem J 448 (3), 343-352 (2012)
   PUBMED   23005341
  REMARK    GeneRIF: High molecular mass complexes are formed with
            alpha-lactalbumin and alphaB-crystallin, preventing the amorphous
            aggregation of alpha-lactalbumin.
REFERENCE   6  (residues 1 to 142)
  AUTHORS   Heine,W.E., Klein,P.D. and Reeds,P.J.
  TITLE     The importance of alpha-lactalbumin in infant nutrition
  JOURNAL   J Nutr 121 (3), 277-283 (1991)
   PUBMED   2002399
  REMARK    Review article
REFERENCE   7  (residues 1 to 142)
  AUTHORS   Davies,M.S., West,L.F., Davis,M.B., Povey,S. and Craig,R.K.
  TITLE     The gene for human alpha-lactalbumin is assigned to chromosome
            12q13
  JOURNAL   Ann Hum Genet 51 (3), 183-188 (1987)
   PUBMED   3479943
REFERENCE   8  (residues 1 to 142)
  AUTHORS   Hall,L., Emery,D.C., Davies,M.S., Parker,D. and Craig,R.K.
  TITLE     Organization and sequence of the human alpha-lactalbumin gene
  JOURNAL   Biochem J 242 (3), 735-742 (1987)
   PUBMED   2954544
REFERENCE   9  (residues 1 to 142)
  AUTHORS   Hall,L., Craig,R.K., Edbrooke,M.R. and Campbell,P.N.
  TITLE     Comparison of the nucleotide sequence of cloned human and
            guinea-pig pre-alpha-lactalbumin cDNA with that of chick
            pre-lysozyme cDNA suggests evolution from a common ancestral gene
  JOURNAL   Nucleic Acids Res 10 (11), 3503-3515 (1982)
   PUBMED   6285305
REFERENCE   10 (residues 1 to 142)
  AUTHORS   Findlay,J.B. and Brew,K.
  TITLE     The complete amino-acid sequence of human -lactalbumin
  JOURNAL   Eur J Biochem 27 (1), 65-86 (1972)
   PUBMED   5049057
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC089987.26.
            
            Summary: This gene encodes alpha-lactalbumin, a principal protein
            of milk. Alpha-lactalbumin forms the regulatory subunit of the
            lactose synthase (LS) heterodimer and beta
            1,4-galactosyltransferase (beta4Gal-T1) forms the catalytic
            component. Together, these proteins enable LS to produce lactose by
            transfering galactose moieties to glucose. As a monomer,
            alpha-lactalbumin strongly binds calcium and zinc ions and may
            possess bactericidal or antitumor activity. A folding variant of
            alpha-lactalbumin, called HAMLET, likely induces apoptosis in tumor
            and immature cells. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.14197.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.11"
     Protein         1..142
                     /product="alpha-lactalbumin precursor"
                     /EC_number="2.4.1.22"
                     /note="lactose synthase B protein; alpha-lactalbumin;
                     lysozyme-like protein 7; lysozyme G"
                     /calculated_mol_wt=14078
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2165
     mat_peptide     20..142
                     /product="Alpha-lactalbumin. /id=PRO_0000018444"
                     /note="propagated from UniProtKB/Swiss-Prot (P00709.1)"
                     /calculated_mol_wt=14078
     Region          20..138
                     /region_name="Lys"
                     /note="C-type lysozyme/alpha-lactalbumin family;
                     pfam00062"
                     /db_xref="CDD:395016"
     Site            order(50..51,62..63,124..125,128..129,133,136..137)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:340384"
     Site            order(50..51,62..63,124..125,128..129,133,136..137)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:340384"
     Site            64
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18780401; propagated from
                     UniProtKB/Swiss-Prot (P00709.1)"
     Site            90
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine, atypical, partial.
                     /evidence=ECO:0000269|Ref.9; propagated from
                     UniProtKB/Swiss-Prot (P00709.1)"
     CDS             1..142
                     /gene="LALBA"
                     /gene_synonym="HAMLET; LYZG"
                     /coded_by="NM_001384350.1:128..556"
                     /db_xref="CCDS:CCDS8765.1"
                     /db_xref="GeneID:3906"
                     /db_xref="HGNC:HGNC:6480"
                     /db_xref="MIM:149750"
ORIGIN      
        1 mrffvplflv gilfpailak qftkcelsql lkdidgyggi alpelictmf htsgydtqai
       61 vennesteyg lfqisnklwc kssqvpqsrn icdiscdkfl ddditddimc akkildikgi
      121 dywlahkalc tekleqwlce kl
//
LOCUS       NP_001036024             869 aa            linear   PRI 21-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4 gamma 2 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001036024
VERSION     NP_001036024.3
DBSOURCE    REFSEQ: accession NM_001042559.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 869)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 869)
  AUTHORS   Shen,Y., Zhang,Y., Wang,Q., Jiang,B., Jiang,X. and Luo,B.
  TITLE     MicroRNA-877-5p promotes osteoblast differentiation by targeting
            EIF4G2 expression
  JOURNAL   J Orthop Surg Res 19 (1), 134 (2024)
   PUBMED   38342889
  REMARK    GeneRIF: MicroRNA-877-5p promotes osteoblast differentiation by
            targeting EIF4G2 expression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 869)
  AUTHORS   Meril,S., Bahlsen,M., Eisenstein,M., Savidor,A., Levin,Y.,
            Bialik,S., Pietrokovski,S. and Kimchi,A.
  TITLE     Loss-of-function cancer-linked mutations in the EIF4G2
            non-canonical translation initiation factor
  JOURNAL   Life Sci Alliance 7 (3), e202302338 (2023)
   PUBMED   38129098
  REMARK    GeneRIF: Loss-of-function cancer-linked mutations in the EIF4G2
            non-canonical translation initiation factor.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 869)
  AUTHORS   Jia,Z., Wang,Y., Gao,J., Zheng,M., Wang,P. and Zu,G.
  TITLE     miR-379-5P INHIBITION ENHANCES INTESTINAL EPITHELIAL PROLIFERATION
            AND BARRIER FUNCTION RECOVERY AFTER ISCHEMIA/REPERFUSION BY
            TARGETING EIF4G2
  JOURNAL   Shock 60 (4), 594-602 (2023)
   PUBMED   37646610
  REMARK    GeneRIF: miR-379-5P INHIBITION ENHANCES INTESTINAL EPITHELIAL
            PROLIFERATION AND BARRIER FUNCTION RECOVERY AFTER
            ISCHEMIA/REPERFUSION BY TARGETING EIF4G2.
REFERENCE   5  (residues 1 to 869)
  AUTHORS   Takahashi,K., Maruyama,M., Tokuzawa,Y., Murakami,M., Oda,Y.,
            Yoshikane,N., Makabe,K.W., Ichisaka,T. and Yamanaka,S.
  TITLE     Evolutionarily conserved non-AUG translation initiation in
            NAT1/p97/DAP5 (EIF4G2)
  JOURNAL   Genomics 85 (3), 360-371 (2005)
   PUBMED   15718103
  REMARK    GeneRIF: Exclusive use of a GUG translation initiation codon is
            conserved in human, chicken, Xenopus, and zebrafish.
REFERENCE   6  (residues 1 to 869)
  AUTHORS   Pyronnet,S., Imataka,H., Gingras,A.C., Fukunaga,R., Hunter,T. and
            Sonenberg,N.
  TITLE     Human eukaryotic translation initiation factor 4G (eIF4G) recruits
            mnk1 to phosphorylate eIF4E
  JOURNAL   EMBO J 18 (1), 270-279 (1999)
   PUBMED   9878069
REFERENCE   7  (residues 1 to 869)
  AUTHORS   Imataka,H. and Sonenberg,N.
  TITLE     Human eukaryotic translation initiation factor 4G (eIF4G) possesses
            two separate and independent binding sites for eIF4A
  JOURNAL   Mol Cell Biol 17 (12), 6940-6947 (1997)
   PUBMED   9372926
REFERENCE   8  (residues 1 to 869)
  AUTHORS   Levy-Strumpf,N., Deiss,L.P., Berissi,H. and Kimchi,A.
  TITLE     DAP-5, a novel homolog of eukaryotic translation initiation factor
            4G isolated as a putative modulator of gamma interferon-induced
            programmed cell death
  JOURNAL   Mol Cell Biol 17 (3), 1615-1625 (1997)
   PUBMED   9032289
REFERENCE   9  (residues 1 to 869)
  AUTHORS   Imataka,H., Olsen,H.S. and Sonenberg,N.
  TITLE     A new translational regulator with homology to eukaryotic
            translation initiation factor 4G
  JOURNAL   EMBO J 16 (4), 817-825 (1997)
   PUBMED   9049310
  REMARK    GeneRIF: translation starts exclusively at a non-AUG translation
            initiation codon (GUG).
REFERENCE   10 (residues 1 to 869)
  AUTHORS   Shaughnessy,J.D. Jr., Jenkins,N.A. and Copeland,N.G.
  TITLE     cDNA cloning, expression analysis, and chromosomal localization of
            a gene with high homology to wheat eIF-(iso)4F and mammalian eIF-4G
  JOURNAL   Genomics 39 (2), 192-197 (1997)
   PUBMED   9027506
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB072494.1, BC111548.1,
            DB272352.1 and AI362365.1.
            
            On Feb 25, 2010 this sequence version replaced NP_001036024.2.
            
            Summary: Translation initiation is mediated by specific recognition
            of the cap structure by eukaryotic translation initiation factor 4F
            (eIF4F), which is a cap binding protein complex that consists of
            three subunits: eIF4A, eIF4E and eIF4G. The protein encoded by this
            gene shares similarity with the C-terminal region of eIF4G that
            contains the binding sites for eIF4A and eIF3; eIF4G, in addition,
            contains a binding site for eIF4E at the N-terminus. Unlike eIF4G,
            which supports cap-dependent and independent translation, this gene
            product functions as a general repressor of translation by forming
            translationally inactive complexes. In vitro and in vivo studies
            indicate that translation of this mRNA initiates exclusively at a
            non-AUG (GUG) codon. Alternatively spliced transcript variants
            encoding different isoforms of this gene have been described.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the central coding region, compared to variant 1, resulting
            in a shorter isoform (2), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853566.4283.1,
                                           SRR11853564.4459.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            non-AUG initiation codon :: PMID: 9049310, 15718103
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..869
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..869
                     /product="eukaryotic translation initiation factor 4 gamma
                     2 isoform 2"
                     /note="eIF-4-gamma 2; eukaryotic translation initiation
                     factor 4G-like 1; death-associated protein 5;
                     aging-associated protein 1; DAP-5; eIF4G 2; eIF-4G 2"
                     /calculated_mol_wt=98020
     Region          78..308
                     /region_name="MIF4G"
                     /note="MIF4G domain; pfam02854"
                     /db_xref="CDD:397130"
     Region          <439..>505
                     /region_name="PRK12757"
                     /note="cell division protein FtsN; Provisional"
                     /db_xref="CDD:237191"
     Region          506..619
                     /region_name="MA3"
                     /note="Domain in DAP-5, eIF4G, MA-3 and other proteins;
                     smart00544"
                     /db_xref="CDD:214714"
     Region          702..838
                     /region_name="W2_eIF4G1_like"
                     /note="C-terminal W2 domain of eukaryotic translation
                     initiation factor 4 gamma 1 and similar proteins; cd11559"
                     /db_xref="CDD:211397"
     CDS             1..869
                     /gene="EIF4G2"
                     /gene_synonym="AAG1; DAP5; NAT1; P97"
                     /coded_by="NM_001042559.3:309..2918"
                     /note="isoform 2 is encoded by transcript variant 2;
                     non-AUG (GUG) translation initiation codon"
                     /db_xref="CCDS:CCDS41618.1"
                     /db_xref="GeneID:1982"
                     /db_xref="HGNC:HGNC:3297"
                     /db_xref="MIM:602325"
ORIGIN      
        1 mesaiaegga srfsassggg gsrgapqhyp ktagnseflg ktpgqnaqkw iparstrrdd
       61 nsaannsane kerhdaifrk vrgilnkltp ekfdklclel lnvgveskli lkgvillivd
      121 kaleepkyss lyaqlclrla edapnfdgpa aegqpgqkqs ttfrrllisk lqdefenrtr
      181 nvdvydkren pllpeeeeqr aiakikmlgn ikfigelgkl dlihesilhk ciktllekkk
      241 rvqlkdmged leclcqimrt vgprldhera kslmdqyfar mcslmlskel parirfllqd
      301 tvelrehhwv prkafldngp ktinqirqda vkdlgvfipa pmaqgmrsdf flegpfmppr
      361 mkmdrdplgg ladmfgqmpg sgigtgpgvi qdrfsptmgr hrsnqlfngh gghimpptqs
      421 qfgemggkfm ksqislrpaq sflmnknqvp klqpqitmip psaqpprtqt pplgqtpqlg
      481 lktnppliqe kpaktskkpp pskeellklt etvvteylns gnaneavngv remrapkhfl
      541 pemlskviil sldrsdedke kasslisllk qegiatsdnf mqaflnvldq cpklevdipl
      601 vksylaqfaa raiiselvsi selaqplesg thfplfllcl qqlaklqdre wltelfqqsk
      661 vnmqkmlpei dqnkdrmlei legkglsflf pllklekell kqikldpspq tiykwikdni
      721 spklhvdkgf vnilmtsflq yissevnpps detdsssaps keqleqekql llsfkpvmqk
      781 flhdhvdlqv salyalqvhc ynsnfpkgml lrffvhfydm eiieeeafla wkeditqefp
      841 gkgkalfqvn qwltwletae eeeseeead
//
LOCUS       NP_001158018             559 aa            linear   PRI 21-NOV-2025
DEFINITION  disrupted in schizophrenia 1 protein isoform i [Homo sapiens].
ACCESSION   NP_001158018
VERSION     NP_001158018.1
DBSOURCE    REFSEQ: accession NM_001164546.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Pils,M., Rutsch,J., Eren,F., Engberg,G., Piehl,F., Cervenka,S.,
            Sellgren,C., Trossbach,S., Willbold,D., Erhardt,S., Bannach,O. and
            Korth,C.
  TITLE     Disrupted-in-schizophrenia 1 protein aggregates in cerebrospinal
            fluid are elevated in patients with first-episode psychosis
  JOURNAL   Psychiatry Clin Neurosci 77 (12), 665-671 (2023)
   PUBMED   37668563
  REMARK    GeneRIF: Disrupted-in-schizophrenia 1 protein aggregates in
            cerebrospinal fluid are elevated in patients with first-episode
            psychosis.
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Habibi,S., Yaghoubzad-Maleki,M., Heshmati,E. and Khalifeh,K.
  TITLE     Effects of representative point mutations on dynamic behavior of
            the DISC1-Ndel1 complex: a molecular dynamics study
  JOURNAL   J Biomol Struct Dyn 41 (22), 13228-13234 (2023)
   PUBMED   36858606
  REMARK    GeneRIF: Effects of representative point mutations on dynamic
            behavior of the DISC1-Ndel1 complex: a molecular dynamics study.
REFERENCE   4  (residues 1 to 559)
  AUTHORS   Li,W., Jiang,H., Chen,X., Yang,K., Deng,X., Tang,Z., Hu,Z.,
            Zhang,X., Lin,S., Zou,Y. and Wu,H.
  TITLE     The variants in PTPRB, TRAF3IP3, and DISC1 genes were associated
            with Graves' disease in the Chinese population
  JOURNAL   Medicine (Baltimore) 101 (45), e31501 (2022)
   PUBMED   36397361
  REMARK    GeneRIF: The variants in PTPRB, TRAF3IP3, and DISC1 genes were
            associated with Graves' disease in the Chinese population.
REFERENCE   5  (residues 1 to 559)
  AUTHORS   Guardiola-Ripoll,M., Sotero-Moreno,A., Almodovar-Paya,C.,
            Hostalet,N., Guerrero-Pedraza,A., Ramiro,N., Ortiz-Gil,J.,
            Arias,B., Madre,M., Soler-Vidal,J., Salvador,R., McKenna,P.J.,
            Pomarol-Clotet,E. and Fatjo-Vilas,M.
  TITLE     Combining fMRI and DISC1 gene haplotypes to understand working
            memory-related brain activity in schizophrenia
  JOURNAL   Sci Rep 12 (1), 7351 (2022)
   PUBMED   35513527
  REMARK    GeneRIF: Combining fMRI and DISC1 gene haplotypes to understand
            working memory-related brain activity in schizophrenia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 559)
  AUTHORS   Ozeki,Y., Tomoda,T., Kleiderlein,J., Kamiya,A., Bord,L., Fujii,K.,
            Okawa,M., Yamada,N., Hatten,M.E., Snyder,S.H., Ross,C.A. and
            Sawa,A.
  TITLE     Disrupted-in-Schizophrenia-1 (DISC-1): mutant truncation prevents
            binding to NudE-like (NUDEL) and inhibits neurite outgrowth
  JOURNAL   Proc Natl Acad Sci U S A 100 (1), 289-294 (2003)
   PUBMED   12506198
  REMARK    GeneRIF: Mutant truncation prevents binding to NudE-like (NUDEL)
            and inhibits neurite outgrowth
            Erratum:[Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13969]
REFERENCE   7  (residues 1 to 559)
  AUTHORS   Blackwood,D.H., Fordyce,A., Walker,M.T., St Clair,D.M.,
            Porteous,D.J. and Muir,W.J.
  TITLE     Schizophrenia and affective disorders--cosegregation with a
            translocation at chromosome 1q42 that directly disrupts
            brain-expressed genes: clinical and P300 findings in a family
  JOURNAL   Am J Hum Genet 69 (2), 428-433 (2001)
   PUBMED   11443544
REFERENCE   8  (residues 1 to 559)
  AUTHORS   Ekelund,J., Hovatta,I., Parker,A., Paunio,T., Varilo,T., Martin,R.,
            Suhonen,J., Ellonen,P., Chan,G., Sinsheimer,J.S., Sobel,E.,
            Juvonen,H., Arajarvi,R., Partonen,T., Suvisaari,J., Lonnqvist,J.,
            Meyer,J. and Peltonen,L.
  TITLE     Chromosome 1 loci in Finnish schizophrenia families
  JOURNAL   Hum Mol Genet 10 (15), 1611-1617 (2001)
   PUBMED   11468279
REFERENCE   9  (residues 1 to 559)
  AUTHORS   Millar,J.K., Christie,S., Semple,C.A. and Porteous,D.J.
  TITLE     Chromosomal location and genomic structure of the human
            translin-associated factor X gene (TRAX; TSNAX) revealed by
            intergenic splicing to DISC1, a gene disrupted by a translocation
            segregating with schizophrenia
  JOURNAL   Genomics 67 (1), 69-77 (2000)
   PUBMED   10945471
REFERENCE   10 (residues 1 to 559)
  AUTHORS   Millar,J.K., Wilson-Annan,J.C., Anderson,S., Christie,S.,
            Taylor,M.S., Semple,C.A., Devon,R.S., St Clair,D.M., Muir,W.J.,
            Blackwood,D.H. and Porteous,D.J.
  TITLE     Disruption of two novel genes by a translocation co-segregating
            with schizophrenia
  JOURNAL   Hum Mol Genet 9 (9), 1415-1423 (2000)
   PUBMED   10814723
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL626763.11 and FJ804190.1.
            
            Summary: This gene encodes a protein with multiple coiled coil
            motifs which is located in the nucleus, cytoplasm and mitochondria.
            The protein is involved in neurite outgrowth and cortical
            development through its interaction with other proteins. This gene
            is disrupted in a t(1;11)(q42.1;q14.3) translocation which
            segregates with schizophrenia and related psychiatric disorders in
            a large Scottish family. Alternate transcriptional splice variants,
            encoding different isoforms, have been characterized. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (i) lacks three internal exons and
            three 3' exons but has an alternate 3' segment, as compared to
            variant L. Variants i and j encode the same isoform (i), which is
            much shorter and has a distinct C-terminus, as compared to isoform
            L.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ804190.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.2"
     Protein         1..559
                     /product="disrupted in schizophrenia 1 protein isoform i"
                     /note="disrupted in schizophrenia 1 protein"
                     /calculated_mol_wt=60134
     Region          1..292
                     /region_name="Interaction with MAP1A.
                     /evidence=ECO:0000269|PubMed:12812986"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRI5.3)"
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRI5.3)"
     Region          179..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRI5.3)"
     Region          197..203
                     /region_name="Interaction with FBXW7.
                     /evidence=ECO:0000269|PubMed:28727686"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRI5.3)"
     Region          221..257
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRI5.3)"
     Region          278..323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRI5.3)"
     Region          <329..>488
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     CDS             1..559
                     /gene="DISC1"
                     /gene_synonym="C1orf136; SCZD9"
                     /coded_by="NM_001164546.2:79..1758"
                     /note="isoform i is encoded by transcript variant i"
                     /db_xref="CCDS:CCDS53485.1"
                     /db_xref="GeneID:27185"
                     /db_xref="HGNC:HGNC:2888"
                     /db_xref="MIM:605210"
ORIGIN      
        1 mpgggpqgap aaaggggvsh ragsrdclpp aacfrrrrla rrpgymrsst gpgigflspa
       61 vgtlfrfpgg vsgeeshhse srarqcglds rgllvrspvs ksaaaptvts vrgtsahfgi
      121 qlrggtrlpd rlswpcgpgs agwqqefaam dssetldasw eaacsdgarr vraagslpsa
      181 elssnscspg cgpevpptpp gshsaftssf sfirlslgsa gergeaegcp psreaeshcq
      241 spqemgakaa sldgphedpr clsrpfslla trvsadlaqa arnssrperd mhslpdmdpg
      301 ssssldpsla gcggdgssgs gdahswdtll rkwepvlrdc llrnrrqmev islrlklqkl
      361 qedavenddy dkaetlqqrl edleqekisl hfqlpsrqpa lssflghlaa qvqaalrrga
      421 tqqasgddth tplrmeprll eptaqdslhv sitrrdwllq ekqqlqkeie alqarmfvle
      481 akdqqlrrei eeqeqqlqwq gcdltplvgq lslgqlqevs kalqdtlasa gqipfhaepp
      541 etirrnkceg kyyevhgnt
//
LOCUS       NP_001340601             396 aa            linear   PRI 21-NOV-2025
DEFINITION  WD repeat-containing protein 20 isoform 20 [Homo sapiens].
ACCESSION   NP_001340601
VERSION     NP_001340601.1
DBSOURCE    REFSEQ: accession NM_001353672.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Jiang,L., Qi,X., Lai,M., Zhou,J., Yuan,M., You,J., Liu,Q., Pan,J.,
            Zhao,L., Ying,M., Ji,J., Li,K., Zhang,Y., Pan,W., He,Q., Yang,B.
            and Cao,J.
  TITLE     WDR20 prevents hepatocellular carcinoma senescence by orchestrating
            the simultaneous USP12/46-mediated deubiquitination of c-Myc
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2407904121 (2024)
   PUBMED   39432777
  REMARK    GeneRIF: WDR20 prevents hepatocellular carcinoma senescence by
            orchestrating the simultaneous USP12/46-mediated deubiquitination
            of c-Myc.
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Ng,V.H., Spencer,Z., Neitzel,L.R., Nayak,A., Loberg,M.A., Shen,C.,
            Kassel,S.N., Kroh,H.K., An,Z., Anthony,C.C., Bryant,J.M.,
            Lawson,A., Goldsmith,L., Benchabane,H., Hansen,A.G., Li,J.,
            D'Souza,S., Lebensohn,A.M., Rohatgi,R., Weiss,W.A., Weiss,V.L.,
            Williams,C., Hong,C.C., Robbins,D.J., Ahmed,Y. and Lee,E.
  TITLE     The USP46 complex deubiquitylates LRP6 to promote Wnt/beta-catenin
            signaling
  JOURNAL   Nat Commun 14 (1), 6173 (2023)
   PUBMED   37798301
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Olazabal-Herrero,A., Bilbao-Arribas,M., Carlevaris,O., Sendino,M.,
            Varela-Martinez,E., Jugo,B.M., Berra,E. and Rodriguez,J.A.
  TITLE     The dystrophia myotonica WD repeat-containing protein DMWD and
            WDR20 differentially regulate USP12 deubiquitinase
  JOURNAL   FEBS J 288 (20), 5943-5963 (2021)
   PUBMED   33844468
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 396)
  AUTHORS   Dahlberg,C.L. and Juo,P.
  TITLE     The WD40-repeat proteins WDR-20 and WDR-48 bind and activate the
            deubiquitinating enzyme USP-46 to promote the abundance of the
            glutamate receptor GLR-1 in the ventral nerve cord of
            Caenorhabditis elegans
  JOURNAL   J Biol Chem 289 (6), 3444-3456 (2014)
   PUBMED   24356955
REFERENCE   8  (residues 1 to 396)
  AUTHORS   Kee,Y., Yang,K., Cohn,M.A., Haas,W., Gygi,S.P. and D'Andrea,A.D.
  TITLE     WDR20 regulates activity of the USP12 x UAF1 deubiquitinating
            enzyme complex
  JOURNAL   J Biol Chem 285 (15), 11252-11257 (2010)
   PUBMED   20147737
  REMARK    GeneRIF: WDR20 serves as a stimulatory subunit for preserving and
            regulating the activity of the subset of the UAF1 x USP12 complexes
REFERENCE   9  (residues 1 to 396)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   10 (residues 1 to 396)
  AUTHORS   Smith,T.F.
  TITLE     Diversity of WD-repeat proteins
  JOURNAL   Subcell Biochem 48, 20-30 (2008)
   PUBMED   18925368
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133223.5 and AL359402.3.
            
            Summary: This gene encodes a WD repeat-containing protein that
            functions to preserve and regulate the activity of the USP12-UAF1
            deubiquitinating enzyme complex. Multiple alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Jun 2011].
            
            Transcript Variant: This variant (28), as well as variants 24-27,
            29, and 30, encodes isoform 20.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4500136.1,
                                           SRR1803612.132938.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.31"
     Protein         1..396
                     /product="WD repeat-containing protein 20 isoform 20"
                     /note="WD repeat-containing protein 20"
                     /calculated_mol_wt=43418
     Region          <35..141
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          50..86
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          93..126
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..396
                     /gene="WDR20"
                     /gene_synonym="Bun107; DMR"
                     /coded_by="NM_001353672.2:455..1645"
                     /note="isoform 20 is encoded by transcript variant 28"
                     /db_xref="GeneID:91833"
                     /db_xref="HGNC:HGNC:19667"
                     /db_xref="MIM:617741"
ORIGIN      
        1 mylynvehtc gttaphyqll kqgesfavht ckskstrnpl lkwtvgegal nefafspdgk
       61 flacvsqdgf lrvfnfdsve lhgtmksyfg gllcvcwspd gkyivtgged dlvtvwsfvd
      121 crviarghgh kswvsvvafd pyttsveegd pmefsgsded fqdllhfgrd ranstqsrls
      181 krnstdsrpv svtyrfgsvg qdtqlclwdl tedilfphqp lsrarthtnv mnatsppags
      241 ngnsvttpgn svppplprsn slphsavsna gskssvmdga iasgvskfat lslhdrkerh
      301 hekdhkrnhs mghisskssd klnlvtktkt dpaktlgtpl cprmedvpll eplickkiah
      361 erltvlifle dcivtacqeg fictwgrpgk vvsfnp
//
LOCUS       NP_001171591             451 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 1 isoform g [Homo sapiens].
ACCESSION   NP_001171591
VERSION     NP_001171591.1
DBSOURCE    REFSEQ: accession NM_001178120.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Petersen,M. and Dubielecka,P.
  TITLE     Adaptor protein Abelson interactor 1 in homeostasis and disease
  JOURNAL   Cell Commun Signal 22 (1), 468 (2024)
   PUBMED   39354505
  REMARK    GeneRIF: Adaptor protein Abelson interactor 1 in homeostasis and
            disease.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Jin,M., Xie,M., Liu,Y., Song,H., Zhang,M., Li,W., Li,X., Jia,N.,
            Dong,L., Lu,Q., Xue,F., Yan,L. and Yu,Q.
  TITLE     Circulating miR-30e-3p induces disruption of neurite development in
            SH-SY5Y cells by targeting ABI1, a novel biomarker for
            schizophrenia
  JOURNAL   J Psychiatr Res 174, 84-93 (2024)
   PUBMED   38626565
  REMARK    GeneRIF: Circulating miR-30e-3p induces disruption of neurite
            development in SH-SY5Y cells by targeting ABI1, a novel biomarker
            for schizophrenia.
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Lin,T., Guo,J., Peng,Y., Li,M., Liu,Y., Yu,X., Wu,N. and Yu,W.
  TITLE     Pan-cancer transcriptomic data of ABI1 transcript variants and
            molecular constitutive elements identifies novel cancer metastatic
            and prognostic biomarkers
  JOURNAL   Cancer Biomark 39 (1), 49-62 (2024)
   PUBMED   37545215
  REMARK    GeneRIF: Pan-cancer transcriptomic data of ABI1 transcript variants
            and molecular constitutive elements identifies novel cancer
            metastatic and prognostic biomarkers.
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Fan,P.D. and Goff,S.P.
  TITLE     Abl interactor 1 binds to sos and inhibits epidermal growth factor-
            and v-Abl-induced activation of extracellular signal-regulated
            kinases
  JOURNAL   Mol Cell Biol 20 (20), 7591-7601 (2000)
   PUBMED   11003655
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Scita,G., Nordstrom,J., Carbone,R., Tenca,P., Giardina,G.,
            Gutkind,S., Bjarnegard,M., Betsholtz,C. and Di Fiore,P.P.
  TITLE     EPS8 and E3B1 transduce signals from Ras to Rac
  JOURNAL   Nature 401 (6750), 290-293 (1999)
   PUBMED   10499589
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Taki,T., Shibuya,N., Taniwaki,M., Hanada,R., Morishita,K.,
            Bessho,F., Yanagisawa,M. and Hayashi,Y.
  TITLE     ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL
            gene in acute myeloid leukemia with t(10;11)(p11.2;q23)
  JOURNAL   Blood 92 (4), 1125-1130 (1998)
   PUBMED   9694699
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Ziemnicka-Kotula,D., Xu,J., Gu,H., Potempska,A., Kim,K.S.,
            Jenkins,E.C., Trenkner,E. and Kotula,L.
  TITLE     Identification of a candidate human spectrin Src homology 3
            domain-binding protein suggests a general mechanism of association
            of tyrosine kinases with the spectrin-based membrane skeleton
  JOURNAL   J Biol Chem 273 (22), 13681-13692 (1998)
   PUBMED   9593709
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Biesova,Z., Piccoli,C. and Wong,W.T.
  TITLE     Isolation and characterization of e3B1, an eps8 binding protein
            that regulates cell growth
  JOURNAL   Oncogene 14 (2), 233-241 (1997)
   PUBMED   9010225
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB040151.1, AF001628.2 and
            AL390961.17.
            
            Summary: This gene encodes a member of the Abelson-interactor
            family of adaptor proteins. These proteins facilitate signal
            transduction as components of several multiprotein complexes, and
            regulate actin polymerization and cytoskeletal remodeling through
            interactions with Abelson tyrosine kinases. The encoded protein
            plays a role in macropinocytosis as a component of the WAVE2
            complex, and also forms a complex with EPS8 and SOS1 that mediates
            signal transduction from Ras to Rac. This gene may play a role in
            the progression of several malignancies including melanoma, colon
            cancer and breast cancer, and a t(10;11) chromosomal translocation
            involving this gene and the MLL gene has been associated with acute
            myeloid leukemia. Alternatively spliced transcript variants
            encoding multiple isoforms have been observed for this gene, and a
            pseudogene of this gene is located on the long arm of chromosome
            14. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (7) lacks two alternate in-frame
            coding exons and uses a different splice site, compared to variant
            1. The resulting protein (isoform g) has the same N- and C-termini
            but is shorter when it is compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB209268.1, AF001628.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.1"
     Protein         1..451
                     /product="abl interactor 1 isoform g"
                     /note="nap1 binding protein; interactor protein AblBP4;
                     Abl-interactor protein 1 long; Abelson interactor 1;
                     abl-binding protein 4; eps8 SH3 domain-binding protein;
                     spectrin SH3 domain-binding protein 1"
                     /calculated_mol_wt=49174
     Region          93..156
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          393..451
                     /region_name="SH3_Abi1"
                     /note="Src homology 3 domain of Abl Interactor 1; cd11971"
                     /db_xref="CDD:212904"
     Site            order(398,400,403,407,425..426,439,441..442)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212904"
     CDS             1..451
                     /gene="ABI1"
                     /gene_synonym="ABI-1; ABLBP4; E3B1; NAP1BP; SSH3BP;
                     SSH3BP1"
                     /coded_by="NM_001178120.2:96..1451"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS53499.1"
                     /db_xref="GeneID:10006"
                     /db_xref="HGNC:HGNC:11320"
                     /db_xref="MIM:603050"
ORIGIN      
        1 maelqmllee eipsgkrali esyqnltrva dycennyiqa tdkrkaleet kayttqslas
       61 vayqinalan nvlqlldiqa sqlrrmessi nhisqtvdih kekvarreig ilttnkntsr
      121 thkiiapanm erpvryirkp idytvlddvg hgvkwlkakh gnnqpartgt lsrtnpptqk
      181 ppsppmsgrg tlgrntpykt lepvkpptvp ndymtsparl gsqhspgrta slnqrprths
      241 gssggsgsre nsgsssigip iavptpsppt igpapgsapg sqygtmtrqi srhnsttsst
      301 ssggyrrtps vtaqfsaqph vnggplysqn siadsptppp ppppddipmf ddsppppppp
      361 pvdyedeeaa vvqyndpyad gdpawapkny iekvvaiydy tkdkddelsf megaiiyvik
      421 knddgwyegv cnrvtglfpg nyvesimhyt d
//
LOCUS       NP_001372194             184 aa            linear   PRI 21-NOV-2025
DEFINITION  protein tyrosine phosphatase type IVA 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001372194
VERSION     NP_001372194.1
DBSOURCE    REFSEQ: accession NM_001385265.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Cho,M.J., Lee,D.G., Lee,J.W., Hwang,B., Yoon,S.J., Lee,S.J.,
            Park,Y.J., Park,S.H., Lee,H.G., Kim,Y.H., Lee,C.H., Lee,J.,
            Lee,N.K., Han,T.S., Cho,H.S., Moon,J.H., Lee,G.S., Bae,K.H.,
            Hwang,G.S., Lee,S.H., Chung,S.J., Shim,S., Cho,J., Oh,G.T.,
            Kwon,Y.G., Park,J.G. and Min,J.K.
  TITLE     Endothelial PTP4A1 mitigates vascular inflammation via USF1/A20
            axis-mediated NF-kappaB inactivation
  JOURNAL   Cardiovasc Res 119 (5), 1265-1278 (2023)
   PUBMED   36534975
  REMARK    GeneRIF: Endothelial PTP4A1 mitigates vascular inflammation via
            USF1/A20 axis-mediated NF-kappaB inactivation.
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Hu,H., Ye,L. and Liu,Z.
  TITLE     GINS2 regulates the proliferation and apoptosis of colon cancer
            cells through PTP4A1
  JOURNAL   Mol Med Rep 25 (4) (2022)
   PUBMED   35137928
  REMARK    GeneRIF: GINS2 regulates the proliferation and apoptosis of colon
            cancer cells through PTP4A1.
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Li,O., Jiang,B., Yi,W.M., Zhang,Y., Yang,P.Z., Guo,C., Sun,Z.P. and
            Peng,C.
  TITLE     LncRNA NEAT1 promotes cell proliferation, migration, and invasion
            via the miR-186-5p/PTP4A1 axis in cholangiocarcinoma
  JOURNAL   Kaohsiung J Med Sci 37 (5), 379-391 (2021)
   PUBMED   33502823
  REMARK    GeneRIF: LncRNA NEAT1 promotes cell proliferation, migration, and
            invasion via the miR-186-5p/PTP4A1 axis in cholangiocarcinoma.
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Andreev,D.E., O'Connor,P.B., Fahey,C., Kenny,E.M., Terenin,I.M.,
            Dmitriev,S.E., Cormican,P., Morris,D.W., Shatsky,I.N. and
            Baranov,P.V.
  TITLE     Translation of 5' leaders is pervasive in genes resistant to eIF2
            repression
  JOURNAL   Elife 4, e03971 (2015)
   PUBMED   25621764
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 184)
  AUTHORS   Tsujimoto,H., Nishizuka,S., Redpath,J.L. and Stanbridge,E.J.
  TITLE     Differential gene expression in tumorigenic and nontumorigenic HeLa
            x normal human fibroblast hybrid cells
  JOURNAL   Mol Carcinog 26 (4), 298-304 (1999)
   PUBMED   10569806
REFERENCE   8  (residues 1 to 184)
  AUTHORS   Peng,Y., Genin,A., Spinner,N.B., Diamond,R.H. and Taub,R.
  TITLE     The gene encoding human nuclear protein tyrosine phosphatase,
            PRL-1. Cloning, chromosomal localization, and identification of an
            intron enhancer
  JOURNAL   J Biol Chem 273 (27), 17286-17295 (1998)
   PUBMED   9642300
REFERENCE   9  (residues 1 to 184)
  AUTHORS   Dayton,M.A. and Knobloch,T.J.
  TITLE     Multiple phosphotyrosine phosphatase mRNAs are expressed in the
            human lung fibroblast cell line WI-38
  JOURNAL   Recept Signal Transduct 7 (4), 241-256 (1997)
   PUBMED   9633825
REFERENCE   10 (residues 1 to 184)
  AUTHORS   Cates,C.A., Michael,R.L., Stayrook,K.R., Harvey,K.A., Burke,Y.D.,
            Randall,S.K., Crowell,P.L. and Crowell,D.N.
  TITLE     Prenylation of oncogenic human PTP(CAAX) protein tyrosine
            phosphatases
  JOURNAL   Cancer Lett 110 (1-2), 49-55 (1996)
   PUBMED   9018080
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL135905.6.
            
            Summary: This gene encodes a member of a small class of prenylated
            protein tyrosine phosphatases (PTPs), which contain a PTP domain
            and a characteristic C-terminal prenylation motif. The encoded
            protein is a cell signaling molecule that plays regulatory roles in
            a variety of cellular processes, including cell proliferation and
            migration. The protein may also be involved in cancer development
            and metastasis. This tyrosine phosphatase is a nuclear protein, but
            may associate with plasma membrane by means of its prenylation
            motif. Pseudogenes related to this gene are located on chromosomes
            1, 2, 5, 7, 11 and X. [provided by RefSeq, Jun 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2544779.1,
                                           SRR14038192.3148661.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q12"
     Protein         1..184
                     /product="protein tyrosine phosphatase type IVA 1 isoform
                     3"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase type IVA protein 1;
                     protein-tyrosine phosphatase of regenerating liver 1;
                     PVT1/PTP4A1 fusion; protein tyrosine phosphatase type IVA,
                     member 1"
                     /calculated_mol_wt=20120
     Region          1..135
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     Region          97..132
                     /region_name="Interaction with ATF5.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93096.2)"
     CDS             1..184
                     /gene="PTP4A1"
                     /gene_synonym="HH72; PRL-1; PRL1; PTP(CAAX1); PTPCAAX1"
                     /coded_by="NM_001385265.1:686..1240"
                     /note="isoform 3 is encoded by transcript variant 11"
                     /db_xref="GeneID:7803"
                     /db_xref="HGNC:HGNC:9634"
                     /db_xref="MIM:601585"
ORIGIN      
        1 marmnrpapv evtyknmrfl ithnptnatl nkfieelkky gvttivrvce atydttlvek
       61 egihvldwpf ddgappsnqi vddwlslvki kfreepgcci avhcvaglgr apvlvalali
      121 eggmkyedav qfirhgvell tasnfciwrs ivlkcgcvsk iptviettva fnkigvpnat
      181 gsgt
//
LOCUS       NP_001231800             749 aa            linear   PRI 21-NOV-2025
DEFINITION  disabled homolog 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001231800
VERSION     NP_001231800.1
DBSOURCE    REFSEQ: accession NM_001244871.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 749)
  AUTHORS   Price,Z.K., Lokman,N.A., Sugiyama,M., Koya,Y., Yoshihara,M.,
            Oehler,M.K., Kajiyama,H. and Ricciardelli,C.
  TITLE     Disabled-2: a protein up-regulated by high molecular weight
            hyaluronan has both tumor promoting and tumor suppressor roles in
            ovarian cancer
  JOURNAL   Cell Mol Life Sci 80 (11), 320 (2023)
   PUBMED   37815603
  REMARK    GeneRIF: Disabled-2: a protein up-regulated by high molecular
            weight hyaluronan has both tumor promoting and tumor suppressor
            roles in ovarian cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 749)
  AUTHORS   Li,Y.P., Adi,D., Wang,Y.H., Wang,Y.T., Li,X.L., Fu,Z.Y., Liu,F.,
            Aizezi,A., Abuzhalihan,J., Gai,M., Ma,X., Li,X.M., Xie,X. and Ma,Y.
  TITLE     Genetic polymorphism of the Dab2 gene and its association with Type
            2 Diabetes Mellitus in the Chinese Uyghur population
  JOURNAL   PeerJ 11, e15536 (2023)
   PUBMED   37361044
  REMARK    GeneRIF: Genetic polymorphism of the Dab2 gene and its association
            with Type 2 Diabetes Mellitus in the Chinese Uyghur population.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 749)
  AUTHORS   Price,Z.K., Lokman,N.A., Yoshihara,M., Kajiyama,H., Oehler,M.K. and
            Ricciardelli,C.
  TITLE     Disabled-2 (DAB2): A Key Regulator of Anti- and Pro-Tumorigenic
            Pathways
  JOURNAL   Int J Mol Sci 24 (1), 696 (2022)
   PUBMED   36614139
  REMARK    GeneRIF: Disabled-2 (DAB2): A Key Regulator of Anti- and
            Pro-Tumorigenic Pathways.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 749)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 749)
  AUTHORS   Fazili,Z., Sun,W., Mittelstaedt,S., Cohen,C. and Xu,X.X.
  TITLE     Disabled-2 inactivation is an early step in ovarian tumorigenicity
  JOURNAL   Oncogene 18 (20), 3104-3113 (1999)
   PUBMED   10340382
REFERENCE   7  (residues 1 to 749)
  AUTHORS   Mok,S.C., Chan,W.Y., Wong,K.K., Cheung,K.K., Lau,C.C., Ng,S.W.,
            Baldini,A., Colitti,C.V., Rock,C.O. and Berkowitz,R.S.
  TITLE     DOC-2, a candidate tumor suppressor gene in human epithelial
            ovarian cancer
  JOURNAL   Oncogene 16 (18), 2381-2387 (1998)
   PUBMED   9620555
REFERENCE   8  (residues 1 to 749)
  AUTHORS   Xu,X.X., Yi,T., Tang,B. and Lambeth,J.D.
  TITLE     Disabled-2 (Dab2) is an SH3 domain-binding partner of Grb2
  JOURNAL   Oncogene 16 (12), 1561-1569 (1998)
   PUBMED   9569023
REFERENCE   9  (residues 1 to 749)
  AUTHORS   Albertsen,H.M., Smith,S.A., Melis,R., Williams,B., Holik,P.,
            Stevens,J. and White,R.
  TITLE     Sequence, genomic structure, and chromosomal assignment of human
            DOC-2
  JOURNAL   Genomics 33 (2), 207-213 (1996)
   PUBMED   8660969
REFERENCE   10 (residues 1 to 749)
  AUTHORS   Mok,S.C., Wong,K.K., Chan,R.K., Lau,C.C., Tsao,S.W., Knapp,R.C. and
            Berkowitz,R.S.
  TITLE     Molecular cloning of differentially expressed genes in human
            epithelial ovarian cancer
  JOURNAL   Gynecol Oncol 52 (2), 247-252 (1994)
   PUBMED   8314147
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB989218.1, AF188298.1,
            U53446.1, AK130136.1 and AI739507.1.
            
            Summary: This gene encodes a mitogen-responsive phosphoprotein. It
            is expressed in normal ovarian epithelial cells, but is
            down-regulated or absent from ovarian carcinoma cell lines,
            suggesting its role as a tumor suppressor. This protein binds to
            the SH3 domains of GRB2, an adaptor protein that couples tyrosine
            kinase receptors to SOS (a guanine nucleotide exchange factor for
            Ras), via its C-terminal proline-rich sequences, and may thus
            modulate growth factor/Ras pathways by competing with SOS for
            binding to GRB2. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Transcript Variant: This variant (2) lacks an in-frame coding exon
            compared to variant 1. This results in a shorter isoform (2)
            missing an internal protein segment compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2229717.1,
                                           SRR14038191.4008818.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.1"
     Protein         1..749
                     /product="disabled homolog 2 isoform 2"
                     /note="disabled homolog 2, mitogen-responsive
                     phosphoprotein; adaptor molecule disabled-2; DAB2,
                     clathrin adaptor protein; differentially expressed in
                     ovarian carcinoma 2; Dab, mitogen-responsive
                     phosphoprotein, homolog 2; differentially-expressed
                     protein 2"
                     /calculated_mol_wt=80098
     Region          35..172
                     /region_name="PTB_Dab"
                     /note="Disabled (Dab) Phosphotyrosine-binding domain;
                     cd01215"
                     /db_xref="CDD:269926"
     Site            order(53,87,89..90,132,150)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269926"
     Site            order(64,118..122,139,159,162..163,166)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:269926"
     CDS             1..749
                     /gene="DAB2"
                     /gene_synonym="DOC-2; DOC2"
                     /coded_by="NM_001244871.2:279..2528"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58946.1"
                     /db_xref="GeneID:1601"
                     /db_xref="HGNC:HGNC:2662"
                     /db_xref="MIM:601236"
ORIGIN      
        1 msnevetsat ngqpdqqaap kapskkekkk gpektdeyll arfkgdgvky kakligiddv
       61 pdargdkmsq dsmmklkgma aagrsqgqhk qriwvnisls gikiidektg viehehpvnk
      121 isfiardvtd nrafgyvcgg egqhqffaik tgqqaeplvv dlkdlfqviy nvkkkeeekk
      181 kieeaskave ngsealmild dqtnklkses kdillvdlns eidtnqnslr enpfltngit
      241 scslprptpq asflpenafs anlnffptpn pdpfrddpft qpdqstpssf dslkspdqkk
      301 enssssstpl sngplngdvd yfgqqfdqis nrtgkqeaqa gpwpfsssqt qpavrtqngv
      361 sereqngfsv ksspnpfvgs ppkglsiqng vkqdlessvq ssphdsiaii pppqstkpgr
      421 grrtakssan dllasdifap pvsepsgqas ptgqptalqp npldlfktsa papvgplvgl
      481 ggvtvtlpqa gpwntaslvf nqspsmapga mmggqpsgfs qpvifgtspa vsgwnqpspf
      541 aastpppvpv vwgpsasvap nawsttsplg npfqsnifpa pavstqppsm hssllvtppq
      601 pppragppkd issdaftald plgdkeikdv kemfkdfqlr qppavparkg eqtssgtlsa
      661 fasyfnskvg ipqenadhdd fdanqllnki neppkpaprq vslpvtkstd nafenpffkd
      721 sfgssqasva ssqpvssemy rdpfgnpfa
//
LOCUS       NP_001387292             249 aa            linear   PRI 21-NOV-2025
DEFINITION  single-stranded DNA-binding protein 2 isoform 30 [Homo sapiens].
ACCESSION   NP_001387292
VERSION     NP_001387292.1
DBSOURCE    REFSEQ: accession NM_001400363.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Schwab,C., Roberts,K., Boer,J.M., Gohring,G., Steinemann,D.,
            Vora,A., Macartney,C., Hough,R., Thorn,Z., Dillon,R., Escherich,G.,
            Cazzaniga,G., Schlegelberger,B., Loh,M., den Boer,M.L.,
            Moorman,A.V. and Harrison,C.J.
  TITLE     SSBP2-CSF1R is a recurrent fusion in B-lineage acute lymphoblastic
            leukemia with diverse genetic presentation and variable outcome
  JOURNAL   Blood 137 (13), 1835-1838 (2021)
   PUBMED   33197935
  REMARK    GeneRIF: SSBP2-CSF1R is a recurrent fusion in B-lineage acute
            lymphoblastic leukemia with diverse genetic presentation and
            variable outcome.
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Wang,H., Kim,J., Wang,Z., Yan,X.X., Dean,A. and Xu,W.
  TITLE     Crystal structure of human LDB1 in complex with SSBP2
  JOURNAL   Proc Natl Acad Sci U S A 117 (2), 1042-1048 (2020)
   PUBMED   31892537
  REMARK    GeneRIF: Single-stranded DNA binding proteins (SSBPs) interact
            specifically with the LDB/Chip conserved domain (LCCD) of LDB
            proteins and stabilize LDBs by preventing their proteasomal
            degradation, thus promoting their functions in gene regulation.
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Kim,H., Kim,Y., Bang,S., Park,S., Jee,S., Sim,J., Shin,S.J.,
            Paik,S.S. and Jang,K.
  TITLE     Low Expression of Single-stranded DNA Binding Protein 2 (SSBP2)
            Predicts Unfavourable Postoperative Outcomes in Patients With Clear
            Cell Renal Cell Carcinoma
  JOURNAL   In Vivo 34 (1), 101-107 (2020)
   PUBMED   31882468
  REMARK    GeneRIF: CcRCC with low SSBP2 expression was associated with
            adverse clinicopathological characteristics and poor patient
            outcomes.
REFERENCE   6  (residues 1 to 249)
  AUTHORS   Fleisig,H.B., Orazio,N.I., Liang,H., Tyler,A.F., Adams,H.P.,
            Weitzman,M.D. and Nagarajan,L.
  TITLE     Adenoviral E1B55K oncoprotein sequesters candidate leukemia
            suppressor sequence-specific single-stranded DNA-binding protein 2
            into aggresomes
  JOURNAL   Oncogene 26 (33), 4797-4805 (2007)
   PUBMED   17311003
  REMARK    GeneRIF: Results suggest that subverting SSBP2 function by
            oncoprotein E1B55K may contribute to cell transformation by viral
            oncoproteins.
REFERENCE   7  (residues 1 to 249)
  AUTHORS   Liang,H., Samanta,S. and Nagarajan,L.
  TITLE     SSBP2, a candidate tumor suppressor gene, induces growth arrest and
            differentiation of myeloid leukemia cells
  JOURNAL   Oncogene 24 (16), 2625-2634 (2005)
   PUBMED   15782145
  REMARK    GeneRIF: Our findings are consistent with human SSBP2 being a novel
            regulator of hematopoietic growth and differentiation, whose loss
            confers a block in differentiation advantage to myeloid leukemic
            cells.
REFERENCE   8  (residues 1 to 249)
  AUTHORS   Castro,P., Liang,H., Liang,J.C. and Nagarajan,L.
  TITLE     A novel, evolutionarily conserved gene family with putative
            sequence-specific single-stranded DNA-binding activity
  JOURNAL   Genomics 80 (1), 78-85 (2002)
   PUBMED   12079286
  REMARK    GeneRIF: Member of a closely related, evolutionarily conserved, and
            ubiquitously expressed gene family, potential tumor suppressor
REFERENCE   9  (residues 1 to 249)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 249)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016562.7, AC093250.3,
            AC026419.5 and AC010623.10.
            
            Summary: This gene encodes a subunit of a protein complex that
            interacts with single-stranded DNA and is involved in the DNA
            damage response and maintenance of genome stability. The encoded
            protein may also play a role in telomere repair. A variant of this
            gene may be associated with survival in human glioblastoma
            patients. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.160202.1,
                                           SRR14038194.850067.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.1"
     Protein         1..249
                     /product="single-stranded DNA-binding protein 2 isoform
                     30"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein 2"
                     /calculated_mol_wt=25293
     Region          <12..226
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     CDS             1..249
                     /gene="SSBP2"
                     /gene_synonym="HSPC116; SOSS-B2"
                     /coded_by="NM_001400363.1:319..1068"
                     /note="isoform 30 is encoded by transcript variant 35"
                     /db_xref="GeneID:23635"
                     /db_xref="HGNC:HGNC:15831"
                     /db_xref="MIM:607389"
ORIGIN      
        1 mpvgpvppgf fqpfmspryp ggprpplrip nqalggvpgs qpllpsgmdp trqqghpnmg
       61 gpmqrmtppr gmvplgpqny ggamrpplna lggpgmpgmn mgpgggrpwp nptnansipy
      121 ssaspgnyvg ppggggppgt pimpspadst nsgdnmytlm navppgpnrp nfpmgpgsdg
      181 pmgglggmes hhmngslgsg dmdsisknsp nnmslsnqpg tprddgemgg nflnpfqses
      241 yspsmtmsv
//
LOCUS       NP_001344937             526 aa            linear   PRI 21-NOV-2025
DEFINITION  germ cell-less protein-like 2 [Homo sapiens].
ACCESSION   NP_001344937 NP_071916
VERSION     NP_001344937.1
DBSOURCE    REFSEQ: accession NM_001358008.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Padyukov,L., Seielstad,M., Ong,R.T., Ding,B., Ronnelid,J.,
            Seddighzadeh,M., Alfredsson,L. and Klareskog,L.
  CONSRTM   Epidemiological Investigation of Rheumatoid Arthritis (EIRA) study
            group
  TITLE     A genome-wide association study suggests contrasting associations
            in ACPA-positive versus ACPA-negative rheumatoid arthritis
  JOURNAL   Ann Rheum Dis 70 (2), 259-265 (2011)
   PUBMED   21156761
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Marques,A.C., Dupanloup,I., Vinckenbosch,N., Reymond,A. and
            Kaessmann,H.
  TITLE     Emergence of young human genes after a burst of retroposition in
            primates
  JOURNAL   PLoS Biol 3 (11), e357 (2005)
   PUBMED   16201836
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Tao,W.A., Wollscheid,B., O'Brien,R., Eng,J.K., Li,X.J.,
            Bodenmiller,B., Watts,J.D., Hood,L. and Aebersold,R.
  TITLE     Quantitative phosphoproteome analysis using a dendrimer conjugation
            chemistry and tandem mass spectrometry
  JOURNAL   Nat Methods 2 (8), 591-598 (2005)
   PUBMED   16094384
REFERENCE   6  (residues 1 to 526)
  AUTHORS   Furukawa,M., He,Y.J., Borchers,C. and Xiong,Y.
  TITLE     Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin
            ligases
  JOURNAL   Nat Cell Biol 5 (11), 1001-1007 (2003)
   PUBMED   14528312
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC033886.2 and AC136632.3.
            
            On Jul 29, 2022 this sequence version replaced NP_071916.2.
            
            Summary: This locus shares a high degree of identity with the
            multi-exon germ cell-less gene on chromosome 2. Despite its
            single-exon nature, this chromosome 5 locus contains an open
            reading frame that could putatively encode a full-length germ
            cell-less related protein. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC024185.1, AK315701.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000463439.3/ ENSP00000497178.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..526
                     /product="germ cell-less protein-like 2"
                     /note="germ cell-less related; putative germ cell-less
                     protein-like 1-like; germ cell-less, spermatogenesis
                     associated 2"
                     /calculated_mol_wt=60168
     Region          1..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEA9.2)"
     Region          49..55
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEA9.2)"
     Region          85..91
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEA9.2)"
     Region          93..207
                     /region_name="BTB_POZ_GCL"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Drosophila
                     melanogaster protein germ cell-less (GCL) and similar
                     proteins; cd18305"
                     /db_xref="CDD:349614"
     Region          208..285
                     /region_name="BACK_GCL"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Drosophila melanogaster protein germ cell-less (GCL) and
                     similar proteins; cd18495"
                     /db_xref="CDD:350570"
     CDS             1..526
                     /gene="GMCL2"
                     /gene_synonym="GCL; GMCL1L; GMCL1P1"
                     /coded_by="NM_001358008.2:73..1653"
                     /db_xref="CCDS:CCDS4433.1"
                     /db_xref="GeneID:64396"
                     /db_xref="HGNC:HGNC:19717"
                     /db_xref="MIM:618629"
ORIGIN      
        1 mgssssrvlg qprralaqqe qgarargsar rpdtgddaas ygfcycpgsh krkrssgacr
       61 ycdpdshree heeegdkqqp llntparkkl rstskyiyqt lflngensdi kicalgeewr
      121 lhkiylcqsg yfssmfsgsw kessmniiel eipdqnidvd alqvafgsly rddvlikpsr
      181 vvailaaacm lqldgliqqc getmketinv ktvcgyytsv eiygldsvkk kclewllnnl
      241 mthqnvklfk elginvmkql igssnlfvmq vemdvyttlk kwmflqlvps wngslkqllt
      301 etdvwfskqr kdfegmafle tepgkpfvsv frhlrlqyii sdlasariie qdgivpsewl
      361 ssvykqqwfa mlraeqdrev gpqeinkedl egnsmrcgrk lakdgeyywc wtgfnfgfdl
      421 lviytngyii fkrntlnqpr sgsvslrprr siafrlrlas fdssgklvcs rttgyqilil
      481 kkdqeqvvmn ldsrfltfpl yiccnflyis pekgiennrh penpen
//
LOCUS       NP_001379009             759 aa            linear   PRI 21-NOV-2025
DEFINITION  cysteine-rich protein 2-binding protein isoform 4 [Homo sapiens].
ACCESSION   NP_001379009
VERSION     NP_001379009.1
DBSOURCE    REFSEQ: accession NM_001392080.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Gong,Y., Liu,M., Zhang,Q., Li,J., Cai,H., Ran,J., Ma,L., Ma,Y. and
            Quan,S.
  TITLE     Lysine acetyltransferase 14 mediates TGF-beta-induced fibrosis in
            ovarian endometrioma via co-operation with serum response factor
  JOURNAL   J Transl Med 22 (1), 561 (2024)
   PUBMED   38867256
  REMARK    GeneRIF: Lysine acetyltransferase 14 mediates TGF-beta-induced
            fibrosis in ovarian endometrioma via co-operation with serum
            response factor.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 759)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 759)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 759)
  AUTHORS   Viita,T., Kyheroinen,S., Prajapati,B., Virtanen,J., Frilander,M.J.,
            Varjosalo,M. and Vartiainen,M.K.
  TITLE     Nuclear actin interactome analysis links actin to KAT14 histone
            acetyl transferase and mRNA splicing
  JOURNAL   J Cell Sci 132 (8) (2019)
   PUBMED   30890647
  REMARK    GeneRIF: Actin binds directly to the hATAC subunit KAT14, and
            modulates its histone acetyl transferase activity in vitro and in
            cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 759)
  AUTHORS   Orpinell,M., Fournier,M., Riss,A., Nagy,Z., Krebs,A.R., Frontini,M.
            and Tora,L.
  TITLE     The ATAC acetyl transferase complex controls mitotic progression by
            targeting non-histone substrates
  JOURNAL   EMBO J 29 (14), 2381-2394 (2010)
   PUBMED   20562830
REFERENCE   7  (residues 1 to 759)
  AUTHORS   Nagy,Z., Riss,A., Fujiyama,S., Krebs,A., Orpinell,M., Jansen,P.,
            Cohen,A., Stunnenberg,H.G., Kato,S. and Tora,L.
  TITLE     The metazoan ATAC and SAGA coactivator HAT complexes regulate
            different sets of inducible target genes
  JOURNAL   Cell Mol Life Sci 67 (4), 611-628 (2010)
   PUBMED   19936620
REFERENCE   8  (residues 1 to 759)
  AUTHORS   Guelman,S., Kozuka,K., Mao,Y., Pham,V., Solloway,M.J., Wang,J.,
            Wu,J., Lill,J.R. and Zha,J.
  TITLE     The double-histone-acetyltransferase complex ATAC is essential for
            mammalian development
  JOURNAL   Mol Cell Biol 29 (5), 1176-1188 (2009)
   PUBMED   19103755
REFERENCE   9  (residues 1 to 759)
  AUTHORS   Wang,Y.L., Faiola,F., Xu,M., Pan,S. and Martinez,E.
  TITLE     Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel
            NC2-like histone fold module that interacts with the TATA-binding
            protein
  JOURNAL   J Biol Chem 283 (49), 33808-33815 (2008)
   PUBMED   18838386
REFERENCE   10 (residues 1 to 759)
  AUTHORS   Weiskirchen,R. and Gressner,A.M.
  TITLE     The cysteine- and glycine-rich LIM domain protein CRP2 specifically
            interacts with a novel human protein (CRP2BP)
  JOURNAL   Biochem Biophys Res Commun 274 (3), 655-663 (2000)
   PUBMED   10924333
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL050321.11 and KF459584.1.
            
            Summary: CSRP2 is a protein containing two LIM domains, which are
            double zinc finger motifs found in proteins of diverse function.
            CSRP2 and some related proteins are thought to act as protein
            adapters, bridging two or more proteins to form a larger protein
            complex. The protein encoded by this gene binds to one of the LIM
            domains of CSRP2 and contains an acetyltransferase domain. Although
            the encoded protein has been detected in the cytoplasm, it is
            predominantly a nuclear protein. Alternatively spliced transcript
            variants have been described. [provided by RefSeq, Jun 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2514007.1,
                                           SRR14038193.2462777.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145240, SAMEA2146982
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.23"
     Protein         1..759
                     /product="cysteine-rich protein 2-binding protein isoform
                     4"
                     /note="CRP2 binding protein; ATAC component 2 homolog;
                     CRP2 binding partner; cysteine-rich protein 2-binding
                     protein; CSRP2-binding protein; ADA2A-containing complex
                     subunit 2"
                     /calculated_mol_wt=85944
     Region          663..738
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
     CDS             1..759
                     /gene="KAT14"
                     /gene_synonym="ATAC2; CRP2BP; CSRP2BP; dJ717M23.1;
                     PRO1194"
                     /coded_by="NM_001392080.1:643..2922"
                     /note="isoform 4 is encoded by transcript variant 15"
                     /db_xref="GeneID:57325"
                     /db_xref="HGNC:HGNC:15904"
                     /db_xref="MIM:617501"
ORIGIN      
        1 mdssihlssl isrhddeatr tstsegleeg evegetlliv esedqasvdl shdqsgdsln
       61 sdegdvswme eqlsyfcdkc qkwipasqlr eqlsylkgdn ffrftcsdcs adgkeqyerl
      121 kltwqqvvml amynlslegs grqgyfrwke dicafiekhw tfllgnrkkt stwwstvagc
      181 lsvgspmyfr sgaqefgepg wwklvhnkpp tmkpegekls astlkikask ptldpiitve
      241 glrkrasrnp vesamelkek rsrtqeakdi rraqkeaagf ldrstsstpv kfisrgrrpd
      301 vilekgevid fsslsssdrt pltspspsps ldfsapgtpa shsatpslls eadlipdvmp
      361 pqalfhddde megdgvidpg meyvpppags vasgpvvgvr kkvrgpeqik qeveseeekp
      421 drmdidsedt dsntslqtra rekrkpqlek dtkpkepryt pvsiyeekll lkrleacpga
      481 vamtpearrl krklivrqak rdrglplfdl dqvvnaalll vdgiygakeg gisrlpagqa
      541 tyrttcqdfr ildryqtslp srkgfrhqtt kflyrlvgse dmavdqsivs pytsrilkpy
      601 irsdphwtpe pdapldycyv rpnhiptins mcqeffwpgi dlseclqypd fsvvvlykkv
      661 iiafgfmvpd vkyneayisf lfvhpewrra giatfmiyhl iqtcmgkdvt lhvsasnpam
      721 llyqkfgfkt eeyvldfydk yyplesteck hafflrlrr
//
LOCUS       NP_006210               1070 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            beta isoform isoform 1 [Homo sapiens].
ACCESSION   NP_006210 XP_005247587
VERSION     NP_006210.1
DBSOURCE    REFSEQ: accession NM_006219.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Liu,L., Feng,X., Fan,C., Kong,D., Feng,X., Sun,C., Xu,Y., Li,B.,
            Jiang,Y. and Zheng,C.
  TITLE     PDCD4 interacting with PIK3CB and CTSZ promotes the apoptosis of
            multiple myeloma cells
  JOURNAL   FASEB J 38 (16), e70024 (2024)
   PUBMED   39190024
  REMARK    GeneRIF: PDCD4 interacting with PIK3CB and CTSZ promotes the
            apoptosis of multiple myeloma cells.
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Liu,G., Hou,Y., Jin,X., Zhang,Y., Sun,C., Huang,C., Ren,Y., Gao,J.,
            Wang,X. and Jiang,X.
  TITLE     PI3K/HSCB axis facilitates FOG1 nuclear translocation to promote
            erythropoiesis and megakaryopoiesis
  JOURNAL   Elife 13, 95815 (2024)
   PUBMED   38757931
  REMARK    GeneRIF: PI3K/HSCB axis facilitates FOG1 nuclear translocation to
            promote erythropoiesis and megakaryopoiesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1070)
  AUTHORS   Duewell,B.R., Wilson,N.E., Bailey,G.M., Peabody,S.E. and
            Hansen,S.D.
  TITLE     Molecular dissection of PI3Kbeta synergistic activation by receptor
            tyrosine kinases, GbetaGgamma, and Rho-family GTPases
  JOURNAL   Elife 12, 88991 (2024)
   PUBMED   38713746
  REMARK    GeneRIF: Molecular dissection of PI3Kbeta synergistic activation by
            receptor tyrosine kinases, GbetaGgamma, and Rho-family GTPases.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1070)
  AUTHORS   Xu,W., Chen,Y., Zhang,Z., Jiang,Y. and Wang,Z.
  TITLE     Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma
  JOURNAL   Med Oncol 40 (8), 221 (2023)
   PUBMED   37402056
  REMARK    GeneRIF: Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1070)
  AUTHORS   Milani,D., Mazzoni,M., Borgatti,P., Zauli,G., Cantley,L. and
            Capitani,S.
  TITLE     Extracellular human immunodeficiency virus type-1 Tat protein
            activates phosphatidylinositol 3-kinase in PC12 neuronal cells
  JOURNAL   J Biol Chem 271 (38), 22961-22964 (1996)
   PUBMED   8798481
REFERENCE   7  (residues 1 to 1070)
  AUTHORS   Bonnefoy-Berard,N., Liu,Y.C., von Willebrand,M., Sung,A., Elly,C.,
            Mustelin,T., Yoshida,H., Ishizaka,K. and Altman,A.
  TITLE     Inhibition of phosphatidylinositol 3-kinase activity by association
            with 14-3-3 proteins in T cells
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10142-10146 (1995)
   PUBMED   7479742
REFERENCE   8  (residues 1 to 1070)
  AUTHORS   Hu,P. and Schlessinger,J.
  TITLE     Direct association of p110 beta phosphatidylinositol 3-kinase with
            p85 is mediated by an N-terminal fragment of p110 beta
  JOURNAL   Mol Cell Biol 14 (4), 2577-2583 (1994)
   PUBMED   8139559
REFERENCE   9  (residues 1 to 1070)
  AUTHORS   Hu,P., Mondino,A., Skolnik,E.Y. and Schlessinger,J.
  TITLE     Cloning of a novel, ubiquitously expressed human
            phosphatidylinositol 3-kinase and identification of its binding
            site on p85
  JOURNAL   Mol Cell Biol 13 (12), 7677-7688 (1993)
   PUBMED   8246984
REFERENCE   10 (residues 1 to 1070)
  AUTHORS   Carpenter,C.L., Duckworth,B.C., Auger,K.R., Cohen,B.,
            Schaffhausen,B.S. and Cantley,L.C.
  TITLE     Purification and characterization of phosphoinositide 3-kinase from
            rat liver
  JOURNAL   J Biol Chem 265 (32), 19704-19711 (1990)
   PUBMED   2174051
  REMARK    GeneRIF: This paper reports the first purification of a
            phosphoinositide 3-kinase and shows that the protein is a
            heterodimer of an 85 kd regulatory subunit that mediates binding to
            phosphorylated proteins and a 110 kd catalytic subunit.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC067728.25, AC117389.5, BC114432.1, AC020890.22 and AI623206.1.
            
            On Jul 5, 2019 this sequence version replaced XP_005247587.1.
            
            Summary: This gene encodes an isoform of the catalytic subunit of
            phosphoinositide 3-kinase (PI3K). These kinases are important in
            signaling pathways involving receptors on the outer membrane of
            eukaryotic cells and are named for their catalytic subunit. The
            encoded protein is the catalytic subunit for PI3Kbeta (PI3KB).
            PI3KB has been shown to be part of the activation pathway in
            neutrophils which have bound immune complexes at sites of injury or
            infection. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (1) represent the longer
            transcript and encodes the longer protein (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.4019984.1,
                                           SRR11853562.23969.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000674063.1/ ENSP00000501150.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..1070
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit beta isoform isoform 1"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.1.153"
                     /note="PI3-kinase p110 subunit beta; PtdIns-3-kinase p110;
                     PI3K-beta; PI3-kinase subunit beta; ptdIns-3-kinase
                     subunit beta; ptdIns-3-kinase subunit p110-beta;
                     phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa
                     catalytic subunit beta; serine/threonine protein kinase
                     PIK3CB; phosphoinositide-3-kinase, catalytic, beta
                     polypeptide"
                     /calculated_mol_wt=122632
     Region          41..118
                     /region_name="PI3K_p85B"
                     /note="PI3-kinase family, p85-binding domain; smart00143"
                     /db_xref="CDD:197539"
     Region          180..288
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, Ras-binding domain; smart00144"
                     /db_xref="CDD:197540"
     Region          324..501
                     /region_name="C2_PI3K_class_I_beta_delta"
                     /note="C2 domain present in class I beta and delta
                     phosphatidylinositol 3-kinases (PI3Ks); cd08693"
                     /db_xref="CDD:176075"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI9; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     Region          410..418
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Region          532..702
                     /region_name="PI3Ka_I"
                     /note="Phosphoinositide 3-kinase (PI3K) class I, accessory
                     domain; PIK domain is conserved in all PI3 and
                     PI4-kinases. Its role is unclear but it has been suggested
                     to be involved in substrate presentation. In general, PI3K
                     class I prefer phosphoinositol (4,5)...; cd00872"
                     /db_xref="CDD:238444"
     Region          706..1067
                     /region_name="PI3Kc_IA_beta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase beta; cd05173"
                     /db_xref="CDD:270717"
     Region          778..784
                     /region_name="G-loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(779,781..783,785,803,805,808,839,851..854,859,862,
                     924,926,936..937)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270717"
     Site            order(846..847,874..875,878,948..949,962,965,973..976,979,
                     1046,1049..1050,1052..1053)
                     /site_type="other"
                     /note="regulatory subunit interface [polypeptide binding]"
                     /db_xref="CDD:270717"
     Site            893
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270717"
     Region          916..924
                     /region_name="Catalytic loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            916..924
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270717"
     Region          935..961
                     /region_name="Activation loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(937..950,956..961)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270717"
     Site            1070
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12502714; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     CDS             1..1070
                     /gene="PIK3CB"
                     /gene_synonym="P110BETA; PI3K; PI3KBETA; PIK3C1"
                     /coded_by="NM_006219.3:356..3568"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3104.1"
                     /db_xref="GeneID:5291"
                     /db_xref="HGNC:HGNC:8976"
                     /db_xref="MIM:602925"
ORIGIN      
        1 mcfsfimppa madildiwav dsqiasdgsi pvdfllptgi yiqlevprea tisyikqmlw
       61 kqvhnypmfn llmdidsymf acvnqtavye eledetrrlc dvrpflpvlk lvtrscdpge
      121 kldskigvli gkglhefdsl kdpevnefrr kmrkfseeki lslvglswmd wlkqtyppeh
      181 epsipenled klyggkliva vhfencqdvf sfqvspnmnp ikvnelaiqk rltihgkede
      241 vspydyvlqv sgrveyvfgd hpliqfqyir ncvmnralph filvecckik kmyeqemiai
      301 eaainrnssn lplplppkkt riishvwenn npfqivlvkg nklnteetvk vhvraglfhg
      361 tellcktivs sevsgkndhi wneplefdin icdlprmarl cfavyavldk vktkkstkti
      421 npskyqtirk agkvhypvaw vntmvfdfkg qlrtgdiilh swssfpdele emlnpmgtvq
      481 tnpytenata lhvkfpenkk qpyyyppfdk iiekaaeias sdsanvssrg gkkflpvlke
      541 ildrdplsql cenemdliwt lrqdcreifp qslpklllsi kwnkledvaq lqallqiwpk
      601 lpprealell dfnypdqyvr eyavgclrqm sdeelsqyll qlvqvlkyep fldcalsrfl
      661 leralgnrri gqflfwhlrs evhipavsvq fgvileaycr gsvghmkvls kqvealnklk
      721 tlnsliklna vklnrakgke amhtclkqsa yrealsdlqs plnpcvilse lyvekckymd
      781 skmkplwlvy nnkvfgedsv gvifkngddl rqdmltlqml rlmdllwkea gldlrmlpyg
      841 clatgdrsgl ievvstseti adiqlnssnv aaaaafnkda llnwlkeyns gddldraiee
      901 ftlscagycv asyvlgigdr hsdnimvkkt gqlfhidfgh ilgnfkskfg ikrervpfil
      961 tydfihviqq gktgntekfg rfrqcceday lilrrhgnlf itlfalmlta glpeltsvkd
     1021 iqylkdslal gkseeealkq fkqkfdealr eswttkvnwm ahtvrkdyrs
//
LOCUS       NP_001123914             189 aa            linear   PRI 21-NOV-2025
DEFINITION  GTPase HRas isoform 1 [Homo sapiens].
ACCESSION   NP_001123914
VERSION     NP_001123914.1
DBSOURCE    REFSEQ: accession NM_001130442.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Ling,C., Liu,S.S., Wang,Y.Y., Huo,G.T., Yang,Y.W., Xu,N., Wang,H.,
            Wu,Y., Miao,Y.F., Fu,R., Zhao,Y.W. and Fan,C.F.
  TITLE     Overexpression of wild-type HRAS drives non-alcoholic
            steatohepatitis to hepatocellular carcinoma in mice
  JOURNAL   Zool Res 45 (3), 551-566 (2024)
   PUBMED   38757223
  REMARK    GeneRIF: Overexpression of wild-type HRAS drives non-alcoholic
            steatohepatitis to hepatocellular carcinoma in mice.
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Devi,P., Dwivedi,R., Sankar,R., Jain,A., Gupta,S. and Gupta,S.
  TITLE     Unraveling the Genetic Web: H-Ras Expression and Mutation in Oral
            Squamous Cell Carcinoma-A Systematic Review
  JOURNAL   Head Neck Pathol 18 (1), 21 (2024)
   PUBMED   38502412
  REMARK    GeneRIF: Unraveling the Genetic Web: H-Ras Expression and Mutation
            in Oral Squamous Cell Carcinoma-A Systematic Review.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Zhang,Q., Zheng,L., Bai,Y., Su,C., Che,Y., Xu,J., Sun,K., Ni,J.,
            Huang,L., Shen,Y., Jia,L., Xu,L., Yin,R., Li,M. and Hu,J.
  TITLE     ITPR1-AS1 promotes small cell lung cancer metastasis by
            facilitating P21HRAS splicing and stabilizing DDX3X to activate the
            cRaf-MEK-ERK cascade
  JOURNAL   Cancer Lett 577, 216426 (2023)
   PUBMED   37820992
  REMARK    GeneRIF: ITPR1-AS1 promotes small cell lung cancer metastasis by
            facilitating P21[HRAS] splicing and stabilizing DDX3X to activate
            the cRaf-MEK-ERK cascade.
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Wang,J., Al-Majid,D., Brenner,J.C. and Smith,J.D.
  TITLE     Mutant HRas Signaling and Rationale for Use of Farnesyltransferase
            Inhibitors in Head and Neck Squamous Cell Carcinoma
  JOURNAL   Target Oncol 18 (5), 643-655 (2023)
   PUBMED   37665491
  REMARK    GeneRIF: Mutant HRas Signaling and Rationale for Use of
            Farnesyltransferase Inhibitors in Head and Neck Squamous Cell
            Carcinoma.
            Review article
REFERENCE   6  (residues 1 to 189)
  AUTHORS   Gripp,K.W. and Weaver,K.N.
  TITLE     HRAS-Related Costello Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301680
REFERENCE   7  (residues 1 to 189)
  AUTHORS   Sakai,E., Rikimaru,K., Ueda,M., Matsumoto,Y., Ishii,N., Enomoto,S.,
            Yamamoto,H. and Tsuchida,N.
  TITLE     The p53 tumor-suppressor gene and ras oncogene mutations in oral
            squamous-cell carcinoma
  JOURNAL   Int J Cancer 52 (6), 867-872 (1992)
   PUBMED   1459726
REFERENCE   8  (residues 1 to 189)
  AUTHORS   Tanci,P., Genuardi,M., Santini,S.A. and Neri,G.
  TITLE     PCR detection of an insertion/deletion polymorphism in intron 1 of
            the HRAS1 locus
  JOURNAL   Nucleic Acids Res 20 (5), 1157 (1992)
   PUBMED   1549493
REFERENCE   9  (residues 1 to 189)
  AUTHORS   Kinsella,B.T., Erdman,R.A. and Maltese,W.A.
  TITLE     Posttranslational modification of Ha-ras p21 by farnesyl versus
            geranylgeranyl isoprenoids is determined by the COOH-terminal amino
            acid
  JOURNAL   Proc Natl Acad Sci U S A 88 (20), 8934-8938 (1991)
   PUBMED   1924354
REFERENCE   10 (residues 1 to 189)
  AUTHORS   Tong,L.A., de Vos,A.M., Milburn,M.V. and Kim,S.H.
  TITLE     Crystal structures at 2.2 A resolution of the catalytic domains of
            normal ras protein and an oncogenic mutant complexed with GDP
  JOURNAL   J Mol Biol 217 (3), 503-516 (1991)
   PUBMED   1899707
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC137894.5, BM808879.1,
            BQ674260.1 and BQ574535.1.
            
            Summary: This gene belongs to the Ras oncogene family, whose
            members are related to the transforming genes of mammalian sarcoma
            retroviruses. The products encoded by these genes function in
            signal transduction pathways. These proteins can bind GTP and GDP,
            and they have intrinsic GTPase activity. This protein undergoes a
            continuous cycle of de- and re-palmitoylation, which regulates its
            rapid exchange between the plasma membrane and the Golgi apparatus.
            Mutations in this gene cause Costello syndrome, a disease
            characterized by increased growth at the prenatal stage, growth
            deficiency at the postnatal stage, predisposition to tumor
            formation, cognitive disability, skin and musculoskeletal
            abnormalities, distinctive facial appearance and cardiovascular
            abnormalities. Defects in this gene are implicated in a variety of
            cancers, including bladder cancer, follicular thyroid cancer, and
            oral squamous cell carcinoma. Multiple transcript variants, which
            encode different isoforms, have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) differs in the 3' UTR,
            compared to variant 1. Both variants 1 and 3 encode the same
            isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.161016.1,
                                           SRR14372079.2208141.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..189
                     /product="GTPase HRas isoform 1"
                     /EC_number="3.6.5.2"
                     /note="Ha-Ras1 proto-oncoprotein; Ras family small GTP
                     binding protein H-Ras; Harvey rat sarcoma viral oncogene
                     homolog; p19 H-RasIDX protein; transforming protein p21;
                     GTPase HRas; GTP- and GDP-binding peptide B;
                     transformation gene: oncogene HAMSV; c-has/bas p21
                     protein; v-Ha-ras Harvey rat sarcoma viral oncogene
                     homolog; Harvey rat sarcoma viral oncoprotein"
                     /calculated_mol_wt=21167
     mat_peptide     1..186
                     /product="GTPase HRas. /id=PRO_0000042996"
                     /note="propagated from UniProtKB/Swiss-Prot (P01112.1)"
                     /calculated_mol_wt=20999
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine, in GTPase HRas, alternate.
                     /evidence=ECO:0000269|Ref.12; propagated from
                     UniProtKB/Swiss-Prot (P01112.1)"
     mat_peptide     2..186
                     /product="GTPase HRas, N-terminally processed.
                     /id=PRO_0000326476"
                     /note="propagated from UniProtKB/Swiss-Prot (P01112.1)"
                     /calculated_mol_wt=20868
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in GTPase HRas, N-terminally
                     processed. /evidence=ECO:0000269|Ref.12; propagated from
                     UniProtKB/Swiss-Prot (P01112.1)"
     Region          3..164
                     /region_name="H_N_K_Ras_like"
                     /note="Ras GTPase family containing H-Ras,N-Ras and
                     K-Ras4A/4B; cd04138"
                     /db_xref="CDD:133338"
     Site            10..17
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133338"
     Site            order(11..12,59..60)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133338"
     Site            order(12..18,28..30,32,35,60,116..117,119..120,145..146)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133338"
     Site            order(17..18,30..32,34,37,40..41,54..55,57,59..61,63..65,
                     67,69..71,73,102..103,147)
                     /site_type="other"
                     /note="GEF interaction site [polypeptide binding]"
                     /db_xref="CDD:133338"
     Site            order(25,37..41)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:133338"
     Region          32..40
                     /region_name="Effector region"
                     /note="propagated from UniProtKB/Swiss-Prot (P01112.1)"
     Site            33..40
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133338"
     Site            35
                     /site_type="glycosylation"
                     /note="(Microbial infection) O-linked (Glc) threonine, by
                     P.sordellii toxin TcsL.
                     /evidence=ECO:0000269|PubMed:19744486,
                     ECO:0000269|PubMed:8626575, ECO:0000269|PubMed:8626586,
                     ECO:0000269|PubMed:9632667; propagated from
                     UniProtKB/Swiss-Prot (P01112.1)"
     Site            35
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133338"
     Site            57..60
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133338"
     Site            59..77
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133338"
     Site            116..119
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133338"
     Site            145..147
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133338"
     Region          166..185
                     /region_name="Hypervariable region"
                     /note="propagated from UniProtKB/Swiss-Prot (P01112.1)"
     Site            186
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000269|PubMed:8626715; propagated from
                     UniProtKB/Swiss-Prot (P01112.1)"
     CDS             1..189
                     /gene="HRAS"
                     /gene_synonym="C-BAS/HAS; C-H-RAS; C-HA-RAS1; CTLO;
                     H-RASIDX; HAMSV; HRAS1; p21ras; RASH1"
                     /coded_by="NM_001130442.3:215..784"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS7698.1"
                     /db_xref="GeneID:3265"
                     /db_xref="HGNC:HGNC:5173"
                     /db_xref="MIM:190020"
ORIGIN      
        1 mteyklvvvg aggvgksalt iqliqnhfvd eydptiedsy rkqvvidget clldildtag
       61 qeeysamrdq ymrtgegflc vfainntksf edihqyreqi krvkdsddvp mvlvgnkcdl
      121 aartvesrqa qdlarsygip yietsaktrq gvedafytlv reirqhklrk lnppdesgpg
      181 cmsckcvls
//
LOCUS       NP_001371659            1129 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 26 [Homo sapiens].
ACCESSION   NP_001371659 XP_024309298
VERSION     NP_001371659.1
DBSOURCE    REFSEQ: accession NM_001384730.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1129)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1129)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1129)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1129)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1129)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1129)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1129)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1129)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1129)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1129)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            On Jun 26, 2020 this sequence version replaced XP_024309298.1.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.649700.1,
                                           SRR18074969.487422.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1129
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1129
                     /product="microtubule-associated protein 4 isoform 26"
                     /note="MAP-4"
                     /calculated_mol_wt=118651
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          225..522
                     /region_name="17 X 14 AA tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          339..378
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            498
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          <552..896
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            562
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            601
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          618..968
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            620
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            673
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10791892,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            690
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            700
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            764
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10791892,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            774
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            780
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            802
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            804
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            830
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            905
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          <908..929
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            918
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            919
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          969..999
                     /region_name="Tau/MAP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          969..998
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            977
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          1000..1030
                     /region_name="Tau/MAP 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1000..1029
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          1031..1062
                     /region_name="Tau/MAP 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1031..1061
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            1050
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1051..1129
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            1122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            1128
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     CDS             1..1129
                     /gene="MAP4"
                     /coded_by="NM_001384730.1:96..3485"
                     /note="isoform 26 is encoded by transcript variant 12"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiegsptef leekmayqey pnsqnwpedt nfcfqpeqvv dpiqtdpfkm
      121 yhdddladlv fpssatadts ifagqndplk dsygmspcnt avvpqgwsve alnsphsesf
      181 vspeavaepp qptavplela keiemaseer ppaqaleimm glkttdmaps ketemalakd
      241 malatkteva lakdmesptk ldvtlakdmq psmesdmalv kdmelpteke valvkdvrwp
      301 tetdvssakn vvlpteteva pakdvtllke teraspikmd lapskdmgpp kenkketera
      361 spikmdlaps kdmgppkenk ivpakdlvll seievaqand iissteissa ekvalssete
      421 valardmtlp petnviltkd kalpleaeva pvkdmaqlpe teiapakdva pstvkevgll
      481 kdmsplsete malgkdvtpp petevvlikn vclppemeva ltedqvpalk teaplakdgv
      541 ltlannvtpa kdvpplsete atpvpikdme iaqtqkgise dshleslqdv gqsaaptfmi
      601 spetvtgtgk kcslpaeeds vleklgerkp cnsqpselss etsgiarpee grpvvsgtgn
      661 dittppnkel ppspekktkp lattqpakts tskaktqpts lpkqpaptti gglnkkpmsl
      721 asglvpaapp krpavasarp silpskdvkp kpiadakape kraspskpas apasrsgsks
      781 tqtvakttta aavastgpss rspstllpkk ptaiktegkp aevkkmtaks vpadlsrpks
      841 tstssmkktt tlsgtapaag vvpsrvkatp mpsrpsttpf idkkptsakp ssttprlsrl
      901 atntsapdlk nvrskvgste nikhqpgggr akvekkteaa attrkpesna vtktagpias
      961 aqkqpagkvq ivskkvsysh iqskcgskdn ikhvpgggnv qiqnkkvdis kvsskcgska
     1021 nikhkpgggd vkiesqklnf kekaqakvgs ldnvghlpag gavktegggs eaplcpgppa
     1081 geepaiseaa peagaptsas glnghptlsg ggdqreaqtl dsqiqetsi
//
LOCUS       NP_003619               1192 aa            linear   PRI 21-NOV-2025
DEFINITION  plakophilin-4 isoform a [Homo sapiens].
ACCESSION   NP_003619
VERSION     NP_003619.2
DBSOURCE    REFSEQ: accession NM_003628.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1192)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1192)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1192)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1192)
  AUTHORS   Park,S.S., Ponce-Balbuena,D., Kuick,R., Guerrero-Serna,G., Yoon,J.,
            Mellacheruvu,D., Conlon,K.P., Basrur,V., Nesvizhskii,A.I.,
            Jalife,J. and Rual,J.F.
  TITLE     Kir2.1 Interactome Mapping Uncovers PKP4 as a Modulator of the
            Kir2.1-Regulated Inward Rectifier Potassium Currents
  JOURNAL   Mol Cell Proteomics 19 (9), 1436-1449 (2020)
   PUBMED   32541000
  REMARK    GeneRIF: Kir2.1 Interactome Mapping Uncovers PKP4 as a Modulator of
            the Kir2.1-Regulated Inward Rectifier Potassium Currents.
REFERENCE   5  (residues 1 to 1192)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 1192)
  AUTHORS   Stahl,B., Diehlmann,A. and Sudhof,T.C.
  TITLE     Direct interaction of Alzheimer's disease-related presenilin 1 with
            armadillo protein p0071
  JOURNAL   J Biol Chem 274 (14), 9141-9148 (1999)
   PUBMED   10092585
REFERENCE   7  (residues 1 to 1192)
  AUTHORS   Levesque,G., Yu,G., Nishimura,M., Zhang,D.M., Levesque,L., Yu,H.,
            Xu,D., Liang,Y., Rogaeva,E., Ikeda,M., Duthie,M., Murgolo,N.,
            Wang,L., VanderVere,P., Bayne,M.L., Strader,C.D., Rommens,J.M.,
            Fraser,P.E. and St George-Hyslop,P.
  TITLE     Presenilins interact with armadillo proteins including
            neural-specific plakophilin-related protein and beta-catenin
  JOURNAL   J Neurochem 72 (3), 999-1008 (1999)
   PUBMED   10037471
REFERENCE   8  (residues 1 to 1192)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   9  (residues 1 to 1192)
  AUTHORS   Paffenholz,R. and Franke,W.W.
  TITLE     Identification and localization of a neurally expressed member of
            the plakoglobin/armadillo multigene family
  JOURNAL   Differentiation 61 (5), 293-304 (1997)
   PUBMED   9342840
REFERENCE   10 (residues 1 to 1192)
  AUTHORS   Hatzfeld,M. and Nachtsheim,C.
  TITLE     Cloning and characterization of a new armadillo family member,
            p0071, associated with the junctional plaque: evidence for a
            subfamily of closely related proteins
  JOURNAL   J Cell Sci 109 (Pt 11), 2767-2778 (1996)
   PUBMED   8937994
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008070.4 and AC005042.2.
            
            On Oct 6, 2004 this sequence version replaced NP_003619.1.
            
            Summary: Armadillo-like proteins are characterized by a series of
            armadillo repeats, first defined in the Drosophila 'armadillo' gene
            product, that are typically 42 to 45 amino acids in length. These
            proteins can be divided into subfamilies based on their number of
            repeats, their overall sequence similarity, and the dispersion of
            the repeats throughout their sequences. Members of the
            p120(ctn)/plakophilin subfamily of Armadillo-like proteins,
            including CTNND1, CTNND2, PKP1, PKP2, PKP4, and ARVCF. PKP4 may be
            a component of desmosomal plaque and other adhesion plaques and is
            thought to be involved in regulating junctional plaque organization
            and cadherin function. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Feb 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853561.16876.1,
                                           SRR18074969.651014.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000389759.8/ ENSP00000374409.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.1"
     Protein         1..1192
                     /product="plakophilin-4 isoform a"
                     /note="catenin 4"
                     /calculated_mol_wt=131738
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          73..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Region          <194..347
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            254
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            270
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Region          290..310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Region          323..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Region          415..455
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Region          518..557
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          530..555
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(546,550,554,588,592,596,633,637,641)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          559..598
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          560..599
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          563..599
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          603..644
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          604..644
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          607..642
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          649..700
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          660..702
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          706..751
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          708..749
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          773..810
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            776
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          815..855
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          825..855
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          848..>969
                     /region_name="PLN03200"
                     /note="cellulose synthase-interactive protein;
                     Provisional"
                     /db_xref="CDD:215629"
     Region          862..901
                     /region_name="ARM 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          865..900
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          867..899
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(890,894,898,936,940,944,982,986)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          906..947
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          949..993
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          950..993
                     /region_name="ARM 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Region          953..988
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            1013
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            1017
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            1045
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Region          1058..1086
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99569.2)"
     Site            1091
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     Site            1135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FH0; propagated from
                     UniProtKB/Swiss-Prot (Q99569.2)"
     CDS             1..1192
                     /gene="PKP4"
                     /gene_synonym="p0071"
                     /coded_by="NM_003628.6:273..3851"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33305.1"
                     /db_xref="GeneID:8502"
                     /db_xref="HGNC:HGNC:9026"
                     /db_xref="MIM:604276"
ORIGIN      
        1 mpapeqaslv eegqpqtrqe aastgpgmep ettattilas vkeqelqfqr ltreleverq
       61 ivasqlercr lgaespsias tssteksfpw rstdvpntgv skprvsdavq pnnylirtep
      121 eqgtlyspeq tslhesegsl gnsrsstqmn sysdsgyqea gsfhnsqnvs kadnrqqhsf
      181 igstnnhvvr nsraegqtlv qpsvanramr rvssvpsraq spsyvistgv spsrgslrts
      241 lgsgfgspsv tdprplnpsa yssttlpaar aaspysqrpa sptairrigs vtsrqtsnpn
      301 gptpqyqtta rvgspltltd aqtrvaspsq gqvgssspkr sgmtavpqhl gpslqrtvhd
      361 meqfgqqqyd iyermvpprp dsltglrssy asqhsqlgqd lrsavspdlh itpiyegrty
      421 yspvyrspnh gtvelqgsqt alyrtgsvgi gnlqrtssqr stltyqrnny alnttatyae
      481 pyrpiqyrvq ecnynrlqha vpaddgttrs psidsiqkdp refawrdpel pevihmlqhq
      541 fpsvqanaaa ylqhlcfgdn kvkmevcrlg gikhlvdlld hrvlevqkna cgalrnlvfg
      601 kstdenkiam knvggipall rllrksidae vrelvtgvlw nlsscdavkm tiirdalstl
      661 tntvivphsg wnnssfdddh kikfqtslvl rnttgclrnl ssageearkq mrsceglvds
      721 llyvihtcvn tsdydsktve ncvctlrnls yrlelevpqa rllglneldd llgkespskd
      781 sepscwgkkk kkkkrtpqed qwdgvgpipg lskspkgvem lwhpsvvkpy ltllaessnp
      841 atlegsagsl qnlsagnwkf aayiraavrk ekglpilvel lrmdndrvvs svatalrnma
      901 ldvrnkelig kyamrdlvnr lpggngpsvl sdetmaaicc alhevtsknm enakaladsg
      961 gieklvnitk grgdrsslkv vkaaaqvlnt lwqyrdlrsi ykkdgwnqnh fitpvstler
     1021 drfkshpsls ttnqqmspii qsvgstsssp allgirdprs eydrtqppmq yynsqgdath
     1081 kglypgsskp spiyissyss pareqnrrlq hqqlyysqdd snrknfdayr lylqsphsye
     1141 dpyfddrvhf pastdystqy glksttnyvd fystkrpsyr aeqypgspds wv
//
LOCUS       NP_001364322            2302 aa            linear   PRI 21-NOV-2025
DEFINITION  myomegalin isoform 15 [Homo sapiens].
ACCESSION   NP_001364322 XP_016858388
VERSION     NP_001364322.1
DBSOURCE    REFSEQ: accession NM_001377393.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2302)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2302)
  AUTHORS   Pan,R., Dai,J., Liang,W., Wang,H., Ye,L., Ye,S., Lin,Z., Huang,S.,
            Xiong,Y., Zhang,L., Lu,L., Wang,O., Shen,X., Liao,W. and Lu,X.
  TITLE     PDE4DIP contributes to colorectal cancer growth and chemoresistance
            through modulation of the NF1/RAS signaling axis
  JOURNAL   Cell Death Dis 14 (6), 373 (2023)
   PUBMED   37355626
  REMARK    GeneRIF: PDE4DIP contributes to colorectal cancer growth and
            chemoresistance through modulation of the NF1/RAS signaling axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2302)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   4  (residues 1 to 2302)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 2302)
  AUTHORS   Abou Ziki,M.D., Bhat,N., Neogi,A., Driscoll,T.P., Ugwu,N., Liu,Y.,
            Smith,E., Abboud,J.M., Chouairi,S., Schwartz,M.A., Akar,J.G. and
            Mani,A.
  TITLE     Epistatic interaction of PDE4DIP and DES mutations in familial
            atrial fibrillation with slow conduction
  JOURNAL   Hum Mutat 42 (10), 1279-1293 (2021)
   PUBMED   34289528
  REMARK    GeneRIF: Epistatic interaction of PDE4DIP and DES mutations in
            familial atrial fibrillation with slow conduction.
REFERENCE   6  (residues 1 to 2302)
  AUTHORS   Shimada,H., Kuboshima,M., Shiratori,T., Nabeya,Y., Takeuchi,A.,
            Takagi,H., Nomura,F., Takiguchi,M., Ochiai,T. and Hiwasa,T.
  TITLE     Serum anti-myomegalin antibodies in patients with esophageal
            squamous cell carcinoma
  JOURNAL   Int J Oncol 30 (1), 97-103 (2007)
   PUBMED   17143517
  REMARK    GeneRIF: MMGL-antibody is significantly with a favorable prognosis.
            Consequently, MMGL-anatibodies may be a useful tumor marker to
            diagnose and establish a prognosis in patients with esophageal
            squamous cell carcinoma.
REFERENCE   7  (residues 1 to 2302)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 2302)
  AUTHORS   Soejima,H., Kawamoto,S., Akai,J., Miyoshi,O., Arai,Y., Morohka,T.,
            Matsuo,S., Niikawa,N., Kimura,A., Okubo,K. and Mukai,T.
  TITLE     Isolation of novel heart-specific genes using the BodyMap database
  JOURNAL   Genomics 74 (1), 115-120 (2001)
   PUBMED   11374908
REFERENCE   9  (residues 1 to 2302)
  AUTHORS   Verde,I., Pahlke,G., Salanova,M., Zhang,G., Wang,S., Coletti,D.,
            Onuffer,J., Jin,S.L. and Conti,M.
  TITLE     Myomegalin is a novel protein of the golgi/centrosome that
            interacts with a cyclic nucleotide phosphodiesterase
  JOURNAL   J Biol Chem 276 (14), 11189-11198 (2001)
   PUBMED   11134006
REFERENCE   10 (residues 1 to 2302)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC245389.1, AC239802.3 and
            AC239804.2.
            
            On Jan 9, 2020 this sequence version replaced XP_016858388.1.
            
            Summary: The protein encoded by this gene serves to anchor
            phosphodiesterase 4D to the Golgi/centrosome region of the cell.
            Defects in this gene may be a cause of myeloproliferative disorder
            (MBD) associated with eosinophilia. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.57389.1,
                                           SRR1803611.57609.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2302
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     Protein         1..2302
                     /product="myomegalin isoform 15"
                     /note="myomegalin; cardiomyopathy-associated protein 2"
                     /calculated_mol_wt=260537
     Region          69..745
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          72..139
                     /region_name="Cnn_1N"
                     /note="Centrosomin N-terminal motif 1; pfam07989"
                     /db_xref="CDD:462333"
     Region          419..1232
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1508..1577
                     /region_name="Olduvai"
                     /note="Olduvai domain; pfam06758"
                     /db_xref="CDD:429104"
     Region          <1797..>1974
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..2302
                     /gene="PDE4DIP"
                     /gene_synonym="CMYA2; MMGL"
                     /coded_by="NM_001377393.2:267..7175"
                     /note="isoform 15 is encoded by transcript variant 15"
                     /db_xref="GeneID:9659"
                     /db_xref="HGNC:HGNC:15580"
                     /db_xref="MIM:608117"
ORIGIN      
        1 meqtwtrdyf aeddgemvpr tshtaaflsd tkdrgppvqs qiwrsgekvp fvqtyslraf
       61 ekppqvqtqa lrdfekhlnd lkkenfslkl riyfleermq qkyeasredi ykrnielkve
      121 veslkrelqd kkqhldktwa dvenlnsqne aelrrqfeer qqetehvyel lenkiqllqe
      181 esrlakneaa rmaalveaek ecnlelsekl kgvtknwedv pgdqvkpdqy tealaqrdkr
      241 ieelnqslaa qerlveqlsr ekqqllhlle eptsmevqpm teellkqqkl nshettitqq
      301 svsdshlael qekiqqteat nkilqeklne msyelkcaqe ssqkqdgtiq nlketlksre
      361 reteelyqvi egqndtmakl remlhqsqlg qlhssegtsp aqqqvalldl qsalfcsqle
      421 iqklqrvvrq kerqladakq cvqfveaaah eseqqkeasw khnqelrkal qqlqeelqnk
      481 sqqlraweae kyneirtqeq niqhlnhsls hkeqllqefr ellqyrdnsd ktleanemll
      541 eklrqrihdk avaleraide kfsaleekek elrqlrlavr erdhdlerlr dvlssneatm
      601 qsmesllrak gleveqlstt cqnlqwlkee metkfsrwqk eqesiiqqlq tslhdrnkev
      661 edlsatllck lgpgqseiae elcqrlqrke rmlqdllsdr nkqvleheme iqgllqsvst
      721 reqesqaaae klvqalmern selqalrqyl ggrdslmsqa pisnqqaevt ptgrlgkqtd
      781 qgsmqipsrd dstsltaked vsiprstlgd ldtvagleke lsnakeelel makkeresqm
      841 elsalqsmma vqeeelqvqa admesltrni qikedlikdl qmqlvdpedi pamerltqev
      901 lllrekvasv esqgqeisgn rrqqlllmle glvdersrln ealqaerqly sslvkfhahp
      961 esserdrtlq velegaqvlr srleevlgrs lerlnrletl aaiggaaagd dtedtsteft
     1021 dsieeeaahh shqqlvkval ekslatvetq npsfsppspm ggdsnrclqe emlhlraefh
     1081 qhleekrkae eelkelkaqi eeagfssvsh irntmlslcl enaelkeqmg eamsdgweie
     1141 edkekgeldn qsqprdpgpq safslpgstq hlrsqlsqck qryqdlqekl llseatvfaq
     1201 anelekyrvm ltgeslvkqd skqiqvdlqd lgyetcgrse neaereetts peceehnslk
     1261 emvlmeglcs eqgrrgstla ssserkplen qlgkqeefrv ygksenilvl rkdikdlkaq
     1321 lqnankviqn lksrvrslsv tsdysssler prklravgtl egssphsvpd edegwlsdgt
     1381 gafyspglqa kkdlesliqr vsqleaqlpk ngleeklaee lrsaswpgky dsliqdqare
     1441 lsylrqkire grgicylitr hakdtvksfe dllrsndidy ylgqsfreql aqgsqlterl
     1501 tsklstkdhk sekdqaglep lalrlsrelq ekekvievlq akldarsltp ssshalsdsh
     1561 rspsstsfls deleacsdmd ivseythyee kkaspshsds ihhsshsavl sskpsstsas
     1621 qgakaesnsn pislptpqnt pkeanqahsg fhfhsipkla slpqaplpsa pssflpfspt
     1681 gplllgccet pvvslaeaqq elqmlqkqlg esastvppas tatllsndle adssyylnsa
     1741 qphspprgti elgrilepgy lgssgkwdvm rpqkgsvsgd lssgssvyql nskptgadll
     1801 eehlgeirnl rqrleesici ndrlreqleh rltstargrg stsnfysqgl esipqlcnen
     1861 rvlrednrrl qaqlshvsre hsqeteslre allssrshlq elekelehqk verqqlledl
     1921 rekqqevlhf reerlslqen dsrlqhklvl lqqqceekqq lfeslqselq iyealygnsk
     1981 kglkayslda chqiplssdl shlvaevral rgqleqsiqg nnclrlqlqq qlesgagkas
     2041 lspssinqnf pastdpgnkq lllqdsavsp pvrdvgmnsp alvfpssass tpgsetpiin
     2101 ranglgldts pvmktppkle gdatdgsfan khgrhvighi ddysalrqqi aegkllvkki
     2161 vslvrsacsf pgleaqgtev lgskgihelr sstsalhhal eesaslltmf wraalpsthi
     2221 pvlpgkvges terellelrt kvskqerllq sttehlknan qqkesmeqfi vsqltrthdv
     2281 lkkartnlev kslralpctp al
//
LOCUS       NP_001362665             399 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform mmm [Homo sapiens].
ACCESSION   NP_001362665
VERSION     NP_001362665.1
DBSOURCE    REFSEQ: accession NM_001375736.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 399)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 399)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 399)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 399)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 399)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.79749.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..399
                     /product="abl interactor 2 isoform mmm"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=42362
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62484; propagated from
                     UniProtKB/Swiss-Prot (Q9NYB9.1)"
     Region          <156..283
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          338..398
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(346,348,351,355,373..374,387,389..390)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..399
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375736.1:122..1321"
                     /note="isoform mmm is encoded by transcript variant 70"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqs adkqraleet kayttqslas
       61 vaylintlan nvlqmldiqa sqlrrmessi nhisqvstqn mkmgglprtt pptqkppspp
      121 msgkgtlgss gssggshpss rsssrensgs gsvgvpiavp tpsppsvfpa pagsagtppl
      181 patsasapap lvpatvpsst apdaaaggaq tladgftspt ppvvsstppt ghpvqfysmn
      241 rpasrhtppt iggslpyrrp psitsqtslq nqmnggpfys qnpvsdtppp pppveepvfd
      301 espppppppe dyeeeeaavv eysdpyaeed ppwaprsyle kvvaiydytk dkedelsfqe
      361 gaiiyvikkn ddgwyegvmn gvtglfpgny vesimhyse
//
LOCUS       NP_001352002             453 aa            linear   PRI 21-NOV-2025
DEFINITION  adenylosuccinate synthetase isozyme 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001352002
VERSION     NP_001352002.1
DBSOURCE    REFSEQ: accession NM_001365073.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Baresova,V., Krijt,M., Skopova,V., Souckova,O., Kmoch,S. and
            Zikanova,M.
  TITLE     CRISPR-Cas9 induced mutations along de novo purine synthesis in
            HeLa cells result in accumulation of individual enzyme substrates
            and affect purinosome formation
  JOURNAL   Mol Genet Metab 119 (3), 270-277 (2016)
   PUBMED   27590927
REFERENCE   5  (residues 1 to 453)
  AUTHORS   Stepinski,J., Pawelczyk,T., Bizon,D. and Angielski,S.
  TITLE     Purine nucleotide cycle in rat renal cortex and medulla under
            conditions that mimic normal and low oxygen supply
  JOURNAL   Kidney Int 50 (4), 1195-1201 (1996)
   PUBMED   8887278
REFERENCE   6  (residues 1 to 453)
  AUTHORS   Powell,S.M., Zalkin,H. and Dixon,J.E.
  TITLE     Cloning and characterization of the cDNA encoding human
            adenylosuccinate synthetase
  JOURNAL   FEBS Lett 303 (1), 4-10 (1992)
   PUBMED   1592113
REFERENCE   7  (residues 1 to 453)
  AUTHORS   Zalkin,H. and Dixon,J.E.
  TITLE     De novo purine nucleotide biosynthesis
  JOURNAL   Prog Nucleic Acid Res Mol Biol 42, 259-287 (1992)
   PUBMED   1574589
  REMARK    Review article
REFERENCE   8  (residues 1 to 453)
  AUTHORS   Lai,L.W., Hart,I.M. and Patterson,D.
  TITLE     A gene correcting the defect in the CHO mutant Ade -H, deficient in
            a branch point enzyme (adenylosuccinate synthetase) of de novo
            purine biosynthesis, is located on the long arm of chromosome 1
  JOURNAL   Genomics 9 (2), 322-328 (1991)
   PUBMED   2004783
REFERENCE   9  (residues 1 to 453)
  AUTHORS   Ogawa,H., Shiraki,H., Matsuda,Y. and Nakagawa,H.
  TITLE     Interaction of adenylosuccinate synthetase with F-actin
  JOURNAL   Eur J Biochem 85 (2), 331-337 (1978)
   PUBMED   648524
REFERENCE   10 (residues 1 to 453)
  AUTHORS   Van der Weyden,M.B. and Kelly,W.N.
  TITLE     Human adenylosuccinate synthetase. Partial purification, kinetic
            and regulatory properties of the enzyme from placenta
  JOURNAL   J Biol Chem 249 (22), 7282-7289 (1974)
   PUBMED   4436310
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL591594.9 and AL645465.15.
            
            Summary: This gene encodes the enzyme adenylosuccinate synthetase
            which catalyzes the first committed step in the conversion of
            inosine monophosphate to adenosine monophosphate. A pseudogene of
            this gene is found on chromosome 17.[provided by RefSeq, Nov 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.41070.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q44"
     Protein         1..453
                     /product="adenylosuccinate synthetase isozyme 2 isoform 2"
                     /EC_number="6.3.4.4"
                     /note="adenylosuccinate synthetase, acidic isozyme;
                     IMP--aspartate ligase 2; adenylosuccinate synthetase
                     (Ade(-)H-complementing); L-type adenylosuccinate
                     synthetase; adenylosuccinate synthetase, liver isozyme;
                     AMPSase 2; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=49653
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P30520.3)"
     Region          32..450
                     /region_name="Adenylsucc_synt"
                     /note="Adenylosuccinate synthetase; pfam00709"
                     /db_xref="CDD:459912"
     CDS             1..453
                     /gene="ADSS2"
                     /gene_synonym="ADEH; ADSS; ADSS 2"
                     /coded_by="NM_001365073.2:244..1605"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:159"
                     /db_xref="HGNC:HGNC:292"
                     /db_xref="MIM:103060"
ORIGIN      
        1 mafaetypaa sslpngdcgr prarpggnrv tvvlgaqwgd egkgkvvdll aqdadivcrc
       61 qggnnaghtv vvdsveydfh llpsgiinpn vtafigngvv ihlpglfeea eknvqkgkgl
      121 egwekrliis drahivfdfh qaadgiqeqq rqeqagknlg ttkkgigpvy sskaarsglr
      181 mcdlvsdfdg fserfkvlan qyksiyptle idiegelqkl kgymekikpm vrdgvyflye
      241 alhgppkkil veganaalld idfgtypfvt ssnctvggvc tglgmppqnv gevygvvkay
      301 ttrvgigafp teqdneigel lqtrgrefgv ttgrkrrcgw ldlvllkyah mingftalal
      361 tkldildmft eikvgvaykl dgeiiphipe vlnkvevqyk tlpgwntdis narafkelpv
      421 naqnyvrfie delqipvkwi gvgksresmi qlf
//
LOCUS       NP_004978                325 aa            linear   PRI 21-NOV-2025
DEFINITION  LIM and senescent cell antigen-like-containing domain protein 1
            isoform b [Homo sapiens].
ACCESSION   NP_004978 XP_943866
VERSION     NP_004978.2
DBSOURCE    REFSEQ: accession NM_004987.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Caliskan,Y., Ozluk,Y., Kurashima,K., Mirioglu,S., Dirim,A.B.,
            Hurdogan,O., Oto,O.A., Syn,M., Nazzal,M., Jain,A., Edwards,J.,
            Yazici,H. and Lentine,K.L.
  TITLE     LIM Zinc Finger Domain Containing 1 Risk Genotype of Recipient Is
            Associated with Renal Tubular Inflammation in Kidney
            Transplantation
  JOURNAL   Genes (Basel) 15 (6), 773 (2024)
   PUBMED   38927709
  REMARK    GeneRIF: LIM Zinc Finger Domain Containing 1 Risk Genotype of
            Recipient Is Associated with Renal Tubular Inflammation in Kidney
            Transplantation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Li,Y., Wang,S., Li,G., Gao,C., Cui,Z., Cong,M., Hu,J., Zhang,M.,
            Jin,X., Sun,H. and Kong,D.
  TITLE     The RNA-binding protein RBMS3 inhibits the progression of colon
            cancer by regulating the stability of LIMS1 mRNA
  JOURNAL   Cancer Med 13 (7), e7129 (2024)
   PUBMED   38618967
  REMARK    GeneRIF: The RNA-binding protein RBMS3 inhibits the progression of
            colon cancer by regulating the stability of LIMS1 mRNA.
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Gorska,A. and Mazur,A.J.
  TITLE     Integrin-linked kinase (ILK): the known vs. the unknown and
            perspectives
  JOURNAL   Cell Mol Life Sci 79 (2), 100 (2022)
   PUBMED   35089438
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Gubin,A.N., Njoroge,J.M., Bouffard,G.G. and Miller,J.L.
  TITLE     Gene expression in proliferating human erythroid cells
  JOURNAL   Genomics 59 (2), 168-177 (1999)
   PUBMED   10409428
REFERENCE   8  (residues 1 to 325)
  AUTHORS   Tu,Y., Li,F., Goicoechea,S. and Wu,C.
  TITLE     The LIM-only protein PINCH directly interacts with integrin-linked
            kinase and is recruited to integrin-rich sites in spreading cells
  JOURNAL   Mol Cell Biol 19 (3), 2425-2434 (1999)
   PUBMED   10022929
REFERENCE   9  (residues 1 to 325)
  AUTHORS   Tu,Y., Li,F. and Wu,C.
  TITLE     Nck-2, a novel Src homology2/3-containing adaptor protein that
            interacts with the LIM-only protein PINCH and components of growth
            factor receptor kinase-signaling pathways
  JOURNAL   Mol Biol Cell 9 (12), 3367-3382 (1998)
   PUBMED   9843575
REFERENCE   10 (residues 1 to 325)
  AUTHORS   Rearden,A.
  TITLE     A new LIM protein containing an autoepitope homologous to
            'senescent cell antigen'
  JOURNAL   Biochem Biophys Res Commun 201 (3), 1124-1131 (1994)
   PUBMED   7517666
  REMARK    Erratum:[Biochem Biophys Res Commun 2001 Apr 13;282(4):1074]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG942518.1, U09284.2,
            AC010095.6 and AL110164.1.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_943866.1, NP_004978.1.
            
            Summary: The protein encoded by this gene is an adaptor protein
            which contains five LIM domains, or double zinc fingers. The
            protein is likely involved in integrin signaling through its LIM
            domain-mediated interaction with integrin-linked kinase, found in
            focal adhesion plaques. It is also thought to act as a bridge
            linking integrin-linked kinase to NCK adaptor protein 2, which is
            involved in growth factor receptor kinase signaling pathways. Its
            localization to the periphery of spreading cells also suggests that
            this protein may play a role in integrin-mediated cell adhesion or
            spreading. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.89528.1,
                                           SRR5189661.97190.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q12.3"
     Protein         1..325
                     /product="LIM and senescent cell antigen-like-containing
                     domain protein 1 isoform b"
                     /note="LIM and senescent cell antigen-like-containing
                     domain protein 1; renal carcinoma antigen NY-REN-48; LIM
                     and senescent cell antigen-like domains 1; LIM-type zinc
                     finger domains 1; particularly interesting new Cys-His
                     protein 1"
                     /calculated_mol_wt=37120
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:12665801; propagated from
                     UniProtKB/Swiss-Prot (P48059.4)"
     Region          10..68
                     /region_name="LIM1_PINCH"
                     /note="The first LIM domain of protein PINCH; cd09331"
                     /db_xref="CDD:188717"
     Site            order(10,13,32,35,38,41,59,62)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188717"
     Site            order(12..13,15,37,39..43,53..54,56,61..62,64..68)
                     /site_type="other"
                     /note="ILK binding interface"
                     /db_xref="CDD:188717"
     Region          71..122
                     /region_name="LIM2_PINCH"
                     /note="The second LIM domain of protein PINCH; cd09332"
                     /db_xref="CDD:188718"
     Site            order(71,74,91,94,97,100,118,121)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188718"
     Region          135..185
                     /region_name="LIM3_PINCH"
                     /note="The third LIM domain of protein PINCH; cd09333"
                     /db_xref="CDD:188719"
     Site            order(135,138,155,158,161,164,181,184)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188719"
     Region          191..244
                     /region_name="LIM4_PINCH"
                     /note="The fourth LIM domain of protein PINCH; cd09334"
                     /db_xref="CDD:188720"
     Site            order(192,196..199)
                     /site_type="other"
                     /note="N(i)ck binding interface"
                     /db_xref="CDD:188720"
     Site            order(193,196,213,216,219,222,240,243)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188720"
     Region          252..305
                     /region_name="LIM5_PINCH"
                     /note="The fifth LIM domain of protein PINCH; cd09335"
                     /db_xref="CDD:188721"
     Site            order(252,255,272,275,278,281,300,303)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188721"
     CDS             1..325
                     /gene="LIMS1"
                     /gene_synonym="PINCH; PINCH-1; PINCH1"
                     /coded_by="NM_004987.6:125..1102"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS2078.1"
                     /db_xref="GeneID:3987"
                     /db_xref="HGNC:HGNC:6616"
                     /db_xref="MIM:602567"
ORIGIN      
        1 manalasatc erckggfapa ekivnsngel yheqcfvcaq cfqqfpeglf yefegrkyce
       61 hdfqmlfapc chqcgefiig rvikamnnsw hpecfrcdlc qevladigfv knagrhlcrp
      121 chnrekargl gkyicqkcha iideqplifk ndpyhpdhfn cancgkelta darelkgely
      181 clpchdkmgv picgacrrpi egrvvnamgk qwhvehfvca kcekpflghr hyerkglayc
      241 ethynqlfgd vcfhcnrvie gdvvsalnka wcvncfacst cntkltlknk fvefdmkpvc
      301 kkcyekfple lkkrlkklae tlgrk
//
LOCUS       NP_001308004             724 aa            linear   PRI 21-NOV-2025
DEFINITION  disks large homolog 4 isoform 4 [Homo sapiens].
ACCESSION   NP_001308004 XP_005256549
VERSION     NP_001308004.1
DBSOURCE    REFSEQ: accession NM_001321075.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Fadahunsi,N., Petersen,J., Metz,S., Jakobsen,A., Vad Mathiesen,C.,
            Silke Buch-Rasmussen,A., Kurgan,N., Kjaergaard Larsen,J.,
            Andersen,R.C., Topilko,T., Svendsen,C., Apuschkin,M., Skovbjerg,G.,
            Hendrik Schmidt,J., Houser,G., Elgaard Jager,S., Bach,A.,
            Deshmukh,A.S., Kilpelainen,T.O., Stromgaard,K., Madsen,K.L. and
            Clemmensen,C.
  TITLE     Targeting postsynaptic glutamate receptor scaffolding proteins
            PSD-95 and PICK1 for obesity treatment
  JOURNAL   Sci Adv 10 (9), eadg2636 (2024)
   PUBMED   38427737
  REMARK    GeneRIF: Targeting postsynaptic glutamate receptor scaffolding
            proteins PSD-95 and PICK1 for obesity treatment.
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Shen,Z., Sun,D., Savastano,A., Varga,S.J., Cima-Omori,M.S.,
            Becker,S., Honigmann,A. and Zweckstetter,M.
  TITLE     Multivalent Tau/PSD-95 interactions arrest in vitro condensates and
            clusters mimicking the postsynaptic density
  JOURNAL   Nat Commun 14 (1), 6839 (2023)
   PUBMED   37891164
  REMARK    GeneRIF: Multivalent Tau/PSD-95 interactions arrest in vitro
            condensates and clusters mimicking the postsynaptic density.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Shimizu,H. and Hohjoh,H.
  TITLE     FMRP, FXR1 protein and Dlg4 mRNA, which are associated with fragile
            X syndrome, are involved in the ubiquitin-proteasome system
  JOURNAL   Sci Rep 13 (1), 1956 (2023)
   PUBMED   36732356
  REMARK    GeneRIF: FMRP, FXR1 protein and Dlg4 mRNA, which are associated
            with fragile X syndrome, are involved in the ubiquitin-proteasome
            system.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 724)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 724)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 724)
  AUTHORS   Niethammer,M., Kim,E. and Sheng,M.
  TITLE     Interaction between the C terminus of NMDA receptor subunits and
            multiple members of the PSD-95 family of membrane-associated
            guanylate kinases
  JOURNAL   J Neurosci 16 (7), 2157-2163 (1996)
   PUBMED   8601796
REFERENCE   7  (residues 1 to 724)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   8  (residues 1 to 724)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 724)
  AUTHORS   Kornau,H.C., Schenker,L.T., Kennedy,M.B. and Seeburg,P.H.
  TITLE     Domain interaction between NMDA receptor subunits and the
            postsynaptic density protein PSD-95
  JOURNAL   Science 269 (5231), 1737-1740 (1995)
   PUBMED   7569905
REFERENCE   10 (residues 1 to 724)
  AUTHORS   Tumer,Z., Dye,T.J., Prada,C., White-Brown,A.M., MacKenzie,A. and
            Levy,A.M.
  TITLE     DLG4-Related Synaptopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37347881
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC336011.1, AK293835.1,
            BC030203.1, BG059570.1 and AC120057.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 18, 2016 this sequence version replaced XP_005256549.1.
            
            Summary: This gene encodes a member of the membrane-associated
            guanylate kinase (MAGUK) family. It heteromultimerizes with another
            MAGUK protein, DLG2, and is recruited into NMDA receptor and
            potassium channel clusters. These two MAGUK proteins may interact
            at postsynaptic sites to form a multimeric scaffold for the
            clustering of receptors, ion channels, and associated signaling
            proteins. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293835.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399506.9/ ENSP00000382425.2
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..724
                     /product="disks large homolog 4 isoform 4"
                     /note="disks large homolog 4; Tax interaction protein 15;
                     post-synaptic density protein 95; synapse-associated
                     protein 90; discs large homolog 4"
                     /calculated_mol_wt=80365
     Region          11..64
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          15..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78352.3)"
     Region          63..151
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62108; propagated from
                     UniProtKB/Swiss-Prot (P78352.3)"
     Site            order(74..80,97,100,130,134,137..138)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62108; propagated from
                     UniProtKB/Swiss-Prot (P78352.3)"
     Region          160..244
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(169..175,192,195,225,229,232..233)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q62108; propagated from
                     UniProtKB/Swiss-Prot (P78352.3)"
     Region          245..312
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31016; propagated from
                     UniProtKB/Swiss-Prot (P78352.3)"
     Region          310..400
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(322..328,339,342,372,376,379..380)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62108; propagated from
                     UniProtKB/Swiss-Prot (P78352.3)"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62108; propagated from
                     UniProtKB/Swiss-Prot (P78352.3)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q62108; propagated from
                     UniProtKB/Swiss-Prot (P78352.3)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62108; propagated from
                     UniProtKB/Swiss-Prot (P78352.3)"
     Site            425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62108; propagated from
                     UniProtKB/Swiss-Prot (P78352.3)"
     Region          430..495
                     /region_name="SH3_DLG4"
                     /note="Src Homology 3 domain of Disks Large homolog 4;
                     cd12030"
                     /db_xref="CDD:212963"
     Site            order(434,456)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212963"
     Site            order(437,439,442,451,469..470,489,491..492)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212963"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31016; propagated from
                     UniProtKB/Swiss-Prot (P78352.3)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62108; propagated from
                     UniProtKB/Swiss-Prot (P78352.3)"
     Region          533..711
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     Site            580
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q62108; propagated from
                     UniProtKB/Swiss-Prot (P78352.3)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62108; propagated from
                     UniProtKB/Swiss-Prot (P78352.3)"
     Site            654
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P31016; propagated from
                     UniProtKB/Swiss-Prot (P78352.3)"
     Site            715
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q62108; propagated from
                     UniProtKB/Swiss-Prot (P78352.3)"
     CDS             1..724
                     /gene="DLG4"
                     /gene_synonym="MRD62; PSD95; SAP-90; SAP90"
                     /coded_by="NM_001321075.3:481..2655"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS82050.1"
                     /db_xref="GeneID:1742"
                     /db_xref="HGNC:HGNC:2903"
                     /db_xref="MIM:602887"
ORIGIN      
        1 mdclcivttk kyryqdedtp plehspahlp nqansppviv ntdtleapgy elqvngtege
       61 meyeeitler gnsglgfsia ggtdnphigd dpsifitkii pggaaaqdgr lrvndsilfv
      121 nevdvrevth saavealkea gsivrlyvmr rkppaekvme iklikgpkgl gfsiaggvgn
      181 qhipgdnsiy vtkiieggaa hkdgrlqigd kilavnsvgl edvmhedava alkntydvvy
      241 lkvakpsnay lsdsyappdi ttsysqhldn eishssylgt dyptamtpts prryspvakd
      301 llgeedipre prrivihrgs tglgfnivgg edgegifisf ilaggpadls gelrkgdqil
      361 svngvdlrna sheqaaialk nagqtvtiia qykpeeysrf eakihdlreq lmnsslgsgt
      421 aslrsnpkrg fyiralfdyd ktkdcgflsq alsfrfgdvl hvidasdeew wqarrvhsds
      481 etddigfips krrverrews rlkakdwgss sgsqgredsv lsyetvtqme vhyarpiiil
      541 gptkdrandd llsefpdkfg scvphttrpk reyeidgrdy hfvssrekme kdiqahkfie
      601 agqynshlyg tsvqsvreva eqgkhcildv sanavrrlqa ahlhpiaifi rprslenvle
      661 inkriteeqa rkafdratkl eqeftecfsa ivegdsfeei yhkvkrvied lsgpyiwvpa
      721 rerl
//
LOCUS       NP_001275716             462 aa            linear   PRI 21-NOV-2025
DEFINITION  TOM1-like protein 2 isoform 5 [Homo sapiens].
ACCESSION   NP_001275716 XP_005256522
VERSION     NP_001275716.1
DBSOURCE    REFSEQ: accession NM_001288787.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Shinde,S.R., Mick,D.U., Aoki,E., Rodrigues,R.B., Gygi,S.P. and
            Nachury,M.V.
  TITLE     The ancestral ESCRT protein TOM1L2 selects ubiquitinated cargoes
            for retrieval from cilia
  JOURNAL   Dev Cell 58 (8), 677-693 (2023)
   PUBMED   37019113
  REMARK    GeneRIF: The ancestral ESCRT protein TOM1L2 selects ubiquitinated
            cargoes for retrieval from cilia.
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Zhang,Y., Wolf-Yadlin,A., Ross,P.L., Pappin,D.J., Rush,J.,
            Lauffenburger,D.A. and White,F.M.
  TITLE     Time-resolved mass spectrometry of tyrosine phosphorylation sites
            in the epidermal growth factor receptor signaling network reveals
            dynamic modules
  JOURNAL   Mol Cell Proteomics 4 (9), 1240-1250 (2005)
   PUBMED   15951569
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Bi,W., Yan,J., Stankiewicz,P., Park,S.S., Walz,K., Boerkoel,C.F.,
            Potocki,L., Shaffer,L.G., Devriendt,K., Nowaczyk,M.J., Inoue,K. and
            Lupski,J.R.
  TITLE     Genes in a refined Smith-Magenis syndrome critical deletion
            interval on chromosome 17p11.2 and the syntenic region of the mouse
  JOURNAL   Genome Res 12 (5), 713-728 (2002)
   PUBMED   11997338
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Seranski,P., Heiss,N.S., Dhorne-Pollet,S., Radelof,U., Korn,B.,
            Hennig,S., Backes,E., Schmidt,S., Wiemann,S., Schwarz,C.E.,
            Lehrach,H. and Poustka,A.
  TITLE     Transcription mapping in a medulloblastoma breakpoint interval and
            Smith-Magenis syndrome candidate region: identification of 53
            transcriptional units and new candidate genes
  JOURNAL   Genomics 56 (1), 1-11 (1999)
   PUBMED   10036180
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA235267.1, AK301944.1,
            AC122129.9 and BM976586.1.
            
            On Jan 4, 2014 this sequence version replaced XP_005256522.1.
            
            Summary: This gene belongs to a small gene family whose members
            have an N-terminal VHS domain followed by a GAT domain; domains
            which typically participate in vesicular trafficking. The canonical
            protein encoded by this gene also has a C-terminal clathrin binding
            motif. This protein has been shown to interact with Tollip,
            clathrin and ubiquitin and is thought to play a role in endosomal
            sorting. This gene resides in the 3.7 Mb deletion of chromosome
            region 17p11.2 that is associated with Smith-Magenis syndrome.
            Alternative splicing results in multiple transcript variants
            encoding distinct proteins. [provided by RefSeq, Apr 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3085541.1,
                                           SRR14038197.2522873.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..462
                     /product="TOM1-like protein 2 isoform 5"
                     /note="TOM1-like protein 2; target of myb1-like 2; target
                     of Myb-like protein 2"
                     /calculated_mol_wt=50378
     Region          12..123
                     /region_name="VHS_ENTH_ANTH"
                     /note="VHS, ENTH and ANTH domain superfamily; cl02544"
                     /db_xref="CDD:470608"
     Region          173..264
                     /region_name="GAT_TM1L2"
                     /note="canonical GAT domain found in target of Myb-like
                     protein 2 (Tom1L2); cd14238"
                     /db_xref="CDD:410585"
     Site            order(184..185,188..189,191..192,195..196,199,212,
                     215..216)
                     /site_type="other"
                     /note="putative ubiquitin binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410585"
     CDS             1..462
                     /gene="TOM1L2"
                     /coded_by="NM_001288787.2:88..1476"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS74002.1"
                     /db_xref="GeneID:146691"
                     /db_xref="HGNC:HGNC:11984"
                     /db_xref="MIM:615519"
ORIGIN      
        1 mefllgnpfs tpvgqcleka tdgslqsedw tlnmeicdii neteegpkda iralkkrlng
       61 nrnyrevmla ltvletcvkn cghrfhilva nrdfidsvlv kiispknnpp tivqdkvlal
      121 iqsvpevdpa atmprsqsqq rtsagsyssp ppapysapqa palsvtgpit anseqiarlr
      181 seldvvrgnt kvmsemltem vpgqedssdl ellqelnrtc ramqqrivel isrvsneevt
      241 eellhvnddl nnvflryerf eryrsgrsvq nasngvlnev tednlidlgp gspavvspmv
      301 gntappssls sqlagldlgt esvsgtlssl qqcnprdgfd mfaqtrgnsl aeqrktvtye
      361 dpqavgglas aldnrkqsse gipvaqpsvm ddievwlrtd lkgddleegv tseefdkfle
      421 erakaaemvp dlpsppmeap apasnpsgrk kpersedalf al
//
LOCUS       NP_001269368             141 aa            linear   PRI 21-NOV-2025
DEFINITION  biogenesis of lysosome-related organelles complex 1 subunit 2
            isoform 4 [Homo sapiens].
ACCESSION   NP_001269368
VERSION     NP_001269368.1
DBSOURCE    REFSEQ: accession NM_001282439.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 141)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 141)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 141)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 141)
  AUTHORS   Yordanov,T.E., Hipolito,V.E.B., Liebscher,G., Vogel,G.F.,
            Stasyk,T., Herrmann,C., Geley,S., Teis,D., Botelho,R.J., Hess,M.W.
            and Huber,L.A.
  TITLE     Biogenesis of lysosome-related organelles complex-1 (BORC)
            regulates late endosomal/lysosomal size through PIKfyve-dependent
            phosphatidylinositol-3,5-bisphosphate
  JOURNAL   Traffic 20 (9), 674-696 (2019)
   PUBMED   31314175
REFERENCE   5  (residues 1 to 141)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 141)
  AUTHORS   Wang,Z., Wei,H., Yu,Y., Sun,J., Yang,Y., Xing,G., Wu,S., Zhou,Y.,
            Zhu,Y., Zhang,C., Zhou,T., Zhao,X., Sun,Q. and He,F.
  TITLE     Characterization of Ceap-11 and Ceap-16, two novel
            splicing-variant-proteins, associated with centrosome, microtubule
            aggregation and cell proliferation
  JOURNAL   J Mol Biol 343 (1), 71-82 (2004)
   PUBMED   15381421
REFERENCE   7  (residues 1 to 141)
  AUTHORS   Starcevic,M. and Dell'Angelica,E.C.
  TITLE     Identification of snapin and three novel proteins (BLOS1, BLOS2,
            and BLOS3/reduced pigmentation) as subunits of biogenesis of
            lysosome-related organelles complex-1 (BLOC-1)
  JOURNAL   J Biol Chem 279 (27), 28393-28401 (2004)
   PUBMED   15102850
  REMARK    GeneRIF: Biogenesis of lysosome-related organelles complex-1
            (BLOC-1) subunit 2 (BLOS2).BLOC-1 is required for the biogenesis of
            melanosomes and platelet dense granules.
REFERENCE   8  (residues 1 to 141)
  AUTHORS   Li,W., Zhang,Q., Oiso,N., Novak,E.K., Gautam,R., O'Brien,E.P.,
            Tinsley,C.L., Blake,D.J., Spritz,R.A., Copeland,N.G., Jenkins,N.A.,
            Amato,D., Roe,B.A., Starcevic,M., Dell'Angelica,E.C., Elliott,R.W.,
            Mishra,V., Kingsmore,S.F., Paylor,R.E. and Swank,R.T.
  TITLE     Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant
            dysbindin, a member of the biogenesis of lysosome-related
            organelles complex 1 (BLOC-1)
  JOURNAL   Nat Genet 35 (1), 84-89 (2003)
   PUBMED   12923531
REFERENCE   9  (residues 1 to 141)
  AUTHORS   Ciciotte,S.L., Gwynn,B., Moriyama,K., Huizing,M., Gahl,W.A.,
            Bonifacino,J.S. and Peters,L.L.
  TITLE     Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a
            novel protein that is part of the pallidin-muted complex (BLOC-1)
  JOURNAL   Blood 101 (11), 4402-4407 (2003)
   PUBMED   12576321
REFERENCE   10 (residues 1 to 141)
  AUTHORS   Moriyama,K. and Bonifacino,J.S.
  TITLE     Pallidin is a component of a multi-protein complex involved in the
            biogenesis of lysosome-related organelles
  JOURNAL   Traffic 3 (9), 666-677 (2002)
   PUBMED   12191018
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB456773.1, BU608851.1, CB218039.1, DB296446.1, AL138921.14 and
            BX112121.1.
            
            Summary: This gene encodes a protein with multiple functions. The
            encoded protein has been found in association with the centrosome,
            shown to co-localize with gamma-tubulin, and also found to be one
            of the proteins in the BLOC-1 complex which functions in the
            formation of lysosome-related organelles. A pseudogene of this gene
            is located on the X chromosome. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Feb 2012].
            
            Transcript Variant: This variant (6) uses an alternate in-frame
            splice site in the 3' coding region, compared to variant 1. This
            results in a shorter protein (isoform 4), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2247961.1,
                                           SRR1803615.177145.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..141
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.31"
     Protein         1..141
                     /product="biogenesis of lysosome-related organelles
                     complex 1 subunit 2 isoform 4"
                     /note="centrosome protein oncogene; biogenesis of
                     lysosome-related organelles complex 1 subunit 2;
                     centrosomal 10 kDa protein; BLOC-1 subunit 2; 11 kDa
                     centrosome associated protein"
                     /calculated_mol_wt=15701
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6QNY1.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q6QNY1.1)"
     Region          42..136
                     /region_name="BLOC1_2"
                     /note="Biogenesis of lysosome-related organelles complex-1
                     subunit 2; pfam10046"
                     /db_xref="CDD:462951"
     CDS             1..141
                     /gene="BLOC1S2"
                     /gene_synonym="BLOS2; BORCS2; CEAP; CEAP11"
                     /coded_by="NM_001282439.2:22..447"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:282991"
                     /db_xref="HGNC:HGNC:20984"
                     /db_xref="MIM:609768"
ORIGIN      
        1 maaaaegvla trsdepardd aavetaeeak epaeaditel crdmfskmat yltgeltats
       61 edykllenmn kltslkylem kdiainisrn lkdlnqkyag lqpyldqinv ieeqvaaleq
      121 aaykldaysk klakykklek r
//
LOCUS       NP_000070                457 aa            linear   PRI 21-NOV-2025
DEFINITION  acetylcholine receptor subunit alpha isoform b precursor [Homo
            sapiens].
ACCESSION   NP_000070
VERSION     NP_000070.1
DBSOURCE    REFSEQ: accession NM_000079.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Rodriguez Cruz,P.M., Ravenscroft,G., Natera,D., Carr,A., Manzur,A.,
            Liu,W.W., Vella,N.R., Jerico,I., Gonzalez-Quereda,L., Gallano,P.,
            Montalto,S.A., Davis,M.R., Lamont,P.J., Laing,N.G., Bourque,P.,
            Nascimento,A., Muntoni,F., Polavarapu,K., Lochmuller,H., Palace,J.
            and Beeson,D.
  TITLE     A novel phenotype of AChR-deficiency syndrome with predominant
            facial and distal weakness resulting from the inclusion of an
            evolutionary alternatively-spliced exon in CHRNA1
  JOURNAL   Neuromuscul Disord 33 (2), 161-168 (2023)
   PUBMED   36634413
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Lin,J.B., Kang,M.Q., Huang,L.P., Zhuo,Y., Li,X. and Lai,F.C.
  TITLE     CHRNA1 promotes the pathogenesis of primary focal hyperhidrosis
  JOURNAL   Mol Cell Neurosci 111, 103598 (2021)
   PUBMED   33476802
  REMARK    GeneRIF: CHRNA1 promotes the pathogenesis of primary focal
            hyperhidrosis.
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Kudryavtsev,D., Isaeva,A., Barkova,D., Spirova,E., Mukhutdinova,R.,
            Kasheverov,I. and Tsetlin,V.
  TITLE     Point Mutations of Nicotinic Receptor alpha1 Subunit Reveal New
            Molecular Features of G153S Slow-Channel Myasthenia
  JOURNAL   Molecules 26 (5), 1278 (2021)
   PUBMED   33652901
  REMARK    GeneRIF: Point Mutations of Nicotinic Receptor alpha1 Subunit
            Reveal New Molecular Features of G153S Slow-Channel Myasthenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Uzawa,A., Ozawa,Y., Yasuda,M., Oda,F., Kojima,Y., Kawaguchi,N.,
            Kanai,T., Himuro,K. and Kuwabara,S.
  TITLE     Increased serum acetylcholine receptor alpha1 subunit protein in
            anti-acetylcholine receptor antibody-positive myasthenia gravis
  JOURNAL   J Neuroimmunol 339, 577125 (2020)
   PUBMED   31855720
  REMARK    GeneRIF: Serum AChR alpha1 subunit protein concentrations were
            higher in patients with ant-AChR antibody-positive myasthenia
            gravis than those in controls.
REFERENCE   5  (residues 1 to 457)
  AUTHORS   Wang,M., Liu,D., Schwender,H., Wang,H., Wang,P., Zhou,Z., Li,J.,
            Wu,T., Zhu,H. and Beaty,T.H.
  TITLE     Evaluating the effect of nicotinic cholinergic receptor genes on
            the risk of nonsyndromic cleft lip with or without cleft palate
  JOURNAL   Oral Dis 24 (6), 1068-1072 (2018)
   PUBMED   29688589
  REMARK    GeneRIF: In our analysis, we found one pair of SNPs in CHRNA1 and
            CHRNA7, plus one pair of SNPs in CHRNA2 and CHRNA3 reached
            corrected significance in tests for GxG interaction. Our study
            suggested evidence of interactions between CHRNs in controlling the
            risk of NSCL/P.
REFERENCE   6  (residues 1 to 457)
  AUTHORS   Abicht,A., Muller,J.S. and Lochmuller,H.
  TITLE     Congenital Myasthenic Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301347
REFERENCE   7  (residues 1 to 457)
  AUTHORS   Yu,X.M. and Hall,Z.W.
  TITLE     Extracellular domains mediating epsilon subunit interactions of
            muscle acetylcholine receptor
  JOURNAL   Nature 352 (6330), 64-67 (1991)
   PUBMED   1712080
REFERENCE   8  (residues 1 to 457)
  AUTHORS   Beeson,D., Jeremiah,S., West,L.F., Povey,S. and Newsom-Davis,J.
  TITLE     Assignment of the human nicotinic acetylcholine receptor genes: the
            alpha and delta subunit genes to chromosome 2 and the beta subunit
            gene to chromosome 17
  JOURNAL   Ann Hum Genet 54 (3), 199-208 (1990)
   PUBMED   2221824
REFERENCE   9  (residues 1 to 457)
  AUTHORS   Beeson,D., Morris,A., Vincent,A. and Newsom-Davis,J.
  TITLE     The human muscle nicotinic acetylcholine receptor alpha-subunit
            exist as two isoforms: a novel exon
  JOURNAL   EMBO J 9 (7), 2101-2106 (1990)
   PUBMED   1694127
REFERENCE   10 (residues 1 to 457)
  AUTHORS   Hohlfeld,R., Toyka,K.V., Miner,L.L., Walgrave,S.L. and
            Conti-Tronconi,B.M.
  TITLE     Amphipathic segment of the nicotinic receptor alpha subunit
            contains epitopes recognized by T lymphocytes in myasthenia gravis
  JOURNAL   J Clin Invest 81 (3), 657-660 (1988)
   PUBMED   2449458
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK315312.1, Y00762.1 and
            BC043196.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The muscle acetylcholine receptor consiststs of 5 subunits
            of 4 different types: 2 alpha subunits and 1 each of the beta,
            gamma, and delta subunits. This gene encodes an alpha subunit that
            plays a role in acetlycholine binding/channel gating. Alternatively
            spliced transcript variants encoding different isoforms have been
            identified. [provided by RefSeq, Nov 2012].
            
            Transcript Variant: This variant (2) lacks an in-frame segment of
            the coding region, compared to variant 1. It encodes a shorter
            isoform (b), that is missing an internal segment compared to
            isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK315312.1, Y00762.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158800, SAMEA2162946
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000348749.9/ ENSP00000261008.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..457
                     /product="acetylcholine receptor subunit alpha isoform b
                     precursor"
                     /note="cholinergic receptor, nicotinic, alpha polypeptide
                     1 (muscle); cholinergic receptor, nicotinic alpha 1;
                     nicotinic cholinergic receptor alpha 1; acetylcholine
                     receptor subunit alpha; nicotinic acetylcholine receptor
                     alpha subunit; muscle nicotinic acetylcholine receptor;
                     acetylcholine receptor, nicotinic, alpha 1 (muscle);
                     cholinergic receptor, nicotinic, alpha 1 (muscle)"
                     /calculated_mol_wt=49697
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2160
     Region          4..447
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     mat_peptide     21..457
                     /product="acetylcholine receptor subunit alpha isoform b"
                     /calculated_mol_wt=49697
     Region          22..231
                     /region_name="LGIC_ECD_nAChR_A1"
                     /note="extracellular domain of nicotinic acetylcholine
                     receptor subunit alpha 1 (CHRNA1); cd19014"
                     /db_xref="CDD:349815"
     Site            order(59,61,67..68,75,97,99,108..109,111,113..114,118,
                     120..121,125..127,129,139,141,143,147,169,230)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349815"
     Region          148..162
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349815"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P02708.3)"
     Site            233..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P02708.3)"
     Site            265..285
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P02708.3)"
     Site            297..317
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P02708.3)"
     Site            428..448
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P02708.3)"
     CDS             1..457
                     /gene="CHRNA1"
                     /gene_synonym="ACHRA; ACHRD; CHRNA; CMS1A; CMS1B; CMS2A;
                     FCCMS; SCCMS"
                     /coded_by="NM_000079.4:79..1452"
                     /note="isoform b precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS2261.1"
                     /db_xref="GeneID:1134"
                     /db_xref="HGNC:HGNC:1955"
                     /db_xref="MIM:100690"
ORIGIN      
        1 mepwpllllf slcsaglvlg sehetrlvak lfkdyssvvr pvedhrqvve vtvglqliql
       61 invdevnqiv ttnvrlkqqw vdynlkwnpd dyggvkkihi psekiwrpdl vlynnadgdf
      121 aivkftkvll qytghitwtp paifksycei ivthfpfdeq ncsmklgtwt ydgsvvainp
      181 esdqpdlsnf mesgewvike srgwkhsvty sccpdtpyld ityhfvmqrl plyfivnvii
      241 pcllfsfltg lvfylptdsg ekmtlsisvl lsltvfllvi velipstssa vpligkymlf
      301 tmvfviasii itvivinthh rspsthvmpn wvrkvfidti pnimffstmk rpsrekqdkk
      361 iftedidisd isgkpgpppm gfhsplikhp evksaiegik yiaetmksdq esnnaaaewk
      421 yvamvmdhil lgvfmlvcii gtlavfagrl ielnqqg
//
LOCUS       NP_001364446             760 aa            linear   PRI 21-NOV-2025
DEFINITION  gephyrin isoform 6 [Homo sapiens].
ACCESSION   NP_001364446 XP_016876408
VERSION     NP_001364446.1
DBSOURCE    REFSEQ: accession NM_001377517.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 760)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 760)
  AUTHORS   Dos Reis,R., Kornobis,E., Pereira,A., Tores,F., Carrasco,J.,
            Gautier,C., Jahannault-Talignani,C., Nitschke,P., Muchardt,C.,
            Schlosser,A., Maric,H.M., Ango,F. and Allemand,E.
  TITLE     Complex regulation of Gephyrin splicing is a determinant of
            inhibitory postsynaptic diversity
  JOURNAL   Nat Commun 13 (1), 3507 (2022)
   PUBMED   35717442
  REMARK    GeneRIF: Complex regulation of Gephyrin splicing is a determinant
            of inhibitory postsynaptic diversity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 760)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 760)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 760)
  AUTHORS   Mammoto,A., Sasaki,T., Asakura,T., Hotta,I., Imamura,H.,
            Takahashi,K., Matsuura,Y., Shirao,T. and Takai,Y.
  TITLE     Interactions of drebrin and gephyrin with profilin
  JOURNAL   Biochem Biophys Res Commun 243 (1), 86-89 (1998)
   PUBMED   9473484
REFERENCE   6  (residues 1 to 760)
  AUTHORS   Meyer,G., Kirsch,J., Betz,H. and Langosch,D.
  TITLE     Identification of a gephyrin binding motif on the glycine receptor
            beta subunit
  JOURNAL   Neuron 15 (3), 563-572 (1995)
   PUBMED   7546736
REFERENCE   7  (residues 1 to 760)
  AUTHORS   Misko,A., Mahtani,K., Abbott,J., Schwarz,G. and Atwal,P.
  TITLE     Molybdenum Cofactor Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   34870926
REFERENCE   8  (residues 1 to 760)
  AUTHORS   Balint,B. and Thomas,R.
  TITLE     Hereditary Hyperekplexia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301437
REFERENCE   9  (residues 1 to 760)
  AUTHORS   Prior,P., Schmitt,B., Grenningloh,G., Pribilla,I., Multhaup,G.,
            Beyreuther,K., Maulet,Y., Werner,P., Langosch,D., Kirsch,J. et al.
  TITLE     Primary structure and alternative splice variants of gephyrin, a
            putative glycine receptor-tubulin linker protein
  JOURNAL   Neuron 8 (6), 1161-1170 (1992)
   PUBMED   1319186
REFERENCE   10 (residues 1 to 760)
  AUTHORS   Kirsch,J., Langosch,D., Prior,P., Littauer,U.Z., Schmitt,B. and
            Betz,H.
  TITLE     The 93-kDa glycine receptor-associated protein binds to tubulin
  JOURNAL   J Biol Chem 266 (33), 22242-22245 (1991)
   PUBMED   1657993
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355093.3, AL133241.3,
            AL117667.4, AL049835.3, AL159179.3 and AL135978.4.
            
            On Jan 16, 2020 this sequence version replaced XP_016876408.1.
            
            Summary: This gene encodes a neuronal assembly protein that anchors
            inhibitory neurotransmitter receptors to the postsynaptic
            cytoskeleton via high affinity binding to a receptor subunit domain
            and tubulin dimers. In nonneuronal tissues, the encoded protein is
            also required for molybdenum cofactor biosynthesis. Mutations in
            this gene may be associated with the neurological condition
            hyperplexia and also lead to molybdenum cofactor deficiency.
            Numerous alternatively spliced transcript variants encoding
            different isoforms have been described; however, the full-length
            nature of all transcript variants is not currently known. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.92650.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..760
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3-q24.1"
     Protein         1..760
                     /product="gephyrin isoform 6"
                     /EC_number="2.10.1.1"
                     /EC_number="2.7.7.75"
                     /calculated_mol_wt=82476
     Region          15..169
                     /region_name="MogA_MoaB"
                     /note="MogA_MoaB family. Members of this family are
                     involved in biosynthesis of the molybdenum cofactor (MoCF)
                     an essential cofactor of a diverse group of redox enzymes.
                     MoCF biosynthesis is an evolutionarily conserved pathway
                     present in eubacteria, archaea; cd00886"
                     /db_xref="CDD:238451"
     Site            order(87..89,119,145..146,150,153)
                     /site_type="active"
                     /note="MPT binding site [active]"
                     /db_xref="CDD:238451"
     Site            order(89,91..92,94,98,106..108,113,116..117,127,130,169)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:238451"
     Region          351..757
                     /region_name="MoeA"
                     /note="MoeA family. Members of this family are involved in
                     biosynthesis of the molybdenum cofactor (MoCF), an
                     essential cofactor of a diverse group of redox enzymes.
                     MoCF biosynthesis is an evolutionarily conserved pathway
                     present in eubacteria, archaea and...; cd00887"
                     /db_xref="CDD:238452"
     Site            order(372,487,502..505,507,510..511,513,547,549,552,681,
                     722,753)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238452"
     Site            order(530..531,533,573,597)
                     /site_type="active"
                     /note="putative functional site [active]"
                     /db_xref="CDD:238452"
     Site            order(597..599,649..650,654,657)
                     /site_type="active"
                     /note="putative MPT binding site [active]"
                     /db_xref="CDD:238452"
     CDS             1..760
                     /gene="GPHN"
                     /gene_synonym="GEPH; GPH; GPHRYN; HKPX1; MOCODC"
                     /coded_by="NM_001377517.1:382..2664"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:10243"
                     /db_xref="HGNC:HGNC:15465"
                     /db_xref="MIM:603930"
ORIGIN      
        1 mategmiltn hdhqirvgvl tvsdscfrnl aedrsginlk dlvqdpsllg gtisaykivp
       61 deieeiketl idwcdekeln lilttggtgf aprdvtpeat keviereapg malamlmgsl
      121 nvtplgmlsr pvcgirgktl iinlpgskkg sqecfqfilp alphaidllr daivkvkevh
      181 deledlpspp pplsppptts phkqtedkgv qceeeeeekk dsgvasteds ssshitaaai
      241 aakipdsiis rgvqvlprdt aslsttpses praqatsrls tascptpklh rkleelrdhl
      301 egnvkgyslr vnvqsrcssk enilrashsa vditkvarrh rmspfpltsm dkafitvlem
      361 tpvlgteiin yrdgmgrvla qdvyakdnlp pfpasvkdgy avraadgpgd rfiigesqag
      421 eqptqtvmpg qvmrvttgap ipcgadavvq vedtelires ddgteelevr ilvqarpgqd
      481 irpighdikr gecvlakgth mgpseiglla tvgvtevevn kfpvvavmst gnellnpedd
      541 llpgkirdsn rstllatiqe hgyptinlgi vgdnpddlln alnegisrad viitsggvsm
      601 gekdylkqvl didlhaqihf grvfmkpglp ttfatldidg vrkiifalpg npvsavvtcn
      661 lfvvpalrkm qgildprpti ikarlscdvk ldprpeyhrc iltwhhqepl pwaqstgnqm
      721 ssrlmsmrsa ngllmlppkt eqyvelhkge vvdvmvigrl
//
LOCUS       NP_001380287             340 aa            linear   PRI 21-NOV-2025
DEFINITION  citramalyl-CoA lyase, mitochondrial isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001380287
VERSION     NP_001380287.1
DBSOURCE    REFSEQ: accession NM_001393358.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Griffith,C.M., Conrotte,J.F., Paydar,P., Xie,X.,
            Heins-Marroquin,U., Gavotto,F., Jager,C., Ellens,K.W. and
            Linster,C.L.
  TITLE     CLYBL averts vitamin B12 depletion by repairing malyl-CoA
  JOURNAL   Nat Chem Biol 21 (6), 906-915 (2025)
   PUBMED   40108300
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Shen,H., Campanello,G.C., Flicker,D., Grabarek,Z., Hu,J., Luo,C.,
            Banerjee,R. and Mootha,V.K.
  TITLE     The Human Knockout Gene CLYBL Connects Itaconate to Vitamin B12
  JOURNAL   Cell 171 (4), 771-782 (2017)
   PUBMED   29056341
  REMARK    GeneRIF: Study reports that CLYBL loss leads to a cell-autonomous
            defect in the mitochondrial B12 metabolism and that itaconyl-CoA is
            a cofactor-inactivating, substrate-analog inhibitor of the
            mitochondrial B12-dependent methylmalonyl-CoA mutase
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Bossini-Castillo,L., de Kovel,C., Kallberg,H., van 't Slot,R.,
            Italiaander,A., Coenen,M., Tak,P.P., Posthumus,M.D., Wijmenga,C.,
            Huizinga,T., van der Helm-van Mil,A.H., Stoeken-Rijsbergen,G.,
            Rodriguez-Rodriguez,L., Balsa,A., Gonzalez-Alvaro,I.,
            Gonzalez-Gay,M.A., Gomez-Vaquero,C., Franke,B., Vermeulen,S., van
            der Horst-Bruinsma,Ie., Dijkmans,B.A., Wolbink,G.J., Ophoff,R.A.,
            Maehlen,M.T., van Riel,P., Merriman,M., Klareskog,L., Lie,B.A.,
            Merriman,T., Crusius,J.B., Brouwer,E., Martin,J., de Vries,N.,
            Toes,R., Padyukov,L. and Koeleman,B.P.
  CONSRTM   LifeLines Cohort Study
  TITLE     A genome-wide association study of rheumatoid arthritis without
            antibodies against citrullinated peptides
  JOURNAL   Ann Rheum Dis 74 (3), e15 (2015)
   PUBMED   24532677
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Strittmatter,L., Li,Y., Nakatsuka,N.J., Calvo,S.E., Grabarek,Z. and
            Mootha,V.K.
  TITLE     CLYBL is a polymorphic human enzyme with malate synthase and
            beta-methylmalate synthase activity
  JOURNAL   Hum Mol Genet 23 (9), 2313-2323 (2014)
   PUBMED   24334609
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Lin,X., Lu,D., Gao,Y., Tao,S., Yang,X., Feng,J., Tan,A., Zhang,H.,
            Hu,Y., Qin,X., Kim,S.T., Peng,T., Li,L., Mo,L., Zhang,S.,
            Trent,J.M., Mo,Z., Zheng,S.L., Xu,J. and Sun,J.
  TITLE     Genome-wide association study identifies novel loci associated with
            serum level of vitamin B12 in Chinese men
  JOURNAL   Hum Mol Genet 21 (11), 2610-2617 (2012)
   PUBMED   22367966
REFERENCE   7  (residues 1 to 340)
  AUTHORS   Morikawa,J., Nishimura,Y., Uchida,A. and Tanaka,T.
  TITLE     Molecular cloning of novel mouse and human putative citrate lyase
            beta-subunit
  JOURNAL   Biochem Biophys Res Commun 289 (5), 1282-1286 (2001)
   PUBMED   11741334
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL139035.27 and AL137139.9.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2142680 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q32.3"
     Protein         1..340
                     /product="citramalyl-CoA lyase, mitochondrial isoform 1
                     precursor"
                     /EC_number="2.3.3.9"
                     /EC_number="4.1.3.25"
                     /EC_number="3.1.2.30"
                     /note="citrate lyase subunit beta-like protein,
                     mitochondrial; malate synthase; beta-methylmalate
                     synthase; citramalyl-CoA lyase, mitochondrial;
                     (3S)-malyl-CoA thioesterase; citrate lyase beta like"
                     /calculated_mol_wt=35015
     transit_peptide 1..22
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q8N0X4.2)"
                     /calculated_mol_wt=2363
     mat_peptide     23..340
                     /product="Citramalyl-CoA lyase, mitochondrial.
                     /id=PRO_0000286389"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N0X4.2)"
                     /calculated_mol_wt=35015
     Region          44..340
                     /region_name="CitE"
                     /note="Citrate lyase beta subunit [Carbohydrate transport
                     and metabolism]; COG2301"
                     /db_xref="CDD:441876"
     Site            57
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8R4N0; propagated from
                     UniProtKB/Swiss-Prot (Q8N0X4.2)"
     Site            61
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8R4N0; propagated from
                     UniProtKB/Swiss-Prot (Q8N0X4.2)"
     Site            82
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8R4N0; propagated from
                     UniProtKB/Swiss-Prot (Q8N0X4.2)"
     Site            92
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8R4N0; propagated from
                     UniProtKB/Swiss-Prot (Q8N0X4.2)"
     CDS             1..340
                     /gene="CLYBL"
                     /gene_synonym="CLB"
                     /coded_by="NM_001393358.1:7..1029"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 5"
                     /db_xref="CCDS:CCDS32002.1"
                     /db_xref="GeneID:171425"
                     /db_xref="HGNC:HGNC:18355"
                     /db_xref="MIM:609686"
ORIGIN      
        1 malrllrraa rgaaaaallr lkaslaadip rlgysssshh kyiprravly vpgndekkik
       61 kipslnvdca vldcedgvaa nkknearlri vktledidlg ptekcvrvns vssglaeedl
      121 etllqsrvlp sslmlpkves peeiqwfadk fsfhlkgrkl eqpmnlipfv etamgllnfk
      181 avceetlkvg pqvglfldav vfggedfras igatssketl dilyarqkiv viakafglqa
      241 idlvyidfrd gagllrqsre gaamgftgkq vihpnqiavv qeqfspspek ikwaeeliaa
      301 fkehqqlgkg aftfqgsmid mpllkqaqnt vtlatsikek
//
LOCUS       NP_001364154            1149 aa            linear   PRI 21-NOV-2025
DEFINITION  plakophilin-4 isoform b [Homo sapiens].
ACCESSION   NP_001364154
VERSION     NP_001364154.1
DBSOURCE    REFSEQ: accession NM_001377225.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1149)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1149)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1149)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1149)
  AUTHORS   Park,S.S., Ponce-Balbuena,D., Kuick,R., Guerrero-Serna,G., Yoon,J.,
            Mellacheruvu,D., Conlon,K.P., Basrur,V., Nesvizhskii,A.I.,
            Jalife,J. and Rual,J.F.
  TITLE     Kir2.1 Interactome Mapping Uncovers PKP4 as a Modulator of the
            Kir2.1-Regulated Inward Rectifier Potassium Currents
  JOURNAL   Mol Cell Proteomics 19 (9), 1436-1449 (2020)
   PUBMED   32541000
  REMARK    GeneRIF: Kir2.1 Interactome Mapping Uncovers PKP4 as a Modulator of
            the Kir2.1-Regulated Inward Rectifier Potassium Currents.
REFERENCE   5  (residues 1 to 1149)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 1149)
  AUTHORS   Stahl,B., Diehlmann,A. and Sudhof,T.C.
  TITLE     Direct interaction of Alzheimer's disease-related presenilin 1 with
            armadillo protein p0071
  JOURNAL   J Biol Chem 274 (14), 9141-9148 (1999)
   PUBMED   10092585
REFERENCE   7  (residues 1 to 1149)
  AUTHORS   Levesque,G., Yu,G., Nishimura,M., Zhang,D.M., Levesque,L., Yu,H.,
            Xu,D., Liang,Y., Rogaeva,E., Ikeda,M., Duthie,M., Murgolo,N.,
            Wang,L., VanderVere,P., Bayne,M.L., Strader,C.D., Rommens,J.M.,
            Fraser,P.E. and St George-Hyslop,P.
  TITLE     Presenilins interact with armadillo proteins including
            neural-specific plakophilin-related protein and beta-catenin
  JOURNAL   J Neurochem 72 (3), 999-1008 (1999)
   PUBMED   10037471
REFERENCE   8  (residues 1 to 1149)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   9  (residues 1 to 1149)
  AUTHORS   Paffenholz,R. and Franke,W.W.
  TITLE     Identification and localization of a neurally expressed member of
            the plakoglobin/armadillo multigene family
  JOURNAL   Differentiation 61 (5), 293-304 (1997)
   PUBMED   9342840
REFERENCE   10 (residues 1 to 1149)
  AUTHORS   Hatzfeld,M. and Nachtsheim,C.
  TITLE     Cloning and characterization of a new armadillo family member,
            p0071, associated with the junctional plaque: evidence for a
            subfamily of closely related proteins
  JOURNAL   J Cell Sci 109 (Pt 11), 2767-2778 (1996)
   PUBMED   8937994
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008070.4 and AC005042.2.
            
            Summary: Armadillo-like proteins are characterized by a series of
            armadillo repeats, first defined in the Drosophila 'armadillo' gene
            product, that are typically 42 to 45 amino acids in length. These
            proteins can be divided into subfamilies based on their number of
            repeats, their overall sequence similarity, and the dispersion of
            the repeats throughout their sequences. Members of the
            p120(ctn)/plakophilin subfamily of Armadillo-like proteins,
            including CTNND1, CTNND2, PKP1, PKP2, PKP4, and ARVCF. PKP4 may be
            a component of desmosomal plaque and other adhesion plaques and is
            thought to be involved in regulating junctional plaque organization
            and cadherin function. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Feb 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR3218371.330812.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1149
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.1"
     Protein         1..1149
                     /product="plakophilin-4 isoform b"
                     /note="catenin 4"
                     /calculated_mol_wt=127014
     Region          <194..347
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          530..555
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(546,550,554,588,592,596,633,637,641)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          559..598
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          563..599
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          603..644
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          607..642
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          649..700
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          708..749
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          825..855
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          848..>969
                     /region_name="PLN03200"
                     /note="cellulose synthase-interactive protein;
                     Provisional"
                     /db_xref="CDD:215629"
     Region          865..900
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          867..899
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(890,894,898,936,940,944,982,986)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          906..947
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          949..993
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          953..988
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     CDS             1..1149
                     /gene="PKP4"
                     /gene_synonym="p0071"
                     /coded_by="NM_001377225.1:270..3719"
                     /note="isoform b is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS33306.1"
                     /db_xref="GeneID:8502"
                     /db_xref="HGNC:HGNC:9026"
                     /db_xref="MIM:604276"
ORIGIN      
        1 mpapeqaslv eegqpqtrqe aastgpgmep ettattilas vkeqelqfqr ltreleverq
       61 ivasqlercr lgaespsias tssteksfpw rstdvpntgv skprvsdavq pnnylirtep
      121 eqgtlyspeq tslhesegsl gnsrsstqmn sysdsgyqea gsfhnsqnvs kadnrqqhsf
      181 igstnnhvvr nsraegqtlv qpsvanramr rvssvpsraq spsyvistgv spsrgslrts
      241 lgsgfgspsv tdprplnpsa yssttlpaar aaspysqrpa sptairrigs vtsrqtsnpn
      301 gptpqyqtta rvgspltltd aqtrvaspsq gqvgssspkr sgmtavpqhl gpslqrtvhd
      361 meqfgqqqyd iyermvpprp dsltglrssy asqhsqlgqd lrsavspdlh itpiyegrty
      421 yspvyrspnh gtvelqgsqt alyrtgsvgi gnlqrtssqr stltyqrnny alnttatyae
      481 pyrpiqyrvq ecnynrlqha vpaddgttrs psidsiqkdp refawrdpel pevihmlqhq
      541 fpsvqanaaa ylqhlcfgdn kvkmevcrlg gikhlvdlld hrvlevqkna cgalrnlvfg
      601 kstdenkiam knvggipall rllrksidae vrelvtgvlw nlsscdavkm tiirdalstl
      661 tntvivphsg wnnssfdddh kikfqtslvl rnttgclrnl ssageearkq mrsceglvds
      721 llyvihtcvn tsdydsktve ncvctlrnls yrlelevpqa rllglneldd llgkespskd
      781 sepscwgkkk kkkkrtpqed qwdgvgpipg lskspkgvem lwhpsvvkpy ltllaessnp
      841 atlegsagsl qnlsagnwkf aayiraavrk ekglpilvel lrmdndrvvs svatalrnma
      901 ldvrnkelig kyamrdlvnr lpggngpsvl sdetmaaicc alhevtsknm enakaladsg
      961 gieklvnitk grgdrsslkv vkaaaqvlnt lwqyrdlrsi ykkdgwnqnh fitpvstler
     1021 drfkshpsls ttnqqmspii qsgsskpspi yissysspar eqnrrlqhqq lyysqddsnr
     1081 knfdayrlyl qsphsyedpy fddrvhfpas tdystqyglk sttnyvdfys tkrpsyraeq
     1141 ypgspdswv
//
LOCUS       NP_853556                319 aa            linear   PRI 21-NOV-2025
DEFINITION  replication factor C subunit 5 isoform 2 [Homo sapiens].
ACCESSION   NP_853556 XP_001132724
VERSION     NP_853556.2
DBSOURCE    REFSEQ: accession NM_181578.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Wang,F., He,Q., Yao,N.Y., O'Donnell,M.E. and Li,H.
  TITLE     The human ATAD5 has evolved unique structural elements to function
            exclusively as a PCNA unloader
  JOURNAL   Nat Struct Mol Biol 31 (11), 1680-1691 (2024)
   PUBMED   38871854
REFERENCE   3  (residues 1 to 319)
  AUTHORS   He,Q., Wang,F., O'Donnell,M.E. and Li,H.
  TITLE     Cryo-EM reveals a nearly complete PCNA loading process and unique
            features of the human alternative clamp loader CTF18-RFC
  JOURNAL   Proc Natl Acad Sci U S A 121 (18), e2319727121 (2024)
   PUBMED   38669181
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Yao,H., Zhou,X., Zhou,A., Chen,J., Chen,G., Shi,X., Shi,B., Tai,Q.,
            Mi,X., Zhou,G., Wang,S., Sun,J., Yang,X., Yang,Y., Cao,H., Zhou,D.,
            Sun,L., Yao,Y. and He,S.
  TITLE     RFC5, regulated by circ_0038985/miR-3614-5p, functions as an
            oncogene in the progression of colorectal cancer
  JOURNAL   Mol Carcinog 62 (6), 771-785 (2023)
   PUBMED   36988339
  REMARK    GeneRIF: RFC5, regulated by circ_0038985/miR-3614-5p, functions as
            an oncogene in the progression of colorectal cancer.
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Li,W.J., Wu,D.W., Zhou,Y.F., Zhang,C.W. and Liao,X.W.
  TITLE     Prognostic biomarker replication factor C subunit 5 and its
            correlation with immune infiltrates in acute myeloid leukemia
  JOURNAL   Hematology 27 (1), 555-564 (2022)
   PUBMED   35544695
  REMARK    GeneRIF: Prognostic biomarker replication factor C subunit 5 and
            its correlation with immune infiltrates in acute myeloid leukemia.
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Wood,R.D. and Shivji,M.K.
  TITLE     Which DNA polymerases are used for DNA-repair in eukaryotes?
  JOURNAL   Carcinogenesis 18 (4), 605-610 (1997)
   PUBMED   9111189
  REMARK    Review article
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Mossi,R., Jonsson,Z.O., Allen,B.L., Hardin,S.H. and Hubscher,U.
  TITLE     Replication factor C interacts with the C-terminal side of
            proliferating cell nuclear antigen
  JOURNAL   J Biol Chem 272 (3), 1769-1776 (1997)
   PUBMED   8999859
REFERENCE   8  (residues 1 to 319)
  AUTHORS   Uhlmann,F., Cai,J., Flores-Rozas,H., Dean,F.B., Finkelstein,J.,
            O'Donnell,M. and Hurwitz,J.
  TITLE     In vitro reconstitution of human replication factor C from its five
            subunits
  JOURNAL   Proc Natl Acad Sci U S A 93 (13), 6521-6526 (1996)
   PUBMED   8692848
REFERENCE   9  (residues 1 to 319)
  AUTHORS   Okumura,K., Nogami,M., Taguchi,H., Dean,F.B., Chen,M., Pan,Z.Q.,
            Hurwitz,J., Shiratori,A., Murakami,Y., Ozawa,K. et al.
  TITLE     Assignment of the 36.5-kDa (RFC5), 37-kDa (RFC4), 38-kDa (RFC3),
            and 40-kDa (RFC2) subunit genes of human replication factor C to
            chromosome bands 12q24.2-q24.3, 3q27, 13q12.3-q13, and 7q11.23
  JOURNAL   Genomics 25 (1), 274-278 (1995)
   PUBMED   7774928
REFERENCE   10 (residues 1 to 319)
  AUTHORS   O'Donnell,M., Onrust,R., Dean,F.B., Chen,M. and Hurwitz,J.
  TITLE     Homology in accessory proteins of replicative polymerases--E. coli
            to humans
  JOURNAL   Nucleic Acids Res 21 (1), 1-3 (1993)
   PUBMED   8441605
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU121576.1, AK094575.1,
            AC131159.5 and BC001866.1.
            
            On Jul 18, 2008 this sequence version replaced NP_853556.1.
            
            Summary: This gene encodes the smallest subunit of the replication
            factor C complex, which consists of five distinct subunits (140,
            40, 38, 37, and 36 kDa) and is required for DNA replication. This
            subunit interacts with the C-terminal region of proliferating cell
            nuclear antigen and is required to open and load proliferating cell
            nuclear antigen onto DNA during S phase. It is a member of the AAA+
            (ATPases associated with various cellular activities) ATPase family
            and forms a core complex with the 38 and 40 kDa subunits that
            possesses DNA-dependent ATPase activity. A related pseudogene has
            been identified on chromosome 9. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Nov 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and 5'
            coding region, and uses an alternate start codon, compared to
            variant 1. The resulting isoform (2) has a distinct and shorter
            N-terminus, compared to isoform 1. Variants 2 and 3 encode the same
            isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK094575.1, SRR18074968.1864670.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.23"
     Protein         1..319
                     /product="replication factor C subunit 5 isoform 2"
                     /note="RFC, 36.5 kD subunit; A1 36 kDa subunit;
                     replication factor C, 36-kDa subunit; replication factor C
                     (activator 1) 5, 36.5kDa; RF-C 36 kDa subunit"
                     /calculated_mol_wt=35974
     Region          2..308
                     /region_name="rfc"
                     /note="replication factor C small subunit; Reviewed;
                     PRK00440"
                     /db_xref="CDD:234763"
     CDS             1..319
                     /gene="RFC5"
                     /gene_synonym="RFC36"
                     /coded_by="NM_181578.5:553..1512"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS41843.2"
                     /db_xref="GeneID:5985"
                     /db_xref="HGNC:HGNC:9973"
                     /db_xref="MIM:600407"
ORIGIN      
        1 mvekyrpqtl ndlishqdil stiqkfined rlphlllygp pgtgktstil acakqlykdk
       61 efgsmvleln asddrgidii rgpilsfast rtifkkgfkl vildeadamt qdaqnalrrv
      121 iekftentrf clicnylski ipalqsrctr frfgpltpel mvprlehvve eekvdisedg
      181 mkalvtlssg dmrralnilq stnmafgkvt eetvytctgh plksdianil dwmlnqdftt
      241 ayrnitelkt lkglalhdil teihlfvhrv dfpssvrihl ltkmadieyr lsvgtnekiq
      301 lssliaafqv trdlivaea
//
LOCUS       NP_001229787             339 aa            linear   PRI 21-NOV-2025
DEFINITION  cAMP-dependent protein kinase catalytic subunit beta isoform 5
            [Homo sapiens].
ACCESSION   NP_001229787
VERSION     NP_001229787.1
DBSOURCE    REFSEQ: accession NM_001242858.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Tanaka,M., Takeshita,K., Kunita,A., Hasegawa,K. and Ushiku,T.
  TITLE     PRKACA/PRKACB Fusions in Pancreatobiliary Intraductal Oncocytic
            Papillary Neoplasms Including Those With Atypical Morphology: An
            Analysis of 22 Cases Expanding Morphologic Spectrum
  JOURNAL   Am J Surg Pathol 48 (8), 1032-1040 (2024)
   PUBMED   38841868
  REMARK    GeneRIF: PRKACA/PRKACB Fusions in Pancreatobiliary Intraductal
            Oncocytic Papillary Neoplasms Including Those With Atypical
            Morphology: An Analysis of 22 Cases Expanding Morphologic Spectrum.
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Pei,W., Yin,W., Yu,T., Zhang,X., Zhang,Q., Yang,X., Shi,C., Shen,W.
            and Liu,G.
  TITLE     Dual-Specificity Phosphatase 4 Promotes Malignant Features in
            Colorectal Cancer Through Cyclic-AMP Response Element Binding
            Protein/Protein Kinase CAMP-Activated Catalytic Subunit Beta
            Activation
  JOURNAL   Dig Dis Sci 69 (8), 2856-2874 (2024)
   PUBMED   38824257
  REMARK    GeneRIF: Dual-Specificity Phosphatase 4 Promotes Malignant Features
            in Colorectal Cancer Through Cyclic-AMP Response Element Binding
            Protein/Protein Kinase CAMP-Activated Catalytic Subunit Beta
            Activation.
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Itoh,T., Omori,Y., Seino,M., Hirose,K., Date,F., Ono,Y.,
            Mizukami,Y., Aoki,S., Ishida,M., Mizuma,M., Morikawa,T.,
            Higuchi,R., Honda,G., Okamura,Y., Kinoshita,K., Unno,M. and
            Furukawa,T.
  TITLE     Gene Rearrangement and Expression of PRKACA and PRKACB Govern
            Morphobiology of Pancreatobiliary Oncocytic Neoplasms
  JOURNAL   Mod Pathol 37 (1), 100358 (2024)
   PUBMED   37871652
  REMARK    GeneRIF: Gene Rearrangement and Expression of PRKACA and PRKACB
            Govern Morphobiology of Pancreatobiliary Oncocytic Neoplasms.
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Maimaitiaili,Y., Fukumura,Y., Hirabayashi,K., Kinowaki,Y.,
            Naito,Y., Saito,A., Rong,L., Nakahodo,J. and Yao,T.
  TITLE     Investigation of -PRKACA/-PRKACB fusion genes in oncocytic tumors
            of the pancreatobiliary and other systems
  JOURNAL   Virchows Arch 481 (6), 865-876 (2022)
   PUBMED   36152045
  REMARK    GeneRIF: Investigation of -PRKACA/-PRKACB fusion genes in oncocytic
            tumors of the pancreatobiliary and other systems.
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Orstavik,S., Reinton,N., Frengen,E., Langeland,B.T., Jahnsen,T. and
            Skalhegg,B.S.
  TITLE     Identification of novel splice variants of the human catalytic
            subunit Cbeta of cAMP-dependent protein kinase
  JOURNAL   Eur J Biochem 268 (19), 5066-5073 (2001)
   PUBMED   11589697
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Scarpetta,M.A. and Uhler,M.D.
  TITLE     Evidence for two additional isoforms of the endogenous protein
            kinase inhibitor of cAMP-dependent protein kinase in mouse
  JOURNAL   J Biol Chem 268 (15), 10927-10931 (1993)
   PUBMED   7684369
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Da Silva,J.D., Tkachenko,N. and Soares,A.R.
  TITLE     Ellis-van Creveld Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37903214
REFERENCE   8  (residues 1 to 339)
  AUTHORS   Simard,J., Berube,D., Sandberg,M., Grzeschik,K.H., Gagne,R.,
            Hansson,V. and Jahnsen,T.
  TITLE     Assignment of the gene encoding the catalytic subunit C beta of
            cAMP-dependent protein kinase to the p36 band on chromosome 1
  JOURNAL   Hum Genet 88 (6), 653-657 (1992)
   PUBMED   1551670
REFERENCE   9  (residues 1 to 339)
  AUTHORS   Beebe,S.J., Oyen,O., Sandberg,M., Froysa,A., Hansson,V. and
            Jahnsen,T.
  TITLE     Molecular cloning of a tissue-specific protein kinase (C gamma)
            from human testis--representing a third isoform for the catalytic
            subunit of cAMP-dependent protein kinase
  JOURNAL   Mol Endocrinol 4 (3), 465-475 (1990)
   PUBMED   2342480
REFERENCE   10 (residues 1 to 339)
  AUTHORS   Taylor,S.S., Buechler,J.A. and Yonemoto,W.
  TITLE     cAMP-dependent protein kinase: framework for a diverse family of
            regulatory enzymes
  JOURNAL   Annu Rev Biochem 59, 971-1005 (1990)
   PUBMED   2165385
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC322547.1, AK304375.1,
            BX641026.1 and AL450063.14.
            
            Summary: The protein encoded by this gene is a member of the
            serine/threonine protein kinase family. The encoded protein is a
            catalytic subunit of cAMP (cyclic AMP)-dependent protein kinase,
            which mediates signalling though cAMP. cAMP signaling is important
            to a number of processes, including cell proliferaton and
            differentiation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2014].
            
            Transcript Variant: This variant (5) differs in the 5' exon
            structure, compared to variant 1. The encoded isoform (5, also
            known as Cbeta3) has a distinct N-terminus and is shorter than
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1861663.1,
                                           SRR14038195.560656.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.1"
     Protein         1..339
                     /product="cAMP-dependent protein kinase catalytic subunit
                     beta isoform 5"
                     /EC_number="2.7.11.11"
                     /note="protein kinase A catalytic subunit beta; protein
                     kinase, cAMP-dependent, catalytic, beta; protein kinase,
                     cAMP-dependent, beta catalytic subunit"
                     /calculated_mol_wt=39346
     Region          30..319
                     /region_name="STKc_PKA"
                     /note="Catalytic subunit of the Serine/Threonine Kinase,
                     cAMP-dependent protein kinase; cd14209"
                     /db_xref="CDD:271111"
     Site            order(38..44,46,59,61,93,109..112,116,155,157,159..160,
                     162,172..173,316)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271111"
     Site            order(39..44,46,59,61,71,93,109..110,112,116,118,122,155,
                     157..160,162,172..173,176,187,189..192,219,223..225,
                     228..230,232,235,316,319)
                     /site_type="active"
                     /db_xref="CDD:271111"
     Site            order(40,42..43,71..73,116,118,122,155,157..159,176,
                     187..192,219,223..225,228..230,232,235..236,319)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271111"
     Site            order(42,72..73,75..76,116,118,122,157..159,176,183,
                     185..190,193,200..202,219,232..233,236..237,240,319)
                     /site_type="other"
                     /note="regulatory subunit interface [polypeptide binding]"
                     /db_xref="CDD:271111"
     Site            172..192
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271111"
     CDS             1..339
                     /gene="PRKACB"
                     /gene_synonym="CAFD2; PKA C-beta; PKACB"
                     /coded_by="NM_001242858.3:109..1128"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS72813.1"
                     /db_xref="GeneID:5567"
                     /db_xref="HGNC:HGNC:9381"
                     /db_xref="MIM:176892"
ORIGIN      
        1 mgllkeflak akedflkkwe nptqnnagle dferkktlgt gsfgrvmlvk hkateqyyam
       61 kildkqkvvk lkqiehtlne krilqavnfp flvrleyafk dnsnlymvme yvpggemfsh
      121 lrrigrfsep harfyaaqiv ltfeylhsld liyrdlkpen llidhqgyiq vtdfgfakrv
      181 kgrtwtlcgt peylapeiil skgynkavdw walgvliyem aagyppffad qpiqiyekiv
      241 sgkvrfpshf ssdlkdllrn llqvdltkrf gnlkngvsdi kthkwfattd wiaiyqrkve
      301 apfipkfrgs gdtsnfddye eedirvsite kcakefgef
//
LOCUS       NP_001244126             702 aa            linear   PRI 21-NOV-2025
DEFINITION  cullin-3 isoform 2 [Homo sapiens].
ACCESSION   NP_001244126
VERSION     NP_001244126.1
DBSOURCE    REFSEQ: accession NM_001257197.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Cacioppo,R., Gillis,A., Shlamovitz,I., Zeller,A., Castiblanco,D.,
            Crisp,A., Haworth,B., Arabiotorre,A., Abyaneh,P., Bao,Y.,
            Sale,J.E., Berry,S. and Tufegdzic Vidakovic,A.
  TITLE     CRL3ARMC5 ubiquitin ligase and Integrator phosphatase form parallel
            mechanisms to control early stages of RNA Pol II transcription
  JOURNAL   Mol Cell 84 (24), 4808-4823 (2024)
   PUBMED   39667934
REFERENCE   3  (residues 1 to 702)
  AUTHORS   Blears,D., Lou,J., Fong,N., Mitter,R., Sheridan,R.M., He,D.,
            Dirac-Svejstrup,A.B., Bentley,D. and Svejstrup,J.Q.
  TITLE     Redundant pathways for removal of defective RNA polymerase II
            complexes at a promoter-proximal pause checkpoint
  JOURNAL   Mol Cell 84 (24), 4790-4807 (2024)
   PUBMED   39504960
REFERENCE   4  (residues 1 to 702)
  AUTHORS   Pratummanee,K., Kerdkumthong,K., Roytrakul,S., Tantimetta,P.,
            Runsaeng,P., Saeheng,S. and Obchoei,S.
  TITLE     Knockdown of cullin 3 inhibits progressive phenotypes and increases
            chemosensitivity in cholangiocarcinoma cells
  JOURNAL   Mol Med Rep 30 (5) (2024)
   PUBMED   39239747
  REMARK    GeneRIF: Knockdown of cullin 3 inhibits progressive phenotypes and
            increases chemosensitivity in cholangiocarcinoma cells.
REFERENCE   5  (residues 1 to 702)
  AUTHORS   Boyden,L.M., Choi,M., Choate,K.A., Nelson-Williams,C.J., Farhi,A.,
            Toka,H.R., Tikhonova,I.R., Bjornson,R., Mane,S.M., Colussi,G.,
            Lebel,M., Gordon,R.D., Semmekrot,B.A., Poujol,A., Valimaki,M.J., De
            Ferrari,M.E., Sanjad,S.A., Gutkin,M., Karet,F.E., Tucci,J.R.,
            Stockigt,J.R., Keppler-Noreuil,K.M., Porter,C.C., Anand,S.K.,
            Whiteford,M.L., Davis,I.D., Dewar,S.B., Bettinelli,A.,
            Fadrowski,J.J., Belsha,C.W., Hunley,T.E., Nelson,R.D.,
            Trachtman,H., Cole,T.R., Pinsk,M., Bockenhauer,D., Shenoy,M.,
            Vaidyanathan,P., Foreman,J.W., Rasoulpour,M., Thameem,F.,
            Al-Shahrouri,H.Z., Radhakrishnan,J., Gharavi,A.G., Goilav,B. and
            Lifton,R.P.
  TITLE     Mutations in kelch-like 3 and cullin 3 cause hypertension and
            electrolyte abnormalities
  JOURNAL   Nature 482 (7383), 98-102 (2012)
   PUBMED   22266938
  REMARK    GeneRIF: fundamental role for KLHL3 and CUL3 in blood pressure,
            K(+) and pH homeostasis
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 702)
  AUTHORS   Kershnar,E., Wu,S.Y. and Chiang,C.M.
  TITLE     Immunoaffinity purification and functional characterization of
            human transcription factor IIH and RNA polymerase II from clonal
            cell lines that conditionally express epitope-tagged subunits of
            the multiprotein complexes
  JOURNAL   J Biol Chem 273 (51), 34444-34453 (1998)
   PUBMED   9852112
REFERENCE   7  (residues 1 to 702)
  AUTHORS   Du,M., Sansores-Garcia,L., Zu,Z. and Wu,K.K.
  TITLE     Cloning and expression analysis of a novel salicylate suppressible
            gene, Hs-CUL-3, a member of cullin/Cdc53 family
  JOURNAL   J Biol Chem 273 (38), 24289-24292 (1998)
   PUBMED   9733711
REFERENCE   8  (residues 1 to 702)
  AUTHORS   Michel,J.J. and Xiong,Y.
  TITLE     Human CUL-1, but not other cullin family members, selectively
            interacts with SKP1 to form a complex with SKP2 and cyclin A
  JOURNAL   Cell Growth Differ 9 (6), 435-449 (1998)
   PUBMED   9663463
REFERENCE   9  (residues 1 to 702)
  AUTHORS   Kipreos,E.T., Lander,L.E., Wing,J.P., He,W.W. and Hedgecock,E.M.
  TITLE     cul-1 is required for cell cycle exit in C. elegans and identifies
            a novel gene family
  JOURNAL   Cell 85 (6), 829-839 (1996)
   PUBMED   8681378
REFERENCE   10 (residues 1 to 702)
  AUTHORS   Ellison,D.H.
  TITLE     Pseudohypoaldosteronism Type II
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22073419
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ688156.1, AK299644.1,
            AB014517.2 and AC073052.5.
            
            Summary: This gene encodes a member of the cullin protein family.
            The encoded protein plays a critical role in the polyubiquitination
            and subsequent degradation of specific protein substrates as the
            core component and scaffold protein of an E3 ubiquitin ligase
            complex. Complexes including the encoded protein may also play a
            role in late endosome maturation. Mutations in this gene are a
            cause of type 2E pseudohypoaldosteronism. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene. [provided by RefSeq, Mar 2012].
            
            Transcript Variant: This variant (2) lacks an exon in the 5' coding
            region, but maintains the reading frame, comapred to variant 1. The
            encoded isoform (2) is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK299644.1, SRR14372079.3025189.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q36.2"
     Protein         1..702
                     /product="cullin-3 isoform 2"
                     /calculated_mol_wt=80962
     Region          32..599
                     /region_name="Cullin"
                     /note="Cullin family; pfam00888"
                     /db_xref="CDD:459983"
     Region          632..694
                     /region_name="Cullin_Nedd8"
                     /note="Cullin protein neddylation domain; pfam10557"
                     /db_xref="CDD:463146"
     CDS             1..702
                     /gene="CUL3"
                     /gene_synonym="CUL-3; NEDAUS; PHA2E"
                     /coded_by="NM_001257197.2:355..2463"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58751.1"
                     /db_xref="GeneID:8452"
                     /db_xref="HGNC:HGNC:2553"
                     /db_xref="MIM:603136"
ORIGIN      
        1 msnlskgtgs rkdtkmrira fpvredvlns lnnnflqtln qawndhqtam vmirdilmym
       61 drvyvqqnnv envynlglii frdqvvrygc irdhlrqtll dmiarerkge vvdrgairna
      121 cqmlmilgle grsvyeedfe apflemsaef fqmesqkfla ensasvyikk vearineeie
      181 rvmhcldkst eepivkvver eliskhmkti vemensglvh mlkngktedl gcmyklfsrv
      241 pnglktmcec mssylreqgk alvseegegk npvdyiqgll dlksrfdrfl lesfnndrlf
      301 kqtiagdfey flnlnsrspe ylslfiddkl kkgvkglteq evetildkam vlfrfmqekd
      361 vferyykqhl arrlltnksv sddseknmis klktecgcqf tsklegmfrd msisnttmde
      421 frqhlqatgv slggvdltvr vlttgywptq satpkcnipp aprhafeifr rfylakhsgr
      481 qltlqhhmgs adlnatfygp vkkedgsevg vggaqvtgsn trkhilqvst fqmtilmlfn
      541 nrekytfeei qqetdipere lvralqslac gkptqrvltk epkskeieng hiftvndqft
      601 sklhrvkiqt vaakqgesdp erketrqkvd ddrkheieaa ivrimksrkk mqhnvlvaev
      661 tqqlkarflp spvvikkrie gliereylar tpedrkvyty va
//
LOCUS       NP_002122                 96 aa            linear   PRI 21-NOV-2025
DEFINITION  high mobility group protein HMG-I/HMG-Y isoform b [Homo sapiens].
ACCESSION   NP_002122
VERSION     NP_002122.1
DBSOURCE    REFSEQ: accession NM_002131.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Olan,I., Ando-Kuri,M., Parry,A.J., Handa,T., Schoenfelder,S.,
            Fraser,P., Ohkawa,Y., Kimura,H., Narita,M. and Narita,M.
  TITLE     HMGA1 orchestrates chromatin compartmentalization and sequesters
            genes into 3D networks coordinating senescence heterogeneity
  JOURNAL   Nat Commun 15 (1), 6891 (2024)
   PUBMED   39134516
  REMARK    GeneRIF: HMGA1 orchestrates chromatin compartmentalization and
            sequesters genes into 3D networks coordinating senescence
            heterogeneity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 96)
  AUTHORS   Li,K.J., Hong,Y., Yu,Y.Z., Xie,Z., Lv,D.J., Wang,C., Xie,T.,
            Chen,H., Chen,Z.S., Zeng,J. and Zhao,S.C.
  TITLE     NAT10 Promotes Prostate Cancer Growth and Metastasis by Acetylating
            mRNAs of HMGA1 and KRT8
  JOURNAL   Adv Sci (Weinh) 11 (32), e2310131 (2024)
   PUBMED   38922788
  REMARK    GeneRIF: NAT10 Promotes Prostate Cancer Growth and Metastasis by
            Acetylating mRNAs of HMGA1 and KRT8.
REFERENCE   4  (residues 1 to 96)
  AUTHORS   Wang,L., Zhang,J., Xia,M., Liu,C., Zu,X. and Zhong,J.
  TITLE     High Mobility Group A1 (HMGA1): Structure, Biological Function, and
            Therapeutic Potential
  JOURNAL   Int J Biol Sci 18 (11), 4414-4431 (2022)
   PUBMED   35864955
  REMARK    GeneRIF: High Mobility Group A1 (HMGA1): Structure, Biological
            Function, and Therapeutic Potential.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 96)
  AUTHORS   Sumter,T.F., Xian,L., Huso,T., Koo,M., Chang,Y.T., Almasri,T.N.,
            Chia,L., Inglis,C., Reid,D. and Resar,L.M.
  TITLE     The High Mobility Group A1 (HMGA1) Transcriptome in Cancer and
            Development
  JOURNAL   Curr Mol Med 16 (4), 353-393 (2016)
   PUBMED   26980699
  REMARK    Review article
REFERENCE   6  (residues 1 to 96)
  AUTHORS   Friedmann,M., Holth,L.T., Zoghbi,H.Y. and Reeves,R.
  TITLE     Organization, inducible-expression and chromosome localization of
            the human HMG-I(Y) nonhistone protein gene
  JOURNAL   Nucleic Acids Res 21 (18), 4259-4267 (1993)
   PUBMED   8414980
REFERENCE   7  (residues 1 to 96)
  AUTHORS   Nissen,M.S., Langan,T.A. and Reeves,R.
  TITLE     Phosphorylation by cdc2 kinase modulates DNA binding activity of
            high mobility group I nonhistone chromatin protein
  JOURNAL   J Biol Chem 266 (30), 19945-19952 (1991)
   PUBMED   1939057
REFERENCE   8  (residues 1 to 96)
  AUTHORS   Reeves,R. and Nissen,M.S.
  TITLE     The A.T-DNA-binding domain of mammalian high mobility group I
            chromosomal proteins. A novel peptide motif for recognizing DNA
            structure
  JOURNAL   J Biol Chem 265 (15), 8573-8582 (1990)
   PUBMED   1692833
REFERENCE   9  (residues 1 to 96)
  AUTHORS   Eckner,R. and Birnstiel,M.L.
  TITLE     Cloning of cDNAs coding for human HMG I and HMG Y proteins: both
            are capable of binding to the octamer sequence motif
  JOURNAL   Nucleic Acids Res 17 (15), 5947-5959 (1989)
   PUBMED   2505228
REFERENCE   10 (residues 1 to 96)
  AUTHORS   Johnson,K.R., Lehn,D.A. and Reeves,R.
  TITLE     Alternative processing of mRNAs encoding mammalian chromosomal
            high-mobility-group proteins HMG-I and HMG-Y
  JOURNAL   Mol Cell Biol 9 (5), 2114-2123 (1989)
   PUBMED   2701943
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA049639.1, BC004924.2,
            AL354740.29 and BC008832.2.
            
            Summary: This gene encodes a chromatin-associated protein involved
            in the regulation of gene transcription, integration of
            retroviruses into chromosomes, and the metastatic progression of
            cancer cells. The encoded protein preferentially binds to the minor
            groove of AT-rich regions in double-stranded DNA. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. Pseudogenes of this gene have been identified on
            multiple chromosomes. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site compared to variant 1, resulting in a shorter isoform
            (b, also called HMG-Y) than isoform a. Variants 2, 4, 5, 7, and 8
            encode the same isoform (b).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.592650.1,
                                           SRR3476690.394917.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..96
                     /product="high mobility group protein HMG-I/HMG-Y isoform
                     b"
                     /note="nonhistone chromosomal high-mobility group protein
                     HMG-I/HMG-Y; high mobility group protein HMG-I/HMG-Y; high
                     mobility group protein R; high mobility group protein A1"
                     /calculated_mol_wt=10548
     CDS             1..96
                     /gene="HMGA1"
                     /gene_synonym="HMG-R; HMGA1A; HMGIY"
                     /coded_by="NM_002131.4:250..540"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4788.1"
                     /db_xref="GeneID:3159"
                     /db_xref="HGNC:HGNC:5010"
                     /db_xref="MIM:600701"
ORIGIN      
        1 msessskssq plaskqekdg tekrgrgrpr kqppkepsev ptpkrprgrp kgsknkgaak
       61 trkttttpgr kprgrpkkle keeeegisqe sseeeq
//
LOCUS       NP_001387144            1127 aa            linear   PRI 21-NOV-2025
DEFINITION  protein transport protein Sec31A isoform 26 [Homo sapiens].
ACCESSION   NP_001387144
VERSION     NP_001387144.1
DBSOURCE    REFSEQ: accession NM_001400215.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1127)
  AUTHORS   Tobias,E.S., Lucas-Herald,A.K., Sagar,D., Montezano,A.C.,
            Rios,F.J., De Lucca Camargo,L., Hamilton,G., Gazdagh,G.,
            Diver,L.A., Williams,N., Herzyk,P., Touyz,R.M., Greenfield,A.,
            McGowan,R. and Ahmed,S.F.
  TITLE     SEC31A may be associated with pituitary hormone deficiency and
            gonadal dysgenesis
  JOURNAL   Endocrine 84 (2), 345-349 (2024)
   PUBMED   38400880
  REMARK    GeneRIF: SEC31A may be associated with pituitary hormone deficiency
            and gonadal dysgenesis.
REFERENCE   2  (residues 1 to 1127)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1127)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1127)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1127)
  AUTHORS   Jin,L., Pahuja,K.B., Wickliffe,K.E., Gorur,A., Baumgartel,C.,
            Schekman,R. and Rape,M.
  TITLE     Ubiquitin-dependent regulation of COPII coat size and function
  JOURNAL   Nature 482 (7386), 495-500 (2012)
   PUBMED   22358839
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1127)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1127)
  AUTHORS   Kim,J.H., Hong,J.A., Pih,K.T. and Hwang,I.
  TITLE     Identification and isolation of differentially expressed genes in
            osmotically stressed human oral keratinocytes
  JOURNAL   Arch Oral Biol 46 (4), 335-341 (2001)
   PUBMED   11269867
REFERENCE   8  (residues 1 to 1127)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 1127)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   10 (residues 1 to 1127)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021105.13 and AC108469.5.
            
            Summary: The protein encoded by this gene shares similarity with
            the yeast Sec31 protein, and is a component of the outer layer of
            the coat protein complex II (COPII). The encoded protein is
            involved in vesicle budding from the endoplasmic reticulum (ER) and
            contains multiple WD repeats near the N-terminus and a proline-rich
            region in the C-terminal half. It associates with the protein
            encoded by the SEC13 homolog, nuclear pore and COPII coat complex
            component (SEC13), and is required for ER-Golgi transport.
            Monoubiquitylation of this protein by CUL3-KLHL12 was found to
            regulate the size of COPII coats to accommodate unusually shaped
            cargo. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.1176038.1,
                                           SRR14038197.2393602.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1127
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..1127
                     /product="protein transport protein Sec31A isoform 26"
                     /note="yeast Sec31p homolog; protein transport protein
                     Sec31A; web1-like protein; SEC31 homolog A, COPII coat
                     complex component; SEC31-related protein A; SEC31-like
                     protein 1; SEC31 homolog A, COPII coating complex
                     component"
                     /calculated_mol_wt=123007
     Region          <35..278
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(37,41,47..48,63,67,85,90,96..97,110,131,136,
                     142..143,155..156,177,181,190..191,204..205,223,228,
                     234..235,247..248,266,271,277..278)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          71..108
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          118..154
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          160..203
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          209..248
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          252..277
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <480..>603
                     /region_name="ACE1-Sec16-like"
                     /note="Ancestral coatomer element 1 (ACE1) of COPII coat
                     complex assembly protein Sec16; cl14807"
                     /db_xref="CDD:449359"
     Site            order(481..485,487,489,500,502,503..504,506..507,511,517,
                     525,537,540,565..566)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187750"
     Region          <707..>1005
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     CDS             1..1127
                     /gene="SEC31A"
                     /gene_synonym="ABP125; ABP130; HPBKS; HSPC275; HSPC334;
                     NEDSOSB; SEC31L1"
                     /coded_by="NM_001400215.1:109..3492"
                     /note="isoform 26 is encoded by transcript variant 49"
                     /db_xref="GeneID:22872"
                     /db_xref="HGNC:HGNC:17052"
                     /db_xref="MIM:610257"
ORIGIN      
        1 mepcpesphl psnryhkliw gpykmdskgd vsgvliagge ngniilydps kiiagdkevv
       61 iaqndkhtgp vraldvnifq tnlvasgane seiyiwdlnn fatpmtpgak tqppedisci
      121 awnrqvqhil asaspsgrat vwdlrknepi ikvsdhsnrm hcsglawhpd vatqmvlase
      181 ddrlpviqmw dlrfassplr vlenhargil aiawsmadpe lllscgkdak ilcsnpntge
      241 vlyelptntq wcfdiqwcpr npavlsaasf dgrisvysim ggstdglrqk qvdklsssfg
      301 nldpfgtgqp lpplqipqqt aqhsivlplk kppkwirrpv gasfsfggkl vtfenvrmps
      361 hqgaeqqqqq hhvfisqvvt ekeflsrsdq lqqavqsqgf inycqkkida sqtefeknvw
      421 sflkvnfedd srgkylellg yrkedlgkkh ikeekeesef lpssggtfni svsgdidgli
      481 tqalltgnfe savdlclhdn rmadaiilai aggqellart qkkyfaksqs kitrlitavv
      541 mknwkeives cdlknwreal aavltyakpd efsalcdllg trlenegdsl lqtqaclcyi
      601 cagnveklva cwtkaqdgsh plslqdliek vvilrkavql tqamdtstvg vllaakmsqy
      661 anllaaqgsi aaalaflpdn tnqpnimqlr drlcraqgep vaghespkip yekqqlpkgr
      721 pgpvaghhqm prvqtqqyyp hgenppppgf imhgnvnpna agqlptspgh mhtqvppypq
      781 pqpyqpaqpy pfgtggsamy rpqqpvappt snaypntpyi ssassytgqs qlyaaqhqas
      841 sptsspatsf ppppssgasf qhggpgapps ssayalppgt tgtlpaasel pasqrtgpqn
      901 gwndppalnr vpkkkkmpen fmppvpitsp imnplgdpqs qmlqqqpsap vplssqssfp
      961 qphlpggqpf hgvqqplgqt gmppsfskpn iegapgapig ntfqhvqslp tkkitkkpip
     1021 dehlilkttf edliqrclss atdpqtkrkl ddaskrlefl ydklreqtls ptitsglhni
     1081 arsietrnys egltmhthiv stsnfsetsa fmpvlkvvlt qanklgv
//
LOCUS       NP_001171593             422 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 1 isoform i [Homo sapiens].
ACCESSION   NP_001171593
VERSION     NP_001171593.1
DBSOURCE    REFSEQ: accession NM_001178122.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Petersen,M. and Dubielecka,P.
  TITLE     Adaptor protein Abelson interactor 1 in homeostasis and disease
  JOURNAL   Cell Commun Signal 22 (1), 468 (2024)
   PUBMED   39354505
  REMARK    GeneRIF: Adaptor protein Abelson interactor 1 in homeostasis and
            disease.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Jin,M., Xie,M., Liu,Y., Song,H., Zhang,M., Li,W., Li,X., Jia,N.,
            Dong,L., Lu,Q., Xue,F., Yan,L. and Yu,Q.
  TITLE     Circulating miR-30e-3p induces disruption of neurite development in
            SH-SY5Y cells by targeting ABI1, a novel biomarker for
            schizophrenia
  JOURNAL   J Psychiatr Res 174, 84-93 (2024)
   PUBMED   38626565
  REMARK    GeneRIF: Circulating miR-30e-3p induces disruption of neurite
            development in SH-SY5Y cells by targeting ABI1, a novel biomarker
            for schizophrenia.
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Lin,T., Guo,J., Peng,Y., Li,M., Liu,Y., Yu,X., Wu,N. and Yu,W.
  TITLE     Pan-cancer transcriptomic data of ABI1 transcript variants and
            molecular constitutive elements identifies novel cancer metastatic
            and prognostic biomarkers
  JOURNAL   Cancer Biomark 39 (1), 49-62 (2024)
   PUBMED   37545215
  REMARK    GeneRIF: Pan-cancer transcriptomic data of ABI1 transcript variants
            and molecular constitutive elements identifies novel cancer
            metastatic and prognostic biomarkers.
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Fan,P.D. and Goff,S.P.
  TITLE     Abl interactor 1 binds to sos and inhibits epidermal growth factor-
            and v-Abl-induced activation of extracellular signal-regulated
            kinases
  JOURNAL   Mol Cell Biol 20 (20), 7591-7601 (2000)
   PUBMED   11003655
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Scita,G., Nordstrom,J., Carbone,R., Tenca,P., Giardina,G.,
            Gutkind,S., Bjarnegard,M., Betsholtz,C. and Di Fiore,P.P.
  TITLE     EPS8 and E3B1 transduce signals from Ras to Rac
  JOURNAL   Nature 401 (6750), 290-293 (1999)
   PUBMED   10499589
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Taki,T., Shibuya,N., Taniwaki,M., Hanada,R., Morishita,K.,
            Bessho,F., Yanagisawa,M. and Hayashi,Y.
  TITLE     ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL
            gene in acute myeloid leukemia with t(10;11)(p11.2;q23)
  JOURNAL   Blood 92 (4), 1125-1130 (1998)
   PUBMED   9694699
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Ziemnicka-Kotula,D., Xu,J., Gu,H., Potempska,A., Kim,K.S.,
            Jenkins,E.C., Trenkner,E. and Kotula,L.
  TITLE     Identification of a candidate human spectrin Src homology 3
            domain-binding protein suggests a general mechanism of association
            of tyrosine kinases with the spectrin-based membrane skeleton
  JOURNAL   J Biol Chem 273 (22), 13681-13692 (1998)
   PUBMED   9593709
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Biesova,Z., Piccoli,C. and Wong,W.T.
  TITLE     Isolation and characterization of e3B1, an eps8 binding protein
            that regulates cell growth
  JOURNAL   Oncogene 14 (2), 233-241 (1997)
   PUBMED   9010225
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB040151.1, FJ380057.1 and
            AL390961.17.
            
            Summary: This gene encodes a member of the Abelson-interactor
            family of adaptor proteins. These proteins facilitate signal
            transduction as components of several multiprotein complexes, and
            regulate actin polymerization and cytoskeletal remodeling through
            interactions with Abelson tyrosine kinases. The encoded protein
            plays a role in macropinocytosis as a component of the WAVE2
            complex, and also forms a complex with EPS8 and SOS1 that mediates
            signal transduction from Ras to Rac. This gene may play a role in
            the progression of several malignancies including melanoma, colon
            cancer and breast cancer, and a t(10;11) chromosomal translocation
            involving this gene and the MLL gene has been associated with acute
            myeloid leukemia. Alternatively spliced transcript variants
            encoding multiple isoforms have been observed for this gene, and a
            pseudogene of this gene is located on the long arm of chromosome
            14. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (9) lacks two alternate in-frame
            coding exons, compared to variant 1. The resulting protein (isoform
            i) has the same N- and C-termini but is shorter when it is compared
            to isoform a. This isoform has also been called 'variant 41'.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.223912.1, FJ380057.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.1"
     Protein         1..422
                     /product="abl interactor 1 isoform i"
                     /note="nap1 binding protein; interactor protein AblBP4;
                     Abl-interactor protein 1 long; Abelson interactor 1;
                     abl-binding protein 4; eps8 SH3 domain-binding protein;
                     spectrin SH3 domain-binding protein 1"
                     /calculated_mol_wt=46255
     Region          93..156
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          364..422
                     /region_name="SH3_Abi1"
                     /note="Src homology 3 domain of Abl Interactor 1; cd11971"
                     /db_xref="CDD:212904"
     Site            order(369,371,374,378,396..397,410,412..413)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212904"
     CDS             1..422
                     /gene="ABI1"
                     /gene_synonym="ABI-1; ABLBP4; E3B1; NAP1BP; SSH3BP;
                     SSH3BP1"
                     /coded_by="NM_001178122.2:96..1364"
                     /note="isoform i is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS73078.1"
                     /db_xref="GeneID:10006"
                     /db_xref="HGNC:HGNC:11320"
                     /db_xref="MIM:603050"
ORIGIN      
        1 maelqmllee eipsgkrali esyqnltrva dycennyiqa tdkrkaleet kayttqslas
       61 vayqinalan nvlqlldiqa sqlrrmessi nhisqtvdih kekvarreig ilttnkntsr
      121 thkiiapanm erpvryirkp idytvlddvg hgvkwlkakh gnnqpartgt lsrtnpptqk
      181 ppsppmsgrg tlgrntpykt lepvkpptvp ndymtsparl gsqhspgrta slnqrprths
      241 gssggsgsre nsgsssigip iavptpsppt igpvsiappp ppmpqltpqi pltgfvarvq
      301 eniadsptpp pppppddipm fddspppppp ppvdyedeea avvqyndpya dgdpawapkn
      361 yiekvvaiyd ytkdkddels fmegaiiyvi kknddgwyeg vcnrvtglfp gnyvesimhy
      421 td
//
LOCUS       NP_001373887             597 aa            linear   PRI 21-NOV-2025
DEFINITION  solute carrier organic anion transporter family member 1A2 isoform
            5 [Homo sapiens].
ACCESSION   NP_001373887
VERSION     NP_001373887.1
DBSOURCE    REFSEQ: accession NM_001386958.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Flogel,S., Tust,M., Boussettaoui,S., Fischer,D. and Grundemann,D.
  TITLE     Enhancing transporter activity in heterologous expression systems
            with SAHA: a 2500-times more potent and odorless alternative to
            butyrate
  JOURNAL   FEBS Open Bio 15 (6), 906-913 (2025)
   PUBMED   40052353
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Kataoka,H., Akiyoshi,T., Uchida,Y., Imaoka,A., Terasaki,T. and
            Ohtani,H.
  TITLE     The Effects of N-Glycosylation on the Expression and Transport
            Activity of OATP1A2 and OATP2B1
  JOURNAL   J Pharm Sci 113 (5), 1376-1384 (2024)
   PUBMED   38432624
  REMARK    GeneRIF: The Effects of N-Glycosylation on the Expression and
            Transport Activity of OATP1A2 and OATP2B1.
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Han,H., Akiyoshi,T., Morita,T., Kataoka,H., Katayama,K., Yajima,K.,
            Imaoka,A. and Ohtani,H.
  TITLE     Comparison of the transport kinetics of fexofenadine and its pH
            dependency among OATP1A2 genetic variants
  JOURNAL   Drug Metab Pharmacokinet 47, 100470 (2022)
   PUBMED   36116173
  REMARK    GeneRIF: Comparison of the transport kinetics of fexofenadine and
            its pH dependency among OATP1A2 genetic variants.
REFERENCE   4  (residues 1 to 597)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 597)
  AUTHORS   Hau,R.K., Klein,R.R., Wright,S.H. and Cherrington,N.J.
  TITLE     Localization of Xenobiotic Transporters Expressed at the Human
            Blood-Testis Barrier
  JOURNAL   Drug Metab Dispos 50 (6), 770-780 (2022)
   PUBMED   35307651
REFERENCE   6  (residues 1 to 597)
  AUTHORS   Kullak-Ublick,G.A., Fisch,T., Oswald,M., Hagenbuch,B., Meier,P.J.,
            Beuers,U. and Paumgartner,G.
  TITLE     Dehydroepiandrosterone sulfate (DHEAS): identification of a carrier
            protein in human liver and brain
  JOURNAL   FEBS Lett 424 (3), 173-176 (1998)
   PUBMED   9539145
REFERENCE   7  (residues 1 to 597)
  AUTHORS   Meier,P.J., Eckhardt,U., Schroeder,A., Hagenbuch,B. and Stieger,B.
  TITLE     Substrate specificity of sinusoidal bile acid and organic anion
            uptake systems in rat and human liver
  JOURNAL   Hepatology 26 (6), 1667-1677 (1997)
   PUBMED   9398014
  REMARK    Review article
REFERENCE   8  (residues 1 to 597)
  AUTHORS   Kullak-Ublick,G.A., Beuers,U., Fahney,C., Hagenbuch,B., Meier,P.J.
            and Paumgartner,G.
  TITLE     Identification and functional characterization of the promoter
            region of the human organic anion transporting polypeptide gene
  JOURNAL   Hepatology 26 (4), 991-997 (1997)
   PUBMED   9328325
REFERENCE   9  (residues 1 to 597)
  AUTHORS   Kullak-Ublick,G.A., Beuers,U., Meier,P.J., Domdey,H. and
            Paumgartner,G.
  TITLE     Assignment of the human organic anion transporting polypeptide
            (OATP) gene to chromosome 12p12 by fluorescence in situ
            hybridization
  JOURNAL   J Hepatol 25 (6), 985-987 (1996)
   PUBMED   9007731
REFERENCE   10 (residues 1 to 597)
  AUTHORS   Kullak-Ublick,G.A., Hagenbuch,B., Stieger,B., Schteingart,C.D.,
            Hofmann,A.F., Wolkoff,A.W. and Meier,P.J.
  TITLE     Molecular and functional characterization of an organic anion
            transporting polypeptide cloned from human liver
  JOURNAL   Gastroenterology 109 (4), 1274-1282 (1995)
   PUBMED   7557095
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022224.22.
            
            Summary: This gene encodes a sodium-independent transporter which
            mediates cellular uptake of organic ions in the liver. Its
            substrates include bile acids, bromosulphophthalein, and some
            steroidal compounds. The protein is a member of the SLC21A family
            of solute carriers. Alternative splicing of this gene results in
            multiple transcript variants. [provided by RefSeq, Dec 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.203644.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2150585
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..597
                     /product="solute carrier organic anion transporter family
                     member 1A2 isoform 5"
                     /note="organic anion transporting polypeptide A; solute
                     carrier family 21 (organic anion transporter), member 3;
                     sodium-independent organic anion transporter; OATP-1;
                     solute carrier family 21 member 3; organic
                     anion-transporting polypeptide 1"
                     /calculated_mol_wt=65797
     Region          1..518
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            order(13..14,17..18,21,53,152..153,155..157,160,180,
                     183..184,187,305,308..309,312..314,317,346,350,391..392,
                     396,400,461,464..465,468..469,472)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341016"
     CDS             1..597
                     /gene="SLCO1A2"
                     /gene_synonym="OATP; OATP-A; OATP1A2; SLC21A3"
                     /coded_by="NM_001386958.1:167..1960"
                     /note="isoform 5 is encoded by transcript variant 34"
                     /db_xref="GeneID:6579"
                     /db_xref="HGNC:HGNC:10956"
                     /db_xref="MIM:602883"
ORIGIN      
        1 mfllaitcaf vsktlsgsym nsmltqierq fniptslvgf ingsfeignl lliifvsyfg
       61 tklhrpimig igcvvmglgc flkslphflm nqyeyestvs vsgnlssnsf lcmengtqil
      121 rptqdpsect kevkslmwvy vlvgnivrgm getpilplgi syiedfakfe nsplyiglve
      181 tgaiigplig lllasfcanv yvdtgfvntd dliitptdtr wvgawwfgfl icagvnvlta
      241 ipffflpntl pkegletnad iiknenedkq keevkkekyg itkdflpfmk slscnpiyml
      301 filvsviqfn afvnmisfmp kyleqqygis ssdaiflmgi ynlppicigy iigglimkkf
      361 kitvkqaahi gcwlslleyl lyflsflmtc enssvvgint syegipqdly vendifadcn
      421 vdcncpskiw dpvcgnngls ylsaclagce tsigtginmv fqncsciqts gnssavlglc
      481 dkgpdcslml qyflilsams sfiyslaaip gymvllrcmk seekslgvgl htfctrvfag
      541 ipapiyfgal mdstclhwgt lkcgesgacr iydsttfsrd tesifsglyf qgcwnsk
//
LOCUS       NP_001272333             152 aa            linear   PRI 21-NOV-2025
DEFINITION  THO complex subunit 7 isoform 2 [Homo sapiens].
ACCESSION   NP_001272333 XP_005265551
VERSION     NP_001272333.1
DBSOURCE    REFSEQ: accession NM_001285404.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Katahira,J., Senokuchi,K. and Hieda,M.
  TITLE     Human THO maintains the stability of repetitive DNA
  JOURNAL   Genes Cells 25 (5), 334-342 (2020)
   PUBMED   32065701
  REMARK    GeneRIF: Human THO maintains the stability of repetitive DNA.
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 152)
  AUTHORS   He,T.S., Xie,T., Li,J., Yang,Y.X., Li,C., Wang,W., Cao,L., Rao,H.,
            Ju,C. and Xu,L.G.
  TITLE     THO Complex Subunit 7 Homolog Negatively Regulates Cellular
            Antiviral Response against RNA Viruses by Targeting TBK1
  JOURNAL   Viruses 11 (2), 158 (2019)
   PUBMED   30769920
  REMARK    GeneRIF: THOC7 negatively regulates type I IFN production by
            promoting TBK1 proteasomal degradation in Sendai virus infection
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 152)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   6  (residues 1 to 152)
  AUTHORS   Masuda,S., Das,R., Cheng,H., Hurt,E., Dorman,N. and Reed,R.
  TITLE     Recruitment of the human TREX complex to mRNA during splicing
  JOURNAL   Genes Dev 19 (13), 1512-1517 (2005)
   PUBMED   15998806
REFERENCE   7  (residues 1 to 152)
  AUTHORS   Guo,S., Hakimi,M.A., Baillat,D., Chen,X., Farber,M.J.,
            Klein-Szanto,A.J., Cooch,N.S., Godwin,A.K. and Shiekhattar,R.
  TITLE     Linking transcriptional elongation and messenger RNA export to
            metastatic breast cancers
  JOURNAL   Cancer Res 65 (8), 3011-3016 (2005)
   PUBMED   15833825
REFERENCE   8  (residues 1 to 152)
  AUTHORS   Tascou,S., Kang,T.W., Trappe,R., Engel,W. and Burfeind,P.
  TITLE     Identification and characterization of NIF3L1 BP1, a novel
            cytoplasmic interaction partner of the NIF3L1 protein
  JOURNAL   Biochem Biophys Res Commun 309 (2), 440-448 (2003)
   PUBMED   12951069
REFERENCE   9  (residues 1 to 152)
  AUTHORS   Sato,S., Tomomori-Sato,C., Banks,C.A., Sorokina,I., Parmely,T.J.,
            Kong,S.E., Jin,J., Cai,Y., Lane,W.S., Brower,C.S., Conaway,R.C. and
            Conaway,J.W.
  TITLE     Identification of mammalian Mediator subunits with similarities to
            yeast Mediator subunits Srb5, Srb6, Med11, and Rox3
  JOURNAL   J Biol Chem 278 (17), 15123-15127 (2003)
   PUBMED   12584197
REFERENCE   10 (residues 1 to 152)
  AUTHORS   Kleiderlein,J.J., Nisson,P.E., Jessee,J., Li,W.B., Becker,K.G.,
            Derby,M.L., Ross,C.A. and Margolis,R.L.
  TITLE     CCG repeats in cDNAs from human brain
  JOURNAL   Hum Genet 103 (6), 666-673 (1998)
   PUBMED   9921901
  REMARK    Erratum:[Hum Genet 1999 Jan;104(1):113]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104162.2, BI914906.1, AF104914.2 and BC065012.1.
            
            On Oct 16, 2013 this sequence version replaced XP_005265551.1.
            
            Transcript Variant: This variant (3) differs in its 5' UTR and
            initiates translation at a downstream start codon, compared to
            variant (1). The encoded isoform (2) has a shorter N-terminus,
            compared to isoform 1. Both variant 2 and 3 encode the same
            isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3421950.1,
                                           SRR18074968.1706842.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.1"
     Protein         1..152
                     /product="THO complex subunit 7 isoform 2"
                     /note="Ngg1 interacting factor 3 like 1 binding protein 1;
                     functional spliceosome-associated protein 24; THO complex
                     subunit 7 homolog; NIF3L1-binding protein 1; THO complex 7
                     homolog; ngg1-interacting factor 3-like protein 1-binding
                     protein 1"
                     /calculated_mol_wt=17725
     Region          <1..87
                     /region_name="THOC7"
                     /note="Tho complex subunit 7; pfam05615"
                     /db_xref="CDD:461692"
     CDS             1..152
                     /gene="THOC7"
                     /gene_synonym="fSAP24; hTREX30; NIF3L1BP1"
                     /coded_by="NM_001285404.2:440..898"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS74957.1"
                     /db_xref="GeneID:80145"
                     /db_xref="HGNC:HGNC:29874"
                     /db_xref="MIM:611965"
ORIGIN      
        1 mlstlsqcef smgktllvyd mnlremenye kiykeiecsi agahekiaec kkqilqakri
       61 rknrqeydal akviqhhpdr hetlkeleal gkelehlshi kesvedklel rrkqfhvlls
      121 tihelqqtle ndeklsevee aqeasmetdp kp
//
LOCUS       NP_001350654            1539 aa            linear   PRI 21-NOV-2025
DEFINITION  AT-rich interactive domain-containing protein 1B isoform 4 [Homo
            sapiens].
ACCESSION   NP_001350654 XP_016866598
VERSION     NP_001350654.1
DBSOURCE    REFSEQ: accession NM_001363725.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1539)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1539)
  AUTHORS   Bosch,E., Guse,E., Kirchner,P., Winterpacht,A., Walther,M.,
            Alders,M., Kerkhof,J., Ekici,A.B., Sticht,H., Sadikovic,B., Reis,A.
            and Vasileiou,G.
  TITLE     The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation
  JOURNAL   Hum Genet 143 (8), 965-978 (2024)
   PUBMED   39028335
  REMARK    GeneRIF: The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation.
REFERENCE   3  (residues 1 to 1539)
  AUTHORS   Huang,X., Li,H., Yang,S., Ma,M., Lian,Y., Wu,X., Qi,X., Wang,X.,
            Rong,W. and Sheng,X.
  TITLE     De novo variation in ARID1B gene causes Coffin-Siris syndrome 1 in
            a Chinese family with excessive early-onset high myopia
  JOURNAL   BMC Med Genomics 17 (1), 142 (2024)
   PUBMED   38790056
  REMARK    GeneRIF: De novo variation in ARID1B gene causes Coffin-Siris
            syndrome 1 in a Chinese family with excessive early-onset high
            myopia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1539)
  AUTHORS   Hurlstone,A.F., Olave,I.A., Barker,N., van Noort,M. and Clevers,H.
  TITLE     Cloning and characterization of hELD/OSA1, a novel BRG1 interacting
            protein
  JOURNAL   Biochem J 364 (Pt 1), 255-264 (2002)
   PUBMED   11988099
  REMARK    GeneRIF: Cloning and characterization of hELD/OSA1, a novel BRG1
            interacting protein.
REFERENCE   5  (residues 1 to 1539)
  AUTHORS   Phelan,M.L., Sif,S., Narlikar,G.J. and Kingston,R.E.
  TITLE     Reconstitution of a core chromatin remodeling complex from SWI/SNF
            subunits
  JOURNAL   Mol Cell 3 (2), 247-253 (1999)
   PUBMED   10078207
REFERENCE   6  (residues 1 to 1539)
  AUTHORS   Imbert,G., Saudou,F., Yvert,G., Devys,D., Trottier,Y.,
            Garnier,J.M., Weber,C., Mandel,J.L., Cancel,G., Abbas,N., Durr,A.,
            Didierjean,O., Stevanin,G., Agid,Y. and Brice,A.
  TITLE     Cloning of the gene for spinocerebellar ataxia 2 reveals a locus
            with high sensitivity to expanded CAG/glutamine repeats
  JOURNAL   Nat Genet 14 (3), 285-291 (1996)
   PUBMED   8896557
REFERENCE   7  (residues 1 to 1539)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
REFERENCE   8  (residues 1 to 1539)
  AUTHORS   Vergano,S.A., van der Sluijs,P.J. and Santen,G.
  TITLE     ARID1B-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31132234
REFERENCE   9  (residues 1 to 1539)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
REFERENCE   10 (residues 1 to 1539)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049820.23 and AL591545.6.
            
            On May 29, 2018 this sequence version replaced XP_016866598.1.
            
            Summary: This locus encodes an AT-rich DNA interacting
            domain-containing protein. The encoded protein is a component of
            the SWI/SNF chromatin remodeling complex and may play a role in
            cell-cycle activation. The protein encoded by this locus is similar
            to AT-rich interactive domain-containing protein 1A. These two
            proteins function as alternative, mutually exclusive ARID-subunits
            of the SWI/SNF complex. The associated complexes play opposing
            roles. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            coding sequence compared to variant 3. The resulting isoform (4) is
            shorter at the N-terminus compared to isoform 3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3891561.1,
                                           SRR1803613.13873.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145893, SAMEA2156670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1539
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..1539
                     /product="AT-rich interactive domain-containing protein 1B
                     isoform 4"
                     /note="BRG1-binding protein ELD/OSA1; ELD (eyelid)/OSA
                     protein; BRG1-associated factor 250b; ARID
                     domain-containing protein 1B; AT rich interactive domain
                     1B (SWI1-like)"
                     /calculated_mol_wt=167679
     Region          <1..>236
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          357..449
                     /region_name="ARID_ARID1B"
                     /note="ARID/BRIGHT DNA binding domain of AT-rich
                     interactive domain-containing protein 1B (ARID1B) and
                     similar proteins; cd16877"
                     /db_xref="CDD:350641"
     Site            order(379..385,410,412..413,416,426,428..430,432)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350641"
     Region          470..>850
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          1230..1485
                     /region_name="BAF250_C"
                     /note="SWI/SNF-like complex subunit BAF250/Osa; pfam12031"
                     /db_xref="CDD:463439"
     CDS             1..1539
                     /gene="ARID1B"
                     /gene_synonym="6A3-5; BAF250B; BRIGHT; CSS1; DAN15;
                     ELD/OSA1; MRD12; OSA2; P250R; SMARCF2"
                     /coded_by="NM_001363725.2:390..5009"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS87460.1"
                     /db_xref="GeneID:57492"
                     /db_xref="HGNC:HGNC:18040"
                     /db_xref="MIM:614556"
ORIGIN      
        1 mppqppgsqs essshpalsq spmpqergfm agtqrnpqma qygpqqtgps msphpspggq
       61 mhagissfqq snssgtygpq msqygpqgny srppaysgvp sasysgpgpg mgisannqmh
      121 gqgpsqpcga vplgrmpsag mqnrpfpgnm ssmtpsspgm sqqggpgmgp pmptvnrkaq
      181 eaaaavmqaa ansaqsrqgs fpgmnqsglm assspysqpm nnssslmntq appysmapam
      241 vnssaasvgl admmspgesk lplplkadgk eegtpqpesk skdsyssqgi sqpptpgnlp
      301 vpspmspssa sissfhgdes dsisspgwpk tpsspkssss tttgekitkv yelgneperk
      361 lwvdryltfm eergspvssl pavgkkpldl frlyvcvkei gglaqvnknk kwrelatnln
      421 vgtsssaass lkkqyiqylf afeckierge epppevfstg dtkkqpklqp pspansgslq
      481 gpqtpqstgs nsmaevpgdl kpptpastph gqmtpmqggr sstisvhdpf sdvsdssfpk
      541 rnsmtpnapy qqgmsmpdvm grmpyepnkd pfggmrkvpg ssepfmtqgq mpnssmqdmy
      601 nqspsgamsn lgmgqrqqfp ygasydrrhe pygqqypgqg ppsgqppygg hqpglypqqp
      661 nykrhmdgmy gppakrhegd mynmqyssqq qemynqyggs ysgpdrrpiq gqypypysre
      721 rmqgpgqiqt hgippqmmgg plqssssegp qqnmwaarnd mpypyqnrqg pggptqappy
      781 pgmnrtddmm vpdqrinhes qwpshvsqrq pymsssasmq pitrppqpsy qtppslpnhi
      841 srapspasfq rslenrmsps kspflpsmkm qkvmptvpts qvtgpppqpp pirreitfpp
      901 gsveasqpvl kqrrkitskd ivtpeawrvm mslksgllae stwaldtini llyddstvat
      961 fnlsqlsgfl ellveyfrkc lidifgilme yevgdpsqka ldhnaarkdd sqsladdsgk
     1021 eeedaecidd deedeedeee dsektesdek ssialtapda aadpkekpkq askfdklpik
     1081 ivkknnlfvv drsdklgrvq efnsgllhwq lgggdttehi qthfeskmei pprrrppppl
     1141 ssagrkkeqe gkgdseeqqe ksiiatiddv lsarpgalpe danpgpqtes skfpfgiqqa
     1201 kshrniklle deprsrdetp lctiahwqds lakrcicvsn ivrslsfvpg ndaemskhpg
     1261 lvlilgklil lhhehperkr apqtyekeed edkgvacskd ewwwdclevl rdntlvtlan
     1321 isgqldlsay tesiclpild gllhwmvcps aeaqdpfptv gpnsvlspqr lvletlckls
     1381 iqdnnvdlil atppfsrqek fyatlvryvg drknpvcrem smallsnlaq gdalaaraia
     1441 vqkgsignli sfledgvtma qyqqsqhnlm hmqppplepp svdmmcraak allamarvde
     1501 nrsefllheg rlldisisav lnslvasvic dvlfqigql
//
LOCUS       NP_079049                416 aa            linear   PRI 21-NOV-2025
DEFINITION  bifunctional peptidase and arginyl-hydroxylase JMJD5 isoform 2
            [Homo sapiens].
ACCESSION   NP_079049
VERSION     NP_079049.2
DBSOURCE    REFSEQ: accession NM_024773.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Shen,J., Liu,G., Qi,H., Xiang,X. and Shao,J.
  TITLE     JMJD5 inhibits lung cancer progression by facilitating EGFR
            proteasomal degradation
  JOURNAL   Cell Death Dis 14 (10), 657 (2023)
   PUBMED   37813845
  REMARK    GeneRIF: JMJD5 inhibits lung cancer progression by facilitating
            EGFR proteasomal degradation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Wang,H., Wang,J., Liu,J., Wang,Y., Xia,G. and Huang,X.
  TITLE     Jumonji-C domain-containing protein 5 suppresses proliferation and
            aerobic glycolysis in pancreatic cancer cells in a c-Myc-dependent
            manner
  JOURNAL   Cell Signal 93, 110282 (2022)
   PUBMED   35176452
  REMARK    GeneRIF: Jumonji-C domain-containing protein 5 suppresses
            proliferation and aerobic glycolysis in pancreatic cancer cells in
            a c-Myc-dependent manner.
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Liu,H., Ramachandran,S., Fong,N., Phang,T., Lee,S., Parsa,P.,
            Liu,X., Harmacek,L., Danhorn,T., Song,T., Oh,S., Zhang,Q., Chen,Z.,
            Zhang,Q., Tu,T.H., Happoldt,C., O'Conner,B., Janknecht,R., Li,C.Y.,
            Marrack,P., Kappler,J., Leach,S. and Zhang,G.
  TITLE     JMJD5 couples with CDK9 to release the paused RNA polymerase II
  JOURNAL   Proc Natl Acad Sci U S A 117 (33), 19888-19895 (2020)
   PUBMED   32747552
  REMARK    GeneRIF: JMJD5 couples with CDK9 to release the paused RNA
            polymerase II.
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Youn,M.Y., Yokoyama,A., Fujiyama-Nakamura,S., Ohtake,F.,
            Minehata,K., Yasuda,H., Suzuki,T., Kato,S. and Imai,Y.
  TITLE     JMJD5, a Jumonji C (JmjC) domain-containing protein, negatively
            regulates osteoclastogenesis by facilitating NFATc1 protein
            degradation
  JOURNAL   J Biol Chem 287 (16), 12994-13004 (2012)
   PUBMED   22375008
  REMARK    GeneRIF: JMJD5 is a post-translational co-repressor for NFATc1 that
            attenuates osteoclastogenesis.
REFERENCE   7  (residues 1 to 416)
  AUTHORS   Jones,M.A., Covington,M.F., DiTacchio,L., Vollmers,C., Panda,S. and
            Harmer,S.L.
  TITLE     Jumonji domain protein JMJD5 functions in both the plant and human
            circadian systems
  JOURNAL   Proc Natl Acad Sci U S A 107 (50), 21623-21628 (2010)
   PUBMED   21115819
  REMARK    GeneRIF: Data show that both Arabidopsis jmjd5 mutant seedlings and
            mammalian cell cultures deficient for the human ortholog of this
            gene have similar fast-running circadian oscillations compared with
            WT.
REFERENCE   8  (residues 1 to 416)
  AUTHORS   Hsia,D.A., Tepper,C.G., Pochampalli,M.R., Hsia,E.Y., Izumiya,C.,
            Huerta,S.B., Wright,M.E., Chen,H.W., Kung,H.J. and Izumiya,Y.
  TITLE     KDM8, a H3K36me2 histone demethylase that acts in the cyclin A1
            coding region to regulate cancer cell proliferation
  JOURNAL   Proc Natl Acad Sci U S A 107 (21), 9671-9676 (2010)
   PUBMED   20457893
  REMARK    GeneRIF: show that JMJD5 (now renamed KDM8), demethylates H3K36me2
            and is required for cell cycle progression.
REFERENCE   9  (residues 1 to 416)
  AUTHORS   Shi,Y.
  TITLE     Histone lysine demethylases: emerging roles in development,
            physiology and disease
  JOURNAL   Nat Rev Genet 8 (11), 829-833 (2007)
   PUBMED   17909537
  REMARK    Review article
REFERENCE   10 (residues 1 to 416)
  AUTHORS   Suzuki,T., Minehata,K., Akagi,K., Jenkins,N.A. and Copeland,N.G.
  TITLE     Tumor suppressor gene identification using retroviral insertional
            mutagenesis in Blm-deficient mice
  JOURNAL   EMBO J 25 (14), 3422-3431 (2006)
   PUBMED   16858412
  REMARK    GeneRIF: Identifies five novel candidate tumor suppressor genes in
            mouse, including Pou2f2, Hivep3, Jmjd5, Fbxl10 and a protein
            similar to human N4BP3.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC027911.1, AK225066.1 and
            BQ022832.1.
            
            On Feb 21, 2009 this sequence version replaced NP_079049.1.
            
            Summary: This gene likely encodes a histone lysine demethylase.
            Studies of a similar protein in mouse indicate a potential role for
            this protein as a tumor suppressor. Alternatively spliced
            transcript variants have been described.[provided by RefSeq, Feb
            2009].
            
            Transcript Variant: This variant (2) uses an alternate 5' terminal
            exon and initiates translation at a downstream start codon,
            compared to variant 1. The encoded isoform (2) is shorter than
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.136893.1,
                                           SRR1803614.136097.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000286096.9/ ENSP00000286096.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.1"
     Protein         1..416
                     /product="bifunctional peptidase and arginyl-hydroxylase
                     JMJD5 isoform 2"
                     /EC_number="1.14.11.73"
                     /note="lysine-specific demethylase 8; jmjC
                     domain-containing protein 5; JmjC arginyl-hydroxylase;
                     jumonji domain-containing protein 5; jumonji domain
                     containing 5; lysine (K)-specific demethylase 8; arginyl
                     C3-hydroxylase KDM8; jumonji C domain-containing protein
                     5; bifunctional peptidase and arginyl-hydroxylase JMJD5;
                     L-arginine (3R)-hydroxylase KDM8"
                     /calculated_mol_wt=47139
     Region          1..110
                     /region_name="Interaction with RCCD1.
                     /evidence=ECO:0000269|PubMed:24981860"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N371.1)"
     Region          195..416
                     /region_name="Cupin_8"
                     /note="Cupin-like domain; pfam13621"
                     /db_xref="CDD:463936"
     CDS             1..416
                     /gene="KDM8"
                     /gene_synonym="JMJD5"
                     /coded_by="NM_024773.3:143..1393"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10627.1"
                     /db_xref="GeneID:79831"
                     /db_xref="HGNC:HGNC:25840"
                     /db_xref="MIM:611917"
ORIGIN      
        1 magdthcpae plaregtlwe alrallphsk edlkldlgek versvvtllq ratelfyegr
       61 rdeclqssev ildyswekln tgtwqdvdkd wrrvyaigcl lkalclcqap edantvaaal
      121 rvcdmgllmg aailgdillk vaailqthlp gkrpargslp eqpctkkara dhglipdvkl
      181 ektvprlhrp slqhfreqfl vpgrpvilkg vadhwpcmqk wsleyiqeia gcrtvpvevg
      241 srytdeewsq tlmtvnefis kyivneprdv gylaqhqlfd qipelkqdis ipdycslgdg
      301 eeeeitinaw fgpqgtispl hqdpqqnflv qvmgrkyirl yspqesgaly phdthllhnt
      361 sqvdvenpdl ekfpkfakap flscilspge ilfipvkywh yvraldlsfs vsfwws
//
LOCUS       NP_001317275             248 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform Tpm1.13 [Homo sapiens].
ACCESSION   NP_001317275 XP_016878030
VERSION     NP_001317275.1
DBSOURCE    REFSEQ: accession NM_001330346.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 248)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11 and BC007433.2.
            
            On Aug 23, 2016 this sequence version replaced XP_016878030.1.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Transcript Variant: This variant (Tpm1.13, also known as variant
            11) has a different 5' structure compared to variant Tpm1.1. It
            encodes isoform Tpm1.13, which has a distinct N-terminus, compared
            to isoform Tpm1.1st. Variants Tpm1.8, Tpm1.9 and Tpm1.13 encode
            isoforms that are the same length, but have distinct protein
            sequences.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.568067.1,
                                           ERR279841.4143.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..248
                     /product="tropomyosin alpha-1 chain isoform Tpm1.13"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=28449
     Region          12..246
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..248
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001330346.2:88..834"
                     /note="isoform Tpm1.13 is encoded by transcript variant
                     Tpm1.13"
                     /db_xref="CCDS:CCDS81894.1"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 magsssleav rrkirslqeq adaaeeragt lqreldherk lretaeadva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkviesraqk deekmeiqei qlkeakhiae
      121 dadrkyeeva rklviiesdl eraeeraels egkcaeleee lktvtnnlks leaqaekysq
      181 kedryeeeik vlsdklkeae traefaersv tkleksiddl edelyaqklk ykaiseeldh
      241 alndmtsi
//
LOCUS       NP_001340212             178 aa            linear   PRI 21-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 2 [Homo sapiens].
ACCESSION   NP_001340212
VERSION     NP_001340212.1
DBSOURCE    REFSEQ: accession NM_001353283.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2005064.1,
                                           SRR1803611.26086.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..178
                     /product="CYFIP-related Rac1 interactor B isoform 2"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=20062
     Region          <1..174
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..178
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353283.2:610..1146"
                     /note="isoform 2 is encoded by transcript variant 45"
                     /db_xref="CCDS:CCDS83327.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mtnpaiqndf syyrrtlsrm rinnvpaege nevnnelanr mslfyaeatp mlktlsdatt
       61 kfvsenknlp ienttdclst masvcrvmle tpeyrsrftn eetvsfclrv mvgviilydh
      121 vhpvgafakt skidmkgcik vlkdqppnsv egllnalryt tkhlndetts kqiksmlq
//
LOCUS       NP_001373975             346 aa            linear   PRI 21-NOV-2025
DEFINITION  heparan sulfate glucosamine 3-O-sulfotransferase 5 [Homo sapiens].
ACCESSION   NP_001373975
VERSION     NP_001373975.1
DBSOURCE    REFSEQ: accession NM_001387046.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Wang,Q., Xiang,B., Deng,W., Wu,J., Li,M., Ma,X., Wang,Y., Jiang,L.,
            McAlonan,G., Chua,S.E., Sham,P.C., Hu,X. and Li,T.
  TITLE     Genome-wide association analysis with gray matter volume as a
            quantitative phenotype in first-episode treatment-naive patients
            with schizophrenia
  JOURNAL   PLoS One 8 (9), e75083 (2013)
   PUBMED   24086445
  REMARK    Erratum:[PLoS One. 2015 Apr 07;10(4):e0122945. doi:
            10.1371/journal.pone.0122945. PMID: 25848962]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Vieira,A.R., McHenry,T.G., Daack-Hirsch,S., Murray,J.C. and
            Marazita,M.L.
  TITLE     Candidate gene/loci studies in cleft lip/palate and dental
            anomalies finds novel susceptibility genes for clefts
  JOURNAL   Genet Med 10 (9), 668-674 (2008)
   PUBMED   18978678
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Chen,J. and Liu,J.
  TITLE     Characterization of the structure of antithrombin-binding heparan
            sulfate generated by heparan sulfate 3-O-sulfotransferase 5
  JOURNAL   Biochim Biophys Acta 1725 (2), 190-200 (2005)
   PUBMED   16099108
  REMARK    GeneRIF: Structural analysis of 3-OST-5 HS(act) revealed that the
            antithrombin-binding site of 3-OST-5 HS(act) is located within a
            domain clustered with N-sulfated glucosamine units.
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Duncan,M.B., Chen,J., Krise,J.P. and Liu,J.
  TITLE     The biosynthesis of anticoagulant heparan sulfate by the heparan
            sulfate 3-O-sulfotransferase isoform 5
  JOURNAL   Biochim Biophys Acta 1671 (1-3), 34-43 (2004)
   PUBMED   15026143
  REMARK    GeneRIF: Results demonstrate that the human 3-O-sulfotransferase
            isoform 5 gene is capable of synthesizing anticoagulant heparan
            sulfate (HS) in CHO cells and may contribute to the biosynthesis of
            HS in humans.
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Chen,J., Duncan,M.B., Carrick,K., Pope,R.M. and Liu,J.
  TITLE     Biosynthesis of 3-O-sulfated heparan sulfate: unique substrate
            specificity of heparan sulfate 3-O-sulfotransferase isoform 5
  JOURNAL   Glycobiology 13 (11), 785-794 (2003)
   PUBMED   12907690
REFERENCE   6  (residues 1 to 346)
  AUTHORS   Mochizuki,H., Yoshida,K., Gotoh,M., Sugioka,S., Kikuchi,N.,
            Kwon,Y.D., Tawada,A., Maeyama,K., Inaba,N., Hiruma,T., Kimata,K.
            and Narimatsu,H.
  TITLE     Characterization of a heparan sulfate 3-O-sulfotransferase-5, an
            enzyme synthesizing a tetrasulfated disaccharide
  JOURNAL   J Biol Chem 278 (29), 26780-26787 (2003)
   PUBMED   12740361
  REMARK    GeneRIF: Recombinant 3-OST-5 only exhibited sulfotransferase
            activity toward heparan sulfate and heparin. 3-OST-5 was highly
            expressed in fetal brain, followed by adult brain and spinal cord,
            and at very low or undetectable levels in other tissues.
REFERENCE   7  (residues 1 to 346)
  AUTHORS   Xia,G., Chen,J., Tiwari,V., Ju,W., Li,J.P., Malmstrom,A., Shukla,D.
            and Liu,J.
  TITLE     Heparan sulfate 3-O-sulfotransferase isoform 5 generates both an
            antithrombin-binding site and an entry receptor for herpes simplex
            virus, type 1
  JOURNAL   J Biol Chem 277 (40), 37912-37919 (2002)
   PUBMED   12138164
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136446.14, AL500524.10 and AL355498.10.
            
            Summary: HS3ST5 belongs to a group of heparan sulfate
            3-O-sulfotransferases (EC 2.8.2.23) that transfer sulfate from
            3-prime-phosphoadenosine 5-prime phosphosulfate (PAPS) to heparan
            sulfate and heparin (Mochizuki et al., 2003 [PubMed
            12740361]).[supplied by OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.125766.1,
                                           SRR1660809.220962.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1966682,
                                           SAMEA1968968 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21-q22.1"
     Protein         1..346
                     /product="heparan sulfate glucosamine 3-O-sulfotransferase
                     5"
                     /EC_number="2.8.2.23"
                     /note="heparan sulfate 3-OST-5; h3-OST-5; heparan sulfate
                     3-O-sulfotransferase 5; heparan sulfate D-glucosaminyl
                     3-O-sulfotransferase 5; heparan sulfate (glucosamine)
                     3-O-sulfotransferase 5"
                     /calculated_mol_wt=40277
     Site            13..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZT8.1)"
     Region          90..330
                     /region_name="Sulfotransfer_1"
                     /note="Sulfotransferase domain; cl21551"
                     /db_xref="CDD:473908"
     Site            287
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZT8.1)"
     CDS             1..346
                     /gene="HS3ST5"
                     /gene_synonym="3-OST-5; 3OST5; HS3OST5; NBLA04021"
                     /coded_by="NM_001387046.1:1056..2096"
                     /db_xref="CCDS:CCDS34517.1"
                     /db_xref="GeneID:222537"
                     /db_xref="HGNC:HGNC:19419"
                     /db_xref="MIM:609407"
ORIGIN      
        1 mlfkqqawlr qkllvlgsla vgsllylvar vgsldrlqpi cpiegrlgga rtqaefplra
       61 lqfkrgllhe frkgnaskeq vrlhdlvqql pkaiiigvrk ggtralleml nlhpavvkas
      121 qeihffdnde nygkgiewyr kkmpfsypqq itiekspayf iteevperiy kmnssiklli
      181 ivrepttrai sdytqvlegk erknktyykf eklaidpntc evntkykavr tsiytkhler
      241 wlkyfpieqf hvvdgdrlit eplpelqlve kflnlppris qynlyfnatr gfyclrfnii
      301 fnkclagskg rihpevdpsv itklrkffhp fnqkfyqitg rtlnwp
//
LOCUS       NP_001191890             347 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-B-cell leukemia transcription factor 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001191890
VERSION     NP_001191890.1
DBSOURCE    REFSEQ: accession NM_001204961.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Huang,N., Zhang,H., Huang,Z., Wu,X., Zhang,N., Jiang,Y., Chen,C.
            and Zhuang,J.
  TITLE     Whole Exome Sequencing Revealing a Novel PBX1 Gene Variant in a
            Chinese Family Causing Recurrent Neonatal Death
  JOURNAL   Birth Defects Res 116 (8), e2396 (2024)
   PUBMED   39189629
  REMARK    GeneRIF: Whole Exome Sequencing Revealing a Novel PBX1 Gene Variant
            in a Chinese Family Causing Recurrent Neonatal Death.
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Choi,S.C., Park,Y.P., Roach,T., Jimenez,D., Fisher,A., Zadeh,M.,
            Ma,L., Sobel,E.S., Ge,Y., Mohamadzadeh,M. and Morel,L.
  TITLE     Lupus susceptibility gene Pbx1 controls the development, stability,
            and function of regulatory T cells via Rtkn2 expression
  JOURNAL   Sci Adv 10 (13), eadi4310 (2024)
   PUBMED   38536923
  REMARK    GeneRIF: Lupus susceptibility gene Pbx1 controls the development,
            stability, and function of regulatory T cells via Rtkn2 expression.
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Kao,T.W., Chen,H.H., Lin,J., Wang,T.L. and Shen,Y.A.
  TITLE     PBX1 as a novel master regulator in cancer: Its regulation,
            molecular biology, and therapeutic applications
  JOURNAL   Biochim Biophys Acta Rev Cancer 1879 (2), 189085 (2024)
   PUBMED   38341110
  REMARK    GeneRIF: PBX1 as a novel master regulator in cancer: Its
            regulation, molecular biology, and therapeutic applications.
            Review article
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Zhang,L., Guo,H., Zhang,X., Wang,L., Wei,F., Zhao,Y., Wang,B.,
            Meng,Y. and Li,Y.
  TITLE     Small nucleolar RNA Snora73 promotes psoriasis progression by
            sponging miR-3074-5p and regulating PBX1 expression
  JOURNAL   Funct Integr Genomics 24 (1), 15 (2024)
   PUBMED   38240925
  REMARK    GeneRIF: Small nucleolar RNA Snora73 promotes psoriasis progression
            by sponging miR-3074-5p and regulating PBX1 expression.
            Erratum:[Funct Integr Genomics. 2024 Jan 30;24(1):21. doi:
            10.1007/s10142-024-01306-1. PMID: 38286903]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Lu,Q., Knoepfler,P.S., Scheele,J., Wright,D.D. and Kamps,M.P.
  TITLE     Both Pbx1 and E2A-Pbx1 bind the DNA motif ATCAATCAA cooperatively
            with the products of multiple murine Hox genes, some of which are
            themselves oncogenes
  JOURNAL   Mol Cell Biol 15 (7), 3786-3795 (1995)
   PUBMED   7791786
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Monica,K., Galili,N., Nourse,J., Saltman,D. and Cleary,M.L.
  TITLE     PBX2 and PBX3, new homeobox genes with extensive homology to the
            human proto-oncogene PBX1
  JOURNAL   Mol Cell Biol 11 (12), 6149-6157 (1991)
   PUBMED   1682799
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Hunger,S.P., Galili,N., Carroll,A.J., Crist,W.M., Link,M.P. and
            Cleary,M.L.
  TITLE     The t(1;19)(q23;p13) results in consistent fusion of E2A and PBX1
            coding sequences in acute lymphoblastic leukemias
  JOURNAL   Blood 77 (4), 687-693 (1991)
   PUBMED   1671560
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Kamps,M.P., Murre,C., Sun,X.H. and Baltimore,D.
  TITLE     A new homeobox gene contributes the DNA binding domain of the
            t(1;19) translocation protein in pre-B ALL
  JOURNAL   Cell 60 (4), 547-555 (1990)
   PUBMED   1967983
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Nourse,J., Mellentin,J.D., Galili,N., Wilkinson,J., Stanbridge,E.,
            Smith,S.D. and Cleary,M.L.
  TITLE     Chromosomal translocation t(1;19) results in synthesis of a
            homeobox fusion mRNA that codes for a potential chimeric
            transcription factor
  JOURNAL   Cell 60 (4), 535-545 (1990)
   PUBMED   1967982
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359255.12, DB270853.1,
            DA760179.1, BC143451.1, AK291415.1, BX647313.1, DA483403.1,
            AK022962.1, AL390119.25 and AL049381.1.
            
            Summary: This gene encodes a nuclear protein that belongs to the
            PBX homeobox family of transcriptional factors. Studies in mice
            suggest that this gene may be involved in the regulation of
            osteogenesis and required for skeletal patterning and programming.
            A chromosomal translocation, t(1;19) involving this gene and
            TCF3/E2A gene, is associated with pre-B-cell acute lymphoblastic
            leukemia. The resulting fusion protein, in which the DNA binding
            domain of E2A is replaced by the DNA binding domain of this
            protein, transforms cells by constitutively activating
            transcription of genes regulated by the PBX protein family.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jun
            2017].
            
            Transcript Variant: This variant (2) is missing an internal coding
            exon compared to variant 1. This results in a frame-shift and a
            shorter isoform (2, also known as isoform PBX1b) with a distinct
            C-terminus compared to isoform 1. Variants 2 and 5 encode the same
            isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143451.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..347
                     /product="pre-B-cell leukemia transcription factor 1
                     isoform 2"
                     /note="pre-B-cell leukemia transcription factor 1;
                     homeobox protein PRL; homeobox protein PBX1; pre-B-cell
                     leukemia homeobox 1"
                     /calculated_mol_wt=38296
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P40424.1)"
     Region          42..232
                     /region_name="PBC"
                     /note="PBC domain; pfam03792"
                     /db_xref="CDD:461052"
     Region          45..124
                     /region_name="PBC-A.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01322"
                     /note="propagated from UniProtKB/Swiss-Prot (P40424.1)"
     Site            88..89
                     /site_type="other"
                     /note="Breakpoint for translocation to form TCF3-PBX1
                     oncogene; propagated from UniProtKB/Swiss-Prot (P40424.1)"
     Region          127..232
                     /region_name="PBC-B.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01322"
                     /note="propagated from UniProtKB/Swiss-Prot (P40424.1)"
     Region          234..294
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(234..238,240,260,266,279,281..282,285..286,288..290,
                     292..293)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(236,239,282,285..286,289)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            286
                     /site_type="other"
                     /note="Required for binding to the NFIL3 promoter.
                     /evidence=ECO:0000250|UniProtKB:P41778; propagated from
                     UniProtKB/Swiss-Prot (P40424.1)"
     CDS             1..347
                     /gene="PBX1"
                     /gene_synonym="CAKUHED"
                     /coded_by="NM_001204961.2:640..1683"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55654.1"
                     /db_xref="GeneID:5087"
                     /db_xref="HGNC:HGNC:8632"
                     /db_xref="MIM:176310"
ORIGIN      
        1 mdeqprlmhs hagvgmaghp glsqhlqdga ggtegeggrk qdigdilqqi mtitdqslde
       61 aqarkhalnc hrmkpalfnv lceikektvl sirgaqeeep tdpqlmrldn mllaegvagp
      121 ekgggsaaaa aaaaasggag sdnsvehsdy raklsqirqi yhtelekyeq acneftthvm
      181 nllreqsrtr pispkeierm vsiihrkfss iqmqlkqstc eavmilrsrf ldarrkrrnf
      241 nkqateilne yfyshlsnpy pseeakeela kkcgitvsqv snwfgnkrir ykknigkfqe
      301 eaniyaakta vtatnvsahg sqanspstpn saggypspcy qpdrriq
//
LOCUS       NP_002084                433 aa            linear   PRI 21-NOV-2025
DEFINITION  glycogen synthase kinase-3 beta isoform 1 [Homo sapiens].
ACCESSION   NP_002084
VERSION     NP_002084.2
DBSOURCE    REFSEQ: accession NM_002093.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Chen,F., Li,Y., Zhao,L., Lin,C., Zhou,Y., Ye,W., Wan,W., Zou,H. and
            Xue,Y.
  TITLE     Anti-inflammatory effects of MerTK by inducing M2 macrophage
            polarization via PI3K/Akt/GSK-3beta pathway in gout
  JOURNAL   Int Immunopharmacol 142 (Pt A), 112942 (2024)
   PUBMED   39217874
  REMARK    GeneRIF: Anti-inflammatory effects of MerTK by inducing M2
            macrophage polarization via PI3K/Akt/GSK-3beta pathway in gout.
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Toral-Rios,D., Pichardo-Rojas,P., Ruiz-Sanchez,E.,
            Rosas-Carrasco,O., Carvajal-Garcia,R., Galvez-Coutino,D.C.,
            Martinez-Rodriguez,N.L., Rubio-Chavez,A.D., Alcantara-Flores,M.,
            Lopez-Ramirez,A., Martinez-Rosas,A.R., Ruiz-Chow,A.A.,
            Alonso-Vanegas,M. and Campos-Pena,V.
  TITLE     Synergistic Effect between the APOE epsilon4 Allele with Genetic
            Variants of GSK3B and MAPT: Differential Profile between Refractory
            Epilepsy and Alzheimer Disease
  JOURNAL   Int J Mol Sci 25 (18), 10228 (2024)
   PUBMED   39337715
  REMARK    GeneRIF: Synergistic Effect between the APOE epsilon4 Allele with
            Genetic Variants of GSK3B and MAPT: Differential Profile between
            Refractory Epilepsy and Alzheimer Disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Enos,M.D., Gavagan,M., Jameson,N., Zalatan,J.G. and Weis,W.I.
  TITLE     Structural and functional effects of phosphopriming and scaffolding
            in the kinase GSK-3beta
  JOURNAL   Sci Signal 17 (852), eado0881 (2024)
   PUBMED   39226374
  REMARK    GeneRIF: Structural and functional effects of phosphopriming and
            scaffolding in the kinase GSK-3beta.
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Zhao,J., Wei,M., Guo,M., Wang,M., Niu,H., Xu,T. and Zhou,Y.
  TITLE     GSK3: A potential target and pending issues for treatment of
            Alzheimer's disease
  JOURNAL   CNS Neurosci Ther 30 (7), e14818 (2024)
   PUBMED   38946682
  REMARK    GeneRIF: GSK3: A potential target and pending issues for treatment
            of Alzheimer's disease.
            Review article
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Plyte,S.E., Hughes,K., Nikolakaki,E., Pulverer,B.J. and
            Woodgett,J.R.
  TITLE     Glycogen synthase kinase-3: functions in oncogenesis and
            development
  JOURNAL   Biochim Biophys Acta 1114 (2-3), 147-162 (1992)
   PUBMED   1333807
  REMARK    Review article
REFERENCE   7  (residues 1 to 433)
  AUTHORS   Goedert,M., Cohen,E.S., Jakes,R. and Cohen,P.
  TITLE     p42 MAP kinase phosphorylation sites in microtubule-associated
            protein tau are dephosphorylated by protein phosphatase 2A1.
            Implications for Alzheimer's disease [corrected]
  JOURNAL   FEBS Lett 312 (1), 95-99 (1992)
   PUBMED   1330687
  REMARK    Erratum:[FEBS Lett 1992 Nov 23;313(2):203]
REFERENCE   8  (residues 1 to 433)
  AUTHORS   Goode,N., Hughes,K., Woodgett,J.R. and Parker,P.J.
  TITLE     Differential regulation of glycogen synthase kinase-3 beta by
            protein kinase C isotypes
  JOURNAL   J Biol Chem 267 (24), 16878-16882 (1992)
   PUBMED   1324914
REFERENCE   9  (residues 1 to 433)
  AUTHORS   Rylatt,D.B., Aitken,A., Bilham,T., Condon,G.D., Embi,N. and
            Cohen,P.
  TITLE     Glycogen synthase from rabbit skeletal muscle. Amino acid sequence
            at the sites phosphorylated by glycogen synthase kinase-3, and
            extension of the N-terminal sequence containing the site
            phosphorylated by phosphorylase kinase
  JOURNAL   Eur J Biochem 107 (2), 529-537 (1980)
   PUBMED   6772446
REFERENCE   10 (residues 1 to 433)
  AUTHORS   Ameli,N.O., Teymoorian,G.A., Saleh,H. and Slamdoost,A.
  TITLE     Proceedings: Aneurysmal bone cysts of the spine
  JOURNAL   Acta Neurochir (Wien) 31 (3-4), 273 (1975)
   PUBMED   1181841
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092910.9, BC012760.2,
            DA477189.1, BC000251.1, AC069444.17 and CA312249.1.
            
            On Jun 10, 2002 this sequence version replaced NP_002084.1.
            
            Summary: The protein encoded by this gene is a serine-threonine
            kinase belonging to the glycogen synthase kinase subfamily. It is a
            negative regulator of glucose homeostasis and is involved in energy
            metabolism, inflammation, ER-stress, mitochondrial dysfunction, and
            apoptotic pathways. Defects in this gene have been associated with
            Parkinson disease and Alzheimer disease. [provided by RefSeq, Aug
            2017].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853559.23498.1,
                                           SRR11853563.23481.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.33"
     Protein         1..433
                     /product="glycogen synthase kinase-3 beta isoform 1"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.11.26"
                     /note="GSK-3 beta; serine/threonine-protein kinase GSK3B"
                     /calculated_mol_wt=47903
     Region          51..356
                     /region_name="STKc_GSK3"
                     /note="The catalytic domain of the Serine/Threonine
                     Kinase, Glycogen Synthase Kinase 3; cd14137"
                     /db_xref="CDD:271039"
     Site            order(62..66,70,83,85,96,110,132..135,138,140..141,181,
                     183,185..186,188,200,203,214,216..219,221,259)
                     /site_type="active"
                     /db_xref="CDD:271039"
     Site            order(62..65,70,83,85,110,132..135,138,183,185..186,188,
                     200)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271039"
     Site            order(66..67,212..220,228..229,260..264,266..267,271,
                     291..294)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:271039"
     Site            order(96,140,181,183,203,214,216..219,221,259)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271039"
     Site            order(199..209,211..221)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271039"
     Site            order(228,263..264,266..267,270..271,291..296)
                     /site_type="other"
                     /note="axin binding site [polypeptide binding]"
                     /db_xref="CDD:271039"
     CDS             1..433
                     /gene="GSK3B"
                     /coded_by="NM_002093.4:1014..2315"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2996.1"
                     /db_xref="GeneID:2932"
                     /db_xref="HGNC:HGNC:4617"
                     /db_xref="MIM:605004"
ORIGIN      
        1 msgrprttsf aesckpvqqp safgsmkvsr dkdgskvttv vatpgqgpdr pqevsytdtk
       61 vigngsfgvv yqaklcdsge lvaikkvlqd krfknrelqi mrkldhcniv rlryffyssg
      121 ekkdevylnl vldyvpetvy rvarhysrak qtlpviyvkl ymyqlfrsla yihsfgichr
      181 dikpqnllld pdtavlklcd fgsakqlvrg epnvsyicsr yyrapelifg atdytssidv
      241 wsagcvlael llgqpifpgd sgvdqlveii kvlgtptreq iremnpnyte fkfpqikahp
      301 wtkdssgtgh ftsgvrvfrp rtppeaialc srlleytpta rltpleacah sffdelrdpn
      361 vklpngrdtp alfnfttqel ssnpplatil ipphariqaa astptnataa sdantgdrgq
      421 tnnaasasas nst
//
LOCUS       NP_003042                500 aa            linear   PRI 21-NOV-2025
DEFINITION  monocarboxylate transporter 1 [Homo sapiens].
ACCESSION   NP_003042
VERSION     NP_003042.3
DBSOURCE    REFSEQ: accession NM_003051.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Gasser,B., Dossegger,A., Giraud,M.N. and Fluck,M.
  TITLE     T-Allele Carriers of Mono Carboxylate Transporter One Gene
            Polymorphism rs1049434 Demonstrate Altered Substrate Metabolization
            during Exhaustive Exercise
  JOURNAL   Genes (Basel) 15 (7), 918 (2024)
   PUBMED   39062697
  REMARK    GeneRIF: T-Allele Carriers of Mono Carboxylate Transporter One Gene
            Polymorphism rs1049434 Demonstrate Altered Substrate Metabolization
            during Exhaustive Exercise.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Seka,D.J., Schulz,A.K., Thaker,T.M. and Tomasiak,T.M.
  TITLE     The N-terminal signature motif on the transporter MCT1 is critical
            for CD147-mediated trafficking
  JOURNAL   J Biol Chem 300 (6), 107333 (2024)
   PUBMED   38820650
  REMARK    GeneRIF: The N-terminal signature motif on the transporter MCT1 is
            critical for CD147-mediated trafficking.
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Jin,M., Yuan,T., Tian,K., Li,J., Huang,Q., Chi,Y. and Huang,G.
  TITLE     Oncogenic circ-SLC16A1 promotes progression of non-small cell lung
            cancer via regulation of the miR-1287-5p/profilin 2 axis
  JOURNAL   Cell Mol Biol Lett 29 (1), 43 (2024)
   PUBMED   38539084
  REMARK    GeneRIF: Oncogenic circ-SLC16A1 promotes progression of non-small
            cell lung cancer via regulation of the miR-1287-5p/profilin 2 axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 500)
  AUTHORS   Grove,D.J., Russell,P.J. and Kearse,M.G.
  TITLE     To initiate or not to initiate: A critical assessment of eIF2A,
            eIF2D, and MCT-1.DENR to deliver initiator tRNA to ribosomes
  JOURNAL   Wiley Interdiscip Rev RNA 15 (2), e1833 (2024)
   PUBMED   38433101
  REMARK    GeneRIF: To initiate or not to initiate: A critical assessment of
            eIF2A, eIF2D, and MCT-1.DENR to deliver initiator tRNA to
            ribosomes.
            Review article
REFERENCE   6  (residues 1 to 500)
  AUTHORS   Garcia,C.K., Li,X., Luna,J. and Francke,U.
  TITLE     cDNA cloning of the human monocarboxylate transporter 1 and
            chromosomal localization of the SLC16A1 locus to 1p13.2-p12
  JOURNAL   Genomics 23 (2), 500-503 (1994)
   PUBMED   7835905
REFERENCE   7  (residues 1 to 500)
  AUTHORS   Garcia,C.K., Goldstein,J.L., Pathak,R.K., Anderson,R.G. and
            Brown,M.S.
  TITLE     Molecular characterization of a membrane transporter for lactate,
            pyruvate, and other monocarboxylates: implications for the Cori
            cycle
  JOURNAL   Cell 76 (5), 865-873 (1994)
   PUBMED   8124722
REFERENCE   8  (residues 1 to 500)
  AUTHORS   Gillis,D.
  TITLE     Nonsyndromic Genetic Hyperinsulinism Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301549
REFERENCE   9  (residues 1 to 500)
  AUTHORS   Kim,C.M., Goldstein,J.L. and Brown,M.S.
  TITLE     cDNA cloning of MEV, a mutant protein that facilitates cellular
            uptake of mevalonate, and identification of the point mutation
            responsible for its gain of function
  JOURNAL   J Biol Chem 267 (32), 23113-23121 (1992)
   PUBMED   1429658
REFERENCE   10 (residues 1 to 500)
  AUTHORS   Cori,C.F.
  TITLE     The glucose-lactic acid cycle and gluconeogenesis
  JOURNAL   Curr Top Cell Regul 18, 377-387 (1981)
   PUBMED   7273846
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158844.14.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 6, 2006 this sequence version replaced NP_003042.2.
            
            Summary: The protein encoded by this gene is a proton-linked
            monocarboxylate transporter that catalyzes the movement of many
            monocarboxylates, such as lactate and pyruvate, across the plasma
            membrane. Mutations in this gene are associated with erythrocyte
            lactate transporter defect. Alternatively spliced transcript
            variants have been found for this gene.[provided by RefSeq, Oct
            2009].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript. Variants 1 and 2 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL162079.1, BC026317.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369626.8/ ENSP00000358640.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.2"
     Protein         1..500
                     /product="monocarboxylate transporter 1"
                     /note="solute carrier family 16 (monocarboxylic acid
                     transporters), member 1; MCT 1; solute carrier family 16,
                     member 1 (monocarboxylic acid transporter 1); solute
                     carrier family 16 (monocarboxylate transporter), member 1"
                     /calculated_mol_wt=53813
     Region          1..455
                     /region_name="2A0113"
                     /note="monocarboxylate transporter 1; TIGR00892"
                     /db_xref="CDD:273325"
     Site            23..44
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53985.3)"
     Site            56..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53985.3)"
     Site            85..105
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53985.3)"
     Site            110..132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53985.3)"
     Site            147..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53985.3)"
     Site            175..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53985.3)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P53986; propagated from
                     UniProtKB/Swiss-Prot (P53985.3)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P53985.3)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P53986; propagated from
                     UniProtKB/Swiss-Prot (P53985.3)"
     Site            262..288
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53985.3)"
     Site            296..317
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53985.3)"
     Site            329..349
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53985.3)"
     Site            354..375
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53985.3)"
     Site            390..410
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53985.3)"
     Site            422..443
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P53985.3)"
     Region          454..500
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P53985.3)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P53985.3)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P53985.3)"
     Site            467
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P53985.3)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P53985.3)"
     Site            498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P53985.3)"
     CDS             1..500
                     /gene="SLC16A1"
                     /gene_synonym="HHF7; MCT; MCT1; MCT1D"
                     /coded_by="NM_003051.4:207..1709"
                     /db_xref="CCDS:CCDS858.1"
                     /db_xref="GeneID:6566"
                     /db_xref="HGNC:HGNC:10922"
                     /db_xref="MIM:600682"
ORIGIN      
        1 mppavggpvg ytppdggwgw avvigafisi gfsyafpksi tvffkeiegi fhattsevsw
       61 issimlavmy gggpissilv nkygsrivmi vggclsgcgl iaasfcntvq qlyvcigvig
      121 glglafnlnp altmigkyfy krrplangla magspvflct laplnqvffg ifgwrgsfli
      181 lgglllnccv agalmrpigp kptkagkdks kaslekagks gvkkdlhdan tdligrhpkq
      241 ekrsvfqtin qfldltlfth rgfllylsgn vimffglfap lvflssygks qhysseksaf
      301 llsilafvdm varpsmglva ntkpirpriq yffaasvvan gvchmlapls ttyvgfcvya
      361 gffgfafgwl ssvlfetlmd lvgpqrfssa vglvtivecc pvllgppllg rlndmygdyk
      421 ytywacgvvl iisgiylfig mginyrllak eqkaneqkke skeeetsidv agkpnevtka
      481 aespdqkdtd ggpkeeespv
//
LOCUS       NP_001229858             549 aa            linear   PRI 21-NOV-2025
DEFINITION  ankyrin repeat and SAM domain-containing protein 3 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001229858
VERSION     NP_001229858.1
DBSOURCE    REFSEQ: accession NM_001242929.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Shamseldin,H.E., Yakulov,T.A., Hashem,A., Walz,G. and Alkuraya,F.S.
  TITLE     ANKS3 is mutated in a family with autosomal recessive laterality
            defect
  JOURNAL   Hum Genet 135 (11), 1233-1239 (2016)
   PUBMED   27417436
  REMARK    GeneRIF: Consistent with the proposed role of the ANKS3 variant in
            the pathogenesis of the reported family's phenotype, we show that
            the mutant RNA failed to rescue the laterality defect in anks3
            morphants compared to wild-type RNA. Furthermore, we describe a new
            mutant anks3 line that also displays laterality defect in the
            homozygous state
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Ramachandran,H., Engel,C., Muller,B., Dengjel,J., Walz,G. and
            Yakulov,T.A.
  TITLE     Anks3 alters the sub-cellular localization of the Nek7 kinase
  JOURNAL   Biochem Biophys Res Commun 464 (3), 901-907 (2015)
   PUBMED   26188091
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Leettola,C.N., Knight,M.J., Cascio,D., Hoffman,S. and Bowie,J.U.
  TITLE     Characterization of the SAM domain of the PKD-related protein ANKS6
            and its interaction with ANKS3
  JOURNAL   BMC Struct Biol 14, 17 (2014)
   PUBMED   24998259
  REMARK    GeneRIF: Study finds that ANKS3-SAM polymerizes and ANKS6-SAM can
            bind to one end of the polymer; study presents crystal structures
            of both the ANKS3-SAM polymer and the ANKS3-SAM/ANKS6-SAM complex,
            revealing the molecular details of their association.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 549)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   8  (residues 1 to 549)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DR004376.1, AC020663.1, BX333650.2, AC023830.9, AK123496.1 and
            AI560632.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2582797.1,
                                           SRR14038196.1617662.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..549
                     /product="ankyrin repeat and SAM domain-containing protein
                     3 isoform 2"
                     /note="ankyrin repeat and SAM domain-containing protein 3"
                     /calculated_mol_wt=60270
     Region          <39..>113
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(40..41,44..46,48..49,53,56,61,63,67..68,71..73,
                     75..76,80,83,92,94,96,100..101,104..106,108..109,112,115)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          61..92
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          317..380
                     /region_name="SAM_ANKS3"
                     /note="SAM domain of ANKS3 subfamily; cd09519"
                     /db_xref="CDD:188918"
     CDS             1..549
                     /gene="ANKS3"
                     /coded_by="NM_001242929.2:119..1768"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS73820.1"
                     /db_xref="GeneID:124401"
                     /db_xref="HGNC:HGNC:29422"
                     /db_xref="MIM:617310"
ORIGIN      
        1 mselsdease pellnrslsm whglgtqvsg eeldvpldlh taasigqyev vkecvqrepi
       61 cgftplmeaa aagheiivqy flnhgvkvda rdhsgatarm lakqyghmki valmdtysps
      121 lpkslyrspe kyedlsssde scpapqrqrp crkkgvsihe gpralaritg iglggraprp
      181 ryeqapprgy vtfnssgenp leeeglccrd vtspinerdv esssssssre ehafcanlgp
      241 vqsssssegl araqglssea svesnedsdh ackssarkqa ksymktknpd sqwppraatd
      301 regflaessp qtqrapysgp qdlaalleqi gclkylqvfe eqdvdlrifl tltesdlkei
      361 gitlfgpkrk mtsaiarwhs sarppgdale layadrleae mqelaiqlhk rceeveatrg
      421 qvcqeqelra vvesclleqd raredlqarl retwalarda alvldqlrac qaelssrvrq
      481 dqppgaatlg lavppadskg wqaslqamsl pelsgaledr vremgqalcl vtqsleklqv
      541 lngkkwret
//
LOCUS       NP_001020268             212 aa            linear   PRI 21-NOV-2025
DEFINITION  proteasome subunit alpha-type 8 isoform 3 [Homo sapiens].
ACCESSION   NP_001020268
VERSION     NP_001020268.1
DBSOURCE    REFSEQ: accession NM_001025097.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Zivkovic,D., Sanchez Dafun,A., Menneteau,T., Schahl,A., Lise,S.,
            Kervarrec,C., Toste Rego,A., da Fonseca,P.C.A., Chavent,M.,
            Pineau,C., Burlet-Schiltz,O., Marcoux,J. and Bousquet,M.P.
  TITLE     Proteasome complexes experience profound structural and functional
            rearrangements throughout mammalian spermatogenesis
  JOURNAL   Proc Natl Acad Sci U S A 119 (15), e2116826119 (2022)
   PUBMED   35377789
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Teumer,A., Holtfreter,B., Volker,U., Petersmann,A., Nauck,M.,
            Biffar,R., Volzke,H., Kroemer,H.K., Meisel,P., Homuth,G. and
            Kocher,T.
  TITLE     Genome-wide association study of chronic periodontitis in a general
            German population
  JOURNAL   J Clin Periodontol 40 (11), 977-985 (2013)
   PUBMED   24024966
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Kirin,M., Chandra,A., Charteris,D.G., Hayward,C., Campbell,S.,
            Celap,I., Bencic,G., Vatavuk,Z., Kirac,I., Richards,A.J.,
            Tenesa,A., Snead,M.P., Fleck,B.W., Singh,J., Harsum,S.,
            Maclaren,R.E., den Hollander,A.I., Dunlop,M.G., Hoyng,C.B.,
            Wright,A.F., Campbell,H., Vitart,V. and Mitry,D.
  TITLE     Genome-wide association study identifies genetic risk underlying
            primary rhegmatogenous retinal detachment
  JOURNAL   Hum Mol Genet 22 (15), 3174-3185 (2013)
   PUBMED   23585552
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Qian,M.X., Pang,Y., Liu,C.H., Haratake,K., Du,B.Y., Ji,D.Y.,
            Wang,G.F., Zhu,Q.Q., Song,W., Yu,Y., Zhang,X.X., Huang,H.T.,
            Miao,S., Chen,L.B., Zhang,Z.H., Liang,Y.N., Liu,S., Cha,H.,
            Yang,D., Zhai,Y., Komatsu,T., Tsuruta,F., Li,H., Cao,C., Li,W.,
            Li,G.H., Cheng,Y., Chiba,T., Wang,L., Goldberg,A.L., Shen,Y. and
            Qiu,X.B.
  TITLE     Acetylation-mediated proteasomal degradation of core histones
            during DNA repair and spermatogenesis
  JOURNAL   Cell 153 (5), 1012-1024 (2013)
   PUBMED   23706739
REFERENCE   5  (residues 1 to 212)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   6  (residues 1 to 212)
  AUTHORS   Nusbaum,C., Zody,M.C., Borowsky,M.L., Kamal,M., Kodira,C.D.,
            Taylor,T.D., Whittaker,C.A., Chang,J.L., Cuomo,C.A., Dewar,K.,
            FitzGerald,M.G., Yang,X., Abouelleil,A., Allen,N.R., Anderson,S.,
            Bloom,T., Bugalter,B., Butler,J., Cook,A., DeCaprio,D., Engels,R.,
            Garber,M., Gnirke,A., Hafez,N., Hall,J.L., Norman,C.H., Itoh,T.,
            Jaffe,D.B., Kuroki,Y., Lehoczky,J., Lui,A., Macdonald,P.,
            Mauceli,E., Mikkelsen,T.S., Naylor,J.W., Nicol,R., Nguyen,C.,
            Noguchi,H., O'Leary,S.B., O'Neill,K., Piqani,B., Smith,C.L.,
            Talamas,J.A., Topham,K., Totoki,Y., Toyoda,A., Wain,H.M.,
            Young,S.K., Zeng,Q., Zimmer,A.R., Fujiyama,A., Hattori,M.,
            Birren,B.W., Sakaki,Y. and Lander,E.S.
  TITLE     DNA sequence and analysis of human chromosome 18
  JOURNAL   Nature 437 (7058), 551-555 (2005)
   PUBMED   16177791
  REMARK    Erratum:[Nature. 2005 Dec 1;438(7068):696. O'Neill, Keith [added]]
REFERENCE   7  (residues 1 to 212)
  AUTHORS   Margottin-Goguet,F., Hsu,J.Y., Loktev,A., Hsieh,H.M., Reimann,J.D.
            and Jackson,P.K.
  TITLE     Prophase destruction of Emi1 by the SCF(betaTrCP/Slimb) ubiquitin
            ligase activates the anaphase promoting complex to allow
            progression beyond prometaphase
  JOURNAL   Dev Cell 4 (6), 813-826 (2003)
   PUBMED   12791267
REFERENCE   8  (residues 1 to 212)
  AUTHORS   Claverol,S., Burlet-Schiltz,O., Girbal-Neuhauser,E., Gairin,J.E.
            and Monsarrat,B.
  TITLE     Mapping and structural dissection of human 20 S proteasome using
            proteomic approaches
  JOURNAL   Mol Cell Proteomics 1 (8), 567-578 (2002)
   PUBMED   12376572
  REMARK    GeneRIF: This article provides an overview of some of the
            components in the human 20 S proteasome.
REFERENCE   9  (residues 1 to 212)
  AUTHORS   Geley,S., Kramer,E., Gieffers,C., Gannon,J., Peters,J.M. and
            Hunt,T.
  TITLE     Anaphase-promoting complex/cyclosome-dependent proteolysis of human
            cyclin A starts at the beginning of mitosis and is not subject to
            the spindle assembly checkpoint
  JOURNAL   J Cell Biol 153 (1), 137-148 (2001)
   PUBMED   11285280
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC042820.1 and BC025393.1.
            
            Transcript Variant: This variant (3) uses two different alternate
            in-frame splice sites in the coding region, compared to variant 1,
            resulting in a shorter isoform (3).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025393.1, CV024283.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q11.2"
     Protein         1..212
                     /product="proteasome subunit alpha-type 8 isoform 3"
                     /EC_number="3.4.25.1"
                     /note="proteasome (prosome, macropain) subunit, alpha
                     type, 8; proteasome subunit alpha-type 8; proteasome
                     subunit alpha 8; alpha4s; proteasome alpha 4 subunit"
                     /calculated_mol_wt=23571
     Region          5..175
                     /region_name="Ntn_hydrolase"
                     /note="The Ntn hydrolases (N-terminal nucleophile) are a
                     diverse superfamily of of enzymes that are activated
                     autocatalytically via an N-terminally lcated nucleophilic
                     amino acid. N-terminal nucleophile (NTN-) hydrolase
                     superfamily, which contains a...; cl00467"
                     /db_xref="CDD:469781"
     CDS             1..212
                     /gene="PSMA8"
                     /gene_synonym="PSMA7L"
                     /coded_by="NM_001025097.2:98..736"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS45843.1"
                     /db_xref="GeneID:143471"
                     /db_xref="HGNC:HGNC:22985"
                     /db_xref="MIM:617841"
ORIGIN      
        1 masrydrait vfspdghlfq veyaqeavkk gstavgirgl tadarvvinr arvecqshkl
       61 tvedpvtvey itrfiatlkq kytqsngrrp fgisalivgf dddgisrlyq tdpsgtyhaw
      121 kanaigrsak tvreflekny tedaiasdse aiklaikall evvqsggkni elaiirrnqp
      181 lkmfsakeve lyvteiekek eeaekkkskk sv
//
LOCUS       NP_001371748            1066 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 76 [Homo sapiens].
ACCESSION   NP_001371748
VERSION     NP_001371748.1
DBSOURCE    REFSEQ: accession NM_001384819.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1066)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1066)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1066)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1066)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1066)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1066)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1066)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.1323932.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1066
                     /product="microtubule-associated protein 4 isoform 76"
                     /note="MAP-4"
                     /calculated_mol_wt=112176
     Region          <575..919
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <931..952
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          954..983
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1066
                     /gene="MAP4"
                     /coded_by="NM_001384819.1:96..3296"
                     /note="isoform 76 is encoded by transcript variant 77"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgsp tefleekmay qeypnsqnwp
      121 edtnfcfqpe qvvdpiqtdp fkmyhdddla dlvfpssata dtsifagqnd plkdsygmsp
      181 cntavvpqgw svealnsphs esfvspeava eppqptavpl elakeiemas eerppaqale
      241 immglkttdm apsketemal akdmalatkt evalakdmes ptkldvtlak dmqpsmesdm
      301 alvkdmelpt ekevalvkdv rwptetdvss aknvvlptet evapakdvtl lketeraspi
      361 kmdlapskdm gppkenkket eraspikmdl apskdmgppk enkivpakdl vllseievaq
      421 andiisstei ssaekvalss etevalardm tlppetnvil tkdkalplea evapvkdmaq
      481 lpeteiapak dvapstvkev gllkdmspls etemalgkdv tpppetevvl iknvclppem
      541 evaltedqvp alkteaplak dgvltlannv tpakdvppls eteatpvpik dmeiaqtqkg
      601 isedshlesl qdvgqsaapt fmispetvtg tgkkcslpae edsvleklge rkpcnsqpse
      661 lssetsgiar peegrpvvsg tgndittppn kelppspekk tkplattqpa ktstskaktq
      721 ptslpkqpap ttigglnkkp mslasglvpa appkrpavas arpsilpskd vkpkpiadak
      781 apekraspsk pasapasrsg skstqtvakt ttaaavastg pssrspstll pkkptaikte
      841 gkpaevkkmt aksvpadlsr pkststssmk ktttlsgtap aagvvpsrvk atpmpsrpst
      901 tpfidkkpts akpssttprl srlatntsap dlknvrskvg stenikhqpg ggrvqiqnkk
      961 vdiskvsskc gskanikhkp gggdvkiesq klnfkekaqa ktegggseap lcpgppagee
     1021 paiseaapea gaptsasgln ghptlsgggd qreaqtldsq iqetsi
//
LOCUS       NP_001273278             657 aa            linear   PRI 21-NOV-2025
DEFINITION  kin of IRRE-like protein 1 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001273278
VERSION     NP_001273278.1
DBSOURCE    REFSEQ: accession NM_001286349.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 657)
  AUTHORS   Wang,T., Chen,S., Wang,Z., Li,S., Fei,X., Wang,T. and Zhang,M.
  TITLE     KIRREL promotes the proliferation of gastric cancer cells and
            angiogenesis through the PI3K/AKT/mTOR pathway
  JOURNAL   J Cell Mol Med 28 (1), e18020 (2024)
   PUBMED   37909722
  REMARK    GeneRIF: KIRREL promotes the proliferation of gastric cancer cells
            and angiogenesis through the PI3K/AKT/mTOR pathway.
REFERENCE   3  (residues 1 to 657)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 657)
  AUTHORS   Gu,Y., Wang,Y., Sha,Z., He,C., Zhu,Y., Li,J., Yu,A., Zhong,Z.,
            Wang,X., Sun,Y., Lan,F. and Yu,F.X.
  TITLE     Transmembrane protein KIRREL1 regulates Hippo signaling via a
            feedback loop and represents a therapeutic target in YAP/TAZ-active
            cancers
  JOURNAL   Cell Rep 40 (9), 111296 (2022)
   PUBMED   36044856
  REMARK    GeneRIF: Transmembrane protein KIRREL1 regulates Hippo signaling
            via a feedback loop and represents a therapeutic target in
            YAP/TAZ-active cancers.
REFERENCE   5  (residues 1 to 657)
  AUTHORS   Paul,A., Annunziato,S., Lu,B., Sun,T., Evrova,O., Planas-Paz,L.,
            Orsini,V., Terracciano,L.M., Charlat,O., Loureiro,Z.Y., Ji,L.,
            Zamponi,R., Sigoillot,F., Lei,H., Lindeman,A., Russ,C.,
            Reece-Hoyes,J.S., Nicholson,T.B., Tchorz,J.S. and Cong,F.
  TITLE     Cell adhesion molecule KIRREL1 is a feedback regulator of Hippo
            signaling recruiting SAV1 to cell-cell contact sites
  JOURNAL   Nat Commun 13 (1), 930 (2022)
   PUBMED   35177623
  REMARK    GeneRIF: Cell adhesion molecule KIRREL1 is a feedback regulator of
            Hippo signaling recruiting SAV1 to cell-cell contact sites.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 657)
  AUTHORS   Barletta,G.M., Kovari,I.A., Verma,R.K., Kerjaschki,D. and
            Holzman,L.B.
  TITLE     Nephrin and Neph1 co-localize at the podocyte foot process
            intercellular junction and form cis hetero-oligomers
  JOURNAL   J Biol Chem 278 (21), 19266-19271 (2003)
   PUBMED   12646566
REFERENCE   7  (residues 1 to 657)
  AUTHORS   Huber,T.B., Schmidts,M., Gerke,P., Schermer,B., Zahn,A.,
            Hartleben,B., Sellin,L., Walz,G. and Benzing,T.
  TITLE     The carboxyl terminus of Neph family members binds to the PDZ
            domain protein zonula occludens-1
  JOURNAL   J Biol Chem 278 (15), 13417-13421 (2003)
   PUBMED   12578837
REFERENCE   8  (residues 1 to 657)
  AUTHORS   Gerke,P., Huber,T.B., Sellin,L., Benzing,T. and Walz,G.
  TITLE     Homodimerization and heterodimerization of the glomerular podocyte
            proteins nephrin and NEPH1
  JOURNAL   J Am Soc Nephrol 14 (4), 918-926 (2003)
   PUBMED   12660326
REFERENCE   9  (residues 1 to 657)
  AUTHORS   Sellin,L., Huber,T.B., Gerke,P., Quack,I., Pavenstadt,H. and
            Walz,G.
  TITLE     NEPH1 defines a novel family of podocin interacting proteins
  JOURNAL   FASEB J 17 (1), 115-117 (2003)
   PUBMED   12424224
REFERENCE   10 (residues 1 to 657)
  AUTHORS   Donoviel,D.B., Freed,D.D., Vogel,H., Potter,D.G., Hawkins,E.,
            Barrish,J.P., Mathur,B.N., Turner,C.A., Geske,R., Montgomery,C.A.,
            Starbuck,M., Brandt,M., Gupta,A., Ramirez-Solis,R., Zambrowicz,B.P.
            and Powell,D.R.
  TITLE     Proteinuria and perinatal lethality in mice lacking NEPH1, a novel
            protein with homology to NEPHRIN
  JOURNAL   Mol Cell Biol 21 (14), 4829-4836 (2001)
   PUBMED   11416156
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK297788.1, AL139010.29 and AA628934.1.
            
            Summary: NEPH1 is a member of the nephrin-like protein family,
            which includes NEPH2 (MIM 607761) and NEPH3 (MIM 607762). The
            cytoplasmic domains of these proteins interact with the C terminus
            of podocin (NPHS2; MIM 604766), and the genes are expressed in
            kidney podocytes, cells involved in ensuring size- and
            charge-selective ultrafiltration (Sellin et al., 2003 [PubMed
            12424224]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (2) lacks two in-frame exons in
            the 5' coding region compared to variant 1. The encoded isoform (2)
            is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297788.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.1"
     Protein         1..657
                     /product="kin of IRRE-like protein 1 isoform 2 precursor"
                     /note="nephrin related; kin of IRRE-like protein 1;
                     nephrin-like protein 1; kin of irregular chiasm-like
                     protein 1; kin of IRRE like"
                     /calculated_mol_wt=70901
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1839
     Region          22..119
                     /region_name="IgI_2_KIRREL3-like"
                     /note="Second immunoglobulin (Ig)-like domain of Kirrel
                     (kin of irregular chiasm-like) 3, and similar domains;
                     member of the I-set of Ig superfamily (IgSF) domains;
                     cd05759"
                     /db_xref="CDD:409416"
     Region          23..26
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409416"
     Region          29..33
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409416"
     Region          40..47
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409416"
     Region          52..57
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409416"
     Region          60..62
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409416"
     Region          65..72
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409416"
     Region          79..87
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409416"
     Region          96..104
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409416"
     Region          110..116
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409416"
     Region          122..191
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          208..273
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          291..388
                     /region_name="IgI_5_KIRREL3"
                     /note="Fifth immunoglobulin (Ig)-like domain of Kirrel
                     (kin of irregular chiasm-like) 3 protein; member of the
                     I-set of Ig superfamily (IgSF) domains; cd05898"
                     /db_xref="CDD:409479"
     Region          292..296
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409479"
     Region          298..301
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409479"
     Region          309..316
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409479"
     Region          323..328
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409479"
     Region          330..333
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409479"
     Region          341..348
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409479"
     Region          351..358
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409479"
     Region          369..376
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409479"
     Region          379..386
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409479"
     CDS             1..657
                     /gene="KIRREL1"
                     /gene_synonym="KIRREL; NEPH1; NPHS23"
                     /coded_by="NM_001286349.2:33..2006"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS72952.1"
                     /db_xref="GeneID:55243"
                     /db_xref="HGNC:HGNC:15734"
                     /db_xref="MIM:607428"
ORIGIN      
        1 mlsllvwilt lsdtfsqvpp edtridggpv illqagtphn ltcrafnakp aatiiwfrdg
       61 tqqegavast ellkdgkret tvsqllinpt dldigrvftc rsmneaipsg ketsieldvh
      121 hpptvtlsie pqtvqegerv vftcqatanp eilgyrwakg gfliedahes ryetnvdysf
      181 ftepvscevh nkvgstnvst lvnvhfapri vvdpkptttd igsdvtltcv wvgnppltlt
      241 wtkkdsnmvl snsnqlllks vtqadagtyt craivprigv aerevplyvn gppiisseav
      301 qyavrgdggk vecfigstpp pdriawawke nflevgtler ytvertnsgs gvlstltinn
      361 vmeadfqthy nctawnsfgp gtaiiqleer evlpvgiiag atigasilli fffialvffl
      421 yrrrkgsrkd vtlrkldikv etvnrepltm hsdreddtas vstatrvmka iyssfkddvd
      481 lkqdlrcdti dtreeyemkd ptngyynvra hedrpssrav lyadyrapgp arfdgrpssr
      541 lshssgyaql ntysrgpasd ygpeptppgp aapagtdtts qlsyenyekf nshpfpgaag
      601 yptyrlgypq appsglertp yeaydpigky atatrfsyts qhsdygqrfq qrmqthv
//
LOCUS       NP_004002               2344 aa            linear   PRI 21-NOV-2025
DEFINITION  dystrophin isoform Dp260-1 [Homo sapiens].
ACCESSION   NP_004002
VERSION     NP_004002.3
DBSOURCE    REFSEQ: accession NM_004011.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2344)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2344)
  AUTHORS   Chen,L., Luo,X., Wang,H., Tian,Y. and Liu,Y.
  TITLE     Identifying inversions with breakpoints in the Dystrophin gene
            through long-read sequencing: report of two cases
  JOURNAL   BMC Med Genomics 17 (1), 227 (2024)
   PUBMED   39251998
  REMARK    GeneRIF: Identifying inversions with breakpoints in the Dystrophin
            gene through long-read sequencing: report of two cases.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2344)
  AUTHORS   Davies,K.E. and Vogt,J.
  TITLE     Long-term clinical follow-up of a family with Becker muscular
            dystrophy associated with a large deletion in the DMD gene
  JOURNAL   Neuromuscul Disord 39, 5-9 (2024)
   PUBMED   38653179
  REMARK    GeneRIF: Long-term clinical follow-up of a family with Becker
            muscular dystrophy associated with a large deletion in the DMD
            gene.
            Erratum:[Neuromuscul Disord. 2024 Jun;39:54. doi:
            10.1016/j.nmd.2024.05.010. PMID: 38801812]
REFERENCE   4  (residues 1 to 2344)
  AUTHORS   Achermann,J.C. and Vilain,E.J.
  TITLE     NR0B1-Related Adrenal Hypoplasia Congenita
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301604
REFERENCE   5  (residues 1 to 2344)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   6  (residues 1 to 2344)
  AUTHORS   Darras,B.T., Urion,D.K. and Ghosh,P.S.
  TITLE     Dystrophinopathies
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301298
REFERENCE   7  (residues 1 to 2344)
  AUTHORS   Nigro,V., Politano,L., Nigro,G., Romano,S.C., Molinari,A.M. and
            Puca,G.A.
  TITLE     Detection of a nonsense mutation in the dystrophin gene by multiple
            SSCP
  JOURNAL   Hum Mol Genet 1 (7), 517-520 (1992)
   PUBMED   1307253
REFERENCE   8  (residues 1 to 2344)
  AUTHORS   Gorecki,D.C., Monaco,A.P., Derry,J.M., Walker,A.P., Barnard,E.A.
            and Barnard,P.J.
  TITLE     Expression of four alternative dystrophin transcripts in brain
            regions regulated by different promoters
  JOURNAL   Hum Mol Genet 1 (7), 505-510 (1992)
   PUBMED   1307251
REFERENCE   9  (residues 1 to 2344)
  AUTHORS   Lederfein,D., Levy,Z., Augier,N., Mornet,D., Morris,G., Fuchs,O.,
            Yaffe,D. and Nudel,U.
  TITLE     A 71-kilodalton protein is a major product of the Duchenne muscular
            dystrophy gene in brain and other nonmuscle tissues
  JOURNAL   Proc Natl Acad Sci U S A 89 (12), 5346-5350 (1992)
   PUBMED   1319059
REFERENCE   10 (residues 1 to 2344)
  AUTHORS   Koenig,M., Monaco,A.P. and Kunkel,L.M.
  TITLE     The complete sequence of dystrophin predicts a rod-shaped
            cytoskeletal protein
  JOURNAL   Cell 53 (2), 219-228 (1988)
   PUBMED   3282674
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109609.5, AL139278.12,
            AC096506.5, AC093193.11, AC079864.22, AC093167.11, AC079175.24,
            AC079177.21, AC090632.13, AC078958.30, AC079143.17 and AC006061.1.
            
            On Jun 2, 2019 this sequence version replaced NP_004002.2.
            
            Summary: This gene spans a genomic range of greater than 2 Mb and
            encodes a large protein containing an N-terminal actin-binding
            domain and multiple spectrin repeats. The encoded protein forms a
            component of the dystrophin-glycoprotein complex (DGC), which
            bridges the inner cytoskeleton and the extracellular matrix.
            Deletions, duplications, and point mutations at this gene locus may
            cause Duchenne muscular dystrophy (DMD), Becker muscular dystrophy
            (BMD), or cardiomyopathy. Alternative promoter usage and
            alternative splicing result in numerous distinct transcript
            variants and protein isoforms for this gene. [provided by RefSeq,
            Dec 2016].
            
            Transcript Variant: transcript Dp260-1 uses exons 30-79, and
            originates from a promoter/exon 1 sequence located in intron 29 of
            the dystrophin gene. As a result, Dp260-1 contains a 95 bp exon 1
            encoding a unique N-terminal 16 aa MTEIILLIFFPAYFLN-sequence that
            replaces amino acids 1-1357 of the full-length dystrophin product
            (Dp427m isoform).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1965299, SAMEA1966682
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2344
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp21.2-p21.1"
     Protein         1..2344
                     /product="dystrophin isoform Dp260-1"
                     /note="mutant dystrophin"
                     /calculated_mol_wt=271307
     Region          1..16
                     /region_name="dystrophin Dp260-1 unique N-terminus"
     Region          27..122
                     /region_name="repeat region 10"
     Region          <32..>597
                     /region_name="235kDa-fam"
                     /note="reticulocyte binding/rhoptry protein; TIGR01612"
                     /db_xref="CDD:130673"
     Region          120..227
                     /region_name="repeat region 11"
     Region          228..335
                     /region_name="repeat region 12"
     Region          336..437
                     /region_name="repeat region 13"
     Region          438..533
                     /region_name="repeat region 14"
     Region          439..627
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          534..632
                     /region_name="repeat region 15"
     Site            535..540
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          537..761
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cl02488"
                     /db_xref="CDD:413338"
     Region          651..760
                     /region_name="repeat region 16"
     Site            653..658
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          761..867
                     /region_name="repeat region 17"
     Region          764..979
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          868..977
                     /region_name="repeat region 18"
     Site            order(868..870,872..874)
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          978..1082
                     /region_name="repeat region 19"
     Region          980..1238
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cl02488"
                     /db_xref="CDD:413338"
     Region          1083..1129
                     /region_name="hinge region 3"
     Site            1128..1133
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1130..1236
                     /region_name="repeat region 20"
     Region          1131..1347
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          1237..1345
                     /region_name="repeat region 21"
     Site            1237..1242
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1346..1461
                     /region_name="repeat region 22"
     Region          1349..1592
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          1462..1590
                     /region_name="repeat region 23"
     Site            1462..1467
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1591..1699
                     /region_name="repeat region 24"
     Region          1593..1699
                     /region_name="Spectrin"
                     /note="Spectrin repeat; pfam00435"
                     /db_xref="CDD:395348"
     Region          1673..1771
                     /region_name="hinge region 4"
     Site            1700..1704
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1715..1751
                     /region_name="WW-domain"
     Region          1718..1747
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(1731,1742)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Site            1739..2067
                     /site_type="binding"
                     /note="dystroglycan binding site"
     Region          1759..1959
                     /region_name="Cysteine-rich domain"
     Region          1784..1945
                     /region_name="EFh_DMD"
                     /note="EF-hand-like motif found in dystrophin; cd16246"
                     /db_xref="CDD:320004"
     Site            order(1784..1785,1787..1788,1806,1810,1814,1816..1817,
                     1820,1831..1837,1839..1840,1843,1849,1862,1903..1904,1906)
                     /site_type="other"
                     /note="Domain interface"
                     /db_xref="CDD:320004"
     Region          1784..1823
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          1789..1816
                     /region_name="EF-hand 1"
     Region          1830..1864
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          1837..1865
                     /region_name="EF-hand 2"
     Site            1847..1849
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:320004"
     Region          1870..1906
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          1919..1945
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          1959..2344
                     /region_name="Carboxy-terminal region"
     Region          1966..2013
                     /region_name="ZZ-domain"
     Region          1970..2018
                     /region_name="ZZ_dystrophin"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     dystrophin and dystrobrevin. The ZZ motif coordinates two
                     zinc ions and most likely participates in ligand binding
                     or molecular scaffolding. Dystrophin attaches actin
                     filaments to an integral membrane...; cd02334"
                     /db_xref="CDD:239074"
     Site            order(1972,1975,1987,1990,1996,1999,2009,2013)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(1972,1975,1996,1999)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(1973,1984,1986,1992,1994)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(1985,2000,2015,2018)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(1987,1990,2009,2013)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239074"
     Site            2103..2153
                     /site_type="binding"
                     /note="alpha1-syntrophin binding site"
     Site            2154..2194
                     /site_type="binding"
                     /note="beta1-syntrophin binding site"
     Region          2217..2252
                     /region_name="(Leu)6-heptad repeat"
     CDS             1..2344
                     /gene="DMD"
                     /gene_synonym="BMD; CMD3B; DXS142; DXS164; DXS206; DXS230;
                     DXS239; DXS268; DXS269; DXS270; DXS272; MRX85"
                     /coded_by="NM_004011.4:20..7054"
                     /note="isoform Dp260-1 is encoded by transcript variant
                     Dp260-1"
                     /db_xref="GeneID:1756"
                     /db_xref="HGNC:HGNC:2928"
                     /db_xref="MIM:300377"
ORIGIN      
        1 mtemilliff payflnavrr qklleqsiqs aqetekslhl iqesltfidk qlaayiadkv
       61 daaqmpqeaq kiqsdltshe isleemkkhn qgkeaaqrvl sqidvaqkkl qdvsmkfrlf
      121 qkpanfeqrl qeskmildev kmhlpaletk sveqevvqsq lnhcvnlyks lsevksevem
      181 viktgrqivq kkqtenpkel dervtalklh ynelgakvte rkqqlekclk lsrkmrkemn
      241 vltewlaatd meltkrsave gmpsnldsev awgkatqkei ekqkvhlksi tevgealktv
      301 lgkketlved klsllnsnwi avtsraeewl nllleyqkhm etfdqnvdhi tkwiiqadtl
      361 ldesekkkpq qkedvlkrlk aelndirpkv dstrdqaanl manrgdhcrk lvepqiseln
      421 hrfaaishri ktgkasiplk eleqfnsdiq kllepleaei qqgvnlkeed fnkdmnedne
      481 gtvkellqrg dnlqqritde rkreeikikq qllqtkhnal kdlrsqrrkk aleishqwyq
      541 ykrqaddllk clddiekkla slpeprderk ikeidrelqk kkeelnavrr qaeglsedga
      601 amaveptqiq lskrwreies kfaqfrrlnf aqihtvreet mmvmtedmpl eisyvpstyl
      661 teithvsqal leveqllnap dlcakdfedl fkqeeslkni kdslqqssgr idiihskkta
      721 alqsatpver vklqealsql dfqwekvnkm ykdrqgrfdr svekwrrfhy dikifnqwlt
      781 eaeqflrktq ipenwehaky kwylkelqdg igqrqtvvrt lnatgeeiiq qssktdasil
      841 qeklgslnlr wqevckqlsd rkkrleeqkn ilsefqrdln efvlwleead niasiplepg
      901 keqqlkekle qvkllveelp lrqgilkqln etggpvlvsa pispeeqdkl enklkqtnlq
      961 wikvsralpe kqgeieaqik dlgqlekkle dleeqlnhll lwlspirnql eiynqpnqeg
     1021 pfdvketeia vqakqpdvee ilskgqhlyk ekpatqpvkr kledlssewk avnrllqelr
     1081 akqpdlapgl ttigasptqt vtlvtqpvvt ketaisklem psslmlevpa ladfnrawte
     1141 ltdwlslldq viksqrvmvg dledinemii kqkatmqdle qrrpqleeli taaqnlknkt
     1201 snqeartiit drieriqnqw devqehlqnr rqqlnemlkd stqwleakee aeqvlgqara
     1261 kleswkegpy tvdaiqkkit etkqlakdlr qwqtnvdvan dlalkllrdy saddtrkvhm
     1321 iteninaswr sihkrvsere aaleethrll qqfpldlekf lawlteaett anvlqdatrk
     1381 erlledskgv kelmkqwqdl qgeieahtdv yhnldensqk ilrslegsdd avllqrrldn
     1441 mnfkwselrk kslnirshle assdqwkrlh lslqellvwl qlkddelsrq apiggdfpav
     1501 qkqndvhraf krelktkepv imstletvri flteqplegl eklyqeprel ppeeraqnvt
     1561 rllrkqaeev nteweklnlh sadwqrkide tlerlrelqe atdeldlklr qaevikgswq
     1621 pvgdllidsl qdhlekvkal rgeiaplken vshvndlarq lttlgiqlsp ynlstledln
     1681 trwkllqvav edrvrqlhea hrdfgpasqh flstsvqgpw eraispnkvp yyinhetqtt
     1741 cwdhpkmtel yqsladlnnv rfsayrtamk lrrlqkalcl dllslsaacd aldqhnlkqn
     1801 dqpmdilqii nclttiydrl eqehnnlvnv plcvdmclnw llnvydtgrt grirvlsfkt
     1861 giislckahl edkyrylfkq vasstgfcdq rrlglllhds iqiprqlgev asfggsniep
     1921 svrscfqfan nkpeieaalf ldwmrlepqs mvwlpvlhrv aaaetakhqa kcnickecpi
     1981 igfryrslkh fnydicqscf fsgrvakghk mhypmveyct pttsgedvrd fakvlknkfr
     2041 tkryfakhpr mgylpvqtvl egdnmetpvt linfwpvdsa passpqlshd dthsriehya
     2101 srlaemensn gsylndsisp nesiddehll iqhycqslnq dsplsqprsp aqilislese
     2161 ergelerila dleeenrnlq aeydrlkqqh ehkglsplps ppemmptspq sprdaeliae
     2221 akllrqhkgr learmqiled hnkqlesqlh rlrqlleqpq aeakvngttv sspstslqrs
     2281 dssqpmllrv vgsqtsdsmg eedllsppqd tstgleevme qlnnsfpssr grntpgkpmr
     2341 edtm
//
LOCUS       NP_000158                524 aa            linear   PRI 21-NOV-2025
DEFINITION  glycerol kinase isoform b [Homo sapiens].
ACCESSION   NP_000158
VERSION     NP_000158.1
DBSOURCE    REFSEQ: accession NM_000167.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Ying,F., Chen,X. and Lv,L.
  TITLE     Glycerol kinase enzyme is a prognostic predictor in esophageal
            carcinoma and is associated with immune cell infiltration
  JOURNAL   Sci Rep 14 (1), 3922 (2024)
   PUBMED   38365953
  REMARK    GeneRIF: Glycerol kinase enzyme is a prognostic predictor in
            esophageal carcinoma and is associated with immune cell
            infiltration.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Rani,R.M., Syngkli,S., Nongkhlaw,J. and Das,B.
  TITLE     Expression and characterisation of human glycerol kinase: the role
            of solubilising agents and molecular chaperones
  JOURNAL   Biosci Rep 43 (4) (2023)
   PUBMED   37021775
  REMARK    GeneRIF: Expression and characterisation of human glycerol kinase:
            the role of solubilising agents and molecular chaperones.
            Erratum:[Biosci Rep. 2023 Oct 31;43(10):BSR-2022-2258_COR. doi:
            10.1042/BSR-2022-2258_COR. PMID: 37860917]
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 524)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 524)
  AUTHORS   Sargent,C.A., Young,C., Marsh,S., Ferguson-Smith,M.A. and
            Affara,N.A.
  TITLE     The glycerol kinase gene family: structure of the Xp gene, and
            related intronless retroposons
  JOURNAL   Hum Mol Genet 3 (8), 1317-1324 (1994)
   PUBMED   7987308
REFERENCE   7  (residues 1 to 524)
  AUTHORS   Achermann,J.C. and Vilain,E.J.
  TITLE     NR0B1-Related Adrenal Hypoplasia Congenita
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301604
REFERENCE   8  (residues 1 to 524)
  AUTHORS   Love,D.R., Bloomfield,J.F., Kenwrick,S.J., Yates,J.R. and
            Davies,K.E.
  TITLE     Physical mapping distal to the DMD locus
  JOURNAL   Genomics 8 (1), 106-112 (1990)
   PUBMED   2081587
REFERENCE   9  (residues 1 to 524)
  AUTHORS   Pillers,D.A., Weleber,R.G., Powell,B.R., Hanna,C.E., Magenis,R.E.
            and Buist,N.R.
  TITLE     Aland Island eye disease (Forsius-Eriksson ocular albinism) and an
            Xp21 deletion in a patient with Duchenne muscular dystrophy,
            glycerol kinase deficiency, and congenital adrenal hypoplasia
  JOURNAL   Am J Med Genet 36 (1), 23-28 (1990)
   PUBMED   2159212
REFERENCE   10 (residues 1 to 524)
  AUTHORS   Kaneko,M., Kurokawa,M. and Ishibashi,S.
  TITLE     Binding and function of mitochondrial glycerol kinase in comparison
            with those of mitochondrial hexokinase
  JOURNAL   Arch Biochem Biophys 237 (1), 135-141 (1985)
   PUBMED   2982325
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC042421.1, AK313215.1,
            AK294938.1, AA689298.1, AC112496.2 and AW300142.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the FGGY
            kinase family. This protein is a key enzyme in the regulation of
            glycerol uptake and metabolism. It catalyzes the phosphorylation of
            glycerol by ATP, yielding ADP and glycerol-3-phosphate. Mutations
            in this gene are associated with glycerol kinase deficiency (GKD).
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Mar
            2011].
            
            Transcript Variant: This variant (2) lacks an in-frame coding exon
            compared to variant 1. This results in a shorter isoform (b)
            missing a 6 aa protein segment compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2011722.1, AK313215.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp21.2"
     Protein         1..524
                     /product="glycerol kinase isoform b"
                     /EC_number="2.7.1.30"
                     /note="ATP:glycerol 3-phosphotransferase; glycerokinase"
                     /calculated_mol_wt=57358
     Region          11..510
                     /region_name="ASKHA_NBD_FGGY_GK1-3-like"
                     /note="nucleotide-binding domain (NBD) of metazoan
                     glycerol kinase 1-3 (GK1-3) and similar proteins; cd07792"
                     /db_xref="CDD:466802"
     CDS             1..524
                     /gene="GK"
                     /gene_synonym="GK1; GKD"
                     /coded_by="NM_000167.6:116..1690"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS35224.1"
                     /db_xref="GeneID:2710"
                     /db_xref="HGNC:HGNC:4289"
                     /db_xref="MIM:300474"
ORIGIN      
        1 maaskkavlg plvgavdqgt sstrflvfns ktaellshhq veikqefpre gwveqdpkei
       61 lhsvyeciek tceklgqlni disnikaigv snqrettvvw dkitgeplyn avvwldlrtq
      121 stveslskri pgnnnfvksk tglplstyfs avklrwlldn vrkvqkavee kralfgtids
      181 wliwsltggv nggvhctdvt nasrtmlfni hslewdkqlc effgipmeil pnvrssseiy
      241 glmkagaleg vpisgclgdq saalvgqmcf qigqakntyg tgcfllcntg hkcvfsdhgl
      301 lttvayklgr dkpvyyaleg svaiagavir wlrdnlgiik tseeieklak evgtsygcyf
      361 vpafsglyap ywepsargii cgltqftnkc hiafaaleav cfqtreilda mnrdcgipls
      421 hlqvdggmts nkilmqlqad ilyipvvkps mpettalgaa maagaaegvg vwslepedls
      481 avtmerfepq inaeeseiry stwkkavmks mgwvttqspe sgip
//
LOCUS       NP_001305446             619 aa            linear   PRI 21-NOV-2025
DEFINITION  cell division cycle protein 16 homolog isoform 2 [Homo sapiens].
ACCESSION   NP_001305446 XP_005266261
VERSION     NP_001305446.1
DBSOURCE    REFSEQ: accession NM_001318517.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Hu,F., Fong,K.O., Cheung,M.P.L., Liu,J.A., Liang,R., Li,T.W.,
            Sharma,R., Ip,P.P., Yang,X. and Cheung,M.
  TITLE     DEPDC1B Promotes Melanoma Angiogenesis and Metastasis through
            Sequestration of Ubiquitin Ligase CDC16 to Stabilize Secreted
            SCUBE3
  JOURNAL   Adv Sci (Weinh) 9 (10), e2105226 (2022)
   PUBMED   35088579
  REMARK    GeneRIF: DEPDC1B Promotes Melanoma Angiogenesis and Metastasis
            through Sequestration of Ubiquitin Ligase CDC16 to Stabilize
            Secreted SCUBE3.
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 619)
  AUTHORS   Wu,H., Zhang,X., Shen,Q., Liu,Y., Gao,Y., Wang,G., Lv,M., Hua,R.,
            Xu,Y., Zhou,P., Wei,Z., Tao,F., He,X., Cao,Y. and Liu,M.
  TITLE     A homozygous loss-of-function mutation in FBXO43 causes human
            non-obstructive azoospermia
  JOURNAL   Clin Genet 101 (1), 55-64 (2022)
   PUBMED   34595750
REFERENCE   5  (residues 1 to 619)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 619)
  AUTHORS   Grossberger,R., Gieffers,C., Zachariae,W., Podtelejnikov,A.V.,
            Schleiffer,A., Nasmyth,K., Mann,M. and Peters,J.M.
  TITLE     Characterization of the DOC1/APC10 subunit of the yeast and the
            human anaphase-promoting complex
  JOURNAL   J Biol Chem 274 (20), 14500-14507 (1999)
   PUBMED   10318877
REFERENCE   7  (residues 1 to 619)
  AUTHORS   Kallio,M., Weinstein,J., Daum,J.R., Burke,D.J. and Gorbsky,G.J.
  TITLE     Mammalian p55CDC mediates association of the spindle checkpoint
            protein Mad2 with the cyclosome/anaphase-promoting complex, and is
            involved in regulating anaphase onset and late mitotic events
  JOURNAL   J Cell Biol 141 (6), 1393-1406 (1998)
   PUBMED   9628895
REFERENCE   8  (residues 1 to 619)
  AUTHORS   Yu,H., Peters,J.M., King,R.W., Page,A.M., Hieter,P. and
            Kirschner,M.W.
  TITLE     Identification of a cullin homology region in a subunit of the
            anaphase-promoting complex
  JOURNAL   Science 279 (5354), 1219-1222 (1998)
   PUBMED   9469815
REFERENCE   9  (residues 1 to 619)
  AUTHORS   Ollendorff,V. and Donoghue,D.J.
  TITLE     The serine/threonine phosphatase PP5 interacts with CDC16 and
            CDC27, two tetratricopeptide repeat-containing subunits of the
            anaphase-promoting complex
  JOURNAL   J Biol Chem 272 (51), 32011-32018 (1997)
   PUBMED   9405394
REFERENCE   10 (residues 1 to 619)
  AUTHORS   Tugendreich,S., Tomkiel,J., Earnshaw,W. and Hieter,P.
  TITLE     CDC27Hs colocalizes with CDC16Hs to the centrosome and mitotic
            spindle and is essential for the metaphase to anaphase transition
  JOURNAL   Cell 81 (2), 261-268 (1995)
   PUBMED   7736578
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC391369.1, AK315302.1,
            U18291.1 and BM663581.1.
            
            On Jan 8, 2016 this sequence version replaced XP_005266261.1.
            
            Summary: The protein encoded by this gene functions as a protein
            ubiquitin ligase and is a component of the multiprotein APC
            complex. The APC complex is a cyclin degradation system that
            governs exit from mitosis by targeting cell cycle proteins for
            degredation by the 26S proteasome. Each component protein of the
            APC complex is highly conserved among eukaryotic organisms. This
            protein, and other APC complex proteins, contain a
            tetratricopeptide repeat (TPR) domain; a protein domain that is
            often involved in protein-protein interactions and the assembly of
            multiprotein complexes. Multiple alternatively spliced transcript
            variants, encoding distinct proteins, have been identified.
            [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice acceptor site in the 5' coding region and lacks an exon
            segment in the 3' UTR, compared to variant 2. Variants 3 and 5
            encode the same isoform (2), which is one amino acid shorter than
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U18291.1, SRR14038197.964418.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..619
                     /product="cell division cycle protein 16 homolog isoform
                     2"
                     /note="cell division cycle protein 16 homolog; cell
                     division cycle 16 homolog; anaphase-promoting complex,
                     subunit 6; cyclosome subunit 6"
                     /calculated_mol_wt=71396
     Region          4..33
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          15..93
                     /region_name="ANAPC3"
                     /note="Anaphase-promoting complex, cyclosome, subunit 3;
                     pfam12895"
                     /db_xref="CDD:463743"
     Region          36..64
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          36..61
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          69..93
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          69..92
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     Region          127..158
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          163..186
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          197..221
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          231..259
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          266..293
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          274..>439
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          297..328
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          298..328
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          333..361
                     /region_name="TPR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          335..361
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          366..396
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          368..396
                     /region_name="TPR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          372..>521
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          401..433
                     /region_name="TPR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          401..429
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(402,405..406,409..410,412,436,448..449,452..453,
                     455..456,479,482..483,486..487,490)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          434..473
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          441..473
                     /region_name="TPR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          478..507
                     /region_name="TPR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          478..505
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     Site            559
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     Region          573..598
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Site            580
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     CDS             1..619
                     /gene="CDC16"
                     /gene_synonym="ANAPC6; APC6; CDC16Hs; CUT9"
                     /coded_by="NM_001318517.3:189..2048"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS81786.1"
                     /db_xref="GeneID:8881"
                     /db_xref="HGNC:HGNC:1720"
                     /db_xref="MIM:603461"
ORIGIN      
        1 mnlerlrkrv rqyldqqqyq salfwadkva slsrepqdiy wlaqclylta qyhraahalr
       61 srkldklyea crylaarchy aakehqqald vldmeepink rlfekylkde sgfkdpssdw
      121 emsqssikss icllrgkiyd aldnrtlaty sykealkldv ycfeafdllt shhmltaqee
      181 kelleslpls klcneeqell rflfenklkk ynkpsetvip esvdglqenl dvvvslaerh
      241 yyncdfkmcy kltsvvmekd pfhasclpvh igtlvelnka nelfylshkl vdlypsnpvs
      301 wfavgcyylm vghkneharr ylskattlek tygpawiayg hsfavesehd qamaayftaa
      361 qlmkgchlpm lyigleyglt nnsklaerff sqalsiaped pfvmhevgvv afqngewkta
      421 ekwfldalek ikaignevtv dkwepllnnl ghvcrklkky aealdyhrqa lvlipqnast
      481 ysaigyihsl mgnfenavdy fhtalglrrd dtfsvtmlgh ciemyigdse ayigadikdk
      541 lkcydfdvht mktlkniisp pwdfrefeve kqtaeetglt pletsrktpd srpsleetfe
      601 iemnesdmml etsmsdhst
//
LOCUS       NP_004195                581 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
            isoform 2 [Homo sapiens].
ACCESSION   NP_004195
VERSION     NP_004195.2
DBSOURCE    REFSEQ: accession NM_004204.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Shekhar,B.R., Rupani,K., Parkar,S.R., Nayak,A.S., Kumbhar,B.V.,
            Khare,S.P., Menon,S., Gawde,H. and Das,D.K.
  TITLE     Identifying novel risk conferring genes involved in glycosylation
            processes with familial schizophrenia in an Indian cohort:
            Prediction of ADAMTS9 gene variant for structural stability
  JOURNAL   Gene 872, 147443 (2023)
   PUBMED   37105505
  REMARK    GeneRIF: Identifying novel risk conferring genes involved in
            glycosylation processes with familial schizophrenia in an Indian
            cohort: Prediction of ADAMTS9 gene variant for structural
            stability.
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 581)
  AUTHORS   Johnstone,D.L., Nguyen,T.T.M., Zambonin,J., Kernohan,K.D.,
            St-Denis,A., Baratang,N.V., Hartley,T., Geraghty,M.T., Richer,J.,
            Majewski,J., Bareke,E., Guerin,A., Pendziwiat,M., Pena,L.D.M.,
            Braakman,H.M.H., Gripp,K.W., Edmondson,A.C., He,M., Spillmann,R.C.,
            Eklund,E.A., Bayat,A., McMillan,H.J., Boycott,K.M. and Campeau,P.M.
  TITLE     Early infantile epileptic encephalopathy due to biallelic
            pathogenic variants in PIGQ: Report of seven new subjects and
            review of the literature
  JOURNAL   J Inherit Metab Dis 43 (6), 1321-1332 (2020)
   PUBMED   32588908
  REMARK    Review article
            Erratum:[J Inherit Metab Dis. 2023 Jan;46(1):156. doi:
            10.1002/jimd.12362. PMID: 36646502]
REFERENCE   5  (residues 1 to 581)
  AUTHORS   Wang,X., Lopez,O.L., Sweet,R.A., Becker,J.T., DeKosky,S.T.,
            Barmada,M.M., Demirci,F.Y. and Kamboh,M.I.
  TITLE     Genetic determinants of disease progression in Alzheimer's disease
  JOURNAL   J Alzheimers Dis 43 (2), 649-655 (2015)
   PUBMED   25114068
  REMARK    GeneRIF: Genome-wide association analyses identified four
            suggestive loci (PAX3, CCRN4L, PIGQ, and ADAM19)determinants of
            disease progression in Alzheimer's disease
REFERENCE   6  (residues 1 to 581)
  AUTHORS   Kinoshita,T. and Inoue,N.
  TITLE     Dissecting and manipulating the pathway for
            glycosylphos-phatidylinositol-anchor biosynthesis
  JOURNAL   Curr Opin Chem Biol 4 (6), 632-638 (2000)
   PUBMED   11102867
  REMARK    Review article
REFERENCE   7  (residues 1 to 581)
  AUTHORS   Watanabe,R., Murakami,Y., Marmor,M.D., Inoue,N., Maeda,Y., Hino,J.,
            Kangawa,K., Julius,M. and Kinoshita,T.
  TITLE     Initial enzyme for glycosylphosphatidylinositol biosynthesis
            requires PIG-P and is regulated by DPM2
  JOURNAL   EMBO J 19 (16), 4402-4411 (2000)
   PUBMED   10944123
REFERENCE   8  (residues 1 to 581)
  AUTHORS   Hong,Y., Ohishi,K., Watanabe,R., Endo,Y., Maeda,Y. and Kinoshita,T.
  TITLE     GPI1 stabilizes an enzyme essential in the first step of
            glycosylphosphatidylinositol biosynthesis
  JOURNAL   J Biol Chem 274 (26), 18582-18588 (1999)
   PUBMED   10373468
REFERENCE   9  (residues 1 to 581)
  AUTHORS   Tiede,A., Schubert,J., Nischan,C., Jensen,I., Westfall,B.,
            Taron,C.H., Orlean,P. and Schmidt,R.E.
  TITLE     Human and mouse Gpi1p homologues restore
            glycosylphosphatidylinositol membrane anchor biosynthesis in yeast
            mutants
  JOURNAL   Biochem J 334 (Pt 3) (Pt 3), 609-616 (1998)
   PUBMED   9729469
REFERENCE   10 (residues 1 to 581)
  AUTHORS   Watanabe,R., Inoue,N., Westfall,B., Taron,C.H., Orlean,P.,
            Takeda,J. and Kinoshita,T.
  TITLE     The first step of glycosylphosphatidylinositol biosynthesis is
            mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1
  JOURNAL   EMBO J 17 (4), 877-885 (1998)
   PUBMED   9463366
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA206420.1, BC006377.2,
            AB003723.1 and AK314361.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 29, 2002 this sequence version replaced NP_004195.1.
            
            Summary: This gene is involved in the first step in
            glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The
            GPI-anchor is a glycolipid found on many blood cells and serves to
            anchor proteins to the cell surface. This gene encodes a
            N-acetylglucosaminyl transferase component that is part of the
            complex that catalyzes transfer of N-acetylglucosamine (GlcNAc)
            from UDP-GlcNAc to phosphatidylinositol (PI). Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (2) has an additional exon in the
            3' coding region, which results in a frameshift and an early stop
            codon, compared to variant 1. The encoded isoform (2) is shorter
            and has a distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3645385.1, AB003723.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321878.10/ ENSP00000326674.6
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..581
                     /product="phosphatidylinositol
                     N-acetylglucosaminyltransferase subunit Q isoform 2"
                     /EC_number="2.4.1.198"
                     /note="N-acetylglucosaminyl transferase component Gpi1;
                     phosphatidylinositol glycan, class Q; phosphatidylinositol
                     N-acetylglucosaminyltransferase subunit Q;
                     N-acetylglucosamyl transferase component GPI1; c407A10.1
                     (GPI1 (N-acetylglucosaminyl transferase component));
                     PIG-Q; phosphatidylinositol-glycan biosynthesis class Q
                     protein"
                     /calculated_mol_wt=65213
     Region          247..509
                     /region_name="Gpi1"
                     /note="N-acetylglucosaminyl transferase component (Gpi1);
                     pfam05024"
                     /db_xref="CDD:461527"
     Site            278..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRB3.3)"
     Site            349..371
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRB3.3)"
     Site            378..400
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRB3.3)"
     Site            446..468
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRB3.3)"
     Site            475..497
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRB3.3)"
     CDS             1..581
                     /gene="PIGQ"
                     /gene_synonym="c407A10.1; DEE77; EIEE77; GPI1; GPIBD19;
                     MCAHS4"
                     /coded_by="NM_004204.5:139..1884"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10412.1"
                     /db_xref="GeneID:9091"
                     /db_xref="HGNC:HGNC:14135"
                     /db_xref="MIM:605754"
ORIGIN      
        1 mvlkaffptc cvstdsgllv grwvpeqssa vvlavlhfpf ipiqvkqlla qvrqasqvgv
       61 avlgtwchcr qepeeslgrf leslgavfph epwlrlcrer ggtfwsceat hrqaptapga
      121 pgedqvmlif ydqrqvllsq lhlptvlpdr qagattastg glaavfdtva rsevlfrsdr
      181 fdegpvrlsh wqsegveasi laelarrasg piclllasll slvsavsacr vfklwplsfl
      241 gsklstceql rhrlehltli fstrkaenpa qlmrkantva svlldvalgl mllswlhgrs
      301 righladalv pvadhvaeel qhllqwlmga paglkmnral dqvlgrffly hihlwisyih
      361 lmspfvehil whvglsaclg ltvalsllsd iialltfhiy cfyvygarly clkihglssl
      421 wrlfrgkkwn vlrqrvdscs ydldqlfigt llftillfll pttalyylvf tllrllvvav
      481 qglihllvdl inslplyslg lrlcrpyrla agvkfrvlrh eagrplrllm qinplpysrv
      541 vhtyrlpscg chpkhswgal crklflgeli ypwrqrgdkq d
//
LOCUS       NP_003771                372 aa            linear   PRI 21-NOV-2025
DEFINITION  beta-1,4-galactosyltransferase 2 isoform b [Homo sapiens].
ACCESSION   NP_003771
VERSION     NP_003771.1
DBSOURCE    REFSEQ: accession NM_003780.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Pallet,N., Belleville-Rolland,T., Savalle,A., Lejeune,M., Mauge,L.,
            Bertil,S., Loriot,M.A. and Gaussem,P.
  TITLE     Beta-1,4-galactosyltransferase 2 c.909C>T gene variant is
            predictive of on-clopidogrel platelet reactivity
  JOURNAL   Pharmacogenomics 19 (12), 937-945 (2018)
   PUBMED   30020015
  REMARK    GeneRIF: In individuals under dual antiplatelet therapy, B4GALT2
            c.909C>T is an independent genetic predictor of on-treatment
            platelet reactivity.
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Dekkers,G., Plomp,R., Koeleman,C.A., Visser,R., von Horsten,H.H.,
            Sandig,V., Rispens,T., Wuhrer,M. and Vidarsson,G.
  TITLE     Multi-level glyco-engineering techniques to generate IgG with
            defined Fc-glycans
  JOURNAL   Sci Rep 6, 36964 (2016)
   PUBMED   27872474
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Venkitachalam,S., Revoredo,L., Varadan,V., Fecteau,R.E., Ravi,L.,
            Lutterbaugh,J., Markowitz,S.D., Willis,J.E., Gerken,T.A. and
            Guda,K.
  TITLE     Biochemical and functional characterization of
            glycosylation-associated mutational landscapes in colon cancer
  JOURNAL   Sci Rep 6, 23642 (2016)
   PUBMED   27004849
  REMARK    GeneRIF: Study provides evidence that mutations in B3GNT2, B4GALT2,
            and ST6GALNAC2 underlie aberrant glycosylation, and contribute to
            the pathogenesis of molecular subsets of colon and other
            gastrointestinal malignancies.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Brockhausen,I., Dowler,T. and Paulsen,H.
  TITLE     Site directed processing: role of amino acid sequences and
            glycosylation of acceptor glycopeptides in the assembly of extended
            mucin type O-glycan core 2
  JOURNAL   Biochim Biophys Acta 1790 (10), 1244-1257 (2009)
   PUBMED   19524017
  REMARK    GeneRIF: Data show that Beta4-Gal-transferase (beta4GalT) extends
            core 2 and forms the backbone structure for biologically important
            epitopes.
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Guo,S., Sato,T., Shirane,K. and Furukawa,K.
  TITLE     Galactosylation of N-linked oligosaccharides by human
            beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed
            in Sf-9 cells
  JOURNAL   Glycobiology 11 (10), 813-820 (2001)
   PUBMED   11588157
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Amado,M., Almeida,R., Schwientek,T. and Clausen,H.
  TITLE     Identification and characterization of large galactosyltransferase
            gene families: galactosyltransferases for all functions
  JOURNAL   Biochim Biophys Acta 1473 (1), 35-53 (1999)
   PUBMED   10580128
  REMARK    Review article
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Lo,N.W., Shaper,J.H., Pevsner,J. and Shaper,N.L.
  TITLE     The expanding beta 4-galactosyltransferase gene family: messages
            from the databanks
  JOURNAL   Glycobiology 8 (5), 517-526 (1998)
   PUBMED   9597550
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Almeida,R., Amado,M., David,L., Levery,S.B., Holmes,E.H., Merkx,G.,
            van Kessel,A.G., Rygaard,E., Hassan,H., Bennett,E. and Clausen,H.
  TITLE     A family of human beta4-galactosyltransferases. Cloning and
            expression of two novel UDP-galactose:beta-n-acetylglucosamine
            beta1, 4-galactosyltransferases, beta4Gal-T2 and beta4Gal-T3
  JOURNAL   J Biol Chem 272 (51), 31979-31991 (1997)
   PUBMED   9405390
  REMARK    Erratum:[J Biol Chem 1998 Jul 17;273(29):18674]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL535811.3, AK095873.1 and
            BC096821.1.
            
            Summary: This gene is one of seven beta-1,4-galactosyltransferase
            (beta4GalT) genes. They encode type II membrane-bound glycoproteins
            that appear to have exclusive specificity for the donor substrate
            UDP-galactose; all transfer galactose in a beta1,4 linkage to
            similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a
            distinct function in the biosynthesis of different glycoconjugates
            and saccharide structures. As type II membrane proteins, they have
            an N-terminal hydrophobic signal sequence that directs the protein
            to the Golgi apparatus and which then remains uncleaved to function
            as a transmembrane anchor. By sequence similarity, the beta4GalTs
            form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and
            beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. The enzyme
            encoded by this gene synthesizes N-acetyllactosamine in glycolipids
            and glycoproteins. Its substrate specificity is affected by
            alpha-lactalbumin but it is not expressed in lactating mammary
            tissue. Three transcript variants encoding two different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2011].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (b) is
            shorter at the N-terminus compared to isoform a. Variants 2 and 3
            both encode isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC096821.1, SRR18074967.3258074.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372324.6/ ENSP00000361399.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..372
                     /product="beta-1,4-galactosyltransferase 2 isoform b"
                     /EC_number="2.4.1.22"
                     /EC_number="2.4.1.90"
                     /EC_number="2.4.1.38"
                     /note="beta-4-GalT2; beta-N-acetylglucosaminyl-glycolipid
                     beta-1,4-galactosyltransferase 2; UDP-Gal:betaGlcNAc beta
                     1,4- galactosyltransferase 2; UDP-Gal:betaGlcNAc beta
                     1,4-galactosyltransferase, polypeptide 2; beta-1,4-GalTase
                     2; UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2;
                     UDP-galactose:beta-N-acetylglucosamine
                     beta-1,4-galactosyltransferase 2; nal synthase; lactose
                     synthase A protein; N-acetyllactosamine synthase;
                     beta-N-acetylglucosaminylglycopeptide
                     beta-1,4-galactosyltransferase"
                     /calculated_mol_wt=41841
     Site            16..36
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60909.1)"
     Region          56..97
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60909.1)"
     Site            66
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60909.1)"
     Site            71
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60909.1)"
     Region          145..361
                     /region_name="b4GalT"
                     /note="Beta-4-Galactosyltransferase is involved in the
                     formation of the poly-N-acetyllactosamine core structures
                     present in glycoproteins and glycosphingolipids; cd00899"
                     /db_xref="CDD:132999"
     Site            order(150,152,154,189,216..218)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:132999"
     Site            order(216,218,311)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:132999"
     Site            357
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60909.1)"
     CDS             1..372
                     /gene="B4GALT2"
                     /gene_synonym="B4Gal-T2; B4Gal-T3; beta4Gal-T2"
                     /coded_by="NM_003780.5:355..1473"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS506.1"
                     /db_xref="GeneID:8704"
                     /db_xref="HGNC:HGNC:925"
                     /db_xref="MIM:604013"
ORIGIN      
        1 msrllggtle rvckavlllc llhflvavil yfdvyaqhla ffsrfsargp ahalhpaass
       61 sssssncsrp natasssglp evpsalpgpt aptlppcpds ppglvgrlli eftspmpler
      121 vqrenpgvlm ggrytppdct paqtvaviip frhrehhlry wlhylhpilr rqrlrygvyv
      181 inqhgedtfn rakllnvgfl ealkedaayd cfifsdvdlv pmddrnlyrc gdqprhfaia
      241 mdkfgfrlpy agyfggvsgl skaqflring fpneywgwgg edddifnris ltgmkisrpd
      301 irigryrmik hdrdkhnepn pqrftkiqnt kltmkrdgig svryqvlevs rqplftnitv
      361 digrppswpp rg
//
LOCUS       NP_001362505             258 aa            linear   PRI 21-NOV-2025
DEFINITION  cAMP-dependent protein kinase catalytic subunit beta isoform 25
            [Homo sapiens].
ACCESSION   NP_001362505 XP_016857202
VERSION     NP_001362505.1
DBSOURCE    REFSEQ: accession NM_001375576.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Tanaka,M., Takeshita,K., Kunita,A., Hasegawa,K. and Ushiku,T.
  TITLE     PRKACA/PRKACB Fusions in Pancreatobiliary Intraductal Oncocytic
            Papillary Neoplasms Including Those With Atypical Morphology: An
            Analysis of 22 Cases Expanding Morphologic Spectrum
  JOURNAL   Am J Surg Pathol 48 (8), 1032-1040 (2024)
   PUBMED   38841868
  REMARK    GeneRIF: PRKACA/PRKACB Fusions in Pancreatobiliary Intraductal
            Oncocytic Papillary Neoplasms Including Those With Atypical
            Morphology: An Analysis of 22 Cases Expanding Morphologic Spectrum.
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Pei,W., Yin,W., Yu,T., Zhang,X., Zhang,Q., Yang,X., Shi,C., Shen,W.
            and Liu,G.
  TITLE     Dual-Specificity Phosphatase 4 Promotes Malignant Features in
            Colorectal Cancer Through Cyclic-AMP Response Element Binding
            Protein/Protein Kinase CAMP-Activated Catalytic Subunit Beta
            Activation
  JOURNAL   Dig Dis Sci 69 (8), 2856-2874 (2024)
   PUBMED   38824257
  REMARK    GeneRIF: Dual-Specificity Phosphatase 4 Promotes Malignant Features
            in Colorectal Cancer Through Cyclic-AMP Response Element Binding
            Protein/Protein Kinase CAMP-Activated Catalytic Subunit Beta
            Activation.
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Itoh,T., Omori,Y., Seino,M., Hirose,K., Date,F., Ono,Y.,
            Mizukami,Y., Aoki,S., Ishida,M., Mizuma,M., Morikawa,T.,
            Higuchi,R., Honda,G., Okamura,Y., Kinoshita,K., Unno,M. and
            Furukawa,T.
  TITLE     Gene Rearrangement and Expression of PRKACA and PRKACB Govern
            Morphobiology of Pancreatobiliary Oncocytic Neoplasms
  JOURNAL   Mod Pathol 37 (1), 100358 (2024)
   PUBMED   37871652
  REMARK    GeneRIF: Gene Rearrangement and Expression of PRKACA and PRKACB
            Govern Morphobiology of Pancreatobiliary Oncocytic Neoplasms.
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Maimaitiaili,Y., Fukumura,Y., Hirabayashi,K., Kinowaki,Y.,
            Naito,Y., Saito,A., Rong,L., Nakahodo,J. and Yao,T.
  TITLE     Investigation of -PRKACA/-PRKACB fusion genes in oncocytic tumors
            of the pancreatobiliary and other systems
  JOURNAL   Virchows Arch 481 (6), 865-876 (2022)
   PUBMED   36152045
  REMARK    GeneRIF: Investigation of -PRKACA/-PRKACB fusion genes in oncocytic
            tumors of the pancreatobiliary and other systems.
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Orstavik,S., Reinton,N., Frengen,E., Langeland,B.T., Jahnsen,T. and
            Skalhegg,B.S.
  TITLE     Identification of novel splice variants of the human catalytic
            subunit Cbeta of cAMP-dependent protein kinase
  JOURNAL   Eur J Biochem 268 (19), 5066-5073 (2001)
   PUBMED   11589697
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Scarpetta,M.A. and Uhler,M.D.
  TITLE     Evidence for two additional isoforms of the endogenous protein
            kinase inhibitor of cAMP-dependent protein kinase in mouse
  JOURNAL   J Biol Chem 268 (15), 10927-10931 (1993)
   PUBMED   7684369
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Da Silva,J.D., Tkachenko,N. and Soares,A.R.
  TITLE     Ellis-van Creveld Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37903214
REFERENCE   8  (residues 1 to 258)
  AUTHORS   Simard,J., Berube,D., Sandberg,M., Grzeschik,K.H., Gagne,R.,
            Hansson,V. and Jahnsen,T.
  TITLE     Assignment of the gene encoding the catalytic subunit C beta of
            cAMP-dependent protein kinase to the p36 band on chromosome 1
  JOURNAL   Hum Genet 88 (6), 653-657 (1992)
   PUBMED   1551670
REFERENCE   9  (residues 1 to 258)
  AUTHORS   Beebe,S.J., Oyen,O., Sandberg,M., Froysa,A., Hansson,V. and
            Jahnsen,T.
  TITLE     Molecular cloning of a tissue-specific protein kinase (C gamma)
            from human testis--representing a third isoform for the catalytic
            subunit of cAMP-dependent protein kinase
  JOURNAL   Mol Endocrinol 4 (3), 465-475 (1990)
   PUBMED   2342480
REFERENCE   10 (residues 1 to 258)
  AUTHORS   Taylor,S.S., Buechler,J.A. and Yonemoto,W.
  TITLE     cAMP-dependent protein kinase: framework for a diverse family of
            regulatory enzymes
  JOURNAL   Annu Rev Biochem 59, 971-1005 (1990)
   PUBMED   2165385
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359504.29 and AL450063.14.
            
            On Oct 29, 2019 this sequence version replaced XP_016857202.1.
            
            Summary: The protein encoded by this gene is a member of the
            serine/threonine protein kinase family. The encoded protein is a
            catalytic subunit of cAMP (cyclic AMP)-dependent protein kinase,
            which mediates signalling though cAMP. cAMP signaling is important
            to a number of processes, including cell proliferaton and
            differentiation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2543897.1,
                                           SRR11853559.1664.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.1"
     Protein         1..258
                     /product="cAMP-dependent protein kinase catalytic subunit
                     beta isoform 25"
                     /EC_number="2.7.11.11"
                     /note="protein kinase A catalytic subunit beta; protein
                     kinase, cAMP-dependent, catalytic, beta; protein kinase,
                     cAMP-dependent, beta catalytic subunit"
                     /calculated_mol_wt=29693
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05132; propagated from
                     UniProtKB/Swiss-Prot (P22694.2)"
     Region          42..>258
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(50..53,56,58,71,73,105,121..124,167,171..172,174,
                     184..185)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P68181; propagated from
                     UniProtKB/Swiss-Prot (P22694.2)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05132; propagated from
                     UniProtKB/Swiss-Prot (P22694.2)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P05132; propagated from
                     UniProtKB/Swiss-Prot (P22694.2)"
     CDS             1..258
                     /gene="PRKACB"
                     /gene_synonym="CAFD2; PKA C-beta; PKACB"
                     /coded_by="NM_001375576.1:248..1024"
                     /note="isoform 25 is encoded by transcript variant 25"
                     /db_xref="GeneID:5567"
                     /db_xref="HGNC:HGNC:9381"
                     /db_xref="MIM:176892"
ORIGIN      
        1 mgnaatakkg sevesvkefl akakedflkk wenptqnnag ledferkktl gtgsfgrvml
       61 vkhkateqyy amkildkqkv vklkqiehtl nekrilqavn fpflvrleya fkdnsnlymv
      121 meyvpggemf shlrrigrfs epharfyaaq ivltfeylhs ldliyrdlkp enllidhqgy
      181 iqvtdfgfak rvkgrtwtlc gtpeylapei ilskgynkav dwwalgvliy emaagyppff
      241 adqpiqiyek ivsgkqnf
//
LOCUS       NP_001289438             584 aa            linear   PRI 21-NOV-2025
DEFINITION  72 kDa type IV collagenase isoform 3 [Homo sapiens].
ACCESSION   NP_001289438
VERSION     NP_001289438.1
DBSOURCE    REFSEQ: accession NM_001302509.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Hung,C.C., Tsai,C.L., Chin,Y.T., Wang,Y.C., Liu,C.H., Lin,M.L.,
            Chen,S.S., He,J.L., Tsai,C.W., Su,C.H., Bau,D.T. and Chang,W.S.
  TITLE     Impacts of Matrix Metalloproteinase-2 Promoter Genotypes on Breast
            Cancer Risk
  JOURNAL   Cancer Genomics Proteomics 21 (5), 502-510 (2024)
   PUBMED   39191502
  REMARK    GeneRIF: Impacts of Matrix Metalloproteinase-2 Promoter Genotypes
            on Breast Cancer Risk.
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Liang,S., Li,L., Guo,Z., Sun,H. and Yang,Y.
  TITLE     Co-expression of CD44v6 and MMP2 predicts lung metastasis and
            unfavorable prognosis in osteosarcoma
  JOURNAL   Future Oncol 20 (25), 1799-1806 (2024)
   PUBMED   39011948
  REMARK    GeneRIF: Co-expression of CD44v6 and MMP2 predicts lung metastasis
            and unfavorable prognosis in osteosarcoma.
REFERENCE   4  (residues 1 to 584)
  AUTHORS   DeCoux,A., Lindsey,M.L., Villarreal,F., Garcia,R.A. and Schulz,R.
  TITLE     Myocardial matrix metalloproteinase-2: inside out and upside down
  JOURNAL   J Mol Cell Cardiol 77, 64-72 (2014)
   PUBMED   25261607
  REMARK    GeneRIF: The roles of MMP-2 in cardiac injury and repair. [Review]
            Review article
REFERENCE   5  (residues 1 to 584)
  AUTHORS   Verslegers,M., Lemmens,K., Van Hove,I. and Moons,L.
  TITLE     Matrix metalloproteinase-2 and -9 as promising benefactors in
            development, plasticity and repair of the nervous system
  JOURNAL   Prog Neurobiol 105, 60-78 (2013)
   PUBMED   23567503
  REMARK    Review article
REFERENCE   6  (residues 1 to 584)
  AUTHORS   Nagase,H., Visse,R. and Murphy,G.
  TITLE     Structure and function of matrix metalloproteinases and TIMPs
  JOURNAL   Cardiovasc Res 69 (3), 562-573 (2006)
   PUBMED   16405877
  REMARK    Review article
REFERENCE   7  (residues 1 to 584)
  AUTHORS   Bhavani,G.S., Shah,H., Shukla,A. and Girisha,K.M.
  TITLE     Multicentric Osteolysis Nodulosis and Arthropathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27413800
REFERENCE   8  (residues 1 to 584)
  AUTHORS   Devarajan,P., Johnston,J.J., Ginsberg,S.S., Van Wart,H.E. and
            Berliner,N.
  TITLE     Structure and expression of neutrophil gelatinase cDNA. Identity
            with type IV collagenase from HT1080 cells
  JOURNAL   J Biol Chem 267 (35), 25228-25232 (1992)
   PUBMED   1460022
REFERENCE   9  (residues 1 to 584)
  AUTHORS   Levy,A.T., Cioce,V., Sobel,M.E., Garbisa,S., Grigioni,W.F.,
            Liotta,L.A. and Stetler-Stevenson,W.G.
  TITLE     Increased expression of the Mr 72,000 type IV collagenase in human
            colonic adenocarcinoma
  JOURNAL   Cancer Res 51 (1), 439-444 (1991)
   PUBMED   1846313
REFERENCE   10 (residues 1 to 584)
  AUTHORS   Huhtala,P., Chow,L.T. and Tryggvason,K.
  TITLE     Structure of the human type IV collagenase gene
  JOURNAL   J Biol Chem 265 (19), 11077-11082 (1990)
   PUBMED   2162831
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK301536.1, BX357054.2 and
            BQ004983.1.
            
            Summary: This gene is a member of the matrix metalloproteinase
            (MMP) gene family, that are zinc-dependent enzymes capable of
            cleaving components of the extracellular matrix and molecules
            involved in signal transduction. The protein encoded by this gene
            is a gelatinase A, type IV collagenase, that contains three
            fibronectin type II repeats in its catalytic site that allow
            binding of denatured type IV and V collagen and elastin. Unlike
            most MMP family members, activation of this protein can occur on
            the cell membrane. This enzyme can be activated extracellularly by
            proteases, or, intracellulary by its S-glutathiolation with no
            requirement for proteolytical removal of the pro-domain. This
            protein is thought to be involved in multiple pathways including
            roles in the nervous system, endometrial menstrual breakdown,
            regulation of vascularization, and metastasis. Mutations in this
            gene have been associated with Winchester syndrome and
            Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Oct 2014].
            
            Transcript Variant: This variant (4) contains an alternate 5'
            terminal exon, and initiates translation at a downstream start
            codon, compared to variant 1. The encoded isoform (3) has a shorter
            N-terminus than isoform 1. Variants 3, 4, and 5 all encode the same
            isoform (3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301536.1, SRR14038197.2113583.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..584
                     /product="72 kDa type IV collagenase isoform 3"
                     /EC_number="3.4.24.24"
                     /note="neutrophil gelatinase; matrix metalloproteinase-II;
                     collagenase type IV-A; matrix metallopeptidase 2
                     (gelatinase A, 72kDa gelatinase, 72kDa type IV
                     collagenase); matrix metalloproteinase-2"
                     /calculated_mol_wt=65634
     Region          42..370
                     /region_name="Peptidase_M10"
                     /note="Matrixin; pfam00413"
                     /db_xref="CDD:425668"
     Region          150..198
                     /region_name="FN2"
                     /note="Fibronectin type 2 domain; smart00059"
                     /db_xref="CDD:128373"
     Site            order(161,163,168,182,189,195,197)
                     /site_type="active"
                     /note="putative gelatin-binding site [active]"
                     /db_xref="CDD:238019"
     Region          208..256
                     /region_name="FN2"
                     /note="Fibronectin type 2 domain; smart00059"
                     /db_xref="CDD:128373"
     Site            order(219,221,226,240,247,253,255)
                     /site_type="active"
                     /note="putative gelatin-binding site [active]"
                     /db_xref="CDD:238019"
     Region          266..314
                     /region_name="FN2"
                     /note="Fibronectin type 2 domain; smart00059"
                     /db_xref="CDD:128373"
     Site            order(277,279,284,298,305,311,313)
                     /site_type="active"
                     /note="putative gelatin-binding site [active]"
                     /db_xref="CDD:238019"
     Region          390..584
                     /region_name="HX"
                     /note="Hemopexin-like repeats.; Hemopexin is a
                     heme-binding protein that transports heme to the liver.
                     Hemopexin-like repeats occur in vitronectin and some
                     matrix metalloproteinases family (matrixins). The HX
                     repeats of some matrixins bind tissue inhibitor of...;
                     cd00094"
                     /db_xref="CDD:238046"
     Site            order(400,402,445,447,493,495,542,544)
                     /site_type="metal-binding"
                     /note="Metal binding sites [ion binding]"
                     /db_xref="CDD:238046"
     CDS             1..584
                     /gene="MMP2"
                     /gene_synonym="CLG4; CLG4A; MMP-2; MMP-II; MONA; TBE-1"
                     /coded_by="NM_001302509.2:141..1895"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS76869.1"
                     /db_xref="GeneID:4313"
                     /db_xref="HGNC:HGNC:7166"
                     /db_xref="MIM:120360"
ORIGIN      
        1 mqkffglpqt gdldqntiet mrkprcgnpd vanynffprk pkwdknqity riigytpdld
       61 petvddafar afqvwsdvtp lrfsrihdge adiminfgrw ehgdgypfdg kdgllahafa
      121 pgtgvggdsh fdddelwtlg egqvvrvkyg nadgeyckfp flfngkeyns ctdtgrsdgf
      181 lwcsttynfe kdgkygfcph ealftmggna egqpckfpfr fqgtsydsct tegrtdgyrw
      241 cgttedydrd kkygfcpeta mstvggnseg apcvfpftfl gnkyesctsa grsdgkmwca
      301 ttanydddrk wgfcpdqgys lflvaahefg hamglehsqd pgalmapiyt ytknfrlsqd
      361 dikgiqelyg aspdidlgtg ptptlgpvtp eickqdivfd giaqirgeif ffkdrfiwrt
      421 vtprdkpmgp llvatfwpel pekidavyea pqeekavffa gneywiysas tlergypkpl
      481 tslglppdvq rvdaafnwsk nkktyifagd kfwrynevkk kmdpgfpkli adawnaipdn
      541 ldavvdlqgg ghsyffkgay ylklenqslk svkfgsiksd wlgc
//
LOCUS       NP_001362954             573 aa            linear   PRI 21-NOV-2025
DEFINITION  protein 4.1 isoform 18 [Homo sapiens].
ACCESSION   NP_001362954 XP_016856089
VERSION     NP_001362954.1
DBSOURCE    REFSEQ: accession NM_001376025.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Terada,N., Saitoh,Y., Saito,M., Yamada,T., Kamijo,A., Yoshizawa,T.
            and Sakamoto,T.
  TITLE     Recent Progress on Genetically Modified Animal Models for Membrane
            Skeletal Proteins: The 4.1 and MPP Families
  JOURNAL   Genes (Basel) 14 (10), 1942 (2023)
   PUBMED   37895291
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 573)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 573)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 573)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 573)
  AUTHORS   Dalla Venezia,N., Gilsanz,F., Alloisio,N., Ducluzeau,M.T.,
            Benz,E.J. Jr. and Delaunay,J.
  TITLE     Homozygous 4.1(-) hereditary elliptocytosis associated with a point
            mutation in the downstream initiation codon of protein 4.1 gene
  JOURNAL   J Clin Invest 90 (5), 1713-1717 (1992)
   PUBMED   1430200
REFERENCE   7  (residues 1 to 573)
  AUTHORS   Jons,T. and Drenckhahn,D.
  TITLE     Identification of the binding interface involved in linkage of
            cytoskeletal protein 4.1 to the erythrocyte anion exchanger
  JOURNAL   EMBO J 11 (8), 2863-2867 (1992)
   PUBMED   1639060
REFERENCE   8  (residues 1 to 573)
  AUTHORS   Subrahmanyam,G., Bertics,P.J. and Anderson,R.A.
  TITLE     Phosphorylation of protein 4.1 on tyrosine-418 modulates its
            function in vitro
  JOURNAL   Proc Natl Acad Sci U S A 88 (12), 5222-5226 (1991)
   PUBMED   1647028
REFERENCE   9  (residues 1 to 573)
  AUTHORS   Conboy,J.G., Chan,J.Y., Chasis,J.A., Kan,Y.W. and Mohandas,N.
  TITLE     Tissue- and development-specific alternative RNA splicing regulates
            expression of multiple isoforms of erythroid membrane protein 4.1
  JOURNAL   J Biol Chem 266 (13), 8273-8280 (1991)
   PUBMED   2022644
REFERENCE   10 (residues 1 to 573)
  AUTHORS   Horne,W.C., Prinz,W.C. and Tang,E.K.
  TITLE     Identification of two cAMP-dependent phosphorylation sites on
            erythrocyte protein 4.1
  JOURNAL   Biochim Biophys Acta 1055 (1), 87-92 (1990)
   PUBMED   2171679
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL009181.1, AL138785.8 and
            AL357500.17.
            
            On Nov 7, 2019 this sequence version replaced XP_016856089.1.
            
            Summary: The protein encoded by this gene, together with spectrin
            and actin, constitute the red cell membrane cytoskeletal network.
            This complex plays a critical role in erythrocyte shape and
            deformability. Mutations in this gene are associated with type 1
            elliptocytosis (EL1). Alternatively spliced transcript variants
            encoding different isoforms have been described for this
            gene.[provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.157474.1,
                                           SRR1803614.111833.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162841, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.3"
     Protein         1..573
                     /product="protein 4.1 isoform 18"
                     /note="protein 4.1; erythrocyte surface protein band 4.1;
                     P4.1; EPB4.1; elliptocytosis 1, RH-linked"
                     /calculated_mol_wt=65202
     Region          2..192
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          187..280
                     /region_name="FERM_C_4_1_family"
                     /note="FERM domain C-lobe of Protein 4.1 family; cd13184"
                     /db_xref="CDD:270005"
     Site            order(196,213,215,221)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270005"
     Site            order(225,230..233,268,272,275..276)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Site            268..279
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Region          290..333
                     /region_name="FA"
                     /note="FERM adjacent (FA); pfam08736"
                     /db_xref="CDD:462582"
     Region          458..506
                     /region_name="SAB"
                     /note="SAB domain; pfam04382"
                     /db_xref="CDD:461285"
     CDS             1..573
                     /gene="EPB41"
                     /gene_synonym="4.1R; EL1; HE"
                     /coded_by="NM_001376025.1:729..2450"
                     /note="isoform 18 is encoded by transcript variant 19"
                     /db_xref="GeneID:2035"
                     /db_xref="HGNC:HGNC:3377"
                     /db_xref="MIM:130500"
ORIGIN      
        1 mhckvslldd tvyecvvekh akgqdllkrv cehlnlleed yfglaiwdna tsktwldsak
       61 eikkqvrgvp wnftfnvkfy ppdpaqlted itryylclql rqdivagrlp csfatlallg
      121 sytiqselgd ydpelhgvdy vsdfklapnq tkeleekvme lhksyrsmtp aqadleflen
      181 akklsmygvd lhkakdlegv diilgvcssg llvykdklri nrfpwpkvlk isykrssffi
      241 kirpgeqeqy estigfklps yraakklwkv cvehhtffrl tstdtipksk flalgskfry
      301 sgrtqaqtrq asalidrpap hfertaskra srsldgaaav dsadrsprpt sapaitqgqv
      361 aeggvldasa kktvvpkaqk etvkaevkke deppeqaepe pteawkvekt hievtvptsn
      421 gdqtqklaek tedlirmrkk krerldgeni yirhsnlmle dldksqeeik khhasiselk
      481 knfmesvpep rpsewdkrls thspfrtlni ngqiptgegv kktsvlpser kspsyflpdt
      541 yhlgvckepv lnfqtdqrrl aqlrelrakf fls
//
LOCUS       NP_001288759             784 aa            linear   PRI 21-NOV-2025
DEFINITION  ATP-binding cassette sub-family C member 4 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001288759
VERSION     NP_001288759.1
DBSOURCE    REFSEQ: accession NM_001301830.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Ranjit,S., Wang,Y., Zhu,J., Cheepala,S.B., Schuetz,E.G., Cho,W.J.,
            Xu,B., Robinson,C.G., Wu,G., Naren,A.P. and Schuetz,J.D.
  TITLE     ABCC4 impacts megakaryopoiesis and protects megakaryocytes against
            6-mercaptopurine induced cytotoxicity
  JOURNAL   Drug Resist Updat 72, 101017 (2024)
   PUBMED   37988981
  REMARK    GeneRIF: ABCC4 impacts megakaryopoiesis and protects megakaryocytes
            against 6-mercaptopurine induced cytotoxicity.
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Bloch,M., Raj,I., Pape,T. and Taylor,N.M.I.
  TITLE     Structural and mechanistic basis of substrate transport by the
            multidrug transporter MRP4
  JOURNAL   Structure 31 (11), 1407-1418 (2023)
   PUBMED   37683641
  REMARK    GeneRIF: Structural and mechanistic basis of substrate transport by
            the multidrug transporter MRP4.
REFERENCE   3  (residues 1 to 784)
  AUTHORS   Huang,C., Xu,R., Zhu,X. and Jiang,H.
  TITLE     m6A-modified circABCC4 promotes stemness and metastasis of prostate
            cancer by recruiting IGF2BP2 to increase stability of CCAR1
  JOURNAL   Cancer Gene Ther 30 (10), 1426-1440 (2023)
   PUBMED   37563361
  REMARK    GeneRIF: m6A-modified circABCC4 promotes stemness and metastasis of
            prostate cancer by recruiting IGF2BP2 to increase stability of
            CCAR1.
REFERENCE   4  (residues 1 to 784)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 784)
  AUTHORS   Adachi,M., Sampath,J., Lan,L.B., Sun,D., Hargrove,P., Flatley,R.,
            Tatum,A., Edwards,M.Z., Wezeman,M., Matherly,L., Drake,R. and
            Schuetz,J.
  TITLE     Expression of MRP4 confers resistance to ganciclovir and
            compromises bystander cell killing
  JOURNAL   J Biol Chem 277 (41), 38998-39004 (2002)
   PUBMED   12105214
  REMARK    GeneRIF: These findings indicate that a nucleotide transporter,
            such as MRP4, modulates the cellular response to ganciclovir and
            thus may influence not only the efficacy of antiviral therapy, but
            also prodrug-based gene therapy.
REFERENCE   6  (residues 1 to 784)
  AUTHORS   Lee,K., Belinsky,M.G., Bell,D.W., Testa,J.R. and Kruh,G.D.
  TITLE     Isolation of MOAT-B, a widely expressed multidrug
            resistance-associated protein/canalicular multispecific organic
            anion transporter-related transporter
  JOURNAL   Cancer Res 58 (13), 2741-2747 (1998)
   PUBMED   9661885
REFERENCE   7  (residues 1 to 784)
  AUTHORS   Kool,M., de Haas,M., Scheffer,G.L., Scheper,R.J., van Eijk,M.J.,
            Juijn,J.A., Baas,F. and Borst,P.
  TITLE     Analysis of expression of cMOAT (MRP2), MRP3, MRP4, and MRP5,
            homologues of the multidrug resistance-associated protein gene
            (MRP1), in human cancer cell lines
  JOURNAL   Cancer Res 57 (16), 3537-3547 (1997)
   PUBMED   9270026
REFERENCE   8  (residues 1 to 784)
  AUTHORS   Allikmets,R., Gerrard,B., Hutchinson,A. and Dean,M.
  TITLE     Characterization of the human ABC superfamily: isolation and
            mapping of 21 new genes using the expressed sequence tags database
  JOURNAL   Hum Mol Genet 5 (10), 1649-1655 (1996)
   PUBMED   8894702
REFERENCE   9  (residues 1 to 784)
  AUTHORS   Pichaud,F., Frendo,J.L., Delage-Mourroux,R., de Vernejoul,M.C.,
            Moukhtar,M.S. and Jullienne,A.
  TITLE     Sequence of a novel mRNA coding for a C-terminal-truncated form of
            human NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase
  JOURNAL   Gene 162 (2), 319-322 (1995)
   PUBMED   7557451
REFERENCE   10 (residues 1 to 784)
  AUTHORS   Ponticelli,A.S. and Smith,G.R.
  TITLE     Meiotic recombination-deficient mutants of Schizosaccharomyces
            pombe
  JOURNAL   Genetics 123 (1), 45-54 (1989)
   PUBMED   2806887
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL356257.14, AK290317.1,
            AK296247.1, CN410193.1 and BX113883.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the MRP subfamily which is involved in
            multi-drug resistance. This family member plays a role in cellular
            detoxification as a pump for its substrate, organic anions. It may
            also function in prostaglandin-mediated cAMP signaling in
            ciliogenesis. Alternative splicing of this gene results in multiple
            transcript variants. [provided by RefSeq, Sep 2014].
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon in the 5' coding region, and also lacks several 3' exons but
            contains an alternate 3' terminal exon, and it thus differs in the
            3' coding region and 3' UTR, compared to variant 1. The encoded
            isoform (4) has a distinct and shorter C-terminus, compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296247.1, SRR14038193.1679351.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q32.1"
     Protein         1..784
                     /product="ATP-binding cassette sub-family C member 4
                     isoform 4"
                     /EC_number="7.6.2.2"
                     /EC_number="7.6.2.3"
                     /note="canalicular multispecific organic anion transporter
                     (ABC superfamily); multidrug resistance-associated protein
                     4; bA464I2.1 (ATP-binding cassette, sub-family C
                     (CFTR/MRP), member 4); MRP/cMOAT-related ABC transporter;
                     multi-specific organic anion transporter B"
                     /calculated_mol_wt=88008
     Region          12..>758
                     /region_name="PLN03130"
                     /note="ABC transporter C family member; Provisional"
                     /db_xref="CDD:215595"
     CDS             1..784
                     /gene="ABCC4"
                     /gene_synonym="MOAT-B; MOATB; MRP4"
                     /coded_by="NM_001301830.2:138..2492"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS76643.1"
                     /db_xref="GeneID:10257"
                     /db_xref="HGNC:HGNC:55"
                     /db_xref="MIM:605250"
ORIGIN      
        1 mlpvyqevkp nplqdanlcs rvffwwlnpl fkighkrrle eddmysvlpe drsqhlgeel
       61 qgfwdkevlr aendaqkpsl traiikcywk sylvlgiftl iealrlsnma mgktttgqiv
      121 nllsndvnkf dqvtvflhfl wagplqaiav tallwmeigi sclagmavli illplqscfg
      181 klfsslrskt atftdarirt mnevitgiri ikmyaweksf snlitnlrkk eiskilrssc
      241 lrgmnlasff saskiivfvt fttyvllgsv itasrvfvav tlygavrltv tlffpsaier
      301 vseaivsirr iqtfllldei sqrnrqlpsd gkkmvhvqdf tafwdkaset ptlqglsftv
      361 rpgellavvg pvgagkssll savlgelaps hglvsvhgri ayvsqqpwvf sgtlrsnilf
      421 gkkyekerye kvikacalkk dlqlledgdl tvigdrgttl sggqkarvnl aravyqdadi
      481 yllddplsav daevsrhlfe lcicqilhek itilvthqlq ylkaasqili lkdgkmvqkg
      541 tyteflksgi dfgsllkkdn eeseqppvpg tptlrnrtfs essvwsqqss rpslkdgale
      601 sqdtenvpvt lseenrsegk vgfqayknyf ragahwivfi flillntaaq vayvlqdwwl
      661 sywankqsml nvtvngggnv tekldlnwyl giysgltvat vlfgiarsll vfyvlvnssq
      721 tlhnkmfesi lkapvlffdr npigrilnrf skdighlddl lpltfldfiq rwdlavlswl
      781 vsns
//
LOCUS       NP_001167622             325 aa            linear   PRI 21-NOV-2025
DEFINITION  ADP-ribosylation factor-like protein 13B isoform 3 [Homo sapiens].
ACCESSION   NP_001167622
VERSION     NP_001167622.1
DBSOURCE    REFSEQ: accession NM_001174151.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Lin,Z., Shen,Y., Li,Y., Lu,C., Zhu,Y., He,R., Cao,Z., Yin,Z.,
            Gao,H., Guo,B., Ma,X., Cao,M. and Luo,M.
  TITLE     Novel compound heterozygous variants in ARL13B lead to Joubert
            syndrome
  JOURNAL   J Cell Physiol 239 (4), e31189 (2024)
   PUBMED   38219074
  REMARK    GeneRIF: Novel compound heterozygous variants in ARL13B lead to
            Joubert syndrome.
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Shi,P., Tian,J., Mallinger,J.C., Ling,D., Deleyrolle,L.P.,
            McIntyre,J.C., Caspary,T., Breunig,J.J. and Sarkisian,M.R.
  TITLE     Increasing Ciliary ARL13B Expression Drives Active and
            Inhibitor-Resistant Smoothened and GLI into Glioma Primary Cilia
  JOURNAL   Cells 12 (19), 2354 (2023)
   PUBMED   37830570
  REMARK    GeneRIF: Increasing Ciliary ARL13B Expression Drives Active and
            Inhibitor-Resistant Smoothened and GLI into Glioma Primary Cilia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Mahajan,D., Madugula,V. and Lu,L.
  TITLE     Rab8 and TNPO1 are ciliary transport adaptors for GTPase Arl13b by
            interacting with its RVEP motif containing ciliary targeting
            sequence
  JOURNAL   J Biol Chem 299 (5), 104604 (2023)
   PUBMED   36907439
  REMARK    GeneRIF: Rab8 and TNPO1 are ciliary transport adaptors for GTPase
            Arl13b by interacting with its RVEP motif containing ciliary
            targeting sequence.
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Hori,Y., Kobayashi,T., Kikko,Y., Kontani,K. and Katada,T.
  TITLE     Domain architecture of the atypical Arf-family GTPase Arl13b
            involved in cilia formation
  JOURNAL   Biochem Biophys Res Commun 373 (1), 119-124 (2008)
   PUBMED   18554500
  REMARK    GeneRIF: These findings suggest that N and C domains of Arl13b
            cooperatively regulate its ciliary localization and that N
            domain-dependent self-association of Arl13b may be important for
            its function in cilia biogenesis.
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Cantagrel,V., Silhavy,J.L., Bielas,S.L., Swistun,D., Marsh,S.E.,
            Bertrand,J.Y., Audollent,S., Attie-Bitach,T., Holden,K.R.,
            Dobyns,W.B., Traver,D., Al-Gazali,L., Ali,B.R., Lindner,T.H.,
            Caspary,T., Otto,E.A., Hildebrandt,F., Glass,I.A., Logan,C.V.,
            Johnson,C.A., Bennett,C., Brancati,F., Valente,E.M., Woods,C.G. and
            Gleeson,J.G.
  CONSRTM   International Joubert Syndrome Related Disorders Study Group
  TITLE     Mutations in the cilia gene ARL13B lead to the classical form of
            Joubert syndrome
  JOURNAL   Am J Hum Genet 83 (2), 170-179 (2008)
   PUBMED   18674751
  REMARK    GeneRIF: ARL13B has an evolutionarily conserved role mediating
            cilia function in multiple organs
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   8  (residues 1 to 325)
  AUTHORS   Fan,Y., Esmail,M.A., Ansley,S.J., Blacque,O.E., Boroevich,K.,
            Ross,A.J., Moore,S.J., Badano,J.L., May-Simera,H., Compton,D.S.,
            Green,J.S., Lewis,R.A., van Haelst,M.M., Parfrey,P.S.,
            Baillie,D.L., Beales,P.L., Katsanis,N., Davidson,W.S. and
            Leroux,M.R.
  TITLE     Mutations in a member of the Ras superfamily of small GTP-binding
            proteins causes Bardet-Biedl syndrome
  JOURNAL   Nat Genet 36 (9), 989-993 (2004)
   PUBMED   15314642
REFERENCE   9  (residues 1 to 325)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 325)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC117474.7, AL713789.1 and
            AA775026.1.
            
            Summary: This gene encodes a member of the ADP-ribosylation
            factor-like family. The encoded protein is a small GTPase that
            contains both N-terminal and C-terminal guanine nucleotide-binding
            motifs. This protein is localized in the cilia and plays a role in
            cilia formation and in maintenance of cilia. Mutations in this gene
            are the cause of Joubert syndrome 8. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Mar 2010].
            
            Transcript Variant: This variant (4) differs in the 3' UTR, lacks
            an in-frame exon in the 5' coding region and uses a downstream
            start codon, compared to variant 1. The encoded isoform 3 has a
            shorter N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL713789.1, SRR18074967.39331.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q11.1-q11.2"
     Protein         1..325
                     /product="ADP-ribosylation factor-like protein 13B isoform
                     3"
                     /note="ADP-ribosylation factor-like 2-like 1; ARL2-like
                     protein 1; ADP ribosylation factor like GTPase 13B"
                     /calculated_mol_wt=36956
     Region          <1..86
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            27..30
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133361"
     Site            63..65
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133361"
     Region          <96..138
                     /region_name="CCDC47"
                     /note="PAT complex subunit CCDC47; cl46382"
                     /db_xref="CDD:480722"
     CDS             1..325
                     /gene="ARL13B"
                     /gene_synonym="ARL2L1; JBTS8"
                     /coded_by="NM_001174151.2:508..1485"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS54615.1"
                     /db_xref="GeneID:200894"
                     /db_xref="HGNC:HGNC:25419"
                     /db_xref="MIM:608922"
ORIGIN      
        1 meetkeamse mlrhprisgk pilvlankqd kegalgeadv ieclsleklv nehkclcqie
       61 pcsaisgygk kidksikkgl ywllhviard fdalneriqk etteqralee qekqeraerv
      121 rklreerkqn eqeqaeldgt sglaeldpep tnpfqpiasv iienegkler ekknqkmekd
      181 sdgchlkhkm eheqietqgq vnhngqknne fglvenykea ltqqlknede tdrpslesan
      241 gkkktkklrm krnhrvepln iddcapespt pppppppvgw gtpkvtrlpk leplgethhn
      301 dfyrkplppl avpqrpnsda hdvis
//
LOCUS       NP_001387                763 aa            linear   PRI 21-NOV-2025
DEFINITION  dual specificity tyrosine-phosphorylation-regulated kinase 1A
            isoform 1 [Homo sapiens].
ACCESSION   NP_001387
VERSION     NP_001387.2
DBSOURCE    REFSEQ: accession NM_001396.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 763)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 763)
  AUTHORS   Wang,P., Sarkar,S., Zhang,M., Xiao,T., Kong,F., Zhang,Z.,
            Balasubramanian,D., Jayaram,N., Datta,S., He,R., Wu,P., Chao,P.,
            Zhang,Y., Washburn,M., Florens,L.A., Nagarkar-Jaiswal,S.,
            Jaiswal,M. and Mohan,M.
  TITLE     DYRK1A interacts with the tuberous sclerosis complex and promotes
            mTORC1 activity
  JOURNAL   Elife 12, 88318 (2024)
   PUBMED   39436397
  REMARK    GeneRIF: DYRK1A interacts with the tuberous sclerosis complex and
            promotes mTORC1 activity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 763)
  AUTHORS   Pastor,F., Charles,E., Di Vona,C., Chapelle,M., Rivoire,M.,
            Passot,G., Chabot,B., de la Luna,S., Lucifora,J., Durantel,D. and
            Salvetti,A.
  TITLE     The dual-specificity kinase DYRK1A interacts with the Hepatitis B
            virus genome and regulates the production of viral RNA
  JOURNAL   PLoS One 19 (10), e0311655 (2024)
   PUBMED   39405283
  REMARK    GeneRIF: The dual-specificity kinase DYRK1A interacts with the
            Hepatitis B virus genome and regulates the production of viral RNA.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 763)
  AUTHORS   Guimera,J., Casas,C., Estivill,X. and Pritchard,M.
  TITLE     Human minibrain homologue (MNBH/DYRK1): characterization,
            alternative splicing, differential tissue expression, and
            overexpression in Down syndrome
  JOURNAL   Genomics 57 (3), 407-418 (1999)
   PUBMED   10329007
REFERENCE   5  (residues 1 to 763)
  AUTHORS   Wang,J., Kudoh,J., Shintani,A., Minoshima,S. and Shimizu,N.
  TITLE     Identification of two novel 5' noncoding exons in human MNB/DYRK
            gene and alternatively spliced transcripts
  JOURNAL   Biochem Biophys Res Commun 250 (3), 704-710 (1998)
   PUBMED   9784410
REFERENCE   6  (residues 1 to 763)
  AUTHORS   Song,W.J., Sternberg,L.R., Kasten-Sportes,C., Keuren,M.L.,
            Chung,S.H., Slack,A.C., Miller,D.E., Glover,T.W., Chiang,P.W.,
            Lou,L. and Kurnit,D.M.
  TITLE     Isolation of human and murine homologues of the Drosophila
            minibrain gene: human homologue maps to 21q22.2 in the Down
            syndrome 'critical region'
  JOURNAL   Genomics 38 (3), 331-339 (1996)
   PUBMED   8975710
REFERENCE   7  (residues 1 to 763)
  AUTHORS   Guimera,J., Casas,C., Pucharcos,C., Solans,A., Domenech,A.,
            Planas,A.M., Ashley,J., Lovett,M., Estivill,X. and Pritchard,M.A.
  TITLE     A human homologue of Drosophila minibrain (MNB) is expressed in the
            neuronal regions affected in Down syndrome and maps to the critical
            region
  JOURNAL   Hum Mol Genet 5 (9), 1305-1310 (1996)
   PUBMED   8872470
REFERENCE   8  (residues 1 to 763)
  AUTHORS   Shindoh,N., Kudoh,J., Maeda,H., Yamaki,A., Minoshima,S., Shimizu,Y.
            and Shimizu,N.
  TITLE     Cloning of a human homolog of the Drosophila minibrain/rat Dyrk
            gene from 'the Down syndrome critical region' of chromosome 21
  JOURNAL   Biochem Biophys Res Commun 225 (1), 92-99 (1996)
   PUBMED   8769099
REFERENCE   9  (residues 1 to 763)
  AUTHORS   Schultz,S.J. and Nigg,E.A.
  TITLE     Identification of 21 novel human protein kinases, including 3
            members of a family related to the cell cycle regulator nimA of
            Aspergillus nidulans
  JOURNAL   Cell Growth Differ 4 (10), 821-830 (1993)
   PUBMED   8274451
REFERENCE   10 (residues 1 to 763)
  AUTHORS   van Bon,B.W.M., Coe,B.P., de Vries,B.B.A. and Eichler,E.E.
  TITLE     DYRK1A Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26677511
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001437.1, AP001428.1,
            AP001413.1, KF457264.1, AP001421.1 and KF511415.1.
            
            On Feb 19, 2002 this sequence version replaced NP_001387.1.
            
            Summary: This gene encodes a member of the Dual-specificity
            tyrosine phosphorylation-regulated kinase (DYRK) family. This
            member contains a nuclear targeting signal sequence, a protein
            kinase domain, a leucine zipper motif, and a highly conservative
            13-consecutive-histidine repeat. It catalyzes its
            autophosphorylation on serine/threonine and tyrosine residues. It
            may play a significant role in a signaling pathway regulating cell
            proliferation and may be involved in brain development. This gene
            is a homolog of Drosophila mnb (minibrain) gene and rat Dyrk gene.
            It is localized in the Down syndrome critical region of chromosome
            21, and is considered to be a strong candidate gene for learning
            defects associated with Down syndrome. Alternative splicing of this
            gene generates several transcript variants differing from each
            other either in the 5' UTR or in the 3' coding region. These
            variants encode at least five different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.172986.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2153980
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..763
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.13"
     Protein         1..763
                     /product="dual specificity
                     tyrosine-phosphorylation-regulated kinase 1A isoform 1"
                     /EC_number="2.7.11.23"
                     /EC_number="2.7.12.1"
                     /note="dual specificity YAK1-related kinase;
                     serine/threonine-specific protein kinase; mnb protein
                     kinase homolog hp86; serine/threonine kinase MNB; MNB/DYRK
                     protein kinase; protein kinase minibrain homolog; dual
                     specificity tyrosine-(Y)-phosphorylation regulated kinase
                     1A"
                     /calculated_mol_wt=85453
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Region          32..57
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Region          115..136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Region          117..134
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Region          148..484
                     /region_name="PKc_DYRK1"
                     /note="Catalytic domain of the protein kinase,
                     Dual-specificity tYrosine-phosphorylated and -Regulated
                     Kinase 1; cd14226"
                     /db_xref="CDD:271128"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            order(165..169,173,186,188,202,222,238..241,244,246..247,
                     287,289,291..292,294,307,310,319,321..324,326,363)
                     /site_type="active"
                     /db_xref="CDD:271128"
     Site            order(165..169,173,186,188,222,238..241,244,287,289,
                     291..292,294,307)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271128"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            order(202,246,287,289,310,319,321..324,326,363)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271128"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q63470; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            306..326
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271128"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Region          408..442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Region          485..540
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            538
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61214; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Region          595..625
                     /region_name="Histidine-rich domain (HRD).
                     /evidence=ECO:0000269|PubMed:29849146"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Region          596..679
                     /region_name="Disordered.
                     /evidence=ECO:0000269|PubMed:29849146"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Region          744..763
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Site            748
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     CDS             1..763
                     /gene="DYRK1A"
                     /gene_synonym="DYRK; DYRK1; HP86; MNB; MNBH; MRD7"
                     /coded_by="NM_001396.5:339..2630"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42925.1"
                     /db_xref="GeneID:1859"
                     /db_xref="HGNC:HGNC:3091"
                     /db_xref="MIM:600855"
ORIGIN      
        1 mhtggetsac kpssvrlaps fsfhaaglqm agqmphshqy sdrrqpnisd qqvsalsysd
       61 qiqqpltnqv mpdivmlqrr mpqtfrdpat aplrklsvdl iktykhinev yyakkkrrhq
      121 qgqgddsshk kerkvyndgy dddnydyivk ngekwmdrye idsligkgsf gqvvkaydrv
      181 eqewvaikii knkkaflnqa qievrllelm nkhdtemkyy ivhlkrhfmf rnhlclvfem
      241 lsynlydllr ntnfrgvsln ltrkfaqqmc tallflatpe lsiihcdlkp enillcnpkr
      301 saikivdfgs scqlgqriyq yiqsrfyrsp evllgmpydl aidmwslgci lvemhtgepl
      361 fsganevdqm nkivevlgip pahildqapk arkffeklpd gtwnlkktkd gkreykppgt
      421 rklhnilgve tggpggrrag esghtvadyl kfkdlilrml dydpktriqp yyalqhsffk
      481 ktadegtnts nsvstspame qsqssgttss tssssggssg tsnsgrarsd pthqhrhsgg
      541 hftaavqamd cethspqvrq qfpaplgwsg teaptqvtve thpvqettfh vapqqnalhh
      601 hhgnsshhhh hhhhhhhhhg qqalgnrtrp rvynsptnss stqdsmevgh shhsmtslss
      661 sttssstsss stgnqgnqay qnrpvaantl dfgqngamdv nltvysnprq etgiaghpty
      721 qfsantgpah ymteghltmr qgadreespm tgvcvqqspv ass
//
LOCUS       NP_001153208             485 aa            linear   PRI 21-NOV-2025
DEFINITION  BUD13 homolog isoform 2 [Homo sapiens].
ACCESSION   NP_001153208
VERSION     NP_001153208.1
DBSOURCE    REFSEQ: accession NM_001159736.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Kornak,U., Saha,N., Keren,B., Neumann,A., Taylor Tavares,A.L.,
            Piard,J., Kopp,J., Rodrigues Alves,J.G., Rodriguez de Los
            Santos,M., El Choubassi,N., Ehmke,N., Jager,M., Spielmann,M.,
            Pantel,J.T., Lejeune,E., Fauler,B., Mielke,T., Hecht,J.,
            Meierhofer,D., Strom,T.M., Laugel,V., Brice,A., Mundlos,S.,
            Bertoli-Avella,A., Bauer,P., Heyd,F., Boute,O., Dupont,J.,
            Depienne,C., Van Maldergem,L. and Fischer-Zirnsak,B.
  TITLE     Alternative splicing of BUD13 determines the severity of a
            developmental disorder with lipodystrophy and progeroid features
  JOURNAL   Genet Med 24 (9), 1927-1940 (2022)
   PUBMED   35670808
  REMARK    GeneRIF: Alternative splicing of BUD13 determines the severity of a
            developmental disorder with lipodystrophy and progeroid features.
REFERENCE   5  (residues 1 to 485)
  AUTHORS   Masjoudi,S., Sedaghati-Khayat,B., Givi,N.J., Bonab,L.N.H., Azizi,F.
            and Daneshpour,M.S.
  TITLE     Kernel machine SNP set analysis finds the association of BUD13,
            ZPR1, and APOA5 variants with metabolic syndrome in Tehran
            Cardio-metabolic Genetics Study
  JOURNAL   Sci Rep 11 (1), 10305 (2021)
   PUBMED   33986338
  REMARK    GeneRIF: Kernel machine SNP set analysis finds the association of
            BUD13, ZPR1, and APOA5 variants with metabolic syndrome in Tehran
            Cardio-metabolic Genetics Study.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 485)
  AUTHORS   Hegele,R.A., Ban,M.R., Hsueh,N., Kennedy,B.A., Cao,H., Zou,G.Y.,
            Anand,S., Yusuf,S., Huff,M.W. and Wang,J.
  TITLE     A polygenic basis for four classical Fredrickson
            hyperlipoproteinemia phenotypes that are characterized by
            hypertriglyceridemia
  JOURNAL   Hum Mol Genet 18 (21), 4189-4194 (2009)
   PUBMED   19656773
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 485)
  AUTHORS   Baranzini,S.E., Wang,J., Gibson,R.A., Galwey,N., Naegelin,Y.,
            Barkhof,F., Radue,E.W., Lindberg,R.L., Uitdehaag,B.M.,
            Johnson,M.R., Angelakopoulou,A., Hall,L., Richardson,J.C.,
            Prinjha,R.K., Gass,A., Geurts,J.J., Kragt,J., Sombekke,M.,
            Vrenken,H., Qualley,P., Lincoln,R.R., Gomez,R., Caillier,S.J.,
            George,M.F., Mousavi,H., Guerrero,R., Okuda,D.T., Cree,B.A.,
            Green,A.J., Waubant,E., Goodin,D.S., Pelletier,D., Matthews,P.M.,
            Hauser,S.L., Kappos,L., Polman,C.H. and Oksenberg,J.R.
  TITLE     Genome-wide association analysis of susceptibility and clinical
            phenotype in multiple sclerosis
  JOURNAL   Hum Mol Genet 18 (4), 767-778 (2009)
   PUBMED   19010793
REFERENCE   8  (residues 1 to 485)
  AUTHORS   Kooner,J.S., Chambers,J.C., Aguilar-Salinas,C.A., Hinds,D.A.,
            Hyde,C.L., Warnes,G.R., Gomez Perez,F.J., Frazer,K.A., Elliott,P.,
            Scott,J., Milos,P.M., Cox,D.R. and Thompson,J.F.
  TITLE     Genome-wide scan identifies variation in MLXIPL associated with
            plasma triglycerides
  JOURNAL   Nat Genet 40 (2), 149-151 (2008)
   PUBMED   18193046
REFERENCE   9  (residues 1 to 485)
  AUTHORS   Kathiresan,S., Melander,O., Guiducci,C., Surti,A., Burtt,N.P.,
            Rieder,M.J., Cooper,G.M., Roos,C., Voight,B.F., Havulinna,A.S.,
            Wahlstrand,B., Hedner,T., Corella,D., Tai,E.S., Ordovas,J.M.,
            Berglund,G., Vartiainen,E., Jousilahti,P., Hedblad,B.,
            Taskinen,M.R., Newton-Cheh,C., Salomaa,V., Peltonen,L., Groop,L.,
            Altshuler,D.M. and Orho-Melander,M.
  TITLE     Six new loci associated with blood low-density lipoprotein
            cholesterol, high-density lipoprotein cholesterol or triglycerides
            in humans
  JOURNAL   Nat Genet 40 (2), 189-197 (2008)
   PUBMED   18193044
  REMARK    Erratum:[Nat Genet. 2008 Nov;40(11):1384]
REFERENCE   10 (residues 1 to 485)
  AUTHORS   Dziembowski,A., Ventura,A.P., Rutz,B., Caspary,F., Faux,C.,
            Halgand,F., Laprevote,O. and Seraphin,B.
  TITLE     Proteomic analysis identifies a new complex required for nuclear
            pre-mRNA retention and splicing
  JOURNAL   EMBO J 23 (24), 4847-4856 (2004)
   PUBMED   15565172
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK057832.1, AK311068.1 and CA432582.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the middle portion of the coding region compared to
            variant 1. This results in a shorter protein (isoform 2) compared
            to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225164.1, AK057832.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..485
                     /product="BUD13 homolog isoform 2"
                     /note="functional spliceosome-associated protein 71; BUD13
                     homolog"
                     /calculated_mol_wt=55436
     Region          <136..>271
                     /region_name="MSCRAMM_ClfB"
                     /note="MSCRAMM family adhesin clumping factor ClfB;
                     NF033845"
                     /db_xref="CDD:468203"
     Region          326..468
                     /region_name="Bud13"
                     /note="Pre-mRNA-splicing factor of RES complex; pfam09736"
                     /db_xref="CDD:462867"
     CDS             1..485
                     /gene="BUD13"
                     /gene_synonym="ACHPS; Cwc26; fSAP71"
                     /coded_by="NM_001159736.2:24..1481"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS53712.1"
                     /db_xref="GeneID:84811"
                     /db_xref="HGNC:HGNC:28199"
                     /db_xref="MIM:620691"
ORIGIN      
        1 maaapplska eylkrylsga dagvdrgses grkrrkkrpk pggaggkgmr ivdddvswta
       61 isttklekee eeddgdlpvv aefvderpee vkqmeafrss akwkllgghn edlpsnrhfr
      121 hdtpdssprr vrhgtpdpsp rkdrhdtpdp sprrarhdtp dpsplrgarh dsdtspprri
      181 rhdssdtspp rrarhdspdp spprrpqhns sgdcqkatds dlssprhkqs pghqdsdsdl
      241 spprnrprhr ssdsdlsppr rrqrtkssds dlspprrsqp pgkkaahmys gaktglvltd
      301 iqreqqelke qdqetmafea efqyaetvfr dksgrkrnlk lerleqrrka ekdserdely
      361 aqwgkglaqs rqqqqnveda mkemqkplar yiddedldrm lreqeregdp manfikknka
      421 kenknkkvrp rysgpapppn rfniwpgyrw dgvdrsngfe qkrfarlask kaveelaykw
      481 svedm
//
LOCUS       NP_000544               1432 aa            linear   PRI 21-NOV-2025
DEFINITION  bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN [Homo
            sapiens].
ACCESSION   NP_000544
VERSION     NP_000544.2
DBSOURCE    REFSEQ: accession NM_000553.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1432)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1432)
  AUTHORS   Silva,J.P.L., Donaires,F.S., Gutierrez-Rodrigues,F., Martins,D.J.,
            Carvalho,V.S., Santana,B.A., Cunha,R.L.G., Kajigaya,S.,
            Menck,C.F.M., Young,N.S., Kjeldsen,E. and Calado,R.T.
  TITLE     RecQ helicase expression in patients with telomeropathies
  JOURNAL   Mol Biol Rep 51 (1), 754 (2024)
   PUBMED   38874681
  REMARK    GeneRIF: RecQ helicase expression in patients with telomeropathies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1432)
  AUTHORS   Yoon,J.H., Sellamuthu,K., Prakash,L. and Prakash,S.
  TITLE     WRN exonuclease imparts high fidelity on translesion synthesis by Y
            family DNA polymerases
  JOURNAL   Genes Dev 38 (5-6), 213-232 (2024)
   PUBMED   38503516
  REMARK    GeneRIF: WRN exonuclease imparts high fidelity on translesion
            synthesis by Y family DNA polymerases.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1432)
  AUTHORS   Zong,D., Koussa,N.C., Cornwell,J.A., Pankajam,A.V., Kruhlak,M.J.,
            Wong,N., Chari,R., Cappell,S.D. and Nussenzweig,A.
  TITLE     Comprehensive mapping of cell fates in microsatellite unstable
            cancer cells supports dual targeting of WRN and ATR
  JOURNAL   Genes Dev 37 (19-20), 913-928 (2023)
   PUBMED   37932011
  REMARK    GeneRIF: Comprehensive mapping of cell fates in microsatellite
            unstable cancer cells supports dual targeting of WRN and ATR.
REFERENCE   5  (residues 1 to 1432)
  AUTHORS   Shin,S., Hyun,K., Lee,J., Joo,D., Kulikowicz,T., Bohr,V.A., Kim,J.
            and Hohng,S.
  TITLE     Werner syndrome protein works as a dimer for unwinding and
            replication fork regression
  JOURNAL   Nucleic Acids Res 51 (1), 337-348 (2023)
   PUBMED   36583333
  REMARK    GeneRIF: Werner syndrome protein works as a dimer for unwinding and
            replication fork regression.
REFERENCE   6  (residues 1 to 1432)
  AUTHORS   Matsumoto,T., Imamura,O., Yamabe,Y., Kuromitsu,J., Tokutake,Y.,
            Shimamoto,A., Suzuki,N., Satoh,M., Kitao,S., Ichikawa,K.,
            Kataoka,H., Sugawara,K., Thomas,W., Mason,B., Tsuchihashi,Z.,
            Drayna,D., Sugawara,M., Sugimoto,M., Furuichi,Y. and Goto,M.
  TITLE     Mutation and haplotype analyses of the Werner's syndrome gene based
            on its genomic structure: genetic epidemiology in the Japanese
            population
  JOURNAL   Hum Genet 100 (1), 123-130 (1997)
   PUBMED   9225981
REFERENCE   7  (residues 1 to 1432)
  AUTHORS   Ye,L., Miki,T., Nakura,J., Oshima,J., Kamino,K., Rakugi,H.,
            Ikegami,H., Higaki,J., Edland,S.D., Martin,G.M. and Ogihara,T.
  TITLE     Association of a polymorphic variant of the Werner helicase gene
            with myocardial infarction in a Japanese population
  JOURNAL   Am J Med Genet 68 (4), 494-498 (1997)
   PUBMED   9021029
  REMARK    Erratum:[Am J Med Genet 1997 May 2;70(1):103]
REFERENCE   8  (residues 1 to 1432)
  AUTHORS   Yu,C.E., Oshima,J., Fu,Y.H., Wijsman,E.M., Hisama,F., Alisch,R.,
            Matthews,S., Nakura,J., Miki,T., Ouais,S., Martin,G.M., Mulligan,J.
            and Schellenberg,G.D.
  TITLE     Positional cloning of the Werner's syndrome gene
  JOURNAL   Science 272 (5259), 258-262 (1996)
   PUBMED   8602509
REFERENCE   9  (residues 1 to 1432)
  AUTHORS   Oshima,J., Martin,G.M. and Hisama,F.M.
  TITLE     Werner Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301687
REFERENCE   10 (residues 1 to 1432)
  AUTHORS   Goto,M., Rubenstein,M., Weber,J., Woods,K. and Drayna,D.
  TITLE     Genetic linkage of Werner's syndrome to five markers on chromosome
            8
  JOURNAL   Nature 355 (6362), 735-738 (1992)
   PUBMED   1741060
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC084736.5 and AC009563.12.
            
            On Jul 26, 2006 this sequence version replaced NP_000544.1.
            
            Summary: This gene encodes a member of the RecQ subfamily of DNA
            helicase proteins. The encoded nuclear protein is important in the
            maintenance of genome stability and plays a role in DNA repair,
            replication, transcription and telomere maintenance. This protein
            contains a N-terminal 3' to 5' exonuclease domain, an ATP-dependent
            helicase domain and RQC (RecQ helicase conserved region) domain in
            its central region, and a C-terminal HRDC (helicase RNase D
            C-terminal) domain and nuclear localization signal. Defects in this
            gene are the cause of Werner syndrome, an autosomal recessive
            disorder characterized by accelerated aging and an elevated risk
            for certain cancers. [provided by RefSeq, Aug 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.890559.1, AF091214.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000298139.7/ ENSP00000298139.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p12"
     Protein         1..1432
                     /product="bifunctional 3'-5' exonuclease/ATP-dependent
                     helicase WRN"
                     /EC_number="5.6.2.4"
                     /note="Werner syndrome ATP-dependent helicase; Werner
                     syndrome protein; Werner syndrome, RecQ helicase-like;
                     exonuclease WRN; recQ protein-like 2; DNA helicase,
                     RecQ-like type 3; Werner syndrome RecQ like helicase"
                     /calculated_mol_wt=162331
     Region          2..277
                     /region_name="Interaction with WRNIP1.
                     /evidence=ECO:0000250|UniProtKB:O09053"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14191.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q14191.2)"
     Region          11..23
                     /region_name="KBM 1.
                     /evidence=ECO:0000305|PubMed:27063109"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14191.2)"
     Region          61..229
                     /region_name="RNaseD_like"
                     /note="DEDDy 3'-5' exonuclease domain of RNase D, WRN, and
                     similar proteins; cd06129"
                     /db_xref="CDD:176650"
     Site            order(82..85,138..139,141..143,176..177,212,216)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176650"
     Site            order(82,84,143,212,216)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176650"
     Site            order(83..85,138..139,141..142,176..177,212,216)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:176650"
     Site            145
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000305|PubMed:20159463; propagated from
                     UniProtKB/Swiss-Prot (Q14191.2)"
     Region          <156..480
                     /region_name="PTZ00341"
                     /note="Ring-infected erythrocyte surface antigen;
                     Provisional"
                     /db_xref="CDD:173534"
     Region          424..477
                     /region_name="2 X 27 AA tandem repeats of
                     H-L-S-P-N-D-N-E-N-D-T-S-Y-V-I-E-S-D-E-D-L-E-M-E-M-L-K"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14191.2)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q14191.2)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q14191.2)"
     Site            453
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q14191.2)"
     Site            467
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q14191.2)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14191.2)"
     Region          498..529
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14191.2)"
     Region          538..1010
                     /region_name="recQ_fam"
                     /note="ATP-dependent DNA helicase, RecQ family; TIGR00614"
                     /db_xref="CDD:129701"
     Region          668..671
                     /region_name="DEAH box.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00541"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14191.2)"
     Region          987..993
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000269|PubMed:20159463"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14191.2)"
     Site            1037
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000305|PubMed:20159463; propagated from
                     UniProtKB/Swiss-Prot (Q14191.2)"
     Site            1133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14191.2)"
     Region          1156..1229
                     /region_name="HRDC"
                     /note="Helicase and RNase D C-terminal; smart00341"
                     /db_xref="CDD:128635"
     Region          1258..1352
                     /region_name="HTH_40"
                     /note="Helix-turn-helix domain; pfam14493"
                     /db_xref="CDD:464189"
     Site            1400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14191.2)"
     Region          1403..1412
                     /region_name="KBM 2.
                     /evidence=ECO:0000305|PubMed:27063109"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14191.2)"
     Region          1419..1432
                     /region_name="XLM. /evidence=ECO:0000305|PubMed:27063109"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14191.2)"
     CDS             1..1432
                     /gene="WRN"
                     /gene_synonym="RECQ3; RECQL2; RECQL3"
                     /coded_by="NM_000553.6:241..4539"
                     /db_xref="CCDS:CCDS6082.1"
                     /db_xref="GeneID:7486"
                     /db_xref="HGNC:HGNC:12791"
                     /db_xref="MIM:604611"
ORIGIN      
        1 msekkletta qqrkcpewmn vqnkrcavee rkacvrksvf eddlpfleft gsivysydas
       61 dcsflsedis mslsdgdvvg fdmewpplyn rgklgkvali qlcvseskcy lfhvssmsvf
      121 pqglkmllen kavkkagvgi egdqwkllrd fdiklknfve ltdvankklk ctetwslnsl
      181 vkhllgkqll kdksircsnw skfpltedqk lyaatdayag fiiyrnleil ddtvqrfain
      241 keeeillsdm nkqltsisee vmdlakhlph afsklenprr vsillkdise nlyslrrmii
      301 gstnietelr psnnlnllsf edsttggvqq kqirehevli hvedetwdpt ldhlakhdge
      361 dvlgnkverk edgfedgved nklkenmera clmslditeh elqileqqsq eeylsdiayk
      421 stehlspndn endtsyvies dedlememlk hlspndnend tsyviesded lememlksle
      481 nlnsgtvept hskclkmern lglptkeeee ddeneanege edddkdflwp apneeqvtcl
      541 kmyfghssfk pvqwkvihsv leerrdnvav matgygkslc fqyppvyvgk iglvisplis
      601 lmedqvlqlk msnipacflg saqsenvltd iklgkyrivy vtpeycsgnm gllqqleadi
      661 gitliavdea hcisewghdf rdsfrklgsl ktalpmvpiv altatasssi redivrclnl
      721 rnpqitctgf drpnlylevr rktgnilqdl qpflvktssh wefegptiiy cpsrkmtqqv
      781 tgelrklnls cgtyhagmsf strkdihhrf vrdeiqcvia tiafgmgink adirqvihyg
      841 apkdmesyyq eigragrdgl qsschvlwap adinlnrhll teirnekfrl yklkmmakme
      901 kylhssrcrr qiilshfedk qvqkaslgim gtekccdncr srldhcysmd dsedtswdfg
      961 pqafkllsav dilgekfgig lpilflrgsn sqrladqyrr hslfgtgkdq teswwkafsr
     1021 qlitegflve vsrynkfmki caltkkgrnw lhkantesqs lilqaneelc pkklllpssk
     1081 tvssgtkehc ynqvpvelst ekksnlekly sykpcdkiss gsniskksim vqspekayss
     1141 sqpvisaqeq etqivlygkl vearqkhank mdvppailat nkilvdmakm rpttvenvkr
     1201 idgvsegkaa mlapllevik hfcqtnsvqt dlfsstkpqe eqktslvakn kictlsqsma
     1261 ityslfqekk mplksiaesr ilplmtigmh lsqavkagcp ldleragltp evqkiiadvi
     1321 rnppvnsdms kislirmlvp enidtylihm aieilkhgpd sglqpscdvn krrcfpgsee
     1381 icssskrske evgintetss aerkrrlpvw fakgsdtskk lmdktkrggl fs
//
LOCUS       NP_932173               2016 aa            linear   PRI 21-NOV-2025
DEFINITION  sodium channel protein type 5 subunit alpha isoform a [Homo
            sapiens].
ACCESSION   NP_932173 XP_945788
VERSION     NP_932173.1
DBSOURCE    REFSEQ: accession NM_198056.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2016)
  AUTHORS   Hu,Y., Zhang,C., Wang,S., Xiong,H., Xie,W., Zeng,Z., Cai,H.,
            Wang,Q.K. and Lu,Z.
  TITLE     14-3-3epsilon/YWHAE regulates the transcriptional expression of
            cardiac sodium channel NaV1.5
  JOURNAL   Heart Rhythm 21 (11), 2320-2329 (2024)
   PUBMED   38750908
  REMARK    GeneRIF: 14-3-3epsilon/YWHAE regulates the transcriptional
            expression of cardiac sodium channel NaV1.5.
REFERENCE   2  (residues 1 to 2016)
  AUTHORS   Cadena-Ullauri,S., Guevara-Ramirez,P., Ruiz-Pozo,V.A.,
            Tamayo-Trujillo,R., Paz-Cruz,E., Simancas-Racines,D.,
            Ibarra-Castillo,R., Laso-Bayas,J.L. and Zambrano,A.K.
  TITLE     Genomic analysis of an Ecuadorian individual carrying an SCN5A rare
            variant
  JOURNAL   BMC Cardiovasc Disord 24 (1), 388 (2024)
   PUBMED   39068398
  REMARK    GeneRIF: Genomic analysis of an Ecuadorian individual carrying an
            SCN5A rare variant.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2016)
  AUTHORS   Tariq,U., Sarkar,S., Malladi,N., Kumar,R., Bugga,P., Chakraborty,P.
            and Banerjee,S.K.
  TITLE     Knockdown of SCN5A alters metabolic-associated genes and aggravates
            hypertrophy in the cardiomyoblast
  JOURNAL   Mol Biol Rep 51 (1), 661 (2024)
   PUBMED   38758505
  REMARK    GeneRIF: Knockdown of SCN5A alters metabolic-associated genes and
            aggravates hypertrophy in the cardiomyoblast.
            Erratum:[Mol Biol Rep. 2024 Jul 26;51(1):852. doi:
            10.1007/s11033-024-09742-9. PMID: 39060789]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2016)
  AUTHORS   Wright,K.M., Nathan,S., Jiang,H., Xia,W., Kim,H., Chakouri,N.,
            Nwafor,J.N., Fossier,L., Srinivasan,L., Chen,Z., Boronina,T.,
            Post,J., Paul,S., Cole,R.N., Ben-Johny,M., Cole,P.A. and
            Gabelli,S.B.
  TITLE     NEDD4L intramolecular interactions regulate its auto and substrate
            NaV1.5 ubiquitination
  JOURNAL   J Biol Chem 300 (3), 105715 (2024)
   PUBMED   38309503
  REMARK    GeneRIF: NEDD4L intramolecular interactions regulate its auto and
            substrate NaV1.5 ubiquitination.
REFERENCE   5  (residues 1 to 2016)
  AUTHORS   George,A.L. Jr., Varkony,T.A., Drabkin,H.A., Han,J., Knops,J.F.,
            Finley,W.H., Brown,G.B., Ward,D.C. and Haas,M.
  TITLE     Assignment of the human heart tetrodotoxin-resistant voltage-gated
            Na+ channel alpha-subunit gene (SCN5A) to band 3p21
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 67-70 (1995)
   PUBMED   7956363
REFERENCE   6  (residues 1 to 2016)
  AUTHORS   Jiang,C., Atkinson,D., Towbin,J.A., Splawski,I., Lehmann,M.H.,
            Li,H., Timothy,K., Taggart,R.T., Schwartz,P.J., Vincent,G.M. et al.
  TITLE     Two long QT syndrome loci map to chromosomes 3 and 7 with evidence
            for further heterogeneity
  JOURNAL   Nat Genet 8 (2), 141-147 (1994)
   PUBMED   7842012
REFERENCE   7  (residues 1 to 2016)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   8  (residues 1 to 2016)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 2016)
  AUTHORS   Groffen,A.J., Bikker,H. and Christiaans,I.
  TITLE     Long QT Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301308
REFERENCE   10 (residues 1 to 2016)
  AUTHORS   Gellens,M.E., George,A.L. Jr., Chen,L.Q., Chahine,M., Horn,R.,
            Barchi,R.L. and Kallen,R.G.
  TITLE     Primary structure and functional expression of the human cardiac
            tetrodotoxin-insensitive voltage-dependent sodium channel
  JOURNAL   Proc Natl Acad Sci U S A 89 (2), 554-558 (1992)
   PUBMED   1309946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP006241.1, BU845010.1,
            M77235.1, AB158469.2 and AF482988.1.
            
            On Mar 4, 2006 this sequence version replaced XP_945788.1.
            
            Summary: The protein encoded by this gene is an integral membrane
            protein and tetrodotoxin-resistant voltage-gated sodium channel
            subunit. This protein is found primarily in cardiac muscle and is
            responsible for the initial upstroke of the action potential in an
            electrocardiogram. Defects in this gene have been associated with
            long QT syndrome type 3 (LQT3), atrial fibrillation,
            cardiomyopathy, and Brugada syndrome 1, all autosomal dominant
            cardiac diseases. Alternative splicing results in several
            transcript variants encoding different isoforms. [provided by
            RefSeq, May 2022].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M77235.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2016
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.2"
     Protein         1..2016
                     /product="sodium channel protein type 5 subunit alpha
                     isoform a"
                     /note="cardiac tetrodotoxin-insensitive voltage-dependent
                     sodium channel alpha subunit; sodium channel protein type
                     5 subunit alpha; voltage-gated sodium channel subunit
                     alpha Nav1.5; sodium channel protein cardiac muscle
                     subunit alpha; sodium channel, voltage-gated, type V,
                     alpha subunit"
                     /calculated_mol_wt=226810
     Region          28..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Region          113..420
                     /region_name="I. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          130..423
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            130..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            158..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            189..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            214
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            217..236
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            250..272
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            283
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            288
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            291
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            318
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:P15389; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            328
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            387..413
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            457
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Region          461..591
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P15389; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Region          507..667
                     /region_name="Na_trans_cytopl"
                     /note="Cytoplasmic domain of voltage-gated Na+ ion
                     channel; pfam11933"
                     /db_xref="CDD:463401"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            513
                     /site_type="methylation"
                     /note="Dimethylated arginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            526
                     /site_type="methylation"
                     /note="Dimethylated arginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JJV9; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            680
                     /site_type="methylation"
                     /note="Dimethylated arginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Region          699..969
                     /region_name="II. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          716..927
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            720..737
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            740
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            747..769
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            776..796
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            803
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            807..821
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            839..860
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            864
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            913..941
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          953..1200
                     /region_name="Na_trans_assoc"
                     /note="Sodium ion transport-associated; pfam06512"
                     /db_xref="CDD:461936"
     Region          1005..1141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          1187..1501
                     /region_name="III. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          1204..1479
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1204..1225
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1237..1259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1269..1291
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1298..1317
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1331..1355
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1365
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1374
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1388
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1446..1470
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          1471..1523
                     /region_name="Na_channel_gate"
                     /note="Inactivation gate of the voltage-gated sodium
                     channel alpha subunits; cd13433"
                     /db_xref="CDD:240441"
     Site            1485..1488
                     /site_type="other"
                     /note="putative hydrophobic latch"
                     /db_xref="CDD:240441"
     Site            1503
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000305|PubMed:19666841; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Region          1510..1807
                     /region_name="IV. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          1528..1782
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1529..1547
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1559..1580
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1590..1612
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1620..1640
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1651..1679
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1736
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1746..1771
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          1839..1901
                     /region_name="Interaction with FGF13.
                     /evidence=ECO:0000269|PubMed:22705208"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          1959..2016
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          1974..1977
                     /region_name="Interaction with NEDD4, NEDD4L and WWP2.
                     /evidence=ECO:0000269|PubMed:15548568"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     CDS             1..2016
                     /gene="SCN5A"
                     /gene_synonym="CDCD2; CMD1E; CMPD2; HB1; HB2; HBBD; HH1;
                     ICCD; IVF; LQT3; Nav1.5; PFHB1; SSS1; VF1"
                     /coded_by="NM_198056.3:210..6260"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46796.1"
                     /db_xref="GeneID:6331"
                     /db_xref="HGNC:HGNC:10593"
                     /db_xref="MIM:600163"
ORIGIN      
        1 manfllprgt ssfrrftres laaiekrmae kqargsttlq esreglpeee aprpqldlqa
       61 skklpdlygn ppqeligepl edldpfystq ktfivlnkgk tifrfsatna lyvlspfhpi
      121 rraavkilvh slfnmlimct iltncvfmaq hdpppwtkyv eytftaiytf eslvkilarg
      181 fclhaftflr dpwnwldfsv iimayttefv dlgnvsalrt frvlralkti svisglktiv
      241 galiqsvkkl advmvltvfc lsvfaliglq lfmgnlrhkc vrnftalngt ngsveadglv
      301 wesldlylsd penyllkngt sdvllcgnss dagtcpegyr clkagenpdh gytsfdsfaw
      361 aflalfrlmt qdcwerlyqq tlrsagkiym iffmlviflg sfylvnlila vvamayeeqn
      421 qatiaeteek ekrfqeamem lkkehealti rgvdtvsrss lemsplapvn sherrskrrk
      481 rmssgteecg edrlpksdse dgpramnhls ltrglsrtsm kprssrgsif tfrrrdlgse
      541 adfaddenst ageseshhts llvpwplrrt saqgqpspgt sapghalhgk knstvdcngv
      601 vsllgagdpe atspgshllr pvmlehppdt ttpseepggp qmltsqapcv dgfeepgarq
      661 ralsavsvlt saleeleesr hkcppcwnrl aqryliwecc plwmsikqgv klvvmdpftd
      721 ltitmcivln tlfmalehyn mtsefeemlq vgnlvftgif taemtfkiia ldpyyyfqqg
      781 wnifdsiivi lslmelglsr msnlsvlrsf rllrvfklak swptlntlik iignsvgalg
      841 nltlvlaiiv fifavvgmql fgknyselrd sdsgllprwh mmdffhafli ifrilcgewi
      901 etmwdcmevs gqslcllvfl lvmvignlvv lnlflallls sfsadnltap dedremnnlq
      961 lalariqrgl rfvkrttwdf ccgllrqrpq kpaalaaqgq lpsciatpys ppppetekvp
     1021 ptrketrfee geqpgqgtpg dpepvcvpia vaesdtddqe edeenslgte eesskqqesq
     1081 pvsggpeapp dsrtwsqvsa tasseaeasa sqadwrqqwk aepqapgcge tpedscsegs
     1141 tadmtntael leqipdlgqd vkdpedcfte gcvrrcpcca vdttqapgkv wwrlrktcyh
     1201 ivehswfetf iifmillssg alafediyle erktikvlle yadkmftyvf vlemllkwva
     1261 ygfkkyftna wcwldflivd vslvslvant lgfaemgpik slrtlralrp lralsrfegm
     1321 rvvvnalvga ipsimnvllv clifwlifsi mgvnlfagkf grcinqtegd lplnytivnn
     1381 ksqceslnlt gelywtkvkv nfdnvgagyl allqvatfkg wmdimyaavd srgyeeqpqw
     1441 eynlymyiyf vifiifgsff tlnlfigvii dnfnqqkkkl ggqdifmtee qkkyynamkk
     1501 lgskkpqkpi prplnkyqgf ifdivtkqaf dvtimflicl nmvtmmvetd dqspekinil
     1561 akinllfvai ftgecivkla alrhyyftns wnifdfvvvi lsivgtvlsd iiqkyffspt
     1621 lfrvirlari grilrlirga kgirtllfal mmslpalfni glllflvmfi ysifgmanfa
     1681 yvkweagidd mfnfqtfans mlclfqitts agwdgllspi lntgppycdp tlpnsngsrg
     1741 dcgspavgil ffttyiiisf livvnmyiai ilenfsvate esteplsedd fdmfyeiwek
     1801 fdpeatqfie ysvlsdfada lseplriakp nqislinmdl pmvsgdrihc mdilfaftkr
     1861 vlgesgemda lkiqmeekfm aanpskisye pitttlrrkh eevsamviqr afrrhllqrs
     1921 lkhasflfrq qagsglseed aperegliay vmsenfsrpl gppssssiss tsfppsydsv
     1981 tratsdnlqv rgsdyshsed ladfppspdr dresiv
//
LOCUS       NP_001363284             810 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger CCCH domain-containing protein 11A isoform 1 [Homo
            sapiens].
ACCESSION   NP_001363284
VERSION     NP_001363284.1
DBSOURCE    REFSEQ: accession NM_001376355.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Kases,K., Schubert,E., Hajikhezri,Z., Larsson,M., Devi,P.,
            Darweesh,M., Andersson,L., Akusjarvi,G., Punga,T. and Younis,S.
  TITLE     The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts
  JOURNAL   J Biol Chem 299 (8), 104959 (2023)
   PUBMED   37356722
  REMARK    GeneRIF: The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts.
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 810)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 810)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114402.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.7024.1, SRR1803613.1241.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..810
                     /product="zinc finger CCCH domain-containing protein 11A
                     isoform 1"
                     /note="zinc finger CCCH-type domain containing 11A; zinc
                     finger CCCH domain-containing protein 11A"
                     /calculated_mol_wt=89000
     Region          1..110
                     /region_name="zf-CCCH_3"
                     /note="Zinc-finger containing family; pfam15663"
                     /db_xref="CDD:464787"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          139..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          223..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          285..351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          367..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          482..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          715..768
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     CDS             1..810
                     /gene="ZC3H11A"
                     /gene_synonym="ZC3HDC11A"
                     /coded_by="NM_001376355.1:413..2845"
                     /note="isoform 1 is encoded by transcript variant 31"
                     /db_xref="CCDS:CCDS30978.1"
                     /db_xref="GeneID:9877"
                     /db_xref="HGNC:HGNC:29093"
                     /db_xref="MIM:613513"
ORIGIN      
        1 mpnqgedcyf ffystctkgd scpfrhceaa ignetvctlw qegrcfrqvc rfrhmeidkk
       61 rseipcywen qptgcqklnc afhhnrgryv dglflppskt vlptvpespe eevkasqlsv
      121 qqnklsvqsn pspqlrsvmk vessenvpsp thppvvinaa dddeddddqf seegdetktp
      181 tlqptpevhn glrvtsvrkp avnikqgecl nfgiktleei kskkmkeksk kqgegssgvs
      241 slllhpepvp gpekenvrtv vrtvtlstkq geeplvrlsl terlgkrkfs aggdsdpplk
      301 rslaqrlgkk veapetnidk tpkkaqvsks lkerlgmsad pdnedatdkv nkvgeihvkt
      361 leeilleras qkrgelqtkl ktegpsktdd stsgarssst iriktfsevl aekkhrqqea
      421 erqkskkdtt ciklkidsei kktvvlppiv asrgqseepa gktksmqevh iktleeikle
      481 kalrvqqsse sstsspsqhe atpgarrllr itkrtgmkee knlqegnevd sqssirteak
      541 easgettgvd itkiqvkrce tmrekhmqkq qereksvltp lrgdvascnt qvaekpvlta
      601 vpgitrhltk rlptkssqkv evetsgigds llnvkcaaqt lekrgkakpk vnvkpsvvkv
      661 vsspklapkr kavemhaavi aavkplssss vlqeppakka avavvplvse dksvtvpeae
      721 nprdslvlpp tqsssdsspp evsgpsssqm smktrrlssa stgkpplsve ddfekliwei
      781 sggkleaeid ldpgkdeddl llelsemids
//
LOCUS       NP_001071171             486 aa            linear   PRI 21-NOV-2025
DEFINITION  mesoderm induction early response protein 1 isoform e [Homo
            sapiens].
ACCESSION   NP_001071171
VERSION     NP_001071171.2
DBSOURCE    REFSEQ: accession NM_001077703.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Wang,S., Fairall,L., Pham,T.K., Ragan,T.J., Vashi,D., Collins,M.O.,
            Dominguez,C. and Schwabe,J.W.R.
  TITLE     A potential histone-chaperone activity for the MIER1 histone
            deacetylase complex
  JOURNAL   Nucleic Acids Res 51 (12), 6006-6019 (2023)
   PUBMED   37099381
  REMARK    GeneRIF: A potential histone-chaperone activity for the MIER1
            histone deacetylase complex.
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 486)
  AUTHORS   McCarthy,P.L., Mercer,F.C., Savicky,M.W., Carter,B.A., Paterno,G.D.
            and Gillespie,L.L.
  TITLE     Changes in subcellular localisation of MI-ER1 alpha, a novel
            oestrogen receptor-alpha interacting protein, is associated with
            breast cancer progression
  JOURNAL   Br J Cancer 99 (4), 639-646 (2008)
   PUBMED   18665173
  REMARK    GeneRIF: Loss of nuclear MI-ER1 alpha might contribute to the
            development of invasive breast carcinoma
REFERENCE   6  (residues 1 to 486)
  AUTHORS   Wang,L., Charroux,B., Kerridge,S. and Tsai,C.C.
  TITLE     Atrophin recruits HDAC1/2 and G9a to modify histone H3K9 and to
            determine cell fates
  JOURNAL   EMBO Rep 9 (6), 555-562 (2008)
   PUBMED   18451879
REFERENCE   7  (residues 1 to 486)
  AUTHORS   Ding,Z., Gillespie,L.L., Mercer,F.C. and Paterno,G.D.
  TITLE     The SANT domain of human MI-ER1 interacts with Sp1 to interfere
            with GC box recognition and repress transcription from its own
            promoter
  JOURNAL   J Biol Chem 279 (27), 28009-28016 (2004)
   PUBMED   15117948
  REMARK    GeneRIF: the association of hMI-ER1 with Sp1 represents a novel
            mechanism for the negative regulation of Sp1 target promoters
REFERENCE   8  (residues 1 to 486)
  AUTHORS   Ding,Z., Gillespie,L.L. and Paterno,G.D.
  TITLE     Human MI-ER1 alpha and beta function as transcriptional repressors
            by recruitment of histone deacetylase 1 to their conserved ELM2
            domain
  JOURNAL   Mol Cell Biol 23 (1), 250-258 (2003)
   PUBMED   12482978
  REMARK    GeneRIF: we investigated the role of hMI-ER1alpha and hMI-ER1beta
            in the regulation of transcription.We demonstrate that this
            repressor activity is due to interaction and recruitment of a
            trichostatin A-sensitive histone deacetylase 1 (HDAC1).
REFERENCE   9  (residues 1 to 486)
  AUTHORS   Paterno,G.D., Ding,Z., Lew,Y.Y., Nash,G.W., Mercer,F.C. and
            Gillespie,L.L.
  TITLE     Genomic organization of the human mi-er1 gene and characterization
            of alternatively spliced isoforms: regulated use of a facultative
            intron determines subcellular localization
  JOURNAL   Gene 295 (1), 79-88 (2002)
   PUBMED   12242014
  REMARK    GeneRIF: Results demonstrate that alternate use of a facultative
            intron regulates the subcellular localization of hMI-ER1 proteins
            and this may have important implications for hMI-ER1 function.
REFERENCE   10 (residues 1 to 486)
  AUTHORS   Paterno,G.D., Mercer,F.C., Chayter,J.J., Yang,X., Robb,J.D. and
            Gillespie,L.L.
  TITLE     Molecular cloning of human er1 cDNA and its differential expression
            in breast tumours and tumour-derived cell lines
  JOURNAL   Gene 222 (1), 77-82 (1998)
   PUBMED   9813250
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK302061.1, AY124187.1,
            AL500525.4 and BM987758.1.
            
            On Mar 28, 2009 this sequence version replaced NP_001071171.1.
            
            Summary: This gene encodes a protein that was first identified in
            Xenopus laevis by its role in a mesoderm induction early response
            (MIER). The encoded protein functions as a transcriptional
            regulator. Alternatively spliced transcript variants encode
            multiple isoforms, some of which lack a C-terminal nuclear
            localization signal. [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (5) lacks an alternate exon in the
            5' coding region, uses an alternate upstream translation start
            site, and lacks an alternate segment in the 3' coding region,
            compared to variant 1. The resulting isoform (e) has a longer and
            distinct N-terminus and a shorter and distinct C-terminus, compared
            to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.164866.1,
                                           SRR1803611.163451.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..486
                     /product="mesoderm induction early response protein 1
                     isoform e"
                     /note="mesoderm induction early response protein 1;
                     mesoderm induction early response 1 homolog; mesoderm
                     induction early response 1, transcriptional regulator"
                     /calculated_mol_wt=54410
     Region          235..284
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          341..385
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(341,371..372,374..375,377..379,381..383)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          395..>460
                     /region_name="MIER1_3_C"
                     /note="Mesoderm induction early response protein 1/3
                     C-terminal; pfam19426"
                     /db_xref="CDD:437258"
     CDS             1..486
                     /gene="MIER1"
                     /gene_synonym="ER1; MI-ER1"
                     /coded_by="NM_001077703.3:40..1500"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS53325.1"
                     /db_xref="GeneID:57708"
                     /db_xref="HGNC:HGNC:29657"
                     /db_xref="MIM:616848"
ORIGIN      
        1 mdgassgggg sseggggssg sgygvvarfs qclaefrtwl rtnwlrfnad ktdvmlpsve
       61 ssspggsats ddhefdpsad mlvhdfdder tleeeemmeg etnfsseied laregdmpih
      121 ellslygygs tvrlpeedee eeeeeeeged dedadnddns gcsgenkeen ikdssgqede
      181 tqssnddpsq svasqdaqei irprrckyfd tnseveeese ededyipsed wkkeimvgsm
      241 fqaeipvgic rykenekvye nddqllwdpe ylpedkviif lkdasrrtgd ekgveaipeg
      301 shikdneqal yelvkcnfdt eealrrlrfn vkaareelsv wteeecrnfe qglkaygkdf
      361 hliqankvrt rsvgecvafy ymwkkseryd ffaqqtrfgk kkynlhpgvt dymdrlldes
      421 esaassraps ppptasnssn sqsekedgtv stanqngvss ngpgilqmll pvhfsaissr
      481 anaflk
//
LOCUS       NP_001316678             303 aa            linear   PRI 21-NOV-2025
DEFINITION  N-terminal EF-hand calcium-binding protein 2 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001316678 XP_011521437
VERSION     NP_001316678.1
DBSOURCE    REFSEQ: accession NM_001329749.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Bueno,D., Narayan Dey,P., Schacht,T., Wolf,C., Wullner,V.,
            Morpurgo,E., Rojas-Charry,L., Sessinghaus,L., Leukel,P., Sommer,C.,
            Radyushkin,K., Florin,L., Baumgart,J., Stamm,P., Daiber,A.,
            Horta,G., Nardi,L., Vasic,V., Schmeisser,M.J., Hellwig,A.,
            Oskamp,A., Bauer,A., Anand,R., Reichert,A.S., Ritz,S., Nocera,G.,
            Jacob,C., Peper,J., Silies,M., Frauenknecht,K.B.M., Schafer,M.K.E.
            and Methner,A.
  TITLE     NECAB2 is an endosomal protein important for striatal function
  JOURNAL   Free Radic Biol Med 208, 643-656 (2023)
   PUBMED   37722569
  REMARK    GeneRIF: NECAB2 is an endosomal protein important for striatal
            function.
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Zhang,M.D., Barde,S., Szodorai,E., Josephson,A., Mitsios,N.,
            Watanabe,M., Attems,J., Lubec,G., Kovacs,G.G., Uhlen,M., Mulder,J.,
            Harkany,T. and Hokfelt,T.
  TITLE     Comparative anatomical distribution of neuronal calcium-binding
            protein (NECAB) 1 and -2 in rodent and human spinal cord
  JOURNAL   Brain Struct Funct 221 (7), 3803-3823 (2016)
   PUBMED   26843217
  REMARK    GeneRIF: Study suggests that the phenotypic segregation of Neuronal
            calcium-binding protein 1 and -2 (NECAB1 and -2) to respective
            excitatory and inhibitory spinal systems can underpin functional
            modalities in determining the fidelity of synaptic
            neurotransmission and neuronal responsiveness, and might bear
            translational relevance to humans.
            Erratum:[Brain Struct Funct. 2016 Sep;221(7):3843. doi:
            10.1007/s00429-016-1236-7. PMID: 27206425]
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Canela,L., Fernandez-Duenas,V., Albergaria,C., Watanabe,M.,
            Lluis,C., Mallol,J., Canela,E.I., Franco,R., Lujan,R. and
            Ciruela,F.
  TITLE     The association of metabotropic glutamate receptor type 5 with the
            neuronal Ca2+-binding protein 2 modulates receptor function
  JOURNAL   J Neurochem 111 (2), 555-567 (2009)
   PUBMED   19694902
  REMARK    GeneRIF: NECAB2 by its physical interaction with mGlu(5b) receptor
            modulates receptor function
REFERENCE   8  (residues 1 to 303)
  AUTHORS   Canela,L., Lujan,R., Lluis,C., Burgueno,J., Mallol,J., Canela,E.I.,
            Franco,R. and Ciruela,F.
  TITLE     The neuronal Ca(2+) -binding protein 2 (NECAB2) interacts with the
            adenosine A(2A) receptor and modulates the cell surface expression
            and function of the receptor
  JOURNAL   Mol Cell Neurosci 36 (1), 1-12 (2007)
   PUBMED   17689978
REFERENCE   9  (residues 1 to 303)
  AUTHORS   Sugita,S., Ho,A. and Sudhof,T.C.
  TITLE     NECABs: a family of neuronal Ca(2+)-binding proteins with an
            unusual domain structure and a restricted expression pattern
  JOURNAL   Neuroscience 112 (1), 51-63 (2002)
   PUBMED   12044471
REFERENCE   10 (residues 1 to 303)
  AUTHORS   Bernier,G., Vukovich,W., Neidhardt,L., Herrmann,B.G. and Gruss,P.
  TITLE     Isolation and characterization of a downstream target of Pax6 in
            the mammalian retinal primordium
  JOURNAL   Development 128 (20), 3987-3994 (2001)
   PUBMED   11641222
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC040169.7.
            
            On Jul 27, 2016 this sequence version replaced XP_011521437.1.
            
            Summary: The protein encoded by this gene is a neuronal
            calcium-binding protein that binds to and modulates the function of
            at least two receptors, adenosine A(2A) receptor and metabotropic
            glutamate receptor type 5. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (3) lacks an alternate coding exon
            compared to variant 1. The resulting isoform (3) has a shorter and
            distinct N-terminus compared to isoform 1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2142586 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.3"
     Protein         1..303
                     /product="N-terminal EF-hand calcium-binding protein 2
                     isoform 3"
                     /note="neuronal calcium binding 2; EF-hand calcium-binding
                     protein 2; neuronal calcium-binding protein 2;
                     synaptotagmin-interacting protein 2"
                     /calculated_mol_wt=34191
     Region          205..275
                     /region_name="ABM"
                     /note="Antibiotic biosynthesis monooxygenase; pfam03992"
                     /db_xref="CDD:427635"
     CDS             1..303
                     /gene="NECAB2"
                     /gene_synonym="EFCBP2; stip-2"
                     /coded_by="NM_001329749.2:225..1136"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82019.1"
                     /db_xref="GeneID:54550"
                     /db_xref="HGNC:HGNC:23746"
                     /db_xref="MIM:618130"
ORIGIN      
        1 mmmgscpwrn sssslqmasl mrknwrisft rltlttpnyf vdhmgdyedv lasletlnhs
       61 vlkamgytkk vyeggsnvdq fvtrfllket anqiqsllss vesaveaiee qtsqlrqnhi
      121 kpshsaaqtw cgsptpasap nhklmameqg ktlpsateda keegleaqis rlaeligrle
      181 skalwfdlqq rlsdedgtnm hlqlvrqema vcpeqlsefl dslrqylrgt tgvrncfhit
      241 avrlsdgftf viyefwetee awkrhlqspl ckafrhvkvd tlsqpealsr ilvpaawctv
      301 grd
//
LOCUS       NP_004184               1859 aa            linear   PRI 21-NOV-2025
DEFINITION  Golgi-specific brefeldin A-resistance guanine nucleotide exchange
            factor 1 isoform 1 [Homo sapiens].
ACCESSION   NP_004184
VERSION     NP_004184.1
DBSOURCE    REFSEQ: accession NM_004193.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1859)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1859)
  AUTHORS   Hirano,J., Hayashi,T., Kitamura,K., Nishimura,Y., Shimizu,H.,
            Okamoto,T., Okada,K., Uemura,K., Yeh,M.T., Ono,C., Taguwa,S.,
            Muramatsu,M. and Matsuura,Y.
  TITLE     Enterovirus 3A protein disrupts endoplasmic reticulum homeostasis
            through interaction with GBF1
  JOURNAL   J Virol 98 (7), e0081324 (2024)
   PUBMED   38904364
  REMARK    GeneRIF: Enterovirus 3A protein disrupts endoplasmic reticulum
            homeostasis through interaction with GBF1.
REFERENCE   3  (residues 1 to 1859)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1859)
  AUTHORS   Navare,A.T., Mast,F.D., Olivier,J.P., Bertomeu,T., Neal,M.L.,
            Carpp,L.N., Kaushansky,A., Coulombe-Huntington,J., Tyers,M. and
            Aitchison,J.D.
  TITLE     Viral protein engagement of GBF1 induces host cell vulnerability
            through synthetic lethality
  JOURNAL   J Cell Biol 221 (11) (2022)
   PUBMED   36305789
  REMARK    GeneRIF: Viral protein engagement of GBF1 induces host cell
            vulnerability through synthetic lethality.
REFERENCE   5  (residues 1 to 1859)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1859)
  AUTHORS   Garcia-Mata,R. and Sztul,E.
  TITLE     The membrane-tethering protein p115 interacts with GBF1, an ARF
            guanine-nucleotide-exchange factor
  JOURNAL   EMBO Rep 4 (3), 320-325 (2003)
   PUBMED   12634853
  REMARK    GeneRIF: novel interaction between p115 and Golgi-specific
            brefeldin-A-resistant factor 1 (GBF1)
REFERENCE   7  (residues 1 to 1859)
  AUTHORS   Kawamoto,K., Yoshida,Y., Tamaki,H., Torii,S., Shinotsuka,C.,
            Yamashina,S. and Nakayama,K.
  TITLE     GBF1, a guanine nucleotide exchange factor for ADP-ribosylation
            factors, is localized to the cis-Golgi and involved in membrane
            association of the COPI coat
  JOURNAL   Traffic 3 (7), 483-495 (2002)
   PUBMED   12047556
  REMARK    GeneRIF: detailed subcellular localization to the cis-Golgi
REFERENCE   8  (residues 1 to 1859)
  AUTHORS   Verhoeven,K., Villanova,M., Rossi,A., Malandrini,A., De Jonghe,P.
            and Timmerman,V.
  TITLE     Localization of the gene for the intermediate form of
            Charcot-Marie-Tooth to chromosome 10q24.1-q25.1
  JOURNAL   Am J Hum Genet 69 (4), 889-894 (2001)
   PUBMED   11533914
REFERENCE   9  (residues 1 to 1859)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   10 (residues 1 to 1859)
  AUTHORS   Mansour,S.J., Herbrick,J.A., Scherer,S.W. and Melancon,P.
  TITLE     Human GBF1 is a ubiquitously expressed gene of the sec7 domain
            family mapping to 10q24
  JOURNAL   Genomics 54 (2), 323-327 (1998)
   PUBMED   9828135
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160011.35, AL356420.14 and
            AL121928.13.
            
            Summary: This gene encodes a member of the Sec7 domain family. The
            encoded protein is a guanine nucleotide exchange factor that
            regulates the recruitment of proteins to membranes by mediating GDP
            to GTP exchange. The encoded protein is localized to the Golgi
            apparatus and plays a role in vesicular trafficking by activating
            ADP ribosylation factor 1. The encoded protein has also been
            identified as an important host factor for viral replication.
            Multiple transcript variants have been observed for this gene.
            [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.201996.1, AF068755.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1859
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..1859
                     /product="Golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1 isoform 1"
                     /note="golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1; BFA-resistant GEF 1"
                     /calculated_mol_wt=206316
     Region          1..211
                     /region_name="DCB, DCB:DCB domain and DCB:HUS domain
                     interaction. /evidence=ECO:0000250|UniProtKB:Q9R1D7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          215..266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          <429..>1178
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          530..550
                     /region_name="HUS, DCB:HUS domain interaction.
                     /evidence=ECO:0000250|UniProtKB:Q9R1D7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          619..665
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          699..884
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          886..1370
                     /region_name="Phosphatidylinositol-phosphate binding,
                     required for translocation to the leading edge and for
                     ARF1 activation upon GPCR signaling.
                     /evidence=ECO:0000269|PubMed:22573891"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1284..1335
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1316
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1337
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AMPK.
                     /evidence=ECO:0000269|PubMed:18063581; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1350..1370
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1430..1483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1725..1808
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1773
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1784
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          <1794..1857
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1859
                     /gene="GBF1"
                     /gene_synonym="ARF1GEF; CMT2GG; CMTDI2; CMTDIA"
                     /coded_by="NM_004193.3:261..5840"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7533.1"
                     /db_xref="GeneID:8729"
                     /db_xref="HGNC:HGNC:4181"
                     /db_xref="MIM:603698"
ORIGIN      
        1 mvdkniyiiq geinivvgai krnarwstht pldeerdpll hsfghlkevl nsitelseie
       61 pnvflrpfle virsedttgp itglaltsvn kflsyalidp thegtaegme nmadavthar
      121 fvgtdpasde vvlmkilqvl rtllltpvga hltnesvcei mqscfricfe mrlsellrks
      181 aehtlvdmvq llftrlpqfk eepknyvgtn mkklkmragg msdsskwkkq krsprpprhm
      241 tkvtpgselp tpngttlssn ltggmpfidv ptpissasse aasavvspst dsglefssqt
      301 tskedltdle qpgspgysta tepgsselgv peqpdlqegt hveksqsasv esipevleec
      361 tspadhsdsa svhdmdyvnp rgvrftqssq kegtalvpyg lpcirelfrf lisltnphdr
      421 hnsevmihmg lhlltvales apvaqcqtll glikdemcrh lfqllsierl nlyaaslrvc
      481 fllfesmreh lkfqmemyik klmeiitven pkmpyemkem aleaivqlwr ipsfvtelyi
      541 nydcdyycsn lfeeltklls knafpvsgql ytthllslda lltvidstea hcqakvlnsl
      601 tqqekketar psceivdgtr easntertas dgkavgmasd ipglhlpggg rlppehgksg
      661 csdleeavds gadkkfarkp prfscllpdp relieiknkk kllitgteqf nqkpkkgiqf
      721 lqekglltip mdntevaqwl renprldkkm igefvsdrkn idllesfvst fsfqglrlde
      781 alrlyleafr lpgeapviqr lleafterwm ncngspfans dacfslayav imlntdqhnh
      841 nvrkqnapmt leefrknlkg vnggkdfeqd iledmyhaik neeivmpeeq tglvrenyvw
      901 nvllhrgatp egiflrvpta sydldlftmt wgptiaalsy vfdksleeti iqkaisgfrk
      961 camisahygl sdvfdnliis lckftalsse sienlpsvfg snpkahiaak tvfhlahrhg
     1021 dilregwkni meamlqlfra qllpkamiev edfvdpngki slqreetpsn rgestvlsfv
     1081 swltlsgpeq ssvrgpsten qeakrvalec ikqcdpekmi teskflqles lqelmkalvs
     1141 vtpdeetyde edaafcleml lrivlenrdr vgcvwqtvrd hlyhlcvqaq dfcflverav
     1201 vgllrlairl lrreeisaqv llslrilllm kpsvlsrvsh qvayglhell ktnaanihsg
     1261 ddwatlftll ecigsgvkpp aalqatarad apdagaqsds elpsyhqndv sldrgytsds
     1321 evytdhgrpg kihrsatdad vvnsgwlvvg kddvdnskpg psrpgpspli nqysltvgld
     1381 lgphdtksll kcveslsfiv rdaahitpdn felcvktlri fveaslnggc ksqekrgksh
     1441 kydskgnrfk kkskegsmlr rprtssqhas rggqsddded egvpasyhtv slqvsqdlld
     1501 lmhtlhtraa siysswaeeq rhletggqki eadsrtlwah cwcpllqgia clccdarrqv
     1561 rmqaltylqr allvhdlqkl dalewescfn kvlfplltkl lenispadvg gmeetrmras
     1621 tllskvflqh lspllslstf aalwltildf mdkymhagss dllseaipes lknmllvmdt
     1681 aeifhsadar gggpsalwei tweridcflp hlrdelfkqt viqdpmpmep qgqkplasah
     1741 ltsaagdtrt pghppppeip selgacdfek pespraasss spgspvassp srlsptpdgp
     1801 pplaqpplil qplasplqvg vppmtlpiil npalieatsp vpllatprpt dpiptsevn
//
LOCUS       NP_060215               1721 aa            linear   PRI 21-NOV-2025
DEFINITION  BCL-6 corepressor isoform a [Homo sapiens].
ACCESSION   NP_060215
VERSION     NP_060215.4
DBSOURCE    REFSEQ: accession NM_017745.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1721)
  AUTHORS   Batkova,M., Havlovicova,M., Nocar,A., Dudakova,L., Macek,M.,
            Liskova,P. and Dostalova,T.
  TITLE     Dental abnormalities observed in the oculo-facio-cardio-dental
            (OFCD) syndrome present in two Czech families bearing novel de novo
            BCOR pathogenic variants
  JOURNAL   BMC Oral Health 24 (1), 1264 (2024)
   PUBMED   39438869
  REMARK    GeneRIF: Dental abnormalities observed in the
            oculo-facio-cardio-dental (OFCD) syndrome present in two Czech
            families bearing novel de novo BCOR pathogenic variants.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1721)
  AUTHORS   Giner,F., Medina-Ceballos,E., Lopez-Reig,R., Machado,I.,
            Lopez-Guerrero,J.A., Navarro,S., Rubio-Martinez,L.A., Espino,M.,
            Mayordomo-Aranda,E. and Llombart-Bosch,A.
  TITLE     The Combined Immunohistochemical Expression of GLI1 and BCOR in
            Synovial Sarcomas for the Identification of Three Risk Groups and
            Their Prognostic Outcomes: A Study of 52 Patients
  JOURNAL   Int J Mol Sci 25 (14), 7615 (2024)
   PUBMED   39062853
  REMARK    GeneRIF: The Combined Immunohistochemical Expression of GLI1 and
            BCOR in Synovial Sarcomas for the Identification of Three Risk
            Groups and Their Prognostic Outcomes: A Study of 52 Patients.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1721)
  AUTHORS   Mavridou,E., Lema Fernandez,A.G., Nardelli,C., Pierini,V.,
            Quintini,M., Arniani,S., Di Giacomo,D., Crescenzi,B., Matteucci,C.,
            Sambani,C. and Mecucci,C.
  TITLE     A novel t(X;21)(p11.4;q22.12) translocation adds to the role of
            BCOR and RUNX1 in myelodysplastic syndromes and acute myeloid
            leukemias
  JOURNAL   Genes Chromosomes Cancer 63 (4), e23235 (2024)
   PUBMED   38656651
  REMARK    GeneRIF: A novel t(X;21)(p11.4;q22.12) translocation adds to the
            role of BCOR and RUNX1 in myelodysplastic syndromes and acute
            myeloid leukemias.
REFERENCE   4  (residues 1 to 1721)
  AUTHORS   Pierron,G., Tirode,F., Lucchesi,C., Reynaud,S., Ballet,S.,
            Cohen-Gogo,S., Perrin,V., Coindre,J.M. and Delattre,O.
  TITLE     A new subtype of bone sarcoma defined by BCOR-CCNB3 gene fusion
  JOURNAL   Nat Genet 44 (4), 461-466 (2012)
   PUBMED   22387997
  REMARK    GeneRIF: A new fusion was observed between BCOR (encoding the BCL6
            co-repressor) and CCNB3 (encoding the testis-specific cyclin B3) on
            the X chromosome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1721)
  AUTHORS   Tomsig,J.L., Snyder,S.L. and Creutz,C.E.
  TITLE     Identification of targets for calcium signaling through the copine
            family of proteins. Characterization of a coiled-coil
            copine-binding motif
  JOURNAL   J Biol Chem 278 (12), 10048-10054 (2003)
   PUBMED   12522145
REFERENCE   6  (residues 1 to 1721)
  AUTHORS   Ng,D., Hadley,D.W., Tifft,C.J. and Biesecker,L.G.
  TITLE     Genetic heterogeneity of syndromic X-linked recessive
            microphthalmia-anophthalmia: is Lenz microphthalmia a single
            disorder?
  JOURNAL   Am J Med Genet 110 (4), 308-314 (2002)
   PUBMED   12116202
REFERENCE   7  (residues 1 to 1721)
  AUTHORS   Tang,T.T., Dowbenko,D., Jackson,A., Toney,L., Lewin,D.A., Dent,A.L.
            and Lasky,L.A.
  TITLE     The forkhead transcription factor AFX activates apoptosis by
            induction of the BCL-6 transcriptional repressor
  JOURNAL   J Biol Chem 277 (16), 14255-14265 (2002)
   PUBMED   11777915
  REMARK    GeneRIF: The forkhead transcription factor AFX activates apoptosis
            by induction of the BCL-6 transcriptional repressor.
REFERENCE   8  (residues 1 to 1721)
  AUTHORS   Huynh,K.D., Fischle,W., Verdin,E. and Bardwell,V.J.
  TITLE     BCoR, a novel corepressor involved in BCL-6 repression
  JOURNAL   Genes Dev 14 (14), 1810-1823 (2000)
   PUBMED   10898795
  REMARK    GeneRIF: Function:BCoR is a transcriptional corepressor for BCL-6.
            Nomenclature:BCoR (BCL-6 corepressor)
REFERENCE   9  (residues 1 to 1721)
  AUTHORS   Ng,D.
  TITLE     Lenz Microphthalmia Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301694
REFERENCE   10 (residues 1 to 1721)
  AUTHORS   Bardakjian,T., Weiss,A. and Schneider,A.
  TITLE     Microphthalmia/Anophthalmia/Coloboma Spectrum - RETIRED CHAPTER,
            FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301552
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL591802.28, AL698729.1,
            BC114220.1, AC092198.5 and AK056538.1.
            
            On May 22, 2002 this sequence version replaced NP_060215.3.
            
            Summary: The protein encoded by this gene was identified as an
            interacting corepressor of BCL6, a POZ/zinc finger transcription
            repressor that is required for germinal center formation and may
            influence apoptosis. This protein selectively interacts with the
            POZ domain of BCL6, but not with eight other POZ proteins. Specific
            class I and II histone deacetylases (HDACs) have been shown to
            interact with this protein, which suggests a possible link between
            the two classes of HDACs. Several transcript variants encoding
            different isoforms have been found for this gene. A pseudogene of
            this gene is found on chromosome Y.[provided by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (1) uses an alternate in-frame
            splice site compared to variant 5. The resulting isoform (a) has
            the same N- and C-termini but is shorter compared to isoform c.
            Variants 1 and 3 both encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF317391.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1721
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.4"
     Protein         1..1721
                     /product="BCL-6 corepressor isoform a"
                     /note="BCL-6 interacting corepressor; BCL6 interacting
                     corepressor; BCL-6 coreceptor"
                     /calculated_mol_wt=188072
     Region          <257..673
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          309..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          388..438
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            392
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          498..514
                     /region_name="Interaction with BCL6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          557..641
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          737..760
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          773..794
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          815..844
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGN4; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1168..1380
                     /region_name="BCOR"
                     /note="BCL-6 co-repressor, non-ankyrin-repeat region;
                     pfam15808"
                     /db_xref="CDD:434953"
     Region          1186..1294
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGN4; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1376
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1396..1417
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          <1427..1559
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1428..1461
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1429..1460
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1430,1434..1435,1438..1440,1442..1443,1447,1450,
                     1460,1462,1464,1468..1469,1472..1474,1476..1477,1481,1484,
                     1493,1495,1497,1501..1502,1505..1507,1509..1510,1514,1517)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1462..1493
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1462..1491
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1495..1524
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1495..1524
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1600..1714
                     /region_name="Necessary and sufficient for interaction
                     with PCGF1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1600..1713
                     /region_name="PUFD"
                     /note="BCORL-PCGF1-binding domain; pfam16553"
                     /db_xref="CDD:465171"
     Site            order(1602..1603,1605..1609,1611..1613,1615,1617,1626,
                     1628,1670..1672,1674..1675,1677..1678,1695,1706,1708,
                     1710..1712)
                     /site_type="other"
                     /note="RAWUL domain interface [polypeptide binding]"
                     /db_xref="CDD:271224"
     CDS             1..1721
                     /gene="BCOR"
                     /gene_synonym="ANOP2; MAA2; MCOPS2"
                     /coded_by="NM_017745.6:785..5950"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14250.1"
                     /db_xref="GeneID:54880"
                     /db_xref="HGNC:HGNC:20893"
                     /db_xref="MIM:300485"
ORIGIN      
        1 mlsatplygn vhswmnserv rmcgasedrk ilvndgdask arlelreenp lnhnvvdast
       61 ahridglaal smdrtglire glrvpgnivy sslcglgsek greaatstlg glgfssernp
      121 emqfkpntpe tveasavsgk ppngfsaiyk tppgiqksav ataealgldr pasdkqspln
      181 ingasylrlp wvnpymegat paiypfldsp nkyslnmyka llpqqsysla qplyspvctn
      241 gerflylppp hyvgphipss laspmrlstp saspaipplv hcadkslpwk mgvspgnpvd
      301 shayphiqns kqprvpsaka vtsglpgdta lllppsprps prvhlptqpa adtysefhkh
      361 yaristspsv alskpymtvs sefpaarlsn gkypkapegg egaqpvpgha rktavqdrkd
      421 gssppllekq tvtkdvtdkp ldlsskvvdv daskadhmkk maptvlvhsr agsglvlsgs
      481 eipketlspp gngcaiyrse iistapsswv vpgpspneen ngksmslknk aldwaipqqr
      541 ssscprmggt davitnvsgs vssagrpasa spapnanadg tktsrssvet tpsviqhvgq
      601 ppatpakhss stsskgakas npepsfkane nglppssifl spneafrspp ipyprsylpy
      661 papegiavsp lslhgkgpvy phpvllpngs lfpghlapkp glpyglptgr pefvtyqdal
      721 glgmvhpmli phtpieitke ekperrsrsh eraryedptl rnrfseilet sstklhpdvp
      781 tdknlkpnpn wnqgktvvks dklvyvdllr eepdaktdtn vskpsfaaes vgqsaeppkp
      841 svepalqqhr dfialreelg risdfhetyt fkqpvftvsk dsvlagtnke nlglpvstpf
      901 lepplgsdgp avtfgktqed pkpfcvgsap psvdvtptyt kdgadeaesn dgkvlkpkps
      961 klakriansa gyvgdrfkcv ttelyadssq lsreqralqm eglqedsilc lpaayceram
     1021 mrfselemke regghpatkd semckfspad werlkgnqdk kpksvtleea iaeqneserc
     1081 eysvgnkhrd pfeapedkdl pvekyfverq pvseppadqv asdmphsptl rvdrkrkvsg
     1141 dsshtettae evpedpllka krrrvskglh pkkqrhllhl rerweqqvsa adgkpgrqsr
     1201 kevtqatqpe aipqgtnite ekpgrkraea kgnrswsees lkpsdneqgl pvfsgsppmk
     1261 slsstsaggk kqaqpscapa srppakqqki kenqktdvlc adeeedcqaa sllqkytdns
     1321 ekpsgkrlck tkhlipqesr rglpltgeyy venadgkvtv rrfrkrpeps sdydlspakq
     1381 epkpfdrlqq llpasqstql pcssspqett qsrpmppear rlivnknage tllqraarlg
     1441 yeevvlycle nkicdvnhrd nagycalhea cargwlnivr hlleygadvn csaqdgtrpl
     1501 hdavendhle ivrlllsyga dptlatysgr timkmthsel mekfltdyln dlqgrnddda
     1561 sgtwdfygss vcepddesgy dvlanppgpe dqdddddays dvfefefset pllpcyniqv
     1621 svaqgprnwl llsdvlkklk mssrifrcnf pnveivtiae aefyrqvsas llfscskdle
     1681 afnpeskell dlveftneiq tllgssvewl hpsdlasdny w
//
LOCUS       NP_001340444             597 aa            linear   PRI 21-NOV-2025
DEFINITION  integrator complex subunit 10 isoform l [Homo sapiens].
ACCESSION   NP_001340444
VERSION     NP_001340444.1
DBSOURCE    REFSEQ: accession NM_001353515.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Lin,M.H., Jensen,M.K., Elrod,N.D., Chu,H.F., Haseley,M., Beam,A.C.,
            Huang,K.L., Chiang,W., Russell,W.K., Williams,K., Proschel,C.,
            Wagner,E.J. and Tong,L.
  TITLE     Cytoplasmic binding partners of the Integrator endonuclease INTS11
            and its paralog CPSF73 are required for their nuclear function
  JOURNAL   Mol Cell 84 (15), 2900-2917 (2024)
   PUBMED   39032490
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Razew,M., Fraudeau,A., Pfleiderer,M.M., Linares,R. and Galej,W.P.
  TITLE     Structural basis of the Integrator complex assembly and association
            with transcription factors
  JOURNAL   Mol Cell 84 (13), 2542-2552 (2024)
   PUBMED   38823386
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Fianu,I., Ochmann,M., Walshe,J.L., Dybkov,O., Cruz,J.N., Urlaub,H.
            and Cramer,P.
  TITLE     Structural basis of Integrator-dependent RNA polymerase II
            termination
  JOURNAL   Nature 629 (8010), 219-227 (2024)
   PUBMED   38570683
REFERENCE   4  (residues 1 to 597)
  AUTHORS   Offley,S.R., Pfleiderer,M.M., Zucco,A., Fraudeau,A., Welsh,S.A.,
            Razew,M., Galej,W.P. and Gardini,A.
  TITLE     A combinatorial approach to uncover an additional Integrator
            subunit
  JOURNAL   Cell Rep 42 (3), 112244 (2023)
   PUBMED   36920904
REFERENCE   5  (residues 1 to 597)
  AUTHORS   Wu,Y., Lin,Z., Luo,M., Yu,X., Chen,S. and Liu,L.
  TITLE     Effects of genetic polymorphisms in INTS10 and their interaction
            with environmental factors on progression from persistent HBV
            infection to hepatocellular carcinoma
  JOURNAL   Mol Carcinog 60 (9), 620-626 (2021)
   PUBMED   34133796
  REMARK    GeneRIF: Effects of genetic polymorphisms in INTS10 and their
            interaction with environmental factors on progression from
            persistent HBV infection to hepatocellular carcinoma.
REFERENCE   6  (residues 1 to 597)
  AUTHORS   Weissglas-Volkov,D., Aguilar-Salinas,C.A., Nikkola,E., Deere,K.A.,
            Cruz-Bautista,I., Arellano-Campos,O., Munoz-Hernandez,L.L.,
            Gomez-Munguia,L., Ordonez-Sanchez,M.L., Reddy,P.M., Lusis,A.J.,
            Matikainen,N., Taskinen,M.R., Riba,L., Cantor,R.M.,
            Sinsheimer,J.S., Tusie-Luna,T. and Pajukanta,P.
  TITLE     Genomic study in Mexicans identifies a new locus for triglycerides
            and refines European lipid loci
  JOURNAL   J Med Genet 50 (5), 298-308 (2013)
   PUBMED   23505323
REFERENCE   7  (residues 1 to 597)
  AUTHORS   Ellinghaus,E., Stanulla,M., Richter,G., Ellinghaus,D., te
            Kronnie,G., Cario,G., Cazzaniga,G., Horstmann,M., Panzer
            Grumayer,R., Cave,H., Trka,J., Cinek,O., Teigler-Schlegel,A.,
            ElSharawy,A., Hasler,R., Nebel,A., Meissner,B., Bartram,T.,
            Lescai,F., Franceschi,C., Giordan,M., Nurnberg,P., Heinzow,B.,
            Zimmermann,M., Schreiber,S., Schrappe,M. and Franke,A.
  TITLE     Identification of germline susceptibility loci in
            ETV6-RUNX1-rearranged childhood acute lymphoblastic leukemia
  JOURNAL   Leukemia 26 (5), 902-909 (2012)
   PUBMED   22076464
REFERENCE   8  (residues 1 to 597)
  AUTHORS   Kooner,J.S., Chambers,J.C., Aguilar-Salinas,C.A., Hinds,D.A.,
            Hyde,C.L., Warnes,G.R., Gomez Perez,F.J., Frazer,K.A., Elliott,P.,
            Scott,J., Milos,P.M., Cox,D.R. and Thompson,J.F.
  TITLE     Genome-wide scan identifies variation in MLXIPL associated with
            plasma triglycerides
  JOURNAL   Nat Genet 40 (2), 149-151 (2008)
   PUBMED   18193046
REFERENCE   9  (residues 1 to 597)
  AUTHORS   Baillat,D., Hakimi,M.A., Naar,A.M., Shilatifard,A., Cooch,N. and
            Shiekhattar,R.
  TITLE     Integrator, a multiprotein mediator of small nuclear RNA
            processing, associates with the C-terminal repeat of RNA polymerase
            II
  JOURNAL   Cell 123 (2), 265-276 (2005)
   PUBMED   16239144
REFERENCE   10 (residues 1 to 597)
  AUTHORS   Yuryev,A. and Wennogle,L.P.
  TITLE     Novel raf kinase protein-protein interactions found by an
            exhaustive yeast two-hybrid analysis
  JOURNAL   Genomics 81 (2), 112-125 (2003)
   PUBMED   12620389
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC107964.4.
            
            Summary: INTS10 is a subunit of the Integrator complex, which
            associates with the C-terminal domain of RNA polymerase II large
            subunit (POLR2A; MIM 180660) and mediates 3-prime end processing of
            small nuclear RNAs U1 (RNU1; MIM 180680) and U2 (RNU2; MIM 180690)
            (Baillat et al., 2005 [PubMed 16239144]).[supplied by OMIM, Mar
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853566.26289.1,
                                           SRR11853559.30706.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..597
                     /product="integrator complex subunit 10 isoform l"
                     /calculated_mol_wt=68957
     CDS             1..597
                     /gene="INTS10"
                     /gene_synonym="C8orf35; INT10"
                     /coded_by="NM_001353515.2:593..2386"
                     /note="isoform l is encoded by transcript variant 12"
                     /db_xref="GeneID:55174"
                     /db_xref="HGNC:HGNC:25548"
                     /db_xref="MIM:611353"
ORIGIN      
        1 mllkvteqcf ntlersemll lllrrfpetv vqhgvglgea lleaetieeq espvncfrkl
       61 fvcdvlplii nnhdvrlpan llykylnkaa efyinyvtrs tqienqhqga qdtsdlmsps
      121 krssqkyiie gltekssqiv dpwerlfkil nvvgmrcewq mdkgrrsygd ilhrmkdlcr
      181 ymnnfdseah akyknqvvys tmlvffknaf qyvnsiqpsl fqgpnapsqv plvlledvsn
      241 vygdveidrn khihkkrkla egrektmssd dedcsakgrn rhivvnkael anstevlesf
      301 klareswell yslefldkef triclawktd twlwlriflt dmiiyqgqyk kaiaslhhla
      361 alqgsisqpq itgqgtlehq raliqlatch falgeyrmtc ekvldlmcym vlpiqdggks
      421 qeepskvkpk frkgsdlkll pctskaimpy clhlmlacfk lraftdnrdd malghvivll
      481 qqewprgenl flkavnkicq qgnfqyenff nyvtnidmle efaylrtqeg gkihlellpn
      541 qgmlikhhtv trgitkgvke dfrlamerqv srcgenlmvv lhrfcineki lllqtlt
//
LOCUS       NP_001188306             511 aa            linear   PRI 21-NOV-2025
DEFINITION  alpha-aminoadipic semialdehyde dehydrogenase isoform 2 [Homo
            sapiens].
ACCESSION   NP_001188306 XP_003120518 XP_003120519 XP_003120520 XP_003120521
            XP_003120522 XP_003120523 XP_003120524 XP_003120525 XP_003120526
VERSION     NP_001188306.1
DBSOURCE    REFSEQ: accession NM_001201377.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Yang,J.S., Morris,A.J., Kamizaki,K., Chen,J., Stark,J.,
            Oldham,W.M., Nakamura,T., Mishima,E., Loscalzo,J., Minami,Y.,
            Conrad,M., Henry,W.S. and Hsu,V.W.
  TITLE     ALDH7A1 protects against ferroptosis by generating membrane NADH
            and regulating FSP1
  JOURNAL   Cell 188 (10), 2569-2585 (2025)
   PUBMED   40233740
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Korasick,D.A., Buckley,D.P., Palpacelli,A., Cursio,I., Cesaroni,E.,
            Cheng,J. and Tanner,J.J.
  TITLE     Biochemical, structural, and computational analyses of two new
            clinically identified missense mutations of ALDH7A1
  JOURNAL   Chem Biol Interact 394, 110993 (2024)
   PUBMED   38604394
  REMARK    GeneRIF: Biochemical, structural, and computational analyses of two
            new clinically identified missense mutations of ALDH7A1.
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Crowther,L.M., Poms,M., Zandl-Lang,M., Abela,L., Hartmann,H.,
            Seiler,M., Mathis,D. and Plecko,B.
  TITLE     Metabolomics analysis of antiquitin deficiency in cultured human
            cells and plasma: Relevance to pyridoxine-dependent epilepsy
  JOURNAL   J Inherit Metab Dis 46 (1), 129-142 (2023)
   PUBMED   36225138
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Lu,H.J., Chuang,C.Y., Chen,M.K., Su,C.W., Yang,W.E., Yeh,C.M.,
            Lai,K.M., Tang,C.H., Lin,C.W. and Yang,S.F.
  TITLE     The impact of ALDH7A1 variants in oral cancer development and
            prognosis
  JOURNAL   Aging (Albany NY) 14 (10), 4556-4571 (2022)
   PUBMED   35613852
  REMARK    GeneRIF: The impact of ALDH7A1 variants in oral cancer development
            and prognosis.
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Brocker,C., Lassen,N., Estey,T., Pappa,A., Cantore,M., Orlova,V.V.,
            Chavakis,T., Kavanagh,K.L., Oppermann,U. and Vasiliou,V.
  TITLE     Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in
            cellular defense against hyperosmotic stress
  JOURNAL   J Biol Chem 285 (24), 18452-18463 (2010)
   PUBMED   20207735
  REMARK    GeneRIF: ALDH7A1 is a novel aldehyde dehydrogenase expressed in
            multiple subcellular compartments that protects against
            hyperosmotic stress by generating osmolytes and metabolizing toxic
            aldehydes
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Wong,J.W., Chan,C.L., Tang,W.K., Cheng,C.H. and Fong,W.P.
  TITLE     Is antiquitin a mitochondrial Enzyme?
  JOURNAL   J Cell Biochem 109 (1), 74-81 (2010)
   PUBMED   19885858
  REMARK    GeneRIF: antiquitin was present not only in the cytosol but also in
            the mitochondria.
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Cormier-Daire,V., Dagoneau,N., Nabbout,R., Burglen,L., Penet,C.,
            Soufflet,C., Desguerre,I., Munnich,A. and Dulac,O.
  TITLE     A gene for pyridoxine-dependent epilepsy maps to chromosome 5q31
  JOURNAL   Am J Hum Genet 67 (4), 991-993 (2000)
   PUBMED   10978228
REFERENCE   8  (residues 1 to 511)
  AUTHORS   Skvorak,A.B., Robertson,N.G., Yin,Y., Weremowicz,S., Her,H.,
            Bieber,F.R., Beisel,K.W., Lynch,E.D., Beier,D.R. and Morton,C.C.
  TITLE     An ancient conserved gene expressed in the human inner ear:
            identification, expression analysis, and chromosomal mapping of
            human and mouse antiquitin (ATQ1)
  JOURNAL   Genomics 46 (2), 191-199 (1997)
   PUBMED   9417906
REFERENCE   9  (residues 1 to 511)
  AUTHORS   Lee,P., Kuhl,W., Gelbart,T., Kamimura,T., West,C. and Beutler,E.
  TITLE     Homology between a human protein and a protein of the green garden
            pea
  JOURNAL   Genomics 21 (2), 371-378 (1994)
   PUBMED   8088832
REFERENCE   10 (residues 1 to 511)
  AUTHORS   Gospe,S.M. Jr.
  TITLE     Pyridoxine-Dependent Epilepsy - ALDH7A1
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301659
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099513.3 and AC093535.2.
            
            On or before Jan 20, 2011 this sequence version replaced
            XP_003120518.1, XP_003120523.1, XP_003120519.1, XP_003120522.1,
            XP_003120525.1, XP_003120521.1, XP_003120524.1, XP_003120520.1,
            XP_003120526.1.
            
            Summary: The protein encoded by this gene is a member of subfamily
            7 in the aldehyde dehydrogenase gene family. These enzymes are
            thought to play a major role in the detoxification of aldehydes
            generated by alcohol metabolism and lipid peroxidation. This
            particular member has homology to a previously described protein
            from the green garden pea, the 26g pea turgor protein. It is also
            involved in lysine catabolism that is known to occur in the
            mitochondrial matrix. Recent reports show that this protein is
            found both in the cytosol and the mitochondria, and the two forms
            likely arise from the use of alternative translation initiation
            sites. An additional variant encoding a different isoform has also
            been found for this gene. Mutations in this gene are associated
            with pyridoxine-dependent epilepsy. Several related pseudogenes
            have also been identified. [provided by RefSeq, Jan 2011].
            
            Transcript Variant: This variant (1) encodes two isoforms resulting
            from the use of alternative in-frame translation initiation codons.
            The longer isoform (1) is derived from an upstream AUG (at nt
            193-195), while the shorter isoform (2) is derived from a
            downstream AUG (at nt 277-279). This RefSeq represents the shorter
            isoform, which is found in the cytosol (PMIDs: 20207735 and
            19885858).
            
            Sequence Note: This Refseq, containing three potential in-frame
            translation initiation codons (all with weak Kozak signals), is
            annotated with a CDS starting from a downstream start codon (at nt
            277-279), which results in a shorter, soluble isoform that is
            localized in the cytosol (PMIDs: 20207735 and 19885858). A longer
            isoform, resulting from the use of an upstream start codon (at nt
            193-195) and localized in the mitochondria, is represented in a
            separate RefSeq (NM_001182.4). The use of another upstream start
            codon (at nt 112-114) that is present in only a subset of higher
            mammals, would increase the protein length by another 27 aa. This
            RefSeq record was created from transcript and genomic sequence data
            to make the sequence consistent with the reference genome assembly.
            The extent of this transcript is supported by transcript
            alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3045768.1,
                                           SRR18074967.2778040.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG   :: downstream AUG is associated
                                                  with N-terminal localization
                                                  signal (PMID:19885858)
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q23.2"
     Protein         1..511
                     /product="alpha-aminoadipic semialdehyde dehydrogenase
                     isoform 2"
                     /EC_number="1.2.1.3"
                     /EC_number="1.2.1.8"
                     /EC_number="1.2.1.31"
                     /note="26g turgor protein homolog; alpha-aminoadipic
                     semialdehyde dehydrogenase; alpha-AASA dehydrogenase; P6c
                     dehydrogenase; antiquitin-1; betaine aldehyde
                     dehydrogenase; delta1-piperideine-6-carboxylate
                     dehydrogenase; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=55236
     Region          25..499
                     /region_name="ALDH_F7_AASADH"
                     /note="NAD+-dependent alpha-aminoadipic semialdehyde
                     dehydrogenase, ALDH family members 7A1 and 7B; cd07130"
                     /db_xref="CDD:143448"
     Site            order(72,78,81,87,94,133..134,136,138,140,142..145,
                     152..153,155,252,255..256,259,264..265,292,328,340,414,
                     437,443..444,448,451,453..456,462..463,467,471,478,
                     482..483,486,490..495,497..498)
                     /site_type="other"
                     /note="tetrameric interface [polypeptide binding]"
                     /db_xref="CDD:143448"
     Site            order(164..167,190,192..193,230..231,244..247,250,253,
                     268..270,302,399,468)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:143448"
     Site            order(167,268,299,302)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143448"
     CDS             1..511
                     /gene="ALDH7A1"
                     /gene_synonym="ATQ1; EPD; EPEO4; PDE"
                     /coded_by="NM_001201377.2:106..1641"
                     /note="isoform 2 is encoded by transcript variant 1"
                     /db_xref="GeneID:501"
                     /db_xref="HGNC:HGNC:877"
                     /db_xref="MIM:107323"
ORIGIN      
        1 mstllinqpq yawlkelglr eenegvyngs wggrgevitt ycpannepia rvrqasvady
       61 eetvkkarea wkiwadipap krgeivrqig dalrekiqvl gslvslemgk ilvegvgevq
      121 eyvdicdyav glsrmiggpi lpsersghal ieqwnpvglv giitafnfpv avygwnnaia
      181 micgnvclwk gapttslisv avtkiiakvl ednklpgaic sltcggadig tamakdervn
      241 llsftgstqv gkqvglmvqe rfgrsllelg gnnaiiafed adlslvvpsa lfaavgtagq
      301 rcttarrlfi hesihdevvn rlkkayaqir vgnpwdpnvl ygplhtkqav smflgaveea
      361 kkeggtvvyg gkvmdrpgny veptivtglg hdasiahtet fapilyvfkf kneeevfawn
      421 nevkqglsss iftkdlgrif rwlgpkgsdc givnvnipts gaeiggafgg ekhtgggres
      481 gsdawkqymr rstctinysk dlplaqgikf q
//
LOCUS       NP_001230271            1030 aa            linear   PRI 21-NOV-2025
DEFINITION  coiled-coil domain-containing protein 40 isoform 2 [Homo sapiens].
ACCESSION   NP_001230271
VERSION     NP_001230271.1
DBSOURCE    REFSEQ: accession NM_001243342.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Wilken,A., Hoben,I.M., Wolter,A., Loges,N.T., Olbrich,H., Aprea,I.,
            Dworniczak,B., Raidt,J. and Omran,H.
  TITLE     Primary Ciliary Dyskinesia Associated Disease-Causing Variants in
            CCDC39 and CCDC40 Cause Axonemal Absence of Inner Dynein Arm Heavy
            Chains DNAH1, DNAH6, and DNAH7
  JOURNAL   Cells 13 (14), 1200 (2024)
   PUBMED   39056782
  REMARK    GeneRIF: Primary Ciliary Dyskinesia Associated Disease-Causing
            Variants in CCDC39 and CCDC40 Cause Axonemal Absence of Inner
            Dynein Arm Heavy Chains DNAH1, DNAH6, and DNAH7.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Liu,L., Zhou,K., Song,Y. and Liu,X.
  TITLE     CCDC40 mutation as a cause of infertility in a Chinese family with
            primary ciliary dyskinesia
  JOURNAL   Medicine (Baltimore) 100 (51), e28275 (2021)
   PUBMED   34941110
  REMARK    GeneRIF: CCDC40 mutation as a cause of infertility in a Chinese
            family with primary ciliary dyskinesia.
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1030)
  AUTHORS   Fassad,M.R., Shoman,W.I., Morsy,H., Patel,M.P., Radwan,N.,
            Jenkins,L., Cullup,T., Fouda,E., Mitchison,H.M. and Fasseeh,N.
  TITLE     Clinical and genetic spectrum in 33 Egyptian families with
            suspected primary ciliary dyskinesia
  JOURNAL   Clin Genet 97 (3), 509-515 (2020)
   PUBMED   31650533
  REMARK    GeneRIF: Clinical and genetic spectrum in 33 Egyptian families with
            suspected primary ciliary dyskinesia.
REFERENCE   5  (residues 1 to 1030)
  AUTHORS   Antony,D., Becker-Heck,A., Zariwala,M.A., Schmidts,M.,
            Onoufriadis,A., Forouhan,M., Wilson,R., Taylor-Cox,T., Dewar,A.,
            Jackson,C., Goggin,P., Loges,N.T., Olbrich,H., Jaspers,M.,
            Jorissen,M., Leigh,M.W., Wolf,W.E., Daniels,M.L., Noone,P.G.,
            Ferkol,T.W., Sagel,S.D., Rosenfeld,M., Rutman,A., Dixit,A.,
            O'Callaghan,C., Lucas,J.S., Hogg,C., Scambler,P.J., Emes,R.D.,
            Chung,E.M., Shoemark,A., Knowles,M.R., Omran,H. and Mitchison,H.M.
  CONSRTM   Uk10k
  TITLE     Mutations in CCDC39 and CCDC40 are the major cause of primary
            ciliary dyskinesia with axonemal disorganization and absent inner
            dynein arms
  JOURNAL   Hum Mutat 34 (3), 462-472 (2013)
   PUBMED   23255504
  REMARK    GeneRIF: This study shows that CCDC39 and CCDC40 mutations are the
            major cause of Primary ciliary dyskinesia in patients with the
            previously termed 'radial spoke defect'.
REFERENCE   6  (residues 1 to 1030)
  AUTHORS   Blanchon,S., Legendre,M., Copin,B., Duquesnoy,P., Montantin,G.,
            Kott,E., Dastot,F., Jeanson,L., Cachanado,M., Rousseau,A.,
            Papon,J.F., Beydon,N., Brouard,J., Crestani,B., Deschildre,A.,
            Desir,J., Dollfus,H., Leheup,B., Tamalet,A., Thumerelle,C.,
            Vojtek,A.M., Escalier,D., Coste,A., de Blic,J., Clement,A.,
            Escudier,E. and Amselem,S.
  TITLE     Delineation of CCDC39/CCDC40 mutation spectrum and associated
            phenotypes in primary ciliary dyskinesia
  JOURNAL   J Med Genet 49 (6), 410-416 (2012)
   PUBMED   22693285
  REMARK    GeneRIF: Aiming to delineate the CCDC39/CCDC40 mutation spectrum
            and associated phenotypes, a large cohort of patients with IDA
            defects were screened. Biallelic CCDC39 or CCDC40 mutations were
            identified in 30/34 unrelated families with IDA defects.
REFERENCE   7  (residues 1 to 1030)
  AUTHORS   Nakhleh,N., Francis,R., Giese,R.A., Tian,X., Li,Y., Zariwala,M.A.,
            Yagi,H., Khalifa,O., Kureshi,S., Chatterjee,B., Sabol,S.L.,
            Swisher,M., Connelly,P.S., Daniels,M.P., Srinivasan,A., Kuehl,K.,
            Kravitz,N., Burns,K., Sami,I., Omran,H., Barmada,M., Olivier,K.,
            Chawla,K.K., Leigh,M., Jonas,R., Knowles,M., Leatherbury,L. and
            Lo,C.W.
  TITLE     High prevalence of respiratory ciliary dysfunction in congenital
            heart disease patients with heterotaxy
  JOURNAL   Circulation 125 (18), 2232-2242 (2012)
   PUBMED   22499950
REFERENCE   8  (residues 1 to 1030)
  AUTHORS   Becker-Heck,A., Zohn,I.E., Okabe,N., Pollock,A., Lenhart,K.B.,
            Sullivan-Brown,J., McSheene,J., Loges,N.T., Olbrich,H.,
            Haeffner,K., Fliegauf,M., Horvath,J., Reinhardt,R., Nielsen,K.G.,
            Marthin,J.K., Baktai,G., Anderson,K.V., Geisler,R., Niswander,L.,
            Omran,H. and Burdine,R.D.
  TITLE     The coiled-coil domain containing protein CCDC40 is essential for
            motile cilia function and left-right axis formation
  JOURNAL   Nat Genet 43 (1), 79-84 (2011)
   PUBMED   21131974
  REMARK    GeneRIF: CCDC40 mutations in humans result in a variant of primary
            ciliary dyskinesia characterized by misplacement of the central
            pair of microtubules and defective assembly of inner dynein arms
            and dynein regulatory complexes.
REFERENCE   9  (residues 1 to 1030)
  AUTHORS   Wang,J., Lin,J., Chang,Y., Li,P. and Yang,Y.
  TITLE     MCM3AP, a novel HBV integration site in hepatocellular carcinoma
            and its implication in hepatocarcinogenesis
  JOURNAL   J Huazhong Univ Sci Technolog Med Sci 30 (4), 425-429 (2010)
   PUBMED   20714864
REFERENCE   10 (residues 1 to 1030)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB230102.1, BC035251.1,
            DA842356.1, AB046860.1, AC087741.18 and BQ009577.1.
            
            Summary: This gene encodes a protein that is necessary for motile
            cilia function. It functions in correct left-right axis formation
            by regulating the assembly of the inner dynein arm and the dynein
            regulatory complexes, which control ciliary beat. Mutations in this
            gene cause ciliary dyskinesia type 15, a disorder due to defects in
            cilia motility. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (2) differs in the 3' coding
            region and 3' UTR, compared to variant 1. The encoded isoform (2)
            has a distinct and shorter C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2145240 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..1030
                     /product="coiled-coil domain-containing protein 40 isoform
                     2"
                     /note="coiled-coil domain-containing protein 40;
                     coiled-coil domain containing 40"
                     /calculated_mol_wt=116670
     Region          1..197
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G0X9.2)"
     Region          251..274
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G0X9.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BI79; propagated from
                     UniProtKB/Swiss-Prot (Q4G0X9.2)"
     Region          299..>960
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          780..878
                     /region_name="BRE1"
                     /note="BRE1 E3 ubiquitin ligase; pfam08647"
                     /db_xref="CDD:462547"
     CDS             1..1030
                     /gene="CCDC40"
                     /gene_synonym="CFAP172; CILD15; FAP172"
                     /coded_by="NM_001243342.2:22..3114"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58604.1"
                     /db_xref="GeneID:55036"
                     /db_xref="HGNC:HGNC:26090"
                     /db_xref="MIM:613799"
ORIGIN      
        1 maepggaagr shpedgsase gekegnnesh mvsppekddg qkgeeavgst ehpeevttqa
       61 eaaieegeve tegeaavege eeavsygdae seeeyyytet sspegqisaa dttypyfspp
      121 qelpgeeayd svsgeaglqg fqqeatgppe srerrvtspe pshgvlgpse qmgqvtsgpa
      181 vgrltgstee pqgqvlpmgv qhrfrlshgs diessdleef vsqepvippg vpdahpregd
      241 lpvfqdqiqq psteegamae rvesegsdee aedegsqlvv ldpdhplmvr fqaalknyln
      301 rqieklkldl qelvvatkqs raqrqelgvn lyevqqhlvh lqkllekshd rhamasserr
      361 qkeeelqaar alytktcaaa neerkklaal qtemenlalh lfymqnidqd mrddirvmtq
      421 vvkkaeteri raeiekkkqd lyvdqlttra qqleedialf eaqylaqaed trilrkavse
      481 acteidaisv ekrrimqqwa sslvgmkhrd eahravleal rgcqhqakst dgeieaykks
      541 imkeeeknek lasilnrtet eatllqkltt qcltkqvalq sqfntyrltl qdtedalsqd
      601 qleqmiltee lqairqaiqg elelrrktda aireklqehm tsnkttkyfn qlilrlqkek
      661 tnmmthlski ngdiaqttld ithtssrlda hqktlveldq dvkkvnelit nsqseisrrt
      721 ilierkqgli nflnkqlerm vselggeevg pleleikrls klidehdgka vqaqvtwlrl
      781 qqemvkvtqe qeeqlaslda skkelhimeq kklrveskie qekkeqkeie hhmkdldndl
      841 kklnmlmnkn rcsseeleqn nrvtenefvr slkasereti kmqdklnqls eekatllnql
      901 veaehqimlw ekkiqlakem rssvdseigq teiramkgei hrmkkycrtt qdahrhvheq
      961 hgthagtctk ntgraqarar ttrdarghvh eqhgtragtc tnntgraqar artrdarrhv
     1021 hehrthtara
//
LOCUS       NP_001305895             508 aa            linear   PRI 21-NOV-2025
DEFINITION  translation initiation factor eIF2B subunit delta isoform 5 [Homo
            sapiens].
ACCESSION   NP_001305895 XP_005264689
VERSION     NP_001305895.1
DBSOURCE    REFSEQ: accession NM_001318966.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Shivaram,S., Nagappa,M., Seshagiri,D.V., Saini,J., Govindaraj,P.,
            Sinha,S., Bindu,P.S. and Taly,A.B.
  TITLE     Leukodystrophy Due to eIF2B Mutations in Adults
  JOURNAL   Can J Neurol Sci 49 (5), 708-712 (2022)
   PUBMED   34663487
  REMARK    GeneRIF: Leukodystrophy Due to eIF2B Mutations in Adults.
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Yang,W. and Hinnebusch,A.G.
  TITLE     Identification of a regulatory subcomplex in the guanine nucleotide
            exchange factor eIF2B that mediates inhibition by phosphorylated
            eIF2
  JOURNAL   Mol Cell Biol 16 (11), 6603-6616 (1996)
   PUBMED   8887689
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Price,N.T., Mellor,H., Craddock,B.L., Flowers,K.M., Kimball,S.R.,
            Wilmer,T., Jefferson,L.S. and Proud,C.G.
  TITLE     eIF2B, the guanine nucleotide-exchange factor for eukaryotic
            initiation factor 2. Sequence conservation between the alpha, beta
            and delta subunits of eIF2B from mammals and yeast
  JOURNAL   Biochem J 318 (Pt 2) (Pt 2), 637-643 (1996)
   PUBMED   8929216
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Welsh,G.I., Miyamoto,S., Price,N.T., Safer,B. and Proud,C.G.
  TITLE     T-cell activation leads to rapid stimulation of translation
            initiation factor eIF2B and inactivation of glycogen synthase
            kinase-3
  JOURNAL   J Biol Chem 271 (19), 11410-11413 (1996)
   PUBMED   8626696
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Henderson,R.A., Krissansen,G.W., Yong,R.Y., Leung,E., Watson,J.D.
            and Dholakia,J.N.
  TITLE     The delta-subunit of murine guanine nucleotide exchange factor
            eIF-2B. Characterization of cDNAs predicts isoforms differing at
            the amino-terminal end
  JOURNAL   J Biol Chem 269 (48), 30517-30523 (1994)
   PUBMED   7982969
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   10 (residues 1 to 508)
  AUTHORS   van der Knaap,M.S., Fogli,A., Boespflug-Tanguy,O., Abbink,T.E.M.
            and Schiffmann,R.
  TITLE     Childhood Ataxia with Central Nervous System Hypomyelination /
            Vanishing White Matter
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301435
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC074117.7, AK300734.1,
            AF218009.1 and AF112207.1.
            
            On Jan 20, 2016 this sequence version replaced XP_005264689.1.
            
            Summary: Eukaryotic initiation factor 2B (EIF2B), which is
            necessary for protein synthesis, is a GTP exchange factor composed
            of five different subunits. The protein encoded by this gene is the
            fourth, or delta, subunit. Defects in this gene are a cause of
            leukoencephalopathy with vanishing white matter (VWM) and
            ovarioleukodystrophy. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (5) differs in the 5' UTR and
            coding sequence compared to variant 4. The resulting isoform (5) is
            shorter at the N-terminus compared to isoform 4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF218009.1, SRR14038197.2353930.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..508
                     /product="translation initiation factor eIF2B subunit
                     delta isoform 5"
                     /note="translation initiation factor eIF-2b delta subunit;
                     translation initiation factor eIF-2B subunit delta; eIF-2B
                     GDP-GTP exchange factor subunit delta; eukaryotic
                     translation initiation factor 2B subunit 4 delta;
                     eukaryotic translation initiation factor 2B, subunit 4
                     delta, 67kDa; eIF2B GDP-GTP exchange factor subunit delta;
                     translation initiation factor eIF2B subunit delta"
                     /calculated_mol_wt=56025
     Region          204..494
                     /region_name="IF-2B"
                     /note="Initiation factor 2 subunit family; pfam01008"
                     /db_xref="CDD:395798"
     CDS             1..508
                     /gene="EIF2B4"
                     /gene_synonym="EIF-2B; EIF2B; EIF2Bdelta; VWM4"
                     /coded_by="NM_001318966.2:248..1774"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:8890"
                     /db_xref="HGNC:HGNC:3260"
                     /db_xref="MIM:606687"
ORIGIN      
        1 mkaelppgpg avgremtkee klqlrkekkq qkkkrkeekg aepetgsavs aaqcqvgptr
       61 elpesgiqlg tprekvpagr skaelraerr akqeaeralk qarkgeqggp ppkaspstag
      121 etpsgvkrlp eypqvddlll rrlvkkperq qvptrkdygs kvslfshlpq ysrqnsltqf
      181 msipssvihp amvrlglqys qglvsgsnar ciallralqq viqdyttppn eelsrdlvnk
      241 lkpymsfltq crplsasmhn aikflnkeit svgsskreee akselraaid ryvqekivla
      301 aqaisrfayq kisngdvilv ygcsslvsri lqeawtegrr frvvvvdsrp wlegrhtlrs
      361 lvhagvpasy llipaasyvl pevskvllga hallangsvm srvgtaqlal varahnvpvl
      421 vccetykfce rvqtdafvsn elddpddlqc krgehvalan wqnhaslrll nlvydvtppe
      481 lvdlvitelg mipcssvpvv lrvkssdq
//
LOCUS       NP_001374640            1040 aa            linear   PRI 21-NOV-2025
DEFINITION  activated CDC42 kinase 1 isoform 8 [Homo sapiens].
ACCESSION   NP_001374640
VERSION     NP_001374640.1
DBSOURCE    REFSEQ: accession NM_001387711.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Zheng,D., Wei,Z., Zhang,C., Liu,W., Gong,C., Wu,F. and Guo,W.
  TITLE     ZNF692 promotes osteosarcoma cell proliferation, migration, and
            invasion through TNK2-mediated activation of the MEK/ERK pathway
  JOURNAL   Biol Direct 19 (1), 28 (2024)
   PUBMED   38650011
  REMARK    GeneRIF: ZNF692 promotes osteosarcoma cell proliferation,
            migration, and invasion through TNK2-mediated activation of the
            MEK/ERK pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Hodder,S., Fox,M., Binti Ahmad Mokhtar,A.M., Mott,H.R. and Owen,D.
  TITLE     ACKnowledging the role of the Activated-Cdc42 associated kinase
            (ACK) in regulating protein stability in cancer
  JOURNAL   Small GTPases 14 (1), 14-25 (2023)
   PUBMED   37194323
  REMARK    GeneRIF: ACKnowledging the role of the Activated-Cdc42 associated
            kinase (ACK) in regulating protein stability in cancer.
            Review article
REFERENCE   4  (residues 1 to 1040)
  AUTHORS   Zhou,A., Zhang,W. and Wang,B.
  TITLE     Host factor TNK2 is required for influenza virus infection
  JOURNAL   Genes Genomics 45 (6), 771-781 (2023)
   PUBMED   37133719
  REMARK    GeneRIF: Host factor TNK2 is required for influenza virus
            infection.
REFERENCE   5  (residues 1 to 1040)
  AUTHORS   Kan,Y., Paung,Y., Seeliger,M.A. and Miller,W.T.
  TITLE     Domain Architecture of the Nonreceptor Tyrosine Kinase Ack1
  JOURNAL   Cells 12 (6), 900 (2023)
   PUBMED   36980241
  REMARK    GeneRIF: Domain Architecture of the Nonreceptor Tyrosine Kinase
            Ack1.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1040)
  AUTHORS   Kato,J., Kaziro,Y. and Satoh,T.
  TITLE     Activation of the guanine nucleotide exchange factor Dbl following
            ACK1-dependent tyrosine phosphorylation
  JOURNAL   Biochem Biophys Res Commun 268 (1), 141-147 (2000)
   PUBMED   10652228
REFERENCE   7  (residues 1 to 1040)
  AUTHORS   Eisenmann,K.M., McCarthy,J.B., Simpson,M.A., Keely,P.J., Guan,J.L.,
            Tachibana,K., Lim,L., Manser,E., Furcht,L.T. and Iida,J.
  TITLE     Melanoma chondroitin sulphate proteoglycan regulates cell spreading
            through Cdc42, Ack-1 and p130cas
  JOURNAL   Nat Cell Biol 1 (8), 507-513 (1999)
   PUBMED   10587647
REFERENCE   8  (residues 1 to 1040)
  AUTHORS   Mott,H.R., Owen,D., Nietlispach,D., Lowe,P.N., Manser,E., Lim,L.
            and Laue,E.D.
  TITLE     Structure of the small G protein Cdc42 bound to the GTPase-binding
            domain of ACK
  JOURNAL   Nature 399 (6734), 384-388 (1999)
   PUBMED   10360579
REFERENCE   9  (residues 1 to 1040)
  AUTHORS   Satoh,T., Kato,J., Nishida,K. and Kaziro,Y.
  TITLE     Tyrosine phosphorylation of ACK in response to temperature
            shift-down, hyperosmotic shock, and epidermal growth factor
            stimulation
  JOURNAL   FEBS Lett 386 (2-3), 230-234 (1996)
   PUBMED   8647288
REFERENCE   10 (residues 1 to 1040)
  AUTHORS   Manser,E., Leung,T., Salihuddin,H., Tan,L. and Lim,L.
  TITLE     A non-receptor tyrosine kinase that inhibits the GTPase activity of
            p21cdc42
  JOURNAL   Nature 363 (6427), 364-367 (1993)
   PUBMED   8497321
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124944.8.
            
            Summary: This gene encodes a tyrosine kinase that binds Cdc42Hs in
            its GTP-bound form and inhibits both the intrinsic and
            GTPase-activating protein (GAP)-stimulated GTPase activity of
            Cdc42Hs. This binding is mediated by a unique sequence of 47 amino
            acids C-terminal to an SH3 domain. The protein may be involved in a
            regulatory mechanism that sustains the GTP-bound active form of
            Cdc42Hs and which is directly linked to a tyrosine phosphorylation
            signal transduction pathway. Several alternatively spliced
            transcript variants have been identified from this gene, but the
            full-length nature of only two transcript variants has been
            determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3356604.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..1040
                     /product="activated CDC42 kinase 1 isoform 8"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="activated p21cdc42Hs kinase; activated
                     Cdc42-associated kinase 1; tyrosine kinase non-receptor
                     protein 2"
                     /calculated_mol_wt=114679
     Region          1..110
                     /region_name="SAM-like domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          6..67
                     /region_name="SAM_TNK-like"
                     /note="SAM domain of TNK(ACK)-like non-receptor
                     tyrosine-protein kinases; cd09539"
                     /db_xref="CDD:188938"
     Region          90..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          130..387
                     /region_name="PTKc_Ack_like"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Activated Cdc42-associated kinase; cd05040"
                     /db_xref="CDD:270636"
     Site            order(132..134,140,156,158,205..208,212,252,256..257,259,
                     270,289..293,302,336)
                     /site_type="active"
                     /db_xref="CDD:270636"
     Site            order(132..134,140,156,158,205..208,212,252,256..257,259,
                     270)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270636"
     Site            order(252,256,289..293,302,336)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270636"
     Site            order(269..279,281..295)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270636"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000269|PubMed:15308621,
                     ECO:0000269|PubMed:16472662, ECO:0000269|PubMed:20333297,
                     ECO:0000269|PubMed:20623637, ECO:0000269|PubMed:20979614,
                     ECO:0000269|PubMed:21169560, ECO:0000269|PubMed:21309750,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Region          395..444
                     /region_name="SH3_9"
                     /note="Variant SH3 domain; pfam14604"
                     /db_xref="CDD:434066"
     Site            order(397,399,404,422,424,439,441..442)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212754"
     Region          449..514
                     /region_name="GTPase_binding"
                     /note="GTPase binding; pfam09027"
                     /db_xref="CDD:430374"
     Region          497..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:21169560; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Region          <543..849
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          623..652
                     /region_name="Required for interaction with SRC.
                     /evidence=ECO:0000269|PubMed:21309750"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          632..635
                     /region_name="Required for interaction with NEDD4.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          659..702
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          718..840
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Site            724
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Region          733..876
                     /region_name="EBD domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          774..840
                     /region_name="Inhibitor_Mig-6"
                     /note="EGFR receptor inhibitor Mig-6; pfam11555"
                     /db_xref="CDD:463294"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:21169560; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Site            839
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O54967; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Site            859
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:21169560; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Site            872
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:21169560; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Site            881
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Region          917..957
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          961..1004
                     /region_name="UBA_ACK1"
                     /note="UBA domain found in activated Cdc42 kinase 1 (ACK1)
                     and similar proteins; cd14274"
                     /db_xref="CDD:270460"
     Region          991..1030
                     /region_name="UBA_TNK1"
                     /note="UBA domain found in non-receptor tyrosine-protein
                     kinase TNK1 and similar proteins; cd14328"
                     /db_xref="CDD:270513"
     CDS             1..1040
                     /gene="TNK2"
                     /gene_synonym="ACK; ACK-1; ACK1; p21cdc42Hs"
                     /coded_by="NM_001387711.1:52..3174"
                     /note="isoform 8 is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS93441.1"
                     /db_xref="GeneID:10188"
                     /db_xref="HGNC:HGNC:19297"
                     /db_xref="MIM:606994"
ORIGIN      
        1 mqpeegtgwl lellsevqlq qyflrlrddl nvtrlshfey vknedlekig mgrpgqrrlw
       61 eavkrrkalc krkswmskvf sgkrleaefp phhsqstfrk tspapggpag egplqsltcl
      121 igekdlrlle klgdgsfgvv rrgewdapsg ktvsvavkcl kpdvlsqpea mddfirevna
      181 mhsldhrnli rlygvvltpp mkmvtelapl gslldrlrkh qghfllgtls ryavqvaegm
      241 gyleskrfih rdlaarnlll atrdlvkigd fglmralpqn ddhyvmqehr kvpfawcape
      301 slktrtfsha sdtwmfgvtl wemftygqep wiglngsqil hkidkegerl prpedcpqdi
      361 ynvmvqcwah kpedrptfva lrdflleaqp tdmralqdfe epdklhiqmn dvitviegra
      421 enywwrgqnt rtlcvgpfpr nvvtsvagls aqdisqplqn sfihtghgds dprhcwgfpd
      481 ridelylgnp mdppdllsve lstsrppqhl ggvkkptydp vsedqdplss dfkrlglrkp
      541 glprglwlak psarvpgtka srgsgaevtl idfgeepvvp alrpcapsla qlamdacsll
      601 detppqsptr alprplhptp vvdwdarplp pppayddvaq deddfeicsi nstlvgagvp
      661 agpsqgqtny afvpeqarpp pplednlflp pqgggkppss aqtaeifqal qqecmrqlqa
      721 pagspapsps pggddkpqvp prvpipprpt rphvqlspap pgeeetsqwp gpaspprvpp
      781 replspqgsr tpsplvppgs splpprlsss pgktmpttqs fasdpkyatp qviqapgpra
      841 gpcilpivrd gkkvssthyy llperpsyle ryqrflreaq speeptplpv plllpppstp
      901 apaaptatvr pmpqaaldpk anfstnnsnp garpppprat arlpqrgcpg dgpeagrpad
      961 kiqmlqamvh gvtteecqaa lqchgwsvqr aaqylkveql fglglrprge chkvlemfdw
     1021 nleqagchll gswgpahhkr
//
LOCUS       NP_002649                431 aa            linear   PRI 21-NOV-2025
DEFINITION  urokinase-type plasminogen activator isoform 1 preproprotein [Homo
            sapiens].
ACCESSION   NP_002649
VERSION     NP_002649.2
DBSOURCE    REFSEQ: accession NM_002658.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Li,D., Ding,C., Huang,F., Chang,M., Lu,Z., Li,G., Li,Y., Gao,H. and
            Sun,F.
  TITLE     Bioinformatics Analysis of the Expression and Prognostic Value of
            PLAU Gene in Wilms' Tumor
  JOURNAL   Anticancer Res 44 (9), 3829-3842 (2024)
   PUBMED   39197889
  REMARK    GeneRIF: Bioinformatics Analysis of the Expression and Prognostic
            Value of PLAU Gene in Wilms' Tumor.
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Guo,J., Wang,H., Huang,C., Lai,C., Shang,W., Luo,S. and Chen,L.
  TITLE     PLAU, transcriptionally negatively regulated by GATA6, promotes
            lung squamous carcinoma cell proliferation and migration
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (5), 119744 (2024)
   PUBMED   38702016
  REMARK    GeneRIF: PLAU, transcriptionally negatively regulated by GATA6,
            promotes lung squamous carcinoma cell proliferation and migration.
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Cui,X., Sun,H., Liu,X., Bai,Y., Bai,Y., Cui,Y., Wang,B., Zhang,S.
            and Li,X.
  TITLE     PLAU promotes cell proliferation and migration of head and neck
            cancer via STAT3 signaling pathway
  JOURNAL   Exp Cell Res 438 (2), 114056 (2024)
   PUBMED   38663475
  REMARK    GeneRIF: PLAU promotes cell proliferation and migration of head and
            neck cancer via STAT3 signaling pathway.
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Cetinsoy,O., Anyanwu,I., Krishnanand,H., Natarajan,G.,
            Ramachandran,N., Thomas,A. and Brookes,K.J.
  TITLE     Gene Association Study of the Urokinase Plasminogen Activator and
            Its Receptor Gene in Alzheimer's Disease
  JOURNAL   J Alzheimers Dis 99 (1), 241-250 (2024)
   PUBMED   38669542
  REMARK    GeneRIF: Gene Association Study of the Urokinase Plasminogen
            Activator and Its Receptor Gene in Alzheimer's Disease.
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Mekkawy,A.H., Pourgholami,M.H. and Morris,D.L.
  TITLE     Involvement of urokinase-type plasminogen activator system in
            cancer: an overview
  JOURNAL   Med Res Rev 34 (5), 918-956 (2014)
   PUBMED   24549574
  REMARK    Review article
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Naldini,L., Tamagnone,L., Vigna,E., Sachs,M., Hartmann,G.,
            Birchmeier,W., Daikuhara,Y., Tsubouchi,H., Blasi,F. and
            Comoglio,P.M.
  TITLE     Extracellular proteolytic cleavage by urokinase is required for
            activation of hepatocyte growth factor/scatter factor
  JOURNAL   EMBO J 11 (13), 4825-4833 (1992)
   PUBMED   1334458
REFERENCE   8  (residues 1 to 431)
  AUTHORS   Li,X., Smith,R.A. and Dobson,C.M.
  TITLE     Sequential 1H NMR assignments and secondary structure of the
            kringle domain from urokinase
  JOURNAL   Biochemistry 31 (40), 9562-9571 (1992)
   PUBMED   1327118
REFERENCE   9  (residues 1 to 431)
  AUTHORS   Stephens,R.W., Aumailley,M., Timpl,R., Reisberg,T., Tapiovaara,H.,
            Myohanen,H., Murphy-Ullrich,J. and Vaheri,A.
  TITLE     Urokinase binding to laminin-nidogen. Structural requirements and
            interactions with heparin
  JOURNAL   Eur J Biochem 207 (3), 937-942 (1992)
   PUBMED   1499567
REFERENCE   10 (residues 1 to 431)
  AUTHORS   Moroi,M. and Aoki,N.
  TITLE     Isolation and characterization of alpha2-plasmin inhibitor from
            human plasma. A novel proteinase inhibitor which inhibits
            activator-induced clot lysis
  JOURNAL   J Biol Chem 251 (19), 5956-5965 (1976)
   PUBMED   134998
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC349055.1, BC013575.2,
            AL596247.22 and AB208961.1.
            
            On Jan 1, 2020 this sequence version replaced NP_002649.1.
            
            Summary: This gene encodes a secreted serine protease that converts
            plasminogen to plasmin. The encoded preproprotein is
            proteolytically processed to generate A and B polypeptide chains.
            These chains associate via a single disulfide bond to form the
            catalytically inactive high molecular weight urokinase-type
            plasminogen activator (HMW-uPA). HMW-uPA can be further processed
            into the catalytically active low molecular weight urokinase-type
            plasminogen activator (LMW-uPA). This low molecular weight form
            does not bind to the urokinase-type plasminogen activator receptor.
            Mutations in this gene may be associated with Quebec platelet
            disorder and late-onset Alzheimer's disease. Alternative splicing
            results in multiple transcript variants, at least one of which
            encodes an isoform that is proteolytically processed. [provided by
            RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M15476.1, AK312960.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372764.4/ ENSP00000361850.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..431
                     /product="urokinase-type plasminogen activator isoform 1
                     preproprotein"
                     /EC_number="3.4.21.73"
                     /note="plasminogen activator, urinary; U-plasminogen
                     activator; urokinase-type plasminogen activator"
                     /calculated_mol_wt=46384
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2158
     mat_peptide     21..431
                     /product="Urokinase-type plasminogen activator.
                     /id=PRO_0000028318"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=46384
     mat_peptide     21..177
                     /product="Urokinase-type plasminogen activator long chain
                     A. /id=PRO_0000028319"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=17849
     Region          34..57
                     /region_name="Binds urokinase plasminogen activator
                     surface receptor. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
     Site            38
                     /site_type="glycosylation"
                     /note="O-linked (Fuc) threonine.
                     /evidence=ECO:0000269|PubMed:2023947; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Region          67..152
                     /region_name="KR"
                     /note="Kringle domain; Kringle domains are believed to
                     play a role in binding mediators, such as peptides, other
                     proteins, membranes, or phospholipids. They are autonomous
                     structural domains, found in a varying number of copies,
                     in blood clotting and...; cd00108"
                     /db_xref="CDD:238056"
     Site            79
                     /site_type="active"
                     /note="putative domain interaction site [active]"
                     /db_xref="CDD:238056"
     Site            order(94,104,132,134,143)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Region          152..177
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
     mat_peptide     156..177
                     /product="Urokinase-type plasminogen activator short chain
                     A. /id=PRO_0000028320"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=2574
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9151681; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Site            177..178
                     /site_type="cleavage"
                     /note="Cleavage, during zymogen activation; propagated
                     from UniProtKB/Swiss-Prot (P00749.3)"
     mat_peptide     179..431
                     /product="Urokinase-type plasminogen activator chain B.
                     /id=PRO_0000028321"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=28425
     Region          179..422
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            179
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(224,275,376)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            322
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine. /id=CAR_000026;
                     propagated from UniProtKB/Swiss-Prot (P00749.3)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9151681; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Site            order(370,395,397)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..431
                     /gene="PLAU"
                     /gene_synonym="ATF; BDPLT5; QPD; u-PA; UPA; URK"
                     /coded_by="NM_002658.6:119..1414"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS7339.1"
                     /db_xref="GeneID:5328"
                     /db_xref="HGNC:HGNC:9052"
                     /db_xref="MIM:191840"
ORIGIN      
        1 mrallarlll cvlvvsdskg snelhqvpsn cdclnggtcv snkyfsnihw cncpkkfggq
       61 hceidksktc yegnghfyrg kastdtmgrp clpwnsatvl qqtyhahrsd alqlglgkhn
      121 ycrnpdnrrr pwcyvqvglk llvqecmvhd cadgkkpssp peelkfqcgq ktlrprfkii
      181 ggefttienq pwfaaiyrrh rggsvtyvcg gslispcwvi sathcfidyp kkedyivylg
      241 rsrlnsntqg emkfevenli lhkdysadtl ahhndiallk irskegrcaq psrtiqticl
      301 psmyndpqfg tsceitgfgk enstdylype qlkmtvvkli shrecqqphy ygsevttkml
      361 caadpqwktd scqgdsggpl vcslqgrmtl tgivswgrgc alkdkpgvyt rvshflpwir
      421 shtkeengla l
//
LOCUS       NP_940966                457 aa            linear   PRI 21-NOV-2025
DEFINITION  dynein axonemal heavy chain 12 isoform 2 [Homo sapiens].
ACCESSION   NP_940966 XP_351556
VERSION     NP_940966.2
DBSOURCE    REFSEQ: accession NM_198564.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Yang,M., Hussain,H.M.J., Khan,M., Muhammad,Z., Zhou,J., Ma,A.,
            Huang,X., Ye,J., Chen,M., Zhi,A., Liu,T., Khan,R., Asim,A.,
            Shah,W., Zeb,A., Ahmad,N., Zhang,H., Xu,B., Ma,H., Shi,Q. and
            Shi,B.
  TITLE     Deficiency in DNAH12 causes male infertility by impairing DNAH1 and
            DNALI1 recruitment in humans and mice
  JOURNAL   Elife 13, 100350 (2025)
   PUBMED   40146200
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Johansson,M., Rocha,N., Zwart,W., Jordens,I., Janssen,L., Kuijl,C.,
            Olkkonen,V.M. and Neefjes,J.
  TITLE     Activation of endosomal dynein motors by stepwise assembly of
            Rab7-RILP-p150Glued, ORP1L, and the receptor betalll spectrin
  JOURNAL   J Cell Biol 176 (4), 459-471 (2007)
   PUBMED   17283181
  REMARK    GeneRIF: Dynein will initiate translocation of late endosomes to
            microtubule minus ends only after interacting with betaIII
            spectrin, which requires the activities of Rab7-RILP and ORP1L.
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Driskell,O.J., Mironov,A., Allan,V.J. and Woodman,P.G.
  TITLE     Dynein is required for receptor sorting and the morphogenesis of
            early endosomes
  JOURNAL   Nat Cell Biol 9 (1), 113-120 (2007)
   PUBMED   17173037
  REMARK    GeneRIF: We show that EGF relocates to the cell centre in a
            dynein-dependent fashion, concomitant with the sorting away of
            transferrin receptor, although it remains in Rab5-positive early
            endosomes.
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Neesen,J., Koehler,M.R., Kirschner,R., Steinlein,C.,
            Kreutzberger,J., Engel,W. and Schmid,M.
  TITLE     Identification of dynein heavy chain genes expressed in human and
            mouse testis: chromosomal localization of an axonemal dynein gene
  JOURNAL   Gene 200 (1-2), 193-202 (1997)
   PUBMED   9373155
REFERENCE   5  (residues 1 to 457)
  AUTHORS   Chapelin,C., Duriez,B., Magnino,F., Goossens,M., Escudier,E. and
            Amselem,S.
  TITLE     Isolation of several human axonemal dynein heavy chain genes:
            genomic structure of the catalytic site, phylogenetic analysis and
            chromosomal assignment
  JOURNAL   FEBS Lett 412 (2), 325-330 (1997)
   PUBMED   9256245
REFERENCE   6  (residues 1 to 457)
  AUTHORS   Vaughan,K.T., Mikami,A., Paschal,B.M., Holzbaur,E.L., Hughes,S.M.,
            Echeverri,C.J., Moore,K.J., Gilbert,D.J., Copeland,N.G.,
            Jenkins,N.A. and Vallee,R.B.
  TITLE     Multiple mouse chromosomal loci for dynein-based motility
  JOURNAL   Genomics 36 (1), 29-38 (1996)
   PUBMED   8812413
REFERENCE   7  (residues 1 to 457)
  AUTHORS   Vaisberg,E.A., Grissom,P.M. and McIntosh,J.R.
  TITLE     Mammalian cells express three distinct dynein heavy chains that are
            localized to different cytoplasmic organelles
  JOURNAL   J Cell Biol 133 (4), 831-842 (1996)
   PUBMED   8666668
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CD708076.1, AK126276.1, CD684932.1 and AC092418.3.
            
            On Mar 9, 2006 this sequence version replaced NP_940966.1.
            
            Transcript Variant: This variant (2) lacks multiple 3' exons but
            has an alternate 3' exon, as compared to variant 3. The resulting
            isoform (2) is much shorter and has a different C-terminus, as
            compared to isoform 3.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK126276.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.3"
     Protein         1..457
                     /product="dynein axonemal heavy chain 12 isoform 2"
                     /note="dynein, axonemal, heavy polypeptide 12; dynein,
                     heavy chain-5; axonemal dynein heavy chain isotype3;
                     ciliary dynein heavy chain 12; axonemal beta dynein heavy
                     chain 12; dynein heavy chain domain-containing protein 2"
                     /calculated_mol_wt=52555
     CDS             1..457
                     /gene="DNAH12"
                     /gene_synonym="DHC3; DLP12; DLP3; DNAH12L; DNAH7L;
                     DNAHC12; DNAHC3; DNHD2; HDHC3; HL-19; HL19; SPGF100"
                     /coded_by="NM_198564.4:182..1555"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS33771.1"
                     /db_xref="GeneID:201625"
                     /db_xref="HGNC:HGNC:2943"
                     /db_xref="MIM:603340"
ORIGIN      
        1 msdankaaia aekealnlkl ppivhlpeni gvdtptqskl lkyrrskeqq qkinqlvidg
       61 akrnldrtlg krtpllpppd ypqtmtsemk kkgfnyiymk qcvessplvp iqqewldhml
      121 rlipeslkeg kereellesl inevssdfen smkrylvqsv lvkppvksle deggplpesp
      181 vgldysnpwh ssyvqarnqi fsnlhiihpt mkmlldlgyt tfadtvlldf tgirakgpid
      241 ceslktdlsi qtrnaeekim ntwypkvinl ftkkealegv kpekldafys cvstlmsnql
      301 kdllrrtveg fvklfdpkdq qrlpifkiel tfdddkmefy ptfqdlednv lslveriaea
      361 lqnvqtipsw lsgtstpvnl dtelpehvlh wavdtlkaav hrnlegarkh yetyvekynw
      421 lldgtaveni etfqtedhtf deyteeldcw vvwevyf
//
LOCUS       NP_000924               1194 aa            linear   PRI 21-NOV-2025
DEFINITION  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4
            isoform a [Homo sapiens].
ACCESSION   NP_000924 XP_024307670
VERSION     NP_000924.3
DBSOURCE    REFSEQ: accession NM_000933.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1194)
  AUTHORS   Aparicio-Bautista,D.I., Jimenez-Ortega,R.F., Becerra-Cervera,A.,
            Aquino-Galvez,A., de Leon-Suarez,V.P., Casas-Avila,L., Salmeron,J.,
            Hidalgo-Bravo,A., Rivera-Paredez,B. and Velazquez-Cruz,R.
  TITLE     Interaction between MARK3 (rs11623869), PLCB4 (rs6086746) and
            GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women
  JOURNAL   Front Endocrinol (Lausanne) 15, 1392063 (2024)
   PUBMED   38715801
  REMARK    GeneRIF: Interaction between MARK3 (rs11623869), PLCB4 (rs6086746)
            and GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1194)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1194)
  AUTHORS   Kanai,S.M., Heffner,C., Cox,T.C., Cunningham,M.L., Perez,F.A.,
            Bauer,A.M., Reigan,P., Carter,C., Murray,S.A. and Clouthier,D.E.
  TITLE     Auriculocondylar syndrome 2 results from the dominant-negative
            action of PLCB4 variants
  JOURNAL   Dis Model Mech 15 (4) (2022)
   PUBMED   35284927
  REMARK    GeneRIF: Auriculocondylar syndrome 2 results from the
            dominant-negative action of PLCB4 variants.
REFERENCE   4  (residues 1 to 1194)
  AUTHORS   Phan,H.T.N., Kim,N.H., Wei,W., Tall,G.G. and Smrcka,A.V.
  TITLE     Uveal melanoma-associated mutations in PLCbeta4 are constitutively
            activating and promote melanocyte proliferation and tumorigenesis
  JOURNAL   Sci Signal 14 (713), eabj4243 (2021)
   PUBMED   34905385
  REMARK    GeneRIF: Uveal melanoma-associated mutations in PLCbeta4 are
            constitutively activating and promote melanocyte proliferation and
            tumorigenesis.
REFERENCE   5  (residues 1 to 1194)
  AUTHORS   Tsai,D.J., Fang,W.H., Wu,L.W., Tai,M.C., Kao,C.C., Huang,S.M.,
            Chen,W.T., Hsiao,P.J., Chiu,C.C., Su,W., Wu,C.C. and Su,S.L.
  TITLE     The Polymorphism at PLCB4 Promoter (rs6086746) Changes the Binding
            Affinity of RUNX2 and Affects Osteoporosis Susceptibility: An
            Analysis of Bioinformatics-Based Case-Control Study and Functional
            Validation
  JOURNAL   Front Endocrinol (Lausanne) 12, 730686 (2021)
   PUBMED   34899595
  REMARK    GeneRIF: The Polymorphism at PLCB4 Promoter (rs6086746) Changes the
            Binding Affinity of RUNX2 and Affects Osteoporosis Susceptibility:
            An Analysis of Bioinformatics-Based Case-Control Study and
            Functional Validation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1194)
  AUTHORS   Lyu,M.S., Park,D.J., Rhee,S.G. and Kozak,C.A.
  TITLE     Genetic mapping of the human and mouse phospholipase C genes
  JOURNAL   Mamm Genome 7 (7), 501-504 (1996)
   PUBMED   8672127
REFERENCE   7  (residues 1 to 1194)
  AUTHORS   Alvarez,R.A., Ghalayini,A.J., Xu,P., Hardcastle,A.,
            Bhattacharya,S., Rao,P.N., Pettenati,M.J., Anderson,R.E. and
            Baehr,W.
  TITLE     cDNA sequence and gene locus of the human retinal
            phosphoinositide-specific phospholipase-C beta 4 (PLCB4)
  JOURNAL   Genomics 29 (1), 53-61 (1995)
   PUBMED   8530101
REFERENCE   8  (residues 1 to 1194)
  AUTHORS   Zauli,G., Previati,M., Caramelli,E., Bassini,A., Falcieri,E.,
            Gibellini,D., Bertolaso,L., Bosco,D., Robuffo,I. and Capitani,S.
  TITLE     Exogenous human immunodeficiency virus type-1 Tat protein
            selectively stimulates a phosphatidylinositol-specific
            phospholipase C nuclear pathway in the Jurkat T cell line
  JOURNAL   Eur J Immunol 25 (9), 2695-2700 (1995)
   PUBMED   7589147
REFERENCE   9  (residues 1 to 1194)
  AUTHORS   Berstein,G., Blank,J.L., Jhon,D.Y., Exton,J.H., Rhee,S.G. and
            Ross,E.M.
  TITLE     Phospholipase C-beta 1 is a GTPase-activating protein for Gq/11,
            its physiologic regulator
  JOURNAL   Cell 70 (3), 411-418 (1992)
   PUBMED   1322796
REFERENCE   10 (residues 1 to 1194)
  AUTHORS   Banno,Y., Yada,Y. and Nozawa,Y.
  TITLE     Purification and characterization of membrane-bound phospholipase C
            specific for phosphoinositides from human platelets
  JOURNAL   J Biol Chem 263 (23), 11459-11465 (1988)
   PUBMED   2841328
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121898.23, AL121909.10,
            AL023805.2 and AL031652.4.
            
            On or before Dec 17, 2019 this sequence version replaced
            XP_024307670.1, NP_000924.2.
            
            Summary: The protein encoded by this gene catalyzes the formation
            of inositol 1,4,5-trisphosphate and diacylglycerol from
            phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium
            as a cofactor and plays an important role in the intracellular
            transduction of many extracellular signals in the retina. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Feb 2010].
            
            Transcript Variant: This variant (1) lacks an alternate in-frame
            exon in the central coding region and includes an alternate exon in
            the 3' coding region that results in a frameshift, compared to
            variant 3. The complete exon combination of the 5' UTR for this
            variant has not been determined. The resulting isoform (a) lacks an
            internal segment and has a longer and distinct C-terminus, compared
            to isoform c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.224246.1,
                                           SRR1660803.262900.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1194
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.3-p12.2"
     Protein         1..1194
                     /product="1-phosphatidylinositol 4,5-bisphosphate
                     phosphodiesterase beta-4 isoform a"
                     /EC_number="3.1.4.11"
                     /note="PLC-beta-4; triphosphoinositide phosphodiesterase;
                     phosphoinositidase C; monophosphatidylinositol
                     phosphodiesterase;
                     1-phosphatidyl-D-myo-inositol-4,5-bisphosphate;
                     inositoltrisphosphohydrolase; dJ1119D9.2 (Phopholipase C,
                     beta 4 (1-Phosphatidylinositol-4,5-Bisphosphate
                     Phosphodiesterase Beta 4)); phosphoinositide phospholipase
                     C-beta-4"
                     /calculated_mol_wt=135976
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.4;
                     propagated from UniProtKB/Swiss-Prot (Q15147.3)"
     Region          17..143
                     /region_name="PH_PLC_beta"
                     /note="Phospholipase C-beta (PLC-beta) pleckstrin homology
                     (PH) domain; cd13361"
                     /db_xref="CDD:270167"
     Site            order(22,24,36,53,117)
                     /site_type="other"
                     /note="Rac1 binding site [polypeptide binding]"
                     /db_xref="CDD:270167"
     Site            order(25,27,33,35,37,52..53)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270167"
     Region          148..300
                     /region_name="EFh_PI-PLCbeta4"
                     /note="EF-hand motif found in phosphoinositide
                     phospholipase C beta 4 (PI-PLC-beta4); cd16211"
                     /db_xref="CDD:320041"
     Region          148..177
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320041"
     Region          183..212
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320041"
     Region          221..250
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320041"
     Region          267..300
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320041"
     Region          312..668
                     /region_name="PI-PLCc_beta"
                     /note="Catalytic domain of metazoan
                     phosphoinositide-specific phospholipase C-beta; cd08591"
                     /db_xref="CDD:176533"
     Site            order(328..329,358,360,375,409,461,463,594,621,623)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176533"
     Site            order(328,375)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176533"
     Site            order(329,358,360,409)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:176533"
     Region          482..511
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15147.3)"
     Region          702..818
                     /region_name="C2_PLC_like"
                     /note="C2 domain present in Phosphoinositide-specific
                     phospholipases C (PLC); cd00275"
                     /db_xref="CDD:175974"
     Site            order(719,745,776,778,780,782)
                     /site_type="other"
                     /note="Ca2+ binding pocket [ion binding]"
                     /db_xref="CDD:175974"
     Region          <847..1194
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          863..895
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15147.3)"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15147.3)"
     Region          913..955
                     /region_name="DUF1154"
                     /note="Protein of unknown function (DUF1154); pfam06631"
                     /db_xref="CDD:461969"
     Region          1082..1110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15147.3)"
     CDS             1..1194
                     /gene="PLCB4"
                     /gene_synonym="ARCND2; ARCND2A; ARCND2B; PI-PLC"
                     /coded_by="NM_000933.4:255..3839"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13104.1"
                     /db_xref="GeneID:5332"
                     /db_xref="HGNC:HGNC:9059"
                     /db_xref="MIM:600810"
ORIGIN      
        1 makpyefnwq kevpsflqeg avfdryeees fvfepnclfk vdefgffltw rsegkegqvl
       61 ecslinsirs gaipkdpkil aaleavgkse ndlegrivcv csgtdlvnis ftymvaenpe
      121 vtkqwveglr siihnfrann vspmtclkkh wmklafmtnt ngkipvrsit rtfasgktek
      181 vifqalkelg lpsgkndeie ptafsyekfy eltqkicprt diedlfkkin gdktdyltvd
      241 qlvsflnehq rdprlneilf pfydakramq iiemyepded lkkkglissd gfcrylmsde
      301 napvfldrle lyqemdhpla hyfissshnt yltgrqfggk ssvemyrqvl lagcrcveld
      361 cwdgkgedqe piithgkamc tdilfkdviq aiketafvts eypvilsfen hcskyqqykm
      421 skycedlfgd lllkqalesh plepgralps pndlkrkili knkrlkpeve kkqlealrsm
      481 meagesaspa nileddneee iesadqeeea hpefkfgnel saddlghkea vansvkkglv
      541 tvedeqawma sykyvgattn ihpylstmin yaqpvkfqgf hvaeernihy nmssfnesvg
      601 lgylkthaie fvnynkrqms riypkggrvd ssnympqifw nagcqmvsln yqtpdlamql
      661 nqgkfeyngs cgyllkpdfm rrpdrtfdpf setpvdgvia atcsvqvisg qflsdkkigt
      721 yvevdmyglp tdtirkefrt rmvmnnglnp vyneesfvfr kvilpdlavl riavyddnnk
      781 ligqrilpld glqagyrhis lrnegnkpls lptifcnivl ktyvpdgfgd ivdalsdpkk
      841 flsitekrad qmramgiets diadvpsdts kndkkgkant akanvtpqss selrptttaa
      901 lasgveakkg ielipqvrie dlkqmkaylk hlkkqqkeln slkkkhakeh stmqklhctq
      961 vdkivaqydk eksthekile kamkkkggsn clemkketei kiqtltsdhk skvkeivaqh
     1021 tkewsemint hsaeeqeird lhlsqqcell kkllinaheq qtqqlklshd reskemrahq
     1081 akismenska isqdksiknk aererrvrel nssntkkfle erkrlamkqs kemdqlkkvq
     1141 lehleflekq neqllkscha vsqtqgegda adgeigsrdg pqtsnssmkl qnan
//
LOCUS       NP_001304765             242 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb group RING finger protein 3 isoform a [Homo sapiens].
ACCESSION   NP_001304765
VERSION     NP_001304765.1
DBSOURCE    REFSEQ: accession NM_001317836.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Hu,Y., Cheng,Y., Jiang,X., Zhang,Y., Wang,H., Ren,H., Xu,Y.,
            Jiang,J., Wang,Q., Su,H., Zhang,B. and Qiu,X.
  TITLE     PCGF3 promotes the proliferation and migration of non-small cell
            lung cancer cells via the PI3K/AKT signaling pathway
  JOURNAL   Exp Cell Res 400 (2), 112496 (2021)
   PUBMED   33485844
  REMARK    GeneRIF: PCGF3 promotes the proliferation and migration of
            non-small cell lung cancer cells via the PI3K/AKT signaling
            pathway.
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Mu,G., Xiang,Q., Zhang,Z., Liu,C., Zhang,H., Liu,Z., Pang,X.,
            Jiang,J., Xie,Q., Zhou,S., Wang,Z., Hu,K., Wang,Z., Jiang,S.,
            Qin,X. and Cui,Y.
  TITLE     PNPT1 and PCGF3 variants associated with angiotensin-converting
            enzyme inhibitor-induced cough: a nested case-control genome-wide
            study
  JOURNAL   Pharmacogenomics 21 (9), 601-614 (2020)
   PUBMED   32397904
  REMARK    GeneRIF: PNPT1 and PCGF3 variants associated with
            angiotensin-converting enzyme inhibitor-induced cough: a nested
            case-control genome-wide study.
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Purohit,G., Mukherjee,A.K., Sharma,S. and Chowdhury,S.
  TITLE     Extratelomeric Binding of the Telomere Binding Protein TRF2 at the
            PCGF3 Promoter Is G-Quadruplex Motif-Dependent
  JOURNAL   Biochemistry 57 (16), 2317-2324 (2018)
   PUBMED   29589913
  REMARK    GeneRIF: We demonstrate that promoter binding by TRF2 mediates
            PCGF3 promoter activity, and both the N-terminal and C-terminal
            domains of TRF2 are necessary for promoter activity.
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Marcon,E., Ni,Z., Pu,S., Turinsky,A.L., Trimble,S.S., Olsen,J.B.,
            Silverman-Gavrila,R., Silverman-Gavrila,L., Phanse,S., Guo,H.,
            Zhong,G., Guo,X., Young,P., Bailey,S., Roudeva,D., Zhao,D.,
            Hewel,J., Li,J., Graslund,S., Paduch,M., Kossiakoff,A.A.,
            Lupien,M., Emili,A., Wodak,S.J. and Greenblatt,J.
  TITLE     Human-chromatin-related protein interactions identify a demethylase
            complex required for chromosome segregation
  JOURNAL   Cell Rep 8 (1), 297-310 (2014)
   PUBMED   24981860
REFERENCE   7  (residues 1 to 242)
  AUTHORS   Woodsmith,J., Jenn,R.C. and Sanderson,C.M.
  TITLE     Systematic analysis of dimeric E3-RING interactions reveals
            increased combinatorial complexity in human ubiquitination networks
  JOURNAL   Mol Cell Proteomics 11 (7), M111.016162 (2012)
   PUBMED   22493164
REFERENCE   8  (residues 1 to 242)
  AUTHORS   Oudot-Mellakh,T., Cohen,W., Germain,M., Saut,N., Kallel,C.,
            Zelenika,D., Lathrop,M., Tregouet,D.A. and Morange,P.E.
  TITLE     Genome wide association study for plasma levels of natural
            anticoagulant inhibitors and protein C anticoagulant pathway: the
            MARTHA project
  JOURNAL   Br J Haematol 157 (2), 230-239 (2012)
   PUBMED   22443383
REFERENCE   9  (residues 1 to 242)
  AUTHORS   Gao,Z., Zhang,J., Bonasio,R., Strino,F., Sawai,A., Parisi,F.,
            Kluger,Y. and Reinberg,D.
  TITLE     PCGF homologs, CBX proteins, and RYBP define functionally distinct
            PRC1 family complexes
  JOURNAL   Mol Cell 45 (3), 344-356 (2012)
   PUBMED   22325352
REFERENCE   10 (residues 1 to 242)
  AUTHORS   Vandamme,J., Volkel,P., Rosnoblet,C., Le Faou,P. and Angrand,P.O.
  TITLE     Interaction proteomics analysis of polycomb proteins defines
            distinct PRC1 complexes in mammalian cells
  JOURNAL   Mol Cell Proteomics 10 (4), M110.002642 (2011)
   PUBMED   21282530
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107464.5 and AC139887.3.
            
            Summary: The protein encoded by this gene contains a C3HC4 type
            RING finger, which is a motif known to be involved in
            protein-protein interactions. The specific function of this protein
            has not yet been determined. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). Variants 1-7 all encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.689155.1,
                                           SRR14038197.2095885.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..242
                     /product="polycomb group RING finger protein 3 isoform a"
                     /note="ring finger protein 3; polycomb group RING finger
                     protein 3; RING finger protein 3A"
                     /calculated_mol_wt=27984
     Region          4..69
                     /region_name="RING-HC_PCGF3"
                     /note="RING finger found in polycomb group RING finger
                     protein 3 (PCGF3) and similar proteins; cd16735"
                     /db_xref="CDD:438393"
     Site            order(16,20,22..23,26,28..29,31..35,38..41,43..44)
                     /site_type="other"
                     /note="putative heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:438393"
     Region          115..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KNV8.1)"
     Region          132..242
                     /region_name="Interaction with BCORL1.
                     /evidence=ECO:0000269|PubMed:27568929"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KNV8.1)"
     Region          154..236
                     /region_name="RAWUL_PCGF3"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in polycomb group RING finger protein
                     3 (PCGF3) and similar proteins; cd17083"
                     /db_xref="CDD:340603"
     CDS             1..242
                     /gene="PCGF3"
                     /gene_synonym="DONG1; RNF3; RNF3A"
                     /coded_by="NM_001317836.3:428..1156"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3339.2"
                     /db_xref="GeneID:10336"
                     /db_xref="HGNC:HGNC:10066"
                     /db_xref="MIM:617543"
ORIGIN      
        1 mltrkiklwd inahitcrlc sgylidattv teclhtfcrs clvkyleenn tcptcrivih
       61 qshplqyigh drtmqdivyk lvpglqeaem rkqrefyhkl gmevpgdikg etcsakqhld
      121 shrngetkad dssnkeaaee kpeedndyhr sdeqvsicle cnssklrglk rkwircsaqa
      181 tvlhlkkfia kklnlssfne ldilcneeil gkdhtlkfvv vtrwrfkkap lllhyrpkmd
      241 ll
//
LOCUS       NP_001005746             502 aa            linear   PRI 21-NOV-2025
DEFINITION  voltage-dependent L-type calcium channel subunit beta-4 isoform c
            [Homo sapiens].
ACCESSION   NP_001005746
VERSION     NP_001005746.1
DBSOURCE    REFSEQ: accession NM_001005746.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Westhoff,M. and Dixon,R.E.
  TITLE     Mechanisms and Regulation of Cardiac CaV1.2 Trafficking
  JOURNAL   Int J Mol Sci 22 (11), 5927 (2021)
   PUBMED   34072954
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Coste de Bagneaux,P., von Elsner,L., Bierhals,T., Campiglio,M.,
            Johannsen,J., Obermair,G.J., Hempel,M., Flucher,B.E. and Kutsche,K.
  TITLE     A homozygous missense variant in CACNB4 encoding the auxiliary
            calcium channel beta4 subunit causes a severe neurodevelopmental
            disorder and impairs channel and non-channel functions
  JOURNAL   PLoS Genet 16 (3), e1008625 (2020)
   PUBMED   32176688
  REMARK    GeneRIF: The homozygous CACNB4 p.(Leu126Pro) variant underlies the
            severe neurological phenotype in the two siblings.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Vendel,A.C., Terry,M.D., Striegel,A.R., Iverson,N.M.,
            Leuranguer,V., Rithner,C.D., Lyons,B.A., Pickard,G.E., Tobet,S.A.
            and Horne,W.A.
  TITLE     Alternative splicing of the voltage-gated Ca2+ channel beta4
            subunit creates a uniquely folded N-terminal protein binding domain
            with cell-specific expression in the cerebellar cortex
  JOURNAL   J Neurosci 26 (10), 2635-2644 (2006)
   PUBMED   16525042
REFERENCE   5  (residues 1 to 502)
  AUTHORS   Helton,T.D. and Horne,W.A.
  TITLE     Alternative splicing of the beta 4 subunit has alpha1 subunit
            subtype-specific effects on Ca2+ channel gating
  JOURNAL   J Neurosci 22 (5), 1573-1582 (2002)
   PUBMED   11880487
REFERENCE   6  (residues 1 to 502)
  AUTHORS   Escayg,A., Jones,J.M., Kearney,J.A., Hitchcock,P.F. and
            Meisler,M.H.
  TITLE     Calcium channel beta 4 (CACNB4): human ortholog of the mouse
            epilepsy gene lethargic
  JOURNAL   Genomics 50 (1), 14-22 (1998)
   PUBMED   9628818
REFERENCE   7  (residues 1 to 502)
  AUTHORS   Burgess,D.L., Jones,J.M., Meisler,M.H. and Noebels,J.L.
  TITLE     Mutation of the Ca2+ channel beta subunit gene Cchb4 is associated
            with ataxia and seizures in the lethargic (lh) mouse
  JOURNAL   Cell 88 (3), 385-392 (1997)
   PUBMED   9039265
REFERENCE   8  (residues 1 to 502)
  AUTHORS   Diriong,S., Lory,P., Williams,M.E., Ellis,S.B., Harpold,M.M. and
            Taviaux,S.
  TITLE     Chromosomal localization of the human genes for alpha 1A, alpha 1B,
            and alpha 1E voltage-dependent Ca2+ channel subunits
  JOURNAL   Genomics 30 (3), 605-609 (1995)
   PUBMED   8825650
REFERENCE   9  (residues 1 to 502)
  AUTHORS   Spacey,S.
  TITLE     Episodic Ataxia Type 2 - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301674
REFERENCE   10 (residues 1 to 502)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079790.6, AK316045.1,
            AC097448.2 and T23939.1.
            
            Summary: This gene encodes a member of the beta subunit family of
            voltage-dependent calcium channel complex proteins. Calcium
            channels mediate the influx of calcium ions into the cell upon
            membrane polarization and consist of a complex of alpha-1,
            alpha-2/delta, beta, and gamma subunits in a 1:1:1:1 ratio. Various
            versions of each of these subunits exist, either expressed from
            similar genes or the result of alternative splicing. The protein
            encoded by this locus plays an important role in calcium channel
            function by modulating G protein inhibition, increasing peak
            calcium current, controlling the alpha-1 subunit membrane targeting
            and shifting the voltage dependence of activation and inactivation.
            Certain mutations in this gene have been associated with idiopathic
            generalized epilepsy (IGE), juvenile myoclonic epilepsy (JME), and
            episodic ataxia, type 5. [provided by RefSeq, Aug 2016].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and 5'
            coding region, compared to variant 2. The resulting isoform (c) has
            a shorter and distinct N-terminus, compared to isoform b.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1110762.1,
                                           SRR1803613.33573.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q23.3"
     Protein         1..502
                     /product="voltage-dependent L-type calcium channel subunit
                     beta-4 isoform c"
                     /note="dihydropyridine-sensitive L-type, calcium channel
                     beta-4 subunit; voltage-dependent L-type calcium channel
                     subunit beta-4; calcium channel voltage-dependent subunit
                     beta 4"
                     /calculated_mol_wt=56291
     Region          32..73
                     /region_name="VGCC_beta4Aa_N"
                     /note="Voltage gated calcium channel subunit beta domain
                     4Aa N terminal; pfam12052"
                     /db_xref="CDD:463445"
     Region          73..140
                     /region_name="SH3_CACNB4"
                     /note="Src Homology 3 domain of Voltage-dependent L-type
                     calcium channel subunit beta4; cd12043"
                     /db_xref="CDD:212976"
     Site            order(83,85,88,99,117..118,134,136..137)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212976"
     Region          200..380
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..502
                     /gene="CACNB4"
                     /gene_synonym="CAB4; CACNLB4; EA5; EIG9; EJM; EJM4; EJM6"
                     /coded_by="NM_001005746.4:115..1623"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS46427.1"
                     /db_xref="GeneID:785"
                     /db_xref="HGNC:HGNC:1404"
                     /db_xref="MIM:601949"
ORIGIN      
        1 mdvvargttt rrsrlkrsdg sttstsfilr qgsadsytsr psdsdvslee dreairqere
       61 qqaaiqlera kskpvafavk tnvsycgald edvpvpstai sfdakdflhi kekynndwwi
      121 grlvkegcei gfipsplrle niriqqeqkr grfhggkssg nsssslgemv sgtfratpts
      181 takqkqkvte hippydvvps mrpvvlvgps lkgyevtdmm qkalfdflkh rfdgrisitr
      241 vtadislakr svlnnpskra iiersntrss laevqseier ifelarslql vvldadtinh
      301 paqliktsla piivhvkvss pkvlqrliks rgksqskhln vqlvaadkla qcppemfdvi
      361 ldenqledac ehlgeyleay wrathttsst pmtpllgrnl gstalspypt aisglqsqrm
      421 rhsnhstens pierrslmts denyhnerar ksrnrlssss qhsrdhyplv eedypdsyqd
      481 tykphrnrgs pggyshdsrh rl
//
LOCUS       NP_001273036             197 aa            linear   PRI 21-NOV-2025
DEFINITION  autophagy protein 5 isoform b [Homo sapiens].
ACCESSION   NP_001273036 XP_005267288
VERSION     NP_001273036.1
DBSOURCE    REFSEQ: accession NM_001286107.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Li,S., Zhang,B.W., Lou,Q.Q., Liu,Y., Wei,Z.J., Huang,J., Yao,K.H.,
            Xu,Q.R., Fan,J., Xi,Y., Yang,L. and Chen,S.
  TITLE     ATG5 nonautophagically regulates inflammation and differentiation
            in mouse embryonic stem cells
  JOURNAL   Autophagy 20 (8), 1897-1898 (2024)
   PUBMED   38477302
  REMARK    GeneRIF: ATG5 nonautophagically regulates inflammation and
            differentiation in mouse embryonic stem cells.
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Li,Q., Wen,W., Wang,Y., Gong,T., Wang,X., Tan,Q., Fan,B., Xie,H.,
            Li,Y., Li,S., Yang,C., Zhou,Z., Duan,X., Lin,W. and Chen,L.
  TITLE     Autophagy-related protein 5 (ATG5) interacts with bone marrow
            stromal cell antigen 2 (BST2) to stimulate HBV replication through
            antagonizing the antiviral activity of BST2
  JOURNAL   J Med Virol 96 (5), e29659 (2024)
   PUBMED   38747016
  REMARK    GeneRIF: Autophagy-related protein 5 (ATG5) interacts with bone
            marrow stromal cell antigen 2 (BST2) to stimulate HBV replication
            through antagonizing the antiviral activity of BST2.
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Chen,F., Wu,L., Zhang,M., Kan,M., Chen,H., Wang,X. and Qu,J.
  TITLE     Autophagy-related 5 in acute ischemic stroke: Variation and linkage
            with neurofunction, and survival
  JOURNAL   Ann Clin Transl Neurol 11 (4), 856-865 (2024)
   PUBMED   38530706
  REMARK    GeneRIF: Autophagy-related 5 in acute ischemic stroke: Variation
            and linkage with neurofunction, and survival.
REFERENCE   5  (residues 1 to 197)
  AUTHORS   Qu,J., Wu,L., Zhang,M., Kan,M., Chen,H., Shi,Y., Wang,S., Wang,X.
            and Chen,F.
  TITLE     Serum autophagy-related gene 5 level in stroke patients:
            correlation with CD4+ T cells and cognition impairment during a
            3-year follow-up
  JOURNAL   Braz J Med Biol Res 57, e13019 (2024)
   PUBMED   38511768
  REMARK    GeneRIF: Serum autophagy-related gene 5 level in stroke patients:
            correlation with CD4+ T cells and cognition impairment during a
            3-year follow-up.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 197)
  AUTHORS   Tanida,I., Tanida-Miyake,E., Ueno,T. and Kominami,E.
  TITLE     The human homolog of Saccharomyces cerevisiae Apg7p is a
            Protein-activating enzyme for multiple substrates including human
            Apg12p, GATE-16, GABARAP, and MAP-LC3
  JOURNAL   J Biol Chem 276 (3), 1701-1706 (2001)
   PUBMED   11096062
REFERENCE   7  (residues 1 to 197)
  AUTHORS   Schmeiser,K., Armstrong,S., Hammond,E.M. and Grand,R.J.
  TITLE     Assignment of the yeast APG5 human homologue APG5L to chromosome
            band 6q21 by fluorescence in situ hybridisation
  JOURNAL   Cytogenet Cell Genet 87 (3-4), 213-214 (1999)
   PUBMED   10702672
REFERENCE   8  (residues 1 to 197)
  AUTHORS   Mizushima,N., Sugita,H., Yoshimori,T. and Ohsumi,Y.
  TITLE     A new protein conjugation system in human. The counterpart of the
            yeast Apg12p conjugation system essential for autophagy
  JOURNAL   J Biol Chem 273 (51), 33889-33892 (1998)
   PUBMED   9852036
REFERENCE   9  (residues 1 to 197)
  AUTHORS   Hammond,E.M., Brunet,C.L., Johnson,G.D., Parkhill,J., Milner,A.E.,
            Brady,G., Gregory,C.D. and Grand,R.J.
  TITLE     Homology between a human apoptosis specific protein and the product
            of APG5, a gene involved in autophagy in yeast
  JOURNAL   FEBS Lett 425 (3), 391-395 (1998)
   PUBMED   9563500
REFERENCE   10 (residues 1 to 197)
  AUTHORS   Grand,R.J., Milner,A.E., Mustoe,T., Johnson,G.D., Owen,D.,
            Grant,M.L. and Gregory,C.D.
  TITLE     A novel protein expressed in mammalian cells undergoing apoptosis
  JOURNAL   Exp Cell Res 218 (2), 439-451 (1995)
   PUBMED   7796880
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP297166.1, CR749386.1 and
            BX537904.1.
            
            On Oct 30, 2013 this sequence version replaced XP_005267288.1.
            
            Summary: The protein encoded by this gene, in combination with
            autophagy protein 12, functions as an E1-like activating enzyme in
            a ubiquitin-like conjugating system. The encoded protein is
            involved in several cellular processes, including autophagic
            vesicle formation, mitochondrial quality control after oxidative
            damage, negative regulation of the innate antiviral immune
            response, lymphocyte development and proliferation, MHC II antigen
            presentation, adipocyte differentiation, and apoptosis. Several
            transcript variants encoding different protein isoforms have been
            found for this gene. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (3) lacks an exon in the 5' coding
            region and initiates translation at an alternate start codon,
            compared to variant 1. The encoded isoform (b) has a distinct
            N-terminus and is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749386.1, SRR18074967.2950941.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..197
                     /product="autophagy protein 5 isoform b"
                     /note="apoptosis-specific protein; ATG5 autophagy related
                     5 homolog; APG5 autophagy 5-like"
                     /calculated_mol_wt=22800
     Region          1..192
                     /region_name="APG5"
                     /note="Autophagy protein Apg5; pfam04106"
                     /db_xref="CDD:461175"
     CDS             1..197
                     /gene="ATG5"
                     /gene_synonym="APG5; APG5-LIKE; APG5L; ASP; hAPG5; SCAR25"
                     /coded_by="NM_001286107.2:400..993"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS69159.1"
                     /db_xref="GeneID:9474"
                     /db_xref="HGNC:HGNC:589"
                     /db_xref="MIM:604261"
ORIGIN      
        1 mhypigllfd llasssalpw nitvhfksfp ekdllhcpsk daieahfmsc mkeadalkhk
       61 sqvinemqkk dhkqlwmglq ndrfdqfwai nrklmeypae engfryipfr iyqttterpf
      121 iqklfrpvaa dgqlhtlgdl lkevcpsaid pedgekknqv mihgiepmle tplqwlsehl
      181 sypdnflhis iipqptd
//
LOCUS       NP_950245                384 aa            linear   PRI 21-NOV-2025
DEFINITION  5-cytosine rRNA methyltransferase NSUN4 isoform a [Homo sapiens].
ACCESSION   NP_950245 XP_371247
VERSION     NP_950245.2
DBSOURCE    REFSEQ: accession NM_199044.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Zhao,Z., Zhou,Y., Lv,P., Zhou,T., Liu,H., Xie,Y., Wu,Z., Wang,X.,
            Zhao,H., Zheng,J. and Jiang,X.
  TITLE     NSUN4 mediated RNA 5-methylcytosine promotes the malignant
            progression of glioma through improving the CDC42 mRNA
            stabilization
  JOURNAL   Cancer Lett 597, 217059 (2024)
   PUBMED   38876383
  REMARK    GeneRIF: NSUN4 mediated RNA 5-methylcytosine promotes the malignant
            progression of glioma through improving the CDC42 mRNA
            stabilization.
            Erratum:[Cancer Lett. 2025 Feb 1;610:217351. doi:
            10.1016/j.canlet.2024.217351. PMID: 39616022]
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Kim,S., Tan,S., Ku,J., Widowati,T.A., Ku,D., Lee,K., You,K. and
            Kim,Y.
  TITLE     RNA 5-methylcytosine marks mitochondrial double-stranded RNAs for
            degradation and cytosolic release
  JOURNAL   Mol Cell 84 (15), 2935-2948 (2024)
   PUBMED   39019044
  REMARK    Erratum:[Mol Cell. 2025 Feb 20;85(4):857. doi:
            10.1016/j.molcel.2025.01.029. PMID: 39909040]
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Nguyen,T.G., Ritter,C. and Kummer,E.
  TITLE     Structural insights into the role of GTPBP10 in the RNA maturation
            of the mitoribosome
  JOURNAL   Nat Commun 14 (1), 7991 (2023)
   PUBMED   38042949
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Cui,M., Qu,F., Wang,L., Liu,X., Yu,J., Tang,Z. and Cheng,D.
  TITLE     m5C RNA methyltransferase-related gene NSUN4 stimulates malignant
            progression of hepatocellular carcinoma and can be a prognostic
            marker
  JOURNAL   Cancer Biomark 33 (3), 389-400 (2022)
   PUBMED   34744073
  REMARK    GeneRIF: m5C RNA methyltransferase-related gene NSUN4 stimulates
            malignant progression of hepatocellular carcinoma and can be a
            prognostic marker.
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Yakubovskaya,E., Guja,K.E., Mejia,E., Castano,S., Hambardjieva,E.,
            Choi,W.S. and Garcia-Diaz,M.
  TITLE     Structure of the essential MTERF4:NSUN4 protein complex reveals how
            an MTERF protein collaborates to facilitate rRNA modification
  JOURNAL   Structure 20 (11), 1940-1947 (2012)
   PUBMED   23022348
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Spahr,H., Habermann,B., Gustafsson,C.M., Larsson,N.G. and
            Hallberg,B.M.
  TITLE     Structure of the human MTERF4-NSUN4 protein complex that regulates
            mitochondrial ribosome biogenesis
  JOURNAL   Proc Natl Acad Sci U S A 109 (38), 15253-15258 (2012)
   PUBMED   22949673
  REMARK    GeneRIF: analysis of the 3D crystal structure of the human
            MTERF4-NSUN4 complex
REFERENCE   8  (residues 1 to 384)
  AUTHORS   Camara,Y., Asin-Cayuela,J., Park,C.B., Metodiev,M.D., Shi,Y.,
            Ruzzenente,B., Kukat,C., Habermann,B., Wibom,R., Hultenby,K.,
            Franz,T., Erdjument-Bromage,H., Tempst,P., Hallberg,B.M.,
            Gustafsson,C.M. and Larsson,N.G.
  TITLE     MTERF4 regulates translation by targeting the methyltransferase
            NSUN4 to the mammalian mitochondrial ribosome
  JOURNAL   Cell Metab 13 (5), 527-539 (2011)
   PUBMED   21531335
REFERENCE   9  (residues 1 to 384)
  AUTHORS   Gratacos,M., Costas,J., de Cid,R., Bayes,M., Gonzalez,J.R.,
            Baca-Garcia,E., de Diego,Y., Fernandez-Aranda,F.,
            Fernandez-Piqueras,J., Guitart,M., Martin-Santos,R., Martorell,L.,
            Menchon,J.M., Roca,M., Saiz-Ruiz,J., Sanjuan,J., Torrens,M.,
            Urretavizcaya,M., Valero,J., Vilella,E., Estivill,X. and
            Carracedo,A.
  CONSRTM   Psychiatric Genetics Network Group
  TITLE     Identification of new putative susceptibility genes for several
            psychiatric disorders by association analysis of regulatory and
            non-synonymous SNPs of 306 genes involved in neurotransmission and
            neurodevelopment
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 150B (6), 808-816 (2009)
   PUBMED   19086053
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 384)
  AUTHORS   Wang,D.D., Shu,Z., Lieser,S.A., Chen,P.L. and Lee,W.H.
  TITLE     Human mitochondrial SUV3 and polynucleotide phosphorylase form a
            330-kDa heteropentamer to cooperatively degrade double-stranded RNA
            with a 3'-to-5' directionality
  JOURNAL   J Biol Chem 284 (31), 20812-20821 (2009)
   PUBMED   19509288
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL122001.32.
            
            On or before Jan 27, 2004 this sequence version replaced
            XP_371247.1, NP_950245.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.232110.1,
                                           ERR4352441.361195.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000474844.6/ ENSP00000419740.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p33"
     Protein         1..384
                     /product="5-cytosine rRNA methyltransferase NSUN4 isoform
                     a"
                     /note="putative methyltransferase NSUN4; NOL1/NOP2/Sun
                     domain family member 4; sperm head and tail associated
                     protein; 5-methylcytosine rRNA methyltransferase NSUN4;
                     NOP2/Sun RNA methyltransferase family member 4; NOP2/Sun
                     domain family, member 4; 5-methylcytosine tRNA
                     methyltransferase NSUN4; 5-cytosine tRNA methyltransferase
                     NSUN4; mRNA cytosine C(5)-methyltransferase NSUN4;
                     5-cytosine rRNA methyltransferase NSUN4"
                     /calculated_mol_wt=40234
     transit_peptide 1..25
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:22949673,
                     ECO:0000269|PubMed:23022348; propagated from
                     UniProtKB/Swiss-Prot (Q96CB9.2)"
                     /calculated_mol_wt=2872
     mat_peptide     26..384
                     /product="5-cytosine rRNA methyltransferase NSUN4.
                     /id=PRO_0000289234"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CB9.2)"
                     /calculated_mol_wt=40234
     Region          <135..326
                     /region_name="RsmB"
                     /note="16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF
                     family [Translation, ribosomal structure and biogenesis];
                     COG0144"
                     /db_xref="CDD:439914"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96CB9.2)"
     CDS             1..384
                     /gene="NSUN4"
                     /gene_synonym="SHTAP"
                     /coded_by="NM_199044.4:21..1175"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS534.1"
                     /db_xref="GeneID:387338"
                     /db_xref="HGNC:HGNC:31802"
                     /db_xref="MIM:615394"
ORIGIN      
        1 maaltlrgvr ellkrvdlat vprrhrykkk waatepkfpa vrlalqnfdm tysvqfgdlw
       61 psirvsllse qkygalvnnf aawdhvsakl eqlsakdfvn eaishwelqs eggqsaapsp
      121 aswacspnlr cftfdrgdis rfpparpgsl gvmeyylmda asllpvlalg lqpgdivldl
      181 caapggktla llqtgccrnl aandlspsri arlqkilhsy vpeeirdgnq vrvtswdgrk
      241 wgelegdtyd rvlvdvpctt drhslheeen nifkrsrkke rqilpvlqvq llaagllatk
      301 pgghvvystc slshlqneyv vqgaiellan qysiqvqved lthfrrvfmd tfcffsscqv
      361 gelvipnlma nfgpmyfckm rrlt
//
LOCUS       NP_001351967             338 aa            linear   PRI 21-NOV-2025
DEFINITION  cytohesin-1 isoform 5 [Homo sapiens].
ACCESSION   NP_001351967
VERSION     NP_001351967.1
DBSOURCE    REFSEQ: accession NM_001365038.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Manzanillo,P., Mouchess,M., Ota,N., Dai,B., Ichikawa,R., Wuster,A.,
            Haley,B., Alvarado,G., Kwon,Y., Caothien,R., Roose-Girma,M.,
            Warming,S., McKenzie,B.S., Keir,M.E., Scherl,A., Ouyang,W. and
            Yi,T.
  TITLE     Inflammatory Bowel Disease Susceptibility Gene C1ORF106 Regulates
            Intestinal Epithelial Permeability
  JOURNAL   Immunohorizons 2 (5), 164-171 (2018)
   PUBMED   31022698
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Nagel,W., Zeitlmann,L., Schilcher,P., Geiger,C., Kolanus,J. and
            Kolanus,W.
  TITLE     Phosphoinositide 3-OH kinase activates the beta2 integrin adhesion
            pathway and induces membrane recruitment of cytohesin-1
  JOURNAL   J Biol Chem 273 (24), 14853-14861 (1998)
   PUBMED   9614087
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Meacci,E., Tsai,S.C., Adamik,R., Moss,J. and Vaughan,M.
  TITLE     Cytohesin-1, a cytosolic guanine nucleotide-exchange protein for
            ADP-ribosylation factor
  JOURNAL   Proc Natl Acad Sci U S A 94 (5), 1745-1748 (1997)
   PUBMED   9050849
REFERENCE   8  (residues 1 to 338)
  AUTHORS   Kolanus,W., Nagel,W., Schiller,B., Zeitlmann,L., Godar,S.,
            Stockinger,H. and Seed,B.
  TITLE     Alpha L beta 2 integrin/LFA-1 binding to ICAM-1 induced by
            cytohesin-1, a cytoplasmic regulatory molecule
  JOURNAL   Cell 86 (2), 233-242 (1996)
   PUBMED   8706128
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Dixon,B., Mansour,M. and Pohajdak,B.
  TITLE     Assignment of human B2-1 gene (D17S811E) to chromosome 17qter by
            PCR analysis of somatic cell hybrids and fluorescence in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 63 (1), 42-44 (1993)
   PUBMED   8449036
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Liu,L. and Pohajdak,B.
  TITLE     Cloning and sequencing of a human cDNA from cytolytic NK/T cells
            with homology to yeast SEC7
  JOURNAL   Biochim Biophys Acta 1132 (1), 75-78 (1992)
   PUBMED   1511013
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022966.13 and AC099804.3.
            
            Summary: The protein encoded by this gene is a member of the PSCD
            family. Members of this family have identical structural
            organization that consists of an N-terminal coiled-coil motif, a
            central Sec7 domain, and a C-terminal pleckstrin homology (PH)
            domain. The coiled-coil motif is involved in homodimerization, the
            Sec7 domain contains guanine-nucleotide exchange protein activity,
            and the PH domain interacts with phospholipids and is responsible
            for association of PSCDs with membranes. Members of this family
            appear to mediate the regulation of protein sorting and membrane
            trafficking. This gene is highly expressed in natural killer and
            peripheral T cells, and regulates the adhesiveness of integrins at
            the plasma membrane of lymphocytes. A pseudogene of this gene has
            been defined on the X chromosome. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.241567.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..338
                     /product="cytohesin-1 isoform 5"
                     /note="pleckstrin homology, Sec7 and coiled-coil domains
                     1; cytoadhesin 1; homolog of secretory protein SEC7; SEC7
                     homolog B2-1; PH, SEC7 and coiled-coil domain-containing
                     protein 1"
                     /calculated_mol_wt=39282
     Region          3..185
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          200..319
                     /region_name="PH_GRP1-like"
                     /note="General Receptor for Phosphoinositides-1-like
                     Pleckstrin homology (PH) domain; cd01252"
                     /db_xref="CDD:269954"
     Site            order(200,227,229,231,241,244,246,277..279,281,284..289,
                     319)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:269954"
     Site            order(210,213,217,219,221,232,242,280,291..292)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269954"
     CDS             1..338
                     /gene="CYTH1"
                     /gene_synonym="B2-1; CYTOHESIN-1; D17S811E; PSCD1; SEC7"
                     /coded_by="NM_001365038.2:426..1442"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:9267"
                     /db_xref="HGNC:HGNC:9501"
                     /db_xref="MIM:182115"
ORIGIN      
        1 mqrnkqvamg rkkfnmdpkk giqfliendl lkntcediaq flykgeglnk taigdylger
       61 defniqvlha fvelheftdl nlvqalrqfl wsfrlpgeaq kidrmmeafa qrycqcnngv
      121 fqstdtcyvl sfaiimlnts lhnpnvkdkp tverfiamnr gindggdlpe ellrnlyesi
      181 knepfkiped dgndlthtff npdregwllk lggrvktwkr rwfiltdncl yyfeyttdke
      241 prgiiplenl sirevedskk pncfelyipd nkdqvikack teadgrvveg nhtvyrisap
      301 tpeekeewik cikaaisrdp fyemlaarkk kvsstkrh
//
LOCUS       NP_001364122             429 aa            linear   PRI 21-NOV-2025
DEFINITION  C-terminal-binding protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001364122 XP_016863256
VERSION     NP_001364122.1
DBSOURCE    REFSEQ: accession NM_001377193.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Kong,Y., Yang,G., Feng,X., Ji,Z., Wang,X., Shao,Y., Meng,J.,
            Yao,G., Ren,C. and Yang,G.
  TITLE     CTBP1 links metabolic syndrome to polycystic ovary syndrome through
            interruption of aromatase and SREBP1
  JOURNAL   Commun Biol 7 (1), 1174 (2024)
   PUBMED   39294274
  REMARK    GeneRIF: CTBP1 links metabolic syndrome to polycystic ovary
            syndrome through interruption of aromatase and SREBP1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Zhou,J., Yan,X., Liu,Y. and Yang,J.
  TITLE     Succinylation of CTBP1 mediated by KAT2A suppresses its inhibitory
            activity on the transcription of CDH1 to promote the progression of
            prostate cancer
  JOURNAL   Biochem Biophys Res Commun 650, 9-16 (2023)
   PUBMED   36764210
  REMARK    GeneRIF: Succinylation of CTBP1 mediated by KAT2A suppresses its
            inhibitory activity on the transcription of CDH1 to promote the
            progression of prostate cancer.
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Lou,L.Q., Zhou,W.Q., Song,X. and Chen,Z.
  TITLE     Elevation of hsa-miR-7-5p level mediated by CtBP1-p300-AP1 complex
            targets ATXN1 to trigger NF-kappaB-dependent inflammation response
  JOURNAL   J Mol Med (Berl) 101 (3), 223-235 (2023)
   PUBMED   36629882
  REMARK    GeneRIF: Elevation of hsa-miR-7-5p level mediated by CtBP1-p300-AP1
            complex targets ATXN1 to trigger NF-kappaB-dependent inflammation
            response.
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Tseng,C., Han,Y., Lv,Z., Song,Q., Wang,K., Shen,H. and Chen,Z.
  TITLE     The CRL4DCAF6 E3 ligase ubiquitinates CtBP1/2 to induce apoptotic
            signalling and promote intervertebral disc degeneration
  JOURNAL   J Mol Med (Berl) 101 (1-2), 171-181 (2023)
   PUBMED   36688959
  REMARK    GeneRIF: The CRL4[DCAF6] E3 ligase ubiquitinates CtBP1/2 to induce
            apoptotic signalling and promote intervertebral disc degeneration.
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Schaeper,U., Subramanian,T., Lim,L., Boyd,J.M. and Chinnadurai,G.
  TITLE     Interaction between a cellular protein that binds to the C-terminal
            region of adenovirus E1A (CtBP) and a novel cellular protein is
            disrupted by E1A through a conserved PLDLS motif
  JOURNAL   J Biol Chem 273 (15), 8549-8552 (1998)
   PUBMED   9535825
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Katsanis,N. and Fisher,E.M.
  TITLE     A novel C-terminal binding protein (CTBP2) is closely related to
            CTBP1, an adenovirus E1A-binding protein, and maps to human
            chromosome 21q21.3
  JOURNAL   Genomics 47 (2), 294-299 (1998)
   PUBMED   9479502
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Schaeper,U., Boyd,J.M., Verma,S., Uhlmann,E., Subramanian,T. and
            Chinnadurai,G.
  TITLE     Molecular cloning and characterization of a cellular phosphoprotein
            that interacts with a conserved C-terminal domain of adenovirus E1A
            involved in negative modulation of oncogenic transformation
  JOURNAL   Proc Natl Acad Sci U S A 92 (23), 10467-10471 (1995)
   PUBMED   7479821
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1998 Nov 24;95(24):14584]
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Boyd,J.M., Subramanian,T., Schaeper,U., La Regina,M., Bayley,S. and
            Chinnadurai,G.
  TITLE     A region in the C-terminus of adenovirus 2/5 E1a protein is
            required for association with a cellular phosphoprotein and
            important for the negative modulation of T24-ras mediated
            transformation, tumorigenesis and metastasis
  JOURNAL   EMBO J 12 (2), 469-478 (1993)
   PUBMED   8440238
REFERENCE   10 (residues 1 to 429)
  AUTHORS   Battaglia,A., Carey,J.C. and South,S.T.
  TITLE     Wolf-Hirschhorn Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301362
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092535.4.
            
            On Dec 17, 2019 this sequence version replaced XP_016863256.1.
            
            Summary: This gene encodes a protein that binds to the C-terminus
            of adenovirus E1A proteins. This phosphoprotein is a
            transcriptional repressor and may play a role during cellular
            proliferation. This protein and the product of a second closely
            related gene, CTBP2, can dimerize. Both proteins can also interact
            with a polycomb group protein complex which participates in
            regulation of gene expression during development. Alternative
            splicing of transcripts from this gene results in multiple
            transcript variants. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2723145.1,
                                           SRR14038194.2506537.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..429
                     /product="C-terminal-binding protein 1 isoform 2"
                     /note="brefeldin A-ribosylated substrate"
                     /calculated_mol_wt=46274
     Region          17..335
                     /region_name="CtBP_dh"
                     /note="C-terminal binding protein (CtBP),
                     D-isomer-specific 2-hydroxyacid dehydrogenases related
                     repressor; cd05299"
                     /db_xref="CDD:240624"
     Site            order(86,89..90,255,304,307)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240624"
     Site            order(89,117,169..170,172..174,192..196,225..227,229,232,
                     253..255,279..280,304,306..307)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240624"
     CDS             1..429
                     /gene="CTBP1"
                     /gene_synonym="BARS; HADDTS"
                     /coded_by="NM_001377193.1:531..1820"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS43203.1"
                     /db_xref="GeneID:1487"
                     /db_xref="HGNC:HGNC:2494"
                     /db_xref="MIM:602618"
ORIGIN      
        1 msgvrppimn gplhprplva lldgrdctve mpilkdvatv afcdaqstqe ihekvlneav
       61 galmyhtitl tredlekfka lriivrigsg fdnidiksag dlgiavcnvp aasveetads
      121 tlchilnlyr ratwlhqalr egtrvqsveq irevasgaar irgetlgiig lgrvgqaval
      181 rakafgfnvl fydpylsdgv eralglqrvs tlqdllfhsd cvtlhcglne hnhhlindft
      241 vkqmrqgafl vntargglvd ekalaqalke grirgaaldv hesepfsfsq gplkdapnli
      301 ctphaawyse qasiemreea areirraitg ripdslkncv nkdhltaath wasmdpavvh
      361 pelngaayry ppgvvgvapt gipaavegiv psamslshgl ppvahpphap spgqtvkpea
      421 drdhasdql
//
LOCUS       NP_001258949             637 aa            linear   PRI 21-NOV-2025
DEFINITION  neurexin 3 isoform 4 precursor [Homo sapiens].
ACCESSION   NP_001258949
VERSION     NP_001258949.1
DBSOURCE    REFSEQ: accession NM_001272020.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Gulec,G., Cosan,D.T., Sahin,F.M., Calis,I.U., Sonkurt,M.D.,
            Kosger,F. and Essizoglu,A.
  TITLE     Association of Nicotine Use Disorder with Neurexin 3 Gene
            Polymorphisms
  JOURNAL   Turk Psikiyatri Derg 32 (3), 160-166 (2021)
   PUBMED   34647286
  REMARK    GeneRIF: Association of Nicotine Use Disorder with Neurexin 3 Gene
            Polymorphisms.', trans 'Nikotin Kullanim Bozuklugunun Neurexin 3
            Gen Polimorfizmi ile Iliskisi.
REFERENCE   3  (residues 1 to 637)
  AUTHORS   Hishimoto,A., Liu,Q.R., Drgon,T., Pletnikova,O., Walther,D.,
            Zhu,X.G., Troncoso,J.C. and Uhl,G.R.
  TITLE     Neurexin 3 polymorphisms are associated with alcohol dependence and
            altered expression of specific isoforms
  JOURNAL   Hum Mol Genet 16 (23), 2880-2891 (2007)
   PUBMED   17804423
  REMARK    GeneRIF: details of NRXN3's gene structure and variants, and
            association of NRXN3 SNPs with alcohol dependence
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 637)
  AUTHORS   Occhi,G., Rampazzo,A., Beffagna,G. and Antonio Danieli,G.
  TITLE     Identification and characterization of heart-specific splicing of
            human neurexin 3 mRNA (NRXN3)
  JOURNAL   Biochem Biophys Res Commun 298 (1), 151-155 (2002)
   PUBMED   12379233
  REMARK    GeneRIF: Identification and characterization of heart-specific
            splicing of neurexin 3 mRNA
REFERENCE   5  (residues 1 to 637)
  AUTHORS   Tabuchi,K. and Sudhof,T.C.
  TITLE     Structure and evolution of neurexin genes: insight into the
            mechanism of alternative splicing
  JOURNAL   Genomics 79 (6), 849-859 (2002)
   PUBMED   12036300
REFERENCE   6  (residues 1 to 637)
  AUTHORS   Rowen,L., Young,J., Birditt,B., Kaur,A., Madan,A., Philipps,D.L.,
            Qin,S., Minx,P., Wilson,R.K., Hood,L. and Graveley,B.R.
  TITLE     Analysis of the human neurexin genes: alternative splicing and the
            generation of protein diversity
  JOURNAL   Genomics 79 (4), 587-597 (2002)
   PUBMED   11944992
REFERENCE   7  (residues 1 to 637)
  AUTHORS   Missler,M., Hammer,R.E. and Sudhof,T.C.
  TITLE     Neurexophilin binding to alpha-neurexins. A single LNS domain
            functions as an independently folding ligand-binding unit
  JOURNAL   J Biol Chem 273 (52), 34716-34723 (1998)
   PUBMED   9856994
  REMARK    GeneRIF: N-terminal sequencing of rat neurexin III alpha provides
            evidence for signal peptide
REFERENCE   8  (residues 1 to 637)
  AUTHORS   Missler,M. and Sudhof,T.C.
  TITLE     Neurexins: three genes and 1001 products
  JOURNAL   Trends Genet 14 (1), 20-26 (1998)
   PUBMED   9448462
  REMARK    Review article
REFERENCE   9  (residues 1 to 637)
  AUTHORS   Ichtchenko,K., Nguyen,T. and Sudhof,T.C.
  TITLE     Structures, alternative splicing, and neurexin binding of multiple
            neuroligins
  JOURNAL   J Biol Chem 271 (5), 2676-2682 (1996)
   PUBMED   8576240
REFERENCE   10 (residues 1 to 637)
  AUTHORS   Ushkaryov,Y.A., Hata,Y., Ichtchenko,K., Moomaw,C., Afendis,S.,
            Slaughter,C.A. and Sudhof,T.C.
  TITLE     Conserved domain structure of beta-neurexins. Unusual cleaved
            signal sequences in receptor-like neuronal cell-surface proteins
  JOURNAL   J Biol Chem 269 (16), 11987-11992 (1994)
   PUBMED   8163501
  REMARK    GeneRIF: N-terminal sequencing of cow neurexin III beta provides
            evidence for signal peptide
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK056530.1, BC150194.1 and
            AF123462.1.
            
            Summary: This gene encodes a member of a family of proteins that
            function in the nervous system as receptors and cell adhesion
            molecules. Extensive alternative splicing and the use of
            alternative promoters results in multiple transcript variants and
            protein isoforms for this gene, but the full-length nature of many
            of these variants has not been determined. Transcripts that
            initiate from an upstream promoter encode alpha isoforms, which
            contain epidermal growth factor-like (EGF-like) sequences and
            laminin G domains. Transcripts initiating from the downstream
            promoter encode beta isoforms, which lack EGF-like sequences.
            Genetic variation at this locus has been associated with a range of
            behavioral phenotypes, including alcohol dependence and autism
            spectrum disorder. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            contains multiple differences in the coding region, including the
            lack of multiple 5' exons, compared to variant 1. It initiates
            translation at an alternate start codon. The encoded isoform (4) is
            shorter and has a distinct N-terminus, compared to isoform 1. This
            variant encodes a beta isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.549912.1,
                                           SRR7410570.549957.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3-q31.1"
     Protein         1..637
                     /product="neurexin 3 isoform 4 precursor"
                     /note="neurexin III; neurexin-3-alpha"
                     /calculated_mol_wt=65102
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4221
     mat_peptide     36..637
                     /product="neurexin 3 isoform 4"
                     /calculated_mol_wt=65102
     Region          86..235
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Region          563..619
                     /region_name="Syndecan"
                     /note="Syndecan domain; pfam01034"
                     /db_xref="CDD:460035"
     Region          583..601
                     /region_name="4.1m"
                     /note="putative band 4.1 homologues' binding motif;
                     smart00294"
                     /db_xref="CDD:128590"
     CDS             1..637
                     /gene="NRXN3"
                     /gene_synonym="C14orf60"
                     /coded_by="NM_001272020.2:913..2826"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS61515.1"
                     /db_xref="GeneID:9369"
                     /db_xref="HGNC:HGNC:8010"
                     /db_xref="MIM:600567"
ORIGIN      
        1 mhlriharrs pprrpawtlg iwflfwgciv ssvwsssnva sssstssspg shsqhehhfh
       61 gskhhsvpis iyrspvslrg ghagatyifg ksgglilytw pandrpstrs drlavgfstt
      121 vkdgilvrid sapglgdflq lhieqgkigv vfnigtvdis ikeertpvnd gkyhvvrftr
      181 nggnatlqvd nwpvnehypt grqltifntq aqiaiggkdk grlfqgqlsg lyydglkvln
      241 maaennpnik ingsvrlvge vpsilgttqt tsmppemstt vmettttmat tttrknrsta
      301 siqptsddlv ssaecssdde dfvecepstg gelvipllve dplatppiat rapsitlppt
      361 frplltiiet tkdslsmtse aglpclsdqg sdgcdddglv isgygsgetf dsnlpptdde
      421 dfyttfslvt dkslstsife ggykahapkw eskdfrpnkv setsrtttts lspelirfta
      481 ssssgmvpkl pagkmnnrdl kpqpdivllp lptayeldst klksplitsp mfrnvptanp
      541 tepgirrvpg aseviresss ttgmvvgiva aaalcilill yamykyrnrd egsyqvdetr
      601 nyisnsaqsn gtlmkekqqs sksghkkqkn kdreyyv
//
LOCUS       NP_001364177             389 aa            linear   PRI 21-NOV-2025
DEFINITION  pleckstrin homology domain-containing family A member 1 isoform 6
            [Homo sapiens].
ACCESSION   NP_001364177
VERSION     NP_001364177.1
DBSOURCE    REFSEQ: accession NM_001377248.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Huang,Q. and Xiang,Y.
  TITLE     Polymorphisms in Selected Genes and Their Association with
            Age-Related Macular Degeneration in a Chinese Population
  JOURNAL   Med Sci Monit 24, 1693-1700 (2018)
   PUBMED   29565837
  REMARK    GeneRIF: investigated the association of PLEKHA1 958A/G,
            polymorphisms with Age-Related Macular Degeneration (AMD) risk.
            PLEKHA1 958A/G polymorphism was associated with a decreased AMD
            risk (additive model: aOR=0.722, 95% CI=0.450-0.979, P=0.019;
            allele model: aOR=0.883, 95% CI=0.736-0.992, P=0.014)
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Kortvely,E. and Ueffing,M.
  TITLE     Gene Structure of the 10q26 Locus: A Clue to Cracking the
            ARMS2/HTRA1 Riddle?
  JOURNAL   Adv Exp Med Biol 854, 23-29 (2016)
   PUBMED   26427389
  REMARK    GeneRIF: Studies indicate that the high-risk allele of the 10q26
            locus encompasses three genes, PLEKHA1, ARMS2, and HTRA1 with high
            linkage disequilibrium.
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Gupta,D., Gupta,V., Singh,V., Chawla,S., Parveen,F., Agrawal,S. and
            Phadke,S.R.
  TITLE     Study of Polymorphisms in CX3CR1, PLEKHA1 and VEGF genes as risk
            factors for age-related macular degeneration in Indian patients
  JOURNAL   Arch Med Res 45 (6), 489-494 (2014)
   PUBMED   25050486
  REMARK    GeneRIF: CX3CR1 (T280M and V249I) and PLEKHA1 (A320T) polymorphisms
            were not found to be associated with age-related macular
            degeneration in an Indian population.
REFERENCE   5  (residues 1 to 389)
  AUTHORS   Hogan,A., Yakubchyk,Y., Chabot,J., Obagi,C., Daher,E., Maekawa,K.
            and Gee,S.H.
  TITLE     The phosphoinositol 3,4-bisphosphate-binding protein TAPP1
            interacts with syntrophins and regulates actin cytoskeletal
            organization
  JOURNAL   J Biol Chem 279 (51), 53717-53724 (2004)
   PUBMED   15485858
  REMARK    GeneRIF: syntrophins regulate the localization of TAPP1, which may
            be important for remodeling the actin cytoskeleton in response to
            growth factor stimulation
REFERENCE   6  (residues 1 to 389)
  AUTHORS   Kimber,W.A., Deak,M., Prescott,A.R. and Alessi,D.R.
  TITLE     Interaction of the protein tyrosine phosphatase PTPL1 with the
            PtdIns(3,4)P2-binding adaptor protein TAPP1
  JOURNAL   Biochem J 376 (Pt 2), 525-535 (2003)
   PUBMED   14516276
  REMARK    GeneRIF: TAPP1 binds to protein tyrosine phosphatase PTPL1.
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Marshall,A.J., Krahn,A.K., Ma,K., Duronio,V. and Hou,S.
  TITLE     TAPP1 and TAPP2 are targets of phosphatidylinositol 3-kinase
            signaling in B cells: sustained plasma membrane recruitment
            triggered by the B-cell antigen receptor
  JOURNAL   Mol Cell Biol 22 (15), 5479-5491 (2002)
   PUBMED   12101241
REFERENCE   8  (residues 1 to 389)
  AUTHORS   Kimber,W.A., Trinkle-Mulcahy,L., Cheung,P.C., Deak,M.,
            Marsden,L.J., Kieloch,A., Watt,S., Javier,R.T., Gray,A.,
            Downes,C.P., Lucocq,J.M. and Alessi,D.R.
  TITLE     Evidence that the tandem-pleckstrin-homology-domain-containing
            protein TAPP1 interacts with Ptd(3,4)P2 and the
            multi-PDZ-domain-containing protein MUPP1 in vivo
  JOURNAL   Biochem J 361 (Pt 3), 525-536 (2002)
   PUBMED   11802782
REFERENCE   9  (residues 1 to 389)
  AUTHORS   Thomas,C.C., Dowler,S., Deak,M., Alessi,D.R. and van Aalten,D.M.
  TITLE     Crystal structure of the phosphatidylinositol
            3,4-bisphosphate-binding pleckstrin homology (PH) domain of tandem
            PH-domain-containing protein 1 (TAPP1): molecular basis of lipid
            specificity
  JOURNAL   Biochem J 358 (Pt 2), 287-294 (2001)
   PUBMED   11513726
REFERENCE   10 (residues 1 to 389)
  AUTHORS   Dowler,S., Currie,R.A., Campbell,D.G., Deak,M., Kular,G.,
            Downes,C.P. and Alessi,D.R.
  TITLE     Identification of pleckstrin-homology-domain-containing proteins
            with novel phosphoinositide-binding specificities
  JOURNAL   Biochem J 351 (Pt 1), 19-31 (2000)
   PUBMED   11001876
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX664700.3 and BX842242.1.
            
            Summary: This gene encodes a pleckstrin homology domain-containing
            adapter protein. The encoded protein is localized to the plasma
            membrane where it specifically binds phosphatidylinositol
            3,4-bisphosphate. This protein may be involved in the formation of
            signaling complexes in the plasma membrane. Polymorphisms in this
            gene are associated with age-related macular degeneration.
            Alternate splicing results in multiple transcript variants. A
            pseudogene of this gene is found on chromosome 5.[provided by
            RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.196806.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..389
                     /product="pleckstrin homology domain-containing family A
                     member 1 isoform 6"
                     /note="tandem PH domain-containing protein 1; pleckstrin
                     homology domain containing, family A (phosphoinositide
                     binding specific) member 1"
                     /calculated_mol_wt=44233
     Region          1..117
                     /region_name="PH1_TAPP1_2"
                     /note="Tandem PH-domain-containing proteins 1 and 2
                     Pleckstrin homology (PH) domain, N-terminal repeat;
                     cd13270"
                     /db_xref="CDD:270089"
     Region          185..298
                     /region_name="PH2_TAPP1_2"
                     /note="Tandem PH-domain-containing proteins 1 and 2
                     Pleckstrin homology (PH) domain, C-terminal repeat;
                     cd13271"
                     /db_xref="CDD:270090"
     Site            order(200,202..203,211,222,232..233,265)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270090"
     CDS             1..389
                     /gene="PLEKHA1"
                     /gene_synonym="TAPP1"
                     /coded_by="NM_001377248.1:190..1359"
                     /note="isoform 6 is encoded by transcript variant 20"
                     /db_xref="GeneID:59338"
                     /db_xref="HGNC:HGNC:14335"
                     /db_xref="MIM:607772"
ORIGIN      
        1 mpyvdrqnri cgfldieene nsgkflrryf ildtredsfv wymdnpqnlp sgssrvgaik
       61 ltyiskvsda tklrpkaefc fvmnagmrky flqandqqdl vewvnvlnka ikitvpkqsd
      121 sqpnsdnlsr hgecgkkqvs yrtdivggvp iitptqkeev necgesidrn nlkrsqshlp
      181 yftpkppqds avikagycvk qgavmknwkr ryfqldenti gyfkseleke plrviplkev
      241 hkvqeckqsd immrdnlfei vttsrtfyvq adspeemhsw ikavsgaiva qrgpgrsass
      301 lctvfqmrqa rrlsnpciqr sippvlqnpn tlsvlptqpp pphipqplaa tlwsqplpwr
      361 sedftsllpr ssqgtsrsrl slqenqlpk
//
LOCUS       NP_001382228            2462 aa            linear   PRI 21-NOV-2025
DEFINITION  myomegalin isoform 18 [Homo sapiens].
ACCESSION   NP_001382228
VERSION     NP_001382228.1
DBSOURCE    REFSEQ: accession NM_001395299.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2462)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2462)
  AUTHORS   Pan,R., Dai,J., Liang,W., Wang,H., Ye,L., Ye,S., Lin,Z., Huang,S.,
            Xiong,Y., Zhang,L., Lu,L., Wang,O., Shen,X., Liao,W. and Lu,X.
  TITLE     PDE4DIP contributes to colorectal cancer growth and chemoresistance
            through modulation of the NF1/RAS signaling axis
  JOURNAL   Cell Death Dis 14 (6), 373 (2023)
   PUBMED   37355626
  REMARK    GeneRIF: PDE4DIP contributes to colorectal cancer growth and
            chemoresistance through modulation of the NF1/RAS signaling axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2462)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   4  (residues 1 to 2462)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 2462)
  AUTHORS   Abou Ziki,M.D., Bhat,N., Neogi,A., Driscoll,T.P., Ugwu,N., Liu,Y.,
            Smith,E., Abboud,J.M., Chouairi,S., Schwartz,M.A., Akar,J.G. and
            Mani,A.
  TITLE     Epistatic interaction of PDE4DIP and DES mutations in familial
            atrial fibrillation with slow conduction
  JOURNAL   Hum Mutat 42 (10), 1279-1293 (2021)
   PUBMED   34289528
  REMARK    GeneRIF: Epistatic interaction of PDE4DIP and DES mutations in
            familial atrial fibrillation with slow conduction.
REFERENCE   6  (residues 1 to 2462)
  AUTHORS   Shimada,H., Kuboshima,M., Shiratori,T., Nabeya,Y., Takeuchi,A.,
            Takagi,H., Nomura,F., Takiguchi,M., Ochiai,T. and Hiwasa,T.
  TITLE     Serum anti-myomegalin antibodies in patients with esophageal
            squamous cell carcinoma
  JOURNAL   Int J Oncol 30 (1), 97-103 (2007)
   PUBMED   17143517
  REMARK    GeneRIF: MMGL-antibody is significantly with a favorable prognosis.
            Consequently, MMGL-anatibodies may be a useful tumor marker to
            diagnose and establish a prognosis in patients with esophageal
            squamous cell carcinoma.
REFERENCE   7  (residues 1 to 2462)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 2462)
  AUTHORS   Soejima,H., Kawamoto,S., Akai,J., Miyoshi,O., Arai,Y., Morohka,T.,
            Matsuo,S., Niikawa,N., Kimura,A., Okubo,K. and Mukai,T.
  TITLE     Isolation of novel heart-specific genes using the BodyMap database
  JOURNAL   Genomics 74 (1), 115-120 (2001)
   PUBMED   11374908
REFERENCE   9  (residues 1 to 2462)
  AUTHORS   Verde,I., Pahlke,G., Salanova,M., Zhang,G., Wang,S., Coletti,D.,
            Onuffer,J., Jin,S.L. and Conti,M.
  TITLE     Myomegalin is a novel protein of the golgi/centrosome that
            interacts with a cyclic nucleotide phosphodiesterase
  JOURNAL   J Biol Chem 276 (14), 11189-11198 (2001)
   PUBMED   11134006
REFERENCE   10 (residues 1 to 2462)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC239802.3 and AC239804.2.
            
            Summary: The protein encoded by this gene serves to anchor
            phosphodiesterase 4D to the Golgi/centrosome region of the cell.
            Defects in this gene may be a cause of myeloproliferative disorder
            (MBD) associated with eosinophilia. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..2462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     Protein         1..2462
                     /product="myomegalin isoform 18"
                     /note="myomegalin; cardiomyopathy-associated protein 2"
                     /calculated_mol_wt=276634
     Region          1..376
                     /region_name="SMYLE_N"
                     /note="Short myomegalin-like EB1 binding proteins,
                     N-terminal domain; pfam18615"
                     /db_xref="CDD:465822"
     Region          403..1201
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1714..1783
                     /region_name="Olduvai"
                     /note="Olduvai domain; pfam06758"
                     /db_xref="CDD:429104"
     Region          <1941..>2118
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..2462
                     /gene="PDE4DIP"
                     /gene_synonym="CMYA2; MMGL"
                     /coded_by="NM_001395299.1:408..7796"
                     /note="isoform 18 is encoded by transcript variant 18"
                     /db_xref="GeneID:9659"
                     /db_xref="HGNC:HGNC:15580"
                     /db_xref="MIM:608117"
ORIGIN      
        1 mkeicricar elcgnqrrwi fhtasklnlq vllshvlgkd vprdgkaefa cskcafmldr
       61 iyrfdtviar iealsierlq klllekdrlk fciasmyrkn nddsgaeika gngtvdmsvl
      121 pdarysallq edfaysgfec wvenedqiqe phschgsegp gnrprrcrgc aalrvadsdy
      181 eaickvprkv arsiscgpss rwstsictee palsevgppd lastkvppdg esmeeetpgs
      241 svesldasvq asppqqkdee tersakelgk cdccsddqap qhgcnhklel alsmikgldy
      301 kpiqsprgsr lpipvksslp gakpgpsmtd gvssgflnrs lkplyktpvs yplelsdlqe
      361 lwddlcedyl plrvqpmtee llkqqklnsh ettitqqsvs dshlaelqek iqqteatnki
      421 lqeklnemsy elkcaqessq kqdgtiqnlk etlksreret eelyqviegq ndtmaklrem
      481 lhqsqlgqlh ssegtspaqq qvalldlqsa lfcsqleiqk lqrvvrqker qladakqcvq
      541 fveaaahese qqkeaswkhn qelrkalqql qeelqnksqq lraweaekyn eirtqeqniq
      601 hlnhslshke qllqefrell qyrdnsdktl eanemllekl rqrihdkava leraidekfs
      661 aleekekelr qlrlavrerd hdlerlrdvl ssneatmqsm esllrakgle veqlsttcqn
      721 lqwlkeemet kfsrwqkeqe siiqqlqtsl hdrnkevedl satllcklgp gqseiaeelc
      781 qrlqrkerml qdllsdrnkq vlehemeiqg llqsvstreq esqaaaeklv qalmernsel
      841 qalrqylggr dslmsqapis nqqaevtptg rlgkqtdqgs mqipsrddst sltakedvsi
      901 prstlgdldt vaglekelsn akeelelmak keresqmels alqsmmavqe eelqvqaadm
      961 esltrniqik edlikdlqmq lvdpedipam erltqevlll rekvasvesq gqeisgnrrq
     1021 qlllmleglv dersrlneal qaerqlyssl vkfhahpess erdrtlqvel egaqvlrsrl
     1081 eevlgrsler lnrletlaai ggaaagddte dtsteftdsi eeeaahhshq qlvkvaleks
     1141 latvetqnps fsppspmggd snrclqeeml hlraefhqhl eekrkaeeel kelkaqieea
     1201 gfssvshirn tmlslclena elkeqmgeam sdgweieedk ekgevmvetv vtkeglsess
     1261 lqaefrklqg klknahniin llkeqlvlss kegnskltpe llvhltstie rintelvgsp
     1321 gkhqhqeegn vtvrpfprpq sldlgatftv dahqldnqsq prdpgpqsaf slpgstqhlr
     1381 sqlsqckqry qdlqekllls eatvfaqane lekyrvmlse slvkqdskqi qvdlqdlgye
     1441 tcgrseneae reettspece ehnslkemvl meglcseqgr rgstlassse rkplenqlgk
     1501 qeefrvygks enilvlrkdi kdlkaqlqna nkviqnlksr vrslsvtsdy ssslerprkl
     1561 ravgtlegss phsvpdedeg wlsdgtgafy spglqakkdl esliqrvsql eaqlpkngle
     1621 eklaeelrsa swpgkydsli qdqarelsyl rqkiregrgi cylitrhakd tvksfedllr
     1681 sndidyylgq sfreqlaqgs qlterltskl stkdhksekd qagleplalr lsrelqekek
     1741 vievlqakld arsltpsssh alsdshrsps stsflsdele acsdmdivse ythyeekkas
     1801 pshsdsihhs shsavlsskp sstsasqgak aesnsnpisl ptpqntpkea nqahsgastv
     1861 ppastatlls ndleadssyy lnsaqphspp rgtielgril epgylgssgk wdvmrpqkgs
     1921 vsgdlssgss vyqlnskptg adlleehlge irnlrqrlee sicindrlre qlehrltsta
     1981 rgrgstsnfy sqglesipql cnenrvlred nrrlqaqlsh vsrehsqete slreallssr
     2041 shlqelekel ehqkverqql ledlrekqqe vlhfreerls lqendsrlqh klvllqqqce
     2101 ekqqlfeslq selqiyealy gnskkglkay sldachqipl ssdlshlvae vralrgqleq
     2161 siqgnnclrl qlqqqlesga gkaslspssi nqnfpastdp gnkqlllqds avsppvrdvg
     2221 mnspalvfps sasstpgset piinranglg ldtspvmktp pklegdatdg sfankhgrhv
     2281 ighiddysal rqqiaegkll vkkivslvrs acsfpgleaq gtevlgskgi helrsstsal
     2341 hhaleesasl ltmfwraalp sthipvlpgk vgesterell elrtkvskqe rllqsttehl
     2401 knanqqkesm eqfivsqltr thdvlkkart nleepckkrs hqkslkqqer wacppfvqlp
     2461 ic
//
LOCUS       NP_065913                771 aa            linear   PRI 21-NOV-2025
DEFINITION  leucine-rich repeat and fibronectin type III domain-containing
            protein 1 precursor [Homo sapiens].
ACCESSION   NP_065913 XP_290842 XP_945666
VERSION     NP_065913.1
DBSOURCE    REFSEQ: accession NM_020862.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 771)
  AUTHORS   Ruan,B., Feng,X., Chen,X., Dong,Z., Wang,Q., Xu,K., Tian,J.,
            Liu,J., Chen,Z., Shi,W., Wang,M., Qian,L. and Ding,Q.
  TITLE     Identification of a Set of Genes Improving Survival Prediction in
            Kidney Renal Clear Cell Carcinoma through Integrative Reanalysis of
            Transcriptomic Data
  JOURNAL   Dis Markers 2020, 8824717 (2020)
   PUBMED   33110456
  REMARK    GeneRIF: Identification of a Set of Genes Improving Survival
            Prediction in Kidney Renal Clear Cell Carcinoma through Integrative
            Reanalysis of Transcriptomic Data.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 771)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   3  (residues 1 to 771)
  AUTHORS   Morimura,N., Inoue,T., Katayama,K. and Aruga,J.
  TITLE     Comparative analysis of structure, expression and PSD95-binding
            capacity of Lrfn, a novel family of neuronal transmembrane proteins
  JOURNAL   Gene 380 (2), 72-83 (2006)
   PUBMED   16828986
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011445.6.
            
            On or before Jun 29, 2007 this sequence version replaced
            XP_290842.2, XP_945666.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853566.14184.1,
                                           SRR14038192.3799666.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000248668.5/ ENSP00000248668.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..771
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..771
                     /product="leucine-rich repeat and fibronectin type III
                     domain-containing protein 1 precursor"
                     /note="leucine-rich repeat and fibronectin type III
                     domain-containing protein 1; synaptic adhesion-like
                     molecule 2; CTC-246B18.8"
                     /calculated_mol_wt=79230
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3107
     mat_peptide     32..771
                     /product="Leucine-rich repeat and fibronectin type III
                     domain-containing protein 1. /id=PRO_0000334145"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P244.2)"
                     /calculated_mol_wt=79230
     Region          66..87
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P244.2)"
     Region          67..90
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <69..326
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Site            87
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9P244.2)"
     Region          90..111
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P244.2)"
     Region          91..114
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          114..135
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P244.2)"
     Region          115..138
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          138..159
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P244.2)"
     Region          139..163
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          163..184
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P244.2)"
     Region          164..187
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          187..208
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P244.2)"
     Region          188..211
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          211..232
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P244.2)"
     Region          212..230
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          299..387
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          317..321
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          330..334
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            343
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9P244.2)"
     Region          353..357
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          367..372
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          380..383
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          397..422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P244.2)"
     Region          426..500
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            537..557
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P244.2)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q9P244.2)"
     Region          654..743
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P244.2)"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P244.2)"
     Region          768..771
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P244.2)"
     CDS             1..771
                     /gene="LRFN1"
                     /gene_synonym="SALM2"
                     /coded_by="NM_020862.2:197..2512"
                     /db_xref="CCDS:CCDS46071.1"
                     /db_xref="GeneID:57622"
                     /db_xref="HGNC:HGNC:29290"
                     /db_xref="MIM:612807"
ORIGIN      
        1 mapgpfssal lspppaalpf llllwagasr gqpcpgrcic qnvaptltml caktgllfvp
       61 paidrrvvel rltdnfiaav rrrdfanmts lvhltlsrnt igqvaagafa dlralralhl
      121 dsnrlaevrg dqlrglgnlr hlilgnnqir rvesaafdaf lstvedldls ynnlealpwe
      181 avgqmvnlnt ltldhnlidh iaegtfvqlh klvrldmtsn rlhklppdgl flrsqgtgpk
      241 pptpltvsfg gnplhcncel lwlrrltred dletcatpeh ltdryfwsip eeeflceppl
      301 itrqaggral vvegqavslr cravgdpepv vhwvapdgrl lgnssrtrvr gdgtldvtit
      361 tlrdsgtftc iasnaageat apvevcvvpl plmapppaap ppltepgssd iatpgrpgan
      421 dsaaerrlva aeltsnsvli rwpaqrpvpg irmyqvqyns svddslvyrm ipstsqtflv
      481 ndlaagrayd lcvlavyddg atalpatrvv gcvqfttagd papcrplrah flggtmiiai
      541 ggvivasvlv fivllmiryk vygdgdsrrv kgsrslprvs hvcsqtngag tgaaqapalp
      601 aqdhyealre vesqaapava veakameaet asaepevvlg rslggsatsl cllpseetsg
      661 eesraavgpr rsrsgalepp tsapptlalv pggaaarprp qqrysfdgdy galfqshsyp
      721 rrarrtkrhr stphldgagg gaagedgdlg lgsaraclaf tstewmlest v
//
LOCUS       NP_001308764             545 aa            linear   PRI 21-NOV-2025
DEFINITION  cleavage and polyadenylation specificity factor subunit 3 isoform c
            [Homo sapiens].
ACCESSION   NP_001308764
VERSION     NP_001308764.1
DBSOURCE    REFSEQ: accession NM_001321835.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Zhang,Y., Liu,D., Guo,D., Lin,W., Lu,W., Hu,L., Chen,S. and Chen,C.
  TITLE     CPSF3 regulates alternative polyadenylation of CNIH2 to promote
            esophageal squamous cell carcinoma progression
  JOURNAL   Cancer Lett 593, 216925 (2024)
   PUBMED   38718887
  REMARK    GeneRIF: CPSF3 regulates alternative polyadenylation of CNIH2 to
            promote esophageal squamous cell carcinoma progression.
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Alahmari,A.A., Chaubey,A.H., Jonnakuti,V.S., Tisdale,A.A.,
            Schwarz,C.D., Cornwell,A.C., Maraszek,K.E., Paterson,E.J., Kim,M.,
            Venkat,S., Gomez,E.C., Wang,J., Gurova,K.V., Yalamanchili,H.K. and
            Feigin,M.E.
  TITLE     CPSF3 inhibition blocks pancreatic cancer cell proliferation
            through disruption of core histone mRNA processing
  JOURNAL   RNA 30 (3), 281-297 (2024)
   PUBMED   38191171
  REMARK    GeneRIF: CPSF3 inhibition blocks pancreatic cancer cell
            proliferation through disruption of core histone mRNA processing.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Shen,P., Ye,K., Xiang,H., Zhang,Z., He,Q., Zhang,X., Cai,M.C.,
            Chen,J., Sun,Y., Lin,L., Qi,C., Zhang,M., Cheung,L.W.T., Shi,T.,
            Yin,X., Li,Y., Di,W., Zang,R., Tan,L. and Zhuang,G.
  TITLE     Therapeutic targeting of CPSF3-dependent transcriptional
            termination in ovarian cancer
  JOURNAL   Sci Adv 9 (47), eadj0123 (2023)
   PUBMED   37992178
  REMARK    GeneRIF: Therapeutic targeting of CPSF3-dependent transcriptional
            termination in ovarian cancer.
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Huang,J., Liu,X., Sun,Y., Li,Z., Lin,M.H., Hamilton,K.,
            Mandel,C.R., Sandmeir,F., Conti,E., Oyala,P.H. and Tong,L.
  TITLE     An examination of the metal ion content in the active sites of
            human endonucleases CPSF73 and INTS11
  JOURNAL   J Biol Chem 299 (4), 103047 (2023)
   PUBMED   36822327
  REMARK    GeneRIF: An examination of the metal ion content in the active
            sites of human endonucleases CPSF73 and INTS11.
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   6  (residues 1 to 545)
  AUTHORS   McCracken,S., Fong,N., Yankulov,K., Ballantyne,S., Pan,G.,
            Greenblatt,J., Patterson,S.D., Wickens,M. and Bentley,D.L.
  TITLE     The C-terminal domain of RNA polymerase II couples mRNA processing
            to transcription
  JOURNAL   Nature 385 (6614), 357-361 (1997)
   PUBMED   9002523
REFERENCE   7  (residues 1 to 545)
  AUTHORS   Jenny,A., Minvielle-Sebastia,L., Preker,P.J. and Keller,W.
  TITLE     Sequence similarity between the 73-kilodalton protein of mammalian
            CPSF and a subunit of yeast polyadenylation factor I
  JOURNAL   Science 274 (5292), 1514-1517 (1996)
   PUBMED   8929409
REFERENCE   8  (residues 1 to 545)
  AUTHORS   Murthy,K.G. and Manley,J.L.
  TITLE     The 160-kD subunit of human cleavage-polyadenylation specificity
            factor coordinates pre-mRNA 3'-end formation
  JOURNAL   Genes Dev 9 (21), 2672-2683 (1995)
   PUBMED   7590244
REFERENCE   9  (residues 1 to 545)
  AUTHORS   Jenny,A., Hauri,H.P. and Keller,W.
  TITLE     Characterization of cleavage and polyadenylation specificity factor
            and cloning of its 100-kilodalton subunit
  JOURNAL   Mol Cell Biol 14 (12), 8183-8190 (1994)
   PUBMED   7969155
REFERENCE   10 (residues 1 to 545)
  AUTHORS   Thuresson,A.C., Astrom,J., Astrom,A., Gronvik,K.O. and Virtanen,A.
  TITLE     Multiple forms of poly(A) polymerases in human cells
  JOURNAL   Proc Natl Acad Sci U S A 91 (3), 979-983 (1994)
   PUBMED   8302877
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC420903.1, DA478774.1,
            BC014106.1 and AA635764.1.
            
            Summary: This gene encodes a member of the metallo-beta-lactamase
            family. The encoded protein is a 73kDa subunit of the cleavage and
            polyadenylation specificity factor and functions as an endonuclease
            that recognizes the pre-mRNA 3'-cleavage site AAUAAA prior to
            polyadenylation. It also cleaves after the pre-mRNA sequence ACCCA
            during histone 3'-end pre-mRNA processing. [provided by RefSeq, Oct
            2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.4128009.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.1"
     Protein         1..545
                     /product="cleavage and polyadenylation specificity factor
                     subunit 3 isoform c"
                     /note="cleavage and polyadenylation specificity factor
                     subunit 3; mRNA 3'-end-processing endonuclease CPSF-73;
                     cleavage and polyadenylation specific factor 3, 73kDa"
                     /calculated_mol_wt=61667
     Region          <18..317
                     /region_name="COG1782"
                     /note="Predicted metal-dependent RNase, contains
                     metallo-beta-lactamase and KH domains [General function
                     prediction only]"
                     /db_xref="CDD:441388"
     Region          340..543
                     /region_name="CPSF73-100_C"
                     /note="Pre-mRNA 3'-end-processing endonuclease
                     polyadenylation factor C-term; pfam11718"
                     /db_xref="CDD:463330"
     CDS             1..545
                     /gene="CPSF3"
                     /gene_synonym="CPSF-73; CPSF73; NEDMHS; NEDMHSN"
                     /coded_by="NM_001321835.2:410..2047"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="GeneID:51692"
                     /db_xref="HGNC:HGNC:2326"
                     /db_xref="MIM:606029"
ORIGIN      
        1 mpqklfidgf flimsklghv lgaamfmiei agvkllytgd fsrqedrhlm aaeipnikpd
       61 iliiestygt hihekreere arfcntvhdi vnrggrglip vfalgraqel llildeywqn
      121 hpelhdipiy yasslakkcm avyqtyvnam ndkirkqini nnpfvfkhis nlksmdhfdd
      181 igpsvvmasp gmmqsglsre lfeswctdkr ngviiagycv egtlakhims epeeittmsg
      241 qklplkmsvd yisfsahtdy qqtsefiral kpphvilvhg eqnemarlka alireyednd
      301 evhievhnpr nteavtlnfr geklakvmgf ladkkpeqgq rvsgilvkrn fnyhilspcd
      361 lsnytdlams tvkqtqaipy tgpfnllcyq lqkltgdvee leiqekpalk vfknitviqe
      421 pgmvvlewla npsndmyadt vttvilevqs npkirkgavq kvskklemhv yskrleimlq
      481 difgedcvsv kddsilsvtv dgktanlnle trtveceegs eddeslremv elaaqrlyea
      541 ltpvh
//
LOCUS       NP_001304160             314 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial carrier homolog 2 isoform 1x [Homo sapiens].
ACCESSION   NP_001304160
VERSION     NP_001304160.1
DBSOURCE    REFSEQ: accession NM_001317231.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Ulupinar,P., Caglayan,E., Rayaman,E., Nagata,K. and Turan,K.
  TITLE     The mitochondrial carrier homolog 2 is involved in down-regulation
            of influenza A virus replication
  JOURNAL   Mol Biol Rep 51 (1), 642 (2024)
   PUBMED   38727866
  REMARK    GeneRIF: The mitochondrial carrier homolog 2 is involved in
            down-regulation of influenza A virus replication.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Zheng,X. and Chu,B.
  TITLE     The biology of mitochondrial carrier homolog 2
  JOURNAL   Mitochondrion 75, 101837 (2024)
   PUBMED   38158152
  REMARK    GeneRIF: The biology of mitochondrial carrier homolog 2.
            Review article
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Goldman,A., Mullokandov,M., Zaltsman,Y., Regev,L., Levin-Zaidman,S.
            and Gross,A.
  TITLE     MTCH2 cooperates with MFN2 and lysophosphatidic acid synthesis to
            sustain mitochondrial fusion
  JOURNAL   EMBO Rep 25 (1), 45-67 (2024)
   PUBMED   38177900
  REMARK    GeneRIF: MTCH2 cooperates with MFN2 and lysophosphatidic acid
            synthesis to sustain mitochondrial fusion.
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Eswarappa,S.M., Potdar,A.A., Koch,W.J., Fan,Y., Vasu,K.,
            Lindner,D., Willard,B., Graham,L.M., DiCorleto,P.E. and Fox,P.L.
  TITLE     Programmed translational readthrough generates antiangiogenic
            VEGF-Ax
  JOURNAL   Cell 157 (7), 1605-1618 (2014)
   PUBMED   24949972
REFERENCE   6  (residues 1 to 314)
  AUTHORS   Renstrom,F., Payne,F., Nordstrom,A., Brito,E.C., Rolandsson,O.,
            Hallmans,G., Barroso,I., Nordstrom,P. and Franks,P.W.
  CONSRTM   GIANT Consortium
  TITLE     Replication and extension of genome-wide association study results
            for obesity in 4923 adults from northern Sweden
  JOURNAL   Hum Mol Genet 18 (8), 1489-1496 (2009)
   PUBMED   19164386
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 314)
  AUTHORS   Willer,C.J., Speliotes,E.K., Loos,R.J., Li,S., Lindgren,C.M.,
            Heid,I.M., Berndt,S.I., Elliott,A.L., Jackson,A.U., Lamina,C.,
            Lettre,G., Lim,N., Lyon,H.N., McCarroll,S.A., Papadakis,K., Qi,L.,
            Randall,J.C., Roccasecca,R.M., Sanna,S., Scheet,P., Weedon,M.N.,
            Wheeler,E., Zhao,J.H., Jacobs,L.C., Prokopenko,I., Soranzo,N.,
            Tanaka,T., Timpson,N.J., Almgren,P., Bennett,A., Bergman,R.N.,
            Bingham,S.A., Bonnycastle,L.L., Brown,M., Burtt,N.P., Chines,P.,
            Coin,L., Collins,F.S., Connell,J.M., Cooper,C., Smith,G.D.,
            Dennison,E.M., Deodhar,P., Elliott,P., Erdos,M.R., Estrada,K.,
            Evans,D.M., Gianniny,L., Gieger,C., Gillson,C.J., Guiducci,C.,
            Hackett,R., Hadley,D., Hall,A.S., Havulinna,A.S., Hebebrand,J.,
            Hofman,A., Isomaa,B., Jacobs,K.B., Johnson,T., Jousilahti,P.,
            Jovanovic,Z., Khaw,K.T., Kraft,P., Kuokkanen,M., Kuusisto,J.,
            Laitinen,J., Lakatta,E.G., Luan,J., Luben,R.N., Mangino,M.,
            McArdle,W.L., Meitinger,T., Mulas,A., Munroe,P.B., Narisu,N.,
            Ness,A.R., Northstone,K., O'Rahilly,S., Purmann,C., Rees,M.G.,
            Ridderstrale,M., Ring,S.M., Rivadeneira,F., Ruokonen,A.,
            Sandhu,M.S., Saramies,J., Scott,L.J., Scuteri,A., Silander,K.,
            Sims,M.A., Song,K., Stephens,J., Stevens,S., Stringham,H.M.,
            Tung,Y.C., Valle,T.T., Van Duijn,C.M., Vimaleswaran,K.S.,
            Vollenweider,P., Waeber,G., Wallace,C., Watanabe,R.M.,
            Waterworth,D.M., Watkins,N., Witteman,J.C., Zeggini,E., Zhai,G.,
            Zillikens,M.C., Altshuler,D., Caulfield,M.J., Chanock,S.J.,
            Farooqi,I.S., Ferrucci,L., Guralnik,J.M., Hattersley,A.T., Hu,F.B.,
            Jarvelin,M.R., Laakso,M., Mooser,V., Ong,K.K., Ouwehand,W.H.,
            Salomaa,V., Samani,N.J., Spector,T.D., Tuomi,T., Tuomilehto,J.,
            Uda,M., Uitterlinden,A.G., Wareham,N.J., Deloukas,P.,
            Frayling,T.M., Groop,L.C., Hayes,R.B., Hunter,D.J., Mohlke,K.L.,
            Peltonen,L., Schlessinger,D., Strachan,D.P., Wichmann,H.E.,
            McCarthy,M.I., Boehnke,M., Barroso,I., Abecasis,G.R. and
            Hirschhorn,J.N.
  CONSRTM   Wellcome Trust Case Control Consortium; Genetic Investigation of
            ANthropometric Traits Consortium
  TITLE     Six new loci associated with body mass index highlight a neuronal
            influence on body weight regulation
  JOURNAL   Nat Genet 41 (1), 25-34 (2009)
   PUBMED   19079261
  REMARK    GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 314)
  AUTHORS   Grinberg,M., Schwarz,M., Zaltsman,Y., Eini,T., Niv,H.,
            Pietrokovski,S. and Gross,A.
  TITLE     Mitochondrial carrier homolog 2 is a target of tBID in cells
            signaled to die by tumor necrosis factor alpha
  JOURNAL   Mol Cell Biol 25 (11), 4579-4590 (2005)
   PUBMED   15899861
  REMARK    GeneRIF: Mtch2 is a mitochondrial target of tBID and possibly
            participates in the mitochondrial apoptotic program.
REFERENCE   9  (residues 1 to 314)
  AUTHORS   Yerushalmi,G.M., Leibowitz-Amit,R., Shaharabany,M. and Tsarfaty,I.
  TITLE     Met-HGF/SF signal transduction induces mimp, a novel mitochondrial
            carrier homologue, which leads to mitochondrial depolarization
  JOURNAL   Neoplasia 4 (6), 510-522 (2002)
   PUBMED   12407445
REFERENCE   10 (residues 1 to 314)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK313032.1, AY380792.1 and
            AC104942.5.
            
            Summary: This gene encodes a member of the SLC25 family of
            nuclear-encoded transporters that are localized in the inner
            mitochondrial membrane. Members of this superfamily are involved in
            many metabolic pathways and cell functions. Genome-wide association
            studies in human have identified single-nucleotide polymorphisms in
            several loci associated with obesity. This gene is one such locus,
            which is highly expressed in white adipose tissue and adipocytes,
            and thought to play a regulatory role in adipocyte differentiation
            and biology. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. A recent study
            showed this gene to be an authentic stop codon readthrough target
            that can produce two isoforms from the same mRNA by use of
            alternative in-frame translation termination codons. [provided by
            RefSeq, Dec 2017].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes two isoforms, which result from the use of
            alternative in-frame translation termination codons. The shorter
            isoform (1) results from translation termination at the upstream
            UGA stop codon, while the longer isoform (1x) results from UGA stop
            codon readthrough to the downstream UAG termination codon. This
            RefSeq represents the longer, C-terminally extended isoform (1x).
            As the UGA stop codon has been reported to specify several
            alternative amino acids (tryptophan, cysteine, arginine and
            serine), its location in the longer isoform is denoted by an 'X'.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY380792.1, AK223097.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            stop codon readthrough             :: PMID: 24949972
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..314
                     /product="mitochondrial carrier homolog 2 isoform 1x"
                     /note="met-induced mitochondrial protein; mitochondrial
                     carrier homolog 2; solute carrier family 25, member 50"
                     /calculated_mol_wt=34206
     Region          128..>192
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     CDS             1..314
                     /gene="MTCH2"
                     /gene_synonym="HSPC032; MIMP; SLC25A50"
                     /coded_by="NM_001317231.2:95..1039"
                     /note="isoform 1x is encoded by transcript variant 1"
                     /db_xref="GeneID:23788"
                     /db_xref="HGNC:HGNC:17587"
                     /db_xref="MIM:613221"
ORIGIN      
        1 madaasqvll gsgltilsqp lmyvkvliqv gyeplpptig rnifgrqvcq lpglfsyaqh
       61 iasidgrrgl ftgltprlcs gvlgtvvhgk vlqhyqesdk geelgpgnvq kevsssfdhv
      121 ikettremia rsaatlithp fhvitlrsmv qfigreskyc glcdsiitiy reegilgffa
      181 glvprllgdi lslwlcnsla ylvntyalds gvstmnemks ysqavtgffa smltypfvlv
      241 snlmavnncg laggcppysp iytswidcwc mlqkegnmsr gnslffrkvp fgktyccdlk
      301 mlixrcgagt vtfl
//
LOCUS       NP_001123313            2138 aa            linear   PRI 21-NOV-2025
DEFINITION  voltage-dependent L-type calcium channel subunit alpha-1C isoform
            15 [Homo sapiens].
ACCESSION   NP_001123313
VERSION     NP_001123313.1
DBSOURCE    REFSEQ: accession NM_001129841.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2138)
  AUTHORS   Zhang,X., Liang,X., Cheng,X., Chen,J., Deng,W., Zhang,Y., Cui,L.,
            Cheng,X., Li,X., Yang,C., Ye,B. and Cao,L.
  TITLE     [CACNA1C rs58619945 genotype influences the cortical thickness of
            attention network among patients with Bipolar disorder]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 41 (9), 1045-1052 (2024)
   PUBMED   39217481
  REMARK    GeneRIF: [CACNA1C rs58619945 genotype influences the cortical
            thickness of attention network among patients with Bipolar
            disorder].
REFERENCE   2  (residues 1 to 2138)
  AUTHORS   Yang,Y., Zhu,Z., Hui,L. and Sun,P.
  TITLE     Effects of CACNA1C and ANK3 on cognitive function in patients with
            bipolar disorder
  JOURNAL   Prog Neuropsychopharmacol Biol Psychiatry 133, 111016 (2024)
   PUBMED   38657895
  REMARK    GeneRIF: Effects of CACNA1C and ANK3 on cognitive function in
            patients with bipolar disorder.
REFERENCE   3  (residues 1 to 2138)
  AUTHORS   Almodovar-Paya,C., Guardiola-Ripoll,M., Giralt-Lopez,M.,
            Oscoz-Irurozqui,M., Canales-Rodriguez,E.J., Madre,M.,
            Soler-Vidal,J., Ramiro,N., Callado,L.F., Arias,B., Gallego,C.,
            Pomarol-Clotet,E. and Fatjo-Vilas,M.
  TITLE     NRN1 epistasis with BDNF and CACNA1C: mediation effects on symptom
            severity through neuroanatomical changes in schizophrenia
  JOURNAL   Brain Struct Funct 229 (5), 1299-1315 (2024)
   PUBMED   38720004
  REMARK    GeneRIF: NRN1 epistasis with BDNF and CACNA1C: mediation effects on
            symptom severity through neuroanatomical changes in schizophrenia.
REFERENCE   4  (residues 1 to 2138)
  AUTHORS   Gao,S., Yao,X., Chen,J., Huang,G., Fan,X., Xue,L., Li,Z., Wu,T.,
            Zheng,Y., Huang,J., Jin,X., Wang,Y., Wang,Z., Yu,Y., Liu,L.,
            Pan,X., Song,C. and Yan,N.
  TITLE     Structural basis for human Cav1.2 inhibition by multiple drugs and
            the neurotoxin calciseptine
  JOURNAL   Cell 186 (24), 5363-5374 (2023)
   PUBMED   37972591
  REMARK    GeneRIF: Structural basis for human Cav1.2 inhibition by multiple
            drugs and the neurotoxin calciseptine.
REFERENCE   5  (residues 1 to 2138)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   6  (residues 1 to 2138)
  AUTHORS   Napolitano,C. and Priori,S.G.
  TITLE     CACNA1C-Related Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301577
REFERENCE   7  (residues 1 to 2138)
  AUTHORS   Groffen,A.J., Bikker,H. and Christiaans,I.
  TITLE     Long QT Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301308
REFERENCE   8  (residues 1 to 2138)
  AUTHORS   Sun,W., McPherson,J.D., Hoang,D.Q., Wasmuth,J.J., Evans,G.A. and
            Montal,M.
  TITLE     Mapping of a human brain voltage-gated calcium channel to human
            chromosome 12p13-pter
  JOURNAL   Genomics 14 (4), 1092-1094 (1992)
   PUBMED   1335957
REFERENCE   9  (residues 1 to 2138)
  AUTHORS   Powers,P.A., Gregg,R.G. and Hogan,K.
  TITLE     Linkage mapping of the human gene for the alpha 1 subunit of the
            cardiac DHP-sensitive Ca2+ channel (CACNL1A1) to chromosome
            12p13.2-pter using a dinucleotide repeat
  JOURNAL   Genomics 14 (1), 206-207 (1992)
   PUBMED   1330882
REFERENCE   10 (residues 1 to 2138)
  AUTHORS   Soldatov,N.M.
  TITLE     Molecular diversity of L-type Ca2+ channel transcripts in human
            fibroblasts
  JOURNAL   Proc Natl Acad Sci U S A 89 (10), 4628-4632 (1992)
   PUBMED   1316612
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005342.1, Z34809.1 and
            AC007618.21.
            
            Summary: This gene encodes an alpha-1 subunit of a
            voltage-dependent calcium channel. Calcium channels mediate the
            influx of calcium ions into the cell upon membrane polarization.
            The alpha-1 subunit consists of 24 transmembrane segments and forms
            the pore through which ions pass into the cell. The calcium channel
            consists of a complex of alpha-1, alpha-2/delta, beta, and gamma
            subunits in a 1:1:1:1 ratio. There are multiple isoforms of each of
            these proteins, either encoded by different genes or the result of
            alternative splicing of transcripts. The protein encoded by this
            gene binds to and is inhibited by dihydropyridine. Alternative
            splicing results in many transcript variants encoding different
            proteins. Some of the predicted proteins may not produce functional
            ion channel subunits. [provided by RefSeq, Oct 2012].
            
            Transcript Variant: This variant (15), also referred to has HLCC69,
            lacks three alternate in-frame exons, compared to variant 1,
            resulting in a shorter protein (isoform 15), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z34809.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2147975
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2138
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..2138
                     /product="voltage-dependent L-type calcium channel subunit
                     alpha-1C isoform 15"
                     /note="calcium channel, cardic dihydropyridine-sensitive,
                     alpha-1 subunit; DHPR, alpha-1 subunit; voltage-dependent
                     L-type Ca2+ channel alpha 1 subunit; calcium channel,
                     voltage-dependent, L type, alpha 1C subunit; CACNA1C
                     intronic transcript 2; CACNA1C intronic transcript 2
                     (non-protein coding)"
                     /calculated_mol_wt=239419
     Region          123..416
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          523..764
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          899..1176
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          1218..1487
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          1496..1549
                     /region_name="GPHH"
                     /note="Voltage-dependent L-type calcium channel,
                     IQ-associated; pfam16905"
                     /db_xref="CDD:465306"
     Region          1559..1633
                     /region_name="Ca_chan_IQ"
                     /note="Voltage gated calcium channel IQ domain; pfam08763"
                     /db_xref="CDD:462591"
     Region          1653..2088
                     /region_name="CAC1F_C"
                     /note="Voltage-gated calcium channel subunit alpha,
                     C-term; pfam16885"
                     /db_xref="CDD:465298"
     CDS             1..2138
                     /gene="CACNA1C"
                     /gene_synonym="CACH2; CACN2; CACNA1C-IT2; CACNL1A1;
                     CaV1.2; CCHL1A1; LQT8; NEDHLSS; TS; TS. LQT8"
                     /coded_by="NM_001129841.2:577..6993"
                     /note="isoform 15 is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS44798.1"
                     /db_xref="GeneID:775"
                     /db_xref="HGNC:HGNC:1390"
                     /db_xref="MIM:114205"
ORIGIN      
        1 mvnentrmyi peenhqgsny gsprpahanm nanaaaglap ehiptpgaal swqaaidaar
       61 qaklmgsagn atistvsstq rkrqqygkpk kqgsttatrp prallcltlk npirracisi
      121 vewkpfeiii lltifancva laiyipfped dsnatnsnle rveylfliif tveaflkvia
      181 ygllfhpnay lrngwnlldf iivvvglfsa ileqatkadg analggkgag fdvkalrafr
      241 vlrplrlvsg vpslqvvlns iikamvpllh iallvlfvii iyaiiglelf mgkmhktcyn
      301 qegiadvpae ddpspcalet ghgrqcqngt vckpgwdgpk hgitnfdnfa famltvfqci
      361 tmegwtdvly wvndavgrdw pwiyfvtlii igsffvlnlv lgvlsgefsk erekakargd
      421 fqklrekqql eedlkgyldw itqaedidpe nedegmdeek prnmsmptse tesvntenva
      481 ggdiegencg arlahrisks kfsrywrrwn rfcrrkcraa vksnvfywlv iflvflntlt
      541 iasehynqpn wltevqdtan kallalftae mllkmyslgl qayfvslfnr fdcfvvcggi
      601 letilvetki msplgisvlr cvrllrifki trywnslsnl vasllnsvrs iaslllllfl
      661 fiiifsllgm qlfggkfnfd emqtrrstfd nfpqslltvf qiltgedwns vmydgimayg
      721 gpsfpgmlvc iyfiilficg nyillnvfla iavdnladae sltsaqkeee eekerkklar
      781 taspekkqel vekpavgesk eekielksit adgesppatk inmddlqpne nedkspypnp
      841 ettgeedeee pempvgprpr plselhlkek avpmpeasaf fifssnnrfr lqchrivndt
      901 iftnlilffi llssislaae dpvqhtsfrn hilgnadyvf tsiftleiil kmtaygaflh
      961 kgsfcrnyfn ildllvvsvs lisfgiqssa invvkilrvl rvlrplrain rakglkhvvq
     1021 cvfvairtig nivivttllq fmfacigvql fkgklytcsd sskqteaeck gnyitykdge
     1081 vdhpiiqprs wenskfdfdn vlaammalft vstfegwpel lyrsidshte dkgpiynyrv
     1141 eisiffiiyi iiiaffmmni fvgfvivtfq eqgeqeyknc eldknqrqcv eyalkarplr
     1201 ryipknqhqy kvwyvvnsty feylmfvlil lnticlamqh ygqsclfkia mnilnmlftg
     1261 lftvemilkl iafkpkgyfs dpwnvfdfli vigsiidvil setnpaehtq cspsmnaeen
     1321 srisitffrl frvmrlvkll srgegirtll wtfiksfqal pyvallivml ffiyavigmq
     1381 vfgkialndt teinrnnnfq tfpqavlllf rcatgeawqd imlacmpgkk capesepsns
     1441 tegetpcgss favfyfisfy mlcafliinl fvavimdnfd yltrdwsilg phhldefkri
     1501 waeydpeakg rikhldvvtl lrriqpplgf gklcphrvac krlvsmnmpl nsdgtvmfna
     1561 tlfalvrtal riktegnleq aneelraiik kiwkrtsmkl ldqvvppagd devtvgkfya
     1621 tfliqeyfrk fkkrkeqglv gkpsqrnals lqaglrtlhd igpeirrais gdltaeeeld
     1681 kamkeavsaa seddifrrag glfgnhvsyy qsdgrsafpq tfttqrplhi nkagssqgdt
     1741 espsheklvd stftpssyss tgsnaninna nntalgrlpr pagypstvst veghgpplsp
     1801 airvqevawk lssnrchsre sqaamagqee tsqdetyevk mnhdteacse psllstemls
     1861 yqddenrqlt lpeedkrdir qspkrgflrs aslgrrasfh leclkrqkdr ggdisqktvl
     1921 plhlvhhqal avaglspllq rshspasfpr pfatppatpg srgwppqpvp tlrlegvess
     1981 eklnssfpsi hcgswaettp ggggssaarr vrpvslmvps qagapgrqfh gsasslveav
     2041 liseglgqfa qdpkfievtt qeladacdmt ieemesaadn ilsggapqsp ngallpfvnc
     2101 rdagqdragg eedagcvrar grpseeelqd srvyvssl
//
LOCUS       NP_055526                991 aa            linear   PRI 21-NOV-2025
DEFINITION  centriolar coiled-coil protein of 110 kDa isoform 2 [Homo sapiens].
ACCESSION   NP_055526
VERSION     NP_055526.4
DBSOURCE    REFSEQ: accession NM_014711.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Iyer,S.S., Chen,F., Ogunmolu,F.E., Moradi,S., Volkov,V.A., van
            Grinsven,E.J., van Hoorn,C., Wu,J., Andrea,N., Hua,S., Jiang,K.,
            Vakonakis,I., Potocnjak,M., Herzog,F., Gigant,B., Gudimchuk,N.,
            Stecker,K.E., Dogterom,M., Steinmetz,M.O. and Akhmanova,A.
  TITLE     Centriolar cap proteins CP110 and CPAP control slow elongation of
            microtubule plus ends
  JOURNAL   J Cell Biol 224 (3) (2025)
   PUBMED   39847124
REFERENCE   2  (residues 1 to 991)
  AUTHORS   Xie,S., Naslavsky,N. and Caplan,S.
  TITLE     Emerging insights into CP110 removal during early steps of
            ciliogenesis
  JOURNAL   J Cell Sci 137 (4) (2024)
   PUBMED   38415788
  REMARK    GeneRIF: Emerging insights into CP110 removal during early steps of
            ciliogenesis.
            Review article
REFERENCE   3  (residues 1 to 991)
  AUTHORS   Xie,S., Naslavsky,N. and Caplan,S.
  TITLE     EHD1 promotes CP110 ubiquitination by centriolar satellite delivery
            of HERC2 to the mother centriole
  JOURNAL   EMBO Rep 24 (6), e56317 (2023)
   PUBMED   37074924
  REMARK    GeneRIF: EHD1 promotes CP110 ubiquitination by centriolar satellite
            delivery of HERC2 to the mother centriole.
REFERENCE   4  (residues 1 to 991)
  AUTHORS   Wang,Y., Zhang,Y., Guo,X., Zheng,Y., Zhang,X., Feng,S. and Wu,H.Y.
  TITLE     CCP5 and CCP6 retain CP110 and negatively regulate ciliogenesis
  JOURNAL   BMC Biol 21 (1), 124 (2023)
   PUBMED   37226238
  REMARK    GeneRIF: CCP5 and CCP6 retain CP110 and negatively regulate
            ciliogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 991)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   6  (residues 1 to 991)
  AUTHORS   Casenghi,M., Meraldi,P., Weinhart,U., Duncan,P.I., Korner,R. and
            Nigg,E.A.
  TITLE     Polo-like kinase 1 regulates Nlp, a centrosome protein involved in
            microtubule nucleation
  JOURNAL   Dev Cell 5 (1), 113-125 (2003)
   PUBMED   12852856
REFERENCE   7  (residues 1 to 991)
  AUTHORS   Chen,Z., Indjeian,V.B., McManus,M., Wang,L. and Dynlacht,B.D.
  TITLE     CP110, a cell cycle-dependent CDK substrate, regulates centrosome
            duplication in human cells
  JOURNAL   Dev Cell 3 (3), 339-350 (2002)
   PUBMED   12361598
  REMARK    GeneRIF: CP110, a cell cycle-dependent CDK substrate, regulates
            centrosome duplication (CP110)
REFERENCE   8  (residues 1 to 991)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   9  (residues 1 to 991)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   10 (residues 1 to 991)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY798911.2, AB007879.1, AC012621.8, BP360952.1, DA370828.1,
            CB066937.1, DB504255.1 and BC036654.2.
            
            On Apr 22, 2016 this sequence version replaced NP_055526.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036654.2, AB007879.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.3"
     Protein         1..991
                     /product="centriolar coiled-coil protein of 110 kDa
                     isoform 2"
                     /note="centrosomal protein CP110; centrosomal protein of
                     110 kDa; centriolar coiled-coil protein of 110 kDa;
                     centriolar coiled-coil protein 110kDa"
                     /calculated_mol_wt=111093
     Region          1..223
                     /region_name="CEP97 binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Region          29..106
                     /region_name="CaM_bind"
                     /note="Calcium-dependent calmodulin binding; pfam16025"
                     /db_xref="CDD:464981"
     Region          64..82
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Region          67..82
                     /region_name="Required for interaction with CEP290.
                     /evidence=ECO:0000269|PubMed:18694559"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:26304236; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000305|PubMed:26304236; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Region          350..565
                     /region_name="Interaction with CEP76.
                     /evidence=ECO:0000269|PubMed:19460342"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSH4; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSH4; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43303.3)"
     Region          611..633
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Region          <638..>704
                     /region_name="Stathmin"
                     /note="Stathmin family; pfam00836"
                     /db_xref="CDD:459956"
     Region          <639..>808
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          781..821
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     Region          909..924
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O43303.3)"
     CDS             1..991
                     /gene="CCP110"
                     /gene_synonym="Cep110; CP110"
                     /coded_by="NM_014711.6:306..3281"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10579.1"
                     /db_xref="GeneID:9738"
                     /db_xref="HGNC:HGNC:24342"
                     /db_xref="MIM:609544"
ORIGIN      
        1 meeyekfcek slariqeasl stesflpaqs esislirfhg vailspllni ekrkemqqek
       61 qkaldveark qvnrkkallt rvqeildnvq vrkapnasdf dqwemetvys nsevrnlnvp
      121 atfpnsfpsh tehstaakld kiagilpldn edqcktdgid lardsegfns pkqcdssnis
      181 hveneafpkt ssatpqetli sdgpfsvneq qdlpllaevi pdpyvmslqn lmkkskeyie
      241 reqsrrslrg sinrivnesh ldkehdavev adcvkekgql tgkhcvsvip dkpslnksnv
      301 llqgastqas smsmpvlasf skvdipirtg hptvlesnsd fkviptfvte nnviksltgs
      361 yaklpspeps mspkmhrrrs rtssachili nnpinacels pkgkeqamdl iiqdtdentn
      421 vpeimpklpt dlagvcsskv yvgkntsevk edvvlgksnq vcqssgnhle nkvthglvtv
      481 egqltsderg ahimnstcaa mpklhepyas sqciaspnfg tvsglkpasm lekncslqte
      541 lnksydvknp spllmqnqnt rqqmdtpmvs cgneqfldns fekvkrrldl didglqkenc
      601 pyvitsgite qerqhlpekr ypkgsgfvnk nkmlgtsske seellkskml afeemrkrle
      661 eqhaqqlsll iaeqereqer lqkeieeqek mlkekkamta easeldinna velewrkisd
      721 sslletmlsq adslhtsnsn ssgftnsamq ysfvsaneap fylwgsstsg ltklsvtrpf
      781 graktrwsqv fsleiqakfn kitavakgfl trrlmqtdkl kqlrqtvkdt mefirsfqse
      841 aplkrgivsa qdaslqervl aqlraalygi hdiffvmdaa ermsilhhdr evrkekmlrq
      901 mdkmksprva lsaatqksld rkkymkaaem gmpnkkflvk qnpsetrvlq pnqgqnapvh
      961 rllsrqgsic rknpkkaakc cdnlrrqhsl g
//
LOCUS       NP_001364180             372 aa            linear   PRI 21-NOV-2025
DEFINITION  pleckstrin homology domain-containing family A member 1 isoform 9
            [Homo sapiens].
ACCESSION   NP_001364180
VERSION     NP_001364180.1
DBSOURCE    REFSEQ: accession NM_001377251.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Huang,Q. and Xiang,Y.
  TITLE     Polymorphisms in Selected Genes and Their Association with
            Age-Related Macular Degeneration in a Chinese Population
  JOURNAL   Med Sci Monit 24, 1693-1700 (2018)
   PUBMED   29565837
  REMARK    GeneRIF: investigated the association of PLEKHA1 958A/G,
            polymorphisms with Age-Related Macular Degeneration (AMD) risk.
            PLEKHA1 958A/G polymorphism was associated with a decreased AMD
            risk (additive model: aOR=0.722, 95% CI=0.450-0.979, P=0.019;
            allele model: aOR=0.883, 95% CI=0.736-0.992, P=0.014)
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Kortvely,E. and Ueffing,M.
  TITLE     Gene Structure of the 10q26 Locus: A Clue to Cracking the
            ARMS2/HTRA1 Riddle?
  JOURNAL   Adv Exp Med Biol 854, 23-29 (2016)
   PUBMED   26427389
  REMARK    GeneRIF: Studies indicate that the high-risk allele of the 10q26
            locus encompasses three genes, PLEKHA1, ARMS2, and HTRA1 with high
            linkage disequilibrium.
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Gupta,D., Gupta,V., Singh,V., Chawla,S., Parveen,F., Agrawal,S. and
            Phadke,S.R.
  TITLE     Study of Polymorphisms in CX3CR1, PLEKHA1 and VEGF genes as risk
            factors for age-related macular degeneration in Indian patients
  JOURNAL   Arch Med Res 45 (6), 489-494 (2014)
   PUBMED   25050486
  REMARK    GeneRIF: CX3CR1 (T280M and V249I) and PLEKHA1 (A320T) polymorphisms
            were not found to be associated with age-related macular
            degeneration in an Indian population.
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Hogan,A., Yakubchyk,Y., Chabot,J., Obagi,C., Daher,E., Maekawa,K.
            and Gee,S.H.
  TITLE     The phosphoinositol 3,4-bisphosphate-binding protein TAPP1
            interacts with syntrophins and regulates actin cytoskeletal
            organization
  JOURNAL   J Biol Chem 279 (51), 53717-53724 (2004)
   PUBMED   15485858
  REMARK    GeneRIF: syntrophins regulate the localization of TAPP1, which may
            be important for remodeling the actin cytoskeleton in response to
            growth factor stimulation
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Kimber,W.A., Deak,M., Prescott,A.R. and Alessi,D.R.
  TITLE     Interaction of the protein tyrosine phosphatase PTPL1 with the
            PtdIns(3,4)P2-binding adaptor protein TAPP1
  JOURNAL   Biochem J 376 (Pt 2), 525-535 (2003)
   PUBMED   14516276
  REMARK    GeneRIF: TAPP1 binds to protein tyrosine phosphatase PTPL1.
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Marshall,A.J., Krahn,A.K., Ma,K., Duronio,V. and Hou,S.
  TITLE     TAPP1 and TAPP2 are targets of phosphatidylinositol 3-kinase
            signaling in B cells: sustained plasma membrane recruitment
            triggered by the B-cell antigen receptor
  JOURNAL   Mol Cell Biol 22 (15), 5479-5491 (2002)
   PUBMED   12101241
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Kimber,W.A., Trinkle-Mulcahy,L., Cheung,P.C., Deak,M.,
            Marsden,L.J., Kieloch,A., Watt,S., Javier,R.T., Gray,A.,
            Downes,C.P., Lucocq,J.M. and Alessi,D.R.
  TITLE     Evidence that the tandem-pleckstrin-homology-domain-containing
            protein TAPP1 interacts with Ptd(3,4)P2 and the
            multi-PDZ-domain-containing protein MUPP1 in vivo
  JOURNAL   Biochem J 361 (Pt 3), 525-536 (2002)
   PUBMED   11802782
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Thomas,C.C., Dowler,S., Deak,M., Alessi,D.R. and van Aalten,D.M.
  TITLE     Crystal structure of the phosphatidylinositol
            3,4-bisphosphate-binding pleckstrin homology (PH) domain of tandem
            PH-domain-containing protein 1 (TAPP1): molecular basis of lipid
            specificity
  JOURNAL   Biochem J 358 (Pt 2), 287-294 (2001)
   PUBMED   11513726
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Dowler,S., Currie,R.A., Campbell,D.G., Deak,M., Kular,G.,
            Downes,C.P. and Alessi,D.R.
  TITLE     Identification of pleckstrin-homology-domain-containing proteins
            with novel phosphoinositide-binding specificities
  JOURNAL   Biochem J 351 (Pt 1), 19-31 (2000)
   PUBMED   11001876
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX664700.3 and BX842242.1.
            
            Summary: This gene encodes a pleckstrin homology domain-containing
            adapter protein. The encoded protein is localized to the plasma
            membrane where it specifically binds phosphatidylinositol
            3,4-bisphosphate. This protein may be involved in the formation of
            signaling complexes in the plasma membrane. Polymorphisms in this
            gene are associated with age-related macular degeneration.
            Alternate splicing results in multiple transcript variants. A
            pseudogene of this gene is found on chromosome 5.[provided by
            RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853561.4267.1,
                                           SRR1803615.160740.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..372
                     /product="pleckstrin homology domain-containing family A
                     member 1 isoform 9"
                     /note="tandem PH domain-containing protein 1; pleckstrin
                     homology domain containing, family A (phosphoinositide
                     binding specific) member 1"
                     /calculated_mol_wt=42346
     Region          1..110
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          174..287
                     /region_name="PH2_TAPP1_2"
                     /note="Tandem PH-domain-containing proteins 1 and 2
                     Pleckstrin homology (PH) domain, C-terminal repeat;
                     cd13271"
                     /db_xref="CDD:270090"
     Site            order(189,191..192,200,211,221..222,254)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270090"
     CDS             1..372
                     /gene="PLEKHA1"
                     /gene_synonym="TAPP1"
                     /coded_by="NM_001377251.1:190..1308"
                     /note="isoform 9 is encoded by transcript variant 23"
                     /db_xref="GeneID:59338"
                     /db_xref="HGNC:HGNC:14335"
                     /db_xref="MIM:607772"
ORIGIN      
        1 mpyvdrqnri cgfldieene nsgkflrryf ildtredsfv wymdnpqnlp sgssrvgaik
       61 ltyiskvsda tklrpkaefc fvmnagmrky flqandqqdl vewvpkqsds qpnsdnlsrh
      121 gecgkkqvsy rtdivggvpi itptqkeevn ecgesidrnn lkrsqshlpy ftpkppqdsa
      181 vikagycvkq gavmknwkrr yfqldentig yfkselekep lrviplkevh kvqeckqsdi
      241 mmrdnlfeiv ttsrtfyvqa dspeemhswi kavsgaivaq rgpgrsassm rqarrlsnpc
      301 iqrsippvlq npntlsvlpt qpppphipqp laatlwsqpl pwrsedftsl lprssqgtsr
      361 srlslqenql pk
//
LOCUS       NP_004583                951 aa            linear   PRI 21-NOV-2025
DEFINITION  splicing factor, suppressor of white-apricot homolog isoform 2
            [Homo sapiens].
ACCESSION   NP_004583
VERSION     NP_004583.2
DBSOURCE    REFSEQ: accession NM_004592.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 951)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 951)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 951)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 951)
  AUTHORS   Crisci,A., Raleff,F., Bagdiul,I., Raabe,M., Urlaub,H., Rain,J.C.
            and Kramer,A.
  TITLE     Mammalian splicing factor SF1 interacts with SURP domains of U2
            snRNP-associated proteins
  JOURNAL   Nucleic Acids Res 43 (21), 10456-10473 (2015)
   PUBMED   26420826
REFERENCE   5  (residues 1 to 951)
  AUTHORS   Moayedi,Y., Basch,M.L., Pacheco,N.L., Gao,S.S., Wang,R.,
            Harrison,W., Xiao,N., Oghalai,J.S., Overbeek,P.A., Mardon,G. and
            Groves,A.K.
  TITLE     The candidate splicing factor Sfswap regulates growth and
            patterning of inner ear sensory organs
  JOURNAL   PLoS Genet 10 (1), e1004055 (2014)
   PUBMED   24391519
REFERENCE   6  (residues 1 to 951)
  AUTHORS   Brasch-Andersen,C., Tan,Q., Borglum,A.D., Haagerup,A., Larsen,T.R.,
            Vestbo,J. and Kruse,T.A.
  TITLE     Significant linkage to chromosome 12q24.32-q24.33 and
            identification of SFRS8 as a possible asthma susceptibility gene
  JOURNAL   Thorax 61 (10), 874-879 (2006)
   PUBMED   16738036
REFERENCE   7  (residues 1 to 951)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 951)
  AUTHORS   Sarkissian,M., Winne,A. and Lafyatis,R.
  TITLE     The mammalian homolog of suppressor-of-white-apricot regulates
            alternative mRNA splicing of CD45 exon 4 and fibronectin IIICS
  JOURNAL   J Biol Chem 271 (49), 31106-31114 (1996)
   PUBMED   8940107
REFERENCE   9  (residues 1 to 951)
  AUTHORS   Denhez,F. and Lafyatis,R.
  TITLE     Conservation of regulated alternative splicing and identification
            of functional domains in vertebrate homologs to the Drosophila
            splicing regulator, suppressor-of-white-apricot
  JOURNAL   J Biol Chem 269 (23), 16170-16179 (1994)
   PUBMED   8206918
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC117500.13 and AC131009.7.
            
            On Sep 18, 2002 this sequence version replaced NP_004583.1.
            
            Summary: This gene encodes a human homolog of Drosophila splicing
            regulatory protein. This gene autoregulates its expression by
            control of splicing of its first two introns. In addition, it also
            regulates the splicing of fibronectin and CD45 genes. Two
            transcript variants encoding different isoforms have been
            identified. [provided by RefSeq, May 2012].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (2) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U08377.1, BC136678.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261674.9/ ENSP00000261674.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..951
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.33"
     Protein         1..951
                     /product="splicing factor, suppressor of white-apricot
                     homolog isoform 2"
                     /note="splicing factor, arginine/serine-rich 8
                     (suppressor-of-white-apricot, Drosophila homolog);
                     splicing factor SWAP homolog; splicing factor,
                     arginine/serine-rich 8 (suppressor-of-white-apricot
                     homolog, Drosophila); suppressor of white apricot protein
                     homolog; splicing factor, suppressor of white-apricot
                     family; splicing factor, suppressor of white-apricot
                     homolog"
                     /calculated_mol_wt=104691
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12872.3)"
     Region          35..155
                     /region_name="DRY_EERY"
                     /note="Alternative splicing regulator; pfam09750"
                     /db_xref="CDD:462881"
     Region          155..185
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12872.3)"
     Region          209..262
                     /region_name="SWAP"
                     /note="Suppressor-of-White-APricot splicing regulator;
                     smart00648"
                     /db_xref="CDD:197818"
     Region          211..253
                     /region_name="SURP motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12872.3)"
     Region          272..298
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12872.3)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q12872.3)"
     Site            315
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q12872.3)"
     Region          332..354
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12872.3)"
     Region          404..439
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12872.3)"
     Region          457..508
                     /region_name="SWAP"
                     /note="Suppressor-of-White-APricot splicing regulator;
                     smart00648"
                     /db_xref="CDD:197818"
     Region          459..499
                     /region_name="SURP motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12872.3)"
     Region          512..569
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12872.3)"
     Region          592..927
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12872.3)"
     Site            604
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q12872.3)"
     Region          <637..718
                     /region_name="rpsP"
                     /note="30S ribosomal protein S16; Provisional; PRK14521"
                     /db_xref="CDD:237744"
     Site            642
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q12872.3)"
     Site            832
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12872.3)"
     Site            834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12872.3)"
     Site            905
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3USH5; propagated from
                     UniProtKB/Swiss-Prot (Q12872.3)"
     Site            909
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q12872.3)"
     CDS             1..951
                     /gene="SFSWAP"
                     /gene_synonym="SFRS8; SWAP"
                     /coded_by="NM_004592.4:141..2996"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9273.1"
                     /db_xref="GeneID:6433"
                     /db_xref="HGNC:HGNC:10790"
                     /db_xref="MIM:601945"
ORIGIN      
        1 mygasggrak perksgakee agpggagggg srvellvfgy acklfrdder alaqeqgqhl
       61 ipwmgdhkil idrydgrghl hdlseydaey stwnrdyqls eeeariealc deerylalht
      121 dlleeearqe eeykrlseal aedgsynavg ftygsdyydp septeeeeps kqrekneaen
      181 leeneepfva plglsvpsdv elpptakmha iiertasfvc rqgaqfeiml kakqarnsqf
      241 dflrfdhyln pyykfiqkam kegrytvlae nksdekkksg vssdnedddd eedgnylhps
      301 lfaskkcnrl eelmkplkvv dpdhplaalv rkaqadsstp tphnadgapv qpsqveytad
      361 stvaamyysy ymlpdgtycl appppgidvt tyystlpagv tvsnspgvtt tappppgttp
      421 lpppttaets sgatsttttt salapvaaii ppppdvqpvi dklaeyvarn glkfetsvra
      481 kndqrfeflq pwhqynayye fkkqfflqke ggdsmqavsa peeaptdsap ekpsdagedg
      541 apedaaevga ragsggkkea sssktvpdgk lvkasfapis faikakendl lpleknrvkl
      601 dddsdddees kegqessssa antnpavapp cvvveekkpq ltqeeleakq akqkledrla
      661 aaareklaqa skeskekqlq aerkrkaalf lqtlknplpe aeagkieesp fsveessttp
      721 cplltggrpl ptlevkppdr psskskdppr eeekekkkkk hkkrsrtrsr spkyhsssks
      781 rsrshskakh slpsayrtvr rsrsrsrspr rrahsperrr eersvptayr vsrspgasrk
      841 rtrsrsphek kkkrrsrsrt kskarsqsvs pskqaaprpa apaahsahsa svspvesrgs
      901 sqersrgvsq ekeaqissai vssvqskitq dlmakvraml aasknlqtsa s
//
LOCUS       NP_001258918             584 aa            linear   PRI 21-NOV-2025
DEFINITION  centrosomal protein of 76 kDa isoform b [Homo sapiens].
ACCESSION   NP_001258918
VERSION     NP_001258918.1
DBSOURCE    REFSEQ: accession NM_001271989.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 584)
  AUTHORS   Takeda,Y., Yamazaki,K., Hashimoto,K., Watanabe,K., Chinen,T. and
            Kitagawa,D.
  TITLE     The centriole protein CEP76 negatively regulates PLK1 activity in
            the cytoplasm for proper mitotic progression
  JOURNAL   J Cell Sci 133 (19) (2020)
   PUBMED   32878946
  REMARK    GeneRIF: The centriole protein CEP76 negatively regulates PLK1
            activity in the cytoplasm for proper mitotic progression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 584)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 584)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   7  (residues 1 to 584)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   8  (residues 1 to 584)
  AUTHORS   Tsang,W.Y., Spektor,A., Vijayakumar,S., Bista,B.R., Li,J.,
            Sanchez,I., Duensing,S. and Dynlacht,B.D.
  TITLE     Cep76, a centrosomal protein that specifically restrains centriole
            reduplication
  JOURNAL   Dev Cell 16 (5), 649-660 (2009)
   PUBMED   19460342
  REMARK    GeneRIF: Enforced Cep76 expression specifically inhibits centriole
            amplification in cells undergoing multiple rounds of duplication
            without preventing the formation of extra procentrioles from a
            parental template.
REFERENCE   9  (residues 1 to 584)
  AUTHORS   Hassan,M.J., Chishti,M.S., Jamal,S.M., Tariq,M. and Ahmad,W.
  TITLE     A syndromic form of autosomal recessive congenital microcephaly
            (Jawad syndrome) maps to chromosome 18p11.22-q11.2
  JOURNAL   Hum Genet 123 (1), 77-82 (2008)
   PUBMED   18071751
REFERENCE   10 (residues 1 to 584)
  AUTHORS   Andersen,J.S., Wilkinson,C.J., Mayor,T., Mortensen,P., Nigg,E.A.
            and Mann,M.
  TITLE     Proteomic characterization of the human centrosome by protein
            correlation profiling
  JOURNAL   Nature 426 (6966), 570-574 (2003)
   PUBMED   14654843
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK298223.1, AK303117.1,
            BC026307.1, DA476378.1 and AP005482.4.
            
            Summary: This gene encodes a centrosomal protein which regulates
            centriole amplification by limiting centriole duplication to once
            per cell cycle. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            coding region, compared to variant 1. It encodes isoform (b) which
            is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303117.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.21"
     Protein         1..584
                     /product="centrosomal protein of 76 kDa isoform b"
                     /note="centrosomal protein 76kDa"
                     /calculated_mol_wt=65602
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q0VEJ0; propagated from
                     UniProtKB/Swiss-Prot (Q8TAP6.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8TAP6.1)"
     Region          <96..183
                     /region_name="CEP76-C2"
                     /note="CEP76 C2 domain; pfam15627"
                     /db_xref="CDD:464781"
     CDS             1..584
                     /gene="CEP76"
                     /gene_synonym="C18orf9; HsT1705"
                     /coded_by="NM_001271989.2:176..1930"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS62390.1"
                     /db_xref="GeneID:79959"
                     /db_xref="HGNC:HGNC:25727"
                     /db_xref="MIM:620791"
ORIGIN      
        1 mslppekase lkqlihqqls kmdvhgrire ilaetireel apdqqhlste dlikalrrrg
       61 iiddvmkeln fvtdsveqel psspkqpicf drqstlkksd gtrmadsttm lsisdpihmv
      121 liktdifget tlvasyflew rsvlgsengv tsltvelmgv gteskvsvgi lniklemypp
      181 lnqtlsqevv ntqlalerqk taekerlflv yakqwwreyl qirpshnsrl vkifaqdeng
      241 inrpvcsyvk plragrlldt prqaarfvnv lgyerapvig gggkqeqwct llaflcrnkg
      301 dcedhanllc slllgyglea fvcvgtkakg vphawvmtcg tdgaitfwes ltghryihkp
      361 tnpdeppvae qpkplypyrt igcvfnhqmf lgncqpsdav etcvfdlnde skwkpmseea
      421 iksvcapgat tslppfpplc astidasvts neiemqlrll vsehrkdlgl ttvwedqlsy
      481 llspalasye ferttsisag neefqdairr avpdghtfkg fpihfvyrna rrafatclrs
      541 pfceeiiccr gdqvrlavrv rvftypesac avwimfacky rsvl
//
LOCUS       NP_001373265             403 aa            linear   PRI 21-NOV-2025
DEFINITION  angiopoietin-2 isoform e precursor [Homo sapiens].
ACCESSION   NP_001373265
VERSION     NP_001373265.1
DBSOURCE    REFSEQ: accession NM_001386336.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Pastura,P., McDaniel,C.G., Alharbi,S., Fox,D., Coleman,B.,
            Malik,P., Adams,D.M. and Le Cras,T.D.
  TITLE     NRASQ61R mutation drives elevated angiopoietin-2 expression in
            human endothelial cells and a genetic mouse model
  JOURNAL   Pediatr Blood Cancer 71 (7), e31032 (2024)
   PUBMED   38711167
  REMARK    GeneRIF: NRAS[Q61R] mutation drives elevated angiopoietin-2
            expression in human endothelial cells and a genetic mouse model.
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Meder,L., Orschel,C.I., Otto,C.J., Koker,M., Bragelmann,J.,
            Ercanoglu,M.S., Dahling,S., Compes,A., Selenz,C., Nill,M.,
            Dietlein,F., Florin,A., Eich,M.L., Borchmann,S., Odenthal,M.,
            Blazquez,R., Hilberg,F., Klein,F., Hallek,M., Buttner,R.,
            Reinhardt,H.C. and Ullrich,R.T.
  TITLE     Blocking the angiopoietin-2-dependent integrin beta-1 signaling
            axis abrogates small cell lung cancer invasion and metastasis
  JOURNAL   JCI Insight 9 (10), e166402 (2024)
   PUBMED   38775153
  REMARK    GeneRIF: Blocking the angiopoietin-2-dependent integrin beta-1
            signaling axis abrogates small cell lung cancer invasion and
            metastasis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Wang,X., Huang,J., Liu,J., Sun,Y., Feng,X., Jin,Y. and Zhou,W.
  TITLE     Silencing ANGPT2 alleviates ulcerative colitis by regulating
            autophagy-mediated NLRP3 inflammasome inactivation via the mTOR
            signaling pathway
  JOURNAL   Braz J Med Biol Res 57, e13379 (2024)
   PUBMED   38808888
  REMARK    GeneRIF: Silencing ANGPT2 alleviates ulcerative colitis by
            regulating autophagy-mediated NLRP3 inflammasome inactivation via
            the mTOR signaling pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Smadja,D.M., Guerin,C.L., Chocron,R., Yatim,N., Boussier,J.,
            Gendron,N., Khider,L., Hadjadj,J., Goudot,G., Debuc,B., Juvin,P.,
            Hauw-Berlemont,C., Augy,J.L., Peron,N., Messas,E., Planquette,B.,
            Sanchez,O., Charbit,B., Gaussem,P., Duffy,D., Terrier,B.,
            Mirault,T. and Diehl,J.L.
  TITLE     Angiopoietin-2 as a marker of endothelial activation is a good
            predictor factor for intensive care unit admission of COVID-19
            patients
  JOURNAL   Angiogenesis 23 (4), 611-620 (2020)
   PUBMED   32458111
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Akwii,R.G., Sajib,M.S., Zahra,F.T. and Mikelis,C.M.
  TITLE     Role of Angiopoietin-2 in Vascular Physiology and Pathophysiology
  JOURNAL   Cells 8 (5), 471 (2019)
   PUBMED   31108880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 403)
  AUTHORS   Scholz,A., Plate,K.H. and Reiss,Y.
  TITLE     Angiopoietin-2: a multifaceted cytokine that functions in both
            angiogenesis and inflammation
  JOURNAL   Ann N Y Acad Sci 1347, 45-51 (2015)
   PUBMED   25773744
  REMARK    Review article
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Fagiani,E. and Christofori,G.
  TITLE     Angiopoietins in angiogenesis
  JOURNAL   Cancer Lett 328 (1), 18-26 (2013)
   PUBMED   22922303
  REMARK    Review article
REFERENCE   8  (residues 1 to 403)
  AUTHORS   Witzenbichler,B., Maisonpierre,P.C., Jones,P., Yancopoulos,G.D. and
            Isner,J.M.
  TITLE     Chemotactic properties of angiopoietin-1 and -2, ligands for the
            endothelial-specific receptor tyrosine kinase Tie2
  JOURNAL   J Biol Chem 273 (29), 18514-18521 (1998)
   PUBMED   9660821
REFERENCE   9  (residues 1 to 403)
  AUTHORS   Cheung,A.H., Stewart,R.J. and Marsden,P.A.
  TITLE     Endothelial Tie2/Tek ligands angiopoietin-1 (ANGPT1) and
            angiopoietin-2 (ANGPT2): regional localization of the human genes
            to 8q22.3-q23 and 8p23
  JOURNAL   Genomics 48 (3), 389-391 (1998)
   PUBMED   9545648
REFERENCE   10 (residues 1 to 403)
  AUTHORS   Maisonpierre,P.C., Suri,C., Jones,P.F., Bartunkova,S.,
            Wiegand,S.J., Radziejewski,C., Compton,D., McClain,J.,
            Aldrich,T.H., Papadopoulos,N., Daly,T.J., Davis,S., Sato,T.N. and
            Yancopoulos,G.D.
  TITLE     Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo
            angiogenesis
  JOURNAL   Science 277 (5322), 55-60 (1997)
   PUBMED   9204896
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018398.10.
            
            Summary: This gene belongs to the angiopoietin family of growth
            factors. The protein encoded by this gene is an antagonist of
            angiopoietin 1, and both angiopoietin 1 and angiopoietin 2 are
            ligands for the endothelial TEK receptor tyrosine kinase.
            Angiopoietin 2 is upregulated in multiple inflammatory diseases and
            is implicated in the direct control of inflammation-related
            signaling pathways. The encoded protein affects angiogenesis during
            embryogenesis and tumorigenesis, disrupts the vascular remodeling
            ability of angiopoietin 1, and may induce endothelial cell
            apoptosis. This gene serves a prognostic biomarker for acute
            respiratory distress syndrome. [provided by RefSeq, Aug 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p23.1"
     Protein         1..403
                     /product="angiopoietin-2 isoform e precursor"
                     /note="angiopoietin-2a; Tie2-ligand; angiopoietin-2B"
                     /calculated_mol_wt=44664
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1886
     Region          <78..>295
                     /region_name="CCDC158"
                     /note="Coiled-coil domain-containing protein 158;
                     pfam15921"
                     /db_xref="CDD:464943"
     Site            89
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O15123.1)"
     Site            119
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O15123.1)"
     Site            133
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O15123.1)"
     Site            151
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O15123.1)"
     Site            240
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O15123.1)"
     Region          280..>403
                     /region_name="FBG"
                     /note="Fibrinogen-related domains (FReDs); smart00186"
                     /db_xref="CDD:214548"
     Site            304
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O15123.1)"
     Site            400
                     /site_type="other"
                     /note="gamma-gamma dimer interface [polypeptide binding]"
                     /db_xref="CDD:238040"
     CDS             1..403
                     /gene="ANGPT2"
                     /gene_synonym="AGPT2; ANG2; LMPHM10"
                     /coded_by="NM_001386336.1:312..1523"
                     /note="isoform e precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:285"
                     /db_xref="HGNC:HGNC:485"
                     /db_xref="MIM:601922"
ORIGIN      
        1 mwqivfftls cdlvlaaayn nfrksmdsig kkqyqvqhgs csytfllpem dncrsssspy
       61 vsnavqrdap leyddsvqrl qvlenimenn tqwlmkleny iqdnmkkemv eiqqnavqnq
      121 tavmieigtn llnqtaeqtr kltdveaqvl nqttrlelql lehslstnkl ekqildqtse
      181 inklqdknsf lekkvlamed khiiqlqsik eekdqlqvlv skqnsiieel ekkivtatvn
      241 nsvlqkqqhd lmetvnnllt mmstsnsakd ptvakeeqis frdcaevfks ghttngiytl
      301 tfpnsteeik aycdmeaggg gwtiiqrred gsvdfqrtwk eykvgfgnps geywlgnefv
      361 sqltnqqryv lkihlkdweg neayslyehf ylsseelnyr lvv
//
LOCUS       NP_001269471             951 aa            linear   PRI 21-NOV-2025
DEFINITION  synaptonemal complex protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001269471
VERSION     NP_001269471.1
DBSOURCE    REFSEQ: accession NM_001282542.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 951)
  AUTHORS   Nabi,S., Askari,M., Rezaei-Gazik,M., Salehi,N., Almadani,N.,
            Tahamtani,Y. and Totonchi,M.
  TITLE     A rare frameshift mutation in SYCP1 is associated with human male
            infertility
  JOURNAL   Mol Hum Reprod 28 (4) (2022)
   PUBMED   35377450
  REMARK    GeneRIF: A rare frameshift mutation in SYCP1 is associated with
            human male infertility.
REFERENCE   2  (residues 1 to 951)
  AUTHORS   Dunce,J.M., Dunne,O.M., Ratcliff,M., Millan,C., Madgwick,S.,
            Uson,I. and Davies,O.R.
  TITLE     Structural basis of meiotic chromosome synapsis through SYCP1
            self-assembly
  JOURNAL   Nat Struct Mol Biol 25 (7), 557-569 (2018)
   PUBMED   29915389
  REMARK    GeneRIF: SYCP1 has an obligate tetrameric structure in which an
            N-terminal four-helical bundle bifurcates into two elongated
            C-terminal dimeric coiled-coils. This building block assembles into
            a zipper-like lattice through two self-assembly sites. N-terminal
            sites undergo cooperative head-to-head assembly in the midline,
            while C-terminal sites interact back to back on the chromosome
            axis.
REFERENCE   3  (residues 1 to 951)
  AUTHORS   Seo,E.K., Choi,J.Y., Jeong,J.H., Kim,Y.G. and Park,H.H.
  TITLE     Crystal Structure of C-Terminal Coiled-Coil Domain of SYCP1 Reveals
            Non-Canonical Anti-Parallel Dimeric Structure of Transverse
            Filament at the Synaptonemal Complex
  JOURNAL   PLoS One 11 (8), e0161379 (2016)
   PUBMED   27548613
  REMARK    GeneRIF: Crystal structure of C-terminal coiled-coil domain of
            SYCP1 reveals non-canonical anti-parallel dimeric structure of
            transverse filament at the synaptonemal complex.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 951)
  AUTHORS   Cahoon,C.K. and Hawley,R.S.
  TITLE     Regulating the construction and demolition of the synaptonemal
            complex
  JOURNAL   Nat Struct Mol Biol 23 (5), 369-377 (2016)
   PUBMED   27142324
  REMARK    Review article
REFERENCE   5  (residues 1 to 951)
  AUTHORS   Park,H.H.
  TITLE     X-ray crystallographic studies of the middle part of the human
            synaptonemal complex protein 1 coiled-coil domain
  JOURNAL   Acta Crystallogr F Struct Biol Commun 71 (Pt 9), 1131-1134 (2015)
   PUBMED   26323297
  REMARK    GeneRIF: crystal structure of the middle part of the human
            synaptonemal complex protein 1 coiled-coil domain
REFERENCE   6  (residues 1 to 951)
  AUTHORS   Eichmuller,S., Usener,D., Dummer,R., Stein,A., Thiel,D. and
            Schadendorf,D.
  TITLE     Serological detection of cutaneous T-cell lymphoma-associated
            antigens
  JOURNAL   Proc Natl Acad Sci U S A 98 (2), 629-634 (2001)
   PUBMED   11149944
REFERENCE   7  (residues 1 to 951)
  AUTHORS   Tureci,O., Sahin,U., Zwick,C., Koslowski,M., Seitz,G. and
            Pfreundschuh,M.
  TITLE     Identification of a meiosis-specific protein as a member of the
            class of cancer/testis antigens
  JOURNAL   Proc Natl Acad Sci U S A 95 (9), 5211-5216 (1998)
   PUBMED   9560255
REFERENCE   8  (residues 1 to 951)
  AUTHORS   Meuwissen,R.L., Meerts,I., Hoovers,J.M., Leschot,N.J. and
            Heyting,C.
  TITLE     Human synaptonemal complex protein 1 (SCP1): isolation and
            characterization of the cDNA and chromosomal localization of the
            gene
  JOURNAL   Genomics 39 (3), 377-384 (1997)
   PUBMED   9119375
REFERENCE   9  (residues 1 to 951)
  AUTHORS   Kondoh,N., Nishina,Y., Tsuchida,J., Koga,M., Tanaka,H., Uchida,K.,
            Inazawa,J., Taketo,M., Nozaki,M., Nojima,H., Matsumiya,K.,
            Namiki,M., Okuyama,A. and Nishimune,Y.
  TITLE     Assignment of synaptonemal complex protein 1 (SCP1) to human
            chromosome 1p13 by fluorescence in situ hybridization and its
            expression in the testis
  JOURNAL   Cytogenet Cell Genet 78 (2), 103-104 (1997)
   PUBMED   9371398
REFERENCE   10 (residues 1 to 951)
  AUTHORS   Meuwissen,R.L., Offenberg,H.H., Dietrich,A.J., Riesewijk,A., van
            Iersel,M. and Heyting,C.
  TITLE     A coiled-coil related protein specific for synapsed regions of
            meiotic prophase chromosomes
  JOURNAL   EMBO J 11 (13), 5091-5100 (1992)
   PUBMED   1464329
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK315268.1 and AA868393.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            lacks an in-frame exon in the 3' coding region, compared to variant
            1. The encoded isoform (2) is shorter, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK315268.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..951
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.2"
     Protein         1..951
                     /product="synaptonemal complex protein 1 isoform 2"
                     /note="cancer/testis antigen 8; testicular tissue protein
                     Li 191"
                     /calculated_mol_wt=111109
     Region          28..767
                     /region_name="SCP-1"
                     /note="Synaptonemal complex protein 1 (SCP-1); pfam05483"
                     /db_xref="CDD:114219"
     CDS             1..951
                     /gene="SYCP1"
                     /gene_synonym="CT8; HOM-TES-14; SCP-1; SCP1"
                     /coded_by="NM_001282542.2:184..3039"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS72840.1"
                     /db_xref="GeneID:6847"
                     /db_xref="HGNC:HGNC:11487"
                     /db_xref="MIM:602162"
ORIGIN      
        1 mekqkpfalf vpprssssqv savkpqtlgg dstffksfnk cteddfefpf aktnlsknge
       61 nidsdpalqk vnflpvleqv gnsdchyqeg lkdsdlense glsrvyskly keaekikkwk
      121 vsteaelrqk esklqenrki ieaqrkaiqe lqfgnekvsl kleegiqenk dlikennatr
      181 hlcnllketc arsaektkky eyereetrqv ymdlnnniek mitafeelrv qaensrlemh
      241 fklkedyeki qhleqeykke indkekqvsl lliqiteken kmkdltflle esrdkvnqle
      301 ektklqsenl kqsiekqhhl tkeledikvs lqrsvstqka leedlqiatk ticqlteeke
      361 tqmeesnkar aahsfvvtef ettvcsleel lrteqqrlek nedqlkiltm elqkkssele
      421 emtkltnnke veleelkkvl geketllyen kqfekiaeel kgteqeligl lqarekevhd
      481 leiqltaitt seqyyskevk dlktelenek lknteltshc nklslenkel tqetsdmtle
      541 lknqqedinn nkkqeermlk qienlqetet qlrneleyvr eelkqkrdev kckldkseen
      601 cnnlrkqven knkyieelqq enkalkkkgt aeskqlnvye ikvnklelel esakqkfgei
      661 tdtyqkeied kkiseenlle evekakviad eavklqkeid krcqhkiaem valmekhkhq
      721 ydkiieerds elglykskeq eqsslrasle klkreakent atlkekkdkk tqtflletpe
      781 iywkldskav psqtvsrnft svdhgiskdk rdylwtsakn tlstplpkay tvktptkpkl
      841 qqrenlnipi eeskkkrkma fefdinsdss ettdllsmvs eeetlktlyr nnnppashlc
      901 vktpkkapss lttpgstlkf gairkmredr waviakmdrk kklkeaeklf v
//
LOCUS       NP_001317259             489 aa            linear   PRI 21-NOV-2025
DEFINITION  luc7-like protein 3 isoform 2 [Homo sapiens].
ACCESSION   NP_001317259 XP_005257505
VERSION     NP_001317259.1
DBSOURCE    REFSEQ: accession NM_001330330.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Daniels,N.J., Hershberger,C.E., Gu,X., Schueger,C.,
            DiPasquale,W.M., Brick,J., Saunthararajah,Y., Maciejewski,J.P. and
            Padgett,R.A.
  TITLE     Functional analyses of human LUC7-like proteins involved in
            splicing regulation and myeloid neoplasms
  JOURNAL   Cell Rep 35 (2), 108989 (2021)
   PUBMED   33852859
  REMARK    GeneRIF: Functional analyses of human LUC7-like proteins involved
            in splicing regulation and myeloid neoplasms.
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Szlavicz,E., Olah,P., Szabo,K., Pagani,F., Bata-Csorgo,Z.,
            Kemeny,L. and Szell,M.
  TITLE     Analysis of psoriasis-relevant gene expression and exon usage
            alterations after silencing of SR-rich splicing regulators
  JOURNAL   Exp Dermatol 27 (6), 656-662 (2018)
   PUBMED   29512856
  REMARK    GeneRIF: In our present RNA-Seq experiment, we demonstrated that
            the LUC7L3 and SFRS18 splicing factors contribute to the regulation
            of several well-known psoriasis-associated pathways, including the
            IFN signalling pathway, antiviral immunity and ubiquitination.
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Szlavicz,E., Szabo,K., Groma,G., Bata-Csorgo,Z., Pagani,F.,
            Kemeny,L. and Szell,M.
  TITLE     Splicing factors differentially expressed in psoriasis alter mRNA
            maturation of disease-associated EDA+ fibronectin
  JOURNAL   Mol Cell Biochem 436 (1-2), 189-199 (2017)
   PUBMED   28589370
  REMARK    GeneRIF: results indicate that LUC7L3, PPIG, and SFRS18 are not
            only implicated in EDA+ fibronectin formation, but also that they
            could possess multiple roles in psoriasis-associated molecular
            abnormalities.
            Erratum:[Mol Cell Biochem. 2017 Dec;436(1-2):201. doi:
            10.1007/s11010-017-3105-y. PMID: 28770468]
REFERENCE   6  (residues 1 to 489)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 489)
  AUTHORS   Umehara,H., Nishii,Y., Morishima,M., Kakehi,Y., Kioka,N.,
            Amachi,T., Koizumi,J., Hagiwara,M. and Ueda,K.
  TITLE     Effect of cisplatin treatment on speckled distribution of a
            serine/arginine-rich nuclear protein CROP/Luc7A
  JOURNAL   Biochem Biophys Res Commun 301 (2), 324-329 (2003)
   PUBMED   12565863
  REMARK    GeneRIF: These results suggest that cisplatin affects RNA splicing
            by changing the subnuclear distribution of proteins including
            cisplatin resistance-associated overexpressed protein (CROP).
REFERENCE   8  (residues 1 to 489)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   9  (residues 1 to 489)
  AUTHORS   Chin,L.S., Singh,S.K., Wang,Q. and Murray,S.F.
  TITLE     Identification of okadaic-acid-induced genes by mRNA differential
            display in glioma cells
  JOURNAL   J Biomed Sci 7 (2), 152-159 (2000)
   PUBMED   10754390
REFERENCE   10 (residues 1 to 489)
  AUTHORS   Nishii,Y., Morishima,M., Kakehi,Y., Umehara,K., Kioka,N.,
            Terano,Y., Amachi,T. and Ueda,K.
  TITLE     CROP/Luc7A, a novel serine/arginine-rich nuclear protein, isolated
            from cisplatin-resistant cell line
  JOURNAL   FEBS Lett 465 (2-3), 153-156 (2000)
   PUBMED   10631324
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA218563.1, BC047043.1,
            AK225980.1 and AC005921.3.
            
            On Aug 23, 2016 this sequence version replaced XP_005257505.1.
            
            Summary: This gene encodes a protein with an N-terminal half that
            contains cysteine/histidine motifs and leucine zipper-like repeats,
            and the C-terminal half is rich in arginine and glutamate residues
            (RE domain) and arginine and serine residues (RS domain). This
            protein localizes with a speckled pattern in the nucleus, and could
            be involved in the formation of splicesome via the RE and RS
            domains. Two alternatively spliced transcript variants encoding the
            same protein have been found for this gene. [provided by RefSeq,
            Aug 2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.75338.1,
                                           SRR1803615.107547.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.33"
     Protein         1..489
                     /product="luc7-like protein 3 isoform 2"
                     /note="LUC7-like 3; luc7-like protein 3; CRE-associated
                     protein 1; cAMP regulatory element-associated protein 1;
                     okadaic acid-inducible phosphoprotein OA48-18; cisplatin
                     resistance-associated-overexpressed protein"
                     /calculated_mol_wt=58089
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O95232.2)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O95232.2)"
     Region          4..246
                     /region_name="LUC7"
                     /note="LUC7 N_terminus; pfam03194"
                     /db_xref="CDD:460842"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95232.2)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95232.2)"
     Site            231
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O95232.2)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O95232.2)"
     Site            425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O95232.2)"
     CDS             1..489
                     /gene="LUC7L3"
                     /gene_synonym="CRA; CREAP-1; CROP; hLuc7A; LUC7A; OA48-18"
                     /coded_by="NM_001330330.2:131..1600"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82158.1"
                     /db_xref="GeneID:51747"
                     /db_xref="HGNC:HGNC:24309"
                     /db_xref="MIM:609434"
ORIGIN      
        1 misaaqllde lmgrdrnlap dekrsnvrwd hesvckyylc gfcpaelftn trsdlgpcek
       61 ihdenlrkqy ekssrfmkvg yerdflrylq sllaeverri rrgharlals qnqqssgaag
      121 ptgkneekiq vltdkidvll qqieelgseg kveeaqgmmk lveqlkeere llrsttstie
      181 sfaaqekqme vcevcgafli vgdaqsrvdd hlmgkqhmgy akikatveel keklrkrtee
      241 pdrderlkke kqereereke rerereerer krrreeeere kerardrerr krsrsrsrhs
      301 srtsdrrcsr srdhkrsrsr errrsrsrdr rrsrshdrse rkhrsrsrdr rrsksrdrks
      361 ykhrsksrdr eqdrkskeke krgsddkkss vksgsrekqs edtnteskes dtknevngts
      421 ediksevqrk yaqmkmelsr vrrhtkasse gkdsvvlqni lryivlsqlf csrlvpplvc
      481 lfgnyrphl
//
LOCUS       NP_001357905             594 aa            linear   PRI 21-NOV-2025
DEFINITION  la-related protein 7 isoform 4 [Homo sapiens].
ACCESSION   NP_001357905
VERSION     NP_001357905.1
DBSOURCE    REFSEQ: accession NM_001370976.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Kao,T.L., Huang,Y.C., Chen,Y.H., Baumann,P. and Tseng,C.K.
  TITLE     LARP3, LARP7, and MePCE are involved in the early stage of human
            telomerase RNA biogenesis
  JOURNAL   Nat Commun 15 (1), 5955 (2024)
   PUBMED   39009594
  REMARK    GeneRIF: LARP3, LARP7, and MePCE are involved in the early stage of
            human telomerase RNA biogenesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 594)
  AUTHORS   Yan,P., Li,Z., Xiong,J., Geng,Z., Wei,W., Zhang,Y., Wu,G.,
            Zhuang,T., Tian,X., Liu,Z., Liu,J., Sun,K., Chen,F., Zhang,Y.,
            Zeng,C., Huang,Y. and Zhang,B.
  TITLE     LARP7 ameliorates cellular senescence and aging by allosterically
            enhancing SIRT1 deacetylase activity
  JOURNAL   Cell Rep 37 (8), 110038 (2021)
   PUBMED   34818543
  REMARK    GeneRIF: LARP7 ameliorates cellular senescence and aging by
            allosterically enhancing SIRT1 deacetylase activity.
REFERENCE   6  (residues 1 to 594)
  AUTHORS   Xue,Y., Yang,Z., Chen,R. and Zhou,Q.
  TITLE     A capping-independent function of MePCE in stabilizing 7SK snRNA
            and facilitating the assembly of 7SK snRNP
  JOURNAL   Nucleic Acids Res 38 (2), 360-369 (2010)
   PUBMED   19906723
REFERENCE   7  (residues 1 to 594)
  AUTHORS   Markert,A., Grimm,M., Martinez,J., Wiesner,J., Meyerhans,A.,
            Meyuhas,O., Sickmann,A. and Fischer,U.
  TITLE     The La-related protein LARP7 is a component of the 7SK
            ribonucleoprotein and affects transcription of cellular and viral
            polymerase II genes
  JOURNAL   EMBO Rep 9 (6), 569-575 (2008)
   PUBMED   18483487
  REMARK    GeneRIF: Results suggest that LARP7 is a negative transcriptional
            regulator of polymerase II genes, acting by means of the 7SK RNP
            system.
REFERENCE   8  (residues 1 to 594)
  AUTHORS   Krueger,B.J., Jeronimo,C., Roy,B.B., Bouchard,A., Barrandon,C.,
            Byers,S.A., Searcey,C.E., Cooper,J.J., Bensaude,O., Cohen,E.A.,
            Coulombe,B. and Price,D.H.
  TITLE     LARP7 is a stable component of the 7SK snRNP while P-TEFb, HEXIM1
            and hnRNP A1 are reversibly associated
  JOURNAL   Nucleic Acids Res 36 (7), 2219-2229 (2008)
   PUBMED   18281698
  REMARK    GeneRIF: Results indicate LARP7 is a 7SK-binding protein.
REFERENCE   9  (residues 1 to 594)
  AUTHORS   He,N., Jahchan,N.S., Hong,E., Li,Q., Bayfield,M.A., Maraia,R.J.,
            Luo,K. and Zhou,Q.
  TITLE     A La-related protein modulates 7SK snRNP integrity to suppress
            P-TEFb-dependent transcriptional elongation and tumorigenesis
  JOURNAL   Mol Cell 29 (5), 588-599 (2008)
   PUBMED   18249148
  REMARK    GeneRIF: Results identify PIP7S as a La-related protein stably
            associated with and required for 7SK snRNP integrity.
REFERENCE   10 (residues 1 to 594)
  AUTHORS   Biewenga,P., Buist,M.R., Moerland,P.D., Ver Loren van Themaat,E.,
            van Kampen,A.H., ten Kate,F.J. and Baas,F.
  TITLE     Gene expression in early stage cervical cancer
  JOURNAL   Gynecol Oncol 108 (3), 520-526 (2008)
   PUBMED   18191186
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106864.5.
            
            Summary: This gene encodes a protein which is found in the 7SK
            snRNP (small nuclear ribonucleoprotein). This snRNP complex
            inhibits a cyclin-dependent kinase, positive transcription
            elongation factor b, which is required for paused RNA polymerase II
            at a promoter to begin transcription elongation. A pseudogene of
            this gene is located on chromosome 3. Alternative splicing results
            in multiple transcript variants. [provided by RefSeq, May 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.1459513.1,
                                           SRR14038194.4433134.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..594
                     /product="la-related protein 7 isoform 4"
                     /note="P-TEFb-interaction protein for 7SK stability;
                     La-related protein 7; La ribonucleoprotein domain family
                     member 7"
                     /calculated_mol_wt=68135
     Region          30..111
                     /region_name="LARP_7"
                     /note="La RNA-binding domain of La-related protein 7;
                     cd08032"
                     /db_xref="CDD:153401"
     Site            order(41,44..45,50,53..54,56,77..79)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153401"
     Region          126..205
                     /region_name="RRM1_LARP7"
                     /note="RNA recognition motif 1 (RRM1) found in La-related
                     protein 7 (LARP7) and similar proteins; cd12290"
                     /db_xref="CDD:409732"
     Region          466..547
                     /region_name="RRM2_LARP7"
                     /note="RNA recognition motif 2 in La-related protein 7
                     (LARP7) and similar proteins; cd12542"
                     /db_xref="CDD:409958"
     CDS             1..594
                     /gene="LARP7"
                     /gene_synonym="ALAZS; HDCMA18P; hLARP7; PIP7S"
                     /coded_by="NM_001370976.1:100..1884"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS93569.1"
                     /db_xref="GeneID:51574"
                     /db_xref="HGNC:HGNC:24912"
                     /db_xref="MIM:612026"
ORIGIN      
        1 metesgnqek vmeeestekk kevekkkrsr vkqvladiak qvdfwfgdan lhkdrflreq
       61 ieksrdgyvd isllvsfnkm kklttdgkli aralrssavv eldlegtrir rkkplgerpk
      121 dedertvyve llpknvnhsw iervfgkcgn vvyisiphyk stgdpkgfaf vefetkeqaa
      181 kaieflnnpp eeaprkpgif pktvknkpip alrvvekkkk kkkkgrmkke dniqakeenm
      241 dtsntsiskm krsrptsegs diestepqkq cskkkkkrdr veasslpevr tgkrkrssse
      301 daeslaprsk vkkiiqkdii keaseasken rapclngelf ylfqdieist eeekdtgdlk
      361 dssllktkrk hkkkhkerhk mgeeviplrv lsksewmdlk keylalqkas maslkktisq
      421 iksesemetd sgvpqntgmk nektanreec rtqekvnatg pqfvsgvivk iisteplpgr
      481 kqvrdtlaai sevlyvdlle gdtecharfk tpedaqavin ayteinkkhc wkleilsgdh
      541 eqrywqkilv drqaklnqpr ekkrgtekli tkaekirlak tqqaskhirf seyd
//
LOCUS       NP_001305461             108 aa            linear   PRI 21-NOV-2025
DEFINITION  trafficking protein particle complex subunit 2-like protein isoform
            9 [Homo sapiens].
ACCESSION   NP_001305461
VERSION     NP_001305461.1
DBSOURCE    REFSEQ: accession NM_001318532.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Abaji,M., Mignon-Ravix,C., Gorokhova,S., Cacciagli,P., Mortreux,J.,
            Molinari,F., Chabrol,B., Sigaudy,S., Villard,L. and Riccardi,F.
  TITLE     TRAPPC2L-related disorder: first homozygous protein-truncating
            variant and further delineation of the phenotype
  JOURNAL   J Med Genet 60 (10), 1021-1025 (2023)
   PUBMED   36849228
  REMARK    GeneRIF: TRAPPC2L-related disorder: first homozygous
            protein-truncating variant and further delineation of the
            phenotype.
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Al-Deri,N., Okur,V., Ahimaz,P., Milev,M., Valivullah,Z., Hagen,J.,
            Sheng,Y., Chung,W., Sacher,M. and Ganapathi,M.
  TITLE     A novel homozygous variant in TRAPPC2L results in a
            neurodevelopmental disorder and disrupts TRAPP complex function
  JOURNAL   J Med Genet 58 (9), 592-601 (2021)
   PUBMED   32843486
  REMARK    GeneRIF: A novel homozygous variant in TRAPPC2L results in a
            neurodevelopmental disorder and disrupts TRAPP complex function.
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Scrivens,P.J., Noueihed,B., Shahrzad,N., Hul,S., Brunet,S. and
            Sacher,M.
  TITLE     C4orf41 and TTC-15 are mammalian TRAPP components with a role at an
            early stage in ER-to-Golgi trafficking
  JOURNAL   Mol Biol Cell 22 (12), 2083-2093 (2011)
   PUBMED   21525244
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Choi,C., Davey,M., Schluter,C., Pandher,P., Fang,Y., Foster,L.J.
            and Conibear,E.
  TITLE     Organization and assembly of the TRAPPII complex
  JOURNAL   Traffic 12 (6), 715-725 (2011)
   PUBMED   21453443
REFERENCE   8  (residues 1 to 108)
  AUTHORS   Westlake,C.J., Baye,L.M., Nachury,M.V., Wright,K.J., Ervin,K.E.,
            Phu,L., Chalouni,C., Beck,J.S., Kirkpatrick,D.S., Slusarski,D.C.,
            Sheffield,V.C., Scheller,R.H. and Jackson,P.K.
  TITLE     Primary cilia membrane assembly is initiated by Rab11 and transport
            protein particle II (TRAPPII) complex-dependent trafficking of
            Rabin8 to the centrosome
  JOURNAL   Proc Natl Acad Sci U S A 108 (7), 2759-2764 (2011)
   PUBMED   21273506
REFERENCE   9  (residues 1 to 108)
  AUTHORS   Garcia,S.A. and Nagai,M.A.
  TITLE     Transcriptional regulation of bidirectional gene pairs by
            17-beta-estradiol in MCF-7 breast cancer cells
  JOURNAL   Braz J Med Biol Res 44 (2), 112-122 (2011)
   PUBMED   21180879
REFERENCE   10 (residues 1 to 108)
  AUTHORS   Scrivens,P.J., Shahrzad,N., Moores,A., Morin,A., Brunet,S. and
            Sacher,M.
  TITLE     TRAPPC2L is a novel, highly conserved TRAPP-interacting protein
  JOURNAL   Traffic 10 (6), 724-736 (2009)
   PUBMED   19416478
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA209193.1, AK310805.1,
            BC011369.1 and BC017440.1.
            
            Summary: This gene encodes a protein that interacts with the
            tethering factor trafficking protein particle (TRAPP complex).
            TRAPP complexes mediate the contact between vescicles and target
            membranes, and thus, are involved in vescicle-mediated transport of
            proteins and lipids. The encoded protein is related to the X-linked
            trafficking protein particle complex 2. A related pseudogene is
            located on the X chromosome. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (9) differs in the 5' UTR and 5'
            coding region, uses an alternate start codon and uses an alternate
            in-frame splice site in the 3' coding region, compared to variant
            1. It encodes isoform 9, which is shorter and has a distinct
            N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.9930.1,
                                           SRR1660809.153969.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..108
                     /product="trafficking protein particle complex subunit
                     2-like protein isoform 9"
                     /note="hematopoietic stem/progenitor cells 176;
                     trafficking protein particle complex subunit 2-like
                     protein; trafficking protein particle complex 2 like"
                     /calculated_mol_wt=12091
     Region          <39..104
                     /region_name="longin-like"
                     /note="Longin-like domains; cl38905"
                     /db_xref="CDD:365781"
     CDS             1..108
                     /gene="TRAPPC2L"
                     /gene_synonym="HSPC176; PERRB"
                     /coded_by="NM_001318532.2:434..760"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:51693"
                     /db_xref="HGNC:HGNC:30887"
                     /db_xref="MIM:610970"
ORIGIN      
        1 mgiscdsrlp hfskvrahrg pstgspcvts afpnqlcryg yvtnskvkfv mvvdssntal
       61 rdneirsmfr klhnsytdvm cnpfynpgdr iqsrafdnmv tsmmiqvc
//
LOCUS       NP_569707               1898 aa            linear   PRI 21-NOV-2025
DEFINITION  receptor-type tyrosine-protein phosphatase F isoform 2 precursor
            [Homo sapiens].
ACCESSION   NP_569707
VERSION     NP_569707.2
DBSOURCE    REFSEQ: accession NM_130440.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1898)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   2  (residues 1 to 1898)
  AUTHORS   Nguyen,M.Q., Taniguchi,M., Yasumura,M., Iguchi,T. and Sato,M.
  TITLE     Cytoneme-like protrusion formation induced by LAR is promoted by
            receptor dimerization
  JOURNAL   Biol Open 11 (7) (2022)
   PUBMED   35735010
  REMARK    GeneRIF: Cytoneme-like protrusion formation induced by LAR is
            promoted by receptor dimerization.
REFERENCE   3  (residues 1 to 1898)
  AUTHORS   Gan,T., Stevens,A.T., Xiong,X., Wen,Y.A., Farmer,T.N., Li,A.T.,
            Stevens,P.D., Golshani,S., Weiss,H.L., Evers,B.M. and Gao,T.
  TITLE     Inhibition of protein tyrosine phosphatase receptor type F
            suppresses Wnt signaling in colorectal cancer
  JOURNAL   Oncogene 39 (44), 6789-6801 (2020)
   PUBMED   32973331
  REMARK    GeneRIF: Inhibition of protein tyrosine phosphatase receptor type F
            suppresses Wnt signaling in colorectal cancer.
REFERENCE   4  (residues 1 to 1898)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   5  (residues 1 to 1898)
  AUTHORS   Vilstrup,J., Simonsen,A., Birkefeldt,T., Strandbygard,D.,
            Lyngso,J., Pedersen,J.S. and Thirup,S.
  TITLE     Crystal and solution structures of fragments of the human leucocyte
            common antigen-related protein
  JOURNAL   Acta Crystallogr D Struct Biol 76 (Pt 5), 406-417 (2020)
   PUBMED   32355037
  REMARK    GeneRIF: Crystal and solution structures of fragments of the human
            leucocyte common antigen-related protein.
REFERENCE   6  (residues 1 to 1898)
  AUTHORS   Hashimoto,N., Feener,E.P., Zhang,W.R. and Goldstein,B.J.
  TITLE     Insulin receptor protein-tyrosine phosphatases. Leukocyte common
            antigen-related phosphatase rapidly deactivates the insulin
            receptor kinase by preferential dephosphorylation of the receptor
            regulatory domain
  JOURNAL   J Biol Chem 267 (20), 13811-13814 (1992)
   PUBMED   1321126
REFERENCE   7  (residues 1 to 1898)
  AUTHORS   Jirik,F.R., Harder,K.W., Melhado,I.G., Anderson,L.L. and
            Duncan,A.M.
  TITLE     The gene for leukocyte antigen-related tyrosine phosphatase (LAR)
            is localized to human chromosome 1p32, a region frequently deleted
            in tumors of neuroectodermal origin
  JOURNAL   Cytogenet Cell Genet 61 (4), 266-268 (1992)
   PUBMED   1486801
REFERENCE   8  (residues 1 to 1898)
  AUTHORS   Streuli,M., Krueger,N.X., Thai,T., Tang,M. and Saito,H.
  TITLE     Distinct functional roles of the two intracellular phosphatase like
            domains of the receptor-linked protein tyrosine phosphatases LCA
            and LAR
  JOURNAL   EMBO J 9 (8), 2399-2407 (1990)
   PUBMED   1695146
REFERENCE   9  (residues 1 to 1898)
  AUTHORS   Streuli,M., Krueger,N.X., Tsai,A.Y. and Saito,H.
  TITLE     A family of receptor-linked protein tyrosine phosphatases in humans
            and Drosophila
  JOURNAL   Proc Natl Acad Sci U S A 86 (22), 8698-8702 (1989)
   PUBMED   2554325
REFERENCE   10 (residues 1 to 1898)
  AUTHORS   Streuli,M., Krueger,N.X., Hall,L.R., Schlossman,S.F. and Saito,H.
  TITLE     A new member of the immunoglobulin superfamily that has a
            cytoplasmic region homologous to the leukocyte common antigen
  JOURNAL   J Exp Med 168 (5), 1523-1530 (1988)
   PUBMED   2972792
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Y00815.1, BC048768.1,
            AC092815.2 and BU624266.1.
            
            On Jun 23, 2006 this sequence version replaced NP_569707.1.
            
            Summary: The protein encoded by this gene is a member of the
            protein tyrosine phosphatase (PTP) family. PTPs are known to be
            signaling molecules that regulate a variety of cellular processes
            including cell growth, differentiation, mitotic cycle, and
            oncogenic transformation. This PTP possesses an extracellular
            region, a single transmembrane region, and two tandem
            intracytoplasmic catalytic domains, and thus represents a
            receptor-type PTP. The extracellular region contains three Ig-like
            domains, and nine non-Ig like domains similar to that of
            neural-cell adhesion molecule. This PTP was shown to function in
            the regulation of epithelial cell-cell contacts at adherents
            junctions, as well as in the control of beta-catenin signaling. An
            increased expression level of this protein was found in the
            insulin-responsive tissue of obese, insulin-resistant individuals,
            and may contribute to the pathogenesis of insulin resistance. Two
            alternatively spliced transcript variants of this gene, which
            encode distinct proteins, have been reported. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region compared to variant 1. The encoded
            isoform (2) is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB177857.1, BC048768.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1898
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.2"
     Protein         1..1898
                     /product="receptor-type tyrosine-protein phosphatase F
                     isoform 2 precursor"
                     /EC_number="3.1.3.48"
                     /note="leukocyte antigen-related (LAR) PTP receptor;
                     receptor-linked protein-tyrosine phosphatase LAR;
                     LCA-homolog; leukocyte antigen-related tyrosine
                     phosphatase; protein tyrosine phosphatase, receptor type,
                     F polypeptide; leukocyte common antigen related"
                     /calculated_mol_wt=208852
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2854
     Region          33..124
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          50..54
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          63..67
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          86..93
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          104..109
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          117..120
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            117
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10586.2)"
     Region          136..226
                     /region_name="IgI_2_RPTP_IIa_LAR_like"
                     /note="Second immunoglobulin (Ig)-like domain of the
                     receptor protein tyrosine phosphatase (RPTP)-F; member of
                     the I-set of IgSF domains; cd05738"
                     /db_xref="CDD:409400"
     Region          136..138
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409400"
     Region          143..147
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409400"
     Region          150..159
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409400"
     Region          164..170
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409400"
     Region          172..174
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409400"
     Region          183..187
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409400"
     Region          190..195
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409400"
     Region          204..211
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409400"
     Region          214..225
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409400"
     Region          235..316
                     /region_name="IgI_3_RPTP_IIa_LAR_like"
                     /note="Third immunoglobulin (Ig)-like domain of the
                     receptor protein tyrosine phosphatase (RPTP)-F (also known
                     as LAR), type IIa; member of the I-set of IgSF domains;
                     cd05739"
                     /db_xref="CDD:409401"
     Region          235..237
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409401"
     Region          241..245
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409401"
     Region          248..256
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409401"
     Site            250
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10586.2)"
     Region          261..267
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409401"
     Region          269..271
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409401"
     Region          274..278
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409401"
     Region          283..288
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409401"
     Region          295..302
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409401"
     Site            295
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10586.2)"
     Region          306..315
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409401"
     Region          <307..712
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          398..417
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10586.2)"
     Region          559..988
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          693..712
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10586.2)"
     Site            721
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10586.2)"
     Site            957
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P10586.2)"
     Region          1007..>1066
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            1255..1275
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P10586.2)"
     Site            1296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P10586.2)"
     Region          1326..1601
                     /region_name="R-PTPc-F-1"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase F, repeat 1; cd14626"
                     /db_xref="CDD:350474"
     Region          1603..1893
                     /region_name="R-PTP-F-2"
                     /note="PTP-like domain of receptor-type tyrosine-protein
                     phosphatase F, repeat 2; cd14629"
                     /db_xref="CDD:350477"
     CDS             1..1898
                     /gene="PTPRF"
                     /gene_synonym="BNAH2; LAR"
                     /coded_by="NM_130440.4:334..6030"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS490.2"
                     /db_xref="GeneID:5792"
                     /db_xref="HGNC:HGNC:9670"
                     /db_xref="MIM:179590"
ORIGIN      
        1 mapepapgrt mvplvpalvm lglvagahgd skpvfikvpe dqtglsggva sfvcqatgep
       61 kpritwmkkg kkvssqrfev iefddgagsv lriqplrvqr deaiyectat nslgeintsa
      121 klsvleeeql ppgfpsidmg pqlkvvekar tatmlcaagg npdpeiswfk dflpvdpats
      181 ngrikqlrsg alqiessees dqgkyecvat nsagtrysap anlyvrvrrv aprfsippss
      241 qevmpggsvn ltcvavgapm pyvkwmmgae eltkedempv grnvlelsnv vrsanytcva
      301 isslgmieat aqvtvkalpk ppidlvvtet tatsvtltwd sgnsepvtyy giqyraagte
      361 gpfqevdgva ttrysiggls pfseyafrvl avnsigrgpp seavrartge qapsspprrv
      421 qarmlsastm lvqweppeep nglvrgyrvy ytpdsrrppn awhkhntdag llttvgsllp
      481 gityslrvla ftavgdgpps ptiqvktqqg vpaqpadfqa evesdtriql swllppqeri
      541 imyelvywaa ededqqhkvt fdptssytle dlkpdtlyrf qlaarsdmgv gvftptiear
      601 taqstpsapp qkvmcvsmgs ttvrvswvpp padsrngvit qysvayeavd gedrgrhvvd
      661 gisrehsswd lvglekwtey rvwvrahtdv gpgpesspvl vrtdedvpsg pprkvevepl
      721 nstavhvywk lpvpskqhgq irgyqvtyvr lengeprglp iiqdvmlaea qettisgltp
      781 ettysvtvaa yttkgdgars kpkivtttga vpgrptmmis ttamntallq whppkelpge
      841 llgyrlqycr adearpntid fgkddqhftv tglhkgttyi frlaaknrag lgeefekeir
      901 tpedlpsgfp qnlhvtgltt sttelawdpp vlaerngrii sytvvfrdin sqqelqnitt
      961 dtrftltglk pdttydikvr awtskgsgpl spsiqsrtmp veqvfaknfr vaaamktsvl
     1021 lswevpdsyk savpfkilyn gqsvevdghs mrkliadlqp nteysfvlmn rgssagglqh
     1081 lvsirtapdl lphkplpasa yiedgrfdls mphvqdpslv rwfyivvvpi drvggsmltp
     1141 rwstpeelel delleaieqg geeqrrrrrq aerlkpyvaa qldvlpetft lgdkknyrgf
     1201 ynrplspdls yqcfvlaslk epmdqkryas spysdeivvq vtpaqqqeep emlwvtgpvl
     1261 aviliilivi aillfkrkrt hspsskdeqs iglkdsllah ssdpvemrrl nyqtpgmrdh
     1321 ppipitdlad nierlkandg lkfsqeyesi dpgqqftwen snlevnkpkn ryanviaydh
     1381 srviltsidg vpgsdyinan yidgyrkqna yiatqgplpe tmgdfwrmvw eqrtatvvmm
     1441 trleeksrvk cdqywpargt etcgliqvtl ldtvelatyt vrtfalhksg ssekrelrqf
     1501 qfmawpdhgv peyptpilaf lrrvkacnpl dagpmvvhcs agvgrtgcfi vidamlermk
     1561 hektvdiygh vtcmrsqrny mvqtedqyvf ihealleaat cghtevparn lyahiqklgq
     1621 vppgesvtam elefkllass kahtsrfisa nlpcnkfknr lvnimpyelt rvclqpirgv
     1681 egsdyinasf ldgyrqqkay iatqgplaes tedfwrmlwe hnstiivmlt klremgrekc
     1741 hqywpaersa ryqyfvvdpm aeynmpqyil refkvtdard gqsrtirqfq ftdwpeqgvp
     1801 ktgegfidfi gqvhktkeqf gqdgpitvhc sagvgrtgvf itlsivlerm ryegvvdmfq
     1861 tvktlrtqrp amvqtedqyq lcyraaleyl gsfdhyat
//
LOCUS       NP_001239322             635 aa            linear   PRI 21-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001239322
VERSION     NP_001239322.1
DBSOURCE    REFSEQ: accession NM_001252393.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 635)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 635)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 635)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 635)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 635)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 635)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 635)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 635)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB252973.1, AK074400.1 and
            AW589284.1.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Transcript Variant: This variant (7) uses two alternate splice
            sites in the 3' coding region, compared to variant 1. The resulting
            isoform (4) is longer and contains a distinct C-terminus, compared
            to isoform 1. Variants 6 and 7 encode the same protein (isoform 4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB252973.1, SRR14038196.3559381.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..635
                     /product="TNFAIP3-interacting protein 1 isoform 4"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=71657
     Region          14..>149
                     /region_name="Speriolin_N"
                     /note="Speriolin N terminus; pfam15058"
                     /db_xref="CDD:434426"
     Region          61..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          94..412
                     /region_name="Interaction with Nef"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Region          <214..>251
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          252..283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          <298..>538
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          351..367
                     /region_name="Interaction with Shigella flexneri ipah9.8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          431..588
                     /region_name="Required for inhibitory activity of
                     TNF-induced NF-kappa-B activation. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          452..510
                     /region_name="Ubiquitin-binding domain (UBD)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Region          524..530
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            552
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17632516; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            571
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9WUU8; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            599
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     CDS             1..635
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001252393.2:192..2099"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS58985.1"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 megrgpyriy dpggsvpsge asaaferlvk ensrlkekmq gikmlgelle esqmeatrlr
       61 qkaeelvkdn ellpppspsl gsfdplaelt gkdsnvtasp tapacpsdkp apvqkppssg
      121 tssefevvtp eeqnspesss hanamalgpl predgnlmlh lqrlettlsv caeepdhgql
      181 fthlgrmale fnrlaskvhk neqrtsilqt lceqlrkene alkakldkgl eqrdqaaerl
      241 reenlelkkl lmsngnkega sgrpgspkme gtgkkavagq qqasvtagkv pevvalgaae
      301 kkvkmleqqr sellevnkqw dqhfrsmkqq yeqkitelrq kladlqkqvt dleaereqkq
      361 rdfdrkllla kskiemeetd keqltaeake lrqkvkylqd qlspltrqre yqekeiqrln
      421 kaleealsiq tppsspptaf gspegagall rkqelvtqne llkqqvkife edfqrersdr
      481 ermneekeel kkqveklqaq vtlsnaqlka fkdeekarea lrqqkrkaka sgeryhveph
      541 pehlcgaypy ayppmpamvp hhgfedwsqi ryppppmame hppplpnsrl fhlpeytwrl
      601 pcggvrnpnq ssqvmdppta rptepepadl rlprn
//
LOCUS       NP_001003678             326 aa            linear   PRI 21-NOV-2025
DEFINITION  centriolar satellite-associated tubulin polyglutamylase complex
            regulator 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001003678
VERSION     NP_001003678.1
DBSOURCE    REFSEQ: accession NM_001003678.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Wang,L., Paudyal,S.C., Kang,Y., Owa,M., Liang,F.X., Spektor,A.,
            Knaut,H., Sanchez,I. and Dynlacht,B.D.
  TITLE     Regulators of tubulin polyglutamylation control nuclear shape and
            cilium disassembly by balancing microtubule and actin assembly
  JOURNAL   Cell Res 32 (2), 190-209 (2022)
   PUBMED   34782749
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   6  (residues 1 to 326)
  AUTHORS   He,L., Wu,W.J., Yang,J.K., Cheng,H., Zuo,X.B., Lai,W., Gao,T.W.,
            Ma,C.L., Luo,N., Huang,J.Q., Lu,F.Y., Liu,Y.Q., Huang,Y.J.,
            Lu,Q.J., Zhang,H.L., Wang,L., Wang,W.Z., Wang,M.M., Xiao,S.X.,
            Sun,Q., Li,C.Y., Bai,Y.P., Li,H., Zhou,Z.C., Zhou,F.S., Chen,G.,
            Liang,B., Qi,J., Yang,X.Y., Yang,T., Zheng,X., Sun,L.D., Zhang,X.J.
            and Zhang,Y.P.
  TITLE     Two new susceptibility loci 1q24.2 and 11p11.2 confer risk to
            severe acne
  JOURNAL   Nat Commun 5, 2870 (2014)
   PUBMED   24399259
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Smith,N.L., Huffman,J.E., Strachan,D.P., Huang,J., Dehghan,A.,
            Trompet,S., Lopez,L.M., Shin,S.Y., Baumert,J., Vitart,V., Bis,J.C.,
            Wild,S.H., Rumley,A., Yang,Q., Uitterlinden,A.G., Stott,D.J.,
            Davies,G., Carter,A.M., Thorand,B., Polasek,O., McKnight,B.,
            Campbell,H., Rudnicka,A.R., Chen,M.H., Buckley,B.M., Harris,S.E.,
            Peters,A., Pulanic,D., Lumley,T., de Craen,A.J., Liewald,D.C.,
            Gieger,C., Campbell,S., Ford,I., Gow,A.J., Luciano,M.,
            Porteous,D.J., Guo,X., Sattar,N., Tenesa,A., Cushman,M.,
            Slagboom,P.E., Visscher,P.M., Spector,T.D., Illig,T., Rudan,I.,
            Bovill,E.G., Wright,A.F., McArdle,W.L., Tofler,G., Hofman,A.,
            Westendorp,R.G., Starr,J.M., Grant,P.J., Karakas,M., Hastie,N.D.,
            Psaty,B.M., Wilson,J.F., Lowe,G.D., O'Donnell,C.J., Witteman,J.C.,
            Jukema,J.W., Deary,I.J., Soranzo,N., Koenig,W. and Hayward,C.
  TITLE     Genetic predictors of fibrin D-dimer levels in healthy adults
  JOURNAL   Circulation 123 (17), 1864-1872 (2011)
   PUBMED   21502573
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Kitazawa,H., Iida,J., Uchida,A., Haino-Fukushima,K., Itoh,T.J.,
            Hotani,H., Ookata,K., Murofushi,H., Bulinski,J.C., Kishimoto,T. and
            Hisanaga,S.
  TITLE     Ser787 in the proline-rich region of human MAP4 is a critical
            phosphorylation site that reduces its activity to promote tubulin
            polymerization
  JOURNAL   Cell Struct Funct 25 (1), 33-39 (2000)
   PUBMED   10791892
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB027437.1, CK724853.1, BU728094.1 and AC090589.9.
            
            Transcript Variant: This variant (4) has an alternate 3' terminal
            exon, compared to variant 2. The resulting isoform (4) has a
            shorter and distinct C-terminus, compared to isoform 2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.92103.1,
                                           SRR5189667.39715.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..326
                     /product="centriolar satellite-associated tubulin
                     polyglutamylase complex regulator 1 isoform 4"
                     /note="UPF0705 protein C11orf49; centriolar
                     satellite-associated tubulin polyglutamylation protein 1"
                     /calculated_mol_wt=37400
     Region          1..225
                     /region_name="Required for interaction with TPGS1, LRRC49,
                     and TTLL1. /evidence=ECO:0000269|PubMed:34782749"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6J7.2)"
     Region          1..111
                     /region_name="Required for interaction with PCM1.
                     /evidence=ECO:0000269|PubMed:34782749"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6J7.2)"
     Region          13..68
                     /region_name="DD_C11orf49"
                     /note="dimerization/docking (D/D) domain found in UPF0705
                     protein C11orf49 and similar proteins; cd22959"
                     /db_xref="CDD:438528"
     CDS             1..326
                     /gene="CSTPP1"
                     /gene_synonym="C11orf49"
                     /coded_by="NM_001003678.3:46..1026"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS31479.1"
                     /db_xref="GeneID:79096"
                     /db_xref="HGNC:HGNC:28720"
                     /db_xref="MIM:620479"
ORIGIN      
        1 mlsperlalp dyeylaqrhv ltymedavcq llenredisq ygiarfftey fnsvcqgthi
       61 lfrefsfvqa tphnrvsflr afwrcfrtvg kngdlltmke yhcllqllcp dfpleltqka
      121 arivlmddam dclmsfsdfl fafqiqfyys efldsvaaiy edllsgknpn tvivptsssg
      181 qhrqrpalgg agtlegveas lfyqclenlc drhkyscppp alvkealsnv qrltfygflm
      241 alskhrginq algalpdkgd lmhdpamdee lerlvvrskl hrtsrqhrak epgafgfqrr
      301 ekqealervs sasvptpyhy rwepre
//
LOCUS       NP_001341504             606 aa            linear   PRI 21-NOV-2025
DEFINITION  leucine-rich repeat and immunoglobulin-like domain-containing nogo
            receptor-interacting protein 2 precursor [Homo sapiens].
ACCESSION   NP_001341504
VERSION     NP_001341504.1
DBSOURCE    REFSEQ: accession NM_001354575.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Huang,X., Liang,W., Yang,R., Jin,L., Zhao,K., Chen,J., Shang,X.,
            Zhou,Y., Wang,X. and Yu,H.
  TITLE     Variations in the LINGO2 and GLIS3 Genes and Gene-Environment
            Interactions Increase Gestational Diabetes Mellitus Risk in Chinese
            Women
  JOURNAL   Environ Sci Technol 58 (26), 11596-11605 (2024)
   PUBMED   38888423
  REMARK    GeneRIF: Variations in the LINGO2 and GLIS3 Genes and
            Gene-Environment Interactions Increase Gestational Diabetes
            Mellitus Risk in Chinese Women.
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Su,T., Ren,Q., Lu,Y., Tai,W., Zhu,Y., Li,Z., Wen,J., Hu,L.,
            Zhang,L. and Ma,J.
  TITLE     A genetic variant in LINGO2 contributes to the risk of gestational
            diabetes mellitus in a Chinese population
  JOURNAL   J Cell Physiol 234 (5), 7012-7018 (2019)
   PUBMED   30426492
  REMARK    GeneRIF: LINGO2 rs824248 may serve as a susceptibility marker for
            gestational diabetes mellitus in Chinese females.
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Jo,J.H., Park,S.B., Park,S., Lee,H.S., Kim,C., Jung,D.E. and
            Song,S.Y.
  TITLE     Novel Gastric Cancer Stem Cell-Related Marker LINGO2 Is Associated
            with Cancer Cell Phenotype and Patient Outcome
  JOURNAL   Int J Mol Sci 20 (3), 555 (2019)
   PUBMED   30696080
  REMARK    GeneRIF: These indicate the involvement of LINGO2 in gastric cancer
            initiation and progression by altering cell motility, stemness, and
            tumorigenicity.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 606)
  AUTHORS   Vilarino-Guell,C., Wider,C., Ross,O.A., Jasinska-Myga,B.,
            Kachergus,J., Cobb,S.A., Soto-Ortolaza,A.I., Behrouz,B.,
            Heckman,M.G., Diehl,N.N., Testa,C.M., Wszolek,Z.K., Uitti,R.J.,
            Jankovic,J., Louis,E.D., Clark,L.N., Rajput,A. and Farrer,M.J.
  TITLE     LINGO1 and LINGO2 variants are associated with essential tremor and
            Parkinson disease
  JOURNAL   Neurogenetics 11 (4), 401-408 (2010)
   PUBMED   20369371
  REMARK    GeneRIF: LINGO1 and LINGO2 variants are associated with essential
            tremor and Parkinson disease
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 606)
  AUTHORS   Ichikawa,S., Koller,D.L., Padgett,L.R., Lai,D., Hui,S.L.,
            Peacock,M., Foroud,T. and Econs,M.J.
  TITLE     Replication of previous genome-wide association studies of bone
            mineral density in premenopausal American women
  JOURNAL   J Bone Miner Res 25 (8), 1821-1829 (2010)
   PUBMED   20200978
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 606)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 606)
  AUTHORS   Carim-Todd,L., Escarceller,M., Estivill,X. and Sumoy,L.
  TITLE     LRRN6A/LERN1 (leucine-rich repeat neuronal protein 1), a novel gene
            with enriched expression in limbic system and neocortex
  JOURNAL   Eur J Neurosci 18 (12), 3167-3182 (2003)
   PUBMED   14686891
REFERENCE   10 (residues 1 to 606)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL162388.8, AL158072.9, AL592206.5, AL353683.7, AL596323.10,
            AL353746.6 and BX538226.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803614.86983.1, DN991981.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968189 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.2-p21.1"
     Protein         1..606
                     /product="leucine-rich repeat and immunoglobulin-like
                     domain-containing nogo receptor-interacting protein 2
                     precursor"
                     /note="leucine rich repeat neuronal 6C; leucine-rich
                     repeat and immunoglobulin-like domain-containing nogo
                     receptor-interacting protein 2; leucine-rich repeat
                     neuronal protein 3; leucine-rich repeat neuronal protein
                     6C"
                     /calculated_mol_wt=65178
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2907
     Region          27..60
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; smart00013"
                     /db_xref="CDD:214470"
     mat_peptide     28..606
                     /product="Leucine-rich repeat and immunoglobulin-like
                     domain-containing nogo receptor-interacting protein 2.
                     /id=PRO_0000324389"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L985.1)"
                     /calculated_mol_wt=65178
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7L985.1)"
     Region          39..57
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          48..>340
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          58..79
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L985.1)"
     Region          59..82
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          82..103
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L985.1)"
     Region          83..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          106..127
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L985.1)"
     Region          107..130
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..151
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L985.1)"
     Site            130
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7L985.1)"
     Region          131..154
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          154..175
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L985.1)"
     Region          155..178
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          178..199
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L985.1)"
     Region          179..202
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            188
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7L985.1)"
     Region          202..223
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L985.1)"
     Region          203..250
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          226..247
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L985.1)"
     Region          250..271
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L985.1)"
     Region          251..274
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          274..295
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L985.1)"
     Region          275..298
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            279
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7L985.1)"
     Region          298..319
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L985.1)"
     Region          299..322
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          322..343
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L985.1)"
     Region          323..343
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            327
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7L985.1)"
     Region          355..408
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Region          411..500
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          428..432
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          441..445
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          466..470
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          480..485
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          493..496
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            546..566
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L985.1)"
     CDS             1..606
                     /gene="LINGO2"
                     /gene_synonym="LERN3; LRRN6C"
                     /coded_by="NM_001354575.2:702..2522"
                     /db_xref="CCDS:CCDS6524.1"
                     /db_xref="GeneID:158038"
                     /db_xref="HGNC:HGNC:21207"
                     /db_xref="MIM:609793"
ORIGIN      
        1 mlhtaiscwq pflglavvli fmgstigcpa rcecsaqnks vschrrrlia ipegipietk
       61 ildlsknrlk svnpeefisy plleeidlsd niianvepga fnnlfnlrsl rlkgnrlklv
      121 plgvftglsn ltkldisenk ivilldymfq dlhnlkslev gdndlvyish rafsgllsle
      181 qltlekcnlt avptealshl rslislhlkh lninnmpvya fkrlfhlkhl eidywplldm
      241 mpanslygln ltslsvtntn lstvpflafk hlvylthlnl synpistiea gmfsdlirlq
      301 elhivgaqlr tiephsfqgl rflrvlnvsq nlletleenv fsspralevl sinnnplacd
      361 crllwilqrq ptlqfggqqp mcagpdtire rsfkdfhsta lsfyftckkp kirekklqhl
      421 lvdegqtvql ecsadgdpqp viswvtprrr fittksngra tvlgdgtlei rfaqdqdsgm
      481 yvciasnaag ndtftasltv kgfasdrfly anrtpmymtd sndtisngtn antfsldlkt
      541 ilvstamgcf tflgvvlfcf lllfvwsrgk gkhknsidle yvprknngav vegevagprr
      601 fnmkmi
//
LOCUS       NP_001273574             662 aa            linear   PRI 21-NOV-2025
DEFINITION  alpha-adducin isoform e [Homo sapiens].
ACCESSION   NP_001273574
VERSION     NP_001273574.1
DBSOURCE    REFSEQ: accession NM_001286645.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 662)
  AUTHORS   Sydorchuk,L., Lytvyn,B., Sydorchuk,A., Yarynych,Y., Daruvuri,S.P.,
            Semenenko,S., Hoshovska,A., Sydorchuk,R. and Biryuk,I.
  TITLE     Alpha-adducin 1 (rs4961) gene and its expression associated with
            sodium sensitivity in hypertensive patients: a cohort study in the
            western Ukrainian population
  JOURNAL   Endocr Regul 58 (1), 195-205 (2024)
   PUBMED   39352780
  REMARK    GeneRIF: Alpha-adducin 1 (rs4961) gene and its expression
            associated with sodium sensitivity in hypertensive patients: a
            cohort study in the western Ukrainian population.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 662)
  AUTHORS   Gonzalez-Fernandez,E., Fan,L., Wang,S., Liu,Y., Gao,W.,
            Thomas,K.N., Fan,F. and Roman,R.J.
  TITLE     The adducin saga: pleiotropic genomic targets for precision
            medicine in human hypertension-vascular, renal, and cognitive
            diseases
  JOURNAL   Physiol Genomics 54 (2), 58-70 (2022)
   PUBMED   34859687
  REMARK    GeneRIF: The adducin saga: pleiotropic genomic targets for
            precision medicine in human hypertension-vascular, renal, and
            cognitive diseases.
            Review article
REFERENCE   4  (residues 1 to 662)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 662)
  AUTHORS   Liang,X., Zhou,Y. and Li,S.
  TITLE     Association of TBXA2R, P2Y12 and ADD1 genes polymorphisms with
            ischemic stroke susceptibility: A metaanalysis
  JOURNAL   Clin Invest Med 43 (3), E33-E43 (2020)
   PUBMED   32971583
  REMARK    GeneRIF: Association of TBXA2R, P2Y12 and ADD1 genes polymorphisms
            with ischemic stroke susceptibility: A metaanalysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 662)
  AUTHORS   Goldberg,Y.P., Lin,B.Y., Andrew,S.E., Nasir,J., Graham,R.,
            Glaves,M.L., Hutchinson,G., Theilmann,J., Ginzinger,D.G.,
            Schappert,K. et al.
  TITLE     Cloning and mapping of the alpha-adducin gene close to D4S95 and
            assessment of its relationship to Huntington disease
  JOURNAL   Hum Mol Genet 1 (9), 669-675 (1992)
   PUBMED   1284592
REFERENCE   7  (residues 1 to 662)
  AUTHORS   Taylor,S.A., Snell,R.G., Buckler,A., Ambrose,C., Duyao,M.,
            Church,D., Lin,C.S., Altherr,M., Bates,G.P., Groot,N. et al.
  TITLE     Cloning of the alpha-adducin gene from the Huntington's disease
            candidate region of chromosome 4 by exon amplification
  JOURNAL   Nat Genet 2 (3), 223-227 (1992)
   PUBMED   1345173
REFERENCE   8  (residues 1 to 662)
  AUTHORS   Joshi,R., Gilligan,D.M., Otto,E., McLaughlin,T. and Bennett,V.
  TITLE     Primary structure and domain organization of human alpha and beta
            adducin
  JOURNAL   J Cell Biol 115 (3), 665-675 (1991)
   PUBMED   1840603
REFERENCE   9  (residues 1 to 662)
  AUTHORS   Mangeat,P.H.
  TITLE     Interaction of biological membranes with the cytoskeletal framework
            of living cells
  JOURNAL   Biol Cell 64 (3), 261-281 (1988)
   PUBMED   2976282
  REMARK    Review article
REFERENCE   10 (residues 1 to 662)
  AUTHORS   Gardner,K. and Bennett,V.
  TITLE     Modulation of spectrin-actin assembly by erythrocyte adducin
  JOURNAL   Nature 328 (6128), 359-362 (1987)
   PUBMED   3600811
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC042998.1 and BU729599.1.
            
            Summary: Adducins are a family of cytoskeletal proteins encoded by
            three genes (alpha, beta, and gamma). Adducin acts as a heterodimer
            of the related alpha, beta, or gamma subunits. The protein encoded
            by this gene represents the alpha subunit. Alpha- and beta-adducin
            include a protease-resistant N-terminal region and a
            protease-sensitive, hydrophilic C-terminal region. Adducin binds
            with high affinity to Ca(2+)/calmodulin and is a substrate for
            protein kinases A and C. [provided by RefSeq, Aug 2017].
            
            Transcript Variant: This variant (5) differs in the 5' UTR and
            contains two additional alternate exons compared to variant 1. The
            resulting isoform (e) has an alternate in-frame segment and a
            shorter and distinct C-terminus compared to isoform a. Variants 5
            and 11 both encode the same isoform (e).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC042998.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..662
                     /product="alpha-adducin isoform e"
                     /note="erythrocyte adducin alpha subunit; alpha-adducin;
                     adducin 1 (alpha); alpha-adducin 1"
                     /calculated_mol_wt=73251
     Region          145..391
                     /region_name="Aldolase_II"
                     /note="Class II Aldolase and Adducin head (N-terminal)
                     domain. Aldolases are ubiquitous enzymes catalyzing
                     central steps of carbohydrate metabolism. Based on
                     enzymatic mechanisms, this superfamily has been divided
                     into two distinct classes (Class I and II); cl00214"
                     /db_xref="CDD:469663"
     Site            order(151,155,163,188,190..191,241,243..244,249..251,259,
                     261..262,273,301,312,319,323,330,348)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238232"
     Site            order(168,185..186,211..213,239,241,302)
                     /site_type="active"
                     /db_xref="CDD:238232"
     Site            order(239,241,302)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238232"
     CDS             1..662
                     /gene="ADD1"
                     /gene_synonym="ADDA"
                     /coded_by="NM_001286645.2:864..2852"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS75094.1"
                     /db_xref="GeneID:118"
                     /db_xref="HGNC:HGNC:243"
                     /db_xref="MIM:102680"
ORIGIN      
        1 mngdsraavv tspppttaph keryfdrvde nnpeylrern mapdlrqdfn mmeqkkrvsm
       61 ilqspafcee lesmiqeqfk kgknptglla lqqiadfmtt nvpnvypaap qggmaalnms
      121 lgmvtpvndl rgsdsiaydk gekllrckla afyrladlfg wsqliynhit trvnseqehf
      181 livpfgllys evtasslvki nlqgdivdrg stnlgvnqag ftlhsaiyaa rpdvkcvvhi
      241 htpagaavsa mkcgllpisp ealslgevay hdyhgilvde eekvliqknl gpkskvlilr
      301 nhglvsvges veeafyyihn lvvaceiqvr tlasaggpdn lvllnpekyk aksrspgspv
      361 gegtgsppkw qigeqefeal mrmldnlgyr tgypyrypal rekskkysdv evpasvtgys
      421 fasdgdsgtc splrhsfqkq qrektrwlns grgdeaseeg qngsspkskt kwtkedghrt
      481 stsavpnlfv plntnpkevq emrnkireqn lqdiktagpq sqvlcgvvmd rslvqdapls
      541 dctetiegle lteqtfspak slsfrkgelv taskaiieke yqphvivstt gpnpfttltd
      601 releeyrrev erkqkgseen ldeareqkek sppdqpavph pppstpikle egdgcareyl
      661 lp
//
LOCUS       NP_001387131            1194 aa            linear   PRI 21-NOV-2025
DEFINITION  protein transport protein Sec31A isoform 20 [Homo sapiens].
ACCESSION   NP_001387131
VERSION     NP_001387131.1
DBSOURCE    REFSEQ: accession NM_001400202.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1194)
  AUTHORS   Tobias,E.S., Lucas-Herald,A.K., Sagar,D., Montezano,A.C.,
            Rios,F.J., De Lucca Camargo,L., Hamilton,G., Gazdagh,G.,
            Diver,L.A., Williams,N., Herzyk,P., Touyz,R.M., Greenfield,A.,
            McGowan,R. and Ahmed,S.F.
  TITLE     SEC31A may be associated with pituitary hormone deficiency and
            gonadal dysgenesis
  JOURNAL   Endocrine 84 (2), 345-349 (2024)
   PUBMED   38400880
  REMARK    GeneRIF: SEC31A may be associated with pituitary hormone deficiency
            and gonadal dysgenesis.
REFERENCE   2  (residues 1 to 1194)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1194)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1194)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1194)
  AUTHORS   Jin,L., Pahuja,K.B., Wickliffe,K.E., Gorur,A., Baumgartel,C.,
            Schekman,R. and Rape,M.
  TITLE     Ubiquitin-dependent regulation of COPII coat size and function
  JOURNAL   Nature 482 (7386), 495-500 (2012)
   PUBMED   22358839
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1194)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1194)
  AUTHORS   Kim,J.H., Hong,J.A., Pih,K.T. and Hwang,I.
  TITLE     Identification and isolation of differentially expressed genes in
            osmotically stressed human oral keratinocytes
  JOURNAL   Arch Oral Biol 46 (4), 335-341 (2001)
   PUBMED   11269867
REFERENCE   8  (residues 1 to 1194)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 1194)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   10 (residues 1 to 1194)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021105.13 and AC108469.5.
            
            Summary: The protein encoded by this gene shares similarity with
            the yeast Sec31 protein, and is a component of the outer layer of
            the coat protein complex II (COPII). The encoded protein is
            involved in vesicle budding from the endoplasmic reticulum (ER) and
            contains multiple WD repeats near the N-terminus and a proline-rich
            region in the C-terminal half. It associates with the protein
            encoded by the SEC13 homolog, nuclear pore and COPII coat complex
            component (SEC13), and is required for ER-Golgi transport.
            Monoubiquitylation of this protein by CUL3-KLHL12 was found to
            regulate the size of COPII coats to accommodate unusually shaped
            cargo. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.793711.1,
                                           SRR18074969.1184547.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1194
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..1194
                     /product="protein transport protein Sec31A isoform 20"
                     /note="yeast Sec31p homolog; protein transport protein
                     Sec31A; web1-like protein; SEC31 homolog A, COPII coat
                     complex component; SEC31-related protein A; SEC31-like
                     protein 1; SEC31 homolog A, COPII coating complex
                     component"
                     /calculated_mol_wt=130390
     Region          13..332
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(26,40,46..47,52..53,91,95,101..102,117,121,139,144,
                     150..151,164,185,190,196..197,209..210,231,235,244..245,
                     258..259,277,282,288..289,301..302,320,325,331..332)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          70..119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          125..162
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          172..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          263..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          306..331
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <534..>657
                     /region_name="ACE1-Sec16-like"
                     /note="Ancestral coatomer element 1 (ACE1) of COPII coat
                     complex assembly protein Sec16; cl14807"
                     /db_xref="CDD:449359"
     Site            order(535..539,541,543,554,556,557..558,560..561,565,571,
                     579,591,594,619..620)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187750"
     Region          864..>1090
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     CDS             1..1194
                     /gene="SEC31A"
                     /gene_synonym="ABP125; ABP130; HPBKS; HSPC275; HSPC334;
                     NEDSOSB; SEC31L1"
                     /coded_by="NM_001400202.1:68..3652"
                     /note="isoform 20 is encoded by transcript variant 36"
                     /db_xref="GeneID:22872"
                     /db_xref="HGNC:HGNC:17052"
                     /db_xref="MIM:610257"
ORIGIN      
        1 mklkevdrta mqawspaqnh piylatgtsa qqldatfstn asleifeldl sdpsldmksc
       61 atfssshryh kliwgpykmd skgdvsgvli aggengniil ydpskiiagd kevviaqndk
      121 htgpvraldv nifqtnlvas ganeseiyiw dlnnfatpmt pgaktqpped isciawnrqv
      181 qhilasasps gratvwdlrk nepiikvsdh snrmhcsgla whpdvatqmv laseddrlpv
      241 iqmwdlrfas splrvlenha rgilaiawsm adpelllscg kdakilcsnp ntgevlyelp
      301 tntqwcfdiq wcprnpavls aasfdgrisv ysimggstdg lrqkqvdkls ssfgnldpfg
      361 tgqplpplqi pqqtaqhsiv lplkkppkwi rrpvgasfsf ggklvtfenv rmpshqgaeq
      421 qqqqhhvfis qvvtekefls rsdqlqqavq sqgfinycqk kidasqtefe knvwsflkvn
      481 feddsrgkyl ellgyrkedl gkkhikeeke eseflpssgg tfnisvsgdi dglitqallt
      541 gnfesavdlc lhdnrmadai ilaiaggqel lartqkkyfa ksqskitrli tavvmknwke
      601 ivescdlknw realaavlty akpdefsalc dllgtrlene gdsllqtqac lcyicagnve
      661 klvacwtkaq dgshplslqd liekvvilrk avqltqamdt stvgvllaak msqyanllaa
      721 qgsiaaalaf lpdntnqpni mqlrdrlcra qgepvaghes pkipyekqql pkgrpgpvag
      781 hhqmprvqtq qyyphgenpp ppgfimhgnv npnaagqlpt spghmhtqvp pypqpqpyqp
      841 aqpypfgtgg samyrpqqpv apptsnaypn tpyissassy tgqsqlyaaq hqassptssp
      901 atsfppppss gasfqhggpg appsssayal ppgttgtlpa aselpasqrt enqsiqdqap
      961 mlegpqngwn dppalnrvpk kkkmpenfmp pvpitspimn plgdpqsqml qqqpsapvpl
     1021 ssqssfpqph lpggqpfhgv qqplgqtgmp psfskpnieg apgapigntf qhvqslptkk
     1081 itkkpipdeh lilkttfedl iqrclssatd pqtkrkldda skrleflydk lreqtlspti
     1141 tsglhniars ietrnysegl tmhthivsts nfsetsafmp vlkvvltqan klgv
//
LOCUS       NP_001128711             274 aa            linear   PRI 21-NOV-2025
DEFINITION  L-lactate dehydrogenase A chain isoform 2 [Homo sapiens].
ACCESSION   NP_001128711
VERSION     NP_001128711.1
DBSOURCE    REFSEQ: accession NM_001135239.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Hu,C., Zhang,W., Jia,Y., Zhao,J., Chen,Q., Hao,C. and Yu,Y.
  TITLE     USP4 promotes PTC progression by stabilizing LDHA and activating
            the MAPK and AKT signaling pathway
  JOURNAL   Aging (Albany NY) 16 (19), 12850-12865 (2024)
   PUBMED   39393052
  REMARK    GeneRIF: USP4 promotes PTC progression by stabilizing LDHA and
            activating the MAPK and AKT signaling pathway.
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Zhuo,Z., Wang,Y. and Xu,Y.
  TITLE     Advancements in research on lactate dehydrogenase A in urinary
            system tumors
  JOURNAL   BMC Urol 24 (1), 187 (2024)
   PUBMED   39215270
  REMARK    GeneRIF: Advancements in research on lactate dehydrogenase A in
            urinary system tumors.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Vats,P., Singh,J., Srivastava,S.K., Kumar,A. and Nema,R.
  TITLE     LncRNA TMPO-AS1 Promotes Triple-Negative Breast Cancer by Sponging
            miR-383-5p to Trigger the LDHA Axis
  JOURNAL   Asian Pac J Cancer Prev 25 (8), 2929-2944 (2024)
   PUBMED   39205592
  REMARK    GeneRIF: LncRNA TMPO-AS1 Promotes Triple-Negative Breast Cancer by
            Sponging miR-383-5p to Trigger the LDHA Axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Papulino,C., Chianese,U., Ali,A., Favale,G., Tuccillo,C.,
            Ciardiello,F., Di Mauro,A., Mignogna,C., Ferrara,G., Budillon,A.,
            Megchelenbrink,W.L., Del Gaudio,N., Conte,M., Merciai,F.,
            Campiglia,P., Altucci,L., Carafa,V., Sommella,E. and Benedetti,R.
  TITLE     Inverse FASN and LDHA correlation drives metabolic resistance in
            breast cancer
  JOURNAL   J Transl Med 22 (1), 676 (2024)
   PUBMED   39044184
  REMARK    GeneRIF: Inverse FASN and LDHA correlation drives metabolic
            resistance in breast cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Miyajima,H., Shimizu,T. and Kaneko,E.
  TITLE     [Gene expression in lactate dehydrogenase-A subunit deficiency]
  JOURNAL   Rinsho Shinkeigaku 32 (10), 1087-1092 (1992)
   PUBMED   1297552
REFERENCE   7  (residues 1 to 274)
  AUTHORS   Sudo,K., Maekawa,M., Shioya,M., Ikeda,K., Takahashi,N., Isogai,Y.,
            Li,S.S., Kanno,T., Machida,K. and Toriumi,J.
  TITLE     Molecular analysis of genetic mutation in electrophoretic variant
            of human lactate dehydrogenase-A(M) subunit
  JOURNAL   Biochem Int 27 (6), 1051-1057 (1992)
   PUBMED   1445373
REFERENCE   8  (residues 1 to 274)
  AUTHORS   Maekawa,M., Sudo,K., Li,S.S. and Kanno,T.
  TITLE     Genotypic analysis of families with lactate dehydrogenase A (M)
            deficiency by selective DNA amplification
  JOURNAL   Hum Genet 88 (1), 34-38 (1991)
   PUBMED   1959923
REFERENCE   9  (residues 1 to 274)
  AUTHORS   Maekawa,M., Sudo,K., Li,S.S. and Kanno,T.
  TITLE     Analysis of genetic mutations in human lactate dehydrogenase-A(M)
            deficiency using DNA conformation polymorphism in combination with
            polyacrylamide gradient gel and silver staining
  JOURNAL   Biochem Biophys Res Commun 180 (2), 1083-1090 (1991)
   PUBMED   1953713
REFERENCE   10 (residues 1 to 274)
  AUTHORS   LeVan,K.M. and Goldberg,E.
  TITLE     Properties of human testis-specific lactate dehydrogenase expressed
            from Escherichia coli
  JOURNAL   Biochem J 273 (Pt 3) (Pt 3), 587-592 (1991)
   PUBMED   1996957
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK296667.1, AC084117.6 and
            BM995301.1.
            
            Summary: This gene encodes the A subunit of lactate dehydrogenase
            enzyme which catalyzes the reversible conversion of pyruvate to
            lactate with the concomitant oxidation of NADH to NAD in anaerobic
            glycolysis. The protein is found predominantly in skeletal muscle
            and belongs to the lactate dehydrogenase family. Mutations in this
            gene have been linked to exertional myoglobinuria. The human genome
            contains several non-transcribed pseudogenes of this gene.
            [provided by RefSeq, Sep 2023].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            central coding region, compared to variant 1. The resulting isoform
            (2) lacks a segment of the LDH domain but has the same N- and
            C-termini, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.304666.1, AK296667.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.1"
     Protein         1..274
                     /product="L-lactate dehydrogenase A chain isoform 2"
                     /EC_number="1.1.1.27"
                     /note="L-lactate dehydrogenase A chain; lactate
                     dehydrogenase M; LDH muscle subunit; renal carcinoma
                     antigen NY-REN-59; proliferation-inducing gene 19; LDH-A;
                     LDH-M; cell proliferation-inducing gene 19 protein;
                     epididymis secretory sperm binding protein Li 133P"
                     /calculated_mol_wt=30074
     Region          19..271
                     /region_name="LDH_1"
                     /note="A subgroup of L-lactate dehydrogenases; cd05293"
                     /db_xref="CDD:133429"
     Site            order(20,123,126,128,145,150,207..209,212,239..240,243,
                     245..247)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:133429"
     Site            order(33,38,60..61,64,66..67,111,113..114,120,186..187,
                     190..193)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133429"
     CDS             1..274
                     /gene="LDHA"
                     /gene_synonym="GSD11; HEL-S-133P; LDHM; PIG19"
                     /coded_by="NM_001135239.2:99..923"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44549.1"
                     /db_xref="GeneID:3939"
                     /db_xref="HGNC:HGNC:6535"
                     /db_xref="MIM:150000"
ORIGIN      
        1 matlkdqliy nllkeeqtpq nkitvvgvga vgmacaisil mkdladelal vdviedklkg
       61 emmdlqhgsl flrtpkivsg kvdiltyvaw kisgfpknrv igsgcnldsa rfrylmgerl
      121 gvhplschgw vlgehgdssv pvwsgmnvag vslktlhpdl gtdkdkeqwk evhkqvvesa
      181 yeviklkgyt swaiglsvad laesimknlr rvhpvstmik glygikddvf lsvpcilgqn
      241 gisdlvkvtl tseeearlkk sadtlwgiqk elqf
//
LOCUS       NP_001369463             701 aa            linear   PRI 21-NOV-2025
DEFINITION  amyloid beta precursor like protein 2 isoform 18 [Homo sapiens].
ACCESSION   NP_001369463
VERSION     NP_001369463.1
DBSOURCE    REFSEQ: accession NM_001382534.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Tao,Z., Huang,J. and Li,J.
  TITLE     Comprehensive intratumoral heterogeneity landscaping of liver
            hepatocellular carcinoma and discerning of APLP2 in cancer
            progression
  JOURNAL   Environ Toxicol 39 (2), 612-625 (2024)
   PUBMED   37515494
  REMARK    GeneRIF: Comprehensive intratumoral heterogeneity landscaping of
            liver hepatocellular carcinoma and discerning of APLP2 in cancer
            progression.
REFERENCE   3  (residues 1 to 701)
  AUTHORS   Huang,X., Yang,J., Xi,H., Zhang,M., Oh,Y., Jin,Z. and Zheng,Z.
  TITLE     Implication of Amyloid Precursor-like Protein 2 Expression in
            Cutaneous Squamous Cell Carcinoma Pathogenesis
  JOURNAL   In Vivo 38 (1), 399-408 (2024)
   PUBMED   38148084
  REMARK    GeneRIF: Implication of Amyloid Precursor-like Protein 2 Expression
            in Cutaneous Squamous Cell Carcinoma Pathogenesis.
REFERENCE   4  (residues 1 to 701)
  AUTHORS   Chen,J., Tang,F., Li,H., Wu,X., Yang,Y., Liu,Z., Huang,X., Wang,J.,
            Zheng,R., Wang,L., Liu,H., Xu,J., Wang,P. and Liu,F.
  TITLE     Mycobacterium tuberculosis suppresses APLP2 expression to enhance
            its survival in macrophage
  JOURNAL   Int Immunopharmacol 124 (Pt B), 111058 (2023)
   PUBMED   37844466
  REMARK    GeneRIF: Mycobacterium tuberculosis suppresses APLP2 expression to
            enhance its survival in macrophage.
REFERENCE   5  (residues 1 to 701)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 701)
  AUTHORS   Blangy,A., Vidal,F., Cuzin,F., Yang,Y.H., Boulukos,K. and
            Rassoulzadegan,M.
  TITLE     CDEBP, a site-specific DNA-binding protein of the 'APP-like'
            family, is required during the early development of the mouse
  JOURNAL   J Cell Sci 108 (Pt 2), 675-683 (1995)
   PUBMED   7539437
REFERENCE   7  (residues 1 to 701)
  AUTHORS   von der Kammer,H., Hanes,J., Klaudiny,J. and Scheit,K.H.
  TITLE     A human amyloid precursor-like protein is highly homologous to a
            mouse sequence-specific DNA-binding protein
  JOURNAL   DNA Cell Biol 13 (11), 1137-1143 (1994)
   PUBMED   7702756
REFERENCE   8  (residues 1 to 701)
  AUTHORS   Bush,A.I., Pettingell,W.H. Jr., de Paradis,M., Tanzi,R.E. and
            Wasco,W.
  TITLE     The amyloid beta-protein precursor and its mammalian homologues.
            Evidence for a zinc-modulated heparin-binding superfamily
  JOURNAL   J Biol Chem 269 (43), 26618-26621 (1994)
   PUBMED   7929392
REFERENCE   9  (residues 1 to 701)
  AUTHORS   von der Kammer,H., Loffler,C., Hanes,J., Klaudiny,J., Scheit,K.H.
            and Hansmann,I.
  TITLE     The gene for the amyloid precursor-like protein APLP2 is assigned
            to human chromosome 11q23-q25
  JOURNAL   Genomics 20 (2), 308-311 (1994)
   PUBMED   8020984
REFERENCE   10 (residues 1 to 701)
  AUTHORS   Wasco,W., Gurubhagavatula,S., Paradis,M.D., Romano,D.M.,
            Sisodia,S.S., Hyman,B.T., Neve,R.L. and Tanzi,R.E.
  TITLE     Isolation and characterization of APLP2 encoding a homologue of the
            Alzheimer's associated amyloid beta protein precursor
  JOURNAL   Nat Genet 5 (1), 95-100 (1993)
   PUBMED   8220435
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003041.3 and AP001183.6.
            
            Summary: This gene encodes amyloid precursor- like protein 2
            (APLP2), which is a member of the APP (amyloid precursor protein)
            family including APP, APLP1 and APLP2. This protein is ubiquitously
            expressed. It contains heparin-, copper- and zinc- binding domains
            at the N-terminus, BPTI/Kunitz inhibitor and E2 domains in the
            middle region, and transmembrane and intracellular domains at the
            C-terminus. This protein interacts with major histocompatibility
            complex (MHC) class I molecules. The synergy of this protein and
            the APP is required to mediate neuromuscular transmission, spatial
            learning and synaptic plasticity. This protein has been implicated
            in the pathogenesis of Alzheimer's disease. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            identified. [provided by RefSeq, Aug 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2148093
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.3"
     Protein         1..701
                     /product="amyloid beta precursor like protein 2 isoform
                     18"
                     /note="amyloid precursor protein homolog HSD-2; CDEI
                     box-binding protein; amyloid beta (A4) precursor-like
                     protein 2; testicular tissue protein Li 23; sperm membrane
                     protein YWK-II"
                     /calculated_mol_wt=79831
     Region          42..204
                     /region_name="A4_EXTRA"
                     /note="amyloid A4; smart00006"
                     /db_xref="CDD:128326"
     Region          309..485
                     /region_name="APP_E2"
                     /note="E2 domain of amyloid precursor protein; pfam12925"
                     /db_xref="CDD:463752"
     Region          618..698
                     /region_name="JMTM_APLP2"
                     /note="juxtamembrane and transmembrane (JMTM) domain found
                     in amyloid-like protein 2 (APLP-2) and similar proteins;
                     cd21709"
                     /db_xref="CDD:411992"
     Site            order(618..619,633,636..637,640..641,643..644,647..648,
                     651,654)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:411992"
     Site            order(619..621,637..638,640..641,643..648,651..656)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:411992"
     CDS             1..701
                     /gene="APLP2"
                     /gene_synonym="APLP-2; APPH; APPL2; CDEBP"
                     /coded_by="NM_001382534.1:85..2190"
                     /note="isoform 18 is encoded by transcript variant 20"
                     /db_xref="GeneID:334"
                     /db_xref="HGNC:HGNC:598"
                     /db_xref="MIM:104776"
ORIGIN      
        1 maatgtaaaa atgrllllll vgltapalal agyiealaan agtgfavaep qiamfcgkln
       61 mhvniqtgkw epdptgtksc fetkeevlqy cqemypelqi tnvmeanqrv sidnwcrrdk
      121 kqcksrfvtp fkclvgefvs dvllvpekcq ffhkermevc enhqhwhtvv keacltqgmt
      181 lysygmllpc gvdqfhgtey vccpqtkiig svskeeeeed eeeeeeedee edydvyksef
      241 pteadledft eaavdedded eeegeevved rdyyydtfkg ddyneenpte pgsdgtmsdk
      301 eithdvkvpp tplptndvdv yfetsaddne harfqkakeq leirhrnrmd rvkkeweeae
      361 lqaknlpkae rqtliqhfqa mvkalekeaa sekqqlveth larveamlnd rrrmalenyl
      421 aalqsdppra lrryvraenk drlhtirhyq hvlavdpeka aqmksqvmth lhvieerrnq
      481 slsllykvpy vaqeiqeeid ellqeqradm dqftasiset pvdvrvssee seeippfhpf
      541 hpfpalpene dtqpelyhpm kkgsgvgeqd ggligaeekv insknkvden mvidetldvk
      601 emifnaervg gleeeresvg plredfslss saligllvia vaiatvivis lvmlrkrqyg
      661 tishgivevd pmltpeerhl nkmqnhgyen ptykyleqmq i
//
LOCUS       NP_690607                445 aa            linear   PRI 21-NOV-2025
DEFINITION  inward rectifier potassium channel 4 [Homo sapiens].
ACCESSION   NP_690607
VERSION     NP_690607.1
DBSOURCE    REFSEQ: accession NM_152868.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Wu,X.Y. and Yu,X.Y.
  TITLE     Overexpression of KCNJ4 correlates with cancer progression and
            unfavorable prognosis in lung adenocarcinoma
  JOURNAL   J Biochem Mol Toxicol 33 (4), e22270 (2019)
   PUBMED   30512237
  REMARK    GeneRIF: results shed some light on the contribution of KCNJ4
            functioning as a significant player in LADC, implying that KCNJ4
            might be a valuable prognostic biomarker and a potential
            therapeutic target for LADC treatment
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Agopian,A.J., Mitchell,L.E., Glessner,J., Bhalla,A.D., Sewda,A.,
            Hakonarson,H. and Goldmuntz,E.
  TITLE     Genome-wide association study of maternal and inherited loci for
            conotruncal heart defects
  JOURNAL   PLoS One 9 (5), e96057 (2014)
   PUBMED   24800985
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Ivarsson,Y., Arnold,R., McLaughlin,M., Nim,S., Joshi,R., Ray,D.,
            Liu,B., Teyra,J., Pawson,T., Moffat,J., Li,S.S., Sidhu,S.S. and
            Kim,P.M.
  TITLE     Large-scale interaction profiling of PDZ domains through proteomic
            peptide-phage display using human and viral phage peptidomes
  JOURNAL   Proc Natl Acad Sci U S A 111 (7), 2542-2547 (2014)
   PUBMED   24550280
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Coulter,K.L., Perier,F., Radeke,C.M. and Vandenberg,C.A.
  TITLE     Identification and molecular localization of a pH-sensing domain
            for the inward rectifier potassium channel HIR
  JOURNAL   Neuron 15 (5), 1157-1168 (1995)
   PUBMED   7576658
REFERENCE   7  (residues 1 to 445)
  AUTHORS   Budarf,M.L., Perier,F., Barnoski,B.L., Bell,C.J. and
            Vandenberg,C.A.
  TITLE     Assignment of the human hippocampal inward rectifier potassium
            channel (HIR) gene to 22q13.1
  JOURNAL   Genomics 26 (3), 625-629 (1995)
   PUBMED   7607694
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Makhina,E.N., Kelly,A.J., Lopatin,A.N., Mercer,R.W. and
            Nichols,C.G.
  TITLE     Cloning and expression of a novel human brain inward rectifier
            potassium channel
  JOURNAL   J Biol Chem 269 (32), 20468-20474 (1994)
   PUBMED   8051145
REFERENCE   9  (residues 1 to 445)
  AUTHORS   Tang,W. and Yang,X.C.
  TITLE     Cloning a novel human brain inward rectifier potassium channel and
            its functional expression in Xenopus oocytes
  JOURNAL   FEBS Lett 348 (3), 239-243 (1994)
   PUBMED   8034048
REFERENCE   10 (residues 1 to 445)
  AUTHORS   Perier,F., Radeke,C.M. and Vandenberg,C.A.
  TITLE     Primary structure and characterization of a small-conductance
            inwardly rectifying potassium channel from human hippocampus
  JOURNAL   Proc Natl Acad Sci U S A 91 (13), 6240-6244 (1994)
   PUBMED   8016146
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z97056.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Several different potassium channels are known to be
            involved with electrical signaling in the nervous system. One class
            is activated by depolarization whereas a second class is not. The
            latter are referred to as inwardly rectifying K+ channels, and they
            have a greater tendency to allow potassium to flow into the cell
            rather than out of it. This asymmetry in potassium ion conductance
            plays a key role in the excitability of muscle cells and neurons.
            The protein encoded by this gene is an integral membrane protein
            and member of the inward rectifier potassium channel family. The
            encoded protein has a small unitary conductance compared to other
            members of this protein family. Two transcript variants encoding
            the same protein have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U24056.1, CR456507.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303592.3/ ENSP00000306497.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..445
                     /product="inward rectifier potassium channel 4"
                     /note="hippocampal inward rectifier potassium channel;
                     potassium channel, inwardly rectifying subfamily J, member
                     4; inward rectifier K(+) channel Kir2.3; potassium
                     voltage-gated channel subfamily J member 4"
                     /calculated_mol_wt=49369
     Region          22..178
                     /region_name="IRK"
                     /note="Inward rectifier potassium channel transmembrane
                     domain; pfam01007"
                     /db_xref="CDD:460023"
     Site            56..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48050.1)"
     Region          91..111
                     /region_name="Val/Gly/Ala/Pro stretch"
                     /note="propagated from UniProtKB/Swiss-Prot (P48050.1)"
     Region          134..139
                     /region_name="Selectivity filter. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P48050.1)"
     Site            149..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48050.1)"
     Site            164
                     /site_type="other"
                     /note="Role in the control of polyamine-mediated channel
                     gating and in the blocking by intracellular magnesium.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P48050.1)"
     Region          185..357
                     /region_name="IRK_C"
                     /note="Inward rectifier potassium channel C-terminal
                     domain; pfam17655"
                     /db_xref="CDD:465439"
     Region          443..445
                     /region_name="PDZ-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P48050.1)"
     CDS             1..445
                     /gene="KCNJ4"
                     /gene_synonym="HIR; HIRK2; HRK1; IRK-3; IRK3; Kir2.3"
                     /coded_by="NM_152868.3:260..1597"
                     /db_xref="CCDS:CCDS13971.1"
                     /db_xref="GeneID:3761"
                     /db_xref="HGNC:HGNC:6265"
                     /db_xref="MIM:600504"
ORIGIN      
        1 mhghsrngqa hvprrkrrnr fvkkngqcnv yfanlsnksq rymadifttc vdtrwrymlm
       61 ifsaaflvsw lffgllfwci affhgdleas pgvpaaggpa aggggaapva pkpcimhvng
      121 flgaflfsve tqttigygfr cvteecplav iavvvqsivg cvidsfmigt imakmarpkk
      181 raqtllfshh avisvrdgkl clmwrvgnlr kshiveahvr aqlikpymtq egeylpldqr
      241 dlnvgydigl driflvspii ivheidedsp lygmgkeele sedfeivvil egmveatamt
      301 tqarssylas eilwghrfep vvfeekshyk vdysrfhkty evagtpccsa relqeskitv
      361 lpapppppsa fcyenelalm sqeeeemeee aaaaaavaag lgleagskee agiirmlefg
      421 shldlermqa slpldnisyr resai
//
LOCUS       NP_006810                543 aa            linear   PRI 21-NOV-2025
DEFINITION  stress-induced-phosphoprotein 1 isoform b [Homo sapiens].
ACCESSION   NP_006810
VERSION     NP_006810.1
DBSOURCE    REFSEQ: accession NM_006819.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Stetskaya,T.A., Krapiva,A.B., Kobzeva,K.A., Gurtovoy,D.E.,
            Komkova,G.V., Polonikov,A.V. and Bushueva,O.Y.
  TITLE     Polymorphism in Genes Encoding Adaptor Proteins ST13 and STIP1 and
            the Risk of Ischemic Stroke: a Pilot Study
  JOURNAL   Bull Exp Biol Med 176 (4), 477-480 (2024)
   PUBMED   38492099
  REMARK    GeneRIF: Polymorphism in Genes Encoding Adaptor Proteins ST13 and
            STIP1 and the Risk of Ischemic Stroke: a Pilot Study.
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Hua,H., Su,T., Han,L., Zhang,L., Huang,Y., Zhang,N. and Yang,M.
  TITLE     LINC01226 promotes gastric cancer progression through enhancing
            cytoplasm-to-nucleus translocation of STIP1 and stabilizing
            beta-catenin protein
  JOURNAL   Cancer Lett 577, 216436 (2023)
   PUBMED   37806517
  REMARK    GeneRIF: LINC01226 promotes gastric cancer progression through
            enhancing cytoplasm-to-nucleus translocation of STIP1 and
            stabilizing beta-catenin protein.
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Guo,Z. and Guo,L.
  TITLE     Tumor-promoting action of ubiquitin protease 43 in gastric cancer
            progression through deubiquitination and stabilization of
            stress-inducible phosphoprotein 1
  JOURNAL   Exp Cell Res 430 (2), 113714 (2023)
   PUBMED   37442266
  REMARK    GeneRIF: Tumor-promoting action of ubiquitin protease 43 in gastric
            cancer progression through deubiquitination and stabilization of
            stress-inducible phosphoprotein 1.
REFERENCE   5  (residues 1 to 543)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 543)
  AUTHORS   Zou,J., Guo,Y., Guettouche,T., Smith,D.F. and Voellmy,R.
  TITLE     Repression of heat shock transcription factor HSF1 activation by
            HSP90 (HSP90 complex) that forms a stress-sensitive complex with
            HSF1
  JOURNAL   Cell 94 (4), 471-480 (1998)
   PUBMED   9727490
REFERENCE   7  (residues 1 to 543)
  AUTHORS   Dittmar,K.D., Demady,D.R., Stancato,L.F., Krishna,P. and Pratt,W.B.
  TITLE     Folding of the glucocorticoid receptor by the heat shock protein
            (hsp) 90-based chaperone machinery. The role of p23 is to stabilize
            receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70
  JOURNAL   J Biol Chem 272 (34), 21213-21220 (1997)
   PUBMED   9261129
REFERENCE   8  (residues 1 to 543)
  AUTHORS   Dittmar,K.D. and Pratt,W.B.
  TITLE     Folding of the glucocorticoid receptor by the reconstituted
            Hsp90-based chaperone machinery. The initial
            hsp90.p60.hsp70-dependent step is sufficient for creating the
            steroid binding conformation
  JOURNAL   J Biol Chem 272 (20), 13047-13054 (1997)
   PUBMED   9148915
REFERENCE   9  (residues 1 to 543)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 543)
  AUTHORS   Honore,B., Leffers,H., Madsen,P., Rasmussen,H.H., Vandekerckhove,J.
            and Celis,J.E.
  TITLE     Molecular cloning and expression of a transformation-sensitive
            human protein containing the TPR motif and sharing identity to the
            stress-inducible yeast protein STI1
  JOURNAL   J Biol Chem 267 (12), 8485-8491 (1992)
   PUBMED   1569099
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA781468.1 and M86752.1.
            
            Summary: STIP1 is an adaptor protein that coordinates the functions
            of HSP70 (see HSPA1A; MIM 140550) and HSP90 (see HSP90AA1; MIM
            140571) in protein folding. It is thought to assist in the transfer
            of proteins from HSP70 to HSP90 by binding both HSP90 and
            substrate-bound HSP70. STIP1 also stimulates the ATPase activity of
            HSP70 and inhibits the ATPase activity of HSP90, suggesting that it
            regulates both the conformations and ATPase cycles of these
            chaperones (Song and Masison, 2005 [PubMed 16100115]).[supplied by
            OMIM, Jul 2009].
            
            Transcript Variant: This variant (2) uses an alternate 5' terminal
            exon and thus differs in the 5' UTR and 5' coding region, and uses
            an alternate start codon, compared to variant 1. The encoded
            isoform (b) has a distinct N-terminus and is shorter than isoform
            a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC002987.1, SRR1803614.190480.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000305218.9/ ENSP00000305958.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..543
                     /product="stress-induced-phosphoprotein 1 isoform b"
                     /note="Hsp70/Hsp90-organizing protein; NY-REN-11 antigen;
                     hsc70/Hsp90-organizing protein; epididymis secretory sperm
                     binding protein Li 94n; transformation-sensitive protein
                     IEF SSP 3521; renal carcinoma antigen NY-REN-11"
                     /calculated_mol_wt=62508
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895;
                     propagated from UniProtKB/Swiss-Prot (P31948.1)"
     Region          4..37
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P31948.1)"
     Region          <7..532
                     /region_name="3a0801s09"
                     /note="mitochondrial precursor proteins import receptor
                     (72 kDa mitochondrial outermembrane protein)
                     (mitochondrial import receptor for the ADP/ATP carrier)
                     (translocase of outermembrane tom70); TIGR00990"
                     /db_xref="CDD:273380"
     Region          7..32
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(8..9,12..13,15,39,42..43,46..47,49..50,73,76..77,
                     80..81,84)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Site            8
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P31948.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P31948.1)"
     Region          37..67
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          38..71
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P31948.1)"
     Region          72..105
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P31948.1)"
     Region          72..100
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          192..233
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P31948.1)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P31948.1)"
     Region          222..239
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P31948.1)"
     Region          225..258
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P31948.1)"
     Site            order(229..230,233..234,236,260,263..264,267..268,
                     270..271,301,304..305,308..309,312)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          229..253
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          258..288
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          259..292
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P31948.1)"
     Region          300..333
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P31948.1)"
     Region          300..328
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            301
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P31948.1)"
     Site            312
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P31948.1)"
     Site            325
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P31948.1)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P31948.1)"
     Site            344
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P31948.1)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (P31948.1)"
     Region          360..393
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P31948.1)"
     Site            order(364..365,368..369,371,395,398..399,402..403,
                     405..406,429,432..433,436..437,440)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          364..388
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          393..423
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          394..427
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P31948.1)"
     Region          428..461
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P31948.1)"
     Region          428..456
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            446
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P31948.1)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P31948.1)"
     CDS             1..543
                     /gene="STIP1"
                     /gene_synonym="HEL-S-94n; HOP; IEF-SSP-3521; P60; STI1;
                     STI1L"
                     /coded_by="NM_006819.3:92..1723"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS8058.1"
                     /db_xref="GeneID:10963"
                     /db_xref="HGNC:HGNC:11387"
                     /db_xref="MIM:605063"
ORIGIN      
        1 meqvnelkek gnkalsvgni ddalqcysea ikldphnhvl ysnrsaayak kgdyqkayed
       61 gcktvdlkpd wgkgysrkaa aleflnrfee akrtyeeglk heannpqlke glqnmearla
      121 erkfmnpfnm pnlyqklesd prtrtllsdp tyrelieqlr nkpsdlgtkl qdprimttls
      181 vllgvdlgsm deeeeiatpp pppppkketk pepmeedlpe nkkqalkeke lgndaykkkd
      241 fdtalkhydk akeldptnmt yitnqaavyf ekgdynkcre lcekaievgr enredyrqia
      301 kayarignsy fkeekykdai hfynkslaeh rtpdvlkkcq qaekilkeqe rlayinpdla
      361 leeknkgnec fqkgdypqam khyteaikrn pkdaklysnr aacytkllef qlalkdceec
      421 iqleptfikg ytrkaaalea mkdytkamdv yqkaldldss ckeaadgyqr cmmaqynrhd
      481 spedvkrram adpevqqims dpamrlileq mqkdpqalse hlknpviaqk iqklmdvgli
      541 air
//
LOCUS       NP_001373927            1084 aa            linear   PRI 21-NOV-2025
DEFINITION  angiomotin isoform 1 [Homo sapiens].
ACCESSION   NP_001373927 XP_011529177
VERSION     NP_001373927.1
DBSOURCE    REFSEQ: accession NM_001386998.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1084)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1084)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   3  (residues 1 to 1084)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1084)
  AUTHORS   Rheinemann,L., Thompson,T., Mercenne,G., Paine,E.L., Peterson,F.C.,
            Volkman,B.F., Alam,S.L., Alian,A. and Sundquist,W.I.
  TITLE     Interactions between AMOT PPxY motifs and NEDD4L WW domains
            function in HIV-1 release
  JOURNAL   J Biol Chem 297 (2), 100975 (2021)
   PUBMED   34284061
  REMARK    GeneRIF: Interactions between AMOT PPxY motifs and NEDD4L WW
            domains function in HIV-1 release.
REFERENCE   5  (residues 1 to 1084)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1084)
  AUTHORS   Bratt,A., Wilson,W.J., Troyanovsky,B., Aase,K., Kessler,R., Van
            Meir,E.G. and Holmgren,L.
  TITLE     Angiomotin belongs to a novel protein family with conserved
            coiled-coil and PDZ binding domains
  JOURNAL   Gene 298 (1), 69-77 (2002)
   PUBMED   12406577
  REMARK    Erratum:[Gene. 2003 May 22;310;231. Meir, EG [corrected to Van
            Meir, EG]]
REFERENCE   7  (residues 1 to 1084)
  AUTHORS   Zetter,B.R.
  TITLE     Hold that line. Angiomotin regulates endothelial cell motility
  JOURNAL   J Cell Biol 152 (6), F35-F36 (2001)
   PUBMED   11257132
REFERENCE   8  (residues 1 to 1084)
  AUTHORS   Troyanovsky,B., Levchenko,T., Mansson,G., Matvijenko,O. and
            Holmgren,L.
  TITLE     Angiomotin: an angiostatin binding protein that regulates
            endothelial cell migration and tube formation
  JOURNAL   J Cell Biol 152 (6), 1247-1254 (2001)
   PUBMED   11257124
REFERENCE   9  (residues 1 to 1084)
  AUTHORS   Rubinstein,M.H.
  TITLE     A new granulation method for compressed tablets [proceedings]
  JOURNAL   J Pharm Pharmacol 28 Suppl, 67P (1976)
   PUBMED   12345
REFERENCE   10 (residues 1 to 1084)
  AUTHORS   Aoyagi,F., Fujino,T. and Ohshiro,T.
  TITLE     Detection of small vessels for microsurgery by a Doppler flowmeter
  JOURNAL   Plast Reconstr Surg 55 (3), 372-373 (1975)
   PUBMED   123345
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004827.1.
            
            On Sep 18, 2020 this sequence version replaced XP_011529177.1.
            
            Summary: This gene belongs to the motin family of angiostatin
            binding proteins characterized by conserved coiled-coil domains and
            C-terminal PDZ binding motifs. The encoded protein is expressed
            predominantly in endothelial cells of capillaries as well as larger
            vessels of the placenta where it may mediate the inhibitory effect
            of angiostatin on tube formation and the migration of endothelial
            cells toward growth factors during the formation of new blood
            vessels. Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.879755.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1084
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq23"
     Protein         1..1084
                     /product="angiomotin isoform 1"
                     /calculated_mol_wt=117955
     Region          24..86
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VCS5.1)"
     Region          185..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VCS5.1)"
     Region          <191..>328
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     Region          224..268
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VCS5.1)"
     Region          300..424
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VCS5.1)"
     Region          410..751
                     /region_name="Involved in interaction with YAP1.
                     /evidence=ECO:0000269|PubMed:21205866"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VCS5.1)"
     Region          <433..>677
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          599..806
                     /region_name="Angiomotin_C"
                     /note="Angiomotin C terminal; pfam12240"
                     /db_xref="CDD:463503"
     Site            714
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VHG2; propagated from
                     UniProtKB/Swiss-Prot (Q4VCS5.1)"
     Region          837..876
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VCS5.1)"
     Region          995..1041
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VCS5.1)"
     Region          1081..1084
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4VCS5.1)"
     CDS             1..1084
                     /gene="AMOT"
                     /coded_by="NM_001386998.1:743..3997"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS48154.1"
                     /db_xref="GeneID:154796"
                     /db_xref="HGNC:HGNC:17810"
                     /db_xref="MIM:300410"
ORIGIN      
        1 mrnseeqpsg gttvlqrllq eqlrygnpse nrsllaihqq atgngppfps gsgnpgpqsd
       61 vlspqdhhqq lvahaarqep qgqeiqsenl imekqlsprm qnneelptye eakvqsqyfr
      121 gqqhasvgaa fyvtgvtnqk mrtegrpsvq rlnpgkmhqd eglrdlkqgh vrslserlmq
      181 mslatsgvka hppvtsapls ppqpndlykn ptsssefyka qgplpnqhsl kgmehrgppp
      241 eypfkgmppq svvckpqepg hfysehrlnq pgrtegqlmr yqhppeygaa rpaqdislpl
      301 sarnsqphsp tssltsggsl pllqsppstr lsparhplvp nqgdhsahlp rpqqhflpnq
      361 ahqgdhyrls qpglsqqqqq qqqqhhhhhh hqqqqqqqpq qqpgeaysam praqpssasy
      421 qpvpadpfai vsraqqmvei lsdenrnlrq elegcyekva rlqkveteiq rvseayenlv
      481 kssskreale kamrnklege irrmhdfnrd lrerletank qlaekeyegs edtrktisql
      541 faknkesqre kekleaelat arstnedqrr hieirdqals naqakvvkle eelkkkqvyv
      601 dkvekmqqal vqlqaacekr eqlehrlrtr lereleslri qqrqgncqpt nvseynaaal
      661 mellrekeer ilaleadmtk weqkyleenv mrhfaldaaa tvaaqrdttv ishspntsyd
      721 taleariqke eeeilmankr cldmegrikt lhaqiiekda mikvlqqrsr kepskteqls
      781 cmrpakslms isnagsglls hsstltgspi meekrddksw kgslgillgg dyraeyvpst
      841 pspvppstpl lsahsktgsr dcstqtergt esnktaavap isvpapvaaa ataaaitata
      901 atitttmvaa apvavaaaaa paaaaapspa taaataaavs paaagqipaa asvasaaava
      961 psaaaaaavq vapaapapvp apalvpvpap aaaqasapaq tqaptsapav aptpaptptp
     1021 avaqaevpas patgpgphrl sipsltcnpd ktdgpvfhsn tlerktpiqi lgqepdaemv
     1081 eyli
//
LOCUS       NP_001382232            2372 aa            linear   PRI 21-NOV-2025
DEFINITION  myomegalin isoform 22 [Homo sapiens].
ACCESSION   NP_001382232
VERSION     NP_001382232.1
DBSOURCE    REFSEQ: accession NM_001395303.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2372)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2372)
  AUTHORS   Pan,R., Dai,J., Liang,W., Wang,H., Ye,L., Ye,S., Lin,Z., Huang,S.,
            Xiong,Y., Zhang,L., Lu,L., Wang,O., Shen,X., Liao,W. and Lu,X.
  TITLE     PDE4DIP contributes to colorectal cancer growth and chemoresistance
            through modulation of the NF1/RAS signaling axis
  JOURNAL   Cell Death Dis 14 (6), 373 (2023)
   PUBMED   37355626
  REMARK    GeneRIF: PDE4DIP contributes to colorectal cancer growth and
            chemoresistance through modulation of the NF1/RAS signaling axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2372)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   4  (residues 1 to 2372)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 2372)
  AUTHORS   Abou Ziki,M.D., Bhat,N., Neogi,A., Driscoll,T.P., Ugwu,N., Liu,Y.,
            Smith,E., Abboud,J.M., Chouairi,S., Schwartz,M.A., Akar,J.G. and
            Mani,A.
  TITLE     Epistatic interaction of PDE4DIP and DES mutations in familial
            atrial fibrillation with slow conduction
  JOURNAL   Hum Mutat 42 (10), 1279-1293 (2021)
   PUBMED   34289528
  REMARK    GeneRIF: Epistatic interaction of PDE4DIP and DES mutations in
            familial atrial fibrillation with slow conduction.
REFERENCE   6  (residues 1 to 2372)
  AUTHORS   Shimada,H., Kuboshima,M., Shiratori,T., Nabeya,Y., Takeuchi,A.,
            Takagi,H., Nomura,F., Takiguchi,M., Ochiai,T. and Hiwasa,T.
  TITLE     Serum anti-myomegalin antibodies in patients with esophageal
            squamous cell carcinoma
  JOURNAL   Int J Oncol 30 (1), 97-103 (2007)
   PUBMED   17143517
  REMARK    GeneRIF: MMGL-antibody is significantly with a favorable prognosis.
            Consequently, MMGL-anatibodies may be a useful tumor marker to
            diagnose and establish a prognosis in patients with esophageal
            squamous cell carcinoma.
REFERENCE   7  (residues 1 to 2372)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 2372)
  AUTHORS   Soejima,H., Kawamoto,S., Akai,J., Miyoshi,O., Arai,Y., Morohka,T.,
            Matsuo,S., Niikawa,N., Kimura,A., Okubo,K. and Mukai,T.
  TITLE     Isolation of novel heart-specific genes using the BodyMap database
  JOURNAL   Genomics 74 (1), 115-120 (2001)
   PUBMED   11374908
REFERENCE   9  (residues 1 to 2372)
  AUTHORS   Verde,I., Pahlke,G., Salanova,M., Zhang,G., Wang,S., Coletti,D.,
            Onuffer,J., Jin,S.L. and Conti,M.
  TITLE     Myomegalin is a novel protein of the golgi/centrosome that
            interacts with a cyclic nucleotide phosphodiesterase
  JOURNAL   J Biol Chem 276 (14), 11189-11198 (2001)
   PUBMED   11134006
REFERENCE   10 (residues 1 to 2372)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC245389.1, AC239802.3 and
            AC239804.2.
            
            Summary: The protein encoded by this gene serves to anchor
            phosphodiesterase 4D to the Golgi/centrosome region of the cell.
            Defects in this gene may be a cause of myeloproliferative disorder
            (MBD) associated with eosinophilia. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.233443.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     Protein         1..2372
                     /product="myomegalin isoform 22"
                     /note="myomegalin; cardiomyopathy-associated protein 2"
                     /calculated_mol_wt=268193
     Region          140..816
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          143..210
                     /region_name="Cnn_1N"
                     /note="Centrosomin N-terminal motif 1; pfam07989"
                     /db_xref="CDD:462333"
     Region          492..1202
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1140..>1290
                     /region_name="ETAA1"
                     /note="Ewing's tumour-associated antigen 1 homolog;
                     pfam15350"
                     /db_xref="CDD:464665"
     Region          1578..1647
                     /region_name="Olduvai"
                     /note="Olduvai domain; pfam06758"
                     /db_xref="CDD:429104"
     Region          <1867..>2044
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..2372
                     /gene="PDE4DIP"
                     /gene_synonym="CMYA2; MMGL"
                     /coded_by="NM_001395303.1:72..7190"
                     /note="isoform 22 is encoded by transcript variant 22"
                     /db_xref="GeneID:9659"
                     /db_xref="HGNC:HGNC:15580"
                     /db_xref="MIM:608117"
ORIGIN      
        1 mkgtdsgscc rrrcdfgccc rasrrahytp yrsgdatrtp qsprqtpsre rrrpepagsw
       61 aaaaeeeeaa aaatpwmrdy faeddgemvp rtshtaafls dtkdrgppvq sqiwrsgekv
      121 pfvqtyslra fekppqvqtq alrdfekhln dlkkenfslk lriyfleerm qqkyeasred
      181 iykrnielkv eveslkrelq dkkqhldktw advenlnsqn eaelrrqfee rqqetehvye
      241 llenkiqllq eesrlaknea armaalveae kecnlelsek lkgvtknwed vpgdqvkpdq
      301 ytealaqrdk rieelnqsla aqerlveqls rekqqllhll eeptsmevqp mteellkqqk
      361 lnshettitq qsvsdshlae lqekiqqtea tnkilqekln emsyelkcaq essqkqdgti
      421 qnlketlksr ereteelyqv iegqndtmak lremlhqsql gqlhssegts paqqqvalld
      481 lqsalfcsql eiqklqrvvr qkerqladak qcvqfveaaa heseqqkeas wkhnqelrka
      541 lqqlqeelqn ksqqlrawea ekyneirtqe qniqhlnhsl shkeqllqef rellqyrdns
      601 dktleaneml leklrqrihd kavaleraid ekfsaleeke kelrqlrlav rerdhdlerl
      661 rdvlssneat mqsmesllra kgleveqlst tcqnlqwlke emetkfsrwq keqesiiqql
      721 qtslhdrnke vedlsatllc klgpgqseia eelcqrlqrk ermlqdllsd rnkqvlehem
      781 eiqgllqsvs treqesqaaa eklvqalmer nselqalrqy lggrdslmsq apisnqqaev
      841 tptgrlgkqt dqgsmqipsr ddstsltake dvsiprstlg dldtvaglek elsnakeele
      901 lmakkeresq melsalqsmm avqeeelqvq aadmesltrn iqikedlikd lqmqlvdped
      961 ipamerltqe vlllrekvas vesqgqeisg nrrqqlllml eglvdersrl nealqaerql
     1021 ysslvkfhah pesserdrtl qvelegaqvl rsrleevlgr slerlnrlet laaiggaaag
     1081 ddtedtstef tdsieeeaah hshqqlvkva lekslatvet qnpsfsppsp mggdsnrclq
     1141 eemlhlraef hqhleekrka eeelkelkaq ieeagfssvs hirntmlslc lenaelkeqm
     1201 geamsdgwei eedkekgeld nqsqprdpgp qsafslpgst qhlrsqlsqc kqryqdlqek
     1261 lllseatvfa qanelekyrv mlseslvkqd skqiqvdlqd lgyetcgrse neaereetts
     1321 peceehnslk emvlmeglcs eqgrrgstla ssserkplen qlgkqeefrv ygksenilvl
     1381 rkdikdlkaq lqnankviqn lksrvrslsv tsdysssler prklravgtl egssphsvpd
     1441 edegwlsdgt gafyspglqa kkdlesliqr vsqleaqlpk ngleeklaee lrsaswpgky
     1501 dsliqdqare lsylrqkire grgicylitr hakdtvksfe dllrsndidy ylgqsfreql
     1561 aqgsqlterl tsklstkdhk sekdqaglep lalrlsrelq ekekvievlq akldarsltp
     1621 ssshalsdsh rspsstsfls deleacsdmd ivseythyee kkaspshsds ihhsshsavl
     1681 sskpsstsas qgakaesnsn pislptpqnt pkeanqahsg fhfhsipkla slpqaplpsa
     1741 pssflpfspt gplllgccet pvvslaeaqq elqmlqkqlg esastvppas tatllsndle
     1801 adssyylnsa qphspprgti elgrilepgy lgssgkwdvm rpqkgsvsgd lssgssvyql
     1861 nskptgadll eehlgeirnl rqrleesici ndrlreqleh rltstargrg stsnfysqgl
     1921 esipqlcnen rvlrednrrl qaqlshvsre hsqeteslre allssrshlq elekelehqk
     1981 verqqlledl rekqqevlhf reerlslqen dsrlqhklvl lqqqceekqq lfeslqselq
     2041 iyealygnsk kglkayslda chqiplssdl shlvaevral rgqleqsiqg nnclrlqlqq
     2101 qlesgagkas lspssinqnf pastdpgnkq lllqdsavsp pvrdvgmnsp alvfpssass
     2161 tpgsetpiin ranglgldts pvmktppkle gdatdgsfan khgrhvighi ddysalrqqi
     2221 aegkllvkki vslvrsacsf pgleaqgtev lgskgihelr sstsalhhal eesaslltmf
     2281 wraalpsthi pvlpgkvges terellelrt kvskqerllq sttehlknan qqkesmeqfi
     2341 vsqltrthdv lkkartnlev kslralpctp al
//
LOCUS       NP_001028723             457 aa            linear   PRI 21-NOV-2025
DEFINITION  TOM1-like protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001028723
VERSION     NP_001028723.1
DBSOURCE    REFSEQ: accession NM_001033551.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Shinde,S.R., Mick,D.U., Aoki,E., Rodrigues,R.B., Gygi,S.P. and
            Nachury,M.V.
  TITLE     The ancestral ESCRT protein TOM1L2 selects ubiquitinated cargoes
            for retrieval from cilia
  JOURNAL   Dev Cell 58 (8), 677-693 (2023)
   PUBMED   37019113
  REMARK    GeneRIF: The ancestral ESCRT protein TOM1L2 selects ubiquitinated
            cargoes for retrieval from cilia.
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 457)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 457)
  AUTHORS   Zhang,Y., Wolf-Yadlin,A., Ross,P.L., Pappin,D.J., Rush,J.,
            Lauffenburger,D.A. and White,F.M.
  TITLE     Time-resolved mass spectrometry of tyrosine phosphorylation sites
            in the epidermal growth factor receptor signaling network reveals
            dynamic modules
  JOURNAL   Mol Cell Proteomics 4 (9), 1240-1250 (2005)
   PUBMED   15951569
REFERENCE   7  (residues 1 to 457)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   8  (residues 1 to 457)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   9  (residues 1 to 457)
  AUTHORS   Bi,W., Yan,J., Stankiewicz,P., Park,S.S., Walz,K., Boerkoel,C.F.,
            Potocki,L., Shaffer,L.G., Devriendt,K., Nowaczyk,M.J., Inoue,K. and
            Lupski,J.R.
  TITLE     Genes in a refined Smith-Magenis syndrome critical deletion
            interval on chromosome 17p11.2 and the syntenic region of the mouse
  JOURNAL   Genome Res 12 (5), 713-728 (2002)
   PUBMED   11997338
REFERENCE   10 (residues 1 to 457)
  AUTHORS   Seranski,P., Heiss,N.S., Dhorne-Pollet,S., Radelof,U., Korn,B.,
            Hennig,S., Backes,E., Schmidt,S., Wiemann,S., Schwarz,C.E.,
            Lehrach,H. and Poustka,A.
  TITLE     Transcription mapping in a medulloblastoma breakpoint interval and
            Smith-Magenis syndrome candidate region: identification of 53
            transcriptional units and new candidate genes
  JOURNAL   Genomics 56 (1), 1-11 (1999)
   PUBMED   10036180
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC051650.1, AC122129.9 and
            BM976586.1.
            
            Summary: This gene belongs to a small gene family whose members
            have an N-terminal VHS domain followed by a GAT domain; domains
            which typically participate in vesicular trafficking. The canonical
            protein encoded by this gene also has a C-terminal clathrin binding
            motif. This protein has been shown to interact with Tollip,
            clathrin and ubiquitin and is thought to play a role in endosomal
            sorting. This gene resides in the 3.7 Mb deletion of chromosome
            region 17p11.2 that is associated with Smith-Magenis syndrome.
            Alternative splicing results in multiple transcript variants
            encoding distinct proteins. [provided by RefSeq, Apr 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.2324549.1, BC051650.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..457
                     /product="TOM1-like protein 2 isoform 1"
                     /note="TOM1-like protein 2; target of myb1-like 2; target
                     of Myb-like protein 2"
                     /calculated_mol_wt=49833
     Region          12..98
                     /region_name="VHS_ENTH_ANTH"
                     /note="VHS, ENTH and ANTH domain superfamily; cl02544"
                     /db_xref="CDD:470608"
     Region          168..259
                     /region_name="GAT_TM1L2"
                     /note="canonical GAT domain found in target of Myb-like
                     protein 2 (Tom1L2); cd14238"
                     /db_xref="CDD:410585"
     Site            order(179..180,183..184,186..187,190..191,194,207,
                     210..211)
                     /site_type="other"
                     /note="putative ubiquitin binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410585"
     CDS             1..457
                     /gene="TOM1L2"
                     /coded_by="NM_001033551.3:88..1461"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32584.1"
                     /db_xref="GeneID:146691"
                     /db_xref="HGNC:HGNC:11984"
                     /db_xref="MIM:615519"
ORIGIN      
        1 mefllgnpfs tpvgqcleka tdgslqsedw tlnmeicdii neteegpkda iralkkrlng
       61 nrnyrevmla ltawadafrs spdltgvvhi yeelkrkgve fpmadldals pihtpqrsvp
      121 evdpaatmpr sqsqqrtsag sysspppapy sapqapalsv tgpitanseq iarlrseldv
      181 vrgntkvmse mltemvpgqe dssdlellqe lnrtcramqq rivelisrvs neevteellh
      241 vnddlnnvfl ryerferyrs grsvqnasng vlnevtednl idlgpgspav vspmvgntap
      301 psslssqlag ldlgtesvsg tlsslqqcnp rdgfdmfaqt rgnslaeqrk tvtyedpqav
      361 gglasaldnr kqssegipva qpsvmddiev wlrtdlkgdd leegvtseef dkfleeraka
      421 aemvpdlpsp pmeapapasn psgrkkpers edalfal
//
LOCUS       NP_001340904             289 aa            linear   PRI 21-NOV-2025
DEFINITION  STAM-binding protein isoform 3 [Homo sapiens].
ACCESSION   NP_001340904 XP_016858666
VERSION     NP_001340904.1
DBSOURCE    REFSEQ: accession NM_001353975.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Zhang,W., Xu,Z., Du,Y., Liu,T., Xiong,Z., Hu,J., Chen,L., Peng,X.
            and Zhou,F.
  TITLE     Identification of STAM-binding protein as a target for the
            treatment of gemcitabine resistance pancreatic cancer in a
            nutrient-poor microenvironment
  JOURNAL   Cell Death Dis 15 (9), 657 (2024)
   PUBMED   39242557
  REMARK    GeneRIF: Identification of STAM-binding protein as a target for the
            treatment of gemcitabine resistance pancreatic cancer in a
            nutrient-poor microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Li,L., Yang,X., He,M., Xu,X., Xuan,X., Zhang,J., Zhang,L., Xu,H.
            and Li,D.
  TITLE     The expression and clinical significance of STAMBP in breast cancer
  JOURNAL   Mol Biol Rep 50 (1), 899-906 (2023)
   PUBMED   36309616
  REMARK    GeneRIF: The expression and clinical significance of STAMBP in
            breast cancer.
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Yang,Q., Yan,D., Zou,C., Xue,Q., Lin,S., Huang,Q., Li,X., Tang,D.,
            Chen,X. and Liu,J.
  TITLE     The deubiquitinating enzyme STAMBP is a newly discovered driver of
            triple-negative breast cancer progression that maintains RAI14
            protein stability
  JOURNAL   Exp Mol Med 54 (11), 2047-2059 (2022)
   PUBMED   36434041
  REMARK    GeneRIF: The deubiquitinating enzyme STAMBP is a newly discovered
            driver of triple-negative breast cancer progression that maintains
            RAI14 protein stability.
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Yu,S., E,C. and Yang,J.
  TITLE     STAM binding protein regulated by hsa_circ_0007334 exerts oncogenic
            potential in pancreatic cancer
  JOURNAL   Pancreatology 22 (7), 1003-1012 (2022)
   PUBMED   36089485
  REMARK    GeneRIF: STAM binding protein regulated by hsa_circ_0007334 exerts
            oncogenic potential in pancreatic cancer.
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Itoh,F., Asao,H., Sugamura,K., Heldin,C.H., ten Dijke,P. and
            Itoh,S.
  TITLE     Promoting bone morphogenetic protein signaling through negative
            regulation of inhibitory Smads
  JOURNAL   EMBO J 20 (15), 4132-4142 (2001)
   PUBMED   11483516
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Endo,K., Takeshita,T., Kasai,H., Sasaki,Y., Tanaka,N., Asao,H.,
            Kikuchi,K., Yamada,M., Chenb,M., O'Shea,J.J. and Sugamura,K.
  TITLE     STAM2, a new member of the STAM family, binding to the Janus
            kinases
  JOURNAL   FEBS Lett 477 (1-2), 55-61 (2000)
   PUBMED   10899310
REFERENCE   8  (residues 1 to 289)
  AUTHORS   Tanaka,N., Kaneko,K., Asao,H., Kasai,H., Endo,Y., Fujita,T.,
            Takeshita,T. and Sugamura,K.
  TITLE     Possible involvement of a novel STAM-associated molecule 'AMSH' in
            intracellular signal transduction mediated by cytokines
  JOURNAL   J Biol Chem 274 (27), 19129-19135 (1999)
   PUBMED   10383417
REFERENCE   9  (residues 1 to 289)
  AUTHORS   Asada,H., Ishii,N., Sasaki,Y., Endo,K., Kasai,H., Tanaka,N.,
            Takeshita,T., Tsuchiya,S., Konno,T. and Sugamura,K.
  TITLE     Grf40, A novel Grb2 family member, is involved in T cell signaling
            through interaction with SLP-76 and LAT
  JOURNAL   J Exp Med 189 (9), 1383-1390 (1999)
   PUBMED   10224278
REFERENCE   10 (residues 1 to 289)
  AUTHORS   Carter,M.T., Mirzaa,G., McDonell,L.M. and Boycott,K.M.
  TITLE     Microcephaly-Capillary Malformation Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24354023
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073046.7.
            
            On Aug 29, 2017 this sequence version replaced XP_016858666.1.
            
            Summary: Cytokine-mediated signal transduction in the JAK-STAT
            cascade requires the involvement of adaptor molecules. One such
            signal-transducing adaptor molecule contains an SH3 domain that is
            required for induction of MYC and cell growth. The protein encoded
            by this gene binds to the SH3 domain of the signal-transducing
            adaptor molecule, and plays a critical role in cytokine-mediated
            signaling for MYC induction and cell cycle progression. Multiple
            alternatively spliced transcript variants encoding the same protein
            isoform have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.944536.1,
                                           SRR18074967.1111778.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..289
                     /product="STAM-binding protein isoform 3"
                     /EC_number="3.1.2.15"
                     /note="associated molecule with the SH3 domain of STAM;
                     endosome-associated ubiquitin isopeptidase; testicular
                     secretory protein Li 54"
                     /calculated_mol_wt=32160
     Region          119..289
                     /region_name="MPN_AMSH_like"
                     /note="Mov34/MPN/PAD-1 family; cd08066"
                     /db_xref="CDD:163697"
     Site            order(145,200,202,210,213)
                     /site_type="active"
                     /note="MPN+ (JAMM) motif [active]"
                     /db_xref="CDD:163697"
     Site            order(147..149,174..178,181..182,185,188,194..195,198,200,
                     202,210,212..213,215..216,219..220,222..223,260)
                     /site_type="other"
                     /note="Distal ubiquitin recognition interface [polypeptide
                     binding]"
                     /db_xref="CDD:163697"
     Site            order(174,202,205..206,208,210..211,260..262)
                     /site_type="active"
                     /note="Proximal ubiquitin recognition interface [active]"
                     /db_xref="CDD:163697"
     Site            order(200,202,213)
                     /site_type="other"
                     /note="Zinc-binding site [ion binding]"
                     /db_xref="CDD:163697"
     CDS             1..289
                     /gene="STAMBP"
                     /gene_synonym="AMSH; MICCAP"
                     /coded_by="NM_001353975.2:782..1651"
                     /note="isoform 3 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS92779.1"
                     /db_xref="GeneID:10617"
                     /db_xref="HGNC:HGNC:16950"
                     /db_xref="MIM:606247"
ORIGIN      
        1 maiqqeleke kqrvaqqkqq qleqeqfhaf eemirnqele kerlkivqef gkvdpglggp
       61 lvpdlekpsl dvfptltvss iqpsdchttv rpakppvvdr slkpgalsns esiptidglr
      121 hvvvpgrlcp qflqlasant argvetcgil cgklmrneft ithvlipkqs agsdycnten
      181 eeelfliqdq qglitlgwih thptqtafls svdlhthcsy qmmlpesvai vcspkfqetg
      241 ffkltdhgle eisscrqkgf hphskdpplf cscshvtvvd ravtitdlr
//
LOCUS       NP_001307066             288 aa            linear   PRI 21-NOV-2025
DEFINITION  large ribosomal subunit protein eL6 isoform 1 [Homo sapiens].
ACCESSION   NP_001307066 XP_006719611
VERSION     NP_001307066.1
DBSOURCE    REFSEQ: accession NM_001320137.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Kennedy,S.A., Jarboui,M.A., Srihari,S., Raso,C., Bryan,K.,
            Dernayka,L., Charitou,T., Bernal-Llinares,M., Herrera-Montavez,C.,
            Krstic,A., Matallanas,D., Kotlyar,M., Jurisica,I., Curak,J.,
            Wong,V., Stagljar,I., LeBihan,T., Imrie,L., Pillai,P., Lynn,M.A.,
            Fasterius,E., Al-Khalili Szigyarto,C., Breen,J., Kiel,C.,
            Serrano,L., Rauch,N., Rukhlenko,O., Kholodenko,B.N.,
            Iglesias-Martinez,L.F., Ryan,C.J., Pilkington,R., Cammareri,P.,
            Sansom,O., Shave,S., Auer,M., Horn,N., Klose,F., Ueffing,M.,
            Boldt,K., Lynn,D.J. and Kolch,W.
  TITLE     Extensive rewiring of the EGFR network in colorectal cancer cells
            expressing transforming levels of KRASG13D
  JOURNAL   Nat Commun 11 (1), 499 (2020)
   PUBMED   31980649
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Wei,J., Kishton,R.J., Angel,M., Conn,C.S., Dalla-Venezia,N.,
            Marcel,V., Vincent,A., Catez,F., Ferre,S., Ayadi,L., Marchand,V.,
            Dersh,D., Gibbs,J.S., Ivanov,I.P., Fridlyand,N., Coute,Y.,
            Diaz,J.J., Qian,S.B., Staudt,L.M., Restifo,N.P. and Yewdell,J.W.
  TITLE     Ribosomal Proteins Regulate MHC Class I Peptide Generation for
            Immunosurveillance
  JOURNAL   Mol Cell 73 (6), 1162-1173 (2019)
   PUBMED   30712990
  REMARK    GeneRIF: 60S ribosomal proteins L6 (RPL6) and RPL28, which are
            adjacent on the ribosome, play opposite roles in generating an
            influenza A virus-encoded peptide. Depleting RPL6 decreases
            ubiquitin-dependent peptide presentation, whereas depleting RPL28
            increases ubiquitin-dependent and -independent peptide
            presentation.
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Ohta,K., Endo,T., Gunji,K. and Onaya,T.
  TITLE     Isolation of a cDNA whose expression is markedly increased in
            malignantly transformed FRTL cells and neoplastic human thyroid
            tissues
  JOURNAL   J Mol Endocrinol 12 (1), 85-92 (1994)
   PUBMED   8185817
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Zaman,G.J.
  TITLE     Sequence of a cDNA encoding human ribosomal protein L26 and of a
            cDNA probably encoding human ribosomal protein L6
  JOURNAL   Nucleic Acids Res 21 (7), 1673 (1993)
   PUBMED   8479925
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Morita,T., Sato,T., Nyunoya,H., Tsujimoto,A., Takahara,J., Irino,S.
            and Shimotohno,K.
  TITLE     Isolation of a cDNA clone encoding DNA-binding protein (TAXREB107)
            that binds specifically to domain C of the tax-responsive enhancer
            element in the long terminal repeat of human T-cell leukemia virus
            type I
  JOURNAL   AIDS Res Hum Retroviruses 9 (2), 115-121 (1993)
   PUBMED   8457378
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Nika,H. and Hultin,T.
  TITLE     Location of the sulfhydryl groups involved in disulfide interaction
            between the neighboring proteins L6 and L29 in mammalian ribosomes.
            S-cleavage of the cyanylated proteins in polyacrylamide gels after
            separation by dodecylsulfate gel electrophoresis
  JOURNAL   Eur J Biochem 142 (3), 521-526 (1984)
   PUBMED   6468376
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Todokoro,K., Ulbrich,N., Chan,Y.L. and Wool,I.G.
  TITLE     Characterization of the binding of rat liver ribosomal proteins L6,
            L8, L19, S9, and S13 to 5.8 S ribosomal ribonucleic acid
  JOURNAL   J Biol Chem 256 (14), 7207-7212 (1981)
   PUBMED   7251593
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP285025.1, CB140996.1,
            CD049618.1, BC004138.2 and AI583261.1.
            
            On Feb 12, 2016 this sequence version replaced XP_006719611.1.
            
            Summary: This gene encodes a protein component of the 60S ribosomal
            subunit. This protein can bind specifically to domain C of the
            tax-responsive enhancer element of human T-cell leukemia virus type
            1, and may participate in tax-mediated transactivation of
            transcription. As is typical for genes encoding ribosomal proteins,
            there are multiple processed pseudogenes of this gene dispersed
            throughout the genome. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, 3, 4, 5, 6, and 7 encode the same
            isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.113846.1,
                                           SRR1163657.213055.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.13"
     Protein         1..288
                     /product="large ribosomal subunit protein eL6 isoform 1"
                     /note="60S ribosomal protein L6; tax-responsive enhancer
                     element-binding protein 107; DNA-binding protein
                     TAXREB107; neoplasm-related protein C140; large ribosomal
                     subunit protein eL6"
                     /calculated_mol_wt=32597
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02878.3)"
     Region          36..95
                     /region_name="Ribosomal_L6e_N"
                     /note="Ribosomal protein L6, N-terminal domain; pfam03868"
                     /db_xref="CDD:427554"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679; propagated from
                     UniProtKB/Swiss-Prot (Q02878.3)"
     Region          136..288
                     /region_name="KOW_RPL6"
                     /note="KOW motif of Ribosomal Protein L6; cd13156"
                     /db_xref="CDD:240520"
     Site            order(136,138,154..158,160,171..172,179..183,185,187..190,
                     192..193,219,243,246..247,269,272..274,278..279)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:240520"
     Site            239
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q02878.3)"
     CDS             1..288
                     /gene="RPL6"
                     /gene_synonym="eL6; L6; SHUJUN-2; TAXREB107; TXREB1"
                     /coded_by="NM_001320137.2:210..1076"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS9162.1"
                     /db_xref="GeneID:6128"
                     /db_xref="HGNC:HGNC:10362"
                     /db_xref="MIM:603703"
ORIGIN      
        1 magekvekpd tkekkpeakk vdaggkvkkg nlkakkpkkg kphcsrnpvl vrgigrysrs
       61 amysrkamyk rkysaakskv ekkkkekvla tvtkpvggdk nggtrvvklr kmpryypted
      121 vprkllshgk kpfsqhvrkl rasitpgtil iiltgrhrgk rvvflkqlas glllvtgplv
      181 lnrvplrrth qkfviatstk idisnvkipk hltdayfkkk klrkprhqeg eifdtekeky
      241 eiteqrkidq kavdsqilpk ikaipqlqgy lrsvfaltng iyphklvf
//
LOCUS       NP_001337391            1027 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 1 isoform 56 [Homo
            sapiens].
ACCESSION   NP_001337391
VERSION     NP_001337391.1
DBSOURCE    REFSEQ: accession NM_001350462.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1027)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1027)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1027)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 1027)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 1027)
  AUTHORS   Ruhle,F., Witten,A., Barysenka,A., Huge,A., Arning,A., Heller,C.,
            Krumpel,A., Mesters,R., Franke,A., Lieb,W., Riemenschneider,M.,
            Hiersche,M., Limperger,V., Nowak-Gottl,U. and Stoll,M.
  TITLE     Rare genetic variants in SMAP1, B3GAT2, and RIMS1 contribute to
            pediatric venous thromboembolism
  JOURNAL   Blood 129 (6), 783-790 (2017)
   PUBMED   28011674
  REMARK    GeneRIF: The study identified a region on chromosome 6 comprising
            the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus
            for pediatric venous thromboembolism.
REFERENCE   6  (residues 1 to 1027)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 1027)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
REFERENCE   8  (residues 1 to 1027)
  AUTHORS   Schoch,S., Castillo,P.E., Jo,T., Mukherjee,K., Geppert,M., Wang,Y.,
            Schmitz,F., Malenka,R.C. and Sudhof,T.C.
  TITLE     RIM1alpha forms a protein scaffold for regulating neurotransmitter
            release at the active zone
  JOURNAL   Nature 415 (6869), 321-326 (2002)
   PUBMED   11797009
REFERENCE   9  (residues 1 to 1027)
  AUTHORS   Coppola,T., Magnin-Luthi,S., Perret-Menoud,V., Gattesco,S.,
            Schiavo,G. and Regazzi,R.
  TITLE     Direct interaction of the Rab3 effector RIM with Ca2+ channels,
            SNAP-25, and synaptotagmin
  JOURNAL   J Biol Chem 276 (35), 32756-32762 (2001)
   PUBMED   11438518
REFERENCE   10 (residues 1 to 1027)
  AUTHORS   Betz,A., Thakur,P., Junge,H.J., Ashery,U., Rhee,J.S., Scheuss,V.,
            Rosenmund,C., Rettig,J. and Brose,N.
  TITLE     Functional interaction of the active zone proteins Munc13-1 and
            RIM1 in synaptic vesicle priming
  JOURNAL   Neuron 30 (1), 183-196 (2001)
   PUBMED   11343654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590011.5, AL445256.18 and
            AL035633.18.
            
            Summary: The protein encoded by this gene is a RAS gene superfamily
            member that regulates synaptic vesicle exocytosis. This gene also
            plays a role in the regulation of voltage-gated calcium channels
            during neurotransmitter and insulin release. Mutations have
            suggested a role cognition and have been identified as the cause of
            cone-rod dystrophy type 7. Multiple transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Mar 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.87543.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1027
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..1027
                     /product="regulating synaptic membrane exocytosis protein
                     1 isoform 56"
                     /note="RAB3-interacting protein 2; rab3-interacting
                     molecule 1; rab-3-interacting protein 2"
                     /calculated_mol_wt=114454
     Region          45..141
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(66..72,87,90,120,124,127..128)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          193..319
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(224,230,285,287,295)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          858..1003
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(915,919..920,922,925,953,955,957,1001..1002)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..1027
                     /gene="RIMS1"
                     /gene_synonym="CORD7; RAB3IP2; RIM; RIM1"
                     /coded_by="NM_001350462.2:176..3259"
                     /note="isoform 56 is encoded by transcript variant 56"
                     /db_xref="GeneID:22999"
                     /db_xref="HGNC:HGNC:17282"
                     /db_xref="MIM:606629"
ORIGIN      
        1 meysvsmwkp gdldyywldp atwhsretsp isshpvtwqp skegdrligr vilnkrttmp
       61 kdsgallglk vvggkmtdlg rlgafitkvk kgsladvvgh lragdevlew ngkplpgatn
      121 eevyniiles ksepqveiiv srpigdipri pesshpples ssssfesqkm erpsisvisp
      181 tspgalkdap qvlpgqlsvk lwydkvghql ivnvlqatdl parvdgrprn pyvkmyflpd
      241 rsdkskrrtk tvkkilepkw nqtfvyshvh rrdfrermle itvwdqprvq eeeseflgei
      301 lieletalld dephwyklqt hdesslplpq pspfmprrhi hgessskklq rsqrisdsdi
      361 sdyevddgig vvppvgyrss aresksttlt vpeqqrtthh rsrsvsphrg ndqgkprsrl
      421 pnvplqrsld eihptrrsrs ptrhhdasrs pvdhrtrdvd sqylseqdse llmlprakrg
      481 rsaeclhtts elqpfldrar sastnclrpd tslhsperer vlptclsrrg haapratdqp
      541 virgkhpars rssehssirt lcsmhhlvpg gsappspllt rmhrqrsptq sppadtsfss
      601 rrgrqlpqvp vrsgsieqas lvveertrqm kmkvhrfkqt tgsgssqeld reqyskynih
      661 kdqyrscdnv sakssdsdvs dvsaisrtss asrlsstsfm seqserprgr issftpkmqg
      721 rrmgtsgrsi mkstsvsgem ytlehndgsq sdtavgtvga ggkkrrssls akvvaivsrr
      781 srstsqlsqt esghkklkst iqrstetgma aemrkmvrqp srestdgsin syssegnlif
      841 pgvrlgadsq fsdfldglgp aqlvgrqtla tpamgdiqig medkkgqlev evirarsltq
      901 kpgskstpap yvkvylleng aciakkktri arktldplyq qslvfdespq gkvlqvivwg
      961 dygrmdhkcf mgvaqillee ldlssmvigw yklfppsslv dptltpltrr asqsslesst
     1021 gppcirs
//
LOCUS       NP_001371803            1083 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 64 [Homo sapiens].
ACCESSION   NP_001371803
VERSION     NP_001371803.1
DBSOURCE    REFSEQ: accession NM_001384874.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1083)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1083)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1083)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1083)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1083)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1083)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1083)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1083
                     /product="microtubule-associated protein 4 isoform 64"
                     /note="MAP-4"
                     /calculated_mol_wt=113843
     Region          <545..889
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <901..922
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          924..953
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          955..984
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          986..1016
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1083
                     /gene="MAP4"
                     /coded_by="NM_001384874.1:96..3347"
                     /note="isoform 64 is encoded by transcript variant 120"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgsp tefleekmay qeypnsqnwp
      121 edtnfcfqpe qvvdpiqtdp fkmyhdddla dlvfpssata dtsifagqnd plkdsyeava
      181 eppqptavpl elakeiemas eerppaqale immglkttdm apsketemal akdmalatkt
      241 evalakdmes ptkldvtlak dmqpsmesdm alvkdmelpt ekevalvkdv rwptetdvss
      301 aknvvlptet evapakdvtl lketeraspi kmdlapskdm gppkenkket eraspikmdl
      361 apskdmgppk enkivpakdl vllseievaq andiisstei ssaekvalss etevalardm
      421 tlppetnvil tkdkalplea evapvkdmaq lpeteiapak dvapstvkev gllkdmspls
      481 etemalgkdv tpppetevvl iknvclppem evaltedqvp alkteaplak dgvltlannv
      541 tpakdvppls eteatpvpik dmeiaqtqkg isedshlesl qdvgqsaapt fmispetvtg
      601 tgkkcslpae edsvleklge rkpcnsqpse lssetsgiar peegrpvvsg tgndittppn
      661 kelppspekk tkplattqpa ktstskaktq ptslpkqpap ttigglnkkp mslasglvpa
      721 appkrpavas arpsilpskd vkpkpiadak apekraspsk pasapasrsg skstqtvakt
      781 ttaaavastg pssrspstll pkkptaikte gkpaevkkmt aksvpadlsr pkststssmk
      841 ktttlsgtap aagvvpsrvk atpmpsrpst tpfidkkpts akpssttprl srlatntsap
      901 dlknvrskvg stenikhqpg ggrvqivskk vsyshiqskc gskdnikhvp gggnvqiqnk
      961 kvdiskvssk cgskanikhk pgggdvkies qklnfkekaq akvgsldnvg hlpaggavkt
     1021 egggseaplc pgppageepa iseaapeaga ptsasglngh ptlsgggdqr eaqtldsqiq
     1081 etn
//
LOCUS       NP_000222                291 aa            linear   PRI 21-NOV-2025
DEFINITION  gamma-sarcoglycan isoform 1 [Homo sapiens].
ACCESSION   NP_000222
VERSION     NP_000222.2
DBSOURCE    REFSEQ: accession NM_000231.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Zhu,Y., Burg,T., Neyrinck,K., Vervliet,T., Nami,F., Vervoort,E.,
            Ahuja,K., Sassano,M.L., Chai,Y.C., Tharkeshwar,A.K., De Smedt,J.,
            Hu,H., Bultynck,G., Agostinis,P., Swinnen,J.V., Van Den Bosch,L.,
            da Costa,R.F.M. and Verfaillie,C.
  TITLE     Disruption of MAM integrity in mutant FUS oligodendroglial
            progenitors from hiPSCs
  JOURNAL   Acta Neuropathol 147 (1), 6 (2024)
   PUBMED   38170217
  REMARK    GeneRIF: Disruption of MAM integrity in mutant FUS oligodendroglial
            progenitors from hiPSCs.
            Erratum:[Acta Neuropathol. 2024 Jun 13;147(1):99. doi:
            10.1007/s00401-024-02748-4. PMID: 38871840]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Pluta,N., Hoffjan,S., Zimmer,F., Kohler,C., Lucke,T., Mohr,J.,
            Vorgerd,M., Nguyen,H.H.P., Atlan,D., Wolf,B., Zaum,A.K. and Rost,S.
  TITLE     Homozygous Inversion on Chromosome 13 Involving SGCG Detected by
            Short Read Whole Genome Sequencing in a Patient Suffering from
            Limb-Girdle Muscular Dystrophy
  JOURNAL   Genes (Basel) 13 (10), 1752 (2022)
   PUBMED   36292638
  REMARK    GeneRIF: Homozygous Inversion on Chromosome 13 Involving SGCG
            Detected by Short Read Whole Genome Sequencing in a Patient
            Suffering from Limb-Girdle Muscular Dystrophy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Nikpay,M., Lau,P., Soubeyrand,S., Whytock,K.L., Beehler,K.,
            Pileggi,C., Ghosh,S., Harper,M.E., Dent,R. and McPherson,R.
  TITLE     SGCG rs679482 Associates With Weight Loss Success in Response to an
            Intensively Supervised Outpatient Program
  JOURNAL   Diabetes 69 (9), 2017-2026 (2020)
   PUBMED   32527767
  REMARK    GeneRIF: SGCG rs679482 Associates With Weight Loss Success in
            Response to an Intensively Supervised Outpatient Program.
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Jamaleddine,M., Harris,M.S., Liyanage,L. and Cook,G.A.
  TITLE     Expression, purification, and structural analysis of the
            full-length human integral membrane protein gamma-sarcoglycan
  JOURNAL   Protein Expr Purif 167, 105525 (2020)
   PUBMED   31682967
  REMARK    GeneRIF: Expression, purification, and structural analysis of the
            full-length human integral membrane protein gamma-sarcoglycan.
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Jung,D., Leturcq,F., Sunada,Y., Duclos,F., Tome,F.M., Moomaw,C.,
            Merlini,L., Azibi,K., Chaouch,M., Slaughter,C., Fardeau,M.,
            Kaplan,J.C. and Campbell,K.P.
  TITLE     Absence of gamma-sarcoglycan (35 DAG) in autosomal recessive
            muscular dystrophy linked to chromosome 13q12
  JOURNAL   FEBS Lett 381 (1-2), 15-20 (1996)
   PUBMED   8641426
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Noguchi,S., McNally,E.M., Ben Othmane,K., Hagiwara,Y., Mizuno,Y.,
            Yoshida,M., Yamamoto,H., Bonnemann,C.G., Gussoni,E., Denton,P.H.,
            Kyriakides,T., Middleton,L., Hentati,F., Ben Hamida,M., Nonaka,I.,
            Vance,J.M., Kunkel,L.M. and Ozawa,E.
  TITLE     Mutations in the dystrophin-associated protein gamma-sarcoglycan in
            chromosome 13 muscular dystrophy
  JOURNAL   Science 270 (5237), 819-822 (1995)
   PUBMED   7481775
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Ben Othmane,K., Speer,M.C., Stauffer,J., Blel,S., Middleton,L., Ben
            Hamida,C., Etribi,A., Loeb,D., Hentati,F., Roses,A.D. et al.
  TITLE     Evidence for linkage disequilibrium in chromosome 13-linked
            Duchenne-like muscular dystrophy (LGMD2C)
  JOURNAL   Am J Hum Genet 57 (3), 732-734 (1995)
   PUBMED   7668303
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Jorde,L.B., Watkins,W.S., Viskochil,D., O'Connell,P. and Ward,K.
  TITLE     Linkage disequilibrium in the neurofibromatosis 1 (NF1) region:
            implications for gene mapping
  JOURNAL   Am J Hum Genet 53 (5), 1038-1050 (1993)
   PUBMED   8105688
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL356287.16, DA897096.1,
            BC074778.2, AL157766.9 and U34976.1.
            
            On Feb 4, 2020 this sequence version replaced NP_000222.1.
            
            Summary: This gene encodes gamma-sarcoglycan, one of several
            sarcolemmal transmembrane glycoproteins that interact with
            dystrophin. The dystrophin-glycoprotein complex (DGC) spans the
            sarcolemma and is comprised of dystrophin, syntrophin, alpha- and
            beta-dystroglycans and sarcoglycans. The DGC provides a structural
            link between the subsarcolemmal cytoskeleton and the extracellular
            matrix of muscle cells. Defects in the encoded protein can lead to
            early onset autosomal recessive muscular dystrophy, in particular
            limb-girdle muscular dystrophy, type 2C (LGMD2C). [provided by
            RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U34976.1, BC109321.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2147596
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000218867.4/ ENSP00000218867.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.12"
     Protein         1..291
                     /product="gamma-sarcoglycan isoform 1"
                     /note="35kD dystrophin-associated glycoprotein;
                     gamma-sarcoglycan; 35 kDa dystrophin-associated
                     glycoprotein; sarcoglycan, gamma (35kDa
                     dystrophin-associated glycoprotein)"
                     /calculated_mol_wt=32248
     Region          25..278
                     /region_name="Sarcoglycan_1"
                     /note="Sarcoglycan complex subunit protein; pfam04790"
                     /db_xref="CDD:461428"
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13326.4)"
     Site            110
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13326.4)"
     CDS             1..291
                     /gene="SGCG"
                     /gene_synonym="35DAG; A4; DAGA4; DMDA; DMDA1; gamma-SG;
                     LGMD2C; LGMDR5; MAM; SCARMD2"
                     /coded_by="NM_000231.3:98..973"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9299.1"
                     /db_xref="GeneID:6445"
                     /db_xref="HGNC:HGNC:10809"
                     /db_xref="MIM:608896"
ORIGIN      
        1 mvreqyttat egicierpen qyvykigiyg wrkrclylfv lllliilvvn laltiwilkv
       61 mwfspagmgh lcvtkdglrl egeseflfpl yakeihsrvd sslllqstqn vtvnarnseg
      121 evtgrlkvgp kmvevqnqqf qinsndgkpl ftvdekevvv gtdklrvtgp egalfehsve
      181 tplvradpfq dlrlesptrs lsmdaprgvh iqahagkiea lsqmdilfhs sdgmlvldae
      241 tvclpklvqg twgpsgssqs lyeicvcpdg klylsvagvs ttcqehnhic l
//
LOCUS       NP_001295041             585 aa            linear   PRI 21-NOV-2025
DEFINITION  kelch-like protein 28 isoform 1 [Homo sapiens].
ACCESSION   NP_001295041 XP_005267826
VERSION     NP_001295041.1
DBSOURCE    REFSEQ: accession NM_001308112.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL049870.3, BC057794.1, AK289855.1 and HY342026.1.
            
            On Apr 22, 2015 this sequence version replaced XP_005267826.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1314195.1, BC057794.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q21.2"
     Protein         1..585
                     /product="kelch-like protein 28 isoform 1"
                     /note="BTB (POZ) domain containing 5; kelch-like protein
                     28; BTB/POZ domain-containing protein 5; kelch-like 28"
                     /calculated_mol_wt=65822
     Region          49..567
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          335..386
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          390..433
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          437..479
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          483..527
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          530..573
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     CDS             1..585
                     /gene="KLHL28"
                     /gene_synonym="BTBD5"
                     /coded_by="NM_001308112.2:558..2315"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS76675.1"
                     /db_xref="GeneID:54813"
                     /db_xref="HGNC:HGNC:19741"
ORIGIN      
        1 mhfkckysyp alyqmdhtsp tymlanlthl hseqllqgln llrqhhelcd iilrvgdvki
       61 hahkvvlasv spyfkamftg nlsekensev efqcidetal qaiveyaytg tvfisqdtve
      121 sllpaanllq iklvlkecca flesqldpgn cigisrfaet ygcrdlylaa tkyicqnfea
      181 vcqteeffel thadldeivs ndclnvatee tvfyaleswi kydvqerqky laqllnsvrl
      241 pllsvkfltr lyeanhlird drtckhllne alkyhfmpeh rlshqtvlmt rprcapkvlc
      301 avggksglfa cldsvemyfp qndswiglap lnipryefgi cvldqkvyvi ggiatnvrpg
      361 vtirkhensv ecwnpdtntw tslermnesr stlgvvvlag elyalggydg qsylqsveky
      421 ipkirkwqpv apmtttrscf aaavldgmiy aiggygpahm nsverydpsk dswemvasma
      481 dkrihfgvgv mlgfifvvgg hngvshlssi erydphqnqw tvcrpmkepr tgvgaavidn
      541 ylyvvgghsg ssylntvqky dpisdtwlds agmiycrcnf gltal
//
LOCUS       NP_004010                340 aa            linear   PRI 21-NOV-2025
DEFINITION  dystrophin isoform Dp40 [Homo sapiens].
ACCESSION   NP_004010
VERSION     NP_004010.1
DBSOURCE    REFSEQ: accession NM_004019.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Chen,L., Luo,X., Wang,H., Tian,Y. and Liu,Y.
  TITLE     Identifying inversions with breakpoints in the Dystrophin gene
            through long-read sequencing: report of two cases
  JOURNAL   BMC Med Genomics 17 (1), 227 (2024)
   PUBMED   39251998
  REMARK    GeneRIF: Identifying inversions with breakpoints in the Dystrophin
            gene through long-read sequencing: report of two cases.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Davies,K.E. and Vogt,J.
  TITLE     Long-term clinical follow-up of a family with Becker muscular
            dystrophy associated with a large deletion in the DMD gene
  JOURNAL   Neuromuscul Disord 39, 5-9 (2024)
   PUBMED   38653179
  REMARK    GeneRIF: Long-term clinical follow-up of a family with Becker
            muscular dystrophy associated with a large deletion in the DMD
            gene.
            Erratum:[Neuromuscul Disord. 2024 Jun;39:54. doi:
            10.1016/j.nmd.2024.05.010. PMID: 38801812]
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Achermann,J.C. and Vilain,E.J.
  TITLE     NR0B1-Related Adrenal Hypoplasia Congenita
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301604
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Darras,B.T., Urion,D.K. and Ghosh,P.S.
  TITLE     Dystrophinopathies
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301298
REFERENCE   7  (residues 1 to 340)
  AUTHORS   Nigro,V., Politano,L., Nigro,G., Romano,S.C., Molinari,A.M. and
            Puca,G.A.
  TITLE     Detection of a nonsense mutation in the dystrophin gene by multiple
            SSCP
  JOURNAL   Hum Mol Genet 1 (7), 517-520 (1992)
   PUBMED   1307253
REFERENCE   8  (residues 1 to 340)
  AUTHORS   Gorecki,D.C., Monaco,A.P., Derry,J.M., Walker,A.P., Barnard,E.A.
            and Barnard,P.J.
  TITLE     Expression of four alternative dystrophin transcripts in brain
            regions regulated by different promoters
  JOURNAL   Hum Mol Genet 1 (7), 505-510 (1992)
   PUBMED   1307251
REFERENCE   9  (residues 1 to 340)
  AUTHORS   Lederfein,D., Levy,Z., Augier,N., Mornet,D., Morris,G., Fuchs,O.,
            Yaffe,D. and Nudel,U.
  TITLE     A 71-kilodalton protein is a major product of the Duchenne muscular
            dystrophy gene in brain and other nonmuscle tissues
  JOURNAL   Proc Natl Acad Sci U S A 89 (12), 5346-5350 (1992)
   PUBMED   1319059
REFERENCE   10 (residues 1 to 340)
  AUTHORS   Koenig,M., Monaco,A.P. and Kunkel,L.M.
  TITLE     The complete sequence of dystrophin predicts a rod-shaped
            cytoskeletal protein
  JOURNAL   Cell 53 (2), 219-228 (1988)
   PUBMED   3282674
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078958.30, S42206.1 and
            M18533.1.
            
            Summary: This gene spans a genomic range of greater than 2 Mb and
            encodes a large protein containing an N-terminal actin-binding
            domain and multiple spectrin repeats. The encoded protein forms a
            component of the dystrophin-glycoprotein complex (DGC), which
            bridges the inner cytoskeleton and the extracellular matrix.
            Deletions, duplications, and point mutations at this gene locus may
            cause Duchenne muscular dystrophy (DMD), Becker muscular dystrophy
            (BMD), or cardiomyopathy. Alternative promoter usage and
            alternative splicing result in numerous distinct transcript
            variants and protein isoforms for this gene. [provided by RefSeq,
            Dec 2016].
            
            Transcript Variant: transcript Dp40 uses exons 63-70. The 5' UTR
            and encoded first 7 aa are identical to that in transcript Dp71,
            but the stop codon lies at the splice junction of the exon/intron
            70. The 3' UTR includes nt from intron 70 which includes an
            alternative polyadenylation site. The Dp40 isoform lacks the normal
            C-terminal end of full-length dystrophin (aa 3409-3685).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.310007.1,
                                           SRR14038191.1877313.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp21.2-p21.1"
     Protein         1..340
                     /product="dystrophin isoform Dp40"
                     /note="mutant dystrophin"
                     /calculated_mol_wt=39123
     Region          1..7
                     /region_name="dystrophin Dp71/40 unique N-terminus"
     Site            12..340
                     /site_type="binding"
                     /note="dystroglycan binding site"
     Region          32..232
                     /region_name="Cysteine-rich domain"
     Region          57..218
                     /region_name="EFh_DMD"
                     /note="EF-hand-like motif found in dystrophin; cd16246"
                     /db_xref="CDD:320004"
     Site            order(57..58,60..61,79,83,87,89..90,93,104..110,112..113,
                     116,122,135,176..177,179)
                     /site_type="other"
                     /note="Domain interface"
                     /db_xref="CDD:320004"
     Region          57..96
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          62..89
                     /region_name="EF-hand 1"
     Region          103..137
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          110..138
                     /region_name="EF-hand 2"
     Site            120..122
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:320004"
     Region          143..179
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          192..218
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          239..286
                     /region_name="ZZ-domain"
     Region          243..291
                     /region_name="ZZ_dystrophin"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     dystrophin and dystrobrevin. The ZZ motif coordinates two
                     zinc ions and most likely participates in ligand binding
                     or molecular scaffolding. Dystrophin attaches actin
                     filaments to an integral membrane...; cd02334"
                     /db_xref="CDD:239074"
     Site            order(245,248,260,263,269,272,282,286)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(245,248,269,272)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(246,257,259,265,267)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(258,273,288,291)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(260,263,282,286)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239074"
     CDS             1..340
                     /gene="DMD"
                     /gene_synonym="BMD; CMD3B; DXS142; DXS164; DXS206; DXS230;
                     DXS239; DXS268; DXS269; DXS270; DXS272; MRX85"
                     /coded_by="NM_004019.3:126..1148"
                     /note="isoform Dp40 is encoded by transcript variant Dp40"
                     /db_xref="GeneID:1756"
                     /db_xref="HGNC:HGNC:2928"
                     /db_xref="MIM:300377"
ORIGIN      
        1 mreqlkghet qttcwdhpkm telyqsladl nnvrfsayrt amklrrlqka lcldllslsa
       61 acdaldqhnl kqndqpmdil qiinclttiy drleqehnnl vnvplcvdmc lnwllnvydt
      121 grtgrirvls fktgiislck ahledkyryl fkqvasstgf cdqrrlglll hdsiqiprql
      181 gevasfggsn iepsvrscfq fannkpeiea alfldwmrle pqsmvwlpvl hrvaaaetak
      241 hqakcnicke cpiigfryrs lkhfnydicq scffsgrvak ghkmhypmve yctpttsged
      301 vrdfakvlkn kfrtkryfak hprmgylpvq tvlegdnmet
//
LOCUS       NP_001374639            1040 aa            linear   PRI 21-NOV-2025
DEFINITION  activated CDC42 kinase 1 isoform 8 [Homo sapiens].
ACCESSION   NP_001374639
VERSION     NP_001374639.1
DBSOURCE    REFSEQ: accession NM_001387710.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1040)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1040)
  AUTHORS   Zheng,D., Wei,Z., Zhang,C., Liu,W., Gong,C., Wu,F. and Guo,W.
  TITLE     ZNF692 promotes osteosarcoma cell proliferation, migration, and
            invasion through TNK2-mediated activation of the MEK/ERK pathway
  JOURNAL   Biol Direct 19 (1), 28 (2024)
   PUBMED   38650011
  REMARK    GeneRIF: ZNF692 promotes osteosarcoma cell proliferation,
            migration, and invasion through TNK2-mediated activation of the
            MEK/ERK pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1040)
  AUTHORS   Hodder,S., Fox,M., Binti Ahmad Mokhtar,A.M., Mott,H.R. and Owen,D.
  TITLE     ACKnowledging the role of the Activated-Cdc42 associated kinase
            (ACK) in regulating protein stability in cancer
  JOURNAL   Small GTPases 14 (1), 14-25 (2023)
   PUBMED   37194323
  REMARK    GeneRIF: ACKnowledging the role of the Activated-Cdc42 associated
            kinase (ACK) in regulating protein stability in cancer.
            Review article
REFERENCE   4  (residues 1 to 1040)
  AUTHORS   Zhou,A., Zhang,W. and Wang,B.
  TITLE     Host factor TNK2 is required for influenza virus infection
  JOURNAL   Genes Genomics 45 (6), 771-781 (2023)
   PUBMED   37133719
  REMARK    GeneRIF: Host factor TNK2 is required for influenza virus
            infection.
REFERENCE   5  (residues 1 to 1040)
  AUTHORS   Kan,Y., Paung,Y., Seeliger,M.A. and Miller,W.T.
  TITLE     Domain Architecture of the Nonreceptor Tyrosine Kinase Ack1
  JOURNAL   Cells 12 (6), 900 (2023)
   PUBMED   36980241
  REMARK    GeneRIF: Domain Architecture of the Nonreceptor Tyrosine Kinase
            Ack1.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1040)
  AUTHORS   Kato,J., Kaziro,Y. and Satoh,T.
  TITLE     Activation of the guanine nucleotide exchange factor Dbl following
            ACK1-dependent tyrosine phosphorylation
  JOURNAL   Biochem Biophys Res Commun 268 (1), 141-147 (2000)
   PUBMED   10652228
REFERENCE   7  (residues 1 to 1040)
  AUTHORS   Eisenmann,K.M., McCarthy,J.B., Simpson,M.A., Keely,P.J., Guan,J.L.,
            Tachibana,K., Lim,L., Manser,E., Furcht,L.T. and Iida,J.
  TITLE     Melanoma chondroitin sulphate proteoglycan regulates cell spreading
            through Cdc42, Ack-1 and p130cas
  JOURNAL   Nat Cell Biol 1 (8), 507-513 (1999)
   PUBMED   10587647
REFERENCE   8  (residues 1 to 1040)
  AUTHORS   Mott,H.R., Owen,D., Nietlispach,D., Lowe,P.N., Manser,E., Lim,L.
            and Laue,E.D.
  TITLE     Structure of the small G protein Cdc42 bound to the GTPase-binding
            domain of ACK
  JOURNAL   Nature 399 (6734), 384-388 (1999)
   PUBMED   10360579
REFERENCE   9  (residues 1 to 1040)
  AUTHORS   Satoh,T., Kato,J., Nishida,K. and Kaziro,Y.
  TITLE     Tyrosine phosphorylation of ACK in response to temperature
            shift-down, hyperosmotic shock, and epidermal growth factor
            stimulation
  JOURNAL   FEBS Lett 386 (2-3), 230-234 (1996)
   PUBMED   8647288
REFERENCE   10 (residues 1 to 1040)
  AUTHORS   Manser,E., Leung,T., Salihuddin,H., Tan,L. and Lim,L.
  TITLE     A non-receptor tyrosine kinase that inhibits the GTPase activity of
            p21cdc42
  JOURNAL   Nature 363 (6427), 364-367 (1993)
   PUBMED   8497321
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124944.8.
            
            Summary: This gene encodes a tyrosine kinase that binds Cdc42Hs in
            its GTP-bound form and inhibits both the intrinsic and
            GTPase-activating protein (GAP)-stimulated GTPase activity of
            Cdc42Hs. This binding is mediated by a unique sequence of 47 amino
            acids C-terminal to an SH3 domain. The protein may be involved in a
            regulatory mechanism that sustains the GTP-bound active form of
            Cdc42Hs and which is directly linked to a tyrosine phosphorylation
            signal transduction pathway. Several alternatively spliced
            transcript variants have been identified from this gene, but the
            full-length nature of only two transcript variants has been
            determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4099922.1,
                                           SRR14038193.1293537.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1040
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..1040
                     /product="activated CDC42 kinase 1 isoform 8"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="activated p21cdc42Hs kinase; activated
                     Cdc42-associated kinase 1; tyrosine kinase non-receptor
                     protein 2"
                     /calculated_mol_wt=114679
     Region          1..110
                     /region_name="SAM-like domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          6..67
                     /region_name="SAM_TNK-like"
                     /note="SAM domain of TNK(ACK)-like non-receptor
                     tyrosine-protein kinases; cd09539"
                     /db_xref="CDD:188938"
     Region          90..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          130..387
                     /region_name="PTKc_Ack_like"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Activated Cdc42-associated kinase; cd05040"
                     /db_xref="CDD:270636"
     Site            order(132..134,140,156,158,205..208,212,252,256..257,259,
                     270,289..293,302,336)
                     /site_type="active"
                     /db_xref="CDD:270636"
     Site            order(132..134,140,156,158,205..208,212,252,256..257,259,
                     270)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270636"
     Site            order(252,256,289..293,302,336)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270636"
     Site            order(269..279,281..295)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270636"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000269|PubMed:15308621,
                     ECO:0000269|PubMed:16472662, ECO:0000269|PubMed:20333297,
                     ECO:0000269|PubMed:20623637, ECO:0000269|PubMed:20979614,
                     ECO:0000269|PubMed:21169560, ECO:0000269|PubMed:21309750,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Region          395..444
                     /region_name="SH3_9"
                     /note="Variant SH3 domain; pfam14604"
                     /db_xref="CDD:434066"
     Site            order(397,399,404,422,424,439,441..442)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212754"
     Region          449..514
                     /region_name="GTPase_binding"
                     /note="GTPase binding; pfam09027"
                     /db_xref="CDD:430374"
     Region          497..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:21169560; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Region          <543..849
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          623..652
                     /region_name="Required for interaction with SRC.
                     /evidence=ECO:0000269|PubMed:21309750"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          632..635
                     /region_name="Required for interaction with NEDD4.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          659..702
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          718..840
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Site            724
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Region          733..876
                     /region_name="EBD domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          774..840
                     /region_name="Inhibitor_Mig-6"
                     /note="EGFR receptor inhibitor Mig-6; pfam11555"
                     /db_xref="CDD:463294"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:21169560; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Site            839
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O54967; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Site            859
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:21169560; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Site            872
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:21169560; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Site            881
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q07912.3)"
     Region          917..957
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07912.3)"
     Region          961..1004
                     /region_name="UBA_ACK1"
                     /note="UBA domain found in activated Cdc42 kinase 1 (ACK1)
                     and similar proteins; cd14274"
                     /db_xref="CDD:270460"
     Region          991..1030
                     /region_name="UBA_TNK1"
                     /note="UBA domain found in non-receptor tyrosine-protein
                     kinase TNK1 and similar proteins; cd14328"
                     /db_xref="CDD:270513"
     CDS             1..1040
                     /gene="TNK2"
                     /gene_synonym="ACK; ACK-1; ACK1; p21cdc42Hs"
                     /coded_by="NM_001387710.1:111..3233"
                     /note="isoform 8 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS93441.1"
                     /db_xref="GeneID:10188"
                     /db_xref="HGNC:HGNC:19297"
                     /db_xref="MIM:606994"
ORIGIN      
        1 mqpeegtgwl lellsevqlq qyflrlrddl nvtrlshfey vknedlekig mgrpgqrrlw
       61 eavkrrkalc krkswmskvf sgkrleaefp phhsqstfrk tspapggpag egplqsltcl
      121 igekdlrlle klgdgsfgvv rrgewdapsg ktvsvavkcl kpdvlsqpea mddfirevna
      181 mhsldhrnli rlygvvltpp mkmvtelapl gslldrlrkh qghfllgtls ryavqvaegm
      241 gyleskrfih rdlaarnlll atrdlvkigd fglmralpqn ddhyvmqehr kvpfawcape
      301 slktrtfsha sdtwmfgvtl wemftygqep wiglngsqil hkidkegerl prpedcpqdi
      361 ynvmvqcwah kpedrptfva lrdflleaqp tdmralqdfe epdklhiqmn dvitviegra
      421 enywwrgqnt rtlcvgpfpr nvvtsvagls aqdisqplqn sfihtghgds dprhcwgfpd
      481 ridelylgnp mdppdllsve lstsrppqhl ggvkkptydp vsedqdplss dfkrlglrkp
      541 glprglwlak psarvpgtka srgsgaevtl idfgeepvvp alrpcapsla qlamdacsll
      601 detppqsptr alprplhptp vvdwdarplp pppayddvaq deddfeicsi nstlvgagvp
      661 agpsqgqtny afvpeqarpp pplednlflp pqgggkppss aqtaeifqal qqecmrqlqa
      721 pagspapsps pggddkpqvp prvpipprpt rphvqlspap pgeeetsqwp gpaspprvpp
      781 replspqgsr tpsplvppgs splpprlsss pgktmpttqs fasdpkyatp qviqapgpra
      841 gpcilpivrd gkkvssthyy llperpsyle ryqrflreaq speeptplpv plllpppstp
      901 apaaptatvr pmpqaaldpk anfstnnsnp garpppprat arlpqrgcpg dgpeagrpad
      961 kiqmlqamvh gvtteecqaa lqchgwsvqr aaqylkveql fglglrprge chkvlemfdw
     1021 nleqagchll gswgpahhkr
//
LOCUS       NP_001337353             794 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 1 isoform 20 [Homo
            sapiens].
ACCESSION   NP_001337353
VERSION     NP_001337353.1
DBSOURCE    REFSEQ: accession NM_001350424.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 794)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 794)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 794)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 794)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 794)
  AUTHORS   Ruhle,F., Witten,A., Barysenka,A., Huge,A., Arning,A., Heller,C.,
            Krumpel,A., Mesters,R., Franke,A., Lieb,W., Riemenschneider,M.,
            Hiersche,M., Limperger,V., Nowak-Gottl,U. and Stoll,M.
  TITLE     Rare genetic variants in SMAP1, B3GAT2, and RIMS1 contribute to
            pediatric venous thromboembolism
  JOURNAL   Blood 129 (6), 783-790 (2017)
   PUBMED   28011674
  REMARK    GeneRIF: The study identified a region on chromosome 6 comprising
            the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus
            for pediatric venous thromboembolism.
REFERENCE   6  (residues 1 to 794)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 794)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
REFERENCE   8  (residues 1 to 794)
  AUTHORS   Schoch,S., Castillo,P.E., Jo,T., Mukherjee,K., Geppert,M., Wang,Y.,
            Schmitz,F., Malenka,R.C. and Sudhof,T.C.
  TITLE     RIM1alpha forms a protein scaffold for regulating neurotransmitter
            release at the active zone
  JOURNAL   Nature 415 (6869), 321-326 (2002)
   PUBMED   11797009
REFERENCE   9  (residues 1 to 794)
  AUTHORS   Coppola,T., Magnin-Luthi,S., Perret-Menoud,V., Gattesco,S.,
            Schiavo,G. and Regazzi,R.
  TITLE     Direct interaction of the Rab3 effector RIM with Ca2+ channels,
            SNAP-25, and synaptotagmin
  JOURNAL   J Biol Chem 276 (35), 32756-32762 (2001)
   PUBMED   11438518
REFERENCE   10 (residues 1 to 794)
  AUTHORS   Betz,A., Thakur,P., Junge,H.J., Ashery,U., Rhee,J.S., Scheuss,V.,
            Rosenmund,C., Rettig,J. and Brose,N.
  TITLE     Functional interaction of the active zone proteins Munc13-1 and
            RIM1 in synaptic vesicle priming
  JOURNAL   Neuron 30 (1), 183-196 (2001)
   PUBMED   11343654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590011.5, AL445256.18 and
            AL035633.18.
            
            Summary: The protein encoded by this gene is a RAS gene superfamily
            member that regulates synaptic vesicle exocytosis. This gene also
            plays a role in the regulation of voltage-gated calcium channels
            during neurotransmitter and insulin release. Mutations have
            suggested a role cognition and have been identified as the cause of
            cone-rod dystrophy type 7. Multiple transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Mar 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.106278.1,
                                           SRR1660805.243988.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..794
                     /product="regulating synaptic membrane exocytosis protein
                     1 isoform 20"
                     /note="RAB3-interacting protein 2; rab3-interacting
                     molecule 1; rab-3-interacting protein 2"
                     /calculated_mol_wt=89098
     Region          45..141
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(66..72,87,90,120,124,127..128)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          193..319
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(224,230,285,287,295)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          625..770
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(682,686..687,689,692,720,722,724,768..769)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..794
                     /gene="RIMS1"
                     /gene_synonym="CORD7; RAB3IP2; RIM; RIM1"
                     /coded_by="NM_001350424.2:388..2772"
                     /note="isoform 20 is encoded by transcript variant 20"
                     /db_xref="GeneID:22999"
                     /db_xref="HGNC:HGNC:17282"
                     /db_xref="MIM:606629"
ORIGIN      
        1 meysvsmwkp gdldyywldp atwhsretsp isshpvtwqp skegdrligr vilnkrttmp
       61 kdsgallglk vvggkmtdlg rlgafitkvk kgsladvvgh lragdevlew ngkplpgatn
      121 eevyniiles ksepqveiiv srpigdipri pesshpples ssssfesqkm erpsisvisp
      181 tspgalkdap qvlpgqlsvk lwydkvghql ivnvlqatdl parvdgrprn pyvkmyflpd
      241 rsdkskrrtk tvkkilepkw nqtfvyshvh rrdfrermle itvwdqprvq eeeseflgei
      301 lieletalld dephwyklqt hdesslplpq pspfmprrhi hgessskklq rsqrisdsdi
      361 sdyevddgig vvppvgyrss aresksttlt vpeqqrtthh rsrsvsphrg ndqgkprsrl
      421 pnvplqrsld eihptrrsrs ptrhhdasrs pvdhrtrdvd sqylseqdse llmlprakrg
      481 rsaeclhtts elqpfldrar sastnclrpd tslhsperer mhrqrsptqs ppadtsfssr
      541 rgrqlpqvpv rsgsieqesg hkklkstiqr stetgmaaem rkmvrqpsre stdgsinsys
      601 segnlifpgv rlgadsqfsd fldglgpaql vgrqtlatpa mgdiqigmed kkgqlevevi
      661 rarsltqkpg skstpapyvk vyllengaci akkktriark tldplyqqsl vfdespqgkv
      721 lqvivwgdyg rmdhkcfmgv aqilleeldl ssmvigwykl fppsslvdpt ltpltrrasq
      781 sslesstgpp cirs
//
LOCUS       NP_056078               3036 aa            linear   PRI 21-NOV-2025
DEFINITION  dmX-like protein 2 isoform 2 [Homo sapiens].
ACCESSION   NP_056078
VERSION     NP_056078.2
DBSOURCE    REFSEQ: accession NM_015263.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 3036)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 3036)
  AUTHORS   Wonkam-Tingang,E., Schrauwen,I., Esoh,K.K., Bharadwaj,T.,
            Nouel-Saied,L.M., Acharya,A., Nasir,A., Leal,S.M. and Wonkam,A.
  TITLE     A novel variant in DMXL2 gene is associated with autosomal dominant
            non-syndromic hearing impairment (DFNA71) in a Cameroonian family
  JOURNAL   Exp Biol Med (Maywood) 246 (13), 1524-1532 (2021)
   PUBMED   33715530
  REMARK    GeneRIF: A novel variant in DMXL2 gene is associated with autosomal
            dominant non-syndromic hearing impairment (DFNA71) in a Cameroonian
            family.
            Erratum:[Exp Biol Med (Maywood). 2021 Nov;246(21):NP5. doi:
            10.1177/15353702211040362. PMID: 34749523]
REFERENCE   3  (residues 1 to 3036)
  AUTHORS   Jaskolka,M.C., Winkley,S.R. and Kane,P.M.
  TITLE     RAVE and Rabconnectin-3 Complexes as Signal Dependent Regulators of
            Organelle Acidification
  JOURNAL   Front Cell Dev Biol 9, 698190 (2021)
   PUBMED   34249946
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 3036)
  AUTHORS   Esposito,A., Falace,A., Wagner,M., Gal,M., Mei,D., Conti,V.,
            Pisano,T., Aprile,D., Cerullo,M.S., De Fusco,A., Giovedi,S.,
            Seibt,A., Magen,D., Polster,T., Eran,A., Stenton,S.L., Fiorillo,C.,
            Ravid,S., Mayatepek,E., Hafner,H., Wortmann,S., Levanon,E.Y.,
            Marini,C., Mandel,H., Benfenati,F., Distelmaier,F., Fassio,A. and
            Guerrini,R.
  TITLE     Biallelic DMXL2 mutations impair autophagy and cause Ohtahara
            syndrome with progressive course
  JOURNAL   Brain 142 (12), 3876-3891 (2019)
   PUBMED   31688942
  REMARK    GeneRIF: Impaired lysosomal function and autophagy caused by
            biallelic DMXL2 mutations affect neuronal development and synapse
            formation and result in Ohtahara syndrome with profound
            developmental impairment and reduced life expectancy.
            Erratum:[Brain. 2020 Feb 1;143(2):e16. doi: 10.1093/brain/awz397.
            PMID: 31840736]
REFERENCE   5  (residues 1 to 3036)
  AUTHORS   Costain,G., Walker,S., Argiropoulos,B., Baribeau,D.A.,
            Bassett,A.S., Boot,E., Devriendt,K., Kellam,B., Marshall,C.R.,
            Prasad,A., Serrano,M.A., Stavropoulos,D.J., Twede,H.,
            Vermeesch,J.R., Vorstman,J.A.S. and Scherer,S.W.
  TITLE     Rare copy number variations affecting the synaptic gene DMXL2 in
            neurodevelopmental disorders
  JOURNAL   J Neurodev Disord 11 (1), 3 (2019)
   PUBMED   30732576
  REMARK    GeneRIF: Disruption of DMXL2 may predispose to NDDs including
            autism spectrum disorder.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 3036)
  AUTHORS   Tata,B., Huijbregts,L., Jacquier,S., Csaba,Z., Genin,E., Meyer,V.,
            Leka,S., Dupont,J., Charles,P., Chevenne,D., Carel,J.C., Leger,J.
            and de Roux,N.
  TITLE     Haploinsufficiency of Dmxl2, encoding a synaptic protein, causes
            infertility associated with a loss of GnRH neurons in mouse
  JOURNAL   PLoS Biol 12 (9), e1001952 (2014)
   PUBMED   25248098
  REMARK    GeneRIF: Haploinsufficiency of Dmxl2, encoding a synaptic protein,
            causes infertility associated with a loss of GnRH neurons in humans
            and mice.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 3036)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   8  (residues 1 to 3036)
  AUTHORS   Sethi,N., Yan,Y., Quek,D., Schupbach,T. and Kang,Y.
  TITLE     Rabconnectin-3 is a functional regulator of mammalian Notch
            signaling
  JOURNAL   J Biol Chem 285 (45), 34757-34764 (2010)
   PUBMED   20810660
  REMARK    GeneRIF: an important role for Rabconnectin-3 and V-ATPase activity
            in the Notch signaling pathway in mammalian cells.
REFERENCE   9  (residues 1 to 3036)
  AUTHORS   Luke,M.M., O'Meara,E.S., Rowland,C.M., Shiffman,D., Bare,L.A.,
            Arellano,A.R., Longstreth,W.T. Jr., Lumley,T., Rice,K., Tracy,R.P.,
            Devlin,J.J. and Psaty,B.M.
  TITLE     Gene variants associated with ischemic stroke: the cardiovascular
            health study
  JOURNAL   Stroke 40 (2), 363-368 (2009)
   PUBMED   19023099
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 3036)
  AUTHORS   Nagano,F., Kawabe,H., Nakanishi,H., Shinohara,M.,
            Deguchi-Tawarada,M., Takeuchi,M., Sasaki,T. and Takai,Y.
  TITLE     Rabconnectin-3, a novel protein that binds both GDP/GTP exchange
            protein and GTPase-activating protein for Rab3 small G protein
            family
  JOURNAL   J Biol Chem 277 (12), 9629-9632 (2002)
   PUBMED   11809763
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020892.7 and AC066613.7.
            
            On Dec 8, 2006 this sequence version replaced NP_056078.1.
            
            Summary: This gene encodes a protein with 12 WD domains. Proteins
            with WD domains are involved in many functions including
            participation in signal transduction pathways. Participation of the
            encoded protein in regulation of the Notch signaling pathway has
            been demonstrated in vitro using several human cell lines
            (PMID:20810660). A gene encoding a similar protein is located on
            chromosome 5. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Aug
            2011].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region compared to variant 1. The
            resulting protein (isoform 2) is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF389880.1, SRR1803617.84795.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..3036
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.2"
     Protein         1..3036
                     /product="dmX-like protein 2 isoform 2"
                     /note="rabconnectin-3; dmX-like protein 2"
                     /calculated_mol_wt=339512
     Region          <45..268
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          61..102
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          108..145
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          109..171
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          167..207
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          174..225
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          230..278
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          235..268
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BPN8; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          417..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          492..532
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BPN8; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          595..634
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          751..803
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          878..920
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          932..959
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            944
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            945
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          1000..1037
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            1140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            1143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            1151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          1163..1204
                     /region_name="WD 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          1171..1902
                     /region_name="Rav1p_C"
                     /note="RAVE protein 1 C terminal; pfam12234"
                     /db_xref="CDD:432413"
     Region          1244..1281
                     /region_name="WD 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            1287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BPN8; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            1400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            1417
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BPN8; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            1857
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          1927..1952
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            1984
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          1999..2033
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            2022
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BPN8; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            2399
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Site            2640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BPN8; propagated from
                     UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          2761..2800
                     /region_name="WD 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          2766..3018
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          2804..2843
                     /region_name="WD 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          2810..2850
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2850..2892
                     /region_name="WD 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          2855..2897
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2898..2937
                     /region_name="WD 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          2904..2939
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2940..2979
                     /region_name="WD 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     Region          2945..2981
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2992..3030
                     /region_name="WD 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDJ6.2)"
     CDS             1..3036
                     /gene="DMXL2"
                     /gene_synonym="DEE81; DFNA71; EIEE81; PEPNS; RC3"
                     /coded_by="NM_015263.5:227..9337"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10141.1"
                     /db_xref="GeneID:23312"
                     /db_xref="HGNC:HGNC:2938"
                     /db_xref="MIM:612186"
ORIGIN      
        1 mhlhqvltga vnpgdncysv gsvgdvpfta ygsgcdivil andfecvqii pgakhgniqv
       61 scvecsnqqg riaasygnav cifeplgins hkrncqlkcq wlktgqffls svtynlawdp
      121 qdnrlltatd siqlwappgd dileeeeeid ntvppvlndw kcvwqcktsv svhlmewspd
      181 geyfatagkd dcllkvwypm tgwkssiipq dhhevkrrqs stqfsfvyla hpravtgfsw
      241 rktskymprg svcnvlltsc hdgvcrlwae tllpedcllg eqicetttss iasslshagr
      301 hkdriqhale tihhlknlrk gqrrssvlvt haelmpdqta mhevqrhish hanalchfhi
      361 aasinpatdi pnvlvgtafn vddgnggfvv hwlnnkefhf tsstevfmhq lrklsdkqvd
      421 henddadred eehsqedrer glhmkldhdl sldreseagt gssehedger egsprtysrl
      481 svpmplptvl ldrkietllt ewnknpdmlf tihpvdgtfl vwhvkyldey npgifrqvqv
      541 sfssripvaf psgdasslsk nimmyacina tkdshhtllh qegmsvgsph gsqphsrshs
      601 thmnilaptv mmiskhidgs lnqwavtfad ksafttvltv shkfrycghr fhlndlachs
      661 vlpllltssh hnalltpeld cqwdsdnkls rlmdpvkhik gsskqplrna atrtfhdpna
      721 iyselilwrv dpigplsytg gvselarins lhtsafsnva wlptlipsyc lgtycnsasa
      781 cfvasdgknl rlyqavvdar klldelsdpe sskligevfn ivsqqstarp gciieldait
      841 nqcgsntqll hvfqedfiig ykphkedmek keteiffqps qgyrpppfse kfflvviekd
      901 snnnsilhmw hlhlksvqac lakasegass esllsvpgqk nvdsspetsp svspmphsss
      961 ianlqtaskl ilssrlvysq pldlpesvev iratpsaghl ssssiypvcl apylvvttcs
     1021 dnkvrfwkcc meanpecnks dekeiyhwkr wplmndeged nsstvsivgr pvavscsytg
     1081 rlavaykqpi hhngfvskef smhvcifece stggsewvle qtihlddlvk vgsvldsrvs
     1141 vdsnlfvysk sdallskdry lipnikhlvh ldwvskedgs hiltvgvgan ifmygrlsgi
     1201 vteqtnskdg vavitlplgg sikqgvksrw vllrsidlvs svdgtpslpv slswvrdgil
     1261 vvgmdcemhv yaqwkhavkf gdteadssna eeaamqdhst fksnmlarks vvegtaisdd
     1321 vfcsptviqd gglfeaahvl sptlpqyhpt qllelmdlgk vrrakailsh lvkciageva
     1381 ivrdpdageg tkrhlsrtis vsgstaketv tvgkdgtrdy teidsipplp lyallaadqd
     1441 tsyriseest kipqsyedqt vsqpedqyse lfqiqdiptd didlepekre nkskvinlsq
     1501 ygpayfgqeh arvlsshlmh sslpgltrle qmflvaladt vattstelde srdkscsgrd
     1561 tldecglryl lamrlhtcll tslpplyrvq llhqgvstch fawafhseae eelinmipai
     1621 qrgdpqwsel ramgigwwvr nintlrrcie kvakasfqrn ndaldaalfy lsmkkkavvw
     1681 glfrsqhdek mttffshnfn edrwrkaalk nafsllgkqr feqsaaffll agslkdaiev
     1741 clekmediql amviarlyes efetsstyis ilnqkilgcq kdgsgfsckr lhpdpflrsl
     1801 aywvmkdytr aldtlleqtp keddehqvii kscnpvafsf ynylrthpll irrnlaspeg
     1861 tlatlglkte knfvdkinli erklffttan ahfkvgcpvl alevlskipk vtktsalsak
     1921 kdqpdfishr mddvpshska lsdgngssgi ewsnvtssqy dwsqpivkvd eeplnldwge
     1981 dhdsaldeee ddavglvmks tdarekdkqs dqkasdpnml ltpqeeddpe gdtevdviae
     2041 qlkfraclki lmtelrtlat gyevdggklr fqlynwleke iaalheicnh esvikeyssk
     2101 tyskvesdll dqeemvdkpd igsyerhqie rrrlqakreh aerrkswlqk nqdllrvfls
     2161 ycslhgaqgg glasvrmelk fllqesqqet tvkqlqsplp lpttlpllsa siastktvia
     2221 npvlylnnhi hdilytivqm ktpphpsied vkvhtlhsla aslsasiyqa lcdshsysqt
     2281 egnqftgmay qglllsdrrr lrtesieeha tpnsspaqwp gvsslinlls saqdedqpkl
     2341 nillceavva vylsllihal atnssselfr laahplnnrm waavfgggvk lvvkprrqse
     2401 nisappvlse didkhrrrfn mrmlvpgrpv kdatpppvpa erpsykekfi ppelsmwdyf
     2461 vakpflplsd sgviydsdes ihsdeeddaf fsdtqiqehq dpnsyswall hltmvklalh
     2521 nvknffpiag lefselpvts plgiaviknl enweqilqek mdqfegpppn yintyptdls
     2581 vgagpailrn kamlepentp fksrdssafp vkrlwhflvk qevlqetfir yiftkkrkqs
     2641 eveadlgypg gkakvihkes dmimafsvnk ancneivlas thdvqeldvt sllacqsyiw
     2701 igeeydresk ssddvdyrgs tttlyqpsat sysasqvhpp sslpwlgtgq tstgasvlmk
     2761 rnlhnvkrmt shpvhqyylt gaqdgsvrmf ewtrpqqlvc frqagnarvt rlyfnsqgnk
     2821 cgvadgegfl siwqvnqtas npkpymswqc hskatsdfaf itssslvats ghsndnrnvc
     2881 lwdtlispgn slihgftchd hgatvlqyap kqqllisggr kghvcifdir qrqlihtfqa
     2941 hdsaikalal dpyeeyfttg saegnikvwr ltghglihsf ksehakqsif rnigagvmqi
     3001 diiqgnrlfs cgadgtlktr vlpnafnipn rildil
//
LOCUS       NP_001371608            1154 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 17 [Homo sapiens].
ACCESSION   NP_001371608
VERSION     NP_001371608.1
DBSOURCE    REFSEQ: accession NM_001384679.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1154)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1154)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1154)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1154)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1154)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1154)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1154)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1154)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1154)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1154)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2599318.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1154
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1154
                     /product="microtubule-associated protein 4 isoform 17"
                     /note="MAP-4"
                     /calculated_mol_wt=121203
     Region          <686..975
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          994..1023
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          1025..1054
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          1056..1086
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1154
                     /gene="MAP4"
                     /coded_by="NM_001384679.1:96..3560"
                     /note="isoform 17 is encoded by transcript variant 8"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgsp tefleekmay qeypnsqnwp
      121 edtnfcfqpe qvvdpiqtdp fkmyhdddla dlvfpssata dtsifagqnd plkdsygmsp
      181 cntavvpqgw svealnsphs esfvspeava eppqptavpl elakeiemas eerppaqale
      241 immglkttdm apsketemal akdmalatkt evalakdmes ptkldvtlak dmqpsmesdm
      301 alvkdmelpt ekevalvkdv rwptetdvss aknvvlptet evapakdvtl lketeraspi
      361 kmdlapskdm gppkenkket eraspikmdl apskdmgppk enkivpakdl vllseievaq
      421 andiisstei ssaekvalss etevalardm tlppetnvil tkdkalplea evapvkdmaq
      481 lpeteiapak dvapstvkev gllkdmspls etemalgkdv tpppetevvl iknvclppem
      541 evaltedqvp alkteaplak dgvltlannv tpakdvppls eteatpvpik dmeiaqtqkg
      601 isedshlesl qdvgqsaapt fmispetvtg tgkkcslpae edsvleklge rkpcnsqpse
      661 lssetsvcls sstvyqqlgm svygiarpee grpvvsgtgn dittppnkel ppspekktkp
      721 lattqpakts tskaktqpts lpkqpaptti gglnkkpmsl asglvpaapp krpavasarp
      781 silpskdvkp kpiadakape kraspskpas apasrsgsks tqtvakttta aavastgpss
      841 rspstllpkk ptaiktegkp aevkkmtaks vpadlsrpks tstssmkktt tlsgtapaag
      901 vvpsrvkatp mpsrpsttpf idkkptsakp ssttprlsrl atntsapdlk nvrskakvek
      961 kteaaattrk pesnavtkta gpiasaqkqp agkvqivskk vsyshiqskc gskdnikhvp
     1021 gggnvqiqnk kvdiskvssk cgskanikhk pgggdvkies qklnfkekaq akvgsldnvg
     1081 hlpaggavkt egggseaplc pgppageepa iseaapeaga ptsasglngh ptlsgggdqr
     1141 eaqtldsqiq etsi
//
LOCUS       NP_001009570             339 aa            linear   PRI 21-NOV-2025
DEFINITION  T-complex protein 1 subunit eta isoform b [Homo sapiens].
ACCESSION   NP_001009570
VERSION     NP_001009570.1
DBSOURCE    REFSEQ: accession NM_001009570.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Huang,X., Wang,H., Xu,F., Lv,L., Wang,R., Jiang,B., Liu,T., Hu,H.
            and Jiang,Y.
  TITLE     Overexpression of chaperonin containing TCP1 subunit 7 has
            diagnostic and prognostic value for hepatocellular carcinoma
  JOURNAL   Aging (Albany NY) 14 (2), 747-769 (2022)
   PUBMED   35073517
  REMARK    GeneRIF: Overexpression of chaperonin containing TCP1 subunit 7 has
            diagnostic and prognostic value for hepatocellular carcinoma.
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Okitsu,Y., Nagano,M., Yamagata,T., Ito,C., Toshimori,K., Dohra,H.,
            Fujii,W. and Yogo,K.
  TITLE     Dlec1 is required for spermatogenesis and male fertility in mice
  JOURNAL   Sci Rep 10 (1), 18883 (2020)
   PUBMED   33144677
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Imai,Y., Soda,M., Murakami,T., Shoji,M., Abe,K. and Takahashi,R.
  TITLE     A product of the human gene adjacent to parkin is a component of
            Lewy bodies and suppresses Pael receptor-induced cell death
  JOURNAL   J Biol Chem 278 (51), 51901-51910 (2003)
   PUBMED   14532270
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Yokota,S., Yanagi,H., Yura,T. and Kubota,H.
  TITLE     Cytosolic chaperonin-containing t-complex polypeptide 1 changes the
            content of a particular subunit species concomitant with substrate
            binding and folding activities during the cell cycle
  JOURNAL   Eur J Biochem 268 (17), 4664-4673 (2001)
   PUBMED   11532003
  REMARK    GeneRIF: Functional characterization of the CCT complex and its
            subunits in mouse.
REFERENCE   8  (residues 1 to 339)
  AUTHORS   Won,K.A., Schumacher,R.J., Farr,G.W., Horwich,A.L. and Reed,S.I.
  TITLE     Maturation of human cyclin E requires the function of eukaryotic
            chaperonin CCT
  JOURNAL   Mol Cell Biol 18 (12), 7584-7589 (1998)
   PUBMED   9819444
REFERENCE   9  (residues 1 to 339)
  AUTHORS   Liou,A.K. and Willison,K.R.
  TITLE     Elucidation of the subunit orientation in CCT (chaperonin
            containing TCP1) from the subunit composition of CCT
            micro-complexes
  JOURNAL   EMBO J 16 (14), 4311-4316 (1997)
   PUBMED   9250675
REFERENCE   10 (residues 1 to 339)
  AUTHORS   Hynes,G., Celis,J.E., Lewis,V.A., Carne,A., U,S., Lauridsen,J.B.
            and Willison,K.R.
  TITLE     Analysis of chaperonin-containing TCP-1 subunits in the human
            keratinocyte two-dimensional protein database: further
            characterisation of antibodies to individual subunits
  JOURNAL   Electrophoresis 17 (11), 1720-1727 (1996)
   PUBMED   8982604
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC395264.1, AK293597.1,
            AK098825.1 and CX781741.1.
            
            Summary: This gene encodes a molecular chaperone that is a member
            of the chaperonin containing TCP1 complex (CCT), also known as the
            TCP1 ring complex (TRiC). This complex consists of two identical
            stacked rings, each containing eight different proteins. Unfolded
            polypeptides enter the central cavity of the complex and are folded
            in an ATP-dependent manner. The complex folds various proteins,
            including actin and tubulin. Alternative splicing results in
            multiple transcript variants. Related pseudogenes have been
            identified on chromosomes 5 and 6. [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            segment of the 5' coding region, compared to variant 1, resulting
            in a shorter isoform (b), compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293597.1, SRR14038193.872863.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.2"
     Protein         1..339
                     /product="T-complex protein 1 subunit eta isoform b"
                     /note="chaperonin containing t-complex polypeptide 1, eta
                     subunit; T-complex protein 1 subunit eta; HIV-1 Nef
                     interacting protein; CCT-eta; TCP-1-eta; chaperonin
                     containing T-complex polypeptide 1 subunit 7"
                     /calculated_mol_wt=37368
     Region          <1..321
                     /region_name="chaperonin_like"
                     /note="chaperonin_like superfamily. Chaperonins are
                     involved in productive folding of proteins. They share a
                     common general morphology, a double toroid of 2 stacked
                     rings, each composed of 7-9 subunits. There are 2 main
                     chaperonin groups. The symmetry of type I...; cl02777"
                     /db_xref="CDD:351886"
     CDS             1..339
                     /gene="CCT7"
                     /gene_synonym="CCTETA; CCTH; NIP7-1; TCP1ETA"
                     /coded_by="NM_001009570.3:72..1091"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42696.1"
                     /db_xref="GeneID:10574"
                     /db_xref="HGNC:HGNC:1622"
                     /db_xref="MIM:605140"
ORIGIN      
        1 mmdsqlvagv afkktfsyag femqpkkyhn pkiallnvel elkaekdnae irvhtvedyq
       61 aivdaewnil ydklekihhs gakvvlsklp igdvatqyfa drdmfcagrv peedlkrtmm
      121 acggsiqtsv nalsadvlgr cqvfeetqig gerynfftgc pkaktctfil rggaeqfmee
      181 terslhdaim ivrraiknds vvagggaiem elskylrdys rtipgkqqll igayakalei
      241 iprqlcdnag fdatnilnkl rarhaqggtw ygvdinnedi adnfeafvwe pamvrinalt
      301 aaseaacliv svdetiknpr stvdaptaag rgrgrgrph
//
LOCUS       NP_001365780             240 aa            linear   PRI 21-NOV-2025
DEFINITION  myeloid leukemia factor 1 isoform 11 [Homo sapiens].
ACCESSION   NP_001365780
VERSION     NP_001365780.1
DBSOURCE    REFSEQ: accession NM_001378851.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Tang,Z., Yang,Y., Chen,W. and Liang,T.
  TITLE     Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling
  JOURNAL   Hepatol Commun 7 (8), e0204 (2023)
   PUBMED   37486965
  REMARK    GeneRIF: Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Huang,D., Liu,C., Sun,X., Sun,X., Qu,Y., Tang,Y., Li,G. and Tong,T.
  TITLE     CRL4DCAF8 and USP11 oppositely regulate the stability of myeloid
            leukemia factors (MLFs)
  JOURNAL   Biochem Biophys Res Commun 529 (2), 127-132 (2020)
   PUBMED   32703400
  REMARK    GeneRIF: CRL4(DCAF8) and USP11 oppositely regulate the stability of
            myeloid leukemia factors (MLFs).
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Darracq,A., Pak,H., Bourgoin,V., Zmiri,F., Dellaire,G., Affar,E.B.
            and Milot,E.
  TITLE     NPM and NPM-MLF1 interact with chromatin remodeling complexes and
            influence their recruitment to specific genes
  JOURNAL   PLoS Genet 15 (11), e1008463 (2019)
   PUBMED   31675375
  REMARK    GeneRIF: the abnormal gene regulation imposed by NPM-MLF1 can be
            characterized by the enhanced recruitment of NuRD to gene
            regulatory regions. Thus, different mechanisms would orchestrate
            the dysregulation of NPM function in NPMc+- versus
            NPM1-MLF1-associated leukemia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Yoneda-Kato,N., Tomoda,K., Umehara,M., Arata,Y. and Kato,J.Y.
  TITLE     Myeloid leukemia factor 1 regulates p53 by suppressing COP1 via
            COP9 signalosome subunit 3
  JOURNAL   EMBO J 24 (9), 1739-1749 (2005)
   PUBMED   15861129
REFERENCE   7  (residues 1 to 240)
  AUTHORS   Hanissian,S.H., Akbar,U., Teng,B., Janjetovic,Z., Hoffmann,A.,
            Hitzler,J.K., Iscove,N., Hamre,K., Du,X., Tong,Y., Mukatira,S.,
            Robertson,J.H. and Morris,S.W.
  TITLE     cDNA cloning and characterization of a novel gene encoding the
            MLF1-interacting protein MLF1IP
  JOURNAL   Oncogene 23 (20), 3700-3707 (2004)
   PUBMED   15116101
REFERENCE   8  (residues 1 to 240)
  AUTHORS   Arber,D.A., Chang,K.L., Lyda,M.H., Bedell,V., Spielberger,R. and
            Slovak,M.L.
  TITLE     Detection of NPM/MLF1 fusion in t(3;5)-positive acute myeloid
            leukemia and myelodysplasia
  JOURNAL   Hum Pathol 34 (8), 809-813 (2003)
   PUBMED   14506644
  REMARK    GeneRIF: These findings suggest that an NPM/MLF1 fusion is the
            primary molecular abnormality in t(3;5) MDS and AML with
            multilineage dysplasia, and that cases with NPM/MLF1 may be
            clinically distinct from other MDS-associated disease
REFERENCE   9  (residues 1 to 240)
  AUTHORS   Lim,R., Winteringham,L.N., Williams,J.H., McCulloch,R.K.,
            Ingley,E., Tiao,J.Y., Lalonde,J.P., Tsai,S., Tilbrook,P.A., Sun,Y.,
            Wu,X., Morris,S.W. and Klinken,S.P.
  TITLE     MADM, a novel adaptor protein that mediates phosphorylation of the
            14-3-3 binding site of myeloid leukemia factor 1
  JOURNAL   J Biol Chem 277 (43), 40997-41008 (2002)
   PUBMED   12176995
  REMARK    GeneRIF: phosphorylation of 14-3-3 binding site by MADM
REFERENCE   10 (residues 1 to 240)
  AUTHORS   Yoneda-Kato,N., Look,A.T., Kirstein,M.N., Valentine,M.B.,
            Raimondi,S.C., Cohen,K.J., Carroll,A.J. and Morris,S.W.
  TITLE     The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid
            leukemia produces a novel fusion gene, NPM-MLF1
  JOURNAL   Oncogene 12 (2), 265-275 (1996)
   PUBMED   8570204
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106707.9 and AC025033.20.
            
            Summary: This gene encodes an oncoprotein which is thought to play
            a role in the phenotypic determination of hemopoetic cells.
            Translocations between this gene and nucleophosmin have been
            associated with myelodysplastic syndrome and acute myeloid
            leukemia. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.284829.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.32"
     Protein         1..240
                     /product="myeloid leukemia factor 1 isoform 11"
                     /note="myelodysplasia-myeloid leukemia factor 1; testis
                     tissue sperm-binding protein Li 49e"
                     /calculated_mol_wt=27061
     Region          1..174
                     /region_name="Mlf1IP"
                     /note="Myelodysplasia-myeloid leukemia factor
                     1-interacting protein; pfam10248"
                     /db_xref="CDD:463022"
     CDS             1..240
                     /gene="MLF1"
                     /coded_by="NM_001378851.1:108..830"
                     /note="isoform 11 is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS93413.1"
                     /db_xref="GeneID:4291"
                     /db_xref="HGNC:HGNC:7125"
                     /db_xref="MIM:601402"
ORIGIN      
        1 mfrmlnssfe ddpffsvglc sfkgfagdit tisvklmhtd vssfqtmdqm vsnmrnymqk
       61 lernfgqlsv dpnghsfcss svmtyskigd eppkvfqast qtrrapggik etrkamrdsd
      121 sglekmaigh hihdrahvik ksknkktgde evnqefinmn esdahafdee wqsevlkykp
      181 grhnlgntrm rsvghenpgs relkrrekpq qspaiehgrr snvlgdklhi kgssvksnkk
//
LOCUS       NP_001129283             221 aa            linear   PRI 21-NOV-2025
DEFINITION  SIN3-HDAC complex-associated factor [Homo sapiens].
ACCESSION   NP_001129283
VERSION     NP_001129283.1
DBSOURCE    REFSEQ: accession NM_001135811.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Jhuang,Y.L., Yang,C.W., Tseng,Y.F., Hsu,C.L., Li,H.Y., Yuan,R.H.
            and Jeng,Y.M.
  TITLE     SIN3-HDAC complex-associated factor, a chromatin remodelling gene
            located in the 12p amplicon, is a potential germ cell
            tumour-specific oncogene
  JOURNAL   J Pathol 258 (4), 353-365 (2022)
   PUBMED   36056608
  REMARK    GeneRIF: SIN3-HDAC complex-associated factor, a chromatin
            remodelling gene located in the 12p amplicon, is a potential germ
            cell tumour-specific oncogene.
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Zhang,Y., Li,J.H., Yuan,Q.G. and Yang,W.B.
  TITLE     Restraint of FAM60A has a cancer-inhibiting role in pancreatic
            carcinoma via the effects on the Akt/GSK-3beta/beta-catenin
            signaling pathway
  JOURNAL   Environ Toxicol 37 (6), 1432-1444 (2022)
   PUBMED   35213078
  REMARK    GeneRIF: Restraint of FAM60A has a cancer-inhibiting role in
            pancreatic carcinoma via the effects on the
            Akt/GSK-3beta/beta-catenin signaling pathway.
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Sun,Y.H., Sun,X.W., Yang,L., Cheng,B. and Chen,Y.L.
  TITLE     [Research Progress of FAM60A in the Regulation of Cellular
            Function]
  JOURNAL   Zhongguo Yi Xue Ke Xue Yuan Xue Bao 43 (3), 469-474 (2021)
   PUBMED   34238425
  REMARK    GeneRIF: [Research Progress of FAM60A in the Regulation of Cellular
            Function].
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 221)
  AUTHORS   Joshi,P., Greco,T.M., Guise,A.J., Luo,Y., Yu,F., Nesvizhskii,A.I.
            and Cristea,I.M.
  TITLE     The functional interactome landscape of the human histone
            deacetylase family
  JOURNAL   Mol Syst Biol 9, 672 (2013)
   PUBMED   23752268
REFERENCE   8  (residues 1 to 221)
  AUTHORS   Smith,K.T., Sardiu,M.E., Martin-Brown,S.A., Seidel,C.,
            Mushegian,A., Egidy,R., Florens,L., Washburn,M.P. and Workman,J.L.
  TITLE     Human family with sequence similarity 60 member A (FAM60A) protein:
            a new subunit of the Sin3 deacetylase complex
  JOURNAL   Mol Cell Proteomics 11 (12), 1815-1828 (2012)
   PUBMED   22984288
  REMARK    GeneRIF: studies reveal that loss of FAM60A or another component of
            the Sin3 complex, SDS3, leads to a change in cell morphology and an
            increase in cell migration
REFERENCE   9  (residues 1 to 221)
  AUTHORS   Munoz,I.M., MacArtney,T., Sanchez-Pulido,L., Ponting,C.P., Rocha,S.
            and Rouse,J.
  TITLE     Family with sequence similarity 60A (FAM60A) protein is a cell
            cycle-fluctuating regulator of the SIN3-HDAC1 histone deacetylase
            complex
  JOURNAL   J Biol Chem 287 (39), 32346-32353 (2012)
   PUBMED   22865885
  REMARK    GeneRIF: Family with sequence similarity 60A (FAM60A) protein is a
            cell cycle-fluctuating regulator of the SIN3-HDAC1 histone
            deacetylase complex.
REFERENCE   10 (residues 1 to 221)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC000024.2, AF087885.1, DR763430.1 and BC004462.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2, and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.6788.1,
                                           SRR11853562.7049.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p11.21"
     Protein         1..221
                     /product="SIN3-HDAC complex-associated factor"
                     /note="tera protein homolog; protein FAM60A; family with
                     sequence similarity 60 member A"
                     /calculated_mol_wt=24721
     Region          2..198
                     /region_name="FAM60A"
                     /note="Protein Family FAM60A; pfam15396"
                     /db_xref="CDD:464703"
     Region          112..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP50.1)"
     Region          201..221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP50.1)"
     CDS             1..221
                     /gene="SINHCAF"
                     /gene_synonym="C12orf14; FAM60A; L4; TERA"
                     /coded_by="NM_001135811.2:290..955"
                     /db_xref="CCDS:CCDS8723.1"
                     /db_xref="GeneID:58516"
                     /db_xref="HGNC:HGNC:30702"
                     /db_xref="MIM:615027"
ORIGIN      
        1 mfgfhkpkmy rsiegccicr akssssrftd skryekdfqs cfglhetrsg dicnacvllv
       61 krwkklpags kknwnhvvda ragpslkttl kpkkvktlsg nriksnqisk lqkefkrhns
      121 dahsttssas paqspcysnq sddgsdtema sgsnrtpvfs fldltywkrq kiccgiiykg
      181 rfgevlidth lfkpccsnkk aaaekpeeqg peplpistqe w
//
LOCUS       NP_001166150             407 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger protein 764 isoform 2 [Homo sapiens].
ACCESSION   NP_001166150
VERSION     NP_001166150.1
DBSOURCE    REFSEQ: accession NM_001172679.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Helleboid,P.Y., Heusel,M., Duc,J., Piot,C., Thorball,C.W.,
            Coluccio,A., Pontis,J., Imbeault,M., Turelli,P., Aebersold,R. and
            Trono,D.
  TITLE     The interactome of KRAB zinc finger proteins reveals the
            evolutionary history of their functional diversification
  JOURNAL   EMBO J 38 (18), e101220 (2019)
   PUBMED   31403225
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Fadda,A., Syed,N., Mackeh,R., Papadopoulou,A., Suzuki,S.,
            Jithesh,P.V. and Kino,T.
  TITLE     Genome-wide Regulatory Roles of the C2H2-type Zinc Finger Protein
            ZNF764 on the Glucocorticoid Receptor
  JOURNAL   Sci Rep 7, 41598 (2017)
   PUBMED   28139699
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Kino,T., Pavlatou,M.G., Moraitis,A.G., Nemery,R.L., Raygada,M. and
            Stratakis,C.A.
  TITLE     ZNF764 haploinsufficiency may explain partial glucocorticoid,
            androgen, and thyroid hormone resistance associated with 16p11.2
            microdeletion
  JOURNAL   J Clin Endocrinol Metab 97 (8), E1557-E1566 (2012)
   PUBMED   22577170
  REMARK    GeneRIF: effect of ZNF764 on the glucocorticoid receptor
            transcriptional activity was mediated through cooperation with a
            general nuclear hormone receptor coactivator, transcriptional
            intermediary factor 1
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC002310.1, BF725095.1, AK093992.1 and BC008821.2.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the coding region, compared to variant 1. The
            resulting isoform (2) lacks one internal amino acid, compared to
            isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.262734.1, AK093992.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267766, SAMN03267783
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395091.3/ ENSP00000378526.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..407
                     /product="zinc finger protein 764 isoform 2"
                     /calculated_mol_wt=44741
     Region          26..85
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          176..196
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          189..211
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          204..224
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          228..>293
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          232..252
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(237,239,241,243..244,247..248,251,265,267,271..272,
                     275..276,279,293,295,297,299..300,303..304,307)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          260..280
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          288..308
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          300..325
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          316..336
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          332..351
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          344..364
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..407
                     /gene="ZNF764"
                     /coded_by="NM_001172679.2:193..1416"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54001.1"
                     /db_xref="GeneID:92595"
                     /db_xref="HGNC:HGNC:28200"
                     /db_xref="MIM:619524"
ORIGIN      
        1 mapplaplpp rdpngagpew repgavsfad vavyfcreew gclrpaqral yrdvmretyg
       61 hlsalgiggn kpaliswvee eaelwgpaaq dpevakcqtq tdpdsrnkkk erqregtgal
      121 ekpdpvaags pglkspqaps agppygweql skaphrgrps lcahppvpra dqrhgcyvcg
      181 ksfawrstlv ehvyshtgek pfhctdcgkg fghasslskh raihrgerph rclecgraft
      241 qrsaltshlr vhtgekpygc adcgrrfsqs salyqhrrvh sgetpfpcpd cgrafaypsd
      301 lrrhvrthtg ekpypcpdcg rcfrqssema ahrrthsgek pypcpqcgrr fgqksavakh
      361 qwvhrpgagg hrgrvagrls vtltpghgdl dppvgfqlyp eifqecg
//
LOCUS       NP_001032209            1304 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal cell adhesion molecule isoform A precursor [Homo sapiens].
ACCESSION   NP_001032209 XP_005250430
VERSION     NP_001032209.1
DBSOURCE    REFSEQ: accession NM_001037132.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1304)
  AUTHORS   Wang,C., Wang,Z., Fu,L., Du,J., Ji,F. and Qiu,X.
  TITLE     CircNRCAM up-regulates NRCAM to promote papillary thyroid carcinoma
            progression
  JOURNAL   J Endocrinol Invest 47 (5), 1215-1226 (2024)
   PUBMED   38485895
  REMARK    GeneRIF: CircNRCAM up-regulates NRCAM to promote papillary thyroid
            carcinoma progression.
REFERENCE   2  (residues 1 to 1304)
  AUTHORS   Zhou,L., He,L., Liu,C.H., Qiu,H., Zheng,L., Sample,K.M., Wu,Q.,
            Li,J., Xie,K., Ampuero,J., Li,Z., Lv,D., Liu,M., Romero-Gomez,M.,
            Hu,Y. and Tang,H.
  TITLE     Liver cancer stem cell dissemination and metastasis: uncovering the
            role of NRCAM in hepatocellular carcinoma
  JOURNAL   J Exp Clin Cancer Res 42 (1), 311 (2023)
   PUBMED   37993901
  REMARK    GeneRIF: Liver cancer stem cell dissemination and metastasis:
            uncovering the role of NRCAM in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1304)
  AUTHORS   Sannes,A.C., Christensen,J.O., Nielsen,M.B. and Gjerstad,J.
  TITLE     Stress-induced headache in the general working population is
            moderated by the NRCAM rs2300043 genotype
  JOURNAL   Scand J Pain 23 (2), 326-332 (2022)
   PUBMED   36181733
  REMARK    GeneRIF: Stress-induced headache in the general working population
            is moderated by the NRCAM rs2300043 genotype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1304)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 1304)
  AUTHORS   Bai,C. and Chen,D.G.
  TITLE     NRCAM acts as a prognostic biomarker and promotes the tumor
            progression in gastric cancer via EMT pathway
  JOURNAL   Tissue Cell 77, 101859 (2022)
   PUBMED   35763884
  REMARK    GeneRIF: NRCAM acts as a prognostic biomarker and promotes the
            tumor progression in gastric cancer via EMT pathway.
REFERENCE   6  (residues 1 to 1304)
  AUTHORS   Wang,B., Williams,H., Du,J.S., Terrett,J. and Kenwrick,S.
  TITLE     Alternative splicing of human NrCAM in neural and nonneural tissues
  JOURNAL   Mol Cell Neurosci 10 (5-6), 287-295 (1998)
   PUBMED   9604207
REFERENCE   7  (residues 1 to 1304)
  AUTHORS   Grumet,M.
  TITLE     Nr-CAM: a cell adhesion molecule with ligand and receptor functions
  JOURNAL   Cell Tissue Res 290 (2), 423-428 (1997)
   PUBMED   9321706
  REMARK    Review article
REFERENCE   8  (residues 1 to 1304)
  AUTHORS   Sakurai,T., Lustig,M., Nativ,M., Hemperly,J.J., Schlessinger,J.,
            Peles,E. and Grumet,M.
  TITLE     Induction of neurite outgrowth through contactin and Nr-CAM by
            extracellular regions of glial receptor tyrosine phosphatase beta
  JOURNAL   J Cell Biol 136 (4), 907-918 (1997)
   PUBMED   9049255
REFERENCE   9  (residues 1 to 1304)
  AUTHORS   Volkmer,H., Leuschner,R., Zacharias,U. and Rathjen,F.G.
  TITLE     Neurofascin induces neurites by heterophilic interactions with
            axonal NrCAM while NrCAM requires F11 on the axonal surface to
            extend neurites
  JOURNAL   J Cell Biol 135 (4), 1059-1069 (1996)
   PUBMED   8922386
REFERENCE   10 (residues 1 to 1304)
  AUTHORS   Lane,R.P., Chen,X.N., Yamakawa,K., Vielmetter,J., Korenberg,J.R.
            and Dreyer,W.J.
  TITLE     Characterization of a highly conserved human homolog to the chicken
            neural cell surface protein Bravo/Nr-CAM that maps to chromosome
            band 7q31
  JOURNAL   Genomics 35 (3), 456-465 (1996)
   PUBMED   8812479
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005058.1, AC007567.2 and
            AC005683.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 3, 2019 this sequence version replaced XP_005250430.1.
            
            Summary: Cell adhesion molecules (CAMs) are members of the
            immunoglobulin superfamily. This gene encodes a neuronal cell
            adhesion molecule with multiple immunoglobulin-like C2-type domains
            and fibronectin type-III domains. This ankyrin-binding protein is
            involved in neuron-neuron adhesion and promotes directional
            signaling during axonal cone growth. This gene is also expressed in
            non-neural tissues and may play a general role in cell-cell
            communication via signaling from its intracellular domain to the
            actin cytoskeleton during directional cell migration. Allelic
            variants of this gene have been associated with autism and
            addiction vulnerability. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1), as well as variant 7, encodes
            isoform A.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AJ001057.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379028.8/ ENSP00000368314.3
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1304
                     /product="neuronal cell adhesion molecule isoform A
                     precursor"
                     /note="NgCAM-related cell adhesion molecule; neuronal
                     surface protein Bravo"
                     /calculated_mol_wt=141124
     sig_peptide     1..24
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
                     /calculated_mol_wt=2785
     mat_peptide     25..1304
                     /product="Neuronal cell adhesion molecule.
                     /id=PRO_0000015057"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92823.3)"
                     /calculated_mol_wt=141124
     Region          46..140
                     /region_name="IgI_NrCAM"
                     /note="Immunoglobulin (Ig)-like domain of NrCAM (Ng
                     (neuronglia) CAM-related cell adhesion molecule); member
                     of the I-set of Ig superfamily (IgSF) domains; cd05874"
                     /db_xref="CDD:409458"
     Region          46..50
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409458"
     Region          55..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409458"
     Region          64..71
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409458"
     Region          77..82
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409458"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          85..87
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409458"
     Region          94..97
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409458"
     Region          102..106
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409458"
     Region          119..127
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409458"
     Region          130..140
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409458"
     Region          149..238
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          163..167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          177..181
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          200..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          215..220
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          231..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            245
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            251
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          277..358
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          288..292
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          301..305
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            314
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          323..327
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          337..342
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          350..353
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          362..450
                     /region_name="Ig4_NrCAM"
                     /note="Fourth immunoglobulin (Ig)-like domain of NrCAM
                     (NgCAM-related cell adhesion molecule); cd05868"
                     /db_xref="CDD:409454"
     Region          378..382
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409454"
     Region          391..395
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409454"
     Region          415..419
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409454"
     Region          429..434
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409454"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          442..445
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409454"
     Region          459..542
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          472..476
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          485..489
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            507
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          508..512
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          522..527
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          535..538
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          546..1109
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            619
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          647..737
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(647,713,728)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            716
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            order(729..730,732..733)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            802
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            858
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            993
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1009
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1019
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1072
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1083
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1168..1190
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92823.3)"
     Region          1191..1280
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     Region          1199..1304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1221
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q810U4; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1225
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q810U4; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q810U4; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q810U4; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q810U4; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97686; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q810U4; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q810U4; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q810U4; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     CDS             1..1304
                     /gene="NRCAM"
                     /gene_synonym="NEDNMS"
                     /coded_by="NM_001037132.4:526..4440"
                     /note="isoform A precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS47686.1"
                     /db_xref="GeneID:4897"
                     /db_xref="HGNC:HGNC:7994"
                     /db_xref="MIM:601581"
ORIGIN      
        1 mqlkimpkkk rlsagrvpli lflcqmisal evpldpklle dlvqpptitq qspkdyiidp
       61 reniviqcea kgkpppsfsw trngthfdid kdplvtmkpg tgtliinims egkaetyegv
      121 yqctarnerg aavsnnivvr psrsplwtke klepitlqsg qslvlpcrpp iglpppiifw
      181 mdnsfqrlpq servsqglng dlyfsnvlpe dtredyicya rfnhtqtiqq kqpisvkvis
      241 vdelndtiaa nlsdtefyga kssrerpptf ltpegnasnk eelrgnvlsl eciaeglptp
      301 iiywakedgm lpknrtvykn fektlqiihv seadsgnyqc iaknalgaih htisvrvkaa
      361 pywitapqnl vlspgedgtl icrangnpkp riswltngvp ieiapddpsr kidgdtiifs
      421 nvqerssavy qcnasneygy llanafvnvl aeppriltpa ntlyqvianr palldcaffg
      481 splptiewfk gakgsalhed iyvlhengtl eipvaqkdst gtytcvarnk lgmaknevhl
      541 eikdptwivk qpeyavvqrg smvsfeckvk hdhtlsltvl wlkdnrelps derftvdkdh
      601 lvvadvsddd sgtytcvant tldsvsasav lsvvaptptp apvydvpnpp fdleltdqld
      661 ksvqlswtpg ddnnspitkf iieyedamhk pglwhhqtev sgtqttaqlk lspyvnysfr
      721 vmavnsigks lpseaseqyl tkasepdknp taveglgsep dnlvitwkpl ngfesngpgl
      781 qykvswrqkd gddewtsvvv anvskyivsg tptfvpylik vqalndmgfa pepavvmghs
      841 gedlpmvapg nvrvnvvnst laevhwdpvp lksirghlqg yriyywktqs sskrnrrhie
      901 kkiltfqgsk thgmlpglep fshytlnvrv vngkgegpas pdrvfntpeg vpsapsslki
      961 vnptldsltl ewdppshpng ilteytlkyq pinsthelgp lvdlkipank trwtlknlnf
     1021 strykfyfya qtsagsgsqi teeavttvde agilppdvga gkvqavnpri snltaaaaet
     1081 yanisweyeg pehvnfyvey gvagskeewr keivngsrsf fglkglmpgt aykvrvgavg
     1141 dsgfvssedv fetgpamasr qvdiatqgwf iglmcavall ilillivcfi rrnkggkypv
     1201 kekedahadp eiqpmkeddg tfgeysdaed hkplkkgsrt psdrtvkked sddslvdyge
     1261 gvngqfnedg sfigqysgkk ekepaegnes seapspvnam nsfv
//
LOCUS       NP_001369241             347 aa            linear   PRI 21-NOV-2025
DEFINITION  ataxin-7-like protein 3 isoform b [Homo sapiens].
ACCESSION   NP_001369241
VERSION     NP_001369241.1
DBSOURCE    REFSEQ: accession NM_001382312.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Passet,M., Kim,R., Gachet,S., Sigaux,F., Chaumeil,J., Galland,A.,
            Sexton,T., Quentin,S., Hernandez,L., Larcher,L., Bergugnat,H.,
            Ye,T., Karasu,N., Caye,A., Heizmann,B., Duluc,I., Chevallier,P.,
            Rousselot,P., Huguet,F., Leguay,T., Hunault,M., Pflumio,F.,
            Freund,J.N., Lobry,C., Lheritier,V., Dombret,H., Domon-Dell,C.,
            Soulier,J., Boissel,N. and Clappier,E.
  TITLE     Concurrent CDX2 cis-deregulation and UBTF::ATXN7L3 fusion define a
            novel high-risk subtype of B-cell ALL
  JOURNAL   Blood 139 (24), 3505-3518 (2022)
   PUBMED   35316324
  REMARK    GeneRIF: Concurrent CDX2 cis-deregulation and UBTF::ATXN7L3 fusion
            define a novel high-risk subtype of B-cell ALL.
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Kimura,S., Montefiori,L., Iacobucci,I., Zhao,Y., Gao,Q.,
            Paietta,E.M., Haferlach,C., Laird,A.D., Mead,P.E., Gu,Z., Stock,W.,
            Litzow,M., Rowe,J.M., Luger,S.M., Hunger,S.P., Ryland,G.L.,
            Schmidt,B., Ekert,P.G., Oshlack,A., Grimmond,S.M., Rehn,J.,
            Breen,J., Yeung,D., White,D.L., Aldoss,I., Jabbour,E.J., Pui,C.H.,
            Meggendorfer,M., Walter,W., Kern,W., Haferlach,T., Brady,S.,
            Zhang,J., Roberts,K.G., Blombery,P. and Mullighan,C.G.
  TITLE     Enhancer retargeting of CDX2 and UBTF::ATXN7L3 define a subtype of
            high-risk B-progenitor acute lymphoblastic leukemia
  JOURNAL   Blood 139 (24), 3519-3531 (2022)
   PUBMED   35192684
  REMARK    GeneRIF: Enhancer retargeting of CDX2 and UBTF::ATXN7L3 define a
            subtype of high-risk B-progenitor acute lymphoblastic leukemia.
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Helmlinger,D., Hardy,S., Sasorith,S., Klein,F., Robert,F.,
            Weber,C., Miguet,L., Potier,N., Van-Dorsselaer,A., Wurtz,J.M.,
            Mandel,J.L., Tora,L. and Devys,D.
  TITLE     Ataxin-7 is a subunit of GCN5 histone acetyltransferase-containing
            complexes
  JOURNAL   Hum Mol Genet 13 (12), 1257-1265 (2004)
   PUBMED   15115762
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Martinez,E., Palhan,V.B., Tjernberg,A., Lymar,E.S., Gamper,A.M.,
            Kundu,T.K., Chait,B.T. and Roeder,R.G.
  TITLE     Human STAGA complex is a chromatin-acetylating transcription
            coactivator that interacts with pre-mRNA splicing and DNA
            damage-binding factors in vivo
  JOURNAL   Mol Cell Biol 21 (20), 6782-6795 (2001)
   PUBMED   11564863
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Brand,M., Moggs,J.G., Oulad-Abdelghani,M., Lejeune,F.,
            Dilworth,F.J., Stevenin,J., Almouzni,G. and Tora,L.
  TITLE     UV-damaged DNA-binding protein in the TFTC complex links DNA damage
            recognition to nucleosome acetylation
  JOURNAL   EMBO J 20 (12), 3187-3196 (2001)
   PUBMED   11406595
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Brand,M., Yamamoto,K., Staub,A. and Tora,L.
  TITLE     Identification of TATA-binding protein-free TAFII-containing
            complex subunits suggests a role in nucleosome acetylation and
            signal transduction
  JOURNAL   J Biol Chem 274 (26), 18285-18289 (1999)
   PUBMED   10373431
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Wieczorek,E., Brand,M., Jacq,X. and Tora,L.
  TITLE     Function of TAF(II)-containing complex without TBP in transcription
            by RNA polymerase II
  JOURNAL   Nature 393 (6681), 187-191 (1998)
   PUBMED   9603525
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004596.2.
            
            Transcript Variant: This variant (5), as well as variants 2, 4, and
            6, encodes isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853559.14314.1,
                                           SRR11853561.12761.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..347
                     /product="ataxin-7-like protein 3 isoform b"
                     /calculated_mol_wt=38520
     Region          80..112
                     /region_name="Sgf11"
                     /note="Sgf11 (transcriptional regulation protein);
                     pfam08209"
                     /db_xref="CDD:369754"
     Region          116..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CW9.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q14CW9.1)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14CW9.1)"
     Region          <208..>237
                     /region_name="SCA7"
                     /note="zinc-binding domain; pfam08313"
                     /db_xref="CDD:462422"
     Region          275..347
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CW9.1)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q14CW9.1)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14CW9.1)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14CW9.1)"
     CDS             1..347
                     /gene="ATXN7L3"
                     /gene_synonym="HATONS; SGF11"
                     /coded_by="NM_001382312.1:878..1921"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS42345.1"
                     /db_xref="GeneID:56970"
                     /db_xref="HGNC:HGNC:25416"
                     /db_xref="MIM:619010"
ORIGIN      
        1 mkmeemslsg ldnskleaia qeiyadlved sclgfcfevh ravkcgyffl ddtdpdsmkd
       61 feivdqpgld ifgqvfnqwk skecvcpncs rsiaasrfap hlekclgmgr nssrianrri
      121 ansnnmnkse sdqednddin dndwsygsek kakkrksdkn pnsprrsksl khkngelsns
      181 dpfkynnstg isyetlgpee lrsllttqcg visehtkkmc trslrcpqht deqrrtvriy
      241 flgpsavlpe vessldndsf dmtdsqalis rlqwdgssdl spsdsgsskt senqgwglgt
      301 nssesrktkk kkshlslvgt asglgsnkkk kpkppapptp siyddin
//
LOCUS       NP_001092283             369 aa            linear   PRI 21-NOV-2025
DEFINITION  septin-8 isoform d [Homo sapiens].
ACCESSION   NP_001092283
VERSION     NP_001092283.1
DBSOURCE    REFSEQ: accession NM_001098813.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Liu,H., Yan,P., Wu,C., Rao,M., Zhu,J., Lv,L., Li,W., Liang,Y.,
            Qi,S., Lu,K. and Kong,E.
  TITLE     Palmitoylated Sept8-204 modulates learning and anxiety by
            regulating filopodia arborization and actin dynamics
  JOURNAL   Sci Signal 16 (814), eadi8645 (2023)
   PUBMED   38051778
  REMARK    GeneRIF: Palmitoylated Sept8-204 modulates learning and anxiety by
            regulating filopodia arborization and actin dynamics.
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Keele,G.R., Prokop,J.W., He,H., Holl,K., Littrell,J., Deal,A.W.,
            Kim,Y., Kyle,P.B., Attipoe,E., Johnson,A.C., Uhl,K.L.,
            Sirpilla,O.L., Jahanbakhsh,S., Robinson,M., Levy,S., Valdar,W.,
            Garrett,M.R. and Solberg Woods,L.C.
  TITLE     Sept8/SEPTIN8 involvement in cellular structure and kidney damage
            is identified by genetic mapping and a novel human tubule hypoxic
            model
  JOURNAL   Sci Rep 11 (1), 2071 (2021)
   PUBMED   33483609
  REMARK    GeneRIF: Sept8/SEPTIN8 involvement in cellular structure and kidney
            damage is identified by genetic mapping and a novel human tubule
            hypoxic model.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Macara,I.G., Baldarelli,R., Field,C.M., Glotzer,M., Hayashi,Y.,
            Hsu,S.C., Kennedy,M.B., Kinoshita,M., Longtine,M., Low,C.,
            Maltais,L.J., McKenzie,L., Mitchison,T.J., Nishikawa,T., Noda,M.,
            Petty,E.M., Peifer,M., Pringle,J.R., Robinson,P.J., Roth,D.,
            Russell,S.E., Stuhlmann,H., Tanaka,M., Tanaka,T., Trimble,W.S.,
            Ware,J., Zeleznik-Le,N.J. and Zieger,B.
  TITLE     Mammalian septins nomenclature
  JOURNAL   Mol Biol Cell 13 (12), 4111-4113 (2002)
   PUBMED   12475938
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Yang,T., Gao,Y.K. and Chen,J.Y.
  TITLE     KIAA0202, a human septin family member, interacting with hPFTAIRE1
  JOURNAL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 34 (4),
            520-525 (2002)
   PUBMED   12098780
REFERENCE   8  (residues 1 to 369)
  AUTHORS   Blaser,S., Jersch,K., Hainmann,I., Wunderle,D., Zgaga-Griesz,A.,
            Busse,A. and Zieger,B.
  TITLE     Human septin-septin interaction: CDCrel-1 partners with KIAA0202
  JOURNAL   FEBS Lett 519 (1-3), 169-172 (2002)
   PUBMED   12023038
REFERENCE   9  (residues 1 to 369)
  AUTHORS   Wenderfer,S.E., Slack,J.P., McCluskey,T.S. and Monaco,J.J.
  TITLE     Identification of 40 genes on a 1-Mb contig around the IL-4
            cytokine family gene cluster on mouse chromosome 11
  JOURNAL   Genomics 63 (3), 354-373 (2000)
   PUBMED   10704283
REFERENCE   10 (residues 1 to 369)
  AUTHORS   Frazer,K.A., Ueda,Y., Zhu,Y., Gifford,V.R., Garofalo,M.R.,
            Mohandas,N., Martin,C.H., Palazzolo,M.J., Cheng,J.F. and Rubin,E.M.
  TITLE     Computational and biological analysis of 680 kb of DNA sequence
            from the human 5q31 cytokine gene cluster region
  JOURNAL   Genome Res 7 (5), 495-512 (1997)
   PUBMED   9149945
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004775.1, DA261871.1,
            AF440763.1 and AF179995.1.
            
            Summary: This gene is a member of the septin family of nucleotide
            binding proteins, originally described in yeast as cell division
            cycle regulatory proteins. Septins are highly conserved in yeast,
            Drosophila, and mouse, and appear to regulate cytoskeletal
            organization. Disruption of septin function disturbs cytokinesis
            and results in large multinucleate or polyploid cells. Multiple
            alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jul
            2014].
            
            Transcript Variant: This variant (4) differs in the 5' and 3' UTRs
            and has multiple coding region differences, compared to variant 1.
            These differences cause translation initiation at a downstream AUG
            and translation termination at an alternate stop codon. The
            resulting isoform (d) is shorter at the N- and C-termini compared
            to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4330519.1,
                                           SRR14038191.1018150.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.1"
     Protein         1..369
                     /product="septin-8 isoform d"
                     /calculated_mol_wt=43388
     Region          1..249
                     /region_name="CDC_Septin"
                     /note="CDC/Septin GTPase family; cd01850"
                     /db_xref="CDD:206649"
     Site            18..26
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206649"
     Site            20
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206649"
     Site            43..46
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            order(45..83,85..92)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Site            126..129
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            181..183
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     CDS             1..369
                     /gene="SEPTIN8"
                     /gene_synonym="SEP2; SEPT8; Septin-8"
                     /coded_by="NM_001098813.2:488..1597"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS47262.1"
                     /db_xref="GeneID:23176"
                     /db_xref="HGNC:HGNC:16511"
                     /db_xref="MIM:608418"
ORIGIN      
        1 mntlfnttfe teeashheac vrlrpqtydl qesnvqlklt ivdavgfgdq inkdesyrpi
       61 vdyidaqfen ylqeelkirr slfdyhdtri hvclyfitpt ghslksldlv tmkkldskvn
      121 iipiiakadt iskselhkfk ikimgelvsn gvqiyqfptd deavaeinav mnahlpfavv
      181 gsteevkvgn klvrarqypw gvvqvenenh cdfvklreml irvnmedlre qthsrhyely
      241 rrckleemgf qdsdgdsqpf slqetyeakr keflselqrk eeemrqmfvn kvketelelk
      301 ekerelhekf ehlkrvhqee krkveekrre leeetnafnr rkaavealqs qalhatsqqp
      361 lrkdkdkkn
//
LOCUS       NP_001186871            2476 aa            linear   PRI 21-NOV-2025
DEFINITION  protein DOP1A isoform b [Homo sapiens].
ACCESSION   NP_001186871
VERSION     NP_001186871.1
DBSOURCE    REFSEQ: accession NM_001199942.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2476)
  AUTHORS   Mahajan,D., Tie,H.C., Chen,B. and Lu,L.
  TITLE     Dopey1-Mon2 complex binds to dual-lipids and recruits kinesin-1 for
            membrane trafficking
  JOURNAL   Nat Commun 10 (1), 3218 (2019)
   PUBMED   31324769
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2476)
  AUTHORS   Lend,A.K., Kazantseva,A., Kivil,A., Valvere,V. and Palm,K.
  TITLE     Diagnostic significance of alternative splice variants of REST and
            DOPEY1 in the peripheral blood of patients with breast cancer
  JOURNAL   Tumour Biol 36 (4), 2473-2480 (2015)
   PUBMED   25424701
  REMARK    GeneRIF: Assessment of REST-N50 and DOPEY1v2 may prove useful in
            diagnostic blood tests of breast cancer. REST-N50 shows a high
            potential as a blood biomarker for evaluating the effectiveness of
            therapy in the neoadjuvant setting.
REFERENCE   3  (residues 1 to 2476)
  AUTHORS   Gillingham,A.K., Whyte,J.R., Panic,B. and Munro,S.
  TITLE     Mon2, a relative of large Arf exchange factors, recruits Dop1 to
            the Golgi apparatus
  JOURNAL   J Biol Chem 281 (4), 2273-2280 (2006)
   PUBMED   16301316
REFERENCE   4  (residues 1 to 2476)
  AUTHORS   Pascon,R.C. and Miller,B.L.
  TITLE     Morphogenesis in Aspergillus nidulans requires Dopey (DopA), a
            member of a novel family of leucine zipper-like proteins conserved
            from yeast to humans
  JOURNAL   Mol Microbiol 36 (6), 1250-1264 (2000)
   PUBMED   10931277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL139333.10 and AL121716.16.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 5' coding region and has an alternate in-frame
            exon in the 3' coding region compared to variant 1. The resulting
            protein (isoform b) is longer compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.147909.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2476
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..2476
                     /product="protein DOP1A isoform b"
                     /note="homolog of yeast DOP1; protein dopey-1; dopey
                     family member 1; protein DOP1A"
                     /calculated_mol_wt=278666
     Region          11..297
                     /region_name="Dopey_N"
                     /note="Dopey, N-terminal; pfam04118"
                     /db_xref="CDD:461183"
     Region          550..591
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWR5.1)"
     Region          616..637
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWR5.1)"
     Region          696..724
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWR5.1)"
     Site            1257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BL99; propagated from
                     UniProtKB/Swiss-Prot (Q5JWR5.1)"
     Region          1273..1306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWR5.1)"
     Region          <2082..2318
                     /region_name="Dopey_N"
                     /note="Dopey, N-terminal; cl04407"
                     /db_xref="CDD:471021"
     CDS             1..2476
                     /gene="DOP1A"
                     /gene_synonym="dJ202D23.2; DOP1; DOPEY1; KIAA1117"
                     /coded_by="NM_001199942.2:256..7686"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS64467.1"
                     /db_xref="GeneID:23033"
                     /db_xref="HGNC:HGNC:21194"
                     /db_xref="MIM:616823"
ORIGIN      
        1 mnteelells dskyrnyvaa idkalknfey ssewadlisa lgklnkvlqn nakyqvvpkk
       61 ltigkrlaqc lhpalpggvh rkaletyeii fkiigpkrla kdlflyssgl fpllanaams
      121 vkptllslye iyylplgktl kpglqglltg ilpgleegse yyertnmlle kvaaavdqsa
      181 fysalwgsll tspavrlpgi tyvlahlnrk lsmedqlyii gsdielmvea vstsvqdssv
      241 lvqrstldli lfcfpfhmsq atrpdmiril saalhvvlrr dmslnrrlya wllgprstrh
      301 snpeehatyy fttfskellv qamvgilqvn gfgeentlmq dlkpfrilis lldkpelgpv
      361 iledvlievf rtlysqckae ldlqteppfs kdhaqlsskl renkktaeli ktanllfnsf
      421 epyymwdyva rwfeeccrrt lhvrlqigpg dsndsselql tnfcllvdfl ldivslptrs
      481 mrvlcqetyi eiqtehlpql llrmisalts hlqtlhlsel tdslrlcski lskvqpplls
      541 astggvlqfp sgqnnsvkew edkkvssvsh enptevfedg enppssrsse sgftefiqyq
      601 adrtddidre lsegqgaaai pigstssete tastvgseet iiqtpsvvtq gtatrsrkta
      661 qktamqccle yvqqfltrli nlyiiqnnsf sqslatehqg dlgreqgets kwdrnsqgdv
      721 kekniskqkt skeylsafla acqlflecss fpvyiaegnh tselrsekle tdcehvqppq
      781 wlqtlmnacs qasdfsvqsv aislvmdlvg ltqsvamvtg eninsvepaq plspnqgrva
      841 vvirppltqg nlryiaekte ffkhvaltlw dqlgdgtpqh hqksvelfyq lhnlvpsssi
      901 cedvisqqlt hkdkkirmea hakfavlwhl trdlhinkss sfvrsfdrsl fimldslnsl
      961 dgstssvgqa wlnqvlqrhd iarvleplll lllhpktqrv svqrvqaery wnkspcypge
     1021 esdkhfmqnf acsnvsqvql itskgngekp ltmdeienfs ltvnplsdrl sllstsseti
     1081 pmvvsdfdlp dqqieilqss dsgcsqssag dnlsyevdpe tvnaqedsqm pkesspdddv
     1141 qqvvfdlick vvsglevesa svtsqleiea mppkcsdidp deetikiedd siqqsqnall
     1201 snessqflsv saegghecva ngisrnsssp cisgtthtlh dssvasietk srqrshssiq
     1261 fsfkeklsek vseketivke sgkqpgakpk vklarkkddd kkkssneklk qtsvffsdgl
     1321 dlenwyscge gdiseiesdm gspgsrkspn fnihplyqhv llylqlydss rtlyafsaik
     1381 ailktnpiaf vnaisttsvn naytpqlsll qnllarhris vmgkdfyshi pvdsnhnfrs
     1441 smyieilisl clyymrshyp thvkvtaqdl ignrnmqmms ieiltllfte lakviessak
     1501 gfpsfisdml skckvqkvil hcllssifsa qkwhsekmag knlvaveegf sedslinfse
     1561 defdngstlq sqllkvlqrl ivlehrvmti peenetgfdf vvsdlehisp hqpmtslqyl
     1621 haqpitcqgm flcaviralh qhcackmhpq wiglitstlp ymgkvlqrvv vsvtlqlcrn
     1681 ldnliqqyky etglsdsrpl wmasiippdm iltllegita iihyclldpt tqyhqllvsv
     1741 dqkhlfears gilsilhmim ssvtllwsil hqadssekmt iaasasltti nlgatknlrq
     1801 qilellgpis mnhgvhfmaa iafvwnerrq nktttrtkvi paaseeqlll velvrsisvm
     1861 raetviqtvk evlkqppaia kdkkhlslev cmlqffyayi qripvpnlvd swasllillk
     1921 dsiqlslpap gqflilgvln efimknpsle nkkdqrdlqd vthkivdaig aiagssleqt
     1981 twlrrnlevk pspkimvdgt nlesdvedml spametanit psvysvhalt llsevlahll
     2041 dmvfysdeke rvipllvnim hyvvpylrnh sahnapsyra cvqllsslsg yqytrrawkk
     2101 eafdlfmdps ffqmdascvn hwraimdnlm thdkttfrdl mtrvavaqss slnlfanrdv
     2161 eleqramllk rlafaifsse idqyqkylpd iqerlveslr lpqvptlhsq vflffrvlll
     2221 rmspqhltsl wptmitelvq vfllmeqelt adedisrtsg psvagletty tggngfstsy
     2281 nsqrwlnlyl sackfldlal alpsenlpqf qmyrwafipe asddsglevr rqgihqrefk
     2341 pyvvrlakll rkrakdkeed fktvilegle makhqknpee dnsgrtlgwe pghllltict
     2401 vrsmeqllpf fnvlsqvfns kvtsrcgghs gspilysnaf pnkdmklenh kpcsskarqk
     2461 ieemvekdfl egmikt
//
LOCUS       NP_001340446             507 aa            linear   PRI 21-NOV-2025
DEFINITION  integrator complex subunit 10 isoform n [Homo sapiens].
ACCESSION   NP_001340446
VERSION     NP_001340446.1
DBSOURCE    REFSEQ: accession NM_001353517.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Lin,M.H., Jensen,M.K., Elrod,N.D., Chu,H.F., Haseley,M., Beam,A.C.,
            Huang,K.L., Chiang,W., Russell,W.K., Williams,K., Proschel,C.,
            Wagner,E.J. and Tong,L.
  TITLE     Cytoplasmic binding partners of the Integrator endonuclease INTS11
            and its paralog CPSF73 are required for their nuclear function
  JOURNAL   Mol Cell 84 (15), 2900-2917 (2024)
   PUBMED   39032490
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Razew,M., Fraudeau,A., Pfleiderer,M.M., Linares,R. and Galej,W.P.
  TITLE     Structural basis of the Integrator complex assembly and association
            with transcription factors
  JOURNAL   Mol Cell 84 (13), 2542-2552 (2024)
   PUBMED   38823386
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Fianu,I., Ochmann,M., Walshe,J.L., Dybkov,O., Cruz,J.N., Urlaub,H.
            and Cramer,P.
  TITLE     Structural basis of Integrator-dependent RNA polymerase II
            termination
  JOURNAL   Nature 629 (8010), 219-227 (2024)
   PUBMED   38570683
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Offley,S.R., Pfleiderer,M.M., Zucco,A., Fraudeau,A., Welsh,S.A.,
            Razew,M., Galej,W.P. and Gardini,A.
  TITLE     A combinatorial approach to uncover an additional Integrator
            subunit
  JOURNAL   Cell Rep 42 (3), 112244 (2023)
   PUBMED   36920904
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Wu,Y., Lin,Z., Luo,M., Yu,X., Chen,S. and Liu,L.
  TITLE     Effects of genetic polymorphisms in INTS10 and their interaction
            with environmental factors on progression from persistent HBV
            infection to hepatocellular carcinoma
  JOURNAL   Mol Carcinog 60 (9), 620-626 (2021)
   PUBMED   34133796
  REMARK    GeneRIF: Effects of genetic polymorphisms in INTS10 and their
            interaction with environmental factors on progression from
            persistent HBV infection to hepatocellular carcinoma.
REFERENCE   6  (residues 1 to 507)
  AUTHORS   Weissglas-Volkov,D., Aguilar-Salinas,C.A., Nikkola,E., Deere,K.A.,
            Cruz-Bautista,I., Arellano-Campos,O., Munoz-Hernandez,L.L.,
            Gomez-Munguia,L., Ordonez-Sanchez,M.L., Reddy,P.M., Lusis,A.J.,
            Matikainen,N., Taskinen,M.R., Riba,L., Cantor,R.M.,
            Sinsheimer,J.S., Tusie-Luna,T. and Pajukanta,P.
  TITLE     Genomic study in Mexicans identifies a new locus for triglycerides
            and refines European lipid loci
  JOURNAL   J Med Genet 50 (5), 298-308 (2013)
   PUBMED   23505323
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Ellinghaus,E., Stanulla,M., Richter,G., Ellinghaus,D., te
            Kronnie,G., Cario,G., Cazzaniga,G., Horstmann,M., Panzer
            Grumayer,R., Cave,H., Trka,J., Cinek,O., Teigler-Schlegel,A.,
            ElSharawy,A., Hasler,R., Nebel,A., Meissner,B., Bartram,T.,
            Lescai,F., Franceschi,C., Giordan,M., Nurnberg,P., Heinzow,B.,
            Zimmermann,M., Schreiber,S., Schrappe,M. and Franke,A.
  TITLE     Identification of germline susceptibility loci in
            ETV6-RUNX1-rearranged childhood acute lymphoblastic leukemia
  JOURNAL   Leukemia 26 (5), 902-909 (2012)
   PUBMED   22076464
REFERENCE   8  (residues 1 to 507)
  AUTHORS   Kooner,J.S., Chambers,J.C., Aguilar-Salinas,C.A., Hinds,D.A.,
            Hyde,C.L., Warnes,G.R., Gomez Perez,F.J., Frazer,K.A., Elliott,P.,
            Scott,J., Milos,P.M., Cox,D.R. and Thompson,J.F.
  TITLE     Genome-wide scan identifies variation in MLXIPL associated with
            plasma triglycerides
  JOURNAL   Nat Genet 40 (2), 149-151 (2008)
   PUBMED   18193046
REFERENCE   9  (residues 1 to 507)
  AUTHORS   Baillat,D., Hakimi,M.A., Naar,A.M., Shilatifard,A., Cooch,N. and
            Shiekhattar,R.
  TITLE     Integrator, a multiprotein mediator of small nuclear RNA
            processing, associates with the C-terminal repeat of RNA polymerase
            II
  JOURNAL   Cell 123 (2), 265-276 (2005)
   PUBMED   16239144
REFERENCE   10 (residues 1 to 507)
  AUTHORS   Yuryev,A. and Wennogle,L.P.
  TITLE     Novel raf kinase protein-protein interactions found by an
            exhaustive yeast two-hybrid analysis
  JOURNAL   Genomics 81 (2), 112-125 (2003)
   PUBMED   12620389
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC107964.4.
            
            Summary: INTS10 is a subunit of the Integrator complex, which
            associates with the C-terminal domain of RNA polymerase II large
            subunit (POLR2A; MIM 180660) and mediates 3-prime end processing of
            small nuclear RNAs U1 (RNU1; MIM 180680) and U2 (RNU2; MIM 180690)
            (Baillat et al., 2005 [PubMed 16239144]).[supplied by OMIM, Mar
            2008].
            
            Transcript Variant: This variant (14), along with variants 15 and
            16, encodes isoform n.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.240516.1,
                                           SRR3476690.466213.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..507
                     /product="integrator complex subunit 10 isoform n"
                     /calculated_mol_wt=58441
     CDS             1..507
                     /gene="INTS10"
                     /gene_synonym="C8orf35; INT10"
                     /coded_by="NM_001353517.2:801..2324"
                     /note="isoform n is encoded by transcript variant 14"
                     /db_xref="GeneID:55174"
                     /db_xref="HGNC:HGNC:25548"
                     /db_xref="MIM:611353"
ORIGIN      
        1 mspskrssqk yiieglteks sqivdpwerl fkilnvvgmr cewqmdkgrr sygdilhrmk
       61 dlcrymnnfd seahakyknq vvystmlvff knafqyvnsi qpslfqgpna psqvplvlle
      121 dvsnvygdve idrnkhihkk rklaegrekt mssddedcsa kgrnrhivvn kaelanstev
      181 lesfklares wellyslefl dkeftricla wktdtwlwlr ifltdmiiyq gqykkaiasl
      241 hhlaalqgsi sqpqitgqgt lehqraliql atchfalgey rmtcekvldl mcymvlpiqd
      301 ggksqeepsk vkpkfrkgsd lkllpctska impyclhlml acfklraftd nrddmalghv
      361 ivllqqewpr genlflkavn kicqqgnfqy enffnyvtni dmleefaylr tqeggkihle
      421 llpnqgmlik pssppmgllq qeflpvlqps iqtadrhhtv trgitkgvke dfrlamerqv
      481 srcgenlmvv lhrfcineki lllqtlt
//
LOCUS       NP_001363695             558 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 25 [Homo sapiens].
ACCESSION   NP_001363695 XP_005265835
VERSION     NP_001363695.1
DBSOURCE    REFSEQ: accession NM_001376766.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Muckenfuss,L.M., Migenda Herranz,A.C., Boneberg,F.M., Clerici,M.
            and Jinek,M.
  TITLE     Fip1 is a multivalent interaction scaffold for processing factors
            in human mRNA 3' end biogenesis
  JOURNAL   Elife 11, e80332 (2022)
   PUBMED   36073787
  REMARK    GeneRIF: Fip1 is a multivalent interaction scaffold for processing
            factors in human mRNA 3' end biogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Tennenbaum,J., Groh,M., Venditti,L., Campos-Gazeau,F., Chalayer,E.,
            De Broucker,T., Hamidou,M., Hunault,M., Lyoubi,A., Meunier,R.,
            Muron,T., Sene,D., Slama,B., Guidoux,C., Lefevre,G., Kahn,J.E.,
            Denier,C. and Rohmer,J.
  TITLE     FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a Treatable
            Cause of Watershed Infarction
  JOURNAL   Stroke 52 (10), e605-e609 (2021)
   PUBMED   34304603
  REMARK    GeneRIF: FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a
            Treatable Cause of Watershed Infarction.
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 558)
  AUTHORS   Helbig,G., Lewandowski,K., Swiderska,A., Rodzaj,M., Seferynska,I.
            and Gajkowska-Kulik,J.
  TITLE     Exquisite response to imatinib mesylate in FIP1L1-PDGFRA-mutated
            hypereosinophilic syndrome: a 12-year experience of the Polish
            Hypereosinophilic Syndrome Study Group
  JOURNAL   Pol Arch Intern Med 130 (3), 255-257 (2020)
   PUBMED   32125294
  REMARK    GeneRIF: Exquisite response to imatinib mesylate in
            FIP1L1-PDGFRA-mutated hypereosinophilic syndrome: a 12-year
            experience of the Polish Hypereosinophilic Syndrome Study Group.
REFERENCE   6  (residues 1 to 558)
  AUTHORS   Cools,J., Quentmeier,H., Huntly,B.J., Marynen,P., Griffin,J.D.,
            Drexler,H.G. and Gilliland,D.G.
  TITLE     The EOL-1 cell line as an in vitro model for the study of
            FIP1L1-PDGFRA-positive chronic eosinophilic leukemia
  JOURNAL   Blood 103 (7), 2802-2805 (2004)
   PUBMED   14630792
  REMARK    GeneRIF: results indicate that the fusion of FIP1L1 to PDGFRA
            occurs rarely in leukemia cell lines
REFERENCE   7  (residues 1 to 558)
  AUTHORS   Kaufmann,I., Martin,G., Friedlein,A., Langen,H. and Keller,W.
  TITLE     Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements
            and stimulates poly(A) polymerase
  JOURNAL   EMBO J 23 (3), 616-626 (2004)
   PUBMED   14749727
REFERENCE   8  (residues 1 to 558)
  AUTHORS   Pardanani,A., Ketterling,R.P., Brockman,S.R., Flynn,H.C.,
            Paternoster,S.F., Shearer,B.M., Reeder,T.L., Li,C.Y., Cross,N.C.,
            Cools,J., Gilliland,D.G., Dewald,G.W. and Tefferi,A.
  TITLE     CHIC2 deletion, a surrogate for FIP1L1-PDGFRA fusion, occurs in
            systemic mastocytosis associated with eosinophilia and predicts
            response to imatinib mesylate therapy
  JOURNAL   Blood 102 (9), 3093-3096 (2003)
   PUBMED   12842979
  REMARK    GeneRIF: observations suggest that the FIP1L1-PDGFRA rearrangement
            occurs in an early hematopoietic progenitor and suggests that the
            molecular pathogenesis for a subset of SMCD patients is similar to
            that of HES
REFERENCE   9  (residues 1 to 558)
  AUTHORS   Griffin,J.H., Leung,J., Bruner,R.J., Caligiuri,M.A. and
            Briesewitz,R.
  TITLE     Discovery of a fusion kinase in EOL-1 cells and idiopathic
            hypereosinophilic syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (13), 7830-7835 (2003)
   PUBMED   12808148
REFERENCE   10 (residues 1 to 558)
  AUTHORS   Cools,J., DeAngelo,D.J., Gotlib,J., Stover,E.H., Legare,R.D.,
            Cortes,J., Kutok,J., Clark,J., Galinsky,I., Griffin,J.D.,
            Cross,N.C., Tefferi,A., Malone,J., Alam,R., Schrier,S.L.,
            Schmid,J., Rose,M., Vandenberghe,P., Verhoef,G., Boogaerts,M.,
            Wlodarska,I., Kantarjian,H., Marynen,P., Coutre,S.E., Stone,R. and
            Gilliland,D.G.
  TITLE     A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes
            as a therapeutic target of imatinib in idiopathic hypereosinophilic
            syndrome
  JOURNAL   N Engl J Med 348 (13), 1201-1214 (2003)
   PUBMED   12660384
  REMARK    GeneRIF: The hypereosinophilic syndrome may result from a novel
            fusion tyrosine kinase - FIP1L1-PDGFRalpha - that is a consequence
            of an interstitial chromosomal deletion.
            GeneRIF: Describes the fusion gene Fip1-like-1-PDGFRalpha in
            patients with idiopathic hypereosinophilic syndrome, mostly
            responsive to imatinib therapy.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098821.3 and AC058822.6.
            
            On Nov 20, 2019 this sequence version replaced XP_005265835.1.
            
            Summary: This gene encodes a subunit of the CPSF (cleavage and
            polyadenylation specificity factor) complex that polyadenylates the
            3' end of mRNA precursors. This gene, the homolog of yeast Fip1
            (factor interacting with PAP), binds to U-rich sequences of
            pre-mRNA and stimulates poly(A) polymerase activity. Its N-terminus
            contains a PAP-binding site and its C-terminus an RNA-binding
            domain. An interstitial chromosomal deletion on 4q12 creates an
            in-frame fusion of human genes FIP1L1 and PDGFRA (platelet-derived
            growth factor receptor, alpha). The FIP1L1-PDGFRA fusion gene
            encodes a constitutively activated tyrosine kinase that joins the
            first 233 amino acids of FIP1L1 to the last 523 amino acids of
            PDGFRA. This gene fusion and chromosomal deletion is the cause of
            some forms of idiopathic hypereosinophilic syndrome (HES). This
            syndrome, recently reclassified as chronic eosinophilic leukemia
            (CEL), is responsive to treatment with tyrosine kinase inhibitors.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.250126.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..558
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     25"
                     /note="rearranged in hypereosinophilia; pre-mRNA
                     3'-end-processing factor FIP1; FIP1-like 1 protein; factor
                     interacting with PAP; FIP1 like 1; FIP1L1 cleavage and
                     polyadenylation specific factor subunit"
                     /calculated_mol_wt=60529
     Region          154..196
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     CDS             1..558
                     /gene="FIP1L1"
                     /gene_synonym="FIP1; hFip1; Rhe"
                     /coded_by="NM_001376766.1:199..1875"
                     /note="isoform 25 is encoded by transcript variant 25"
                     /db_xref="CCDS:CCDS93496.1"
                     /db_xref="GeneID:81608"
                     /db_xref="HGNC:HGNC:19124"
                     /db_xref="MIM:607686"
ORIGIN      
        1 msageverlv selsggtggd eeeewlyggp wdvhvhsdla kdldenever peeenasanp
       61 psgiedetae ngvpkpkvte teddsdsdsd ddeddvhvti gdiktgapqy gsygtapvnl
      121 niktggrvyg ttgtkvkgvd ldapgsingv pllevdldsf edkpwrkpga dlsdyfnygf
      181 nedtwkayce kqkrirmgle vipvtsttnk itaedctmev tpgaeiqdgr fnlfkvqqgr
      241 tgnseketal pstkaeftsp pslfktglpp srnstssqsq tstasrkans svgkwqdryg
      301 raespdlrrl pgaidvigqt itisrvegrr ranensniqv lsersatevd nnfskpppff
      361 ppgappthlp pppflppppt vstapplipp pgipitvppp gfppppgapp psliptiesg
      421 hssgydsrsa rafpygnamk ndtdtgnmqk evmsvteqve kkkndiekdd tgrkrkpdis
      481 llevivdvam kvkkeivtgd tntknlkeak kekkravslp lnrrapklhl qnrhgfgllc
      541 ilvpevdtin lvifldnv
//
LOCUS       NP_001243692             324 aa            linear   PRI 21-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 1 [Homo sapiens].
ACCESSION   NP_001243692
VERSION     NP_001243692.1
DBSOURCE    REFSEQ: accession NM_001256763.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX419336.2, BC003599.1, AK130372.1 and AC022973.5.
            
            Transcript Variant: This variant (1) and variant 2 encode the same
            protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.214778.1,
                                           SRR1660807.202013.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 1"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=36617
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001256763.2:341..1315"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6361.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mgnllkvltc tdleqgpnff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqik smlq
//
LOCUS       NP_001026883             359 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial calcium uniporter regulator 1 [Homo sapiens].
ACCESSION   NP_001026883
VERSION     NP_001026883.1
DBSOURCE    REFSEQ: accession NM_001031713.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Fan,L., Yang,H., Zhang,B. and Ding,H.
  TITLE     MCUR1 is a prognostic biomarker for ovarian cancer patients
  JOURNAL   Cancer Biomark 33 (3), 311-316 (2022)
   PUBMED   34459387
  REMARK    GeneRIF: MCUR1 is a prognostic biomarker for ovarian cancer
            patients.
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Zulkifli,M., Neff,J.K., Timbalia,S.A., Garza,N.M., Chen,Y.,
            Watrous,J.D., Murgia,M., Trivedi,P.P., Anderson,S.K., Tomar,D.,
            Nilsson,R., Madesh,M., Jain,M. and Gohil,V.M.
  TITLE     Yeast homologs of human MCUR1 regulate mitochondrial proline
            metabolism
  JOURNAL   Nat Commun 11 (1), 4866 (2020)
   PUBMED   32978391
  REMARK    GeneRIF: Yeast homologs of human MCUR1 regulate mitochondrial
            proline metabolism.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 359)
  AUTHORS   Chaudhuri,D., Artiga,D.J., Abiria,S.A. and Clapham,D.E.
  TITLE     Mitochondrial calcium uniporter regulator 1 (MCUR1) regulates the
            calcium threshold for the mitochondrial permeability transition
  JOURNAL   Proc Natl Acad Sci U S A 113 (13), E1872-E1880 (2016)
   PUBMED   26976564
  REMARK    GeneRIF: MCUR1 regulates the calcium threshold for the
            mitochondrial permeability transition.
REFERENCE   7  (residues 1 to 359)
  AUTHORS   Vais,H., Tanis,J.E., Muller,M., Payne,R., Mallilankaraman,K. and
            Foskett,J.K.
  TITLE     MCUR1, CCDC90A, Is a Regulator of the Mitochondrial Calcium
            Uniporter
  JOURNAL   Cell Metab 22 (4), 533-535 (2015)
   PUBMED   26445506
REFERENCE   8  (residues 1 to 359)
  AUTHORS   Paupe,V., Prudent,J., Dassa,E.P., Rendon,O.Z. and Shoubridge,E.A.
  TITLE     CCDC90A (MCUR1) is a cytochrome c oxidase assembly factor and not a
            regulator of the mitochondrial calcium uniporter
  JOURNAL   Cell Metab 21 (1), 109-116 (2015)
   PUBMED   25565209
  REMARK    GeneRIF: CCDC90A is not directly implicated in MCU function, and
            that the Ca2+ uptake defect associated with loss of CCDC90A
            function is likely secondary to the respiratory chain deficiency.
REFERENCE   9  (residues 1 to 359)
  AUTHORS   Mallilankaraman,K., Cardenas,C., Doonan,P.J., Chandramoorthy,H.C.,
            Irrinki,K.M., Golenar,T., Csordas,G., Madireddi,P., Yang,J.,
            Muller,M., Miller,R., Kolesar,J.E., Molgo,J., Kaufman,B.,
            Hajnoczky,G., Foskett,J.K. and Madesh,M.
  TITLE     MCUR1 is an essential component of mitochondrial Ca2+ uptake that
            regulates cellular metabolism
  JOURNAL   Nat Cell Biol 14 (12), 1336-1343 (2012)
   PUBMED   23178883
  REMARK    Erratum:[Nat Cell Biol. 2013 Jan;15(1):123]
REFERENCE   10 (residues 1 to 359)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL023583.25.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.25322.1,
                                           SRR11853563.27808.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000379170.9/
                                                  ENSP00000368468.3
            RefSeq Select criteria             :: based on manual assertion,
                                                  conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p23"
     Protein         1..359
                     /product="mitochondrial calcium uniporter regulator 1"
                     /EC_number="1.1.1.41"
                     /note="coiled-coil domain-containing protein 90A,
                     mitochondrial; coiled-coil domain containing 90A; MCU
                     regulator 1; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=39563
     Site            69..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AQ8.1)"
     Region          166..358
                     /region_name="CCDC90-like"
                     /note="Coiled-coil domain-containing protein 90-like;
                     pfam07798"
                     /db_xref="CDD:462268"
     Site            339..358
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AQ8.1)"
     CDS             1..359
                     /gene="MCUR1"
                     /gene_synonym="C6orf79; CCDC90A; FMP32"
                     /coded_by="NM_001031713.4:129..1208"
                     /db_xref="CCDS:CCDS35495.1"
                     /db_xref="GeneID:63933"
                     /db_xref="HGNC:HGNC:21097"
                     /db_xref="MIM:616952"
ORIGIN      
        1 mdcgsvggqr tqrlpgrqrl lflpvglsgr pggsetsarr clsalsdglg alrprapaar
       61 ggvsraspll llllvpsprl aaaaprrqlg dwersrlgya appagrssaw rcspgvaaaa
      121 galpqyhgpa palvscrrel slsagslqle rkrrdftssg srklyfdtha lvclledngf
      181 atqqaeiivs alvkileanm divykdmvtk mqqeitfqqv msqianvkkd miileksefs
      241 alraenekik lelhqlkqqv mdevikvrtd tkldfnleks rvkelyslne kkllelrtei
      301 valhaqqdra ltqtdrkiet evaglktmle shkldnikyl agsiftcltv algfyrlwi
//
LOCUS       NP_001265855             616 aa            linear   PRI 21-NOV-2025
DEFINITION  peptidylprolyl isomerase domain and WD repeat-containing protein 1
            isoform 2 [Homo sapiens].
ACCESSION   NP_001265855
VERSION     NP_001265855.1
DBSOURCE    REFSEQ: accession NM_001278926.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Han,H.F., Chen,Q. and Zhao,W.W.
  TITLE     Long non-coding RNA RP11-284F21.9 functions as a ceRNA regulating
            PPWD1 by competitively binding to miR-769-3p in cervical carcinoma
  JOURNAL   Biosci Rep 40 (9) (2020)
   PUBMED   32936290
  REMARK    GeneRIF: Long non-coding RNA RP11-284F21.9 functions as a ceRNA
            regulating PPWD1 by competitively binding to miR-769-3p in cervical
            carcinoma.
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Zhang,X., Yan,C., Zhan,X., Li,L., Lei,J. and Shi,Y.
  TITLE     Structure of the human activated spliceosome in three
            conformational states
  JOURNAL   Cell Res 28 (3), 307-322 (2018)
   PUBMED   29360106
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Davis,T.L., Walker,J.R., Campagna-Slater,V., Finerty,P.J.,
            Paramanathan,R., Bernstein,G., MacKenzie,F., Tempel,W., Ouyang,H.,
            Lee,W.H., Eisenmesser,E.Z. and Dhe-Paganon,S.
  TITLE     Structural and biochemical characterization of the human
            cyclophilin family of peptidyl-prolyl isomerases
  JOURNAL   PLoS Biol 8 (7), e1000439 (2010)
   PUBMED   20676357
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Davis,T.L., Walker,J.R., Ouyang,H., MacKenzie,F., Butler-Cole,C.,
            Newman,E.M., Eisenmesser,E.Z. and Dhe-Paganon,S.
  TITLE     The crystal structure of human WD40 repeat-containing
            peptidylprolyl isomerase (PPWD1)
  JOURNAL   FEBS J 275 (9), 2283-2295 (2008)
   PUBMED   18397323
  REMARK    GeneRIF: The crystal structure of human PPWD1 was studied.
REFERENCE   6  (residues 1 to 616)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK300022.1, BC015385.1 and AC008560.6.
            
            Transcript Variant: This variant (2) includes an alternate exon in
            the 5' region and uses a downstream start codon, compared to
            variant 1. It encodes isoform 2 which is shorter and has a distinct
            N-terminus, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK300022.1, SRR14038197.2026670.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..616
                     /product="peptidylprolyl isomerase domain and WD
                     repeat-containing protein 1 isoform 2"
                     /EC_number="5.2.1.8"
                     /note="peptidylprolyl isomerase domain and WD
                     repeat-containing protein 1; spliceosome-associated
                     cyclophilin; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=70146
     Region          <59..289
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          106..147
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          161..189
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          196..247
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          253..296
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          465..613
                     /region_name="cyclophilin_WD40"
                     /note="cyclophilin-type peptidylprolyl cis- trans
                     isomerases (cyclophilins) having a WD40 domain. This group
                     consists of several hypothetical and putative eukaryotic
                     and bacterial proteins which have a cyclophilin domain and
                     a WD40 domain. Function of the...; cd01927"
                     /db_xref="CDD:238908"
     Site            order(504..505,510,561,563,571)
                     /site_type="active"
                     /db_xref="CDD:238908"
     CDS             1..616
                     /gene="PPWD1"
                     /coded_by="NM_001278926.2:143..1993"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS64161.1"
                     /db_xref="GeneID:23398"
                     /db_xref="HGNC:HGNC:28954"
                     /db_xref="MIM:618274"
ORIGIN      
        1 mrrtksagld lylwrqhwpr rgkqphevgi snsylvlefe rvyldnlpsa smyersymhr
       61 dvithvvctk tdfiitashd ghvkfwkkie egiefvkhfr shlgviesia vssegalfcs
      121 vgddkamkvf dvvnfdminm lklgyfpgqc ewiycpgdai ssvaasekst gkifiydgrg
      181 dnqplhifdk lhtspltqir lnpvykavvs sdksgmieyw tgppheykfp knvnweyktd
      241 tdlyefakck ayptsvcfsp dgkkiatigs drkvrifrfv tgklmrvfde slsmftelqq
      301 mrqqlpdmef grrmaverel ekvdavrlin ivfdetghfv lygtmlgikv invetnrcvr
      361 ilgkqenirv mqlalfqgia kkhraattie mkasenpvlq niqadptivc tsfkknrfym
      421 ftkrepedtk sadsdrdvfn ekpskeevma atqaegpkrv sdsaiihtsm gdihtklfpv
      481 ecpktvenfc vhsrngyyng htfhriikgf miqtgdptgt gmggesiwgg efedefhstl
      541 rhdrpytlsm anagsntngs qffitvvptp wldnkhtvfg rvtkgmevvq risnvkvnpk
      601 tdkpyedvsi initvk
//
LOCUS       NP_001171903             424 aa            linear   PRI 21-NOV-2025
DEFINITION  protein kinase C and casein kinase substrate in neurons protein 3
            [Homo sapiens].
ACCESSION   NP_001171903
VERSION     NP_001171903.1
DBSOURCE    REFSEQ: accession NM_001184974.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Tanaka,M., Nanba,D., Mori,S., Shiba,F., Ishiguro,H., Yoshino,K.,
            Matsuura,N. and Higashiyama,S.
  TITLE     ADAM binding protein Eve-1 is required for ectodomain shedding of
            epidermal growth factor receptor ligands
  JOURNAL   J Biol Chem 279 (40), 41950-41959 (2004)
   PUBMED   15280379
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Kessels,M.M. and Qualmann,B.
  TITLE     The syndapin protein family: linking membrane trafficking with the
            cytoskeleton
  JOURNAL   J Cell Sci 117 (Pt 15), 3077-3086 (2004)
   PUBMED   15226389
  REMARK    Review article
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Mori,S., Tanaka,M., Nanba,D., Nishiwaki,E., Ishiguro,H.,
            Higashiyama,S. and Matsuura,N.
  TITLE     PACSIN3 binds ADAM12/meltrin alpha and up-regulates ectodomain
            shedding of heparin-binding epidermal growth factor-like growth
            factor
  JOURNAL   J Biol Chem 278 (46), 46029-46034 (2003)
   PUBMED   12952982
  REMARK    GeneRIF: PACSIN3 has a novel function as an up-regulator in the
            signaling of proHB-EGF shedding induced by TPA and angiotensin II
REFERENCE   8  (residues 1 to 424)
  AUTHORS   Sumoy,L., Pluvinet,R., Andreu,N., Estivill,X. and Escarceller,M.
  TITLE     PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the
            pacsin-syndapin-FAP52 gene family
  JOURNAL   Gene 262 (1-2), 199-205 (2001)
   PUBMED   11179684
REFERENCE   9  (residues 1 to 424)
  AUTHORS   Modregger,J., Ritter,B., Witter,B., Paulsson,M. and Plomann,M.
  TITLE     All three PACSIN isoforms bind to endocytic proteins and inhibit
            endocytosis
  JOURNAL   J Cell Sci 113 Pt 24, 4511-4521 (2000)
   PUBMED   11082044
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Howard,L., Nelson,K.K., Maciewicz,R.A. and Blobel,C.P.
  TITLE     Interaction of the metalloprotease disintegrins MDC9 and MDC15 with
            two SH3 domain-containing proteins, endophilin I and SH3PX1
  JOURNAL   J Biol Chem 274 (44), 31693-31699 (1999)
   PUBMED   10531379
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC090589.9, AF149825.1 and
            BC007914.2.
            
            Summary: This gene is a member of the protein kinase C and casein
            kinase substrate in neurons family. The encoded protein is involved
            in linking the actin cytoskeleton with vesicle formation.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF149825.1, SRR18074967.1615563.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..424
                     /product="protein kinase C and casein kinase substrate in
                     neurons protein 3"
                     /note="syndapin III; SH3 domain-containing protein 6511"
                     /calculated_mol_wt=48356
     Region          16..273
                     /region_name="BAR"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain, a
                     dimerization module that binds membranes and detects
                     membrane curvature; cl12013"
                     /db_xref="CDD:472257"
     Site            order(25,28..29,33,35..36,39..40,42..43,53..54,56..57,
                     60..61,63..64,67,87,90..91,232,235..236,238,240,243..244,
                     246..247,250..251,254..255,257..258,261..262,264..265)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153365"
     Region          155..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JB8; propagated from
                     UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Region          311..364
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Region          365..420
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(372,374,377,381,400..401,415,417..418)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212930"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKS6.2)"
     CDS             1..424
                     /gene="PACSIN3"
                     /gene_synonym="CMYO27; SDPIII"
                     /coded_by="NM_001184974.2:186..1460"
                     /db_xref="CCDS:CCDS31481.1"
                     /db_xref="GeneID:29763"
                     /db_xref="HGNC:HGNC:8572"
                     /db_xref="MIM:606513"
ORIGIN      
        1 mapeedagge alggsfweag nyrrtvqrve dghrlcgdlv scfqerarie kayaqqladw
       61 arkwrgtvek gpqygtleka whafftaaer lsalhlevre klqgqdserv rawqrgafhr
      121 pvlggfresr aaedgfrkaq kpwlkrlkev easkksyhaa rkdektaqtr eshakadsav
      181 sqeqlrklqe rvercakeae ktkaqyeqtl aelhrytpry medmeqafet cqaaerqrll
      241 ffkdmlltlh qhldlsssek fhelhrdlhq gieaasdeed lrwwrsthgp gmamnwpqfe
      301 ewsldtqrti srkekggrsp devtltsivp trdgtapppq spgspgtgqd eewsdeespr
      361 kaatgvrvra lydyagqead elsfrageel lkmseedeqg wcqgqlqsgr iglypanyve
      421 cvga
//
LOCUS       NP_872272               1015 aa            linear   PRI 21-NOV-2025
DEFINITION  ephrin type-A receptor 5 isoform b [Homo sapiens].
ACCESSION   NP_872272
VERSION     NP_872272.2
DBSOURCE    REFSEQ: accession NM_182472.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1015)
  AUTHORS   Han,X., Liu,T., Zhai,J., Liu,C., Wang,W., Nie,C., Wang,Q., Zhu,X.,
            Zhou,H. and Tian,W.
  TITLE     Association between EPHA5 methylation status in peripheral blood
            leukocytes and the risk and prognosis of gastric cancer
  JOURNAL   PeerJ 10, e13774 (2022)
   PUBMED   36164608
  REMARK    GeneRIF: Association between EPHA5 methylation status in peripheral
            blood leukocytes and the risk and prognosis of gastric cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1015)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   3  (residues 1 to 1015)
  AUTHORS   Liu,C., He,Y., Feng,X., Li,J. and Wang,J.
  TITLE     Expression of EPHA5 in lung adenocarcinoma is associated with lymph
            node metastasis and EGFR mutation
  JOURNAL   APMIS 130 (6), 338-345 (2022)
   PUBMED   35332588
  REMARK    GeneRIF: Expression of EPHA5 in lung adenocarcinoma is associated
            with lymph node metastasis and EGFR mutation.
REFERENCE   4  (residues 1 to 1015)
  AUTHORS   Abouhashem,N., Harb,O., Elwan,A., Zaitoun,M. and Saraya,Y.
  TITLE     Immunohistochemical evaluation of forkhead box A1 and EphA5 markers
            in serous ovarian carcinomas, and their impact on the clinical
            outcome of patients
  JOURNAL   Pol J Pathol 73 (2), 120-133 (2022)
   PUBMED   36345952
  REMARK    GeneRIF: Immunohistochemical evaluation of forkhead box A1 and
            EphA5 markers in serous ovarian carcinomas, and their impact on the
            clinical outcome of patients.
REFERENCE   5  (residues 1 to 1015)
  AUTHORS   Zhou,R.
  TITLE     Regulation of topographic projection by the Eph family receptor Bsk
            (EphA5) and its ligands
  JOURNAL   Cell Tissue Res 290 (2), 251-259 (1997)
   PUBMED   9321686
  REMARK    Review article
REFERENCE   6  (residues 1 to 1015)
  AUTHORS   Miescher,G.C., Taylor,V., Olivieri,G., Mindermann,T., Schrock,E.
            and Steck,A.J.
  TITLE     Extensive splice variation and localization of the EHK-1 receptor
            tyrosine kinase in adult human brain and glial tumors
  JOURNAL   Brain Res Mol Brain Res 46 (1-2), 17-24 (1997)
   PUBMED   9191074
REFERENCE   7  (residues 1 to 1015)
  AUTHORS   Gale,N.W., Holland,S.J., Valenzuela,D.M., Flenniken,A., Pan,L.,
            Ryan,T.E., Henkemeyer,M., Strebhardt,K., Hirai,H., Wilkinson,D.G.,
            Pawson,T., Davis,S. and Yancopoulos,G.D.
  TITLE     Eph receptors and ligands comprise two major specificity subclasses
            and are reciprocally compartmentalized during embryogenesis
  JOURNAL   Neuron 17 (1), 9-19 (1996)
   PUBMED   8755474
REFERENCE   8  (residues 1 to 1015)
  AUTHORS   Winslow,J.W., Moran,P., Valverde,J., Shih,A., Yuan,J.Q., Wong,S.C.,
            Tsai,S.P., Goddard,A., Henzel,W.J., Hefti,F. et al.
  TITLE     Cloning of AL-1, a ligand for an Eph-related tyrosine kinase
            receptor involved in axon bundle formation
  JOURNAL   Neuron 14 (5), 973-981 (1995)
   PUBMED   7748564
REFERENCE   9  (residues 1 to 1015)
  AUTHORS   Fox,G.M., Holst,P.L., Chute,H.T., Lindberg,R.A., Janssen,A.M.,
            Basu,R. and Welcher,A.A.
  TITLE     cDNA cloning and tissue distribution of five human EPH-like
            receptor protein-tyrosine kinases
  JOURNAL   Oncogene 10 (5), 897-905 (1995)
   PUBMED   7898931
REFERENCE   10 (residues 1 to 1015)
  AUTHORS   Spritz,R.A., Strunk,K.M., Lee,S.T., Lu-Kuo,J.M., Ward,D.C., Le
            Paslier,D., Altherr,M.R., Dorman,T.E. and Moir,D.T.
  TITLE     A YAC contig spanning a cluster of human type III receptor protein
            tyrosine kinase genes (PDGFRA-KIT-KDR) in chromosome segment 4q12
  JOURNAL   Genomics 22 (2), 431-436 (1994)
   PUBMED   7528718
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB209375.1, AC104137.5,
            BC136257.1, X95425.1, AC018683.4, L36644.1 and BX537946.1.
            
            On Jan 27, 2009 this sequence version replaced NP_872272.1.
            
            Summary: This gene belongs to the ephrin receptor subfamily of the
            protein-tyrosine kinase family. EPH and EPH-related receptors have
            been implicated in mediating developmental events, particularly in
            the nervous system. Receptors in the EPH subfamily typically have a
            single kinase domain and an extracellular region containing a
            Cys-rich domain and 2 fibronectin type III repeats. The ephrin
            receptors are divided into 2 groups based on the similarity of
            their extracellular domain sequences and their affinities for
            binding ephrin-A and ephrin-B ligands. Alternatively spliced
            transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            and lacks an alternate exon in the coding region compared to
            variant 3. The resulting protein (isoform b) is shorter but has the
            same N- and C-termini compared to isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L36644.1, SRR14038195.653935.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1015
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q13.1-q13.2"
     Protein         1..1015
                     /product="ephrin type-A receptor 5 isoform b"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-A receptor 5; receptor protein-tyrosine
                     kinase HEK7; tyrosine-protein kinase receptor EHK-1;
                     EPH-like kinase 7; EPH homology kinase 1; brain-specific
                     kinase; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=112493
     Region          60..232
                     /region_name="EphR_LBD_A5"
                     /note="Ligand Binding Domain of Ephrin type-A Receptor 5;
                     cd10483"
                     /db_xref="CDD:198451"
     Site            order(84,86..90,97..98,100,102,133,135,140..141,183,
                     187..188,191..193,220..222,224)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198451"
     Region          <355..>583
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          469..559
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(469,532,547)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(548..549,551..552)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          575..650
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Region          648..914
                     /region_name="PTKc_EphR_A"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphA Ephrin Receptors; cd05066"
                     /db_xref="CDD:270651"
     Site            order(659,661..663,667,683,685,731..732,734,778,782..783,
                     785,796,815..819,828,862)
                     /site_type="active"
                     /db_xref="CDD:270651"
     Site            order(659..663,667,683,685,731..734,737..738,782..783,785,
                     796)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270651"
     Site            order(778,782,815..819,828,862)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270651"
     Site            795..821
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270651"
     Region          943..1008
                     /region_name="SAM_EPH-A5"
                     /note="SAM domain of EPH-A5 subfamily of tyrosine kinase
                     receptors; cd09546"
                     /db_xref="CDD:188945"
     Site            order(960,993)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188945"
     CDS             1..1015
                     /gene="EPHA5"
                     /gene_synonym="CEK7; EHK-1; EHK1; EK7; HEK7; TYRO4"
                     /coded_by="NM_182472.5:748..3795"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3514.1"
                     /db_xref="GeneID:2044"
                     /db_xref="HGNC:HGNC:3389"
                     /db_xref="MIM:600004"
ORIGIN      
        1 mrgsgprgag rrrppsgggd tpitpaslag cysaprrapl wtclllcaal rtllaspsne
       61 vnlldsrtvm gdlgwiafpk ngweeigevd enyapihtyq vckvmeqnqn nwlltswisn
      121 egasrifiel kftlrdcnsl pgglgtcket fnmyyfesdd qngrnikenq yikidtiaad
      181 esfteldlgd rvmklntevr dvgplskkgf ylafqdvgac ialvsvrvyy kkcpsvvrhl
      241 avfpdtitga dssqllevsg scvnhsvtde ppkmhcsaeg ewlvpigkcm ckagyeekng
      301 tcqvcrpgff kasphiqscg kcpphsythe eastscvcek dyfrresdpp tmactrppsa
      361 prnaisnvne tsvflewipp adtggrkdvs yyiackkcns hagvceecgg hvrylprqsg
      421 lkntsvmmvd llahtnytfe ieavngvsdl spgarqyvsv nvttnqaaps pvtnvkkgki
      481 aknsislswq epdrpngiil eyeikyfekd qetsytiiks kettitaegl kpasvyvfqi
      541 rartaagygv fsrrfefett pvfaassdqs qipviavsvt vgvillavvi gvllsgrrcg
      601 yskakqdpee ekmhfhnghi klpgvrtyid phtyedpnqa vhefakeiea scitiervig
      661 agefgevcsg rlklpgkrel pvaiktlkvg ytekqrrdfl geasimgqfd hpniihlegv
      721 vtkskpvmiv teymengsld tflkkndgqf tviqlvgmlr gisagmkyls dmgyvhrdla
      781 arnilinsnl vckvsdfgls rvleddpeaa yttrggkipi rwtapeaiaf rkftsasdvw
      841 sygivmwevv sygerpywem tnqdvikave egyrlpspmd cpaalyqlml dcwqkernsr
      901 pkfdeivnml dklirnpssl ktlvnascrv snllaehspl gsgayrsvge wleaikmgry
      961 teifmengys smdavaqvtl edlrrlgvtl vghqkkimns lqemkvqlvn gmvpl
//
LOCUS       NP_001274453             388 aa            linear   PRI 21-NOV-2025
DEFINITION  M-phase inducer phosphatase 2 isoform 9 [Homo sapiens].
ACCESSION   NP_001274453
VERSION     NP_001274453.1
DBSOURCE    REFSEQ: accession NM_001287524.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Pan,X., Xu,C., Cheng,G., Chen,Z., Liu,M. and Mei,Y.
  TITLE     Transcription factor E2F3 activates CDC25B to regulate DNA damage
            and promote mitoxantrone resistance in stomach adenocarcinoma
  JOURNAL   Mol Biol Rep 51 (1), 90 (2024)
   PUBMED   38194158
  REMARK    GeneRIF: Transcription factor E2F3 activates CDC25B to regulate DNA
            damage and promote mitoxantrone resistance in stomach
            adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Li,L.P., Li,H.X., Zhou,H., Li,W.Y., Wang,R.L., Zhang,Y.C. and Ma,Y.
  TITLE     Exploring the mechanism of C473D mutation on CDC25B causing weak
            binding affinity with CDK2/CyclinA by molecular dynamics study
  JOURNAL   J Biomol Struct Dyn 41 (22), 12552-12564 (2023)
   PUBMED   36655391
  REMARK    GeneRIF: Exploring the mechanism of C473D mutation on CDC25B
            causing weak binding affinity with CDK2/CyclinA by molecular
            dynamics study.
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Baldin,V., Cans,C., Superti-Furga,G. and Ducommun,B.
  TITLE     Alternative splicing of the human CDC25B tyrosine phosphatase.
            Possible implications for growth control?
  JOURNAL   Oncogene 14 (20), 2485-2495 (1997)
   PUBMED   9188863
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Conklin,D.S., Galaktionov,K. and Beach,D.
  TITLE     14-3-3 proteins associate with cdc25 phosphatases
  JOURNAL   Proc Natl Acad Sci U S A 92 (17), 7892-7896 (1995)
   PUBMED   7644510
REFERENCE   8  (residues 1 to 388)
  AUTHORS   Galaktionov,K. and Beach,D.
  TITLE     Specific activation of cdc25 tyrosine phosphatases by B-type
            cyclins: evidence for multiple roles of mitotic cyclins
  JOURNAL   Cell 67 (6), 1181-1194 (1991)
   PUBMED   1836978
REFERENCE   9  (residues 1 to 388)
  AUTHORS   Nagata,A., Igarashi,M., Jinno,S., Suto,K. and Okayama,H.
  TITLE     An additional homolog of the fission yeast cdc25+ gene occurs in
            humans and is highly expressed in some cancer cells
  JOURNAL   New Biol 3 (10), 959-968 (1991)
   PUBMED   1662986
REFERENCE   10 (residues 1 to 388)
  AUTHORS   Strausfeld,U., Labbe,J.C., Fesquet,D., Cavadore,J.C., Picard,A.,
            Sadhu,K., Russell,P. and Doree,M.
  TITLE     Dephosphorylation and activation of a p34cdc2/cyclin B complex in
            vitro by human CDC25 protein
  JOURNAL   Nature 351 (6323), 242-245 (1991)
   PUBMED   1828290
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109804.41, DA065196.1,
            BX640836.1, BC051711.1 and DA107932.1.
            
            Summary: CDC25B is a member of the CDC25 family of phosphatases.
            CDC25B activates the cyclin dependent kinase CDC2 by removing two
            phosphate groups and it is required for entry into mitosis. CDC25B
            shuttles between the nucleus and the cytoplasm due to nuclear
            localization and nuclear export signals. The protein is nuclear in
            the M and G1 phases of the cell cycle and moves to the cytoplasm
            during S and G2. CDC25B has oncogenic properties, although its role
            in tumor formation has not been determined. Multiple transcript
            variants for this gene exist. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (10) differs in the 5' UTR and has
            multiple coding region differences, compared to variant 1, which
            causes translation initiation at a downstream start codon. The
            resulting protein (isoform 9) has a shorter N-terminus and lacks an
            internal region compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX640836.1, SRR14372080.578497.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..388
                     /product="M-phase inducer phosphatase 2 isoform 9"
                     /EC_number="3.1.3.48"
                     /note="M-phase inducer phosphatase 2; dual specificity
                     phosphatase Cdc25B; CDC25 homolog B"
                     /calculated_mol_wt=44824
     Region          <1..191
                     /region_name="M-inducer_phosp"
                     /note="M-phase inducer phosphatase; pfam06617"
                     /db_xref="CDD:461962"
     Region          220..339
                     /region_name="Cdc25"
                     /note="Cdc25 phosphatases are members of the Rhodanese
                     Homology Domain superfamily. They activate the cell
                     division kinases throughout the cell cycle progression.
                     Cdc25 phosphatases dephosphorylate phosphotyrosine and
                     phosphothreonine residues, in order to...; cd01530"
                     /db_xref="CDD:238788"
     Site            295..301
                     /site_type="active"
                     /note="oxyanion binding site [active]"
                     /db_xref="CDD:238788"
     Site            295
                     /site_type="active"
                     /note="active site residue [active]"
                     /db_xref="CDD:238788"
     CDS             1..388
                     /gene="CDC25B"
                     /gene_synonym="MPIP2"
                     /coded_by="NM_001287524.2:314..1480"
                     /note="isoform 9 is encoded by transcript variant 10"
                     /db_xref="GeneID:994"
                     /db_xref="HGNC:HGNC:1726"
                     /db_xref="MIM:116949"
ORIGIN      
        1 mpdgfvfkmp wkpthpssth alaewasrre afaqrpssap dlmclspdrk meveelspla
       61 lgrfsltpae gdteeddgfv dilesdlkdd davppgmesl isaplvktle keeekdlvmy
      121 skcqrlfrsp smpcsvirpi lkrlerpqdr dtpvqnkrrr svtppeeqqe aeepkarvlr
      181 skslchdeie nlldsdhrel igdyskafll qtvdgkhqdl kyispetmva lltgkfsniv
      241 dkfvivdcry pyeyegghik tavnlplerd aesfllkspi apcsldkrvi lifhcefsse
      301 rgprmcrfir erdravndyp slyypemyil kggykeffpq hpnfcepqdy rpmnheafkd
      361 elktfrlktr swagersrre lcsrlqdq
//
LOCUS       NP_001005505            1145 aa            linear   PRI 21-NOV-2025
DEFINITION  voltage-dependent calcium channel subunit alpha-2/delta-2 isoform a
            precursor [Homo sapiens].
ACCESSION   NP_001005505
VERSION     NP_001005505.1
DBSOURCE    REFSEQ: accession NM_001005505.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1145)
  AUTHORS   Westhoff,M. and Dixon,R.E.
  TITLE     Mechanisms and Regulation of Cardiac CaV1.2 Trafficking
  JOURNAL   Int J Mol Sci 22 (11), 5927 (2021)
   PUBMED   34072954
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1145)
  AUTHORS   Dolphin,A.C.
  TITLE     Voltage-gated calcium channels and their auxiliary subunits:
            physiology and pathophysiology and pharmacology
  JOURNAL   J Physiol 594 (19), 5369-5390 (2016)
   PUBMED   27273705
  REMARK    Review article
REFERENCE   3  (residues 1 to 1145)
  AUTHORS   Warnier,M., Roudbaraki,M., Derouiche,S., Delcourt,P., Bokhobza,A.,
            Prevarskaya,N. and Mariot,P.
  TITLE     CACNA2D2 promotes tumorigenesis by stimulating cell proliferation
            and angiogenesis
  JOURNAL   Oncogene 34 (42), 5383-5394 (2015)
   PUBMED   25619833
  REMARK    GeneRIF: show that the action of alpha2delta2 on tumor development
            occurs not only through a stimulation of proliferation
REFERENCE   4  (residues 1 to 1145)
  AUTHORS   Pippucci,T., Parmeggiani,A., Palombo,F., Maresca,A., Angius,A.,
            Crisponi,L., Cucca,F., Liguori,R., Valentino,M.L., Seri,M. and
            Carelli,V.
  TITLE     A novel null homozygous mutation confirms CACNA2D2 as a gene
            mutated in epileptic encephalopathy
  JOURNAL   PLoS One 8 (12), e82154 (2013)
   PUBMED   24358150
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1145)
  AUTHORS   Rhodin,A., Gronbladh,A., Ginya,H., Nilsson,K.W., Rosenblad,A.,
            Zhou,Q., Enlund,M., Hallberg,M., Gordh,T. and Nyberg,F.
  TITLE     Combined analysis of circulating beta-endorphin with gene
            polymorphisms in OPRM1, CACNAD2 and ABCB1 reveals correlation with
            pain, opioid sensitivity and opioid-related side effects
  JOURNAL   Mol Brain 6, 8 (2013)
   PUBMED   23402298
  REMARK    GeneRIF: The investigation of single nucleotide polymorphisms in
            three genes that have a functional impact on the opioid response:
            OPRM1, ABCB1 and the calcium channel complex subunit CACNA2D2, is
            reported.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1145)
  AUTHORS   Edvardson,S., Oz,S., Abulhijaa,F.A., Taher,F.B., Shaag,A.,
            Zenvirt,S., Dascal,N. and Elpeleg,O.
  TITLE     Early infantile epileptic encephalopathy associated with a high
            voltage gated calcium channelopathy
  JOURNAL   J Med Genet 50 (2), 118-123 (2013)
   PUBMED   23339110
REFERENCE   7  (residues 1 to 1145)
  AUTHORS   Angeloni,D., Duh,F.M., Wei,M.F., Johnson,B.E. and Lerman,M.I.
  TITLE     A G-to-A single nucleotide polymorphism in intron 2 of the human
            CACNA2D2 gene that maps at 3p21.3
  JOURNAL   Mol Cell Probes 15 (2), 125-127 (2001)
   PUBMED   11292331
REFERENCE   8  (residues 1 to 1145)
  AUTHORS   Lerman,M.I. and Minna,J.D.
  TITLE     The 630-kb lung cancer homozygous deletion region on human
            chromosome 3p21.3: identification and evaluation of the resident
            candidate tumor suppressor genes. The International Lung Cancer
            Chromosome 3p21.3 Tumor Suppressor Gene Consortium
  JOURNAL   Cancer Res 60 (21), 6116-6133 (2000)
   PUBMED   11085536
REFERENCE   9  (residues 1 to 1145)
  AUTHORS   Gao,B., Sekido,Y., Maximov,A., Saad,M., Forgacs,E., Latif,F.,
            Wei,M.H., Lerman,M., Lee,J.H., Perez-Reyes,E., Bezprozvanny,I. and
            Minna,J.D.
  TITLE     Functional properties of a new voltage-dependent calcium channel
            alpha(2)delta auxiliary subunit gene (CACNA2D2)
  JOURNAL   J Biol Chem 275 (16), 12237-12242 (2000)
   PUBMED   10766861
REFERENCE   10 (residues 1 to 1145)
  AUTHORS   Hobom,M., Dai,S., Marais,E., Lacinova,L., Hofmann,F. and
            Klugbauer,N.
  TITLE     Neuronal distribution and functional characterization of the
            calcium channel alpha2delta-2 subunit
  JOURNAL   Eur J Neurosci 12 (4), 1217-1226 (2000)
   PUBMED   10762351
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL450422.2, AF040709.1,
            Z84492.2 and BF373910.1.
            
            Summary: Calcium channels mediate the entry of calcium ions into
            the cell upon membrane polarization. This gene encodes the
            alpha-2/delta subunit of the voltage-dependent calcium channel
            complex. The complex consists of the main channel-forming subunit
            alpha-1, and auxiliary subunits alpha-2/delta, beta, and gamma. The
            auxiliary subunits function in the assembly and membrane
            localization of the complex, and modulate calcium currents and
            channel activation/inactivation kinetics. The subunit encoded by
            this gene undergoes post-translational cleavage to yield the
            extracellular alpha2 peptide and a membrane-anchored delta
            polypeptide. This subunit is a receptor for the antiepileptic drug,
            gabapentin. Mutations in this gene are associated with early
            infantile epileptic encephalopathy. Single nucleotide polymorphisms
            in this gene are correlated with increased sensitivity to opioid
            drugs. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Mar 2014].
            
            Transcript Variant: This variant (1) lacks an alternate in-frame
            exon in the central coding region and uses an alternate in-frame
            splice site in the 3' coding region compared to variant 3. The
            encoded isoform (a) is shorter than isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF040709.1, BC152438.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1145
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1145
                     /product="voltage-dependent calcium channel subunit
                     alpha-2/delta-2 isoform a precursor"
                     /note="gene 26; alpha 2 delta calcium channel subunit;
                     voltage-gated calcium channel subunit alpha-2/delta-2;
                     calcium channel, voltage-dependent, alpha 2/delta subunit
                     2; alpha2delta-2"
                     /calculated_mol_wt=127489
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NY47.2)"
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NY47.2)"
                     /calculated_mol_wt=1799
     mat_peptide     19..1145
                     /product="voltage-dependent calcium channel subunit
                     alpha-2/delta-2 isoform a"
                     /calculated_mol_wt=127489
     mat_peptide     19..994
                     /product="voltage-dependent calcium channel subunit
                     alpha-2/delta-2 isoform a"
                     /exception="alternative processing"
                     /calculated_mol_wt=110786
     Region          141..265
                     /region_name="VWA_N"
                     /note="VWA N-terminal; pfam08399"
                     /db_xref="CDD:462464"
     Region          277..456
                     /region_name="vWA_VGCC_like"
                     /note="VWA Voltage gated Calcium channel like:
                     Voltage-gated calcium channels are a complex of five
                     proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The
                     alpha 2 and delta subunits result from proteolytic
                     processing of a single gene product and carries at...;
                     cd01463"
                     /db_xref="CDD:238740"
     Site            order(297,299,301,369,401)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238740"
     Region          297..301
                     /region_name="MIDAS-like motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NY47.2)"
     Site            386
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q9NY47.2)"
     Site            418
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NY47.2)"
     Region          <448..531
                     /region_name="HK_sensor"
                     /note="Sensor domains of Histidine Kinase receptors;
                     cl38916"
                     /db_xref="CDD:365792"
     Site            507
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NY47.2)"
     Region          533..642
                     /region_name="HK_sensor"
                     /note="Sensor domains of Histidine Kinase receptors;
                     cl38916"
                     /db_xref="CDD:365792"
     Site            540
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NY47.2)"
     Site            624
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NY47.2)"
     Region          662..1106
                     /region_name="VGCC_alpha2"
                     /note="Neuronal voltage-dependent calcium channel alpha
                     2acd; pfam08473"
                     /db_xref="CDD:462488"
     Site            854
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NY47.2)"
     mat_peptide     995..1145
                     /product="voltage-dependent calcium channel subunit
                     alpha-2/delta-2 isoform a"
                     /exception="alternative processing"
                     /calculated_mol_wt=16721
     Site            1109..1129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NY47.2)"
     CDS             1..1145
                     /gene="CACNA2D2"
                     /gene_synonym="CACNA2D; CASVDD"
                     /coded_by="NM_001005505.3:212..3649"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS63647.1"
                     /db_xref="GeneID:9254"
                     /db_xref="HGNC:HGNC:1400"
                     /db_xref="MIM:607082"
ORIGIN      
        1 mavpartcga srpgpartar pwpgcgphpg pgtrrptsgp prplwlllpl lpllaapgas
       61 aysfpqqhtm qhwarrleqe vdgvmrifgg vqqlreiykd nrnlfevqen epqklvekva
      121 gdieslldrk vqalkrlada aenfqkahrw qdnikeediv yydakadael ddpesedver
      181 gskastlrld fiedpnfknk vnysyaavqi ptdiykgstv ilnelnwtea lenvfmenrr
      241 qdptllwqvf gsatgvtryy patpwrapkk idlydvrrrp wyiqgasspk dmviivdvsg
      301 svsgltlklm ktsvcemldt lsdddyvnva sfnekaqpvs cfthlvqanv rnkkvfkeav
      361 qgmvakgttg ykagfeyafd qlqnsnitra ncnkmimmft dggedrvqdv fekynwpnrt
      421 vrvftfsvgq hnydvtplqw macankgyyf eipsigairi ntqeyldvlg rpmvlagkea
      481 kqvqwtnvye dalglglvvt gtlpvfnltq dgpgekknql ilgvmgidva lndikrltpn
      541 ytlgangyvf aidlngyvll hpnlkpqttn frepvtldfl daeledenke eirrsmidgn
      601 kghkqirtlv kslderyide vtrnytwvpi rstnyslglv lppystfylq anlsdqilqv
      661 kyfefllpss feseghvfia preyckdlna sdnnteflkn fielmekvtp dskqcnnfll
      721 hnlildtgit qqlvervwrd qdlntyslla vfaatdggit rvfpnkaaed wtenpepfna
      781 sfyrrsldnh gyvfkpphqd allrplelen dtvgilvsta velslgrrtl rpavvgvkld
      841 leawaekfkv lasnrthqdq pqkcgpnshc emdcevnned llcvliddgg flvlsnqnhq
      901 wdqvgrffse vdanlmlaly nnsfytrkes ydyqaacapq ppgnlgaapr gvfvptvadf
      961 lnlawwtsaa awslfqqlly gliyhswfqa dpaeaegspe tresscvmkq tqyyfgsvna
     1021 synaiidcgn csrlfhaqrl tntnllfvva ekplcsqcea grllqkethc padgpeqcel
     1081 vqrpryrrgp hicfdynate dtsdcgrgas fppslgvlvs lqlllllglp prpqpqvlvh
     1141 asrrl
//
LOCUS       NP_001373875             584 aa            linear   PRI 21-NOV-2025
DEFINITION  solute carrier organic anion transporter family member 1A2 isoform
            7 [Homo sapiens].
ACCESSION   NP_001373875
VERSION     NP_001373875.1
DBSOURCE    REFSEQ: accession NM_001386946.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Flogel,S., Tust,M., Boussettaoui,S., Fischer,D. and Grundemann,D.
  TITLE     Enhancing transporter activity in heterologous expression systems
            with SAHA: a 2500-times more potent and odorless alternative to
            butyrate
  JOURNAL   FEBS Open Bio 15 (6), 906-913 (2025)
   PUBMED   40052353
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Kataoka,H., Akiyoshi,T., Uchida,Y., Imaoka,A., Terasaki,T. and
            Ohtani,H.
  TITLE     The Effects of N-Glycosylation on the Expression and Transport
            Activity of OATP1A2 and OATP2B1
  JOURNAL   J Pharm Sci 113 (5), 1376-1384 (2024)
   PUBMED   38432624
  REMARK    GeneRIF: The Effects of N-Glycosylation on the Expression and
            Transport Activity of OATP1A2 and OATP2B1.
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Han,H., Akiyoshi,T., Morita,T., Kataoka,H., Katayama,K., Yajima,K.,
            Imaoka,A. and Ohtani,H.
  TITLE     Comparison of the transport kinetics of fexofenadine and its pH
            dependency among OATP1A2 genetic variants
  JOURNAL   Drug Metab Pharmacokinet 47, 100470 (2022)
   PUBMED   36116173
  REMARK    GeneRIF: Comparison of the transport kinetics of fexofenadine and
            its pH dependency among OATP1A2 genetic variants.
REFERENCE   4  (residues 1 to 584)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 584)
  AUTHORS   Hau,R.K., Klein,R.R., Wright,S.H. and Cherrington,N.J.
  TITLE     Localization of Xenobiotic Transporters Expressed at the Human
            Blood-Testis Barrier
  JOURNAL   Drug Metab Dispos 50 (6), 770-780 (2022)
   PUBMED   35307651
REFERENCE   6  (residues 1 to 584)
  AUTHORS   Kullak-Ublick,G.A., Fisch,T., Oswald,M., Hagenbuch,B., Meier,P.J.,
            Beuers,U. and Paumgartner,G.
  TITLE     Dehydroepiandrosterone sulfate (DHEAS): identification of a carrier
            protein in human liver and brain
  JOURNAL   FEBS Lett 424 (3), 173-176 (1998)
   PUBMED   9539145
REFERENCE   7  (residues 1 to 584)
  AUTHORS   Meier,P.J., Eckhardt,U., Schroeder,A., Hagenbuch,B. and Stieger,B.
  TITLE     Substrate specificity of sinusoidal bile acid and organic anion
            uptake systems in rat and human liver
  JOURNAL   Hepatology 26 (6), 1667-1677 (1997)
   PUBMED   9398014
  REMARK    Review article
REFERENCE   8  (residues 1 to 584)
  AUTHORS   Kullak-Ublick,G.A., Beuers,U., Fahney,C., Hagenbuch,B., Meier,P.J.
            and Paumgartner,G.
  TITLE     Identification and functional characterization of the promoter
            region of the human organic anion transporting polypeptide gene
  JOURNAL   Hepatology 26 (4), 991-997 (1997)
   PUBMED   9328325
REFERENCE   9  (residues 1 to 584)
  AUTHORS   Kullak-Ublick,G.A., Beuers,U., Meier,P.J., Domdey,H. and
            Paumgartner,G.
  TITLE     Assignment of the human organic anion transporting polypeptide
            (OATP) gene to chromosome 12p12 by fluorescence in situ
            hybridization
  JOURNAL   J Hepatol 25 (6), 985-987 (1996)
   PUBMED   9007731
REFERENCE   10 (residues 1 to 584)
  AUTHORS   Kullak-Ublick,G.A., Hagenbuch,B., Stieger,B., Schteingart,C.D.,
            Hofmann,A.F., Wolkoff,A.W. and Meier,P.J.
  TITLE     Molecular and functional characterization of an organic anion
            transporting polypeptide cloned from human liver
  JOURNAL   Gastroenterology 109 (4), 1274-1282 (1995)
   PUBMED   7557095
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022224.22.
            
            Summary: This gene encodes a sodium-independent transporter which
            mediates cellular uptake of organic ions in the liver. Its
            substrates include bile acids, bromosulphophthalein, and some
            steroidal compounds. The protein is a member of the SLC21A family
            of solute carriers. Alternative splicing of this gene results in
            multiple transcript variants. [provided by RefSeq, Dec 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.38276.1,
                                           SRR1660809.170760.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..584
                     /product="solute carrier organic anion transporter family
                     member 1A2 isoform 7"
                     /note="organic anion transporting polypeptide A; solute
                     carrier family 21 (organic anion transporter), member 3;
                     sodium-independent organic anion transporter; OATP-1;
                     solute carrier family 21 member 3; organic
                     anion-transporting polypeptide 1"
                     /calculated_mol_wt=64325
     Region          1..518
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     Site            order(13..14,17..18,21,53,152..153,155..157,160,180,
                     183..184,187,305,308..309,312..314,317,346,350,391..392,
                     396,400,461,464..465,468..469,472)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341016"
     CDS             1..584
                     /gene="SLCO1A2"
                     /gene_synonym="OATP; OATP-A; OATP1A2; SLC21A3"
                     /coded_by="NM_001386946.1:167..1921"
                     /note="isoform 7 is encoded by transcript variant 26"
                     /db_xref="GeneID:6579"
                     /db_xref="HGNC:HGNC:10956"
                     /db_xref="MIM:602883"
ORIGIN      
        1 mfllaitcaf vsktlsgsym nsmltqierq fniptslvgf ingsfeignl lliifvsyfg
       61 tklhrpimig igcvvmglgc flkslphflm nqyeyestvs vsgnlssnsf lcmengtqil
      121 rptqdpsect kevkslmwvy vlvgnivrgm getpilplgi syiedfakfe nsplyiglve
      181 tgaiigplig lllasfcanv yvdtgfvntd dliitptdtr wvgawwfgfl icagvnvlta
      241 ipffflpntl pkegletnad iiknenedkq keevkkekyg itkdflpfmk slscnpiyml
      301 filvsviqfn afvnmisfmp kyleqqygis ssdaiflmgi ynlppicigy iigglimkkf
      361 kitvkqaahi gcwlslleyl lyflsflmtc enssvvgint syegipqdly vendifadcn
      421 vdcncpskiw dpvcgnngls ylsaclagce tsigtginmv fqncsciqts gnssavlglc
      481 dkgpdcslml qyflilsams sfiyslaaip gymvllrcmk seekslgvgl htfctrvfag
      541 ipapiyfgal mdstclhwgt lkcgesgacr iydsttfrls fypa
//
LOCUS       NP_001333263             508 aa            linear   PRI 21-NOV-2025
DEFINITION  autophagy-related protein 13 isoform d [Homo sapiens].
ACCESSION   NP_001333263 XP_016874097
VERSION     NP_001333263.1
DBSOURCE    REFSEQ: accession NM_001346334.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Patel,A. and Faesen,A.C.
  TITLE     Metamorphosis by ATG13 and ATG101 in human autophagy initiation
  JOURNAL   Autophagy 20 (4), 968-969 (2024)
   PUBMED   37394799
  REMARK    GeneRIF: Metamorphosis by ATG13 and ATG101 in human autophagy
            initiation.
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Nguyen,A. and Faesen,A.C.
  TITLE     The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis
  JOURNAL   FEBS Lett 598 (1), 114-126 (2024)
   PUBMED   37567770
  REMARK    GeneRIF: The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis.
            Review article
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Karabi,Z., Moradian,F. and Kheirabadi,M.
  TITLE     The effect of lactoferrin on ULK1 and ATG13 genes expression in
            breast cancer cell line MCF7 and bioinformatics studies of protein
            interaction between lactoferrin and the autophagy initiation
            complex
  JOURNAL   Cell Biochem Biophys 80 (4), 795-806 (2022)
   PUBMED   36169801
  REMARK    GeneRIF: The effect of lactoferrin on ULK1 and ATG13 genes
            expression in breast cancer cell line MCF7 and bioinformatics
            studies of protein interaction between lactoferrin and the
            autophagy initiation complex.
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Gottschalk,G., Peterson,D., Knox,K., Maynard,M., Whelan,R.J. and
            Roy,A.
  TITLE     Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE)
  JOURNAL   Mol Cell Neurosci 120, 103731 (2022)
   PUBMED   35487443
  REMARK    GeneRIF: Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE).
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Jung,C.H., Jun,C.B., Ro,S.H., Kim,Y.M., Otto,N.M., Cao,J., Kundu,M.
            and Kim,D.H.
  TITLE     ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy
            machinery
  JOURNAL   Mol Biol Cell 20 (7), 1992-2003 (2009)
   PUBMED   19225151
  REMARK    GeneRIF: The ULK-Atg13-FIP200 complexes are direct targets of mTOR
            and important regulators of autophagy in response to mTOR
            signaling.
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Hosokawa,N., Hara,T., Kaizuka,T., Kishi,C., Takamura,A., Miura,Y.,
            Iemura,S., Natsume,T., Takehana,K., Yamada,N., Guan,J.L., Oshiro,N.
            and Mizushima,N.
  TITLE     Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200
            complex required for autophagy
  JOURNAL   Mol Biol Cell 20 (7), 1981-1991 (2009)
   PUBMED   19211835
  REMARK    GeneRIF: mTORC1 suppresses autophagy through direct regulation of
            the approximately 3-MDa ULK1-Atg13-FIP200 complex.
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Chan,E.Y., Longatti,A., McKnight,N.C. and Tooze,S.A.
  TITLE     Kinase-inactivated ULK proteins inhibit autophagy via their
            conserved C-terminal domains using an Atg13-independent mechanism
  JOURNAL   Mol Cell Biol 29 (1), 157-171 (2009)
   PUBMED   18936157
  REMARK    GeneRIF: The functions of ULK1 and ULK2 are controlled by
            autophosphorylation and conformational changes involving exposure
            of the C-terminal domain and interaction with the putative human
            homologue of Atg13.
            GeneRIF: The gene product is the functional homologue of yeast
            Atg13, and required for autophagy in mammalian cells.
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Meijer,W.H., van der Klei,I.J., Veenhuis,M. and Kiel,J.A.
  TITLE     ATG genes involved in non-selective autophagy are conserved from
            yeast to man, but the selective Cvt and pexophagy pathways also
            require organism-specific genes
  JOURNAL   Autophagy 3 (2), 106-116 (2007)
   PUBMED   17204848
REFERENCE   10 (residues 1 to 508)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC127035.6 and AC115088.6.
            
            On Oct 9, 2016 this sequence version replaced XP_016874097.1.
            
            Summary: The protein encoded by this gene is an autophagy factor
            and a target of the TOR kinase signaling pathway. The encoded
            protein is essential for autophagosome formation and mitophagy.
            [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (30), as well as variants 29 and
            31-33, encodes isoform d.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.60996.1,
                                           SRR18074969.3081205.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..508
                     /product="autophagy-related protein 13 isoform d"
                     /note="autophagy-related protein 13; ATG13 autophagy
                     related 13 homolog"
                     /calculated_mol_wt=55419
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O75143.1)"
     Region          19..192
                     /region_name="ATG13"
                     /note="Autophagy-related protein 13; pfam10033"
                     /db_xref="CDD:431003"
     Region          127..134
                     /region_name="Important for interaction with ATG101.
                     /evidence=ECO:0000269|PubMed:26299944"
                     /note="propagated from UniProtKB/Swiss-Prot (O75143.1)"
     Region          296..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75143.1)"
     Region          323..352
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75143.1)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ULK1.
                     /evidence=ECO:0000269|PubMed:21855797,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75143.1)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75143.1)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75143.1)"
     Region          396..430
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75143.1)"
     Region          435..438
                     /region_name="LIR. /evidence=ECO:0000305|PubMed:24290141"
                     /note="propagated from UniProtKB/Swiss-Prot (O75143.1)"
     CDS             1..508
                     /gene="ATG13"
                     /gene_synonym="KIAA0652; PARATARG8"
                     /coded_by="NM_001346334.2:408..1934"
                     /note="isoform d is encoded by transcript variant 30"
                     /db_xref="GeneID:9776"
                     /db_xref="HGNC:HGNC:29091"
                     /db_xref="MIM:615088"
ORIGIN      
        1 metdlnsqdr kdldkfikff alktvqvivq arlgekictr ssssptgsdw fnlaikdipe
       61 vtheakkala gqlpavgrsm cveislktse gdsmeleiwc lemnekcdke ikvsytvynr
      121 lslllkslla itrvtpayrl srkqgheyvi lyriyfgevq lsglgegfqt vrvgtvgtpv
      181 gtitlscayr inlafmstrq fertppimgi iidhfvdrpy pssspmhpcn yrtagedtgv
      241 iypsvedsqe vcttsfstsp psqpaalgvg sadlaypvvf aaglnathph qlmvpgkegg
      301 vplapnqpvh gtqadqerla tctpsdrthc aatpsssedt etvsnssegr asphdvleti
      361 fvrkvgafvn kpinqvtlts ldipfamfap knleledtdp mvnppdspet esplqgslhs
      421 dgssggssgn thddfvmidf kpafskddil pmdlgtfyre fqnppqlssl sidigaqsma
      481 edldslpekl avheknvref dafvetlq
//
LOCUS       NP_006700               1210 aa            linear   PRI 21-NOV-2025
DEFINITION  histone-lysine N-methyltransferase EHMT2 isoform a [Homo sapiens].
ACCESSION   NP_006700
VERSION     NP_006700.3
DBSOURCE    REFSEQ: accession NM_006709.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1210)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1210)
  AUTHORS   Sun,L., Liu,R., Wu,Z.J., Liu,Z.Y., Wan,A.H., Yan,S., Liu,C.,
            Liang,H., Xiao,M., You,N., Lou,Y., Deng,Y., Bu,X., Chen,D.,
            Huang,J., Zhang,X., Kuang,D.M. and Wan,G.
  TITLE     Galectin-7 Induction by EHMT2 Inhibition Enhances Immunity in
            Microsatellite Stability Colorectal Cancer
  JOURNAL   Gastroenterology 166 (3), 466-482 (2024)
   PUBMED   38065340
  REMARK    GeneRIF: Galectin-7 Induction by EHMT2 Inhibition Enhances Immunity
            in Microsatellite Stability Colorectal Cancer.
REFERENCE   3  (residues 1 to 1210)
  AUTHORS   Muneer,A., Wang,L., Xie,L., Zhang,F., Wu,B., Mei,L., Lenarcic,E.M.,
            Feng,E.H., Song,J., Xiong,Y., Yu,X., Wang,C., Jain,K., Strahl,B.D.,
            Cook,J.G., Wan,Y.Y., Moorman,N.J., Song,H., Jin,J. and Chen,X.
  TITLE     Non-canonical function of histone methyltransferase G9a in the
            translational regulation of chronic inflammation
  JOURNAL   Cell Chem Biol 30 (12), 1525-1541 (2023)
   PUBMED   37858336
  REMARK    GeneRIF: Non-canonical function of histone methyltransferase G9a in
            the translational regulation of chronic inflammation.
REFERENCE   4  (residues 1 to 1210)
  AUTHORS   Souza,B.K., Freire,N.H., Monteiro,T.S., Herlinger,A.L., Jaeger,M.,
            Dalmolin,M.G.S., de Farias,C.B., Gregianin,L., Brunetto,A.T.,
            Brunetto,A.L., Thiele,C.J. and Roesler,R.
  TITLE     Histone Methyltransferases G9a/Ehmt2 and GLP/Ehmt1 Are Associated
            with Cell Viability and Poorer Prognosis in Neuroblastoma and Ewing
            Sarcoma
  JOURNAL   Int J Mol Sci 24 (20), 15242 (2023)
   PUBMED   37894922
  REMARK    GeneRIF: Histone Methyltransferases G9a/Ehmt2 and GLP/Ehmt1 Are
            Associated with Cell Viability and Poorer Prognosis in
            Neuroblastoma and Ewing Sarcoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1210)
  AUTHORS   Fang,Z., Wang,Y., Huang,B., Chen,X., Jiang,R. and Yin,M.
  TITLE     Depletion of G9A attenuates imiquimod-induced psoriatic dermatitis
            via targeting EDAR-NF-kappaB signaling in keratinocyte
  JOURNAL   Cell Death Dis 14 (9), 627 (2023)
   PUBMED   37739945
  REMARK    GeneRIF: Depletion of G9A attenuates imiquimod-induced psoriatic
            dermatitis via targeting EDAR-NF-kappaB signaling in keratinocyte.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1210)
  AUTHORS   Ogawa,H., Ishiguro,K., Gaubatz,S., Livingston,D.M. and Nakatani,Y.
  TITLE     A complex with chromatin modifiers that occupies E2F- and
            Myc-responsive genes in G0 cells
  JOURNAL   Science 296 (5570), 1132-1136 (2002)
   PUBMED   12004135
REFERENCE   7  (residues 1 to 1210)
  AUTHORS   Brown,S.E., Campbell,R.D. and Sanderson,C.M.
  TITLE     Novel NG36/G9a gene products encoded within the human and mouse MHC
            class III regions
  JOURNAL   Mamm Genome 12 (12), 916-924 (2001)
   PUBMED   11707778
REFERENCE   8  (residues 1 to 1210)
  AUTHORS   Tachibana,M., Sugimoto,K., Fukushima,T. and Shinkai,Y.
  TITLE     Set domain-containing protein, G9a, is a novel lysine-preferring
            mammalian histone methyltransferase with hyperactivity and specific
            selectivity to lysines 9 and 27 of histone H3
  JOURNAL   J Biol Chem 276 (27), 25309-25317 (2001)
   PUBMED   11316813
REFERENCE   9  (residues 1 to 1210)
  AUTHORS   Milner,C.M. and Campbell,R.D.
  TITLE     The G9a gene in the human major histocompatibility complex encodes
            a novel protein containing ankyrin-like repeats
  JOURNAL   Biochem J 290 (Pt 3) (Pt 3), 811-818 (1993)
   PUBMED   8457211
  REMARK    Erratum:[Biochem J 1993 Jun 15;292(Pt 3):952]
REFERENCE   10 (residues 1 to 1210)
  AUTHORS   Spies,T., Bresnahan,M. and Strominger,J.L.
  TITLE     Human major histocompatibility complex contains a minimum of 19
            genes between the complement cluster and HLA-B
  JOURNAL   Proc Natl Acad Sci U S A 86 (22), 8955-8958 (1989)
   PUBMED   2813433
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY067184.1, BC009351.1,
            CN397400.1 and X69838.1.
            
            On Aug 21, 2007 this sequence version replaced NP_006700.2.
            
            Summary: This gene encodes a methyltransferase that methylates
            lysine residues of histone H3. Methylation of H3 at lysine 9 by
            this protein results in recruitment of additional epigenetic
            regulators and repression of transcription. This gene was initially
            thought to be two different genes, NG36 and G9a, adjacent to each
            other in the HLA locus. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2, also known as NG36/G9a) uses
            an alternate 5' UTR and 5' coding region, contains an alternate
            in-frame exon in the 5' coding region, and lacks an alternate
            in-frame exon compared to variant 3. It encodes isoform a, which is
            shorter and has a distinct N-terminus, compared to isoform c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC009351.1, AJ315532.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375537.9/ ENSP00000364687.4
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..1210
                     /product="histone-lysine N-methyltransferase EHMT2 isoform
                     a"
                     /EC_number="2.1.1.367"
                     /note="G9A histone methyltransferase; ankyrin
                     repeat-containing protein; HLA-B associated transcript 8;
                     histone H3-K9 methyltransferase 3; euchromatic
                     histone-lysine N-methyltransferase 2; H3-K9-HMTase 3;
                     lysine N-methyltransferase 1C; histone-lysine
                     N-methyltransferase, H3 lysine-9 specific 3;
                     histone-lysine N-methyltransferase EHMT2"
                     /calculated_mol_wt=132240
     Region          1..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Region          <42..204
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            185
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, by EHMT2, alternate.
                     /evidence=ECO:0000269|PubMed:18438403;
                     N6,N6-dimethyllysine, by EHMT2, alternate.
                     /evidence=ECO:0000269|PubMed:18438403; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Region          <218..326
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Region          280..386
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z148; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Region          420..549
                     /region_name="EHMT_ZBD"
                     /note="Zinc-binding domain of euchromatic histone lysine
                     methyltransferases EHMT1 and EHTM2; cd20905"
                     /db_xref="CDD:411018"
     Region          548..608
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            555
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            569
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Region          628..887
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          649..678
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Region          684..713
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Region          686..715
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          717..746
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Region          750..782
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          750..780
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Region          784..813
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Region          785..815
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(786,790..791,794..796,798..799,803,806,815,817,819,
                     823..824,827..829,831..832,836,839,848,850,852,856..857,
                     860..862,864..865,869,872,881)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          817..848
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          817..846
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Region          817..819
                     /region_name="Histone H3K9me binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Region          850..881
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          850..879
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Region          948..1186
                     /region_name="SET_EHMT2"
                     /note="SET domain (including pre-SET and post-SET domains)
                     found in euchromatic histone-lysine N-methyltransferase 2
                     (EHMT2) and similar proteins; cd10533"
                     /db_xref="CDD:380931"
     Site            order(1048..1050,1074,1077..1078,1080,1083..1088,1091,
                     1109..1113,1121,1123,1153..1154,1157..1158,1161..1162,
                     1166..1169)
                     /site_type="active"
                     /db_xref="CDD:380931"
     Site            order(1048..1050,1084..1085,1109..1113,1154)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380931"
     Site            1067
                     /site_type="other"
                     /note="Histone H3K9me binding. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            order(1074,1077..1078,1080,1083,1086,1088,1098,1157..1158,
                     1162)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:380931"
     Region          1074..1093
                     /region_name="Interaction with histone H3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            order(1115,1168,1170,1175)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380931"
     Region          1154..1157
                     /region_name="Interaction with histone H3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            1204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     Site            1210
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96KQ7.3)"
     CDS             1..1210
                     /gene="EHMT2"
                     /gene_synonym="BAT8; C6orf30; G9A; GAT8; KMT1C; NG36"
                     /coded_by="NM_006709.5:22..3654"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4725.1"
                     /db_xref="GeneID:10919"
                     /db_xref="HGNC:HGNC:14129"
                     /db_xref="MIM:604599"
ORIGIN      
        1 maaaagaaaa aaaegeapae mgallleket rgatervhgs lgdtprseet lpkatpdsle
       61 pagpsspasv tvtvgdegad tpvgatplig desenlegdg dlrggrillg hatksfpssp
      121 skggscpsra kmsmtgagks ppsvqslamr llsmpgaqga aaagsepppa ttspegqpkv
      181 hrarktmskp gngqppvpek rppeiqhfrm sddvhslgkv tsdlakrrkl nsggglseel
      241 gsarrsgevt ltkgdpgsle ewetvvgddf slyydsysvd ervdsdskse vealteqlse
      301 eeeeeeeeee eeeeeeeeee eeedeesgnq sdrsgssgrr kakkkwrkds pwvkpsrkrr
      361 krepprakep rgvngvgssg pseymevplg slelpsegtl spnhagvsnd tssletergf
      421 eelplcscrm eapkidrise raghkcmate svdgelsgcn aailkretmr pssrvalmvl
      481 cethrarmvk hhccpgcgyf ctagtflech pdfrvahrfh kacvsqlngm vfcphcgeda
      541 seaqevtipr gdgvtppagt aapappplsq dvpgradtsq psarmrghge prrppcdpla
      601 dtidssgpsl tlpnggclsa vglplgpgre alekalviqe serrkklrfh prqlylsvkq
      661 gelqkvilml ldnldpnfqs dqqskrtplh aaaqkgsvei chvllqagan inavdkqqrt
      721 plmeavvnnh levarymvqr ggcvyskeed gstclhhaak ignlemvsll lstgqvdvna
      781 qdsggwtpii waaehkhiev irmlltrgad vtltdneeni clhwasftgs aaiaevllna
      841 rcdlhavnyh gdtplhiaar esyhdcvllf lsrganpelr nkegdtawdl tpersdvwfa
      901 lqlnrklrlg vgnrairtek iicrdvargy envpipcvng vdgepcpedy kyisencets
      961 tmnidrnith lqhctcvddc sssnclcgql sircwydkdg rllqefnkie pplifecnqa
     1021 cscwrncknr vvqsgikvrl qlyrtakmgw gvralqtipq gtficeyvge lisdaeadvr
     1081 eddsylfdld nkdgevycid aryygnisrf inhlcdpnii pvrvfmlhqd lrfpriaffs
     1141 srdirtgeel gfdygdrfwd ikskyftcqc gsekckhsae aialeqsrla rldphpellp
     1201 elgslppvnt
//
LOCUS       NP_001265662             668 aa            linear   PRI 21-NOV-2025
DEFINITION  T-cell activation Rho GTPase-activating protein isoform d [Homo
            sapiens].
ACCESSION   NP_001265662
VERSION     NP_001265662.1
DBSOURCE    REFSEQ: accession NM_001278733.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Xu,Z., Zheng,T., Zheng,Z., Jiang,W., Huang,L., Deng,K., Yuan,L.,
            Qin,F., Sun,Y., Qin,J. and Li,S.
  TITLE     TAGAP expression influences CD4+ T cell differentiation, immune
            infiltration, and cytotoxicity in LUAD through the STAT pathway:
            implications for immunotherapy
  JOURNAL   Front Immunol 14, 1224340 (2023)
   PUBMED   37744350
  REMARK    GeneRIF: TAGAP expression influences CD4+ T cell differentiation,
            immune infiltration, and cytotoxicity in LUAD through the STAT
            pathway: implications for immunotherapy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Shri Preethi,M. and Asha Devi,S.
  TITLE     An attempt to unravel the association of TAGAP gene SNPs with
            rheumatoid arthritis in the Indian population using high-resolution
            melting analysis
  JOURNAL   Gene 834, 146584 (2022)
   PUBMED   35597527
  REMARK    GeneRIF: An attempt to unravel the association of TAGAP gene SNPs
            with rheumatoid arthritis in the Indian population using
            high-resolution melting analysis.
REFERENCE   4  (residues 1 to 668)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 668)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 668)
  AUTHORS   Romanos,J., Barisani,D., Trynka,G., Zhernakova,A., Bardella,M.T.
            and Wijmenga,C.
  TITLE     Six new coeliac disease loci replicated in an Italian population
            confirm association with coeliac disease
  JOURNAL   J Med Genet 46 (1), 60-63 (2009)
   PUBMED   18805825
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 668)
  AUTHORS   Hunt,K.A., Zhernakova,A., Turner,G., Heap,G.A., Franke,L.,
            Bruinenberg,M., Romanos,J., Dinesen,L.C., Ryan,A.W., Panesar,D.,
            Gwilliam,R., Takeuchi,F., McLaren,W.M., Holmes,G.K., Howdle,P.D.,
            Walters,J.R., Sanders,D.S., Playford,R.J., Trynka,G., Mulder,C.J.,
            Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M., O'Morain,C.,
            Kennedy,N.P., Kelleher,D., Pennington,D.J., Strachan,D.P.,
            McArdle,W.L., Mein,C.A., Wapenaar,M.C., Deloukas,P., McGinnis,R.,
            McManus,R., Wijmenga,C. and van Heel,D.A.
  TITLE     Newly identified genetic risk variants for celiac disease related
            to the immune response
  JOURNAL   Nat Genet 40 (4), 395-402 (2008)
   PUBMED   18311140
  REMARK    GeneRIF: Genome-wide association study of gene-disease association.
            (HuGE Navigator)
REFERENCE   8  (residues 1 to 668)
  AUTHORS   Sommer,C.A., Pavarino-Bertelli,E.C., Goloni-Bertollo,E.M. and
            Henrique-Silva,F.
  TITLE     Identification of dysregulated genes in lymphocytes from children
            with Down syndrome
  JOURNAL   Genome 51 (1), 19-29 (2008)
   PUBMED   18356936
REFERENCE   9  (residues 1 to 668)
  AUTHORS   Chang,I.F. and Hsiao,H.Y.
  TITLE     Induction of RhoGAP and pathological changes characteristic of
            Alzheimer's disease by UAHFEMF discharge in rat brain
  JOURNAL   Curr Alzheimer Res 2 (5), 559-569 (2005)
   PUBMED   16375659
REFERENCE   10 (residues 1 to 668)
  AUTHORS   Mao,M., Biery,M.C., Kobayashi,S.V., Ward,T., Schimmack,G.,
            Burchard,J., Schelter,J.M., Dai,H., He,Y.D. and Linsley,P.S.
  TITLE     T lymphocyte activation gene identification by coregulated
            expression on DNA microarrays
  JOURNAL   Genomics 83 (6), 989-999 (2004)
   PUBMED   15177553
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA819174.1, AF385429.1 and
            AL035530.11.
            
            Summary: This gene encodes a member of the Rho GTPase-activator
            protein superfamily. The encoded protein may function as a Rho
            GTPase-activating protein. Alterations in this gene may be
            associated with several diseases, including rheumatoid arthritis,
            celiac disease, and multiple sclerosis. Alternate splicing results
            in multiple transcript variants encoding distinct isoforms.
            [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (4) uses an alternate 5'-most
            exon, lacks a portion of the 5' coding region, and initiates
            translation at a downstream start codon, compared to variant 2. The
            encoded isoform (d) has a shorter N-terminus, compared to isoform
            b.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1865614.1,
                                           SRR14038193.1523329.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670, SAMEA2144835
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..668
                     /product="T-cell activation Rho GTPase-activating protein
                     isoform d"
                     /calculated_mol_wt=73417
     Region          22..218
                     /region_name="RhoGAP_ARHGAP20"
                     /note="RhoGAP (GTPase-activator protein [GAP] for Rho-like
                     small GTPases) domain of ArhGAP20-like proteins. ArhGAP20,
                     also known as KIAA1391 and RA-RhoGAP, contains a RhoGAP, a
                     RA, and a PH domain, and ANXL repeats. ArhGAP20 is
                     activated by Rap1 and induces...; cd04402"
                     /db_xref="CDD:239867"
     Site            order(60,96,100,169,172..173,200)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239867"
     Site            60
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239867"
     CDS             1..668
                     /gene="TAGAP"
                     /gene_synonym="ARHGAP47; FKSG15; IDDM21; TAGAP1"
                     /coded_by="NM_001278733.2:151..2157"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:117289"
                     /db_xref="HGNC:HGNC:15669"
                     /db_xref="MIM:609667"
ORIGIN      
        1 mrrlspasdf sgaletdlka slfdqplsii cgdsdtlprp iqdiltilcl kgpstegifr
       61 raanekarke lkeelnsgda vdlerlpvhl lavvfkdflr siprkllssd lfeewmgale
      121 mqdeedriea lkqvadklpr pnllllkhlv yvlhliskns evnrmdssnl aicigpnmlt
      181 lendqslsfe aqkdlnnkvk tlveflidnc feifgenipv hssitsddsl ehtdssdvst
      241 lqndsaydsn dpdvesnsss gisspsrqpq vpmataagld sagpqdarev spepivstva
      301 rlksslaqpd rrysepsmps sqeclesrvt nqtltksegd fpvprvgsrl eseeaedpfp
      361 eevfpavqgk tkrpvdlkik nlapgsvlpr alvlkafsss sldassdssp vaspsspkrn
      421 ffsrhqsftt ktekgkpsre ikkhsmsftf aphkkvltkn lsagsgksqd ftrdhvprgv
      481 rkesqlagri vqengcethn qtargfclrp halsvddvfq gadwerpgsp psyeeamqgp
      541 aarlvasesq tvgsmtvgsm rarmleahcl lpplppahhv edsrhrgske plpghglspl
      601 perwkqsrtv hasgdslghv sgpgrpellp lrtvsesvqr nkrdclvrrc sqpvfeadqf
      661 qyakesyi
//
LOCUS       NP_004936                866 aa            linear   PRI 21-NOV-2025
DEFINITION  dynamin-2 isoform 3 [Homo sapiens].
ACCESSION   NP_004936
VERSION     NP_004936.2
DBSOURCE    REFSEQ: accession NM_004945.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 866)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 866)
  AUTHORS   Bayones,L., Guerra-Fernandez,M.J., Figueroa-Cares,C., Gallo,L.I.,
            Alfonso-Bueno,S., Caspe,O., Canal,M.P., Baez-Matus,X.,
            Gonzalez-Jamett,A., Cardenas,A.M. and Marengo,F.D.
  TITLE     Dynamin-2 mutations linked to neonatal-onset centronuclear myopathy
            impair exocytosis and endocytosis in adrenal chromaffin cells
  JOURNAL   J Neurochem 168 (9), 3268-3283 (2024)
   PUBMED   39126680
  REMARK    GeneRIF: Dynamin-2 mutations linked to neonatal-onset centronuclear
            myopathy impair exocytosis and endocytosis in adrenal chromaffin
            cells.
REFERENCE   3  (residues 1 to 866)
  AUTHORS   Perdreau-Dahl,H., Lipsett,D.B., Frisk,M., Kermani,F., Carlson,C.R.,
            Brech,A., Shen,X., Bergan-Dahl,A., Hou,Y., Tuomainen,T., Tavi,P.,
            Jones,P.P., Lunde,M., Wasserstrom,J.A., Laporte,J., Ullrich,N.D.,
            Christensen,G., Morth,J.P. and Louch,W.E.
  TITLE     BIN1, Myotubularin, and Dynamin-2 Coordinate T-Tubule Growth in
            Cardiomyocytes
  JOURNAL   Circ Res 132 (11), e188-e205 (2023)
   PUBMED   37139790
  REMARK    GeneRIF: BIN1, Myotubularin, and Dynamin-2 Coordinate T-Tubule
            Growth in Cardiomyocytes.
REFERENCE   4  (residues 1 to 866)
  AUTHORS   Sobh,M., Aref,S., Al Agdar,M., El Zafrany,M. and El-Sokkary,A.M.A.
  TITLE     Implication of Dynamin-2 (DNM2) Mutations in Adult T-cell Acute
            Lymphoblastic Leukemia
  JOURNAL   Asian Pac J Cancer Prev 24 (4), 1257-1264 (2023)
   PUBMED   37116148
  REMARK    GeneRIF: Implication of Dynamin-2 (DNM2) Mutations in Adult T-cell
            Acute Lymphoblastic Leukemia.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 866)
  AUTHORS   Kasai,K., Shin,H.W., Shinotsuka,C., Murakami,K. and Nakayama,K.
  TITLE     Dynamin II is involved in endocytosis but not in the formation of
            transport vesicles from the trans-Golgi network
  JOURNAL   J Biochem 125 (4), 780-789 (1999)
   PUBMED   10101292
REFERENCE   6  (residues 1 to 866)
  AUTHORS   Klocke,R., Augustin,A., Ronsiek,M., Stief,A., van der Putten,H. and
            Jockusch,H.
  TITLE     Dynamin genes Dnm1 and Dnm2 are located on proximal mouse
            chromosomes 2 and 9, respectively
  JOURNAL   Genomics 41 (2), 290-292 (1997)
   PUBMED   9143510
REFERENCE   7  (residues 1 to 866)
  AUTHORS   Diatloff-Zito,C., Gordon,A.J., Duchaud,E. and Merlin,G.
  TITLE     Isolation of an ubiquitously expressed cDNA encoding human dynamin
            II, a member of the large GTP-binding protein family
  JOURNAL   Gene 163 (2), 301-306 (1995)
   PUBMED   7590285
REFERENCE   8  (residues 1 to 866)
  AUTHORS   Zuchner,S. and Tao,F.
  TITLE     DNM2-Related Intermediate Charcot-Marie-Tooth Neuropathy - RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20614582
REFERENCE   9  (residues 1 to 866)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   10 (residues 1 to 866)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011475.6, AC011552.6,
            AC112707.2, BC054501.1 and BU621654.1.
            
            On Dec 10, 2004 this sequence version replaced NP_004936.1.
            
            Summary: Dynamins represent one of the subfamilies of GTP-binding
            proteins. These proteins share considerable sequence similarity
            over the N-terminal portion of the molecule, which contains the
            GTPase domain. Dynamins are associated with microtubules. They have
            been implicated in cell processes such as endocytosis and cell
            motility, and in alterations of the membrane that accompany certain
            activities such as bone resorption by osteoclasts. Dynamins bind
            many proteins that bind actin and other cytoskeletal proteins.
            Dynamins can also self-assemble, a process that stimulates GTPase
            activity. Five alternatively spliced transcripts encoding different
            proteins have been described. Additional alternatively spliced
            transcripts may exist, but their full-length nature has not been
            determined. [provided by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon, compared to variant 1. The resulting protein (isoform 3) is
            shorter, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L36983.1, BC054501.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..866
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..866
                     /product="dynamin-2 isoform 3"
                     /EC_number="3.6.5.5"
                     /note="dynamin II"
                     /calculated_mol_wt=97521
     Region          6..245
                     /region_name="DYNc"
                     /note="Dynamin, GTPase; smart00053"
                     /db_xref="CDD:197491"
     Region          38..45
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (P50570.2)"
     Site            38..45
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206738"
     Site            order(39,41..46,59..60,65,136,206,208..209,235..239,242)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206738"
     Site            order(40..41,140,153,178,180,182..185,187..188,209,
                     211..214,238..240)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:206738"
     Region          64..66
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (P50570.2)"
     Site            65
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206738"
     Site            69..71
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206738"
     Region          136..139
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (P50570.2)"
     Site            136..139
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206738"
     Site            order(138..139,169..170)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206738"
     Region          205..208
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (P50570.2)"
     Site            205..208
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206738"
     Region          215..502
                     /region_name="Dynamin_M"
                     /note="Dynamin central region; pfam01031"
                     /db_xref="CDD:460033"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000250|UniProtKB:P39052,
                     ECO:0000305|PubMed:34744632; propagated from
                     UniProtKB/Swiss-Prot (P50570.2)"
     Region          235..238
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (P50570.2)"
     Site            235..237
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206738"
     Site            299
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P39054; propagated from
                     UniProtKB/Swiss-Prot (P50570.2)"
     Region          514..625
                     /region_name="PH_dynamin"
                     /note="Dynamin pleckstrin homology (PH) domain; cd01256"
                     /db_xref="CDD:269958"
     Site            order(516,518..519,521,538,607..608,611,614..615,618)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:269958"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000250|UniProtKB:P39052,
                     ECO:0000305|PubMed:34744632; propagated from
                     UniProtKB/Swiss-Prot (P50570.2)"
     Site            594
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P50570.2)"
     Region          645..735
                     /region_name="GED"
                     /note="Dynamin GTPase effector domain; pfam02212"
                     /db_xref="CDD:460495"
     Region          <733..864
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          737..866
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50570.2)"
     Site            751
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P50570.2)"
     Site            760
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:P39052; propagated from
                     UniProtKB/Swiss-Prot (P50570.2)"
     Site            844
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-alpha.
                     /evidence=ECO:0000269|PubMed:36445308; propagated from
                     UniProtKB/Swiss-Prot (P50570.2)"
     CDS             1..866
                     /gene="DNM2"
                     /gene_synonym="CMT2M; CMTDI1; CMTDIB; DI-CMTB; DYN2;
                     DYNII; LCCS5"
                     /coded_by="NM_004945.4:165..2765"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS32907.1"
                     /db_xref="GeneID:1785"
                     /db_xref="HGNC:HGNC:2974"
                     /db_xref="MIM:602378"
ORIGIN      
        1 mgnrgmeeli plvnklqdaf ssigqschld lpqiavvggq sagkssvlen fvgrdflprg
       61 sgivtrrpli lqlifskteh aeflhckskk ftdfdevrqe ieaetdrvtg tnkgispvpi
      121 nlrvysphvl nltlidlpgi tkvpvgdqpp dieyqikdmi lqfisressl ilavtpanmd
      181 lansdalkla kevdpqglrt igvitkldlm degtdardvl enkllplrrg yigvvnrsqk
      241 diegkkdira alaaerkffl shpayrhmad rmgtphlqkt lnqqltnhir eslpalrskl
      301 qsqllsleke veeyknfrpd dptrktkall qmvqqfgvdf ekriegsgdq vdtlelsgga
      361 rinrifherf pfelvkmefd ekdlrreisy aiknihgvrt glftpdlafe aivkkqvvkl
      421 kepclkcvdl viqelintvr qctsklssyp rlreeteriv ttyireregr tkdqilllid
      481 ieqsyintnh edfigfanaq qrstqlnkkr aipnqvirrg wltinnislm kggskeywfv
      541 ltaeslswyk deeekekkym lpldnlkird vekgfmsnkh vfaifnteqr nvykdlrqie
      601 lacdsqedvd swkasflrag vypekdqaen edgaqentfs mdpqlerqve tirnlvdsyv
      661 aiinksirdl mpktimhlmi nntkafihhe llaylyssad qsslmeesad qaqrrddmlr
      721 myhalkealn iigdiststv stpvpppvdd twlqsasshs ptpqrrpvss ihppgrppav
      781 rgptpgppli pvpvgaaasf sappipsrpg pqsvfansdl fpappqipsr pvrippgipp
      841 gvpsrrppaa psrptiirpa epslld
//
LOCUS       NP_001340594             408 aa            linear   PRI 21-NOV-2025
DEFINITION  WD repeat-containing protein 20 isoform 18 [Homo sapiens].
ACCESSION   NP_001340594 XP_016877268
VERSION     NP_001340594.1
DBSOURCE    REFSEQ: accession NM_001353665.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Jiang,L., Qi,X., Lai,M., Zhou,J., Yuan,M., You,J., Liu,Q., Pan,J.,
            Zhao,L., Ying,M., Ji,J., Li,K., Zhang,Y., Pan,W., He,Q., Yang,B.
            and Cao,J.
  TITLE     WDR20 prevents hepatocellular carcinoma senescence by orchestrating
            the simultaneous USP12/46-mediated deubiquitination of c-Myc
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2407904121 (2024)
   PUBMED   39432777
  REMARK    GeneRIF: WDR20 prevents hepatocellular carcinoma senescence by
            orchestrating the simultaneous USP12/46-mediated deubiquitination
            of c-Myc.
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Ng,V.H., Spencer,Z., Neitzel,L.R., Nayak,A., Loberg,M.A., Shen,C.,
            Kassel,S.N., Kroh,H.K., An,Z., Anthony,C.C., Bryant,J.M.,
            Lawson,A., Goldsmith,L., Benchabane,H., Hansen,A.G., Li,J.,
            D'Souza,S., Lebensohn,A.M., Rohatgi,R., Weiss,W.A., Weiss,V.L.,
            Williams,C., Hong,C.C., Robbins,D.J., Ahmed,Y. and Lee,E.
  TITLE     The USP46 complex deubiquitylates LRP6 to promote Wnt/beta-catenin
            signaling
  JOURNAL   Nat Commun 14 (1), 6173 (2023)
   PUBMED   37798301
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Olazabal-Herrero,A., Bilbao-Arribas,M., Carlevaris,O., Sendino,M.,
            Varela-Martinez,E., Jugo,B.M., Berra,E. and Rodriguez,J.A.
  TITLE     The dystrophia myotonica WD repeat-containing protein DMWD and
            WDR20 differentially regulate USP12 deubiquitinase
  JOURNAL   FEBS J 288 (20), 5943-5963 (2021)
   PUBMED   33844468
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Dahlberg,C.L. and Juo,P.
  TITLE     The WD40-repeat proteins WDR-20 and WDR-48 bind and activate the
            deubiquitinating enzyme USP-46 to promote the abundance of the
            glutamate receptor GLR-1 in the ventral nerve cord of
            Caenorhabditis elegans
  JOURNAL   J Biol Chem 289 (6), 3444-3456 (2014)
   PUBMED   24356955
REFERENCE   8  (residues 1 to 408)
  AUTHORS   Kee,Y., Yang,K., Cohn,M.A., Haas,W., Gygi,S.P. and D'Andrea,A.D.
  TITLE     WDR20 regulates activity of the USP12 x UAF1 deubiquitinating
            enzyme complex
  JOURNAL   J Biol Chem 285 (15), 11252-11257 (2010)
   PUBMED   20147737
  REMARK    GeneRIF: WDR20 serves as a stimulatory subunit for preserving and
            regulating the activity of the subset of the UAF1 x USP12 complexes
REFERENCE   9  (residues 1 to 408)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   10 (residues 1 to 408)
  AUTHORS   Smith,T.F.
  TITLE     Diversity of WD-repeat proteins
  JOURNAL   Subcell Biochem 48, 20-30 (2008)
   PUBMED   18925368
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133223.5 and AL359402.3.
            
            On Jul 21, 2017 this sequence version replaced XP_016877268.1.
            
            Summary: This gene encodes a WD repeat-containing protein that
            functions to preserve and regulate the activity of the USP12-UAF1
            deubiquitinating enzyme complex. Multiple alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Jun 2011].
            
            Transcript Variant: This variant (21), as well as variants 18-20
            and 22, encodes isoform 18.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.78349.1,
                                           SRR3476690.254760.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2147596
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.31"
     Protein         1..408
                     /product="WD repeat-containing protein 20 isoform 18"
                     /note="WD repeat-containing protein 20"
                     /calculated_mol_wt=44373
     Region          <35..141
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          50..86
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          93..126
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..408
                     /gene="WDR20"
                     /gene_synonym="Bun107; DMR"
                     /coded_by="NM_001353665.2:179..1405"
                     /note="isoform 18 is encoded by transcript variant 21"
                     /db_xref="GeneID:91833"
                     /db_xref="HGNC:HGNC:19667"
                     /db_xref="MIM:617741"
ORIGIN      
        1 mylynvehtc gttaphyqll kqgesfavht ckskstrnpl lkwtvgegal nefafspdgk
       61 flacvsqdgf lrvfnfdsve lhgtmksyfg gllcvcwspd gkyivtgged dlvtvwsfvd
      121 crviarghgh kswvsvvafd pyttsveegd pmefsgsded fqdllhfgrd ranstqsrls
      181 krnstdsrpv svtyrfgsvg qdtqlclwdl tedilfphqp lsrarthtnv mnatsppags
      241 ngnsvttpgn svppplprsn slphsavsna gskssvmdga iasgvskfat lslhdrkerh
      301 hekdhkrnhs mghisskssd klnlvtktkt dpaktlgtpl cprmedvpll eplickkiah
      361 erltvlifle dcivtacqeg fictwgrpgk vgslsspsqa sspggtvv
//
LOCUS       NP_001191056             499 aa            linear   PRI 21-NOV-2025
DEFINITION  inositol 1,4,5-triphosphate receptor associated 2 isoform a [Homo
            sapiens].
ACCESSION   NP_001191056
VERSION     NP_001191056.1
DBSOURCE    REFSEQ: accession NM_001204127.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Okumura,W., Tadahira,K., Kozono,T., Tamura-Nakano,M., Sato,H.,
            Matsui,H., Dohi,T., Rohrer,J., Tonozuka,T. and Nishikawa,A.
  TITLE     Jaw1/LRMP is associated with the maintenance of Golgi ribbon
            structure
  JOURNAL   J Biochem 173 (5), 383-392 (2023)
   PUBMED   36689741
  REMARK    GeneRIF: Jaw1/LRMP is associated with the maintenance of Golgi
            ribbon structure.
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Okumura,W., Kozono,T., Sato,H., Matsui,H., Takagi,T., Tonozuka,T.
            and Nishikawa,A.
  TITLE     Jaw1/LRMP increases Ca2+ influx upon GPCR stimulation with
            heterogeneous effect on the activity of each ITPR subtype
  JOURNAL   Sci Rep 12 (1), 9476 (2022)
   PUBMED   35676525
  REMARK    GeneRIF: Jaw1/LRMP increases Ca(2+) influx upon GPCR stimulation
            with heterogeneous effect on the activity of each ITPR subtype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Cruz,V.E., Esra Demircioglu,F. and Schwartz,T.U.
  TITLE     Structural Analysis of Different LINC Complexes Reveals Distinct
            Binding Modes
  JOURNAL   J Mol Biol 432 (23), 6028-6041 (2020)
   PUBMED   33058875
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Bataille,P., Michaud,V., Robert,M.P., Bekel,L., Leclerc-Mercier,S.,
            Harroche,A., Celerier,C., Lasseaux,E., Borgel,D.,
            Bremond-Gignac,D., Bodemer,C., Arveiler,B. and Hadj-Rabia,S.
  TITLE     Clinical variability and probable founder effect in oculocutaneous
            albinism type 7
  JOURNAL   Clin Genet 97 (3), 527-528 (2020)
   PUBMED   31694064
  REMARK    GeneRIF: Clinical variability and probable founder effect in
            oculocutaneous albinism type 7.
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Kohno,T., Kunitoh,H., Suzuki,K., Yamamoto,S., Kuchiba,A.,
            Matsuno,Y., Yanagitani,N. and Yokota,J.
  TITLE     Association of KRAS polymorphisms with risk for lung adenocarcinoma
            accompanied by atypical adenomatous hyperplasias
  JOURNAL   Carcinogenesis 29 (5), 957-963 (2008)
   PUBMED   18299280
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Manenti,G., Galbiati,F., Pettinicchio,A., Spinola,M., Piconese,S.,
            Leoni,V.P., Conti,B., Ravagnani,F., Incarbone,M., Pastorino,U. and
            Dragani,T.A.
  TITLE     A V141L polymorphism of the human LRMP gene is associated with
            survival of lung cancer patients
  JOURNAL   Carcinogenesis 27 (7), 1386-1390 (2006)
   PUBMED   16410263
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Snyder,H.L., Bacik,I., Bennink,J.R., Kearns,G., Behrens,T.W.,
            Bachi,T., Orlowski,M. and Yewdell,J.W.
  TITLE     Two novel routes of transporter associated with antigen processing
            (TAP)-independent major histocompatibility complex class I antigen
            processing
  JOURNAL   J Exp Med 186 (7), 1087-1098 (1997)
   PUBMED   9314557
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Behrens,T.W., Kearns,G.M., Rivard,J.J., Bernstein,H.D.,
            Yewdell,J.W. and Staudt,L.M.
  TITLE     Carboxyl-terminal targeting and novel post-translational processing
            of JAW1, a lymphoid protein of the endoplasmic reticulum
  JOURNAL   J Biol Chem 271 (38), 23528-23534 (1996)
   PUBMED   8798562
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Behrens,T.W., Jagadeesh,J., Scherle,P., Kearns,G., Yewdell,J. and
            Staudt,L.M.
  TITLE     Jaw1, A lymphoid-restricted membrane protein localized to the
            endoplasmic reticulum
  JOURNAL   J Immunol 153 (2), 682-690 (1994)
   PUBMED   8021504
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK303256.1, AC023510.16 and
            AW206014.1.
            
            Summary: The protein encode dby this gene is expressed in a
            developmentally regulated manner in lymphoid cell lines and
            tissues. The protein is localized to the cytoplasmic face of the
            endoplasmic reticulum. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303256.1, SRR14038191.3601063.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..499
                     /product="inositol 1,4,5-triphosphate receptor associated
                     2 isoform a"
                     /note="protein Jaw1; lymphoid restricted membrane protein"
                     /calculated_mol_wt=56082
     Region          4..499
                     /region_name="MRVI1"
                     /note="MRVI1 protein; pfam05781"
                     /db_xref="CDD:461738"
     CDS             1..499
                     /gene="IRAG2"
                     /gene_synonym="JAW1; LRMP"
                     /coded_by="NM_001204127.2:485..1984"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS8701.1"
                     /db_xref="GeneID:4033"
                     /db_xref="HGNC:HGNC:6690"
                     /db_xref="MIM:602003"
ORIGIN      
        1 mnddpsmeen gvervcpesl lqsreysslp lprhtsstdg titssdpgle ilnmascdld
       61 rnslckkeed trsasptiea qgtspahdni afqdstskdk tilnleakee petieehkke
      121 hasgdsvvsp lpvttvksvn lrqsentsan ekeveaeflr lslgfkcdwf tlekrvklee
      181 rsrdlaeenl kkeitnclkl lesltplced dnqaqeiikk leksikflsq caarvasrae
      241 mlgainqesr vskavevmiq hvenlkrmya kehaeleelk qvllqnersf npleddddcq
      301 ikkrsaslns kpsslrrvti aslprnigna gmvagmennd rfsrrssswr ilgskqsehr
      361 pslprfisty swadaeeekc elktkddsep sgeetvertr kpslsekknn pskwdvssvy
      421 dtiaswatnl kssirkanka lwlsiafivl faalmsfltg qlfqksvdaa ptqqedswts
      481 lehilwpftr lrhngpppv
//
LOCUS       NP_510867                164 aa            linear   PRI 21-NOV-2025
DEFINITION  cyclin-dependent kinase inhibitor 1 isoform 1 [Homo sapiens].
ACCESSION   NP_510867
VERSION     NP_510867.1
DBSOURCE    REFSEQ: accession NM_078467.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Hu,F., Zhao,L., Wang,J., Li,X., Xue,Z., Ma,Y., Zheng,M., Chen,C.,
            Tong,M., Guo,X., Li,H., Jin,H., Xie,Q., Zhang,X., Huang,C. and
            Huang,H.
  TITLE     TRIM40 interacts with ROCK1 directly and inhibits colorectal cancer
            cell proliferation through the c-Myc/p21 axis
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (8), 119855 (2024)
   PUBMED   39357549
  REMARK    GeneRIF: TRIM40 interacts with ROCK1 directly and inhibits
            colorectal cancer cell proliferation through the c-Myc/p21 axis.
REFERENCE   3  (residues 1 to 164)
  AUTHORS   de Azevedo,S.S.D., Ribeiro-Alves,M., Cortes,F.H., Delatorre,E.,
            Hoagland,B., Villela,L.M., Grinsztejn,B., Veloso,V.G.,
            Morgado,M.G., Souza,T.M.L. and Bello,G.
  TITLE     HIV-1 controllers exhibit an enhanced antiretroviral innate state
            characterised by overexpression of p21 and MCPIP1 and silencing of
            ERVK-6 RNA expression
  JOURNAL   Mem Inst Oswaldo Cruz 119, e240071 (2024)
   PUBMED   39292108
  REMARK    GeneRIF: HIV-1 controllers exhibit an enhanced antiretroviral
            innate state characterised by overexpression of p21 and MCPIP1 and
            silencing of ERVK-6 RNA expression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 164)
  AUTHORS   White-Gilbertson,S., Lu,P., Saatci,O., Sahin,O., Delaney,J.R.,
            Ogretmen,B. and Voelkel-Johnson,C.
  TITLE     Transcriptome analysis of polyploid giant cancer cells and their
            progeny reveals a functional role for p21 in polyploidization and
            depolyploidization
  JOURNAL   J Biol Chem 300 (4), 107136 (2024)
   PUBMED   38447798
  REMARK    GeneRIF: Transcriptome analysis of polyploid giant cancer cells and
            their progeny reveals a functional role for p21 in polyploidization
            and depolyploidization.
REFERENCE   5  (residues 1 to 164)
  AUTHORS   Shuai,Y., Zhang,H., Liu,C., Wang,J., Jiang,Y., Sun,J., Gao,X.,
            Bo,X., Xiao,X., Liao,X., Huang,C., Chen,H. and Jiang,G.
  TITLE     CLIC3 interacts with NAT10 to inhibit N4-acetylcytidine
            modification of p21 mRNA and promote bladder cancer progression
  JOURNAL   Cell Death Dis 15 (1), 9 (2024)
   PUBMED   38182571
  REMARK    GeneRIF: CLIC3 interacts with NAT10 to inhibit N4-acetylcytidine
            modification of p21 mRNA and promote bladder cancer progression.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 164)
  AUTHORS   Kim,K.M., Cho,H. and Kim,Y.K.
  TITLE     The upstream open reading frame of cyclin-dependent kinase
            inhibitor 1A mRNA negatively regulates translation of the
            downstream main open reading frame
  JOURNAL   Biochem Biophys Res Commun 424 (3), 469-475 (2012)
   PUBMED   22771799
  REMARK    GeneRIF: These findings provide biological insights into the
            possible role of nonsense-mediated mRNA decay in diverse biological
            pathways mediated by CDKN1A.
REFERENCE   7  (residues 1 to 164)
  AUTHORS   Kearsey,J.M., Coates,P.J., Prescott,A.R., Warbrick,E. and Hall,P.A.
  TITLE     Gadd45 is a nuclear cell cycle regulated protein which interacts
            with p21Cip1
  JOURNAL   Oncogene 11 (9), 1675-1683 (1995)
   PUBMED   7478594
REFERENCE   8  (residues 1 to 164)
  AUTHORS   Hall,M., Bates,S. and Peters,G.
  TITLE     Evidence for different modes of action of cyclin-dependent kinase
            inhibitors: p15 and p16 bind to kinases, p21 and p27 bind to
            cyclins
  JOURNAL   Oncogene 11 (8), 1581-1588 (1995)
   PUBMED   7478582
REFERENCE   9  (residues 1 to 164)
  AUTHORS   Mousses,S., Ozcelik,H., Lee,P.D., Malkin,D., Bull,S.B. and
            Andrulis,I.L.
  TITLE     Two variants of the CIP1/WAF1 gene occur together and are
            associated with human cancer
  JOURNAL   Hum Mol Genet 4 (6), 1089-1092 (1995)
   PUBMED   7655464
REFERENCE   10 (residues 1 to 164)
  AUTHORS   Demetrick,D.J., Matsumoto,S., Hannon,G.J., Okamoto,K., Xiong,Y.,
            Zhang,H. and Beach,D.H.
  TITLE     Chromosomal mapping of the genes for the human cell cycle proteins
            cyclin C (CCNC), cyclin E (CCNE), p21 (CDKN1) and KAP (CDKN3)
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 190-192 (1995)
   PUBMED   7698009
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z85996.1.
            
            Summary: This gene encodes a potent cyclin-dependent kinase
            inhibitor. The encoded protein binds to and inhibits the activity
            of cyclin-cyclin-dependent kinase2 or -cyclin-dependent kinase4
            complexes, and thus functions as a regulator of cell cycle
            progression at G1. The expression of this gene is tightly
            controlled by the tumor suppressor protein p53, through which this
            protein mediates the p53-dependent cell cycle G1 phase arrest in
            response to a variety of stress stimuli. This protein can interact
            with proliferating cell nuclear antigen, a DNA polymerase accessory
            factor, and plays a regulatory role in S phase DNA replication and
            DNA damage repair. This protein was reported to be specifically
            cleaved by CASP3-like caspases, which thus leads to a dramatic
            activation of cyclin-dependent kinase2, and may be instrumental in
            the execution of apoptosis following caspase activation. Mice that
            lack this gene have the ability to regenerate damaged or missing
            tissue. Multiple alternatively spliced variants have been found for
            this gene. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks
            an in-frame portion of the 5' coding region, and initiates
            translation at a downstream start codon, compared to variant 3. The
            resulting isoform (1) has a shorter N-terminus, compared to isoform
            2. Variants 1, 2, 4, 5, and 10 all encode the same isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU154329.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147975 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: lack of evidence for use of
                                                upstream AUG
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..164
                     /product="cyclin-dependent kinase inhibitor 1 isoform 1"
                     /note="melanoma differentiation associated protein 6;
                     CDK-interaction protein 1; wild-type p53-activated
                     fragment 1; DNA synthesis inhibitor; cyclin-dependent
                     kinase inhibitor 1; CDK-interacting protein 1;
                     cyclin-dependent kinase inhibitor 1A (p21, Cip1)"
                     /calculated_mol_wt=17988
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:15574338; propagated from
                     UniProtKB/Swiss-Prot (P38936.3)"
     Region          17..24
                     /region_name="Required for binding cyclins"
                     /note="propagated from UniProtKB/Swiss-Prot (P38936.3)"
     Region          21..66
                     /region_name="CDI"
                     /note="Cyclin-dependent kinase inhibitor; pfam02234"
                     /db_xref="CDD:460503"
     Region          53..58
                     /region_name="Required for binding CDKs"
                     /note="propagated from UniProtKB/Swiss-Prot (P38936.3)"
     Region          76..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P38936.3)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by LKB1.
                     /evidence=ECO:0000269|PubMed:25329316; propagated from
                     UniProtKB/Swiss-Prot (P38936.3)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta.
                     /evidence=ECO:0000269|PubMed:18794347; propagated from
                     UniProtKB/Swiss-Prot (P38936.3)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P38936.3)"
     Region          140..164
                     /region_name="PIP-box K+4 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P38936.3)"
     Region          141..156
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P38936.3)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA, PKB/AKT1, PIM1 and PIM2.
                     /evidence=ECO:0000269|PubMed:10753973,
                     ECO:0000269|PubMed:11463845, ECO:0000269|PubMed:12431783,
                     ECO:0000269|PubMed:16982699, ECO:0000269|PubMed:20307683;
                     propagated from UniProtKB/Swiss-Prot (P38936.3)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC and NUAK1.
                     /evidence=ECO:0000269|PubMed:10753973,
                     ECO:0000269|PubMed:25329316; propagated from
                     UniProtKB/Swiss-Prot (P38936.3)"
     Region          152..164
                     /region_name="Interaction with TRIM39.
                     /evidence=ECO:0000269|PubMed:23213251"
                     /note="propagated from UniProtKB/Swiss-Prot (P38936.3)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC, in vitro.
                     /evidence=ECO:0000269|PubMed:10753973; propagated from
                     UniProtKB/Swiss-Prot (P38936.3)"
     CDS             1..164
                     /gene="CDKN1A"
                     /gene_synonym="CAP20; CDKN1; CIP1; MDA-6; P21; p21CIP1;
                     SDI1; WAF1"
                     /coded_by="NM_078467.3:100..594"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4824.1"
                     /db_xref="GeneID:1026"
                     /db_xref="HGNC:HGNC:1784"
                     /db_xref="MIM:116899"
ORIGIN      
        1 msepagdvrq npcgskacrr lfgpvdseql srdcdalmag ciqearerwn fdfvtetple
       61 gdfawervrg lglpklylpt gprrgrdelg ggrrpgtspa llqgtaeedh vdlslsctlv
      121 prsgeqaegs pggpgdsqgr krrqtsmtdf yhskrrlifs krkp
//
LOCUS       NP_036219                519 aa            linear   PRI 21-NOV-2025
DEFINITION  general transcription factor 3C polypeptide 5 isoform 2 [Homo
            sapiens].
ACCESSION   NP_036219
VERSION     NP_036219.2
DBSOURCE    REFSEQ: accession NM_012087.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Iwata-Otsubo,A., Skraban,C.M., Yoshimura,A., Sakata,T.,
            Alves,C.A.P., Fiordaliso,S.K., Kuroda,Y., Vengoechea,J.,
            Grochowsky,A., Ernste,P., Lulis,L., Nesbitt,A., Tayoun,A.A.,
            Gray,C., Towne,M.C., Radtke,K., Normand,E.A., Rhodes,L., Seiler,C.,
            Shirahige,K. and Izumi,K.
  TITLE     Biallelic variants in GTF3C5, a regulator of RNA polymerase
            III-mediated transcription, cause a multisystem developmental
            disorder
  JOURNAL   Hum Genet 143 (3), 437-453 (2024)
   PUBMED   38520561
  REMARK    GeneRIF: Biallelic variants in GTF3C5, a regulator of RNA
            polymerase III-mediated transcription, cause a multisystem
            developmental disorder.
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Dumay-Odelot,H., Marck,C., Durrieu-Gaillard,S., Lefebvre,O.,
            Jourdain,S., Prochazkova,M., Pflieger,A. and Teichmann,M.
  TITLE     Identification, molecular cloning, and characterization of the
            sixth subunit of human transcription factor TFIIIC
  JOURNAL   J Biol Chem 282 (23), 17179-17189 (2007)
   PUBMED   17409385
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Hirschowitz,E.A., Hiestand,D.M. and Yannelli,J.R.
  TITLE     Vaccines for lung cancer
  JOURNAL   J Thorac Oncol 1 (1), 93-104 (2006)
   PUBMED   17409835
  REMARK    Review article
REFERENCE   5  (residues 1 to 519)
  AUTHORS   Hsieh,Y.J., Kundu,T.K., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     The TFIIIC90 subunit of TFIIIC interacts with multiple components
            of the RNA polymerase III machinery and contains a histone-specific
            acetyltransferase activity
  JOURNAL   Mol Cell Biol 19 (11), 7697-7704 (1999)
   PUBMED   10523658
REFERENCE   6  (residues 1 to 519)
  AUTHORS   Hsieh,Y.J., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     Cloning and characterization of two evolutionarily conserved
            subunits (TFIIIC102 and TFIIIC63) of human TFIIIC and their
            involvement in functional interactions with TFIIIB and RNA
            polymerase III
  JOURNAL   Mol Cell Biol 19 (7), 4944-4952 (1999)
   PUBMED   10373544
REFERENCE   7  (residues 1 to 519)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK055092.1 and AJ420443.1.
            
            On Mar 25, 2008 this sequence version replaced NP_036219.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 3' coding region, compared to variant 1, which results
            in a shorter isoform (2), compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017337.2, AK225761.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372097.10/ ENSP00000361169.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..519
                     /product="general transcription factor 3C polypeptide 5
                     isoform 2"
                     /note="transcription factor IIIC, 63 kD; general
                     transcription factor 3C polypeptide 5; TF3C-epsilon;
                     TFIIIC 63 kDa subunit; transcription factor IIIC subunit
                     epsilon; transcription factor IIIC 63 kDa subunit; general
                     transcription factor IIIC, polypeptide 5, 63kDa"
                     /calculated_mol_wt=59440
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5Q8.2)"
     Region          25..132
                     /region_name="Tau95_N"
                     /note="Tau95 Triple barrel domain; pfam17682"
                     /db_xref="CDD:465457"
     Region          168..322
                     /region_name="Tau95"
                     /note="RNA polymerase III transcription factor (TF)IIIC
                     subunit HTH domain; pfam09734"
                     /db_xref="CDD:462865"
     Region          465..519
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q8.2)"
     CDS             1..519
                     /gene="GTF3C5"
                     /gene_synonym="TFiiiC2-63; TFIIIC63; TFIIICepsilon"
                     /coded_by="NM_012087.4:16..1575"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6958.1"
                     /db_xref="GeneID:9328"
                     /db_xref="HGNC:HGNC:4668"
                     /db_xref="MIM:604890"
ORIGIN      
        1 maaeaadlgl gaavpvelrr errmvcveyp gvvrdvakml ptlggeegvs riyadptkrl
       61 elyfrpkdpy chpvcanrfs tsslllrirk rtrrqkgvlg teahsevtfd meilgiisti
      121 ykfqgmsdfq ylavhteagg khtsmydkvl mlrpekeaff hqelplyipp pifsrldapv
      181 dyfyrpetqh regynnppis genliglsra rrphnaifvn fedeevpkqp leaaaqtwrr
      241 vctnpvdrkv eeelrklfdi rpiwsrnavk anisvhpdkl kvllpfiayy mitgpwrslw
      301 irfgydprkn pdakiyqvld frircgmkhg yapsdlpvka krstynyslp itvkktssql
      361 vtmhdlkqgl gpsgtsgark passkyklkd svyifregal ppyrqmfyql cdlnveelqk
      421 iihrndgaen scterdgwcl pktsdelrdt mslmirqtir skrpalfsss akadggkeql
      481 tyesgedeed eeeeeeeeed fkpsdgsene meteildyv
//
LOCUS       NP_001287840             383 aa            linear   PRI 21-NOV-2025
DEFINITION  myotilin isoform c [Homo sapiens].
ACCESSION   NP_001287840 XP_005272186
VERSION     NP_001287840.1
DBSOURCE    REFSEQ: accession NM_001300911.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Guglielmi,V., Pancheri,E., Cannone,E., Nigro,V., Malatesta,M.,
            Vettori,A., Giorgetti,A., Torella,A., Aurino,S., Cisterna,B.,
            Marchetto,G., Tomelleri,G., Tonin,P., Schiavone,M. and Vattemi,G.
  TITLE     A novel in-frame deletion in MYOT causes an early adult onset
            distal myopathy
  JOURNAL   Clin Genet 104 (6), 705-710 (2023)
   PUBMED   37553249
  REMARK    GeneRIF: A novel in-frame deletion in MYOT causes an early adult
            onset distal myopathy.
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Cannone,E., Guglielmi,V., Marchetto,G., Tobia,C., Gnutti,B.,
            Cisterna,B., Tonin,P., Barbon,A., Vattemi,G. and Schiavone,M.
  TITLE     Human Mutated MYOT and CRYAB Genes Cause a Myopathic Phenotype in
            Zebrafish
  JOURNAL   Int J Mol Sci 24 (14), 11483 (2023)
   PUBMED   37511242
  REMARK    GeneRIF: Human Mutated MYOT and CRYAB Genes Cause a Myopathic
            Phenotype in Zebrafish.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Lin,Z.J., Xu,J.M., Ji,H.Y., Jiang,Y.Q., Su,J., Fan,L.L. and Yu,R.
  TITLE     Silencing MYOT Expression May Inhibit Autophagy in Human Skeletal
            Muscle Cells
  JOURNAL   Dis Markers 2023, 3350685 (2023)
   PUBMED   36776921
  REMARK    GeneRIF: Silencing MYOT Expression May Inhibit Autophagy in Human
            Skeletal Muscle Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Salmikangas,P., Mykkanen,O.M., Gronholm,M., Heiska,L., Kere,J. and
            Carpen,O.
  TITLE     Myotilin, a novel sarcomeric protein with two Ig-like domains, is
            encoded by a candidate gene for limb-girdle muscular dystrophy
  JOURNAL   Hum Mol Genet 8 (7), 1329-1336 (1999)
   PUBMED   10369880
REFERENCE   6  (residues 1 to 383)
  AUTHORS   Bartoloni,L., Horrigan,S.K., Viles,K.D., Gilchrist,J.M.,
            Stajich,J.M., Vance,J.M., Yamaoka,L.H., Pericak-Vance,M.A.,
            Westbrook,C.A. and Speer,M.C.
  TITLE     Use of a CEPH meiotic breakpoint panel to refine the locus of
            limb-girdle muscular dystrophy type 1A (LGMD1A) to a 2-Mb interval
            on 5q31
  JOURNAL   Genomics 54 (2), 250-255 (1998)
   PUBMED   9828127
REFERENCE   7  (residues 1 to 383)
  AUTHORS   Selcen,D. and Engel,A.G.
  TITLE     Myofibrillar Myopathy - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301672
REFERENCE   8  (residues 1 to 383)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   9  (residues 1 to 383)
  AUTHORS   Speer,M.C., Yamaoka,L.H., Gilchrist,J.H., Gaskell,C.P.,
            Stajich,J.M., Vance,J.M., Kazantsev,A., Lastra,A.A., Haynes,C.S.,
            Beckmann,J.S. et al.
  TITLE     Confirmation of genetic heterogeneity in limb-girdle muscular
            dystrophy: linkage of an autosomal dominant form to chromosome 5q
  JOURNAL   Am J Hum Genet 50 (6), 1211-1217 (1992)
   PUBMED   1598902
REFERENCE   10 (residues 1 to 383)
  AUTHORS   Dixon,M.J., Read,A.P., Donnai,D., Colley,A., Dixon,J. and
            Williamson,R.
  TITLE     The gene for Treacher Collins syndrome maps to the long arm of
            chromosome 5
  JOURNAL   Am J Hum Genet 49 (1), 17-22 (1991)
   PUBMED   1676560
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA896167.1, AK300076.1 and
            AF133820.2.
            
            On Jul 16, 2014 this sequence version replaced XP_005272186.1.
            
            Summary: This gene encodes a cystoskeletal protein which plays a
            significant role in the stability of thin filaments during muscle
            contraction. This protein binds F-actin, crosslinks actin
            filaments, and prevents latrunculin A-induced filament disassembly.
            Mutations in this gene have been associated with limb-girdle
            muscular dystrophy and myofibrillar myopathies. Several
            alternatively spliced transcript variants of this gene have been
            described, but the full-length nature of some of these variants has
            not been determined.[provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (3) lacks an internal segment in
            the 5' region, which results in translation initiation at a
            downstream start codon, compared to variant 1. The resulting
            isoform (c) has a shorter N-terminus, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.16313.1, AK300076.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154361, SAMEA2155550
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.2"
     Protein         1..383
                     /product="myotilin isoform c"
                     /note="titin immunoglobulin domain protein (myotilin); 57
                     kDa cytoskeletal protein; myofibrillar titin-like Ig
                     domains protein"
                     /calculated_mol_wt=42773
     Region          135..225
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          152..156
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          165..169
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          191..195
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          205..210
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          218..221
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          234..325
                     /region_name="IgI_Myotilin_C"
                     /note="C-terminal immunoglobulin (Ig)-like domain of
                     myotilin; member of the I-set of Ig superfamily (IgSF)
                     domains; cd05892"
                     /db_xref="CDD:409473"
     Region          234..237
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409473"
     Region          240..245
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409473"
     Region          250..257
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409473"
     Region          264..270
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409473"
     Region          271..274
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409473"
     Region          281..287
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409473"
     Region          290..300
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409473"
     Region          304..312
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409473"
     Region          314..325
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409473"
     CDS             1..383
                     /gene="MYOT"
                     /gene_synonym="LGMD1; LGMD1A; MFM3; TTID; TTOD"
                     /coded_by="NM_001300911.2:300..1451"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS75309.1"
                     /db_xref="GeneID:9499"
                     /db_xref="HGNC:HGNC:12399"
                     /db_xref="MIM:604103"
ORIGIN      
        1 mdsnyqqssa gqpinakpsq tanakpiprt pdheiqgske aliqdlerkl kckdtllhng
       61 nqrltyeekm arrllgpqna aavfqaqdds gaqdsqqhns eharlqvpts qvrsrstsrg
      121 dvndqdaiqe kfypprfiqv penmsidegr fcrmdfkvsg lpapdvswyl ngrtvqsddl
      181 hkmivsekgl hslifevvra sdagayacva knrageatft vqldvlakeh krapmfiykp
      241 qskkvlegds vklecqisai pppklfwkrn nemvqfntdr islyqdntgr vtllikdvnk
      301 kdagwytvsa vneagvttcn trldvtarpn qtlpapkqlr vrptfskyla lngkglnvkq
      361 afnpegefqr laaqsglyes eel
//
LOCUS       NP_001007069             292 aa            linear   PRI 21-NOV-2025
DEFINITION  syntenin-1 isoform 2 [Homo sapiens].
ACCESSION   NP_001007069
VERSION     NP_001007069.1
DBSOURCE    REFSEQ: accession NM_001007068.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Yu,J., Yu,S., Bai,J., Zhu,Z., Gao,Y. and Li,Y.
  TITLE     SDCBP modulates tumor microenvironment, tumor progression and
            anti-PD1 efficacy in colorectal cancer
  JOURNAL   Cancer Gene Ther 31 (5), 755-765 (2024)
   PUBMED   38555398
  REMARK    GeneRIF: SDCBP modulates tumor microenvironment, tumor progression
            and anti-PD1 efficacy in colorectal cancer.
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Li,R., Ma,Z., Zheng,W., Xiao,Y., Wang,Z., Yi,J., Wang,Y. and
            Chen,C.
  TITLE     Anaplasma phagocytophilum Ats-1 enhances exosome secretion through
            Syntenin-1
  JOURNAL   BMC Microbiol 23 (1), 271 (2023)
   PUBMED   37759206
  REMARK    GeneRIF: Anaplasma phagocytophilum Ats-1 enhances exosome secretion
            through Syntenin-1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Liu,J., Bai,W., Zhou,T., Xie,Y., Yang,B., Sun,J., Wang,Y., Li,X.,
            Hou,X., Liu,Z., Fu,D., Yan,J., Jiang,W., Zhao,K., Zhou,B., Yuan,S.,
            Guo,Y., Wang,H., Chang,A., Gao,S., Shi,L., Huang,C., Yang,S. and
            Hao,J.
  TITLE     SDCBP promotes pancreatic cancer progression by preventing YAP1
            from beta-TrCP-mediated proteasomal degradation
  JOURNAL   Gut 72 (9), 1722-1737 (2023)
   PUBMED   36828627
  REMARK    GeneRIF: SDCBP promotes pancreatic cancer progression by preventing
            YAP1 from beta-TrCP-mediated proteasomal degradation.
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Lee,K.M., Seo,E.C., Lee,J.H., Kim,H.J. and Hwangbo,C.
  TITLE     The Multifunctional Protein Syntenin-1: Regulator of Exosome
            Biogenesis, Cellular Function, and Tumor Progression
  JOURNAL   Int J Mol Sci 24 (11), 9418 (2023)
   PUBMED   37298370
  REMARK    GeneRIF: The Multifunctional Protein Syntenin-1: Regulator of
            Exosome Biogenesis, Cellular Function, and Tumor Progression.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Fernandez-Larrea,J., Merlos-Suarez,A., Urena,J.M., Baselga,J. and
            Arribas,J.
  TITLE     A role for a PDZ protein in the early secretory pathway for the
            targeting of proTGF-alpha to the cell surface
  JOURNAL   Mol Cell 3 (4), 423-433 (1999)
   PUBMED   10230395
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Lin,D., Gish,G.D., Songyang,Z. and Pawson,T.
  TITLE     The carboxyl terminus of B class ephrins constitutes a PDZ domain
            binding motif
  JOURNAL   J Biol Chem 274 (6), 3726-3733 (1999)
   PUBMED   9920925
REFERENCE   8  (residues 1 to 292)
  AUTHORS   Torres,R., Firestein,B.L., Dong,H., Staudinger,J., Olson,E.N.,
            Huganir,R.L., Bredt,D.S., Gale,N.W. and Yancopoulos,G.D.
  TITLE     PDZ proteins bind, cluster, and synaptically colocalize with Eph
            receptors and their ephrin ligands
  JOURNAL   Neuron 21 (6), 1453-1463 (1998)
   PUBMED   9883737
REFERENCE   9  (residues 1 to 292)
  AUTHORS   Lin,J.J., Jiang,H. and Fisher,P.B.
  TITLE     Melanoma differentiation associated gene-9, mda-9, is a human gamma
            interferon responsive gene
  JOURNAL   Gene 207 (2), 105-110 (1998)
   PUBMED   9511750
REFERENCE   10 (residues 1 to 292)
  AUTHORS   Grootjans,J.J., Zimmermann,P., Reekmans,G., Smets,A., Degeest,G.,
            Durr,J. and David,G.
  TITLE     Syntenin, a PDZ protein that binds syndecan cytoplasmic domains
  JOURNAL   Proc Natl Acad Sci U S A 94 (25), 13683-13688 (1997)
   PUBMED   9391086
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG772269.1, BC013254.2 and
            U83463.1.
            
            Summary: The protein encoded by this gene was initially identified
            as a molecule linking syndecan-mediated signaling to the
            cytoskeleton. The syntenin protein contains tandemly repeated PDZ
            domains that bind the cytoplasmic, C-terminal domains of a variety
            of transmembrane proteins. This protein may also affect
            cytoskeletal-membrane organization, cell adhesion, protein
            trafficking, and the activation of transcription factors. The
            protein is primarily localized to membrane-associated adherens
            junctions and focal adhesions but is also found at the endoplasmic
            reticulum and nucleus. Alternative splicing results in multiple
            transcript variants encoding different isoforms. Related
            pseudogenes have been identified on multiple chromosomes. [provided
            by RefSeq, Jan 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.2685719.1,
                                           SRR14038191.1274035.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.1"
     Protein         1..292
                     /product="syntenin-1 isoform 2"
                     /note="melanoma differentiation associated protein-9;
                     scaffold protein Pbp1; pro-TGF-alpha cytoplasmic
                     domain-interacting protein 18; syntenin-1; syndecan
                     binding protein (syntenin); syndecan-binding protein 1"
                     /calculated_mol_wt=31631
     Region          107..185
                     /region_name="PDZ1_syntenin-like"
                     /note="PDZ domain 1 of syntenin-1, syntenin-2, and related
                     domains; cd06721"
                     /db_xref="CDD:467204"
     Site            order(118..124,133,136,165,169,172..173)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467204"
     Region          187..264
                     /region_name="PDZ2_syntenin-like"
                     /note="PDZ domain 2 of syntenin-1, syntenin-2, and related
                     domains; cd06794"
                     /db_xref="CDD:467256"
     Site            order(202..208,213,216,245,249,252..253)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467256"
     CDS             1..292
                     /gene="SDCBP"
                     /gene_synonym="MDA-9; MDA9; SDCBP1; ST1; SYCL; TACIP18"
                     /coded_by="NM_001007068.2:59..937"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS47863.1"
                     /db_xref="GeneID:6386"
                     /db_xref="HGNC:HGNC:10662"
                     /db_xref="MIM:602217"
ORIGIN      
        1 mslypsledl kaqtafsanp anpailseas apiphdgnly prlypelsqy mglslneeei
       61 ranvavvsga plqgqlvarp ssinymvapv tgndvgirra eikqgirevi lckdqdgkig
      121 lrlksidngi fvqlvqansp aslvglrfgd qvlqingenc agwssdkahk vlkqafgeki
      181 tmtirdrpfe rtitmhkdst ghvgfifkng kitsivkdss aarngllteh niceingqnv
      241 iglkdsqiad ilstsgtvvt itimpafife hiikrmapsi mkslmdhtip ev
//
LOCUS       NP_001186088             463 aa            linear   PRI 21-NOV-2025
DEFINITION  peptidase inhibitor 16 precursor [Homo sapiens].
ACCESSION   NP_001186088
VERSION     NP_001186088.1
DBSOURCE    REFSEQ: accession NM_001199159.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Chen,Q., Jiang,L.Y., Cao,C., Liu,F.Y., Li,D.R., Wu,P.F. and
            Jiang,K.R.
  TITLE     Peptidase inhibitor 16 promotes proliferation of pancreatic ductal
            adenocarcinoma cells through OASL signaling
  JOURNAL   Mol Carcinog 63 (5), 938-950 (2024)
   PUBMED   38353288
  REMARK    GeneRIF: Peptidase inhibitor 16 promotes proliferation of
            pancreatic ductal adenocarcinoma cells through OASL signaling.
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Wang,F., Gu,X., Lin,S., Wu,Q., Sun,Y., Zhang,Q., Luo,A., Feng,X.,
            Wang,L., Xu,L., Sun,W. and Tan,W.
  TITLE     Peptidase inhibitor 16 promotes inflammatory arthritis by
            suppressing Foxp3 expression via regulating K48-linked ubiquitin
            degradation Bmi-1 in regulatory T cells
  JOURNAL   Clin Immunol 259, 109883 (2024)
   PUBMED   38147957
  REMARK    GeneRIF: Peptidase inhibitor 16 promotes inflammatory arthritis by
            suppressing Foxp3 expression via regulating K48-linked ubiquitin
            degradation Bmi-1 in regulatory T cells.
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Hope,C.M., Welch,J., Mohandas,A., Pederson,S., Hill,D.,
            Gundsambuu,B., Eastaff-Leung,N., Grosse,R., Bresatz,S., Ang,G.,
            Papademetrios,M., Zola,H., Duhen,T., Campbell,D., Brown,C.Y.,
            Krumbiegel,D., Sadlon,T., Couper,J.J. and Barry,S.C.
  TITLE     Peptidase inhibitor 16 identifies a human regulatory T-cell subset
            with reduced FOXP3 expression over the first year of recent onset
            type 1 diabetes
  JOURNAL   Eur J Immunol 49 (8), 1235-1250 (2019)
   PUBMED   31127857
  REMARK    GeneRIF: this study shows that Peptidase inhibitor 16 identifies a
            human regulatory T-cell subset with reduced FOXP3 expression over
            the first year of recent onset type 1 diabetes
REFERENCE   6  (residues 1 to 463)
  AUTHORS   Nicholson,I.C., Mavrangelos,C., Bird,D.R., Bresatz-Atkins,S.,
            Eastaff-Leung,N.G., Grose,R.H., Gundsambuu,B., Hill,D.,
            Millard,D.J., Sadlon,T.J., To,S., Zola,H., Barry,S.C. and
            Krumbiegel,D.
  TITLE     PI16 is expressed by a subset of human memory Treg with enhanced
            migration to CCL17 and CCL20
  JOURNAL   Cell Immunol 275 (1-2), 12-18 (2012)
   PUBMED   22533972
  REMARK    GeneRIF: PI16-positive Treg showed enhanced in vitro migration
            towards the inflammatory chemokines CCL17 and CCL20, suggesting
            they can migrate to sites of inflammation
REFERENCE   7  (residues 1 to 463)
  AUTHORS   Bozaoglu,K., Curran,J.E., Stocker,C.J., Zaibi,M.S., Segal,D.,
            Konstantopoulos,N., Morrison,S., Carless,M., Dyer,T.D., Cole,S.A.,
            Goring,H.H., Moses,E.K., Walder,K., Cawthorne,M.A., Blangero,J. and
            Jowett,J.B.
  TITLE     Chemerin, a novel adipokine in the regulation of angiogenesis
  JOURNAL   J Clin Endocrinol Metab 95 (5), 2476-2485 (2010)
   PUBMED   20237162
REFERENCE   8  (residues 1 to 463)
  AUTHORS   Reeves,J.R., Dulude,H., Panchal,C., Daigneault,L. and Ramnani,D.M.
  TITLE     Prognostic value of prostate secretory protein of 94 amino acids
            and its binding protein after radical prostatectomy
  JOURNAL   Clin Cancer Res 12 (20 Pt 1), 6018-6022 (2006)
   PUBMED   17062675
  REMARK    GeneRIF: a novel and independent prognostic markers following
            radical prostatectomy for prostate cancer.
REFERENCE   9  (residues 1 to 463)
  AUTHORS   Reeves,J.R., Xuan,J.W., Arfanis,K., Morin,C., Garde,S.V.,
            Ruiz,M.T., Wisniewski,J., Panchal,C. and Tanner,J.E.
  TITLE     Identification, purification and characterization of a novel human
            blood protein with binding affinity for prostate secretory protein
            of 94 amino acids
  JOURNAL   Biochem J 385 (Pt 1), 105-114 (2005)
   PUBMED   15344909
  REMARK    GeneRIF: A new blood protein PSP94-binding protein (PSPBP) is
            identified that binds prostate secretory protein of 94 amino acids
            (PSP94).
REFERENCE   10 (residues 1 to 463)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB178215.1, DA342875.1, BC022399.1 and AL050088.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AK075470.1, BC022399.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968968, SAMEA2154665 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..463
                     /product="peptidase inhibitor 16 precursor"
                     /note="protease inhibitor 16; microseminoprotein,
                     beta-binding protein; PSP94-binding protein; cysteine-rich
                     secretory protein 9"
                     /calculated_mol_wt=46721
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2768
     mat_peptide     28..463
                     /product="peptidase inhibitor 16"
                     /calculated_mol_wt=46721
     Region          33..166
                     /region_name="CAP_PI16_HrTT-1"
                     /note="CAP (cysteine-rich secretory proteins, antigen 5,
                     and pathogenesis-related 1 proteins) domain of peptidase
                     inhibitor 16 and HrTT-1 protein; cd05559"
                     /db_xref="CDD:349405"
     Site            114
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXB8.1)"
     Region          262..281
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXB8.1)"
     Region          303..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXB8.1)"
     Region          383..408
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXB8.1)"
     Region          386..395
                     /region_name="O-glycosylated at one site"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXB8.1)"
     Site            403
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXB8.1)"
     Site            409
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXB8.1)"
     CDS             1..463
                     /gene="PI16"
                     /gene_synonym="CD364; CRISP9; MSMBBP; PSPBP"
                     /coded_by="NM_001199159.2:191..1582"
                     /db_xref="CCDS:CCDS34440.1"
                     /db_xref="GeneID:221476"
                     /db_xref="HGNC:HGNC:21245"
ORIGIN      
        1 mhgscsflml llplllllva ttgpvgaltd eekrlmvelh nlyraqvspt asdmlhmrwd
       61 eelaafakay arqcvwghnk ergrrgenlf aitdegmdvp lameewhher ehynlsaatc
      121 spgqmcghyt qvvwakteri gcgshfcekl qgveetniel lvcnyeppgn vkgkrpyqeg
      181 tpcsqcpsgy hcknslcepi gspedaqdlp ylvteapsfr ateasdsrkm gtpsslatgi
      241 paflvtevsg slatkalpav etqaptslat kdppsmatea ppcvttevps ilaahslpsl
      301 deepvtfpks thvpipksad kvtdktkvps rspensldpk msltgarell phaqeeaeae
      361 aelppssevl asvfpaqdkp gelqatldht ghtsskslpn fpntsatana tggralalqs
      421 slpgaegpdk psvvsglnsg pghvwgpllg llllpplvla gif
//
LOCUS       NP_001276915             200 aa            linear   PRI 21-NOV-2025
DEFINITION  TIMELESS-interacting protein isoform 2 [Homo sapiens].
ACCESSION   NP_001276915 XP_005254580
VERSION     NP_001276915.1
DBSOURCE    REFSEQ: accession NM_001289986.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Arai,H., Xiao,Y., Millstein,J., Wang,J., Battaglin,F.,
            Kawanishi,N., Jayachandran,P., Soni,S., Zhang,W., Mancao,C.,
            Salhia,B., Mumenthaler,S.M., Parikh,A.R. and Lenz,H.J.
  TITLE     Germline polymorphisms in genes maintaining the replication fork
            predict the efficacy of oxaliplatin and irinotecan in patients with
            metastatic colorectal cancer
  JOURNAL   Br J Cancer 126 (1), 72-78 (2022)
   PUBMED   34689170
  REMARK    GeneRIF: Germline polymorphisms in genes maintaining the
            replication fork predict the efficacy of oxaliplatin and irinotecan
            in patients with metastatic colorectal cancer.
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Grabarczyk,D.B.
  TITLE     The Fork Protection Complex: A Regulatory Hub at the Head of the
            Replisome
  JOURNAL   Subcell Biochem 99, 83-107 (2022)
   PUBMED   36151374
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Lerner,L.K., Holzer,S., Kilkenny,M.L., Svikovic,S., Murat,P.,
            Schiavone,D., Eldridge,C.B., Bittleston,A., Maman,J.D., Branzei,D.,
            Stott,K., Pellegrini,L. and Sale,J.E.
  TITLE     Timeless couples G-quadruplex detection with processing by DDX11
            helicase during DNA replication
  JOURNAL   EMBO J 39 (18), e104185 (2020)
   PUBMED   32705708
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 200)
  AUTHORS   Gotter,A.L., Suppa,C. and Emanuel,B.S.
  TITLE     Mammalian TIMELESS and Tipin are evolutionarily conserved
            replication fork-associated factors
  JOURNAL   J Mol Biol 366 (1), 36-52 (2007)
   PUBMED   17141802
  REMARK    GeneRIF: TIM and Tipin are functional orthologs of their
            replisome-associated yeast counterparts capable of coordinating
            replication with genotoxic stress responses, and distinguishes
            mammalian TIM from the circadian-specific paralogs.
REFERENCE   7  (residues 1 to 200)
  AUTHORS   Yoshizawa-Sugata,N. and Masai,H.
  TITLE     Human Tim/Timeless-interacting protein, Tipin, is required for
            efficient progression of S phase and DNA replication checkpoint
  JOURNAL   J Biol Chem 282 (4), 2729-2740 (2007)
   PUBMED   17102137
  REMARK    GeneRIF: Tipin is a checkpoint mediator that cooperates with Tim
            and may regulate the nuclear relocation of Claspin in response to
            replication checkpoint
REFERENCE   8  (residues 1 to 200)
  AUTHORS   Chou,D.M. and Elledge,S.J.
  TITLE     Tipin and Timeless form a mutually protective complex required for
            genotoxic stress resistance and checkpoint function
  JOURNAL   Proc Natl Acad Sci U S A 103 (48), 18143-18147 (2006)
   PUBMED   17116885
  REMARK    GeneRIF: observation explains the similar checkpoint phenotypes
            observed in both Tipin- and Timeless-depleted cells
REFERENCE   9  (residues 1 to 200)
  AUTHORS   Gotter,A.L.
  TITLE     Tipin, a novel timeless-interacting protein, is developmentally
            co-expressed with timeless and disrupts its self-association
  JOURNAL   J Mol Biol 331 (1), 167-176 (2003)
   PUBMED   12875843
REFERENCE   10 (residues 1 to 200)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            
            On Feb 14, 2014 this sequence version replaced XP_005254580.1.
            
            Summary: The protein encoded by this gene is part of the replisome
            complex, a group of proteins that support DNA replication. It binds
            TIM, which is involved in circadian rhythm regulation, and aids in
            protecting cells against DNA damage and stress. Two pseudogenes and
            two transcript variants encoding different isoforms have been found
            for this gene. [provided by RefSeq, Jul 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK299233.1, SRR14038195.1620482.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..200
                     /product="TIMELESS-interacting protein isoform 2"
                     /note="timeless-interacting protein; CSM3 homolog"
                     /calculated_mol_wt=23152
     Region          <2..47
                     /region_name="Swi3"
                     /note="Replication Fork Protection Component Swi3;
                     pfam07962"
                     /db_xref="CDD:462324"
     CDS             1..200
                     /gene="TIPIN"
                     /coded_by="NM_001289986.2:283..885"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:54962"
                     /db_xref="HGNC:HGNC:30750"
                     /db_xref="MIM:610716"
ORIGIN      
        1 mlirhmehwa hrlfpklqfe dfidrveylg skkevqtclk rirldlpilh edfvsnndev
       61 aennehdvts teldpfltnl sesemfasel srslteeqqq riernkqlal errqakllsn
      121 sqtlgndmlm ntprahtvee vntdedqkee snglnedild npcndaiant lneeetlldq
      181 sfknvqqqld atsrnitear
//
LOCUS       NP_958848                319 aa            linear   PRI 21-NOV-2025
DEFINITION  periphilin-1 isoform 4 [Homo sapiens].
ACCESSION   NP_958848
VERSION     NP_958848.1
DBSOURCE    REFSEQ: accession NM_201440.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Bloor,S., Wit,N. and Lehner,P.J.
  TITLE     RNA binding by Periphilin plays an essential role in initiating
            silencing by the HUSH complex
  JOURNAL   Nucleic Acids Res 53 (2) (2025)
   PUBMED   39658355
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Jensvold,Z.D., Flood,J.R., Christenson,A.E. and Lewis,P.W.
  TITLE     Interplay between Two Paralogous Human Silencing Hub (HuSH)
            Complexes in Regulating LINE-1 Element Silencing
  JOURNAL   Nat Commun 15 (1), 9492 (2024)
   PUBMED   39489739
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Tunbak,H., Enriquez-Gasca,R., Tie,C.H.C., Gould,P.A., Mlcochova,P.,
            Gupta,R.K., Fernandes,L., Holt,J., van der Veen,A.G.,
            Giampazolias,E., Burns,K.H., Maillard,P.V. and Rowe,H.M.
  TITLE     The HUSH complex is a gatekeeper of type I interferon through
            epigenetic regulation of LINE-1s
  JOURNAL   Nat Commun 11 (1), 5387 (2020)
   PUBMED   33144593
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Prigozhin,D.M., Douse,C.H., Farleigh,L.E., Albecka,A.,
            Tchasovnikarova,I.A., Timms,R.T., Oda,S.I., Adolf,F.,
            Freund,S.M.V., Maslen,S., Lehner,P.J. and Modis,Y.
  TITLE     Periphilin self-association underpins epigenetic silencing by the
            HUSH complex
  JOURNAL   Nucleic Acids Res 48 (18), 10313-10328 (2020)
   PUBMED   32976585
  REMARK    GeneRIF: Periphilin self-association underpins epigenetic silencing
            by the HUSH complex.
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Kurita,M., Suzuki,H., Masai,H., Mizumoto,K., Ogata,E.,
            Nishimoto,I., Aiso,S. and Matsuoka,M.
  TITLE     Overexpression of CR/periphilin downregulates Cdc7 expression and
            induces S-phase arrest
  JOURNAL   Biochem Biophys Res Commun 324 (2), 554-561 (2004)
   PUBMED   15474462
  REMARK    GeneRIF: CR (periphilin) retards S-phase progression by modifying
            expression of Cdc7 and other genes involved in progression of DNA
            replication
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Goehler,H., Lalowski,M., Stelzl,U., Waelter,S., Stroedicke,M.,
            Worm,U., Droege,A., Lindenberg,K.S., Knoblich,M., Haenig,C.,
            Herbst,M., Suopanki,J., Scherzinger,E., Abraham,C., Bauer,B.,
            Hasenbank,R., Fritzsche,A., Ludewig,A.H., Bussow,K., Coleman,S.H.,
            Gutekunst,C.A., Landwehrmeyer,B.G., Lehrach,H. and Wanker,E.E.
  TITLE     A protein interaction network links GIT1, an enhancer of huntingtin
            aggregation, to Huntington's disease
  JOURNAL   Mol Cell 15 (6), 853-865 (2004)
   PUBMED   15383276
  REMARK    Erratum:[Mol Cell. 2005 Jul 22;19(2):287. Buessow, Konrad
            [corrected to Bussow, Konrad]]
REFERENCE   8  (residues 1 to 319)
  AUTHORS   Kazerounian,S. and Aho,S.
  TITLE     Characterization of periphilin, a widespread, highly insoluble
            nuclear protein and potential constituent of the keratinocyte
            cornified envelope
  JOURNAL   J Biol Chem 278 (38), 36707-36717 (2003)
   PUBMED   12853457
  REMARK    GeneRIF: periphilin is potentially involved in epithelial
            differentiation and contributes to epidermal integrity and barrier
            formation
REFERENCE   9  (residues 1 to 319)
  AUTHORS   Kazerounian,S., Uitto,J. and Aho,S.
  TITLE     Unique role for the periplakin tail in intermediate filament
            association: specific binding to keratin 8 and vimentin
  JOURNAL   Exp Dermatol 11 (5), 428-438 (2002)
   PUBMED   12366696
REFERENCE   10 (residues 1 to 319)
  AUTHORS   Line,A., Stengrevics,A., Slucka,Z., Li,G., Jankevics,E. and
            Rees,R.C.
  TITLE     Serological identification and expression analysis of gastric
            cancer-associated genes
  JOURNAL   Br J Cancer 86 (11), 1824-1830 (2002)
   PUBMED   12087473
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK129910.1, AY157850.1,
            CA444170.1 and AC079601.25.
            
            Summary: The protein encoded by this gene is one of the several
            proteins that become sequentially incorporated into the cornified
            cell envelope during the terminal differentiation of keratinocyte
            at the outer layers of epidermis. This protein interacts with
            periplakin, which is known as a precursor of the cornified cell
            envelope. The cellular localization pattern and insolubility of
            this protein suggest that it may play a role in epithelial
            differentiation and contribute to epidermal integrity and barrier
            formation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (4) has multiple differences
            compared to variant 1. The resulting isoform (4) has distinct N-
            and C-termini, as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1462931.1,
                                           SRR14038197.2305741.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..319
                     /product="periphilin-1 isoform 4"
                     /note="gastric cancer antigen Ga50; CDC7 expression
                     repressor"
                     /calculated_mol_wt=36821
     Region          237..309
                     /region_name="periphilin-like"
                     /note="Vertebrate periphilin-1 and similar proteins;
                     cd22896"
                     /db_xref="CDD:439377"
     Site            order(242,246..247,250,253..254,257..258,261..262,265,283,
                     286..287,290..291,294..295,297..298,301..302,305)
                     /site_type="other"
                     /note="heterotrimer interface [polypeptide binding]"
                     /db_xref="CDD:439377"
     CDS             1..319
                     /gene="PPHLN1"
                     /gene_synonym="CR; HSPC206; HSPC232"
                     /coded_by="NM_201440.2:106..1065"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS55817.1"
                     /db_xref="GeneID:51535"
                     /db_xref="HGNC:HGNC:19369"
                     /db_xref="MIM:608150"
ORIGIN      
        1 mayrrdemws egryeyerip rerapprshp sdesgyrwtr ddhsasrqpe yrdmrdgfrr
       61 ksfysshyar erspykrdnt ffrespvgrk dsphsrsgss vssrsysper sksysfhqsq
      121 hrksvrpgas ykrqnegnpe rdkerpvqsl ktsrdtspss gsavssskvl dkpsrlteke
      181 laeaaskwaa ekleksdesn lpeiseyeag staplftdqp eepesntthg ielfedsqlt
      241 trskaiaskt keieqvyrqd cetfgmvvkm liekdpslek siqfalrqnl heigercvee
      301 lkhfiaeydt stqdfgepf
//
LOCUS       NP_001309165             774 aa            linear   PRI 21-NOV-2025
DEFINITION  ribosomal protein S6 kinase alpha-5 isoform l [Homo sapiens].
ACCESSION   NP_001309165
VERSION     NP_001309165.1
DBSOURCE    REFSEQ: accession NM_001322236.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 774)
  AUTHORS   Xu,P., Tao,Y., Zhang,H., Jin,M., Xu,H., Zou,S., Deng,F., Huang,L.,
            Zhang,H., Wang,X., Tang,X., Wang,Y., Yin,L. and Sun,X.
  TITLE     Associations of MSK1 Methylation and Executive Function With
            Suicidal Ideation in Adolescents With Major Depressive Disorder: A
            Prospective Cohort Study
  JOURNAL   J Clin Psychiatry 85 (1) (2024)
   PUBMED   38385994
  REMARK    GeneRIF: Associations of MSK1 Methylation and Executive Function
            With Suicidal Ideation in Adolescents With Major Depressive
            Disorder: A Prospective Cohort Study.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 774)
  AUTHORS   Sattarifard,H., Safaei,A., Khazeeva,E., Rastegar,M. and Davie,J.R.
  TITLE     Mitogen- and stress-activated protein kinase (MSK1/2) regulated
            gene expression in normal and disease states
  JOURNAL   Biochem Cell Biol 101 (3), 204-219 (2023)
   PUBMED   36812480
  REMARK    GeneRIF: Mitogen- and stress-activated protein kinase (MSK1/2)
            regulated gene expression in normal and disease states.
            Review article
REFERENCE   4  (residues 1 to 774)
  AUTHORS   Akbar,N., Forteath,C., Hussain,M.S., Reyskens,K., Belch,J.J.F.,
            Lang,C.C., Mordi,I.R., Bhalraam,U., Arthur,J.S.C. and Khan,F.
  TITLE     Mitogen and Stress-Activated Kinases 1 and 2 Mediate Endothelial
            Dysfunction
  JOURNAL   Int J Mol Sci 22 (16), 8655 (2021)
   PUBMED   34445361
  REMARK    GeneRIF: Mitogen and Stress-Activated Kinases 1 and 2 Mediate
            Endothelial Dysfunction.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 774)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 774)
  AUTHORS   Thomson,S., Clayton,A.L., Hazzalin,C.A., Rose,S., Barratt,M.J. and
            Mahadevan,L.C.
  TITLE     The nucleosomal response associated with immediate-early gene
            induction is mediated via alternative MAP kinase cascades: MSK1 as
            a potential histone H3/HMG-14 kinase
  JOURNAL   EMBO J 18 (17), 4779-4793 (1999)
   PUBMED   10469656
REFERENCE   7  (residues 1 to 774)
  AUTHORS   New,L., Zhao,M., Li,Y., Bassett,W.W., Feng,Y., Ludwig,S.,
            Padova,F.D., Gram,H. and Han,J.
  TITLE     Cloning and characterization of RLPK, a novel RSK-related protein
            kinase
  JOURNAL   J Biol Chem 274 (2), 1026-1032 (1999)
   PUBMED   9873047
REFERENCE   8  (residues 1 to 774)
  AUTHORS   Jain,N., Zhang,T., Fong,S.L., Lim,C.P. and Cao,X.
  TITLE     Repression of Stat3 activity by activation of mitogen-activated
            protein kinase (MAPK)
  JOURNAL   Oncogene 17 (24), 3157-3167 (1998)
   PUBMED   9872331
REFERENCE   9  (residues 1 to 774)
  AUTHORS   Deak,M., Clifton,A.D., Lucocq,L.M. and Alessi,D.R.
  TITLE     Mitogen- and stress-activated protein kinase-1 (MSK1) is directly
            activated by MAPK and SAPK2/p38, and may mediate activation of CREB
  JOURNAL   EMBO J 17 (15), 4426-4441 (1998)
   PUBMED   9687510
REFERENCE   10 (residues 1 to 774)
  AUTHORS   Chung,J., Uchida,E., Grammer,T.C. and Blenis,J.
  TITLE     STAT3 serine phosphorylation by ERK-dependent and -independent
            pathways negatively modulates its tyrosine phosphorylation
  JOURNAL   Mol Cell Biol 17 (11), 6508-6516 (1997)
   PUBMED   9343414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL121784.5, AL133454.6 and AL159191.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.194597.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.11"
     Protein         1..774
                     /product="ribosomal protein S6 kinase alpha-5 isoform l"
                     /EC_number="2.7.11.1"
                     /note="RSK-like protein kinase; nuclear mitogen- and
                     stress-activated protein kinase 1; ribosomal protein S6
                     kinase alpha-5; RSKL; S6K-alpha-5; 90 kDa ribosomal
                     protein S6 kinase 5; ribosomal protein S6 kinase, 90kDa,
                     polypeptide 5"
                     /calculated_mol_wt=86676
     Region          48..352
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(55..58,61,63,79,81,115,131..134,177,181..182,184,
                     194..195)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270765"
     Region          390..699
                     /region_name="STKc_MSK1_C"
                     /note="C-terminal catalytic domain of the Serine/Threonine
                     Kinase, Mitogen and stress-activated kinase 1; cd14179"
                     /db_xref="CDD:271081"
     Site            order(404..408,412,425,427,454,470..473,477,479,515..516,
                     518,520..521,523,536..537,540,555..559,561,688)
                     /site_type="active"
                     /db_xref="CDD:271081"
     Site            order(404..406,425,470..473,477,520..521,523,536,688)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271081"
     Site            order(408,477,479,515..516,518,520,540,555..559,561)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271081"
     Site            536..559
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271081"
     CDS             1..774
                     /gene="RPS6KA5"
                     /gene_synonym="MSK1; MSPK1; RLPK"
                     /coded_by="NM_001322236.2:208..2532"
                     /note="isoform l is encoded by transcript variant 12"
                     /db_xref="GeneID:9252"
                     /db_xref="HGNC:HGNC:10434"
                     /db_xref="MIM:603607"
ORIGIN      
        1 meeeggssgg aagtsadggd ggeqlltvkh elrtanltgh aekvgienfe llkvlgtgay
       61 gkvflvrkis ghdtgklyam kvlkkativq kakttehtrt erqvlehirq spflvtlhya
      121 fqtetklhli ldyinggelf thlsqrerft ehevqiyvge ivlalehlhk lgiiyrdikl
      181 enilldsngh vvltdfglsk efvadeavdw wslgvlmyel ltgaspftvd geknsqaeis
      241 rrilkseppy pqemsalakd liqrllmkdp kkrlgcgprd adeikehlff qkinwddlaa
      301 kkvpapfkpv irdeldvsnf aeeftemdpt yspaalpqss eklfqgysfv apsilfkrna
      361 avidplqfhm gverpgvtnv arsammkdsp fyqhydldlk dkplgegsfs icrkcvhkks
      421 nqafavkiis krmeantqke italklcegh pnivklhevf hdqlhtflvm ellnggelfe
      481 rikkkkhfse teasyimrkl vsavshmhdv gvvhrdlkpe nllftdendn leikiidfgf
      541 arlkppdnqp lktpcftlhy aapellnqng ydescdlwsl gvilytmlsg qvpfqshdrs
      601 ltctsaveim kkikkgdfsf egeawknvsq eakdliqgll tvdpnkrlkm sglrynewlq
      661 dgsqlssnpl mtpdilgssg aavhtcvkat fhafnkykre gfclqnvdka plakrrkmkk
      721 tststetrss ssesshssss hshgkttptk tlqpsnpads nnpetlfqfs dsva
//
LOCUS       NP_001310877             994 aa            linear   PRI 21-NOV-2025
DEFINITION  DIS3-like exonuclease 1 isoform 7 [Homo sapiens].
ACCESSION   NP_001310877
VERSION     NP_001310877.1
DBSOURCE    REFSEQ: accession NM_001323948.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Huntzinger,E., Sinteff,J., Morlet,B. and Seraphin,B.
  TITLE     HELZ2: a new, interferon-regulated, human 3'-5' exoribonuclease of
            the RNB family is expressed from a non-canonical initiation codon
  JOURNAL   Nucleic Acids Res 51 (17), 9279-9293 (2023)
   PUBMED   37602378
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 994)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 994)
  AUTHORS   Lee,J.Y., Moon,S., Kim,Y.K., Lee,S.H., Lee,B.S., Park,M.Y.,
            Park,J.E., Jang,Y. and Han,B.G.
  TITLE     Genome-based exome sequencing analysis identifies GYG1, DIS3L and
            DDRGK1 are associated with myocardial infarction in Koreans
  JOURNAL   J Genet 96 (6), 1041-1046 (2017)
   PUBMED   29321365
  REMARK    GeneRIF: we screened the susceptibility loci for Myocardial
            infarction (MI) using exome sequencing and validated candidate
            variants in replication sets. We identified that three genes (GYG1,
            DIS3L and DDRGK1) were associated with MI at the discovery and
            replication stages.
REFERENCE   6  (residues 1 to 994)
  AUTHORS   Li,L., Fridley,B.L., Kalari,K., Niu,N., Jenkins,G., Batzler,A.,
            Abo,R.P., Schaid,D. and Wang,L.
  TITLE     Discovery of genetic biomarkers contributing to variation in drug
            response of cytidine analogues using human lymphoblastoid cell
            lines
  JOURNAL   BMC Genomics 15, 93 (2014)
   PUBMED   24483146
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 994)
  AUTHORS   Lubas,M., Damgaard,C.K., Tomecki,R., Cysewski,D., Jensen,T.H. and
            Dziembowski,A.
  TITLE     Exonuclease hDIS3L2 specifies an exosome-independent 3'-5'
            degradation pathway of human cytoplasmic mRNA
  JOURNAL   EMBO J 32 (13), 1855-1868 (2013)
   PUBMED   23756462
REFERENCE   8  (residues 1 to 994)
  AUTHORS   Staals,R.H., Bronkhorst,A.W., Schilders,G., Slomovic,S.,
            Schuster,G., Heck,A.J., Raijmakers,R. and Pruijn,G.J.
  TITLE     Dis3-like 1: a novel exoribonuclease associated with the human
            exosome
  JOURNAL   EMBO J 29 (14), 2358-2367 (2010)
   PUBMED   20531389
  REMARK    GeneRIF: Data indicate that hDis3L1 is a novel exosome-associated
            exoribonuclease in the cytoplasm of human cells.
REFERENCE   9  (residues 1 to 994)
  AUTHORS   Tomecki,R., Kristiansen,M.S., Lykke-Andersen,S., Chlebowski,A.,
            Larsen,K.M., Szczesny,R.J., Drazkowska,K., Pastula,A.,
            Andersen,J.S., Stepien,P.P., Dziembowski,A. and Jensen,T.H.
  TITLE     The human core exosome interacts with differentially localized
            processive RNases: hDIS3 and hDIS3L
  JOURNAL   EMBO J 29 (14), 2342-2357 (2010)
   PUBMED   20531386
  REMARK    GeneRIF: Data show that hDIS3 and hDIS3L are active exonucleases,
            but only hDIS3 has retained endonucleolytic activity, and suggest
            that three different ribonucleases can serve as catalytic subunits
            for the exosome in human cells.
REFERENCE   10 (residues 1 to 994)
  AUTHORS   Slomovic,S., Fremder,E., Staals,R.H., Pruijn,G.J. and Schuster,G.
  TITLE     Addition of poly(A) and poly(A)-rich tails during RNA degradation
            in the cytoplasm of human cells
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7407-7412 (2010)
   PUBMED   20368444
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            
            Summary: The cytoplasmic RNA exosome complex degrades unstable
            mRNAs and is involved in the regular turnover of other mRNAs. The
            protein encoded by this gene contains 3'-5' exoribonuclease
            activity and is a catalytic component of this complex. [provided by
            RefSeq, May 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.61928.1,
                                           SRR1660807.172342.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..994
                     /product="DIS3-like exonuclease 1 isoform 7"
                     /EC_number="3.1.13.1"
                     /note="DIS3-like exonuclease 1; DIS3 mitotic control
                     homolog-like"
                     /calculated_mol_wt=113020
     Region          14..128
                     /region_name="PIN_SF"
                     /note="PIN (PilT N terminus) domain: Superfamily; cl28905"
                     /db_xref="CDD:475124"
     Region          178..806
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
     Region          821..896
                     /region_name="Rrp44_S1"
                     /note="S1 domain; pfam17215"
                     /db_xref="CDD:435792"
     CDS             1..994
                     /gene="DIS3L"
                     /gene_synonym="DIS3L1"
                     /coded_by="NM_001323948.2:273..3257"
                     /note="isoform 7 is encoded by transcript variant 13"
                     /db_xref="GeneID:115752"
                     /db_xref="HGNC:HGNC:28698"
                     /db_xref="MIM:614183"
ORIGIN      
        1 mgrsragspr elqasccrce adiacfaatd gkllssdvth yvipdwkvvq dyleilefpe
       61 lkgiifmqta cqavqhqrgr rsiynaavwy yhhcqdrmpi vmvtedeeai qqygsetegv
      121 fvitfknyld nfwpdlkaah elcdsilqsr rerenesqes hgkeypehlp levleagiks
      181 gryiqgilnv nkhraqieaf vrlqgasskd sdlvsdilih gmkarnrsih gdvvvvellp
      241 knewkgrtva lcendcddka sgespsepmp tgrvvgilqk nwrdyvvtfp skeevqsqgk
      301 naqkilvtpw dyripkiris tqqaetlqdf rvvvridswe stsvypnghf vrvlgrigdl
      361 egeiatilve nsisvipfse aqmcempvnt pespwkvspe eeqkrkdlrk shlvfsidpk
      421 gcedvddtls vrtlnngnle lgvhiadvth fvapnsyidi eartrattyy ladrrydmlp
      481 svlsadlcsl lggvdryavs imweldkasy eikkvwygrt iirsayklfy eaaqelldgn
      541 lsvvddipef kdldeksrqa kleelvwaig kltdiarhvr akrdgcgale legvevcvql
      601 ddkknihdli pkqplevhet vaecmilanh wvakkiwesf phqallrqhp pphqeffsel
      661 recakakgff idtrsnktla dsldnandph dpivnrllrs matqamsnal yfstgscaee
      721 efhhyglald kythftspir rysdivvhrl lmaaiskdkk meikgnlfsn kdleelcrhi
      781 nnrnqaaqhs qkqstelfqc myfkdkdpat eercisdgvi ysirtngvll fiprfgikga
      841 aylknkdglv iscgpdscse wkpgslqrfq nkitstttdg esvtfhlfdh vtvrisiqas
      901 rchsdtirle iisnkpykip ntelihqssp llkselvkev tksveeaqla qevkvniiqe
      961 eyqeyrqtkg rslytlleei rdlalldvsn nygi
//
LOCUS       NP_001265442             659 aa            linear   PRI 21-NOV-2025
DEFINITION  cullin-4A isoform 2 [Homo sapiens].
ACCESSION   NP_001265442
VERSION     NP_001265442.1
DBSOURCE    REFSEQ: accession NM_001278513.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Jia,Y., Huo,X., Wu,L., Zhang,H., Xu,W. and Leng,H.
  TITLE     circSNTB2 and CUL4A Induces Dysfunction of Nucleus Pulposus Cells
            by Competitively Binding miR-665
  JOURNAL   Biochem Genet 62 (2), 968-986 (2024)
   PUBMED   37507642
  REMARK    GeneRIF: circSNTB2 and CUL4A Induces Dysfunction of Nucleus
            Pulposus Cells by Competitively Binding miR-665.
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Tavlas,P., Nikou,S., Geramoutsou,C., Bosgana,P., Tsaniras,S.C.,
            Melachrinou,M., Maroulis,I. and Bravou,V.
  TITLE     CUL4A Ubiquitin Ligase Is an Independent Predictor of Overall
            Survival in Pancreatic Adenocarcinoma
  JOURNAL   Cancer Genomics Proteomics 21 (2), 166-177 (2024)
   PUBMED   38423594
  REMARK    GeneRIF: CUL4A Ubiquitin Ligase Is an Independent Predictor of
            Overall Survival in Pancreatic Adenocarcinoma.
REFERENCE   4  (residues 1 to 659)
  AUTHORS   Hu,Y., Zhang,R., Lu,S., Zhang,W., Wang,D., Ge,Y., Jiang,F., Qin,X.
            and Liu,Y.
  TITLE     S100 Calcium Binding Protein A16 Promotes Cell Proliferation by
            triggering LATS1 ubiquitin degradation mediated by CUL4A ligase to
            inhibit Hippo pathway in Glioma development
  JOURNAL   Int J Biol Sci 19 (7), 2034-2052 (2023)
   PUBMED   37151881
  REMARK    GeneRIF: S100 Calcium Binding Protein A16 Promotes Cell
            Proliferation by triggering LATS1 ubiquitin degradation mediated by
            CUL4A ligase to inhibit Hippo pathway in Glioma development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 659)
  AUTHORS   Ito,T., Ando,H., Suzuki,T., Ogura,T., Hotta,K., Imamura,Y.,
            Yamaguchi,Y. and Handa,H.
  TITLE     Identification of a primary target of thalidomide teratogenicity
  JOURNAL   Science 327 (5971), 1345-1350 (2010)
   PUBMED   20223979
REFERENCE   6  (residues 1 to 659)
  AUTHORS   Angers,S., Li,T., Yi,X., MacCoss,M.J., Moon,R.T. and Zheng,N.
  TITLE     Molecular architecture and assembly of the DDB1-CUL4A ubiquitin
            ligase machinery
  JOURNAL   Nature 443 (7111), 590-593 (2006)
   PUBMED   16964240
  REMARK    GeneRIF: crystallographic analyses of the virally hijacked form of
            the human DDB1-CUL4A-ROC1 machinery
REFERENCE   7  (residues 1 to 659)
  AUTHORS   Ohta,T., Michel,J.J., Schottelius,A.J. and Xiong,Y.
  TITLE     ROC1, a homolog of APC11, represents a family of cullin partners
            with an associated ubiquitin ligase activity
  JOURNAL   Mol Cell 3 (4), 535-541 (1999)
   PUBMED   10230407
REFERENCE   8  (residues 1 to 659)
  AUTHORS   Chen,L.C., Manjeshwar,S., Lu,Y., Moore,D., Ljung,B.M., Kuo,W.L.,
            Dairkee,S.H., Wernick,M., Collins,C. and Smith,H.S.
  TITLE     The human homologue for the Caenorhabditis elegans cul-4 gene is
            amplified and overexpressed in primary breast cancers
  JOURNAL   Cancer Res 58 (16), 3677-3683 (1998)
   PUBMED   9721878
REFERENCE   9  (residues 1 to 659)
  AUTHORS   Osaka,F., Kawasaki,H., Aida,N., Saeki,M., Chiba,T., Kawashima,S.,
            Tanaka,K. and Kato,S.
  TITLE     A new NEDD8-ligating system for cullin-4A
  JOURNAL   Genes Dev 12 (15), 2263-2268 (1998)
   PUBMED   9694792
REFERENCE   10 (residues 1 to 659)
  AUTHORS   Kipreos,E.T., Lander,L.E., Wing,J.P., He,W.W. and Hedgecock,E.M.
  TITLE     cul-1 is required for cell cycle exit in C. elegans and identifies
            a novel gene family
  JOURNAL   Cell 85 (6), 829-839 (1996)
   PUBMED   8681378
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL137002.19 and AL136221.38.
            
            Summary: CUL4A is the ubiquitin ligase component of a multimeric
            complex involved in the degradation of DNA damage-response proteins
            (Liu et al., 2009 [PubMed 19481525]).[supplied by OMIM, Oct 2009].
            
            Transcript Variant: This variant (3) utilizes an alternate 5'
            terminal exon, compared to variant 1, resulting in an isoform (2)
            with a shorter N-terminus. Variants 2, 3, 5, 6, and 7 all encode
            the same isoform (2).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314835.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..659
                     /product="cullin-4A isoform 2"
                     /note="CUL-4A"
                     /calculated_mol_wt=76690
     Region          2..560
                     /region_name="Cullin"
                     /note="Cullin family; pfam00888"
                     /db_xref="CDD:459983"
     Region          588..653
                     /region_name="Cullin_Nedd8"
                     /note="Cullin protein neddylation domain; smart00884"
                     /db_xref="CDD:214883"
     CDS             1..659
                     /gene="CUL4A"
                     /coded_by="NM_001278513.3:568..2547"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS9533.1"
                     /db_xref="GeneID:8451"
                     /db_xref="HGNC:HGNC:2554"
                     /db_xref="MIM:603137"
ORIGIN      
        1 mlykqlrqac edhvqaqilp fredsldsvl flkkintcwq dhcrqmimir siflfldrty
       61 vlqnstlpsi wdmglelfrt hiisdkmvqs ktidgillli erersgeavd rsllrsllgm
      121 lsdlqvykds felkfleetn clyaaegqrl mqerevpeyl nhvskrleee gdrvityldh
      181 stqkpliacv ekqllgehlt ailqkgldhl ldenrvpdla qmyqlfsrvr ggqqallqhw
      241 seyiktfgta ivinpekdkd mvqdlldfkd kvdhvievcf qknerfvnlm kesfetfink
      301 rpnkpaelia khvdsklrag nkeatdeele rtldkimilf rfihgkdvfe afykkdlakr
      361 llvgksasvd aeksmlsklk hecgaaftsk legmfkdmel skdimvhfkq hmqnqsdsgp
      421 idltvniltm gywptytpme vhltpemikl qevfkafylg khsgrklqwq ttlghavlka
      481 efkegkkefq vslfqtlvll mfnegdgfsf eeikmatgie dselrrtlqs lacgkarvli
      541 kspkgkeved gdkfifngef khklfrikin qiqmketvee qvsttervfq drqyqidaai
      601 vrimkmrktl ghnllvsely nqlkfpvkpg dlkkriesli drdymerdkd npnqyhyva
//
LOCUS       NP_000529                272 aa            linear   PRI 21-NOV-2025
DEFINITION  regulatory factor X-associated protein [Homo sapiens].
ACCESSION   NP_000529
VERSION     NP_000529.1
DBSOURCE    REFSEQ: accession NM_000538.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Ding,G., Xu,X., Li,D., Chen,Y., Wang,W., Ping,D., Jia,S. and Cao,L.
  TITLE     Fisetin inhibits proliferation of pancreatic adenocarcinoma by
            inducing DNA damage via RFXAP/KDM4A-dependent histone H3K36
            demethylation
  JOURNAL   Cell Death Dis 11 (10), 893 (2020)
   PUBMED   33093461
  REMARK    GeneRIF: Fisetin inhibits proliferation of pancreatic
            adenocarcinoma by inducing DNA damage via RFXAP/KDM4A-dependent
            histone H3K36 demethylation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Masternak,K., Barras,E., Zufferey,M., Conrad,B., Corthals,G.,
            Aebersold,R., Sanchez,J.C., Hochstrasser,D.F., Mach,B. and Reith,W.
  TITLE     A gene encoding a novel RFX-associated transactivator is mutated in
            the majority of MHC class II deficiency patients
  JOURNAL   Nat Genet 20 (3), 273-277 (1998)
   PUBMED   9806546
REFERENCE   7  (residues 1 to 272)
  AUTHORS   Villard,J., Lisowska-Grospierre,B., van den Elsen,P., Fischer,A.,
            Reith,W. and Mach,B.
  TITLE     Mutation of RFXAP, a regulator of MHC class II genes, in primary
            MHC class II deficiency
  JOURNAL   N Engl J Med 337 (11), 748-753 (1997)
   PUBMED   9287230
REFERENCE   8  (residues 1 to 272)
  AUTHORS   Durand,B., Sperisen,P., Emery,P., Barras,E., Zufferey,M., Mach,B.
            and Reith,W.
  TITLE     RFXAP, a novel subunit of the RFX DNA binding complex is mutated in
            MHC class II deficiency
  JOURNAL   EMBO J 16 (5), 1045-1055 (1997)
   PUBMED   9118943
REFERENCE   9  (residues 1 to 272)
  AUTHORS   Mach,B., Steimle,V., Martinez-Soria,E. and Reith,W.
  TITLE     Regulation of MHC class II genes: lessons from a disease
  JOURNAL   Annu Rev Immunol 14, 301-331 (1996)
   PUBMED   8717517
  REMARK    Review article
REFERENCE   10 (residues 1 to 272)
  AUTHORS   Reith,W., Siegrist,C.A., Durand,B., Barras,E. and Mach,B.
  TITLE     Function of major histocompatibility complex class II promoters
            requires cooperative binding between factors RFX and NF-Y
  JOURNAL   Proc Natl Acad Sci U S A 91 (2), 554-558 (1994)
   PUBMED   8290561
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI823132.1, BC026088.1 and
            AL159973.16.
            
            Summary: Major histocompatibility (MHC) class II molecules are
            transmembrane proteins that have a central role in development and
            control of the immune system. The protein encoded by this gene,
            along with regulatory factor X-associated ankyrin-containing
            protein and regulatory factor-5, forms a complex that binds to the
            X box motif of certain MHC class II gene promoters and activates
            their transcription. Once bound to the promoter, this complex
            associates with the non-DNA-binding factor MHC class II
            transactivator, which controls the cell type specificity and
            inducibility of MHC class II gene expression. Mutations in this
            gene have been linked to bare lymphocyte syndrome type II,
            complementation group D. Transcript variants utilizing different
            polyA signals have been found for this gene. [provided by RefSeq,
            Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because transcript sequence consistent with
            the reference genome assembly was not available for all regions of
            the RefSeq transcript. The extent of this transcript is supported
            by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC026088.1, SRR11853558.6302.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000255476.3/ ENSP00000255476.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q13.3"
     Protein         1..272
                     /product="regulatory factor X-associated protein"
                     /note="RFX-associated protein; RFX DNA-binding complex 36
                     kDa subunit"
                     /calculated_mol_wt=28101
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00287.1)"
     Region          74..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00287.1)"
     Region          140..>243
                     /region_name="RFXA_RFXANK_bdg"
                     /note="Regulatory factor X-associated C-terminal binding
                     domain; pfam15289"
                     /db_xref="CDD:434600"
     Region          163..178
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00287.1)"
     Region          175..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00287.1)"
     Region          214..270
                     /region_name="C-terminal domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00287.1)"
     CDS             1..272
                     /gene="RFXAP"
                     /gene_synonym="MHC2D4"
                     /coded_by="NM_000538.4:137..955"
                     /db_xref="CCDS:CCDS9359.1"
                     /db_xref="GeneID:5994"
                     /db_xref="HGNC:HGNC:9988"
                     /db_xref="MIM:601861"
ORIGIN      
        1 meaqgvaega gpgaasgvph paalapaaap tlapasvaaa asqftllvmq pcagqdeaaa
       61 pggsvgagkp vrylcegagd geeeagedea dlldtsdppg ggesaasled ledeethsgg
      121 egssggarrr gsgggsmskt ctyegcsett sqvakqrkpw mckkhrnkmy kdkykkkksd
      181 qalncggtas tgsagnvkle esadnilsiv kqrtgsfgdr parptlleqv lnqkrlsllr
      241 spevvqflqk qqqllnqqvl eqrqqqfpgt sm
//
LOCUS       NP_671710                216 aa            linear   PRI 21-NOV-2025
DEFINITION  Kv channel-interacting protein 4 isoform 2 [Homo sapiens].
ACCESSION   NP_671710
VERSION     NP_671710.1
DBSOURCE    REFSEQ: accession NM_147181.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Mosley,J.D., Shaffer,C.M., Van Driest,S.L., Weeke,P.E., Wells,Q.S.,
            Karnes,J.H., Velez Edwards,D.R., Wei,W.Q., Teixeira,P.L.,
            Bastarache,L., Crawford,D.C., Li,R., Manolio,T.A., Bottinger,E.P.,
            McCarty,C.A., Linneman,J.G., Brilliant,M.H., Pacheco,J.A.,
            Thompson,W., Chisholm,R.L., Jarvik,G.P., Crosslin,D.R.,
            Carrell,D.S., Baldwin,E., Ralston,J., Larson,E.B., Grafton,J.,
            Scrol,A., Jouni,H., Kullo,I.J., Tromp,G., Borthwick,K.M.,
            Kuivaniemi,H., Carey,D.J., Ritchie,M.D., Bradford,Y., Verma,S.S.,
            Chute,C.G., Veluchamy,A., Siddiqui,M.K., Palmer,C.N., Doney,A.,
            MahmoudPour,S.H., Maitland-van der Zee,A.H., Morris,A.D.,
            Denny,J.C. and Roden,D.M.
  TITLE     A genome-wide association study identifies variants in KCNIP4
            associated with ACE inhibitor-induced cough
  JOURNAL   Pharmacogenomics J 16 (3), 231-237 (2016)
   PUBMED   26169577
  REMARK    GeneRIF: Results indicate that SNPs in KCNIP4 may modulate ACE
            inhibitor-induced cough risk.
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 216)
  AUTHORS   Kitazawa,M., Kubo,Y. and Nakajo,K.
  TITLE     The stoichiometry and biophysical properties of the Kv4 potassium
            channel complex with K+ channel-interacting protein (KChIP)
            subunits are variable, depending on the relative expression level
  JOURNAL   J Biol Chem 289 (25), 17597-17609 (2014)
   PUBMED   24811166
  REMARK    GeneRIF: Subunit counting by single-molecule imaging revealed that
            the bound number of KChIP4 in each Kv4.2.KChIP4 complex was
            dependent on the expression level of KChIP4.
REFERENCE   6  (residues 1 to 216)
  AUTHORS   Bonne,A., Vreede,L., Kuiper,R.P., Bodmer,D., Jansen,C., Eleveld,M.,
            van Erp,F., Arkesteijn,G., Hoogerbrugge,N., van Ravenswaaij,C.,
            Schoenmakers,E.F. and Geurts van Kessel,A.
  TITLE     Mapping of constitutional translocation breakpoints in renal cell
            cancer patients: identification of KCNIP4 as a candidate gene
  JOURNAL   Cancer Genet Cytogenet 179 (1), 11-18 (2007)
   PUBMED   17981209
  REMARK    GeneRIF: Mutation of KCNIP4 is associated with renal cell
            carcinoma.
REFERENCE   7  (residues 1 to 216)
  AUTHORS   Chen,C.P., Lee,L. and Chang,L.S.
  TITLE     Effects of metal-binding properties of human Kv channel-interacting
            proteins on their molecular structure and binding with Kv4.2
            channel
  JOURNAL   Protein J 25 (5), 345-351 (2006)
   PUBMED   16951992
  REMARK    GeneRIF: The conformational change with metal-bound KChIP4.1 is
            crucial for its interaction with Kv channel but not for KChIP2.2,
            and that the Mg2+- and Ca2+-binding properties of KChIP2.2 and
            KChIP4.1 have different effects on their molecular structure.
REFERENCE   8  (residues 1 to 216)
  AUTHORS   Pruunsild,P. and Timmusk,T.
  TITLE     Structure, alternative splicing, and expression of the human and
            mouse KCNIP gene family
  JOURNAL   Genomics 86 (5), 581-593 (2005)
   PUBMED   16112838
REFERENCE   9  (residues 1 to 216)
  AUTHORS   Morohashi,Y., Hatano,N., Ohya,S., Takikawa,R., Watabiki,T.,
            Takasugi,N., Imaizumi,Y., Tomita,T. and Iwatsubo,T.
  TITLE     Molecular cloning and characterization of CALP/KChIP4, a novel
            EF-hand protein interacting with presenilin 2 and voltage-gated
            potassium channel subunit Kv4
  JOURNAL   J Biol Chem 277 (17), 14965-14975 (2002)
   PUBMED   11847232
  REMARK    GeneRIF: cloning and investigation of interaction with presenilin 2
            and voltage-gated potassium channel subunit Kv4
REFERENCE   10 (residues 1 to 216)
  AUTHORS   Holmqvist,M.H., Cao,J., Hernandez-Pineda,R., Jacobson,M.D.,
            Carroll,K.I., Sung,M.A., Betty,M., Ge,P., Gilbride,K.J.,
            Brown,M.E., Jurman,M.E., Lawson,D., Silos-Santiago,I., Xie,Y.,
            Covarrubias,M., Rhodes,K.J., Distefano,P.S. and An,W.F.
  TITLE     Elimination of fast inactivation in Kv4 A-type potassium channels
            by an auxiliary subunit domain
  JOURNAL   Proc Natl Acad Sci U S A 99 (2), 1035-1040 (2002)
   PUBMED   11805342
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC113606.3, BI596848.1,
            AF367024.1, AC104065.3 and BX648990.1.
            
            Summary: This gene encodes a member of the family of voltage-gated
            potassium (Kv) channel-interacting proteins (KCNIPs), which belong
            to the recoverin branch of the EF-hand superfamily. Members of the
            KCNIP family are small calcium binding proteins. They all have
            EF-hand-like domains, and differ from each other in the N-terminus.
            They are integral subunit components of native Kv4 channel
            complexes. They may regulate A-type currents, and hence neuronal
            excitability, in response to changes in intracellular calcium. This
            protein member also interacts with presenilin. Multiple
            alternatively spliced transcript variants encoding distinct
            isoforms have been identified for this gene. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            coding region, as compared to variant 1. Isoform 2, also known as
            KCHIP4.2, is thus missing an internal segment, as compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK289661.1, SRR3476690.804351.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.31-p15.2"
     Protein         1..216
                     /product="Kv channel-interacting protein 4 isoform 2"
                     /note="calsenilin-like protein; a-type potassium channel
                     modulatory protein 4; Kv channel interacting protein 4"
                     /calculated_mol_wt=24877
     Region          65..112
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cl08302"
                     /db_xref="CDD:415501"
     Region          <94..201
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..216
                     /gene="KCNIP4"
                     /gene_synonym="CALP; KCHIP4"
                     /coded_by="NM_147181.4:142..792"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43215.1"
                     /db_xref="GeneID:80333"
                     /db_xref="HGNC:HGNC:30083"
                     /db_xref="MIM:608182"
ORIGIN      
        1 mnvrrvesis aqleeasstg dsvedelema tvrhrpeale lleaqskftk kelqilyrgf
       61 knecpsgvvn eetfkeiysq ffpqgdstty ahflfnafdt dhngavsfed fikglsillr
      121 gtvqeklnwa fnlydinkdg yitkeemldi mkaiydmmgk ctypvlkeda prqhvetffq
      181 kmdknkdgvv tidefiescq kdenimrsmq lfenvi
//
LOCUS       NP_001341964             301 aa            linear   PRI 21-NOV-2025
DEFINITION  5'-AMP-activated protein kinase catalytic subunit alpha-1 isoform 6
            [Homo sapiens].
ACCESSION   NP_001341964 XP_006714545
VERSION     NP_001341964.1
DBSOURCE    REFSEQ: accession NM_001355035.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Yang,J.S., Morris,A.J., Kamizaki,K., Chen,J., Stark,J.,
            Oldham,W.M., Nakamura,T., Mishima,E., Loscalzo,J., Minami,Y.,
            Conrad,M., Henry,W.S. and Hsu,V.W.
  TITLE     ALDH7A1 protects against ferroptosis by generating membrane NADH
            and regulating FSP1
  JOURNAL   Cell 188 (10), 2569-2585 (2025)
   PUBMED   40233740
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Santana,C.V.N., Magno,L.A.V., Ramos,A.V., Rios,M.A., Sandrim,V.C.,
            De Marco,L.A., de Miranda,D.M. and Romano-Silva,M.A.
  TITLE     Genetic Variations in AMPK, FOXO3A, and POMC Increase the Risk of
            Extreme Obesity
  JOURNAL   J Obes 2024, 3813621 (2024)
   PUBMED   39484290
  REMARK    GeneRIF: Genetic Variations in AMPK, FOXO3A, and POMC Increase the
            Risk of Extreme Obesity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Jeon,H.Y., Lee,A.J., Moon,C.H. and Ha,K.S.
  TITLE     Regulation of AMPK and GAPDH by Transglutaminase 2 Plays a Pivotal
            Role in Microvascular Leakage in Diabetic Retinas
  JOURNAL   Diabetes 73 (10), 1756-1766 (2024)
   PUBMED   39024127
  REMARK    GeneRIF: Regulation of AMPK and GAPDH by Transglutaminase 2 Plays a
            Pivotal Role in Microvascular Leakage in Diabetic Retinas.
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Kong,M., Chen,Z., Lin,Z., Yin,P. and Zhao,Q.
  TITLE     SIGMAR1 targets AMPK/ULK1 pathway to inhibit SH-SY5Y cell apoptosis
            by regulating endoplasmic reticulum stress and autophagy
  JOURNAL   Funct Integr Genomics 24 (4), 134 (2024)
   PUBMED   39107544
  REMARK    GeneRIF: SIGMAR1 targets AMPK/ULK1 pathway to inhibit SH-SY5Y cell
            apoptosis by regulating endoplasmic reticulum stress and autophagy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Vladimirov,S.N., Ivanov,A.V., Karpova,G.G., Musolyamov,A.K.,
            Egorov,T.A., Thiede,B., Wittmann-Liebold,B. and Otto,A.
  TITLE     Characterization of the human small-ribosomal-subunit proteins by
            N-terminal and internal sequencing, and mass spectrometry
  JOURNAL   Eur J Biochem 239 (1), 144-149 (1996)
   PUBMED   8706699
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Woods,A., Cheung,P.C., Smith,F.C., Davison,M.D., Scott,J.,
            Beri,R.K. and Carling,D.
  TITLE     Characterization of AMP-activated protein kinase beta and gamma
            subunits. Assembly of the heterotrimeric complex in vitro
  JOURNAL   J Biol Chem 271 (17), 10282-10290 (1996)
   PUBMED   8626596
REFERENCE   8  (residues 1 to 301)
  AUTHORS   Stapleton,D., Mitchelhill,K.I., Gao,G., Widmer,J., Michell,B.J.,
            Teh,T., House,C.M., Fernandez,C.S., Cox,T., Witters,L.A. and
            Kemp,B.E.
  TITLE     Mammalian AMP-activated protein kinase subfamily
  JOURNAL   J Biol Chem 271 (2), 611-614 (1996)
   PUBMED   8557660
REFERENCE   9  (residues 1 to 301)
  AUTHORS   Grove,J.R., Banerjee,P., Balasubramanyam,A., Coffer,P.J.,
            Price,D.J., Avruch,J. and Woodgett,J.R.
  TITLE     Cloning and expression of two human p70 S6 kinase polypeptides
            differing only at their amino termini
  JOURNAL   Mol Cell Biol 11 (11), 5541-5550 (1991)
   PUBMED   1922062
REFERENCE   10 (residues 1 to 301)
  AUTHORS   Munday,M.R., Campbell,D.G., Carling,D. and Hardie,D.G.
  TITLE     Identification by amino acid sequencing of three major regulatory
            phosphorylation sites on rat acetyl-CoA carboxylase
  JOURNAL   Eur J Biochem 175 (2), 331-338 (1988)
   PUBMED   2900138
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008810.8.
            
            On Sep 2, 2017 this sequence version replaced XP_006714545.1.
            
            Summary: The protein encoded by this gene belongs to the ser/thr
            protein kinase family. It is the catalytic subunit of the
            5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular
            energy sensor conserved in all eukaryotic cells. The kinase
            activity of AMPK is activated by the stimuli that increase the
            cellular AMP/ATP ratio. AMPK regulates the activities of a number
            of key metabolic enzymes through phosphorylation. It protects cells
            from stresses that cause ATP depletion by switching off
            ATP-consuming biosynthetic pathways. Alternatively spliced
            transcript variants encoding distinct isoforms have been observed.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (6), as well as variants 7 and 8,
            encodes isoform 6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.9618.1,
                                           SRR1660809.166412.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.1"
     Protein         1..301
                     /product="5'-AMP-activated protein kinase catalytic
                     subunit alpha-1 isoform 6"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.11.26"
                     /EC_number="2.7.11.31"
                     /note="5'-AMP-activated protein kinase, catalytic alpha-1
                     chain; AMP -activate kinase alpha 1 subunit; AMP-activated
                     protein kinase, catalytic, alpha-1; protein kinase,
                     AMP-activated, alpha 1 catalytic subunit; 5'-AMP-activated
                     protein kinase catalytic subunit alpha-1; AMPK, alpha, 1;
                     AMPK subunit alpha-1; tau-protein kinase PRKAA1; ACACA
                     kinase; HMGCR kinase; acetyl-CoA carboxylase kinase;
                     hydroxymethylglutaryl-CoA reductase kinase"
                     /calculated_mol_wt=34599
     Region          <1..21
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          38..102
                     /region_name="UBA_AID_AAPK1"
                     /note="UBA-like autoinhibitory domain (AID) found in
                     vertebrate 5'-AMP-activated protein kinase catalytic
                     subunit alpha-1 (AMPKalpha-1); cd14403"
                     /db_xref="CDD:270586"
     Region          146..299
                     /region_name="AMPKA1_C"
                     /note="C-terminal regulatory domain of 5'-AMP-activated
                     protein kinase (AMPK) alpha 1 catalytic subunit; cd12199"
                     /db_xref="CDD:213384"
     Site            order(146..152,154,159,181..183,203..207,212,215..218,220,
                     285,288..290,292..293,297)
                     /site_type="other"
                     /note="beta subunit interface [polypeptide binding]"
                     /db_xref="CDD:213384"
     Site            order(146,191,193,283..284,286..287,290)
                     /site_type="other"
                     /note="gamma subunit interface [polypeptide binding]"
                     /db_xref="CDD:213384"
     CDS             1..301
                     /gene="PRKAA1"
                     /gene_synonym="AMPK; AMPK alpha 1; AMPKa1"
                     /coded_by="NM_001355035.2:675..1580"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:5562"
                     /db_xref="HGNC:HGNC:9376"
                     /db_xref="MIM:602739"
ORIGIN      
        1 mlqvdpmkra tikdirehew fkqdlpkylf pedpsysstm iddealkevc ekfecseeev
       61 lsclynrnhq dplavayhli idnrrimnea kdfylatspp dsflddhhlt rphpervpfl
      121 vaetprarht ldelnpqksk hqgvrkakwh lgirsqsrpn dimaevcrai kqldyewkvv
      181 npyylrvrrk npvtstyskm slqlyqvdsr tylldfrsid deiteaksgt atpqrsgsvs
      241 nyrscqrsds daeaqgksse vsltssvtsl dsspvdltpr pgshtieffe mcanlikila
      301 q
//
LOCUS       NP_001230208             576 aa            linear   PRI 21-NOV-2025
DEFINITION  malonate--CoA ligase ACSF3, mitochondrial isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001230208
VERSION     NP_001230208.1
DBSOURCE    REFSEQ: accession NM_001243279.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Liu,Y., Chen,S.H., Jin,X. and Li,Y.M.
  TITLE     Analysis of differentially expressed genes and microRNAs in
            alcoholic liver disease
  JOURNAL   Int J Mol Med 31 (3), 547-554 (2013)
   PUBMED   23337955
  REMARK    GeneRIF: ACSF3 was significantly upregulated, and was involved in
            fatty acid and lipid metabolism and accelerated liver injury in
            alcoholic liver disease.
REFERENCE   5  (residues 1 to 576)
  AUTHORS   Salaverria,I., Akasaka,T., Gesk,S., Szczepanowski,M., Burkhardt,B.,
            Harder,L., Damm-Welk,C., Oschlies,I., Klapper,W., Dyer,M.J. and
            Siebert,R.
  TITLE     The CBFA2T3/ACSF3 locus is recurrently involved in IGH chromosomal
            translocation t(14;16)(q32;q24) in pediatric B-cell lymphoma with
            germinal center phenotype
  JOURNAL   Genes Chromosomes Cancer 51 (4), 338-343 (2012)
   PUBMED   22420028
  REMARK    GeneRIF: data indicate that the CBFA2T3/ACSF3 locus is a novel
            recurrent oncogenic target of immunoglobulin heavy chain
            translocations, which might contribute to the pathogenesis of
            pediatric GC-derived B-cell lymphoma.
REFERENCE   6  (residues 1 to 576)
  AUTHORS   Witkowski,A., Thweatt,J. and Smith,S.
  TITLE     Mammalian ACSF3 protein is a malonyl-CoA synthetase that supplies
            the chain extender units for mitochondrial fatty acid synthesis
  JOURNAL   J Biol Chem 286 (39), 33729-33736 (2011)
   PUBMED   21846720
  REMARK    GeneRIF: Mammalian ACSF3 protein is a malonyl-CoA synthetase that
            supplies the chain extender units for mitochondrial fatty acid
            synthesis.
REFERENCE   7  (residues 1 to 576)
  AUTHORS   Alfares,A., Nunez,L.D., Al-Thihli,K., Mitchell,J., Melancon,S.,
            Anastasio,N., Ha,K.C., Majewski,J., Rosenblatt,D.S. and
            Braverman,N.
  TITLE     Combined malonic and methylmalonic aciduria: exome sequencing
            reveals mutations in the ACSF3 gene in patients with a non-classic
            phenotype
  JOURNAL   J Med Genet 48 (9), 602-605 (2011)
   PUBMED   21785126
  REMARK    GeneRIF: ACSF3 is a candidate gene for non-classical CMAMMA
            observed in our patients.
REFERENCE   8  (residues 1 to 576)
  AUTHORS   Sloan,J.L., Johnston,J.J., Manoli,I., Chandler,R.J., Krause,C.,
            Carrillo-Carrasco,N., Chandrasekaran,S.D., Sysol,J.R., O'Brien,K.,
            Hauser,N.S., Sapp,J.C., Dorward,H.M., Huizing,M., Barshop,B.A.,
            Berry,S.A., James,P.M., Champaigne,N.L., de Lonlay,P.,
            Valayannopoulos,V., Geschwind,M.D., Gavrilov,D.K., Nyhan,W.L.,
            Biesecker,L.G. and Venditti,C.P.
  CONSRTM   NIH Intramural Sequencing Center Group
  TITLE     Exome sequencing identifies ACSF3 as a cause of combined malonic
            and methylmalonic aciduria
  JOURNAL   Nat Genet 43 (9), 883-886 (2011)
   PUBMED   21841779
  REMARK    GeneRIF: mutations in ACSF3, encoding a putative methylmalonyl-CoA
            and malonyl-CoA synthetase, were identified as a cause of combined
            malonic and methylmalonic aciduria.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 576)
  AUTHORS   Chen,H., Kim,H.U., Weng,H. and Browse,J.
  TITLE     Malonyl-CoA synthetase, encoded by ACYL ACTIVATING ENZYME13, is
            essential for growth and development of Arabidopsis
  JOURNAL   Plant Cell 23 (6), 2247-2262 (2011)
   PUBMED   21642549
REFERENCE   10 (residues 1 to 576)
  AUTHORS   Watkins,P.A., Maiguel,D., Jia,Z. and Pevsner,J.
  TITLE     Evidence for 26 distinct acyl-coenzyme A synthetase genes in the
            human genome
  JOURNAL   J Lipid Res 48 (12), 2736-2750 (2007)
   PUBMED   17762044
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM148793.1, BC028399.1,
            AC135782.4 and AC009113.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the acyl-CoA synthetase
            family of enzymes that activate fatty acids by catalyzing the
            formation of a thioester linkage between fatty acids and coenzyme
            A. The encoded protein is localized to mitochondria, has high
            specificity for malonate and methylmalonate and possesses
            malonyl-CoA synthetase activity. Mutations in this gene are a cause
            of combined malonic and methylmalonic aciduria. Alternatively
            spliced transcript variants have been observed for this gene.
            [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 4 encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.831849.1,
                                           SRR18074969.2679710.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000614302.5/
                                                  ENSP00000479130.1
            RefSeq Select criteria             :: based on manual assertion,
                                                  conservation, expression,
                                                  longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..576
                     /product="malonate--CoA ligase ACSF3, mitochondrial
                     isoform 1 precursor"
                     /EC_number="6.2.1.76"
                     /note="acyl-CoA synthetase family member 3, mitochondrial;
                     malonyl-CoA synthetase; malonate--CoA ligase ACSF3,
                     mitochondrial"
                     /calculated_mol_wt=54868
     transit_peptide 1..83
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q4G176.3)"
                     /calculated_mol_wt=9281
     Region          55..571
                     /region_name="MCS"
                     /note="Malonyl-CoA synthetase (MCS); cd05941"
                     /db_xref="CDD:341264"
     mat_peptide     84..576
                     /product="Malonate--CoA ligase ACSF3, mitochondrial.
                     /id=PRO_0000315800"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G176.3)"
                     /calculated_mol_wt=54868
     Site            order(199,202..207,209..210)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341264"
     Site            order(202,242..243,246..248,293,295,299,332..334,353..358,
                     362,378,457,468,476,478,480,483,512,548)
                     /site_type="active"
                     /db_xref="CDD:341264"
     Site            order(202,332..334,353..358,378,457,468,476,478,483)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341264"
     Site            order(242..243,246..248,293,295,299,332,354,356..358,362,
                     478,480..482,512,548)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341264"
     CDS             1..576
                     /gene="ACSF3"
                     /coded_by="NM_001243279.3:339..2069"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS10974.1"
                     /db_xref="GeneID:197322"
                     /db_xref="HGNC:HGNC:27288"
                     /db_xref="MIM:614245"
ORIGIN      
        1 mlphvvltfr rlgcalascr laparhrgsg llhtapvars drsapvftra lafgdrialv
       61 dqhgrhtyre lysrslrlsq eicrlcgcvg gdlreervsf lcandasyvv aqwaswmsgg
      121 vavplyrkhp aaqleyvicd sqssvvlasq eylellspvv rklgvpllpl tpaiytgave
      181 epaevpvpeq gwrnkgamii ytsgttgrpk gvlsthqnir avvtglvhkw awtkddvilh
      241 vlplhhvhgv vnallcplwv gatcvmmpef spqqvwekfl ssetprinvf mavptiytkl
      301 meyydrhftq phaqdflrav ceekirlmvs gsaalplpvl ekwknitght llerygmtei
      361 gmalsgpltt avrlpgsvgt plpgvqvriv senpqreacs ytihaegder gtkvtpgfee
      421 kegellvrgp svfreywnkp eetksaftld gwfktgdtvv fkdgqywirg rtsvdiiktg
      481 gykvsaleve whllahpsit dvavigvpdm twgqrvtavv tlreghslsh relkewarnv
      541 lapyavpsel vlveeiprnq mgkidkkali rhfhps
//
LOCUS       NP_001229345             520 aa            linear   PRI 21-NOV-2025
DEFINITION  WD repeat-containing protein 20 isoform 6 [Homo sapiens].
ACCESSION   NP_001229345
VERSION     NP_001229345.1
DBSOURCE    REFSEQ: accession NM_001242416.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Jiang,L., Qi,X., Lai,M., Zhou,J., Yuan,M., You,J., Liu,Q., Pan,J.,
            Zhao,L., Ying,M., Ji,J., Li,K., Zhang,Y., Pan,W., He,Q., Yang,B.
            and Cao,J.
  TITLE     WDR20 prevents hepatocellular carcinoma senescence by orchestrating
            the simultaneous USP12/46-mediated deubiquitination of c-Myc
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2407904121 (2024)
   PUBMED   39432777
  REMARK    GeneRIF: WDR20 prevents hepatocellular carcinoma senescence by
            orchestrating the simultaneous USP12/46-mediated deubiquitination
            of c-Myc.
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Ng,V.H., Spencer,Z., Neitzel,L.R., Nayak,A., Loberg,M.A., Shen,C.,
            Kassel,S.N., Kroh,H.K., An,Z., Anthony,C.C., Bryant,J.M.,
            Lawson,A., Goldsmith,L., Benchabane,H., Hansen,A.G., Li,J.,
            D'Souza,S., Lebensohn,A.M., Rohatgi,R., Weiss,W.A., Weiss,V.L.,
            Williams,C., Hong,C.C., Robbins,D.J., Ahmed,Y. and Lee,E.
  TITLE     The USP46 complex deubiquitylates LRP6 to promote Wnt/beta-catenin
            signaling
  JOURNAL   Nat Commun 14 (1), 6173 (2023)
   PUBMED   37798301
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Olazabal-Herrero,A., Bilbao-Arribas,M., Carlevaris,O., Sendino,M.,
            Varela-Martinez,E., Jugo,B.M., Berra,E. and Rodriguez,J.A.
  TITLE     The dystrophia myotonica WD repeat-containing protein DMWD and
            WDR20 differentially regulate USP12 deubiquitinase
  JOURNAL   FEBS J 288 (20), 5943-5963 (2021)
   PUBMED   33844468
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Dahlberg,C.L. and Juo,P.
  TITLE     The WD40-repeat proteins WDR-20 and WDR-48 bind and activate the
            deubiquitinating enzyme USP-46 to promote the abundance of the
            glutamate receptor GLR-1 in the ventral nerve cord of
            Caenorhabditis elegans
  JOURNAL   J Biol Chem 289 (6), 3444-3456 (2014)
   PUBMED   24356955
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Kee,Y., Yang,K., Cohn,M.A., Haas,W., Gygi,S.P. and D'Andrea,A.D.
  TITLE     WDR20 regulates activity of the USP12 x UAF1 deubiquitinating
            enzyme complex
  JOURNAL   J Biol Chem 285 (15), 11252-11257 (2010)
   PUBMED   20147737
  REMARK    GeneRIF: WDR20 serves as a stimulatory subunit for preserving and
            regulating the activity of the subset of the UAF1 x USP12 complexes
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Smith,T.F.
  TITLE     Diversity of WD-repeat proteins
  JOURNAL   Subcell Biochem 48, 20-30 (2008)
   PUBMED   18925368
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK225852.1, AL832242.1 and
            AF327354.1.
            
            Summary: This gene encodes a WD repeat-containing protein that
            functions to preserve and regulate the activity of the USP12-UAF1
            deubiquitinating enzyme complex. Multiple alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Jun 2011].
            
            Transcript Variant: This variant (6) lacks an alternate in-frame
            exon in the central coding region, compared to variant 1, resulting
            in an isoform (6) that is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.19218.1,
                                           SRR1803617.91418.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.31"
     Protein         1..520
                     /product="WD repeat-containing protein 20 isoform 6"
                     /note="WD repeat-containing protein 20"
                     /calculated_mol_wt=57033
     Region          92..157
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <147..253
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          162..198
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          205..238
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..520
                     /gene="WDR20"
                     /gene_synonym="Bun107; DMR"
                     /coded_by="NM_001242416.2:28..1590"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS55945.1"
                     /db_xref="GeneID:91833"
                     /db_xref="HGNC:HGNC:19667"
                     /db_xref="MIM:617741"
ORIGIN      
        1 mategggkem neiktqfttr eglykllphs eysrpnrvpf nsqgsnpvrv sfvnlndqsg
       61 ngdrlcfnvg relyfyiykg vrkrlidksr vtcvkwvpgs eslflvahss gnmylynveh
      121 tcgttaphyq llkqgesfav htckskstrn pllkwtvgeg alnefafspd gkflacvsqd
      181 gflrvfnfds velhgtmksy fggllcvcws pdgkyivtgg eddlvtvwsf vdcrviargh
      241 ghkswvsvva fdpyttsvee gdpmefsgsd edfqdllhfg rdranstqsr lskrnstdsr
      301 pvsvtyrfgs vgqdtqlclw dltedilfph qplsrartht nvmnatsppa gsngnsvttp
      361 gnsvppplpr snslphsavs nagskssvmd gaiasgvskf atlslhdrke rhhekdhkrn
      421 hsmghissks sdklnlvtkt ktdpaktlgt plcprmedvp lleplickki aherltvlif
      481 ledcivtacq egfictwgrp gkvgslssps qasspggtvv
//
LOCUS       NP_851825                508 aa            linear   PRI 21-NOV-2025
DEFINITION  WD repeat-containing protein 20 isoform 3 [Homo sapiens].
ACCESSION   NP_851825
VERSION     NP_851825.1
DBSOURCE    REFSEQ: accession NM_181308.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Jiang,L., Qi,X., Lai,M., Zhou,J., Yuan,M., You,J., Liu,Q., Pan,J.,
            Zhao,L., Ying,M., Ji,J., Li,K., Zhang,Y., Pan,W., He,Q., Yang,B.
            and Cao,J.
  TITLE     WDR20 prevents hepatocellular carcinoma senescence by orchestrating
            the simultaneous USP12/46-mediated deubiquitination of c-Myc
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2407904121 (2024)
   PUBMED   39432777
  REMARK    GeneRIF: WDR20 prevents hepatocellular carcinoma senescence by
            orchestrating the simultaneous USP12/46-mediated deubiquitination
            of c-Myc.
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Ng,V.H., Spencer,Z., Neitzel,L.R., Nayak,A., Loberg,M.A., Shen,C.,
            Kassel,S.N., Kroh,H.K., An,Z., Anthony,C.C., Bryant,J.M.,
            Lawson,A., Goldsmith,L., Benchabane,H., Hansen,A.G., Li,J.,
            D'Souza,S., Lebensohn,A.M., Rohatgi,R., Weiss,W.A., Weiss,V.L.,
            Williams,C., Hong,C.C., Robbins,D.J., Ahmed,Y. and Lee,E.
  TITLE     The USP46 complex deubiquitylates LRP6 to promote Wnt/beta-catenin
            signaling
  JOURNAL   Nat Commun 14 (1), 6173 (2023)
   PUBMED   37798301
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Olazabal-Herrero,A., Bilbao-Arribas,M., Carlevaris,O., Sendino,M.,
            Varela-Martinez,E., Jugo,B.M., Berra,E. and Rodriguez,J.A.
  TITLE     The dystrophia myotonica WD repeat-containing protein DMWD and
            WDR20 differentially regulate USP12 deubiquitinase
  JOURNAL   FEBS J 288 (20), 5943-5963 (2021)
   PUBMED   33844468
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Dahlberg,C.L. and Juo,P.
  TITLE     The WD40-repeat proteins WDR-20 and WDR-48 bind and activate the
            deubiquitinating enzyme USP-46 to promote the abundance of the
            glutamate receptor GLR-1 in the ventral nerve cord of
            Caenorhabditis elegans
  JOURNAL   J Biol Chem 289 (6), 3444-3456 (2014)
   PUBMED   24356955
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Kee,Y., Yang,K., Cohn,M.A., Haas,W., Gygi,S.P. and D'Andrea,A.D.
  TITLE     WDR20 regulates activity of the USP12 x UAF1 deubiquitinating
            enzyme complex
  JOURNAL   J Biol Chem 285 (15), 11252-11257 (2010)
   PUBMED   20147737
  REMARK    GeneRIF: WDR20 serves as a stimulatory subunit for preserving and
            regulating the activity of the subset of the UAF1 x USP12 complexes
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   10 (residues 1 to 508)
  AUTHORS   Smith,T.F.
  TITLE     Diversity of WD-repeat proteins
  JOURNAL   Subcell Biochem 48, 20-30 (2008)
   PUBMED   18925368
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP363522.1, BX248274.1 and
            BC028387.2.
            
            Summary: This gene encodes a WD repeat-containing protein that
            functions to preserve and regulate the activity of the USP12-UAF1
            deubiquitinating enzyme complex. Multiple alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Jun 2011].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon in the central coding region and differs in the 3' coding
            region and 3' UTR, compared to variant 1. The encoded isoform (3)
            has a distinct C-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.33433.1,
                                           SRR1803611.278182.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.31"
     Protein         1..508
                     /product="WD repeat-containing protein 20 isoform 3"
                     /note="WD repeat-containing protein 20"
                     /calculated_mol_wt=56078
     Region          92..157
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <147..253
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          162..198
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          205..238
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..508
                     /gene="WDR20"
                     /gene_synonym="Bun107; DMR"
                     /coded_by="NM_181308.3:28..1554"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS9970.1"
                     /db_xref="GeneID:91833"
                     /db_xref="HGNC:HGNC:19667"
                     /db_xref="MIM:617741"
ORIGIN      
        1 mategggkem neiktqfttr eglykllphs eysrpnrvpf nsqgsnpvrv sfvnlndqsg
       61 ngdrlcfnvg relyfyiykg vrkrlidksr vtcvkwvpgs eslflvahss gnmylynveh
      121 tcgttaphyq llkqgesfav htckskstrn pllkwtvgeg alnefafspd gkflacvsqd
      181 gflrvfnfds velhgtmksy fggllcvcws pdgkyivtgg eddlvtvwsf vdcrviargh
      241 ghkswvsvva fdpyttsvee gdpmefsgsd edfqdllhfg rdranstqsr lskrnstdsr
      301 pvsvtyrfgs vgqdtqlclw dltedilfph qplsrartht nvmnatsppa gsngnsvttp
      361 gnsvppplpr snslphsavs nagskssvmd gaiasgvskf atlslhdrke rhhekdhkrn
      421 hsmghissks sdklnlvtkt ktdpaktlgt plcprmedvp lleplickki aherltvlif
      481 ledcivtacq egfictwgrp gkvvsfnp
//
LOCUS       NP_001193971             285 aa            linear   PRI 21-NOV-2025
DEFINITION  protein arginine N-methyltransferase 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001193971
VERSION     NP_001193971.1
DBSOURCE    REFSEQ: accession NM_001207042.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Walton,J., Ng,A.S.N., Arevalo,K., Apostoli,A., Meens,J.,
            Karamboulas,C., St-Germain,J., Prinos,P., Dmytryshyn,J., Chen,E.,
            Arrowsmith,C.H., Raught,B. and Ailles,L.
  TITLE     PRMT1 inhibition perturbs RNA metabolism and induces DNA damage in
            clear cell renal cell carcinoma
  JOURNAL   Nat Commun 15 (1), 8232 (2024)
   PUBMED   39300069
  REMARK    GeneRIF: PRMT1 inhibition perturbs RNA metabolism and induces DNA
            damage in clear cell renal cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Wang,H., Li,Y., Wu,N., Lv,C. and Wang,Y.
  TITLE     P4HB regulates the TGFbeta/SMAD3 signaling pathway through PRMT1 to
            participate in high glucose-induced epithelial-mesenchymal
            transition and fibrosis of renal tubular epithelial cells
  JOURNAL   BMC Nephrol 25 (1), 297 (2024)
   PUBMED   39251943
  REMARK    GeneRIF: P4HB regulates the TGFbeta/SMAD3 signaling pathway through
            PRMT1 to participate in high glucose-induced epithelial-mesenchymal
            transition and fibrosis of renal tubular epithelial cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Yoshimatsu,M., Toyokawa,G., Hayami,S., Unoki,M., Tsunoda,T.,
            Field,H.I., Kelly,J.D., Neal,D.E., Maehara,Y., Ponder,B.A.,
            Nakamura,Y. and Hamamoto,R.
  TITLE     Dysregulation of PRMT1 and PRMT6, Type I arginine
            methyltransferases, is involved in various types of human cancers
  JOURNAL   Int J Cancer 128 (3), 562-573 (2011)
   PUBMED   20473859
  REMARK    GeneRIF: PRMT1 may be involved in human carcinogenesis and may thus
            be a therapeutic target for various types of cancer.
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Scorilas,A., Black,M.H., Talieri,M. and Diamandis,E.P.
  TITLE     Genomic organization, physical mapping, and expression analysis of
            the human protein arginine methyltransferase 1 gene
  JOURNAL   Biochem Biophys Res Commun 278 (2), 349-359 (2000)
   PUBMED   11097842
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Abramovich,C., Yakobson,B., Chebath,J. and Revel,M.
  TITLE     A protein-arginine methyltransferase binds to the intracytoplasmic
            domain of the IFNAR1 chain in the type I interferon receptor
  JOURNAL   EMBO J 16 (2), 260-266 (1997)
   PUBMED   9029147
REFERENCE   8  (residues 1 to 285)
  AUTHORS   Hoodless,P.A., Haerry,T., Abdollah,S., Stapleton,M., O'Connor,M.B.,
            Attisano,L. and Wrana,J.L.
  TITLE     MADR1, a MAD-related protein that functions in BMP2 signaling
            pathways
  JOURNAL   Cell 85 (4), 489-500 (1996)
   PUBMED   8653785
REFERENCE   9  (residues 1 to 285)
  AUTHORS   Rajpurohit,R., Lee,S.O., Park,J.O., Paik,W.K. and Kim,S.
  TITLE     Enzymatic methylation of recombinant heterogeneous nuclear RNP
            protein A1. Dual substrate specificity for
            S-adenosylmethionine:histone-arginine N-methyltransferase
  JOURNAL   J Biol Chem 269 (2), 1075-1082 (1994)
   PUBMED   8288564
REFERENCE   10 (residues 1 to 285)
  AUTHORS   Baldwin,G.S. and Carnegie,P.R.
  TITLE     Specific enzymic methylation of an arginine in the experimental
            allergic encephalomyelitis protein from human myelin
  JOURNAL   Science 171 (3971), 579-581 (1971)
   PUBMED   4924231
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC421815.1, BX352789.2 and
            AI193116.1.
            
            Summary: This gene encodes a member of the protein arginine
            N-methyltransferase (PRMT) family. Post-translational modification
            of target proteins by PRMTs plays an important regulatory role in
            many biological processes, whereby PRMTs methylate arginine
            residues by transferring methyl groups from S-adenosyl-L-methionine
            to terminal guanidino nitrogen atoms. The encoded protein is a type
            I PRMT and is responsible for the majority of cellular arginine
            methylation activity. Increased expression of this gene may play a
            role in many types of cancer. Alternatively spliced transcript
            variants encoding multiple isoforms have been observed for this
            gene, and a pseudogene of this gene is located on the long arm of
            chromosome 5. [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (4) lacks three exons in the
            coding region, but maintains the reading frame, compared to variant
            1. The encoded isoform (4) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX352789.2, SRR14038192.3187884.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..285
                     /product="protein arginine N-methyltransferase 1 isoform
                     4"
                     /EC_number="2.1.1.319"
                     /note="HMT1 (hnRNP methyltransferase, S. cerevisiae)-like
                     2; protein arginine N-methyltransferase 1; interferon
                     receptor 1-bound protein 4; histone-arginine
                     N-methyltransferase PRMT1; heterogeneous nuclear
                     ribonucleoprotein methyltransferase 1-like 2; highly
                     conserved protein 1"
                     /calculated_mol_wt=32562
     Region          45..>167
                     /region_name="COG4076"
                     /note="Predicted RNA methylase [General function
                     prediction only]"
                     /db_xref="CDD:443253"
     CDS             1..285
                     /gene="PRMT1"
                     /gene_synonym="ANM1; HCP1; HRMT1L2; IR1B4"
                     /coded_by="NM_001207042.3:11..868"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS74425.1"
                     /db_xref="GeneID:3276"
                     /db_xref="HGNC:HGNC:5187"
                     /db_xref="MIM:602950"
ORIGIN      
        1 maaaeaanci mevscgqaes sekpnaedmt skdyyfdsya hfgiheemlk devrtltyrn
       61 smfhnrhlfk dkvvldvgsg tgilcmfaak agarkvigie cssisdyavk ivkankldhv
      121 vtiikgkvee velpvekvdi iisewmgycl fyesmlntvl yardkwlevd iytvkvedlt
      181 ftspfclqvk rndyvhalva yfnieftrch krtgfstspe spythwkqtv fymedyltvk
      241 tgeeifgtig mrpnaknnrd ldftidldfk gqlcelscst dyrmr
//
LOCUS       NP_001371284             555 aa            linear   PRI 21-NOV-2025
DEFINITION  double-strand-break repair protein rad21-like protein 1 isoform 2
            [Homo sapiens].
ACCESSION   NP_001371284 XP_024307732
VERSION     NP_001371284.1
DBSOURCE    REFSEQ: accession NM_001384355.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Shi,Z., Gao,H., Bai,X.C. and Yu,H.
  TITLE     Cryo-EM structure of the human cohesin-NIPBL-DNA complex
  JOURNAL   Science 368 (6498), 1454-1459 (2020)
   PUBMED   32409525
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Minase,G., Miyamoto,T., Miyagawa,Y., Iijima,M., Ueda,H., Saijo,Y.,
            Namiki,M. and Sengoku,K.
  TITLE     Single-nucleotide polymorphisms in the human RAD21L gene may be a
            genetic risk factor for Japanese patients with azoospermia caused
            by meiotic arrest and Sertoli cell-only syndrome
  JOURNAL   Hum Fertil (Camb) 20 (3), 217-220 (2017)
   PUBMED   28635411
  REMARK    GeneRIF: The association of three single-nucleotide polymorphisms
            with azoospermia, especially Sertoli cell-only syndrome, was
            studied in Japanese men.
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Li,L., Fridley,B.L., Kalari,K., Niu,N., Jenkins,G., Batzler,A.,
            Abo,R.P., Schaid,D. and Wang,L.
  TITLE     Discovery of genetic biomarkers contributing to variation in drug
            response of cytidine analogues using human lymphoblastoid cell
            lines
  JOURNAL   BMC Genomics 15, 93 (2014)
   PUBMED   24483146
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 555)
  AUTHORS   Gutierrez-Caballero,C., Herran,Y., Sanchez-Martin,M., Suja,J.A.,
            Barbero,J.L., Llano,E. and Pendas,A.M.
  TITLE     Identification and molecular characterization of the mammalian
            alpha-kleisin RAD21L
  JOURNAL   Cell Cycle 10 (9), 1477-1487 (2011)
   PUBMED   21527826
  REMARK    GeneRIF: RAD21L is identified as a novel cohesin complex subunit
            homologous to mammalian RAD21/REC8/alpha-kleisin subfamily.
REFERENCE   5  (residues 1 to 555)
  AUTHORS   Baranzini,S.E., Wang,J., Gibson,R.A., Galwey,N., Naegelin,Y.,
            Barkhof,F., Radue,E.W., Lindberg,R.L., Uitdehaag,B.M.,
            Johnson,M.R., Angelakopoulou,A., Hall,L., Richardson,J.C.,
            Prinjha,R.K., Gass,A., Geurts,J.J., Kragt,J., Sombekke,M.,
            Vrenken,H., Qualley,P., Lincoln,R.R., Gomez,R., Caillier,S.J.,
            George,M.F., Mousavi,H., Guerrero,R., Okuda,D.T., Cree,B.A.,
            Green,A.J., Waubant,E., Goodin,D.S., Pelletier,D., Matthews,P.M.,
            Hauser,S.L., Kappos,L., Polman,C.H. and Oksenberg,J.R.
  TITLE     Genome-wide association analysis of susceptibility and clinical
            phenotype in multiple sclerosis
  JOURNAL   Hum Mol Genet 18 (4), 767-778 (2009)
   PUBMED   19010793
REFERENCE   6  (residues 1 to 555)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL031665.19.
            
            On Jun 16, 2020 this sequence version replaced XP_024307732.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2897566.1,
                                           SRR5189667.243758.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000683101.1/ ENSP00000507397.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..555
                     /product="double-strand-break repair protein rad21-like
                     protein 1 isoform 2"
                     /note="double-strand-break repair protein rad21-like
                     protein 1; RAD21-like 1"
                     /calculated_mol_wt=63065
     Region          1..100
                     /region_name="Rad21_Rec8_N"
                     /note="N terminus of Rad21 / Rec8 like protein; pfam04825"
                     /db_xref="CDD:461446"
     Region          290..370
                     /region_name="Rad21_Rec8_M_NXP1-like"
                     /note="Middle HEAT-repeat binding domain found in Homo
                     sapiens nuclear matrix protein 1 (NXP-1) and similar
                     proteins; cd21792"
                     /db_xref="CDD:439294"
     Site            order(296..298,301..308,311,314..315,317..318,320..327,
                     329..335,337..339,342..343,346..356,358..359,362..363,
                     365..370)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:439294"
     Region          501..552
                     /region_name="Rad21_Rec8"
                     /note="Conserved region of Rad21 / Rec8 like protein;
                     pfam04824"
                     /db_xref="CDD:335912"
     CDS             1..555
                     /gene="RAD21L1"
                     /gene_synonym="dJ545L17.2; RAD21L"
                     /coded_by="NM_001384355.1:130..1797"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS92998.1"
                     /db_xref="GeneID:642636"
                     /db_xref="HGNC:HGNC:16271"
                     /db_xref="MIM:619533"
ORIGIN      
        1 mfythvlmsk rgplakiwla ahwekkltka hvfecnleit iekilspkvk ialrtsghll
       61 lgvvriynrk akylladcse aflkmkmtfc pglvdlpken feasynaitl peefhdfdtq
      121 nmnaidvseh ftqnqsrpee itlrenfdnd lifqaesfge eseilrrhsf fddnillnss
      181 gpliehssgs ltgerslfyd sgdgfgdega agemidnllq ddqnilledm hlnreislps
      241 eppnslavep dnsecicvpe nekmnetill steeegftld pidisdiaek rkgkkrrlli
      301 dpikelsskv ihkqltsfad tlmvlelapp tqrlmmwkkr ggvhtllsta aqdlihaelk
      361 mlftkcflss gfklgrkmiq kesvreevgn qnivetsmmq epnyqqelsk pqtwkdvigg
      421 sqhsshedtn kninsedive mvslaaeess lmndlfaqei eyspvelesl sneenieter
      481 wngrilqmln rlresnkmgm qsfslmklcr nsdrkqaaak fysflvlkkq laielsqsap
      541 yadiiatmgp mfyni
//
LOCUS       NP_001381086            1196 aa            linear   PRI 21-NOV-2025
DEFINITION  regulator of G-protein signaling 12 isoform 4 [Homo sapiens].
ACCESSION   NP_001381086
VERSION     NP_001381086.1
DBSOURCE    REFSEQ: accession NM_001394157.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1196)
  AUTHORS   Sneddon,W.B., Ramineni,S., Van Doorn,G.E., Hepler,J.R. and
            Friedman,P.A.
  TITLE     Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport
  JOURNAL   Biochem Biophys Res Commun 733, 150700 (2024)
   PUBMED   39293332
  REMARK    GeneRIF: Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport.
REFERENCE   2  (residues 1 to 1196)
  AUTHORS   Yuan,G., Yang,S. and Yang,S.
  TITLE     RGS12 represses oral squamous cell carcinoma by driving M1
            polarization of tumor-associated macrophages via controlling
            ciliary MYCBP2/KIF2A signaling
  JOURNAL   Int J Oral Sci 15 (1), 11 (2023)
   PUBMED   36797232
  REMARK    GeneRIF: RGS12 represses oral squamous cell carcinoma by driving M1
            polarization of tumor-associated macrophages via controlling
            ciliary MYCBP2/KIF2A signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1196)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1196)
  AUTHORS   Yuan,G., Fu,C., Yang,S.T., Yuh,D.Y., Hajishengallis,G. and Yang,S.
  TITLE     RGS12 Drives Macrophage Activation and Osteoclastogenesis in
            Periodontitis
  JOURNAL   J Dent Res 101 (4), 448-457 (2022)
   PUBMED   34796776
  REMARK    GeneRIF: RGS12 Drives Macrophage Activation and Osteoclastogenesis
            in Periodontitis.
REFERENCE   5  (residues 1 to 1196)
  AUTHORS   Yuan,G., Huang,Y., Yang,S.T., Ng,A. and Yang,S.
  TITLE     RGS12 inhibits the progression and metastasis of multiple myeloma
            by driving M1 macrophage polarization and activation in the bone
            marrow microenvironment
  JOURNAL   Cancer Commun (Lond) 42 (1), 60-64 (2022)
   PUBMED   34931491
  REMARK    GeneRIF: RGS12 inhibits the progression and metastasis of multiple
            myeloma by driving M1 macrophage polarization and activation in the
            bone marrow microenvironment.
REFERENCE   6  (residues 1 to 1196)
  AUTHORS   Schiff,M.L., Siderovski,D.P., Jordan,J.D., Brothers,G., Snow,B., De
            Vries,L., Ortiz,D.F. and Diverse-Pierluissi,M.
  TITLE     Tyrosine-kinase-dependent recruitment of RGS12 to the N-type
            calcium channel
  JOURNAL   Nature 408 (6813), 723-727 (2000)
   PUBMED   11130074
REFERENCE   7  (residues 1 to 1196)
  AUTHORS   Chatterjee,T.K. and Fisher,R.A.
  TITLE     Novel alternative splicing and nuclear localization of human RGS12
            gene products
  JOURNAL   J Biol Chem 275 (38), 29660-29671 (2000)
   PUBMED   10869340
REFERENCE   8  (residues 1 to 1196)
  AUTHORS   Frohme,M., Scharm,B., Delius,H., Knecht,R. and Hoheisel,J.D.
  TITLE     Use of representational difference analysis and cDNA arrays for
            transcriptional profiling of tumor tissue
  JOURNAL   Ann N Y Acad Sci 910, 85-104 (2000)
   PUBMED   10911908
  REMARK    Review article
REFERENCE   9  (residues 1 to 1196)
  AUTHORS   Snow,B.E., Hall,R.A., Krumins,A.M., Brothers,G.M., Bouchard,D.,
            Brothers,C.A., Chung,S., Mangion,J., Gilman,A.G., Lefkowitz,R.J.
            and Siderovski,D.P.
  TITLE     GTPase activating specificity of RGS12 and binding specificity of
            an alternatively spliced PDZ (PSD-95/Dlg/ZO-1) domain
  JOURNAL   J Biol Chem 273 (28), 17749-17755 (1998)
   PUBMED   9651375
REFERENCE   10 (residues 1 to 1196)
  AUTHORS   Snow,B.E., Antonio,L., Suggs,S., Gutstein,H.B. and Siderovski,D.P.
  TITLE     Molecular cloning and expression analysis of rat Rgs12 and Rgs14
  JOURNAL   Biochem Biophys Res Commun 233 (3), 770-777 (1997)
   PUBMED   9168931
  REMARK    GeneRIF: shows chromosomal mapping information for human locus.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645949.16 and AL590235.23.
            
            Summary: This gene encodes a member of the 'regulator of G protein
            signaling' (RGS) gene family. The encoded protein may function as a
            guanosine triphosphatase (GTPase)-activating protein as well as a
            transcriptional repressor. This protein may play a role in
            tumorigenesis. Multiple transcript variants encoding distinct
            isoforms have been identified for this gene. Other alternative
            splice variants have been described but their biological nature has
            not been determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2142853,
                              SAMEA2148874 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..1196
                     /product="regulator of G-protein signaling 12 isoform 4"
                     /note="regulator of G-protein signalling 12"
                     /calculated_mol_wt=130451
     Region          21..96
                     /region_name="PDZ_RGS12-like"
                     /note="PDZ domain of regulator of G-protein signaling 12
                     (RGS12), and related domains; cd06710"
                     /db_xref="CDD:467194"
     Site            order(31..37,45,48,77,81,84..85)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467194"
     Region          228..359
                     /region_name="PTB_RGS12"
                     /note="Regulator of G-protein signaling 12
                     Phosphotyrosine-binding (PTB) PH-like fold; cd13162"
                     /db_xref="CDD:269984"
     Site            order(233,310,341)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269984"
     Site            order(299..304,317,352,356)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269984"
     Region          716..830
                     /region_name="RGS_RGS12"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the RGS12 protein; cd08742"
                     /db_xref="CDD:188696"
     Site            order(736..738,740..741,778..783,785..786,813,815..817,
                     821)
                     /site_type="other"
                     /note="G-alpha-3 interaction site [polypeptide binding]"
                     /db_xref="CDD:188696"
     Region          836..951
                     /region_name="RGS12_us1"
                     /note="Unstructured region of RGS12; pfam16613"
                     /db_xref="CDD:465199"
     Region          962..1031
                     /region_name="RBD1_RGS12"
                     /note="Ras-binding domain (RBD) 1 of regulator of G
                     protein signaling 12 (RGS12); cd17136"
                     /db_xref="CDD:340656"
     Site            order(967,988,990,1011)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340656"
     Region          1032..1104
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     Region          1153..>1176
                     /region_name="RGS12_us2"
                     /note="Unstructured region between RBD and GoLoco;
                     pfam16611"
                     /db_xref="CDD:435461"
     CDS             1..1196
                     /gene="RGS12"
                     /coded_by="NM_001394157.1:181..3771"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:6002"
                     /db_xref="HGNC:HGNC:9994"
                     /db_xref="MIM:602512"
ORIGIN      
        1 mfrageaskr plpgpspprv rsvevargra gygftlsgqa pcvlscvmrg spadfvglra
       61 gdqilavnei nvkkashedv vkligkcsgv lhmviaegvg rfescssdee gglyegkgwl
      121 kpkldskalg inraervvee mqsggifnmi fenpslcasn seplklkqrs lsesaatrfd
      181 vghesinnpn pnmlskeeis kvihddsvfs igleshddfa ldasilnvam ivgylgsiel
      241 pstssnlesd slqairgcmr rlraeqkihs lvtmkimhdc vqlstdkagv vaeypaekla
      301 fsavcpddrr ffglvtmqtn ddgslaqeee galrtschvf mvdpdlfnhk ihqgiarrfg
      361 fectadpdtn gclefpassl pvlqfisvly rdmgeliegm rarafldgda dahqnnstss
      421 nsdsgignfh qeeksnrvlv vdlggsssrh gpggsawdgv ggrgaqpwga pwtgpfcpdp
      481 egsppfeaah qtdrfwdlnk hlgpaspvev ppaslrssvp pskrgtvgag cgfnqrwlpv
      541 hvlrewqcgh tsdqdsytds tdgwssincg tlpppmskip adryrvegsf aqpplnapkr
      601 ewsrkafgmq sifgphrnvr ktkedkkgsk fgrgtgltqp sqrtsarrsf grskrfsitr
      661 slddlesatv sdgeltgadl kdcvsnnsls snaslpsvqs crrlrerrva swavsferll
      721 qdpvgvryfs dflrkefsee nilfwqacey fnhvpahdkk elsyrareif skflcskatt
      781 pvnidsqaql addvlraphp dmfkeqqlqi fnlmkfdsyt rflksplyqe cilaevegra
      841 lpdsqqvpss paskhslgsd hssvstpkkl sgksksgrsl neelgdedse kkrkgaffsw
      901 srtrstgrsq kkrehgdhad dalhangglc rresqgsvss agsldlseac rtlapekdka
      961 tkhccihlpd gtscvvavka gfsikdilsg lcerhginga aadlflvggd kplvlhqdss
     1021 ilesrdlrle krtlfrldlv pinrsvglka kptkpvtevl rpvvarygld lsgllvrlsg
     1081 ekepldlgap issldgqrvv leekdpsrgk vlpwgswvrp aafgdglvar ppphpdaqep
     1141 allralvenp sadkqkgvpv kqntavnsss rnhsatsfls lfpklrateq mtnvgc
//
LOCUS       NP_001316064             407 aa            linear   PRI 21-NOV-2025
DEFINITION  cytoplasmic dynein 1 light intermediate chain 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001316064
VERSION     NP_001316064.1
DBSOURCE    REFSEQ: accession NM_001329135.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Keren-Kaplan,T., Saric,A., Ghosh,S., Williamson,C.D., Jia,R., Li,Y.
            and Bonifacino,J.S.
  TITLE     RUFY3 and RUFY4 are ARL8 effectors that promote coupling of
            endolysosomes to dynein-dynactin
  JOURNAL   Nat Commun 13 (1), 1506 (2022)
   PUBMED   35314674
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Kumari,A., Kumar,C., Pergu,R., Kumar,M., Mahale,S.P., Wasnik,N. and
            Mylavarapu,S.V.S.
  TITLE     Phosphorylation and Pin1 binding to the LIC1 subunit selectively
            regulate mitotic dynein functions
  JOURNAL   J Cell Biol 220 (12) (2021)
   PUBMED   34709360
  REMARK    GeneRIF: Phosphorylation and Pin1 binding to the LIC1 subunit
            selectively regulate mitotic dynein functions.
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Tan,S.C., Scherer,J. and Vallee,R.B.
  TITLE     Recruitment of dynein to late endosomes and lysosomes through light
            intermediate chains
  JOURNAL   Mol Biol Cell 22 (4), 467-477 (2011)
   PUBMED   21169557
  REMARK    GeneRIF: using a variety of complementary approaches, our results
            indicate a novel specific role for the LICs in dynein recruitment
            to components of the late endocytic pathway.
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Horgan,C.P., Hanscom,S.R. and McCaffrey,M.W.
  TITLE     Dynein LIC1 localizes to the mitotic spindle and midbody and LIC2
            localizes to spindle poles during cell division
  JOURNAL   Cell Biol Int 35 (2), 171-178 (2011)
   PUBMED   20964624
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Sivaram,M.V., Wadzinski,T.L., Redick,S.D., Manna,T. and Doxsey,S.J.
  TITLE     Dynein light intermediate chain 1 is required for progress through
            the spindle assembly checkpoint
  JOURNAL   EMBO J 28 (7), 902-914 (2009)
   PUBMED   19229290
  REMARK    GeneRIF: Dynein light intermediate chain 1 is required for progress
            through the spindle assembly checkpoint
REFERENCE   8  (residues 1 to 407)
  AUTHORS   Pfister,K.K., Fisher,E.M., Gibbons,I.R., Hays,T.S., Holzbaur,E.L.,
            McIntosh,J.R., Porter,M.E., Schroer,T.A., Vaughan,K.T.,
            Witman,G.B., King,S.M. and Vallee,R.B.
  TITLE     Cytoplasmic dynein nomenclature
  JOURNAL   J Cell Biol 171 (3), 411-413 (2005)
   PUBMED   16260502
REFERENCE   9  (residues 1 to 407)
  AUTHORS   Bielli,A., Thornqvist,P.O., Hendrick,A.G., Finn,R., Fitzgerald,K.
            and McCaffrey,M.W.
  TITLE     The small GTPase Rab4A interacts with the central region of
            cytoplasmic dynein light intermediate chain-1
  JOURNAL   Biochem Biophys Res Commun 281 (5), 1141-1153 (2001)
   PUBMED   11243854
REFERENCE   10 (residues 1 to 407)
  AUTHORS   Tynan,S.H., Purohit,A., Doxsey,S.J. and Vallee,R.B.
  TITLE     Light intermediate chain 1 defines a functional subfraction of
            cytoplasmic dynein which binds to pericentrin
  JOURNAL   J Biol Chem 275 (42), 32763-32768 (2000)
   PUBMED   10893222
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK074348.1.
            
            Summary: The protein encoded by this gene belongs to light
            intermediate subunit family, whose members are components of the
            multiprotein cytoplasmic dynein complex, which is involved in
            intracellular trafficking and chromosome segregation during
            mitosis. The protein plays a role in moving the spindle assembly
            checkpoint (SAC) from kinetochores to spindle poles. The protein
            may also mediate binding to other cargo molecules to facilitate
            intracellular vesicle trafficking. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (2) lacks two consecutive
            alternate exons in the 5' coding region, compared to variant 1. It
            encodes isoform 2, which is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293253.1, SRR1803617.183424.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.3"
     Protein         1..407
                     /product="cytoplasmic dynein 1 light intermediate chain 1
                     isoform 2"
                     /note="dynein, cytoplasmic, light intermediate polypeptide
                     1; dynein light chain A; dynein light intermediate chain
                     1, cytosolic"
                     /calculated_mol_wt=43063
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6G9.3)"
     Region          43..401
                     /region_name="DLIC"
                     /note="Dynein light intermediate chain (DLIC); pfam05783"
                     /db_xref="CDD:368612"
     CDS             1..407
                     /gene="DYNC1LI1"
                     /gene_synonym="DLC-A; DLIC-1; DNCLI1; LIC1"
                     /coded_by="NM_001329135.2:89..1312"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS87058.1"
                     /db_xref="GeneID:51143"
                     /db_xref="HGNC:HGNC:18745"
                     /db_xref="MIM:615890"
ORIGIN      
        1 maavgrvgsf gssppglsst ytggplgnei asgnggaaag ddedgqnlws cilsevstrs
       61 rsklpagknv lllvirdfqe yvepgedfpa spqrrntasq edkddsvvlp lgadtlthnl
      121 gipvlvvctk cdaisvleke hdyrdehfdf iqshirkfcl qygaaliyts vkenknidlv
      181 ykyivqklyg fpykipavvv ekdavfipag wdndkkigil henfqtlkae dnfediitkp
      241 pvrkfvheke imaeddqvfl mklqsllakq pptaagrpvd asprvpggsp rtpnrsvssn
      301 vasvspipag skkidpnmka gatsegvlan ffnsllskkt gspggpgvsg gspaggaggg
      361 ssglppstkk sgqkpvldvh aeldritrkp vtvspttpts ptegeas
//
LOCUS       NP_001308707             435 aa            linear   PRI 21-NOV-2025
DEFINITION  gamma-1-syntrophin isoform 3 [Homo sapiens].
ACCESSION   NP_001308707
VERSION     NP_001308707.1
DBSOURCE    REFSEQ: accession NM_001321778.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Orvedahl,A., Sumpter,R. Jr., Xiao,G., Ng,A., Zou,Z., Tang,Y.,
            Narimatsu,M., Gilpin,C., Sun,Q., Roth,M., Forst,C.V., Wrana,J.L.,
            Zhang,Y.E., Luby-Phelps,K., Xavier,R.J., Xie,Y. and Levine,B.
  TITLE     Image-based genome-wide siRNA screen identifies selective autophagy
            factors
  JOURNAL   Nature 480 (7375), 113-117 (2011)
   PUBMED   22020285
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Hafner,A., Obermajer,N. and Kos,J.
  TITLE     gamma-1-syntrophin mediates trafficking of gamma-enolase towards
            the plasma membrane and enhances its neurotrophic activity
  JOURNAL   Neurosignals 18 (4), 246-258 (2010)
   PUBMED   21358174
  REMARK    GeneRIF: Brain-specific gamma1-syntrophin participates in
            gamma-enolase translocation towards the plasma membrane, a
            pre-requisite for its neurotrophic activity.
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Hogan,A., Yakubchyk,Y., Chabot,J., Obagi,C., Daher,E., Maekawa,K.
            and Gee,S.H.
  TITLE     The phosphoinositol 3,4-bisphosphate-binding protein TAPP1
            interacts with syntrophins and regulates actin cytoskeletal
            organization
  JOURNAL   J Biol Chem 279 (51), 53717-53724 (2004)
   PUBMED   15485858
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Bashiardes,S., Veile,R., Allen,M., Wise,C.A., Dobbs,M.,
            Morcuende,J.A., Szappanos,L., Herring,J.A., Bowcock,A.M. and
            Lovett,M.
  TITLE     SNTG1, the gene encoding gamma1-syntrophin: a candidate gene for
            idiopathic scoliosis
  JOURNAL   Hum Genet 115 (1), 81-89 (2004)
   PUBMED   15088139
  REMARK    GeneRIF: Observational study of genotype prevalence. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 435)
  AUTHORS   Hogan,A., Shepherd,L., Chabot,J., Quenneville,S., Prescott,S.M.,
            Topham,M.K. and Gee,S.H.
  TITLE     Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta.
            Regulation of nuclear localization by PDZ interactions
  JOURNAL   J Biol Chem 276 (28), 26526-26533 (2001)
   PUBMED   11352924
REFERENCE   9  (residues 1 to 435)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   10 (residues 1 to 435)
  AUTHORS   Piluso,G., Mirabella,M., Ricci,E., Belsito,A., Abbondanza,C.,
            Servidei,S., Puca,A.A., Tonali,P., Puca,G.A. and Nigro,V.
  TITLE     Gamma1- and gamma2-syntrophins, two novel dystrophin-binding
            proteins localized in neuronal cells
  JOURNAL   J Biol Chem 275 (21), 15851-15860 (2000)
   PUBMED   10747910
  REMARK    GeneRIF: suggests a differentiated role of a modified
            dystrophin-associated complex in the central nervous system
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC023842.5, AK314084.1,
            AC087173.5 and BG194056.1.
            
            Summary: The protein encoded by this gene is a member of the
            syntrophin family. Syntrophins are cytoplasmic peripheral membrane
            proteins that typically contain 2 pleckstrin homology (PH) domains,
            a PDZ domain that bisects the first PH domain, and a C-terminal
            domain that mediates dystrophin binding. This family member plays a
            role in mediating gamma-enolase trafficking to the plasma membrane
            and in enhancing its neurotrophic activity. Mutations in this gene
            are associated with idiopathic scoliosis. Alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Mar 2016].
            
            Transcript Variant: This variant (8) differs in the 5' UTR and
            lacks two 3' exons but contains an alternate 3' terminal exon, and
            it thus differs in the 3' coding region and 3' UTR, compared to
            variant 1. The encoded isoform (3) has a distinct C-terminus and is
            shorter than isoform 1. Variants 5, 6, 7 and 8 all encode isoform
            3.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.40840.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..435
                     /product="gamma-1-syntrophin isoform 3"
                     /note="gamma1-syntrophin; syntrophin 4;
                     gamma-1-syntrophin"
                     /calculated_mol_wt=48794
     Region          56..138
                     /region_name="PDZ_syntrophin-like"
                     /note="PDZ domain of syntrophins, and related domains;
                     cd06801"
                     /db_xref="CDD:467262"
     Site            order(67..73,85,88,118,122,125..126)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467262"
     Region          191..259
                     /region_name="PH"
                     /note="Pleckstrin homology (PH) domain; cd00821"
                     /db_xref="CDD:275388"
     Region          284..389
                     /region_name="PH"
                     /note="Pleckstrin homology domain; smart00233"
                     /db_xref="CDD:214574"
     CDS             1..435
                     /gene="SNTG1"
                     /gene_synonym="G1SYN; SYN4"
                     /coded_by="NM_001321778.2:393..1700"
                     /note="isoform 3 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS87608.1"
                     /db_xref="GeneID:54212"
                     /db_xref="HGNC:HGNC:13740"
                     /db_xref="MIM:608714"
ORIGIN      
        1 mdfrtaceet ktgicllqdg nqepfkvrlh lakdilmiqe qdvicvsgep fysgertvti
       61 rrqtvggfgl sikggaehni pvvvskiske qraelsgllf igdailqing invrkcrhee
      121 vvqvlrnage evtltvsflk rapaflklpl nedcacapsd qssgtssplc dsglhlnyhp
      181 nntdtlscss wptspglrwe krwcdlrlip llhsrfsqyv pgtdlsrqna fqviavdgvc
      241 tgiiqclsae dcvdwlqaia tnisnltkhn ikkinrnfpv nqqivymgwc eareqdplqd
      301 rvysptflal rgsclykfla ppvttwdwtr aektfsvyei mckilkdsdl ldrrkqcftv
      361 qsesgedlyf svelesdlaq werafqtatf leveriqckt yacvleshlm gltidfstgf
      421 icfdaatkvm csgql
//
LOCUS       NP_001336020             659 aa            linear   PRI 21-NOV-2025
DEFINITION  TBC1 domain family member 5 isoform e [Homo sapiens].
ACCESSION   NP_001336020 XP_016863056
VERSION     NP_001336020.1
DBSOURCE    REFSEQ: accession NM_001349091.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Tu,Y.X.I., Sydor,A.M., Coyaud,E., Laurent,E.M.N., Dyer,D.,
            Mellouk,N., St-Germain,J., Vernon,R.M., Forman-Kay,J.D., Li,T.,
            Hua,R., Zhao,K., Ridgway,N.D., Kim,P.K., Raught,B. and Brumell,J.H.
  TITLE     Global Proximity Interactome of the Human Macroautophagy Pathway
  JOURNAL   Autophagy 18 (5), 1174-1186 (2022)
   PUBMED   34524948
REFERENCE   4  (residues 1 to 659)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 659)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 659)
  AUTHORS   Seaman,M.N., Harbour,M.E., Tattersall,D., Read,E. and Bright,N.
  TITLE     Membrane recruitment of the cargo-selective retromer subcomplex is
            catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP
            TBC1D5
  JOURNAL   J Cell Sci 122 (Pt 14), 2371-2382 (2009)
   PUBMED   19531583
  REMARK    GeneRIF: Membrane recruitment of the cargo-selective retromer
            subcomplex VPS35/29/26 is catalysed by the small GTPase Rab7 and
            inhibited by the Rab-GAP TBC1D5.
REFERENCE   7  (residues 1 to 659)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
REFERENCE   8  (residues 1 to 659)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   9  (residues 1 to 659)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 659)
  AUTHORS   Brill,L.M., Salomon,A.R., Ficarro,S.B., Mukherji,M.,
            Stettler-Gill,M. and Peters,E.C.
  TITLE     Robust phosphoproteomic profiling of tyrosine phosphorylation sites
            from human T cells using immobilized metal affinity chromatography
            and tandem mass spectrometry
  JOURNAL   Anal Chem 76 (10), 2763-2772 (2004)
   PUBMED   15144186
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104451.2, AC144531.2, AC090960.3 and AC090644.2.
            
            On Mar 3, 2017 this sequence version replaced XP_016863056.1.
            
            Transcript Variant: This variant (21), as well as variants 17, 18,
            19, and 20, encodes isoform e.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3563656.1,
                                           SRR14038194.1333592.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..659
                     /product="TBC1 domain family member 5 isoform e"
                     /calculated_mol_wt=73027
     Region          19..245
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     CDS             1..659
                     /gene="TBC1D5"
                     /coded_by="NM_001349091.2:525..2504"
                     /note="isoform e is encoded by transcript variant 21"
                     /db_xref="GeneID:9779"
                     /db_xref="HGNC:HGNC:19166"
                     /db_xref="MIM:615740"
ORIGIN      
        1 minnplsqde gslwnkffqd kelrsmieqd vkrtfpemqf fqqenvrkil tdvlfcyare
       61 neqllykqgm hellapivfv lhcdhqaflh asesaqpsee mktvlnpeyl ehdayavfsq
      121 lmetaepwfs tfehdgqkgk etlmtpipfa rpqdlgptia ivtkvnqiqd hllkkhdiel
      181 ymhlnrleia pqiyglrwvr llfgrefplq dllvvwdalf adglslglvd yifvamllyi
      241 rdalissnyq tclgllmhyp figdvhslil kalflrdpkr nprpvtyqfh pnldyykarg
      301 adlmnksrtn akgaplnink vsnslinfgr klispamapg saggpvpggn ssssssvvip
      361 trtsaeapsh hlqqqqqqqr lmksesmpvq lnkglsskni ssspsveslp ggreftgspp
      421 ssatkkdsff snisrsrshs ktmgrkesee eleaqisflq gqlndldamc kycakvmdth
      481 lvniqdvilq enlekedqil vslaglkqik dilkgslrfn qsqleaeene qitiadnhyc
      541 ssgqgqgrgq gqsvqmsgai kqassetpgc tdrgnsddfi liskdddgss argsfsgqaq
      601 plrtlrstsg ksqapvcspl vfsdplmgpa sasssnpsss pdddsskdsg ftivspldi
//
LOCUS       NP_001372182             714 aa            linear   PRI 21-NOV-2025
DEFINITION  amyloid-beta precursor protein isoform k precursor [Homo sapiens].
ACCESSION   NP_001372182
VERSION     NP_001372182.1
DBSOURCE    REFSEQ: accession NM_001385253.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Majernikova,N., Marmolejo-Garza,A., Salinas,C.S., Luu,M.D.A.,
            Zhang,Y., Trombetta-Lima,M., Tomin,T., Birner-Gruenberger,R.,
            Lehtonen,S., Koistinaho,J., Wolters,J.C., Ayton,S., den
            Dunnen,W.F.A. and Dolga,A.M.
  TITLE     The link between amyloid beta and ferroptosis pathway in
            Alzheimer's disease progression
  JOURNAL   Cell Death Dis 15 (10), 782 (2024)
   PUBMED   39468028
  REMARK    GeneRIF: The link between amyloid beta and ferroptosis pathway in
            Alzheimer's disease progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 714)
  AUTHORS   Munch,N.S., Das,S. and Seeger,S.
  TITLE     Unveiling the effect of CaCl2 on amyloid beta aggregation via
            supercritical angle Raman and fluorescence spectroscopy and
            microscopy
  JOURNAL   Phys Chem Chem Phys 26 (41), 26266-26276 (2024)
   PUBMED   39371012
  REMARK    GeneRIF: Unveiling the effect of CaCl2 on amyloid beta aggregation
            via supercritical angle Raman and fluorescence spectroscopy and
            microscopy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 714)
  AUTHORS   Tsoy,A., Umbayev,B., Kassenova,A., Kaupbayeva,B. and Askarova,S.
  TITLE     Pathology of Amyloid-beta (Abeta) Peptide Peripheral Clearance in
            Alzheimer's Disease
  JOURNAL   Int J Mol Sci 25 (20), 10964 (2024)
   PUBMED   39456746
  REMARK    GeneRIF: Pathology of Amyloid-beta (Abeta) Peptide Peripheral
            Clearance in Alzheimer's Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 714)
  AUTHORS   Soscia,S.J., Kirby,J.E., Washicosky,K.J., Tucker,S.M.,
            Ingelsson,M., Hyman,B., Burton,M.A., Goldstein,L.E., Duong,S.,
            Tanzi,R.E. and Moir,R.D.
  TITLE     The Alzheimer's disease-associated amyloid beta-protein is an
            antimicrobial peptide
  JOURNAL   PLoS One 5 (3), e9505 (2010)
   PUBMED   20209079
  REMARK    GeneRIF: Alzheimer's disease-associated amyloid beta-protein
            peptides display antimicrobial activity against C. albicans, E.
            coli, S. epidermidis, S. pneumoniae, S. aureus, L. monocytogenes,
            E. faecalis, and S. agalactiae.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 714)
  AUTHORS   Bird,T.D.
  TITLE     Early-Onset Familial Alzheimer Disease - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301414
REFERENCE   7  (residues 1 to 714)
  AUTHORS   Bird,T.D.
  TITLE     Alzheimer Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301340
REFERENCE   8  (residues 1 to 714)
  AUTHORS   Mant,R., Asherson,P., Gill,M., McGuffin,P., Owen,M., Wert,S.E.,
            Gregory,R.J., Smith,A.E., Cohn,J.A., Wilson,J.M. et al.
  TITLE     Schizophrenia scepticism
  JOURNAL   Nat Genet 2 (1), 12 (1992)
   PUBMED   1303244
REFERENCE   9  (residues 1 to 714)
  AUTHORS   Mullan,M., Crawford,F., Axelman,K., Houlden,H., Lilius,L.,
            Winblad,B. and Lannfelt,L.
  TITLE     A pathogenic mutation for probable Alzheimer's disease in the APP
            gene at the N-terminus of beta-amyloid
  JOURNAL   Nat Genet 1 (5), 345-347 (1992)
   PUBMED   1302033
REFERENCE   10 (residues 1 to 714)
  AUTHORS   Hendriks,L., van Duijn,C.M., Cras,P., Cruts,M., Van Hul,W., van
            Harskamp,F., Warren,A., McInnis,M.G., Antonarakis,S.E., Martin,J.J.
            et al.
  TITLE     Presenile dementia and cerebral haemorrhage linked to a mutation at
            codon 692 of the beta-amyloid precursor protein gene
  JOURNAL   Nat Genet 1 (3), 218-221 (1992)
   PUBMED   1303239
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001439.1, AP001441.1,
            AP001440.1, KC877827.1, AP001442.1 and AP001443.1.
            
            Summary: This gene encodes a cell surface receptor and
            transmembrane precursor protein that is cleaved by secretases to
            form a number of peptides. Some of these peptides are secreted and
            can bind to the acetyltransferase complex APBB1/TIP60 to promote
            transcriptional activation, while others form the protein basis of
            the amyloid plaques found in the brains of patients with Alzheimer
            disease. In addition, two of the peptides are antimicrobial
            peptides, having been shown to have bacteriocidal and antifungal
            activities. Mutations in this gene have been implicated in
            autosomal dominant Alzheimer disease and cerebroarterial
            amyloidosis (cerebral amyloid angiopathy). Multiple transcript
            variants encoding several different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2014].
            
            Transcript Variant: This variant (11) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (k) has the same
            N- and C-termini but is shorter compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1723848.1,
                                           SRR14038192.1903816.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            Protein has antimicrobial activity :: PMID: 20209079
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..714
                     /product="amyloid-beta precursor protein isoform k
                     precursor"
                     /note="peptidase nexin-II; cerebral vascular amyloid
                     peptide; protease nexin-II; amyloid beta A4 protein;
                     beta-amyloid peptide; alzheimer disease amyloid protein;
                     beta-amyloid peptide(1-40); beta-amyloid peptide(1-42);
                     amyloid precursor protein; beta-amyloid precursor protein;
                     testicular tissue protein Li 2; amyloid beta (A4)
                     precursor protein; alzheimer disease amyloid A4 protein
                     homolog"
                     /calculated_mol_wt=79007
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1781
     Region          24..188
                     /region_name="A4_EXTRA"
                     /note="amyloid A4; smart00006"
                     /db_xref="CDD:128326"
     Region          310..492
                     /region_name="APP_E2"
                     /note="E2 domain of amyloid precursor protein; pfam12925"
                     /db_xref="CDD:463752"
     Region          637..711
                     /region_name="JMTM_Notch_APP"
                     /note="juxtamembrane and transmembrane (JMTM) domain found
                     in Notch and APP family proteins; cl41775"
                     /db_xref="CDD:425406"
     Site            order(650..651,653..654,656..662,664..669)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411983"
     CDS             1..714
                     /gene="APP"
                     /gene_synonym="AAA; ABETA; ABPP; AD1; alpha-sAPP; APPI;
                     CTFgamma; CVAP; PN-II; PN2; preA4"
                     /coded_by="NM_001385253.1:151..2295"
                     /note="isoform k precursor is encoded by transcript
                     variant 11"
                     /db_xref="GeneID:351"
                     /db_xref="HGNC:HGNC:620"
                     /db_xref="MIM:104760"
ORIGIN      
        1 mlpglallll aawtaralev ptdgnaglla epqiamfcgr lnmhmnvqng kwdsdpsgtk
       61 tcidtkegil qycqevypel qitnvveanq pvtiqnwckr grkqckthph fvipyrclvg
      121 efvsdallvp dkckflhqer mdvcethlhw htvaketcse kstnlhdygm llpcgidkfr
      181 gvefvccpla eesdnvdsad aeeddsdvww ggadtdyadg sedkvvevae eeevaeveee
      241 eadddedded gdeveeeaee pyeeatertt siattttttt esveevvrvs qsllkttqep
      301 lardpvklpt taastpdavd kyletpgden ehahfqkake rleakhrerm sqvmreweea
      361 erqaknlpka dkkaviqhfq ekvesleqea anerqqlvet hmarveamln drrrlaleny
      421 italqavppr prhvfnmlkk yvraeqkdrq htlkhfehvr mvdpkkaaqi rsqvmthlrv
      481 iyermnqsls llynvpavae eiqdevdell qkeqnysddv lanmisepri sygndalmps
      541 ltetkttvel lpvngefsld dlqpwhsfga dsvpantene vepvdarpaa drglttrpgs
      601 gltnikteei sevkmdaefr hdsgyevhhq klvffaedvg snkgaiiglm vggvviatvi
      661 vitlvmlkkk qytsihhgvv evdaavtpee rhlskmqqng yenptykffe qmqn
//
LOCUS       NP_001374862            3027 aa            linear   PRI 21-NOV-2025
DEFINITION  dmX-like protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001374862
VERSION     NP_001374862.1
DBSOURCE    REFSEQ: accession NM_001387933.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 3027)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 3027)
  AUTHORS   Jaskolka,M.C., Winkley,S.R. and Kane,P.M.
  TITLE     RAVE and Rabconnectin-3 Complexes as Signal Dependent Regulators of
            Organelle Acidification
  JOURNAL   Front Cell Dev Biol 9, 698190 (2021)
   PUBMED   34249946
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 3027)
  AUTHORS   Davis,L.K., Meyer,K.J., Schindler,E.I., Beck,J.S., Rudd,D.S.,
            Grundstad,A.J., Scheetz,T.E., Braun,T.A., Fingert,J.H.,
            Alward,W.L., Kwon,Y.H., Folk,J.C., Russell,S.R., Wassink,T.H.,
            Sheffield,V.C. and Stone,E.M.
  TITLE     Copy number variations and primary open-angle glaucoma
  JOURNAL   Invest Ophthalmol Vis Sci 52 (10), 7122-7133 (2011)
   PUBMED   21310917
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 3027)
  AUTHORS   Oshikawa,M., Tsutsui,C., Ikegami,T., Fuchida,Y., Matsubara,M.,
            Toyama,S., Usami,R., Ohtoko,K. and Kato,S.
  TITLE     Full-length transcriptome analysis of human retina-derived cell
            lines ARPE-19 and Y79 using the vector-capping method
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6662-6670 (2011)
   PUBMED   21697133
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 3027)
  AUTHORS   Koldehoff,M., Zakrzewski,J.L., Klein-Hitpass,L., Beelen,D.W. and
            Elmaagacli,A.H.
  TITLE     Gene profiling of growth factor independence 1B gene (Gfi-1B) in
            leukemic cells
  JOURNAL   Int J Hematol 87 (1), 39-47 (2008)
   PUBMED   18224412
REFERENCE   6  (residues 1 to 3027)
  AUTHORS   van den Boom,J., Wolter,M., Blaschke,B., Knobbe,C.B. and
            Reifenberger,G.
  TITLE     Identification of novel genes associated with astrocytoma
            progression using suppression subtractive hybridization and
            real-time reverse transcription-polymerase chain reaction
  JOURNAL   Int J Cancer 119 (10), 2330-2338 (2006)
   PUBMED   16865689
REFERENCE   7  (residues 1 to 3027)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   8  (residues 1 to 3027)
  AUTHORS   Kraemer,C., Enklaar,T., Zabel,B. and Schmidt,E.R.
  TITLE     Mapping and structure of DMXL1, a human homologue of the DmX gene
            from Drosophila melanogaster coding for a WD repeat protein
  JOURNAL   Genomics 64 (1), 97-101 (2000)
   PUBMED   10708522
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC118465.2 and AC027320.5.
            
            Summary: The protein encoded by this gene is a member of the WD
            repeat superfamily of proteins, which have regulatory functions.
            This gene is expressed in many tissue types including several types
            of eye tissue, and it has been associated with ocular phenotypes.
            In addition, it is upregulated in cultured cells that overexpress
            growth factor independence 1B, a transcription factor that is
            essential for hematopoietic cell development. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Nov
            2014].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4212694.1,
                                           SRR14038197.2471864.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..3027
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q23.1"
     Protein         1..3027
                     /product="dmX-like protein 1 isoform 2"
                     /note="dmX-like protein 1"
                     /calculated_mol_wt=337709
     Region          108..145
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          114..148
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          162..218
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          166..206
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          229..277
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          234..267
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          420..450
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PNC0; propagated from
                     UniProtKB/Swiss-Prot (Q9Y485.3)"
     Site            425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PNC0; propagated from
                     UniProtKB/Swiss-Prot (Q9Y485.3)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          476..516
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          563..584
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Site            574
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PNC0; propagated from
                     UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          580..621
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          628..665
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          848..895
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Site            918
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y485.3)"
     Site            924
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          968..1010
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          1134..1175
                     /region_name="WD 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          1142..1875
                     /region_name="Rav1p_C"
                     /note="RAVE protein 1 C terminal; pfam12234"
                     /db_xref="CDD:432413"
     Region          1211..1251
                     /region_name="WD 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Site            1830
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y485.3)"
     Site            1896
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y485.3)"
     Site            1908
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y485.3)"
     Site            1970
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          2367..2412
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          2446..2468
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          2742..2783
                     /region_name="WD 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          2747..3004
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          2785..2824
                     /region_name="WD 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          2791..2836
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2836..2878
                     /region_name="WD 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          2841..2883
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2884..2923
                     /region_name="WD 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          2890..2925
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2926..2965
                     /region_name="WD 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     Region          2931..2967
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2978..3016
                     /region_name="WD 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y485.3)"
     CDS             1..3027
                     /gene="DMXL1"
                     /coded_by="NM_001387933.1:187..9270"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS4125.1"
                     /db_xref="GeneID:1657"
                     /db_xref="HGNC:HGNC:2937"
                     /db_xref="MIM:605671"
ORIGIN      
        1 mnlhqvltga vnpgdhcfsv gsigdqrfta yasgcdivil gsdferlqii pgakhgniqv
       61 gcvdcsmqqg kiaasygnvi sifepvnlpk qkknlelysq wqksgqffle siahnitwdp
      121 tgsrlltgss ylqlwsntnl ekptedenln ktdlnfgdwk ciwhcktasq vhlmkfspdg
      181 effatagkdd cllkvwynve nwrtavtspd gssekqsqge idfsfvylah pravngfswr
      241 ktskympras vcnvlltcck dnvcrlwvet flpndcllyg gdcshwtesi nltnnfkrna
      301 sskervqnal evnlrhfrrg rrrslalvah tgylphqqdp hhvhrntplh analchfhia
      361 asinpatdip llpsitslsl neneektgpf vvhwlnnkel hftlsmevfl qqlrksfeqp
      421 sseasvedsn qadvksdeet ddgvddlkin pekkelgcdk mvpnssftsl ssaaidhqie
      481 vllsewskna dmlfsihpmd gsllvwhvdw ldeyqpgmfr qvqvsfvsri pvafptgdan
      541 slcksimmya ctknvdlaiq qgkqkpsglt rstsmlissg hnkssnslkl siftpnvmmi
      601 skhadgslnq wlvsfaeesa fstvlsishk srycghrfhl ndlachsvlp lllttshhna
      661 lrtpdvdnpe qpfdalniee csltqqnkst vdvafqdpsa vyselilwrv dpvgplsfsg
      721 gvselarins lhvsafsnva wlptlipsyc lgaycnspsa cfvasdgqyl rlyeavidak
      781 kllselsnpe iskyvgevfn ivsqqstarp gciialdpit klhgrktqll hvfeedfiln
      841 nlekkslgkd silsnagssp ngfsekfyli viectqdnrs llhmwnlhlk sipvsldekv
      901 dtklseavwq peehyssspe kilspfsqky qacranlqst srltlfsemv ysqelhlpeg
      961 veiisikpsa ghlssssiyp acsapyllat scsdekvrfw rcrvtdgesa tskngkidla
     1021 yiweewplli edglqsnssi tvpgrpvevs cahtnrlava ykqpasnsrs sqdfvmhvsi
     1081 fecestggsc wvleqtihld elstvldsgi svdsnlvayn kqdmylsske nitsntkhlv
     1141 hldwmsredg shiltvgigs klfmygplag kvqdqtgket lafplwestk vvplskfvll
     1201 rsvdlvssvd gsppfpvsls wvrdgilvvg mdcemhvycq wqpsskqepv itdsysgstp
     1261 sitslikqsn sssglhppkk tltrsmtsla qkicgkktaf dpsvdmedsg lfeaahvlsp
     1321 tlpqyhplql lelmdlgkvr rakailshlv kciagevval neaesnherr lrsltisasg
     1381 sttrdpqafn kaentdytei dsvpplplya llaadddscy sslekssnes tlsksnqlsk
     1441 esydelfqtq llmtdthmle tdeentkprv idlsqyspty fgpehaqvls ghllhsslpg
     1501 lsrmeqmslm aladtiatts tdigesrdrs qggetldecg lkfllavrlh tflttslpay
     1561 raqllhqgls tshfawafhs vaeeellnml pamqkddptw selramgvgw wvrntrilrk
     1621 ciekvakaaf yrkndpldaa ifylamkkka viwglyraek ntrmtqffgh nfederwrka
     1681 alknafsllg kqrfehsaaf fllagclrda ievcleklnd iqlalviarl yesefdtsaa
     1741 yksilrkkvl gidspvselc slninmhhdp flrsmaywil edysgaletl ikqpirendd
     1801 qvlsasnptv fnfynylrth plllrrhfgs sdtfsthmsl tgksglagti nlserrlfft
     1861 tasahlkagc pmlalevlsk mpkvikktrp fyrassfldt skdcspsspl kldaredkss
     1921 avdwsqslin gfgsssegss ekqsnstlsf dwsqpsvvfq ddslelkwds dndeenedvp
     1981 ismkelkplq rktdkklddi ssnytesfst ldendllnps ediiavqlkf raclkiltve
     2041 lrtlstgyei dggklryqly hwlekevial qrtcdfcsda eelqsafgrn edefglneda
     2101 edlphqtkvk qlrenfqekr qwllkyqsll rmflsycilh gshggglasv rmelilllqe
     2161 sqqetseplf ssplseqtsv pllfactana ktvvanpllh lsnlthdilh aiinfdspph
     2221 pdiqsnkvyv mhtlaaslsa ciyqclcgsh nyssfqtnqf tgmvyqtvll phrpslktgs
     2281 ldealtpnts paqwpgitcl irllnssgee aqsgltvllc eiltavylsl fihglathss
     2341 nelfrivahp lnekmwsavf gggahvpske qthsktlpvs slveegekqn krfrpskmsc
     2401 resapltpss apvsqeslav kekfippels iwdyfiakpf lpssqsraey dseeslgsdd
     2461 ddndddddvl asdfhlqehs nsnsyswslm rlamvqlvln nlktfypfag hdlaelpvss
     2521 plchavlktl qcweqvllrr leihggppqn yiashtaees lsagpailrh kalleptntp
     2581 fkskhhlals vkrlwqylvk qeeiqetfik niftkkrcln eieadlgypg gkariihkes
     2641 diitafavnk anrnciaias shdvqeldvs gilatqvytw vdddievetk gsedflviha
     2701 rddltavqgt tpythsnpgt pinmpwlgst qtgrgasvmi kkainnvrrm tshptlpyyl
     2761 tgaqdgsvrm fewghsqqit cfrsggnsrv trmrfnyqgn kfgivdadgy lslyqtnwkc
     2821 cpvtgsmpkp yltwqchnkt andfvfvsss sliataglst dnrnvclwdt lvapanslvh
     2881 aftchdsgat vlayapkhql lisggrkgft yvfdlcqrqq rqlfqshdsp vkavavdpte
     2941 eyfvtgsaeg nikiwslstf gllhtfvseh arqsifrnig tgvmqietgp anhifscgad
     3001 gtmkmrilpd qfsplnevlk ndvkfml
//
LOCUS       NP_001259041             211 aa            linear   PRI 21-NOV-2025
DEFINITION  membrane progestin receptor delta isoform 7 [Homo sapiens].
ACCESSION   NP_001259041
VERSION     NP_001259041.1
DBSOURCE    REFSEQ: accession NM_001272112.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Yang,M., Li,J.C., Tao,C., Wu,S., Liu,B., Shu,Q., Li,B. and Zhu,R.
  TITLE     PAQR6 Upregulation Is Associated with AR Signaling and Unfavorite
            Prognosis in Prostate Cancers
  JOURNAL   Biomolecules 11 (9), 1383 (2021)
   PUBMED   34572596
  REMARK    GeneRIF: PAQR6 Upregulation Is Associated with AR Signaling and
            Unfavorite Prognosis in Prostate Cancers.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Huang,X., Dai,F.F., Gaisano,G., Giglou,K., Han,J., Zhang,M.,
            Kittanakom,S., Wong,V., Wei,L., Showalter,A.D., Sloop,K.W.,
            Stagljar,I. and Wheeler,M.B.
  TITLE     The identification of novel proteins that interact with the GLP-1
            receptor and restrain its activity
  JOURNAL   Mol Endocrinol 27 (9), 1550-1563 (2013)
   PUBMED   23864651
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Pang,Y., Dong,J. and Thomas,P.
  TITLE     Characterization, neurosteroid binding and brain distribution of
            human membrane progesterone receptors delta and {epsilon} (mPRdelta
            and mPR{epsilon}) and mPRdelta involvement in neurosteroid
            inhibition of apoptosis
  JOURNAL   Endocrinology 154 (1), 283-295 (2013)
   PUBMED   23161870
  REMARK    GeneRIF: The results suggest that PAQR6 and PAQR9 (mPRdelta and
            mPRepsilon) function as mPRs coupled to G proteins and are
            potential intermediaries of nonclassical antiapoptotic actions of
            neurosteroids in the central nervous system.
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Kamatani,Y., Matsuda,K., Okada,Y., Kubo,M., Hosono,N., Daigo,Y.,
            Nakamura,Y. and Kamatani,N.
  TITLE     Genome-wide association study of hematological and biochemical
            traits in a Japanese population
  JOURNAL   Nat Genet 42 (3), 210-215 (2010)
   PUBMED   20139978
REFERENCE   6  (residues 1 to 211)
  AUTHORS   Smith,J.L., Kupchak,B.R., Garitaonandia,I., Hoang,L.K., Maina,A.S.,
            Regalla,L.M. and Lyons,T.J.
  TITLE     Heterologous expression of human mPRalpha, mPRbeta and mPRgamma in
            yeast confirms their ability to function as membrane progesterone
            receptors
  JOURNAL   Steroids 73 (11), 1160-1173 (2008)
   PUBMED   18603275
  REMARK    GeneRIF: PAQR6 is a previously uncharacterized PAQR which is also
            capable of responding to progesterone.
REFERENCE   7  (residues 1 to 211)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   8  (residues 1 to 211)
  AUTHORS   Tang,Y.T., Hu,T., Arterburn,M., Boyle,B., Bright,J.M., Emtage,P.C.
            and Funk,W.D.
  TITLE     PAQR proteins: a novel membrane receptor family defined by an
            ancient 7-transmembrane pass motif
  JOURNAL   J Mol Evol 61 (3), 372-380 (2005)
   PUBMED   16044242
REFERENCE   9  (residues 1 to 211)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK295916.1, BI819919.1, AK316034.1, AF455046.1, AA310453.1 and
            AL135927.14.
            
            Transcript Variant: This variant (11) has multiple differences and
            initiates translation at an alternate start codon, compared to
            variant 1. Variants 8 through 12 encode the same isoform (7), which
            has a distinct N-terminus and is shorter, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI819919.1, SRR3476690.584445.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..211
                     /product="membrane progestin receptor delta isoform 7"
                     /note="mPR delta; membrane progesterone receptor delta;
                     progestin and adipoQ receptor family member VI; membrane
                     progesterone P4 receptor delta; progesterone and adipoQ
                     receptor family member 6; membrane progestin receptor
                     delta"
                     /calculated_mol_wt=23108
     CDS             1..211
                     /gene="PAQR6"
                     /gene_synonym="PRdelta"
                     /coded_by="NM_001272112.2:493..1128"
                     /note="isoform 7 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS72945.1"
                     /db_xref="GeneID:79957"
                     /db_xref="HGNC:HGNC:30132"
                     /db_xref="MIM:614579"
ORIGIN      
        1 matissarcs lassspptcl kgwhqdalit satatsysts vqcwaptssw rqcwliwdha
       61 epgwphrnlp wawqaqwphw swlqlgtysl lllsqppcfg ppvhalccrv ahwrgvprpn
      121 nseapsltls wrgqrpgpsa deeprfgpnq vgthlslept gaeerghrre greeegclgg
      181 laecerdreg aldgsgrsae glrgemhacp g
//
LOCUS       NP_001229777             358 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase RNF146 isoform a [Homo sapiens].
ACCESSION   NP_001229777
VERSION     NP_001229777.1
DBSOURCE    REFSEQ: accession NM_001242848.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Li,W., Han,Q., Zhu,Y., Zhou,Y., Zhang,J., Wu,W., Li,Y., Liu,L.,
            Qiu,Y., Hu,K. and Yin,D.
  TITLE     SUMOylation of RNF146 results in Axin degradation and activation of
            Wnt/beta-catenin signaling to promote the progression of
            hepatocellular carcinoma
  JOURNAL   Oncogene 42 (21), 1728-1740 (2023)
   PUBMED   37029301
  REMARK    GeneRIF: SUMOylation of RNF146 results in Axin degradation and
            activation of Wnt/beta-catenin signaling to promote the progression
            of hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Xu,Y.R., Shi,M.L., Zhang,Y., Kong,N., Wang,C., Xiao,Y.F., Du,S.S.,
            Zhu,Q.Y. and Lei,C.Q.
  TITLE     Tankyrases inhibit innate antiviral response by PARylating
            VISA/MAVS and priming it for RNF146-mediated ubiquitination and
            degradation
  JOURNAL   Proc Natl Acad Sci U S A 119 (26), e2122805119 (2022)
   PUBMED   35733260
  REMARK    GeneRIF: Tankyrases inhibit innate antiviral response by PARylating
            VISA/MAVS and priming it for RNF146-mediated ubiquitination and
            degradation.
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Zhang,Y., Liu,S., Mickanin,C., Feng,Y., Charlat,O., Michaud,G.A.,
            Schirle,M., Shi,X., Hild,M., Bauer,A., Myer,V.E., Finan,P.M.,
            Porter,J.A., Huang,S.M. and Cong,F.
  TITLE     RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin
            degradation and Wnt signalling
  JOURNAL   Nat Cell Biol 13 (5), 623-629 (2011)
   PUBMED   21478859
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Menachem,T.D., Laitman,Y., Kaufman,B. and Friedman,E.
  TITLE     The RNF146 and ECHDC1 genes as candidates for inherited breast and
            ovarian cancer in Jewish Ashkenazi women
  JOURNAL   Fam Cancer 8 (4), 399-402 (2009)
   PUBMED   19517271
  REMARK    GeneRIF: Mutations in the coding regions of the RNF146 and ECHDC1
            genes do not contribute to the burden of inherited predisposition
            of breast cancer in Ashkenazi high risk women.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 358)
  AUTHORS   Gold,B., Kirchhoff,T., Stefanov,S., Lautenberger,J., Viale,A.,
            Garber,J., Friedman,E., Narod,S., Olshen,A.B., Gregersen,P.,
            Kosarin,K., Olsh,A., Bergeron,J., Ellis,N.A., Klein,R.J.,
            Clark,A.G., Norton,L., Dean,M., Boyd,J. and Offit,K.
  TITLE     Genome-wide association study provides evidence for a breast cancer
            risk locus at 6q22.33
  JOURNAL   Proc Natl Acad Sci U S A 105 (11), 4340-4345 (2008)
   PUBMED   18326623
  REMARK    GeneRIF: Genome-wide association study of gene-disease association.
            (HuGE Navigator)
REFERENCE   9  (residues 1 to 358)
  AUTHORS   von Rotz,R.C., Kins,S., Hipfel,R., von der Kammer,H. and
            Nitsch,R.M.
  TITLE     The novel cytosolic RING finger protein dactylidin is up-regulated
            in brains of patients with Alzheimer's disease
  JOURNAL   Eur J Neurosci 21 (5), 1289-1298 (2005)
   PUBMED   15813938
  REMARK    GeneRIF: Dactylidin may function early in the progression of
            Alzheimer's disease.
REFERENCE   10 (residues 1 to 358)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA145911.1 and AJ420549.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR,
            compared to variant 1. Variants 1-7 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4369108.1,
                                           SRR18074967.3455556.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.33"
     Protein         1..358
                     /product="E3 ubiquitin-protein ligase RNF146 isoform a"
                     /EC_number="2.3.2.27"
                     /note="dactylidin; RING-type E3 ubiquitin transferase
                     RNF146; E3 ubiquitin-protein ligase RNF146; iduna"
                     /calculated_mol_wt=38688
     Region          34..83
                     /region_name="RING-HC_RNF146"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 146 (RNF146) and similar proteins; cd16546"
                     /db_xref="CDD:438208"
     Site            order(37..38,40,69,71..72)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438208"
     Region          103..175
                     /region_name="WWE"
                     /note="Domain in Deltex and TRIP12 homologues. Possibly
                     involved in regulation of ubiquitin-mediated proteolysis;
                     smart00678"
                     /db_xref="CDD:128922"
     CDS             1..358
                     /gene="RNF146"
                     /coded_by="NM_001242848.2:302..1378"
                     /note="isoform a is encoded by transcript variant 6"
                     /db_xref="GeneID:81847"
                     /db_xref="HGNC:HGNC:21336"
                     /db_xref="MIM:612137"
ORIGIN      
        1 magcgeidhs inmlptnrka nescsntaps ltvpecaicl qtcvhpvslp ckhvfcylcv
       61 kgaswlgkrc alcrqeiped fldkptllsp eelkaasrgn geyawyyegr ngwwqydert
      121 sreledafsk gkkntemlia gflyvadlen mvqyrrnehg rrrkikrdii dipkkgvagl
      181 rldcdantvn laressadga dsvsaqsgas vqplvssvrp ltsvdgqlts patpspdast
      241 sledsfahlq lsgdntaers hrgegeedhe spssgrvpap dtsieetesd assdsedvsa
      301 vvaqhsltqq rllvsnanqt vpdrsdrsgt drsvagggtv svsvrsrrpd gqctvtev
//
LOCUS       NP_001258719             611 aa            linear   PRI 21-NOV-2025
DEFINITION  cytoplasmic dynein 1 intermediate chain 2 isoform 4 [Homo sapiens].
ACCESSION   NP_001258719
VERSION     NP_001258719.1
DBSOURCE    REFSEQ: accession NM_001271790.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 611)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 611)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 611)
  AUTHORS   Habu,T. and Kim,J.
  TITLE     Dynein intermediate chain 2c (DNCI2c) complex is essential for
            exiting Mad2-dependent spindle assembly checkpoint
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1868 (12), 119120 (2021)
   PUBMED   34400173
  REMARK    GeneRIF: Dynein intermediate chain 2c (DNCI2c) complex is essential
            for exiting Mad2-dependent spindle assembly checkpoint.
REFERENCE   5  (residues 1 to 611)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 611)
  AUTHORS   Sivaram,M.V., Wadzinski,T.L., Redick,S.D., Manna,T. and Doxsey,S.J.
  TITLE     Dynein light intermediate chain 1 is required for progress through
            the spindle assembly checkpoint
  JOURNAL   EMBO J 28 (7), 902-914 (2009)
   PUBMED   19229290
REFERENCE   7  (residues 1 to 611)
  AUTHORS   Pfister,K.K., Fisher,E.M., Gibbons,I.R., Hays,T.S., Holzbaur,E.L.,
            McIntosh,J.R., Porter,M.E., Schroer,T.A., Vaughan,K.T.,
            Witman,G.B., King,S.M. and Vallee,R.B.
  TITLE     Cytoplasmic dynein nomenclature
  JOURNAL   J Cell Biol 171 (3), 411-413 (2005)
   PUBMED   16260502
REFERENCE   8  (residues 1 to 611)
  AUTHORS   Davies,T.H., Ning,Y.M. and Sanchez,E.R.
  TITLE     A new first step in activation of steroid receptors:
            hormone-induced switching of FKBP51 and FKBP52 immunophilins
  JOURNAL   J Biol Chem 277 (7), 4597-4600 (2002)
   PUBMED   11751894
REFERENCE   9  (residues 1 to 611)
  AUTHORS   Crackower,M.A., Sinasac,D.S., Xia,J., Motoyama,J., Prochazka,M.,
            Rommens,J.M., Scherer,S.W. and Tsui,L.C.
  TITLE     Cloning and characterization of two cytoplasmic dynein intermediate
            chain genes in mouse and human
  JOURNAL   Genomics 55 (3), 257-267 (1999)
   PUBMED   10049579
REFERENCE   10 (residues 1 to 611)
  AUTHORS   Vaughan,K.T. and Vallee,R.B.
  TITLE     Cytoplasmic dynein binds dynactin through a direct interaction
            between the intermediate chains and p150Glued
  JOURNAL   J Cell Biol 131 (6 Pt 1), 1507-1516 (1995)
   PUBMED   8522607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA435365.1, AY037160.1 and
            AC068039.6.
            
            Summary: This gene encodes a member of the dynein intermediate
            chain family. The encoded protein is a non-catalytic component of
            the cytoplasmic dynein 1 complex, which acts as a retrograde
            microtubule motor to transport organelles and vesicles. A
            pseudogene of this gene is located on chromosome 10. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Nov 2012].
            
            Transcript Variant: This variant (7) has multiple differences in
            the coding region but maintains the reading frame, compared to
            variant 1. The encoded isoform (4) is shorter, compared to isoform
            1. Both variants 7 and 8 encode the same isoform (4).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.191074.1, AY037160.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..611
                     /product="cytoplasmic dynein 1 intermediate chain 2
                     isoform 4"
                     /note="dynein, cytoplasmic, intermediate polypeptide 2; DH
                     IC-2; dynein intermediate chain 2, cytosolic; testis
                     tissue sperm-binding protein Li 66n"
                     /calculated_mol_wt=68167
     Region          107..137
                     /region_name="Dynein_IC2"
                     /note="Cytoplasmic dynein 1 intermediate chain 2;
                     pfam11540"
                     /db_xref="CDD:463291"
     Region          256..305
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <283..573
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          313..351
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          359..400
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          408..455
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          463..495
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          501..539
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          547..573
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..611
                     /gene="DYNC1I2"
                     /gene_synonym="DIC74; DNCI2; IC2; NEDMIBA"
                     /coded_by="NM_001271790.2:169..2004"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS63057.1"
                     /db_xref="GeneID:1781"
                     /db_xref="HGNC:HGNC:2964"
                     /db_xref="MIM:603331"
ORIGIN      
        1 msdkselkae lerkkqrlaq ireekkrkee erkkketdqk keavapvqee sdlekkrrea
       61 eallqsmglt pespivpppm spssksvstp seagsqdsgd gavgsrrgpi klgmakitqv
      121 dfppreivty tketqtpvma qpkedeeedd dvvapkppie peeektlkkd eendskapph
      181 elteeekqqi lhseeflsff dhstrivera lseqiniffd ysgrdledke geiqagakls
      241 lnrqffderw skhrvvscld wssqypellv asynnnedap hepdgvalvw nmkykkttpe
      301 yvfhcqsavm satfakfhpn lvvggtysgq ivlwdnrsnk rtpvqrtpls aaahthpvyc
      361 vnvvgtqnah nlisistdgk icswsldmls hpqdsmelvh kqskavavts msfpvgdvnn
      421 fvvgseegsv ytacrhgska gisemfeghq gpitgihcha avgavdfshl fvtssfdwtv
      481 klwttknnkp lysfednady vydvmwspth palfacvdgm grldlwnlnn dtevptasis
      541 vegnpalnrv rwthsgreia vgdsegqivi ydvgeiavpr ndewarfgrt laeinanrad
      601 aeeeaatrip a
//
LOCUS       NP_001139523             275 aa            linear   PRI 21-NOV-2025
DEFINITION  inactive hydroxysteroid dehydrogenase-like protein 1 isoform b
            [Homo sapiens].
ACCESSION   NP_001139523
VERSION     NP_001139523.1
DBSOURCE    REFSEQ: accession NM_001146051.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Meier,M., Tokarz,J., Haller,F., Mindnich,R. and Adamski,J.
  TITLE     Human and zebrafish hydroxysteroid dehydrogenase like 1 (HSDL1)
            proteins are inactive enzymes but conserved among species
  JOURNAL   Chem Biol Interact 178 (1-3), 197-205 (2009)
   PUBMED   19026618
  REMARK    GeneRIF: characterized the subcellular localization as well as the
            tissue distribution and performed a screen for putative substrates
            of HSDL1 enzymes
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC306668.1, AK299798.1, BC104218.1, BC018084.1, AK025626.1,
            AK074878.1, DB525323.1 and H40440.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            segment in the coding region, compared to variant 1. The encoded
            isoform (b) is shorter compared to isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2876111.1,
                                           SRR18074967.1762839.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.1"
     Protein         1..275
                     /product="inactive hydroxysteroid dehydrogenase-like
                     protein 1 isoform b"
                     /note="inactive hydroxysteroid dehydrogenase-like protein
                     1; steroid dehydrogenase-like protein; short chain
                     dehydrogenase/reductase family 12C member 3"
                     /calculated_mol_wt=30730
     Region          67..254
                     /region_name="17beta-HSD1_like_SDR_c"
                     /note="17-beta-hydroxysteroid dehydrogenases (17beta-HSDs)
                     types -1, -3, and -12, -like, classical (c) SDRs; cd05356"
                     /db_xref="CDD:187614"
     Site            order(122,150,163,167)
                     /site_type="active"
                     /db_xref="CDD:187614"
     CDS             1..275
                     /gene="HSDL1"
                     /gene_synonym="SDR12C3"
                     /coded_by="NM_001146051.2:167..994"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54046.1"
                     /db_xref="GeneID:83693"
                     /db_xref="HGNC:HGNC:16475"
                     /db_xref="MIM:619067"
ORIGIN      
        1 maavdsfyll yreiarscnc ymealalvga wytarksitv icdfyslirl hfiprlgsra
       61 dlikqygrwa vvsgatdgig kayaeelasr glniilisrn eeklqyftql sedklwdiin
      121 vniaaaslmv hvvlpgmver kkgaivtiss gscckptpql aafsaskayl dhfsralqye
      181 yaskgifvqs lipfyvatsm tapsnflhrc swlvpspkvy ahhavstlgi skrttgywsh
      241 siqflfaqym pewlwvwgan ilnrslrkea lscta
//
LOCUS       NP_001341361             862 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA-processing factor 40 homolog A isoform 3 [Homo sapiens].
ACCESSION   NP_001341361
VERSION     NP_001341361.1
DBSOURCE    REFSEQ: accession NM_001354432.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Choudhary,B. and Norris,A.
  TITLE     Conserved role for spliceosomal component PRPF40A in microexon
            splicing
  JOURNAL   RNA 31 (1), 43-50 (2024)
   PUBMED   39389624
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 862)
  AUTHORS   Martinez-Lumbreras,S., Trager,L.K., Mulorz,M.M., Payr,M.,
            Dikaya,V., Hipp,C., Konig,J. and Sattler,M.
  TITLE     Intramolecular autoinhibition regulates the selectivity of PRPF40A
            tandem WW domains for proline-rich motifs
  JOURNAL   Nat Commun 15 (1), 3888 (2024)
   PUBMED   38719828
  REMARK    GeneRIF: Intramolecular autoinhibition regulates the selectivity of
            PRPF40A tandem WW domains for proline-rich motifs.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 862)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 862)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 862)
  AUTHORS   Allen,M., Friedler,A., Schon,O. and Bycroft,M.
  TITLE     The structure of an FF domain from human HYPA/FBP11
  JOURNAL   J Mol Biol 323 (3), 411-416 (2002)
   PUBMED   12381297
  REMARK    GeneRIF: Data describe the structure of an FF domain from
            HYPA/FBP11, which differs from those of other
            phosphopeptide-binding domains and represents a novel
            phosphopeptide-binding fold.
REFERENCE   7  (residues 1 to 862)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   8  (residues 1 to 862)
  AUTHORS   Bedford,M.T., Reed,R. and Leder,P.
  TITLE     WW domain-mediated interactions reveal a spliceosome-associated
            protein that binds a third class of proline-rich motif: the proline
            glycine and methionine-rich motif
  JOURNAL   Proc Natl Acad Sci U S A 95 (18), 10602-10607 (1998)
   PUBMED   9724750
REFERENCE   9  (residues 1 to 862)
  AUTHORS   Faber,P.W., Barnes,G.T., Srinidhi,J., Chen,J., Gusella,J.F. and
            MacDonald,M.E.
  TITLE     Huntingtin interacts with a family of WW domain proteins
  JOURNAL   Hum Mol Genet 7 (9), 1463-1474 (1998)
   PUBMED   9700202
REFERENCE   10 (residues 1 to 862)
  AUTHORS   Chan,D.C., Bedford,M.T. and Leder,P.
  TITLE     Formin binding proteins bear WWP/WW domains that bind proline-rich
            peptides and functionally resemble SH3 domains
  JOURNAL   EMBO J 15 (5), 1045-1054 (1996)
   PUBMED   8605874
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079344.5 and AC012443.8.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (3) is
            shorter at the N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q23.3"
     Protein         1..862
                     /product="pre-mRNA-processing factor 40 homolog A isoform
                     3"
                     /note="formin binding protein 3; Huntingtin-interacting
                     protein A; NY-REN-6 antigen; Fas-ligand associated factor
                     1; formin-binding protein 11; huntingtin yeast partner A;
                     fas ligand-associated factor 1; pre-mRNA processing factor
                     40 homolog A; renal carcinoma antigen NY-REN-6;
                     huntingtin-interacting protein 10; PRP40 pre-mRNA
                     processing factor 40 homolog A"
                     /calculated_mol_wt=98658
     Region          38..701
                     /region_name="PRP40"
                     /note="Splicing factor [RNA processing and modification];
                     COG5104"
                     /db_xref="CDD:227435"
     CDS             1..862
                     /gene="PRPF40A"
                     /gene_synonym="FBP-11; FBP11; FLAF1; FNBP3; HIP-10; HIP10;
                     HYPA; NY-REN-6; Prp40"
                     /coded_by="NM_001354432.4:656..3244"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:55660"
                     /db_xref="HGNC:HGNC:16463"
                     /db_xref="MIM:612941"
ORIGIN      
        1 mpgmmssvmp gmmmshmsqa smqpalppgv nsmdvaagta sgaksmwteh kspdgrtyyy
       61 ntetkqstwe kpddlktpae qllskcpwke yksdsgkpyy ynsqtkesrw akpkeledle
      121 gyqntivags litksnlham ikaeesskqe ectttstapv ptteipttms tmaaaeaaaa
      181 vvaaaaaaaa aaaaananas tsasntvsgt vpvvpepevt sivatvvdne ntvtisteeq
      241 aqltstpaiq dqsvevssnt geetskqetv adftpkkeee esqpakktyt wntkeeakqa
      301 fkellkekrv psnasweqam kmiindprys alaklsekkq afnaykvqte keekeearsk
      361 ykeakesfqr flenhekmts ttrykkaeqm fgemevwnai serdrleiye dvlfflskke
      421 keqakqlrkr nwealknild nmanvtystt wseaqqylmd nptfaedeel qnmdkedali
      481 cfeehirale keeeeekqks llrerrrqrk nresfqifld elhehgqlhs msswmelypt
      541 issdirftnm lgqpvfslgs taldlfkfyv edlkaryhde kkiikdilkd kgfvvevntt
      601 fedfvaiiss tkrsttldag niklafnsll ekaearerer ekeearkmkr kesafksmlk
      661 qaappielda vwedirerfv kepafeditl eserkrifkd fmhvlehecq hhhsknkkhs
      721 kkskkhhrkr srsrsgsdsd dddshskkkr qrsesrsase hsssaesers ykkskkhkkk
      781 skkrrhksds pesdaerekd kkekdresek drtrqrsesk hkspkkktgk dsgnwdtsgs
      841 elsegelekr rrtlleqldd dq
//
LOCUS       NP_001365906             510 aa            linear   PRI 21-NOV-2025
DEFINITION  F-box/WD repeat-containing protein 11 isoform G [Homo sapiens].
ACCESSION   NP_001365906 XP_005265915
VERSION     NP_001365906.1
DBSOURCE    REFSEQ: accession NM_001378977.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Tan,P., Cai,S., Huang,Z., Li,M., Liu,S., Chen,J., Fu,W. and Zhao,L.
  TITLE     E3 ubiquitin ligase FBXW11 as a novel inflammatory biomarker is
            associated with immune infiltration and NF-kappaB pathway
            activation in pancreatitis and pancreatic cancer
  JOURNAL   Cell Signal 116, 111033 (2024)
   PUBMED   38182068
  REMARK    GeneRIF: E3 ubiquitin ligase FBXW11 as a novel inflammatory
            biomarker is associated with immune infiltration and NF-kappaB
            pathway activation in pancreatitis and pancreatic cancer.
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Dalle Carbonare,L., Gomez Lira,M., Minoia,A., Bertacco,J., Orsi,S.,
            Lauriola,A., Li Vigni,V., Gandini,A., Antoniazzi,F., Zipeto,D.,
            Mottes,M., Bhandary,L., Guardavaccaro,D. and Valenti,M.T.
  TITLE     Expression of FBXW11 in normal and disease-associated osteogenic
            cells
  JOURNAL   J Cell Mol Med 27 (11), 1580-1591 (2023)
   PUBMED   37199076
  REMARK    GeneRIF: Expression of FBXW11 in normal and disease-associated
            osteogenic cells.
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Nardone,C., Palanski,B.A., Scott,D.C., Timms,R.T., Barber,K.W.,
            Gu,X., Mao,A., Leng,Y., Watson,E.V., Schulman,B.A., Cole,P.A. and
            Elledge,S.J.
  TITLE     A central role for regulated protein stability in the control of
            TFE3 and MITF by nutrients
  JOURNAL   Mol Cell 83 (1), 57-73 (2023)
   PUBMED   36608670
REFERENCE   5  (residues 1 to 510)
  AUTHORS   Chen,C., Zhou,H., Zhang,X., Liu,Z. and Ma,X.
  TITLE     Association of FBXW11 levels with tumor development and prognosis
            in chondrosarcoma
  JOURNAL   Cancer Biomark 35 (4), 429-437 (2022)
   PUBMED   36404534
  REMARK    GeneRIF: Association of FBXW11 levels with tumor development and
            prognosis in chondrosarcoma.
REFERENCE   6  (residues 1 to 510)
  AUTHORS   Koike,J., Sagara,N., Kirikoshi,H., Takagi,A., Miwa,T., Hirai,M. and
            Katoh,M.
  TITLE     Molecular cloning and genomic structure of the betaTRCP2 gene on
            chromosome 5q35.1
  JOURNAL   Biochem Biophys Res Commun 269 (1), 103-109 (2000)
   PUBMED   10694485
REFERENCE   7  (residues 1 to 510)
  AUTHORS   Suzuki,H., Chiba,T., Suzuki,T., Fujita,T., Ikenoue,T., Omata,M.,
            Furuichi,K., Shikama,H. and Tanaka,K.
  TITLE     Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds to
            IkappaBalpha for signal-dependent ubiquitination
  JOURNAL   J Biol Chem 275 (4), 2877-2884 (2000)
   PUBMED   10644755
REFERENCE   8  (residues 1 to 510)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
REFERENCE   9  (residues 1 to 510)
  AUTHORS   Ohta,T., Michel,J.J., Schottelius,A.J. and Xiong,Y.
  TITLE     ROC1, a homolog of APC11, represents a family of cullin partners
            with an associated ubiquitin ligase activity
  JOURNAL   Mol Cell 3 (4), 535-541 (1999)
   PUBMED   10230407
REFERENCE   10 (residues 1 to 510)
  AUTHORS   Fuchs,S.Y., Chen,A., Xiong,Y., Pan,Z.Q. and Ronai,Z.
  TITLE     HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and
            Cullin1 and targets the phosphorylation-dependent degradation of
            IkappaB and beta-catenin
  JOURNAL   Oncogene 18 (12), 2039-2046 (1999)
   PUBMED   10321728
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC113342.2, AC011387.5 and
            AC011410.6.
            
            On Mar 17, 2020 this sequence version replaced XP_005265915.1.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box),
            which function in phosphorylation-dependent ubiquitination. The
            F-box proteins are divided into 3 classes: Fbws containing WD-40
            domains, Fbls containing leucine-rich repeats, and Fbxs containing
            either different protein-protein interaction modules or no
            recognizable motifs. The protein encoded by this gene belongs to
            the Fbws class and, in addition to an F-box, contains multiple WD40
            repeats. This gene contains at least 14 exons, and its alternative
            splicing generates 3 transcript variants diverging at the
            presence/absence of two alternate exons. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853564.22872.1,
                                           SRR11853563.27458.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.1"
     Protein         1..510
                     /product="F-box/WD repeat-containing protein 11 isoform G"
                     /note="F-box and WD-40 domain protein 11; F-box and WD-40
                     domain protein 1B; beta-transducin repeat-containing
                     protein 2; F-box protein Fbw1b; F-box/WD repeat-containing
                     protein 11; homologous to Slimb protein; F-box/WD
                     repeat-containing protein 1B; F-box and WD repeats protein
                     beta-TrCP2"
                     /calculated_mol_wt=58634
     Region          46..84
                     /region_name="Beta-TrCP_D"
                     /note="D domain of beta-TrCP; pfam12125"
                     /db_xref="CDD:463465"
     Region          84..134
                     /region_name="F-box_FBXW1B"
                     /note="F-box domain found in F-box/WD repeat-containing
                     protein 1B (FBXW1B) and similar proteins; cd22183"
                     /db_xref="CDD:438954"
     Site            order(84..87,90..91,96,98..99,103,106..108,111,113..114,
                     116..120,122..123)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438954"
     Region          211..246
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <217..486
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          252..286
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          291..328
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          335..368
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          374..408
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          414..457
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          463..485
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..510
                     /gene="FBXW11"
                     /gene_synonym="BTRC2; BTRCP2; Fbw11; FBW1B; FBXW1B; Hos;
                     NEDJED"
                     /coded_by="NM_001378977.1:356..1888"
                     /note="isoform G is encoded by transcript variant 7"
                     /db_xref="GeneID:23291"
                     /db_xref="HGNC:HGNC:13607"
                     /db_xref="MIM:605651"
ORIGIN      
        1 medqnedesp kkntlwqisn gtssvivsrk rpsegnyqke kdlcikyfdq wsesdqvefv
       61 ehlisrmchy qhghinsylk pmlqrdfita lpeqgldhia enilsyldar slcaaelvck
      121 ewqrvisegm lwkkliermv rtdplwkgls errgwdqylf knrptdgppn sfyrslypki
      181 iqdietiesn wrcgrhnlqr iqcrsenskg vyclqyddek iisglrdnsi kiwdktslec
      241 lkvltghtgs vlclqyderv ivtgssdstv rvwdvntgev lntlihhnea vlhlrfsngl
      301 mvtcskdrsi avwdmasatd itlrrvlvgh raavnvvdfd dkyivsasgd rtikvwstst
      361 cefvrtlngh krgiaclqyr drlvvsgssd ntirlwdiec gaclrvlegh eelvrcirfd
      421 nkrivsgayd gkikvwdlqa aldprapast lclrtlvehs grvfrlqfde fqiissshdd
      481 tiliwdflnv ppsaqnetrs psrtytyisr
//
LOCUS       NP_001334963             449 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 1 isoform r [Homo sapiens].
ACCESSION   NP_001334963
VERSION     NP_001334963.1
DBSOURCE    REFSEQ: accession NM_001348034.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Petersen,M. and Dubielecka,P.
  TITLE     Adaptor protein Abelson interactor 1 in homeostasis and disease
  JOURNAL   Cell Commun Signal 22 (1), 468 (2024)
   PUBMED   39354505
  REMARK    GeneRIF: Adaptor protein Abelson interactor 1 in homeostasis and
            disease.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Jin,M., Xie,M., Liu,Y., Song,H., Zhang,M., Li,W., Li,X., Jia,N.,
            Dong,L., Lu,Q., Xue,F., Yan,L. and Yu,Q.
  TITLE     Circulating miR-30e-3p induces disruption of neurite development in
            SH-SY5Y cells by targeting ABI1, a novel biomarker for
            schizophrenia
  JOURNAL   J Psychiatr Res 174, 84-93 (2024)
   PUBMED   38626565
  REMARK    GeneRIF: Circulating miR-30e-3p induces disruption of neurite
            development in SH-SY5Y cells by targeting ABI1, a novel biomarker
            for schizophrenia.
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Lin,T., Guo,J., Peng,Y., Li,M., Liu,Y., Yu,X., Wu,N. and Yu,W.
  TITLE     Pan-cancer transcriptomic data of ABI1 transcript variants and
            molecular constitutive elements identifies novel cancer metastatic
            and prognostic biomarkers
  JOURNAL   Cancer Biomark 39 (1), 49-62 (2024)
   PUBMED   37545215
  REMARK    GeneRIF: Pan-cancer transcriptomic data of ABI1 transcript variants
            and molecular constitutive elements identifies novel cancer
            metastatic and prognostic biomarkers.
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Fan,P.D. and Goff,S.P.
  TITLE     Abl interactor 1 binds to sos and inhibits epidermal growth factor-
            and v-Abl-induced activation of extracellular signal-regulated
            kinases
  JOURNAL   Mol Cell Biol 20 (20), 7591-7601 (2000)
   PUBMED   11003655
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Scita,G., Nordstrom,J., Carbone,R., Tenca,P., Giardina,G.,
            Gutkind,S., Bjarnegard,M., Betsholtz,C. and Di Fiore,P.P.
  TITLE     EPS8 and E3B1 transduce signals from Ras to Rac
  JOURNAL   Nature 401 (6750), 290-293 (1999)
   PUBMED   10499589
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Taki,T., Shibuya,N., Taniwaki,M., Hanada,R., Morishita,K.,
            Bessho,F., Yanagisawa,M. and Hayashi,Y.
  TITLE     ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL
            gene in acute myeloid leukemia with t(10;11)(p11.2;q23)
  JOURNAL   Blood 92 (4), 1125-1130 (1998)
   PUBMED   9694699
REFERENCE   9  (residues 1 to 449)
  AUTHORS   Ziemnicka-Kotula,D., Xu,J., Gu,H., Potempska,A., Kim,K.S.,
            Jenkins,E.C., Trenkner,E. and Kotula,L.
  TITLE     Identification of a candidate human spectrin Src homology 3
            domain-binding protein suggests a general mechanism of association
            of tyrosine kinases with the spectrin-based membrane skeleton
  JOURNAL   J Biol Chem 273 (22), 13681-13692 (1998)
   PUBMED   9593709
REFERENCE   10 (residues 1 to 449)
  AUTHORS   Biesova,Z., Piccoli,C. and Wong,W.T.
  TITLE     Isolation and characterization of e3B1, an eps8 binding protein
            that regulates cell growth
  JOURNAL   Oncogene 14 (2), 233-241 (1997)
   PUBMED   9010225
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139404.9 and AL390961.17.
            
            Summary: This gene encodes a member of the Abelson-interactor
            family of adaptor proteins. These proteins facilitate signal
            transduction as components of several multiprotein complexes, and
            regulate actin polymerization and cytoskeletal remodeling through
            interactions with Abelson tyrosine kinases. The encoded protein
            plays a role in macropinocytosis as a component of the WAVE2
            complex, and also forms a complex with EPS8 and SOS1 that mediates
            signal transduction from Ras to Rac. This gene may play a role in
            the progression of several malignancies including melanoma, colon
            cancer and breast cancer, and a t(10;11) chromosomal translocation
            involving this gene and the MLL gene has been associated with acute
            myeloid leukemia. Alternatively spliced transcript variants
            encoding multiple isoforms have been observed for this gene, and a
            pseudogene of this gene is located on the long arm of chromosome
            14. [provided by RefSeq, Sep 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.85597.1,
                                           SRR1803617.374006.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.1"
     Protein         1..449
                     /product="abl interactor 1 isoform r"
                     /note="nap1 binding protein; interactor protein AblBP4;
                     Abl-interactor protein 1 long; Abelson interactor 1;
                     abl-binding protein 4; eps8 SH3 domain-binding protein;
                     spectrin SH3 domain-binding protein 1"
                     /calculated_mol_wt=48868
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.13,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Region          18..79
                     /region_name="Required for binding to WASF1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZM5; propagated from
                     UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Region          93..156
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Site            95..96
                     /site_type="other"
                     /note="Breakpoint for translocation to form
                     KMT2A/MLL1-ABI1; propagated from UniProtKB/Swiss-Prot
                     (Q8IZP0.4)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1.
                     /evidence=ECO:0000269|PubMed:18328268,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8CBW3; propagated from
                     UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Region          391..449
                     /region_name="SH3_Abi1"
                     /note="Src homology 3 domain of Abl Interactor 1; cd11971"
                     /db_xref="CDD:212904"
     Site            order(396,398,401,405,423..424,437,439..440)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212904"
     CDS             1..449
                     /gene="ABI1"
                     /gene_synonym="ABI-1; ABLBP4; E3B1; NAP1BP; SSH3BP;
                     SSH3BP1"
                     /coded_by="NM_001348034.2:96..1445"
                     /note="isoform r is encoded by transcript variant 18"
                     /db_xref="GeneID:10006"
                     /db_xref="HGNC:HGNC:11320"
                     /db_xref="MIM:603050"
ORIGIN      
        1 maelqmllee eipsgkrali esyqnltrva dycennyiqa tdkrkaleet kayttqslas
       61 vayqinalan nvlqlldiqa sqlrrmessi nhisqtvdih kekvarreig ilttnkntsr
      121 thkiiapanm erpvryirkp idytvlddvg hgvkwlkakh gnnqpartgt lsrtnpptqk
      181 ppsppmsgrg tlgrntpykt lepvkpptvp ndymtsparl gsqhspgrta slnqrprths
      241 gssggsgsre nsgsssigip iavptpsppt igpenisvpp psgappappl apllpvstvi
      301 vsiapppppm pqltpqiplt gfvarvqeni adsptppppp ppddipmfdd sppppppppv
      361 dyedeeaavv qyndpyadgd pawapknyie kvvaiydytk dkddelsfme gaiiyvikkn
      421 ddgwyegvcn rvtglfpgny vesimhytd
//
LOCUS       NP_001139247             457 aa            linear   PRI 21-NOV-2025
DEFINITION  peptidyl-prolyl cis-trans isomerase FKBP5 isoform 1 [Homo sapiens].
ACCESSION   NP_001139247
VERSION     NP_001139247.1
DBSOURCE    REFSEQ: accession NM_001145775.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Zhang,Y., Yue,W. and Li,J.
  TITLE     The association of FKBP5 gene polymorphism with genetic
            susceptibility to depression and response to antidepressant
            treatment- a systematic review
  JOURNAL   BMC Psychiatry 24 (1), 274 (2024)
   PUBMED   38609904
  REMARK    GeneRIF: The association of FKBP5 gene polymorphism with genetic
            susceptibility to depression and response to antidepressant
            treatment- a systematic review.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Zimmer,C., Jimeno,B. and Martin,L.B.
  TITLE     HPA flexibility and FKBP5: promising physiological targets for
            conservation
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 379 (1898), 20220512 (2024)
   PUBMED   38310934
  REMARK    GeneRIF: HPA flexibility and FKBP5: promising physiological targets
            for conservation.
            Review article
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Grossmann,N.L., Weihs,A., Kuhn,L., Sauer,S., Roh,S., Wiechmann,T.,
            Rex-Haffner,M., Volzke,H., Volker,U., Binder,E.B., Teumer,A.,
            Homuth,G., Klinger-Konig,J. and Grabe,H.J.
  TITLE     Methylation Patterns of the FKBP5 Gene in Association with
            Childhood Maltreatment and Depressive Disorders
  JOURNAL   Int J Mol Sci 25 (3), 1485 (2024)
   PUBMED   38338761
  REMARK    GeneRIF: Methylation Patterns of the FKBP5 Gene in Association with
            Childhood Maltreatment and Depressive Disorders.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 457)
  AUTHORS   Stroud,L.R., Jao,N.C., Ward,L.G., Lee,S.Y. and Marsit,C.J.
  TITLE     Differential impact of prenatal PTSD symptoms and preconception
            trauma exposure on placental NR3C1 and FKBP5 methylation
  JOURNAL   Stress 27 (1), 2321595 (2024)
   PUBMED   38676353
  REMARK    GeneRIF: Differential impact of prenatal PTSD symptoms and
            preconception trauma exposure on placental NR3C1 and FKBP5
            methylation.
REFERENCE   6  (residues 1 to 457)
  AUTHORS   Nair,S.C., Rimerman,R.A., Toran,E.J., Chen,S., Prapapanich,V.,
            Butts,R.N. and Smith,D.F.
  TITLE     Molecular cloning of human FKBP51 and comparisons of immunophilin
            interactions with Hsp90 and progesterone receptor
  JOURNAL   Mol Cell Biol 17 (2), 594-603 (1997)
   PUBMED   9001212
REFERENCE   7  (residues 1 to 457)
  AUTHORS   Johnson,J., Corbisier,R., Stensgard,B. and Toft,D.
  TITLE     The involvement of p23, hsp90, and immunophilins in the assembly of
            progesterone receptor complexes
  JOURNAL   J Steroid Biochem Mol Biol 56 (1-6 Spec No), 31-37 (1996)
   PUBMED   8603045
REFERENCE   8  (residues 1 to 457)
  AUTHORS   Baughman,G., Wiederrecht,G.J., Campbell,N.F., Martin,M.M. and
            Bourgeois,S.
  TITLE     FKBP51, a novel T-cell-specific immunophilin capable of calcineurin
            inhibition
  JOURNAL   Mol Cell Biol 15 (8), 4395-4402 (1995)
   PUBMED   7542743
REFERENCE   9  (residues 1 to 457)
  AUTHORS   Smith,D.F., Albers,M.W., Schreiber,S.L., Leach,K.L. and Deibel,M.R.
            Jr.
  TITLE     FKBP54, a novel FK506-binding protein in avian progesterone
            receptor complexes and HeLa extracts
  JOURNAL   J Biol Chem 268 (32), 24270-24273 (1993)
   PUBMED   7693698
REFERENCE   10 (residues 1 to 457)
  AUTHORS   Smith,D.F., Baggenstoss,B.A., Marion,T.N. and Rimerman,R.A.
  TITLE     Two FKBP-related proteins are associated with progesterone receptor
            complexes
  JOURNAL   J Biol Chem 268 (24), 18365-18371 (1993)
   PUBMED   7688746
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC042605.1, KF458140.1,
            AL033519.42 and AW182642.1.
            
            Summary: The protein encoded by this gene is a member of the
            immunophilin protein family, which play a role in immunoregulation
            and basic cellular processes involving protein folding and
            trafficking. This encoded protein is a cis-trans prolyl isomerase
            that binds to the immunosuppressants FK506 and rapamycin. It is
            thought to mediate calcineurin inhibition. It also interacts
            functionally with mature hetero-oligomeric progesterone receptor
            complexes along with the 90 kDa heat shock protein and P23 protein.
            This gene has been found to have multiple polyadenylation sites.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC042605.1, SRR14038197.2295202.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467147, SAMN04284274
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..457
                     /product="peptidyl-prolyl cis-trans isomerase FKBP5
                     isoform 1"
                     /EC_number="5.2.1.8"
                     /note="54 kDa progesterone receptor-associated
                     immunophilin; T-cell FK506-binding protein; peptidylprolyl
                     cis-trans isomerase; rotamase; FF1 antigen; HSP90-binding
                     immunophilin; peptidyl-prolyl cis-trans isomerase FKBP5;
                     androgen-regulated protein 6; FKBP-51; 51 kDa FKBP; PPIase
                     FKBP5; FK506 binding protein 5; 51 kDa FK506-binding
                     protein"
                     /calculated_mol_wt=51081
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13451.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q13451.2)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13451.2)"
     Site            28
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:28147277; propagated from
                     UniProtKB/Swiss-Prot (Q13451.2)"
     Region          43..135
                     /region_name="FKBP_C"
                     /note="FKBP-type peptidyl-prolyl cis-trans isomerase;
                     pfam00254"
                     /db_xref="CDD:459735"
     Site            155
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:28147277; propagated from
                     UniProtKB/Swiss-Prot (Q13451.2)"
     Region          266..>403
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          268..301
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13451.2)"
     Region          268..296
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          317..350
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13451.2)"
     Region          319..345
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(321..322,325..326,328,352,355..356,359..360,
                     362..363,386,389..390,393..394,397)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          350..380
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          351..384
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13451.2)"
     Region          420..457
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13451.2)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13451.2)"
     CDS             1..457
                     /gene="FKBP5"
                     /gene_synonym="AIG6; FKBP51; FKBP54; P54; PPIase; Ptg-10"
                     /coded_by="NM_001145775.3:317..1690"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4808.1"
                     /db_xref="GeneID:2289"
                     /db_xref="HGNC:HGNC:3721"
                     /db_xref="MIM:602623"
ORIGIN      
        1 mttdegaknn eesptatvae qgeditskkd rgvlkivkrv gngeetpmig dkvyvhykgk
       61 lsngkkfdss hdrnepfvfs lgkgqvikaw digvatmkkg eichllckpe yaygsagslp
      121 kipsnatlff eielldfkge dlfedggiir rtkrkgegys npnegatvei hlegrcggrm
      181 fdcrdvaftv gegedhdipi gidkalekmq reeqcilylg prygfgeagk pkfgiepnae
      241 liyevtlksf ekakeswemd tkekleqaai vkekgtvyfk ggkymqaviq ygkivswlem
      301 eyglsekesk asesfllaaf lnlamcylkl reytkavecc dkalgldsan ekglyrrgea
      361 qllmnefesa kgdfekvlev npqnkaarlq ismcqkkake hnerdrriya nmfkkfaeqd
      421 akeeankamg kktsegvtne kgtdsqamee ekpeghv
//
LOCUS       NP_001129473             542 aa            linear   PRI 21-NOV-2025
DEFINITION  tyrosine-protein kinase ABL2 isoform e [Homo sapiens].
ACCESSION   NP_001129473
VERSION     NP_001129473.1
DBSOURCE    REFSEQ: accession NM_001136001.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Miao,Y. and Liu,J.
  TITLE     Tumor-suppressive action of miR-30a-5p in lung adenocarcinoma
            correlates with ABL2 inhibition and PI3K/AKT pathway inactivation
  JOURNAL   Clin Transl Oncol 26 (2), 398-413 (2024)
   PUBMED   37479901
  REMARK    GeneRIF: Tumor-suppressive action of miR-30a-5p in lung
            adenocarcinoma correlates with ABL2 inhibition and PI3K/AKT pathway
            inactivation.
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Kabirova,M., Reichenstein,M., Borovok,N., Sheinin,A., Gorobets,D.
            and Michaelevski,I.
  TITLE     Abl2 Kinase Differentially Regulates iGluRs Current Activity and
            Synaptic Localization
  JOURNAL   Cell Mol Neurobiol 43 (6), 2785-2799 (2023)
   PUBMED   36689065
  REMARK    GeneRIF: Abl2 Kinase Differentially Regulates iGluRs Current
            Activity and Synaptic Localization.
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Wu,K., Wu,H., Lyu,W., Kim,Y., Furdui,C.M., Anderson,K.S. and
            Koleske,A.J.
  TITLE     Platelet-derived growth factor receptor beta activates Abl2 via
            direct binding and phosphorylation
  JOURNAL   J Biol Chem 297 (1), 100883 (2021)
   PUBMED   34144039
  REMARK    GeneRIF: Platelet-derived growth factor receptor beta activates
            Abl2 via direct binding and phosphorylation.
REFERENCE   5  (residues 1 to 542)
  AUTHORS   Bianchi,C., Torsello,B., Angeloni,V., Bombelli,S., Soldi,M.,
            Invernizzi,L., Brambilla,P. and Perego,R.A.
  TITLE     Eight full-length abelson related gene (Arg) isoforms are
            constitutively expressed in caki-1 cell line and cell distribution
            of two isoforms has been analyzed after transfection
  JOURNAL   J Cell Biochem 105 (5), 1219-1227 (2008)
   PUBMED   18810762
REFERENCE   6  (residues 1 to 542)
  AUTHORS   Perego,R.A., Corizzato,M., Bianchi,C., Eroini,B. and Bosari,S.
  TITLE     N- and C-terminal isoforms of Arg quantified by real-time PCR are
            specifically expressed in human normal and neoplastic cells, in
            neoplastic cell lines, and in HL-60 cell differentiation
  JOURNAL   Mol Carcinog 42 (4), 229-239 (2005)
   PUBMED   15765532
REFERENCE   7  (residues 1 to 542)
  AUTHORS   Wang,B. and Kruh,G.D.
  TITLE     Subcellular localization of the Arg protein tyrosine kinase
  JOURNAL   Oncogene 13 (1), 193-197 (1996)
   PUBMED   8700546
REFERENCE   8  (residues 1 to 542)
  AUTHORS   Muller,A.J., Pendergast,A.M., Havlik,M.H., Puil,L., Pawson,T. and
            Witte,O.N.
  TITLE     A limited set of SH2 domains binds BCR through a high-affinity
            phosphotyrosine-independent interaction
  JOURNAL   Mol Cell Biol 12 (11), 5087-5093 (1992)
   PUBMED   1383690
REFERENCE   9  (residues 1 to 542)
  AUTHORS   Kruh,G.D., Perego,R., Miki,T. and Aaronson,S.A.
  TITLE     The complete coding sequence of arg defines the Abelson subfamily
            of cytoplasmic tyrosine kinases
  JOURNAL   Proc Natl Acad Sci U S A 87 (15), 5802-5806 (1990)
   PUBMED   2198571
REFERENCE   10 (residues 1 to 542)
  AUTHORS   Kruh,G.D., King,C.R., Kraus,M.H., Popescu,N.C., Amsbaugh,S.C.,
            McBride,W.O. and Aaronson,S.A.
  TITLE     A novel human gene closely related to the abl proto-oncogene
  JOURNAL   Science 234 (4783), 1545-1548 (1986)
   PUBMED   3787260
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL512326.25, AK311045.1 and
            BC065912.1.
            
            Summary: This gene encodes a member of the Abelson family of
            nonreceptor tyrosine protein kinases. The protein is highly similar
            to the c-abl oncogene 1 protein, including the tyrosine kinase, SH2
            and SH3 domains, and it plays a role in cytoskeletal rearrangements
            through its C-terminal F-actin- and microtubule-binding sequences.
            This gene is expressed in both normal and tumor cells, and is
            involved in translocation with the ets variant 6 gene in leukemia.
            Multiple alternatively spliced transcript variants encoding
            different protein isoforms have been found for this gene. [provided
            by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (e) lacks an alternate in-frame
            exon in the 5' coding region, and differs in the 3' coding region
            and 3' UTR, compared to variant b. The resulting isoform (e) has a
            distinct C-terminus and is shorter than isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK311045.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..542
                     /product="tyrosine-protein kinase ABL2 isoform e"
                     /EC_number="2.7.10.2"
                     /note="tyrosine-protein kinase ARG; abelson-related gene
                     protein; Abelson tyrosine-protein kinase 2; c-abl oncogene
                     2, non-receptor tyrosine kinase; v-abl Abelson murine
                     leukemia viral oncogene homolog 2"
                     /calculated_mol_wt=60733
     Region          90..143
                     /region_name="SH3_Abl"
                     /note="Src homology 3 domain of the Protein Tyrosine
                     Kinase, Abelson kinase; cd11850"
                     /db_xref="CDD:212784"
     Site            order(95,97,100..102,104,119,123..124,135,137,139..140)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212784"
     Site            order(99..102,121,123)
                     /site_type="other"
                     /note="PTKc domain interface [polypeptide binding]"
                     /db_xref="CDD:212784"
     Region          148..241
                     /region_name="SH2_ABL"
                     /note="Src homology 2 (SH2) domain found in Abelson murine
                     lymphosarcoma virus (ABL) proteins; cd09935"
                     /db_xref="CDD:198189"
     Site            order(159,187,200)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198189"
     Region          260..522
                     /region_name="PTKc_Abl"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Abelson kinase; cd05052"
                     /db_xref="CDD:270645"
     Site            order(273,275..277,294,296,341,343,347,395,406,424..426,
                     428,436,470,474)
                     /site_type="active"
                     /db_xref="CDD:270645"
     Site            order(273,275,278,294,296,311,315,324,340..341,343,347,
                     395,405..406)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270645"
     Site            order(288..289,319..321,325,367,399..400,518..519)
                     /site_type="other"
                     /note="SH3/SH2 domain interface [polypeptide binding]"
                     /db_xref="CDD:270645"
     Site            order(365..366,369,454,457..458,487..488)
                     /site_type="other"
                     /note="myristoyl binding site [chemical binding]"
                     /db_xref="CDD:270645"
     Site            405..429
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270645"
     Site            order(424..426,428,436,470,474)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270645"
     CDS             1..542
                     /gene="ABL2"
                     /gene_synonym="ABLL; ARG"
                     /coded_by="NM_001136001.2:281..1909"
                     /note="isoform e is encoded by transcript variant e"
                     /db_xref="GeneID:27"
                     /db_xref="HGNC:HGNC:77"
                     /db_xref="MIM:164690"
ORIGIN      
        1 mgqqvgrvge apglqqpqpr girgssaarp sgrrrdpagr ttetgfnift qhealhrpyg
       61 cdvepqalne airwsskenl lgatesdpnl fvalydfvas gdntlsitkg eklrvlgynq
      121 ngewsevrsk ngqgwvpsny itpvnslekh swyhgpvsrs aaeyllssli ngsflvrese
      181 sspgqlsisl ryegrvyhyr inttadgkvy vtaesrfstl aelvhhhstv adglvttlhy
      241 papkcnkptv ygvspihdkw emertditmk hklgggqyge vyvgvwkkys ltvavktlke
      301 dtmeveeflk eaavmkeikh pnlvqllgvc tleppfyivt eympygnlld ylrecnreev
      361 tavvllymat qissameyle kknfihrdla arnclvgenh vvkvadfgls rlmtgdtyta
      421 hagakfpikw tapeslaynt fsiksdvwaf gvllweiaty gmspypgidl sqvydllekg
      481 yrmeqpegcp pkvyelmrac wkwspadrps faethqafet mfhdssisev llhcanqtci
      541 tl
//
LOCUS       NP_001363278             810 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger CCCH domain-containing protein 11A isoform 1 [Homo
            sapiens].
ACCESSION   NP_001363278
VERSION     NP_001363278.1
DBSOURCE    REFSEQ: accession NM_001376349.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Kases,K., Schubert,E., Hajikhezri,Z., Larsson,M., Devi,P.,
            Darweesh,M., Andersson,L., Akusjarvi,G., Punga,T. and Younis,S.
  TITLE     The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts
  JOURNAL   J Biol Chem 299 (8), 104959 (2023)
   PUBMED   37356722
  REMARK    GeneRIF: The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts.
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 810)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 810)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114402.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.96199.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..810
                     /product="zinc finger CCCH domain-containing protein 11A
                     isoform 1"
                     /note="zinc finger CCCH-type domain containing 11A; zinc
                     finger CCCH domain-containing protein 11A"
                     /calculated_mol_wt=89000
     Region          1..110
                     /region_name="zf-CCCH_3"
                     /note="Zinc-finger containing family; pfam15663"
                     /db_xref="CDD:464787"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          139..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          223..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          285..351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          367..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          482..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          715..768
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     CDS             1..810
                     /gene="ZC3H11A"
                     /gene_synonym="ZC3HDC11A"
                     /coded_by="NM_001376349.1:683..3115"
                     /note="isoform 1 is encoded by transcript variant 25"
                     /db_xref="CCDS:CCDS30978.1"
                     /db_xref="GeneID:9877"
                     /db_xref="HGNC:HGNC:29093"
                     /db_xref="MIM:613513"
ORIGIN      
        1 mpnqgedcyf ffystctkgd scpfrhceaa ignetvctlw qegrcfrqvc rfrhmeidkk
       61 rseipcywen qptgcqklnc afhhnrgryv dglflppskt vlptvpespe eevkasqlsv
      121 qqnklsvqsn pspqlrsvmk vessenvpsp thppvvinaa dddeddddqf seegdetktp
      181 tlqptpevhn glrvtsvrkp avnikqgecl nfgiktleei kskkmkeksk kqgegssgvs
      241 slllhpepvp gpekenvrtv vrtvtlstkq geeplvrlsl terlgkrkfs aggdsdpplk
      301 rslaqrlgkk veapetnidk tpkkaqvsks lkerlgmsad pdnedatdkv nkvgeihvkt
      361 leeilleras qkrgelqtkl ktegpsktdd stsgarssst iriktfsevl aekkhrqqea
      421 erqkskkdtt ciklkidsei kktvvlppiv asrgqseepa gktksmqevh iktleeikle
      481 kalrvqqsse sstsspsqhe atpgarrllr itkrtgmkee knlqegnevd sqssirteak
      541 easgettgvd itkiqvkrce tmrekhmqkq qereksvltp lrgdvascnt qvaekpvlta
      601 vpgitrhltk rlptkssqkv evetsgigds llnvkcaaqt lekrgkakpk vnvkpsvvkv
      661 vsspklapkr kavemhaavi aavkplssss vlqeppakka avavvplvse dksvtvpeae
      721 nprdslvlpp tqsssdsspp evsgpsssqm smktrrlssa stgkpplsve ddfekliwei
      781 sggkleaeid ldpgkdeddl llelsemids
//
LOCUS       NP_689580                362 aa            linear   PRI 21-NOV-2025
DEFINITION  protein mab-21-like 3 [Homo sapiens].
ACCESSION   NP_689580
VERSION     NP_689580.2
DBSOURCE    REFSEQ: accession NM_152367.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL121982.19 and AK096035.1.
            
            On Dec 31, 2009 this sequence version replaced NP_689580.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3799346.1,
                                           SRR18074968.734284.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369500.4/ ENSP00000358512.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.1"
     Protein         1..362
                     /product="protein mab-21-like 3"
                     /note="DANGER family member 5"
                     /calculated_mol_wt=42226
     Region          58..248
                     /region_name="Mab-21"
                     /note="Mab-21 protein nucleotidyltransferase domain;
                     pfam03281"
                     /db_xref="CDD:460873"
     Region          255..351
                     /region_name="Mab-21_C"
                     /note="Mab-21 protein HhH/H2TH-like domain; pfam20266"
                     /db_xref="CDD:466416"
     CDS             1..362
                     /gene="MAB21L3"
                     /gene_synonym="C1orf161; D5"
                     /coded_by="NM_152367.3:504..1592"
                     /db_xref="CCDS:CCDS886.1"
                     /db_xref="GeneID:126868"
                     /db_xref="HGNC:HGNC:26787"
ORIGIN      
        1 mkyltvgdle dcllnkvdlr rqqisqavee vqkvvhhltt nisnqdirfq avpysdtyne
       61 nikvlapsqf lvtvpikgla gyreareqhw ryytlqgtrl pcplrdpegl qqwleveqfm
      121 kslwqwhetd vnidgdivpa kvllvfrklv enavrtchls gkvsllgnrs avwvavetsa
      181 yqvelelvpa veipttwskk arwprclqrw psqervecik sfgfnllacs nyhwqlsflr
      241 aeqvlleqld edggcrrkcf qvmrhlkedi wcpgnrpvit shhlqtvlfw tcekyphfkd
      301 wqvfskaflr lvrklhkcvs qhflkhyfvr nsnlfqctnp teldtvaqkl atflknpqig
      361 pp
//
LOCUS       NP_001269813             204 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase III subunit RPC8 isoform a [Homo
            sapiens].
ACCESSION   NP_001269813
VERSION     NP_001269813.1
DBSOURCE    REFSEQ: accession NM_001282884.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Ramsay,E.P., Abascal-Palacios,G., Daiss,J.L., King,H., Gouge,J.,
            Pilsl,M., Beuron,F., Morris,E., Gunkel,P., Engel,C. and Vannini,A.
  TITLE     Structure of human RNA polymerase III
  JOURNAL   Nat Commun 11 (1), 6409 (2020)
   PUBMED   33335104
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Franca,M.M., Han,X., Funari,M.F.A., Lerario,A.M., Nishi,M.Y.,
            Fontenele,E.G.P., Domenice,S., Jorge,A.A.L., Garcia-Galiano,D.,
            Elias,C.F. and Mendonca,B.B.
  TITLE     Exome Sequencing Reveals the POLR3H Gene as a Novel Cause of
            Primary Ovarian Insufficiency
  JOURNAL   J Clin Endocrinol Metab 104 (7), 2827-2841 (2019)
   PUBMED   30830215
  REMARK    GeneRIF: A pathogenic homozygous missense mutation (c.149A>G;
            p.Asp50Gly) in the POLR3H gene in two unrelated families with
            primary ovarian insufficiency was identified.
REFERENCE   6  (residues 1 to 204)
  AUTHORS   Owen,T.J., O'Neil,J.D., Dawson,C.W., Hu,C., Chen,X., Yao,Y.,
            Wood,V.H., Mitchell,L.E., White,R.J., Young,L.S. and Arrand,J.R.
  TITLE     Epstein-Barr virus-encoded EBNA1 enhances RNA polymerase
            III-dependent EBER expression through induction of EBER-associated
            cellular transcription factors
  JOURNAL   Mol Cancer 9, 241 (2010)
   PUBMED   20843307
  REMARK    GeneRIF: Findings reveal that RNA polymerase III-dependent EBER
            expression through induction of cellular transcription factors and
            add to the repertoire of EBNA1's transcription-regulatory
            properties.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 204)
  AUTHORS   Greco-Stewart,V.S., Schissel,E. and Pelchat,M.
  TITLE     The hepatitis delta virus RNA genome interacts with the human RNA
            polymerases I and III
  JOURNAL   Virology 386 (1), 12-15 (2009)
   PUBMED   19246067
  REMARK    GeneRIF: The authors demonstrate the interaction of both RNA
            polymerase I and III with hepatitis delta virus RNA, both in vitro
            and in human cells.
REFERENCE   8  (residues 1 to 204)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   9  (residues 1 to 204)
  AUTHORS   Hu,P., Wu,S., Sun,Y., Yuan,C.C., Kobayashi,R., Myers,M.P. and
            Hernandez,N.
  TITLE     Characterization of human RNA polymerase III identifies orthologues
            for Saccharomyces cerevisiae RNA polymerase III subunits
  JOURNAL   Mol Cell Biol 22 (22), 8044-8055 (2002)
   PUBMED   12391170
REFERENCE   10 (residues 1 to 204)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL023553.5, BU584298.1, AB051452.1, AK000365.1 and BM701572.1.
            
            Transcript Variant: This variant (5) differs in the 5' UTR,
            compared to variant 1. Variants 1, 3, 5, and 6 encode the same
            isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR456459.1, SRR14038191.2134939.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..204
                     /product="DNA-directed RNA polymerase III subunit RPC8
                     isoform a"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerase III subunit RPC8;
                     polymerase (RNA) III subunit H; RNA nucleotidyltransferase
                     (DNA-directed); RNA polymerase III subunit C8;
                     DNA-directed RNA polymerase III subunit H; DNA-directed
                     RNA polymerase III subunit 22.9 kDa polypeptide;
                     polymerase (RNA) III (DNA directed) polypeptide H
                     (22.9kD)"
                     /calculated_mol_wt=22787
     Region          2..81
                     /region_name="RNAP_III_Rpc25_N"
                     /note="Rpc25, N-terminal ribonucleoprotein (RNP) domain.
                     Rpc25 is a subunit of eukaryotic RNA polymerase (RNAP) III
                     and is homologous to Rpa43 of eukaryotic RNAP I, Rpb7 of
                     eukaryotic RNAP II, and RpoE of archaeal RNAP. Rpc25 has
                     two domains, an N-terminal RNP...; cd04330"
                     /db_xref="CDD:239822"
     Site            order(2..6,8,28,31..32,46..49,73,78,80)
                     /site_type="other"
                     /note="Rpc17 interaction site [polypeptide binding]"
                     /db_xref="CDD:239822"
     Region          83..201
                     /region_name="RNA_pol_Rbc25"
                     /note="RNA polymerase III subunit Rpc25; pfam08292"
                     /db_xref="CDD:400543"
     Region          158..179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y535.1)"
     CDS             1..204
                     /gene="POLR3H"
                     /gene_synonym="C25; RPC22.9; RPC8"
                     /coded_by="NM_001282884.2:117..731"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS14018.1"
                     /db_xref="GeneID:171568"
                     /db_xref="HGNC:HGNC:30349"
                     /db_xref="MIM:619801"
ORIGIN      
        1 mfvlvemvdt vrippwqfer klndsiaeel nkklankvvy nvglciclfd itkledayvf
       61 pgdgashtkv hfrcvvfhpf ldeiligkik gcspegvhvs lgffddilip peslqqpakf
      121 deaeqvwvwe yeteegahdl ymdtgeeirf rvvdesfvdt sptgpssada ttsseelpkk
      181 eapytlvgsi sepglgllsw wtsn
//
LOCUS       NP_001012331             790 aa            linear   PRI 21-NOV-2025
DEFINITION  high affinity nerve growth factor receptor isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_001012331
VERSION     NP_001012331.1
DBSOURCE    REFSEQ: accession NM_001012331.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 790)
  AUTHORS   Zhang,W., Schmitz,A.A., Kallionpaa,R.E., Perala,M., Pitkanen,N.,
            Tukiainen,M., Alanne,E., Johrens,K., Schulze-Rath,R., Farahmand,B.
            and Zong,J.
  TITLE     Neurotrophic tyrosine receptor kinase gene fusions in adult and
            pediatric patients with solid tumors: a clinicogenomic biobank and
            record linkage study of expression frequency and patient
            characteristics from Finland
  JOURNAL   Acta Oncol 63, 542-551 (2024)
   PUBMED   38967220
  REMARK    GeneRIF: Neurotrophic tyrosine receptor kinase gene fusions in
            adult and pediatric patients with solid tumors: a clinicogenomic
            biobank and record linkage study of expression frequency and
            patient characteristics from Finland.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   3  (residues 1 to 790)
  AUTHORS   Cappabianca,L., Ruggieri,M., Sebastiano,M., Sbaffone,M.,
            Martelli,I., Ruggeri,P., Di Padova,M., Farina,A.R. and Mackay,A.R.
  TITLE     Molecular Characterization and Inhibition of a Novel Stress-Induced
            Mitochondrial Protecting Role for Misfolded TrkAIII in Human
            SH-SY5Y Neuroblastoma Cells
  JOURNAL   Int J Mol Sci 25 (10), 5475 (2024)
   PUBMED   38791513
  REMARK    GeneRIF: Molecular Characterization and Inhibition of a Novel
            Stress-Induced Mitochondrial Protecting Role for Misfolded TrkAIII
            in Human SH-SY5Y Neuroblastoma Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 790)
  AUTHORS   Dvorak,O., Slavickova,M., Laco,J., Stepan,M., Cermakova,E. and
            Spacek,J.
  TITLE     DNA hypermethylation of tumor suppressor genes TWIST1, GATA4, MUS81
            and NTRK1 in endometrial hyperplasia
  JOURNAL   Ceska Gynekol 89 (4), 261-268 (2024)
   PUBMED   39242200
  REMARK    GeneRIF: DNA hypermethylation of tumor suppressor genes TWIST1,
            GATA4, MUS81 and NTRK1 in endometrial hyperplasia.
REFERENCE   5  (residues 1 to 790)
  AUTHORS   Schon,K.R., Parker,A.P.J. and Woods,C.G.
  TITLE     Congenital Insensitivity to Pain Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29419974
REFERENCE   6  (residues 1 to 790)
  AUTHORS   Indo,Y.
  TITLE     NTRK1 Congenital Insensitivity to Pain with Anhidrosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301726
REFERENCE   7  (residues 1 to 790)
  AUTHORS   Loeb,D.M., Tsao,H., Cobb,M.H. and Greene,L.A.
  TITLE     NGF and other growth factors induce an association between ERK1 and
            the NGF receptor, gp140prototrk
  JOURNAL   Neuron 9 (6), 1053-1065 (1992)
   PUBMED   1463607
REFERENCE   8  (residues 1 to 790)
  AUTHORS   Jing,S., Tapley,P. and Barbacid,M.
  TITLE     Nerve growth factor mediates signal transduction through trk
            homodimer receptors
  JOURNAL   Neuron 9 (6), 1067-1079 (1992)
   PUBMED   1281417
REFERENCE   9  (residues 1 to 790)
  AUTHORS   Greco,A., Pierotti,M.A., Bongarzone,I., Pagliardini,S., Lanzi,C.
            and Della Porta,G.
  TITLE     TRK-T1 is a novel oncogene formed by the fusion of TPR and TRK
            genes in human papillary thyroid carcinomas
  JOURNAL   Oncogene 7 (2), 237-242 (1992)
   PUBMED   1532241
REFERENCE   10 (residues 1 to 790)
  AUTHORS   Schneider,R. and Schweiger,M.
  TITLE     A novel modular mosaic of cell adhesion motifs in the extracellular
            domains of the neurogenic trk and trkB tyrosine kinase receptors
  JOURNAL   Oncogene 6 (10), 1807-1811 (1991)
   PUBMED   1656363
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158169.17, M23102.1,
            BC062580.1 and BM685020.1.
            
            Summary: This gene encodes a member of the neurotrophic tyrosine
            kinase receptor (NTKR) family. This kinase is a membrane-bound
            receptor that, upon neurotrophin binding, phosphorylates itself and
            members of the MAPK pathway. The presence of this kinase leads to
            cell differentiation and may play a role in specifying sensory
            neuron subtypes. Mutations in this gene have been associated with
            congenital insensitivity to pain, anhidrosis, self-mutilating
            behavior, cognitive disability and cancer. Alternate
            transcriptional splice variants of this gene have been found, but
            only three have been characterized to date. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (1) lacks an internal, in-frame
            exon, compared to variant 2, resulting in a shorter isoform (1)
            lacking an internal segment compared to isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M23102.1, BC144239.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.1"
     Protein         1..790
                     /product="high affinity nerve growth factor receptor
                     isoform 1 precursor"
                     /EC_number="2.7.10.1"
                     /note="Oncogene TRK; tyrosine kinase receptor A; high
                     affinity nerve growth factor receptor; TRK1-transforming
                     tyrosine kinase protein; gp140trk; tropomyosin-related
                     kinase A; neurotrophic tyrosine kinase, receptor, type 1;
                     tropomyosin receptor kinase A"
                     /calculated_mol_wt=83552
     sig_peptide     1..32
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04629.4)"
                     /calculated_mol_wt=3347
     Site            67
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04629.4)"
     Region          68..92
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          90..113
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P04629.4)"
     Region          92..150
                     /region_name="LRR_8"
                     /note="Leucine rich repeat; pfam13855"
                     /db_xref="CDD:404697"
     Region          93..116
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            95
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:17196528; propagated from
                     UniProtKB/Swiss-Prot (P04629.4)"
     Region          116..137
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P04629.4)"
     Region          117..139
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:17196528; propagated from
                     UniProtKB/Swiss-Prot (P04629.4)"
     Region          140..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          151..192
                     /region_name="LRRCT_2"
                     /note="Leucine rich repeat C-terminal motif; pfam16920"
                     /db_xref="CDD:465313"
     Site            188
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:17196528,
                     ECO:0007744|PDB:2IFG; propagated from UniProtKB/Swiss-Prot
                     (P04629.4)"
     Region          195..282
                     /region_name="Ig_TrkABC_d4"
                     /note="Fourth domain (immunoglobulin-like) of Trk
                     receptors TrkA, TrkB, and TrkC; cd04972"
                     /db_xref="CDD:409361"
     Region          195..201
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409361"
     Site            202
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04629.4)"
     Region          210..219
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409361"
     Region          222..229
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409361"
     Region          231..233
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409361"
     Region          236..243
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409361"
     Region          246..255
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409361"
     Site            253
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04629.4)"
     Region          262..269
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409361"
     Site            262
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:17196528,
                     ECO:0007744|PDB:2IFG; propagated from UniProtKB/Swiss-Prot
                     (P04629.4)"
     Region          272..279
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409361"
     Site            281..282
                     /site_type="other"
                     /note="interdomain interface [polypeptide binding]"
                     /db_xref="CDD:409361"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:17196528,
                     ECO:0007744|PDB:2IFG; propagated from UniProtKB/Swiss-Prot
                     (P04629.4)"
     Region          285..379
                     /region_name="IgI_TrKABC_d5"
                     /note="Fifth domain (immunoglobulin-like) of Trk receptors
                     TrkA, TrkB, and TrkC; member of the I-set of Ig
                     superfamily (IgSF) domains; cd04971"
                     /db_xref="CDD:409360"
     Region          285..291
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409360"
     Region          293..296
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409360"
     Region          299..307
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409360"
     Site            308
                     /site_type="other"
                     /note="interdomain interface [polypeptide binding]"
                     /db_xref="CDD:409360"
     Region          310..317
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409360"
     Site            318
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04629.4)"
     Region          320..323
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409360"
     Site            323
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04629.4)"
     Region          328..334
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409360"
     Site            order(333,349..350,353)
                     /site_type="other"
                     /note="receptor binding site [polypeptide binding]"
                     /db_xref="CDD:409360"
     Site            338
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04629.4)"
     Region          341..349
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409360"
     Region          357..365
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409360"
     Site            358
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:17196528,
                     ECO:0007744|PDB:2IFG; propagated from UniProtKB/Swiss-Prot
                     (P04629.4)"
     Region          368..376
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409360"
     Site            395
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04629.4)"
     Site            418..433
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04629.4)"
     Region          463..484
                     /region_name="Interaction with SQSTM1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P04629.4)"
     Site            480
                     /site_type="other"
                     /note="Breakpoint for translocation to form TRK-T1;
                     propagated from UniProtKB/Swiss-Prot (P04629.4)"
     Site            490
                     /site_type="other"
                     /note="Interaction with SHC1; propagated from
                     UniProtKB/Swiss-Prot (P04629.4)"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15488758,
                     ECO:0000269|PubMed:27676246, ECO:0000269|PubMed:8155326;
                     propagated from UniProtKB/Swiss-Prot (P04629.4)"
     Region          498..777
                     /region_name="PTKc_TrkA"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Tropomyosin Related Kinase A; cd05092"
                     /db_xref="CDD:270674"
     Site            order(510..514,518,536,538,583..586,589..590,644,648..649,
                     651,662,680..684,693,727)
                     /site_type="active"
                     /db_xref="CDD:270674"
     Site            order(510..511,513..514,518,536,538,583..586,589..590,
                     648..649,651,662)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270674"
     Region          531..535
                     /region_name="DXXLL.
                     /evidence=ECO:0000269|PubMed:26446845"
                     /note="propagated from UniProtKB/Swiss-Prot (P04629.4)"
     Region          601..605
                     /region_name="DXXLL.
                     /evidence=ECO:0000269|PubMed:26446845"
                     /note="propagated from UniProtKB/Swiss-Prot (P04629.4)"
     Site            order(644,648,680..684,693,727)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270674"
     Site            661..686
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270674"
     Site            670
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:8155326; propagated from
                     UniProtKB/Swiss-Prot (P04629.4)"
     Site            674
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15488758,
                     ECO:0000269|PubMed:8155326; propagated from
                     UniProtKB/Swiss-Prot (P04629.4)"
     Site            675
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15488758,
                     ECO:0000269|PubMed:8155326; propagated from
                     UniProtKB/Swiss-Prot (P04629.4)"
     Site            785
                     /site_type="other"
                     /note="Interaction with PLCG1; propagated from
                     UniProtKB/Swiss-Prot (P04629.4)"
     Site            785
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15488758,
                     ECO:0000269|PubMed:7510697, ECO:0000269|PubMed:8155326;
                     propagated from UniProtKB/Swiss-Prot (P04629.4)"
     CDS             1..790
                     /gene="NTRK1"
                     /gene_synonym="MTC; p140-TrkA; TRK; Trk-A; TRK1; TRKA"
                     /coded_by="NM_001012331.2:71..2443"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS30891.1"
                     /db_xref="GeneID:4914"
                     /db_xref="HGNC:HGNC:8031"
                     /db_xref="MIM:191315"
ORIGIN      
        1 mlrggrrgql gwhswaagpg sllawlilas agaapcpdac cphgssglrc trdgaldslh
       61 hlpgaenlte lyienqqhlq hlelrdlrgl gelrnltivk sglrfvapda fhftprlsrl
      121 nlsfnalesl swktvqglsl qelvlsgnpl hcscalrwlq rweeeglggv peqklqchgq
      181 gplahmpnas cgvptlkvqv pnasvdvgdd vllrcqvegr gleqagwilt eleqsatvmk
      241 sgglpslglt lanvtsdlnr knvtcwaend vgraevsvqv nvsfpasvql htavemhhwc
      301 ipfsvdgqpa pslrwlfngs vlnetsfift eflepaanet vrhgclrlnq pthvnngnyt
      361 llaanpfgqa sasimaafmd npfefnpedp ipdtnstsgd pvekkdetpf gvsvavglav
      421 faclflstll lvlnkcgrrn kfginrpavl apedglamsl hfmtlggssl sptegkgsgl
      481 qghiienpqy fsdacvhhik rrdivlkwel gegafgkvfl aechnllpeq dkmlvavkal
      541 keasesarqd fqreaelltm lqhqhivrff gvctegrpll mvfeymrhgd lnrflrshgp
      601 dakllagged vapgplglgq llavasqvaa gmvylaglhf vhrdlatrnc lvgqglvvki
      661 gdfgmsrdiy stdyyrvggr tmlpirwmpp esilyrkftt esdvwsfgvv lweiftygkq
      721 pwyqlsntea idcitqgrel erpracppev yaimrgcwqr epqqrhsikd vharlqalaq
      781 appvyldvlg
//
LOCUS       NP_001362683             401 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform d [Homo sapiens].
ACCESSION   NP_001362683
VERSION     NP_001362683.1
DBSOURCE    REFSEQ: accession NM_001375754.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 401)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 401)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 401)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 401)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            Transcript Variant: This variant (6), as well as variant 4, encodes
            isoform d.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2322592.1,
                                           SRR14038191.745456.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..401
                     /product="abl interactor 2 isoform d"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=44278
     Region          48..111
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          340..400
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(348,350,353,357,375..376,389,391..392)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..401
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375754.1:329..1534"
                     /note="isoform d is encoded by transcript variant 6"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 mscrcwisrh psyegwnlqs iifhkqirgv dlestfvtkf gnncslrlne tvdihkekva
       61 rreigilttn kntsrthkii apanlerpvr yirkpidyti lddighgvkv stqnmkmggl
      121 prttpptqkp psppmsgkgt lgrhspyrtl epvrppvvpn dyvpsptrnm apsqqspvrt
      181 asvnqrnrty sssgssggsh pssrsssren sgsgsvgvpi avptpsppsv fpghpvqfys
      241 mnrpasrhtp ptiggslpyr rppsitsqts lqnqmnggpf ysqnpvsdtp pppppveepv
      301 fdespppppp pedyeeeeaa vveysdpyae edppwaprsy lekvvaiydy tkdkedelsf
      361 qegaiiyvik knddgwyegv mngvtglfpg nyvesimhys e
//
LOCUS       NP_001358104            1083 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal cell adhesion molecule isoform kk precursor [Homo
            sapiens].
ACCESSION   NP_001358104
VERSION     NP_001358104.1
DBSOURCE    REFSEQ: accession NM_001371175.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1083)
  AUTHORS   Wang,C., Wang,Z., Fu,L., Du,J., Ji,F. and Qiu,X.
  TITLE     CircNRCAM up-regulates NRCAM to promote papillary thyroid carcinoma
            progression
  JOURNAL   J Endocrinol Invest 47 (5), 1215-1226 (2024)
   PUBMED   38485895
  REMARK    GeneRIF: CircNRCAM up-regulates NRCAM to promote papillary thyroid
            carcinoma progression.
REFERENCE   2  (residues 1 to 1083)
  AUTHORS   Zhou,L., He,L., Liu,C.H., Qiu,H., Zheng,L., Sample,K.M., Wu,Q.,
            Li,J., Xie,K., Ampuero,J., Li,Z., Lv,D., Liu,M., Romero-Gomez,M.,
            Hu,Y. and Tang,H.
  TITLE     Liver cancer stem cell dissemination and metastasis: uncovering the
            role of NRCAM in hepatocellular carcinoma
  JOURNAL   J Exp Clin Cancer Res 42 (1), 311 (2023)
   PUBMED   37993901
  REMARK    GeneRIF: Liver cancer stem cell dissemination and metastasis:
            uncovering the role of NRCAM in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1083)
  AUTHORS   Sannes,A.C., Christensen,J.O., Nielsen,M.B. and Gjerstad,J.
  TITLE     Stress-induced headache in the general working population is
            moderated by the NRCAM rs2300043 genotype
  JOURNAL   Scand J Pain 23 (2), 326-332 (2022)
   PUBMED   36181733
  REMARK    GeneRIF: Stress-induced headache in the general working population
            is moderated by the NRCAM rs2300043 genotype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1083)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 1083)
  AUTHORS   Bai,C. and Chen,D.G.
  TITLE     NRCAM acts as a prognostic biomarker and promotes the tumor
            progression in gastric cancer via EMT pathway
  JOURNAL   Tissue Cell 77, 101859 (2022)
   PUBMED   35763884
  REMARK    GeneRIF: NRCAM acts as a prognostic biomarker and promotes the
            tumor progression in gastric cancer via EMT pathway.
REFERENCE   6  (residues 1 to 1083)
  AUTHORS   Wang,B., Williams,H., Du,J.S., Terrett,J. and Kenwrick,S.
  TITLE     Alternative splicing of human NrCAM in neural and nonneural tissues
  JOURNAL   Mol Cell Neurosci 10 (5-6), 287-295 (1998)
   PUBMED   9604207
REFERENCE   7  (residues 1 to 1083)
  AUTHORS   Grumet,M.
  TITLE     Nr-CAM: a cell adhesion molecule with ligand and receptor functions
  JOURNAL   Cell Tissue Res 290 (2), 423-428 (1997)
   PUBMED   9321706
  REMARK    Review article
REFERENCE   8  (residues 1 to 1083)
  AUTHORS   Sakurai,T., Lustig,M., Nativ,M., Hemperly,J.J., Schlessinger,J.,
            Peles,E. and Grumet,M.
  TITLE     Induction of neurite outgrowth through contactin and Nr-CAM by
            extracellular regions of glial receptor tyrosine phosphatase beta
  JOURNAL   J Cell Biol 136 (4), 907-918 (1997)
   PUBMED   9049255
REFERENCE   9  (residues 1 to 1083)
  AUTHORS   Volkmer,H., Leuschner,R., Zacharias,U. and Rathjen,F.G.
  TITLE     Neurofascin induces neurites by heterophilic interactions with
            axonal NrCAM while NrCAM requires F11 on the axonal surface to
            extend neurites
  JOURNAL   J Cell Biol 135 (4), 1059-1069 (1996)
   PUBMED   8922386
REFERENCE   10 (residues 1 to 1083)
  AUTHORS   Lane,R.P., Chen,X.N., Yamakawa,K., Vielmetter,J., Korenberg,J.R.
            and Dreyer,W.J.
  TITLE     Characterization of a highly conserved human homolog to the chicken
            neural cell surface protein Bravo/Nr-CAM that maps to chromosome
            band 7q31
  JOURNAL   Genomics 35 (3), 456-465 (1996)
   PUBMED   8812479
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005058.1, AC007567.2 and
            AC005683.2.
            
            Summary: Cell adhesion molecules (CAMs) are members of the
            immunoglobulin superfamily. This gene encodes a neuronal cell
            adhesion molecule with multiple immunoglobulin-like C2-type domains
            and fibronectin type-III domains. This ankyrin-binding protein is
            involved in neuron-neuron adhesion and promotes directional
            signaling during axonal cone growth. This gene is also expressed in
            non-neural tissues and may play a general role in cell-cell
            communication via signaling from its intracellular domain to the
            actin cytoskeleton during directional cell migration. Allelic
            variants of this gene have been associated with autism and
            addiction vulnerability. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1846375.1,
                                           SRR14038193.2759332.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1083
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1083
                     /product="neuronal cell adhesion molecule isoform kk
                     precursor"
                     /note="NgCAM-related cell adhesion molecule; neuronal
                     surface protein Bravo"
                     /calculated_mol_wt=116612
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3315
     Region          40..134
                     /region_name="IgI_NrCAM"
                     /note="Immunoglobulin (Ig)-like domain of NrCAM (Ng
                     (neuronglia) CAM-related cell adhesion molecule); member
                     of the I-set of Ig superfamily (IgSF) domains; cd05874"
                     /db_xref="CDD:409458"
     Region          40..44
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409458"
     Region          49..53
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409458"
     Region          58..65
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409458"
     Region          71..76
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409458"
     Site            77
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          79..81
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409458"
     Region          88..91
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409458"
     Region          96..100
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409458"
     Region          113..121
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409458"
     Region          124..134
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409458"
     Region          143..232
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          157..161
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          171..175
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          194..198
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          209..214
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            217
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          225..228
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            239
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            245
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            270
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          271..352
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          282..286
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          295..299
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            308
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          317..321
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          331..336
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          344..347
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          356..444
                     /region_name="Ig4_NrCAM"
                     /note="Fourth immunoglobulin (Ig)-like domain of NrCAM
                     (NgCAM-related cell adhesion molecule); cd05868"
                     /db_xref="CDD:409454"
     Region          372..376
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409454"
     Region          385..389
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409454"
     Region          409..413
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409454"
     Region          423..428
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409454"
     Site            427
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          436..439
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409454"
     Region          453..536
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          466..470
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          479..483
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            501
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          502..506
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          516..521
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          529..532
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          539..618
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          557..561
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          572..576
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          <581..945
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          593..597
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          607..612
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            613
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          631..721
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(631,697,712)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            700
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            order(713..714,716..717)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            786
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            842
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          970..1059
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     CDS             1..1083
                     /gene="NRCAM"
                     /gene_synonym="NEDNMS"
                     /coded_by="NM_001371175.1:526..3777"
                     /note="isoform kk precursor is encoded by transcript
                     variant 66"
                     /db_xref="GeneID:4897"
                     /db_xref="HGNC:HGNC:7994"
                     /db_xref="MIM:601581"
ORIGIN      
        1 mqlkimpkkk rlsagrvpli lflcqmisal evpldlvqpp titqqspkdy iidprenivi
       61 qceakgkppp sfswtrngth fdidkdplvt mkpgtgtlii nimsegkaet yegvyqctar
      121 nergaavsnn ivvrpsrspl wtkeklepit lqsgqslvlp crppiglppp iifwmdnsfq
      181 rlpqservsq glngdlyfsn vlpedtredy icyarfnhtq tiqqkqpisv kvisvdelnd
      241 tiaanlsdte fygakssrer pptfltpegn asnkeelrgn vlsleciaeg lptpiiywak
      301 edgmlpknrt vyknfektlq iihvseadsg nyqciaknal gaihhtisvr vkaapywita
      361 pqnlvlspge dgtlicrang npkpriswlt ngvpieiapd dpsrkidgdt iifsnvqers
      421 savyqcnasn eygyllanaf vnvlaeppri ltpantlyqv ianrpalldc affgsplpti
      481 ewfkgakgsa lhediyvlhe ngtleipvaq kdstgtytcv arnklgmakn evhleikdpt
      541 wivkqpeyav vqrgsmvsfe ckvkhdhtls ltvlwlkdnr elpsderftv dkdhlvvadv
      601 sdddsgtytc vanttldsvs asavlsvvdv pnppfdlelt dqldksvqls wtpgddnnsp
      661 itkfiieyed amhkpglwhh qtevsgtqtt aqlklspyvn ysfrvmavns igkslpseas
      721 eqyltkasep dknptavegl gsepdnlvit wkplngfesn gpglqykvsw rqkdgddewt
      781 svvvanvsky ivsgtptfvp ylikvqalnd mgfapepavv mghsgedlpm vapgnvrvnv
      841 vnstlaevhw dpvplksirg hlqgyriyyw ktqssskrnr rhiekkiltf qgskthgmlp
      901 glepfshytl nvrvvngkge gpaspdrvfn tpegamasrq vdiatqgwfi glmcavalli
      961 lillivcfir rnkggkypvk ekedahadpe iqpmkeddgt fgeysdaedh kplkkgsrtp
     1021 sdrtvkkeds ddslvdygeg vngqfnedgs figqysgkke kepaegness eapspvnamn
     1081 sfv
//
LOCUS       NP_001271139             181 aa            linear   PRI 21-NOV-2025
DEFINITION  mediator of RNA polymerase II transcription subunit 6 isoform 3
            [Homo sapiens].
ACCESSION   NP_001271139 XP_005267303
VERSION     NP_001271139.1
DBSOURCE    REFSEQ: accession NM_001284210.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Marcon,E., Ni,Z., Pu,S., Turinsky,A.L., Trimble,S.S., Olsen,J.B.,
            Silverman-Gavrila,R., Silverman-Gavrila,L., Phanse,S., Guo,H.,
            Zhong,G., Guo,X., Young,P., Bailey,S., Roudeva,D., Zhao,D.,
            Hewel,J., Li,J., Graslund,S., Paduch,M., Kossiakoff,A.A.,
            Lupien,M., Emili,A., Wodak,S.J. and Greenblatt,J.
  TITLE     Human-chromatin-related protein interactions identify a demethylase
            complex required for chromosome segregation
  JOURNAL   Cell Rep 8 (1), 297-310 (2014)
   PUBMED   24981860
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Ito,M., Yuan,C.X., Malik,S., Gu,W., Fondell,J.D., Yamamura,S.,
            Fu,Z.Y., Zhang,X., Qin,J. and Roeder,R.G.
  TITLE     Identity between TRAP and SMCC complexes indicates novel pathways
            for the function of nuclear receptors and diverse mammalian
            activators
  JOURNAL   Mol Cell 3 (3), 361-370 (1999)
   PUBMED   10198638
REFERENCE   7  (residues 1 to 181)
  AUTHORS   Gu,W., Malik,S., Ito,M., Yuan,C.X., Fondell,J.D., Zhang,X.,
            Martinez,E., Qin,J. and Roeder,R.G.
  TITLE     A novel human SRB/MED-containing cofactor complex, SMCC, involved
            in transcription regulation
  JOURNAL   Mol Cell 3 (1), 97-108 (1999)
   PUBMED   10024883
  REMARK    Erratum:[Mol Cell 1999 Apr;3(4):following 541]
REFERENCE   8  (residues 1 to 181)
  AUTHORS   Sun,X., Zhang,Y., Cho,H., Rickert,P., Lees,E., Lane,W. and
            Reinberg,D.
  TITLE     NAT, a human complex containing Srb polypeptides that functions as
            a negative regulator of activated transcription
  JOURNAL   Mol Cell 2 (2), 213-222 (1998)
   PUBMED   9734358
REFERENCE   9  (residues 1 to 181)
  AUTHORS   Jiang,Y.W., Veschambre,P., Erdjument-Bromage,H., Tempst,P.,
            Conaway,J.W., Conaway,R.C. and Kornberg,R.D.
  TITLE     Mammalian mediator of transcriptional regulation and its possible
            role as an end-point of signal transduction pathways
  JOURNAL   Proc Natl Acad Sci U S A 95 (15), 8538-8543 (1998)
   PUBMED   9671713
REFERENCE   10 (residues 1 to 181)
  AUTHORS   Lee,Y.C., Min,S., Gim,B.S. and Kim,Y.J.
  TITLE     A transcriptional mediator protein that is required for activation
            of many RNA polymerase II promoters and is conserved from yeast to
            humans
  JOURNAL   Mol Cell Biol 17 (8), 4622-4632 (1997)
   PUBMED   9234719
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK304361.1, AK300460.1, BM999935.1 and DA869309.1.
            
            On Sep 26, 2013 this sequence version replaced XP_005267303.1.
            
            Transcript Variant: This variant (3) uses an alternate splice site
            and lacks an alternate exon in the coding region, which results in
            a frameshift, compared to variant 1. The encoded isoform (3) is
            shorter and has a distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK304361.1, DC418252.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.2"
     Protein         1..181
                     /product="mediator of RNA polymerase II transcription
                     subunit 6 isoform 3"
                     /note="mediator of RNA polymerase II transcription subunit
                     6; renal carcinoma antigen NY-REN-28; activator-recruited
                     cofactor 33 kDa component; CTD-2540L5.5"
                     /calculated_mol_wt=20728
     Region          13..140
                     /region_name="Med6"
                     /note="MED6 mediator sub complex component; pfam04934"
                     /db_xref="CDD:461490"
     CDS             1..181
                     /gene="MED6"
                     /gene_synonym="ARC33; NY-REN-28"
                     /coded_by="NM_001284210.2:19..564"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS61483.1"
                     /db_xref="GeneID:10001"
                     /db_xref="HGNC:HGNC:19970"
                     /db_xref="MIM:602984"
ORIGIN      
        1 maavdirdnl lgiswvdssw ipilnsgsvl dyfsersnpf ydrtcnnevv kmqrltlehl
       61 nqmvgieyil lhaqepilfi irkqqrqspa qvipladyyi iagviyqapd lgsvinsrvl
      121 tavhgiqsaf deamsycryh pskgywwhfk dheeqakawr kacssgsnke rgrtytrnck
      181 t
//
LOCUS       NP_001363290             810 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger CCCH domain-containing protein 11A isoform 1 [Homo
            sapiens].
ACCESSION   NP_001363290
VERSION     NP_001363290.1
DBSOURCE    REFSEQ: accession NM_001376361.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Kases,K., Schubert,E., Hajikhezri,Z., Larsson,M., Devi,P.,
            Darweesh,M., Andersson,L., Akusjarvi,G., Punga,T. and Younis,S.
  TITLE     The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts
  JOURNAL   J Biol Chem 299 (8), 104959 (2023)
   PUBMED   37356722
  REMARK    GeneRIF: The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts.
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 810)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 810)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114402.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.22450.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..810
                     /product="zinc finger CCCH domain-containing protein 11A
                     isoform 1"
                     /note="zinc finger CCCH-type domain containing 11A; zinc
                     finger CCCH domain-containing protein 11A"
                     /calculated_mol_wt=89000
     Region          1..110
                     /region_name="zf-CCCH_3"
                     /note="Zinc-finger containing family; pfam15663"
                     /db_xref="CDD:464787"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          139..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          223..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          285..351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          367..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          482..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          715..768
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     CDS             1..810
                     /gene="ZC3H11A"
                     /gene_synonym="ZC3HDC11A"
                     /coded_by="NM_001376361.1:894..3326"
                     /note="isoform 1 is encoded by transcript variant 37"
                     /db_xref="CCDS:CCDS30978.1"
                     /db_xref="GeneID:9877"
                     /db_xref="HGNC:HGNC:29093"
                     /db_xref="MIM:613513"
ORIGIN      
        1 mpnqgedcyf ffystctkgd scpfrhceaa ignetvctlw qegrcfrqvc rfrhmeidkk
       61 rseipcywen qptgcqklnc afhhnrgryv dglflppskt vlptvpespe eevkasqlsv
      121 qqnklsvqsn pspqlrsvmk vessenvpsp thppvvinaa dddeddddqf seegdetktp
      181 tlqptpevhn glrvtsvrkp avnikqgecl nfgiktleei kskkmkeksk kqgegssgvs
      241 slllhpepvp gpekenvrtv vrtvtlstkq geeplvrlsl terlgkrkfs aggdsdpplk
      301 rslaqrlgkk veapetnidk tpkkaqvsks lkerlgmsad pdnedatdkv nkvgeihvkt
      361 leeilleras qkrgelqtkl ktegpsktdd stsgarssst iriktfsevl aekkhrqqea
      421 erqkskkdtt ciklkidsei kktvvlppiv asrgqseepa gktksmqevh iktleeikle
      481 kalrvqqsse sstsspsqhe atpgarrllr itkrtgmkee knlqegnevd sqssirteak
      541 easgettgvd itkiqvkrce tmrekhmqkq qereksvltp lrgdvascnt qvaekpvlta
      601 vpgitrhltk rlptkssqkv evetsgigds llnvkcaaqt lekrgkakpk vnvkpsvvkv
      661 vsspklapkr kavemhaavi aavkplssss vlqeppakka avavvplvse dksvtvpeae
      721 nprdslvlpp tqsssdsspp evsgpsssqm smktrrlssa stgkpplsve ddfekliwei
      781 sggkleaeid ldpgkdeddl llelsemids
//
LOCUS       NP_004951                526 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding protein FUS isoform 1 [Homo sapiens].
ACCESSION   NP_004951
VERSION     NP_004951.1
DBSOURCE    REFSEQ: accession NM_004960.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Hou,X., Shi,W., Luo,W., Luo,Y., Huang,X., Li,J., Ji,N. and Chen,Q.
  TITLE     FUS::DDIT3 Fusion Protein in the Development of Myxoid Liposarcoma
            and Possible Implications for Therapy
  JOURNAL   Biomolecules 14 (10), 1297 (2024)
   PUBMED   39456230
  REMARK    GeneRIF: FUS::DDIT3 Fusion Protein in the Development of Myxoid
            Liposarcoma and Possible Implications for Therapy.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Vazquez-Sanchez,S., Tilkin,B., Gasset-Rosa,F., Zhang,S., Piol,D.,
            McAlonis-Downes,M., Artates,J., Govea-Perez,N., Verresen,Y.,
            Guo,L., Cleveland,D.W., Shorter,J. and Da Cruz,S.
  TITLE     Frontotemporal dementia-like disease progression elicited by seeded
            aggregation and spread of FUS
  JOURNAL   Mol Neurodegener 19 (1), 46 (2024)
   PUBMED   38862967
  REMARK    GeneRIF: Frontotemporal dementia-like disease progression elicited
            by seeded aggregation and spread of FUS.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Chen,Y., Pei,X., Chen,L. and Chen,L.
  TITLE     A dynamic regulatory switch for phase separation of FUS protein:
            Zinc ions and zinc finger domain
  JOURNAL   Biochem Biophys Res Commun 710, 149862 (2024)
   PUBMED   38593618
  REMARK    GeneRIF: A dynamic regulatory switch for phase separation of FUS
            protein: Zinc ions and zinc finger domain.
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Ranji,P., Jonasson,E., Andersson,L., Filges,S., Luna Santamaria,M.,
            Vannas,C., Dolatabadi,S., Gustafsson,A., Myklebost,O.,
            Hakansson,J., Fagman,H., Landberg,G., Aman,P. and Stahlberg,A.
  TITLE     Deciphering the role of FUS::DDIT3 expression and tumor
            microenvironment in myxoid liposarcoma development
  JOURNAL   J Transl Med 22 (1), 389 (2024)
   PUBMED   38671504
  REMARK    GeneRIF: Deciphering the role of FUS::DDIT3 expression and tumor
            microenvironment in myxoid liposarcoma development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Shiramasa,Y., Yamamoto,R., Kashiwagi,N., Sasaki,F., Imai,S.,
            Ike,M., Kitazawa,S., Kameda,T. and Kitahara,R.
  TITLE     An aberrant fused in sarcoma liquid droplet of amyotrophic lateral
            sclerosis pathological variant, R495X, accelerates liquid-solid
            phase transition
  JOURNAL   Sci Rep 14 (1), 8914 (2024)
   PUBMED   38632300
  REMARK    GeneRIF: An aberrant fused in sarcoma liquid droplet of amyotrophic
            lateral sclerosis pathological variant, R495X, accelerates
            liquid-solid phase transition.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 526)
  AUTHORS   Panagopoulos,I., Mandahl,N., Ron,D., Hoglund,M., Nilbert,M.,
            Mertens,F., Mitelman,F. and Aman,P.
  TITLE     Characterization of the CHOP breakpoints and fusion transcripts in
            myxoid liposarcomas with the 12;16 translocation
  JOURNAL   Cancer Res 54 (24), 6500-6503 (1994)
   PUBMED   7987849
REFERENCE   7  (residues 1 to 526)
  AUTHORS   Ichikawa,H., Shimizu,K., Hayashi,Y. and Ohki,M.
  TITLE     An RNA-binding protein gene, TLS/FUS, is fused to ERG in human
            myeloid leukemia with t(16;21) chromosomal translocation
  JOURNAL   Cancer Res 54 (11), 2865-2868 (1994)
   PUBMED   8187069
REFERENCE   8  (residues 1 to 526)
  AUTHORS   Rabbitts,T.H., Forster,A., Larson,R. and Nathan,P.
  TITLE     Fusion of the dominant negative transcription regulator CHOP with a
            novel gene FUS by translocation t(12;16) in malignant liposarcoma
  JOURNAL   Nat Genet 4 (2), 175-180 (1993)
   PUBMED   7503811
REFERENCE   9  (residues 1 to 526)
  AUTHORS   Siddique,N. and Siddique,T.
  TITLE     Amyotrophic Lateral Sclerosis Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301623
REFERENCE   10 (residues 1 to 526)
  AUTHORS   Eneroth,M., Mandahl,N., Heim,S., Willen,H., Rydholm,A.,
            Alberts,K.A. and Mitelman,F.
  TITLE     Localization of the chromosomal breakpoints of the t(12;16) in
            liposarcoma to subbands 12q13.3 and 16p11.2
  JOURNAL   Cancer Genet Cytogenet 48 (1), 101-107 (1990)
   PUBMED   2372777
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009088.9 and BC002459.1.
            
            Summary: This gene encodes a multifunctional protein component of
            the heterogeneous nuclear ribonucleoprotein (hnRNP) complex. The
            hnRNP complex is involved in pre-mRNA splicing and the export of
            fully processed mRNA to the cytoplasm. This protein belongs to the
            FET family of RNA-binding proteins which have been implicated in
            cellular processes that include regulation of gene expression,
            maintenance of genomic integrity and mRNA/microRNA processing.
            Alternative splicing results in multiple transcript variants.
            Defects in this gene result in amyotrophic lateral sclerosis type
            6. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000402.2, AK290936.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000254108.12/ ENSP00000254108.8
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..526
                     /product="RNA-binding protein FUS isoform 1"
                     /note="heterogeneous nuclear ribonucleoprotein P2; fused
                     in sarcoma; fusion gene in myxoid liposarcoma; 75 kDa
                     DNA-pairing protein; RNA-binding protein FUS; oncogene
                     TLS; fus-like protein; oncogene FUS; translocated in
                     liposarcoma protein"
                     /calculated_mol_wt=53295
     Region          1..286
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35637.1)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:29897835; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:29897835; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000269|PubMed:18620545; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            175
                     /site_type="other"
                     /note="Breakpoint for translocation to form chimeric
                     FUS/ATF1 protein; propagated from UniProtKB/Swiss-Prot
                     (P35637.1)"
     Site            216
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            218
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            242
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            244
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            248
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            251
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            259
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            266..267
                     /site_type="other"
                     /note="Breakpoint for translocation to form FUS/TLS-CHOP
                     oncogene; propagated from UniProtKB/Swiss-Prot (P35637.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Region          283..368
                     /region_name="RRM_FUS_TAF15"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     fused in Ewing's sarcoma protein (FUS), TATA-binding
                     protein-associated factor 15 (TAF15) and similar proteins;
                     cd12535"
                     /db_xref="CDD:409951"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Region          375..424
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35637.1)"
     Site            377
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            383
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            386
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            388
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            394
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            407
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:12964758;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P56959; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Region          422..449
                     /region_name="zf-RanBP"
                     /note="Zn-finger in Ran binding protein and others;
                     pfam00641"
                     /db_xref="CDD:395516"
     Region          444..526
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35637.1)"
     Site            473
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            476
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            481
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            485
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            487
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            491
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            495
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            498
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            503
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:12964758;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     CDS             1..526
                     /gene="FUS"
                     /gene_synonym="ALS6; altFUS; ETM4; FUS1; HNRNPP2; POMP75;
                     TLS"
                     /coded_by="NM_004960.4:77..1657"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10707.1"
                     /db_xref="GeneID:2521"
                     /db_xref="HGNC:HGNC:4010"
                     /db_xref="MIM:137070"
ORIGIN      
        1 masndytqqa tqsygayptq pgqgysqqss qpygqqsysg ysqstdtsgy gqssyssygq
       61 sqntgygtqs tpqgygstgg ygssqssqss ygqqssypgy gqqpapssts gsygsssqss
      121 sygqpqsgsy sqqpsyggqq qsygqqqsyn ppqgygqqnq ynsssggggg gggggnygqd
      181 qssmssgggs gggygnqdqs ggggsggygq qdrggrgrgg sggggggggg gynrssggye
      241 prgrgggrgg rggmggsdrg gfnkfggprd qgsrhdseqd nsdnntifvq glgenvties
      301 vadyfkqigi iktnkktgqp minlytdret gklkgeatvs fddppsakaa idwfdgkefs
      361 gnpikvsfat rradfnrggg ngrggrgrgg pmgrggyggg gsggggrggf psgggggggq
      421 qragdwkcpn ptcenmnfsw rnecnqckap kpdgpgggpg gshmggnygd drrggrggyd
      481 rggyrgrggd rggfrggrgg gdrggfgpgk mdsrgehrqd rrerpy
//
LOCUS       NP_001387115            1207 aa            linear   PRI 21-NOV-2025
DEFINITION  protein transport protein Sec31A isoform 17 [Homo sapiens].
ACCESSION   NP_001387115
VERSION     NP_001387115.1
DBSOURCE    REFSEQ: accession NM_001400186.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1207)
  AUTHORS   Tobias,E.S., Lucas-Herald,A.K., Sagar,D., Montezano,A.C.,
            Rios,F.J., De Lucca Camargo,L., Hamilton,G., Gazdagh,G.,
            Diver,L.A., Williams,N., Herzyk,P., Touyz,R.M., Greenfield,A.,
            McGowan,R. and Ahmed,S.F.
  TITLE     SEC31A may be associated with pituitary hormone deficiency and
            gonadal dysgenesis
  JOURNAL   Endocrine 84 (2), 345-349 (2024)
   PUBMED   38400880
  REMARK    GeneRIF: SEC31A may be associated with pituitary hormone deficiency
            and gonadal dysgenesis.
REFERENCE   2  (residues 1 to 1207)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1207)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1207)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1207)
  AUTHORS   Jin,L., Pahuja,K.B., Wickliffe,K.E., Gorur,A., Baumgartel,C.,
            Schekman,R. and Rape,M.
  TITLE     Ubiquitin-dependent regulation of COPII coat size and function
  JOURNAL   Nature 482 (7386), 495-500 (2012)
   PUBMED   22358839
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1207)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1207)
  AUTHORS   Kim,J.H., Hong,J.A., Pih,K.T. and Hwang,I.
  TITLE     Identification and isolation of differentially expressed genes in
            osmotically stressed human oral keratinocytes
  JOURNAL   Arch Oral Biol 46 (4), 335-341 (2001)
   PUBMED   11269867
REFERENCE   8  (residues 1 to 1207)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 1207)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   10 (residues 1 to 1207)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021105.13 and AC108469.5.
            
            Summary: The protein encoded by this gene shares similarity with
            the yeast Sec31 protein, and is a component of the outer layer of
            the coat protein complex II (COPII). The encoded protein is
            involved in vesicle budding from the endoplasmic reticulum (ER) and
            contains multiple WD repeats near the N-terminus and a proline-rich
            region in the C-terminal half. It associates with the protein
            encoded by the SEC13 homolog, nuclear pore and COPII coat complex
            component (SEC13), and is required for ER-Golgi transport.
            Monoubiquitylation of this protein by CUL3-KLHL12 was found to
            regulate the size of COPII coats to accommodate unusually shaped
            cargo. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.179862.1,
                                           SRR14038197.1430191.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1207
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..1207
                     /product="protein transport protein Sec31A isoform 17"
                     /note="yeast Sec31p homolog; protein transport protein
                     Sec31A; web1-like protein; SEC31 homolog A, COPII coat
                     complex component; SEC31-related protein A; SEC31-like
                     protein 1; SEC31 homolog A, COPII coating complex
                     component"
                     /calculated_mol_wt=131605
     Region          4..47
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          13..332
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(26,40,46..47,52..53,91,95,101..102,117,121,139,144,
                     150..151,164,185,190,196..197,209..210,231,235,244..245,
                     258..259,277,282,288..289,301..302,320,325,331..332)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          68..111
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          70..119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          120..160
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          125..162
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          161..471
                     /region_name="Interaction with SEC13.
                     /evidence=ECO:0000269|PubMed:16957052"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          172..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          263..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          306..331
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            514
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94979.3)"
     Site            519
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (O94979.3)"
     Region          <560..>683
                     /region_name="ACE1-Sec16-like"
                     /note="Ancestral coatomer element 1 (ACE1) of COPII coat
                     complex assembly protein Sec16; cl14807"
                     /db_xref="CDD:449359"
     Site            order(561..565,567,569,580,582,583..584,586..587,591,597,
                     605,617,620,645..646)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187750"
     Region          778..895
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Site            786
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          787..1100
                     /region_name="Interaction with PDCD6.
                     /evidence=ECO:0000269|PubMed:16957052"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          <787..>1085
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          829..835
                     /region_name="ALG-2-binding site motif-2 (ABS-2)"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          911..1083
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Site            1148
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94979.3)"
     Site            1150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O94979.3)"
     CDS             1..1207
                     /gene="SEC31A"
                     /gene_synonym="ABP125; ABP130; HPBKS; HSPC275; HSPC334;
                     NEDSOSB; SEC31L1"
                     /coded_by="NM_001400186.1:71..3694"
                     /note="isoform 17 is encoded by transcript variant 27"
                     /db_xref="GeneID:22872"
                     /db_xref="HGNC:HGNC:17052"
                     /db_xref="MIM:610257"
ORIGIN      
        1 mklkevdrta mqawspaqnh piylatgtsa qqldatfstn asleifeldl sdpsldmksc
       61 atfssshryh kliwgpykmd skgdvsgvli aggengniil ydpskiiagd kevviaqndk
      121 htgpvraldv nifqtnlvas ganeseiyiw dlnnfatpmt pgaktqpped isciawnrqv
      181 qhilasasps gratvwdlrk nepiikvsdh snrmhcsgla whpdvatqmv laseddrlpv
      241 iqmwdlrfas splrvlenha rgilaiawsm adpelllscg kdakilcsnp ntgevlyelp
      301 tntqwcfdiq wcprnpavls aasfdgrisv ysimggstdg lrqkqvdkls ssfgnldpfg
      361 tgqplpplqi pqqtaqhsiv lplkkppkwi rrpvgasfsf ggklvtfenv rmpshqgaeq
      421 qqqqhhvfis qvvtekefls rsdqlqqavq sqgfinycqk kidasqtefe knvwsflkvn
      481 feddsrgkyl ellgyrkedl gkkalkdsdq vaqsdgeesp aaeeqllgeh ikeekeesef
      541 lpssggtfni svsgdidgli tqalltgnfe savdlclhdn rmadaiilai aggqellart
      601 qkkyfaksqs kitrlitavv mknwkeives cdlknwreal aavltyakpd efsalcdllg
      661 trlenegdsl lqtqaclcyi cagnveklva cwtkaqdgsh plslqdliek vvilrkavql
      721 tqamdtstvg vllaakmsqy anllaaqgsi aaalaflpdn tnqpnimqlr drlcraqgep
      781 vaghespkip yekqqlpkgr pgpvaghhqm prvqtqqyyp hgenppppgf imhgnvnpna
      841 agqlptspgh mhtqvppypq pqpyqpaqpy pfgtggsamy rpqqpvappt snaypntpyi
      901 ssassytgqs qlyaaqhqas sptsspatsf ppppssgasf qhggpgapps ssayalppgt
      961 tgtlpaasel pasqrtgpqn gwndppalnr vpkkkkmpen fmppvpitsp imnplgdpqs
     1021 qmlqqqpsap vplssqssfp qphlpggqpf hgvqqplgqt gmppsfskpn iegapgapig
     1081 ntfqhvqslp tkkitkkpip dehlilkttf edliqrclss atdpqtkrkl ddaskrlefl
     1141 ydklreqtls ptitsglhni arsietrnys egltmhthiv stsnfsetsa fmpvlkvvlt
     1201 qanklgv
//
LOCUS       NP_954649                708 aa            linear   PRI 21-NOV-2025
DEFINITION  kin of IRRE-like protein 2 isoform c precursor [Homo sapiens].
ACCESSION   NP_954649
VERSION     NP_954649.3
DBSOURCE    REFSEQ: accession NM_199180.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 708)
  AUTHORS   Voskarides,K., Stefanou,C., Pieri,M., Demosthenous,P., Felekkis,K.,
            Arsali,M., Athanasiou,Y., Xydakis,D., Stylianou,K., Daphnis,E.,
            Goulielmos,G., Loizou,P., Savige,J., Hohne,M., Volker,L.A.,
            Benzing,T., Maxwell,P.H., Gale,D.P., Gorski,M., Boger,C.,
            Kollerits,B., Kronenberg,F., Paulweber,B., Zavros,M., Pierides,A.
            and Deltas,C.
  TITLE     A functional variant in NEPH3 gene confers high risk of renal
            failure in primary hematuric glomerulopathies. Evidence for
            predisposition to microalbuminuria in the general population
  JOURNAL   PLoS One 12 (3), e0174274 (2017)
   PUBMED   28334007
  REMARK    GeneRIF: SNP V353M confers high risk of renal failure in primary
            hematuric glomerulopathies and predisposition to microalbuminuria
            in the general population
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 708)
  AUTHORS   Yesildag,B., Bock,T., Herrmanns,K., Wollscheid,B. and Stoffel,M.
  TITLE     Kin of IRRE-like Protein 2 Is a Phosphorylated Glycoprotein That
            Regulates Basal Insulin Secretion
  JOURNAL   J Biol Chem 290 (43), 25891-25906 (2015)
   PUBMED   26324709
REFERENCE   5  (residues 1 to 708)
  AUTHORS   Ristola,M. and Lehtonen,S.
  TITLE     Functions of the podocyte proteins nephrin and Neph3 and the
            transcriptional regulation of their genes
  JOURNAL   Clin Sci (Lond) 126 (5), 315-328 (2014)
   PUBMED   24219158
  REMARK    GeneRIF: summarize the current knowledge of the functions of
            nephrin and Neph-family proteins and transcription factors and
            agents that control nephrin and Neph3 gene expression.
            Review article
REFERENCE   6  (residues 1 to 708)
  AUTHORS   Ristola,M., Arpiainen,S., Saleem,M.A., Mathieson,P.W., Welsh,G.I.,
            Lehtonen,S. and Holthofer,H.
  TITLE     Regulation of Neph3 gene in podocytes--key roles of transcription
            factors NF-kappaB and Sp1
  JOURNAL   BMC Mol Biol 10, 83 (2009)
   PUBMED   19703278
  REMARK    GeneRIF: NF-kappaB and Sp1 response elements are essential for the
            basal transcriptional activity of the Neph3 promoter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 708)
  AUTHORS   Ihalmo,P., Schmid,H., Rastaldi,M.P., Mattinzoli,D., Langham,R.G.,
            Luimula,P., Kilpikari,R., Lassila,M., Gilbert,R.E., Kerjaschki,D.,
            Kretzler,M. and Holthofer,H.
  TITLE     Expression of filtrin in human glomerular diseases
  JOURNAL   Nephrol Dial Transplant 22 (7), 1903-1909 (2007)
   PUBMED   17442742
REFERENCE   8  (residues 1 to 708)
  AUTHORS   Rinta-Valkama,J., Aaltonen,P., Lassila,M., Palmen,T.,
            Tossavainen,P., Knip,M. and Holthofer,H.
  TITLE     Densin and filtrin in the pancreas and in the kidney, targets for
            humoral autoimmunity in patients with type 1 diabetes
  JOURNAL   Diabetes Metab Res Rev 23 (2), 119-126 (2007)
   PUBMED   16741999
  REMARK    GeneRIF: Filtrin can act as autoantigen, and autoantibodies against
            these can be detected in patients with type 1 diabetes.
REFERENCE   9  (residues 1 to 708)
  AUTHORS   Sun,C., Kilburn,D., Lukashin,A., Crowell,T., Gardner,H.,
            Brundiers,R., Diefenbach,B. and Carulli,J.P.
  TITLE     Kirrel2, a novel immunoglobulin superfamily gene expressed
            primarily in beta cells of the pancreatic islets
  JOURNAL   Genomics 82 (2), 130-142 (2003)
   PUBMED   12837264
  REMARK    GeneRIF: KIRREL2 protein is a beta-cell-expressed Ig domain protein
            and may be involved in pancreas development or beta cell function
REFERENCE   10 (residues 1 to 708)
  AUTHORS   Ihalmo,P., Palmen,T., Ahola,H., Valtonen,E. and Holthofer,H.
  TITLE     Filtrin is a novel member of nephrin-like proteins
  JOURNAL   Biochem Biophys Res Commun 300 (2), 364-370 (2003)
   PUBMED   12504092
  REMARK    GeneRIF: Identification of Filtrin as a member of nephrin-like
            proteins.
            GeneRIF: Filtrin is a novel protein with substantial homology to
            nephrin. It is a transmembrane protein of the immunoglobulin
            superfamily (apparent molecular weight 107 kDa) and most
            prominently expressed in the pancreas, lymph nodes as well as
            kidney glomerulus.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC007312.1, AB593116.1 and
            BM693057.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 17, 2014 this sequence version replaced NP_954649.2.
            
            Summary: This gene encodes a type I transmembrane protein and
            member of the immunoglobulin superfamily of cell adhesion
            molecules. The encoded protein localizes to adherens junctions in
            pancreatic beta cells and regulates insulin secretion.
            Autoantibodies against the encoded protein have been detected in
            serum from patients with type 1 diabetes. This gene may also play a
            role in glomerular development and decreased expression of this
            gene has been observed in human glomerular diseases. This gene and
            the related opposite-strand gene nephrin (GeneID: 527362) are
            regulated by a bidirectional promoter. [provided by RefSeq, Jul
            2016].
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longest isoform (c).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB593116.1, AY358742.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151405, SAMEA2153347
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360202.10/ ENSP00000353331.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..708
                     /product="kin of IRRE-like protein 2 isoform c precursor"
                     /note="nephrin-like gene 1; nephrin-like protein 3; kin of
                     irregular chiasm-like protein 2; kin of IRRE like 2"
                     /calculated_mol_wt=72748
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2363
     mat_peptide     21..708
                     /product="Kin of IRRE-like protein 2. /id=PRO_0000015096"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWL6.3)"
                     /calculated_mol_wt=72748
     Region          30..119
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          41..45
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          53..57
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          86..90
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          100..105
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          125..223
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          142..146
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            143
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UWL6.3)"
     Region          149..151
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWL6.3)"
     Region          157..161
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          187..191
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          201..206
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          216..219
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          226..295
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            301
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UWL6.3)"
     Region          312..378
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          397..501
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          415..419
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          429..433
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          467..471
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          482..487
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            484
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UWL6.3)"
     Region          495..498
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            511..531
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWL6.3)"
     Region          545..601
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWL6.3)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSU7; propagated from
                     UniProtKB/Swiss-Prot (Q6UWL6.3)"
     Site            603
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSU7; propagated from
                     UniProtKB/Swiss-Prot (Q6UWL6.3)"
     Site            604
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSU7; propagated from
                     UniProtKB/Swiss-Prot (Q6UWL6.3)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSU7; propagated from
                     UniProtKB/Swiss-Prot (Q6UWL6.3)"
     Region          684..708
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UWL6.3)"
     CDS             1..708
                     /gene="KIRREL2"
                     /gene_synonym="FILTRIN; NEPH3; NLG1"
                     /coded_by="NM_199180.4:210..2336"
                     /note="isoform c precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS12481.1"
                     /db_xref="GeneID:84063"
                     /db_xref="HGNC:HGNC:18816"
                     /db_xref="MIM:607762"
ORIGIN      
        1 mlrmrvpall vllfcfrgra gpsphflqqp edlvvllgee arlpcalgay wglvqwtksg
       61 lalggqrdlp gwsrywisgn aangqhdlhi rpveledeas yecqatqagl rsrpaqlhvl
      121 vppeapqvlg gpsvslvagv panltcrsrg darptpellw frdgvlldga tfhqtllkeg
      181 tpgsvestlt ltpfshddga tfvcrarsqa lptgrdtait lslqyppevt lsasphtvqe
      241 gekviflcqa taqppvtgyr wakggspvlg argprlevva dasfltepvs cevsnavgsa
      301 nrstaldvlf gpilqakpep vsvdvgedas fscawrgnpl prvtwtrrgg aqvlgsgatl
      361 rlpsvgpeda gdyvcraeag lsglrggaae arltvnappv vtalhsapaf lrgparlqcl
      421 vfaspapdav vwswdegfle agsqgrflve tfpapesrgg lgpglisvlh isgtqesdfs
      481 rsfncsarnr lgeggaqasl grrdllptvr ivagvaaatt tllmvitgva lccwrhskas
      541 asfseqknlm ripgssdgss srgpeeeetg sredrgpivh tdhsdlvlee egtletkdpt
      601 ngyykvrgvs vslslgeapg gglflpppsp lgppgtptfy dfnphlgmvp pcrlyrarag
      661 ylttphpraf tsyikptsfg ppdlapgtpp fpyaafptps hprlqthv
//
LOCUS       NP_001335669            1311 aa            linear   PRI 21-NOV-2025
DEFINITION  kinase D-interacting substrate of 220 kDa isoform 9 [Homo sapiens].
ACCESSION   NP_001335669
VERSION     NP_001335669.1
DBSOURCE    REFSEQ: accession NM_001348740.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1311)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1311)
  AUTHORS   Zhang,J., Zhang,Y., Shang,Q., Cheng,Y., Su,Y., Zhang,J., Wang,T.,
            Ding,J., Li,Y., Xie,Y. and Xing,Q.
  TITLE     Gain-of-Function KIDINS220 Variants Disrupt Neuronal Development
            and Cause Cerebral Palsy
  JOURNAL   Mov Disord 39 (3), 498-509 (2024)
   PUBMED   38148610
  REMARK    GeneRIF: Gain-of-Function KIDINS220 Variants Disrupt Neuronal
            Development and Cause Cerebral Palsy.
REFERENCE   3  (residues 1 to 1311)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1311)
  AUTHORS   Bondeson,D.P., Paolella,B.R., Asfaw,A., Rothberg,M.V.,
            Skipper,T.A., Langan,C., Mesa,G., Gonzalez,A., Surface,L.E.,
            Ito,K., Kazachkova,M., Colgan,W.N., Warren,A., Dempster,J.M.,
            Krill-Burger,J.M., Ericsson,M., Tang,A.A., Fung,I., Chambers,E.S.,
            Abdusamad,M., Dumont,N., Doench,J.G., Piccioni,F., Root,D.E.,
            Boehm,J., Hahn,W.C., Mannstadt,M., McFarland,J.M., Vazquez,F. and
            Golub,T.R.
  TITLE     Phosphate dysregulation via the XPR1-KIDINS220 protein complex is a
            therapeutic vulnerability in ovarian cancer
  JOURNAL   Nat Cancer 3 (6), 681-695 (2022)
   PUBMED   35437317
  REMARK    GeneRIF: Phosphate dysregulation via the XPR1-KIDINS220 protein
            complex is a therapeutic vulnerability in ovarian cancer.
REFERENCE   5  (residues 1 to 1311)
  AUTHORS   Scholz-Starke,J. and Cesca,F.
  TITLE     Stepping Out of the Shade: Control of Neuronal Activity by the
            Scaffold Protein Kidins220/ARMS
  JOURNAL   Front Cell Neurosci 10, 68 (2016)
   PUBMED   27013979
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1311)
  AUTHORS   Arevalo,J.C., Yano,H., Teng,K.K. and Chao,M.V.
  TITLE     A unique pathway for sustained neurotrophin signaling through an
            ankyrin-rich membrane-spanning protein
  JOURNAL   EMBO J 23 (12), 2358-2368 (2004)
   PUBMED   15167895
REFERENCE   7  (residues 1 to 1311)
  AUTHORS   Riol-Blanco,L., Iglesias,T., Sanchez-Sanchez,N., de la Rosa,G.,
            Sanchez-Ruiloba,L., Cabrera-Poch,N., Torres,A., Longo,I.,
            Garcia-Bordas,J., Longo,N., Tejedor,A., Sanchez-Mateos,P. and
            Rodriguez-Fernandez,J.L.
  TITLE     The neuronal protein Kidins220 localizes in a raft compartment at
            the leading edge of motile immature dendritic cells
  JOURNAL   Eur J Immunol 34 (1), 108-118 (2004)
   PUBMED   14971036
REFERENCE   8  (residues 1 to 1311)
  AUTHORS   Kong,H., Boulter,J., Weber,J.L., Lai,C. and Chao,M.V.
  TITLE     An evolutionarily conserved transmembrane protein that is a novel
            downstream target of neurotrophin and ephrin receptors
  JOURNAL   J Neurosci 21 (1), 176-185 (2001)
   PUBMED   11150334
REFERENCE   9  (residues 1 to 1311)
  AUTHORS   Iglesias,T., Cabrera-Poch,N., Mitchell,M.P., Naven,T.J.,
            Rozengurt,E. and Schiavo,G.
  TITLE     Identification and cloning of Kidins220, a novel neuronal substrate
            of protein kinase D
  JOURNAL   J Biol Chem 275 (51), 40048-40056 (2000)
   PUBMED   10998417
REFERENCE   10 (residues 1 to 1311)
  AUTHORS   Kaplan,D.R. and Miller,F.D.
  TITLE     Signal transduction by the neurotrophin receptors
  JOURNAL   Curr Opin Cell Biol 9 (2), 213-221 (1997)
   PUBMED   9069267
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012495.9, AC011747.8 and
            AK094521.1.
            
            Summary: This gene encodes a transmembrane protein that is
            preferentially expressed in the nervous system where it controls
            neuronal cell survival, differentiation into exons and dendrites,
            and synaptic plasticity. The encoded protein interacts with
            membrane receptors, cytosolic signaling components, and
            cytoskeletal proteins, serving as a scaffold that mediates
            crosstalk between the neurotrophin pathway and several other
            intracellular signaling pathways. Aberrant expression of this gene
            is associated with the onset of various neuropsychiatric disorders
            and neurodegenerative diseases, including Alzheimer's disease.
            Naturally occurring mutations in this gene are associated with a
            syndrome characterized by spastic paraplegia, intellectual
            disability, nystagmus and obesity. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Feb 2017].
            
            Transcript Variant: This variant (10) has multiple coding region
            differences and differs in the 3' UTR, compared to variant 1. The
            encoded isoform (10) is shorter and has a distinct C-terminus,
            compared to isoform 1. Both variants 9 and 10 encode the same
            isoform (9).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.112325.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1311
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.1"
     Protein         1..1311
                     /product="kinase D-interacting substrate of 220 kDa
                     isoform 9"
                     /note="ankyrin repeat-rich membrane-spanning protein;
                     kinase D-interacting substrate 220kDa"
                     /calculated_mol_wt=145917
     Region          18..307
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          38..68
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(39,43..44,47..49,51..52,56,59,68,70,72,76..77,
                     80..82,84..85,89,92,101,103,105,109..110,113..115,
                     117..118,122,125)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          70..101
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          103..132
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          170..198
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          236..267
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          269..299
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          274..366
                     /region_name="Ank_2"
                     /note="Ankyrin repeats (3 copies); pfam12796"
                     /db_xref="CDD:463710"
     Region          302..332
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          335..366
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <349..413
                     /region_name="PHA02736"
                     /note="Viral ankyrin protein; Provisional"
                     /db_xref="CDD:165103"
     Region          441..954
                     /region_name="KAP_NTPase"
                     /note="KAP family P-loop domain; pfam07693"
                     /db_xref="CDD:462231"
     CDS             1..1311
                     /gene="KIDINS220"
                     /gene_synonym="ARMS; SINO; VENARG"
                     /coded_by="NM_001348740.2:171..4106"
                     /note="isoform 9 is encoded by transcript variant 10"
                     /db_xref="GeneID:57498"
                     /db_xref="HGNC:HGNC:29508"
                     /db_xref="MIM:615759"
ORIGIN      
        1 msvlisqsvi nyveeenipa lkallekckd vdernecgqt plmiaaeqgn leivkelikn
       61 gancnledld nwtalisask eghvhiveel lkcgvnlehr dmggwtalmw acykgrtdvv
      121 elllshganp svtglqysvy piiwaagrgh adivhlllqn gakvncsdky gttplvwaar
      181 kghlecvkhl lamgadvdqe gansmtaliv avkggytqsv keilkrnpnv nltdkdgnta
      241 lmiaskeght eivqdlldag tyvnipdrsg dtvligavrg ghveivrall qkyadidirg
      301 qdnktalywa vekgnatmvr dilqcnpdte ictkdgetpl ikatkmrnie vvellldkga
      361 kvsavdkkgd tplhiairgr srklaelllr npkdgrllyr pnkagetpyn idcshqksil
      421 tqifgarhls ptetdgdmlg ydlyssalad ilseptmqpp icvglyaqwg sgksfllkkl
      481 edemktfagq qieplfqfsw livfltlllc gglgllfaft vhpnlgiavs lsflallyif
      541 fiviyfggrr egeswnwawv lstrlarhig ylelllklmf vnppelpeqt tkalpvrflf
      601 tdynrlssvg getslaemia tlsdaceref gflatrlfrv fktedtqgkk kwkktcclps
      661 fviflfiigc iisgitllai frvdpkhltv navlisiasv vglafvlncr twwqvldsll
      721 nsqrkrlhna asklhklkse gfmkvlkcev elmarmakti dsftqnqtrl vviidgldac
      781 eqdkvlqmld tvrvlfskgp fiaifasdph iiikainqnl nsvlrdsnin ghdymrnivh
      841 lpvflnsrgl snarkflvts atngdvpcsd ttgiqedadr rvsqnslgem tklgsktaln
      901 rrdtyrrrqm qrtitrqmsf dltkllvted wfsdispqtm rrllnivsvt grllranqis
      961 fnwdrlaswi nlteqwpyrt swlilyleet egipdqmtlk tiyeriskni pttkdvepll
     1021 eidgdirnfe vflssrtpvl vardvkvflp ctvnldpklr eiiadvraar eqisigglay
     1081 pplplhegpp rapsgysqpp svcsstsfng pfaggvvspq phssyysgmt gpqhpfynrg
     1141 sgpapgpvvl lnslnvdavc eklkqiegld qsmlpqyctt ikkaningrv laqcnidelk
     1201 kemnmnfgdw hlfrstvlem rnaeshvvpe dprflsesss gpaphgepar rashnelpht
     1261 elssqtpytl nfsfeelntl gldegaprhs nlswqeenag leidsssedp d
//
LOCUS       NP_006223                150 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerases I, II, and III subunit RPABC3 isoform
            2 [Homo sapiens].
ACCESSION   NP_006223 XP_006713731
VERSION     NP_006223.2
DBSOURCE    REFSEQ: accession NM_006232.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 150)
  AUTHORS   Zhao,D., Liu,W., Chen,K., Wu,Z., Yang,H. and Xu,Y.
  TITLE     Structure of the human RNA polymerase I elongation complex
  JOURNAL   Cell Discov 7 (1), 97 (2021)
   PUBMED   34671025
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 150)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   6  (residues 1 to 150)
  AUTHORS   Kato,H., Sumimoto,H., Pognonec,P., Chen,C.H., Rosen,C.A. and
            Roeder,R.G.
  TITLE     HIV-1 Tat acts as a processivity factor in vitro in conjunction
            with cellular elongation factors
  JOURNAL   Genes Dev 6 (4), 655-666 (1992)
   PUBMED   1559613
REFERENCE   7  (residues 1 to 150)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
REFERENCE   8  (residues 1 to 150)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 150)
  AUTHORS   Southgate,C., Zapp,M.L. and Green,M.R.
  TITLE     Activation of transcription by HIV-1 Tat protein tethered to
            nascent RNA through another protein
  JOURNAL   Nature 345 (6276), 640-642 (1990)
   PUBMED   2190099
REFERENCE   10 (residues 1 to 150)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078797.20.
            
            On or before Nov 5, 2016 this sequence version replaced
            XP_006713731.1, NP_006223.1.
            
            Summary: The three eukaryotic RNA polymerases are complex
            multisubunit enzymes that play a central role in the transcription
            of nuclear genes. This gene encodes an essential and highly
            conserved subunit of RNA polymerase II that is shared by the other
            two eukaryotic DNA-directed RNA polymerases, I and III. Alternative
            splicing results in multiple transcript variants of this gene.
            [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 3' coding region, which results in a frameshift, compared to
            variant 1. It encodes isoform 2, which has a shorter and distinct
            C-terminus, compared to isoform 1. Variants 2 and 8-14 all encode
            the same isoform (2).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3185127.1,
                                           SRR14038193.71669.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000456318.6/ ENSP00000392913.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..150
                     /product="DNA-directed RNA polymerases I, II, and III
                     subunit RPABC3 isoform 2"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerases I, II, and III subunit
                     RPABC3; RPB8 homolog; DNA-directed RNA polymerase II
                     subunit H; DNA-directed RNA polymerases I, II, and III
                     17.1 kDa polypeptide; polymerase (RNA) II (DNA directed)
                     polypeptide H; polymerase (RNA) II subunit H"
                     /calculated_mol_wt=17012
     Region          2..147
                     /region_name="RPOL8c"
                     /note="RNA polymerase subunit 8; smart00658"
                     /db_xref="CDD:197821"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P52434.4)"
     Region          16..40
                     /region_name="Non-specific ssDNA binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P52434.4)"
     CDS             1..150
                     /gene="POLR2H"
                     /gene_synonym="RPABC3; RPB17; RPB8"
                     /coded_by="NM_006232.5:1058..1510"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3264.1"
                     /db_xref="GeneID:5437"
                     /db_xref="HGNC:HGNC:9195"
                     /db_xref="MIM:606023"
ORIGIN      
        1 magilfedif dvkdidpegk kfdrvsrlhc esesfkmdli ldvniqiypv dlgdkfrlvi
       61 astlyedgtl ddgeynptdd rpsradqfey vmygkvyrie gdetsteaat rlsayvsygg
      121 llmrlqgdan nlhgfevdsr vyllmkklaf
//
LOCUS       NP_001269810            1188 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 2 isoform c [Homo
            sapiens].
ACCESSION   NP_001269810 XP_005251166
VERSION     NP_001269810.1
DBSOURCE    REFSEQ: accession NM_001282881.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1188)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1188)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   3  (residues 1 to 1188)
  AUTHORS   Mechaussier,S., Almoallem,B., Zeitz,C., Van Schil,K., Jeddawi,L.,
            Van Dorpe,J., Duenas Rey,A., Condroyer,C., Pelle,O., Polak,M.,
            Boddaert,N., Bahi-Buisson,N., Cavallin,M., Bacquet,J.L.,
            Mouallem-Beziere,A., Zambrowski,O., Sahel,J.A., Audo,I., Kaplan,J.,
            Rozet,J.M., De Baere,E. and Perrault,I.
  TITLE     Loss of Function of RIMS2 Causes a Syndromic Congenital Cone-Rod
            Synaptic Disease with Neurodevelopmental and Pancreatic Involvement
  JOURNAL   Am J Hum Genet 106 (6), 859-871 (2020)
   PUBMED   32470375
  REMARK    GeneRIF: Loss of Function of RIMS2 Causes a Syndromic Congenital
            Cone-Rod Synaptic Disease with Neurodevelopmental and Pancreatic
            Involvement.
            Erratum:[Am J Hum Genet. 2020 Sep 3;107(3):580. doi:
            10.1016/j.ajhg.2020.08.004. PMID: 32888510]
REFERENCE   4  (residues 1 to 1188)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 1188)
  AUTHORS   Kim,K.T., Lee,J.S., Lee,B.W., Seok,H., Jeon,H.S., Kim,J.H. and
            Chung,J.H.
  TITLE     Association between regulating synaptic membrane exocytosis 2 gene
            polymorphisms and degenerative lumbar scoliosis
  JOURNAL   Biomed Rep 1 (4), 619-623 (2013)
   PUBMED   24648997
REFERENCE   6  (residues 1 to 1188)
  AUTHORS   Sun,L., Bittner,M.A. and Holz,R.W.
  TITLE     Rim, a component of the presynaptic active zone and modulator of
            exocytosis, binds 14-3-3 through its N terminus
  JOURNAL   J Biol Chem 278 (40), 38301-38309 (2003)
   PUBMED   12871946
REFERENCE   7  (residues 1 to 1188)
  AUTHORS   Fukuda,M.
  TITLE     Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and
            Noc2. Identification of a critical determinant of Rab3A/Rab27A
            recognition by Rim2
  JOURNAL   J Biol Chem 278 (17), 15373-15380 (2003)
   PUBMED   12578829
REFERENCE   8  (residues 1 to 1188)
  AUTHORS   Wang,Y. and Sudhof,T.C.
  TITLE     Genomic definition of RIM proteins: evolutionary amplification of a
            family of synaptic regulatory proteins
  JOURNAL   Genomics 81 (2), 126-137 (2003)
   PUBMED   12620390
REFERENCE   9  (residues 1 to 1188)
  AUTHORS   Kashima,Y., Miki,T., Shibasaki,T., Ozaki,N., Miyazaki,M., Yano,H.
            and Seino,S.
  TITLE     Critical role of cAMP-GEFII--Rim2 complex in incretin-potentiated
            insulin secretion
  JOURNAL   J Biol Chem 276 (49), 46046-46053 (2001)
   PUBMED   11598134
REFERENCE   10 (residues 1 to 1188)
  AUTHORS   Fenster,S.D., Chung,W.J., Zhai,R., Cases-Langhoff,C., Voss,B.,
            Garner,A.M., Kaempf,U., Kindler,S., Gundelfinger,E.D. and
            Garner,C.C.
  TITLE     Piccolo, a presynaptic zinc finger protein structurally related to
            bassoon
  JOURNAL   Neuron 25 (1), 203-214 (2000)
   PUBMED   10707984
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP230765.1, AB018294.1 and
            AP002849.2.
            
            On Sep 20, 2013 this sequence version replaced XP_005251166.1.
            
            Summary: The protein encoded by this gene is a presynaptic protein
            that interacts with RAB3, a protein important for normal
            neurotransmitter release. The encoded protein can also bind several
            other synaptic proteins, including UNC-13 homolog B,
            ELKS/Rab6-interacting/CAST family member 1, and synaptotagmin 1.
            This protein is involved in synaptic membrane exocytosis.
            Polymorphisms in this gene have been associated with degenerative
            lumbar scoliosis. [provided by RefSeq, Feb 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.176491.1,
                                           SRR1803613.180778.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1188
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..1188
                     /product="regulating synaptic membrane exocytosis protein
                     2 isoform c"
                     /note="RAB3 interacting protein 3; regulating synaptic
                     membrane exocytosis protein 2; nuclear protein; non-small
                     cell lung cancer RimL3a protein; non-small cell lung
                     cancer RimL3c protein; rab3-interacting molecule 2;
                     rab-3-interacting protein 3; rab-3-interacting molecule 2;
                     Rab3-interacting protein"
                     /calculated_mol_wt=135120
     Region          431..530
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(455..461,476,479,509,513,516..517)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          582..708
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(613,619,674,676,684)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          1019..1164
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(1076,1080..1081,1083,1086,1114,1116,1118,1162..1163)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..1188
                     /gene="RIMS2"
                     /gene_synonym="CRSDS; OBOE; RAB3IP3; RIM2"
                     /coded_by="NM_001282881.2:289..3855"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS64948.1"
                     /db_xref="GeneID:9699"
                     /db_xref="HGNC:HGNC:17283"
                     /db_xref="MIM:606630"
ORIGIN      
        1 mqfetlrqvc nsvlshfhgv fssppnilqn elfgqtlnna rkrspsvsrd qnrrydqree
       61 reeysqyats dtamprspsd yadrrsqhep qfyedsdhls yrdsnrrshr hskeyivdde
      121 dvesrdeyer qrreeeyqsr yrsdpnlary pvkpqpyeeq mrihaevsra rherrhsdvs
      181 lanadledsr ismlrmdrps rqrsiserra amenqrsysm ertreaqgps syaqrttnhs
      241 pptprrsplp idrpdlrrtd slrkqhhldp ssavrktkre kmetmlrnds lssdqsesvr
      301 ppppkphksk kggkmrqisl ssseeelast peytscddve iesesvsekg dsqkgkrkts
      361 eqavlsdsnt rserqkemmy fgghsleedl ewsepqikds gvdtcssttl neehshsdkh
      421 pvtwqpskdg drligrilln krlkdgsvpr dsgamlglkv vggkmtesgr lcafitkvkk
      481 gsladtvghl rpgdevlewn grllqgatfe evyniilesk pepqvelvvs rpigdiprip
      541 dsthaqless sssfesqkmd rpsisvtspm spgmlrdvpq flsgqlsikl wfdkvghqli
      601 vtilgakdlp sredgrprnp yvkiyflpdr sdknkrrtkt vkktlepkwn qtfiyspvhr
      661 refrermlei tlwdqarvre eeseflgeil ieletalldd ephwyklqth dvsslplphp
      721 spymprrqlh gesptrrlqr skrisdsevs dydcddgigv vsdyrhdgrd lqsstlsvpe
      781 qvmssnhcsp sgsphrvdvi grtrswspsv pppqsrnveq glrgtrtmtg hyntisrmdr
      841 hrvmddhysp drdrdceaad rqpyhrsrst eqrpllertt trsrsterpd tnlmrsmpsl
      901 mtgrsappsp alsrshprtg svqtspsstp vagrrgrqlp qlppkgtldr kaggkklrst
      961 vqrstetgla vemrnwmtrq asrestdgsm nsyssegnli fpgvrlasds qfsdfldglg
     1021 paqlvgrqtl atpamgdiqv gmmdkkgqle veiirarglv vkpgsktlpa pyvkvylldn
     1081 gvciakkktk varktleply qqllsfeesp qgkvlqiivw gdygrmdhks fmgvaqilld
     1141 elelsnmvig wfklfppssl vdptlapltr rasqssless tgpsysrs
//
LOCUS       NP_008973                124 aa            linear   PRI 21-NOV-2025
DEFINITION  ribonuclease P protein subunit p14 [Homo sapiens].
ACCESSION   NP_008973
VERSION     NP_008973.1
DBSOURCE    REFSEQ: accession NM_007042.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Wu,J., Niu,S., Tan,M., Huang,C., Li,M., Song,Y., Wang,Q., Chen,J.,
            Shi,S., Lan,P. and Lei,M.
  TITLE     Cryo-EM Structure of the Human Ribonuclease P Holoenzyme
  JOURNAL   Cell 175 (5), 1393-1404 (2018)
   PUBMED   30454648
REFERENCE   6  (residues 1 to 124)
  AUTHORS   Autio,K.J., Kastaniotis,A.J., Pospiech,H., Miinalainen,I.J.,
            Schonauer,M.S., Dieckmann,C.L. and Hiltunen,J.K.
  TITLE     An ancient genetic link between vertebrate mitochondrial fatty acid
            synthesis and RNA processing
  JOURNAL   FASEB J 22 (2), 569-578 (2008)
   PUBMED   17898086
REFERENCE   7  (residues 1 to 124)
  AUTHORS   Jiang,T., Guerrier-Takada,C. and Altman,S.
  TITLE     Protein-RNA interactions in the subunits of human nuclear RNase P
  JOURNAL   RNA 7 (7), 937-941 (2001)
   PUBMED   11455963
REFERENCE   8  (residues 1 to 124)
  AUTHORS   Jiang,T. and Altman,S.
  TITLE     Protein-protein interactions with subunits of human nuclear RNase P
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 920-925 (2001)
   PUBMED   11158571
REFERENCE   9  (residues 1 to 124)
  AUTHORS   Jarrous,N., Wolenski,J.S., Wesolowski,D., Lee,C. and Altman,S.
  TITLE     Localization in the nucleolus and coiled bodies of protein subunits
            of the ribonucleoprotein ribonuclease P
  JOURNAL   J Cell Biol 146 (3), 559-572 (1999)
   PUBMED   10444065
REFERENCE   10 (residues 1 to 124)
  AUTHORS   Jarrous,N., Eder,P.S., Wesolowski,D. and Altman,S.
  TITLE     Rpp14 and Rpp29, two protein subunits of human ribonuclease P
  JOURNAL   RNA 5 (2), 153-157 (1999)
   PUBMED   10024167
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC360931.1, BC002441.1 and
            AC098479.2.
            
            Summary: This gene encodes a subunit of ribonuclease P and has 3'
            to 5' exoribonuclease activity. Transcripts for this gene are
            bicistronic and include a conserved downstream open reading frame
            for the hydroxyacyl-thioester dehydratase type 2 (HTD2) gene.
            [provided by RefSeq, May 2017].
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853564.19467.1,
                                           SRR14038193.4160652.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295959.10/ ENSP00000295959.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.3"
     Protein         1..124
                     /product="ribonuclease P protein subunit p14"
                     /EC_number="3.1.26.5"
                     /note="ribonuclease P/MRP 14kDa subunit"
                     /calculated_mol_wt=13562
     Region          35..108
                     /region_name="RNase_P_Rpp14"
                     /note="Rpp14/Pop5 family; pfam01900"
                     /db_xref="CDD:460379"
     CDS             1..124
                     /gene="RPP14"
                     /gene_synonym="P14"
                     /coded_by="NM_007042.6:195..569"
                     /db_xref="CCDS:CCDS2888.1"
                     /db_xref="GeneID:11102"
                     /db_xref="HGNC:HGNC:30327"
                     /db_xref="MIM:606112"
ORIGIN      
        1 mpapaatyer vvyknpseyh ymkvclefqd cgvglnaaqf kqllisavkd lfgevdaalp
       61 ldiltyeekt lsailricss glvklwsslt llgsykgkkc afrviqvspf llalsgnsre
      121 lvld
//
LOCUS       NP_055103                177 aa            linear   PRI 21-NOV-2025
DEFINITION  centromere protein R isoform 2 [Homo sapiens].
ACCESSION   NP_055103
VERSION     NP_055103.3
DBSOURCE    REFSEQ: accession NM_014288.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Tian,T., Chen,L., Dou,Z., Yang,Z., Gao,X., Yuan,X., Wang,C.,
            Liu,R., Shen,Z., Gui,P., Teng,M., Meng,X., Hill,D.L., Li,L.,
            Zhang,X., Liu,X., Sun,L., Zang,J. and Yao,X.
  TITLE     Structural insights into human CCAN complex assembled onto DNA
  JOURNAL   Cell Discov 8 (1), 90 (2022)
   PUBMED   36085283
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Liang,Q., Tan,C., Xiao,F., Yin,F., Liu,M., Lei,L., Wu,L., Yang,Y.,
            Tan,H.J.J., Liu,S. and Zeng,X.
  TITLE     Integrated profiling identifies ITGB3BP as prognostic biomarker for
            hepatocellular carcinoma
  JOURNAL   Bosn J Basic Med Sci 21 (6), 712-723 (2021)
   PUBMED   33974527
  REMARK    GeneRIF: Integrated profiling identifies ITGB3BP as prognostic
            biomarker for hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Cao,Z., Ge,S., Xu,Z. and Ma,Y.Q.
  TITLE     beta3-Endonexin interacts with ninein in vascular endothelial cells
            to promote angiogenesis
  JOURNAL   Biochem Biophys Res Commun 566, 75-79 (2021)
   PUBMED   34118594
  REMARK    GeneRIF: beta3-Endonexin interacts with ninein in vascular
            endothelial cells to promote angiogenesis.
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Li,D., Wang,F. and Samuels,H.H.
  TITLE     Domain structure of the NRIF3 family of coregulators suggests
            potential dual roles in transcriptional regulation
  JOURNAL   Mol Cell Biol 21 (24), 8371-8384 (2001)
   PUBMED   11713274
REFERENCE   6  (residues 1 to 177)
  AUTHORS   Ohtoshi,A., Maeda,T., Higashi,H., Ashizawa,S., Yamada,M. and
            Hatakeyama,M.
  TITLE     beta3-endonexin as a novel inhibitor of cyclin A-associated kinase
  JOURNAL   Biochem Biophys Res Commun 267 (3), 947-952 (2000)
   PUBMED   10673397
REFERENCE   7  (residues 1 to 177)
  AUTHORS   Tang,S., Gao,Y. and Ware,J.A.
  TITLE     Enhancement of endothelial cell migration and in vitro tube
            formation by TAP20, a novel beta 5 integrin-modulating, PKC
            theta-dependent protein
  JOURNAL   J Cell Biol 147 (5), 1073-1084 (1999)
   PUBMED   10579726
REFERENCE   8  (residues 1 to 177)
  AUTHORS   Li,D., Desai-Yajnik,V., Lo,E., Schapira,M., Abagyan,R. and
            Samuels,H.H.
  TITLE     NRIF3 is a novel coactivator mediating functional specificity of
            nuclear hormone receptors
  JOURNAL   Mol Cell Biol 19 (10), 7191-7202 (1999)
   PUBMED   10490654
REFERENCE   9  (residues 1 to 177)
  AUTHORS   Kashiwagi,H., Schwartz,M.A., Eigenthaler,M., Davis,K.A.,
            Ginsberg,M.H. and Shattil,S.J.
  TITLE     Affinity modulation of platelet integrin alphaIIbbeta3 by
            beta3-endonexin, a selective binding partner of the beta3 integrin
            cytoplasmic tail
  JOURNAL   J Cell Biol 137 (6), 1433-1443 (1997)
   PUBMED   9182673
REFERENCE   10 (residues 1 to 177)
  AUTHORS   Shattil,S.J., O'Toole,T., Eigenthaler,M., Thon,V., Williams,M.,
            Babior,B.M. and Ginsberg,M.H.
  TITLE     Beta 3-endonexin, a novel polypeptide that interacts specifically
            with the cytoplasmic tail of the integrin beta 3 subunit
  JOURNAL   J Cell Biol 131 (3), 807-816 (1995)
   PUBMED   7593198
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU853146.1, BC009929.2 and
            AA873717.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 11, 2003 this sequence version replaced NP_055103.2.
            
            Summary: This gene encodes a transcriptional coregulator that binds
            to and enhances the activity of members of the nuclear receptor
            families, thyroid hormone receptors and retinoid X receptors. This
            protein also acts as a corepressor of NF-kappaB-dependent
            signaling. This protein induces apoptosis in breast cancer cells
            through a caspase 2-mediated signaling pathway. This protein is
            also a component of the centromere-specific histone H3 variant
            nucleosome associated complex (CENP-NAC) and may be involved in
            mitotic progression by recruiting the histone H3 variant CENP-A to
            the centromere. Alternate splicing results in multiple transcript
            variants. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1. Isoform 2 is
            shorter, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC009929.2, AF175306.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000271002.15/ ENSP00000271002.10
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..177
                     /product="centromere protein R isoform 2"
                     /note="beta 3 endonexin; centromere protein R; integrin
                     beta-3-binding protein; nuclear receptor-interacting
                     factor 3; integrin beta 3 binding protein
                     (beta3-endonexin)"
                     /calculated_mol_wt=20063
     Region          9..13
                     /region_name="LXXLL motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13352.2)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13352.2)"
     Region          20..50
                     /region_name="DD1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13352.2)"
     Region          25..161
                     /region_name="CENP-R"
                     /note="Kinetochore component, CENP-R; pfam06729"
                     /db_xref="CDD:429086"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:11713274; propagated from
                     UniProtKB/Swiss-Prot (Q13352.2)"
     Region          41..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13352.2)"
     Region          63..66
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13352.2)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13352.2)"
     Region          172..176
                     /region_name="LXXIL motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13352.2)"
     CDS             1..177
                     /gene="ITGB3BP"
                     /gene_synonym="CENP-R; CENPR; HSU37139; NRIF3; TAP20"
                     /coded_by="NM_014288.5:93..626"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS30736.1"
                     /db_xref="GeneID:23421"
                     /db_xref="HGNC:HGNC:6157"
                     /db_xref="MIM:605494"
ORIGIN      
        1 mpvkrslkld glleensfdp skitrkksvi tyspttgtcq mslfasptss eeqkhrngls
       61 nekrkklnhp slteskestt kdndefmmll skveklseei meimqnlssi qalegsrele
      121 nligiscash flkremqktk elmtkvnkqk lfekstglph kasrhldsye flkailn
//
LOCUS       NP_001385211             301 aa            linear   PRI 21-NOV-2025
DEFINITION  TIMELESS-interacting protein isoform 1 [Homo sapiens].
ACCESSION   NP_001385211 XP_011520045
VERSION     NP_001385211.1
DBSOURCE    REFSEQ: accession NM_001398282.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Arai,H., Xiao,Y., Millstein,J., Wang,J., Battaglin,F.,
            Kawanishi,N., Jayachandran,P., Soni,S., Zhang,W., Mancao,C.,
            Salhia,B., Mumenthaler,S.M., Parikh,A.R. and Lenz,H.J.
  TITLE     Germline polymorphisms in genes maintaining the replication fork
            predict the efficacy of oxaliplatin and irinotecan in patients with
            metastatic colorectal cancer
  JOURNAL   Br J Cancer 126 (1), 72-78 (2022)
   PUBMED   34689170
  REMARK    GeneRIF: Germline polymorphisms in genes maintaining the
            replication fork predict the efficacy of oxaliplatin and irinotecan
            in patients with metastatic colorectal cancer.
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Grabarczyk,D.B.
  TITLE     The Fork Protection Complex: A Regulatory Hub at the Head of the
            Replisome
  JOURNAL   Subcell Biochem 99, 83-107 (2022)
   PUBMED   36151374
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Lerner,L.K., Holzer,S., Kilkenny,M.L., Svikovic,S., Murat,P.,
            Schiavone,D., Eldridge,C.B., Bittleston,A., Maman,J.D., Branzei,D.,
            Stott,K., Pellegrini,L. and Sale,J.E.
  TITLE     Timeless couples G-quadruplex detection with processing by DDX11
            helicase during DNA replication
  JOURNAL   EMBO J 39 (18), e104185 (2020)
   PUBMED   32705708
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Gotter,A.L., Suppa,C. and Emanuel,B.S.
  TITLE     Mammalian TIMELESS and Tipin are evolutionarily conserved
            replication fork-associated factors
  JOURNAL   J Mol Biol 366 (1), 36-52 (2007)
   PUBMED   17141802
  REMARK    GeneRIF: TIM and Tipin are functional orthologs of their
            replisome-associated yeast counterparts capable of coordinating
            replication with genotoxic stress responses, and distinguishes
            mammalian TIM from the circadian-specific paralogs.
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Yoshizawa-Sugata,N. and Masai,H.
  TITLE     Human Tim/Timeless-interacting protein, Tipin, is required for
            efficient progression of S phase and DNA replication checkpoint
  JOURNAL   J Biol Chem 282 (4), 2729-2740 (2007)
   PUBMED   17102137
  REMARK    GeneRIF: Tipin is a checkpoint mediator that cooperates with Tim
            and may regulate the nuclear relocation of Claspin in response to
            replication checkpoint
REFERENCE   8  (residues 1 to 301)
  AUTHORS   Chou,D.M. and Elledge,S.J.
  TITLE     Tipin and Timeless form a mutually protective complex required for
            genotoxic stress resistance and checkpoint function
  JOURNAL   Proc Natl Acad Sci U S A 103 (48), 18143-18147 (2006)
   PUBMED   17116885
  REMARK    GeneRIF: observation explains the similar checkpoint phenotypes
            observed in both Tipin- and Timeless-depleted cells
REFERENCE   9  (residues 1 to 301)
  AUTHORS   Gotter,A.L.
  TITLE     Tipin, a novel timeless-interacting protein, is developmentally
            co-expressed with timeless and disrupts its self-association
  JOURNAL   J Mol Biol 331 (1), 167-176 (2003)
   PUBMED   12875843
REFERENCE   10 (residues 1 to 301)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            
            On Dec 14, 2021 this sequence version replaced XP_011520045.1.
            
            Summary: The protein encoded by this gene is part of the replisome
            complex, a group of proteins that support DNA replication. It binds
            TIM, which is involved in circadian rhythm regulation, and aids in
            protecting cells against DNA damage and stress. Two pseudogenes and
            two transcript variants encoding different isoforms have been found
            for this gene. [provided by RefSeq, Jul 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.98540.1,
                                           SRR14038191.1835401.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..301
                     /product="TIMELESS-interacting protein isoform 1"
                     /note="timeless-interacting protein; CSM3 homolog"
                     /calculated_mol_wt=34424
     Region          1..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Region          66..148
                     /region_name="Swi3"
                     /note="Replication Fork Protection Component Swi3;
                     pfam07962"
                     /db_xref="CDD:462324"
     Region          67..143
                     /region_name="Interaction with TIMELESS.
                     /evidence=ECO:0000269|PubMed:23359676"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Region          240..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVW5.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BVW5.2)"
     CDS             1..301
                     /gene="TIPIN"
                     /coded_by="NM_001398282.1:552..1457"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS10215.1"
                     /db_xref="GeneID:54962"
                     /db_xref="HGNC:HGNC:30750"
                     /db_xref="MIM:610716"
ORIGIN      
        1 mlepqengvi dlpdyehved etfppfpppa sperqdgegt epdeesgnga pvrvppkrtv
       61 krnipkldaq rliserglpa lrhvfdkakf kgkgheaedl kmlirhmehw ahrlfpklqf
      121 edfidrveyl gskkevqtcl krirldlpil hedfvsnnde vaennehdvt steldpfltn
      181 lsesemfase lsrslteeqq qriernkqla lerrqaklls nsqtlgndml mntprahtve
      241 evntdedqke esnglnedil dnpcndaian tlneeetlld qsfknvqqql datsrnitea
      301 r
//
LOCUS       NP_001340438             715 aa            linear   PRI 21-NOV-2025
DEFINITION  integrator complex subunit 10 isoform e [Homo sapiens].
ACCESSION   NP_001340438
VERSION     NP_001340438.1
DBSOURCE    REFSEQ: accession NM_001353509.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Lin,M.H., Jensen,M.K., Elrod,N.D., Chu,H.F., Haseley,M., Beam,A.C.,
            Huang,K.L., Chiang,W., Russell,W.K., Williams,K., Proschel,C.,
            Wagner,E.J. and Tong,L.
  TITLE     Cytoplasmic binding partners of the Integrator endonuclease INTS11
            and its paralog CPSF73 are required for their nuclear function
  JOURNAL   Mol Cell 84 (15), 2900-2917 (2024)
   PUBMED   39032490
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Razew,M., Fraudeau,A., Pfleiderer,M.M., Linares,R. and Galej,W.P.
  TITLE     Structural basis of the Integrator complex assembly and association
            with transcription factors
  JOURNAL   Mol Cell 84 (13), 2542-2552 (2024)
   PUBMED   38823386
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Fianu,I., Ochmann,M., Walshe,J.L., Dybkov,O., Cruz,J.N., Urlaub,H.
            and Cramer,P.
  TITLE     Structural basis of Integrator-dependent RNA polymerase II
            termination
  JOURNAL   Nature 629 (8010), 219-227 (2024)
   PUBMED   38570683
REFERENCE   4  (residues 1 to 715)
  AUTHORS   Offley,S.R., Pfleiderer,M.M., Zucco,A., Fraudeau,A., Welsh,S.A.,
            Razew,M., Galej,W.P. and Gardini,A.
  TITLE     A combinatorial approach to uncover an additional Integrator
            subunit
  JOURNAL   Cell Rep 42 (3), 112244 (2023)
   PUBMED   36920904
REFERENCE   5  (residues 1 to 715)
  AUTHORS   Wu,Y., Lin,Z., Luo,M., Yu,X., Chen,S. and Liu,L.
  TITLE     Effects of genetic polymorphisms in INTS10 and their interaction
            with environmental factors on progression from persistent HBV
            infection to hepatocellular carcinoma
  JOURNAL   Mol Carcinog 60 (9), 620-626 (2021)
   PUBMED   34133796
  REMARK    GeneRIF: Effects of genetic polymorphisms in INTS10 and their
            interaction with environmental factors on progression from
            persistent HBV infection to hepatocellular carcinoma.
REFERENCE   6  (residues 1 to 715)
  AUTHORS   Weissglas-Volkov,D., Aguilar-Salinas,C.A., Nikkola,E., Deere,K.A.,
            Cruz-Bautista,I., Arellano-Campos,O., Munoz-Hernandez,L.L.,
            Gomez-Munguia,L., Ordonez-Sanchez,M.L., Reddy,P.M., Lusis,A.J.,
            Matikainen,N., Taskinen,M.R., Riba,L., Cantor,R.M.,
            Sinsheimer,J.S., Tusie-Luna,T. and Pajukanta,P.
  TITLE     Genomic study in Mexicans identifies a new locus for triglycerides
            and refines European lipid loci
  JOURNAL   J Med Genet 50 (5), 298-308 (2013)
   PUBMED   23505323
REFERENCE   7  (residues 1 to 715)
  AUTHORS   Ellinghaus,E., Stanulla,M., Richter,G., Ellinghaus,D., te
            Kronnie,G., Cario,G., Cazzaniga,G., Horstmann,M., Panzer
            Grumayer,R., Cave,H., Trka,J., Cinek,O., Teigler-Schlegel,A.,
            ElSharawy,A., Hasler,R., Nebel,A., Meissner,B., Bartram,T.,
            Lescai,F., Franceschi,C., Giordan,M., Nurnberg,P., Heinzow,B.,
            Zimmermann,M., Schreiber,S., Schrappe,M. and Franke,A.
  TITLE     Identification of germline susceptibility loci in
            ETV6-RUNX1-rearranged childhood acute lymphoblastic leukemia
  JOURNAL   Leukemia 26 (5), 902-909 (2012)
   PUBMED   22076464
REFERENCE   8  (residues 1 to 715)
  AUTHORS   Kooner,J.S., Chambers,J.C., Aguilar-Salinas,C.A., Hinds,D.A.,
            Hyde,C.L., Warnes,G.R., Gomez Perez,F.J., Frazer,K.A., Elliott,P.,
            Scott,J., Milos,P.M., Cox,D.R. and Thompson,J.F.
  TITLE     Genome-wide scan identifies variation in MLXIPL associated with
            plasma triglycerides
  JOURNAL   Nat Genet 40 (2), 149-151 (2008)
   PUBMED   18193046
REFERENCE   9  (residues 1 to 715)
  AUTHORS   Baillat,D., Hakimi,M.A., Naar,A.M., Shilatifard,A., Cooch,N. and
            Shiekhattar,R.
  TITLE     Integrator, a multiprotein mediator of small nuclear RNA
            processing, associates with the C-terminal repeat of RNA polymerase
            II
  JOURNAL   Cell 123 (2), 265-276 (2005)
   PUBMED   16239144
REFERENCE   10 (residues 1 to 715)
  AUTHORS   Yuryev,A. and Wennogle,L.P.
  TITLE     Novel raf kinase protein-protein interactions found by an
            exhaustive yeast two-hybrid analysis
  JOURNAL   Genomics 81 (2), 112-125 (2003)
   PUBMED   12620389
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC107964.4.
            
            Summary: INTS10 is a subunit of the Integrator complex, which
            associates with the C-terminal domain of RNA polymerase II large
            subunit (POLR2A; MIM 180660) and mediates 3-prime end processing of
            small nuclear RNAs U1 (RNU1; MIM 180680) and U2 (RNU2; MIM 180690)
            (Baillat et al., 2005 [PubMed 16239144]).[supplied by OMIM, Mar
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.75701.1,
                                           SRR1660809.82905.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..715
                     /product="integrator complex subunit 10 isoform e"
                     /calculated_mol_wt=82375
     CDS             1..715
                     /gene="INTS10"
                     /gene_synonym="C8orf35; INT10"
                     /coded_by="NM_001353509.2:123..2270"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="GeneID:55174"
                     /db_xref="HGNC:HGNC:25548"
                     /db_xref="MIM:611353"
ORIGIN      
        1 msaqgdcefl vqrarelvpq dlwaakawli tarslypadf niqyemytie rnaertatag
       61 rllydmfvnf pdqpvvwrei siitsalrnd sqdkqtqflr slfetlpgrv qcemllkvte
      121 qcfntlerse mlllllrrfp etvvqhgvgl gealleaeti eeqespvncf rklfvcdvlp
      181 liinnhdvrl panllykyln kaaefyinyv trstqienqh qgaqdtsdlm spskrssqky
      241 iiegltekss qivdpwersy gdilhrmkdl crymnnfdse ahakyknqvv ystmlvffkn
      301 afqyvnsiqp slfqgpnaps qvplvlledv snvygdveid rnkhihkkrk laegrektms
      361 sddedcsakg rnrhivvnka elanstevle sfklareswe llyslefldk eftriclawk
      421 tdtwlwlrif ltdmiiyqgq ykkaiaslhh laalqgsisq pqitgqgtle hqraliqlat
      481 chfalgeyrm tcekvldlmc ymvlpiqdgg ksqeepskvk pkfrkgsdlk llpctskaim
      541 pyclhlmlac fklraftdnr ddmalghviv llqqewprge nlflkavnki cqqgnfqyen
      601 ffnyvtnidm leefaylrtq eggkihlell pnqgmlikps sppmgllqqe flpvlqpsiq
      661 tadrhhtvtr gitkgvkedf rlamerqvsr cgenlmvvlh rfcinekill lqtlt
//
LOCUS       NP_004750                370 aa            linear   PRI 21-NOV-2025
DEFINITION  MAP kinase-activated protein kinase 2 isoform 1 [Homo sapiens].
ACCESSION   NP_004750
VERSION     NP_004750.1
DBSOURCE    REFSEQ: accession NM_004759.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Morgan,D., Berggren,K.L., Spiess,C.D., Smith,H.M., Tejwani,A.,
            Weir,S.J., Lominska,C.E., Thomas,S.M. and Gan,G.N.
  TITLE     Mitogen-activated protein kinase-activated protein kinase-2 (MK2)
            and its role in cell survival, inflammatory signaling, and
            migration in promoting cancer
  JOURNAL   Mol Carcinog 61 (2), 173-199 (2022)
   PUBMED   34559922
  REMARK    GeneRIF: Mitogen-activated protein kinase-activated protein
            kinase-2 (MK2) and its role in cell survival, inflammatory
            signaling, and migration in promoting cancer.
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Suzuki,T., Hoshina,M., Nishijima,S., Hoshina,N., Kikuguchi,C.,
            Tomohiro,T., Fukao,A., Fujiwara,T. and Yamamoto,T.
  TITLE     Regulation of CCR4-NOT complex deadenylase activity and cellular
            responses by MK2-dependent phosphorylation of CNOT2
  JOURNAL   RNA Biol 19 (1), 234-246 (2022)
   PUBMED   35129087
  REMARK    GeneRIF: Regulation of CCR4-NOT complex deadenylase activity and
            cellular responses by MK2-dependent phosphorylation of CNOT2.
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Gutierrez-Prat,N., Cubillos-Rojas,M., Canovas,B., Kuzmanic,A.,
            Gupta,J., Igea,A., Llonch,E., Gaestel,M. and Nebreda,A.R.
  TITLE     MK2 degradation as a sensor of signal intensity that controls
            stress-induced cell fate
  JOURNAL   Proc Natl Acad Sci U S A 118 (29) (2021)
   PUBMED   34272277
  REMARK    GeneRIF: MK2 degradation as a sensor of signal intensity that
            controls stress-induced cell fate.
REFERENCE   6  (residues 1 to 370)
  AUTHORS   Engel,K., Schultz,H., Martin,F., Kotlyarov,A., Plath,K., Hahn,M.,
            Heinemann,U. and Gaestel,M.
  TITLE     Constitutive activation of mitogen-activated protein
            kinase-activated protein kinase 2 by mutation of phosphorylation
            sites and an A-helix motif
  JOURNAL   J Biol Chem 270 (45), 27213-27221 (1995)
   PUBMED   7592979
REFERENCE   7  (residues 1 to 370)
  AUTHORS   Lavoie,J.N., Lambert,H., Hickey,E., Weber,L.A. and Landry,J.
  TITLE     Modulation of cellular thermoresistance and actin filament
            stability accompanies phosphorylation-induced changes in the
            oligomeric structure of heat shock protein 27
  JOURNAL   Mol Cell Biol 15 (1), 505-516 (1995)
   PUBMED   7799959
REFERENCE   8  (residues 1 to 370)
  AUTHORS   Stokoe,D., Engel,K., Campbell,D.G., Cohen,P. and Gaestel,M.
  TITLE     Identification of MAPKAP kinase 2 as a major enzyme responsible for
            the phosphorylation of the small mammalian heat shock proteins
  JOURNAL   FEBS Lett 313 (3), 307-313 (1992)
   PUBMED   1332886
REFERENCE   9  (residues 1 to 370)
  AUTHORS   Sharp,N.
  TITLE     No more money for nursing education?
  JOURNAL   Nurs Manage 21 (9), 24-25 (1990)
   PUBMED   2402373
REFERENCE   10 (residues 1 to 370)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL591846.15, BC036060.1,
            BC052584.1 and BU621009.1.
            
            Summary: This gene encodes a member of the Ser/Thr protein kinase
            family. This kinase is regulated through direct phosphorylation by
            p38 MAP kinase. In conjunction with p38 MAP kinase, this kinase is
            known to be involved in many cellular processes including stress
            and inflammatory responses, nuclear export, gene expression
            regulation and cell proliferation. Heat shock protein HSP27 was
            shown to be one of the substrates of this kinase in vivo. Two
            transcript variants encoding two different isoforms have been found
            for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript but encodes the shorter isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2812422.1,
                                           SRR14038196.2616692.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..370
                     /product="MAP kinase-activated protein kinase 2 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="MAP kinase-activated protein kinase 2; MAPKAP
                     kinase 2; mitogen-activated protein kinase-activated
                     protein kinase 2"
                     /calculated_mol_wt=42072
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49137.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8846784; propagated from
                     UniProtKB/Swiss-Prot (P49137.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:8846784; propagated from
                     UniProtKB/Swiss-Prot (P49137.1)"
     Region          61..353
                     /region_name="STKc_MAPKAPK2"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Mitogen-activated protein kinase-activated protein kinase
                     2; cd14170"
                     /db_xref="CDD:271072"
     Site            order(70..75,78,91,93,118,138..141,145,147,185..186,188,
                     190..191,193,206..207,210,224..228,230)
                     /site_type="active"
                     /db_xref="CDD:271072"
     Site            order(70..75,78,91,93,118,138..141,191,193,206..207)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271072"
     Site            order(72..75,77,227..231,235,237,240,261,263..266,
                     280..281,283..284,308..309,347..348,350..352)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:271072"
     Site            order(74,145,147,185..186,188,190,210,224..228,230)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271072"
     Site            206..228
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271072"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK14.
                     /evidence=ECO:0000269|PubMed:8846784; propagated from
                     UniProtKB/Swiss-Prot (P49137.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14.
                     /evidence=ECO:0000269|PubMed:8846784; propagated from
                     UniProtKB/Swiss-Prot (P49137.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P49137.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK14.
                     /evidence=ECO:0000269|PubMed:8846784,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P49137.1)"
     CDS             1..370
                     /gene="MAPKAPK2"
                     /gene_synonym="MAPKAP-K2; MK-2; MK2"
                     /coded_by="NM_004759.5:326..1438"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1466.1"
                     /db_xref="GeneID:9261"
                     /db_xref="HGNC:HGNC:6887"
                     /db_xref="MIM:602006"
ORIGIN      
        1 mlsnsqgqsp pvpfpapapp pqpptpalph ppaqpppppp qqfpqfhvks glqikknaii
       61 ddykvtsqvl glgingkvlq ifnkrtqekf alkmlqdcpk arrevelhwr asqcphivri
      121 vdvyenlyag rkcllivmec ldggelfsri qdrgdqafte reaseimksi geaiqylhsi
      181 niahrdvkpe nllytskrpn ailkltdfgf akettshnsl ttpcytpyyv apevlgpeky
      241 dkscdmwslg vimyillcgy ppfysnhgla ispgmktrir mgqyefpnpe wsevseevkm
      301 lirnllktep tqrmtitefm nhpwimqstk vpqtplhtsr vlkedkerwe dvkgclhdkn
      361 sdqatwltrl
//
LOCUS       NP_001358900             924 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase I subunit RPA2 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001358900
VERSION     NP_001358900.1
DBSOURCE    REFSEQ: accession NM_001371971.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Ford,B.L., Wei,T., Liu,H., Scull,C.E., Najmi,S.M., Pitts,S.,
            Fan,W., Schneider,D.A. and Laiho,M.
  TITLE     Expression of RNA polymerase I catalytic core is influenced by
            RPA12
  JOURNAL   PLoS One 18 (5), e0285660 (2023)
   PUBMED   37167337
  REMARK    GeneRIF: Expression of RNA polymerase I catalytic core is
            influenced by RPA12.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 924)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 924)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   5  (residues 1 to 924)
  AUTHORS   Zhao,D., Liu,W., Chen,K., Wu,Z., Yang,H. and Xu,Y.
  TITLE     Structure of the human RNA polymerase I elongation complex
  JOURNAL   Cell Discov 7 (1), 97 (2021)
   PUBMED   34671025
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 924)
  AUTHORS   Miller,G., Panov,K.I., Friedrich,J.K., Trinkle-Mulcahy,L.,
            Lamond,A.I. and Zomerdijk,J.C.
  TITLE     hRRN3 is essential in the SL1-mediated recruitment of RNA
            Polymerase I to rRNA gene promoters
  JOURNAL   EMBO J 20 (6), 1373-1382 (2001)
   PUBMED   11250903
REFERENCE   7  (residues 1 to 924)
  AUTHORS   Jansa,P., Mason,S.W., Hoffmann-Rohrer,U. and Grummt,I.
  TITLE     Cloning and functional characterization of PTRF, a novel protein
            which induces dissociation of paused ternary transcription
            complexes
  JOURNAL   EMBO J 17 (10), 2855-2864 (1998)
   PUBMED   9582279
REFERENCE   8  (residues 1 to 924)
  AUTHORS   Seither,P., Zatsepina,O., Hoffmann,M. and Grummt,I.
  TITLE     Constitutive and strong association of PAF53 with RNA polymerase I
  JOURNAL   Chromosoma 106 (4), 216-225 (1997)
   PUBMED   9254723
REFERENCE   9  (residues 1 to 924)
  AUTHORS   Seither,P. and Grummt,I.
  TITLE     Molecular cloning of RPA2, the gene encoding the second largest
            subunit of mouse RNA polymerase I
  JOURNAL   Genomics 37 (1), 135-139 (1996)
   PUBMED   8921381
REFERENCE   10 (residues 1 to 924)
  AUTHORS   Barbosa,M., Jabs,E.W. and Huston,S.
  TITLE     Treacher Collins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301704
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012442.7.
            
            Summary: Eukaryotic RNA polymerase I (pol I) is responsible for the
            transcription of ribosomal RNA (rRNA) genes and production of rRNA,
            the primary component of ribosomes. Pol I is a multisubunit enzyme
            composed of 6 to 14 polypeptides, depending on the species. Most of
            the mass of the pol I complex derives from the 2 largest subunits,
            Rpa1 and Rpa2 in yeast. POLR1B is homologous to Rpa2 (Seither and
            Grummt, 1996 [PubMed 8921381]).[supplied by OMIM, Mar 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2067804.1,
                                           SRR11853564.15940.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.1"
     Protein         1..924
                     /product="DNA-directed RNA polymerase I subunit RPA2
                     isoform 5"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerase I subunit RPA2;
                     DNA-directed RNA polymerase I 135kDa polypeptide; RNA
                     polymerase I subunit 2; DNA-directed RNA polymerase I 135
                     kDa polypeptide; polymerase (RNA) I polypeptide B, 128kDa;
                     polymerase (RNA) I subunit B"
                     /calculated_mol_wt=104369
     Region          <9..205
                     /region_name="RNA_pol_Rpb2_1"
                     /note="RNA polymerase beta subunit; pfam04563"
                     /db_xref="CDD:367994"
     Region          <130..922
                     /region_name="RNA_pol_B_RPB2"
                     /note="RNA polymerase beta subunit. RNA polymerases
                     catalyse the DNA dependent polymerization of RNA.
                     Prokaryotes contain a single RNA polymerase compared to
                     three in eukaryotes (not including mitochondrial. and
                     chloroplast polymerases). Each RNA polymerase...; cd00653"
                     /db_xref="CDD:238353"
     Site            order(274,276..278,280,283,288,449,467..469,471,534..537,
                     540,542..544,679,681,683,705,707,710,713,718,722,739,770,
                     778..780,782,795,798..800,802..803,824..826,830,832..833,
                     835,837..842,844..849,853,902,906,908,910..911,913,
                     915..918,920,922)
                     /site_type="other"
                     /note="RPB1 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     Region          352..410
                     /region_name="RNA_pol_Rpa2_4"
                     /note="RNA polymerase I, Rpa2 specific domain; pfam06883"
                     /db_xref="CDD:462028"
     Site            order(507..508,529,531,552,555,688,701,728..729,731,766,
                     783)
                     /site_type="other"
                     /note="RPB10 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     Site            order(540,554,687,772)
                     /site_type="other"
                     /note="RPB11 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     Site            order(554..555,559,661,663,688..690,693,695..696,771..778,
                     780)
                     /site_type="other"
                     /note="RPB3 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     Site            order(559,597,599,603..605,607)
                     /site_type="other"
                     /note="RPB12 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     CDS             1..924
                     /gene="POLR1B"
                     /gene_synonym="A135; RPA135; RPA2; Rpo1-2; TCS4"
                     /coded_by="NM_001371971.1:531..3305"
                     /note="isoform 5 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS62990.1"
                     /db_xref="GeneID:84172"
                     /db_xref="HGNC:HGNC:20454"
                     /db_xref="MIM:602000"
ORIGIN      
        1 mhcvreehsa vnmnlhylen gtvmlnfiyr kelfflplgf alkalvsfsd yqifqelikg
       61 keddsflrns vsqmlrivme egcstqkqvl nylgecfrvk lnvpdwypne qaaeflfnqc
      121 icihlksnte kfymlclmtr klfalakgec mednpdslvn qevltpgqlf lmflkekleg
      181 wlvsikiafd kkaqktsvsm ntdnlmrift mgidltkpfe ylfatgnlrs ktglgllqds
      241 glcvvadkln firylshfrc vhrgadfakm rtttvrrllp eswgflcpvh tpdgepcglm
      301 nhltavcevv tqfvytasip allcnlgvtp idgaphrsys ecypvlldgv mvgwvdkdla
      361 pgiadslrhf kvlrekripp wmevvlipmt gkpslypglf lfttpcrlvr pvqnlalgke
      421 eligtmeqif mnvaifedev fagvtthqel fphsllsvia nfipfsdhnq sprnmyqcqm
      481 gkqtmgfpll tyqdrsdnkl yrlqtpqspl vrpsmydyyd mdnypigtna ivavisytgy
      541 dmedamivnk aswergfahg svyksefidl sekikqgdss lvfgikpgdp rvlqkldddg
      601 lpfigaklqy gdpyysylnl ntgesfvmyy kskencvvdn ikvcsndtgs gkfkcvcitm
      661 rvprnptigd kfasrhgqkg ilsrlwpaed mpftesgmvp dilfnphgfp srmtigmlie
      721 smagksaalh glchdatpfi fseensaley fgemlkaagy nfygterlys gisglelead
      781 ifigvvyyqr lrhmvsdkfq vrttgardrv tnqpiggrnv qggirfgeme rdallahgts
      841 fllhdrlfnc sdrsvahvcv kcgsllspll ekpppswsam rnrkynctlc srsdtidtvs
      901 vpyvfryfva elaamnikvk ldvv
//
LOCUS       NP_001245147             205 aa            linear   PRI 21-NOV-2025
DEFINITION  protein MIS12 homolog [Homo sapiens].
ACCESSION   NP_001245147
VERSION     NP_001245147.1
DBSOURCE    REFSEQ: accession NM_001258218.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Wu,Z., Shi,Y., Lu,M., Song,M., Yu,Z., Wang,J., Wang,S., Ren,J.,
            Yang,Y.G., Liu,G.H., Zhang,W., Ci,W. and Qu,J.
  TITLE     METTL3 counteracts premature aging via m6A-dependent stabilization
            of MIS12 mRNA
  JOURNAL   Nucleic Acids Res 48 (19), 11083-11096 (2020)
   PUBMED   33035345
  REMARK    GeneRIF: METTL3 counteracts premature aging via m6A-dependent
            stabilization of MIS12 mRNA.
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Kline,S.L., Cheeseman,I.M., Hori,T., Fukagawa,T. and Desai,A.
  TITLE     The human Mis12 complex is required for kinetochore assembly and
            proper chromosome segregation
  JOURNAL   J Cell Biol 173 (1), 9-17 (2006)
   PUBMED   16585270
  REMARK    GeneRIF: These results indicate that a four-subunit Mis12 complex
            plays an essential role in chromosome segregation in vertebrates
            and contributes to mitotic kinetochore assembly.
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Obuse,C., Iwasaki,O., Kiyomitsu,T., Goshima,G., Toyoda,Y. and
            Yanagida,M.
  TITLE     A conserved Mis12 centromere complex is linked to heterochromatic
            HP1 and outer kinetochore protein Zwint-1
  JOURNAL   Nat Cell Biol 6 (11), 1135-1141 (2004)
   PUBMED   15502821
REFERENCE   8  (residues 1 to 205)
  AUTHORS   Cheeseman,I.M., Niessen,S., Anderson,S., Hyndman,F., Yates,J.R.
            3rd, Oegema,K. and Desai,A.
  TITLE     A conserved protein network controls assembly of the outer
            kinetochore and its ability to sustain tension
  JOURNAL   Genes Dev 18 (18), 2255-2268 (2004)
   PUBMED   15371340
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Goshima,G., Kiyomitsu,T., Yoda,K. and Yanagida,M.
  TITLE     Human centromere chromatin protein hMis12, essential for equal
            segregation, is independent of CENP-A loading pathway
  JOURNAL   J Cell Biol 160 (1), 25-39 (2003)
   PUBMED   12515822
  REMARK    GeneRIF: hMIS12 has a role in mitosis and localizes at kinetochores
REFERENCE   10 (residues 1 to 205)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK056072.1 and AL136906.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. Variants 1-5 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000229.1, AK056072.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..205
                     /product="protein MIS12 homolog"
                     /note="homolog of yeast Mis12; MIS12 homolog; MIS12, MIND
                     kinetochore complex component, homolog"
                     /calculated_mol_wt=24009
     Region          8..140
                     /region_name="Mis12"
                     /note="Mis12 protein; pfam05859"
                     /db_xref="CDD:461761"
     CDS             1..205
                     /gene="MIS12"
                     /gene_synonym="2510025F08Rik; hMis12; KNTC2AP; MTW1"
                     /coded_by="NM_001258218.2:160..777"
                     /db_xref="CCDS:CCDS11074.1"
                     /db_xref="GeneID:79003"
                     /db_xref="HGNC:HGNC:24967"
                     /db_xref="MIM:609178"
ORIGIN      
        1 msvdpmtyea qffgftpqtc mlriyiafqd ylfevmqave qvilkkldgi pdcdispvqi
       61 rkctekflcf mkghfdnlfs kmeqlflqli lripsnillp edkcketpys eedfqhlqke
      121 ieqlqekykt elctkqalla eleeqkivqa klkqtltffd elhnvgrdhg tsdfreslvs
      181 lvqnsrklqn irdnvekesk rlkis
//
LOCUS       NP_001372790            2455 aa            linear   PRI 21-NOV-2025
DEFINITION  protein DOP1A isoform c [Homo sapiens].
ACCESSION   NP_001372790 XP_024302143
VERSION     NP_001372790.1
DBSOURCE    REFSEQ: accession NM_001385861.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2455)
  AUTHORS   Mahajan,D., Tie,H.C., Chen,B. and Lu,L.
  TITLE     Dopey1-Mon2 complex binds to dual-lipids and recruits kinesin-1 for
            membrane trafficking
  JOURNAL   Nat Commun 10 (1), 3218 (2019)
   PUBMED   31324769
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2455)
  AUTHORS   Lend,A.K., Kazantseva,A., Kivil,A., Valvere,V. and Palm,K.
  TITLE     Diagnostic significance of alternative splice variants of REST and
            DOPEY1 in the peripheral blood of patients with breast cancer
  JOURNAL   Tumour Biol 36 (4), 2473-2480 (2015)
   PUBMED   25424701
  REMARK    GeneRIF: Assessment of REST-N50 and DOPEY1v2 may prove useful in
            diagnostic blood tests of breast cancer. REST-N50 shows a high
            potential as a blood biomarker for evaluating the effectiveness of
            therapy in the neoadjuvant setting.
REFERENCE   3  (residues 1 to 2455)
  AUTHORS   Gillingham,A.K., Whyte,J.R., Panic,B. and Munro,S.
  TITLE     Mon2, a relative of large Arf exchange factors, recruits Dop1 to
            the Golgi apparatus
  JOURNAL   J Biol Chem 281 (4), 2273-2280 (2006)
   PUBMED   16301316
REFERENCE   4  (residues 1 to 2455)
  AUTHORS   Pascon,R.C. and Miller,B.L.
  TITLE     Morphogenesis in Aspergillus nidulans requires Dopey (DopA), a
            member of a novel family of leucine zipper-like proteins conserved
            from yeast to humans
  JOURNAL   Mol Microbiol 36 (6), 1250-1264 (2000)
   PUBMED   10931277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL139333.10 and AL121716.16.
            
            On Jul 29, 2020 this sequence version replaced XP_024302143.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2953885.1,
                                           SRR18074967.1978032.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2455
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..2455
                     /product="protein DOP1A isoform c"
                     /note="homolog of yeast DOP1; protein dopey-1; dopey
                     family member 1; protein DOP1A"
                     /calculated_mol_wt=276052
     Region          11..294
                     /region_name="Dopey_N"
                     /note="Dopey, N-terminal; pfam04118"
                     /db_xref="CDD:461183"
     Region          549..590
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWR5.1)"
     Region          615..636
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWR5.1)"
     Region          695..723
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWR5.1)"
     Site            1256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BL99; propagated from
                     UniProtKB/Swiss-Prot (Q5JWR5.1)"
     Region          1272..1305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWR5.1)"
     Region          <2081..2317
                     /region_name="Dopey_N"
                     /note="Dopey, N-terminal; cl04407"
                     /db_xref="CDD:471021"
     CDS             1..2455
                     /gene="DOP1A"
                     /gene_synonym="dJ202D23.2; DOP1; DOPEY1; KIAA1117"
                     /coded_by="NM_001385861.1:163..7530"
                     /note="isoform c is encoded by transcript variant 8"
                     /db_xref="GeneID:23033"
                     /db_xref="HGNC:HGNC:21194"
                     /db_xref="MIM:616823"
ORIGIN      
        1 mnteelells dskyrnyvaa idkalknfey ssewadlisa lgklnkvlqn nakyqvvpkk
       61 ltigkrlaqc lhpalpggvh rkaletyeii fkiigpkrla kdlflyssgl fpllanaams
      121 vkptllslye iyylplgktl kpglqglltg ilpgleegse yyertnmlle kvaaavdqsa
      181 fysalwgsll tspavrlpgi tyvlahlnrk lsmedqlyii gsdielmvea vstsvqdssv
      241 lvqrstldli lfcfpfhmsq atrpdmiril saalhvvlrr dmslnrrlya wllgfdnnga
      301 iigprstrhs npeehatyyf ttfskellvq amvgilqvng fgeentlmqd lkpfrilisl
      361 ldkpelgpvi ledvlievfr tlysqckael dlqteppfsk dhaqlssklr enkktaelik
      421 tanllfnsfe pyymwdyvar wfeeccrrtl hvrlqigpgd sndsselqlt nfcllvdfll
      481 divsletyie iqtehlpqll lrmisaltsh lqtlhlselt dslrlcskil skvqppllsa
      541 stggvlqfps gqnnsvkewe dkkvssvshe nptevfedge nppssrsses gftefiqyqa
      601 drtddidrel segqgaaaip igstssetet astvgseeti iqtpsvvtqg tatrsrktaq
      661 ktamqccley vqqfltrlin lyiiqnnsfs qslatehqgd lgreqgetsk wdrnsqgdvk
      721 ekniskqkts keylsaflaa cqlflecssf pvyiaegnht selrseklet dcehvqppqw
      781 lqtlmnacsq asdfsvqsva islvmdlvgl tqsvamvtge ninsvepaqp lspnqgrvav
      841 virppltqgn lryiaektef fkhvaltlwd qlgdgtpqhh qksvelfyql hnlvpsssic
      901 edvisqqlth kdkkirmeah akfavlwhlt rdlhinksss fvrsfdrslf imldslnsld
      961 gstssvgqaw lnqvlqrhdi arvlepllll llhpktqrvs vqrvqaeryw nkspcypgee
     1021 sdkhfmqnfa csnvsqvqli tskgngekpl tmdeienfsl tvnplsdrls llstssetip
     1081 mvvsdfdlpd qqieilqssd sgcsqssagd nlsyevdpet vnaqedsqmp kesspdddvq
     1141 qvvfdlickv vsglevesas vtsqleieam ppkcsdidpd eetikiedds iqqsqnalls
     1201 nessqflsvs aegghecvan gisrnssspc isgtthtlhd ssvasietks rqrshssiqf
     1261 sfkeklsekv seketivkes gkqpgakpkv klarkkdddk kkssneklkq tsvffsdgld
     1321 lenwyscgeg diseiesdmg spgsrkspnf nihplyqhvl lylqlydssr tlyafsaika
     1381 ilktnpiafv naisttsvnn aytpqlsllq nllarhrisv mgkdfyship vdsnhnfrss
     1441 myieilislc lyymrshypt hvkvtaqdli gnrnmqmmsi eiltllftel akviessakg
     1501 fpsfisdmls kckvqkvilh cllssifsaq kwhsekmagk nlvaveegfs edslinfsed
     1561 efdngstlqs qllkvlqrli vlehrvmtip eenetgfdfv vsdlehisph qpmtslqylh
     1621 aqpitcqgmf lcaviralhq hcackmhpqw iglitstlpy mgkvlqrvvv svtlqlcrnl
     1681 dnliqqykye tglsdsrplw masiippdmi ltllegitai ihyclldptt qyhqllvsvd
     1741 qkhlfearsg ilsilhmims svtllwsilh qadssekmti aasaslttin lgatknlrqq
     1801 ilellgpism nhgvhfmaai afvwnerrqn ktttrtkvip aaseeqlllv elvrsisvmr
     1861 aetviqtvke vlkqppaiak dkkhlslevc mlqffyayiq ripvpnlvds wasllillkd
     1921 siqlslpapg qflilgvlne fimknpslen kkdqrdlqdv thkivdaiga iagssleqtt
     1981 wlrrnlevkp spkimvdgtn lesdvedmls pametanitp svysvhaltl lsevlahlld
     2041 mvfysdeker vipllvnimh yvvpylrnhs ahnapsyrac vqllsslsgy qytrrawkke
     2101 afdlfmdpsf fqmdascvnh wraimdnlmt hdkttfrdlm trvavaqsss lnlfanrdve
     2161 leqramllkr lafaifssei dqyqkylpdi qerlveslrl pqvptlhsqv flffrvlllr
     2221 mspqhltslw ptmitelvqv fllmeqelta dedisrtsgp svaglettyt ggngfstsyn
     2281 sqrwlnlyls ackfldlala lpsenlpqfq myrwafipea sddsglevrr qgihqrefkp
     2341 yvvrlakllr krakknpeed nsgrtlgwep ghllltictv rsmeqllpff nvlsqvfnsk
     2401 vtsrcgghsg spilysnafp nkdmklenhk pcsskarqki eemvekdfle gmikt
//
LOCUS       NP_001350902             159 aa            linear   PRI 21-NOV-2025
DEFINITION  calaxin isoform b [Homo sapiens].
ACCESSION   NP_001350902 XP_016869315
VERSION     NP_001350902.1
DBSOURCE    REFSEQ: accession NM_001363973.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hjeij,R., Aprea,I., Poeta,M., Nothe-Menchen,T., Bracht,D.,
            Raidt,J., Honecker,B.I., Dougherty,G.W., Olbrich,H., Schwartz,O.,
            Keller,U., Nusse,H., Diderich,K.E.M., Vogelberg,C., Santamaria,F.
            and Omran,H.
  TITLE     Pathogenic variants in CLXN encoding the outer dynein arm
            docking-associated calcium-binding protein calaxin cause primary
            ciliary dyskinesia
  JOURNAL   Genet Med 25 (5), 100798 (2023)
   PUBMED   36727596
  REMARK    GeneRIF: Pathogenic variants in CLXN encoding the outer dynein arm
            docking-associated calcium-binding protein calaxin cause primary
            ciliary dyskinesia.
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Braschi,B., Omran,H., Witman,G.B., Pazour,G.J., Pfister,K.K.,
            Bruford,E.A. and King,S.M.
  TITLE     Consensus nomenclature for dyneins and associated assembly factors
  JOURNAL   J Cell Biol 221 (2) (2022)
   PUBMED   35006274
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Gui,M., Farley,H., Anujan,P., Anderson,J.R., Maxwell,D.W.,
            Whitchurch,J.B., Botsch,J.J., Qiu,T., Meleppattu,S., Singh,S.K.,
            Zhang,Q., Thompson,J., Lucas,J.S., Bingle,C.D., Norris,D.P., Roy,S.
            and Brown,A.
  TITLE     De novo identification of mammalian ciliary motility proteins using
            cryo-EM
  JOURNAL   Cell 184 (23), 5791-5806 (2021)
   PUBMED   34715025
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Pineau,C., Hikmet,F., Zhang,C., Oksvold,P., Chen,S., Fagerberg,L.,
            Uhlen,M. and Lindskog,C.
  TITLE     Cell Type-Specific Expression of Testis Elevated Genes Based on
            Transcriptomics and Antibody-Based Proteomics
  JOURNAL   J Proteome Res 18 (12), 4215-4230 (2019)
   PUBMED   31429579
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Sasaki,K., Shiba,K., Nakamura,A., Kawano,N., Satouh,Y.,
            Yamaguchi,H., Morikawa,M., Shibata,D., Yanase,R., Jokura,K.,
            Nomura,M., Miyado,M., Takada,S., Ueno,H., Nonaka,S., Baba,T.,
            Ikawa,M., Kikkawa,M., Miyado,K. and Inaba,K.
  TITLE     Calaxin is required for cilia-driven determination of vertebrate
            laterality
  JOURNAL   Commun Biol 2, 226 (2019)
   PUBMED   31240264
  REMARK    Erratum:[Commun Biol. 2019 Jul 4;2:254. doi:
            10.1038/s42003-019-0512-5. PMID: 31286071]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 159)
  AUTHORS   Aouizerat,B.E., Vittinghoff,E., Musone,S.L., Pawlikowska,L.,
            Kwok,P.Y., Olgin,J.E. and Tseng,Z.H.
  TITLE     GWAS for discovery and replication of genetic loci associated with
            sudden cardiac arrest in patients with coronary artery disease
  JOURNAL   BMC Cardiovasc Disord 11, 29 (2011)
   PUBMED   21658281
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 159)
  AUTHORS   Takeuchi,F., Isono,M., Katsuya,T., Yamamoto,K., Yokota,M.,
            Sugiyama,T., Nabika,T., Fujioka,A., Ohnaka,K., Asano,H., Yamori,Y.,
            Yamaguchi,S., Kobayashi,S., Takayanagi,R., Ogihara,T. and Kato,N.
  TITLE     Blood pressure and hypertension are associated with 7 loci in the
            Japanese population
  JOURNAL   Circulation 121 (21), 2302-2309 (2010)
   PUBMED   20479155
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 159)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB204697.1, DC414358.1, BP376567.1, BC025676.1, CB250588.1 and
            AC022915.14.
            
            On Jun 3, 2018 this sequence version replaced XP_016869315.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.1858871.1,
                                           SRR1803611.68322.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..159
                     /product="calaxin isoform b"
                     /note="EF-hand calcium-binding domain-containing protein
                     1; EF-hand calcium binding domain 1; outer dynein arm
                     docking complex subunit 5"
                     /calculated_mol_wt=18367
     Region          <17..124
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..159
                     /gene="CLXN"
                     /gene_synonym="CILD53; EFCAB1; ODAD5"
                     /coded_by="NM_001363973.3:118..597"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS47853.1"
                     /db_xref="GeneID:79645"
                     /db_xref="HGNC:HGNC:25678"
                     /db_xref="MIM:619564"
ORIGIN      
        1 mnrkklqklt dtltknckhl frgfdkdndg cvnvlewihg lslflrgsle ekmkycfevf
       61 dlngdgfisk eemfhmlkns llkqpseedp degikdlvei tlkkmdhdhd gklsfadyel
      121 avreetllle afgpclpdpk sqmefeaqvf kdpnefndm
//
LOCUS       NP_001107654             460 aa            linear   PRI 21-NOV-2025
DEFINITION  interleukin-1 receptor-associated kinase 4 isoform a [Homo
            sapiens].
ACCESSION   NP_001107654
VERSION     NP_001107654.1
DBSOURCE    REFSEQ: accession NM_001114182.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Fisch,D., Zhang,T., Sun,H., Ma,W., Tan,Y., Gygi,S.P., Higgins,D.E.
            and Kagan,J.C.
  TITLE     Molecular definition of the endogenous Toll-like receptor
            signalling pathways
  JOURNAL   Nature 631 (8021), 635-644 (2024)
   PUBMED   38961291
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Liu,Y., Yuan,J., Zhang,Y., Qin,F., Bai,X., Sun,W., Chen,T., Liu,F.,
            Zheng,Y., Qi,X., Zhao,W., Liu,B. and Gao,C.
  TITLE     OTUD5 promotes the inflammatory immune response by enhancing MyD88
            oligomerization and Myddosome formation
  JOURNAL   Cell Death Differ 31 (6), 753-767 (2024)
   PUBMED   38605168
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Peterson,J., Balogh Sivars,K., Bianco,A. and Roper,K.
  TITLE     Toll-like receptor signalling via IRAK4 affects epithelial
            integrity and tightness through regulation of junctional tension
  JOURNAL   Development 150 (24) (2023)
   PUBMED   37997696
  REMARK    GeneRIF: Toll-like receptor signalling via IRAK4 affects epithelial
            integrity and tightness through regulation of junctional tension.
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Cooray,S., Price-Kuehne,F., Hong,Y., Omoyinmi,E., Burleigh,A.,
            Gilmour,K.C., Ahmad,B., Choi,S., Bahar,M.W., Torpiano,P.,
            Gagunashvili,A., Jensen,B., Bellos,E., Sancho-Shimizu,V.,
            Herberg,J.A., Mankad,K., Kumar,A., Kaliakatsos,M., Worth,A.J.J.,
            Eleftheriou,D., Whittaker,E. and Brogan,P.A.
  TITLE     Neuroinflammation, autoinflammation, splenomegaly and anemia caused
            by bi-allelic mutations in IRAK4
  JOURNAL   Front Immunol 14, 1231749 (2023)
   PUBMED   37744344
  REMARK    GeneRIF: Neuroinflammation, autoinflammation, splenomegaly and
            anemia caused by bi-allelic mutations in IRAK4.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 460)
  AUTHORS   Wang,Z., Liu,J., Sudom,A., Ayres,M., Li,S., Wesche,H., Powers,J.P.
            and Walker,N.P.
  TITLE     Crystal structures of IRAK-4 kinase in complex with inhibitors: a
            serine/threonine kinase with tyrosine as a gatekeeper
  JOURNAL   Structure 14 (12), 1835-1844 (2006)
   PUBMED   17161373
  REMARK    GeneRIF: crystallographic analysis of IRAK-4 kinase in complex with
            inhibitors
REFERENCE   6  (residues 1 to 460)
  AUTHORS   Suzuki,N. and Saito,T.
  TITLE     IRAK-4--a shared NF-kappaB activator in innate and acquired
            immunity
  JOURNAL   Trends Immunol 27 (12), 566-572 (2006)
   PUBMED   17046325
  REMARK    GeneRIF: Although each system seems to possess distinct activation
            mechanisms, interleukin-1 receptor-associated kinase (IRAK)-4 is
            essential for NF-kappaB activation in Toll-like receptor (TLR) and
            T-cell receptor (TCR) signaling pathways.
            Review article
REFERENCE   7  (residues 1 to 460)
  AUTHORS   Burns,K., Clatworthy,J., Martin,L., Martinon,F., Plumpton,C.,
            Maschera,B., Lewis,A., Ray,K., Tschopp,J. and Volpe,F.
  TITLE     Tollip, a new component of the IL-1RI pathway, links IRAK to the
            IL-1 receptor
  JOURNAL   Nat Cell Biol 2 (6), 346-351 (2000)
   PUBMED   10854325
REFERENCE   8  (residues 1 to 460)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   9  (residues 1 to 460)
  AUTHORS   Scherer,D.C., Brockman,J.A., Chen,Z., Maniatis,T. and Ballard,D.W.
  TITLE     Signal-induced degradation of I kappa B alpha requires
            site-specific ubiquitination
  JOURNAL   Proc Natl Acad Sci U S A 92 (24), 11259-11263 (1995)
   PUBMED   7479976
REFERENCE   10 (residues 1 to 460)
  AUTHORS   Siu,G., Strauss,E.C., Lai,E. and Hood,L.E.
  TITLE     Analysis of a human V beta gene subfamily
  JOURNAL   J Exp Med 164 (5), 1600-1614 (1986)
   PUBMED   3772297
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK304583.1, AY340963.1,
            AC093012.9 and AI126481.1.
            
            Summary: This gene encodes a kinase that activates NF-kappaB in
            both the Toll-like receptor (TLR) and T-cell receptor (TCR)
            signaling pathways. The protein is essential for most innate immune
            responses. Mutations in this gene result in IRAK4 deficiency and
            recurrent invasive pneumococcal disease. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). Variants 1, 2, and 13 all encode the same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY340963.1, SRR11853559.7580.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..460
                     /product="interleukin-1 receptor-associated kinase 4
                     isoform a"
                     /EC_number="2.7.11.1"
                     /note="renal carcinoma antigen NY-REN-64"
                     /calculated_mol_wt=51399
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NWZ3.1)"
     Region          9..106
                     /region_name="Death_IRAK4"
                     /note="Death domain of Interleukin-1 Receptor-Associated
                     Kinase 4; cd08793"
                     /db_xref="CDD:260060"
     Site            order(12,14,16..17,20,47..48,52,55..56,59,69,72..73,76,78)
                     /site_type="other"
                     /note="IRAK4-MyD88 interaction site [polypeptide binding]"
                     /db_xref="CDD:260060"
     Site            order(25,28..30,34,37,46,50,54,92..96,98)
                     /site_type="other"
                     /note="IRAK4-IRAK2 interaction site [polypeptide binding]"
                     /db_xref="CDD:260060"
     Site            34
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NWZ3.1)"
     Region          170..457
                     /region_name="STKc_IRAK4"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Interleukin-1 Receptor Associated Kinase 4; cd14158"
                     /db_xref="CDD:271060"
     Site            order(192..196,200,211,213,246,262..265,269,271,311,313,
                     315..316,318,329,332,350..353)
                     /site_type="active"
                     /db_xref="CDD:271060"
     Site            order(192..196,200,211,213,246,262..265,269,311,313,
                     315..316,318,329)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271060"
     Site            order(196,269,271,311,313,315,332,350..353)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271060"
     Site            order(328..340,342..353)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271060"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17312103, ECO:0000269|Ref.32;
                     propagated from UniProtKB/Swiss-Prot (Q9NWZ3.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17161373,
                     ECO:0000269|PubMed:17312103, ECO:0000269|Ref.32;
                     propagated from UniProtKB/Swiss-Prot (Q9NWZ3.1)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17161373,
                     ECO:0000269|PubMed:17312103; propagated from
                     UniProtKB/Swiss-Prot (Q9NWZ3.1)"
     CDS             1..460
                     /gene="IRAK4"
                     /gene_synonym="IMD67; IPD1; IRAK-4; NY-REN-64; REN64"
                     /coded_by="NM_001114182.3:124..1506"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8744.1"
                     /db_xref="GeneID:51135"
                     /db_xref="HGNC:HGNC:17967"
                     /db_xref="MIM:606883"
ORIGIN      
        1 mnkpitpsty vrclnvglir klsdfidpqe gwkklavaik kpsgddrynq fhirrfeall
       61 qtgksptsel lfdwgttnct vgdlvdlliq neffapasll lpdavpktan tlpskeaitv
      121 qqkqmpfcdk drtlmtpvqn leqsymppds sspenkslev sdtrfhsfsf yelknvtnnf
      181 derpisvggn kmgeggfgvv ykgyvnnttv avkklaamvd itteelkqqf dqeikvmakc
      241 qhenlvellg fssdgddlcl vyvympngsl ldrlscldgt pplswhmrck iaqgaangin
      301 flhenhhihr diksanilld eaftakisdf glarasekfa qtvmtsrivg ttaymapeal
      361 rgeitpksdi ysfgvvllei itglpavdeh repqllldik eeiedeekti edyidkkmnd
      421 adstsveamy svasqclhek knkrpdikkv qqllqemtas
//
LOCUS       NP_001374940            1162 aa            linear   PRI 21-NOV-2025
DEFINITION  large proline-rich protein BAG6 isoform 5 [Homo sapiens].
ACCESSION   NP_001374940
VERSION     NP_001374940.1
DBSOURCE    REFSEQ: accession NM_001388011.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1162)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 1162)
  AUTHORS   Alashkar Alhamwe,B., Ponath,V., Alhamdan,F., Dorsam,B.,
            Landwehr,C., Linder,M., Pauck,K., Miethe,S., Garn,H.,
            Finkernagel,F., Brichkina,A., Lauth,M., Tiwari,D.K., Buchholz,M.,
            Bachurski,D., Elmshauser,S., Nist,A., Stiewe,T., Pogge von
            Strandmann,L., Szymanski,W., Beutgen,V., Graumann,J.,
            Teply-Szymanski,J., Keber,C., Denkert,C., Jacob,R., Preusser,C. and
            Pogge von Strandmann,E.
  TITLE     BAG6 restricts pancreatic cancer progression by suppressing the
            release of IL33-presenting extracellular vesicles and the
            activation of mast cells
  JOURNAL   Cell Mol Immunol 21 (8), 918-931 (2024)
   PUBMED   38942797
  REMARK    GeneRIF: BAG6 restricts pancreatic cancer progression by
            suppressing the release of IL33-presenting extracellular vesicles
            and the activation of mast cells.
REFERENCE   3  (residues 1 to 1162)
  AUTHORS   Liu,L., Wu,J., Yan,Y., Cheng,S., Yu,S. and Wang,Y.
  TITLE     DERL2 (derlin 2) stabilizes BAG6 (BAG cochaperone 6) in
            chemotherapy resistance of cholangiocarcinoma
  JOURNAL   J Physiol Biochem 80 (1), 81-97 (2024)
   PUBMED   37815698
  REMARK    GeneRIF: DERL2 (derlin 2) stabilizes BAG6 (BAG cochaperone 6) in
            chemotherapy resistance of cholangiocarcinoma.
REFERENCE   4  (residues 1 to 1162)
  AUTHORS   Roboti,P., Lawless,C. and High,S.
  TITLE     Mitochondrial antiviral-signalling protein is a client of the BAG6
            protein quality control complex
  JOURNAL   J Cell Sci 135 (9) (2022)
   PUBMED   35543156
  REMARK    GeneRIF: Mitochondrial antiviral-signalling protein is a client of
            the BAG6 protein quality control complex.
REFERENCE   5  (residues 1 to 1162)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1162)
  AUTHORS   Ozaki,T., Hanaoka,E., Naka,M., Nakagawara,A. and Sakiyama,S.
  TITLE     Cloning and characterization of rat BAT3 cDNA
  JOURNAL   DNA Cell Biol 18 (6), 503-512 (1999)
   PUBMED   10390159
REFERENCE   7  (residues 1 to 1162)
  AUTHORS   Cross,S.J., Tonks,S., Trowsdale,J. and Campbell,R.D.
  TITLE     Novel detection of restriction fragment length polymorphisms in the
            human major histocompatibility complex
  JOURNAL   Immunogenetics 34 (6), 376-384 (1991)
   PUBMED   1684176
REFERENCE   8  (residues 1 to 1162)
  AUTHORS   Banerji,J., Sands,J., Strominger,J.L. and Spies,T.
  TITLE     A gene pair from the human major histocompatibility complex encodes
            large proline-rich proteins with multiple repeated motifs and a
            single ubiquitin-like domain
  JOURNAL   Proc Natl Acad Sci U S A 87 (6), 2374-2378 (1990)
   PUBMED   2156268
REFERENCE   9  (residues 1 to 1162)
  AUTHORS   Spies,T., Bresnahan,M. and Strominger,J.L.
  TITLE     Human major histocompatibility complex contains a minimum of 19
            genes between the complement cluster and HLA-B
  JOURNAL   Proc Natl Acad Sci U S A 86 (22), 8955-8958 (1989)
   PUBMED   2813433
REFERENCE   10 (residues 1 to 1162)
  AUTHORS   Spies,T., Blanck,G., Bresnahan,M., Sands,J. and Strominger,J.L.
  TITLE     A new cluster of genes within the human major histocompatibility
            complex
  JOURNAL   Science 243 (4888), 214-217 (1989)
   PUBMED   2911734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL662801.7.
            
            Summary: This gene was first characterized as part of a cluster of
            genes located within the human major histocompatibility complex
            class III region. This gene encodes a nuclear protein that is
            cleaved by caspase 3 and is implicated in the control of apoptosis.
            In addition, the protein forms a complex with E1A binding protein
            p300 and is required for the acetylation of p53 in response to DNA
            damage. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2957767.1,
                                           SRR11853565.24591.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1162
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..1162
                     /product="large proline-rich protein BAG6 isoform 5"
                     /note="scythe; large proline-rich protein BAT3; large
                     proline-rich protein BAG6; protein G3; HLA-B-associated
                     transcript 3; protein Scythe; BAG family molecular
                     chaperone regulator 6; BCL2 associated athanogene 6"
                     /calculated_mol_wt=122212
     Region          17..87
                     /region_name="Ubl_BAG6"
                     /note="ubiquitin-like (Ubl) domain found in
                     BCL2-associated athanogene 6 (BAG6) and similar proteins;
                     cd01809"
                     /db_xref="CDD:340507"
     Site            order(22..25,58,60,62..65,83..87)
                     /site_type="other"
                     /note="ZF interaction site [polypeptide binding]"
                     /db_xref="CDD:340507"
     Region          270..386
                     /region_name="BAG6"
                     /note="BCL2-associated athanogene 6; pfam12057"
                     /db_xref="CDD:463449"
     Region          <935..1126
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     CDS             1..1162
                     /gene="BAG6"
                     /gene_synonym="BAG-6; BAT3; D6S52E; G3"
                     /coded_by="NM_001388011.1:158..3646"
                     /note="isoform 5 is encoded by transcript variant 51"
                     /db_xref="CCDS:CCDS93882.1"
                     /db_xref="GeneID:7917"
                     /db_xref="HGNC:HGNC:13919"
                     /db_xref="MIM:142590"
ORIGIN      
        1 mepndststa veepdslevl vktldsqtrt fivgaqmnvk efkehiaasv sipsekqrli
       61 yqgrvlqddk klqeynvggk vihlverapp qthlpsgass gtgsasathg ggsppgtrgp
      121 gasvhdrnan syvmvgtfnl psdgsavdvh inmeqapiqs eprvrlvmaq hmirdiqtll
      181 srmecrggpq pqhsqpppqp pavtpepval ssqtsepves eapprepmea eeveerapaq
      241 npeltpgpap agptpapetn apnhpspaey vevlqelqrl esrlqpflqr yyevlgaaat
      301 tdynnnhegr eedqrlinlv geslrllgnt fvalsdlrcn lactpprhlh vvrpmshytt
      361 pmvlqqaaip iqinvgttvt mtgngtrppp tpnaeapppg pgqassvaps stnvessaeg
      421 apppgpappp atshprviri shqsvepvvm mhmniqdsgt qpggvpsapt gplgppghgq
      481 tlgstliqlp slppefmhav ahqithqamv aavasaaagq qvpgfptapt rvviarptpp
      541 qarpshpggp pvsgtlqgag lgtnaslaqm vsglvgqllm qpvlvaqgtp gmapppapat
      601 asasagttnt attagpapgg paqppptpqp smadlqfsql lgnllgpagp gaggsgvasp
      661 titvampgvp aflqgmtdfl qatqtapppp ppppppppap eqqtmpppgs psggagspgg
      721 lgleslspef ftsvvqgvls sllgslgara gssesiaafi qrlsgssnif epgadgalgf
      781 fgallsllcq nfsmvdvvml lhghfqplqr lqpqlrsffh qhylggqept psnirmatht
      841 litgleeyvr esfslvqvqp gvdiirtnle flqeqfnsia ahvlhctdsg fgarllelcn
      901 qglfeclaln lhclggqqme laavingrir rmsrgvnpsl vswlttmmgl rlqvvlehmp
      961 vgpdailryv rrvgdppqpl peepmevqga eraspepqre naspapgtta eeamsrgppp
     1021 apeggsrdeq dgasaetepw aaavppewvp iiqqdiqsqr kvkpqpplsd aylsgmpakr
     1081 rktmqgegpq lllseavsra akaagarplt speslsrdle apevqesyrq qlrsdiqkrl
     1141 qedpnyspqr fpnaqrafad dp
//
LOCUS       NP_001254704             132 aa            linear   PRI 21-NOV-2025
DEFINITION  intraflagellar transport protein 20 homolog isoform 3 [Homo
            sapiens].
ACCESSION   NP_001254704
VERSION     NP_001254704.1
DBSOURCE    REFSEQ: accession NM_001267775.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Li,L., Chen,Y., Liao,W., Yu,Q., Lin,H., Shi,Y., Zhang,L., Fu,G.,
            Wang,Z., Li,X., Kong,X., Zhou,T. and Qin,L.
  TITLE     Associations of IFT20 and GM130 protein expressions with
            clinicopathological features and survival of patients with lung
            adenocarcinoma
  JOURNAL   BMC Cancer 22 (1), 809 (2022)
   PUBMED   35869490
  REMARK    GeneRIF: Associations of IFT20 and GM130 protein expressions with
            clinicopathological features and survival of patients with lung
            adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 132)
  AUTHORS   Grinchuk,O.V., Motakis,E. and Kuznetsov,V.A.
  TITLE     Complex sense-antisense architecture of TNFAIP1/POLDIP2 on 17q11.2
            represents a novel transcriptional structural-functional gene
            module involved in breast cancer progression
  JOURNAL   BMC Genomics 11 Suppl 1 (Suppl 1), S9 (2010)
   PUBMED   20158880
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 132)
  AUTHORS   Finetti,F., Paccani,S.R., Riparbelli,M.G., Giacomello,E.,
            Perinetti,G., Pazour,G.J., Rosenbaum,J.L. and Baldari,C.T.
  TITLE     Intraflagellar transport is required for polarized recycling of the
            TCR/CD3 complex to the immune synapse
  JOURNAL   Nat Cell Biol 11 (11), 1332-1339 (2009)
   PUBMED   19855387
REFERENCE   7  (residues 1 to 132)
  AUTHORS   Jurczyk,A., Gromley,A., Redick,S., San Agustin,J., Witman,G.,
            Pazour,G.J., Peters,D.J. and Doxsey,S.
  TITLE     Pericentrin forms a complex with intraflagellar transport proteins
            and polycystin-2 and is required for primary cilia assembly
  JOURNAL   J Cell Biol 166 (5), 637-643 (2004)
   PUBMED   15337773
REFERENCE   8  (residues 1 to 132)
  AUTHORS   Yin,G., Dai,J., Ji,C., Ni,X., Shu,G., Ye,X., Dai,J., Wu,Q., Gu,S.,
            Xie,Y., Zhao,R.C. and Mao,Y.
  TITLE     Cloning and characterization of the human IFT20 gene
  JOURNAL   Mol Biol Rep 30 (4), 255-260 (2003)
   PUBMED   14672413
  REMARK    GeneRIF: Data report the molecular cloning and characterization of
            a novel human cDNA encoding a putative protein of 158 amino acid
            residues which shares high homology to Mus musculus intraflagellar
            transport protein mIFT20.
REFERENCE   9  (residues 1 to 132)
  AUTHORS   Baker,S.A., Freeman,K., Luby-Phelps,K., Pazour,G.J. and
            Besharse,J.C.
  TITLE     IFT20 links kinesin II with a mammalian intraflagellar transport
            complex that is conserved in motile flagella and sensory cilia
  JOURNAL   J Biol Chem 278 (36), 34211-34218 (2003)
   PUBMED   12821668
REFERENCE   10 (residues 1 to 132)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Ray,S., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human retina for the NEIBank
            Project: retbindin, an abundant, novel retinal cDNA and alternative
            splicing of other retina-preferred gene transcripts
  JOURNAL   Mol Vis 8, 196-204 (2002)
   PUBMED   12107411
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL713094.1, BE619475.1,
            BC002640.2 and AI768816.1.
            
            Summary: This gene encodes a intraflagellar transport protein
            important for intracellular transport. The encoded protein forms
            part of a complex involved in trafficking of proteins from the
            Golgi body, including recycling of immune signalling components
            (Finetti et al., PubMed: 19855387). This gene is part of a complex
            set of sense-antisense loci that may be co-regulated. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed for this gene. A pseudogene of this gene is located on the
            long arm of chromosome 14.[provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and uses
            a downstream in-frame start codon, compared to variant 1. Variants
            3 and 4 encode the same isoform (3), which has a shorter N-terminus
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.348412.1,
                                           ERR1172420.2709.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2163105 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..132
                     /product="intraflagellar transport protein 20 homolog
                     isoform 3"
                     /note="intraflagellar transport protein 20 homolog;
                     intraflagellar transport protein IFT20; intraflagellar
                     transport 20 homolog"
                     /calculated_mol_wt=15150
     Region          11..119
                     /region_name="IFT20"
                     /note="Intraflagellar transport complex B, subunit 20;
                     pfam14931"
                     /db_xref="CDD:464383"
     Region          70..132
                     /region_name="IFT57-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY31.1)"
     CDS             1..132
                     /gene="IFT20"
                     /coded_by="NM_001267775.2:172..570"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58534.1"
                     /db_xref="GeneID:90410"
                     /db_xref="HGNC:HGNC:30989"
                     /db_xref="MIM:614394"
ORIGIN      
        1 makdilgeag lhfdelnklr vldpevtqqt ielkeeckdf vdkigqfqki vgglielvdq
       61 lakeaenekm kaigarnllk siakqreaqq qqlqaliaek kmqleryrve yealckveae
      121 qnefidqfif qk
//
LOCUS       NP_001373394             407 aa            linear   PRI 21-NOV-2025
DEFINITION  plasminogen activator inhibitor 1 isoform 11 precursor [Homo
            sapiens].
ACCESSION   NP_001373394
VERSION     NP_001373394.1
DBSOURCE    REFSEQ: accession NM_001386465.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Doelker,T., Gallwas,J. and Grundker,C.
  TITLE     Suppressing Expression of SERPINE1/PAI1 Through Activation of GPER1
            Reduces Progression of Vulvar Carcinoma
  JOURNAL   Cancer Genomics Proteomics 21 (6), 566-579 (2024)
   PUBMED   39467628
  REMARK    GeneRIF: Suppressing Expression of SERPINE1/PAI1 Through Activation
            of GPER1 Reduces Progression of Vulvar Carcinoma.
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Khoukaz,H.B., Vadali,M., Schoenherr,A., Ramirez-Perez,F.I.,
            Morales-Quinones,M., Sun,Z., Fujie,S., Foote,C.A., Lyu,Z., Zeng,S.,
            Augenreich,M.A., Cai,D., Chen,S.Y., Joshi,T., Ji,Y., Hill,M.A.,
            Martinez-Lemus,L.A. and Fay,W.P.
  TITLE     PAI-1 Regulates the Cytoskeleton and Intrinsic Stiffness of
            Vascular Smooth Muscle Cells
  JOURNAL   Arterioscler Thromb Vasc Biol 44 (10), 2191-2203 (2024)
   PUBMED   38868940
  REMARK    GeneRIF: PAI-1 Regulates the Cytoskeleton and Intrinsic Stiffness
            of Vascular Smooth Muscle Cells.
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Guo,X., Zhou,H., Liu,Y., Xu,W., Kanwore,K. and Zhang,L.
  TITLE     Glial-Cell-Line-Derived Neurotrophic Factor Promotes Glioblastoma
            Cell Migration and Invasion via the SMAD2/3-SERPINE1-Signaling Axis
  JOURNAL   Int J Mol Sci 25 (18), 10229 (2024)
   PUBMED   39337713
  REMARK    GeneRIF: Glial-Cell-Line-Derived Neurotrophic Factor Promotes
            Glioblastoma Cell Migration and Invasion via the
            SMAD2/3-SERPINE1-Signaling Axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Yatsenko,T., Rios,R., Nogueira,T., Salama,Y., Takahashi,S.,
            Adachi,E., Tabe,Y., Hattori,N., Osada,T., Naito,T., Takahashi,K.,
            Hattori,K. and Heissig,B.
  TITLE     The influence of 4G/5G polymorphism in the
            plasminogen-activator-inhibitor-1 promoter on COVID-19 severity and
            endothelial dysfunction
  JOURNAL   Front Immunol 15, 1445294 (2024)
   PUBMED   39281671
  REMARK    GeneRIF: The influence of 4G/5G polymorphism in the
            plasminogen-activator-inhibitor-1 promoter on COVID-19 severity and
            endothelial dysfunction.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Heiman,M., Gupta,S., Lewandowska,M. and Shapiro,A.D.
  TITLE     Complete Plasminogen Activator Inhibitor 1 Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   28771291
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Fay,W.P., Shapiro,A.D., Shih,J.L., Schleef,R.R. and Ginsburg,D.
  TITLE     Brief report: complete deficiency of plasminogen-activator
            inhibitor type 1 due to a frame-shift mutation
  JOURNAL   N Engl J Med 327 (24), 1729-1733 (1992)
   PUBMED   1435917
REFERENCE   8  (residues 1 to 407)
  AUTHORS   Koh,S.C., Wong,P.C., Yuen,R., Chua,S.E., Ng,B.L. and Ratnam,S.S.
  TITLE     Concentration of plasminogen activators and inhibitor in the human
            endometrium at different phases of the menstrual cycle
  JOURNAL   J Reprod Fertil 96 (2), 407-413 (1992)
   PUBMED   1339823
REFERENCE   9  (residues 1 to 407)
  AUTHORS   Hagege,J., Peraldi,M.N., Rondeau,E., Adida,C., Delarue,F.,
            Medcalf,R., Schleuning,W.D. and Sraer,J.D.
  TITLE     Plasminogen activator inhibitor-1 deposition in the extracellular
            matrix of cultured human mesangial cells
  JOURNAL   Am J Pathol 141 (1), 117-128 (1992)
   PUBMED   1632457
REFERENCE   10 (residues 1 to 407)
  AUTHORS   Ehrlich,H.J., Gebbink,R.K., Keijer,J., Linders,M., Preissner,K.T.
            and Pannekoek,H.
  TITLE     Alteration of serpin specificity by a protein cofactor. Vitronectin
            endows plasminogen activator inhibitor 1 with thrombin inhibitory
            properties
  JOURNAL   J Biol Chem 265 (22), 13029-13035 (1990)
   PUBMED   1695900
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004876.2.
            
            Summary: This gene encodes a member of the serine proteinase
            inhibitor (serpin) superfamily. This member is the principal
            inhibitor of tissue plasminogen activator (tPA) and urokinase
            (uPA), and hence is an inhibitor of fibrinolysis. The protein also
            functions as a component of innate antiviral immunity. Defects in
            this gene are the cause of plasminogen activator inhibitor-1
            deficiency (PAI-1 deficiency), and high concentrations of the gene
            product are associated with thrombophilia. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3208508.1,
                                           SRR14038194.4200740.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..407
                     /product="plasminogen activator inhibitor 1 isoform 11
                     precursor"
                     /note="serine (or cysteine) proteinase inhibitor, clade E
                     (nexin, plasminogen activator inhibitor type 1), member 1;
                     endothelial plasminogen activator inhibitor; serpin E1;
                     serpin peptidase inhibitor, clade E (nexin, plasminogen
                     activator inhibitor type 1), member 1"
                     /calculated_mol_wt=43187
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2309
     Region          29..407
                     /region_name="serpinE1_PAI-1"
                     /note="serpin family E member 1, plasminogen activator
                     inhibitor-1; cd02051"
                     /db_xref="CDD:381007"
     Site            order(124,133..134,137,143,145..148,154,158,161..162)
                     /site_type="other"
                     /note="vitronectin binding site [polypeptide binding]"
                     /db_xref="CDD:381007"
     Site            order(172..173,346,348)
                     /site_type="other"
                     /note="putative Cl binding site [ion binding]"
                     /db_xref="CDD:381007"
     Site            order(228,230,233,235,245,264,292..295,361..362,369..378)
                     /site_type="other"
                     /note="plasminogen activator binding site [polypeptide
                     binding]"
                     /db_xref="CDD:381007"
     Site            232
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05121.1)"
     Site            288
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05121.1)"
     Site            352
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P05121.1)"
     Site            order(355..362,368..385)
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381007"
     Site            374..375
                     /site_type="other"
                     /note="Reactive bond; propagated from UniProtKB/Swiss-Prot
                     (P05121.1)"
     CDS             1..407
                     /gene="SERPINE1"
                     /gene_synonym="PAI; PAI-1; PAI1; PLANH1"
                     /coded_by="NM_001386465.1:143..1366"
                     /note="isoform 11 precursor is encoded by transcript
                     variant 11"
                     /db_xref="GeneID:5054"
                     /db_xref="HGNC:HGNC:8583"
                     /db_xref="MIM:173360"
ORIGIN      
        1 mqmspaltcl vlglalvfge gsavhhppsy vahlasdfgv rvfqqvaqas kdrnvvfspy
       61 gvasvlamlq lttggetqqq iqaamgfkid dkgmapalrh lykelmgpwn kdeisttdai
      121 fvqrdlklvq gfmphffrlf rstvkqvdfs everarfiin dwvkthtkgm isnllgkgav
      181 dqltrlvlvn alyfngqwkt pfpdssthrr lfhksdgstv svpmmaqtnk fnytefttpd
      241 ghyydilelp yhgdtlsmfi aapyekevpl saltnilsaq lishwkgnmt rlprllvlpk
      301 fsletevdlr kplenlgmtd mfrqfqadft slsdqeplhv aqalqkvkie vnesgtvass
      361 stgesgsavi vsarmapeei imdrpflfvv rhnptgtvlf mgqvmep
//
LOCUS       NP_001362621             464 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform ff [Homo sapiens].
ACCESSION   NP_001362621 XP_016858618
VERSION     NP_001362621.1
DBSOURCE    REFSEQ: accession NM_001375692.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 464)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 464)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 464)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 464)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            On Oct 31, 2019 this sequence version replaced XP_016858618.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.3146.1,
                                           SRR1803616.60484.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..464
                     /product="abl interactor 2 isoform ff"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=49964
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62484; propagated from
                     UniProtKB/Swiss-Prot (Q9NYB9.1)"
     Region          93..156
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          <221..348
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          403..463
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(411,413,416,420,438..439,452,454..455)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..464
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375692.1:122..1516"
                     /note="isoform ff is encoded by transcript variant 37"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqs adkqraleet kayttqslas
       61 vaylintlan nvlqmldiqa sqlrrmessi nhisqtvdih kekvarreig ilttnkntsr
      121 thkiiapanl erpvryirkp idytilddig hgvkwllrfk vstqnmkmgg lprttpptqk
      181 ppsppmsgkg tlgssgssgg shpssrsssr ensgsgsvgv piavptpspp svfpapagsa
      241 gtpplpatsa sapaplvpat vpsstapdaa aggaqtladg ftsptppvvs stpptghpvq
      301 fysmnrpasr htpptiggsl pyrrppsits qtslqnqmng gpfysqnpvs dtppppppve
      361 epvfdesppp ppppedyeee eaavveysdp yaeedppwap rsylekvvai ydytkdkede
      421 lsfqegaiiy vikknddgwy egvmngvtgl fpgnyvesim hyse
//
LOCUS       NP_001350467             919 aa            linear   PRI 21-NOV-2025
DEFINITION  TRPM8 channel-associated factor 2 isoform C [Homo sapiens].
ACCESSION   NP_001350467 XP_006715990
VERSION     NP_001350467.1
DBSOURCE    REFSEQ: accession NM_001363538.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Yun,D., Liang,J., Wang,X., Fan,J., Wang,X., Li,J., Ren,X., Liu,J.,
            Ren,X., Zhang,H., Shang,G., Jin,W., Chen,L., Li,T., Zhang,C., Yu,S.
            and Yang,X.
  TITLE     TCAF2 drives glioma cellular migratory/invasion properties through
            STAT3 signaling
  JOURNAL   Mol Cell Biochem 479 (7), 1801-1815 (2024)
   PUBMED   38019450
  REMARK    GeneRIF: TCAF2 drives glioma cellular migratory/invasion properties
            through STAT3 signaling.
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Li,Y., Li,J., Chen,H., Lu,B., Lu,F., Chen,H., Liu,H. and Qian,C.
  TITLE     TCAF2 is associated with the immune microenvironment, promotes
            pathogenesis, and impairs prognosis in glioma
  JOURNAL   Gene 883, 147667 (2023)
   PUBMED   37506986
  REMARK    GeneRIF: TCAF2 is associated with the immune microenvironment,
            promotes pathogenesis, and impairs prognosis in glioma.
REFERENCE   4  (residues 1 to 919)
  AUTHORS   Li,X., Qi,Q., Li,Y., Miao,Q., Yin,W., Pan,J., Zhao,Z., Chen,X.,
            Yang,F., Zhou,X., Huang,M., Wang,C., Deng,L., Huang,D., Qi,M.,
            Fan,S., Zhang,Y., Qiu,S., Deng,W., Liu,T., Chen,M., Ye,W. and
            Zhang,D.
  TITLE     TCAF2 in Pericytes Promotes Colorectal Cancer Liver Metastasis via
            Inhibiting Cold-Sensing TRPM8 Channel
  JOURNAL   Adv Sci (Weinh) 10 (30), e2302717 (2023)
   PUBMED   37635201
  REMARK    GeneRIF: TCAF2 in Pericytes Promotes Colorectal Cancer Liver
            Metastasis via Inhibiting Cold-Sensing TRPM8 Channel.
REFERENCE   5  (residues 1 to 919)
  AUTHORS   Hsieh,P., Dang,V., Vollger,M.R., Mao,Y., Huang,T.H., Dishuck,P.C.,
            Baker,C., Cantsilieris,S., Lewis,A.P., Munson,K.M., Sorensen,M.,
            Welch,A.E., Underwood,J.G. and Eichler,E.E.
  TITLE     Evidence for opposing selective forces operating on human-specific
            duplicated TCAF genes in Neanderthals and humans
  JOURNAL   Nat Commun 12 (1), 5118 (2021)
   PUBMED   34433829
  REMARK    GeneRIF: Evidence for opposing selective forces operating on
            human-specific duplicated TCAF genes in Neanderthals and humans.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 919)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 919)
  AUTHORS   Gkika,D., Lemonnier,L., Shapovalov,G., Gordienko,D., Poux,C.,
            Bernardini,M., Bokhobza,A., Bidaux,G., Degerny,C., Verreman,K.,
            Guarmit,B., Benahmed,M., de Launoit,Y., Bindels,R.J., Fiorio Pla,A.
            and Prevarskaya,N.
  TITLE     TRP channel-associated factors are a novel protein family that
            regulates TRPM8 trafficking and activity
  JOURNAL   J Cell Biol 208 (1), 89-107 (2015)
   PUBMED   25559186
  REMARK    GeneRIF: Report novel TRP channel-associated factors that modulate
            TRPM8 activity.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073264.5 and AC106862.3.
            
            On May 24, 2018 this sequence version replaced XP_006715990.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.179878.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000684770.1/ ENSP00000506869.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q35"
     Protein         1..919
                     /product="TRPM8 channel-associated factor 2 isoform C"
                     /note="family with sequence similarity 139, member A;
                     protein FAM115C; family with sequence similarity 115,
                     member C; TRP channel-associated factor 2"
                     /calculated_mol_wt=100775
     Region          522..632
                     /region_name="M60-like_N"
                     /note="N-terminal domain of M60-like peptidases;
                     pfam17291"
                     /db_xref="CDD:435844"
     Region          633..889
                     /region_name="Peptidase_M60"
                     /note="Peptidase M60, enhancin and enhancin-like;
                     pfam13402"
                     /db_xref="CDD:433178"
     CDS             1..919
                     /gene="TCAF2"
                     /gene_synonym="FAM115C; FAM139A; GATD9; GATD9B"
                     /coded_by="NM_001363538.2:59..2818"
                     /note="isoform C is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS87559.1"
                     /db_xref="GeneID:285966"
                     /db_xref="HGNC:HGNC:26878"
                     /db_xref="MIM:616252"
ORIGIN      
        1 matiaaaafe almdgvtcwd vprgpipsel lligeaafpv mvndkgqvli aassygrgrl
       61 vvvshegyls htglapflln avswlcpcpg apvgvhpsla plvnilqdag leaqvkpepg
      121 eplgvycina yndtltatli qfvkhgggll iggqawywas qhgpdkvlsr fpgnkvtsva
      181 gvyftdtygd rdrfkvskkv pkiplhvryg edvrqdqqql legiseldir tggvpsqllv
      241 hgalafplgl daslncflaa ahygrgrvvl aahecllcap kmgpfllnav rwlargqtgk
      301 vgvntnlkdl cpllsehglq cslephlnsd lcvycckays dkeakqlqef vaegggllig
      361 gqawwwasqn pghcplagfp gniilncfgl silpqtlkag cfpvptpemr syhfrkalsq
      421 fqailnheng nleksclakl rvdgaaflqi paegvpayis lhrllrkmlr gsglpavsre
      481 npvasdsyea avlslatgla hsgtdcsqla qglgtwtcss slypskhpit veinginpgn
      541 ndcwvstgly llegqnaevs lseaaasagl rvqigchtdd ltkarklsra pvvthqcwmd
      601 rtersvsclw ggllyvivpk gsqlgpvpvt irgavpapyy klgktsleew krqmqenlap
      661 wgelatdnii ltvpttnlqa lkdpepvlrl wdemmqavar laaepfpfrr perivadvqi
      721 sagwmhsgyp imchlesvke iinemdmrsr gvwgpihelg hnqqrhgwef pphtteatcn
      781 lwsvyvhetv lgipraqahe alsppererr ikahlgkgap lcdwnvwtal etylqlqeaf
      841 gwepftqlfa eyqtlshlpk dntgrmnlwv kkfsekvkkn lvpffeawgw piqkevadsl
      901 aslpewqenp mqvylrark
//
LOCUS       NP_001035702             153 aa            linear   PRI 21-NOV-2025
DEFINITION  protein SSX4 isoform b [Homo sapiens].
ACCESSION   NP_001035702
VERSION     NP_001035702.1
DBSOURCE    REFSEQ: accession NM_001040612.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Ayyoub,M., Merlo,A., Hesdorffer,C.S., Rimoldi,D., Speiser,D.,
            Cerottini,J.C., Chen,Y.T., Old,L.J., Stevanovic,S. and Valmori,D.
  TITLE     CD4+ T cell responses to SSX-4 in melanoma patients
  JOURNAL   J Immunol 174 (8), 5092-5099 (2005)
   PUBMED   15814740
REFERENCE   6  (residues 1 to 153)
  AUTHORS   Chen,C.H., Chen,G.J., Lee,H.S., Huang,G.T., Yang,P.M., Tsai,L.J.,
            Chen,D.S. and Sheu,J.C.
  TITLE     Expressions of cancer-testis antigens in human hepatocellular
            carcinomas
  JOURNAL   Cancer Lett 164 (2), 189-195 (2001)
   PUBMED   11179834
REFERENCE   7  (residues 1 to 153)
  AUTHORS   dos Santos,N.R., de Bruijn,D.R. and van Kessel,A.G.
  TITLE     Molecular mechanisms underlying human synovial sarcoma development
  JOURNAL   Genes Chromosomes Cancer 30 (1), 1-14 (2001)
   PUBMED   11107170
  REMARK    Review article
REFERENCE   8  (residues 1 to 153)
  AUTHORS   Skytting,B., Nilsson,G., Brodin,B., Xie,Y., Lundeberg,J., Uhlen,M.
            and Larsson,O.
  TITLE     A novel fusion gene, SYT-SSX4, in synovial sarcoma
  JOURNAL   J Natl Cancer Inst 91 (11), 974-975 (1999)
   PUBMED   10359553
REFERENCE   9  (residues 1 to 153)
  AUTHORS   Gure,A.O., Tureci,O., Sahin,U., Tsang,S., Scanlan,M.J., Jager,E.,
            Knuth,A., Pfreundschuh,M., Old,L.J. and Chen,Y.T.
  TITLE     SSX: a multigene family with several members transcribed in normal
            testis and human cancer
  JOURNAL   Int J Cancer 72 (6), 965-971 (1997)
   PUBMED   9378559
REFERENCE   10 (residues 1 to 153)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL606490.15, AA312651.1,
            BE866727.1, BC137395.1 and CD671168.1.
            
            Summary: The product of this gene belongs to the family of highly
            homologous synovial sarcoma X (SSX) breakpoint proteins. These
            proteins may function as transcriptional repressors. They are also
            capable of eliciting spontaneously humoral and cellular immune
            responses in cancer patients, and are potentially useful targets in
            cancer vaccine-based immunotherapy. SSX1, SSX2 and SSX4 genes have
            been involved in the t(X;18) translocation characteristically found
            in all synovial sarcomas. This translocation results in the fusion
            of the synovial sarcoma translocation gene on chromosome 18 to one
            of the SSX genes on chromosome X. Chromosome Xp11 contains a
            segmental duplication resulting in two identical copies of synovial
            sarcoma, X breakpoint 4, SSX4 and SSX4B, in tail-to-tail
            orientation. This gene, SSX4B, represents the more centromeric
            copy. Two transcript variants encoding distinct isoforms have been
            identified for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an exon in the 3' coding
            region compared to variant 1. This results in a frame-shift, and a
            shorter isoform (b) with a distinct C-terminus compared to isoform
            a.
            
            CCDS Note: SSXB4 is identical to SSX4 as it produces the same
            protein product. This protein is likey to be functional despite
            arising from a duplication, therefore this CCDS has been retained.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.23"
     Protein         1..153
                     /product="protein SSX4 isoform b"
                     /note="protein SSX4; cancer/testis antigen 5.4; synovial
                     sarcoma, X breakpoint 4B"
                     /calculated_mol_wt=17787
     Region          23..82
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     CDS             1..153
                     /gene="SSX4B"
                     /gene_synonym="CT5.4"
                     /coded_by="NM_001040612.4:120..581"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43935.1"
                     /db_xref="GeneID:548313"
                     /db_xref="HGNC:HGNC:16880"
ORIGIN      
        1 mngddafarr prddaqisek lrkafddiak yfskkewekm kssekivyvy mklnyevmtk
       61 lgfkvtlppf mrskraadfh gndfgndrnh rnqverpqmt fgslqrifpk dpkggnmpgp
      121 tdcvressww fmkrsatlrk mtsnsprgyd tcp
//
LOCUS       NP_001382253             738 aa            linear   PRI 21-NOV-2025
DEFINITION  myomegalin isoform 43 [Homo sapiens].
ACCESSION   NP_001382253
VERSION     NP_001382253.1
DBSOURCE    REFSEQ: accession NM_001395324.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Pan,R., Dai,J., Liang,W., Wang,H., Ye,L., Ye,S., Lin,Z., Huang,S.,
            Xiong,Y., Zhang,L., Lu,L., Wang,O., Shen,X., Liao,W. and Lu,X.
  TITLE     PDE4DIP contributes to colorectal cancer growth and chemoresistance
            through modulation of the NF1/RAS signaling axis
  JOURNAL   Cell Death Dis 14 (6), 373 (2023)
   PUBMED   37355626
  REMARK    GeneRIF: PDE4DIP contributes to colorectal cancer growth and
            chemoresistance through modulation of the NF1/RAS signaling axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 738)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   4  (residues 1 to 738)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 738)
  AUTHORS   Abou Ziki,M.D., Bhat,N., Neogi,A., Driscoll,T.P., Ugwu,N., Liu,Y.,
            Smith,E., Abboud,J.M., Chouairi,S., Schwartz,M.A., Akar,J.G. and
            Mani,A.
  TITLE     Epistatic interaction of PDE4DIP and DES mutations in familial
            atrial fibrillation with slow conduction
  JOURNAL   Hum Mutat 42 (10), 1279-1293 (2021)
   PUBMED   34289528
  REMARK    GeneRIF: Epistatic interaction of PDE4DIP and DES mutations in
            familial atrial fibrillation with slow conduction.
REFERENCE   6  (residues 1 to 738)
  AUTHORS   Shimada,H., Kuboshima,M., Shiratori,T., Nabeya,Y., Takeuchi,A.,
            Takagi,H., Nomura,F., Takiguchi,M., Ochiai,T. and Hiwasa,T.
  TITLE     Serum anti-myomegalin antibodies in patients with esophageal
            squamous cell carcinoma
  JOURNAL   Int J Oncol 30 (1), 97-103 (2007)
   PUBMED   17143517
  REMARK    GeneRIF: MMGL-antibody is significantly with a favorable prognosis.
            Consequently, MMGL-anatibodies may be a useful tumor marker to
            diagnose and establish a prognosis in patients with esophageal
            squamous cell carcinoma.
REFERENCE   7  (residues 1 to 738)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 738)
  AUTHORS   Soejima,H., Kawamoto,S., Akai,J., Miyoshi,O., Arai,Y., Morohka,T.,
            Matsuo,S., Niikawa,N., Kimura,A., Okubo,K. and Mukai,T.
  TITLE     Isolation of novel heart-specific genes using the BodyMap database
  JOURNAL   Genomics 74 (1), 115-120 (2001)
   PUBMED   11374908
REFERENCE   9  (residues 1 to 738)
  AUTHORS   Verde,I., Pahlke,G., Salanova,M., Zhang,G., Wang,S., Coletti,D.,
            Onuffer,J., Jin,S.L. and Conti,M.
  TITLE     Myomegalin is a novel protein of the golgi/centrosome that
            interacts with a cyclic nucleotide phosphodiesterase
  JOURNAL   J Biol Chem 276 (14), 11189-11198 (2001)
   PUBMED   11134006
REFERENCE   10 (residues 1 to 738)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC239802.3.
            
            Summary: The protein encoded by this gene serves to anchor
            phosphodiesterase 4D to the Golgi/centrosome region of the cell.
            Defects in this gene may be a cause of myeloproliferative disorder
            (MBD) associated with eosinophilia. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     Protein         1..738
                     /product="myomegalin isoform 43"
                     /note="myomegalin; cardiomyopathy-associated protein 2"
                     /calculated_mol_wt=84995
     Region          24..>212
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          <123..>713
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..738
                     /gene="PDE4DIP"
                     /gene_synonym="CMYA2; MMGL"
                     /coded_by="NM_001395324.1:21..2237"
                     /note="isoform 43 is encoded by transcript variant 43"
                     /db_xref="GeneID:9659"
                     /db_xref="HGNC:HGNC:15580"
                     /db_xref="MIM:608117"
ORIGIN      
        1 mteellkqqk lnshettitq qsvsdshlae lqekiqqtea tnkilqekln emsyelkcaq
       61 essqkqdgti qnlketlksr ereteelyqv iegqndtmak lremlhqsql gqlhssegts
      121 paqqqvalld lqsalfcsql eiqklqrvvr qkerqladak qcvqfveaaa heseqqkeas
      181 wkhnqelrka lqqlqeelqn ksqqlrawea ekyneirtqe qniqhlnhsl shkeqllqef
      241 rellqyrdns dktleaneml leklrqrihd kavaleraid ekfsaleeke kelrqlrlav
      301 rerdhdlerl rdvlssneat mqsmesllra kgleveqlst tcqnlqwlke emetkfsrwq
      361 keqesiiqql qtslhdrnke dlsatllckl gpgqseiaee lcqrlqrker mlqdllsdrn
      421 kqvlehemei qgllqsvstr eqesqaaaek lvqalmerns elqalrqylg grdslmsqap
      481 isnqqaevtp tgrlgkqtdq gsmqipsrdd stsltakedv siprstlgdl dtvaglekel
      541 snakeelelm akkeresqme lsalqsmmav qeeelqvqaa dmesltrniq ikedlikdlq
      601 mqlvdpedip amerltqevl llrekvasve sqgqeisgnr rqqlllmleg lvdersrlne
      661 alqaerqlys slvkfhahpe sserdrtlqv elegaqvlrs rleevlgrsl erlnrletla
      721 aigggelesv rihhkhay
//
LOCUS       NP_758860                349 aa            linear   PRI 21-NOV-2025
DEFINITION  membrane cofactor protein isoform 14 precursor [Homo sapiens].
ACCESSION   NP_758860
VERSION     NP_758860.1
DBSOURCE    REFSEQ: accession NM_172350.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Grodstein,F., Lemos,B., Yang,J., de Paiva Lopes,K., Vialle,R.A.,
            Seyfried,N., Wang,Y., Shireby,G., Hannon,E., Thomas,A., Brookes,K.,
            Mill,J., De Jager,P.L. and Bennett,D.A.
  TITLE     Genetic architecture of epigenetic cortical clock age in brain
            tissue from older individuals: alterations in CD46 and other loci
  JOURNAL   Epigenetics 19 (1), 2392050 (2024)
   PUBMED   39169872
  REMARK    GeneRIF: Genetic architecture of epigenetic cortical clock age in
            brain tissue from older individuals: alterations in CD46 and other
            loci.
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Thi,T.N., Thanh,H.D., Nguyen,V.T., Kwon,S.Y., Moon,C., Hwang,E.C.
            and Jung,C.
  TITLE     Complement regulatory protein CD46 promotes bladder cancer
            metastasis through activation of MMP9
  JOURNAL   Int J Oncol 65 (1) (2024)
   PUBMED   38847230
  REMARK    GeneRIF: Complement regulatory protein CD46 promotes bladder cancer
            metastasis through activation of MMP9.
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Vassiliev,P., Gusev,E., Komelkova,M., Kochetkov,A., Dobrynina,M.
            and Sarapultsev,A.
  TITLE     Computational Analysis of CD46 Protein Interaction with SARS-CoV-2
            Structural Proteins: Elucidating a Putative Viral Entry Mechanism
            into Human Cells
  JOURNAL   Viruses 15 (12), 2297 (2023)
   PUBMED   38140538
  REMARK    GeneRIF: Computational Analysis of CD46 Protein Interaction with
            SARS-CoV-2 Structural Proteins: Elucidating a Putative Viral Entry
            Mechanism into Human Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Richards,A., Kemp,E.J., Liszewski,M.K., Goodship,J.A., Lampe,A.K.,
            Decorte,R., Muslumanoglu,M.H., Kavukcu,S., Filler,G., Pirson,Y.,
            Wen,L.S., Atkinson,J.P. and Goodship,T.H.
  TITLE     Mutations in human complement regulator, membrane cofactor protein
            (CD46), predispose to development of familial hemolytic uremic
            syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (22), 12966-12971 (2003)
   PUBMED   14566051
  REMARK    GeneRIF: Mutations predispose to development of familial hemolytic
            uremic syndrome.
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Martin,B. and Smith,R.J.H.
  TITLE     C3 Glomerulopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301598
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Noris,M., Bresin,E., Mele,C. and Remuzzi,G.
  TITLE     Genetic Atypical Hemolytic-Uremic Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301541
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Russell,S.M., Sparrow,R.L., McKenzie,I.F. and Purcell,D.F.
  TITLE     Tissue-specific and allelic expression of the complement regulator
            CD46 is controlled by alternative splicing
  JOURNAL   Eur J Immunol 22 (6), 1513-1518 (1992)
   PUBMED   1601037
REFERENCE   8  (residues 1 to 349)
  AUTHORS   Adams,E.M., Brown,M.C., Nunge,M., Krych,M. and Atkinson,J.P.
  TITLE     Contribution of the repeating domains of membrane cofactor protein
            (CD46) of the complement system to ligand binding and cofactor
            activity
  JOURNAL   J Immunol 147 (9), 3005-3011 (1991)
   PUBMED   1717583
REFERENCE   9  (residues 1 to 349)
  AUTHORS   Post,T.W., Liszewski,M.K., Adams,E.M., Tedja,I., Miller,E.A. and
            Atkinson,J.P.
  TITLE     Membrane cofactor protein of the complement system: alternative
            splicing of serine/threonine/proline-rich exons and cytoplasmic
            tails produces multiple isoforms that correlate with protein
            phenotype
  JOURNAL   J Exp Med 174 (1), 93-102 (1991)
   PUBMED   1711570
REFERENCE   10 (residues 1 to 349)
  AUTHORS   Lublin,D.M., Liszewski,M.K., Post,T.W., Arce,M.A., Le Beau,M.M.,
            Rebentisch,M.B., Lemons,L.S., Seya,T. and Atkinson,J.P.
  TITLE     Molecular cloning and chromosomal localization of human membrane
            cofactor protein (MCP). Evidence for inclusion in the multigene
            family of complement-regulatory proteins
  JOURNAL   J Exp Med 168 (1), 181-194 (1988)
   PUBMED   3260937
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB078198.1, D84105.1 and
            BC030594.2.
            
            Summary: The protein encoded by this gene is a type I membrane
            protein and is a regulatory part of the complement system. The
            encoded protein has cofactor activity for inactivation of
            complement components C3b and C4b by serum factor I, which protects
            the host cell from damage by complement. In addition, the encoded
            protein can act as a receptor for the Edmonston strain of measles
            virus, human herpesvirus-6, and type IV pili of pathogenic
            Neisseria. Finally, the protein encoded by this gene may be
            involved in the fusion of the spermatozoa with the oocyte during
            fertilization. Mutations at this locus have been associated with
            susceptibility to hemolytic uremic syndrome. Alternatively spliced
            transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (n) lacks three alternate in-frame
            exons as well as an alternate segment compared to variant a, which
            causes a frameshift. The resulting isoform (14) is shorter and has
            a distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D84105.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.2"
     Protein         1..349
                     /product="membrane cofactor protein isoform 14 precursor"
                     /note="CD46 antigen, complement regulatory protein;
                     membrane cofactor protein (CD46, trophoblast-lymphocyte
                     cross-reactive antigen); complement membrane cofactor
                     protein; measles virus receptor; trophoblast leucocyte
                     common antigen; antigen identified by monoclonal antibody
                     TRA-2-10; trophoblast leukocyte common antigen; CD46
                     molecule, complement regulatory protein"
                     /calculated_mol_wt=35475
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3869
     mat_peptide     35..349
                     /product="membrane cofactor protein isoform 14"
                     /calculated_mol_wt=35475
     Region          54..285
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     CDS             1..349
                     /gene="CD46"
                     /gene_synonym="AHUS2; MCP; MIC10; TLX; TRA2.10"
                     /coded_by="NM_172350.3:160..1209"
                     /note="isoform 14 precursor is encoded by transcript
                     variant n"
                     /db_xref="CCDS:CCDS1479.1"
                     /db_xref="GeneID:4179"
                     /db_xref="HGNC:HGNC:6953"
                     /db_xref="MIM:120920"
ORIGIN      
        1 meppgrrecp fpswrfpgll laamvlllys fsdaceeppt feameligkp kpyyeigerv
       61 dykckkgyfy ipplathtic drnhtwlpvs ddacyretcp yirdplngqa vpangtyefg
      121 yqmhficneg yyligeeily celkgsvaiw sgkppicekv lctpppkikn gkhtfsevev
      181 feyldavtys cdpapgpdpf sligestiyc gdnsvwsraa peckvvkcrf pvvengkqis
      241 gfgkkfyyka tvmfecdkgf yldgsdtivc dsnstwdppv pkclkgprpt ykppvsnypg
      301 ypkpeegild sldvwviavi viaigkqmve lnmpltrlnq plqqsreae
//
LOCUS       NP_001121683             554 aa            linear   PRI 21-NOV-2025
DEFINITION  nudC domain-containing protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001121683
VERSION     NP_001121683.1
DBSOURCE    REFSEQ: accession NM_001128211.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Han,B., He,J., Chen,Q., Yuan,M., Zeng,X., Li,Y., Zeng,Y., He,M.,
            Feng,D. and Ma,D.
  TITLE     Identifying the role of NUDCD1 in human tumors from clinical and
            molecular mechanisms: a study based on comprehensive bioinformatics
            and experimental validation
  JOURNAL   Aging (Albany NY) 15 (12), 5611-5649 (2023)
   PUBMED   37338527
  REMARK    GeneRIF: Identifying the role of NUDCD1 in human tumors from
            clinical and molecular mechanisms: a study based on comprehensive
            bioinformatics and experimental validation.
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Feng,W.M., Gong,H., Wang,Y.C., Wang,Y., Xue,T., Zhang,T. and Cui,G.
  TITLE     NudCD1 as a prognostic marker in colorectal cancer and its role in
            the upregulation of cellular spindle assembly checkpoint genes and
            LIS1 pathways
  JOURNAL   BMC Cancer 22 (1), 981 (2022)
   PUBMED   36104662
  REMARK    GeneRIF: NudCD1 as a prognostic marker in colorectal cancer and its
            role in the upregulation of cellular spindle assembly checkpoint
            genes and LIS1 pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 554)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 554)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 554)
  AUTHORS   Taipale,M., Tucker,G., Peng,J., Krykbaeva,I., Lin,Z.Y., Larsen,B.,
            Choi,H., Berger,B., Gingras,A.C. and Lindquist,S.
  TITLE     A quantitative chaperone interaction network reveals the
            architecture of cellular protein homeostasis pathways
  JOURNAL   Cell 158 (2), 434-448 (2014)
   PUBMED   25036637
REFERENCE   7  (residues 1 to 554)
  AUTHORS   Wang,Q., Li,M., Wang,Y., Zhang,Y., Jin,S., Xie,G., Liu,Z., Wang,S.,
            Zhang,H., Shen,L. and Ge,H.
  TITLE     RNA interference targeting CML66, a novel tumor antigen, inhibits
            proliferation, invasion and metastasis of HeLa cells
  JOURNAL   Cancer Lett 269 (1), 127-138 (2008)
   PUBMED   18534745
  REMARK    GeneRIF: CML66 may play an oncogenic role in ways of favoring tumor
            cells proliferation, invasion and metastasis-associated with
            multiple pathways.
REFERENCE   8  (residues 1 to 554)
  AUTHORS   Jin,S., Wang,Y., Zhang,Y., Zhang,H.Z., Wang,S.J., Tang,J.Q.,
            Chen,H.J. and Ge,H.L.
  TITLE     Humoral immune responses against tumor-associated antigen OVA66
            originally defined by serological analysis of recombinant cDNA
            expression libraries and its potentiality in cellular immunity
  JOURNAL   Cancer Sci 99 (8), 1670-1678 (2008)
   PUBMED   18754882
  REMARK    GeneRIF: study identified a novel gene, OVA66, which was expressed
            significantly higher in cancer patients than normal controls; IgG
            level against OVA66 was significantly elevated in the serum of
            cancer patients from different histological types of cancer [OVA66]
REFERENCE   9  (residues 1 to 554)
  AUTHORS   Yan,Y., Phan,L., Yang,F., Talpaz,M., Yang,Y., Xiong,Z., Ng,B.,
            Timchenko,N.A., Wu,C.J., Ritz,J., Wang,H. and Yang,X.F.
  TITLE     A novel mechanism of alternative promoter and splicing regulates
            the epitope generation of tumor antigen CML66-L
  JOURNAL   J Immunol 172 (1), 651-660 (2004)
   PUBMED   14688378
  REMARK    GeneRIF: An alternative promoter (CML66-S short isoform) has been
            identified in combination with alternative splicing as a novel
            mechanism for regulation of the epitope generation of a self-tumor
            antigen.
REFERENCE   10 (residues 1 to 554)
  AUTHORS   Yang,X.F., Wu,C.J., McLaughlin,S., Chillemi,A., Wang,K.S.,
            Canning,C., Alyea,E.P., Kantoff,P., Soiffer,R.J., Dranoff,G. and
            Ritz,J.
  TITLE     CML66, a broadly immunogenic tumor antigen, elicits a humoral
            immune response associated with remission of chronic myelogenous
            leukemia
  JOURNAL   Proc Natl Acad Sci U S A 98 (13), 7492-7497 (2001)
   PUBMED   11416219
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC021237.5, AK307663.1 and BC043406.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR and 5'
            CDS, compared to variant 1, resulting in a protein (isoform 2) with
            a shorter, distinct N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK307663.1, AF521133.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q23.1"
     Protein         1..554
                     /product="nudC domain-containing protein 1 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="chronic myelogenous leukemia tumor antigen 66; nudC
                     domain-containing protein 1; tumor antigen CML66"
                     /calculated_mol_wt=63371
     Region          249..332
                     /region_name="p23_NUDCD1_like"
                     /note="p23_NUDCD1: p23-like NUD (nuclear distribution)
                     C-like domain found in human NUD (nuclear distribution) C
                     domain-containing protein 1, NUDCD1 (also known as CML66),
                     and similar proteins. NUDCD1/CML66 is a broadly
                     immunogenic tumor associated antigen; cd06493"
                     /db_xref="CDD:107242"
     CDS             1..554
                     /gene="NUDCD1"
                     /gene_synonym="CML66; OVA66"
                     /coded_by="NM_001128211.2:100..1764"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47910.1"
                     /db_xref="GeneID:84955"
                     /db_xref="HGNC:HGNC:24306"
                     /db_xref="MIM:606109"
ORIGIN      
        1 mlylqgwsmp avaevklrdd qytlehmhaf gmynylhcds wyqdsvyyid tlgrimnltv
       61 mldtalgkpr evfrlptdlt acdnrlcasi hfssstwvtl sdgtgrlyvi gtgergnsas
      121 ekweimfnee lgdpfiiihs isllnaeehs iatlllriek eeldmkgsgf yvslewvtis
      181 kknqdnkkye iikrdilrgk svphyaaiep dgnglmivsy ksltfvqagq dleenmdedi
      241 sekikeplyy wqqteddltv tirlpedstk ediqiqflpd hinivlkdhq flegklyssi
      301 dhesstwiik esnsleisli kknegltwpe lvigdkqgel irdsaqcaai aerlmhltse
      361 elnpnpdkek ppcnaqelee cdiffeesss lcrfdgntlk tthvvnlgsn qylfsvivdp
      421 kempcfclrh dvdallwqph sskqddmweh iatfnalgyv qaskrdkkff acapnysyaa
      481 lceclrrvfi yrqpapmstv lynrkegrqv gqvakqqvas letndpilgf qatnerlfvl
      541 ttknlflikv nten
//
LOCUS       NP_005165                297 aa            linear   PRI 21-NOV-2025
DEFINITION  ATP synthase F(1) complex subunit gamma, mitochondrial isoform H
            (heart) precursor [Homo sapiens].
ACCESSION   NP_005165
VERSION     NP_005165.1
DBSOURCE    REFSEQ: accession NM_005174.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Pecina,P., Nuskova,H., Karbanova,V., Kaplanova,V., Mracek,T. and
            Houstek,J.
  TITLE     Role of the mitochondrial ATP synthase central stalk subunits gamma
            and delta in the activity and assembly of the mammalian enzyme
  JOURNAL   Biochim Biophys Acta Bioenerg 1859 (5), 374-381 (2018)
   PUBMED   29499186
  REMARK    GeneRIF: Both gamma and delta subunits silenced cells displayed
            decreased ATP synthase function - lowered rate of ADP-stimulated
            respiration, a two-fold increased sensitivity of respiration to
            inhibitor oligomycin, and impaired utilization of mitochondrial
            membrane potential for ADP phosphorylation.
REFERENCE   6  (residues 1 to 297)
  AUTHORS   Elston,T., Wang,H. and Oster,G.
  TITLE     Energy transduction in ATP synthase
  JOURNAL   Nature 391 (6666), 510-513 (1998)
   PUBMED   9461222
REFERENCE   7  (residues 1 to 297)
  AUTHORS   Abrahams,J.P., Leslie,A.G., Lutter,R. and Walker,J.E.
  TITLE     Structure at 2.8 A resolution of F1-ATPase from bovine heart
            mitochondria
  JOURNAL   Nature 370 (6491), 621-628 (1994)
   PUBMED   8065448
REFERENCE   8  (residues 1 to 297)
  AUTHORS   Jabs,E.W., Thomas,P.J., Bernstein,M., Coss,C., Ferreira,G.C. and
            Pedersen,P.L.
  TITLE     Chromosomal localization of genes required for the terminal steps
            of oxidative metabolism: alpha and gamma subunits of ATP synthase
            and the phosphate carrier
  JOURNAL   Hum Genet 93 (5), 600-602 (1994)
   PUBMED   8168843
REFERENCE   9  (residues 1 to 297)
  AUTHORS   Matsuda,C., Endo,H., Ohta,S. and Kagawa,Y.
  TITLE     Gene structure of human mitochondrial ATP synthase gamma-subunit.
            Tissue specificity produced by alternative RNA splicing
  JOURNAL   J Biol Chem 268 (33), 24950-24958 (1993)
   PUBMED   8227057
REFERENCE   10 (residues 1 to 297)
  AUTHORS   Boyer,P.D., Cross,R.L. and Momsen,W.
  TITLE     A new concept for energy coupling in oxidative phosphorylation
            based on a molecular explanation of the oxygen exchange reactions
  JOURNAL   Proc Natl Acad Sci U S A 70 (10), 2837-2839 (1973)
   PUBMED   4517936
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ893894.1, D16563.1 and
            BC026049.1.
            
            Summary: This gene encodes a subunit of mitochondrial ATP synthase.
            Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an
            electrochemical gradient of protons across the inner membrane
            during oxidative phosphorylation. ATP synthase is composed of two
            linked multi-subunit complexes: the soluble catalytic core, F1, and
            the membrane-spanning component, Fo, comprising the proton channel.
            The catalytic portion of mitochondrial ATP synthase consists of 5
            different subunits (alpha, beta, gamma, delta, and epsilon)
            assembled with a stoichiometry of 3 alpha, 3 beta, and a single
            representative of the other 3. The proton channel consists of three
            main subunits (a, b, c). This gene encodes the gamma subunit of the
            catalytic core. Alternatively spliced transcript variants encoding
            different isoforms have been identified. This gene also has a
            pseudogene on chromosome 14. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks a segment in the coding
            region compared to variant 1. The resulting isoform (H), also known
            as a heart type isoform, contains a shorter and distinct C-terminus
            compared to isoform L.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D16563.1, BG751390.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p14"
     Protein         1..297
                     /product="ATP synthase F(1) complex subunit gamma,
                     mitochondrial isoform H (heart) precursor"
                     /EC_number="3.6.1.14"
                     /note="mitochondrial ATP synthase, gamma subunit 1; ATP
                     synthase gamma chain, mitochondrial; ATP synthase subunit
                     gamma, mitochondrial; F-ATPase gamma subunit; ATP
                     synthase, H+ transporting, mitochondrial F1 complex, gamma
                     polypeptide 1; ATP synthase F(1) complex subunit gamma,
                     mitochondrial"
                     /calculated_mol_wt=30051
     transit_peptide 1..25
                     /note="Mitochondrion; propagated from UniProtKB/Swiss-Prot
                     (P36542.1)"
                     /calculated_mol_wt=2848
     Region          26..297
                     /region_name="ATPsyn_F1gamma"
                     /note="ATP synthase, F1 gamma subunit; TIGR01146"
                     /db_xref="CDD:273469"
     Site            order(29,34,40,44,47..48,50..51,54..55,100,102..105,
                     135..136,139..140,143,260,263..264,267,273,276..277,
                     279..280,283..284,287,289..294)
                     /site_type="other"
                     /note="core domain interface [polypeptide binding]"
                     /db_xref="CDD:213394"
     Site            39
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q91VR2; propagated from
                     UniProtKB/Swiss-Prot (P36542.1)"
     Site            55
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P36542.1)"
     Site            order(65..66,68..69,72,75..76,225,228..229,232)
                     /site_type="other"
                     /note="delta subunit interface [polypeptide binding]"
                     /db_xref="CDD:213394"
     Site            115
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q91VR2; propagated from
                     UniProtKB/Swiss-Prot (P36542.1)"
     Site            order(138,150..155,228,231..232)
                     /site_type="other"
                     /note="epsilon subunit interface [polypeptide binding]"
                     /db_xref="CDD:213394"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P36542.1)"
     Site            154
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P36542.1)"
     Site            197
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P36542.1)"
     CDS             1..297
                     /gene="ATP5F1C"
                     /gene_synonym="ATP5C; ATP5C1; ATP5CL1"
                     /coded_by="NM_005174.4:32..925"
                     /note="isoform H (heart) precursor is encoded by
                     transcript variant 2"
                     /db_xref="CCDS:CCDS7081.1"
                     /db_xref="GeneID:509"
                     /db_xref="HGNC:HGNC:833"
                     /db_xref="MIM:108729"
ORIGIN      
        1 mfsragvagl sawtlqpqwi qvrnmatlkd itrrlksikn iqkitksmkm vaaakyarae
       61 relkpariyg lgslalyeka dikgpedkkk hlligvssdr glcgaihssi akqmksevat
      121 ltaagkevml vgigdkirgi lyrthsdqfl vafkevgrkp ptfgdasvia lellnsgyef
      181 degsiifnkf rsvisyktee kpifslntva sadsmsiydd idadvlqnyq eynlaniiyy
      241 slkesttseq sarmtamdna sknasemidk ltltfnrtrq avitkeliei isgaaal
//
LOCUS       NP_037414                806 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase UHRF1 isoform 2 [Homo sapiens].
ACCESSION   NP_037414
VERSION     NP_037414.3
DBSOURCE    REFSEQ: accession NM_013282.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 806)
  AUTHORS   Tiedemann,R.L., Hrit,J., Du,Q., Wiseman,A.K., Eden,H.E.,
            Dickson,B.M., Kong,X., Chomiak,A.A., Vaughan,R.M., Tibben,B.M.,
            Hebert,J.M., David,Y., Zhou,W., Baylin,S.B., Jones,P.A., Clark,S.J.
            and Rothbart,S.B.
  TITLE     UHRF1 ubiquitin ligase activity supports the maintenance of
            low-density CpG methylation
  JOURNAL   Nucleic Acids Res 52 (22), 13733-13756 (2024)
   PUBMED   39607687
REFERENCE   2  (residues 1 to 806)
  AUTHORS   Tan,L., Yin,T., Xiang,H., Wang,L., Mudgal,P., Chen,J., Ding,Y.,
            Wang,G., Lim,B.J.W., Huang,Y., Huang,D., Liang,Y., Alexander,P.B.,
            Xiang,K., Wang,E., Yan,C., Ma,Z., Tan,M., Li,Q.J. and Wang,X.F.
  TITLE     Aberrant cytoplasmic expression of UHRF1 restrains the
            MHC-I-mediated anti-tumor immune response
  JOURNAL   Nat Commun 15 (1), 8569 (2024)
   PUBMED   39362877
  REMARK    GeneRIF: Aberrant cytoplasmic expression of UHRF1 restrains the
            MHC-I-mediated anti-tumor immune response.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 806)
  AUTHORS   Unoki,M., Uemura,S., Fujimoto,A. and Sasaki,H.
  TITLE     The maternal protein NLRP5 stabilizes UHRF1 in the cytoplasm:
            implication for the pathogenesis of multilocus imprinting
            disturbance
  JOURNAL   Hum Mol Genet 33 (18), 1575-1583 (2024)
   PUBMED   38868925
  REMARK    GeneRIF: The maternal protein NLRP5 stabilizes UHRF1 in the
            cytoplasm: implication for the pathogenesis of multilocus
            imprinting disturbance.
REFERENCE   4  (residues 1 to 806)
  AUTHORS   Shiraishi,N., Konuma,T., Chiba,Y., Hokazono,S., Nakamura,N.,
            Islam,M.H., Nakanishi,M., Nishiyama,A. and Arita,K.
  TITLE     Structure of human DPPA3 bound to the UHRF1 PHD finger reveals its
            functional and structural differences from mouse DPPA3
  JOURNAL   Commun Biol 7 (1), 746 (2024)
   PUBMED   38898124
  REMARK    GeneRIF: Structure of human DPPA3 bound to the UHRF1 PHD finger
            reveals its functional and structural differences from mouse DPPA3.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 806)
  AUTHORS   Bronner,C., Krifa,M. and Mousli,M.
  TITLE     Increasing role of UHRF1 in the reading and inheritance of the
            epigenetic code as well as in tumorogenesis
  JOURNAL   Biochem Pharmacol 86 (12), 1643-1649 (2013)
   PUBMED   24134914
  REMARK    GeneRIF: reviews the principles how UHRF1 acts as an epigenetic
            reader and discusses the properties of UHRF1 to be a biomarker as
            well as a therapeutic target
            Review article
REFERENCE   6  (residues 1 to 806)
  AUTHORS   Muto,M., Fujimori,A., Nenoi,M., Daino,K., Matsuda,Y., Kuroiwa,A.,
            Kubo,E., Kanari,Y., Utsuno,M., Tsuji,H., Ukai,H., Mita,K.,
            Takahagi,M. and Tatsumi,K.
  TITLE     Isolation and Characterization of a Novel Human Radiosusceptibility
            Gene, NP95
  JOURNAL   Radiat Res 166 (5), 723-733 (2006)
   PUBMED   17067204
  REMARK    GeneRIF: These findings collectively indicate that the human NP95
            gene is the functional orthologue of the murine Np95 gene.
REFERENCE   7  (residues 1 to 806)
  AUTHORS   Citterio,E., Papait,R., Nicassio,F., Vecchi,M., Gomiero,P.,
            Mantovani,R., Di Fiore,P.P. and Bonapace,I.M.
  TITLE     Np95 is a histone-binding protein endowed with ubiquitin ligase
            activity
  JOURNAL   Mol Cell Biol 24 (6), 2526-2535 (2004)
   PUBMED   14993289
REFERENCE   8  (residues 1 to 806)
  AUTHORS   Mousli,M., Hopfner,R., Abbady,A.Q., Monte,D., Jeanblanc,M.,
            Oudet,P., Louis,B. and Bronner,C.
  TITLE     ICBP90 belongs to a new family of proteins with an expression that
            is deregulated in cancer cells
  JOURNAL   Br J Cancer 89 (1), 120-127 (2003)
   PUBMED   12838312
  REMARK    GeneRIF: ICBP90 expression altered in cancer cell lines and
            upregulated by E2F-1 overexpression, with efficiency depending on
            cancer status of cell line
REFERENCE   9  (residues 1 to 806)
  AUTHORS   Hopfner,R., Mousli,M., Garnier,J.M., Redon,R., du Manoir,S.,
            Chatton,B., Ghyselinck,N., Oudet,P. and Bronner,C.
  TITLE     Genomic structure and chromosomal mapping of the gene coding for
            ICBP90, a protein involved in the regulation of the topoisomerase
            IIalpha gene expression
  JOURNAL   Gene 266 (1-2), 15-23 (2001)
   PUBMED   11290415
REFERENCE   10 (residues 1 to 806)
  AUTHORS   Hopfner,R., Mousli,M., Jeltsch,J.M., Voulgaris,A., Lutz,Y.,
            Marin,C., Bellocq,J.P., Oudet,P. and Bronner,C.
  TITLE     ICBP90, a novel human CCAAT binding protein, involved in the
            regulation of topoisomerase IIalpha expression
  JOURNAL   Cancer Res 60 (1), 121-128 (2000)
   PUBMED   10646863
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB177624.1, BC113875.1,
            AK074377.1, AC104525.4 and AK025578.1.
            
            On Sep 30, 2006 this sequence version replaced NP_037414.2.
            
            Summary: This gene encodes a member of a subfamily of RING-finger
            type E3 ubiquitin ligases. The protein binds to specific DNA
            sequences, and recruits a histone deacetylase to regulate gene
            expression. Its expression peaks at late G1 phase and continues
            during G2 and M phases of the cell cycle. It plays a major role in
            the G1/S transition by regulating topoisomerase IIalpha and
            retinoblastoma gene expression, and functions in the p53-dependent
            DNA damage checkpoint. It is regarded as a hub protein for the
            integration of epigenetic information. This gene is up-regulated in
            various cancers, and it is therefore considered to be a therapeutic
            target. Multiple transcript variants encoding different isoforms
            have been found for this gene. A related pseudogene exists on
            chromosome 12. [provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            initiates translation from an alternate start codon, compared to
            variant 1. The resulting isoform (2) has a distinct N-terminus and
            is longer than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB177624.1, AF274048.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..806
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..806
                     /product="E3 ubiquitin-protein ligase UHRF1 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="inverted CCAAT box-binding protein of 90 kDa;
                     nuclear zinc finger protein Np95; RING finger protein 106;
                     transcription factor ICBP90; E3 ubiquitin-protein ligase
                     UHRF1; ubiquitin-like PHD and RING finger
                     domain-containing protein 1; nuclear phosphoprotein 95;
                     nuclear protein 95; RING-type E3 ubiquitin transferase
                     UHRF1; inverted CCAAT box binding protein 90"
                     /calculated_mol_wt=90970
     Region          14..87
                     /region_name="Ubl_UHRF1"
                     /note="ubiquitin-like (Ubl) domain found in ubiquitin-like
                     PHD and RING finger domain-containing protein 1(UHRF1);
                     cd17122"
                     /db_xref="CDD:340642"
     Region          145..297
                     /region_name="TTD"
                     /note="Tandem tudor domain within UHRF1; pfam12148"
                     /db_xref="CDD:463474"
     Region          330..376
                     /region_name="PHD_UHRF1"
                     /note="PHD finger found in ubiquitin-like PHD and RING
                     finger domain-containing protein 1 (UHRF1); cd15616"
                     /db_xref="CDD:277088"
     Site            order(330,337,340..341,343..347,349..350,366..371)
                     /site_type="other"
                     /note="histone H3 binding site [polypeptide binding]"
                     /db_xref="CDD:277088"
     Region          430..597
                     /region_name="SAD_SRA"
                     /note="SAD/SRA domain; pfam02182"
                     /db_xref="CDD:460476"
     Region          727..806
                     /region_name="RING-HC_UHRF1"
                     /note="RING finger, HC subclass, found in ubiquitin-like
                     PHD and RING finger domain-containing protein 1 (UHRF1);
                     cd16769"
                     /db_xref="CDD:438425"
     CDS             1..806
                     /gene="UHRF1"
                     /gene_synonym="hNP95; hUHRF1; huNp95; ICBP90; Np95;
                     RNF106; TDRD22"
                     /coded_by="NM_013282.5:481..2901"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS74262.1"
                     /db_xref="GeneID:29128"
                     /db_xref="HGNC:HGNC:12556"
                     /db_xref="MIM:607990"
ORIGIN      
        1 mgvfavppls adtmwiqvrt mdgrqthtvd slsrltkvee lrrkiqelfh vepglqrlfy
       61 rgkqmedght lfdyevrlnd tiqllvrqsl vlphstkerd selsdtdsgc clgqsesdks
      121 sthgeaaaet dsrpadedmw detelglykv neyvdardtn mgawfeaqvv rvtrkapsrd
      181 epcsstsrpa leedviyhvk yddypengvv qmnsrdvrar artiikwqdl evgqvvmlny
      241 npdnpkergf wydaeisrkr etrtarelya nvvlgddsln dcriifvdev fkierpgegs
      301 pmvdnpmrrk sgpsckhckd dvnrlcrvca chlcggrqdp dkqlmcdecd mafhiycldp
      361 plssvpsede wycpecrnda sevvlagerl reskkkakma satsssqrdw gkgmacvgrt
      421 kectivpsnh ygpipgipvg tmwrfrvqvs esgvhrphva gihgrsndga yslvlaggye
      481 ddvdhgnfft ytgsggrdls gnkrtaeqsc dqkltntnra lalncfapin dqegaeakdw
      541 rsgkpvrvvr nvkggknsky apaegnrydg iykvvkywpe kgksgflvwr yllrrdddep
      601 gpwtkegkdr ikklgltmqy pegylealan rerekenskr eeeeqqeggf asprtgkgkw
      661 krksagggps ragsprrtsk ktkvepyslt aqqsslired ksnaklwnev laslkdrpas
      721 gspfqlflsk veetfqcicc qelvfrpitt vcqhnvckdc ldrsfraqvf scpacrydlg
      781 rsyamqvnqp lqtvlnqlfp gygngr
//
LOCUS       NP_694593                482 aa            linear   PRI 21-NOV-2025
DEFINITION  tyrosine-protein kinase Fyn isoform c [Homo sapiens].
ACCESSION   NP_694593
VERSION     NP_694593.1
DBSOURCE    REFSEQ: accession NM_153048.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Zhu,J., Shi,L. and Su,Y.
  TITLE     FYN as an emerging biological biomarker for prognosis and potential
            therapeutic target in LGG
  JOURNAL   Neurol Res 46 (9), 787-795 (2024)
   PUBMED   38752708
  REMARK    GeneRIF: FYN as an emerging biological biomarker for prognosis and
            potential therapeutic target in LGG.
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Yang,K., Belrose,J., Trepanier,C.H., Lei,G., Jackson,M.F. and
            MacDonald,J.F.
  TITLE     Fyn, a potential target for Alzheimer's disease
  JOURNAL   J Alzheimers Dis 27 (2), 243-252 (2011)
   PUBMED   21799250
  REMARK    GeneRIF: [review] Recent evidence cited in this review suggests
            that alterations in Fyn, a Src family kinase, might contribute to
            Alzheimer's disease pathogenesis.
            Review article
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Saito,Y.D., Jensen,A.R., Salgia,R. and Posadas,E.M.
  TITLE     Fyn: a novel molecular target in cancer
  JOURNAL   Cancer 116 (7), 1629-1637 (2010)
   PUBMED   20151426
  REMARK    Review article
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Rigley,K., Slocombe,P., Proudfoot,K., Wahid,S., Mandair,K. and
            Bebbington,C.
  TITLE     Human p59fyn(T) regulates OKT3-induced calcium influx by a
            mechanism distinct from PIP2 hydrolysis in Jurkat T cells
  JOURNAL   J Immunol 154 (3), 1136-1145 (1995)
   PUBMED   7822789
  REMARK    Erratum:[J Immunol 1995 Apr 15;154(8):4223]
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Gout,I., Dhand,R., Panayotou,G., Fry,M.J., Hiles,I., Otsu,M. and
            Waterfield,M.D.
  TITLE     Expression and characterization of the p85 subunit of the
            phosphatidylinositol 3-kinase complex and a related p85 beta
            protein by using the baculovirus expression system
  JOURNAL   Biochem J 288 (Pt 2) (Pt 2), 395-405 (1992)
   PUBMED   1334406
REFERENCE   7  (residues 1 to 482)
  AUTHORS   Thomas,P.M. and Samelson,L.E.
  TITLE     The glycophosphatidylinositol-anchored Thy-1 molecule interacts
            with the p60fyn protein tyrosine kinase in T cells
  JOURNAL   J Biol Chem 267 (17), 12317-12322 (1992)
   PUBMED   1351058
REFERENCE   8  (residues 1 to 482)
  AUTHORS   Brickell,P.M.
  TITLE     The p60c-src family of protein-tyrosine kinases: structure,
            regulation, and function
  JOURNAL   Crit Rev Oncog 3 (4), 401-446 (1992)
   PUBMED   1384720
  REMARK    Review article
REFERENCE   9  (residues 1 to 482)
  AUTHORS   Kawakami,T., Pennington,C.Y. and Robbins,K.C.
  TITLE     Isolation and oncogenic potential of a novel human src-like gene
  JOURNAL   Mol Cell Biol 6 (12), 4195-4201 (1986)
   PUBMED   3099169
REFERENCE   10 (residues 1 to 482)
  AUTHORS   Semba,K., Nishizawa,M., Miyajima,N., Yoshida,M.C., Sukegawa,J.,
            Yamanashi,Y., Sasaki,M., Yamamoto,T. and Toyoshima,K.
  TITLE     yes-related protooncogene, syn, belongs to the protein-tyrosine
            kinase family
  JOURNAL   Proc Natl Acad Sci U S A 83 (15), 5459-5463 (1986)
   PUBMED   3526330
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC032496.1, Z97989.1 and
            BP391373.1.
            
            Summary: This gene is a member of the protein-tyrosine kinase
            oncogene family. It encodes a membrane-associated tyrosine kinase
            that has been implicated in the control of cell growth. The protein
            associates with the p85 subunit of phosphatidylinositol 3-kinase
            and interacts with the fyn-binding protein. Alternatively spliced
            transcript variants encoding distinct isoforms exist. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR, and
            lacks an alternate in-frame exon in the central coding region,
            compared to variant 1, resulting in an isoform (c) that is shorter
            than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032496.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..482
                     /product="tyrosine-protein kinase Fyn isoform c"
                     /EC_number="2.7.10.2"
                     /note="tyrosine-protein kinase Fyn; src-like kinase; c-syn
                     protooncogene; tyrosine kinase p59fyn(T); OKT3-induced
                     calcium influx regulator; src/yes-related novel;
                     proto-oncogene Syn; proto-oncogene c-Fyn; FYN oncogene
                     related to SRC, FGR, YES"
                     /calculated_mol_wt=54383
     Region          85..140
                     /region_name="SH3_Fyn_Yrk"
                     /note="Src homology 3 domain of Fyn and Yrk Protein
                     Tyrosine Kinases; cd12006"
                     /db_xref="CDD:212939"
     Site            order(91,93,96..97,100,116..119,132,134,136..137)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212939"
     Site            order(93,96..100,116,119,132)
                     /site_type="other"
                     /note="SAP interaction site [polypeptide binding]"
                     /db_xref="CDD:212939"
     Region          145..245
                     /region_name="SH2_Src_Fyn"
                     /note="Src homology 2 (SH2) domain found in Fyn; cd10368"
                     /db_xref="CDD:198231"
     Site            order(156,176,178..181,186,202,204,237)
                     /site_type="other"
                     /note="autoinhibitory site [polypeptide binding]"
                     /db_xref="CDD:198231"
     Site            order(156,176,202,204)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198231"
     Site            order(203,231)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198231"
     Region          231..467
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     CDS             1..482
                     /gene="FYN"
                     /gene_synonym="p59-FYN; SLK; SYN"
                     /coded_by="NM_153048.4:54..1502"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS5096.1"
                     /db_xref="GeneID:2534"
                     /db_xref="HGNC:HGNC:4037"
                     /db_xref="MIM:137025"
ORIGIN      
        1 mgcvqckdke atklteerdg slnqssgyry gtdptpqhyp sfgvtsipny nnfhaaggqg
       61 ltvfggvnss shtgtlrtrg gtgvtlfval ydyeartedd lsfhkgekfq ilnssegdww
      121 earslttget gyipsnyvap vdsiqaeewy fgklgrkdae rqllsfgnpr gtflireset
      181 tkgayslsir dwddmkgdhv khykirkldn ggyyittraq fetlqqlvqh ysgtwngntk
      241 vaiktlkpgt mspesfleea qimkklkhdk lvqlyavvse epiyivteym nkgslldflk
      301 dgegralklp nlvdmaaqva agmayiermn yihrdlrsan ilvgnglick iadfglarli
      361 edneytarqg akfpikwtap eaalygrfti ksdvwsfgil ltelvtkgrv pypgmnnrev
      421 leqvergyrm pcpqdcpisl helmihcwkk dpeerptfey lqsfledyft atepqyqpge
      481 nl
//
LOCUS       NP_001290372             286 aa            linear   PRI 21-NOV-2025
DEFINITION  protein HEXIM2 isoform 1 [Homo sapiens].
ACCESSION   NP_001290372
VERSION     NP_001290372.1
DBSOURCE    REFSEQ: accession NM_001303443.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Walker,F.M., Sobral,L.M., Danis,E., Sanford,B., Donthula,S.,
            Balakrishnan,I., Wang,D., Pierce,A., Karam,S.D., Kargar,S.,
            Serkova,N.J., Foreman,N.K., Venkataraman,S., Dowell,R., Vibhakar,R.
            and Dahl,N.A.
  TITLE     Rapid P-TEFb-dependent transcriptional reorganization underpins the
            glioma adaptive response to radiotherapy
  JOURNAL   Nat Commun 15 (1), 4616 (2024)
   PUBMED   38816355
  REMARK    GeneRIF: Rapid P-TEFb-dependent transcriptional reorganization
            underpins the glioma adaptive response to radiotherapy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Li,Q., Price,J.P., Byers,S.A., Cheng,D., Peng,J. and Price,D.H.
  TITLE     Analysis of the large inactive P-TEFb complex indicates that it
            contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two
            P-TEFb molecules containing Cdk9 phosphorylated at threonine 186
  JOURNAL   J Biol Chem 280 (31), 28819-28826 (2005)
   PUBMED   15965233
  REMARK    GeneRIF: Positive transcription elongation factor b regulates
            eukaryotic gene expression at the level of elongation and is
            controlled by the reversible association with HEXIM2.
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Fraldi,A., Varrone,F., Napolitano,G., Michels,A.A., Majello,B.,
            Bensaude,O. and Lania,L.
  TITLE     Inhibition of Tat activity by the HEXIM1 protein
  JOURNAL   Retrovirology 2, 42 (2005)
   PUBMED   15992410
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 286)
  AUTHORS   Byers,S.A., Price,J.P., Cooper,J.J., Li,Q. and Price,D.H.
  TITLE     HEXIM2, a HEXIM1-related protein, regulates positive transcription
            elongation factor b through association with 7SK
  JOURNAL   J Biol Chem 280 (16), 16360-16367 (2005)
   PUBMED   15713662
  REMARK    GeneRIF: utilization of HEXIM1 or HEXIM2 to bind and inhibit P-TEFb
            can be differentially regulated in vivo.
REFERENCE   9  (residues 1 to 286)
  AUTHORS   Yik,J.H., Chen,R., Pezda,A.C. and Zhou,Q.
  TITLE     Compensatory contributions of HEXIM1 and HEXIM2 in maintaining the
            balance of active and inactive positive transcription elongation
            factor b complexes for control of transcription
  JOURNAL   J Biol Chem 280 (16), 16368-16376 (2005)
   PUBMED   15713661
  REMARK    GeneRIF: HEXIM2 can functionally and quantitatively compensate for
            the loss of HEXIM1
REFERENCE   10 (residues 1 to 286)
  AUTHORS   Michels,A.A., Nguyen,V.T., Fraldi,A., Labas,V., Edwards,M.,
            Bonnet,F., Lania,L. and Bensaude,O.
  TITLE     MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a
            transcription-dependent manner
  JOURNAL   Mol Cell Biol 23 (14), 4859-4869 (2003)
   PUBMED   12832472
  REMARK    Erratum:[Mol Cell Biol. 2003 Dec;23(24):9405]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI829844.1, CN425800.1 and
            AK056946.1.
            
            Summary: This gene encodes a member of the HEXIM family of
            proteins. This protein is a component of the 7SK small nuclear
            ribonucleoprotein. This protein has been found to negatively
            regulate the kinase activity of the cyclin-dependent kinase P-TEFb,
            which phosphorylates multiple target proteins to promote
            transcriptional elongation. This gene is located approximately 7 kb
            downstream from related family member HEXIM1 on chromosome 17.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2015].
            
            Transcript Variant: This variant (9) differs in the 5' UTR compared
            to variant 1. Variants 1-9 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1286611.1,
                                           SRR14243140.7140715.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..286
                     /product="protein HEXIM2 isoform 1"
                     /note="hexamethylene-bis-acetamide-inducible transcript 2;
                     hexamethylene bis-acetamide inducible 2; MAQ1 paralog;
                     protein HEXIM2; hexamethylene bis-acetamide-inducible
                     protein 2; hexamethylene bisacetamide inducible 2"
                     /calculated_mol_wt=32287
     Region          1..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Region          102..227
                     /region_name="HEXIM"
                     /note="Hexamethylene bis-acetamide-inducible protein;
                     pfam15313"
                     /db_xref="CDD:464638"
     Region          140..143
                     /region_name="Interaction with P-TEFb"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Region          216..>271
                     /region_name="YabA"
                     /note="Regulator of replication initiation timing YabA
                     [Replication, recombination and repair]; COG4467"
                     /db_xref="CDD:443564"
     Region          226..286
                     /region_name="Interaction with CCNT1, HEXIM1 and HEXIM2.
                     /evidence=ECO:0000269|PubMed:15713661,
                     ECO:0000269|PubMed:15994294"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     CDS             1..286
                     /gene="HEXIM2"
                     /gene_synonym="L3"
                     /coded_by="NM_001303443.2:258..1118"
                     /note="isoform 1 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS11496.1"
                     /db_xref="GeneID:124790"
                     /db_xref="HGNC:HGNC:28591"
                     /db_xref="MIM:615695"
ORIGIN      
        1 mmatpnqtac naespvalee aktsgapgsp qtpperhdsg gslpltprme shsededlag
       61 avgglgwnsr sprtqspggc saeavlarkk hrrrpskrkr hwrpylelsw aekqqrderq
      121 sqrasrvree mfakgqpvap ynttqflmnd rdpeepnldv phgishpgss geseagdsdg
      181 rgrahgefqr kdfsetyerf hteslqgrsk qelvrdylel ekrlsqaeee trrlqqlqac
      241 tgqqscrqve elaaevqrlr tenqrlrqen qmwnregcrc deepgt
//
LOCUS       NP_001278014             463 aa            linear   PRI 21-NOV-2025
DEFINITION  adhesion G protein-coupled receptor A1 isoform 2 [Homo sapiens].
ACCESSION   NP_001278014
VERSION     NP_001278014.1
DBSOURCE    REFSEQ: accession NM_001291085.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Krasnova,O.A., Kulakova,K.A., Sopova,J.V., Smirnov,E.Y.,
            Silonov,S.A., Lomert,E.V., Bystrova,O.A., Martynova,M.G. and
            Neganova,I.E.
  TITLE     Essential Role of Adhesion GPCR, GPR123, for Human Pluripotent Stem
            Cells and Reprogramming towards Pluripotency
  JOURNAL   Cells 12 (2), 304 (2023)
   PUBMED   36672239
  REMARK    GeneRIF: Essential Role of Adhesion GPCR, GPR123, for Human
            Pluripotent Stem Cells and Reprogramming towards Pluripotency.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Liu,Y., Wang,G., Cui,T. and Lv,L.
  TITLE     Adhesion GPR123 is an indicator for recurrence and prognosis in
            bladder cancer
  JOURNAL   Genes Genomics 43 (11), 1317-1325 (2021)
   PUBMED   33945147
  REMARK    GeneRIF: Adhesion GPR123 is an indicator for recurrence and
            prognosis in bladder cancer.
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Mills,J.D., Kavanagh,T., Kim,W.S., Chen,B.J., Kawahara,Y.,
            Halliday,G.M. and Janitz,M.
  TITLE     Unique transcriptome patterns of the white and grey matter
            corroborate structural and functional heterogeneity in the human
            frontal lobe
  JOURNAL   PLoS One 8 (10), e78480 (2013)
   PUBMED   24194939
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Lagerstrom,M.C., Rabe,N., Haitina,T., Kalnina,I., Hellstrom,A.R.,
            Klovins,J., Kullander,K. and Schioth,H.B.
  TITLE     The evolutionary history and tissue mapping of GPR123: specific CNS
            expression pattern predominantly in thalamic nuclei and regions
            containing large pyramidal cells
  JOURNAL   J Neurochem 100 (4), 1129-1142 (2007)
   PUBMED   17212699
  REMARK    GeneRIF: Studies indicate that the orthologs of GP123 in mouse and
            rat play a role in the regulation of neuronal signaling pathways.
REFERENCE   6  (residues 1 to 463)
  AUTHORS   Bjarnadottir,T.K., Geirardsdottir,K., Ingemansson,M., Mirza,M.A.,
            Fredriksson,R. and Schioth,H.B.
  TITLE     Identification of novel splice variants of Adhesion G
            protein-coupled receptors
  JOURNAL   Gene 387 (1-2), 38-48 (2007)
   PUBMED   17056209
REFERENCE   7  (residues 1 to 463)
  AUTHORS   Bjarnadottir,T.K., Fredriksson,R., Hoglund,P.J., Gloriam,D.E.,
            Lagerstrom,M.C. and Schioth,H.B.
  TITLE     The human and mouse repertoire of the adhesion family of
            G-protein-coupled receptors
  JOURNAL   Genomics 84 (1), 23-33 (2004)
   PUBMED   15203201
REFERENCE   8  (residues 1 to 463)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   9  (residues 1 to 463)
  AUTHORS   Vassilatis,D.K., Hohmann,J.G., Zeng,H., Li,F., Ranchalis,J.E.,
            Mortrud,M.T., Brown,A., Rodriguez,S.S., Weller,J.R., Wright,A.C.,
            Bergmann,J.E. and Gaitanaris,G.A.
  TITLE     The G protein-coupled receptor repertoires of human and mouse
  JOURNAL   Proc Natl Acad Sci U S A 100 (8), 4903-4908 (2003)
   PUBMED   12679517
REFERENCE   10 (residues 1 to 463)
  AUTHORS   Fredriksson,R., Gloriam,D.E., Hoglund,P.J., Lagerstrom,M.C. and
            Schioth,H.B.
  TITLE     There exist at least 30 human G-protein-coupled receptors with long
            Ser/Thr-rich N-termini
  JOURNAL   Biochem Biophys Res Commun 301 (3), 725-734 (2003)
   PUBMED   12565841
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB058731.1, AL445199.37 and
            BC044247.1.
            
            Summary: This gene encodes a protein that belongs to the adhesion
            family of G-protein-coupled receptors. Members of this family
            function in several sensory systems and regulate blood pressure,
            immune responses, food intake and development. A similar protein in
            rodents is thought to play a role in in the regulation of neuronal
            signaling pathways. Several alternatively spliced transcript
            variants of this gene have been described, but the full-length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Mar 2014].
            
            Transcript Variant: This variant (2) represents the use of an
            alternate promoter, contains a different 5' structure and uses a
            downstream start codon compared to variant 1. The resulting protein
            (isoform 2) has a shorter N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AY255564.1, SRR1660809.390789.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2145743, SAMEA2154665 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.3"
     Protein         1..463
                     /product="adhesion G protein-coupled receptor A1 isoform
                     2"
                     /note="probable G-protein coupled receptor 123"
                     /calculated_mol_wt=49970
     Region          <1..226
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          37..53
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:410628"
     Region          75..98
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:410628"
     Region          159..181
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:410628"
     Region          188..213
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:410628"
     CDS             1..463
                     /gene="ADGRA1"
                     /gene_synonym="GPR123"
                     /coded_by="NM_001291085.2:130..1521"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS76362.1"
                     /db_xref="GeneID:84435"
                     /db_xref="HGNC:HGNC:13838"
                     /db_xref="MIM:612302"
ORIGIN      
        1 mlwigvtarn iykqvtkkap lcldtdqppy prqpllrfyl vsggvpfiic gvtaatnirn
       61 ygtededtay cwmawepslg afygpaaiit lvtcvyflgt yvqlrrhpgr ryelrtqpee
      121 qrrlatpegg rgirpgtppa hdapgasvlq nehsfqaqlr aaaftlflft atwafgalav
      181 sqghfldmvf sclygafcvt lglfvlihhc akredvwqcw waccpprkda hpaldangaa
      241 lgraaclhsp glgqprgfah ppgpckmtnl qaaqghascl spatpccakm hcepltadea
      301 hvhlqeegaf ghdphlhgcl qgrtkppyfs rhpaeepeya yhipssldgs prssrtdspp
      361 ssldgpagth tlacctqgdp fpmvtqpegs dgspalyscp tqpgreaalg pghlemlrrt
      421 qslpfggpsq nglpkgklle glpfgtdgtg nirtgpwkne ttv
//
LOCUS       NP_001265471             218 aa            linear   PRI 21-NOV-2025
DEFINITION  dixin isoform c [Homo sapiens].
ACCESSION   NP_001265471
VERSION     NP_001265471.1
DBSOURCE    REFSEQ: accession NM_001278542.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Huang,C.Q., Yang,P., Liu,J., Wang,Y.P., Hao,D.D. and Yang,X.
  TITLE     Circular RNA circ_0000423 promotes gastric cancer cell
            proliferation, migration and invasion via the
            microR-582-3p/Disheveled-Axin domain containing 1 axis
  JOURNAL   Bioengineered 12 (2), 12755-12766 (2021)
   PUBMED   34898351
  REMARK    GeneRIF: Circular RNA circ_0000423 promotes gastric cancer cell
            proliferation, migration and invasion via the
            microR-582-3p/Disheveled-Axin domain containing 1 axis.
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Chen,Z.F., Wang,Y., Sun,L.L., Ding,S.Y. and Jinag,H.
  TITLE     LncRNA SNHG20 enhances the progression of oral squamous cell
            carcinoma by regulating the miR-29a/DIXDC1/Wnt regulatory axis
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (10), 5436-5445 (2020)
   PUBMED   32495922
  REMARK    GeneRIF: LncRNA SNHG20 enhances the progression of oral squamous
            cell carcinoma by regulating the miR-29a/DIXDC1/Wnt regulatory
            axis.
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Wu,Y., Jing,X., Ma,X., Wu,Y., Ding,X., Fan,W. and Fan,M.
  TITLE     DIXDC1 co-localizes and interacts with gamma-tubulin in HEK293
            cells
  JOURNAL   Cell Biol Int 33 (6), 697-701 (2009)
   PUBMED   19375513
  REMARK    GeneRIF: The GFP-tag fused DIXDC1 exogenously expressed co-localize
            with gamma-tubulin both at interphase and mitotic phase in the
            centrosomes.
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Jing,X.T., Wu,H.T., Wu,Y., Ma,X., Liu,S.H., Wu,Y.R., Ding,X.F.,
            Peng,X.Z., Qiang,B.Q., Yuan,J.G., Fan,W.H. and Fan,M.
  TITLE     DIXDC1 promotes retinoic acid-induced neuronal differentiation and
            inhibits gliogenesis in P19 cells
  JOURNAL   Cell Mol Neurobiol 29 (1), 55-67 (2009)
   PUBMED   18629627
  REMARK    GeneRIF: DIXDC1 might play an important role during neurogenesis,
            overexpression of DIXDC1 in embryonic carcinoma P19 cells promoted
            neuronal differentiation, and inhibited gliogenesis induced by
            retinoic acid.
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Camargo,L.M., Collura,V., Rain,J.C., Mizuguchi,K., Hermjakob,H.,
            Kerrien,S., Bonnert,T.P., Whiting,P.J. and Brandon,N.J.
  TITLE     Disrupted in Schizophrenia 1 Interactome: evidence for the close
            connectivity of risk genes and a potential synaptic basis for
            schizophrenia
  JOURNAL   Mol Psychiatry 12 (1), 74-86 (2007)
   PUBMED   17043677
REFERENCE   8  (residues 1 to 218)
  AUTHORS   Wang,X., Zheng,L., Zeng,Z., Zhou,G., Chien,J., Qian,C.,
            Vasmatzis,G., Shridhar,V., Chen,L. and Liu,W.
  TITLE     DIXDC1 isoform, l-DIXDC1, is a novel filamentous actin-binding
            protein
  JOURNAL   Biochem Biophys Res Commun 347 (1), 22-30 (2006)
   PUBMED   16814745
  REMARK    GeneRIF: Thus, our data provide the first evidence that l-DIXDC1
            may act as a novel branching component in the Wnt signaling pathway
            targeting both beta-catenin-TCF complex for gene expression and
            cytoskeleton for regulating dynamics of actin filaments.
REFERENCE   9  (residues 1 to 218)
  AUTHORS   Wong,C.K., Luo,W., Deng,Y., Zou,H., Ye,Z. and Lin,S.C.
  TITLE     The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal
            kinase activation by Axin and dishevelled through distinct
            mechanisms
  JOURNAL   J Biol Chem 279 (38), 39366-39373 (2004)
   PUBMED   15262978
  REMARK    GeneRIF: Ccd1 inhibits Axin-mediated JNK activation by
            simultaneously adopting two distinct mechanisms, one through
            conformational changes that disallow MEKK1 binding and the other
            via direct sequestration of MEKK4.
REFERENCE   10 (residues 1 to 218)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     KIAA1735 gene on human chromosome 11q23.1 encodes a novel protein
            with myosine-tail homologous domain and C-terminal DIX domain
  JOURNAL   Int J Oncol 23 (1), 145-150 (2003)
   PUBMED   12792787
  REMARK    GeneRIF: KIAA1735 maps to human chromosome 11q23.1 and encodes a
            novel protein with a myosine-tail homologous domain and C-terminal
            DIX domain
            GeneRIF: MTHDIX (KIAA1735) protein consists of Myosine-tail
            homologous (MTH) domain and C-terminal DIX domain.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY037299.1, BC048294.1 and
            AP000907.6.
            
            Summary: The protein encoded by this gene is a positive regulator
            of the Wnt signaling pathway. The encoded protein is found
            associated with gamma tubulin at the centrosome. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (3) contains multiple differences
            in the UTRs and coding region, compared to variant 1, including the
            lack of multiple 3' coding exons. The encoded isoform (c) is
            shorter and has distinct N- and C- termini, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1678456.1,
                                           SRR18074969.997655.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.1"
     Protein         1..218
                     /product="dixin isoform c"
                     /note="dixin; coiled-coil protein DIX1"
                     /calculated_mol_wt=24182
     Region          21..127
                     /region_name="CH_DIXDC1"
                     /note="calponin homology (CH) domain found in Dixin and
                     similar proteins; cd21213"
                     /db_xref="CDD:409062"
     Site            order(21,25,79,81..82,85..86,88,97..105,110,112..113,
                     115..116,119..120,123)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409062"
     CDS             1..218
                     /gene="DIXDC1"
                     /gene_synonym="CCD1"
                     /coded_by="NM_001278542.2:110..766"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS60957.1"
                     /db_xref="GeneID:85458"
                     /db_xref="HGNC:HGNC:23695"
                     /db_xref="MIM:610493"
ORIGIN      
        1 mgtqvvmrfn nsllptepsq qlqayvawvn aqlkkrpavk pvqdlrqdlr dgvilaylie
       61 ivageklsgv qlspgnqqem knnvekvlqf vaskkirmhq tsakdivdgn lksimrlvla
      121 laahfkpgss rtvnqgrdsr aplqshrphc atavaqgaaa aladvchdms rsgrdvfryr
      181 qrnssmdeei enpywsvral vqqyegqqrs psesscsr
//
LOCUS       NP_001333786             837 aa            linear   PRI 21-NOV-2025
DEFINITION  tuftelin-interacting protein 11 isoform 1 [Homo sapiens].
ACCESSION   NP_001333786
VERSION     NP_001333786.1
DBSOURCE    REFSEQ: accession NM_001346857.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Chen,J., Wu,M., Yang,Y., Ruan,C., Luo,Y., Song,L., Wu,T., Huang,J.,
            Yang,B. and Liu,T.
  TITLE     TFIP11 promotes replication fork reversal to preserve genome
            stability
  JOURNAL   Nat Commun 15 (1), 1262 (2024)
   PUBMED   38341452
  REMARK    GeneRIF: TFIP11 promotes replication fork reversal to preserve
            genome stability.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 837)
  AUTHORS   Duchemin,A., O'Grady,T., Hanache,S., Mereau,A., Thiry,M.,
            Wacheul,L., Michaux,C., Perpete,E., Hervouet,E., Peixoto,P.,
            Ernst,F.G.M., Audic,Y., Dequiedt,F., Lafontaine,D.L.J. and
            Mottet,D.
  TITLE     DHX15-independent roles for TFIP11 in U6 snRNA modification,
            U4/U6.U5 tri-snRNP assembly and pre-mRNA splicing fidelity
  JOURNAL   Nat Commun 12 (1), 6648 (2021)
   PUBMED   34789764
  REMARK    GeneRIF: DHX15-independent roles for TFIP11 in U6 snRNA
            modification, U4/U6.U5 tri-snRNP assembly and pre-mRNA splicing
            fidelity.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 837)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 837)
  AUTHORS   Wang,H.J., Tannukit,S., Wen,X., Shapiro,J.L., Snead,M.L. and
            Paine,M.L.
  TITLE     Using the yeast two-hybrid assay to discover protein partners for
            the leucine-rich amelogenin peptide and for tuftelin-interacting
            protein 11
  JOURNAL   Eur J Oral Sci 114 Suppl 1, 276-9 (2006)
   PUBMED   16674698
REFERENCE   7  (residues 1 to 837)
  AUTHORS   Wen,X., Lei,Y.P., Zhou,Y.L., Okamoto,C.T., Snead,M.L. and
            Paine,M.L.
  TITLE     Structural organization and cellular localization of
            tuftelin-interacting protein 11 (TFIP11)
  JOURNAL   Cell Mol Life Sci 62 (9), 1038-1046 (2005)
   PUBMED   15868102
  REMARK    GeneRIF: TFIP11 is a novel splicing factor and transfected
            TFIP11-GFP fusion protein was found to locate in a novel subnuclear
            TFIP body.
REFERENCE   8  (residues 1 to 837)
  AUTHORS   Jurica,M.S. and Moore,M.J.
  TITLE     Pre-mRNA splicing: awash in a sea of proteins
  JOURNAL   Mol Cell 12 (1), 5-14 (2003)
   PUBMED   12887888
  REMARK    Review article
REFERENCE   9  (residues 1 to 837)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   10 (residues 1 to 837)
  AUTHORS   Paine,C.T., Paine,M.L., Luo,W., Okamoto,C.T., Lyngstadaas,S.P. and
            Snead,M.L.
  TITLE     A tuftelin-interacting protein (TIP39) localizes to the apical
            secretory pole of mouse ameloblasts
  JOURNAL   J Biol Chem 275 (29), 22284-22292 (2000)
   PUBMED   10806191
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z95115.1, Z99714.2 and
            AI468631.1.
            
            Summary: This gene encodes a protein component of the spliceosome
            that promotes the release of the lariat-intron during late-stage
            splicing through the recruitment of a pre-mRNA splicing factor
            called DEAH-box helicase 15. The encoded protein contains a G-patch
            domain, a hallmark of RNA-processing proteins, that binds DEAH-box
            helicase 15. This protein contains an atypical nuclear localization
            sequence as well as a nuclear speckle-targeting sequence, enabling
            it to localize to distinct speckled regions within the cell
            nucleus. Polymorphisms in this gene are associated with dental
            caries suggesting a role in amelogenesis. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Nov
            2016].
            
            Transcript Variant: This variant (3) uses an alternate splice site
            in the 5' UTR, compared to variant 1. Variants 1-6 encode the same
            isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1723080.1,
                                           SRR14038191.4201292.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.1"
     Protein         1..837
                     /product="tuftelin-interacting protein 11 isoform 1"
                     /note="septin and tuftelin-interacting protein 1;
                     sip1/tuftelin interacting protein"
                     /calculated_mol_wt=96689
     Region          1..50
                     /region_name="Required for interaction with DHX15.
                     /evidence=ECO:0000269|PubMed:19103666"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBB9.1)"
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBB9.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5U2Y6; propagated from
                     UniProtKB/Swiss-Prot (Q9UBB9.1)"
     Region          23..104
                     /region_name="TIP_N"
                     /note="Tuftelin interacting protein N terminal; pfam12457"
                     /db_xref="CDD:463593"
     Region          53..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBB9.1)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBB9.1)"
     Region          85..133
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBB9.1)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBB9.1)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UBB9.1)"
     Region          149..193
                     /region_name="G-patch"
                     /note="G-patch domain; pfam01585"
                     /db_xref="CDD:396249"
     Region          179..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBB9.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBB9.1)"
     Region          397..666
                     /region_name="GCFC"
                     /note="GC-rich sequence DNA-binding factor-like protein;
                     pfam07842"
                     /db_xref="CDD:400273"
     Region          700..705
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBB9.1)"
     Region          710..734
                     /region_name="Required for nuclear speckle localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBB9.1)"
     CDS             1..837
                     /gene="TFIP11"
                     /gene_synonym="bK445C9.6; NTR1; Spp382; STIP; STIP-1;
                     TIP39"
                     /coded_by="NM_001346857.2:288..2801"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS13838.1"
                     /db_xref="GeneID:24144"
                     /db_xref="HGNC:HGNC:17165"
                     /db_xref="MIM:612747"
ORIGIN      
        1 mslshlyrdg egriddddde renfeitdwd lqnefnpnrq rhwqtkeeat ygvwaerdsd
       61 derpsfggkr ardysapvnf isaglkkgaa eeaeledsdd eekpvkqddf pkdfgprklk
      121 tggnfkpsqk gfaggtksfm dfgswerhtk gigqkllqkm gyvpgrglgk naqgiinpie
      181 akqrkgkgav gaygserttq smqdfpvvds eeeaeeefqk elsqwrkdps gskkkpkysy
      241 ktveelkakg riskkltapq kelsqvkvid mtgreqkvyy sysqishkhn vpddglplqs
      301 qqlpqsgkea kapgfalpel ehnlqllidl teqeiiqndr qlqyerdmvv nlfhelekmt
      361 evldheervi snlskvlemv eecerrmqpd csnpltldec arifetlqdk yyeeyrmsdr
      421 vdlavaivyp lmkeyfkewd plkdctygte iiskwkslle ndqllshggq dlsadafhrl
      481 iwevwmpfvr nivtqwqprn cdpmvdflds wvhiipvwil dnildqlifp klqkevenwn
      541 pltdtvpihs wihpwlplmq arleplyspi rsklssalqk whpsdssakl ilqpwkdvft
      601 pgsweafmvk nivpklgmcl gelvinphqq hmdafywvid wegmisvssl vgllekhffp
      661 kwlqvlcswl snspnyeeit kwylgwksmf sdqvlahpsv kdkfnealdi mnravssnvg
      721 aymqpgaren iaylthterr kdfqyeamqe rreaenmaqr gigvaassvp mnfkdlietk
      781 aeehnivfmp vigkrhegkq lytfgriviy idrgvvfvqg ektwvptslq slidmak
//
LOCUS       NP_001238968             249 aa            linear   PRI 21-NOV-2025
DEFINITION  ras-related protein Rab-5C isoform b [Homo sapiens].
ACCESSION   NP_001238968
VERSION     NP_001238968.1
DBSOURCE    REFSEQ: accession NM_001252039.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Wang,X., Cheng,J., Shen,L., Chen,M., Sun,K., Li,J., Li,M., Ma,C.
            and Wei,L.
  TITLE     Rab5c promotes RSV and ADV replication by autophagy in respiratory
            epithelial cells
  JOURNAL   Virus Res 341, 199324 (2024)
   PUBMED   38242290
  REMARK    GeneRIF: Rab5c promotes RSV and ADV replication by autophagy in
            respiratory epithelial cells.
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Koop,K., Yuan,W., Tessadori,F., Rodriguez-Polanco,W.R., Grubbs,J.,
            Zhang,B., Osmond,M., Graham,G., Sawyer,S., Conboy,E., Vetrini,F.,
            Treat,K., Ploski,R., Pienkowski,V.M., Klosowska,A., Fieg,E.,
            Krier,J., Mallebranche,C., Alban,Z., Aldinger,K.A., Ritter,D.,
            Macnamara,E., Sullivan,B., Herriges,J., Alaimo,J.T., Helbig,C.,
            Ellis,C.A., van Eyk,C., Gecz,J., Farrugia,D., Osei-Owusu,I.,
            Ades,L., van den Boogaard,M.J., Fuchs,S., Bakker,J., Duran,K.,
            Dawson,Z.D., Lindsey,A., Huang,H., Baldridge,D., Silverman,G.A.,
            Grant,B.D., Raizen,D., van Haaften,G., Pak,S.C., Rehmann,H.,
            Schedl,T. and van Hasselt,P.
  CONSRTM   Undiagnosed Diseases Network
  TITLE     Macrocephaly and developmental delay caused by missense variants in
            RAB5C
  JOURNAL   Hum Mol Genet 32 (21), 3063-3077 (2023)
   PUBMED   37552066
  REMARK    GeneRIF: Macrocephaly and developmental delay caused by missense
            variants in RAB5C.
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Wen,X., Yan,Z., Du,J., Dai,J., Liu,M., Wang,X. and Wang,N.
  TITLE     Effects of miR-145 targeting rab5c and regulating MAPK / ERK
            signaling pathway on proliferation and invasion of thyroid
            papillary carcinoma cells
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (1), 44-47 (2023)
   PUBMED   37213158
  REMARK    GeneRIF: Effects of miR-145 targeting rab5c and regulating MAPK /
            ERK signaling pathway on proliferation and invasion of thyroid
            papillary carcinoma cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Li,X., Chen,X., Fu,C., Xie,M. and Ouyang,S.
  TITLE     Long Non-Coding RNA BCAR4 Promotes Oxaliplatin Resistance in
            Colorectal Cancer by Modulating miR-484-3p/RAB5C Expression
  JOURNAL   Chemotherapy 68 (3), 119-130 (2023)
   PUBMED   36657426
  REMARK    GeneRIF: Long Non-Coding RNA BCAR4 Promotes Oxaliplatin Resistance
            in Colorectal Cancer by Modulating miR-484-3p/RAB5C Expression.
REFERENCE   6  (residues 1 to 249)
  AUTHORS   Clemens,D.L., Lee,B.Y. and Horwitz,M.A.
  TITLE     Deviant expression of Rab5 on phagosomes containing the
            intracellular pathogens Mycobacterium tuberculosis and Legionella
            pneumophila is associated with altered phagosomal fate
  JOURNAL   Infect Immun 68 (5), 2671-2684 (2000)
   PUBMED   10768959
REFERENCE   7  (residues 1 to 249)
  AUTHORS   Bucci,C., Chiariello,M., Lattero,D., Maiorano,M. and Bruni,C.B.
  TITLE     Interaction cloning and characterization of the cDNA encoding the
            human prenylated rab acceptor (PRA1)
  JOURNAL   Biochem Biophys Res Commun 258 (3), 657-662 (1999)
   PUBMED   10329441
REFERENCE   8  (residues 1 to 249)
  AUTHORS   Alvarez-Dominguez,C. and Stahl,P.D.
  TITLE     Interferon-gamma selectively induces Rab5a synthesis and processing
            in mononuclear cells
  JOURNAL   J Biol Chem 273 (51), 33901-33904 (1998)
   PUBMED   9852039
REFERENCE   9  (residues 1 to 249)
  AUTHORS   Han,H.J., Sudo,K., Inazawa,J. and Nakamura,Y.
  TITLE     Isolation and mapping of a human gene (RABL) encoding a small
            GTP-binding protein homologous to the Ras-related RAB gene
  JOURNAL   Cytogenet Cell Genet 73 (1-2), 137-139 (1996)
   PUBMED   8646882
REFERENCE   10 (residues 1 to 249)
  AUTHORS   Albertsen,H.M., Smith,S.A., Mazoyer,S., Fujimoto,E., Stevens,J.,
            Williams,B., Rodriguez,P., Cropp,C.S., Slijepcevic,P., Carlson,M.
            et al.
  TITLE     A physical map and candidate genes in the BRCA1 region on
            chromosome 17q12-21
  JOURNAL   Nat Genet 7 (4), 472-479 (1994)
   PUBMED   7951316
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP222378.1, AK310234.1, AC003104.1 and BC106039.1.
            
            Summary: Members of the Rab protein family are small GTPases of the
            Ras superfamily that are thought to ensure fidelity in the process
            of docking and/or fusion of vesicles with their correct acceptor
            compartment (Han et al., 1996 [PubMed 8646882]).[supplied by OMIM,
            Nov 2010].
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            contains an alternate exon and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (b) is longer and has a distinct N-terminus, compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.396694.1,
                                           SRR3476690.1172186.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..249
                     /product="ras-related protein Rab-5C isoform b"
                     /EC_number="3.6.5.2"
                     /note="RAB5C, member of RAS oncogene family; ras-related
                     protein Rab-5C"
                     /calculated_mol_wt=26904
     Region          54..216
                     /region_name="Rab5_related"
                     /note="Rab-related GTPase family includes Rab5 and Rab22;
                     regulates early endosome fusion; cd01860"
                     /db_xref="CDD:206653"
     Site            54..56
                     /site_type="other"
                     /note="Rab subfamily motif 1 (RabSF1)"
                     /db_xref="CDD:206653"
     Site            61..68
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206653"
     Site            order(63..69,79..80,85..86,112,167..168,170,197..199)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206653"
     Site            order(69..80,84..85)
                     /site_type="other"
                     /note="Rab subfamily motif 2 (RabSF2)"
                     /db_xref="CDD:206653"
     Site            order(79,84..92)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206653"
     Site            order(84,88..95,102,104)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206653"
     Site            86
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206653"
     Site            order(87..88,90,108..109,116,118,120..122)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206653"
     Site            87..91
                     /site_type="other"
                     /note="Rab family motif 1 (RabF1)"
                     /db_xref="CDD:206653"
     Site            order(89..91,93,115,122..123)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:206653"
     Site            104..108
                     /site_type="other"
                     /note="Rab family motif 2 (RabF2)"
                     /db_xref="CDD:206653"
     Site            109..112
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206653"
     Site            order(112,114..124)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206653"
     Site            115..120
                     /site_type="other"
                     /note="Rab family motif 3 (RabF3)"
                     /db_xref="CDD:206653"
     Site            123..124
                     /site_type="other"
                     /note="Rab family motif 4 (RabF4)"
                     /db_xref="CDD:206653"
     Site            132..137
                     /site_type="other"
                     /note="Rab family motif 5 (RabF5)"
                     /db_xref="CDD:206653"
     Site            159..164
                     /site_type="other"
                     /note="Rab subfamily motif 3 (RabSF3)"
                     /db_xref="CDD:206653"
     Site            167..170
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206653"
     Site            197..199
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206653"
     Site            213..215
                     /site_type="other"
                     /note="Rab subfamily motif 4 (RabSF4)"
                     /db_xref="CDD:206653"
     CDS             1..249
                     /gene="RAB5C"
                     /gene_synonym="L1880; RAB5CL; RAB5L; RABL"
                     /coded_by="NM_001252039.2:303..1052"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58551.1"
                     /db_xref="GeneID:5878"
                     /db_xref="HGNC:HGNC:9785"
                     /db_xref="MIM:604037"
ORIGIN      
        1 melswrspsp lsaslhstsp hphalwttta gramagrgga arpngpaagn kicqfklvll
       61 gesavgkssl vlrfvkgqfh eyqestigaa fltqtvcldd ttvkfeiwdt agqeryhsla
      121 pmyyrgaqaa ivvyditntd tfaraknwvk elqrqaspni vialagnkad laskravefq
      181 eaqayaddns llfmetsakt amnvneifma iakklpknep qnatgapgrn rgvdlqennp
      241 asrsqccsn
//
LOCUS       NP_602307                670 aa            linear   PRI 21-NOV-2025
DEFINITION  solute carrier organic anion transporter family member 1A2 isoform
            1 [Homo sapiens].
ACCESSION   NP_602307
VERSION     NP_602307.1
DBSOURCE    REFSEQ: accession NM_134431.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Flogel,S., Tust,M., Boussettaoui,S., Fischer,D. and Grundemann,D.
  TITLE     Enhancing transporter activity in heterologous expression systems
            with SAHA: a 2500-times more potent and odorless alternative to
            butyrate
  JOURNAL   FEBS Open Bio 15 (6), 906-913 (2025)
   PUBMED   40052353
REFERENCE   2  (residues 1 to 670)
  AUTHORS   Kataoka,H., Akiyoshi,T., Uchida,Y., Imaoka,A., Terasaki,T. and
            Ohtani,H.
  TITLE     The Effects of N-Glycosylation on the Expression and Transport
            Activity of OATP1A2 and OATP2B1
  JOURNAL   J Pharm Sci 113 (5), 1376-1384 (2024)
   PUBMED   38432624
  REMARK    GeneRIF: The Effects of N-Glycosylation on the Expression and
            Transport Activity of OATP1A2 and OATP2B1.
REFERENCE   3  (residues 1 to 670)
  AUTHORS   Han,H., Akiyoshi,T., Morita,T., Kataoka,H., Katayama,K., Yajima,K.,
            Imaoka,A. and Ohtani,H.
  TITLE     Comparison of the transport kinetics of fexofenadine and its pH
            dependency among OATP1A2 genetic variants
  JOURNAL   Drug Metab Pharmacokinet 47, 100470 (2022)
   PUBMED   36116173
  REMARK    GeneRIF: Comparison of the transport kinetics of fexofenadine and
            its pH dependency among OATP1A2 genetic variants.
REFERENCE   4  (residues 1 to 670)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 670)
  AUTHORS   Hau,R.K., Klein,R.R., Wright,S.H. and Cherrington,N.J.
  TITLE     Localization of Xenobiotic Transporters Expressed at the Human
            Blood-Testis Barrier
  JOURNAL   Drug Metab Dispos 50 (6), 770-780 (2022)
   PUBMED   35307651
REFERENCE   6  (residues 1 to 670)
  AUTHORS   Kullak-Ublick,G.A., Fisch,T., Oswald,M., Hagenbuch,B., Meier,P.J.,
            Beuers,U. and Paumgartner,G.
  TITLE     Dehydroepiandrosterone sulfate (DHEAS): identification of a carrier
            protein in human liver and brain
  JOURNAL   FEBS Lett 424 (3), 173-176 (1998)
   PUBMED   9539145
REFERENCE   7  (residues 1 to 670)
  AUTHORS   Meier,P.J., Eckhardt,U., Schroeder,A., Hagenbuch,B. and Stieger,B.
  TITLE     Substrate specificity of sinusoidal bile acid and organic anion
            uptake systems in rat and human liver
  JOURNAL   Hepatology 26 (6), 1667-1677 (1997)
   PUBMED   9398014
  REMARK    Review article
REFERENCE   8  (residues 1 to 670)
  AUTHORS   Kullak-Ublick,G.A., Beuers,U., Fahney,C., Hagenbuch,B., Meier,P.J.
            and Paumgartner,G.
  TITLE     Identification and functional characterization of the promoter
            region of the human organic anion transporting polypeptide gene
  JOURNAL   Hepatology 26 (4), 991-997 (1997)
   PUBMED   9328325
REFERENCE   9  (residues 1 to 670)
  AUTHORS   Kullak-Ublick,G.A., Beuers,U., Meier,P.J., Domdey,H. and
            Paumgartner,G.
  TITLE     Assignment of the human organic anion transporting polypeptide
            (OATP) gene to chromosome 12p12 by fluorescence in situ
            hybridization
  JOURNAL   J Hepatol 25 (6), 985-987 (1996)
   PUBMED   9007731
REFERENCE   10 (residues 1 to 670)
  AUTHORS   Kullak-Ublick,G.A., Hagenbuch,B., Stieger,B., Schteingart,C.D.,
            Hofmann,A.F., Wolkoff,A.W. and Meier,P.J.
  TITLE     Molecular and functional characterization of an organic anion
            transporting polypeptide cloned from human liver
  JOURNAL   Gastroenterology 109 (4), 1274-1282 (1995)
   PUBMED   7557095
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006559.6 and AC022224.22.
            
            Summary: This gene encodes a sodium-independent transporter which
            mediates cellular uptake of organic ions in the liver. Its
            substrates include bile acids, bromosulphophthalein, and some
            steroidal compounds. The protein is a member of the SLC21A family
            of solute carriers. Alternative splicing of this gene results in
            multiple transcript variants. [provided by RefSeq, Dec 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein. The
            translation of this protein may be modulated by multiple upstream
            ORFs that are present in the 5' UTR.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF279784.1, SRR14038194.1031296.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2148874,
                                           SAMEA2150585 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..670
                     /product="solute carrier organic anion transporter family
                     member 1A2 isoform 1"
                     /note="organic anion transporting polypeptide A; solute
                     carrier family 21 (organic anion transporter), member 3;
                     sodium-independent organic anion transporter; OATP-1;
                     solute carrier family 21 member 3; organic
                     anion-transporting polypeptide 1"
                     /calculated_mol_wt=74014
     Region          1..625
                     /region_name="oat"
                     /note="sodium-independent organic anion transporter;
                     TIGR00805"
                     /db_xref="CDD:273279"
     Site            21..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            60..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            87..111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            124
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P46721.1)"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P46721.1)"
     Site            156..184
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            204..224
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            243..267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            312..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            354..377
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            382..405
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            412
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P46721.1)"
     Site            419
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P46721.1)"
     Site            514..536
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            546..571
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     Site            606..623
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P46721.1)"
     CDS             1..670
                     /gene="SLCO1A2"
                     /gene_synonym="OATP; OATP-A; OATP1A2; SLC21A3"
                     /coded_by="NM_134431.5:790..2802"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8686.1"
                     /db_xref="GeneID:6579"
                     /db_xref="HGNC:HGNC:10956"
                     /db_xref="MIM:602883"
ORIGIN      
        1 mgetekriet hrirclsklk mfllaitcaf vsktlsgsym nsmltqierq fniptslvgf
       61 ingsfeignl lliifvsyfg tklhrpimig igcvvmglgc flkslphflm nqyeyestvs
      121 vsgnlssnsf lcmengtqil rptqdpsect kevkslmwvy vlvgnivrgm getpilplgi
      181 syiedfakfe nsplyiglve tgaiigplig lllasfcanv yvdtgfvntd dliitptdtr
      241 wvgawwfgfl icagvnvlta ipffflpntl pkegletnad iiknenedkq keevkkekyg
      301 itkdflpfmk slscnpiyml filvsviqfn afvnmisfmp kyleqqygis ssdaiflmgi
      361 ynlppicigy iigglimkkf kitvkqaahi gcwlslleyl lyflsflmtc enssvvgint
      421 syegipqdly vendifadcn vdcncpskiw dpvcgnngls ylsaclagce tsigtginmv
      481 fqncsciqts gnssavlglc dkgpdcslml qyflilsams sfiyslaaip gymvllrcmk
      541 seekslgvgl htfctrvfag ipapiyfgal mdstclhwgt lkcgesgacr iydsttfryi
      601 ylglpaalrg ssfvpaliil illrkchlpg enassgteli etkvkgkene ckdiyqkstv
      661 lkddelktkl
//
LOCUS       NP_001362677             370 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform zzz [Homo sapiens].
ACCESSION   NP_001362677
VERSION     NP_001362677.1
DBSOURCE    REFSEQ: accession NM_001375748.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 370)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 370)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 370)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 370)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 370)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.650545.1,
                                           SRR18074969.1574290.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..370
                     /product="abl interactor 2 isoform zzz"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=40647
     Region          19..82
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          309..369
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(317,319,322,326,344..345,358,360..361)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..370
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375748.1:340..1452"
                     /note="isoform zzz is encoded by transcript variant 83"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 mldiqasqlr rmessinhis qtvdihkekv arreigiltt nkntsrthki iapanlerpv
       61 ryirkpidyt ilddighgvk vstqnmkmgg lprttpptqk ppsppmsgkg tlgrhspyrt
      121 lepvrppvvp ndyvpsptrn mapsqqspvr tasvnqrnrt ysssgssggs hpssrsssre
      181 nsgsgsvgvp iavptpspps vfpghpvqfy smnrpasrht pptiggslpy rrppsitsqt
      241 slqnqmnggp fysqnpdtpp ppppveepvf desppppppp edyeeeeaav veysdpyaee
      301 dppwaprsyl ekvvaiydyt kdkedelsfq egaiiyvikk nddgwyegvm ngvtglfpgn
      361 yvesimhyse
//
LOCUS       NP_001265202             688 aa            linear   PRI 21-NOV-2025
DEFINITION  SRSF protein kinase 2 isoform b precursor [Homo sapiens].
ACCESSION   NP_001265202
VERSION     NP_001265202.1
DBSOURCE    REFSEQ: accession NM_001278273.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Yip,R.P.H., Kwok,D.C.Y., Lai,L.T.F., Ho,S.M., Wong,I.C.K.,
            Chan,C.P., Lau,W.C.Y. and Ngo,J.C.K.
  TITLE     SRPK2 Mediates HBV Core Protein Phosphorylation and Capsid Assembly
            via Docking Interaction
  JOURNAL   PLoS Pathog 20 (2), e1011978 (2024)
   PUBMED   38324561
  REMARK    GeneRIF: SRPK2 Mediates HBV Core Protein Phosphorylation and Capsid
            Assembly via Docking Interaction.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 688)
  AUTHORS   Yang,Z. and Ding,W.X.
  TITLE     The pre-mRNA alternative splicing regulated by SRPK2: A new player
            in alcohol-associated liver disease?
  JOURNAL   Hepatology 78 (5), 1329-1331 (2023)
   PUBMED   37183907
  REMARK    GeneRIF: The pre-mRNA alternative splicing regulated by SRPK2: A
            new player in alcohol-associated liver disease?
REFERENCE   5  (residues 1 to 688)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 688)
  AUTHORS   Koizumi,J., Okamoto,Y., Onogi,H., Mayeda,A., Krainer,A.R. and
            Hagiwara,M.
  TITLE     The subcellular localization of SF2/ASF is regulated by direct
            interaction with SR protein kinases (SRPKs)
  JOURNAL   J Biol Chem 274 (16), 11125-11131 (1999)
   PUBMED   10196197
REFERENCE   7  (residues 1 to 688)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
REFERENCE   8  (residues 1 to 688)
  AUTHORS   Kuroyanagi,N., Onogi,H., Wakabayashi,T. and Hagiwara,M.
  TITLE     Novel SR-protein-specific kinase, SRPK2, disassembles nuclear
            speckles
  JOURNAL   Biochem Biophys Res Commun 242 (2), 357-364 (1998)
   PUBMED   9446799
REFERENCE   9  (residues 1 to 688)
  AUTHORS   Bedford,M.T., Chan,D.C. and Leder,P.
  TITLE     FBP WW domains and the Abl SH3 domain bind to a specific class of
            proline-rich ligands
  JOURNAL   EMBO J 16 (9), 2376-2383 (1997)
   PUBMED   9171351
REFERENCE   10 (residues 1 to 688)
  AUTHORS   Gui,J.F., Lane,W.S. and Fu,X.D.
  TITLE     A serine kinase regulates intracellular localization of splicing
            factors in the cell cycle
  JOURNAL   Nature 369 (6482), 678-682 (1994)
   PUBMED   8208298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC068547.1, AC004884.1, BC035214.1, AC005070.1 and BU632662.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (b)
            has a shorter and distinct N-terminus compared to isoform a.
            Variants 2, 3, and 4 all encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC068547.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.3"
     Protein         1..688
                     /product="SRSF protein kinase 2 isoform b precursor"
                     /EC_number="2.7.11.1"
                     /note="SFRS protein kinase 2; serine/arginine-rich
                     splicing factor kinase 2; SR protein kinase 2;
                     serine/threonine-protein kinase SRPK2; serine kinase
                     SRPK2; SR-protein-specific kinase 2; serine/arginine-rich
                     protein-specific kinase 2"
                     /calculated_mol_wt=77396
     mat_peptide     1..139
                     /product="SRSF protein kinase 2 N-terminal.
                     /id=PRO_0000414751"
                     /note="propagated from UniProtKB/Swiss-Prot (P78362.3)"
                     /calculated_mol_wt=15552
     Region          1..65
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78362.3)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Region          68..>256
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(87..90,93,95,108,110,146,166..169,214,218..219,221)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271119"
     Site            139..140
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3.
                     /evidence=ECO:0000269|PubMed:21056976; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     mat_peptide     140..688
                     /product="SRSF protein kinase 2 C-terminal.
                     /id=PRO_0000414752"
                     /note="propagated from UniProtKB/Swiss-Prot (P78362.3)"
                     /calculated_mol_wt=61993
     Region          239..277
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78362.3)"
     Region          329..444
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78362.3)"
     Region          <341..383
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P78362.3)"
     Site            403..404
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3.
                     /evidence=ECO:0000269|PubMed:21056976; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Region          469..501
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78362.3)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O54781; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O54781; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O54781; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O54781; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O54781; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:19592491; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Site            494
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P78362.3)"
     Region          <504..686
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P78362.3)"
     CDS             1..688
                     /gene="SRPK2"
                     /gene_synonym="SFRSK2"
                     /coded_by="NM_001278273.2:182..2248"
                     /note="isoform b precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS5735.1"
                     /db_xref="GeneID:6733"
                     /db_xref="HGNC:HGNC:11306"
                     /db_xref="MIM:602980"
ORIGIN      
        1 msvnseksss serpepqqka plvppppppp pppppplpdp tppepeeeil gsddeeqedp
       61 adyckggyhp vkigdlfngr yhvirklgwg hfstvwlcwd mqgkrfvamk vvksaqhyte
      121 taldeikllk cvresdpsdp nkdmvvqlid dfkisgmngi hvcmvfevlg hhllkwiiks
      181 nyqglpvrcv ksiirqvlqg ldylhskcki ihtdikpeni lmcvddayvr rmaaeatewq
      241 kagapppsgs avstapqqkp igkisknkkk klkkkqkrqa ellekrlqei eelereaerk
      301 iieenitsaa psndqdgeyc pevklkttgl eeaaeaetak dngeaedqee kedaekenie
      361 kdeddvdqel anidptwies pktnghieng pfsleqqldd edddeedcpn peeynldepn
      421 aesdytysss yeqfngelpn grhkipesqf pefstslfsg slepvacgsv lsegsplteq
      481 eesspshdrs rtvsasstgd lpkaktraad llvnpldprn adkirvkiad lgnacwvhkh
      541 ftediqtrqy rsievligag ystpadiwst acmafelatg dylfephsge dysrdedhia
      601 hiiellgsip rhfalsgkys reffnrrgel rhitklkpws lfdvlvekyg wphedaaqft
      661 dflipmlemv pekrasagec lrhpwlns
//
LOCUS       NP_689787                616 aa            linear   PRI 21-NOV-2025
DEFINITION  tetratricopeptide repeat protein 39B isoform 1 [Homo sapiens].
ACCESSION   NP_689787
VERSION     NP_689787.3
DBSOURCE    REFSEQ: accession NM_152574.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Steinthorsdottir,V., Thorleifsson,G., Aradottir,K., Feenstra,B.,
            Sigurdsson,A., Stefansdottir,L., Kristinsdottir,A.M., Zink,F.,
            Halldorsson,G.H., Munk Nielsen,N., Geller,F., Melbye,M.,
            Gudbjartsson,D.F., Geirsson,R.T., Thorsteinsdottir,U. and
            Stefansson,K.
  TITLE     Common variants upstream of KDR encoding VEGFR2 and in TTC39B
            associate with endometriosis
  JOURNAL   Nat Commun 7, 12350 (2016)
   PUBMED   27453397
  REMARK    GeneRIF: association of rs519664[T] in TTC39B on 9p22 with
            endometriosis, is reported.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Rodriguez,S., Gaunt,T.R., Guo,Y., Zheng,J., Barnes,M.R., Tang,W.,
            Danish,F., Johnson,A., Castillo,B.A., Li,Y.R., Hakonarson,H.,
            Buxbaum,S.G., Palmer,T., Tsai,M.Y., Lange,L.A., Ebrahim,S., Davey
            Smith,G., Lawlor,D.A., Folsom,A.R., Hoogeveen,R., Reiner,A.,
            Keating,B. and Day,I.N.
  TITLE     Lipids, obesity and gallbladder disease in women: insights from
            genetic studies using the cardiovascular gene-centric 50K SNP array
  JOURNAL   Eur J Hum Genet 24 (1), 106-112 (2016)
   PUBMED   25920552
  REMARK    GeneRIF: Two new polymorphisms associated with gall bladder disease
            and obesity in women have been identified, GCKR rs1260326, and
            TTC39B rs686030.
REFERENCE   6  (residues 1 to 616)
  AUTHORS   O'Seaghdha,C.M., Yang,Q., Glazer,N.L., Leak,T.S., Dehghan,A.,
            Smith,A.V., Kao,W.H., Lohman,K., Hwang,S.J., Johnson,A.D.,
            Hofman,A., Uitterlinden,A.G., Chen,Y.D., Brown,E.M.,
            Siscovick,D.S., Harris,T.B., Psaty,B.M., Coresh,J., Gudnason,V.,
            Witteman,J.C., Liu,Y.M., Kestenbaum,B.R., Fox,C.S. and Kottgen,A.
  CONSRTM   GEFOS Consortium
  TITLE     Common variants in the calcium-sensing receptor gene are associated
            with total serum calcium levels
  JOURNAL   Hum Mol Genet 19 (21), 4296-4303 (2010)
   PUBMED   20705733
REFERENCE   7  (residues 1 to 616)
  AUTHORS   Waterworth,D.M., Ricketts,S.L., Song,K., Chen,L., Zhao,J.H.,
            Ripatti,S., Aulchenko,Y.S., Zhang,W., Yuan,X., Lim,N., Luan,J.,
            Ashford,S., Wheeler,E., Young,E.H., Hadley,D., Thompson,J.R.,
            Braund,P.S., Johnson,T., Struchalin,M., Surakka,I., Luben,R.,
            Khaw,K.T., Rodwell,S.A., Loos,R.J., Boekholdt,S.M., Inouye,M.,
            Deloukas,P., Elliott,P., Schlessinger,D., Sanna,S., Scuteri,A.,
            Jackson,A., Mohlke,K.L., Tuomilehto,J., Roberts,R., Stewart,A.,
            Kesaniemi,Y.A., Mahley,R.W., Grundy,S.M., McArdle,W., Cardon,L.,
            Waeber,G., Vollenweider,P., Chambers,J.C., Boehnke,M.,
            Abecasis,G.R., Salomaa,V., Jarvelin,M.R., Ruokonen,A., Barroso,I.,
            Epstein,S.E., Hakonarson,H.H., Rader,D.J., Reilly,M.P.,
            Witteman,J.C., Hall,A.S., Samani,N.J., Strachan,D.P., Barter,P.,
            van Duijn,C.M., Kooner,J.S., Peltonen,L., Wareham,N.J.,
            McPherson,R., Mooser,V. and Sandhu,M.S.
  CONSRTM   Wellcome Trust Case Control Consortium
  TITLE     Genetic variants influencing circulating lipid levels and risk of
            coronary artery disease
  JOURNAL   Arterioscler Thromb Vasc Biol 30 (11), 2264-2276 (2010)
   PUBMED   20864672
REFERENCE   8  (residues 1 to 616)
  AUTHORS   Teslovich,T.M., Musunuru,K., Smith,A.V., Edmondson,A.C.,
            Stylianou,I.M., Koseki,M., Pirruccello,J.P., Ripatti,S.,
            Chasman,D.I., Willer,C.J., Johansen,C.T., Fouchier,S.W., Isaacs,A.,
            Peloso,G.M., Barbalic,M., Ricketts,S.L., Bis,J.C., Aulchenko,Y.S.,
            Thorleifsson,G., Feitosa,M.F., Chambers,J., Orho-Melander,M.,
            Melander,O., Johnson,T., Li,X., Guo,X., Li,M., Shin Cho,Y., Jin
            Go,M., Jin Kim,Y., Lee,J.Y., Park,T., Kim,K., Sim,X., Twee-Hee
            Ong,R., Croteau-Chonka,D.C., Lange,L.A., Smith,J.D., Song,K., Hua
            Zhao,J., Yuan,X., Luan,J., Lamina,C., Ziegler,A., Zhang,W.,
            Zee,R.Y., Wright,A.F., Witteman,J.C., Wilson,J.F., Willemsen,G.,
            Wichmann,H.E., Whitfield,J.B., Waterworth,D.M., Wareham,N.J.,
            Waeber,G., Vollenweider,P., Voight,B.F., Vitart,V.,
            Uitterlinden,A.G., Uda,M., Tuomilehto,J., Thompson,J.R., Tanaka,T.,
            Surakka,I., Stringham,H.M., Spector,T.D., Soranzo,N., Smit,J.H.,
            Sinisalo,J., Silander,K., Sijbrands,E.J., Scuteri,A., Scott,J.,
            Schlessinger,D., Sanna,S., Salomaa,V., Saharinen,J., Sabatti,C.,
            Ruokonen,A., Rudan,I., Rose,L.M., Roberts,R., Rieder,M.,
            Psaty,B.M., Pramstaller,P.P., Pichler,I., Perola,M., Penninx,B.W.,
            Pedersen,N.L., Pattaro,C., Parker,A.N., Pare,G., Oostra,B.A.,
            O'Donnell,C.J., Nieminen,M.S., Nickerson,D.A., Montgomery,G.W.,
            Meitinger,T., McPherson,R., McCarthy,M.I., McArdle,W., Masson,D.,
            Martin,N.G., Marroni,F., Mangino,M., Magnusson,P.K., Lucas,G.,
            Luben,R., Loos,R.J., Lokki,M.L., Lettre,G., Langenberg,C.,
            Launer,L.J., Lakatta,E.G., Laaksonen,R., Kyvik,K.O., Kronenberg,F.,
            Konig,I.R., Khaw,K.T., Kaprio,J., Kaplan,L.M., Johansson,A.,
            Jarvelin,M.R., Janssens,A.C., Ingelsson,E., Igl,W., Kees
            Hovingh,G., Hottenga,J.J., Hofman,A., Hicks,A.A., Hengstenberg,C.,
            Heid,I.M., Hayward,C., Havulinna,A.S., Hastie,N.D., Harris,T.B.,
            Haritunians,T., Hall,A.S., Gyllensten,U., Guiducci,C., Groop,L.C.,
            Gonzalez,E., Gieger,C., Freimer,N.B., Ferrucci,L., Erdmann,J.,
            Elliott,P., Ejebe,K.G., Doring,A., Dominiczak,A.F., Demissie,S.,
            Deloukas,P., de Geus,E.J., de Faire,U., Crawford,G., Collins,F.S.,
            Chen,Y.D., Caulfield,M.J., Campbell,H., Burtt,N.P.,
            Bonnycastle,L.L., Boomsma,D.I., Boekholdt,S.M., Bergman,R.N.,
            Barroso,I., Bandinelli,S., Ballantyne,C.M., Assimes,T.L.,
            Quertermous,T., Altshuler,D., Seielstad,M., Wong,T.Y., Tai,E.S.,
            Feranil,A.B., Kuzawa,C.W., Adair,L.S., Taylor,H.A. Jr.,
            Borecki,I.B., Gabriel,S.B., Wilson,J.G., Holm,H.,
            Thorsteinsdottir,U., Gudnason,V., Krauss,R.M., Mohlke,K.L.,
            Ordovas,J.M., Munroe,P.B., Kooner,J.S., Tall,A.R., Hegele,R.A.,
            Kastelein,J.J., Schadt,E.E., Rotter,J.I., Boerwinkle,E.,
            Strachan,D.P., Mooser,V., Stefansson,K., Reilly,M.P., Samani,N.J.,
            Schunkert,H., Cupples,L.A., Sandhu,M.S., Ridker,P.M., Rader,D.J.,
            van Duijn,C.M., Peltonen,L., Abecasis,G.R., Boehnke,M. and
            Kathiresan,S.
  TITLE     Biological, clinical and population relevance of 95 loci for blood
            lipids
  JOURNAL   Nature 466 (7307), 707-713 (2010)
   PUBMED   20686565
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   9  (residues 1 to 616)
  AUTHORS   Kathiresan,S., Willer,C.J., Peloso,G.M., Demissie,S., Musunuru,K.,
            Schadt,E.E., Kaplan,L., Bennett,D., Li,Y., Tanaka,T., Voight,B.F.,
            Bonnycastle,L.L., Jackson,A.U., Crawford,G., Surti,A., Guiducci,C.,
            Burtt,N.P., Parish,S., Clarke,R., Zelenika,D., Kubalanza,K.A.,
            Morken,M.A., Scott,L.J., Stringham,H.M., Galan,P., Swift,A.J.,
            Kuusisto,J., Bergman,R.N., Sundvall,J., Laakso,M., Ferrucci,L.,
            Scheet,P., Sanna,S., Uda,M., Yang,Q., Lunetta,K.L., Dupuis,J., de
            Bakker,P.I., O'Donnell,C.J., Chambers,J.C., Kooner,J.S.,
            Hercberg,S., Meneton,P., Lakatta,E.G., Scuteri,A., Schlessinger,D.,
            Tuomilehto,J., Collins,F.S., Groop,L., Altshuler,D., Collins,R.,
            Lathrop,G.M., Melander,O., Salomaa,V., Peltonen,L.,
            Orho-Melander,M., Ordovas,J.M., Boehnke,M., Abecasis,G.R.,
            Mohlke,K.L. and Cupples,L.A.
  TITLE     Common variants at 30 loci contribute to polygenic dyslipidemia
  JOURNAL   Nat Genet 41 (1), 56-65 (2009)
   PUBMED   19060906
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   10 (residues 1 to 616)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL591393.10.
            
            On May 26, 2021 this sequence version replaced NP_689787.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2745566.1,
                                           SRR11853564.26971.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000512701.7/ ENSP00000422496.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p22.3"
     Protein         1..616
                     /product="tetratricopeptide repeat protein 39B isoform 1"
                     /note="tetratricopeptide repeat protein 39B; TPR repeat
                     protein 39B"
                     /calculated_mol_wt=69969
     Region          76..532
                     /region_name="Iml2-TPR_39"
                     /note="Iml2/Tetratricopeptide repeat protein 39;
                     pfam10300"
                     /db_xref="CDD:463047"
     Region          528..592
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     CDS             1..616
                     /gene="TTC39B"
                     /gene_synonym="C9orf52"
                     /coded_by="NM_152574.3:92..1942"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6477.3"
                     /db_xref="GeneID:158219"
                     /db_xref="HGNC:HGNC:23704"
                     /db_xref="MIM:613574"
ORIGIN      
        1 mallgsrael eadedvfeda letisisshs dmatsslhfa scdtqqaprq rgastvssss
       61 stkvdlksgl eecavalnlf lsnkftdale llrpwakesm yhalgystiv vlqavltfeq
      121 qdiqngisam kdalqtcqky rkkytvvesf ssllsrgsle qlseeemhae icyaecllqk
      181 aaltfvqden minfikgglk irtsyqiyke clsilheiqk nklqqeffye feggvklgsg
      241 afnlmlsllp ariirllefi gfsgnrelgl lqlregasgr smrsalcclt ilafhtyisl
      301 ilgtgevnva eaerllapfl qqfpngslvl fyhariellk gnleeaqevf qkcisvqeew
      361 kqfhhlcywe lmwinvfqqn wmqayyysdl lckeskwska tyvflkaail smlpeedvva
      421 tnenvvtlfr qvdslkqria gksiptekfa vrkarrysas lpapvklilp alemmyvwng
      481 fsivskrkdl senllvtvek aeaalqsqnf nsfsvddecl vkllkgcclk nlqrplqael
      541 cynhvvesek llkydhylvp ftlfelasly ksqgeidkai kfletarnny kdyslesrlh
      601 friqaalhlw rkpssd
//
LOCUS       NP_001352528             954 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA-processing factor 40 homolog A isoform 7 [Homo sapiens].
ACCESSION   NP_001352528 XP_016859943
VERSION     NP_001352528.1
DBSOURCE    REFSEQ: accession NM_001365599.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 954)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 954)
  AUTHORS   Choudhary,B. and Norris,A.
  TITLE     Conserved role for spliceosomal component PRPF40A in microexon
            splicing
  JOURNAL   RNA 31 (1), 43-50 (2024)
   PUBMED   39389624
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 954)
  AUTHORS   Martinez-Lumbreras,S., Trager,L.K., Mulorz,M.M., Payr,M.,
            Dikaya,V., Hipp,C., Konig,J. and Sattler,M.
  TITLE     Intramolecular autoinhibition regulates the selectivity of PRPF40A
            tandem WW domains for proline-rich motifs
  JOURNAL   Nat Commun 15 (1), 3888 (2024)
   PUBMED   38719828
  REMARK    GeneRIF: Intramolecular autoinhibition regulates the selectivity of
            PRPF40A tandem WW domains for proline-rich motifs.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 954)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 954)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 954)
  AUTHORS   Allen,M., Friedler,A., Schon,O. and Bycroft,M.
  TITLE     The structure of an FF domain from human HYPA/FBP11
  JOURNAL   J Mol Biol 323 (3), 411-416 (2002)
   PUBMED   12381297
  REMARK    GeneRIF: Data describe the structure of an FF domain from
            HYPA/FBP11, which differs from those of other
            phosphopeptide-binding domains and represents a novel
            phosphopeptide-binding fold.
REFERENCE   7  (residues 1 to 954)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   8  (residues 1 to 954)
  AUTHORS   Bedford,M.T., Reed,R. and Leder,P.
  TITLE     WW domain-mediated interactions reveal a spliceosome-associated
            protein that binds a third class of proline-rich motif: the proline
            glycine and methionine-rich motif
  JOURNAL   Proc Natl Acad Sci U S A 95 (18), 10602-10607 (1998)
   PUBMED   9724750
REFERENCE   9  (residues 1 to 954)
  AUTHORS   Faber,P.W., Barnes,G.T., Srinidhi,J., Chen,J., Gusella,J.F. and
            MacDonald,M.E.
  TITLE     Huntingtin interacts with a family of WW domain proteins
  JOURNAL   Hum Mol Genet 7 (9), 1463-1474 (1998)
   PUBMED   9700202
REFERENCE   10 (residues 1 to 954)
  AUTHORS   Chan,D.C., Bedford,M.T. and Leder,P.
  TITLE     Formin binding proteins bear WWP/WW domains that bind proline-rich
            peptides and functionally resemble SH3 domains
  JOURNAL   EMBO J 15 (5), 1045-1054 (1996)
   PUBMED   8605874
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079344.5 and AC012443.8.
            
            On Sep 12, 2018 this sequence version replaced XP_016859943.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..954
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q23.3"
     Protein         1..954
                     /product="pre-mRNA-processing factor 40 homolog A isoform
                     7"
                     /note="formin binding protein 3; Huntingtin-interacting
                     protein A; NY-REN-6 antigen; Fas-ligand associated factor
                     1; formin-binding protein 11; huntingtin yeast partner A;
                     fas ligand-associated factor 1; pre-mRNA processing factor
                     40 homolog A; renal carcinoma antigen NY-REN-6;
                     huntingtin-interacting protein 10; PRP40 pre-mRNA
                     processing factor 40 homolog A"
                     /calculated_mol_wt=108340
     Region          152..793
                     /region_name="PRP40"
                     /note="Splicing factor [RNA processing and modification];
                     COG5104"
                     /db_xref="CDD:227435"
     CDS             1..954
                     /gene="PRPF40A"
                     /gene_synonym="FBP-11; FBP11; FLAF1; FNBP3; HIP-10; HIP10;
                     HYPA; NY-REN-6; Prp40"
                     /coded_by="NM_001365599.4:23..2887"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:55660"
                     /db_xref="HGNC:HGNC:16463"
                     /db_xref="MIM:612941"
ORIGIN      
        1 mcsgsgrrrs slsptmrpgt gaergglmvs emeshppsqg pgdgerrlsg sslcsgswvs
       61 adgflrrrps mghpgmhyap mgmhpmgqra nmppvphgmm pqmmppmggp pmgqmpgmms
      121 svmpgmmmsh msqasmqpal ppgvnsmdva agtasgaksm wtehkspdgr tyyyntetkq
      181 stwekpddlk tpaeqllskc pwkeyksdsg kpyyynsqtk esrwakpkel edleamikae
      241 esskqeectt tstapvptte ipttmstmaa aeaaaavvaa aaaaaaaaaa ananastsas
      301 ntvsgtvpvv pepevtsiva tvvdnentvt isteeqaqlt stpaiqdqsv evssntgeet
      361 skqetvadft pkkeeeesqp akktytwntk eeakqafkel lkekrvpsna sweqamkmii
      421 ndprysalak lsekkqafna ykvqtekeek eearskykea kesfqrflen hekmtsttry
      481 kkaeqmfgem evwnaiserd rleiyedvlf flskkekeqa kqlrkrnwea lknildnman
      541 vtysttwsea qqylmdnptf aedeelqnmd kedalicfee hiralekeee eekqksllre
      601 rrrqrknres fqifldelhe hgqlhsmssw melyptissd irftnmlgqp gstaldlfkf
      661 yvedlkaryh dekkiikdil kdkgfvvevn ttfedfvaii sstkrsttld agniklafns
      721 llekaearer erekeearkm krkesafksm lkqaappiel davwedirer fvkepafedi
      781 tleserkrif kdfmhvlehe cqhhhsknkk hskkskkhhr krsrsrsgsd sddddshskk
      841 krqrsesrsa sehsssaese rsykkskkhk kkskkrrhks dspesdaere kdkkekdres
      901 ekdrtrqrse skhkspkkkt gkdsgnwdts gselsegele krrrtlleql dddq
//
LOCUS       NP_001381244             174 aa            linear   PRI 21-NOV-2025
DEFINITION  kinetochore protein Spc24 isoform 6 [Homo sapiens].
ACCESSION   NP_001381244
VERSION     NP_001381244.1
DBSOURCE    REFSEQ: accession NM_001394315.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Yue,H., Wu,K., Liu,K., Gou,L., Huang,A. and Tang,H.
  TITLE     LINC02154 promotes the proliferation and metastasis of
            hepatocellular carcinoma by enhancing SPC24 promoter activity and
            activating the PI3K-AKT signaling pathway
  JOURNAL   Cell Oncol (Dordr) 45 (3), 447-462 (2022)
   PUBMED   35543858
  REMARK    GeneRIF: LINC02154 promotes the proliferation and metastasis of
            hepatocellular carcinoma by enhancing SPC24 promoter activity and
            activating the PI3K-AKT signaling pathway.
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Wang,Y., Yang,H., Zhang,G., Luo,C., Zhang,S., Luo,R. and Deng,B.
  TITLE     hsa-miR-7-5p suppresses proliferation, migration and promotes
            apoptosis in hepatocellular carcinoma cell lines by inhibiting
            SPC24 expression
  JOURNAL   Biochem Biophys Res Commun 561, 80-87 (2021)
   PUBMED   34020142
  REMARK    GeneRIF: hsa-miR-7-5p suppresses proliferation, migration and
            promotes apoptosis in hepatocellular carcinoma cell lines by
            inhibiting SPC24 expression.
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 174)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   7  (residues 1 to 174)
  AUTHORS   Ciferri,C., De Luca,J., Monzani,S., Ferrari,K.J., Ristic,D.,
            Wyman,C., Stark,H., Kilmartin,J., Salmon,E.D. and Musacchio,A.
  TITLE     Architecture of the human ndc80-hec1 complex, a critical
            constituent of the outer kinetochore
  JOURNAL   J Biol Chem 280 (32), 29088-29095 (2005)
   PUBMED   15961401
  REMARK    GeneRIF: the Spc24, Spc25, Nuf2, and Ndc80/Hec1 complex is a
            faithful copy of the endogenous Ndc80 complex
REFERENCE   8  (residues 1 to 174)
  AUTHORS   Ahonen,L.J., Kallio,M.J., Daum,J.R., Bolton,M., Manke,I.A.,
            Yaffe,M.B., Stukenberg,P.T. and Gorbsky,G.J.
  TITLE     Polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope
            and modulates the association of spindle-checkpoint proteins at
            kinetochores
  JOURNAL   Curr Biol 15 (12), 1078-1089 (2005)
   PUBMED   15964272
REFERENCE   9  (residues 1 to 174)
  AUTHORS   Bharadwaj,R., Qi,W. and Yu,H.
  TITLE     Identification of two novel components of the human NDC80
            kinetochore complex
  JOURNAL   J Biol Chem 279 (13), 13076-13085 (2004)
   PUBMED   14699129
  REMARK    GeneRIF: hSPC24 is a component of the human NDC80 kinetochore
            complex
REFERENCE   10 (residues 1 to 174)
  AUTHORS   McCleland,M.L., Kallio,M.J., Barrett-Wilt,G.A., Kestner,C.A.,
            Shabanowitz,J., Hunt,D.F., Gorbsky,G.J. and Stukenberg,P.T.
  TITLE     The vertebrate Ndc80 complex contains Spc24 and Spc25 homologs,
            which are required to establish and maintain
            kinetochore-microtubule attachment
  JOURNAL   Curr Biol 14 (2), 131-137 (2004)
   PUBMED   14738735
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011485.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..174
                     /product="kinetochore protein Spc24 isoform 6"
                     /note="kinetochore protein Spc24; hSpc24; spindle pole
                     body component 24 homolog; SPC24, NDC80 kinetochore
                     complex component, homolog"
                     /calculated_mol_wt=19543
     Region          1..131
                     /region_name="Interaction with the N-terminus of SPBC25"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBT2.3)"
     Region          1..69
                     /region_name="Interaction with the NDC80-CDCA1 subcomplex"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBT2.3)"
     Region          <3..>128
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NBT2.3)"
     Region          82..>145
                     /region_name="Spc24"
                     /note="Spc24 subunit of Ndc80; pfam08286"
                     /db_xref="CDD:429899"
     CDS             1..174
                     /gene="SPC24"
                     /gene_synonym="SPBC24"
                     /coded_by="NM_001394315.1:7..531"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:147841"
                     /db_xref="HGNC:HGNC:26913"
                     /db_xref="MIM:609394"
ORIGIN      
        1 maafrdieev sqgllsllga nraeaqqrrl lgrheqvver lletqdgaek qlreiltmek
       61 evaqsllnak eqvhqggvel qqleaglqea geedtrlkas llqltrelee lkeieadler
      121 qekevdedtt vtipsavyva qlyhqgvcls atvcpdsarh qrdkirvtwf sshc
//
LOCUS       NP_001245283             962 aa            linear   PRI 21-NOV-2025
DEFINITION  116 kDa U5 small nuclear ribonucleoprotein component isoform c
            [Homo sapiens].
ACCESSION   NP_001245283
VERSION     NP_001245283.1
DBSOURCE    REFSEQ: accession NM_001258354.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 962)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 962)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 962)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 962)
  AUTHORS   Schneider,S., Brandina,I., Peter,D., Lagad,S., Fraudeau,A.,
            Portell-Montserrat,J., Tholen,J., Zhao,J. and Galej,W.P.
  TITLE     Structure of the human 20S U5 snRNP
  JOURNAL   Nat Struct Mol Biol 31 (5), 752-756 (2024)
   PUBMED   38467877
REFERENCE   5  (residues 1 to 962)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   6  (residues 1 to 962)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   7  (residues 1 to 962)
  AUTHORS   Makarov,E.M., Makarova,O.V., Achsel,T. and Luhrmann,R.
  TITLE     The human homologue of the yeast splicing factor prp6p contains
            multiple TPR elements and is stably associated with the U5 snRNP
            via protein-protein interactions
  JOURNAL   J Mol Biol 298 (4), 567-575 (2000)
   PUBMED   10788320
REFERENCE   8  (residues 1 to 962)
  AUTHORS   Achsel,T., Ahrens,K., Brahms,H., Teigelkamp,S. and Luhrmann,R.
  TITLE     The human U5-220kD protein (hPrp8) forms a stable RNA-free complex
            with several U5-specific proteins, including an RNA unwindase, a
            homologue of ribosomal elongation factor EF-2, and a novel WD-40
            protein
  JOURNAL   Mol Cell Biol 18 (11), 6756-6766 (1998)
   PUBMED   9774689
REFERENCE   9  (residues 1 to 962)
  AUTHORS   Fabrizio,P., Laggerbauer,B., Lauber,J., Lane,W.S. and Luhrmann,R.
  TITLE     An evolutionarily conserved U5 snRNP-specific protein is a
            GTP-binding factor closely related to the ribosomal translocase
            EF-2
  JOURNAL   EMBO J 16 (13), 4092-4106 (1997)
   PUBMED   9233818
REFERENCE   10 (residues 1 to 962)
  AUTHORS   Lines,M., Hartley,T., MacDonald,S.K. and Boycott,K.M.
  TITLE     Mandibulofacial Dysostosis with Microcephaly
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24999515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC015936.14 and AK297392.1.
            
            Summary: This gene encodes a GTPase which is a component of the
            spliceosome complex which processes precursor mRNAs to produce
            mature mRNAs. Mutations in this gene are associated with
            mandibulofacial dysostosis with microcephaly. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (4) uses an alternate in-frame
            splice site in the 5' coding region compared to variant 1. The
            resulting protein (isoform c) is shorter compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297392.1, SRR14038197.240616.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..962
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..962
                     /product="116 kDa U5 small nuclear ribonucleoprotein
                     component isoform c"
                     /note="116 kDa U5 small nuclear ribonucleoprotein
                     component; hSNU114; SNU114 homolog; U5 snRNP-specific
                     protein, 116 kDa; elongation factor Tu GTP-binding
                     domain-containing protein 2"
                     /calculated_mol_wt=108153
     Region          1..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15029.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q15029.1)"
     Region          4..110
                     /region_name="EFTUD2"
                     /note="116 kDa U5 small nuclear ribonucleoprotein
                     component N-terminus; pfam16004"
                     /db_xref="CDD:464968"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15029.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15029.1)"
     Region          122..944
                     /region_name="PRK13351"
                     /note="elongation factor G-like protein; cl46912"
                     /db_xref="CDD:481252"
     CDS             1..962
                     /gene="EFTUD2"
                     /gene_synonym="MFDGA; MFDM; SNRNP116; Snrp116; Snu114;
                     U5-116KD"
                     /coded_by="NM_001258354.2:82..2970"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS59295.1"
                     /db_xref="GeneID:9343"
                     /db_xref="HGNC:HGNC:30858"
                     /db_xref="MIM:603892"
ORIGIN      
        1 mdtdlydefg nyigpeldsd edddelgret kdldemdddd ddddvgdhdd dhpgmevvlh
       61 edkkyyptae evygpeveti vqeedtqplt epiikpvktk kftlmeqtlp vtvyemdfla
      121 dlmdnselir nvtlcghlhh gkthpeirkr ydqdlcytdi lfteqergvg ikstpvtvvl
      181 pdtkgksylf nimdtpghvn fsdevtaglr isdgvvlfid aaegvmlnte rlikhavqer
      241 lavtvcinki drlilelklp ptdayyklrh ivdevnglis mystdenlil spllgnvcfs
      301 ssqysicftl gsfakiyadt fgdinyqefa krlwgdiyfn pktrkftkka ptsssqrsfv
      361 efileplyki laqvvgdvdt slprtldelg ihltkeelkl nirpllrlvc kkffgeftgf
      421 vdmcvqhips pkvgakpkie htytggvdsd lgeamsdcdp dgplmchttk mystddgvqf
      481 hafgrvlsgt ihagqpvkvl genytledee dsqictvgrl wisvaryhie vnrvpagnwv
      541 liegvdqpiv ktatiteprg neeaqifrpl kfnttsviki avepvnpsel pkmldglrkv
      601 nksypslttk veesgehvil gtgelyldcv mhdlrkmyse idikvadpvv tfcetvvets
      661 slkcfaetpn kknkitmiae plekglaedi enevvqitwn rkklgeffqt kydwdllaar
      721 siwafgpdat gpnilvddtl psevdkallg svkdsivqgf qwgtregplc delirnvkfk
      781 ildavvaqep lhrgggqiip tarrvvysaf lmatprlmep yyfvevqapa dcvsavytvl
      841 arrrghvtqd apipgsplyt ikafipaids fgfetdlrth tqgqafslsv fhhwqivpgd
      901 pldksivirp lepqpaphla refmiktrrr kglsedvsis kffddpmlle lakqdvvlny
      961 pm
//
LOCUS       NP_783856                153 aa            linear   PRI 21-NOV-2025
DEFINITION  protein SSX4 isoform b [Homo sapiens].
ACCESSION   NP_783856 XP_001125871
VERSION     NP_783856.1
DBSOURCE    REFSEQ: accession NM_175729.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Stark,M.S., Tom,L.N., Boyle,G.M., Bonazzi,V.F., Soyer,H.P.,
            Herington,A.C., Pollock,P.M. and Hayward,N.K.
  TITLE     The 'melanoma-enriched' microRNA miR-4731-5p acts as a tumour
            suppressor
  JOURNAL   Oncotarget 7 (31), 49677-49687 (2016)
   PUBMED   27331623
  REMARK    GeneRIF: loss of miR-4731 expression in stage IV patient tumors
            supports melanoma growth by, in part, reducing its regulatory
            control of SSX expression levels
REFERENCE   6  (residues 1 to 153)
  AUTHORS   Brodin,B., Haslam,K., Yang,K., Bartolazzi,A., Xie,Y., Starborg,M.,
            Lundeberg,J. and Larsson,O.
  TITLE     Cloning and characterization of spliced fusion transcript variants
            of synovial sarcoma: SYT/SSX4, SYT/SSX4v, and SYT/SSX2v. Possible
            regulatory role of the fusion gene product in wild type SYT
            expression
  JOURNAL   Gene 268 (1-2), 173-182 (2001)
   PUBMED   11368913
REFERENCE   7  (residues 1 to 153)
  AUTHORS   Chen,C.H., Chen,G.J., Lee,H.S., Huang,G.T., Yang,P.M., Tsai,L.J.,
            Chen,D.S. and Sheu,J.C.
  TITLE     Expressions of cancer-testis antigens in human hepatocellular
            carcinomas
  JOURNAL   Cancer Lett 164 (2), 189-195 (2001)
   PUBMED   11179834
REFERENCE   8  (residues 1 to 153)
  AUTHORS   dos Santos,N.R., de Bruijn,D.R. and van Kessel,A.G.
  TITLE     Molecular mechanisms underlying human synovial sarcoma development
  JOURNAL   Genes Chromosomes Cancer 30 (1), 1-14 (2001)
   PUBMED   11107170
  REMARK    Review article
REFERENCE   9  (residues 1 to 153)
  AUTHORS   Skytting,B., Nilsson,G., Brodin,B., Xie,Y., Lundeberg,J., Uhlen,M.
            and Larsson,O.
  TITLE     A novel fusion gene, SYT-SSX4, in synovial sarcoma
  JOURNAL   J Natl Cancer Inst 91 (11), 974-975 (1999)
   PUBMED   10359553
REFERENCE   10 (residues 1 to 153)
  AUTHORS   Gure,A.O., Tureci,O., Sahin,U., Tsang,S., Scanlan,M.J., Jager,E.,
            Knuth,A., Pfreundschuh,M., Old,L.J. and Chen,Y.T.
  TITLE     SSX: a multigene family with several members transcribed in normal
            testis and human cancer
  JOURNAL   Int J Cancer 72 (6), 965-971 (1997)
   PUBMED   9378559
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL606490.15.
            
            On Sep 20, 2006 this sequence version replaced XP_001125871.1.
            
            Summary: The product of this gene belongs to the family of highly
            homologous synovial sarcoma X (SSX) breakpoint proteins. These
            proteins may function as transcriptional repressors. They are also
            capable of eliciting spontaneously humoral and cellular immune
            responses in cancer patients, and are potentially useful targets in
            cancer vaccine-based immunotherapy. SSX1, SSX2 and SSX4 genes have
            been involved in the t(X;18) translocation characteristically found
            in all synovial sarcomas. This translocation results in the fusion
            of the synovial sarcoma translocation gene on chromosome 18 to one
            of the SSX genes on chromosome X. Chromosome Xp11 contains a
            segmental duplication resulting in two identical copies of synovial
            sarcoma, X breakpoint 4, SSX4 and SSX4B, in tail-to-tail
            orientation. This gene, SSX4, represents the more telomeric copy.
            Two transcript variants encoding distinct isoforms have been
            identified for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks a segment in the coding
            region which leads to a frameshift, compared to variant 1. The
            resulting isoform (b) contains a shorter and distinct C-terminus
            compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC103864.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.23"
     Protein         1..153
                     /product="protein SSX4 isoform b"
                     /note="protein SSX4; cancer/testis antigen 5.4; synovial
                     sarcoma, X breakpoint 4"
                     /calculated_mol_wt=17787
     Region          23..82
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     CDS             1..153
                     /gene="SSX4"
                     /gene_synonym="CT5.4"
                     /coded_by="NM_175729.2:47..508"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43934.1"
                     /db_xref="GeneID:6759"
                     /db_xref="HGNC:HGNC:11338"
                     /db_xref="MIM:300326"
ORIGIN      
        1 mngddafarr prddaqisek lrkafddiak yfskkewekm kssekivyvy mklnyevmtk
       61 lgfkvtlppf mrskraadfh gndfgndrnh rnqverpqmt fgslqrifpk dpkggnmpgp
      121 tdcvressww fmkrsatlrk mtsnsprgyd tcp
//
LOCUS       NP_001293083             486 aa            linear   PRI 21-NOV-2025
DEFINITION  T-complex protein 1 subunit epsilon isoform c [Homo sapiens].
ACCESSION   NP_001293083
VERSION     NP_001293083.1
DBSOURCE    REFSEQ: accession NM_001306154.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Wu,S. and Peng,L.
  TITLE     Increased CCT5 expression is a potential unfavourable factor
            promoting the growth of nasopharyngeal carcinoma
  JOURNAL   J Int Med Res 52 (9), 3000605241271754 (2024)
   PUBMED   39286844
  REMARK    GeneRIF: Increased CCT5 expression is a potential unfavourable
            factor promoting the growth of nasopharyngeal carcinoma.
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Scalia,F., Lo Bosco,G., Paladino,L., Vitale,A.M., Noori,L., Conway
            de Macario,E., Macario,A.J.L., Bucchieri,F., Cappello,F. and Lo
            Celso,F.
  TITLE     Structural and Dynamic Disturbances Revealed by Molecular Dynamics
            Simulations Predict the Impact on Function of CCT5 Chaperonin
            Mutations Associated with Rare Severe Distal Neuropathies
  JOURNAL   Int J Mol Sci 24 (3), 2018 (2023)
   PUBMED   36768350
  REMARK    GeneRIF: Structural and Dynamic Disturbances Revealed by Molecular
            Dynamics Simulations Predict the Impact on Function of CCT5
            Chaperonin Mutations Associated with Rare Severe Distal
            Neuropathies.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Sergeeva,O.A., Tran,M.T., Haase-Pettingell,C. and King,J.A.
  TITLE     Biochemical characterization of mutants in chaperonin proteins CCT4
            and CCT5 associated with hereditary sensory neuropathy
  JOURNAL   J Biol Chem 289 (40), 27470-27480 (2014)
   PUBMED   25124038
  REMARK    GeneRIF: H147R CCT5 was not as efficient in chaperoning these
            substrates as wild type CCT5.
REFERENCE   6  (residues 1 to 486)
  AUTHORS   Bouhouche,A., Benomar,A., Bouslam,N., Chkili,T. and Yahyaoui,M.
  TITLE     Mutation in the epsilon subunit of the cytosolic
            chaperonin-containing t-complex peptide-1 (Cct5) gene causes
            autosomal recessive mutilating sensory neuropathy with spastic
            paraplegia
  JOURNAL   J Med Genet 43 (5), 441-443 (2006)
   PUBMED   16399879
  REMARK    GeneRIF: A missense mutation within the CCT5 gene is associated
            with autosomal recessive mutilating sensory neuropathy with spastic
            paraplegia.
REFERENCE   7  (residues 1 to 486)
  AUTHORS   Roperch,J.P., Lethrone,F., Prieur,S., Piouffre,L., Israeli,D.,
            Tuynder,M., Nemani,M., Pasturaud,P., Gendron,M.C., Dausset,J.,
            Oren,M., Amson,R.B. and Telerman,A.
  TITLE     SIAH-1 promotes apoptosis and tumor suppression through a network
            involving the regulation of protein folding, unfolding, and
            trafficking: identification of common effectors with p53 and
            p21(Waf1)
  JOURNAL   Proc Natl Acad Sci U S A 96 (14), 8070-8073 (1999)
   PUBMED   10393949
REFERENCE   8  (residues 1 to 486)
  AUTHORS   Liou,A.K. and Willison,K.R.
  TITLE     Elucidation of the subunit orientation in CCT (chaperonin
            containing TCP1) from the subunit composition of CCT
            micro-complexes
  JOURNAL   EMBO J 16 (14), 4311-4316 (1997)
   PUBMED   9250675
REFERENCE   9  (residues 1 to 486)
  AUTHORS   Roobol,A., Holmes,F.E., Hayes,N.V., Baines,A.J. and Carden,M.J.
  TITLE     Cytoplasmic chaperonin complexes enter neurites developing in vitro
            and differ in subunit composition within single cells
  JOURNAL   J Cell Sci 108 (Pt 4), 1477-1488 (1995)
   PUBMED   7615668
REFERENCE   10 (residues 1 to 486)
  AUTHORS   Kubota,H., Hynes,G., Carne,A., Ashworth,A. and Willison,K.
  TITLE     Identification of six Tcp-1-related genes encoding divergent
            subunits of the TCP-1-containing chaperonin
  JOURNAL   Curr Biol 4 (2), 89-99 (1994)
   PUBMED   7953530
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from FJ224303.1 and AK302368.1.
            
            Summary: The protein encoded by this gene is a molecular chaperone
            that is a member of the chaperonin containing TCP1 complex (CCT),
            also known as the TCP1 ring complex (TRiC). This complex consists
            of two identical stacked rings, each containing eight different
            proteins. Unfolded polypeptides enter the central cavity of the
            complex and are folded in an ATP-dependent manner. The complex
            folds various proteins, including actin and tubulin. Mutations in
            this gene cause hereditary sensory and autonomic neuropathy with
            spastic paraplegia (HSNSP). Alternative splicing results in
            multiple transcript variants. Related pseudogenes have been
            identified on chromosomes 5 and 13. [provided by RefSeq, Apr 2015].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1, resulting in
            an isoform (c) that is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.367250.1, AK302368.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.2"
     Protein         1..486
                     /product="T-complex protein 1 subunit epsilon isoform c"
                     /note="T-complex protein 1 subunit epsilon; epididymis
                     secretory protein Li 69; chaperonin containing TCP1,
                     subunit 5 (epsilon); chaperonin containing T-complex
                     polypeptide 1 subunit 5"
                     /calculated_mol_wt=53718
     Region          10..480
                     /region_name="TCP1_epsilon"
                     /note="TCP-1 (CTT or eukaryotic type II) chaperonin
                     family, epsilon subunit. Chaperonins are involved in
                     productive folding of proteins. They share a common
                     general morphology, a double toroid of 2 stacked rings. In
                     contrast to bacterial group I chaperonins...; cd03339"
                     /db_xref="CDD:239455"
     Site            order(52..54,116,349,367,407,451,453)
                     /site_type="other"
                     /note="ATP/Mg binding site [chemical binding]"
                     /db_xref="CDD:239455"
     Site            order(387,405,414,416..417,420)
                     /site_type="active"
                     /note="stacking interactions [active]"
                     /db_xref="CDD:239455"
     CDS             1..486
                     /gene="CCT5"
                     /gene_synonym="CCT-epsilon; CCTE; HEL-S-69; HSNSP;
                     PNAS-102; TCP-1-epsilon"
                     /coded_by="NM_001306154.2:62..1522"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82989.1"
                     /db_xref="GeneID:22948"
                     /db_xref="HGNC:HGNC:1618"
                     /db_xref="MIM:610150"
ORIGIN      
        1 masmgtlafd eygrpfliik dqdrksrlmg lealkshima akavantmrt slgpnvlaga
       61 lleeaeqlld rgihpiriad gyeqaarvai ehldkisdsv lvdikdtepl iqtakttlgs
      121 kvvnschrqm aeiavnavlt vadmerrdvd felikvegkv ggrledtkli kgvivdkdfs
      181 hpqmpkkved akiailtcpf eppkpktkhk ldvtsvedyk alqkyekekf eemiqqiket
      241 ganlaicqwg fddeanhlll qnnlpavrwv ggpeieliai atggrivprf seltaeklgf
      301 aglvqeisfg ttkdkmlvie qcknsravti firggnkmii eeakrslhda lcvirnlird
      361 nrvvygggaa eiscalavsq eadkcptleq yamrafadal evipmalsen sgmnpiqtmt
      421 evrarqvkem npalgidclh kgtndmkqqh vietligkkq qislatqmvr milkiddirk
      481 pgesee
//
LOCUS       NP_758863                369 aa            linear   PRI 21-NOV-2025
DEFINITION  membrane cofactor protein isoform 6 precursor [Homo sapiens].
ACCESSION   NP_758863
VERSION     NP_758863.1
DBSOURCE    REFSEQ: accession NM_172353.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Grodstein,F., Lemos,B., Yang,J., de Paiva Lopes,K., Vialle,R.A.,
            Seyfried,N., Wang,Y., Shireby,G., Hannon,E., Thomas,A., Brookes,K.,
            Mill,J., De Jager,P.L. and Bennett,D.A.
  TITLE     Genetic architecture of epigenetic cortical clock age in brain
            tissue from older individuals: alterations in CD46 and other loci
  JOURNAL   Epigenetics 19 (1), 2392050 (2024)
   PUBMED   39169872
  REMARK    GeneRIF: Genetic architecture of epigenetic cortical clock age in
            brain tissue from older individuals: alterations in CD46 and other
            loci.
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Thi,T.N., Thanh,H.D., Nguyen,V.T., Kwon,S.Y., Moon,C., Hwang,E.C.
            and Jung,C.
  TITLE     Complement regulatory protein CD46 promotes bladder cancer
            metastasis through activation of MMP9
  JOURNAL   Int J Oncol 65 (1) (2024)
   PUBMED   38847230
  REMARK    GeneRIF: Complement regulatory protein CD46 promotes bladder cancer
            metastasis through activation of MMP9.
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Vassiliev,P., Gusev,E., Komelkova,M., Kochetkov,A., Dobrynina,M.
            and Sarapultsev,A.
  TITLE     Computational Analysis of CD46 Protein Interaction with SARS-CoV-2
            Structural Proteins: Elucidating a Putative Viral Entry Mechanism
            into Human Cells
  JOURNAL   Viruses 15 (12), 2297 (2023)
   PUBMED   38140538
  REMARK    GeneRIF: Computational Analysis of CD46 Protein Interaction with
            SARS-CoV-2 Structural Proteins: Elucidating a Putative Viral Entry
            Mechanism into Human Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Richards,A., Kemp,E.J., Liszewski,M.K., Goodship,J.A., Lampe,A.K.,
            Decorte,R., Muslumanoglu,M.H., Kavukcu,S., Filler,G., Pirson,Y.,
            Wen,L.S., Atkinson,J.P. and Goodship,T.H.
  TITLE     Mutations in human complement regulator, membrane cofactor protein
            (CD46), predispose to development of familial hemolytic uremic
            syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (22), 12966-12971 (2003)
   PUBMED   14566051
  REMARK    GeneRIF: Mutations predispose to development of familial hemolytic
            uremic syndrome.
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Martin,B. and Smith,R.J.H.
  TITLE     C3 Glomerulopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301598
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Noris,M., Bresin,E., Mele,C. and Remuzzi,G.
  TITLE     Genetic Atypical Hemolytic-Uremic Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301541
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Russell,S.M., Sparrow,R.L., McKenzie,I.F. and Purcell,D.F.
  TITLE     Tissue-specific and allelic expression of the complement regulator
            CD46 is controlled by alternative splicing
  JOURNAL   Eur J Immunol 22 (6), 1513-1518 (1992)
   PUBMED   1601037
REFERENCE   8  (residues 1 to 369)
  AUTHORS   Adams,E.M., Brown,M.C., Nunge,M., Krych,M. and Atkinson,J.P.
  TITLE     Contribution of the repeating domains of membrane cofactor protein
            (CD46) of the complement system to ligand binding and cofactor
            activity
  JOURNAL   J Immunol 147 (9), 3005-3011 (1991)
   PUBMED   1717583
REFERENCE   9  (residues 1 to 369)
  AUTHORS   Post,T.W., Liszewski,M.K., Adams,E.M., Tedja,I., Miller,E.A. and
            Atkinson,J.P.
  TITLE     Membrane cofactor protein of the complement system: alternative
            splicing of serine/threonine/proline-rich exons and cytoplasmic
            tails produces multiple isoforms that correlate with protein
            phenotype
  JOURNAL   J Exp Med 174 (1), 93-102 (1991)
   PUBMED   1711570
REFERENCE   10 (residues 1 to 369)
  AUTHORS   Lublin,D.M., Liszewski,M.K., Post,T.W., Arce,M.A., Le Beau,M.M.,
            Rebentisch,M.B., Lemons,L.S., Seya,T. and Atkinson,J.P.
  TITLE     Molecular cloning and chromosomal localization of human membrane
            cofactor protein (MCP). Evidence for inclusion in the multigene
            family of complement-regulatory proteins
  JOURNAL   J Exp Med 168 (1), 181-194 (1988)
   PUBMED   3260937
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB078198.1, X59407.1 and
            BC030594.2.
            
            Summary: The protein encoded by this gene is a type I membrane
            protein and is a regulatory part of the complement system. The
            encoded protein has cofactor activity for inactivation of
            complement components C3b and C4b by serum factor I, which protects
            the host cell from damage by complement. In addition, the encoded
            protein can act as a receptor for the Edmonston strain of measles
            virus, human herpesvirus-6, and type IV pili of pathogenic
            Neisseria. Finally, the protein encoded by this gene may be
            involved in the fusion of the spermatozoa with the oocyte during
            fertilization. Mutations at this locus have been associated with
            susceptibility to hemolytic uremic syndrome. Alternatively spliced
            transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (f) lacks an alternate in-frame
            exon and an exon containing the stop codon compared to variant a.
            The resulting isoform (6) is shorter and has a distinct C-terminus
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC007046.1, SRR11853562.2962.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.2"
     Protein         1..369
                     /product="membrane cofactor protein isoform 6 precursor"
                     /note="CD46 antigen, complement regulatory protein;
                     membrane cofactor protein (CD46, trophoblast-lymphocyte
                     cross-reactive antigen); complement membrane cofactor
                     protein; measles virus receptor; trophoblast leucocyte
                     common antigen; antigen identified by monoclonal antibody
                     TRA-2-10; trophoblast leukocyte common antigen; CD46
                     molecule, complement regulatory protein"
                     /calculated_mol_wt=37508
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3869
     mat_peptide     35..369
                     /product="membrane cofactor protein isoform 6"
                     /calculated_mol_wt=37508
     Region          54..285
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     CDS             1..369
                     /gene="CD46"
                     /gene_synonym="AHUS2; MCP; MIC10; TLX; TRA2.10"
                     /coded_by="NM_172353.3:160..1269"
                     /note="isoform 6 precursor is encoded by transcript
                     variant f"
                     /db_xref="CCDS:CCDS1481.1"
                     /db_xref="GeneID:4179"
                     /db_xref="HGNC:HGNC:6953"
                     /db_xref="MIM:120920"
ORIGIN      
        1 meppgrrecp fpswrfpgll laamvlllys fsdaceeppt feameligkp kpyyeigerv
       61 dykckkgyfy ipplathtic drnhtwlpvs ddacyretcp yirdplngqa vpangtyefg
      121 yqmhficneg yyligeeily celkgsvaiw sgkppicekv lctpppkikn gkhtfsevev
      181 feyldavtys cdpapgpdpf sligestiyc gdnsvwsraa peckvvkcrf pvvengkqis
      241 gfgkkfyyka tvmfecdkgf yldgsdtivc dsnstwdppv pkclkgprpt ykppvsnypg
      301 ypkpeegild sldvwviavi viaivvgvav icvvpyrylq rrkkkgkadg gaeyatyqtk
      361 sttpaeqrg
//
LOCUS       NP_001295182             252 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate--cysteine ligase regulatory subunit isoform 2 [Homo
            sapiens].
ACCESSION   NP_001295182 XP_005270811
VERSION     NP_001295182.1
DBSOURCE    REFSEQ: accession NM_001308253.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Da,D., Pan,Z., Zeng,L., Dang,Y., Dang,C., Huang,Y., Shi,D. and
            Li,H.
  TITLE     Glutamate-cysteine ligase catalytic and its modifier function as
            novel immunotargets in gastric adenocarcinoma
  JOURNAL   Asian J Surg 46 (1), 143-149 (2023)
   PUBMED   35241341
  REMARK    GeneRIF: Glutamate-cysteine ligase catalytic and its modifier
            function as novel immunotargets in gastric adenocarcinoma.
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Yang,C., Xi,M., Liu,H., Bai,H., Jiang,C., Liu,Q. and Fan,P.
  TITLE     Association of Polymorphisms of Glutamate Cysteine Ligase Genes
            GCLC C-129 T and GCLM C-588 T with Risk of Polycystic Ovary
            Syndrome in Chinese Women
  JOURNAL   Reprod Sci 29 (6), 1790-1800 (2022)
   PUBMED   34642912
  REMARK    GeneRIF: Association of Polymorphisms of Glutamate Cysteine Ligase
            Genes GCLC C-129 T and GCLM C-588 T with Risk of Polycystic Ovary
            Syndrome in Chinese Women.
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Mazloomi,S., Khodadadi,I., Alizadeh,N. and Shafiee,G.
  TITLE     Association of glutamate cystein ligase (GCL) activity
            Peroxiredoxin 4 (prxR4) and apelin levels in women with
            preeclampsia
  JOURNAL   Pregnancy Hypertens 23, 163-168 (2021)
   PUBMED   33421846
  REMARK    GeneRIF: Association of glutamate cystein ligase (GCL) activity
            Peroxiredoxin 4 (prxR4) and apelin levels in women with
            preeclampsia.
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Misra,I. and Griffith,O.W.
  TITLE     Expression and purification of human gamma-glutamylcysteine
            synthetase
  JOURNAL   Protein Expr Purif 13 (2), 268-276 (1998)
   PUBMED   9675072
REFERENCE   7  (residues 1 to 252)
  AUTHORS   Sierra-Rivera,E., Dasouki,M., Summar,M.L., Krishnamani,M.R.,
            Meredith,M., Rao,P.N., Phillips,J.A. 3rd and Freeman,M.L.
  TITLE     Assignment of the human gene (GLCLR) that encodes the regulatory
            subunit of gamma-glutamylcysteine synthetase to chromosome 1p21
  JOURNAL   Cytogenet Cell Genet 72 (2-3), 252-254 (1996)
   PUBMED   8978789
REFERENCE   8  (residues 1 to 252)
  AUTHORS   Tsuchiya,K., Mulcahy,R.T., Reid,L.L., Disteche,C.M. and
            Kavanagh,T.J.
  TITLE     Mapping of the glutamate-cysteine ligase catalytic subunit gene
            (GLCLC) to human chromosome 6p12 and mouse chromosome 9D-E and of
            the regulatory subunit gene (GLCLR) to human chromosome 1p21-p22
            and mouse chromosome 3H1-3
  JOURNAL   Genomics 30 (3), 630-632 (1995)
   PUBMED   8825659
REFERENCE   9  (residues 1 to 252)
  AUTHORS   Gipp,J.J., Bailey,H.H. and Mulcahy,R.T.
  TITLE     Cloning and sequencing of the cDNA for the light subunit of human
            liver gamma-glutamylcysteine synthetase and relative mRNA levels
            for heavy and light subunits in human normal tissues
  JOURNAL   Biochem Biophys Res Commun 206 (2), 584-589 (1995)
   PUBMED   7826375
REFERENCE   10 (residues 1 to 252)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG501583.1, AB809606.1,
            BC041809.1, CB123306.1, CN272168.1, BQ049850.1, N53134.1,
            CN422503.1, BF513627.1, BM982562.1 and BU754400.1.
            
            On May 15, 2015 this sequence version replaced XP_005270811.1.
            
            Summary: Glutamate-cysteine ligase, also known as
            gamma-glutamylcysteine synthetase, is the first rate limiting
            enzyme of glutathione synthesis. The enzyme consists of two
            subunits, a heavy catalytic subunit and a light regulatory subunit.
            Gamma glutamylcysteine synthetase deficiency has been implicated in
            some forms of hemolytic anemia. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, Apr 2015].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1. It encodes
            isoform 2 which has the same N- and C-termini, but is shorter than
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1571919.1,
                                           SRR14038193.703065.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.1"
     Protein         1..252
                     /product="glutamate--cysteine ligase regulatory subunit
                     isoform 2"
                     /EC_number="6.3.2.2"
                     /note="GSC light chain; glutamate-cysteine ligase
                     (gamma-glutamylcysteine synthetase), regulatory (30.8kD);
                     glutamate-cysteine ligase regulatory protein; GCS light
                     chain; glutamate-cysteine ligase modifier subunit delta2
                     alternative splicing; gamma-ECS regulatory subunit;
                     gamma-glutamylcysteine synthetase regulatory subunit"
                     /calculated_mol_wt=28004
     Region          <64..>189
                     /region_name="AKR_SF"
                     /note="Aldo-keto reductase (AKR) superfamily; cl00470"
                     /db_xref="CDD:444925"
     CDS             1..252
                     /gene="GCLM"
                     /gene_synonym="GLCLR"
                     /coded_by="NM_001308253.2:268..1026"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS81352.1"
                     /db_xref="GeneID:2730"
                     /db_xref="HGNC:HGNC:4312"
                     /db_xref="MIM:601176"
ORIGIN      
        1 mgtdsraaka llarartlhl qtgnllnwgr lrkkcpsths eeefpdvlec tvshavekin
       61 pdereemkvs aklfivesns ssstrsavdm acsvlgvaql dsviiasppi edgvnlsleh
      121 lqpyweelen lvqskkivai gtsdldktql eqlyqwaqvk pnsnqvnlas ccvmppdlta
      181 fakqfdiqll thndpkells easfqealqe sipdiqahew vplwllrysv ivksrgiiks
      241 kgyilqakrr gs
//
LOCUS       NP_001349652             438 aa            linear   PRI 21-NOV-2025
DEFINITION  drebrin-like protein isoform f [Homo sapiens].
ACCESSION   NP_001349652 XP_011513627
VERSION     NP_001349652.1
DBSOURCE    REFSEQ: accession NM_001362723.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Ghosh,A., Enderlein,J. and Butkevich,E.
  TITLE     Dimerization of Human Drebrin-like Protein Governs Its Biological
            Activity
  JOURNAL   Biochemistry 59 (16), 1553-1558 (2020)
   PUBMED   32282191
  REMARK    GeneRIF: Dimerization of Human Drebrin-like Protein Governs Its
            Biological Activity.
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 438)
  AUTHORS   Yamazaki,H., Takahashi,H., Aoki,T. and Shirao,T.
  TITLE     Molecular cloning and dendritic localization of rat SH3P7
  JOURNAL   Eur J Neurosci 14 (6), 998-1008 (2001)
   PUBMED   11595038
REFERENCE   7  (residues 1 to 438)
  AUTHORS   Ensenat,D., Yao,Z., Wang,X.S., Kori,R., Zhou,G., Lee,S.C. and
            Tan,T.H.
  TITLE     A novel src homology 3 domain-containing adaptor protein, HIP-55,
            that interacts with hematopoietic progenitor kinase 1
  JOURNAL   J Biol Chem 274 (48), 33945-33950 (1999)
   PUBMED   10567356
  REMARK    Erratum:[J Biol Chem 2000 May 5;275(18):14004]
REFERENCE   8  (residues 1 to 438)
  AUTHORS   Lee,C.G., Morse,H.C. 3rd, Kay,B.K. and Kozak,C.A.
  TITLE     Genetic mapping of eight SH3 domain genes on seven mouse
            chromosomes
  JOURNAL   Mamm Genome 10 (4), 402-404 (1999)
   PUBMED   10087302
REFERENCE   9  (residues 1 to 438)
  AUTHORS   Larbolette,O., Wollscheid,B., Schweikert,J., Nielsen,P.J. and
            Wienands,J.
  TITLE     SH3P7 is a cytoskeleton adapter protein and is coupled to signal
            transduction from lymphocyte antigen receptors
  JOURNAL   Mol Cell Biol 19 (2), 1539-1546 (1999)
   PUBMED   9891087
REFERENCE   10 (residues 1 to 438)
  AUTHORS   Gipson,I.K., Spurr-Michaud,S., Moccia,R., Zhan,Q., Toribara,N.,
            Ho,S.B., Gargiulo,A.R. and Hill,J.A. 3rd.
  TITLE     MUC4 and MUC5B transcripts are the prevalent mucin messenger
            ribonucleic acids of the human endocervix
  JOURNAL   Biol Reprod 60 (1), 58-64 (1999)
   PUBMED   9858486
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC404852.1, AK027367.1, DT220937.1, BC011677.2 and AC017116.7.
            
            On Apr 26, 2018 this sequence version replaced XP_011513627.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.59269.1,
                                           SRR1803613.10717.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..438
                     /product="drebrin-like protein isoform f"
                     /note="src homology 3 domain-containing protein HIP-55;
                     drebrin-like protein; drebrin-F; cervical SH3P7; SH3
                     domain-containing protein 7; cervical mucin-associated
                     protein; HPK1-interacting protein of 55 kDa; actin-binding
                     protein 1"
                     /calculated_mol_wt=48824
     Region          3..138
                     /region_name="ADF_drebrin_like"
                     /note="ADF homology domain of drebrin and actin-binding
                     protein 1 (abp1); cd11281"
                     /db_xref="CDD:200437"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q62418; propagated from
                     UniProtKB/Swiss-Prot (Q9UJU6.1)"
     Site            order(78,92,119,122)
                     /site_type="other"
                     /note="putative F-actin interface [polypeptide binding]"
                     /db_xref="CDD:200437"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UJU6.1)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UJU6.1)"
     Site            176
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9UJU6.1)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UJU6.1)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     Phosphoserine. /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UJU6.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UJU6.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UJU6.1)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UJU6.1)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UJU6.1)"
     Site            296
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9UJU6.1)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UJU6.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q62418; propagated from
                     UniProtKB/Swiss-Prot (Q9UJU6.1)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q62418; propagated from
                     UniProtKB/Swiss-Prot (Q9UJU6.1)"
     Site            369..370
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3; propagated from
                     UniProtKB/Swiss-Prot (Q9UJU6.1)"
     Region          383..436
                     /region_name="SH3_Abp1_eu"
                     /note="Src homology 3 domain of eumetazoan Actin-binding
                     protein 1; cd11960"
                     /db_xref="CDD:212893"
     Site            order(388,390,393,396..397,415..416,428,430,432..433)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212893"
     CDS             1..438
                     /gene="DBNL"
                     /gene_synonym="ABP1; HIP-55; HIP55; SH3P7"
                     /coded_by="NM_001362723.2:37..1353"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="GeneID:28988"
                     /db_xref="HGNC:HGNC:2696"
                     /db_xref="MIM:610106"
ORIGIN      
        1 maanlsrngp alqeayvrvv teksptdwal ftyegnsndi rvagtgeggl eemveelnsg
       61 kvmyafcrvk dpnsglpkfv linwtgegvn dvrkgacash vstmasflkg ahvtinarae
      121 edvepecime kvakasgany sfhkesgrfq dvgpqapvgs vyqktnavse ikrvgkdsfw
      181 akaekeeenr rleekrraee aqrqleqerr erelreaarr eqryqeqgge aspqrtweqq
      241 qevvsrnrne qgstcaslqe savhpreifk qkeramstts isspqpgklr spflqkqltq
      301 pethfgrepa aaisrpradl paeepapstp pclvqaeeea vyeeppeqet fyeqpplvqq
      361 qgagsehidh hiqgqglsgq glcaralydy qaaddteisf dpenlitgie videgwwrgy
      421 gpdghfgmfp anyvelie
//
LOCUS       NP_001337843            1020 aa            linear   PRI 21-NOV-2025
DEFINITION  cytoplasmic dynein 2 intermediate chain 1 isoform b [Homo sapiens].
ACCESSION   NP_001337843 XP_016867872
VERSION     NP_001337843.1
DBSOURCE    REFSEQ: accession NM_001350914.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1020)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1020)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1020)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1020)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1020)
  AUTHORS   Vuolo,L., Stevenson,N.L., Mukhopadhyay,A.G., Roberts,A.J. and
            Stephens,D.J.
  TITLE     Cytoplasmic dynein-2 at a glance
  JOURNAL   J Cell Sci 133 (6) (2020)
   PUBMED   32229580
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1020)
  AUTHORS   Asante,D., Stevenson,N.L. and Stephens,D.J.
  TITLE     Subunit composition of the human cytoplasmic dynein-2 complex
  JOURNAL   J Cell Sci 127 (Pt 21), 4774-4787 (2014)
   PUBMED   25205765
REFERENCE   7  (residues 1 to 1020)
  AUTHORS   Taipale,M., Tucker,G., Peng,J., Krykbaeva,I., Lin,Z.Y., Larsen,B.,
            Choi,H., Berger,B., Gingras,A.C. and Lindquist,S.
  TITLE     A quantitative chaperone interaction network reveals the
            architecture of cellular protein homeostasis pathways
  JOURNAL   Cell 158 (2), 434-448 (2014)
   PUBMED   25036637
REFERENCE   8  (residues 1 to 1020)
  AUTHORS   McInerney-Leo,A.M., Schmidts,M., Cortes,C.R., Leo,P.J., Gener,B.,
            Courtney,A.D., Gardiner,B., Harris,J.A., Lu,Y., Marshall,M.,
            Scambler,P.J., Beales,P.L., Brown,M.A., Zankl,A., Mitchison,H.M.,
            Duncan,E.L. and Wicking,C.
  CONSRTM   UK10K Consortium
  TITLE     Short-rib polydactyly and Jeune syndromes are caused by mutations
            in WDR60
  JOURNAL   Am J Hum Genet 93 (3), 515-523 (2013)
   PUBMED   23910462
  REMARK    GeneRIF: These findings show that WDR60 mutations can cause
            skeletal ciliopathies and suggest a role for WDR60 in ciliogenesis.
REFERENCE   9  (residues 1 to 1020)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   10 (residues 1 to 1020)
  AUTHORS   Lettre,G., Jackson,A.U., Gieger,C., Schumacher,F.R., Berndt,S.I.,
            Sanna,S., Eyheramendy,S., Voight,B.F., Butler,J.L., Guiducci,C.,
            Illig,T., Hackett,R., Heid,I.M., Jacobs,K.B., Lyssenko,V., Uda,M.,
            Boehnke,M., Chanock,S.J., Groop,L.C., Hu,F.B., Isomaa,B., Kraft,P.,
            Peltonen,L., Salomaa,V., Schlessinger,D., Hunter,D.J., Hayes,R.B.,
            Abecasis,G.R., Wichmann,H.E., Mohlke,K.L. and Hirschhorn,J.N.
  CONSRTM   Diabetes Genetics Initiative; FUSION; KORA; Prostate, Lung
            Colorectal and Ovarian Cancer Screening Trial; Nurses' Health
            Study; SardiNIA
  TITLE     Identification of ten loci associated with height highlights new
            biological pathways in human growth
  JOURNAL   Nat Genet 40 (5), 584-591 (2008)
   PUBMED   18391950
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124833.1 and AC004863.5.
            
            On Apr 27, 2017 this sequence version replaced XP_016867872.1.
            
            Summary: This gene encodes a member of the WD repeat protein
            family. WD repeats are minimally conserved regions of approximately
            40 amino acids typically bracketed by gly-his and trp-asp (GH-WD)
            and may facilitate the formation of heterotrimeric or multiprotein
            complexes. Members of this family are involved in a variety of
            cellular processes including cell cycle progression, signal
            transduction, apoptosis, and gene regulation. The encoded protein
            contains four WD repeats and may play a role in the formation of
            cilia. Mutations in this gene have been associated with short-rib
            polydactyly and Jeune syndromes. [provided by RefSeq, Mar 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.265715.1,
                                           SRR18074969.3155225.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119, SAMEA2155751
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1020
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.3"
     Protein         1..1020
                     /product="cytoplasmic dynein 2 intermediate chain 1
                     isoform b"
                     /note="WD repeat-containing protein 60; testicular
                     secretory protein Li 66; WD repeat domain 60; cytoplasmic
                     dynein 2 intermediate chain 1"
                     /calculated_mol_wt=116882
     Region          <5..289
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          599..627
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          687..729
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          736..765
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          780..811
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <866..938
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          867..903
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..1020
                     /gene="DYNC2I1"
                     /gene_synonym="CFAP163; DIC6; FAP163; SRPS6; SRTD8; WDR60"
                     /coded_by="NM_001350914.2:378..3440"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:55112"
                     /db_xref="HGNC:HGNC:21862"
                     /db_xref="MIM:615462"
ORIGIN      
        1 mdlpehkepr crdpdqdars rdrvaevhta kesprgerdr drqrerrrda kdrekeklke
       61 khreaekshs rgkdrekekd rrarkeelrq tvahhnllgq etrdrqller aerkgrsvsk
      121 vrseekdeds ergdedrerr yrerklqygd skdnplkywl ykeegerrhr kprepdrdnk
      181 hreksstrek rekyskeksn sfsdkgeerh kekrhkegfh fdderhqsnv drkeksakde
      241 prkresqnge hrnrgasskr dgtssqhaen lvrnhgkdkd srrkhgheeg ssvwwkldqr
      301 pggeetveie keetdlenar adaytasced dfedyeddfe vcdgdddess nepesrekle
      361 elplaqkkei qeiqrainae nerigelslk lfqkrgrtef ekeprtdtns spsrasvcgi
      421 fvdfasashr qksrtqalkq kmrstkllrl idldfsftfs lldlppvney dmyirnfgkk
      481 ntkqayvqcn ednverdiqt eeietrevwt qhpgestvvs ggseqrdtsd avvmpkidtp
      541 rlcsflraac qvmavlleed rlaaepswnl raqdralyfs dsssqlntsl pflqnrkvss
      601 lhtsrvqrqm vvsvhdlpek sfvplldsky vlcvwdiwqp sgpqkvlice sqvtccclsp
      661 lkafllfagt ahgsvvvwdl redsrlhysv tlsdgfwtfr tatfstdgil tsvnhrsplq
      721 avepistsvh kkqsfvlspf stqeemsgls fhiasldesg vlnvwvvvel pkadiagsis
      781 dlglmpggrv klvhsaliql gdslshkgne fwgttqtlnv kflpsdpnhf iigtdmglis
      841 hgtrqdlrva pklfkpqqhg irpvkvnvid fspfgepifl agcsdgsirl hqlssafpll
      901 qwdsstdsha vtglqwsptr pavflvqddt sniyiwdllq sdlgpvakqq vspnrlvama
      961 avgepekagg sflalvlara sgsidiqhlk rrwaapevde cnrlrlllqe alwpegklhk
//
LOCUS       NP_573572                675 aa            linear   PRI 21-NOV-2025
DEFINITION  angiomotin isoform 2 [Homo sapiens].
ACCESSION   NP_573572
VERSION     NP_573572.1
DBSOURCE    REFSEQ: accession NM_133265.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 675)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   3  (residues 1 to 675)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 675)
  AUTHORS   Rheinemann,L., Thompson,T., Mercenne,G., Paine,E.L., Peterson,F.C.,
            Volkman,B.F., Alam,S.L., Alian,A. and Sundquist,W.I.
  TITLE     Interactions between AMOT PPxY motifs and NEDD4L WW domains
            function in HIV-1 release
  JOURNAL   J Biol Chem 297 (2), 100975 (2021)
   PUBMED   34284061
  REMARK    GeneRIF: Interactions between AMOT PPxY motifs and NEDD4L WW
            domains function in HIV-1 release.
REFERENCE   5  (residues 1 to 675)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 675)
  AUTHORS   Bratt,A., Wilson,W.J., Troyanovsky,B., Aase,K., Kessler,R., Van
            Meir,E.G. and Holmgren,L.
  TITLE     Angiomotin belongs to a novel protein family with conserved
            coiled-coil and PDZ binding domains
  JOURNAL   Gene 298 (1), 69-77 (2002)
   PUBMED   12406577
  REMARK    Erratum:[Gene. 2003 May 22;310;231. Meir, EG [corrected to Van
            Meir, EG]]
REFERENCE   7  (residues 1 to 675)
  AUTHORS   Zetter,B.R.
  TITLE     Hold that line. Angiomotin regulates endothelial cell motility
  JOURNAL   J Cell Biol 152 (6), F35-F36 (2001)
   PUBMED   11257132
REFERENCE   8  (residues 1 to 675)
  AUTHORS   Troyanovsky,B., Levchenko,T., Mansson,G., Matvijenko,O. and
            Holmgren,L.
  TITLE     Angiomotin: an angiostatin binding protein that regulates
            endothelial cell migration and tube formation
  JOURNAL   J Cell Biol 152 (6), 1247-1254 (2001)
   PUBMED   11257124
REFERENCE   9  (residues 1 to 675)
  AUTHORS   Rubinstein,M.H.
  TITLE     A new granulation method for compressed tablets [proceedings]
  JOURNAL   J Pharm Pharmacol 28 Suppl, 67P (1976)
   PUBMED   12345
REFERENCE   10 (residues 1 to 675)
  AUTHORS   Aoyagi,F., Fujino,T. and Ohshiro,T.
  TITLE     Detection of small vessels for microsurgery by a Doppler flowmeter
  JOURNAL   Plast Reconstr Surg 55 (3), 372-373 (1975)
   PUBMED   123345
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004827.1.
            
            Summary: This gene belongs to the motin family of angiostatin
            binding proteins characterized by conserved coiled-coil domains and
            C-terminal PDZ binding motifs. The encoded protein is expressed
            predominantly in endothelial cells of capillaries as well as larger
            vessels of the placenta where it may mediate the inhibitory effect
            of angiostatin on tube formation and the migration of endothelial
            cells toward growth factors during the formation of new blood
            vessels. Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF286598.1, SRR11853563.35447.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq23"
     Protein         1..675
                     /product="angiomotin isoform 2"
                     /calculated_mol_wt=72409
     Region          <24..>268
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          190..397
                     /region_name="Angiomotin_C"
                     /note="Angiomotin C terminal; pfam12240"
                     /db_xref="CDD:463503"
     CDS             1..675
                     /gene="AMOT"
                     /coded_by="NM_133265.5:813..2840"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS14563.1"
                     /db_xref="GeneID:154796"
                     /db_xref="HGNC:HGNC:17810"
                     /db_xref="MIM:300410"
ORIGIN      
        1 mpraqpssas yqpvpadpfa ivsraqqmve ilsdenrnlr qelegcyekv arlqkvetei
       61 qrvseayenl vkssskreal ekamrnkleg eirrmhdfnr dlrerletan kqlaekeyeg
      121 sedtrktisq lfaknkesqr ekekleaela tarstnedqr rhieirdqal snaqakvvkl
      181 eeelkkkqvy vdkvekmqqa lvqlqaacek reqlehrlrt rlereleslr iqqrqgncqp
      241 tnvseynaaa lmellrekee rilaleadmt kweqkyleen vmrhfaldaa atvaaqrdtt
      301 vishspntsy dtaleariqk eeeeilmank rcldmegrik tlhaqiiekd amikvlqqrs
      361 rkepskteql scmrpakslm sisnagsgll shsstltgsp imeekrddks wkgslgillg
      421 gdyraeyvps tpspvppstp llsahsktgs rdcstqterg tesnktaava pisvpapvaa
      481 aataaaitat aatitttmva aapvavaaaa apaaaaapsp ataaataaav spaaagqipa
      541 aasvasaaav apsaaaaaav qvapaapapv papalvpvpa paaaqasapa qtqaptsapa
      601 vaptpaptpt pavaqaevpa spatgpgphr lsipsltcnp dktdgpvfhs ntlerktpiq
      661 ilgqepdaem veyli
//
LOCUS       NP_001337450            2460 aa            linear   PRI 21-NOV-2025
DEFINITION  myomegalin isoform 11 [Homo sapiens].
ACCESSION   NP_001337450 XP_016858369
VERSION     NP_001337450.1
DBSOURCE    REFSEQ: accession NM_001350521.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2460)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2460)
  AUTHORS   Pan,R., Dai,J., Liang,W., Wang,H., Ye,L., Ye,S., Lin,Z., Huang,S.,
            Xiong,Y., Zhang,L., Lu,L., Wang,O., Shen,X., Liao,W. and Lu,X.
  TITLE     PDE4DIP contributes to colorectal cancer growth and chemoresistance
            through modulation of the NF1/RAS signaling axis
  JOURNAL   Cell Death Dis 14 (6), 373 (2023)
   PUBMED   37355626
  REMARK    GeneRIF: PDE4DIP contributes to colorectal cancer growth and
            chemoresistance through modulation of the NF1/RAS signaling axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2460)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   4  (residues 1 to 2460)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 2460)
  AUTHORS   Abou Ziki,M.D., Bhat,N., Neogi,A., Driscoll,T.P., Ugwu,N., Liu,Y.,
            Smith,E., Abboud,J.M., Chouairi,S., Schwartz,M.A., Akar,J.G. and
            Mani,A.
  TITLE     Epistatic interaction of PDE4DIP and DES mutations in familial
            atrial fibrillation with slow conduction
  JOURNAL   Hum Mutat 42 (10), 1279-1293 (2021)
   PUBMED   34289528
  REMARK    GeneRIF: Epistatic interaction of PDE4DIP and DES mutations in
            familial atrial fibrillation with slow conduction.
REFERENCE   6  (residues 1 to 2460)
  AUTHORS   Shimada,H., Kuboshima,M., Shiratori,T., Nabeya,Y., Takeuchi,A.,
            Takagi,H., Nomura,F., Takiguchi,M., Ochiai,T. and Hiwasa,T.
  TITLE     Serum anti-myomegalin antibodies in patients with esophageal
            squamous cell carcinoma
  JOURNAL   Int J Oncol 30 (1), 97-103 (2007)
   PUBMED   17143517
  REMARK    GeneRIF: MMGL-antibody is significantly with a favorable prognosis.
            Consequently, MMGL-anatibodies may be a useful tumor marker to
            diagnose and establish a prognosis in patients with esophageal
            squamous cell carcinoma.
REFERENCE   7  (residues 1 to 2460)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 2460)
  AUTHORS   Soejima,H., Kawamoto,S., Akai,J., Miyoshi,O., Arai,Y., Morohka,T.,
            Matsuo,S., Niikawa,N., Kimura,A., Okubo,K. and Mukai,T.
  TITLE     Isolation of novel heart-specific genes using the BodyMap database
  JOURNAL   Genomics 74 (1), 115-120 (2001)
   PUBMED   11374908
REFERENCE   9  (residues 1 to 2460)
  AUTHORS   Verde,I., Pahlke,G., Salanova,M., Zhang,G., Wang,S., Coletti,D.,
            Onuffer,J., Jin,S.L. and Conti,M.
  TITLE     Myomegalin is a novel protein of the golgi/centrosome that
            interacts with a cyclic nucleotide phosphodiesterase
  JOURNAL   J Biol Chem 276 (14), 11189-11198 (2001)
   PUBMED   11134006
REFERENCE   10 (residues 1 to 2460)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC245389.1, AC239802.3 and
            AC239804.2.
            
            On Apr 17, 2017 this sequence version replaced XP_016858369.1.
            
            Summary: The protein encoded by this gene serves to anchor
            phosphodiesterase 4D to the Golgi/centrosome region of the cell.
            Defects in this gene may be a cause of myeloproliferative disorder
            (MBD) associated with eosinophilia. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..2460
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     Protein         1..2460
                     /product="myomegalin isoform 11"
                     /note="myomegalin; cardiomyopathy-associated protein 2"
                     /calculated_mol_wt=278598
     Region          140..816
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          143..210
                     /region_name="Cnn_1N"
                     /note="Centrosomin N-terminal motif 1; pfam07989"
                     /db_xref="CDD:462333"
     Region          492..1248
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          1689..1758
                     /region_name="Olduvai"
                     /note="Olduvai domain; pfam06758"
                     /db_xref="CDD:429104"
     Region          <1978..>2155
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..2460
                     /gene="PDE4DIP"
                     /gene_synonym="CMYA2; MMGL"
                     /coded_by="NM_001350521.4:72..7454"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:9659"
                     /db_xref="HGNC:HGNC:15580"
                     /db_xref="MIM:608117"
ORIGIN      
        1 mkgtdsgscc rrrcdfgccc rasrrahytp yrsgdatrtp qsprqtpsre rrrpepagsw
       61 aaaaeeeeaa aaatpwmrdy faeddgemvp rtshtaafls dtkdrgppvq sqiwrsgekv
      121 pfvqtyslra fekppqvqtq alrdfekhln dlkkenfslk lriyfleerm qqkyeasred
      181 iykrnielkv eveslkrelq dkkqhldktw advenlnsqn eaelrrqfee rqqetehvye
      241 llenkiqllq eesrlaknea armaalveae kecnlelsek lkgvtknwed vpgdqvkpdq
      301 ytealaqrdk rieelnqsla aqerlveqls rekqqllhll eeptsmevqp mteellkqqk
      361 lnshettitq qsvsdshlae lqekiqqtea tnkilqekln emsyelkcaq essqkqdgti
      421 qnlketlksr ereteelyqv iegqndtmak lremlhqsql gqlhssegts paqqqvalld
      481 lqsalfcsql eiqklqrvvr qkerqladak qcvqfveaaa heseqqkeas wkhnqelrka
      541 lqqlqeelqn ksqqlrawea ekyneirtqe qniqhlnhsl shkeqllqef rellqyrdns
      601 dktleaneml leklrqrihd kavaleraid ekfsaleeke kelrqlrlav rerdhdlerl
      661 rdvlssneat mqsmesllra kgleveqlst tcqnlqwlke emetkfsrwq keqesiiqql
      721 qtslhdrnke vedlsatllc klgpgqseia eelcqrlqrk ermlqdllsd rnkqvlehem
      781 eiqgllqsvs treqesqaaa eklvqalmer nselqalrqy lggrdslmsq apisnqqaev
      841 tptgrlgkqt dqgsmqipsr ddstsltake dvsiprstlg dldtvaglek elsnakeele
      901 lmakkeresq melsalqsmm avqeeelqvq aadmesltrn iqikedlikd lqmqlvdped
      961 ipamerltqe vlllrekvas vesqgqeisg nrrqqlllml eglvdersrl nealqaerql
     1021 ysslvkfhah pesserdrtl qvelegaqvl rsrleevlgr slerlnrlet laaiggaaag
     1081 ddtedtstef tdsieeeaah hshqqlvkva lekslatvet qnpsfsppsp mggdsnrclq
     1141 eemlhlraef hqhleekrka eeelkelkaq ieeagfssvs hirntmlslc lenaelkeqm
     1201 geamsdgwei eedkekgevm vetvvtkegl sesslqaefr klqgklknah niinllkeql
     1261 vlsskegnsk ltpellvhlt stierintel vgspgkhqhq eegnvtvrpf prpqsldlga
     1321 tftvdahqld nqsqprdpgp qsafslpgst qhlrsqlsqc kqryqdlqek lllseatvfa
     1381 qanelekyrv mltgeslvkq dskqiqvdlq dlgyetcgrs eneaereett speceehnsl
     1441 kemvlmeglc seqgrrgstl assserkple nqlgkqeefr vygksenilv lrkdikdlka
     1501 qlqnankviq nlksrvrsls vtsdysssle rprklravgt legssphsvp dedegwlsdg
     1561 tgafyspglq akkdlesliq rvsqleaqlp kngleeklae elrsaswpgk ydsliqdqar
     1621 elsylrqkir egrgicylit rhakdtvksf edllrsndid yylgqsfreq laqgsqlter
     1681 ltsklstkdh ksekdqagle plalrlsrel qekekvievl qakldarslt pssshalsds
     1741 hrspsstsfl sdeleacsdm divseythye ekkaspshsd sihhsshsav lsskpsstsa
     1801 sqgakaesns npislptpqn tpkeanqahs gfhfhsipkl aslpqaplps apssflpfsp
     1861 tgplllgcce tpvvslaeaq qelqmlqkql gesastvppa statllsndl eadssyylns
     1921 aqphspprgt ielgrilepg ylgssgkwdv mrpqkgsvsg dlssgssvyq lnskptgadl
     1981 leehlgeirn lrqrleesic indrlreqle hrltstargr gstsnfysqg lesipqlcne
     2041 nrvlrednrr lqaqlshvsr ehsqeteslr eallssrshl qelekelehq kverqqlled
     2101 lrekqqevlh freerlslqe ndsrlqhklv llqqqceekq qlfeslqsel qiyealygns
     2161 kkglkaysld achqiplssd lshlvaevra lrgqleqsiq gnnclrlqlq qqlesgagka
     2221 slspssinqn fpastdpgnk qlllqglgld tspvmktppk legdatdgsf ankhgrhvig
     2281 hiddysalrq qiaegkllvk kivslvrsac sfpgleaqgt evlgskgihe lrsstsalhh
     2341 aleesasllt mfwraalpst hipvlpgkvg esterellel rtkvskqerl lqsttehlkn
     2401 anqqkesmeq fivsqltrth dvlkkartnl eepckkrshq kslkqqerwa cppfvqlpic
//
LOCUS       NP_001363713             518 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 43 [Homo sapiens].
ACCESSION   NP_001363713
VERSION     NP_001363713.1
DBSOURCE    REFSEQ: accession NM_001376784.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Muckenfuss,L.M., Migenda Herranz,A.C., Boneberg,F.M., Clerici,M.
            and Jinek,M.
  TITLE     Fip1 is a multivalent interaction scaffold for processing factors
            in human mRNA 3' end biogenesis
  JOURNAL   Elife 11, e80332 (2022)
   PUBMED   36073787
  REMARK    GeneRIF: Fip1 is a multivalent interaction scaffold for processing
            factors in human mRNA 3' end biogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Tennenbaum,J., Groh,M., Venditti,L., Campos-Gazeau,F., Chalayer,E.,
            De Broucker,T., Hamidou,M., Hunault,M., Lyoubi,A., Meunier,R.,
            Muron,T., Sene,D., Slama,B., Guidoux,C., Lefevre,G., Kahn,J.E.,
            Denier,C. and Rohmer,J.
  TITLE     FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a Treatable
            Cause of Watershed Infarction
  JOURNAL   Stroke 52 (10), e605-e609 (2021)
   PUBMED   34304603
  REMARK    GeneRIF: FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a
            Treatable Cause of Watershed Infarction.
REFERENCE   4  (residues 1 to 518)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 518)
  AUTHORS   Helbig,G., Lewandowski,K., Swiderska,A., Rodzaj,M., Seferynska,I.
            and Gajkowska-Kulik,J.
  TITLE     Exquisite response to imatinib mesylate in FIP1L1-PDGFRA-mutated
            hypereosinophilic syndrome: a 12-year experience of the Polish
            Hypereosinophilic Syndrome Study Group
  JOURNAL   Pol Arch Intern Med 130 (3), 255-257 (2020)
   PUBMED   32125294
  REMARK    GeneRIF: Exquisite response to imatinib mesylate in
            FIP1L1-PDGFRA-mutated hypereosinophilic syndrome: a 12-year
            experience of the Polish Hypereosinophilic Syndrome Study Group.
REFERENCE   6  (residues 1 to 518)
  AUTHORS   Cools,J., Quentmeier,H., Huntly,B.J., Marynen,P., Griffin,J.D.,
            Drexler,H.G. and Gilliland,D.G.
  TITLE     The EOL-1 cell line as an in vitro model for the study of
            FIP1L1-PDGFRA-positive chronic eosinophilic leukemia
  JOURNAL   Blood 103 (7), 2802-2805 (2004)
   PUBMED   14630792
  REMARK    GeneRIF: results indicate that the fusion of FIP1L1 to PDGFRA
            occurs rarely in leukemia cell lines
REFERENCE   7  (residues 1 to 518)
  AUTHORS   Kaufmann,I., Martin,G., Friedlein,A., Langen,H. and Keller,W.
  TITLE     Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements
            and stimulates poly(A) polymerase
  JOURNAL   EMBO J 23 (3), 616-626 (2004)
   PUBMED   14749727
REFERENCE   8  (residues 1 to 518)
  AUTHORS   Pardanani,A., Ketterling,R.P., Brockman,S.R., Flynn,H.C.,
            Paternoster,S.F., Shearer,B.M., Reeder,T.L., Li,C.Y., Cross,N.C.,
            Cools,J., Gilliland,D.G., Dewald,G.W. and Tefferi,A.
  TITLE     CHIC2 deletion, a surrogate for FIP1L1-PDGFRA fusion, occurs in
            systemic mastocytosis associated with eosinophilia and predicts
            response to imatinib mesylate therapy
  JOURNAL   Blood 102 (9), 3093-3096 (2003)
   PUBMED   12842979
  REMARK    GeneRIF: observations suggest that the FIP1L1-PDGFRA rearrangement
            occurs in an early hematopoietic progenitor and suggests that the
            molecular pathogenesis for a subset of SMCD patients is similar to
            that of HES
REFERENCE   9  (residues 1 to 518)
  AUTHORS   Griffin,J.H., Leung,J., Bruner,R.J., Caligiuri,M.A. and
            Briesewitz,R.
  TITLE     Discovery of a fusion kinase in EOL-1 cells and idiopathic
            hypereosinophilic syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (13), 7830-7835 (2003)
   PUBMED   12808148
REFERENCE   10 (residues 1 to 518)
  AUTHORS   Cools,J., DeAngelo,D.J., Gotlib,J., Stover,E.H., Legare,R.D.,
            Cortes,J., Kutok,J., Clark,J., Galinsky,I., Griffin,J.D.,
            Cross,N.C., Tefferi,A., Malone,J., Alam,R., Schrier,S.L.,
            Schmid,J., Rose,M., Vandenberghe,P., Verhoef,G., Boogaerts,M.,
            Wlodarska,I., Kantarjian,H., Marynen,P., Coutre,S.E., Stone,R. and
            Gilliland,D.G.
  TITLE     A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes
            as a therapeutic target of imatinib in idiopathic hypereosinophilic
            syndrome
  JOURNAL   N Engl J Med 348 (13), 1201-1214 (2003)
   PUBMED   12660384
  REMARK    GeneRIF: The hypereosinophilic syndrome may result from a novel
            fusion tyrosine kinase - FIP1L1-PDGFRalpha - that is a consequence
            of an interstitial chromosomal deletion.
            GeneRIF: Describes the fusion gene Fip1-like-1-PDGFRalpha in
            patients with idiopathic hypereosinophilic syndrome, mostly
            responsive to imatinib therapy.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098821.3 and AC058822.6.
            
            Summary: This gene encodes a subunit of the CPSF (cleavage and
            polyadenylation specificity factor) complex that polyadenylates the
            3' end of mRNA precursors. This gene, the homolog of yeast Fip1
            (factor interacting with PAP), binds to U-rich sequences of
            pre-mRNA and stimulates poly(A) polymerase activity. Its N-terminus
            contains a PAP-binding site and its C-terminus an RNA-binding
            domain. An interstitial chromosomal deletion on 4q12 creates an
            in-frame fusion of human genes FIP1L1 and PDGFRA (platelet-derived
            growth factor receptor, alpha). The FIP1L1-PDGFRA fusion gene
            encodes a constitutively activated tyrosine kinase that joins the
            first 233 amino acids of FIP1L1 to the last 523 amino acids of
            PDGFRA. This gene fusion and chromosomal deletion is the cause of
            some forms of idiopathic hypereosinophilic syndrome (HES). This
            syndrome, recently reclassified as chronic eosinophilic leukemia
            (CEL), is responsive to treatment with tyrosine kinase inhibitors.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.470009.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..518
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     43"
                     /note="rearranged in hypereosinophilia; pre-mRNA
                     3'-end-processing factor FIP1; FIP1-like 1 protein; factor
                     interacting with PAP; FIP1 like 1; FIP1L1 cleavage and
                     polyadenylation specific factor subunit"
                     /calculated_mol_wt=56077
     Region          139..181
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     CDS             1..518
                     /gene="FIP1L1"
                     /gene_synonym="FIP1; hFip1; Rhe"
                     /coded_by="NM_001376784.1:199..1755"
                     /note="isoform 43 is encoded by transcript variant 43"
                     /db_xref="GeneID:81608"
                     /db_xref="HGNC:HGNC:19124"
                     /db_xref="MIM:607686"
ORIGIN      
        1 msageverlv selsggtggd eeeewlygde neverpeeen asanppsgie detaengvpk
       61 pkvtetedds dsdsdddedd vhvtigdikt gapqygsygt apvnlniktg grvygttgtk
      121 vkgvdldapg singvpllev dldsfedkpw rkpgadlsdy fnygfnedtw kaycekqkri
      181 rmglevipvt sttnkitqgr tgnseketal pstkaeftsp pslfktglpp srnstssqsq
      241 tstasrkans svgkwqdryg raespdlrrl pgaidvigqt itisrvegrr ranensniqv
      301 lsersatevd nnfskpppff ppgappthlp pppflppppt vstapplipp pgipitvppp
      361 gfppppgapp psliptiesg hssgydsrsa rafpygnamk ndtdtgnmqk evmsvteqve
      421 kkkndiekdd tgrkrkpdis llevivdvam kvkkeivtgd tntknlkeak kekkravslp
      481 lnrrapklhl qnrhgfgllc ilvpevdtin lvifldnv
//
LOCUS       NP_001358097            1211 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal cell adhesion molecule isoform D precursor [Homo sapiens].
ACCESSION   NP_001358097
VERSION     NP_001358097.1
DBSOURCE    REFSEQ: accession NM_001371168.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1211)
  AUTHORS   Wang,C., Wang,Z., Fu,L., Du,J., Ji,F. and Qiu,X.
  TITLE     CircNRCAM up-regulates NRCAM to promote papillary thyroid carcinoma
            progression
  JOURNAL   J Endocrinol Invest 47 (5), 1215-1226 (2024)
   PUBMED   38485895
  REMARK    GeneRIF: CircNRCAM up-regulates NRCAM to promote papillary thyroid
            carcinoma progression.
REFERENCE   2  (residues 1 to 1211)
  AUTHORS   Zhou,L., He,L., Liu,C.H., Qiu,H., Zheng,L., Sample,K.M., Wu,Q.,
            Li,J., Xie,K., Ampuero,J., Li,Z., Lv,D., Liu,M., Romero-Gomez,M.,
            Hu,Y. and Tang,H.
  TITLE     Liver cancer stem cell dissemination and metastasis: uncovering the
            role of NRCAM in hepatocellular carcinoma
  JOURNAL   J Exp Clin Cancer Res 42 (1), 311 (2023)
   PUBMED   37993901
  REMARK    GeneRIF: Liver cancer stem cell dissemination and metastasis:
            uncovering the role of NRCAM in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1211)
  AUTHORS   Sannes,A.C., Christensen,J.O., Nielsen,M.B. and Gjerstad,J.
  TITLE     Stress-induced headache in the general working population is
            moderated by the NRCAM rs2300043 genotype
  JOURNAL   Scand J Pain 23 (2), 326-332 (2022)
   PUBMED   36181733
  REMARK    GeneRIF: Stress-induced headache in the general working population
            is moderated by the NRCAM rs2300043 genotype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1211)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 1211)
  AUTHORS   Bai,C. and Chen,D.G.
  TITLE     NRCAM acts as a prognostic biomarker and promotes the tumor
            progression in gastric cancer via EMT pathway
  JOURNAL   Tissue Cell 77, 101859 (2022)
   PUBMED   35763884
  REMARK    GeneRIF: NRCAM acts as a prognostic biomarker and promotes the
            tumor progression in gastric cancer via EMT pathway.
REFERENCE   6  (residues 1 to 1211)
  AUTHORS   Wang,B., Williams,H., Du,J.S., Terrett,J. and Kenwrick,S.
  TITLE     Alternative splicing of human NrCAM in neural and nonneural tissues
  JOURNAL   Mol Cell Neurosci 10 (5-6), 287-295 (1998)
   PUBMED   9604207
REFERENCE   7  (residues 1 to 1211)
  AUTHORS   Grumet,M.
  TITLE     Nr-CAM: a cell adhesion molecule with ligand and receptor functions
  JOURNAL   Cell Tissue Res 290 (2), 423-428 (1997)
   PUBMED   9321706
  REMARK    Review article
REFERENCE   8  (residues 1 to 1211)
  AUTHORS   Sakurai,T., Lustig,M., Nativ,M., Hemperly,J.J., Schlessinger,J.,
            Peles,E. and Grumet,M.
  TITLE     Induction of neurite outgrowth through contactin and Nr-CAM by
            extracellular regions of glial receptor tyrosine phosphatase beta
  JOURNAL   J Cell Biol 136 (4), 907-918 (1997)
   PUBMED   9049255
REFERENCE   9  (residues 1 to 1211)
  AUTHORS   Volkmer,H., Leuschner,R., Zacharias,U. and Rathjen,F.G.
  TITLE     Neurofascin induces neurites by heterophilic interactions with
            axonal NrCAM while NrCAM requires F11 on the axonal surface to
            extend neurites
  JOURNAL   J Cell Biol 135 (4), 1059-1069 (1996)
   PUBMED   8922386
REFERENCE   10 (residues 1 to 1211)
  AUTHORS   Lane,R.P., Chen,X.N., Yamakawa,K., Vielmetter,J., Korenberg,J.R.
            and Dreyer,W.J.
  TITLE     Characterization of a highly conserved human homolog to the chicken
            neural cell surface protein Bravo/Nr-CAM that maps to chromosome
            band 7q31
  JOURNAL   Genomics 35 (3), 456-465 (1996)
   PUBMED   8812479
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005058.1, AC007567.2 and
            AC005683.2.
            
            Summary: Cell adhesion molecules (CAMs) are members of the
            immunoglobulin superfamily. This gene encodes a neuronal cell
            adhesion molecule with multiple immunoglobulin-like C2-type domains
            and fibronectin type-III domains. This ankyrin-binding protein is
            involved in neuron-neuron adhesion and promotes directional
            signaling during axonal cone growth. This gene is also expressed in
            non-neural tissues and may play a general role in cell-cell
            communication via signaling from its intracellular domain to the
            actin cytoskeleton during directional cell migration. Allelic
            variants of this gene have been associated with autism and
            addiction vulnerability. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (14), as well as variants 4, 12,
            and 13, encodes isoform D.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1211
                     /product="neuronal cell adhesion molecule isoform D
                     precursor"
                     /note="NgCAM-related cell adhesion molecule; neuronal
                     surface protein Bravo"
                     /calculated_mol_wt=130517
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3315
     Region          46..140
                     /region_name="IgI_NrCAM"
                     /note="Immunoglobulin (Ig)-like domain of NrCAM (Ng
                     (neuronglia) CAM-related cell adhesion molecule); member
                     of the I-set of Ig superfamily (IgSF) domains; cd05874"
                     /db_xref="CDD:409458"
     Region          46..50
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409458"
     Region          55..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409458"
     Region          64..71
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409458"
     Region          77..82
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409458"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          85..87
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409458"
     Region          94..97
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409458"
     Region          102..106
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409458"
     Region          119..127
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409458"
     Region          130..140
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409458"
     Region          149..238
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          163..167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          177..181
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          200..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          215..220
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          231..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            245
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            251
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          277..358
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          288..292
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          301..305
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            314
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          323..327
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          337..342
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          350..353
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          362..450
                     /region_name="Ig4_NrCAM"
                     /note="Fourth immunoglobulin (Ig)-like domain of NrCAM
                     (NgCAM-related cell adhesion molecule); cd05868"
                     /db_xref="CDD:409454"
     Region          378..382
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409454"
     Region          391..395
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409454"
     Region          415..419
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409454"
     Region          429..434
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409454"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          442..445
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409454"
     Region          459..542
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          472..476
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          485..489
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            507
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          508..512
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          522..527
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          535..538
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          546..1060
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            619
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          647..737
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(647,713,728)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            716
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            order(729..730,732..733)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            802
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            858
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            993
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1009
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1019
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          1098..1187
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     CDS             1..1211
                     /gene="NRCAM"
                     /gene_synonym="NEDNMS"
                     /coded_by="NM_001371168.1:680..4315"
                     /note="isoform D precursor is encoded by transcript
                     variant 14"
                     /db_xref="CCDS:CCDS75652.1"
                     /db_xref="GeneID:4897"
                     /db_xref="HGNC:HGNC:7994"
                     /db_xref="MIM:601581"
ORIGIN      
        1 mqlkimpkkk rlsagrvpli lflcqmisal evpldpklle dlvqpptitq qspkdyiidp
       61 reniviqcea kgkpppsfsw trngthfdid kdplvtmkpg tgtliinims egkaetyegv
      121 yqctarnerg aavsnnivvr psrsplwtke klepitlqsg qslvlpcrpp iglpppiifw
      181 mdnsfqrlpq servsqglng dlyfsnvlpe dtredyicya rfnhtqtiqq kqpisvkvis
      241 vdelndtiaa nlsdtefyga kssrerpptf ltpegnasnk eelrgnvlsl eciaeglptp
      301 iiywakedgm lpknrtvykn fektlqiihv seadsgnyqc iaknalgaih htisvrvkaa
      361 pywitapqnl vlspgedgtl icrangnpkp riswltngvp ieiapddpsr kidgdtiifs
      421 nvqerssavy qcnasneygy llanafvnvl aeppriltpa ntlyqvianr palldcaffg
      481 splptiewfk gakgsalhed iyvlhengtl eipvaqkdst gtytcvarnk lgmaknevhl
      541 eikdptwivk qpeyavvqrg smvsfeckvk hdhtlsltvl wlkdnrelps derftvdkdh
      601 lvvadvsddd sgtytcvant tldsvsasav lsvvaptptp apvydvpnpp fdleltdqld
      661 ksvqlswtpg ddnnspitkf iieyedamhk pglwhhqtev sgtqttaqlk lspyvnysfr
      721 vmavnsigks lpseaseqyl tkasepdknp taveglgsep dnlvitwkpl ngfesngpgl
      781 qykvswrqkd gddewtsvvv anvskyivsg tptfvpylik vqalndmgfa pepavvmghs
      841 gedlpmvapg nvrvnvvnst laevhwdpvp lksirghlqg yriyywktqs sskrnrrhie
      901 kkiltfqgsk thgmlpglep fshytlnvrv vngkgegpas pdrvfntpeg vpsapsslki
      961 vnptldsltl ewdppshpng ilteytlkyq pinsthelgp lvdlkipank trwtlknlnf
     1021 strykfyfya qtsagsgsqi teeavttvde agilppdvga gkamasrqvd iatqgwfigl
     1081 mcavallili llivcfirrn kggkypvkek edahadpeiq pmkeddgtfg eysdaedhkp
     1141 lkkgsrtpsd rtvkkedsdd slvdygegvn gqfnedgsfi gqysgkkeke paegnessea
     1201 pspvnamnsf v
//
LOCUS       NP_001265547             362 aa            linear   PRI 21-NOV-2025
DEFINITION  tyrosine-protein phosphatase non-receptor type 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001265547
VERSION     NP_001265547.1
DBSOURCE    REFSEQ: accession NM_001278618.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Coronell-Tovar,A., Pardo,J.P., Rodriguez-Romero,A.,
            Sosa-Peinado,A., Vasquez-Bochm,L., Cano-Sanchez,P.,
            Alvarez-Anorve,L.I. and Gonzalez-Andrade,M.
  TITLE     Protein tyrosine phosphatase 1B (PTP1B) function, structure, and
            inhibition strategies to develop antidiabetic drugs
  JOURNAL   FEBS Lett 598 (15), 1811-1838 (2024)
   PUBMED   38724486
  REMARK    GeneRIF: Protein tyrosine phosphatase 1B (PTP1B) function,
            structure, and inhibition strategies to develop antidiabetic drugs.
            Review article
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Datta,R., Mukherjee,D., Podolsky,M.J., Yang,C.D., Alba,D.L.,
            Singh,S., Arnold,T.D., Koliwad,S., Lizama,C.O. and Atabai,K.
  TITLE     PTP1B mediates the inhibitory effect of MFGE8 on insulin signaling
            through the beta5 integrin
  JOURNAL   J Biol Chem 300 (2), 105631 (2024)
   PUBMED   38199575
  REMARK    GeneRIF: PTP1B mediates the inhibitory effect of MFGE8 on insulin
            signaling through the beta5 integrin.
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Sharma,S., Skaist Mehlman,T., Sagabala,R.S., Boivin,B. and
            Keedy,D.A.
  TITLE     High-resolution double vision of the allosteric phosphatase PTP1B
  JOURNAL   Acta Crystallogr F Struct Biol Commun 80 (Pt 1), 1-12 (2024)
   PUBMED   38133579
  REMARK    GeneRIF: High-resolution double vision of the allosteric
            phosphatase PTP1B.
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Hsu,M.F., Ito,Y., Singh,J.P., Hsu,S.F., Wells,A., Jen,K.Y.,
            Meng,T.C. and Haj,F.G.
  TITLE     Protein tyrosine phosphatase 1B is a regulator of alpha-actinin4 in
            the glomerular podocyte
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (1), 119590 (2024)
   PUBMED   37730132
  REMARK    GeneRIF: Protein tyrosine phosphatase 1B is a regulator of
            alpha-actinin4 in the glomerular podocyte.
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Chen,J., Parsons,S. and Brautigan,D.L.
  TITLE     Tyrosine phosphorylation of protein phosphatase 2A in response to
            growth stimulation and v-src transformation of fibroblasts
  JOURNAL   J Biol Chem 269 (11), 7957-7962 (1994)
   PUBMED   7510677
REFERENCE   7  (residues 1 to 362)
  AUTHORS   Frangioni,J.V., Beahm,P.H., Shifrin,V., Jost,C.A. and Neel,B.G.
  TITLE     The nontransmembrane tyrosine phosphatase PTP-1B localizes to the
            endoplasmic reticulum via its 35 amino acid C-terminal sequence
  JOURNAL   Cell 68 (3), 545-560 (1992)
   PUBMED   1739967
REFERENCE   8  (residues 1 to 362)
  AUTHORS   Brown-Shimer,S., Johnson,K.A., Lawrence,J.B., Johnson,C.,
            Bruskin,A., Green,N.R. and Hill,D.E.
  TITLE     Molecular cloning and chromosome mapping of the human gene encoding
            protein phosphotyrosyl phosphatase 1B
  JOURNAL   Proc Natl Acad Sci U S A 87 (13), 5148-5152 (1990)
   PUBMED   2164224
REFERENCE   9  (residues 1 to 362)
  AUTHORS   Chernoff,J., Schievella,A.R., Jost,C.A., Erikson,R.L. and Neel,B.G.
  TITLE     Cloning of a cDNA for a major human protein-tyrosine-phosphatase
  JOURNAL   Proc Natl Acad Sci U S A 87 (7), 2735-2739 (1990)
   PUBMED   2157211
REFERENCE   10 (residues 1 to 362)
  AUTHORS   Charbonneau,H., Tonks,N.K., Kumar,S., Diltz,C.D., Harrylock,M.,
            Cool,D.E., Krebs,E.G., Fischer,E.H. and Walsh,K.A.
  TITLE     Human placenta protein-tyrosine-phosphatase: amino acid sequence
            and relationship to a family of receptor-like proteins
  JOURNAL   Proc Natl Acad Sci U S A 86 (14), 5252-5256 (1989)
   PUBMED   2546149
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK299830.1, BC015660.2,
            DB332370.1, AI474453.1 and AL133230.25.
            
            Summary: The protein encoded by this gene is the founding member of
            the protein tyrosine phosphatase (PTP) family, which was isolated
            and identified based on its enzymatic activity and amino acid
            sequence. PTPs catalyze the hydrolysis of the phosphate monoesters
            specifically on tyrosine residues. Members of the PTP family share
            a highly conserved catalytic motif, which is essential for the
            catalytic activity. PTPs are known to be signaling molecules that
            regulate a variety of cellular processes including cell growth,
            differentiation, mitotic cycle, and oncogenic transformation. This
            PTP has been shown to act as a negative regulator of insulin
            signaling by dephosphorylating the phosphotryosine residues of
            insulin receptor kinase. This PTP was also reported to
            dephosphorylate epidermal growth factor receptor kinase, as well as
            JAK2 and TYK2 kinases, which implicated the role of this PTP in
            cell growth control, and cell response to interferon stimulation.
            Two transcript variants encoding different isoforms have been found
            for this gene. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (2) lacks an alternate exon in the
            5' coding region and uses a downstream start codon compared to
            variant 1. It encodes isoform 2, which has a shorter N-terminus
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK299830.1, SRR14038196.2100279.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.13"
     Protein         1..362
                     /product="tyrosine-protein phosphatase non-receptor type 1
                     isoform 2"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase, placental;
                     protein-tyrosine phosphatase 1B"
                     /calculated_mol_wt=41129
     Region          <1..219
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     CDS             1..362
                     /gene="PTPN1"
                     /gene_synonym="PTP1B"
                     /coded_by="NM_001278618.2:274..1362"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS63309.1"
                     /db_xref="GeneID:5770"
                     /db_xref="HGNC:HGNC:9642"
                     /db_xref="MIM:176885"
ORIGIN      
        1 meeaqrsyil tqgplpntcg hfwemvweqk srgvvmlnrv mekgslkcaq ywpqkeekem
       61 ifedtnlklt lisediksyy tvrqlelenl ttqetreilh fhyttwpdfg vpespasfln
      121 flfkvresgs lspehgpvvv hcsagigrsg tfcladtcll lmdkrkdpss vdikkvllem
      181 rkfrmgliqt adqlrfsyla viegakfimg dssvqdqwke lshedleppp ehipppprpp
      241 krilephngk creffpnhqw vkeetqedkd cpikeekgsp lnaapygies msqdtevrsr
      301 vvggslrgaq aaspakgeps lpekdedhal sywkpflvnm cvatvltaga ylcyrflfns
      361 nt
//
LOCUS       NP_001096034             208 aa            linear   PRI 21-NOV-2025
DEFINITION  intraflagellar transport protein 43 homolog isoform 2 [Homo
            sapiens].
ACCESSION   NP_001096034
VERSION     NP_001096034.1
DBSOURCE    REFSEQ: accession NM_001102564.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 208)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 208)
  AUTHORS   Wang,M.X., Itoh,M., Li,S., Hida,Y., Ohta,K., Hayakawa,M.,
            Nishida,E., Ueda,M., Islam,S., Tana and Nakagawa,T.
  TITLE     CED-4 is an mRNA-binding protein that delivers ced-3 mRNA to
            ribosomes
  JOURNAL   Biochem Biophys Res Commun 470 (1), 48-53 (2016)
   PUBMED   26740177
  REMARK    GeneRIF: These results suggest that CED-4 forms a complex with
            ced-3 mRNA and delivers it to ribosomes for translation.
REFERENCE   7  (residues 1 to 208)
  AUTHORS   Cornejo-Garcia,J.A., Liou,L.B., Blanca-Lopez,N., Dona,I.,
            Chen,C.H., Chou,Y.C., Chuang,H.P., Wu,J.Y., Chen,Y.T., Plaza-Seron
            Mdel,C., Mayorga,C., Gueant-Rodriguez,R.M., Lin,S.C., Torres,M.J.,
            Campo,P., Rondon,C., Laguna,J.J., Fernandez,J., Gueant,J.L.,
            Canto,G., Blanca,M. and Lee,M.T.
  TITLE     Genome-wide association study in NSAID-induced acute
            urticaria/angioedema in Spanish and Han Chinese populations
  JOURNAL   Pharmacogenomics 14 (15), 1857-1869 (2013)
   PUBMED   24236485
REFERENCE   8  (residues 1 to 208)
  AUTHORS   Arts,H.H., Bongers,E.M., Mans,D.A., van Beersum,S.E., Oud,M.M.,
            Bolat,E., Spruijt,L., Cornelissen,E.A., Schuurs-Hoeijmakers,J.H.,
            de Leeuw,N., Cormier-Daire,V., Brunner,H.G., Knoers,N.V. and
            Roepman,R.
  TITLE     C14ORF179 encoding IFT43 is mutated in Sensenbrenner syndrome
  JOURNAL   J Med Genet 48 (6), 390-395 (2011)
   PUBMED   21378380
  REMARK    GeneRIF: C14ORF179 encoding IFT43 is mutated in Sensenbrenner
            syndrome.
REFERENCE   9  (residues 1 to 208)
  AUTHORS   Mukhopadhyay,S., Wen,X., Chih,B., Nelson,C.D., Lane,W.S.,
            Scales,S.J. and Jackson,P.K.
  TITLE     TULP3 bridges the IFT-A complex and membrane phosphoinositides to
            promote trafficking of G protein-coupled receptors into primary
            cilia
  JOURNAL   Genes Dev 24 (19), 2180-2193 (2010)
   PUBMED   20889716
REFERENCE   10 (residues 1 to 208)
  AUTHORS   Tan,W., Lin,A. and Keppler-Noreuil,K.
  TITLE     Cranioectodermal Dysplasia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24027799
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF107885.2 and AC008015.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a subunit of the intraflagellar
            transport complex A (IFT-A). IFT-A is a multiprotein complex that
            plays an important role in cilia assembly and maintenance by
            mediating retrograde ciliary transport. Mutations in this gene are
            a cause of cranioectodermal dysplasia-3 (CED3), also known as
            Sensenbrenner syndrome. Alternatively spliced transcript variants
            encoding multiple isoforms have been observed for this gene.
            [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (2) lacks an exon and contains two
            alternate exons in the coding region, but maintains the reading
            frame, compared to variant 1. The encoded isoform (2) is shorter
            than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DR423699.1, CB851159.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000314067.11/ ENSP00000324177.6
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..208
                     /product="intraflagellar transport protein 43 homolog
                     isoform 2"
                     /note="IFT complex A subunit; intraflagellar transport
                     protein 43 homolog; intraflagellar transport 43 homolog"
                     /calculated_mol_wt=23398
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q96FT9.3)"
     Region          18..65
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FT9.3)"
     Region          64..193
                     /region_name="IFT43"
                     /note="Intraflagellar transport protein 43; pfam15305"
                     /db_xref="CDD:464631"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96FT9.3)"
     CDS             1..208
                     /gene="IFT43"
                     /gene_synonym="C14orf179; CED3; RP81; SRTD18"
                     /coded_by="NM_001102564.3:25..651"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS41973.1"
                     /db_xref="GeneID:112752"
                     /db_xref="HGNC:HGNC:29669"
                     /db_xref="MIM:614068"
ORIGIN      
        1 medlldldee lryslatsra kmgrraqqes aqaenhlngk nssltltget ssaklprcrq
       61 ggwagdsvka skfrrkasee iedfrlrpqs lngsdyggdi piipdleevq eedfvlqvaa
      121 ppsiqikrvm tyrdldndlm kysaiqtldg eidlklltkv lapehevred dvgwdwdhlf
      181 tevssevlte wdplqteked pagqarht
//
LOCUS       NP_006256                631 aa            linear   PRI 21-NOV-2025
DEFINITION  double-strand-break repair protein rad21 homolog [Homo sapiens].
ACCESSION   NP_006256
VERSION     NP_006256.1
DBSOURCE    REFSEQ: accession NM_006265.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Su,X.A., Stopsack,K.H., Schmidt,D.R., Ma,D., Li,Z., Scheet,P.A.,
            Penney,K.L., Lotan,T.L., Abida,W., DeArment,E.G., Lu,K., Janas,T.,
            Hu,S., Vander Heiden,M.G., Loda,M., Boselli,M., Amon,A. and
            Mucci,L.A.
  TITLE     RAD21 promotes oncogenesis and lethal progression of prostate
            cancer
  JOURNAL   Proc Natl Acad Sci U S A 121 (36), e2405543121 (2024)
   PUBMED   39190349
  REMARK    GeneRIF: RAD21 promotes oncogenesis and lethal progression of
            prostate cancer.
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Xu,X., Wang,D., Xu,W., Li,H., Chen,N., Li,N., Yao,Q., Chen,W.,
            Zhong,J. and Mao,W.
  TITLE     NIPBL-mediated RAD21 facilitates tumorigenicity by the PI3K pathway
            in non-small-cell lung cancer
  JOURNAL   Commun Biol 7 (1), 206 (2024)
   PUBMED   38378967
  REMARK    GeneRIF: NIPBL-mediated RAD21 facilitates tumorigenicity by the
            PI3K pathway in non-small-cell lung cancer.
            Erratum:[Commun Biol. 2024 Apr 1;7(1):397. doi:
            10.1038/s42003-024-06085-w. PMID: 38561443]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Sadano,H., Sugimoto,H., Sakai,F., Nomura,N. and Osumi,T.
  TITLE     NXP-1, a human protein related to Rad21/Scc1/Mcd1, is a component
            of the nuclear matrix
  JOURNAL   Biochem Biophys Res Commun 267 (1), 418-422 (2000)
   PUBMED   10623634
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Parisi,S., McKay,M.J., Molnar,M., Thompson,M.A., van der Spek,P.J.,
            van Drunen-Schoenmaker,E., Kanaar,R., Lehmann,E., Hoeijmakers,J.H.
            and Kohli,J.
  TITLE     Rec8p, a meiotic recombination and sister chromatid cohesion
            phosphoprotein of the Rad21p family conserved from fission yeast to
            humans
  JOURNAL   Mol Cell Biol 19 (5), 3515-3528 (1999)
   PUBMED   10207075
REFERENCE   6  (residues 1 to 631)
  AUTHORS   McKay,M.J., Troelstra,C., van der Spek,P., Kanaar,R., Smit,B.,
            Hagemeijer,A., Bootsma,D. and Hoeijmakers,J.H.
  TITLE     Sequence conservation of the rad21 Schizosaccharomyces pombe DNA
            double-strand break repair gene in human and mouse
  JOURNAL   Genomics 36 (2), 305-315 (1996)
   PUBMED   8812457
REFERENCE   7  (residues 1 to 631)
  AUTHORS   Tuysuz,B., Gunes,N. and Alkaya,D.U.
  TITLE     Trichorhinophalangeal Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   28426188
REFERENCE   8  (residues 1 to 631)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
REFERENCE   9  (residues 1 to 631)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   10 (residues 1 to 631)
  AUTHORS   Deardorff,M.A., Noon,S.E. and Krantz,I.D.
  TITLE     Cornelia de Lange Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301283
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA328186.1 and BC050381.1.
            
            Summary: The protein encoded by this gene is highly similar to the
            gene product of Schizosaccharomyces pombe rad21, a gene involved in
            the repair of DNA double-strand breaks, as well as in chromatid
            cohesion during mitosis. This protein is a nuclear phospho-protein,
            which becomes hyperphosphorylated in cell cycle M phase. The highly
            regulated association of this protein with mitotic chromatin
            specifically at the centromere region suggests its role in sister
            chromatid cohesion in mitotic cells. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC050381.1, D38551.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000297338.7/ ENSP00000297338.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.11"
     Protein         1..631
                     /product="double-strand-break repair protein rad21
                     homolog"
                     /note="protein involved in DNA double-strand break repair;
                     nuclear matrix protein 1; NXP-1; SCC1 homolog; sister
                     chromatid cohesion 1; RAD21 homolog; kleisin"
                     /calculated_mol_wt=71559
     Region          1..104
                     /region_name="Rad21_Rec8_N"
                     /note="N terminus of Rad21 / Rec8 like protein; pfam04825"
                     /db_xref="CDD:461446"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O60216.2)"
     Region          126..282
                     /region_name="Required for interaction with SMARCA5.
                     /evidence=ECO:0000269|PubMed:12198550"
                     /note="propagated from UniProtKB/Swiss-Prot (O60216.2)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O60216.2)"
     Region          154..171
                     /region_name="Interaction with NIPBL.
                     /evidence=ECO:0000269|PubMed:32409525"
                     /note="propagated from UniProtKB/Swiss-Prot (O60216.2)"
     Site            172..173
                     /site_type="cleavage"
                     /note="Cleavage, by ESPL1.
                     /evidence=ECO:0000269|PubMed:11509732; propagated from
                     UniProtKB/Swiss-Prot (O60216.2)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O60216.2)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60216.2)"
     Region          258..285
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60216.2)"
     Site            279..280
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3 or caspase-7.
                     /evidence=ECO:0000269|PubMed:12417729; propagated from
                     UniProtKB/Swiss-Prot (O60216.2)"
     Region          287..403
                     /region_name="Interaction with WAPL and PDS5B.
                     /evidence=ECO:0000269|PubMed:19696148"
                     /note="propagated from UniProtKB/Swiss-Prot (O60216.2)"
     Region          316..395
                     /region_name="Rad21_Rec8_M_NXP1-like"
                     /note="Middle HEAT-repeat binding domain found in Homo
                     sapiens nuclear matrix protein 1 (NXP-1) and similar
                     proteins; cd21792"
                     /db_xref="CDD:439294"
     Site            order(322..324,327..334,337,340..341,343..344,346..353,
                     355..361,363..365,368..369,372..382,384..385,388..389,
                     391..395)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:439294"
     Region          362..403
                     /region_name="Interaction with STAG1.
                     /evidence=ECO:0000269|PubMed:19696148"
                     /note="propagated from UniProtKB/Swiss-Prot (O60216.2)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60216.2)"
     Region          423..489
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60216.2)"
     Site            450..451
                     /site_type="cleavage"
                     /note="Cleavage, by ESPL1.
                     /evidence=ECO:0000269|PubMed:11509732; propagated from
                     UniProtKB/Swiss-Prot (O60216.2)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60216.2)"
     Region          517..558
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60216.2)"
     Site            545
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60216.2)"
     Region          574..628
                     /region_name="Rad21_Rec8"
                     /note="Conserved region of Rad21 / Rec8 like protein;
                     pfam04824"
                     /db_xref="CDD:335912"
     Site            623
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60216.2)"
     CDS             1..631
                     /gene="RAD21"
                     /gene_synonym="CDLS4; hHR21; HR21; HRAD21; MCD1; MGS;
                     NXP1; SCC1"
                     /coded_by="NM_006265.3:199..2094"
                     /db_xref="CCDS:CCDS6321.1"
                     /db_xref="GeneID:5885"
                     /db_xref="HGNC:HGNC:9811"
                     /db_xref="MIM:606462"
ORIGIN      
        1 mfyahfvlsk rgplakiwla ahwdkkltka hvfecnless vesiispkvk malrtsghll
       61 lgvvriyhrk akylladcne afikikmafr pgvvdlpeen reaaynaitl peefhdfdqp
      121 lpdlddidva qqfslnqsrv eeitmreevg nisilqendf gdfgmddrei mregsafedd
      181 dmlvstttsn llleseqsts nlnekinhle yedqykddnf gegndggild dklisnndgg
      241 ifddppalse agvmlpeqpa hddmdeddnv smggpdspds vdpvepmptm tdqttlvpne
      301 eeafalepid itvketkakr krklivdsvk eldsktiraq lsdysdivtt ldlapptkkl
      361 mmwketggve klfslpaqpl wnnrllklft rcltplvped lrkrrkggea dnldeflkef
      421 enpevpredq qqqhqqrdvi depiieepsr lqesvmeasr tnidesampp pppqgvkrka
      481 gqidpepvmp pqqveqmeip pvelppeepp nicqlipele llpekekeke kekeddeeee
      541 dedasggdqd qeerrwnkrt qqmlhglqra laktgaesis llelcrntnr kqaaakfysf
      601 lvlkkqqaie ltqeepysdi iatpgprfhi i
//
LOCUS       NP_001372621             116 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 135 [Homo sapiens].
ACCESSION   NP_001372621
VERSION     NP_001372621.1
DBSOURCE    REFSEQ: accession NM_001385692.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 116)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 116)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 116)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 116)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 116)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 116)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 116)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 116)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 116)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 116)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.46270.1,
                                           SRR1660805.226399.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..116
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..116
                     /product="microtubule-associated protein 4 isoform 135"
                     /note="MAP-4"
                     /calculated_mol_wt=12143
     CDS             1..116
                     /gene="MAP4"
                     /coded_by="NM_001385692.1:103..453"
                     /note="isoform 135 is encoded by transcript variant 143"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedlplpp hpaslsfhlp ldtpsskptl langghgveg sdttea
//
LOCUS       NP_001165883             524 aa            linear   PRI 21-NOV-2025
DEFINITION  vang-like protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001165883
VERSION     NP_001165883.1
DBSOURCE    REFSEQ: accession NM_001172412.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Feng,X., Ye,Y., Zhang,J., Zhang,Y., Zhao,S., Mak,J.C.W., Otomo,N.,
            Zhao,Z., Niu,Y., Yonezawa,Y., Li,G., Lin,M., Li,X., Cheung,P.W.H.,
            Xu,K., Takeda,K., Wang,S., Xie,J., Kotani,T., Choi,V.N.T.,
            Song,Y.Q., Yang,Y., Luk,K.D.K., Lee,K.S., Li,Z., Li,P.S.,
            Leung,C.Y.H., Lin,X., Wang,X., Qiu,G., Watanabe,K., Wu,Z.,
            Posey,J.E., Ikegawa,S., Lupski,J.R., Cheung,J.P.Y., Zhang,T.J.,
            Gao,B. and Wu,N.
  CONSRTM   DISCO (Deciphering disorders Involving Scoliosis and COmorbidities)
            study group; Japanese Early Onset Scoliosis Research Group
  TITLE     Core planar cell polarity genes VANGL1 and VANGL2 in predisposition
            to congenital vertebral malformations
  JOURNAL   Proc Natl Acad Sci U S A 121 (18), e2310283121 (2024)
   PUBMED   38669183
  REMARK    GeneRIF: Core planar cell polarity genes VANGL1 and VANGL2 in
            predisposition to congenital vertebral malformations.
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Fatima,U., Khan,S., Riaz,S.U., Mehdi,H., Iftikhar,M. and Fatima,N.
  TITLE     Myelomeningocele among Pakistani population
  JOURNAL   J Pak Med Assoc 72 (5), 874-877 (2022)
   PUBMED   35713047
  REMARK    GeneRIF: Myelomeningocele among Pakistani population.
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Jiang,S.H., Mercan,S., Papa,I., Moldovan,M., Walters,G.D.,
            Koina,M., Fadia,M., Stanley,M., Lea-Henry,T., Cook,A., Ellyard,J.,
            McMorran,B., Sundaram,M., Thomson,R., Canete,P.F., Hoy,W.,
            Hutton,H., Srivastava,M., McKeon,K., de la Rua Figueroa,I.,
            Cervera,R., Faria,R., D'Alfonso,S., Gatto,M., Athanasopoulos,V.,
            Field,M., Mathews,J., Cho,E., Andrews,T.D., Kitching,A.R.,
            Cook,M.C., Riquelme,M.A., Bahlo,M. and Vinuesa,C.G.
  TITLE     Deletions in VANGL1 are a risk factor for antibody-mediated kidney
            disease
  JOURNAL   Cell Rep Med 2 (12), 100475 (2021)
   PUBMED   35028616
  REMARK    GeneRIF: Deletions in VANGL1 are a risk factor for
            antibody-mediated kidney disease.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 524)
  AUTHORS   Zhou,H., Wu,J., Leng,S., Hou,C., Mo,L., Xie,X., Wang,L. and Xu,Y.
  TITLE     Knockdown of circular RNA VANGL1 inhibits TGF-beta-induced
            epithelial-mesenchymal transition in melanoma cells by sponging
            miR-150-5p
  JOURNAL   J Cell Mol Med 25 (23), 10837-10845 (2021)
   PUBMED   34750955
  REMARK    GeneRIF: Knockdown of circular RNA VANGL1 inhibits TGF-beta-induced
            epithelial-mesenchymal transition in melanoma cells by sponging
            miR-150-5p.
REFERENCE   6  (residues 1 to 524)
  AUTHORS   Kalabis,J., Rosenberg,I. and Podolsky,D.K.
  TITLE     Vangl1 protein acts as a downstream effector of intestinal trefoil
            factor (ITF)/TFF3 signaling and regulates wound healing of
            intestinal epithelium
  JOURNAL   J Biol Chem 281 (10), 6434-6441 (2006)
   PUBMED   16410243
  REMARK    GeneRIF: VANGL protein may serve as an effector mediating the
            intestinal trefoil factor (ITF) healing response of the intestinal
            mucosa.
REFERENCE   7  (residues 1 to 524)
  AUTHORS   Doudney,K., Ybot-Gonzalez,P., Paternotte,C., Stevenson,R.E.,
            Greene,N.D., Moore,G.E., Copp,A.J. and Stanier,P.
  TITLE     Analysis of the planar cell polarity gene Vangl2 and its
            co-expressed paralogue Vangl1 in neural tube defect patients
  JOURNAL   Am J Med Genet A 136 (1), 90-92 (2005)
   PUBMED   15952208
  REMARK    Erratum:[Am J Med Genet A. 2005 Nov 1;138(4):415]
REFERENCE   8  (residues 1 to 524)
  AUTHORS   Lee,J.H., Park,S.R., Chay,K.O., Seo,Y.W., Kook,H., Ahn,K.Y.,
            Kim,Y.J. and Kim,K.K.
  TITLE     KAI1 COOH-terminal interacting tetraspanin (KITENIN), a member of
            the tetraspanin family, interacts with KAI1, a tumor metastasis
            suppressor, and enhances metastasis of cancer
  JOURNAL   Cancer Res 64 (12), 4235-4243 (2004)
   PUBMED   15205336
REFERENCE   9  (residues 1 to 524)
  AUTHORS   Yagyu,R., Hamamoto,R., Furukawa,Y., Okabe,H., Yamamura,T. and
            Nakamura,Y.
  TITLE     Isolation and characterization of a novel human gene, VANGL1, as a
            therapeutic target for hepatocellular carcinoma
  JOURNAL   Int J Oncol 20 (6), 1173-1178 (2002)
   PUBMED   12011995
REFERENCE   10 (residues 1 to 524)
  AUTHORS   Katoh,M.
  TITLE     Molecular cloning and characterization of Strabismus 2 (STB2)
  JOURNAL   Int J Oncol 20 (5), 993-998 (2002)
   PUBMED   11956595
  REMARK    GeneRIF: Molecular cloning and characterization of Strabismus 2
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB057596.1 and AL450389.12.
            
            Summary: This gene encodes a member of the tretraspanin family. The
            encoded protein may be involved in mediating intestinal trefoil
            factor induced wound healing in the intestinal mucosa. Mutations in
            this gene are associated with neural tube defects. Alternate
            splicing results in multiple transcript variants. [provided by
            RefSeq, Feb 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB057596.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.1"
     Protein         1..524
                     /product="vang-like protein 1 isoform 1"
                     /note="strabismus 2; KAI1 C-terminal interacting
                     tetraspanin; vang-like protein 1; van Gogh-like protein 1;
                     loop-tail protein 2 homolog; vang-like 1 (van gogh,
                     Drosophila)"
                     /calculated_mol_wt=59844
     Region          1..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAA9.1)"
     Region          25..524
                     /region_name="Strabismus"
                     /note="Strabismus protein; pfam06638"
                     /db_xref="CDD:461971"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80Z96; propagated from
                     UniProtKB/Swiss-Prot (Q8TAA9.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80Z96; propagated from
                     UniProtKB/Swiss-Prot (Q8TAA9.1)"
     Site            118..138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAA9.1)"
     Site            152..172
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAA9.1)"
     Site            183..203
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAA9.1)"
     Site            223..243
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAA9.1)"
     CDS             1..524
                     /gene="VANGL1"
                     /gene_synonym="KITENIN; LPP2; STB2; STBM2"
                     /coded_by="NM_001172412.2:216..1790"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS883.1"
                     /db_xref="GeneID:81839"
                     /db_xref="HGNC:HGNC:15512"
                     /db_xref="MIM:610132"
ORIGIN      
        1 mdtestysgy syysshskks hrqgertrer hksprnkdgr gseksvtiqp ptgepllgnd
       61 strteevqdd nwgetttait gtsehsisqe diariskdme dsvgldckry lgltvasflg
      121 llvfltpiaf illppilwrd elepcgtice glfismafkl lilligtwal ffrkrradmp
      181 rvfvfralll vliflfvvsy wlfygvrild srdrnyqgiv qyavslvdal lfihylaivl
      241 lelrqlqpmf tlqvvrstdg esrfyslghl siqraalvvl enyykdftiy npnlltaskf
      301 raakhmaglk vynvdgpsnn atgqsramia aaarrrdssh nelyyeeaeh errvkkrkar
      361 lvvaveeafi hiqrlqaeeq qkapgevmdp reaaqaifps maralqkylr itrqqnyhsm
      421 esilqhlafc itngmtpkaf lerylsagpt lqydkdrwls tqwrlvsdea vtnglrdgiv
      481 fvlkcldfsl vvnvkkipfi ilseefidpk shkfvlrlqs etsv
//
LOCUS       NP_001381517             108 aa            linear   PRI 21-NOV-2025
DEFINITION  ragulator complex protein LAMTOR4 isoform 5 [Homo sapiens].
ACCESSION   NP_001381517
VERSION     NP_001381517.1
DBSOURCE    REFSEQ: accession NM_001394588.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Gamallat,Y., Alwazan,H., Turko,R., Dang,V., Seyedi,S., Ghosh,S. and
            Bismar,T.A.
  TITLE     Elevated LAMTOR4 Expression Is Associated with Lethal Prostate
            Cancer and Its Knockdown Decreases Cell Proliferation, Invasion,
            and Migration In Vitro
  JOURNAL   Int J Mol Sci 25 (15), 8100 (2024)
   PUBMED   39125671
  REMARK    GeneRIF: Elevated LAMTOR4 Expression Is Associated with Lethal
            Prostate Cancer and Its Knockdown Decreases Cell Proliferation,
            Invasion, and Migration In Vitro.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Zhang,S., Lee,S.H., Nie,L., Huang,Y., Zou,G., Jung,Y.S., Jun,S.,
            Zhang,J., Lien,E.M., Chen,J. and Park,J.I.
  TITLE     Lysosomal TMEM9-LAMTOR4-controlled mTOR signaling integrity is
            required for mammary tumorigenesis
  JOURNAL   Cancer Commun (Lond) 43 (1), 159-163 (2023)
   PUBMED   36336962
  REMARK    GeneRIF: Lysosomal TMEM9-LAMTOR4-controlled mTOR signaling
            integrity is required for mammary tumorigenesis.
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Rebsamen,M., Pochini,L., Stasyk,T., de Araujo,M.E., Galluccio,M.,
            Kandasamy,R.K., Snijder,B., Fauster,A., Rudashevskaya,E.L.,
            Bruckner,M., Scorzoni,S., Filipek,P.A., Huber,K.V., Bigenzahn,J.W.,
            Heinz,L.X., Kraft,C., Bennett,K.L., Indiveri,C., Huber,L.A. and
            Superti-Furga,G.
  TITLE     SLC38A9 is a component of the lysosomal amino acid sensing
            machinery that controls mTORC1
  JOURNAL   Nature 519 (7544), 477-481 (2015)
   PUBMED   25561175
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Blandin,G., Marchand,S., Charton,K., Daniele,N., Gicquel,E.,
            Boucheteil,J.B., Bentaib,A., Barrault,L., Stockholm,D., Bartoli,M.
            and Richard,I.
  TITLE     A human skeletal muscle interactome centered on proteins involved
            in muscular dystrophies: LGMD interactome
  JOURNAL   Skelet Muscle 3 (1), 3 (2013)
   PUBMED   23414517
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 108)
  AUTHORS   Bar-Peled,L., Schweitzer,L.D., Zoncu,R. and Sabatini,D.M.
  TITLE     Ragulator is a GEF for the rag GTPases that signal amino acid
            levels to mTORC1
  JOURNAL   Cell 150 (6), 1196-1208 (2012)
   PUBMED   22980980
  REMARK    GeneRIF: Study identified HBXIP and C7orf59 as two additional
            Ragulator components that are required for mTORC1 activation by
            amino acids.
REFERENCE   9  (residues 1 to 108)
  AUTHORS   Sancak,Y., Bar-Peled,L., Zoncu,R., Markhard,A.L., Nada,S. and
            Sabatini,D.M.
  TITLE     Ragulator-Rag complex targets mTORC1 to the lysosomal surface and
            is necessary for its activation by amino acids
  JOURNAL   Cell 141 (2), 290-303 (2010)
   PUBMED   20381137
REFERENCE   10 (residues 1 to 108)
  AUTHORS   Toulza,E., Mattiuzzo,N.R., Galliano,M.F., Jonca,N., Dossat,C.,
            Jacob,D., de Daruvar,A., Wincker,P., Serre,G. and Guerrin,M.
  TITLE     Large-scale identification of human genes implicated in epidermal
            barrier function
  JOURNAL   Genome Biol 8 (6), R107 (2007)
   PUBMED   17562024
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073842.5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB498044.1, SRR18074968.628848.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..108
                     /product="ragulator complex protein LAMTOR4 isoform 5"
                     /note="UPF0539 protein C7orf59; late endosomal/lysosomal
                     adaptor and MAPK and MTOR activator 4; ragulator complex
                     protein LAMTOR4"
                     /calculated_mol_wt=11205
     CDS             1..108
                     /gene="LAMTOR4"
                     /gene_synonym="C7orf59"
                     /coded_by="NM_001394588.1:56..382"
                     /note="isoform 5 is encoded by transcript variant 8"
                     /db_xref="GeneID:389541"
                     /db_xref="HGNC:HGNC:33772"
                     /db_xref="MIM:618834"
ORIGIN      
        1 mvsedacarg paggsasllp slcgfpltsa ltqgleripd qlgylvlseg avlassgdle
       61 ndeqaasais elvstacgfr lhrgmnvpfk rlsgvsllqw slenthcw
//
LOCUS       NP_055408                656 aa            linear   PRI 21-NOV-2025
DEFINITION  CXXC-type zinc finger protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_055408
VERSION     NP_055408.2
DBSOURCE    REFSEQ: accession NM_014593.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Li,C., Zhang,Y., Shen,J., Bao,H., Zhao,Y., Li,D., Li,S., Liu,Y.,
            Yang,J., Zhou,Z., Gao,K., Zhao,L., Pei,Y., Lu,Y., Pan,Z. and Cai,B.
  TITLE     Cfp1 Controls Cardiomyocyte Maturation by Modifying Histone H3K4me3
            of Structural, Metabolic, and Contractile Related Genes
  JOURNAL   Adv Sci (Weinh) 11 (11), e2305992 (2024)
   PUBMED   38196272
  REMARK    GeneRIF: Cfp1 Controls Cardiomyocyte Maturation by Modifying
            Histone H3K4me3 of Structural, Metabolic, and Contractile Related
            Genes.
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Yang,S.C., Park,M., Hong,K.H., La,H., Park,C., Wang,P., Li,G.,
            Chen,Q., Choi,Y., DeMayo,F.J., Lydon,J.P., Skalnik,D.G., Lim,H.J.,
            Hong,S.H., Park,S.H., Kim,Y.S., Kim,H.R. and Song,H.
  TITLE     CFP1 governs uterine epigenetic landscapes to intervene in
            progesterone responses for uterine physiology and suppression of
            endometriosis
  JOURNAL   Nat Commun 14 (1), 3220 (2023)
   PUBMED   37270588
  REMARK    GeneRIF: CFP1 governs uterine epigenetic landscapes to intervene in
            progesterone responses for uterine physiology and suppression of
            endometriosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Yang,L.Q., Hu,H.Y., Han,Y., Tang,Z.Y., Gao,J., Zhou,Q.Y., Liu,Y.X.,
            Chen,H.S., Xu,T.N., Ao,L., Xu,Y., Che,X., Jiang,Y.B., Xu,C.W.,
            Zhang,X.C., Jiang,Y.X., Heger,M., Wang,X.M., Cheng,S.Q. and
            Pan,W.W.
  TITLE     CpG-binding protein CFP1 promotes ovarian cancer cell proliferation
            by regulating BST2 transcription
  JOURNAL   Cancer Gene Ther 29 (12), 1895-1907 (2022)
   PUBMED   35864225
  REMARK    GeneRIF: CpG-binding protein CFP1 promotes ovarian cancer cell
            proliferation by regulating BST2 transcription.
REFERENCE   5  (residues 1 to 656)
  AUTHORS   Yang,Y., Yang,Y., Chan,K. and Couture,J.F.
  TITLE     Analyzing the impact of CFP1 mutational landscape on epigenetic
            signaling
  JOURNAL   FASEB J 35 (8), e21790 (2021)
   PUBMED   34320252
  REMARK    GeneRIF: Analyzing the impact of CFP1 mutational landscape on
            epigenetic signaling.
            Review article
REFERENCE   6  (residues 1 to 656)
  AUTHORS   Lee,J.H., Voo,K.S. and Skalnik,D.G.
  TITLE     Identification and characterization of the DNA binding domain of
            CpG-binding protein
  JOURNAL   J Biol Chem 276 (48), 44669-44676 (2001)
   PUBMED   11572867
REFERENCE   7  (residues 1 to 656)
  AUTHORS   Carlone,D.L. and Skalnik,D.G.
  TITLE     CpG binding protein is crucial for early embryonic development
  JOURNAL   Mol Cell Biol 21 (22), 7601-7606 (2001)
   PUBMED   11604496
REFERENCE   8  (residues 1 to 656)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 656)
  AUTHORS   Fujino,T., Hasegawa,M., Shibata,S., Kishimoto,T., Imai,S. and
            Takano,T.
  TITLE     PCCX1, a novel DNA-binding protein with PHD finger and CXXC domain,
            is regulated by proteolysis
  JOURNAL   Biochem Biophys Res Commun 271 (2), 305-310 (2000)
   PUBMED   10799292
REFERENCE   10 (residues 1 to 656)
  AUTHORS   Voo,K.S., Carlone,D.L., Jacobsen,B.M., Flodin,A. and Skalnik,D.G.
  TITLE     Cloning of a mammalian transcriptional activator that binds
            unmethylated CpG motifs and shares a CXXC domain with DNA
            methyltransferase, human trithorax, and methyl-CpG binding domain
            protein 1
  JOURNAL   Mol Cell Biol 20 (6), 2108-2121 (2000)
   PUBMED   10688657
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB031069.1.
            
            On Aug 21, 2007 this sequence version replaced NP_055408.1.
            
            Summary: This gene encodes a protein that functions as a
            transcriptional activator that binds specifically to non-methylated
            CpG motifs through its CXXC domain. The protein is a component of
            the SETD1 complex, regulates gene expression and is essential for
            vertebrate development. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the mid-coding region, compared to variant 1,
            resulting in a shorter protein (isoform 2), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB031069.1, AL136862.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000285106.11/ ENSP00000285106.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..656
                     /product="CXXC-type zinc finger protein 1 isoform 2"
                     /note="DNA-binding protein with PHD finger and CXXC
                     domain; CXXC finger 1 (PHD domain); zinc finger, CpG
                     binding-type containing 1; CpG binding protein;
                     cpG-binding protein; CXXC-type zinc finger protein 1; PHD
                     finger and CXXC domain-containing protein 1"
                     /calculated_mol_wt=75581
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Region          28..73
                     /region_name="PHD_Cfp1"
                     /note="PHD finger found in CXXC-type zinc finger protein 1
                     (Cfp1); cd15553"
                     /db_xref="CDD:277028"
     Site            order(28,39..43,47,68)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277028"
     Region          84..162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Region          162..208
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          219..287
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Region          311..373
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0U4.2)"
     Region          400..636
                     /region_name="CpG_bind_C"
                     /note="CpG binding protein C-terminal domain; pfam12269"
                     /db_xref="CDD:463514"
     CDS             1..656
                     /gene="CXXC1"
                     /gene_synonym="2410002I16Rik; 5830420C16Rik; CFP1; CGBP;
                     hCGBP; HsT2645; PCCX1; PHF18; SPP1; ZCGPC1"
                     /coded_by="NM_014593.4:104..2074"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS11945.1"
                     /db_xref="GeneID:30827"
                     /db_xref="HGNC:HGNC:24343"
                     /db_xref="MIM:609150"
ORIGIN      
        1 megdgsdpep pdagedskse ngenapiyci crkpdincfm igcdncnewf hgdciritek
       61 makairewyc recrekdpkl eiryrhkksr erdgnerdss eprdegggrk rpvpdpdlqr
      121 ragsgtgvga mlargsasph ksspqplvat psqhhqqqqq qikrsarmcg eceacrrted
      181 cghcdfcrdm kkfggpnkir qkcrlrqcql raresykyfp sslspvtpse slprprrplp
      241 tqqqpqpsqk lgriredega vasstvkepp eatatpepls dedlpldpdl yqdfcagafd
      301 dhglpwmsdt eespfldpal rkravkvkhv krrekksekk keerykrhrq kqkhkdkwkh
      361 peradakdpa slpqclgpgc vrpaqpssky csddcgmkla anriyeilpq riqqwqqspc
      421 iaeehgkkll erirreqqsa rtrlqemerr fheleaiilr akqqavrede esnegdsddt
      481 dlqifcvscg hpinprvalr hmercyakye sqtsfgsmyp triegatrlf cdvynpqskt
      541 yckrlqvlcp ehsrdpkvpa devcgcplvr dvfeltgdfc rlpkrqcnrh ycweklrrae
      601 vdlervrvwy kldelfeqer nvrtamtnra gllalmlhqt iqhdplttdl rssadr
//
LOCUS       NP_001341688             662 aa            linear   PRI 21-NOV-2025
DEFINITION  alpha-adducin isoform e [Homo sapiens].
ACCESSION   NP_001341688 XP_016863197
VERSION     NP_001341688.1
DBSOURCE    REFSEQ: accession NM_001354759.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 662)
  AUTHORS   Sydorchuk,L., Lytvyn,B., Sydorchuk,A., Yarynych,Y., Daruvuri,S.P.,
            Semenenko,S., Hoshovska,A., Sydorchuk,R. and Biryuk,I.
  TITLE     Alpha-adducin 1 (rs4961) gene and its expression associated with
            sodium sensitivity in hypertensive patients: a cohort study in the
            western Ukrainian population
  JOURNAL   Endocr Regul 58 (1), 195-205 (2024)
   PUBMED   39352780
  REMARK    GeneRIF: Alpha-adducin 1 (rs4961) gene and its expression
            associated with sodium sensitivity in hypertensive patients: a
            cohort study in the western Ukrainian population.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 662)
  AUTHORS   Gonzalez-Fernandez,E., Fan,L., Wang,S., Liu,Y., Gao,W.,
            Thomas,K.N., Fan,F. and Roman,R.J.
  TITLE     The adducin saga: pleiotropic genomic targets for precision
            medicine in human hypertension-vascular, renal, and cognitive
            diseases
  JOURNAL   Physiol Genomics 54 (2), 58-70 (2022)
   PUBMED   34859687
  REMARK    GeneRIF: The adducin saga: pleiotropic genomic targets for
            precision medicine in human hypertension-vascular, renal, and
            cognitive diseases.
            Review article
REFERENCE   4  (residues 1 to 662)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 662)
  AUTHORS   Liang,X., Zhou,Y. and Li,S.
  TITLE     Association of TBXA2R, P2Y12 and ADD1 genes polymorphisms with
            ischemic stroke susceptibility: A metaanalysis
  JOURNAL   Clin Invest Med 43 (3), E33-E43 (2020)
   PUBMED   32971583
  REMARK    GeneRIF: Association of TBXA2R, P2Y12 and ADD1 genes polymorphisms
            with ischemic stroke susceptibility: A metaanalysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 662)
  AUTHORS   Goldberg,Y.P., Lin,B.Y., Andrew,S.E., Nasir,J., Graham,R.,
            Glaves,M.L., Hutchinson,G., Theilmann,J., Ginzinger,D.G.,
            Schappert,K. et al.
  TITLE     Cloning and mapping of the alpha-adducin gene close to D4S95 and
            assessment of its relationship to Huntington disease
  JOURNAL   Hum Mol Genet 1 (9), 669-675 (1992)
   PUBMED   1284592
REFERENCE   7  (residues 1 to 662)
  AUTHORS   Taylor,S.A., Snell,R.G., Buckler,A., Ambrose,C., Duyao,M.,
            Church,D., Lin,C.S., Altherr,M., Bates,G.P., Groot,N. et al.
  TITLE     Cloning of the alpha-adducin gene from the Huntington's disease
            candidate region of chromosome 4 by exon amplification
  JOURNAL   Nat Genet 2 (3), 223-227 (1992)
   PUBMED   1345173
REFERENCE   8  (residues 1 to 662)
  AUTHORS   Joshi,R., Gilligan,D.M., Otto,E., McLaughlin,T. and Bennett,V.
  TITLE     Primary structure and domain organization of human alpha and beta
            adducin
  JOURNAL   J Cell Biol 115 (3), 665-675 (1991)
   PUBMED   1840603
REFERENCE   9  (residues 1 to 662)
  AUTHORS   Mangeat,P.H.
  TITLE     Interaction of biological membranes with the cytoskeletal framework
            of living cells
  JOURNAL   Biol Cell 64 (3), 261-281 (1988)
   PUBMED   2976282
  REMARK    Review article
REFERENCE   10 (residues 1 to 662)
  AUTHORS   Gardner,K. and Bennett,V.
  TITLE     Modulation of spectrin-actin assembly by erythrocyte adducin
  JOURNAL   Nature 328 (6128), 359-362 (1987)
   PUBMED   3600811
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121750.22, BX465861.7 and
            AL390065.20.
            
            On Aug 29, 2017 this sequence version replaced XP_016863197.1.
            
            Summary: Adducins are a family of cytoskeletal proteins encoded by
            three genes (alpha, beta, and gamma). Adducin acts as a heterodimer
            of the related alpha, beta, or gamma subunits. The protein encoded
            by this gene represents the alpha subunit. Alpha- and beta-adducin
            include a protease-resistant N-terminal region and a
            protease-sensitive, hydrophilic C-terminal region. Adducin binds
            with high affinity to Ca(2+)/calmodulin and is a substrate for
            protein kinases A and C. [provided by RefSeq, Aug 2017].
            
            Transcript Variant: This variant (11), as well as variant 5,
            encodes isoform e.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.82849.1,
                                           SRR1803612.269337.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..662
                     /product="alpha-adducin isoform e"
                     /note="erythrocyte adducin alpha subunit; alpha-adducin;
                     adducin 1 (alpha); alpha-adducin 1"
                     /calculated_mol_wt=73251
     Region          145..391
                     /region_name="Aldolase_II"
                     /note="Class II Aldolase and Adducin head (N-terminal)
                     domain. Aldolases are ubiquitous enzymes catalyzing
                     central steps of carbohydrate metabolism. Based on
                     enzymatic mechanisms, this superfamily has been divided
                     into two distinct classes (Class I and II); cl00214"
                     /db_xref="CDD:469663"
     Site            order(151,155,163,188,190..191,241,243..244,249..251,259,
                     261..262,273,301,312,319,323,330,348)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238232"
     Site            order(168,185..186,211..213,239,241,302)
                     /site_type="active"
                     /db_xref="CDD:238232"
     Site            order(239,241,302)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238232"
     CDS             1..662
                     /gene="ADD1"
                     /gene_synonym="ADDA"
                     /coded_by="NM_001354759.2:202..2190"
                     /note="isoform e is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS75094.1"
                     /db_xref="GeneID:118"
                     /db_xref="HGNC:HGNC:243"
                     /db_xref="MIM:102680"
ORIGIN      
        1 mngdsraavv tspppttaph keryfdrvde nnpeylrern mapdlrqdfn mmeqkkrvsm
       61 ilqspafcee lesmiqeqfk kgknptglla lqqiadfmtt nvpnvypaap qggmaalnms
      121 lgmvtpvndl rgsdsiaydk gekllrckla afyrladlfg wsqliynhit trvnseqehf
      181 livpfgllys evtasslvki nlqgdivdrg stnlgvnqag ftlhsaiyaa rpdvkcvvhi
      241 htpagaavsa mkcgllpisp ealslgevay hdyhgilvde eekvliqknl gpkskvlilr
      301 nhglvsvges veeafyyihn lvvaceiqvr tlasaggpdn lvllnpekyk aksrspgspv
      361 gegtgsppkw qigeqefeal mrmldnlgyr tgypyrypal rekskkysdv evpasvtgys
      421 fasdgdsgtc splrhsfqkq qrektrwlns grgdeaseeg qngsspkskt kwtkedghrt
      481 stsavpnlfv plntnpkevq emrnkireqn lqdiktagpq sqvlcgvvmd rslvqdapls
      541 dctetiegle lteqtfspak slsfrkgelv taskaiieke yqphvivstt gpnpfttltd
      601 releeyrrev erkqkgseen ldeareqkek sppdqpavph pppstpikle egdgcareyl
      661 lp
//
LOCUS       NP_001243664             331 aa            linear   PRI 21-NOV-2025
DEFINITION  single-stranded DNA-binding protein 2 isoform 5 [Homo sapiens].
ACCESSION   NP_001243664
VERSION     NP_001243664.1
DBSOURCE    REFSEQ: accession NM_001256735.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Schwab,C., Roberts,K., Boer,J.M., Gohring,G., Steinemann,D.,
            Vora,A., Macartney,C., Hough,R., Thorn,Z., Dillon,R., Escherich,G.,
            Cazzaniga,G., Schlegelberger,B., Loh,M., den Boer,M.L.,
            Moorman,A.V. and Harrison,C.J.
  TITLE     SSBP2-CSF1R is a recurrent fusion in B-lineage acute lymphoblastic
            leukemia with diverse genetic presentation and variable outcome
  JOURNAL   Blood 137 (13), 1835-1838 (2021)
   PUBMED   33197935
  REMARK    GeneRIF: SSBP2-CSF1R is a recurrent fusion in B-lineage acute
            lymphoblastic leukemia with diverse genetic presentation and
            variable outcome.
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Wang,H., Kim,J., Wang,Z., Yan,X.X., Dean,A. and Xu,W.
  TITLE     Crystal structure of human LDB1 in complex with SSBP2
  JOURNAL   Proc Natl Acad Sci U S A 117 (2), 1042-1048 (2020)
   PUBMED   31892537
  REMARK    GeneRIF: Single-stranded DNA binding proteins (SSBPs) interact
            specifically with the LDB/Chip conserved domain (LCCD) of LDB
            proteins and stabilize LDBs by preventing their proteasomal
            degradation, thus promoting their functions in gene regulation.
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Kim,H., Kim,Y., Bang,S., Park,S., Jee,S., Sim,J., Shin,S.J.,
            Paik,S.S. and Jang,K.
  TITLE     Low Expression of Single-stranded DNA Binding Protein 2 (SSBP2)
            Predicts Unfavourable Postoperative Outcomes in Patients With Clear
            Cell Renal Cell Carcinoma
  JOURNAL   In Vivo 34 (1), 101-107 (2020)
   PUBMED   31882468
  REMARK    GeneRIF: CcRCC with low SSBP2 expression was associated with
            adverse clinicopathological characteristics and poor patient
            outcomes.
REFERENCE   6  (residues 1 to 331)
  AUTHORS   Fleisig,H.B., Orazio,N.I., Liang,H., Tyler,A.F., Adams,H.P.,
            Weitzman,M.D. and Nagarajan,L.
  TITLE     Adenoviral E1B55K oncoprotein sequesters candidate leukemia
            suppressor sequence-specific single-stranded DNA-binding protein 2
            into aggresomes
  JOURNAL   Oncogene 26 (33), 4797-4805 (2007)
   PUBMED   17311003
  REMARK    GeneRIF: Results suggest that subverting SSBP2 function by
            oncoprotein E1B55K may contribute to cell transformation by viral
            oncoproteins.
REFERENCE   7  (residues 1 to 331)
  AUTHORS   Liang,H., Samanta,S. and Nagarajan,L.
  TITLE     SSBP2, a candidate tumor suppressor gene, induces growth arrest and
            differentiation of myeloid leukemia cells
  JOURNAL   Oncogene 24 (16), 2625-2634 (2005)
   PUBMED   15782145
  REMARK    GeneRIF: Our findings are consistent with human SSBP2 being a novel
            regulator of hematopoietic growth and differentiation, whose loss
            confers a block in differentiation advantage to myeloid leukemic
            cells.
REFERENCE   8  (residues 1 to 331)
  AUTHORS   Castro,P., Liang,H., Liang,J.C. and Nagarajan,L.
  TITLE     A novel, evolutionarily conserved gene family with putative
            sequence-specific single-stranded DNA-binding activity
  JOURNAL   Genomics 80 (1), 78-85 (2002)
   PUBMED   12079286
  REMARK    GeneRIF: Member of a closely related, evolutionarily conserved, and
            ubiquitously expressed gene family, potential tumor suppressor
REFERENCE   9  (residues 1 to 331)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 331)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016562.7, AC093250.3,
            AC026419.5 and AC010623.10.
            
            Summary: This gene encodes a subunit of a protein complex that
            interacts with single-stranded DNA and is involved in the DNA
            damage response and maintenance of genome stability. The encoded
            protein may also play a role in telomere repair. A variant of this
            gene may be associated with survival in human glioblastoma
            patients. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR936787.1, SRR14038192.2891770.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.1"
     Protein         1..331
                     /product="single-stranded DNA-binding protein 2 isoform 5"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein 2"
                     /calculated_mol_wt=34869
     Region          19..45
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          <92..308
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     CDS             1..331
                     /gene="SSBP2"
                     /gene_synonym="HSPC116; SOSS-B2"
                     /coded_by="NM_001256735.3:56..1051"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS58961.1"
                     /db_xref="GeneID:23635"
                     /db_xref="HGNC:HGNC:15831"
                     /db_xref="MIM:607389"
ORIGIN      
        1 mygkgksnss avpsdsqare klalyvyeyl lhvgaqksaq tflseirwek nitlgeppgf
       61 lhswwcvfwd lycaaperre tcehsseaka fhdypfmspr ypggprpplr ipnqalggvp
      121 gsqpllpsgm dptrqqghpn mggpmqrmtp prgmvplgpq nyggamrppl nalggpgmpg
      181 mnmgpgggrp wpnptnansi pyssaspgny vgppggggpp gtpimpspad stnsgdnmyt
      241 lmnavppgpn rpnfpmgpgs dgpmgglggm eshhmngslg sgdmdsiskn spnnmslsnq
      301 pgtprddgem ggnflnpfqs esyspsmtms v
//
LOCUS       NP_001287674            1166 aa            linear   PRI 21-NOV-2025
DEFINITION  protein transport protein Sec31A isoform 7 [Homo sapiens].
ACCESSION   NP_001287674 XP_005262909
VERSION     NP_001287674.1
DBSOURCE    REFSEQ: accession NM_001300745.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1166)
  AUTHORS   Tobias,E.S., Lucas-Herald,A.K., Sagar,D., Montezano,A.C.,
            Rios,F.J., De Lucca Camargo,L., Hamilton,G., Gazdagh,G.,
            Diver,L.A., Williams,N., Herzyk,P., Touyz,R.M., Greenfield,A.,
            McGowan,R. and Ahmed,S.F.
  TITLE     SEC31A may be associated with pituitary hormone deficiency and
            gonadal dysgenesis
  JOURNAL   Endocrine 84 (2), 345-349 (2024)
   PUBMED   38400880
  REMARK    GeneRIF: SEC31A may be associated with pituitary hormone deficiency
            and gonadal dysgenesis.
REFERENCE   2  (residues 1 to 1166)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1166)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1166)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1166)
  AUTHORS   Jin,L., Pahuja,K.B., Wickliffe,K.E., Gorur,A., Baumgartel,C.,
            Schekman,R. and Rape,M.
  TITLE     Ubiquitin-dependent regulation of COPII coat size and function
  JOURNAL   Nature 482 (7386), 495-500 (2012)
   PUBMED   22358839
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1166)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1166)
  AUTHORS   Kim,J.H., Hong,J.A., Pih,K.T. and Hwang,I.
  TITLE     Identification and isolation of differentially expressed genes in
            osmotically stressed human oral keratinocytes
  JOURNAL   Arch Oral Biol 46 (4), 335-341 (2001)
   PUBMED   11269867
REFERENCE   8  (residues 1 to 1166)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 1166)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   10 (residues 1 to 1166)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021105.13 and AC108469.5.
            
            On Jul 11, 2014 this sequence version replaced XP_005262909.1.
            
            Summary: The protein encoded by this gene shares similarity with
            the yeast Sec31 protein, and is a component of the outer layer of
            the coat protein complex II (COPII). The encoded protein is
            involved in vesicle budding from the endoplasmic reticulum (ER) and
            contains multiple WD repeats near the N-terminus and a proline-rich
            region in the C-terminal half. It associates with the protein
            encoded by the SEC13 homolog, nuclear pore and COPII coat complex
            component (SEC13), and is required for ER-Golgi transport.
            Monoubiquitylation of this protein by CUL3-KLHL12 was found to
            regulate the size of COPII coats to accommodate unusually shaped
            cargo. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (8) lacks two consecutive
            alternate in-frame exons in the central coding region and uses an
            alternate in-frame splice site in the 3' coding region, compared to
            variant 5. The encoded isoform (7) has the same N- and C-termini,
            but is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143492.2, SRR14038196.327215.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1166
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..1166
                     /product="protein transport protein Sec31A isoform 7"
                     /note="yeast Sec31p homolog; protein transport protein
                     Sec31A; web1-like protein; SEC31 homolog A, COPII coat
                     complex component; SEC31-related protein A; SEC31-like
                     protein 1; SEC31 homolog A, COPII coating complex
                     component"
                     /calculated_mol_wt=127425
     Region          13..332
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(26,40,46..47,52..53,91,95,101..102,117,121,139,144,
                     150..151,164,185,190,196..197,209..210,231,235,244..245,
                     258..259,277,282,288..289,301..302,320,325,331..332)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          70..119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          125..162
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          172..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          263..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          306..331
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <534..>657
                     /region_name="ACE1-Sec16-like"
                     /note="Ancestral coatomer element 1 (ACE1) of COPII coat
                     complex assembly protein Sec16; cl14807"
                     /db_xref="CDD:449359"
     Site            order(535..539,541,543,554,556,557..558,560..561,565,571,
                     579,591,594,619..620)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187750"
     Region          <754..>1049
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     CDS             1..1166
                     /gene="SEC31A"
                     /gene_synonym="ABP125; ABP130; HPBKS; HSPC275; HSPC334;
                     NEDSOSB; SEC31L1"
                     /coded_by="NM_001300745.3:71..3571"
                     /note="isoform 7 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS75156.1"
                     /db_xref="GeneID:22872"
                     /db_xref="HGNC:HGNC:17052"
                     /db_xref="MIM:610257"
ORIGIN      
        1 mklkevdrta mqawspaqnh piylatgtsa qqldatfstn asleifeldl sdpsldmksc
       61 atfssshryh kliwgpykmd skgdvsgvli aggengniil ydpskiiagd kevviaqndk
      121 htgpvraldv nifqtnlvas ganeseiyiw dlnnfatpmt pgaktqpped isciawnrqv
      181 qhilasasps gratvwdlrk nepiikvsdh snrmhcsgla whpdvatqmv laseddrlpv
      241 iqmwdlrfas splrvlenha rgilaiawsm adpelllscg kdakilcsnp ntgevlyelp
      301 tntqwcfdiq wcprnpavls aasfdgrisv ysimggstdg lrqkqvdkls ssfgnldpfg
      361 tgqplpplqi pqqtaqhsiv lplkkppkwi rrpvgasfsf ggklvtfenv rmpshqgaeq
      421 qqqqhhvfis qvvtekefls rsdqlqqavq sqgfinycqk kidasqtefe knvwsflkvn
      481 feddsrgkyl ellgyrkedl gkkhikeeke eseflpssgg tfnisvsgdi dglitqallt
      541 gnfesavdlc lhdnrmadai ilaiaggqel lartqkkyfa ksqskitrli tavvmknwke
      601 ivescdlknw realaavlty akpdefsalc dllgtrlene gdsllqtqac lcyicagnve
      661 klvacwtkaq dgshplslqd liekvvilrk avqltqamdt stvgvllaak msqyanllaa
      721 qgsiaaalaf lpdntnqpni mqlrdrlcra qgepvaghes pkipyekqql pkgrpgpvag
      781 hhqmprvqtq qyyphgenpp ppgfimhgnv npnaagqlpt spghmhtqvp pypqpqpyqp
      841 aqpypfgtgg samyrpqqpv apptsnaypn tpyissassy tgqsqlyaaq hqassptssp
      901 atsfppppss gasfqhggpg appsssayal ppgttgpqng wndppalnrv pkkkkmpenf
      961 mppvpitspi mnplgdpqsq mlqqqpsapv plssqssfpq phlpggqpfh gvqqplgqtg
     1021 mppsfskpni egapgapign tfqhvqslpt kkitkkpipd ehlilkttfe dliqrclssa
     1081 tdpqtkrkld daskrlefly dklreqtlsp titsglhnia rsietrnyse gltmhthivs
     1141 tsnfsetsaf mpvlkvvltq anklgv
//
LOCUS       NP_036290                428 aa            linear   PRI 21-NOV-2025
DEFINITION  F-box/LRR-repeat protein 3 [Homo sapiens].
ACCESSION   NP_036290
VERSION     NP_036290.1
DBSOURCE    REFSEQ: accession NM_012158.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Luo,J., Tao,H., Wen,Z., Chen,L., Hu,H. and Guan,H.
  TITLE     [Tumor-associated fibroblasts promotes proliferation and migration
            of prostate cancer cells by suppressing FBXL3 via upregulating
            hsa-miR-18b-5p]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 44 (7), 1284-1296 (2024)
   PUBMED   39051074
  REMARK    GeneRIF: [Tumor-associated fibroblasts promotes proliferation and
            migration of prostate cancer cells by suppressing FBXL3 via
            upregulating hsa-miR-18b-5p].
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Ansar,M., Paracha,S.A., Serretti,A., Sarwar,M.T., Khan,J.,
            Ranza,E., Falconnet,E., Iwaszkiewicz,J., Shah,S.F., Qaisar,A.A.,
            Santoni,F.A., Zoete,V., Megarbane,A., Ahmed,J., Colombo,R.,
            Makrythanasis,P. and Antonarakis,S.E.
  TITLE     Biallelic variants in FBXL3 cause intellectual disability, delayed
            motor development and short stature
  JOURNAL   Hum Mol Genet 28 (6), 972-979 (2019)
   PUBMED   30481285
  REMARK    GeneRIF: we conclude that homozygous FBXL3 LoF variants likely
            cause autosomal recessive ID, short stature, developmental delay
            and facial dysmorphism in humans, and that the Cys358Arg FBXL3
            variant likely adds the circadian phenotype because of abnormal
            interaction with CRY1 and CRY2
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Wang,D., Han,X., Li,C. and Bai,W.
  TITLE     FBXL3 is regulated by miRNA-4735-3p and suppresses cell
            proliferation and migration in non-small cell lung cancer
  JOURNAL   Pathol Res Pract 215 (2), 358-365 (2019)
   PUBMED   30594330
  REMARK    GeneRIF: FBXL3 was regulated by miR-4735-3p and suppressed cell
            proliferation and invasion in non-small cell lung cancer.
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Busino,L., Bassermann,F., Maiolica,A., Lee,C., Nolan,P.M.,
            Godinho,S.I., Draetta,G.F. and Pagano,M.
  TITLE     SCFFbxl3 controls the oscillation of the circadian clock by
            directing the degradation of cryptochrome proteins
  JOURNAL   Science 316 (5826), 900-904 (2007)
   PUBMED   17463251
  REMARK    GeneRIF: study demonstrates that the SCF(Fbxl3)ubiquitin ligase
            controls the oscillations of the circadian clock by mediating the
            degradation of Cry1 and Cry2 proteins
            Erratum:[Science. 2024 May 24;384(6698):eadq4777. doi:
            10.1126/science.adq4777. PMID: 38781400]
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Ilyin,G.P., Rialland,M., Pigeon,C. and Guguen-Guillouzo,C.
  TITLE     cDNA cloning and expression analysis of new members of the
            mammalian F-box protein family
  JOURNAL   Genomics 67 (1), 40-47 (2000)
   PUBMED   10945468
REFERENCE   8  (residues 1 to 428)
  AUTHORS   Chiaur,D.S., Murthy,S., Cenciarelli,C., Parks,W., Loda,M.,
            Inghirami,G., Demetrick,D. and Pagano,M.
  TITLE     Five human genes encoding F-box proteins: chromosome mapping and
            analysis in human tumors
  JOURNAL   Cytogenet Cell Genet 88 (3-4), 255-258 (2000)
   PUBMED   10828603
REFERENCE   9  (residues 1 to 428)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   10 (residues 1 to 428)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC001226.1.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box),
            which function in phosphorylation-dependent ubiquitination. The
            F-box proteins are divided into 3 classes: Fbws containing WD-40
            domains, Fbls containing leucine-rich repeats, and Fbxs containing
            either different protein-protein interaction modules or no
            recognizable motifs. The protein encoded by this gene belongs to
            the Fbls class and, in addition to an F-box, contains several
            tandem leucine-rich repeats and is localized in the nucleus.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072448.1, AL833187.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2152568, SAMEA2152798
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355619.10/ ENSP00000347834.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q22.3"
     Protein         1..428
                     /product="F-box/LRR-repeat protein 3"
                     /note="F-box protein Fbl3a; F-box and leucine-rich repeat
                     protein 3A; F-box/LRR-repeat protein 3A"
                     /calculated_mol_wt=48576
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKT7.1)"
     Region          34..76
                     /region_name="F-box_FBXL3"
                     /note="F-box domain found in F-box/LRR-repeat protein 3
                     (FBXL3) and similar proteins; cd22178"
                     /db_xref="CDD:438949"
     Site            order(35..37,39,43,46..47,50..51,53..55,57..64,66..67)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438949"
     Region          79..428
                     /region_name="FBXL3_LRR"
                     /note="Leucine-rich repeat domain of F-box/LRR-repeat
                     protein 3; cd23957"
                     /db_xref="CDD:467832"
     Site            order(82,92..93,95,97..98,101)
                     /site_type="other"
                     /note="SKP1 interface [polypeptide binding]"
                     /db_xref="CDD:467832"
     Site            order(86..91,119,145..149,181,207,254,256,258,260..262,
                     265,288,292,294,312,314,316..317,336,338..340,343,
                     364..368,389,391,393,406,423..428)
                     /site_type="other"
                     /note="CRY2 interface [polypeptide binding]"
                     /db_xref="CDD:467832"
     Region          119..146
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKT7.1)"
     Region          174..199
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          181..207
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKT7.1)"
     Region          200..225
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          208..233
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKT7.1)"
     Region          234..259
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKT7.1)"
     Region          252..286
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          287..333
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          316..341
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKT7.1)"
     Region          334..360
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          343..368
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKT7.1)"
     Region          361..383
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          369..394
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKT7.1)"
     CDS             1..428
                     /gene="FBXL3"
                     /gene_synonym="FBL3; FBL3A; FBXL3A; IDDSFAS"
                     /coded_by="NM_012158.4:335..1621"
                     /db_xref="CCDS:CCDS9457.1"
                     /db_xref="GeneID:26224"
                     /db_xref="HGNC:HGNC:13599"
                     /db_xref="MIM:605653"
ORIGIN      
        1 mkrggrdsdr nsseegtaek skklrttneh sqtcdwgnll qdiilqvfky lplldrahas
       61 qvcrnwnqvf hmpdlwrcfe felnqpatsy lkathpelik qiikrhsnhl qyvsfkvdss
      121 kesaeaacdi lsqlvncslk tlglistarp sfmdlpkshf isaltvvfvn skslsslkid
      181 dtpvddpslk vlvannsdtl kllkmsscph vspagilcva dqchglrela lnyhllsdel
      241 llalssekhv rlehlridvv senpgqthfh tiqksswdaf irhspkvnlv myfflyeeef
      301 dpffryeipa thlyfgrsvs kdvlgrvgmt cprlvelvvc anglrpldee liriaerckn
      361 lsaiglgece vscsafvefv kmcggrlsql simeevlipd qkysleqihw evskhlgrvw
      421 fpdmmptw
//
LOCUS       NP_001374802             832 aa            linear   PRI 21-NOV-2025
DEFINITION  protein mono-ADP-ribosyltransferase PARP9 isoform d [Homo sapiens].
ACCESSION   NP_001374802
VERSION     NP_001374802.1
DBSOURCE    REFSEQ: accession NM_001387873.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 832)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 832)
  AUTHORS   Pandi,K., Angabo,S., Makkawi,H., Benyamini,H., Elgavish,S. and
            Nussbaum,G.
  TITLE     P. gingivalis-Induced TLR2 Interactome Analysis Reveals Association
            with PARP9
  JOURNAL   J Dent Res 103 (3), 329-338 (2024)
   PUBMED   38344758
  REMARK    GeneRIF: P. gingivalis-Induced TLR2 Interactome Analysis Reveals
            Association with PARP9.
REFERENCE   3  (residues 1 to 832)
  AUTHORS   Thirunavukkarasu,S., Ahmed,M., Rosa,B.A., Boothby,M., Cho,S.H.,
            Rangel-Moreno,J., Mbandi,S.K., Schreiber,V., Gupta,A., Zuniga,J.,
            Mitreva,M., Kaushal,D., Scriba,T.J. and Khader,S.A.
  TITLE     Poly(ADP-ribose) polymerase 9 mediates early protection against
            Mycobacterium tuberculosis infection by regulating type I IFN
            production
  JOURNAL   J Clin Invest 133 (12), e158630 (2023)
   PUBMED   37200107
  REMARK    GeneRIF: Poly(ADP-ribose) polymerase 9 mediates early protection
            against Mycobacterium tuberculosis infection by regulating type I
            IFN production.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 832)
  AUTHORS   Russo,L.C., Tomasin,R., Matos,I.A., Manucci,A.C., Sowa,S.T.,
            Dale,K., Caldecott,K.W., Lehtio,L., Schechtman,D., Meotti,F.C.,
            Bruni-Cardoso,A. and Hoch,N.C.
  TITLE     The SARS-CoV-2 Nsp3 macrodomain reverses PARP9/DTX3L-dependent
            ADP-ribosylation induced by interferon signaling
  JOURNAL   J Biol Chem 297 (3), 101041 (2021)
   PUBMED   34358560
  REMARK    GeneRIF: The SARS-CoV-2 Nsp3 macrodomain reverses
            PARP9/DTX3L-dependent ADP-ribosylation induced by interferon
            signaling.
REFERENCE   5  (residues 1 to 832)
  AUTHORS   Xing,J., Zhang,A., Du,Y., Fang,M., Minze,L.J., Liu,Y.J., Li,X.C.
            and Zhang,Z.
  TITLE     Identification of poly(ADP-ribose) polymerase 9 (PARP9) as a
            noncanonical sensor for RNA virus in dendritic cells
  JOURNAL   Nat Commun 12 (1), 2681 (2021)
   PUBMED   33976210
  REMARK    GeneRIF: Identification of poly(ADP-ribose) polymerase 9 (PARP9) as
            a noncanonical sensor for RNA virus in dendritic cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 832)
  AUTHORS   Jha,R., Agarwal,A., Mahfouz,R., Paasch,U., Grunewald,S.,
            Sabanegh,E., Yadav,S.P. and Sharma,R.
  TITLE     Determination of Poly (ADP-ribose) polymerase (PARP) homologues in
            human ejaculated sperm and its correlation with sperm maturation
  JOURNAL   Fertil Steril 91 (3), 782-790 (2009)
   PUBMED   18339380
  REMARK    GeneRIF: Determination of Poly (ADP-ribose) polymerase (PARP)
            homologues in human ejaculated sperm and its correlation with sperm
            maturation.
REFERENCE   7  (residues 1 to 832)
  AUTHORS   Juszczynski,P., Kutok,J.L., Li,C., Mitra,J., Aguiar,R.C. and
            Shipp,M.A.
  TITLE     BAL1 and BBAP are regulated by a gamma interferon-responsive
            bidirectional promoter and are overexpressed in diffuse large
            B-cell lymphomas with a prominent inflammatory infiltrate
  JOURNAL   Mol Cell Biol 26 (14), 5348-5359 (2006)
   PUBMED   16809771
  REMARK    GeneRIF: BAL1 and BBAP are located on chromosome 3q21 in a
            head-to-head orientation and are regulated by a
            IFN-gamma-responsive bidirectional promoter.
REFERENCE   8  (residues 1 to 832)
  AUTHORS   Aguiar,R.C., Takeyama,K., He,C., Kreinbrink,K. and Shipp,M.A.
  TITLE     B-aggressive lymphoma family proteins have unique domains that
            modulate transcription and exhibit poly(ADP-ribose) polymerase
            activity
  JOURNAL   J Biol Chem 280 (40), 33756-33765 (2005)
   PUBMED   16061477
REFERENCE   9  (residues 1 to 832)
  AUTHORS   Takeyama,K., Aguiar,R.C., Gu,L., He,C., Freeman,G.J., Kutok,J.L.,
            Aster,J.C. and Shipp,M.A.
  TITLE     The BAL-binding protein BBAP and related Deltex family members
            exhibit ubiquitin-protein isopeptide ligase activity
  JOURNAL   J Biol Chem 278 (24), 21930-21937 (2003)
   PUBMED   12670957
REFERENCE   10 (residues 1 to 832)
  AUTHORS   Aguiar,R.C., Yakushijin,Y., Kharbanda,S., Salgia,R., Fletcher,J.A.
            and Shipp,M.A.
  TITLE     BAL is a novel risk-related gene in diffuse large B-cell lymphomas
            that enhances cellular migration
  JOURNAL   Blood 96 (13), 4328-4334 (2000)
   PUBMED   11110709
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092908.9 and AC096861.5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.2377008.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..832
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.1"
     Protein         1..832
                     /product="protein mono-ADP-ribosyltransferase PARP9
                     isoform d"
                     /EC_number="2.4.2.30"
                     /note="poly [ADP-ribose] polymerase 9; poly (ADP-ribose)
                     polymerase 9; PARP-9; b aggressive lymphoma protein;
                     ADP-ribosyltransferase diphtheria toxin-like 9; protein
                     mono-ADP-ribosyltransferase PARP9"
                     /calculated_mol_wt=93934
     Region          95..255
                     /region_name="Macro_Af1521_BAL-like"
                     /note="macrodomain, Af1521-like family; cd02907"
                     /db_xref="CDD:394877"
     Site            order(103..105,116..118,122..128,130,216..222)
                     /site_type="other"
                     /note="ADP-ribose binding site [chemical binding]"
                     /db_xref="CDD:394877"
     Region          288..464
                     /region_name="Macro_BAL-like"
                     /note="macrodomain, B-aggressive lymphoma (BAL)-like
                     family; cd02903"
                     /db_xref="CDD:394874"
     Site            order(303..305,315..317,323..326,329,407..413,447,453)
                     /site_type="other"
                     /note="ADP-ribose binding site [chemical binding]"
                     /db_xref="CDD:394874"
     Region          680..799
                     /region_name="TCCD_inducible_PARP_like"
                     /note="Poly(ADP-ribose) polymerases catalyse the covalent
                     attachment of ADP-ribose units from NAD+ to itself and to
                     a limited number of other DNA binding proteins, which
                     decreases their affinity for DNA. Poly(ADP-ribose)
                     polymerase is a regulatory component...; cd01439"
                     /db_xref="CDD:238719"
     Site            order(682..686,689,693,697..699,701,714..716,726,782)
                     /site_type="other"
                     /note="nad+ binding pocket [chemical binding]"
                     /db_xref="CDD:238719"
     CDS             1..832
                     /gene="PARP9"
                     /gene_synonym="ARTD9; BAL; BAL1; MGC:7868"
                     /coded_by="NM_001387873.1:146..2644"
                     /note="isoform d is encoded by transcript variant 15"
                     /db_xref="GeneID:83666"
                     /db_xref="HGNC:HGNC:24118"
                     /db_xref="MIM:612065"
ORIGIN      
        1 mdfsmkvfaq ifpqwrkgnt eeclpykcse tgalgenysw qipinhndfk ilknnerqlc
       61 evlqnkfgci stlvspvqeg nskslqvfrk mltprielsv wkddltthav davvnaaned
      121 llhggglala lvkaggfeiq eeskqfvary gkvsageiav tgagrlpckq iihavgprwm
      181 ewdkqgctgk lqraivsiln yviyknthik tvaipalssg ifqfplnlct ktivetirvs
      241 lqgkpmmsnl keihlvsned ptvaafkaas efilgkselg qettpsfnam vvnnltlqiv
      301 qghiewqtad vivnsvnphd itvgpvaksi lqqagvemks eflatkakqf qrsqlvlvtk
      361 gfnlfckyiy hvlwhsefpk pqilkhamke clekcieqni tsisfpalgt gnmeikketa
      421 aeilfdevlt fakdhvkhql tvkfvifptd leiykafsse makrskmlsl nnysvpqstr
      481 eekrenglea rspainlmgf nveemyeaha wiqrilslqn hhiiennhil ylgrkehdil
      541 sqlqktssvs iteiispgrt eleiegarad lievvmnied mlckvqeema rkkerglwrs
      601 lgqwtiqqqk tqdemkenii flkcpvpptq elldqkkqfe kcglqvlkve kidnevlmaa
      661 fqrkkkmmee klhrqpvshr lfqqvpyqfc nvvcrvgfqr mystpcdpky gagiyftknl
      721 knlaekakki saadkliyvf eaevltgffc qghplnivpp plspgaidgh dsvvdnvssp
      781 etfvifsgmq aipqylwtct qeyvqsqdys sgpmrpfaqh pwrgfasgsp vd
//
LOCUS       NP_001307562             470 aa            linear   PRI 21-NOV-2025
DEFINITION  myc box-dependent-interacting protein 1 isoform 14 [Homo sapiens].
ACCESSION   NP_001307562 XP_005263703
VERSION     NP_001307562.1
DBSOURCE    REFSEQ: accession NM_001320633.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Saha,O., Melo de Farias,A.R., Pelletier,A., Siedlecki-Wullich,D.,
            Landeira,B.S., Gadaut,J., Carrier,A., Vreulx,A.C., Guyot,K.,
            Shen,Y., Bonnefond,A., Amouyel,P., Tcw,J., Kilinc,D., Queiroz,C.M.,
            Delahaye,F., Lambert,J.C. and Costa,M.R.
  TITLE     The Alzheimer's disease risk gene BIN1 regulates activity-dependent
            gene expression in human-induced glutamatergic neurons
  JOURNAL   Mol Psychiatry 29 (9), 2634-2646 (2024)
   PUBMED   38514804
  REMARK    GeneRIF: The Alzheimer's disease risk gene BIN1 regulates
            activity-dependent gene expression in human-induced glutamatergic
            neurons.
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Picas,L., Andre-Arpin,C., Comunale,F., Bousquet,H., Tsai,F.C.,
            Rico,F., Maiuri,P., Pernier,J., Bodin,S., Nicot,A.S., Laporte,J.,
            Bassereau,P., Goud,B., Gauthier-Rouviere,C. and Miserey,S.
  TITLE     BIN1 regulates actin-membrane interactions during IRSp53-dependent
            filopodia formation
  JOURNAL   Commun Biol 7 (1), 549 (2024)
   PUBMED   38724689
  REMARK    GeneRIF: BIN1 regulates actin-membrane interactions during
            IRSp53-dependent filopodia formation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Garcia-Agudo,L.F., Shi,Z., Smith,I.F., Kramar,E.A., Tran,K.,
            Kawauchi,S., Wang,S., Collins,S., Walker,A., Shi,K.X., Neumann,J.,
            Liang,H.Y., Da Cunha,C., Milinkeviciute,G., Morabito,S.,
            Miyoshi,E., Rezaie,N., Gomez-Arboledas,A., Arvilla,A.M.,
            Ghaemi,D.I., Tenner,A.J., LaFerla,F.M., Wood,M.A., Mortazavi,A.,
            Swarup,V., MacGregor,G.R. and Green,K.N.
  TITLE     BIN1K358R suppresses glial response to plaques in mouse model of
            Alzheimer's disease
  JOURNAL   Alzheimers Dement 20 (4), 2922-2942 (2024)
   PUBMED   38460121
  REMARK    GeneRIF: BIN1[K358R] suppresses glial response to plaques in mouse
            model of Alzheimer's disease.
REFERENCE   5  (residues 1 to 470)
  AUTHORS   Kaur,I., Behl,T., Sundararajan,G., Panneerselvam,P.,
            Vijayakumar,A.R., Senthilkumar,G.P., Venkatachalam,T., Jaglan,D.,
            Yadav,S., Anwer,K., Fuloria,N.K., Sehgal,A., Gulati,M. and
            Chigurupati,S.
  TITLE     BIN1 in the Pursuit of Ousting the Alzheimer's Reign: Impact on
            Amyloid and Tau Neuropathology
  JOURNAL   Neurotox Res 41 (6), 698-707 (2023)
   PUBMED   37847429
  REMARK    GeneRIF: BIN1 in the Pursuit of Ousting the Alzheimer's Reign:
            Impact on Amyloid and Tau Neuropathology.
            Review article
REFERENCE   6  (residues 1 to 470)
  AUTHORS   Ramjaun,A.R., Micheva,K.D., Bouchelet,I. and McPherson,P.S.
  TITLE     Identification and characterization of a nerve terminal-enriched
            amphiphysin isoform
  JOURNAL   J Biol Chem 272 (26), 16700-16706 (1997)
   PUBMED   9195986
REFERENCE   7  (residues 1 to 470)
  AUTHORS   Butler,M.H., David,C., Ochoa,G.C., Freyberg,Z., Daniell,L.,
            Grabs,D., Cremona,O. and De Camilli,P.
  TITLE     Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs
            family, is concentrated in the cortical cytomatrix of axon initial
            segments and nodes of ranvier in brain and around T tubules in
            skeletal muscle
  JOURNAL   J Cell Biol 137 (6), 1355-1367 (1997)
   PUBMED   9182667
REFERENCE   8  (residues 1 to 470)
  AUTHORS   Leprince,C., Romero,F., Cussac,D., Vayssiere,B., Berger,R.,
            Tavitian,A. and Camonis,J.H.
  TITLE     A new member of the amphiphysin family connecting endocytosis and
            signal transduction pathways
  JOURNAL   J Biol Chem 272 (24), 15101-15105 (1997)
   PUBMED   9182529
REFERENCE   9  (residues 1 to 470)
  AUTHORS   Sakamuro,D., Elliott,K.J., Wechsler-Reya,R. and Prendergast,G.C.
  TITLE     BIN1 is a novel MYC-interacting protein with features of a tumour
            suppressor
  JOURNAL   Nat Genet 14 (1), 69-77 (1996)
   PUBMED   8782822
  REMARK    GeneRIF: A nucleocytosolic myc-interacting isoform of Bin1 has
            properties of a tumor suppressor.
REFERENCE   10 (residues 1 to 470)
  AUTHORS   Negorev,D., Riethman,H., Wechsler-Reya,R., Sakamuro,D.,
            Prendergast,G.C. and Simon,D.
  TITLE     The Bin1 gene localizes to human chromosome 2q14 by PCR analysis of
            somatic cell hybrids and fluorescence in situ hybridization
  JOURNAL   Genomics 33 (2), 329-331 (1996)
   PUBMED   8725406
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL713697.1, AK295300.1,
            AC012508.10, BC004101.2 and BM711160.1.
            
            On Mar 2, 2016 this sequence version replaced XP_005263703.1.
            
            Summary: This gene encodes several isoforms of a nucleocytoplasmic
            adaptor protein, one of which was initially identified as a
            MYC-interacting protein with features of a tumor suppressor.
            Isoforms that are expressed in the central nervous system may be
            involved in synaptic vesicle endocytosis and may interact with
            dynamin, synaptojanin, endophilin, and clathrin. Isoforms that are
            expressed in muscle and ubiquitously expressed isoforms localize to
            the cytoplasm and nucleus and activate a caspase-independent
            apoptotic process. Studies in mouse suggest that this gene plays an
            important role in cardiac muscle development. Alternate splicing of
            the gene results in several transcript variants encoding different
            isoforms. Aberrant splice variants expressed in tumor cell lines
            have also been described. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (14) lacks four alternate in-frame
            exons compared to variant 1. The resulting isoform (14) has the
            same N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295300.1, SRR11853560.16479.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..470
                     /product="myc box-dependent-interacting protein 1 isoform
                     14"
                     /note="amphiphysin II; box dependant MYC interacting
                     protein 1; amphiphysin-like protein; box-dependent
                     myc-interacting protein 1; amphiphysin 2"
                     /calculated_mol_wt=51565
     Region          2..122
                     /region_name="Interaction with BIN2.
                     /evidence=ECO:0000269|PubMed:10903846"
                     /note="propagated from UniProtKB/Swiss-Prot (O00499.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O00499.1)"
     Region          31..272
                     /region_name="BAR_Amphiphysin_I_II"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin
                     I and II; cd07611"
                     /db_xref="CDD:153295"
     Site            order(50,53..54,58,61,64..65,68,78..79,81..82,85..86,
                     88..89,92,100,228,231..232,234,239..240,242..243,246..247,
                     249..250,253..254,256..257,261,264)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153295"
     Site            order(73,80,139,142,145..146,170)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153295"
     Region          <260..>356
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00499.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O00499.1)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O00499.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19367720; propagated from
                     UniProtKB/Swiss-Prot (O00499.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O00499.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O00499.1)"
     Region          398..469
                     /region_name="SH3_Bin1"
                     /note="Src Homology 3 domain of Bridging integrator 1
                     (Bin1), also called Amphiphysin-2; cd12139"
                     /db_xref="CDD:213015"
     Site            order(409..415,434,436..439,462,464..465)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213015"
     CDS             1..470
                     /gene="BIN1"
                     /gene_synonym="AMPH2; AMPHL; CNM2; SH3P9"
                     /coded_by="NM_001320633.2:212..1624"
                     /note="isoform 14 is encoded by transcript variant 14"
                     /db_xref="GeneID:274"
                     /db_xref="HGNC:HGNC:1052"
                     /db_xref="MIM:601248"
ORIGIN      
        1 maemgskgvt agkiasnvqk kltraqekvl qklgkadetk deqfeqcvqn fnkqltegtr
       61 lqkdlrtyla svkamheask klneclqevy epdwpgrdea nkiaenndll wmdyhqklvd
      121 qalltmdtyl gqfpdiksri akrgrklvdy dsarhhyesl qtakkkdeak iakpvsllek
      181 aapqwcqgkl qahlvaqtnl lrnqaeeeli kaqkvfeemn vdlqeelpsl wnsrvgfyvn
      241 tfqsiaglee nfhkemskln qnlndvlvgl ekqhgsntft vkaqpsdnap akgnkspspp
      301 dgspaatpei rvnhepepag gatpgatlpk spsqpaease vaggtqpaag aqepgetaas
      361 eaassslpav vvetfpatvn gtveggsgag rldlppgfmf kvqaqhdyta tdtdelqlka
      421 gdvvlvipfq npeeqdegwl mgvkesdwnq hkelekcrgv fpenftervp
//
LOCUS       NP_001307559             410 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 1 isoform 6 precursor [Homo
            sapiens].
ACCESSION   NP_001307559
VERSION     NP_001307559.1
DBSOURCE    REFSEQ: accession NM_001320630.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Chatterjee,M., Saha,S., Dutta,N., Sinha,S. and Mukhopadhyay,K.
  TITLE     Kainate receptor subunit 1 (GRIK1) risk variants and GRIK1
            deficiency were detected in the Indian ADHD probands
  JOURNAL   Sci Rep 12 (1), 18449 (2022)
   PUBMED   36323684
  REMARK    GeneRIF: Kainate receptor subunit 1 (GRIK1) risk variants and GRIK1
            deficiency were detected in the Indian ADHD probands.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Hirbec,H., Francis,J.C., Lauri,S.E., Braithwaite,S.P., Coussen,F.,
            Mulle,C., Dev,K.K., Coutinho,V., Meyer,G., Isaac,J.T.,
            Collingridge,G.L. and Henley,J.M.
  TITLE     Rapid and differential regulation of AMPA and kainate receptors at
            hippocampal mossy fibre synapses by PICK1 and GRIP
  JOURNAL   Neuron 37 (4), 625-638 (2003)
   PUBMED   12597860
  REMARK    Erratum:[Neuron. 2003 May 22;38(4):673. Couthino V [corrected to
            Coutinho V]]
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Barbon,A. and Barlati,S.
  TITLE     Genomic organization, proposed alternative splicing mechanisms, and
            RNA editing structure of GRIK1
  JOURNAL   Cytogenet Cell Genet 88 (3-4), 236-239 (2000)
   PUBMED   10828597
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Bortolotto,Z.A., Clarke,V.R., Delany,C.M., Parry,M.C., Smolders,I.,
            Vignes,M., Ho,K.H., Miu,P., Brinton,B.T., Fantaske,R., Ogden,A.,
            Gates,M., Ornstein,P.L., Lodge,D., Bleakman,D. and
            Collingridge,G.L.
  TITLE     Kainate receptors are involved in synaptic plasticity
  JOURNAL   Nature 402 (6759), 297-301 (1999)
   PUBMED   10580501
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Clarke,V.R., Ballyk,B.A., Hoo,K.H., Mandelzys,A., Pellizzari,A.,
            Bath,C.P., Thomas,J., Sharpe,E.F., Davies,C.H., Ornstein,P.L.,
            Schoepp,D.D., Kamboj,R.K., Collingridge,G.L., Lodge,D. and
            Bleakman,D.
  TITLE     A hippocampal GluR5 kainate receptor regulating inhibitory synaptic
            transmission
  JOURNAL   Nature 389 (6651), 599-603 (1997)
   PUBMED   9335499
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Nutt,S.L. and Kamboj,R.K.
  TITLE     RNA editing of human kainate receptor subunits
  JOURNAL   Neuroreport 5 (18), 2625-2629 (1994)
   PUBMED   7696618
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Roche,K.W., Raymond,L.A., Blackstone,C. and Huganir,R.L.
  TITLE     Transmembrane topology of the glutamate receptor subunit GluR6
  JOURNAL   J Biol Chem 269 (16), 11679-11682 (1994)
   PUBMED   8163463
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Gregor,P., O'Hara,B.F., Yang,X. and Uhl,G.R.
  TITLE     Expression and novel subunit isoforms of glutamate receptor genes
            GluR5 and GluR6
  JOURNAL   Neuroreport 4 (12), 1343-1346 (1993)
   PUBMED   8260617
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC028238.1.
            
            Summary: Glutamate receptors are the predominant excitatory
            neurotransmitter receptors in the mammalian brain and are activated
            in a variety of normal neurophysiologic processes. This gene
            product belongs to the kainate family of glutamate receptors, which
            are composed of four subunits and function as ligand-activated ion
            channels. The subunit encoded by this gene is subject to RNA
            editing (CAG->CGG; Q->R) within the second transmembrane domain,
            which is thought to alter the properties of ion flow. Alternative
            splicing, resulting in transcript variants encoding different
            isoforms, has been noted for this gene. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028238.1, SRR14038191.2844068.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            undergoes RNA editing :: PMID: 7696618, 10828597
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..410
                     /product="glutamate receptor ionotropic, kainate 1 isoform
                     6 precursor"
                     /note="excitatory amino acid receptor 3; glutamate
                     receptor 5; glutamate receptor ionotropic, kainate 1;
                     GluK1(del_e2)"
                     /calculated_mol_wt=43449
     sig_peptide     1..30
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
                     /calculated_mol_wt=3510
     Region          38..403
                     /region_name="PBP1_iGluR_Kainate"
                     /note="N-terminal leucine-isoleucine-valine binding
                     protein (LIVBP)-like domain of the kainate receptors;
                     cd06382"
                     /db_xref="CDD:380605"
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            order(88..90,94,125,177,180,184,187,190..191,201..204)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380605"
     Site            276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            379
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     CDS             1..410
                     /gene="GRIK1"
                     /gene_synonym="EAA3; EEA3; GLR5; GluK1; gluR-5; GLUR5"
                     /coded_by="NM_001320630.2:497..1729"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:2897"
                     /db_xref="HGNC:HGNC:4579"
                     /db_xref="MIM:138245"
ORIGIN      
        1 mehgtllaqp glwtrdtswa llyflcyilp qtapqvlrig gifetvenep vnveelafkf
       61 avtsinrnrt lmpnttltyd iqrinlfdsf easrracdql algvaalfgp shsssvsavq
      121 sicnalevph iqtrwkhpsv dnkdlfyinl ypdyaaisra ildlvlyynw ktvtvvyeds
      181 tglirlqeli kapsryniki kirqlpsgnk dakpllkemk kgkefyvifd cshetaaeil
      241 kqilfmgmmt eyyhyffttl dlfaldlely rysgvnmtgf rllnidnphv ssiiekwsme
      301 rlqapprpet glldgmmtte aalmydavym vaiashrasq ltvsslqchr hkpwrlgprf
      361 mnlikearwd gltghitfnk tnglrkdfdl diislkeegt ekvtsltink
//
LOCUS       NP_001317023            1500 aa            linear   PRI 21-NOV-2025
DEFINITION  neurexin-1 isoform alpha13 precursor [Homo sapiens].
ACCESSION   NP_001317023 XP_016860806
VERSION     NP_001317023.1
DBSOURCE    REFSEQ: accession NM_001330094.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1500)
  AUTHORS   Sebastian,R., Jin,K., Pavon,N., Bansal,R., Potter,A., Song,Y.,
            Babu,J., Gabriel,R., Sun,Y., Aronow,B. and Pak,C.
  TITLE     Schizophrenia-associated NRXN1 deletions induce
            developmental-timing- and cell-type-specific vulnerabilities in
            human brain organoids
  JOURNAL   Nat Commun 14 (1), 3770 (2023)
   PUBMED   37355690
  REMARK    GeneRIF: Schizophrenia-associated NRXN1 deletions induce
            developmental-timing- and cell-type-specific vulnerabilities in
            human brain organoids.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1500)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1500)
  AUTHORS   Rhoades,R., Henry,B., Prichett,D., Fang,Y. and Teng,S.
  TITLE     Computational Saturation Mutagenesis to Investigate the Effects of
            Neurexin-1 Mutations on AlphaFold Structure
  JOURNAL   Genes (Basel) 13 (5), 789 (2022)
   PUBMED   35627176
  REMARK    GeneRIF: Computational Saturation Mutagenesis to Investigate the
            Effects of Neurexin-1 Mutations on AlphaFold Structure.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1500)
  AUTHORS   Aksu Uzunhan,T. and Ayaz,A.
  TITLE     Homozygous exonic and intragenic NRXN1 deletion presenting as
            either West syndrome or autism spectrum disorder in two siblings
  JOURNAL   Clin Neurol Neurosurg 214, 107141 (2022)
   PUBMED   35101781
  REMARK    GeneRIF: Homozygous exonic and intragenic NRXN1 deletion presenting
            as either West syndrome or autism spectrum disorder in two
            siblings.
REFERENCE   5  (residues 1 to 1500)
  AUTHORS   Yan,Q., Weyn-Vanhentenryck,S.M., Wu,J., Sloan,S.A., Zhang,Y.,
            Chen,K., Wu,J.Q., Barres,B.A. and Zhang,C.
  TITLE     Systematic discovery of regulated and conserved alternative exons
            in the mammalian brain reveals NMD modulating chromatin regulators
  JOURNAL   Proc Natl Acad Sci U S A 112 (11), 3445-3450 (2015)
   PUBMED   25737549
REFERENCE   6  (residues 1 to 1500)
  AUTHORS   Tabuchi,K. and Sudhof,T.C.
  TITLE     Structure and evolution of neurexin genes: insight into the
            mechanism of alternative splicing
  JOURNAL   Genomics 79 (6), 849-859 (2002)
   PUBMED   12036300
REFERENCE   7  (residues 1 to 1500)
  AUTHORS   Rowen,L., Young,J., Birditt,B., Kaur,A., Madan,A., Philipps,D.L.,
            Qin,S., Minx,P., Wilson,R.K., Hood,L. and Graveley,B.R.
  TITLE     Analysis of the human neurexin genes: alternative splicing and the
            generation of protein diversity
  JOURNAL   Genomics 79 (4), 587-597 (2002)
   PUBMED   11944992
REFERENCE   8  (residues 1 to 1500)
  AUTHORS   Ichtchenko,K., Hata,Y., Nguyen,T., Ullrich,B., Missler,M.,
            Moomaw,C. and Sudhof,T.C.
  TITLE     Neuroligin 1: a splice site-specific ligand for beta-neurexins
  JOURNAL   Cell 81 (3), 435-443 (1995)
   PUBMED   7736595
REFERENCE   9  (residues 1 to 1500)
  AUTHORS   Ullrich,B., Ushkaryov,Y.A. and Sudhof,T.C.
  TITLE     Cartography of neurexins: more than 1000 isoforms generated by
            alternative splicing and expressed in distinct subsets of neurons
  JOURNAL   Neuron 14 (3), 497-507 (1995)
   PUBMED   7695896
REFERENCE   10 (residues 1 to 1500)
  AUTHORS   Ushkaryov,Y.A., Petrenko,A.G., Geppert,M. and Sudhof,T.C.
  TITLE     Neurexins: synaptic cell surface proteins related to the
            alpha-latrotoxin receptor and laminin
  JOURNAL   Science 257 (5066), 50-56 (1992)
   PUBMED   1621094
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007682.3, AC009234.3,
            AC007462.3, AC068725.5, AC069550.4 and AC078994.3.
            
            On Aug 16, 2016 this sequence version replaced XP_016860806.1.
            
            Summary: This gene encodes a single-pass type I membrane protein
            that belongs to the neurexin family. Neurexins are cell-surface
            receptors that bind neuroligins to form Ca(2+)-dependent
            neurexin/neuroligin complexes at synapses in the central nervous
            system. This complex is required for efficient neurotransmission
            and is involved in the formation of synaptic contacts. Three
            members of this gene family have been studied in detail and are
            estimated to generate over 3,000 variants through the use of two
            alternative promoters (alpha and beta) and extensive alternative
            splicing in each family member. Recently, a third promoter (gamma)
            was identified for this gene in the 3' region. Mutations in this
            gene are associated with Pitt-Hopkins-like syndrome-2 and may
            contribute to susceptibility to schizophrenia. [provided by RefSeq,
            Aug 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1966682, SAMEA1968189
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1500
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.3"
     Protein         1..1500
                     /product="neurexin-1 isoform alpha13 precursor"
                     /note="neurexin I"
                     /calculated_mol_wt=161740
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3097
     Region          30..190
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Region          303..442
                     /region_name="LamG"
                     /note="Laminin G domain; smart00282"
                     /db_xref="CDD:214598"
     Region          499..648
                     /region_name="LamG"
                     /note="Laminin G domain; smart00282"
                     /db_xref="CDD:214598"
     Region          676..709
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          742..872
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          929..1057
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          1152..1300
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          1445..1463
                     /region_name="4.1m"
                     /note="putative band 4.1 homologues' binding motif;
                     smart00294"
                     /db_xref="CDD:128590"
     CDS             1..1500
                     /gene="NRXN1"
                     /gene_synonym="Hs.22998; PTHSL2; SCZD17"
                     /coded_by="NM_001330094.2:1074..5576"
                     /note="isoform alpha13 precursor is encoded by transcript
                     variant alpha13"
                     /db_xref="GeneID:9378"
                     /db_xref="HGNC:HGNC:8008"
                     /db_xref="MIM:600565"
ORIGIN      
        1 mgtallqrgg cfllclslll lgcwaelgsg lefpgaegqw trfpkwnacc esemsfqlkt
       61 rsarglvlyf ddegfcdfle liltrggrlq lsfsifcaep atlladtpvn dgawhsvrir
      121 rqfrnttlfi dqveakwvev kskrrdmtvf sglfvgglpp elraaalklt lasvrerepf
      181 kgwirdvrvn ssqvlpvdsg evklddeppn sgggspceag eegeggvcln ggvcsvvddq
      241 avcdcsrtgf rgkdcsqedn nveglahlmm gdqgkeeyia tfkgseyfcy dlsqnpiqss
      301 sdeitlsfkt lqrnglmlht gksadyvnla lkngavslvi nlgsgafeal vepvngkfnd
      361 nawhdvkvtr nlrqhsgigh amvtisvdgi ltttgytqed ytmlgsddff yvggspstad
      421 lpgspvsnnf mgclkevvyk nndvrlelsr lakqgdpkmk ihgvvafkce nvatldpitf
      481 etpesfislp kwnakktgsi sfdfrttepn glilfshgkp rhqkdakhpq mikvdffaie
      541 mldghlylll dmgsgtikik allkkvndge wyhvdfqrdg rsgtisvntl rtpytapges
      601 eildlddely lgglpenkag lvfptevwta llnygyvgci rdlfidgqsk dirqmaevqs
      661 tagvkpscsk etakpclsnp cknngmcrdg wnryvcdcsg tgylgrscer eatvlsydgs
      721 mfmkiqlpvv mhteaedvsl rfrsqraygi lmattsrdsa dtlrleldag rvkltvnldc
      781 irincnsskg petlfagynl ndnewhtvrv vrrgkslklt vddqqamtgq magdhtrlef
      841 hnietgiite rrylssvpsn fighlqsltf ngmayidlck ngdidyceln arfgfrniia
      901 dpvtfktkss yvalatlqay tsmhlffqfk ttsldglily nsgdgndfiv velvkgylhy
      961 vfdlgnganl ikgssnkpln dnqwhnvmis rdtsnlhtvk idtkittqit agarnldlks
     1021 dlyiggvake tykslpklvh akegfqgcla svdlngrlpd lisdalfcng qiergcegps
     1081 ttcqedscsn qgvclqqwdg fscdcsmtsf sgplcndpgt tyifskgggq itykwppndr
     1141 pstradrlai gfstvqkeav lvrvdsssgl gdylelhihq gkigvkfnvg tddiaieesn
     1201 aiindgkyhv vrftrsggna tlqvdswpvi erypagnndn erlaiarqri pyrlgrvvde
     1261 wlldkgrqlt ifnsqatiii ggkeqgqpfq gqlsglyyng lkvlnmaaen daniaivgnv
     1321 rlvgevpssm ttestatamq semstsimet tttlatstar rgkpptkepi sqttddilva
     1381 saecpsdded idpcepssan ptraggrepy pgsaevires ssttgmvvgi vaaaalcili
     1441 llyamykyrn rdegsyhvde srnyisnsaq sngavvkekq pssakssnkn kknkdkeyyv
//
LOCUS       NP_001372183             173 aa            linear   PRI 21-NOV-2025
DEFINITION  protein tyrosine phosphatase type IVA 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001372183 XP_016866759
VERSION     NP_001372183.1
DBSOURCE    REFSEQ: accession NM_001385254.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Cho,M.J., Lee,D.G., Lee,J.W., Hwang,B., Yoon,S.J., Lee,S.J.,
            Park,Y.J., Park,S.H., Lee,H.G., Kim,Y.H., Lee,C.H., Lee,J.,
            Lee,N.K., Han,T.S., Cho,H.S., Moon,J.H., Lee,G.S., Bae,K.H.,
            Hwang,G.S., Lee,S.H., Chung,S.J., Shim,S., Cho,J., Oh,G.T.,
            Kwon,Y.G., Park,J.G. and Min,J.K.
  TITLE     Endothelial PTP4A1 mitigates vascular inflammation via USF1/A20
            axis-mediated NF-kappaB inactivation
  JOURNAL   Cardiovasc Res 119 (5), 1265-1278 (2023)
   PUBMED   36534975
  REMARK    GeneRIF: Endothelial PTP4A1 mitigates vascular inflammation via
            USF1/A20 axis-mediated NF-kappaB inactivation.
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Hu,H., Ye,L. and Liu,Z.
  TITLE     GINS2 regulates the proliferation and apoptosis of colon cancer
            cells through PTP4A1
  JOURNAL   Mol Med Rep 25 (4) (2022)
   PUBMED   35137928
  REMARK    GeneRIF: GINS2 regulates the proliferation and apoptosis of colon
            cancer cells through PTP4A1.
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 173)
  AUTHORS   Li,O., Jiang,B., Yi,W.M., Zhang,Y., Yang,P.Z., Guo,C., Sun,Z.P. and
            Peng,C.
  TITLE     LncRNA NEAT1 promotes cell proliferation, migration, and invasion
            via the miR-186-5p/PTP4A1 axis in cholangiocarcinoma
  JOURNAL   Kaohsiung J Med Sci 37 (5), 379-391 (2021)
   PUBMED   33502823
  REMARK    GeneRIF: LncRNA NEAT1 promotes cell proliferation, migration, and
            invasion via the miR-186-5p/PTP4A1 axis in cholangiocarcinoma.
REFERENCE   6  (residues 1 to 173)
  AUTHORS   Andreev,D.E., O'Connor,P.B., Fahey,C., Kenny,E.M., Terenin,I.M.,
            Dmitriev,S.E., Cormican,P., Morris,D.W., Shatsky,I.N. and
            Baranov,P.V.
  TITLE     Translation of 5' leaders is pervasive in genes resistant to eIF2
            repression
  JOURNAL   Elife 4, e03971 (2015)
   PUBMED   25621764
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 173)
  AUTHORS   Tsujimoto,H., Nishizuka,S., Redpath,J.L. and Stanbridge,E.J.
  TITLE     Differential gene expression in tumorigenic and nontumorigenic HeLa
            x normal human fibroblast hybrid cells
  JOURNAL   Mol Carcinog 26 (4), 298-304 (1999)
   PUBMED   10569806
REFERENCE   8  (residues 1 to 173)
  AUTHORS   Peng,Y., Genin,A., Spinner,N.B., Diamond,R.H. and Taub,R.
  TITLE     The gene encoding human nuclear protein tyrosine phosphatase,
            PRL-1. Cloning, chromosomal localization, and identification of an
            intron enhancer
  JOURNAL   J Biol Chem 273 (27), 17286-17295 (1998)
   PUBMED   9642300
REFERENCE   9  (residues 1 to 173)
  AUTHORS   Dayton,M.A. and Knobloch,T.J.
  TITLE     Multiple phosphotyrosine phosphatase mRNAs are expressed in the
            human lung fibroblast cell line WI-38
  JOURNAL   Recept Signal Transduct 7 (4), 241-256 (1997)
   PUBMED   9633825
REFERENCE   10 (residues 1 to 173)
  AUTHORS   Cates,C.A., Michael,R.L., Stayrook,K.R., Harvey,K.A., Burke,Y.D.,
            Randall,S.K., Crowell,P.L. and Crowell,D.N.
  TITLE     Prenylation of oncogenic human PTP(CAAX) protein tyrosine
            phosphatases
  JOURNAL   Cancer Lett 110 (1-2), 49-55 (1996)
   PUBMED   9018080
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL135905.6.
            
            On Jul 13, 2020 this sequence version replaced XP_016866759.1.
            
            Summary: This gene encodes a member of a small class of prenylated
            protein tyrosine phosphatases (PTPs), which contain a PTP domain
            and a characteristic C-terminal prenylation motif. The encoded
            protein is a cell signaling molecule that plays regulatory roles in
            a variety of cellular processes, including cell proliferation and
            migration. The protein may also be involved in cancer development
            and metastasis. This tyrosine phosphatase is a nuclear protein, but
            may associate with plasma membrane by means of its prenylation
            motif. Pseudogenes related to this gene are located on chromosomes
            1, 2, 5, 7, 11 and X. [provided by RefSeq, Jun 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.679746.1,
                                           SRR14038193.3496651.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q12"
     Protein         1..173
                     /product="protein tyrosine phosphatase type IVA 1 isoform
                     1"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase type IVA protein 1;
                     protein-tyrosine phosphatase of regenerating liver 1;
                     PVT1/PTP4A1 fusion; protein tyrosine phosphatase type IVA,
                     member 1"
                     /calculated_mol_wt=19684
     mat_peptide     1..170
                     /product="Protein tyrosine phosphatase type IVA 1.
                     /id=PRO_0000094780"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93096.2)"
                     /calculated_mol_wt=19471
     Region          1..167
                     /region_name="PTP-IVa1"
                     /note="protein tyrosine phosphatase type IVA 1; cd18537"
                     /db_xref="CDD:350513"
     Site            order(5,7,72..73,108..110,137..140,142,144)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:350513"
     Site            order(47,53..54,56,59,64..68)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:350513"
     Region          97..132
                     /region_name="Interaction with ATF5.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93096.2)"
     Site            170
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q93096.2)"
     CDS             1..173
                     /gene="PTP4A1"
                     /gene_synonym="HH72; PRL-1; PRL1; PTP(CAAX1); PTPCAAX1"
                     /coded_by="NM_001385254.1:797..1318"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4965.1"
                     /db_xref="GeneID:7803"
                     /db_xref="HGNC:HGNC:9634"
                     /db_xref="MIM:601585"
ORIGIN      
        1 marmnrpapv evtyknmrfl ithnptnatl nkfieelkky gvttivrvce atydttlvek
       61 egihvldwpf ddgappsnqi vddwlslvki kfreepgcci avhcvaglgr apvlvalali
      121 eggmkyedav qfirqkrrga fnskqllyle kyrpkmrlrf kdsnghrnnc ciq
//
LOCUS       NP_001138238             438 aa            linear   PRI 21-NOV-2025
DEFINITION  dnaJ homolog subfamily C member 7 isoform 2 [Homo sapiens].
ACCESSION   NP_001138238
VERSION     NP_001138238.1
DBSOURCE    REFSEQ: accession NM_001144766.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Wang,S., Zheng,X., Wei,Q., Lin,J., Yang,T., Xiao,Y., Jiang,Q.,
            Li,C. and Shang,H.
  TITLE     Rare DNAJC7 Variants May Play a Minor Role in Chinese Patients with
            ALS
  JOURNAL   Mol Neurobiol 61 (4), 2265-2269 (2024)
   PUBMED   37870677
  REMARK    GeneRIF: Rare DNAJC7 Variants May Play a Minor Role in Chinese
            Patients with ALS.
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Dilliott,A.A., Andary,C.M., Stoltz,M., Petropavlovskiy,A.A.,
            Farhan,S.M.K. and Duennwald,M.L.
  TITLE     DnaJC7 in Amyotrophic Lateral Sclerosis
  JOURNAL   Int J Mol Sci 23 (8), 4076 (2022)
   PUBMED   35456894
  REMARK    GeneRIF: DnaJC7 in Amyotrophic Lateral Sclerosis.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Moffatt,N.S., Bruinsma,E., Uhl,C., Obermann,W.M. and Toft,D.
  TITLE     Role of the cochaperone Tpr2 in Hsp90 chaperoning
  JOURNAL   Biochemistry 47 (31), 8203-8213 (2008)
   PUBMED   18620420
  REMARK    GeneRIF: Data show that Tpr2 associates with Hsp90 and Hsp70
            complexes, promoted the accumulation of Hsp70 in PR heterocomplexes
            in the presence of Hsp90. Thus, Tpr2 has the potential to regulate
            PR chaperoning.
REFERENCE   6  (residues 1 to 438)
  AUTHORS   Camargo,L.M., Collura,V., Rain,J.C., Mizuguchi,K., Hermjakob,H.,
            Kerrien,S., Bonnert,T.P., Whiting,P.J. and Brandon,N.J.
  TITLE     Disrupted in Schizophrenia 1 Interactome: evidence for the close
            connectivity of risk genes and a potential synaptic basis for
            schizophrenia
  JOURNAL   Mol Psychiatry 12 (1), 74-86 (2007)
   PUBMED   17043677
REFERENCE   7  (residues 1 to 438)
  AUTHORS   Rush,J., Moritz,A., Lee,K.A., Guo,A., Goss,V.L., Spek,E.J.,
            Zhang,H., Zha,X.M., Polakiewicz,R.D. and Comb,M.J.
  TITLE     Immunoaffinity profiling of tyrosine phosphorylation in cancer
            cells
  JOURNAL   Nat Biotechnol 23 (1), 94-101 (2005)
   PUBMED   15592455
REFERENCE   8  (residues 1 to 438)
  AUTHORS   Brychzy,A., Rein,T., Winklhofer,K.F., Hartl,F.U., Young,J.C. and
            Obermann,W.M.
  TITLE     Cofactor Tpr2 combines two TPR domains and a J domain to regulate
            the Hsp70/Hsp90 chaperone system
  JOURNAL   EMBO J 22 (14), 3613-3623 (2003)
   PUBMED   12853476
  REMARK    GeneRIF: TPR2 combines two TPR domains and a J domain to regulate
            the Hsp70/Hsp90 chaperone system.
REFERENCE   9  (residues 1 to 438)
  AUTHORS   Ohtsuka,K. and Hata,M.
  TITLE     Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a
            proposal for their classification and nomenclature
  JOURNAL   Cell Stress Chaperones 5 (2), 98-112 (2000)
   PUBMED   11147971
REFERENCE   10 (residues 1 to 438)
  AUTHORS   Murthy,A.E., Bernards,A., Church,D., Wasmuth,J. and Gusella,J.F.
  TITLE     Identification and characterization of two novel tetratricopeptide
            repeat-containing genes
  JOURNAL   DNA Cell Biol 15 (9), 727-735 (1996)
   PUBMED   8836031
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC105024.8, AK298860.1,
            AC125257.4 and BQ445927.1.
            
            Summary: This gene encodes a member of the DNAJ heat shock protein
            40 family of proteins that is characterized by two N-terminal
            tetratricopeptide repeat domains and a C-terminal DNAJ domain. This
            protein binds the chaperone proteins heat shock proteins 70 and 90
            in an ATP-dependent manner and may function as a co-chaperone.
            Pseudogenes of this gene are found on chromosomes 1 and 6.
            Alternate splicing results in multiple transcript
            variants.[provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (2) is
            shorter at the N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK298860.1, SRR14038191.472980.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..438
                     /product="dnaJ homolog subfamily C member 7 isoform 2"
                     /note="tetratricopeptide repeat domain 2; dnaJ homolog
                     subfamily C member 7; TPR repeat protein 2;
                     tetratricopeptide repeat protein 2; DnaJ (Hsp40) homolog,
                     subfamily C, member 7"
                     /calculated_mol_wt=49966
     Region          5..35
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          11..>191
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          40..68
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          89..114
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(90..91,94..95,97,121,124..125,128..129,131..132,155,
                     158..159,162..163,166)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          113..342
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          119..149
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          154..182
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(201,204..205,208..209,211,239,242..243,246..247,
                     249..250,273,276..277,280..281,284)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          201..228
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          233..267
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          272..300
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          321..>392
                     /region_name="PRK10767"
                     /note="chaperone protein DnaJ; Provisional"
                     /db_xref="CDD:236757"
     CDS             1..438
                     /gene="DNAJC7"
                     /gene_synonym="DJ11; DJC7; TPR2; TTC2"
                     /coded_by="NM_001144766.3:215..1531"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45678.1"
                     /db_xref="GeneID:7266"
                     /db_xref="HGNC:HGNC:12392"
                     /db_xref="MIM:601964"
ORIGIN      
        1 mcpknasyyg nraatlmmlg rfrealgdaq qsvrlddsfv rghlregkch lslgnamaac
       61 rsfqraleld hknaqaqqef knanavmeye kiaetdfekr dfrkvvfcmd ralefapach
      121 rfkilkaecl amlgrypeaq svasdilrmd stnadalyvr glclyyedci ekavqffvqa
      181 lrmapdheka ciacrnakal kakkedgnka fkegnyklay elytealgid pnniktnakl
      241 ycnrgtvnsk lrklddaied ctnavklddt yikaylrraq cymdteqyee avrdyekvyq
      301 tektkehkql lknaqlelkk skrkdyykil gvdknasede ikkayrkral mhhpdrhsga
      361 saevqkeeek kfkevgeaft ilsdpkkktr ydsgqdldee gmnmgdfdpn nifkaffggp
      421 ggfsfeasgp gnfffqfg
//
LOCUS       NP_001273104            1054 aa            linear   PRI 21-NOV-2025
DEFINITION  C2 domain-containing protein 5 isoform b [Homo sapiens].
ACCESSION   NP_001273104 XP_005253591
VERSION     NP_001273104.1
DBSOURCE    REFSEQ: accession NM_001286175.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1054)
  AUTHORS   Chapman,D.E., Reddy,B.J.N., Huy,B., Bovyn,M.J., Cruz,S.J.S.,
            Al-Shammari,Z.M., Han,H., Wang,W., Smith,D.S. and Gross,S.P.
  TITLE     Regulation of in vivo dynein force production by CDK5 and
            14-3-3epsilon and KIAA0528
  JOURNAL   Nat Commun 10 (1), 228 (2019)
   PUBMED   30651536
  REMARK    GeneRIF: Study finds that CDK5, 14-3-3 epsilon, and KIAA0528 are
            all essential for cytoplasmic dynein force adaptation and that they
            regulate the transport of lipid droplets, lysosomes, and
            mitochondria.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1054)
  AUTHORS   Lu,Y., Ma,J., Li,Y., Huang,J., Zhang,S., Yin,Z., Ren,J., Huang,K.,
            Wu,G., Yang,K. and Xu,S.
  TITLE     CDP138 silencing inhibits TGF-beta/Smad signaling to impair
            radioresistance and metastasis via GDF15 in lung cancer
  JOURNAL   Cell Death Dis 8 (9), e3036 (2017)
   PUBMED   28880265
  REMARK    GeneRIF: Enhanced radiosensitivity and decreased migration in cells
            caused by CDP138 knockdown are partially dependent on GDF15
            inhibition.
            Erratum:[Cell Death Dis. 2024 Jul 31;15(7):549. doi:
            10.1038/s41419-024-06823-2. PMID: 39085215]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1054)
  AUTHORS   Xu,S., Li,X., Gong,Z., Wang,W., Li,Y., Nair,B.C., Piao,H., Yang,K.,
            Wu,G. and Chen,J.
  TITLE     Proteomic analysis of the human cyclin-dependent kinase family
            reveals a novel CDK5 complex involved in cell growth and migration
  JOURNAL   Mol Cell Proteomics 13 (11), 2986-3000 (2014)
   PUBMED   25096995
REFERENCE   7  (residues 1 to 1054)
  AUTHORS   Xie,X., Gong,Z., Mansuy-Aubert,V., Zhou,Q.L., Tatulian,S.A.,
            Sehrt,D., Gnad,F., Brill,L.M., Motamedchaboki,K., Chen,Y.,
            Czech,M.P., Mann,M., Kruger,M. and Jiang,Z.Y.
  TITLE     C2 domain-containing phosphoprotein CDP138 regulates GLUT4
            insertion into the plasma membrane
  JOURNAL   Cell Metab 14 (3), 378-389 (2011)
   PUBMED   21907143
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK310753.1, BC117143.1, AK295862.1, BP418369.1 and AY166851.1.
            
            On Oct 31, 2013 this sequence version replaced XP_005253591.1.
            
            Transcript Variant: This variant (3) lacks an exon, contains two
            alternate exons, and uses an alternate splice site, but maintains
            the reading frame, compared to variant 1. The encoded isoform (b)
            is longer than isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295862.1, SRR1803612.278393.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..1054
                     /product="C2 domain-containing protein 5 isoform b"
                     /note="138 kDa C2 domain-containing phosphoprotein; C2
                     domain-containing protein 5"
                     /calculated_mol_wt=116338
     Region          5..114
                     /region_name="C2_KIAA0528-like"
                     /note="C2 domain found in the Human KIAA0528 cDNA clone;
                     cd08688"
                     /db_xref="CDD:176070"
     CDS             1..1054
                     /gene="C2CD5"
                     /gene_synonym="CDP138; KIAA0528"
                     /coded_by="NM_001286175.2:253..3417"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS66339.1"
                     /db_xref="GeneID:9847"
                     /db_xref="HGNC:HGNC:29062"
                     /db_xref="MIM:618044"
ORIGIN      
        1 mpgklkvkiv agrhlpvmdr asdltdafve vkfgnttfkt dvylkslnpq wnsewfkfev
       61 ddedlqdepl qitvldhdty sandaigkvy ididpllyse aatvisgwfp iydtihgirg
      121 einvvvkvdl fndlnrfrqs scgvkffctt sipkcyravi ihgfveelvv nedpeyqwid
      181 rirtprasne arqrlislms gelqrkiglk vlemrgnavv gylqcfdleg esglvvraig
      241 tactldklss paaflpacns pskemkespl vhppshgcrs thnspihtat gsrltqnfsv
      301 svptliytgm gsgsagkegg pfkallrqqt qsaleqrefp fftltafppg flvhvggvvs
      361 arsvklldri hnpafvgimg ntrsyklldw nsfnsdepet rdawwaeirq eikshakalg
      421 chavvgyses tsiceevcil sasgtaavln prflqdgtve gcleqrleen lptrcgfchi
      481 pydelnmpfp ahltycyncr kqkvpdvlft tidlptdatv igkgcliqar lcrlkkkaqa
      541 eanataisnl lpfmeyevht qlmnklklkg mnalfglriq itvgenmlmg lasatgvyla
      601 alptpggiqi agktpndgsy eqhishmqkk indtiaknke lyeinppeis eeiigspipe
      661 prqrsrllrs qsessdevte ldlshgkkda fvleiddtda medvhslltd vpppsgfysc
      721 nteimpginn wtseiqmfts vrvirlssln ltnqalnknf ndlcenllks lyfklrsmip
      781 cclchvnftv slpedeliqv tvtavaitfd knqalqttkt pvekslqras tdneellqfp
      841 lelcsdslps hpfppakehl esassnsgip aaqrdrcssw ieliklkaqt irrgsikttm
      901 tvekaspvgd gnfrnrsapp canstvgvvk mtplsfipga kitkylgiin mffirettsl
      961 reeggvsgfl hafiaevfam vrahvaalgg navvsyimkq cvfmenpnkn qaqclinvsg
     1021 davvfvresd levvssqqpt tncqsscteg evtt
//
LOCUS       NP_001341855             143 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
            epsilon isoform isoform d [Homo sapiens].
ACCESSION   NP_001341855
VERSION     NP_001341855.1
DBSOURCE    REFSEQ: accession NM_001354926.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Wu,C.G., Balakrishnan,V.K., Merrill,R.A., Parihar,P.S.,
            Konovolov,K., Chen,Y.C., Xu,Z., Wei,H., Sundaresan,R., Cui,Q.,
            Wadzinski,B.E., Swingle,M.R., Musiyenko,A., Chung,W.K.,
            Honkanen,R.E., Suzuki,A., Huang,X., Strack,S. and Xing,Y.
  TITLE     B56delta long-disordered arms form a dynamic PP2A regulation
            interface coupled with global allostery and Jordan's syndrome
            mutations
  JOURNAL   Proc Natl Acad Sci U S A 121 (1), e2310727120 (2024)
   PUBMED   38150499
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Santos,A., Cristobal,I., Carames,C., Luque,M., Sanz-Alvarez,M.,
            Madoz-Gurpide,J., Rojo,F. and Garcia-Foncillas,J.
  TITLE     Deregulation of the miR-19b/PPP2R5E Signaling Axis Shows High
            Functional Impact in Colorectal Cancer Cells
  JOURNAL   Int J Mol Sci 24 (9), 7779 (2023)
   PUBMED   37175484
  REMARK    GeneRIF: Deregulation of the miR-19b/PPP2R5E Signaling Axis Shows
            High Functional Impact in Colorectal Cancer Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Virshup,D.M. and Shenolikar,S.
  TITLE     From promiscuity to precision: protein phosphatases get a makeover
  JOURNAL   Mol Cell 33 (5), 537-545 (2009)
   PUBMED   19285938
  REMARK    Review article
REFERENCE   5  (residues 1 to 143)
  AUTHORS   Eichhorn,P.J., Creyghton,M.P. and Bernards,R.
  TITLE     Protein phosphatase 2A regulatory subunits and cancer
  JOURNAL   Biochim Biophys Acta 1795 (1), 1-15 (2009)
   PUBMED   18588945
  REMARK    Review article
REFERENCE   6  (residues 1 to 143)
  AUTHORS   Tung,H.Y., De Rocquigny,H., Zhao,L.J., Cayla,X., Roques,B.P. and
            Ozon,R.
  TITLE     Direct activation of protein phosphatase-2A0 by HIV-1 encoded
            protein complex NCp7:vpr
  JOURNAL   FEBS Lett 401 (2-3), 197-201 (1997)
   PUBMED   9013886
REFERENCE   7  (residues 1 to 143)
  AUTHORS   McCright,B., Rivers,A.M., Audlin,S. and Virshup,D.M.
  TITLE     The B56 family of protein phosphatase 2A (PP2A) regulatory subunits
            encodes differentiation-induced phosphoproteins that target PP2A to
            both nucleus and cytoplasm
  JOURNAL   J Biol Chem 271 (36), 22081-22089 (1996)
   PUBMED   8703017
REFERENCE   8  (residues 1 to 143)
  AUTHORS   McCright,B., Brothman,A.R. and Virshup,D.M.
  TITLE     Assignment of human protein phosphatase 2A regulatory subunit genes
            b56alpha, b56beta, b56gamma, b56delta, and b56epsilon
            (PPP2R5A-PPP2R5E), highly expressed in muscle and brain, to
            chromosome regions 1q41, 11q12, 3p21, 6p21.1, and 7p11.2 --> p12
  JOURNAL   Genomics 36 (1), 168-170 (1996)
   PUBMED   8812429
REFERENCE   9  (residues 1 to 143)
  AUTHORS   Zolnierowicz,S., Van Hoof,C., Andjelkovic,N., Cron,P., Stevens,I.,
            Merlevede,W., Goris,J. and Hemmings,B.A.
  TITLE     The variable subunit associated with protein phosphatase 2A0
            defines a novel multimember family of regulatory subunits
  JOURNAL   Biochem J 317 (Pt 1) (Pt 1), 187-194 (1996)
   PUBMED   8694763
REFERENCE   10 (residues 1 to 143)
  AUTHORS   McCright,B. and Virshup,D.M.
  TITLE     Identification of a new family of protein phosphatase 2A regulatory
            subunits
  JOURNAL   J Biol Chem 270 (44), 26123-26128 (1995)
   PUBMED   7592815
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136038.5, BC056156.1 and
            AL132992.4.
            
            Summary: The protein encoded by this gene belongs to the
            phosphatase 2A regulatory subunit B family. Protein phosphatase 2A
            is one of the four major Ser/Thr phosphatases, and it is implicated
            in the negative control of cell growth and division. It consists of
            a common heteromeric core enzyme, which is composed of a catalytic
            subunit and a constant regulatory subunit, that associates with a
            variety of regulatory subunits. The B regulatory subunit might
            modulate substrate selectivity and catalytic activity. This gene
            encodes an epsilon isoform of the regulatory subunit B56 subfamily.
            Multiple transcript variants encoding several different isoforms
            have been found for this gene. [provided by RefSeq, Aug 2013].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC056156.1, SRR14038193.280707.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2142348,
                                           SAMEA2153733 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..143
                     /product="serine/threonine-protein phosphatase 2A 56 kDa
                     regulatory subunit epsilon isoform isoform d"
                     /note="PP2A, B subunit, B' epsilon; PP2A, B subunit, B56
                     epsilon; PP2A, B subunit, PR61 epsilon; PP2A, B subunit,
                     R5 epsilon; serine/threonine protein phosphatase 2A, 56
                     kDa regulatory subunit, epsilon; protein phosphatase 2
                     regulatory subunit B', epsilon"
                     /calculated_mol_wt=16304
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16537.1)"
     Region          2..>67
                     /region_name="B56"
                     /note="Protein phosphatase 2A regulatory B subunit (B56
                     family); cl27532"
                     /db_xref="CDD:474937"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q16537.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16537.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q16537.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q16537.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q16537.1)"
     Region          55..>120
                     /region_name="B56"
                     /note="Protein phosphatase 2A regulatory B subunit (B56
                     family); cl27532"
                     /db_xref="CDD:474937"
     CDS             1..143
                     /gene="PPP2R5E"
                     /gene_synonym="B56E; B56epsilon"
                     /coded_by="NM_001354926.2:607..1038"
                     /note="isoform d is encoded by transcript variant 7"
                     /db_xref="GeneID:5529"
                     /db_xref="HGNC:HGNC:9313"
                     /db_xref="MIM:601647"
ORIGIN      
        1 mssapttpps vdkvdgfsrk svrkarqkrs qsssqfrsqg kpieltplpl lkdvpsseqp
       61 elflkklqqc cvifdfmdtl sdlkmkeykr stlnelvdyi tisrgclteq typevvrmvs
      121 fffsprtlls ifhsdsqvyi lqe
//
LOCUS       NP_001304700             257 aa            linear   PRI 21-NOV-2025
DEFINITION  large ribosomal subunit protein uL2 [Homo sapiens].
ACCESSION   NP_001304700 XP_011515512
VERSION     NP_001304700.1
DBSOURCE    REFSEQ: accession NM_001317771.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Sun,T., Zhu,W., Ru,Q. and Zheng,Y.
  TITLE     Silencing RPL8 inhibits the progression of hepatocellular carcinoma
            by down-regulating the mTORC1 signalling pathway
  JOURNAL   Hum Cell 36 (2), 725-737 (2023)
   PUBMED   36577883
  REMARK    GeneRIF: Silencing RPL8 inhibits the progression of hepatocellular
            carcinoma by down-regulating the mTORC1 signalling pathway.
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Fan,S., Zhang,S., Kong,D., Wang,H., Shi,Y., Wang,Z. and Zheng,H.
  TITLE     Integrative Multi-Omics Analysis of Identified Ferroptosis-Marker
            RPL8 as a Candidate Oncogene Correlates with Poor Prognosis and
            Immune Infiltration in Liver Cancer
  JOURNAL   Comb Chem High Throughput Screen 26 (7), 1298-1310 (2023)
   PUBMED   36017842
  REMARK    GeneRIF: Integrative Multi-Omics Analysis of Identified
            Ferroptosis-Marker RPL8 as a Candidate Oncogene Correlates with
            Poor Prognosis and Immune Infiltration in Liver Cancer.
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   7  (residues 1 to 257)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   8  (residues 1 to 257)
  AUTHORS   Uhlein,M., Weglohner,W., Urlaub,H. and Wittmann-Liebold,B.
  TITLE     Functional implications of ribosomal protein L2 in protein
            biosynthesis as shown by in vivo replacement studies
  JOURNAL   Biochem J 331 (Pt 2) (Pt 2), 423-430 (1998)
   PUBMED   9531480
REFERENCE   9  (residues 1 to 257)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 257)
  AUTHORS   Hanes,J., Klaudiny,J., von der Kammer,H. and Scheit,K.H.
  TITLE     Characterization by cDNA cloning of the mRNA of human ribosomal
            protein L8
  JOURNAL   Biochem Biophys Res Commun 197 (3), 1223-1228 (1993)
   PUBMED   7506540
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF235103.5, CB128790.1,
            BQ929065.1 and BM783910.1.
            
            On Dec 9, 2015 this sequence version replaced XP_011515512.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L2P family of ribosomal proteins. It is located in the
            cytoplasm. In rat, the protein associates with the 5.8S rRNA, very
            likely participates in the binding of aminoacyl-tRNA, and is a
            constituent of the elongation factor 2-binding site at the
            ribosomal subunit interface. Alternatively spliced transcript
            variants encoding the same protein exist. As is typical for genes
            encoding ribosomal proteins, there are multiple processed
            pseudogenes of this gene dispersed through the genome. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1-4 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.427029.1,
                                           SRR1163658.221450.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..257
                     /product="large ribosomal subunit protein uL2"
                     /note="60S ribosomal protein L8"
                     /calculated_mol_wt=27894
     Region          1..254
                     /region_name="PTZ00180"
                     /note="60S ribosomal protein L8; Provisional"
                     /db_xref="CDD:173464"
     Region          207..232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62917.2)"
     Site            216
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyhistidine.
                     /evidence=ECO:0000269|PubMed:23103944; propagated from
                     UniProtKB/Swiss-Prot (P62917.2)"
     CDS             1..257
                     /gene="RPL8"
                     /gene_synonym="L8; uL2"
                     /coded_by="NM_001317771.2:137..910"
                     /db_xref="CCDS:CCDS6433.1"
                     /db_xref="GeneID:6132"
                     /db_xref="HGNC:HGNC:10368"
                     /db_xref="MIM:604177"
ORIGIN      
        1 mgrvirgqrk gagsvfrahv khrkgaarlr avdfaerhgy ikgivkdiih dpgrgaplak
       61 vvfrdpyrfk krtelfiaae gihtgqfvyc gkkaqlnign vlpvgtmpeg tivccleekp
      121 gdrgklaras gnyatvishn petkktrvkl psgskkviss anravvgvva gggridkpil
      181 kagrayhkyk akrncwprvr gvamnpvehp fgggnhqhig kpstirrdap agrkvgliaa
      241 rrtgrlrgtk tvqeken
//
LOCUS       NP_001296790             335 aa            linear   PRI 21-NOV-2025
DEFINITION  protein GNAS isoform h [Homo sapiens].
ACCESSION   NP_001296790
VERSION     NP_001296790.1
DBSOURCE    REFSEQ: accession NM_001309861.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lin,J., Nie,Q., Cheng,J., Zhong,Y.N., Zhang,T., Zhang,X., Ge,X.,
            Ding,Y., Niu,C., Gao,Y., Wang,K., Gao,M., Wang,X., Chen,W., Yun,C.,
            Ye,C., Xu,J., Shaoyong,W., Zhang,L., Shang,P., Luo,X., Zhang,Z.,
            Zheng,X., Sha,X., Zhang,J., Nie,S., Zhang,X., Ren,F., Liu,H.,
            Dong,E., Yu,X., Ji,L., Pang,Y., Sun,J.P. and Jiang,C.
  TITLE     A microbial amino-acid-conjugated bile acid, tryptophan-cholic
            acid, improves glucose homeostasis via the orphan receptor MRGPRE
  JOURNAL   Cell 188 (17), 4530-4548 (2025)
   PUBMED   40446798
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Crane,J.L., Shamblott,M.J., Axelman,J., Hsu,S., Levine,M.A. and
            Germain-Lee,E.L.
  TITLE     Imprinting status of Galpha(s), NESP55, and XLalphas in cell
            cultures derived from human embryonic germ cells: GNAS imprinting
            in human embryonic germ cells
  JOURNAL   Clin Transl Sci 2 (5), 355-360 (2009)
   PUBMED   20443919
  REMARK    GeneRIF: analysis of the imprinting Status of Galpha(s), NESP55,
            and XLalphas in cell cultures derived from human embryonic germ
            cells
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Bastepe,M.
  TITLE     The GNAS Locus: Quintessential Complex Gene Encoding Gsalpha,
            XLalphas, and other Imprinted Transcripts
  JOURNAL   Curr Genomics 8 (6), 398-414 (2007)
   PUBMED   19412439
  REMARK    GeneRIF: GNAS locus has a highly complex imprinted expression
            pattern, giving rise to transcripts (including non-coding) that are
            maternally, paternally, or biallelically expressed.
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Jakobsen,A.M., Ahlman,H., Kolby,L., Abrahamsson,J.,
            Fischer-Colbrie,R. and Nilsson,O.
  TITLE     NESP55, a novel chromogranin-like peptide, is expressed in
            endocrine tumours of the pancreas and adrenal medulla but not in
            ileal carcinoids
  JOURNAL   Br J Cancer 88 (11), 1746-1754 (2003)
   PUBMED   12771991
  REMARK    GeneRIF: Neuroendocrine secretory protein 55 is found in a subset
            of neuroendocrine tumours showing differentiation towards adrenal
            chromaffin cells and pancreatic islets cells and not in ileal
            carcinoids
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Freson,K., Jaeken,J., Van Helvoirt,M., de Zegher,F.,
            Wittevrongel,C., Thys,C., Hoylaerts,M.F., Vermylen,J. and Van
            Geet,C.
  TITLE     Functional polymorphisms in the paternally expressed XLalphas and
            its cofactor ALEX decrease their mutual interaction and enhance
            receptor-mediated cAMP formation
  JOURNAL   Hum Mol Genet 12 (10), 1121-1130 (2003)
   PUBMED   12719376
REFERENCE   6  (residues 1 to 335)
  AUTHORS   Weiss,U., Ischia,R., Eder,S., Lovisetti-Scamihorn,P., Bauer,R. and
            Fischer-Colbrie,R.
  TITLE     Neuroendocrine secretory protein 55 (NESP55): alternative splicing
            onto transcripts of the GNAS gene and posttranslational processing
            of a maternally expressed protein
  JOURNAL   Neuroendocrinology 71 (3), 177-186 (2000)
   PUBMED   10729789
REFERENCE   7  (residues 1 to 335)
  AUTHORS   Ischia,R., Lovisetti-Scamihorn,P., Hogue-Angeletti,R.,
            Wolkersdorfer,M., Winkler,H. and Fischer-Colbrie,R.
  TITLE     Molecular cloning and characterization of NESP55, a novel
            chromogranin-like precursor of a peptide with 5-HT1B receptor
            antagonist activity
  JOURNAL   J Biol Chem 272 (17), 11657-11662 (1997)
   PUBMED   9111083
REFERENCE   8  (residues 1 to 335)
  AUTHORS   Haldeman-Englert,C.R., Hurst,A.C.E. and Levine,M.A.
  TITLE     Disorders of GNAS Inactivation
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29072892
REFERENCE   9  (residues 1 to 335)
  AUTHORS   Szymczuk,V., Florenzano,P., de Castro,L.F., Collins,M.T. and
            Boyce,A.M.
  TITLE     Fibrous Dysplasia / McCune-Albright Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719192
REFERENCE   10 (residues 1 to 335)
  AUTHORS   Weinstein,L.S., Gejman,P.V., de Mazancourt,P., American,N. and
            Spiegel,A.M.
  TITLE     A heterozygous 4-bp deletion mutation in the Gs alpha gene (GNAS1)
            in a patient with Albright hereditary osteodystrophy
  JOURNAL   Genomics 13 (4), 1319-1321 (1992)
   PUBMED   1505964
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN273438.1, AK315874.1 and
            AF105253.1.
            
            Summary: This locus has a highly complex imprinted expression
            pattern. It gives rise to maternally, paternally, and biallelically
            expressed transcripts that are derived from four alternative
            promoters and 5' exons. Some transcripts contain a differentially
            methylated region (DMR) at their 5' exons, and this DMR is commonly
            found in imprinted genes and correlates with transcript expression.
            An antisense transcript is produced from an overlapping locus on
            the opposite strand. One of the transcripts produced from this
            locus, and the antisense transcript, are paternally expressed
            noncoding RNAs, and may regulate imprinting in this region. In
            addition, one of the transcripts contains a second overlapping ORF,
            which encodes a structurally unrelated protein - Alex. Alternative
            splicing of downstream exons is also observed, which results in
            different forms of the stimulatory G-protein alpha subunit, a key
            element of the classical signal transduction pathway linking
            receptor-ligand interactions with the activation of adenylyl
            cyclase and a variety of cellular reponses. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            Mutations in this gene result in pseudohypoparathyroidism type 1a,
            pseudohypoparathyroidism type 1b, Albright hereditary
            osteodystrophy, pseudopseudohypoparathyroidism, McCune-Albright
            syndrome, progressive osseus heteroplasia, polyostotic fibrous
            dysplasia of bone, and some pituitary tumors. [provided by RefSeq,
            Aug 2012].
            
            Transcript Variant: This variant (11) contains an alternate 5'
            terminal exon, compared to variant 1. Variants 9 and 11 encode the
            same isoform h (described in PMID:21713996), which has a shorter
            N-terminus, compared to isoform GNASL.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.169120.1,
                                           SRR5189667.214898.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 19412439
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.32"
     Protein         1..335
                     /product="protein GNAS isoform h"
                     /note="secretogranin VI; G protein subunit alpha S;
                     guanine nucleotide binding protein (G protein), alpha
                     stimulating activity polypeptide 1; guanine nucleotide
                     regulatory protein; adenylate cyclase-stimulating G alpha
                     protein; protein ALEX; extra large alphas protein;
                     alternative gene product encoded by XL-exon"
                     /calculated_mol_wt=38867
     Region          1..329
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Site            order(34,38,42,45,48..49,69,72,113,142,167,175,179)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Site            140..148
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            145
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(146,148,150,161,163,167..169,171,174..175,177..180)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(148,173,176..177,180)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            164..167
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            165..181
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Site            233..236
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(298..309,311..314)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Site            306..308
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..335
                     /gene="GNAS"
                     /gene_synonym="AHO; AIMAH1; C20orf45; GNAS1; GPSA; GSA;
                     GSP; NESP; PITA3; POH; SCG6; SgVI"
                     /coded_by="NM_001309861.2:295..1302"
                     /note="isoform h is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS93068.1"
                     /db_xref="GeneID:2778"
                     /db_xref="HGNC:HGNC:4392"
                     /db_xref="MIM:139320"
ORIGIN      
        1 mrilhvngfn geggeedpqa arsnsdgeka tkvqdiknnl keaietivaa msnlvppvel
       61 anpenqfrvd yilsvmnvpd fdfppefyeh akalwedegv racyersney qlidcaqyfl
      121 dkidvikqad yvpsdqdllr crvltsgife tkfqvdkvnf hmfdvggqrd errkwiqcfn
      181 dvtaiifvva sssynmvire dnqtnrlqea lnlfksiwnn rwlrtisvil flnkqdllae
      241 kvlagkskie dyfpefaryt tpedatpepg edprvtraky firdeflris tasgdgrhyc
      301 yphftcavdt enirrvfndc rdiiqrmhlr qyell
//
LOCUS       NP_001365070            1238 aa            linear   PRI 21-NOV-2025
DEFINITION  protocadherin Fat 3 isoform 3 precursor [Homo sapiens].
ACCESSION   NP_001365070
VERSION     NP_001365070.1
DBSOURCE    REFSEQ: accession NM_001378141.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1238)
  AUTHORS   Jiang,Z., Zhu,M., Zhang,L., Cui,H., Jiang,R. and Yang,Y.
  TITLE     Antitumor immunity and prognosis value elicited by FAT3 and LRP1B
            co-mutation in endometrial cancer
  JOURNAL   Gynecol Oncol 187, 1-11 (2024)
   PUBMED   38696842
  REMARK    GeneRIF: Antitumor immunity and prognosis value elicited by FAT3
            and LRP1B co-mutation in endometrial cancer.
REFERENCE   2  (residues 1 to 1238)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1238)
  AUTHORS   Nada,D., Julien,C., Papillon-Cavanagh,S., Majewski,J., Elbakry,M.,
            Elremaly,W., Samuels,M.E. and Moreau,A.
  TITLE     Identification of FAT3 as a new candidate gene for adolescent
            idiopathic scoliosis
  JOURNAL   Sci Rep 12 (1), 12298 (2022)
   PUBMED   35853984
  REMARK    GeneRIF: Identification of FAT3 as a new candidate gene for
            adolescent idiopathic scoliosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1238)
  AUTHORS   Jiang,H., Tian,Y., Zhao,X., Zhang,L. and Wu,Z.
  TITLE     A circular RNA derived from FAT atypical cadherin 3 promotes lung
            cancer progression via forming a regulatory loop with oncogenic
            ELAV like RNA binding protein 1
  JOURNAL   J Biochem 171 (5), 519-528 (2022)
   PUBMED   34647573
  REMARK    GeneRIF: A circular RNA derived from FAT atypical cadherin 3
            promotes lung cancer progression via forming a regulatory loop with
            oncogenic ELAV like RNA binding protein 1.
REFERENCE   5  (residues 1 to 1238)
  AUTHORS   Aviles,E.C., Krol,A., Henle,S.J., Burroughs-Garcia,J., Deans,M.R.
            and Goodrich,L.V.
  TITLE     Fat3 acts through independent cytoskeletal effectors to coordinate
            asymmetric cell behaviors during polarized circuit assembly
  JOURNAL   Cell Rep 38 (5), 110307 (2022)
   PUBMED   35108541
  REMARK    GeneRIF: Fat3 acts through independent cytoskeletal effectors to
            coordinate asymmetric cell behaviors during polarized circuit
            assembly.
REFERENCE   6  (residues 1 to 1238)
  AUTHORS   Zhu,M., Zhang,L., Cui,H., Zhao,Q., Wang,H., Zhai,B., Jiang,R. and
            Jiang,Z.
  TITLE     Co-Mutation of FAT3 and LRP1B in Lung Adenocarcinoma Defines a
            Unique Subset Correlated With the Efficacy of Immunotherapy
  JOURNAL   Front Immunol 12, 800951 (2022)
   PUBMED   35069585
  REMARK    GeneRIF: Co-Mutation of FAT3 and LRP1B in Lung Adenocarcinoma
            Defines a Unique Subset Correlated With the Efficacy of
            Immunotherapy.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1238)
  AUTHORS   Cheng,H., Burroughs-Garcia,J., Birkness,J.E., Trinidad,J.C. and
            Deans,M.R.
  TITLE     Disparate Regulatory Mechanisms Control Fat3 and P75NTR Protein
            Transport through a Conserved Kif5-Interaction Domain
  JOURNAL   PLoS One 11 (10), e0165519 (2016)
   PUBMED   27788242
  REMARK    GeneRIF: For Fat3, the Kif5-ID is regulated by alternative
            splicing, and the timecourse of splicing suggests that the
            distribution of Fat3 may switch between early and later stages of
            retinal development. In contrast, P75NTR binding to Kif5B is
            enhanced by tyrosine phosphorylation and thus has the potential to
            be dynamically regulated on a more rapid time scale
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1238)
  AUTHORS   Zheng,J.S., Arnett,D.K., Lee,Y.C., Shen,J., Parnell,L.D.,
            Smith,C.E., Richardson,K., Li,D., Borecki,I.B., Ordovas,J.M. and
            Lai,C.Q.
  TITLE     Genome-wide contribution of genotype by environment interaction to
            variation of diabetes-related traits
  JOURNAL   PLoS One 8 (10), e77442 (2013)
   PUBMED   24204828
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1238)
  AUTHORS   Wu,Q.
  TITLE     Comparative genomics and diversifying selection of the clustered
            vertebrate protocadherin genes
  JOURNAL   Genetics 169 (4), 2179-2188 (2005)
   PUBMED   15744052
REFERENCE   10 (residues 1 to 1238)
  AUTHORS   Mitsui,K., Nakajima,D., Ohara,O. and Nakayama,M.
  TITLE     Mammalian fat3: a large protein that contains multiple cadherin and
            EGF-like motifs
  JOURNAL   Biochem Biophys Res Commun 290 (4), 1260-1266 (2002)
   PUBMED   11811999
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP003124.3, AP000722.5, AP000805.4 and AP002514.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.26704.1,
                                           SRR14372080.4501200.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA2142853 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1238
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.3"
     Protein         1..1238
                     /product="protocadherin Fat 3 isoform 3 precursor"
                     /note="cadherin-related family member 10; protocadherin
                     Fat 3; cadherin family member 15; FAT tumor suppressor
                     homolog 3"
                     /calculated_mol_wt=133904
     sig_peptide     1..32
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3415
     Region          47..153
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            49
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDW7.3)"
     Site            order(54..55,118,120,150,152..153)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          162..262
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(169..170,220,222,258,260..261)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          286..>357
                     /region_name="CA_like"
                     /note="Cadherin repeat-like domain; cl46864"
                     /db_xref="CDD:481204"
     Site            342
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDW7.3)"
     Region          380..468
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(387..388,436,438,464,466..467)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          477..574
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            482
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDW7.3)"
     Site            order(483..484,535,537,570,572..573)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            563
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDW7.3)"
     Region          592..672
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            668
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDW7.3)"
     Region          733..827
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(737..738,790,792,823,825..826)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            800
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDW7.3)"
     Region          835..931
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(842..843,893,895,928,930..931)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            880
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDW7.3)"
     Site            899
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDW7.3)"
     Region          940..1018
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            1007
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TDW7.3)"
     Region          1049..1144
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(1054..1055,1107,1109,1140,1142..1143)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          1152..>1204
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     CDS             1..1238
                     /gene="FAT3"
                     /gene_synonym="CDHF15; CDHR10; hFat3"
                     /coded_by="NM_001378141.1:375..4091"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:120114"
                     /db_xref="HGNC:HGNC:23112"
                     /db_xref="MIM:612483"
ORIGIN      
        1 mdiimghcvg trppacclil llfkllatvs qglpgtgplg fhfthsiyna tvyensaart
       61 yvnsqsrmgi tlidlswdik yrivsgdeeg ffkaeeviia dfcflrirtk ggnsailnre
      121 iqdnyllivk gsvrgedlea wtkvniqvld mndlrplfsp ttysvtiaes tplrtsvaqv
      181 tatdadigsn gefyyyfknk vdlfsvhpts gvislsgrln ydeknrydle ilavdrgmkl
      241 ygnngvssta klyvhierin ehaptihvvt hvpfslekep tyavvtvddl ddgangeies
      301 vsivagdpld qfflakegkw lneykikerk qidwesfpyg ynltlqakdk gspqkcsalk
      361 avyignptrd tvpirfekev ydvsisefsp pgvvvaivkl spepidveyk lspgedavyf
      421 kinprsgliv tarplntvkk evyklevtnk egdlkaqvti siedandhtp efqqplyday
      481 vnesvpvgts vltvsasdkd kgengyitys iaslnllpfv inqftgvist teeldfessp
      541 eiyrfivras dwgspyrhes evnvtirign vndnsplfek vacqgvisyd fpvgghitav
      601 saididelel vkykiisgne lgffylnpds gvlqlkkslt nsgikngnfa lritatdgen
      661 ladpmsinis vlhgkvssks fscretrvaq klaekllika kangklnled gfldfysinr
      721 qgpyfdksfp sdvavkedlp vganilkika ydadsgfngk vlftisdgnt dscfnidmet
      781 gqlkvlmpmd rehtdlylln itiydlgnpq ksswrlltin vedandnspv fiqdsysvni
      841 lessgigtei iqveardkdl gsngevtysv ltdtqqfain sstgivyvad qldreskany
      901 slkieardka esgqqlfsvv tlkvflddvn dcspafipss ysvkvledlp vgtviawlet
      961 hdpdlglggq vryslvndyn grfeidkasg airlskeldy ekqqfynltv rakdkgrpvs
     1021 lssvsfveve vvdvnenlht pyfpdfavvg svkensrigt svlqvtarde dsgrdgeiqy
     1081 sirdgsglgr fsiddesgvi taadildret mgsywltvya tdrgvvplys tievyieved
     1141 vndnapltse piyypvvmen spkdvsviqi qaedpdsssn ekltyritsg npqnffaini
     1201 ktgwkslgil ksrsqqiwcl egalfldcre lsfcyvlt
//
LOCUS       NP_001371278             298 aa            linear   PRI 21-NOV-2025
DEFINITION  dual oxidase maturation factor 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001371278 XP_006720818
VERSION     NP_001371278.1
DBSOURCE    REFSEQ: accession NM_001384349.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Kohda,A., Kamakura,S., Hayase,J. and Sumimoto,H.
  TITLE     The NADPH oxidases DUOX1 and DUOX2 are sorted to the apical plasma
            membrane in epithelial cells via their respective maturation
            factors DUOXA1 and DUOXA2
  JOURNAL   Genes Cells 29 (10), 921-930 (2024)
   PUBMED   39126279
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Wu,J.X., Liu,R., Song,K. and Chen,L.
  TITLE     Structures of human dual oxidase 1 complex in low-calcium and
            high-calcium states
  JOURNAL   Nat Commun 12 (1), 155 (2021)
   PUBMED   33420071
  REMARK    GeneRIF: Structures of human dual oxidase 1 complex in low-calcium
            and high-calcium states.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Meng,Y., Chen,C.W., Yung,M.M.H., Sun,W., Sun,J., Li,Z., Li,J.,
            Li,Z., Zhou,W., Liu,S.S., Cheung,A.N.Y., Ngan,H.Y.S.,
            Braisted,J.C., Kai,Y., Peng,W., Tzatsos,A., Li,Y., Dai,Z.,
            Zheng,W., Chan,D.W. and Zhu,W.
  TITLE     DUOXA1-mediated ROS production promotes cisplatin resistance by
            activating ATR-Chk1 pathway in ovarian cancer
  JOURNAL   Cancer Lett 428, 104-116 (2018)
   PUBMED   29704517
  REMARK    GeneRIF: Study shows that DUOXA1 is overexpressed in
            platinum-resistant ovarian cancer (OC) cells, resulting in over
            production of reactive oxygen species (ROS). Elevated ROS level
            sustains the activation of ATR-Chk1 pathway, leading to resistance
            to cisplatin in OC cells. Clinical studies also confirm the
            activation of ATR and DOUXA1 in OC patients, and elevated DOUXA1 or
            ATR-Chk1 pathway correlates with poor prognosis.
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Ostrakhovitch,E.A. and Semenikhin,O.A.
  TITLE     p53-mediated regulation of neuronal differentiation via regulation
            of dual oxidase maturation factor 1
  JOURNAL   Neurosci Lett 494 (1), 80-85 (2011)
   PUBMED   21362455
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Christophe-Hobertus,C. and Christophe,D.
  TITLE     Delimitation and functional characterization of the bidirectional
            THOX-DUOXA promoter regions in thyrocytes
  JOURNAL   Mol Cell Endocrinol 317 (1-2), 161-167 (2010)
   PUBMED   20060878
REFERENCE   6  (residues 1 to 298)
  AUTHORS   Ostrakhovitch,E.A. and Li,S.S.
  TITLE     NIP1/DUOXA1 expression in epithelial breast cancer cells:
            regulation of cell adhesion and actin dynamics
  JOURNAL   Breast Cancer Res Treat 119 (3), 773-786 (2010)
   PUBMED   19322654
  REMARK    GeneRIF: DUOXA1 transient overexpression affected the cell-cell
            adhesion by modulating the actin cytoskeleton
REFERENCE   7  (residues 1 to 298)
  AUTHORS   Luxen,S., Noack,D., Frausto,M., Davanture,S., Torbett,B.E. and
            Knaus,U.G.
  TITLE     Heterodimerization controls localization of Duox-DuoxA NADPH
            oxidases in airway cells
  JOURNAL   J Cell Sci 122 (Pt 8), 1238-1247 (2009)
   PUBMED   19339556
  REMARK    GeneRIF: Heterodimerization controls localization of Duox-DuoxA
            NADPH oxidases in airway cells.
REFERENCE   8  (residues 1 to 298)
  AUTHORS   Morand,S., Ueyama,T., Tsujibe,S., Saito,N., Korzeniowska,A. and
            Leto,T.L.
  TITLE     Duox maturation factors form cell surface complexes with Duox
            affecting the specificity of reactive oxygen species generation
  JOURNAL   FASEB J 23 (4), 1205-1218 (2009)
   PUBMED   19074510
REFERENCE   9  (residues 1 to 298)
  AUTHORS   Grasberger,H. and Refetoff,S.
  TITLE     Identification of the maturation factor for dual oxidase. Evolution
            of an eukaryotic operon equivalent
  JOURNAL   J Biol Chem 281 (27), 18269-18272 (2006)
   PUBMED   16651268
REFERENCE   10 (residues 1 to 298)
  AUTHORS   Qin,H., Percival-Smith,A., Li,C., Jia,C.Y., Gloor,G. and Li,S.S.
  TITLE     A novel transmembrane protein recruits numb to the plasma membrane
            during asymmetric cell division
  JOURNAL   J Biol Chem 279 (12), 11304-11312 (2004)
   PUBMED   14670962
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091117.5.
            
            On Jun 16, 2020 this sequence version replaced XP_006720818.1.
            
            Summary: Dual oxidases DUOX1 and DUOX2 are NADPH oxidases which are
            involved in hydrogen peroxide production necessary for thyroid
            hormonogenesis. They form a heterodimer with specific maturation
            factors DUOXA1 and DUOXA2, respectively, which is essential for the
            maturation and function of the DUOX enzyme complexes. This gene
            encodes the DUOX1 activator or maturation factor DUOXA1. Rat
            studies identified a bidirectional promoter which controls the
            transcription of the DUOX1 and DUOXA1 genes. This protein is
            cotransported to the cell surface when coexpressed with DUOX1 and
            is retained in the endoplasmic reticulum when expressed without
            DUOX1 protein. The expression of this gene or the DUOX1 gene is not
            suppressed by thyroglobulin (Tg), a macromolecular precursor in
            thyroid hormone synthesis, while the expression of the DUOX2 and
            DUOXA2 are significantly suppressed by the Tg. This protein is also
            a p53-regulated neurogenic factor involved in p53 dependent
            neuronal differentiation. Multiple alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: EU927395.1, SRR1660809.263750.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2144120, SAMEA2144333 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.1"
     Protein         1..298
                     /product="dual oxidase maturation factor 1 isoform 4"
                     /note="homolog of Drosophila Numb-interacting protein;
                     dual oxidase activator 1; dual oxidase maturation factor 1
                     gamma; dual oxidase maturation factor 1 delta; dual
                     oxidase maturation factor 1 alpha; dual oxidase maturation
                     factor 1 beta"
                     /calculated_mol_wt=32980
     Region          10..242
                     /region_name="DuoxA"
                     /note="Dual oxidase maturation factor; pfam10204"
                     /db_xref="CDD:462995"
     CDS             1..298
                     /gene="DUOXA1"
                     /gene_synonym="mol; NIP; NUMBIP"
                     /coded_by="NM_001384349.1:331..1227"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS61619.1"
                     /db_xref="GeneID:90527"
                     /db_xref="HGNC:HGNC:26507"
                     /db_xref="MIM:612771"
ORIGIN      
        1 matlghtfpf yagpkptfpm dttlasiimi fltalatfiv ilpgirgktr lfwllrvvts
       61 lfigaailgt pvqqlnetin yneeftwrlg enyaeeyaka lekglpdpvl ylaekftprs
      121 pcglyrqyrl aghytsamlw vaflcwllan vmlsmpvlvy ggymllatgi fqllallffs
      181 matsltspcp lhlgasvlht hhgpafwitl ttgllcvllg lamavahrmq phrlkaffnq
      241 svdedpmlew speeggllsp ryrsmadspk sqdiplseas stkayckeah pkdpdcal
//
LOCUS       NP_001335424            1358 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 2 isoform p [Homo
            sapiens].
ACCESSION   NP_001335424
VERSION     NP_001335424.1
DBSOURCE    REFSEQ: accession NM_001348495.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1358)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1358)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   3  (residues 1 to 1358)
  AUTHORS   Mechaussier,S., Almoallem,B., Zeitz,C., Van Schil,K., Jeddawi,L.,
            Van Dorpe,J., Duenas Rey,A., Condroyer,C., Pelle,O., Polak,M.,
            Boddaert,N., Bahi-Buisson,N., Cavallin,M., Bacquet,J.L.,
            Mouallem-Beziere,A., Zambrowski,O., Sahel,J.A., Audo,I., Kaplan,J.,
            Rozet,J.M., De Baere,E. and Perrault,I.
  TITLE     Loss of Function of RIMS2 Causes a Syndromic Congenital Cone-Rod
            Synaptic Disease with Neurodevelopmental and Pancreatic Involvement
  JOURNAL   Am J Hum Genet 106 (6), 859-871 (2020)
   PUBMED   32470375
  REMARK    GeneRIF: Loss of Function of RIMS2 Causes a Syndromic Congenital
            Cone-Rod Synaptic Disease with Neurodevelopmental and Pancreatic
            Involvement.
            Erratum:[Am J Hum Genet. 2020 Sep 3;107(3):580. doi:
            10.1016/j.ajhg.2020.08.004. PMID: 32888510]
REFERENCE   4  (residues 1 to 1358)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 1358)
  AUTHORS   Kim,K.T., Lee,J.S., Lee,B.W., Seok,H., Jeon,H.S., Kim,J.H. and
            Chung,J.H.
  TITLE     Association between regulating synaptic membrane exocytosis 2 gene
            polymorphisms and degenerative lumbar scoliosis
  JOURNAL   Biomed Rep 1 (4), 619-623 (2013)
   PUBMED   24648997
REFERENCE   6  (residues 1 to 1358)
  AUTHORS   Sun,L., Bittner,M.A. and Holz,R.W.
  TITLE     Rim, a component of the presynaptic active zone and modulator of
            exocytosis, binds 14-3-3 through its N terminus
  JOURNAL   J Biol Chem 278 (40), 38301-38309 (2003)
   PUBMED   12871946
REFERENCE   7  (residues 1 to 1358)
  AUTHORS   Fukuda,M.
  TITLE     Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and
            Noc2. Identification of a critical determinant of Rab3A/Rab27A
            recognition by Rim2
  JOURNAL   J Biol Chem 278 (17), 15373-15380 (2003)
   PUBMED   12578829
REFERENCE   8  (residues 1 to 1358)
  AUTHORS   Wang,Y. and Sudhof,T.C.
  TITLE     Genomic definition of RIM proteins: evolutionary amplification of a
            family of synaptic regulatory proteins
  JOURNAL   Genomics 81 (2), 126-137 (2003)
   PUBMED   12620390
REFERENCE   9  (residues 1 to 1358)
  AUTHORS   Kashima,Y., Miki,T., Shibasaki,T., Ozaki,N., Miyazaki,M., Yano,H.
            and Seino,S.
  TITLE     Critical role of cAMP-GEFII--Rim2 complex in incretin-potentiated
            insulin secretion
  JOURNAL   J Biol Chem 276 (49), 46046-46053 (2001)
   PUBMED   11598134
REFERENCE   10 (residues 1 to 1358)
  AUTHORS   Fenster,S.D., Chung,W.J., Zhai,R., Cases-Langhoff,C., Voss,B.,
            Garner,A.M., Kaempf,U., Kindler,S., Gundelfinger,E.D. and
            Garner,C.C.
  TITLE     Piccolo, a presynaptic zinc finger protein structurally related to
            bassoon
  JOURNAL   Neuron 25 (1), 203-214 (2000)
   PUBMED   10707984
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012213.8, AC090686.4,
            AP001572.3, AC107933.6 and AP002849.2.
            
            Summary: The protein encoded by this gene is a presynaptic protein
            that interacts with RAB3, a protein important for normal
            neurotransmitter release. The encoded protein can also bind several
            other synaptic proteins, including UNC-13 homolog B,
            ELKS/Rab6-interacting/CAST family member 1, and synaptotagmin 1.
            This protein is involved in synaptic membrane exocytosis.
            Polymorphisms in this gene have been associated with degenerative
            lumbar scoliosis. [provided by RefSeq, Feb 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.205073.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1358
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..1358
                     /product="regulating synaptic membrane exocytosis protein
                     2 isoform p"
                     /note="RAB3 interacting protein 3; regulating synaptic
                     membrane exocytosis protein 2; nuclear protein; non-small
                     cell lung cancer RimL3a protein; non-small cell lung
                     cancer RimL3c protein; rab3-interacting molecule 2;
                     rab-3-interacting protein 3; rab-3-interacting molecule 2;
                     Rab3-interacting protein"
                     /calculated_mol_wt=154224
     Region          30..154
                     /region_name="PHD_SF"
                     /note="PHD finger superfamily; cl22851"
                     /db_xref="CDD:473978"
     Region          590..689
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(614..620,635,638,668,672,675..676)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          741..867
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(772,778,833,835,843)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          1189..1334
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(1246,1250..1251,1253,1256,1284,1286,1288,1332..1333)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..1358
                     /gene="RIMS2"
                     /gene_synonym="CRSDS; OBOE; RAB3IP3; RIM2"
                     /coded_by="NM_001348495.2:278..4354"
                     /note="isoform p is encoded by transcript variant 16"
                     /db_xref="GeneID:9699"
                     /db_xref="HGNC:HGNC:17283"
                     /db_xref="MIM:606630"
ORIGIN      
        1 msapvgprgr lapipaasqp plqpempdls hlteeerkii lavmdrqkke eekeqsvlkk
       61 lhqqfemyke qvkkmgeesq qqqeqkgdap tcgichktkf adgcghncsy cqtkfcarcg
      121 grvslrsnkv mwvcnlcrkq qeiltksgaw fynsgsntpq qpdqkvlrgl rneeapqekk
      181 pklheqtqfq gpsgdlsvpa veksrshglt rqhsikngsg vkhhiasdia sdrktssell
      241 nskiisrkrs psvsrdqnrr ydqreereey sqyatsdtam prspsdyadr rsqhepqfye
      301 dsdhlsyrds nrrshrhske yivddedves rdeyerqrre eeyqsryrsd pnlarypvkp
      361 qpyeeqmrih aevsrarher rhsdvslana dledsrisml rmdrpsrqrs iserraamen
      421 qrsysmertr eaqgpssyaq rttnhspptp rrsplpidrp dlrrtdslrk qhhldpssav
      481 rktkrekmet mlrndslssd qsesvrpppp kphkskkggk mrqislssse eelastpeyt
      541 scddveiese svsekgdmdy nwldhtswhs seaspmslhp vtwqpskdgd rligrillnk
      601 rlkdgsvprd sgamlglkvv ggkmtesgrl cafitkvkkg sladtvghlr pgdevlewng
      661 rllqgatfee vyniileskp epqvelvvsr pigdipripd sthaqlesss ssfesqkmdr
      721 psisvtspms pgmlrdvpqf lsgqlsiklw fdkvghqliv tilgakdlps redgrprnpy
      781 vkiyflpdrs dknkrrtktv kktlepkwnq tfiyspvhrr efrermleit lwdqarvree
      841 eseflgeili eletalldde phwyklqthd vsslplphps pymprrqlhg esptrrlqrs
      901 krisdsevsd ydcddgigvv sdyrhdgrdl qsstlsvpeq vmssnhcsps gsphrvdvig
      961 rtrswspsvp ppqsrnveqg lrgtrtmtgh yntisrmdrh rvmddhyspd rdrdceaadr
     1021 qpyhrsrste qrpllerttt rsrsterpdt nlmrsmpslm tgrsappspa lsrshprtgs
     1081 vqtspsstpv agrrgrqlpq lppkgtldrn ngvkeiepye eaggkklrst vqrstetgla
     1141 vemrnwmtrq asrestdgsm nsyssegnli fpgvrlasds qfsdfldglg paqlvgrqtl
     1201 atpamgdiqv gmmdkkgqle veiirarglv vkpgsktlpa pyvkvylldn gvciakkktk
     1261 varktleply qqllsfeesp qgkvlqiivw gdygrmdhks fmgvaqilld elelsnmvig
     1321 wfklfppssl vdptlapltr rasqssless tgpsysrs
//
LOCUS       NP_001337875             260 aa            linear   PRI 21-NOV-2025
DEFINITION  actin-related protein 3B isoform 6 [Homo sapiens].
ACCESSION   NP_001337875 XP_016867953
VERSION     NP_001337875.1
DBSOURCE    REFSEQ: accession NM_001350946.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Abella,J.V., Galloni,C., Pernier,J., Barry,D.J., Kjaer,S.,
            Carlier,M.F. and Way,M.
  TITLE     Isoform diversity in the Arp2/3 complex determines actin filament
            dynamics
  JOURNAL   Nat Cell Biol 18 (1), 76-86 (2016)
   PUBMED   26655834
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Shin,J.H., Gulesserian,T., Weitzdoerfer,R., Fountoulakis,M. and
            Lubec,G.
  TITLE     Derangement of hypothetical proteins in fetal Down's syndrome brain
  JOURNAL   Neurochem Res 29 (6), 1307-1316 (2004)
   PUBMED   15176487
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Shindo-Okada,N. and Iigo,M.
  TITLE     Expression of the Arp11 gene suppresses the tumorigenicity of PC-14
            human lung adenocarcinoma cells
  JOURNAL   Biochem Biophys Res Commun 312 (4), 889-896 (2003)
   PUBMED   14651955
  REMARK    GeneRIF: Thus, overexpression of Arp11 may suppress tumorigenicity
            in nude mice.
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Eckley,D.M. and Schroer,T.A.
  TITLE     Interactions between the evolutionarily conserved, actin-related
            protein, Arp11, actin, and Arp1
  JOURNAL   Mol Biol Cell 14 (7), 2645-2654 (2003)
   PUBMED   12857853
REFERENCE   8  (residues 1 to 260)
  AUTHORS   Shindo-Okada,N. and Shimizu,K.
  TITLE     Isolation of a novel actin-related gene expressed in low-metastatic
            PC-14 human lung adenocarcinoma
  JOURNAL   Biochem Biophys Res Commun 280 (1), 61-67 (2001)
   PUBMED   11162478
REFERENCE   9  (residues 1 to 260)
  AUTHORS   Jay,P., Berge-Lefranc,J.L., Massacrier,A., Roessler,E., Wallis,D.,
            Muenke,M., Gastaldi,M., Taviaux,S., Cau,P. and Berta,P.
  TITLE     ARP3beta, the gene encoding a new human actin-related protein, is
            alternatively spliced and predominantly expressed in brain neuronal
            cells
  JOURNAL   Eur J Biochem 267 (10), 2921-2928 (2000)
   PUBMED   10806390
REFERENCE   10 (residues 1 to 260)
  AUTHORS   Machesky,L.M. and Gould,K.L.
  TITLE     The Arp2/3 complex: a multifunctional actin organizer
  JOURNAL   Curr Opin Cell Biol 11 (1), 117-121 (1999)
   PUBMED   10047519
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092180.5 and AC072057.8.
            
            On Apr 27, 2017 this sequence version replaced XP_016867953.1.
            
            Summary: This gene encodes a member of the actin-related proteins
            (ARP), which form multiprotein complexes and share 35-55% amino
            acid identity with conventional actin. The protein encoded by this
            gene may have a regulatory role in the actin cytoskeleton and
            induce cell-shape change and motility. Pseudogenes of this gene are
            located on chromosomes 2, 4, 10, 16, 22 and Y. Alternative splicing
            results in multiple transcript variants and protein isoforms.
            [provided by RefSeq, Jul 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.536207.1,
                                           SRR14038193.3542673.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1-q36.2"
     Protein         1..260
                     /product="actin-related protein 3B isoform 6"
                     /note="actin-related protein 3-beta; actin-related protein
                     Arp11; ARP3-beta; actin-like protein 3B; actin-related
                     protein ARP4; ARP3 actin related protein 3 homolog B"
                     /calculated_mol_wt=29858
     Region          <1..252
                     /region_name="ASKHA_ATPase-like"
                     /note="ATPase-like domain of the ASKHA (Acetate and Sugar
                     Kinases/Hsc70/Actin) superfamily; cl49607"
                     /db_xref="CDD:483947"
     CDS             1..260
                     /gene="ACTR3B"
                     /gene_synonym="ARP11; ARP3BETA"
                     /coded_by="NM_001350946.2:340..1122"
                     /note="isoform 6 is encoded by transcript variant 9"
                     /db_xref="GeneID:57180"
                     /db_xref="HGNC:HGNC:17256"
ORIGIN      
        1 merfmeqvvf kylraepedh yflmteppln tpenreylae imfesfnvpg lyiavqavla
       61 laaswtsrqv gertltgivi dsgdgvthvi pvaegyvigs cikhipiagr dityfiqqll
      121 rerevgippe qsletakaik ekycyicpdi vkefakydvd prkwikqytg inainqkkfv
      181 idvgyerflg peiffhpefa npdfmesisd vvdeviqncp idvrrplykp effqvchtkk
      241 dyeeygpsic rhnpvfgvms
//
LOCUS       NP_689735                226 aa            linear   PRI 21-NOV-2025
DEFINITION  ADP-ribosylation factor-like protein 6-interacting protein 6
            isoform a [Homo sapiens].
ACCESSION   NP_689735
VERSION     NP_689735.1
DBSOURCE    REFSEQ: accession NM_152522.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Abumansour,I.S., Hijazi,H., Alazmi,A., Alzahrani,F., Bashiri,F.A.,
            Hassan,H., Alhaddab,M. and Alkuraya,F.S.
  TITLE     ARL6IP6, a susceptibility locus for ischemic stroke, is mutated in
            a patient with syndromic Cutis Marmorata Telangiectatica Congenita
  JOURNAL   Hum Genet 134 (8), 815-822 (2015)
   PUBMED   25957586
  REMARK    GeneRIF: ARL6IP6 as a novel candidate gene for a syndromic form of
            CMTC.
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Ingley,E., Williams,J.H., Walker,C.E., Tsai,S., Colley,S.,
            Sayer,M.S., Tilbrook,P.A., Sarna,M., Beaumont,J.G. and Klinken,S.P.
  TITLE     A novel ADP-ribosylation like factor (ARL-6), interacts with the
            protein-conducting channel SEC61beta subunit
  JOURNAL   FEBS Lett 459 (1), 69-74 (1999)
   PUBMED   10508919
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079344.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.2706632.1,
                                           SRR18074969.1592613.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326446.10/ ENSP00000315357.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q23.3"
     Protein         1..226
                     /product="ADP-ribosylation factor-like protein
                     6-interacting protein 6 isoform a"
                     /note="ADP-ribosylation factor-like protein 6-interacting
                     protein 6; regulated by phosphonoformate; phosphonoformate
                     immuno-associated protein 1; ARL-6-interacting protein 6;
                     ADP-ribosylation-like factor 6 interacting protein 6;
                     ADP-ribosylation factor GTPase 6 interacting protein 6;
                     ADP-ribosylation factor-like 6 interacting protein 6; ADP
                     ribosylation factor like GTPase 6 interacting protein 6"
                     /calculated_mol_wt=24545
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6S5.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q8N6S5.1)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q8N6S5.1)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N6S5.1)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N6S5.1)"
     Region          66..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6S5.1)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N6S5.1)"
     Site            111..131
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6S5.1)"
     Region          138..214
                     /region_name="ARL6IP6"
                     /note="Haemopoietic lineage transmembrane helix;
                     pfam15062"
                     /db_xref="CDD:405709"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6S5.1)"
     Site            205..225
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6S5.1)"
     CDS             1..226
                     /gene="ARL6IP6"
                     /gene_synonym="AIP-6; AIP6; PFAAP1"
                     /coded_by="NM_152522.7:6..686"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2197.1"
                     /db_xref="GeneID:151188"
                     /db_xref="HGNC:HGNC:24048"
                     /db_xref="MIM:616495"
ORIGIN      
        1 msfaesgwrs alrrrgpgtp gpvarpsyss ftqgdswgeg evdeeegcdq vardlraefs
       61 agawseprkr svlppdgngs pvlpdkrngi fpaaagsraq prrwpvqvls ilcsllfail
      121 lafllaiayl ivkelhaenl kneddvdtgl lgfwtlliis ltagfsccsf swtvtyfdsf
      181 epgmfpptpl sparfkkltg hsfhmgysma ilngivaalt vawclm
//
LOCUS       NP_000593                402 aa            linear   PRI 21-NOV-2025
DEFINITION  plasminogen activator inhibitor 1 isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_000593
VERSION     NP_000593.1
DBSOURCE    REFSEQ: accession NM_000602.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Doelker,T., Gallwas,J. and Grundker,C.
  TITLE     Suppressing Expression of SERPINE1/PAI1 Through Activation of GPER1
            Reduces Progression of Vulvar Carcinoma
  JOURNAL   Cancer Genomics Proteomics 21 (6), 566-579 (2024)
   PUBMED   39467628
  REMARK    GeneRIF: Suppressing Expression of SERPINE1/PAI1 Through Activation
            of GPER1 Reduces Progression of Vulvar Carcinoma.
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Khoukaz,H.B., Vadali,M., Schoenherr,A., Ramirez-Perez,F.I.,
            Morales-Quinones,M., Sun,Z., Fujie,S., Foote,C.A., Lyu,Z., Zeng,S.,
            Augenreich,M.A., Cai,D., Chen,S.Y., Joshi,T., Ji,Y., Hill,M.A.,
            Martinez-Lemus,L.A. and Fay,W.P.
  TITLE     PAI-1 Regulates the Cytoskeleton and Intrinsic Stiffness of
            Vascular Smooth Muscle Cells
  JOURNAL   Arterioscler Thromb Vasc Biol 44 (10), 2191-2203 (2024)
   PUBMED   38868940
  REMARK    GeneRIF: PAI-1 Regulates the Cytoskeleton and Intrinsic Stiffness
            of Vascular Smooth Muscle Cells.
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Guo,X., Zhou,H., Liu,Y., Xu,W., Kanwore,K. and Zhang,L.
  TITLE     Glial-Cell-Line-Derived Neurotrophic Factor Promotes Glioblastoma
            Cell Migration and Invasion via the SMAD2/3-SERPINE1-Signaling Axis
  JOURNAL   Int J Mol Sci 25 (18), 10229 (2024)
   PUBMED   39337713
  REMARK    GeneRIF: Glial-Cell-Line-Derived Neurotrophic Factor Promotes
            Glioblastoma Cell Migration and Invasion via the
            SMAD2/3-SERPINE1-Signaling Axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Yatsenko,T., Rios,R., Nogueira,T., Salama,Y., Takahashi,S.,
            Adachi,E., Tabe,Y., Hattori,N., Osada,T., Naito,T., Takahashi,K.,
            Hattori,K. and Heissig,B.
  TITLE     The influence of 4G/5G polymorphism in the
            plasminogen-activator-inhibitor-1 promoter on COVID-19 severity and
            endothelial dysfunction
  JOURNAL   Front Immunol 15, 1445294 (2024)
   PUBMED   39281671
  REMARK    GeneRIF: The influence of 4G/5G polymorphism in the
            plasminogen-activator-inhibitor-1 promoter on COVID-19 severity and
            endothelial dysfunction.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Heiman,M., Gupta,S., Lewandowska,M. and Shapiro,A.D.
  TITLE     Complete Plasminogen Activator Inhibitor 1 Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   28771291
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Fay,W.P., Shapiro,A.D., Shih,J.L., Schleef,R.R. and Ginsburg,D.
  TITLE     Brief report: complete deficiency of plasminogen-activator
            inhibitor type 1 due to a frame-shift mutation
  JOURNAL   N Engl J Med 327 (24), 1729-1733 (1992)
   PUBMED   1435917
REFERENCE   8  (residues 1 to 402)
  AUTHORS   Koh,S.C., Wong,P.C., Yuen,R., Chua,S.E., Ng,B.L. and Ratnam,S.S.
  TITLE     Concentration of plasminogen activators and inhibitor in the human
            endometrium at different phases of the menstrual cycle
  JOURNAL   J Reprod Fertil 96 (2), 407-413 (1992)
   PUBMED   1339823
REFERENCE   9  (residues 1 to 402)
  AUTHORS   Hagege,J., Peraldi,M.N., Rondeau,E., Adida,C., Delarue,F.,
            Medcalf,R., Schleuning,W.D. and Sraer,J.D.
  TITLE     Plasminogen activator inhibitor-1 deposition in the extracellular
            matrix of cultured human mesangial cells
  JOURNAL   Am J Pathol 141 (1), 117-128 (1992)
   PUBMED   1632457
REFERENCE   10 (residues 1 to 402)
  AUTHORS   Ehrlich,H.J., Gebbink,R.K., Keijer,J., Linders,M., Preissner,K.T.
            and Pannekoek,H.
  TITLE     Alteration of serpin specificity by a protein cofactor. Vitronectin
            endows plasminogen activator inhibitor 1 with thrombin inhibitory
            properties
  JOURNAL   J Biol Chem 265 (22), 13029-13035 (1990)
   PUBMED   1695900
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN309001.1, BC010860.1,
            M16006.1 and AI752990.1.
            
            Summary: This gene encodes a member of the serine proteinase
            inhibitor (serpin) superfamily. This member is the principal
            inhibitor of tissue plasminogen activator (tPA) and urokinase
            (uPA), and hence is an inhibitor of fibrinolysis. The protein also
            functions as a component of innate antiviral immunity. Defects in
            this gene are the cause of plasminogen activator inhibitor-1
            deficiency (PAI-1 deficiency), and high concentrations of the gene
            product are associated with thrombophilia. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M16006.1, SRR11853566.25644.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in immune response or antiviral
                                      activity
            MANE Ensembl match     :: ENST00000223095.5/ ENSP00000223095.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..402
                     /product="plasminogen activator inhibitor 1 isoform 2
                     precursor"
                     /note="serine (or cysteine) proteinase inhibitor, clade E
                     (nexin, plasminogen activator inhibitor type 1), member 1;
                     endothelial plasminogen activator inhibitor; serpin E1;
                     serpin peptidase inhibitor, clade E (nexin, plasminogen
                     activator inhibitor type 1), member 1"
                     /calculated_mol_wt=42769
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2309
     mat_peptide     24..402
                     /product="Plasminogen activator inhibitor 1.
                     /id=PRO_0000032499"
                     /note="propagated from UniProtKB/Swiss-Prot (P05121.1)"
                     /calculated_mol_wt=42769
     Region          29..402
                     /region_name="serpinE1_PAI-1"
                     /note="serpin family E member 1, plasminogen activator
                     inhibitor-1; cd02051"
                     /db_xref="CDD:381007"
     Site            order(124,133..134,137,143,145..148,154,158,161..162)
                     /site_type="other"
                     /note="vitronectin binding site [polypeptide binding]"
                     /db_xref="CDD:381007"
     Site            order(172..173,346,348)
                     /site_type="other"
                     /note="putative Cl binding site [ion binding]"
                     /db_xref="CDD:381007"
     Site            order(228,230,233,235,245,264,292..295,361..362,364..373)
                     /site_type="other"
                     /note="plasminogen activator binding site [polypeptide
                     binding]"
                     /db_xref="CDD:381007"
     Site            232
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05121.1)"
     Site            288
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05121.1)"
     Site            352
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P05121.1)"
     Site            355..380
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381007"
     Site            369..370
                     /site_type="other"
                     /note="Reactive bond; propagated from UniProtKB/Swiss-Prot
                     (P05121.1)"
     CDS             1..402
                     /gene="SERPINE1"
                     /gene_synonym="PAI; PAI-1; PAI1; PLANH1"
                     /coded_by="NM_000602.5:143..1351"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS5711.1"
                     /db_xref="GeneID:5054"
                     /db_xref="HGNC:HGNC:8583"
                     /db_xref="MIM:173360"
ORIGIN      
        1 mqmspaltcl vlglalvfge gsavhhppsy vahlasdfgv rvfqqvaqas kdrnvvfspy
       61 gvasvlamlq lttggetqqq iqaamgfkid dkgmapalrh lykelmgpwn kdeisttdai
      121 fvqrdlklvq gfmphffrlf rstvkqvdfs everarfiin dwvkthtkgm isnllgkgav
      181 dqltrlvlvn alyfngqwkt pfpdssthrr lfhksdgstv svpmmaqtnk fnytefttpd
      241 ghyydilelp yhgdtlsmfi aapyekevpl saltnilsaq lishwkgnmt rlprllvlpk
      301 fsletevdlr kplenlgmtd mfrqfqadft slsdqeplhv aqalqkvkie vnesgtvass
      361 stavivsarm apeeiimdrp flfvvrhnpt gtvlfmgqvm ep
//
LOCUS       NP_001244067             752 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase Itchy homolog isoform 3 [Homo sapiens].
ACCESSION   NP_001244067
VERSION     NP_001244067.1
DBSOURCE    REFSEQ: accession NM_001257138.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Shen,S., Cai,D., Liang,H., Zeng,G., Liu,W., Yan,R., Yu,X.,
            Zhang,H., Liu,S., Li,W., Deng,R., Lu,X., Liu,Y., Sun,J. and Guo,H.
  TITLE     NEDD4 family ubiquitin ligase AIP4 interacts with Alix to enable
            HBV naked capsid egress in an Alix ubiquitination-independent
            manner
  JOURNAL   PLoS Pathog 20 (9), e1012485 (2024)
   PUBMED   39259704
  REMARK    GeneRIF: NEDD4 family ubiquitin ligase AIP4 interacts with Alix to
            enable HBV naked capsid egress in an Alix
            ubiquitination-independent manner.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Gahlot,P., Kravic,B., Rota,G., van den Boom,J., Levantovsky,S.,
            Schulze,N., Maspero,E., Polo,S., Behrends,C. and Meyer,H.
  TITLE     Lysosomal damage sensing and lysophagy initiation by SPG20-ITCH
  JOURNAL   Mol Cell 84 (8), 1556-1569 (2024)
   PUBMED   38503285
  REMARK    GeneRIF: Lysosomal damage sensing and lysophagy initiation by
            SPG20-ITCH.
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Totland,M.Z., Knudsen,L.M., Rasmussen,N.L., Omori,Y., Sorensen,V.,
            Elster,V.C.W., Stenersen,J.M., Larsen,M., Jensen,C.L., Zickfeldt
            Lade,A.A., Bruusgaard,E., Basing,S., Kryeziu,K., Brech,A.,
            Aasen,T., Lothe,R.A. and Leithe,E.
  TITLE     The E3 ubiquitin ligase ITCH negatively regulates intercellular
            communication via gap junctions by targeting connexin43 for
            lysosomal degradation
  JOURNAL   Cell Mol Life Sci 81 (1), 171 (2024)
   PUBMED   38597989
  REMARK    GeneRIF: The E3 ubiquitin ligase ITCH negatively regulates
            intercellular communication via gap junctions by targeting
            connexin43 for lysosomal degradation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 752)
  AUTHORS   Lohr,N.J., Molleston,J.P., Strauss,K.A., Torres-Martinez,W.,
            Sherman,E.A., Squires,R.H., Rider,N.L., Chikwava,K.R.,
            Cummings,O.W., Morton,D.H. and Puffenberger,E.G.
  TITLE     Human ITCH E3 ubiquitin ligase deficiency causes syndromic
            multisystem autoimmune disease
  JOURNAL   Am J Hum Genet 86 (3), 447-453 (2010)
   PUBMED   20170897
  REMARK    GeneRIF: describe, in ten patients, identification of a mutation
            resulting in truncation of ITCH. These patients not only have
            multisystem autoimmune disease but also display morphologic and
            developmental abnormalities.
REFERENCE   6  (residues 1 to 752)
  AUTHORS   Chen,X., Wen,S., Fukuda,M.N., Gavva,N.R., Hsu,D., Akama,T.O.,
            Yang-Feng,T. and Shen,C.K.
  TITLE     Human ITCH is a coregulator of the hematopoietic transcription
            factor NF-E2
  JOURNAL   Genomics 73 (2), 238-241 (2001)
   PUBMED   11318614
  REMARK    GeneRIF: gene expression regulation; coregulates hematopoietic
            transcription factor NF-E2
REFERENCE   7  (residues 1 to 752)
  AUTHORS   Qiu,L., Joazeiro,C., Fang,N., Wang,H.Y., Elly,C., Altman,Y.,
            Fang,D., Hunter,T. and Liu,Y.C.
  TITLE     Recognition and ubiquitination of Notch by Itch, a hect-type E3
            ubiquitin ligase
  JOURNAL   J Biol Chem 275 (46), 35734-35737 (2000)
   PUBMED   10940313
REFERENCE   8  (residues 1 to 752)
  AUTHORS   Winberg,G., Matskova,L., Chen,F., Plant,P., Rotin,D., Gish,G.,
            Ingham,R., Ernberg,I. and Pawson,T.
  TITLE     Latent membrane protein 2A of Epstein-Barr virus binds WW domain E3
            protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases
  JOURNAL   Mol Cell Biol 20 (22), 8526-8535 (2000)
   PUBMED   11046148
REFERENCE   9  (residues 1 to 752)
  AUTHORS   Wood,J.D., Yuan,J., Margolis,R.L., Colomer,V., Duan,K., Kushi,J.,
            Kaminsky,Z., Kleiderlein,J.J., Sharp,A.H. and Ross,C.A.
  TITLE     Atrophin-1, the DRPLA gene product, interacts with two families of
            WW domain-containing proteins
  JOURNAL   Mol Cell Neurosci 11 (3), 149-160 (1998)
   PUBMED   9647693
REFERENCE   10 (residues 1 to 752)
  AUTHORS   Perry,W.L., Hustad,C.M., Swing,D.A., O'Sullivan,T.N., Jenkins,N.A.
            and Copeland,N.G.
  TITLE     The itchy locus encodes a novel ubiquitin protein ligase that is
            disrupted in a18H mice
  JOURNAL   Nat Genet 18 (2), 143-146 (1998)
   PUBMED   9462742
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL356299.16, AL705688.1,
            AK304090.1, AF038564.1, AL109923.29, AA730741.1 and BG928040.1.
            
            Summary: This gene encodes a member of the Nedd4 family of HECT
            domain E3 ubiquitin ligases. HECT domain E3 ubiquitin ligases
            transfer ubiquitin from E2 ubiquitin-conjugating enzymes to protein
            substrates, thus targeting specific proteins for lysosomal
            degradation. The encoded protein plays a role in multiple cellular
            processes including erythroid and lymphoid cell differentiation and
            the regulation of immune responses. Mutations in this gene are a
            cause of syndromic multisystem autoimmune disease. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed for this gene. [provided by RefSeq, Mar 2012].
            
            Transcript Variant: This variant (3) lacks two internal exons and
            initiates translation at a downstream, in-frame start codon,
            compared to variant 1. The encoded isoform (3) is shorter than
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK304090.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..752
                     /product="E3 ubiquitin-protein ligase Itchy homolog
                     isoform 3"
                     /EC_number="2.3.2.26"
                     /note="atrophin-1 interacting protein 4; NFE2-associated
                     polypeptide 1; itchy E3 ubiquitin protein ligase homolog;
                     HECT-type E3 ubiquitin transferase Itchy homolog"
                     /calculated_mol_wt=86367
     Region          <1..30
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Region          177..206
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          <208..752
                     /region_name="HUL4"
                     /note="Ubiquitin-protein ligase [Posttranslational
                     modification, protein turnover, chaperones]; COG5021"
                     /db_xref="CDD:227354"
     CDS             1..752
                     /gene="ITCH"
                     /gene_synonym="ADMFD; AIF4; AIP4; NAPP1"
                     /coded_by="NM_001257138.3:364..2622"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58769.1"
                     /db_xref="GeneID:83737"
                     /db_xref="HGNC:HGNC:13890"
                     /db_xref="MIM:606409"
ORIGIN      
        1 mkleevvvtl qlggdkepte tigdlsicld glqlesevvt ngettcsesa sqnddgsrsk
       61 detrvstngs ddpedagage nrrvsgnnsp slsnggfkps rpprpsrppp ptprrpasvn
      121 gspsatsesd gsstgslppt ntntntsega tsgliiplti sggsgprpln pvtqaplppg
      181 weqrvdqhgr vyyvdhvekr ttwdrpeplp pgwerrvdnm griyyvdhft rtttwqrptl
      241 esvrnyeqwq lqrsqlqgam qqfnqrfiyg nqdlfatsqs kefdplgplp pgwekrtdsn
      301 grvyfvnhnt ritqwedprs qgqlnekplp egwemrftvd gipyfvdhnr rtttyidprt
      361 gksaldngpq iayvrdfkak vqyfrfwcqq lampqhikit vtrktlfeds fqqimsfspq
      421 dlrrrlwvif pgeegldygg varewfflls hevlnpmycl feyagkdnyc lqinpasyin
      481 pdhlkyfrfi grfiamalfh gkfidtgfsl pfykrilnkp vglkdlesid pefynsliwv
      541 kennieecdl emyfsvdkei lgeikshdlk pnggnilvte enkeeyirmv aewrlsrgve
      601 eqtqaffegf neilpqqylq yfdakelevl lcgmqeidln dwqrhaiyrh yartskqimw
      661 fwqfvkeidn ekrmrllqfv tgtcrlpvgg fadlmgsngp qkfciekvgk enwlprshtc
      721 fnrldlppyk syeqlkekll faieetegfg qe
//
LOCUS       NP_001362962             606 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA-splicing factor CWC22 homolog isoform c [Homo sapiens].
ACCESSION   NP_001362962
VERSION     NP_001362962.1
DBSOURCE    REFSEQ: accession NM_001376033.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Han,S.W., Ahn,J.Y., Lee,S., Noh,Y.S., Jung,H.C., Lee,M.H.,
            Park,H.J., Chun,H.J., Choi,S.J., Kim,E.S. and Lee,J.Y.
  TITLE     Gene expression network analysis of lymph node involvement in colon
            cancer identifies AHSA2, CDK10, and CWC22 as possible prognostic
            markers
  JOURNAL   Sci Rep 10 (1), 7170 (2020)
   PUBMED   32345988
  REMARK    GeneRIF: Gene expression network analysis of lymph node involvement
            in colon cancer identifies AHSA2, CDK10, and CWC22 as possible
            prognostic markers.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 606)
  AUTHORS   Tao,S., Wang,Z., Feng,J., Hsu,F.C., Jin,G., Kim,S.T., Zhang,Z.,
            Gronberg,H., Zheng,L.S., Isaacs,W.B., Xu,J. and Sun,J.
  TITLE     A genome-wide search for loci interacting with known prostate
            cancer risk-associated genetic variants
  JOURNAL   Carcinogenesis 33 (3), 598-603 (2012)
   PUBMED   22219177
REFERENCE   7  (residues 1 to 606)
  AUTHORS   Hegele,A., Kamburov,A., Grossmann,A., Sourlis,C., Wowro,S.,
            Weimann,M., Will,C.L., Pena,V., Luhrmann,R. and Stelzl,U.
  TITLE     Dynamic protein-protein interaction wiring of the human spliceosome
  JOURNAL   Mol Cell 45 (4), 567-580 (2012)
   PUBMED   22365833
REFERENCE   8  (residues 1 to 606)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   9  (residues 1 to 606)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   10 (residues 1 to 606)
  AUTHORS   Kelly,W.G., Xu,S., Montgomery,M.K. and Fire,A.
  TITLE     Distinct requirements for somatic and germline expression of a
            generally expressed Caernorhabditis elegans gene
  JOURNAL   Genetics 146 (1), 227-238 (1997)
   PUBMED   9136012
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC068194.6 and AC096587.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3601976.1,
                                           SRR1660805.195758.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.3"
     Protein         1..606
                     /product="pre-mRNA-splicing factor CWC22 homolog isoform
                     c"
                     /note="functional spliceosome-associated protein b;
                     pre-mRNA-splicing factor CWC22 homolog; nucampholin
                     homolog; CWC22 homolog, spliceosome-associated protein;
                     CWC22 spliceosome associated protein homolog"
                     /calculated_mol_wt=70398
     Region          1..129
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCG8.3)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCG8.3)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9HCG8.3)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C5N3; propagated from
                     UniProtKB/Swiss-Prot (Q9HCG8.3)"
     Region          164..345
                     /region_name="MIF4G"
                     /note="Middle domain of eukaryotic initiation factor 4G
                     (eIF4G); smart00543"
                     /db_xref="CDD:214713"
     Region          404..443
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCG8.3)"
     Region          455..561
                     /region_name="MA3"
                     /note="MA3 domain; cl02653"
                     /db_xref="CDD:413424"
     CDS             1..606
                     /gene="CWC22"
                     /gene_synonym="EIF4GL; fSAPb; NCM"
                     /coded_by="NM_001376033.1:151..1971"
                     /note="isoform c is encoded by transcript variant 5"
                     /db_xref="GeneID:57703"
                     /db_xref="HGNC:HGNC:29322"
                     /db_xref="MIM:615186"
ORIGIN      
        1 mkssvaqikp ssghdrrenl nsyqrnsspe dryeeqersp rdrdyfdysr sdyehsrrgr
       61 sydssmesrn rdrekrrere rdtdrkrsrk spspgrrnpe tsvtqsssaq depatkkkkd
      121 eldplltrtg gayippaklr mmqeqitdkn slayqrmswe alkksingli nkvnisnisi
      181 iiqellqeni vrgrgllsrs vlqaqsaspi fthvyaalva iinskfpqig elilkrliln
      241 frkgyrrndk qlcltaskfv ahlinqnvah evlclemltl llerptddsv evaigflkec
      301 glkltqvspr ginaiferlr nilheseidk rvqymievmf avrkdgfkdh piilegldlv
      361 eeddqfthml pleddynped vlnvfkmdpn fmeneekyka ikkeildegd tdsntdqdag
      421 sseedeeeee eegeedeegq kvtihdktei nlvsfrrtiy laiqssldfe ecahkllkme
      481 fpesqtkelc nmildccaqq rtyekffgll agrfcmlkke ymesfegifk eqydtihrle
      541 tnklrnvakm fahllytdsl pwsvlecikl seetttsssr ifvkiffqel ceymglpkln
      601 arlkdd
//
LOCUS       NP_001242974             582 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            beta isoform isoform 2 [Homo sapiens].
ACCESSION   NP_001242974
VERSION     NP_001242974.1
DBSOURCE    REFSEQ: accession NM_001256045.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Liu,L., Feng,X., Fan,C., Kong,D., Feng,X., Sun,C., Xu,Y., Li,B.,
            Jiang,Y. and Zheng,C.
  TITLE     PDCD4 interacting with PIK3CB and CTSZ promotes the apoptosis of
            multiple myeloma cells
  JOURNAL   FASEB J 38 (16), e70024 (2024)
   PUBMED   39190024
  REMARK    GeneRIF: PDCD4 interacting with PIK3CB and CTSZ promotes the
            apoptosis of multiple myeloma cells.
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Liu,G., Hou,Y., Jin,X., Zhang,Y., Sun,C., Huang,C., Ren,Y., Gao,J.,
            Wang,X. and Jiang,X.
  TITLE     PI3K/HSCB axis facilitates FOG1 nuclear translocation to promote
            erythropoiesis and megakaryopoiesis
  JOURNAL   Elife 13, 95815 (2024)
   PUBMED   38757931
  REMARK    GeneRIF: PI3K/HSCB axis facilitates FOG1 nuclear translocation to
            promote erythropoiesis and megakaryopoiesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Duewell,B.R., Wilson,N.E., Bailey,G.M., Peabody,S.E. and
            Hansen,S.D.
  TITLE     Molecular dissection of PI3Kbeta synergistic activation by receptor
            tyrosine kinases, GbetaGgamma, and Rho-family GTPases
  JOURNAL   Elife 12, 88991 (2024)
   PUBMED   38713746
  REMARK    GeneRIF: Molecular dissection of PI3Kbeta synergistic activation by
            receptor tyrosine kinases, GbetaGgamma, and Rho-family GTPases.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 582)
  AUTHORS   Xu,W., Chen,Y., Zhang,Z., Jiang,Y. and Wang,Z.
  TITLE     Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma
  JOURNAL   Med Oncol 40 (8), 221 (2023)
   PUBMED   37402056
  REMARK    GeneRIF: Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 582)
  AUTHORS   Milani,D., Mazzoni,M., Borgatti,P., Zauli,G., Cantley,L. and
            Capitani,S.
  TITLE     Extracellular human immunodeficiency virus type-1 Tat protein
            activates phosphatidylinositol 3-kinase in PC12 neuronal cells
  JOURNAL   J Biol Chem 271 (38), 22961-22964 (1996)
   PUBMED   8798481
REFERENCE   7  (residues 1 to 582)
  AUTHORS   Bonnefoy-Berard,N., Liu,Y.C., von Willebrand,M., Sung,A., Elly,C.,
            Mustelin,T., Yoshida,H., Ishizaka,K. and Altman,A.
  TITLE     Inhibition of phosphatidylinositol 3-kinase activity by association
            with 14-3-3 proteins in T cells
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10142-10146 (1995)
   PUBMED   7479742
REFERENCE   8  (residues 1 to 582)
  AUTHORS   Hu,P. and Schlessinger,J.
  TITLE     Direct association of p110 beta phosphatidylinositol 3-kinase with
            p85 is mediated by an N-terminal fragment of p110 beta
  JOURNAL   Mol Cell Biol 14 (4), 2577-2583 (1994)
   PUBMED   8139559
REFERENCE   9  (residues 1 to 582)
  AUTHORS   Hu,P., Mondino,A., Skolnik,E.Y. and Schlessinger,J.
  TITLE     Cloning of a novel, ubiquitously expressed human
            phosphatidylinositol 3-kinase and identification of its binding
            site on p85
  JOURNAL   Mol Cell Biol 13 (12), 7677-7688 (1993)
   PUBMED   8246984
REFERENCE   10 (residues 1 to 582)
  AUTHORS   Carpenter,C.L., Duckworth,B.C., Auger,K.R., Cohen,B.,
            Schaffhausen,B.S. and Cantley,L.C.
  TITLE     Purification and characterization of phosphoinositide 3-kinase from
            rat liver
  JOURNAL   J Biol Chem 265 (32), 19704-19711 (1990)
   PUBMED   2174051
  REMARK    GeneRIF: This paper reports the first purification of a
            phosphoinositide 3-kinase and shows that the protein is a
            heterodimer of an 85 kd regulatory subunit that mediates binding to
            phosphorylated proteins and a 110 kd catalytic subunit.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK293754.1, AC117389.5, AC020890.22 and AI623206.1.
            
            Summary: This gene encodes an isoform of the catalytic subunit of
            phosphoinositide 3-kinase (PI3K). These kinases are important in
            signaling pathways involving receptors on the outer membrane of
            eukaryotic cells and are named for their catalytic subunit. The
            encoded protein is the catalytic subunit for PI3Kbeta (PI3KB).
            PI3KB has been shown to be part of the activation pathway in
            neutrophils which have bound immune complexes at sites of injury or
            infection. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at a
            downstream AUG compared to variant 1. The resulting protein
            (isoform 2) is shorter and has a distinct N-terminus compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293754.1, SRR1803615.63220.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..582
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit beta isoform isoform 2"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.1.153"
                     /note="PI3-kinase p110 subunit beta; PtdIns-3-kinase p110;
                     PI3K-beta; PI3-kinase subunit beta; ptdIns-3-kinase
                     subunit beta; ptdIns-3-kinase subunit p110-beta;
                     phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa
                     catalytic subunit beta; serine/threonine protein kinase
                     PIK3CB; phosphoinositide-3-kinase, catalytic, beta
                     polypeptide"
                     /calculated_mol_wt=66703
     Region          <1..30
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Region          44..214
                     /region_name="PI3Ka_I"
                     /note="Phosphoinositide 3-kinase (PI3K) class I, accessory
                     domain; PIK domain is conserved in all PI3 and
                     PI4-kinases. Its role is unclear but it has been suggested
                     to be involved in substrate presentation. In general, PI3K
                     class I prefer phosphoinositol (4,5)...; cd00872"
                     /db_xref="CDD:238444"
     Region          218..579
                     /region_name="PI3Kc_IA_beta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase beta; cd05173"
                     /db_xref="CDD:270717"
     Site            order(291,293..295,297,315,317,320,351,363..366,371,374,
                     436,438,448..449)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270717"
     Site            order(358..359,386..387,390,460..461,474,477,485..488,491,
                     558,561..562,564..565)
                     /site_type="other"
                     /note="regulatory subunit interface [polypeptide binding]"
                     /db_xref="CDD:270717"
     Site            405
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270717"
     Site            428..436
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270717"
     Site            order(449..462,468..473)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270717"
     CDS             1..582
                     /gene="PIK3CB"
                     /gene_synonym="P110BETA; PI3K; PI3KBETA; PIK3C1"
                     /coded_by="NM_001256045.2:347..2095"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:5291"
                     /db_xref="HGNC:HGNC:8976"
                     /db_xref="MIM:602925"
ORIGIN      
        1 mlnpmgtvqt npytenatal hvkfpenkkq pyyyppfdks rggkkflpvl keildrdpls
       61 qlcenemdli wtlrqdcrei fpqslpklll sikwnkledv aqlqallqiw pklppreale
      121 lldfnypdqy vreyavgclr qmsdeelsqy llqlvqvlky epfldcalsr flleralgnr
      181 rigqflfwhl rsevhipavs vqfgvileay crgsvghmkv lskqvealnk lktlnslikl
      241 navklnrakg keamhtclkq sayrealsdl qsplnpcvil selyvekcky mdskmkplwl
      301 vynnkvfged svgvifkngd dlrqdmltlq mlrlmdllwk eagldlrmlp ygclatgdrs
      361 glievvstse tiadiqlnss nvaaaaafnk dallnwlkey nsgddldrai eeftlscagy
      421 cvasyvlgig drhsdnimvk ktgqlfhidf ghilgnfksk fgikrervpf iltydfihvi
      481 qqgktgntek fgrfrqcced aylilrrhgn lfitlfalml taglpeltsv kdiqylkdsl
      541 algkseeeal kqfkqkfdea lreswttkvn wmahtvrkdy rs
//
LOCUS       NP_004963               1132 aa            linear   PRI 21-NOV-2025
DEFINITION  tyrosine-protein kinase JAK2 isoform a [Homo sapiens].
ACCESSION   NP_004963
VERSION     NP_004963.1
DBSOURCE    REFSEQ: accession NM_004972.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1132)
  AUTHORS   Shin,J.J., Suk,K. and Lee,W.H.
  TITLE     LncRNA BRE-AS1 regulates the JAK2/STAT3-mediated inflammatory
            activation via the miR-30b-5p/SOC3 axis in THP-1 cells
  JOURNAL   Sci Rep 14 (1), 25726 (2024)
   PUBMED   39468152
  REMARK    GeneRIF: LncRNA BRE-AS1 regulates the JAK2/STAT3-mediated
            inflammatory activation via the miR-30b-5p/SOC3 axis in THP-1
            cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1132)
  AUTHORS   Chen,H., Ge,X., Li,C., Zeng,J. and Wang,X.
  TITLE     Structure and assembly of the human IL-12 signaling complex
  JOURNAL   Structure 32 (10), 1640-1651 (2024)
   PUBMED   39111304
REFERENCE   3  (residues 1 to 1132)
  AUTHORS   Peng,Z., Fang,C., Yuan,H., Zhu,Y., Ren,Z., Lu,M. and Hu,K.
  TITLE     miR-135b-5p promotes gastric carcinogenesis by targeting
            CLIP4-mediated JAK2/STAT3 signal pathway
  JOURNAL   Cell Signal 122, 111339 (2024)
   PUBMED   39121973
  REMARK    GeneRIF: miR-135b-5p promotes gastric carcinogenesis by targeting
            CLIP4-mediated JAK2/STAT3 signal pathway.
REFERENCE   4  (residues 1 to 1132)
  AUTHORS   Haage,T.R., Charakopoulos,E., Bhuria,V., Baldauf,C.K., Korthals,M.,
            Handschuh,J., Muller,P., Li,J., Harit,K., Nishanth,G., Frey,S.,
            Bottcher,M., Fischer,K.D., Dudeck,J., Dudeck,A., Lipka,D.B.,
            Schraven,B., Green,A.R., Muller,A.J., Mougiakakos,D. and Fischer,T.
  TITLE     Neutrophil-specific expression of JAK2-V617F or CALRmut induces
            distinct inflammatory profiles in myeloproliferative neoplasia
  JOURNAL   J Hematol Oncol 17 (1), 43 (2024)
   PUBMED   38853260
  REMARK    GeneRIF: Neutrophil-specific expression of JAK2-V617F or CALRmut
            induces distinct inflammatory profiles in myeloproliferative
            neoplasia.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1132)
  AUTHORS   Zhao,Y., Liang,B., Sheng,S., Wang,C., Jin,B., Zhang,X., Cheng,Y.,
            Shen,C. and Zheng,F.
  TITLE     AIM2 inflammasome regulated by the IFN-gamma/JAK2/STAT1 pathway
            promotes activation and pyroptosis of monocytes in Coronary Artery
            Disease
  JOURNAL   Immun Inflamm Dis 12 (6), e1317 (2024)
   PUBMED   38869352
  REMARK    GeneRIF: AIM2 inflammasome regulated by the IFN-gamma/JAK2/STAT1
            pathway promotes activation and pyroptosis of monocytes in Coronary
            Artery Disease.
REFERENCE   6  (residues 1 to 1132)
  AUTHORS   Tavernier,J., Tuypens,T., Plaetinck,G., Verhee,A., Fiers,W. and
            Devos,R.
  TITLE     Molecular basis of the membrane-anchored and two soluble isoforms
            of the human interleukin 5 receptor alpha subunit
  JOURNAL   Proc Natl Acad Sci U S A 89 (15), 7041-7045 (1992)
   PUBMED   1495999
REFERENCE   7  (residues 1 to 1132)
  AUTHORS   Pritchard,M.A., Baker,E., Callen,D.F., Sutherland,G.R. and
            Wilks,A.F.
  TITLE     Two members of the JAK family of protein tyrosine kinases map to
            chromosomes 1p31.3 and 9p24
  JOURNAL   Mamm Genome 3 (1), 36-38 (1992)
   PUBMED   1581631
REFERENCE   8  (residues 1 to 1132)
  AUTHORS   Wilks,A.F., Harpur,A.G., Kurban,R.R., Ralph,S.J., Zurcher,G. and
            Ziemiecki,A.
  TITLE     Two novel protein-tyrosine kinases, each with a second
            phosphotransferase-related catalytic domain, define a new class of
            protein kinase
  JOURNAL   Mol Cell Biol 11 (4), 2057-2065 (1991)
   PUBMED   1848670
REFERENCE   9  (residues 1 to 1132)
  AUTHORS   Hayashida,K., Kitamura,T., Gorman,D.M., Arai,K., Yokota,T. and
            Miyajima,A.
  TITLE     Molecular cloning of a second subunit of the receptor for human
            granulocyte-macrophage colony-stimulating factor (GM-CSF):
            reconstitution of a high-affinity GM-CSF receptor
  JOURNAL   Proc Natl Acad Sci U S A 87 (24), 9655-9659 (1990)
   PUBMED   1702217
REFERENCE   10 (residues 1 to 1132)
  AUTHORS   Jones,S.S., D'Andrea,A.D., Haines,L.L. and Wong,G.G.
  TITLE     Human erythropoietin receptor: cloning, expression, and biologic
            characterization
  JOURNAL   Blood 76 (1), 31-35 (1990)
   PUBMED   2163696
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF005216.1, AL158147.17,
            AF058925.2, AI923337.1 and AL161450.14.
            
            Summary: This gene encodes a non-receptor tyrosine kinase that
            plays a central role in cytokine and growth factor signalling. The
            primary isoform of this protein has an N-terminal FERM domain that
            is required for erythropoietin receptor association, an SH2 domain
            that binds STAT transcription factors, a pseudokinase domain and a
            C-terminal tyrosine kinase domain. Cytokine binding induces
            autophosphorylation and activation of this kinase. This kinase then
            recruits and phosphorylates signal transducer and activator of
            transcription (STAT) proteins. Growth factors like TGF-beta 1 also
            induce phosphorylation and activation of this kinase and
            translocation of downstream STAT proteins to the nucleus where they
            influence gene transcription. Mutations in this gene are associated
            with numerous inflammatory diseases and malignancies. This gene is
            a downstream target of the pleiotropic cytokine IL6 that is
            produced by B cells, T cells, dendritic cells and macrophages to
            produce an immune response or inflammation. Disregulation of the
            IL6/JAK2/STAT3 signalling pathways produces increased cellular
            proliferation and myeloproliferative neoplasms of hematopoietic
            stem cells. A nonsynonymous mutation in the pseudokinase domain of
            this gene disrupts the domains inhibitory effect and results in
            constitutive tyrosine phosphorylation activity and hypersensitivity
            to cytokine signalling. This gene and the IL6/JAK2/STAT3 signalling
            pathway is a therapeutic target for the treatment of excessive
            inflammatory responses to viral infections. Alternative splicing
            results in multiple transcript variants encoding distinct isoforms.
            [provided by RefSeq, Jul 2020].
            
            Transcript Variant: This variant (1), along with variants 2, 3, and
            4, all encode the same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF058925.2, SRR18074968.3599583.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in cytokine storm inflammatory
                                      response
            MANE Ensembl match     :: ENST00000381652.4/ ENSP00000371067.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1132
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.1"
     Protein         1..1132
                     /product="tyrosine-protein kinase JAK2 isoform a"
                     /EC_number="2.7.10.2"
                     /note="tyrosine-protein kinase JAK2; Janus kinase 2 (a
                     protein tyrosine kinase); JAK-2"
                     /calculated_mol_wt=130543
     Region          1..239
                     /region_name="Interaction with cytokine/interferon/growth
                     hormone receptors. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O60674.2)"
     Region          39..134
                     /region_name="FERM_F1"
                     /note="FERM F1 ubiquitin-like domain; pfam18379"
                     /db_xref="CDD:465733"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q62120; propagated from
                     UniProtKB/Swiss-Prot (O60674.2)"
     Region          143..261
                     /region_name="FERM_F2"
                     /note="FERM F2 acyl-CoA binding protein-like domain;
                     pfam18377"
                     /db_xref="CDD:436450"
     Region          266..386
                     /region_name="FERM_C_JAK2"
                     /note="FERM domain C-lobe of Janus kinase (JAK) 2;
                     cd13333"
                     /db_xref="CDD:270141"
     Site            order(274,295,297,316)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270141"
     Site            order(320,325..328,366,370,373..374)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270141"
     Site            352..353
                     /site_type="other"
                     /note="Breakpoint for translocation to form PCM1-JAK2
                     fusion protein; propagated from UniProtKB/Swiss-Prot
                     (O60674.2)"
     Site            366..377
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270141"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q62120; propagated from
                     UniProtKB/Swiss-Prot (O60674.2)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q62120; propagated from
                     UniProtKB/Swiss-Prot (O60674.2)"
     Region          386..482
                     /region_name="SH2_Jak2"
                     /note="Src homology 2 (SH2) domain in the Janus kinase 2
                     (Jak2) proteins; cd10379"
                     /db_xref="CDD:198242"
     Site            order(406,426,451,453)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198242"
     Site            442..443
                     /site_type="other"
                     /note="Breakpoint for translocation to form PCM1-JAK2
                     fusion protein; propagated from UniProtKB/Swiss-Prot
                     (O60674.2)"
     Site            450..451
                     /site_type="other"
                     /note="Breakpoint for translocation to form PCM1-JAK2
                     fusion protein; propagated from UniProtKB/Swiss-Prot
                     (O60674.2)"
     Site            order(452,481)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198242"
     Site            504..505
                     /site_type="other"
                     /note="Breakpoint for translocation to form PCM1-JAK2
                     fusion protein; propagated from UniProtKB/Swiss-Prot
                     (O60674.2)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62120; propagated from
                     UniProtKB/Swiss-Prot (O60674.2)"
     Region          545..806
                     /region_name="PTK_Jak2_rpt1"
                     /note="Pseudokinase (repeat 1) domain of the Protein
                     Tyrosine Kinase, Janus kinase 2; cd05078"
                     /db_xref="CDD:270663"
     Site            order(551,554..555,557,559,579,581,626..629,633,673,
                     677..678,680,699,711..715,724,759)
                     /site_type="active"
                     /db_xref="CDD:270663"
     Site            order(551,554..555,557,559,579,581,626..629,633,673,
                     677..678,680)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270663"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60674.2)"
     Site            617
                     /site_type="other"
                     /note="V617F mutation site"
                     /db_xref="CDD:270663"
     Site            order(673,677,711..715,724,759)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270663"
     Site            698..717
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270663"
     Site            710..711
                     /site_type="other"
                     /note="Breakpoint for translocation to form PCM1-JAK2
                     fusion protein; propagated from UniProtKB/Swiss-Prot
                     (O60674.2)"
     Site            813
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q62120; propagated from
                     UniProtKB/Swiss-Prot (O60674.2)"
     Region          844..1127
                     /region_name="PTKc_Jak2_rpt2"
                     /note="Catalytic (repeat 2) domain of the Protein Tyrosine
                     Kinase, Janus kinase 2; cd14205"
                     /db_xref="CDD:271107"
     Site            order(855..857,863,880,911,929..933,935,976,980..981,983,
                     993..994,1013..1017,1026,1075)
                     /site_type="active"
                     /db_xref="CDD:271107"
     Site            order(855..857,863,880,911,929..933,935,980..981,983,
                     993..994)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271107"
     Site            868
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q62120; propagated from
                     UniProtKB/Swiss-Prot (O60674.2)"
     Site            966
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q62120; propagated from
                     UniProtKB/Swiss-Prot (O60674.2)"
     Site            972
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q62120; propagated from
                     UniProtKB/Swiss-Prot (O60674.2)"
     Site            order(976,980,1013..1017,1026,1075)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271107"
     Site            993..1019
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271107"
     Site            1007
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:16174768; propagated from
                     UniProtKB/Swiss-Prot (O60674.2)"
     Site            1008
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:16174768; propagated from
                     UniProtKB/Swiss-Prot (O60674.2)"
     CDS             1..1132
                     /gene="JAK2"
                     /gene_synonym="JTK10"
                     /coded_by="NM_004972.4:468..3866"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6457.1"
                     /db_xref="GeneID:3717"
                     /db_xref="HGNC:HGNC:6192"
                     /db_xref="MIM:147796"
ORIGIN      
        1 mgmacltmte megtstssiy qngdisgnan smkqidpvlq vylyhslgks eadyltfpsg
       61 eyvaeeicia askacgitpv yhnmfalmse teriwyppnh vfhidestrh nvlyrirfyf
      121 prwycsgsnr ayrhgisrga eapllddfvm sylfaqwrhd fvhgwikvpv thetqeeclg
      181 mavldmmria kendqtplai ynsisyktfl pkcirakiqd yhiltrkrir yrfrrfiqqf
      241 sqckatarnl klkylinlet lqsafytekf evkepgsgps geeifatiii tgnggiqwsr
      301 gkhkesetlt eqdlqlycdf pniidvsikq anqegsnesr vvtihkqdgk nleielsslr
      361 ealsfvslid gyyrltadah hylckevapp avleniqsnc hgpismdfai sklkkagnqt
      421 glyvlrcspk dfnkyfltfa verenvieyk hclitknene eynlsgtkkn fsslkdllnc
      481 yqmetvrsdn iifqftkccp pkpkdksnll vfrtngvsdv ptsptlqrpt hmnqmvfhki
      541 rnedlifnes lgqgtftkif kgvrrevgdy gqlhetevll kvldkahrny sesffeaasm
      601 msklshkhlv lnygvcvcgd enilvqefvk fgsldtylkk nkncinilwk levakqlawa
      661 mhfleentli hgnvcaknil lireedrktg nppfiklsdp gisitvlpkd ilqeripwvp
      721 pecienpknl nlatdkwsfg ttlweicsgg dkplsaldsq rklqfyedrh qlpapkwael
      781 anlinncmdy epdfrpsfra iirdlnslft pdyelltend mlpnmrigal gfsgafedrd
      841 ptqfeerhlk flqqlgkgnf gsvemcrydp lqdntgevva vkklqhstee hlrdfereie
      901 ilkslqhdni vkykgvcysa grrnlklime ylpygslrdy lqkhkeridh ikllqytsqi
      961 ckgmeylgtk ryihrdlatr nilvenenrv kigdfgltkv lpqdkeyykv kepgespifw
     1021 yapesltesk fsvasdvwsf gvvlyelfty ieksksppae fmrmigndkq gqmivfhlie
     1081 llknngrlpr pdgcpdeiym imtecwnnnv nqrpsfrdla lrvdqirdnm ag
//
LOCUS       NP_002637               1634 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing
            subunit beta isoform 1 [Homo sapiens].
ACCESSION   NP_002637 XP_011507932
VERSION     NP_002637.3
DBSOURCE    REFSEQ: accession NM_002646.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1634)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1634)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 1634)
  AUTHORS   Gozzelino,L., Kochlamazashvili,G., Baldassari,S., Mackintosh,A.I.,
            Licchetta,L., Iovino,E., Liu,Y.C., Bennett,C.A., Bennett,M.F.,
            Damiano,J.A., Zsurka,G., Marconi,C., Giangregorio,T., Magini,P.,
            Kuijpers,M., Maritzen,T., Norata,G.D., Baulac,S., Canafoglia,L.,
            Seri,M., Tinuper,P., Scheffer,I.E., Bahlo,M., Berkovic,S.F.,
            Hildebrand,M.S., Kunz,W.S., Giordano,L., Bisulli,F., Martini,M.,
            Haucke,V., Hirsch,E. and Pippucci,T.
  TITLE     Defective lipid signalling caused by mutations in PIK3C2B underlies
            focal epilepsy
  JOURNAL   Brain 145 (7), 2313-2331 (2022)
   PUBMED   35786744
  REMARK    GeneRIF: Defective lipid signalling caused by mutations in PIK3C2B
            underlies focal epilepsy.
REFERENCE   4  (residues 1 to 1634)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   5  (residues 1 to 1634)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1634)
  AUTHORS   Ueno,H., Honda,H., Nakamoto,T., Yamagata,T., Sasaki,K.,
            Miyagawa,K., Mitani,K., Yazaki,Y. and Hirai,H.
  TITLE     The phosphatidylinositol 3' kinase pathway is required for the
            survival signal of leukocyte tyrosine kinase
  JOURNAL   Oncogene 14 (25), 3067-3072 (1997)
   PUBMED   9223670
REFERENCE   7  (residues 1 to 1634)
  AUTHORS   Brown,R.A., Ho,L.K., Weber-Hall,S.J., Shipley,J.M. and Fry,M.J.
  TITLE     Identification and cDNA cloning of a novel mammalian C2
            domain-containing phosphoinositide 3-kinase, HsC2-PI3K
  JOURNAL   Biochem Biophys Res Commun 233 (2), 537-544 (1997)
   PUBMED   9144573
REFERENCE   8  (residues 1 to 1634)
  AUTHORS   Milani,D., Mazzoni,M., Borgatti,P., Zauli,G., Cantley,L. and
            Capitani,S.
  TITLE     Extracellular human immunodeficiency virus type-1 Tat protein
            activates phosphatidylinositol 3-kinase in PC12 neuronal cells
  JOURNAL   J Biol Chem 271 (38), 22961-22964 (1996)
   PUBMED   8798481
REFERENCE   9  (residues 1 to 1634)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
REFERENCE   10 (residues 1 to 1634)
  AUTHORS   Kozutsumi,H., Toyoshima,H., Hagiwara,K., Yazaki,Y. and Hirai,H.
  TITLE     Human ltk receptor tyrosine kinase binds to PLC-gamma 1, PI3-K, GAP
            and Raf-1 in vivo
  JOURNAL   Oncogene 9 (10), 2991-2998 (1994)
   PUBMED   8084603
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL606489.26, AK308153.1,
            BC132876.1 and Y11312.1.
            
            On or before Jan 7, 2020 this sequence version replaced
            XP_011507932.1, NP_002637.2.
            
            Summary: The protein encoded by this gene belongs to the
            phosphoinositide 3-kinase (PI3K) family. PI3-kinases play roles in
            signaling pathways involved in cell proliferation, oncogenic
            transformation, cell survival, cell migration, and intracellular
            protein trafficking. This protein contains a lipid kinase catalytic
            domain as well as a C-terminal C2 domain, a characteristic of class
            II PI3-kinases. C2 domains act as calcium-dependent phospholipid
            binding motifs that mediate translocation of proteins to membranes,
            and may also mediate protein-protein interactions. The PI3-kinase
            activity of this protein is sensitive to low nanomolar levels of
            the inhibitor wortmanin. The C2 domain of this protein was shown to
            bind phospholipids but not Ca2+, which suggests that this enzyme
            may function in a calcium-independent manner. [provided by RefSeq,
            Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: Y11312.1, BC136645.1 [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1634
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..1634
                     /product="phosphatidylinositol 4-phosphate 3-kinase C2
                     domain-containing subunit beta isoform 1"
                     /EC_number="2.7.1.137"
                     /EC_number="2.7.1.154"
                     /note="phosphatidylinositol 3-kinase C2 domain-containing
                     beta polypeptide; PTDINS-3-kinase C2 beta; PI3K-C2beta;
                     PI3K-C2-beta; ptdIns-3-kinase C2 subunit beta;
                     phosphoinositide 3-kinase-C2-beta; phosphatidylinositol
                     4-phosphate 3-kinase C2 domain-containing subunit beta;
                     phosphoinositide-3-kinase, class 2, beta polypeptide"
                     /calculated_mol_wt=184638
     Region          2..298
                     /region_name="Interaction with GRB2.
                     /evidence=ECO:0000269|PubMed:11533253"
                     /note="propagated from UniProtKB/Swiss-Prot (O00750.2)"
     Region          45..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00750.2)"
     Region          259..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00750.2)"
     Region          364..466
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, ras-binding domain; pfam00794"
                     /db_xref="CDD:395642"
     Region          622..794
                     /region_name="C2A_PI3K_class_II"
                     /note="C2 domain first repeat present in class II
                     phosphatidylinositol 3-kinases (PI3Ks); cd04012"
                     /db_xref="CDD:175979"
     Region          813..981
                     /region_name="PI3Ka_II"
                     /note="Phosphoinositide 3-kinase (PI3K) class II,
                     accessory domain (PIK domain); PIK domain is conserved in
                     all PI3 and PI4-kinases. Its role is unclear but it has
                     been suggested to be involved in substrate presentation.
                     In general, class II PI3-kinases...; cd00869"
                     /db_xref="CDD:238441"
     Region          987..1340
                     /region_name="PI3Kc_C2_beta"
                     /note="Catalytic domain of Class II Phosphoinositide
                     3-kinase beta; cd00895"
                     /db_xref="CDD:119421"
     Region          1056..1062
                     /region_name="G-loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (O00750.2)"
     Site            order(1057,1059..1061,1063,1081,1083,1086,1117,1129..1132,
                     1137,1140,1200,1202,1212..1213)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:119421"
     Region          1192..1200
                     /region_name="Catalytic loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (O00750.2)"
     Site            1192..1200
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:119421"
     Region          1211..1237
                     /region_name="Activation loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (O00750.2)"
     Site            1213..1237
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:119421"
     Region          1369..1477
                     /region_name="PX_PI3K_C2_beta"
                     /note="The phosphoinositide binding Phox Homology Domain
                     of the Beta Isoform of Class II Phosphoinositide
                     3-Kinases; cd07290"
                     /db_xref="CDD:132823"
     Site            order(1405..1407,1431..1432,1446)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132823"
     Region          1505..1627
                     /region_name="C2B_PI3K_class_II"
                     /note="C2 domain second repeat present in class II
                     phosphatidylinositol 3-kinases (PI3Ks); cd08381"
                     /db_xref="CDD:176027"
     Site            1555..1565
                     /site_type="active"
                     /note="nuclear localization signal [active]"
                     /db_xref="CDD:176027"
     CDS             1..1634
                     /gene="PIK3C2B"
                     /gene_synonym="C2-PI3K"
                     /coded_by="NM_002646.4:1334..6238"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1446.1"
                     /db_xref="GeneID:5287"
                     /db_xref="HGNC:HGNC:8972"
                     /db_xref="MIM:602838"
ORIGIN      
        1 msstqgngeh wkslesvgis rkelamaeal qmeydalsrl rhdkeenrak qnadpslisw
       61 depgvdfysk pagrrtdlkl lrglsgsdpt lnynslspqe gppnhstsqg pqpgsdpwpk
      121 gslsgdylyi fdgsdggvss spgpgdiegs ckklsppplp prasiwdtpp lpprkgspss
      181 skisqpsdin tfslveqlpg kllehrilee eevlggggqg rllgsvdydg indaitrlnl
      241 kstydaemlr datrgwkegr gpldfskdts gkpvarsktm ppqvpprtya srygnrknat
      301 pgknrrisaa pvgsrphtva nghelfevse erdeevaafc hmldilrsgs diqdyfltgy
      361 vwsavtpspe hlgdevnlkv tvlcdrlqea ltftcncsst vdlliyqtlc ythddlrnvd
      421 vgdfvlkpcg leeflqnkha lgsheyiqyc rkfdidirlq lmeqkvvrsd lartvnddqs
      481 pstlnylvhl qerpvkqtis rqalsllfdt yhnevdafll adgdfplkad rvvqsvkaic
      541 nalaavetpe itsalnqlpp cpsrmqpkiq kdpsvlavre nrekvvealt aaildlvely
      601 cntfnadfqt avpgsrkhdl vqeachfars laftvyathr ipiiwatsye dfylscslsh
      661 ggkelcsplq trrahfskyl fhlivwdqqi cfpvqvnrlp retllcatly alpipppgss
      721 seankqrrvp ealgwvttpl fnfrqvltcg rkllglwpat qenpsarwsa pnfhqpdsvi
      781 lqidfptsaf dikftsppgd kfspryefgs lreedqrklk dimqkeslyw ltdadkkrlw
      841 ekryychsev sslplvlasa pswewaclpd iyvllkqwth mnhqdalgll hatfpdqevr
      901 rmavqwigsl sdaelldylp qlvqalkyec yldsplvrfl lkravsdlrv thyffwllkd
      961 glkdsqfsir yqyllaallc ccgkglreef nrqcwlvnal aklaqqvrea apsarqgilr
     1021 tgleevkqff alngscrlpl spsllvkgiv prdcsyfnsn avplklsfqn vdplgenirv
     1081 ifkcgddlrq dmltlqmiri mskiwvqegl dmrmvifrcf stgrgrgmve mipnaetlrk
     1141 iqvehgvtgs fkdrpladwl qkhnpgedey ekavenfiys cagccvatyv lgicdrhndn
     1201 imlkttghmf hidfgrflgh aqmfgnikrd rapfvftsdm ayvinggdkp ssrfhdfvdl
     1261 ccqaynlirk hthlflnllg lmlscgipel sdledlkyvy dalrpqdtea nattyftrli
     1321 esslgsvatk lnffihnlaq mkftgsddrl tlsfasrtht lkssgrisdv flcrhekifh
     1381 pnkgyiyvvk vmrentheat yiqrtfeefq elhnklrllf psshlpsfps rfvigrsrge
     1441 avaerrreel ngyiwhliha ppevaecdlv ytffhplprd ekamgtspap kssdgtwarp
     1501 vgkvggevkl sisyknnklf imvmhirglq llqdgndpdp yvkiyllpdp qkttkrktkv
     1561 arktcnptyn emlvydgipk gdlqqrelql svlseqgfwe nvllgevnir lreldlaqek
     1621 tgwfalgsrs hgtl
//
LOCUS       NP_001164237             406 aa            linear   PRI 21-NOV-2025
DEFINITION  ligand-dependent corepressor isoform 2 [Homo sapiens].
ACCESSION   NP_001164237
VERSION     NP_001164237.1
DBSOURCE    REFSEQ: accession NM_001170766.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Flindris,S., Katsoulas,N., Goussia,A., Lazaris,A.C.,
            Navrozoglou,I., Paschopoulos,M. and Thymara,I.
  TITLE     The Expression of NRIP1 and LCOR in Endometrioid Endometrial Cancer
  JOURNAL   In Vivo 35 (5), 2631-2640 (2021)
   PUBMED   34410950
  REMARK    GeneRIF: The Expression of NRIP1 and LCOR in Endometrioid
            Endometrial Cancer.
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   7  (residues 1 to 406)
  AUTHORS   White,J.H., Fernandes,I., Mader,S. and Yang,X.J.
  TITLE     Corepressor recruitment by agonist-bound nuclear receptors
  JOURNAL   Vitam Horm 68, 123-143 (2004)
   PUBMED   15193453
  REMARK    Review article
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Shi,Y., Sawada,J., Sui,G., Affar el,B., Whetstine,J.R., Lan,F.,
            Ogawa,H., Luke,M.P., Nakatani,Y. and Shi,Y.
  TITLE     Coordinated histone modifications mediated by a CtBP co-repressor
            complex
  JOURNAL   Nature 422 (6933), 735-738 (2003)
   PUBMED   12700765
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Kunieda,T., Park,J.M., Takeuchi,H. and Kubo,T.
  TITLE     Identification and characterization of Mlr1,2: two mouse homologues
            of Mblk-1, a transcription factor from the honeybee brain(1)
  JOURNAL   FEBS Lett 535 (1-3), 61-65 (2003)
   PUBMED   12560079
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Fernandes,I., Bastien,Y., Wai,T., Nygard,K., Lin,R., Cormier,O.,
            Lee,H.S., Eng,F., Bertos,N.R., Pelletier,N., Mader,S., Han,V.K.,
            Yang,X.J. and White,J.H.
  TITLE     Ligand-dependent nuclear receptor corepressor LCoR functions by
            histone deacetylase-dependent and -independent mechanisms
  JOURNAL   Mol Cell 11 (1), 139-150 (2003)
   PUBMED   12535528
  REMARK    GeneRIF: Data show that LCoR (ligand-dependent nuclear receptor
            corepressor) represents a class of corepressor that attenuates
            agonist-activated nuclear receptor signaling by multiple mechanisms
            [Ligand-dependent nuclear receptor corepressor].
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA788606.1, BC053359.1, AL442123.12 and AB072899.1.
            
            Summary: LCOR is a transcriptional corepressor widely expressed in
            fetal and adult tissues that is recruited to agonist-bound nuclear
            receptors through a single LxxLL motif, also referred to as a
            nuclear receptor (NR) box (Fernandes et al., 2003 [PubMed
            12535528]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR, 3' UTR,
            and coding region, compared to variant 1. This results in a protein
            (isoform 2) that maintains the reading frame but is shorter at the
            C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053359.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2152798
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.1"
     Protein         1..406
                     /product="ligand-dependent corepressor isoform 2"
                     /note="mblk1-related protein 2"
                     /calculated_mol_wt=43952
     Region          1..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JN0.2)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96JN0.2)"
     Region          53..57
                     /region_name="Interaction with nuclear receptors"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JN0.2)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96JN0.2)"
     Region          64..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JN0.2)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96JN0.2)"
     Region          299..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JN0.2)"
     Region          339..345
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JN0.2)"
     Region          352..395
                     /region_name="HTH_psq"
                     /note="helix-turn-helix, Psq domain; pfam05225"
                     /db_xref="CDD:283007"
     CDS             1..406
                     /gene="LCOR"
                     /gene_synonym="C10orf12; MLR2"
                     /coded_by="NM_001170766.2:506..1726"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS53561.1"
                     /db_xref="GeneID:84458"
                     /db_xref="HGNC:HGNC:29503"
                     /db_xref="MIM:607698"
ORIGIN      
        1 mqrmiqqfaa eytsknsstq dpsqpnstkn qslpkaspvt tsptaattqn pvlskllmad
       61 qdspldltvr ksqsepseqd gvldlstkks pcagstslsh spgcsstqgn grpgrpsqyr
      121 pdglrsgdgv pprslqdgtr egfghstslk vplarslqis eellsrnqls taaslgpsgl
      181 qnhgqhlils reaswakphy efnlsrmkfr gngalsnisd lpflaensaf pkmalqakqd
      241 gkkdvshssp vdlkipqvrg mdlswesrtg dqysysslvm gsqtesalsk klrailpkqs
      301 rksmldagpd swgsdaeqst sgqpyptsdq egdpgskqpr kkrgryrqyn seileeaisv
      361 vmsgkmsvsk aqsiygiphs tleykvkerl gtlknppkkk mklmsg
//
LOCUS       NP_001274526             472 aa            linear   PRI 21-NOV-2025
DEFINITION  excitatory amino acid transporter 5 isoform 3 [Homo sapiens].
ACCESSION   NP_001274526 XP_005271191
VERSION     NP_001274526.1
DBSOURCE    REFSEQ: accession NM_001287597.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Lee,A., Balcar,V.J., McCombe,P. and Pow,D.V.
  TITLE     Human brain neurons express a novel splice variant of excitatory
            amino acid transporter 5 (hEAAT5v)
  JOURNAL   J Comp Neurol 528 (17), 3134-3142 (2020)
   PUBMED   32173860
  REMARK    GeneRIF: Human brain neurons express a novel splice variant of
            excitatory amino acid transporter 5 (hEAAT5v).
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Melville,S.A., Buros,J., Parrado,A.R., Vardarajan,B., Logue,M.W.,
            Shen,L., Risacher,S.L., Kim,S., Jun,G., DeCarli,C., Lunetta,K.L.,
            Baldwin,C.T., Saykin,A.J. and Farrer,L.A.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative
  TITLE     Multiple loci influencing hippocampal degeneration identified by
            genome scan
  JOURNAL   Ann Neurol 72 (1), 65-75 (2012)
   PUBMED   22745009
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Oshikawa,M., Tsutsui,C., Ikegami,T., Fuchida,Y., Matsubara,M.,
            Toyama,S., Usami,R., Ohtoko,K. and Kato,S.
  TITLE     Full-length transcriptome analysis of human retina-derived cell
            lines ARPE-19 and Y79 using the vector-capping method
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6662-6670 (2011)
   PUBMED   21697133
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 472)
  AUTHORS   Chung,S.A., Taylor,K.E., Graham,R.R., Nititham,J., Lee,A.T.,
            Ortmann,W.A., Jacob,C.O., Alarcon-Riquelme,M.E., Tsao,B.P.,
            Harley,J.B., Gaffney,P.M., Moser,K.L., Petri,M., Demirci,F.Y.,
            Kamboh,M.I., Manzi,S., Gregersen,P.K., Langefeld,C.D., Behrens,T.W.
            and Criswell,L.A.
  CONSRTM   SLEGEN
  TITLE     Differential genetic associations for systemic lupus erythematosus
            based on anti-dsDNA autoantibody production
  JOURNAL   PLoS Genet 7 (3), e1001323 (2011)
   PUBMED   21408207
REFERENCE   6  (residues 1 to 472)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 472)
  AUTHORS   Gratacos,M., Costas,J., de Cid,R., Bayes,M., Gonzalez,J.R.,
            Baca-Garcia,E., de Diego,Y., Fernandez-Aranda,F.,
            Fernandez-Piqueras,J., Guitart,M., Martin-Santos,R., Martorell,L.,
            Menchon,J.M., Roca,M., Saiz-Ruiz,J., Sanjuan,J., Torrens,M.,
            Urretavizcaya,M., Valero,J., Vilella,E., Estivill,X. and
            Carracedo,A.
  CONSRTM   Psychiatric Genetics Network Group
  TITLE     Identification of new putative susceptibility genes for several
            psychiatric disorders by association analysis of regulatory and
            non-synonymous SNPs of 306 genes involved in neurotransmission and
            neurodevelopment
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 150B (6), 808-816 (2009)
   PUBMED   19086053
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 472)
  AUTHORS   Boehmer,C., Rajamanickam,J., Schniepp,R., Kohler,K., Wulff,P.,
            Kuhl,D., Palmada,M. and Lang,F.
  TITLE     Regulation of the excitatory amino acid transporter EAAT5 by the
            serum and glucocorticoid dependent kinases SGK1 and SGK3
  JOURNAL   Biochem Biophys Res Commun 329 (2), 738-742 (2005)
   PUBMED   15737648
  REMARK    GeneRIF: In conclusion, the kinases SGK1 and SGK3 increase EAAT5
            activity by increasing cell surface abundance of the carrier.
REFERENCE   9  (residues 1 to 472)
  AUTHORS   Wistow,G., Bernstein,S.L., Ray,S., Wyatt,M.K., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human iris for the NEIBank
            Project: steroid-response factors and similarities with retinal
            pigment epithelium
  JOURNAL   Mol Vis 8, 185-195 (2002)
   PUBMED   12107412
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 472)
  AUTHORS   Arriza,J.L., Eliasof,S., Kavanaugh,M.P. and Amara,S.G.
  TITLE     Excitatory amino acid transporter 5, a retinal glutamate
            transporter coupled to a chloride conductance
  JOURNAL   Proc Natl Acad Sci U S A 94 (8), 4155-4160 (1997)
   PUBMED   9108121
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445183.19, AB593060.1, BC012119.1, CD672672.1 and AB593061.1.
            
            On Dec 18, 2013 this sequence version replaced XP_005271191.1.
            
            Transcript Variant: This variant (3) lacks an in-frame segment and
            uses an alternate in-frame splice site in the central coding
            region, compared to variant 1. The encoded isoform (3) is shorter,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB593061.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..472
                     /product="excitatory amino acid transporter 5 isoform 3"
                     /note="excitatory amino acid transporter 5 (retinal
                     glutamate transporter); solute carrier family 1 (glutamate
                     transporter), member 7"
                     /calculated_mol_wt=51113
     Region          15..403
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     CDS             1..472
                     /gene="SLC1A7"
                     /gene_synonym="AAAT; EAAT5"
                     /coded_by="NM_001287597.2:190..1608"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS72796.1"
                     /db_xref="GeneID:6512"
                     /db_xref="HGNC:HGNC:10945"
                     /db_xref="MIM:604471"
ORIGIN      
        1 mvphailarg rdvcrrngll ilsvlsvivg cllgfflrtr rlspqeisyf qfpgellmrm
       61 lkmmilplvv srnmfpanlv eatfkqyrtk ttpvvkspkv apeeapprri liygvqeeng
      121 shvqnfaldl tpppevvyks epgtsdgmnv lgivffsatm gimlgrmgds gaplvsfcqc
      181 lnesvmkiva vavwyfpfgi vfliagkile mddpravgkk lgfysvtvvc glvlhglfil
      241 pllyffitkk npivfirgil qallialats sssatlpitf kcllennhid rriarfvlpv
      301 gatinmdgta lyeavaaifi aqvnnyeldf gqiitisita taasigaagi pqaglvtmvi
      361 vltsvglptd ditliiavdw aldrfrtmin vlgdalaagi mahicrkdfa rdtgtetcfp
      421 spetaalrdq aseppgdrgs paewlceecs rglrahpgph lppprprssg ag
//
LOCUS       NP_001269045             749 aa            linear   PRI 21-NOV-2025
DEFINITION  transcription factor RFX3 isoform b [Homo sapiens].
ACCESSION   NP_001269045 XP_005251593
VERSION     NP_001269045.1
DBSOURCE    REFSEQ: accession NM_001282116.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 749)
  AUTHORS   Qian,Y., Cheng,B., Luo,J., Hu,Y., Gao,L. and Cheng,H.
  TITLE     CircRFX3 Up-regulates Its Host Gene RFX3 to Facilitate
            Tumorigenesis and Progression of Glioma
  JOURNAL   J Mol Neurosci 72 (6), 1195-1207 (2022)
   PUBMED   35416616
  REMARK    GeneRIF: CircRFX3 Up-regulates Its Host Gene RFX3 to Facilitate
            Tumorigenesis and Progression of Glioma.
REFERENCE   3  (residues 1 to 749)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 749)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 749)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 749)
  AUTHORS   Nakayama,A., Murakami,H., Maeyama,N., Yamashiro,N., Sakakibara,A.,
            Mori,N. and Takahashi,M.
  TITLE     Role for RFX transcription factors in non-neuronal cell-specific
            inactivation of the microtubule-associated protein MAP1A promoter
  JOURNAL   J Biol Chem 278 (1), 233-240 (2003)
   PUBMED   12411430
  REMARK    GeneRIF: Data show that two regulatory factor for X box (RFX1 and
            3) binding sites in exon1 of both the mouse and human
            microtubule-associated protein (MAP1A) gene are important for
            effective transcriptional repression in non-neuronal cells.
REFERENCE   7  (residues 1 to 749)
  AUTHORS   Morotomi-Yano,K., Yano,K., Saito,H., Sun,Z., Iwama,A. and Miki,Y.
  TITLE     Human regulatory factor X 4 (RFX4) is a testis-specific dimeric
            DNA-binding protein that cooperates with other human RFX members
  JOURNAL   J Biol Chem 277 (1), 836-842 (2002)
   PUBMED   11682486
REFERENCE   8  (residues 1 to 749)
  AUTHORS   Iwama,A., Pan,J., Zhang,P., Reith,W., Mach,B., Tenen,D.G. and
            Sun,Z.
  TITLE     Dimeric RFX proteins contribute to the activity and lineage
            specificity of the interleukin-5 receptor alpha promoter through
            activation and repression domains
  JOURNAL   Mol Cell Biol 19 (6), 3940-3950 (1999)
   PUBMED   10330134
REFERENCE   9  (residues 1 to 749)
  AUTHORS   Emery,P., Durand,B., Mach,B. and Reith,W.
  TITLE     RFX proteins, a novel family of DNA binding proteins conserved in
            the eukaryotic kingdom
  JOURNAL   Nucleic Acids Res 24 (5), 803-807 (1996)
   PUBMED   8600444
REFERENCE   10 (residues 1 to 749)
  AUTHORS   Reith,W., Ucla,C., Barras,E., Gaud,A., Durand,B.,
            Herrero-Sanchez,C., Kobr,M. and Mach,B.
  TITLE     RFX1, a transactivator of hepatitis B virus enhancer I, belongs to
            a novel family of homodimeric and heterodimeric DNA-binding
            proteins
  JOURNAL   Mol Cell Biol 14 (2), 1230-1244 (1994)
   PUBMED   8289803
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL365202.19, AL354941.10 and
            AL133549.11.
            
            On Aug 31, 2013 this sequence version replaced XP_005251593.1.
            
            Summary: This gene is a member of the regulatory factor X gene
            family, which encodes transcription factors that contain a
            highly-conserved winged helix DNA binding domain. The protein
            encoded by this gene is structurally related to regulatory factors
            X1, X2, X4, and X5. It is a transcriptional activator that can bind
            DNA as a monomer or as a heterodimer with other RFX family members.
            Multiple transcript variants encoding different isoforms have been
            described for this gene. [provided by RefSeq, Aug 2013].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.228756.1,
                                           SRR14038195.590129.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000617270.5/ ENSP00000482598.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.2"
     Protein         1..749
                     /product="transcription factor RFX3 isoform b"
                     /note="DNA binding protein RFX3; transcription factor
                     RFX3; regulatory factor X, 3 (influences HLA class II
                     expression)"
                     /calculated_mol_wt=83399
     Region          <51..138
                     /region_name="RFX1_trans_act"
                     /note="RFX1 transcription activation region; pfam04589"
                     /db_xref="CDD:461362"
     Region          184..258
                     /region_name="RFX_DNA_binding"
                     /note="RFX DNA-binding domain; pfam02257"
                     /db_xref="CDD:460512"
     Region          663..699
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48380.2)"
     CDS             1..749
                     /gene="RFX3"
                     /coded_by="NM_001282116.2:264..2513"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS6449.1"
                     /db_xref="GeneID:5991"
                     /db_xref="HGNC:HGNC:9984"
                     /db_xref="MIM:601337"
ORIGIN      
        1 mqtsetgsdt gstvtlqtsv asqaavptqv vqqvpvqqqv qqvqtvqqvq hvypaqvqyv
       61 egsdtvytng airtttypyt etqmysqntg gnyfdtqgss aqvttvvssh smvgtggiqm
      121 gvtggqliss sggtyligns mensghsvth ttraspatie maietlqksd glsthrssll
      181 nshlqwlldn yetaegvslp rstlynhylr hcqehkldpv naasfgklir sifmglrtrr
      241 lgtrgnskyh yygirvkpds plnrlqedmq ymamrqqpmq qkqrykpmqk vdgvadgftg
      301 sgqqtgtsve qtviaqsqhh qqfldasral pefgeveiss lpdgttfedi kslqslyreh
      361 ceaildvvvn lqfslieklw qtfwryspst ptdgttites snlseiesrl pkaklitlck
      421 hesilkwmcn cdhgmyqalv eilipdvlrp ipsaltqair nfakslegwl snamnnipqr
      481 miqtkvaavs afaqtlrryt slnhlaqaar avlqntsqin qmlsdlnrvd fanvqeqasw
      541 vcqcddnmvq rletdfkmtl qqqstleqwa awldnvmmqa lkpyegrpsf pkaarqfllk
      601 wsfyssmvir dltlrsaasf gsfhlirlly deymfylveh rvaqatgetp iavmgefgdl
      661 navspgnldk degsevesem deelddssep qakrektels qafpvgcmqp vletgvqpsl
      721 lnpihsehiv tstqtirqcs atgntytav
//
LOCUS       NP_001371087             489 aa            linear   PRI 21-NOV-2025
DEFINITION  fibulin-5 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001371087
VERSION     NP_001371087.1
DBSOURCE    REFSEQ: accession NM_001384158.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Zhao,M., Rong,R., Zhang,C., Yang,H., Han,X., Fan,Z., Zheng,Y. and
            Zhang,J.
  TITLE     FBLN5 was Regulated by PRDM9, and Promoted Senescence and
            Osteogenic Differentiation of Human Periodontal Ligament Stem Cells
  JOURNAL   Curr Stem Cell Res Ther 19 (3), 417-425 (2024)
   PUBMED   37608663
  REMARK    GeneRIF: FBLN5 was Regulated by PRDM9, and Promoted Senescence and
            Osteogenic Differentiation of Human Periodontal Ligament Stem
            Cells.
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Masood,M., Ding,Q., Cawte,A.D., Rueda,D.S., Grimm,S.W., Yague,E.
            and El-Bahrawy,M.
  TITLE     Genetic screening for anticancer genes highlights FBLN5 as a
            synthetic lethal partner of MYC
  JOURNAL   Cell Commun Signal 21 (1), 295 (2023)
   PUBMED   37864183
  REMARK    GeneRIF: Genetic screening for anticancer genes highlights FBLN5 as
            a synthetic lethal partner of MYC.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Kapuganti,R.S., Bharati,B., Mohanty,P.P. and Alone,D.P.
  TITLE     Genetic variants and haplotypes in fibulin-5 (FBLN5) are associated
            with pseudoexfoliation glaucoma but not with pseudoexfoliation
            syndrome
  JOURNAL   Biosci Rep 43 (3) (2023)
   PUBMED   36794549
  REMARK    GeneRIF: Genetic variants and haplotypes in fibulin-5 (FBLN5) are
            associated with pseudoexfoliation glaucoma but not with
            pseudoexfoliation syndrome.
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Li,Y., Yang,X. and Lu,D.
  TITLE     Knockdown of ubiquitin-conjugating enzyme E2T (UBE2T) suppresses
            lung adenocarcinoma progression via targeting fibulin-5 (FBLN5)
  JOURNAL   Bioengineered 13 (5), 11867-11880 (2022)
   PUBMED   35543375
  REMARK    GeneRIF: Knockdown of ubiquitin-conjugating enzyme E2T (UBE2T)
            suppresses lung adenocarcinoma progression via targeting fibulin-5
            (FBLN5).
REFERENCE   6  (residues 1 to 489)
  AUTHORS   Yanagisawa,H., Davis,E.C., Starcher,B.C., Ouchi,T., Yanagisawa,M.,
            Richardson,J.A. and Olson,E.N.
  TITLE     Fibulin-5 is an elastin-binding protein essential for elastic fibre
            development in vivo
  JOURNAL   Nature 415 (6868), 168-171 (2002)
   PUBMED   11805834
REFERENCE   7  (residues 1 to 489)
  AUTHORS   Kobayashi,M. and Hanai,R.
  TITLE     M phase-specific association of human topoisomerase IIIbeta with
            chromosomes
  JOURNAL   Biochem Biophys Res Commun 287 (1), 282-287 (2001)
   PUBMED   11549288
REFERENCE   8  (residues 1 to 489)
  AUTHORS   Nakamura,T., Ruiz-Lozano,P., Lindner,V., Yabe,D., Taniwaki,M.,
            Furukawa,Y., Kobuke,K., Tashiro,K., Lu,Z., Andon,N.L., Schaub,R.,
            Matsumori,A., Sasayama,S., Chien,K.R. and Honjo,T.
  TITLE     DANCE, a novel secreted RGD protein expressed in developing,
            atherosclerotic, and balloon-injured arteries
  JOURNAL   J Biol Chem 274 (32), 22476-22483 (1999)
   PUBMED   10428823
REFERENCE   9  (residues 1 to 489)
  AUTHORS   Kowal,R.C., Jolsin,J.M., Olson,E.N. and Schultz,R.A.
  TITLE     Assignment of fibulin-5 (FBLN5) to human chromosome 14q31 by in
            situ hybridization and radiation hybrid mapping
  JOURNAL   Cytogenet Cell Genet 87 (1-2), 2-3 (1999)
   PUBMED   10640802
REFERENCE   10 (residues 1 to 489)
  AUTHORS   Van Maldergem,L. and Loeys,B.
  TITLE     FBLN5-Related Cutis Laxa
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301756
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049872.3 and AL590328.2.
            
            Summary: The protein encoded by this gene is a secreted,
            extracellular matrix protein containing an Arg-Gly-Asp (RGD) motif
            and calcium-binding EGF-like domains. It promotes adhesion of
            endothelial cells through interaction of integrins and the RGD
            motif. It is prominently expressed in developing arteries but less
            so in adult vessels. However, its expression is reinduced in
            balloon-injured vessels and atherosclerotic lesions, notably in
            intimal vascular smooth muscle cells and endothelial cells.
            Therefore, the protein encoded by this gene may play a role in
            vascular development and remodeling. Defects in this gene are a
            cause of autosomal dominant cutis laxa, autosomal recessive cutis
            laxa type I (CL type I), and age-related macular degeneration type
            3 (ARMD3). [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX248290.1, SRR14372080.3715499.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.12"
     Protein         1..489
                     /product="fibulin-5 isoform 2 precursor"
                     /note="urine p50 protein; developmental arteries and
                     neural crest EGF-like protein; testis tissue sperm-binding
                     protein Li 75n; embryonic vascular EGF-like
                     repeat-containing protein"
                     /calculated_mol_wt=51765
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2379
     Region          168..199
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF domain; pfam07645"
                     /db_xref="CDD:429571"
     Region          216..246
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          248..286
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(248,251,264)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          299..327
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     CDS             1..489
                     /gene="FBLN5"
                     /gene_synonym="ADCL2; ARCL1A; ARMD3; CMT1H; DANCE; EVEC;
                     FIBL-5; HNARMD; UP50"
                     /coded_by="NM_001384158.1:466..1935"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS91919.1"
                     /db_xref="GeneID:10516"
                     /db_xref="HGNC:HGNC:3602"
                     /db_xref="MIM:604580"
ORIGIN      
        1 mpgikriltv tilalclpsp gnaqaqctng fdldrqsgqc ldgvslsspr lecngaisah
       61 cnlclpgssd ssasasqvag itdidecrti peacrgdmmc vnqnggylci prtnpvyrgp
      121 ysnpystpys gpypaaappl sapnyptisr plicrfgyqm desnqcvdvd ecatdshqcn
      181 ptqicinteg gytcsctdgy wllegqcldi decrygycqq lcanvpgsys ctcnpgftln
      241 edgrscqdvn ecatenpcvq tcvntygsfi crcdpgyele edgvhcsdmd ecsfseflcq
      301 hecvnqpgty fcscppgyil lddnrscqdi necehrnhtc nlqqtcynlq ggfkcidpir
      361 ceepylrisd nrcmcpaenp gcrdqpftil yrdmdvvsgr svpadifqmq attrypgayy
      421 ifqiksgneg refymrqtgp isatlvmtrp ikgpreiqld lemitvntvi nfrgssvirl
      481 riyvsqypf
//
LOCUS       NP_001091967            1093 aa            linear   PRI 21-NOV-2025
DEFINITION  small G protein signaling modulator 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001091967
VERSION     NP_001091967.1
DBSOURCE    REFSEQ: accession NM_001098497.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Li,J., Wang,J., Ding,Y., Zhao,J. and Wang,W.
  TITLE     Prognostic biomarker SGSM1 and its correlation with immune
            infiltration in gliomas
  JOURNAL   BMC Cancer 22 (1), 466 (2022)
   PUBMED   35484511
  REMARK    GeneRIF: Prognostic biomarker SGSM1 and its correlation with immune
            infiltration in gliomas.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1093)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1093)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 1093)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 1093)
  AUTHORS   Nottingham,R.M., Pusapati,G.V., Ganley,I.G., Barr,F.A.,
            Lambright,D.G. and Pfeffer,S.R.
  TITLE     RUTBC2 protein, a Rab9A effector and GTPase-activating protein for
            Rab36
  JOURNAL   J Biol Chem 287 (27), 22740-22748 (2012)
   PUBMED   22637480
  REMARK    GeneRIF: These data show that RUTBC2 can act as a Rab36 GAP in
            cells and suggest that RUTBC2 links Rab9A function to Rab36
            function in the endosomal system.
REFERENCE   7  (residues 1 to 1093)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   8  (residues 1 to 1093)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1093)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
REFERENCE   10 (residues 1 to 1093)
  AUTHORS   Yang,H., Sasaki,T., Minoshima,S. and Shimizu,N.
  TITLE     Identification of three novel proteins (SGSM1, 2, 3) which modulate
            small G protein (RAP and RAB)-mediated signaling pathway
  JOURNAL   Genomics 90 (2), 249-260 (2007)
   PUBMED   17509819
  REMARK    GeneRIF: Identification of novel protein SGSM1 which modulate small
            G protein (RAP and RAB)-mediated signaling pathway.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP000359.1, AW028652.1, AB275761.1, BM930881.1 and AL050312.8.
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon, and includes an alternate in-frame exon, compared to variant
            1, resulting in a shorter protein (isoform 3), compared to isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB275761.1, SRR1803611.109626.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000400358.9/ ENSP00000383211.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.23"
     Protein         1..1093
                     /product="small G protein signaling modulator 1 isoform 3"
                     /note="RUN and TBC1 domain containing 2; small G protein
                     signaling modulator 1 protein; RUN and TBC1
                     domain-containing protein 2"
                     /calculated_mol_wt=123709
     Region          20..196
                     /region_name="RUN_SGSM1"
                     /note="RUN domain found in small G protein signaling
                     modulator 1 (SGSM1) and similar proteins; cd17703"
                     /db_xref="CDD:439065"
     Region          254..425
                     /region_name="PH_RUTBC"
                     /note="Rab-binding Pleckstrin homology domain (PH) of
                     small G-protein signaling modulator 1 and similar
                     proteins; cd15784"
                     /db_xref="CDD:275431"
     Region          <881..1050
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     CDS             1..1093
                     /gene="SGSM1"
                     /gene_synonym="RUTBC2"
                     /coded_by="NM_001098497.3:116..3397"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS46675.1"
                     /db_xref="GeneID:129049"
                     /db_xref="HGNC:HGNC:29410"
                     /db_xref="MIM:611417"
ORIGIN      
        1 masapaeaet rqrllrtvkk evkqimeeav trkfvhedss hiisfcaave acvlhglrrr
       61 aagflrsnki aalfmkvgkn fppaedlsrk vqdleqlies arnqiqglqe nvrklpklpn
      121 lsplaikhlw irtalfekvl dkivhylven sskyyekeal lmdpvdgpil asllvgpcal
      181 eytkmktadh fwtdpsadel vqrhrihssh vrqdsptkrp alciqkrhss gsmddrpsls
      241 ardyveslhq nsratllygk nnvlvqprdd meavpgylsl hqtadvmtlk wtpnqlmngs
      301 vgdldyeksv ywdyamtirl eeivylhchq qvdsggtvvl vsqdgiqrpp frfpkgghll
      361 qflsclengl lphgqldppl wsqrgkgkvf pklrkrspqg saestssdkd ddeatdyvfr
      421 iiypgmqsef vpqdlmdvsv snlpslwqps prksscsscs qsgsadgsst ngcnherapl
      481 kllcdnmkyq ilsrafygwl aycrhlstvr thlsalvnhm ivspdlpcda gqgltariwe
      541 qylhdstsye eqellrliyy ggiqpeirka vwpfllghyq fgmteterke vdeqihacya
      601 qtmaewlgce aivrqreres haaalakcss gasldshlhr mlhrdstisn essqscssgr
      661 qnirlhsdss sstqvfesvd eveqveaegr leekqpkipn gnlvngtcsp dsghpsshnf
      721 ssglsehsep slstedsvld aqrntptvlr prdgsvddrq sseattsqde apreelavqd
      781 slesdllane smdefmsitg sldmalpekd dvvmegwrss etekhgqads ednlseepem
      841 eslfpalasl avttsanevs pvsssgvtys pelldlytvn lhriekdvqr cdrnywyftp
      901 anleklrnim csyiwqhiei gyvqgmcdll apllvildde alafscftel mkrmnqnfph
      961 ggamdthfan mrsliqilds elfelmhqng dythfyfcyr wflldfkrel vyddvflvwe
     1021 tiwaakhvss ahyvlfiala lvevyrdiil ennmdftdii kffnemaerh ntkqvlklar
     1081 dlvykvqtli enk
//
LOCUS       NP_000717                520 aa            linear   PRI 21-NOV-2025
DEFINITION  voltage-dependent L-type calcium channel subunit beta-4 isoform b
            [Homo sapiens].
ACCESSION   NP_000717
VERSION     NP_000717.2
DBSOURCE    REFSEQ: accession NM_000726.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Westhoff,M. and Dixon,R.E.
  TITLE     Mechanisms and Regulation of Cardiac CaV1.2 Trafficking
  JOURNAL   Int J Mol Sci 22 (11), 5927 (2021)
   PUBMED   34072954
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Coste de Bagneaux,P., von Elsner,L., Bierhals,T., Campiglio,M.,
            Johannsen,J., Obermair,G.J., Hempel,M., Flucher,B.E. and Kutsche,K.
  TITLE     A homozygous missense variant in CACNB4 encoding the auxiliary
            calcium channel beta4 subunit causes a severe neurodevelopmental
            disorder and impairs channel and non-channel functions
  JOURNAL   PLoS Genet 16 (3), e1008625 (2020)
   PUBMED   32176688
  REMARK    GeneRIF: The homozygous CACNB4 p.(Leu126Pro) variant underlies the
            severe neurological phenotype in the two siblings.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Vendel,A.C., Terry,M.D., Striegel,A.R., Iverson,N.M.,
            Leuranguer,V., Rithner,C.D., Lyons,B.A., Pickard,G.E., Tobet,S.A.
            and Horne,W.A.
  TITLE     Alternative splicing of the voltage-gated Ca2+ channel beta4
            subunit creates a uniquely folded N-terminal protein binding domain
            with cell-specific expression in the cerebellar cortex
  JOURNAL   J Neurosci 26 (10), 2635-2644 (2006)
   PUBMED   16525042
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Helton,T.D. and Horne,W.A.
  TITLE     Alternative splicing of the beta 4 subunit has alpha1 subunit
            subtype-specific effects on Ca2+ channel gating
  JOURNAL   J Neurosci 22 (5), 1573-1582 (2002)
   PUBMED   11880487
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Escayg,A., Jones,J.M., Kearney,J.A., Hitchcock,P.F. and
            Meisler,M.H.
  TITLE     Calcium channel beta 4 (CACNB4): human ortholog of the mouse
            epilepsy gene lethargic
  JOURNAL   Genomics 50 (1), 14-22 (1998)
   PUBMED   9628818
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Burgess,D.L., Jones,J.M., Meisler,M.H. and Noebels,J.L.
  TITLE     Mutation of the Ca2+ channel beta subunit gene Cchb4 is associated
            with ataxia and seizures in the lethargic (lh) mouse
  JOURNAL   Cell 88 (3), 385-392 (1997)
   PUBMED   9039265
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Diriong,S., Lory,P., Williams,M.E., Ellis,S.B., Harpold,M.M. and
            Taviaux,S.
  TITLE     Chromosomal localization of the human genes for alpha 1A, alpha 1B,
            and alpha 1E voltage-dependent Ca2+ channel subunits
  JOURNAL   Genomics 30 (3), 605-609 (1995)
   PUBMED   8825650
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Spacey,S.
  TITLE     Episodic Ataxia Type 2 - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301674
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079790.6, BC075049.2,
            AC097448.2 and T23939.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 23, 2004 this sequence version replaced NP_000717.1.
            
            Summary: This gene encodes a member of the beta subunit family of
            voltage-dependent calcium channel complex proteins. Calcium
            channels mediate the influx of calcium ions into the cell upon
            membrane polarization and consist of a complex of alpha-1,
            alpha-2/delta, beta, and gamma subunits in a 1:1:1:1 ratio. Various
            versions of each of these subunits exist, either expressed from
            similar genes or the result of alternative splicing. The protein
            encoded by this locus plays an important role in calcium channel
            function by modulating G protein inhibition, increasing peak
            calcium current, controlling the alpha-1 subunit membrane targeting
            and shifting the voltage dependence of activation and inactivation.
            Certain mutations in this gene have been associated with idiopathic
            generalized epilepsy (IGE), juvenile myoclonic epilepsy (JME), and
            episodic ataxia, type 5. [provided by RefSeq, Aug 2016].
            
            Transcript Variant: This variant (2) encodes the longest isoform
            (b). This isoform has a b-type N-terminus.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.243248.1,
                                           SRR1660809.12727.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000539935.7/ ENSP00000438949.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q23.3"
     Protein         1..520
                     /product="voltage-dependent L-type calcium channel subunit
                     beta-4 isoform b"
                     /note="dihydropyridine-sensitive L-type, calcium channel
                     beta-4 subunit; voltage-dependent L-type calcium channel
                     subunit beta-4; calcium channel voltage-dependent subunit
                     beta 4"
                     /calculated_mol_wt=58038
     Region          1..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00305.2)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D4A055; propagated from
                     UniProtKB/Swiss-Prot (O00305.2)"
     Region          50..91
                     /region_name="VGCC_beta4Aa_N"
                     /note="Voltage gated calcium channel subunit beta domain
                     4Aa N terminal; pfam12052"
                     /db_xref="CDD:463445"
     Region          91..158
                     /region_name="SH3_CACNB4"
                     /note="Src Homology 3 domain of Voltage-dependent L-type
                     calcium channel subunit beta4; cd12043"
                     /db_xref="CDD:212976"
     Site            order(101,103,106,117,135..136,152,154..155)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212976"
     Region          166..185
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00305.2)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0S4; propagated from
                     UniProtKB/Swiss-Prot (O00305.2)"
     Region          218..398
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0S4; propagated from
                     UniProtKB/Swiss-Prot (O00305.2)"
     Region          425..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00305.2)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D4A055; propagated from
                     UniProtKB/Swiss-Prot (O00305.2)"
     Site            506
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8R0S4; propagated from
                     UniProtKB/Swiss-Prot (O00305.2)"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D4A055; propagated from
                     UniProtKB/Swiss-Prot (O00305.2)"
     CDS             1..520
                     /gene="CACNB4"
                     /gene_synonym="CAB4; CACNLB4; EA5; EIG9; EJM; EJM4; EJM6"
                     /coded_by="NM_000726.5:34..1596"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS46426.1"
                     /db_xref="GeneID:785"
                     /db_xref="HGNC:HGNC:1404"
                     /db_xref="MIM:601949"
ORIGIN      
        1 mssssyakng tadgphspts qvargtttrr srlkrsdgst tstsfilrqg sadsytsrps
       61 dsdvsleedr eairqereqq aaiqleraks kpvafavktn vsycgalded vpvpstaisf
      121 dakdflhike kynndwwigr lvkegceigf ipsplrleni riqqeqkrgr fhggkssgns
      181 ssslgemvsg tfratptsta kqkqkvtehi ppydvvpsmr pvvlvgpslk gyevtdmmqk
      241 alfdflkhrf dgrisitrvt adislakrsv lnnpskraii ersntrssla evqseierif
      301 elarslqlvv ldadtinhpa qliktslapi ivhvkvsspk vlqrliksrg ksqskhlnvq
      361 lvaadklaqc ppemfdvild enqledaceh lgeyleaywr athttsstpm tpllgrnlgs
      421 talspyptai sglqsqrmrh snhstenspi errslmtsde nyhnerarks rnrlssssqh
      481 srdhyplvee dypdsyqdty kphrnrgspg gyshdsrhrl
//
LOCUS       NP_001317211             218 aa            linear   PRI 21-NOV-2025
DEFINITION  mitotic-spindle organizing protein 2B isoform 1 [Homo sapiens].
ACCESSION   NP_001317211 XP_011510190
VERSION     NP_001317211.1
DBSOURCE    REFSEQ: accession NM_001330282.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Serna,M., Zimmermann,F., Vineethakumari,C., Gonzalez-Rodriguez,N.,
            Llorca,O. and Luders,J.
  TITLE     CDK5RAP2 activates microtubule nucleator gammaTuRC by facilitating
            template formation and actin release
  JOURNAL   Dev Cell 59 (23), 3175-3188 (2024)
   PUBMED   39321809
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Wieczorek,M., Huang,T.L., Urnavicius,L., Hsia,K.C. and Kapoor,T.M.
  TITLE     MZT Proteins Form Multi-Faceted Structural Modules in the
            gamma-Tubulin Ring Complex
  JOURNAL   Cell Rep 31 (13), 107791 (2020)
   PUBMED   32610146
  REMARK    GeneRIF: MZT Proteins Form Multi-Faceted Structural Modules in the
            gamma-Tubulin Ring Complex.
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Liu,X., Salokas,K., Tamene,F., Jiu,Y., Weldatsadik,R.G., Ohman,T.
            and Varjosalo,M.
  TITLE     An AP-MS- and BioID-compatible MAC-tag enables comprehensive
            mapping of protein interactions and subcellular localizations
  JOURNAL   Nat Commun 9 (1), 1188 (2018)
   PUBMED   29568061
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Hutchins,J.R., Toyoda,Y., Hegemann,B., Poser,I., Heriche,J.K.,
            Sykora,M.M., Augsburg,M., Hudecz,O., Buschhorn,B.A., Bulkescher,J.,
            Conrad,C., Comartin,D., Schleiffer,A., Sarov,M., Pozniakovsky,A.,
            Slabicki,M.M., Schloissnig,S., Steinmacher,I., Leuschner,M.,
            Ssykor,A., Lawo,S., Pelletier,L., Stark,H., Nasmyth,K.,
            Ellenberg,J., Durbin,R., Buchholz,F., Mechtler,K., Hyman,A.A. and
            Peters,J.M.
  TITLE     Systematic analysis of human protein complexes identifies
            chromosome segregation proteins
  JOURNAL   Science 328 (5978), 593-599 (2010)
   PUBMED   20360068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC018804.9.
            
            On Aug 20, 2016 this sequence version replaced XP_011510190.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410571.69583.1,
                                           SRR7410570.207731.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144835
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q21.1"
     Protein         1..218
                     /product="mitotic-spindle organizing protein 2B isoform 1"
                     /note="mitotic-spindle organizing protein associated with
                     a ring of gamma-tubulin 2B; family with sequence
                     similarity 128, member B"
                     /calculated_mol_wt=22150
     Region          9..96
                     /region_name="MOZART2"
                     /note="Mitotic-spindle organizing gamma-tubulin ring
                     associated; pfam12926"
                     /db_xref="CDD:432879"
     Region          <84..>214
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     CDS             1..218
                     /gene="MZT2B"
                     /gene_synonym="FAM128B; MOZART2B"
                     /coded_by="NM_001330282.2:22..678"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS82511.1"
                     /db_xref="GeneID:80097"
                     /db_xref="HGNC:HGNC:25886"
                     /db_xref="MIM:613450"
ORIGIN      
        1 maaqgvgpgp gsaappglea arqklalrrk kvlsteemel yelaqaagga idpdvfkilv
       61 dllklnvapl avfqmlksmc agqrlasepq dpaavslpts svpetreasf lsarnssppa
      121 rpsfssspqp aaspvllhsp aathsplspg ppgslrlscc lfspfagrnk gsaalggala
      181 laerssregs sqrmprqpsa trlpkgggpg ksptrgst
//
LOCUS       NP_001341630            1997 aa            linear   PRI 21-NOV-2025
DEFINITION  sodium channel protein type 5 subunit alpha isoform g [Homo
            sapiens].
ACCESSION   NP_001341630
VERSION     NP_001341630.1
DBSOURCE    REFSEQ: accession NM_001354701.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1997)
  AUTHORS   Hu,Y., Zhang,C., Wang,S., Xiong,H., Xie,W., Zeng,Z., Cai,H.,
            Wang,Q.K. and Lu,Z.
  TITLE     14-3-3epsilon/YWHAE regulates the transcriptional expression of
            cardiac sodium channel NaV1.5
  JOURNAL   Heart Rhythm 21 (11), 2320-2329 (2024)
   PUBMED   38750908
  REMARK    GeneRIF: 14-3-3epsilon/YWHAE regulates the transcriptional
            expression of cardiac sodium channel NaV1.5.
REFERENCE   2  (residues 1 to 1997)
  AUTHORS   Cadena-Ullauri,S., Guevara-Ramirez,P., Ruiz-Pozo,V.A.,
            Tamayo-Trujillo,R., Paz-Cruz,E., Simancas-Racines,D.,
            Ibarra-Castillo,R., Laso-Bayas,J.L. and Zambrano,A.K.
  TITLE     Genomic analysis of an Ecuadorian individual carrying an SCN5A rare
            variant
  JOURNAL   BMC Cardiovasc Disord 24 (1), 388 (2024)
   PUBMED   39068398
  REMARK    GeneRIF: Genomic analysis of an Ecuadorian individual carrying an
            SCN5A rare variant.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1997)
  AUTHORS   Tariq,U., Sarkar,S., Malladi,N., Kumar,R., Bugga,P., Chakraborty,P.
            and Banerjee,S.K.
  TITLE     Knockdown of SCN5A alters metabolic-associated genes and aggravates
            hypertrophy in the cardiomyoblast
  JOURNAL   Mol Biol Rep 51 (1), 661 (2024)
   PUBMED   38758505
  REMARK    GeneRIF: Knockdown of SCN5A alters metabolic-associated genes and
            aggravates hypertrophy in the cardiomyoblast.
            Erratum:[Mol Biol Rep. 2024 Jul 26;51(1):852. doi:
            10.1007/s11033-024-09742-9. PMID: 39060789]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1997)
  AUTHORS   Wright,K.M., Nathan,S., Jiang,H., Xia,W., Kim,H., Chakouri,N.,
            Nwafor,J.N., Fossier,L., Srinivasan,L., Chen,Z., Boronina,T.,
            Post,J., Paul,S., Cole,R.N., Ben-Johny,M., Cole,P.A. and
            Gabelli,S.B.
  TITLE     NEDD4L intramolecular interactions regulate its auto and substrate
            NaV1.5 ubiquitination
  JOURNAL   J Biol Chem 300 (3), 105715 (2024)
   PUBMED   38309503
  REMARK    GeneRIF: NEDD4L intramolecular interactions regulate its auto and
            substrate NaV1.5 ubiquitination.
REFERENCE   5  (residues 1 to 1997)
  AUTHORS   George,A.L. Jr., Varkony,T.A., Drabkin,H.A., Han,J., Knops,J.F.,
            Finley,W.H., Brown,G.B., Ward,D.C. and Haas,M.
  TITLE     Assignment of the human heart tetrodotoxin-resistant voltage-gated
            Na+ channel alpha-subunit gene (SCN5A) to band 3p21
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 67-70 (1995)
   PUBMED   7956363
REFERENCE   6  (residues 1 to 1997)
  AUTHORS   Jiang,C., Atkinson,D., Towbin,J.A., Splawski,I., Lehmann,M.H.,
            Li,H., Timothy,K., Taggart,R.T., Schwartz,P.J., Vincent,G.M. et al.
  TITLE     Two long QT syndrome loci map to chromosomes 3 and 7 with evidence
            for further heterogeneity
  JOURNAL   Nat Genet 8 (2), 141-147 (1994)
   PUBMED   7842012
REFERENCE   7  (residues 1 to 1997)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   8  (residues 1 to 1997)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 1997)
  AUTHORS   Groffen,A.J., Bikker,H. and Christiaans,I.
  TITLE     Long QT Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301308
REFERENCE   10 (residues 1 to 1997)
  AUTHORS   Gellens,M.E., George,A.L. Jr., Chen,L.Q., Chahine,M., Horn,R.,
            Barchi,R.L. and Kallen,R.G.
  TITLE     Primary structure and functional expression of the human cardiac
            tetrodotoxin-insensitive voltage-dependent sodium channel
  JOURNAL   Proc Natl Acad Sci U S A 89 (2), 554-558 (1992)
   PUBMED   1309946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP006241.1.
            
            Summary: The protein encoded by this gene is an integral membrane
            protein and tetrodotoxin-resistant voltage-gated sodium channel
            subunit. This protein is found primarily in cardiac muscle and is
            responsible for the initial upstroke of the action potential in an
            electrocardiogram. Defects in this gene have been associated with
            long QT syndrome type 3 (LQT3), atrial fibrillation,
            cardiomyopathy, and Brugada syndrome 1, all autosomal dominant
            cardiac diseases. Alternative splicing results in several
            transcript variants encoding different isoforms. [provided by
            RefSeq, May 2022].
            
            Transcript Variant: This variant (7) lacks two alternate coding
            exons, contains another alternate coding exon, and uses an
            alternate in-frame splice junction compared to variant 1. The
            resulting isoform (g) has the same N- and C-termini but is shorter
            compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: KC858891.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1968189,
                                    SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1997
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.2"
     Protein         1..1997
                     /product="sodium channel protein type 5 subunit alpha
                     isoform g"
                     /note="cardiac tetrodotoxin-insensitive voltage-dependent
                     sodium channel alpha subunit; sodium channel protein type
                     5 subunit alpha; voltage-gated sodium channel subunit
                     alpha Nav1.5; sodium channel protein cardiac muscle
                     subunit alpha; sodium channel, voltage-gated, type V,
                     alpha subunit"
                     /calculated_mol_wt=224683
     Region          28..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Region          113..420
                     /region_name="I. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          130..423
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            130..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            158..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            189..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            214
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            217..236
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            250..272
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            283
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            288
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            291
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            318
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:P15389; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            328
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            387..413
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            457
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Region          461..591
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P15389; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Region          507..667
                     /region_name="Na_trans_cytopl"
                     /note="Cytoplasmic domain of voltage-gated Na+ ion
                     channel; pfam11933"
                     /db_xref="CDD:463401"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            513
                     /site_type="methylation"
                     /note="Dimethylated arginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            526
                     /site_type="methylation"
                     /note="Dimethylated arginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JJV9; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            680
                     /site_type="methylation"
                     /note="Dimethylated arginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Region          699..969
                     /region_name="II. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          716..927
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            720..737
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            740
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            747..769
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            776..796
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            803
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            807..821
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            839..860
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            864
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            913..941
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          953..1199
                     /region_name="Na_trans_assoc"
                     /note="Sodium ion transport-associated; pfam06512"
                     /db_xref="CDD:461936"
     Region          1203..1460
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1203..1224
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1236..1258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1268..1290
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1297..1316
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1330..1354
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1364
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1373
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1379
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1387
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1427..1451
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          1452..1504
                     /region_name="Na_channel_gate"
                     /note="Inactivation gate of the voltage-gated sodium
                     channel alpha subunits; cd13433"
                     /db_xref="CDD:240441"
     Site            1466..1469
                     /site_type="other"
                     /note="putative hydrophobic latch"
                     /db_xref="CDD:240441"
     Site            1484
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000305|PubMed:19666841; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Region          1491..1788
                     /region_name="IV. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          1509..1763
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1510..1528
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1540..1561
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1571..1593
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1601..1621
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1632..1660
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1717
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            1727..1752
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          1820..1882
                     /region_name="Interaction with FGF13.
                     /evidence=ECO:0000269|PubMed:22705208"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          1940..1997
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          1955..1958
                     /region_name="Interaction with NEDD4, NEDD4L and WWP2.
                     /evidence=ECO:0000269|PubMed:15548568"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     CDS             1..1997
                     /gene="SCN5A"
                     /gene_synonym="CDCD2; CMD1E; CMPD2; HB1; HB2; HBBD; HH1;
                     ICCD; IVF; LQT3; Nav1.5; PFHB1; SSS1; VF1"
                     /coded_by="NM_001354701.2:210..6203"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="GeneID:6331"
                     /db_xref="HGNC:HGNC:10593"
                     /db_xref="MIM:600163"
ORIGIN      
        1 manfllprgt ssfrrftres laaiekrmae kqargsttlq esreglpeee aprpqldlqa
       61 skklpdlygn ppqeligepl edldpfystq ktfivlnkgk tifrfsatna lyvlspfhpi
      121 rraavkilvh slfnmlimct iltncvfmaq hdpppwtkyv eytftaiytf eslvkilarg
      181 fclhaftflr dpwnwldfsv iimayvseni klgnlsalrt frvlralkti svipglktiv
      241 galiqsvkkl advmvltvfc lsvfaliglq lfmgnlrhkc vrnftalngt ngsveadglv
      301 wesldlylsd penyllkngt sdvllcgnss dagtcpegyr clkagenpdh gytsfdsfaw
      361 aflalfrlmt qdcwerlyqq tlrsagkiym iffmlviflg sfylvnlila vvamayeeqn
      421 qatiaeteek ekrfqeamem lkkehealti rgvdtvsrss lemsplapvn sherrskrrk
      481 rmssgteecg edrlpksdse dgpramnhls ltrglsrtsm kprssrgsif tfrrrdlgse
      541 adfaddenst ageseshhts llvpwplrrt saqgqpspgt sapghalhgk knstvdcngv
      601 vsllgagdpe atspgshllr pvmlehppdt ttpseepggp qmltsqapcv dgfeepgarq
      661 ralsavsvlt saleeleesr hkcppcwnrl aqryliwecc plwmsikqgv klvvmdpftd
      721 ltitmcivln tlfmalehyn mtsefeemlq vgnlvftgif taemtfkiia ldpyyyfqqg
      781 wnifdsiivi lslmelglsr msnlsvlrsf rllrvfklak swptlntlik iignsvgalg
      841 nltlvlaiiv fifavvgmql fgknyselrd sdsgllprwh mmdffhafli ifrilcgewi
      901 etmwdcmevs gqslcllvfl lvmvignlvv lnlflallls sfsadnltap dedremnnlq
      961 lalariqrgl rfvkrttwdf ccgllrqrpq kpaalaaqgq lpsciatpys ppppetekvp
     1021 ptrketrfee geqpgqgtpg dpepvcvpia vaesdtddqe edeenslgte eesskqesqp
     1081 vsggpeappd srtwsqvsat asseaeasas qadwrqqwka epqapgcget pedscsegst
     1141 admtntaell eqipdlgqdv kdpedcfteg cvrrcpccav dttqapgkvw wrlrktcyhi
     1201 vehswfetfi ifmillssga lafediylee rktikvlley adkmftyvfv lemllkwvay
     1261 gfkkyftnaw cwldflivdv slvslvantl gfaemgpiks lrtlralrpl ralsrfegmr
     1321 vvvnalvgai psimnvllvc lifwlifsim gvnlfagkfg rcinqtegdl plnytivnnk
     1381 sqceslnltg elywtkvkvn fdnvgagyla llqvyeeqpq weynlymyiy fvifiifgsf
     1441 ftlnlfigvi idnfnqqkkk lggqdifmte eqkkyynamk klgskkpqkp iprplnkyqg
     1501 fifdivtkqa fdvtimflic lnmvtmmvet ddqspekini lakinllfva iftgecivkl
     1561 aalrhyyftn swnifdfvvv ilsivgtvls diiqkyffsp tlfrvirlar igrilrlirg
     1621 akgirtllfa lmmslpalfn iglllflvmf iysifgmanf ayvkweagid dmfnfqtfan
     1681 smlclfqitt sagwdgllsp ilntgppycd ptlpnsngsr gdcgspavgi lffttyiiis
     1741 flivvnmyia iilenfsvat eesteplsed dfdmfyeiwe kfdpeatqfi eysvlsdfad
     1801 alseplriak pnqislinmd lpmvsgdrih cmdilfaftk rvlgesgemd alkiqmeekf
     1861 maanpskisy epitttlrrk heevsamviq rafrrhllqr slkhasflfr qqagsglsee
     1921 dapereglia yvmsenfsrp lgppssssis stsfppsyds vtratsdnlq vrgsdyshse
     1981 dladfppspd rdresiv
//
LOCUS       NP_001156787             701 aa            linear   PRI 21-NOV-2025
DEFINITION  F-box/LRR-repeat protein 17 [Homo sapiens].
ACCESSION   NP_001156787
VERSION     NP_001156787.2
DBSOURCE    REFSEQ: accession NM_001163315.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 701)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 701)
  AUTHORS   Kang,H.M., Kim,D.H., Kim,M., Min,Y., Jeong,B., Noh,K.H., Lee,D.Y.,
            Cho,H.S., Kim,N.S., Jung,C.R. and Lim,J.H.
  TITLE     FBXL17/spastin axis as a novel therapeutic target of hereditary
            spastic paraplegia
  JOURNAL   Cell Biosci 12 (1), 110 (2022)
   PUBMED   35869491
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 701)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 701)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   5  (residues 1 to 701)
  AUTHORS   Mena,E.L., Jevtic,P., Greber,B.J., Gee,C.L., Lew,B.G., Akopian,D.,
            Nogales,E., Kuriyan,J. and Rape,M.
  TITLE     Structural basis for dimerization quality control
  JOURNAL   Nature 586 (7829), 452-456 (2020)
   PUBMED   32814905
  REMARK    GeneRIF: Structural basis for dimerization quality control.
REFERENCE   6  (residues 1 to 701)
  AUTHORS   Candille,S.I., Absher,D.M., Beleza,S., Bauchet,M., McEvoy,B.,
            Garrison,N.A., Li,J.Z., Myers,R.M., Barsh,G.S., Tang,H. and
            Shriver,M.D.
  TITLE     Genome-wide association studies of quantitatively measured skin,
            hair, and eye pigmentation in four European populations
  JOURNAL   PLoS One 7 (10), e48294 (2012)
   PUBMED   23118974
REFERENCE   7  (residues 1 to 701)
  AUTHORS   Hart,A.B., Engelhardt,B.E., Wardle,M.C., Sokoloff,G., Stephens,M.,
            de Wit,H. and Palmer,A.A.
  TITLE     Genome-wide association study of d-amphetamine response in healthy
            volunteers identifies putative associations, including cadherin 13
            (CDH13)
  JOURNAL   PLoS One 7 (8), e42646 (2012)
   PUBMED   22952603
REFERENCE   8  (residues 1 to 701)
  AUTHORS   Ichikawa,S., Koller,D.L., Padgett,L.R., Lai,D., Hui,S.L.,
            Peacock,M., Foroud,T. and Econs,M.J.
  TITLE     Replication of previous genome-wide association studies of bone
            mineral density in premenopausal American women
  JOURNAL   J Bone Miner Res 25 (8), 1821-1829 (2010)
   PUBMED   20200978
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 701)
  AUTHORS   Xiao,G.G., Zhou,B.S., Somlo,G., Portnow,J., Juhasz,A., Un,F.,
            Chew,H., Gandara,D. and Yen,Y.
  TITLE     Identification of F-box/LLR-repeated protein 17 as potential useful
            biomarker for breast cancer therapy
  JOURNAL   Cancer Genomics Proteomics 5 (3-4), 151-160 (2008)
   PUBMED   18820369
  REMARK    GeneRIF: F-box protein 17 (FBXL17) can serve as a therapeutic
            target and surrogate marker for breast cancer therapy.
            Erratum:[Cancer Genomics Proteomics. 2010 May-Jun;7(3):171]
REFERENCE   10 (residues 1 to 701)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008462.6, AC092274.2, AC008513.7 and AC011419.7.
            
            On Aug 8, 2009 this sequence version replaced NP_001156787.1.
            
            Summary: Members of the F-box protein family, such as FBXL17, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3929799.1,
                                           SRR14038191.2795187.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000542267.7/ ENSP00000437464.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..701
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q21.3"
     Protein         1..701
                     /product="F-box/LRR-repeat protein 17"
                     /note="F-box only protein 13"
                     /calculated_mol_wt=75564
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UF56.3)"
     Region          72..94
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UF56.3)"
     Region          227..300
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UF56.3)"
     Region          320..368
                     /region_name="F-box_FBXO13"
                     /note="F-box domain found in F-box only protein 13
                     (FBXO13) and similar proteins; cd22092"
                     /db_xref="CDD:438864"
     Site            order(324,328,331..332,335..336,340,342..343,348..350,352)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438864"
     Region          362..387
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          388..413
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          411..573
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          414..439
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          440..465
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          466..491
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          492..517
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          542..567
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          547..>660
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          568..618
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          619..644
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          645..670
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..701
                     /gene="FBXL17"
                     /gene_synonym="Fbl17; Fbx13; FBXO13"
                     /coded_by="NM_001163315.3:408..2513"
                     /db_xref="CCDS:CCDS54886.1"
                     /db_xref="GeneID:64839"
                     /db_xref="HGNC:HGNC:13615"
                     /db_xref="MIM:609083"
ORIGIN      
        1 mghllskepr nrpsqkrprc cswcrrrrpl lrlprrtpak vppqpaaprs rdcffrgpcm
       61 lcfivhspga papagpeeep plsppprdga yaaasssqhl arryaalaae dcaaaarrfl
      121 lssaaaaaaa aasasspasc ckelglaaaa aweqqgrslf laslgpvrfl gppaavqlfr
      181 gptpspaelp tppemvckrk gagvpactpc kqprcggggc gggggggggg gpagggaspp
      241 rppdagccqa peqppqplcp ppssptsega pteaggdavr aggtaplsaq qqhecgdadc
      301 respenpcdc hrepppetpd inqlppsill kifsnlslde rclsaslvck ywrdlcldfq
      361 fwkqldlssr qqvtdellek iasrsqniie inisdcrsms dngvcvlafk cpgllrytay
      421 rckqlsdtsi iavashcpll qkvhvgnqdk ltdeglkqlg skcrelkdih fgqcykisde
      481 gmiviakgcl klqriymqen klvtdqsvka faehcpelqy vgfmgcsvts kgvihltklr
      541 nlssldlrhi teldnetvme ivkrcknlss lnlclnwiin drcveviake gqnlkelylv
      601 sckitdyali aigrysmtie tvdvgwckei tdqgatliaq sskslrylgl mrcdkvnevt
      661 veqlvqqyph itfstvlqdc krtlerayqm gwtpnmsaas s
//
LOCUS       NP_001155136             600 aa            linear   PRI 21-NOV-2025
DEFINITION  radial spoke head protein 4 homolog A isoform 2 [Homo sapiens].
ACCESSION   NP_001155136
VERSION     NP_001155136.1
DBSOURCE    REFSEQ: accession NM_001161664.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   De Jesus-Rojas,W., Melendez-Montanez,J., Muniz-Hernandez,J.,
            Marra-Nazario,A., Alvarado-Huerta,F., Santos-Lopez,A.,
            Ramos-Benitez,M.J. and Mosquera,R.A.
  TITLE     The RSPH4A Gene in Primary Ciliary Dyskinesia
  JOURNAL   Int J Mol Sci 24 (3), 1936 (2023)
   PUBMED   36768259
  REMARK    GeneRIF: The RSPH4A Gene in Primary Ciliary Dyskinesia.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Zhang,X., Xiao,Z., Zhang,J., Xu,C., Liu,S., Cheng,L., Zhou,S.,
            Zhao,S., Zhang,Y., Wu,J., Wang,Y. and Liu,M.
  TITLE     Differential requirements of IQUB for the assembly of radial spoke
            1 and the motility of mouse cilia and flagella
  JOURNAL   Cell Rep 41 (8), 111683 (2022)
   PUBMED   36417862
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Zhao,Y., Pinskey,J., Lin,J., Yin,W., Sears,P.R., Daniels,L.A.,
            Zariwala,M.A., Knowles,M.R., Ostrowski,L.E. and Nicastro,D.
  TITLE     Structural insights into the cause of human RSPH4A primary ciliary
            dyskinesia
  JOURNAL   Mol Biol Cell 32 (12), 1202-1209 (2021)
   PUBMED   33852348
  REMARK    GeneRIF: Structural insights into the cause of human RSPH4A primary
            ciliary dyskinesia.
REFERENCE   4  (residues 1 to 600)
  AUTHORS   Takeuchi,K., Kitano,M., Kiyotoshi,H., Ikegami,K., Ogawa,S.,
            Ikejiri,M., Nagao,M., Fujisawa,T. and Nakatani,K.
  TITLE     A targeted next-generation sequencing panel reveals novel mutations
            in Japanese patients with primary ciliary dyskinesia
  JOURNAL   Auris Nasus Larynx 45 (3), 585-591 (2018)
   PUBMED   28939216
  REMARK    GeneRIF: A novel mutation causing primary ciliary dyskinesia was
            found in Japanese patients.
REFERENCE   5  (residues 1 to 600)
  AUTHORS   Frommer,A., Hjeij,R., Loges,N.T., Edelbusch,C., Jahnke,C.,
            Raidt,J., Werner,C., Wallmeier,J., Grosse-Onnebrink,J., Olbrich,H.,
            Cindric,S., Jaspers,M., Boon,M., Memari,Y., Durbin,R.,
            Kolb-Kokocinski,A., Sauer,S., Marthin,J.K., Nielsen,K.G.,
            Amirav,I., Elias,N., Kerem,E., Shoseyov,D., Haeffner,K. and
            Omran,H.
  TITLE     Immunofluorescence Analysis and Diagnosis of Primary Ciliary
            Dyskinesia with Radial Spoke Defects
  JOURNAL   Am J Respir Cell Mol Biol 53 (4), 563-573 (2015)
   PUBMED   25789548
  REMARK    GeneRIF: Absence of RSPH4A due to mutations in RSPH4A results in
            deficient axonemal assembly of the RS head components RSPH1 and
            RSPH9.
REFERENCE   6  (residues 1 to 600)
  AUTHORS   Daniels,M.L., Leigh,M.W., Davis,S.D., Armstrong,M.C., Carson,J.L.,
            Hazucha,M., Dell,S.D., Eriksson,M., Collins,F.S., Knowles,M.R. and
            Zariwala,M.A.
  TITLE     Founder mutation in RSPH4A identified in patients of Hispanic
            descent with primary ciliary dyskinesia
  JOURNAL   Hum Mutat 34 (10), 1352-1356 (2013)
   PUBMED   23798057
  REMARK    GeneRIF: the c.921+3_6delAAGT splice site mutation in RSPH4A is a
            founder mutation that is a common cause of PCD without situs
            abnormalities in patients of Hispanic Puerto Rican descent.
REFERENCE   7  (residues 1 to 600)
  AUTHORS   Antony,D., Becker-Heck,A., Zariwala,M.A., Schmidts,M.,
            Onoufriadis,A., Forouhan,M., Wilson,R., Taylor-Cox,T., Dewar,A.,
            Jackson,C., Goggin,P., Loges,N.T., Olbrich,H., Jaspers,M.,
            Jorissen,M., Leigh,M.W., Wolf,W.E., Daniels,M.L., Noone,P.G.,
            Ferkol,T.W., Sagel,S.D., Rosenfeld,M., Rutman,A., Dixit,A.,
            O'Callaghan,C., Lucas,J.S., Hogg,C., Scambler,P.J., Emes,R.D.,
            Chung,E.M., Shoemark,A., Knowles,M.R., Omran,H. and Mitchison,H.M.
  CONSRTM   Uk10k
  TITLE     Mutations in CCDC39 and CCDC40 are the major cause of primary
            ciliary dyskinesia with axonemal disorganization and absent inner
            dynein arms
  JOURNAL   Hum Mutat 34 (3), 462-472 (2013)
   PUBMED   23255504
REFERENCE   8  (residues 1 to 600)
  AUTHORS   Zietkiewicz,E., Bukowy-Bieryllo,Z., Voelkel,K., Klimek,B.,
            Dmenska,H., Pogorzelski,A., Sulikowska-Rowinska,A., Rutkiewicz,E.
            and Witt,M.
  TITLE     Mutations in radial spoke head genes and ultrastructural cilia
            defects in East-European cohort of primary ciliary dyskinesia
            patients
  JOURNAL   PLoS One 7 (3), e33667 (2012)
   PUBMED   22448264
  REMARK    GeneRIF: Mutations in RSPH4A leads to ultrastructural cilia defects
            and ciliary dyskinesia.
REFERENCE   9  (residues 1 to 600)
  AUTHORS   Castleman,V.H., Romio,L., Chodhari,R., Hirst,R.A., de Castro,S.C.,
            Parker,K.A., Ybot-Gonzalez,P., Emes,R.D., Wilson,S.W., Wallis,C.,
            Johnson,C.A., Herrera,R.J., Rutman,A., Dixon,M., Shoemark,A.,
            Bush,A., Hogg,C., Gardiner,R.M., Reish,O., Greene,N.D.,
            O'Callaghan,C., Purton,S., Chung,E.M. and Mitchison,H.M.
  TITLE     Mutations in radial spoke head protein genes RSPH9 and RSPH4A cause
            primary ciliary dyskinesia with central-microtubular-pair
            abnormalities
  JOURNAL   Am J Hum Genet 84 (2), 197-209 (2009)
   PUBMED   19200523
REFERENCE   10 (residues 1 to 600)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK299754.1, BC106949.2 and
            CB851663.1.
            
            Summary: This gene encodes a protein that appears to be a component
            the radial spoke head, as determined by homology to similar
            proteins in the biflagellate alga Chlamydomonas reinhardtii and
            other ciliates. Radial spokes, which are regularly spaced along
            cilia, sperm, and flagella axonemes, consist of a thin 'stalk' and
            a bulbous 'head' that form a signal transduction scaffold between
            the central pair of microtubules and dynein. Mutations in this gene
            cause primary ciliary dyskinesia 1, a disease arising from
            dysmotility of motile cilia and sperm. Alternative splicing results
            in multiple transcript variants. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (2) is missing an exon in the 3'
            coding region compared to variant 1. This results in a frame-shift,
            and a shorter isoform (2) with a distinct C-terminus compared to
            isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC106949.2, SRR14038197.453963.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145240, SAMEA2158188
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.1"
     Protein         1..600
                     /product="radial spoke head protein 4 homolog A isoform 2"
                     /note="radial spokehead-like 3; radial spoke head protein
                     4 homolog A; radial spoke head-like protein 3; radial
                     spoke head 4 homolog A"
                     /calculated_mol_wt=67275
     Region          1..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5TD94.1)"
     Region          <18..217
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          214..>554
                     /region_name="Radial_spoke"
                     /note="Radial spokehead-like protein; pfam04712"
                     /db_xref="CDD:461405"
     Region          375..410
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5TD94.1)"
     Site            396
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BYM7; propagated from
                     UniProtKB/Swiss-Prot (Q5TD94.1)"
     Region          506..526
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5TD94.1)"
     CDS             1..600
                     /gene="RSPH4A"
                     /gene_synonym="CILD11; dJ412I7.1; RSHL3; RSPH6B"
                     /coded_by="NM_001161664.2:146..1948"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55051.1"
                     /db_xref="GeneID:345895"
                     /db_xref="HGNC:HGNC:21558"
                     /db_xref="MIM:612647"
ORIGIN      
        1 medstspkqe kenqeelget rrpwegktaa spqysepess epleakqgpe tgrqsrssrp
       61 wspqsraktp lggpagpets spapvsprep ssspsplapa rqdlaappqs drttsvipea
      121 gtpypdpleq ssdkrestph htsqsegntf qqsqqpkphl cgrrdvsynn akqkelrfdv
      181 fqeedsnsdy dlqqpapggs evapsmleit iqnakayllk tssnsgfnly dhlsnmltki
      241 lnerpenavd ifenisqdvk mahfskkfda lqnenellpt yeiaekqkal flqghlegvd
      301 qeledeiaen alpnvmesaf yfeqagvglg tdetyrifla lkqltdthpi qrcrfwgkil
      361 glemnyivae vefregedee eveeedvaee rdngeseahe deedelpksf ykapqaipke
      421 esrtgankyv yfvcnepgrp wvklppvipa qiviarkikk fftgrldapi isyppfpgne
      481 snylraqiar isagthvspl gfyqfgeeeg eeeeeaeggr nsfeenpdfe giqvidlves
      541 lsnwvhhvqh ilsqrfriyp pgqhgypqis fhnmllqsfn ptfglehmps pmakslkist
//
LOCUS       NP_001180413             362 aa            linear   PRI 21-NOV-2025
DEFINITION  LIM and senescent cell antigen-like-containing domain protein 1
            isoform e [Homo sapiens].
ACCESSION   NP_001180413
VERSION     NP_001180413.1
DBSOURCE    REFSEQ: accession NM_001193484.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Caliskan,Y., Ozluk,Y., Kurashima,K., Mirioglu,S., Dirim,A.B.,
            Hurdogan,O., Oto,O.A., Syn,M., Nazzal,M., Jain,A., Edwards,J.,
            Yazici,H. and Lentine,K.L.
  TITLE     LIM Zinc Finger Domain Containing 1 Risk Genotype of Recipient Is
            Associated with Renal Tubular Inflammation in Kidney
            Transplantation
  JOURNAL   Genes (Basel) 15 (6), 773 (2024)
   PUBMED   38927709
  REMARK    GeneRIF: LIM Zinc Finger Domain Containing 1 Risk Genotype of
            Recipient Is Associated with Renal Tubular Inflammation in Kidney
            Transplantation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Li,Y., Wang,S., Li,G., Gao,C., Cui,Z., Cong,M., Hu,J., Zhang,M.,
            Jin,X., Sun,H. and Kong,D.
  TITLE     The RNA-binding protein RBMS3 inhibits the progression of colon
            cancer by regulating the stability of LIMS1 mRNA
  JOURNAL   Cancer Med 13 (7), e7129 (2024)
   PUBMED   38618967
  REMARK    GeneRIF: The RNA-binding protein RBMS3 inhibits the progression of
            colon cancer by regulating the stability of LIMS1 mRNA.
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Gorska,A. and Mazur,A.J.
  TITLE     Integrin-linked kinase (ILK): the known vs. the unknown and
            perspectives
  JOURNAL   Cell Mol Life Sci 79 (2), 100 (2022)
   PUBMED   35089438
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   7  (residues 1 to 362)
  AUTHORS   Gubin,A.N., Njoroge,J.M., Bouffard,G.G. and Miller,J.L.
  TITLE     Gene expression in proliferating human erythroid cells
  JOURNAL   Genomics 59 (2), 168-177 (1999)
   PUBMED   10409428
REFERENCE   8  (residues 1 to 362)
  AUTHORS   Tu,Y., Li,F., Goicoechea,S. and Wu,C.
  TITLE     The LIM-only protein PINCH directly interacts with integrin-linked
            kinase and is recruited to integrin-rich sites in spreading cells
  JOURNAL   Mol Cell Biol 19 (3), 2425-2434 (1999)
   PUBMED   10022929
REFERENCE   9  (residues 1 to 362)
  AUTHORS   Tu,Y., Li,F. and Wu,C.
  TITLE     Nck-2, a novel Src homology2/3-containing adaptor protein that
            interacts with the LIM-only protein PINCH and components of growth
            factor receptor kinase-signaling pathways
  JOURNAL   Mol Biol Cell 9 (12), 3367-3382 (1998)
   PUBMED   9843575
REFERENCE   10 (residues 1 to 362)
  AUTHORS   Rearden,A.
  TITLE     A new LIM protein containing an autoepitope homologous to
            'senescent cell antigen'
  JOURNAL   Biochem Biophys Res Commun 201 (3), 1124-1131 (1994)
   PUBMED   7517666
  REMARK    Erratum:[Biochem Biophys Res Commun 2001 Apr 13;282(4):1074]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK304260.1, AF527761.1,
            AC010095.6 and AL110164.1.
            
            Summary: The protein encoded by this gene is an adaptor protein
            which contains five LIM domains, or double zinc fingers. The
            protein is likely involved in integrin signaling through its LIM
            domain-mediated interaction with integrin-linked kinase, found in
            focal adhesion plaques. It is also thought to act as a bridge
            linking integrin-linked kinase to NCK adaptor protein 2, which is
            involved in growth factor receptor kinase signaling pathways. Its
            localization to the periphery of spreading cells also suggests that
            this protein may play a role in integrin-mediated cell adhesion or
            spreading. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.369271.1, AK304260.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q12.3"
     Protein         1..362
                     /product="LIM and senescent cell antigen-like-containing
                     domain protein 1 isoform e"
                     /note="LIM and senescent cell antigen-like-containing
                     domain protein 1; renal carcinoma antigen NY-REN-48; LIM
                     and senescent cell antigen-like domains 1; LIM-type zinc
                     finger domains 1; particularly interesting new Cys-His
                     protein 1"
                     /calculated_mol_wt=41440
     Region          47..105
                     /region_name="LIM1_PINCH"
                     /note="The first LIM domain of protein PINCH; cd09331"
                     /db_xref="CDD:188717"
     Site            order(47,50,69,72,75,78,96,99)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188717"
     Site            order(49..50,52,74,76..80,90..91,93,98..99,101..105)
                     /site_type="other"
                     /note="ILK binding interface"
                     /db_xref="CDD:188717"
     Region          108..159
                     /region_name="LIM2_PINCH"
                     /note="The second LIM domain of protein PINCH; cd09332"
                     /db_xref="CDD:188718"
     Site            order(108,111,128,131,134,137,155,158)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188718"
     Region          172..222
                     /region_name="LIM3_PINCH"
                     /note="The third LIM domain of protein PINCH; cd09333"
                     /db_xref="CDD:188719"
     Site            order(172,175,192,195,198,201,218,221)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188719"
     Region          228..281
                     /region_name="LIM4_PINCH"
                     /note="The fourth LIM domain of protein PINCH; cd09334"
                     /db_xref="CDD:188720"
     Site            order(229,233..236)
                     /site_type="other"
                     /note="N(i)ck binding interface"
                     /db_xref="CDD:188720"
     Site            order(230,233,250,253,256,259,277,280)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188720"
     Region          289..342
                     /region_name="LIM5_PINCH"
                     /note="The fifth LIM domain of protein PINCH; cd09335"
                     /db_xref="CDD:188721"
     Site            order(289,292,309,312,315,318,337,340)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188721"
     CDS             1..362
                     /gene="LIMS1"
                     /gene_synonym="PINCH; PINCH-1; PINCH1"
                     /coded_by="NM_001193484.2:105..1193"
                     /note="isoform e is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS54384.1"
                     /db_xref="GeneID:3987"
                     /db_xref="HGNC:HGNC:6616"
                     /db_xref="MIM:602567"
ORIGIN      
        1 mtalqlkels hsglyrrrrd rpdslrvngl peeelsnman alasatcerc kggfapaeki
       61 vnsngelyhe qcfvcaqcfq qfpeglfyef egrkycehdf qmlfapcchq cgefiigrvi
      121 kamnnswhpe cfrcdlcqev ladigfvkna grhlcrpchn rekarglgky icqkchaiid
      181 eqplifkndp yhpdhfncan cgkeltadar elkgelyclp chdkmgvpic gacrrpiegr
      241 vvnamgkqwh vehfvcakce kpflghrhye rkglayceth ynqlfgdvcf hcnrviegdv
      301 vsalnkawcv ncfacstcnt kltlknkfve fdmkpvckkc yekfplelkk rlkklaetlg
      361 rk
//
LOCUS       NP_002390                381 aa            linear   PRI 21-NOV-2025
DEFINITION  homeobox protein Meis2 isoform f [Homo sapiens].
ACCESSION   NP_002390
VERSION     NP_002390.1
DBSOURCE    REFSEQ: accession NM_002399.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Xiao,Y., Liu,Y., Sun,Y., Huang,C. and Zhong,S.
  TITLE     MEIS2 suppresses breast cancer development by downregulating IL10
  JOURNAL   Cancer Rep (Hoboken) 7 (5), e2064 (2024)
   PUBMED   38711262
  REMARK    GeneRIF: MEIS2 suppresses breast cancer development by
            downregulating IL10.
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Li,D. and Hu,A.
  TITLE     LINC-PINT suppresses breast cancer cell proliferation and migration
            via MEIS2/PPP3CC/NF-kappaB pathway by sponging miR-576-5p
  JOURNAL   Am J Med Sci 367 (3), 201-211 (2024)
   PUBMED   37660994
  REMARK    GeneRIF: LINC-PINT suppresses breast cancer cell proliferation and
            migration via MEIS2/PPP3CC/NF-kappaB pathway by sponging
            miR-576-5p.
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Arunachalam,V., Lea,R., Hoy,W., Lee,S., Mott,S., Savige,J.,
            Mathews,J.D., McMorran,B.J. and Nagaraj,S.H.
  TITLE     Novel genetic markers for chronic kidney disease in a
            geographically isolated population of Indigenous Australians:
            Individual and multiple phenotype genome-wide association study
  JOURNAL   Genome Med 16 (1), 29 (2024)
   PUBMED   38347632
  REMARK    GeneRIF: Novel genetic markers for chronic kidney disease in a
            geographically isolated population of Indigenous Australians:
            Individual and multiple phenotype genome-wide association study.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Xu,H., Chen,S., Li,J., Weng,S., Ren,Y., Zhang,Y., Wang,L., Liu,L.,
            Guo,C., Xing,Z., Luo,P., Cheng,Q., Han,X. and Liu,Z.
  TITLE     Cellular Ligand-Receptor Perturbations Unravel MEIS2 as a Key
            Factor for the Aggressive Progression and Prognosis in Stage II/III
            Colorectal Cancer
  JOURNAL   J Proteome Res 23 (2), 760-774 (2024)
   PUBMED   38153233
  REMARK    GeneRIF: Cellular Ligand-Receptor Perturbations Unravel MEIS2 as a
            Key Factor for the Aggressive Progression and Prognosis in Stage
            II/III Colorectal Cancer.
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Fujino,T., Yamazaki,Y., Largaespada,D.A., Jenkins,N.A.,
            Copeland,N.G., Hirokawa,K. and Nakamura,T.
  TITLE     Inhibition of myeloid differentiation by Hoxa9, Hoxb8, and Meis
            homeobox genes
  JOURNAL   Exp Hematol 29 (7), 856-863 (2001)
   PUBMED   11438208
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Liu,Y., MacDonald,R.J. and Swift,G.H.
  TITLE     DNA binding and transcriptional activation by a PDX1.PBX1b.MEIS2b
            trimer and cooperation with a pancreas-specific basic
            helix-loop-helix complex
  JOURNAL   J Biol Chem 276 (21), 17985-17993 (2001)
   PUBMED   11279116
REFERENCE   8  (residues 1 to 381)
  AUTHORS   Yang,Y., Hwang,C.K., D'Souza,U.M., Lee,S.H., Junn,E. and
            Mouradian,M.M.
  TITLE     Three-amino acid extension loop homeodomain proteins Meis2 and TGIF
            differentially regulate transcription
  JOURNAL   J Biol Chem 275 (27), 20734-20741 (2000)
   PUBMED   10764806
REFERENCE   9  (residues 1 to 381)
  AUTHORS   Smith,J.E., Afonja,O., Yee,H.T., Inghirami,G. and Takeshita,K.
  TITLE     Chromosomal mapping to 15q14 and expression analysis of the human
            MEIS2 homeobox gene
  JOURNAL   Mamm Genome 8 (12), 951-952 (1997)
   PUBMED   9383298
REFERENCE   10 (residues 1 to 381)
  AUTHORS   Steelman,S., Moskow,J.J., Muzynski,K., North,C., Druck,T.,
            Montgomery,J.C., Huebner,K., Daar,I.O. and Buchberg,A.M.
  TITLE     Identification of a conserved family of Meis1-related homeobox
            genes
  JOURNAL   Genome Res 7 (2), 142-156 (1997)
   PUBMED   9049632
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078909.7, AK300247.1,
            BC001516.2, BM679305.1 and AC018563.7.
            
            Summary: This gene encodes a homeobox protein belonging to the TALE
            ('three amino acid loop extension') family of
            homeodomain-containing proteins. TALE homeobox proteins are highly
            conserved transcription regulators, and several members have been
            shown to be essential contributors to developmental programs.
            Multiple transcript variants encoding distinct isoforms have been
            described for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (f) differs in the 5' UTR and
            coding sequence compared to variant a. The resulting isoform (f)
            has a shorter and distinct N-terminus and lacks an alternate
            internal segment compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001844.2, SRR1803617.27572.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q14"
     Protein         1..381
                     /product="homeobox protein Meis2 isoform f"
                     /note="Meis homolog 2; TALE homeobox protein Meis2;
                     Meis1-related gene 1; meis1-related protein 1; Meis1,
                     myeloid ecotropic viral integration site 1 homolog 2"
                     /calculated_mol_wt=41411
     Region          97..181
                     /region_name="Meis_PKNOX_N"
                     /note="N-terminal of Homeobox Meis and PKNOX1; pfam16493"
                     /db_xref="CDD:465140"
     Site            order(269,312,315..316,319)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Region          282..320
                     /region_name="Homeobox_KN"
                     /note="Homeobox KN domain; pfam05920"
                     /db_xref="CDD:428673"
     CDS             1..381
                     /gene="MEIS2"
                     /gene_synonym="CPCMR; HsT18361; MRG1"
                     /coded_by="NM_002399.4:448..1593"
                     /note="isoform f is encoded by transcript variant f"
                     /db_xref="CCDS:CCDS42014.1"
                     /db_xref="GeneID:4212"
                     /db_xref="HGNC:HGNC:7001"
                     /db_xref="MIM:601740"
ORIGIN      
        1 mdgvgvpasm ygdphaprpi ppvhhlnhgp plhatqhyga haphpnvmpa smgsavndal
       61 krdkdaiygh plfpllalvf ekcelatctp repgvaggdv cssdsfnedi avfakqvrae
      121 kplfssnpel dnlmiqaiqv lrfhllelek vhelcdnfch ryisclkgkm pidlviderd
      181 gssksdheel sgsstnladh npsswrdhdd atsthsagtp gpssgghasq sgdnsseqgd
      241 gldnsvaspg tgddddpdkd kkrqkkrgif pkvatnimra wlfqhlthpy pseeqkkqla
      301 qdtgltilqv nnwfinarrr ivqpmidqsn ravsqgaays pegqpmgsfv ldgqqhmgir
      361 pagpmsgmgm nmgmdgqwhy m
//
LOCUS       NP_057207                460 aa            linear   PRI 21-NOV-2025
DEFINITION  interleukin-1 receptor-associated kinase 4 isoform a [Homo
            sapiens].
ACCESSION   NP_057207
VERSION     NP_057207.2
DBSOURCE    REFSEQ: accession NM_016123.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Fisch,D., Zhang,T., Sun,H., Ma,W., Tan,Y., Gygi,S.P., Higgins,D.E.
            and Kagan,J.C.
  TITLE     Molecular definition of the endogenous Toll-like receptor
            signalling pathways
  JOURNAL   Nature 631 (8021), 635-644 (2024)
   PUBMED   38961291
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Liu,Y., Yuan,J., Zhang,Y., Qin,F., Bai,X., Sun,W., Chen,T., Liu,F.,
            Zheng,Y., Qi,X., Zhao,W., Liu,B. and Gao,C.
  TITLE     OTUD5 promotes the inflammatory immune response by enhancing MyD88
            oligomerization and Myddosome formation
  JOURNAL   Cell Death Differ 31 (6), 753-767 (2024)
   PUBMED   38605168
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Peterson,J., Balogh Sivars,K., Bianco,A. and Roper,K.
  TITLE     Toll-like receptor signalling via IRAK4 affects epithelial
            integrity and tightness through regulation of junctional tension
  JOURNAL   Development 150 (24) (2023)
   PUBMED   37997696
  REMARK    GeneRIF: Toll-like receptor signalling via IRAK4 affects epithelial
            integrity and tightness through regulation of junctional tension.
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Cooray,S., Price-Kuehne,F., Hong,Y., Omoyinmi,E., Burleigh,A.,
            Gilmour,K.C., Ahmad,B., Choi,S., Bahar,M.W., Torpiano,P.,
            Gagunashvili,A., Jensen,B., Bellos,E., Sancho-Shimizu,V.,
            Herberg,J.A., Mankad,K., Kumar,A., Kaliakatsos,M., Worth,A.J.J.,
            Eleftheriou,D., Whittaker,E. and Brogan,P.A.
  TITLE     Neuroinflammation, autoinflammation, splenomegaly and anemia caused
            by bi-allelic mutations in IRAK4
  JOURNAL   Front Immunol 14, 1231749 (2023)
   PUBMED   37744344
  REMARK    GeneRIF: Neuroinflammation, autoinflammation, splenomegaly and
            anemia caused by bi-allelic mutations in IRAK4.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 460)
  AUTHORS   Wang,Z., Liu,J., Sudom,A., Ayres,M., Li,S., Wesche,H., Powers,J.P.
            and Walker,N.P.
  TITLE     Crystal structures of IRAK-4 kinase in complex with inhibitors: a
            serine/threonine kinase with tyrosine as a gatekeeper
  JOURNAL   Structure 14 (12), 1835-1844 (2006)
   PUBMED   17161373
  REMARK    GeneRIF: crystallographic analysis of IRAK-4 kinase in complex with
            inhibitors
REFERENCE   6  (residues 1 to 460)
  AUTHORS   Suzuki,N. and Saito,T.
  TITLE     IRAK-4--a shared NF-kappaB activator in innate and acquired
            immunity
  JOURNAL   Trends Immunol 27 (12), 566-572 (2006)
   PUBMED   17046325
  REMARK    GeneRIF: Although each system seems to possess distinct activation
            mechanisms, interleukin-1 receptor-associated kinase (IRAK)-4 is
            essential for NF-kappaB activation in Toll-like receptor (TLR) and
            T-cell receptor (TCR) signaling pathways.
            Review article
REFERENCE   7  (residues 1 to 460)
  AUTHORS   Burns,K., Clatworthy,J., Martin,L., Martinon,F., Plumpton,C.,
            Maschera,B., Lewis,A., Ray,K., Tschopp,J. and Volpe,F.
  TITLE     Tollip, a new component of the IL-1RI pathway, links IRAK to the
            IL-1 receptor
  JOURNAL   Nat Cell Biol 2 (6), 346-351 (2000)
   PUBMED   10854325
REFERENCE   8  (residues 1 to 460)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   9  (residues 1 to 460)
  AUTHORS   Scherer,D.C., Brockman,J.A., Chen,Z., Maniatis,T. and Ballard,D.W.
  TITLE     Signal-induced degradation of I kappa B alpha requires
            site-specific ubiquitination
  JOURNAL   Proc Natl Acad Sci U S A 92 (24), 11259-11263 (1995)
   PUBMED   7479976
REFERENCE   10 (residues 1 to 460)
  AUTHORS   Siu,G., Strauss,E.C., Lai,E. and Hood,L.E.
  TITLE     Analysis of a human V beta gene subfamily
  JOURNAL   J Exp Med 164 (5), 1600-1614 (1986)
   PUBMED   3772297
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK304583.1, AK314288.1,
            BC013316.1, AC093012.9 and AI126481.1.
            
            On Feb 2, 2008 this sequence version replaced NP_057207.1.
            
            Summary: This gene encodes a kinase that activates NF-kappaB in
            both the Toll-like receptor (TLR) and T-cell receptor (TCR)
            signaling pathways. The protein is essential for most innate immune
            responses. Mutations in this gene result in IRAK4 deficiency and
            recurrent invasive pneumococcal disease. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, and 13 all encode the same isoform
            (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000528.1, AF155118.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000613694.5/ ENSP00000479889.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..460
                     /product="interleukin-1 receptor-associated kinase 4
                     isoform a"
                     /EC_number="2.7.11.1"
                     /note="renal carcinoma antigen NY-REN-64"
                     /calculated_mol_wt=51399
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NWZ3.1)"
     Region          9..106
                     /region_name="Death_IRAK4"
                     /note="Death domain of Interleukin-1 Receptor-Associated
                     Kinase 4; cd08793"
                     /db_xref="CDD:260060"
     Site            order(12,14,16..17,20,47..48,52,55..56,59,69,72..73,76,78)
                     /site_type="other"
                     /note="IRAK4-MyD88 interaction site [polypeptide binding]"
                     /db_xref="CDD:260060"
     Site            order(25,28..30,34,37,46,50,54,92..96,98)
                     /site_type="other"
                     /note="IRAK4-IRAK2 interaction site [polypeptide binding]"
                     /db_xref="CDD:260060"
     Site            34
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NWZ3.1)"
     Region          170..457
                     /region_name="STKc_IRAK4"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Interleukin-1 Receptor Associated Kinase 4; cd14158"
                     /db_xref="CDD:271060"
     Site            order(192..196,200,211,213,246,262..265,269,271,311,313,
                     315..316,318,329,332,350..353)
                     /site_type="active"
                     /db_xref="CDD:271060"
     Site            order(192..196,200,211,213,246,262..265,269,311,313,
                     315..316,318,329)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271060"
     Site            order(196,269,271,311,313,315,332,350..353)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271060"
     Site            order(328..340,342..353)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271060"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17312103, ECO:0000269|Ref.32;
                     propagated from UniProtKB/Swiss-Prot (Q9NWZ3.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17161373,
                     ECO:0000269|PubMed:17312103, ECO:0000269|Ref.32;
                     propagated from UniProtKB/Swiss-Prot (Q9NWZ3.1)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17161373,
                     ECO:0000269|PubMed:17312103; propagated from
                     UniProtKB/Swiss-Prot (Q9NWZ3.1)"
     CDS             1..460
                     /gene="IRAK4"
                     /gene_synonym="IMD67; IPD1; IRAK-4; NY-REN-64; REN64"
                     /coded_by="NM_016123.4:76..1458"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS8744.1"
                     /db_xref="GeneID:51135"
                     /db_xref="HGNC:HGNC:17967"
                     /db_xref="MIM:606883"
ORIGIN      
        1 mnkpitpsty vrclnvglir klsdfidpqe gwkklavaik kpsgddrynq fhirrfeall
       61 qtgksptsel lfdwgttnct vgdlvdlliq neffapasll lpdavpktan tlpskeaitv
      121 qqkqmpfcdk drtlmtpvqn leqsymppds sspenkslev sdtrfhsfsf yelknvtnnf
      181 derpisvggn kmgeggfgvv ykgyvnnttv avkklaamvd itteelkqqf dqeikvmakc
      241 qhenlvellg fssdgddlcl vyvympngsl ldrlscldgt pplswhmrck iaqgaangin
      301 flhenhhihr diksanilld eaftakisdf glarasekfa qtvmtsrivg ttaymapeal
      361 rgeitpksdi ysfgvvllei itglpavdeh repqllldik eeiedeekti edyidkkmnd
      421 adstsveamy svasqclhek knkrpdikkv qqllqemtas
//
LOCUS       NP_001002905             311 aa            linear   PRI 21-NOV-2025
DEFINITION  olfactory receptor 8G1 [Homo sapiens].
ACCESSION   NP_001002905
VERSION     NP_001002905.1
DBSOURCE    REFSEQ: accession NM_001002905.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Young,J.M., Endicott,R.M., Parghi,S.S., Walker,M., Kidd,J.M. and
            Trask,B.J.
  TITLE     Extensive copy-number variation of the human olfactory receptor
            gene family
  JOURNAL   Am J Hum Genet 83 (2), 228-242 (2008)
   PUBMED   18674749
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Malnic,B., Godfrey,P.A. and Buck,L.B.
  TITLE     The human olfactory receptor gene family
  JOURNAL   Proc Natl Acad Sci U S A 101 (8), 2584-2589 (2004)
   PUBMED   14983052
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 May 4;101(18):7205]
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Fuchs,T., Malecova,B., Linhart,C., Sharan,R., Khen,M., Herwig,R.,
            Shmulevich,D., Elkon,R., Steinfath,M., O'Brien,J.K., Radelof,U.,
            Lehrach,H., Lancet,D. and Shamir,R.
  TITLE     DEFOG: a practical scheme for deciphering families of genes
  JOURNAL   Genomics 80 (3), 295-302 (2002)
   PUBMED   12213199
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Vanderhaeghen,P., Schurmans,S., Vassart,G. and Parmentier,M.
  TITLE     Specific repertoire of olfactory receptor genes in the male germ
            cells of several mammalian species
  JOURNAL   Genomics 39 (3), 239-246 (1997)
   PUBMED   9119360
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FO680687.2 and AP002965.3.
            
            Summary: Olfactory receptors interact with odorant molecules in the
            nose, to initiate a neuronal response that triggers the perception
            of a smell. The olfactory receptor proteins are members of a large
            family of G-protein-coupled receptors (GPCR) arising from single
            coding-exon genes. Olfactory receptors share a 7-transmembrane
            domain structure with many neurotransmitter and hormone receptors
            and are responsible for the recognition and G protein-mediated
            transduction of odorant signals. The olfactory receptor gene family
            is the largest in the genome. This family member represents a
            polymorphic pseudogene, whereby some individuals have a functional
            allele that encodes a full-length protein, while others have a
            non-functional allele due to the presence of an early stop codon
            and a 3' end deletion. [provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (1, coding) represents the longer
            transcript and encodes the supported protein. It represents the
            functional allele, as described in PMID: 18674749 and found in the
            GRCh38 reference genome assembly.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence because no single transcript was available for the
            full length of the gene. This RefSeq is supported by partial
            transcript and paralogous alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1968968, SAMEA2148093
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000641972.1/ ENSP00000493289.1
            polymorphic pseudogene :: PMID: 18674749
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.2"
     Protein         1..311
                     /product="olfactory receptor 8G1"
                     /note="olfactory receptor, family 8, subfamily G, member 1
                     pseudogene; olfactory receptor TPCR25; olfactory receptor
                     OR11-281"
                     /calculated_mol_wt=34773
     Site            5
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15617.2)"
     Site            6
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15617.2)"
     Region          16..305
                     /region_name="7tmA_OR8D-like"
                     /note="olfactory receptor subfamily 8D and related
                     proteins, member of the class A family of
                     seven-transmembrane G protein-coupled receptors; cd15406"
                     /db_xref="CDD:320528"
     Region          26..52
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320528"
     Site            26..46
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15617.2)"
     Site            55..75
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15617.2)"
     Region          59..85
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320528"
     Site            order(81,84..85,97..102,104..105,108,153,155..159,195,
                     198..200,202..204,206..207,252,255..256,258..259,262,
                     268..269,271..273,276,279..280)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320528"
     Region          97..127
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320528"
     Site            100..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15617.2)"
     Region          140..161
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320528"
     Site            140..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15617.2)"
     Region          195..225
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320528"
     Site            198..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15617.2)"
     Region          232..262
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320528"
     Site            238..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15617.2)"
     Region          269..294
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320528"
     Site            272..292
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15617.2)"
     CDS             1..311
                     /gene="OR8G1"
                     /gene_synonym="HSTPCR25; OR8G1P; TPCR25"
                     /coded_by="NM_001002905.2:367..1302"
                     /db_xref="CCDS:CCDS73407.1"
                     /db_xref="GeneID:26494"
                     /db_xref="HGNC:HGNC:8484"
ORIGIN      
        1 msgennssvt efilaglseq pelqlplfll flgiyvvtvv gnlgmttliw lsshlhtpmy
       61 yflsslsfid fchstvitpk mlvnfvtekn iisypecmtq lyfflvfaia echmlaamay
      121 drymaicspl lysviisnka cfslilgvyi iglvcasvht gcmfrvqfck fdlinhyfcd
      181 llpllklscs siyvnkllil cvgafnilvp sltilcsyif iiasilhirs tegrskafst
      241 csshmlavvi ffgsaafmyl qpssissmdq gkvssvfyti ivpmlnpliy slrnkdvhvs
      301 lkkmlqrrtl l
//
LOCUS       NP_001374709             162 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor protein D52 isoform 10 [Homo sapiens].
ACCESSION   NP_001374709
VERSION     NP_001374709.1
DBSOURCE    REFSEQ: accession NM_001387780.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Zhang,J., Li,Z., Han,J., Tian,Z., Meng,Q. and Niu,W.
  TITLE     KLF7 enhances the invasion and migration of colorectal cancer cells
            via the miR-139-5p/TPD52 axis
  JOURNAL   Cancer Biol Ther 25 (1), 2385172 (2024)
   PUBMED   39097779
  REMARK    GeneRIF: KLF7 enhances the invasion and migration of colorectal
            cancer cells via the miR-139-5p/TPD52 axis.
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Li,Y., Zhu,X., Zhang,C., Yin,Y., Chen,L., Liu,Y., He,A. and Xia,F.
  TITLE     Long noncoding RNA FTX promotes epithelial-mesenchymal transition
            of epithelial ovarian cancer through modulating miR-7515/TPD52 and
            activating Met/Akt/mTOR
  JOURNAL   Histol Histopathol 38 (12), 1487-1498 (2023)
   PUBMED   37140169
  REMARK    GeneRIF: Long noncoding RNA FTX promotes epithelial-mesenchymal
            transition of epithelial ovarian cancer through modulating
            miR-7515/TPD52 and activating Met/Akt/mTOR.
REFERENCE   4  (residues 1 to 162)
  AUTHORS   Khan,K., Zafar,S., Badshah,Y., Ashraf,N.M., Rafiq,M., Danish,L.,
            Shabbir,M., Trembley,J.H., Afsar,T., Almajwal,A. and Razak,S.
  TITLE     Cross talk of tumor protein D52 (TPD52) with KLF9, PKCepsilon, and
            MicroRNA 223 in ovarian cancer
  JOURNAL   J Ovarian Res 16 (1), 202 (2023)
   PUBMED   37833790
  REMARK    GeneRIF: Cross talk of tumor protein D52 (TPD52) with KLF9,
            PKCepsilon, and MicroRNA 223 in ovarian cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 162)
  AUTHORS   Liu,S., Hu,C., Li,M., Zhou,W., Wang,R. and Xiao,Y.
  TITLE     Androgen receptor suppresses lung cancer invasion and increases
            cisplatin response via decreasing TPD52 expression
  JOURNAL   Int J Biol Sci 19 (12), 3709-3725 (2023)
   PUBMED   37564195
  REMARK    GeneRIF: Androgen receptor suppresses lung cancer invasion and
            increases cisplatin response via decreasing TPD52 expression.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 162)
  AUTHORS   Wang,R., He,H., Sun,X., Xu,J., Marshall,F.F., Zhau,H., Chung,L.W.,
            Fu,H. and He,D.
  TITLE     Transcription variants of the prostate-specific PrLZ gene and their
            interaction with 14-3-3 proteins
  JOURNAL   Biochem Biophys Res Commun 389 (3), 455-460 (2009)
   PUBMED   19732746
  REMARK    GeneRIF: Alternative splicing may contribute to abnormally enhanced
            PrLZ levels in prostate cancer, and interaction with 14-3-3
            proteins may be a mechanism by which PrLZ promotes cell
            proliferation and survival during prostate cancer development and
            progression.
REFERENCE   7  (residues 1 to 162)
  AUTHORS   Byrne,J.A., Nourse,C.R., Basset,P. and Gunning,P.
  TITLE     Identification of homo- and heteromeric interactions between
            members of the breast carcinoma-associated D52 protein family using
            the yeast two-hybrid system
  JOURNAL   Oncogene 16 (7), 873-881 (1998)
   PUBMED   9484778
REFERENCE   8  (residues 1 to 162)
  AUTHORS   Byrne,J.A., Mattei,M.G. and Basset,P.
  TITLE     Definition of the tumor protein D52 (TPD52) gene family through
            cloning of D52 homologues in human (hD53) and mouse (mD52)
  JOURNAL   Genomics 35 (3), 523-532 (1996)
   PUBMED   8812487
REFERENCE   9  (residues 1 to 162)
  AUTHORS   Chen,S.L., Maroulakou,I.G., Green,J.E., Romano-Spica,V., Modi,W.,
            Lautenberger,J. and Bhat,N.K.
  TITLE     Isolation and characterization of a novel gene expressed in
            multiple cancers
  JOURNAL   Oncogene 12 (4), 741-751 (1996)
   PUBMED   8632896
REFERENCE   10 (residues 1 to 162)
  AUTHORS   Byrne,J.A., Tomasetto,C., Garnier,J.M., Rouyer,N., Mattei,M.G.,
            Bellocq,J.P., Rio,M.C. and Basset,P.
  TITLE     A screening method to identify genes commonly overexpressed in
            carcinomas and the identification of a novel complementary DNA
            sequence
  JOURNAL   Cancer Res 55 (13), 2896-2903 (1995)
   PUBMED   7796418
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009686.14.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2142348,
                              SAMEA2142586 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.13"
     Protein         1..162
                     /product="tumor protein D52 isoform 10"
                     /EC_number="2.7.1.21"
                     /note="prostate and colon associated protein; prostate
                     leucine zipper; protein N8"
                     /calculated_mol_wt=17727
     Region          52..146
                     /region_name="TPD52"
                     /note="Tumour protein D52 family; pfam04201"
                     /db_xref="CDD:461225"
     CDS             1..162
                     /gene="TPD52"
                     /gene_synonym="D52; hD52; N8L; PC-1; PrLZ"
                     /coded_by="NM_001387780.1:206..694"
                     /note="isoform 10 is encoded by transcript variant 15"
                     /db_xref="GeneID:7163"
                     /db_xref="HGNC:HGNC:12005"
                     /db_xref="MIM:604068"
ORIGIN      
        1 meeprrteds vqttgllrtd pvpeegedva atisatetls eeeqeelrre lakveeeiqt
       61 lsqvlaakek hlaeikrklg inslqelkqn iakgwqdvta tsaykktset lsqagqkasa
      121 afssvgsvit kkledvknsp tfksfeekve nlkahpssil st
//
LOCUS       NP_932348                915 aa            linear   PRI 21-NOV-2025
DEFINITION  coiled-coil domain-containing protein 57 isoform 1 [Homo sapiens].
ACCESSION   NP_932348 XP_001134355 XP_001134356 XP_001134357
VERSION     NP_932348.2
DBSOURCE    REFSEQ: accession NM_198082.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 915)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   2  (residues 1 to 915)
  AUTHORS   Gurkaslar,H.K., Culfa,E., Arslanhan,M.D., Lince-Faria,M. and
            Firat-Karalar,E.N.
  TITLE     CCDC57 Cooperates with Microtubules and Microcephaly Protein CEP63
            and Regulates Centriole Duplication and Mitotic Progression
  JOURNAL   Cell Rep 31 (6), 107630 (2020)
   PUBMED   32402286
  REMARK    GeneRIF: CCDC57 Cooperates with Microtubules and Microcephaly
            Protein CEP63 and Regulates Centriole Duplication and Mitotic
            Progression.
REFERENCE   3  (residues 1 to 915)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 915)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 915)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 915)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 915)
  AUTHORS   Shin,S.Y., Fauman,E.B., Petersen,A.K., Krumsiek,J., Santos,R.,
            Huang,J., Arnold,M., Erte,I., Forgetta,V., Yang,T.P., Walter,K.,
            Menni,C., Chen,L., Vasquez,L., Valdes,A.M., Hyde,C.L., Wang,V.,
            Ziemek,D., Roberts,P., Xi,L., Grundberg,E., Waldenberger,M.,
            Richards,J.B., Mohney,R.P., Milburn,M.V., John,S.L., Trimmer,J.,
            Theis,F.J., Overington,J.P., Suhre,K., Brosnan,M.J., Gieger,C.,
            Kastenmuller,G., Spector,T.D. and Soranzo,N.
  CONSRTM   Multiple Tissue Human Expression Resource (MuTHER) Consortium
  TITLE     An atlas of genetic influences on human blood metabolites
  JOURNAL   Nat Genet 46 (6), 543-550 (2014)
   PUBMED   24816252
REFERENCE   8  (residues 1 to 915)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   9  (residues 1 to 915)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 915)
  AUTHORS   Ozyildirim,A.M., Wistow,G.J., Gao,J., Wang,J., Dickinson,D.P.,
            Frierson,H.F. Jr. and Laurie,G.W.
  TITLE     The lacrimal gland transcriptome is an unusually rich source of
            rare and poorly characterized gene transcripts
  JOURNAL   Invest Ophthalmol Vis Sci 46 (5), 1572-1580 (2005)
   PUBMED   15851553
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC132872.17, BC110997.1, BE146089.1, AK074059.1 and AW338721.1.
            
            On or before Sep 20, 2006 this sequence version replaced
            XP_001134357.1, XP_001134355.1, XP_001134356.1, NP_932348.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..915
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..915
                     /product="coiled-coil domain-containing protein 57 isoform
                     1"
                     /EC_number="4.2.1.59"
                     /note="coiled-coil domain-containing protein 57"
                     /calculated_mol_wt=102908
     Region          1..502
                     /region_name="Centrosomal targeting domain.
                     /evidence=ECO:0000269|PubMed:32402286"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAC2.3)"
     Region          <9..>598
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          555..574
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAC2.3)"
     Region          606..915
                     /region_name="Microtubule binding domain.
                     /evidence=ECO:0000269|PubMed:32402286"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAC2.3)"
     Region          606..653
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAC2.3)"
     Region          724..915
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAC2.3)"
     CDS             1..915
                     /gene="CCDC57"
                     /coded_by="NM_198082.4:67..2814"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS92419.1"
                     /db_xref="GeneID:284001"
                     /db_xref="HGNC:HGNC:27564"
ORIGIN      
        1 mlplgsepal nelllrkeee wralqahrtq lqeaalqdtr sqleeaqgkl rclqedfvyn
       61 lqvleerdle lerydaafaq areweearra evselkieaa klrqalarea rkveelqqqq
      121 qlafqehrle lervhsdkng eidhhreqye nlkwtlerkl eeldgelalq rqelllefes
      181 kmrkrehefr lqadnmsnta lsrelkvkll hkelealkea gakaaeslqr aeatnaeler
      241 klqsragelq dleamsrarv kdledklhsv qltrkkeeet fkrkheeldr larekdavlv
      301 avkgahveql qelqtrvlel qahcetleaq lrraewrqad takekdaaid qlredastvk
      361 sawdaqiaql skemvsrdlq iqtlqeeevk lkaqvarsqq dierykqqls laverersle
      421 rdqvqlgldw qrrcddierd qiqksealiq glsmaksqva aklqeteqal qeqevvlkav
      481 tlerdqavqa lrmhglprpg aqmllrqhee eiskdfpsse iqrlreqnts lrnaiaqmrk
      541 emealshqip ppiqtaaest danqpdpeag gdaatpdyvl aleaeirtlk hkfktlekhl
      601 edvldplkms sphaesqpsv rtstettggs aqagqaggsv qagqaggsvq agpvssglal
      661 rklgdrvqll nllvtrlrqk vlreplepaa lqrelprevd qvhlevlelr kqvaelgkhl
      721 riaqhggaep sgrkqppasd avalgredak saedeapsrh lgkhqprsaq vgsrldalqg
      781 pktqhsihtv tcksprqked rspkppqapq hpeehgrqsh ssssfasgtl qdmwrlldlg
      841 sspsgvtsqg dstpelpapp aadrrpvkmq agiatpgmkt aaqakakttg asrshpakak
      901 gcqrppkirn ynimd
//
LOCUS       NP_055642                810 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger CCCH domain-containing protein 11A isoform 1 [Homo
            sapiens].
ACCESSION   NP_055642 XP_378929
VERSION     NP_055642.3
DBSOURCE    REFSEQ: accession NM_014827.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Kases,K., Schubert,E., Hajikhezri,Z., Larsson,M., Devi,P.,
            Darweesh,M., Andersson,L., Akusjarvi,G., Punga,T. and Younis,S.
  TITLE     The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts
  JOURNAL   J Biol Chem 299 (8), 104959 (2023)
   PUBMED   37356722
  REMARK    GeneRIF: The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts.
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 810)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 810)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114402.2.
            
            On Sep 20, 2006 this sequence version replaced NP_055642.2.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1-7 encode the same protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014268.2, SRR1803615.169668.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..810
                     /product="zinc finger CCCH domain-containing protein 11A
                     isoform 1"
                     /note="zinc finger CCCH-type domain containing 11A; zinc
                     finger CCCH domain-containing protein 11A"
                     /calculated_mol_wt=89000
     Region          1..110
                     /region_name="zf-CCCH_3"
                     /note="Zinc-finger containing family; pfam15663"
                     /db_xref="CDD:464787"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          139..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          223..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          285..351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          367..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          482..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          715..768
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     CDS             1..810
                     /gene="ZC3H11A"
                     /gene_synonym="ZC3HDC11A"
                     /coded_by="NM_014827.6:617..3049"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS30978.1"
                     /db_xref="GeneID:9877"
                     /db_xref="HGNC:HGNC:29093"
                     /db_xref="MIM:613513"
ORIGIN      
        1 mpnqgedcyf ffystctkgd scpfrhceaa ignetvctlw qegrcfrqvc rfrhmeidkk
       61 rseipcywen qptgcqklnc afhhnrgryv dglflppskt vlptvpespe eevkasqlsv
      121 qqnklsvqsn pspqlrsvmk vessenvpsp thppvvinaa dddeddddqf seegdetktp
      181 tlqptpevhn glrvtsvrkp avnikqgecl nfgiktleei kskkmkeksk kqgegssgvs
      241 slllhpepvp gpekenvrtv vrtvtlstkq geeplvrlsl terlgkrkfs aggdsdpplk
      301 rslaqrlgkk veapetnidk tpkkaqvsks lkerlgmsad pdnedatdkv nkvgeihvkt
      361 leeilleras qkrgelqtkl ktegpsktdd stsgarssst iriktfsevl aekkhrqqea
      421 erqkskkdtt ciklkidsei kktvvlppiv asrgqseepa gktksmqevh iktleeikle
      481 kalrvqqsse sstsspsqhe atpgarrllr itkrtgmkee knlqegnevd sqssirteak
      541 easgettgvd itkiqvkrce tmrekhmqkq qereksvltp lrgdvascnt qvaekpvlta
      601 vpgitrhltk rlptkssqkv evetsgigds llnvkcaaqt lekrgkakpk vnvkpsvvkv
      661 vsspklapkr kavemhaavi aavkplssss vlqeppakka avavvplvse dksvtvpeae
      721 nprdslvlpp tqsssdsspp evsgpsssqm smktrrlssa stgkpplsve ddfekliwei
      781 sggkleaeid ldpgkdeddl llelsemids
//
LOCUS       NP_001358052            1214 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal cell adhesion molecule isoform G precursor [Homo sapiens].
ACCESSION   NP_001358052
VERSION     NP_001358052.1
DBSOURCE    REFSEQ: accession NM_001371123.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1214)
  AUTHORS   Wang,C., Wang,Z., Fu,L., Du,J., Ji,F. and Qiu,X.
  TITLE     CircNRCAM up-regulates NRCAM to promote papillary thyroid carcinoma
            progression
  JOURNAL   J Endocrinol Invest 47 (5), 1215-1226 (2024)
   PUBMED   38485895
  REMARK    GeneRIF: CircNRCAM up-regulates NRCAM to promote papillary thyroid
            carcinoma progression.
REFERENCE   2  (residues 1 to 1214)
  AUTHORS   Zhou,L., He,L., Liu,C.H., Qiu,H., Zheng,L., Sample,K.M., Wu,Q.,
            Li,J., Xie,K., Ampuero,J., Li,Z., Lv,D., Liu,M., Romero-Gomez,M.,
            Hu,Y. and Tang,H.
  TITLE     Liver cancer stem cell dissemination and metastasis: uncovering the
            role of NRCAM in hepatocellular carcinoma
  JOURNAL   J Exp Clin Cancer Res 42 (1), 311 (2023)
   PUBMED   37993901
  REMARK    GeneRIF: Liver cancer stem cell dissemination and metastasis:
            uncovering the role of NRCAM in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1214)
  AUTHORS   Sannes,A.C., Christensen,J.O., Nielsen,M.B. and Gjerstad,J.
  TITLE     Stress-induced headache in the general working population is
            moderated by the NRCAM rs2300043 genotype
  JOURNAL   Scand J Pain 23 (2), 326-332 (2022)
   PUBMED   36181733
  REMARK    GeneRIF: Stress-induced headache in the general working population
            is moderated by the NRCAM rs2300043 genotype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1214)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 1214)
  AUTHORS   Bai,C. and Chen,D.G.
  TITLE     NRCAM acts as a prognostic biomarker and promotes the tumor
            progression in gastric cancer via EMT pathway
  JOURNAL   Tissue Cell 77, 101859 (2022)
   PUBMED   35763884
  REMARK    GeneRIF: NRCAM acts as a prognostic biomarker and promotes the
            tumor progression in gastric cancer via EMT pathway.
REFERENCE   6  (residues 1 to 1214)
  AUTHORS   Wang,B., Williams,H., Du,J.S., Terrett,J. and Kenwrick,S.
  TITLE     Alternative splicing of human NrCAM in neural and nonneural tissues
  JOURNAL   Mol Cell Neurosci 10 (5-6), 287-295 (1998)
   PUBMED   9604207
REFERENCE   7  (residues 1 to 1214)
  AUTHORS   Grumet,M.
  TITLE     Nr-CAM: a cell adhesion molecule with ligand and receptor functions
  JOURNAL   Cell Tissue Res 290 (2), 423-428 (1997)
   PUBMED   9321706
  REMARK    Review article
REFERENCE   8  (residues 1 to 1214)
  AUTHORS   Sakurai,T., Lustig,M., Nativ,M., Hemperly,J.J., Schlessinger,J.,
            Peles,E. and Grumet,M.
  TITLE     Induction of neurite outgrowth through contactin and Nr-CAM by
            extracellular regions of glial receptor tyrosine phosphatase beta
  JOURNAL   J Cell Biol 136 (4), 907-918 (1997)
   PUBMED   9049255
REFERENCE   9  (residues 1 to 1214)
  AUTHORS   Volkmer,H., Leuschner,R., Zacharias,U. and Rathjen,F.G.
  TITLE     Neurofascin induces neurites by heterophilic interactions with
            axonal NrCAM while NrCAM requires F11 on the axonal surface to
            extend neurites
  JOURNAL   J Cell Biol 135 (4), 1059-1069 (1996)
   PUBMED   8922386
REFERENCE   10 (residues 1 to 1214)
  AUTHORS   Lane,R.P., Chen,X.N., Yamakawa,K., Vielmetter,J., Korenberg,J.R.
            and Dreyer,W.J.
  TITLE     Characterization of a highly conserved human homolog to the chicken
            neural cell surface protein Bravo/Nr-CAM that maps to chromosome
            band 7q31
  JOURNAL   Genomics 35 (3), 456-465 (1996)
   PUBMED   8812479
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005058.1, AC007567.2 and
            AC005683.2.
            
            Summary: Cell adhesion molecules (CAMs) are members of the
            immunoglobulin superfamily. This gene encodes a neuronal cell
            adhesion molecule with multiple immunoglobulin-like C2-type domains
            and fibronectin type-III domains. This ankyrin-binding protein is
            involved in neuron-neuron adhesion and promotes directional
            signaling during axonal cone growth. This gene is also expressed in
            non-neural tissues and may play a general role in cell-cell
            communication via signaling from its intracellular domain to the
            actin cytoskeleton during directional cell migration. Allelic
            variants of this gene have been associated with autism and
            addiction vulnerability. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (24), as well as variant 25,
            encodes isoform G.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1214
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1214
                     /product="neuronal cell adhesion molecule isoform G
                     precursor"
                     /note="NgCAM-related cell adhesion molecule; neuronal
                     surface protein Bravo"
                     /calculated_mol_wt=130833
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3315
     Region          46..140
                     /region_name="IgI_NrCAM"
                     /note="Immunoglobulin (Ig)-like domain of NrCAM (Ng
                     (neuronglia) CAM-related cell adhesion molecule); member
                     of the I-set of Ig superfamily (IgSF) domains; cd05874"
                     /db_xref="CDD:409458"
     Region          46..50
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409458"
     Region          55..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409458"
     Region          64..71
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409458"
     Region          77..82
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409458"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          85..87
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409458"
     Region          94..97
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409458"
     Region          102..106
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409458"
     Region          119..127
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409458"
     Region          130..140
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409458"
     Region          149..238
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          163..167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409432"
     Region          177..181
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409432"
     Region          200..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409432"
     Region          215..220
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409432"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          231..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409432"
     Site            245
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            251
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          277..358
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          288..292
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          301..305
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            314
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          323..327
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          337..342
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          350..353
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          362..450
                     /region_name="Ig4_NrCAM"
                     /note="Fourth immunoglobulin (Ig)-like domain of NrCAM
                     (NgCAM-related cell adhesion molecule); cd05868"
                     /db_xref="CDD:409454"
     Region          378..382
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409454"
     Region          391..395
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409454"
     Region          415..419
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409454"
     Region          429..434
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409454"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          442..445
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409454"
     Region          459..542
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          472..476
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          485..489
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            507
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          508..512
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          522..527
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          535..538
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          546..1051
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            619
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          647..737
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(647,713,728)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            716
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            order(729..730,732..733)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            802
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            858
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            993
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1009
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1019
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          1101..1190
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     CDS             1..1214
                     /gene="NRCAM"
                     /gene_synonym="NEDNMS"
                     /coded_by="NM_001371123.1:383..4027"
                     /note="isoform G precursor is encoded by transcript
                     variant 24"
                     /db_xref="GeneID:4897"
                     /db_xref="HGNC:HGNC:7994"
                     /db_xref="MIM:601581"
ORIGIN      
        1 mqlkimpkkk rlsagrvpli lflcqmisal evpldpklle dlvqpptitq qspkdyiidp
       61 reniviqcea kgkpppsfsw trngthfdid kdplvtmkpg tgtliinims egkaetyegv
      121 yqctarnerg aavsnnivvr psrsplwtke klepitlqsg qslvlpcrpp iglpppiifw
      181 mdnsfqrlpq servsqglng dlyfsnvlpe dtredyicya rfnhtqtiqq kqpisvkvis
      241 vdelndtiaa nlsdtefyga kssrerpptf ltpegnasnk eelrgnvlsl eciaeglptp
      301 iiywakedgm lpknrtvykn fektlqiihv seadsgnyqc iaknalgaih htisvrvkaa
      361 pywitapqnl vlspgedgtl icrangnpkp riswltngvp ieiapddpsr kidgdtiifs
      421 nvqerssavy qcnasneygy llanafvnvl aeppriltpa ntlyqvianr palldcaffg
      481 splptiewfk gakgsalhed iyvlhengtl eipvaqkdst gtytcvarnk lgmaknevhl
      541 eikdptwivk qpeyavvqrg smvsfeckvk hdhtlsltvl wlkdnrelps derftvdkdh
      601 lvvadvsddd sgtytcvant tldsvsasav lsvvaptptp apvydvpnpp fdleltdqld
      661 ksvqlswtpg ddnnspitkf iieyedamhk pglwhhqtev sgtqttaqlk lspyvnysfr
      721 vmavnsigks lpseaseqyl tkasepdknp taveglgsep dnlvitwkpl ngfesngpgl
      781 qykvswrqkd gddewtsvvv anvskyivsg tptfvpylik vqalndmgfa pepavvmghs
      841 gedlpmvapg nvrvnvvnst laevhwdpvp lksirghlqg yriyywktqs sskrnrrhie
      901 kkiltfqgsk thgmlpglep fshytlnvrv vngkgegpas pdrvfntpeg vpsapsslki
      961 vnptldsltl ewdppshpng ilteytlkyq pinsthelgp lvdlkipank trwtlknlnf
     1021 strykfyfya qtsagsgsqi teeavttvde gkmagilppd vgagkamasr qvdiatqgwf
     1081 iglmcavall ilillivcfi rrnkggkypv kekedahadp eiqpmkeddg tfgeysdaed
     1141 hkplkkgsrt psdrtvkked sddslvdyge gvngqfnedg sfigqysgkk ekepaegnes
     1201 seapspvnam nsfv
//
LOCUS       NP_001337373             937 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 1 isoform 40 [Homo
            sapiens].
ACCESSION   NP_001337373 XP_016866038
VERSION     NP_001337373.1
DBSOURCE    REFSEQ: accession NM_001350444.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 937)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 937)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 937)
  AUTHORS   Ruhle,F., Witten,A., Barysenka,A., Huge,A., Arning,A., Heller,C.,
            Krumpel,A., Mesters,R., Franke,A., Lieb,W., Riemenschneider,M.,
            Hiersche,M., Limperger,V., Nowak-Gottl,U. and Stoll,M.
  TITLE     Rare genetic variants in SMAP1, B3GAT2, and RIMS1 contribute to
            pediatric venous thromboembolism
  JOURNAL   Blood 129 (6), 783-790 (2017)
   PUBMED   28011674
  REMARK    GeneRIF: The study identified a region on chromosome 6 comprising
            the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus
            for pediatric venous thromboembolism.
REFERENCE   6  (residues 1 to 937)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 937)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
REFERENCE   8  (residues 1 to 937)
  AUTHORS   Schoch,S., Castillo,P.E., Jo,T., Mukherjee,K., Geppert,M., Wang,Y.,
            Schmitz,F., Malenka,R.C. and Sudhof,T.C.
  TITLE     RIM1alpha forms a protein scaffold for regulating neurotransmitter
            release at the active zone
  JOURNAL   Nature 415 (6869), 321-326 (2002)
   PUBMED   11797009
REFERENCE   9  (residues 1 to 937)
  AUTHORS   Coppola,T., Magnin-Luthi,S., Perret-Menoud,V., Gattesco,S.,
            Schiavo,G. and Regazzi,R.
  TITLE     Direct interaction of the Rab3 effector RIM with Ca2+ channels,
            SNAP-25, and synaptotagmin
  JOURNAL   J Biol Chem 276 (35), 32756-32762 (2001)
   PUBMED   11438518
REFERENCE   10 (residues 1 to 937)
  AUTHORS   Betz,A., Thakur,P., Junge,H.J., Ashery,U., Rhee,J.S., Scheuss,V.,
            Rosenmund,C., Rettig,J. and Brose,N.
  TITLE     Functional interaction of the active zone proteins Munc13-1 and
            RIM1 in synaptic vesicle priming
  JOURNAL   Neuron 30 (1), 183-196 (2001)
   PUBMED   11343654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590011.5, AL445256.18 and
            AL035633.18.
            
            On Apr 14, 2017 this sequence version replaced XP_016866038.1.
            
            Summary: The protein encoded by this gene is a RAS gene superfamily
            member that regulates synaptic vesicle exocytosis. This gene also
            plays a role in the regulation of voltage-gated calcium channels
            during neurotransmitter and insulin release. Mutations have
            suggested a role cognition and have been identified as the cause of
            cone-rod dystrophy type 7. Multiple transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Mar 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.237859.1,
                                           SRR1803614.76514.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..937
                     /product="regulating synaptic membrane exocytosis protein
                     1 isoform 40"
                     /note="RAB3-interacting protein 2; rab3-interacting
                     molecule 1; rab-3-interacting protein 2"
                     /calculated_mol_wt=104384
     Region          68..164
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(89..95,110,113,143,147,150..151)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          216..342
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(247,253,308,310,318)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          345..>556
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          768..913
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(825,829..830,832,835,863,865,867,911..912)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..937
                     /gene="RIMS1"
                     /gene_synonym="CORD7; RAB3IP2; RIM; RIM1"
                     /coded_by="NM_001350444.2:231..3044"
                     /note="isoform 40 is encoded by transcript variant 40"
                     /db_xref="GeneID:22999"
                     /db_xref="HGNC:HGNC:17282"
                     /db_xref="MIM:606629"
ORIGIN      
        1 mcapgihvss egweevrsvd seegtiearr avagdldyyw ldpatwhsre tspisshpvt
       61 wqpskegdrl igrvilnkrt tmpkdsgall glkvvggkmt dlgrlgafit kvkkgsladv
      121 vghlragdev lewngkplpg atneevynii lesksepqve iivsrpigdi pripesshpp
      181 lesssssfes qkmerpsisv isptspgalk dapqvlpgql svklwydkvg hqlivnvlqa
      241 tdlparvdgr prnpyvkmyf lpdrsdkskr rtktvkkile pkwnqtfvys hvhrrdfrer
      301 mleitvwdqp rvqeeesefl geilieleta llddephwyk lqthdesslp lpqpspfmpr
      361 rhihgesssk klqrsqrisd sdisdyevdd gigvvppgyr ssareskstt ltvpeqqrtt
      421 hhrsrsvsph rgndqgkprs rlpnvplqrs ldeihptrrs rsptrhhdas rspvdhrtrd
      481 vdsqylseqd rmhrqrsptq sppadtsfss rrgrqlpqvp vrsgsieqas lvveertrqm
      541 kmkvhrfkqt tgsgssqeld reqyskynih kdqyrscdnv sakssdsdvs dvsaisrtss
      601 asrlsstsfm seqserprgr issftpkmqg rrmgtsgrsi mkstsvsgem ytlehndgsq
      661 sdtavgtvga ggkkrrssls akvvaivsrr srstsqlsqt esghkklkst iqrstetgma
      721 aemrkmvrqp srestdgsin syssegnlif pgvrlgadsq fsdfldglgp aqlvgrqtla
      781 tpamgdiqig medkkgqlev evirarsltq kpgskstpap yvkvylleng aciakkktri
      841 arktldplyq qslvfdespq gkvlqvivwg dygrmdhkcf mgvaqillee ldlssmvigw
      901 yklfppsslv dptltpltrr asqsslesst gppcirs
//
LOCUS       NP_001336991            1660 aa            linear   PRI 21-NOV-2025
DEFINITION  protein TANC1 isoform 3 [Homo sapiens].
ACCESSION   NP_001336991 XP_016860646
VERSION     NP_001336991.1
DBSOURCE    REFSEQ: accession NM_001350062.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1660)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1660)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1660)
  AUTHORS   Wu,D., Li,Y., Ren,Q., Pei,S., Wang,L., Yang,L., Chong,Y., Sun,S.,
            Hao,J. and Feng,F.
  TITLE     TANC1 methylation as a novel biomarker for the diagnosis of
            patients with anti-tuberculosis drug-induced liver injury
  JOURNAL   Sci Rep 11 (1), 17423 (2021)
   PUBMED   34465797
  REMARK    GeneRIF: TANC1 methylation as a novel biomarker for the diagnosis
            of patients with anti-tuberculosis drug-induced liver injury.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1660)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1660)
  AUTHORS   Yang,Q., Liu,H., Li,Z., Wang,Y. and Liu,W.
  TITLE     Purification and mutagenesis studies of TANC1 ankyrin repeats
            domain provide clues to understand mis-sense variants from diseases
  JOURNAL   Biochem Biophys Res Commun 514 (2), 358-364 (2019)
   PUBMED   31040020
  REMARK    GeneRIF: mis-sense variants tested in this study may either affect
            protein folding or disrupt the interaction between TANC1/2 AR
            domains and their binding partners
REFERENCE   6  (residues 1 to 1660)
  AUTHORS   Fachal,L., Gomez-Caamano,A., Barnett,G.C., Peleteiro,P.,
            Carballo,A.M., Calvo-Crespo,P., Kerns,S.L., Sanchez-Garcia,M.,
            Lobato-Busto,R., Dorling,L., Elliott,R.M., Dearnaley,D.P.,
            Sydes,M.R., Hall,E., Burnet,N.G., Carracedo,A., Rosenstein,B.S.,
            West,C.M., Dunning,A.M. and Vega,A.
  TITLE     A three-stage genome-wide association study identifies a
            susceptibility locus for late radiotherapy toxicity at 2q24.1
  JOURNAL   Nat Genet 46 (8), 891-894 (2014)
   PUBMED   24974847
REFERENCE   7  (residues 1 to 1660)
  AUTHORS   Avirneni-Vadlamudi,U., Galindo,K.A., Endicott,T.R., Paulson,V.,
            Cameron,S. and Galindo,R.L.
  TITLE     Drosophila and mammalian models uncover a role for the myoblast
            fusion gene TANC1 in rhabdomyosarcoma
  JOURNAL   J Clin Invest 122 (1), 403-407 (2012)
   PUBMED   22182840
REFERENCE   8  (residues 1 to 1660)
  AUTHORS   Granot-Hershkovitz,E., Raas-Rothschild,A., Frumkin,A., Granot,D.,
            Silverstein,S. and Abeliovich,D.
  TITLE     Complex chromosomal rearrangement in a girl with
            psychomotor-retardation and a de novo inversion: inv(2)(p15;q24.2)
  JOURNAL   Am J Med Genet A 155A (8), 1825-1832 (2011)
   PUBMED   21739571
REFERENCE   9  (residues 1 to 1660)
  AUTHORS   Aouizerat,B.E., Vittinghoff,E., Musone,S.L., Pawlikowska,L.,
            Kwok,P.Y., Olgin,J.E. and Tseng,Z.H.
  TITLE     GWAS for discovery and replication of genetic loci associated with
            sudden cardiac arrest in patients with coronary artery disease
  JOURNAL   BMC Cardiovasc Disord 11, 29 (2011)
   PUBMED   21658281
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1660)
  AUTHORS   Suzuki,T., Li,W., Zhang,J.P., Tian,Q.B., Sakagami,H., Usuda,N.,
            Kondo,H., Fujii,T. and Endo,S.
  TITLE     A novel scaffold protein, TANC, possibly a rat homolog of
            Drosophila rolling pebbles (rols), forms a multiprotein complex
            with various postsynaptic density proteins
  JOURNAL   Eur J Neurosci 21 (2), 339-350 (2005)
   PUBMED   15673434
  REMARK    GeneRIF: Discusses cloning and expression of Rat TANC1 and
            preliminary cloning of human TANC1, which resulted in recovery of a
            partial cDNA.
            Erratum:[Eur J Neurosci. 2005 Feb;21(3):825. Usada, Nobuteru
            [corrected to Usuda, Nobuteru]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC010093.8 and AC009307.4.
            
            On Apr 1, 2017 this sequence version replaced XP_016860646.1.
            
            Transcript Variant: This variant (3) encodes isoform 3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2143371.1,
                                           SRR1803617.103866.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1660
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.2"
     Protein         1..1660
                     /product="protein TANC1 isoform 3"
                     /note="rolling pebbles homolog B; TPR domain,
                     ankyrin-repeat and coiled-coil-containing; protein TANC1;
                     tetratricopeptide repeat, ankyrin repeat and coiled-coil
                     domain-containing protein 1"
                     /calculated_mol_wt=181384
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          63..99
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          <320..>621
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
     Region          738..764
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(739..740,743..745,747..748,752,755,764,766,768,
                     772..773,776..778,780..781,785,788,797,799,801,805..806,
                     809..811,813..814,818)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          747..>1004
                     /region_name="PHA03100"
                     /note="ankyrin repeat protein; Provisional; cl39094"
                     /db_xref="CDD:476869"
     Region          766..797
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          878..1084
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          878..908
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          914..941
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          944..974
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(945,949..950,953..955,957..958,962,965,974,976,978,
                     982..983,986..988,990..991,995,998,1007,1009,1011,
                     1015..1016,1019..1021,1023..1024,1028,1031,1040)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          976..1007
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1009..1040
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1042..1067
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1072..>1209
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          1091..1116
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(1092..1093,1096..1097,1099,1136,1139..1140,
                     1143..1144,1146..1147,1170,1173..1174,1177..1178,1181)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          1134..1164
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1169..1197
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..1660
                     /gene="TANC1"
                     /gene_synonym="ROLSB; TANC"
                     /coded_by="NM_001350062.2:269..5251"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:85461"
                     /db_xref="HGNC:HGNC:29364"
                     /db_xref="MIM:611397"
ORIGIN      
        1 mlkavlkksr eggkggkkea gsdfgpetsp vlhldhsads pvsslptaed tyrvslakgv
       61 smslpsspll prqshlvqsr vnkkspgpvr kpkyvesprv pgdavimpfr evakptepde
      121 hatsstkled lsyldgqrna plrtsirlpw hntagarfap ykpqdillkp llfevpsitt
      181 dsvfvgrdwl fhqieenlrn telaenrgav vvgnvgfgkt aiisklvals chgsrmrqia
      241 snspgsspkt sdptqdlhft pllspsssts asstaktplg sisaenqrpr edavkylask
      301 vvayhycqad ntytclvpef vhsiaallcr shqlaayrdl likepqlqsm lslrscvqdp
      361 vaafkrgvle pltnlrneqk ipeeeyiili dglneaefhk pdygdtlssf itkiiskfpa
      421 wlklivtvra nfqeiisalp fvklslddfp dnkdihsdlh ayvqhrvhss qdilsnisln
      481 gkadatligk vsshlvlrsl gsylylkltl dlfqrghlvi ksasykvvpv slselyllqc
      541 nmkfmtqsaf eralpilnva laslhpmtde qifqainagh iqgeqgwedf qqrmdalscf
      601 likrrdktrm fchpsfrewl vwradgenta flceprngha llafmfsrqe gklnrqqtme
      661 lghhilkahi fkglskktgi ssshlqalwi gysteglsaa laslrnlytp nvkvsrllil
      721 gganvnyrte vlnnapilcv qshlgheevv tlllefgacl dgtsengmta lcyaaaaghm
      781 klvclltkkg vrvdhldkkg qcalvhsalr ghgdilqyll tcewspgppq pgtlrkshal
      841 qqaltaaasm ghssvvqcll gmekehevev ngtdtlwget altaaagrgk levcelllgh
      901 gaavsrtnrr gvpplfcaar qghwqivrll lergcdvnls dkqgrtplmv aaceghlstv
      961 efllskgaal ssldkeglsa lswaclkghr avvqylveeg aaidqtdkng rtpldlaafy
     1021 gdaetvlylv ekgaviehvd hsgmrpldra igcrntsvvv allrkgaklg naawamatsk
     1081 pdiliillqk lmeegnvmyk kgkmkeaaqr yqyalrkfpr egfgedmrpf nelrvslyln
     1141 lsrcrrktnd fgmaeefask alelkpksye afyararakr nsrqfvaala dlqeavklcp
     1201 tnqevkrlla rveeeckqlq rsqqqkqqgp lpaplndsen eedtptpgls dhfhseetee
     1261 eetspqeesv sptprsqpss svpssyirnl qeglqskgrp vspqsragig kslrepvaqp
     1321 glllqpskqa qivktsqhlg sgqsavrngs mkvqissqnp ppspmpgria atpagsrtqh
     1381 legtgtfttr agcghfgdrl gpsqnvrlqc gengpahplp sktktterll shssvavdaa
     1441 ppnqgglatc sdvrhpaslt ssgssgspss sikmssstss ltssssfsdg fkvqgpdtri
     1501 kdkvvthvqs gtaehrprnt pfmgimdkta rfqqqsnpps rswhcpapeg lltntssaag
     1561 lqsantekps lmqvggynnq aktcsvstls asvhngaqvk eleeskcqip vhsqenritk
     1621 tvshlyqesi skqqphisne ahrshltaak pkrsfiesnv
//
LOCUS       NP_001137301             335 aa            linear   PRI 21-NOV-2025
DEFINITION  coiled-coil domain-containing protein 68 [Homo sapiens].
ACCESSION   NP_001137301 XP_005266828
VERSION     NP_001137301.1
DBSOURCE    REFSEQ: accession NM_001143829.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Li,Q., Chen,Q., Zheng,T., Wang,F., Teng,J., Zhou,H. and Chen,J.
  TITLE     CCDC68 Maintains Mitotic Checkpoint Activation by Promoting CDC20
            Integration into the MCC
  JOURNAL   Adv Sci (Weinh) 11 (35), e2406009 (2024)
   PUBMED   39018254
  REMARK    GeneRIF: CCDC68 Maintains Mitotic Checkpoint Activation by
            Promoting CDC20 Integration into the MCC.
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Li,X., Li,H., Pei,X., Zhou,Y. and Wei,Z.
  TITLE     CCDC68 Upregulation by IL-6 Promotes Endometrial Carcinoma
            Progression
  JOURNAL   J Interferon Cytokine Res 41 (1), 12-19 (2021)
   PUBMED   33471616
  REMARK    GeneRIF: CCDC68 Upregulation by IL-6 Promotes Endometrial Carcinoma
            Progression.
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 335)
  CONSRTM   Cross-Disorder Group of the Psychiatric Genomics Consortium
  TITLE     Identification of risk loci with shared effects on five major
            psychiatric disorders: a genome-wide analysis
  JOURNAL   Lancet 381 (9875), 1371-1379 (2013)
   PUBMED   23453885
  REMARK    Erratum:[Lancet. 2013 Apr 20;381(9875):1360]
REFERENCE   7  (residues 1 to 335)
  CONSRTM   Schizophrenia Psychiatric Genome-Wide Association Study (GWAS)
            Consortium
  TITLE     Genome-wide association study identifies five new schizophrenia
            loci
  JOURNAL   Nat Genet 43 (10), 969-976 (2011)
   PUBMED   21926974
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 335)
  AUTHORS   Grassi,M.A., Tikhomirov,A., Ramalingam,S., Below,J.E., Cox,N.J. and
            Nicolae,D.L.
  TITLE     Genome-wide meta-analysis for severe diabetic retinopathy
  JOURNAL   Hum Mol Genet 20 (12), 2472-2481 (2011)
   PUBMED   21441570
REFERENCE   9  (residues 1 to 335)
  AUTHORS   Gerhardt,A., Usener,D., Keese,M., Sturm,J., Schadendorf,D. and
            Eichmuller,S.
  TITLE     Tissue expression and sero-reactivity of tumor-specific antigens in
            colorectal cancer
  JOURNAL   Cancer Lett 208 (2), 197-206 (2004)
   PUBMED   15142679
REFERENCE   10 (residues 1 to 335)
  AUTHORS   Eichmuller,S., Usener,D., Dummer,R., Stein,A., Thiel,D. and
            Schadendorf,D.
  TITLE     Serological detection of cutaneous T-cell lymphoma-associated
            antigens
  JOURNAL   Proc Natl Acad Sci U S A 98 (2), 629-634 (2001)
   PUBMED   11149944
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK058097.1, AC098848.7 and AI823801.1.
            
            On Aug 31, 2013 this sequence version replaced XP_005266828.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK058097.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..335
                     /product="coiled-coil domain-containing protein 68"
                     /note="CTCL tumor antigen se57-1; cutaneous T-cell
                     lymphoma associated antigen; CTCL-associated antigen
                     se57-1; cutaneous T-cell lymphoma-associated antigen
                     se57-1"
                     /calculated_mol_wt=38738
     Region          <94..>304
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..335
                     /gene="CCDC68"
                     /gene_synonym="SE57-1"
                     /coded_by="NM_001143829.2:173..1180"
                     /db_xref="CCDS:CCDS11959.1"
                     /db_xref="GeneID:80323"
                     /db_xref="HGNC:HGNC:24350"
                     /db_xref="MIM:616909"
ORIGIN      
        1 mttvtvttei pprdkmedns alyestsahi ieeteyvkki rttlqkirtq mfkdeirhds
       61 tnhkldakhc gnlqqgsdse mdpsccsldl lmkkikgkdl qllemnkene vlkiklqasr
      121 eagaaalrnv aqrlfenyqt qseevrkkqe dskqllqvnk lekeqklkqh venlnqvaek
      181 leekhsqite lenlvqrmek ekrtllerkl slenkllqlk ssatygkscq dlqreisilq
      241 eqishlqfvi hsqhqnlrsv iqemeglknn lkeqdkrien lrekvnilea qnkelktqva
      301 lssetprtkv skavstselk tegvspylml irlrk
//
LOCUS       NP_001334967             796 aa            linear   PRI 21-NOV-2025
DEFINITION  protein PTHB1 isoform 6 [Homo sapiens].
ACCESSION   NP_001334967 XP_016867481
VERSION     NP_001334967.1
DBSOURCE    REFSEQ: accession NM_001348038.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Zhang,Y., Xu,M., Zhang,M., Yang,G. and Li,X.
  TITLE     A Novel BBS9 Mutation Identified via Whole-Exome Sequencing in a
            Chinese Family with Bardet-Biedl Syndrome
  JOURNAL   Biomed Res Int 2021, 4514967 (2021)
   PUBMED   34692830
  REMARK    GeneRIF: A Novel BBS9 Mutation Identified via Whole-Exome
            Sequencing in a Chinese Family with Bardet-Biedl Syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 796)
  AUTHORS   Jeziorny,K., Antosik,K., Jakiel,P., Mlynarski,W., Borowiec,M. and
            Zmyslowska,A.
  TITLE     Next-Generation Sequencing in the Diagnosis of Patients with
            Bardet-Biedl Syndrome-New Variants and Relationship with
            Hyperglycemia and Insulin Resistance
  JOURNAL   Genes (Basel) 11 (11), 1283 (2020)
   PUBMED   33138063
  REMARK    GeneRIF: Next-Generation Sequencing in the Diagnosis of Patients
            with Bardet-Biedl Syndrome-New Variants and Relationship with
            Hyperglycemia and Insulin Resistance.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 796)
  AUTHORS   Nachury,M.V., Loktev,A.V., Zhang,Q., Westlake,C.J., Peranen,J.,
            Merdes,A., Slusarski,D.C., Scheller,R.H., Bazan,J.F.,
            Sheffield,V.C. and Jackson,P.K.
  TITLE     A core complex of BBS proteins cooperates with the GTPase Rab8 to
            promote ciliary membrane biogenesis
  JOURNAL   Cell 129 (6), 1201-1213 (2007)
   PUBMED   17574030
REFERENCE   6  (residues 1 to 796)
  AUTHORS   Nishimura,D.Y., Swiderski,R.E., Searby,C.C., Berg,E.M.,
            Ferguson,A.L., Hennekam,R., Merin,S., Weleber,R.G., Biesecker,L.G.,
            Stone,E.M. and Sheffield,V.C.
  TITLE     Comparative genomics and gene expression analysis identifies BBS9,
            a new Bardet-Biedl syndrome gene
  JOURNAL   Am J Hum Genet 77 (6), 1021-1033 (2005)
   PUBMED   16380913
  REMARK    GeneRIF: Comparative genomics and gene expression analysis
            identifies PHTB1 protein as BBS9, a new Bardet-Biedl syndrome gene.
REFERENCE   7  (residues 1 to 796)
  AUTHORS   Vernon,E.G., Malik,K., Reynolds,P., Powlesland,R., Dallosso,A.R.,
            Jackson,S., Henthorn,K., Green,E.D. and Brown,K.W.
  TITLE     The parathyroid hormone-responsive B1 gene is interrupted by a
            t(1;7)(q42;p15) breakpoint associated with Wilms' tumour
  JOURNAL   Oncogene 22 (9), 1371-1380 (2003)
   PUBMED   12618763
  REMARK    GeneRIF: gene is interrupted by a t(1;7)(q42;p15) breakpoint
            associated with Wilms' tumour; new alternately spliced isoforms
            were found in a wide range of adult and foetal tissues
REFERENCE   8  (residues 1 to 796)
  AUTHORS   Adams,A.E., Rosenblatt,M. and Suva,L.J.
  TITLE     Identification of a novel parathyroid hormone-responsive gene in
            human osteoblastic cells
  JOURNAL   Bone 24 (4), 305-313 (1999)
   PUBMED   10221542
REFERENCE   9  (residues 1 to 796)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 796)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC074338.1, AC007312.1,
            AC087070.2, AC006195.1 and AC078833.5.
            
            On Jan 4, 2017 this sequence version replaced XP_016867481.1.
            
            Summary: This gene is downregulated by parathyroid hormone in
            osteoblastic cells, and therefore is thought to be involved in
            parathyroid hormone action in bones. The exact function of this
            gene has not yet been determined. Alternatively spliced transcript
            variants encoding different isoforms have been identified.
            [provided by RefSeq, Jan 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1968832 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.3"
     Protein         1..796
                     /product="protein PTHB1 isoform 6"
                     /note="protein PTHB1; PTH-responsive osteosarcoma B1
                     protein; bardet-Biedl syndrome 9 protein; parathyroid
                     hormone-responsive B1 gene protein"
                     /calculated_mol_wt=89176
     Region          <2..327
                     /region_name="PHTB1_N"
                     /note="PTHB1 N-terminus; pfam14727"
                     /db_xref="CDD:464284"
     Region          350..728
                     /region_name="PHTB1_C"
                     /note="PTHB1 C-terminus; pfam14728"
                     /db_xref="CDD:464285"
     CDS             1..796
                     /gene="BBS9"
                     /gene_synonym="B1; C18; D1; PTHB1"
                     /coded_by="NM_001348038.3:767..3157"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="GeneID:27241"
                     /db_xref="HGNC:HGNC:30000"
                     /db_xref="MIM:607968"
ORIGIN      
        1 mlhlavlhsr klcvysvsgt lgnvehgnqc qmklmyehnl qrtacnmtyg sfggvkgrdl
       61 iciqsmdgml mvfeqesyaf grflpgfllp gplayssrtd sfltvsscqq vesykyqvla
      121 fatdadkrqe teqqklgsgk rlvvdwtlni geqaldiciv sfnqsassvf vlgernffcl
      181 kdngqirfmk kldwspscfl pycsvsegti ntlignhnnm lhiyqdvtlk watqlphipv
      241 avrvgclhdl kgvivtlsdd ghlqcsylgt dpslfqapnv qsrelnydel dvemkelqki
      301 ikdvnksqgv wpmtereddl nvsvvvspnf dsvsqatdve vgtdlvpsvt vkvtlqnrvi
      361 lqkaklsvyv qppleltcdq ftfefmtpdl trtvsfsvyl krsytpsele gnavvsysrp
      421 tdrnpdgipr viqckfrlpl kliclpgqps ktashkitid tnkspvslls lfpgfasqsd
      481 ddqvnvmgfh flggaritvl asktsqryri qseqfedlwl itnelilrlq eyfekqgvkd
      541 facsfsgsip lqeyfelidh hfelringek leellserav qfraiqrrll arfkdktpap
      601 lqhldtlldg tykqvialad aveenqgnlf qsftrlksat hlvillialw qklsadqvai
      661 leaaflplqe dtqelgweet vdaaishllk tclsksskeq alnlnsqlni pkdtsqlkkh
      721 itllcdrlsk ggrlclstda aapqtmvmpg gcttipesdl eersveqdst elftnhrhlt
      781 aetprpevsp lqgvse
//
LOCUS       NP_001349597             475 aa            linear   PRI 21-NOV-2025
DEFINITION  dnaJ homolog subfamily C member 2 isoform 4 [Homo sapiens].
ACCESSION   NP_001349597 XP_005250326
VERSION     NP_001349597.1
DBSOURCE    REFSEQ: accession NM_001362668.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Yang,F., Hu,A., Guo,Y., Wang,J., Li,D., Wang,X., Jin,S., Yuan,B.,
            Cai,S., Zhou,Y., Li,Q., Chen,G., Gao,H., Zheng,L. and Tong,Q.
  TITLE     p113 isoform encoded by CUX1 circular RNA drives tumor progression
            via facilitating ZRF1/BRD4 transactivation
  JOURNAL   Mol Cancer 20 (1), 123 (2021)
   PUBMED   34579723
  REMARK    GeneRIF: p113 isoform encoded by CUX1 circular RNA drives tumor
            progression via facilitating ZRF1/BRD4 transactivation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Liu,H., Li,J., Zhao,H., Liu,X. and Ye,X.
  TITLE     DNAJC2 is reversely regulated by miR-627-3p, promoting the
            proliferation of colorectal cancer
  JOURNAL   Mol Med Rep 24 (2) (2021)
   PUBMED   34165158
  REMARK    GeneRIF: DNAJC2 is reversely regulated by miR6273p, promoting the
            proliferation of colorectal cancer.
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Hundley,H.A., Walter,W., Bairstow,S. and Craig,E.A.
  TITLE     Human Mpp11 J protein: ribosome-tethered molecular chaperones are
            ubiquitous
  JOURNAL   Science 308 (5724), 1032-1034 (2005)
   PUBMED   15802566
  REMARK    GeneRIF: concluded that Mpp11, an ortholog of yeast Zuo, is a
            ribosome-associated J protein; proposed that in metazoans,
            ribosome-associated Zuo and Mpp11 orthologs recruit cytosolic Hsc70
            to short ribosome-bound nascent chains as they exit the ribosome
REFERENCE   7  (residues 1 to 475)
  AUTHORS   Greiner,J., Ringhoffer,M., Taniguchi,M., Li,L., Schmitt,A.,
            Shiku,H., Dohner,H. and Schmitt,M.
  TITLE     mRNA expression of leukemia-associated antigens in patients with
            acute myeloid leukemia for the development of specific
            immunotherapies
  JOURNAL   Int J Cancer 108 (5), 704-711 (2004)
   PUBMED   14696097
REFERENCE   8  (residues 1 to 475)
  AUTHORS   Greiner,J., Ringhoffer,M., Taniguchi,M., Hauser,T., Schmitt,A.,
            Dohner,H. and Schmitt,M.
  TITLE     Characterization of several leukemia-associated antigens inducing
            humoral immune responses in acute and chronic myeloid leukemia
  JOURNAL   Int J Cancer 106 (2), 224-231 (2003)
   PUBMED   12800198
REFERENCE   9  (residues 1 to 475)
  AUTHORS   Resto,V.A., Caballero,O.L., Buta,M.R., Westra,W.H., Wu,L.,
            Westendorf,J.M., Jen,J., Hieter,P. and Sidransky,D.
  TITLE     A putative oncogenic role for MPP11 in head and neck squamous cell
            cancer
  JOURNAL   Cancer Res 60 (19), 5529-5535 (2000)
   PUBMED   11034098
REFERENCE   10 (residues 1 to 475)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA691752.1, BC056682.1,
            BX279826.1, BC000859.1 and AI140595.1.
            
            On Apr 24, 2018 this sequence version replaced XP_005250326.1.
            
            Summary: This gene is a member of the M-phase phosphoprotein (MPP)
            family. The gene encodes a phosphoprotein with a J domain and a Myb
            DNA-binding domain which localizes to both the nucleus and the
            cytosol. The protein is capable of forming a heterodimeric complex
            that associates with ribosomes, acting as a molecular chaperone for
            nascent polypeptide chains as they exit the ribosome. This protein
            was identified as a leukemia-associated antigen and expression of
            the gene is upregulated in leukemic blasts. Also, chromosomal
            aberrations involving this gene are associated with primary head
            and neck squamous cell tumors. This gene has a pseudogene on
            chromosome 6. Alternatively spliced variants which encode different
            protein isoforms have been described. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (4) contains an alternate exon in
            its 5' UTR, resulting in the use of a downstream start codon
            relative to variant 1. The encoded protein (isoform 3) has a
            shorter N-terminus than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3243570.1,
                                           SRR1803616.145990.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..475
                     /product="dnaJ homolog subfamily C member 2 isoform 4"
                     /note="M-phase phosphoprotein 11; dnaJ homolog subfamily C
                     member 2; zuotin-related factor 1; DnaJ (Hsp40) homolog,
                     subfamily C, member 2"
                     /calculated_mol_wt=55271
     Region          <1..222
                     /region_name="ZUO1"
                     /note="Ribosome-associated chaperone zuotin [Translation,
                     ribosomal structure and biogenesis / Posttranslational
                     modification, protein turnover, chaperones]; COG5269"
                     /db_xref="CDD:227594"
     Region          198..274
                     /region_name="RAC_head"
                     /note="Ribosome-associated complex head domain; pfam16717"
                     /db_xref="CDD:435537"
     Region          307..360
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cd00167"
                     /db_xref="CDD:238096"
     Site            order(308,348..349,351..352,354..356,358..360)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238096"
     Region          407..454
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cd00167"
                     /db_xref="CDD:238096"
     Site            order(408,441..442,444..445,447..449,451..453)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238096"
     CDS             1..475
                     /gene="DNAJC2"
                     /gene_synonym="MPHOSPH11; MPP11; ZRF1; ZUO1"
                     /coded_by="NM_001362668.2:631..2058"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:27000"
                     /db_xref="HGNC:HGNC:13192"
                     /db_xref="MIM:605502"
ORIGIN      
        1 mlsdpvkrra fnsvdptfdn svpskseakd nffevftpvf ernsrwsnkk nvpklgdmns
       61 sfedvdifys fwynfdswre fsyldeeeke kaecrderrw iekqnratra qrkkeemnri
      121 rtlvdnaysc dprikkfkee ekakkeaekk akaeakrkeq eakekqrqae leaarlakek
      181 eeeevrqqal lakkekdiqk kaikkerqkl rnscktwnhf sdneaervkm meeveklcdr
      241 lelaslqcln etltsctkev gkaalekqie eineqirkek eeaearmrqa skntekstgg
      301 ggngsknwse ddlqllikav nlfpagtnsr wevianymni hsssgvkrta kdvigkaksl
      361 qkldphqkdd inkkafdkfk kehgvvpqad natpserfeg pytdftpwtt eeqklleqal
      421 ktypvntper wekiaeavpg rtkkdcmkry kelvemvkak kaaqeqvlna srakk
//
LOCUS       NP_001339540             395 aa            linear   PRI 21-NOV-2025
DEFINITION  propionyl-CoA carboxylase alpha chain, mitochondrial isoform j
            [Homo sapiens].
ACCESSION   NP_001339540 XP_016876107
VERSION     NP_001339540.1
DBSOURCE    REFSEQ: accession NM_001352611.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Wang,J., Cui,M., Liu,Y., Chen,M., Xu,J., Xia,J., Sun,J., Jiang,L.,
            Fang,W., Song,H. and Cheng,C.
  TITLE     The mitochondrial carboxylase PCCA interacts with Listeria
            monocytogenes phospholipase PlcB to modulate bacterial survival
  JOURNAL   Appl Environ Microbiol 90 (6), e0213523 (2024)
   PUBMED   38727222
  REMARK    GeneRIF: The mitochondrial carboxylase PCCA interacts with Listeria
            monocytogenes phospholipase PlcB to modulate bacterial survival.
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Bychkov,I., Galushkin,A., Filatova,A., Nekrasov,A., Kurkina,M.,
            Baydakova,G., Ilyushkina,A., Skoblov,M. and Zakharova,E.
  TITLE     Functional Analysis of the PCCA and PCCB Gene Variants Predicted to
            Affect Splicing
  JOURNAL   Int J Mol Sci 22 (8), 4154 (2021)
   PUBMED   33923806
  REMARK    GeneRIF: Functional Analysis of the PCCA and PCCB Gene Variants
            Predicted to Affect Splicing.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Galarreta Aima,C.I., Shchelochkov,O.A., Jerves Serrano,T. and
            Venditti,C.P.
  TITLE     Propionic Acidemia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22593918
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Kennerknecht,I., Klett,C. and Hameister,H.
  TITLE     Assignment of the human gene propionyl coenzyme A carboxylase,
            alpha-chain, (PCCA) to chromosome 13q32 by in situ hybridization
  JOURNAL   Genomics 14 (2), 550-551 (1992)
   PUBMED   1427880
REFERENCE   8  (residues 1 to 395)
  AUTHORS   Lamhonwah,A.M., Mahuran,D. and Gravel,R.A.
  TITLE     Human mitochondrial propionyl-CoA carboxylase: localization of the
            N-terminus of the pro- and mature alpha chains in the deduced
            primary sequence of a full-length cDNA
  JOURNAL   Nucleic Acids Res 17 (11), 4396 (1989)
   PUBMED   2740237
REFERENCE   9  (residues 1 to 395)
  AUTHORS   Lamhonwah,A.M., Quan,F. and Gravel,R.A.
  TITLE     Sequence homology around the biotin-binding site of human
            propionyl-CoA carboxylase and pyruvate carboxylase
  JOURNAL   Arch Biochem Biophys 254 (2), 631-636 (1987)
   PUBMED   3555348
REFERENCE   10 (residues 1 to 395)
  AUTHORS   Lamhonwah,A.M., Barankiewicz,T.J., Willard,H.F., Mahuran,D.J.,
            Quan,F. and Gravel,R.A.
  TITLE     Isolation of cDNA clones coding for the alpha and beta chains of
            human propionyl-CoA carboxylase: chromosomal assignments and DNA
            polymorphisms associated with PCCA and PCCB genes
  JOURNAL   Proc Natl Acad Sci U S A 83 (13), 4864-4868 (1986)
   PUBMED   3460076
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355338.33, AL356575.8,
            AL353697.21 and AL136526.27.
            
            On Jun 18, 2017 this sequence version replaced XP_016876107.1.
            
            Summary: The protein encoded by this gene is the alpha subunit of
            the heterodimeric mitochondrial enzyme Propionyl-CoA carboxylase.
            PCCA encodes the biotin-binding region of this enzyme. Mutations in
            either PCCA or PCCB (encoding the beta subunit) lead to an enzyme
            deficiency resulting in propionic acidemia. Multiple transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, May 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.67161.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2155590
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q32.3"
     Protein         1..395
                     /product="propionyl-CoA carboxylase alpha chain,
                     mitochondrial isoform j"
                     /EC_number="6.4.1.3"
                     /note="propionyl Coenzyme A carboxylase, alpha
                     polypeptide; propionyl-CoA carboxylase alpha chain,
                     mitochondrial; PCCase alpha subunit; propanoyl-CoA:carbon
                     dioxide ligase alpha subunit; pccA complementation group;
                     propionyl-CoA carboxylase alpha subunit; propionyl CoA
                     carboxylase, alpha polypeptide"
                     /calculated_mol_wt=43409
     Region          <1..197
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          210..320
                     /region_name="PCC_BT"
                     /note="Propionyl-coenzyme A carboxylase BT domain;
                     pfam18140"
                     /db_xref="CDD:465666"
     Region          328..394
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(351,360..362,369)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            361
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
     CDS             1..395
                     /gene="PCCA"
                     /coded_by="NM_001352611.2:895..2082"
                     /note="isoform j is encoded by transcript variant 10"
                     /db_xref="GeneID:5095"
                     /db_xref="HGNC:HGNC:8653"
                     /db_xref="MIM:232000"
ORIGIN      
        1 mgeqavalar avkyssagtv eflvdskknf yflemntrlq vehpvtecit gldlvqemir
       61 vakgyplrhk qadiringwa vecrvyaedp yksfglpsig rlsqyqeplh lpgvrvdsgi
      121 qpgsdisiyy dpmisklity gsdrtealkr madaldnyvi rgvthniall reviinsrfv
      181 kgdistkfls dvypdgfkgh mltkseknql laiasslfva fqlraqhfqe nsrmpvikpd
      241 ianwelsvkl hdkvhtvvas nngsvfsvev dgsklnvtst wnlaspllsv svdgtqrtvq
      301 ykvniltrla aelnkfmlek vtedtssvlr spmpgvvvav svkpgdavae gqeicvieam
      361 kmqnsmtagk tgtvksvhcq agdtvgegdl lvele
//
LOCUS       NP_001552                255 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 9 precursor [Homo
            sapiens].
ACCESSION   NP_001552 XP_011539688
VERSION     NP_001552.2
DBSOURCE    REFSEQ: accession NM_001561.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Ji,X., Huang,G., Peng,Y., Wang,J., Cai,X., Yang,E., Zhu,L., Wu,Y.,
            Sha,W., Wang,F., Shen,L. and Shen,H.
  TITLE     CD137 expression and signal function drive pleiotropic gammadelta
            T-cell effector functions that inhibit intracellular M.
            tuberculosis growth
  JOURNAL   Clin Immunol 266, 110331 (2024)
   PUBMED   39067675
  REMARK    GeneRIF: CD137 expression and signal function drive pleiotropic
            gammadelta T-cell effector functions that inhibit intracellular M.
            tuberculosis growth.
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Solorzano,J.L., Menendez,V., Parra,E., Solis,L., Salazar,R.,
            Garcia-Cosio,M., Climent,F., Fernandez,S., Diaz,E.,
            Francisco-Cruz,A., Khoury,J., Jiang,M., Tamegnon,A., Montalban,C.,
            Melero,I., Wistuba,I., De Andrea,C. and F Garcia,J.
  TITLE     Multiplex spatial analysis reveals increased CD137 expression and
            m-MDSC neighboring tumor cells in refractory classical Hodgkin
            Lymphoma
  JOURNAL   Oncoimmunology 13 (1), 2388304 (2024)
   PUBMED   39135889
  REMARK    GeneRIF: Multiplex spatial analysis reveals increased CD137
            expression and m-MDSC neighboring tumor cells in refractory
            classical Hodgkin Lymphoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Rath,U., Mester,P., Schwarz,H., Schmid,S., Muller,M., Buechler,C.
            and Pavel,V.
  TITLE     Soluble CD137: A Potential Prognostic Biomarker in Critically Ill
            Patients
  JOURNAL   Int J Mol Sci 24 (24), 17518 (2023)
   PUBMED   38139346
  REMARK    GeneRIF: Soluble CD137: A Potential Prognostic Biomarker in
            Critically Ill Patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 255)
  AUTHORS   Wu,Q., Pan,C., Zhou,Y., Wang,S., Xie,L., Zhou,W., Ding,L., Chen,T.,
            Qian,J., Su,R., Gao,X., Mei,Z., Qiao,Y., Yin,S., Wu,Y., Wang,J.,
            Zhou,L. and Zheng,S.
  TITLE     Targeting neuropilin-1 abolishes anti-PD-1-upregulated regulatory T
            cells and synergizes with 4-1BB agonist for liver cancer treatment
  JOURNAL   Hepatology 78 (5), 1402-1417 (2023)
   PUBMED   36811396
  REMARK    GeneRIF: Targeting neuropilin-1 abolishes anti-PD-1-upregulated
            regulatory T cells and synergizes with 4-1BB agonist for liver
            cancer treatment.
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Schwarz,H., Blanco,F.J., von Kempis,J., Valbracht,J. and Lotz,M.
  TITLE     ILA, a member of the human nerve growth factor/tumor necrosis
            factor receptor family, regulates T-lymphocyte proliferation and
            survival
  JOURNAL   Blood 87 (7), 2839-2845 (1996)
   PUBMED   8639902
REFERENCE   7  (residues 1 to 255)
  AUTHORS   Zhou,Z., Kim,S., Hurtado,J., Lee,Z.H., Kim,K.K., Pollok,K.E. and
            Kwon,B.S.
  TITLE     Characterization of human homologue of 4-1BB and its ligand
  JOURNAL   Immunol Lett 45 (1-2), 67-73 (1995)
   PUBMED   7622190
REFERENCE   8  (residues 1 to 255)
  AUTHORS   Alderson,M.R., Smith,C.A., Tough,T.W., Davis-Smith,T.,
            Armitage,R.J., Falk,B., Roux,E., Baker,E., Sutherland,G.R. and
            Din,W.S.
  TITLE     Molecular and biological characterization of human 4-1BB and its
            ligand
  JOURNAL   Eur J Immunol 24 (9), 2219-2227 (1994)
   PUBMED   8088337
REFERENCE   9  (residues 1 to 255)
  AUTHORS   Schwarz,H., Tuckwell,J. and Lotz,M.
  TITLE     A receptor induced by lymphocyte activation (ILA): a new member of
            the human nerve-growth-factor/tumor-necrosis-factor receptor family
  JOURNAL   Gene 134 (2), 295-298 (1993)
   PUBMED   8262389
REFERENCE   10 (residues 1 to 255)
  AUTHORS   Kwon,B.S. and Weissman,S.M.
  TITLE     cDNA sequences of two inducible T-cell genes
  JOURNAL   Proc Natl Acad Sci U S A 86 (6), 1963-1967 (1989)
   PUBMED   2784565
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP381234.1, BC006196.2 and
            AL009183.10.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Aug 13, 2019 this sequence version replaced
            XP_011539688.1, NP_001552.1.
            
            Summary: The protein encoded by this gene is a member of the
            TNF-receptor superfamily. This receptor contributes to the clonal
            expansion, survival, and development of T cells. It can also induce
            proliferation in peripheral monocytes, enhance T cell apoptosis
            induced by TCR/CD3 triggered activation, and regulate CD28
            co-stimulation to promote Th1 cell responses. The expression of
            this receptor is induced by lymphocyte activation. TRAF adaptor
            proteins have been shown to bind to this receptor and transduce the
            signals leading to activation of NF-kappaB. [provided by RefSeq,
            Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853566.146.1, SRR11853564.132.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2149876
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377507.8/ ENSP00000366729.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.23"
     Protein         1..255
                     /product="tumor necrosis factor receptor superfamily
                     member 9 precursor"
                     /note="interleukin-activated receptor, homolog of mouse
                     Ly63; receptor protein 4-1BB; induced by lymphocyte
                     activation (ILA); CD137 antigen; homolog of mouse 4-1BB; T
                     cell antigen ILA; 4-1BB ligand receptor; T-cell antigen
                     4-1BB homolog; tumor necrosis factor receptor superfamily
                     member 9"
                     /calculated_mol_wt=25302
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2615
     Region          23..160
                     /region_name="TNFRSF9"
                     /note="Tumor necrosis factor receptor superfamily member 9
                     (TNFRSF9), also known as CD137; cd13410"
                     /db_xref="CDD:276915"
     Region          23..45
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276915"
     mat_peptide     24..255
                     /product="Tumor necrosis factor receptor superfamily
                     member 9. /id=PRO_0000034577"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07011.1)"
                     /calculated_mol_wt=25302
     Region          24..45
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07011.1)"
     Region          47..86
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07011.1)"
     Region          48..86
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276915"
     Region          87..118
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07011.1)"
     Region          88..117
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276915"
     Region          119..159
                     /region_name="TNFR-Cys 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07011.1)"
     Region          120..158
                     /region_name="CRD4"
                     /note="CRD4 [structural motif]"
                     /db_xref="CDD:276915"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07011.1)"
     Site            149
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07011.1)"
     Region          161..180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07011.1)"
     Site            187..213
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07011.1)"
     Region          214..255
                     /region_name="Interaction with LRR-1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07011.1)"
     CDS             1..255
                     /gene="TNFRSF9"
                     /gene_synonym="4-1BB; CD137; CDw137; ILA; IMD109"
                     /coded_by="NM_001561.6:141..908"
                     /db_xref="CCDS:CCDS92.1"
                     /db_xref="GeneID:3604"
                     /db_xref="HGNC:HGNC:11924"
                     /db_xref="MIM:602250"
ORIGIN      
        1 mgnscyniva tlllvlnfer trslqdpcsn cpagtfcdnn rnqicspcpp nsfssaggqr
       61 tcdicrqckg vfrtrkecss tsnaecdctp gfhclgagcs mceqdckqgq eltkkgckdc
      121 cfgtfndqkr gicrpwtncs ldgksvlvng tkerdvvcgp spadlspgas svtppapare
      181 pghspqiisf flaltstall fllffltlrf svvkrgrkkl lyifkqpfmr pvqttqeedg
      241 cscrfpeeee ggcel
//
LOCUS       NP_001371756            1059 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 79 [Homo sapiens].
ACCESSION   NP_001371756
VERSION     NP_001371756.1
DBSOURCE    REFSEQ: accession NM_001384827.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1059)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1059)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1059)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1059)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1059)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1059)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1059)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1059)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1059)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1059)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2156236.1,
                                           SRR14038194.2243631.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1059
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1059
                     /product="microtubule-associated protein 4 isoform 79"
                     /note="MAP-4"
                     /calculated_mol_wt=111284
     Region          <653..906
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <907..928
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          930..959
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          961..991
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1059
                     /gene="MAP4"
                     /coded_by="NM_001384827.1:96..3275"
                     /note="isoform 79 is encoded by transcript variant 82"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgsp tefleekmay qeypnsqnwp
      121 edtnfcfqpe qvvdpiqtdp fkmyhdddla dlvfpssata dtsifagqnd plkdsygmsp
      181 cntavvpqgw svealnsphs esfvspeava eppqptavpl elakeiemas eerppaqale
      241 immglkttdm apsketemal akdmalatkt evalakdmes ptkldvtlak dmqpsmesdm
      301 alvkdmelpt ekevalvkdv rwptetdvss aknvvlptet evapakdvtl lketeraspi
      361 kmdlapskdm gppkenkket eraspikmdl apskdmgppk enkivpakdl vllseievaq
      421 andiisstei ssaekvalss etevalardm tlppetnvil tkdkalplea evapvkdmaq
      481 lpeteiapak dvapstvkev gllkdmspls etemalgkdv tpppetevvl iknvclppem
      541 evaltedqvp alkteaplak dgvltlannv tpakdvppls eteatpvpik dmeiaqtqkg
      601 isedshlesl qdvgqsaapt fmispetvtg tgkkcslpae edsvleklge rkpcnsqpse
      661 lssetsgiar peegrpvvsg tgndittppn kelppspekk tkqpapttig glnkkpmsla
      721 sglvpaappk rpavasarps ilpskdvkpk piadakapek raspskpasa pasrsgskst
      781 qtvaktttaa avastgpssr spstllpkkp taiktegkpa evkkmtaksv padlsrpkst
      841 stssmkkttt lsgtapaagv vpsrvkatpm psrpsttpfi dkkptsakps sttprlsrla
      901 tntsapdlkn vrskvgsten ikhqpgggrv qiqnkkvdis kvsskcgska nikhkpgggd
      961 vkiesqklnf kekaqakvgs ldnvghlpag gavktegggs eaplcpgppa geepaiseaa
     1021 peagaptsas glnghptlsg ggdqreaqtl dsqiqetsi
//
LOCUS       NP_001378826            1536 aa            linear   PRI 21-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4 gamma 3 isoform 7 [Homo
            sapiens].
ACCESSION   NP_001378826
VERSION     NP_001378826.1
DBSOURCE    REFSEQ: accession NM_001391897.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1536)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1536)
  AUTHORS   Kang,J.Y., Wen,Z., Pan,D., Zhang,Y., Li,Q., Zhong,A., Yu,X.,
            Wu,Y.C., Chen,Y., Zhang,X., Kou,P.C., Geng,J., Wang,Y.Y., Hua,M.M.,
            Zong,R., Li,B., Shi,H.J., Li,D., Fu,X.D., Li,J., Nelson,D.L.,
            Guo,X., Zhou,Y., Gou,L.T., Huang,Y. and Liu,M.F.
  TITLE     LLPS of FXR1 drives spermiogenesis by activating translation of
            stored mRNAs
  JOURNAL   Science 377 (6607), eabj6647 (2022)
   PUBMED   35951695
REFERENCE   3  (residues 1 to 1536)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1536)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 1536)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1536)
  AUTHORS   Waskiewicz,A.J., Johnson,J.C., Penn,B., Mahalingam,M., Kimball,S.R.
            and Cooper,J.A.
  TITLE     Phosphorylation of the cap-binding protein eukaryotic translation
            initiation factor 4E by protein kinase Mnk1 in vivo
  JOURNAL   Mol Cell Biol 19 (3), 1871-1880 (1999)
   PUBMED   10022874
REFERENCE   7  (residues 1 to 1536)
  AUTHORS   Pyronnet,S., Imataka,H., Gingras,A.C., Fukunaga,R., Hunter,T. and
            Sonenberg,N.
  TITLE     Human eukaryotic translation initiation factor 4G (eIF4G) recruits
            mnk1 to phosphorylate eIF4E
  JOURNAL   EMBO J 18 (1), 270-279 (1999)
   PUBMED   9878069
REFERENCE   8  (residues 1 to 1536)
  AUTHORS   Gingras,A.C., Raught,B. and Sonenberg,N.
  TITLE     eIF4 initiation factors: effectors of mRNA recruitment to ribosomes
            and regulators of translation
  JOURNAL   Annu Rev Biochem 68, 913-963 (1999)
   PUBMED   10872469
  REMARK    Review article
REFERENCE   9  (residues 1 to 1536)
  AUTHORS   Imataka,H., Gradi,A. and Sonenberg,N.
  TITLE     A newly identified N-terminal amino acid sequence of human eIF4G
            binds poly(A)-binding protein and functions in poly(A)-dependent
            translation
  JOURNAL   EMBO J 17 (24), 7480-7489 (1998)
   PUBMED   9857202
REFERENCE   10 (residues 1 to 1536)
  AUTHORS   Gradi,A., Imataka,H., Svitkin,Y.V., Rom,E., Raught,B., Morino,S.
            and Sonenberg,N.
  TITLE     A novel functional human eukaryotic translation initiation factor
            4G
  JOURNAL   Mol Cell Biol 18 (1), 334-342 (1998)
   PUBMED   9418880
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031005.2, AL627311.16,
            AL358392.19 and AL606477.11.
            
            Summary: The protein encoded by this gene is thought to be part of
            the eIF4F protein complex, which is involved in mRNA cap
            recognition and transport of mRNAs to the ribosome. Interestingly,
            a microRNA (miR-520c-3p) has been found that negatively regulates
            synthesis of the encoded protein, and this leads to a global
            decrease in protein translation and cell proliferation. Therefore,
            this protein is a key component of the anti-tumor activity of
            miR-520c-3p. [provided by RefSeq, May 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038193.3143236.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1536
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     Protein         1..1536
                     /product="eukaryotic translation initiation factor 4 gamma
                     3 isoform 7"
                     /note="eIF-4-gamma 3; eIF-4-gamma II"
                     /calculated_mol_wt=171069
     Region          <107..>322
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          706..934
                     /region_name="MIF4G"
                     /note="MIF4G domain; pfam02854"
                     /db_xref="CDD:397130"
     Region          1173..1285
                     /region_name="MA3"
                     /note="MA3 domain; pfam02847"
                     /db_xref="CDD:397128"
     Region          1379..1507
                     /region_name="W2_eIF4G1_like"
                     /note="C-terminal W2 domain of eukaryotic translation
                     initiation factor 4 gamma 1 and similar proteins; cd11559"
                     /db_xref="CDD:211397"
     Region          <1486..1532
                     /region_name="W2"
                     /note="C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon;
                     cl17013"
                     /db_xref="CDD:473053"
     CDS             1..1536
                     /gene="EIF4G3"
                     /gene_synonym="eIF-4G 3; eIF4G 3; eIF4GII"
                     /coded_by="NM_001391897.1:902..5512"
                     /note="isoform 7 is encoded by transcript variant 10"
                     /db_xref="GeneID:8672"
                     /db_xref="HGNC:HGNC:3298"
                     /db_xref="MIM:603929"
ORIGIN      
        1 mmvnhlpmpy pvpqgpqyci pqyrhsgppy vgppqqypvq ppgpgpfypg pgpgdfpnay
       61 gtpfypsqpv yqsapiivpt qqqpppakre kktirirdpn qggkditeei msgggsrnpt
      121 ppigrptstp tppqlpsqvp ehspvvygtv esahlaastp vtaasdqkqe ekpkpdpvlk
      181 spspvlrlvl sgekkeqegq tsettaivsi aelplppspt tvssvarsti aaptssalss
      241 qpifttaidd rcelsspred tipipsltsc tetsdplptn endddickkp csvapndipl
      301 vsstnlinei ngvseklsat esiveivkqe vlpltlelei lenppeemkl ecipapitps
      361 tvpsfpptpp tppaspphtp vivpaaattv sspsaaitvq rvleedesir tclsedakei
      421 qnkieveadg qteeildsqn lnsrrspvpa qiaitvpktw kkpkdrtrtt eemleaelel
      481 kaeeelsidk vleseqdkms qgfhperdps dlkkvkavee ngeeaepvrn gaesvsegeg
      541 idansgstds sgdgvtfpfk peswkptdte gkkqydrefl ldfqfmpaci qkpeglppis
      601 dvvldkinqp klpmrtldpr ilprgpdftp afadfgrqtp ggrgvpllnv gsrrsqpgqr
      661 reprkiitvs vkedvhlkka enawkpsqkr dsqaddpeni ktqelfrkvr silnkltpqm
      721 fnqlmkqvsg ltvdteerlk gvidlvfeka idepsfsvay anmcrclvtl kvpmadkpgn
      781 tvnfrkllln rcqkefekdk adddvfekkq keleaasape ertrlhdele eakdkarrrs
      841 ignikfigel fklkmlteai mhdcvvkllk nhdeeslecl crllttigkd ldfekakprm
      901 dqyfnqmeki vkerktssri rfmlqdvidl rlcnwvsrra dqgpktieqi hkeakieeqe
      961 eqrkvqqlmt kekrrpgvqr vdeggwntvq gaknsrvldp skflkitkpt idekiqlvpk
     1021 aqlgswgkgs sggakasetd alrssassln rfsalqppap sgstpstpve fdsrrtltsr
     1081 gsmgrekndk plpsatarpn tfmrggsskd lldnqsqeeq rremletvkq ltggvdvern
     1141 steaernktr esakpeisam sahdkaalse eelerksksi ideflhindf keamqcveel
     1201 naqgllhvfv rvgvestler sqitrdhmgq llyqlvqsek lskqdffkgf setleladdm
     1261 aidiphiwly laelvtpmlk eggismrelt iefskpllpv gragvllsei lhllckqmsh
     1321 kkvgalwrea dlswkdflpe gedvhnflle qkldfiesds pcssealskk elsaeelykr
     1381 lekliiedka ndeqifdwve anldeiqmss ptflralmta vckaaiiads stfrvdtavi
     1441 kqrvpillky ldsdtekelq alyalqasiv kldqpanllr mffdclydee visedafykw
     1501 esskdpaeqn gkgvalksvt afftwlreae eesedn
//
LOCUS       NP_001362650             430 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform xx [Homo sapiens].
ACCESSION   NP_001362650 XP_016858628
VERSION     NP_001362650.1
DBSOURCE    REFSEQ: accession NM_001375721.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 430)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 430)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 430)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 430)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 430)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            On Oct 31, 2019 this sequence version replaced XP_016858628.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1758642.1,
                                           SRR18074969.3559953.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..430
                     /product="abl interactor 2 isoform xx"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=47373
     Region          48..111
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          369..429
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(377,379,382,386,404..405,418,420..421)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..430
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375721.1:333..1625"
                     /note="isoform xx is encoded by transcript variant 55"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 mscrcwisrh psyegwnlqs iifhkqirgv dlestfvtkf gnncslrlne tvdihkekva
       61 rreigilttn kntsrthkii apanlerpvr yirkpidyti lddighgvkv stqnmkmggl
      121 prttpptqkp psppmsgkgt lgrhspyrtl epvrppvvpn dyvpsptrnm apsqqspvrt
      181 asvnqrnrty sssgssggsh pssrsssren sgsgsvgvpi avptpsppsv fpghpvqfys
      241 mnrpasrhtp ptiggslpyr rppsitsqts lqnqmnggpf ysqnpvslap pppsilqvtp
      301 qlplmgfvar vqenisdtpp ppppveepvf desppppppp edyeeeeaav veysdpyaee
      361 dppwaprsyl ekvvaiydyt kdkedelsfq egaiiyvikk nddgwyegvm ngvtglfpgn
      421 yvesimhyse
//
LOCUS       NP_001077377             789 aa            linear   PRI 21-NOV-2025
DEFINITION  protein kintoun isoform 2 [Homo sapiens].
ACCESSION   NP_001077377
VERSION     NP_001077377.1
DBSOURCE    REFSEQ: accession NM_001083908.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 789)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 789)
  AUTHORS   Dong,L., Zhang,L., Li,X., Mei,S., Shen,Y., Fu,L., Zhao,S., Tang,X.
            and Tang,Y.
  TITLE     Clinical and genetic analysis of two patients with primary ciliary
            dyskinesia caused by a novel variant of DNAAF2
  JOURNAL   BMC Pediatr 23 (1), 616 (2023)
   PUBMED   38053031
  REMARK    GeneRIF: Clinical and genetic analysis of two patients with primary
            ciliary dyskinesia caused by a novel variant of DNAAF2.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 789)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 789)
  AUTHORS   Sun,M., Zhang,Y., JiyunYang, Wang,Y., Tan,H., Wang,H., Lei,T.,
            Li,X., Zhang,X., Xiong,W., Dou,K. and Ma,Y.
  TITLE     Novel compound heterozygous DNAAF2 mutations cause primary ciliary
            dyskinesia in a Han Chinese family
  JOURNAL   J Assist Reprod Genet 37 (9), 2159-2170 (2020)
   PUBMED   32638265
  REMARK    GeneRIF: Novel compound heterozygous DNAAF2 mutations cause primary
            ciliary dyskinesia in a Han Chinese family.
REFERENCE   5  (residues 1 to 789)
  AUTHORS   Maurizy,C., Quinternet,M., Abel,Y., Verheggen,C., Santo,P.E.,
            Bourguet,M., C F Paiva,A., Bragantini,B., Chagot,M.E., Robert,M.C.,
            Abeza,C., Fabre,P., Fort,P., Vandermoere,F., M F Sousa,P.,
            Rain,J.C., Charpentier,B., Cianferani,S., Bandeiras,T.M.,
            Pradet-Balade,B., Manival,X. and Bertrand,E.
  TITLE     The RPAP3-Cterminal domain identifies R2TP-like quaternary
            chaperones
  JOURNAL   Nat Commun 9 (1), 2093 (2018)
   PUBMED   29844425
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 789)
  AUTHORS   Tarkar,A., Loges,N.T., Slagle,C.E., Francis,R., Dougherty,G.W.,
            Tamayo,J.V., Shook,B., Cantino,M., Schwartz,D., Jahnke,C.,
            Olbrich,H., Werner,C., Raidt,J., Pennekamp,P., Abouhamed,M.,
            Hjeij,R., Kohler,G., Griese,M., Li,Y., Lemke,K., Klena,N., Liu,X.,
            Gabriel,G., Tobita,K., Jaspers,M., Morgan,L.C., Shapiro,A.J.,
            Letteboer,S.J., Mans,D.A., Carson,J.L., Leigh,M.W., Wolf,W.E.,
            Chen,S., Lucas,J.S., Onoufriadis,A., Plagnol,V., Schmidts,M.,
            Boldt,K., Roepman,R., Zariwala,M.A., Lo,C.W., Mitchison,H.M.,
            Knowles,M.R., Burdine,R.D., Loturco,J.J. and Omran,H.
  CONSRTM   UK10K
  TITLE     DYX1C1 is required for axonemal dynein assembly and ciliary
            motility
  JOURNAL   Nat Genet 45 (9), 995-1003 (2013)
   PUBMED   23872636
REFERENCE   7  (residues 1 to 789)
  AUTHORS   Orvedahl,A., Sumpter,R. Jr., Xiao,G., Ng,A., Zou,Z., Tang,Y.,
            Narimatsu,M., Gilpin,C., Sun,Q., Roth,M., Forst,C.V., Wrana,J.L.,
            Zhang,Y.E., Luby-Phelps,K., Xavier,R.J., Xie,Y. and Levine,B.
  TITLE     Image-based genome-wide siRNA screen identifies selective autophagy
            factors
  JOURNAL   Nature 480 (7375), 113-117 (2011)
   PUBMED   22020285
REFERENCE   8  (residues 1 to 789)
  AUTHORS   Omran,H., Kobayashi,D., Olbrich,H., Tsukahara,T., Loges,N.T.,
            Hagiwara,H., Zhang,Q., Leblond,G., O'Toole,E., Hara,C., Mizuno,H.,
            Kawano,H., Fliegauf,M., Yagi,T., Koshida,S., Miyawaki,A.,
            Zentgraf,H., Seithe,H., Reinhardt,R., Watanabe,Y., Kamiya,R.,
            Mitchell,D.R. and Takeda,H.
  TITLE     Ktu/PF13 is required for cytoplasmic pre-assembly of axonemal
            dyneins
  JOURNAL   Nature 456 (7222), 611-616 (2008)
   PUBMED   19052621
  REMARK    GeneRIF: Ktu/PF13 is one of the long-sought proteins involved in
            pre-assembly of dynein arm complexes in the cytoplasm before
            intraflagellar transport loads them for the ciliary compartment.
REFERENCE   9  (residues 1 to 789)
  AUTHORS   Heilig,R., Eckenberg,R., Petit,J.L., Fonknechten,N., Da Silva,C.,
            Cattolico,L., Levy,M., Barbe,V., de Berardinis,V., Ureta-Vidal,A.,
            Pelletier,E., Vico,V., Anthouard,V., Rowen,L., Madan,A., Qin,S.,
            Sun,H., Du,H., Pepin,K., Artiguenave,F., Robert,C., Cruaud,C.,
            Bruls,T., Jaillon,O., Friedlander,L., Samson,G., Brottier,P.,
            Cure,S., Segurens,B., Aniere,F., Samain,S., Crespeau,H., Abbasi,N.,
            Aiach,N., Boscus,D., Dickhoff,R., Dors,M., Dubois,I., Friedman,C.,
            Gouyvenoux,M., James,R., Madan,A., Mairey-Estrada,B., Mangenot,S.,
            Martins,N., Menard,M., Oztas,S., Ratcliffe,A., Shaffer,T.,
            Trask,B., Vacherie,B., Bellemere,C., Belser,C., Besnard-Gonnet,M.,
            Bartol-Mavel,D., Boutard,M., Briez-Silla,S., Combette,S.,
            Dufosse-Laurent,V., Ferron,C., Lechaplais,C., Louesse,C.,
            Muselet,D., Magdelenat,G., Pateau,E., Petit,E.,
            Sirvain-Trukniewicz,P., Trybou,A., Vega-Czarny,N., Bataille,E.,
            Bluet,E., Bordelais,I., Dubois,M., Dumont,C., Guerin,T.,
            Haffray,S., Hammadi,R., Muanga,J., Pellouin,V., Robert,D.,
            Wunderle,E., Gauguet,G., Roy,A., Sainte-Marthe,L., Verdier,J.,
            Verdier-Discala,C., Hillier,L., Fulton,L., McPherson,J.,
            Matsuda,F., Wilson,R., Scarpelli,C., Gyapay,G., Wincker,P.,
            Saurin,W., Quetier,F., Waterston,R., Hood,L. and Weissenbach,J.
  TITLE     The DNA sequence and analysis of human chromosome 14
  JOURNAL   Nature 421 (6923), 601-607 (2003)
   PUBMED   12508121
  REMARK    Erratum:[Nature. 2023 Aug;620(7973):E17. doi:
            10.1038/s41586-023-06403-y. PMID: 37491470]
REFERENCE   10 (residues 1 to 789)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139099.3.
            
            Summary: This gene encodes a highly conserved protein involved in
            the preassembly of dynein arm complexes which power cilia. These
            complexes are found in some cilia and are assembled in the
            cytoplasm prior to transport for cilia formation. Mutations in this
            gene have been associated with primary ciliary dyskinesia. Multiple
            transcript variants encoding different isoforms have been found for
            this gene.[provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon, compared to variant 1, resulting in a shorter protein
            (isoform 2), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC011400.1, SRR14038195.102394.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2161836, SAMEA2467143
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q21.3"
     Protein         1..789
                     /product="protein kintoun isoform 2"
                     /note="kintoun; protein kintoun; dynein assembly factor 2,
                     axonemal"
                     /calculated_mol_wt=85469
     Region          43..209
                     /region_name="PIH1"
                     /note="PIH1 N-terminal domain; pfam08190"
                     /db_xref="CDD:369738"
     Region          250..349
                     /region_name="PIH1_CS"
                     /note="PIH1 CS-like domain; pfam18201"
                     /db_xref="CDD:408028"
     CDS             1..789
                     /gene="DNAAF2"
                     /gene_synonym="C14orf104; CILD10; KTU; PF13"
                     /coded_by="NM_001083908.2:96..2465"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45100.1"
                     /db_xref="GeneID:55172"
                     /db_xref="HGNC:HGNC:20188"
                     /db_xref="MIM:612517"
ORIGIN      
        1 makaaasssl edldlsgeev qrltsafqdp efrrmfsqya eeltdpenrr ryeaeitale
       61 rergvevrfv hpepghvlrt sldgarrcfv nvcsnalvga pssrpgsggd rgaapgshws
      121 lpyslapgre yagrsssrym vydvvfhpda lalarrhegf rqmldatale avekqfgvkl
      181 drrnaktlka kykgtpeaav lrtplpgvip arpdgepkgp lpdfpypyqy paapgpraps
      241 ppeaalqpap teprysvvqr hhvdlqdyrc srdsapspvp helvitielp llrsaeqaal
      301 evtrkllcld srkpdyrlrl slpypvddgr gkaqfnkarr qlvvtlpvvl paarrepava
      361 vaaaapeesa drsgtdgqac asaregeagp arsraedggh dtcvagaags gvttlgdpev
      421 apppaaagee rvpkpgeqdl srhagsppgs veepspggen spggggspcl ssrslawgss
      481 agresargds svetreeseg tggqrsacam ggpgtksgep lcppllcnqd ketltlliqv
      541 priqpqslqg dlnplwyklr fsaqdlvysf flqfapenkl sttepvisis snnavielak
      601 speshghwre wyygvnndsl elqecsnsdq lqgkeervne eshltekeyi ehcntpttds
      661 dssiavkalq idsfglvtcf qqesldvsqm ilgksqqpes kmqsefikek satcsneekd
      721 nlnesvitee ketdgdhlss llnkttvhni pgfdsiketn mqdgsvqvik dhvtncafsf
      781 qnsllydld
//
LOCUS       NP_001362617             473 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform bb [Homo sapiens].
ACCESSION   NP_001362617 XP_016858615
VERSION     NP_001362617.1
DBSOURCE    REFSEQ: accession NM_001375688.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 473)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 473)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 473)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 473)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 473)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 473)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            On Oct 31, 2019 this sequence version replaced XP_016858615.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2722088.1,
                                           SRR14038192.1248706.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..473
                     /product="abl interactor 2 isoform bb"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=52114
     Region          93..156
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          412..472
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(420,422,425,429,447..448,461,463..464)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..473
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375688.1:122..1543"
                     /note="isoform bb is encoded by transcript variant 33"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqs adkqraleet kayttqslas
       61 vaylintlan nvlqmldiqa sqlrrmessi nhisqtvdih kekvarreig ilttnkntsr
      121 thkiiapanl erpvryirkp idytilddig hgvkvstqnm kmgglprttp ptqkppsppm
      181 sgkgtlgrhs pyrtlepvrp pvvpndyvps ptrnmapsqq spvrtasvnq rnrtysssgs
      241 sggshpssrs ssrensgsgs vgvpiavptp sppsvfpghp vqfysmnrpa srhtpptigg
      301 slpyrrppsi tsqtslqnqm nggpfysqnp vslappppsi lqvtpqlplm gfvarvqenn
      361 tppppppvee pvfdespppp pppedyeeee aavveysdpy aeedppwapr sylekvvaiy
      421 dytkdkedel sfqegaiiyv ikknddgwye gvmngvtglf pgnyvesimh yse
//
LOCUS       NP_001104792             882 aa            linear   PRI 21-NOV-2025
DEFINITION  ATP-dependent RNA helicase DDX54 isoform 1 [Homo sapiens].
ACCESSION   NP_001104792
VERSION     NP_001104792.1
DBSOURCE    REFSEQ: accession NM_001111322.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 882)
  AUTHORS   Zhang,Y., Guo,H. and Zhang,H.
  TITLE     SNHG10/DDX54/PBX3 Feedback Loop Contributes to Gastric Cancer Cell
            Growth
  JOURNAL   Dig Dis Sci 66 (6), 1875-1884 (2021)
   PUBMED   32712782
  REMARK    GeneRIF: SNHG10/DDX54/PBX3 Feedback Loop Contributes to Gastric
            Cancer Cell Growth.
REFERENCE   2  (residues 1 to 882)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 882)
  AUTHORS   Paine,I., Posey,J.E., Grochowski,C.M., Jhangiani,S.N.,
            Rosenheck,S., Kleyner,R., Marmorale,T., Yoon,M., Wang,K.,
            Robison,R., Cappuccio,G., Pinelli,M., Magli,A., Coban Akdemir,Z.,
            Hui,J., Yeung,W.L., Wong,B.K.Y., Ortega,L., Bekheirnia,M.R.,
            Bierhals,T., Hempel,M., Johannsen,J., Santer,R., Aktas,D.,
            Alikasifoglu,M., Bozdogan,S., Aydin,H., Karaca,E., Bayram,Y.,
            Ityel,H., Dorschner,M., White,J.J., Wilichowski,E., Wortmann,S.B.,
            Casella,E.B., Kitajima,J.P., Kok,F., Monteiro,F., Muzny,D.M.,
            Bamshad,M., Gibbs,R.A., Sutton,V.R., Van Esch,H.,
            Brunetti-Pierri,N., Hildebrandt,F., Brautbar,A., Van den
            Veyver,I.B., Glass,I., Lessel,D., Lyon,G.J. and Lupski,J.R.
  CONSRTM   University of Washington Center for Mendelian Genomics,
            Baylor-Hopkins Center for Mendelian Genomics, Telethon Undiagnosed
            Diseases Program
  TITLE     Paralog Studies Augment Gene Discovery: DDX and DHX Genes
  JOURNAL   Am J Hum Genet 105 (2), 302-316 (2019)
   PUBMED   31256877
  REMARK    GeneRIF: Missense mutation in DDX54 gene is associated with
            neurodevelopmental disorder.
REFERENCE   4  (residues 1 to 882)
  AUTHORS   Aslibekyan,S., An,P., Frazier-Wood,A.C., Kabagambe,E.K.,
            Irvin,M.R., Straka,R.J., Tiwari,H.K., Tsai,M.Y., Hopkins,P.N.,
            Borecki,I.B., Ordovas,J.M. and Arnett,D.K.
  TITLE     Preliminary evidence of genetic determinants of adiponectin
            response to fenofibrate in the Genetics of Lipid Lowering Drugs and
            Diet Network
  JOURNAL   Nutr Metab Cardiovasc Dis 23 (10), 987-994 (2013)
   PUBMED   23149075
REFERENCE   5  (residues 1 to 882)
  AUTHORS   Zhan,R., Yamamoto,M., Ueki,T., Yoshioka,N., Tanaka,K., Morisaki,H.,
            Seiwa,C., Yamamoto,Y., Kawano,H., Tsuruo,Y., Watanabe,K., Asou,H.
            and Aiso,S.
  TITLE     A DEAD-box RNA helicase Ddx54 protein in oligodendrocytes is
            indispensable for myelination in the central nervous system
  JOURNAL   J Neurosci Res 91 (3), 335-348 (2013)
   PUBMED   23239230
  REMARK    GeneRIF: Ddx54 plays an important role in central nervous system
            myelination, presumably in myelin sheath formation after the
            differentiation of oligodendrocytes.
REFERENCE   6  (residues 1 to 882)
  AUTHORS   Satoh,J., Nanri,Y. and Yamamura,T.
  TITLE     Rapid identification of 14-3-3-binding proteins by protein
            microarray analysis
  JOURNAL   J Neurosci Methods 152 (1-2), 278-288 (2006)
   PUBMED   16260042
  REMARK    GeneRIF: Identifies dead box polypeptide 54 as a 14-3-3-binding
            protein.
REFERENCE   7  (residues 1 to 882)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
  REMARK    GeneRIF: Kinetic analysis of DEAD box helicases, including DEAD box
            polypeptide 54, in response to transcription inhibition.
REFERENCE   8  (residues 1 to 882)
  AUTHORS   Rajendran,R.R., Nye,A.C., Frasor,J., Balsara,R.D., Martini,P.G. and
            Katzenellenbogen,B.S.
  TITLE     Regulation of nuclear receptor transcriptional activity by a novel
            DEAD box RNA helicase (DP97)
  JOURNAL   J Biol Chem 278 (7), 4628-4638 (2003)
   PUBMED   12466272
REFERENCE   9  (residues 1 to 882)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
  REMARK    GeneRIF: Identifies DEAD box polypeptide 54 (similar to RIKEN cDNA
            2410015A15 gene) as one of 213 different nucleolar proteins in HeLa
            cells.
REFERENCE   10 (residues 1 to 882)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
  REMARK    GeneRIF: Identifies DEAD (Asp-Glu-Ala-Asp) box polypeptide 54
            (locus 79039) as a novel nucleolar protein in HeLa cells.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF478457.1 and BC005848.2.
            
            Summary: This gene encodes a member of the DEAD box protein family.
            DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this family
            are believed to be involved in embryogenesis, spermatogenesis, and
            cellular growth and division. The nucleolar protein encoded by this
            gene interacts in a hormone-dependent manner with nuclear
            receptors, and represses their transcriptional activity.
            Alternative splice variants that encode different isoforms have
            been found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF478457.1, SRR7346977.1630778.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..882
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.13"
     Protein         1..882
                     /product="ATP-dependent RNA helicase DDX54 isoform 1"
                     /EC_number="3.6.4.13"
                     /note="DEAD box helicase 97 KDa; ATP-dependent RNA
                     helicase DDX54; DEAD box protein 54; DEAD box RNA helicase
                     97 kDa; ATP-dependent RNA helicase DP97; DEAD
                     (Asp-Glu-Ala-Asp) box polypeptide 54; apoptosis related
                     protein 5; DEAD box polypeptide, 97kD"
                     /calculated_mol_wt=98535
     Region          1..78
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDD1.2)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8TDD1.2)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8TDD1.2)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8TDD1.2)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDD1.2)"
     Region          96..300
                     /region_name="DEADc_DDX54"
                     /note="DEAD-box helicase domain of DEAD box protein 54;
                     cd17959"
                     /db_xref="CDD:350717"
     Region          96..124
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDD1.2)"
     Region          98..>524
                     /region_name="PRK04537"
                     /note="ATP-dependent RNA helicase RhlB; Provisional"
                     /db_xref="CDD:235307"
     Site            order(115..116,118..120,123,141..148)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350717"
     Region          247..250
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDD1.2)"
     Region          596..698
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDD1.2)"
     Region          605..647
                     /region_name="Interaction with nuclear receptors"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDD1.2)"
     Site            644
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TDD1.2)"
     Site            696
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8TDD1.2)"
     Site            698
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8TDD1.2)"
     Region          714..774
                     /region_name="DBP10CT"
                     /note="DBP10CT (NUC160) domain; pfam08147"
                     /db_xref="CDD:462373"
     Site            782
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8TDD1.2)"
     Site            788
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TDD1.2)"
     CDS             1..882
                     /gene="DDX54"
                     /gene_synonym="DP97"
                     /coded_by="NM_001111322.2:28..2676"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44984.1"
                     /db_xref="GeneID:79039"
                     /db_xref="HGNC:HGNC:20084"
                     /db_xref="MIM:611665"
ORIGIN      
        1 maadkgpaag prsraamaqw rkkkglrkrr gaasqargsd sedgefeiqa eddararklg
       61 pgrplptfpt sectsdvepd tremvraqnk kkkksggfqs mglsypvfkg imkkgykvpt
      121 piqrktipvi ldgkdvvama rtgsgktacf llpmferlkt hsaqtgaral ilsptrelal
      181 qtlkftkelg kftglktali lggdrmedqf aalhenpdii iatpgrlvhv avemslklqs
      241 veyvvfdead rlfemgfaeq lqeiiarlpg ghqtvlfsat lpkllvefar agltepvlir
      301 ldvdtklneq lktsfflvre dtkaavllhl lhnvvrpqdq tvvfvatkhh aeyltelltt
      361 qrvscahiys aldptarkin lakftlgkcs tlivtdlaar gldiplldnv inysfpakgk
      421 lflhrvgrva ragrsgtays lvapdeipyl ldlhlflgrs ltlarplkep sgvagvdgml
      481 grvpqsvvde edsglqstle aslelrglar vadnaqqqyv rsrpapspes ikrakemdlv
      541 glglhplfss rfeeeelqrl rlvdsiknyr sratifeina ssrdlcsqvm rakrqkdrka
      601 iarfqqgqqg rqeqqegpvg papsrpalqe kqpekeeeee agesvedifs evvgrkrqrs
      661 gpnrgakrrr eearqrdqef yipyrpkdfd serglsisge ggafeqqaag avldlmgdea
      721 qnltrgrqql kwdrkkkrfv gqsgqedkkk iktesgryis ssykrdlyqk wkqkqkiddr
      781 dsdeegasdr rgperrggkr drgqagasrp hapgtpagrv rpelktkqqi lkqrrraqkl
      841 hflqrgglkq lsarnrrrvq elqqgafgrg arskkgkmrk rm
//
LOCUS       NP_001371667            1164 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 14 [Homo sapiens].
ACCESSION   NP_001371667
VERSION     NP_001371667.1
DBSOURCE    REFSEQ: accession NM_001384738.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1164)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1164)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1164)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1164)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1164)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1164)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1164)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1847917.1,
                                           SRR14038196.1874375.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1164
                     /product="microtubule-associated protein 4 isoform 14"
                     /note="MAP-4"
                     /calculated_mol_wt=121967
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          260..557
                     /region_name="17 X 14 AA tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          374..413
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            396
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            519
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            538
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            583
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          <587..931
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            592
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          653..1003
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            699
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            708
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10791892,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            725
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            735
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            799
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10791892,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            809
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            815
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            837
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            839
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            865
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            940
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          <943..964
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            953
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            954
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          1004..1034
                     /region_name="Tau/MAP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1004..1033
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            1012
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          1035..1065
                     /region_name="Tau/MAP 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1035..1064
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          1066..1097
                     /region_name="Tau/MAP 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1066..1096
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            1085
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1086..1164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            1157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            1163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     CDS             1..1164
                     /gene="MAP4"
                     /coded_by="NM_001384738.1:96..3590"
                     /note="isoform 14 is encoded by transcript variant 19"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttges kslgmasgsg sptefleekm
      121 ayqeypnsqn wpedtnfcfq peqvvdpiqt dpfkmyhddd ladlvfpssa tadtsifagq
      181 ndplkdsygm spcntavvpq gwsvealnsp hsesfvspea vaeppqptav plelakeiem
      241 aseerppaqa leimmglktt dmapsketem alakdmalat ktevalakdm esptkldvtl
      301 akdmqpsmes dmalvkdmel ptekevalvk dvrwptetdv ssaknvvlpt etevapakdv
      361 tllketeras pikmdlapsk dmgppkenkk eteraspikm dlapskdmgp pkenkivpak
      421 dlvllseiev aqandiisst eissaekval ssetevalar dmtlppetnv iltkdkalpl
      481 eaevapvkdm aqlpeteiap akdvapstvk evgllkdmsp lsetemalgk dvtpppetev
      541 vliknvclpp emevaltedq vpalkteapl akdgvltlan nvtpakdvpp lseteatpvp
      601 ikdmeiaqtq kgisedshle slqdvgqsaa ptfmispetv tgtgkkcslp aeedsvlekl
      661 gerkpcnsqp selssetsgi arpeegrpvv sgtgndittp pnkelppspe kktkplattq
      721 paktstskak tqptslpkqp apttigglnk kpmslasglv paappkrpav asarpsilps
      781 kdvkpkpiad akapekrasp skpasapasr sgskstqtva ktttaaavas tgpssrspst
      841 llpkkptaik tegkpaevkk mtaksvpadl srpkststss mkktttlsgt apaagvvpsr
      901 vkatpmpsrp sttpfidkkp tsakpssttp rlsrlatnts apdlknvrsk vgstenikhq
      961 pgggrakvek kteaaattrk pesnavtkta gpiasaqkqp agkvqivskk vsyshiqskc
     1021 gskdnikhvp gggnvqiqnk kvdiskvssk cgskanikhk pgggdvkies qklnfkekaq
     1081 akvgsldnvg hlpaggavkt egggseaplc pgppageepa iseaapeaga ptsasglngh
     1141 ptlsgggdqr eaqtldsqiq etsi
//
LOCUS       NP_671711                188 aa            linear   PRI 21-NOV-2025
DEFINITION  Kv channel-interacting protein 4 isoform 3 [Homo sapiens].
ACCESSION   NP_671711
VERSION     NP_671711.1
DBSOURCE    REFSEQ: accession NM_147182.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Mosley,J.D., Shaffer,C.M., Van Driest,S.L., Weeke,P.E., Wells,Q.S.,
            Karnes,J.H., Velez Edwards,D.R., Wei,W.Q., Teixeira,P.L.,
            Bastarache,L., Crawford,D.C., Li,R., Manolio,T.A., Bottinger,E.P.,
            McCarty,C.A., Linneman,J.G., Brilliant,M.H., Pacheco,J.A.,
            Thompson,W., Chisholm,R.L., Jarvik,G.P., Crosslin,D.R.,
            Carrell,D.S., Baldwin,E., Ralston,J., Larson,E.B., Grafton,J.,
            Scrol,A., Jouni,H., Kullo,I.J., Tromp,G., Borthwick,K.M.,
            Kuivaniemi,H., Carey,D.J., Ritchie,M.D., Bradford,Y., Verma,S.S.,
            Chute,C.G., Veluchamy,A., Siddiqui,M.K., Palmer,C.N., Doney,A.,
            MahmoudPour,S.H., Maitland-van der Zee,A.H., Morris,A.D.,
            Denny,J.C. and Roden,D.M.
  TITLE     A genome-wide association study identifies variants in KCNIP4
            associated with ACE inhibitor-induced cough
  JOURNAL   Pharmacogenomics J 16 (3), 231-237 (2016)
   PUBMED   26169577
  REMARK    GeneRIF: Results indicate that SNPs in KCNIP4 may modulate ACE
            inhibitor-induced cough risk.
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 188)
  AUTHORS   Kitazawa,M., Kubo,Y. and Nakajo,K.
  TITLE     The stoichiometry and biophysical properties of the Kv4 potassium
            channel complex with K+ channel-interacting protein (KChIP)
            subunits are variable, depending on the relative expression level
  JOURNAL   J Biol Chem 289 (25), 17597-17609 (2014)
   PUBMED   24811166
  REMARK    GeneRIF: Subunit counting by single-molecule imaging revealed that
            the bound number of KChIP4 in each Kv4.2.KChIP4 complex was
            dependent on the expression level of KChIP4.
REFERENCE   6  (residues 1 to 188)
  AUTHORS   Bonne,A., Vreede,L., Kuiper,R.P., Bodmer,D., Jansen,C., Eleveld,M.,
            van Erp,F., Arkesteijn,G., Hoogerbrugge,N., van Ravenswaaij,C.,
            Schoenmakers,E.F. and Geurts van Kessel,A.
  TITLE     Mapping of constitutional translocation breakpoints in renal cell
            cancer patients: identification of KCNIP4 as a candidate gene
  JOURNAL   Cancer Genet Cytogenet 179 (1), 11-18 (2007)
   PUBMED   17981209
  REMARK    GeneRIF: Mutation of KCNIP4 is associated with renal cell
            carcinoma.
REFERENCE   7  (residues 1 to 188)
  AUTHORS   Chen,C.P., Lee,L. and Chang,L.S.
  TITLE     Effects of metal-binding properties of human Kv channel-interacting
            proteins on their molecular structure and binding with Kv4.2
            channel
  JOURNAL   Protein J 25 (5), 345-351 (2006)
   PUBMED   16951992
  REMARK    GeneRIF: The conformational change with metal-bound KChIP4.1 is
            crucial for its interaction with Kv channel but not for KChIP2.2,
            and that the Mg2+- and Ca2+-binding properties of KChIP2.2 and
            KChIP4.1 have different effects on their molecular structure.
REFERENCE   8  (residues 1 to 188)
  AUTHORS   Pruunsild,P. and Timmusk,T.
  TITLE     Structure, alternative splicing, and expression of the human and
            mouse KCNIP gene family
  JOURNAL   Genomics 86 (5), 581-593 (2005)
   PUBMED   16112838
REFERENCE   9  (residues 1 to 188)
  AUTHORS   Morohashi,Y., Hatano,N., Ohya,S., Takikawa,R., Watabiki,T.,
            Takasugi,N., Imaizumi,Y., Tomita,T. and Iwatsubo,T.
  TITLE     Molecular cloning and characterization of CALP/KChIP4, a novel
            EF-hand protein interacting with presenilin 2 and voltage-gated
            potassium channel subunit Kv4
  JOURNAL   J Biol Chem 277 (17), 14965-14975 (2002)
   PUBMED   11847232
  REMARK    GeneRIF: cloning and investigation of interaction with presenilin 2
            and voltage-gated potassium channel subunit Kv4
REFERENCE   10 (residues 1 to 188)
  AUTHORS   Holmqvist,M.H., Cao,J., Hernandez-Pineda,R., Jacobson,M.D.,
            Carroll,K.I., Sung,M.A., Betty,M., Ge,P., Gilbride,K.J.,
            Brown,M.E., Jurman,M.E., Lawson,D., Silos-Santiago,I., Xie,Y.,
            Covarrubias,M., Rhodes,K.J., Distefano,P.S. and An,W.F.
  TITLE     Elimination of fast inactivation in Kv4 A-type potassium channels
            by an auxiliary subunit domain
  JOURNAL   Proc Natl Acad Sci U S A 99 (2), 1035-1040 (2002)
   PUBMED   11805342
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC113606.3, BI596848.1,
            AY029176.1, AC104065.3 and BX648990.1.
            
            Summary: This gene encodes a member of the family of voltage-gated
            potassium (Kv) channel-interacting proteins (KCNIPs), which belong
            to the recoverin branch of the EF-hand superfamily. Members of the
            KCNIP family are small calcium binding proteins. They all have
            EF-hand-like domains, and differ from each other in the N-terminus.
            They are integral subunit components of native Kv4 channel
            complexes. They may regulate A-type currents, and hence neuronal
            excitability, in response to changes in intracellular calcium. This
            protein member also interacts with presenilin. Multiple
            alternatively spliced transcript variants encoding distinct
            isoforms have been identified for this gene. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (3) has an alternate exon which
            lacks an in-frame start codon, as compared to variant 1. Use of a
            downstream start codon results in an isoform (3, also known as
            KCHIP4.3) that has a shorter N-terminus, as compared to isoform 1.
            Variants 3 and 6 encode the same isoform (3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803617.57109.1, SRR1803614.206532.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2156099 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.31-p15.2"
     Protein         1..188
                     /product="Kv channel-interacting protein 4 isoform 3"
                     /note="calsenilin-like protein; a-type potassium channel
                     modulatory protein 4; Kv channel interacting protein 4"
                     /calculated_mol_wt=21814
     Region          37..84
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cl08302"
                     /db_xref="CDD:415501"
     Region          <66..173
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..188
                     /gene="KCNIP4"
                     /gene_synonym="CALP; KCHIP4"
                     /coded_by="NM_147182.4:338..904"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS47035.1"
                     /db_xref="GeneID:80333"
                     /db_xref="HGNC:HGNC:30083"
                     /db_xref="MIM:608182"
ORIGIN      
        1 matvrhrpea lelleaqskf tkkelqilyr gfknecpsgv vneetfkeiy sqffpqgdst
       61 tyahflfnaf dtdhngavsf edfikglsil lrgtvqekln wafnlydink dgyitkeeml
      121 dimkaiydmm gkctypvlke daprqhvetf fqkmdknkdg vvtidefies cqkdenimrs
      181 mqlfenvi
//
LOCUS       NP_001365343            1089 aa            linear   PRI 21-NOV-2025
DEFINITION  histone deacetylase 4 isoform 1 [Homo sapiens].
ACCESSION   NP_001365343 XP_006712941
VERSION     NP_001365343.1
DBSOURCE    REFSEQ: accession NM_001378414.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Liu,W. and Luo,G.
  TITLE     NEDD9 is transcriptionally regulated by HDAC4 and promotes breast
            cancer metastasis and macrophage M2 polarization via the
            FAK/NF-kappaB signaling pathway
  JOURNAL   Neoplasia 57, 101059 (2024)
   PUBMED   39326322
  REMARK    GeneRIF: NEDD9 is transcriptionally regulated by HDAC4 and promotes
            breast cancer metastasis and macrophage M2 polarization via the
            FAK/NF-kappaB signaling pathway.
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1089)
  AUTHORS   Di Giorgio,E., Dalla,E., Tolotto,V., D'Este,F., Paluvai,H.,
            Ranzino,L. and Brancolini,C.
  TITLE     HDAC4 influences the DNA damage response and counteracts senescence
            by assembling with HDAC1/HDAC2 to control H2BK120 acetylation and
            homology-directed repair
  JOURNAL   Nucleic Acids Res 52 (14), 8218-8240 (2024)
   PUBMED   38874468
  REMARK    GeneRIF: HDAC4 influences the DNA damage response and counteracts
            senescence by assembling with HDAC1/HDAC2 to control H2BK120
            acetylation and homology-directed repair.
REFERENCE   5  (residues 1 to 1089)
  AUTHORS   Chen,Q. and Lao,J.
  TITLE     Interference with Histone Deacetylase 4 Regulates c-Jun N-terminal
            Kinase/Activating Protein-1 Signaling to Ameliorate Sepsis-induced
            Alveolar Epithelial Cell Injury
  JOURNAL   J Physiol Investig 67 (4), 174-186 (2024)
   PUBMED   39133038
  REMARK    GeneRIF: Interference with Histone Deacetylase 4 Regulates c-Jun
            N-terminal Kinase/Activating Protein-1 Signaling to Ameliorate
            Sepsis-induced Alveolar Epithelial Cell Injury.
REFERENCE   6  (residues 1 to 1089)
  AUTHORS   Pazin,M.J. and Kadonaga,J.T.
  TITLE     What's up and down with histone deacetylation and transcription?
  JOURNAL   Cell 89 (3), 325-328 (1997)
   PUBMED   9150131
  REMARK    Review article
REFERENCE   7  (residues 1 to 1089)
  AUTHORS   Wolffe,A.P.
  TITLE     Transcriptional control. Sinful repression
  JOURNAL   Nature 387 (6628), 16-17 (1997)
   PUBMED   9139815
REFERENCE   8  (residues 1 to 1089)
  AUTHORS   Ohara,O., Nagase,T., Ishikawa,K., Nakajima,D., Ohira,M., Seki,N.
            and Nomura,N.
  TITLE     Construction and characterization of human brain cDNA libraries
            suitable for analysis of cDNA clones encoding relatively large
            proteins
  JOURNAL   DNA Res 4 (1), 53-59 (1997)
   PUBMED   9179496
REFERENCE   9  (residues 1 to 1089)
  AUTHORS   Wilson,L.C., Leverton,K., Oude Luttikhuis,M.E., Oley,C.A.,
            Flint,J., Wolstenholme,J., Duckett,D.P., Barrow,M.A., Leonard,J.V.,
            Read,A.P. et al.
  TITLE     Brachydactyly and mental retardation: an Albright hereditary
            osteodystrophy-like syndrome localized to 2q37
  JOURNAL   Am J Hum Genet 56 (2), 400-407 (1995)
   PUBMED   7847374
REFERENCE   10 (residues 1 to 1089)
  AUTHORS   Doherty,E.S. and Lacbawan,F.L.
  TITLE     2q37 Microdeletion Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301337
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC062017.6 and AC017028.11.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 12, 2020 this sequence version replaced XP_006712941.1.
            
            Summary: Histones play a critical role in transcriptional
            regulation, cell cycle progression, and developmental events.
            Histone acetylation/deacetylation alters chromosome structure and
            affects transcription factor access to DNA. The protein encoded by
            this gene belongs to class II of the histone deacetylase/acuc/apha
            family. It possesses histone deacetylase activity and represses
            transcription when tethered to a promoter. This protein does not
            bind DNA directly, but through transcription factors MEF2C and
            MEF2D. It seems to interact in a multiprotein complex with RbAp48
            and HDAC3. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853566.16775.1,
                                           SRR14038194.3429702.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000543185.6/ ENSP00000440481.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..1089
                     /product="histone deacetylase 4 isoform 1"
                     /EC_number="3.5.1.98"
                     /note="histone deacetylase A"
                     /calculated_mol_wt=119574
     Region          <91..152
                     /region_name="ClassIIa_HDAC4_Gln-rich-N"
                     /note="Glutamine-rich N-terminal helical domain of HDAC4,
                     a Class IIa histone deacetylase; cd10162"
                     /db_xref="CDD:197398"
     Site            order(93,97,108..109,112,119,123..124)
                     /site_type="other"
                     /note="dimer interface A, B [polypeptide binding]"
                     /db_xref="CDD:197398"
     Region          118..313
                     /region_name="Interaction with MEF2A.
                     /evidence=ECO:0000269|PubMed:10487761"
                     /note="propagated from UniProtKB/Swiss-Prot (P56524.3)"
     Region          133..166
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56524.3)"
     Region          206..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56524.3)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NZM9; propagated from
                     UniProtKB/Swiss-Prot (P56524.3)"
     Region          240..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56524.3)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK4 and SIK1.
                     /evidence=ECO:0000269|PubMed:10958686; propagated from
                     UniProtKB/Swiss-Prot (P56524.3)"
     Region          349..354
                     /region_name="PxLPxI/L motif, mediates interaction with
                     ANKRA2 and 14-3-3 proteins.
                     /evidence=ECO:0000269|PubMed:22649097"
                     /note="propagated from UniProtKB/Swiss-Prot (P56524.3)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22649097,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P56524.3)"
     Site            472
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK4 and SIK1.
                     /evidence=ECO:0000269|PubMed:10958686; propagated from
                     UniProtKB/Swiss-Prot (P56524.3)"
     Region          514..536
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56524.3)"
     Region          553..590
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56524.3)"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NZM9; propagated from
                     UniProtKB/Swiss-Prot (P56524.3)"
     Region          631..651
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56524.3)"
     Site            637
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK4.
                     /evidence=ECO:0000269|PubMed:10958686,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P56524.3)"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P56524.3)"
     Region          654..1062
                     /region_name="HDAC4"
                     /note="Histone deacetylase 4; cd10006"
                     /db_xref="CDD:212530"
     Region          660..1089
                     /region_name="Histone deacetylase"
                     /note="propagated from UniProtKB/Swiss-Prot (P56524.3)"
     Site            order(807..808,816..817,845,847,939,979)
                     /site_type="active"
                     /db_xref="CDD:212530"
     Region          1056..1089
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P56524.3)"
     Region          1066..1089
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56524.3)"
     CDS             1..1089
                     /gene="HDAC4"
                     /gene_synonym="AHO3; BDMR; HA6116; HD4; HDAC-4; HDAC-A;
                     HDACA; NEDCHF; NEDCHID"
                     /coded_by="NM_001378414.1:263..3532"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS92981.1"
                     /db_xref="GeneID:9759"
                     /db_xref="HGNC:HGNC:14063"
                     /db_xref="MIM:605314"
ORIGIN      
        1 mssqshpdgl sgrdqpvell nparvnhmps tvdvatalpl qvapsavpmd lrldhqfslp
       61 vaepalreqq lqqellalkq kqqiqrqili aefqrqheql srqheaqlhe hikqqqemla
      121 mkhqqelleh qrklerhrqe qelekqhreq klqqlknkek gkesavaste vkmklqefvl
      181 nkkkalahrn lnhcissdpr ywygktqhss ldqssppqsg vstsynhpvl gmydakddfp
      241 lrktasepnl klrsrlkqkv aerrsspllr rkdgpvvtal kkrpldvtds acssapgsgp
      301 sspnnssgsv saengiapav psipaetsla hrlvaregsa aplplytsps lpnitlglpa
      361 tgpsagtagq qdaerltlpa lqqrlslfpg thltpylsts plerdggaah spllqhmvll
      421 eqppaqaplv tdwylsglga lplhaqslvg adrvspsihk lrqhrplgrt qsaplpqnaq
      481 alqhlviqqq hqqflekhkq qfqqqqlqmn kiipkpsepa rqpeshpeet eeelrehqal
      541 ldepyldrlp gqkeahaqag vqvkqepies deeeaeppre vepgqrqpse qellfrqqal
      601 lleqqrihql rnyqasmeaa gipvsfgghr plsraqsspa satfpvsvqe pptkprfttg
      661 lvydtlmlkh qctcgssssh pehagriqsi wsrlqetglr gkcecirgrk atleelqtvh
      721 seahtllygt nplnrqklds kkllgslasv fvrlpcggvg vdsdtiwnev hsagaarlav
      781 gcvvelvfkv atgelkngfa vvrppghhae estpmgfcyf nsvavaakll qqrlsvskil
      841 ivdwdvhhgn gtqqafysdp svlymslhry ddgnffpgsg apdevgtgpg vgfnvnmaft
      901 ggldppmgda eylaafrtvv mpiasefapd vvlvssgfda veghptplgg ynlsarcfgy
      961 ltkqlmglag grivlalegg hdltaicdas eacvsallgn eldplpekvl qqrpnanavr
     1021 smekvmeihs kywrclqrtt stagrsliea qtceneeaet vtamaslsvg vkpaekrpde
     1081 epmeeeppl
//
LOCUS       NP_001306006              96 aa            linear   PRI 21-NOV-2025
DEFINITION  high mobility group protein HMG-I/HMG-Y isoform b [Homo sapiens].
ACCESSION   NP_001306006
VERSION     NP_001306006.1
DBSOURCE    REFSEQ: accession NM_001319077.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Olan,I., Ando-Kuri,M., Parry,A.J., Handa,T., Schoenfelder,S.,
            Fraser,P., Ohkawa,Y., Kimura,H., Narita,M. and Narita,M.
  TITLE     HMGA1 orchestrates chromatin compartmentalization and sequesters
            genes into 3D networks coordinating senescence heterogeneity
  JOURNAL   Nat Commun 15 (1), 6891 (2024)
   PUBMED   39134516
  REMARK    GeneRIF: HMGA1 orchestrates chromatin compartmentalization and
            sequesters genes into 3D networks coordinating senescence
            heterogeneity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 96)
  AUTHORS   Li,K.J., Hong,Y., Yu,Y.Z., Xie,Z., Lv,D.J., Wang,C., Xie,T.,
            Chen,H., Chen,Z.S., Zeng,J. and Zhao,S.C.
  TITLE     NAT10 Promotes Prostate Cancer Growth and Metastasis by Acetylating
            mRNAs of HMGA1 and KRT8
  JOURNAL   Adv Sci (Weinh) 11 (32), e2310131 (2024)
   PUBMED   38922788
  REMARK    GeneRIF: NAT10 Promotes Prostate Cancer Growth and Metastasis by
            Acetylating mRNAs of HMGA1 and KRT8.
REFERENCE   4  (residues 1 to 96)
  AUTHORS   Wang,L., Zhang,J., Xia,M., Liu,C., Zu,X. and Zhong,J.
  TITLE     High Mobility Group A1 (HMGA1): Structure, Biological Function, and
            Therapeutic Potential
  JOURNAL   Int J Biol Sci 18 (11), 4414-4431 (2022)
   PUBMED   35864955
  REMARK    GeneRIF: High Mobility Group A1 (HMGA1): Structure, Biological
            Function, and Therapeutic Potential.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 96)
  AUTHORS   Sumter,T.F., Xian,L., Huso,T., Koo,M., Chang,Y.T., Almasri,T.N.,
            Chia,L., Inglis,C., Reid,D. and Resar,L.M.
  TITLE     The High Mobility Group A1 (HMGA1) Transcriptome in Cancer and
            Development
  JOURNAL   Curr Mol Med 16 (4), 353-393 (2016)
   PUBMED   26980699
  REMARK    Review article
REFERENCE   6  (residues 1 to 96)
  AUTHORS   Friedmann,M., Holth,L.T., Zoghbi,H.Y. and Reeves,R.
  TITLE     Organization, inducible-expression and chromosome localization of
            the human HMG-I(Y) nonhistone protein gene
  JOURNAL   Nucleic Acids Res 21 (18), 4259-4267 (1993)
   PUBMED   8414980
REFERENCE   7  (residues 1 to 96)
  AUTHORS   Nissen,M.S., Langan,T.A. and Reeves,R.
  TITLE     Phosphorylation by cdc2 kinase modulates DNA binding activity of
            high mobility group I nonhistone chromatin protein
  JOURNAL   J Biol Chem 266 (30), 19945-19952 (1991)
   PUBMED   1939057
REFERENCE   8  (residues 1 to 96)
  AUTHORS   Reeves,R. and Nissen,M.S.
  TITLE     The A.T-DNA-binding domain of mammalian high mobility group I
            chromosomal proteins. A novel peptide motif for recognizing DNA
            structure
  JOURNAL   J Biol Chem 265 (15), 8573-8582 (1990)
   PUBMED   1692833
REFERENCE   9  (residues 1 to 96)
  AUTHORS   Eckner,R. and Birnstiel,M.L.
  TITLE     Cloning of cDNAs coding for human HMG I and HMG Y proteins: both
            are capable of binding to the octamer sequence motif
  JOURNAL   Nucleic Acids Res 17 (15), 5947-5959 (1989)
   PUBMED   2505228
REFERENCE   10 (residues 1 to 96)
  AUTHORS   Johnson,K.R., Lehn,D.A. and Reeves,R.
  TITLE     Alternative processing of mRNAs encoding mammalian chromosomal
            high-mobility-group proteins HMG-I and HMG-Y
  JOURNAL   Mol Cell Biol 9 (5), 2114-2123 (1989)
   PUBMED   2701943
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA049639.1, M23616.1,
            AL354740.29 and BC008832.2.
            
            Summary: This gene encodes a chromatin-associated protein involved
            in the regulation of gene transcription, integration of
            retroviruses into chromosomes, and the metastatic progression of
            cancer cells. The encoded protein preferentially binds to the minor
            groove of AT-rich regions in double-stranded DNA. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. Pseudogenes of this gene have been identified on
            multiple chromosomes. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (8) uses an alternate splice site
            in the 5' UTR and uses an alternate in-frame splice site compared
            to variant 1. It encodes isoform b (also called HMG-Y), which is
            shorter than isoform a. Variants 2, 4, 5, 7, and 8 encode the same
            isoform (b).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M23616.1, SRR6380197.116229.17
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2147920
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..96
                     /product="high mobility group protein HMG-I/HMG-Y isoform
                     b"
                     /note="nonhistone chromosomal high-mobility group protein
                     HMG-I/HMG-Y; high mobility group protein HMG-I/HMG-Y; high
                     mobility group protein R; high mobility group protein A1"
                     /calculated_mol_wt=10548
     CDS             1..96
                     /gene="HMGA1"
                     /gene_synonym="HMG-R; HMGA1A; HMGIY"
                     /coded_by="NM_001319077.2:248..538"
                     /note="isoform b is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS4788.1"
                     /db_xref="GeneID:3159"
                     /db_xref="HGNC:HGNC:5010"
                     /db_xref="MIM:600701"
ORIGIN      
        1 msessskssq plaskqekdg tekrgrgrpr kqppkepsev ptpkrprgrp kgsknkgaak
       61 trkttttpgr kprgrpkkle keeeegisqe sseeeq
//
LOCUS       NP_001308638             757 aa            linear   PRI 21-NOV-2025
DEFINITION  diacylglycerol kinase iota isoform 3 [Homo sapiens].
ACCESSION   NP_001308638
VERSION     NP_001308638.1
DBSOURCE    REFSEQ: accession NM_001321709.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 757)
  AUTHORS   Bai,M., Ke,S., Yu,H., Xu,Y., Yu,Y., Lu,S., Wang,C., Huang,J.,
            Ma,Y., Dai,W. and Wu,Y.
  TITLE     Key molecules associated with thyroid carcinoma prognosis: A study
            based on transcriptome sequencing and GEO datasets
  JOURNAL   Front Immunol 13, 964891 (2022)
   PUBMED   36059514
  REMARK    GeneRIF: Key molecules associated with thyroid carcinoma prognosis:
            A study based on transcriptome sequencing and GEO datasets.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 757)
  AUTHORS   Etcheverry,A., Aubry,M., Idbaih,A., Vauleon,E., Marie,Y., Menei,P.,
            Boniface,R., Figarella-Branger,D., Karayan-Tapon,L., Quillien,V.,
            Sanson,M., de Tayrac,M., Delattre,J.Y. and Mosser,J.
  TITLE     DGKI methylation status modulates the prognostic value of MGMT in
            glioblastoma patients treated with combined radio-chemotherapy with
            temozolomide
  JOURNAL   PLoS One 9 (9), e104455 (2014)
   PUBMED   25233099
  REMARK    GeneRIF: the DGKI methylation status identified 22% of poorly
            responding patients in the low-risk group
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 757)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   5  (residues 1 to 757)
  AUTHORS   Zhang,C. and Pierce,B.L.
  TITLE     Genetic susceptibility to accelerated cognitive decline in the US
            Health and Retirement Study
  JOURNAL   Neurobiol Aging 35 (6), 1512 (2014)
   PUBMED   24468470
REFERENCE   6  (residues 1 to 757)
  AUTHORS   Yang,J., Seo,J., Nair,R., Han,S., Jang,S., Kim,K., Han,K.,
            Paik,S.K., Choi,J., Lee,S., Bae,Y.C., Topham,M.K., Prescott,S.M.,
            Rhee,J.S., Choi,S.Y. and Kim,E.
  TITLE     DGKiota regulates presynaptic release during mGluR-dependent LTD
  JOURNAL   EMBO J 30 (1), 165-180 (2011)
   PUBMED   21119615
REFERENCE   7  (residues 1 to 757)
  AUTHORS   Moskvina,V., Craddock,N., Holmans,P., Nikolov,I., Pahwa,J.S.,
            Green,E., Owen,M.J. and O'Donovan,M.C.
  CONSRTM   Wellcome Trust Case Control Consortium
  TITLE     Gene-wide analyses of genome-wide association data sets: evidence
            for multiple common risk alleles for schizophrenia and bipolar
            disorder and for overlap in genetic risk
  JOURNAL   Mol Psychiatry 14 (3), 252-260 (2009)
   PUBMED   19065143
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 757)
  AUTHORS   Bex,C., Knauth,K., Dambacher,S. and Buchberger,A.
  TITLE     A yeast two-hybrid system reconstituting substrate recognition of
            the von Hippel-Lindau tumor suppressor protein
  JOURNAL   Nucleic Acids Res 35 (21), e142 (2007)
   PUBMED   17986458
REFERENCE   9  (residues 1 to 757)
  AUTHORS   Bowne,S.J., Sullivan,L.S., Ding,L., Traer,E., Prescott,S.M.,
            Birch,D.G., Kennan,A., Humphries,P. and Daiger,S.P.
  TITLE     Evaluation of human diacylglycerol kinase(iota), DGKI, a homolog of
            Drosophila rdgA, in inherited retinopathy mapping to 7q
  JOURNAL   Mol Vis 6, 6-9 (2000)
   PUBMED   10706894
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 757)
  AUTHORS   Ding,L., Traer,E., McIntyre,T.M., Zimmerman,G.A. and Prescott,S.M.
  TITLE     The cloning and characterization of a novel human diacylglycerol
            kinase, DGKiota
  JOURNAL   J Biol Chem 273 (49), 32746-32752 (1998)
   PUBMED   9830018
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022173.7, AB209167.1,
            DR002813.1, AF061936.1, DA696180.1, AC078842.2 and AW237608.1.
            
            Summary: This gene is a member of the type IV diacylglycerol kinase
            subfamily.  Diacylglycerol kinases regulate the intracellular
            concentration of diacylglycerol through its phosphorylation,
            producing phosphatidic acid.  The specific role of the enzyme
            encoded by this gene is undetermined, however, it may play a
            crucial role in the production of phosphatidic acid in the retina
            or in recessive forms of retinal degeneration. [provided by RefSeq,
            Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.107799.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q33"
     Protein         1..757
                     /product="diacylglycerol kinase iota isoform 3"
                     /EC_number="2.7.1.107"
                     /note="DAG kinase iota; diglyceride kinase iota"
                     /calculated_mol_wt=84834
     Region          <1..23
                     /region_name="C1"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     superfamily; cl00040"
                     /db_xref="CDD:412127"
     Region          78..199
                     /region_name="DAGKc"
                     /note="Diacylglycerol kinase catalytic domain (presumed);
                     smart00046"
                     /db_xref="CDD:214487"
     Region          226..383
                     /region_name="DAGKa"
                     /note="Diacylglycerol kinase accessory domain (presumed);
                     smart00045"
                     /db_xref="CDD:214486"
     Region          617..648
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <621..756
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(650,652,656..657,660..662,664..665,669,672,683,685,
                     688,692..693,696..698,700..701,705,708,717,719,721,
                     725..726,729..731,733..734,738)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          650..683
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          685..717
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..757
                     /gene="DGKI"
                     /gene_synonym="DGK-IOTA"
                     /coded_by="NM_001321709.2:681..2954"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:9162"
                     /db_xref="HGNC:HGNC:2855"
                     /db_xref="MIM:604072"
ORIGIN      
        1 mlhhieepcs lgahaavivp ptwiikvkkp qnslkasnrk kkrtsfkrka skrgmeqenk
       61 grpfvikpis splmkpllvf vnpksggnqg tkvlqmfmwy lnprqvfdls qegpkdalel
      121 yrkvpnlril acggdgtvgw ilsildelql spqppvgvlp lgtgndlart lnwgggytde
      181 pvskilcqve dgtvvqldrw nlhvernpdl ppeeledgvc klplnvfnny fslgfdahvt
      241 lefhesrean pekfnsrfrn kmfyagaafs dflqrssrdl skhvkvvcdg tdltpkiqel
      301 kfqcivflni prycagtmpw gnpgdhhdfe pqrhddgyie vigftmasla alqvgghger
      361 lhqcrevmll tyksipmqvd gepcrlapam irislrnqan mvqkskrrts mpllndpqsv
      421 pdrlrirvnk islqdyegfh ydkeklreas iplgilvvrg dcdletcrmy idrlqedlqs
      481 vssgsqrvhy qdhetsfpra lsaqrlsprw cfldatsadr fyridrsqeh lhfvmeisqd
      541 eifildpdmv vsqpagtppg mpdlvveqas gisdwwnpal rkrmlsdsgl gmiapyyeds
      601 dlkdlshsrv lqspvssedh ailqaviagd lmkliesykn ggslliqgpd hcsllhyaak
      661 tgngeivkyi ldhgpselld madsetgeta lhkaacqrnr avcqllvdag aslrktdskg
      721 ktpqeraqqa gdpdlaayle srqnykvigh edletav
//
LOCUS       NP_001157863             491 aa            linear   PRI 21-NOV-2025
DEFINITION  metal-response element-binding transcription factor 2 isoform c
            [Homo sapiens].
ACCESSION   NP_001157863
VERSION     NP_001157863.1
DBSOURCE    REFSEQ: accession NM_001164391.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Hu,X., Liu,Y., Shen,H., Zhang,T. and Liang,T.
  TITLE     MTF2 facilitates the advancement of osteosarcoma through mediating
            EZH2/SFRP1/Wnt signaling
  JOURNAL   J Orthop Surg Res 19 (1), 467 (2024)
   PUBMED   39118123
  REMARK    GeneRIF: MTF2 facilitates the advancement of osteosarcoma through
            mediating EZH2/SFRP1/Wnt signaling.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Ngubo,M., Moradi,F., Ito,C.Y. and Stanford,W.L.
  TITLE     Tissue-Specific Tumour Suppressor and Oncogenic Activities of the
            Polycomb-like Protein MTF2
  JOURNAL   Genes (Basel) 14 (10), 1879 (2023)
   PUBMED   37895228
  REMARK    GeneRIF: Tissue-Specific Tumour Suppressor and Oncogenic Activities
            of the Polycomb-like Protein MTF2.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Tang,C., Lv,Y., Ding,K., Cao,Y., Ma,Z., Yang,L., Zhang,Q., Zhou,H.,
            Wang,Y., Liu,Z. and Cao,X.
  TITLE     Comprehensive Pan-Cancer Analysis of MTF2 Effects on Human Tumors
  JOURNAL   Curr Probl Cancer 47 (3), 100957 (2023)
   PUBMED   37027952
  REMARK    GeneRIF: Comprehensive Pan-Cancer Analysis of MTF2 Effects on Human
            Tumors.
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Musselman,C.A., Avvakumov,N., Watanabe,R., Abraham,C.G.,
            Lalonde,M.E., Hong,Z., Allen,C., Roy,S., Nunez,J.K., Nickoloff,J.,
            Kulesza,C.A., Yasui,A., Cote,J. and Kutateladze,T.G.
  TITLE     Molecular basis for H3K36me3 recognition by the Tudor domain of
            PHF1
  JOURNAL   Nat Struct Mol Biol 19 (12), 1266-1272 (2012)
   PUBMED   23142980
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Wang,S., Robertson,G.P. and Zhu,J.
  TITLE     A novel human homologue of Drosophila polycomblike gene is
            up-regulated in multiple cancers
  JOURNAL   Gene 343 (1), 69-78 (2004)
   PUBMED   15563832
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Mididoddi,S., McGuirt,J.P., Sens,M.A., Todd,J.H. and Sens,D.A.
  TITLE     Isoform-specific expression of metallothionein mRNA in the
            developing and adult human kidney
  JOURNAL   Toxicol Lett 85 (1), 17-27 (1996)
   PUBMED   8619255
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Inouye,C., Remondelli,P., Karin,M. and Elledge,S.
  TITLE     Isolation of a cDNA encoding a metal response element binding
            protein using a novel expression cloning procedure: the one hybrid
            system
  JOURNAL   DNA Cell Biol 13 (7), 731-742 (1994)
   PUBMED   7772254
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB173315.1, AK302776.1, AF072814.1, AL117354.12 and BQ025793.1.
            
            Transcript Variant: This variant (3) lacks an alternate portion of
            a coding exon compared to variant 1, that causes a frameshift. The
            resulting isoform (c) is shorter at the N-terminus compared to
            isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments. Variants 3
            and 4 both encode the same isoform (c).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302776.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.1"
     Protein         1..491
                     /product="metal-response element-binding transcription
                     factor 2 isoform c"
                     /note="putative DNA binding protein; polycomb-like 2;
                     hPCl2; polycomb-like protein 2; metal regulatory
                     transcription factor 2; metal-response element DNA-binding
                     protein M96; tudor domain containing 19A"
                     /calculated_mol_wt=55594
     Region          2..54
                     /region_name="PHD1_MTF2"
                     /note="PHD finger 1 found in metal-response
                     element-binding transcription factor 2 (MTF2); cd15578"
                     /db_xref="CDD:277053"
     Site            order(2,16..20,24,47)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277053"
     Region          101..152
                     /region_name="PHD2_MTF2"
                     /note="PHD finger 2 found in metal-response
                     element-binding transcription factor 2 (MTF2); cd15580"
                     /db_xref="CDD:277055"
     Site            order(101,113..117,121,145)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277055"
     Region          442..489
                     /region_name="Mtf2_C"
                     /note="Polycomb-like MTF2 factor 2; pfam14061"
                     /db_xref="CDD:464077"
     CDS             1..491
                     /gene="MTF2"
                     /gene_synonym="dJ976O13.2; M96; PCL2; TDRD19A"
                     /coded_by="NM_001164391.2:471..1946"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS53341.1"
                     /db_xref="GeneID:22823"
                     /db_xref="HGNC:HGNC:29535"
                     /db_xref="MIM:609882"
ORIGIN      
        1 mvcticqeey seapnemvic dkcgqgyhql chtphidssv idsdekwlcr qcvfatttkr
       61 ggalkkgpna kalqvmkqtl pysvadlewd aghktnvqqc ycycggpgdw ylkmlqcckc
      121 kqwfheacvq clqkpmlfgd rfytficsvc ssgpeylkrl plqwvdiahl clynlsvihk
      181 kkyfdselel mtyinenwdr lhpgeladtp kseryehvle alndyktmfm sgkeikkkkh
      241 lfglrirvpp vppnvafkae kepegtshef kikgrkaskp isdsrevsng iekkgkkksv
      301 grppgpytrk miqktaepll dkesisenpt ldlpcsigrt egtahssnts dvdftgassa
      361 kettsssisr hyglsdsrkr trtgrswpaa iphlrrrrgr lprralqtqn seivkddegk
      421 edyqfdelnt eilnnladqe lqlnhlknsi tsyfgaagri acgekyrvla rrvtldgkvq
      481 ylvewegata s
//
LOCUS       NP_001153633            1962 aa            linear   PRI 21-NOV-2025
DEFINITION  sodium channel protein type 5 subunit alpha isoform f [Homo
            sapiens].
ACCESSION   NP_001153633
VERSION     NP_001153633.1
DBSOURCE    REFSEQ: accession NM_001160161.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1962)
  AUTHORS   Hu,Y., Zhang,C., Wang,S., Xiong,H., Xie,W., Zeng,Z., Cai,H.,
            Wang,Q.K. and Lu,Z.
  TITLE     14-3-3epsilon/YWHAE regulates the transcriptional expression of
            cardiac sodium channel NaV1.5
  JOURNAL   Heart Rhythm 21 (11), 2320-2329 (2024)
   PUBMED   38750908
  REMARK    GeneRIF: 14-3-3epsilon/YWHAE regulates the transcriptional
            expression of cardiac sodium channel NaV1.5.
REFERENCE   2  (residues 1 to 1962)
  AUTHORS   Cadena-Ullauri,S., Guevara-Ramirez,P., Ruiz-Pozo,V.A.,
            Tamayo-Trujillo,R., Paz-Cruz,E., Simancas-Racines,D.,
            Ibarra-Castillo,R., Laso-Bayas,J.L. and Zambrano,A.K.
  TITLE     Genomic analysis of an Ecuadorian individual carrying an SCN5A rare
            variant
  JOURNAL   BMC Cardiovasc Disord 24 (1), 388 (2024)
   PUBMED   39068398
  REMARK    GeneRIF: Genomic analysis of an Ecuadorian individual carrying an
            SCN5A rare variant.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1962)
  AUTHORS   Tariq,U., Sarkar,S., Malladi,N., Kumar,R., Bugga,P., Chakraborty,P.
            and Banerjee,S.K.
  TITLE     Knockdown of SCN5A alters metabolic-associated genes and aggravates
            hypertrophy in the cardiomyoblast
  JOURNAL   Mol Biol Rep 51 (1), 661 (2024)
   PUBMED   38758505
  REMARK    GeneRIF: Knockdown of SCN5A alters metabolic-associated genes and
            aggravates hypertrophy in the cardiomyoblast.
            Erratum:[Mol Biol Rep. 2024 Jul 26;51(1):852. doi:
            10.1007/s11033-024-09742-9. PMID: 39060789]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1962)
  AUTHORS   Wright,K.M., Nathan,S., Jiang,H., Xia,W., Kim,H., Chakouri,N.,
            Nwafor,J.N., Fossier,L., Srinivasan,L., Chen,Z., Boronina,T.,
            Post,J., Paul,S., Cole,R.N., Ben-Johny,M., Cole,P.A. and
            Gabelli,S.B.
  TITLE     NEDD4L intramolecular interactions regulate its auto and substrate
            NaV1.5 ubiquitination
  JOURNAL   J Biol Chem 300 (3), 105715 (2024)
   PUBMED   38309503
  REMARK    GeneRIF: NEDD4L intramolecular interactions regulate its auto and
            substrate NaV1.5 ubiquitination.
REFERENCE   5  (residues 1 to 1962)
  AUTHORS   George,A.L. Jr., Varkony,T.A., Drabkin,H.A., Han,J., Knops,J.F.,
            Finley,W.H., Brown,G.B., Ward,D.C. and Haas,M.
  TITLE     Assignment of the human heart tetrodotoxin-resistant voltage-gated
            Na+ channel alpha-subunit gene (SCN5A) to band 3p21
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 67-70 (1995)
   PUBMED   7956363
REFERENCE   6  (residues 1 to 1962)
  AUTHORS   Jiang,C., Atkinson,D., Towbin,J.A., Splawski,I., Lehmann,M.H.,
            Li,H., Timothy,K., Taggart,R.T., Schwartz,P.J., Vincent,G.M. et al.
  TITLE     Two long QT syndrome loci map to chromosomes 3 and 7 with evidence
            for further heterogeneity
  JOURNAL   Nat Genet 8 (2), 141-147 (1994)
   PUBMED   7842012
REFERENCE   7  (residues 1 to 1962)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   8  (residues 1 to 1962)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 1962)
  AUTHORS   Groffen,A.J., Bikker,H. and Christiaans,I.
  TITLE     Long QT Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301308
REFERENCE   10 (residues 1 to 1962)
  AUTHORS   Gellens,M.E., George,A.L. Jr., Chen,L.Q., Chahine,M., Horn,R.,
            Barchi,R.L. and Kallen,R.G.
  TITLE     Primary structure and functional expression of the human cardiac
            tetrodotoxin-insensitive voltage-dependent sodium channel
  JOURNAL   Proc Natl Acad Sci U S A 89 (2), 554-558 (1992)
   PUBMED   1309946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP006241.1, BC051374.1,
            AB158470.2, BC140813.1, AF482988.1 and AY038064.1.
            
            Summary: The protein encoded by this gene is an integral membrane
            protein and tetrodotoxin-resistant voltage-gated sodium channel
            subunit. This protein is found primarily in cardiac muscle and is
            responsible for the initial upstroke of the action potential in an
            electrocardiogram. Defects in this gene have been associated with
            long QT syndrome type 3 (LQT3), atrial fibrillation,
            cardiomyopathy, and Brugada syndrome 1, all autosomal dominant
            cardiac diseases. Alternative splicing results in several
            transcript variants encoding different isoforms. [provided by
            RefSeq, May 2022].
            
            Transcript Variant: This variant (6) uses an alternate, duplicated
            exon in the 5' coding region and lacks an alternate in-frame exon
            in the central coding region, compared to variant 1. The resulting
            isoform (f) differs at a few internal aa near the N-terminus and
            lacks a 54-aa segment, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AB158470.2 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1968189,
                                    SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1962
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.2"
     Protein         1..1962
                     /product="sodium channel protein type 5 subunit alpha
                     isoform f"
                     /note="cardiac tetrodotoxin-insensitive voltage-dependent
                     sodium channel alpha subunit; sodium channel protein type
                     5 subunit alpha; voltage-gated sodium channel subunit
                     alpha Nav1.5; sodium channel protein cardiac muscle
                     subunit alpha; sodium channel, voltage-gated, type V,
                     alpha subunit"
                     /calculated_mol_wt=221173
     Region          130..423
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          507..667
                     /region_name="Na_trans_cytopl"
                     /note="Cytoplasmic domain of voltage-gated Na+ ion
                     channel; pfam11933"
                     /db_xref="CDD:463401"
     Region          716..927
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          953..1146
                     /region_name="Na_trans_assoc"
                     /note="Sodium ion transport-associated; pfam06512"
                     /db_xref="CDD:461936"
     Region          1150..1425
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          1417..1469
                     /region_name="Na_channel_gate"
                     /note="Inactivation gate of the voltage-gated sodium
                     channel alpha subunits; cd13433"
                     /db_xref="CDD:240441"
     Site            1431..1434
                     /site_type="other"
                     /note="putative hydrophobic latch"
                     /db_xref="CDD:240441"
     Region          1474..1728
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     CDS             1..1962
                     /gene="SCN5A"
                     /gene_synonym="CDCD2; CMD1E; CMPD2; HB1; HB2; HBBD; HH1;
                     ICCD; IVF; LQT3; Nav1.5; PFHB1; SSS1; VF1"
                     /coded_by="NM_001160161.2:210..6098"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS54569.1"
                     /db_xref="GeneID:6331"
                     /db_xref="HGNC:HGNC:10593"
                     /db_xref="MIM:600163"
ORIGIN      
        1 manfllprgt ssfrrftres laaiekrmae kqargsttlq esreglpeee aprpqldlqa
       61 skklpdlygn ppqeligepl edldpfystq ktfivlnkgk tifrfsatna lyvlspfhpi
      121 rraavkilvh slfnmlimct iltncvfmaq hdpppwtkyv eytftaiytf eslvkilarg
      181 fclhaftflr dpwnwldfsv iimayvseni klgnlsalrt frvlralkti svipglktiv
      241 galiqsvkkl advmvltvfc lsvfaliglq lfmgnlrhkc vrnftalngt ngsveadglv
      301 wesldlylsd penyllkngt sdvllcgnss dagtcpegyr clkagenpdh gytsfdsfaw
      361 aflalfrlmt qdcwerlyqq tlrsagkiym iffmlviflg sfylvnlila vvamayeeqn
      421 qatiaeteek ekrfqeamem lkkehealti rgvdtvsrss lemsplapvn sherrskrrk
      481 rmssgteecg edrlpksdse dgpramnhls ltrglsrtsm kprssrgsif tfrrrdlgse
      541 adfaddenst ageseshhts llvpwplrrt saqgqpspgt sapghalhgk knstvdcngv
      601 vsllgagdpe atspgshllr pvmlehppdt ttpseepggp qmltsqapcv dgfeepgarq
      661 ralsavsvlt saleeleesr hkcppcwnrl aqryliwecc plwmsikqgv klvvmdpftd
      721 ltitmcivln tlfmalehyn mtsefeemlq vgnlvftgif taemtfkiia ldpyyyfqqg
      781 wnifdsiivi lslmelglsr msnlsvlrsf rllrvfklak swptlntlik iignsvgalg
      841 nltlvlaiiv fifavvgmql fgknyselrd sdsgllprwh mmdffhafli ifrilcgewi
      901 etmwdcmevs gqslcllvfl lvmvignlvv lnlflallls sfsadnltap dedremnnlq
      961 lalariqrgl rfvkrttwdf ccgllrqrpq kpaalaaqgq lpsciatpys ppppetekvp
     1021 ptrketrfee geqpgqgtpg dpepvcvpia vaesdtddqe edeenslgte eesskqtped
     1081 scsegstadm tntaelleqi pdlgqdvkdp edcftegcvr rcpccavdtt qapgkvwwrl
     1141 rktcyhiveh swfetfiifm illssgalaf ediyleerkt ikvlleyadk mftyvfvlem
     1201 llkwvaygfk kyftnawcwl dflivdvslv slvantlgfa emgpikslrt lralrplral
     1261 srfegmrvvv nalvgaipsi mnvllvclif wlifsimgvn lfagkfgrci nqtegdlpln
     1321 ytivnnksqc eslnltgely wtkvkvnfdn vgagylallq vatfkgwmdi myaavdsrgy
     1381 eeqpqweynl ymyiyfvifi ifgsfftlnl figviidnfn qqkkklggqd ifmteeqkky
     1441 ynamkklgsk kpqkpiprpl nkyqgfifdi vtkqafdvti mfliclnmvt mmvetddqsp
     1501 ekinilakin llfvaiftge civklaalrh yyftnswnif dfvvvilsiv gtvlsdiiqk
     1561 yffsptlfrv irlarigril rlirgakgir tllfalmmsl palfniglll flvmfiysif
     1621 gmanfayvkw eagiddmfnf qtfansmlcl fqittsagwd gllspilntg ppycdptlpn
     1681 sngsrgdcgs pavgilfftt yiiisflivv nmyiaiilen fsvateeste plseddfdmf
     1741 yeiwekfdpe atqfieysvl sdfadalsep lriakpnqis linmdlpmvs gdrihcmdil
     1801 faftkrvlge sgemdalkiq meekfmaanp skisyepitt tlrrkheevs amviqrafrr
     1861 hllqrslkha sflfrqqags glseedaper egliayvmse nfsrplgpps sssisstsfp
     1921 psydsvtrat sdnlqvrgsd yshsedladf ppspdrdres iv
//
LOCUS       NP_001271245             311 aa            linear   PRI 21-NOV-2025
DEFINITION  malonate--CoA ligase ACSF3, mitochondrial isoform 2 [Homo sapiens].
ACCESSION   NP_001271245
VERSION     NP_001271245.1
DBSOURCE    REFSEQ: accession NM_001284316.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Liu,Y., Chen,S.H., Jin,X. and Li,Y.M.
  TITLE     Analysis of differentially expressed genes and microRNAs in
            alcoholic liver disease
  JOURNAL   Int J Mol Med 31 (3), 547-554 (2013)
   PUBMED   23337955
  REMARK    GeneRIF: ACSF3 was significantly upregulated, and was involved in
            fatty acid and lipid metabolism and accelerated liver injury in
            alcoholic liver disease.
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Salaverria,I., Akasaka,T., Gesk,S., Szczepanowski,M., Burkhardt,B.,
            Harder,L., Damm-Welk,C., Oschlies,I., Klapper,W., Dyer,M.J. and
            Siebert,R.
  TITLE     The CBFA2T3/ACSF3 locus is recurrently involved in IGH chromosomal
            translocation t(14;16)(q32;q24) in pediatric B-cell lymphoma with
            germinal center phenotype
  JOURNAL   Genes Chromosomes Cancer 51 (4), 338-343 (2012)
   PUBMED   22420028
  REMARK    GeneRIF: data indicate that the CBFA2T3/ACSF3 locus is a novel
            recurrent oncogenic target of immunoglobulin heavy chain
            translocations, which might contribute to the pathogenesis of
            pediatric GC-derived B-cell lymphoma.
REFERENCE   6  (residues 1 to 311)
  AUTHORS   Witkowski,A., Thweatt,J. and Smith,S.
  TITLE     Mammalian ACSF3 protein is a malonyl-CoA synthetase that supplies
            the chain extender units for mitochondrial fatty acid synthesis
  JOURNAL   J Biol Chem 286 (39), 33729-33736 (2011)
   PUBMED   21846720
  REMARK    GeneRIF: Mammalian ACSF3 protein is a malonyl-CoA synthetase that
            supplies the chain extender units for mitochondrial fatty acid
            synthesis.
REFERENCE   7  (residues 1 to 311)
  AUTHORS   Alfares,A., Nunez,L.D., Al-Thihli,K., Mitchell,J., Melancon,S.,
            Anastasio,N., Ha,K.C., Majewski,J., Rosenblatt,D.S. and
            Braverman,N.
  TITLE     Combined malonic and methylmalonic aciduria: exome sequencing
            reveals mutations in the ACSF3 gene in patients with a non-classic
            phenotype
  JOURNAL   J Med Genet 48 (9), 602-605 (2011)
   PUBMED   21785126
  REMARK    GeneRIF: ACSF3 is a candidate gene for non-classical CMAMMA
            observed in our patients.
REFERENCE   8  (residues 1 to 311)
  AUTHORS   Sloan,J.L., Johnston,J.J., Manoli,I., Chandler,R.J., Krause,C.,
            Carrillo-Carrasco,N., Chandrasekaran,S.D., Sysol,J.R., O'Brien,K.,
            Hauser,N.S., Sapp,J.C., Dorward,H.M., Huizing,M., Barshop,B.A.,
            Berry,S.A., James,P.M., Champaigne,N.L., de Lonlay,P.,
            Valayannopoulos,V., Geschwind,M.D., Gavrilov,D.K., Nyhan,W.L.,
            Biesecker,L.G. and Venditti,C.P.
  CONSRTM   NIH Intramural Sequencing Center Group
  TITLE     Exome sequencing identifies ACSF3 as a cause of combined malonic
            and methylmalonic aciduria
  JOURNAL   Nat Genet 43 (9), 883-886 (2011)
   PUBMED   21841779
  REMARK    GeneRIF: mutations in ACSF3, encoding a putative methylmalonyl-CoA
            and malonyl-CoA synthetase, were identified as a cause of combined
            malonic and methylmalonic aciduria.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 311)
  AUTHORS   Chen,H., Kim,H.U., Weng,H. and Browse,J.
  TITLE     Malonyl-CoA synthetase, encoded by ACYL ACTIVATING ENZYME13, is
            essential for growth and development of Arabidopsis
  JOURNAL   Plant Cell 23 (6), 2247-2262 (2011)
   PUBMED   21642549
REFERENCE   10 (residues 1 to 311)
  AUTHORS   Watkins,P.A., Maiguel,D., Jia,Z. and Pevsner,J.
  TITLE     Evidence for 26 distinct acyl-coenzyme A synthetase genes in the
            human genome
  JOURNAL   J Lipid Res 48 (12), 2736-2750 (2007)
   PUBMED   17762044
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM148793.1, BX402632.2,
            BQ953430.1, BX325026.2, AC009113.8 and BI837487.1.
            
            Summary: This gene encodes a member of the acyl-CoA synthetase
            family of enzymes that activate fatty acids by catalyzing the
            formation of a thioester linkage between fatty acids and coenzyme
            A. The encoded protein is localized to mitochondria, has high
            specificity for malonate and methylmalonate and possesses
            malonyl-CoA synthetase activity. Mutations in this gene are a cause
            of combined malonic and methylmalonic aciduria. Alternatively
            spliced transcript variants have been observed for this gene.
            [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (3) lacks two exons, one of which
            contains a portion of the 5' UTR and the other which contains a
            portion of the 5' coding region including the start codon, compared
            to variant 1. These differences cause translation initiation at a
            downstream start codon and result in an isoform (2) with a shorter
            N-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064609.1, SRR14038196.1570683.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..311
                     /product="malonate--CoA ligase ACSF3, mitochondrial
                     isoform 2"
                     /EC_number="6.2.1.76"
                     /note="acyl-CoA synthetase family member 3, mitochondrial;
                     malonyl-CoA synthetase; malonate--CoA ligase ACSF3,
                     mitochondrial"
                     /calculated_mol_wt=35011
     Region          <1..306
                     /region_name="Adenylate forming domain, Class I
                     superfamily"
                     /note="This family includes acyl- and aryl-CoA ligases, as
                     well as the adenylation domain of nonribosomal peptide
                     synthetases and firefly luciferases. The adenylate-forming
                     enzymes catalyze an ATP-dependent two-step reaction to
                     first activate a carboxylate...; cl17068"
                     /db_xref="CDD:473059"
     Site            order(28,30..31,34,66..67,88..93,192,203,206,215..218,279)
                     /site_type="active"
                     /db_xref="CDD:341228"
     Site            order(30..31,34,66,215..217,273,279)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Site            order(66..67,88..93,192,203,206,218,298)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341228"
     CDS             1..311
                     /gene="ACSF3"
                     /coded_by="NM_001284316.2:271..1206"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS73926.1"
                     /db_xref="GeneID:197322"
                     /db_xref="HGNC:HGNC:27288"
                     /db_xref="MIM:614245"
ORIGIN      
        1 mmpefspqqv wekflssetp rinvfmavpt iytklmeyyd rhftqphaqd flravceeki
       61 rlmvsgsaal plpvlekwkn itghtllery gmteigmals gplttavrlp gsvgtplpgv
      121 qvrivsenpq reacsytiha egdergtkvt pgfeekegel lvrgpsvfre ywnkpeetks
      181 aftldgwfkt gdtvvfkdgq ywirgrtsvd iiktggykvs alevewhlla hpsitdvavi
      241 gvpdmtwgqr vtavvtlreg hslshrelke warnvlapya vpselvlvee iprnqmgkid
      301 kkalirhfhp s
//
LOCUS       NP_001356996            1066 aa            linear   PRI 21-NOV-2025
DEFINITION  ubiquitin-associated protein 2 isoform 7 [Homo sapiens].
ACCESSION   NP_001356996
VERSION     NP_001356996.2
DBSOURCE    REFSEQ: accession NM_001370067.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Lv,Z., Shi,Y., Wu,H., Cao,K., Liu,X. and Wang,C.
  TITLE     Novel Circular RNA CircUBAP2 Drives Tumor Progression by Regulating
            the miR-143/TFAP2B Axis in Prostate Cancer
  JOURNAL   Protein Pept Lett 31 (1), 61-73 (2024)
   PUBMED   37962045
  REMARK    GeneRIF: Novel Circular RNA CircUBAP2 Drives Tumor Progression by
            Regulating the miR-143/TFAP2B Axis in Prostate Cancer.
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Chou,M.C., Wang,Y.H., Chen,F.Y., Kung,C.Y., Wu,K.P., Kuo,J.C.,
            Chan,S.J., Cheng,M.L., Lin,C.Y., Chou,Y.C., Ho,M.C., Firestine,S.,
            Huang,J.R. and Chen,R.H.
  TITLE     PAICS ubiquitination recruits UBAP2 to trigger phase separation for
            purinosome assembly
  JOURNAL   Mol Cell 83 (22), 4123-4140 (2023)
   PUBMED   37848033
  REMARK    GeneRIF: PAICS ubiquitination recruits UBAP2 to trigger phase
            separation for purinosome assembly.
REFERENCE   4  (residues 1 to 1066)
  AUTHORS   Herlihy,A.E., Boeing,S., Weems,J.C., Walker,J.,
            Dirac-Svejstrup,A.B., Lehner,M.H., Conaway,R.C., Conaway,J.W. and
            Svejstrup,J.Q.
  TITLE     UBAP2/UBAP2L regulate UV-induced ubiquitylation of RNA polymerase
            II and are the human orthologues of yeast Def1
  JOURNAL   DNA Repair (Amst) 115, 103343 (2022)
   PUBMED   35633597
  REMARK    GeneRIF: UBAP2/UBAP2L regulate UV-induced ubiquitylation of RNA
            polymerase II and are the human orthologues of yeast Def1.
REFERENCE   5  (residues 1 to 1066)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 1066)
  AUTHORS   Zuo,L., Saba,L., Wang,K., Zhang,X., Krystal,J.H., Tabakoff,B. and
            Luo,X.
  TITLE     Exome-wide association study of replicable nonsynonymous variants
            conferring risk for alcohol dependence
  JOURNAL   J Stud Alcohol Drugs 74 (4), 622-625 (2013)
   PUBMED   23739027
  REMARK    GeneRIF: By incorporating the information from bioinformatics and
            RNA expression analyses, we identified at least two of the most
            promising risk genes for alcohol dependence: APOER2 and UBAP2
REFERENCE   7  (residues 1 to 1066)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 1066)
  AUTHORS   Venturelli,E., Villa,C., Fenoglio,C., Clerici,F., Marcone,A.,
            Benussi,L., Ghidoni,R., Gallone,S., Scalabrini,D., Cortini,F.,
            Fumagalli,G., Cappa,S., Binetti,G., Franceschi,M., Rainero,I.,
            Giordana,M.T., Mariani,C., Bresolin,N., Scarpini,E. and
            Galimberti,D.
  TITLE     Is KIF24 a genetic risk factor for Frontotemporal Lobar
            Degeneration?
  JOURNAL   Neurosci Lett 482 (3), 240-244 (2010)
   PUBMED   20670673
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1066)
  AUTHORS   Dieci,G., Preti,M. and Montanini,B.
  TITLE     Eukaryotic snoRNAs: a paradigm for gene expression flexibility
  JOURNAL   Genomics 94 (2), 83-88 (2009)
   PUBMED   19446021
  REMARK    GeneRIF: UBAP2 serves as a host gene for snoRNAs
            Review article
REFERENCE   10 (residues 1 to 1066)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The UBA domain: a sequence motif present in multiple enzyme classes
            of the ubiquitination pathway
  JOURNAL   Trends Biochem Sci 21 (5), 172-173 (1996)
   PUBMED   8871400
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354989.13 and AL139113.21.
            
            On Aug 14, 2020 this sequence version replaced NP_001356996.1.
            
            Summary: The protein encoded by this gene contains a UBA (ubiquitin
            associated) domain, which is characteristic of proteins that
            function in the ubiquitination pathway. This gene may show
            increased expression in the adrenal gland and lymphatic tissues.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853564.27073.1,
                                           SRR14038194.1844785.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..1066
                     /product="ubiquitin-associated protein 2 isoform 7"
                     /note="AD-012 protein; RNA polymerase II degradation
                     factor UBAP2"
                     /calculated_mol_wt=111558
     Region          53..90
                     /region_name="UBA_UBP2_like"
                     /note="UBA domain found in ubiquitin-associated protein 2
                     (UBAP-2) like proteins; cd14277"
                     /db_xref="CDD:270463"
     Region          459..488
                     /region_name="DUF3697"
                     /note="Ubiquitin-associated protein 2; pfam12478"
                     /db_xref="CDD:372135"
     CDS             1..1066
                     /gene="UBAP2"
                     /gene_synonym="UBAP-2"
                     /coded_by="NM_001370067.2:105..3305"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS6548.1"
                     /db_xref="GeneID:55833"
                     /db_xref="HGNC:HGNC:14185"
ORIGIN      
        1 mmtsvssdhc rgarekpqis aaqstqpqkq vvqataeqmr laqvifdknd sdfeakvkql
       61 mevtgknqde civalhdcng dvnkainill egnsdttswe tvgckkknfa kensenkenr
      121 ekksekessr grgnnnrkgr ggnrgrefrg eengidcnqv dkpsdrgkra rgrelasnth
      181 niaqdlsnks syglkgawkn sveewttedw tedlsetkvf tassapaenh ilpgqsidlv
      241 allqkpvphs qaseansfet sqqqgfgqal vftnsqhnnq mapgtgssta vnscspqsls
      301 svlgsgfgel appkmanits sqildqlkap slgqftttps tqqnstshpt tttswdlkpp
      361 tsqssvlshl dfksqpepsp vlsqlsqrqq hqsqavtvpp pglesfpsqa klrestpgds
      421 pstvnkllql psttienisv svhqpqpkhi klakrrippa skipasavem pgsadvtgln
      481 vqfgalefgs epslsefgsa pssensnqip islyskslse plntslsmts avqnstytts
      541 vitscsltss slnsaspvam sssydqssvh nripyqspvs ssesapgtim nghgggrsqq
      601 tldtpkttgp psalpsvssl psttsctall pstsqhtgdl tssplsqlss slsshqssls
      661 ahaalsssts hthasvesas shqssatfst aatsvsssas sgaslsssmn tanslclggt
      721 pasasssssr aaplvtsgka ppnlpqgvpp llhnqylvgp ggllpaypiy gydelqmlqs
      781 rlpvdyygip faaptalasr dgslannpyp gdvtkfgrgd saspapattp aqpqqsqsqt
      841 hhtaqqpfvn palppgysyt glpyytgmps afqygptmfv ppasakqhgv nlstptppfq
      901 qasgygqhgy stgyddltqg taagdyskgg yagssqapnk sagsgpgkgv svsssttglp
      961 dmtgsvynkt qtfdkqgfha gtpppfslps vlgstgplas gaapgyappp flhilpahqq
     1021 phsqllhhhl pqdaqsgsgq rsqpsslqpk sqaskpaygn spywtn
//
LOCUS       NP_001112357             452 aa            linear   PRI 21-NOV-2025
DEFINITION  glycine receptor subunit alpha-2 isoform A precursor [Homo
            sapiens].
ACCESSION   NP_001112357
VERSION     NP_001112357.1
DBSOURCE    REFSEQ: accession NM_001118885.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Tian,Q., Tong,P., Chen,G., Deng,M., Cai,T., Tian,R., Zhang,Z.,
            Xia,K. and Hu,Z.
  TITLE     GLRA2 gene mutations cause high myopia in humans and mice
  JOURNAL   J Med Genet 60 (2), 193-203 (2023)
   PUBMED   35396272
  REMARK    GeneRIF: GLRA2 gene mutations cause high myopia in humans and mice.
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Aboheimed,G.I., AlRasheed,M.M., Almudimeegh,S., Pena-Guerra,K.A.,
            Cardona-Londono,K.J., Salih,M.A., Seidahmed,M.Z., Al-Mohanna,F.,
            Colak,D., Harvey,R.J., Harvey,K., Arold,S.T., Kaya,N. and Ruiz,A.J.
  TITLE     Clinical, genetic, and functional characterization of the glycine
            receptor beta-subunit A455P variant in a family affected by
            hyperekplexia syndrome
  JOURNAL   J Biol Chem 298 (7), 102018 (2022)
   PUBMED   35526563
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Raltschev,C., Hetsch,F., Winkelmann,A., Meier,J.C. and Semtner,M.
  TITLE     Electrophysiological Signature of Homomeric and Heteromeric Glycine
            Receptor Channels
  JOURNAL   J Biol Chem 291 (34), 18030-18040 (2016)
   PUBMED   27382060
  REMARK    GeneRIF: data show that the current-voltage relationships of
            homomeric channels formed by the alpha2 or alpha3 subunits change
            upon receptor desensitization from a linear to an inwardly
            rectifying shape, in contrast to their heteromeric counterparts.
REFERENCE   4  (residues 1 to 452)
  AUTHORS   McCracken,L.M., Trudell,J.R., McCracken,M.L. and Harris,R.A.
  TITLE     Zinc-dependent modulation of alpha2- and alpha3-glycine receptor
            subunits by ethanol
  JOURNAL   Alcohol Clin Exp Res 37 (12), 2002-2010 (2013)
   PUBMED   23895467
REFERENCE   5  (residues 1 to 452)
  AUTHORS   Wegner,F., Kraft,R., Busse,K., Hartig,W., Ahrens,J., Leffler,A.,
            Dengler,R. and Schwarz,J.
  TITLE     Differentiated human midbrain-derived neural progenitor cells
            express excitatory strychnine-sensitive glycine receptors
            containing alpha2beta subunits
  JOURNAL   PLoS One 7 (5), e36946 (2012)
   PUBMED   22606311
  REMARK    GeneRIF: investigated neural progenitor cells in respect to their
            glycine receptor function and subunit expression using
            electrophysiology, calcium imaging, immunocytochemistry, and
            quantitative real-time PCR
REFERENCE   6  (residues 1 to 452)
  AUTHORS   Davies,D.L., Crawford,D.K., Trudell,J.R., Mihic,S.J. and
            Alkana,R.L.
  TITLE     Multiple sites of ethanol action in alpha1 and alpha2 glycine
            receptors suggested by sensitivity to pressure antagonism
  JOURNAL   J Neurochem 89 (5), 1175-1185 (2004)
   PUBMED   15147510
  REMARK    GeneRIF: Effects of 12 times normal atmospheric pressure of
            helium-oxygen gas (pressure) on ethanol-induced potentiation of
            GlyR function in Xenopus oocytes expressing human alpha1, alpha2 or
            the mutant alpha1(A52S) GlyRs were measured by voltage clamp
            technics
REFERENCE   7  (residues 1 to 452)
  AUTHORS   Feng,J., Craddock,N., Jones,I.R., Cook,E.H. Jr., Goldman,D.,
            Heston,L.L., Peltonen,L., DeLisi,L.E. and Sommer,S.S.
  TITLE     Systematic screening for mutations in the glycine receptor alpha2
            subunit gene (GLRA2) in patients with schizophrenia and other
            psychiatric diseases
  JOURNAL   Psychiatr Genet 11 (1), 45-48 (2001)
   PUBMED   11409700
REFERENCE   8  (residues 1 to 452)
  AUTHORS   Cummings,C.J., Dahle,E.J. and Zoghbi,H.Y.
  TITLE     Analysis of the genomic structure of the human glycine receptor
            alpha2 subunit gene and exclusion of this gene as a candidate for
            Rett syndrome
  JOURNAL   Am J Med Genet 78 (2), 176-178 (1998)
   PUBMED   9674912
REFERENCE   9  (residues 1 to 452)
  AUTHORS   Monani,U. and Burghes,A.H.
  TITLE     Structure of the human alpha 2 subunit gene of the glycine
            receptor--use of vectorette and Alu-exon PCR
  JOURNAL   Genome Res 6 (12), 1200-1206 (1996)
   PUBMED   8973915
REFERENCE   10 (residues 1 to 452)
  AUTHORS   Grenningloh,G., Schmieden,V., Schofield,P.R., Seeburg,P.H.,
            Siddique,T., Mohandas,T.K., Becker,C.M. and Betz,H.
  TITLE     Alpha subunit variants of the human glycine receptor: primary
            structures, functional expression and chromosomal localization of
            the corresponding genes
  JOURNAL   EMBO J 9 (3), 771-776 (1990)
   PUBMED   2155780
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK312591.1, BC045547.1 and
            AA081959.1.
            
            Summary: The glycine receptor consists of two subunits, alpha and
            beta, and acts as a pentamer. The protein encoded by this gene is
            an alpha subunit and can bind strychnine. Several transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, Jan 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1 and 2 encode the same isoform
            (A).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK312591.1, SRR1803612.31499.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..452
                     /product="glycine receptor subunit alpha-2 isoform A
                     precursor"
                     /note="glycine receptor subunit alpha-2; glycine receptor,
                     alpha-2 polypeptide; glycine receptor alpha 2 subunit"
                     /calculated_mol_wt=48802
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3219
     mat_peptide     28..452
                     /product="glycine receptor subunit alpha-2 isoform A"
                     /calculated_mol_wt=48802
     Region          46..441
                     /region_name="LIC"
                     /note="Cation transporter family protein; TIGR00860"
                     /db_xref="CDD:273305"
     Site            72
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23416.1)"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23416.1)"
     Site            257..278
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23416.1)"
     Site            284..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23416.1)"
     Site            295
                     /site_type="other"
                     /note="Important for obstruction of the ion pore in the
                     closed conformation.
                     /evidence=ECO:0000250|UniProtKB:P23415; propagated from
                     UniProtKB/Swiss-Prot (P23416.1)"
     Site            316..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23416.1)"
     Site            421..441
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23416.1)"
     CDS             1..452
                     /gene="GLRA2"
                     /gene_synonym="GLR; MRXSP"
                     /coded_by="NM_001118885.2:333..1691"
                     /note="isoform A precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS14160.1"
                     /db_xref="GeneID:2742"
                     /db_xref="HGNC:HGNC:4327"
                     /db_xref="MIM:305990"
ORIGIN      
        1 mnrqlvnilt alfaffletn hfrtafckdh dsrsgkqpsq tlspsdfldk lmgrtsgyda
       61 rirpnfkgpp vnvtcnifin sfgsvtettm dyrvniflrq qwndsrlays eypddsldld
      121 psmldsiwkp dlffanekga nfhdvttdnk llriskngkv lysirltltl scpmdlknfp
      181 mdvqtctmql esfgytmndl ifewlsdgpv qvaegltlpq filkeekelg yctkhyntgk
      241 ftcievkfhl erqmgyyliq myipsllivi lswvsfwinm daaparvalg ittvltmttq
      301 ssgsraslpk vsyvkaidiw mavcllfvfa alleyaavnf vsrqhkeflr lrrrqkrqnk
      361 eedvtresrf nfsgygmghc lqvkdgtavk atpanplpqp pkdgdaikkk fvdrakridt
      421 israafplaf lifnifywit ykiirhedvh kk
//
LOCUS       NP_001129965             543 aa            linear   PRI 21-NOV-2025
DEFINITION  sodium-dependent lysophosphatidylcholine symporter 1 isoform 1
            [Homo sapiens].
ACCESSION   NP_001129965
VERSION     NP_001129965.1
DBSOURCE    REFSEQ: accession NM_001136493.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Origuela,V., Ferrer-Aguilar,P., Gazquez,A., Perez-Cruz,M.,
            Gomez-Roig,M.D., Gomez-Llorente,C. and Larque,E.
  TITLE     Placental MFSD2A expression in fetal growth restriction and
            maternal and fetal DHA status
  JOURNAL   Placenta 150, 31-38 (2024)
   PUBMED   38583303
  REMARK    GeneRIF: Placental MFSD2A expression in fetal growth restriction
            and maternal and fetal DHA status.
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Yuan,W., Qiu,Z.M., Li,H., Huang,M., Yuan,J.J., Niu,S.L., Chen,Q.,
            Yang,Q.W. and Ouyang,Q.
  TITLE     Investigation of the Binding Interaction of Mfsd2a with NEDD4-2 via
            Molecular Dynamics Simulations
  JOURNAL   ACS Chem Neurosci 15 (2), 382-393 (2024)
   PUBMED   38155530
  REMARK    GeneRIF: Investigation of the Binding Interaction of Mfsd2a with
            NEDD4-2 via Molecular Dynamics Simulations.
REFERENCE   3  (residues 1 to 543)
  AUTHORS   He,M., Kuk,A.C.Y., Ding,M., Chin,C.F., Galam,D.L.A., Nah,J.M.,
            Tan,B.C., Yeo,H.L., Chua,G.L., Benke,P.I., Wenk,M.R., Ho,L.,
            Torta,F. and Silver,D.L.
  TITLE     Spns1 is a lysophospholipid transporter mediating lysosomal
            phospholipid salvage
  JOURNAL   Proc Natl Acad Sci U S A 119 (40), e2210353119 (2022)
   PUBMED   36161949
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Martinez-Molledo,M., Nji,E. and Reyes,N.
  TITLE     Structural insights into the lysophospholipid brain uptake
            mechanism and its inhibition by syncytin-2
  JOURNAL   Nat Struct Mol Biol 29 (6), 604-612 (2022)
   PUBMED   35710838
  REMARK    GeneRIF: Structural insights into the lysophospholipid brain uptake
            mechanism and its inhibition by syncytin-2.
REFERENCE   5  (residues 1 to 543)
  AUTHORS   Khuller,K., Yigit,G., Martinez Grijalva,C., Altmuller,J.,
            Thiele,H., Nurnberg,P., Elcioglu,N.H., Yeter,B., Hehr,U., Stein,A.,
            Della Marina,A., Koninger,A., Depienne,C., Kaiser,F.J., Wollnik,B.
            and Kuechler,A.
  TITLE     MFSD2A-associated primary microcephaly - Expanding the clinical and
            mutational spectrum of this ultra-rare disease
  JOURNAL   Eur J Med Genet 64 (10), 104310 (2021)
   PUBMED   34400370
  REMARK    GeneRIF: MFSD2A-associated primary microcephaly - Expanding the
            clinical and mutational spectrum of this ultra-rare disease.
REFERENCE   6  (residues 1 to 543)
  AUTHORS   Spinola,M., Falvella,F.S., Colombo,F., Sullivan,J.P., Shames,D.S.,
            Girard,L., Spessotto,P., Minna,J.D. and Dragani,T.A.
  TITLE     MFSD2A is a novel lung tumor suppressor gene modulating cell cycle
            and matrix attachment
  JOURNAL   Mol Cancer 9, 62 (2010)
   PUBMED   20236515
  REMARK    GeneRIF: MFSD2A is a novel lung cancer tumor suppressor gene that
            regulates cell cycle progression and matrix attachment.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 543)
  AUTHORS   Angers,M., Uldry,M., Kong,D., Gimble,J.M. and Jetten,A.M.
  TITLE     Mfsd2a encodes a novel major facilitator superfamily
            domain-containing protein highly induced in brown adipose tissue
            during fasting and adaptive thermogenesis
  JOURNAL   Biochem J 416 (3), 347-355 (2008)
   PUBMED   18694395
  REMARK    GeneRIF: Results identify Mfsd2a (major facilitator superfamily
            domain-containing protein 2a) and an additional closely related
            protein Mfsd2b, and suggest that Mfsd2a plays a role in adaptive
            thermogenesis.
REFERENCE   8  (residues 1 to 543)
  AUTHORS   Esnault,C., Priet,S., Ribet,D., Vernochet,C., Bruls,T.,
            Lavialle,C., Weissenbach,J. and Heidmann,T.
  TITLE     A placenta-specific receptor for the fusogenic, endogenous
            retrovirus-derived, human syncytin-2
  JOURNAL   Proc Natl Acad Sci U S A 105 (45), 17532-17537 (2008)
   PUBMED   18988732
  REMARK    GeneRIF: MFSD2 is a placenta-specific receptor for the fusogenic,
            endogenous retrovirus-derived, human syncytin-2, and plays a role
            in placenta morphogenesis.
REFERENCE   9  (residues 1 to 543)
  AUTHORS   Spinola,M., Falvella,F.S., Galvan,A., Pignatiello,C., Leoni,V.P.,
            Pastorino,U., Paroni,R., Chen,S., Skaug,V., Haugen,A. and
            Dragani,T.A.
  TITLE     Ethnic differences in frequencies of gene polymorphisms in the
            MYCL1 region and modulation of lung cancer patients' survival
  JOURNAL   Lung Cancer 55 (3), 271-277 (2007)
   PUBMED   17145094
  REMARK    GeneRIF: three additional SNPs in the MFSD2 genes showed ethnic
            differences in allelic frequencies
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 543)
  AUTHORS   Yamada,S., Ohira,M., Horie,H., Ando,K., Takayasu,H., Suzuki,Y.,
            Sugano,S., Hirata,T., Goto,T., Matsunaga,T., Hiyama,E., Hayashi,Y.,
            Ando,H., Suita,S., Kaneko,M., Sasaki,F., Hashizume,K., Ohnuma,N.
            and Nakagawara,A.
  TITLE     Expression profiling and differential screening between
            hepatoblastomas and the corresponding normal livers: identification
            of high expression of the PLK1 oncogene as a poor-prognostic
            indicator of hepatoblastomas
  JOURNAL   Oncogene 23 (35), 5901-5911 (2004)
   PUBMED   15221005
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP321361.1, AK093223.1 and
            DB376308.1.
            
            Summary: The protein encoded by this gene is a transmembrane
            protein and sodium-dependent lysophosphatidylcholine transporter.
            The encoded protein is involved in the establishment of the
            blood-brain barrier and is required for brain growth and function.
            Defects in this gene are a cause of a progressive microcephaly
            syndrome. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK093223.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.2"
     Protein         1..543
                     /product="sodium-dependent lysophosphatidylcholine
                     symporter 1 isoform 1"
                     /note="major facilitator superfamily domain-containing
                     protein 2A; sodium-dependent LPC symporter 1;
                     sodium-dependent lysophosphatidylcholine symporter 1;
                     major facilitator superfamily domain containing 2A"
                     /calculated_mol_wt=60039
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NA29.1)"
     Site            41..70
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NA29.1)"
     Region          46..509
                     /region_name="MFS_NLS1_MFSD2A"
                     /note="Sodium-dependent lysophosphatidylcholine symporter
                     1 of the Major Facilitator Superfamily of transporters;
                     cd17451"
                     /db_xref="CDD:341009"
     Site            order(56..57,60..61,64,110,171..172,174..176,179,200,
                     203..204,207,314,317..318,321..323,326,354,358,407..408,
                     412,416,441,444..445,448..449,452)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:341009"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NA29.1)"
     Site            128..147
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NA29.1)"
     Site            158..182
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NA29.1)"
     Site            190..221
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NA29.1)"
     Site            230
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:21677192; propagated from
                     UniProtKB/Swiss-Prot (Q8NA29.1)"
     Site            240
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305|PubMed:21677192; propagated from
                     UniProtKB/Swiss-Prot (Q8NA29.1)"
     Site            242..275
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NA29.1)"
     Site            307..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NA29.1)"
     Site            345..363
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NA29.1)"
     Site            368..389
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NA29.1)"
     Site            393..429
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NA29.1)"
     Site            440..466
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NA29.1)"
     Site            479..502
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NA29.1)"
     CDS             1..543
                     /gene="MFSD2A"
                     /gene_synonym="HsMFSD2A; MCPH15; MFSD2; NEDMISBA; NLS1;
                     SLC59A1"
                     /coded_by="NM_001136493.3:149..1780"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44118.1"
                     /db_xref="GeneID:84879"
                     /db_xref="HGNC:HGNC:25897"
                     /db_xref="MIM:614397"
ORIGIN      
        1 makgegaesg saagllptsi lqsterpaqv kkepkkkkqq lsvcnklcya lggapyqvtg
       61 calgfflqiy lldvaqkdee vvfcfssfqv gpfsasiilf vgrawdaitd plvglcisks
      121 pwtclgrlmp wiifstplav iayfliwfvp dfphgqtywy llfyclfetm vtcfhvpysa
      181 ltmfisteqt erdsatayrm tvevlgtvlg taiqgqivgq adtpcfqdln sstvasqsan
      241 hthgttshre tqkayllaag vivciyiica vililgvreq repyeaqqse piayfrglrl
      301 vmshgpyikl itgflftsla fmlvegnfvl fctytlgfrn efqnlllaim lsatltipiw
      361 qwfltrfgkk tavyvgissa vpflilvalm esnliityav avaagisvaa afllpwsmlp
      421 dviddfhlkq phfhgtepif fsfyvfftkf asgvslgist lsldfagyqt rgcsqpervk
      481 ftlnmlvtma pivlillgll lfkmypidee rrrqnkkalq alrdeasssg csetdstela
      541 sil
//
LOCUS       NP_001091968            1032 aa            linear   PRI 21-NOV-2025
DEFINITION  small G protein signaling modulator 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001091968
VERSION     NP_001091968.1
DBSOURCE    REFSEQ: accession NM_001098498.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Li,J., Wang,J., Ding,Y., Zhao,J. and Wang,W.
  TITLE     Prognostic biomarker SGSM1 and its correlation with immune
            infiltration in gliomas
  JOURNAL   BMC Cancer 22 (1), 466 (2022)
   PUBMED   35484511
  REMARK    GeneRIF: Prognostic biomarker SGSM1 and its correlation with immune
            infiltration in gliomas.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1032)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 1032)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 1032)
  AUTHORS   Nottingham,R.M., Pusapati,G.V., Ganley,I.G., Barr,F.A.,
            Lambright,D.G. and Pfeffer,S.R.
  TITLE     RUTBC2 protein, a Rab9A effector and GTPase-activating protein for
            Rab36
  JOURNAL   J Biol Chem 287 (27), 22740-22748 (2012)
   PUBMED   22637480
  REMARK    GeneRIF: These data show that RUTBC2 can act as a Rab36 GAP in
            cells and suggest that RUTBC2 links Rab9A function to Rab36
            function in the endosomal system.
REFERENCE   7  (residues 1 to 1032)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   8  (residues 1 to 1032)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1032)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
REFERENCE   10 (residues 1 to 1032)
  AUTHORS   Yang,H., Sasaki,T., Minoshima,S. and Shimizu,N.
  TITLE     Identification of three novel proteins (SGSM1, 2, 3) which modulate
            small G protein (RAP and RAB)-mediated signaling pathway
  JOURNAL   Genomics 90 (2), 249-260 (2007)
   PUBMED   17509819
  REMARK    GeneRIF: Identification of novel protein SGSM1 which modulate small
            G protein (RAP and RAB)-mediated signaling pathway.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP000359.1, AW028652.1, AB275761.1, AB075821.1, BC111698.1,
            BM930881.1 and AL050312.8.
            
            Transcript Variant: This variant (4) lacks two alternate in-frame
            exons, compared to variant 1, resulting in a shorter protein
            (isoform 4), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1573094.1,
                                           SRR14038195.2060024.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2155550
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.23"
     Protein         1..1032
                     /product="small G protein signaling modulator 1 isoform 4"
                     /note="RUN and TBC1 domain containing 2; small G protein
                     signaling modulator 1 protein; RUN and TBC1
                     domain-containing protein 2"
                     /calculated_mol_wt=116906
     Region          20..196
                     /region_name="RUN_SGSM1"
                     /note="RUN domain found in small G protein signaling
                     modulator 1 (SGSM1) and similar proteins; cd17703"
                     /db_xref="CDD:439065"
     Region          254..425
                     /region_name="PH_RUTBC"
                     /note="Rab-binding Pleckstrin homology domain (PH) of
                     small G-protein signaling modulator 1 and similar
                     proteins; cd15784"
                     /db_xref="CDD:275431"
     Region          <820..989
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     CDS             1..1032
                     /gene="SGSM1"
                     /gene_synonym="RUTBC2"
                     /coded_by="NM_001098498.3:116..3214"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:129049"
                     /db_xref="HGNC:HGNC:29410"
                     /db_xref="MIM:611417"
ORIGIN      
        1 masapaeaet rqrllrtvkk evkqimeeav trkfvhedss hiisfcaave acvlhglrrr
       61 aagflrsnki aalfmkvgkn fppaedlsrk vqdleqlies arnqiqglqe nvrklpklpn
      121 lsplaikhlw irtalfekvl dkivhylven sskyyekeal lmdpvdgpil asllvgpcal
      181 eytkmktadh fwtdpsadel vqrhrihssh vrqdsptkrp alciqkrhss gsmddrpsls
      241 ardyveslhq nsratllygk nnvlvqprdd meavpgylsl hqtadvmtlk wtpnqlmngs
      301 vgdldyeksv ywdyamtirl eeivylhchq qvdsggtvvl vsqdgiqrpp frfpkgghll
      361 qflsclengl lphgqldppl wsqrgkgkvf pklrkrspqg saestssdkd ddeatdyvfr
      421 iiypgmqsef vpqdlmdvsv snlpslwqps prksscsscs qsgsadgsst ngcnherapl
      481 kllcdnmkyq ilsrafygwl aycrhlstvr thlsalvnhm ivspdlpcda gqgltariwe
      541 qylhdstsye eqellrliyy ggiqpeirka vwpfllghyq fgmteterke ssqscssgrq
      601 nirlhsdsss stqvfesvde veqveaegrl eekqpkipng nlvngtcspd sghpsshnfs
      661 sglsehseps lstedsvlda qrntptvlrp rdgsvddrqs seattsqdea preelavqds
      721 lesdllanes mdefmsitgs ldmalpekdd vvmegwrsse tekhgqadse dnlseepeme
      781 slfpalasla vttsanevsp vsssgvtysp elldlytvnl hriekdvqrc drnywyftpa
      841 nleklrnimc syiwqhieig yvqgmcdlla pllvilddea lafscftelm krmnqnfphg
      901 gamdthfanm rsliqildse lfelmhqngd ythfyfcyrw flldfkrelv yddvflvwet
      961 iwaakhvssa hyvlfialal vevyrdiile nnmdftdiik ffnemaerhn tkqvlklard
     1021 lvykvqtlie nk
//
LOCUS       NP_001317078             161 aa            linear   PRI 21-NOV-2025
DEFINITION  B9 domain-containing protein 1 isoform j [Homo sapiens].
ACCESSION   NP_001317078 XP_005256664
VERSION     NP_001317078.1
DBSOURCE    REFSEQ: accession NM_001330149.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Okazaki,M., Kobayashi,T., Chiba,S., Takei,R., Liang,L., Nakayama,K.
            and Katoh,Y.
  TITLE     Formation of the B9-domain protein complex MKS1-B9D2-B9D1 is
            essential as a diffusion barrier for ciliary membrane proteins
  JOURNAL   Mol Biol Cell 31 (20), 2259-2268 (2020)
   PUBMED   32726168
  REMARK    GeneRIF: Formation of the B9-domain protein complex MKS1-B9D2-B9D1
            is essential as a diffusion barrier for ciliary membrane proteins.
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 161)
  AUTHORS   Hopp,K., Heyer,C.M., Hommerding,C.J., Henke,S.A., Sundsbak,J.L.,
            Patel,S., Patel,P., Consugar,M.B., Czarnecki,P.G., Gliem,T.J.,
            Torres,V.E., Rossetti,S. and Harris,P.C.
  TITLE     B9D1 is revealed as a novel Meckel syndrome (MKS) gene by targeted
            exon-enriched next-generation sequencing and deletion analysis
  JOURNAL   Hum Mol Genet 20 (13), 2524-2534 (2011)
   PUBMED   21493627
  REMARK    GeneRIF: B9D1 is a novel Meckel syndrome gene
REFERENCE   6  (residues 1 to 161)
  AUTHORS   Bialas,N.J., Inglis,P.N., Li,C., Robinson,J.F., Parker,J.D.,
            Healey,M.P., Davis,E.E., Inglis,C.D., Toivonen,T., Cottell,D.C.,
            Blacque,O.E., Quarmby,L.M., Katsanis,N. and Leroux,M.R.
  TITLE     Functional interactions between the ciliopathy-associated Meckel
            syndrome 1 (MKS1) protein and two novel MKS1-related (MKSR)
            proteins
  JOURNAL   J Cell Sci 122 (Pt 5), 611-624 (2009)
   PUBMED   19208769
  REMARK    GeneRIF: MKS-1 and MKS-1-related proteins 1 and 2 (MKSR-1/EPPB9,
            MKSR-2/B9D2), localize to transition zones/basal bodies of sensory
            cilia; subcellular localization is largely co-dependent, pointing
            to a functional relationship between the proteins
REFERENCE   7  (residues 1 to 161)
  AUTHORS   Williams,C.L., Winkelbauer,M.E., Schafer,J.C., Michaud,E.J. and
            Yoder,B.K.
  TITLE     Functional redundancy of the B9 proteins and nephrocystins in
            Caenorhabditis elegans ciliogenesis
  JOURNAL   Mol Biol Cell 19 (5), 2154-2168 (2008)
   PUBMED   18337471
  REMARK    GeneRIF: Ciliary transition zone localization.  Functions in a
            module with related proteins (MKS1 and B9D1) that cooperates with
            nephrocystins in ciliogenesis.
REFERENCE   8  (residues 1 to 161)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   9  (residues 1 to 161)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 161)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY047032.1, AC124066.6 and
            BM129815.1.
            
            On Aug 18, 2016 this sequence version replaced XP_005256664.1.
            
            Summary: This gene encodes a B9 domain-containing protein, one of
            several that are involved in ciliogenesis. Alterations in
            expression of this gene have been found in a family with Meckel
            syndrome. Meckel syndrome has been associated with at least six
            different genes. This gene is located within the Smith-Magenis
            syndrome region on chromosome 17. [provided by RefSeq, Mar 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM129815.1, SRR14038195.1461471.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..161
                     /product="B9 domain-containing protein 1 isoform j"
                     /note="endothelial precursor protein B9; B9
                     domain-containing protein 1; MKS1-related protein 1; B9
                     protein domain 1"
                     /calculated_mol_wt=17892
     Region          11..157
                     /region_name="B9-C2"
                     /note="Ciliary basal body-associated, B9 protein;
                     pfam07162"
                     /db_xref="CDD:462108"
     CDS             1..161
                     /gene="B9D1"
                     /gene_synonym="B9; EPPB9; JBTS27; MKS9; MKSR-1; MKSR1"
                     /coded_by="NM_001330149.2:155..640"
                     /note="isoform j is encoded by transcript variant 10"
                     /db_xref="GeneID:27077"
                     /db_xref="HGNC:HGNC:24123"
                     /db_xref="MIM:614144"
ORIGIN      
        1 mataspsvfl lmvngqvesa qfpeyddlyc kycfvygqdw aptagleegi sqitsksqdv
       61 rqalvwnfpi dvtfkstnpy gwpqivlsvy gpdvfgndvv rgygavhvpf spgrhkrtip
      121 mfvpestskl qkftswfmgr rpeytdpkvv aqgegreaqp g
//
LOCUS       NP_001363263             810 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger CCCH domain-containing protein 11A isoform 1 [Homo
            sapiens].
ACCESSION   NP_001363263 XP_016858446
VERSION     NP_001363263.1
DBSOURCE    REFSEQ: accession NM_001376334.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Kases,K., Schubert,E., Hajikhezri,Z., Larsson,M., Devi,P.,
            Darweesh,M., Andersson,L., Akusjarvi,G., Punga,T. and Younis,S.
  TITLE     The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts
  JOURNAL   J Biol Chem 299 (8), 104959 (2023)
   PUBMED   37356722
  REMARK    GeneRIF: The RNA-binding protein ZC3H11A interacts with the nuclear
            poly(A)-binding protein PABPN1 and alters polyadenylation of viral
            transcripts.
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 810)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 810)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114402.2.
            
            On Nov 14, 2019 this sequence version replaced XP_016858446.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.69549.1,
                                           SRR1803614.22574.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..810
                     /product="zinc finger CCCH domain-containing protein 11A
                     isoform 1"
                     /note="zinc finger CCCH-type domain containing 11A; zinc
                     finger CCCH domain-containing protein 11A"
                     /calculated_mol_wt=89000
     Region          1..110
                     /region_name="zf-CCCH_3"
                     /note="Zinc-finger containing family; pfam15663"
                     /db_xref="CDD:464787"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          139..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          223..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          285..351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          367..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75152.3)"
     Region          482..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     Region          715..768
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75152.3)"
     CDS             1..810
                     /gene="ZC3H11A"
                     /gene_synonym="ZC3HDC11A"
                     /coded_by="NM_001376334.1:1911..4343"
                     /note="isoform 1 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS30978.1"
                     /db_xref="GeneID:9877"
                     /db_xref="HGNC:HGNC:29093"
                     /db_xref="MIM:613513"
ORIGIN      
        1 mpnqgedcyf ffystctkgd scpfrhceaa ignetvctlw qegrcfrqvc rfrhmeidkk
       61 rseipcywen qptgcqklnc afhhnrgryv dglflppskt vlptvpespe eevkasqlsv
      121 qqnklsvqsn pspqlrsvmk vessenvpsp thppvvinaa dddeddddqf seegdetktp
      181 tlqptpevhn glrvtsvrkp avnikqgecl nfgiktleei kskkmkeksk kqgegssgvs
      241 slllhpepvp gpekenvrtv vrtvtlstkq geeplvrlsl terlgkrkfs aggdsdpplk
      301 rslaqrlgkk veapetnidk tpkkaqvsks lkerlgmsad pdnedatdkv nkvgeihvkt
      361 leeilleras qkrgelqtkl ktegpsktdd stsgarssst iriktfsevl aekkhrqqea
      421 erqkskkdtt ciklkidsei kktvvlppiv asrgqseepa gktksmqevh iktleeikle
      481 kalrvqqsse sstsspsqhe atpgarrllr itkrtgmkee knlqegnevd sqssirteak
      541 easgettgvd itkiqvkrce tmrekhmqkq qereksvltp lrgdvascnt qvaekpvlta
      601 vpgitrhltk rlptkssqkv evetsgigds llnvkcaaqt lekrgkakpk vnvkpsvvkv
      661 vsspklapkr kavemhaavi aavkplssss vlqeppakka avavvplvse dksvtvpeae
      721 nprdslvlpp tqsssdsspp evsgpsssqm smktrrlssa stgkpplsve ddfekliwei
      781 sggkleaeid ldpgkdeddl llelsemids
//
LOCUS       NP_001035859             541 aa            linear   PRI 21-NOV-2025
DEFINITION  centrosomal protein of 63 kDa isoform b [Homo sapiens].
ACCESSION   NP_001035859
VERSION     NP_001035859.1
DBSOURCE    REFSEQ: accession NM_001042400.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Kodani,A., Knopp,K.A., Di Lullo,E., Retallack,H., Kriegstein,A.R.,
            DeRisi,J.L. and Reiter,J.F.
  TITLE     Zika virus alters centrosome organization to suppress the innate
            immune response
  JOURNAL   EMBO Rep 23 (9), e52211 (2022)
   PUBMED   35793002
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Ling,H., Cao,C.H., Han,K., Lv,Y.R., Ma,X.D., Cao,J.H., Chen,J.W.,
            Li,S., Lin,J.L., Fang,Y.J., Pan,Z.Z., Xie,D. and Wang,F.W.
  TITLE     CEP63 upregulates YAP1 to promote colorectal cancer progression
            through stabilizing RNA binding protein FXR1
  JOURNAL   Oncogene 41 (39), 4433-4445 (2022)
   PUBMED   35989368
  REMARK    GeneRIF: CEP63 upregulates YAP1 to promote colorectal cancer
            progression through stabilizing RNA binding protein FXR1.
REFERENCE   3  (residues 1 to 541)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Liu,C., Yu,F., Ma,R., Zhang,L., Du,G., Niu,D. and Yin,D.
  TITLE     Cep63 knockout inhibits the malignant phenotypes of papillary
            thyroid cancer cell line TPC-1
  JOURNAL   Oncol Rep 46 (3) (2021)
   PUBMED   34296302
  REMARK    GeneRIF: Cep63 knockout inhibits the malignant phenotypes of
            papillary thyroid cancer cell line TPC1.
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Mahjabeen,I., Maqsood,Y., Abbasi,R., Ahmed,M.W. and Kayani,M.A.
  TITLE     Polymorphism in miRNA target sites of CEP-63 and CEP-152 ring
            complex influences expression of CEP genes and favors tumorigenesis
            in glioma
  JOURNAL   Future Oncol 17 (25), 3355-3372 (2021)
   PUBMED   34156311
  REMARK    GeneRIF: Polymorphism in miRNA target sites of CEP-63 and CEP-152
            ring complex influences expression of CEP genes and favors
            tumorigenesis in glioma.
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Morris,J.A., Kandpal,G., Ma,L. and Austin,C.P.
  TITLE     DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated
            protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL:
            regulation and loss of interaction with mutation
  JOURNAL   Hum Mol Genet 12 (13), 1591-1608 (2003)
   PUBMED   12812986
REFERENCE   7  (residues 1 to 541)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   8  (residues 1 to 541)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   9  (residues 1 to 541)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   10 (residues 1 to 541)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010207.18, AC026117.15,
            AC139764.5 and AC109912.10.
            
            Summary: This gene encodes a protein with six coiled-coil domains.
            The protein is localized to the centrosome, a non-membraneous
            organelle that functions as the major microtubule-organizing center
            in animal cells. Several alternatively spliced transcript variants
            have been found, but their biological validity has not been
            determined. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1608549.1, BC068997.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.2"
     Protein         1..541
                     /product="centrosomal protein of 63 kDa isoform b"
                     /note="centrosome protein CEP63; centrosomal protein
                     63kDa"
                     /calculated_mol_wt=62884
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q96MT8.1)"
     Region          18..280
                     /region_name="CEP63"
                     /note="Centrosomal protein of 63 kDa; pfam17045"
                     /db_xref="CDD:465338"
     Region          <136..464
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96MT8.1)"
     CDS             1..541
                     /gene="CEP63"
                     /gene_synonym="SCKL6"
                     /coded_by="NM_001042400.3:172..1797"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43153.1"
                     /db_xref="GeneID:80254"
                     /db_xref="HGNC:HGNC:25815"
                     /db_xref="MIM:614724"
ORIGIN      
        1 meallegiqn rghgggflts ceaelqelmk qidimvahkk sewegrthal etclkireqe
       61 lkslrsqldv thkevgmlhq qveehekikq emtmeykqel kklheelcil krsyeklqkk
      121 qmrefrgntk nhredrseie rltakieefr qksldwekqr liyqqqvssl eaqrkalaeq
      181 seiiqaqlvn rkqklesvel ssqseiqhls sklerandti caneleierl tmrvndlvgt
      241 smtvlqeqqq keeklresek llealqeekr elkaalqsqe nliheariqk eklqekvkat
      301 ntqhaveair preeslaekk ytsqgqgdld svlsqlnfth tsedllqaev tclegslesv
      361 satckqlsqe lmekyeelkr meahnneyka eikklkeqil qgeqsyssal egmkmeishl
      421 tqelhqrdit iastkgsssd mekrlraemq kaedkavehk eildqleslk lenrhlsemv
      481 mklelglhec slpvsplgsi atrfleeeel rshhilerld ahieelkres ektvrqftal
      541 k
//
LOCUS       NP_001387286             308 aa            linear   PRI 21-NOV-2025
DEFINITION  single-stranded DNA-binding protein 2 isoform 25 [Homo sapiens].
ACCESSION   NP_001387286
VERSION     NP_001387286.1
DBSOURCE    REFSEQ: accession NM_001400357.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Schwab,C., Roberts,K., Boer,J.M., Gohring,G., Steinemann,D.,
            Vora,A., Macartney,C., Hough,R., Thorn,Z., Dillon,R., Escherich,G.,
            Cazzaniga,G., Schlegelberger,B., Loh,M., den Boer,M.L.,
            Moorman,A.V. and Harrison,C.J.
  TITLE     SSBP2-CSF1R is a recurrent fusion in B-lineage acute lymphoblastic
            leukemia with diverse genetic presentation and variable outcome
  JOURNAL   Blood 137 (13), 1835-1838 (2021)
   PUBMED   33197935
  REMARK    GeneRIF: SSBP2-CSF1R is a recurrent fusion in B-lineage acute
            lymphoblastic leukemia with diverse genetic presentation and
            variable outcome.
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Wang,H., Kim,J., Wang,Z., Yan,X.X., Dean,A. and Xu,W.
  TITLE     Crystal structure of human LDB1 in complex with SSBP2
  JOURNAL   Proc Natl Acad Sci U S A 117 (2), 1042-1048 (2020)
   PUBMED   31892537
  REMARK    GeneRIF: Single-stranded DNA binding proteins (SSBPs) interact
            specifically with the LDB/Chip conserved domain (LCCD) of LDB
            proteins and stabilize LDBs by preventing their proteasomal
            degradation, thus promoting their functions in gene regulation.
REFERENCE   5  (residues 1 to 308)
  AUTHORS   Kim,H., Kim,Y., Bang,S., Park,S., Jee,S., Sim,J., Shin,S.J.,
            Paik,S.S. and Jang,K.
  TITLE     Low Expression of Single-stranded DNA Binding Protein 2 (SSBP2)
            Predicts Unfavourable Postoperative Outcomes in Patients With Clear
            Cell Renal Cell Carcinoma
  JOURNAL   In Vivo 34 (1), 101-107 (2020)
   PUBMED   31882468
  REMARK    GeneRIF: CcRCC with low SSBP2 expression was associated with
            adverse clinicopathological characteristics and poor patient
            outcomes.
REFERENCE   6  (residues 1 to 308)
  AUTHORS   Fleisig,H.B., Orazio,N.I., Liang,H., Tyler,A.F., Adams,H.P.,
            Weitzman,M.D. and Nagarajan,L.
  TITLE     Adenoviral E1B55K oncoprotein sequesters candidate leukemia
            suppressor sequence-specific single-stranded DNA-binding protein 2
            into aggresomes
  JOURNAL   Oncogene 26 (33), 4797-4805 (2007)
   PUBMED   17311003
  REMARK    GeneRIF: Results suggest that subverting SSBP2 function by
            oncoprotein E1B55K may contribute to cell transformation by viral
            oncoproteins.
REFERENCE   7  (residues 1 to 308)
  AUTHORS   Liang,H., Samanta,S. and Nagarajan,L.
  TITLE     SSBP2, a candidate tumor suppressor gene, induces growth arrest and
            differentiation of myeloid leukemia cells
  JOURNAL   Oncogene 24 (16), 2625-2634 (2005)
   PUBMED   15782145
  REMARK    GeneRIF: Our findings are consistent with human SSBP2 being a novel
            regulator of hematopoietic growth and differentiation, whose loss
            confers a block in differentiation advantage to myeloid leukemic
            cells.
REFERENCE   8  (residues 1 to 308)
  AUTHORS   Castro,P., Liang,H., Liang,J.C. and Nagarajan,L.
  TITLE     A novel, evolutionarily conserved gene family with putative
            sequence-specific single-stranded DNA-binding activity
  JOURNAL   Genomics 80 (1), 78-85 (2002)
   PUBMED   12079286
  REMARK    GeneRIF: Member of a closely related, evolutionarily conserved, and
            ubiquitously expressed gene family, potential tumor suppressor
REFERENCE   9  (residues 1 to 308)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 308)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016562.7, AC093250.3,
            AC026419.5 and AC010623.10.
            
            Summary: This gene encodes a subunit of a protein complex that
            interacts with single-stranded DNA and is involved in the DNA
            damage response and maintenance of genome stability. The encoded
            protein may also play a role in telomere repair. A variant of this
            gene may be associated with survival in human glioblastoma
            patients. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.205924.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.1"
     Protein         1..308
                     /product="single-stranded DNA-binding protein 2 isoform
                     25"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein 2"
                     /calculated_mol_wt=31915
     Region          19..45
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          83..307
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     CDS             1..308
                     /gene="SSBP2"
                     /gene_synonym="HSPC116; SOSS-B2"
                     /coded_by="NM_001400357.1:56..982"
                     /note="isoform 25 is encoded by transcript variant 28"
                     /db_xref="GeneID:23635"
                     /db_xref="HGNC:HGNC:15831"
                     /db_xref="MIM:607389"
ORIGIN      
        1 mygkgksnss avpsdsqare klalyvyeyl lhvgaqksaq tflseirwek nitlgeppgf
       61 lhswwcvfwd lycaaperre tcehsseaka fhdysaaaap spvlgnippg dgmpvgpvpp
      121 gffqalggvp gsqpllpsgm dptrqqghpn mggpmqrmtp prgmvplgpq nyggamrppl
      181 nalggpgmpg mnmgpgggrp wpnptnansi pyssaspgny vgppggggpp gtpimpspad
      241 stnsgdnmyt lmnavppgpn rpnfpmgpgs dgpmgglggm eshhmngslg sgdmdsisky
      301 spsmtmsv
//
LOCUS       NP_001372329             464 aa            linear   PRI 21-NOV-2025
DEFINITION  interferon regulatory factor 9 isoform 1 [Homo sapiens].
ACCESSION   NP_001372329
VERSION     NP_001372329.1
DBSOURCE    REFSEQ: accession NM_001385400.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Ritter,J., Szelinski,F., Aue,A., Stefanski,A.L., Rincon-Arevalo,H.,
            Chen,Y., Nitschke,E., Dang,V.D., Wiedemann,A., Schrezenmeier,E.,
            Lino,A.C. and Dorner,T.
  TITLE     Elevated unphosphorylated STAT1 and IRF9 in T and B cells of
            primary sjogren's syndrome: Novel biomarkers for disease activity
            and subsets
  JOURNAL   J Autoimmun 147, 103243 (2024)
   PUBMED   38788537
  REMARK    GeneRIF: Elevated unphosphorylated STAT1 and IRF9 in T and B cells
            of primary sjogren's syndrome: Novel biomarkers for disease
            activity and subsets.
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Calvo-Apalategi,A., Nevado,M.L., Bravo-Gallego,L.Y.,
            Gonzalez-Granado,L.I., Allende,L.M., Pena,R.R., Lopez-Granados,E.
            and Reyburn,H.T.
  TITLE     The lack of either IRF9, or STAT2, has surprisingly little effect
            on human natural killer cell development and function
  JOURNAL   Immunology 172 (3), 440-450 (2024)
   PUBMED   38514903
  REMARK    GeneRIF: The lack of either IRF9, or STAT2, has surprisingly little
            effect on human natural killer cell development and function.
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Nowicka,H., Sekrecka,A., Blaszczyk,K., Kluzek,K., Chang,C.Y.,
            Wesoly,J., Lee,C.K. and Bluyssen,H.A.R.
  TITLE     ISGF3 and STAT2/IRF9 Control Basal and IFN-Induced Transcription
            through Genome-Wide Binding of Phosphorylated and Unphosphorylated
            Complexes to Common ISRE-Containing ISGs
  JOURNAL   Int J Mol Sci 24 (24), 17635 (2023)
   PUBMED   38139463
  REMARK    GeneRIF: ISGF3 and STAT2/IRF9 Control Basal and IFN-Induced
            Transcription through Genome-Wide Binding of Phosphorylated and
            Unphosphorylated Complexes to Common ISRE-Containing ISGs.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 464)
  AUTHORS   You,Y., Grasso,E., Alvero,A., Condon,J., Dimova,T., Hu,A., Ding,J.,
            Alexandrova,M., Manchorova,D., Dimitrova,V., Liao,A. and Mor,G.
  TITLE     Twist1-IRF9 Interaction Is Necessary for IFN-Stimulated Gene
            Anti-Zika Viral Infection
  JOURNAL   J Immunol 210 (12), 1899-1912 (2023)
   PUBMED   37144865
  REMARK    GeneRIF: Twist1-IRF9 Interaction Is Necessary for IFN-Stimulated
            Gene Anti-Zika Viral Infection.
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Martinez-Moczygemba,M., Gutch,M.J., French,D.L. and Reich,N.C.
  TITLE     Distinct STAT structure promotes interaction of STAT2 with the p48
            subunit of the interferon-alpha-stimulated transcription factor
            ISGF3
  JOURNAL   J Biol Chem 272 (32), 20070-20076 (1997)
   PUBMED   9242679
REFERENCE   7  (residues 1 to 464)
  AUTHORS   Horvath,C.M., Stark,G.R., Kerr,I.M. and Darnell,J.E. Jr.
  TITLE     Interactions between STAT and non-STAT proteins in the
            interferon-stimulated gene factor 3 transcription complex
  JOURNAL   Mol Cell Biol 16 (12), 6957-6964 (1996)
   PUBMED   8943351
REFERENCE   8  (residues 1 to 464)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
REFERENCE   9  (residues 1 to 464)
  AUTHORS   David,M., Romero,G., Zhang,Z.Y., Dixon,J.E. and Larner,A.C.
  TITLE     In vitro activation of the transcription factor ISGF3 by interferon
            alpha involves a membrane-associated tyrosine phosphatase and
            tyrosine kinase
  JOURNAL   J Biol Chem 268 (9), 6593-6599 (1993)
   PUBMED   8454630
REFERENCE   10 (residues 1 to 464)
  AUTHORS   Veals,S.A., Schindler,C., Leonard,D., Fu,X.Y., Aebersold,R.,
            Darnell,J.E. Jr. and Levy,D.E.
  TITLE     Subunit of an alpha-interferon-responsive transcription factor is
            related to interferon regulatory factor and Myb families of
            DNA-binding proteins
  JOURNAL   Mol Cell Biol 12 (8), 3315-3324 (1992)
   PUBMED   1630447
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136295.3.
            
            Summary: This gene encodes a member of the interferon regulatory
            factor (IRF) family, a group of transcription factors with diverse
            roles, including virus-mediated activation of interferon, and
            modulation of cell growth, differentiation, apoptosis, and immune
            system activity. Members of the IRF family are characterized by a
            conserved N-terminal DNA-binding domain containing tryptophan (W)
            repeats. Mutations in this gene result in Immunodeficiency 65.
            [provided by RefSeq, Jul 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1497569.1,
                                           SRR18074968.1445481.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..464
                     /product="interferon regulatory factor 9 isoform 1"
                     /note="interferon-stimulated transcription factor 3, gamma
                     48kDa; interferon-stimulated transcription factor 3, gamma
                     (48kD); ISGF-3 gamma; ISGF3 p48 subunit;
                     interferon-stimulated gene factor 3 gamma; transcriptional
                     regulator ISGF3 subunit gamma; IFN-alpha-responsive
                     transcription factor subunit"
                     /calculated_mol_wt=50762
     Region          11..115
                     /region_name="IRF"
                     /note="Interferon regulatory factor transcription factor;
                     pfam00605"
                     /db_xref="CDD:459863"
     Site            order(44,83,85..86,89)
                     /site_type="other"
                     /note="DNA sequence recognition sites [nucleotide
                     binding]"
                     /db_xref="CDD:238051"
     Site            order(88..89,91,94)
                     /site_type="metal-binding"
                     /db_xref="CDD:238051"
     Region          226..>340
                     /region_name="IRF-3"
                     /note="Interferon-regulatory factor 3; pfam10401"
                     /db_xref="CDD:463076"
     CDS             1..464
                     /gene="IRF9"
                     /gene_synonym="IRF-9; ISGF3; ISGF3G; p48"
                     /coded_by="NM_001385400.1:76..1470"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS91853.1"
                     /db_xref="GeneID:10379"
                     /db_xref="HGNC:HGNC:6131"
                     /db_xref="MIM:147574"
ORIGIN      
        1 masgrarctr klrnwvveqv esgqfpgvcw ddtaktmfri pwkhagkqdf redqdaaffk
       61 awaifkgkyk egdtggpavw ktrlrcalnk ssefkevper grmdvaepyk vyqllppgiv
      121 sgqpgtqkvp skrqhssvss erkeeedamq nctlspsvlq dslnneeega sggavhsdig
      181 ssssssspep qevtdtteap fqgdqrslef llppepapgr avlspdysll ltfiyngrvv
      241 geaqvqsldc rlvaepsgse ssmeqvlfpk pgpleptqrl lsqlergilv asnprglfvq
      301 rlcpipiswn apqappgpgp hllpsnecve lfrtayfcrd ppcslcmall rlcvaypvwp
      361 yaqpgsylaa llqprqwkrw frlgqvlsgp gpptevpgnt eflgrepwlq pystesyhse
      421 dgaglcpila gadsraagsh svpgvepggp ifhltslffl splk
//
LOCUS       NP_001003703             108 aa            linear   PRI 21-NOV-2025
DEFINITION  ATP synthase peripheral stalk subunit F6, mitochondrial isoform a
            precursor [Homo sapiens].
ACCESSION   NP_001003703
VERSION     NP_001003703.1
DBSOURCE    REFSEQ: accession NM_001003703.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Hochstrasser,D.F., Frutiger,S., Paquet,N., Bairoch,A., Ravier,F.,
            Pasquali,C., Sanchez,J.C., Tissot,J.D., Bjellqvist,B., Vargas,R. et
            al.
  TITLE     Human liver protein map: a reference database established by
            microsequencing and gel comparison
  JOURNAL   Electrophoresis 13 (12), 992-1001 (1992)
   PUBMED   1286669
REFERENCE   8  (residues 1 to 108)
  AUTHORS   Higuti,T., Tsurumi,C., Kawamura,Y., Tsujita,H., Osaka,F.,
            Yoshihara,Y., Tani,I., Tanaka,K. and Ichihara,A.
  TITLE     Molecular cloning of cDNA for the import precursor of human
            coupling factor 6 of H(+)-ATP synthase in mitochondria
  JOURNAL   Biochem Biophys Res Commun 178 (2), 793-799 (1991)
   PUBMED   1830479
REFERENCE   9  (residues 1 to 108)
  AUTHORS   Javed,A.A., Ogata,K. and Sanadi,D.R.
  TITLE     Human mitochondrial ATP synthase: cloning cDNA for the
            nuclear-encoded precursor of coupling factor 6
  JOURNAL   Gene 97 (2), 307-310 (1991)
   PUBMED   1825642
REFERENCE   10 (residues 1 to 108)
  AUTHORS   Boyer,P.D., Cross,R.L. and Momsen,W.
  TITLE     A new concept for energy coupling in oxidative phosphorylation
            based on a molecular explanation of the oxygen exchange reactions
  JOURNAL   Proc Natl Acad Sci U S A 70 (10), 2837-2839 (1973)
   PUBMED   4517936
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ268216.1, BC001178.1,
            BC066310.1 and AI085837.1.
            
            Summary: Mitochondrial ATP synthase catalyzes ATP synthesis,
            utilizing an electrochemical gradient of protons across the inner
            membrane during oxidative phosphorylation. It is composed of two
            linked multi-subunit complexes: the soluble catalytic core, F1, and
            the membrane-spanning component, Fo, which comprises the proton
            channel. The F1 complex consists of 5 different subunits (alpha,
            beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3
            beta, and a single representative of the other 3. The Fo complex
            has nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene
            encodes the F6 subunit of the Fo complex. The F6 subunit is
            required for F1 and Fo interactions. Alternatively spliced
            transcript variants encoding different isoforms have been
            identified for this gene. This gene has 1 or more pseudogenes.
            [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2, 3, 4, 6 and 7 encode the same isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM772791.1, DA684306.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000284971.8/
                                                  ENSP00000284971.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..108
                     /product="ATP synthase peripheral stalk subunit F6,
                     mitochondrial isoform a precursor"
                     /EC_number="3.6.1.14"
                     /note="ATP synthase, H+ transporting, mitochondrial F0
                     complex, subunit F6; coupling factor 6; mitochondrial ATP
                     synthase, subunit F6; mitochondrial ATPase coupling factor
                     6; mitochondrial ATP synthase, coupling factor 6; ATP
                     synthase-coupling factor 6, mitochondrial;
                     proliferation-inducing protein 36; ATPase subunit F6; ATP
                     synthase, H+ transporting, mitochondrial Fo complex
                     subunit F6; ATP synthase subunit h; ATP synthase
                     peripheral stalk subunit F6, mitochondrial"
                     /calculated_mol_wt=8960
     Region          1..96
                     /region_name="ATP-synt_F6"
                     /note="Mitochondrial ATP synthase coupling factor 6;
                     pfam05511"
                     /db_xref="CDD:461669"
     transit_peptide 1..32
                     /calculated_mol_wt=3645
     mat_peptide     33..108
                     /product="ATP synthase peripheral stalk subunit F6,
                     mitochondrial isoform a"
                     /calculated_mol_wt=8960
     Site            41
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P18859.1)"
     Site            46
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P18859.1)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P18859.1)"
     Site            79
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P97450; propagated from
                     UniProtKB/Swiss-Prot (P18859.1)"
     Site            94
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P97450; propagated from
                     UniProtKB/Swiss-Prot (P18859.1)"
     Site            99
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P18859.1)"
     Site            105
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P18859.1)"
     CDS             1..108
                     /gene="ATP5PF"
                     /gene_synonym="ATP5; ATP5A; ATP5J; ATPM; CF6; F6"
                     /coded_by="NM_001003703.2:60..386"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS13574.1"
                     /db_xref="GeneID:522"
                     /db_xref="HGNC:HGNC:847"
                     /db_xref="MIM:603152"
ORIGIN      
        1 milqrlfrfs svirsavsvh lrrnigvtav afnkeldpiq klfvdkirey kskrqtsggp
       61 vdasseyqqe lerelfklkq mfgnadmntf ptfkfedpkf eviekpqa
//
LOCUS       NP_001166170             959 aa            linear   PRI 21-NOV-2025
DEFINITION  peroxisome proliferator-activated receptor gamma coactivator 1-beta
            isoform 3 [Homo sapiens].
ACCESSION   NP_001166170
VERSION     NP_001166170.1
DBSOURCE    REFSEQ: accession NM_001172699.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 959)
  AUTHORS   Huang,M., Prasad,R.B., Coral,D.E., Hjort,L., Minja,D.T.R.,
            Mulder,H., Franks,P.W. and Kalamajski,S.
  TITLE     Human Genetic Variation at rs10071329 Correlates With
            Adiposity-Related Traits, Modulates PPARGC1B Expression, and Alters
            Brown Adipocyte Function
  JOURNAL   Diabetes 73 (4), 637-645 (2024)
   PUBMED   38190589
  REMARK    GeneRIF: Human Genetic Variation at rs10071329 Correlates With
            Adiposity-Related Traits, Modulates PPARGC1B Expression, and Alters
            Brown Adipocyte Function.
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Shimoda,F., Naito,T., Kakuta,Y., Kawai,Y., Tokunaga,K.,
            Shimoyama,Y., Moroi,R., Shiga,H., Nagasaki,M., Kinouchi,Y. and
            Masamune,A.
  CONSRTM   NCBN Controls WGS Consortium
  TITLE     HLA-DQA1*05 and upstream variants of PPARGC1B are associated with
            infliximab persistence in Japanese Crohn's disease patients
  JOURNAL   Pharmacogenomics J 23 (6), 141-148 (2023)
   PUBMED   37460671
  REMARK    GeneRIF: HLA-DQA1*05 and upstream variants of PPARGC1B are
            associated with infliximab persistence in Japanese Crohn's disease
            patients.
REFERENCE   4  (residues 1 to 959)
  AUTHORS   Torres,H.M., Yeo,D. and Westendorf,J.J.
  TITLE     Pulling rank with RNA: RANKL promotes the association of
            PGC-1beta/RNA complexes with NCoR/HDAC3 to activate gene expression
            in osteoclasts
  JOURNAL   Mol Cell 83 (19), 3397-3399 (2023)
   PUBMED   37802020
  REMARK    GeneRIF: Pulling rank with RNA: RANKL promotes the association of
            PGC-1beta/RNA complexes with NCoR/HDAC3 to activate gene expression
            in osteoclasts.
REFERENCE   5  (residues 1 to 959)
  AUTHORS   Chen,S., Zhang,P., Feng,J., Li,R., Chen,J., Zheng,W.V., Zhang,H.
            and Yao,P.
  TITLE     LMP1 mediates tumorigenesis through persistent epigenetic
            modifications and PGC1beta upregulation
  JOURNAL   Oncol Rep 49 (3) (2023)
   PUBMED   36734290
  REMARK    GeneRIF: LMP1 mediates tumorigenesis through persistent epigenetic
            modifications and PGC1beta upregulation.
REFERENCE   6  (residues 1 to 959)
  AUTHORS   Meirhaeghe,A., Crowley,V., Lenaghan,C., Lelliott,C., Green,K.,
            Stewart,A., Hart,K., Schinner,S., Sethi,J.K., Yeo,G., Brand,M.D.,
            Cortright,R.N., O'Rahilly,S., Montague,C. and Vidal-Puig,A.J.
  TITLE     Characterization of the human, mouse and rat PGC1 beta
            (peroxisome-proliferator-activated receptor-gamma co-activator 1
            beta) gene in vitro and in vivo
  JOURNAL   Biochem J 373 (Pt 1), 155-165 (2003)
   PUBMED   12678921
REFERENCE   7  (residues 1 to 959)
  AUTHORS   Lin,J., Puigserver,P., Donovan,J., Tarr,P. and Spiegelman,B.M.
  TITLE     Peroxisome proliferator-activated receptor gamma coactivator 1beta
            (PGC-1beta), a novel PGC-1-related transcription coactivator
            associated with host cell factor
  JOURNAL   J Biol Chem 277 (3), 1645-1648 (2002)
   PUBMED   11733490
REFERENCE   8  (residues 1 to 959)
  AUTHORS   Ek,J., Andersen,G., Urhammer,S.A., Gaede,P.H., Drivsholm,T.,
            Borch-Johnsen,K., Hansen,T. and Pedersen,O.
  TITLE     Mutation analysis of peroxisome proliferator-activated
            receptor-gamma coactivator-1 (PGC-1) and relationships of
            identified amino acid polymorphisms to Type II diabetes mellitus
  JOURNAL   Diabetologia 44 (12), 2220-2226 (2001)
   PUBMED   11793024
REFERENCE   9  (residues 1 to 959)
  AUTHORS   Knutti,D., Kaul,A. and Kralli,A.
  TITLE     A tissue-specific coactivator of steroid receptors, identified in a
            functional genetic screen
  JOURNAL   Mol Cell Biol 20 (7), 2411-2422 (2000)
   PUBMED   10713165
REFERENCE   10 (residues 1 to 959)
  AUTHORS   Esterbauer,H., Oberkofler,H., Krempler,F. and Patsch,W.
  TITLE     Human peroxisome proliferator activated receptor gamma coactivator
            1 (PPARGC1) gene: cDNA sequence, genomic organization, chromosomal
            localization, and tissue expression
  JOURNAL   Genomics 62 (1), 98-102 (1999)
   PUBMED   10585775
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK123614.1, AC008545.3 and
            CA435617.1.
            
            Summary: The protein encoded by this gene stimulates the activity
            of several transcription factors and nuclear receptors, including
            estrogen receptor alpha, nuclear respiratory factor 1, and
            glucocorticoid receptor. The encoded protein may be involved in fat
            oxidation, non-oxidative glucose metabolism, and the regulation of
            energy expenditure. This protein is downregulated in prediabetic
            and type 2 diabetes mellitus patients. Certain allelic variations
            in this gene increase the risk of the development of obesity. Three
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Mar 2010].
            
            Transcript Variant: This variant (3) represents use of an alternate
            promoter and 5' UTR, uses a distinct start codon, and lacks an
            alternate in-frame exon in the 5' coding region, compared to
            variant 1. The resulting isoform (3) has a shorter and distinct
            N-terminus and lacks an internal segment, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK123614.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2152798
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..959
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator 1-beta isoform 3"
                     /note="PGC-1-related estrogen receptor alpha coactivator;
                     PPARGC-1-beta; PPAR-gamma coactivator 1-beta; peroxisome
                     proliferator-activated receptor gamma, coactivator 1 beta;
                     PPARgamma coactivator 1 beta; PPARAGCIbeta"
                     /calculated_mol_wt=106099
     Region          831..927
                     /region_name="RRM_PPARGC1B"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator 1-beta
                     (PGC-1-beta) and similar proteins; cd12356"
                     /db_xref="CDD:409792"
     CDS             1..959
                     /gene="PPARGC1B"
                     /gene_synonym="ERRL1; PERC; PGC-1(beta); PGC1B"
                     /coded_by="NM_001172699.2:198..3077"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS54934.1"
                     /db_xref="GeneID:133522"
                     /db_xref="HGNC:HGNC:30022"
                     /db_xref="MIM:608886"
ORIGIN      
        1 mgggsgeeql yadfpeldls qldasdfdsa tcfgelqwcp ensetepnqy spddselfqi
       61 dseneallae ltktlddipe ddvglaafpa ldggdalsct saspapssap pspapekpsa
      121 papevdelsl adstqdkkap mmqsqsrsct elhkhltsaq cclqdrglqp pclqsprlpa
      181 kedkepgedc pspqpapasp rdslalgrad pgapvsqedm qamvqlirym htyclpqrkl
      241 ppqtpeplpk acsnpsqqvr srpwsrhhsk aswaefsilr ellaqdvlcd vskpyrlatp
      301 vyasltprsr prppkdsqas pgrpssveev riaaspkstg prpslrplrl evkrevrrpa
      361 rlqqqeeede eeeeeeeeee keeeeewgrk rpgrglpwtk lgrklessvc pvrrsrrlnp
      421 elgpwltfad eplvpsepqg alpslclapk aydverelgs ptdedsgqdq qllrgpqipa
      481 lespcesgcg dmdedpscpq lpprdsprcl mlalsqsdpt fgkksfeqtl tvelcgtagl
      541 tppttppykp teedpfkpdi khslgkeial slpspeglsl katpgaahkl pkkhpersel
      601 lshlrhataq pasqagqkrp fscsfgdhdy cqvlrpegvl qrkvlrswep sgvhledwpq
      661 qgapwaeaqa pgreedrscd agappkdstl lrdheirasl tkhfglleta leeedlasck
      721 speydtvfed sssssgessf lpeeeeeege eeeeddeeed sgvsptcsdh cpyqsppska
      781 nrqlcsrsrs ssgsspchsw spatrrnfrc esrgpcsdrt psirharkrr ekaigegrvv
      841 yiqnlssdms srelkrrfev fgeieecevl trnrrgekyg fityrcseha alsltkgaal
      901 rkrnepsfql sygglrhfcw prytdydsns eealpasgks kyeamdfdsl lkeaqqslh
//
LOCUS       NP_067061                221 aa            linear   PRI 21-NOV-2025
DEFINITION  SIN3-HDAC complex-associated factor [Homo sapiens].
ACCESSION   NP_067061
VERSION     NP_067061.1
DBSOURCE    REFSEQ: accession NM_021238.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Jhuang,Y.L., Yang,C.W., Tseng,Y.F., Hsu,C.L., Li,H.Y., Yuan,R.H.
            and Jeng,Y.M.
  TITLE     SIN3-HDAC complex-associated factor, a chromatin remodelling gene
            located in the 12p amplicon, is a potential germ cell
            tumour-specific oncogene
  JOURNAL   J Pathol 258 (4), 353-365 (2022)
   PUBMED   36056608
  REMARK    GeneRIF: SIN3-HDAC complex-associated factor, a chromatin
            remodelling gene located in the 12p amplicon, is a potential germ
            cell tumour-specific oncogene.
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Zhang,Y., Li,J.H., Yuan,Q.G. and Yang,W.B.
  TITLE     Restraint of FAM60A has a cancer-inhibiting role in pancreatic
            carcinoma via the effects on the Akt/GSK-3beta/beta-catenin
            signaling pathway
  JOURNAL   Environ Toxicol 37 (6), 1432-1444 (2022)
   PUBMED   35213078
  REMARK    GeneRIF: Restraint of FAM60A has a cancer-inhibiting role in
            pancreatic carcinoma via the effects on the
            Akt/GSK-3beta/beta-catenin signaling pathway.
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Sun,Y.H., Sun,X.W., Yang,L., Cheng,B. and Chen,Y.L.
  TITLE     [Research Progress of FAM60A in the Regulation of Cellular
            Function]
  JOURNAL   Zhongguo Yi Xue Ke Xue Yuan Xue Bao 43 (3), 469-474 (2021)
   PUBMED   34238425
  REMARK    GeneRIF: [Research Progress of FAM60A in the Regulation of Cellular
            Function].
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 221)
  AUTHORS   Joshi,P., Greco,T.M., Guise,A.J., Luo,Y., Yu,F., Nesvizhskii,A.I.
            and Cristea,I.M.
  TITLE     The functional interactome landscape of the human histone
            deacetylase family
  JOURNAL   Mol Syst Biol 9, 672 (2013)
   PUBMED   23752268
REFERENCE   8  (residues 1 to 221)
  AUTHORS   Smith,K.T., Sardiu,M.E., Martin-Brown,S.A., Seidel,C.,
            Mushegian,A., Egidy,R., Florens,L., Washburn,M.P. and Workman,J.L.
  TITLE     Human family with sequence similarity 60 member A (FAM60A) protein:
            a new subunit of the Sin3 deacetylase complex
  JOURNAL   Mol Cell Proteomics 11 (12), 1815-1828 (2012)
   PUBMED   22984288
  REMARK    GeneRIF: studies reveal that loss of FAM60A or another component of
            the Sin3 complex, SDS3, leads to a change in cell morphology and an
            increase in cell migration
REFERENCE   9  (residues 1 to 221)
  AUTHORS   Munoz,I.M., MacArtney,T., Sanchez-Pulido,L., Ponting,C.P., Rocha,S.
            and Rouse,J.
  TITLE     Family with sequence similarity 60A (FAM60A) protein is a cell
            cycle-fluctuating regulator of the SIN3-HDAC1 histone deacetylase
            complex
  JOURNAL   J Biol Chem 287 (39), 32346-32353 (2012)
   PUBMED   22865885
  REMARK    GeneRIF: Family with sequence similarity 60A (FAM60A) protein is a
            cell cycle-fluctuating regulator of the SIN3-HDAC1 histone
            deacetylase complex.
REFERENCE   10 (residues 1 to 221)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC000024.2, DR763430.1 and BC004462.1.
            
            Transcript Variant: This variant (2) uses a different splice site
            in the 5' UTR, compared to variant 1. Variants 1, 2, and 3 encode
            the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL157432.1, SRR14038197.321701.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p11.21"
     Protein         1..221
                     /product="SIN3-HDAC complex-associated factor"
                     /note="tera protein homolog; protein FAM60A; family with
                     sequence similarity 60 member A"
                     /calculated_mol_wt=24721
     Region          2..198
                     /region_name="FAM60A"
                     /note="Protein Family FAM60A; pfam15396"
                     /db_xref="CDD:464703"
     Region          112..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP50.1)"
     Region          201..221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP50.1)"
     CDS             1..221
                     /gene="SINHCAF"
                     /gene_synonym="C12orf14; FAM60A; L4; TERA"
                     /coded_by="NM_021238.3:286..951"
                     /db_xref="CCDS:CCDS8723.1"
                     /db_xref="GeneID:58516"
                     /db_xref="HGNC:HGNC:30702"
                     /db_xref="MIM:615027"
ORIGIN      
        1 mfgfhkpkmy rsiegccicr akssssrftd skryekdfqs cfglhetrsg dicnacvllv
       61 krwkklpags kknwnhvvda ragpslkttl kpkkvktlsg nriksnqisk lqkefkrhns
      121 dahsttssas paqspcysnq sddgsdtema sgsnrtpvfs fldltywkrq kiccgiiykg
      181 rfgevlidth lfkpccsnkk aaaekpeeqg peplpistqe w
//
LOCUS       NP_001073879             875 aa            linear   PRI 21-NOV-2025
DEFINITION  F-box only protein 41 [Homo sapiens].
ACCESSION   NP_001073879 XP_001133175 XP_006712013
VERSION     NP_001073879.2
DBSOURCE    REFSEQ: accession NM_001080410.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 875)
  AUTHORS   Agrawal,Y., Sharma,T., Islam,S., Nadkarni,K.S. and Santra,M.K.
  TITLE     F-box protein FBXO41 suppresses breast cancer growth by inducing
            autophagic cell death through facilitating proteasomal degradation
            of oncogene SKP2
  JOURNAL   Int J Biochem Cell Biol 147, 106228 (2022)
   PUBMED   35598880
  REMARK    GeneRIF: F-box protein FBXO41 suppresses breast cancer growth by
            inducing autophagic cell death through facilitating proteasomal
            degradation of oncogene SKP2.
REFERENCE   2  (residues 1 to 875)
  AUTHORS   Agrawal,Y., Nadkarni,K.S., Gupta,N.A., Manne,R.K. and Santra,M.K.
  TITLE     F-box protein FBXO41 plays vital role in arsenic trioxide-mediated
            autophagic death of cancer cells
  JOURNAL   Toxicol Appl Pharmacol 441, 115973 (2022)
   PUBMED   35278439
  REMARK    GeneRIF: F-box protein FBXO41 plays vital role in arsenic
            trioxide-mediated autophagic death of cancer cells.
REFERENCE   3  (residues 1 to 875)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 875)
  AUTHORS   Mukherjee,C., Holubowska,A., Schwedhelm-Domeyer,N., Mitkovski,M.,
            Lee,S.J., Kannan,M., Matz,A., Vadhvani,M. and Stegmuller,J.
  TITLE     Loss of the neuron-specific F-box protein FBXO41 models an
            ataxia-like phenotype in mice with neuronal migration defects and
            degeneration in the cerebellum
  JOURNAL   J Neurosci 35 (23), 8701-8717 (2015)
   PUBMED   26063905
  REMARK    GeneRIF: This study show that FBXO41 is a critical factor, not only
            for neuronal migration in the cerebellum, but also for its
            long-term integrity.
REFERENCE   5  (residues 1 to 875)
  AUTHORS   Liang,H., Song,Z., Lei,J., Tang,J., Xu,H., Deng,X., Qi,Y., Zheng,W.
            and Deng,H.
  TITLE     Genetic analysis of the F-box only protein 41 gene in Chinese Han
            patients with Parkinson's disease
  JOURNAL   Parkinsonism Relat Disord 19 (10), 918-920 (2013)
   PUBMED   23777664
  REMARK    GeneRIF: Our finding suggests that the FBXO41gene may be a non-X
            chromosome-related Parkinson disease risk factor
REFERENCE   6  (residues 1 to 875)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   7  (residues 1 to 875)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   8  (residues 1 to 875)
  AUTHORS   Watanabe,N., Arai,H., Nishihara,Y., Taniguchi,M., Watanabe,N.,
            Hunter,T. and Osada,H.
  TITLE     M-phase kinases induce phospho-dependent ubiquitination of somatic
            Wee1 by SCFbeta-TrCP
  JOURNAL   Proc Natl Acad Sci U S A 101 (13), 4419-4424 (2004)
   PUBMED   15070733
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010913.9.
            
            On or before Jul 11, 2019 this sequence version replaced
            XP_006712013.1, NP_001073879.1.
            
            Summary: This gene encodes a member of the F-box protein family,
            which is characterized by an approximately 40 amino acid motif, the
            F-box. F-box proteins constitute one of the four subunits of the
            SCF ubiquitin protein ligase complex that plays a role in
            phosphorylation-dependent ubiquitination. F-box proteins are
            divided into three classes depending on the interaction substrate
            domain each contains in addition to the F-box motif: FBXW proteins
            contain WD-40 domains, FBXL proteins contain leucine-rich repeats,
            and FBXO proteins contain either different protein-protein
            interaction modules or no recognizable motifs. The protein encoded
            by this gene belongs to the FBXO class. [provided by RefSeq, Feb
            2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: AB075820.1, SRR14038193.2905745.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.2"
     Protein         1..875
                     /product="F-box only protein 41"
                     /calculated_mol_wt=94366
     Region          85..110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF61.5)"
     Region          165..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF61.5)"
     Region          <202..>344
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          211..491
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          347..542
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF61.5)"
     Site            360
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6NS60; propagated from
                     UniProtKB/Swiss-Prot (Q8TF61.5)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NS60; propagated from
                     UniProtKB/Swiss-Prot (Q8TF61.5)"
     Site            479
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6NS60; propagated from
                     UniProtKB/Swiss-Prot (Q8TF61.5)"
     Region          547..593
                     /region_name="F-box_FBXO41"
                     /note="F-box domain found in F-box only protein 41
                     (FBXO41) and similar proteins; cd22109"
                     /db_xref="CDD:438881"
     Site            order(551,556,559..560,563..564,568,570..571,575..577,579)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438881"
     Region          659..685
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          686..712
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          713..744
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          745..769
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Site            762
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NS60; propagated from
                     UniProtKB/Swiss-Prot (Q8TF61.5)"
     Region          770..796
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          797..821
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..875
                     /gene="FBXO41"
                     /gene_synonym="FBX41"
                     /coded_by="NM_001080410.4:1010..3637"
                     /db_xref="CCDS:CCDS46337.2"
                     /db_xref="GeneID:150726"
                     /db_xref="HGNC:HGNC:29409"
                     /db_xref="MIM:609108"
ORIGIN      
        1 masldlpyrc prcgehkrfr slsslrahle yshtyetlyi lsktnsicdg aaaaaaaaaa
       61 asgfplapep aallavpgar revfestsfq gkeqaagpsp aaphllhhhh hhaplahfpg
      121 dlvpaslpce elaepglvpa aaaryalrei eiplgelfar ksvassacst pppgpgpgpc
      181 pgpasaspas pspadvayee glarlkiral eklevdrrle rlseeveqki agqvgrlqae
      241 lerkaaelet arqesarlgr ekeeleeras elsrqvdvsv ellaslkqdl vhkeqelsrk
      301 qqevvqidqf lketaareas aklrlqqfie elleradrae rqlqvisssc gstpsaslgr
      361 ggggggagpn argpgrmreh hvgpavpnty avsrhgssps tgassrvpaa sqssgcydsd
      421 slelprpeeg apedsgpggl gtraqaangg sersqpprss glrrqaiqnw qrrprrhste
      481 geegdvsdvg srtteseaeg pldaprpgpa magplsscrl sarpeggsgr grraervsps
      541 rsnevispei lkmraalfci ftyldtrtll haaevcrdwr fvarhpavwt rvllenarvc
      601 skflamlaqw ctqahsltlq nlkprqrgkk eskeeyarst rgcleagles llkaaggnll
      661 ilrishcpni ltdrslwlas cycralqavt yrsatdpvgh eviwalgagc reivslqvap
      721 lhpcqqptrf snrclqmigr cwphlralgv ggagcgvqgl aslarncmrl qvleldhvse
      781 itqevaaevc reglkgleml vltatpvtpk allhfnsicr nlksivvqig iadyfkepss
      841 peaqklfedm vtklqalrrr pgfskilhik veggc
//
LOCUS       NP_001334960             420 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 1 isoform o [Homo sapiens].
ACCESSION   NP_001334960
VERSION     NP_001334960.1
DBSOURCE    REFSEQ: accession NM_001348031.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Petersen,M. and Dubielecka,P.
  TITLE     Adaptor protein Abelson interactor 1 in homeostasis and disease
  JOURNAL   Cell Commun Signal 22 (1), 468 (2024)
   PUBMED   39354505
  REMARK    GeneRIF: Adaptor protein Abelson interactor 1 in homeostasis and
            disease.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Jin,M., Xie,M., Liu,Y., Song,H., Zhang,M., Li,W., Li,X., Jia,N.,
            Dong,L., Lu,Q., Xue,F., Yan,L. and Yu,Q.
  TITLE     Circulating miR-30e-3p induces disruption of neurite development in
            SH-SY5Y cells by targeting ABI1, a novel biomarker for
            schizophrenia
  JOURNAL   J Psychiatr Res 174, 84-93 (2024)
   PUBMED   38626565
  REMARK    GeneRIF: Circulating miR-30e-3p induces disruption of neurite
            development in SH-SY5Y cells by targeting ABI1, a novel biomarker
            for schizophrenia.
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Lin,T., Guo,J., Peng,Y., Li,M., Liu,Y., Yu,X., Wu,N. and Yu,W.
  TITLE     Pan-cancer transcriptomic data of ABI1 transcript variants and
            molecular constitutive elements identifies novel cancer metastatic
            and prognostic biomarkers
  JOURNAL   Cancer Biomark 39 (1), 49-62 (2024)
   PUBMED   37545215
  REMARK    GeneRIF: Pan-cancer transcriptomic data of ABI1 transcript variants
            and molecular constitutive elements identifies novel cancer
            metastatic and prognostic biomarkers.
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Fan,P.D. and Goff,S.P.
  TITLE     Abl interactor 1 binds to sos and inhibits epidermal growth factor-
            and v-Abl-induced activation of extracellular signal-regulated
            kinases
  JOURNAL   Mol Cell Biol 20 (20), 7591-7601 (2000)
   PUBMED   11003655
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   7  (residues 1 to 420)
  AUTHORS   Scita,G., Nordstrom,J., Carbone,R., Tenca,P., Giardina,G.,
            Gutkind,S., Bjarnegard,M., Betsholtz,C. and Di Fiore,P.P.
  TITLE     EPS8 and E3B1 transduce signals from Ras to Rac
  JOURNAL   Nature 401 (6750), 290-293 (1999)
   PUBMED   10499589
REFERENCE   8  (residues 1 to 420)
  AUTHORS   Taki,T., Shibuya,N., Taniwaki,M., Hanada,R., Morishita,K.,
            Bessho,F., Yanagisawa,M. and Hayashi,Y.
  TITLE     ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL
            gene in acute myeloid leukemia with t(10;11)(p11.2;q23)
  JOURNAL   Blood 92 (4), 1125-1130 (1998)
   PUBMED   9694699
REFERENCE   9  (residues 1 to 420)
  AUTHORS   Ziemnicka-Kotula,D., Xu,J., Gu,H., Potempska,A., Kim,K.S.,
            Jenkins,E.C., Trenkner,E. and Kotula,L.
  TITLE     Identification of a candidate human spectrin Src homology 3
            domain-binding protein suggests a general mechanism of association
            of tyrosine kinases with the spectrin-based membrane skeleton
  JOURNAL   J Biol Chem 273 (22), 13681-13692 (1998)
   PUBMED   9593709
REFERENCE   10 (residues 1 to 420)
  AUTHORS   Biesova,Z., Piccoli,C. and Wong,W.T.
  TITLE     Isolation and characterization of e3B1, an eps8 binding protein
            that regulates cell growth
  JOURNAL   Oncogene 14 (2), 233-241 (1997)
   PUBMED   9010225
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139404.9 and AL390961.17.
            
            Summary: This gene encodes a member of the Abelson-interactor
            family of adaptor proteins. These proteins facilitate signal
            transduction as components of several multiprotein complexes, and
            regulate actin polymerization and cytoskeletal remodeling through
            interactions with Abelson tyrosine kinases. The encoded protein
            plays a role in macropinocytosis as a component of the WAVE2
            complex, and also forms a complex with EPS8 and SOS1 that mediates
            signal transduction from Ras to Rac. This gene may play a role in
            the progression of several malignancies including melanoma, colon
            cancer and breast cancer, and a t(10;11) chromosomal translocation
            involving this gene and the MLL gene has been associated with acute
            myeloid leukemia. Alternatively spliced transcript variants
            encoding multiple isoforms have been observed for this gene, and a
            pseudogene of this gene is located on the long arm of chromosome
            14. [provided by RefSeq, Sep 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.18534.1,
                                           SRR1660807.96491.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.1"
     Protein         1..420
                     /product="abl interactor 1 isoform o"
                     /note="nap1 binding protein; interactor protein AblBP4;
                     Abl-interactor protein 1 long; Abelson interactor 1;
                     abl-binding protein 4; eps8 SH3 domain-binding protein;
                     spectrin SH3 domain-binding protein 1"
                     /calculated_mol_wt=45777
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.13,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Region          18..79
                     /region_name="Required for binding to WASF1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZM5; propagated from
                     UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Region          93..156
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Site            95..96
                     /site_type="other"
                     /note="Breakpoint for translocation to form
                     KMT2A/MLL1-ABI1; propagated from UniProtKB/Swiss-Prot
                     (Q8IZP0.4)"
     Region          159..290
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1.
                     /evidence=ECO:0000269|PubMed:18328268,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8CBW3; propagated from
                     UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IZP0.4)"
     Region          362..420
                     /region_name="SH3_Abi1"
                     /note="Src homology 3 domain of Abl Interactor 1; cd11971"
                     /db_xref="CDD:212904"
     Site            order(367,369,372,376,394..395,408,410..411)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212904"
     CDS             1..420
                     /gene="ABI1"
                     /gene_synonym="ABI-1; ABLBP4; E3B1; NAP1BP; SSH3BP;
                     SSH3BP1"
                     /coded_by="NM_001348031.2:96..1358"
                     /note="isoform o is encoded by transcript variant 15"
                     /db_xref="GeneID:10006"
                     /db_xref="HGNC:HGNC:11320"
                     /db_xref="MIM:603050"
ORIGIN      
        1 maelqmllee eipsgkrali esyqnltrva dycennyiqa tdkrkaleet kayttqslas
       61 vayqinalan nvlqlldiqa sqlrrmessi nhisqtvdih kekvarreig ilttnkntsr
      121 thkiiapanm erpvryirkp idytvlddvg hgvkwlkakh gnnqpartgt lsrtnpptqk
      181 ppsppmsgrg tlgrntpykt lepvkpptvp ndymtsparl gsqhspgrta slnqrprths
      241 gssggsgsre nsgsssigip iavptpsppt igpenisvpp psgappappl apllpvstvi
      301 vadsptpppp pppddipmfd dspppppppp vdyedeeaav vqyndpyadg dpawapknyi
      361 ekvvaiydyt kdkddelsfm egaiiyvikk nddgwyegvc nrvtglfpgn yvesimhytd
//
LOCUS       NP_001387276             328 aa            linear   PRI 21-NOV-2025
DEFINITION  single-stranded DNA-binding protein 2 isoform 10 [Homo sapiens].
ACCESSION   NP_001387276
VERSION     NP_001387276.1
DBSOURCE    REFSEQ: accession NM_001400347.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Schwab,C., Roberts,K., Boer,J.M., Gohring,G., Steinemann,D.,
            Vora,A., Macartney,C., Hough,R., Thorn,Z., Dillon,R., Escherich,G.,
            Cazzaniga,G., Schlegelberger,B., Loh,M., den Boer,M.L.,
            Moorman,A.V. and Harrison,C.J.
  TITLE     SSBP2-CSF1R is a recurrent fusion in B-lineage acute lymphoblastic
            leukemia with diverse genetic presentation and variable outcome
  JOURNAL   Blood 137 (13), 1835-1838 (2021)
   PUBMED   33197935
  REMARK    GeneRIF: SSBP2-CSF1R is a recurrent fusion in B-lineage acute
            lymphoblastic leukemia with diverse genetic presentation and
            variable outcome.
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Wang,H., Kim,J., Wang,Z., Yan,X.X., Dean,A. and Xu,W.
  TITLE     Crystal structure of human LDB1 in complex with SSBP2
  JOURNAL   Proc Natl Acad Sci U S A 117 (2), 1042-1048 (2020)
   PUBMED   31892537
  REMARK    GeneRIF: Single-stranded DNA binding proteins (SSBPs) interact
            specifically with the LDB/Chip conserved domain (LCCD) of LDB
            proteins and stabilize LDBs by preventing their proteasomal
            degradation, thus promoting their functions in gene regulation.
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Kim,H., Kim,Y., Bang,S., Park,S., Jee,S., Sim,J., Shin,S.J.,
            Paik,S.S. and Jang,K.
  TITLE     Low Expression of Single-stranded DNA Binding Protein 2 (SSBP2)
            Predicts Unfavourable Postoperative Outcomes in Patients With Clear
            Cell Renal Cell Carcinoma
  JOURNAL   In Vivo 34 (1), 101-107 (2020)
   PUBMED   31882468
  REMARK    GeneRIF: CcRCC with low SSBP2 expression was associated with
            adverse clinicopathological characteristics and poor patient
            outcomes.
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Fleisig,H.B., Orazio,N.I., Liang,H., Tyler,A.F., Adams,H.P.,
            Weitzman,M.D. and Nagarajan,L.
  TITLE     Adenoviral E1B55K oncoprotein sequesters candidate leukemia
            suppressor sequence-specific single-stranded DNA-binding protein 2
            into aggresomes
  JOURNAL   Oncogene 26 (33), 4797-4805 (2007)
   PUBMED   17311003
  REMARK    GeneRIF: Results suggest that subverting SSBP2 function by
            oncoprotein E1B55K may contribute to cell transformation by viral
            oncoproteins.
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Liang,H., Samanta,S. and Nagarajan,L.
  TITLE     SSBP2, a candidate tumor suppressor gene, induces growth arrest and
            differentiation of myeloid leukemia cells
  JOURNAL   Oncogene 24 (16), 2625-2634 (2005)
   PUBMED   15782145
  REMARK    GeneRIF: Our findings are consistent with human SSBP2 being a novel
            regulator of hematopoietic growth and differentiation, whose loss
            confers a block in differentiation advantage to myeloid leukemic
            cells.
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Castro,P., Liang,H., Liang,J.C. and Nagarajan,L.
  TITLE     A novel, evolutionarily conserved gene family with putative
            sequence-specific single-stranded DNA-binding activity
  JOURNAL   Genomics 80 (1), 78-85 (2002)
   PUBMED   12079286
  REMARK    GeneRIF: Member of a closely related, evolutionarily conserved, and
            ubiquitously expressed gene family, potential tumor suppressor
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016562.7, AC093250.3,
            AC026419.5 and AC010623.10.
            
            Summary: This gene encodes a subunit of a protein complex that
            interacts with single-stranded DNA and is involved in the DNA
            damage response and maintenance of genome stability. The encoded
            protein may also play a role in telomere repair. A variant of this
            gene may be associated with survival in human glioblastoma
            patients. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.241584.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.1"
     Protein         1..328
                     /product="single-stranded DNA-binding protein 2 isoform
                     10"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein 2"
                     /calculated_mol_wt=34175
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CYZ8; propagated from
                     UniProtKB/Swiss-Prot (P81877.2)"
     Region          19..45
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          83..327
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     Region          147..171
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P81877.2)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P81877.2)"
     CDS             1..328
                     /gene="SSBP2"
                     /gene_synonym="HSPC116; SOSS-B2"
                     /coded_by="NM_001400347.1:56..1042"
                     /note="isoform 10 is encoded by transcript variant 18"
                     /db_xref="GeneID:23635"
                     /db_xref="HGNC:HGNC:15831"
                     /db_xref="MIM:607389"
ORIGIN      
        1 mygkgksnss avpsdsqare klalyvyeyl lhvgaqksaq tflseirwek nitlgeppgf
       61 lhswwcvfwd lycaaperre tcehsseaka fhdysaaaap spvlgnippg dgmpvgpvpp
      121 gffqpfmspr ypggprpplr ipnqalggvp gsqpllpsgm dptrqqghpn mggpmqrmtp
      181 prgmvplgpq nyggamrppl nalggpgmpg mnmgpgggrp wpnptnansi pyssaspgny
      241 vgppggggpp gtpimpspad stnsgdnmyt lmnavppgpn rpnfpmgpgs dgpmgglggm
      301 eshhmngslg sgdmdsisky spsmtmsv
//
LOCUS       NP_001188357             384 aa            linear   PRI 21-NOV-2025
DEFINITION  Golgi reassembly-stacking protein 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001188357
VERSION     NP_001188357.1
DBSOURCE    REFSEQ: accession NM_001201428.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Yang,F., Chen,L., Wen,B., Wang,X., Wang,L., Ji,K. and Liu,H.
  TITLE     Golgi Reassembly Stacking Protein 2 Modulates Myometrial
            Contractility during Labor by Affecting ATP Production
  JOURNAL   Int J Mol Sci 24 (12), 10116 (2023)
   PUBMED   37373263
  REMARK    GeneRIF: Golgi Reassembly Stacking Protein 2 Modulates Myometrial
            Contractility during Labor by Affecting ATP Production.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Ahat,E., Song,Y., Xia,K., Reid,W., Li,J., Bui,S., Zhang,F.,
            Linhardt,R.J. and Wang,Y.
  TITLE     GRASP depletion-mediated Golgi fragmentation impairs
            glycosaminoglycan synthesis, sulfation, and secretion
  JOURNAL   Cell Mol Life Sci 79 (4), 199 (2022)
   PUBMED   35312866
  REMARK    GeneRIF: GRASP depletion-mediated Golgi fragmentation impairs
            glycosaminoglycan synthesis, sulfation, and secretion.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Duran,J.M., Kinseth,M., Bossard,C., Rose,D.W., Polishchuk,R.,
            Wu,C.C., Yates,J., Zimmerman,T. and Malhotra,V.
  TITLE     The role of GRASP55 in Golgi fragmentation and entry of cells into
            mitosis
  JOURNAL   Mol Biol Cell 19 (6), 2579-2587 (2008)
   PUBMED   18385516
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Lane,J.D., Lucocq,J., Pryde,J., Barr,F.A., Woodman,P.G., Allan,V.J.
            and Lowe,M.
  TITLE     Caspase-mediated cleavage of the stacking protein GRASP65 is
            required for Golgi fragmentation during apoptosis
  JOURNAL   J Cell Biol 156 (3), 495-509 (2002)
   PUBMED   11815631
  REMARK    GeneRIF: GRASP65 is an important structural component required for
            maintenance of Golgi apparatus integrity
REFERENCE   8  (residues 1 to 384)
  AUTHORS   Short,B., Preisinger,C., Korner,R., Kopajtich,R., Byron,O. and
            Barr,F.A.
  TITLE     A GRASP55-rab2 effector complex linking Golgi structure to membrane
            traffic
  JOURNAL   J Cell Biol 155 (6), 877-883 (2001)
   PUBMED   11739401
  REMARK    GeneRIF: GRASP55 forms an effector complex for the small GTPase
            rab2, together with a conserved coiled-coil protein golgin-45
            (JEM-1).
REFERENCE   9  (residues 1 to 384)
  AUTHORS   Jesch,S.A., Lewis,T.S., Ahn,N.G. and Linstedt,A.D.
  TITLE     Mitotic phosphorylation of Golgi reassembly stacking protein 55 by
            mitogen-activated protein kinase ERK2
  JOURNAL   Mol Biol Cell 12 (6), 1811-1817 (2001)
   PUBMED   11408587
REFERENCE   10 (residues 1 to 384)
  AUTHORS   Kuo,A., Zhong,C., Lane,W.S. and Derynck,R.
  TITLE     Transmembrane transforming growth factor-alpha tethers to the PDZ
            domain-containing, Golgi membrane-associated protein p59/GRASP55
  JOURNAL   EMBO J 19 (23), 6427-6439 (2000)
   PUBMED   11101516
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL117430.1, AC010092.4 and
            BQ004408.1.
            
            Summary: This gene encodes a member of the Golgi reassembly
            stacking protein family. These proteins may play a role in the
            stacking of Golgi cisternae and Golgi ribbon formation, as well as
            Golgi fragmentation during apoptosis or mitosis. The encoded
            protein also plays a role in the intracellular transport of
            transforming growth factor alpha and may function as a molecular
            chaperone. A pseudogene of this gene is located on the short arm of
            chromosome 2. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Jan 2011].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream start codon, compared to variant 1. The resulting
            isoform (2) has a shorter N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.152945.1, AL117430.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..384
                     /product="Golgi reassembly-stacking protein 2 isoform 2"
                     /note="golgi phosphoprotein 6; golgi reassembly stacking
                     protein 2, 55kDa; Golgi reassembly-stacking protein 2"
                     /calculated_mol_wt=39637
     Region          1..136
                     /region_name="GRASP55_65"
                     /note="GRASP55/65 PDZ-like domain; pfam04495"
                     /db_xref="CDD:427981"
     Region          <173..329
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..384
                     /gene="GORASP2"
                     /gene_synonym="GOLPH6; GRASP55; GRS2; p59"
                     /coded_by="NM_001201428.2:226..1380"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:26003"
                     /db_xref="HGNC:HGNC:17500"
                     /db_xref="MIM:608693"
ORIGIN      
        1 mliyssktle lretsvtpsn lwggqgllgv sirfcsfdga nenvwhvlev esnspaalag
       61 lrphsdyiig adtvmnesed lfsliethea kplklyvynt dtdncrevii tpnsawggeg
      121 slgcgigygy lhriptrpfe egkkislpgq magtpitplk dgftevqlss vnppslsppg
      181 ttgieqsltg lsisstppav ssvlstgvpt vpllppqvnq sltsvppmnp attlpglmpl
      241 paglpnlpnl nlnlpaphim pgvglpelvn pglpplpsmp prnlpgiapl plpseflpsf
      301 plvpesssaa ssgellsslp ptsnapsdpa tttakadaas sltvdvtppt akapttvedr
      361 vgdstpvsek pvsaavdana sesp
//
LOCUS       NP_001180512            1192 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal cell adhesion molecule isoform E precursor [Homo sapiens].
ACCESSION   NP_001180512
VERSION     NP_001180512.1
DBSOURCE    REFSEQ: accession NM_001193583.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1192)
  AUTHORS   Wang,C., Wang,Z., Fu,L., Du,J., Ji,F. and Qiu,X.
  TITLE     CircNRCAM up-regulates NRCAM to promote papillary thyroid carcinoma
            progression
  JOURNAL   J Endocrinol Invest 47 (5), 1215-1226 (2024)
   PUBMED   38485895
  REMARK    GeneRIF: CircNRCAM up-regulates NRCAM to promote papillary thyroid
            carcinoma progression.
REFERENCE   2  (residues 1 to 1192)
  AUTHORS   Zhou,L., He,L., Liu,C.H., Qiu,H., Zheng,L., Sample,K.M., Wu,Q.,
            Li,J., Xie,K., Ampuero,J., Li,Z., Lv,D., Liu,M., Romero-Gomez,M.,
            Hu,Y. and Tang,H.
  TITLE     Liver cancer stem cell dissemination and metastasis: uncovering the
            role of NRCAM in hepatocellular carcinoma
  JOURNAL   J Exp Clin Cancer Res 42 (1), 311 (2023)
   PUBMED   37993901
  REMARK    GeneRIF: Liver cancer stem cell dissemination and metastasis:
            uncovering the role of NRCAM in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1192)
  AUTHORS   Sannes,A.C., Christensen,J.O., Nielsen,M.B. and Gjerstad,J.
  TITLE     Stress-induced headache in the general working population is
            moderated by the NRCAM rs2300043 genotype
  JOURNAL   Scand J Pain 23 (2), 326-332 (2022)
   PUBMED   36181733
  REMARK    GeneRIF: Stress-induced headache in the general working population
            is moderated by the NRCAM rs2300043 genotype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1192)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 1192)
  AUTHORS   Bai,C. and Chen,D.G.
  TITLE     NRCAM acts as a prognostic biomarker and promotes the tumor
            progression in gastric cancer via EMT pathway
  JOURNAL   Tissue Cell 77, 101859 (2022)
   PUBMED   35763884
  REMARK    GeneRIF: NRCAM acts as a prognostic biomarker and promotes the
            tumor progression in gastric cancer via EMT pathway.
REFERENCE   6  (residues 1 to 1192)
  AUTHORS   Wang,B., Williams,H., Du,J.S., Terrett,J. and Kenwrick,S.
  TITLE     Alternative splicing of human NrCAM in neural and nonneural tissues
  JOURNAL   Mol Cell Neurosci 10 (5-6), 287-295 (1998)
   PUBMED   9604207
REFERENCE   7  (residues 1 to 1192)
  AUTHORS   Grumet,M.
  TITLE     Nr-CAM: a cell adhesion molecule with ligand and receptor functions
  JOURNAL   Cell Tissue Res 290 (2), 423-428 (1997)
   PUBMED   9321706
  REMARK    Review article
REFERENCE   8  (residues 1 to 1192)
  AUTHORS   Sakurai,T., Lustig,M., Nativ,M., Hemperly,J.J., Schlessinger,J.,
            Peles,E. and Grumet,M.
  TITLE     Induction of neurite outgrowth through contactin and Nr-CAM by
            extracellular regions of glial receptor tyrosine phosphatase beta
  JOURNAL   J Cell Biol 136 (4), 907-918 (1997)
   PUBMED   9049255
REFERENCE   9  (residues 1 to 1192)
  AUTHORS   Volkmer,H., Leuschner,R., Zacharias,U. and Rathjen,F.G.
  TITLE     Neurofascin induces neurites by heterophilic interactions with
            axonal NrCAM while NrCAM requires F11 on the axonal surface to
            extend neurites
  JOURNAL   J Cell Biol 135 (4), 1059-1069 (1996)
   PUBMED   8922386
REFERENCE   10 (residues 1 to 1192)
  AUTHORS   Lane,R.P., Chen,X.N., Yamakawa,K., Vielmetter,J., Korenberg,J.R.
            and Dreyer,W.J.
  TITLE     Characterization of a highly conserved human homolog to the chicken
            neural cell surface protein Bravo/Nr-CAM that maps to chromosome
            band 7q31
  JOURNAL   Genomics 35 (3), 456-465 (1996)
   PUBMED   8812479
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005058.1, DA292156.1,
            BX538010.1, BC115736.1, AK127035.1 and BU735065.1.
            
            Summary: Cell adhesion molecules (CAMs) are members of the
            immunoglobulin superfamily. This gene encodes a neuronal cell
            adhesion molecule with multiple immunoglobulin-like C2-type domains
            and fibronectin type-III domains. This ankyrin-binding protein is
            involved in neuron-neuron adhesion and promotes directional
            signaling during axonal cone growth. This gene is also expressed in
            non-neural tissues and may play a general role in cell-cell
            communication via signaling from its intracellular domain to the
            actin cytoskeleton during directional cell migration. Allelic
            variants of this gene have been associated with autism and
            addiction vulnerability. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (5) differs in the 5' UTR and
            lacks three in-frame exons in the coding region, compared to
            variant 1. The encoded protein (isoform E) is shorter than isoform
            A. Variants 5 and 15-22 all encode the same isoform (E).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC115736.1, SRR1803614.6935.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1192
                     /product="neuronal cell adhesion molecule isoform E
                     precursor"
                     /note="NgCAM-related cell adhesion molecule; neuronal
                     surface protein Bravo"
                     /calculated_mol_wt=128448
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3315
     Region          46..140
                     /region_name="IgI_NrCAM"
                     /note="Immunoglobulin (Ig)-like domain of NrCAM (Ng
                     (neuronglia) CAM-related cell adhesion molecule); member
                     of the I-set of Ig superfamily (IgSF) domains; cd05874"
                     /db_xref="CDD:409458"
     Region          46..50
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409458"
     Region          55..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409458"
     Region          64..71
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409458"
     Region          77..82
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409458"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          85..87
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409458"
     Region          94..97
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409458"
     Region          102..106
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409458"
     Region          119..127
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409458"
     Region          130..140
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409458"
     Region          149..238
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          163..167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          177..181
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          200..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          215..220
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          231..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            257
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          258..339
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          269..273
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          282..286
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            295
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          304..308
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          318..323
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          331..334
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          343..431
                     /region_name="Ig4_NrCAM"
                     /note="Fourth immunoglobulin (Ig)-like domain of NrCAM
                     (NgCAM-related cell adhesion molecule); cd05868"
                     /db_xref="CDD:409454"
     Region          359..363
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409454"
     Region          372..376
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409454"
     Region          396..400
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409454"
     Region          410..415
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409454"
     Site            414
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          423..426
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409454"
     Region          440..523
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          453..457
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          466..470
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            488
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          489..493
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          503..508
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          516..519
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          527..1041
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            600
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          628..718
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(628,694,709)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            697
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            order(710..711,713..714)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            783
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            839
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            974
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            990
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1000
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          1079..1168
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     CDS             1..1192
                     /gene="NRCAM"
                     /gene_synonym="NEDNMS"
                     /coded_by="NM_001193583.2:526..4104"
                     /note="isoform E precursor is encoded by transcript
                     variant 5"
                     /db_xref="CCDS:CCDS55153.1"
                     /db_xref="GeneID:4897"
                     /db_xref="HGNC:HGNC:7994"
                     /db_xref="MIM:601581"
ORIGIN      
        1 mqlkimpkkk rlsagrvpli lflcqmisal evpldpklle dlvqpptitq qspkdyiidp
       61 reniviqcea kgkpppsfsw trngthfdid kdplvtmkpg tgtliinims egkaetyegv
      121 yqctarnerg aavsnnivvr psrsplwtke klepitlqsg qslvlpcrpp iglpppiifw
      181 mdnsfqrlpq servsqglng dlyfsnvlpe dtredyicya rfnhtqtiqq kqpisvkvis
      241 akssrerppt fltpegnasn keelrgnvls leciaeglpt piiywakedg mlpknrtvyk
      301 nfektlqiih vseadsgnyq ciaknalgai hhtisvrvka apywitapqn lvlspgedgt
      361 licrangnpk priswltngv pieiapddps rkidgdtiif snvqerssav yqcnasneyg
      421 yllanafvnv laeppriltp antlyqvian rpalldcaff gsplptiewf kgakgsalhe
      481 diyvlhengt leipvaqkds tgtytcvarn klgmaknevh leikdptwiv kqpeyavvqr
      541 gsmvsfeckv khdhtlsltv lwlkdnrelp sderftvdkd hlvvadvsdd dsgtytcvan
      601 ttldsvsasa vlsvvaptpt papvydvpnp pfdleltdql dksvqlswtp gddnnspitk
      661 fiieyedamh kpglwhhqte vsgtqttaql klspyvnysf rvmavnsigk slpseaseqy
      721 ltkasepdkn ptaveglgse pdnlvitwkp lngfesngpg lqykvswrqk dgddewtsvv
      781 vanvskyivs gtptfvpyli kvqalndmgf apepavvmgh sgedlpmvap gnvrvnvvns
      841 tlaevhwdpv plksirghlq gyriyywktq ssskrnrrhi ekkiltfqgs kthgmlpgle
      901 pfshytlnvr vvngkgegpa spdrvfntpe gvpsapsslk ivnptldslt lewdppshpn
      961 gilteytlky qpinsthelg plvdlkipan ktrwtlknln fstrykfyfy aqtsagsgsq
     1021 iteeavttvd eagilppdvg agkamasrqv diatqgwfig lmcavallil illivcfirr
     1081 nkggkypvke kedahadpei qpmkeddgtf geysdaedhk plkkgsrtps drtvkkedsd
     1141 dslvdygegv ngqfnedgsf igqysgkkek epaegnesse apspvnamns fv
//
LOCUS       NP_001336863             470 aa            linear   PRI 21-NOV-2025
DEFINITION  torsin-1A-interacting protein 2 isoform b [Homo sapiens].
ACCESSION   NP_001336863 XP_005244996
VERSION     NP_001336863.1
DBSOURCE    REFSEQ: accession NM_001349934.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Kafantari,E., Hernandez,V.J., Necpal,J., Leonidou,M., Baureder,R.,
            Hedberg-Oldfors,C., Jech,R., Zech,M., Schwartz,T.U. and
            Puschmann,A.
  TITLE     TOR1AIP2 as a candidate gene for dystonia-hemichorea/hemiballism
  JOURNAL   Parkinsonism Relat Disord 134, 107781 (2025)
   PUBMED   40088780
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Laudermilch,E., Tsai,P.L., Graham,M., Turner,E., Zhao,C. and
            Schlieker,C.
  TITLE     Dissecting Torsin/cofactor function at the nuclear envelope: a
            genetic study
  JOURNAL   Mol Biol Cell 27 (25), 3964-3971 (2016)
   PUBMED   27798237
REFERENCE   5  (residues 1 to 470)
  AUTHORS   Demircioglu,F.E., Sosa,B.A., Ingram,J., Ploegh,H.L. and
            Schwartz,T.U.
  TITLE     Structures of TorsinA and its disease-mutant complexed with an
            activator reveal the molecular basis for primary dystonia
  JOURNAL   Elife 5, e17983 (2016)
   PUBMED   27490483
  REMARK    GeneRIF: A comparison of these structures shows, in atomic detail,
            the subtle differences in TorsinADeltaE-LULL1 activator
            interactions that separate the healthy from the diseased state.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 470)
  AUTHORS   Rose,A.E., Brown,R.S. and Schlieker,C.
  TITLE     Torsins: not your typical AAA+ ATPases
  JOURNAL   Crit Rev Biochem Mol Biol 50 (6), 532-549 (2015)
   PUBMED   26592310
  REMARK    Review article
REFERENCE   7  (residues 1 to 470)
  AUTHORS   Rose,A.E., Zhao,C., Turner,E.M., Steyer,A.M. and Schlieker,C.
  TITLE     Arresting a Torsin ATPase reshapes the endoplasmic reticulum
  JOURNAL   J Biol Chem 289 (1), 552-564 (2014)
   PUBMED   24275647
REFERENCE   8  (residues 1 to 470)
  AUTHORS   Zhao,C., Brown,R.S., Chase,A.R., Eisele,M.R. and Schlieker,C.
  TITLE     Regulation of Torsin ATPases by LAP1 and LULL1
  JOURNAL   Proc Natl Acad Sci U S A 110 (17), E1545-E1554 (2013)
   PUBMED   23569223
  REMARK    GeneRIF: LAP1 and LULL1 as regulatory cofactors that are
            responsible for the activation of TorA's ATPase activity.
REFERENCE   9  (residues 1 to 470)
  AUTHORS   Vander Heyden,A.B., Naismith,T.V., Snapp,E.L., Hodzic,D. and
            Hanson,P.I.
  TITLE     LULL1 retargets TorsinA to the nuclear envelope revealing an
            activity that is impaired by the DYT1 dystonia mutation
  JOURNAL   Mol Biol Cell 20 (11), 2661-2672 (2009)
   PUBMED   19339278
  REMARK    GeneRIF: Data suggest that LULL1 regulates the distribution and
            activity of TorA within the ER and NE lumen and reveal functional
            defects in the mutant protein responsible for DYT1 dystonia.
REFERENCE   10 (residues 1 to 470)
  AUTHORS   Goodchild,R.E. and Dauer,W.T.
  TITLE     The AAA+ protein torsinA interacts with a conserved domain present
            in LAP1 and a novel ER protein
  JOURNAL   J Cell Biol 168 (6), 855-862 (2005)
   PUBMED   15767459
  REMARK    GeneRIF: identifed a novel transmembrane protein, lumenal domain
            like LAP1 (LULL1), which appears to interact with torsinA; it
            resides in the main endoplasmic reticulum.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359853.18.
            
            On Mar 30, 2017 this sequence version replaced XP_005244996.1.
            
            Summary: One of the two protein isoforms encoded by this gene is a
            type II integral membrane protein found in the endoplasmic
            reticulum (ER). The encoded protein is a cofactor for the ATPase
            TorsinA, regulating the amount of TorsinA present in the ER
            compared to that found in the nuclear envelope. Defects in this
            protein are a cause of early onset primary dystonia, a
            neuromuscular disease. The other isoform encoded by this gene is an
            interferon alpha responsive protein whose cellular role has yet to
            be determined. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (6), as well as variants 2, 3, and
            7-9, encodes isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1459024.1,
                                           SRR14038193.2591491.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..470
                     /product="torsin-1A-interacting protein 2 isoform b"
                     /note="interferon responsive gene 15; lumenal domain like
                     LAP1; 15 kDa interferon-responsive protein; torsin A
                     interacting protein 2"
                     /calculated_mol_wt=51132
     Region          1..222
                     /region_name="LAP1_N"
                     /note="Lamina-associated polypeptide 1, N-terminal;
                     pfam20443"
                     /db_xref="CDD:466592"
     Region          1..174
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFQ8.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8NFQ8.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8NFQ8.1)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NFQ8.1)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NFQ8.1)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8NFQ8.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NFQ8.1)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NFQ8.1)"
     Site            215..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFQ8.1)"
     Region          236..470
                     /region_name="Interaction with TOR1A.
                     /evidence=ECO:0000269|PubMed:23569223"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFQ8.1)"
     Region          237..469
                     /region_name="LAP1_C"
                     /note="Lamina-associated polypeptide 1, AAA+ activator
                     domain; pfam05609"
                     /db_xref="CDD:461691"
     Site            286
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFQ8.1)"
     CDS             1..470
                     /gene="TOR1AIP2"
                     /gene_synonym="IFRG15; LULL1; NET9"
                     /coded_by="NM_001349934.2:790..2202"
                     /note="isoform b is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS1334.1"
                     /db_xref="GeneID:163590"
                     /db_xref="HGNC:HGNC:24055"
                     /db_xref="MIM:614513"
ORIGIN      
        1 madsglrepq edsqkdlend psvnsqaqet tiiasnaeea eilhsacgls kdhqeveteg
       61 pesadtgdks espdeanvgk hpkdkteden kqsfldggkg hhlpsenlgk epldpdpshs
      121 psdkvgrada hlgsssvalp keasdgtgas qeppttdsqe aqspghssag qegedtlrrr
      181 llapeagshp qqtqkleeik enaqdtmrqi nkkgfwsygp vilvvlvvav vassvnsyys
      241 spaqqvpknp aleaflaqfs qledkfpgqs sflwqrgrkf lqkhlnasnp tepatiifta
      301 aregretlkc lshhvadayt ssqkvspiqi dgagrtwqds dtvkllvdle lsygfengqk
      361 aavvhhfesf pagstlifyk ycdhenaafk dvalvltvll eeetleasvg preteekvrd
      421 llwakftnsd tptsfnhmds dklsglwsri shlvlpvqpv ssieeqgclf
//
LOCUS       NP_001364428             304 aa            linear   PRI 21-NOV-2025
DEFINITION  non-homologous end-joining factor 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001364428
VERSION     NP_001364428.1
DBSOURCE    REFSEQ: accession NM_001377499.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Vu,D.D., Bonucci,A., Breniere,M., Cisneros-Aguirre,M.,
            Pelupessy,P., Wang,Z., Carlier,L., Bouvignies,G., Cortes,P.,
            Aggarwal,A.K., Blackledge,M., Gueroui,Z., Belle,V., Stark,J.M.,
            Modesti,M. and Ferrage,F.
  TITLE     Multivalent interactions of the disordered regions of XLF and XRCC4
            foster robust cellular NHEJ and drive the formation of
            ligation-boosting condensates in vitro
  JOURNAL   Nat Struct Mol Biol 31 (11), 1732-1744 (2024)
   PUBMED   38898102
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Seif-El-Dahan,M., Kefala-Stavridi,A., Frit,P., Hardwick,S.W.,
            Chirgadze,D.Y., Maia De Oliviera,T., Andreani,J., Britton,S.,
            Barboule,N., Bossaert,M., Pandurangan,A.P., Meek,K., Blundell,T.L.,
            Ropars,V., Calsou,P., Charbonnier,J.B. and Chaplin,A.K.
  TITLE     PAXX binding to the NHEJ machinery explains functional redundancy
            with XLF
  JOURNAL   Sci Adv 9 (22), eadg2834 (2023)
   PUBMED   37256950
  REMARK    GeneRIF: PAXX binding to the NHEJ machinery explains functional
            redundancy with XLF.
            Erratum:[Sci Adv. 2023 Sep 29;9(39):eadj8489. doi:
            10.1126/sciadv.adj8489. PMID: 37774037]
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Chaplin,A.K., Hardwick,S.W., Stavridi,A.K., Buehl,C.J., Goff,N.J.,
            Ropars,V., Liang,S., De Oliveira,T.M., Chirgadze,D.Y., Meek,K.,
            Charbonnier,J.B. and Blundell,T.L.
  TITLE     Cryo-EM of NHEJ supercomplexes provides insights into DNA repair
  JOURNAL   Mol Cell 81 (16), 3400-3409 (2021)
   PUBMED   34352203
  REMARK    GeneRIF: Cryo-EM of NHEJ supercomplexes provides insights into DNA
            repair.
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Andres,S.N., Modesti,M., Tsai,C.J., Chu,G. and Junop,M.S.
  TITLE     Crystal structure of human XLF: a twist in nonhomologous DNA
            end-joining
  JOURNAL   Mol Cell 28 (6), 1093-1101 (2007)
   PUBMED   18158905
  REMARK    GeneRIF: Mutational analysis of XLF and XRCC4 reveals a potential
            interaction interface, suggesting a mechanism for how XLF
            stimulates the ligation of mismatched ends.
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Tsai,C.J., Kim,S.A. and Chu,G.
  TITLE     Cernunnos/XLF promotes the ligation of mismatched and noncohesive
            DNA ends
  JOURNAL   Proc Natl Acad Sci U S A 104 (19), 7851-7856 (2007)
   PUBMED   17470781
  REMARK    GeneRIF: Cernunnos/XRCC4-like factor promotes a mismatched end
            (MEnd) DNA ligase activity to facilitate joining and to preserve
            DNA sequence.
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Revy,P. and de Villartay,J.P.
  TITLE     [Cernunnos, a novel DNA repair factor essential for the immune
            system]
  JOURNAL   Med Sci (Paris) 22 (6-7), 569-570 (2006)
   PUBMED   16828027
  REMARK    GeneRIF: DNA repair protein involved in lymphocyte activation and
            cell division.
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Callebaut,I., Malivert,L., Fischer,A., Mornon,J.P., Revy,P. and de
            Villartay,J.P.
  TITLE     Cernunnos interacts with the XRCC4 x DNA-ligase IV complex and is
            homologous to the yeast nonhomologous end-joining factor Nej1
  JOURNAL   J Biol Chem 281 (20), 13857-13860 (2006)
   PUBMED   16571728
  REMARK    GeneRIF: Cernunnos physically interacts with the XRCC4 x DNA-ligase
            IV complex
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Ahnesorg,P., Smith,P. and Jackson,S.P.
  TITLE     XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA
            nonhomologous end-joining
  JOURNAL   Cell 124 (2), 301-313 (2006)
   PUBMED   16439205
  REMARK    GeneRIF: Studies on the binding of XLF and its role in DNA repair.
            GeneRIF: The XLF-encoded protein (XRRC4 like factor, FLJ12610) is
            involved in DNA double-strand break repair via nonhomologous
            end-joining and associates with the Ligase IV-XRCC4 complex. XLF is
            mutated in a number of radiosensitive and immuno-deficient
            patients.
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Buck,D., Malivert,L., de Chasseval,R., Barraud,A., Fondaneche,M.C.,
            Sanal,O., Plebani,A., Stephan,J.L., Hufnagel,M., le Deist,F.,
            Fischer,A., Durandy,A., de Villartay,J.P. and Revy,P.
  TITLE     Cernunnos, a novel nonhomologous end-joining factor, is mutated in
            human immunodeficiency with microcephaly
  JOURNAL   Cell 124 (2), 287-299 (2006)
   PUBMED   16439204
  REMARK    GeneRIF: Cernunnos-XLF is a new Non-homologous End Joining pathway
            protein, which if mutated results in several conditions
            -immunodeficiency and developmental anomalies and other conditions,
            which likely result from inability to repair spontaneous DNA
            damage.
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Dai,Y., Kysela,B., Hanakahi,L.A., Manolis,K., Riballo,E., Stumm,M.,
            Harville,T.O., West,S.C., Oettinger,M.A. and Jeggo,P.A.
  TITLE     Nonhomologous end joining and V(D)J recombination require an
            additional factor
  JOURNAL   Proc Natl Acad Sci U S A 100 (5), 2462-2467 (2003)
   PUBMED   12604777
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068946.4 and AC097468.3.
            
            Summary: Double-strand breaks in DNA result from genotoxic stresses
            and are among the most damaging of DNA lesions. This gene encodes a
            DNA repair factor essential for the nonhomologous end-joining
            pathway, which preferentially mediates repair of double-stranded
            breaks. Mutations in this gene cause different kinds of severe
            combined immunodeficiency disorders. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1831567.1,
                                           SRR14038196.381.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..304
                     /product="non-homologous end-joining factor 1 isoform 2"
                     /note="XRCC4-like factor; protein cernunnos; nonhomologous
                     end-joining factor 1"
                     /calculated_mol_wt=33733
     Region          1..135
                     /region_name="Globular head.
                     /evidence=ECO:0000305|PubMed:16571728"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Region          12..174
                     /region_name="XLF"
                     /note="XLF-Cernunnos, XRcc4-like factor, NHEJ component;
                     pfam09302"
                     /db_xref="CDD:462749"
     Site            115
                     /site_type="other"
                     /note="Leu-lock. /evidence=ECO:0000303|PubMed:21775435;
                     propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PRKDC.
                     /evidence=ECO:0000269|PubMed:18644470,
                     ECO:0000269|PubMed:22228831, ECO:0000269|PubMed:28500754;
                     propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PRKDC.
                     /evidence=ECO:0000269|PubMed:18644470,
                     ECO:0000269|PubMed:22228831, ECO:0000269|PubMed:28500754;
                     propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PRKDC.
                     /evidence=ECO:0000269|PubMed:18644470,
                     ECO:0000269|PubMed:22228831, ECO:0000269|PubMed:28500754;
                     propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PRKDC.
                     /evidence=ECO:0000269|PubMed:18644470,
                     ECO:0000269|PubMed:22228831, ECO:0000269|PubMed:28500754;
                     propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Region          260..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18644470,
                     ECO:0000269|PubMed:22228831; propagated from
                     UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:18644470,
                     ECO:0000269|PubMed:22228831; propagated from
                     UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     Region          294..304
                     /region_name="XLM. /evidence=ECO:0000305|PubMed:27063109"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H9Q4.1)"
     CDS             1..304
                     /gene="NHEJ1"
                     /gene_synonym="IMD124; MCOPCB13; XLF"
                     /coded_by="NM_001377499.1:97..1011"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92945.1"
                     /db_xref="GeneID:79840"
                     /db_xref="HGNC:HGNC:25737"
                     /db_xref="MIM:611290"
ORIGIN      
        1 meeleqgllm qpwawlqlae nsllakvfit kqgyallvsd lqqvwheqvd tsvvsqrake
       61 lnkrltappa aflchldnll rpllkdaahp seatfscdcv adalilrvrs elsglpfywn
      121 fhcmlaspsl vsqhlirplm gmslalqcqv relatllhmk dleiqdyqes gatlirdrlk
      181 tepfeensfl eqfmieklpe acsigdgkpf vmnlqdlyma vttqevqvgq khqgagepsr
      241 gdphtsnsas lqgidsqcvn qpeqlvssap tlsapekest gtsgplqrpq lskvkrkkpr
      301 glfs
//
LOCUS       NP_001304098              64 aa            linear   PRI 21-NOV-2025
DEFINITION  small nuclear ribonucleoprotein G isoform e [Homo sapiens].
ACCESSION   NP_001304098
VERSION     NP_001304098.1
DBSOURCE    REFSEQ: accession NM_001317169.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   2  (residues 1 to 64)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 64)
  AUTHORS   Schneider,S., Brandina,I., Peter,D., Lagad,S., Fraudeau,A.,
            Portell-Montserrat,J., Tholen,J., Zhao,J. and Galej,W.P.
  TITLE     Structure of the human 20S U5 snRNP
  JOURNAL   Nat Struct Mol Biol 31 (5), 752-756 (2024)
   PUBMED   38467877
REFERENCE   4  (residues 1 to 64)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   5  (residues 1 to 64)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   6  (residues 1 to 64)
  AUTHORS   Fury,M.G., Zhang,W., Christodoulopoulos,I. and Zieve,G.W.
  TITLE     Multiple protein: protein interactions between the snRNP common
            core proteins
  JOURNAL   Exp Cell Res 237 (1), 63-69 (1997)
   PUBMED   9417867
REFERENCE   7  (residues 1 to 64)
  AUTHORS   Liu,Q., Fischer,U., Wang,F. and Dreyfuss,G.
  TITLE     The spinal muscular atrophy disease gene product, SMN, and its
            associated protein SIP1 are in a complex with spliceosomal snRNP
            proteins
  JOURNAL   Cell 90 (6), 1013-1021 (1997)
   PUBMED   9323129
REFERENCE   8  (residues 1 to 64)
  AUTHORS   Plessel,G., Luhrmann,R. and Kastner,B.
  TITLE     Electron microscopy of assembly intermediates of the snRNP core:
            morphological similarities between the RNA-free (E.F.G) protein
            heteromer and the intact snRNP core
  JOURNAL   J Mol Biol 265 (2), 87-94 (1997)
   PUBMED   9020971
REFERENCE   9  (residues 1 to 64)
  AUTHORS   Hermann,H., Fabrizio,P., Raker,V.A., Foulaki,K., Hornig,H.,
            Brahms,H. and Luhrmann,R.
  TITLE     snRNP Sm proteins share two evolutionarily conserved sequence
            motifs which are involved in Sm protein-protein interactions
  JOURNAL   EMBO J 14 (9), 2076-2088 (1995)
   PUBMED   7744013
REFERENCE   10 (residues 1 to 64)
  AUTHORS   Heinrichs,V., Hackl,W. and Luhrmann,R.
  TITLE     Direct binding of small nuclear ribonucleoprotein G to the Sm site
            of small nuclear RNA. Ultraviolet light cross-linking of protein G
            to the AAU stretch within the Sm site (AAUUUGUGG) of U1 small
            nuclear ribonucleoprotein reconstituted in vitro
  JOURNAL   J Mol Biol 227 (1), 15-28 (1992)
   PUBMED   1387914
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY168189.1, AC079338.5 and
            AI742299.1.
            
            Summary: The protein encoded by this gene is a component of the U1,
            U2, U4, and U5 small nuclear ribonucleoprotein complexes,
            precursors of the spliceosome. The encoded protein may also be a
            part of the U7 small nuclear ribonucleoprotein complex, which
            participates in the processing of the 3' end of histone
            transcripts. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Nov
            2015].
            
            Transcript Variant: This variant (6) contains two alternate exons
            in place of the first exon compared to variant 1. The resulting
            isoform (e) is shorter at the N-terminus compared to isoform a.
            Variants 5 and 6 both encode the same isoform (e).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HY177398.1, HY372248.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..64
                     /product="small nuclear ribonucleoprotein G isoform e"
                     /EC_number="1.8.1.4"
                     /note="small nuclear ribonucleoprotein G; snRNP-G; sm
                     protein G"
                     /calculated_mol_wt=6970
     Region          1..62
                     /region_name="Sm_G"
                     /note="Sm protein G; cd01719"
                     /db_xref="CDD:212466"
     Site            order(5..11,13..25,27..31)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212466"
     Site            order(8,13,26,47,49..50,52,55..59,61)
                     /site_type="other"
                     /note="heptamer interface [polypeptide binding]"
                     /db_xref="CDD:212466"
     Site            order(25,27,51,53)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212466"
     Site            47..58
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212466"
     CDS             1..64
                     /gene="SNRPG"
                     /gene_synonym="Sm-G; SMG"
                     /coded_by="NM_001317169.2:191..385"
                     /note="isoform e is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS82461.1"
                     /db_xref="GeneID:6637"
                     /db_xref="HGNC:HGNC:11163"
                     /db_xref="MIM:603542"
ORIGIN      
        1 mdkklslkln ggrhvqgilr gfdpfmnlvi decvematsg qqnnigmvvi rgnsiimlea
       61 lerv
//
LOCUS       NP_115805                669 aa            linear   PRI 21-NOV-2025
DEFINITION  leucine zipper putative tumor suppressor 2 isoform a [Homo
            sapiens].
ACCESSION   NP_115805 XP_046743
VERSION     NP_115805.1
DBSOURCE    REFSEQ: accession NM_032429.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Liu,R., Zhou,D., Yu,B. and Zhou,Z.
  TITLE     Phosphorylation of LZTS2 by PLK1 activates the Wnt pathway
  JOURNAL   Cell Signal 120, 111226 (2024)
   PUBMED   38740232
  REMARK    GeneRIF: Phosphorylation of LZTS2 by PLK1 activates the Wnt
            pathway.
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Peng,Y., Greenland,N.Y., Lang,U.E. and Stohr,B.A.
  TITLE     LZTS2: A novel and independent prognostic biomarker for clear cell
            renal cell carcinoma
  JOURNAL   Pathol Res Pract 232, 153831 (2022)
   PUBMED   35287088
  REMARK    GeneRIF: LZTS2: A novel and independent prognostic biomarker for
            clear cell renal cell carcinoma.
REFERENCE   4  (residues 1 to 669)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 669)
  AUTHORS   Schmeisser,M.J., Grabrucker,A.M., Bockmann,J. and Boeckers,T.M.
  TITLE     Synaptic cross-talk between N-methyl-D-aspartate receptors and
            LAPSER1-beta-catenin at excitatory synapses
  JOURNAL   J Biol Chem 284 (42), 29146-29157 (2009)
   PUBMED   19703901
REFERENCE   6  (residues 1 to 669)
  AUTHORS   Sudo,H. and Maru,Y.
  TITLE     LAPSER1/LZTS2: a pluripotent tumor suppressor linked to the
            inhibition of katanin-mediated microtubule severing
  JOURNAL   Hum Mol Genet 17 (16), 2524-2540 (2008)
   PUBMED   18490357
  REMARK    GeneRIF: LAPSER1 C terminal domain inhibits
            katanin(p80/p60)-mediated microtubule severing in vitro.
REFERENCE   7  (residues 1 to 669)
  AUTHORS   Cho,H.H., Song,J.S., Yu,J.M., Yu,S.S., Choi,S.J., Kim,D.H. and
            Jung,J.S.
  TITLE     Differential effect of NF-kappaB activity on beta-catenin/Tcf
            pathway in various cancer cells
  JOURNAL   FEBS Lett 582 (5), 616-622 (2008)
   PUBMED   18242184
REFERENCE   8  (residues 1 to 669)
  AUTHORS   Hyun Hwa,Cho., Hye Joon,Joo., Ji Sun,Song., Yong Chan,Bae. and Jin
            Sup,Jung.
  TITLE     Crossregulation of beta-catenin/Tcf pathway by NF-kappaB is
            mediated by lzts2 in human adipose tissue-derived mesenchymal stem
            cells
  JOURNAL   Biochim Biophys Acta 1783 (3), 419-428 (2008)
   PUBMED   17950943
  REMARK    GeneRIF: The reciprocal crosstalk between beta-catenin/Tcf pathway
            and NF-kappaB signaling in hMSCs is mediated through the regulation
            of lzts2 expression.
REFERENCE   9  (residues 1 to 669)
  AUTHORS   Thyssen,G., Li,T.H., Lehmann,L., Zhuo,M., Sharma,M. and Sun,Z.
  TITLE     LZTS2 is a novel beta-catenin-interacting protein and regulates the
            nuclear export of beta-catenin
  JOURNAL   Mol Cell Biol 26 (23), 8857-8867 (2006)
   PUBMED   17000760
  REMARK    GeneRIF: LZTS2 is a beta-catenin-interacting protein and modulates
            beta-catenin signaling and localization
REFERENCE   10 (residues 1 to 669)
  AUTHORS   Cabeza-Arvelaiz,Y., Thompson,T.C., Sepulveda,J.L. and Chinault,A.C.
  TITLE     LAPSER1: a novel candidate tumor suppressor gene from 10q24.3
  JOURNAL   Oncogene 20 (46), 6707-6717 (2001)
   PUBMED   11709705
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133215.17, HY039896.1 and
            BC006212.2.
            
            On Mar 22, 2004 this sequence version replaced XP_046743.3.
            
            Summary: The protein encoded by this gene belongs to the leucine
            zipper tumor suppressor family of proteins, which function in
            transcription regulation and cell cycle control. This family member
            can repress beta-catenin-mediated transcriptional activation and is
            a negative regulator of the Wnt signaling pathway. It negatively
            regulates microtubule severing at centrosomes, and is necessary for
            central spindle formation and cytokinesis completion. It is
            implicated in cancer, where it may inhibit cell proliferation and
            decrease susceptibility to tumor development. Alternative splicing
            of this gene results in multiple transcript variants. [provided by
            RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Variants 1, 2 and 3
            all encode isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC006212.2, SRR3476690.848579.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.31"
     Protein         1..669
                     /product="leucine zipper putative tumor suppressor 2
                     isoform a"
                     /note="protein LAPSER1; leucine zipper, putative tumor
                     suppressor 2"
                     /calculated_mol_wt=72629
     Region          1..332
                     /region_name="Required for centrosomal localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRK4.2)"
     Region          1..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRK4.2)"
     Region          92..131
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRK4.2)"
     Region          150..201
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRK4.2)"
     Region          215..323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRK4.2)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91YU6; propagated from
                     UniProtKB/Swiss-Prot (Q9BRK4.2)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91YU6; propagated from
                     UniProtKB/Swiss-Prot (Q9BRK4.2)"
     Region          <333..>538
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          439..636
                     /region_name="Fez1"
                     /note="pfam06818"
                     /db_xref="CDD:462015"
     Region          447..669
                     /region_name="Sufficient for interaction with CTNNB1.
                     /evidence=ECO:0000269|PubMed:17000760"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRK4.2)"
     Region          450..669
                     /region_name="Sufficient for interaction with KATNB1 and
                     for inhibition of katanin-mediated microtubule severing.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRK4.2)"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BRK4.2)"
     Region          631..640
                     /region_name="Nuclear export signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRK4.2)"
     CDS             1..669
                     /gene="LZTS2"
                     /gene_synonym="LAPSER1"
                     /coded_by="NM_032429.4:207..2216"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7507.1"
                     /db_xref="GeneID:84445"
                     /db_xref="HGNC:HGNC:29381"
                     /db_xref="MIM:610454"
ORIGIN      
        1 maivqtlpvp lepapeaata pqapvmgsvs slisgrpcpg gpapprhhgp pgptffrqqd
       61 gllrggyeaq eplcpavppr kavpvtsfty inedfrtesp pspssdveda reqrahnahl
      121 rgpppklipv sgkleknmek ilirptafkp vlpkprgaps lpsfmgprat glsgsqgslt
      181 qlfggpasss sssssssaad kplafsgwas gcpsgtlsds grnslsslpt ystggaeptt
      241 sspgghlpsh gsgrgalpgp argvptgpsh sdsgrssssk stgslggrva ggllgsgtra
      301 spdssscger spppppppps deallhcvle gklrdreael qqlrdslden eatmcqayee
      361 rqrhwqrere alredcaaqa qraqraqqll qlqvfqlqqe krqlqddfaq llqereqler
      421 rcatlereqr elgprleetk wevcqksgei sllkqqlkes qaelvqkgse lvalrvalre
      481 aratlrvseg rarglqeaar areleleacs qelqrhrqea eqlrekagql daeaaglrep
      541 pvppatadpf llaesdeakv qraaagvggs lraqverlrv elqrerrrge eqrdsfeger
      601 lawqaekeqv iryqkqlqhn yiqmyrrnrq leqelqqlsl eleareladl glaeqapcic
      661 leeitatei
//
LOCUS       NP_001363703             538 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 33 [Homo sapiens].
ACCESSION   NP_001363703
VERSION     NP_001363703.1
DBSOURCE    REFSEQ: accession NM_001376774.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Muckenfuss,L.M., Migenda Herranz,A.C., Boneberg,F.M., Clerici,M.
            and Jinek,M.
  TITLE     Fip1 is a multivalent interaction scaffold for processing factors
            in human mRNA 3' end biogenesis
  JOURNAL   Elife 11, e80332 (2022)
   PUBMED   36073787
  REMARK    GeneRIF: Fip1 is a multivalent interaction scaffold for processing
            factors in human mRNA 3' end biogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Tennenbaum,J., Groh,M., Venditti,L., Campos-Gazeau,F., Chalayer,E.,
            De Broucker,T., Hamidou,M., Hunault,M., Lyoubi,A., Meunier,R.,
            Muron,T., Sene,D., Slama,B., Guidoux,C., Lefevre,G., Kahn,J.E.,
            Denier,C. and Rohmer,J.
  TITLE     FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a Treatable
            Cause of Watershed Infarction
  JOURNAL   Stroke 52 (10), e605-e609 (2021)
   PUBMED   34304603
  REMARK    GeneRIF: FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a
            Treatable Cause of Watershed Infarction.
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Helbig,G., Lewandowski,K., Swiderska,A., Rodzaj,M., Seferynska,I.
            and Gajkowska-Kulik,J.
  TITLE     Exquisite response to imatinib mesylate in FIP1L1-PDGFRA-mutated
            hypereosinophilic syndrome: a 12-year experience of the Polish
            Hypereosinophilic Syndrome Study Group
  JOURNAL   Pol Arch Intern Med 130 (3), 255-257 (2020)
   PUBMED   32125294
  REMARK    GeneRIF: Exquisite response to imatinib mesylate in
            FIP1L1-PDGFRA-mutated hypereosinophilic syndrome: a 12-year
            experience of the Polish Hypereosinophilic Syndrome Study Group.
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Cools,J., Quentmeier,H., Huntly,B.J., Marynen,P., Griffin,J.D.,
            Drexler,H.G. and Gilliland,D.G.
  TITLE     The EOL-1 cell line as an in vitro model for the study of
            FIP1L1-PDGFRA-positive chronic eosinophilic leukemia
  JOURNAL   Blood 103 (7), 2802-2805 (2004)
   PUBMED   14630792
  REMARK    GeneRIF: results indicate that the fusion of FIP1L1 to PDGFRA
            occurs rarely in leukemia cell lines
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Kaufmann,I., Martin,G., Friedlein,A., Langen,H. and Keller,W.
  TITLE     Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements
            and stimulates poly(A) polymerase
  JOURNAL   EMBO J 23 (3), 616-626 (2004)
   PUBMED   14749727
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Pardanani,A., Ketterling,R.P., Brockman,S.R., Flynn,H.C.,
            Paternoster,S.F., Shearer,B.M., Reeder,T.L., Li,C.Y., Cross,N.C.,
            Cools,J., Gilliland,D.G., Dewald,G.W. and Tefferi,A.
  TITLE     CHIC2 deletion, a surrogate for FIP1L1-PDGFRA fusion, occurs in
            systemic mastocytosis associated with eosinophilia and predicts
            response to imatinib mesylate therapy
  JOURNAL   Blood 102 (9), 3093-3096 (2003)
   PUBMED   12842979
  REMARK    GeneRIF: observations suggest that the FIP1L1-PDGFRA rearrangement
            occurs in an early hematopoietic progenitor and suggests that the
            molecular pathogenesis for a subset of SMCD patients is similar to
            that of HES
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Griffin,J.H., Leung,J., Bruner,R.J., Caligiuri,M.A. and
            Briesewitz,R.
  TITLE     Discovery of a fusion kinase in EOL-1 cells and idiopathic
            hypereosinophilic syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (13), 7830-7835 (2003)
   PUBMED   12808148
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Cools,J., DeAngelo,D.J., Gotlib,J., Stover,E.H., Legare,R.D.,
            Cortes,J., Kutok,J., Clark,J., Galinsky,I., Griffin,J.D.,
            Cross,N.C., Tefferi,A., Malone,J., Alam,R., Schrier,S.L.,
            Schmid,J., Rose,M., Vandenberghe,P., Verhoef,G., Boogaerts,M.,
            Wlodarska,I., Kantarjian,H., Marynen,P., Coutre,S.E., Stone,R. and
            Gilliland,D.G.
  TITLE     A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes
            as a therapeutic target of imatinib in idiopathic hypereosinophilic
            syndrome
  JOURNAL   N Engl J Med 348 (13), 1201-1214 (2003)
   PUBMED   12660384
  REMARK    GeneRIF: The hypereosinophilic syndrome may result from a novel
            fusion tyrosine kinase - FIP1L1-PDGFRalpha - that is a consequence
            of an interstitial chromosomal deletion.
            GeneRIF: Describes the fusion gene Fip1-like-1-PDGFRalpha in
            patients with idiopathic hypereosinophilic syndrome, mostly
            responsive to imatinib therapy.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098821.3 and AC058822.6.
            
            Summary: This gene encodes a subunit of the CPSF (cleavage and
            polyadenylation specificity factor) complex that polyadenylates the
            3' end of mRNA precursors. This gene, the homolog of yeast Fip1
            (factor interacting with PAP), binds to U-rich sequences of
            pre-mRNA and stimulates poly(A) polymerase activity. Its N-terminus
            contains a PAP-binding site and its C-terminus an RNA-binding
            domain. An interstitial chromosomal deletion on 4q12 creates an
            in-frame fusion of human genes FIP1L1 and PDGFRA (platelet-derived
            growth factor receptor, alpha). The FIP1L1-PDGFRA fusion gene
            encodes a constitutively activated tyrosine kinase that joins the
            first 233 amino acids of FIP1L1 to the last 523 amino acids of
            PDGFRA. This gene fusion and chromosomal deletion is the cause of
            some forms of idiopathic hypereosinophilic syndrome (HES). This
            syndrome, recently reclassified as chronic eosinophilic leukemia
            (CEL), is responsive to treatment with tyrosine kinase inhibitors.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3805447.1,
                                           SRR14038194.3928870.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..538
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     33"
                     /note="rearranged in hypereosinophilia; pre-mRNA
                     3'-end-processing factor FIP1; FIP1-like 1 protein; factor
                     interacting with PAP; FIP1 like 1; FIP1L1 cleavage and
                     polyadenylation specific factor subunit"
                     /calculated_mol_wt=60288
     Region          154..196
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     CDS             1..538
                     /gene="FIP1L1"
                     /gene_synonym="FIP1; hFip1; Rhe"
                     /coded_by="NM_001376774.1:199..1815"
                     /note="isoform 33 is encoded by transcript variant 33"
                     /db_xref="GeneID:81608"
                     /db_xref="HGNC:HGNC:19124"
                     /db_xref="MIM:607686"
ORIGIN      
        1 msageverlv selsggtggd eeeewlyggp wdvhvhsdla kdldenever peeenasanp
       61 psgiedetae ngvpkpkvte teddsdsdsd ddeddvhvti gdiktgapqy gsygtapvnl
      121 niktggrvyg ttgtkvkgvd ldapgsingv pllevdldsf edkpwrkpga dlsdyfnygf
      181 nedtwkayce kqkrirmgle vipvtsttnk itvqqgrtgn seketalpst kaeftsppsl
      241 fktglppsrr lpgaidvigq titisrvegr rranensniq vlsersatev dnnfskpppf
      301 fppgappthl ppppflpppp tvstapplip ppgfppppga pppsliptie sghssgydsr
      361 sarafpygnv afphlpgsap swpslvdtsk qwdyyarrek drdrerdrdr erdrdrdrer
      421 ertrererer dhsptpsvfn rfvgdeeryr yreyaergye rhrasrekee rhrerrhrek
      481 eetrhkssrs nsrrrhesee gdshrrhkhk kskrskegke agsepapeqe steatpae
//
LOCUS       NP_001338783             917 aa            linear   PRI 21-NOV-2025
DEFINITION  liprin-beta-2 isoform 5 [Homo sapiens].
ACCESSION   NP_001338783
VERSION     NP_001338783.2
DBSOURCE    REFSEQ: accession NM_001351854.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 917)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 917)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 917)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 917)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 917)
  AUTHORS   Wu,Y., Yu,H., Zheng,S.L., Feng,B., Kapron,A.L., Na,R., Boyle,J.L.,
            Shah,S., Shi,Z., Ewing,C.M., Wiley,K.E., Luo,J., Walsh,P.C.,
            Carter,H.B., Helfand,B.T., Cooney,K.A., Xu,J. and Isaacs,W.B.
  TITLE     Germline mutations in PPFIBP2 are associated with lethal prostate
            cancer
  JOURNAL   Prostate 78 (16), 1222-1228 (2018)
   PUBMED   30043417
  REMARK    GeneRIF: germline mutations in a novel gene, PPFIBP2,
            differentiated risk for lethal prostate cancer from low-risk cases
            and were associated with shorter survival times after diagnosis.
REFERENCE   6  (residues 1 to 917)
  AUTHORS   von Thun,A., Birtwistle,M., Kalna,G., Grindlay,J., Strachan,D.,
            Kolch,W., von Kriegsheim,A. and Norman,J.C.
  TITLE     ERK2 drives tumour cell migration in three-dimensional
            microenvironments by suppressing expression of Rab17 and
            liprin-beta2
  JOURNAL   J Cell Sci 125 (Pt 6), 1465-1477 (2012)
   PUBMED   22328529
  REMARK    GeneRIF: Knockdown of either Rab17 or liprin-beta2 restores
            invasiveness of ERK2-depleted cells, indicating that ERK2 drives
            invasion of MDA-MB-231 cells by suppressing expression of these
            genes.
REFERENCE   7  (residues 1 to 917)
  AUTHORS   Colas,E., Perez,C., Cabrera,S., Pedrola,N., Monge,M., Castellvi,J.,
            Eyzaguirre,F., Gregorio,J., Ruiz,A., Llaurado,M., Rigau,M.,
            Garcia,M., Ertekin,T., Montes,M., Lopez-Lopez,R., Carreras,R.,
            Xercavins,J., Ortega,A., Maes,T., Rosell,E., Doll,A., Abal,M.,
            Reventos,J. and Gil-Moreno,A.
  TITLE     Molecular markers of endometrial carcinoma detected in uterine
            aspirates
  JOURNAL   Int J Cancer 129 (10), 2435-2444 (2011)
   PUBMED   21207424
  REMARK    Erratum:[Int J Cancer. 2012 Jun 15;130(12):E4]
REFERENCE   8  (residues 1 to 917)
  AUTHORS   Stafford,R.L., Tang,M.Y., Sawaya,M.R., Phillips,M.L. and Bowie,J.U.
  TITLE     Crystal structure of the central coiled-coil domain from human
            liprin-beta2
  JOURNAL   Biochemistry 50 (18), 3807-3815 (2011)
   PUBMED   21462929
  REMARK    GeneRIF: analysis of crystal structure of the central coiled-coil
            domain from human liprin-beta2
REFERENCE   9  (residues 1 to 917)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 917)
  AUTHORS   Serra-Pages,C., Medley,Q.G., Tang,M., Hart,A. and Streuli,M.
  TITLE     Liprins, a family of LAR transmembrane protein-tyrosine
            phosphatase-interacting proteins
  JOURNAL   J Biol Chem 273 (25), 15611-15620 (1998)
   PUBMED   9624153
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107884.15 and AC104237.2.
            
            On May 21, 2020 this sequence version replaced NP_001338783.1.
            
            Summary: This gene encodes a member of the LAR protein-tyrosine
            phosphatase-interacting protein (liprin) family. The encoded
            protein is a beta liprin and plays a role in axon guidance and
            neuronal synapse development by recruiting LAR protein-tyrosine
            phosphatases to the plasma membrane. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene. [provided by RefSeq, Feb 2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.195034.1,
                                           SRR18074969.3749996.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..917
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..917
                     /product="liprin-beta-2 isoform 5"
                     /note="protein tyrosine phosphatase receptor type f
                     polypeptide-interacting protein-binding protein 2; PTPRF
                     interacting protein, binding protein 2 (liprin beta 2);
                     PPFIA binding protein 2"
                     /calculated_mol_wt=103179
     Region          59..>317
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8ND30.3)"
     Region          356..376
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8ND30.3)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8ND30.3)"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8ND30.3)"
     Region          425..451
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8ND30.3)"
     Region          470..500
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8ND30.3)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8ND30.3)"
     Region          527..553
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8ND30.3)"
     Region          555..618
                     /region_name="SAM_liprin-beta1,2_repeat1"
                     /note="SAM domain of liprin-beta1,2 proteins repeat 1;
                     cd09563"
                     /db_xref="CDD:188962"
     Region          629..691
                     /region_name="SAM_liprin-beta1,2_repeat2"
                     /note="SAM domain of liprin-beta1,2 proteins repeat 2;
                     cd09566"
                     /db_xref="CDD:188965"
     Region          714..785
                     /region_name="SAM_liprin-beta1,2_repeat3"
                     /note="SAM domain of liprin-beta proteins repeat 3;
                     cd09569"
                     /db_xref="CDD:188968"
     CDS             1..917
                     /gene="PPFIBP2"
                     /gene_synonym="Cclp1"
                     /coded_by="NM_001351854.2:160..2913"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:8495"
                     /db_xref="HGNC:HGNC:9250"
                     /db_xref="MIM:603142"
ORIGIN      
        1 masdashale aaleqmdgii agtktgadls dgtcepglas pasymnpfpv lhliedlrla
       61 lemlelpqer aallsqipgp taayikewfe eslsqvnhhs aasnetyqer larlegdkes
      121 lilqvsvltd qveaqgekir dlevcleghq vklnaaeeml qqellsrtsl etqkldlmte
      181 vselklklvg mekeqreqee kqrkaeellq elrhlkikve elenernqye wklkatkaev
      241 aqlqeqvalk daeierlhsq lsrtaalhse shterdqeiq rlkmgmetll lanedkdrri
      301 eeltgllnqy rkvkeivmvt qgpsertlsi neeepeggfs kwnatnkdpe elfkqemppr
      361 cssptvgppp lpqksletra qkklscsled lrsesvdkcm dgnqpfpvle pkdspflaeh
      421 kyptlpgkls gatpngeaak sppticqpda tgssllrlrd tesgwddtav vndlsstssg
      481 tesgpqsplt pdgkrnpkgi kkfwgkirrt qsgnfytdtl gmaefrrggl ratagprlsr
      541 trdskgqksd anapfaqwst ervcawledf glaqyvifar qwvssghtll tatpqdmeke
      601 lgikhplhrk klvlavkain tkqeeksall dhiwvtrwld diglpqykdq fhesrvdrrm
      661 lqyltvndll flkvtsqlhh lsikcaihvl hvnkfnphcl hrrpadesnl spsevvqwsn
      721 hrvmewlrsv dlaeyapnlr gsgvhgglii leprftgdtl amllnippqk tllrrhlttk
      781 fnaligpeae qekrekmasp aytpltttak vrprklgfsh fgnirkkkfd estdyicpme
      841 psdgvsdshr vysgyrglsp ldapeldgld qhqwkhmnfd agpetmdtpt rlssqapptl
      901 qlreklkclr pvdhslg
//
LOCUS       NP_001382409             877 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA-processing factor 40 homolog A isoform 15 [Homo sapiens].
ACCESSION   NP_001382409
VERSION     NP_001382409.1
DBSOURCE    REFSEQ: accession NM_001395480.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 877)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 877)
  AUTHORS   Choudhary,B. and Norris,A.
  TITLE     Conserved role for spliceosomal component PRPF40A in microexon
            splicing
  JOURNAL   RNA 31 (1), 43-50 (2024)
   PUBMED   39389624
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 877)
  AUTHORS   Martinez-Lumbreras,S., Trager,L.K., Mulorz,M.M., Payr,M.,
            Dikaya,V., Hipp,C., Konig,J. and Sattler,M.
  TITLE     Intramolecular autoinhibition regulates the selectivity of PRPF40A
            tandem WW domains for proline-rich motifs
  JOURNAL   Nat Commun 15 (1), 3888 (2024)
   PUBMED   38719828
  REMARK    GeneRIF: Intramolecular autoinhibition regulates the selectivity of
            PRPF40A tandem WW domains for proline-rich motifs.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 877)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 877)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 877)
  AUTHORS   Allen,M., Friedler,A., Schon,O. and Bycroft,M.
  TITLE     The structure of an FF domain from human HYPA/FBP11
  JOURNAL   J Mol Biol 323 (3), 411-416 (2002)
   PUBMED   12381297
  REMARK    GeneRIF: Data describe the structure of an FF domain from
            HYPA/FBP11, which differs from those of other
            phosphopeptide-binding domains and represents a novel
            phosphopeptide-binding fold.
REFERENCE   7  (residues 1 to 877)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   8  (residues 1 to 877)
  AUTHORS   Bedford,M.T., Reed,R. and Leder,P.
  TITLE     WW domain-mediated interactions reveal a spliceosome-associated
            protein that binds a third class of proline-rich motif: the proline
            glycine and methionine-rich motif
  JOURNAL   Proc Natl Acad Sci U S A 95 (18), 10602-10607 (1998)
   PUBMED   9724750
REFERENCE   9  (residues 1 to 877)
  AUTHORS   Faber,P.W., Barnes,G.T., Srinidhi,J., Chen,J., Gusella,J.F. and
            MacDonald,M.E.
  TITLE     Huntingtin interacts with a family of WW domain proteins
  JOURNAL   Hum Mol Genet 7 (9), 1463-1474 (1998)
   PUBMED   9700202
REFERENCE   10 (residues 1 to 877)
  AUTHORS   Chan,D.C., Bedford,M.T. and Leder,P.
  TITLE     Formin binding proteins bear WWP/WW domains that bind proline-rich
            peptides and functionally resemble SH3 domains
  JOURNAL   EMBO J 15 (5), 1045-1054 (1996)
   PUBMED   8605874
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079344.5 and AC012443.8.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..877
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q23.3"
     Protein         1..877
                     /product="pre-mRNA-processing factor 40 homolog A isoform
                     15"
                     /note="formin binding protein 3; Huntingtin-interacting
                     protein A; NY-REN-6 antigen; Fas-ligand associated factor
                     1; formin-binding protein 11; huntingtin yeast partner A;
                     fas ligand-associated factor 1; pre-mRNA processing factor
                     40 homolog A; renal carcinoma antigen NY-REN-6;
                     huntingtin-interacting protein 10; PRP40 pre-mRNA
                     processing factor 40 homolog A"
                     /calculated_mol_wt=99978
     Region          104..134
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(118,129)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          <165..>307
                     /region_name="PHA03255"
                     /note="BDLF3; Provisional"
                     /db_xref="CDD:165513"
     Region          <298..716
                     /region_name="PRP40"
                     /note="Splicing factor [RNA processing and modification];
                     COG5104"
                     /db_xref="CDD:227435"
     CDS             1..877
                     /gene="PRPF40A"
                     /gene_synonym="FBP-11; FBP11; FLAF1; FNBP3; HIP-10; HIP10;
                     HYPA; NY-REN-6; Prp40"
                     /coded_by="NM_001395480.1:23..2656"
                     /note="isoform 15 is encoded by transcript variant 21"
                     /db_xref="GeneID:55660"
                     /db_xref="HGNC:HGNC:16463"
                     /db_xref="MIM:612941"
ORIGIN      
        1 mcsgsgrrrs slsptmrpgt gaergglmmg hpgmhyapmg mhpmgqranm ppvphgmmpq
       61 mmppmggppm gqmpgmmssv mpgmmmshms qasmqpalpq llskcpwkey ksdsgkpyyy
      121 nsqtkesrwa kpkeledleg yqntivagsl itksnlhami kaeesskqee ctttstapvp
      181 tteipttmst maaaeaaaav vaaaaaaaaa aaaananast sasntvsgtv pvvpepevts
      241 ivatvvdnen tvtisteeqa qltstpaiqd qsvevssntg eetskqetva dftpkkeeee
      301 sqpakktytw ntkeeakqaf kellkekrvp snasweqamk miindprysa laklsekkqa
      361 fnaykvqtek eekeearsky keakesfqrf lenhekmtst trykkaeqmf gemevwnais
      421 erdrleiyed vlfflskkek eqakqlrkrn wealknildn manvtysttw seaqqylmdn
      481 ptfaedeelq nmdkedalic feehiralek eeeeekqksl lrerrrqrkn resfqiflde
      541 lhehgqlhsm sswmelypti ssdirftnml gqpgstaldl fkfyvedlka ryhdekkiik
      601 dilkdkgfvv evnttfedfv aiisstkrst tldagnikla fnsllekaea rererekeea
      661 rkmkrkesaf ksmlkqaapp ieldavwedi rerfvkepaf editleserk rifkdfmhvl
      721 ehecqhhhsk nkkhskkskk hhrkrsrsrs gsdsddddsh skkkrqrses rsasehsssa
      781 esersykksk khkkkskkrr hksdspesda erekdkkekd resekdrtrq rseskhkspk
      841 kktgkdsgnw dtsgselseg elekrrrtll eqldddq
//
LOCUS       NP_001356580             338 aa            linear   PRI 21-NOV-2025
DEFINITION  snRNA-activating protein complex subunit 3 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001356580
VERSION     NP_001356580.1
DBSOURCE    REFSEQ: accession NM_001369651.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Sun,J., Li,X., Hou,X., Cao,S., Cao,W., Zhang,Y., Song,J., Wang,M.,
            Wang,H., Yan,X., Li,Z., Roeder,R.G. and Wang,W.
  TITLE     Structural basis of human SNAPc recognizing proximal sequence
            element of snRNA promoter
  JOURNAL   Nat Commun 13 (1), 6871 (2022)
   PUBMED   36369505
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Henry,R.W., Mittal,V., Ma,B., Kobayashi,R. and Hernandez,N.
  TITLE     SNAP19 mediates the assembly of a functional core promoter complex
            (SNAPc) shared by RNA polymerases II and III
  JOURNAL   Genes Dev 12 (17), 2664-2672 (1998)
   PUBMED   9732265
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Henry,R.W., Ma,B., Sadowski,C.L., Kobayashi,R. and Hernandez,N.
  TITLE     Cloning and characterization of SNAP50, a subunit of the
            snRNA-activating protein complex SNAPc
  JOURNAL   EMBO J 15 (24), 7129-7136 (1996)
   PUBMED   9003788
REFERENCE   8  (residues 1 to 338)
  AUTHORS   Bai,L., Wang,Z., Yoon,J.B. and Roeder,R.G.
  TITLE     Cloning and characterization of the beta subunit of human proximal
            sequence element-binding transcription factor and its involvement
            in transcription of small nuclear RNA genes by RNA polymerases II
            and III
  JOURNAL   Mol Cell Biol 16 (10), 5419-5426 (1996)
   PUBMED   8816454
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Henry,R.W., Sadowski,C.L., Kobayashi,R. and Hernandez,N.
  TITLE     A TBP-TAF complex required for transcription of human snRNA genes
            by RNA polymerase II and III
  JOURNAL   Nature 374 (6523), 653-656 (1995)
   PUBMED   7715707
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Bagramian,E.R., Bogdanova,E.A., Krymskaia,M.L. and Sokovykh,S.I.
  TITLE     [Diagnostic importance of determining 17-ketosteroids in
            gynecology]
  JOURNAL   Akush Ginekol (Mosk) (2), 65-67 (1977)
   PUBMED   900378
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL441925.16 and AL359998.21.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.430664.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145313, SAMEA2145774
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p22.3"
     Protein         1..338
                     /product="snRNA-activating protein complex subunit 3
                     isoform 6"
                     /note="snRNA-activating protein complex subunit 3; SNAPc
                     subunit 3; PTF subunit beta; SNAPc 50 kDa subunit;
                     PSE-binding factor subunit beta; snRNA-activating protein
                     complex 50 kDa subunit; proximal sequence element-binding
                     transcription factor subunit beta; small nuclear RNA
                     activating complex, polypeptide 3, 50kD; small nuclear RNA
                     activating complex, polypeptide 3, 50kDa"
                     /calculated_mol_wt=37876
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92966.1)"
     Region          63..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92966.1)"
     Region          202..>329
                     /region_name="SNAPC3"
                     /note="snRNA-activating protein complex (SNAPc), subunit
                     3; pfam12251"
                     /db_xref="CDD:463506"
     CDS             1..338
                     /gene="SNAPC3"
                     /gene_synonym="PTFbeta; SNAP50"
                     /coded_by="NM_001369651.2:5..1021"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:6619"
                     /db_xref="HGNC:HGNC:11136"
                     /db_xref="MIM:602348"
ORIGIN      
        1 maegsrggpt csgvggrqdp vsgsggcnfp eyelpelntr afhvgafgel wrgrlrgagd
       61 lslreppasa lpgsqaadsd redaavardl dcsleaaael ravcgldklk cledgedpev
      121 ipentdlvtl gvrkrflehr eetitidrac rqetfvyeme shaigkkpen sadmieegel
      181 ilsvnilypv ifhkhkehkp yqtmlvlgsq kltqlrdsir cvsdlqigge fsntpdqape
      241 hiskdlyksa ffyfegtfyn dkrypecrdl srtiiewses hdrgygkfqt armedftfnd
      301 lciklgfpyl ychqgdcehv ivitdirlyl nlteyldg
//
LOCUS       NP_001351539             242 aa            linear   PRI 21-NOV-2025
DEFINITION  mitogen-activated protein kinase 9 isoform JNK2 gamma [Homo
            sapiens].
ACCESSION   NP_001351539
VERSION     NP_001351539.1
DBSOURCE    REFSEQ: accession NM_001364610.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Ishibashi,R., Itani,M., Kawashima,A., Arakawa,Y. and Aoki,T.
  TITLE     JNK2-MMP-9 axis facilitates the progression of intracranial
            aneurysms
  JOURNAL   Sci Rep 14 (1), 19458 (2024)
   PUBMED   39169203
  REMARK    GeneRIF: JNK2-MMP-9 axis facilitates the progression of
            intracranial aneurysms.
            Erratum:[Sci Rep. 2025 Sep 18;15(1):32593. doi:
            10.1038/s41598-025-17846-w. PMID: 40968147]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Yang,F., Zhuang,Z., Liu,C., Li,F. and Zhou,J.
  TITLE     Overexpression of circZNF720 Inhibits Hepatocellular Carcinoma
            Progression by Regulating miR-421/MAPK9
  JOURNAL   Mol Biotechnol 66 (5), 1165-1173 (2024)
   PUBMED   38159171
  REMARK    GeneRIF: Overexpression of circZNF720 Inhibits Hepatocellular
            Carcinoma Progression by Regulating miR-421/MAPK9.
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Wang,K., Lu,Q., Luo,Y., Yu,G., Wang,Z., Lin,J., Tan,Z., Lao,Y.,
            Liu,S. and Yang,H.
  TITLE     Circ_MAPK9 promotes STAT3 and LDHA expression by silencing
            miR-642b-3p and affects the progression of hepatocellular carcinoma
  JOURNAL   Biol Direct 19 (1), 4 (2024)
   PUBMED   38163874
  REMARK    GeneRIF: Circ_MAPK9 promotes STAT3 and LDHA expression by silencing
            miR-642b-3p and affects the progression of hepatocellular
            carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Wang,L., Guo,M., Gao,L., Liu,K., Bai,J. and Liu,Z.
  TITLE     JNK2 Promotes Progression of Esophageal Squamous Cell Carcinoma via
            Inhibiting Axin2
  JOURNAL   Curr Pharm Des 29 (37), 2977-2987 (2023)
   PUBMED   37957865
  REMARK    GeneRIF: JNK2 Promotes Progression of Esophageal Squamous Cell
            Carcinoma via Inhibiting Axin2.
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Livingstone,C., Patel,G. and Jones,N.
  TITLE     ATF-2 contains a phosphorylation-dependent transcriptional
            activation domain
  JOURNAL   EMBO J 14 (8), 1785-1797 (1995)
   PUBMED   7737129
REFERENCE   7  (residues 1 to 242)
  AUTHORS   Kallunki,T., Su,B., Tsigelny,I., Sluss,H.K., Derijard,B., Moore,G.,
            Davis,R. and Karin,M.
  TITLE     JNK2 contains a specificity-determining region responsible for
            efficient c-Jun binding and phosphorylation
  JOURNAL   Genes Dev 8 (24), 2996-3007 (1994)
   PUBMED   8001819
REFERENCE   8  (residues 1 to 242)
  AUTHORS   Sluss,H.K., Barrett,T., Derijard,B. and Davis,R.J.
  TITLE     Signal transduction by tumor necrosis factor mediated by JNK
            protein kinases
  JOURNAL   Mol Cell Biol 14 (12), 8376-8384 (1994)
   PUBMED   7969172
REFERENCE   9  (residues 1 to 242)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   10 (residues 1 to 242)
  AUTHORS   Denys,H., Desmet,R., Stragier,M., Vergison,R. and Lemahieu,S.F.
  TITLE     Cystitis emphysematosa
  JOURNAL   Acta Urol Belg 45 (4), 327-331 (1977)
   PUBMED   602896
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008610.7 and AC104115.3.
            
            Summary: The protein encoded by this gene is a member of the MAP
            kinase family. MAP kinases act as an integration point for multiple
            biochemical signals, and are involved in a wide variety of cellular
            processes such as proliferation, differentiation, transcription
            regulation and development. This kinase targets specific
            transcription factors, and thus mediates immediate-early gene
            expression in response to various cell stimuli. It is most closely
            related to MAPK8, both of which are involved in UV radiation
            induced apoptosis, thought to be related to the cytochrome
            c-mediated cell death pathway. This gene and MAPK8 are also known
            as c-Jun N-terminal kinases. This kinase blocks the ubiquitination
            of tumor suppressor p53, and thus it increases the stability of p53
            in nonstressed cells. Studies of this gene's mouse counterpart
            suggest a key role in T-cell differentiation. Several alternatively
            spliced transcript variants encoding distinct isoforms have been
            reported. [provided by RefSeq, Sep 2008].
            
            Transcript Variant: This variant (10), as well as variant JNK2-g,
            encodes isoform JNK2 gamma.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.629864.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..242
                     /product="mitogen-activated protein kinase 9 isoform JNK2
                     gamma"
                     /EC_number="2.7.11.24"
                     /note="c-Jun N-terminal kinase 2; stress-activated protein
                     kinase JNK2; MAP kinase 9; c-Jun kinase 2; MAPK 9;
                     stress-activated protein kinase 1a"
                     /calculated_mol_wt=27203
     Region          25..>231
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(32..35,38,40,53,55,86,108..111,151,155..156,158,
                     168..169)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Region          183..185
                     /region_name="TXY"
                     /note="propagated from UniProtKB/Swiss-Prot (P45984.2)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAP2K7.
                     /evidence=ECO:0000269|PubMed:11062067; propagated from
                     UniProtKB/Swiss-Prot (P45984.2)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by MAP2K4.
                     /evidence=ECO:0000269|PubMed:11062067; propagated from
                     UniProtKB/Swiss-Prot (P45984.2)"
     CDS             1..242
                     /gene="MAPK9"
                     /gene_synonym="JNK-55; JNK2; JNK2A; JNK2ALPHA; JNK2B;
                     JNK2BETA; p54a; p54aSAPK; PRKM9; SAPK; SAPK1a"
                     /coded_by="NM_001364610.2:377..1105"
                     /note="isoform JNK2 gamma is encoded by transcript variant
                     10"
                     /db_xref="CCDS:CCDS47356.1"
                     /db_xref="GeneID:5601"
                     /db_xref="HGNC:HGNC:6886"
                     /db_xref="MIM:602896"
ORIGIN      
        1 msdskcdsqf ysvqvadstf tvlkryqqlk pigsgaqgiv caafdtvlgi nvavkklsrp
       61 fqnqthakra yrelvllkcv nhkniislln vftpqktlee fqdvylvmel mdanlcqvih
      121 meldhermsy llyqmlcgik hlhsagiihr dlkpsnivvk sdctlkildf glartactnf
      181 mmtpyvvtry yrapevilgm gykenvdiws vgcimgelvk gcvifqgtdr ilprdlgpam
      241 ls
//
LOCUS       NP_001099034             871 aa            linear   PRI 21-NOV-2025
DEFINITION  coiled-coil alpha-helical rod protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001099034
VERSION     NP_001099034.1
DBSOURCE    REFSEQ: accession NM_001105564.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Xu,X., Qiu,L., Zhang,M. and Wu,G.
  TITLE     Segregation of nascent GPCRs in the ER-to-Golgi transport by CCHCR1
            via direct interaction
  JOURNAL   J Cell Sci 137 (3) (2024)
   PUBMED   38230433
  REMARK    GeneRIF: Segregation of nascent GPCRs in the ER-to-Golgi transport
            by CCHCR1 via direct interaction.
REFERENCE   3  (residues 1 to 871)
  CONSRTM   COVID-19 Host Genetics Initiative
  TITLE     A first update on mapping the human genetic architecture of
            COVID-19
  JOURNAL   Nature 608 (7921), E1-E10 (2022)
   PUBMED   35922517
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 871)
  AUTHORS   Pisani,C., Onori,A., Gabanella,F., Di Certo,M.G., Passananti,C. and
            Corbi,N.
  TITLE     Identification of protein/mRNA network involving the PSORS1 locus
            gene CCHCR1 and the PSORS4 locus gene HAX1
  JOURNAL   Exp Cell Res 399 (2), 112471 (2021)
   PUBMED   33417922
  REMARK    GeneRIF: Identification of protein/mRNA network involving the
            PSORS1 locus gene CCHCR1 and the PSORS4 locus gene HAX1.
REFERENCE   6  (residues 1 to 871)
  AUTHORS   Xu,Y.C., Wu,R.F., Gu,Y., Yang,Y.S., Yang,M.C., Nwariaku,F.E. and
            Terada,L.S.
  TITLE     Involvement of TRAF4 in oxidative activation of c-Jun N-terminal
            kinase
  JOURNAL   J Biol Chem 277 (31), 28051-28057 (2002)
   PUBMED   12023963
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Asumalahti,K., Veal,C., Laitinen,T., Suomela,S., Allen,M.,
            Elomaa,O., Moser,M., de Cid,R., Ripatti,S., Vorechovsky,I.,
            Marcusson,J.A., Nakagawa,H., Lazaro,C., Estivill,X., Capon,F.,
            Novelli,G., Saarialho-Kere,U., Barker,J., Trembath,R. and Kere,J.
  CONSRTM   Psoriasis Consortium
  TITLE     Coding haplotype analysis supports HCR as the putative
            susceptibility gene for psoriasis at the MHC PSORS1 locus
  JOURNAL   Hum Mol Genet 11 (5), 589-597 (2002)
   PUBMED   11875053
REFERENCE   8  (residues 1 to 871)
  AUTHORS   O'Brien,K.P., Holm,S.J., Nilsson,S., Carlen,L., Rosenmuller,T.,
            Enerback,C., Inerot,A. and Stahle-Backdahl,M.
  TITLE     The HCR gene on 6p21 is unlikely to be a psoriasis susceptibility
            gene
  JOURNAL   J Invest Dermatol 116 (5), 750-754 (2001)
   PUBMED   11348465
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 871)
  AUTHORS   Asumalahti,K., Laitinen,T., Itkonen-Vatjus,R., Lokki,M.L.,
            Suomela,S., Snellman,E., Saarialho-Kere,U. and Kere,J.
  TITLE     A candidate gene for psoriasis near HLA-C, HCR (Pg8), is highly
            polymorphic with a disease-associated susceptibility allele
  JOURNAL   Hum Mol Genet 9 (10), 1533-1542 (2000)
   PUBMED   10888604
  REMARK    Erratum:[Hum Mol Genet 2001 Feb 1;10(3):301]
REFERENCE   10 (residues 1 to 871)
  AUTHORS   Oka,A., Tamiya,G., Tomizawa,M., Ota,M., Katsuyama,Y., Makino,S.,
            Shiina,T., Yoshitome,M., Iizuka,M., Sasao,Y., Iwashita,K.,
            Kawakubo,Y., Sugai,J., Ozawa,A., Ohkido,M., Kimura,M., Bahram,S.
            and Inoko,H.
  TITLE     Association analysis using refined microsatellite markers localizes
            a susceptibility locus for psoriasis vulgaris within a 111 kb
            segment telomeric to the HLA-C gene
  JOURNAL   Hum Mol Genet 8 (12), 2165-2170 (1999)
   PUBMED   10545595
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL662844.12.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein with five coiled-coil
            alpha-helical rod domains that is thought to act as a regulator of
            mRNA metabolism through its interaction with mRNA-decapping protein
            4. It localizes to P-bodies, the site of mRNA metabolism, with an
            N-terminus that is required for this subcellular localization,
            suggesting it is a P-body component. Naturally occurring mutations
            in this gene are associated with psoriasis. [provided by RefSeq,
            May 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB112475.1, BC110535.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: locus in the vicinity of
                                      disease-associated variant(s)
            MANE Ensembl match     :: ENST00000396268.8/ ENSP00000379566.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..871
                     /product="coiled-coil alpha-helical rod protein 1 isoform
                     1"
                     /note="HCR (a-helix coiled-coil rod homologue);
                     StAR-binding protein; putative gene 8 protein;
                     alpha-helical coiled-coil rod protein"
                     /calculated_mol_wt=98876
     Region          116..862
                     /region_name="HCR"
                     /note="Alpha helical coiled-coil rod protein (HCR);
                     pfam07111"
                     /db_xref="CDD:284517"
     CDS             1..871
                     /gene="CCHCR1"
                     /gene_synonym="C6orf18; HCR; pg8; SBP"
                     /coded_by="NM_001105564.2:203..2818"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43445.1"
                     /db_xref="GeneID:54535"
                     /db_xref="HGNC:HGNC:13930"
                     /db_xref="MIM:605310"
ORIGIN      
        1 mwphsagarp wastltgkdp rvmacwcldg lpsglaepwr elwrwrsrpl hcvppfspla
       61 rssrdhrnlr rrgnidgwrq nlepsnnvem fppsgstgli ppshfqarpl stlprmaptw
      121 lsdiplvqpp ghqdvserrl dtqrpqvtmw erdvssdrqe pgrrgrswgl egsqalsqqa
      181 evivrqlqel rrleeevrll retslqqkmr leaqamelea laraekagra eaeglraala
      241 gaevvrknle egsqreleev qrlhqeqlss ltqaheeals sltskaegle kslssletrr
      301 ageakelaea qreaellrkq lsktqedlea qvtlvenlrk yvgeqvpsev hsqtwelerq
      361 klletmqhlq edrdslhata ellqvrvqsl thilalqeee ltrkvqpsds lepeftrkcq
      421 sllnrwrekv falmvqlkaq elehsdsvkq lkgqvaslqe kvtsqsqeqa ilqrslqdka
      481 aevevermga kglqlelsra qearrrwqqq tasaeeqlrl vvnavsssqi wlettmakve
      541 gaaaqlpsln nrlsyavrkv htirgliark lalaqlrqes cplpppvtdv slelqqlree
      601 rnrldaelql sarliqqevg rareqgeaer qqlskvaqql eqelqqtqes laslglqlev
      661 arqgqqeste eaaslrqelt qqqelygqal qekvaevetr lreqlsdter rlnearreha
      721 kavvslrqiq rraaqekers qelrrlqeea rkeegqrlar rlqelerdkn lmlatlqqeg
      781 llsrykqqrl ltvlpslldk kksvvssprp pecsasapva aavptresik gslsvllddl
      841 qdlseaiske eavcqgdnld rcsssnpqms s
//
LOCUS       NP_002030                694 aa            linear   PRI 21-NOV-2025
DEFINITION  GRB2-associated-binding protein 1 isoform b [Homo sapiens].
ACCESSION   NP_002030
VERSION     NP_002030.2
DBSOURCE    REFSEQ: accession NM_002039.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Nam,D.E., Park,S.J., Omole,S., Um,E., Hakami,R.M. and Hahn,Y.S.
  TITLE     Activated Gab1 drives hepatocyte proliferation and anti-apoptosis
            in liver fibrosis via potential involvement of the HGF/c-Met
            signaling axis
  JOURNAL   PLoS One 19 (6), e0306345 (2024)
   PUBMED   38935609
  REMARK    GeneRIF: Activated Gab1 drives hepatocyte proliferation and
            anti-apoptosis in liver fibrosis via potential involvement of the
            HGF/c-Met signaling axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Zhang,Y., Liu,J., Zhi,Y., You,X. and Wei,B.
  TITLE     Association of GAB1 gene with asthma susceptibility and the
            efficacy of inhaled corticosteroids in children
  JOURNAL   BMC Pulm Med 23 (1), 493 (2023)
   PUBMED   38057792
  REMARK    GeneRIF: Association of GAB1 gene with asthma susceptibility and
            the efficacy of inhaled corticosteroids in children.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 694)
  AUTHORS   Boetto,J., Bielle,F., Tran,S., Marijon,P., Peyre,M., Rigau,V. and
            Kalamarides,M.
  TITLE     GAB1 as a Marker of Recurrence in Anterior Skull Base Meningioma
  JOURNAL   Neurosurgery 92 (2), 391-397 (2023)
   PUBMED   36637273
  REMARK    GeneRIF: GAB1 as a Marker of Recurrence in Anterior Skull Base
            Meningioma.
REFERENCE   5  (residues 1 to 694)
  AUTHORS   Chen,J., Kang,Z., Li,S., Wang,C., Zheng,X., Cai,Z., Pan,L., Chen,F.
            and Li,W.
  TITLE     Molecular profile reveals immune-associated markers of
            medulloblastoma for different subtypes
  JOURNAL   Front Immunol 13, 911260 (2022)
   PUBMED   35967388
  REMARK    GeneRIF: Molecular profile reveals immune-associated markers of
            medulloblastoma for different subtypes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 694)
  AUTHORS   Holgado-Madruga,M., Moscatello,D.K., Emlet,D.R., Dieterich,R. and
            Wong,A.J.
  TITLE     Grb2-associated binder-1 mediates phosphatidylinositol 3-kinase
            activation and the promotion of cell survival by nerve growth
            factor
  JOURNAL   Proc Natl Acad Sci U S A 94 (23), 12419-12424 (1997)
   PUBMED   9356464
REFERENCE   7  (residues 1 to 694)
  AUTHORS   Nguyen,L., Holgado-Madruga,M., Maroun,C., Fixman,E.D., Kamikura,D.,
            Fournier,T., Charest,A., Tremblay,M.L., Wong,A.J. and Park,M.
  TITLE     Association of the multisubstrate docking protein Gab1 with the
            hepatocyte growth factor receptor requires a functional Grb2
            binding site involving tyrosine 1356
  JOURNAL   J Biol Chem 272 (33), 20811-20819 (1997)
   PUBMED   9252406
REFERENCE   8  (residues 1 to 694)
  AUTHORS   Fixman,E.D., Holgado-Madruga,M., Nguyen,L., Kamikura,D.M.,
            Fournier,T.M., Wong,A.J. and Park,M.
  TITLE     Efficient cellular transformation by the Met oncoprotein requires a
            functional Grb2 binding site and correlates with phosphorylation of
            the Grb2-associated proteins, Cbl and Gab1
  JOURNAL   J Biol Chem 272 (32), 20167-20172 (1997)
   PUBMED   9242692
REFERENCE   9  (residues 1 to 694)
  AUTHORS   Kanai,M., Goke,M., Tsunekawa,S. and Podolsky,D.K.
  TITLE     Signal transduction pathway of human fibroblast growth factor
            receptor 3. Identification of a novel 66-kDa phosphoprotein
  JOURNAL   J Biol Chem 272 (10), 6621-6628 (1997)
   PUBMED   9045692
REFERENCE   10 (residues 1 to 694)
  AUTHORS   Holgado-Madruga,M., Emlet,D.R., Moscatello,D.K., Godwin,A.K. and
            Wong,A.J.
  TITLE     A Grb2-associated docking protein in EGF- and insulin-receptor
            signalling
  JOURNAL   Nature 379 (6565), 560-564 (1996)
   PUBMED   8596638
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA109618.1, AK289767.1,
            AK022142.1, DA249555.1, AC104685.2, BC030115.1 and AL049449.1.
            
            On Apr 14, 2004 this sequence version replaced NP_002030.1.
            
            Summary: The protein encoded by this gene is a member of the
            IRS1-like multisubstrate docking protein family. It is an important
            mediator of branching tubulogenesis and plays a central role in
            cellular growth response, transformation and apoptosis. Two
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Transcript Variant: This variant (2) lacks an in-frame coding exon
            compared to variant 1, resulting in a shorter isoform (b) with the
            same N- and C-termini, but missing a 30 aa protein segment compared
            to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.48357.1,
                                           SRR1660809.95651.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262994.9/ ENSP00000262994.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.21"
     Protein         1..694
                     /product="GRB2-associated-binding protein 1 isoform b"
                     /note="GRB2-associated binder 1; growth factor receptor
                     bound protein 2-associated protein 1; deafness, autosomal
                     recessive 26"
                     /calculated_mol_wt=76485
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q13480.2)"
     Region          3..125
                     /region_name="PH_Gab1_Gab2"
                     /note="Grb2-associated binding proteins 1 and 2 pleckstrin
                     homology (PH) domain; cd01266"
                     /db_xref="CDD:241297"
     Region          122..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13480.2)"
     Region          194..231
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13480.2)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13480.2)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13480.2)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13480.2)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13480.2)"
     Region          323..386
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13480.2)"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13480.2)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13480.2)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYY0; propagated from
                     UniProtKB/Swiss-Prot (Q13480.2)"
     Region          493..532
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13480.2)"
     Region          544..656
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13480.2)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13480.2)"
     Site            627
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q13480.2)"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13480.2)"
     Site            651
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13480.2)"
     Site            659
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13480.2)"
     Region          671..694
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13480.2)"
     Site            683
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13480.2)"
     CDS             1..694
                     /gene="GAB1"
                     /gene_synonym="DFNB26"
                     /coded_by="NM_002039.4:314..2398"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3759.1"
                     /db_xref="GeneID:2549"
                     /db_xref="HGNC:HGNC:4066"
                     /db_xref="MIM:604439"
ORIGIN      
        1 msggevvcsg wlrksppekk lkryawkrrw fvlrsgrltg dpdvleyykn dhakkpirii
       61 dlnlcqqvda gltfnkkefe nsyifdinti drifylvads eeemnkwvrc icdicgfnpt
      121 eedpvkppgs slqapadlpl aintappstq adsssatlpp pyqlinvpph letlgiqedp
      181 qdylllincq skkpeptrth adsakstsse tdcndnvpsh knpassqskh gmngffqqqm
      241 iydsppsrap sasvdsslyn lprsyshdvl pkvspsstea dgelyvfntp sgtssvetqm
      301 rhvsisydip ptpgntyqip rtfpegtlgq tskldtipdi ppprppkphp ahdrspvetc
      361 siprtasdtd ssyciptagm spsrsntist vdlnklrkda ssqdcydipr afpsdrsssl
      421 egfhnhfkvk nvltvgsvss eeldenyvpm npnspprqhs ssftepiqea nyvpmtpgtf
      481 dfssfgmqvp ppahmgfrss pktpprrpvp vadcepppvd rnlkpdrkvk papleikplp
      541 eweelqapvr spitrsfard ssrfpmsprp dsvhsttsss dshdseenyv pmnpnlssed
      601 pnlfgsnsld ggsspmikpk gdkqveyldl dldsgkstpp rkqkssgsgs svadervdyv
      661 vvdqqktlal kstreawtdg rqstesetpa ksvk
//
LOCUS       NP_059431                400 aa            linear   PRI 21-NOV-2025
DEFINITION  cytohesin-2 isoform 1 [Homo sapiens].
ACCESSION   NP_059431
VERSION     NP_059431.1
DBSOURCE    REFSEQ: accession NM_017457.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Viegas,A., Yin,D.M., Borggrafe,J., Viennet,T., Falke,M.,
            Schmitz,A., Famulok,M. and Etzkorn,M.
  TITLE     Molecular Architecture of a Network of Potential Intracellular EGFR
            Modulators: ARNO, CaM, Phospholipids, and the Juxtamembrane Segment
  JOURNAL   Structure 28 (1), 54-62 (2020)
   PUBMED   31780432
  REMARK    GeneRIF: Molecular Architecture of a Network of Potential
            Intracellular EGFR Modulators: ARNO, CaM, Phospholipids, and the
            Juxtamembrane Segment.
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Manzanillo,P., Mouchess,M., Ota,N., Dai,B., Ichikawa,R., Wuster,A.,
            Haley,B., Alvarado,G., Kwon,Y., Caothien,R., Roose-Girma,M.,
            Warming,S., McKenzie,B.S., Keir,M.E., Scherl,A., Ouyang,W. and
            Yi,T.
  TITLE     Inflammatory Bowel Disease Susceptibility Gene C1ORF106 Regulates
            Intestinal Epithelial Permeability
  JOURNAL   Immunohorizons 2 (5), 164-171 (2018)
   PUBMED   31022698
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 400)
  AUTHORS   Mossessova,E., Gulbis,J.M. and Goldberg,J.
  TITLE     Structure of the guanine nucleotide exchange factor Sec7 domain of
            human arno and analysis of the interaction with ARF GTPase
  JOURNAL   Cell 92 (3), 415-423 (1998)
   PUBMED   9476900
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Frank,S., Upender,S., Hansen,S.H. and Casanova,J.E.
  TITLE     ARNO is a guanine nucleotide exchange factor for ADP-ribosylation
            factor 6
  JOURNAL   J Biol Chem 273 (1), 23-27 (1998)
   PUBMED   9417041
REFERENCE   8  (residues 1 to 400)
  AUTHORS   Meacci,E., Tsai,S.C., Adamik,R., Moss,J. and Vaughan,M.
  TITLE     Cytohesin-1, a cytosolic guanine nucleotide-exchange protein for
            ADP-ribosylation factor
  JOURNAL   Proc Natl Acad Sci U S A 94 (5), 1745-1748 (1997)
   PUBMED   9050849
REFERENCE   9  (residues 1 to 400)
  AUTHORS   Chardin,P., Paris,S., Antonny,B., Robineau,S., Beraud-Dufour,S.,
            Jackson,C.L. and Chabre,M.
  TITLE     A human exchange factor for ARF contains Sec7- and
            pleckstrin-homology domains
  JOURNAL   Nature 384 (6608), 481-484 (1996)
   PUBMED   8945478
REFERENCE   10 (residues 1 to 400)
  AUTHORS   Kolanus,W., Nagel,W., Schiller,B., Zeitlmann,L., Godar,S.,
            Stockinger,H. and Seed,B.
  TITLE     Alpha L beta 2 integrin/LFA-1 binding to ICAM-1 induced by
            cytohesin-1, a cytoplasmic regulatory molecule
  JOURNAL   Cell 86 (2), 233-242 (1996)
   PUBMED   8706128
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC038713.1, AC008403.8 and
            BC012771.2.
            
            Summary: The protein encoded by this gene is a member of the PSCD
            family. Members of this family have identical structural
            organization that consists of an N-terminal coiled-coil motif, a
            central Sec7 domain, and a C-terminal pleckstrin homology (PH)
            domain. The coiled-coil motif is involved in homodimerization, the
            Sec7 domain contains guanine-nucleotide exchange protein (GEP)
            activity, and the PH domain interacts with phospholipids and is
            responsible for association of PSCDs with membranes. Members of
            this family appear to mediate the regulation of protein sorting and
            membrane trafficking. The encoded protein exhibits GEP activity in
            vitro with ARF1, ARF3, and ARF6 and is 83% homologous to CYTH1. Two
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC038713.1, AK292405.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..400
                     /product="cytohesin-2 isoform 1"
                     /note="pleckstrin homology, Sec7 and coiled/coil domains 2
                     (cytohesin-2); ARF nucleotide-binding site opener; ARF
                     exchange factor; PH, SEC7 and coiled-coil
                     domain-containing protein 2; pleckstrin homology, Sec7 and
                     coiled-coil domains 2; CTC-273B12.8"
                     /calculated_mol_wt=46415
     Region          61..243
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          258..378
                     /region_name="PH_GRP1-like"
                     /note="General Receptor for Phosphoinositides-1-like
                     Pleckstrin homology (PH) domain; cd01252"
                     /db_xref="CDD:269954"
     Site            order(258,286,288,290,300,303,305,336..338,340,343..348,
                     378)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:269954"
     Site            order(268,271,276,278,280,291,301,339,350..351)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269954"
     Region          387..395
                     /region_name="C-terminal autoinhibitory region.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99418.2)"
     CDS             1..400
                     /gene="CYTH2"
                     /gene_synonym="ARNO; CTS18; CTS18.1; cytohesin-2; PSCD2;
                     PSCD2L; SEC7L; Sec7p-L; Sec7p-like"
                     /coded_by="NM_017457.6:140..1342"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS86786.1"
                     /db_xref="GeneID:9266"
                     /db_xref="HGNC:HGNC:9502"
                     /db_xref="MIM:602488"
ORIGIN      
        1 medgvyeppd ltpeermele nirrrkqell veiqrlreel seamsevegl eanegsktlq
       61 rnrkmamgrk kfnmdpkkgi qflvenellq ntpeeiarfl ykgeglnkta igdylgeree
      121 lnlavlhafv dlheftdlnl vqalrqflws frlpgeaqki drmmeafaqr yclcnpgvfq
      181 stdtcyvlsf avimlntslh npnvrdkpgl erfvamnrgi neggdlpeel lrnlydsirn
      241 epfkipeddg ndlthtffnp dregwllklg ggrvktwkrr wfiltdncly yfeyttdkep
      301 rgiiplenls irevddprkp ncfelyipnn kgqlikackt eadgrvvegn hmvyrisapt
      361 qeekdewiks iqaavsvdpf yemlaarkkr isvkkkqeqp
//
LOCUS       NP_001269705             924 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase I subunit RPA2 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001269705 XP_005263874
VERSION     NP_001269705.1
DBSOURCE    REFSEQ: accession NM_001282776.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Ford,B.L., Wei,T., Liu,H., Scull,C.E., Najmi,S.M., Pitts,S.,
            Fan,W., Schneider,D.A. and Laiho,M.
  TITLE     Expression of RNA polymerase I catalytic core is influenced by
            RPA12
  JOURNAL   PLoS One 18 (5), e0285660 (2023)
   PUBMED   37167337
  REMARK    GeneRIF: Expression of RNA polymerase I catalytic core is
            influenced by RPA12.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 924)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 924)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   5  (residues 1 to 924)
  AUTHORS   Zhao,D., Liu,W., Chen,K., Wu,Z., Yang,H. and Xu,Y.
  TITLE     Structure of the human RNA polymerase I elongation complex
  JOURNAL   Cell Discov 7 (1), 97 (2021)
   PUBMED   34671025
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 924)
  AUTHORS   Miller,G., Panov,K.I., Friedrich,J.K., Trinkle-Mulcahy,L.,
            Lamond,A.I. and Zomerdijk,J.C.
  TITLE     hRRN3 is essential in the SL1-mediated recruitment of RNA
            Polymerase I to rRNA gene promoters
  JOURNAL   EMBO J 20 (6), 1373-1382 (2001)
   PUBMED   11250903
REFERENCE   7  (residues 1 to 924)
  AUTHORS   Jansa,P., Mason,S.W., Hoffmann-Rohrer,U. and Grummt,I.
  TITLE     Cloning and functional characterization of PTRF, a novel protein
            which induces dissociation of paused ternary transcription
            complexes
  JOURNAL   EMBO J 17 (10), 2855-2864 (1998)
   PUBMED   9582279
REFERENCE   8  (residues 1 to 924)
  AUTHORS   Seither,P., Zatsepina,O., Hoffmann,M. and Grummt,I.
  TITLE     Constitutive and strong association of PAF53 with RNA polymerase I
  JOURNAL   Chromosoma 106 (4), 216-225 (1997)
   PUBMED   9254723
REFERENCE   9  (residues 1 to 924)
  AUTHORS   Seither,P. and Grummt,I.
  TITLE     Molecular cloning of RPA2, the gene encoding the second largest
            subunit of mouse RNA polymerase I
  JOURNAL   Genomics 37 (1), 135-139 (1996)
   PUBMED   8921381
REFERENCE   10 (residues 1 to 924)
  AUTHORS   Barbosa,M., Jabs,E.W. and Huston,S.
  TITLE     Treacher Collins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301704
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012442.7.
            
            On Sep 19, 2013 this sequence version replaced XP_005263874.1.
            
            Summary: Eukaryotic RNA polymerase I (pol I) is responsible for the
            transcription of ribosomal RNA (rRNA) genes and production of rRNA,
            the primary component of ribosomes. Pol I is a multisubunit enzyme
            composed of 6 to 14 polypeptides, depending on the species. Most of
            the mass of the pol I complex derives from the 2 largest subunits,
            Rpa1 and Rpa2 in yeast. POLR1B is homologous to Rpa2 (Seither and
            Grummt, 1996 [PubMed 8921381]).[supplied by OMIM, Mar 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.199570.1, AK301178.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.1"
     Protein         1..924
                     /product="DNA-directed RNA polymerase I subunit RPA2
                     isoform 5"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerase I subunit RPA2;
                     DNA-directed RNA polymerase I 135kDa polypeptide; RNA
                     polymerase I subunit 2; DNA-directed RNA polymerase I 135
                     kDa polypeptide; polymerase (RNA) I polypeptide B, 128kDa;
                     polymerase (RNA) I subunit B"
                     /calculated_mol_wt=104369
     Region          <9..205
                     /region_name="RNA_pol_Rpb2_1"
                     /note="RNA polymerase beta subunit; pfam04563"
                     /db_xref="CDD:367994"
     Region          <130..922
                     /region_name="RNA_pol_B_RPB2"
                     /note="RNA polymerase beta subunit. RNA polymerases
                     catalyse the DNA dependent polymerization of RNA.
                     Prokaryotes contain a single RNA polymerase compared to
                     three in eukaryotes (not including mitochondrial. and
                     chloroplast polymerases). Each RNA polymerase...; cd00653"
                     /db_xref="CDD:238353"
     Site            order(274,276..278,280,283,288,449,467..469,471,534..537,
                     540,542..544,679,681,683,705,707,710,713,718,722,739,770,
                     778..780,782,795,798..800,802..803,824..826,830,832..833,
                     835,837..842,844..849,853,902,906,908,910..911,913,
                     915..918,920,922)
                     /site_type="other"
                     /note="RPB1 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     Region          352..410
                     /region_name="RNA_pol_Rpa2_4"
                     /note="RNA polymerase I, Rpa2 specific domain; pfam06883"
                     /db_xref="CDD:462028"
     Site            order(507..508,529,531,552,555,688,701,728..729,731,766,
                     783)
                     /site_type="other"
                     /note="RPB10 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     Site            order(540,554,687,772)
                     /site_type="other"
                     /note="RPB11 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     Site            order(554..555,559,661,663,688..690,693,695..696,771..778,
                     780)
                     /site_type="other"
                     /note="RPB3 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     Site            order(559,597,599,603..605,607)
                     /site_type="other"
                     /note="RPB12 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     CDS             1..924
                     /gene="POLR1B"
                     /gene_synonym="A135; RPA135; RPA2; Rpo1-2; TCS4"
                     /coded_by="NM_001282776.2:216..2990"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS62990.1"
                     /db_xref="GeneID:84172"
                     /db_xref="HGNC:HGNC:20454"
                     /db_xref="MIM:602000"
ORIGIN      
        1 mhcvreehsa vnmnlhylen gtvmlnfiyr kelfflplgf alkalvsfsd yqifqelikg
       61 keddsflrns vsqmlrivme egcstqkqvl nylgecfrvk lnvpdwypne qaaeflfnqc
      121 icihlksnte kfymlclmtr klfalakgec mednpdslvn qevltpgqlf lmflkekleg
      181 wlvsikiafd kkaqktsvsm ntdnlmrift mgidltkpfe ylfatgnlrs ktglgllqds
      241 glcvvadkln firylshfrc vhrgadfakm rtttvrrllp eswgflcpvh tpdgepcglm
      301 nhltavcevv tqfvytasip allcnlgvtp idgaphrsys ecypvlldgv mvgwvdkdla
      361 pgiadslrhf kvlrekripp wmevvlipmt gkpslypglf lfttpcrlvr pvqnlalgke
      421 eligtmeqif mnvaifedev fagvtthqel fphsllsvia nfipfsdhnq sprnmyqcqm
      481 gkqtmgfpll tyqdrsdnkl yrlqtpqspl vrpsmydyyd mdnypigtna ivavisytgy
      541 dmedamivnk aswergfahg svyksefidl sekikqgdss lvfgikpgdp rvlqkldddg
      601 lpfigaklqy gdpyysylnl ntgesfvmyy kskencvvdn ikvcsndtgs gkfkcvcitm
      661 rvprnptigd kfasrhgqkg ilsrlwpaed mpftesgmvp dilfnphgfp srmtigmlie
      721 smagksaalh glchdatpfi fseensaley fgemlkaagy nfygterlys gisglelead
      781 ifigvvyyqr lrhmvsdkfq vrttgardrv tnqpiggrnv qggirfgeme rdallahgts
      841 fllhdrlfnc sdrsvahvcv kcgsllspll ekpppswsam rnrkynctlc srsdtidtvs
      901 vpyvfryfva elaamnikvk ldvv
//
LOCUS       NP_001284362             348 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein transferase MAEA isoform 6 [Homo sapiens].
ACCESSION   NP_001284362
VERSION     NP_001284362.1
DBSOURCE    REFSEQ: accession NM_001297433.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Zhou,P., Peng,X., Tang,S., Zhang,K., Tan,Z., Li,D., Shen,L.,
            Peng,J. and Yang,L.
  TITLE     E3 ligase MAEA-mediated ubiquitination and degradation of PHD3
            promotes glioblastoma progression
  JOURNAL   Oncogene 42 (16), 1308-1320 (2023)
   PUBMED   36882523
  REMARK    GeneRIF: E3 ligase MAEA-mediated ubiquitination and degradation of
            PHD3 promotes glioblastoma progression.
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Maitland,M.E.R., Lajoie,G.A., Shaw,G.S. and Schild-Poulter,C.
  TITLE     Structural and Functional Insights into GID/CTLH E3 Ligase
            Complexes
  JOURNAL   Int J Mol Sci 23 (11), 5863 (2022)
   PUBMED   35682545
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Imamura,M., Maeda,S., Yamauchi,T., Hara,K., Yasuda,K., Morizono,T.,
            Takahashi,A., Horikoshi,M., Nakamura,M., Fujita,H., Tsunoda,T.,
            Kubo,M., Watada,H., Maegawa,H., Okada-Iwabu,M., Iwabu,M.,
            Shojima,N., Ohshige,T., Omori,S., Iwata,M., Hirose,H., Kaku,K.,
            Ito,C., Tanaka,Y., Tobe,K., Kashiwagi,A., Kawamori,R., Kasuga,M.,
            Kamatani,N., Nakamura,Y. and Kadowaki,T.
  CONSRTM   Diabetes Genetics Replication and Meta-analysis (DIAGRAM)
            Consortium
  TITLE     A single-nucleotide polymorphism in ANK1 is associated with
            susceptibility to type 2 diabetes in Japanese populations
  JOURNAL   Hum Mol Genet 21 (13), 3042-3049 (2012)
   PUBMED   22456796
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Cho,Y.S., Chen,C.H., Hu,C., Long,J., Ong,R.T., Sim,X., Takeuchi,F.,
            Wu,Y., Go,M.J., Yamauchi,T., Chang,Y.C., Kwak,S.H., Ma,R.C.,
            Yamamoto,K., Adair,L.S., Aung,T., Cai,Q., Chang,L.C., Chen,Y.T.,
            Gao,Y., Hu,F.B., Kim,H.L., Kim,S., Kim,Y.J., Lee,J.J., Lee,N.R.,
            Li,Y., Liu,J.J., Lu,W., Nakamura,J., Nakashima,E., Ng,D.P.,
            Tay,W.T., Tsai,F.J., Wong,T.Y., Yokota,M., Zheng,W., Zhang,R.,
            Wang,C., So,W.Y., Ohnaka,K., Ikegami,H., Hara,K., Cho,Y.M.,
            Cho,N.H., Chang,T.J., Bao,Y., Hedman,A.K., Morris,A.P.,
            McCarthy,M.I., Takayanagi,R., Park,K.S., Jia,W., Chuang,L.M.,
            Chan,J.C., Maeda,S., Kadowaki,T., Lee,J.Y., Wu,J.Y., Teo,Y.Y.,
            Tai,E.S., Shu,X.O., Mohlke,K.L., Kato,N., Han,B.G. and Seielstad,M.
  CONSRTM   DIAGRAM Consortium; MuTHER Consortium
  TITLE     Meta-analysis of genome-wide association studies identifies eight
            new loci for type 2 diabetes in east Asians
  JOURNAL   Nat Genet 44 (1), 67-72 (2011)
   PUBMED   22158537
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 348)
  AUTHORS   Kobayashi,N., Yang,J., Ueda,A., Suzuki,T., Tomaru,K., Takeno,M.,
            Okuda,K. and Ishigatsubo,Y.
  TITLE     RanBPM, Muskelin, p48EMLP, p44CTLH, and the armadillo-repeat
            proteins ARMC8alpha and ARMC8beta are components of the CTLH
            complex
  JOURNAL   Gene 396 (2), 236-247 (2007)
   PUBMED   17467196
  REMARK    GeneRIF: RanBPM, ARMC8alpha, ARMC8beta, Muskelin, p48EMLP, and
            p44CTLH form complexes in cells.
REFERENCE   9  (residues 1 to 348)
  AUTHORS   Bala,S., Kumar,A., Soni,S., Sinha,S. and Hanspal,M.
  TITLE     Emp is a component of the nuclear matrix of mammalian cells and
            undergoes dynamic rearrangements during cell division
  JOURNAL   Biochem Biophys Res Commun 342 (4), 1040-1048 (2006)
   PUBMED   16510120
  REMARK    GeneRIF: These results suggest that Emp undergoes dynamic
            rearrangements within the nuclear architecture that are correlated
            with cell division.
REFERENCE   10 (residues 1 to 348)
  AUTHORS   Hanspal,M., Smockova,Y. and Uong,Q.
  TITLE     Molecular identification and functional characterization of a novel
            protein that mediates the attachment of erythroblasts to
            macrophages
  JOURNAL   Blood 92 (8), 2940-2950 (1998)
   PUBMED   9763581
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078852.5, DC299400.1,
            AK298944.1, AK091951.1 and BU607457.1.
            
            Summary: This gene encodes a protein that mediates the attachment
            of erythroblasts to macrophages. This attachment promotes terminal
            maturation and enucleation of erythroblasts, presumably by
            suppressing apoptosis. The encoded protein is an integral membrane
            protein with the N-terminus on the extracellular side and the
            C-terminus on the cytoplasmic side of the cell. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jul 2014].
            
            Transcript Variant: This variant (6) differs in the 5' UTR, lacks
            part of the 5' coding region, and uses a downstream start codon,
            compared to variant 1. The encoded isoform (6) has a shorter
            N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK298944.1, SRR14038195.2689429.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..348
                     /product="E3 ubiquitin-protein transferase MAEA isoform 6"
                     /EC_number="2.3.2.27"
                     /note="erythroblast macrophage protein; GID complex
                     subunit 9, FYV10 homolog; lung cancer-related protein 10;
                     human lung cancer oncogene 10 protein; cell
                     proliferation-inducing gene 5 protein; E3
                     ubiquitin-protein transferase MAEA"
                     /calculated_mol_wt=39651
     Region          72..105
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          112..253
                     /region_name="CTLH"
                     /note="CTLH/CRA C-terminal to LisH motif domain;
                     pfam10607"
                     /db_xref="CDD:402305"
     Region          288..337
                     /region_name="RING-Ubox_Emp"
                     /note="U-box domain, a modified RING finger, found in
                     erythroblast macrophage protein (Emp) and similar
                     proteins; cd16659"
                     /db_xref="CDD:438321"
     CDS             1..348
                     /gene="MAEA"
                     /gene_synonym="EMLP; EMP; GID9; HLC-10; P44EMLP; PIG5"
                     /coded_by="NM_001297433.2:286..1332"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS77888.1"
                     /db_xref="GeneID:10296"
                     /db_xref="HGNC:HGNC:13731"
                     /db_xref="MIM:606801"
ORIGIN      
        1 mvvaelektl sgcpavdsvv slldgvvekl svlkrkaves iqaedesakl ckrriehlke
       61 hssdqpaaas vwkrkrmdrm mvehllrcgy yntavklarq sgiedlvnie mfltakevee
      121 slerretatc lawchdnksr lrkmksclef slriqefiel irqnkrldav rharkhfsqa
      181 egsqldevrq amgmlafppd thispykdll dparwrmliq qfrydnyrlh qlgnnsvftl
      241 tlqaglsaik tpqcykedgs skspdcpvcs rslnklaqpl pmahcansrl vckisgdvmn
      301 ennppmmlpn gyvygynsll sirqddkvvc prtkevfhfs qaekvyim
//
LOCUS       NP_001123628             243 aa            linear   PRI 21-NOV-2025
DEFINITION  myeloid leukemia factor 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001123628
VERSION     NP_001123628.1
DBSOURCE    REFSEQ: accession NM_001130156.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Tang,Z., Yang,Y., Chen,W. and Liang,T.
  TITLE     Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling
  JOURNAL   Hepatol Commun 7 (8), e0204 (2023)
   PUBMED   37486965
  REMARK    GeneRIF: Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Huang,D., Liu,C., Sun,X., Sun,X., Qu,Y., Tang,Y., Li,G. and Tong,T.
  TITLE     CRL4DCAF8 and USP11 oppositely regulate the stability of myeloid
            leukemia factors (MLFs)
  JOURNAL   Biochem Biophys Res Commun 529 (2), 127-132 (2020)
   PUBMED   32703400
  REMARK    GeneRIF: CRL4(DCAF8) and USP11 oppositely regulate the stability of
            myeloid leukemia factors (MLFs).
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Darracq,A., Pak,H., Bourgoin,V., Zmiri,F., Dellaire,G., Affar,E.B.
            and Milot,E.
  TITLE     NPM and NPM-MLF1 interact with chromatin remodeling complexes and
            influence their recruitment to specific genes
  JOURNAL   PLoS Genet 15 (11), e1008463 (2019)
   PUBMED   31675375
  REMARK    GeneRIF: the abnormal gene regulation imposed by NPM-MLF1 can be
            characterized by the enhanced recruitment of NuRD to gene
            regulatory regions. Thus, different mechanisms would orchestrate
            the dysregulation of NPM function in NPMc+- versus
            NPM1-MLF1-associated leukemia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Yoneda-Kato,N., Tomoda,K., Umehara,M., Arata,Y. and Kato,J.Y.
  TITLE     Myeloid leukemia factor 1 regulates p53 by suppressing COP1 via
            COP9 signalosome subunit 3
  JOURNAL   EMBO J 24 (9), 1739-1749 (2005)
   PUBMED   15861129
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Hanissian,S.H., Akbar,U., Teng,B., Janjetovic,Z., Hoffmann,A.,
            Hitzler,J.K., Iscove,N., Hamre,K., Du,X., Tong,Y., Mukatira,S.,
            Robertson,J.H. and Morris,S.W.
  TITLE     cDNA cloning and characterization of a novel gene encoding the
            MLF1-interacting protein MLF1IP
  JOURNAL   Oncogene 23 (20), 3700-3707 (2004)
   PUBMED   15116101
REFERENCE   8  (residues 1 to 243)
  AUTHORS   Arber,D.A., Chang,K.L., Lyda,M.H., Bedell,V., Spielberger,R. and
            Slovak,M.L.
  TITLE     Detection of NPM/MLF1 fusion in t(3;5)-positive acute myeloid
            leukemia and myelodysplasia
  JOURNAL   Hum Pathol 34 (8), 809-813 (2003)
   PUBMED   14506644
  REMARK    GeneRIF: These findings suggest that an NPM/MLF1 fusion is the
            primary molecular abnormality in t(3;5) MDS and AML with
            multilineage dysplasia, and that cases with NPM/MLF1 may be
            clinically distinct from other MDS-associated disease
REFERENCE   9  (residues 1 to 243)
  AUTHORS   Lim,R., Winteringham,L.N., Williams,J.H., McCulloch,R.K.,
            Ingley,E., Tiao,J.Y., Lalonde,J.P., Tsai,S., Tilbrook,P.A., Sun,Y.,
            Wu,X., Morris,S.W. and Klinken,S.P.
  TITLE     MADM, a novel adaptor protein that mediates phosphorylation of the
            14-3-3 binding site of myeloid leukemia factor 1
  JOURNAL   J Biol Chem 277 (43), 40997-41008 (2002)
   PUBMED   12176995
  REMARK    GeneRIF: phosphorylation of 14-3-3 binding site by MADM
REFERENCE   10 (residues 1 to 243)
  AUTHORS   Yoneda-Kato,N., Look,A.T., Kirstein,M.N., Valentine,M.B.,
            Raimondi,S.C., Cohen,K.J., Carroll,A.J. and Morris,S.W.
  TITLE     The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid
            leukemia produces a novel fusion gene, NPM-MLF1
  JOURNAL   Oncogene 12 (2), 265-275 (1996)
   PUBMED   8570204
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB455518.1, AY848702.1 and
            BX647666.1.
            
            Summary: This gene encodes an oncoprotein which is thought to play
            a role in the phenotypic determination of hemopoetic cells.
            Translocations between this gene and nucleophosmin have been
            associated with myelodysplastic syndrome and acute myeloid
            leukemia. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY848702.1, SRR1803616.189573.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.32"
     Protein         1..243
                     /product="myeloid leukemia factor 1 isoform 2"
                     /note="myelodysplasia-myeloid leukemia factor 1; testis
                     tissue sperm-binding protein Li 49e"
                     /calculated_mol_wt=27494
     Region          1..177
                     /region_name="Mlf1IP"
                     /note="Myelodysplasia-myeloid leukemia factor
                     1-interacting protein; pfam10248"
                     /db_xref="CDD:463022"
     CDS             1..243
                     /gene="MLF1"
                     /coded_by="NM_001130156.3:227..958"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS46945.1"
                     /db_xref="GeneID:4291"
                     /db_xref="HGNC:HGNC:7125"
                     /db_xref="MIM:601402"
ORIGIN      
        1 mrqmirsfse pfgrdllsis dgrgrahnrr ghndgedslt htdvssfqtm dqmvsnmrny
       61 mqklernfgq lsvdpnghsf csssvmtysk igdeppkvfq astqtrrapg giketrkamr
      121 dsdsglekma ighhihdrah vikksknkkt gdeevnqefi nmnesdahaf deewqsevlk
      181 ykpgrhnlgn trmrsvghen pgsrelkrre kpqqspaieh grrsnvlgdk lhikgssvks
      241 nkk
//
LOCUS       NP_004822                600 aa            linear   PRI 21-NOV-2025
DEFINITION  mediator of RNA polymerase II transcription subunit 26 [Homo
            sapiens].
ACCESSION   NP_004822
VERSION     NP_004822.2
DBSOURCE    REFSEQ: accession NM_004831.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 600)
  AUTHORS   Lens,Z., Cantrelle,F.X., Peruzzini,R., Hanoulle,X., Dewitte,F.,
            Ferreira,E., Baert,J.L., Monte,D., Aumercier,M., Villeret,V.,
            Verger,A. and Landrieu,I.
  TITLE     Solution Structure of the N-Terminal Domain of Mediator Subunit
            MED26 and Molecular Characterization of Its Interaction with EAF1
            and TAF7
  JOURNAL   J Mol Biol 429 (20), 3043-3055 (2017)
   PUBMED   28893534
  REMARK    GeneRIF: EAF1 (239-268) and TAF7 (205-235) peptide interactions
            were both mapped to the same groove formed by H3 and H4 helices of
            MED26 N-terminal domain.
REFERENCE   5  (residues 1 to 600)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 600)
  AUTHORS   Naar,A.M., Taatjes,D.J., Zhai,W., Nogales,E. and Tjian,R.
  TITLE     Human CRSP interacts with RNA polymerase II CTD and adopts a
            specific CTD-bound conformation
  JOURNAL   Genes Dev 16 (11), 1339-1344 (2002)
   PUBMED   12050112
  REMARK    GeneRIF: Human CRSP interacts with RNA polymerase II CTD and adopts
            a specific CTD-bound conformation
REFERENCE   7  (residues 1 to 600)
  AUTHORS   Mittler,G., Kremmer,E., Timmers,H.T. and Meisterernst,M.
  TITLE     Novel critical role of a human Mediator complex for basal RNA
            polymerase II transcription
  JOURNAL   EMBO Rep 2 (9), 808-813 (2001)
   PUBMED   11559591
REFERENCE   8  (residues 1 to 600)
  AUTHORS   Booth,V., Koth,C.M., Edwards,A.M. and Arrowsmith,C.H.
  TITLE     Structure of a conserved domain common to the transcription factors
            TFIIS, elongin A, and CRSP70
  JOURNAL   J Biol Chem 275 (40), 31266-31268 (2000)
   PUBMED   10811649
REFERENCE   9  (residues 1 to 600)
  AUTHORS   Naar,A.M., Beaurang,P.A., Zhou,S., Abraham,S., Solomon,W. and
            Tjian,R.
  TITLE     Composite co-activator ARC mediates chromatin-directed
            transcriptional activation
  JOURNAL   Nature 398 (6730), 828-832 (1999)
   PUBMED   10235267
REFERENCE   10 (residues 1 to 600)
  AUTHORS   Ryu,S., Zhou,S., Ladurner,A.G. and Tjian,R.
  TITLE     The transcriptional cofactor complex CRSP is required for activity
            of the enhancer-binding protein Sp1
  JOURNAL   Nature 397 (6718), 446-450 (1999)
   PUBMED   9989412
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC024075.4, AF104253.1, AK128435.1 and AC008764.9.
            
            On Feb 25, 2003 this sequence version replaced NP_004822.1.
            
            Summary: The activation of gene transcription is a multistep
            process that is triggered by factors that recognize transcriptional
            enhancer sites in DNA. These factors work with co-activators to
            direct transcriptional initiation by the RNA polymerase II
            apparatus. The protein encoded by this gene is a subunit of the
            CRSP (cofactor required for SP1 activation) complex, which, along
            with TFIID, is required for efficient activation by SP1. This
            protein is also a component of other multisubunit complexes e.g.
            thyroid hormone receptor-(TR-) associated proteins which interact
            with TR and facilitate TR function on DNA templates in conjunction
            with initiation factors and cofactors. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110430.1, SRR14038193.3020669.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263390.8/ ENSP00000263390.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..600
                     /product="mediator of RNA polymerase II transcription
                     subunit 26"
                     /note="cofactor required for Sp1 transcriptional
                     activation, subunit 7 (70kD); cofactor required for Sp1
                     transcriptional activation, subunit 7, 70kDa; ARC70; CRSP
                     complex subunit 7; transcriptional coactivator CRSP70;
                     activator-recruited cofactor 70 kDa component; cofactor
                     required for Sp1 transcriptional activation subunit 7"
                     /calculated_mol_wt=65316
     Region          12..86
                     /region_name="TFS2N"
                     /note="Domain in the N-terminus of transcription
                     elongation factor S-II (and elsewhere); smart00509"
                     /db_xref="CDD:197766"
     Site            order(17..18,21,61..62)
                     /site_type="other"
                     /note="putative RNA polymerase binding site [polypeptide
                     binding]"
                     /db_xref="CDD:238107"
     Region          99..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95402.2)"
     Region          177..417
                     /region_name="Med26_M"
                     /note="Mediator complex subunit 26 middle domain;
                     pfam15694"
                     /db_xref="CDD:464807"
     Region          348..402
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95402.2)"
     Region          419..598
                     /region_name="Med26_C"
                     /note="Mediator complex subunit 26 C-terminal; pfam15693"
                     /db_xref="CDD:464806"
     Region          431..461
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95402.2)"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95402.2)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95402.2)"
     Site            535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95402.2)"
     CDS             1..600
                     /gene="MED26"
                     /gene_synonym="CRSP7; CRSP70"
                     /coded_by="NM_004831.5:262..2064"
                     /db_xref="CCDS:CCDS12347.1"
                     /db_xref="GeneID:9441"
                     /db_xref="HGNC:HGNC:2376"
                     /db_xref="MIM:605043"
ORIGIN      
        1 mtaapaspqq irdrllqaid pqsnirnmva vlevisslek ypitkealee trlgklindv
       61 rkktkneela krakkllrsw qkliepahqh eaalrglaga tgsanggahn crpevgaagp
      121 prsihdlksr ndlqrlpgqr ldrlgsrkrr gdqrdlghpg pppkvskash dplvpnsspl
      181 ptngisgspe sfassldgsg hagpegsrle rdendkhsgk ipvnavrpht sspglgkppg
      241 pclqpkasvl qqldrvdetp gpphpkgppr csfsprnsrh egsfarqqsl yapkgsvpsp
      301 sprpqaldat qvpsplplaq pstppvrrle llpsaespvc wleqpeshqr lagpgckagl
      361 spaepllsra gfspdsskad sdaassggsd skkkkryrpr dytvnldgqv aeagvkpvrl
      421 kerkltfdpm trqikpltqk epvradspvh meqqsrteld kqeakaslqs pfeqtnwkel
      481 srneiiqsyl srqssllsss gaqtpgahhf mseylkqees trqgarqlhv lvpqspptdl
      541 pgltrevtqd dldriqasqw pgvngcqdtq gnwydwtqci sldphgddgr lnilpyvcld
//
LOCUS       NP_001371507             694 aa            linear   PRI 21-NOV-2025
DEFINITION  protein Smaug homolog 2 isoform a [Homo sapiens].
ACCESSION   NP_001371507
VERSION     NP_001371507.1
DBSOURCE    REFSEQ: accession NM_001384578.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 694)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 694)
  AUTHORS   Wu,C., Liu,X., Li,B., Sun,G., Peng,C. and Xiang,D.
  TITLE     miR-451 suppresses the malignant characteristics of colorectal
            cancer via targeting SAMD4B
  JOURNAL   Mol Med Rep 24 (2) (2021)
   PUBMED   34109425
  REMARK    GeneRIF: miR451 suppresses the malignant characteristics of
            colorectal cancer via targeting SAMD4B.
REFERENCE   6  (residues 1 to 694)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   7  (residues 1 to 694)
  AUTHORS   Baez,M.V. and Boccaccio,G.L.
  TITLE     Mammalian Smaug is a translational repressor that forms cytoplasmic
            foci similar to stress granules
  JOURNAL   J Biol Chem 280 (52), 43131-43140 (2005)
   PUBMED   16221671
REFERENCE   8  (residues 1 to 694)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   9  (residues 1 to 694)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 694)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011445.6 and AC005239.1.
            
            Transcript Variant: This variant (14) differs in the 5' UTR
            compared to variant 1. Variants 1 and 3-14 all encode the same
            isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.456579.1,
                                           SRR14038192.4053989.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..694
                     /product="protein Smaug homolog 2 isoform a"
                     /note="smaug homolog B; protein Smaug homolog 2; smaug 2;
                     SAM domain-containing protein 4B; sterile alpha motif
                     domain-containing protein 4B"
                     /calculated_mol_wt=75353
     Region          158..301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XS6; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XS6; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XS6; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Region          296..358
                     /region_name="SAM_Smaug"
                     /note="SAM domain of Smaug subfamily; cd09557"
                     /db_xref="CDD:188956"
     Site            order(312,314..315,343,346..348,355,357)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:188956"
     Region          407..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            555
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            592
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            600
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            602
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Region          607..643
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     CDS             1..694
                     /gene="SAMD4B"
                     /gene_synonym="Smaug2; SMGB"
                     /coded_by="NM_001384578.1:621..2705"
                     /note="isoform a is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS33020.1"
                     /db_xref="GeneID:55095"
                     /db_xref="HGNC:HGNC:25492"
                     /db_xref="MIM:619231"
ORIGIN      
        1 mmfrdqvgil agwfkgwnec eqtvallsll krvtrtqarf lqlclehsla dcndihlles
       61 eansaaivsq wqqeskekvv slllshlpll qpgnteakse ymrllqkvla ysiesnafie
      121 esrqllsyal ihpattledr nalalwlshl eerlasgfrs rpepsyhsrq gsdewggpae
      181 lgpgeagpgw qdkpprengh vpfhpsssvp painsigsna ntglpcqihp splkrsmsli
      241 ptspqvpgew pspeelgara afttpdhapl spqssvassg seqteeqgss rntfqedgsg
      301 mkdvpswlks lrlhkyaalf sqmsyeemmt lteqhlesqn vtkgarhkia lsiqklrerq
      361 svlkslekdv leggnlrnal qelqqiiitp ikaysvlqat vaaatttpta kdgapgeppl
      421 pgaepplahp gtdkgteakd ppavenyppp papaptdgse papapvadgd ipsqftrvmg
      481 kvctqllvsr pdeenitsyl qliekclthe aftetqkkrl lswkqqvlkl lrtfprkaal
      541 emqnyrqqkg wafgsnslpi agsvgmgvar rtqrqfpmpp ralppgrmgl lspsgiggvs
      601 prhaltspsl ggqgrqnlwf anpggsnsmp sqsrssvqrt hslpvhsspq ailmfppdcp
      661 vpgpdleinp tleslclsmt ehalgdgtdk tsti
//
LOCUS       NP_787067                250 aa            linear   PRI 21-NOV-2025
DEFINITION  ATPase SWSAP1 [Homo sapiens].
ACCESSION   NP_787067
VERSION     NP_787067.3
DBSOURCE    REFSEQ: accession NM_175871.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Hengel,S.R., Oppenheimer,K.G., Smith,C.M., Schaich,M.A., Rein,H.L.,
            Martino,J., Darrah,K.E., Witham,M., Ezekwenna,O.C., Burton,K.R.,
            Van Houten,B., Spies,M. and Bernstein,K.A.
  TITLE     The human Shu complex promotes RAD51 activity by modulating RPA
            dynamics on ssDNA
  JOURNAL   Nat Commun 15 (1), 7197 (2024)
   PUBMED   39169038
  REMARK    GeneRIF: The human Shu complex promotes RAD51 activity by
            modulating RPA dynamics on ssDNA.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Matsuzaki,K., Kondo,S., Ishikawa,T. and Shinohara,A.
  TITLE     Human RAD51 paralogue SWSAP1 fosters RAD51 filament by regulating
            the anti-recombinase FIGNL1 AAA+ ATPase
  JOURNAL   Nat Commun 10 (1), 1407 (2019)
   PUBMED   30926776
  REMARK    GeneRIF: SWSAP1 protects RAD51 filaments by antagonizing the
            anti-recombinase, FIGNL1.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 250)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   9  (residues 1 to 250)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
  REMARK    GeneRIF: the human Shu complex (hSWS1.SWSAP1) has an evolutionarily
            conserved function in homologous recombination
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC024575.6.
            
            On Aug 21, 2019 this sequence version replaced NP_787067.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU677559.1, BC068071.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000674460.1/ ENSP00000501355.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..250
                     /product="ATPase SWSAP1"
                     /note="SWS1-associated protein 1; zinc finger, SWIM-type
                     containing 7 associated protein 1; ZSWIM7-associated
                     protein 1"
                     /calculated_mol_wt=26466
     CDS             1..250
                     /gene="SWSAP1"
                     /gene_synonym="C19orf39; SWS1AP1; ZSWIM7AP1"
                     /coded_by="NM_175871.4:16..768"
                     /db_xref="CCDS:CCDS12259.2"
                     /db_xref="GeneID:126074"
                     /db_xref="HGNC:HGNC:26638"
                     /db_xref="MIM:614536"
ORIGIN      
        1 maetlrrvlt rggaawsgee nmpaagppll llgtpgsgkt allfaaalea agegqgpvlf
       61 ltrrplqsmp rgtgttldpm rlqkirfqyp pstrelfrll csaheapgpa pslllldgle
      121 eylaedpepq eaaylialll dtaahfshrl gpgrdcglmv alqtqeeags gdvlhlallq
      181 ryfpaqcwlq pdapgpgehg lraclepggl gprtewwvtf rsdgemmiap wptqagdpss
      241 gkgsssggqp
//
LOCUS       NP_001371795            1039 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 99 [Homo sapiens].
ACCESSION   NP_001371795
VERSION     NP_001371795.1
DBSOURCE    REFSEQ: accession NM_001384866.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1039)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1039)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1039)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1039)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1039)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1039)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1039)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1039)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1039)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1039)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1039
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1039
                     /product="microtubule-associated protein 4 isoform 99"
                     /note="MAP-4"
                     /calculated_mol_wt=109397
     Region          <638..>876
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Region          <818..839
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          879..908
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          910..939
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          941..971
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1039
                     /gene="MAP4"
                     /coded_by="NM_001384866.1:96..3215"
                     /note="isoform 99 is encoded by transcript variant 112"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgsp tefleekmay qeypnsqnwp
      121 edtnfcfqpe qvvdpiqtdp fkmyhdddla dlvfpssata dtsifagqnd plkdsyvple
      181 lakeiemase erppaqalei mmglkttdma psketemala kdmalatkte valakdmesp
      241 tkldvtlakd mqpsmesdma lvkdmelpte kevalvkdvr wptetdvssa knvvlptete
      301 vapakdvtll keteraspik mdlapskdmg ppkenkkete raspikmdla pskdmgppke
      361 nkivpakdlv llseievaqa ndiissteis saekvalsse tevalardmt lppetnvilt
      421 kdkalpleae vapvkdmaql peteiapakd vapstvkevg llkdmsplse temalgkdvt
      481 pppetevvli knvclppeme valtedqvpa lkteaplakd gvltlannvt pakdvpplse
      541 teatpvpikd meiaqtqkgi sedshleslq dvgqsaaptf mispetvtgt gkkcslpaee
      601 dsvleklger kpcnsqpsel ssetsgiarp eegrpvvsgt gndittppnk elppspekkt
      661 kpiadakape kraspskpas apasrsgsks tqtvakttta aavastgpss rspstllpkk
      721 ptaiktegkp aevkkmtaks vpadlsrpks tstssmkktt tlsgtapaag vvpsrvkatp
      781 mpsrpsttpf idkkptsakp ssttprlsrl atntsapdlk nvrskvgste nikhqpgggr
      841 akvekkteaa attrkpesna vtktagpias aqkqpagkvq ivskkvsysh iqskcgskdn
      901 ikhvpgggnv qiqnkkvdis kvsskcgska nikhkpgggd vkiesqklnf kekaqakvgs
      961 ldnvghlpag gavktegggs eaplcpgppa geepaiseaa peagaptsas glnghptlsg
     1021 ggdqreaqtl dsqiqetsi
//
LOCUS       NP_001317369             483 aa            linear   PRI 21-NOV-2025
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily D member 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001317369 XP_016880456
VERSION     NP_001317369.1
DBSOURCE    REFSEQ: accession NM_001330440.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Kim,M., Park,J., Bouhaddou,M., Kim,K., Rojc,A., Modak,M.,
            Soucheray,M., McGregor,M.J., O'Leary,P., Wolf,D., Stevenson,E.,
            Foo,T.K., Mitchell,D., Herrington,K.A., Munoz,D.P., Tutuncuoglu,B.,
            Chen,K.H., Zheng,F., Kreisberg,J.F., Diolaiti,M.E., Gordan,J.D.,
            Coppe,J.P., Swaney,D.L., Xia,B., van 't Veer,L., Ashworth,A.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein interaction landscape of breast cancer
  JOURNAL   Science 374 (6563), eabf3066 (2021)
   PUBMED   34591612
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Schim van der Loeff,I., Sprenkeler,E.G.G., Tool,A.T.J., Abinun,M.,
            Grainger,A., Engelhardt,K.R., van Houdt,M., Janssen,H.,
            Kuijpers,T.W. and Hambleton,S.
  TITLE     Defective neutrophil development and specific granule deficiency
            caused by a homozygous splice-site mutation in SMARCD2
  JOURNAL   J Allergy Clin Immunol 147 (6), 2381-2385 (2021)
   PUBMED   33279574
  REMARK    GeneRIF: Defective neutrophil development and specific granule
            deficiency caused by a homozygous splice-site mutation in SMARCD2.
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Yucel,E., Karakus,I.S., Krolo,A., Kiykim,A., Heredia,R.J.,
            Tamay,Z., Cipe,F.E., Karakoc-Aydiner,E., Ozen,A., Karaman,S.,
            Boztug,K. and Baris,S.
  TITLE     Novel Frameshift Autosomal Recessive Loss-of-Function Mutation in
            SMARCD2 Encoding a Chromatin Remodeling Factor Mediates
            Granulopoiesis
  JOURNAL   J Clin Immunol 41 (1), 59-65 (2021)
   PUBMED   33025377
  REMARK    GeneRIF: Novel Frameshift Autosomal Recessive Loss-of-Function
            Mutation in SMARCD2 Encoding a Chromatin Remodeling Factor Mediates
            Granulopoiesis.
            Review article
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Phelan,M.L., Sif,S., Narlikar,G.J. and Kingston,R.E.
  TITLE     Reconstitution of a core chromatin remodeling complex from SWI/SNF
            subunits
  JOURNAL   Mol Cell 3 (2), 247-253 (1999)
   PUBMED   10078207
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Ring,H.Z., Vameghi-Meyers,V., Wang,W., Crabtree,G.R. and Francke,U.
  TITLE     Five SWI/SNF-related, matrix-associated, actin-dependent regulator
            of chromatin (SMARC) genes are dispersed in the human genome
  JOURNAL   Genomics 51 (1), 140-143 (1998)
   PUBMED   9693044
REFERENCE   8  (residues 1 to 483)
  AUTHORS   Reyes,J.C., Muchardt,C. and Yaniv,M.
  TITLE     Components of the human SWI/SNF complex are enriched in active
            chromatin and are associated with the nuclear matrix
  JOURNAL   J Cell Biol 137 (2), 263-274 (1997)
   PUBMED   9128241
REFERENCE   9  (residues 1 to 483)
  AUTHORS   Wang,W., Cote,J., Xue,Y., Zhou,S., Khavari,P.A., Biggar,S.R.,
            Muchardt,C., Kalpana,G.V., Goff,S.P., Yaniv,M., Workman,J.L. and
            Crabtree,G.R.
  TITLE     Purification and biochemical heterogeneity of the mammalian SWI-SNF
            complex
  JOURNAL   EMBO J 15 (19), 5370-5382 (1996)
   PUBMED   8895581
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK303951.1, AW375602.1 and
            BQ670607.1.
            
            On Aug 29, 2016 this sequence version replaced XP_016880456.1.
            
            Summary: The protein encoded by this gene is a member of the
            SWI/SNF family of proteins, whose members display helicase and
            ATPase activities and which are thought to regulate transcription
            of certain genes by altering the chromatin structure around those
            genes. The encoded protein is part of the large ATP-dependent
            chromatin remodeling complex SNF/SWI and has sequence similarity to
            the yeast Swp73 protein. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303951.1, SRR14038194.4498145.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.3"
     Protein         1..483
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily D member
                     2 isoform 3"
                     /note="mammalian chromatin remodeling complex
                     BRG1-associated factor 60B; Swp73-like protein; chromatin
                     remodeling complex BAF60B subunit; SWI/SNF complex 60 kDa
                     subunit B; SWI/SNF related, matrix associated, actin
                     dependent regulator of chromatin, subfamily d, member 2;
                     SWI/SNF-related matrix-associated actin-dependent
                     regulator of chromatin subfamily D member 2; 60 kDa
                     BRG-1/Brm-associated factor subunit B"
                     /calculated_mol_wt=55108
     Region          10..>100
                     /region_name="PHA03201"
                     /note="uracil DNA glycosylase; Provisional"
                     /db_xref="CDD:165468"
     Region          259..338
                     /region_name="SWIB_BAF60B"
                     /note="SWIB domain found in BRG1-associated factor 60B
                     (BAF60B) and similar proteins; cd17675"
                     /db_xref="CDD:349494"
     Site            order(281,284..285,287..288,291..292,297,302..303,305,322,
                     325..326)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349494"
     CDS             1..483
                     /gene="SMARCD2"
                     /gene_synonym="BAF60B; CRACD2; PRO2451; Rsc6p; SGD2"
                     /coded_by="NM_001330440.2:48..1499"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82188.1"
                     /db_xref="GeneID:6603"
                     /db_xref="HGNC:HGNC:11107"
                     /db_xref="MIM:601736"
ORIGIN      
        1 mgrrvgvevt prwapqkcqg arpqrpgmsp gnrmpmaglq vgppagspfg aaaplrpgmp
       61 ptmmdpfrkr llvpqaqppm paqrrglkrr kmadkvlpqr irelvpesqa ymdllaferk
      121 ldqtiarkrm eiqeaikkpl tqkrklriyi sntfspskae gdsagtagtp ggtpagdkva
      181 swelrvegkl lddpskqkrk fssffkslvi eldkelygpd nhlvewhrmp ttqetdgfqv
      241 krpgdlnvkc tlllmldhqp pqykldprla rllgvhtqtr aaimqalwly ikhnqlqdgh
      301 ereyincnry frqifscgrl rfseipmkla gllqhpdpiv inhvisvdpn dqkktacydi
      361 dvevddplka qmsnflastt nqqeiasldv kihetiesin qlktqrdfml sfstdpqdfi
      421 qewlrsqrrd lkiitdvign peeerraafy hqpwaqeavg rhifakvqqr rqeleqvlgi
      481 rlt
//
LOCUS       NP_001381874             449 aa            linear   PRI 21-NOV-2025
DEFINITION  leucine zipper putative tumor suppressor 2 isoform b [Homo
            sapiens].
ACCESSION   NP_001381874 XP_016872270
VERSION     NP_001381874.1
DBSOURCE    REFSEQ: accession NM_001394945.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Liu,R., Zhou,D., Yu,B. and Zhou,Z.
  TITLE     Phosphorylation of LZTS2 by PLK1 activates the Wnt pathway
  JOURNAL   Cell Signal 120, 111226 (2024)
   PUBMED   38740232
  REMARK    GeneRIF: Phosphorylation of LZTS2 by PLK1 activates the Wnt
            pathway.
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Peng,Y., Greenland,N.Y., Lang,U.E. and Stohr,B.A.
  TITLE     LZTS2: A novel and independent prognostic biomarker for clear cell
            renal cell carcinoma
  JOURNAL   Pathol Res Pract 232, 153831 (2022)
   PUBMED   35287088
  REMARK    GeneRIF: LZTS2: A novel and independent prognostic biomarker for
            clear cell renal cell carcinoma.
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Schmeisser,M.J., Grabrucker,A.M., Bockmann,J. and Boeckers,T.M.
  TITLE     Synaptic cross-talk between N-methyl-D-aspartate receptors and
            LAPSER1-beta-catenin at excitatory synapses
  JOURNAL   J Biol Chem 284 (42), 29146-29157 (2009)
   PUBMED   19703901
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Sudo,H. and Maru,Y.
  TITLE     LAPSER1/LZTS2: a pluripotent tumor suppressor linked to the
            inhibition of katanin-mediated microtubule severing
  JOURNAL   Hum Mol Genet 17 (16), 2524-2540 (2008)
   PUBMED   18490357
  REMARK    GeneRIF: LAPSER1 C terminal domain inhibits
            katanin(p80/p60)-mediated microtubule severing in vitro.
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Cho,H.H., Song,J.S., Yu,J.M., Yu,S.S., Choi,S.J., Kim,D.H. and
            Jung,J.S.
  TITLE     Differential effect of NF-kappaB activity on beta-catenin/Tcf
            pathway in various cancer cells
  JOURNAL   FEBS Lett 582 (5), 616-622 (2008)
   PUBMED   18242184
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Hyun Hwa,Cho., Hye Joon,Joo., Ji Sun,Song., Yong Chan,Bae. and Jin
            Sup,Jung.
  TITLE     Crossregulation of beta-catenin/Tcf pathway by NF-kappaB is
            mediated by lzts2 in human adipose tissue-derived mesenchymal stem
            cells
  JOURNAL   Biochim Biophys Acta 1783 (3), 419-428 (2008)
   PUBMED   17950943
  REMARK    GeneRIF: The reciprocal crosstalk between beta-catenin/Tcf pathway
            and NF-kappaB signaling in hMSCs is mediated through the regulation
            of lzts2 expression.
REFERENCE   9  (residues 1 to 449)
  AUTHORS   Thyssen,G., Li,T.H., Lehmann,L., Zhuo,M., Sharma,M. and Sun,Z.
  TITLE     LZTS2 is a novel beta-catenin-interacting protein and regulates the
            nuclear export of beta-catenin
  JOURNAL   Mol Cell Biol 26 (23), 8857-8867 (2006)
   PUBMED   17000760
  REMARK    GeneRIF: LZTS2 is a beta-catenin-interacting protein and modulates
            beta-catenin signaling and localization
REFERENCE   10 (residues 1 to 449)
  AUTHORS   Cabeza-Arvelaiz,Y., Thompson,T.C., Sepulveda,J.L. and Chinault,A.C.
  TITLE     LAPSER1: a novel candidate tumor suppressor gene from 10q24.3
  JOURNAL   Oncogene 20 (46), 6707-6717 (2001)
   PUBMED   11709705
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133215.17.
            
            On May 11, 2021 this sequence version replaced XP_016872270.1.
            
            Summary: The protein encoded by this gene belongs to the leucine
            zipper tumor suppressor family of proteins, which function in
            transcription regulation and cell cycle control. This family member
            can repress beta-catenin-mediated transcriptional activation and is
            a negative regulator of the Wnt signaling pathway. It negatively
            regulates microtubule severing at centrosomes, and is necessary for
            central spindle formation and cytokinesis completion. It is
            implicated in cancer, where it may inhibit cell proliferation and
            decrease susceptibility to tumor development. Alternative splicing
            of this gene results in multiple transcript variants. [provided by
            RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2623066.1,
                                           SRR14038193.366792.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.31"
     Protein         1..449
                     /product="leucine zipper putative tumor suppressor 2
                     isoform b"
                     /note="protein LAPSER1; leucine zipper, putative tumor
                     suppressor 2"
                     /calculated_mol_wt=50698
     Region          <106..>318
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          219..416
                     /region_name="Fez1"
                     /note="pfam06818"
                     /db_xref="CDD:462015"
     CDS             1..449
                     /gene="LZTS2"
                     /gene_synonym="LAPSER1"
                     /coded_by="NM_001394945.1:207..1556"
                     /note="isoform b is encoded by transcript variant 6"
                     /db_xref="GeneID:84445"
                     /db_xref="HGNC:HGNC:29381"
                     /db_xref="MIM:610454"
ORIGIN      
        1 maivqtlpvp lepapeaata pqapvmgsvs slisgrpcpg gpapprhhgp pgptffrqqd
       61 gllrggyeaq eplcpavppr kavpvtsfty inedfrtesp pspssdveda reqrahnahl
      121 rgpppklipv sgklekayee rqrhwqrere alredcaaqa qraqraqqll qlqvfqlqqe
      181 krqlqddfaq llqereqler rcatlereqr elgprleetk wevcqksgei sllkqqlkes
      241 qaelvqkgse lvalrvalre aratlrvseg rarglqeaar areleleacs qelqrhrqea
      301 eqlrekagql daeaaglrep pvppatadpf llaesdeakv qraaagvggs lraqverlrv
      361 elqrerrrge eqrdsfeger lawqaekeqv iryqkqlqhn yiqmyrrnrq leqelqqlsl
      421 eleareladl glaeqapcic leeitatei
//
LOCUS       NP_001381518              98 aa            linear   PRI 21-NOV-2025
DEFINITION  ragulator complex protein LAMTOR4 isoform 6 [Homo sapiens].
ACCESSION   NP_001381518
VERSION     NP_001381518.1
DBSOURCE    REFSEQ: accession NM_001394589.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Gamallat,Y., Alwazan,H., Turko,R., Dang,V., Seyedi,S., Ghosh,S. and
            Bismar,T.A.
  TITLE     Elevated LAMTOR4 Expression Is Associated with Lethal Prostate
            Cancer and Its Knockdown Decreases Cell Proliferation, Invasion,
            and Migration In Vitro
  JOURNAL   Int J Mol Sci 25 (15), 8100 (2024)
   PUBMED   39125671
  REMARK    GeneRIF: Elevated LAMTOR4 Expression Is Associated with Lethal
            Prostate Cancer and Its Knockdown Decreases Cell Proliferation,
            Invasion, and Migration In Vitro.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 98)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 98)
  AUTHORS   Zhang,S., Lee,S.H., Nie,L., Huang,Y., Zou,G., Jung,Y.S., Jun,S.,
            Zhang,J., Lien,E.M., Chen,J. and Park,J.I.
  TITLE     Lysosomal TMEM9-LAMTOR4-controlled mTOR signaling integrity is
            required for mammary tumorigenesis
  JOURNAL   Cancer Commun (Lond) 43 (1), 159-163 (2023)
   PUBMED   36336962
  REMARK    GeneRIF: Lysosomal TMEM9-LAMTOR4-controlled mTOR signaling
            integrity is required for mammary tumorigenesis.
REFERENCE   6  (residues 1 to 98)
  AUTHORS   Rebsamen,M., Pochini,L., Stasyk,T., de Araujo,M.E., Galluccio,M.,
            Kandasamy,R.K., Snijder,B., Fauster,A., Rudashevskaya,E.L.,
            Bruckner,M., Scorzoni,S., Filipek,P.A., Huber,K.V., Bigenzahn,J.W.,
            Heinz,L.X., Kraft,C., Bennett,K.L., Indiveri,C., Huber,L.A. and
            Superti-Furga,G.
  TITLE     SLC38A9 is a component of the lysosomal amino acid sensing
            machinery that controls mTORC1
  JOURNAL   Nature 519 (7544), 477-481 (2015)
   PUBMED   25561175
REFERENCE   7  (residues 1 to 98)
  AUTHORS   Blandin,G., Marchand,S., Charton,K., Daniele,N., Gicquel,E.,
            Boucheteil,J.B., Bentaib,A., Barrault,L., Stockholm,D., Bartoli,M.
            and Richard,I.
  TITLE     A human skeletal muscle interactome centered on proteins involved
            in muscular dystrophies: LGMD interactome
  JOURNAL   Skelet Muscle 3 (1), 3 (2013)
   PUBMED   23414517
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 98)
  AUTHORS   Bar-Peled,L., Schweitzer,L.D., Zoncu,R. and Sabatini,D.M.
  TITLE     Ragulator is a GEF for the rag GTPases that signal amino acid
            levels to mTORC1
  JOURNAL   Cell 150 (6), 1196-1208 (2012)
   PUBMED   22980980
  REMARK    GeneRIF: Study identified HBXIP and C7orf59 as two additional
            Ragulator components that are required for mTORC1 activation by
            amino acids.
REFERENCE   9  (residues 1 to 98)
  AUTHORS   Sancak,Y., Bar-Peled,L., Zoncu,R., Markhard,A.L., Nada,S. and
            Sabatini,D.M.
  TITLE     Ragulator-Rag complex targets mTORC1 to the lysosomal surface and
            is necessary for its activation by amino acids
  JOURNAL   Cell 141 (2), 290-303 (2010)
   PUBMED   20381137
REFERENCE   10 (residues 1 to 98)
  AUTHORS   Toulza,E., Mattiuzzo,N.R., Galliano,M.F., Jonca,N., Dossat,C.,
            Jacob,D., de Daruvar,A., Wincker,P., Serre,G. and Guerrin,M.
  TITLE     Large-scale identification of human genes implicated in epidermal
            barrier function
  JOURNAL   Genome Biol 8 (6), R107 (2007)
   PUBMED   17562024
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073842.5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..98
                     /product="ragulator complex protein LAMTOR4 isoform 6"
                     /note="UPF0539 protein C7orf59; late endosomal/lysosomal
                     adaptor and MAPK and MTOR activator 4; ragulator complex
                     protein LAMTOR4"
                     /calculated_mol_wt=10271
     CDS             1..98
                     /gene="LAMTOR4"
                     /gene_synonym="C7orf59"
                     /coded_by="NM_001394589.1:56..352"
                     /note="isoform 6 is encoded by transcript variant 9"
                     /db_xref="GeneID:389541"
                     /db_xref="HGNC:HGNC:33772"
                     /db_xref="MIM:618834"
ORIGIN      
        1 mvsedacarg paggsasllp slcgfplssg dlendeqaas aiselvstac gfrlhrgmnv
       61 pfkrlsvvfg ehtllvtvsg qrvfvvkrqn rgrepidv
//
LOCUS       NP_001335423            1402 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 2 isoform o [Homo
            sapiens].
ACCESSION   NP_001335423 XP_016869519
VERSION     NP_001335423.1
DBSOURCE    REFSEQ: accession NM_001348494.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1402)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1402)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   3  (residues 1 to 1402)
  AUTHORS   Mechaussier,S., Almoallem,B., Zeitz,C., Van Schil,K., Jeddawi,L.,
            Van Dorpe,J., Duenas Rey,A., Condroyer,C., Pelle,O., Polak,M.,
            Boddaert,N., Bahi-Buisson,N., Cavallin,M., Bacquet,J.L.,
            Mouallem-Beziere,A., Zambrowski,O., Sahel,J.A., Audo,I., Kaplan,J.,
            Rozet,J.M., De Baere,E. and Perrault,I.
  TITLE     Loss of Function of RIMS2 Causes a Syndromic Congenital Cone-Rod
            Synaptic Disease with Neurodevelopmental and Pancreatic Involvement
  JOURNAL   Am J Hum Genet 106 (6), 859-871 (2020)
   PUBMED   32470375
  REMARK    GeneRIF: Loss of Function of RIMS2 Causes a Syndromic Congenital
            Cone-Rod Synaptic Disease with Neurodevelopmental and Pancreatic
            Involvement.
            Erratum:[Am J Hum Genet. 2020 Sep 3;107(3):580. doi:
            10.1016/j.ajhg.2020.08.004. PMID: 32888510]
REFERENCE   4  (residues 1 to 1402)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 1402)
  AUTHORS   Kim,K.T., Lee,J.S., Lee,B.W., Seok,H., Jeon,H.S., Kim,J.H. and
            Chung,J.H.
  TITLE     Association between regulating synaptic membrane exocytosis 2 gene
            polymorphisms and degenerative lumbar scoliosis
  JOURNAL   Biomed Rep 1 (4), 619-623 (2013)
   PUBMED   24648997
REFERENCE   6  (residues 1 to 1402)
  AUTHORS   Sun,L., Bittner,M.A. and Holz,R.W.
  TITLE     Rim, a component of the presynaptic active zone and modulator of
            exocytosis, binds 14-3-3 through its N terminus
  JOURNAL   J Biol Chem 278 (40), 38301-38309 (2003)
   PUBMED   12871946
REFERENCE   7  (residues 1 to 1402)
  AUTHORS   Fukuda,M.
  TITLE     Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and
            Noc2. Identification of a critical determinant of Rab3A/Rab27A
            recognition by Rim2
  JOURNAL   J Biol Chem 278 (17), 15373-15380 (2003)
   PUBMED   12578829
REFERENCE   8  (residues 1 to 1402)
  AUTHORS   Wang,Y. and Sudhof,T.C.
  TITLE     Genomic definition of RIM proteins: evolutionary amplification of a
            family of synaptic regulatory proteins
  JOURNAL   Genomics 81 (2), 126-137 (2003)
   PUBMED   12620390
REFERENCE   9  (residues 1 to 1402)
  AUTHORS   Kashima,Y., Miki,T., Shibasaki,T., Ozaki,N., Miyazaki,M., Yano,H.
            and Seino,S.
  TITLE     Critical role of cAMP-GEFII--Rim2 complex in incretin-potentiated
            insulin secretion
  JOURNAL   J Biol Chem 276 (49), 46046-46053 (2001)
   PUBMED   11598134
REFERENCE   10 (residues 1 to 1402)
  AUTHORS   Fenster,S.D., Chung,W.J., Zhai,R., Cases-Langhoff,C., Voss,B.,
            Garner,A.M., Kaempf,U., Kindler,S., Gundelfinger,E.D. and
            Garner,C.C.
  TITLE     Piccolo, a presynaptic zinc finger protein structurally related to
            bassoon
  JOURNAL   Neuron 25 (1), 203-214 (2000)
   PUBMED   10707984
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012213.8, AC090686.4,
            AP001572.3, AC107933.6 and AP002849.2.
            
            On Feb 4, 2017 this sequence version replaced XP_016869519.1.
            
            Summary: The protein encoded by this gene is a presynaptic protein
            that interacts with RAB3, a protein important for normal
            neurotransmitter release. The encoded protein can also bind several
            other synaptic proteins, including UNC-13 homolog B,
            ELKS/Rab6-interacting/CAST family member 1, and synaptotagmin 1.
            This protein is involved in synaptic membrane exocytosis.
            Polymorphisms in this gene have been associated with degenerative
            lumbar scoliosis. [provided by RefSeq, Feb 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.18138.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1402
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..1402
                     /product="regulating synaptic membrane exocytosis protein
                     2 isoform o"
                     /note="RAB3 interacting protein 3; regulating synaptic
                     membrane exocytosis protein 2; nuclear protein; non-small
                     cell lung cancer RimL3a protein; non-small cell lung
                     cancer RimL3c protein; rab3-interacting molecule 2;
                     rab-3-interacting protein 3; rab-3-interacting molecule 2;
                     Rab3-interacting protein"
                     /calculated_mol_wt=159258
     Region          30..154
                     /region_name="PHD_SF"
                     /note="PHD finger superfamily; cl22851"
                     /db_xref="CDD:473978"
     Region          623..722
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(647..653,668,671,701,705,708..709)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          774..900
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(805,811,866,868,876)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          1233..1378
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(1290,1294..1295,1297,1300,1328,1330,1332,1376..1377)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..1402
                     /gene="RIMS2"
                     /gene_synonym="CRSDS; OBOE; RAB3IP3; RIM2"
                     /coded_by="NM_001348494.2:278..4486"
                     /note="isoform o is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS94328.1"
                     /db_xref="GeneID:9699"
                     /db_xref="HGNC:HGNC:17283"
                     /db_xref="MIM:606630"
ORIGIN      
        1 msapvgprgr lapipaasqp plqpempdls hlteeerkii lavmdrqkke eekeqsvlkk
       61 lhqqfemyke qvkkmgeesq qqqeqkgdap tcgichktkf adgcghncsy cqtkfcarcg
      121 grvslrsnkv mwvcnlcrkq qeiltksgaw fynsgsntpq qpdqkvlrgl rneeapqekk
      181 pklheqtqfq gpsgdlsvpa veksrshglt rqhsikngsg vkhhiasdia sdrkrspsvs
      241 rdqnrrydqr eereeysqya tsdtamprsp sdyadrrsqh epqfyedsdh lsyrdsnrrs
      301 hrhskeyivd dedvesrdey erqrreeeyq sryrsdpnla rypvkpqpye eqmrihaevs
      361 rarherrhsd vslanadled srismlrmdr psrqrsiser raamenqrsy smertreaqg
      421 pssyaqrttn hspptprrsp lpidrpdlrr tdslrkqhhl dpssavrktk rekmetmlrn
      481 dslssdqses vrppppkphk skkggkmrqi slssseeela stpeytscdd veiesesvse
      541 kgdsqkgkrk tseqavlsds ntrserqkem myfgghslee dlewsepqik dsgvdtcsst
      601 tlneehshsd khpvtwqpsk dgdrligril lnkrlkdgsv prdsgamlgl kvvggkmtes
      661 grlcafitkv kkgsladtvg hlrpgdevle wngrllqgat feevyniile skpepqvelv
      721 vsrpigdipr ipdsthaqle sssssfesqk mdrpsisvts pmspgmlrdv pqflsgqlsi
      781 klwfdkvghq livtilgakd lpsredgrpr npyvkiyflp drsdknkrrt ktvkktlepk
      841 wnqtfiyspv hrrefrerml eitlwdqarv reeeseflge ilieletall ddephwyklq
      901 thdvsslplp hpspymprrq lhgesptrrl qrskrisdse vsdydcddgi gvvsdyrhdg
      961 rdlqsstlsv peqvmssnhc spsgsphrvd vigrtrswsp svpppqsrnv eqglrgtrtm
     1021 tghyntisrm drhrvmddhy spdrdshflt lprsrysqti dhhhrdgrdc eaadrqpyhr
     1081 srsteqrpll ertttrsrst erpdtnlmrs mpslmtgrsa ppspalsrsh prtgsvqtsp
     1141 sstpvagrrg rqlpqlppkg tldrkaggkk lrstvqrste tglavemrnw mtrqasrest
     1201 dgsmnsysse gnlifpgvrl asdsqfsdfl dglgpaqlvg rqtlatpamg diqvgmmdkk
     1261 gqleveiira rglvvkpgsk tlpapyvkvy lldngvciak kktkvarktl eplyqqllsf
     1321 eespqgkvlq iivwgdygrm dhksfmgvaq illdelelsn mvigwfklfp psslvdptla
     1381 pltrrasqss lesstgpsys rs
//
LOCUS       NP_036305                291 aa            linear   PRI 21-NOV-2025
DEFINITION  F-box only protein 25 isoform 3 [Homo sapiens].
ACCESSION   NP_036305
VERSION     NP_036305.2
DBSOURCE    REFSEQ: accession NM_012173.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Quintero-Barceinas,R.S., Gehringer,F., Ducker,C., Saxton,J. and
            Shaw,P.E.
  TITLE     ELK-1 ubiquitination status and transcriptional activity are
            modulated independently of F-Box protein FBXO25
  JOURNAL   J Biol Chem 296, 100214 (2021)
   PUBMED   33428929
  REMARK    GeneRIF: ELK-1 ubiquitination status and transcriptional activity
            are modulated independently of F-Box protein FBXO25.
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Kuzmanov,A., Johansen,P. and Hofbauer,G.
  TITLE     FBXO25 Promotes Cutaneous Squamous Cell Carcinoma Growth and
            Metastasis through Cyclin D1
  JOURNAL   J Invest Dermatol 140 (12), 2496-2504 (2020)
   PUBMED   32335130
  REMARK    GeneRIF: FBXO25 Promotes Cutaneous Squamous Cell Carcinoma Growth
            and Metastasis through Cyclin D1.
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Manfiolli,A.O., Maragno,A.L., Baqui,M.M., Yokoo,S., Teixeira,F.R.,
            Oliveira,E.B. and Gomes,M.D.
  TITLE     FBXO25-associated nuclear domains: a novel subnuclear structure
  JOURNAL   Mol Biol Cell 19 (5), 1848-1861 (2008)
   PUBMED   18287534
  REMARK    GeneRIF: The cellular distribution of FBXO25 and its colocalization
            with some nuclear proteins is investigated by using immunochemical
            and biochemical approaches.
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Hagens,O., Minina,E., Schweiger,S., Ropers,H.H. and Kalscheuer,V.
  TITLE     Characterization of FBX25, encoding a novel brain-expressed F-box
            protein
  JOURNAL   Biochim Biophys Acta 1760 (1), 110-118 (2006)
   PUBMED   16278047
  REMARK    GeneRIF: investigated hFBX25's genomic organization and established
            hFBX25 as an FBP by verifying its interaction with Skp1 and Cul1
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF419858.1, BC012143.2,
            BC050393.1, AA316216.1, AI223050.1 and AC083964.3.
            
            On Sep 22, 2003 this sequence version replaced NP_036305.1.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box),
            which function in phosphorylation-dependent ubiquitination. The
            F-box proteins are divided into 3 classes: Fbws containing WD-40
            domains, Fbls containing leucine-rich repeats, and Fbxs containing
            either different protein-protein interaction modules or no
            recognizable motifs. The protein encoded by this gene belongs to
            the Fbxs class. Three alternatively spliced transcript variants
            encoding distinct isoforms have been found for this gene. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) lacks two internal exons, as
            compared to variant 1. The encoded isoform (3) has an alternate
            N-terminus and lacks an internal segment in the 3' region, as
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2049786.1,
                                           SRR14038196.905964.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p23.3"
     Protein         1..291
                     /product="F-box only protein 25 isoform 3"
                     /note="F-box protein Fbx25; F-box only protein 25"
                     /calculated_mol_wt=33936
     Region          160..204
                     /region_name="F-box_FBXO25"
                     /note="F-box domain found in F-box only protein 25
                     (FBXO25) and similar proteins; cd22099"
                     /db_xref="CDD:438871"
     Site            order(164,168,171..172,175..176,181,183..184,188..190,192)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438871"
     CDS             1..291
                     /gene="FBXO25"
                     /gene_synonym="FBX25"
                     /coded_by="NM_012173.4:268..1143"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS5954.1"
                     /db_xref="GeneID:26260"
                     /db_xref="HGNC:HGNC:13596"
                     /db_xref="MIM:609098"
ORIGIN      
        1 mekysimksm nmhrkkgkrt ilemtqilkr hgyctlgeaf nrldfssaiq dirrfnyvvk
       61 llqliaksql tslsgvaqkn yfnildkivq kvlddhhnpr likdllqdls stlcilirgv
      121 gksvlvgnin iwicrletil awqqqlqdlq mtkqvnnglt lsdlplhmln nilyrfsdgw
      181 diitlgqvtp tlymlsedrq lwkklcqyhf aekqfcrhli lsekghiewk lmyfalqkhy
      241 pakeqygdtl hfcrhcsilf wkdsghpcta adpdscftpv spqhfidlfk f
//
LOCUS       NP_001269283             693 aa            linear   PRI 21-NOV-2025
DEFINITION  integrin beta-6 isoform b precursor [Homo sapiens].
ACCESSION   NP_001269283
VERSION     NP_001269283.1
DBSOURCE    REFSEQ: accession NM_001282354.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Zhang,Y., Chen,Z., Shen,Z., Qian,D., Wang,G., Wang,X., Xi,S. and
            Wang,X.
  TITLE     ITGB6 promotes pancreatic fibrosis and aggravates the malignant
            process of pancreatic cancer via JAK2/STAT3 signaling pathway
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 397 (8), 6093-6106 (2024)
   PUBMED   38418753
  REMARK    GeneRIF: ITGB6 promotes pancreatic fibrosis and aggravates the
            malignant process of pancreatic cancer via JAK2/STAT3 signaling
            pathway.
REFERENCE   2  (residues 1 to 693)
  AUTHORS   Geyer,M., Geyer,F., Reuning,U., Klapproth,S., Wolff,K.D. and
            Nieberler,M.
  TITLE     CRISPR/Cas9-mediated knock out of ITGB6 in human OSCC cells reduced
            migration and proliferation ability
  JOURNAL   Head Face Med 20 (1), 37 (2024)
   PUBMED   38890650
  REMARK    GeneRIF: CRISPR/Cas9-mediated knock out of ITGB6 in human OSCC
            cells reduced migration and proliferation ability.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 693)
  AUTHORS   Liu,L., He,Z., Jiang,Z., Liu,Z. and Zhuang,X.
  TITLE     Acidity-induced ITGB6 promote migration and invasion of lung cancer
            cells by epithelial-mesenchymal transition and focal adhesion
  JOURNAL   Exp Cell Res 436 (1), 113962 (2024)
   PUBMED   38316250
  REMARK    GeneRIF: Acidity-induced ITGB6 promote migration and invasion of
            lung cancer cells by epithelial-mesenchymal transition and focal
            adhesion.
REFERENCE   4  (residues 1 to 693)
  AUTHORS   Munger,J.S., Huang,X., Kawakatsu,H., Griffiths,M.J., Dalton,S.L.,
            Wu,J., Pittet,J.F., Kaminski,N., Garat,C., Matthay,M.A.,
            Rifkin,D.B. and Sheppard,D.
  TITLE     The integrin alpha v beta 6 binds and activates latent TGF beta 1:
            a mechanism for regulating pulmonary inflammation and fibrosis
  JOURNAL   Cell 96 (3), 319-328 (1999)
   PUBMED   10025398
REFERENCE   5  (residues 1 to 693)
  AUTHORS   Huang,X.Z., Chen,A., Agrez,M. and Sheppard,D.
  TITLE     A point mutation in the integrin beta 6 subunit abolishes both
            alpha v beta 6 binding to fibronectin and receptor localization to
            focal contacts
  JOURNAL   Am J Respir Cell Mol Biol 13 (2), 245-251 (1995)
   PUBMED   7626292
REFERENCE   6  (residues 1 to 693)
  AUTHORS   Weinacker,A., Ferrando,R., Elliott,M., Hogg,J., Balmes,J. and
            Sheppard,D.
  TITLE     Distribution of integrins alpha v beta 6 and alpha 9 beta 1 and
            their known ligands, fibronectin and tenascin, in human airways
  JOURNAL   Am J Respir Cell Mol Biol 12 (5), 547-556 (1995)
   PUBMED   7537970
REFERENCE   7  (residues 1 to 693)
  AUTHORS   Fernandez-Ruiz,E. and Sanchez-Madrid,F.
  TITLE     Regional localization of the human integrin beta 6 gene (ITGB6) to
            chromosome 2q24-q31
  JOURNAL   Genomics 21 (3), 638-640 (1994)
   PUBMED   7959743
REFERENCE   8  (residues 1 to 693)
  AUTHORS   Busk,M., Pytela,R. and Sheppard,D.
  TITLE     Characterization of the integrin alpha v beta 6 as a
            fibronectin-binding protein
  JOURNAL   J Biol Chem 267 (9), 5790-5796 (1992)
   PUBMED   1532572
REFERENCE   9  (residues 1 to 693)
  AUTHORS   Krissansen,G.W., Yuan,Q., Jenkins,D., Jiang,W.M., Rooke,L.,
            Spurr,N.K., Eccles,M., Leung,E. and Watson,J.D.
  TITLE     Chromosomal locations of the genes coding for the integrin beta 6
            and beta 7 subunits
  JOURNAL   Immunogenetics 35 (1), 58-61 (1992)
   PUBMED   1729173
REFERENCE   10 (residues 1 to 693)
  AUTHORS   Sheppard,D., Rozzo,C., Starr,L., Quaranta,V., Erle,D.J. and
            Pytela,R.
  TITLE     Complete amino acid sequence of a novel integrin beta subunit (beta
            6) identified in epithelial cells using the polymerase chain
            reaction
  JOURNAL   J Biol Chem 265 (20), 11502-11507 (1990)
   PUBMED   2365683
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB222211.1, CD013946.1,
            BC143656.1, AC080166.6 and AI264144.1.
            
            Summary: This gene encodes a protein that is a member of the
            integrin superfamily. Members of this family are adhesion receptors
            that function in signaling from the extracellular matrix to the
            cell. Integrins are heterodimeric integral membrane proteins
            composed of an alpha chain and a beta chain. The encoded protein
            forms a dimer with an alpha v chain and this heterodimer can bind
            to ligands like fibronectin and transforming growth factor beta 1.
            Alternate splicing results in multiple transcript variants.
            [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (3) lacks two in-frame exons in
            the 5' coding region compared to variant 1. The encoded isoform (b)
            is shorter compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD013946.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.2"
     Protein         1..693
                     /product="integrin beta-6 isoform b precursor"
                     /note="integrin, beta 6"
                     /calculated_mol_wt=73445
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2423
     Region          21..359
                     /region_name="vWFA"
                     /note="Von Willebrand factor type A (vWA) domain was
                     originally found in the blood coagulation protein von
                     Willebrand factor (vWF). Typically, the vWA domain is made
                     up of approximately 200 amino acid residues folded into a
                     classic a/b para-rossmann type of...; cl00057"
                     /db_xref="CDD:469594"
     Region          361..390
                     /region_name="I-EGF_1"
                     /note="Integrin beta epidermal growth factor like domain
                     1; pfam18372"
                     /db_xref="CDD:465729"
     Region          529..611
                     /region_name="Integrin_B_tail"
                     /note="Integrin beta tail domain; pfam07965"
                     /db_xref="CDD:462325"
     Region          639..679
                     /region_name="Integrin_b_cyt"
                     /note="Integrin beta cytoplasmic domain; pfam08725"
                     /db_xref="CDD:462580"
     CDS             1..693
                     /gene="ITGB6"
                     /gene_synonym="AI1H"
                     /coded_by="NM_001282354.2:210..2291"
                     /note="isoform b precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS74597.1"
                     /db_xref="GeneID:3694"
                     /db_xref="HGNC:HGNC:6161"
                     /db_xref="MIM:147558"
ORIGIN      
        1 mgiellclff lflgrndhvq ggaqtlqvhv rqtedypvdl yylmdlsasm dddlntikel
       61 gsrlskemsk ltsnfrlgfg sfvekpvspf vkttpeeian pcssipyfcl ptfgfkhilp
      121 ltndaerfne ivknqkisan idtpeggfda imqaavckek igwrndslhl lvfvsdadsh
      181 fgmdsklagi vipndglchl dskneysmst vleyptigql idklvqnnvl lifavtqeqv
      241 hlyenyakli pgatvgllqk dsgnilqlii sayeelrsev elevlgdteg lnlsftaicn
      301 ngtlfqhqkk cshmkvgdta sfsvtvniph cerrsrhiii kpvglgdale llvspecncd
      361 cqkevevnss kchhgngsfq cgvcachpgh mgprcecged mlstdsckea pdhpscsgrg
      421 dcycgqcich lspygniygp ycqcdnfscv rhkgllcggn gdcdcgecvc rsgwtgeycn
      481 cttstdscvs edgvlcsgrg dcvcgkcvct npgasgptce rcptcgdpcn skrsciechl
      541 saagqareec vdkcklagat iseeedfskd gsvscslqge neclitflit tdnegktiih
      601 sinekdcpkp pnipmimlgv slailligvv llciwkllvs fhdrkevakf eaerskakwq
      661 tgtnplyrgs tstfknvtyk hrekqkvdls tdc
//
LOCUS       NP_001269586             607 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger protein 143 isoform 3 [Homo sapiens].
ACCESSION   NP_001269586 XP_005253181
VERSION     NP_001269586.1
DBSOURCE    REFSEQ: accession NM_001282657.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Narducci,D.N. and Hansen,A.S.
  TITLE     Putative looping factor ZNF143/ZFP143 is an essential
            transcriptional regulator with no looping function
  JOURNAL   Mol Cell 85 (1), 9-23 (2025)
   PUBMED   39708803
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Geng,T., Sun,Q., He,J., Chen,Y., Cheng,W., Shen,J., Liu,B.,
            Zhang,M., Wang,S., Asan,K., Song,M., Gao,Q., Song,Y., Liu,R.,
            Liu,X., Ding,Y., Jing,A., Ye,X., Ren,H., Zeng,K., Zhou,Y.,
            Zhang,B., Ma,S., Liu,W., Liu,S. and Ji,J.
  TITLE     CXXC5 drove inflammation and ovarian cancer proliferation via
            transcriptional activation of ZNF143 and EGR1
  JOURNAL   Cell Signal 119, 111180 (2024)
   PUBMED   38642782
  REMARK    GeneRIF: CXXC5 drove inflammation and ovarian cancer proliferation
            via transcriptional activation of ZNF143 and EGR1.
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Li,M., Chen,J., Zhang,H., Zhang,Y., Wang,J., Shen,Z., Chen,Y.,
            Hou,W. and Chi,C.
  TITLE     LOC644656 promotes cisplatin resistance in cervical cancer by
            recruiting ZNF143 and activating the transcription of E6-AP
  JOURNAL   Cell Signal 117, 111115 (2024)
   PUBMED   38395183
  REMARK    GeneRIF: LOC644656 promotes cisplatin resistance in cervical cancer
            by recruiting ZNF143 and activating the transcription of E6-AP.
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Chen,Y., Li,J., Ma,J. and Bao,Y.
  TITLE     ZNF143 facilitates the growth and migration of glioma cells by
            regulating KPNA2-mediated Hippo signalling
  JOURNAL   Sci Rep 13 (1), 11097 (2023)
   PUBMED   37423952
  REMARK    GeneRIF: ZNF143 facilitates the growth and migration of glioma
            cells by regulating KPNA2-mediated Hippo signalling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 607)
  AUTHORS   Mei,J., Liu,Y., Sheng,Y., Liu,Y., Chen,L., Wang,H., Cheng,M.,
            Zhai,Z. and Xu,L.
  TITLE     ATF1 promotes the malignancy of lung adenocarcinoma cells by
            transcriptionally regulating ZNF143 expression
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 55 (5), 769-782 (2023)
   PUBMED   37158648
  REMARK    GeneRIF: ATF1 promotes the malignancy of lung adenocarcinoma cells
            by transcriptionally regulating ZNF143 expression.
REFERENCE   6  (residues 1 to 607)
  AUTHORS   Schuster,C., Krol,A. and Carbon,P.
  TITLE     Two distinct domains in Staf to selectively activate small nuclear
            RNA-type and mRNA promoters
  JOURNAL   Mol Cell Biol 18 (5), 2650-2658 (1998)
   PUBMED   9566884
REFERENCE   7  (residues 1 to 607)
  AUTHORS   Schaub,M., Myslinski,E., Schuster,C., Krol,A. and Carbon,P.
  TITLE     Staf, a promiscuous activator for enhanced transcription by RNA
            polymerases II and III
  JOURNAL   EMBO J 16 (1), 173-181 (1997)
   PUBMED   9009278
REFERENCE   8  (residues 1 to 607)
  AUTHORS   Schuster,C., Myslinski,E., Krol,A. and Carbon,P.
  TITLE     Staf, a novel zinc finger protein that activates the RNA polymerase
            III promoter of the selenocysteine tRNA gene
  JOURNAL   EMBO J 14 (15), 3777-3787 (1995)
   PUBMED   7641696
REFERENCE   9  (residues 1 to 607)
  AUTHORS   Tommerup,N. and Vissing,H.
  TITLE     Isolation and fine mapping of 16 novel human zinc finger-encoding
            cDNAs identify putative candidate genes for developmental and
            malignant disorders
  JOURNAL   Genomics 27 (2), 259-264 (1995)
   PUBMED   7557990
REFERENCE   10 (residues 1 to 607)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG825506.1, AK297214.1, BC014458.1, CN295530.1 and BF515092.1.
            
            On Sep 17, 2013 this sequence version replaced XP_005253181.1.
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1, resulting in
            an isoform (3) that is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297214.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..607
                     /product="zinc finger protein 143 isoform 3"
                     /EC_number="2.7.10.2"
                     /note="SPH-binding factor; transcriptional activator Staf;
                     hStaf; selenocysteine tRNA gene transcription-activating
                     factor"
                     /calculated_mol_wt=65505
     Region          208..230
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(215,217,219,221..222,225..226,229,245,247,251..252,
                     255..256,259,275,277,279,281..282,285..286,289)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <220..393
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          238..260
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          268..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..320
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          328..350
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          358..380
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          388..407
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..607
                     /gene="ZNF143"
                     /gene_synonym="pHZ-1; SBF; STAF"
                     /coded_by="NM_001282657.2:73..1896"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS60721.1"
                     /db_xref="GeneID:7702"
                     /db_xref="HGNC:HGNC:12928"
                     /db_xref="MIM:603433"
ORIGIN      
        1 mllaqinrds qgmtefpggg meaqhvtlcl teavtvadak lidgqviqle dgsaayvqhv
       61 pipkstgdsl rledgqavql edgttafihh tskdsydqsa lqavqledgt tayihhavqv
      121 pqsdtilaiq adgtvaglht gdatidpdti saleqyaakv sidgsesvag tgmigeneqe
      181 kkmqivlqgh atrvtaksqq sgekafrcey dgcgklytta hhlkvhersh tgdrpyqceh
      241 agcgkafatg yglkshvrth tgekpyrcse dnctksfkts gdlqkhirth tgerpfkcpf
      301 egcgrsftts nirkvhvrth tgerpyycte pgcgrafasa tnyknhvrih tgekpyvctv
      361 pgcdkrftey sslykhhvvh thskpyncnh cgktykqist lamhkrtahn dtepieeeqe
      421 affepppgqg edvlkgsqit yvtgvegddv vstqvatvtq sglsqqvtli sqdgtqhvni
      481 sqadmqaign titmvtqdgt pitvpahdav issagthsva mvtaegtege qvaivaqdla
      541 afhtassemg hqqhshhlvt tetrpltlva tsngtqiavq lgeqpsleea iriasriqqg
      601 etpgldd
//
LOCUS       NP_001364119             430 aa            linear   PRI 21-NOV-2025
DEFINITION  C-terminal-binding protein 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001364119 XP_016863252
VERSION     NP_001364119.1
DBSOURCE    REFSEQ: accession NM_001377190.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Kong,Y., Yang,G., Feng,X., Ji,Z., Wang,X., Shao,Y., Meng,J.,
            Yao,G., Ren,C. and Yang,G.
  TITLE     CTBP1 links metabolic syndrome to polycystic ovary syndrome through
            interruption of aromatase and SREBP1
  JOURNAL   Commun Biol 7 (1), 1174 (2024)
   PUBMED   39294274
  REMARK    GeneRIF: CTBP1 links metabolic syndrome to polycystic ovary
            syndrome through interruption of aromatase and SREBP1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Zhou,J., Yan,X., Liu,Y. and Yang,J.
  TITLE     Succinylation of CTBP1 mediated by KAT2A suppresses its inhibitory
            activity on the transcription of CDH1 to promote the progression of
            prostate cancer
  JOURNAL   Biochem Biophys Res Commun 650, 9-16 (2023)
   PUBMED   36764210
  REMARK    GeneRIF: Succinylation of CTBP1 mediated by KAT2A suppresses its
            inhibitory activity on the transcription of CDH1 to promote the
            progression of prostate cancer.
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Lou,L.Q., Zhou,W.Q., Song,X. and Chen,Z.
  TITLE     Elevation of hsa-miR-7-5p level mediated by CtBP1-p300-AP1 complex
            targets ATXN1 to trigger NF-kappaB-dependent inflammation response
  JOURNAL   J Mol Med (Berl) 101 (3), 223-235 (2023)
   PUBMED   36629882
  REMARK    GeneRIF: Elevation of hsa-miR-7-5p level mediated by CtBP1-p300-AP1
            complex targets ATXN1 to trigger NF-kappaB-dependent inflammation
            response.
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Tseng,C., Han,Y., Lv,Z., Song,Q., Wang,K., Shen,H. and Chen,Z.
  TITLE     The CRL4DCAF6 E3 ligase ubiquitinates CtBP1/2 to induce apoptotic
            signalling and promote intervertebral disc degeneration
  JOURNAL   J Mol Med (Berl) 101 (1-2), 171-181 (2023)
   PUBMED   36688959
  REMARK    GeneRIF: The CRL4[DCAF6] E3 ligase ubiquitinates CtBP1/2 to induce
            apoptotic signalling and promote intervertebral disc degeneration.
REFERENCE   6  (residues 1 to 430)
  AUTHORS   Schaeper,U., Subramanian,T., Lim,L., Boyd,J.M. and Chinnadurai,G.
  TITLE     Interaction between a cellular protein that binds to the C-terminal
            region of adenovirus E1A (CtBP) and a novel cellular protein is
            disrupted by E1A through a conserved PLDLS motif
  JOURNAL   J Biol Chem 273 (15), 8549-8552 (1998)
   PUBMED   9535825
REFERENCE   7  (residues 1 to 430)
  AUTHORS   Katsanis,N. and Fisher,E.M.
  TITLE     A novel C-terminal binding protein (CTBP2) is closely related to
            CTBP1, an adenovirus E1A-binding protein, and maps to human
            chromosome 21q21.3
  JOURNAL   Genomics 47 (2), 294-299 (1998)
   PUBMED   9479502
REFERENCE   8  (residues 1 to 430)
  AUTHORS   Schaeper,U., Boyd,J.M., Verma,S., Uhlmann,E., Subramanian,T. and
            Chinnadurai,G.
  TITLE     Molecular cloning and characterization of a cellular phosphoprotein
            that interacts with a conserved C-terminal domain of adenovirus E1A
            involved in negative modulation of oncogenic transformation
  JOURNAL   Proc Natl Acad Sci U S A 92 (23), 10467-10471 (1995)
   PUBMED   7479821
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1998 Nov 24;95(24):14584]
REFERENCE   9  (residues 1 to 430)
  AUTHORS   Boyd,J.M., Subramanian,T., Schaeper,U., La Regina,M., Bayley,S. and
            Chinnadurai,G.
  TITLE     A region in the C-terminus of adenovirus 2/5 E1a protein is
            required for association with a cellular phosphoprotein and
            important for the negative modulation of T24-ras mediated
            transformation, tumorigenesis and metastasis
  JOURNAL   EMBO J 12 (2), 469-478 (1993)
   PUBMED   8440238
REFERENCE   10 (residues 1 to 430)
  AUTHORS   Battaglia,A., Carey,J.C. and South,S.T.
  TITLE     Wolf-Hirschhorn Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301362
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092535.4.
            
            On Dec 17, 2019 this sequence version replaced XP_016863252.1.
            
            Summary: This gene encodes a protein that binds to the C-terminus
            of adenovirus E1A proteins. This phosphoprotein is a
            transcriptional repressor and may play a role during cellular
            proliferation. This protein and the product of a second closely
            related gene, CTBP2, can dimerize. Both proteins can also interact
            with a polycomb group protein complex which participates in
            regulation of gene expression during development. Alternative
            splicing of transcripts from this gene results in multiple
            transcript variants. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2767174.1,
                                           SRR1803615.149507.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2159764
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..430
                     /product="C-terminal-binding protein 1 isoform 4"
                     /note="brefeldin A-ribosylated substrate"
                     /calculated_mol_wt=46361
     Region          17..335
                     /region_name="CtBP_dh"
                     /note="C-terminal binding protein (CtBP),
                     D-isomer-specific 2-hydroxyacid dehydrogenases related
                     repressor; cd05299"
                     /db_xref="CDD:240624"
     Site            order(86,89..90,255,304,307)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240624"
     Site            order(89,117,169..170,172..174,192..196,225..227,229,232,
                     253..255,279..280,304,306..307)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240624"
     CDS             1..430
                     /gene="CTBP1"
                     /gene_synonym="BARS; HADDTS"
                     /coded_by="NM_001377190.1:531..1823"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS93461.1"
                     /db_xref="GeneID:1487"
                     /db_xref="HGNC:HGNC:2494"
                     /db_xref="MIM:602618"
ORIGIN      
        1 msgvrppimn gplhprplva lldgrdctve mpilkdvatv afcdaqstqe ihekvlneav
       61 galmyhtitl tredlekfka lriivrigsg fdnidiksag dlgiavcnvp aasveetads
      121 tlchilnlyr ratwlhqalr egtrvqsveq irevasgaar irgetlgiig lgrvgqaval
      181 rakafgfnvl fydpylsdgv eralglqrvs tlqdllfhsd cvtlhcglne hnhhlindft
      241 vkqmrqgafl vntargglvd ekalaqalke grirgaaldv hesepfsfsq gplkdapnli
      301 ctphaawyse qasiemreea areirraitg ripdslkncv nkdhltaath wasmdpavvh
      361 pelngaaysr yppgvvgvap tgipaavegi vpsamslshg lppvahppha pspgqtvkpe
      421 adrdhasdql
//
LOCUS       NP_001340037             703 aa            linear   PRI 21-NOV-2025
DEFINITION  centrosomal protein of 63 kDa isoform a [Homo sapiens].
ACCESSION   NP_001340037
VERSION     NP_001340037.1
DBSOURCE    REFSEQ: accession NM_001353108.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Kodani,A., Knopp,K.A., Di Lullo,E., Retallack,H., Kriegstein,A.R.,
            DeRisi,J.L. and Reiter,J.F.
  TITLE     Zika virus alters centrosome organization to suppress the innate
            immune response
  JOURNAL   EMBO Rep 23 (9), e52211 (2022)
   PUBMED   35793002
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Ling,H., Cao,C.H., Han,K., Lv,Y.R., Ma,X.D., Cao,J.H., Chen,J.W.,
            Li,S., Lin,J.L., Fang,Y.J., Pan,Z.Z., Xie,D. and Wang,F.W.
  TITLE     CEP63 upregulates YAP1 to promote colorectal cancer progression
            through stabilizing RNA binding protein FXR1
  JOURNAL   Oncogene 41 (39), 4433-4445 (2022)
   PUBMED   35989368
  REMARK    GeneRIF: CEP63 upregulates YAP1 to promote colorectal cancer
            progression through stabilizing RNA binding protein FXR1.
REFERENCE   3  (residues 1 to 703)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   4  (residues 1 to 703)
  AUTHORS   Liu,C., Yu,F., Ma,R., Zhang,L., Du,G., Niu,D. and Yin,D.
  TITLE     Cep63 knockout inhibits the malignant phenotypes of papillary
            thyroid cancer cell line TPC-1
  JOURNAL   Oncol Rep 46 (3) (2021)
   PUBMED   34296302
  REMARK    GeneRIF: Cep63 knockout inhibits the malignant phenotypes of
            papillary thyroid cancer cell line TPC1.
REFERENCE   5  (residues 1 to 703)
  AUTHORS   Mahjabeen,I., Maqsood,Y., Abbasi,R., Ahmed,M.W. and Kayani,M.A.
  TITLE     Polymorphism in miRNA target sites of CEP-63 and CEP-152 ring
            complex influences expression of CEP genes and favors tumorigenesis
            in glioma
  JOURNAL   Future Oncol 17 (25), 3355-3372 (2021)
   PUBMED   34156311
  REMARK    GeneRIF: Polymorphism in miRNA target sites of CEP-63 and CEP-152
            ring complex influences expression of CEP genes and favors
            tumorigenesis in glioma.
REFERENCE   6  (residues 1 to 703)
  AUTHORS   Morris,J.A., Kandpal,G., Ma,L. and Austin,C.P.
  TITLE     DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated
            protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL:
            regulation and loss of interaction with mutation
  JOURNAL   Hum Mol Genet 12 (13), 1591-1608 (2003)
   PUBMED   12812986
REFERENCE   7  (residues 1 to 703)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   8  (residues 1 to 703)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   9  (residues 1 to 703)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   10 (residues 1 to 703)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010207.18, AC026117.15,
            AC139764.5 and AC109912.10.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein with six coiled-coil domains.
            The protein is localized to the centrosome, a non-membraneous
            organelle that functions as the major microtubule-organizing center
            in animal cells. Several alternatively spliced transcript variants
            have been found, but their biological validity has not been
            determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2057279.1,
                                           SRR1803612.273315.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000675561.1/ ENSP00000502085.1
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.2"
     Protein         1..703
                     /product="centrosomal protein of 63 kDa isoform a"
                     /note="centrosome protein CEP63; centrosomal protein
                     63kDa"
                     /calculated_mol_wt=81213
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q96MT8.1)"
     Region          18..280
                     /region_name="CEP63"
                     /note="Centrosomal protein of 63 kDa; pfam17045"
                     /db_xref="CDD:465338"
     Region          <136..474
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96MT8.1)"
     CDS             1..703
                     /gene="CEP63"
                     /gene_synonym="SCKL6"
                     /coded_by="NM_001353108.3:172..2283"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS3086.1"
                     /db_xref="GeneID:80254"
                     /db_xref="HGNC:HGNC:25815"
                     /db_xref="MIM:614724"
ORIGIN      
        1 meallegiqn rghgggflts ceaelqelmk qidimvahkk sewegrthal etclkireqe
       61 lkslrsqldv thkevgmlhq qveehekikq emtmeykqel kklheelcil krsyeklqkk
      121 qmrefrgntk nhredrseie rltakieefr qksldwekqr liyqqqvssl eaqrkalaeq
      181 seiiqaqlvn rkqklesvel ssqseiqhls sklerandti caneleierl tmrvndlvgt
      241 smtvlqeqqq keeklresek llealqeekr elkaalqsqe nliheariqk eklqekvkat
      301 ntqhaveair preeslaekk ytsqgqgdld svlsqlnfth tsedllqaev tclegslesv
      361 satckqlsqe lmekyeelkr meahnneyka eikklkeqil qgeqsyssal egmkmeishl
      421 tqelhqrdit iastkgsssd mekrlraemq kaedkavehk eildqleslk lenrhlsemv
      481 mklelglhea keisladlqe nyiealnklv senqqlqkdl mntksqleis tqmckkqndr
      541 ifkpthsrtt efkntefkpt hgqhrhdgik tehyktdlhs prgqasdsin pmsrvlspls
      601 pqispcsstr sltsyslckt hslpsaldtn eanfsdtmse smndqeefis scslpvsplg
      661 siatrfleee elrshhiler ldahieelkr esektvrqft alk
//
LOCUS       NP_001386791             438 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 42 [Homo sapiens].
ACCESSION   NP_001386791
VERSION     NP_001386791.1
DBSOURCE    REFSEQ: accession NM_001399862.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 438)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 438)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 438)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 438)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 438)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..438
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 42"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=49448
     Region          8..264
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(58,60,96..97,99,101,121,136..140,142)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(117..127,130..140)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(255,257..264)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          306..433
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..438
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001399862.1:889..2205"
                     /note="isoform 42 is encoded by transcript variant 45"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 msdgsktskf lqegnhqkle rearicrllk hpnivrlhds iseegfhylv fdlvtggelf
       61 edivareyys eadashciqq ilesvnhchl ngivhrdlkp enlllasksk gaavkladfg
      121 laievqgdqq awfgfagtpg ylspevlrkd pygkpvdmwa cgvilyillv gyppfwdedq
      181 hrlyqqikag aydfpspewd tvtpeakdli nkmltinpak ritasealkh pwicqrstva
      241 smmhrqetvd clkkfnarrk lkgailttml atrnfsaksl lkkpdgvkes tessnttied
      301 edvkarkqei ikvteqliea inngdfeayt kicdpgltaf epealgnlve gmdfhrfyfe
      361 nalsksnkpi htiilnphvh lvgddaacia yirltqymdg sgmpktmqse etrvwhrrdg
      421 kwqnvhfhrs gsptvpik
//
LOCUS       NP_001361776             328 aa            linear   PRI 21-NOV-2025
DEFINITION  protein NDRG1 isoform 2 [Homo sapiens].
ACCESSION   NP_001361776
VERSION     NP_001361776.1
DBSOURCE    REFSEQ: accession NM_001374847.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Atkinson,D., Chamova,T., Candayan,A., Kastreva,K., Asenov,O.,
            Litvinenko,I., Estrada-Cuzcano,A., De Vriendt,E., Kukushev,G.,
            Tournev,I. and Jordanova,A.
  TITLE     Identification and Characterization of Novel Founder Mutations in
            NDRG1: Refining the Genetic Landscape of Charcot-Marie-Tooth
            Disease Type 4D in Bulgaria
  JOURNAL   Int J Mol Sci 25 (16), 9047 (2024)
   PUBMED   39201732
  REMARK    GeneRIF: Identification and Characterization of Novel Founder
            Mutations in NDRG1: Refining the Genetic Landscape of
            Charcot-Marie-Tooth Disease Type 4D in Bulgaria.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Gholam Azad,M., Hussaini,M., Russell,T.M., Richardson,V., Kaya,B.,
            Dharmasivam,M. and Richardson,D.R.
  TITLE     Multi-modal mechanisms of the metastasis suppressor, NDRG1:
            Inhibition of WNT/beta-catenin signaling by stabilization of
            protein kinase Calpha
  JOURNAL   J Biol Chem 300 (7), 107417 (2024)
   PUBMED   38815861
  REMARK    GeneRIF: Multi-modal mechanisms of the metastasis suppressor,
            NDRG1: Inhibition of WNT/beta-catenin signaling by stabilization of
            protein kinase Calpha.
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Lian,Z., Tian,P., Ma,S., Chang,T., Liu,R., Feng,Q. and Li,J.
  TITLE     Long noncoding RNA MEG3 regulates cell proliferation and apoptosis
            by disrupting microRNA-9-5p-mediated inhibition of NDRG1 in
            prostate cancer
  JOURNAL   Aging (Albany NY) 16 (2), 1938-1951 (2024)
   PUBMED   38271137
  REMARK    GeneRIF: Long noncoding RNA MEG3 regulates cell proliferation and
            apoptosis by disrupting microRNA-9-5p-mediated inhibition of NDRG1
            in prostate cancer.
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Soror,A.A., Eshagh,R., Fahim,M.R., Jamshidian,A. and Monfared,G.H.
  TITLE     Prostate cancer invasion is promoted by the miR-96-5p-induced NDRG1
            deficiency through NF-kappaB regulation
  JOURNAL   Klin Onkol 38 (2), 95-101 (2024)
   PUBMED   38697817
  REMARK    GeneRIF: Prostate cancer invasion is promoted by the
            miR-96-5p-induced NDRG1 deficiency through NF-kappaB regulation.
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Hunter,M., Bernard,R., Freitas,E., Boyer,A., Morar,B.,
            Martins,I.J., Tournev,I., Jordanova,A., Guergelcheva,V.,
            Ishpekova,B., Kremensky,I., Nicholson,G., Schlotter,B.,
            Lochmuller,H., Voit,T., Colomer,J., Thomas,P.K., Levy,N. and
            Kalaydjieva,L.
  TITLE     Mutation screening of the N-myc downstream-regulated gene 1 (NDRG1)
            in patients with Charcot-Marie-Tooth Disease
  JOURNAL   Hum Mutat 22 (2), 129-135 (2003)
   PUBMED   12872253
  REMARK    GeneRIF: Two disease causing mutations in NDRG1 in
            Charcot-Marie-Tooth Disease patients.
            GeneRIF: Observational study of genotype prevalence. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 328)
  AUTHORS   van Belzen,N., Dinjens,W.N., Diesveld,M.P., Groen,N.A., van der
            Made,A.C., Nozawa,Y., Vlietstra,R., Trapman,J. and Bosman,F.T.
  TITLE     A novel gene which is up-regulated during colon epithelial cell
            differentiation and down-regulated in colorectal neoplasms
  JOURNAL   Lab Invest 77 (1), 85-92 (1997)
   PUBMED   9251681
  REMARK    GeneRIF: NDRG1 up-regulation during colon epithelial cell
            differentiation. First publication on tissue and subcellular
            expression of NDRG1.
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Kokame,K., Kato,H. and Miyata,T.
  TITLE     Homocysteine-respondent genes in vascular endothelial cells
            identified by differential display analysis. GRP78/BiP and novel
            genes
  JOURNAL   J Biol Chem 271 (47), 29659-29665 (1996)
   PUBMED   8939898
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Kalaydjieva,L., Hallmayer,J., Chandler,D., Savov,A., Nikolova,A.,
            Angelicheva,D., King,R.H., Ishpekova,B., Honeyman,K., Calafell,F.,
            Shmarov,A., Petrova,J., Turnev,I., Hristova,A., Moskov,M.,
            Stancheva,S., Petkova,I., Bittles,A.H., Georgieva,V., Middleton,L.
            and Thomas,P.K.
  TITLE     Gene mapping in Gypsies identifies a novel demyelinating neuropathy
            on chromosome 8q24
  JOURNAL   Nat Genet 14 (2), 214-217 (1996)
   PUBMED   8841199
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 4 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301641
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF192304.6, KC877358.1 and
            KC877360.1.
            
            Summary: This gene is a member of the N-myc downregulated gene
            family which belongs to the alpha/beta hydrolase superfamily. The
            protein encoded by this gene is a cytoplasmic protein involved in
            stress responses, hormone responses, cell growth, and
            differentiation. The encoded protein is necessary for p53-mediated
            caspase activation and apoptosis. Mutations in this gene are a
            cause of Charcot-Marie-Tooth disease type 4D, and expression of
            this gene may be a prognostic indicator for several types of
            cancer. Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene. [provided by RefSeq, May
            2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2075579.1,
                                           SRR14038197.1788694.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.22"
     Protein         1..328
                     /product="protein NDRG1 isoform 2"
                     /note="differentiation-related gene 1 protein;
                     nickel-specific induction protein Cap43; reducing agents
                     and tunicamycin-responsive protein; protein regulated by
                     oxygen-1; protein NDRG1; N-myc downstream-regulated gene 1
                     protein"
                     /calculated_mol_wt=35390
     Region          1..250
                     /region_name="Ndr"
                     /note="Ndr family; pfam03096"
                     /db_xref="CDD:397285"
     CDS             1..328
                     /gene="NDRG1"
                     /gene_synonym="CAP43; CMT4D; DRG-1; DRG1; GC4; HMSNL;
                     NDR1; NMSL; PROXY1; RIT42; RTP; TARG1; TDD5"
                     /coded_by="NM_001374847.1:255..1241"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS59113.1"
                     /db_xref="GeneID:10397"
                     /db_xref="HGNC:HGNC:7679"
                     /db_xref="MIM:605262"
ORIGIN      
        1 mnhktcynpl fnyedmqeit qhfavchvda pgqqdgaasf pagymypsmd qlaemlpgvl
       61 qqfglksiig mgtgagayil trfalnnpem veglvlinvn pcaegwmdwa askisgwtqa
      121 lpdmvvshlf gkeemqsnve vvhtyrqhiv ndmnpgnlhl finaynsrrd leierpmpgt
      181 htvtlqcpal lvvgdsspav davvecnskl dptkttllkm adcgglpqis qpaklaeafk
      241 yfvqgmgymp sasmtrlmrs rtasgssvts ldgtrsrsht segtrsrsht segtrsrsht
      301 segahlditp nsgaagnsag pksmevsc
//
LOCUS       NP_001147024              54 aa            linear   PRI 21-NOV-2025
DEFINITION  short coiled-coil protein isoform 3 [Homo sapiens].
ACCESSION   NP_001147024
VERSION     NP_001147024.2
DBSOURCE    REFSEQ: accession NM_001153552.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 54)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 54)
  AUTHORS   Wirth,M., Mouilleron,S., Zhang,W., Sjottem,E., Princely Abudu,Y.,
            Jain,A., Lauritz Olsvik,H., Bruun,J.A., Razi,M., Jefferies,H.B.J.,
            Lee,R., Joshi,D., O'Reilly,N., Johansen,T. and Tooze,S.A.
  TITLE     Phosphorylation of the LIR Domain of SCOC Modulates ATG8 Binding
            Affinity and Specificity
  JOURNAL   J Mol Biol 433 (13), 166987 (2021)
   PUBMED   33845085
  REMARK    GeneRIF: Phosphorylation of the LIR Domain of SCOC Modulates ATG8
            Binding Affinity and Specificity.
            Erratum:[J Mol Biol. 2021 Jul 23;433(15):167049. doi:
            10.1016/j.jmb.2021.167049. PMID: 34052024]
REFERENCE   3  (residues 1 to 54)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 54)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 54)
  AUTHORS   Stringer,S., Minica,C.C., Verweij,K.J., Mbarek,H., Bernard,M.,
            Derringer,J., van Eijk,K.R., Isen,J.D., Loukola,A.,
            Maciejewski,D.F., Mihailov,E., van der Most,P.J., Sanchez-Mora,C.,
            Roos,L., Sherva,R., Walters,R., Ware,J.J., Abdellaoui,A.,
            Bigdeli,T.B., Branje,S.J., Brown,S.A., Bruinenberg,M., Casas,M.,
            Esko,T., Garcia-Martinez,I., Gordon,S.D., Harris,J.M.,
            Hartman,C.A., Henders,A.K., Heath,A.C., Hickie,I.B., Hickman,M.,
            Hopfer,C.J., Hottenga,J.J., Huizink,A.C., Irons,D.E., Kahn,R.S.,
            Korhonen,T., Kranzler,H.R., Krauter,K., van Lier,P.A., Lubke,G.H.,
            Madden,P.A., Magi,R., McGue,M.K., Medland,S.E., Meeus,W.H.,
            Miller,M.B., Montgomery,G.W., Nivard,M.G., Nolte,I.M.,
            Oldehinkel,A.J., Pausova,Z., Qaiser,B., Quaye,L.,
            Ramos-Quiroga,J.A., Richarte,V., Rose,R.J., Shin,J.,
            Stallings,M.C., Stiby,A.I., Wall,T.L., Wright,M.J., Koot,H.M.,
            Paus,T., Hewitt,J.K., Ribases,M., Kaprio,J., Boks,M.P., Snieder,H.,
            Spector,T., Munafo,M.R., Metspalu,A., Gelernter,J., Boomsma,D.I.,
            Iacono,W.G., Martin,N.G., Gillespie,N.A., Derks,E.M. and Vink,J.M.
  TITLE     Genome-wide association study of lifetime cannabis use based on a
            large meta-analytic sample of 32 330 subjects from the
            International Cannabis Consortium
  JOURNAL   Transl Psychiatry 6 (3), e769 (2016)
   PUBMED   27023175
  REMARK    GeneRIF: SCOC SNPs were associated with lifetime cannabis use, but
            the association did not reach genome-wide significance.
            [Meta-Analysis]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 54)
  AUTHORS   Alborghetti,M.R., Furlan Ada,S., da Silva,J.C., Sforca,M.L.,
            Honorato,R.V., Granato,D.C., dos Santos Migueleti,D.L., Neves,J.L.,
            de Oliveira,P.S., Paes-Leme,A.F., Zeri,A.C., de Torriani,I.C. and
            Kobarg,J.
  TITLE     Structural analysis of intermolecular interactions in the kinesin
            adaptor complex fasciculation and elongation protein zeta 1/ short
            coiled-coil protein (FEZ1/SCOCO)
  JOURNAL   PLoS One 8 (10), e76602 (2013)
   PUBMED   24116125
  REMARK    GeneRIF: Studies indicate that FEZ1 (fasciculation and elongation
            protein zeta 1), SCOCO (short coiled-coil protein) and kinesins
            (kinesin heavy chain) are involved in biological transport process.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 54)
  AUTHORS   Behrens,C., Binotti,B., Schmidt,C., Robinson,C.V., Chua,J.J. and
            Kuhnel,K.
  TITLE     Crystal structure of the human short coiled coil protein and
            insights into SCOC-FEZ1 complex formation
  JOURNAL   PLoS One 8 (10), e76355 (2013)
   PUBMED   24098481
  REMARK    GeneRIF: SCOC forms a stable homogeneous complex with the coiled
            coil domain of FEZ1. SCOC dimerization and the SCOC surface residue
            R117 are important for this interaction.
            Erratum:[PLoS One. 2013;8(10).
            doi:10.1371/annotation/cb60d973-58aa-45e0-bbb3-1c7f5a42a8d2]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 54)
  AUTHORS   McKnight,N.C., Jefferies,H.B., Alemu,E.A., Saunders,R.E.,
            Howell,M., Johansen,T. and Tooze,S.A.
  TITLE     Genome-wide siRNA screen reveals amino acid starvation-induced
            autophagy requires SCOC and WAC
  JOURNAL   EMBO J 31 (8), 1931-1946 (2012)
   PUBMED   22354037
  REMARK    GeneRIF: The identification of SCOC and WAC as novel regulatory
            proteins with diverse functions in autophagy contributes towards a
            fuller understanding of autophagosome formation.
REFERENCE   9  (residues 1 to 54)
  AUTHORS   Miyamoto-Sato,E., Fujimori,S., Ishizaka,M., Hirai,N., Masuoka,K.,
            Saito,R., Ozawa,Y., Hino,K., Washio,T., Tomita,M., Yamashita,T.,
            Oshikubo,T., Akasaka,H., Sugiyama,J., Matsumoto,Y. and Yanagawa,H.
  TITLE     A comprehensive resource of interacting protein regions for
            refining human transcription factor networks
  JOURNAL   PLoS One 5 (2), e9289 (2010)
   PUBMED   20195357
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 54)
  AUTHORS   Van Valkenburgh,H., Shern,J.F., Sharer,J.D., Zhu,X. and Kahn,R.A.
  TITLE     ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both
            specific and shared effectors: characterizing ARL1-binding proteins
  JOURNAL   J Biol Chem 276 (25), 22826-22837 (2001)
   PUBMED   11303027
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093671.3.
            
            On Jun 5, 2020 this sequence version replaced NP_001147024.1.
            
            Summary: This gene encodes a short coiled-coiled domain-containing
            protein that localizes to the Golgi apparatus. The encoded protein
            interacts with ADP-ribosylation factor-like proteins. Pseudogenes
            of this gene are found on chromosomes 1 and 14. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Apr 2009].
            
            Transcript Variant: This variant (3) lacks an in-frame exon in the
            coding region, compared to variant 1. The encoded isoform (3) is
            shorter compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF448857.1, SRR14372080.731559.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..54
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.1"
     Protein         1..54
                     /product="short coiled-coil protein isoform 3"
                     /calculated_mol_wt=5979
     Region          <1..45
                     /region_name="DUF2205"
                     /note="Short coiled-coil protein; pfam10224"
                     /db_xref="CDD:431150"
     CDS             1..54
                     /gene="SCOC"
                     /gene_synonym="HRIHFB2072; SCOCO; UNC-69"
                     /coded_by="NM_001153552.2:123..287"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS54807.2"
                     /db_xref="GeneID:60592"
                     /db_xref="HGNC:HGNC:20335"
ORIGIN      
        1 mmnadmddls arvdavkeen lklksenqvl gqyienlmsa ssvfqttdtk skrk
//
LOCUS       NP_001909                482 aa            linear   PRI 21-NOV-2025
DEFINITION  lipoamide acyltransferase component of branched-chain alpha-keto
            acid dehydrogenase complex, mitochondrial isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001909
VERSION     NP_001909.4
DBSOURCE    REFSEQ: accession NM_001918.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Hwang,R.D., Lu,Y., Tang,Q., Periz,G., Park,G., Li,X., Xiang,Q.,
            Liu,Y., Zhang,T. and Wang,J.
  TITLE     DBT is a metabolic switch for maintenance of proteostasis under
            proteasomal impairment
  JOURNAL   Elife 12, 91002 (2024)
   PUBMED   39255192
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Zhang,C., Huang,G., Yang,J., Jiang,Y., Huang,R., Ye,Z., Huang,Y.,
            Hu,H. and Xi,X.
  TITLE     Overexpression of DBT suppresses the aggressiveness of renal clear
            cell carcinoma and correlates with immune infiltration
  JOURNAL   Front Immunol 14, 1197011 (2023)
   PUBMED   37383233
  REMARK    GeneRIF: Overexpression of DBT suppresses the aggressiveness of
            renal clear cell carcinoma and correlates with immune infiltration.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Alijanpour,M., Jazayeri,O., Soleimani Amiri,S. and Brosens,E.
  TITLE     Pathogenic Homozygous Mutations in the DBT Gene (c.1174A>C) Result
            in Maple Syrup Urine Disease in a rs12021720 Carrier
  JOURNAL   Lab Med 53 (6), 596-601 (2022)
   PUBMED   35657820
  REMARK    GeneRIF: Pathogenic Homozygous Mutations in the DBT Gene
            (c.1174A>C) Result in Maple Syrup Urine Disease in a rs12021720
            Carrier.
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Tsuruta,M., Mitsubuchi,H., Mardy,S., Miura,Y., Hayashida,Y.,
            Kinugasa,A., Ishitsu,T., Matsuda,I. and Indo,Y.
  TITLE     Molecular basis of intermittent maple syrup urine disease: novel
            mutations in the E2 gene of the branched-chain alpha-keto acid
            dehydrogenase complex
  JOURNAL   J Hum Genet 43 (2), 91-100 (1998)
   PUBMED   9621512
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Strauss,K.A., Puffenberger,E.G. and Carson,V.J.
  TITLE     Maple Syrup Urine Disease
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301495
REFERENCE   7  (residues 1 to 482)
  AUTHORS   Lau,K.S., Herring,W.J., Chuang,J.L., McKean,M., Danner,D.J.,
            Cox,R.P. and Chuang,D.T.
  TITLE     Structure of the gene encoding dihydrolipoyl transacylase (E2)
            component of human branched chain alpha-keto acid dehydrogenase
            complex and characterization of an E2 pseudogene
  JOURNAL   J Biol Chem 267 (33), 24090-24096 (1992)
   PUBMED   1429740
REFERENCE   8  (residues 1 to 482)
  AUTHORS   Lau,K.S., Chuang,J.L., Herring,W.J., Danner,D.J., Cox,R.P. and
            Chuang,D.T.
  TITLE     The complete cDNA sequence for dihydrolipoyl transacylase (E2) of
            human branched-chain alpha-keto acid dehydrogenase complex
  JOURNAL   Biochim Biophys Acta 1132 (3), 319-321 (1992)
   PUBMED   1420314
REFERENCE   9  (residues 1 to 482)
  AUTHORS   Zneimer,S.M., Lau,K.S., Eddy,R.L., Shows,T.B., Chuang,J.L.,
            Chuang,D.T. and Cox,R.P.
  TITLE     Regional assignment of two genes of the human branched-chain
            alpha-keto acid dehydrogenase complex: the E1 beta gene (BCKDHB) to
            chromosome 6p21-22 and the E2 gene (DBT) to chromosome 1p31
  JOURNAL   Genomics 10 (3), 740-747 (1991)
   PUBMED   1889817
REFERENCE   10 (residues 1 to 482)
  AUTHORS   Fisher,C.W., Lau,K.S., Fisher,C.R., Wynn,R.M., Cox,R.P. and
            Chuang,D.T.
  TITLE     A 17-bp insertion and a Phe215----Cys missense mutation in the
            dihydrolipoyl transacylase (E2) mRNA from a thiamine-responsive
            maple syrup urine disease patient WG-34
  JOURNAL   Biochem Biophys Res Commun 174 (2), 804-809 (1991)
   PUBMED   1847055
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA274670.1, BC016675.1,
            AL445928.8 and AK024946.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 18, 2020 this sequence version replaced NP_001909.3.
            
            Summary: The branched-chain alpha-keto acid dehydrogenase complex
            (BCKD) is an inner-mitochondrial enzyme complex involved in the
            breakdown of the branched-chain amino acids isoleucine, leucine,
            and valine. The BCKD complex is thought to be composed of a core of
            24 transacylase (E2) subunits, and associated decarboxylase (E1),
            dehydrogenase (E3), and regulatory subunits. This gene encodes the
            transacylase (E2) subunit. Mutations in this gene result in maple
            syrup urine disease, type 2. Alternatively spliced transcript
            variants have been described, but their biological validity has not
            been determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X66785.1, SRR1803614.179918.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000370132.8/
                                                  ENSP00000359151.3
            RefSeq Select criteria             :: based on manual assertion,
                                                  conservation, expression,
                                                  longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p21.2"
     Protein         1..482
                     /product="lipoamide acyltransferase component of
                     branched-chain alpha-keto acid dehydrogenase complex,
                     mitochondrial isoform 1 precursor"
                     /EC_number="2.3.1.168"
                     /note="branched chain acyltransferase, E2 component;
                     dihydrolipoyl transacylase; dihydrolipoyllysine-residue
                     (2-methylpropanoyl)transferase; lipoamide acyltransferase
                     component of mitochondrial branched-chain alpha-keto acid
                     dehydrogenase complex; BCKAD E2 subunit; mitochondrial
                     branched chain alpha-keto acid dehydrogenase transacylase
                     subunit (E2b); E2 component of branched chain alpha-keto
                     acid dehydrogenase complex; branched chain 2-oxo-acid
                     dehydrogenase complex component E2; 52 kDa mitochondrial
                     autoantigen of primary biliary cirrhosis; lipoamide
                     acyltransferase component of branched-chain alpha-keto
                     acid dehydrogenase complex, mitochondrial; branched-chain
                     alpha-keto acid dehydrogenase complex component E2;
                     dihydrolipoamide acetyltransferase component of
                     branched-chain alpha-keto acid dehydrogenase complex"
                     /calculated_mol_wt=46400
     transit_peptide 1..61
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P11182.4)"
                     /calculated_mol_wt=7135
     mat_peptide     62..482
                     /product="Lipoamide acyltransferase component of
                     branched-chain alpha-keto acid dehydrogenase complex,
                     mitochondrial. /id=PRO_0000020489"
                     /note="propagated from UniProtKB/Swiss-Prot (P11182.4)"
                     /calculated_mol_wt=46400
     Region          67..482
                     /region_name="PLN02528"
                     /note="2-oxoisovalerate dehydrogenase E2 component"
                     /db_xref="CDD:215289"
     Region          145..160
                     /region_name="Critical for association with PPM1K.
                     /evidence=ECO:0000269|PubMed:22291014"
                     /note="propagated from UniProtKB/Swiss-Prot (P11182.4)"
     Region          147..168
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11182.4)"
     Site            196
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P53395; propagated from
                     UniProtKB/Swiss-Prot (P11182.4)"
     Site            202
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P53395; propagated from
                     UniProtKB/Swiss-Prot (P11182.4)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P11182.4)"
     Site            243
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P53395; propagated from
                     UniProtKB/Swiss-Prot (P11182.4)"
     Site            250
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P53395; propagated from
                     UniProtKB/Swiss-Prot (P11182.4)"
     Site            289
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P53395; propagated from
                     UniProtKB/Swiss-Prot (P11182.4)"
     Site            295
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P11182.4)"
     Site            304
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P53395; propagated from
                     UniProtKB/Swiss-Prot (P11182.4)"
     Site            435
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P53395; propagated from
                     UniProtKB/Swiss-Prot (P11182.4)"
     Site            440
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P53395; propagated from
                     UniProtKB/Swiss-Prot (P11182.4)"
     CDS             1..482
                     /gene="DBT"
                     /gene_synonym="BCATE2; BCKAD-E2; BCKADE2; BCKDH-E2;
                     BCOADC-E2; E2; E2B"
                     /coded_by="NM_001918.5:15..1463"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS767.1"
                     /db_xref="GeneID:1629"
                     /db_xref="HGNC:HGNC:2698"
                     /db_xref="MIM:248610"
ORIGIN      
        1 maavrmlrtw srnagklicv ryfqtcgnvh vlkpnyvcff gypsfkyshp hhflkttaal
       61 rgqvvqfkls digegirevt vkewyvkegd tvsqfdsice vqsdkasvti tsrydgvikk
      121 lyynlddiay vgkplvdiet ealkdseedv vetpavshde hthqeikgrk tlatpavrrl
      181 amenniklse vvgsgkdgri lkedilnyle kqtgailpps pkveimpppp kpkdmtvpil
      241 vskppvftgk dktepikgfq kamvktmsaa lkiphfgycd eidltelvkl reelkpiafa
      301 rgiklsfmpf flkaaslgll qfpilnasvd encqnityka shnigiamdt eqglivpnvk
      361 nvqicsifdi atelnrlqkl gsvsqlsttd ltggtftlsn igsiggtfak pvimppevai
      421 galgsikaip rfnqkgevyk aqimnvswsa dhrvidgatm srfsnlwksy lenpafmlld
      481 lk
//
LOCUS       NP_065857                769 aa            linear   PRI 21-NOV-2025
DEFINITION  gephyrin isoform 1 [Homo sapiens].
ACCESSION   NP_065857
VERSION     NP_065857.1
DBSOURCE    REFSEQ: accession NM_020806.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Dos Reis,R., Kornobis,E., Pereira,A., Tores,F., Carrasco,J.,
            Gautier,C., Jahannault-Talignani,C., Nitschke,P., Muchardt,C.,
            Schlosser,A., Maric,H.M., Ango,F. and Allemand,E.
  TITLE     Complex regulation of Gephyrin splicing is a determinant of
            inhibitory postsynaptic diversity
  JOURNAL   Nat Commun 13 (1), 3507 (2022)
   PUBMED   35717442
  REMARK    GeneRIF: Complex regulation of Gephyrin splicing is a determinant
            of inhibitory postsynaptic diversity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 769)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 769)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 769)
  AUTHORS   Mammoto,A., Sasaki,T., Asakura,T., Hotta,I., Imamura,H.,
            Takahashi,K., Matsuura,Y., Shirao,T. and Takai,Y.
  TITLE     Interactions of drebrin and gephyrin with profilin
  JOURNAL   Biochem Biophys Res Commun 243 (1), 86-89 (1998)
   PUBMED   9473484
REFERENCE   6  (residues 1 to 769)
  AUTHORS   Meyer,G., Kirsch,J., Betz,H. and Langosch,D.
  TITLE     Identification of a gephyrin binding motif on the glycine receptor
            beta subunit
  JOURNAL   Neuron 15 (3), 563-572 (1995)
   PUBMED   7546736
REFERENCE   7  (residues 1 to 769)
  AUTHORS   Misko,A., Mahtani,K., Abbott,J., Schwarz,G. and Atwal,P.
  TITLE     Molybdenum Cofactor Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   34870926
REFERENCE   8  (residues 1 to 769)
  AUTHORS   Balint,B. and Thomas,R.
  TITLE     Hereditary Hyperekplexia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301437
REFERENCE   9  (residues 1 to 769)
  AUTHORS   Prior,P., Schmitt,B., Grenningloh,G., Pribilla,I., Multhaup,G.,
            Beyreuther,K., Maulet,Y., Werner,P., Langosch,D., Kirsch,J. et al.
  TITLE     Primary structure and alternative splice variants of gephyrin, a
            putative glycine receptor-tubulin linker protein
  JOURNAL   Neuron 8 (6), 1161-1170 (1992)
   PUBMED   1319186
REFERENCE   10 (residues 1 to 769)
  AUTHORS   Kirsch,J., Langosch,D., Prior,P., Littauer,U.Z., Schmitt,B. and
            Betz,H.
  TITLE     The 93-kDa glycine receptor-associated protein binds to tubulin
  JOURNAL   J Biol Chem 266 (33), 22242-22245 (1991)
   PUBMED   1657993
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355093.3, AL133241.3,
            AL117667.4, AL049835.3, AL159179.3 and AL135978.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a neuronal assembly protein that anchors
            inhibitory neurotransmitter receptors to the postsynaptic
            cytoskeleton via high affinity binding to a receptor subunit domain
            and tubulin dimers. In nonneuronal tissues, the encoded protein is
            also required for molybdenum cofactor biosynthesis. Mutations in
            this gene may be associated with the neurological condition
            hyperplexia and also lead to molybdenum cofactor deficiency.
            Numerous alternatively spliced transcript variants encoding
            different isoforms have been described; however, the full-length
            nature of all transcript variants is not currently known. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1), also known as GephP1,
            represents the longer transcript and encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC030016.2, AK315569.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000478722.6/ ENSP00000417901.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3-q24.1"
     Protein         1..769
                     /product="gephyrin isoform 1"
                     /EC_number="2.10.1.1"
                     /EC_number="2.7.7.75"
                     /calculated_mol_wt=83317
     Region          15..169
                     /region_name="MogA_MoaB"
                     /note="MogA_MoaB family. Members of this family are
                     involved in biosynthesis of the molybdenum cofactor (MoCF)
                     an essential cofactor of a diverse group of redox enzymes.
                     MoCF biosynthesis is an evolutionarily conserved pathway
                     present in eubacteria, archaea; cd00886"
                     /db_xref="CDD:238451"
     Site            order(87..89,119,145..146,150,153)
                     /site_type="active"
                     /note="MPT binding site [active]"
                     /db_xref="CDD:238451"
     Site            order(89,91..92,94,98,106..108,113,116..117,127,130,169)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:238451"
     Region          360..766
                     /region_name="MoeA"
                     /note="MoeA family. Members of this family are involved in
                     biosynthesis of the molybdenum cofactor (MoCF), an
                     essential cofactor of a diverse group of redox enzymes.
                     MoCF biosynthesis is an evolutionarily conserved pathway
                     present in eubacteria, archaea and...; cd00887"
                     /db_xref="CDD:238452"
     Site            order(381,496,511..514,516,519..520,522,556,558,561,690,
                     731,762)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238452"
     Site            order(539..540,542,582,606)
                     /site_type="active"
                     /note="putative functional site [active]"
                     /db_xref="CDD:238452"
     Site            order(606..608,658..659,663,666)
                     /site_type="active"
                     /note="putative MPT binding site [active]"
                     /db_xref="CDD:238452"
     CDS             1..769
                     /gene="GPHN"
                     /gene_synonym="GEPH; GPH; GPHRYN; HKPX1; MOCODC"
                     /coded_by="NM_020806.5:382..2691"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9777.1"
                     /db_xref="GeneID:10243"
                     /db_xref="HGNC:HGNC:15465"
                     /db_xref="MIM:603930"
ORIGIN      
        1 mategmiltn hdhqirvgvl tvsdscfrnl aedrsginlk dlvqdpsllg gtisaykivp
       61 deieeiketl idwcdekeln lilttggtgf aprdvtpeat keviereapg malamlmgsl
      121 nvtplgmlsr pvcgirgktl iinlpgskkg sqecfqfilp alphaidllr daivkvkevh
      181 deledlpspp pplsppptts phkqtedkgv qceeeeeekk dsgvasteds ssshitaaai
      241 aakkhpfyts pavvmahgeq pipglinysh hstderipds iisrgvqvlp rdtaslsttp
      301 sespraqats rlstascptp kvqsrcsske nilrashsav ditkvarrhr mspfpltsmd
      361 kafitvlemt pvlgteiiny rdgmgrvlaq dvyakdnlpp fpasvkdgya vraadgpgdr
      421 fiigesqage qptqtvmpgq vmrvttgapi pcgadavvqv edteliresd dgteelevri
      481 lvqarpgqdi rpighdikrg ecvlakgthm gpseigllat vgvtevevnk fpvvavmstg
      541 nellnpeddl lpgkirdsnr stllatiqeh gyptinlgiv gdnpddllna lnegisradv
      601 iitsggvsmg ekdylkqvld idlhaqihfg rvfmkpglpt tfatldidgv rkiifalpgn
      661 pvsavvtcnl fvvpalrkmq gildprptii karlscdvkl dprpeyhrci ltwhhqeplp
      721 waqstgnqms srlmsmrsan gllmlppkte qyvelhkgev vdvmvigrl
//
LOCUS       NP_001139585             370 aa            linear   PRI 21-NOV-2025
DEFINITION  mesoderm induction early response protein 1 isoform i [Homo
            sapiens].
ACCESSION   NP_001139585
VERSION     NP_001139585.1
DBSOURCE    REFSEQ: accession NM_001146113.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Wang,S., Fairall,L., Pham,T.K., Ragan,T.J., Vashi,D., Collins,M.O.,
            Dominguez,C. and Schwabe,J.W.R.
  TITLE     A potential histone-chaperone activity for the MIER1 histone
            deacetylase complex
  JOURNAL   Nucleic Acids Res 51 (12), 6006-6019 (2023)
   PUBMED   37099381
  REMARK    GeneRIF: A potential histone-chaperone activity for the MIER1
            histone deacetylase complex.
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 370)
  AUTHORS   McCarthy,P.L., Mercer,F.C., Savicky,M.W., Carter,B.A., Paterno,G.D.
            and Gillespie,L.L.
  TITLE     Changes in subcellular localisation of MI-ER1 alpha, a novel
            oestrogen receptor-alpha interacting protein, is associated with
            breast cancer progression
  JOURNAL   Br J Cancer 99 (4), 639-646 (2008)
   PUBMED   18665173
  REMARK    GeneRIF: Loss of nuclear MI-ER1 alpha might contribute to the
            development of invasive breast carcinoma
REFERENCE   6  (residues 1 to 370)
  AUTHORS   Wang,L., Charroux,B., Kerridge,S. and Tsai,C.C.
  TITLE     Atrophin recruits HDAC1/2 and G9a to modify histone H3K9 and to
            determine cell fates
  JOURNAL   EMBO Rep 9 (6), 555-562 (2008)
   PUBMED   18451879
REFERENCE   7  (residues 1 to 370)
  AUTHORS   Ding,Z., Gillespie,L.L., Mercer,F.C. and Paterno,G.D.
  TITLE     The SANT domain of human MI-ER1 interacts with Sp1 to interfere
            with GC box recognition and repress transcription from its own
            promoter
  JOURNAL   J Biol Chem 279 (27), 28009-28016 (2004)
   PUBMED   15117948
  REMARK    GeneRIF: the association of hMI-ER1 with Sp1 represents a novel
            mechanism for the negative regulation of Sp1 target promoters
REFERENCE   8  (residues 1 to 370)
  AUTHORS   Ding,Z., Gillespie,L.L. and Paterno,G.D.
  TITLE     Human MI-ER1 alpha and beta function as transcriptional repressors
            by recruitment of histone deacetylase 1 to their conserved ELM2
            domain
  JOURNAL   Mol Cell Biol 23 (1), 250-258 (2003)
   PUBMED   12482978
  REMARK    GeneRIF: we investigated the role of hMI-ER1alpha and hMI-ER1beta
            in the regulation of transcription.We demonstrate that this
            repressor activity is due to interaction and recruitment of a
            trichostatin A-sensitive histone deacetylase 1 (HDAC1).
REFERENCE   9  (residues 1 to 370)
  AUTHORS   Paterno,G.D., Ding,Z., Lew,Y.Y., Nash,G.W., Mercer,F.C. and
            Gillespie,L.L.
  TITLE     Genomic organization of the human mi-er1 gene and characterization
            of alternatively spliced isoforms: regulated use of a facultative
            intron determines subcellular localization
  JOURNAL   Gene 295 (1), 79-88 (2002)
   PUBMED   12242014
  REMARK    GeneRIF: Results demonstrate that alternate use of a facultative
            intron regulates the subcellular localization of hMI-ER1 proteins
            and this may have important implications for hMI-ER1 function.
REFERENCE   10 (residues 1 to 370)
  AUTHORS   Paterno,G.D., Mercer,F.C., Chayter,J.J., Yang,X., Robb,J.D. and
            Gillespie,L.L.
  TITLE     Molecular cloning of human er1 cDNA and its differential expression
            in breast tumours and tumour-derived cell lines
  JOURNAL   Gene 222 (1), 77-82 (1998)
   PUBMED   9813250
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK302061.1, BC125217.1,
            AL500525.4 and BM987758.1.
            
            Summary: This gene encodes a protein that was first identified in
            Xenopus laevis by its role in a mesoderm induction early response
            (MIER). The encoded protein functions as a transcriptional
            regulator. Alternatively spliced transcript variants encode
            multiple isoforms, some of which lack a C-terminal nuclear
            localization signal. [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (9) lacks two alternate exons in
            the 5' coding region, initiates translation at a downsteram
            in-frame start codon, and lacks an alternate segment in the 3'
            coding region, compared to variant 1. The resulting isoform (i) has
            a shorter N-terminus and a shorter and distinct C-terminus,
            compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC125217.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1968832 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..370
                     /product="mesoderm induction early response protein 1
                     isoform i"
                     /note="mesoderm induction early response protein 1;
                     mesoderm induction early response 1 homolog; mesoderm
                     induction early response 1, transcriptional regulator"
                     /calculated_mol_wt=42044
     Region          119..168
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          225..269
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(225,255..256,258..259,261..263,265..267)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          279..>344
                     /region_name="MIER1_3_C"
                     /note="Mesoderm induction early response protein 1/3
                     C-terminal; pfam19426"
                     /db_xref="CDD:437258"
     CDS             1..370
                     /gene="MIER1"
                     /gene_synonym="ER1; MI-ER1"
                     /coded_by="NM_001146113.2:242..1354"
                     /note="isoform i is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS53330.1"
                     /db_xref="GeneID:57708"
                     /db_xref="HGNC:HGNC:29657"
                     /db_xref="MIM:616848"
ORIGIN      
        1 mpihellsly gygstvrlpe edeeeeeeee egeddedadn ddnsgcsgen keenikdssg
       61 qedetqssnd dpsqsvasqd aqeiirprrc kyfdtnseve eeseededyi psedwkkeim
      121 vgsmfqaeip vgicrykene kvyenddqll wdpeylpedk viiflkdasr rtgdekgvea
      181 ipegshikdn eqalyelvkc nfdteealrr lrfnvkaare elsvwteeec rnfeqglkay
      241 gkdfhliqan kvrtrsvgec vafyymwkks erydffaqqt rfgkkkynlh pgvtdymdrl
      301 ldesesaass rapsppptas nssnsqseke dgtvstanqn gvssngpgil qmllpvhfsa
      361 issranaflk
//
LOCUS       NP_001358090            1199 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal cell adhesion molecule isoform N precursor [Homo sapiens].
ACCESSION   NP_001358090 XP_005250442
VERSION     NP_001358090.1
DBSOURCE    REFSEQ: accession NM_001371161.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1199)
  AUTHORS   Wang,C., Wang,Z., Fu,L., Du,J., Ji,F. and Qiu,X.
  TITLE     CircNRCAM up-regulates NRCAM to promote papillary thyroid carcinoma
            progression
  JOURNAL   J Endocrinol Invest 47 (5), 1215-1226 (2024)
   PUBMED   38485895
  REMARK    GeneRIF: CircNRCAM up-regulates NRCAM to promote papillary thyroid
            carcinoma progression.
REFERENCE   2  (residues 1 to 1199)
  AUTHORS   Zhou,L., He,L., Liu,C.H., Qiu,H., Zheng,L., Sample,K.M., Wu,Q.,
            Li,J., Xie,K., Ampuero,J., Li,Z., Lv,D., Liu,M., Romero-Gomez,M.,
            Hu,Y. and Tang,H.
  TITLE     Liver cancer stem cell dissemination and metastasis: uncovering the
            role of NRCAM in hepatocellular carcinoma
  JOURNAL   J Exp Clin Cancer Res 42 (1), 311 (2023)
   PUBMED   37993901
  REMARK    GeneRIF: Liver cancer stem cell dissemination and metastasis:
            uncovering the role of NRCAM in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1199)
  AUTHORS   Sannes,A.C., Christensen,J.O., Nielsen,M.B. and Gjerstad,J.
  TITLE     Stress-induced headache in the general working population is
            moderated by the NRCAM rs2300043 genotype
  JOURNAL   Scand J Pain 23 (2), 326-332 (2022)
   PUBMED   36181733
  REMARK    GeneRIF: Stress-induced headache in the general working population
            is moderated by the NRCAM rs2300043 genotype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1199)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 1199)
  AUTHORS   Bai,C. and Chen,D.G.
  TITLE     NRCAM acts as a prognostic biomarker and promotes the tumor
            progression in gastric cancer via EMT pathway
  JOURNAL   Tissue Cell 77, 101859 (2022)
   PUBMED   35763884
  REMARK    GeneRIF: NRCAM acts as a prognostic biomarker and promotes the
            tumor progression in gastric cancer via EMT pathway.
REFERENCE   6  (residues 1 to 1199)
  AUTHORS   Wang,B., Williams,H., Du,J.S., Terrett,J. and Kenwrick,S.
  TITLE     Alternative splicing of human NrCAM in neural and nonneural tissues
  JOURNAL   Mol Cell Neurosci 10 (5-6), 287-295 (1998)
   PUBMED   9604207
REFERENCE   7  (residues 1 to 1199)
  AUTHORS   Grumet,M.
  TITLE     Nr-CAM: a cell adhesion molecule with ligand and receptor functions
  JOURNAL   Cell Tissue Res 290 (2), 423-428 (1997)
   PUBMED   9321706
  REMARK    Review article
REFERENCE   8  (residues 1 to 1199)
  AUTHORS   Sakurai,T., Lustig,M., Nativ,M., Hemperly,J.J., Schlessinger,J.,
            Peles,E. and Grumet,M.
  TITLE     Induction of neurite outgrowth through contactin and Nr-CAM by
            extracellular regions of glial receptor tyrosine phosphatase beta
  JOURNAL   J Cell Biol 136 (4), 907-918 (1997)
   PUBMED   9049255
REFERENCE   9  (residues 1 to 1199)
  AUTHORS   Volkmer,H., Leuschner,R., Zacharias,U. and Rathjen,F.G.
  TITLE     Neurofascin induces neurites by heterophilic interactions with
            axonal NrCAM while NrCAM requires F11 on the axonal surface to
            extend neurites
  JOURNAL   J Cell Biol 135 (4), 1059-1069 (1996)
   PUBMED   8922386
REFERENCE   10 (residues 1 to 1199)
  AUTHORS   Lane,R.P., Chen,X.N., Yamakawa,K., Vielmetter,J., Korenberg,J.R.
            and Dreyer,W.J.
  TITLE     Characterization of a highly conserved human homolog to the chicken
            neural cell surface protein Bravo/Nr-CAM that maps to chromosome
            band 7q31
  JOURNAL   Genomics 35 (3), 456-465 (1996)
   PUBMED   8812479
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005058.1, AC007567.2 and
            AC005683.2.
            
            On Jun 30, 2019 this sequence version replaced XP_005250442.1.
            
            Summary: Cell adhesion molecules (CAMs) are members of the
            immunoglobulin superfamily. This gene encodes a neuronal cell
            adhesion molecule with multiple immunoglobulin-like C2-type domains
            and fibronectin type-III domains. This ankyrin-binding protein is
            involved in neuron-neuron adhesion and promotes directional
            signaling during axonal cone growth. This gene is also expressed in
            non-neural tissues and may play a general role in cell-cell
            communication via signaling from its intracellular domain to the
            actin cytoskeleton during directional cell migration. Allelic
            variants of this gene have been associated with autism and
            addiction vulnerability. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (42), as well as variant 41,
            encodes isoform N.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1199
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1199
                     /product="neuronal cell adhesion molecule isoform N
                     precursor"
                     /note="NgCAM-related cell adhesion molecule; neuronal
                     surface protein Bravo"
                     /calculated_mol_wt=129441
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3315
     Region          46..140
                     /region_name="IgI_NrCAM"
                     /note="Immunoglobulin (Ig)-like domain of NrCAM (Ng
                     (neuronglia) CAM-related cell adhesion molecule); member
                     of the I-set of Ig superfamily (IgSF) domains; cd05874"
                     /db_xref="CDD:409458"
     Region          46..50
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409458"
     Region          55..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409458"
     Region          64..71
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409458"
     Region          77..82
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409458"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          85..87
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409458"
     Region          94..97
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409458"
     Region          102..106
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409458"
     Region          119..127
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409458"
     Region          130..140
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409458"
     Region          149..238
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          163..167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409432"
     Region          177..181
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409432"
     Region          200..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409432"
     Region          215..220
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409432"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          231..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409432"
     Site            245
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            251
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          277..358
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          288..292
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          301..305
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            314
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          323..327
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          337..342
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          350..353
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          362..450
                     /region_name="Ig4_NrCAM"
                     /note="Fourth immunoglobulin (Ig)-like domain of NrCAM
                     (NgCAM-related cell adhesion molecule); cd05868"
                     /db_xref="CDD:409454"
     Region          378..382
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409454"
     Region          391..395
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409454"
     Region          415..419
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409454"
     Region          429..434
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409454"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          442..445
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409454"
     Region          459..542
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          472..476
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          485..489
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            507
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          508..512
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          522..527
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          535..538
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          546..1052
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            619
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          647..737
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(647,713,728)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            716
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            order(729..730,732..733)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            802
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            858
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            993
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1009
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1019
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          1086..1175
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     CDS             1..1199
                     /gene="NRCAM"
                     /gene_synonym="NEDNMS"
                     /coded_by="NM_001371161.1:526..4125"
                     /note="isoform N precursor is encoded by transcript
                     variant 42"
                     /db_xref="GeneID:4897"
                     /db_xref="HGNC:HGNC:7994"
                     /db_xref="MIM:601581"
ORIGIN      
        1 mqlkimpkkk rlsagrvpli lflcqmisal evpldpklle dlvqpptitq qspkdyiidp
       61 reniviqcea kgkpppsfsw trngthfdid kdplvtmkpg tgtliinims egkaetyegv
      121 yqctarnerg aavsnnivvr psrsplwtke klepitlqsg qslvlpcrpp iglpppiifw
      181 mdnsfqrlpq servsqglng dlyfsnvlpe dtredyicya rfnhtqtiqq kqpisvkvis
      241 vdelndtiaa nlsdtefyga kssrerpptf ltpegnasnk eelrgnvlsl eciaeglptp
      301 iiywakedgm lpknrtvykn fektlqiihv seadsgnyqc iaknalgaih htisvrvkaa
      361 pywitapqnl vlspgedgtl icrangnpkp riswltngvp ieiapddpsr kidgdtiifs
      421 nvqerssavy qcnasneygy llanafvnvl aeppriltpa ntlyqvianr palldcaffg
      481 splptiewfk gakgsalhed iyvlhengtl eipvaqkdst gtytcvarnk lgmaknevhl
      541 eikdptwivk qpeyavvqrg smvsfeckvk hdhtlsltvl wlkdnrelps derftvdkdh
      601 lvvadvsddd sgtytcvant tldsvsasav lsvvaptptp apvydvpnpp fdleltdqld
      661 ksvqlswtpg ddnnspitkf iieyedamhk pglwhhqtev sgtqttaqlk lspyvnysfr
      721 vmavnsigks lpseaseqyl tkasepdknp taveglgsep dnlvitwkpl ngfesngpgl
      781 qykvswrqkd gddewtsvvv anvskyivsg tptfvpylik vqalndmgfa pepavvmghs
      841 gedlpmvapg nvrvnvvnst laevhwdpvp lksirghlqg yriyywktqs sskrnrrhie
      901 kkiltfqgsk thgmlpglep fshytlnvrv vngkgegpas pdrvfntpeg vpsapsslki
      961 vnptldsltl ewdppshpng ilteytlkyq pinsthelgp lvdlkipank trwtlknlnf
     1021 strykfyfya qtsagsgsqi teeavttvde amasrqvdia tqgwfiglmc avallilill
     1081 ivcfirrnkg gkypvkeked ahadpeiqpm keddgtfgey sdaedhkplk kgsrtpsdrt
     1141 vkkedsddsl vdygegvngq fnedgsfigq ysgkkekepa egnesseaps pvnamnsfv
//
LOCUS       NP_003894                620 aa            linear   PRI 21-NOV-2025
DEFINITION  cell division cycle protein 16 homolog isoform 1 [Homo sapiens].
ACCESSION   NP_003894
VERSION     NP_003894.3
DBSOURCE    REFSEQ: accession NM_003903.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 620)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 620)
  AUTHORS   Hu,F., Fong,K.O., Cheung,M.P.L., Liu,J.A., Liang,R., Li,T.W.,
            Sharma,R., Ip,P.P., Yang,X. and Cheung,M.
  TITLE     DEPDC1B Promotes Melanoma Angiogenesis and Metastasis through
            Sequestration of Ubiquitin Ligase CDC16 to Stabilize Secreted
            SCUBE3
  JOURNAL   Adv Sci (Weinh) 9 (10), e2105226 (2022)
   PUBMED   35088579
  REMARK    GeneRIF: DEPDC1B Promotes Melanoma Angiogenesis and Metastasis
            through Sequestration of Ubiquitin Ligase CDC16 to Stabilize
            Secreted SCUBE3.
REFERENCE   3  (residues 1 to 620)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 620)
  AUTHORS   Wu,H., Zhang,X., Shen,Q., Liu,Y., Gao,Y., Wang,G., Lv,M., Hua,R.,
            Xu,Y., Zhou,P., Wei,Z., Tao,F., He,X., Cao,Y. and Liu,M.
  TITLE     A homozygous loss-of-function mutation in FBXO43 causes human
            non-obstructive azoospermia
  JOURNAL   Clin Genet 101 (1), 55-64 (2022)
   PUBMED   34595750
REFERENCE   5  (residues 1 to 620)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 620)
  AUTHORS   Grossberger,R., Gieffers,C., Zachariae,W., Podtelejnikov,A.V.,
            Schleiffer,A., Nasmyth,K., Mann,M. and Peters,J.M.
  TITLE     Characterization of the DOC1/APC10 subunit of the yeast and the
            human anaphase-promoting complex
  JOURNAL   J Biol Chem 274 (20), 14500-14507 (1999)
   PUBMED   10318877
REFERENCE   7  (residues 1 to 620)
  AUTHORS   Kallio,M., Weinstein,J., Daum,J.R., Burke,D.J. and Gorbsky,G.J.
  TITLE     Mammalian p55CDC mediates association of the spindle checkpoint
            protein Mad2 with the cyclosome/anaphase-promoting complex, and is
            involved in regulating anaphase onset and late mitotic events
  JOURNAL   J Cell Biol 141 (6), 1393-1406 (1998)
   PUBMED   9628895
REFERENCE   8  (residues 1 to 620)
  AUTHORS   Yu,H., Peters,J.M., King,R.W., Page,A.M., Hieter,P. and
            Kirschner,M.W.
  TITLE     Identification of a cullin homology region in a subunit of the
            anaphase-promoting complex
  JOURNAL   Science 279 (5354), 1219-1222 (1998)
   PUBMED   9469815
REFERENCE   9  (residues 1 to 620)
  AUTHORS   Ollendorff,V. and Donoghue,D.J.
  TITLE     The serine/threonine phosphatase PP5 interacts with CDC16 and
            CDC27, two tetratricopeptide repeat-containing subunits of the
            anaphase-promoting complex
  JOURNAL   J Biol Chem 272 (51), 32011-32018 (1997)
   PUBMED   9405394
REFERENCE   10 (residues 1 to 620)
  AUTHORS   Tugendreich,S., Tomkiel,J., Earnshaw,W. and Hieter,P.
  TITLE     CDC27Hs colocalizes with CDC16Hs to the centrosome and mitotic
            spindle and is essential for the metaphase to anaphase transition
  JOURNAL   Cell 81 (2), 261-268 (1995)
   PUBMED   7736578
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC391369.1, BQ051608.1,
            BQ424567.1 and BU687000.1.
            
            On Nov 24, 2006 this sequence version replaced NP_003894.2.
            
            Summary: The protein encoded by this gene functions as a protein
            ubiquitin ligase and is a component of the multiprotein APC
            complex. The APC complex is a cyclin degradation system that
            governs exit from mitosis by targeting cell cycle proteins for
            degredation by the 26S proteasome. Each component protein of the
            APC complex is highly conserved among eukaryotic organisms. This
            protein, and other APC complex proteins, contain a
            tetratricopeptide repeat (TPR) domain; a protein domain that is
            often involved in protein-protein interactions and the assembly of
            multiprotein complexes. Multiple alternatively spliced transcript
            variants, encoding distinct proteins, have been identified.
            [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) lacks an exon segment in the
            3' UTR, compared to variant 2. Variants 1 and 2 encode the same
            isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853562.9241.1,
                                           SRR11853561.8617.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..620
                     /product="cell division cycle protein 16 homolog isoform
                     1"
                     /note="cell division cycle protein 16 homolog; cell
                     division cycle 16 homolog; anaphase-promoting complex,
                     subunit 6; cyclosome subunit 6"
                     /calculated_mol_wt=71525
     Region          4..33
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          15..94
                     /region_name="ANAPC3"
                     /note="Anaphase-promoting complex, cyclosome, subunit 3;
                     pfam12895"
                     /db_xref="CDD:463743"
     Region          36..65
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          37..62
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          70..94
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          70..93
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Site            112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     Region          128..159
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          164..187
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          198..222
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          232..260
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          267..294
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          275..>440
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          298..329
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          299..329
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          334..362
                     /region_name="TPR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          336..362
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          367..397
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          369..397
                     /region_name="TPR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          373..>522
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          402..434
                     /region_name="TPR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          402..430
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(403,406..407,410..411,413,437,449..450,453..454,
                     456..457,480,483..484,487..488,491)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          435..474
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          442..474
                     /region_name="TPR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          479..508
                     /region_name="TPR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Region          479..506
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     Region          574..599
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13042.2)"
     Site            581
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     Site            595
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q13042.2)"
     CDS             1..620
                     /gene="CDC16"
                     /gene_synonym="ANAPC6; APC6; CDC16Hs; CUT9"
                     /coded_by="NM_003903.5:189..2051"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9542.2"
                     /db_xref="GeneID:8881"
                     /db_xref="HGNC:HGNC:1720"
                     /db_xref="MIM:603461"
ORIGIN      
        1 mnlerlrkrv rqyldqqqyq salfwadkva slsreepqdi ywlaqclylt aqyhraahal
       61 rsrkldklye acrylaarch yaakehqqal dvldmeepin krlfekylkd esgfkdpssd
      121 wemsqssiks sicllrgkiy daldnrtlat ysykealkld vycfeafdll tshhmltaqe
      181 ekelleslpl sklcneeqel lrflfenklk kynkpsetvi pesvdglqen ldvvvslaer
      241 hyyncdfkmc ykltsvvmek dpfhasclpv higtlvelnk anelfylshk lvdlypsnpv
      301 swfavgcyyl mvghknehar rylskattle ktygpawiay ghsfaveseh dqamaayfta
      361 aqlmkgchlp mlyigleygl tnnsklaerf fsqalsiape dpfvmhevgv vafqngewkt
      421 aekwfldale kikaignevt vdkwepllnn lghvcrklkk yaealdyhrq alvlipqnas
      481 tysaigyihs lmgnfenavd yfhtalglrr ddtfsvtmlg hciemyigds eayigadikd
      541 klkcydfdvh tmktlkniis ppwdfrefev ekqtaeetgl tpletsrktp dsrpsleetf
      601 eiemnesdmm letsmsdhst
//
LOCUS       NP_001073913             407 aa            linear   PRI 21-NOV-2025
DEFINITION  immunoglobulin superfamily member 5 [Homo sapiens].
ACCESSION   NP_001073913 XP_086761
VERSION     NP_001073913.1
DBSOURCE    REFSEQ: accession NM_001080444.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Hirabayashi,S., Tajima,M., Yao,I., Nishimura,W., Mori,H. and
            Hata,Y.
  TITLE     JAM4, a junctional cell adhesion molecule interacting with a tight
            junction protein, MAGI-1
  JOURNAL   Mol Cell Biol 23 (12), 4267-4282 (2003)
   PUBMED   12773569
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF121782.1.
            
            On Jan 18, 2007 this sequence version replaced XP_086761.2.
            
            Sequence Note:.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK092516.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380588.5/ ENSP00000369962.4
            RefSeq Select criteria :: based on manual assertion
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.2"
     Protein         1..407
                     /product="immunoglobulin superfamily member 5"
                     /note="immunoglobulin superfamily 5 like; junctional
                     adhesion molecule 4"
                     /calculated_mol_wt=44462
     Region          45..138
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Site            59
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NSI5.2)"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NSI5.2)"
     Region          143..218
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NSI5.2)"
     Site            231
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NSI5.2)"
     Site            267..285
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSI5.2)"
     Region          320..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSI5.2)"
     CDS             1..407
                     /gene="IGSF5"
                     /gene_synonym="GSF5; JAM4"
                     /coded_by="NM_001080444.2:328..1551"
                     /db_xref="CCDS:CCDS33562.1"
                     /db_xref="GeneID:150084"
                     /db_xref="HGNC:HGNC:5952"
                     /db_xref="MIM:610638"
ORIGIN      
        1 mgqkerstad tlpdleewks aaglrwwqta vvdgsgsgne viegpqnarv lkgsqarfnc
       61 tvsqgwklim walsdmvvls vrpmepiitn drftsqrydq ggnftsemii hnvepsdsgn
      121 ircslqnsrl hgsayltvqv mgelfipsvn lvvaenepce vtclpshwtr lpdiswelgl
      181 lvshssyyfv pepsdlqsav silaltpqsn gtltcvatwk slkarksatv nltvircpqd
      241 tggginipgv lsslpslgfs lptwgkvglg lagtmlltpt ctltircccc rrrccgcncc
      301 crccfccrrk rgfriqfqkk sekektnket etesgnensg ynsdeqkttd taslppksce
      361 ssdpeqrnss cgpphqradq rpprpashpq asfnlaspek vsnttvv
//
LOCUS       NP_001512                911 aa            linear   PRI 21-NOV-2025
DEFINITION  general transcription factor 3C polypeptide 2 isoform b [Homo
            sapiens].
ACCESSION   NP_001512
VERSION     NP_001512.1
DBSOURCE    REFSEQ: accession NM_001521.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Peng,F., Zhou,Y., Wang,J., Guo,B., Wei,Y., Deng,H., Wu,Z.,
            Zhang,C., Shi,K., Li,Y., Wang,X., Shore,P., Zhao,S. and Deng,W.
  TITLE     The transcription factor Sp1 modulates RNA polymerase III gene
            transcription by controlling BRF1 and GTF3C2 expression in human
            cells
  JOURNAL   J Biol Chem 295 (14), 4617-4630 (2020)
   PUBMED   32115405
  REMARK    GeneRIF: The transcription factor Sp1 modulates RNA polymerase III
            gene transcription by controlling BRF1 and GTF3C2 expression in
            human cells.
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 911)
  AUTHORS   Kantidakis,T., Ramsbottom,B.A., Birch,J.L., Dowding,S.N. and
            White,R.J.
  TITLE     mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes,
            and targets their repressor Maf1
  JOURNAL   Proc Natl Acad Sci U S A 107 (26), 11823-11828 (2010)
   PUBMED   20543138
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11465]
REFERENCE   5  (residues 1 to 911)
  AUTHORS   Hirschowitz,E.A., Hiestand,D.M. and Yannelli,J.R.
  TITLE     Vaccines for lung cancer
  JOURNAL   J Thorac Oncol 1 (1), 93-104 (2006)
   PUBMED   17409835
  REMARK    Review article
REFERENCE   6  (residues 1 to 911)
  AUTHORS   Wang,Z. and Roeder,R.G.
  TITLE     DNA topoisomerase I and PC4 can interact with human TFIIIC to
            promote both accurate termination and transcription reinitiation by
            RNA polymerase III
  JOURNAL   Mol Cell 1 (5), 749-757 (1998)
   PUBMED   9660958
REFERENCE   7  (residues 1 to 911)
  AUTHORS   Oettel,S., Hartel,F., Kober,I., Iben,S. and Seifart,K.H.
  TITLE     Human transcription factors IIIC2, IIIC1 and a novel component
            IIIC0 fulfil different aspects of DNA binding to various pol III
            genes
  JOURNAL   Nucleic Acids Res 25 (12), 2440-2447 (1997)
   PUBMED   9171097
REFERENCE   8  (residues 1 to 911)
  AUTHORS   Chu,W.M., Wang,Z., Roeder,R.G. and Schmid,C.W.
  TITLE     RNA polymerase III transcription repressed by Rb through its
            interactions with TFIIIB and TFIIIC2
  JOURNAL   J Biol Chem 272 (23), 14755-14761 (1997)
   PUBMED   9169441
REFERENCE   9  (residues 1 to 911)
  AUTHORS   Sinn,E., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     Cloning and characterization of a TFIIIC2 subunit (TFIIIC beta)
            whose presence correlates with activation of RNA polymerase
            III-mediated transcription by adenovirus E1A expression and serum
            factors
  JOURNAL   Genes Dev 9 (6), 675-685 (1995)
   PUBMED   7729686
REFERENCE   10 (residues 1 to 911)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA399212.1, D13636.1 and BC020981.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1550760.1,
                                           SRR14243140.434462.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..911
                     /product="general transcription factor 3C polypeptide 2
                     isoform b"
                     /note="general transcription factor 3C polypeptide 2;
                     TFIIIC 110 kDa subunit; transcription factor IIIC subunit
                     beta; transcription factor IIIC 110 kDa subunit; general
                     transcription factor IIIC, polypeptide 2, beta 110kDa"
                     /calculated_mol_wt=100549
     Region          24..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          <62..255
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          205..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          366..426
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          427..483
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          470..543
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          484..535
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          536..603
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          558..595
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <559..644
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          604..654
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          616..656
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          655..690
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          765..785
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            871
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          889..911
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            892
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            893
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            895
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            901
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     CDS             1..911
                     /gene="GTF3C2"
                     /gene_synonym="TF3C-beta; TFIIIC-BETA; TFIIIC110"
                     /coded_by="NM_001521.4:127..2862"
                     /note="isoform b is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1749.1"
                     /db_xref="GeneID:2976"
                     /db_xref="HGNC:HGNC:4665"
                     /db_xref="MIM:604883"
ORIGIN      
        1 mdtcgvgyva lgeagpvgnm tvvdspgqev lnqldvktss emtsaeasve mslptplpgf
       61 edspdqrrlp peqeslsrle qpdlssemsk vskpraskpg rkrggrtrkg pkrpqqpnpp
      121 saplvpglld qsnplstpmp kkrgrkskae llllklskdl drpesqspkr ppedfetpsg
      181 erprrraaqv allylqelae elstalpapv scpegpkvss ptkpkkirqp aacpggeevd
      241 gaprdedffl qveaedvees egpsesssep epvvprstpr gstsgkqkph crgmapnglp
      301 nhimapvwkc lhltkdfreq khsywefaew iplawkwhll seleaapylp qeeksplfsv
      361 qreglpedgt lyrinrfssi tahperwdvs fftggplwal dwcpvpegag asqyvalfss
      421 pdmnethpls qlhsgpgllq lwglgtlqqe scpgnrahfv ygiacdngci wdlkfcpsga
      481 welpgtprka pllprlglla lacsdgkvll fslphpeall aqqppdavkp aiykvqcvat
      541 lqvgsmqatd psecgqclsl awmptrphqh laagyyngmv vfwnlptnsp lqrirlsdgs
      601 lklypfqcfl ahdqavrtlq wckanshflv sagsdrkikf wdlrrpyepi nsikrflste
      661 lawllpyngv tvaqdncyas yglcgihyid agylgfkayf taprkgtvws lsgsdwlgti
      721 aagdisgeli aailpdmaln pinvkrpver rfpiykadli pyqdspegpd hssassgvpn
      781 ppkartytet vnhhyllfqd tdlgsfhdll rrepmlrmqe geghsqlcld rlqleaihkv
      841 rfspnldsyg wlvsggqsgl vrihfvrgla splghrmqle srahfnamfq pssptrrpgf
      901 sptshrllpt p
//
LOCUS       NP_001371663            1114 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 40 [Homo sapiens].
ACCESSION   NP_001371663 XP_016861898
VERSION     NP_001371663.1
DBSOURCE    REFSEQ: accession NM_001384734.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1114)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1114)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1114)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1114)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1114)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1114)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1114)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1114)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1114)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1114)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            On Jun 26, 2020 this sequence version replaced XP_016861898.1.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.71353.1,
                                           SRR14038193.2094952.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1114
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1114
                     /product="microtubule-associated protein 4 isoform 40"
                     /note="MAP-4"
                     /calculated_mol_wt=117027
     Region          <575..919
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <931..952
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          954..983
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          985..1014
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          1016..1046
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1114
                     /gene="MAP4"
                     /coded_by="NM_001384734.1:96..3440"
                     /note="isoform 40 is encoded by transcript variant 15"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgsp tefleekmay qeypnsqnwp
      121 edtnfcfqpe qvvdpiqtdp fkmyhdddla dlvfpssata dtsifagqnd plkdsygmsp
      181 cntavvpqgw svealnsphs esfvspeava eppqptavpl elakeiemas eerppaqale
      241 immglkttdm apsketemal akdmalatkt evalakdmes ptkldvtlak dmqpsmesdm
      301 alvkdmelpt ekevalvkdv rwptetdvss aknvvlptet evapakdvtl lketeraspi
      361 kmdlapskdm gppkenkket eraspikmdl apskdmgppk enkivpakdl vllseievaq
      421 andiisstei ssaekvalss etevalardm tlppetnvil tkdkalplea evapvkdmaq
      481 lpeteiapak dvapstvkev gllkdmspls etemalgkdv tpppetevvl iknvclppem
      541 evaltedqvp alkteaplak dgvltlannv tpakdvppls eteatpvpik dmeiaqtqkg
      601 isedshlesl qdvgqsaapt fmispetvtg tgkkcslpae edsvleklge rkpcnsqpse
      661 lssetsgiar peegrpvvsg tgndittppn kelppspekk tkplattqpa ktstskaktq
      721 ptslpkqpap ttigglnkkp mslasglvpa appkrpavas arpsilpskd vkpkpiadak
      781 apekraspsk pasapasrsg skstqtvakt ttaaavastg pssrspstll pkkptaikte
      841 gkpaevkkmt aksvpadlsr pkststssmk ktttlsgtap aagvvpsrvk atpmpsrpst
      901 tpfidkkpts akpssttprl srlatntsap dlknvrskvg stenikhqpg ggrvqivskk
      961 vsyshiqskc gskdnikhvp gggnvqiqnk kvdiskvssk cgskanikhk pgggdvkies
     1021 qklnfkekaq akvgsldnvg hlpaggavkt egggseaplc pgppageepa iseaapeaga
     1081 ptsasglngh ptlsgggdqr eaqtldsqiq etsi
//
LOCUS       NP_536351                380 aa            linear   PRI 21-NOV-2025
DEFINITION  protein GNAS isoform GNASS [Homo sapiens].
ACCESSION   NP_536351
VERSION     NP_536351.1
DBSOURCE    REFSEQ: accession NM_080426.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Lin,J., Nie,Q., Cheng,J., Zhong,Y.N., Zhang,T., Zhang,X., Ge,X.,
            Ding,Y., Niu,C., Gao,Y., Wang,K., Gao,M., Wang,X., Chen,W., Yun,C.,
            Ye,C., Xu,J., Shaoyong,W., Zhang,L., Shang,P., Luo,X., Zhang,Z.,
            Zheng,X., Sha,X., Zhang,J., Nie,S., Zhang,X., Ren,F., Liu,H.,
            Dong,E., Yu,X., Ji,L., Pang,Y., Sun,J.P. and Jiang,C.
  TITLE     A microbial amino-acid-conjugated bile acid, tryptophan-cholic
            acid, improves glucose homeostasis via the orphan receptor MRGPRE
  JOURNAL   Cell 188 (17), 4530-4548 (2025)
   PUBMED   40446798
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Crane,J.L., Shamblott,M.J., Axelman,J., Hsu,S., Levine,M.A. and
            Germain-Lee,E.L.
  TITLE     Imprinting status of Galpha(s), NESP55, and XLalphas in cell
            cultures derived from human embryonic germ cells: GNAS imprinting
            in human embryonic germ cells
  JOURNAL   Clin Transl Sci 2 (5), 355-360 (2009)
   PUBMED   20443919
  REMARK    GeneRIF: analysis of the imprinting Status of Galpha(s), NESP55,
            and XLalphas in cell cultures derived from human embryonic germ
            cells
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Bastepe,M.
  TITLE     The GNAS Locus: Quintessential Complex Gene Encoding Gsalpha,
            XLalphas, and other Imprinted Transcripts
  JOURNAL   Curr Genomics 8 (6), 398-414 (2007)
   PUBMED   19412439
  REMARK    GeneRIF: GNAS locus has a highly complex imprinted expression
            pattern, giving rise to transcripts (including non-coding) that are
            maternally, paternally, or biallelically expressed.
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Jakobsen,A.M., Ahlman,H., Kolby,L., Abrahamsson,J.,
            Fischer-Colbrie,R. and Nilsson,O.
  TITLE     NESP55, a novel chromogranin-like peptide, is expressed in
            endocrine tumours of the pancreas and adrenal medulla but not in
            ileal carcinoids
  JOURNAL   Br J Cancer 88 (11), 1746-1754 (2003)
   PUBMED   12771991
  REMARK    GeneRIF: Neuroendocrine secretory protein 55 is found in a subset
            of neuroendocrine tumours showing differentiation towards adrenal
            chromaffin cells and pancreatic islets cells and not in ileal
            carcinoids
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Freson,K., Jaeken,J., Van Helvoirt,M., de Zegher,F.,
            Wittevrongel,C., Thys,C., Hoylaerts,M.F., Vermylen,J. and Van
            Geet,C.
  TITLE     Functional polymorphisms in the paternally expressed XLalphas and
            its cofactor ALEX decrease their mutual interaction and enhance
            receptor-mediated cAMP formation
  JOURNAL   Hum Mol Genet 12 (10), 1121-1130 (2003)
   PUBMED   12719376
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Weiss,U., Ischia,R., Eder,S., Lovisetti-Scamihorn,P., Bauer,R. and
            Fischer-Colbrie,R.
  TITLE     Neuroendocrine secretory protein 55 (NESP55): alternative splicing
            onto transcripts of the GNAS gene and posttranslational processing
            of a maternally expressed protein
  JOURNAL   Neuroendocrinology 71 (3), 177-186 (2000)
   PUBMED   10729789
REFERENCE   7  (residues 1 to 380)
  AUTHORS   Ischia,R., Lovisetti-Scamihorn,P., Hogue-Angeletti,R.,
            Wolkersdorfer,M., Winkler,H. and Fischer-Colbrie,R.
  TITLE     Molecular cloning and characterization of NESP55, a novel
            chromogranin-like precursor of a peptide with 5-HT1B receptor
            antagonist activity
  JOURNAL   J Biol Chem 272 (17), 11657-11662 (1997)
   PUBMED   9111083
REFERENCE   8  (residues 1 to 380)
  AUTHORS   Haldeman-Englert,C.R., Hurst,A.C.E. and Levine,M.A.
  TITLE     Disorders of GNAS Inactivation
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29072892
REFERENCE   9  (residues 1 to 380)
  AUTHORS   Szymczuk,V., Florenzano,P., de Castro,L.F., Collins,M.T. and
            Boyce,A.M.
  TITLE     Fibrous Dysplasia / McCune-Albright Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719192
REFERENCE   10 (residues 1 to 380)
  AUTHORS   Weinstein,L.S., Gejman,P.V., de Mazancourt,P., American,N. and
            Spiegel,A.M.
  TITLE     A heterozygous 4-bp deletion mutation in the Gs alpha gene (GNAS1)
            in a patient with Albright hereditary osteodystrophy
  JOURNAL   Genomics 13 (4), 1319-1321 (1992)
   PUBMED   1505964
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC089157.1, AF493897.1 and
            AF105253.1.
            
            Summary: This locus has a highly complex imprinted expression
            pattern. It gives rise to maternally, paternally, and biallelically
            expressed transcripts that are derived from four alternative
            promoters and 5' exons. Some transcripts contain a differentially
            methylated region (DMR) at their 5' exons, and this DMR is commonly
            found in imprinted genes and correlates with transcript expression.
            An antisense transcript is produced from an overlapping locus on
            the opposite strand. One of the transcripts produced from this
            locus, and the antisense transcript, are paternally expressed
            noncoding RNAs, and may regulate imprinting in this region. In
            addition, one of the transcripts contains a second overlapping ORF,
            which encodes a structurally unrelated protein - Alex. Alternative
            splicing of downstream exons is also observed, which results in
            different forms of the stimulatory G-protein alpha subunit, a key
            element of the classical signal transduction pathway linking
            receptor-ligand interactions with the activation of adenylyl
            cyclase and a variety of cellular reponses. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            Mutations in this gene result in pseudohypoparathyroidism type 1a,
            pseudohypoparathyroidism type 1b, Albright hereditary
            osteodystrophy, pseudopseudohypoparathyroidism, McCune-Albright
            syndrome, progressive osseus heteroplasia, polyostotic fibrous
            dysplasia of bone, and some pituitary tumors. [provided by RefSeq,
            Aug 2012].
            
            Transcript Variant: This variant (3) is biallelically expressed. It
            lacks an internal exon and uses an alternate splice site, compared
            to variant 1. It encodes isoform GNASS, also known as alpha-S1,
            which differs in an internal region and has identical N- and
            C-termini, compared to isoform GNASL.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.383823.1,
                                           ERR279826.2292.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 19412439
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.32"
     Protein         1..380
                     /product="protein GNAS isoform GNASS"
                     /note="secretogranin VI; G protein subunit alpha S;
                     guanine nucleotide binding protein (G protein), alpha
                     stimulating activity polypeptide 1; guanine nucleotide
                     regulatory protein; adenylate cyclase-stimulating G alpha
                     protein; protein ALEX; extra large alphas protein;
                     alternative gene product encoded by XL-exon"
                     /calculated_mol_wt=44135
     Region          41..374
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Site            order(47,52..54,190,209,212,278..279,281,351..352)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206639"
     Site            47..54
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206639"
     Site            order(48..50,79,83,87,90,93..94,114,117,158,187,212,220,
                     224)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Site            185..193
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            190
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(191,193,195,206,208,212..214,216,219..220,222..225)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(193,218,221..222,225)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            209..212
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            210..226
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Site            278..281
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(343..354,356..359)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Site            351..353
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..380
                     /gene="GNAS"
                     /gene_synonym="AHO; AIMAH1; C20orf45; GNAS1; GPSA; GSA;
                     GSP; NESP; PITA3; POH; SCG6; SgVI"
                     /coded_by="NM_080426.4:307..1449"
                     /note="isoform GNASS is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS46624.1"
                     /db_xref="GeneID:2778"
                     /db_xref="HGNC:HGNC:4392"
                     /db_xref="MIM:139320"
ORIGIN      
        1 mgclgnskte dqrneekaqr eankkiekql qkdkqvyrat hrllllgage sgkstivkqm
       61 rilhvngfng dsekatkvqd iknnlkeaie tivaamsnlv ppvelanpen qfrvdyilsv
      121 mnvpdfdfpp efyehakalw edegvracye rsneyqlidc aqyfldkidv ikqadyvpsd
      181 qdllrcrvlt sgifetkfqv dkvnfhmfdv ggqrderrkw iqcfndvtai ifvvasssyn
      241 mvirednqtn rlqealnlfk siwnnrwlrt isvilflnkq dllaekvlag kskiedyfpe
      301 faryttpeda tpepgedprv trakyfirde flristasgd grhycyphft cavdtenirr
      361 vfndcrdiiq rmhlrqyell
//
LOCUS       NP_001387283             311 aa            linear   PRI 21-NOV-2025
DEFINITION  single-stranded DNA-binding protein 2 isoform 22 [Homo sapiens].
ACCESSION   NP_001387283
VERSION     NP_001387283.1
DBSOURCE    REFSEQ: accession NM_001400354.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Schwab,C., Roberts,K., Boer,J.M., Gohring,G., Steinemann,D.,
            Vora,A., Macartney,C., Hough,R., Thorn,Z., Dillon,R., Escherich,G.,
            Cazzaniga,G., Schlegelberger,B., Loh,M., den Boer,M.L.,
            Moorman,A.V. and Harrison,C.J.
  TITLE     SSBP2-CSF1R is a recurrent fusion in B-lineage acute lymphoblastic
            leukemia with diverse genetic presentation and variable outcome
  JOURNAL   Blood 137 (13), 1835-1838 (2021)
   PUBMED   33197935
  REMARK    GeneRIF: SSBP2-CSF1R is a recurrent fusion in B-lineage acute
            lymphoblastic leukemia with diverse genetic presentation and
            variable outcome.
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Wang,H., Kim,J., Wang,Z., Yan,X.X., Dean,A. and Xu,W.
  TITLE     Crystal structure of human LDB1 in complex with SSBP2
  JOURNAL   Proc Natl Acad Sci U S A 117 (2), 1042-1048 (2020)
   PUBMED   31892537
  REMARK    GeneRIF: Single-stranded DNA binding proteins (SSBPs) interact
            specifically with the LDB/Chip conserved domain (LCCD) of LDB
            proteins and stabilize LDBs by preventing their proteasomal
            degradation, thus promoting their functions in gene regulation.
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Kim,H., Kim,Y., Bang,S., Park,S., Jee,S., Sim,J., Shin,S.J.,
            Paik,S.S. and Jang,K.
  TITLE     Low Expression of Single-stranded DNA Binding Protein 2 (SSBP2)
            Predicts Unfavourable Postoperative Outcomes in Patients With Clear
            Cell Renal Cell Carcinoma
  JOURNAL   In Vivo 34 (1), 101-107 (2020)
   PUBMED   31882468
  REMARK    GeneRIF: CcRCC with low SSBP2 expression was associated with
            adverse clinicopathological characteristics and poor patient
            outcomes.
REFERENCE   6  (residues 1 to 311)
  AUTHORS   Fleisig,H.B., Orazio,N.I., Liang,H., Tyler,A.F., Adams,H.P.,
            Weitzman,M.D. and Nagarajan,L.
  TITLE     Adenoviral E1B55K oncoprotein sequesters candidate leukemia
            suppressor sequence-specific single-stranded DNA-binding protein 2
            into aggresomes
  JOURNAL   Oncogene 26 (33), 4797-4805 (2007)
   PUBMED   17311003
  REMARK    GeneRIF: Results suggest that subverting SSBP2 function by
            oncoprotein E1B55K may contribute to cell transformation by viral
            oncoproteins.
REFERENCE   7  (residues 1 to 311)
  AUTHORS   Liang,H., Samanta,S. and Nagarajan,L.
  TITLE     SSBP2, a candidate tumor suppressor gene, induces growth arrest and
            differentiation of myeloid leukemia cells
  JOURNAL   Oncogene 24 (16), 2625-2634 (2005)
   PUBMED   15782145
  REMARK    GeneRIF: Our findings are consistent with human SSBP2 being a novel
            regulator of hematopoietic growth and differentiation, whose loss
            confers a block in differentiation advantage to myeloid leukemic
            cells.
REFERENCE   8  (residues 1 to 311)
  AUTHORS   Castro,P., Liang,H., Liang,J.C. and Nagarajan,L.
  TITLE     A novel, evolutionarily conserved gene family with putative
            sequence-specific single-stranded DNA-binding activity
  JOURNAL   Genomics 80 (1), 78-85 (2002)
   PUBMED   12079286
  REMARK    GeneRIF: Member of a closely related, evolutionarily conserved, and
            ubiquitously expressed gene family, potential tumor suppressor
REFERENCE   9  (residues 1 to 311)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 311)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016562.7, AC093250.3 and
            AC010623.10.
            
            Summary: This gene encodes a subunit of a protein complex that
            interacts with single-stranded DNA and is involved in the DNA
            damage response and maintenance of genome stability. The encoded
            protein may also play a role in telomere repair. A variant of this
            gene may be associated with survival in human glioblastoma
            patients. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1966909.1,
                                           SRR14038194.2467302.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.1"
     Protein         1..311
                     /product="single-stranded DNA-binding protein 2 isoform
                     22"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein 2"
                     /calculated_mol_wt=32610
     Region          19..45
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          <96..288
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     CDS             1..311
                     /gene="SSBP2"
                     /gene_synonym="HSPC116; SOSS-B2"
                     /coded_by="NM_001400354.1:56..991"
                     /note="isoform 22 is encoded by transcript variant 25"
                     /db_xref="GeneID:23635"
                     /db_xref="HGNC:HGNC:15831"
                     /db_xref="MIM:607389"
ORIGIN      
        1 mygkgksnss avpsdsqare klalyvyeyl lhvgaqksaq tflseirwek nitlgeppgf
       61 lhswwcvfwd lycaaperre tcehsseaka fhdyalggvp gsqpllpsgm dptrqqghpn
      121 mggpmqrmtp prgmvplgpq nyggamrppl nalggpgmpg mnmgpgggrp wpnptnansi
      181 pyssaspgny vgppggggpp gtpimpspad stnsgdnmyt lmnavppgpn rpnfpmgpgs
      241 dgpmgglggm eshhmngslg sgdmdsiskn spnnmslsnq pgtprddgem ggnflnpfqs
      301 esyspsmtms v
//
LOCUS       NP_001139574             854 aa            linear   PRI 21-NOV-2025
DEFINITION  protein mono-ADP-ribosyltransferase PARP9 isoform a [Homo sapiens].
ACCESSION   NP_001139574
VERSION     NP_001139574.1
DBSOURCE    REFSEQ: accession NM_001146102.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 854)
  AUTHORS   Pandi,K., Angabo,S., Makkawi,H., Benyamini,H., Elgavish,S. and
            Nussbaum,G.
  TITLE     P. gingivalis-Induced TLR2 Interactome Analysis Reveals Association
            with PARP9
  JOURNAL   J Dent Res 103 (3), 329-338 (2024)
   PUBMED   38344758
  REMARK    GeneRIF: P. gingivalis-Induced TLR2 Interactome Analysis Reveals
            Association with PARP9.
REFERENCE   3  (residues 1 to 854)
  AUTHORS   Thirunavukkarasu,S., Ahmed,M., Rosa,B.A., Boothby,M., Cho,S.H.,
            Rangel-Moreno,J., Mbandi,S.K., Schreiber,V., Gupta,A., Zuniga,J.,
            Mitreva,M., Kaushal,D., Scriba,T.J. and Khader,S.A.
  TITLE     Poly(ADP-ribose) polymerase 9 mediates early protection against
            Mycobacterium tuberculosis infection by regulating type I IFN
            production
  JOURNAL   J Clin Invest 133 (12), e158630 (2023)
   PUBMED   37200107
  REMARK    GeneRIF: Poly(ADP-ribose) polymerase 9 mediates early protection
            against Mycobacterium tuberculosis infection by regulating type I
            IFN production.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 854)
  AUTHORS   Russo,L.C., Tomasin,R., Matos,I.A., Manucci,A.C., Sowa,S.T.,
            Dale,K., Caldecott,K.W., Lehtio,L., Schechtman,D., Meotti,F.C.,
            Bruni-Cardoso,A. and Hoch,N.C.
  TITLE     The SARS-CoV-2 Nsp3 macrodomain reverses PARP9/DTX3L-dependent
            ADP-ribosylation induced by interferon signaling
  JOURNAL   J Biol Chem 297 (3), 101041 (2021)
   PUBMED   34358560
  REMARK    GeneRIF: The SARS-CoV-2 Nsp3 macrodomain reverses
            PARP9/DTX3L-dependent ADP-ribosylation induced by interferon
            signaling.
REFERENCE   5  (residues 1 to 854)
  AUTHORS   Xing,J., Zhang,A., Du,Y., Fang,M., Minze,L.J., Liu,Y.J., Li,X.C.
            and Zhang,Z.
  TITLE     Identification of poly(ADP-ribose) polymerase 9 (PARP9) as a
            noncanonical sensor for RNA virus in dendritic cells
  JOURNAL   Nat Commun 12 (1), 2681 (2021)
   PUBMED   33976210
  REMARK    GeneRIF: Identification of poly(ADP-ribose) polymerase 9 (PARP9) as
            a noncanonical sensor for RNA virus in dendritic cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 854)
  AUTHORS   Jha,R., Agarwal,A., Mahfouz,R., Paasch,U., Grunewald,S.,
            Sabanegh,E., Yadav,S.P. and Sharma,R.
  TITLE     Determination of Poly (ADP-ribose) polymerase (PARP) homologues in
            human ejaculated sperm and its correlation with sperm maturation
  JOURNAL   Fertil Steril 91 (3), 782-790 (2009)
   PUBMED   18339380
  REMARK    GeneRIF: Determination of Poly (ADP-ribose) polymerase (PARP)
            homologues in human ejaculated sperm and its correlation with sperm
            maturation.
REFERENCE   7  (residues 1 to 854)
  AUTHORS   Juszczynski,P., Kutok,J.L., Li,C., Mitra,J., Aguiar,R.C. and
            Shipp,M.A.
  TITLE     BAL1 and BBAP are regulated by a gamma interferon-responsive
            bidirectional promoter and are overexpressed in diffuse large
            B-cell lymphomas with a prominent inflammatory infiltrate
  JOURNAL   Mol Cell Biol 26 (14), 5348-5359 (2006)
   PUBMED   16809771
  REMARK    GeneRIF: BAL1 and BBAP are located on chromosome 3q21 in a
            head-to-head orientation and are regulated by a
            IFN-gamma-responsive bidirectional promoter.
REFERENCE   8  (residues 1 to 854)
  AUTHORS   Aguiar,R.C., Takeyama,K., He,C., Kreinbrink,K. and Shipp,M.A.
  TITLE     B-aggressive lymphoma family proteins have unique domains that
            modulate transcription and exhibit poly(ADP-ribose) polymerase
            activity
  JOURNAL   J Biol Chem 280 (40), 33756-33765 (2005)
   PUBMED   16061477
REFERENCE   9  (residues 1 to 854)
  AUTHORS   Takeyama,K., Aguiar,R.C., Gu,L., He,C., Freeman,G.J., Kutok,J.L.,
            Aster,J.C. and Shipp,M.A.
  TITLE     The BAL-binding protein BBAP and related Deltex family members
            exhibit ubiquitin-protein isopeptide ligase activity
  JOURNAL   J Biol Chem 278 (24), 21930-21937 (2003)
   PUBMED   12670957
REFERENCE   10 (residues 1 to 854)
  AUTHORS   Aguiar,R.C., Yakushijin,Y., Kharbanda,S., Salgia,R., Fletcher,J.A.
            and Shipp,M.A.
  TITLE     BAL is a novel risk-related gene in diffuse large B-cell lymphomas
            that enhances cellular migration
  JOURNAL   Blood 96 (13), 4328-4334 (2000)
   PUBMED   11110709
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC368112.1, AK313494.1 and BC039580.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2008007.1, AK313494.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.1"
     Protein         1..854
                     /product="protein mono-ADP-ribosyltransferase PARP9
                     isoform a"
                     /EC_number="2.4.2.30"
                     /note="poly [ADP-ribose] polymerase 9; poly (ADP-ribose)
                     polymerase 9; PARP-9; b aggressive lymphoma protein;
                     ADP-ribosyltransferase diphtheria toxin-like 9; protein
                     mono-ADP-ribosyltransferase PARP9"
                     /calculated_mol_wt=96213
     Region          117..277
                     /region_name="Macro_Af1521_BAL-like"
                     /note="macrodomain, Af1521-like family; cd02907"
                     /db_xref="CDD:394877"
     Site            order(125..127,138..140,144..150,152,238..244)
                     /site_type="other"
                     /note="ADP-ribose binding site [chemical binding]"
                     /db_xref="CDD:394877"
     Region          310..486
                     /region_name="Macro_BAL-like"
                     /note="macrodomain, B-aggressive lymphoma (BAL)-like
                     family; cd02903"
                     /db_xref="CDD:394874"
     Site            order(325..327,337..339,345..348,351,429..435,469,475)
                     /site_type="other"
                     /note="ADP-ribose binding site [chemical binding]"
                     /db_xref="CDD:394874"
     Region          702..821
                     /region_name="TCCD_inducible_PARP_like"
                     /note="Poly(ADP-ribose) polymerases catalyse the covalent
                     attachment of ADP-ribose units from NAD+ to itself and to
                     a limited number of other DNA binding proteins, which
                     decreases their affinity for DNA. Poly(ADP-ribose)
                     polymerase is a regulatory component...; cd01439"
                     /db_xref="CDD:238719"
     Site            order(704..708,711,715,719..721,723,736..738,748,804)
                     /site_type="other"
                     /note="nad+ binding pocket [chemical binding]"
                     /db_xref="CDD:238719"
     CDS             1..854
                     /gene="PARP9"
                     /gene_synonym="ARTD9; BAL; BAL1; MGC:7868"
                     /coded_by="NM_001146102.2:146..2710"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3014.1"
                     /db_xref="GeneID:83666"
                     /db_xref="HGNC:HGNC:24118"
                     /db_xref="MIM:612065"
ORIGIN      
        1 mdfsmvagaa ayneksgrit slsllfqkvf aqifpqwrkg nteeclpykc setgalgeny
       61 swqipinhnd fkilknnerq lcevlqnkfg cistlvspvq egnskslqvf rkmltpriel
      121 svwkddltth avdavvnaan edllhgggla lalvkaggfe iqeeskqfva rygkvsagei
      181 avtgagrlpc kqiihavgpr wmewdkqgct gklqraivsi lnyviyknth iktvaipals
      241 sgifqfplnl ctktivetir vslqgkpmms nlkeihlvsn edptvaafka asefilgkse
      301 lgqettpsfn amvvnnltlq ivqghiewqt advivnsvnp hditvgpvak silqqagvem
      361 kseflatkak qfqrsqlvlv tkgfnlfcky iyhvlwhsef pkpqilkham keclekcieq
      421 nitsisfpal gtgnmeikke taaeilfdev ltfakdhvkh qltvkfvifp tdleiykafs
      481 semakrskml slnnysvpqs treekrengl earspainlm gfnveemyea hawiqrilsl
      541 qnhhiiennh ilylgrkehd ilsqlqktss vsiteiispg rteleiegar adlievvmni
      601 edmlckvqee markkerglw rslgqwtiqq qktqdemken iiflkcpvpp tqelldqkkq
      661 fekcglqvlk vekidnevlm aafqrkkkmm eeklhrqpvs hrlfqqvpyq fcnvvcrvgf
      721 qrmystpcdp kygagiyftk nlknlaekak kisaadkliy vfeaevltgf fcqghplniv
      781 ppplspgaid ghdsvvdnvs spetfvifsg mqaipqylwt ctqeyvqsqd yssgpmrpfa
      841 qhpwrgfasg spvd
//
LOCUS       NP_001008396              99 aa            linear   PRI 21-NOV-2025
DEFINITION  ragulator complex protein LAMTOR4 isoform 1 [Homo sapiens].
ACCESSION   NP_001008396 XP_371939
VERSION     NP_001008396.1
DBSOURCE    REFSEQ: accession NM_001008395.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Gamallat,Y., Alwazan,H., Turko,R., Dang,V., Seyedi,S., Ghosh,S. and
            Bismar,T.A.
  TITLE     Elevated LAMTOR4 Expression Is Associated with Lethal Prostate
            Cancer and Its Knockdown Decreases Cell Proliferation, Invasion,
            and Migration In Vitro
  JOURNAL   Int J Mol Sci 25 (15), 8100 (2024)
   PUBMED   39125671
  REMARK    GeneRIF: Elevated LAMTOR4 Expression Is Associated with Lethal
            Prostate Cancer and Its Knockdown Decreases Cell Proliferation,
            Invasion, and Migration In Vitro.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 99)
  AUTHORS   Zhang,S., Lee,S.H., Nie,L., Huang,Y., Zou,G., Jung,Y.S., Jun,S.,
            Zhang,J., Lien,E.M., Chen,J. and Park,J.I.
  TITLE     Lysosomal TMEM9-LAMTOR4-controlled mTOR signaling integrity is
            required for mammary tumorigenesis
  JOURNAL   Cancer Commun (Lond) 43 (1), 159-163 (2023)
   PUBMED   36336962
  REMARK    GeneRIF: Lysosomal TMEM9-LAMTOR4-controlled mTOR signaling
            integrity is required for mammary tumorigenesis.
REFERENCE   6  (residues 1 to 99)
  AUTHORS   Rebsamen,M., Pochini,L., Stasyk,T., de Araujo,M.E., Galluccio,M.,
            Kandasamy,R.K., Snijder,B., Fauster,A., Rudashevskaya,E.L.,
            Bruckner,M., Scorzoni,S., Filipek,P.A., Huber,K.V., Bigenzahn,J.W.,
            Heinz,L.X., Kraft,C., Bennett,K.L., Indiveri,C., Huber,L.A. and
            Superti-Furga,G.
  TITLE     SLC38A9 is a component of the lysosomal amino acid sensing
            machinery that controls mTORC1
  JOURNAL   Nature 519 (7544), 477-481 (2015)
   PUBMED   25561175
REFERENCE   7  (residues 1 to 99)
  AUTHORS   Blandin,G., Marchand,S., Charton,K., Daniele,N., Gicquel,E.,
            Boucheteil,J.B., Bentaib,A., Barrault,L., Stockholm,D., Bartoli,M.
            and Richard,I.
  TITLE     A human skeletal muscle interactome centered on proteins involved
            in muscular dystrophies: LGMD interactome
  JOURNAL   Skelet Muscle 3 (1), 3 (2013)
   PUBMED   23414517
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 99)
  AUTHORS   Bar-Peled,L., Schweitzer,L.D., Zoncu,R. and Sabatini,D.M.
  TITLE     Ragulator is a GEF for the rag GTPases that signal amino acid
            levels to mTORC1
  JOURNAL   Cell 150 (6), 1196-1208 (2012)
   PUBMED   22980980
  REMARK    GeneRIF: Study identified HBXIP and C7orf59 as two additional
            Ragulator components that are required for mTORC1 activation by
            amino acids.
REFERENCE   9  (residues 1 to 99)
  AUTHORS   Sancak,Y., Bar-Peled,L., Zoncu,R., Markhard,A.L., Nada,S. and
            Sabatini,D.M.
  TITLE     Ragulator-Rag complex targets mTORC1 to the lysosomal surface and
            is necessary for its activation by amino acids
  JOURNAL   Cell 141 (2), 290-303 (2010)
   PUBMED   20381137
REFERENCE   10 (residues 1 to 99)
  AUTHORS   Toulza,E., Mattiuzzo,N.R., Galliano,M.F., Jonca,N., Dossat,C.,
            Jacob,D., de Daruvar,A., Wincker,P., Serre,G. and Guerrin,M.
  TITLE     Large-scale identification of human genes implicated in epidermal
            barrier function
  JOURNAL   Genome Biol 8 (6), R107 (2007)
   PUBMED   17562024
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CU450474.1 and BI598677.1.
            
            On Dec 16, 2004 this sequence version replaced XP_371939.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC063401.1, BI754529.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341942.10/ ENSP00000343118.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..99
                     /product="ragulator complex protein LAMTOR4 isoform 1"
                     /note="UPF0539 protein C7orf59; late endosomal/lysosomal
                     adaptor and MAPK and MTOR activator 4; ragulator complex
                     protein LAMTOR4"
                     /calculated_mol_wt=10610
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q0VGL1.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in Ragulator complex protein
                     LAMTOR4, N-terminally processed.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (Q0VGL1.1)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:31314152; propagated from
                     UniProtKB/Swiss-Prot (Q0VGL1.1)"
     CDS             1..99
                     /gene="LAMTOR4"
                     /gene_synonym="C7orf59"
                     /coded_by="NM_001008395.4:56..355"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34702.1"
                     /db_xref="GeneID:389541"
                     /db_xref="HGNC:HGNC:33772"
                     /db_xref="MIM:618834"
ORIGIN      
        1 mtsaltqgle ripdqlgylv lsegavlass gdlendeqaa saiselvsta cgfrlhrgmn
       61 vpfkrlsvvf gehtllvtvs gqrvfvvkrq nrgrepidv
//
LOCUS       NP_001258936              60 aa            linear   PRI 21-NOV-2025
DEFINITION  iron-sulfur cluster assembly 2 homolog, mitochondrial isoform 2
            precursor [Homo sapiens].
ACCESSION   NP_001258936
VERSION     NP_001258936.1
DBSOURCE    REFSEQ: accession NM_001272007.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 60)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 60)
  AUTHORS   Bargagna,B., Staderini,T., Lang,S.H., Banci,L. and Camponeschi,F.
  TITLE     Defects in the Maturation of Mitochondrial Iron-Sulfur Proteins:
            Biophysical Investigation of the MMDS3 Causing Gly104Cys Variant of
            IBA57
  JOURNAL   Int J Mol Sci 25 (19), 10466 (2024)
   PUBMED   39408793
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 60)
  AUTHORS   Du,J., Huang,Z., Li,Y., Ren,X., Zhou,C., Liu,R., Zhang,P., Lei,G.,
            Lyu,J., Li,J. and Tan,G.
  TITLE     Copper exerts cytotoxicity through inhibition of iron-sulfur
            cluster biogenesis on ISCA1/ISCA2/ISCU assembly proteins
  JOURNAL   Free Radic Biol Med 204, 359-373 (2023)
   PUBMED   37225108
  REMARK    GeneRIF: Copper exerts cytotoxicity through inhibition of
            iron-sulfur cluster biogenesis on ISCA1/ISCA2/ISCU assembly
            proteins.
REFERENCE   4  (residues 1 to 60)
  AUTHORS   Green,Y.S., Ferreira Dos Santos,M.C., Fuja,D.G., Reichert,E.C.,
            Campos,A.R., Cowman,S.J., Acuna Pilarte,K., Kohan,J., Tripp,S.R.,
            Leibold,E.A., Sirohi,D., Agarwal,N., Liu,X. and Koh,M.Y.
  TITLE     ISCA2 inhibition decreases HIF and induces ferroptosis in clear
            cell renal carcinoma
  JOURNAL   Oncogene 41 (42), 4709-4723 (2022)
   PUBMED   36097192
  REMARK    GeneRIF: ISCA2 inhibition decreases HIF and induces ferroptosis in
            clear cell renal carcinoma.
REFERENCE   5  (residues 1 to 60)
  AUTHORS   Wang,J., Jiang,M., Yue,G., Zhu,L., Wang,X., Liang,M., Wu,X., Li,B.,
            Pang,Y., Tan,G. and Li,J.
  TITLE     ISCA2 deficiency leads to heme synthesis defects and impaired
            erythroid differentiation in K562 cells by indirect ROS-mediated
            IRP1 activation
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (10), 119307 (2022)
   PUBMED   35714932
  REMARK    GeneRIF: ISCA2 deficiency leads to heme synthesis defects and
            impaired erythroid differentiation in K562 cells by indirect
            ROS-mediated IRP1 activation.
REFERENCE   6  (residues 1 to 60)
  AUTHORS   Sheftel,A.D., Wilbrecht,C., Stehling,O., Niggemeyer,B.,
            Elsasser,H.P., Muhlenhoff,U. and Lill,R.
  TITLE     The human mitochondrial ISCA1, ISCA2, and IBA57 proteins are
            required for [4Fe-4S] protein maturation
  JOURNAL   Mol Biol Cell 23 (7), 1157-1166 (2012)
   PUBMED   22323289
  REMARK    GeneRIF: ISCA1, ISCA2, and IBA57 were depleted by RNA interference.
            Depleted cells contained massively swollen and enlarged
            mitochondria that were virtually devoid of cristae membranes,
            demonstrating the importance of these proteins for mitochondrial
            biogenesis.
REFERENCE   7  (residues 1 to 60)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   8  (residues 1 to 60)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 60)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 60)
  AUTHORS   Al-Hassnan,Z.N. and Kaya,N.
  TITLE     ISCA2-Related Mitochondrial Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29470032
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX114918.1, DB501282.1,
            BX248252.1 and AC005479.2.
            
            Summary: The protein encoded by this gene is an A-type iron-sulfur
            cluster (ISC) protein found in mitochondria. The encoded protein
            appears to be involved in the maturation of mitochondrial
            iron-sulfur proteins. Two transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Dec
            2012].
            
            Transcript Variant: This variant (2) lacks an alternate coding exon
            compared to variant 1, that causes a frameshift. The resulting
            isoform (2) has a shorter and distinct C-terminus compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB501282.1, DB485692.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2155770
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 22323289; reported by
                                                  MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..60
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..60
                     /product="iron-sulfur cluster assembly 2 homolog,
                     mitochondrial isoform 2 precursor"
                     /note="iron-sulfur cluster assembly 2 homolog,
                     mitochondrial; HESB-like domain-containing protein 1"
                     /calculated_mol_wt=5449
     transit_peptide 1..8
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q86U28.2)"
                     /calculated_mol_wt=780
     mat_peptide     9..60
                     /product="iron-sulfur cluster assembly 2 homolog,
                     mitochondrial isoform 2"
                     /calculated_mol_wt=5449
     Region          29..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86U28.2)"
     CDS             1..60
                     /gene="ISCA2"
                     /gene_synonym="c14_5557; HBLD1; ISA2; MMDS4"
                     /coded_by="NM_001272007.2:11..193"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS61504.1"
                     /db_xref="GeneID:122961"
                     /db_xref="HGNC:HGNC:19857"
                     /db_xref="MIM:615317"
ORIGIN      
        1 maaawgsslt aatqravtpw prgrlltasl gpqarreass sspeagegqi rltdscvqgi
//
LOCUS       NP_001308714            2349 aa            linear   PRI 21-NOV-2025
DEFINITION  protein TASOR 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001308714
VERSION     NP_001308714.2
DBSOURCE    REFSEQ: accession NM_001321785.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2349)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2349)
  AUTHORS   Jensvold,Z.D., Flood,J.R., Christenson,A.E. and Lewis,P.W.
  TITLE     Interplay between Two Paralogous Human Silencing Hub (HuSH)
            Complexes in Regulating LINE-1 Element Silencing
  JOURNAL   Nat Commun 15 (1), 9492 (2024)
   PUBMED   39489739
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2349)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   4  (residues 1 to 2349)
  AUTHORS   Krishnamoorthy,V., Foglizzo,M., Dilley,R.L., Wu,A., Datta,A.,
            Dutta,P., Campbell,L.J., Degtjarik,O., Musgrove,L.J.,
            Calabrese,A.N., Zeqiraj,E. and Greenberg,R.A.
  TITLE     The SPATA5-SPATA5L1 ATPase complex directs replisome proteostasis
            to ensure genome integrity
  JOURNAL   Cell 187 (9), 2250-2268 (2024)
   PUBMED   38554706
REFERENCE   5  (residues 1 to 2349)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 2349)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   7  (residues 1 to 2349)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   8  (residues 1 to 2349)
  AUTHORS   Savage,S.A., Mirabello,L., Wang,Z., Gastier-Foster,J.M.,
            Gorlick,R., Khanna,C., Flanagan,A.M., Tirabosco,R., Andrulis,I.L.,
            Wunder,J.S., Gokgoz,N., Patino-Garcia,A., Sierrasesumaga,L.,
            Lecanda,F., Kurucu,N., Ilhan,I.E., Sari,N., Serra,M., Hattinger,C.,
            Picci,P., Spector,L.G., Barkauskas,D.A., Marina,N., de Toledo,S.R.,
            Petrilli,A.S., Amary,M.F., Halai,D., Thomas,D.M., Douglass,C.,
            Meltzer,P.S., Jacobs,K., Chung,C.C., Berndt,S.I., Purdue,M.P.,
            Caporaso,N.E., Tucker,M., Rothman,N., Landi,M.T., Silverman,D.T.,
            Kraft,P., Hunter,D.J., Malats,N., Kogevinas,M., Wacholder,S.,
            Troisi,R., Helman,L., Fraumeni,J.F. Jr., Yeager,M., Hoover,R.N. and
            Chanock,S.J.
  TITLE     Genome-wide association study identifies two susceptibility loci
            for osteosarcoma
  JOURNAL   Nat Genet 45 (7), 799-803 (2013)
   PUBMED   23727862
REFERENCE   9  (residues 1 to 2349)
  AUTHORS   Oshikawa,M., Tsutsui,C., Ikegami,T., Fuchida,Y., Matsubara,M.,
            Toyama,S., Usami,R., Ohtoko,K. and Kato,S.
  TITLE     Full-length transcriptome analysis of human retina-derived cell
            lines ARPE-19 and Y79 using the vector-capping method
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6662-6670 (2011)
   PUBMED   21697133
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 2349)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL365356.13 and AL596094.2.
            
            On Aug 14, 2020 this sequence version replaced NP_001308714.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.434722.1,
                                           SRR14038191.2792954.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2349
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p15.1"
     Protein         1..2349
                     /product="protein TASOR 2 isoform 2"
                     /note="protein FAM208B; family with sequence similarity
                     208 member B; protein TASOR 2"
                     /calculated_mol_wt=259586
     Region          94..167
                     /region_name="DUF3699"
                     /note="Protein of unknown function (DUF3699); pfam12480"
                     /db_xref="CDD:463601"
     Region          471..620
                     /region_name="DUF3715"
                     /note="Protein of unknown function (DUF3715); pfam12509"
                     /db_xref="CDD:463613"
     CDS             1..2349
                     /gene="TASOR2"
                     /gene_synonym="bA318E3.2; C10orf18; FAM208B"
                     /coded_by="NM_001321785.2:699..7748"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS91209.1"
                     /db_xref="GeneID:54906"
                     /db_xref="HGNC:HGNC:23484"
                     /db_xref="MIM:621243"
ORIGIN      
        1 mappahksil ersenvlmsp wkgklivqdr mlcdialwst ygamiptqlp qeldfkyvmk
       61 vsslkkrlpe aafrkqnyle ekvcfqdlcf nlyevelsnr qgenidklte ciknkqlaii
      121 kcledrgffi lltssallse pdfggkqmgl hglhlfrspl stgvkdlkve ddismkvipi
      181 lstlncalle tkkslpeeri hpntlvkrhf qelykadrsp slsvapqdrm kdptflgklp
      241 sgfdlippae kcpsesltql nsyfsdpsay ilevstaldl laehpqspcv sdgicdagfs
      301 lvmtpdpefl vseaevrket etkkdseeml kakkrvfpls pasnlrvqpk rkasmphmvq
      361 skkvnlcrpf pkrtasradn ssdspttlkl vkgqfpqkrk rvkgetaskl qseisrgcqe
      421 dgisinsvqp enttaahndl pensivnyds qalnmladla lssatsstpv searnlhcss
      481 elpqndvlls kenslrgtsd heyhrgvktq kgellpnpss drksnsgsdl tvsqdeeslv
      541 pcsqapakaq salteemles sdasqsssvs vehsyalllt ehskkhlqer eilsplfprn
      601 gtkspeaatp vgkvmpfrhq pglllqqkpp ddpvvkpkdr ppsarvkkss csrivlscdd
      661 svkitfkcet eyafsldsky tnnplektvv ralhgpwntd lpdnveevkl llhmwvalfy
      721 snqnkiirss rkvvehsnpa kyvsinstle scelreiees lglekcsads lletneisra
      781 haaevsfrdp ncllpfiktp ltqglelcvq neqkktfare cdpdtqedqn ficsynnevt
      841 geeakqesle tsnlvlsgig stqtngpsvp seeeivqpld strvasysgt vtqatftrty
      901 dgpgsqpvic qssvygtlen kvdildaavq tktgtlqdli qhgspinnec hpslerkddn
      961 mgcavinpep itltfeknah vpiqtegvnt aderttfkke likqvspaas lrhpvstsen
     1021 artqglrdip slvvagqkgt kylcassvgg etldkavcsl qketplpvsl psdktmvmea
     1081 lslakssshl spseevrctq dflsqtqsll glssegllel tqvevdsssa sttlgrqcsl
     1141 ncissgchts gdslelrknh kngpntenmn leafdsvfik qtslsvsrev slelseedsd
     1201 idlaltispp tspreempag eieqfeeapf snlelqdvae eigepeeval tesrevssad
     1261 nvsvypsvse epvenkerkg dnlqpvtlil skenctleia eeinvtsdfp fdsvieevsp
     1321 asspeppvpv ketrpyqavt pcilklhgtq ceksnqisqc esedlgitek envfvgpthp
     1381 vgqdnftqvq qmqvsaempl iltdhpgrtg rptlpgkvte eivssehdeg lsfsgkvqcy
     1441 grelnqpasa akctgdfsps peklvksgnp lqpvsienrn ldlkhlvles seppfgprnv
     1501 ienkslsdtl vsttapsgiv nvsvkqqtsp kssqnhlfpg dlktdegiyl qvksltaasv
     1561 dgaystqgcm csvvptlcss sdnatlthyv rpinaepvfq aqeipagrma sllkngepea
     1621 elhkettgpg tagpqsntts slkgerkaih tlqdvstcet kellnvgvss lcagpyqnta
     1681 dtkenlskep lasfvsesfd tsvcgiateh veiensgegl raeagsetlg rdgevgvnsd
     1741 mhyelsgdsd ldllgdcrnp rldledsytl rgsytrkkdv ptdgyessln fhnnnqedwg
     1801 csswvpgmet slppghwtaa vkkeekcvpp yvqirdlhgi lrtyanfsit kelkdtmrts
     1861 hglrrhpsfs ancglpsswt stwqvaddlt qntldleylr fahklkqtik ngdsqhsass
     1921 anvfpkespt qisigafpst kiseapflhp aprsrspllv tvvesdprpq gqprrgytas
     1981 sldsssswre rcshnrdlrn sqrnhtvsfh lnklkynstv kesrndisli lneyaefnkv
     2041 mknsnqfifq dkelndvsge ataqemylpf pgrsasyedi iidvctnlhv klrsvvkeac
     2101 kstflfylve tedksffvrt knllrkgght eiepqhfcqa fhrendtlii iirnedissh
     2161 lhqipsllkl khfpsvifag vdspgdvldh tyqelfragg fvisddkile avtlvqlkei
     2221 ikileklngn grwkwllhyr enkklkeder vdstahkkni mlksfqsani iellhyhqcd
     2281 srsstkaeil kcllnlqiqh idarfavllt dkptiprevf ensgilvtdv nnfienieki
     2341 aapfrssyw
//
LOCUS       NP_700357                332 aa            linear   PRI 21-NOV-2025
DEFINITION  solute carrier family 22 member 12 isoform b [Homo sapiens].
ACCESSION   NP_700357
VERSION     NP_700357.1
DBSOURCE    REFSEQ: accession NM_153378.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   He,J., Liu,G., Kong,F., Tan,Q., Wang,Z., Yang,M., He,Y., Jia,X.,
            Yan,C., Wang,C. and Qian,H.
  TITLE     Structural basis for the transport and substrate selection of human
            urate transporter 1
  JOURNAL   Cell Rep 43 (8), 114628 (2024)
   PUBMED   39146184
  REMARK    GeneRIF: Structural basis for the transport and substrate selection
            of human urate transporter 1.
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Perdomo-Ramirez,A., Ramos-Trujillo,E. and Claverie-Martin,F.
  CONSRTM   RenalTube Group
  TITLE     New SLC22A12 (URAT1) Variant Associated with Renal Hypouricemia
            Identified by Whole-Exome Sequencing Analysis and Bioinformatics
            Predictions
  JOURNAL   Genes (Basel) 14 (9), 1823 (2023)
   PUBMED   37761963
  REMARK    GeneRIF: New SLC22A12 (URAT1) Variant Associated with Renal
            Hypouricemia Identified by Whole-Exome Sequencing Analysis and
            Bioinformatics Predictions.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Perdomo-Ramirez,A., Cordoba-Lanus,E., Trujillo-Frias,C.J.,
            Gonzalez-Navasa,C., Ramos-Trujillo,E., Luis-Yanes,M.I.,
            Garcia-Nieto,V. and Claverie-Martin,F.
  CONSRTM   RenalTube
  TITLE     Pathogenic Variants of SLC22A12 (URAT1) and SLC2A9 (GLUT9) in
            Spanish Patients with Renal Hypouricemia: Founder Effect of SLC2A9
            Variant c.374C>T; p.(T125M)
  JOURNAL   Int J Mol Sci 24 (9), 8455 (2023)
   PUBMED   37176161
  REMARK    GeneRIF: Pathogenic Variants of SLC22A12 (URAT1) and SLC2A9 (GLUT9)
            in Spanish Patients with Renal Hypouricemia: Founder Effect of
            SLC2A9 Variant c.374C>T; p.(T125M).
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Vargas-Morales,J.M., Guevara-Cruz,M., Aradillas-Garcia,C., G
            Noriega,L., Tovar,A. and Alegria-Torres,J.A.
  TITLE     Polymorphisms of the genes ABCG2, SLC22A12 and XDH and their
            relation with hyperuricemia and hypercholesterolemia in Mexican
            young adults
  JOURNAL   F1000Res 10, 217 (2021)
   PUBMED   34631016
  REMARK    GeneRIF: Polymorphisms of the genes ABCG2, SLC22A12 and XDH and
            their relation with hyperuricemia and hypercholesterolemia in
            Mexican young adults.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Anzai,N., Miyazaki,H., Noshiro,R., Khamdang,S., Chairoungdua,A.,
            Shin,H.J., Enomoto,A., Sakamoto,S., Hirata,T., Tomita,K., Kanai,Y.
            and Endou,H.
  TITLE     The multivalent PDZ domain-containing protein PDZK1 regulates
            transport activity of renal urate-anion exchanger URAT1 via its C
            terminus
  JOURNAL   J Biol Chem 279 (44), 45942-45950 (2004)
   PUBMED   15304510
  REMARK    GeneRIF: PDZK1 plays a role in regulating the functional activity
            of URAT1-mediated urate transport in the apical membrane of renal
            proximal tubules.
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Iwai,N., Mino,Y., Hosoyamada,M., Tago,N., Kokubo,Y. and Endou,H.
  TITLE     A high prevalence of renal hypouricemia caused by inactive SLC22A12
            in Japanese
  JOURNAL   Kidney Int 66 (3), 935-944 (2004)
   PUBMED   15327384
  REMARK    GeneRIF: SLC22A12 is a major gene for hypouricemia but not
            hyperuricemia in Japanese.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 332)
  AUTHORS   Ichida,K., Hosoyamada,M., Hisatome,I., Enomoto,A., Hikita,M.,
            Endou,H. and Hosoya,T.
  TITLE     Clinical and molecular analysis of patients with renal hypouricemia
            in Japan-influence of URAT1 gene on urinary urate excretion
  JOURNAL   J Am Soc Nephrol 15 (1), 164-173 (2004)
   PUBMED   14694169
REFERENCE   9  (residues 1 to 332)
  AUTHORS   Gisler,S.M., Pribanic,S., Bacic,D., Forrer,P., Gantenbein,A.,
            Sabourin,L.A., Tsuji,A., Zhao,Z.S., Manser,E., Biber,J. and
            Murer,H.
  TITLE     PDZK1: I. a major scaffolder in brush borders of proximal tubular
            cells
  JOURNAL   Kidney Int 64 (5), 1733-1745 (2003)
   PUBMED   14531806
REFERENCE   10 (residues 1 to 332)
  AUTHORS   Enomoto,A., Kimura,H., Chairoungdua,A., Shigeta,Y., Jutabha,P.,
            Cha,S.H., Hosoyamada,M., Takeda,M., Sekine,T., Igarashi,T.,
            Matsuo,H., Kikuchi,Y., Oda,T., Ichida,K., Hosoya,T., Shimokata,K.,
            Niwa,T., Kanai,Y. and Endou,H.
  TITLE     Molecular identification of a renal urate anion exchanger that
            regulates blood urate levels
  JOURNAL   Nature 417 (6887), 447-452 (2002)
   PUBMED   12024214
  REMARK    GeneRIF: Molecular identification of a renal urate anion exchanger
            that regulates blood urate levels
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB050269.1, AK055737.1,
            AP001092.5 and BC053348.1.
            
            Summary: The protein encoded by this gene is a member of the
            organic anion transporter (OAT) family, and it acts as a urate
            transporter to regulate urate levels in blood. This protein is an
            integral membrane protein primarily found in epithelial cells of
            the proximal tubule of the kidney. An elevated level of serum
            urate, hyperuricemia, is associated with increased incidences of
            gout, and mutations in this gene cause renal hypouricemia type 1.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2013].
            
            Transcript Variant: This variant (2) contains alternate 5' exon
            structure, lacks a portion of the 5' coding region, and uses a
            downstream in-frame start codon, compared to variant 1. The encoded
            isoform (b) is shorter at the N-terminus, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK055737.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145774, SAMEA2159080
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..332
                     /product="solute carrier family 22 member 12 isoform b"
                     /note="solute carrier family 22 (organic anion/cation
                     transporter), member 12; urate transporter 1; urate anion
                     exchanger 1; renal-specific transporter; organic anion
                     transporter 4-like protein; solute carrier family 22
                     (organic anion/urate transporter), member 12; urate:anion
                     antiporter SLC22A12; urate anion transporter 1"
                     /calculated_mol_wt=35439
     Region          <1..295
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     CDS             1..332
                     /gene="SLC22A12"
                     /gene_synonym="hURAT1; OAT4L; RST; UAT; URAT1"
                     /coded_by="NM_153378.3:735..1733"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:116085"
                     /db_xref="HGNC:HGNC:17989"
                     /db_xref="MIM:607096"
ORIGIN      
        1 mewtaararp lvmtlnslgf sfghgltaav aygvrdwtll qlvvsvpffl cflyswwlae
       61 sarwllttgr ldwglqelwr vaaingkgav qdtltpevll samreelsmg qppaslgtll
      121 rmpglrfrtc istlcwfafg ftffglaldl qalgsnifll qmfigvvdip akmgalllls
      181 hlgrrptlaa slllaglcil antlvphemg alrsalavlg lggvgaaftc itiysselfp
      241 tvlrmtavgl gqmaarggai lgplvrllgv hgpwlpllvy gtvpvlsgla alllpetqsl
      301 plpdtiqdvq nqavkkathg tlgnsvlkst qf
//
LOCUS       NP_000305                403 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and
            dual-specificity protein phosphatase PTEN isoform PTEN [Homo
            sapiens].
ACCESSION   NP_000305
VERSION     NP_000305.3
DBSOURCE    REFSEQ: accession NM_000314.8
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Chowdhury,S.G., Misra,S., Ghosh,G., Mukherjee,A., Gopi,P.,
            Pandya,P., Islam,M.M. and Karmakar,P.
  TITLE     NHEJ is promoted by the phosphorylation and phosphatase activity of
            PTEN via regulation of DNA-PKcs
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (8), 119828 (2024)
   PUBMED   39197593
  REMARK    GeneRIF: NHEJ is promoted by the phosphorylation and phosphatase
            activity of PTEN via regulation of DNA-PKcs.
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Huang,X., Zhang,D., Zhang,D., Guo,J., Gu,G., Wang,Y., Wu,G.,
            Wang,C., Fu,B. and Li,K.
  TITLE     Decoding PTEN: from biological functions to signaling pathways in
            tumors
  JOURNAL   Mol Biol Rep 51 (1), 1089 (2024)
   PUBMED   39446204
  REMARK    GeneRIF: Decoding PTEN: from biological functions to signaling
            pathways in tumors.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Derkyi-Kwarteng,L., Ghartey,F.N., Aidoo,E., Addae,E., Imbeah,E.G.,
            Brown,A.A. and Acquah,S.
  TITLE     A retrospective analysis suggests PTEN expression is associated
            with favorable clinicopathological features of breast cancer
  JOURNAL   Sci Rep 14 (1), 21645 (2024)
   PUBMED   39284903
  REMARK    GeneRIF: A retrospective analysis suggests PTEN expression is
            associated with favorable clinicopathological features of breast
            cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Trujano-Camacho,S., Cantu-de Leon,D., Perez-Yepez,E.,
            Contreras-Romero,C., Coronel-Hernandez,J., Millan-Catalan,O.,
            Rodriguez-Dorantes,M., Lopez-Camarillo,C., Gutierrez-Ruiz,C.,
            Jacobo-Herrera,N. and Perez-Plasencia,C.
  TITLE     HOTAIR Promotes the Hyperactivation of PI3K/Akt and
            Wnt/beta-Catenin Signaling Pathways via PTEN Hypermethylation in
            Cervical Cancer
  JOURNAL   Cells 13 (17), 1484 (2024)
   PUBMED   39273054
  REMARK    GeneRIF: HOTAIR Promotes the Hyperactivation of PI3K/Akt and
            Wnt/beta-Catenin Signaling Pathways via PTEN Hypermethylation in
            Cervical Cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Liang,H., He,S., Yang,J., Jia,X., Wang,P., Chen,X., Zhang,Z.,
            Zou,X., McNutt,M.A., Shen,W.H. and Yin,Y.
  TITLE     PTENalpha, a PTEN isoform translated through alternative
            initiation, regulates mitochondrial function and energy metabolism
  JOURNAL   Cell Metab 19 (5), 836-848 (2014)
   PUBMED   24768297
REFERENCE   6  (residues 1 to 403)
  AUTHORS   Hopkins,B.D., Fine,B., Steinbach,N., Dendy,M., Rapp,Z., Shaw,J.,
            Pappas,K., Yu,J.S., Hodakoski,C., Mense,S., Klein,J., Pegno,S.,
            Sulis,M.L., Goldstein,H., Amendolara,B., Lei,L., Maurer,M.,
            Bruce,J., Canoll,P., Hibshoosh,H. and Parsons,R.
  TITLE     A secreted PTEN phosphatase that enters cells to alter signaling
            and survival
  JOURNAL   Science 341 (6144), 399-402 (2013)
   PUBMED   23744781
  REMARK    GeneRIF: identified a 576-amino acid translational variant of PTEN,
            PTEN-Long, that arises from an alternative translation start site
            519 base pairs upstream of the ATG initiation sequence; PTEN-Long
            is a membrane-permeable lipid phosphatase that is secreted from
            cells and can enter other cells
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Steck,P.A., Pershouse,M.A., Jasser,S.A., Yung,W.K., Lin,H.,
            Ligon,A.H., Langford,L.A., Baumgard,M.L., Hattier,T., Davis,T.,
            Frye,C., Hu,R., Swedlund,B., Teng,D.H. and Tavtigian,S.V.
  TITLE     Identification of a candidate tumour suppressor gene, MMAC1, at
            chromosome 10q23.3 that is mutated in multiple advanced cancers
  JOURNAL   Nat Genet 15 (4), 356-362 (1997)
   PUBMED   9090379
REFERENCE   8  (residues 1 to 403)
  AUTHORS   Li,J., Yen,C., Liaw,D., Podsypanina,K., Bose,S., Wang,S.I., Puc,J.,
            Miliaresis,C., Rodgers,L., McCombie,R., Bigner,S.H.,
            Giovanella,B.C., Ittmann,M., Tycko,B., Hibshoosh,H., Wigler,M.H.
            and Parsons,R.
  TITLE     PTEN, a putative protein tyrosine phosphatase gene mutated in human
            brain, breast, and prostate cancer
  JOURNAL   Science 275 (5308), 1943-1947 (1997)
   PUBMED   9072974
REFERENCE   9  (residues 1 to 403)
  AUTHORS   Peiffer,S.L., Herzog,T.J., Tribune,D.J., Mutch,D.G., Gersell,D.J.
            and Goodfellow,P.J.
  TITLE     Allelic loss of sequences from the long arm of chromosome 10 and
            replication errors in endometrial cancers
  JOURNAL   Cancer Res 55 (9), 1922-1926 (1995)
   PUBMED   7728760
REFERENCE   10 (residues 1 to 403)
  AUTHORS   Yehia,L. and Eng,C.
  TITLE     PTEN Hamartoma Tumor Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301661
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC063965.8.
            
            On Aug 25, 2005 this sequence version replaced NP_000305.2.
            
            Summary: This gene was identified as a tumor suppressor that is
            mutated in a large number of cancers at high frequency. The protein
            encoded by this gene is a phosphatidylinositol-3,4,5-trisphosphate
            3-phosphatase. It contains a tensin like domain as well as a
            catalytic domain similar to that of the dual specificity protein
            tyrosine phosphatases. Unlike most of the protein tyrosine
            phosphatases, this protein preferentially dephosphorylates
            phosphoinositide substrates. It negatively regulates intracellular
            levels of phosphatidylinositol-3,4,5-trisphosphate in cells and
            functions as a tumor suppressor by negatively regulating AKT/PKB
            signaling pathway. The use of a non-canonical (CUG) upstream
            initiation site produces a longer isoform that initiates
            translation with a leucine, and is thought to be preferentially
            associated with the mitochondrial inner membrane. This longer
            isoform may help regulate energy metabolism in the mitochondria. A
            pseudogene of this gene is found on chromosome 9. Alternative
            splicing and the use of multiple translation start codons results
            in multiple transcript variants encoding different isoforms.
            [provided by RefSeq, Feb 2015].
            
            Transcript Variant: This variant (1) encodes multiple isoforms due
            to the use of alternative translation initiation codons. The
            longest isoform (PTEN-L, PMID:23744781; also known as PTENalpha,
            PMID: 24768297) is derived from the use of an upstream non-AUG
            (CUG) start codon, while two shorter isoforms are derived from
            downstream AUG start codons. The most abundant isoform (PTEN),
            which is derived from the use of the 5'-most AUG start codon, is
            represented in this RefSeq.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U92436.1, BC005821.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:24768297)
            MANE Ensembl match               :: ENST00000371953.8/
                                                ENSP00000361021.3
            RefSeq Select criteria           :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.31"
     Protein         1..403
                     /product="phosphatidylinositol 3,4,5-trisphosphate
                     3-phosphatase and dual-specificity protein phosphatase
                     PTEN isoform PTEN"
                     /EC_number="3.1.3.67"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="phosphatidylinositol-3,4,5-trisphosphate
                     3-phosphatase and dual-specificity protein phosphatase
                     PTEN; mitochondrial PTENalpha; MMAC1 phosphatase and
                     tensin homolog deleted on chromosome 10; mutated in
                     multiple advanced cancers 1; phosphatase and tensin-like
                     protein; PTENepsilon; PTEN variant PTEN-K267Rfs*9; PTEN
                     variant PTEN-R234Afs*11; inositol polyphosphate
                     3-phosphatase; mitochondrial phosphatase and tensin
                     protein alpha; protein tyrosine phosphatase; PTEN variant
                     PTEN-L247*"
                     /calculated_mol_wt=47035
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P60484.1)"
     Region          24..181
                     /region_name="PTP_PTEN"
                     /note="protein tyrosine phosphatase-like catalytic domain
                     of phosphatase and tensin homolog; cd14509"
                     /db_xref="CDD:350359"
     Region          188..349
                     /region_name="PTEN_C2"
                     /note="C2 domain of PTEN tumour-suppressor protein;
                     pfam10409"
                     /db_xref="CDD:463081"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08586; propagated from
                     UniProtKB/Swiss-Prot (P60484.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:26166433; propagated from
                     UniProtKB/Swiss-Prot (P60484.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:26166433; propagated from
                     UniProtKB/Swiss-Prot (P60484.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by FRK.
                     /evidence=ECO:0000269|PubMed:19345329; propagated from
                     UniProtKB/Swiss-Prot (P60484.1)"
     Region          338..348
                     /region_name="Required for interaction with NOP53.
                     /evidence=ECO:0000269|PubMed:15355975"
                     /note="propagated from UniProtKB/Swiss-Prot (P60484.1)"
     Region          352..403
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60484.1)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by GSK3-beta and PLK3.
                     /evidence=ECO:0000269|PubMed:12297295,
                     ECO:0000269|PubMed:20940307, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P60484.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2 and PLK3.
                     /evidence=ECO:0000269|PubMed:11035045,
                     ECO:0000269|PubMed:12297295, ECO:0000269|PubMed:20940307;
                     propagated from UniProtKB/Swiss-Prot (P60484.1)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ROCK1 and CK2.
                     /evidence=ECO:0000269|PubMed:11035045; propagated from
                     UniProtKB/Swiss-Prot (P60484.1)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ROCK1 and CK2.
                     /evidence=ECO:0000269|PubMed:11035045; propagated from
                     UniProtKB/Swiss-Prot (P60484.1)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ROCK1 and CK2.
                     /evidence=ECO:0000269|PubMed:11035045; propagated from
                     UniProtKB/Swiss-Prot (P60484.1)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:11035045,
                     ECO:0000269|PubMed:12297295; propagated from
                     UniProtKB/Swiss-Prot (P60484.1)"
     Region          401..403
                     /region_name="PDZ domain-binding.
                     /evidence=ECO:0000250|UniProtKB:O08586"
                     /note="propagated from UniProtKB/Swiss-Prot (P60484.1)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:10646847; propagated from
                     UniProtKB/Swiss-Prot (P60484.1)"
     CDS             1..403
                     /gene="PTEN"
                     /gene_synonym="10q23del; BZS; CWS1; DEC; GLM2; MHAM;
                     MMAC1; PTEN1; PTENbeta; PTENgama; TEP1"
                     /coded_by="NM_000314.8:846..2057"
                     /note="isoform PTEN is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31238.1"
                     /db_xref="GeneID:5728"
                     /db_xref="HGNC:HGNC:9588"
                     /db_xref="MIM:601728"
ORIGIN      
        1 mtaiikeivs rnkrryqedg fdldltyiyp niiamgfpae rlegvyrnni ddvvrfldsk
       61 hknhykiynl caerhydtak fncrvaqypf edhnppqlel ikpfcedldq wlseddnhva
      121 aihckagkgr tgvmicayll hrgkflkaqe aldfygevrt rdkkgvtips qrryvyyysy
      181 llknhldyrp vallfhkmmf etipmfsggt cnpqfvvcql kvkiyssnsg ptrredkfmy
      241 fefpqplpvc gdikveffhk qnkmlkkdkm fhfwvntffi pgpeetsekv engslcdqei
      301 dsicsierad ndkeylvltl tkndldkank dkanryfspn fkvklyftkt veepsnpeas
      361 sstsvtpdvs dnepdhyrys dttdsdpene pfdedqhtqi tkv
//
LOCUS       NP_001378853            1855 aa            linear   PRI 21-NOV-2025
DEFINITION  Golgi-specific brefeldin A-resistance guanine nucleotide exchange
            factor 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001378853
VERSION     NP_001378853.1
DBSOURCE    REFSEQ: accession NM_001391924.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1855)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1855)
  AUTHORS   Hirano,J., Hayashi,T., Kitamura,K., Nishimura,Y., Shimizu,H.,
            Okamoto,T., Okada,K., Uemura,K., Yeh,M.T., Ono,C., Taguwa,S.,
            Muramatsu,M. and Matsuura,Y.
  TITLE     Enterovirus 3A protein disrupts endoplasmic reticulum homeostasis
            through interaction with GBF1
  JOURNAL   J Virol 98 (7), e0081324 (2024)
   PUBMED   38904364
  REMARK    GeneRIF: Enterovirus 3A protein disrupts endoplasmic reticulum
            homeostasis through interaction with GBF1.
REFERENCE   3  (residues 1 to 1855)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1855)
  AUTHORS   Navare,A.T., Mast,F.D., Olivier,J.P., Bertomeu,T., Neal,M.L.,
            Carpp,L.N., Kaushansky,A., Coulombe-Huntington,J., Tyers,M. and
            Aitchison,J.D.
  TITLE     Viral protein engagement of GBF1 induces host cell vulnerability
            through synthetic lethality
  JOURNAL   J Cell Biol 221 (11) (2022)
   PUBMED   36305789
  REMARK    GeneRIF: Viral protein engagement of GBF1 induces host cell
            vulnerability through synthetic lethality.
REFERENCE   5  (residues 1 to 1855)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1855)
  AUTHORS   Garcia-Mata,R. and Sztul,E.
  TITLE     The membrane-tethering protein p115 interacts with GBF1, an ARF
            guanine-nucleotide-exchange factor
  JOURNAL   EMBO Rep 4 (3), 320-325 (2003)
   PUBMED   12634853
  REMARK    GeneRIF: novel interaction between p115 and Golgi-specific
            brefeldin-A-resistant factor 1 (GBF1)
REFERENCE   7  (residues 1 to 1855)
  AUTHORS   Kawamoto,K., Yoshida,Y., Tamaki,H., Torii,S., Shinotsuka,C.,
            Yamashina,S. and Nakayama,K.
  TITLE     GBF1, a guanine nucleotide exchange factor for ADP-ribosylation
            factors, is localized to the cis-Golgi and involved in membrane
            association of the COPI coat
  JOURNAL   Traffic 3 (7), 483-495 (2002)
   PUBMED   12047556
  REMARK    GeneRIF: detailed subcellular localization to the cis-Golgi
REFERENCE   8  (residues 1 to 1855)
  AUTHORS   Verhoeven,K., Villanova,M., Rossi,A., Malandrini,A., De Jonghe,P.
            and Timmerman,V.
  TITLE     Localization of the gene for the intermediate form of
            Charcot-Marie-Tooth to chromosome 10q24.1-q25.1
  JOURNAL   Am J Hum Genet 69 (4), 889-894 (2001)
   PUBMED   11533914
REFERENCE   9  (residues 1 to 1855)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   10 (residues 1 to 1855)
  AUTHORS   Mansour,S.J., Herbrick,J.A., Scherer,S.W. and Melancon,P.
  TITLE     Human GBF1 is a ubiquitously expressed gene of the sec7 domain
            family mapping to 10q24
  JOURNAL   Genomics 54 (2), 323-327 (1998)
   PUBMED   9828135
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160011.35, AL356420.14 and
            AL121928.13.
            
            Summary: This gene encodes a member of the Sec7 domain family. The
            encoded protein is a guanine nucleotide exchange factor that
            regulates the recruitment of proteins to membranes by mediating GDP
            to GTP exchange. The encoded protein is localized to the Golgi
            apparatus and plays a role in vesicular trafficking by activating
            ADP ribosylation factor 1. The encoded protein has also been
            identified as an important host factor for viral replication.
            Multiple transcript variants have been observed for this gene.
            [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC117682.1 [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1855
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..1855
                     /product="Golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1 isoform 3"
                     /note="golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1; BFA-resistant GEF 1"
                     /calculated_mol_wt=205886
     Region          1..211
                     /region_name="DCB, DCB:DCB domain and DCB:HUS domain
                     interaction. /evidence=ECO:0000250|UniProtKB:Q9R1D7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          215..266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          <429..>1178
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          530..550
                     /region_name="HUS, DCB:HUS domain interaction.
                     /evidence=ECO:0000250|UniProtKB:Q9R1D7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          619..665
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          699..884
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          886..1370
                     /region_name="Phosphatidylinositol-phosphate binding,
                     required for translocation to the leading edge and for
                     ARF1 activation upon GPCR signaling.
                     /evidence=ECO:0000269|PubMed:22573891"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1284..1335
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1316
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1337
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AMPK.
                     /evidence=ECO:0000269|PubMed:18063581; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1350..1370
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1430..1483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1721..1804
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1769
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1780
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          <1790..1853
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1855
                     /gene="GBF1"
                     /gene_synonym="ARF1GEF; CMT2GG; CMTDI2; CMTDIA"
                     /coded_by="NM_001391924.1:423..5990"
                     /note="isoform 3 is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS91333.1"
                     /db_xref="GeneID:8729"
                     /db_xref="HGNC:HGNC:4181"
                     /db_xref="MIM:603698"
ORIGIN      
        1 mvdkniyiiq geinivvgai krnarwstht pldeerdpll hsfghlkevl nsitelseie
       61 pnvflrpfle virsedttgp itglaltsvn kflsyalidp thegtaegme nmadavthar
      121 fvgtdpasde vvlmkilqvl rtllltpvga hltnesvcei mqscfricfe mrlsellrks
      181 aehtlvdmvq llftrlpqfk eepknyvgtn mkklkmragg msdsskwkkq krsprpprhm
      241 tkvtpgselp tpngttlssn ltggmpfidv ptpissasse aasavvspst dsglefssqt
      301 tskedltdle qpgspgysta tepgsselgv peqpdlqegt hveksqsasv esipevleec
      361 tspadhsdsa svhdmdyvnp rgvrftqssq kegtalvpyg lpcirelfrf lisltnphdr
      421 hnsevmihmg lhlltvales apvaqcqtll glikdemcrh lfqllsierl nlyaaslrvc
      481 fllfesmreh lkfqmemyik klmeiitven pkmpyemkem aleaivqlwr ipsfvtelyi
      541 nydcdyycsn lfeeltklls knafpvsgql ytthllslda lltvidstea hcqakvlnsl
      601 tqqekketar psceivdgtr easntertas dgkavgmasd ipglhlpggg rlppehgksg
      661 csdleeavds gadkkfarkp prfscllpdp relieiknkk kllitgteqf nqkpkkgiqf
      721 lqekglltip mdntevaqwl renprldkkm igefvsdrkn idllesfvst fsfqglrlde
      781 alrlyleafr lpgeapviqr lleafterwm ncngspfans dacfslayav imlntdqhnh
      841 nvrkqnapmt leefrknlkg vnggkdfeqd iledmyhaik neeivmpeeq tglvrenyvw
      901 nvllhrgatp egiflrvpta sydldlftmt wgptiaalsy vfdksleeti iqkaisgfrk
      961 camisahygl sdvfdnliis lckftalsse sienlpsvfg snpkahiaak tvfhlahrhg
     1021 dilregwkni meamlqlfra qllpkamiev edfvdpngki slqreetpsn rgestvlsfv
     1081 swltlsgpeq ssvrgpsten qeakrvalec ikqcdpekmi teskflqles lqelmkalvs
     1141 vtpdeetyde edaafcleml lrivlenrdr vgcvwqtvrd hlyhlcvqaq dfcflverav
     1201 vgllrlairl lrreeisaqv llslrilllm kpsvlsrvsh qvayglhell ktnaanihsg
     1261 ddwatlftll ecigsgvkpp aalqatarad apdagaqsds elpsyhqndv sldrgytsds
     1321 evytdhgrpg kihrsatdad vvnsgwlvvg kddvdnskpg psrpgpspli nqysltvgld
     1381 lgphdtksll kcveslsfiv rdaahitpdn felcvktlri fveaslnggc ksqekrgksh
     1441 kydskgnrfk kkskegsmlr rprtssqhas rggqsddded egvpasyhtv slqlldlmht
     1501 lhtraasiys swaeeqrhle tggqkieads rtlwahcwcp llqgiaclcc darrqvrmqa
     1561 ltylqrallv hdlqkldale wescfnkvlf plltklleni spadvggmee trmrastlls
     1621 kvflqhlspl lslstfaalw ltildfmdky mhagssdlls eaipeslknm llvmdtaeif
     1681 hsadargggp salweitwer idcflphlrd elfkqtviqd pmpmepqgqk plasahltsa
     1741 agdtrtpghp pppeipselg acdfekpesp raasssspgs pvasspsrls ptpdgpppla
     1801 qpplilqpla splqvgvppm tlpiilnpal ieatspvpll atprptdpip tsevn
//
LOCUS       NP_001358073            1211 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal cell adhesion molecule isoform D precursor [Homo sapiens].
ACCESSION   NP_001358073
VERSION     NP_001358073.1
DBSOURCE    REFSEQ: accession NM_001371144.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1211)
  AUTHORS   Wang,C., Wang,Z., Fu,L., Du,J., Ji,F. and Qiu,X.
  TITLE     CircNRCAM up-regulates NRCAM to promote papillary thyroid carcinoma
            progression
  JOURNAL   J Endocrinol Invest 47 (5), 1215-1226 (2024)
   PUBMED   38485895
  REMARK    GeneRIF: CircNRCAM up-regulates NRCAM to promote papillary thyroid
            carcinoma progression.
REFERENCE   2  (residues 1 to 1211)
  AUTHORS   Zhou,L., He,L., Liu,C.H., Qiu,H., Zheng,L., Sample,K.M., Wu,Q.,
            Li,J., Xie,K., Ampuero,J., Li,Z., Lv,D., Liu,M., Romero-Gomez,M.,
            Hu,Y. and Tang,H.
  TITLE     Liver cancer stem cell dissemination and metastasis: uncovering the
            role of NRCAM in hepatocellular carcinoma
  JOURNAL   J Exp Clin Cancer Res 42 (1), 311 (2023)
   PUBMED   37993901
  REMARK    GeneRIF: Liver cancer stem cell dissemination and metastasis:
            uncovering the role of NRCAM in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1211)
  AUTHORS   Sannes,A.C., Christensen,J.O., Nielsen,M.B. and Gjerstad,J.
  TITLE     Stress-induced headache in the general working population is
            moderated by the NRCAM rs2300043 genotype
  JOURNAL   Scand J Pain 23 (2), 326-332 (2022)
   PUBMED   36181733
  REMARK    GeneRIF: Stress-induced headache in the general working population
            is moderated by the NRCAM rs2300043 genotype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1211)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 1211)
  AUTHORS   Bai,C. and Chen,D.G.
  TITLE     NRCAM acts as a prognostic biomarker and promotes the tumor
            progression in gastric cancer via EMT pathway
  JOURNAL   Tissue Cell 77, 101859 (2022)
   PUBMED   35763884
  REMARK    GeneRIF: NRCAM acts as a prognostic biomarker and promotes the
            tumor progression in gastric cancer via EMT pathway.
REFERENCE   6  (residues 1 to 1211)
  AUTHORS   Wang,B., Williams,H., Du,J.S., Terrett,J. and Kenwrick,S.
  TITLE     Alternative splicing of human NrCAM in neural and nonneural tissues
  JOURNAL   Mol Cell Neurosci 10 (5-6), 287-295 (1998)
   PUBMED   9604207
REFERENCE   7  (residues 1 to 1211)
  AUTHORS   Grumet,M.
  TITLE     Nr-CAM: a cell adhesion molecule with ligand and receptor functions
  JOURNAL   Cell Tissue Res 290 (2), 423-428 (1997)
   PUBMED   9321706
  REMARK    Review article
REFERENCE   8  (residues 1 to 1211)
  AUTHORS   Sakurai,T., Lustig,M., Nativ,M., Hemperly,J.J., Schlessinger,J.,
            Peles,E. and Grumet,M.
  TITLE     Induction of neurite outgrowth through contactin and Nr-CAM by
            extracellular regions of glial receptor tyrosine phosphatase beta
  JOURNAL   J Cell Biol 136 (4), 907-918 (1997)
   PUBMED   9049255
REFERENCE   9  (residues 1 to 1211)
  AUTHORS   Volkmer,H., Leuschner,R., Zacharias,U. and Rathjen,F.G.
  TITLE     Neurofascin induces neurites by heterophilic interactions with
            axonal NrCAM while NrCAM requires F11 on the axonal surface to
            extend neurites
  JOURNAL   J Cell Biol 135 (4), 1059-1069 (1996)
   PUBMED   8922386
REFERENCE   10 (residues 1 to 1211)
  AUTHORS   Lane,R.P., Chen,X.N., Yamakawa,K., Vielmetter,J., Korenberg,J.R.
            and Dreyer,W.J.
  TITLE     Characterization of a highly conserved human homolog to the chicken
            neural cell surface protein Bravo/Nr-CAM that maps to chromosome
            band 7q31
  JOURNAL   Genomics 35 (3), 456-465 (1996)
   PUBMED   8812479
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005058.1, AC007567.2 and
            AC005683.2.
            
            Summary: Cell adhesion molecules (CAMs) are members of the
            immunoglobulin superfamily. This gene encodes a neuronal cell
            adhesion molecule with multiple immunoglobulin-like C2-type domains
            and fibronectin type-III domains. This ankyrin-binding protein is
            involved in neuron-neuron adhesion and promotes directional
            signaling during axonal cone growth. This gene is also expressed in
            non-neural tissues and may play a general role in cell-cell
            communication via signaling from its intracellular domain to the
            actin cytoskeleton during directional cell migration. Allelic
            variants of this gene have been associated with autism and
            addiction vulnerability. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (13), as well as variants 4, 12,
            and 14, encodes isoform D.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1211
                     /product="neuronal cell adhesion molecule isoform D
                     precursor"
                     /note="NgCAM-related cell adhesion molecule; neuronal
                     surface protein Bravo"
                     /calculated_mol_wt=130517
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3315
     Region          46..140
                     /region_name="IgI_NrCAM"
                     /note="Immunoglobulin (Ig)-like domain of NrCAM (Ng
                     (neuronglia) CAM-related cell adhesion molecule); member
                     of the I-set of Ig superfamily (IgSF) domains; cd05874"
                     /db_xref="CDD:409458"
     Region          46..50
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409458"
     Region          55..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409458"
     Region          64..71
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409458"
     Region          77..82
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409458"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          85..87
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409458"
     Region          94..97
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409458"
     Region          102..106
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409458"
     Region          119..127
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409458"
     Region          130..140
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409458"
     Region          149..238
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          163..167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          177..181
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          200..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          215..220
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          231..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            245
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            251
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          277..358
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          288..292
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          301..305
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            314
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          323..327
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          337..342
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          350..353
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          362..450
                     /region_name="Ig4_NrCAM"
                     /note="Fourth immunoglobulin (Ig)-like domain of NrCAM
                     (NgCAM-related cell adhesion molecule); cd05868"
                     /db_xref="CDD:409454"
     Region          378..382
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409454"
     Region          391..395
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409454"
     Region          415..419
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409454"
     Region          429..434
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409454"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          442..445
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409454"
     Region          459..542
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          472..476
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          485..489
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            507
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          508..512
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          522..527
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          535..538
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          546..1060
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            619
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          647..737
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(647,713,728)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            716
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            order(729..730,732..733)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            802
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            858
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            993
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1009
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1019
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          1098..1187
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     CDS             1..1211
                     /gene="NRCAM"
                     /gene_synonym="NEDNMS"
                     /coded_by="NM_001371144.1:790..4425"
                     /note="isoform D precursor is encoded by transcript
                     variant 13"
                     /db_xref="CCDS:CCDS75652.1"
                     /db_xref="GeneID:4897"
                     /db_xref="HGNC:HGNC:7994"
                     /db_xref="MIM:601581"
ORIGIN      
        1 mqlkimpkkk rlsagrvpli lflcqmisal evpldpklle dlvqpptitq qspkdyiidp
       61 reniviqcea kgkpppsfsw trngthfdid kdplvtmkpg tgtliinims egkaetyegv
      121 yqctarnerg aavsnnivvr psrsplwtke klepitlqsg qslvlpcrpp iglpppiifw
      181 mdnsfqrlpq servsqglng dlyfsnvlpe dtredyicya rfnhtqtiqq kqpisvkvis
      241 vdelndtiaa nlsdtefyga kssrerpptf ltpegnasnk eelrgnvlsl eciaeglptp
      301 iiywakedgm lpknrtvykn fektlqiihv seadsgnyqc iaknalgaih htisvrvkaa
      361 pywitapqnl vlspgedgtl icrangnpkp riswltngvp ieiapddpsr kidgdtiifs
      421 nvqerssavy qcnasneygy llanafvnvl aeppriltpa ntlyqvianr palldcaffg
      481 splptiewfk gakgsalhed iyvlhengtl eipvaqkdst gtytcvarnk lgmaknevhl
      541 eikdptwivk qpeyavvqrg smvsfeckvk hdhtlsltvl wlkdnrelps derftvdkdh
      601 lvvadvsddd sgtytcvant tldsvsasav lsvvaptptp apvydvpnpp fdleltdqld
      661 ksvqlswtpg ddnnspitkf iieyedamhk pglwhhqtev sgtqttaqlk lspyvnysfr
      721 vmavnsigks lpseaseqyl tkasepdknp taveglgsep dnlvitwkpl ngfesngpgl
      781 qykvswrqkd gddewtsvvv anvskyivsg tptfvpylik vqalndmgfa pepavvmghs
      841 gedlpmvapg nvrvnvvnst laevhwdpvp lksirghlqg yriyywktqs sskrnrrhie
      901 kkiltfqgsk thgmlpglep fshytlnvrv vngkgegpas pdrvfntpeg vpsapsslki
      961 vnptldsltl ewdppshpng ilteytlkyq pinsthelgp lvdlkipank trwtlknlnf
     1021 strykfyfya qtsagsgsqi teeavttvde agilppdvga gkamasrqvd iatqgwfigl
     1081 mcavallili llivcfirrn kggkypvkek edahadpeiq pmkeddgtfg eysdaedhkp
     1141 lkkgsrtpsd rtvkkedsdd slvdygegvn gqfnedgsfi gqysgkkeke paegnessea
     1201 pspvnamnsf v
//
LOCUS       NP_001269028             470 aa            linear   PRI 21-NOV-2025
DEFINITION  transcriptional coactivator YAP1 isoform 7 [Homo sapiens].
ACCESSION   NP_001269028 XP_005271441
VERSION     NP_001269028.1
DBSOURCE    REFSEQ: accession NM_001282099.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Tang,W., Yang,Y., Fu,Z., Xu,W., Ou,W., Liu,F., Du,P. and Liu,C.Y.
  TITLE     The RNA helicase DDX21 activates YAP to promote tumorigenesis and
            is transcriptionally upregulated by beta-catenin in colorectal
            cancer
  JOURNAL   Oncogene 43 (44), 3227-3239 (2024)
   PUBMED   39285230
  REMARK    GeneRIF: The RNA helicase DDX21 activates YAP to promote
            tumorigenesis and is transcriptionally upregulated by beta-catenin
            in colorectal cancer.
REFERENCE   3  (residues 1 to 470)
  AUTHORS   He,C., Lv,X., Liu,J., Ruan,J., Chen,P., Huang,C., Angeletti,P.C.,
            Hua,G., Moness,M.L., Shi,D., Dhar,A., Yang,S., Murphy,S.,
            Montoute,I., Chen,X., Islam,K.N., George,S., Ince,T.A., Drapkin,R.,
            Guda,C., Davis,J.S. and Wang,C.
  TITLE     HPV-YAP1 oncogenic alliance drives malignant transformation of
            fallopian tube epithelial cells
  JOURNAL   EMBO Rep 25 (10), 4542-4569 (2024)
   PUBMED   39271776
  REMARK    GeneRIF: HPV-YAP1 oncogenic alliance drives malignant
            transformation of fallopian tube epithelial cells.
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Meyer,N.P., Singh,T., Kutys,M.L., Nystul,T.G. and Barber,D.L.
  TITLE     Arp2/3 complex activity enables nuclear YAP for naive pluripotency
            of human embryonic stem cells
  JOURNAL   Elife 13, e89725 (2024)
   PUBMED   39319536
  REMARK    GeneRIF: Arp2/3 complex activity enables nuclear YAP for naive
            pluripotency of human embryonic stem cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 470)
  AUTHORS   Jimbo,N., Ohbayashi,C., Fujii,T., Takeda,M., Mitsui,S., Tanaka,Y.,
            Itoh,T. and Maniwa,Y.
  TITLE     The expression of YAP1 and other transcription factors contributes
            to lineage plasticity in combined small cell lung carcinoma
  JOURNAL   J Pathol Clin Res 10 (5), e70001 (2024)
   PUBMED   39283755
  REMARK    GeneRIF: The expression of YAP1 and other transcription factors
            contributes to lineage plasticity in combined small cell lung
            carcinoma.
REFERENCE   6  (residues 1 to 470)
  AUTHORS   Gaffney,C.J., Oka,T., Mazack,V., Hilman,D., Gat,U., Muramatsu,T.,
            Inazawa,J., Golden,A., Carey,D.J., Farooq,A., Tromp,G. and Sudol,M.
  TITLE     Identification, basic characterization and evolutionary analysis of
            differentially spliced mRNA isoforms of human YAP1 gene
  JOURNAL   Gene 509 (2), 215-222 (2012)
   PUBMED   22939869
REFERENCE   7  (residues 1 to 470)
  AUTHORS   Gavva,N.R., Gavva,R., Ermekova,K., Sudol,M. and Shen,C.J.
  TITLE     Interaction of WW domains with hematopoietic transcription factor
            p45/NF-E2 and RNA polymerase II
  JOURNAL   J Biol Chem 272 (39), 24105-24108 (1997)
   PUBMED   9305852
REFERENCE   8  (residues 1 to 470)
  AUTHORS   Chen,H.I., Einbond,A., Kwak,S.J., Linn,H., Koepf,E., Peterson,S.,
            Kelly,J.W. and Sudol,M.
  TITLE     Characterization of the WW domain of human yes-associated protein
            and its polyproline-containing ligands
  JOURNAL   J Biol Chem 272 (27), 17070-17077 (1997)
   PUBMED   9202023
REFERENCE   9  (residues 1 to 470)
  AUTHORS   Chen,H.I. and Sudol,M.
  TITLE     The WW domain of Yes-associated protein binds a proline-rich ligand
            that differs from the consensus established for Src homology
            3-binding modules
  JOURNAL   Proc Natl Acad Sci U S A 92 (17), 7819-7823 (1995)
   PUBMED   7644498
REFERENCE   10 (residues 1 to 470)
  AUTHORS   Sudol,M., Bork,P., Einbond,A., Kastury,K., Druck,T., Negrini,M.,
            Huebner,K. and Lehman,D.
  TITLE     Characterization of the mammalian YAP (Yes-associated protein) gene
            and its role in defining a novel protein module, the WW domain
  JOURNAL   J Biol Chem 270 (24), 14733-14741 (1995)
   PUBMED   7782338
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001527.5, BC038235.1,
            HE864161.1, BC026212.2, AP000942.6, AL832620.2 and AI128142.1.
            
            On Aug 31, 2013 this sequence version replaced XP_005271441.1.
            
            Summary: This gene encodes a downstream nuclear effector of the
            Hippo signaling pathway which is involved in development, growth,
            repair, and homeostasis. This gene is known to play a role in the
            development and progression of multiple cancers as a
            transcriptional regulator of this signaling pathway and may
            function as a potential target for cancer treatment. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (7) lacks an alternate in-frame
            exon in the coding region, compared to variant 9. The encoded
            protein (isoform 7) represents the YAP1-1delta isoform described in
            Figure 3 of PMID: 22939869. It is shorter, compared to isoform 9.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.229612.1,
                                           SRR14038194.3338793.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.1"
     Protein         1..470
                     /product="transcriptional coactivator YAP1 isoform 7"
                     /note="65 kDa Yes-associated protein; yorkie homolog;
                     yes-associated protein 2; protein yorkie homolog;
                     yes-associated protein YAP65 homolog; transcriptional
                     coactivator YAP1; Yes associated protein 1"
                     /calculated_mol_wt=50338
     Region          174..203
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(188,199)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     CDS             1..470
                     /gene="YAP1"
                     /gene_synonym="COB1; YAP; YAP-1; YAP2; YAP65; YKI"
                     /coded_by="NM_001282099.2:403..1815"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS73374.1"
                     /db_xref="GeneID:10413"
                     /db_xref="HGNC:HGNC:16262"
                     /db_xref="MIM:606608"
ORIGIN      
        1 mdpgqqpppq papqgqgqpp sqppqgqgpp sgpgqpapaa tqaapqappa ghqivhvrgd
       61 setdlealfn avmnpktanv pqtvpmrlrk lpdsffkppe pkshsrqast dagtagaltp
      121 qhvrahsspa slqlgavspg tltptgvvsg paatptaqhl rqssfeipdd vplpagwema
      181 ktssgqryfl nhidqtttwq dprkamlsqm nvtaptsppv qqnmmnsasa mnqrisqsap
      241 vkqppplapq spqggvmggs nsnqqqqmrl qqlqmekerl rlkqqellrq vrpqamrnin
      301 pstanspkcq elalrsqlpt leqdggtqnp vsspgmsqel rtmttnssdp flnsgtyhsr
      361 destdsglsm ssysvprtpd dflnsvdemd tgdtinqstl psqqnrfpdy leaipgtnvd
      421 lgtlegdgmn iegeelmpsl qealssdiln dmesvlaatk ldkesfltwl
//
LOCUS       NP_001361801            1730 aa            linear   PRI 21-NOV-2025
DEFINITION  cullin-7 isoform 1 [Homo sapiens].
ACCESSION   NP_001361801 XP_016867026
VERSION     NP_001361801.1
DBSOURCE    REFSEQ: accession NM_001374872.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1730)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1730)
  AUTHORS   Zhou,H.L., Grimmett,Z.W., Venetos,N.M., Stomberski,C.T., Qian,Z.,
            McLaughlin,P.J., Bansal,P.K., Zhang,R., Reynolds,J.D., Premont,R.T.
            and Stamler,J.S.
  TITLE     An enzyme that selectively S-nitrosylates proteins to regulate
            insulin signaling
  JOURNAL   Cell 186 (26), 5812-5825 (2023)
   PUBMED   38056462
REFERENCE   3  (residues 1 to 1730)
  AUTHORS   Wang,C., Zhao,Z., Zhang,Y., Liang,W., Zhou,C., Lin,W., He,Y.,
            Wu,M., Meng,Z., Liao,Y., Li,M., El Akkawi,M., Zhao,J. and He,Y.
  TITLE     Identification and verification of the prognostic value of CUL7 in
            colon adenocarcinoma
  JOURNAL   Front Immunol 13, 1043512 (2022)
   PUBMED   36304472
  REMARK    GeneRIF: Identification and verification of the prognostic value of
            CUL7 in colon adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1730)
  AUTHORS   Hopf,L.V.M., Baek,K., Klugel,M., von Gronau,S., Xiong,Y. and
            Schulman,B.A.
  TITLE     Structure of CRL7FBXW8 reveals coupling with CUL1-RBX1/ROC1 for
            multi-cullin-RING E3-catalyzed ubiquitin ligation
  JOURNAL   Nat Struct Mol Biol 29 (9), 854-862 (2022)
   PUBMED   35982156
REFERENCE   5  (residues 1 to 1730)
  AUTHORS   Goos,H., Kinnunen,M., Salokas,K., Tan,Z., Liu,X., Yadav,L.,
            Zhang,Q., Wei,G.H. and Varjosalo,M.
  TITLE     Human transcription factor protein interaction networks
  JOURNAL   Nat Commun 13 (1), 766 (2022)
   PUBMED   35140242
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1730)
  AUTHORS   Arai,T., Kasper,J.S., Skaar,J.R., Ali,S.H., Takahashi,C. and
            DeCaprio,J.A.
  TITLE     Targeted disruption of p185/Cul7 gene results in abnormal vascular
            morphogenesis
  JOURNAL   Proc Natl Acad Sci U S A 100 (17), 9855-9860 (2003)
   PUBMED   12904573
REFERENCE   7  (residues 1 to 1730)
  AUTHORS   Dias,D.C., Dolios,G., Wang,R. and Pan,Z.Q.
  TITLE     CUL7: A DOC domain-containing cullin selectively binds Skp1.Fbx29
            to form an SCF-like complex
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16601-16606 (2002)
   PUBMED   12481031
REFERENCE   8  (residues 1 to 1730)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   9  (residues 1 to 1730)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   10 (residues 1 to 1730)
  AUTHORS   Akilapa,R., Irving,M. and Holder-Espinasse,M.
  TITLE     3-M Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355385.15 and AL136304.10.
            
            On Oct 18, 2019 this sequence version replaced XP_016867026.1.
            
            Summary: The protein encoded by this gene is a component of an E3
            ubiquitin-protein ligase complex. The encoded protein interacts
            with TP53, CUL9, and FBXW8 proteins. Defects in this gene are a
            cause of 3M syndrome type 1 (3M1). Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Dec 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1098940.1,
                                           SRR14038196.2602962.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1730
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..1730
                     /product="cullin-7 isoform 1"
                     /calculated_mol_wt=194288
     Region          347..389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14999.2)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14999.2)"
     Region          394..466
                     /region_name="Cul7"
                     /note="Mouse development and cellular proliferation
                     protein Cullin-7; pfam11515"
                     /db_xref="CDD:463286"
     Region          633..655
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14999.2)"
     Region          870..1000
                     /region_name="APC10-CUL7"
                     /note="APC10-like DOC1 domain of CUL7, subunit of the
                     SCF-ROC1-like E3 ubiquitin ligase complex that mediates
                     substrate ubiquitination; cd08665"
                     /db_xref="CDD:176486"
     Site            order(896,924,930,932,992)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:176486"
     Region          <1249..1538
                     /region_name="Cullin"
                     /note="Cullin family; pfam00888"
                     /db_xref="CDD:459983"
     Region          1377..1402
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14999.2)"
     Region          1593..1671
                     /region_name="Cullin_Nedd8"
                     /note="Cullin protein neddylation domain; smart00884"
                     /db_xref="CDD:214883"
     CDS             1..1730
                     /gene="CUL7"
                     /gene_synonym="3M1; CUL-7; dJ20C7.5; KIAA0076"
                     /coded_by="NM_001374872.1:239..5431"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55003.2"
                     /db_xref="GeneID:9820"
                     /db_xref="HGNC:HGNC:21024"
                     /db_xref="MIM:609577"
ORIGIN      
        1 mvgelryref rvplgpglha ypdelirqrv ghdghpeyqi rwlilrrgde gdggsgqvdc
       61 kaehillwms kdeiyanchk mlgedgqvig psqesagevg aldksvleem etdvksliqr
      121 alrqleecvg tippapllht vhvlsayasi epltgvfkdp rvldllmhml sspdyqirws
      181 agrmiqalss hdagegqcge egkageglgr lrdsqdtvag asdlirtrtq illslsqqea
      241 iekhldfdsr callalfaqa tlsehpmsfe giqlpqvpgr vlfslvkryl hvtslldqln
      301 dsaaepgaqn tsapeelsge rgqlelefsm amgtliselv qamrwdqasd rprssarspg
      361 sifqpqladv spglpaaqaq psfrrsrrfr prsefasgnt yalyvrdtlq pgmrvrmldd
      421 yeeisagdeg efrqsnngvp pvqvfwestg rtywvhwhml eilgfeedie dmveadeyqg
      481 avasrvlgra lpawrwrpmt elyavpyvlp ededteeceh ltlaewwell ffikkldgpd
      541 hqevlqilqe nldgeildde ilaelavpie laqdllltlp qrlndsalrd linchvykky
      601 gpealagnqa ypslleaqed vllldaqaqa kdsedaakve akeppsqspn tplqrlvegy
      661 gpagkilldl eqalssegtq enkvkplllq lqrqpqpfla lmqsldtpet nrtlhltvlr
      721 ilkqlvdfpe alllpwheav dacmaclrsp ntdrevlqel ifflhrltsv srdyavvlnq
      781 lgardaiska lekhlgklel aqelrdmvfk cekhahlyrk litnilggci qmvlgqiedh
      841 rrthqpinip ffdvflrylc qgssvevked kcwekvevss nphraskltd hnpktywesn
      901 gsagshyitl hmrrgilirq ltllvaseds symparvvvc ggdstsslht elnsvnvmps
      961 asrvillenl trfwpiiqir ikrcqqggid trirgleilg pkptfwpvfr eqlcrhtrlf
     1021 ymvraqawsq dmaedrrsll hlssrlngal rqeqnfadrf lpddeaaqal gktcwealvs
     1081 pvvqnitspd edgisplgwl ldqylecqea vfnpqsrgpa ffsrvrrlth llvhvepcea
     1141 pppvvatprp kgrnrshdws slatrglpss imrnltrcwr avvekqvnnf ltsswrdddf
     1201 vprycehfni lqnssselfg praafllalq ngcagallkl pflkaahvse qfarhidqqi
     1261 qgsriggaqe merlaqlqqc lqavlifsgl eiattfehyy qhymadrllg vvsswlegav
     1321 leqigpcfpn rlpqqmlqsl stskelqrqf hvyqlqqldq ellkledtek kiqvglgasg
     1381 kehksekeee agaaavvdva egeeeeeene dlyyegampe vsvlvlsrhs wpvasichtl
     1441 nprtclpsyl rgtlnrysnf ynksqshpal ergsqrrlqw twlgwaelqf gnqtlhvstv
     1501 qmwlllylnd lkavsvesll afsglsadml nqaigpltss rgpldlheqk dipggvlkir
     1561 dgskeprsrw divrlippqt ylqaegedgq nlekrrnlln clivrilkah gdeglhidql
     1621 vclvleawqk gpcpprglvs slgkgsacss tdvlscilhl lgkgtlrrhd drpqvlsyav
     1681 pvtvmephte slnpgssgpn ppltfhtlqi rsrgvpyasc tatqsfstfr
//
LOCUS       NP_001371509             692 aa            linear   PRI 21-NOV-2025
DEFINITION  protein Smaug homolog 2 isoform b [Homo sapiens].
ACCESSION   NP_001371509
VERSION     NP_001371509.1
DBSOURCE    REFSEQ: accession NM_001384580.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 692)
  AUTHORS   Wu,C., Liu,X., Li,B., Sun,G., Peng,C. and Xiang,D.
  TITLE     miR-451 suppresses the malignant characteristics of colorectal
            cancer via targeting SAMD4B
  JOURNAL   Mol Med Rep 24 (2) (2021)
   PUBMED   34109425
  REMARK    GeneRIF: miR451 suppresses the malignant characteristics of
            colorectal cancer via targeting SAMD4B.
REFERENCE   6  (residues 1 to 692)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   7  (residues 1 to 692)
  AUTHORS   Baez,M.V. and Boccaccio,G.L.
  TITLE     Mammalian Smaug is a translational repressor that forms cytoplasmic
            foci similar to stress granules
  JOURNAL   J Biol Chem 280 (52), 43131-43140 (2005)
   PUBMED   16221671
REFERENCE   8  (residues 1 to 692)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   9  (residues 1 to 692)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 692)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011445.6 and AC005239.1.
            
            Transcript Variant: This variant (15) differs in the 5' UTR
            compared to variant 2. Variants 2 and 15-19 all encode the same
            isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853566.14200.1,
                                           SRR14038194.2929189.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..692
                     /product="protein Smaug homolog 2 isoform b"
                     /note="smaug homolog B; protein Smaug homolog 2; smaug 2;
                     SAM domain-containing protein 4B; sterile alpha motif
                     domain-containing protein 4B"
                     /calculated_mol_wt=75163
     Region          158..301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XS6; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XS6; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XS6; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Region          296..358
                     /region_name="SAM_Smaug"
                     /note="SAM domain of Smaug subfamily; cd09557"
                     /db_xref="CDD:188956"
     Site            order(312,314..315,343,346..348,355,357)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:188956"
     Region          407..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            555
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            592
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            600
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            602
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Region          607..643
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     CDS             1..692
                     /gene="SAMD4B"
                     /gene_synonym="Smaug2; SMGB"
                     /coded_by="NM_001384580.1:519..2597"
                     /note="isoform b is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS77295.1"
                     /db_xref="GeneID:55095"
                     /db_xref="HGNC:HGNC:25492"
                     /db_xref="MIM:619231"
ORIGIN      
        1 mmfrdqvgil agwfkgwnec eqtvallsll krvtrtqarf lqlclehsla dcndihlles
       61 eansaaivsq wqqeskekvv slllshlpll qpgnteakse ymrllqkvla ysiesnafie
      121 esrqllsyal ihpattledr nalalwlshl eerlasgfrs rpepsyhsrq gsdewggpae
      181 lgpgeagpgw qdkpprengh vpfhpsssvp painsigsna ntglpcqihp splkrsmsli
      241 ptspqvpgew pspeelgara afttpdhapl spqssvassg seqteeqgss rntfqedgsg
      301 mkdvpswlks lrlhkyaalf sqmsyeemmt lteqhlesqn vtkgarhkia lsiqklrerq
      361 svlkslekdv leggnlrnal qelqqiiitp ikaysvlqat vaaatttpta kdgapgeppl
      421 pgaepplahp gtdkgteakd ppavenyppp papaptdgse papapvadgd ipsqftrvmg
      481 kvctqllvsr pdeenitsyl qliekclthe aftetqkkrl lswkqqvlkl lrtfprkaal
      541 emqnyrqqkg wafgsnslpi agsvgmgvar rtqrqfpmpp ralppgrmgl lspsgiggvs
      601 prhaltspsl ggqgrqnlwf anpggsnsmp sqsrssvqrt hslpvhsspq ailmfppdcp
      661 vpgpdleinp tleslclsmt ehalggpsrd lc
//
LOCUS       NP_001358096            1192 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal cell adhesion molecule isoform E precursor [Homo sapiens].
ACCESSION   NP_001358096
VERSION     NP_001358096.1
DBSOURCE    REFSEQ: accession NM_001371167.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1192)
  AUTHORS   Wang,C., Wang,Z., Fu,L., Du,J., Ji,F. and Qiu,X.
  TITLE     CircNRCAM up-regulates NRCAM to promote papillary thyroid carcinoma
            progression
  JOURNAL   J Endocrinol Invest 47 (5), 1215-1226 (2024)
   PUBMED   38485895
  REMARK    GeneRIF: CircNRCAM up-regulates NRCAM to promote papillary thyroid
            carcinoma progression.
REFERENCE   2  (residues 1 to 1192)
  AUTHORS   Zhou,L., He,L., Liu,C.H., Qiu,H., Zheng,L., Sample,K.M., Wu,Q.,
            Li,J., Xie,K., Ampuero,J., Li,Z., Lv,D., Liu,M., Romero-Gomez,M.,
            Hu,Y. and Tang,H.
  TITLE     Liver cancer stem cell dissemination and metastasis: uncovering the
            role of NRCAM in hepatocellular carcinoma
  JOURNAL   J Exp Clin Cancer Res 42 (1), 311 (2023)
   PUBMED   37993901
  REMARK    GeneRIF: Liver cancer stem cell dissemination and metastasis:
            uncovering the role of NRCAM in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1192)
  AUTHORS   Sannes,A.C., Christensen,J.O., Nielsen,M.B. and Gjerstad,J.
  TITLE     Stress-induced headache in the general working population is
            moderated by the NRCAM rs2300043 genotype
  JOURNAL   Scand J Pain 23 (2), 326-332 (2022)
   PUBMED   36181733
  REMARK    GeneRIF: Stress-induced headache in the general working population
            is moderated by the NRCAM rs2300043 genotype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1192)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 1192)
  AUTHORS   Bai,C. and Chen,D.G.
  TITLE     NRCAM acts as a prognostic biomarker and promotes the tumor
            progression in gastric cancer via EMT pathway
  JOURNAL   Tissue Cell 77, 101859 (2022)
   PUBMED   35763884
  REMARK    GeneRIF: NRCAM acts as a prognostic biomarker and promotes the
            tumor progression in gastric cancer via EMT pathway.
REFERENCE   6  (residues 1 to 1192)
  AUTHORS   Wang,B., Williams,H., Du,J.S., Terrett,J. and Kenwrick,S.
  TITLE     Alternative splicing of human NrCAM in neural and nonneural tissues
  JOURNAL   Mol Cell Neurosci 10 (5-6), 287-295 (1998)
   PUBMED   9604207
REFERENCE   7  (residues 1 to 1192)
  AUTHORS   Grumet,M.
  TITLE     Nr-CAM: a cell adhesion molecule with ligand and receptor functions
  JOURNAL   Cell Tissue Res 290 (2), 423-428 (1997)
   PUBMED   9321706
  REMARK    Review article
REFERENCE   8  (residues 1 to 1192)
  AUTHORS   Sakurai,T., Lustig,M., Nativ,M., Hemperly,J.J., Schlessinger,J.,
            Peles,E. and Grumet,M.
  TITLE     Induction of neurite outgrowth through contactin and Nr-CAM by
            extracellular regions of glial receptor tyrosine phosphatase beta
  JOURNAL   J Cell Biol 136 (4), 907-918 (1997)
   PUBMED   9049255
REFERENCE   9  (residues 1 to 1192)
  AUTHORS   Volkmer,H., Leuschner,R., Zacharias,U. and Rathjen,F.G.
  TITLE     Neurofascin induces neurites by heterophilic interactions with
            axonal NrCAM while NrCAM requires F11 on the axonal surface to
            extend neurites
  JOURNAL   J Cell Biol 135 (4), 1059-1069 (1996)
   PUBMED   8922386
REFERENCE   10 (residues 1 to 1192)
  AUTHORS   Lane,R.P., Chen,X.N., Yamakawa,K., Vielmetter,J., Korenberg,J.R.
            and Dreyer,W.J.
  TITLE     Characterization of a highly conserved human homolog to the chicken
            neural cell surface protein Bravo/Nr-CAM that maps to chromosome
            band 7q31
  JOURNAL   Genomics 35 (3), 456-465 (1996)
   PUBMED   8812479
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005058.1, AC007567.2 and
            AC005683.2.
            
            Summary: Cell adhesion molecules (CAMs) are members of the
            immunoglobulin superfamily. This gene encodes a neuronal cell
            adhesion molecule with multiple immunoglobulin-like C2-type domains
            and fibronectin type-III domains. This ankyrin-binding protein is
            involved in neuron-neuron adhesion and promotes directional
            signaling during axonal cone growth. This gene is also expressed in
            non-neural tissues and may play a general role in cell-cell
            communication via signaling from its intracellular domain to the
            actin cytoskeleton during directional cell migration. Allelic
            variants of this gene have been associated with autism and
            addiction vulnerability. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (20), as well as variants 5,
            15-19, 21, and 22, encodes isoform E.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1965299, SAMEA1966682
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1192
                     /product="neuronal cell adhesion molecule isoform E
                     precursor"
                     /note="NgCAM-related cell adhesion molecule; neuronal
                     surface protein Bravo"
                     /calculated_mol_wt=128448
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3315
     Region          46..140
                     /region_name="IgI_NrCAM"
                     /note="Immunoglobulin (Ig)-like domain of NrCAM (Ng
                     (neuronglia) CAM-related cell adhesion molecule); member
                     of the I-set of Ig superfamily (IgSF) domains; cd05874"
                     /db_xref="CDD:409458"
     Region          46..50
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409458"
     Region          55..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409458"
     Region          64..71
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409458"
     Region          77..82
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409458"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          85..87
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409458"
     Region          94..97
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409458"
     Region          102..106
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409458"
     Region          119..127
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409458"
     Region          130..140
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409458"
     Region          149..238
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          163..167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          177..181
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          200..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          215..220
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          231..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            257
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          258..339
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          269..273
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          282..286
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            295
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          304..308
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          318..323
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          331..334
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          343..431
                     /region_name="Ig4_NrCAM"
                     /note="Fourth immunoglobulin (Ig)-like domain of NrCAM
                     (NgCAM-related cell adhesion molecule); cd05868"
                     /db_xref="CDD:409454"
     Region          359..363
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409454"
     Region          372..376
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409454"
     Region          396..400
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409454"
     Region          410..415
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409454"
     Site            414
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          423..426
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409454"
     Region          440..523
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          453..457
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          466..470
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            488
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          489..493
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          503..508
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          516..519
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          527..1041
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            600
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          628..718
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(628,694,709)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            697
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            order(710..711,713..714)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            783
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            839
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            974
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            990
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1000
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          1079..1168
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     CDS             1..1192
                     /gene="NRCAM"
                     /gene_synonym="NEDNMS"
                     /coded_by="NM_001371167.1:644..4222"
                     /note="isoform E precursor is encoded by transcript
                     variant 20"
                     /db_xref="CCDS:CCDS55153.1"
                     /db_xref="GeneID:4897"
                     /db_xref="HGNC:HGNC:7994"
                     /db_xref="MIM:601581"
ORIGIN      
        1 mqlkimpkkk rlsagrvpli lflcqmisal evpldpklle dlvqpptitq qspkdyiidp
       61 reniviqcea kgkpppsfsw trngthfdid kdplvtmkpg tgtliinims egkaetyegv
      121 yqctarnerg aavsnnivvr psrsplwtke klepitlqsg qslvlpcrpp iglpppiifw
      181 mdnsfqrlpq servsqglng dlyfsnvlpe dtredyicya rfnhtqtiqq kqpisvkvis
      241 akssrerppt fltpegnasn keelrgnvls leciaeglpt piiywakedg mlpknrtvyk
      301 nfektlqiih vseadsgnyq ciaknalgai hhtisvrvka apywitapqn lvlspgedgt
      361 licrangnpk priswltngv pieiapddps rkidgdtiif snvqerssav yqcnasneyg
      421 yllanafvnv laeppriltp antlyqvian rpalldcaff gsplptiewf kgakgsalhe
      481 diyvlhengt leipvaqkds tgtytcvarn klgmaknevh leikdptwiv kqpeyavvqr
      541 gsmvsfeckv khdhtlsltv lwlkdnrelp sderftvdkd hlvvadvsdd dsgtytcvan
      601 ttldsvsasa vlsvvaptpt papvydvpnp pfdleltdql dksvqlswtp gddnnspitk
      661 fiieyedamh kpglwhhqte vsgtqttaql klspyvnysf rvmavnsigk slpseaseqy
      721 ltkasepdkn ptaveglgse pdnlvitwkp lngfesngpg lqykvswrqk dgddewtsvv
      781 vanvskyivs gtptfvpyli kvqalndmgf apepavvmgh sgedlpmvap gnvrvnvvns
      841 tlaevhwdpv plksirghlq gyriyywktq ssskrnrrhi ekkiltfqgs kthgmlpgle
      901 pfshytlnvr vvngkgegpa spdrvfntpe gvpsapsslk ivnptldslt lewdppshpn
      961 gilteytlky qpinsthelg plvdlkipan ktrwtlknln fstrykfyfy aqtsagsgsq
     1021 iteeavttvd eagilppdvg agkamasrqv diatqgwfig lmcavallil illivcfirr
     1081 nkggkypvke kedahadpei qpmkeddgtf geysdaedhk plkkgsrtps drtvkkedsd
     1141 dslvdygegv ngqfnedgsf igqysgkkek epaegnesse apspvnamns fv
//
LOCUS       NP_001374650            1008 aa            linear   PRI 21-NOV-2025
DEFINITION  activated CDC42 kinase 1 isoform 13 [Homo sapiens].
ACCESSION   NP_001374650
VERSION     NP_001374650.1
DBSOURCE    REFSEQ: accession NM_001387721.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1008)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1008)
  AUTHORS   Zheng,D., Wei,Z., Zhang,C., Liu,W., Gong,C., Wu,F. and Guo,W.
  TITLE     ZNF692 promotes osteosarcoma cell proliferation, migration, and
            invasion through TNK2-mediated activation of the MEK/ERK pathway
  JOURNAL   Biol Direct 19 (1), 28 (2024)
   PUBMED   38650011
  REMARK    GeneRIF: ZNF692 promotes osteosarcoma cell proliferation,
            migration, and invasion through TNK2-mediated activation of the
            MEK/ERK pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1008)
  AUTHORS   Hodder,S., Fox,M., Binti Ahmad Mokhtar,A.M., Mott,H.R. and Owen,D.
  TITLE     ACKnowledging the role of the Activated-Cdc42 associated kinase
            (ACK) in regulating protein stability in cancer
  JOURNAL   Small GTPases 14 (1), 14-25 (2023)
   PUBMED   37194323
  REMARK    GeneRIF: ACKnowledging the role of the Activated-Cdc42 associated
            kinase (ACK) in regulating protein stability in cancer.
            Review article
REFERENCE   4  (residues 1 to 1008)
  AUTHORS   Zhou,A., Zhang,W. and Wang,B.
  TITLE     Host factor TNK2 is required for influenza virus infection
  JOURNAL   Genes Genomics 45 (6), 771-781 (2023)
   PUBMED   37133719
  REMARK    GeneRIF: Host factor TNK2 is required for influenza virus
            infection.
REFERENCE   5  (residues 1 to 1008)
  AUTHORS   Kan,Y., Paung,Y., Seeliger,M.A. and Miller,W.T.
  TITLE     Domain Architecture of the Nonreceptor Tyrosine Kinase Ack1
  JOURNAL   Cells 12 (6), 900 (2023)
   PUBMED   36980241
  REMARK    GeneRIF: Domain Architecture of the Nonreceptor Tyrosine Kinase
            Ack1.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1008)
  AUTHORS   Kato,J., Kaziro,Y. and Satoh,T.
  TITLE     Activation of the guanine nucleotide exchange factor Dbl following
            ACK1-dependent tyrosine phosphorylation
  JOURNAL   Biochem Biophys Res Commun 268 (1), 141-147 (2000)
   PUBMED   10652228
REFERENCE   7  (residues 1 to 1008)
  AUTHORS   Eisenmann,K.M., McCarthy,J.B., Simpson,M.A., Keely,P.J., Guan,J.L.,
            Tachibana,K., Lim,L., Manser,E., Furcht,L.T. and Iida,J.
  TITLE     Melanoma chondroitin sulphate proteoglycan regulates cell spreading
            through Cdc42, Ack-1 and p130cas
  JOURNAL   Nat Cell Biol 1 (8), 507-513 (1999)
   PUBMED   10587647
REFERENCE   8  (residues 1 to 1008)
  AUTHORS   Mott,H.R., Owen,D., Nietlispach,D., Lowe,P.N., Manser,E., Lim,L.
            and Laue,E.D.
  TITLE     Structure of the small G protein Cdc42 bound to the GTPase-binding
            domain of ACK
  JOURNAL   Nature 399 (6734), 384-388 (1999)
   PUBMED   10360579
REFERENCE   9  (residues 1 to 1008)
  AUTHORS   Satoh,T., Kato,J., Nishida,K. and Kaziro,Y.
  TITLE     Tyrosine phosphorylation of ACK in response to temperature
            shift-down, hyperosmotic shock, and epidermal growth factor
            stimulation
  JOURNAL   FEBS Lett 386 (2-3), 230-234 (1996)
   PUBMED   8647288
REFERENCE   10 (residues 1 to 1008)
  AUTHORS   Manser,E., Leung,T., Salihuddin,H., Tan,L. and Lim,L.
  TITLE     A non-receptor tyrosine kinase that inhibits the GTPase activity of
            p21cdc42
  JOURNAL   Nature 363 (6427), 364-367 (1993)
   PUBMED   8497321
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124944.8.
            
            Summary: This gene encodes a tyrosine kinase that binds Cdc42Hs in
            its GTP-bound form and inhibits both the intrinsic and
            GTPase-activating protein (GAP)-stimulated GTPase activity of
            Cdc42Hs. This binding is mediated by a unique sequence of 47 amino
            acids C-terminal to an SH3 domain. The protein may be involved in a
            regulatory mechanism that sustains the GTP-bound active form of
            Cdc42Hs and which is directly linked to a tyrosine phosphorylation
            signal transduction pathway. Several alternatively spliced
            transcript variants have been identified from this gene, but the
            full-length nature of only two transcript variants has been
            determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2404315.1,
                                           SRR14038196.2096526.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1008
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..1008
                     /product="activated CDC42 kinase 1 isoform 13"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="activated p21cdc42Hs kinase; activated
                     Cdc42-associated kinase 1; tyrosine kinase non-receptor
                     protein 2"
                     /calculated_mol_wt=111139
     Region          6..67
                     /region_name="SAM_TNK-like"
                     /note="SAM domain of TNK(ACK)-like non-receptor
                     tyrosine-protein kinases; cd09539"
                     /db_xref="CDD:188938"
     Region          130..387
                     /region_name="PTKc_Ack_like"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Activated Cdc42-associated kinase; cd05040"
                     /db_xref="CDD:270636"
     Site            order(132..134,140,156,158,205..208,212,252,256..257,259,
                     270,289..293,302,336)
                     /site_type="active"
                     /db_xref="CDD:270636"
     Site            order(132..134,140,156,158,205..208,212,252,256..257,259,
                     270)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270636"
     Site            order(252,256,289..293,302,336)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270636"
     Site            order(269..279,281..295)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270636"
     Region          395..444
                     /region_name="SH3_9"
                     /note="Variant SH3 domain; pfam14604"
                     /db_xref="CDD:434066"
     Site            order(397,399,404,422,424,439,441..442)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212754"
     Region          449..514
                     /region_name="GTPase_binding"
                     /note="GTPase binding; pfam09027"
                     /db_xref="CDD:430374"
     Region          <543..849
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          774..840
                     /region_name="Inhibitor_Mig-6"
                     /note="EGFR receptor inhibitor Mig-6; pfam11555"
                     /db_xref="CDD:463294"
     Region          959..998
                     /region_name="UBA_TNK1"
                     /note="UBA domain found in non-receptor tyrosine-protein
                     kinase TNK1 and similar proteins; cd14328"
                     /db_xref="CDD:270513"
     CDS             1..1008
                     /gene="TNK2"
                     /gene_synonym="ACK; ACK-1; ACK1; p21cdc42Hs"
                     /coded_by="NM_001387721.1:111..3137"
                     /note="isoform 13 is encoded by transcript variant 24"
                     /db_xref="CCDS:CCDS93440.1"
                     /db_xref="GeneID:10188"
                     /db_xref="HGNC:HGNC:19297"
                     /db_xref="MIM:606994"
ORIGIN      
        1 mqpeegtgwl lellsevqlq qyflrlrddl nvtrlshfey vknedlekig mgrpgqrrlw
       61 eavkrrkalc krkswmskvf sgkrleaefp phhsqstfrk tspapggpag egplqsltcl
      121 igekdlrlle klgdgsfgvv rrgewdapsg ktvsvavkcl kpdvlsqpea mddfirevna
      181 mhsldhrnli rlygvvltpp mkmvtelapl gslldrlrkh qghfllgtls ryavqvaegm
      241 gyleskrfih rdlaarnlll atrdlvkigd fglmralpqn ddhyvmqehr kvpfawcape
      301 slktrtfsha sdtwmfgvtl wemftygqep wiglngsqil hkidkegerl prpedcpqdi
      361 ynvmvqcwah kpedrptfva lrdflleaqp tdmralqdfe epdklhiqmn dvitviegra
      421 enywwrgqnt rtlcvgpfpr nvvtsvagls aqdisqplqn sfihtghgds dprhcwgfpd
      481 ridelylgnp mdppdllsve lstsrppqhl ggvkkptydp vsedqdplss dfkrlglrkp
      541 glprglwlak psarvpgtka srgsgaevtl idfgeepvvp alrpcapsla qlamdacsll
      601 detppqsptr alprplhptp vvdwdarplp pppayddvaq deddfeicsi nstlvgagvp
      661 agpsqgqtny afvpeqarpp pplednlflp pqgggkppss aqtaeifqal qqecmrqlqa
      721 pagspapsps pggddkpqvp prvpipprpt rphvqlspap pgeeetsqwp gpaspprvpp
      781 replspqgsr tpsplvppgs splpprlsss pgktmpttqs fasdpkyatp qviqapgpra
      841 gpcilpivrd gkkvssthyy llperpsyle ryqrflreaq speeptplpv plllpppstp
      901 apaaptatvr pmpqaaldpk anfstnnsnp garpppprat arlpqrgcpg dgpeagrpad
      961 kiqmveqlfg lglrprgech kvlemfdwnl eqagchllgs wgpahhkr
//
LOCUS       NP_001364896             891 aa            linear   PRI 21-NOV-2025
DEFINITION  disks large homolog 2 isoform 11 [Homo sapiens].
ACCESSION   NP_001364896 XP_016872755
VERSION     NP_001364896.1
DBSOURCE    REFSEQ: accession NM_001377967.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 891)
  AUTHORS   Li,H., Zhu,J., Liu,X., Liu,L., Huang,S., Wu,A., Xu,Z., Zhang,X.,
            Li,Z., Ni,F., Liu,L. and Dong,J.
  TITLE     Glioma stem cell-derived exosomes induce the transformation of
            astrocytes via the miR-3065-5p/DLG2 signaling axis
  JOURNAL   Glia 72 (5), 857-871 (2024)
   PUBMED   38234042
  REMARK    GeneRIF: Glioma stem cell-derived exosomes induce the
            transformation of astrocytes via the miR-3065-5p/DLG2 signaling
            axis.
REFERENCE   2  (residues 1 to 891)
  AUTHORS   Chen,Y., Karaca,E., Robin,N.H., Goodloe,D., Al-Beshri,A.,
            Dean,S.J., Hurst,A.C.E., Carroll,A.J. and Mikhail,F.M.
  TITLE     DLG2 intragenic exonic deletions reinforce the link to
            neurodevelopmental disorders and suggest a potential association
            with congenital anomalies and dysmorphism
  JOURNAL   Genet Med 26 (1), 101010 (2024)
   PUBMED   37860969
  REMARK    GeneRIF: DLG2 intragenic exonic deletions reinforce the link to
            neurodevelopmental disorders and suggest a potential association
            with congenital anomalies and dysmorphism.
REFERENCE   3  (residues 1 to 891)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 891)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 891)
  AUTHORS   Stathakis,D.G., Lee,D. and Bryant,P.J.
  TITLE     Fine-scale physical map of the 11q21 region surrounding the human
            DLG2 locus, the gene encoding Chapsyn-110
  JOURNAL   Genomics 54 (1), 186-188 (1998)
   PUBMED   9806853
REFERENCE   6  (residues 1 to 891)
  AUTHORS   Irie,M., Hata,Y., Takeuchi,M., Ichtchenko,K., Toyoda,A., Hirao,K.,
            Takai,Y., Rosahl,T.W. and Sudhof,T.C.
  TITLE     Binding of neuroligins to PSD-95
  JOURNAL   Science 277 (5331), 1511-1515 (1997)
   PUBMED   9278515
REFERENCE   7  (residues 1 to 891)
  AUTHORS   Hsueh,Y.P., Kim,E. and Sheng,M.
  TITLE     Disulfide-linked head-to-head multimerization in the mechanism of
            ion channel clustering by PSD-95
  JOURNAL   Neuron 18 (5), 803-814 (1997)
   PUBMED   9182804
REFERENCE   8  (residues 1 to 891)
  AUTHORS   Kim,E., Cho,K.O., Rothschild,A. and Sheng,M.
  TITLE     Heteromultimerization and NMDA receptor-clustering activity of
            Chapsyn-110, a member of the PSD-95 family of proteins
  JOURNAL   Neuron 17 (1), 103-113 (1996)
   PUBMED   8755482
REFERENCE   9  (residues 1 to 891)
  AUTHORS   Brenman,J.E., Chao,D.S., Gee,S.H., McGee,A.W., Craven,S.E.,
            Santillano,D.R., Wu,Z., Huang,F., Xia,H., Peters,M.F.,
            Froehner,S.C. and Bredt,D.S.
  TITLE     Interaction of nitric oxide synthase with the postsynaptic density
            protein PSD-95 and alpha1-syntrophin mediated by PDZ domains
  JOURNAL   Cell 84 (5), 757-767 (1996)
   PUBMED   8625413
REFERENCE   10 (residues 1 to 891)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003305.2, AP002797.3,
            AC023118.4, AP002751.3, AP002370.5, AP000773.4 and AP003026.2.
            
            On Jan 23, 2020 this sequence version replaced XP_016872755.1.
            
            Summary: This gene encodes a member of the membrane-associated
            guanylate kinase (MAGUK) family. The encoded protein forms a
            heterodimer with a related family member that may interact at
            postsynaptic sites to form a multimeric scaffold for the clustering
            of receptors, ion channels, and associated signaling proteins.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. Additional transcript variants have been
            described, but their full-length nature is not known. [provided by
            RefSeq, Dec 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.56613.1,
                                           SRR1803615.21053.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..891
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.1"
     Protein         1..891
                     /product="disks large homolog 2 isoform 11"
                     /note="channel-associated protein of synapses, 110kDa;
                     postsynaptic density protein PSD-93; channel-associated
                     protein of synapse-110; discs, large homolog 2,
                     chapsyn-110; protein phosphatase 1, regulatory subunit 58;
                     disks large homolog 2"
                     /calculated_mol_wt=98298
     Region          43..136
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          135..223
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(146..152,169,172,202,206,209..210)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          232..316
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(241..247,264,267,297,301,304..305)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          317..384
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          457..547
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(469..475,486,489,519,523,526..527)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          573..646
                     /region_name="SH3_DLG2"
                     /note="Src Homology 3 domain of Disks Large homolog 2;
                     cd12032"
                     /db_xref="CDD:212965"
     Site            order(581,603..604)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212965"
     Site            order(584,586,589,598,616..617,636,638..639)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212965"
     Region          700..878
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..891
                     /gene="DLG2"
                     /gene_synonym="chapsyn-110; PPP1R58; PSD-93; PSD93"
                     /coded_by="NM_001377967.1:193..2868"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS91558.1"
                     /db_xref="GeneID:1740"
                     /db_xref="HGNC:HGNC:2901"
                     /db_xref="MIM:603583"
ORIGIN      
        1 mnayltkqhs csrgsdgmda vrsaptlird ahcacgwqrn cqglgyssqt mpssgpggpa
       61 snrtggssfn rtlwdsvrks phktstkgkg tcgehctcph gwfspaqasp apiivntdtl
      121 dtipyvngte ieyefeeitl ergnsglgfs iaggtdnphi gddpgifitk iipggaaaed
      181 grlrvndcil rvnevdvsev shskavealk eagsivrlyv rrrrpiletv veiklfkgpk
      241 glgfsiaggv gnqhipgdns iyvtkiidgg aaqkdgrlqv gdrllmvnny sleevtheea
      301 vailkntsev vylkvgkptt iymtdpygpp dithsysppm enhllsgnng tleyktslpp
      361 ispgryspip khmlvdddyt rppepvystv nklcdkpasp rhyspvecdk sfllsapysh
      421 yhlgllpdse mtshsqhsta trqpsmtlqr avslegeprk vvlhkgstgl gfnivggedg
      481 egifvsfila ggpadlsgel qrgdqilsvn gidlrgashe qaaaalkgag qtvtiiaqyq
      541 pedyarfeak ihdlreqmmn hsmssgsgsl rtnqkrslyv ramfdydksk dsglpsqgls
      601 fkygdilhvi nasddewwqa rrvmlegdse emgvipskrr verkerarlk tvkfnakpgv
      661 idskgdipgl gddgygtktl rgqedlilsy epvtrqeiny trpviilgpm kdrinddlis
      721 efpdkfgscv phttrpkrdy evdgrdyhfv isreqmekdi qehkfieagq yndnlygtsv
      781 qsvrfvaerg khcildvsgn aikrlqvaql ypiaifikpr sleplmemnk rlteeqakkt
      841 ydraikleqe fgeyftaivq gdtlediynq cklvieeqsg pfiwipskek l
//
LOCUS       NP_001335841             373 aa            linear   PRI 21-NOV-2025
DEFINITION  cytoplasmic dynein 2 light intermediate chain 1 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001335841 XP_005264422
VERSION     NP_001335841.1
DBSOURCE    REFSEQ: accession NM_001348912.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Qiu,H., Tsurumi,Y., Katoh,Y. and Nakayama,K.
  TITLE     Combinations of deletion and missense variations of the dynein-2
            DYNC2LI1 subunit found in skeletal ciliopathies cause ciliary
            defects
  JOURNAL   Sci Rep 12 (1), 31 (2022)
   PUBMED   34997029
  REMARK    GeneRIF: Combinations of deletion and missense variations of the
            dynein-2 DYNC2LI1 subunit found in skeletal ciliopathies cause
            ciliary defects.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Zhang,X., You,Y., Xie,X., Xu,H., Zhou,H., Lei,Y., Sun,P., Meng,Y.,
            Wang,L. and Lu,Y.
  TITLE     Whole-exome sequencing identified two novel mutations of DYNC2LI1
            in fetal skeletal ciliopathy
  JOURNAL   Mol Genet Genomic Med 8 (12), e1524 (2020)
   PUBMED   33030252
  REMARK    GeneRIF: Whole-exome sequencing identified two novel mutations of
            DYNC2LI1 in fetal skeletal ciliopathy.
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Vuolo,L., Stevenson,N.L., Mukhopadhyay,A.G., Roberts,A.J. and
            Stephens,D.J.
  TITLE     Cytoplasmic dynein-2 at a glance
  JOURNAL   J Cell Sci 133 (6) (2020)
   PUBMED   32229580
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Perrone,C.A., Tritschler,D., Taulman,P., Bower,R., Yoder,B.K. and
            Porter,M.E.
  TITLE     A novel dynein light intermediate chain colocalizes with the
            retrograde motor for intraflagellar transport at sites of axoneme
            assembly in chlamydomonas and Mammalian cells
  JOURNAL   Mol Biol Cell 14 (5), 2041-2056 (2003)
   PUBMED   12802074
REFERENCE   7  (residues 1 to 373)
  AUTHORS   Mikami,A., Tynan,S.H., Hama,T., Luby-Phelps,K., Saito,T.,
            Crandall,J.E., Besharse,J.C. and Vallee,R.B.
  TITLE     Molecular structure of cytoplasmic dynein 2 and its distribution in
            neuronal and ciliated cells
  JOURNAL   J Cell Sci 115 (Pt 24), 4801-4808 (2002)
   PUBMED   12432068
REFERENCE   8  (residues 1 to 373)
  AUTHORS   Short,B., Preisinger,C., Schaletzky,J., Kopajtich,R. and Barr,F.A.
  TITLE     The Rab6 GTPase regulates recruitment of the dynactin complex to
            Golgi membranes
  JOURNAL   Curr Biol 12 (20), 1792-1795 (2002)
   PUBMED   12401177
REFERENCE   9  (residues 1 to 373)
  AUTHORS   Grissom,P.M., Vaisberg,E.A. and McIntosh,J.R.
  TITLE     Identification of a novel light intermediate chain (D2LIC) for
            mammalian cytoplasmic dynein 2
  JOURNAL   Mol Biol Cell 13 (3), 817-829 (2002)
   PUBMED   11907264
REFERENCE   10 (residues 1 to 373)
  AUTHORS   Da Silva,J.D., Tkachenko,N. and Soares,A.R.
  TITLE     Ellis-van Creveld Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37903214
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011242.8 and AC108476.5.
            
            On Feb 19, 2017 this sequence version replaced XP_005264422.1.
            
            Summary: This gene encodes a protein that is a component of the
            dynein-2 microtubule motor protein complex that plays a role in the
            retrograde transport of cargo in primary cilia via the
            intraflagellar transport system. This gene is ubiquitously
            expressed and its protein, which localizes to the axoneme and Golgi
            apparatus, interacts directly with the cytoplasmic dynein 2 heavy
            chain 1 protein to form part of the multi-protein dynein-2 complex.
            Mutations in this gene produce defects in the dynein-2 complex
            which result in several types of ciliopathy including short-rib
            thoracic dysplasia 15 with polydactyly (SRTD15). Alternative
            splicing results in multiple transcript variants encoding distinct
            isoforms. [provided by RefSeq, Feb 2017].
            
            Transcript Variant: This variant (5) has multiple differences at
            its 3' end, compared to variant 1. This results in a longer protein
            (isoform 5) with a distinct C-terminus, compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3642749.1,
                                           SRR1803614.209359.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p21"
     Protein         1..373
                     /product="cytoplasmic dynein 2 light intermediate chain 1
                     isoform 5"
                     /calculated_mol_wt=41859
     Region          2..>268
                     /region_name="DLIC"
                     /note="Dynein light intermediate chain (DLIC); pfam05783"
                     /db_xref="CDD:368612"
     CDS             1..373
                     /gene="DYNC2LI1"
                     /gene_synonym="CGI-60; D2LIC; LIC3"
                     /coded_by="NM_001348912.2:101..1222"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:51626"
                     /db_xref="HGNC:HGNC:24595"
                     /db_xref="MIM:617083"
ORIGIN      
        1 mpsetlweia kaevekrgin gsegdgaeia ekfvffigsk nggkttiilr cldrdeppkp
       61 tlaleytygr rakghntpkd iahfwelggg tslldlisip itgdtlrtfs lvlvldlskp
      121 ndlwptmenl lqatkshvdk vimklgktna kavsemrqki wnnmpkdhpd helidpfpvp
      181 lviigskydv fqdfesekrk vicktlrfva hyygaslmft sksealllki rgvinqlafg
      241 idksksicvd qnkplfitag ldsfgqigsp pvpendigkl hahspmelwk kvyeklfppk
      301 sintlkdikd pardpqyaen evdemriqkd lahlrrypik kqdktscvad nqdyfqggia
      361 fkkpfqsvdv ctc
//
LOCUS       NP_001119587             261 aa            linear   PRI 21-NOV-2025
DEFINITION  cellular tumor antigen p53 isoform d [Homo sapiens].
ACCESSION   NP_001119587
VERSION     NP_001119587.1
DBSOURCE    REFSEQ: accession NM_001126115.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Mirgayazova,R., Khadiullina,R., Chasov,V., Mingaleeva,R.,
            Miftakhova,R., Rizvanov,A. and Bulatov,E.
  TITLE     Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an Option?
  JOURNAL   Genes (Basel) 11 (6), 704 (2020)
   PUBMED   32630614
  REMARK    GeneRIF: Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an
            Option?
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Flynt,E., Bisht,K., Sridharan,V., Ortiz,M., Towfic,F. and
            Thakurta,A.
  TITLE     Prognosis, Biology, and Targeting of TP53 Dysregulation in Multiple
            Myeloma
  JOURNAL   Cells 9 (2), 287 (2020)
   PUBMED   31991614
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Barnoud,T., Parris,J.L.D. and Murphy,M.E.
  TITLE     Common genetic variants in the TP53 pathway and their impact on
            cancer
  JOURNAL   J Mol Cell Biol 11 (7), 578-585 (2019)
   PUBMED   31152665
  REMARK    GeneRIF: Common genetic variants in the TP53 pathway and their
            impact on cancer.
            Review article
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Hu,W., Chen,S., Thorne,R.F. and Wu,M.
  TITLE     TP53, TP53 Target Genes (DRAM, TIGAR), and Autophagy
  JOURNAL   Adv Exp Med Biol 1206, 127-149 (2019)
   PUBMED   31776983
  REMARK    Review article
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Baugh,E.H., Ke,H., Levine,A.J., Bonneau,R.A. and Chan,C.S.
  TITLE     Why are there hotspot mutations in the TP53 gene in human cancers?
  JOURNAL   Cell Death Differ 25 (1), 154-160 (2018)
   PUBMED   29099487
  REMARK    GeneRIF: TP53 missense mutant alleles that occur in human cancers
            are discussed in the context of high resolution models of these p53
            mutant protein structures to determine the structural features of
            mutations (review).
            Review article
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Aubrey,B.J., Strasser,A. and Kelly,G.L.
  TITLE     Tumor-Suppressor Functions of the TP53 Pathway
  JOURNAL   Cold Spring Harb Perspect Med 6 (5), a026062 (2016)
   PUBMED   27141080
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Soussi,T. and Wiman,K.G.
  TITLE     TP53: an oncogene in disguise
  JOURNAL   Cell Death Differ 22 (8), 1239-1249 (2015)
   PUBMED   26024390
  REMARK    Review article
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Soussi,T.
  TITLE     The TP53 gene network in a postgenomic era
  JOURNAL   Hum Mutat 35 (6), 641-642 (2014)
   PUBMED   24753184
  REMARK    GeneRIF: Recommendations and guidelines for reporting and
            annotating TP53 variants are also provided, to help researchers
            generate standardized data that are easy to understand, analyze,
            and exchange across various cancer variant databases
            Review article
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Anczukow,O., Ware,M.D., Buisson,M., Zetoune,A.B.,
            Stoppa-Lyonnet,D., Sinilnikova,O.M. and Mazoyer,S.
  TITLE     Does the nonsense-mediated mRNA decay mechanism prevent the
            synthesis of truncated BRCA1, CHK2, and p53 proteins?
  JOURNAL   Hum Mutat 29 (1), 65-73 (2008)
   PUBMED   17694537
  REMARK    GeneRIF: the p53 protein encoded by the 770delT allele is as
            abundant as the wild-type protein, as removal of the C-terminal p53
            domain leads to a stabilized mutant protein, whose abundance is
            markedly increased when NMD is inhibited.
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Bourdon,J.C.
  TITLE     p53 Family isoforms
  JOURNAL   Curr Pharm Biotechnol 8 (6), 332-336 (2007)
   PUBMED   18289041
  REMARK    Review article
REFERENCE   11 (residues 1 to 261)
  AUTHORS   Candeias,M.M., Powell,D.J., Roubalova,E., Apcher,S., Bourougaa,K.,
            Vojtesek,B., Bruzzoni-Giovanelli,H. and Fahraeus,R.
  TITLE     Expression of p53 and p53/47 are controlled by alternative
            mechanisms of messenger RNA translation initiation
  JOURNAL   Oncogene 25 (52), 6936-6947 (2006)
   PUBMED   16983332
  REMARK    GeneRIF: harbouring alternative translation initiation sites, the
            p53 mRNA gives rise to different levels of the p53 isoforms which
            help to orchestrate the cell biological outcome of p53 activation
REFERENCE   12 (residues 1 to 261)
  AUTHORS   Murray-Zmijewski,F., Lane,D.P. and Bourdon,J.C.
  TITLE     p53/p63/p73 isoforms: an orchestra of isoforms to harmonise cell
            differentiation and response to stress
  JOURNAL   Cell Death Differ 13 (6), 962-972 (2006)
   PUBMED   16601753
  REMARK    Review article
REFERENCE   13 (residues 1 to 261)
  AUTHORS   Bourdon,J.C., Fernandes,K., Murray-Zmijewski,F., Liu,G., Diot,A.,
            Xirodimas,D.P., Saville,M.K. and Lane,D.P.
  TITLE     p53 isoforms can regulate p53 transcriptional activity
  JOURNAL   Genes Dev 19 (18), 2122-2137 (2005)
   PUBMED   16131611
  REMARK    GeneRIF: p53 isoforms can regulate p53 transcriptional activity.
REFERENCE   14 (residues 1 to 261)
  AUTHORS   Ghosh,A., Stewart,D. and Matlashewski,G.
  TITLE     Regulation of human p53 activity and cell localization by
            alternative splicing
  JOURNAL   Mol Cell Biol 24 (18), 7987-7997 (2004)
   PUBMED   15340061
  REMARK    GeneRIF: mechanism of p53 regulation originating through
            alternative splicing of the human p53 gene resulting in the
            expression of a novel p53 mRNA
REFERENCE   15 (residues 1 to 261)
  AUTHORS   Flaman,J.M., Waridel,F., Estreicher,A., Vannier,A., Limacher,J.M.,
            Gilbert,D., Iggo,R. and Frebourg,T.
  TITLE     The human tumour suppressor gene p53 is alternatively spliced in
            normal cells
  JOURNAL   Oncogene 12 (4), 813-818 (1996)
   PUBMED   8632903
REFERENCE   16 (residues 1 to 261)
  AUTHORS   Schneider,K., Zelley,K., Nichols,K.E., Schwartz Levine,A. and
            Garber,J.
  TITLE     Li-Fraumeni Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301488
REFERENCE   17 (residues 1 to 261)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   18 (residues 1 to 261)
  AUTHORS   Lamb,P. and Crawford,L.
  TITLE     Characterization of the human p53 gene
  JOURNAL   Mol Cell Biol 6 (5), 1379-1385 (1986)
   PUBMED   2946935
REFERENCE   19 (residues 1 to 261)
  AUTHORS   Isobe,M., Emanuel,B.S., Givol,D., Oren,M. and Croce,C.M.
  TITLE     Localization of gene for human p53 tumour antigen to band 17p13
  JOURNAL   Nature 320 (6057), 84-85 (1986)
   PUBMED   3456488
REFERENCE   20 (residues 1 to 261)
  AUTHORS   Benchimol,S., Lamb,P., Crawford,L.V., Sheer,D., Shows,T.B.,
            Bruns,G.A. and Peacock,J.
  TITLE     Transformation associated p53 protein is encoded by a gene on human
            chromosome 17
  JOURNAL   Somat Cell Mol Genet 11 (5), 505-510 (1985)
   PUBMED   2994241
REFERENCE   21 (residues 1 to 261)
  AUTHORS   Harlow,E., Williamson,N.M., Ralston,R., Helfman,D.M. and Adams,T.E.
  TITLE     Molecular cloning and in vitro expression of a cDNA clone for human
            cellular tumor antigen p53
  JOURNAL   Mol Cell Biol 5 (7), 1601-1610 (1985)
   PUBMED   3894933
REFERENCE   22 (residues 1 to 261)
  AUTHORS   Zakut-Houri,R., Bienz-Tadmor,B., Givol,D. and Oren,M.
  TITLE     Human p53 cellular tumor antigen: cDNA sequence and expression in
            COS cells
  JOURNAL   EMBO J 4 (5), 1251-1255 (1985)
   PUBMED   4006916
REFERENCE   23 (residues 1 to 261)
  AUTHORS   Matlashewski,G., Lamb,P., Pim,D., Peacock,J., Crawford,L. and
            Benchimol,S.
  TITLE     Isolation and characterization of a human p53 cDNA clone:
            expression of the human p53 gene
  JOURNAL   EMBO J 3 (13), 3257-3262 (1984)
   PUBMED   6396087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087388.9 and AC007421.13.
            
            Summary: This gene encodes a tumor suppressor protein containing
            transcriptional activation, DNA binding, and oligomerization
            domains. The encoded protein responds to diverse cellular stresses
            to regulate expression of target genes, thereby inducing cell cycle
            arrest, apoptosis, senescence, DNA repair, or changes in
            metabolism. Mutations in this gene are associated with a variety of
            human cancers, including hereditary cancers such as Li-Fraumeni
            syndrome. Alternative splicing of this gene and the use of
            alternate promoters result in multiple transcript variants and
            isoforms. Additional isoforms have also been shown to result from
            the use of alternate translation initiation codons from identical
            transcript variants (PMIDs: 12032546, 20937277). [provided by
            RefSeq, Dec 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ186650.1, SRR14038193.783535.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..261
                     /product="cellular tumor antigen p53 isoform d"
                     /note="tumor protein 53; mutant tumor protein 53; cellular
                     tumor antigen p53; phosphoprotein p53;
                     transformation-related protein 53; antigen NY-CO-13; tumor
                     supressor p53"
                     /calculated_mol_wt=29422
     Region          1..156
                     /region_name="P53"
                     /note="P53 DNA-binding domain; cd08367"
                     /db_xref="CDD:176262"
     Region          28
                     /region_name="alternative start codon"
                     /note="delta133p53alpha"
     Site            order(44,47,106,110)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:176262"
     Site            order(45..47,49)
                     /site_type="other"
                     /note="dimerization site [polypeptide binding]"
                     /db_xref="CDD:176262"
     Site            order(107,109,116,141,143..145,148)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176262"
     Region          187..226
                     /region_name="P53_tetramer"
                     /note="P53 tetramerization motif; pfam07710"
                     /db_xref="CDD:462238"
     CDS             1..261
                     /gene="TP53"
                     /gene_synonym="BCC7; BMFS5; LFS1; P53; TRP53"
                     /coded_by="NM_001126115.2:30..815"
                     /note="isoform d is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS73966.1"
                     /db_xref="GeneID:7157"
                     /db_xref="HGNC:HGNC:11998"
                     /db_xref="MIM:191170"
ORIGIN      
        1 mfcqlaktcp vqlwvdstpp pgtrvramai ykqsqhmtev vrrcphherc sdsdglappq
       61 hlirvegnlr veylddrntf rhsvvvpyep pevgsdctti hynymcnssc mggmnrrpil
      121 tiitledssg nllgrnsfev rvcacpgrdr rteeenlrkk gephhelppg stkralpnnt
      181 ssspqpkkkp ldgeyftlqi rgrerfemfr elnealelkd aqagkepggs rahsshlksk
      241 kgqstsrhkk lmfktegpds d
//
LOCUS       NP_000259                595 aa            linear   PRI 21-NOV-2025
DEFINITION  merlin isoform 1 [Homo sapiens].
ACCESSION   NP_000259
VERSION     NP_000259.1
DBSOURCE    REFSEQ: accession NM_000268.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 595)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 595)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 595)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 595)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 595)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 595)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 595)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 595)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 595)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 595)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF369657.1 and AC004882.3.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF369657.1, SRR18074967.1749160.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000338641.10/ ENSP00000344666.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..595
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..595
                     /product="merlin isoform 1"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=69559
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35240.1)"
     Region          23..222
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          216..312
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(258..259,261..267,276,297,300..301,304)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(258,261..268,276,297,300..301,304)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(294,298)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            297..312
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          307..>367
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          346..465
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          518..595
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PAK.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (P35240.1)"
     CDS             1..595
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_000268.4:367..2154"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13861.1"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 magaiasrms fsslkrkqpk tftvrivtmd aemefncemk wkgkdlfdlv crtlglretw
       61 ffglqytikd tvawlkmdkk vldhdvskee pvtfhflakf ypenaeeelv qeitqhlffl
      121 qvkkqildek iycppeasvl lasyavqaky gdydpsvhkr gflaqeellp krvinlyqmt
      181 pemweerita wyaehrgrar deaemeylki aqdlemygvn yfairnkkgt elllgvdalg
      241 lhiydpenrl tpkisfpwne irnisysdke ftikpldkki dvfkfnsskl rvnklilqlc
      301 ignhdlfmrr rkadslevqq mkaqareeka rkqmerqrla rekqmreeae rtrdelerrl
      361 lqmkeeatma nealmrseet adllaekaqi teeeakllaq kaaeaeqemq rikatairte
      421 eekrlmeqkv leaevlalkm aeeserrake adqlkqdlqe areaerrakq klleiatkpt
      481 yppmnpipap lppdipsfnl igdslsfdfk dtdmkrlsme iekekveyme kskhlqeqln
      541 elkteiealk lkeretaldi lhnensdrgg sskhntikkl tlqsaksrva ffeel
//
LOCUS       NP_001334613             276 aa            linear   PRI 21-NOV-2025
DEFINITION  uroplakin-3b isoform d precursor [Homo sapiens].
ACCESSION   NP_001334613
VERSION     NP_001334613.1
DBSOURCE    REFSEQ: accession NM_001347684.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Moayyeri,A., Hsu,Y.H., Karasik,D., Estrada,K., Xiao,S.M.,
            Nielson,C., Srikanth,P., Giroux,S., Wilson,S.G., Zheng,H.F.,
            Smith,A.V., Pye,S.R., Leo,P.J., Teumer,A., Hwang,J.Y., Ohlsson,C.,
            McGuigan,F., Minster,R.L., Hayward,C., Olmos,J.M.,
            Lyytikainen,L.P., Lewis,J.R., Swart,K.M., Masi,L., Oldmeadow,C.,
            Holliday,E.G., Cheng,S., van Schoor,N.M., Harvey,N.C., Kruk,M., del
            Greco,M. F, Igl,W., Trummer,O., Grigoriou,E., Luben,R., Liu,C.T.,
            Zhou,Y., Oei,L., Medina-Gomez,C., Zmuda,J., Tranah,G., Brown,S.J.,
            Williams,F.M., Soranzo,N., Jakobsdottir,J., Siggeirsdottir,K.,
            Holliday,K.L., Hannemann,A., Go,M.J., Garcia,M., Polasek,O.,
            Laaksonen,M., Zhu,K., Enneman,A.W., McEvoy,M., Peel,R., Sham,P.C.,
            Jaworski,M., Johansson,A., Hicks,A.A., Pludowski,P., Scott,R.,
            Dhonukshe-Rutten,R.A., van der Velde,N., Kahonen,M., Viikari,J.S.,
            Sievanen,H., Raitakari,O.T., Gonzalez-Macias,J., Hernandez,J.L.,
            Mellstrom,D., Ljunggren,O., Cho,Y.S., Volker,U., Nauck,M.,
            Homuth,G., Volzke,H., Haring,R., Brown,M.A., McCloskey,E.,
            Nicholson,G.C., Eastell,R., Eisman,J.A., Jones,G., Reid,I.R.,
            Dennison,E.M., Wark,J., Boonen,S., Vanderschueren,D., Wu,F.C.,
            Aspelund,T., Richards,J.B., Bauer,D., Hofman,A., Khaw,K.T.,
            Dedoussis,G., Obermayer-Pietsch,B., Gyllensten,U.,
            Pramstaller,P.P., Lorenc,R.S., Cooper,C., Kung,A.W., Lips,P.,
            Alen,M., Attia,J., Brandi,M.L., de Groot,L.C., Lehtimaki,T.,
            Riancho,J.A., Campbell,H., Liu,Y., Harris,T.B., Akesson,K.,
            Karlsson,M., Lee,J.Y., Wallaschofski,H., Duncan,E.L., O'Neill,T.W.,
            Gudnason,V., Spector,T.D., Rousseau,F., Orwoll,E., Cummings,S.R.,
            Wareham,N.J., Rivadeneira,F., Uitterlinden,A.G., Prince,R.L.,
            Kiel,D.P., Reeve,J. and Kaptoge,S.K.
  TITLE     Genetic determinants of heel bone properties: genome-wide
            association meta-analysis and replication in the GEFOS/GENOMOS
            consortium
  JOURNAL   Hum Mol Genet 23 (11), 3054-3068 (2014)
   PUBMED   24430505
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Kanamori-Katayama,M., Kaiho,A., Ishizu,Y., Okamura-Oho,Y., Hino,O.,
            Abe,M., Kishimoto,T., Sekihara,H., Nakamura,Y., Suzuki,H.,
            Forrest,A.R. and Hayashizaki,Y.
  TITLE     LRRN4 and UPK3B are markers of primary mesothelial cells
  JOURNAL   PLoS One 6 (10), e25391 (2011)
   PUBMED   21984916
  REMARK    GeneRIF: LRRN4 was only detected in primary mesothelial cells, but
            MSLN and UPK3B were also detected in other cell types.
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Foot,N.J., Dalton,H.E., Shearwin-Whyatt,L.M., Dorstyn,L., Tan,S.S.,
            Yang,B. and Kumar,S.
  TITLE     Regulation of the divalent metal ion transporter DMT1 and iron
            homeostasis by a ubiquitin-dependent mechanism involving Ndfips and
            WWP2
  JOURNAL   Blood 112 (10), 4268-4275 (2008)
   PUBMED   18776082
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Garcia-Espana,A., Chung,P.J., Zhao,X., Lee,A., Pellicer,A., Yu,J.,
            Sun,T.T. and Desalle,R.
  TITLE     Origin of the tetraspanin uroplakins and their co-evolution with
            associated proteins: implications for uroplakin structure and
            function
  JOURNAL   Mol Phylogenet Evol 41 (2), 355-367 (2006)
   PUBMED   16814572
REFERENCE   7  (residues 1 to 276)
  AUTHORS   Deng,F.M., Liang,F.X., Tu,L., Resing,K.A., Hu,P., Supino,M.,
            Hu,C.C., Zhou,G., Ding,M., Kreibich,G. and Sun,T.T.
  TITLE     Uroplakin IIIb, a urothelial differentiation marker, dimerizes with
            uroplakin Ib as an early step of urothelial plaque assembly
  JOURNAL   J Cell Biol 159 (4), 685-694 (2002)
   PUBMED   12446744
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007078.4 and AC004980.5.
            
            Summary: UPK3B is a minor component of the apical plaques of
            mammalian urothelium that binds and dimerizes with uroplakin-1b
            (UPK1B; MIM 602380), one of the major conserved urothelium membrane
            proteins. The other major conserved integral membrane proteins of
            urothelial plaques are UPK1A (MIM 611557), UPK2 (MIM 611558), and
            UPK3A (MIM 611559) (Deng et al., 2002 [PubMed 12446744]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (4) is alternatively spliced at
            the 5' end, differs in the 3' UTR and contains an additional
            internal exon, which causes a frame-shift compared to variant 1.
            The resulting isoform (d) lacks a protein segment in the N-terminal
            region and has a distinct C-terminus compared to isoform a. This
            variant is annotated on the GRCh38 primary human reference genome
            assembly.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.139217.1, BM008901.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142363, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334348.8/ ENSP00000334938.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..276
                     /product="uroplakin-3b isoform d precursor"
                     /note="uroplakin-3b; uroplakin IIIb"
                     /calculated_mol_wt=26850
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2960
     Region          29..202
                     /region_name="UP_IIIb"
                     /note="Uroplakin IIIb; cd09969"
                     /db_xref="CDD:197378"
     CDS             1..276
                     /gene="UPK3B"
                     /gene_synonym="P35; UP3B; UPIIIB"
                     /coded_by="NM_001347684.2:102..932"
                     /note="isoform d precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS87512.1"
                     /db_xref="GeneID:105375355"
                     /db_xref="HGNC:HGNC:21444"
                     /db_xref="MIM:611887"
ORIGIN      
        1 mglpwgqphl glqmlllaln clrpslslel vpytpqitaw dlegkvtatt fsleqprcvf
       61 dglasasdtv wlvvafsnas rgfqnpetla dipaspqllt dghymtlpls pdqlpcgdpm
      121 agsggapvlr vghdhgchqq pfcnaplpgp gpyrvkfllm dtrgspraet kwsdpitlhq
      181 gktpgsidtw pgrrsgsmiv itsilsslag llllaflaas tmrfsslwwp eeapeqlrig
      241 sfmgkrymth hippreaatl pvgckpgldp lpslsp
//
LOCUS       NP_877392                332 aa            linear   PRI 21-NOV-2025
DEFINITION  large neutral amino acids transporter small subunit 2 isoform b
            [Homo sapiens].
ACCESSION   NP_877392
VERSION     NP_877392.1
DBSOURCE    REFSEQ: accession NM_182728.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Crocco,P., Dato,S., La Grotta,R., Passarino,G. and Rose,G.
  TITLE     Evidence for a relationship between genetic polymorphisms of the
            L-DOPA transporter LAT2/4F2hc and risk of hypertension in the
            context of chronic kidney disease
  JOURNAL   BMC Med Genomics 17 (1), 163 (2024)
   PUBMED   38890684
  REMARK    GeneRIF: Evidence for a relationship between genetic polymorphisms
            of the L-DOPA transporter LAT2/4F2hc and risk of hypertension in
            the context of chronic kidney disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Wang,F.M., Xu,L.Q., Zhang,Z.C., Guo,Q., Du,Z.P., Lei,Y., Han,X.,
            Wu,C.Y., Zhao,F. and Chen,J.L.
  TITLE     SLC7A8 overexpression inhibits the growth and metastasis of lung
            adenocarcinoma and is correlated with a dismal prognosis
  JOURNAL   Aging (Albany NY) 16 (2), 1605-1619 (2024)
   PUBMED   38244585
  REMARK    GeneRIF: SLC7A8 overexpression inhibits the growth and metastasis
            of lung adenocarcinoma and is correlated with a dismal prognosis.
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Meng,F., Wang,L., Gao,G., Chen,J., Wang,X., Wu,G. and Miu,Y.
  TITLE     Identification and verification of microRNA signature and key genes
            in the development of osteosarcoma with lung metastasis
  JOURNAL   Medicine (Baltimore) 101 (49), e32258 (2022)
   PUBMED   36626488
  REMARK    GeneRIF: Identification and verification of microRNA signature and
            key genes in the development of osteosarcoma with lung metastasis.
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Min,Q., Wang,Y., Wu,Q., Li,X., Teng,H., Fan,J., Cao,Y., Fan,P. and
            Zhan,Q.
  TITLE     Genomic and epigenomic evolution of acquired resistance to
            combination therapy in esophageal squamous cell carcinoma
  JOURNAL   JCI Insight 6 (17), e150203 (2021)
   PUBMED   34494553
  REMARK    GeneRIF: Genomic and epigenomic evolution of acquired resistance to
            combination therapy in esophageal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Yan,R., Li,Y., Muller,J., Zhang,Y., Singer,S., Xia,L., Zhong,X.,
            Gertsch,J., Altmann,K.H. and Zhou,Q.
  TITLE     Mechanism of substrate transport and inhibition of the human
            LAT1-4F2hc amino acid transporter
  JOURNAL   Cell Discov 7 (1), 16 (2021)
   PUBMED   33758168
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Broer,A., Friedrich,B., Wagner,C.A., Fillon,S., Ganapathy,V.,
            Lang,F. and Broer,S.
  TITLE     Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2
            requires different domains
  JOURNAL   Biochem J 355 (Pt 3), 725-731 (2001)
   PUBMED   11311135
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Rossier,G., Meier,C., Bauch,C., Summa,V., Sordat,B., Verrey,F. and
            Kuhn,L.C.
  TITLE     LAT2, a new basolateral 4F2hc/CD98-associated amino acid
            transporter of kidney and intestine
  JOURNAL   J Biol Chem 274 (49), 34948-34954 (1999)
   PUBMED   10574970
REFERENCE   8  (residues 1 to 332)
  AUTHORS   Bassi,M.T., Sperandeo,M.P., Incerti,B., Bulfone,A., Pepe,A.,
            Surace,E.M., Gattuso,C., De Grandi,A., Buoninconti,A., Riboni,M.,
            Manzoni,M., Andria,G., Ballabio,A., Borsani,G. and Sebastio,G.
  TITLE     SLC7A8, a gene mapping within the lysinuric protein intolerance
            critical region, encodes a new member of the
            glycoprotein-associated amino acid transporter family
  JOURNAL   Genomics 62 (2), 297-303 (1999)
   PUBMED   10610726
REFERENCE   9  (residues 1 to 332)
  AUTHORS   Pineda,M., Fernandez,E., Torrents,D., Estevez,R., Lopez,C.,
            Camps,M., Lloberas,J., Zorzano,A. and Palacin,M.
  TITLE     Identification of a membrane protein, LAT-2, that Co-expresses with
            4F2 heavy chain, an L-type amino acid transport activity with broad
            specificity for small and large zwitterionic amino acids
  JOURNAL   J Biol Chem 274 (28), 19738-19744 (1999)
   PUBMED   10391915
REFERENCE   10 (residues 1 to 332)
  AUTHORS   Borsani,G., Bassi,M.T., Sperandeo,M.P., De Grandi,A.,
            Buoninconti,A., Riboni,M., Manzoni,M., Incerti,B., Pepe,A.,
            Andria,G., Ballabio,A. and Sebastio,G.
  TITLE     SLC7A7, encoding a putative permease-related protein, is mutated in
            patients with lysinuric protein intolerance
  JOURNAL   Nat Genet 21 (3), 297-301 (1999)
   PUBMED   10080183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX248288.1, AB037669.1 and AF135830.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream, in-frame start codon, compared to variant 1. The
            encoded isoform (b) has a shorter N-terminus, compared to isoform
            a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853564.8323.1,
                                           SRR14038197.697552.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..332
                     /product="large neutral amino acids transporter small
                     subunit 2 isoform b"
                     /note="solute carrier family 7 (amino acid transporter,
                     L-type), member 8; solute carrier family 7 (cationic amino
                     acid transporter, y+ system), member 8; large neutral
                     amino acids transporter small subunit 2; integral membrane
                     protein E16H; L-type amino acid transporter 2; solute
                     carrier family 7 (amino acid transporter light chain, L
                     system), member 8"
                     /calculated_mol_wt=37053
     Region          <1..294
                     /region_name="2A0308"
                     /note="L-type amino acid transporter; TIGR00911"
                     /db_xref="CDD:273332"
     CDS             1..332
                     /gene="SLC7A8"
                     /gene_synonym="LAT2; LPI-PC1"
                     /coded_by="NM_182728.3:237..1235"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS41924.1"
                     /db_xref="GeneID:23428"
                     /db_xref="HGNC:HGNC:11066"
                     /db_xref="MIM:604235"
ORIGIN      
        1 mgivqickge yfwlepknaf enfqepdigl valaflqgsf ayggwnflny vteelvdpyk
       61 nlpraifisi plvtfvyvfa nvayvtamsp qellasnava vtfgekllgv mawimpisva
      121 lstfggvngs lftssrlffa gareghlpsv lamihvkrct pipallftci stllmlvtsd
      181 mytlinyvgf inylfygvtv agqivlrwkk pdiprpikin llfpiiyllf wafllvfslw
      241 sepvvcgigl aimltgvpvy flgvywqhkp kcfsdfiell tlvsqkmcvv vypevergsg
      301 teeanedmee qqqpmyqptp tkdkdvagqp qp
//
LOCUS       NP_001373882             514 aa            linear   PRI 21-NOV-2025
DEFINITION  solute carrier organic anion transporter family member 1A2 isoform
            13 [Homo sapiens].
ACCESSION   NP_001373882
VERSION     NP_001373882.1
DBSOURCE    REFSEQ: accession NM_001386953.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Flogel,S., Tust,M., Boussettaoui,S., Fischer,D. and Grundemann,D.
  TITLE     Enhancing transporter activity in heterologous expression systems
            with SAHA: a 2500-times more potent and odorless alternative to
            butyrate
  JOURNAL   FEBS Open Bio 15 (6), 906-913 (2025)
   PUBMED   40052353
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Kataoka,H., Akiyoshi,T., Uchida,Y., Imaoka,A., Terasaki,T. and
            Ohtani,H.
  TITLE     The Effects of N-Glycosylation on the Expression and Transport
            Activity of OATP1A2 and OATP2B1
  JOURNAL   J Pharm Sci 113 (5), 1376-1384 (2024)
   PUBMED   38432624
  REMARK    GeneRIF: The Effects of N-Glycosylation on the Expression and
            Transport Activity of OATP1A2 and OATP2B1.
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Han,H., Akiyoshi,T., Morita,T., Kataoka,H., Katayama,K., Yajima,K.,
            Imaoka,A. and Ohtani,H.
  TITLE     Comparison of the transport kinetics of fexofenadine and its pH
            dependency among OATP1A2 genetic variants
  JOURNAL   Drug Metab Pharmacokinet 47, 100470 (2022)
   PUBMED   36116173
  REMARK    GeneRIF: Comparison of the transport kinetics of fexofenadine and
            its pH dependency among OATP1A2 genetic variants.
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Hau,R.K., Klein,R.R., Wright,S.H. and Cherrington,N.J.
  TITLE     Localization of Xenobiotic Transporters Expressed at the Human
            Blood-Testis Barrier
  JOURNAL   Drug Metab Dispos 50 (6), 770-780 (2022)
   PUBMED   35307651
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Kullak-Ublick,G.A., Fisch,T., Oswald,M., Hagenbuch,B., Meier,P.J.,
            Beuers,U. and Paumgartner,G.
  TITLE     Dehydroepiandrosterone sulfate (DHEAS): identification of a carrier
            protein in human liver and brain
  JOURNAL   FEBS Lett 424 (3), 173-176 (1998)
   PUBMED   9539145
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Meier,P.J., Eckhardt,U., Schroeder,A., Hagenbuch,B. and Stieger,B.
  TITLE     Substrate specificity of sinusoidal bile acid and organic anion
            uptake systems in rat and human liver
  JOURNAL   Hepatology 26 (6), 1667-1677 (1997)
   PUBMED   9398014
  REMARK    Review article
REFERENCE   8  (residues 1 to 514)
  AUTHORS   Kullak-Ublick,G.A., Beuers,U., Fahney,C., Hagenbuch,B., Meier,P.J.
            and Paumgartner,G.
  TITLE     Identification and functional characterization of the promoter
            region of the human organic anion transporting polypeptide gene
  JOURNAL   Hepatology 26 (4), 991-997 (1997)
   PUBMED   9328325
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Kullak-Ublick,G.A., Beuers,U., Meier,P.J., Domdey,H. and
            Paumgartner,G.
  TITLE     Assignment of the human organic anion transporting polypeptide
            (OATP) gene to chromosome 12p12 by fluorescence in situ
            hybridization
  JOURNAL   J Hepatol 25 (6), 985-987 (1996)
   PUBMED   9007731
REFERENCE   10 (residues 1 to 514)
  AUTHORS   Kullak-Ublick,G.A., Hagenbuch,B., Stieger,B., Schteingart,C.D.,
            Hofmann,A.F., Wolkoff,A.W. and Meier,P.J.
  TITLE     Molecular and functional characterization of an organic anion
            transporting polypeptide cloned from human liver
  JOURNAL   Gastroenterology 109 (4), 1274-1282 (1995)
   PUBMED   7557095
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022224.22.
            
            Summary: This gene encodes a sodium-independent transporter which
            mediates cellular uptake of organic ions in the liver. Its
            substrates include bile acids, bromosulphophthalein, and some
            steroidal compounds. The protein is a member of the SLC21A family
            of solute carriers. Alternative splicing of this gene results in
            multiple transcript variants. [provided by RefSeq, Dec 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.185371.1,
                                           SRR1803616.149081.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..514
                     /product="solute carrier organic anion transporter family
                     member 1A2 isoform 13"
                     /note="organic anion transporting polypeptide A; solute
                     carrier family 21 (organic anion transporter), member 3;
                     sodium-independent organic anion transporter; OATP-1;
                     solute carrier family 21 member 3; organic
                     anion-transporting polypeptide 1"
                     /calculated_mol_wt=56569
     Region          <1..469
                     /region_name="oat"
                     /note="sodium-independent organic anion transporter;
                     TIGR00805"
                     /db_xref="CDD:273279"
     CDS             1..514
                     /gene="SLCO1A2"
                     /gene_synonym="OATP; OATP-A; OATP1A2; SLC21A3"
                     /coded_by="NM_001386953.1:676..2220"
                     /note="isoform 13 is encoded by transcript variant 32"
                     /db_xref="GeneID:6579"
                     /db_xref="HGNC:HGNC:10956"
                     /db_xref="MIM:602883"
ORIGIN      
        1 mwvyvlvgni vrgmgetpil plgisyiedf akfensplyi glvetgaiig pliglllasf
       61 canvyvdtgf vntddliitp tdtrwvgaww fgflicagvn vltaipfffl pntlpkegle
      121 tnadiiknen edkqkeevkk ekygitkdfl pfmkslscnp iymlfilvsv iqfnafvnmi
      181 sfmpkyleqq ygisssdaif lmgiynlppi cigyiiggli mkkfkitvkq aahigcwlsl
      241 leyllyflsf lmtcenssvv gintsyegip qdlyvendif adcnvdcncp skiwdpvcgn
      301 nglsylsacl agcetsigtg inmvfqncsc iqtsgnssav lglcdkgpdc slmlqyflil
      361 samssfiysl aaipgymvll rcmkseeksl gvglhtfctr vfagipapiy fgalmdstcl
      421 hwgtlkcges gacriydstt fryiylglpa alrgssfvpa liilillrkc hlpgenassg
      481 telietkvkg keneckdiyq kstvlkddel ktkl
//
LOCUS       NP_005125                933 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 4 regulatory subunit 1 isoform
            b [Homo sapiens].
ACCESSION   NP_005125
VERSION     NP_005125.1
DBSOURCE    REFSEQ: accession NM_005134.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 933)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 933)
  AUTHORS   Xu,W., Hua,Z., Wang,Y., Tang,W., Ou,W., Liu,F., Yang,Y., Ding,W.,
            Wang,Z., Cui,L., Ge,W., Gu,Y., Wang,X., Chen,Y., Liu,C.Y. and Du,P.
  TITLE     AMBRA1 promotes intestinal inflammation by antagonizing PP4R1/PP4c
            mediated IKK dephosphorylation in an autophagy-independent manner
  JOURNAL   Cell Death Differ 31 (5), 618-634 (2024)
   PUBMED   38424148
  REMARK    GeneRIF: AMBRA1 promotes intestinal inflammation by antagonizing
            PP4R1/PP4c mediated IKK dephosphorylation in an
            autophagy-independent manner.
REFERENCE   3  (residues 1 to 933)
  AUTHORS   He,Z., Zhong,Y., Lv,T., Wang,J., Jin,Y., Li,F. and Hu,H.
  TITLE     PP4R1 promotes glycolysis and gallbladder cancer progression
            through facilitating ERK1/2 mediated PKM2 nuclear translocation
  JOURNAL   Cancer Lett 586, 216677 (2024)
   PUBMED   38301910
  REMARK    GeneRIF: PP4R1 promotes glycolysis and gallbladder cancer
            progression through facilitating ERK1/2 mediated PKM2 nuclear
            translocation.
REFERENCE   4  (residues 1 to 933)
  AUTHORS   Zhu,X., Chen,X., Shen,X., Liu,Y., Fu,W., Wang,B., Zhao,L., Yang,F.,
            Mo,N., Zhong,G., Jiang,S. and Yang,Z.
  TITLE     PP4R1 accelerates the malignant progression of NSCLC via
            up-regulating HSPA6 expression and HSPA6-mediated ER stress
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (1), 119588 (2024)
   PUBMED   37739270
  REMARK    GeneRIF: PP4R1 accelerates the malignant progression of NSCLC via
            up-regulating HSPA6 expression and HSPA6-mediated ER stress.
REFERENCE   5  (residues 1 to 933)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 933)
  AUTHORS   Toyo-oka,K., Mori,D., Yano,Y., Shiota,M., Iwao,H., Goto,H.,
            Inagaki,M., Hiraiwa,N., Muramatsu,M., Wynshaw-Boris,A., Yoshiki,A.
            and Hirotsune,S.
  TITLE     Protein phosphatase 4 catalytic subunit regulates Cdk1 activity and
            microtubule organization via NDEL1 dephosphorylation
  JOURNAL   J Cell Biol 180 (6), 1133-1147 (2008)
   PUBMED   18347064
REFERENCE   7  (residues 1 to 933)
  AUTHORS   Gingras,A.C., Caballero,M., Zarske,M., Sanchez,A., Hazbun,T.R.,
            Fields,S., Sonenberg,N., Hafen,E., Raught,B. and Aebersold,R.
  TITLE     A novel, evolutionarily conserved protein phosphatase complex
            involved in cisplatin sensitivity
  JOURNAL   Mol Cell Proteomics 4 (11), 1725-1740 (2005)
   PUBMED   16085932
REFERENCE   8  (residues 1 to 933)
  AUTHORS   Zhang,X., Ozawa,Y., Lee,H., Wen,Y.D., Tan,T.H., Wadzinski,B.E. and
            Seto,E.
  TITLE     Histone deacetylase 3 (HDAC3) activity is regulated by interaction
            with protein serine/threonine phosphatase 4
  JOURNAL   Genes Dev 19 (7), 827-839 (2005)
   PUBMED   15805470
REFERENCE   9  (residues 1 to 933)
  AUTHORS   Wada,T., Miyata,T., Inagi,R., Nangaku,M., Wagatsuma,M., Suzuki,D.,
            Wadzinski,B.E., Okubo,K. and Kurokawa,K.
  TITLE     Cloning and characterization of a novel subunit of protein
            serine/threonine phosphatase 4 from mesangial cells
  JOURNAL   J Am Soc Nephrol 12 (12), 2601-2608 (2001)
   PUBMED   11729228
REFERENCE   10 (residues 1 to 933)
  AUTHORS   Kloeker,S. and Wadzinski,B.E.
  TITLE     Purification and identification of a novel subunit of protein
            serine/threonine phosphatase 4
  JOURNAL   J Biol Chem 274 (9), 5339-5347 (1999)
   PUBMED   10026142
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC060829.1 and AF100744.1.
            
            Summary: This gene encodes one of several alternate regulatory
            subunits of serine/threonine protein phosphatase 4 (PP4). The
            protein features multiple HEAT repeats. This protein forms a
            complex with PP4RC. This complex may have a distinct role from
            other PP4 complexes, including regulation of HDAC3 (Zhang et al.,
            PMID: 15805470). There is also a transcribed pseudogene on
            chromosome 20. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site compared to variant 1.This results in a shorter protein
            (isoform b), compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060829.1, AF111106.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.22"
     Protein         1..933
                     /product="serine/threonine-protein phosphatase 4
                     regulatory subunit 1 isoform b"
                     /note="serine/threonine phosphatase 4;
                     serine/threonine-protein phosphatase 4 regulatory subunit
                     1"
                     /calculated_mol_wt=105064
     Region          48..64
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          65..102
                     /region_name="HEAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          110..147
                     /region_name="HEAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          116..140
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(132..133,136,139..140,174..175,178,181..182,185,
                     214..215,218,221..222,225,253..254,257,260..261,292..293,
                     296,299)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          151..189
                     /region_name="HEAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          156..185
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          191..229
                     /region_name="HEAT 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          195..226
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          231..268
                     /region_name="HEAT 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          235..261
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          270..307
                     /region_name="HEAT 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          272..299
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          309..357
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          396..421
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          436..>454
                     /region_name="WRNPLPNID"
                     /note="Putative WW-binding domain and destruction box;
                     pfam15017"
                     /db_xref="CDD:464448"
     Region          456..482
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          488..525
                     /region_name="HEAT 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          551..589
                     /region_name="HEAT 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Site            order(626..627,630,633..634,664..665,668,671..672,675,
                     702..703,706,709..710,713,743..744,747,750..751,782..783,
                     786,789..790)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          647..675
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          681..717
                     /region_name="HEAT 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          685..714
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          723..751
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          762..791
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          782..820
                     /region_name="HEAT 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          844..881
                     /region_name="HEAT 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF05.1)"
     Region          846..872
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            918
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TF05.1)"
     CDS             1..933
                     /gene="PPP4R1"
                     /gene_synonym="MEG1; PP4(Rmeg); PP4R1"
                     /coded_by="NM_005134.4:76..2877"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42413.1"
                     /db_xref="GeneID:9989"
                     /db_xref="HGNC:HGNC:9320"
                     /db_xref="MIM:604908"
ORIGIN      
        1 madlsllqed lqedadgsld fvsqdemltp lgrldkyaas enifnrqmva rslldtlrev
       61 cdderdciav lerisrladd septvraelm eqvphialfc qenrpsipya fskfllpivv
      121 ryladqnnqv rktsqaalla lleqelierf dvetkvcpvl ieltapdsnd dvkteavaim
      181 ckmapmvgkd iterlilprf cemccdcrmf hvrkvcaanf gdicsvvgqq ateemllprf
      241 fqlcsdnvwg vrkacaecfm avscatcqei rrtklsalfi nlisdpsrwv rqaafqslgp
      301 fistfanpss sgqyfkeesk sseemsvenk nrtrdqeape dvqvrpedtp sdlsvsnssv
      361 ilentmedha aeasgkplge isvpldssll ctlsseshqe aasnendkkp gnyksmlrpe
      421 vgttsqdsal ldqelynsfh fwrtplpeid ldieleqnsg gkpspegpee esegpvpssp
      481 nitmatrkel eemienleph iddpdvkaqv evlsaalras sldaheetis iekrsdlqde
      541 ldinelpnck inqedsvpli sdavenmdst lhyihsdsdl snnssfspde errtkvqdvv
      601 pqalldqyls mtdpsraqtv dteiakhcay slpgvaltlg rqnwhclret yetlasdmqw
      661 kvrrtlafsi helavilgdq ltaadlvpif ngflkdldev rigvlkhlhd flkllhidkr
      721 reylyqlqef lvtdnsrnwr fraelaeqli lllelysprd vydylrpial nlcadkvssv
      781 rwisyklvse mvkklhaatp ptfgvdline lvenfgrcpk wsgrqafvfv cqtvieddcl
      841 pmdqfavhlm phlltlandr vpnvrvllak tlrqtllekd yflasaschq eaveqtimal
      901 qmdrdsdvky fasihpastk isedamstas sty
//
LOCUS       NP_001341557             725 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA mismatch repair protein Mlh1 isoform 7 [Homo sapiens].
ACCESSION   NP_001341557
VERSION     NP_001341557.1
DBSOURCE    REFSEQ: accession NM_001354628.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 725)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 725)
  AUTHORS   Liu,W.J., Lu,J., Zhou,W.X., Liu,J.Z. and Zhou,L.
  TITLE     MLH1 Inhibits Metastatic Potential of Pancreatic Ductal
            Adenocarcinoma via Downregulation of GPRC5C
  JOURNAL   Lab Invest 104 (9), 102107 (2024)
   PUBMED   38964504
  REMARK    GeneRIF: MLH1 Inhibits Metastatic Potential of Pancreatic Ductal
            Adenocarcinoma via Downregulation of GPRC5C.
REFERENCE   4  (residues 1 to 725)
  AUTHORS   Zou,Z.J., Hong,S.F., Zhang,Z.H., Lin,S.Q., Zeng,L.Y., Jiang,X.Y.,
            Chen,B.L. and Ren,J.
  TITLE     [Analysis of gene mutation in a family with Muir-Torre syndrome
            accompanied with extraorbital cystic sebaceous carcinoma]
  JOURNAL   Zhonghua Yi Xue Za Zhi 104 (33), 3154-3157 (2024)
   PUBMED   39168847
  REMARK    GeneRIF: [Analysis of gene mutation in a family with Muir-Torre
            syndrome accompanied with extraorbital cystic sebaceous carcinoma].
REFERENCE   5  (residues 1 to 725)
  AUTHORS   Mirbahari,S.N., Fatemi,N., Savabkar,S., Chaleshi,V., Zali,N.,
            Taleghani,M.Y., Mirzaei,E., Rejali,L., Moghadam,P.K. and
            Mojarad,E.N.
  TITLE     Unmasking early colorectal cancer clues: in silico and in vitro
            investigation of downregulated IGF2, SOCS1, MLH1, and CACNA1G in
            SSA polyps
  JOURNAL   Mol Biol Rep 51 (1), 764 (2024)
   PUBMED   38874740
  REMARK    GeneRIF: Unmasking early colorectal cancer clues: in silico and in
            vitro investigation of downregulated IGF2, SOCS1, MLH1, and CACNA1G
            in SSA polyps.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 725)
  AUTHORS   Nystrom-Lahti,M., Kristo,P., Nicolaides,N.C., Chang,S.Y.,
            Aaltonen,L.A., Moisio,A.L., Jarvinen,H.J., Mecklin,J.P.,
            Kinzler,K.W., Vogelstein,B. et al.
  TITLE     Founding mutations and Alu-mediated recombination in hereditary
            colon cancer
  JOURNAL   Nat Med 1 (11), 1203-1206 (1995)
   PUBMED   7584997
REFERENCE   7  (residues 1 to 725)
  AUTHORS   Charbonnier,F., Martin,C., Scotte,M., Sibert,L., Moreau,V. and
            Frebourg,T.
  TITLE     Alternative splicing of MLH1 messenger RNA in human normal cells
  JOURNAL   Cancer Res 55 (9), 1839-1841 (1995)
   PUBMED   7728749
REFERENCE   8  (residues 1 to 725)
  AUTHORS   Paraf,F., Sasseville,D., Watters,A.K., Narod,S., Ginsburg,O.,
            Shibata,H. and Jothy,S.
  TITLE     Clinicopathological relevance of the association between
            gastrointestinal and sebaceous neoplasms: the Muir-Torre syndrome
  JOURNAL   Hum Pathol 26 (4), 422-427 (1995)
   PUBMED   7705822
  REMARK    Review article
REFERENCE   9  (residues 1 to 725)
  AUTHORS   Hamilton,S.R., Liu,B., Parsons,R.E., Papadopoulos,N., Jen,J.,
            Powell,S.M., Krush,A.J., Berk,T., Cohen,Z., Tetu,B. et al.
  TITLE     The molecular basis of Turcot's syndrome
  JOURNAL   N Engl J Med 332 (13), 839-847 (1995)
   PUBMED   7661930
REFERENCE   10 (residues 1 to 725)
  AUTHORS   Idos,G. and Valle,L.
  TITLE     Lynch Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301390
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011816.17 and AC006583.31.
            
            Summary: The protein encoded by this gene can heterodimerize with
            mismatch repair endonuclease PMS2 to form MutL alpha, part of the
            DNA mismatch repair system. When MutL alpha is bound by MutS beta
            and some accessory proteins, the PMS2 subunit of MutL alpha
            introduces a single-strand break near DNA mismatches, providing an
            entry point for exonuclease degradation. The encoded protein is
            also involved in DNA damage signaling and can heterodimerize with
            DNA mismatch repair protein MLH3 to form MutL gamma, which is
            involved in meiosis. This gene was identified as a locus frequently
            mutated in hereditary nonpolyposis colon cancer (HNPCC). [provided
            by RefSeq, Aug 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1429058.1,
                                           SRR14038195.20928.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.2"
     Protein         1..725
                     /product="DNA mismatch repair protein Mlh1 isoform 7"
                     /note="DNA mismatch repair protein Mlh1; mutL homolog 1,
                     colon cancer, nonpolyposis type 2"
                     /calculated_mol_wt=81084
     Region          6..315
                     /region_name="mutl"
                     /note="DNA mismatch repair protein MutL; TIGR00585"
                     /db_xref="CDD:273155"
     Region          502..725
                     /region_name="Mlh1_C"
                     /note="DNA mismatch repair protein Mlh1 C-terminus;
                     pfam16413"
                     /db_xref="CDD:465109"
     CDS             1..725
                     /gene="MLH1"
                     /gene_synonym="COCA2; FCC2; hMLH1; HNPCC; HNPCC2; LYNCH2;
                     MLH-1; MMRCS1"
                     /coded_by="NM_001354628.2:31..2208"
                     /note="isoform 7 is encoded by transcript variant 21"
                     /db_xref="GeneID:4292"
                     /db_xref="HGNC:HGNC:7127"
                     /db_xref="MIM:120436"
ORIGIN      
        1 msfvagvirr ldetvvnria ageviqrpan aikemiencl dakstsiqvi vkegglkliq
       61 iqdngtgirk edldivcerf ttsklqsfed lasistygfr gealasishv ahvtittkta
      121 dgkcayrasy sdgklkappk pcagnqgtqi tvedlfynia trrkalknps eeygkilevv
      181 grysvhnagi sfsvkkqget vadvrtlpna stvdnirsif gnavsrelie igcedktlaf
      241 kmngyisnan ysvkkcifll finhrlvest slrkaietvy aaylpknthp flylsleisp
      301 qnvdvnvhpt khevhflhee silervqqhi eskllgsnss rmyftqtllp glagpsgemv
      361 ksttsltsss tsgssdkvya hqmvrtdsre qkldaflqpl skplssqpqa ivtedktdis
      421 sgrarqqdee mlelpapaev aaknqslegd ttkgtsemse krgptssnpr krhredsdve
      481 mveddsrkem taactprrri inltsvlslq eeineqghev lremlhnhsf vgcvnpqwal
      541 aqhqtklyll nttklseelf yqiliydfan fgvlrlsepa plfdlamlal dspesgwtee
      601 dgpkeglaey iveflkkkae mladyfslei devnwdeeke cfeslskeca mfysirkqyi
      661 seestlsgqq sevpgsipns wkwtvehivy kalrshilpp khftedgnil qlanlpdlyk
      721 vferc
//
LOCUS       NP_001337395             909 aa            linear   PRI 21-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 1 isoform 60 [Homo
            sapiens].
ACCESSION   NP_001337395
VERSION     NP_001337395.1
DBSOURCE    REFSEQ: accession NM_001350466.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 909)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 909)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 909)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 909)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 909)
  AUTHORS   Ruhle,F., Witten,A., Barysenka,A., Huge,A., Arning,A., Heller,C.,
            Krumpel,A., Mesters,R., Franke,A., Lieb,W., Riemenschneider,M.,
            Hiersche,M., Limperger,V., Nowak-Gottl,U. and Stoll,M.
  TITLE     Rare genetic variants in SMAP1, B3GAT2, and RIMS1 contribute to
            pediatric venous thromboembolism
  JOURNAL   Blood 129 (6), 783-790 (2017)
   PUBMED   28011674
  REMARK    GeneRIF: The study identified a region on chromosome 6 comprising
            the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus
            for pediatric venous thromboembolism.
REFERENCE   6  (residues 1 to 909)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 909)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
REFERENCE   8  (residues 1 to 909)
  AUTHORS   Schoch,S., Castillo,P.E., Jo,T., Mukherjee,K., Geppert,M., Wang,Y.,
            Schmitz,F., Malenka,R.C. and Sudhof,T.C.
  TITLE     RIM1alpha forms a protein scaffold for regulating neurotransmitter
            release at the active zone
  JOURNAL   Nature 415 (6869), 321-326 (2002)
   PUBMED   11797009
REFERENCE   9  (residues 1 to 909)
  AUTHORS   Coppola,T., Magnin-Luthi,S., Perret-Menoud,V., Gattesco,S.,
            Schiavo,G. and Regazzi,R.
  TITLE     Direct interaction of the Rab3 effector RIM with Ca2+ channels,
            SNAP-25, and synaptotagmin
  JOURNAL   J Biol Chem 276 (35), 32756-32762 (2001)
   PUBMED   11438518
REFERENCE   10 (residues 1 to 909)
  AUTHORS   Betz,A., Thakur,P., Junge,H.J., Ashery,U., Rhee,J.S., Scheuss,V.,
            Rosenmund,C., Rettig,J. and Brose,N.
  TITLE     Functional interaction of the active zone proteins Munc13-1 and
            RIM1 in synaptic vesicle priming
  JOURNAL   Neuron 30 (1), 183-196 (2001)
   PUBMED   11343654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590011.5, AL445256.18 and
            AL035633.18.
            
            Summary: The protein encoded by this gene is a RAS gene superfamily
            member that regulates synaptic vesicle exocytosis. This gene also
            plays a role in the regulation of voltage-gated calcium channels
            during neurotransmitter and insulin release. Mutations have
            suggested a role cognition and have been identified as the cause of
            cone-rod dystrophy type 7. Multiple transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Mar 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.77224.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..909
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..909
                     /product="regulating synaptic membrane exocytosis protein
                     1 isoform 60"
                     /note="RAB3-interacting protein 2; rab3-interacting
                     molecule 1; rab-3-interacting protein 2"
                     /calculated_mol_wt=101358
     Region          1..83
                     /region_name="PDZ_RIM-like"
                     /note="PDZ domain of Rab3-interacting molecule 1 (RIM),
                     RIM2, piccolo and related domains; cd06714"
                     /db_xref="CDD:467198"
     Site            order(8..14,29,32,62,66,69..70)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467198"
     Region          135..261
                     /region_name="C2A_RIM1alpha"
                     /note="C2 domain first repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04031"
                     /db_xref="CDD:175997"
     Site            order(166,172,227,229,237)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175997"
     Region          740..885
                     /region_name="C2B_RIM1alpha"
                     /note="C2 domain second repeat contained in
                     Rab3-interacting molecule (RIM) proteins; cd04028"
                     /db_xref="CDD:175994"
     Site            order(797,801..802,804,807,835,837,839,883..884)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:175994"
     CDS             1..909
                     /gene="RIMS1"
                     /gene_synonym="CORD7; RAB3IP2; RIM; RIM1"
                     /coded_by="NM_001350466.2:262..2991"
                     /note="isoform 60 is encoded by transcript variant 60"
                     /db_xref="GeneID:22999"
                     /db_xref="HGNC:HGNC:17282"
                     /db_xref="MIM:606629"
ORIGIN      
        1 mpkdsgallg lkvvggkmtd lgrlgafitk vkkgsladvv ghlragdevl ewngkplpga
       61 tneevyniil esksepqvei ivsrpigdip ripesshppl esssssfesq kmerpsisvi
      121 sptspgalkd apqvlpgqls vklwydkvgh qlivnvlqat dlparvdgrp rnpyvkmyfl
      181 pdrsdkskrr tktvkkilep kwnqtfvysh vhrrdfrerm leitvwdqpr vqeeeseflg
      241 eilieletal lddephwykl qthdesslpl pqpspfmprr hihgessskk lqrsqrisds
      301 disdyevddg igvvppvgyr ssareskstt ltvpeqqrtt hhrsrsvsph rgndqgkprs
      361 rlpnvplqrs ldeihptrrs rsptrhhdas rspvdhrtrd vdsqylseqd sellmlprak
      421 rgrsaeclht tselqpfldr arsastnclr pdtslhsper ermhrqrspt qsppadtsfs
      481 srrgrqlpqv pvrsgsieqe qekynsstka slvveertrq mkmkvhrfkq ttgsgssqel
      541 dreqyskyni hkdqyrscdn vsakssdsdv sdvsaisrts sasrlsstsf mseqserprg
      601 rirrmgtsgr simkstsvsg emytlehndg sqsdtavgtv gaggkkrrss lsakvvaivs
      661 rrsrstsqls qtesghkklk stiqrstetg maaemrkmvr qpsrestdgs insyssegnl
      721 ifpgvrlgad sqfsdfldgl gpaqlvgrqt latpamgdiq igmedkkgql evevirarsl
      781 tqkpgskstp apyvkvylle ngaciakkkt riarktldpl yqqslvfdes pqgkvlqviv
      841 wgdygrmdhk cfmgvaqill eeldlssmvi gwyklfppss lvdptltplt rrasqssles
      901 stgppcirs
//
LOCUS       NP_001373395             410 aa            linear   PRI 21-NOV-2025
DEFINITION  plasminogen activator inhibitor 1 isoform 12 precursor [Homo
            sapiens].
ACCESSION   NP_001373395
VERSION     NP_001373395.1
DBSOURCE    REFSEQ: accession NM_001386466.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Doelker,T., Gallwas,J. and Grundker,C.
  TITLE     Suppressing Expression of SERPINE1/PAI1 Through Activation of GPER1
            Reduces Progression of Vulvar Carcinoma
  JOURNAL   Cancer Genomics Proteomics 21 (6), 566-579 (2024)
   PUBMED   39467628
  REMARK    GeneRIF: Suppressing Expression of SERPINE1/PAI1 Through Activation
            of GPER1 Reduces Progression of Vulvar Carcinoma.
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Khoukaz,H.B., Vadali,M., Schoenherr,A., Ramirez-Perez,F.I.,
            Morales-Quinones,M., Sun,Z., Fujie,S., Foote,C.A., Lyu,Z., Zeng,S.,
            Augenreich,M.A., Cai,D., Chen,S.Y., Joshi,T., Ji,Y., Hill,M.A.,
            Martinez-Lemus,L.A. and Fay,W.P.
  TITLE     PAI-1 Regulates the Cytoskeleton and Intrinsic Stiffness of
            Vascular Smooth Muscle Cells
  JOURNAL   Arterioscler Thromb Vasc Biol 44 (10), 2191-2203 (2024)
   PUBMED   38868940
  REMARK    GeneRIF: PAI-1 Regulates the Cytoskeleton and Intrinsic Stiffness
            of Vascular Smooth Muscle Cells.
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Guo,X., Zhou,H., Liu,Y., Xu,W., Kanwore,K. and Zhang,L.
  TITLE     Glial-Cell-Line-Derived Neurotrophic Factor Promotes Glioblastoma
            Cell Migration and Invasion via the SMAD2/3-SERPINE1-Signaling Axis
  JOURNAL   Int J Mol Sci 25 (18), 10229 (2024)
   PUBMED   39337713
  REMARK    GeneRIF: Glial-Cell-Line-Derived Neurotrophic Factor Promotes
            Glioblastoma Cell Migration and Invasion via the
            SMAD2/3-SERPINE1-Signaling Axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Yatsenko,T., Rios,R., Nogueira,T., Salama,Y., Takahashi,S.,
            Adachi,E., Tabe,Y., Hattori,N., Osada,T., Naito,T., Takahashi,K.,
            Hattori,K. and Heissig,B.
  TITLE     The influence of 4G/5G polymorphism in the
            plasminogen-activator-inhibitor-1 promoter on COVID-19 severity and
            endothelial dysfunction
  JOURNAL   Front Immunol 15, 1445294 (2024)
   PUBMED   39281671
  REMARK    GeneRIF: The influence of 4G/5G polymorphism in the
            plasminogen-activator-inhibitor-1 promoter on COVID-19 severity and
            endothelial dysfunction.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Heiman,M., Gupta,S., Lewandowska,M. and Shapiro,A.D.
  TITLE     Complete Plasminogen Activator Inhibitor 1 Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   28771291
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Fay,W.P., Shapiro,A.D., Shih,J.L., Schleef,R.R. and Ginsburg,D.
  TITLE     Brief report: complete deficiency of plasminogen-activator
            inhibitor type 1 due to a frame-shift mutation
  JOURNAL   N Engl J Med 327 (24), 1729-1733 (1992)
   PUBMED   1435917
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Koh,S.C., Wong,P.C., Yuen,R., Chua,S.E., Ng,B.L. and Ratnam,S.S.
  TITLE     Concentration of plasminogen activators and inhibitor in the human
            endometrium at different phases of the menstrual cycle
  JOURNAL   J Reprod Fertil 96 (2), 407-413 (1992)
   PUBMED   1339823
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Hagege,J., Peraldi,M.N., Rondeau,E., Adida,C., Delarue,F.,
            Medcalf,R., Schleuning,W.D. and Sraer,J.D.
  TITLE     Plasminogen activator inhibitor-1 deposition in the extracellular
            matrix of cultured human mesangial cells
  JOURNAL   Am J Pathol 141 (1), 117-128 (1992)
   PUBMED   1632457
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Ehrlich,H.J., Gebbink,R.K., Keijer,J., Linders,M., Preissner,K.T.
            and Pannekoek,H.
  TITLE     Alteration of serpin specificity by a protein cofactor. Vitronectin
            endows plasminogen activator inhibitor 1 with thrombin inhibitory
            properties
  JOURNAL   J Biol Chem 265 (22), 13029-13035 (1990)
   PUBMED   1695900
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004876.2.
            
            Summary: This gene encodes a member of the serine proteinase
            inhibitor (serpin) superfamily. This member is the principal
            inhibitor of tissue plasminogen activator (tPA) and urokinase
            (uPA), and hence is an inhibitor of fibrinolysis. The protein also
            functions as a component of innate antiviral immunity. Defects in
            this gene are the cause of plasminogen activator inhibitor-1
            deficiency (PAI-1 deficiency), and high concentrations of the gene
            product are associated with thrombophilia. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14243140.9738882.1,
                                           SRR14038194.80895.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..410
                     /product="plasminogen activator inhibitor 1 isoform 12
                     precursor"
                     /note="serine (or cysteine) proteinase inhibitor, clade E
                     (nexin, plasminogen activator inhibitor type 1), member 1;
                     endothelial plasminogen activator inhibitor; serpin E1;
                     serpin peptidase inhibitor, clade E (nexin, plasminogen
                     activator inhibitor type 1), member 1"
                     /calculated_mol_wt=43638
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2309
     Region          29..410
                     /region_name="serpinE1_PAI-1"
                     /note="serpin family E member 1, plasminogen activator
                     inhibitor-1; cd02051"
                     /db_xref="CDD:381007"
     Site            order(132,141..142,145,151,153..156,162,166,169..170)
                     /site_type="other"
                     /note="vitronectin binding site [polypeptide binding]"
                     /db_xref="CDD:381007"
     Site            order(180..181,354,356)
                     /site_type="other"
                     /note="putative Cl binding site [ion binding]"
                     /db_xref="CDD:381007"
     Site            order(236,238,241,243,253,272,300..303,369..370,372..381)
                     /site_type="other"
                     /note="plasminogen activator binding site [polypeptide
                     binding]"
                     /db_xref="CDD:381007"
     Site            240
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05121.1)"
     Site            296
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P05121.1)"
     Site            360
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P05121.1)"
     Site            363..388
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381007"
     Site            377..378
                     /site_type="other"
                     /note="Reactive bond; propagated from UniProtKB/Swiss-Prot
                     (P05121.1)"
     CDS             1..410
                     /gene="SERPINE1"
                     /gene_synonym="PAI; PAI-1; PAI1; PLANH1"
                     /coded_by="NM_001386466.1:143..1375"
                     /note="isoform 12 precursor is encoded by transcript
                     variant 12"
                     /db_xref="GeneID:5054"
                     /db_xref="HGNC:HGNC:8583"
                     /db_xref="MIM:173360"
ORIGIN      
        1 mqmspaltcl vlglalvfge gsavhhppsy vahlasdfgv rvfqqvaqas kdrnvvfspy
       61 gvasvlamlq lttggetqqq iqaamgfkid geprdtrgdk gmapalrhly kelmgpwnkd
      121 eisttdaifv qrdlklvqgf mphffrlfrs tvkqvdfsev erarfiindw vkthtkgmis
      181 nllgkgavdq ltrlvlvnal yfngqwktpf pdssthrrlf hksdgstvsv pmmaqtnkfn
      241 ytefttpdgh yydilelpyh gdtlsmfiaa pyekevplsa ltnilsaqli shwkgnmtrl
      301 prllvlpkfs letevdlrkp lenlgmtdmf rqfqadftsl sdqeplhvaq alqkvkievn
      361 esgtvassst avivsarmap eeiimdrpfl fvvrhnptgt vlfmgqvmep
//
LOCUS       NP_001309094             682 aa            linear   PRI 21-NOV-2025
DEFINITION  transcription factor 12 isoform b [Homo sapiens].
ACCESSION   NP_001309094
VERSION     NP_001309094.1
DBSOURCE    REFSEQ: accession NM_001322165.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Wang,G., Wu,Y., Su,Y., Qu,N., Chen,B., Zhou,D., Yuan,L., Yin,M.,
            Liu,M. and Zhou,W.
  TITLE     TCF12-regulated GRB7 facilitates the HER2+ breast cancer
            progression by activating Notch1 signaling pathway
  JOURNAL   J Transl Med 22 (1), 745 (2024)
   PUBMED   39113057
  REMARK    GeneRIF: TCF12-regulated GRB7 facilitates the HER2+ breast cancer
            progression by activating Notch1 signaling pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 682)
  AUTHORS   Yan,S., Yuan,M., Yang,X., Huang,X., Wu,D., Wang,N., Sun,X., Qin,Y.,
            Fei,Y., Zhao,Z. and Wang,Q.
  TITLE     Lncrna CASC15 Activated By TCF12 Promote Colorectal Cancer
            Progression via EMT
  JOURNAL   Comb Chem High Throughput Screen 27 (8), 1222-1230 (2024)
   PUBMED   37680149
  REMARK    GeneRIF: Lncrna CASC15 Activated By TCF12 Promote Colorectal Cancer
            Progression via EMT.
REFERENCE   4  (residues 1 to 682)
  AUTHORS   Geng,N., Yu,Z., Zeng,X., Xu,D., Gao,H., Yang,M. and Huang,X.
  TITLE     Nuclear Tubulin Enhances CXCR4 Transcription and Promotes
            Chemotaxis Through TCF12 Transcription Factor in human
            Hematopoietic Stem Cells
  JOURNAL   Stem Cell Rev Rep 19 (5), 1328-1339 (2023)
   PUBMED   37067645
  REMARK    GeneRIF: Nuclear Tubulin Enhances CXCR4 Transcription and Promotes
            Chemotaxis Through TCF12 Transcription Factor in human
            Hematopoietic Stem Cells.
REFERENCE   5  (residues 1 to 682)
  AUTHORS   Li,X.P., Jia,Y.L., Duan,Y.Q., Zhao,Y., Yin,X.L., Zhen,S.M.,
            Zhang,Y. and Liu,L.H.
  TITLE     Circular RNA hsa_circ_0002938 (circCRIM1) promotes the progression
            of esophageal squamous cell carcinoma by upregulating transcription
            factor 12
  JOURNAL   Neoplasma 70 (1), 145-157 (2023)
   PUBMED   36916930
  REMARK    GeneRIF: Circular RNA hsa_circ_0002938 (circCRIM1) promotes the
            progression of esophageal squamous cell carcinoma by upregulating
            transcription factor 12.
REFERENCE   6  (residues 1 to 682)
  AUTHORS   Zhang,Y., Doyle,K. and Bina,M.
  TITLE     Interactions of HTF4 with E-box motifs in the long terminal repeat
            of human immunodeficiency virus type 1
  JOURNAL   J Virol 66 (9), 5631-5634 (1992)
   PUBMED   1501295
REFERENCE   7  (residues 1 to 682)
  AUTHORS   Hu,J.S., Olson,E.N. and Kingston,R.E.
  TITLE     HEB, a helix-loop-helix protein related to E2A and ITF2 that can
            modulate the DNA-binding ability of myogenic regulatory factors
  JOURNAL   Mol Cell Biol 12 (3), 1031-1042 (1992)
   PUBMED   1312219
REFERENCE   8  (residues 1 to 682)
  AUTHORS   Zhang,Y. and Bina,M.
  TITLE     The nucleotide sequence of the human transcription factor HTF4a
            cDNA
  JOURNAL   DNA Seq 2 (6), 397-403 (1992)
   PUBMED   1446075
REFERENCE   9  (residues 1 to 682)
  AUTHORS   Sommer,L., Hagenbuchle,O., Wellauer,P.K. and Strubin,M.
  TITLE     Nuclear targeting of the transcription factor PTF1 is mediated by a
            protein subunit that does not bind to the PTF1 cognate sequence
  JOURNAL   Cell 67 (5), 987-994 (1991)
   PUBMED   1720355
REFERENCE   10 (residues 1 to 682)
  AUTHORS   Zhang,Y., Babin,J., Feldhaus,A.L., Singh,H., Sharp,P.A. and Bina,M.
  TITLE     HTF4: a new human helix-loop-helix protein
  JOURNAL   Nucleic Acids Res 19 (16), 4555 (1991)
   PUBMED   1886779
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010999.6, AC090511.3,
            AC090532.1 and AC016525.11.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix (bHLH) E-protein family that recognizes the
            consensus binding site (E-box) CANNTG. This encoded protein is
            expressed in many tissues, among them skeletal muscle, thymus, B-
            and T-cells, and may participate in regulating lineage-specific
            gene expression through the formation of heterodimers with other
            bHLH E-proteins. Several alternatively spliced transcript variants
            of this gene have been described, but the full-length nature of
            some of these variants has not been determined. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.16001.1,
                                           SRR1660803.156533.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.3"
     Protein         1..682
                     /product="transcription factor 12 isoform b"
                     /note="helix-loop-helix transcription factor 4;
                     E-box-binding protein; DNA-binding protein HTF4;
                     transcription factor HTF-4; class B basic helix-loop-helix
                     protein 20"
                     /calculated_mol_wt=72834
     Region          19..27
                     /region_name="9aaTAD"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99081.1)"
     Region          25..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99081.1)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99081.1)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99081.1)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99081.1)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99081.1)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99081.1)"
     Region          119..140
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99081.1)"
     Region          140..219
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99081.1)"
     Region          182..196
                     /region_name="Interaction with RUNX1T1.
                     /evidence=ECO:0000269|PubMed:23812588"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99081.1)"
     Region          281..313
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99081.1)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99081.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99081.1)"
     Region          349..395
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99081.1)"
     Region          462..580
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99081.1)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99081.1)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q99081.1)"
     Site            558
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99081.1)"
     Site            559
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99081.1)"
     Region          571..655
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(579,583,585..587,589,594,615..616)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(592..593,596..597,599..600,603,607,617,620,624,627,
                     630..635)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     Region          632..655
                     /region_name="Class A specific domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99081.1)"
     Region          651..682
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99081.1)"
     CDS             1..682
                     /gene="TCF12"
                     /gene_synonym="bHLHb20; CRS3; HEB; HH26; HsT17266; HTF4;
                     p64; TCF-12"
                     /coded_by="NM_001322165.2:470..2518"
                     /note="isoform b is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS10159.1"
                     /db_xref="GeneID:6938"
                     /db_xref="HGNC:HGNC:11623"
                     /db_xref="MIM:600480"
ORIGIN      
        1 mnpqqqrmaa igtdkelsdl ldfsamfspp vnsgktrptt lgssqfsgsg iderggttsw
       61 gtsgqpspsy dssrgftdsp hysdhlndsr lgaheglspt pfmnsnlmgk tsergsfsly
      121 srdtglpgcq ssllrqdlgl gspaqlsssg kpgtayysfs atssrrrplh dsaaldplqa
      181 kkvrkvppgl pssvyapspn sddfnresps ypspkpptsm fastffmqdg thnssdlwss
      241 sngmsqpgfg gilgtstshm sqsssygnlh shdrlsypph svsptdints lppmssfhrg
      301 stssspyvaa shtppingsd silgtrgnaa gssqtgdalg kalasiyspd htsssfpsnp
      361 stpvgspspl tgtsqwprpg gqapsspsye nslhslqsrm edrldrldda ihvlrnhavg
      421 pstslpaghs dihsllgpsh napigslnsn yggsslvass rsasmvgthr edsvslngnh
      481 svlsstvtts stdlnhktqe nyrgglqsqs gtvvtteikt enkekdenlh eppssddmks
      541 ddessqkdik vssrgrtsst nededlnpeq kierekerrm annarerlrv rdineafkel
      601 grmcqlhlks ekpqtkllil hqavavilsl eqqvrernln pkaaclkrre eekvsavsae
      661 ppttlpgthp glsettnpmg hm
//
LOCUS       NP_005202                972 aa            linear   PRI 21-NOV-2025
DEFINITION  macrophage colony-stimulating factor 1 receptor isoform a precursor
            [Homo sapiens].
ACCESSION   NP_005202 XP_005268432
VERSION     NP_005202.2
DBSOURCE    REFSEQ: accession NM_005211.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 972)
  AUTHORS   Beerepoot,S., Wolf,N.I., van der Knaap,M.S., Nierkens,S. and
            Plantinga,M.
  TITLE     Heterozygous missense CSF1R variants hamper in vitro CD34+-derived
            dendritic cell generation but not in vivo dendritic cell
            development
  JOURNAL   Mol Immunol 174, 41-46 (2024)
   PUBMED   39182279
  REMARK    GeneRIF: Heterozygous missense CSF1R variants hamper in vitro
            CD34+-derived dendritic cell generation but not in vivo dendritic
            cell development.
REFERENCE   2  (residues 1 to 972)
  AUTHORS   Schmitz,A.S., Raju,J., Kohler,W., Klebe,S., Cheheb,K., Reschke,F.,
            Biskup,S., Haack,T.B., Roeben,B., Kellner,M., Rahner,N., Bloch,T.,
            Lemke,J., Bender,B., Schols,L., Hengel,H. and Hayer,S.N.
  TITLE     Novel variants in CSF1R associated with adult-onset
            leukoencephalopathy with axonal spheroids and pigmented glia (ALSP)
  JOURNAL   J Neurol 271 (9), 6025-6037 (2024)
   PUBMED   39031193
  REMARK    GeneRIF: Novel variants in CSF1R associated with adult-onset
            leukoencephalopathy with axonal spheroids and pigmented glia
            (ALSP).
REFERENCE   3  (residues 1 to 972)
  AUTHORS   Orsenigo,F., Stewart,A., Hammer,C.P., Clarke,E., Simpkin,D.,
            Attia,H., Rockall,T., Gordon,S. and Martinez,F.O.
  TITLE     Unifying considerations and evidence of macrophage activation
            mosaicism through human CSF1R and M1/M2 genes
  JOURNAL   Cell Rep 43 (6), 114352 (2024)
   PUBMED   38870011
  REMARK    GeneRIF: Unifying considerations and evidence of macrophage
            activation mosaicism through human CSF1R and M1/M2 genes.
REFERENCE   4  (residues 1 to 972)
  AUTHORS   Dorion,M.F., Casas,D., Shlaifer,I., Yaqubi,M., Fleming,P.,
            Karpilovsky,N., Chen,C.X., Nicouleau,M., Piscopo,V.E.C.,
            MacDougall,E.J., Alluli,A., Goldsmith,T.M., Schneider,A.,
            Dorion,S., Aprahamian,N., MacDonald,A., Thomas,R.A., Dudley,R.W.R.,
            Hall,J.A., Fon,E.A., Antel,J.P., Stratton,J.A., Durcan,T.M., La
            Piana,R. and Healy,L.M.
  TITLE     An adapted protocol to derive microglia from stem cells and its
            application in the study of CSF1R-related disorders
  JOURNAL   Mol Neurodegener 19 (1), 31 (2024)
   PUBMED   38576039
  REMARK    GeneRIF: An adapted protocol to derive microglia from stem cells
            and its application in the study of CSF1R-related disorders.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 972)
  AUTHORS   Lamprecht,B., Walter,K., Kreher,S., Kumar,R., Hummel,M., Lenze,D.,
            Kochert,K., Bouhlel,M.A., Richter,J., Soler,E., Stadhouders,R.,
            Johrens,K., Wurster,K.D., Callen,D.F., Harte,M.F., Giefing,M.,
            Barlow,R., Stein,H., Anagnostopoulos,I., Janz,M., Cockerill,P.N.,
            Siebert,R., Dorken,B., Bonifer,C. and Mathas,S.
  TITLE     Derepression of an endogenous long terminal repeat activates the
            CSF1R proto-oncogene in human lymphoma
  JOURNAL   Nat Med 16 (5), 571-579 (2010)
   PUBMED   20436485
REFERENCE   6  (residues 1 to 972)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   7  (residues 1 to 972)
  AUTHORS   Dulski,J., Sundal,C. and Wszolek,Z.K.
  TITLE     CSF1R-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934315
REFERENCE   8  (residues 1 to 972)
  AUTHORS   Gout,I., Dhand,R., Panayotou,G., Fry,M.J., Hiles,I., Otsu,M. and
            Waterfield,M.D.
  TITLE     Expression and characterization of the p85 subunit of the
            phosphatidylinositol 3-kinase complex and a related p85 beta
            protein by using the baculovirus expression system
  JOURNAL   Biochem J 288 (Pt 2) (Pt 2), 395-405 (1992)
   PUBMED   1334406
REFERENCE   9  (residues 1 to 972)
  AUTHORS   Roberts,W.M., Shapiro,L.H., Ashmun,R.A. and Look,A.T.
  TITLE     Transcription of the human colony-stimulating factor-1 receptor
            gene is regulated by separate tissue-specific promoters
  JOURNAL   Blood 79 (3), 586-593 (1992)
   PUBMED   1531036
REFERENCE   10 (residues 1 to 972)
  AUTHORS   Galland,F., Stefanova,M., Lafage,M. and Birnbaum,D.
  TITLE     Localization of the 5' end of the MCF2 oncogene to human chromosome
            15q15----q23
  JOURNAL   Cytogenet Cell Genet 60 (2), 114-116 (1992)
   PUBMED   1611909
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X03663.1, BX648599.1,
            BC047521.1, BM825705.1 and BQ028933.1.
            
            On or before Aug 31, 2013 this sequence version replaced
            XP_005268432.1, NP_005202.1.
            
            Summary: The protein encoded by this gene is the receptor for
            colony stimulating factor 1, a cytokine which controls the
            production, differentiation, and function of macrophages. This
            receptor mediates most if not all of the biological effects of this
            cytokine. Ligand binding activates the receptor kinase through a
            process of oligomerization and transphosphorylation. The encoded
            protein is a tyrosine kinase transmembrane receptor and member of
            the CSF1/PDGF receptor family of tyrosine-protein kinases.
            Mutations in this gene have been associated with a predisposition
            to myeloid malignancy. The first intron of this gene contains a
            transcriptionally inactive ribosomal protein L7 processed
            pseudogene oriented in the opposite direction. Alternative splicing
            results in multiple transcript variants. Expression of a splice
            variant from an LTR promoter has been found in Hodgkin lymphoma
            (HL), HL cell lines and anaplastic large cell lymphoma. [provided
            by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (1) differs in the 5' UTR compared
            to variant 4. Variants 1, 2, 4, and 5 all encode the same isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X03663.1, SRR7346977.1497178.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..972
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..972
                     /product="macrophage colony-stimulating factor 1 receptor
                     isoform a precursor"
                     /EC_number="2.7.10.1"
                     /note="McDonough feline sarcoma viral (v-fms) oncogene
                     homolog; CD115 antigen; FMS proto-oncogene; macrophage
                     colony stimulating factor I receptor; CSF-1 receptor;
                     proto-oncogene c-Fms"
                     /calculated_mol_wt=106069
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1933
     mat_peptide     20..972
                     /product="Macrophage colony-stimulating factor 1 receptor.
                     /id=PRO_0000016765"
                     /note="propagated from UniProtKB/Swiss-Prot (P07333.2)"
                     /calculated_mol_wt=106069
     Region          28..85
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          38..42
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            45
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Region          55..58
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          66..71
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            73
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Region          81..86
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          94..97
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            153
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Region          203..295
                     /region_name="IgI_3_CSF-1R"
                     /note="Third immunoglobulin domain of the hematopoietic
                     colony-stimulating factor 1 receptor (CSF-1R), and similar
                     domains; member of the I-set of IgSF domains; cd20936"
                     /db_xref="CDD:409530"
     Region          203..208
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409530"
     Region          210..216
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409530"
     Region          220..228
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409530"
     Region          234..238
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409530"
     Site            240
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Region          241..244
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409530"
     Region          248..253
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409530"
     Region          257..265
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409530"
     Region          274..282
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409530"
     Site            275
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Region          285..295
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409530"
     Region          299..400
                     /region_name="IgI_4_SCFR_like"
                     /note="Fourth immunoglobulin (Ig)-like domain of stem cell
                     factor receptor (SCFR), and similar domains; member of the
                     I-set of IgSF domains; cd04975"
                     /db_xref="CDD:409364"
     Region          299..305
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409364"
     Site            302
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Region          309..314
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409364"
     Region          317..327
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409364"
     Region          331..338
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409364"
     Site            335
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Region          340..343
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409364"
     Region          347..352
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409364"
     Site            353
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Region          361..370
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409364"
     Site            order(369..372,375)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409364"
     Region          377..385
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409364"
     Region          388..399
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409364"
     Region          401..489
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            412
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Site            428
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Site            480
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Site            518..538
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07333.2)"
     Region          542..574
                     /region_name="Regulatory juxtamembrane domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P07333.2)"
     Region          543..914
                     /region_name="PTKc_CSF-1R"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Colony-Stimulating Factor-1 Receptor; cd05106"
                     /db_xref="CDD:133237"
     Site            546
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20489731; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Site            561
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P09581; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Site            order(588..589,591..594,596,614,616,664,666,670,778,
                     782..783,785,796,814..818,827,862)
                     /site_type="active"
                     /db_xref="CDD:133237"
     Site            order(588..589,591..594,596,614,616,664,666,670,782..783,
                     785,796)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:133237"
     Site            699
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20489731,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Site            708
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20489731; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Site            723
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20489731; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Site            order(778,782,814..818,827,862)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133237"
     Site            795..820
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:133237"
     Region          796..818
                     /region_name="Activation loop"
                     /note="propagated from UniProtKB/Swiss-Prot (P07333.2)"
     Site            809
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20489731; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Region          918..950
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07333.2)"
     Site            923
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P09581; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     Site            969
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P09581; propagated from
                     UniProtKB/Swiss-Prot (P07333.2)"
     CDS             1..972
                     /gene="CSF1R"
                     /gene_synonym="BANDDOS; C-FMS; CD115; CSF-1R; CSFR; FIM2;
                     FMS; GPSC; HDLS; HDLS1; M-CSF-R"
                     /coded_by="NM_005211.4:286..3204"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4302.1"
                     /db_xref="GeneID:1436"
                     /db_xref="HGNC:HGNC:2433"
                     /db_xref="MIM:164770"
ORIGIN      
        1 mgpgvlllll vatawhgqgi pviepsvpel vvkpgatvtl rcvgngsvew dgppsphwtl
       61 ysdgsssils tnnatfqntg tyrctepgdp lggsaaihly vkdparpwnv laqevvvfed
      121 qdallpcllt dpvleagvsl vrvrgrplmr htnysfspwh gftihrakfi qsqdyqcsal
      181 mggrkvmsis irlkvqkvip gppaltlvpa elvrirgeaa qivcsassvd vnfdvflqhn
      241 ntklaipqqs dfhnnryqkv ltlnldqvdf qhagnyscva snvqgkhsts mffrvvesay
      301 lnlsseqnli qevtvgegln lkvmveaypg lqgfnwtylg pfsdhqpepk lanattkdty
      361 rhtftlslpr lkpseagrys flarnpggwr altfeltlry ppevsviwtf ingsgtllca
      421 asgypqpnvt wlqcsghtdr cdeaqvlqvw ddpypevlsq epfhkvtvqs lltvetlehn
      481 qtyecrahns vgsgswafip isagahthpp deflftpvvv acmsimalll lllllllyky
      541 kqkpkyqvrw kiiesyegns ytfidptqlp ynekwefprn nlqfgktlga gafgkvveat
      601 afglgkedav lkvavkmlks tahadekeal mselkimshl gqhenivnll gacthggpvl
      661 viteyccygd llnflrrkae amlgpslspg qdpeggvdyk nihlekkyvr rdsgfssqgv
      721 dtyvemrpvs tssndsfseq dldkedgrpl elrdllhfss qvaqgmafla skncihrdva
      781 arnvlltngh vakigdfgla rdimndsnyi vkgnarlpvk wmapesifdc vytvqsdvws
      841 ygillweifs lglnpypgil vnskfyklvk dgyqmaqpaf apkniysimq acwalepthr
      901 ptfqqicsfl qeqaqedrre rdytnlpsss rsggsgssss eleeessseh ltcceqgdia
      961 qpllqpnnyq fc
//
LOCUS       NP_001035888             465 aa            linear   PRI 21-NOV-2025
DEFINITION  monocarboxylate transporter 4 [Homo sapiens].
ACCESSION   NP_001035888
VERSION     NP_001035888.1
DBSOURCE    REFSEQ: accession NM_001042423.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Yu,T., Liu,Z., Tao,Q., Xu,X., Li,X., Li,Y., Chen,M., Liu,R.,
            Chen,D., Wu,M. and Yu,J.
  TITLE     Targeting tumor-intrinsic SLC16A3 to enhance anti-PD-1 efficacy via
            tumor immune microenvironment reprogramming
  JOURNAL   Cancer Lett 589, 216824 (2024)
   PUBMED   38522774
  REMARK    GeneRIF: Targeting tumor-intrinsic SLC16A3 to enhance anti-PD-1
            efficacy via tumor immune microenvironment reprogramming.
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Li,Q., Li,Z., Li,J., Qin,X., Wu,F. and Chen,C.
  TITLE     Bone Morphogenetic Protein-4 Promotes Phenotypic Modulation via
            SMAD-4/MCT-4 Axis in Vascular Smooth Muscle Cells
  JOURNAL   J Vasc Res 61 (3), 99-108 (2024)
   PUBMED   38151007
  REMARK    GeneRIF: Bone Morphogenetic Protein-4 Promotes Phenotypic
            Modulation via SMAD-4/MCT-4 Axis in Vascular Smooth Muscle Cells.
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Mukai,Y., Yamaguchi,A., Sakuma,T., Nadai,T., Furugen,A., Narumi,K.
            and Kobayashi,M.
  TITLE     Involvement of SLC16A1/MCT1 and SLC16A3/MCT4 in l-lactate transport
            in the hepatocellular carcinoma cell line
  JOURNAL   Biopharm Drug Dispos 43 (5), 183-191 (2022)
   PUBMED   36104287
  REMARK    GeneRIF: Involvement of SLC16A1/MCT1 and SLC16A3/MCT4 in l-lactate
            transport in the hepatocellular carcinoma cell line.
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Manning Fox,J.E., Meredith,D. and Halestrap,A.P.
  TITLE     Characterisation of human monocarboxylate transporter 4
            substantiates its role in lactic acid efflux from skeletal muscle
  JOURNAL   J Physiol 529 Pt 2 (Pt 2), 285-293 (2000)
   PUBMED   11101640
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Kirk,P., Wilson,M.C., Heddle,C., Brown,M.H., Barclay,A.N. and
            Halestrap,A.P.
  TITLE     CD147 is tightly associated with lactate transporters MCT1 and MCT4
            and facilitates their cell surface expression
  JOURNAL   EMBO J 19 (15), 3896-3904 (2000)
   PUBMED   10921872
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Halestrap,A.P. and Price,N.T.
  TITLE     The proton-linked monocarboxylate transporter (MCT) family:
            structure, function and regulation
  JOURNAL   Biochem J 343 Pt 2 (Pt 2), 281-299 (1999)
   PUBMED   10510291
  REMARK    Review article
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Price,N.T., Jackson,V.N. and Halestrap,A.P.
  TITLE     Cloning and sequencing of four new mammalian monocarboxylate
            transporter (MCT) homologues confirms the existence of a
            transporter family with an ancient past
  JOURNAL   Biochem J 329 (Pt 2) (Pt 2), 321-328 (1998)
   PUBMED   9425115
REFERENCE   10 (residues 1 to 465)
  AUTHORS   Cori,C.F.
  TITLE     The glucose-lactic acid cycle and gluconeogenesis
  JOURNAL   Curr Top Cell Regul 18, 377-387 (1981)
   PUBMED   7273846
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC132872.17.
            
            Summary: Lactic acid and pyruvate transport across plasma membranes
            is catalyzed by members of the proton-linked monocarboxylate
            transporter (MCT) family, which has been designated solute carrier
            family-16. Each MCT appears to have slightly different substrate
            and inhibitor specificities and transport kinetics, which are
            related to the metabolic requirements of the tissues in which it is
            found. The MCTs, which include MCT1 (SLC16A1; MIM 600682) and MCT2
            (SLC16A7; MIM 603654), are characterized by 12 predicted
            transmembrane domains (Price et al., 1998 [PubMed
            9425115]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, 3, 4, 5 and 6 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853565.14099.1,
                                           SRR14038192.3542425.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..465
                     /product="monocarboxylate transporter 4"
                     /note="monocarboxylate transporter 3; solute carrier
                     family 16 (monocarboxylic acid transporters), member 3;
                     solute carrier family 16, member 3 (monocarboxylic acid
                     transporter 4); solute carrier family 16 (monocarboxylate
                     transporter), member 3"
                     /calculated_mol_wt=49338
     Site            18..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Region          21..406
                     /region_name="MFS_MCT3_4"
                     /note="Monocarboxylate transporters 9 and 14, and similar
                     proteins of the Major Facilitator Superfamily of
                     transporters; cd17430"
                     /db_xref="CDD:340988"
     Site            order(32..33,36..37,40,75,126..127,129..131,134,153,
                     156..157,160,235,238..239,242..244,247,274,278,331..332,
                     336,340,356,359..360,363..364,367)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340988"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            85..105
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            110..130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            180..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            228..248
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            265..285
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            295..315
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            318..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            352..372
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            385..405
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Region          419..438
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Region          423..441
                     /region_name="Basolateral sorting signal.
                     /evidence=ECO:0000269|PubMed:21199217"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15427.1)"
     Region          441..465
                     /region_name="Basolateral sorting signal.
                     /evidence=ECO:0000269|PubMed:21199217"
                     /note="propagated from UniProtKB/Swiss-Prot (O15427.1)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O15427.1)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O15427.1)"
     CDS             1..465
                     /gene="SLC16A3"
                     /gene_synonym="MCT 3; MCT 4; MCT-3; MCT-4; MCT3; MCT4"
                     /coded_by="NM_001042423.3:155..1552"
                     /db_xref="CCDS:CCDS11804.1"
                     /db_xref="GeneID:9123"
                     /db_xref="HGNC:HGNC:10924"
                     /db_xref="MIM:603877"
ORIGIN      
        1 mggavvdegp tgvkapdggw gwavlfgcfv itgfsyafpk avsvffkeli qefgigysdt
       61 awissillam lygtgplcsv cvnrfgcrpv mlvgglfasl gmvaasfcrs iiqvylttgv
      121 itglglalnf qpslimlnry fskrrpmang laaagspvfl calsplgqll qdrygwrggf
      181 lilgglllnc cvcaalmrpl vvtaqpgsgp prpsrrlldl svfrdrgfvl yavaasvmvl
      241 glfvppvfvv syakdlgvpd tkaaflltil gfidifarpa agfvaglgkv rpysvylfsf
      301 smffngladl agstagdygg lvvfciffgi sygmvgalqf evlmaivgth kfssaiglvl
      361 lmeavavlvg ppsggkllda thvymyvfil agaevltssl illlgnffci rkkpkepqpe
      421 vaaaeeeklh kppadsgvdl revehflkae pekngevvht petsv
//
LOCUS       NP_060579                582 aa            linear   PRI 21-NOV-2025
DEFINITION  poly(A) RNA polymerase, mitochondrial precursor [Homo sapiens].
ACCESSION   NP_060579
VERSION     NP_060579.3
DBSOURCE    REFSEQ: accession NM_018109.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Kim,J., Taketomi,T., Yamada,A., Uematsu,Y., Ueda,K., Chiba,T. and
            Tsuruta,F.
  TITLE     USP4 regulates TUT1 ubiquitination status in concert with SART3
  JOURNAL   Biochem Biophys Res Commun 701, 149557 (2024)
   PUBMED   38310689
  REMARK    GeneRIF: USP4 regulates TUT1 ubiquitination status in concert with
            SART3.
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 582)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 582)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 582)
  AUTHORS   Nagaike,T., Suzuki,T., Katoh,T. and Ueda,T.
  TITLE     Human mitochondrial mRNAs are stabilized with polyadenylation
            regulated by mitochondria-specific poly(A) polymerase and
            polynucleotide phosphorylase
  JOURNAL   J Biol Chem 280 (20), 19721-19727 (2005)
   PUBMED   15769737
REFERENCE   8  (residues 1 to 582)
  AUTHORS   Tomecki,R., Dmochowska,A., Gewartowski,K., Dziembowski,A. and
            Stepien,P.P.
  TITLE     Identification of a novel human nuclear-encoded mitochondrial
            poly(A) polymerase
  JOURNAL   Nucleic Acids Res 32 (20), 6001-6014 (2004)
   PUBMED   15547249
  REMARK    GeneRIF: Cloning of a human nuclear-encoded mitochondrial poly(A)
            polymerase (hmtPAP)that has a role in mitochondrial RNA processing.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 582)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   10 (residues 1 to 582)
  AUTHORS   Keller,W. and Martin,G.
  TITLE     Gene regulation: reviving the message
  JOURNAL   Nature 419 (6904), 267-268 (2002)
   PUBMED   12239557
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL161651.13 and AL353796.16.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 12, 2008 this sequence version replaced NP_060579.2.
            
            Summary: The protein encoded by this gene is a member of the DNA
            polymerase type-B-like family. This enzyme synthesizes the 3'
            poly(A) tail of mitochondrial transcripts and plays a role in
            replication-dependent histone mRNA degradation.[provided by RefSeq,
            Jan 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2678712.1,
                                           SRR14038196.569501.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000263063.9/
                                                  ENSP00000263063.3
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p11.23"
     Protein         1..582
                     /product="poly(A) RNA polymerase, mitochondrial precursor"
                     /EC_number="2.7.7.19"
                     /note="TUTase 1; terminal uridylyltransferase 1;
                     polynucleotide adenylyltransferase; PAP-associated
                     domain-containing protein 1"
                     /calculated_mol_wt=62145
     transit_peptide 1..37
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9NVV4.1)"
                     /calculated_mol_wt=4045
     mat_peptide     38..582
                     /product="Poly(A) RNA polymerase, mitochondrial.
                     /id=PRO_0000250689"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVV4.1)"
                     /calculated_mol_wt=62145
     Region          62..131
                     /region_name="RL"
                     /note="RL domain; pfam17797"
                     /db_xref="CDD:465510"
     Site            90
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NVV4.1)"
     Region          140..>493
                     /region_name="TRF4"
                     /note="DNA polymerase sigma [Replication, recombination
                     and repair]; COG5260"
                     /db_xref="CDD:227585"
     Region          206..344
                     /region_name="NT_PAP_TUTase"
                     /note="Nucleotidyltransferase (NT) domain of poly(A)
                     polymerases and terminal uridylyl transferases; cd05402"
                     /db_xref="CDD:143392"
     Site            order(230..232,242..243,245,309..310,312,314,325,332..333,
                     336..337)
                     /site_type="active"
                     /db_xref="CDD:143392"
     Site            order(230,309,312,314,325,332..333)
                     /site_type="active"
                     /note="putative primer-binding pocket [active]"
                     /db_xref="CDD:143392"
     Site            order(243,245,325)
                     /site_type="metal-binding"
                     /note="metal binding triad [ion binding]"
                     /db_xref="CDD:143392"
     CDS             1..582
                     /gene="MTPAP"
                     /gene_synonym="PAPD1; SPAX4; TENT6"
                     /coded_by="NM_018109.4:4..1752"
                     /db_xref="CCDS:CCDS7165.1"
                     /db_xref="GeneID:55149"
                     /db_xref="HGNC:HGNC:25532"
                     /db_xref="MIM:613669"
ORIGIN      
        1 mavpgvgllt rlnlcarrrt rvqrpivrll scpgtvakdl rrdeqpsgsv etgfedkipk
       61 rrfsemqner reqaqrtvli hcpekisenk flkylsqfgp innhffyesf glyavvefcq
      121 kesigslqng thtpstamet aipfrsrffn lklknqtser srvrssnqlp rsnkqlfell
      181 cyaesiddql ntllkefqlt eentklrylt csliedmaaa yfpdcivrpf gssvntfgkl
      241 gcdldmfldl detrnlsahk isgnflmefq vknvpseria tqkilsvlge cldhfgpgcv
      301 gvqkilnarc plvrfshqas gfqcdlttnn rialtssell yiygaldsrv ralvfsvrcw
      361 arahsltssi pgawitnfsl tmmvifflqr rsppilptld slktladaed kcviegnnct
      421 fvrdlsrikp sqntetlell lkeffeyfgn fafdknsini rqgreqnkpd ssplyiqnpf
      481 etslnisknv sqsqlqkfvd laresawilq qedtdrpsis snrpwglvsl llpsapnrks
      541 ftkkksnkfa ietvknlles lkgnrtenft ktsgkrtist qt
//
LOCUS       NP_001138503             414 aa            linear   PRI 21-NOV-2025
DEFINITION  urokinase-type plasminogen activator isoform 2 [Homo sapiens].
ACCESSION   NP_001138503
VERSION     NP_001138503.2
DBSOURCE    REFSEQ: accession NM_001145031.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Li,D., Ding,C., Huang,F., Chang,M., Lu,Z., Li,G., Li,Y., Gao,H. and
            Sun,F.
  TITLE     Bioinformatics Analysis of the Expression and Prognostic Value of
            PLAU Gene in Wilms' Tumor
  JOURNAL   Anticancer Res 44 (9), 3829-3842 (2024)
   PUBMED   39197889
  REMARK    GeneRIF: Bioinformatics Analysis of the Expression and Prognostic
            Value of PLAU Gene in Wilms' Tumor.
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Guo,J., Wang,H., Huang,C., Lai,C., Shang,W., Luo,S. and Chen,L.
  TITLE     PLAU, transcriptionally negatively regulated by GATA6, promotes
            lung squamous carcinoma cell proliferation and migration
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (5), 119744 (2024)
   PUBMED   38702016
  REMARK    GeneRIF: PLAU, transcriptionally negatively regulated by GATA6,
            promotes lung squamous carcinoma cell proliferation and migration.
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Cui,X., Sun,H., Liu,X., Bai,Y., Bai,Y., Cui,Y., Wang,B., Zhang,S.
            and Li,X.
  TITLE     PLAU promotes cell proliferation and migration of head and neck
            cancer via STAT3 signaling pathway
  JOURNAL   Exp Cell Res 438 (2), 114056 (2024)
   PUBMED   38663475
  REMARK    GeneRIF: PLAU promotes cell proliferation and migration of head and
            neck cancer via STAT3 signaling pathway.
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Cetinsoy,O., Anyanwu,I., Krishnanand,H., Natarajan,G.,
            Ramachandran,N., Thomas,A. and Brookes,K.J.
  TITLE     Gene Association Study of the Urokinase Plasminogen Activator and
            Its Receptor Gene in Alzheimer's Disease
  JOURNAL   J Alzheimers Dis 99 (1), 241-250 (2024)
   PUBMED   38669542
  REMARK    GeneRIF: Gene Association Study of the Urokinase Plasminogen
            Activator and Its Receptor Gene in Alzheimer's Disease.
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Mekkawy,A.H., Pourgholami,M.H. and Morris,D.L.
  TITLE     Involvement of urokinase-type plasminogen activator system in
            cancer: an overview
  JOURNAL   Med Res Rev 34 (5), 918-956 (2014)
   PUBMED   24549574
  REMARK    Review article
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Naldini,L., Tamagnone,L., Vigna,E., Sachs,M., Hartmann,G.,
            Birchmeier,W., Daikuhara,Y., Tsubouchi,H., Blasi,F. and
            Comoglio,P.M.
  TITLE     Extracellular proteolytic cleavage by urokinase is required for
            activation of hepatocyte growth factor/scatter factor
  JOURNAL   EMBO J 11 (13), 4825-4833 (1992)
   PUBMED   1334458
REFERENCE   8  (residues 1 to 414)
  AUTHORS   Li,X., Smith,R.A. and Dobson,C.M.
  TITLE     Sequential 1H NMR assignments and secondary structure of the
            kringle domain from urokinase
  JOURNAL   Biochemistry 31 (40), 9562-9571 (1992)
   PUBMED   1327118
REFERENCE   9  (residues 1 to 414)
  AUTHORS   Stephens,R.W., Aumailley,M., Timpl,R., Reisberg,T., Tapiovaara,H.,
            Myohanen,H., Murphy-Ullrich,J. and Vaheri,A.
  TITLE     Urokinase binding to laminin-nidogen. Structural requirements and
            interactions with heparin
  JOURNAL   Eur J Biochem 207 (3), 937-942 (1992)
   PUBMED   1499567
REFERENCE   10 (residues 1 to 414)
  AUTHORS   Moroi,M. and Aoki,N.
  TITLE     Isolation and characterization of alpha2-plasmin inhibitor from
            human plasma. A novel proteinase inhibitor which inhibits
            activator-induced clot lysis
  JOURNAL   J Biol Chem 251 (19), 5956-5965 (1976)
   PUBMED   134998
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC349055.1, AK298560.1,
            AL596247.22, BC013575.2 and AB208961.1.
            
            On Jan 1, 2020 this sequence version replaced NP_001138503.1.
            
            Summary: This gene encodes a secreted serine protease that converts
            plasminogen to plasmin. The encoded preproprotein is
            proteolytically processed to generate A and B polypeptide chains.
            These chains associate via a single disulfide bond to form the
            catalytically inactive high molecular weight urokinase-type
            plasminogen activator (HMW-uPA). HMW-uPA can be further processed
            into the catalytically active low molecular weight urokinase-type
            plasminogen activator (LMW-uPA). This low molecular weight form
            does not bind to the urokinase-type plasminogen activator receptor.
            Mutations in this gene may be associated with Quebec platelet
            disorder and late-onset Alzheimer's disease. Alternative splicing
            results in multiple transcript variants, at least one of which
            encodes an isoform that is proteolytically processed. [provided by
            RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at an
            alternate start site compared to variant 1. The encoded isoform (2)
            has a shorter and distinct N-terminus, and lacks a predicted signal
            peptide compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK298560.1, SRR14372080.2477471.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146982, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..414
                     /product="urokinase-type plasminogen activator isoform 2"
                     /EC_number="3.4.21.73"
                     /note="plasminogen activator, urinary; U-plasminogen
                     activator; urokinase-type plasminogen activator"
                     /calculated_mol_wt=46794
     Region          50..135
                     /region_name="KR"
                     /note="Kringle domain; Kringle domains are believed to
                     play a role in binding mediators, such as peptides, other
                     proteins, membranes, or phospholipids. They are autonomous
                     structural domains, found in a varying number of copies,
                     in blood clotting and...; cd00108"
                     /db_xref="CDD:238056"
     Site            62
                     /site_type="active"
                     /note="putative domain interaction site [active]"
                     /db_xref="CDD:238056"
     Site            order(77,87,115,117,126)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Region          162..405
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            162
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(207,258,359)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            order(353,378,380)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..414
                     /gene="PLAU"
                     /gene_synonym="ATF; BDPLT5; QPD; u-PA; UPA; URK"
                     /coded_by="NM_001145031.3:455..1699"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44442.1"
                     /db_xref="GeneID:5328"
                     /db_xref="HGNC:HGNC:9052"
                     /db_xref="MIM:191840"
ORIGIN      
        1 mvfhlrtrye qancdclngg tcvsnkyfsn ihwcncpkkf ggqhceidks ktcyegnghf
       61 yrgkastdtm grpclpwnsa tvlqqtyhah rsdalqlglg khnycrnpdn rrrpwcyvqv
      121 glkllvqecm vhdcadgkkp ssppeelkfq cgqktlrprf kiiggeftti enqpwfaaiy
      181 rrhrggsvty vcggslispc wvisathcfi dypkkedyiv ylgrsrlnsn tqgemkfeve
      241 nlilhkdysa dtlahhndia llkirskegr caqpsrtiqt iclpsmyndp qfgtsceitg
      301 fgkenstdyl ypeqlkmtvv klishrecqq phyygsevtt kmlcaadpqw ktdscqgdsg
      361 gplvcslqgr mtltgivswg rgcalkdkpg vytrvshflp wirshtkeen glal
//
LOCUS       NP_000064                182 aa            linear   PRI 21-NOV-2025
DEFINITION  T-cell surface glycoprotein CD3 gamma chain precursor [Homo
            sapiens].
ACCESSION   NP_000064
VERSION     NP_000064.1
DBSOURCE    REFSEQ: accession NM_000073.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Li,N., Ren,P., Wang,J., Zhu,X., Qiao,X., Zeng,Z., Ye,T., Wang,S.,
            Meng,Z., Gan,H., Liu,S., Sun,Y., Zhu,X., Dou,G. and Gu,R.
  TITLE     Immune-Related Molecules CD3G and FERMT3: Novel Biomarkers
            Associated with Sepsis
  JOURNAL   Int J Mol Sci 25 (2), 749 (2024)
   PUBMED   38255822
  REMARK    GeneRIF: Immune-Related Molecules CD3G and FERMT3: Novel Biomarkers
            Associated with Sepsis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Dong,D., Zheng,L., Lin,J., Zhang,B., Zhu,Y., Li,N., Xie,S.,
            Wang,Y., Gao,N. and Huang,Z.
  TITLE     Structural basis of assembly of the human T cell receptor-CD3
            complex
  JOURNAL   Nature 573 (7775), 546-552 (2019)
   PUBMED   31461748
  REMARK    Erratum:[Nature. 2021 Feb;590(7846):E52. doi:
            10.1038/s41586-021-03245-4. PMID: 33526937]
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Muro,R., Takayanagi,H. and Nitta,T.
  TITLE     T cell receptor signaling for gammadeltaT cell development
  JOURNAL   Inflamm Regen 39, 6 (2019)
   PUBMED   30976362
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Gaud,G., Lesourne,R. and Love,P.E.
  TITLE     Regulatory mechanisms in T cell receptor signalling
  JOURNAL   Nat Rev Immunol 18 (8), 485-497 (2018)
   PUBMED   29789755
  REMARK    Review article
REFERENCE   6  (residues 1 to 182)
  AUTHORS   Lanier,L.L., Chang,C., Spits,H. and Phillips,J.H.
  TITLE     Expression of cytoplasmic CD3 epsilon proteins in activated human
            adult natural killer (NK) cells and CD3 gamma, delta, epsilon
            complexes in fetal NK cells. Implications for the relationship of
            NK and T lymphocytes
  JOURNAL   J Immunol 149 (6), 1876-1880 (1992)
   PUBMED   1387664
REFERENCE   7  (residues 1 to 182)
  AUTHORS   Arnaiz-Villena,A., Timon,M., Corell,A., Perez-Aciego,P.,
            Martin-Villa,J.M. and Regueiro,J.R.
  TITLE     Brief report: primary immunodeficiency caused by mutations in the
            gene encoding the CD3-gamma subunit of the T-lymphocyte receptor
  JOURNAL   N Engl J Med 327 (8), 529-533 (1992)
   PUBMED   1635567
REFERENCE   8  (residues 1 to 182)
  AUTHORS   Cenciarelli,C., Hou,D., Hsu,K.C., Rellahan,B.L., Wiest,D.L.,
            Smith,H.T., Fried,V.A. and Weissman,A.M.
  TITLE     Activation-induced ubiquitination of the T cell antigen receptor
  JOURNAL   Science 257 (5071), 795-797 (1992)
   PUBMED   1323144
REFERENCE   9  (residues 1 to 182)
  AUTHORS   Letourneur,F. and Klausner,R.D.
  TITLE     A novel di-leucine motif and a tyrosine-based motif independently
            mediate lysosomal targeting and endocytosis of CD3 chains
  JOURNAL   Cell 69 (7), 1143-1157 (1992)
   PUBMED   1535555
REFERENCE   10 (residues 1 to 182)
  AUTHORS   Arnaiz-Villena,A., Perez-Aciego,P., Ballestin,C., Sotelo,T.,
            Perez-Seoane,C., Martin-Villa,J.M. and Regueiro,J.R.
  TITLE     Biochemical basis of a novel T lymphocyte receptor immunodeficiency
            by immunohistochemistry. A possible CD3 gamma abnormality
  JOURNAL   Lab Invest 64 (5), 675-681 (1991)
   PUBMED   1709425
  REMARK    GeneRIF: Protein level controlled by OTHER KINASES PROTEINS
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC378393.1, X04145.1,
            DB116263.1, AK310622.1 and AP001582.4.
            
            Summary: The protein encoded by this gene is the CD3-gamma
            polypeptide, which together with CD3-epsilon, -delta and -zeta, and
            the T-cell receptor alpha/beta and gamma/delta heterodimers, forms
            the T-cell receptor-CD3 complex. This complex plays an important
            role in coupling antigen recognition to several intracellular
            signal-transduction pathways. The genes encoding the epsilon, gamma
            and delta polypeptides are located in the same cluster on
            chromosome 11. Defects in this gene are associated with T cell
            immunodeficiency. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3282162.1,
                                           SRR14038196.1560833.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000532917.3/ ENSP00000431445.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..182
                     /product="T-cell surface glycoprotein CD3 gamma chain
                     precursor"
                     /note="CD3g antigen, gamma polypeptide (TiT3 complex);
                     T-cell receptor T3 gamma chain; T-cell antigen receptor
                     complex, gamma subunit of T3; T-cell surface glycoprotein
                     CD3 gamma chain; CD3g molecule, epsilon (CD3-TCR complex);
                     CD3g molecule, gamma (CD3-TCR complex)"
                     /calculated_mol_wt=18222
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2266
     mat_peptide     23..182
                     /product="T-cell surface glycoprotein CD3 gamma chain.
                     /id=PRO_0000014615"
                     /note="propagated from UniProtKB/Swiss-Prot (P09693.1)"
                     /calculated_mol_wt=18222
     Region          35..105
                     /region_name="IgC1_CD3_gamma_delta"
                     /note="Immunoglobulin (Ig)-like domain of Cluster of
                     Differentiation (CD) 3 gamma and delta chains; member of
                     the C1-set of IgSF domains; cd07691"
                     /db_xref="CDD:409488"
     Site            order(35..36,38,84,96..98,100..104)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409488"
     Region          35..39
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409488"
     Region          41..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409488"
     Region          52..56
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409488"
     Site            52
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:8636209; propagated from
                     UniProtKB/Swiss-Prot (P09693.1)"
     Region          58..60
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409488"
     Region          62..65
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409488"
     Region          70..76
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409488"
     Region          82..88
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409488"
     Site            92
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:8636209; propagated from
                     UniProtKB/Swiss-Prot (P09693.1)"
     Region          94..102
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409488"
     Site            117..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P09693.1)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:2540970,
                     ECO:0000269|PubMed:3112151; propagated from
                     UniProtKB/Swiss-Prot (P09693.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000269|PubMed:2540970,
                     ECO:0000269|PubMed:3112151, ECO:0000269|PubMed:8187769;
                     propagated from UniProtKB/Swiss-Prot (P09693.1)"
     Region          153..154
                     /region_name="Di-leucine motif.
                     /evidence=ECO:0000269|PubMed:8187769"
                     /note="propagated from UniProtKB/Swiss-Prot (P09693.1)"
     Region          157..176
                     /region_name="ITAM"
                     /note="Immunoreceptor tyrosine-based activation motif;
                     pfam02189"
                     /db_xref="CDD:426646"
     CDS             1..182
                     /gene="CD3G"
                     /gene_synonym="CD3-GAMMA; CD3GAMMA; IMD17; T3G"
                     /coded_by="NM_000073.3:81..629"
                     /db_xref="CCDS:CCDS8395.1"
                     /db_xref="GeneID:917"
                     /db_xref="HGNC:HGNC:1675"
                     /db_xref="MIM:186740"
ORIGIN      
        1 meqgkglavl ilaiillqgt laqsikgnhl vkvydyqedg svlltcdaea knitwfkdgk
       61 migfltedkk kwnlgsnakd prgmyqckgs qnkskplqvy yrmcqnciel naatisgflf
      121 aeivsifvla vgvyfiagqd gvrqsrasdk qtllpndqly qplkdreddq yshlqgnqlr
      181 rn
//
LOCUS       NP_001376513             150 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerases I, II, and III subunit RPABC3 isoform
            2 [Homo sapiens].
ACCESSION   NP_001376513
VERSION     NP_001376513.1
DBSOURCE    REFSEQ: accession NM_001389584.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 150)
  AUTHORS   Zhao,D., Liu,W., Chen,K., Wu,Z., Yang,H. and Xu,Y.
  TITLE     Structure of the human RNA polymerase I elongation complex
  JOURNAL   Cell Discov 7 (1), 97 (2021)
   PUBMED   34671025
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 150)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   6  (residues 1 to 150)
  AUTHORS   Kato,H., Sumimoto,H., Pognonec,P., Chen,C.H., Rosen,C.A. and
            Roeder,R.G.
  TITLE     HIV-1 Tat acts as a processivity factor in vitro in conjunction
            with cellular elongation factors
  JOURNAL   Genes Dev 6 (4), 655-666 (1992)
   PUBMED   1559613
REFERENCE   7  (residues 1 to 150)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
REFERENCE   8  (residues 1 to 150)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 150)
  AUTHORS   Southgate,C., Zapp,M.L. and Green,M.R.
  TITLE     Activation of transcription by HIV-1 Tat protein tethered to
            nascent RNA through another protein
  JOURNAL   Nature 345 (6276), 640-642 (1990)
   PUBMED   2190099
REFERENCE   10 (residues 1 to 150)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078797.20.
            
            Summary: The three eukaryotic RNA polymerases are complex
            multisubunit enzymes that play a central role in the transcription
            of nuclear genes. This gene encodes an essential and highly
            conserved subunit of RNA polymerase II that is shared by the other
            two eukaryotic DNA-directed RNA polymerases, I and III. Alternative
            splicing results in multiple transcript variants of this gene.
            [provided by RefSeq, Jul 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI761279.1, SRR14243140.1487577.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..150
                     /product="DNA-directed RNA polymerases I, II, and III
                     subunit RPABC3 isoform 2"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerases I, II, and III subunit
                     RPABC3; RPB8 homolog; DNA-directed RNA polymerase II
                     subunit H; DNA-directed RNA polymerases I, II, and III
                     17.1 kDa polypeptide; polymerase (RNA) II (DNA directed)
                     polypeptide H; polymerase (RNA) II subunit H"
                     /calculated_mol_wt=17012
     Region          2..147
                     /region_name="RPOL8c"
                     /note="RNA polymerase subunit 8; smart00658"
                     /db_xref="CDD:197821"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P52434.4)"
     Region          16..40
                     /region_name="Non-specific ssDNA binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P52434.4)"
     CDS             1..150
                     /gene="POLR2H"
                     /gene_synonym="RPABC3; RPB17; RPB8"
                     /coded_by="NM_001389584.1:387..839"
                     /note="isoform 2 is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS3264.1"
                     /db_xref="GeneID:5437"
                     /db_xref="HGNC:HGNC:9195"
                     /db_xref="MIM:606023"
ORIGIN      
        1 magilfedif dvkdidpegk kfdrvsrlhc esesfkmdli ldvniqiypv dlgdkfrlvi
       61 astlyedgtl ddgeynptdd rpsradqfey vmygkvyrie gdetsteaat rlsayvsygg
      121 llmrlqgdan nlhgfevdsr vyllmkklaf
//
LOCUS       NP_001336012             681 aa            linear   PRI 21-NOV-2025
DEFINITION  TBC1 domain family member 5 isoform d [Homo sapiens].
ACCESSION   NP_001336012 XP_005265672
VERSION     NP_001336012.1
DBSOURCE    REFSEQ: accession NM_001349083.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   3  (residues 1 to 681)
  AUTHORS   Tu,Y.X.I., Sydor,A.M., Coyaud,E., Laurent,E.M.N., Dyer,D.,
            Mellouk,N., St-Germain,J., Vernon,R.M., Forman-Kay,J.D., Li,T.,
            Hua,R., Zhao,K., Ridgway,N.D., Kim,P.K., Raught,B. and Brumell,J.H.
  TITLE     Global Proximity Interactome of the Human Macroautophagy Pathway
  JOURNAL   Autophagy 18 (5), 1174-1186 (2022)
   PUBMED   34524948
REFERENCE   4  (residues 1 to 681)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 681)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 681)
  AUTHORS   Seaman,M.N., Harbour,M.E., Tattersall,D., Read,E. and Bright,N.
  TITLE     Membrane recruitment of the cargo-selective retromer subcomplex is
            catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP
            TBC1D5
  JOURNAL   J Cell Sci 122 (Pt 14), 2371-2382 (2009)
   PUBMED   19531583
  REMARK    GeneRIF: Membrane recruitment of the cargo-selective retromer
            subcomplex VPS35/29/26 is catalysed by the small GTPase Rab7 and
            inhibited by the Rab-GAP TBC1D5.
REFERENCE   7  (residues 1 to 681)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
REFERENCE   8  (residues 1 to 681)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   9  (residues 1 to 681)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 681)
  AUTHORS   Brill,L.M., Salomon,A.R., Ficarro,S.B., Mukherji,M.,
            Stettler-Gill,M. and Peters,E.C.
  TITLE     Robust phosphoproteomic profiling of tyrosine phosphorylation sites
            from human T cells using immobilized metal affinity chromatography
            and tandem mass spectrometry
  JOURNAL   Anal Chem 76 (10), 2763-2772 (2004)
   PUBMED   15144186
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104451.2, AC144531.2, AC090960.3 and AC090644.2.
            
            On Mar 3, 2017 this sequence version replaced XP_005265672.1.
            
            Transcript Variant: This variant (13), as well as variants 12, 14,
            15, and 16, encodes isoform d.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2556431.1,
                                           SRR1803613.239671.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..681
                     /product="TBC1 domain family member 5 isoform d"
                     /calculated_mol_wt=75238
     Region          19..245
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     CDS             1..681
                     /gene="TBC1D5"
                     /coded_by="NM_001349083.2:590..2635"
                     /note="isoform d is encoded by transcript variant 13"
                     /db_xref="GeneID:9779"
                     /db_xref="HGNC:HGNC:19166"
                     /db_xref="MIM:615740"
ORIGIN      
        1 minnplsqde gslwnkffqd kelrsmieqd vkrtfpemqf fqqenvrkil tdvlfcyare
       61 neqllykqgm hellapivfv lhcdhqaflh asesaqpsee mktvlnpeyl ehdayavfsq
      121 lmetaepwfs tfehdgqkgk etlmtpipfa rpqdlgptia ivtkvnqiqd hllkkhdiel
      181 ymhlnrleia pqiyglrwvr llfgrefplq dllvvwdalf adglslglvd yifvamllyi
      241 rdalissnyq tclgllmhyp figdvhslil kalflrdpkr nprpvtyqfh pnldyykarg
      301 adlmnksrtn akgaplnink vsnslinfgr klispamapg saggpvpggn ssssssvvip
      361 trtsaeapsh hlqqqqqqqr lmksesmpvq lnkgdvvtgs daqvsvpvqt ltdlqglssk
      421 nissspsves lpggreftgs ppssatkkds ffsnisrsrs hsktmgrkes eeeleaqisf
      481 lqgqlndlda mckycakvmd thlvniqdvi lqenlekedq ilvslaglkq ikdilkgslr
      541 fnqsqleaee neqitiadnh ycssgqgqgr gqgqsvqmsg aikqassetp gctdrgnsdd
      601 filiskdddg ssargsfsgq aqplrtlrst sgksqapvcs plvfsdplmg pasasssnps
      661 sspdddsskd sgftivspld i
//
LOCUS       NP_001091738             911 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA ligase 4 isoform 1 [Homo sapiens].
ACCESSION   NP_001091738
VERSION     NP_001091738.1
DBSOURCE    REFSEQ: accession NM_001098268.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Bayat,L., Abbasi,S., Balasuriya,N. and Schild-Poulter,C.
  TITLE     Critical residues in the Ku70 von Willebrand A domain mediate Ku
            interaction with the LigIV-XRCC4 complex in non-homologous
            end-joining
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (7), 119815 (2024)
   PUBMED   39151475
  REMARK    GeneRIF: Critical residues in the Ku70 von Willebrand A domain
            mediate Ku interaction with the LigIV-XRCC4 complex in
            non-homologous end-joining.
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Nicolle,R., Boutaud,L., Loeuillet,L., Talhi,N., Grotto,S.,
            Bourgon,N., Feresin,A., Coussement,A., Barrois,M., Beaujard,M.P.,
            Rambaud,T., Razavi,F. and Attie-Bitach,T.
  TITLE     Expanding the phenotypic spectrum of LIG4 pathogenic variations:
            neuro-histopathological description of 4 fetuses with stenosis of
            the aqueduct
  JOURNAL   Eur J Hum Genet 32 (5), 545-549 (2024)
   PUBMED   38351293
  REMARK    GeneRIF: Expanding the phenotypic spectrum of LIG4 pathogenic
            variations: neuro-histopathological description of 4 fetuses with
            stenosis of the aqueduct.
REFERENCE   4  (residues 1 to 911)
  AUTHORS   Deng,Y., Ke,T.W., Yueh,T.C., Chin,Y.T., Wang,Y.C., Hung,Y.C.,
            Mong,M.C., Yang,Y.C., Wu,W.T., Chang,W.S., Gu,J., Bau,D.T. and
            Tsai,C.W.
  TITLE     The Contribution of DNA Ligase 4 Polymorphisms to Colorectal Cancer
  JOURNAL   In Vivo 38 (1), 127-133 (2024)
   PUBMED   38148049
  REMARK    GeneRIF: The Contribution of DNA Ligase 4 Polymorphisms to
            Colorectal Cancer.
REFERENCE   5  (residues 1 to 911)
  AUTHORS   Kumari,N., Antil,H., Kumari,S. and Raghavan,S.C.
  TITLE     Deficiency of ligase IV leads to reduced NHEJ, accumulation of DNA
            damage, and can sensitize cells to cancer therapeutics
  JOURNAL   Genomics 115 (6), 110731 (2023)
   PUBMED   37871849
  REMARK    GeneRIF: Deficiency of ligase IV leads to reduced NHEJ,
            accumulation of DNA damage, and can sensitize cells to cancer
            therapeutics.
REFERENCE   6  (residues 1 to 911)
  AUTHORS   Leon,D.A., Chenet,L., Shkolnikov,V.M., Zakharov,S., Shapiro,J.,
            Rakhmanova,G., Vassin,S. and McKee,M.
  TITLE     Huge variation in Russian mortality rates 1984-94: artefact,
            alcohol, or what?
  JOURNAL   Lancet 350 (9075), 383-388 (1997)
   PUBMED   9259651
REFERENCE   7  (residues 1 to 911)
  AUTHORS   Critchlow,S.E., Bowater,R.P. and Jackson,S.P.
  TITLE     Mammalian DNA double-strand break repair protein XRCC4 interacts
            with DNA ligase IV
  JOURNAL   Curr Biol 7 (8), 588-598 (1997)
   PUBMED   9259561
REFERENCE   8  (residues 1 to 911)
  AUTHORS   Grawunder,U., Wilm,M., Wu,X., Kulesza,P., Wilson,T.E., Mann,M. and
            Lieber,M.R.
  TITLE     Activity of DNA ligase IV stimulated by complex formation with
            XRCC4 protein in mammalian cells
  JOURNAL   Nature 388 (6641), 492-495 (1997)
   PUBMED   9242410
REFERENCE   9  (residues 1 to 911)
  AUTHORS   Robins,P. and Lindahl,T.
  TITLE     DNA ligase IV from HeLa cell nuclei
  JOURNAL   J Biol Chem 271 (39), 24257-24261 (1996)
   PUBMED   8798671
REFERENCE   10 (residues 1 to 911)
  AUTHORS   Wei,Y.F., Robins,P., Carter,K., Caldecott,K., Pappin,D.J., Yu,G.L.,
            Wang,R.P., Shell,B.K., Nash,R.A., Schar,P. et al.
  TITLE     Molecular cloning and expression of human cDNAs encoding a novel
            DNA ligase IV and DNA ligase III, an enzyme active in DNA repair
            and recombination
  JOURNAL   Mol Cell Biol 15 (6), 3206-3216 (1995)
   PUBMED   7760816
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX648833.1 and BC037491.2.
            
            Summary: The protein encoded by this gene is a DNA ligase that
            joins single-strand breaks in a double-stranded polydeoxynucleotide
            in an ATP-dependent reaction. This protein is essential for V(D)J
            recombination and DNA double-strand break (DSB) repair through
            nonhomologous end joining (NHEJ). This protein forms a complex with
            the X-ray repair cross complementing protein 4 (XRCC4), and further
            interacts with the DNA-dependent protein kinase (DNA-PK). Both
            XRCC4 and DNA-PK are known to be required for NHEJ. The crystal
            structure of the complex formed by this protein and XRCC4 has been
            resolved. Defects in this gene are the cause of LIG4 syndrome.
            Alternatively spliced transcript variants encoding the same protein
            have been observed. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. Variants 1-3 and 5-10 all encode the same
            isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.17745.1,
                                           SRR1803614.209931.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q33.3"
     Protein         1..911
                     /product="DNA ligase 4 isoform 1"
                     /EC_number="6.5.1.1"
                     /note="polynucleotide ligase; ligase IV, DNA,
                     ATP-dependent; DNA repair enzyme; DNA joinase;
                     polydeoxyribonucleotide synthase [ATP] 4; sealase; DNA
                     ligase IV"
                     /calculated_mol_wt=103840
     Region          81..602
                     /region_name="dnl1"
                     /note="DNA ligase I, ATP-dependent (dnl1); TIGR00574"
                     /db_xref="CDD:273147"
     Region          610..620
                     /region_name="Required for catalytic activity.
                     /evidence=ECO:0000269|PubMed:23523427"
                     /note="propagated from UniProtKB/Swiss-Prot (P49917.2)"
     Region          658..745
                     /region_name="BRCT_DNA_ligase_IV_rpt1"
                     /note="first BRCT domain of DNA ligase 4 (LIG4) and
                     similar proteins; cd17722"
                     /db_xref="CDD:349354"
     Region          750..783
                     /region_name="DNA_ligase_IV"
                     /note="DNA ligase IV; pfam11411"
                     /db_xref="CDD:463272"
     Region          813..900
                     /region_name="BRCT_DNA_ligase_IV_rpt2"
                     /note="second BRCT domain of DNA ligase 4 (LIG4) and
                     similar proteins; cd17717"
                     /db_xref="CDD:349349"
     Site            order(814,835..837,839..840,843..844,846..847,895,
                     898..899)
                     /site_type="other"
                     /note="XRCC4 interaction site [polypeptide binding]"
                     /db_xref="CDD:349349"
     CDS             1..911
                     /gene="LIG4"
                     /gene_synonym="LIG4S"
                     /coded_by="NM_001098268.2:217..2952"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS9508.1"
                     /db_xref="GeneID:3981"
                     /db_xref="HGNC:HGNC:6601"
                     /db_xref="MIM:601837"
ORIGIN      
        1 maasqtsqtv ashvpfadlc stleriqksk graekirhfr efldswrkfh dalhknhkdv
       61 tdsfypamrl ilpqlererm aygiketmla klyiellnlp rdgkdalkll nyrtptgthg
      121 dagdfamiay fvlkprclqk gsltiqqvnd lldsiasnns akrkdlikks llqlitqssa
      181 leqkwlirmi ikdlklgvsq qtifsvfhnd aaelhnvttd lekvcrqlhd psvglsdisi
      241 tlfsafkpml aaiadiehie kdmkhqsfyi etkldgermq mhkdgdvyky fsrngynytd
      301 qfgasptegs ltpfihnafk adiqicildg emmaynpntq tfmqkgtkfd ikrmvedsdl
      361 qtcycvfdvl mvnnkklghe tlrkryeils siftpipgri eivqktqaht knevidalne
      421 aidkreegim vkqplsiykp dkrgegwlki kpeyvsglmd eldilivggy wgkgsrggmm
      481 shflcavaek pppgekpsvf htlsrvgsgc tmkelydlgl klakywkpfh rkappssilc
      541 gtekpevyie pcnsvivqik aaeivpsdmy ktgctlrfpr iekirddkew hecmtlddle
      601 qlrgkasgkl askhlyiggd depqekkrka apkmkkvigi iehlkapnlt nvnkisnife
      661 dvefcvmsgt dsqpkpdlen riaefggyiv qnpgpdtycv iagsenirvk niilsnkhdv
      721 vkpawllecf ktksfvpwqp rfmihmcpst kehfareydc ygdsyfidtd lnqlkevfsg
      781 iknsneqtpe emasliadle yryswdcspl smfrrhtvyl dsyavindls tknegtrlai
      841 kalelrfhga kvvsclaegv shviigedhs rvadfkafrr tfkrkfkilk eswvtdsidk
      901 celqeenqyl i
//
LOCUS       NP_001333020             347 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 1A isoform 2
            [Homo sapiens].
ACCESSION   NP_001333020
VERSION     NP_001333020.1
DBSOURCE    REFSEQ: accession NM_001346091.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Alam,M.S., Gaida,M.M., Witzel,H.R., Otsuka,S., Abbasi,A.,
            Guerin,T., Abdelmaksoud,A., Wong,N., Cam,M.C., Kozlov,S. and
            Ashwell,J.D.
  TITLE     TNFR1 signaling promotes pancreatic tumor growth by limiting
            dendritic cell number and function
  JOURNAL   Cell Rep Med 5 (9), 101696 (2024)
   PUBMED   39178856
  REMARK    GeneRIF: TNFR1 signaling promotes pancreatic tumor growth by
            limiting dendritic cell number and function.
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Montoya-Buelna,M., Alvarado-Navarro,A., Munoz-Valle,J.F.,
            Lopez-Roa,R.I., Guerrero-Velazquez,C. and Fafutis-Morris,M.
  TITLE     Association of polymorphisms in the TNFA, TNFRSF1A and TNFRSF1B
            genes with lepromatous leprosy in Western Mexican patients
  JOURNAL   J Infect Dev Ctries 18 (5), 770-778 (2024)
   PUBMED   38865403
  REMARK    GeneRIF: Association of polymorphisms in the TNFA, TNFRSF1A and
            TNFRSF1B genes with lepromatous leprosy in Western Mexican
            patients.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 347)
  AUTHORS   da Silva,P.B., Romao-Veiga,M., Ribeiro-Vasques,V.R., Peracoli,J.C.,
            Peracoli,M.T.S. and Amaral,L.M.
  TITLE     Progesterone modulates TNF receptors expression by Jurkat cells
            cultured with plasma from pregnant women with preeclampsia
  JOURNAL   Int Immunopharmacol 130, 111701 (2024)
   PUBMED   38382266
  REMARK    GeneRIF: Progesterone modulates TNF receptors expression by Jurkat
            cells cultured with plasma from pregnant women with preeclampsia.
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Liphaus,B.L., Silva,S.C., Palmeira,P., Silva,C.A.,
            Goldenstein-Schainberg,C. and Carneiro-Sampaio,M.
  TITLE     Reduced expressions of apoptosis-related proteins TRAIL, Bcl-2, and
            TNFR1 in NK cells of juvenile-onset systemic lupus erythematosus
            patients: relations with disease activity, nephritis, and
            neuropsychiatric involvement
  JOURNAL   Front Immunol 15, 1327255 (2024)
   PUBMED   38562920
  REMARK    GeneRIF: Reduced expressions of apoptosis-related proteins TRAIL,
            Bcl-2, and TNFR1 in NK cells of juvenile-onset systemic lupus
            erythematosus patients: relations with disease activity, nephritis,
            and neuropsychiatric involvement.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 347)
  AUTHORS   McDermott,M.F., Aksentijevich,I., Galon,J., McDermott,E.M.,
            Ogunkolade,B.W., Centola,M., Mansfield,E., Gadina,M., Karenko,L.,
            Pettersson,T., McCarthy,J., Frucht,D.M., Aringer,M., Torosyan,Y.,
            Teppo,A.M., Wilson,M., Karaarslan,H.M., Wan,Y., Todd,I., Wood,G.,
            Schlimgen,R., Kumarajeewa,T.R., Cooper,S.M., Vella,J.P., Amos,C.I.,
            Mulley,J., Quane,K.A., Molloy,M.G., Ranki,A., Powell,R.J.,
            Hitman,G.A., O'Shea,J.J. and Kastner,D.L.
  TITLE     Germline mutations in the extracellular domains of the 55 kDa TNF
            receptor, TNFR1, define a family of dominantly inherited
            autoinflammatory syndromes
  JOURNAL   Cell 97 (1), 133-144 (1999)
   PUBMED   10199409
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Deuitch,N., Cudrici,C., Ombrello,A. and Aksentijevich,I.
  TITLE     TNF Receptor-Associated Periodic Fever Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36375008
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Zhang,X.M., Weber,I. and Chen,M.J.
  TITLE     Site-directed mutational analysis of human tumor necrosis
            factor-alpha receptor binding site and structure-functional
            relationship
  JOURNAL   J Biol Chem 267 (33), 24069-24075 (1992)
   PUBMED   1331108
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Fuchs,P., Strehl,S., Dworzak,M., Himmler,A. and Ambros,P.F.
  TITLE     Structure of the human TNF receptor 1 (p60) gene (TNFR1) and
            localization to chromosome 12p13 [corrected]
  JOURNAL   Genomics 13 (1), 219-224 (1992)
   PUBMED   1315717
  REMARK    Erratum:[Genomics 1992 Aug;13(4):1384]
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Derre,J., Kemper,O., Cherif,D., Nophar,Y., Berger,R. and Wallach,D.
  TITLE     The gene for the type 1 tumor necrosis factor receptor (TNF-R1) is
            localized on band 12p13
  JOURNAL   Hum Genet 87 (2), 231-233 (1991)
   PUBMED   1648547
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Belokrylov,G.A. and Zhitnukhin,Iu.L.
  TITLE     [Effect of antibodies to rat and human cerebral cortex and white
            matter on heterologous T- and B-cells]
  JOURNAL   Zh Mikrobiol Epidemiol Immunobiol (9), 66-70 (1976)
   PUBMED   1087798
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JN172914.1 and BC010140.2.
            
            Summary: This gene encodes a member of the TNF receptor superfamily
            of proteins. The encoded receptor is found in membrane-bound and
            soluble forms that interact with membrane-bound and soluble forms,
            respectively, of its ligand, tumor necrosis factor alpha. Binding
            of membrane-bound tumor necrosis factor alpha to the membrane-bound
            receptor induces receptor trimerization and activation, which plays
            a role in cell survival, apoptosis, and inflammation. Proteolytic
            processing of the encoded receptor results in release of the
            soluble form of the receptor, which can interact with free tumor
            necrosis factor alpha to inhibit inflammation. Mutations in this
            gene underlie tumor necrosis factor receptor-associated periodic
            syndrome (TRAPS), characterized by fever, abdominal pain and other
            features. Mutations in this gene may also be associated with
            multiple sclerosis in human patients. [provided by RefSeq, Sep
            2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at a
            downstream start site compared to variant 1. The encoded isoform
            (2) has a shorter N-terminus and lacks a predicted signal peptide
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: JN172914.1, AK298729.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..347
                     /product="tumor necrosis factor receptor superfamily
                     member 1A isoform 2"
                     /note="tumor necrosis factor-alpha receptor; tumor
                     necrosis factor binding protein 1; tumor necrosis factor
                     receptor type 1; TNF-R1; TNF-RI; TNFR-I; tumor necrosis
                     factor receptor superfamily member 1A"
                     /calculated_mol_wt=38520
     Region          <1..67
                     /region_name="TNFRSF"
                     /note="Tumor necrosis factor receptor superfamily
                     (TNFRSF); cl22855"
                     /db_xref="CDD:473981"
     Region          142..>258
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          250..330
                     /region_name="Death_TNFR1"
                     /note="Death domain of Tumor Necrosis Factor Receptor 1;
                     cd08313"
                     /db_xref="CDD:176729"
     CDS             1..347
                     /gene="TNFRSF1A"
                     /gene_synonym="CD120a; FPF; p55; p55-R; p60; TBP1; TNF-R;
                     TNF-R-I; TNF-R55; TNFAR; TNFR1; TNFR55; TNFR60"
                     /coded_by="NM_001346091.2:433..1476"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:7132"
                     /db_xref="HGNC:HGNC:11916"
                     /db_xref="MIM:191190"
ORIGIN      
        1 mgqveissct vdrdtvcgcr knqyrhywse nlfqcfncsl clngtvhlsc qekqntvctc
       61 hagfflrene cvscsnckks lectklclpq ienvkgteds gttvllplvi ffglcllsll
      121 figlmyryqr wksklysivc gkstpekege legtttkpla pnpsfsptpg ftptlgfspv
      181 psstftssst ytpgdcpnfa aprrevappy qgadpilata lasdpipnpl qkwedsahkp
      241 qsldtddpat lyavvenvpp lrwkefvrrl glsdheidrl elqngrclre aqysmlatwr
      301 rrtprreatl ellgrvlrdm dllgcledie ealcgpaalp papsllr
//
LOCUS       NP_821070                281 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A activator isoform d [Homo
            sapiens].
ACCESSION   NP_821070
VERSION     NP_821070.1
DBSOURCE    REFSEQ: accession NM_178003.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Crespo,J.R., Martin-Martin,N., Garcia-Longarte,S.,
            Corres-Mendizabal,J., Carlevaris,O., Astobiza,I., Zabala-Letona,A.,
            Guiu,M., Azkargorta,M., Gonzalez-Lopez,M., Macias-Camara,N.,
            Doan,P., Elortza,F., Mendizabal,I., Westermarck,J., Gomis,R.R.,
            Ercilla,A. and Carracedo,A.
  TITLE     The PP2A regulator IER5L supports prostate cancer progression
  JOURNAL   Cell Death Dis 15 (7), 514 (2024)
   PUBMED   39025841
  REMARK    GeneRIF: The PP2A regulator IER5L supports prostate cancer
            progression.
            Erratum:[Cell Death Dis. 2025 Jul 22;16(1):545. doi:
            10.1038/s41419-025-07802-x. PMID: 40695780]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Wasserman,J.S., Faezov,B., Patel,K.R., Kurimchak,A.M.,
            Palacio,S.M., Glass,D.J., Fowle,H., McEwan,B.C., Xu,Q., Zhao,Z.,
            Cressey,L., Johnson,N., Duncan,J.S., Kettenbach,A.N., Dunbrack,R.L.
            Jr. and Grana,X.
  TITLE     FAM122A ensures cell cycle interphase progression and checkpoint
            control by inhibiting B55alpha/PP2A through helical motifs
  JOURNAL   Nat Commun 15 (1), 5776 (2024)
   PUBMED   38982062
  REMARK    GeneRIF: FAM122A ensures cell cycle interphase progression and
            checkpoint control by inhibiting B55alpha/PP2A through helical
            motifs.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Ando,S., Tanaka,K., Matsumoto,M., Oyama,Y., Tomabechi,Y.,
            Yamagata,A., Shirouzu,M., Nakagawa,R., Okimoto,N., Taiji,M.,
            Sato,K. and Ohama,T.
  TITLE     The luciferase-based in vivo protein-protein interaction assay
            revealed that CHK1 promotes PP2A and PME-1 interaction
  JOURNAL   J Biol Chem 300 (5), 107277 (2024)
   PUBMED   38588804
  REMARK    GeneRIF: The luciferase-based in vivo protein-protein interaction
            assay revealed that CHK1 promotes PP2A and PME-1 interaction.
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Wachter,F., Nowak,R.P., Ficarro,S., Marto,J. and Fischer,E.S.
  TITLE     Structural characterization of methylation-independent PP2A
            assembly guides alphafold2Multimer prediction of family-wide PP2A
            complexes
  JOURNAL   J Biol Chem 300 (5), 107268 (2024)
   PUBMED   38582449
  REMARK    GeneRIF: Structural characterization of methylation-independent
            PP2A assembly guides alphafold2Multimer prediction of family-wide
            PP2A complexes.
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Okamoto,K., Kamibayashi,C., Serrano,M., Prives,C., Mumby,M.C. and
            Beach,D.
  TITLE     p53-dependent association between cyclin G and the B' subunit of
            protein phosphatase 2A
  JOURNAL   Mol Cell Biol 16 (11), 6593-6602 (1996)
   PUBMED   8887688
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Van Hoof,C., Aly,M.S., Garcia,A., Cayla,X., Cassiman,J.J.,
            Merlevede,W. and Goris,J.
  TITLE     Structure and chromosomal localization of the human gene of the
            phosphotyrosyl phosphatase activator (PTPA) of protein phosphatase
            2A
  JOURNAL   Genomics 28 (2), 261-272 (1995)
   PUBMED   8530035
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Turowski,P., Fernandez,A., Favre,B., Lamb,N.J. and Hemmings,B.A.
  TITLE     Differential methylation and altered conformation of cytoplasmic
            and nuclear forms of protein phosphatase 2A during cell cycle
            progression
  JOURNAL   J Cell Biol 129 (2), 397-410 (1995)
   PUBMED   7721943
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Cayla,X., Van Hoof,C., Bosch,M., Waelkens,E., Vandekerckhove,J.,
            Peeters,B., Merlevede,W. and Goris,J.
  TITLE     Molecular cloning, expression, and characterization of PTPA, a
            protein that activates the tyrosyl phosphatase activity of protein
            phosphatase 2A
  JOURNAL   J Biol Chem 269 (22), 15668-15675 (1994)
   PUBMED   8195217
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Jakes,S., Mellgren,R.L. and Schlender,K.K.
  TITLE     Isolation and characterization of an inhibitor-sensitive and a
            polycation-stimulated protein phosphatase from rat liver nuclei
  JOURNAL   Biochim Biophys Acta 888 (1), 135-142 (1986)
   PUBMED   3017441
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158151.16.
            
            Summary: Protein phosphatase 2A is one of the four major Ser/Thr
            phosphatases and is implicated in the negative control of cell
            growth and division. Protein phosphatase 2A holoenzymes are
            heterotrimeric proteins composed of a structural subunit A, a
            catalytic subunit C, and a regulatory subunit B. The regulatory
            subunit is encoded by a diverse set of genes that have been grouped
            into the B/PR55, B'/PR61, and B''/PR72 families. These different
            regulatory subunits confer distinct enzymatic specificities and
            intracellular localizations to the holozenzyme. The product of this
            gene belongs to the B' family. This gene encodes a specific
            phosphotyrosyl phosphatase activator of the dimeric form of protein
            phosphatase 2A. Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (5) lacks an in-frame segment of
            the coding region, compared to variant 1. It encodes a shorter
            protein (isoform d), also known as isoform epsilon, that is missing
            an internal segment compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.438203.1,
                                           SRR3476690.132932.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..281
                     /product="serine/threonine-protein phosphatase 2A
                     activator isoform d"
                     /EC_number="5.2.1.8"
                     /note="protein phosphatase 2A, regulatory subunit B' (PR
                     53); PP2A phosphatase activator; phosphotyrosyl
                     phosphatase activator; serine/threonine-protein
                     phosphatase 2A regulatory subunit B'; protein phosphatase
                     2A regulatory subunit 4; protein phosphatase 2 regulatory
                     subunit 4; protein phosphatase 2A activator, regulatory
                     subunit 4"
                     /calculated_mol_wt=31728
     Region          26..275
                     /region_name="PTPA"
                     /note="Phosphotyrosyl phosphate activator (PTPA) protein;
                     pfam03095"
                     /db_xref="CDD:460802"
     Site            order(106,108,110..113,161..162,171..173,175,236,239,245,
                     249,252,256,260,262..263,265..266)
                     /site_type="active"
                     /note="putative interaction site [active]"
                     /db_xref="CDD:239754"
     Site            order(106,108,110..113,162..164,262..263,265..266)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:239754"
     Site            order(106,158..159,161,164..165,167,173,221,223..224,228,
                     265)
                     /site_type="other"
                     /note="peptide-induced dimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:239754"
     Site            order(167..168,231..232,235..236,239,248..249,259..262)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:239754"
     Site            order(167,228,239,248,252,260)
                     /site_type="other"
                     /note="putative PP2A binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:239754"
     CDS             1..281
                     /gene="PTPA"
                     /gene_synonym="PARK25; PP2A; PPP2R4; PR53"
                     /coded_by="NM_178003.3:187..1032"
                     /note="isoform d is encoded by transcript variant 5"
                     /db_xref="GeneID:5524"
                     /db_xref="HGNC:HGNC:9308"
                     /db_xref="MIM:600756"
ORIGIN      
        1 maegerqppp dsseeappat qnfiipkkei htvpdmgkwk rsqayadyig filtlnegvk
       61 gkkltfeyrv seeaenlvat vvpthlaaav pevavylkes vgnstridyg tgheaafaaf
      121 lcclckigvl rvddqiaivf kvfnrylevm rklqktyrme pagsqgvwgl ddfqflpfiw
      181 gssqlidhpy leprhfvdek avnenhkdym flecilfite mktgpfaehs nqlwnisavp
      241 swskvnqgli rmykaeclek fpviqhfkfg sllpihpvts g
//
LOCUS       NP_001387145            1168 aa            linear   PRI 21-NOV-2025
DEFINITION  protein transport protein Sec31A isoform 27 [Homo sapiens].
ACCESSION   NP_001387145
VERSION     NP_001387145.1
DBSOURCE    REFSEQ: accession NM_001400216.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1168)
  AUTHORS   Tobias,E.S., Lucas-Herald,A.K., Sagar,D., Montezano,A.C.,
            Rios,F.J., De Lucca Camargo,L., Hamilton,G., Gazdagh,G.,
            Diver,L.A., Williams,N., Herzyk,P., Touyz,R.M., Greenfield,A.,
            McGowan,R. and Ahmed,S.F.
  TITLE     SEC31A may be associated with pituitary hormone deficiency and
            gonadal dysgenesis
  JOURNAL   Endocrine 84 (2), 345-349 (2024)
   PUBMED   38400880
  REMARK    GeneRIF: SEC31A may be associated with pituitary hormone deficiency
            and gonadal dysgenesis.
REFERENCE   2  (residues 1 to 1168)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1168)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1168)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1168)
  AUTHORS   Jin,L., Pahuja,K.B., Wickliffe,K.E., Gorur,A., Baumgartel,C.,
            Schekman,R. and Rape,M.
  TITLE     Ubiquitin-dependent regulation of COPII coat size and function
  JOURNAL   Nature 482 (7386), 495-500 (2012)
   PUBMED   22358839
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1168)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1168)
  AUTHORS   Kim,J.H., Hong,J.A., Pih,K.T. and Hwang,I.
  TITLE     Identification and isolation of differentially expressed genes in
            osmotically stressed human oral keratinocytes
  JOURNAL   Arch Oral Biol 46 (4), 335-341 (2001)
   PUBMED   11269867
REFERENCE   8  (residues 1 to 1168)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 1168)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   10 (residues 1 to 1168)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021105.13 and AC108469.5.
            
            Summary: The protein encoded by this gene shares similarity with
            the yeast Sec31 protein, and is a component of the outer layer of
            the coat protein complex II (COPII). The encoded protein is
            involved in vesicle budding from the endoplasmic reticulum (ER) and
            contains multiple WD repeats near the N-terminus and a proline-rich
            region in the C-terminal half. It associates with the protein
            encoded by the SEC13 homolog, nuclear pore and COPII coat complex
            component (SEC13), and is required for ER-Golgi transport.
            Monoubiquitylation of this protein by CUL3-KLHL12 was found to
            regulate the size of COPII coats to accommodate unusually shaped
            cargo. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.274183.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1168
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..1168
                     /product="protein transport protein Sec31A isoform 27"
                     /note="yeast Sec31p homolog; protein transport protein
                     Sec31A; web1-like protein; SEC31 homolog A, COPII coat
                     complex component; SEC31-related protein A; SEC31-like
                     protein 1; SEC31 homolog A, COPII coating complex
                     component"
                     /calculated_mol_wt=127160
     Region          13..332
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(26,40,46..47,52..53,91,95,101..102,117,121,139,144,
                     150..151,164,185,190,196..197,209..210,231,235,244..245,
                     258..259,277,282,288..289,301..302,320,325,331..332)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          70..119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          125..162
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          172..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          263..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          306..331
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <560..>683
                     /region_name="ACE1-Sec16-like"
                     /note="Ancestral coatomer element 1 (ACE1) of COPII coat
                     complex assembly protein Sec16; cl14807"
                     /db_xref="CDD:449359"
     Site            order(561..565,567,569,580,582,583..584,586..587,591,597,
                     605,617,620,645..646)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187750"
     Region          890..>1088
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     CDS             1..1168
                     /gene="SEC31A"
                     /gene_synonym="ABP125; ABP130; HPBKS; HSPC275; HSPC334;
                     NEDSOSB; SEC31L1"
                     /coded_by="NM_001400216.1:71..3577"
                     /note="isoform 27 is encoded by transcript variant 50"
                     /db_xref="GeneID:22872"
                     /db_xref="HGNC:HGNC:17052"
                     /db_xref="MIM:610257"
ORIGIN      
        1 mklkevdrta mqawspaqnh piylatgtsa qqldatfstn asleifeldl sdpsldmksc
       61 atfssshryh kliwgpykmd skgdvsgvli aggengniil ydpskiiagd kevviaqndk
      121 htgpvraldv nifqtnlvas ganeseiyiw dlnnfatpmt pgaktqpped isciawnrqv
      181 qhilasasps gratvwdlrk nepiikvsdh snrmhcsgla whpdvatqmv laseddrlpv
      241 iqmwdlrfas splrvlenha rgilaiawsm adpelllscg kdakilcsnp ntgevlyelp
      301 tntqwcfdiq wcprnpavls aasfdgrisv ysimggstdg lrqkqvdkls ssfgnldpfg
      361 tgqplpplqi pqqtaqhsiv lplkkppkwi rrpvgasfsf ggklvtfenv rmpshqgaeq
      421 qqqqhhvfis qvvtekefls rsdqlqqavq sqgfinycqk kidasqtefe knvwsflkvn
      481 feddsrgkyl ellgyrkedl gkkalkdsdq vaqsdgeesp aaeeqllgeh ikeekeesef
      541 lpssggtfni svsgdidgli tqalltgnfe savdlclhdn rmadaiilai aggqellart
      601 qkkyfaksqs kitrlitavv mknwkeives cdlknwreal aavltyakpd efsalcdllg
      661 trlenegdsl lqtqaclcyi cagnveklva cwtkaqdgsh plslqdliek vvilrkavql
      721 tqamdtstvg vllaakmsqy anllaaqgsi aaalaflpdn tnqpnimqlr drlcraqgep
      781 vaghespkip yekqqlpkgr pgpvaghhqm prvqtqqyyp hgenppppgf imhgnvnpna
      841 agqlptspgh mhtqvppypq pqpyqpaqpy pfgtggsamy rpqqpvappt snaypntpyi
      901 ssassytgqs qlyaaqhqas sptsspatsf ppppssgasf qhggpgapps ssayalppgt
      961 tgpqngwndp palnrvpkkk kmpenfmppv pitspimnpl gdpqsqmlqq qpsapvplss
     1021 qssfpqphlp ggqpfhgvqq plgqtgmpps fskpniegap gapigntfqh vqslptkkit
     1081 kkpipdehli lkttfedliq rclssatdpl sptitsglhn iarsietrny segltmhthi
     1141 vstsnfsets afmpvlkvvl tqanklgv
//
LOCUS       NP_001186791             415 aa            linear   PRI 21-NOV-2025
DEFINITION  voltage-gated potassium channel subunit beta-2 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001186791
VERSION     NP_001186791.1
DBSOURCE    REFSEQ: accession NM_001199862.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Lyu,Y., Wang,Q., Liang,J., Zhang,L. and Zhang,H.
  TITLE     The Ion Channel Gene KCNAB2 Is Associated with Poor Prognosis and
            Loss of Immune Infiltration in Lung Adenocarcinoma
  JOURNAL   Cells 11 (21), 3438 (2022)
   PUBMED   36359834
  REMARK    GeneRIF: The Ion Channel Gene KCNAB2 Is Associated with Poor
            Prognosis and Loss of Immune Infiltration in Lung Adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Ashton,C., Rhie,S.K., Carmichael,J.D. and Zada,G.
  TITLE     Role of KCNAB2 expression in modulating hormone secretion in
            somatotroph pituitary adenoma
  JOURNAL   J Neurosurg 134 (3), 787-793 (2020)
   PUBMED   32109873
  REMARK    GeneRIF: Role of KCNAB2 expression in modulating hormone secretion
            in somatotroph pituitary adenoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Kaab,S., Dixon,J., Duc,J., Ashen,D., Nabauer,M., Beuckelmann,D.J.,
            Steinbeck,G., McKinnon,D. and Tomaselli,G.F.
  TITLE     Molecular basis of transient outward potassium current
            downregulation in human heart failure: a decrease in Kv4.3 mRNA
            correlates with a reduction in current density
  JOURNAL   Circulation 98 (14), 1383-1393 (1998)
   PUBMED   9760292
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Nakahira,K., Shi,G., Rhodes,K.J. and Trimmer,J.S.
  TITLE     Selective interaction of voltage-gated K+ channel beta-subunits
            with alpha-subunits
  JOURNAL   J Biol Chem 271 (12), 7084-7089 (1996)
   PUBMED   8636142
REFERENCE   8  (residues 1 to 415)
  AUTHORS   Schultz,D., Litt,M., Smith,L., Thayer,M. and McCormack,K.
  TITLE     Localization of two potassium channel beta subunit genes, KCNA1B
            and KCNA2B
  JOURNAL   Genomics 31 (3), 389-391 (1996)
   PUBMED   8838324
REFERENCE   9  (residues 1 to 415)
  AUTHORS   McCormack,K., McCormack,T., Tanouye,M., Rudy,B. and Stuhmer,W.
  TITLE     Alternative splicing of the human Shaker K+ channel beta 1 gene and
            functional expression of the beta 2 gene product
  JOURNAL   FEBS Lett 370 (1-2), 32-36 (1995)
   PUBMED   7649300
REFERENCE   10 (residues 1 to 415)
  AUTHORS   McCormack,T. and McCormack,K.
  TITLE     Shaker K+ channel beta subunits belong to an NAD(P)H-dependent
            oxidoreductase superfamily
  JOURNAL   Cell 79 (7), 1133-1135 (1994)
   PUBMED   8001150
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL035406.25, AK131252.1 and
            AW327942.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Voltage-gated potassium (Kv) channels represent the most
            complex class of voltage-gated ion channels from both functional
            and structural standpoints. Their diverse functions include
            regulating neurotransmitter release, heart rate, insulin secretion,
            neuronal excitability, epithelial electrolyte transport, smooth
            muscle contraction, and cell volume. Four sequence-related
            potassium channel genes - shaker, shaw, shab, and shal - have been
            identified in Drosophila, and each has been shown to have human
            homolog(s). This gene encodes a member of the potassium channel,
            voltage-gated, shaker-related subfamily. This member is one of the
            beta subunits, which are auxiliary proteins associating with
            functional Kv-alpha subunits. This member alters functional
            properties of the KCNA4 gene product. Alternative splicing of this
            gene results in multiple transcript variants encoding distinct
            isoforms. [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (5) lacks three exons from the 5'
            end and contains two alternate 5' exons and an additional internal
            in-frame exon, as compared to variant 1. The resulting isoform (3)
            has a longer and distinct N-terminus and an additional internal
            segment, as compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK131252.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378083.8/ ENSP00000367323.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.31"
     Protein         1..415
                     /product="voltage-gated potassium channel subunit beta-2
                     isoform 3"
                     /note="K(+) channel subunit beta-2; potassium
                     voltage-gated channel, shaker-related subfamily, beta
                     member 2; potassium channel, voltage gated subfamily A
                     regulatory beta subunit 2"
                     /calculated_mol_wt=46396
     Region          71..395
                     /region_name="Aldo_ket_red_shaker"
                     /note="Shaker potassium channel beta subunit (AKR6A)
                     family of aldo-keto reductase (AKR); cd19141"
                     /db_xref="CDD:381367"
     Site            order(88..90,96,118,122..123,151,154,162,191,236..237,262,
                     291..297,300,302,310..312,352,369..373,377,380..381)
                     /site_type="active"
                     /db_xref="CDD:381367"
     Site            order(118,123,151,191)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381367"
     CDS             1..415
                     /gene="KCNAB2"
                     /gene_synonym="AKR6A5; HKvbeta2; HKvbeta2.1; HKvbeta2.2;
                     KCNA2B; KV-BETA-2"
                     /coded_by="NM_001199862.2:323..1570"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS55570.1"
                     /db_xref="GeneID:8514"
                     /db_xref="HGNC:HGNC:6229"
                     /db_xref="MIM:601142"
ORIGIN      
        1 mlsmtysesl rsvssrchse walhpvrqtd tlelqrlrev raaaqarnme sflrmhglsl
       61 dgctaqrtgm kyrnlgksgl rvsclglgtw vtfggqitde maeqlmtlay dnginlfdta
      121 evyaagkaev vlgniikkkg wrrsslvitt kifwggkaet erglsrkhii eglkaslerl
      181 qleyvdvvfa nrpdpntpme gdpfsssksr tfiieetvra mthvinqgma mywgtsrwss
      241 meimeaysva rqfnltppic eqaeyhmfqr ekvevqlpel fhkigvgamt wsplacgivs
      301 gkydsgippy sraslkgyqw lkdkilseeg rrqqaklkel qaiaerlgct lpqlaiawcl
      361 rnegvssvll gasnadqlme nigaiqvlpk lsssiiheid silgnkpysk kdyrs
//
LOCUS       NP_001362212             564 aa            linear   PRI 21-NOV-2025
DEFINITION  complement factor I isoform 9 preproprotein [Homo sapiens].
ACCESSION   NP_001362212
VERSION     NP_001362212.1
DBSOURCE    REFSEQ: accession NM_001375283.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Moreno,R. and Broderick,L.
  TITLE     Complement factor I deficiency: Diverse phenotypes
  JOURNAL   J Allergy Clin Immunol 156 (2), 305-307 (2025)
   PUBMED   40127737
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Schwotzer,N., Fakhouri,F., Martins,P.V., Delmas,Y., Caillard,S.,
            Zuber,J., Moranne,O., Mesnard,L., Fremeaux-Bacchi,V. and
            El-Sissy,C.
  TITLE     Hot Spot of Complement Factor I Rare Variant p.Ile357Met in
            Patients With Hemolytic Uremic Syndrome
  JOURNAL   Am J Kidney Dis 84 (2), 244-249 (2024)
   PUBMED   38423159
  REMARK    GeneRIF: Hot Spot of Complement Factor I Rare Variant p.Ile357Met
            in Patients With Hemolytic Uremic Syndrome.
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Felberg,A., Bienkowski,M., Stokowy,T., Myszczynski,K.,
            Polakiewicz,Z., Kitowska,K., Sadej,R., Mohlin,F., Kuzniewska,A.,
            Kowalska,D., Stasilojc,G., Jongerius,I., Spaapen,R.,
            Mesa-Guzman,M., Montuenga,L.M., Blom,A.M., Pio,R. and Okroj,M.
  TITLE     Elevated expression of complement factor I in lung cancer cells
            associates with shorter survival-Potentially via non-canonical
            mechanism
  JOURNAL   Transl Res 269, 1-13 (2024)
   PUBMED   38395390
  REMARK    GeneRIF: Elevated expression of complement factor I in lung cancer
            cells associates with shorter survival-Potentially via
            non-canonical mechanism.
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Massey,V., Nguyen,C.E., Francois,T., De Bruycker,J.J., Bonnefoy,A.,
            Lapeyraque,A.L. and Decaluwe,H.
  TITLE     CNS Inflammation as the First Sign of Complement Factor I
            Deficiency: A Severe Myelitis Treated With Intense Immunotherapy
            and Eculizumab
  JOURNAL   Neurol Neuroimmunol Neuroinflamm 11 (2), e200191 (2024)
   PUBMED   38134378
  REMARK    GeneRIF: CNS Inflammation as the First Sign of Complement Factor I
            Deficiency.
REFERENCE   5  (residues 1 to 564)
  AUTHORS   van de Ven,J.P., Nilsson,S.C., Tan,P.L., Buitendijk,G.H.,
            Ristau,T., Mohlin,F.C., Nabuurs,S.B., Schoenmaker-Koller,F.E.,
            Smailhodzic,D., Campochiaro,P.A., Zack,D.J., Duvvari,M.R.,
            Bakker,B., Paun,C.C., Boon,C.J., Uitterlinden,A.G., Liakopoulos,S.,
            Klevering,B.J., Fauser,S., Daha,M.R., Katsanis,N., Klaver,C.C.,
            Blom,A.M., Hoyng,C.B. and den Hollander,A.I.
  TITLE     A functional variant in the CFI gene confers a high risk of
            age-related macular degeneration
  JOURNAL   Nat Genet 45 (7), 813-817 (2013)
   PUBMED   23685748
  REMARK    GeneRIF: these findings demonstrate that rare, highly penetrant
            mutations in CFI contribute to the genetic burden of age-related
            macular degeneration.
REFERENCE   6  (residues 1 to 564)
  AUTHORS   Martin,B. and Smith,R.J.H.
  TITLE     C3 Glomerulopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301598
REFERENCE   7  (residues 1 to 564)
  AUTHORS   Noris,M., Bresin,E., Mele,C. and Remuzzi,G.
  TITLE     Genetic Atypical Hemolytic-Uremic Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301541
REFERENCE   8  (residues 1 to 564)
  AUTHORS   DiScipio,R.G.
  TITLE     Ultrastructures and interactions of complement factors H and I
  JOURNAL   J Immunol 149 (8), 2592-2599 (1992)
   PUBMED   1401896
REFERENCE   9  (residues 1 to 564)
  AUTHORS   Shiang,R., Murray,J.C., Morton,C.C., Buetow,K.H., Wasmuth,J.J.,
            Olney,A.H., Sanger,W.G. and Goldberger,G.
  TITLE     Mapping of the human complement factor I gene to 4q25
  JOURNAL   Genomics 4 (1), 82-86 (1989)
   PUBMED   2563353
REFERENCE   10 (residues 1 to 564)
  AUTHORS   Catterall,C.F., Lyons,A., Sim,R.B., Day,A.J. and Harris,T.J.
  TITLE     Characterization of primary amino acid sequence of human complement
            control protein factor I from an analysis of cDNA clones
  JOURNAL   Biochem J 242 (3), 849-856 (1987)
   PUBMED   2954545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC126283.3.
            
            Summary: This gene encodes a serine proteinase that is essential
            for regulating the complement cascade. The encoded preproprotein is
            cleaved to produce both heavy and light chains, which are linked by
            disulfide bonds to form a heterodimeric glycoprotein. This
            heterodimer can cleave and inactivate the complement components C4b
            and C3b, and it prevents the assembly of the C3 and C5 convertase
            enzymes. Defects in this gene cause complement factor I deficiency,
            an autosomal recessive disease associated with a susceptibility to
            pyogenic infections. Mutations in this gene have been associated
            with a predisposition to atypical hemolytic uremic syndrome, a
            disease characterized by acute renal failure, microangiopathic
            hemolytic anemia and thrombocytopenia. Primary glomerulonephritis
            with immune deposits and age-related macular degeneration are other
            conditions associated with mutations of this gene. [provided by
            RefSeq, Dec 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138515.884116.1,
                                           SRR14372080.206341.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..564
                     /product="complement factor I isoform 9 preproprotein"
                     /EC_number="3.4.21.45"
                     /note="C3b-inactivator; Konglutinogen-activating factor;
                     complement factor I heavy chain; complement component I;
                     C3B/C4B inactivator; complement control protein factor I;
                     light chain of factor I"
                     /calculated_mol_wt=61478
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2281
     Region          43..108
                     /region_name="FIMAC"
                     /note="factor I membrane attack complex; smart00057"
                     /db_xref="CDD:214493"
     Region          114..215
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Region          224..256
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(227,235,246..247)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(239,242,246,252..253)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            249..253
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          257..293
                     /region_name="Ldl_recept_a"
                     /note="Low-density lipoprotein receptor domain class A;
                     pfam00057"
                     /db_xref="CDD:395011"
     Site            order(264,272,283..284)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(276,279,283,289..290)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            286..290
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          321..553
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            321
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(361,410,506)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            order(500,526,528)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..564
                     /gene="CFI"
                     /gene_synonym="AHUS3; ARMD13; C3b-INA; C3BINA; FI; IF;
                     KAF"
                     /coded_by="NM_001375283.1:29..1723"
                     /note="isoform 9 preproprotein is encoded by transcript
                     variant 9"
                     /db_xref="GeneID:3426"
                     /db_xref="HGNC:HGNC:5394"
                     /db_xref="MIM:217030"
ORIGIN      
        1 mkllhvfllf lcfhlrfckv tytsqedlve kkclakkyth lscdkvfcqp wqrciegtcv
       61 cklpyqcpkn gtavcatnrr sfptycqqks leclhpgtkf lnngtctaeg kfsvslkhgn
      121 tdsegivevk lvdqdktmfi cksswsmrea nvacldlgfq qgadtqrrfk lsdlsinste
      181 clhvhcrgle tslaectftk rrtmgyqdfa dvvcytqkad spmddffqcv ngkyisqmka
      241 cdgindcgdq sdelcckacq gkgfhcksgv cipsqyqcng evdcitgede vgcaerrrik
      301 sllpklscgv knrmhirrkr ivggkraqlg dlpwqvaikd asgitcggiy iggcwiltaa
      361 hclraskthr yqiwttvvdw ihpdlkrivi eyvdriifhe nynagtyqnd ialiemkkdg
      421 nkkdcelprs ipacvpwspy lfqpndtciv sgwgrekdne rvfslqwgev klisncskfy
      481 gnrfyekeme cagtydgsid ackgdsggpl vcmdannvty vwgvvswgen cgkpefpgvy
      541 tkvanyfdwi syhvgrpfis qynv
//
LOCUS       NP_001305838             911 aa            linear   PRI 21-NOV-2025
DEFINITION  general transcription factor 3C polypeptide 2 isoform b [Homo
            sapiens].
ACCESSION   NP_001305838 XP_005264330
VERSION     NP_001305838.2
DBSOURCE    REFSEQ: accession NM_001318909.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Peng,F., Zhou,Y., Wang,J., Guo,B., Wei,Y., Deng,H., Wu,Z.,
            Zhang,C., Shi,K., Li,Y., Wang,X., Shore,P., Zhao,S. and Deng,W.
  TITLE     The transcription factor Sp1 modulates RNA polymerase III gene
            transcription by controlling BRF1 and GTF3C2 expression in human
            cells
  JOURNAL   J Biol Chem 295 (14), 4617-4630 (2020)
   PUBMED   32115405
  REMARK    GeneRIF: The transcription factor Sp1 modulates RNA polymerase III
            gene transcription by controlling BRF1 and GTF3C2 expression in
            human cells.
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 911)
  AUTHORS   Kantidakis,T., Ramsbottom,B.A., Birch,J.L., Dowding,S.N. and
            White,R.J.
  TITLE     mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes,
            and targets their repressor Maf1
  JOURNAL   Proc Natl Acad Sci U S A 107 (26), 11823-11828 (2010)
   PUBMED   20543138
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11465]
REFERENCE   5  (residues 1 to 911)
  AUTHORS   Hirschowitz,E.A., Hiestand,D.M. and Yannelli,J.R.
  TITLE     Vaccines for lung cancer
  JOURNAL   J Thorac Oncol 1 (1), 93-104 (2006)
   PUBMED   17409835
  REMARK    Review article
REFERENCE   6  (residues 1 to 911)
  AUTHORS   Wang,Z. and Roeder,R.G.
  TITLE     DNA topoisomerase I and PC4 can interact with human TFIIIC to
            promote both accurate termination and transcription reinitiation by
            RNA polymerase III
  JOURNAL   Mol Cell 1 (5), 749-757 (1998)
   PUBMED   9660958
REFERENCE   7  (residues 1 to 911)
  AUTHORS   Oettel,S., Hartel,F., Kober,I., Iben,S. and Seifart,K.H.
  TITLE     Human transcription factors IIIC2, IIIC1 and a novel component
            IIIC0 fulfil different aspects of DNA binding to various pol III
            genes
  JOURNAL   Nucleic Acids Res 25 (12), 2440-2447 (1997)
   PUBMED   9171097
REFERENCE   8  (residues 1 to 911)
  AUTHORS   Chu,W.M., Wang,Z., Roeder,R.G. and Schmid,C.W.
  TITLE     RNA polymerase III transcription repressed by Rb through its
            interactions with TFIIIB and TFIIIC2
  JOURNAL   J Biol Chem 272 (23), 14755-14761 (1997)
   PUBMED   9169441
REFERENCE   9  (residues 1 to 911)
  AUTHORS   Sinn,E., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     Cloning and characterization of a TFIIIC2 subunit (TFIIIC beta)
            whose presence correlates with activation of RNA polymerase
            III-mediated transcription by adenovirus E1A expression and serum
            factors
  JOURNAL   Genes Dev 9 (6), 675-685 (1995)
   PUBMED   7729686
REFERENCE   10 (residues 1 to 911)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC074117.7, AC109828.4 and AC013413.6.
            
            On Apr 22, 2021 this sequence version replaced NP_001305838.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647092.1, SRR18074969.1217880.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..911
                     /product="general transcription factor 3C polypeptide 2
                     isoform b"
                     /note="general transcription factor 3C polypeptide 2;
                     TFIIIC 110 kDa subunit; transcription factor IIIC subunit
                     beta; transcription factor IIIC 110 kDa subunit; general
                     transcription factor IIIC, polypeptide 2, beta 110kDa"
                     /calculated_mol_wt=100549
     Region          24..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          <62..255
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          205..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          366..426
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          427..483
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          470..543
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          484..535
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          536..603
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          558..595
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <559..644
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          604..654
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          616..656
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          655..690
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          765..785
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            871
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Region          889..911
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            892
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            893
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            895
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     Site            901
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WUA4.2)"
     CDS             1..911
                     /gene="GTF3C2"
                     /gene_synonym="TF3C-beta; TFIIIC-BETA; TFIIIC110"
                     /coded_by="NM_001318909.4:703..3438"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS1749.1"
                     /db_xref="GeneID:2976"
                     /db_xref="HGNC:HGNC:4665"
                     /db_xref="MIM:604883"
ORIGIN      
        1 mdtcgvgyva lgeagpvgnm tvvdspgqev lnqldvktss emtsaeasve mslptplpgf
       61 edspdqrrlp peqeslsrle qpdlssemsk vskpraskpg rkrggrtrkg pkrpqqpnpp
      121 saplvpglld qsnplstpmp kkrgrkskae llllklskdl drpesqspkr ppedfetpsg
      181 erprrraaqv allylqelae elstalpapv scpegpkvss ptkpkkirqp aacpggeevd
      241 gaprdedffl qveaedvees egpsesssep epvvprstpr gstsgkqkph crgmapnglp
      301 nhimapvwkc lhltkdfreq khsywefaew iplawkwhll seleaapylp qeeksplfsv
      361 qreglpedgt lyrinrfssi tahperwdvs fftggplwal dwcpvpegag asqyvalfss
      421 pdmnethpls qlhsgpgllq lwglgtlqqe scpgnrahfv ygiacdngci wdlkfcpsga
      481 welpgtprka pllprlglla lacsdgkvll fslphpeall aqqppdavkp aiykvqcvat
      541 lqvgsmqatd psecgqclsl awmptrphqh laagyyngmv vfwnlptnsp lqrirlsdgs
      601 lklypfqcfl ahdqavrtlq wckanshflv sagsdrkikf wdlrrpyepi nsikrflste
      661 lawllpyngv tvaqdncyas yglcgihyid agylgfkayf taprkgtvws lsgsdwlgti
      721 aagdisgeli aailpdmaln pinvkrpver rfpiykadli pyqdspegpd hssassgvpn
      781 ppkartytet vnhhyllfqd tdlgsfhdll rrepmlrmqe geghsqlcld rlqleaihkv
      841 rfspnldsyg wlvsggqsgl vrihfvrgla splghrmqle srahfnamfq pssptrrpgf
      901 sptshrllpt p
//
LOCUS       NP_001358086            1115 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal cell adhesion molecule isoform dd precursor [Homo
            sapiens].
ACCESSION   NP_001358086 XP_024302550
VERSION     NP_001358086.1
DBSOURCE    REFSEQ: accession NM_001371157.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1115)
  AUTHORS   Wang,C., Wang,Z., Fu,L., Du,J., Ji,F. and Qiu,X.
  TITLE     CircNRCAM up-regulates NRCAM to promote papillary thyroid carcinoma
            progression
  JOURNAL   J Endocrinol Invest 47 (5), 1215-1226 (2024)
   PUBMED   38485895
  REMARK    GeneRIF: CircNRCAM up-regulates NRCAM to promote papillary thyroid
            carcinoma progression.
REFERENCE   2  (residues 1 to 1115)
  AUTHORS   Zhou,L., He,L., Liu,C.H., Qiu,H., Zheng,L., Sample,K.M., Wu,Q.,
            Li,J., Xie,K., Ampuero,J., Li,Z., Lv,D., Liu,M., Romero-Gomez,M.,
            Hu,Y. and Tang,H.
  TITLE     Liver cancer stem cell dissemination and metastasis: uncovering the
            role of NRCAM in hepatocellular carcinoma
  JOURNAL   J Exp Clin Cancer Res 42 (1), 311 (2023)
   PUBMED   37993901
  REMARK    GeneRIF: Liver cancer stem cell dissemination and metastasis:
            uncovering the role of NRCAM in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1115)
  AUTHORS   Sannes,A.C., Christensen,J.O., Nielsen,M.B. and Gjerstad,J.
  TITLE     Stress-induced headache in the general working population is
            moderated by the NRCAM rs2300043 genotype
  JOURNAL   Scand J Pain 23 (2), 326-332 (2022)
   PUBMED   36181733
  REMARK    GeneRIF: Stress-induced headache in the general working population
            is moderated by the NRCAM rs2300043 genotype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1115)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 1115)
  AUTHORS   Bai,C. and Chen,D.G.
  TITLE     NRCAM acts as a prognostic biomarker and promotes the tumor
            progression in gastric cancer via EMT pathway
  JOURNAL   Tissue Cell 77, 101859 (2022)
   PUBMED   35763884
  REMARK    GeneRIF: NRCAM acts as a prognostic biomarker and promotes the
            tumor progression in gastric cancer via EMT pathway.
REFERENCE   6  (residues 1 to 1115)
  AUTHORS   Wang,B., Williams,H., Du,J.S., Terrett,J. and Kenwrick,S.
  TITLE     Alternative splicing of human NrCAM in neural and nonneural tissues
  JOURNAL   Mol Cell Neurosci 10 (5-6), 287-295 (1998)
   PUBMED   9604207
REFERENCE   7  (residues 1 to 1115)
  AUTHORS   Grumet,M.
  TITLE     Nr-CAM: a cell adhesion molecule with ligand and receptor functions
  JOURNAL   Cell Tissue Res 290 (2), 423-428 (1997)
   PUBMED   9321706
  REMARK    Review article
REFERENCE   8  (residues 1 to 1115)
  AUTHORS   Sakurai,T., Lustig,M., Nativ,M., Hemperly,J.J., Schlessinger,J.,
            Peles,E. and Grumet,M.
  TITLE     Induction of neurite outgrowth through contactin and Nr-CAM by
            extracellular regions of glial receptor tyrosine phosphatase beta
  JOURNAL   J Cell Biol 136 (4), 907-918 (1997)
   PUBMED   9049255
REFERENCE   9  (residues 1 to 1115)
  AUTHORS   Volkmer,H., Leuschner,R., Zacharias,U. and Rathjen,F.G.
  TITLE     Neurofascin induces neurites by heterophilic interactions with
            axonal NrCAM while NrCAM requires F11 on the axonal surface to
            extend neurites
  JOURNAL   J Cell Biol 135 (4), 1059-1069 (1996)
   PUBMED   8922386
REFERENCE   10 (residues 1 to 1115)
  AUTHORS   Lane,R.P., Chen,X.N., Yamakawa,K., Vielmetter,J., Korenberg,J.R.
            and Dreyer,W.J.
  TITLE     Characterization of a highly conserved human homolog to the chicken
            neural cell surface protein Bravo/Nr-CAM that maps to chromosome
            band 7q31
  JOURNAL   Genomics 35 (3), 456-465 (1996)
   PUBMED   8812479
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005058.1, AC007567.2 and
            AC005683.2.
            
            On Jun 30, 2019 this sequence version replaced XP_024302550.1.
            
            Summary: Cell adhesion molecules (CAMs) are members of the
            immunoglobulin superfamily. This gene encodes a neuronal cell
            adhesion molecule with multiple immunoglobulin-like C2-type domains
            and fibronectin type-III domains. This ankyrin-binding protein is
            involved in neuron-neuron adhesion and promotes directional
            signaling during axonal cone growth. This gene is also expressed in
            non-neural tissues and may play a general role in cell-cell
            communication via signaling from its intracellular domain to the
            actin cytoskeleton during directional cell migration. Allelic
            variants of this gene have been associated with autism and
            addiction vulnerability. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.44564.1,
                                           SRR1803617.94304.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1115
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1115
                     /product="neuronal cell adhesion molecule isoform dd
                     precursor"
                     /note="NgCAM-related cell adhesion molecule; neuronal
                     surface protein Bravo"
                     /calculated_mol_wt=120474
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3315
     Region          40..134
                     /region_name="IgI_NrCAM"
                     /note="Immunoglobulin (Ig)-like domain of NrCAM (Ng
                     (neuronglia) CAM-related cell adhesion molecule); member
                     of the I-set of Ig superfamily (IgSF) domains; cd05874"
                     /db_xref="CDD:409458"
     Region          40..44
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409458"
     Region          49..53
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409458"
     Region          58..65
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409458"
     Region          71..76
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409458"
     Site            77
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          79..81
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409458"
     Region          88..91
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409458"
     Region          96..100
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409458"
     Region          113..121
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409458"
     Region          124..134
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409458"
     Region          143..232
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          157..161
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          171..175
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          194..198
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          209..214
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            217
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          225..228
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            239
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            245
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            270
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          271..352
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          282..286
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          295..299
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            308
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          317..321
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          331..336
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          344..347
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          356..444
                     /region_name="Ig4_NrCAM"
                     /note="Fourth immunoglobulin (Ig)-like domain of NrCAM
                     (NgCAM-related cell adhesion molecule); cd05868"
                     /db_xref="CDD:409454"
     Region          372..376
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409454"
     Region          385..389
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409454"
     Region          409..413
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409454"
     Region          423..428
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409454"
     Site            427
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          436..439
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409454"
     Region          453..536
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          466..470
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          479..483
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            501
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          502..506
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          516..521
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          529..532
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          542..627
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          557..561
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          572..576
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          596..1036
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          607..612
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            613
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          620..623
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          631..721
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(631,697,712)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            700
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            order(713..714,716..717)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            786
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            842
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            977
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            993
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1003
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          1070..>1105
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     CDS             1..1115
                     /gene="NRCAM"
                     /gene_synonym="NEDNMS"
                     /coded_by="NM_001371157.1:526..3873"
                     /note="isoform dd precursor is encoded by transcript
                     variant 59"
                     /db_xref="GeneID:4897"
                     /db_xref="HGNC:HGNC:7994"
                     /db_xref="MIM:601581"
ORIGIN      
        1 mqlkimpkkk rlsagrvpli lflcqmisal evpldlvqpp titqqspkdy iidprenivi
       61 qceakgkppp sfswtrngth fdidkdplvt mkpgtgtlii nimsegkaet yegvyqctar
      121 nergaavsnn ivvrpsrspl wtkeklepit lqsgqslvlp crppiglppp iifwmdnsfq
      181 rlpqservsq glngdlyfsn vlpedtredy icyarfnhtq tiqqkqpisv kvisvdelnd
      241 tiaanlsdte fygakssrer pptfltpegn asnkeelrgn vlsleciaeg lptpiiywak
      301 edgmlpknrt vyknfektlq iihvseadsg nyqciaknal gaihhtisvr vkaapywita
      361 pqnlvlspge dgtlicrang npkpriswlt ngvpieiapd dpsrkidgdt iifsnvqers
      421 savyqcnasn eygyllanaf vnvlaeppri ltpantlyqv ianrpalldc affgsplpti
      481 ewfkgakgsa lhediyvlhe ngtleipvaq kdstgtytcv arnklgmakn evhleikdpt
      541 wivkqpeyav vqrgsmvsfe ckvkhdhtls ltvlwlkdnr elpsderftv dkdhlvvadv
      601 sdddsgtytc vanttldsvs asavlsvvdv pnppfdlelt dqldksvqls wtpgddnnsp
      661 itkfiieyed amhkpglwhh qtevsgtqtt aqlklspyvn ysfrvmavns igkslpseas
      721 eqyltkasep dknptavegl gsepdnlvit wkplngfesn gpglqykvsw rqkdgddewt
      781 svvvanvsky ivsgtptfvp ylikvqalnd mgfapepavv mghsgedlpm vapgnvrvnv
      841 vnstlaevhw dpvplksirg hlqgyriyyw ktqssskrnr rhiekkiltf qgskthgmlp
      901 glepfshytl nvrvvngkge gpaspdrvfn tpegvpsaps slkivnptld sltlewdpps
      961 hpngilteyt lkyqpinsth elgplvdlki panktrwtlk nlnfstrykf yfyaqtsags
     1021 gsqiteeavt tvdeamasrq vdiatqgwfi glmcavalli lillivcfir rnkggkypvk
     1081 ekedahadpe iqpmkeddgt fgeyrlfsfv ssasf
//
LOCUS       NP_001309196             279 aa            linear   PRI 21-NOV-2025
DEFINITION  U4/U6 small nuclear ribonucleoprotein Prp4 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001309196 XP_005252357
VERSION     NP_001309196.1
DBSOURCE    REFSEQ: accession NM_001322267.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Park,S., Han,S.H., Kim,H.G., Jeong,J., Choi,M., Kim,H.Y., Kim,M.G.,
            Park,J.K., Han,J.E., Cho,G.J., Kim,M.O., Ryoo,Z.Y. and Choi,S.K.
  TITLE     PRPF4 is a novel therapeutic target for the treatment of breast
            cancer by influencing growth, migration, invasion, and apoptosis of
            breast cancer cells via p38 MAPK signaling pathway
  JOURNAL   Mol Cell Probes 47, 101440 (2019)
   PUBMED   31445970
  REMARK    GeneRIF: Results confirmed that the PRPF4 gene was overexpressed in
            various breast cancer cell lines. Its knockdown slows down breast
            cancer progression via suppression of p38 MAPK phosphorylation. In
            conclusion, the PRPF4 gene plays an important role in the growth of
            breast cancer cells.
REFERENCE   6  (residues 1 to 279)
  AUTHORS   Heng,H.H., Wang,A. and Hu,J.
  TITLE     Mapping of the human HPRP3 and HPRP4 genes encoding
            U4/U6-associated splicing factors to chromosomes 1q21.1 and
            9q31-q33
  JOURNAL   Genomics 48 (2), 273-275 (1998)
   PUBMED   9521884
REFERENCE   7  (residues 1 to 279)
  AUTHORS   Horowitz,D.S., Kobayashi,R. and Krainer,A.R.
  TITLE     A new cyclophilin and the human homologues of yeast Prp3 and Prp4
            form a complex associated with U4/U6 snRNPs
  JOURNAL   RNA 3 (12), 1374-1387 (1997)
   PUBMED   9404889
REFERENCE   8  (residues 1 to 279)
  AUTHORS   Wang,A., Forman-Kay,J., Luo,Y., Luo,M., Chow,Y.H., Plumb,J.,
            Friesen,J.D., Tsui,L.C., Heng,H.H., Woolford,J.L. Jr. and Hu,J.
  TITLE     Identification and characterization of human genes encoding Hprp3p
            and Hprp4p, interacting components of the spliceosome
  JOURNAL   Hum Mol Genet 6 (12), 2117-2126 (1997)
   PUBMED   9328476
REFERENCE   9  (residues 1 to 279)
  AUTHORS   Lauber,J., Plessel,G., Prehn,S., Will,C.L., Fabrizio,P.,
            Groning,K., Lane,W.S. and Luhrmann,R.
  TITLE     The human U4/U6 snRNP contains 60 and 90kD proteins that are
            structurally homologous to the yeast splicing factors Prp4p and
            Prp3p
  JOURNAL   RNA 3 (8), 926-941 (1997)
   PUBMED   9257651
  REMARK    Erratum:[RNA 1997 Oct;3(10):1204-6]
REFERENCE   10 (residues 1 to 279)
  AUTHORS   Horowitz,D.S. and Krainer,A.R.
  TITLE     A human protein required for the second step of pre-mRNA splicing
            is functionally related to a yeast splicing factor
  JOURNAL   Genes Dev 11 (1), 139-151 (1997)
   PUBMED   9000057
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL449305.4.
            
            On Apr 8, 2016 this sequence version replaced XP_005252357.1.
            
            Summary: The protein encoded by this gene is part of a heteromeric
            complex that binds U4, U5, and U6 small nuclear RNAs and is
            involved in pre-mRNA splicing. The encoded protein also is a
            mitotic checkpoint protein and a regulator of chemoresistance in
            human ovarian cancer. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Apr 2016].
            
            Transcript Variant: This variant (4) and variant 3 both encode the
            same isoform (3).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4643907.19850.1,
                                           ERR4643846.13669.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..279
                     /product="U4/U6 small nuclear ribonucleoprotein Prp4
                     isoform 3"
                     /note="PRP4/STK/WD splicing factor; U4/U6 small nuclear
                     ribonucleoprotein Prp4; PRP4 homolog; WD splicing factor
                     Prp4; U4/U6 snRNP 60 kDa protein; pre-mRNA processing
                     factor 4; PRP4 pre-mRNA processing factor 4 homolog"
                     /calculated_mol_wt=30946
     Region          <13..276
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          42..78
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          83..119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          126..161
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          167..201
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          209..246
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          252..276
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..279
                     /gene="PRPF4"
                     /gene_synonym="HPRP4; HPRP4P; PRP4; Prp4p; RP70; SNRNP60"
                     /coded_by="NM_001322267.2:855..1694"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:9128"
                     /db_xref="HGNC:HGNC:17349"
                     /db_xref="MIM:607795"
ORIGIN      
        1 mlsfvfdrsg lcklwsvpdc nllhtlrghn tnvgaivfhp kstvsldpkd vnlascaadg
       61 svklwsldsd epvadieght vrvarvmwhp sgrflgttcy drswrlwdle aqeeilhqeg
      121 hsmgvydiaf hqdgslagtg gldafgrvwd lrtgrcimfl eghlkeiygi nfspngyhia
      181 tgsgdntckv wdlrqrrcvy tipahqnlvt gvkfepihgn flltgaydnt akiwthpgws
      241 plktlagheg kvmgldissd gqliatcsyd rtfklwmae
//
LOCUS       NP_001378858            1776 aa            linear   PRI 21-NOV-2025
DEFINITION  Golgi-specific brefeldin A-resistance guanine nucleotide exchange
            factor 1 isoform 13 [Homo sapiens].
ACCESSION   NP_001378858
VERSION     NP_001378858.1
DBSOURCE    REFSEQ: accession NM_001391929.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1776)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1776)
  AUTHORS   Hirano,J., Hayashi,T., Kitamura,K., Nishimura,Y., Shimizu,H.,
            Okamoto,T., Okada,K., Uemura,K., Yeh,M.T., Ono,C., Taguwa,S.,
            Muramatsu,M. and Matsuura,Y.
  TITLE     Enterovirus 3A protein disrupts endoplasmic reticulum homeostasis
            through interaction with GBF1
  JOURNAL   J Virol 98 (7), e0081324 (2024)
   PUBMED   38904364
  REMARK    GeneRIF: Enterovirus 3A protein disrupts endoplasmic reticulum
            homeostasis through interaction with GBF1.
REFERENCE   3  (residues 1 to 1776)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1776)
  AUTHORS   Navare,A.T., Mast,F.D., Olivier,J.P., Bertomeu,T., Neal,M.L.,
            Carpp,L.N., Kaushansky,A., Coulombe-Huntington,J., Tyers,M. and
            Aitchison,J.D.
  TITLE     Viral protein engagement of GBF1 induces host cell vulnerability
            through synthetic lethality
  JOURNAL   J Cell Biol 221 (11) (2022)
   PUBMED   36305789
  REMARK    GeneRIF: Viral protein engagement of GBF1 induces host cell
            vulnerability through synthetic lethality.
REFERENCE   5  (residues 1 to 1776)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1776)
  AUTHORS   Garcia-Mata,R. and Sztul,E.
  TITLE     The membrane-tethering protein p115 interacts with GBF1, an ARF
            guanine-nucleotide-exchange factor
  JOURNAL   EMBO Rep 4 (3), 320-325 (2003)
   PUBMED   12634853
  REMARK    GeneRIF: novel interaction between p115 and Golgi-specific
            brefeldin-A-resistant factor 1 (GBF1)
REFERENCE   7  (residues 1 to 1776)
  AUTHORS   Kawamoto,K., Yoshida,Y., Tamaki,H., Torii,S., Shinotsuka,C.,
            Yamashina,S. and Nakayama,K.
  TITLE     GBF1, a guanine nucleotide exchange factor for ADP-ribosylation
            factors, is localized to the cis-Golgi and involved in membrane
            association of the COPI coat
  JOURNAL   Traffic 3 (7), 483-495 (2002)
   PUBMED   12047556
  REMARK    GeneRIF: detailed subcellular localization to the cis-Golgi
REFERENCE   8  (residues 1 to 1776)
  AUTHORS   Verhoeven,K., Villanova,M., Rossi,A., Malandrini,A., De Jonghe,P.
            and Timmerman,V.
  TITLE     Localization of the gene for the intermediate form of
            Charcot-Marie-Tooth to chromosome 10q24.1-q25.1
  JOURNAL   Am J Hum Genet 69 (4), 889-894 (2001)
   PUBMED   11533914
REFERENCE   9  (residues 1 to 1776)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   10 (residues 1 to 1776)
  AUTHORS   Mansour,S.J., Herbrick,J.A., Scherer,S.W. and Melancon,P.
  TITLE     Human GBF1 is a ubiquitously expressed gene of the sec7 domain
            family mapping to 10q24
  JOURNAL   Genomics 54 (2), 323-327 (1998)
   PUBMED   9828135
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160011.35, AL356420.14 and
            AL121928.13.
            
            Summary: This gene encodes a member of the Sec7 domain family. The
            encoded protein is a guanine nucleotide exchange factor that
            regulates the recruitment of proteins to membranes by mediating GDP
            to GTP exchange. The encoded protein is localized to the Golgi
            apparatus and plays a role in vesicular trafficking by activating
            ADP ribosylation factor 1. The encoded protein has also been
            identified as an important host factor for viral replication.
            Multiple transcript variants have been observed for this gene.
            [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2144333,
                              SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1776
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..1776
                     /product="Golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1 isoform 13"
                     /note="golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1; BFA-resistant GEF 1"
                     /calculated_mol_wt=196914
     Region          <429..>882
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Region          699..881
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          <1457..>1531
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Region          <1711..1774
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1776
                     /gene="GBF1"
                     /gene_synonym="ARF1GEF; CMT2GG; CMTDI2; CMTDIA"
                     /coded_by="NM_001391929.1:261..5591"
                     /note="isoform 13 is encoded by transcript variant 21"
                     /db_xref="GeneID:8729"
                     /db_xref="HGNC:HGNC:4181"
                     /db_xref="MIM:603698"
ORIGIN      
        1 mvdkniyiiq geinivvgai krnarwstht pldeerdpll hsfghlkevl nsitelseie
       61 pnvflrpfle virsedttgp itglaltsvn kflsyalidp thegtaegme nmadavthar
      121 fvgtdpasde vvlmkilqvl rtllltpvga hltnesvcei mqscfricfe mrlsellrks
      181 aehtlvdmvq llftrlpqfk eepknyvgtn mkklkmragg msdsskwkkq krsprpprhm
      241 tkvtpgselp tpngttlssn ltggmpfidv ptpissasse aasavvspst dsglefssqt
      301 tskedltdle qpgspgysta tepgsselgv peqpdlqegt hveksqsasv esipevleec
      361 tspadhsdsa svhdmdyvnp rgvrftqssq kegtalvpyg lpcirelfrf lisltnphdr
      421 hnsevmihmg lhlltvales apvaqcqtll glikdemcrh lfqllsierl nlyaaslrvc
      481 fllfesmreh lkfqmemyik klmeiitven pkmpyemkem aleaivqlwr ipsfvtelyi
      541 nydcdyycsn lfeeltklls knafpvsgql ytthllslda lltvidstea hcqakvlnsl
      601 tqqekketar psceivdgtr easntertas dgkavgmasd ipglhlpggg rlppehgksg
      661 csdleeavds gadkkfarkp prfscllpdp relieiknkk kllitgteqf nqkpkkgiqf
      721 lqekglltip mdntevaqwl renprldkkm igefvsdrkn idllesfvst fsfqglrlde
      781 alrlyleafr lpgeapviqr lleafterwm ncngspfans dacfslayav imlntdqhnh
      841 nvrkqnapmt leefrknlkg vnggkdfeqd iledmyhaik kcamisahyg lsdvfdnlii
      901 slckftalss esienlpsvf gsnpkahiaa ktvfhlahrh gdilregwkn imeamlqlfr
      961 aqllpkamie vedfvdpngk islqreetps nrgestvlsf vswltlsgpe qssvrgpste
     1021 nqeakrvale cikqcdpekm iteskflqle slqelmkalv svtpdeetyd eedaafclem
     1081 llrivlenrd rvgcvwqtvr dhlyhlcvqa qdfcflvera vvgllrlair llrreeisaq
     1141 vllslrilll mkpsvlsrvs hqvayglhel lktnaanihs gddwatlftl lecigsgvkp
     1201 paalqatara dapdagaqsd selpsyhqnd vsldrgytsd sevytdhgrp gkihrsatda
     1261 dvvnsgwlvv gkddvdnskp gpsrpgpspl inqysltvgl dlgphdtksl lkcveslsfi
     1321 vrdaahitpd nfelcvktlr ifveaslngg cksqekrgks hkydskgnrf kkkskegsml
     1381 rrprtssqha srggqsddde degvpasyht vslqlldlmh tlhtraasiy sswaeeqrhl
     1441 etggqkiead srtlwahcwc pllqgiaclc cdarrqvrmq altylqrall vhdlqkldal
     1501 ewescfnkvl fplltkllen ispadvggme etrmrastll skvflqhlsp llslstfaal
     1561 wltildfmdk ymhagssdll seaipeslkn mllvmdtaei fhsadarggg psalweitwe
     1621 ridcflphlr delfkqtviq dpmpmepqgq kplasahlts aagdtrtpgh ppppeipsel
     1681 gacdfekpes praasssspg spvasspsrl sptpdgpppl aqpplilqpl asplqvgvpp
     1741 mtlpiilnpa lieatspvpl latprptdpi ptsevn
//
LOCUS       NP_001381423             825 aa            linear   PRI 21-NOV-2025
DEFINITION  F-box and leucine-rich repeat protein 13 isoform 4 [Homo sapiens].
ACCESSION   NP_001381423 XP_005250262
VERSION     NP_001381423.1
DBSOURCE    REFSEQ: accession NM_001394494.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Walton,T., Gui,M., Velkova,S., Fassad,M.R., Hirst,R.A., Haarman,E.,
            O'Callaghan,C., Bottier,M., Burgoyne,T., Mitchison,H.M. and
            Brown,A.
  TITLE     Axonemal structures reveal mechanoregulatory and disease mechanisms
  JOURNAL   Nature 618 (7965), 625-633 (2023)
   PUBMED   37258679
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Fung,E., Richter,C., Yang,H.B., Schaffer,I., Fischer,R.,
            Kessler,B.M., Bassermann,F. and D'Angiolella,V.
  TITLE     FBXL13 directs the proteolysis of CEP192 to regulate centrosome
            homeostasis and cell migration
  JOURNAL   EMBO Rep 19 (3) (2018)
   PUBMED   29348145
REFERENCE   4  (residues 1 to 825)
  AUTHORS   He,J., Kelly,T.N., Zhao,Q., Li,H., Huang,J., Wang,L., Jaquish,C.E.,
            Sung,Y.J., Shimmin,L.C., Lu,F., Mu,J., Hu,D., Ji,X., Shen,C.,
            Guo,D., Ma,J., Wang,R., Shen,J., Li,S., Chen,J., Mei,H., Chen,C.S.,
            Chen,S., Chen,J., Li,J., Cao,J., Lu,X., Wu,X., Rice,T.K., Gu,C.C.,
            Schwander,K., Hamm,L.L., Liu,D., Rao,D.C., Hixson,J.E. and Gu,D.
  TITLE     Genome-wide association study identifies 8 novel loci associated
            with blood pressure responses to interventions in Han Chinese
  JOURNAL   Circ Cardiovasc Genet 6 (6), 598-607 (2013)
   PUBMED   24165912
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   6  (residues 1 to 825)
  AUTHORS   Curtiss,N.P., Bonifas,J.M., Lauchle,J.O., Balkman,J.D., Kratz,C.P.,
            Emerling,B.M., Green,E.D., Le Beau,M.M. and Shannon,K.M.
  TITLE     Isolation and analysis of candidate myeloid tumor suppressor genes
            from a commonly deleted segment of 7q22
  JOURNAL   Genomics 85 (5), 600-607 (2005)
   PUBMED   15820312
REFERENCE   7  (residues 1 to 825)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073127.11, AC005250.1 and AC006477.4.
            
            On Apr 22, 2021 this sequence version replaced XP_005250262.1.
            
            Summary: Members of the F-box protein family, such as FBXL13, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000440067.4/ ENSP00000390126.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..825
                     /product="F-box and leucine-rich repeat protein 13 isoform
                     4"
                     /note="F-box/LRR-repeat protein 13; dynein regulatory
                     complex subunit 6; cilia and flagella associated protein
                     169"
                     /calculated_mol_wt=94255
     Region          8..50
                     /region_name="DD_FBXL13"
                     /note="dimerization/docking (D/D) domain found in
                     F-box/LRR-repeat protein 13 (FBXL13) and similar proteins;
                     cd22977"
                     /db_xref="CDD:438546"
     Region          <112..>224
                     /region_name="Sfi1"
                     /note="Sfi1 spindle body protein; pfam08457"
                     /db_xref="CDD:430007"
     Region          245..286
                     /region_name="F-box_FBXL13"
                     /note="F-box domain found in F-box/LRR-repeat protein 13
                     (FBXL13) and similar proteins; cd22124"
                     /db_xref="CDD:438896"
     Site            order(248,252,255..256,259..260,264,266..267,271..273,275)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438896"
     Region          285..312
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          312..497
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          313..336
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          337..362
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          363..387
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          388..406
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          416..441
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          442..491
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          468..490
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          492..515
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          518..542
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          529..737
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          543..570
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          571..596
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          597..645
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          646..671
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          672..697
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          698..723
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          724..749
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..825
                     /gene="FBXL13"
                     /gene_synonym="CFAP169; DRC6; Fbl13"
                     /coded_by="NM_001394494.2:27..2504"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS94164.1"
                     /db_xref="GeneID:222235"
                     /db_xref="HGNC:HGNC:21658"
                     /db_xref="MIM:609080"
ORIGIN      
        1 maslrnanpr lknyfkenyi pqvceallcg ilvtcpedpl rylegmimvi iksglqnllw
       61 dmcitpsmkp nirrlsetyl eqlfelddql mtpelmikac sfytghlvkt hfctwrdiar
      121 tnenvvlaek mnravtcynf rlqksvfhhw hsymedqkek lknillriqq iiychkltii
      181 ltkwrntarh kskkkedeli lkhelqlkkw knrlilkraa aeesnfpers ssevflvdet
      241 lkcdisllpe railqiffyl slkdviicgq vnhawmlmtq lnslwnaidf ssvknvipdk
      301 yivstlqrwr lnvlrlnfrg cllrpktfrs vshcrnlqel nvsdcptftd esmrhisegc
      361 pgvlclnlsn ttitnrtmrl lprhfhnlqn lslaycrrft dkglqylnlg ngchkliyld
      421 lsgctqisvq gfryiansct gimhltindm ptltdncvka lvekcsrits lvftgaphis
      481 dctfralsac klrkirfegn krvtdasfkf idknypnlsh iymadckgit dsslrslspl
      541 kqltvlnlan cvrigdmglk qfldgpasmr irelnlsncv rlsdasvmkl sercpnlnyl
      601 slrncehlta qgigyivnif slvsidlsgt disneglnvl srhkklkels vsecyritdd
      661 giqafckssl ilehldvsyc sqlsdmiika laiycinlts lsiagcpkit dsamemlsak
      721 chylhildis gcvlltdqil edlqigckql rilkmqyctn iskkaaqrms skvqqqeynt
      781 ndpprwfgyd regnpvteld nitsskgale ltvkkstyss edqaa
//
LOCUS       NP_001371348             291 aa            linear   PRI 21-NOV-2025
DEFINITION  WD repeat-containing protein 5 isoform 4 [Homo sapiens].
ACCESSION   NP_001371348
VERSION     NP_001371348.1
DBSOURCE    REFSEQ: accession NM_001384419.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Feng,W., Tang,Y., Jing,R., Ju,S. and Zong,W.
  TITLE     Highly expressed B3GALT5-AS1 contributes to gastric cancer
            progression by recruiting WDR5 to mediate B3GALT5 and regulating
            beta-catenin/ZEB1 axis
  JOURNAL   J Cell Mol Med 28 (17), e70061 (2024)
   PUBMED   39224045
  REMARK    GeneRIF: Highly expressed B3GALT5-AS1 contributes to gastric cancer
            progression by recruiting WDR5 to mediate B3GALT5 and regulating
            beta-catenin/ZEB1 axis.
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Yuan,X.N., Shao,Y.C., Guan,X.Q., Liu,Q., Chu,M.F., Yang,Z.L.,
            Li,H., Zhao,S., Tian,Y.H., Zhang,J.W. and Wei,L.
  TITLE     METTL3 orchestrates glycolysis by stabilizing the c-Myc/WDR5
            complex in triple-negative breast cancer
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (5), 119716 (2024)
   PUBMED   38547933
  REMARK    GeneRIF: METTL3 orchestrates glycolysis by stabilizing the
            c-Myc/WDR5 complex in triple-negative breast cancer.
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Huang,X., Zhang,C., Shang,X., Chen,Y., Xiao,Q., Wei,Z., Wang,G.,
            Zhen,X., Xu,G., Min,J., Shen,S. and Liu,Y.
  TITLE     The NTE domain of PTENalpha/beta promotes cancer progression by
            interacting with WDR5 via its SSSRRSS motif
  JOURNAL   Cell Death Dis 15 (5), 335 (2024)
   PUBMED   38744853
  REMARK    GeneRIF: The NTE domain of PTENalpha/beta promotes cancer
            progression by interacting with WDR5 via its SSSRRSS motif.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Streeter,S.A., Williams,A.G., Evans,J.R., Wang,J., Guarnaccia,A.D.,
            Florian,A.C., Al-Tobasei,R., Liu,Q., Tansey,W.P. and
            Weissmiller,A.M.
  TITLE     Mitotic gene regulation by the N-MYC-WDR5-PDPK1 nexus
  JOURNAL   BMC Genomics 25 (1), 360 (2024)
   PUBMED   38605297
  REMARK    GeneRIF: Mitotic gene regulation by the N-MYC-WDR5-PDPK1 nexus.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Wysocka,J., Swigut,T., Milne,T.A., Dou,Y., Zhang,X.,
            Burlingame,A.L., Roeder,R.G., Brivanlou,A.H. and Allis,C.D.
  TITLE     WDR5 associates with histone H3 methylated at K4 and is essential
            for H3 K4 methylation and vertebrate development
  JOURNAL   Cell 121 (6), 859-872 (2005)
   PUBMED   15960974
  REMARK    GeneRIF: The WDR5 is required for binding of the methyltransferase
            complex to the K4-dimethylated H3 tail as well as for global H3 K4
            trimethylation and HOX gene activation in human cells.
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Gori,F. and Demay,M.B.
  TITLE     BIG-3, a novel WD-40 repeat protein, is expressed in the developing
            growth plate and accelerates chondrocyte differentiation in vitro
  JOURNAL   Endocrinology 145 (3), 1050-1054 (2004)
   PUBMED   14657013
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Wysocka,J., Myers,M.P., Laherty,C.D., Eisenman,R.N. and Herr,W.
  TITLE     Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone
            H3-K4 methyltransferase are tethered together selectively by the
            cell-proliferation factor HCF-1
  JOURNAL   Genes Dev 17 (7), 896-911 (2003)
   PUBMED   12670868
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Gori,F., Divieti,P. and Demay,M.B.
  TITLE     Cloning and characterization of a novel WD-40 repeat protein that
            dramatically accelerates osteoblastic differentiation
  JOURNAL   J Biol Chem 276 (49), 46515-46522 (2001)
   PUBMED   11551928
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX649632.2.
            
            Summary: This gene encodes a member of the WD repeat protein
            family. WD repeats are minimally conserved regions of approximately
            40 amino acids typically bracketed by gly-his and trp-asp (GH-WD),
            which may facilitate formation of heterotrimeric or multiprotein
            complexes. Members of this family are involved in a variety of
            cellular processes, including cell cycle progression, signal
            transduction, apoptosis, and gene regulation. This protein contains
            7 WD repeats. Alternatively spliced transcript variants encoding
            the same protein have been identified. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3302844.1,
                                           SRR14038195.1994108.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004, SAMN02400308
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.2"
     Protein         1..291
                     /product="WD repeat-containing protein 5 isoform 4"
                     /note="SWD3, Set1c WD40 repeat protein, homolog;
                     BMP2-induced 3-kb gene protein; WD repeat-containing
                     protein 5; cilia and flagella associated protein 89;
                     BMP-2-induced gene 3 kb"
                     /calculated_mol_wt=31927
     Region          <40..287
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          49..84
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          89..125
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          132..167
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          174..210
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          218..255
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          261..287
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..291
                     /gene="WDR5"
                     /gene_synonym="BIG-3; BIG3; CFAP89; SWD3"
                     /coded_by="NM_001384419.1:178..1053"
                     /note="isoform 4 is encoded by transcript variant 13"
                     /db_xref="GeneID:11091"
                     /db_xref="HGNC:HGNC:12757"
                     /db_xref="MIM:609012"
ORIGIN      
        1 mateekkpet eaaraqptps ssatqskptp vkpnyalkft laghtkavss vkfspngewl
       61 assydktlki wdvssgkclk tlkghsnyvf ccnfnpqsnl ivsgsfdesv riwdvktgkc
      121 lktlpahsdp vsavhfnrdg slivsssydg lcriwdtasg qclktliddd nppvsfvkfs
      181 pngkyilaat ldntlklwdy skgkclktyt ghknekycif anfsvtggkw ivsgsednlv
      241 yiwnlqtkei vqklqghtdv vistachpte niiasaalen dktiklwksd c
//
LOCUS       NP_631907                508 aa            linear   PRI 21-NOV-2025
DEFINITION  splicing regulatory glutamine/lysine-rich protein 1 isoform b [Homo
            sapiens].
ACCESSION   NP_631907
VERSION     NP_631907.1
DBSOURCE    REFSEQ: accession NM_139168.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Chang,C., Rajasekaran,M., Qiao,Y., Dong,H., Wang,Y., Xia,H.,
            Deivasigamani,A., Wu,M., Sekar,K., Gao,H., Sun,M., Niu,Y., Li,Q.,
            Tao,L., Yan,Z., Wang,M., Chen,S., Zhao,S., Chen,D., Li,L., Yang,F.,
            Gao,H., Chen,B., Su,L., Xu,L., Chen,Y., Seshachalam,V.P., Chen,G.,
            Gunaratne,J., Hong,W., Shi,J., Chen,G., Grierson,D.S., Chabot,B.,
            Xie,T., Hui,K.M. and Chen,J.
  TITLE     The aberrant upregulation of exon 10-inclusive SREK1 through SRSF10
            acts as an oncogenic driver in human hepatocellular carcinoma
  JOURNAL   Nat Commun 13 (1), 1363 (2022)
   PUBMED   35296659
  REMARK    GeneRIF: The aberrant upregulation of exon 10-inclusive SREK1
            through SRSF10 acts as an oncogenic driver in human hepatocellular
            carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Abudureheman,Z., Li,L., Zhong,X., Xu,J., Gong,H., Yilamujiang,S.,
            Ren,J., Xie,C., Zheng,A., Tuerxun,D., Abudukadeer,A., Aini,P.,
            Xu,A. and Zou,X.
  TITLE     The rs74794265 SNP of the SREK1 Gene is Associated with COPD in
            Kashi, China
  JOURNAL   Int J Chron Obstruct Pulmon Dis 16, 2631-2636 (2021)
   PUBMED   34556983
  REMARK    GeneRIF: The rs74794265 SNP of the SREK1 Gene is Associated with
            COPD in Kashi, China.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Heese,K., Fujita,M., Akatsu,H., Yamamoto,T., Kosaka,K., Nagai,Y.
            and Sawada,T.
  TITLE     The splicing regulatory protein p18SRP is down-regulated in
            Alzheimer's disease brain
  JOURNAL   J Mol Neurosci 24 (2), 269-276 (2004)
   PUBMED   15456940
  REMARK    GeneRIF: p18SRP is a lysine-rich zinc finger domain-containing
            protein that interacts with the serine-arginine-rich splicing
            regulatory protein SRrp86; it is downregulated in brain of
            Alzheimer disease patients.
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Li,J., Hawkins,I.C., Harvey,C.D., Jennings,J.L., Link,A.J. and
            Patton,J.G.
  TITLE     Regulation of alternative splicing by SRrp86 and its interacting
            proteins
  JOURNAL   Mol Cell Biol 23 (21), 7437-7447 (2003)
   PUBMED   14559993
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Li,J., Barnard,D.C. and Patton,J.G.
  TITLE     A unique glutamic acid-lysine (EK) domain acts as a splicing
            inhibitor
  JOURNAL   J Biol Chem 277 (42), 39485-39492 (2002)
   PUBMED   12183448
  REMARK    GeneRIF: the unique glutamic acid-lysine domain of SRrp86 plays a
            modulatory role controlling serine-arginine domain function
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Barnard,D.C., Li,J., Peng,R. and Patton,J.G.
  TITLE     Regulation of alternative splicing by SRrp86 through coactivation
            and repression of specific SR proteins
  JOURNAL   RNA 8 (4), 526-533 (2002)
   PUBMED   11991645
  REMARK    GeneRIF: SRrp86 can activate SRp20 and repress SC35 in a
            dose-dependent manner both in vitro and in vivo
REFERENCE   10 (residues 1 to 508)
  AUTHORS   Barnard,D.C. and Patton,J.G.
  TITLE     Identification and characterization of a novel serine-arginine-rich
            splicing regulatory protein
  JOURNAL   Mol Cell Biol 20 (9), 3049-3057 (2000)
   PUBMED   10757789
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC067770.1, BC112343.1 and
            AC008772.6.
            
            Summary: This gene encodes a member of a family of
            serine/arginine-rich (SR) splicing proteins containing RNA
            recognition motif (RRM) domains. The encoded protein interacts with
            other SR proteins to modulate splice site selection. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and uses
            a downstream, in-frame start codon, compared to variant 1. The
            encoded isoform (b) has a shorter N-terminus compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC067770.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..508
                     /product="splicing regulatory glutamine/lysine-rich
                     protein 1 isoform b"
                     /note="splicing factor, arginine/serine-rich 12;
                     serine-arginine-rich splicing regulatory protein 508;
                     serine/arginine-rich-splicing regulatory protein 86;
                     splicing regulatory glutamine/lysine-rich protein 1;
                     splicing regulatory glutamic acid/lysine-rich protein 1"
                     /calculated_mol_wt=59249
     Region          62..147
                     /region_name="RRM2_SREK1"
                     /note="RNA recognition motif 2 (RRM2) found in splicing
                     regulatory glutamine/lysine-rich protein 1 (SREK1) and
                     similar proteins; cd12260"
                     /db_xref="CDD:409705"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WXA9.1)"
     Region          173..508
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXA9.1)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WXA9.1)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WXA9.1)"
     CDS             1..508
                     /gene="SREK1"
                     /gene_synonym="SFRS12; SRrp508; SRrp86"
                     /coded_by="NM_139168.4:661..2187"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3991.1"
                     /db_xref="GeneID:140890"
                     /db_xref="HGNC:HGNC:17882"
                     /db_xref="MIM:609268"
ORIGIN      
        1 mtslmpgagl lpiptpnplt tlgvslsslg aipaaaldpn iatlgeipqp plmgnvdpsk
       61 ideirrtvyv gnlnsqttta dqlleffkqv gevkfvrmag detqptrfaf vefadqnsvp
      121 ralafngvmf gdrplkinhs nnaivkppem tpqaaakele evmkrvreaq sfisaaiepe
      181 sgksnerkgg rsrshtrsks rssskshsrr krsqskhrsr shnrsrsrqk drrrsksphk
      241 krsksrerrk srsrshsrdk rkdtrekike kervkekdre kererekere kekergknkd
      301 rdkerekdre kdkekdrere rekehekdrd kekekeqdke kerekdrske idekrkkdkk
      361 srtpprsyna srrsrsssre rrrrrsrsss rsprtsktik rkssrspspr srnkkdkkre
      421 kerdhiserr ererstsmrk ssndrdgkek leknstslke kehnkepdss vskevddkda
      481 prteenkiqh ngncqlneen lstkteav
//
LOCUS       NP_001310250             384 aa            linear   PRI 21-NOV-2025
DEFINITION  mitogen-activated protein kinase 8 isoform beta1 [Homo sapiens].
ACCESSION   NP_001310250
VERSION     NP_001310250.1
DBSOURCE    REFSEQ: accession NM_001323321.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Liu,X., Ye,Z., Rao,D., Chen,Q. and Zhang,Z.
  TITLE     DUSP4 maintains the survival and LSD1 protein stability in
            esophageal squamous cell carcinoma cells by inhibiting JNK
            signaling-dependent autophagy
  JOURNAL   In Vitro Cell Dev Biol Anim 60 (2), 115-122 (2024)
   PUBMED   38286920
  REMARK    GeneRIF: DUSP4 maintains the survival and LSD1 protein stability in
            esophageal squamous cell carcinoma cells by inhibiting JNK
            signaling-dependent autophagy.
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Louw-du Toit,R., Simons,M. and Africander,D.
  TITLE     Progestins and breast cancer hallmarks: The role of the ERK1/2 and
            JNK pathways in estrogen receptor positive breast cancer cells
  JOURNAL   J Steroid Biochem Mol Biol 237, 106440 (2024)
   PUBMED   38048919
  REMARK    GeneRIF: Progestins and breast cancer hallmarks: The role of the
            ERK1/2 and JNK pathways in estrogen receptor positive breast cancer
            cells.
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Chai,F., Peng,H., Qin,L., Liu,C., Zeng,Y., Wang,R., Xu,G., Wang,R.,
            Wei,G., Huang,H., Lan,Y., Chen,W. and Wang,C.
  TITLE     MicroRNA miR-181d-5p regulates the MAPK signaling pathway by
            targeting mitogen-activated protein kinase 8 (MAPK8) to improve
            lupus nephritis
  JOURNAL   Gene 893, 147961 (2024)
   PUBMED   37931853
  REMARK    GeneRIF: MicroRNA miR-181d-5p regulates the MAPK signaling pathway
            by targeting mitogen-activated protein kinase 8 (MAPK8) to improve
            lupus nephritis.
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Feng,Y., Cao,H., Wang,D., Chen,L., Gao,R. and Sun,P.
  TITLE     JNK promotes the progression of castration-resistant prostate
            cancer
  JOURNAL   Acta Biochim Pol 70 (4), 817-822 (2023)
   PUBMED   38099475
  REMARK    GeneRIF: JNK promotes the progression of castration-resistant
            prostate cancer.
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Kharbanda,S., Saleem,A., Shafman,T., Emoto,Y., Taneja,N., Rubin,E.,
            Weichselbaum,R., Woodgett,J., Avruch,J., Kyriakis,J. et al.
  TITLE     Ionizing radiation stimulates a Grb2-mediated association of the
            stress-activated protein kinase with phosphatidylinositol 3-kinase
  JOURNAL   J Biol Chem 270 (32), 18871-18874 (1995)
   PUBMED   7642542
REFERENCE   7  (residues 1 to 384)
  AUTHORS   van Dam,H., Wilhelm,D., Herr,I., Steffen,A., Herrlich,P. and
            Angel,P.
  TITLE     ATF-2 is preferentially activated by stress-activated protein
            kinases to mediate c-jun induction in response to genotoxic agents
  JOURNAL   EMBO J 14 (8), 1798-1811 (1995)
   PUBMED   7737130
REFERENCE   8  (residues 1 to 384)
  AUTHORS   Livingstone,C., Patel,G. and Jones,N.
  TITLE     ATF-2 contains a phosphorylation-dependent transcriptional
            activation domain
  JOURNAL   EMBO J 14 (8), 1785-1797 (1995)
   PUBMED   7737129
REFERENCE   9  (residues 1 to 384)
  AUTHORS   Derijard,B., Raingeaud,J., Barrett,T., Wu,I.H., Han,J.,
            Ulevitch,R.J. and Davis,R.J.
  TITLE     Independent human MAP-kinase signal transduction pathways defined
            by MEK and MKK isoforms
  JOURNAL   Science 267 (5198), 682-685 (1995)
   PUBMED   7839144
  REMARK    Erratum:[Science 1995 Jul 7;269(5220):17]
REFERENCE   10 (residues 1 to 384)
  AUTHORS   Seth,A., Alvarez,E., Gupta,S. and Davis,R.J.
  TITLE     A phosphorylation site located in the NH2-terminal domain of c-Myc
            increases transactivation of gene expression
  JOURNAL   J Biol Chem 266 (35), 23521-23524 (1991)
   PUBMED   1748630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC074325.7 and AC016397.6.
            
            Summary: The protein encoded by this gene is a member of the MAP
            kinase family. MAP kinases act as an integration point for multiple
            biochemical signals, and are involved in a wide variety of cellular
            processes such as proliferation, differentiation, transcription
            regulation and development. This kinase is activated by various
            cell stimuli, and targets specific transcription factors, and thus
            mediates immediate-early gene expression in response to cell
            stimuli. The activation of this kinase by tumor-necrosis factor
            alpha (TNF-alpha) is found to be required for TNF-alpha induced
            apoptosis. This kinase is also involved in UV radiation induced
            apoptosis, which is thought to be related to cytochrom c-mediated
            cell death pathway. Studies of the mouse counterpart of this gene
            suggested that this kinase play a key role in T cell proliferation,
            apoptosis and differentiation. Several alternatively spliced
            transcript variants encoding distinct isoforms have been reported.
            [provided by RefSeq, Apr 2016].
            
            Transcript Variant: This variant (7), along with variants JNK1-b1
            and 11, encodes isoform beta1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.123767.1,
                                           SRR1660809.254748.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q11.22"
     Protein         1..384
                     /product="mitogen-activated protein kinase 8 isoform
                     beta1"
                     /EC_number="2.7.11.24"
                     /note="JUN N-terminal kinase; c-Jun N-terminal kinase 1;
                     MAP kinase 8; stress-activated protein kinase 1;
                     stress-activated protein kinase 1c"
                     /calculated_mol_wt=43891
     Region          25..360
                     /region_name="STKc_JNK"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     c-Jun N-terminal Kinase; cd07850"
                     /db_xref="CDD:270840"
     Site            order(32..38,40,53,55,72,86,108..114,116..117,151,153,
                     155..156,158,168..169,172,183,185..188,190,227)
                     /site_type="active"
                     /db_xref="CDD:270840"
     Site            order(32..38,40,53,55,86,108..114,158,168)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270840"
     Site            order(72,116,151,153,172,183,185..188,190,227)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270840"
     Site            order(112,118,127,130,159..163,323..324,326,329)
                     /site_type="other"
                     /note="KIM docking site [polypeptide binding]"
                     /db_xref="CDD:270840"
     Site            order(168..178,182..190)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270840"
     CDS             1..384
                     /gene="MAPK8"
                     /gene_synonym="JNK; JNK-46; JNK1; JNK1A2; JNK21B1/2;
                     PRKM8; SAPK1; SAPK1c"
                     /coded_by="NM_001323321.2:195..1349"
                     /note="isoform beta1 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS7226.1"
                     /db_xref="GeneID:5599"
                     /db_xref="HGNC:HGNC:6881"
                     /db_xref="MIM:601158"
ORIGIN      
        1 msrskrdnnf ysveigdstf tvlkryqnlk pigsgaqgiv caaydailer nvaikklsrp
       61 fqnqthakra yrelvlmkcv nhkniiglln vftpqkslee fqdvyivmel mdanlcqviq
      121 meldhermsy llyqmlcgik hlhsagiihr dlkpsnivvk sdctlkildf glartagtsf
      181 mmtpyvvtry yrapevilgm gykenvdiws vgcimgemik ggvlfpgtdh idqwnkvieq
      241 lgtpcpefmk klqptvrtyv enrpkyagys feklfpdvlf padsehnklk asqardllsk
      301 mlvidaskri svdealqhpy invwydpsea eapppkipdk qlderehtie ewkeliykev
      361 mdleertkng virgqpspla qvqq
//
LOCUS       NP_001362945             828 aa            linear   PRI 21-NOV-2025
DEFINITION  protein 4.1 isoform 9 [Homo sapiens].
ACCESSION   NP_001362945 XP_011539265
VERSION     NP_001362945.1
DBSOURCE    REFSEQ: accession NM_001376016.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Terada,N., Saitoh,Y., Saito,M., Yamada,T., Kamijo,A., Yoshizawa,T.
            and Sakamoto,T.
  TITLE     Recent Progress on Genetically Modified Animal Models for Membrane
            Skeletal Proteins: The 4.1 and MPP Families
  JOURNAL   Genes (Basel) 14 (10), 1942 (2023)
   PUBMED   37895291
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 828)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 828)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 828)
  AUTHORS   Dalla Venezia,N., Gilsanz,F., Alloisio,N., Ducluzeau,M.T.,
            Benz,E.J. Jr. and Delaunay,J.
  TITLE     Homozygous 4.1(-) hereditary elliptocytosis associated with a point
            mutation in the downstream initiation codon of protein 4.1 gene
  JOURNAL   J Clin Invest 90 (5), 1713-1717 (1992)
   PUBMED   1430200
REFERENCE   7  (residues 1 to 828)
  AUTHORS   Jons,T. and Drenckhahn,D.
  TITLE     Identification of the binding interface involved in linkage of
            cytoskeletal protein 4.1 to the erythrocyte anion exchanger
  JOURNAL   EMBO J 11 (8), 2863-2867 (1992)
   PUBMED   1639060
REFERENCE   8  (residues 1 to 828)
  AUTHORS   Subrahmanyam,G., Bertics,P.J. and Anderson,R.A.
  TITLE     Phosphorylation of protein 4.1 on tyrosine-418 modulates its
            function in vitro
  JOURNAL   Proc Natl Acad Sci U S A 88 (12), 5222-5226 (1991)
   PUBMED   1647028
REFERENCE   9  (residues 1 to 828)
  AUTHORS   Conboy,J.G., Chan,J.Y., Chasis,J.A., Kan,Y.W. and Mohandas,N.
  TITLE     Tissue- and development-specific alternative RNA splicing regulates
            expression of multiple isoforms of erythroid membrane protein 4.1
  JOURNAL   J Biol Chem 266 (13), 8273-8280 (1991)
   PUBMED   2022644
REFERENCE   10 (residues 1 to 828)
  AUTHORS   Horne,W.C., Prinz,W.C. and Tang,E.K.
  TITLE     Identification of two cAMP-dependent phosphorylation sites on
            erythrocyte protein 4.1
  JOURNAL   Biochim Biophys Acta 1055 (1), 87-92 (1990)
   PUBMED   2171679
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL009181.1, AL138785.8 and
            AL357500.17.
            
            On Nov 7, 2019 this sequence version replaced XP_011539265.1.
            
            Summary: The protein encoded by this gene, together with spectrin
            and actin, constitute the red cell membrane cytoskeletal network.
            This complex plays a critical role in erythrocyte shape and
            deformability. Mutations in this gene are associated with type 1
            elliptocytosis (EL1). Alternatively spliced transcript variants
            encoding different isoforms have been described for this
            gene.[provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.260816.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145313, SAMEA2156670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.3"
     Protein         1..828
                     /product="protein 4.1 isoform 9"
                     /note="protein 4.1; erythrocyte surface protein band 4.1;
                     P4.1; EPB4.1; elliptocytosis 1, RH-linked"
                     /calculated_mol_wt=93868
     Region          1..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11171.4)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:15525677,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Region          77..>204
                     /region_name="WTX"
                     /note="WTX protein; pfam09422"
                     /db_xref="CDD:462794"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48193; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Region          136..170
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11171.4)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Region          182..202
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11171.4)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P11171.4)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Region          211..401
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P48193; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Region          396..489
                     /region_name="FERM_C_4_1_family"
                     /note="FERM domain C-lobe of Protein 4.1 family; cd13184"
                     /db_xref="CDD:270005"
     Site            order(405,422,424,430)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270005"
     Site            order(434,439..442,477,481,484..485)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Site            477..488
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Region          494..614
                     /region_name="Hydrophilic"
                     /note="propagated from UniProtKB/Swiss-Prot (P11171.4)"
     Region          499..542
                     /region_name="FA"
                     /note="FERM adjacent (FA); pfam08736"
                     /db_xref="CDD:462582"
     Region          518..572
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11171.4)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:2171679,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            555
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Region          586..611
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11171.4)"
     Region          615..713
                     /region_name="Spectrin--actin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P11171.4)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by EGFR.
                     /evidence=ECO:0000269|PubMed:1647028,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48193; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Region          667..715
                     /region_name="SAB"
                     /note="SAB domain; pfam04382"
                     /db_xref="CDD:461285"
     Site            674
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            684
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            709
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:2171679,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     Site            712
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:15525677,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11171.4)"
     CDS             1..828
                     /gene="EPB41"
                     /gene_synonym="4.1R; EL1; HE"
                     /coded_by="NM_001376016.1:208..2694"
                     /note="isoform 9 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS90899.1"
                     /db_xref="GeneID:2035"
                     /db_xref="HGNC:HGNC:3377"
                     /db_xref="MIM:130500"
ORIGIN      
        1 mttekslvte aensqhqqke egeeainsgq qepqqeescq taaegdnwce qklkasngdt
       61 pthedltknk ertsesrgls rlfssflkrp ksqvseeegk evesdkekge ggqkeiefgt
      121 sldeeiilka piaapepelk tdpsldlhsl ssaetqpaqe elredpdfei kegegleecs
      181 kievkeespq skaetelkas qkpirkhrnm hckvsllddt vyecvvekha kgqdllkrvc
      241 ehlnlleedy fglaiwdnat sktwldsake ikkqvrgvpw nftfnvkfyp pdpaqltedi
      301 tryylclqlr qdivagrlpc sfatlallgs ytiqselgdy dpelhgvdyv sdfklapnqt
      361 keleekvmel hksyrsmtpa qadleflena kklsmygvdl hkakdlegvd iilgvcssgl
      421 lvykdklrin rfpwpkvlki sykrssffik irpgeqeqye stigfklpsy raakklwkvc
      481 vehhtffrlt stdtipkskf lalgskfrys grtqaqtrqa salidrpaph fertaskras
      541 rsldgaaavd sadrsprpts apaitqgqva eggvldasak ktvvpkaqke tvkaevkked
      601 eppeqaepep teawkvekth ievtvptsng dqtqklaekt edlirmrkkk rerldgeniy
      661 irhsnlmled ldksqeeikk hhasiselkk nfmesvpepr psewdkrlst hspfrtlnin
      721 gqiptgegvk ktsvlpserk vggpetqera llvqdeekik rqersteral pqqeneeilp
      781 kvsipipedh kslkkchlyf stfpspripf mmsflvilvl avwwlvfl
//
LOCUS       NP_001229347             581 aa            linear   PRI 21-NOV-2025
DEFINITION  WD repeat-containing protein 20 isoform 8 [Homo sapiens].
ACCESSION   NP_001229347
VERSION     NP_001229347.1
DBSOURCE    REFSEQ: accession NM_001242418.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Jiang,L., Qi,X., Lai,M., Zhou,J., Yuan,M., You,J., Liu,Q., Pan,J.,
            Zhao,L., Ying,M., Ji,J., Li,K., Zhang,Y., Pan,W., He,Q., Yang,B.
            and Cao,J.
  TITLE     WDR20 prevents hepatocellular carcinoma senescence by orchestrating
            the simultaneous USP12/46-mediated deubiquitination of c-Myc
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2407904121 (2024)
   PUBMED   39432777
  REMARK    GeneRIF: WDR20 prevents hepatocellular carcinoma senescence by
            orchestrating the simultaneous USP12/46-mediated deubiquitination
            of c-Myc.
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Ng,V.H., Spencer,Z., Neitzel,L.R., Nayak,A., Loberg,M.A., Shen,C.,
            Kassel,S.N., Kroh,H.K., An,Z., Anthony,C.C., Bryant,J.M.,
            Lawson,A., Goldsmith,L., Benchabane,H., Hansen,A.G., Li,J.,
            D'Souza,S., Lebensohn,A.M., Rohatgi,R., Weiss,W.A., Weiss,V.L.,
            Williams,C., Hong,C.C., Robbins,D.J., Ahmed,Y. and Lee,E.
  TITLE     The USP46 complex deubiquitylates LRP6 to promote Wnt/beta-catenin
            signaling
  JOURNAL   Nat Commun 14 (1), 6173 (2023)
   PUBMED   37798301
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 581)
  AUTHORS   Olazabal-Herrero,A., Bilbao-Arribas,M., Carlevaris,O., Sendino,M.,
            Varela-Martinez,E., Jugo,B.M., Berra,E. and Rodriguez,J.A.
  TITLE     The dystrophia myotonica WD repeat-containing protein DMWD and
            WDR20 differentially regulate USP12 deubiquitinase
  JOURNAL   FEBS J 288 (20), 5943-5963 (2021)
   PUBMED   33844468
REFERENCE   5  (residues 1 to 581)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 581)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 581)
  AUTHORS   Dahlberg,C.L. and Juo,P.
  TITLE     The WD40-repeat proteins WDR-20 and WDR-48 bind and activate the
            deubiquitinating enzyme USP-46 to promote the abundance of the
            glutamate receptor GLR-1 in the ventral nerve cord of
            Caenorhabditis elegans
  JOURNAL   J Biol Chem 289 (6), 3444-3456 (2014)
   PUBMED   24356955
REFERENCE   8  (residues 1 to 581)
  AUTHORS   Kee,Y., Yang,K., Cohn,M.A., Haas,W., Gygi,S.P. and D'Andrea,A.D.
  TITLE     WDR20 regulates activity of the USP12 x UAF1 deubiquitinating
            enzyme complex
  JOURNAL   J Biol Chem 285 (15), 11252-11257 (2010)
   PUBMED   20147737
  REMARK    GeneRIF: WDR20 serves as a stimulatory subunit for preserving and
            regulating the activity of the subset of the UAF1 x USP12 complexes
REFERENCE   9  (residues 1 to 581)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   10 (residues 1 to 581)
  AUTHORS   Smith,T.F.
  TITLE     Diversity of WD-repeat proteins
  JOURNAL   Subcell Biochem 48, 20-30 (2008)
   PUBMED   18925368
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP363522.1, AL832500.1 and
            BC028387.2.
            
            Summary: This gene encodes a WD repeat-containing protein that
            functions to preserve and regulate the activity of the USP12-UAF1
            deubiquitinating enzyme complex. Multiple alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Jun 2011].
            
            Transcript Variant: This variant (8) uses an alternate in-frame
            splice site in the 5' coding region, and differs in the 3' coding
            region and 3' UTR, compared to variant 1. The encoded isoform (8)
            is the same length but has a distinct C-terminus, compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL832500.1, BX642347.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2145313
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.31"
     Protein         1..581
                     /product="WD repeat-containing protein 20 isoform 8"
                     /note="WD repeat-containing protein 20"
                     /calculated_mol_wt=63912
     Region          114..155
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          165..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <220..326
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          235..271
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          278..311
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..581
                     /gene="WDR20"
                     /gene_synonym="Bun107; DMR"
                     /coded_by="NM_001242418.2:28..1773"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:91833"
                     /db_xref="HGNC:HGNC:19667"
                     /db_xref="MIM:617741"
ORIGIN      
        1 mategggkem neiktqfttr eglykllphs eysrpnrvpf nsqgsnpvrv sfvnlndqsg
       61 ngdrlcfnvg relyfyiykg vrkvptrasp epasgaadls kpidkriykg tqptchdfnh
      121 ltataesvsl lvgfsagqvq lidpikkets klfneerlid ksrvtcvkwv pgseslflva
      181 hssgnmylyn vehtcgttap hyqllkqges favhtcksks trnpllkwtv gegalnefaf
      241 spdgkflacv sqdgflrvfn fdsvelhgtm ksyfggllcv cwspdgkyiv tggeddlvtv
      301 wsfvdcrvia rghghkswvs vvafdpytts veegdpmefs gsdedfqdll hfgrdranst
      361 qsrlskrnst dsrpvsvtyr fgsvgqdtql clwdltedil fphqplsrar thtnvmnats
      421 ppagsngnsv ttpgnsvppp lprsnslphs avsnagskss vmdgaiasgv skfatlslhd
      481 rkerhhekdh krnhsmghis skssdklnlv tktktdpakt lgtplcprme dvplleplic
      541 kkiaherltv lifledcivt acqegfictw grpgkvvsfn p
//
LOCUS       NP_001077086            1591 aa            linear   PRI 21-NOV-2025
DEFINITION  RB1-inducible coiled-coil protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001077086
VERSION     NP_001077086.1
DBSOURCE    REFSEQ: accession NM_001083617.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1591)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 1591)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 1591)
  AUTHORS   Eickhorst,C., Babic,R., Rush-Kittle,J., Lucya,L., Imam,F.L.,
            Sanchez-Martin,P., Hollenstein,D.M., Michaelis,J., Munch,C.,
            Meisinger,C., Slade,D., Gamez-Diaz,L. and Kraft,C.
  TITLE     FIP200 Phosphorylation Regulates Late Steps in Mitophagy
  JOURNAL   J Mol Biol 436 (15), 168631 (2024)
   PUBMED   38821350
  REMARK    GeneRIF: FIP200 Phosphorylation Regulates Late Steps in Mitophagy.
REFERENCE   4  (residues 1 to 1591)
  AUTHORS   Liang,J., Cai,H., Hou,C., Song,F., Jiang,Y., Wang,Z., Qiu,D.,
            Zhu,Y., Wang,F., Yu,D. and Hou,J.
  TITLE     METTL14 inhibits malignant progression of oral squamous cell
            carcinoma by targeting the autophagy-related gene RB1CC1 in an
            m6A-IGF2BP2-dependent manner
  JOURNAL   Clin Sci (Lond) 137 (17), 1373-1389 (2023)
   PUBMED   37615536
  REMARK    GeneRIF: METTL14 inhibits malignant progression of oral squamous
            cell carcinoma by targeting the autophagy-related gene RB1CC1 in an
            m6A-IGF2BP2-dependent manner.
REFERENCE   5  (residues 1 to 1591)
  AUTHORS   Wen,J., Zellner,A., Braun,N.C., Bajaj,T., Gassen,N.C., Peitz,M. and
            Brustle,O.
  TITLE     Loss of function of FIP200 in human pluripotent stem cell-derived
            neurons leads to axonal pathology and hyperactivity
  JOURNAL   Transl Psychiatry 13 (1), 143 (2023)
   PUBMED   37137886
  REMARK    GeneRIF: Loss of function of FIP200 in human pluripotent stem
            cell-derived neurons leads to axonal pathology and hyperactivity.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1591)
  AUTHORS   Chano,T., Kontani,K., Teramoto,K., Okabe,H. and Ikegawa,S.
  TITLE     Truncating mutations of RB1CC1 in human breast cancer
  JOURNAL   Nat Genet 31 (3), 285-288 (2002)
   PUBMED   12068296
  REMARK    GeneRIF: RB1CC1 is frequently mutated in breast cancer and shows
            characteristics of a classical tumor-suppressor gene.
REFERENCE   7  (residues 1 to 1591)
  AUTHORS   Chano,T., Ikegawa,S., Saito-Ohara,F., Inazawa,J., Mabuchi,A.,
            Saeki,Y. and Okabe,H.
  TITLE     Isolation, characterization and mapping of the mouse and human
            RB1CC1 genes
  JOURNAL   Gene 291 (1-2), 29-34 (2002)
   PUBMED   12095676
REFERENCE   8  (residues 1 to 1591)
  AUTHORS   Chano,T., Ikegawa,S., Kontani,K., Okabe,H., Baldini,N. and Saeki,Y.
  TITLE     Identification of RB1CC1, a novel human gene that can induce RB1 in
            various human cells
  JOURNAL   Oncogene 21 (8), 1295-1298 (2002)
   PUBMED   11850849
REFERENCE   9  (residues 1 to 1591)
  AUTHORS   Ueda,H., Abbi,S., Zheng,C. and Guan,J.L.
  TITLE     Suppression of Pyk2 kinase and cellular activities by FIP200
  JOURNAL   J Cell Biol 149 (2), 423-430 (2000)
   PUBMED   10769033
REFERENCE   10 (residues 1 to 1591)
  AUTHORS   Maucuer,A., Camonis,J.H. and Sobel,A.
  TITLE     Stathmin interaction with a putative kinase and coiled-coil-forming
            protein domains
  JOURNAL   Proc Natl Acad Sci U S A 92 (8), 3100-3104 (1995)
   PUBMED   7724523
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA326842.1, D86958.1,
            AC113139.2, AC090814.2 and AB059622.1.
            
            Summary: The protein encoded by this gene interacts with signaling
            pathways to coordinately regulate cell growth, cell proliferation,
            apoptosis, autophagy, and cell migration. This tumor suppressor
            also enhances retinoblastoma 1 gene expression in cancer cells.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. [provided by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region, compared to variant 1,
            resulting in a shorter protein (isoform 2).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript matching the
            genomic sequence was available for the full length of the gene. The
            extent of this transcript is supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2500085.1, D86958.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1591
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.23"
     Protein         1..1591
                     /product="RB1-inducible coiled-coil protein 1 isoform 2"
                     /note="200 kDa FAK family kinase-interacting protein;
                     RB1-inducible coiled-coil protein 1; FAK family
                     kinase-interacting protein of 200 kDa; phosphatase 1,
                     regulatory subunit 131"
                     /calculated_mol_wt=182717
     Region          2..76
                     /region_name="Ubl_RB1CC1"
                     /note="ubiquitin-like (Ubl) domain found in retinoblastoma
                     1-inducible coiled-coil protein 1 (RB1CC1) and similar
                     proteins; cd17060"
                     /db_xref="CDD:340580"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESK9; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESK9; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Region          <404..538
                     /region_name="ATG17_like"
                     /note="Autophagy protein ATG17-like domain; pfam04108"
                     /db_xref="CDD:427715"
     Region          566..569
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Region          638..673
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESK9; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Region          731..737
                     /region_name="FFAT. /evidence=ECO:0000269|PubMed:33124732"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            734
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:33124732; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Region          871..1375
                     /region_name="Mplasa_alph_rch"
                     /note="helix-rich Mycoplasma protein; TIGR04523"
                     /db_xref="CDD:275316"
     Site            1091
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESK9; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            1222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     Region          1439..1585
                     /region_name="ATG11"
                     /note="Autophagy-related protein 11; pfam10377"
                     /db_xref="CDD:463063"
     Site            1484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDY2.3)"
     CDS             1..1591
                     /gene="RB1CC1"
                     /gene_synonym="ATG17; CC1; FIP200; PPP1R131"
                     /coded_by="NM_001083617.2:528..5303"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47856.1"
                     /db_xref="GeneID:9821"
                     /db_xref="HGNC:HGNC:15574"
                     /db_xref="MIM:606837"
ORIGIN      
        1 mklyvflvnt gttltfdtel tvqtvadlkh aiqskykiai qhqvlvvngg ecmaadrrvc
       61 tysagtdtnp iflfnkemil cdrppaipkt tfstendmei kveeslmmpa vfhtvasrtq
      121 lalemyevak klcsfceglv hdehlqhqgw aaimanledc snsyqkllfk fesiysnylq
      181 siediklklt hlgtavsvma kipllecltr hsyreclgrl dslpehedse kaemkrstel
      241 vlspdmprtt neslltsfpk svehvspdta daesgkeire scqstvhqqd ettidtkdgd
      301 lpffnvslld winvqdrpnd veslvrkcfd smsrldprii rpfiaecrqt iakldnqnmk
      361 aikgledrly aldqmiascg rlvneqkela qgflanqkra enlkdasvlp dlclshanql
      421 mimlqnhrkl ldikqkctta kqelannlhv rlkwccfvml hadqdgeklq allrlviell
      481 ervkiveals tvpqmyclav vevvrrkmfi khyrewagal vkdgkrlyea ekskresfgk
      541 lfrksflrnr lfrgldswpp sfctqkprkf dcelpdislk dlqflqsfcp sevqpflrvp
      601 llcdfeplhq hvlalhnlvk aaqsldemsq titdllseqk asvsqtspqs assprmesta
      661 gittttsprt pppltvqdpl cpavcpleel spdsidahtf dfetiphpni eqtihqvsld
      721 ldslaespes dfmsavnefv ieenlsspnp isdpqspemm veslyssvin aidsrrmqdt
      781 nvcgkedfgd htslnvqler crvvaqdshf siqtikedlc hfrtfvqkeq cdfsnslkct
      841 aveirniiek vkcsleitlk ekhqkellsl kneyegkldg liketeenen kikklkgelv
      901 cleevlqnkd nefalvkhek eaviclqnek dqkllemeni mhsqnceike lkqsreivle
      961 dlkklhvend eklqllrael qsleqshlke ledtlqvrhi qefekvmtdh rvsleelkke
     1021 nqqiinqiqe shaeiiqeke kqlqelklkv sdlsdtrckl evelalkeae tdeikillee
     1081 sraqqketlk slleqetenl rteisklnqk iqdnnenyqv glaelrtlmt iekdqcisel
     1141 isrheeesni lkaelnkvts lhnqafeiek nlkeqiielq skldselsal erqkdekitq
     1201 qeekyeaiiq nlekdrqklv ssqeqdreql iqklncekde aiqtalkefk lerevvekel
     1261 lekvkhlenq iakspaidst rgdssslvae lqeklqeeka kfleqleeqe krkneemqnv
     1321 rtsliaeqqt nfntvltrek mrkeniindl sdklkstmqq qerdkdlies lsedrarlle
     1381 ekkkleeevs klrsssfvps pyvatapely gacapelpge sdrsavetad egrvdsamet
     1441 smmsvqenih mlseekqrim llertlqlke eenkrlnqrl msqsmssvss rhsekiaird
     1501 fqvgdlvlii lderhdnyvl ftvsptlyfl hseslpaldl kpasgasrrp wvlgkvmeke
     1561 ycqakkaqnr fkvplgtkfy rvkavswnkk v
//
LOCUS       NP_660295                172 aa            linear   PRI 21-NOV-2025
DEFINITION  pancreatic adenocarcinoma up-regulated factor precursor [Homo
            sapiens].
ACCESSION   NP_660295
VERSION     NP_660295.3
DBSOURCE    REFSEQ: accession NM_145252.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Ghosh,S., Ahearn,C.P., Isabella,C.R., Marando,V.M., Dodge,G.J.,
            Bartlett,H., McPherson,R.L., Dugan,A.E., Jain,S., Neznanova,L.,
            Tettelin,H., Putnik,R., Grimes,C.L., Ruhl,S., Kiessling,L.L. and
            Imperiali,B.
  TITLE     Human oral lectin ZG16B acts as a cell wall polysaccharide probe to
            decode host-microbe interactions with oral commensals
  JOURNAL   Proc Natl Acad Sci U S A 120 (22), e2216304120 (2023)
   PUBMED   37216558
  REMARK    GeneRIF: Human oral lectin ZG16B acts as a cell wall polysaccharide
            probe to decode host-microbe interactions with oral commensals.
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Youn,S.E., Jiang,F., Won,H.Y., Hong,D.E., Kang,T.H., Park,Y.Y. and
            Koh,S.S.
  TITLE     PAUF Induces Migration of Human Pancreatic Cancer Cells Exclusively
            via the TLR4/MyD88/NF-kappaB Signaling Pathway
  JOURNAL   Int J Mol Sci 23 (19), 11414 (2022)
   PUBMED   36232715
  REMARK    GeneRIF: PAUF Induces Migration of Human Pancreatic Cancer Cells
            Exclusively via the TLR4/MyD88/NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Yoo,W., Choi,H., Son,Y.H., Lee,J., Jo,S., Jung,D., Kim,Y.J.,
            Koh,S.S., Yang,Y.R., Kwon,E.S., Lee,K.P., Noh,K.H., Kim,K.W.,
            Ko,Y., Jun,E., Kim,S.C. and Kim,S.
  TITLE     Pancreatic cancer induces muscle wasting by promoting the release
            of pancreatic adenocarcinoma upregulated factor
  JOURNAL   Exp Mol Med 53 (3), 432-445 (2021)
   PUBMED   33731895
  REMARK    GeneRIF: Pancreatic cancer induces muscle wasting by promoting the
            release of pancreatic adenocarcinoma upregulated factor.
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Saitou,M., Gaylord,E.A., Xu,E., May,A.J., Neznanova,L., Nathan,S.,
            Grawe,A., Chang,J., Ryan,W., Ruhl,S., Knox,S.M. and Gokcumen,O.
  TITLE     Functional Specialization of Human Salivary Glands and Origins of
            Proteins Intrinsic to Human Saliva
  JOURNAL   Cell Rep 33 (7), 108402 (2020)
   PUBMED   33207190
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Mullins,J.J., Mullins,L.J., Dunbar,D.R., Brammar,W.J., Gross,K.W.
            and Morley,S.D.
  TITLE     Identification of a human ortholog of the mouse Dcpp gene locus,
            encoding a novel member of the CSP-1/Dcpp salivary protein family
  JOURNAL   Physiol Genomics 28 (1), 129-140 (2006)
   PUBMED   16954406
  REMARK    GeneRIF: Bioinformatic analysis identified a putative human
            CSP-1/Dcpp ortholog, HRPE773, expressed predominantly in human
            salivary tissue, that shows 31% amino acid identity and 45% amino
            acid similarity to the mouse Dcpp query sequence.
REFERENCE   7  (residues 1 to 172)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   8  (residues 1 to 172)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   9  (residues 1 to 172)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 172)
  AUTHORS   Kuster,B., Mortensen,P., Andersen,J.S. and Mann,M.
  TITLE     Mass spectrometry allows direct identification of proteins in large
            genomes
  JOURNAL   Proteomics 1 (5), 641-650 (2001)
   PUBMED   11678034
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005361.1.
            
            On Jul 31, 2020 this sequence version replaced NP_660295.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY359021.1, BP334554.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000382280.8/
                                                ENSP00000371715.4
            RefSeq Select criteria           :: based on manual assertion,
                                                conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..172
                     /product="pancreatic adenocarcinoma up-regulated factor
                     precursor"
                     /note="jacalin-like lectin domain containing 2; pancreatic
                     adenocarcinoma upregulated factor; endocrine and exocrine
                     protein; zymogen granule protein 16 homolog B; pancreatic
                     adenocarcinoma up-regulated factor"
                     /calculated_mol_wt=17214
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1683
     mat_peptide     17..172
                     /product="Pancreatic adenocarcinoma up-regulated factor.
                     /id=PRO_0000248073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DA0.4)"
                     /calculated_mol_wt=17214
     Region          21..148
                     /region_name="Jacalin_ZG16_like"
                     /note="Jacalin-like lectin domain of the zymogen granule
                     protein 16 and related proteins; cd09611"
                     /db_xref="CDD:187707"
     Site            order(24..25,46..47,49,51,69..70,91..93,95,113,136,139,
                     141)
                     /site_type="other"
                     /note="putative sugar binding site [chemical binding]"
                     /db_xref="CDD:187707"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96DA0.4)"
     CDS             1..172
                     /gene="ZG16B"
                     /gene_synonym="EECP; HRPE773; JCLN2; PAUF; PRO1567"
                     /coded_by="NM_145252.3:54..572"
                     /db_xref="CCDS:CCDS10479.3"
                     /db_xref="GeneID:124220"
                     /db_xref="HGNC:HGNC:30456"
                     /db_xref="MIM:620477"
ORIGIN      
        1 mlllltlall ggptwagkmy gpgggkyfst tedydheitg lrvsvglllv ksvqvklgds
       61 wdvklgalgg ntqevtlqpg eyitkvfvaf qaflrgmvmy tskdryfyfg kldgqissay
      121 psqegqvlvg iygqyqllgi ksigfewnyp leeptteppv nltysanspv gr
//
LOCUS       NP_658982                283 aa            linear   PRI 21-NOV-2025
DEFINITION  forkhead box protein I1 isoform b [Homo sapiens].
ACCESSION   NP_658982
VERSION     NP_658982.1
DBSOURCE    REFSEQ: accession NM_144769.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   AitRaise,I., Amalou,G., Bakhchane,A., Bousfiha,A., Abdelghaffar,H.,
            Majida,C., Bonnet,C., Petit,C. and Barakat,A.
  TITLE     Homozygous Missense Variants in FOXI1 and TMPRSS3 Genes Associated
            with Non-syndromic Deafness in Moroccan Families
  JOURNAL   Biochem Genet 62 (3), 1914-1924 (2024)
   PUBMED   37777971
  REMARK    GeneRIF: Homozygous Missense Variants in FOXI1 and TMPRSS3 Genes
            Associated with Non-syndromic Deafness in Moroccan Families.
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Huang,L.H., Zhao,X.L., Cheng,X.H., Yu,Y.D., Wen,C., Li,Y.,
            Wang,X.L., Wang,X.Y., Ruan,Y. and En,H.
  TITLE     [Analysis of genotypes on 850 newborns with SLC26A4 single-allele
            mutation and the phenotypes of those with second variant]
  JOURNAL   Zhonghua Er Bi Yan Hou Tou Jing Wai Ke Za Zhi 58 (2), 117-125
            (2023)
   PUBMED   36748152
  REMARK    GeneRIF: [Analysis of genotypes on 850 newborns with SLC26A4
            single-allele mutation and the phenotypes of those with second
            variant].
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Klarov,L.A., Pshennikova,V.G., Romanov,G.P., Cherdonova,A.M.,
            Solovyev,A.V., Teryutin,F.M., Luginov,N.V., Kotlyarov,P.M. and
            Barashkov,N.A.
  TITLE     Analysis of SLC26A4, FOXI1, and KCNJ10 Gene Variants in Patients
            with Incomplete Partition of the Cochlea and Enlarged Vestibular
            Aqueduct (EVA) Anomalies
  JOURNAL   Int J Mol Sci 23 (23), 15372 (2022)
   PUBMED   36499699
  REMARK    GeneRIF: Analysis of SLC26A4, FOXI1, and KCNJ10 Gene Variants in
            Patients with Incomplete Partition of the Cochlea and Enlarged
            Vestibular Aqueduct (EVA) Anomalies.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Li,J., Kang,H. and Kong,X.
  TITLE     [Diagnosis of a Chinese pedigree affected with autosomal recessive
            deafness 4 with enlarged vestibular aqueduct due to compound
            heterozygous variants of FOXI1 gene]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 39 (10), 1080-1084 (2022)
   PUBMED   36184087
  REMARK    GeneRIF: [Diagnosis of a Chinese pedigree affected with autosomal
            recessive deafness 4 with enlarged vestibular aqueduct due to
            compound heterozygous variants of FOXI1 gene].
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Overdier,D.G., Ye,H., Peterson,R.S., Clevidence,D.E. and Costa,R.H.
  TITLE     The winged helix transcriptional activator HFH-3 is expressed in
            the distal tubules of embryonic and adult mouse kidney
  JOURNAL   J Biol Chem 272 (21), 13725-13730 (1997)
   PUBMED   9153225
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Larsson,C., Hellqvist,M., Pierrou,S., White,I., Enerback,S. and
            Carlsson,P.
  TITLE     Chromosomal localization of six human forkhead genes, freac-1
            (FKHL5), -3 (FKHL7), -4 (FKHL8), -5 (FKHL9), -6 (FKHL10), and -8
            (FKHL12)
  JOURNAL   Genomics 30 (3), 464-469 (1995)
   PUBMED   8825632
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Pierrou,S., Hellqvist,M., Samuelsson,L., Enerback,S. and
            Carlsson,P.
  TITLE     Cloning and characterization of seven human forkhead proteins:
            binding site specificity and DNA bending
  JOURNAL   EMBO J 13 (20), 5002-5012 (1994)
   PUBMED   7957066
REFERENCE   8  (residues 1 to 283)
  AUTHORS   Clevidence,D.E., Overdier,D.G., Tao,W., Qian,X., Pani,L., Lai,E.
            and Costa,R.H.
  TITLE     Identification of nine tissue-specific transcription factors of the
            hepatocyte nuclear factor 3/forkhead DNA-binding-domain family
  JOURNAL   Proc Natl Acad Sci U S A 90 (9), 3948-3952 (1993)
   PUBMED   7683413
REFERENCE   9  (residues 1 to 283)
  AUTHORS   Alexander,R.T., Gil-Pena,H., Greenbaum,L.A. and Santos,F.
  TITLE     Hereditary Distal Renal Tubular Acidosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31600044
REFERENCE   10 (residues 1 to 283)
  AUTHORS   Smith,R.J.H., Azaiez,H. and Odell,A.M.
  TITLE     SLC26A4-Related Sensorineural Hearing Loss
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301640
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008660.5 and BC029778.1.
            
            Summary: This gene belongs to the forkhead family of transcription
            factors, which is characterized by a distinct forkhead domain. This
            gene may play an important role in the development of the cochlea
            and vestibulum, as well as in embryogenesis. The encoded protein
            has been found to be required for the transcription of four
            subunits of a proton pump found in the inner ear, the kidney, and
            the epididymis. Mutations in this gene have been associated with
            deafness, autosomal recessive 4. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            coding segment compared to variant 1, resulting in an isoform (b)
            that lacks an internal portion compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC029778.1, AY707089.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.1"
     Protein         1..283
                     /product="forkhead box protein I1 isoform b"
                     /note="forkhead-related activator 6; forkhead-like 10;
                     hepatocyte nuclear factor 3 forkhead homolog 3;
                     HNF-3/fork-head homolog-3; forkhead box protein I1;
                     forkhead-related protein FKHL10; forkhead-related
                     transcription factor 6"
                     /calculated_mol_wt=30683
     Region          124..191
                     /region_name="FH_FOX"
                     /note="Forkhead (FH) domain found in Forkhead box (FOX)
                     family of transcription factors and similar proteins;
                     cl00061"
                     /db_xref="CDD:469596"
     CDS             1..283
                     /gene="FOXI1"
                     /gene_synonym="FKH10; FKHL10; FREAC-6; FREAC6; HFH-3;
                     HFH3"
                     /coded_by="NM_144769.4:62..913"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47337.1"
                     /db_xref="GeneID:2299"
                     /db_xref="HGNC:HGNC:3815"
                     /db_xref="MIM:601093"
ORIGIN      
        1 mssfdlpaps pprcspqfps igqeppemnl yyenffhpqg vpspqrpsfe gggeygatpn
       61 pylwfngptm tpppylpgpn aspflpqayg vqrpllpsvs glggsdlgwl pipsqeelmk
      121 lvrppysysa liamaihgap dkrltlsqiy qyvadnfpfy nkskagwqns irhnlslndc
      181 fkkvprdedd payvsggspt shplvtpgls pepsdktgqn sltfnsfspl tnlsnhsggg
      241 dwanpmptnm lsyggsvlsq fsphfynsvn tsgvlypreg tev
//
LOCUS       NP_001371605            1136 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 23 [Homo sapiens].
ACCESSION   NP_001371605 XP_016861894
VERSION     NP_001371605.1
DBSOURCE    REFSEQ: accession NM_001384676.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1136)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1136)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1136)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1136)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1136)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1136)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1136)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1136)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1136)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1136)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            On Jun 26, 2020 this sequence version replaced XP_016861894.1.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1628105.1,
                                           SRR14038191.3517732.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1136
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1136
                     /product="microtubule-associated protein 4 isoform 23"
                     /note="MAP-4"
                     /calculated_mol_wt=119270
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          50..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          248..545
                     /region_name="17 X 14 AA tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17693683; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          362..401
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          <575..919
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            580
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P27546; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            696
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10791892,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            723
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            787
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10791892,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            797
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            803
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            825
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            853
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            928
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          977..1007
                     /region_name="Tau/MAP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          977..1006
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            985
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Region          1008..1038
                     /region_name="Tau/MAP 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1008..1037
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          1039..1070
                     /region_name="Tau/MAP 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Region          1039..1069
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Site            1058
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27816.3)"
     Site            1130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     Site            1136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P27816.3)"
     CDS             1..1136
                     /gene="MAP4"
                     /coded_by="NM_001384676.1:96..3506"
                     /note="isoform 23 is encoded by transcript variant 5"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgsp tefleekmay qeypnsqnwp
      121 edtnfcfqpe qvvdpiqtdp fkmyhdddla dlvfpssata dtsifagqnd plkdsygmsp
      181 cntavvpqgw svealnsphs esfvspeava eppqptavpl elakeiemas eerppaqale
      241 immglkttdm apsketemal akdmalatkt evalakdmes ptkldvtlak dmqpsmesdm
      301 alvkdmelpt ekevalvkdv rwptetdvss aknvvlptet evapakdvtl lketeraspi
      361 kmdlapskdm gppkenkket eraspikmdl apskdmgppk enkivpakdl vllseievaq
      421 andiisstei ssaekvalss etevalardm tlppetnvil tkdkalplea evapvkdmaq
      481 lpeteiapak dvapstvkev gllkdmspls etemalgkdv tpppetevvl iknvclppem
      541 evaltedqvp alkteaplak dgvltlannv tpakdvppls eteatpvpik dmeiaqtqkg
      601 isedshlesl qdvgqsaapt fmispetvtg tgkkcslpae edsvleklge rkpcnsqpse
      661 lssetsgiar peegrpvvsg tgndittppn kelppspekk tkplattqpa ktstskaktq
      721 ptslpkqpap ttigglnkkp mslasglvpa appkrpavas arpsilpskd vkpkpiadak
      781 apekraspsk pasapasrsg skstqtvakt ttaaavastg pssrspstll pkkptaikte
      841 gkpaevkkmt aksvpadlsr pkststssmk ktttlsgtap aagvvpsrvk atpmpsrpst
      901 tpfidkkpts akpssttprl srlatntsap dlknvrskak vekkteaaat trkpesnavt
      961 ktagpiasaq kqpagkvqiv skkvsyshiq skcgskdnik hvpgggnvqi qnkkvdiskv
     1021 sskcgskani khkpgggdvk iesqklnfke kaqakvgsld nvghlpagga vktegggsea
     1081 plcpgppage epaiseaape agaptsasgl nghptlsggg dqreaqtlds qiqetn
//
LOCUS       NP_001018169             528 aa            linear   PRI 21-NOV-2025
DEFINITION  NEDD8-activating enzyme E1 regulatory subunit isoform b [Homo
            sapiens].
ACCESSION   NP_001018169
VERSION     NP_001018169.1
DBSOURCE    REFSEQ: accession NM_001018159.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Muffels,I.J.J., Schene,I.F., Rehmann,H., Massink,M.P.G., van der
            Wal,M.M., Bauder,C., Labeur,M., Armando,N.G., Lequin,M.H.,
            Houben,M.L., Giltay,J.C., Haitjema,S., Huisman,A., Vansenne,F.,
            Bluvstein,J., Pappas,J., Shailee,L.V., Zarate,Y.A., Mokry,M., van
            Haaften,G.W., Nieuwenhuis,E.E.S., Refojo,D., van Wijk,F.,
            Fuchs,S.A. and van Hasselt,P.M.
  TITLE     Bi-allelic variants in NAE1 cause intellectual disability,
            ischiopubic hypoplasia, stress-mediated lymphopenia and
            neurodegeneration
  JOURNAL   Am J Hum Genet 110 (1), 146-160 (2023)
   PUBMED   36608681
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 528)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 528)
  AUTHORS   Chen,Y., McPhie,D.L., Hirschberg,J. and Neve,R.L.
  TITLE     The amyloid precursor protein-binding protein APP-BP1 drives the
            cell cycle through the S-M checkpoint and causes apoptosis in
            neurons
  JOURNAL   J Biol Chem 275 (12), 8929-8935 (2000)
   PUBMED   10722740
REFERENCE   7  (residues 1 to 528)
  AUTHORS   Hori,T., Osaka,F., Chiba,T., Miyamoto,C., Okabayashi,K.,
            Shimbara,N., Kato,S. and Tanaka,K.
  TITLE     Covalent modification of all members of human cullin family
            proteins by NEDD8
  JOURNAL   Oncogene 18 (48), 6829-6834 (1999)
   PUBMED   10597293
REFERENCE   8  (residues 1 to 528)
  AUTHORS   Loftus,B.J., Kim,U.J., Sneddon,V.P., Kalush,F., Brandon,R.,
            Fuhrmann,J., Mason,T., Crosby,M.L., Barnstead,M., Cronin,L.,
            Deslattes Mays,A., Cao,Y., Xu,R.X., Kang,H.L., Mitchell,S.,
            Eichler,E.E., Harris,P.C., Venter,J.C. and Adams,M.D.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
   PUBMED   10493829
REFERENCE   9  (residues 1 to 528)
  AUTHORS   Gong,L. and Yeh,E.T.
  TITLE     Identification of the activating and conjugating enzymes of the
            NEDD8 conjugation pathway
  JOURNAL   J Biol Chem 274 (17), 12036-12042 (1999)
   PUBMED   10207026
REFERENCE   10 (residues 1 to 528)
  AUTHORS   Chow,N., Korenberg,J.R., Chen,X.N. and Neve,R.L.
  TITLE     APP-BP1, a novel protein that binds to the carboxyl-terminal region
            of the amyloid precursor protein
  JOURNAL   J Biol Chem 271 (19), 11339-11346 (1996)
   PUBMED   8626687
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM785899.1, BM045535.1 and
            BC000480.2.
            
            Summary: The protein encoded by this gene binds to the beta-amyloid
            precursor protein. Beta-amyloid precursor protein is a cell surface
            protein with signal-transducing properties, and it is thought to
            play a role in the pathogenesis of Alzheimer's disease. In
            addition, the encoded protein can form a heterodimer with UBE1C and
            bind and activate NEDD8, a ubiquitin-like protein. This protein is
            required for cell cycle progression through the S/M checkpoint.
            Three transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) contains an alternate exon
            compared to variant 1. The resulting isoform (b) is shorter and has
            a distinct C-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1551893.1,
                                           SRR14038195.774133.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..528
                     /product="NEDD8-activating enzyme E1 regulatory subunit
                     isoform b"
                     /note="amyloid beta precursor protein-binding protein 1,
                     59kD; amyloid beta precursor protein binding protein 1,
                     59kDa; NEDD8-activating enzyme E1 subunit; amyloid
                     protein-binding protein 1; NEDD8-activating enzyme E1
                     regulatory subunit; protooncogene protein 1; APP-BP1;
                     proto-oncogene protein 1; amyloid beta precursor
                     protein-binding protein 1, 59 kDa"
                     /calculated_mol_wt=59289
     Region          12..526
                     /region_name="APPBP1_RUB"
                     /note="Ubiquitin activating enzyme (E1) subunit APPBP1.
                     APPBP1 is part of the heterodimeric activating enzyme
                     (E1), specific for the Rub family of ubiquitin-like
                     proteins (Ubls). E1 enzymes are part of a conjugation
                     cascade to attach Ub or Ubls, covalently to...; cd01493"
                     /db_xref="CDD:238770"
     CDS             1..528
                     /gene="NAE1"
                     /gene_synonym="A-116A10.1; APPBP1; HPP1; NEDFIH; ula-1"
                     /coded_by="NM_001018159.2:194..1780"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42171.1"
                     /db_xref="GeneID:8883"
                     /db_xref="HGNC:HGNC:621"
                     /db_xref="MIM:603385"
ORIGIN      
        1 mdaqqtktne arlwgdhgqe alesahvcli natatgteil knlvlpgigs ftiidgnqvs
       61 gedagnnffl qrssigknra eaameflqel nsdvsgsfve espenlldnd psffcrftvv
      121 vatqlpests lrladvlwns qipllicrty glvgymriii kehpvieshp dnaledlrld
      181 kpfpelrehf qsydldhmek kdhshtpwiv iiakylaqwy setngripkt ykekedfrdl
      241 irqgilknen gapedeenfe eaiknvntal nttqipssie difnddrcin itkqtpsfwi
      301 laralkefva kegqgnlpvr gtipdmiads gkyiklqnvy rekakkdaaa vgnhvakllq
      361 sigqapesis ekelkllcsn saflrvvrcr slaeeygldt inkdeiissm dnpdneivly
      421 lmlravdrfh kqqgrypgvs nyqveedigk lkscltgflq eyglsvmvkd dyvhefcryg
      481 aaephtiaaf lggaaaqevi kiitkqfvif nntyiysgms qtsatfql
//
LOCUS       NP_001139015             510 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger and SCAN domain-containing protein 18 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001139015
VERSION     NP_001139015.1
DBSOURCE    REFSEQ: accession NM_001145543.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Wang,Y., Luo,Y., Fu,S., He,L., Pan,G., Fan,D., Wen,Q. and Fan,Y.
  TITLE     Zinc finger and SCAN domain-containing protein 18 is a potential
            DNA methylation-modified tumor suppressor and biomarker in breast
            cancer
  JOURNAL   Front Endocrinol (Lausanne) 14, 1095604 (2023)
   PUBMED   37223020
  REMARK    GeneRIF: Zinc finger and SCAN domain-containing protein 18 is a
            potential DNA methylation-modified tumor suppressor and biomarker
            in breast cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Li,B., Ren,B., Ma,G., Cai,F., Wang,P., Zeng,Y., Liu,Y., Zhang,L.,
            Yang,Y., Liang,H., Zhang,R. and Deng,J.
  TITLE     Inactivation of ZSCAN18 by promoter hypermethylation drives the
            proliferation via attenuating TP53INP2-mediated autophagy in
            gastric cancer cells
  JOURNAL   Clin Epigenetics 15 (1), 10 (2023)
   PUBMED   36650573
  REMARK    GeneRIF: Inactivation of ZSCAN18 by promoter hypermethylation
            drives the proliferation via attenuating TP53INP2-mediated
            autophagy in gastric cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   5  (residues 1 to 510)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 510)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 510)
  AUTHORS   Qi,L., Zhou,L., Lu,M., Yuan,K., Li,Z., Wu,G., Huang,X., Shen,Y.,
            Zhao,M., Fu,W., Chu,B., Wang,G., Ren,F., Ma,D. and Chen,J.
  TITLE     Development of a highly specific HER2 monoclonal antibody for
            immunohistochemistry using protein microarray chips
  JOURNAL   Biochem Biophys Res Commun 484 (2), 248-254 (2017)
   PUBMED   28111342
REFERENCE   8  (residues 1 to 510)
  AUTHORS   Vedeld,H.M., Andresen,K., Eilertsen,I.A., Nesbakken,A., Seruca,R.,
            Gladhaug,I.P., Thiis-Evensen,E., Rognum,T.O., Boberg,K.M. and
            Lind,G.E.
  TITLE     The novel colorectal cancer biomarkers CDO1, ZSCAN18 and ZNF331 are
            frequently methylated across gastrointestinal cancers
  JOURNAL   Int J Cancer 136 (4), 844-853 (2015)
   PUBMED   24948044
  REMARK    GeneRIF: A high negative correlation between promoter DNA
            methylation and gene expression was observed for CDO1, ZNF331 and
            ZSCAN18 in gastrointestinal tumors.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY280799.1 and BC006205.2.
            
            Transcript Variant: This variant (4) uses a different segment for
            its 5' UTR and lacks a coding region segment, which results in the
            use of a downstream start codon, compared to variant 1. Variants 3
            and 4 encode the same protein (isoform 3), which is shorter when it
            is compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY280799.1, AK022957.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000601144.6/ ENSP00000468934.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..510
                     /product="zinc finger and SCAN domain-containing protein
                     18 isoform 3"
                     /note="zinc finger protein 447; zinc finger and SCAN
                     domain-containing protein 18"
                     /calculated_mol_wt=54673
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC5.2)"
     Region          45..133
                     /region_name="SCAN"
                     /note="SCAN domain; pfam02023"
                     /db_xref="CDD:460417"
     Region          172..191
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC5.2)"
     Region          201..231
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC5.2)"
     Region          <228..265
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          263..413
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC5.2)"
     Region          316..>400
                     /region_name="katE"
                     /note="hydroperoxidase II; Provisional; PRK11249"
                     /db_xref="CDD:236886"
     Region          415..435
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          443..463
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          461..510
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC5.2)"
     CDS             1..510
                     /gene="ZSCAN18"
                     /gene_synonym="ZNF447"
                     /coded_by="NM_001145543.2:178..1710"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS12971.1"
                     /db_xref="GeneID:65982"
                     /db_xref="HGNC:HGNC:21037"
ORIGIN      
        1 mlplekafas prsspappdl ptpgsaagvq qeepetiper tpadlefsrl rfrefvyqea
       61 agphqtlarl helcrqwlmp earskeqmle llvleqflgi lpdkvrpwvv aqypesckka
      121 aslvegladv leepgmllgs pagsssilsd gvyerhmdpl llpgelasps qalgageipa
      181 psetpwlspd plfleqrrvr eakteedgpa nteqklksfp edpqhlgewg hldpaeenlk
      241 syrklllwgy qlsqpdaasr ldteelrlve rdpqgsslpe ggrrqesagc aceeaapagv
      301 lpelpteapp gdaladppsg tteeeeeqpg kapdpqdpqd aesdsatgsq rqsviqqpap
      361 drgtaklgtk rphpedgdgq slegvsssgd sagleagqgp gadepglsrg kpyacgecge
      421 afawlshlme hhsshggrkr yacqgcwktf hfslalaehq kthekeksya lggargpqps
      481 treaqagara ggppesvege appappeaqr
//
LOCUS       NP_001362662             402 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform jjj [Homo sapiens].
ACCESSION   NP_001362662
VERSION     NP_001362662.1
DBSOURCE    REFSEQ: accession NM_001375733.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 402)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 402)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 402)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.170623.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..402
                     /product="abl interactor 2 isoform jjj"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=42872
     Region          39..100
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          <159..286
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          341..401
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(349,351,354,358,376..377,390,392..393)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..402
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375733.1:122..1330"
                     /note="isoform jjj is encoded by transcript variant 67"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqt vdihkekvar reigilttnk
       61 ntsrthkiia panlerpvry irkpidytil ddighgvkvs tqnmkmgglp rttpptqkpp
      121 sppmsgkgtl gssgssggsh pssrsssren sgsgsvgvpi avptpsppsv fpapagsagt
      181 pplpatsasa paplvpatvp sstapdaaag gaqtladgft sptppvvsst pptghpvqfy
      241 smnrpasrht pptiggslpy rrppsitsqt slqnqmnggp fysqnpvsdt ppppppveep
      301 vfdesppppp ppedyeeeea avveysdpya eedppwaprs ylekvvaiyd ytkdkedels
      361 fqegaiiyvi kknddgwyeg vmngvtglfp gnyvesimhy se
//
LOCUS       NP_955456                431 aa            linear   PRI 21-NOV-2025
DEFINITION  NEDD4-like E3 ubiquitin-protein ligase WWP2 isoform WWP2-C [Homo
            sapiens].
ACCESSION   NP_955456
VERSION     NP_955456.1
DBSOURCE    REFSEQ: accession NM_199424.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Wang,H., Lian,X., Wang,K. and Wang,S.
  TITLE     WWP2 binds to NKRF, enhances the NF-kappaB signaling, and promotes
            malignant phenotypes of acute myeloid leukemia cells
  JOURNAL   Biochem Cell Biol 102 (1), 85-95 (2024)
   PUBMED   37921219
  REMARK    GeneRIF: WWP2 binds to NKRF, enhances the NF-kappaB signaling, and
            promotes malignant phenotypes of acute myeloid leukemia cells.
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Lee,K.T., Pranoto,I.K.A., Kim,S.Y., Choi,H.J., To,N.B., Chae,H.,
            Lee,J.Y., Kim,J.E., Kwon,Y.V. and Nam,J.W.
  TITLE     Comparative interactome analysis of alpha-arrestin families in
            human and Drosophila
  JOURNAL   Elife 12, 88328 (2024)
   PUBMED   38270169
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Chantry,A.
  TITLE     WWP2 ubiquitin ligase and its isoforms: new biological insight and
            promising disease targets
  JOURNAL   Cell Cycle 10 (15), 2437-2439 (2011)
   PUBMED   21750408
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Soond,S.M. and Chantry,A.
  TITLE     Selective targeting of activating and inhibitory Smads by distinct
            WWP2 ubiquitin ligase isoforms differentially modulates TGFbeta
            signalling and EMT
  JOURNAL   Oncogene 30 (21), 2451-2462 (2011)
   PUBMED   21258410
  REMARK    GeneRIF: Data show that the WWP2-N isoform interacts with Smad2 and
            Smad3, whereas WWP2-C interacts only with Smad7.
REFERENCE   6  (residues 1 to 431)
  AUTHORS   McDonald,F.J., Western,A.H., McNeil,J.D., Thomas,B.C., Olson,D.R.
            and Snyder,P.M.
  TITLE     Ubiquitin-protein ligase WWP2 binds to and downregulates the
            epithelial Na(+) channel
  JOURNAL   Am J Physiol Renal Physiol 283 (3), F431-F436 (2002)
   PUBMED   12167593
  REMARK    GeneRIF: expression, binding, and functional data all suggest that
            WWP2 is a candidate to regulate ENaC-mediated Na(+) transport in
            epithelia
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Harvey,K.F., Shearwin-Whyatt,L.M., Fotia,A., Parton,R.G. and
            Kumar,S.
  TITLE     N4WBP5, a potential target for ubiquitination by the Nedd4 family
            of proteins, is a novel Golgi-associated protein
  JOURNAL   J Biol Chem 277 (11), 9307-9317 (2002)
   PUBMED   11748237
REFERENCE   8  (residues 1 to 431)
  AUTHORS   Wood,J.D., Yuan,J., Margolis,R.L., Colomer,V., Duan,K., Kushi,J.,
            Kaminsky,Z., Kleiderlein,J.J., Sharp,A.H. and Ross,C.A.
  TITLE     Atrophin-1, the DRPLA gene product, interacts with two families of
            WW domain-containing proteins
  JOURNAL   Mol Cell Neurosci 11 (3), 149-160 (1998)
   PUBMED   9647693
REFERENCE   9  (residues 1 to 431)
  AUTHORS   Jonsson,A.B.
  TITLE     Identification of a human cDNA clone that mediates adherence of
            pathogenic Neisseria to non-binding cells
  JOURNAL   FEMS Microbiol Lett 162 (1), 25-30 (1998)
   PUBMED   9595660
REFERENCE   10 (residues 1 to 431)
  AUTHORS   Pirozzi,G., McConnell,S.J., Uveges,A.J., Carter,J.M., Sparks,A.B.,
            Kay,B.K. and Fowlkes,D.M.
  TITLE     Identification of novel human WW domain-containing proteins by
            cloning of ligand targets
  JOURNAL   J Biol Chem 272 (23), 14611-14616 (1997)
   PUBMED   9169421
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK126332.1, AK316097.1 and
            JN712744.1.
            
            Summary: This gene encodes a member of the Nedd4 family of E3
            ligases, which play an important role in protein ubiquitination.
            The encoded protein contains four WW domains and may play a role in
            multiple processes including chondrogenesis and the regulation of
            oncogenic signaling pathways via interactions with Smad proteins
            and the tumor suppressor PTEN. Alternatively spliced transcript
            variants encoding multiple isoforms have been observed for this
            gene, and a pseudogene of this gene is located on the long arm of
            chromosome 10. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            large portion of the 5' coding region and initiates translation at
            a downstream, in-frame start codon, compared to variant 1. The
            encoded isoform (WWP2-C) has a shorter N-terminus, compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK126332.1, SRR1803614.56815.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..431
                     /product="NEDD4-like E3 ubiquitin-protein ligase WWP2
                     isoform WWP2-C"
                     /EC_number="2.3.2.26"
                     /note="atrophin-1 interacting protein 2; NEDD4-like E3
                     ubiquitin-protein ligase WWP2; HECT-type E3 ubiquitin
                     transferase WWP2"
                     /calculated_mol_wt=50948
     Region          8..38
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(22,33)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          77..429
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(82,112,123,184,358,393..394,397..401,421,428)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(212,215..216,218..219,222,229,231,234..235,237,243,
                     248,265,269)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..431
                     /gene="WWP2"
                     /gene_synonym="AIP2; WWp2-like"
                     /coded_by="NM_199424.3:530..1825"
                     /note="isoform WWP2-C is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58477.1"
                     /db_xref="GeneID:11060"
                     /db_xref="HGNC:HGNC:16804"
                     /db_xref="MIM:602308"
ORIGIN      
        1 miqepalppg wemkytsegv ryfvdhntrt ttfkdprpgf esgtkqgspg aydrsfrwky
       61 hqfrflchsn alpshvkisv srqtlfedsf qqimnmkpyd lrrrlyiimr geegldyggi
      121 arewffllsh evlnpmyclf eyagknnycl qinpassinp dhltyfrfig rfiamalyhg
      181 kfidtgftlp fykrmlnkrp tlkdlesidp efynsivwik ennleecgle lyfiqdmeil
      241 gkvtthelke ggesirvtee nkeeyimllt dwrftrgvee qtkafldgfn evaplewlry
      301 fdekelelml cgmqeidmsd wqkstiyrhy tknskqiqwf wqvvkemdne krirllqfvt
      361 gtcrlpvggf aeligsngpq kfcidkvgke twlprshtcf nrldlppyks yeqlreklly
      421 aieetegfgq e
//
LOCUS       NP_001120666             172 aa            linear   PRI 21-NOV-2025
DEFINITION  CCHC-type zinc finger nucleic acid binding protein isoform 4 [Homo
            sapiens].
ACCESSION   NP_001120666
VERSION     NP_001120666.1
DBSOURCE    REFSEQ: accession NM_001127194.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Liu,X., Chen,Y., Li,Y., Bai,J., Zeng,Z., Wang,M., Dong,Y. and
            Zhou,Y.
  TITLE     STAU1-mediated CNBP mRNA degradation by LINC00665 alters stem cell
            characteristics in ovarian cancer
  JOURNAL   Biol Direct 19 (1), 59 (2024)
   PUBMED   39080743
  REMARK    GeneRIF: STAU1-mediated CNBP mRNA degradation by LINC00665 alters
            stem cell characteristics in ovarian cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Liu,Y., Jiang,H., Hu,K., Zou,H., Zhang,W., Liu,J. and Jian,X.
  TITLE     CircPRMT5 promotes progression of osteosarcoma by recruiting CNBP
            to regulate the translation and stability of CDK6 mRNA
  JOURNAL   PLoS One 19 (4), e0298947 (2024)
   PUBMED   38626179
  REMARK    GeneRIF: CircPRMT5 promotes progression of osteosarcoma by
            recruiting CNBP to regulate the translation and stability of CDK6
            mRNA.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Gil Rosas,M., Centola,C., Torres,M., Mouguelar,V.S., David,A.P.,
            Piga,E.J., Gomez,D., Calcaterra,N.B., Armas,P. and Coux,G.
  TITLE     The transcription of the main gene associated with Treacher-Collins
            syndrome (TCOF1) is regulated by G-quadruplexes and cellular
            nucleic acid binding protein (CNBP)
  JOURNAL   Sci Rep 14 (1), 7472 (2024)
   PUBMED   38553547
  REMARK    GeneRIF: The transcription of the main gene associated with
            Treacher-Collins syndrome (TCOF1) is regulated by G-quadruplexes
            and cellular nucleic acid binding protein (CNBP).
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Chen,Y., Lei,X., Jiang,Z., Humphries,F., Parsi,K.M., Mustone,N.J.,
            Ramos,I., Mutetwa,T., Fernandez-Sesma,A., Maehr,R., Caffrey,D.R.
            and Fitzgerald,K.A.
  TITLE     Cellular nucleic acid-binding protein restricts SARS-CoV-2 by
            regulating interferon and disrupting RNA-protein condensates
  JOURNAL   Proc Natl Acad Sci U S A 120 (47), e2308355120 (2023)
   PUBMED   37963251
  REMARK    GeneRIF: Cellular nucleic acid-binding protein restricts SARS-CoV-2
            by regulating interferon and disrupting RNA-protein condensates.
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Liu,H., Fang,Y., Hou,B., Lin,Q., Zhang,W., Wang,X., Hu,Y., Xu,G.
            and He,Z.
  TITLE     CircPACRGL promoted cell proliferation, migration and invasion as
            well as inhibited cell apoptosis in colorectal cancer via
            regulation of the miR-330-3p/CNBP axis
  JOURNAL   Mol Cell Biochem 478 (7), 1633-1644 (2023)
   PUBMED   36459268
  REMARK    GeneRIF: CircPACRGL promoted cell proliferation, migration and
            invasion as well as inhibited cell apoptosis in colorectal cancer
            via regulation of the miR-330-3p/CNBP axis.
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Flink,I.L. and Morkin,E.
  TITLE     Organization of the gene encoding cellular nucleic acid-binding
            protein
  JOURNAL   Gene 163 (2), 279-282 (1995)
   PUBMED   7590281
REFERENCE   7  (residues 1 to 172)
  AUTHORS   Warden,C.H., Krisans,S.K., Purcell-Huynh,D., Leete,L.M.,
            Daluiski,A., Diep,A., Taylor,B.A. and Lusis,A.J.
  TITLE     Mouse cellular nucleic acid binding proteins: a highly conserved
            family identified by genetic mapping and sequencing
  JOURNAL   Genomics 24 (1), 14-19 (1994)
   PUBMED   7896269
REFERENCE   8  (residues 1 to 172)
  AUTHORS   Kleefeld,F., Erdmann,H. and Schoser,B.
  TITLE     Myotonic Dystrophy Type 2
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301639
REFERENCE   9  (residues 1 to 172)
  AUTHORS   Lusis,A.J., Rajavashisth,T.B., Klisak,I., Heinzmann,C., Mohandas,T.
            and Sparkes,R.S.
  TITLE     Mapping of the gene for CNBP, a finger protein, to human chromosome
            3q13.3-q24
  JOURNAL   Genomics 8 (2), 411-414 (1990)
   PUBMED   2249857
  REMARK    Erratum:[Genomics 1991 Mar;9(3):564]
REFERENCE   10 (residues 1 to 172)
  AUTHORS   Rajavashisth,T.B., Taylor,A.K., Andalibi,A., Svenson,K.L. and
            Lusis,A.J.
  TITLE     Identification of a zinc finger protein that binds to the sterol
            regulatory element
  JOURNAL   Science 245 (4918), 640-643 (1989)
   PUBMED   2562787
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DQ092367.1, AC108673.11 and
            BU616793.1.
            
            Summary: This gene encodes a nucleic-acid binding protein with
            seven zinc-finger domains. The protein has a preference for binding
            single stranded DNA and RNA. The protein functions in
            cap-independent translation of ornithine decarboxylase mRNA, and
            may also function in sterol-mediated transcriptional regulation. A
            CCTG expansion from <30 repeats to 75-11000 repeats in the first
            intron of this gene results in myotonic dystrophy type 2. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant, also known as beta variant 2,
            uses an alternate in-frame splice site in the 5' coding region,
            compared to variant 1, resulting in a shorter protein (isoform 4).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.352060.1,
                                           SRR1803611.90450.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2155590
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.3"
     Protein         1..172
                     /product="CCHC-type zinc finger nucleic acid binding
                     protein isoform 4"
                     /note="zinc finger protein 273; cellular nucleic
                     acid-binding protein; erythroid differentiation-related;
                     zinc finger protein 9 (a cellular retroviral nucleic acid
                     binding protein); sterol regulatory element-binding
                     protein"
                     /calculated_mol_wt=18839
     Region          <6..84
                     /region_name="PTZ00368"
                     /note="universal minicircle sequence binding protein
                     (UMSBP); Provisional"
                     /db_xref="CDD:173561"
     Region          47..166
                     /region_name="PTZ00368"
                     /note="universal minicircle sequence binding protein
                     (UMSBP); Provisional"
                     /db_xref="CDD:173561"
     CDS             1..172
                     /gene="CNBP"
                     /gene_synonym="CNBP1; DM2; PROMM; RNF163; ZCCHC22; ZNF9"
                     /coded_by="NM_001127194.2:136..654"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS46908.1"
                     /db_xref="GeneID:7555"
                     /db_xref="HGNC:HGNC:13164"
                     /db_xref="MIM:116955"
ORIGIN      
        1 mssnecfkcg rsghwarecp tgggrgrgmr srgrgfqfvs sslpdicyrc gesghlakdc
       61 dlqedveacy ncgrgghiak dckepkrere qccyncgkpg hlardcdhad eqkcyscgef
      121 ghiqkdctkv kcyrcgetgh vaincsktse vncyrcgesg hlarectiea ta
//
LOCUS       NP_001123310            2146 aa            linear   PRI 21-NOV-2025
DEFINITION  voltage-dependent L-type calcium channel subunit alpha-1C isoform
            12 [Homo sapiens].
ACCESSION   NP_001123310
VERSION     NP_001123310.1
DBSOURCE    REFSEQ: accession NM_001129838.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2146)
  AUTHORS   Zhang,X., Liang,X., Cheng,X., Chen,J., Deng,W., Zhang,Y., Cui,L.,
            Cheng,X., Li,X., Yang,C., Ye,B. and Cao,L.
  TITLE     [CACNA1C rs58619945 genotype influences the cortical thickness of
            attention network among patients with Bipolar disorder]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 41 (9), 1045-1052 (2024)
   PUBMED   39217481
  REMARK    GeneRIF: [CACNA1C rs58619945 genotype influences the cortical
            thickness of attention network among patients with Bipolar
            disorder].
REFERENCE   2  (residues 1 to 2146)
  AUTHORS   Yang,Y., Zhu,Z., Hui,L. and Sun,P.
  TITLE     Effects of CACNA1C and ANK3 on cognitive function in patients with
            bipolar disorder
  JOURNAL   Prog Neuropsychopharmacol Biol Psychiatry 133, 111016 (2024)
   PUBMED   38657895
  REMARK    GeneRIF: Effects of CACNA1C and ANK3 on cognitive function in
            patients with bipolar disorder.
REFERENCE   3  (residues 1 to 2146)
  AUTHORS   Almodovar-Paya,C., Guardiola-Ripoll,M., Giralt-Lopez,M.,
            Oscoz-Irurozqui,M., Canales-Rodriguez,E.J., Madre,M.,
            Soler-Vidal,J., Ramiro,N., Callado,L.F., Arias,B., Gallego,C.,
            Pomarol-Clotet,E. and Fatjo-Vilas,M.
  TITLE     NRN1 epistasis with BDNF and CACNA1C: mediation effects on symptom
            severity through neuroanatomical changes in schizophrenia
  JOURNAL   Brain Struct Funct 229 (5), 1299-1315 (2024)
   PUBMED   38720004
  REMARK    GeneRIF: NRN1 epistasis with BDNF and CACNA1C: mediation effects on
            symptom severity through neuroanatomical changes in schizophrenia.
REFERENCE   4  (residues 1 to 2146)
  AUTHORS   Gao,S., Yao,X., Chen,J., Huang,G., Fan,X., Xue,L., Li,Z., Wu,T.,
            Zheng,Y., Huang,J., Jin,X., Wang,Y., Wang,Z., Yu,Y., Liu,L.,
            Pan,X., Song,C. and Yan,N.
  TITLE     Structural basis for human Cav1.2 inhibition by multiple drugs and
            the neurotoxin calciseptine
  JOURNAL   Cell 186 (24), 5363-5374 (2023)
   PUBMED   37972591
  REMARK    GeneRIF: Structural basis for human Cav1.2 inhibition by multiple
            drugs and the neurotoxin calciseptine.
REFERENCE   5  (residues 1 to 2146)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   6  (residues 1 to 2146)
  AUTHORS   Napolitano,C. and Priori,S.G.
  TITLE     CACNA1C-Related Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301577
REFERENCE   7  (residues 1 to 2146)
  AUTHORS   Groffen,A.J., Bikker,H. and Christiaans,I.
  TITLE     Long QT Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301308
REFERENCE   8  (residues 1 to 2146)
  AUTHORS   Sun,W., McPherson,J.D., Hoang,D.Q., Wasmuth,J.J., Evans,G.A. and
            Montal,M.
  TITLE     Mapping of a human brain voltage-gated calcium channel to human
            chromosome 12p13-pter
  JOURNAL   Genomics 14 (4), 1092-1094 (1992)
   PUBMED   1335957
REFERENCE   9  (residues 1 to 2146)
  AUTHORS   Powers,P.A., Gregg,R.G. and Hogan,K.
  TITLE     Linkage mapping of the human gene for the alpha 1 subunit of the
            cardiac DHP-sensitive Ca2+ channel (CACNL1A1) to chromosome
            12p13.2-pter using a dinucleotide repeat
  JOURNAL   Genomics 14 (1), 206-207 (1992)
   PUBMED   1330882
REFERENCE   10 (residues 1 to 2146)
  AUTHORS   Soldatov,N.M.
  TITLE     Molecular diversity of L-type Ca2+ channel transcripts in human
            fibroblasts
  JOURNAL   Proc Natl Acad Sci U S A 89 (10), 4628-4632 (1992)
   PUBMED   1316612
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005342.1, Z34813.1 and
            AC007618.21.
            
            Summary: This gene encodes an alpha-1 subunit of a
            voltage-dependent calcium channel. Calcium channels mediate the
            influx of calcium ions into the cell upon membrane polarization.
            The alpha-1 subunit consists of 24 transmembrane segments and forms
            the pore through which ions pass into the cell. The calcium channel
            consists of a complex of alpha-1, alpha-2/delta, beta, and gamma
            subunits in a 1:1:1:1 ratio. There are multiple isoforms of each of
            these proteins, either encoded by different genes or the result of
            alternative splicing of transcripts. The protein encoded by this
            gene binds to and is inhibited by dihydropyridine. Alternative
            splicing results in many transcript variants encoding different
            proteins. Some of the predicted proteins may not produce functional
            ion channel subunits. [provided by RefSeq, Oct 2012].
            
            Transcript Variant: This variant (12), also referred to has HLCC74,
            lacks four alternate in-frame exons and uses an alternate in-frame
            splice site in the 3' coding region, compared to variant 1,
            resulting in a shorter protein (isoform 12), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z34813.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2147975
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2146
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..2146
                     /product="voltage-dependent L-type calcium channel subunit
                     alpha-1C isoform 12"
                     /note="calcium channel, cardic dihydropyridine-sensitive,
                     alpha-1 subunit; DHPR, alpha-1 subunit; voltage-dependent
                     L-type Ca2+ channel alpha 1 subunit; calcium channel,
                     voltage-dependent, L type, alpha 1C subunit; CACNA1C
                     intronic transcript 2; CACNA1C intronic transcript 2
                     (non-protein coding)"
                     /calculated_mol_wt=240163
     Region          123..416
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          523..764
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          899..1176
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          1218..1476
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          1485..1538
                     /region_name="GPHH"
                     /note="Voltage-dependent L-type calcium channel,
                     IQ-associated; pfam16905"
                     /db_xref="CDD:465306"
     Region          1548..1641
                     /region_name="Ca_chan_IQ"
                     /note="Voltage gated calcium channel IQ domain; pfam08763"
                     /db_xref="CDD:462591"
     Region          1661..2096
                     /region_name="CAC1F_C"
                     /note="Voltage-gated calcium channel subunit alpha,
                     C-term; pfam16885"
                     /db_xref="CDD:465298"
     CDS             1..2146
                     /gene="CACNA1C"
                     /gene_synonym="CACH2; CACN2; CACNA1C-IT2; CACNL1A1;
                     CaV1.2; CCHL1A1; LQT8; NEDHLSS; TS; TS. LQT8"
                     /coded_by="NM_001129838.2:577..7017"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS44801.1"
                     /db_xref="GeneID:775"
                     /db_xref="HGNC:HGNC:1390"
                     /db_xref="MIM:114205"
ORIGIN      
        1 mvnentrmyi peenhqgsny gsprpahanm nanaaaglap ehiptpgaal swqaaidaar
       61 qaklmgsagn atistvsstq rkrqqygkpk kqgsttatrp prallcltlk npirracisi
      121 vewkpfeiii lltifancva laiyipfped dsnatnsnle rveylfliif tveaflkvia
      181 ygllfhpnay lrngwnlldf iivvvglfsa ileqatkadg analggkgag fdvkalrafr
      241 vlrplrlvsg vpslqvvlns iikamvpllh iallvlfvii iyaiiglelf mgkmhktcyn
      301 qegiadvpae ddpspcalet ghgrqcqngt vckpgwdgpk hgitnfdnfa famltvfqci
      361 tmegwtdvly wvndavgrdw pwiyfvtlii igsffvlnlv lgvlsgefsk erekakargd
      421 fqklrekqql eedlkgyldw itqaedidpe nedegmdeek prnmsmptse tesvntenva
      481 ggdiegencg arlahrisks kfsrywrrwn rfcrrkcraa vksnvfywlv iflvflntlt
      541 iasehynqpn wltevqdtan kallalftae mllkmyslgl qayfvslfnr fdcfvvcggi
      601 letilvetki msplgisvlr cvrllrifki trywnslsnl vasllnsvrs iaslllllfl
      661 fiiifsllgm qlfggkfnfd emqtrrstfd nfpqslltvf qiltgedwns vmydgimayg
      721 gpsfpgmlvc iyfiilficg nyillnvfla iavdnladae sltsaqkeee eekerkklar
      781 taspekkqel vekpavgesk eekielksit adgesppatk inmddlqpne nedkspypnp
      841 ettgeedeee pempvgprpr plselhlkek avpmpeasaf fifssnnrfr lqchrivndt
      901 iftnlilffi llssislaae dpvqhtsfrn hilgnadyvf tsiftleiil kmtaygaflh
      961 kgsfcrnyfn ildllvvsvs lisfgiqssa invvkilrvl rvlrplrain rakglkhvvq
     1021 cvfvairtig nivivttllq fmfacigvql fkgklytcsd sskqteaeck gnyitykdge
     1081 vdhpiiqprs wenskfdfdn vlaammalft vstfegwpel lyrsidshte dkgpiynyrv
     1141 eisiffiiyi iiiaffmmni fvgfvivtfq eqgeqeyknc eldknqrqcv eyalkarplr
     1201 ryipknqhqy kvwyvvnsty feylmfvlil lnticlamqh ygqsclfkia mnilnmlftg
     1261 lftvemilkl iafkpkhyfc dawntfdali vvgsivdiai tevnnaeens risitffrlf
     1321 rvmrlvklls rgegirtllw tfiksfqalp yvallivmlf fiyavigmqv fgkialndtt
     1381 einrnnnfqt fpqavlllfr catgeawqdi mlacmpgkkc apesepsnst egetpcgssf
     1441 avfyfisfym lcafliinlf vavimdnfdy ltrdwsilgp hhldefkriw aeydpeakgr
     1501 ikhldvvtll rriqpplgfg klcphrvack rlvsmnmpln sdgtvmfnat lfalvrtalr
     1561 ikteegpsps eahqgaedpf rpagnleqan eelraiikki wkrtsmklld qvvppagdde
     1621 vtvgkfyatf liqeyfrkfk krkeqglvgk psqrnalslq aglrtlhdig peirraisgd
     1681 ltaeeeldka mkeavsaase ddifrraggl fgnhvsyyqs dgrsafpqtf ttqrplhink
     1741 agssqgdtes psheklvdst ftpssysstg snaninnann talgrlprpa gypstvstve
     1801 ghgpplspai rvqevawkls snrchsresq aamagqeets qdetyevkmn hdteacseps
     1861 llstemlsyq ddenrqltlp eedkrdirqs pkrgflrsas lgrrasfhle clkrqkdrgg
     1921 disqktvlpl hlvhhqalav aglspllqrs hspasfprpf atppatpgsr gwppqpvptl
     1981 rlegvessek lnssfpsihc gswaettpgg ggssaarrvr pvslmvpsqa gapgrqfhgs
     2041 asslveavli seglgqfaqd pkfievttqe ladacdmtie emesaadnil sggapqspng
     2101 allpfvncrd agqdraggee dagcvrargr pseeelqdsr vyvssl
//
LOCUS       NP_001252524             129 aa            linear   PRI 21-NOV-2025
DEFINITION  prefoldin subunit 6 [Homo sapiens].
ACCESSION   NP_001252524
VERSION     NP_001252524.1
DBSOURCE    REFSEQ: accession NM_001265595.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Frommelt,F., Fossati,A., Uliana,F., Wendt,F., Xue,P., Heusel,M.,
            Wollscheid,B., Aebersold,R., Ciuffa,R. and Gstaiger,M.
  TITLE     DIP-MS: ultra-deep interaction proteomics for the deconvolution of
            protein complexes
  JOURNAL   Nat Methods 21 (4), 635-647 (2024)
   PUBMED   38532014
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Herranz-Montoya,I., Park,S. and Djouder,N.
  TITLE     A comprehensive analysis of prefoldins and their implication in
            cancer
  JOURNAL   iScience 24 (11), 103273 (2021)
   PUBMED   34761191
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Liang,J., Xia,L., Oyang,L., Lin,J., Tan,S., Yi,P., Han,Y., Luo,X.,
            Wang,H., Tang,L., Pan,Q., Tian,Y., Rao,S., Su,M., Shi,Y., Cao,D.,
            Zhou,Y. and Liao,Q.
  TITLE     The functions and mechanisms of prefoldin complex and
            prefoldin-subunits
  JOURNAL   Cell Biosci 10, 87 (2020)
   PUBMED   32699605
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 129)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 129)
  AUTHORS   Simons,C.T., Staes,A., Rommelaere,H., Ampe,C., Lewis,S.A. and
            Cowan,N.J.
  TITLE     Selective contribution of eukaryotic prefoldin subunits to actin
            and tubulin binding
  JOURNAL   J Biol Chem 279 (6), 4196-4203 (2004)
   PUBMED   14634002
REFERENCE   7  (residues 1 to 129)
  AUTHORS   Hansen,W.J., Cowan,N.J. and Welch,W.J.
  TITLE     Prefoldin-nascent chain complexes in the folding of cytoskeletal
            proteins
  JOURNAL   J Cell Biol 145 (2), 265-277 (1999)
   PUBMED   10209023
REFERENCE   8  (residues 1 to 129)
  AUTHORS   Vainberg,I.E., Lewis,S.A., Rommelaere,H., Ampe,C.,
            Vandekerckhove,J., Klein,H.L. and Cowan,N.J.
  TITLE     Prefoldin, a chaperone that delivers unfolded proteins to cytosolic
            chaperonin
  JOURNAL   Cell 93 (5), 863-873 (1998)
   PUBMED   9630229
REFERENCE   9  (residues 1 to 129)
  AUTHORS   Herberg,J.A., Beck,S. and Trowsdale,J.
  TITLE     TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form
            a dense cluster at the centromeric end of the MHC
  JOURNAL   J Mol Biol 277 (4), 839-857 (1998)
   PUBMED   9545376
REFERENCE   10 (residues 1 to 129)
  AUTHORS   Herberg,J.A., Sgouros,J., Jones,T., Copeman,J., Humphray,S.J.,
            Sheer,D., Cresswell,P., Beck,S. and Trowsdale,J.
  TITLE     Genomic analysis of the Tapasin gene, located close to the TAP loci
            in the MHC
  JOURNAL   Eur J Immunol 28 (2), 459-467 (1998)
   PUBMED   9521053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM818422.1 and BE794658.1.
            
            Summary: PFDN6 is a subunit of the heteromeric prefoldin complex
            that chaperones nascent actin (see MIM 102560) and alpha- and
            beta-tubulin (see MIM 602529 and MIM 191130, respectively) chains
            pending their transfer to the cytosolic chaperonin containing TCP1
            (MIM 186980) (CCT) complex (Hansen et al., 1999 [PubMed
            10209023]).[supplied by OMIM, Jul 2010].
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. All variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM818422.1, BM759317.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.32"
     Protein         1..129
                     /product="prefoldin subunit 6"
                     /note="KE2 protein; HLA class II region expressed gene
                     KE2"
                     /calculated_mol_wt=14452
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O15212.1)"
     Region          13..113
                     /region_name="Prefoldin_6"
                     /note="Prefoldin subunit 6; cd23161"
                     /db_xref="CDD:467477"
     Site            order(13,16,24..30,32,60,70..71,73..75,77..79,81..82,
                     84..86,88..90,92..93,108..113)
                     /site_type="other"
                     /note="prefoldin beta subunit /TRiC interface [polypeptide
                     binding]"
                     /db_xref="CDD:467477"
     Region          13..50
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467477"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O15212.1)"
     Site            order(36,39..40,42..43,45..47,49,53..68,71..72,79,83)
                     /site_type="other"
                     /note="prefoldin oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467477"
     Site            66
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O15212.1)"
     Region          70..113
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467477"
     CDS             1..129
                     /gene="PFDN6"
                     /gene_synonym="H2-KE2; HKE2; KE-2; PFD6"
                     /coded_by="NM_001265595.2:111..500"
                     /db_xref="CCDS:CCDS4773.1"
                     /db_xref="GeneID:10471"
                     /db_xref="HGNC:HGNC:4926"
                     /db_xref="MIM:605660"
ORIGIN      
        1 maeliqkklq gevekyqqlq kdlsksmsgr qkleaqlten nivkeelall dgsnvvfkll
       61 gpvlvkqelg earatvgkrl dyitaeikry esqlrdlerq seqqretlaq lqqefqraqa
      121 akagapgka
//
LOCUS       NP_001371506             694 aa            linear   PRI 21-NOV-2025
DEFINITION  protein Smaug homolog 2 isoform a [Homo sapiens].
ACCESSION   NP_001371506 XP_016882410
VERSION     NP_001371506.1
DBSOURCE    REFSEQ: accession NM_001384577.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 694)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 694)
  AUTHORS   Wu,C., Liu,X., Li,B., Sun,G., Peng,C. and Xiang,D.
  TITLE     miR-451 suppresses the malignant characteristics of colorectal
            cancer via targeting SAMD4B
  JOURNAL   Mol Med Rep 24 (2) (2021)
   PUBMED   34109425
  REMARK    GeneRIF: miR451 suppresses the malignant characteristics of
            colorectal cancer via targeting SAMD4B.
REFERENCE   6  (residues 1 to 694)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   7  (residues 1 to 694)
  AUTHORS   Baez,M.V. and Boccaccio,G.L.
  TITLE     Mammalian Smaug is a translational repressor that forms cytoplasmic
            foci similar to stress granules
  JOURNAL   J Biol Chem 280 (52), 43131-43140 (2005)
   PUBMED   16221671
REFERENCE   8  (residues 1 to 694)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   9  (residues 1 to 694)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 694)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011445.6 and AC005239.1.
            
            On Jun 20, 2020 this sequence version replaced XP_016882410.1.
            
            Transcript Variant: This variant (13) differs in the 5' UTR
            compared to variant 1. Variants 1 and 3-14 all encode the same
            isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853565.15317.1,
                                           SRR11853567.15589.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..694
                     /product="protein Smaug homolog 2 isoform a"
                     /note="smaug homolog B; protein Smaug homolog 2; smaug 2;
                     SAM domain-containing protein 4B; sterile alpha motif
                     domain-containing protein 4B"
                     /calculated_mol_wt=75353
     Region          158..301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XS6; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XS6; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XS6; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Region          296..358
                     /region_name="SAM_Smaug"
                     /note="SAM domain of Smaug subfamily; cd09557"
                     /db_xref="CDD:188956"
     Site            order(312,314..315,343,346..348,355,357)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:188956"
     Region          407..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            555
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            592
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            600
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            602
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Region          607..643
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5PRF9.1)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5PRF9.1)"
     CDS             1..694
                     /gene="SAMD4B"
                     /gene_synonym="Smaug2; SMGB"
                     /coded_by="NM_001384577.1:362..2446"
                     /note="isoform a is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS33020.1"
                     /db_xref="GeneID:55095"
                     /db_xref="HGNC:HGNC:25492"
                     /db_xref="MIM:619231"
ORIGIN      
        1 mmfrdqvgil agwfkgwnec eqtvallsll krvtrtqarf lqlclehsla dcndihlles
       61 eansaaivsq wqqeskekvv slllshlpll qpgnteakse ymrllqkvla ysiesnafie
      121 esrqllsyal ihpattledr nalalwlshl eerlasgfrs rpepsyhsrq gsdewggpae
      181 lgpgeagpgw qdkpprengh vpfhpsssvp painsigsna ntglpcqihp splkrsmsli
      241 ptspqvpgew pspeelgara afttpdhapl spqssvassg seqteeqgss rntfqedgsg
      301 mkdvpswlks lrlhkyaalf sqmsyeemmt lteqhlesqn vtkgarhkia lsiqklrerq
      361 svlkslekdv leggnlrnal qelqqiiitp ikaysvlqat vaaatttpta kdgapgeppl
      421 pgaepplahp gtdkgteakd ppavenyppp papaptdgse papapvadgd ipsqftrvmg
      481 kvctqllvsr pdeenitsyl qliekclthe aftetqkkrl lswkqqvlkl lrtfprkaal
      541 emqnyrqqkg wafgsnslpi agsvgmgvar rtqrqfpmpp ralppgrmgl lspsgiggvs
      601 prhaltspsl ggqgrqnlwf anpggsnsmp sqsrssvqrt hslpvhsspq ailmfppdcp
      661 vpgpdleinp tleslclsmt ehalgdgtdk tsti
//
LOCUS       NP_001308762             647 aa            linear   PRI 21-NOV-2025
DEFINITION  cleavage and polyadenylation specificity factor subunit 3 isoform b
            [Homo sapiens].
ACCESSION   NP_001308762 XP_005246225
VERSION     NP_001308762.1
DBSOURCE    REFSEQ: accession NM_001321833.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Zhang,Y., Liu,D., Guo,D., Lin,W., Lu,W., Hu,L., Chen,S. and Chen,C.
  TITLE     CPSF3 regulates alternative polyadenylation of CNIH2 to promote
            esophageal squamous cell carcinoma progression
  JOURNAL   Cancer Lett 593, 216925 (2024)
   PUBMED   38718887
  REMARK    GeneRIF: CPSF3 regulates alternative polyadenylation of CNIH2 to
            promote esophageal squamous cell carcinoma progression.
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Alahmari,A.A., Chaubey,A.H., Jonnakuti,V.S., Tisdale,A.A.,
            Schwarz,C.D., Cornwell,A.C., Maraszek,K.E., Paterson,E.J., Kim,M.,
            Venkat,S., Gomez,E.C., Wang,J., Gurova,K.V., Yalamanchili,H.K. and
            Feigin,M.E.
  TITLE     CPSF3 inhibition blocks pancreatic cancer cell proliferation
            through disruption of core histone mRNA processing
  JOURNAL   RNA 30 (3), 281-297 (2024)
   PUBMED   38191171
  REMARK    GeneRIF: CPSF3 inhibition blocks pancreatic cancer cell
            proliferation through disruption of core histone mRNA processing.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Shen,P., Ye,K., Xiang,H., Zhang,Z., He,Q., Zhang,X., Cai,M.C.,
            Chen,J., Sun,Y., Lin,L., Qi,C., Zhang,M., Cheung,L.W.T., Shi,T.,
            Yin,X., Li,Y., Di,W., Zang,R., Tan,L. and Zhuang,G.
  TITLE     Therapeutic targeting of CPSF3-dependent transcriptional
            termination in ovarian cancer
  JOURNAL   Sci Adv 9 (47), eadj0123 (2023)
   PUBMED   37992178
  REMARK    GeneRIF: Therapeutic targeting of CPSF3-dependent transcriptional
            termination in ovarian cancer.
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Huang,J., Liu,X., Sun,Y., Li,Z., Lin,M.H., Hamilton,K.,
            Mandel,C.R., Sandmeir,F., Conti,E., Oyala,P.H. and Tong,L.
  TITLE     An examination of the metal ion content in the active sites of
            human endonucleases CPSF73 and INTS11
  JOURNAL   J Biol Chem 299 (4), 103047 (2023)
   PUBMED   36822327
  REMARK    GeneRIF: An examination of the metal ion content in the active
            sites of human endonucleases CPSF73 and INTS11.
REFERENCE   5  (residues 1 to 647)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   6  (residues 1 to 647)
  AUTHORS   McCracken,S., Fong,N., Yankulov,K., Ballantyne,S., Pan,G.,
            Greenblatt,J., Patterson,S.D., Wickens,M. and Bentley,D.L.
  TITLE     The C-terminal domain of RNA polymerase II couples mRNA processing
            to transcription
  JOURNAL   Nature 385 (6614), 357-361 (1997)
   PUBMED   9002523
REFERENCE   7  (residues 1 to 647)
  AUTHORS   Jenny,A., Minvielle-Sebastia,L., Preker,P.J. and Keller,W.
  TITLE     Sequence similarity between the 73-kilodalton protein of mammalian
            CPSF and a subunit of yeast polyadenylation factor I
  JOURNAL   Science 274 (5292), 1514-1517 (1996)
   PUBMED   8929409
REFERENCE   8  (residues 1 to 647)
  AUTHORS   Murthy,K.G. and Manley,J.L.
  TITLE     The 160-kD subunit of human cleavage-polyadenylation specificity
            factor coordinates pre-mRNA 3'-end formation
  JOURNAL   Genes Dev 9 (21), 2672-2683 (1995)
   PUBMED   7590244
REFERENCE   9  (residues 1 to 647)
  AUTHORS   Jenny,A., Hauri,H.P. and Keller,W.
  TITLE     Characterization of cleavage and polyadenylation specificity factor
            and cloning of its 100-kilodalton subunit
  JOURNAL   Mol Cell Biol 14 (12), 8183-8190 (1994)
   PUBMED   7969155
REFERENCE   10 (residues 1 to 647)
  AUTHORS   Thuresson,A.C., Astrom,J., Astrom,A., Gronvik,K.O. and Virtanen,A.
  TITLE     Multiple forms of poly(A) polymerases in human cells
  JOURNAL   Proc Natl Acad Sci U S A 91 (3), 979-983 (1994)
   PUBMED   8302877
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC420903.1, DA455023.1,
            BC014106.1 and AA635764.1.
            
            On Mar 31, 2016 this sequence version replaced XP_005246225.1.
            
            Summary: This gene encodes a member of the metallo-beta-lactamase
            family. The encoded protein is a 73kDa subunit of the cleavage and
            polyadenylation specificity factor and functions as an endonuclease
            that recognizes the pre-mRNA 3'-cleavage site AAUAAA prior to
            polyadenylation. It also cleaves after the pre-mRNA sequence ACCCA
            during histone 3'-end pre-mRNA processing. [provided by RefSeq, Oct
            2012].
            
            Transcript Variant: This variant (2) and variant 3 both encode the
            same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.248371.1,
                                           SRR14038194.1727071.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.1"
     Protein         1..647
                     /product="cleavage and polyadenylation specificity factor
                     subunit 3 isoform b"
                     /note="cleavage and polyadenylation specificity factor
                     subunit 3; mRNA 3'-end-processing endonuclease CPSF-73;
                     cleavage and polyadenylation specific factor 3, 73kDa"
                     /calculated_mol_wt=73347
     Region          1..419
                     /region_name="COG1782"
                     /note="Predicted metal-dependent RNase, contains
                     metallo-beta-lactamase and KH domains [General function
                     prediction only]"
                     /db_xref="CDD:441388"
     Region          1..168
                     /region_name="CPSF3-like_MBL-fold"
                     /note="cleavage and polyadenylation specificity factor
                     (CPSF) subunit 3 and related proteins; MBL-fold
                     metallo-hydrolase domain; cd16292"
                     /db_xref="CDD:293850"
     Site            order(34,36,38..39,121,142)
                     /site_type="active"
                     /db_xref="CDD:293850"
     Region          442..645
                     /region_name="CPSF73-100_C"
                     /note="Pre-mRNA 3'-end-processing endonuclease
                     polyadenylation factor C-term; pfam11718"
                     /db_xref="CDD:463330"
     CDS             1..647
                     /gene="CPSF3"
                     /gene_synonym="CPSF-73; CPSF73; NEDMHS; NEDMHSN"
                     /coded_by="NM_001321833.2:461..2404"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS82417.1"
                     /db_xref="GeneID:51692"
                     /db_xref="HGNC:HGNC:2326"
                     /db_xref="MIM:606029"
ORIGIN      
        1 mldcgihpgl egmdalpyid lidpaeidll lishfhldhc galpwflqkt sfkgrtfmth
       61 atkaiyrwll sdyvkvsnis addmlytetd leesmdkiet infhevkeva gikfwcyhag
      121 hvlgaamfmi eiagvkllyt gdfsrqedrh lmaaeipnik pdiliiesty gthihekree
      181 rearfcntvh divnrggrgl ipvfalgraq elllildeyw qnhpelhdip iyyasslakk
      241 cmavyqtyvn amndkirkqi ninnpfvfkh isnlksmdhf ddigpsvvma spgmmqsgls
      301 relfeswctd krngviiagy cvegtlakhi msepeeittm sgqklplkms vdyisfsaht
      361 dyqqtsefir alkpphvilv hgeqnemarl kaalireyed ndevhievhn prnteavtln
      421 frgeklakvm gfladkkpeq gqrvsgilvk rnfnyhilsp cdlsnytdla mstvkqtqai
      481 pytgpfnllc yqlqkltgdv eeleiqekpa lkvfknitvi qepgmvvlew lanpsndmya
      541 dtvttvilev qsnpkirkga vqkvskklem hvyskrleim lqdifgedcv svkddsilsv
      601 tvdgktanln letrtvecee gseddeslre mvelaaqrly ealtpvh
//
LOCUS       NP_001128648             660 aa            linear   PRI 21-NOV-2025
DEFINITION  protein NEDD1 isoform b [Homo sapiens].
ACCESSION   NP_001128648
VERSION     NP_001128648.1
DBSOURCE    REFSEQ: accession NM_001135176.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Timon Perez,K., Scrofani,J. and Vernos,I.
  TITLE     NEDD1-S411 phosphorylation plays a critical function in the
            coordination of microtubule nucleation during mitosis
  JOURNAL   Biol Open 11 (11) (2022)
   PUBMED   36318115
  REMARK    GeneRIF: NEDD1-S411 phosphorylation plays a critical function in
            the coordination of microtubule nucleation during mitosis.
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Chi,W., Wang,G., Xin,G., Jiang,Q. and Zhang,C.
  TITLE     PLK4-phosphorylated NEDD1 facilitates cartwheel assembly and
            centriole biogenesis initiations
  JOURNAL   J Cell Biol 220 (1) (2021)
   PUBMED   33351100
  REMARK    GeneRIF: PLK4-phosphorylated NEDD1 facilitates cartwheel assembly
            and centriole biogenesis initiations.
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Courtheoux,T., Reboutier,D., Vazeille,T., Cremet,J.Y., Benaud,C.,
            Vernos,I. and Prigent,C.
  TITLE     Microtubule nucleation during central spindle assembly requires
            NEDD1 phosphorylation on serine 405 by Aurora A
  JOURNAL   J Cell Sci 132 (10) (2019)
   PUBMED   31028180
  REMARK    GeneRIF: Authors show here that the expression of a NEDD1 isoform
            mimicking phosphorylation by Aurora A is sufficient to restore
            microtubule nucleation in the midzone under conditions of Aurora A
            inhibition.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Fang,C.T., Kuo,H.H., Pan,T.S., Yu,F.C. and Yih,L.H.
  TITLE     HSP70 regulates the function of mitotic centrosomes
  JOURNAL   Cell Mol Life Sci 73 (20), 3949-3960 (2016)
   PUBMED   27137183
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Haren,L. and Merdes,A.
  TITLE     Direct binding of NuMA to tubulin is mediated by a novel sequence
            motif in the tail domain that bundles and stabilizes microtubules
  JOURNAL   J Cell Sci 115 (Pt 9), 1815-1824 (2002)
   PUBMED   11956313
REFERENCE   7  (residues 1 to 660)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   8  (residues 1 to 660)
  AUTHORS   Hsu,H.L. and Yeh,N.H.
  TITLE     Dynamic changes of NuMA during the cell cycle and possible
            appearance of a truncated form of NuMA during apoptosis
  JOURNAL   J Cell Sci 109 (Pt 2), 277-288 (1996)
   PUBMED   8838651
REFERENCE   9  (residues 1 to 660)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   10 (residues 1 to 660)
  AUTHORS   Takai,S., Yoshida,Y., Noda,M., Yamada,K. and Kumar,S.
  TITLE     Assignment of the developmentally regulated gene NEDD1 to human
            chromosome 12q22 by fluorescence in situ hybridization
  JOURNAL   Hum Genet 95 (1), 96-98 (1995)
   PUBMED   7814034
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL832466.1, AK315821.1, AK290058.1, AA236927.1 and AC013417.4.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and uses
            a downstream translation initiation codon, compared to variant 1,
            resulting in an isoform (b) that has a shorter N-terminus, compared
            to isoform a. Both variants 2 and 3 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL832466.1, DRR138524.1032720.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.1"
     Protein         1..660
                     /product="protein NEDD1 isoform b"
                     /note="protein NEDD1; NEDD-1; neural precursor cell
                     expressed developmentally down-regulated protein 1;
                     tubulin gamma complex associated protein 7; neural
                     precursor cell expressed, developmentally down-regulated
                     1"
                     /calculated_mol_wt=71835
     Region          1..31
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Region          24..299
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Site            order(31,51,55,61..62,74..75,94,98,104..105,117..118,135,
                     140,146..147,159,178,184,190..191,203,205,223,228,
                     234..235,247..248,264,269,275..276,289..290)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          32..71
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Region          37..74
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          75..114
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Region          81..117
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          117..156
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Region          123..160
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          160..200
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Region          165..202
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          204..244
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Region          210..246
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          246..285
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Region          251..288
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          289..332
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Region          369..411
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PLK1.
                     /evidence=ECO:0000269|PubMed:19509060; propagated from
                     UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:19509060,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:19509060; propagated from
                     UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Region          507..532
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Site            550
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:19509060; propagated from
                     UniProtKB/Swiss-Prot (Q8NHV4.1)"
     Site            637
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:19509060; propagated from
                     UniProtKB/Swiss-Prot (Q8NHV4.1)"
     CDS             1..660
                     /gene="NEDD1"
                     /gene_synonym="GCP-WD; TUBGCP7"
                     /coded_by="NM_001135176.2:53..2035"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS9063.1"
                     /db_xref="GeneID:121441"
                     /db_xref="HGNC:HGNC:7723"
                     /db_xref="MIM:600372"
ORIGIN      
        1 mqenlrfass gddikiwdas smtlvdkfnp htsphgissi cwssnnnflv tasssgdkiv
       61 vssckckpvp llelaegqkq tcvnlnstsm ylvsgglnnt vniwdlkskr vhrslkdhkd
      121 qvtcvtynwn dcyiasgsls geiilhsvtt nlsstpfghg snqsvrhlky slfkksllgs
      181 vsdngivtlw dvnsqspyhn fdsvhkapas gicfspvnel lfvtigldkr iilydtsskk
      241 lvktlvadtp ltavdfmpdg atlaigssrg kiyqydlrml kspvktisah ktsvqciafq
      301 ystvltkssl nkgcsnkptt vnkrsvnvna asggvqnsgi vreapatsia tvlpqpmtsa
      361 mgkgtvavqe kaglprsint dtlsketdsg knqdfssfdd tgksslgdmf spirddavvn
      421 kgsdesigkg dgfdflpqln svfpprknpv tsstsvlhss plnvfmgspg keenenrdlt
      481 aeskkiymgk qeskdsfkql aklvtsgaes gnlntspssn qtrnsekfek peneieaqli
      541 ceppingsst pnpkiassvt agvasslsek iadsignnrq napltsiqir fiqnmiqetl
      601 ddfreachrd ivnlqvemik qfhmqlnemh sllerysvne glvaeierlr eenkrlrahf
//
LOCUS       NP_001106878             411 aa            linear   PRI 21-NOV-2025
DEFINITION  LIM domain-binding protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001106878
VERSION     NP_001106878.1
DBSOURCE    REFSEQ: accession NM_001113407.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Wang,C., Hu,M., Yu,K., Liu,W., Hu,A., Kuang,Y., Huang,L.,
            Gajendran,B., Zacksenhaus,E., Xiao,X. and Ben-David,Y.
  TITLE     An intricate regulatory circuit between FLI1 and
            GATA1/GATA2/LDB1/ERG dictates erythroid vs. megakaryocytic
            differentiation
  JOURNAL   Mol Med Rep 29 (6) (2024)
   PUBMED   38695236
  REMARK    GeneRIF: An intricate regulatory circuit between FLI1 and
            GATA1/GATA2/LDB1/ERG dictates erythroid vs. megakaryocytic
            differentiation.
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Lu,L., Wang,J., Fang,F., Guo,A., Jiang,S., Tao,Y., Zhang,Y., Li,Y.,
            Zhang,K., Zhang,Z., Zhuo,R., Chu,X., Li,X., Tian,Y., Ma,L.,
            Sang,X., Chen,Y., Yu,J., Yang,Y., Cao,H., Gao,J., Lu,J., Hu,S.,
            Pan,J. and He,H.
  TITLE     LMO2 promotes the development of AML through interaction with
            transcription co-regulator LDB1
  JOURNAL   Cell Death Dis 14 (8), 518 (2023)
   PUBMED   37573405
  REMARK    GeneRIF: LMO2 promotes the development of AML through interaction
            with transcription co-regulator LDB1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Jurata,L.W., Pfaff,S.L. and Gill,G.N.
  TITLE     The nuclear LIM domain interactor NLI mediates homo- and
            heterodimerization of LIM domain transcription factors
  JOURNAL   J Biol Chem 273 (6), 3152-3157 (1998)
   PUBMED   9452425
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Visvader,J.E., Mao,X., Fujiwara,Y., Hahm,K. and Orkin,S.H.
  TITLE     The LIM-domain binding protein Ldb1 and its partner LMO2 act as
            negative regulators of erythroid differentiation
  JOURNAL   Proc Natl Acad Sci U S A 94 (25), 13707-13712 (1997)
   PUBMED   9391090
REFERENCE   8  (residues 1 to 411)
  AUTHORS   Jurata,L.W. and Gill,G.N.
  TITLE     Functional analysis of the nuclear LIM domain interactor NLI
  JOURNAL   Mol Cell Biol 17 (10), 5688-5698 (1997)
   PUBMED   9315627
REFERENCE   9  (residues 1 to 411)
  AUTHORS   Wadman,I.A., Osada,H., Grutz,G.G., Agulnick,A.D., Westphal,H.,
            Forster,A. and Rabbitts,T.H.
  TITLE     The LIM-only protein Lmo2 is a bridging molecule assembling an
            erythroid, DNA-binding complex which includes the TAL1, E47, GATA-1
            and Ldb1/NLI proteins
  JOURNAL   EMBO J 16 (11), 3145-3157 (1997)
   PUBMED   9214632
REFERENCE   10 (residues 1 to 411)
  AUTHORS   Osada,H., Grutz,G.G., Axelson,H., Forster,A. and Rabbitts,T.H.
  TITLE     LIM-only protein Lmo2 forms a protein complex with erythroid
            transcription factor GATA-1
  JOURNAL   Leukemia 11 Suppl 3, 307-312 (1997)
   PUBMED   9209374
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL500527.19.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.176290.1,
                                           SRR12921934.1809785.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467148 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000673968.1/ ENSP00000501277.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..411
                     /product="LIM domain-binding protein 1 isoform 1"
                     /note="carboxy terminal LIM domain protein 2; LIM
                     domain-binding factor-1; LIM domain-binding protein 1;
                     nuclear LIM interactor; LIM domain-binding factor CLIM2;
                     carboxyl-terminal LIM domain-binding protein 2"
                     /calculated_mol_wt=46402
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q86U70.2)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P70662; propagated from
                     UniProtKB/Swiss-Prot (Q86U70.2)"
     Region          70..271
                     /region_name="LIM_bind"
                     /note="LIM-domain binding protein; pfam01803"
                     /db_xref="CDD:426444"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86U70.2)"
     Region          283..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86U70.2)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70662; propagated from
                     UniProtKB/Swiss-Prot (Q86U70.2)"
     Region          336..364
                     /region_name="LID"
                     /note="LIM interaction domain (LID); pfam17916"
                     /db_xref="CDD:465564"
     Region          367..411
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86U70.2)"
     CDS             1..411
                     /gene="LDB1"
                     /gene_synonym="CLIM-2; CLIM2; LDB-1; NLI"
                     /coded_by="NM_001113407.3:259..1494"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44472.1"
                     /db_xref="GeneID:8861"
                     /db_xref="HGNC:HGNC:6532"
                     /db_xref="MIM:603451"
ORIGIN      
        1 msvgcacpgc ssksfklysp keppngnafp pfhpgtmldr dvgptpmypp tylepgigrh
       61 tpygnqtdyr ifelnkrlqn wteecdnlww daftteffed damltitfcl edgpkrytig
      121 rtlipryfrs ifeggately yvlkhpkeaf hsnfvsldcd qgsmvtqhgk pmftqvcveg
      181 rlylefmfdd mmriktwhfs irqhrelipr silamhaqdp qmldqlskni trcglsnstl
      241 nylrlcvile pmqelmsrhk tyslsprdcl ktclfqkwqr mvappaeptr qqpskrrkrk
      301 msggstmssg ggntnnsnsk kkspastfal ssqvpdvmvv geptlmggef gdederlitr
      361 lentqfdaan giddedsfnn spalganspw nskppssqes ksenptsqas q
//
LOCUS       NP_001248340            1003 aa            linear   PRI 21-NOV-2025
DEFINITION  splicing factor, suppressor of white-apricot homolog isoform 1
            [Homo sapiens].
ACCESSION   NP_001248340
VERSION     NP_001248340.1
DBSOURCE    REFSEQ: accession NM_001261411.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1003)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1003)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1003)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 1003)
  AUTHORS   Crisci,A., Raleff,F., Bagdiul,I., Raabe,M., Urlaub,H., Rain,J.C.
            and Kramer,A.
  TITLE     Mammalian splicing factor SF1 interacts with SURP domains of U2
            snRNP-associated proteins
  JOURNAL   Nucleic Acids Res 43 (21), 10456-10473 (2015)
   PUBMED   26420826
REFERENCE   5  (residues 1 to 1003)
  AUTHORS   Moayedi,Y., Basch,M.L., Pacheco,N.L., Gao,S.S., Wang,R.,
            Harrison,W., Xiao,N., Oghalai,J.S., Overbeek,P.A., Mardon,G. and
            Groves,A.K.
  TITLE     The candidate splicing factor Sfswap regulates growth and
            patterning of inner ear sensory organs
  JOURNAL   PLoS Genet 10 (1), e1004055 (2014)
   PUBMED   24391519
REFERENCE   6  (residues 1 to 1003)
  AUTHORS   Brasch-Andersen,C., Tan,Q., Borglum,A.D., Haagerup,A., Larsen,T.R.,
            Vestbo,J. and Kruse,T.A.
  TITLE     Significant linkage to chromosome 12q24.32-q24.33 and
            identification of SFRS8 as a possible asthma susceptibility gene
  JOURNAL   Thorax 61 (10), 874-879 (2006)
   PUBMED   16738036
REFERENCE   7  (residues 1 to 1003)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1003)
  AUTHORS   Sarkissian,M., Winne,A. and Lafyatis,R.
  TITLE     The mammalian homolog of suppressor-of-white-apricot regulates
            alternative mRNA splicing of CD45 exon 4 and fibronectin IIICS
  JOURNAL   J Biol Chem 271 (49), 31106-31114 (1996)
   PUBMED   8940107
REFERENCE   9  (residues 1 to 1003)
  AUTHORS   Denhez,F. and Lafyatis,R.
  TITLE     Conservation of regulated alternative splicing and identification
            of functional domains in vertebrate homologs to the Drosophila
            splicing regulator, suppressor-of-white-apricot
  JOURNAL   J Biol Chem 269 (23), 16170-16179 (1994)
   PUBMED   8206918
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC117500.13 and AC131009.7.
            
            Summary: This gene encodes a human homolog of Drosophila splicing
            regulatory protein. This gene autoregulates its expression by
            control of splicing of its first two introns. In addition, it also
            regulates the splicing of fibronectin and CD45 genes. Two
            transcript variants encoding different isoforms have been
            identified. [provided by RefSeq, May 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC144364.1, SRR14038193.221553.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1003
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.33"
     Protein         1..1003
                     /product="splicing factor, suppressor of white-apricot
                     homolog isoform 1"
                     /note="splicing factor, arginine/serine-rich 8
                     (suppressor-of-white-apricot, Drosophila homolog);
                     splicing factor SWAP homolog; splicing factor,
                     arginine/serine-rich 8 (suppressor-of-white-apricot
                     homolog, Drosophila); suppressor of white apricot protein
                     homolog; splicing factor, suppressor of white-apricot
                     family; splicing factor, suppressor of white-apricot
                     homolog"
                     /calculated_mol_wt=109881
     Region          35..155
                     /region_name="DRY_EERY"
                     /note="Alternative splicing regulator; pfam09750"
                     /db_xref="CDD:462881"
     Region          209..262
                     /region_name="SWAP"
                     /note="Suppressor-of-White-APricot splicing regulator;
                     smart00648"
                     /db_xref="CDD:197818"
     Region          457..508
                     /region_name="SWAP"
                     /note="Suppressor-of-White-APricot splicing regulator;
                     smart00648"
                     /db_xref="CDD:197818"
     Region          <637..718
                     /region_name="rpsP"
                     /note="30S ribosomal protein S16; Provisional; PRK14521"
                     /db_xref="CDD:237744"
     CDS             1..1003
                     /gene="SFSWAP"
                     /gene_synonym="SFRS8; SWAP"
                     /coded_by="NM_001261411.2:141..3152"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS58290.1"
                     /db_xref="GeneID:6433"
                     /db_xref="HGNC:HGNC:10790"
                     /db_xref="MIM:601945"
ORIGIN      
        1 mygasggrak perksgakee agpggagggg srvellvfgy acklfrdder alaqeqgqhl
       61 ipwmgdhkil idrydgrghl hdlseydaey stwnrdyqls eeeariealc deerylalht
      121 dlleeearqe eeykrlseal aedgsynavg ftygsdyydp septeeeeps kqrekneaen
      181 leeneepfva plglsvpsdv elpptakmha iiertasfvc rqgaqfeiml kakqarnsqf
      241 dflrfdhyln pyykfiqkam kegrytvlae nksdekkksg vssdnedddd eedgnylhps
      301 lfaskkcnrl eelmkplkvv dpdhplaalv rkaqadsstp tphnadgapv qpsqveytad
      361 stvaamyysy ymlpdgtycl appppgidvt tyystlpagv tvsnspgvtt tappppgttp
      421 lpppttaets sgatsttttt salapvaaii ppppdvqpvi dklaeyvarn glkfetsvra
      481 kndqrfeflq pwhqynayye fkkqfflqke ggdsmqavsa peeaptdsap ekpsdagedg
      541 apedaaevga ragsggkkea sssktvpdgk lvkasfapis faikakendl lpleknrvkl
      601 dddsdddees kegqessssa antnpavapp cvvveekkpq ltqeeleakq akqkledrla
      661 aaareklaqa skeskekqlq aerkrkaalf lqtlknplpe aeagkieesp fsveessttp
      721 cplltggrpl ptlevkppdr psskskdppr eeekekkkkk hkkrsrtrsr spkyhsssks
      781 rsrshskakh slpsayrtvr rsrvtaspgt lraepcqssa svtaaaepgs yqaastttrf
      841 dsassfegkp gktsrsrsrs prrrahsper rreersvpta yrvsrspgas rkrtrsrsph
      901 ekkkkrrsrs rtkskarsqs vspskqaapr paapaahsah sasvspvesr gssqersrgv
      961 sqekeaqiss aivssvqski tqdlmakvra mlaasknlqt sas
//
LOCUS       NP_001336176             712 aa            linear   PRI 21-NOV-2025
DEFINITION  trafficking kinesin-binding protein 1 isoform 8 [Homo sapiens].
ACCESSION   NP_001336176 XP_005265017
VERSION     NP_001336176.1
DBSOURCE    REFSEQ: accession NM_001349247.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Baltrusaitis,E.E., Ravitch,E.E., Fenton,A.R., Perez,T.A.,
            Holzbaur,E.L.F. and Dominguez,R.
  TITLE     Interaction between the mitochondrial adaptor MIRO and the motor
            adaptor TRAK
  JOURNAL   J Biol Chem 299 (12), 105441 (2023)
   PUBMED   37949220
  REMARK    GeneRIF: Interaction between the mitochondrial adaptor MIRO and the
            motor adaptor TRAK.
REFERENCE   3  (residues 1 to 712)
  AUTHORS   Benhamida,J.K., Harmsen,H.J., Ma,D., William,C.M., Li,B.K.,
            Villafania,L., Sukhadia,P., Mullaney,K.A., Dewan,M.C., Vakiani,E.,
            Karajannis,M.A., Snuderl,M., Zagzag,D., Ladanyi,M., Rosenblum,M.K.
            and Bale,T.A.
  TITLE     Recurrent TRAK1::RAF1 Fusions in pediatric low-grade gliomas
  JOURNAL   Brain Pathol 33 (5), e13185 (2023)
   PUBMED   37399073
  REMARK    GeneRIF: Recurrent TRAK1::RAF1 Fusions in pediatric low-grade
            gliomas.
REFERENCE   4  (residues 1 to 712)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 712)
  AUTHORS   Wu,H., Liu,Y., Li,H., Du,C., Li,K., Dong,S., Meng,Q. and Zhang,H.
  TITLE     TRAK1-Mediated Abnormality of Mitochondrial Fission Increases
            Seizure Susceptibility in Temporal Lobe Epilepsy
  JOURNAL   Mol Neurobiol 58 (3), 1237-1247 (2021)
   PUBMED   33119838
  REMARK    GeneRIF: TRAK1-Mediated Abnormality of Mitochondrial Fission
            Increases Seizure Susceptibility in Temporal Lobe Epilepsy.
REFERENCE   6  (residues 1 to 712)
  AUTHORS   Ozyildirim,A.M., Wistow,G.J., Gao,J., Wang,J., Dickinson,D.P.,
            Frierson,H.F. Jr. and Laurie,G.W.
  TITLE     The lacrimal gland transcriptome is an unusually rich source of
            rare and poorly characterized gene transcripts
  JOURNAL   Invest Ophthalmol Vis Sci 46 (5), 1572-1580 (2005)
   PUBMED   15851553
REFERENCE   7  (residues 1 to 712)
  AUTHORS   Brickley,K., Smith,M.J., Beck,M. and Stephenson,F.A.
  TITLE     GRIF-1 and OIP106, members of a novel gene family of coiled-coil
            domain proteins: association in vivo and in vitro with kinesin
  JOURNAL   J Biol Chem 280 (15), 14723-14732 (2005)
   PUBMED   15644324
  REMARK    GeneRIF: GRIF-1 and OIP106 have roles in protein and/or organelle
            transport in excitable cells in a manner analogous to glutamate
            receptor-interacting-protein 1
REFERENCE   8  (residues 1 to 712)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   9  (residues 1 to 712)
  AUTHORS   Iyer,S.P. and Hart,G.W.
  TITLE     Roles of the tetratricopeptide repeat domain in O-GlcNAc
            transferase targeting and protein substrate specificity
  JOURNAL   J Biol Chem 278 (27), 24608-24616 (2003)
   PUBMED   12724313
REFERENCE   10 (residues 1 to 712)
  AUTHORS   Iyer,S.P., Akimoto,Y. and Hart,G.W.
  TITLE     Identification and cloning of a novel family of coiled-coil domain
            proteins that interact with O-GlcNAc transferase
  JOURNAL   J Biol Chem 278 (7), 5399-5409 (2003)
   PUBMED   12435728
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093414.3 and AC018358.20.
            
            On Mar 9, 2017 this sequence version replaced XP_005265017.1.
            
            Transcript Variant: This variant (8) encodes isoform 8.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.250858.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2151741
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.1"
     Protein         1..712
                     /product="trafficking kinesin-binding protein 1 isoform 8"
                     /note="OGT(O-Glc-NAc transferase)-interacting protein 106
                     KDa; 106 kDa O-GlcNAc transferase-interacting protein;
                     milton homolog 1; O-linked N-acetylglucosamine transferase
                     interacting protein 106; protein Milton; trafficking
                     protein, kinesin binding 1"
                     /calculated_mol_wt=80416
     Region          48..353
                     /region_name="HAP1_N"
                     /note="HAP1 N-terminal conserved region; pfam04849"
                     /db_xref="CDD:461455"
     Region          359..509
                     /region_name="Interaction with HGS.
                     /evidence=ECO:0000269|PubMed:18675823"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Region          414..583
                     /region_name="Milton"
                     /note="Kinesin associated protein; pfam12448"
                     /db_xref="CDD:463588"
     Site            447
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:24995978; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Region          472..495
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PD31; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Region          658..672
                     /region_name="Interaction with OGT.
                     /evidence=ECO:0000269|PubMed:24995978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Site            680
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:24995978; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     CDS             1..712
                     /gene="TRAK1"
                     /gene_synonym="DEE68; EIEE68; MILT1; OIP106"
                     /coded_by="NM_001349247.2:114..2252"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:22906"
                     /db_xref="HGNC:HGNC:29947"
                     /db_xref="MIM:608112"
ORIGIN      
        1 malvfqfgqp vraqplpglc hgklirtnac dvcnstdlpe veiislleeq lphyklradt
       61 iygydhddwl htplispdan idltteqiee tlkyfllcae rvgqmtktyn didavtrlle
      121 ekerdlelaa rigqsllkkn ktlternell eeqvehiree vsqlrhelsm kdellqfyts
      181 aaeesepesv cstplkrnes sssvqnyfhl dslqkklkdl eeenvvlrse asqlktetit
      241 yeekeqqlvn dcvkelrdan vqiasiseel akktedaarq qeeithllsq ivdlqkkaka
      301 caveneelvq hlgaakdaqr qltaelrele dkyaecmeml heaqeelknl rnktmpntts
      361 rryhslglfp mdslaaeieg tmrkelqlee aespdithqk rvfetvrnin qvvkqrsltp
      421 spmnipgsnq ssamnsllss cvstprssfy gsdignvvld nktnsiilet eaadlgnder
      481 skkpgtpgtp gshdletalr rlslrrenyl serrffeeeq erklqelaek gelrsgsltp
      541 tesimslgth srfseftgfs gmsfssrsyl peklqivkpl egsatlhhwq qlaqphlggi
      601 ldprpgvvtk gfrtldvdld evyclndfee ddtgdhislp rlatstpvqh petsahhpgk
      661 cmsqtnstft fttcrilhps deltrvtprs ceeddeaaic pvelrgdigq rv
//
LOCUS       NP_003669                683 aa            linear   PRI 21-NOV-2025
DEFINITION  THO complex subunit 5 [Homo sapiens].
ACCESSION   NP_003669 XP_376002
VERSION     NP_003669.4
DBSOURCE    REFSEQ: accession NM_003678.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Pacheco-Fiallos,B., Vorlander,M.K., Riabov-Bassat,D., Fin,L.,
            O'Reilly,F.J., Ayala,F.I., Schellhaas,U., Rappsilber,J. and
            Plaschka,C.
  TITLE     mRNA recognition and packaging by the human transcription-export
            complex
  JOURNAL   Nature 616 (7958), 828-835 (2023)
   PUBMED   37020021
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Mun,S.H., Oh,B., Lee,M.J., Bae,S., Yang,Y. and Park-Min,K.H.
  TITLE     THOC5 regulates human osteoclastogenesis
  JOURNAL   Eur J Cell Biol 101 (3), 151248 (2022)
   PUBMED   35688054
  REMARK    GeneRIF: THOC5 regulates human osteoclastogenesis.
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 683)
  AUTHORS   Alqassim,E.Y., Sharma,S., Khan,A.N.M.N.H., Emmons,T.R., Cortes
            Gomez,E., Alahmari,A., Singel,K.L., Mark,J., Davidson,B.A., Robert
            McGray,A.J., Liu,Q., Lichty,B.D., Moysich,K.B., Wang,J., Odunsi,K.,
            Segal,B.H. and Baysal,B.E.
  TITLE     RNA editing enzyme APOBEC3A promotes pro-inflammatory M1 macrophage
            polarization
  JOURNAL   Commun Biol 4 (1), 102 (2021)
   PUBMED   33483601
  REMARK    GeneRIF: RNA editing enzyme APOBEC3A promotes pro-inflammatory M1
            macrophage polarization.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 683)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 683)
  AUTHORS   Mancini,A., Koch,A., Whetton,A.D. and Tamura,T.
  TITLE     The M-CSF receptor substrate and interacting protein FMIP is
            governed in its subcellular localization by protein kinase
            C-mediated phosphorylation, and thereby potentiates M-CSF-mediated
            differentiation
  JOURNAL   Oncogene 23 (39), 6581-6589 (2004)
   PUBMED   15221008
REFERENCE   7  (residues 1 to 683)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   8  (residues 1 to 683)
  AUTHORS   Strasser,K., Masuda,S., Mason,P., Pfannstiel,J., Oppizzi,M.,
            Rodriguez-Navarro,S., Rondon,A.G., Aguilera,A., Struhl,K., Reed,R.
            and Hurt,E.
  TITLE     TREX is a conserved complex coupling transcription with messenger
            RNA export
  JOURNAL   Nature 417 (6886), 304-308 (2002)
   PUBMED   11979277
REFERENCE   9  (residues 1 to 683)
  AUTHORS   Tamura,T., Mancini,A., Joos,H., Koch,A., Hakim,C., Dumanski,J.,
            Weidner,K.M. and Niemann,H.
  TITLE     FMIP, a novel Fms-interacting protein, affects
            granulocyte/macrophage differentiation
  JOURNAL   Oncogene 18 (47), 6488-6495 (1999)
   PUBMED   10597251
REFERENCE   10 (residues 1 to 683)
  AUTHORS   Xie,Y.G., Han,F.Y., Peyrard,M., Ruttledge,M.H., Fransson,I.,
            DeJong,P., Collins,J., Dunham,I., Nordenskjold,M. and Dumanski,J.P.
  TITLE     Cloning of a novel, anonymous gene from a megabase-range YAC and
            cosmid contig in the neurofibromatosis type 2/meningioma region on
            human chromosome 22q12
  JOURNAL   Hum Mol Genet 2 (9), 1361-1368 (1993)
   PUBMED   8242058
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005529.7, BX404329.2, CR456542.1, BX400943.2, AB023200.1 and
            BQ184247.1.
            
            On Aug 4, 2004 this sequence version replaced NP_003669.3.
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. All four variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB023200.1, BC003615.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000490103.6/ ENSP00000420306.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..683
                     /product="THO complex subunit 5"
                     /note="functional spliceosome-associated protein 79;
                     NF2/meningioma region protein pK1.3; placental protein
                     39.2; THO complex 5; THO complex subunit 5 homolog;
                     Fms-interacting protein; PP39.2; hTREX90"
                     /calculated_mol_wt=78377
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     Region          2..199
                     /region_name="Interaction with THOC7.
                     /evidence=ECO:0000269|PubMed:19059247"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     Region          2..144
                     /region_name="Interaction with CSF1R.
                     /evidence=ECO:0000250|UniProtKB:Q8BKT7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q13769.2)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BKT7; propagated from
                     UniProtKB/Swiss-Prot (Q13769.2)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BKT7; propagated from
                     UniProtKB/Swiss-Prot (Q13769.2)"
     Region          7..10
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     Region          103..452
                     /region_name="FmiP_Thoc5"
                     /note="Fms-interacting protein/Thoc5; pfam09766"
                     /db_xref="CDD:462889"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:18373705,
                     ECO:0000269|PubMed:23032722; propagated from
                     UniProtKB/Swiss-Prot (Q13769.2)"
     Region          247..683
                     /region_name="Tandem RWD domains.
                     /evidence=ECO:0000269|PubMed:33191911,
                     ECO:0007744|PDB:7APK, ECO:0007744|PDB:7ZNK,
                     ECO:0007744|PDB:7ZNL"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     Region          301..336
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13769.2)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     CDS             1..683
                     /gene="THOC5"
                     /gene_synonym="C22orf19; Fmip; fSAP79; PK1.3"
                     /coded_by="NM_003678.5:99..2150"
                     /db_xref="CCDS:CCDS13859.1"
                     /db_xref="GeneID:8563"
                     /db_xref="HGNC:HGNC:19074"
                     /db_xref="MIM:612733"
ORIGIN      
        1 mssesskkrk pkvirsdgap aegkrnrsdt eqegkyysee aevdlrdpgr dyelykytcq
       61 elqrlmaeiq dlksrggkdv aieieerriq scvhfmtlkk lnrlahirlk kgrdqtheak
      121 qkvdayhlql qnllyevmhl qkeitkclef kskheeidlv sleefykeap pdiskaevtm
      181 gdphqqtlar ldweleqrkr laekyrecls nkekilkeie vkkeylsslq prlnsimqas
      241 lpvqeylfmp fdqahkqyet arhlppplyv lfvqataygq acdktlsvai egsvdeakal
      301 fkppedsqdd esdsdaeeeq ttkrrrptlg vqlddkrkem lkrhplsvml dlkckddsvl
      361 hltfyylmnl nimtvkakvt tamelitpis agdllspdsv lsclypgdhg kktpnpanqy
      421 qfdkvgiltl sdyvlelghp ylwvqklggl hfpkeqpqqt viadhslsas hmettmkllk
      481 trvqsrlalh kqfaslehgi vpvtsdcqyl fpakvvsrlv kwvtvahedy melhftkdiv
      541 daglagdtnl yymaliergt aklqaavvln pgyssippvf qlclnwkgek tnsnddnira
      601 megevnvcyk elcgpwpshq lltnqlqrlc vlldvylete shddsvegpk efpqekmclr
      661 lfrgpsrmkp fkynhpqgff shr
//
LOCUS       NP_001374911            1108 aa            linear   PRI 21-NOV-2025
DEFINITION  large proline-rich protein BAG6 isoform 14 [Homo sapiens].
ACCESSION   NP_001374911
VERSION     NP_001374911.1
DBSOURCE    REFSEQ: accession NM_001387982.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1108)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 1108)
  AUTHORS   Alashkar Alhamwe,B., Ponath,V., Alhamdan,F., Dorsam,B.,
            Landwehr,C., Linder,M., Pauck,K., Miethe,S., Garn,H.,
            Finkernagel,F., Brichkina,A., Lauth,M., Tiwari,D.K., Buchholz,M.,
            Bachurski,D., Elmshauser,S., Nist,A., Stiewe,T., Pogge von
            Strandmann,L., Szymanski,W., Beutgen,V., Graumann,J.,
            Teply-Szymanski,J., Keber,C., Denkert,C., Jacob,R., Preusser,C. and
            Pogge von Strandmann,E.
  TITLE     BAG6 restricts pancreatic cancer progression by suppressing the
            release of IL33-presenting extracellular vesicles and the
            activation of mast cells
  JOURNAL   Cell Mol Immunol 21 (8), 918-931 (2024)
   PUBMED   38942797
  REMARK    GeneRIF: BAG6 restricts pancreatic cancer progression by
            suppressing the release of IL33-presenting extracellular vesicles
            and the activation of mast cells.
REFERENCE   3  (residues 1 to 1108)
  AUTHORS   Liu,L., Wu,J., Yan,Y., Cheng,S., Yu,S. and Wang,Y.
  TITLE     DERL2 (derlin 2) stabilizes BAG6 (BAG cochaperone 6) in
            chemotherapy resistance of cholangiocarcinoma
  JOURNAL   J Physiol Biochem 80 (1), 81-97 (2024)
   PUBMED   37815698
  REMARK    GeneRIF: DERL2 (derlin 2) stabilizes BAG6 (BAG cochaperone 6) in
            chemotherapy resistance of cholangiocarcinoma.
REFERENCE   4  (residues 1 to 1108)
  AUTHORS   Roboti,P., Lawless,C. and High,S.
  TITLE     Mitochondrial antiviral-signalling protein is a client of the BAG6
            protein quality control complex
  JOURNAL   J Cell Sci 135 (9) (2022)
   PUBMED   35543156
  REMARK    GeneRIF: Mitochondrial antiviral-signalling protein is a client of
            the BAG6 protein quality control complex.
REFERENCE   5  (residues 1 to 1108)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1108)
  AUTHORS   Ozaki,T., Hanaoka,E., Naka,M., Nakagawara,A. and Sakiyama,S.
  TITLE     Cloning and characterization of rat BAT3 cDNA
  JOURNAL   DNA Cell Biol 18 (6), 503-512 (1999)
   PUBMED   10390159
REFERENCE   7  (residues 1 to 1108)
  AUTHORS   Cross,S.J., Tonks,S., Trowsdale,J. and Campbell,R.D.
  TITLE     Novel detection of restriction fragment length polymorphisms in the
            human major histocompatibility complex
  JOURNAL   Immunogenetics 34 (6), 376-384 (1991)
   PUBMED   1684176
REFERENCE   8  (residues 1 to 1108)
  AUTHORS   Banerji,J., Sands,J., Strominger,J.L. and Spies,T.
  TITLE     A gene pair from the human major histocompatibility complex encodes
            large proline-rich proteins with multiple repeated motifs and a
            single ubiquitin-like domain
  JOURNAL   Proc Natl Acad Sci U S A 87 (6), 2374-2378 (1990)
   PUBMED   2156268
REFERENCE   9  (residues 1 to 1108)
  AUTHORS   Spies,T., Bresnahan,M. and Strominger,J.L.
  TITLE     Human major histocompatibility complex contains a minimum of 19
            genes between the complement cluster and HLA-B
  JOURNAL   Proc Natl Acad Sci U S A 86 (22), 8955-8958 (1989)
   PUBMED   2813433
REFERENCE   10 (residues 1 to 1108)
  AUTHORS   Spies,T., Blanck,G., Bresnahan,M., Sands,J. and Strominger,J.L.
  TITLE     A new cluster of genes within the human major histocompatibility
            complex
  JOURNAL   Science 243 (4888), 214-217 (1989)
   PUBMED   2911734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL662801.7.
            
            Summary: This gene was first characterized as part of a cluster of
            genes located within the human major histocompatibility complex
            class III region. This gene encodes a nuclear protein that is
            cleaved by caspase 3 and is implicated in the control of apoptosis.
            In addition, the protein forms a complex with E1A binding protein
            p300 and is required for the acetylation of p53 in response to DNA
            damage. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.4004870.1,
                                           SRR14372079.3128223.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1108
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..1108
                     /product="large proline-rich protein BAG6 isoform 14"
                     /note="scythe; large proline-rich protein BAT3; large
                     proline-rich protein BAG6; protein G3; HLA-B-associated
                     transcript 3; protein Scythe; BAG family molecular
                     chaperone regulator 6; BCL2 associated athanogene 6"
                     /calculated_mol_wt=116669
     Region          17..87
                     /region_name="Ubl_BAG6"
                     /note="ubiquitin-like (Ubl) domain found in
                     BCL2-associated athanogene 6 (BAG6) and similar proteins;
                     cd01809"
                     /db_xref="CDD:340507"
     Site            order(22..25,58,60,62..65,83..87)
                     /site_type="other"
                     /note="ZF interaction site [polypeptide binding]"
                     /db_xref="CDD:340507"
     Region          252..368
                     /region_name="BAG6"
                     /note="BCL2-associated athanogene 6; pfam12057"
                     /db_xref="CDD:463449"
     Region          <881..1072
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     CDS             1..1108
                     /gene="BAG6"
                     /gene_synonym="BAG-6; BAT3; D6S52E; G3"
                     /coded_by="NM_001387982.1:276..3602"
                     /note="isoform 14 is encoded by transcript variant 22"
                     /db_xref="GeneID:7917"
                     /db_xref="HGNC:HGNC:13919"
                     /db_xref="MIM:142590"
ORIGIN      
        1 mepndststa veepdslevl vktldsqtrt fivgaqmnvk efkehiaasv sipsekqrli
       61 yqgrvlqddk klqeynvggk vihlverapp qthlpsgass gtgsasathg ggsppgtrgp
      121 gasvhdrnan syvmvgtfnl pseprvrlvm aqhmirdiqt llsrmecrgg pqpqhsqppp
      181 qppavtpepv alssqtsepv eseapprepm eaeeveerap aqnpeltpgp apagptpape
      241 tnapnhpspa eyvevlqelq rlesrlqpfl qryyevlgaa attdynnnhe greedqrlin
      301 lvgeslrllg ntfvalsdlr cnlactpprh lhvvrpmshy ttpmvlqqaa ipiqinvgtt
      361 vtmtgngtrp pptpnaeapp pgpgqassva psstnvessa egapppgpap ppatshprvi
      421 rishqsvepv vmmhmniqds gtqpggvpsa ptgplgppgh gqtlgqqvpg fptaptrvvi
      481 arptppqarp shpggppvsg tlqgaglgtn aslaqmvsgl vgqllmqpvl vaqgtpgmap
      541 ppapatasas agttntatta gpapggpaqp pptpqpsmad lqfsqllgnl lgpagpgagg
      601 sgvasptitv ampgvpaflq gmtdflqatq tapppppppp ppppapeqqt mpppgspsgg
      661 agspgglgle slspefftsv vqgvlssllg slgaragsse siaafiqrls gssnifepga
      721 dgalgffgal lsllcqnfsm vdvvmllhgh fqplqrlqpq lrsffhqhyl ggqeptpsni
      781 rmathtlitg leeyvresfs lvqvqpgvdi irtnleflqe qfnsiaahvl hctdsgfgar
      841 llelcnqglf eclalnlhcl ggqqmelaav ingrirrmsr gvnpslvswl ttmmglrlqv
      901 vlehmpvgpd ailryvrrvg dppqplpeep mevqgaeras pepqrenasp apgttaeeam
      961 srgpppapeg gsrdeqdgas aetepwaaav ppewvpiiqq diqsqrkvkp qpplsdayls
     1021 gmpakrrktm qgegpqllls eavsraakaa garpltspes lsrdleapev qesyrqqlrs
     1081 diqkrlqedp nyspqrfpna qrafaddp
//
LOCUS       NP_001304711             257 aa            linear   PRI 21-NOV-2025
DEFINITION  large ribosomal subunit protein uL2 [Homo sapiens].
ACCESSION   NP_001304711
VERSION     NP_001304711.1
DBSOURCE    REFSEQ: accession NM_001317782.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Sun,T., Zhu,W., Ru,Q. and Zheng,Y.
  TITLE     Silencing RPL8 inhibits the progression of hepatocellular carcinoma
            by down-regulating the mTORC1 signalling pathway
  JOURNAL   Hum Cell 36 (2), 725-737 (2023)
   PUBMED   36577883
  REMARK    GeneRIF: Silencing RPL8 inhibits the progression of hepatocellular
            carcinoma by down-regulating the mTORC1 signalling pathway.
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Fan,S., Zhang,S., Kong,D., Wang,H., Shi,Y., Wang,Z. and Zheng,H.
  TITLE     Integrative Multi-Omics Analysis of Identified Ferroptosis-Marker
            RPL8 as a Candidate Oncogene Correlates with Poor Prognosis and
            Immune Infiltration in Liver Cancer
  JOURNAL   Comb Chem High Throughput Screen 26 (7), 1298-1310 (2023)
   PUBMED   36017842
  REMARK    GeneRIF: Integrative Multi-Omics Analysis of Identified
            Ferroptosis-Marker RPL8 as a Candidate Oncogene Correlates with
            Poor Prognosis and Immune Infiltration in Liver Cancer.
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   7  (residues 1 to 257)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   8  (residues 1 to 257)
  AUTHORS   Uhlein,M., Weglohner,W., Urlaub,H. and Wittmann-Liebold,B.
  TITLE     Functional implications of ribosomal protein L2 in protein
            biosynthesis as shown by in vivo replacement studies
  JOURNAL   Biochem J 331 (Pt 2) (Pt 2), 423-430 (1998)
   PUBMED   9531480
REFERENCE   9  (residues 1 to 257)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 257)
  AUTHORS   Hanes,J., Klaudiny,J., von der Kammer,H. and Scheit,K.H.
  TITLE     Characterization by cDNA cloning of the mRNA of human ribosomal
            protein L8
  JOURNAL   Biochem Biophys Res Commun 197 (3), 1223-1228 (1993)
   PUBMED   7506540
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF235103.5, CB128790.1,
            BG480561.1 and BC030151.2.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L2P family of ribosomal proteins. It is located in the
            cytoplasm. In rat, the protein associates with the 5.8S rRNA, very
            likely participates in the binding of aminoacyl-tRNA, and is a
            constituent of the elongation factor 2-binding site at the
            ribosomal subunit interface. Alternatively spliced transcript
            variants encoding the same protein exist. As is typical for genes
            encoding ribosomal proteins, there are multiple processed
            pseudogenes of this gene dispersed through the genome. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) retains an intron in the 5'
            UTR compared to variant 1. Variants 1-4 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC030151.2, SRR1163655.173826.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000528957.6/ ENSP00000433464.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..257
                     /product="large ribosomal subunit protein uL2"
                     /note="60S ribosomal protein L8"
                     /calculated_mol_wt=27894
     Region          1..254
                     /region_name="PTZ00180"
                     /note="60S ribosomal protein L8; Provisional"
                     /db_xref="CDD:173464"
     Region          207..232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62917.2)"
     Site            216
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyhistidine.
                     /evidence=ECO:0000269|PubMed:23103944; propagated from
                     UniProtKB/Swiss-Prot (P62917.2)"
     CDS             1..257
                     /gene="RPL8"
                     /gene_synonym="L8; uL2"
                     /coded_by="NM_001317782.2:262..1035"
                     /db_xref="CCDS:CCDS6433.1"
                     /db_xref="GeneID:6132"
                     /db_xref="HGNC:HGNC:10368"
                     /db_xref="MIM:604177"
ORIGIN      
        1 mgrvirgqrk gagsvfrahv khrkgaarlr avdfaerhgy ikgivkdiih dpgrgaplak
       61 vvfrdpyrfk krtelfiaae gihtgqfvyc gkkaqlnign vlpvgtmpeg tivccleekp
      121 gdrgklaras gnyatvishn petkktrvkl psgskkviss anravvgvva gggridkpil
      181 kagrayhkyk akrncwprvr gvamnpvehp fgggnhqhig kpstirrdap agrkvgliaa
      241 rrtgrlrgtk tvqeken
//
LOCUS       NP_001278898             589 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA polymerase eta isoform 2 [Homo sapiens].
ACCESSION   NP_001278898
VERSION     NP_001278898.1
DBSOURCE    REFSEQ: accession NM_001291969.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Menck,C.F.M., Galhardo,R.S. and Quinet,A.
  TITLE     The accurate bypass of pyrimidine dimers by DNA polymerase eta
            contributes to ultraviolet-induced mutagenesis
  JOURNAL   Mutat Res 828, 111840 (2024)
   PUBMED   37984186
  REMARK    GeneRIF: The accurate bypass of pyrimidine dimers by DNA polymerase
            eta contributes to ultraviolet-induced mutagenesis.
            Review article
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Richie-Jannetta,R., Pallan,P., Kingsley,P.J., Kamdar,N., Egli,M.
            and Marnett,L.J.
  TITLE     The peroxidation-derived DNA adduct, 6-oxo-M1dG, is a strong block
            to replication by human DNA polymerase eta
  JOURNAL   J Biol Chem 299 (8), 105067 (2023)
   PUBMED   37468099
  REMARK    GeneRIF: The peroxidation-derived DNA adduct, 6-oxo-M1dG, is a
            strong block to replication by human DNA polymerase eta.
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Averill,J.R. and Jung,H.
  TITLE     Mutagenic incorporation of inosine into DNA via T:I mismatch
            formation by human DNA polymerase eta (poleta)
  JOURNAL   Biochem J 480 (9), 649-664 (2023)
   PUBMED   37129084
  REMARK    GeneRIF: Mutagenic incorporation of inosine into DNA via T:I
            mismatch formation by human DNA polymerase eta (poleta).
REFERENCE   4  (residues 1 to 589)
  AUTHORS   Chakraborty,A., Tapryal,N., Islam,A., Sarker,A.H., Manohar,K.,
            Mitra,J., Hegde,M.L. and Hazra,T.
  TITLE     Human DNA polymerase eta promotes RNA-templated error-free repair
            of DNA double-strand breaks
  JOURNAL   J Biol Chem 299 (3), 102991 (2023)
   PUBMED   36758800
  REMARK    GeneRIF: Human DNA polymerase eta promotes RNA-templated error-free
            repair of DNA double-strand breaks.
REFERENCE   5  (residues 1 to 589)
  AUTHORS   Chang,C., Lee Luo,C., Eleraky,S., Lin,A., Zhou,G. and Gao,Y.
  TITLE     Primer terminal ribonucleotide alters the active site dynamics of
            DNA polymerase eta and reduces DNA synthesis fidelity
  JOURNAL   J Biol Chem 299 (3), 102938 (2023)
   PUBMED   36702254
  REMARK    GeneRIF: Primer terminal ribonucleotide alters the active site
            dynamics of DNA polymerase eta and reduces DNA synthesis fidelity.
REFERENCE   6  (residues 1 to 589)
  AUTHORS   Yamada,A., Masutani,C., Iwai,S. and Hanaoka,F.
  TITLE     Complementation of defective translesion synthesis and UV light
            sensitivity in xeroderma pigmentosum variant cells by human and
            mouse DNA polymerase eta
  JOURNAL   Nucleic Acids Res 28 (13), 2473-2480 (2000)
   PUBMED   10871396
REFERENCE   7  (residues 1 to 589)
  AUTHORS   Masutani,C., Kusumoto,R., Iwai,S. and Hanaoka,F.
  TITLE     Mechanisms of accurate translesion synthesis by human DNA
            polymerase eta
  JOURNAL   EMBO J 19 (12), 3100-3109 (2000)
   PUBMED   10856253
REFERENCE   8  (residues 1 to 589)
  AUTHORS   Johnson,R.E., Kondratick,C.M., Prakash,S. and Prakash,L.
  TITLE     hRAD30 mutations in the variant form of xeroderma pigmentosum
  JOURNAL   Science 285 (5425), 263-265 (1999)
   PUBMED   10398605
REFERENCE   9  (residues 1 to 589)
  AUTHORS   Masutani,C., Kusumoto,R., Yamada,A., Dohmae,N., Yokoi,M., Yuasa,M.,
            Araki,M., Iwai,S., Takio,K. and Hanaoka,F.
  TITLE     The XPV (xeroderma pigmentosum variant) gene encodes human DNA
            polymerase eta
  JOURNAL   Nature 399 (6737), 700-704 (1999)
   PUBMED   10385124
REFERENCE   10 (residues 1 to 589)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK307660.1, AK023893.1 and
            AL353602.10.
            
            Summary: This gene encodes a member of the Y family of specialized
            DNA polymerases. It copies undamaged DNA with a lower fidelity than
            other DNA-directed polymerases. However, it accurately replicates
            UV-damaged DNA; when thymine dimers are present, this polymerase
            inserts the complementary nucleotides in the newly synthesized DNA,
            thereby bypassing the lesion and suppressing the mutagenic effect
            of UV-induced DNA damage. This polymerase is thought to be involved
            in hypermutation during immunoglobulin class switch recombination.
            Mutations in this gene result in XPV, a variant type of xeroderma
            pigmentosum. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, May
            2014].
            
            Transcript Variant: This variant (2) lacks two alternate exons
            compared to variant 1. The resulting isoform (2) has a shorter and
            distinct N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK307660.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..589
                     /product="DNA polymerase eta isoform 2"
                     /EC_number="2.7.7.7"
                     /note="xeroderma pigmentosum variant type protein; RAD30
                     homolog A; polymerase (DNA directed), eta; polymerase
                     (DNA) eta; DNA polymerase eta transcript"
                     /calculated_mol_wt=64700
     Region          <66..304
                     /region_name="PolY"
                     /note="Y-family of DNA polymerases; cl28996"
                     /db_xref="CDD:452909"
     Site            order(132..138,169,193..198,227,256..260,262)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176456"
     Region          507..537
                     /region_name="zf_UBZ"
                     /note="Ubiquitin-Binding Zinc Finger; pfam18439"
                     /db_xref="CDD:465769"
     CDS             1..589
                     /gene="POLH"
                     /gene_synonym="RAD30; RAD30A; XP-V; XPV"
                     /coded_by="NM_001291969.2:274..2043"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:5429"
                     /db_xref="HGNC:HGNC:9181"
                     /db_xref="MIM:603968"
ORIGIN      
        1 mklvhlesle vcgqmmlrsy vqifywhkfv spvgkltspk gmrkqglfqw ldslqidnlt
       61 spdlqltvga viveemraai eretgfqcsa gishnkvlak lacglnkpnr qtlvshgsvp
      121 qlfsqmpirk irslggklga svieilgiey mgeltqftes qlqshfgekn gswlyamcrg
      181 iehdpvkprq lpktigcskn fpgktalatr eqvqwwllql aqeleerltk drndndrvat
      241 qlvvsirvqg dkrlsslrrc caltrydahk mshdaftvik ncntsgiqte wsppltmlfl
      301 catkfsasap ssstditsfl ssdpsslpkv pvtsseaktq gsgpavtatk kattslesff
      361 qkaaerqkvk easlssltap tqapmsnsps kpslpfqtsq stgtepffkq kslllkqkql
      421 nnssvsspqq npwsnckalp nslpteypgc vpvcegvskl eesskatpae mdlahnsqsm
      481 hassasksvl evtqkatpnp sllaaedqvp cekcgslvpv wdmpehmdyh falelqksfl
      541 qphssnpqvv savshqgkrn pksplactnk rprpegmqtl esffkplth
//
LOCUS       NP_001138841             782 aa            linear   PRI 21-NOV-2025
DEFINITION  tyrosine-protein phosphatase non-receptor type 3 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001138841
VERSION     NP_001138841.1
DBSOURCE    REFSEQ: accession NM_001145369.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Masuda,S., Onishi,H., Iwamoto,N., Imaizumi,A., Koga,S., Nagao,S.,
            Sakanashi,K., Itoyama,S., Fujimura,A., Komune,N., Kogo,R.,
            Umebayashi,M., Morisaki,T. and Nakagawa,T.
  TITLE     Inhibition of PTPN3 Expressed in Activated Lymphocytes Enhances the
            Antitumor Effects of Anti-PD-1 Therapy in Head and Neck Cancer,
            Especially in Hypoxic Environments
  JOURNAL   J Immunother 47 (3), 89-97 (2024)
   PUBMED   38297883
  REMARK    GeneRIF: Inhibition of PTPN3 Expressed in Activated Lymphocytes
            Enhances the Antitumor Effects of Anti-PD-1 Therapy in Head and
            Neck Cancer, Especially in Hypoxic Environments.
REFERENCE   4  (residues 1 to 782)
  AUTHORS   Zhou,Z., Lin,Z., Wang,M., Wang,L., Ji,Y., Yang,J., Yang,Y., Zhu,G.
            and Liu,T.
  TITLE     Identification and verification of PTPN3 as a novel biomarker in
            predicting cancer prognosis, immunity, and immunotherapeutic
            efficacy
  JOURNAL   Eur J Med Res 29 (1), 12 (2024)
   PUBMED   38173048
  REMARK    GeneRIF: Identification and verification of PTPN3 as a novel
            biomarker in predicting cancer prognosis, immunity, and
            immunotherapeutic efficacy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 782)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   6  (residues 1 to 782)
  AUTHORS   Zhang,S.H., Kobayashi,R., Graves,P.R., Piwnica-Worms,H. and
            Tonks,N.K.
  TITLE     Serine phosphorylation-dependent association of the band
            4.1-related protein-tyrosine phosphatase PTPH1 with 14-3-3beta
            protein
  JOURNAL   J Biol Chem 272 (43), 27281-27287 (1997)
   PUBMED   9341175
REFERENCE   7  (residues 1 to 782)
  AUTHORS   Ikuta,S., Itoh,F., Hinoda,Y., Toyota,M., Makiguchi,Y., Imai,K. and
            Yachi,A.
  TITLE     Expression of cytoskeletal-associated protein tyrosine phosphatase
            PTPH1 mRNA in human hepatocellular carcinoma
  JOURNAL   J Gastroenterol 29 (6), 727-732 (1994)
   PUBMED   7874267
REFERENCE   8  (residues 1 to 782)
  AUTHORS   Itoh,F., Ikuta,S., Hinoda,Y., Arimura,Y., Ohe,M., Adachi,M.,
            Ariyama,T., Inazawa,J., Imai,K. and Yachi,A.
  TITLE     Expression and chromosomal assignment of PTPH1 gene encoding a
            cytosolic protein tyrosine phosphatase homologous to
            cytoskeletal-associated proteins
  JOURNAL   Int J Cancer 55 (6), 947-951 (1993)
   PUBMED   8253532
REFERENCE   9  (residues 1 to 782)
  AUTHORS   Arimura,Y., Hinoda,Y., Itoh,F., Takekawa,M., Tsujisaki,M.,
            Adachi,M., Imai,K. and Yachi,A.
  TITLE     cDNA cloning of new protein tyrosine phosphatases in the human
            colon
  JOURNAL   Tumour Biol 13 (3), 180-186 (1992)
   PUBMED   1626183
REFERENCE   10 (residues 1 to 782)
  AUTHORS   Yang,Q. and Tonks,N.K.
  TITLE     Isolation of a cDNA clone encoding a human protein-tyrosine
            phosphatase with homology to the cytoskeletal-associated proteins
            band 4.1, ezrin, and talin
  JOURNAL   Proc Natl Acad Sci U S A 88 (14), 5949-5953 (1991)
   PUBMED   1648725
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB306298.1, BX648253.1,
            AL162733.9, BX648735.1, DB173093.1, AK096975.1 and AL359963.29.
            
            Summary: The protein encoded by this gene is a member of the
            protein tyrosine phosphatase (PTP) family. PTPs are known to be
            signaling molecules that regulate a variety of cellular processes
            including cell growth, differentiation, mitotic cycle, and
            oncogenic transformation. This protein contains a C-terminal PTP
            domain and an N-terminal domain homologous to the band 4.1
            superfamily of cytoskeletal-associated proteins. P97, a cell cycle
            regulator involved in a variety of membrane related functions, has
            been shown to be a substrate of this PTP. This PTP was also found
            to interact with, and be regulated by adaptor protein 14-3-3 beta.
            Several alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Feb 2009].
            
            Transcript Variant: This variant (3) differs in the 5' UTR, and
            initiates translation from an in-frame downstream AUG, resulting in
            an isoform (3) with a shorter N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX648735.1, SRR14038191.1491575.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.3"
     Protein         1..782
                     /product="tyrosine-protein phosphatase non-receptor type 3
                     isoform 3"
                     /EC_number="3.1.3.48"
                     /note="cytoskeletal-associated protein tyrosine
                     phosphatase; protein-tyrosine phosphatase H1"
                     /calculated_mol_wt=88684
     Region          2..91
                     /region_name="FERM_M"
                     /note="FERM central domain; pfam00373"
                     /db_xref="CDD:459788"
     Region          85..178
                     /region_name="FERM_C_PTPN4_PTPN3_like"
                     /note="FERM domain C-lobe of Protein tyrosine phosphatase
                     non-receptor proteins 3 and 4 (PTPN4 and PTPN3); cd13189"
                     /db_xref="CDD:270010"
     Site            order(95,112,114,120)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270010"
     Site            order(124,129..132,167,171,174..175)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270010"
     Site            167..178
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270010"
     Region          375..464
                     /region_name="PDZ_PTPN3-4-like"
                     /note="PDZ domain of tyrosine-protein phosphatase
                     non-receptor type 3 (PTPN3), tyrosine-protein phosphatase
                     non-receptor type 4 (PTNP4), and related domains; cd06706"
                     /db_xref="CDD:467190"
     Site            order(389..395,407,410,441,445,448..449)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467190"
     Region          500..773
                     /region_name="PTPc-N3"
                     /note="catalytic domain of tyrosine-protein phosphatase
                     non-receptor type 3; cd14600"
                     /db_xref="CDD:350448"
     CDS             1..782
                     /gene="PTPN3"
                     /gene_synonym="PTP-H1; PTPH1"
                     /coded_by="NM_001145369.2:2555..4903"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS48001.1"
                     /db_xref="GeneID:5774"
                     /db_xref="HGNC:HGNC:9655"
                     /db_xref="MIM:176877"
ORIGIN      
        1 mdicegrltc plnsavvlas yavqshfgdy nssihhpgyl sdshfipdqn edfltkvesl
       61 heqhsglkqs eaescyinia rtldfygvel hsgrdlhnld lmigiasagv avyrkyicts
      121 fypwvnilki sfkrkkffih qrqkqaesre hivafnmlny rscknlwksc vehhtffqak
      181 kllpqeknvl sqywtmgsrn tkksvnnqyc kkviggmvwn pamrrslsve hletkslpsr
      241 sppitpnwrs prlrheirkp rhssadnlan emtyiteted vfytykgsla pqdsdsevsq
      301 nrsphqesls ennpaqsylt qkssssvsps snapgscspd gvdqqllddf hrvtkggste
      361 dasqyycdkn dngdsylvli ritpdedgkf gfnlkggvdq kmplvvsrin pespadtcip
      421 klnegdqivl ingrdiseht hdqvvmfika sreshsrela lvirrravrs fadfksedel
      481 nqlfpeaifp mcpeggdtle gsmaqlkkgl esgtvliqfe qlyrkkpgla itfaklpqnl
      541 dknrykdvlp ydttrvllqg nedyinasyv nmeipaanlv nkyiatqgpl phtcaqfwqv
      601 vwdqklsliv mlttltergr tkchqywpdp pdvmnhggfh iqcqsedcti ayvsremlvt
      661 ntqtgeehtv thlqyvawpd hgvpddssdf lefvnyvrsl rvdsepvlvh csagigrtgv
      721 lvtmetamcl ternlpiypl divrkmrdqr ammvqtssqy kfvceailrv yeeglvqmld
      781 ps
//
LOCUS       NP_001358055            1285 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal cell adhesion molecule isoform H precursor [Homo sapiens].
ACCESSION   NP_001358055
VERSION     NP_001358055.1
DBSOURCE    REFSEQ: accession NM_001371126.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1285)
  AUTHORS   Wang,C., Wang,Z., Fu,L., Du,J., Ji,F. and Qiu,X.
  TITLE     CircNRCAM up-regulates NRCAM to promote papillary thyroid carcinoma
            progression
  JOURNAL   J Endocrinol Invest 47 (5), 1215-1226 (2024)
   PUBMED   38485895
  REMARK    GeneRIF: CircNRCAM up-regulates NRCAM to promote papillary thyroid
            carcinoma progression.
REFERENCE   2  (residues 1 to 1285)
  AUTHORS   Zhou,L., He,L., Liu,C.H., Qiu,H., Zheng,L., Sample,K.M., Wu,Q.,
            Li,J., Xie,K., Ampuero,J., Li,Z., Lv,D., Liu,M., Romero-Gomez,M.,
            Hu,Y. and Tang,H.
  TITLE     Liver cancer stem cell dissemination and metastasis: uncovering the
            role of NRCAM in hepatocellular carcinoma
  JOURNAL   J Exp Clin Cancer Res 42 (1), 311 (2023)
   PUBMED   37993901
  REMARK    GeneRIF: Liver cancer stem cell dissemination and metastasis:
            uncovering the role of NRCAM in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1285)
  AUTHORS   Sannes,A.C., Christensen,J.O., Nielsen,M.B. and Gjerstad,J.
  TITLE     Stress-induced headache in the general working population is
            moderated by the NRCAM rs2300043 genotype
  JOURNAL   Scand J Pain 23 (2), 326-332 (2022)
   PUBMED   36181733
  REMARK    GeneRIF: Stress-induced headache in the general working population
            is moderated by the NRCAM rs2300043 genotype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1285)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 1285)
  AUTHORS   Bai,C. and Chen,D.G.
  TITLE     NRCAM acts as a prognostic biomarker and promotes the tumor
            progression in gastric cancer via EMT pathway
  JOURNAL   Tissue Cell 77, 101859 (2022)
   PUBMED   35763884
  REMARK    GeneRIF: NRCAM acts as a prognostic biomarker and promotes the
            tumor progression in gastric cancer via EMT pathway.
REFERENCE   6  (residues 1 to 1285)
  AUTHORS   Wang,B., Williams,H., Du,J.S., Terrett,J. and Kenwrick,S.
  TITLE     Alternative splicing of human NrCAM in neural and nonneural tissues
  JOURNAL   Mol Cell Neurosci 10 (5-6), 287-295 (1998)
   PUBMED   9604207
REFERENCE   7  (residues 1 to 1285)
  AUTHORS   Grumet,M.
  TITLE     Nr-CAM: a cell adhesion molecule with ligand and receptor functions
  JOURNAL   Cell Tissue Res 290 (2), 423-428 (1997)
   PUBMED   9321706
  REMARK    Review article
REFERENCE   8  (residues 1 to 1285)
  AUTHORS   Sakurai,T., Lustig,M., Nativ,M., Hemperly,J.J., Schlessinger,J.,
            Peles,E. and Grumet,M.
  TITLE     Induction of neurite outgrowth through contactin and Nr-CAM by
            extracellular regions of glial receptor tyrosine phosphatase beta
  JOURNAL   J Cell Biol 136 (4), 907-918 (1997)
   PUBMED   9049255
REFERENCE   9  (residues 1 to 1285)
  AUTHORS   Volkmer,H., Leuschner,R., Zacharias,U. and Rathjen,F.G.
  TITLE     Neurofascin induces neurites by heterophilic interactions with
            axonal NrCAM while NrCAM requires F11 on the axonal surface to
            extend neurites
  JOURNAL   J Cell Biol 135 (4), 1059-1069 (1996)
   PUBMED   8922386
REFERENCE   10 (residues 1 to 1285)
  AUTHORS   Lane,R.P., Chen,X.N., Yamakawa,K., Vielmetter,J., Korenberg,J.R.
            and Dreyer,W.J.
  TITLE     Characterization of a highly conserved human homolog to the chicken
            neural cell surface protein Bravo/Nr-CAM that maps to chromosome
            band 7q31
  JOURNAL   Genomics 35 (3), 456-465 (1996)
   PUBMED   8812479
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005058.1, AC007567.2 and
            AC005683.2.
            
            Summary: Cell adhesion molecules (CAMs) are members of the
            immunoglobulin superfamily. This gene encodes a neuronal cell
            adhesion molecule with multiple immunoglobulin-like C2-type domains
            and fibronectin type-III domains. This ankyrin-binding protein is
            involved in neuron-neuron adhesion and promotes directional
            signaling during axonal cone growth. This gene is also expressed in
            non-neural tissues and may play a general role in cell-cell
            communication via signaling from its intracellular domain to the
            actin cytoskeleton during directional cell migration. Allelic
            variants of this gene have been associated with autism and
            addiction vulnerability. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (27), as well as variants 26 and
            28, encodes isoform H.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1285
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1285
                     /product="neuronal cell adhesion molecule isoform H
                     precursor"
                     /note="NgCAM-related cell adhesion molecule; neuronal
                     surface protein Bravo"
                     /calculated_mol_wt=138524
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3315
     Region          46..140
                     /region_name="IgI_NrCAM"
                     /note="Immunoglobulin (Ig)-like domain of NrCAM (Ng
                     (neuronglia) CAM-related cell adhesion molecule); member
                     of the I-set of Ig superfamily (IgSF) domains; cd05874"
                     /db_xref="CDD:409458"
     Region          46..50
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409458"
     Region          55..59
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409458"
     Region          64..71
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409458"
     Region          77..82
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409458"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          85..87
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409458"
     Region          94..97
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409458"
     Region          102..106
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409458"
     Region          119..127
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409458"
     Region          130..140
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409458"
     Region          149..238
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          163..167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409432"
     Region          177..181
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409432"
     Region          200..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409432"
     Region          215..220
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409432"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          231..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409432"
     Site            257
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          258..339
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          269..273
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          282..286
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            295
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          304..308
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          318..323
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          331..334
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          343..431
                     /region_name="Ig4_NrCAM"
                     /note="Fourth immunoglobulin (Ig)-like domain of NrCAM
                     (NgCAM-related cell adhesion molecule); cd05868"
                     /db_xref="CDD:409454"
     Region          359..363
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409454"
     Region          372..376
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409454"
     Region          396..400
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409454"
     Region          410..415
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409454"
     Site            414
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          423..426
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409454"
     Region          440..523
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          453..457
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          466..470
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            488
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          489..493
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          503..508
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          516..519
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          527..1090
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            600
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Region          628..718
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(628,694,709)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            697
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            order(710..711,713..714)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            783
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            839
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            974
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            990
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1000
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1053
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1064
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1096
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1149..1171
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92823.3)"
     Region          1172..1261
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     Region          1180..1285
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1202
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q810U4; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1206
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q810U4; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q810U4; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q810U4; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q810U4; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97686; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q810U4; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q810U4; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     Site            1276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q810U4; propagated from
                     UniProtKB/Swiss-Prot (Q92823.3)"
     CDS             1..1285
                     /gene="NRCAM"
                     /gene_synonym="NEDNMS"
                     /coded_by="NM_001371126.1:680..4537"
                     /note="isoform H precursor is encoded by transcript
                     variant 27"
                     /db_xref="GeneID:4897"
                     /db_xref="HGNC:HGNC:7994"
                     /db_xref="MIM:601581"
ORIGIN      
        1 mqlkimpkkk rlsagrvpli lflcqmisal evpldpklle dlvqpptitq qspkdyiidp
       61 reniviqcea kgkpppsfsw trngthfdid kdplvtmkpg tgtliinims egkaetyegv
      121 yqctarnerg aavsnnivvr psrsplwtke klepitlqsg qslvlpcrpp iglpppiifw
      181 mdnsfqrlpq servsqglng dlyfsnvlpe dtredyicya rfnhtqtiqq kqpisvkvis
      241 akssrerppt fltpegnasn keelrgnvls leciaeglpt piiywakedg mlpknrtvyk
      301 nfektlqiih vseadsgnyq ciaknalgai hhtisvrvka apywitapqn lvlspgedgt
      361 licrangnpk priswltngv pieiapddps rkidgdtiif snvqerssav yqcnasneyg
      421 yllanafvnv laeppriltp antlyqvian rpalldcaff gsplptiewf kgakgsalhe
      481 diyvlhengt leipvaqkds tgtytcvarn klgmaknevh leikdptwiv kqpeyavvqr
      541 gsmvsfeckv khdhtlsltv lwlkdnrelp sderftvdkd hlvvadvsdd dsgtytcvan
      601 ttldsvsasa vlsvvaptpt papvydvpnp pfdleltdql dksvqlswtp gddnnspitk
      661 fiieyedamh kpglwhhqte vsgtqttaql klspyvnysf rvmavnsigk slpseaseqy
      721 ltkasepdkn ptaveglgse pdnlvitwkp lngfesngpg lqykvswrqk dgddewtsvv
      781 vanvskyivs gtptfvpyli kvqalndmgf apepavvmgh sgedlpmvap gnvrvnvvns
      841 tlaevhwdpv plksirghlq gyriyywktq ssskrnrrhi ekkiltfqgs kthgmlpgle
      901 pfshytlnvr vvngkgegpa spdrvfntpe gvpsapsslk ivnptldslt lewdppshpn
      961 gilteytlky qpinsthelg plvdlkipan ktrwtlknln fstrykfyfy aqtsagsgsq
     1021 iteeavttvd eagilppdvg agkvqavnpr isnltaaaae tyanisweye gpehvnfyve
     1081 ygvagskeew rkeivngsrs ffglkglmpg taykvrvgav gdsgfvssed vfetgpamas
     1141 rqvdiatqgw figlmcaval lilillivcf irrnkggkyp vkekedahad peiqpmkedd
     1201 gtfgeysdae dhkplkkgsr tpsdrtvkke dsddslvdyg egvngqfned gsfigqysgk
     1261 kekepaegne sseapspvna mnsfv
//
LOCUS       NP_001371811             748 aa            linear   PRI 21-NOV-2025
DEFINITION  signal transducer and activator of transcription 1-alpha/beta
            isoform 3 [Homo sapiens].
ACCESSION   NP_001371811
VERSION     NP_001371811.1
DBSOURCE    REFSEQ: accession NM_001384882.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 748)
  AUTHORS   Wang,Y., Song,Q., Huang,W., Lin,Y., Wang,X., Wang,C., Willard,B.,
            Zhao,C., Nan,J., Holvey-Bates,E., Wang,Z., Taylor,D., Yang,J. and
            Stark,G.R.
  TITLE     A virus-induced conformational switch of STAT1-STAT2 dimers boosts
            antiviral defenses
  JOURNAL   Cell Res 31 (2), 206-218 (2021)
   PUBMED   32759968
REFERENCE   3  (residues 1 to 748)
  AUTHORS   Decker,T. and Kovarik,P.
  TITLE     Serine phosphorylation of STATs
  JOURNAL   Oncogene 19 (21), 2628-2637 (2000)
   PUBMED   10851062
  REMARK    Review article
REFERENCE   4  (residues 1 to 748)
  AUTHORS   Bowman,T., Garcia,R., Turkson,J. and Jove,R.
  TITLE     STATs in oncogenesis
  JOURNAL   Oncogene 19 (21), 2474-2488 (2000)
   PUBMED   10851046
  REMARK    Review article
REFERENCE   5  (residues 1 to 748)
  AUTHORS   Haddad,B., Pabon-Pena,C.R., Young,H. and Sun,W.H.
  TITLE     Assignment1 of STAT1 to human chromosome 2q32 by FISH and radiation
            hybrids
  JOURNAL   Cytogenet Cell Genet 83 (1-2), 58-59 (1998)
   PUBMED   9925928
REFERENCE   6  (residues 1 to 748)
  AUTHORS   Yan,R., Qureshi,S., Zhong,Z., Wen,Z. and Darnell,J.E. Jr.
  TITLE     The genomic structure of the STAT genes: multiple exons in
            coincident sites in Stat1 and Stat2
  JOURNAL   Nucleic Acids Res 23 (3), 459-463 (1995)
   PUBMED   7885841
REFERENCE   7  (residues 1 to 748)
  AUTHORS   Igarashi,K., Garotta,G., Ozmen,L., Ziemiecki,A., Wilks,A.F.,
            Harpur,A.G., Larner,A.C. and Finbloom,D.S.
  TITLE     Interferon-gamma induces tyrosine phosphorylation of
            interferon-gamma receptor and regulated association of protein
            tyrosine kinases, Jak1 and Jak2, with its receptor
  JOURNAL   J Biol Chem 269 (20), 14333-14336 (1994)
   PUBMED   7514165
REFERENCE   8  (residues 1 to 748)
  AUTHORS   Shuai,K., Horvath,C.M., Huang,L.H., Qureshi,S.A., Cowburn,D. and
            Darnell,J.E. Jr.
  TITLE     Interferon activation of the transcription factor Stat91 involves
            dimerization through SH2-phosphotyrosyl peptide interactions
  JOURNAL   Cell 76 (5), 821-828 (1994)
   PUBMED   7510216
REFERENCE   9  (residues 1 to 748)
  AUTHORS   Schindler,C., Fu,X.Y., Improta,T., Aebersold,R. and Darnell,J.E.
            Jr.
  TITLE     Proteins of transcription factor ISGF-3: one gene encodes the
            91-and 84-kDa ISGF-3 proteins that are activated by interferon
            alpha
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7836-7839 (1992)
   PUBMED   1502203
REFERENCE   10 (residues 1 to 748)
  AUTHORS   Schindler,C., Shuai,K., Prezioso,V.R. and Darnell,J.E. Jr.
  TITLE     Interferon-dependent tyrosine phosphorylation of a latent
            cytoplasmic transcription factor
  JOURNAL   Science 257 (5071), 809-813 (1992)
   PUBMED   1496401
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC067945.4.
            
            Summary: The protein encoded by this gene is a member of the STAT
            protein family. In response to cytokines and growth factors, STAT
            family members are phosphorylated by the receptor associated
            kinases, and then form homo- or heterodimers that translocate to
            the cell nucleus where they act as transcription activators. The
            protein encoded by this gene can be activated by various ligands
            including interferon-alpha, interferon-gamma, EGF, PDGF and IL6.
            This protein mediates the expression of a variety of genes, which
            is thought to be important for cell viability in response to
            different cell stimuli and pathogens. The protein plays an
            important role in immune responses to viral, fungal and
            mycobacterial pathogens. Mutations in this gene are associated with
            Immunodeficiency 31B, 31A, and 31C. [provided by RefSeq, Jun 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2885966.1,
                                           SRR18074967.777735.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.2"
     Protein         1..748
                     /product="signal transducer and activator of transcription
                     1-alpha/beta isoform 3"
                     /note="transcription factor ISGF-3 components p91/p84;
                     signal transducer and activator of transcription
                     1-alpha/beta; signal transducer and activator of
                     transcription 1, 91kD; signal transducer and activator of
                     transcription 1, 91kDa"
                     /calculated_mol_wt=86901
     Region          2..121
                     /region_name="STAT_int"
                     /note="STAT protein, protein interaction domain;
                     smart00964"
                     /db_xref="CDD:214942"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            114
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Region          138..313
                     /region_name="STAT1_CCD"
                     /note="Coiled-coil domain of Signal Transducer and
                     Activator of Transcription 1 (STAT1); cd16851"
                     /db_xref="CDD:341076"
     Site            order(164..165,168..169,172,175..176,179,232,236,239..241,
                     243..244,256..257,259..260,263..264,267,271,274,306,
                     309..311)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:341076"
     Site            175
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            order(239..241,243..244,256..257,260,263..264,267,271,274,
                     302,306,309..310)
                     /site_type="other"
                     /note="CCD-DBD interface [polypeptide binding]"
                     /db_xref="CDD:341076"
     Site            296
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Region          317..475
                     /region_name="STAT1_DBD"
                     /note="DNA-binding domain of Signal Transducer and
                     Activator of Transcription 1 (STAT1); cd16845"
                     /db_xref="CDD:341083"
     Site            order(336,340,409,411,424..425,457..458,461)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:341083"
     Site            366
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            523
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Region          555..705
                     /region_name="SH2_STAT1"
                     /note="Src homology 2 (SH2) domain found in signal
                     transducer and activator of transcription (STAT) 1
                     proteins; cd10372"
                     /db_xref="CDD:198235"
     Site            order(582,600,628,630)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198235"
     Site            order(629,645)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198235"
     Site            635
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            order(639..640,704)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:198235"
     Site            663
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            699
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK1, JAK2 or TYK2.
                     /evidence=ECO:0000269|PubMed:17561467,
                     ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:21135090,
                     ECO:0000269|PubMed:22065572, ECO:0000269|PubMed:26479788,
                     ECO:0000269|PubMed:27796300, ECO:0000269|PubMed:28753426,
                     ECO:0000269|PubMed:38621137, ECO:0000269|PubMed:7657660;
                     propagated from UniProtKB/Swiss-Prot (P42224.2)"
     Site            706
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKE.
                     /evidence=ECO:0000269|PubMed:22065572; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Region          713..737
                     /region_name="STAT1_TAZ2bind"
                     /note="STAT1 TAZ2 binding domain; pfam12162"
                     /db_xref="CDD:432372"
     Site            722
                     /site_type="other"
                     /note="Required for recruitment of EP300/p300.
                     /evidence=ECO:0000269|PubMed:16257975; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            725
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CAMK2 and MAPK14.
                     /evidence=ECO:0000269|PubMed:11972023,
                     ECO:0000269|PubMed:15322115, ECO:0000269|PubMed:16257975,
                     ECO:0000269|PubMed:17897103, ECO:0000269|PubMed:21135090,
                     ECO:0000269|PubMed:22065572, ECO:0000269|PubMed:26479788,
                     ECO:0000269|PubMed:38621137, ECO:0000269|PubMed:7543024,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            743
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKE.
                     /evidence=ECO:0000250|UniProtKB:P42225; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            747
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by IKKB.
                     /evidence=ECO:0000269|PubMed:32209697,
                     ECO:0000269|PubMed:38621137; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     CDS             1..748
                     /gene="STAT1"
                     /gene_synonym="CANDF7; IMD31A; IMD31B; IMD31C; ISGF-3;
                     STAT91"
                     /coded_by="NM_001384882.1:310..2556"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92918.1"
                     /db_xref="GeneID:6772"
                     /db_xref="HGNC:HGNC:11362"
                     /db_xref="MIM:600555"
ORIGIN      
        1 msqwyelqql dskfleqvhq lyddsfpmei rqylaqwlek qdwehaandv sfatirfhdl
       61 lsqlddqysr fslennfllq hnirkskrnl qdnfqedpiq msmiiysclk eerkilenaq
      121 rfnqaqsgni qstvmldkqk eldskvrnvk dkvmciehei ksledlqdey dfkcktlqnr
      181 ehetngvaks dqkqeqlllk kmylmldnkr kevvhkiiel lnvteltqna lindelvewk
      241 rrqqsacigg ppnacldqlq nwftivaesl qqvrqqlkkl eeleqkytye hdpitknkqv
      301 lwdrtfslfq qliqssfvve rqpcmpthpq rplvlktgvq ftvklrllvk lqelnynlkv
      361 kvlfdkdvne rntvkgkfni lgthtkvmnm eestngslaa efrhlqlkeq knagtrtneg
      421 plivteelhs lsfetqlcqp glvidletts lpvvvisnvs qlpsgwasil wynmlvaepr
      481 nlsffltppc arwaqlsevl swqfssvtkr glnvdqlnml gekllgpnas pdglipwtrf
      541 ckenindknf pfwlwiesil elikkhllpl wndgcimgfi skererallk dqqpgtfllr
      601 fsessregai tftwversqn ggepdfhave pytkkelsav tfpdiirnyk vmaaenipen
      661 plkylypnid kdhafgkyys rpkeapepme ldgpkgtgyi ktelisvsev hpsrlqttdn
      721 llpmspeefd evsrivgsve fdsmmntv
//
LOCUS       NP_001340224             178 aa            linear   PRI 21-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 2 [Homo sapiens].
ACCESSION   NP_001340224
VERSION     NP_001340224.1
DBSOURCE    REFSEQ: accession NM_001353295.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.129334.1,
                                           SRR3476690.300955.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..178
                     /product="CYFIP-related Rac1 interactor B isoform 2"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=20062
     Region          <1..174
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..178
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353295.2:673..1209"
                     /note="isoform 2 is encoded by transcript variant 57"
                     /db_xref="CCDS:CCDS83327.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mtnpaiqndf syyrrtlsrm rinnvpaege nevnnelanr mslfyaeatp mlktlsdatt
       61 kfvsenknlp ienttdclst masvcrvmle tpeyrsrftn eetvsfclrv mvgviilydh
      121 vhpvgafakt skidmkgcik vlkdqppnsv egllnalryt tkhlndetts kqiksmlq
//
LOCUS       NP_001138388             706 aa            linear   PRI 21-NOV-2025
DEFINITION  fibroblast growth factor receptor 2 isoform 6 precursor [Homo
            sapiens].
ACCESSION   NP_001138388
VERSION     NP_001138388.1
DBSOURCE    REFSEQ: accession NM_001144916.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Chen,C.P., Huang,J.P., Huang,K.S., Chen,Y.Y., Wu,F.T., Pan,Y.T.,
            Chiu,C.L. and Wang,W.
  TITLE     Perinatal imaging findings of a fetus with Pfeiffer syndrome and a
            heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation in FGFR2
            presenting a cloverleaf skull, craniosynostosis and short limbs on
            prenatal ultrasound mimicking thanatophoric dysplasia type II
  JOURNAL   Taiwan J Obstet Gynecol 63 (3), 387-390 (2024)
   PUBMED   38802203
  REMARK    GeneRIF: Perinatal imaging findings of a fetus with Pfeiffer
            syndrome and a heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation
            in FGFR2 presenting a cloverleaf skull, craniosynostosis and short
            limbs on prenatal ultrasound mimicking thanatophoric dysplasia type
            II.
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Lian,Y., Bodian,D. and Shehu,A.
  TITLE     Elucidating the Role of Wildtype and Variant FGFR2 Structural
            Dynamics in (Dys)Function and Disorder
  JOURNAL   Int J Mol Sci 25 (8), 4523 (2024)
   PUBMED   38674107
  REMARK    GeneRIF: Elucidating the Role of Wildtype and Variant FGFR2
            Structural Dynamics in (Dys)Function and Disorder.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 706)
  AUTHORS   Xu,N., Hung,K.L., Gong,X., Fan,D., Tian,Y., Yan,M., Wei,Y. and
            Wang,S.
  TITLE     Genetic insights into the 'sandwich fusion' subtype of Klippel-Feil
            syndrome: novel FGFR2 mutations identified by 21 cases of
            whole-exome sequencing
  JOURNAL   Orphanet J Rare Dis 19 (1), 141 (2024)
   PUBMED   38561822
  REMARK    GeneRIF: Genetic insights into the 'sandwich fusion' subtype of
            Klippel-Feil syndrome: novel FGFR2 mutations identified by 21 cases
            of whole-exome sequencing.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 706)
  AUTHORS   Wenger,T.L., Hing,A.V. and Evans,K.N.
  TITLE     Apert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31145570
REFERENCE   5  (residues 1 to 706)
  AUTHORS   Wenger,T., Miller,D. and Evans,K.
  TITLE     FGFR Craniosynostosis Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301628
REFERENCE   6  (residues 1 to 706)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   7  (residues 1 to 706)
  AUTHORS   Dell,K.R. and Williams,L.T.
  TITLE     A novel form of fibroblast growth factor receptor 2. Alternative
            splicing of the third immunoglobulin-like domain confers ligand
            binding specificity
  JOURNAL   J Biol Chem 267 (29), 21225-21229 (1992)
   PUBMED   1400433
REFERENCE   8  (residues 1 to 706)
  AUTHORS   Luqmani,Y.A., Graham,M. and Coombes,R.C.
  TITLE     Expression of basic fibroblast growth factor, FGFR1 and FGFR2 in
            normal and malignant human breast, and comparison with other normal
            tissues
  JOURNAL   Br J Cancer 66 (2), 273-280 (1992)
   PUBMED   1380281
REFERENCE   9  (residues 1 to 706)
  AUTHORS   Katoh,M., Hattori,Y., Sasaki,H., Tanaka,M., Sugano,K., Yazaki,Y.,
            Sugimura,T. and Terada,M.
  TITLE     K-sam gene encodes secreted as well as transmembrane receptor
            tyrosine kinase
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 2960-2964 (1992)
   PUBMED   1313574
REFERENCE   10 (residues 1 to 706)
  AUTHORS   Miki,T., Bottaro,D.P., Fleming,T.P., Smith,C.L., Burgess,W.H.,
            Chan,A.M. and Aaronson,S.A.
  TITLE     Determination of ligand-binding specificity by alternative
            splicing: two distinct growth factor receptors encoded by a single
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 246-250 (1992)
   PUBMED   1309608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK308621.1, M97193.1,
            BC037338.2 and CB305736.1.
            
            Summary: The protein encoded by this gene is a member of the
            fibroblast growth factor receptor family, where amino acid sequence
            is highly conserved between members and throughout evolution. FGFR
            family members differ from one another in their ligand affinities
            and tissue distribution. A full-length representative protein
            consists of an extracellular region, composed of three
            immunoglobulin-like domains, a single hydrophobic membrane-spanning
            segment and a cytoplasmic tyrosine kinase domain. The extracellular
            portion of the protein interacts with fibroblast growth factors,
            setting in motion a cascade of downstream signals, ultimately
            influencing mitogenesis and differentiation. This particular family
            member is a high-affinity receptor for acidic, basic and/or
            keratinocyte growth factor, depending on the isoform. Mutations in
            this gene are associated with Crouzon syndrome, Pfeiffer syndrome,
            Craniosynostosis, Apert syndrome, Jackson-Weiss syndrome,
            Beare-Stevenson cutis gyrata syndrome, Saethre-Chotzen syndrome,
            and syndromic craniosynostosis. Multiple alternatively spliced
            transcript variants encoding different isoforms have been noted for
            this gene. [provided by RefSeq, Jan 2009].
            
            Transcript Variant: This variant (6) uses an alternate 5' terminal
            exon, and is missing two consecutive in-frame coding exons,
            compared to transcript variant 1. This results in a shorter isoform
            (6) lacking an internal protein segment compared to isoform 1.
            
            Sequence Note: A downstream AUG translation start codon is selected
            for this RefSeq based on the presence of a strong Kozak consensus
            signal, a strong community standard for the use of the downstream
            start codon, and on a higher probability of an N-terminal signal
            peptide being present in the resulting protein. The use of an
            alternative in-frame upstream AUG start codon would result in a
            protein that is 19 aa longer at the N-terminus. Translation from
            the annotated downstream start codon is likely to occur via leaky
            scanning and/or reinitiation.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK308621.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: community standard (PMID:
                                                15863034)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..706
                     /product="fibroblast growth factor receptor 2 isoform 6
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="protein tyrosine kinase, receptor like 14;
                     bacteria-expressed kinase; keratinocyte growth factor
                     receptor; BEK fibroblast growth factor receptor"
                     /calculated_mol_wt=77118
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2298
     mat_peptide     22..706
                     /product="fibroblast growth factor receptor 2 isoform 6"
                     /calculated_mol_wt=77118
     Region          39..133
                     /region_name="IgI_2_FGFR"
                     /note="Second immunoglobulin (Ig)-like domain of
                     fibroblast growth factor (FGF) receptor; member of the
                     I-set of IgSF domains; cd05857"
                     /db_xref="CDD:409443"
     Region          39..42
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409443"
     Region          50..55
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409443"
     Site            order(51,53,55)
                     /site_type="other"
                     /note="FGF binding site [polypeptide binding]"
                     /db_xref="CDD:409443"
     Site            order(52,59..61,63)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409443"
     Region          59..67
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409443"
     Region          73..78
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409443"
     Region          81..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409443"
     Region          92..95
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409443"
     Region          99..104
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409443"
     Region          113..120
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409443"
     Region          123..133
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409443"
     Region          141..245
                     /region_name="IgI_3_FGFR2"
                     /note="Third immunoglobulin (Ig)-like domain of fibroblast
                     growth factor receptor 2 (FGFR2); member of the I-set of
                     Ig superfamily (IgSF) domains; cd05858"
                     /db_xref="CDD:409444"
     Region          141..144
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409444"
     Region          148..152
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409444"
     Region          160..167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409444"
     Site            order(165,170..172,201..202,206,210,231)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409444"
     Region          171..178
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409444"
     Region          193..198
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409444"
     Region          210..215
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409444"
     Region          223..231
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409444"
     Region          234..242
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409444"
     Region          341..653
                     /region_name="PTKc_FGFR2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Fibroblast Growth Factor Receptor 2; cd05101"
                     /db_xref="CDD:270679"
     Site            order(372..373,375,380,400,402,419,449..452,456,511,
                     515..516,518,529,547..551,560,594)
                     /site_type="active"
                     /db_xref="CDD:270679"
     Site            order(372..373,375,380,400,402,419,449..452,456,515..516,
                     518,529)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270679"
     Site            order(511,515,547..551,560,594)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270679"
     Site            528..553
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270679"
     CDS             1..706
                     /gene="FGFR2"
                     /gene_synonym="BBDS; BEK; BFR-1; CD332; CEK3; CFD1; ECT1;
                     JWS; K-SAM; KGFR; TK14; TK25"
                     /coded_by="NM_001144916.2:442..2562"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:2263"
                     /db_xref="HGNC:HGNC:3689"
                     /db_xref="MIM:176943"
ORIGIN      
        1 mvswgrficl vvvtmatlsl arpsfslved ttlepegapy wtntekmekr lhavpaantv
       61 kfrcpaggnp mptmrwlkng kefkqehrig gykvrnqhws limesvvpsd kgnytcvven
      121 eygsinhtyh ldvversphr pilqaglpan astvvggdve fvckvysdaq phiqwikhve
      181 kngskygpdg lpylkvlkaa gvnttdkeie vlyirnvtfe dageytclag nsigisfhsa
      241 wltvlpapgr ekeitaspdy leiaiycigv fliacmvvtv ilcrmknttk kpdfssqpav
      301 hkltkriplr rqvtvsaess ssmnsntplv rittrlssta dtpmlagvse yelpedpkwe
      361 fprdkltlgk plgegcfgqv vmaeavgidk dkpkeavtva vkmlkddate kdlsdlvsem
      421 emmkmigkhk niinllgact qdgplyvive yaskgnlrey lrarrppgme ysydinrvpe
      481 eqmtfkdlvs ctyqlargme ylasqkcihr dlaarnvlvt ennvmkiadf glardinnid
      541 yykkttngrl pvkwmapeal fdrvythqsd vwsfgvlmwe iftlggspyp gipveelfkl
      601 lkeghrmdkp anctnelymm mrdcwhavps qrptfkqlve dldriltltt neeyldlsqp
      661 leqyspsypd trsscssgdd svfspdpmpy epclpqyphi ngsvkt
//
LOCUS       NP_001295114             428 aa            linear   PRI 21-NOV-2025
DEFINITION  cyclin-L1 isoform 2 [Homo sapiens].
ACCESSION   NP_001295114 XP_005247704
VERSION     NP_001295114.1
DBSOURCE    REFSEQ: accession NM_001308185.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Wang,C., Xu,L., Du,C., Yun,H., Wang,K., Liu,H., Ye,M., Fan,J.,
            Zhou,Y. and Cheng,H.
  TITLE     CDK11 requires a critical activator SAP30BP to regulate pre-mRNA
            splicing
  JOURNAL   EMBO J 42 (24), e114051 (2023)
   PUBMED   38059508
REFERENCE   3  (residues 1 to 428)
  AUTHORS   O'Brien,S., Kelso,S., Steinhart,Z., Orlicky,S., Mis,M., Kim,Y.,
            Lin,S., Sicheri,F. and Angers,S.
  TITLE     SCFFBXW7 regulates G2-M progression through control of CCNL1
            ubiquitination
  JOURNAL   EMBO Rep 23 (12), e55044 (2022)
   PUBMED   36278408
  REMARK    GeneRIF: SCF[FBXW7] regulates G2-M progression through control of
            CCNL1 ubiquitination.
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Zeng,X., Hu,Z., Shen,Y., Wei,X., Gan,J. and Liu,Z.
  TITLE     MiR-5195-3p functions as a tumor suppressor in prostate cancer via
            targeting CCNL1
  JOURNAL   Cell Mol Biol Lett 27 (1), 25 (2022)
   PUBMED   35260070
  REMARK    GeneRIF: MiR-5195-3p functions as a tumor suppressor in prostate
            cancer via targeting CCNL1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Hu,D., Mayeda,A., Trembley,J.H., Lahti,J.M. and Kidd,V.J.
  TITLE     CDK11 complexes promote pre-mRNA splicing
  JOURNAL   J Biol Chem 278 (10), 8623-8629 (2003)
   PUBMED   12501247
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Redon,R., Hussenet,T., Bour,G., Caulee,K., Jost,B., Muller,D.,
            Abecassis,J. and du Manoir,S.
  TITLE     Amplicon mapping and transcriptional analysis pinpoint cyclin L as
            a candidate oncogene in head and neck cancer
  JOURNAL   Cancer Res 62 (21), 6211-6217 (2002)
   PUBMED   12414649
REFERENCE   8  (residues 1 to 428)
  AUTHORS   Dickinson,L.A., Edgar,A.J., Ehley,J. and Gottesfeld,J.M.
  TITLE     Cyclin L is an RS domain protein involved in pre-mRNA splicing
  JOURNAL   J Biol Chem 277 (28), 25465-25473 (2002)
   PUBMED   11980906
  REMARK    GeneRIF: role in pre-mRNA splicing
            GeneRIF: Cyclin L has been shown to associate with the PITSLRE
            kinase and is involved in pre-mRNA processing.
REFERENCE   9  (residues 1 to 428)
  AUTHORS   Berke,J.D., Sgambato,V., Zhu,P.P., Lavoie,B., Vincent,M., Krause,M.
            and Hyman,S.E.
  TITLE     Dopamine and glutamate induce distinct striatal splice forms of
            Ania-6, an RNA polymerase II-associated cyclin
  JOURNAL   Neuron 32 (2), 277-287 (2001)
   PUBMED   11683997
REFERENCE   10 (residues 1 to 428)
  AUTHORS   Bunnell,B.A., Heath,L.S., Adams,D.E., Lahti,J.M. and Kidd,V.J.
  TITLE     Increased expression of a 58-kDa protein kinase leads to changes in
            the CHO cell cycle
  JOURNAL   Proc Natl Acad Sci U S A 87 (19), 7467-7471 (1990)
   PUBMED   2217177
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1991 Mar 15;88(6):2612]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104411.5.
            
            On Apr 28, 2015 this sequence version replaced XP_005247704.1.
            
            Transcript Variant: This variant (2) lacks a 3' exon and includes
            an alternate 3' terminal exon, compared to variant 1. It encodes
            isoform 2 which is shorter and has a distinct C-terminus, compared
            to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK122738.1, SRR14038195.2087746.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.31"
     Protein         1..428
                     /product="cyclin-L1 isoform 2"
                     /note="cyclin L ania-6a; cyclin L gamma; cyclin-L"
                     /calculated_mol_wt=47658
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UK58.1)"
     Region          40..195
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cl40454"
                     /db_xref="CDD:477360"
     Region          88..190
                     /region_name="Cyclin-like 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UK58.1)"
     Region          199..321
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cl40454"
                     /db_xref="CDD:477360"
     Region          203..287
                     /region_name="Cyclin-like 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UK58.1)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UK58.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q9UK58.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UK58.1)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UK58.1)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UK58.1)"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UK58.1)"
     CDS             1..428
                     /gene="CCNL1"
                     /gene_synonym="ania-6a; ANIA6A; BM-001; PRO1073"
                     /coded_by="NM_001308185.2:54..1340"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS77847.1"
                     /db_xref="GeneID:57018"
                     /db_xref="HGNC:HGNC:20569"
                     /db_xref="MIM:613384"
ORIGIN      
        1 masgphstat aaaaassaap saggsssgtt tttttttggi ligdrlysev sltidhslip
       61 eerlsptpsm qdgldlpset dlrilgceli qaagillrlp qvamatgqvl fhrffysksf
      121 vkhsfeivam acinlaskie eaprrirdvi nvfhhlrqlr gkrtpsplil dqnyintknq
      181 vikaerrvlk elgfcvhvkh phkiivmylq vlecernqtl vqtawnymnd slrtnvfvrf
      241 qpetiacaci ylaaralqip lptrphwfll fgtteeeiqe icietlrlyt rkkpnyelle
      301 kevekrkval qeaklkakgl npdgtpalst lggfspaskp ssprevkaee kspisinvkt
      361 vkkepedrqq askspyngvr kdskrsrnsr sasrsrsrtr srsrshtprr qdevllrcpg
      421 rsrtpglk
//
LOCUS       NP_775949                845 aa            linear   PRI 21-NOV-2025
DEFINITION  TRPM8 channel-associated factor 2 isoform A [Homo sapiens].
ACCESSION   NP_775949 NP_001352359 XP_947189 XP_950789
VERSION     NP_775949.2
DBSOURCE    REFSEQ: accession NM_173678.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 845)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 845)
  AUTHORS   Yun,D., Liang,J., Wang,X., Fan,J., Wang,X., Li,J., Ren,X., Liu,J.,
            Ren,X., Zhang,H., Shang,G., Jin,W., Chen,L., Li,T., Zhang,C., Yu,S.
            and Yang,X.
  TITLE     TCAF2 drives glioma cellular migratory/invasion properties through
            STAT3 signaling
  JOURNAL   Mol Cell Biochem 479 (7), 1801-1815 (2024)
   PUBMED   38019450
  REMARK    GeneRIF: TCAF2 drives glioma cellular migratory/invasion properties
            through STAT3 signaling.
REFERENCE   3  (residues 1 to 845)
  AUTHORS   Li,Y., Li,J., Chen,H., Lu,B., Lu,F., Chen,H., Liu,H. and Qian,C.
  TITLE     TCAF2 is associated with the immune microenvironment, promotes
            pathogenesis, and impairs prognosis in glioma
  JOURNAL   Gene 883, 147667 (2023)
   PUBMED   37506986
  REMARK    GeneRIF: TCAF2 is associated with the immune microenvironment,
            promotes pathogenesis, and impairs prognosis in glioma.
REFERENCE   4  (residues 1 to 845)
  AUTHORS   Li,X., Qi,Q., Li,Y., Miao,Q., Yin,W., Pan,J., Zhao,Z., Chen,X.,
            Yang,F., Zhou,X., Huang,M., Wang,C., Deng,L., Huang,D., Qi,M.,
            Fan,S., Zhang,Y., Qiu,S., Deng,W., Liu,T., Chen,M., Ye,W. and
            Zhang,D.
  TITLE     TCAF2 in Pericytes Promotes Colorectal Cancer Liver Metastasis via
            Inhibiting Cold-Sensing TRPM8 Channel
  JOURNAL   Adv Sci (Weinh) 10 (30), e2302717 (2023)
   PUBMED   37635201
  REMARK    GeneRIF: TCAF2 in Pericytes Promotes Colorectal Cancer Liver
            Metastasis via Inhibiting Cold-Sensing TRPM8 Channel.
REFERENCE   5  (residues 1 to 845)
  AUTHORS   Hsieh,P., Dang,V., Vollger,M.R., Mao,Y., Huang,T.H., Dishuck,P.C.,
            Baker,C., Cantsilieris,S., Lewis,A.P., Munson,K.M., Sorensen,M.,
            Welch,A.E., Underwood,J.G. and Eichler,E.E.
  TITLE     Evidence for opposing selective forces operating on human-specific
            duplicated TCAF genes in Neanderthals and humans
  JOURNAL   Nat Commun 12 (1), 5118 (2021)
   PUBMED   34433829
  REMARK    GeneRIF: Evidence for opposing selective forces operating on
            human-specific duplicated TCAF genes in Neanderthals and humans.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 845)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 845)
  AUTHORS   Gkika,D., Lemonnier,L., Shapovalov,G., Gordienko,D., Poux,C.,
            Bernardini,M., Bokhobza,A., Bidaux,G., Degerny,C., Verreman,K.,
            Guarmit,B., Benahmed,M., de Launoit,Y., Bindels,R.J., Fiorio Pla,A.
            and Prevarskaya,N.
  TITLE     TRP channel-associated factors are a novel protein family that
            regulates TRPM8 trafficking and activity
  JOURNAL   J Cell Biol 208 (1), 89-107 (2015)
   PUBMED   25559186
  REMARK    GeneRIF: Report novel TRP channel-associated factors that modulate
            TRPM8 activity.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC113530.1, AC106862.3 and AL832734.1.
            
            On or before Apr 25, 2025 this sequence version replaced
            NP_001352359.1, NP_775949.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because transcript sequence consistent with
            the reference genome assembly was not available for the full extent
            of the RefSeq transcript. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410571.152360.1, BC113530.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..845
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q35"
     Protein         1..845
                     /product="TRPM8 channel-associated factor 2 isoform A"
                     /note="family with sequence similarity 139, member A;
                     protein FAM115C; family with sequence similarity 115,
                     member C; TRP channel-associated factor 2"
                     /calculated_mol_wt=91877
     Region          522..632
                     /region_name="M60-like_N"
                     /note="N-terminal domain of M60-like peptidases;
                     pfam17291"
                     /db_xref="CDD:435844"
     Region          633..>835
                     /region_name="Peptidase_M60"
                     /note="Peptidase M60, enhancin and enhancin-like;
                     pfam13402"
                     /db_xref="CDD:433178"
     CDS             1..845
                     /gene="TCAF2"
                     /gene_synonym="FAM115C; FAM139A; GATD9; GATD9B"
                     /coded_by="NM_173678.3:52..2589"
                     /note="isoform A is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS34769.1"
                     /db_xref="GeneID:285966"
                     /db_xref="HGNC:HGNC:26878"
                     /db_xref="MIM:616252"
ORIGIN      
        1 matiaaaafe almdgvtcwd vprgpipsel lligeaafpv mvndkgqvli aassygrgrl
       61 vvvshegyls htglapflln avswlcpcpg apvgvhpsla plvnilqdag leaqvkpepg
      121 eplgvycina yndtltatli qfvkhgggll iggqawywas qhgpdkvlsr fpgnkvtsva
      181 gvyftdtygd rdrfkvskkv pkiplhvryg edvrqdqqql legiseldir tggvpsqllv
      241 hgalafplgl daslncflaa ahygrgrvvl aahecllcap kmgpfllnav rwlargqtgk
      301 vgvntnlkdl cpllsehglq cslephlnsd lcvycckays dkeakqlqef vaegggllig
      361 gqawwwasqn pghcplagfp gniilncfgl silpqtlkag cfpvptpemr syhfrkalsq
      421 fqailnheng nleksclakl rvdgaaflqi paegvpayis lhrllrkmlr gsglpavsre
      481 npvasdsyea avlslatgla hsgtdcsqla qglgtwtcss slypskhpit veinginpgn
      541 ndcwvstgly llegqnaevs lseaaasagl rvqigchtdd ltkarklsra pvvthqcwmd
      601 rtersvsclw ggllyvivpk gsqlgpvpvt irgavpapyy klgktsleew krqmqenlap
      661 wgelatdnii ltvpttnlqa lkdpepvlrl wdemmqavar laaepfpfrr perivadvqi
      721 sagwmhsgyp imchlesvke iinemdmrsr gvwgpihelg hnqqrhgwef pphtteatcn
      781 lwsvyvhetv lgipraqahe alsppererr ikahlgkgap lcdwnvwtal etylqvlsrn
      841 sgrrg
//
LOCUS       NP_001378831            1622 aa            linear   PRI 21-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4 gamma 3 isoform 11 [Homo
            sapiens].
ACCESSION   NP_001378831
VERSION     NP_001378831.1
DBSOURCE    REFSEQ: accession NM_001391902.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1622)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1622)
  AUTHORS   Kang,J.Y., Wen,Z., Pan,D., Zhang,Y., Li,Q., Zhong,A., Yu,X.,
            Wu,Y.C., Chen,Y., Zhang,X., Kou,P.C., Geng,J., Wang,Y.Y., Hua,M.M.,
            Zong,R., Li,B., Shi,H.J., Li,D., Fu,X.D., Li,J., Nelson,D.L.,
            Guo,X., Zhou,Y., Gou,L.T., Huang,Y. and Liu,M.F.
  TITLE     LLPS of FXR1 drives spermiogenesis by activating translation of
            stored mRNAs
  JOURNAL   Science 377 (6607), eabj6647 (2022)
   PUBMED   35951695
REFERENCE   3  (residues 1 to 1622)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1622)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 1622)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1622)
  AUTHORS   Waskiewicz,A.J., Johnson,J.C., Penn,B., Mahalingam,M., Kimball,S.R.
            and Cooper,J.A.
  TITLE     Phosphorylation of the cap-binding protein eukaryotic translation
            initiation factor 4E by protein kinase Mnk1 in vivo
  JOURNAL   Mol Cell Biol 19 (3), 1871-1880 (1999)
   PUBMED   10022874
REFERENCE   7  (residues 1 to 1622)
  AUTHORS   Pyronnet,S., Imataka,H., Gingras,A.C., Fukunaga,R., Hunter,T. and
            Sonenberg,N.
  TITLE     Human eukaryotic translation initiation factor 4G (eIF4G) recruits
            mnk1 to phosphorylate eIF4E
  JOURNAL   EMBO J 18 (1), 270-279 (1999)
   PUBMED   9878069
REFERENCE   8  (residues 1 to 1622)
  AUTHORS   Gingras,A.C., Raught,B. and Sonenberg,N.
  TITLE     eIF4 initiation factors: effectors of mRNA recruitment to ribosomes
            and regulators of translation
  JOURNAL   Annu Rev Biochem 68, 913-963 (1999)
   PUBMED   10872469
  REMARK    Review article
REFERENCE   9  (residues 1 to 1622)
  AUTHORS   Imataka,H., Gradi,A. and Sonenberg,N.
  TITLE     A newly identified N-terminal amino acid sequence of human eIF4G
            binds poly(A)-binding protein and functions in poly(A)-dependent
            translation
  JOURNAL   EMBO J 17 (24), 7480-7489 (1998)
   PUBMED   9857202
REFERENCE   10 (residues 1 to 1622)
  AUTHORS   Gradi,A., Imataka,H., Svitkin,Y.V., Rom,E., Raught,B., Morino,S.
            and Sonenberg,N.
  TITLE     A novel functional human eukaryotic translation initiation factor
            4G
  JOURNAL   Mol Cell Biol 18 (1), 334-342 (1998)
   PUBMED   9418880
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031005.2, AL627311.16,
            AL358392.19 and AL606477.11.
            
            Summary: The protein encoded by this gene is thought to be part of
            the eIF4F protein complex, which is involved in mRNA cap
            recognition and transport of mRNAs to the ribosome. Interestingly,
            a microRNA (miR-520c-3p) has been found that negatively regulates
            synthesis of the encoded protein, and this leads to a global
            decrease in protein translation and cell proliferation. Therefore,
            this protein is a key component of the anti-tumor activity of
            miR-520c-3p. [provided by RefSeq, May 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1324705.1,
                                           SRR14038191.2035003.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1622
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     Protein         1..1622
                     /product="eukaryotic translation initiation factor 4 gamma
                     3 isoform 11"
                     /note="eIF-4-gamma 3; eIF-4-gamma II"
                     /calculated_mol_wt=180905
     Region          <58..>333
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     Region          792..1020
                     /region_name="MIF4G"
                     /note="MIF4G domain; pfam02854"
                     /db_xref="CDD:397130"
     Region          1259..1371
                     /region_name="MA3"
                     /note="MA3 domain; pfam02847"
                     /db_xref="CDD:397128"
     Region          1465..1593
                     /region_name="W2_eIF4G1_like"
                     /note="C-terminal W2 domain of eukaryotic translation
                     initiation factor 4 gamma 1 and similar proteins; cd11559"
                     /db_xref="CDD:211397"
     Region          <1572..1618
                     /region_name="W2"
                     /note="C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon;
                     cl17013"
                     /db_xref="CDD:473053"
     CDS             1..1622
                     /gene="EIF4G3"
                     /gene_synonym="eIF-4G 3; eIF4G 3; eIF4GII"
                     /coded_by="NM_001391902.1:632..5500"
                     /note="isoform 11 is encoded by transcript variant 15"
                     /db_xref="GeneID:8672"
                     /db_xref="HGNC:HGNC:3298"
                     /db_xref="MIM:603929"
ORIGIN      
        1 mnsqpqtrsp psrtvpihct dnwkrrkvle qtpvyrslag rgwikyciff qrpqiqppra
       61 tipnsspsir pgaqtptavy qanqhimmvn hlpmpypvpq gpqycipqyr hsgppyvgpp
      121 qqypvqppgp gpfypgpgpg dfpnaygtpf ypsqpvyqsa piivptqqqp ppakrekkti
      181 rirdpnqggk diteeimsgg gsrnptppig rptstptppq lpsqvpehsp vvygtvesah
      241 laastpvtaa sdqkqeekpk pdpvlkspsp vlrlvlsgek keqegqtset taivsiaelp
      301 lppspttvss varstiaapt ssalssqpif ttaiddrcel sspredtipi psltsctets
      361 dplptnendd dickkpcsva pndiplvsst nlineingvs eklsatesiv eivkqevlpl
      421 tleleilenp peemklecip apitpstvps fpptpptppa spphtpvivp aaattvssps
      481 aaitvqrvle edesirtcls edakeiqnki eveadgqtee ildsqnlnsr rspvpaqiai
      541 tvpktwkkpk drtrtteeml eaelelkaee elsidkvles eqdkmsqgfh perdpsdlkk
      601 vkaveengee aepvrngaes vsegegidan sgstdssgdg vtfpfkpesw kptdtegkkq
      661 ydreflldfq fmpaciqkpe glppisdvvl dkinqpklpm rtldprilpr gpdftpafad
      721 fgrqtpggrg vpllnvgsrr sqpgqrrepr kiitvsvked vhlkkaenaw kpsqkrdsqa
      781 ddpeniktqe lfrkvrsiln kltpqmfnql mkqvsgltvd teerlkgvid lvfekaidep
      841 sfsvayanmc rclvtlkvpm adkpgntvnf rklllnrcqk efekdkaddd vfekkqkele
      901 aasapeertr lhdeleeakd karrrsigni kfigelfklk mlteaimhdc vvkllknhde
      961 esleclcrll ttigkdldfe kakprmdqyf nqmekivker ktssrirfml qdvidlrlcn
     1021 wvsrradqgp ktieqihkea kieeqeeqrk vqqlmtkekr rpgvqrvdeg gwntvqgakn
     1081 srvldpskfl kitkptidek iqlvpkaqlg swgkgssgga kasetdalrs sasslnrfsa
     1141 lqppapsgst pstpvefdsr rtltsrgsmg rekndkplps atarpntfmr ggsskdlldn
     1201 qsqeeqrrem letvkqltgg vdvernstea ernktresak peisamsahd kaalseeele
     1261 rksksiidef lhindfkeam qcveelnaqg llhvfvrvgv estlersqit rdhmgqllyq
     1321 lvqseklskq dffkgfsetl eladdmaidi phiwlylael vtpmlkeggi smreltiefs
     1381 kpllpvgrag vllseilhll ckqmshkkvg alwreadlsw kdflpegedv hnflleqkld
     1441 fiesdspcss ealskkelsa eelykrlekl iiedkandeq ifdwveanld eiqmssptfl
     1501 ralmtavcka aiiadsstfr vdtavikqrv pillkyldsd tekelqalya lqasivkldq
     1561 panllrmffd clydeevise dafykwessk dpaeqngkgv alksvtafft wlreaeeese
     1621 dn
//
LOCUS       NP_036377                536 aa            linear   PRI 21-NOV-2025
DEFINITION  SNW domain-containing protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_036377
VERSION     NP_036377.1
DBSOURCE    REFSEQ: accession NM_012245.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Leong,G.M., Subramaniam,N., Figueroa,J., Flanagan,J.L.,
            Hayman,M.J., Eisman,J.A. and Kouzmenko,A.P.
  TITLE     Ski-interacting protein interacts with Smad proteins to augment
            transforming growth factor-beta-dependent transcription
  JOURNAL   J Biol Chem 276 (21), 18243-18248 (2001)
   PUBMED   11278756
REFERENCE   7  (residues 1 to 536)
  AUTHORS   Zhou,S., Fujimuro,M., Hsieh,J.J., Chen,L., Miyamoto,A.,
            Weinmaster,G. and Hayward,S.D.
  TITLE     SKIP, a CBF1-associated protein, interacts with the ankyrin repeat
            domain of NotchIC To facilitate NotchIC function
  JOURNAL   Mol Cell Biol 20 (7), 2400-2410 (2000)
   PUBMED   10713164
REFERENCE   8  (residues 1 to 536)
  AUTHORS   Zhou,S., Fujimuro,M., Hsieh,J.J., Chen,L. and Hayward,S.D.
  TITLE     A role for SKIP in EBNA2 activation of CBF1-repressed promoters
  JOURNAL   J Virol 74 (4), 1939-1947 (2000)
   PUBMED   10644367
REFERENCE   9  (residues 1 to 536)
  AUTHORS   Baudino,T.A., Kraichely,D.M., Jefcoat,S.C. Jr., Winchester,S.K.,
            Partridge,N.C. and MacDonald,P.N.
  TITLE     Isolation and characterization of a novel coactivator protein,
            NCoA-62, involved in vitamin D-mediated transcription
  JOURNAL   J Biol Chem 273 (26), 16434-16441 (1998)
   PUBMED   9632709
REFERENCE   10 (residues 1 to 536)
  AUTHORS   Dahl,R., Wani,B. and Hayman,M.J.
  TITLE     The Ski oncoprotein interacts with Skip, the human homolog of
            Drosophila Bx42
  JOURNAL   Oncogene 16 (12), 1579-1586 (1998)
   PUBMED   9569025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008372.6.
            
            Summary: This gene, a member of the SNW gene family, encodes a
            coactivator that enhances transcription from some Pol II promoters.
            This coactivator can bind to the ligand-binding domain of the
            vitamin D receptor and to retinoid receptors to enhance vitamin D-,
            retinoic acid-, estrogen-, and glucocorticoid-mediated gene
            expression. It can also function as a splicing factor by
            interacting with poly(A)-binding protein 2 to directly control the
            expression of muscle-specific genes at the transcriptional level.
            Finally, the protein may be involved in oncogenesis since it
            interacts with a region of SKI oncoproteins that is required for
            transforming activity. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) differs in the 3' UTR and has
            multiple coding region differences, compared to variant 1, one of
            which results in a frameshift. The resulting protein (isoform 2)
            has a distinct C-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF045184.1, U51432.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261531.12/ ENSP00000261531.8
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..536
                     /product="SNW domain-containing protein 1 isoform 2"
                     /note="SKI interacting protein; nuclear receptor
                     coactivator, 62-kD; homolog of Drosophila BX42; nuclear
                     protein SkiP; SNW domain-containing protein 1; nuclear
                     receptor coactivator NCoA-62; ski-interacting protein"
                     /calculated_mol_wt=61364
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13573.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q13573.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13573.1)"
     Region          59..79
                     /region_name="Interaction with PPIL1.
                     /evidence=ECO:0000269|PubMed:16595688"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13573.1)"
     Region          174..339
                     /region_name="SNW"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13573.1)"
     Region          178..334
                     /region_name="SKIP_SNW"
                     /note="SKIP/SNW domain; pfam02731"
                     /db_xref="CDD:460666"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13573.1)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13573.1)"
     Region          209..233
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13573.1)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q13573.1)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13573.1)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13573.1)"
     Region          311..386
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13573.1)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13573.1)"
     Region          470..536
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13573.1)"
     Site            479
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13573.1)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13573.1)"
     CDS             1..536
                     /gene="SNW1"
                     /gene_synonym="Bx42; FUN20; NCOA-62; Prp45; PRPF45; SKIIP;
                     SKIP; SKIP1"
                     /coded_by="NM_012245.3:30..1640"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9867.1"
                     /db_xref="GeneID:22938"
                     /db_xref="HGNC:HGNC:16696"
                     /db_xref="MIM:603055"
ORIGIN      
        1 maltsflpap tqlsqdqlea eekarsqrsr qtslvssrre pppygyrkgw iprlledfgd
       61 ggafpeihva qypldmgrkk kmsnalaiqv dsegkikyda iarqgqskdk viyskytdlv
      121 pkevmnaddp dlqrpdeeai keitektrva leksvsqkva aampvraadk lapaqyiryt
      181 psqqgvafns gakqrvirmv emqkdpmepp rfkinkkipr gppsppapvm hspsrkmtvk
      241 eqqewkippc isnwknakgy tipldkrlaa dgrglqtvhi nenfaklaea lyiadrkare
      301 avemraqver kmaqkekekh eeklremaqk arerragikt hvekedgear erdeirhdrr
      361 kerqhdrnls raapdkrskl qrnenrdise vialgvpnpr tsnevqydqr lfnqskgmds
      421 gfaggedeiy nvydqawrgg kdmaqsiyrp sknldkdmyg ddleariktn rfvpdkefsg
      481 sdrrqrgreg pvqfeedpfg ldkfleeakq hggskrpsds srpkeheheg kkrrke
//
LOCUS       NP_001381776             596 aa            linear   PRI 21-NOV-2025
DEFINITION  kinesin light chain 1 isoform 19 [Homo sapiens].
ACCESSION   NP_001381776
VERSION     NP_001381776.1
DBSOURCE    REFSEQ: accession NM_001394847.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Kikuchi,M., Viet,J., Nagata,K., Sato,M., David,G., Audic,Y.,
            Silverman,M.A., Yamamoto,M., Akatsu,H., Hashizume,Y., Takeda,S.,
            Akamine,S., Miyamoto,T., Uozumi,R., Gotoh,S., Mori,K., Ikeda,M.,
            Paillard,L. and Morihara,T.
  TITLE     Gene-gene functional relationships in Alzheimer's disease: CELF1
            regulates KLC1 alternative splicing
  JOURNAL   Biochem Biophys Res Commun 721, 150025 (2024)
   PUBMED   38768546
  REMARK    GeneRIF: Gene-gene functional relationships in Alzheimer's disease:
            CELF1 regulates KLC1 alternative splicing.
REFERENCE   4  (residues 1 to 596)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 596)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   6  (residues 1 to 596)
  AUTHORS   Gyoeva,F.K., Bybikova,E.M. and Minin,A.A.
  TITLE     An isoform of kinesin light chain specific for the Golgi complex
  JOURNAL   J Cell Sci 113 (Pt 11), 2047-2054 (2000)
   PUBMED   10806115
REFERENCE   7  (residues 1 to 596)
  AUTHORS   Khodjakov,A., Lizunova,E.M., Minin,A.A., Koonce,M.P. and
            Gyoeva,F.K.
  TITLE     A specific light chain of kinesin associates with mitochondria in
            cultured cells
  JOURNAL   Mol Biol Cell 9 (2), 333-343 (1998)
   PUBMED   9450959
REFERENCE   8  (residues 1 to 596)
  AUTHORS   Chernajovsky,Y., Brown,A. and Clark,J.
  TITLE     Human kinesin light (beta) chain gene: DNA sequence and functional
            characterization of its promoter and first exon
  JOURNAL   DNA Cell Biol 15 (11), 965-974 (1996)
   PUBMED   8945637
REFERENCE   9  (residues 1 to 596)
  AUTHORS   Goedert,M., Marsh,S. and Carter,N.
  TITLE     Localization of the human kinesin light chain gene (KNS2) to
            chromosome 14q32.3 by fluorescence in situ hybridization
  JOURNAL   Genomics 32 (1), 173-175 (1996)
   PUBMED   8786116
REFERENCE   10 (residues 1 to 596)
  AUTHORS   Cabeza-Arvelaiz,Y., Shih,L.C., Hardman,N., Asselbergs,F., Bilbe,G.,
            Schmitz,A., White,B., Siciliano,M.J. and Lachman,L.B.
  TITLE     Cloning and genetic characterization of the human kinesin
            light-chain (KLC) gene
  JOURNAL   DNA Cell Biol 12 (10), 881-892 (1993)
   PUBMED   8274221
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139300.6 and AL049840.8.
            
            Summary: Conventional kinesin is a tetrameric molecule composed of
            two heavy chains and two light chains, and transports various
            cargos along microtubules toward their plus ends. The heavy chains
            provide the motor activity, while the light chains bind to various
            cargos. This gene encodes a member of the kinesin light chain
            family. It associates with kinesin heavy chain through an
            N-terminal domain, and six tetratricopeptide repeat (TPR) motifs
            are thought to be involved in binding of cargos such as vesicles,
            mitochondria, and the Golgi complex. Thus, kinesin light chains
            function as adapter molecules and not motors per se. Although
            previously named 'kinesin 2', this gene is not a member of the
            kinesin-2 / kinesin heavy chain subfamily of kinesin motor
            proteins. Extensive alternative splicing produces isoforms with
            different C-termini that are proposed to bind to different cargos;
            however, the full-length nature and/or biological validity of most
            of these variants have not been determined. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3922156.1,
                                           SRR14038195.1653260.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..596
                     /product="kinesin light chain 1 isoform 19"
                     /EC_number="2.7.1.21"
                     /note="kinesin 2 60/70kDa; medulloblastoma antigen
                     MU-MB-2.50"
                     /calculated_mol_wt=67589
     Region          35..>149
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          210..435
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          214..241
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          255..283
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          297..325
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(298,301..302,305..306,308,340,343..344,347..348,
                     350..351,382,385..386,389..390,393)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          338..368
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          381..408
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..596
                     /gene="KLC1"
                     /gene_synonym="KLC; KNS2; KNS2A"
                     /coded_by="NM_001394847.1:286..2076"
                     /note="isoform 19 is encoded by transcript variant 19"
                     /db_xref="GeneID:3831"
                     /db_xref="HGNC:HGNC:6387"
                     /db_xref="MIM:600025"
ORIGIN      
        1 mydnmstmvy ikedkleklt qdeiisktkq viqglealkn ehnsilqsll etlkclkkdd
       61 esnlveeksn mirkslemle lglseaqvmm alsnhlnave sekqklraqv rrlcqenqwl
      121 rdelantqqk lqkseqsvaq leeekkhlef mnqlkkyddd ispsedkdtd stkeplddlf
      181 pndeddpgqg iqqqhssaaa aaqqggyeip arlrtlhnlv iqyasqgrye vavplckqal
      241 edlektsghd hpdvatmlni lalvyrdqnk ykdaanllnd alairektlg kdhpavaatl
      301 nnlavlygkr gkykeaeplc kraleirekv lgkdhpdvak qlnnlallcq nqgkyeevey
      361 yyqraleiyq tklgpddpnv aktknnlasc ylkqgkfkqa etlykeiltr aherefgsvd
      421 denkpiwmha eereeckgkq kdgtsfgeyg gwykackvds ptvtttlknl galyrrqgkf
      481 eaaetleeaa mrsrkqgldn vhkqrvaevl ndpenmekrr sreslnvdvv kyesgpdgge
      541 edgtgslkrs gsfsklrasi rrsseklvrk lkggssrese pknpgneiiv wptrel
//
LOCUS       NP_001358423             398 aa            linear   PRI 21-NOV-2025
DEFINITION  LIM and senescent cell antigen-like-containing domain protein 1
            isoform f [Homo sapiens].
ACCESSION   NP_001358423
VERSION     NP_001358423.1
DBSOURCE    REFSEQ: accession NM_001371494.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Caliskan,Y., Ozluk,Y., Kurashima,K., Mirioglu,S., Dirim,A.B.,
            Hurdogan,O., Oto,O.A., Syn,M., Nazzal,M., Jain,A., Edwards,J.,
            Yazici,H. and Lentine,K.L.
  TITLE     LIM Zinc Finger Domain Containing 1 Risk Genotype of Recipient Is
            Associated with Renal Tubular Inflammation in Kidney
            Transplantation
  JOURNAL   Genes (Basel) 15 (6), 773 (2024)
   PUBMED   38927709
  REMARK    GeneRIF: LIM Zinc Finger Domain Containing 1 Risk Genotype of
            Recipient Is Associated with Renal Tubular Inflammation in Kidney
            Transplantation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Li,Y., Wang,S., Li,G., Gao,C., Cui,Z., Cong,M., Hu,J., Zhang,M.,
            Jin,X., Sun,H. and Kong,D.
  TITLE     The RNA-binding protein RBMS3 inhibits the progression of colon
            cancer by regulating the stability of LIMS1 mRNA
  JOURNAL   Cancer Med 13 (7), e7129 (2024)
   PUBMED   38618967
  REMARK    GeneRIF: The RNA-binding protein RBMS3 inhibits the progression of
            colon cancer by regulating the stability of LIMS1 mRNA.
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Gorska,A. and Mazur,A.J.
  TITLE     Integrin-linked kinase (ILK): the known vs. the unknown and
            perspectives
  JOURNAL   Cell Mol Life Sci 79 (2), 100 (2022)
   PUBMED   35089438
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Gubin,A.N., Njoroge,J.M., Bouffard,G.G. and Miller,J.L.
  TITLE     Gene expression in proliferating human erythroid cells
  JOURNAL   Genomics 59 (2), 168-177 (1999)
   PUBMED   10409428
REFERENCE   8  (residues 1 to 398)
  AUTHORS   Tu,Y., Li,F., Goicoechea,S. and Wu,C.
  TITLE     The LIM-only protein PINCH directly interacts with integrin-linked
            kinase and is recruited to integrin-rich sites in spreading cells
  JOURNAL   Mol Cell Biol 19 (3), 2425-2434 (1999)
   PUBMED   10022929
REFERENCE   9  (residues 1 to 398)
  AUTHORS   Tu,Y., Li,F. and Wu,C.
  TITLE     Nck-2, a novel Src homology2/3-containing adaptor protein that
            interacts with the LIM-only protein PINCH and components of growth
            factor receptor kinase-signaling pathways
  JOURNAL   Mol Biol Cell 9 (12), 3367-3382 (1998)
   PUBMED   9843575
REFERENCE   10 (residues 1 to 398)
  AUTHORS   Rearden,A.
  TITLE     A new LIM protein containing an autoepitope homologous to
            'senescent cell antigen'
  JOURNAL   Biochem Biophys Res Commun 201 (3), 1124-1131 (1994)
   PUBMED   7517666
  REMARK    Erratum:[Biochem Biophys Res Commun 2001 Apr 13;282(4):1074]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010095.6.
            
            Summary: The protein encoded by this gene is an adaptor protein
            which contains five LIM domains, or double zinc fingers. The
            protein is likely involved in integrin signaling through its LIM
            domain-mediated interaction with integrin-linked kinase, found in
            focal adhesion plaques. It is also thought to act as a bridge
            linking integrin-linked kinase to NCK adaptor protein 2, which is
            involved in growth factor receptor kinase signaling pathways. Its
            localization to the periphery of spreading cells also suggests that
            this protein may play a role in integrin-mediated cell adhesion or
            spreading. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3509626.1,
                                           SRR5189655.76206.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q12.3"
     Protein         1..398
                     /product="LIM and senescent cell antigen-like-containing
                     domain protein 1 isoform f"
                     /note="LIM and senescent cell antigen-like-containing
                     domain protein 1; renal carcinoma antigen NY-REN-48; LIM
                     and senescent cell antigen-like domains 1; LIM-type zinc
                     finger domains 1; particularly interesting new Cys-His
                     protein 1"
                     /calculated_mol_wt=45663
     Region          72..130
                     /region_name="LIM1_PINCH"
                     /note="The first LIM domain of protein PINCH; cd09331"
                     /db_xref="CDD:188717"
     Site            order(72,75,94,97,100,103,121,124)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188717"
     Site            order(74..75,77,99,101..105,115..116,118,123..124,
                     126..130)
                     /site_type="other"
                     /note="ILK binding interface"
                     /db_xref="CDD:188717"
     Region          133..184
                     /region_name="LIM2_PINCH"
                     /note="The second LIM domain of protein PINCH; cd09332"
                     /db_xref="CDD:188718"
     Site            order(133,136,153,156,159,162,180,183)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188718"
     Region          197..247
                     /region_name="LIM3_PINCH"
                     /note="The third LIM domain of protein PINCH; cd09333"
                     /db_xref="CDD:188719"
     Site            order(197,200,217,220,223,226,243,246)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188719"
     Region          253..306
                     /region_name="LIM4_PINCH"
                     /note="The fourth LIM domain of protein PINCH; cd09334"
                     /db_xref="CDD:188720"
     Site            order(254,258..261)
                     /site_type="other"
                     /note="N(i)ck binding interface"
                     /db_xref="CDD:188720"
     Site            order(255,258,275,278,281,284,302,305)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188720"
     Region          314..367
                     /region_name="LIM5_PINCH"
                     /note="The fifth LIM domain of protein PINCH; cd09335"
                     /db_xref="CDD:188721"
     Site            order(314,317,334,337,340,343,362,365)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188721"
     CDS             1..398
                     /gene="LIMS1"
                     /gene_synonym="PINCH; PINCH-1; PINCH1"
                     /coded_by="NM_001371494.1:42..1238"
                     /note="isoform f is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS92833.1"
                     /db_xref="GeneID:3987"
                     /db_xref="HGNC:HGNC:6616"
                     /db_xref="MIM:602567"
ORIGIN      
        1 mafsgrarpc iipeneeipr aalntvhean gtederavsk lqrrhsdvkv ykefcdfyak
       61 fnmanalasa tcerckggfa paekivnsng elyheqcfvc aqcfqqfpeg lfyefegrky
      121 cehdfqmlfa pcchqcgefi igrvikamnn swhpecfrcd lcqevladig fvknagrhlc
      181 rpchnrekar glgkyicqkc haiideqpli fkndpyhpdh fncancgkel tadarelkge
      241 lyclpchdkm gvpicgacrr piegrvvnam gkqwhvehfv cakcekpflg hrhyerkgla
      301 ycethynqlf gdvcfhcnrv iegdvvsaln kawcvncfac stcntkltlk dkfveidlkp
      361 vckhcyekmp eefkrrlakr ereakdkdkq kkkkpvcl
//
LOCUS       NP_001350661             392 aa            linear   PRI 21-NOV-2025
DEFINITION  leucine-rich repeat-containing protein 49 isoform 5 [Homo sapiens].
ACCESSION   NP_001350661 XP_011520020
VERSION     NP_001350661.1
DBSOURCE    REFSEQ: accession NM_001363732.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Ruse,C.I., Chin,H.G. and Pradhan,S.
  TITLE     Polyglutamylation: biology and analysis
  JOURNAL   Amino Acids 54 (4), 529-542 (2022)
   PUBMED   35357568
  REMARK    Review article
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Wang,L., Paudyal,S.C., Kang,Y., Owa,M., Liang,F.X., Spektor,A.,
            Knaut,H., Sanchez,I. and Dynlacht,B.D.
  TITLE     Regulators of tubulin polyglutamylation control nuclear shape and
            cilium disassembly by balancing microtubule and actin assembly
  JOURNAL   Cell Res 32 (2), 190-209 (2022)
   PUBMED   34782749
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   4  (residues 1 to 392)
  AUTHORS   De Souza Santos,E., De Bessa,S.A., Netto,M.M. and Nagai,M.A.
  TITLE     Silencing of LRRC49 and THAP10 genes by bidirectional promoter
            hypermethylation is a frequent event in breast cancer
  JOURNAL   Int J Oncol 33 (1), 25-31 (2008)
   PUBMED   18575747
  REMARK    GeneRIF: transcripts of LRRC49/THAP10 bidirectional gene pair are
            co-regulated by estrogen and that hypermethylation of the
            bidirectional promoter region simultaneously silences both genes.
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Janke,C., Rogowski,K., Wloga,D., Regnard,C., Kajava,A.V.,
            Strub,J.M., Temurak,N., van Dijk,J., Boucher,D., van Dorsselaer,A.,
            Suryavanshi,S., Gaertig,J. and Edde,B.
  TITLE     Tubulin polyglutamylase enzymes are members of the TTL domain
            protein family
  JOURNAL   Science 308 (5729), 1758-1762 (2005)
   PUBMED   15890843
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Kitazawa,H., Iida,J., Uchida,A., Haino-Fukushima,K., Itoh,T.J.,
            Hotani,H., Ookata,K., Murofushi,H., Bulinski,J.C., Kishimoto,T. and
            Hisanaga,S.
  TITLE     Ser787 in the proline-rich region of human MAP4 is a critical
            phosphorylation site that reduces its activity to promote tubulin
            polymerization
  JOURNAL   Cell Struct Funct 25 (1), 33-39 (2000)
   PUBMED   10791892
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC090868.4, AC084703.7 and AC013752.10.
            
            On May 29, 2018 this sequence version replaced XP_011520020.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.236576.1,
                                           SRR1803617.274841.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2149178
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q23"
     Protein         1..392
                     /product="leucine-rich repeat-containing protein 49
                     isoform 5"
                     /note="leucine-rich repeat-containing protein 49; tubulin
                     polyglutamylase complex subunit 4; centriolar
                     satellite-associated tubulin polyglutamylation protein 2;
                     polyglutamylase subunit 4; centriolar satellite-associated
                     tubulin polyglutamylase complex regulator 2"
                     /calculated_mol_wt=45309
     CDS             1..392
                     /gene="LRRC49"
                     /gene_synonym="CSTPP2; PGs4"
                     /coded_by="NM_001363732.2:947..2125"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS86472.1"
                     /db_xref="GeneID:54839"
                     /db_xref="HGNC:HGNC:25965"
                     /db_xref="MIM:620497"
ORIGIN      
        1 mmqlrqldmk riteeerrma svlakkeeek kreshkqsll kekkrltinn varqwdlqqq
       61 rvaniatned rkdsdspqdp cqidgstlsa fpeetgplds glnnalqgls vidtylvevd
      121 gdtlslygsg alesldrnws vqtagmittv sftfiefdei vqvlpklkik fpnslhlkfk
      181 etnlvmlqqf nalaqlrrid qltidpqgnp vvnftlwkyy vlfrlshfsm qkingtevtq
      241 ndmimaerlf gilahvasse lpqyrlisil gdarkkqfry lleskgkkpg iineenndsk
      301 rlvgentnra tlnyttrdfy nekleeikek kkfcktyied lvkeateinm knealqklwp
      361 qmfielvrda vieirnknsy mklclqqitd qk
//
LOCUS       NP_001025484             463 aa            linear   PRI 21-NOV-2025
DEFINITION  ceramide kinase-like protein isoform 4 [Homo sapiens].
ACCESSION   NP_001025484
VERSION     NP_001025484.1
DBSOURCE    REFSEQ: accession NM_001030313.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Daich Varela,M., Duignan,E.S., De Silva,S.R., Ba-Abbad,R.,
            Fujinami-Yokokawa,Y., Leo,S., Fujinami,K., Mahroo,O.A.,
            Robson,A.G., Webster,A.R. and Michaelides,M.
  TITLE     CERKL-Associated Retinal Dystrophy: Genetics, Phenotype, and
            Natural History
  JOURNAL   Ophthalmol Retina 7 (10), 918-931 (2023)
   PUBMED   37331655
  REMARK    GeneRIF: CERKL-Associated Retinal Dystrophy: Genetics, Phenotype,
            and Natural History.
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Garcia-Arroyo,R., Marfany,G. and Mirra,S.
  TITLE     CERKL, a Retinal Dystrophy Gene, Regulates Mitochondrial Transport
            and Dynamics in Hippocampal Neurons
  JOURNAL   Int J Mol Sci 23 (19), 11593 (2022)
   PUBMED   36232896
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Downes,S.M., Nguyen,T., Tai,V., Broadgate,S., Shah,M.,
            Al-Khuzaei,S., MacLaren,R.E., Shanks,M., Clouston,P. and Halford,S.
  TITLE     Genetic and Clinical Findings in an Ethnically Diverse Cohort with
            Retinitis Pigmentosa Associated with Pathogenic Variants in CERKL
  JOURNAL   Genes (Basel) 11 (12), 1497 (2020)
   PUBMED   33322828
  REMARK    GeneRIF: Genetic and Clinical Findings in an Ethnically Diverse
            Cohort with Retinitis Pigmentosa Associated with Pathogenic
            Variants in CERKL.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 463)
  AUTHORS   Bornancin,F., Mechtcheriakova,D., Stora,S., Graf,C., Wlachos,A.,
            Devay,P., Urtz,N., Baumruker,T. and Billich,A.
  TITLE     Characterization of a ceramide kinase-like protein
  JOURNAL   Biochim Biophys Acta 1687 (1-3), 31-43 (2005)
   PUBMED   15708351
  REMARK    GeneRIF: Data suggest a functional link between CERKL, a new
            ceramide kinase homolog, and its nucleolar localization.
REFERENCE   7  (residues 1 to 463)
  AUTHORS   Tuson,M., Marfany,G. and Gonzalez-Duarte,R.
  TITLE     Mutation of CERKL, a novel human ceramide kinase gene, causes
            autosomal recessive retinitis pigmentosa (RP26)
  JOURNAL   Am J Hum Genet 74 (1), 128-138 (2004)
   PUBMED   14681825
  REMARK    GeneRIF: Novel mutation in CERKL which encompassed 13 exons is
            identified in retinitis pigmentosa
REFERENCE   8  (residues 1 to 463)
  AUTHORS   Sugiura,M., Kono,K., Liu,H., Shimizugawa,T., Minekura,H.,
            Spiegel,S. and Kohama,T.
  TITLE     Ceramide kinase, a novel lipid kinase. Molecular cloning and
            functional characterization
  JOURNAL   J Biol Chem 277 (26), 23294-23300 (2002)
   PUBMED   11956206
REFERENCE   9  (residues 1 to 463)
  AUTHORS   Bayes,M., Goldaracena,B., Martinez-Mir,A., Iragui-Madoz,M.I.,
            Solans,T., Chivelet,P., Bussaglia,E., Ramos-Arroyo,M.A., Baiget,M.,
            Vilageliu,L., Balcells,S., Gonzalez-Duarte,R. and Grinberg,D.
  TITLE     A new autosomal recessive retinitis pigmentosa locus maps on
            chromosome 2q31-q33
  JOURNAL   J Med Genet 35 (2), 141-145 (1998)
   PUBMED   9507394
REFERENCE   10 (residues 1 to 463)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK293844.1, AY690331.1,
            AC020595.7 and BM969366.1.
            
            Summary: This gene was initially identified as a locus (RP26)
            associated with an autosomal recessive form of retinitis pigmentosa
            (arRP) disease. This gene encodes a protein with ceramide
            kinase-like domains, however, the protein does not phosphorylate
            ceramide and its target substrate is currently unknown. This
            protein may be a negative regulator of apoptosis in photoreceptor
            cells. Mutations in this gene cause a form of retinitis pigmentosa
            characterized by autosomal recessive cone and rod dystrophy
            (arCRD). Alternative splicing of this gene results in multiple
            transcript variants encoding different isoforms and non-coding
            transcripts.[provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (4) lacks three alternate in-frame
            exons in the central coding region, compared to variant 2. The
            resulting isoform (4) lacks an internal segment, compared to
            isoform 2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.175254.1, HQ426675.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.3"
     Protein         1..463
                     /product="ceramide kinase-like protein isoform 4"
                     /note="ceramide kinase like"
                     /calculated_mol_wt=52315
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q49MI3.1)"
     Region          2..9
                     /region_name="Nuclear localization signal 1.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q49MI3.1)"
     Region          102..106
                     /region_name="Nuclear localization signal 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q49MI3.1)"
     Region          251..460
                     /region_name="CERK_C"
                     /note="Ceramide kinase C-terminal domain; pfam19280"
                     /db_xref="CDD:466025"
     CDS             1..463
                     /gene="CERKL"
                     /gene_synonym="RP26"
                     /coded_by="NM_001030313.3:100..1491"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS33341.1"
                     /db_xref="GeneID:375298"
                     /db_xref="HGNC:HGNC:21699"
                     /db_xref="MIM:608381"
ORIGIN      
        1 mpwrrrrnrv saleggreee appeaaavpp alltspqqte aaaerillrg ifeigrdscd
       61 vvlseralrw rpiqperpag dskydllcke efielkdifs vklkrrcsvk qqrsgtllgi
      121 tlficlkkeq nklknstldl inlsedhcdi wfrqfkkila gfpnrpkslk illnpqshkk
      181 eatqvyyekv epllklagik tdvtrstnvl ahslhgvphv itatlhiimg hvqlvdvctf
      241 stagkllrfg fsamfgfggr tlalaekyrw mspnqrrdfa vvkalaklka edceisflpf
      301 nssddvqerr aqgspksdcn dqwqmiqgqf lnvsimaipc lcsvaprgla pntrlnngsm
      361 aliiarntsr pefikhlkry asvknqfnfp fvetytveev kvhprnntgg ynpeeeedet
      421 asencfpwnv dgdlmevase vhirlhprli slyggsmeem ipk
//
LOCUS       NP_001092082             396 aa            linear   PRI 21-NOV-2025
DEFINITION  sialic acid-binding Ig-like lectin 14 precursor [Homo sapiens].
ACCESSION   NP_001092082
VERSION     NP_001092082.1
DBSOURCE    REFSEQ: accession NM_001098612.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Yu,Y., Zhang,Z., Dong,X., Yang,R., Duan,Z., Xiang,Z., Li,J., Li,G.,
            Yan,F., Xue,H., Jiao,D., Lu,J., Lu,H., Zhang,W., Wei,Y., Fan,S.,
            Li,J., Jia,J., Zhang,J., Ji,J., Liu,P., Lu,H., Zhao,H., Chen,S.,
            Wei,C., Chen,H. and Zhu,Z.
  TITLE     Pangenomic analysis of Chinese gastric cancer
  JOURNAL   Nat Commun 13 (1), 5412 (2022)
   PUBMED   36109518
  REMARK    GeneRIF: Genes ACOT1, GSTM1, SIGLEC14 and UGT2B17 are identified as
            highly absent genes in gastric cancer population.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Shaw,B.C., Katsumata,Y., Simpson,J.F., Fardo,D.W. and Estus,S.
  TITLE     Analysis of Genetic Variants Associated with Levels of Immune
            Modulating Proteins for Impact on Alzheimer's Disease Risk Reveal a
            Potential Role for SIGLEC14
  JOURNAL   Genes (Basel) 12 (7), 1008 (2021)
   PUBMED   34208838
  REMARK    GeneRIF: Analysis of Genetic Variants Associated with Levels of
            Immune Modulating Proteins for Impact on Alzheimer's Disease Risk
            Reveal a Potential Role for SIGLEC14.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Tsai,C.M., Riestra,A.M., Ali,S.R., Fong,J.J., Liu,J.Z., Hughes,G.,
            Varki,A. and Nizet,V.
  TITLE     Siglec-14 Enhances NLRP3-Inflammasome Activation in Macrophages
  JOURNAL   J Innate Immun 12 (4), 333-343 (2020)
   PUBMED   31805552
  REMARK    GeneRIF: Siglec-14 Enhances NLRP3-Inflammasome Activation in
            Macrophages.
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Huang,P.J., Low,P.Y., Wang,I., Hsu,S.D. and Angata,T.
  TITLE     Soluble Siglec-14 glycan-recognition protein is generated by
            alternative splicing and suppresses myeloid inflammatory responses
  JOURNAL   J Biol Chem 293 (51), 19645-19658 (2018)
   PUBMED   30377253
  REMARK    GeneRIF: soluble Siglec-14 suppresses pro-inflammatory responses
            triggered by membrane-bound Siglec-14
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Ali,S.R., Fong,J.J., Carlin,A.F., Busch,T.D., Linden,R., Angata,T.,
            Areschoug,T., Parast,M., Varki,N., Murray,J., Nizet,V. and Varki,A.
  TITLE     Siglec-5 and Siglec-14 are polymorphic paired receptors that
            modulate neutrophil and amnion signaling responses to group B
            Streptococcus
  JOURNAL   J Exp Med 211 (6), 1231-1242 (2014)
   PUBMED   24799499
  REMARK    GeneRIF: Data indicate that the Siglec-5/14 genotype influences
            neutrophil responses to group B Streptococcus.
REFERENCE   7  (residues 1 to 396)
  AUTHORS   Angata,T., Ishii,T., Motegi,T., Oka,R., Taylor,R.E., Soto,P.C.,
            Chang,Y.C., Secundino,I., Gao,C.X., Ohtsubo,K., Kitazume,S.,
            Nizet,V., Varki,A., Gemma,A., Kida,K. and Taniguchi,N.
  TITLE     Loss of Siglec-14 reduces the risk of chronic obstructive pulmonary
            disease exacerbation
  JOURNAL   Cell Mol Life Sci 70 (17), 3199-3210 (2013)
   PUBMED   23519826
  REMARK    GeneRIF: Siglec-14 and its downstream signaling pathway facilitate
            the 'infection-inflammation-exacerbation' axis of COPD disease
            progression
REFERENCE   8  (residues 1 to 396)
  AUTHORS   Yamanaka,M., Kato,Y., Angata,T. and Narimatsu,H.
  TITLE     Deletion polymorphism of SIGLEC14 and its functional implications
  JOURNAL   Glycobiology 19 (8), 841-846 (2009)
   PUBMED   19369701
  REMARK    GeneRIF: The presence of the 'SIGLEC14 null' allele in all human
            populations we tested implies an ancient origin, while its allelic
            frequency is higher in Asians compared with Africans and Europeans.
            Siglec-14 may play some role in bacterial infection.
REFERENCE   9  (residues 1 to 396)
  AUTHORS   Angata,T., Hayakawa,T., Yamanaka,M., Varki,A. and Nakamura,M.
  TITLE     Discovery of Siglec-14, a novel sialic acid receptor undergoing
            concerted evolution with Siglec-5 in primates
  JOURNAL   FASEB J 20 (12), 1964-1973 (2006)
   PUBMED   17012248
  REMARK    GeneRIF: Siglec-14 and Siglec-5 appear to be the first glycan
            binding paired receptors. Near-complete sequence identity of the
            amino-terminal part of human Siglec-14 and Siglec-5 indicates
            partial gene conversion between SIGLEC14 and SIGLEC5.
REFERENCE   10 (residues 1 to 396)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC018755.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY854038.1, AK298284.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360844.7/ ENSP00000354090.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..396
                     /product="sialic acid-binding Ig-like lectin 14 precursor"
                     /note="siglec-14"
                     /calculated_mol_wt=42224
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1764
     mat_peptide     17..396
                     /product="Sialic acid-binding Ig-like lectin 14.
                     /id=PRO_0000309314"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08ET2.1)"
                     /calculated_mol_wt=42224
     Region          21..140
                     /region_name="IgV_CD33"
                     /note="Immunoglobulin Variable (IgV) domain at the
                     N-terminus of CD33 and related Siglecs (sialic
                     acid-binding Ig-like lectins); cd05712"
                     /db_xref="CDD:409377"
     Region          21..45
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409377"
     Region          21..25
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409377"
     Region          28..32
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409377"
     Region          34..45
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409377"
     Region          46..55
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409377"
     Region          56..63
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409377"
     Region          56..63
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409377"
     Region          64..87
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409377"
     Region          74..77
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409377"
     Region          88..121
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409377"
     Region          89..93
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409377"
     Region          99..107
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409377"
     Region          114..122
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409377"
     Site            order(119,128..129)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409377"
     Region          122..126
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409377"
     Region          127..140
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409377"
     Region          127..140
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409377"
     Region          146..231
                     /region_name="IgC2_CD33_d2_like"
                     /note="Second immunoglobulin domain of Cluster of
                     Differentiation (CD) 33 and related Siglecs; member of the
                     C2-set of IgSF domains; cd20987"
                     /db_xref="CDD:409579"
     Region          146..150
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409579"
     Region          159..165
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409579"
     Region          177..182
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409579"
     Region          190..209
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08ET2.1)"
     Region          196..202
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409579"
     Region          209..216
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409579"
     Region          223..231
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409579"
     Site            231
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q08ET2.1)"
     Region          264..337
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          270..274
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409540"
     Region          283..287
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409540"
     Region          305..309
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409540"
     Region          316..321
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409540"
     Region          331..334
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409540"
     Site            359..381
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08ET2.1)"
     CDS             1..396
                     /gene="SIGLEC14"
                     /coded_by="NM_001098612.3:67..1257"
                     /db_xref="CCDS:CCDS42604.1"
                     /db_xref="GeneID:100049587"
                     /db_xref="HGNC:HGNC:32926"
                     /db_xref="MIM:618132"
ORIGIN      
        1 mlpllllpll wggslqekpv yelqvqksvt vqeglcvlvp csfsypwrsw ysspplyvyw
       61 frdgeipyya evvatnnpdr rvkpetqgrf rllgdvqkkn cslsigdarm edtgsyffrv
      121 ergrdvkysy qqnklnlevt aliekpdihf leplesgrpt rlscslpgsc eagppltfsw
      181 tgnalspldp ettrsseltl tprpedhgtn ltcqvkrqga qvttertvql nvsyapqnla
      241 isiffrngtg talrilsngm svpiqegqsl flactvdsnp paslswfreg kalnpsqtsm
      301 sgtlelpnig areggeftcr vqhplgsqhl sfilsvqrss sscicvtekq qgswplvltl
      361 irgalmgagf lltygltwiy ytrcggpqqs raerpg
//
LOCUS       NP_006297               1233 aa            linear   PRI 21-NOV-2025
DEFINITION  structural maintenance of chromosomes protein 1A isoform 1 [Homo
            sapiens].
ACCESSION   NP_006297
VERSION     NP_006297.2
DBSOURCE    REFSEQ: accession NM_006306.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1233)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1233)
  AUTHORS   Ibstedt,S., Piccinelli,P., Sydow,S., Koster,J. and Mertens,F.
  TITLE     Structural Variants in the SMC1A Gene Associated With Near-Haploidy
            in Undifferentiated Pleomorphic Sarcomas
  JOURNAL   Genes Chromosomes Cancer 63 (8), e23255 (2024)
   PUBMED   39149945
  REMARK    GeneRIF: Structural Variants in the SMC1A Gene Associated With
            Near-Haploidy in Undifferentiated Pleomorphic Sarcomas.
REFERENCE   3  (residues 1 to 1233)
  AUTHORS   Li,K., Dai,P., Li,J., Liu,L., Cheng,S., Fang,Q. and Wu,B.
  TITLE     AKT/FOXM1/STMN1 signaling pathway activation by SMC1A promotes
            tumor growth in breast cancer
  JOURNAL   J Gene Med 26 (1), e3661 (2024)
   PUBMED   38282144
  REMARK    GeneRIF: AKT/FOXM1/STMN1 signaling pathway activation by SMC1A
            promotes tumor growth in breast cancer.
REFERENCE   4  (residues 1 to 1233)
  AUTHORS   Liu,Y., Fang,X., Wang,Q., Xiao,D., Zhou,T., Kang,K., Peng,Z.,
            Ren,F. and Zhou,J.
  TITLE     SMC1A facilitates gastric cancer cell proliferation, migration, and
            invasion via promoting SNAIL activated EMT
  JOURNAL   BMC Gastroenterol 23 (1), 268 (2023)
   PUBMED   37537540
  REMARK    GeneRIF: SMC1A facilitates gastric cancer cell proliferation,
            migration, and invasion via promoting SNAIL activated EMT.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1233)
  AUTHORS   Chen,Y., Sharp,Z.D. and Lee,W.H.
  TITLE     HEC binds to the seventh regulatory subunit of the 26 S proteasome
            and modulates the proteolysis of mitotic cyclins
  JOURNAL   J Biol Chem 272 (38), 24081-24087 (1997)
   PUBMED   9295362
REFERENCE   6  (residues 1 to 1233)
  AUTHORS   Brown,C.J., Miller,A.P., Carrel,L., Rupert,J.L., Davies,K.E. and
            Willard,H.F.
  TITLE     The DXS423E gene in Xp11.21 escapes X chromosome inactivation
  JOURNAL   Hum Mol Genet 4 (2), 251-255 (1995)
   PUBMED   7757075
REFERENCE   7  (residues 1 to 1233)
  AUTHORS   Rocques,P.J., Clark,J., Ball,S., Crew,J., Gill,S.,
            Christodoulou,Z., Borts,R.H., Louis,E.J., Davies,K.E. and
            Cooper,C.S.
  TITLE     The human SB1.8 gene (DXS423E) encodes a putative chromosome
            segregation protein conserved in lower eukaryotes and prokaryotes
  JOURNAL   Hum Mol Genet 4 (2), 243-249 (1995)
   PUBMED   7757074
REFERENCE   8  (residues 1 to 1233)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
REFERENCE   9  (residues 1 to 1233)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   10 (residues 1 to 1233)
  AUTHORS   Deardorff,M.A., Noon,S.E. and Krantz,I.D.
  TITLE     Cornelia de Lange Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301283
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC080185.1, D80000.2 and
            AC233728.4.
            
            On May 13, 2003 this sequence version replaced NP_006297.1.
            
            Summary: Proper cohesion of sister chromatids is a prerequisite for
            the correct segregation of chromosomes during cell division. The
            cohesin multiprotein complex is required for sister chromatid
            cohesion. This complex is composed partly of two structural
            maintenance of chromosomes (SMC) proteins, SMC3 and either SMC1B or
            the protein encoded by this gene. Most of the cohesin complexes
            dissociate from the chromosomes before mitosis, although those
            complexes at the kinetochore remain. Therefore, the encoded protein
            is thought to be an important part of functional kinetochores. In
            addition, this protein interacts with BRCA1 and is phosphorylated
            by ATM, indicating a potential role for this protein in DNA repair.
            This gene, which belongs to the SMC gene family, is located in an
            area of the X-chromosome that escapes X inactivation. Mutations in
            this gene result in Cornelia de Lange syndrome. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D80000.2, S78271.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322213.9/ ENSP00000323421.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1233
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..1233
                     /product="structural maintenance of chromosomes protein 1A
                     isoform 1"
                     /note="SMC1 (structural maintenance of chromosomes 1,
                     yeast)-like 1; segregation of mitotic chromosomes 1;
                     SMC-1-alpha; SMC protein 1A; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=143102
     Region          3..1210
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; pfam02463"
                     /db_xref="CDD:426784"
     Region          284..308
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14683.2)"
     Region          348..369
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14683.2)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q14683.2)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14683.2)"
     Site            648
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14683.2)"
     Site            713
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14683.2)"
     Region          947..966
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14683.2)"
     Site            957
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000269|PubMed:11877377,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14683.2)"
     Site            962
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14683.2)"
     Site            966
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM and ATR.
                     /evidence=ECO:0000269|PubMed:11877377,
                     ECO:0000269|PubMed:14657349, ECO:0000269|PubMed:22977523,
                     ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q14683.2)"
     Site            970
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14683.2)"
     Site            1037
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CU62; propagated from
                     UniProtKB/Swiss-Prot (Q14683.2)"
     CDS             1..1233
                     /gene="SMC1A"
                     /gene_synonym="CDLS2; DEE85; DXS423E; EIEE85; SB1.8; SMC1;
                     SMC1alpha; SMC1L1; SMCB"
                     /coded_by="NM_006306.4:55..3756"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14352.1"
                     /db_xref="GeneID:8243"
                     /db_xref="HGNC:HGNC:11111"
                     /db_xref="MIM:300040"
ORIGIN      
        1 mgflklieie nfksykgrqi igpfqrftai igpngsgksn lmdaisfvlg ektsnlrvkt
       61 lrdlihgapv gkpaanrafv smvyseegae drtfarvivg gsseykinnk vvqlheysee
      121 leklgilika rnflvfqgav esiamknpke rtalfeeisr sgelaqeydk rkkemvkaee
      181 dtqfnyhrkk niaaerkeak qekeeadryq rlkdevvraq vqlqlfklyh neveieklnk
      241 elasknkeie kdkkrmdkve delkekkkel gkmmreqqqi ekeikekdse lnqkrpqyik
      301 akentshkik kleaakkslq naqkhykkrk gdmdelekem lsvekarqef eermeeesqs
      361 qgrdltleen qvkkyhrlke easkraatla qelekfnrdq kadqdrldle erkkveteak
      421 ikqklreiee nqkrieklee yittskqsle eqkklegelt eevemakrri deinkelnqv
      481 meqlgdarid rqessrqqrk aeimesikrl ypgsvygrli dlcqptqkky qiavtkvlgk
      541 nmdaiivdse ktgrdciqyi keqrgepetf lpldylevkp tdeklrelkg aklvidviry
      601 epphikkalq yacgnalvcd nvedarriaf gghqrhktva ldgtlfqksg visggasdlk
      661 akarrwdeka vdklkekker lteelkeqmk akrkeaelrq vqsqahglqm rlkysqsdle
      721 qtktrhlaln lqeksklese lanfgprind ikriiqsrer emkdlkekmn qvedevfeef
      781 creigvrnir efeeekvkrq neiakkrlef enqktrlgiq ldfeknqlke dqdkvhmweq
      841 tvkkdeneie klkkeeqrhm kiidetmaql qdlknqhlak ksevndknhe meeirkklgg
      901 ankemthlqk evtaietkle qkrsdrhnll qackmqdikl plskgtmddi sqeegssqge
      961 dsvsgsqris siyarealie idygdlcedl kdaqaeeeik qemntlqqkl neqqsvlqri
     1021 aapnmkamek lesvrdkfqe tsdefeaark rakkakqafe qikkerfdrf nacfesvatn
     1081 ideiykalsr nssaqaflgp enpeepyldg inyncvapgk rfrpmdnlsg gektvaalal
     1141 lfaihsykpa pffvldeida aldntnigkv anyikeqstc nfqaivislk eefytkaesl
     1201 igvypeqgdc viskvltfdl tkypdanpnp neq
//
LOCUS       NP_001124323             172 aa            linear   PRI 21-NOV-2025
DEFINITION  cyclin-dependent kinase inhibitor 3 isoform 2 [Homo sapiens].
ACCESSION   NP_001124323
VERSION     NP_001124323.1
DBSOURCE    REFSEQ: accession NM_001130851.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Qin,H., Wang,Q., Xu,J., Zeng,H., Liu,J., Yu,F. and Yang,J.
  TITLE     Integrative analysis of anoikis-related genes prognostic signature
            with immunotherapy and identification of CDKN3 as a key oncogene in
            lung adenocarcinoma
  JOURNAL   Int Immunopharmacol 143 (Pt 1), 113282 (2024)
   PUBMED   39383787
  REMARK    GeneRIF: Integrative analysis of anoikis-related genes prognostic
            signature with immunotherapy and identification of CDKN3 as a key
            oncogene in lung adenocarcinoma.
            Erratum:[Int Immunopharmacol. 2024 Dec 25;143(Pt 3):113584. doi:
            10.1016/j.intimp.2024.113584. PMID: 39580329]
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Zhang,J., Zhang,Y. and Zhang,J.
  TITLE     N6-Methyladenosine modified circ-NAB1 modulates cell cycle and
            epithelial-mesenchymal transition via CDKN3 in endometrial cancer
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (5), 161-169 (2024)
   PUBMED   38814199
  REMARK    GeneRIF: N6-Methyladenosine modified circ-NAB1 modulates cell cycle
            and epithelial-mesenchymal transition via CDKN3 in endometrial
            cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Chen,Y., Li,D., Sha,K., Zhang,X. and Liu,T.
  TITLE     Human pan-cancer analysis of the predictive biomarker for the CDKN3
  JOURNAL   Eur J Med Res 29 (1), 272 (2024)
   PUBMED   38720365
  REMARK    GeneRIF: Human pan-cancer analysis of the predictive biomarker for
            the CDKN3.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Zhu,S. and Fang,Z.
  TITLE     MicroRNA-127-3p Inhibits Cardiomyocyte Inflammation and Apoptosis
            after Acute Myocardial Infarction via Targeting CDKN3
  JOURNAL   Int Heart J 64 (6), 1133-1139 (2023)
   PUBMED   38030294
  REMARK    GeneRIF: MicroRNA-127-3p Inhibits Cardiomyocyte Inflammation and
            Apoptosis after Acute Myocardial Infarction via Targeting CDKN3.
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Poon,R.Y. and Hunter,T.
  TITLE     Dephosphorylation of Cdk2 Thr160 by the cyclin-dependent
            kinase-interacting phosphatase KAP in the absence of cyclin
  JOURNAL   Science 270 (5233), 90-93 (1995)
   PUBMED   7569954
REFERENCE   7  (residues 1 to 172)
  AUTHORS   Demetrick,D.J., Matsumoto,S., Hannon,G.J., Okamoto,K., Xiong,Y.,
            Zhang,H. and Beach,D.H.
  TITLE     Chromosomal mapping of the genes for the human cell cycle proteins
            cyclin C (CCNC), cyclin E (CCNE), p21 (CDKN1) and KAP (CDKN3)
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 190-192 (1995)
   PUBMED   7698009
REFERENCE   8  (residues 1 to 172)
  AUTHORS   Hannon,G.J., Casso,D. and Beach,D.
  TITLE     KAP: a dual specificity phosphatase that interacts with
            cyclin-dependent kinases
  JOURNAL   Proc Natl Acad Sci U S A 91 (5), 1731-1735 (1994)
   PUBMED   8127873
REFERENCE   9  (residues 1 to 172)
  AUTHORS   Harper,J.W., Adami,G.R., Wei,N., Keyomarsi,K. and Elledge,S.J.
  TITLE     The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1
            cyclin-dependent kinases
  JOURNAL   Cell 75 (4), 805-816 (1993)
   PUBMED   8242751
REFERENCE   10 (residues 1 to 172)
  AUTHORS   Gyuris,J., Golemis,E., Chertkov,H. and Brent,R.
  TITLE     Cdi1, a human G1 and S phase protein phosphatase that associates
            with Cdk2
  JOURNAL   Cell 75 (4), 791-803 (1993)
   PUBMED   8242750
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC064965.1.
            
            Summary: The protein encoded by this gene belongs to the dual
            specificity protein phosphatase family. It was identified as a
            cyclin-dependent kinase inhibitor, and has been shown to interact
            with, and dephosphorylate CDK2 kinase, thus prevent the activation
            of CDK2 kinase. This gene was reported to be deleted, mutated, or
            overexpressed in several kinds of cancers. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Transcript Variant: This variant (2) lacks an in-frame segment in
            the CDS, as compared to variant 1. The resulting isoform (2) lacks
            an internal segment, as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064965.1, BU176574.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.2"
     Protein         1..172
                     /product="cyclin-dependent kinase inhibitor 3 isoform 2"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="cyclin-dependent kinase interactor 1;
                     cyclin-dependent kinase interacting protein 2;
                     CDK2-associated dual specificity phosphatase;
                     cyclin-dependent kinase inhibitor; kinase-associated
                     phosphatase; Cdk-associated protein phosphatase"
                     /calculated_mol_wt=19228
     Region          <11..128
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     CDS             1..172
                     /gene="CDKN3"
                     /gene_synonym="CDI1; CIP2; KAP; KAP1"
                     /coded_by="NM_001130851.2:63..581"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45109.1"
                     /db_xref="GeneID:1033"
                     /db_xref="HGNC:HGNC:1791"
                     /db_xref="MIM:123832"
ORIGIN      
        1 mkppssiqts ckfkdvrrnv qkdteelksc giqdifvfct rgelskyrvp nlldlyqqcg
       61 iithhhpiad ggtpdiascc eimeelttcl knyrktlihc ygglgrsclv aaclllylsd
      121 tispeqaids lrdlrgsgai qtikqynylh efrdklaahl ssrdsqsrsv sr
//
LOCUS       NP_001277214             243 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA excision repair protein ERCC-8 isoform 4 [Homo sapiens].
ACCESSION   NP_001277214
VERSION     NP_001277214.1
DBSOURCE    REFSEQ: accession NM_001290285.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Yang,D., Lai,A., Davies,A., Janssen,A.F., Ellis,M.O. and Larrieu,D.
  TITLE     A novel role for CSA in the regulation of nuclear envelope
            integrity: uncovering a non-canonical function
  JOURNAL   Life Sci Alliance 7 (11), e202402745 (2024)
   PUBMED   39209536
  REMARK    GeneRIF: A novel role for CSA in the regulation of nuclear envelope
            integrity: uncovering a non-canonical function.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   van Sluis,M., Yu,Q., van der Woude,M., Gonzalo-Hansen,C.,
            Dealy,S.C., Janssens,R.C., Somsen,H.B., Ramadhin,A.R.,
            Dekkers,D.H.W., Wienecke,H.L., Demmers,J.J.P.G., Raams,A.,
            Davo-Martinez,C., Llerena Schiffmacher,D.A., van Toorn,M.,
            Hackes,D., Thijssen,K.L., Zhou,D., Lammers,J.G., Pines,A.,
            Vermeulen,W., Pothof,J., Demmers,J.A.A., van den Berg,D.L.C.,
            Lans,H. and Marteijn,J.A.
  TITLE     Transcription-coupled DNA-protein crosslink repair by CSB and
            CRL4CSA-mediated degradation
  JOURNAL   Nat Cell Biol 26 (5), 770-783 (2024)
   PUBMED   38600236
  REMARK    GeneRIF: Transcription-coupled DNA-protein crosslink repair by CSB
            and CRL4[CSA]-mediated degradation.
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Carnie,C.J., Acampora,A.C., Bader,A.S., Erdenebat,C., Zhao,S.,
            Bitensky,E., van den Heuvel,D., Parnas,A., Gupta,V.,
            D'Alessandro,G., Sczaniecka-Clift,M., Weickert,P., Aygenli,F.,
            Gotz,M.J., Cordes,J., Esain-Garcia,I., Melidis,L., Wondergem,A.P.,
            Lam,S., Robles,M.S., Balasubramanian,S., Adar,S.,
            Luijsterburg,M.S., Jackson,S.P. and Stingele,J.
  TITLE     Transcription-coupled repair of DNA-protein cross-links depends on
            CSA and CSB
  JOURNAL   Nat Cell Biol 26 (5), 797-810 (2024)
   PUBMED   38600235
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Kokic,G., Yakoub,G., van den Heuvel,D., Wondergem,A.P., van der
            Meer,P.J., van der Weegen,Y., Chernev,A., Fianu,I., Fokkens,T.J.,
            Lorenz,S., Urlaub,H., Cramer,P. and Luijsterburg,M.S.
  TITLE     Structural basis for RNA polymerase II ubiquitylation and
            inactivation in transcription-coupled repair
  JOURNAL   Nat Struct Mol Biol 31 (3), 536-547 (2024)
   PUBMED   38316879
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Liu,M.W., Hu,C.F., Jin,J.Y., Xiang,R., Fan,L.L., Li,Y.L. and Zhu,L.
  TITLE     A compound heterozygous mutation of ERCC8 is responsible for a
            family with Cockayne syndrome
  JOURNAL   Mol Biol Rep 51 (1), 371 (2024)
   PUBMED   38411728
  REMARK    GeneRIF: A compound heterozygous mutation of ERCC8 is responsible
            for a family with Cockayne syndrome.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Selby,C.P. and Sancar,A.
  TITLE     Human transcription-repair coupling factor CSB/ERCC6 is a
            DNA-stimulated ATPase but is not a helicase and does not disrupt
            the ternary transcription complex of stalled RNA polymerase II
  JOURNAL   J Biol Chem 272 (3), 1885-1890 (1997)
   PUBMED   8999876
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Bregman,D.B., Halaban,R., van Gool,A.J., Henning,K.A.,
            Friedberg,E.C. and Warren,S.L.
  TITLE     UV-induced ubiquitination of RNA polymerase II: a novel
            modification deficient in Cockayne syndrome cells
  JOURNAL   Proc Natl Acad Sci U S A 93 (21), 11586-11590 (1996)
   PUBMED   8876179
REFERENCE   8  (residues 1 to 243)
  AUTHORS   Itoh,T., Shiomi,T., Shiomi,N., Harada,Y., Wakasugi,M.,
            Matsunaga,T., Nikaido,O., Friedberg,E.C. and Yamaizumi,M.
  TITLE     Rodent complementation group 8 (ERCC8) corresponds to Cockayne
            syndrome complementation group A
  JOURNAL   Mutat Res 362 (2), 167-174 (1996)
   PUBMED   8596535
REFERENCE   9  (residues 1 to 243)
  AUTHORS   Henning,K.A., Li,L., Iyer,N., McDaniel,L.D., Reagan,M.S.,
            Legerski,R., Schultz,R.A., Stefanini,M., Lehmann,A.R., Mayne,L.V.
            and Friedberg,E.C.
  TITLE     The Cockayne syndrome group A gene encodes a WD repeat protein that
            interacts with CSB protein and a subunit of RNA polymerase II TFIIH
  JOURNAL   Cell 82 (4), 555-564 (1995)
   PUBMED   7664335
REFERENCE   10 (residues 1 to 243)
  AUTHORS   Laugel,V.
  TITLE     Cockayne Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301516
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA169067.1, AK294856.1,
            AK056931.1 and AC104113.3.
            
            Summary: This gene encodes a WD repeat protein, which interacts
            with Cockayne syndrome type B (CSB) protein and with p44 protein, a
            subunit of the RNA polymerase II transcription factor IIH.
            Mutations in this gene have been identified in patients with
            hereditary disease Cockayne syndrome (CS). CS cells are abnormally
            sensitive to ultraviolet radiation and are defective in the repair
            of transcriptionally active genes. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Mar 2014].
            
            Transcript Variant: This variant (4) lacks an alternate internal
            exon and uses a downstream AUG start codon compared to variant 1.
            The resulting isoform (4) has a shorter and distinct N-terminus
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK294856.1, SRR14038194.3587554.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.1"
     Protein         1..243
                     /product="DNA excision repair protein ERCC-8 isoform 4"
                     /note="Cockayne syndrome WD-repeat protein CSA; DNA
                     excision repair protein ERCC-8; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 8; cockayne syndrome WD repeat
                     protein CSA; excision repair cross-complementation group
                     8"
                     /calculated_mol_wt=26683
     Region          <4..208
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          37..90
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          95..131
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          137..178
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..243
                     /gene="ERCC8"
                     /gene_synonym="CKN1; CSA; UVSS2"
                     /coded_by="NM_001290285.2:440..1171"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:1161"
                     /db_xref="HGNC:HGNC:3439"
                     /db_xref="MIM:609412"
ORIGIN      
        1 mgykyitigt rgpkvqlcdl ksgscshilq ghrqeilavs wsprydyila tasadsrvkl
       61 wdvrrasgcl itldqhngkk sqavesanta hngkvnglcf tsdglhlltv gtdnrmrlwn
      121 ssngentlvn ygkvcnnskk glkftvscgc ssefvfvpyg stiavytvys geqitmlkgh
      181 yktvdccvfq snfqelysgs rdcnilawvp slyepvpddd etttksqlnp afedawsssd
      241 eeg
//
LOCUS       NP_001382251             937 aa            linear   PRI 21-NOV-2025
DEFINITION  myomegalin isoform 41 [Homo sapiens].
ACCESSION   NP_001382251
VERSION     NP_001382251.1
DBSOURCE    REFSEQ: accession NM_001395322.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Pan,R., Dai,J., Liang,W., Wang,H., Ye,L., Ye,S., Lin,Z., Huang,S.,
            Xiong,Y., Zhang,L., Lu,L., Wang,O., Shen,X., Liao,W. and Lu,X.
  TITLE     PDE4DIP contributes to colorectal cancer growth and chemoresistance
            through modulation of the NF1/RAS signaling axis
  JOURNAL   Cell Death Dis 14 (6), 373 (2023)
   PUBMED   37355626
  REMARK    GeneRIF: PDE4DIP contributes to colorectal cancer growth and
            chemoresistance through modulation of the NF1/RAS signaling axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 937)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   4  (residues 1 to 937)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 937)
  AUTHORS   Abou Ziki,M.D., Bhat,N., Neogi,A., Driscoll,T.P., Ugwu,N., Liu,Y.,
            Smith,E., Abboud,J.M., Chouairi,S., Schwartz,M.A., Akar,J.G. and
            Mani,A.
  TITLE     Epistatic interaction of PDE4DIP and DES mutations in familial
            atrial fibrillation with slow conduction
  JOURNAL   Hum Mutat 42 (10), 1279-1293 (2021)
   PUBMED   34289528
  REMARK    GeneRIF: Epistatic interaction of PDE4DIP and DES mutations in
            familial atrial fibrillation with slow conduction.
REFERENCE   6  (residues 1 to 937)
  AUTHORS   Shimada,H., Kuboshima,M., Shiratori,T., Nabeya,Y., Takeuchi,A.,
            Takagi,H., Nomura,F., Takiguchi,M., Ochiai,T. and Hiwasa,T.
  TITLE     Serum anti-myomegalin antibodies in patients with esophageal
            squamous cell carcinoma
  JOURNAL   Int J Oncol 30 (1), 97-103 (2007)
   PUBMED   17143517
  REMARK    GeneRIF: MMGL-antibody is significantly with a favorable prognosis.
            Consequently, MMGL-anatibodies may be a useful tumor marker to
            diagnose and establish a prognosis in patients with esophageal
            squamous cell carcinoma.
REFERENCE   7  (residues 1 to 937)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 937)
  AUTHORS   Soejima,H., Kawamoto,S., Akai,J., Miyoshi,O., Arai,Y., Morohka,T.,
            Matsuo,S., Niikawa,N., Kimura,A., Okubo,K. and Mukai,T.
  TITLE     Isolation of novel heart-specific genes using the BodyMap database
  JOURNAL   Genomics 74 (1), 115-120 (2001)
   PUBMED   11374908
REFERENCE   9  (residues 1 to 937)
  AUTHORS   Verde,I., Pahlke,G., Salanova,M., Zhang,G., Wang,S., Coletti,D.,
            Onuffer,J., Jin,S.L. and Conti,M.
  TITLE     Myomegalin is a novel protein of the golgi/centrosome that
            interacts with a cyclic nucleotide phosphodiesterase
  JOURNAL   J Biol Chem 276 (14), 11189-11198 (2001)
   PUBMED   11134006
REFERENCE   10 (residues 1 to 937)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC245389.1 and AC239802.3.
            
            Summary: The protein encoded by this gene serves to anchor
            phosphodiesterase 4D to the Golgi/centrosome region of the cell.
            Defects in this gene may be a cause of myeloproliferative disorder
            (MBD) associated with eosinophilia. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.58112.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     Protein         1..937
                     /product="myomegalin isoform 41"
                     /note="myomegalin; cardiomyopathy-associated protein 2"
                     /calculated_mol_wt=108228
     Region          <28..>519
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          <320..>825
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          <719..>937
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..937
                     /gene="PDE4DIP"
                     /gene_synonym="CMYA2; MMGL"
                     /coded_by="NM_001395322.1:523..3336"
                     /note="isoform 41 is encoded by transcript variant 41"
                     /db_xref="GeneID:9659"
                     /db_xref="HGNC:HGNC:15580"
                     /db_xref="MIM:608117"
ORIGIN      
        1 mqqkyeasre diykrnielk veveslkrel qdkkqhldkt wadvenlnsq neaelrrqfe
       61 erqqetehvy ellenkiqll qeesrlakne aarmaalvea ekecnlelse klkgvtknwe
      121 dvpgdqvkpd qytealaqrd krieelnqsl aaqerlveql srekqqllhl leeptsmevq
      181 pmteellkqq klnshettit qqsvsdshla elqekiqqte atnkilqekl nemsyelkca
      241 qessqkqdgt iqnlketlks rereteelyq viegqndtma klremlhqsq lgqlhssegt
      301 spaqqqvall dlqsalfcsq leiqklqrvv rqkerqlada kqcvqfveaa aheseqqkea
      361 swkhnqelrk alqqlqeelq nksqqlrawe aekyneirtq eqniqhlnhs lshkeqllqe
      421 frellqyrdn sdktleanem lleklrqrih dkavalerai dekfsaleek ekelrqlrla
      481 vrerdhdler lrdvlssnea tmqsmesllr akgleveqls ttcqnlqwlk eemetkfsrw
      541 qkeqesiiqq lqtslhdrnk evedlsatll cklgpgqsei aeelcqrlqr kermlqdlls
      601 drnkqvlehe meiqgllqsv streqesqaa aeklvqalme rnselqalrq ylggrdslms
      661 qapisnqqae vtptgrlgkq tdqgsmqips rddstsltak edvsiprstl gdldtvagle
      721 kelsnakeel elmakkeres qmelsalqsm mavqeeelqv qaadmesltr niqikedlik
      781 dlqmqlvdpe dipamerltq evlllrekva svesqgqeis gnrrqqlllm leglvdersr
      841 lnealqaerq lysslvkfha hpesserdrt lqvelegaqv lrsrleevlg rslerlnrle
      901 tlaaiggaaa gddtedtste ftdsieeeaa hhshqql
//
LOCUS       NP_001352713            1164 aa            linear   PRI 21-NOV-2025
DEFINITION  plasma membrane calcium-transporting ATPase 4 isoform 4c [Homo
            sapiens].
ACCESSION   NP_001352713
VERSION     NP_001352713.1
DBSOURCE    REFSEQ: accession NM_001365784.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Miya,V., Kumar,C., Breed,A.A., Idicula-Thomas,S. and Pathak,B.R.
  TITLE     Mammalian cysteine-rich secretory proteins interact with plasma
            membrane Ca2+ exporter PMCA4b
  JOURNAL   Andrology 12 (5), 1096-1110 (2024)
   PUBMED   37882330
  REMARK    GeneRIF: Mammalian cysteine-rich secretory proteins interact with
            plasma membrane Ca[2+] exporter PMCA4b.
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Yoshie,S., Kuriyama,M., Maekawa,M., Xu,W., Niidome,T., Futaki,S.
            and Hirose,H.
  TITLE     ATP2B4 is an essential gene for epidermal growth factor-induced
            macropinocytosis in A431 cells
  JOURNAL   Genes Cells 29 (6), 512-520 (2024)
   PUBMED   38597132
  REMARK    GeneRIF: ATP2B4 is an essential gene for epidermal growth
            factor-induced macropinocytosis in A431 cells.
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Thiam,A., Nisar,S., Adjemout,M., Gallardo,F., Ka,O., Mbengue,B.,
            Diop,G., Dieye,A., Marquet,S. and Rihet,P.
  TITLE     ATP2B4 regulatory genetic variants are associated with mild malaria
  JOURNAL   Malar J 22 (1), 68 (2023)
   PUBMED   36849945
  REMARK    GeneRIF: ATP2B4 regulatory genetic variants are associated with
            mild malaria.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1164)
  AUTHORS   Joof,F., Hartmann,E., Jarvis,A., Colley,A., Cross,J.H., Avril,M.,
            Prentice,A.M. and Cerami,C.
  TITLE     Genetic variations in human ATP2B4 gene alter Plasmodium falciparum
            in vitro growth in RBCs from Gambian adults
  JOURNAL   Malar J 22 (1), 5 (2023)
   PUBMED   36604655
  REMARK    GeneRIF: Genetic variations in human ATP2B4 gene alter Plasmodium
            falciparum in vitro growth in RBCs from Gambian adults.
            Erratum:[Malar J. 2023 May 25;22(1):164. doi:
            10.1186/s12936-023-04565-8. PMID: 37231516]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1164)
  AUTHORS   Ambartsumyan,L.
  TITLE     Megacystis-Microcolon-Intestinal Hypoperistalsis Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31070878
REFERENCE   6  (residues 1 to 1164)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   7  (residues 1 to 1164)
  AUTHORS   Heim,R., Hug,M., Iwata,T., Strehler,E.E. and Carafoli,E.
  TITLE     Microdiversity of human-plasma-membrane calcium-pump isoform 2
            generated by alternative RNA splicing in the N-terminal coding
            region
  JOURNAL   Eur J Biochem 205 (1), 333-340 (1992)
   PUBMED   1313367
REFERENCE   8  (residues 1 to 1164)
  AUTHORS   Brandt,P., Neve,R.L., Kammesheidt,A., Rhoads,R.E. and Vanaman,T.C.
  TITLE     Analysis of the tissue-specific distribution of mRNAs encoding the
            plasma membrane calcium-pumping ATPases and characterization of an
            alternately spliced form of PMCA4 at the cDNA and genomic levels
  JOURNAL   J Biol Chem 267 (7), 4376-4385 (1992)
   PUBMED   1531651
REFERENCE   9  (residues 1 to 1164)
  AUTHORS   Olson,S., Wang,M.G., Carafoli,E., Strehler,E.E. and McBride,O.W.
  TITLE     Localization of two genes encoding plasma membrane
            Ca2(+)-transporting ATPases to human chromosomes 1q25-32 and
            12q21-23
  JOURNAL   Genomics 9 (4), 629-641 (1991)
   PUBMED   1674727
REFERENCE   10 (residues 1 to 1164)
  AUTHORS   Strehler,E.E., James,P., Fischer,R., Heim,R., Vorherr,T.,
            Filoteo,A.G., Penniston,J.T. and Carafoli,E.
  TITLE     Peptide sequence analysis and molecular cloning reveal two calcium
            pump isoforms in the human erythrocyte membrane
  JOURNAL   J Biol Chem 265 (5), 2835-2842 (1990)
   PUBMED   2137451
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513343.22 and AC114402.2.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type primary ion transport ATPases characterized by the formation
            of an aspartyl phosphate intermediate during the reaction cycle.
            These enzymes remove bivalent calcium ions from eukaryotic cells
            against very large concentration gradients and play a critical role
            in intracellular calcium homeostasis. The mammalian plasma membrane
            calcium ATPase isoforms are encoded by at least four separate genes
            and the diversity of these enzymes is further increased by
            alternative splicing of transcripts. The expression of different
            isoforms and splice variants is regulated in a developmental,
            tissue- and cell type-specific manner, suggesting that these pumps
            are functionally adapted to the physiological needs of particular
            cells and tissues. This gene encodes the plasma membrane calcium
            ATPase isoform 4. Alternatively spliced transcript variants
            encoding different isoforms have been identified. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4), as well as variant 3, encodes
            isoform 4c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.86606.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..1164
                     /product="plasma membrane calcium-transporting ATPase 4
                     isoform 4c"
                     /EC_number="7.2.2.10"
                     /note="sarcolemmal calcium pump; plasma membrane
                     calcium-transporting ATPase 4; ATPase, Ca++ transporting,
                     plasma membrane 4; matrix-remodeling-associated protein 1"
                     /calculated_mol_wt=128691
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P23634.2)"
     Region          20..1052
                     /region_name="ATPase-IIB_Ca"
                     /note="plasma-membrane calcium-translocating P-type
                     ATPase; TIGR01517"
                     /db_xref="CDD:273668"
     Site            93..113
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23634.2)"
     Site            151..171
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23634.2)"
     Region          294..318
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23634.2)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P23634.2)"
     Site            357..376
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23634.2)"
     Site            410..427
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23634.2)"
     Site            841..860
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23634.2)"
     Site            871..891
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23634.2)"
     Site            912..934
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23634.2)"
     Site            953..974
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23634.2)"
     Site            994..1015
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23634.2)"
     Site            1026..1047
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23634.2)"
     Region          1086..1103
                     /region_name="Calmodulin-binding subdomain A.
                     /evidence=ECO:0000269|PubMed:2963820"
                     /note="propagated from UniProtKB/Swiss-Prot (P23634.2)"
     Region          1089..1150
                     /region_name="ATP_Ca_trans_C"
                     /note="Plasma membrane calcium transporter ATPase C
                     terminal; pfam12424"
                     /db_xref="CDD:463575"
     Site            1102
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P23634.2)"
     Region          1104..1113
                     /region_name="Calmodulin-binding subdomain B.
                     /evidence=ECO:0000250|UniProtKB:P20020"
                     /note="propagated from UniProtKB/Swiss-Prot (P23634.2)"
     CDS             1..1164
                     /gene="ATP2B4"
                     /gene_synonym="ATP2B2; MXRA1; PMCA4; PMCA4b; PMCA4x"
                     /coded_by="NM_001365784.2:610..4104"
                     /note="isoform 4c is encoded by transcript variant 4"
                     /db_xref="GeneID:493"
                     /db_xref="HGNC:HGNC:817"
                     /db_xref="MIM:108732"
ORIGIN      
        1 mtnpsdrvlp ansmaesreg dfgctvmelr klmelrsrda ltqinvhygg vqnlcsrlkt
       61 spveglsgnp adlekrrqvf ghnvippkkp ktflelvwea lqdvtliile iaaiislvls
      121 fyrpageene lcgqvattpe deneaqagwi egaailfsvi ivvlvtafnd wskekqfrgl
      181 qcrieqeqkf siirngqliq lpvaeivvgd iaqvkygdll padgiliqgn dlkidesslt
      241 gesdhvkksl dkdpmllsgt hvmegsgrmv vtavgvnsqt giiltllgvn eddegekkkk
      301 gkkqgvpenr nkaktqdgva leiqplnsqe gidneekdkk avkvpkkeks vlqgkltrla
      361 vqigkagllm saltvfilil yfvidnfvin rrpwlpectp iyiqyfvkff iigitvlvva
      421 vpeglplavt islaysvkkm mkdnnlvrhl dacetmgnat aicsdktgtl tmnrmtvvqa
      481 yiggihyrqi pspdvflpkv ldlivngisi nsaytskilp pekegglprq vgnktecall
      541 gfvtdlkqdy qavrnevpee klykvytfns vrksmstvir npnggfrmys kgaseiilrk
      601 cnrildrkge avpfknkdrd dmvrtviepm acdglrtici ayrdfddtep swdneneilt
      661 eltciavvgi edpvrpevpd aiakckqagi tvrmvtgdni ntaraiatkc giltpgddfl
      721 clegkefnrl irnekgeveq ekldkiwpkl rvlarssptd khtlvkgiid stvgehrqvv
      781 avtgdgtndg palkkadvgf amgiagtdva keasdiiltd dnftsivkav mwgrnvydsi
      841 skflqfqltv nvvavivaft gacitqdspl kavqmlwvnl imdtfaslal atepptesll
      901 krrpygrnkp lisrtmmkni lghafyqliv ifilvfagek ffdidsgrka plhsppsqhy
      961 tivfntfvlm qlfneinsrk ihgeknvfsg iyrniifcsv vlgtficqif ivefggkpfs
     1021 ctslslsqwl wclfigigel lwgqfisaip trslkflkea ghgttkeeit kdaegldeid
     1081 haemelrrgq ilwfrglnri qtqidvintf qtgasfkgvl rrqnmgqhld vklvpsssyv
     1141 avapvksspt tsvpavsspp mgse
//
LOCUS       NP_001369238             347 aa            linear   PRI 21-NOV-2025
DEFINITION  ataxin-7-like protein 3 isoform b [Homo sapiens].
ACCESSION   NP_001369238
VERSION     NP_001369238.1
DBSOURCE    REFSEQ: accession NM_001382309.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Passet,M., Kim,R., Gachet,S., Sigaux,F., Chaumeil,J., Galland,A.,
            Sexton,T., Quentin,S., Hernandez,L., Larcher,L., Bergugnat,H.,
            Ye,T., Karasu,N., Caye,A., Heizmann,B., Duluc,I., Chevallier,P.,
            Rousselot,P., Huguet,F., Leguay,T., Hunault,M., Pflumio,F.,
            Freund,J.N., Lobry,C., Lheritier,V., Dombret,H., Domon-Dell,C.,
            Soulier,J., Boissel,N. and Clappier,E.
  TITLE     Concurrent CDX2 cis-deregulation and UBTF::ATXN7L3 fusion define a
            novel high-risk subtype of B-cell ALL
  JOURNAL   Blood 139 (24), 3505-3518 (2022)
   PUBMED   35316324
  REMARK    GeneRIF: Concurrent CDX2 cis-deregulation and UBTF::ATXN7L3 fusion
            define a novel high-risk subtype of B-cell ALL.
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Kimura,S., Montefiori,L., Iacobucci,I., Zhao,Y., Gao,Q.,
            Paietta,E.M., Haferlach,C., Laird,A.D., Mead,P.E., Gu,Z., Stock,W.,
            Litzow,M., Rowe,J.M., Luger,S.M., Hunger,S.P., Ryland,G.L.,
            Schmidt,B., Ekert,P.G., Oshlack,A., Grimmond,S.M., Rehn,J.,
            Breen,J., Yeung,D., White,D.L., Aldoss,I., Jabbour,E.J., Pui,C.H.,
            Meggendorfer,M., Walter,W., Kern,W., Haferlach,T., Brady,S.,
            Zhang,J., Roberts,K.G., Blombery,P. and Mullighan,C.G.
  TITLE     Enhancer retargeting of CDX2 and UBTF::ATXN7L3 define a subtype of
            high-risk B-progenitor acute lymphoblastic leukemia
  JOURNAL   Blood 139 (24), 3519-3531 (2022)
   PUBMED   35192684
  REMARK    GeneRIF: Enhancer retargeting of CDX2 and UBTF::ATXN7L3 define a
            subtype of high-risk B-progenitor acute lymphoblastic leukemia.
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Helmlinger,D., Hardy,S., Sasorith,S., Klein,F., Robert,F.,
            Weber,C., Miguet,L., Potier,N., Van-Dorsselaer,A., Wurtz,J.M.,
            Mandel,J.L., Tora,L. and Devys,D.
  TITLE     Ataxin-7 is a subunit of GCN5 histone acetyltransferase-containing
            complexes
  JOURNAL   Hum Mol Genet 13 (12), 1257-1265 (2004)
   PUBMED   15115762
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Martinez,E., Palhan,V.B., Tjernberg,A., Lymar,E.S., Gamper,A.M.,
            Kundu,T.K., Chait,B.T. and Roeder,R.G.
  TITLE     Human STAGA complex is a chromatin-acetylating transcription
            coactivator that interacts with pre-mRNA splicing and DNA
            damage-binding factors in vivo
  JOURNAL   Mol Cell Biol 21 (20), 6782-6795 (2001)
   PUBMED   11564863
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Brand,M., Moggs,J.G., Oulad-Abdelghani,M., Lejeune,F.,
            Dilworth,F.J., Stevenin,J., Almouzni,G. and Tora,L.
  TITLE     UV-damaged DNA-binding protein in the TFTC complex links DNA damage
            recognition to nucleosome acetylation
  JOURNAL   EMBO J 20 (12), 3187-3196 (2001)
   PUBMED   11406595
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Brand,M., Yamamoto,K., Staub,A. and Tora,L.
  TITLE     Identification of TATA-binding protein-free TAFII-containing
            complex subunits suggests a role in nucleosome acetylation and
            signal transduction
  JOURNAL   J Biol Chem 274 (26), 18285-18289 (1999)
   PUBMED   10373431
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Wieczorek,E., Brand,M., Jacq,X. and Tora,L.
  TITLE     Function of TAF(II)-containing complex without TBP in transcription
            by RNA polymerase II
  JOURNAL   Nature 393 (6681), 187-191 (1998)
   PUBMED   9603525
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004596.2.
            
            Transcript Variant: This variant (2), as well as variants 4, 5, and
            6, encodes isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.78456.1,
                                           SRR12921934.1101016.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000587097.6/ ENSP00000465614.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..347
                     /product="ataxin-7-like protein 3 isoform b"
                     /calculated_mol_wt=38520
     Region          80..112
                     /region_name="Sgf11"
                     /note="Sgf11 (transcriptional regulation protein);
                     pfam08209"
                     /db_xref="CDD:369754"
     Region          116..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CW9.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q14CW9.1)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14CW9.1)"
     Region          <208..>237
                     /region_name="SCA7"
                     /note="zinc-binding domain; pfam08313"
                     /db_xref="CDD:462422"
     Region          275..347
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CW9.1)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q14CW9.1)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14CW9.1)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14CW9.1)"
     CDS             1..347
                     /gene="ATXN7L3"
                     /gene_synonym="HATONS; SGF11"
                     /coded_by="NM_001382309.1:450..1493"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42345.1"
                     /db_xref="GeneID:56970"
                     /db_xref="HGNC:HGNC:25416"
                     /db_xref="MIM:619010"
ORIGIN      
        1 mkmeemslsg ldnskleaia qeiyadlved sclgfcfevh ravkcgyffl ddtdpdsmkd
       61 feivdqpgld ifgqvfnqwk skecvcpncs rsiaasrfap hlekclgmgr nssrianrri
      121 ansnnmnkse sdqednddin dndwsygsek kakkrksdkn pnsprrsksl khkngelsns
      181 dpfkynnstg isyetlgpee lrsllttqcg visehtkkmc trslrcpqht deqrrtvriy
      241 flgpsavlpe vessldndsf dmtdsqalis rlqwdgssdl spsdsgsskt senqgwglgt
      301 nssesrktkk kkshlslvgt asglgsnkkk kpkppapptp siyddin
//
LOCUS       NP_001371769            1041 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein 4 isoform 95 [Homo sapiens].
ACCESSION   NP_001371769
VERSION     NP_001371769.1
DBSOURCE    REFSEQ: accession NM_001384840.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Thapa,N., Chen,M., Cryns,V.L. and Anderson,R.
  TITLE     A p85 isoform switch enhances PI3K activation on endosomes by a
            MAP4- and PI3P-dependent mechanism
  JOURNAL   Cell Rep 43 (5), 114119 (2024)
   PUBMED   38630589
  REMARK    GeneRIF: A p85 isoform switch enhances PI3K activation on endosomes
            by a MAP4- and PI3P-dependent mechanism.
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Xia,X., Ge,Y., Ge,F., Gu,P., Liu,Y., Li,P. and Xu,P.
  TITLE     MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma
  JOURNAL   J Cancer Res Clin Oncol 150 (2), 88 (2024)
   PUBMED   38341398
  REMARK    GeneRIF: MAP4 acts as an oncogene and prognostic marker and affects
            radioresistance by mediating epithelial-mesenchymal transition in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Nishida,K., Matsumura,K., Tamura,M., Nakamichi,T., Shimamori,K.,
            Kuragano,M., Kabir,A.M.R., Kakugo,A., Kotani,S., Nishishita,N. and
            Tokuraku,K.
  TITLE     Effects of three microtubule-associated proteins (MAP2, MAP4, and
            Tau) on microtubules' physical properties and neurite morphology
  JOURNAL   Sci Rep 13 (1), 8870 (2023)
   PUBMED   37258650
  REMARK    GeneRIF: Effects of three microtubule-associated proteins (MAP2,
            MAP4, and Tau) on microtubules' physical properties and neurite
            morphology.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1041)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1041)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1041)
  AUTHORS   Ookata,K., Hisanaga,S., Bulinski,J.C., Murofushi,H., Aizawa,H.,
            Itoh,T.J., Hotani,H., Okumura,E., Tachibana,K. and Kishimoto,T.
  TITLE     Cyclin B interaction with microtubule-associated protein 4 (MAP4)
            targets p34cdc2 kinase to microtubules and is a potential regulator
            of M-phase microtubule dynamics
  JOURNAL   J Cell Biol 128 (5), 849-862 (1995)
   PUBMED   7876309
REFERENCE   7  (residues 1 to 1041)
  AUTHORS   Chapin,S.J., Lue,C.M., Yu,M.T. and Bulinski,J.C.
  TITLE     Differential expression of alternatively spliced forms of MAP4: a
            repertoire of structurally different microtubule-binding domains
  JOURNAL   Biochemistry 34 (7), 2289-2301 (1995)
   PUBMED   7857940
REFERENCE   8  (residues 1 to 1041)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Microtubule stabilization by assembly-promoting
            microtubule-associated proteins: a repeat performance
  JOURNAL   Cell Motil Cytoskeleton 23 (4), 236-243 (1992)
   PUBMED   1477887
  REMARK    Review article
REFERENCE   9  (residues 1 to 1041)
  AUTHORS   West,R.R., Tenbarge,K.M. and Olmsted,J.B.
  TITLE     A model for microtubule-associated protein 4 structure. Domains
            defined by comparisons of human, mouse, and bovine sequences
  JOURNAL   J Biol Chem 266 (32), 21886-21896 (1991)
   PUBMED   1718985
REFERENCE   10 (residues 1 to 1041)
  AUTHORS   Chapin,S.J. and Bulinski,J.C.
  TITLE     Non-neuronal 210 x 10(3) Mr microtubule-associated protein (MAP4)
            contains a domain homologous to the microtubule-binding domains of
            neuronal MAP2 and tau
  JOURNAL   J Cell Sci 98 (Pt 1), 27-36 (1991)
   PUBMED   1905296
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124916.3 and AC139667.5.
            
            Summary: The protein encoded by this gene is a major non-neuronal
            microtubule-associated protein. This protein contains a domain
            similar to the microtubule-binding domains of neuronal
            microtubule-associated protein (MAP2) and microtubule-associated
            protein tau (MAPT/TAU). This protein promotes microtubule assembly,
            and has been shown to counteract destabilization of interphase
            microtubule catastrophe promotion. Cyclin B was found to interact
            with this protein, which targets cell division cycle 2 (CDC2)
            kinase to microtubules. The phosphorylation of this protein affects
            microtubule properties and cell cycle progression. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1041
                     /product="microtubule-associated protein 4 isoform 95"
                     /note="MAP-4"
                     /calculated_mol_wt=109652
     Region          <647..858
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <859..880
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          882..911
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          913..942
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     Region          944..974
                     /region_name="Tubulin-binding"
                     /note="Tau and MAP protein, tubulin-binding repeat;
                     pfam00418"
                     /db_xref="CDD:459807"
     CDS             1..1041
                     /gene="MAP4"
                     /coded_by="NM_001384840.1:96..3221"
                     /note="isoform 95 is encoded by transcript variant 92"
                     /db_xref="GeneID:4134"
                     /db_xref="HGNC:HGNC:6862"
                     /db_xref="MIM:157132"
ORIGIN      
        1 madlsladal tepspdiege ikrdfiatle aeafddvvge tvgktdyipl ldvdektgns
       61 eskkkpcset sqiedtpssk ptllangghg vegsdttgsp tefleekmay qeypnsqnwp
      121 edtnfcfqpe qvvdpiqtdp fkmyhdddla dlvfpssata dtsifagqnd plkdsygmsp
      181 cntavvpqgw svealnsphs esfvspeava eppqptavpl elakeiemas eerppaqale
      241 immglkttdm apsketemal akdmalatkt evalakdmes ptkldvtlak dmqpsmesdm
      301 alvkdmelpt ekevalvkdv rwptetdvss aknvvlptet evapakdvtl lketeraspi
      361 kmdlapskdm gppkenkket eraspikmdl apskdmgppk enkivpakdl vllseievaq
      421 andiisstei ssaekvalss etevalardm tlppetnvil tkdkalplea evapvkdmaq
      481 lpeteiapak dvapstvkev gllkdmspls etemalgkdv tpppetevvl iknvclppem
      541 evaltedqvp alkteaplak dgvltlannv tpakdvppls eteatpvpik dmeiaqtqkg
      601 isedshlesl qdvgqsaapt fmispetvtg tgkkcslpae edsvleklge rkpcnsqpse
      661 lssetsgiar peegrpvvsg tgndittppn kelppspekk tkpiadakap ekraspskpa
      721 sapasrsgsk stqtvakttt aaavastgps srspstllpk kptaiktegk paevkkmtak
      781 svpadlsrpk ststssmkkt ttlsgtapaa gvvpsrvkat pmpsrpsttp fidkkptsak
      841 pssttprlsr latntsapdl knvrskvgst enikhqpggg rvqivskkvs yshiqskcgs
      901 kdnikhvpgg gnvqiqnkkv diskvsskcg skanikhkpg ggdvkiesqk lnfkekaqak
      961 vgsldnvghl paggavkteg ggseaplcpg ppageepais eaapeagapt sasglnghpt
     1021 lsgggdqrea qtldsqiqet n
//
LOCUS       NP_001362661             408 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform iii [Homo sapiens].
ACCESSION   NP_001362661
VERSION     NP_001362661.1
DBSOURCE    REFSEQ: accession NM_001375732.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 408)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 408)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 408)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..408
                     /product="abl interactor 2 isoform iii"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=43716
     Region          39..100
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          <165..292
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          347..407
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(355,357,360,364,382..383,396,398..399)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..408
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375732.1:122..1348"
                     /note="isoform iii is encoded by transcript variant 66"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqt vdihkekvar reigilttnk
       61 ntsrthkiia panlerpvry irkpidytil ddighgvkwl lrfkvstqnm kmgglprttp
      121 ptqkppsppm sgkgtlgssg ssggshpssr sssrensgsg svgvpiavpt psppsvfpap
      181 agsagtpplp atsasapapl vpatvpssta pdaaaggaqt ladgftsptp pvvsstpptg
      241 hpvqfysmnr pasrhtppti ggslpyrrpp sitsqtslqn qmnggpfysq npvsdtpppp
      301 ppveepvfde sppppppped yeeeeaavve ysdpyaeedp pwaprsylek vvaiydytkd
      361 kedelsfqeg aiiyvikknd dgwyegvmng vtglfpgnyv esimhyse
//
LOCUS       NP_001371292            1748 aa            linear   PRI 21-NOV-2025
DEFINITION  RANBP2-like and GRIP domain-containing protein 5/6 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001371292 XP_011510068
VERSION     NP_001371292.1
DBSOURCE    REFSEQ: accession NM_001384363.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1748)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1748)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1748)
  AUTHORS   Sugis,E., Dauvillier,J., Leontjeva,A., Adler,P., Hindie,V.,
            Moncion,T., Collura,V., Daudin,R., Loe-Mie,Y., Herault,Y.,
            Lambert,J.C., Hermjakob,H., Pupko,T., Rain,J.C., Xenarios,I.,
            Vilo,J., Simonneau,M. and Peterson,H.
  TITLE     HENA, heterogeneous network-based data set for Alzheimer's disease
  JOURNAL   Sci Data 6 (1), 151 (2019)
   PUBMED   31413325
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1748)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 1748)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1748)
  AUTHORS   Dephoure,N., Zhou,C., Villen,J., Beausoleil,S.A., Bakalarski,C.E.,
            Elledge,S.J. and Gygi,S.P.
  TITLE     A quantitative atlas of mitotic phosphorylation
  JOURNAL   Proc Natl Acad Sci U S A 105 (31), 10762-10767 (2008)
   PUBMED   18669648
REFERENCE   7  (residues 1 to 1748)
  AUTHORS   Cantin,G.T., Yi,W., Lu,B., Park,S.K., Xu,T., Lee,J.D. and
            Yates,J.R. 3rd.
  TITLE     Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
            efficient phosphoproteomic analysis
  JOURNAL   J Proteome Res 7 (3), 1346-1351 (2008)
   PUBMED   18220336
REFERENCE   8  (residues 1 to 1748)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   9  (residues 1 to 1748)
  AUTHORS   Ciccarelli,F.D., von Mering,C., Suyama,M., Harrington,E.D.,
            Izaurralde,E. and Bork,P.
  TITLE     Complex genomic rearrangements lead to novel primate gene function
  JOURNAL   Genome Res 15 (3), 343-351 (2005)
   PUBMED   15710750
REFERENCE   10 (residues 1 to 1748)
  AUTHORS   Nothwang,H.G., Rensing,C., Kubler,M., Denich,D., Brandl,B.,
            Stubanus,M., Haaf,T., Kurnit,D. and Hildebrandt,F.
  TITLE     Identification of a novel Ran binding protein 2 related gene
            (RANBP2L1) and detection of a gene cluster on human chromosome
            2q11-q12
  JOURNAL   Genomics 47 (3), 383-392 (1998)
   PUBMED   9480752
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC226101.3 and AC108938.3.
            
            On Jun 18, 2020 this sequence version replaced XP_011510068.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.257579.1,
                                           SRR18074967.2260679.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1748
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..1748
                     /product="RANBP2-like and GRIP domain-containing protein
                     5/6 isoform 4"
                     /note="RANBP2-like and GRIP domain-containing protein 7;
                     RANBP2-like and GRIP domain-containing protein 5/6;
                     ranBP2-like 1/2; ran-binding protein 2-like 1/2"
                     /calculated_mol_wt=196835
     Region          <16..205
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(17..18,20,44,47..48,51..52,54..55,78,81..82,85..86,
                     89)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          42..72
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1034..1150
                     /region_name="RanBD2_RanBP2-like"
                     /note="Ran-binding protein 2, Ran binding domain repeat 2;
                     cd13177"
                     /db_xref="CDD:269998"
     Site            order(1048,1050..1052,1057..1062,1079,1081,1083..1084,
                     1086,1088..1090,1093,1095,1099,1103,1113,1115,1128,1132)
                     /site_type="other"
                     /note="putative RAN binding site [polypeptide binding]"
                     /db_xref="CDD:269998"
     Region          1331..1447
                     /region_name="RanBD3_RanBP2-like"
                     /note="Ran-binding protein 2, Ran binding domain repeat 3;
                     cd14685"
                     /db_xref="CDD:270204"
     Site            order(1345,1347..1349,1354..1359,1376,1378,1380..1381,
                     1383,1385..1387,1390,1392,1396,1400,1410,1412,1425,1429)
                     /site_type="other"
                     /note="putative RAN binding site [polypeptide binding]"
                     /db_xref="CDD:270204"
     Region          1624..1688
                     /region_name="Rab_bind"
                     /note="Rab binding domain; pfam16704"
                     /db_xref="CDD:435531"
     Region          1689..1732
                     /region_name="GRIP"
                     /note="GRIP domain; pfam01465"
                     /db_xref="CDD:460221"
     CDS             1..1748
                     /gene="RGPD6"
                     /gene_synonym="RanBP2L1; RanBP2L2; RGP6; RGPD7"
                     /coded_by="NM_001384363.1:106..5352"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS92839.1"
                     /db_xref="GeneID:729540"
                     /db_xref="HGNC:HGNC:32419"
                     /db_xref="MIM:612709"
ORIGIN      
        1 mgprvtvksm kgfyfaklyy eakeydlakk yictyinvqe rdpkahrflg llyeleente
       61 kavecyrrsv elnptqkdlv lkiaellckn dvtdgrakyw veraaklfpg spaiyklkeq
      121 lldcegedgw nklfdliqse lyvrpddvhv nirlvelyrs tkrlkdavah cheaernial
      181 rsslewnscv vqtlkeyles lqclesdksd wqatntdlll ayanlmlltl strdvqenre
      241 llesfdsalq saksslggnd elsatflemk ghfymyagsl llkmgqhgnn vqwralsela
      301 alcyliafqv prpkiklreg kagqnllemm acdrlsqsgh mllslsrgkq dflkevvetf
      361 ankigqsaly dalfssqspk dtsflgsddi gkidvqepel edlarydvga irahngslqh
      421 ltwlglqwns lpalpgirkw lkqlfhrlph etsrletnap esicildlev fllgvvytsh
      481 lqlkekcnsh hssyqplclp fpvckqlcte rqkswwdavc tlihrkavpg nlaklrllvq
      541 heintlraqe khglqpallv hwakylqktg sglnsfygql eyigrsvhyw kkvlpllkii
      601 kknsipepid plfkhfhsvd iqaseiveye edahitfaml davngnieda vtafesiksv
      661 vsywnlalif hrkaediend alspeeqeec rnyltktrdy likiiddgds nlsvvkklpv
      721 plesvkqmln svmqeledys eggplykngs lrnadseikh stpsptkysl spsksykysp
      781 etpprwtedr nsllnmicqq veaikkemqe lklnssksas rhrwptenyg pdsvpdgyqg
      841 sqtfhgaplt vattgpsvyy sqspaynsqy llrpaanvtp tkgssntefk stkegfsipv
      901 sadgfkfgis epgnqekkre kplendtgfq aqdisgrkkg rgvifgqtss tftfadvaks
      961 tsgegfqfgk kdlnfkgfsg ageklfssry gkmankants gdfekddday ktedsddihf
     1021 epvvqmpekv elvtgeegek vlysqgvklf rfdaevrqwk erglgnlkil knevngklrm
     1081 lmrreqvlkv canhwitttm nlkplsgsdr awmwsasdfs dgdaklerla akfktpelae
     1141 efkqkfeecq rllldiplqt phklvdtgra akliqraeem ksglkdfktf ltndqtkvte
     1201 eenkgsgtga agasdttikp naentgptle wdnydlreda lddsvssssv hasplasspv
     1261 rknlfrfdes ttgsnfsfks alslskspak lnqsgtsvgt deesvvtqee erdgqyfepv
     1321 vplpdlvevs sgeeneqvvf shraeiyryd kdvgqwkerg igdikilqny dnkqvrivmr
     1381 rdqvlklcan hritpdmslq nmkgtervwv wtacdfadge rkvehlavrf klqdvadsfk
     1441 kifdeaktaq ekdslitphv srsstpresp cgkiavaile ettrertdvi qgddvadaas
     1501 evevsstset ttkavvsppk fvfvsesvkr ifssekskpf vfgnssatgs lfgfsfnapl
     1561 ksnnsetssv aqsgseskve pkkcelskns dieqssdskv knlsasfpte essinytfkt
     1621 pekepplwha eftkeelvqk lrsttksadh lngllreiea tnavlmeqik llkseirrle
     1681 rnqereksaa nleylknvll qfiflkpgse rerllpvint mlqlspeekg klaavaqdee
     1741 enasrssg
//
LOCUS       NP_001350774             856 aa            linear   PRI 21-NOV-2025
DEFINITION  neuronal-specific septin-3 isoform C [Homo sapiens].
ACCESSION   NP_001350774 XP_016884351
VERSION     NP_001350774.1
DBSOURCE    REFSEQ: accession NM_001363845.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 856)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 856)
  AUTHORS   Toth,V., Vadaszi,H., Ravasz,L., Mittli,D., Matyas,D., Molnar,T.,
            Micsonai,A., Szaniszlo,T., Lorincz,P., Kovacs,R.A., Juhasz,T.,
            Beke-Somfai,T., Juhasz,G., Gyorffy,B.A., Kekesi,K.A. and Kardos,J.
  TITLE     Neuronal-specific septin-3 binds Atg8/LC3B, accumulates and
            localizes to autophagosomes during induced autophagy
  JOURNAL   Cell Mol Life Sci 79 (9), 471 (2022)
   PUBMED   35932293
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 856)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 856)
  AUTHORS   Fischer,M., Frank,D., Rosler,R., Johnsson,N. and Gronemeyer,T.
  TITLE     Biochemical Characterization of a Human Septin Octamer
  JOURNAL   Front Cell Dev Biol 10, 771388 (2022)
   PUBMED   35309913
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 856)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 856)
  AUTHORS   Xue,J., Milburn,P.J., Hanna,B.T., Graham,M.E., Rostas,J.A. and
            Robinson,P.J.
  TITLE     Phosphorylation of septin 3 on Ser-91 by cGMP-dependent protein
            kinase-I in nerve terminals
  JOURNAL   Biochem J 381 (Pt 3), 753-760 (2004)
   PUBMED   15107017
REFERENCE   7  (residues 1 to 856)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   8  (residues 1 to 856)
  AUTHORS   Takehashi,M., Alioto,T., Stedeford,T., Persad,A.S., Banasik,M.,
            Masliah,E., Tanaka,S. and Ueda,K.
  TITLE     Septin 3 gene polymorphism in Alzheimer's disease
  JOURNAL   Gene Expr 11 (5-6), 263-270 (2004)
   PUBMED   15200238
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 856)
  AUTHORS   Methner,A., Leypoldt,F., Joost,P. and Lewerenz,J.
  TITLE     Human septin 3 on chromosome 22q13.2 is upregulated by neuronal
            differentiation
  JOURNAL   Biochem Biophys Res Commun 283 (1), 48-56 (2001)
   PUBMED   11322766
REFERENCE   10 (residues 1 to 856)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z99716.4.
            
            On Jun 3, 2018 this sequence version replaced XP_016884351.1.
            
            Summary: This gene belongs to the septin family of GTPases. Members
            of this family are required for cytokinesis. Expression is
            upregulated by retinoic acid in a human teratocarcinoma cell line.
            The specific function of this gene has not been determined.
            Alternative splicing of this gene results in several transcript
            variants encoding different isoforms. [provided by RefSeq, May
            2018].
            
            Transcript Variant: This variant (C) represents the longest
            transcript and encodes the longest isoform (C).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.159373.1,
                                           SRR1803612.151034.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000644076.2/ ENSP00000494051.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..856
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..856
                     /product="neuronal-specific septin-3 isoform C"
                     /note="neuronal-specific septin-3"
                     /calculated_mol_wt=92237
     Region          557..831
                     /region_name="CDC_Septin"
                     /note="CDC/Septin GTPase family; cd01850"
                     /db_xref="CDD:206649"
     Site            566..573
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206649"
     Site            order(568..574,623,626,705..706,708,763..764)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206649"
     Site            598..606
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206649"
     Site            600
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206649"
     Site            623..626
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            625..671
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Site            705..708
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            763..765
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     CDS             1..856
                     /gene="SEPTIN3"
                     /gene_synonym="bK250D10.3; SEP3; SEPT3"
                     /coded_by="NM_001363845.2:255..2825"
                     /note="isoform C is encoded by transcript variant C"
                     /db_xref="CCDS:CCDS87030.1"
                     /db_xref="GeneID:55964"
                     /db_xref="HGNC:HGNC:10750"
                     /db_xref="MIM:608314"
ORIGIN      
        1 mdhnfapapp emqshgapgp gtsfshshvl grpirpsrlp gggspltpvl rktihldtfp
       61 qshipqtssr lglgartrsv ppqetgialg aslsplptss lvprklssis ltlhqnsqar
      121 sldrplshwe elptpgkkaa pheggrvssp gsppvtlvpg grvhsegpgn pgltksnrml
      181 atekplvssy lalpfqsrla qsapvlaepg slgqghlvsv tdhmptrasp gkgkprargi
      241 prprgrlqra nttvnltamd trtdaarhla tmatnrpsla inlatpntsq ldtgtefpal
      301 diklgtardl ssvgtvksgk tvnlatagti kpgtamnltt vgttkpgmvm dliasepdkl
      361 gkamatrsta kpdmttegia mdsatsdpvk pdtitatvgt srletamala rvnraklgta
      421 knslaldtsr mgtavgsvvp vtpdpatgkt tlgsvnnlti sdvatcllmp srstdlaldn
      481 tnaamdrate pasldlatey kglpetrtda amselvpepr pkpavpmkpm sinsnllgyi
      541 gidtiieqmr kktmktgfdf nimvvgqsgl gkstlvntlf ksqvsrkass wnreekipkt
      601 veikaighvi eeggvkmklt vidtpgfgdq innencwepi ekyineqyek flkeevniar
      661 kkripdtrvh cclyfisptg hslrpldlef mkhlskvvni ipviakadtm tleeksefkq
      721 rvrkelevng iefypqkefd edledktend kirqesmpfa vvgsdkeyqv ngkrvlgrkt
      781 pwgiievenl nhcefallrd fvirthlqdl kevthnihye tyrakrlndn gglppgegll
      841 gtvlppvpat pcptae
//
LOCUS       NP_001071172             433 aa            linear   PRI 21-NOV-2025
DEFINITION  mesoderm induction early response protein 1 isoform f [Homo
            sapiens].
ACCESSION   NP_001071172
VERSION     NP_001071172.1
DBSOURCE    REFSEQ: accession NM_001077704.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Wang,S., Fairall,L., Pham,T.K., Ragan,T.J., Vashi,D., Collins,M.O.,
            Dominguez,C. and Schwabe,J.W.R.
  TITLE     A potential histone-chaperone activity for the MIER1 histone
            deacetylase complex
  JOURNAL   Nucleic Acids Res 51 (12), 6006-6019 (2023)
   PUBMED   37099381
  REMARK    GeneRIF: A potential histone-chaperone activity for the MIER1
            histone deacetylase complex.
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 433)
  AUTHORS   McCarthy,P.L., Mercer,F.C., Savicky,M.W., Carter,B.A., Paterno,G.D.
            and Gillespie,L.L.
  TITLE     Changes in subcellular localisation of MI-ER1 alpha, a novel
            oestrogen receptor-alpha interacting protein, is associated with
            breast cancer progression
  JOURNAL   Br J Cancer 99 (4), 639-646 (2008)
   PUBMED   18665173
  REMARK    GeneRIF: Loss of nuclear MI-ER1 alpha might contribute to the
            development of invasive breast carcinoma
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Wang,L., Charroux,B., Kerridge,S. and Tsai,C.C.
  TITLE     Atrophin recruits HDAC1/2 and G9a to modify histone H3K9 and to
            determine cell fates
  JOURNAL   EMBO Rep 9 (6), 555-562 (2008)
   PUBMED   18451879
REFERENCE   7  (residues 1 to 433)
  AUTHORS   Ding,Z., Gillespie,L.L., Mercer,F.C. and Paterno,G.D.
  TITLE     The SANT domain of human MI-ER1 interacts with Sp1 to interfere
            with GC box recognition and repress transcription from its own
            promoter
  JOURNAL   J Biol Chem 279 (27), 28009-28016 (2004)
   PUBMED   15117948
  REMARK    GeneRIF: the association of hMI-ER1 with Sp1 represents a novel
            mechanism for the negative regulation of Sp1 target promoters
REFERENCE   8  (residues 1 to 433)
  AUTHORS   Ding,Z., Gillespie,L.L. and Paterno,G.D.
  TITLE     Human MI-ER1 alpha and beta function as transcriptional repressors
            by recruitment of histone deacetylase 1 to their conserved ELM2
            domain
  JOURNAL   Mol Cell Biol 23 (1), 250-258 (2003)
   PUBMED   12482978
  REMARK    GeneRIF: we investigated the role of hMI-ER1alpha and hMI-ER1beta
            in the regulation of transcription.We demonstrate that this
            repressor activity is due to interaction and recruitment of a
            trichostatin A-sensitive histone deacetylase 1 (HDAC1).
REFERENCE   9  (residues 1 to 433)
  AUTHORS   Paterno,G.D., Ding,Z., Lew,Y.Y., Nash,G.W., Mercer,F.C. and
            Gillespie,L.L.
  TITLE     Genomic organization of the human mi-er1 gene and characterization
            of alternatively spliced isoforms: regulated use of a facultative
            intron determines subcellular localization
  JOURNAL   Gene 295 (1), 79-88 (2002)
   PUBMED   12242014
  REMARK    GeneRIF: Results demonstrate that alternate use of a facultative
            intron regulates the subcellular localization of hMI-ER1 proteins
            and this may have important implications for hMI-ER1 function.
REFERENCE   10 (residues 1 to 433)
  AUTHORS   Paterno,G.D., Mercer,F.C., Chayter,J.J., Yang,X., Robb,J.D. and
            Gillespie,L.L.
  TITLE     Molecular cloning of human er1 cDNA and its differential expression
            in breast tumours and tumour-derived cell lines
  JOURNAL   Gene 222 (1), 77-82 (1998)
   PUBMED   9813250
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY124188.1, AL500525.4 and
            BM987758.1.
            
            Summary: This gene encodes a protein that was first identified in
            Xenopus laevis by its role in a mesoderm induction early response
            (MIER). The encoded protein functions as a transcriptional
            regulator. Alternatively spliced transcript variants encode
            multiple isoforms, some of which lack a C-terminal nuclear
            localization signal. [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (6) differs in the 5' UTR, lacks a
            portion of the 5' coding region, initiates translation at an
            alternate start codon, and lacks an alternate segment in the 3'
            coding region, compared to variant 1. The resulting isoform (f,
            also known as N3-alpha), has shorter and distinct N- and C-termini,
            compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.235428.1,
                                           SRR1803614.146574.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..433
                     /product="mesoderm induction early response protein 1
                     isoform f"
                     /note="mesoderm induction early response protein 1;
                     mesoderm induction early response 1 homolog; mesoderm
                     induction early response 1, transcriptional regulator"
                     /calculated_mol_wt=48967
     Region          1..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N108.2)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8N108.2)"
     Region          75..173
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N108.2)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N108.2)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8N108.2)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q8N108.2)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8N108.2)"
     Region          180..284
                     /region_name="Interaction with HDAC1.
                     /evidence=ECO:0000269|PubMed:12482978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N108.2)"
     Region          182..231
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          288..332
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(288,318..319,321..322,324..326,328..330)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          342..>407
                     /region_name="MIER1_3_C"
                     /note="Mesoderm induction early response protein 1/3
                     C-terminal; pfam19426"
                     /db_xref="CDD:437258"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N108.2)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N108.2)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8N108.2)"
     CDS             1..433
                     /gene="MIER1"
                     /gene_synonym="ER1; MI-ER1"
                     /coded_by="NM_001077704.3:137..1438"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS41347.1"
                     /db_xref="GeneID:57708"
                     /db_xref="HGNC:HGNC:29657"
                     /db_xref="MIM:616848"
ORIGIN      
        1 maepsvesss pggsatsddh efdpsadmlv hdfddertle eeemmegetn fsseiedlar
       61 egdmpihell slygygstvr lpeedeeeee eeeegedded adnddnsgcs genkeenikd
      121 ssgqedetqs snddpsqsva sqdaqeiirp rrckyfdtns eveeeseede dyipsedwkk
      181 eimvgsmfqa eipvgicryk enekvyendd qllwdpeylp edkviiflkd asrrtgdekg
      241 veaipegshi kdneqalyel vkcnfdteea lrrlrfnvka areelsvwte eecrnfeqgl
      301 kaygkdfhli qankvrtrsv gecvafyymw kkserydffa qqtrfgkkky nlhpgvtdym
      361 drlldesesa assrapsppp tasnssnsqs ekedgtvsta nqngvssngp gilqmllpvh
      421 fsaissrana flk
//
LOCUS       NP_001269837             497 aa            linear   PRI 21-NOV-2025
DEFINITION  T-complex protein 1 subunit theta isoform 3 [Homo sapiens].
ACCESSION   NP_001269837 XP_005260973
VERSION     NP_001269837.1
DBSOURCE    REFSEQ: accession NM_001282908.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Gestaut,D., Roh,S.H., Ma,B., Pintilie,G., Joachimiak,L.A.,
            Leitner,A., Walzthoeni,T., Aebersold,R., Chiu,W. and Frydman,J.
  TITLE     The Chaperonin TRiC/CCT Associates with Prefoldin through a
            Conserved Electrostatic Interface Essential for Cellular
            Proteostasis
  JOURNAL   Cell 177 (3), 751-765 (2019)
   PUBMED   30955883
REFERENCE   5  (residues 1 to 497)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   6  (residues 1 to 497)
  AUTHORS   Yokota,S., Yanagi,H., Yura,T. and Kubota,H.
  TITLE     Cytosolic chaperonin-containing t-complex polypeptide 1 changes the
            content of a particular subunit species concomitant with substrate
            binding and folding activities during the cell cycle
  JOURNAL   Eur J Biochem 268 (17), 4664-4673 (2001)
   PUBMED   11532003
REFERENCE   7  (residues 1 to 497)
  AUTHORS   Hynes,G.M. and Willison,K.R.
  TITLE     Individual subunits of the eukaryotic cytosolic chaperonin mediate
            interactions with binding sites located on subdomains of beta-actin
  JOURNAL   J Biol Chem 275 (25), 18985-18994 (2000)
   PUBMED   10748209
REFERENCE   8  (residues 1 to 497)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   9  (residues 1 to 497)
  AUTHORS   Yamazaki,M., Ono,A., Watanabe,K., Sasaki,K., Tashiro,H. and
            Nomura,T.
  TITLE     Nucleotide sequence surrounding the locus marker D21S246 on human
            chromosome 21
  JOURNAL   DNA Res 2 (4), 187-189 (1995)
   PUBMED   8590283
REFERENCE   10 (residues 1 to 497)
  AUTHORS   Kubota,H., Hynes,G. and Willison,K.
  TITLE     The eighth Cct gene, Cctq, encoding the theta subunit of the
            cytosolic chaperonin containing TCP-1
  JOURNAL   Gene 154 (2), 231-236 (1995)
   PUBMED   7890169
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP248736.1 and BC012584.1.
            
            On Nov 5, 2013 this sequence version replaced XP_005260973.1.
            
            Summary: This gene encodes the theta subunit of the CCT chaperonin,
            which is abundant in the eukaryotic cytosol and may be involved in
            the transport and assembly of newly synthesized proteins.
            Alternative splicing results in multiple transcript variants of
            this gene. A pseudogene related to this gene is located on
            chromosome 1. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (3) uses an alternate splice site
            in the 5' coding region and initiates translation at a downstream
            start codon, compared to variant 1. It encodes isoform 3 which has
            a shorter N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012584.1, SRR14038193.2543627.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..497
                     /product="T-complex protein 1 subunit theta isoform 3"
                     /note="T-complex protein 1 subunit theta; CCT-theta;
                     TCP-1-theta; renal carcinoma antigen NY-REN-15; chaperonin
                     containing TCP1, subunit 8 (theta); chaperonin containing
                     T-complex polypeptide 1 subunit 8"
                     /calculated_mol_wt=53975
     Region          1..488
                     /region_name="chaperonin_like"
                     /note="chaperonin_like superfamily. Chaperonins are
                     involved in productive folding of proteins. They share a
                     common general morphology, a double toroid of 2 stacked
                     rings, each composed of 7-9 subunits. There are 2 main
                     chaperonin groups. The symmetry of type I...; cl02777"
                     /db_xref="CDD:351886"
     Site            order(1..4,6,24,26,30,34,37,331,469..475)
                     /site_type="other"
                     /note="ring oligomerisation interface [polypeptide
                     binding]"
                     /db_xref="CDD:239457"
     Site            order(381,399,408,410..411,414)
                     /site_type="active"
                     /note="stacking interactions [active]"
                     /db_xref="CDD:239457"
     CDS             1..497
                     /gene="CCT8"
                     /gene_synonym="C21orf112; Cctq; D21S246; PRED71"
                     /coded_by="NM_001282908.2:237..1730"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:10694"
                     /db_xref="HGNC:HGNC:1623"
                     /db_xref="MIM:617786"
ORIGIN      
        1 mnkmvinhle klfvtndaat ilrelevqhp aakmivmash mqeqevgdgt nfvlvfagal
       61 lelaeellri glsvsevieg yeiacrkahe ilpnlvccsa knlrdidevs sllrtsimsk
      121 qygnevflak liaqacvsif pdsghfnvdn irvckilgsg issssvlhgm vfkketegdv
      181 tsvkdakiav yscpfdgmit etkgtvlikt aeelmnfskg eenlmdaqvk aiadtganvv
      241 vtggkvadma lhyankynim lvrlnskwdl rrlcktvgat alprltppvl eemghcdsvy
      301 lsevgdtqvv vfkhekedga istivlrgst dnlmddiera vddgvntfkv ltrdkrlvpg
      361 ggateielak qitsygetcp gleqyaikkf aeafeaipra laensgvkan evisklyavh
      421 qegnknvgld ieaevpavkd mleagildty lgkywaikla tnaavtvlrv dqiimakpag
      481 gpkppsgkkd wdddqnd
//
LOCUS       NP_001362951             655 aa            linear   PRI 21-NOV-2025
DEFINITION  protein 4.1 isoform 15 [Homo sapiens].
ACCESSION   NP_001362951
VERSION     NP_001362951.1
DBSOURCE    REFSEQ: accession NM_001376022.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Terada,N., Saitoh,Y., Saito,M., Yamada,T., Kamijo,A., Yoshizawa,T.
            and Sakamoto,T.
  TITLE     Recent Progress on Genetically Modified Animal Models for Membrane
            Skeletal Proteins: The 4.1 and MPP Families
  JOURNAL   Genes (Basel) 14 (10), 1942 (2023)
   PUBMED   37895291
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 655)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Dalla Venezia,N., Gilsanz,F., Alloisio,N., Ducluzeau,M.T.,
            Benz,E.J. Jr. and Delaunay,J.
  TITLE     Homozygous 4.1(-) hereditary elliptocytosis associated with a point
            mutation in the downstream initiation codon of protein 4.1 gene
  JOURNAL   J Clin Invest 90 (5), 1713-1717 (1992)
   PUBMED   1430200
REFERENCE   7  (residues 1 to 655)
  AUTHORS   Jons,T. and Drenckhahn,D.
  TITLE     Identification of the binding interface involved in linkage of
            cytoskeletal protein 4.1 to the erythrocyte anion exchanger
  JOURNAL   EMBO J 11 (8), 2863-2867 (1992)
   PUBMED   1639060
REFERENCE   8  (residues 1 to 655)
  AUTHORS   Subrahmanyam,G., Bertics,P.J. and Anderson,R.A.
  TITLE     Phosphorylation of protein 4.1 on tyrosine-418 modulates its
            function in vitro
  JOURNAL   Proc Natl Acad Sci U S A 88 (12), 5222-5226 (1991)
   PUBMED   1647028
REFERENCE   9  (residues 1 to 655)
  AUTHORS   Conboy,J.G., Chan,J.Y., Chasis,J.A., Kan,Y.W. and Mohandas,N.
  TITLE     Tissue- and development-specific alternative RNA splicing regulates
            expression of multiple isoforms of erythroid membrane protein 4.1
  JOURNAL   J Biol Chem 266 (13), 8273-8280 (1991)
   PUBMED   2022644
REFERENCE   10 (residues 1 to 655)
  AUTHORS   Horne,W.C., Prinz,W.C. and Tang,E.K.
  TITLE     Identification of two cAMP-dependent phosphorylation sites on
            erythrocyte protein 4.1
  JOURNAL   Biochim Biophys Acta 1055 (1), 87-92 (1990)
   PUBMED   2171679
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL009181.1, AL138785.8 and
            AL357500.17.
            
            Summary: The protein encoded by this gene, together with spectrin
            and actin, constitute the red cell membrane cytoskeletal network.
            This complex plays a critical role in erythrocyte shape and
            deformability. Mutations in this gene are associated with type 1
            elliptocytosis (EL1). Alternatively spliced transcript variants
            encoding different isoforms have been described for this
            gene.[provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1477809.1,
                                           SRR14038193.1444717.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.3"
     Protein         1..655
                     /product="protein 4.1 isoform 15"
                     /note="protein 4.1; erythrocyte surface protein band 4.1;
                     P4.1; EPB4.1; elliptocytosis 1, RH-linked"
                     /calculated_mol_wt=73538
     Region          2..192
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          187..280
                     /region_name="FERM_C_4_1_family"
                     /note="FERM domain C-lobe of Protein 4.1 family; cd13184"
                     /db_xref="CDD:270005"
     Site            order(196,213,215,221)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270005"
     Site            order(225,230..233,268,272,275..276)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Site            268..279
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270005"
     Region          290..333
                     /region_name="FA"
                     /note="FERM adjacent (FA); pfam08736"
                     /db_xref="CDD:462582"
     Region          458..506
                     /region_name="SAB"
                     /note="SAB domain; pfam04382"
                     /db_xref="CDD:461285"
     Region          544..651
                     /region_name="4_1_CTD"
                     /note="4.1 protein C-terminal domain (CTD); pfam05902"
                     /db_xref="CDD:461774"
     CDS             1..655
                     /gene="EPB41"
                     /gene_synonym="4.1R; EL1; HE"
                     /coded_by="NM_001376022.1:729..2696"
                     /note="isoform 15 is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS90901.1"
                     /db_xref="GeneID:2035"
                     /db_xref="HGNC:HGNC:3377"
                     /db_xref="MIM:130500"
ORIGIN      
        1 mhckvslldd tvyecvvekh akgqdllkrv cehlnlleed yfglaiwdna tsktwldsak
       61 eikkqvrgvp wnftfnvkfy ppdpaqlted itryylclql rqdivagrlp csfatlallg
      121 sytiqselgd ydpelhgvdy vsdfklapnq tkeleekvme lhksyrsmtp aqadleflen
      181 akklsmygvd lhkakdlegv diilgvcssg llvykdklri nrfpwpkvlk isykrssffi
      241 kirpgeqeqy estigfklps yraakklwkv cvehhtffrl tstdtipksk flalgskfry
      301 sgrtqaqtrq asalidrpap hfertaskra srsldgaaav dsadrsprpt sapaitqgqv
      361 aeggvldasa kktvvpkaqk etvkaevkke deppeqaepe pteawkvekt hievtvptsn
      421 gdqtqklaek tedlirmrkk krerldgeni yirhsnlmle dldksqeeik khhasiselk
      481 knfmesvpep rpsewdkrls thspfrtlni ngqiptgegp plvktqtvti sdnanavkse
      541 iptkdvpivh tetktityea aqtddnsgdl dpgvlltaqt itsetpsstt ttqitktvkg
      601 gisetriekr ivitgdadid hdqvlvqaik eakeqhpdms vtkvvvhqet eiade
//
LOCUS       NP_003832                259 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 10C precursor
            [Homo sapiens].
ACCESSION   NP_003832
VERSION     NP_003832.3
DBSOURCE    REFSEQ: accession NM_003841.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Suehiro,Y., Tsuge,M., Kurihara,M., Uchida,T., Fujino,H., Ono,A.,
            Yamauchi,M., Naswa Makokha,G., Nakahara,T., Murakami,E.,
            Abe-Chayama,H., Kawaoka,T., Miki,D., Imamura,M., Aikata,H., Nelson
            Hayes,C., Fujita,T. and Chayama,K.
  TITLE     Hepatitis B Virus (HBV) Upregulates TRAIL-R3 Expression in
            Hepatocytes Resulting in Escape From Both Cell Apoptosis and
            Suppression of HBV Replication by TRAIL
  JOURNAL   J Infect Dis 227 (5), 686-695 (2023)
   PUBMED   35226068
  REMARK    GeneRIF: Hepatitis B Virus (HBV) Upregulates TRAIL-R3 Expression in
            Hepatocytes Resulting in Escape From Both Cell Apoptosis and
            Suppression of HBV Replication by TRAIL.
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Singh,D., Prasad,C.B., Biswas,D., Tewari,M., Kar,A.G., Ansari,M.A.,
            Singh,S. and Narayan,G.
  TITLE     TRAIL receptors are differentially regulated and clinically
            significant in gallbladder cancer
  JOURNAL   Pathology 52 (3), 348-358 (2020)
   PUBMED   32111400
  REMARK    GeneRIF: TRAIL receptors are differentially regulated and
            clinically significant in gallbladder cancer.
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Ruiz de Almodovar,C., Lopez-Rivas,A., Redondo,J.M. and Rodriguez,A.
  TITLE     Transcription initiation sites and promoter structure of the human
            TRAIL-R3 gene
  JOURNAL   FEBS Lett 531 (2), 304-308 (2002)
   PUBMED   12417331
  REMARK    GeneRIF: analysis of the transcription initiation sites and
            promoter structure of the TRAIL-R3 gene
REFERENCE   7  (residues 1 to 259)
  AUTHORS   MacFarlane,M., Ahmad,M., Srinivasula,S.M., Fernandes-Alnemri,T.,
            Cohen,G.M. and Alnemri,E.S.
  TITLE     Identification and molecular cloning of two novel receptors for the
            cytotoxic ligand TRAIL
  JOURNAL   J Biol Chem 272 (41), 25417-25420 (1997)
   PUBMED   9325248
REFERENCE   8  (residues 1 to 259)
  AUTHORS   Degli-Esposti,M.A., Smolak,P.J., Walczak,H., Waugh,J., Huang,C.P.,
            DuBose,R.F., Goodwin,R.G. and Smith,C.A.
  TITLE     Cloning and characterization of TRAIL-R3, a novel member of the
            emerging TRAIL receptor family
  JOURNAL   J Exp Med 186 (7), 1165-1170 (1997)
   PUBMED   9314565
REFERENCE   9  (residues 1 to 259)
  AUTHORS   Sheridan,J.P., Marsters,S.A., Pitti,R.M., Gurney,A., Skubatch,M.,
            Baldwin,D., Ramakrishnan,L., Gray,C.L., Baker,K., Wood,W.I.,
            Goddard,A.D., Godowski,P. and Ashkenazi,A.
  TITLE     Control of TRAIL-induced apoptosis by a family of signaling and
            decoy receptors
  JOURNAL   Science 277 (5327), 818-821 (1997)
   PUBMED   9242611
REFERENCE   10 (residues 1 to 259)
  AUTHORS   Pan,G., Ni,J., Wei,Y.F., Yu,G., Gentz,R. and Dixit,V.M.
  TITLE     An antagonist decoy receptor and a death domain-containing receptor
            for TRAIL
  JOURNAL   Science 277 (5327), 815-818 (1997)
   PUBMED   9242610
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107959.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 30, 2019 this sequence version replaced NP_003832.2.
            
            Summary: The protein encoded by this gene is a member of the
            TNF-receptor superfamily. This receptor contains an extracellular
            TRAIL-binding domain and a transmembrane domain, but no cytoplasmic
            death domain. This receptor is not capable of inducing apoptosis,
            and is thought to function as an antagonistic receptor that
            protects cells from TRAIL-induced apoptosis. This gene was found to
            be a p53-regulated DNA damage-inducible gene. The expression of
            this gene was detected in many normal tissues but not in most
            cancer cell lines, which may explain the specific sensitivity of
            cancer cells to the apoptosis-inducing activity of TRAIL. [provided
            by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            CCDS Note: This CCDS representation uses a downstream AUG start
            codon. This start codon has a strong Kozak signal and is restricted
            to human. An upstream start codon, which has a weak Kozak signal
            and is conserved in some other primates, is also present. The use
            of the upstream start codon would result in a protein that is 40 aa
            longer at the N-terminus. However, this would eliminate a signal
            peptide that is predicted for the shorter but not the longer
            N-terminus. PMID:9242611 shows experimental evidence for cleavage
            of a signal peptide following aa 25 from the downstream start, and
            this is also confirmed in PMID:15340161. Therefore, the downstream
            start codon is represented for this CCDS.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017852.1, AF014794.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000356864.4/
                                                ENSP00000349324.4
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..259
                     /product="tumor necrosis factor receptor superfamily
                     member 10C precursor"
                     /note="decoy receptor 1; lymphocyte inhibitor of TRAIL;
                     antagonist decoy receptor for TRAIL/Apo-2L; cytotoxic
                     TRAIL receptor-3; decoy TRAIL receptor without death
                     domain; TNF-related apoptosis-inducing ligand receptor 3;
                     tumor necrosis factor receptor superfamily, member 10c,
                     decoy without an intracellular domain"
                     /calculated_mol_wt=24683
     sig_peptide     1..25
                     /note="/evidence=ECO:0000269|PubMed:15340161,
                     ECO:0000269|PubMed:9242611; propagated from
                     UniProtKB/Swiss-Prot (O14798.3)"
                     /calculated_mol_wt=2742
     mat_peptide     26..236
                     /product="Tumor necrosis factor receptor superfamily
                     member 10C. /id=PRO_0000034582"
                     /note="propagated from UniProtKB/Swiss-Prot (O14798.3)"
                     /calculated_mol_wt=22199
     Region          29..66
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14798.3)"
     Region          30..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14798.3)"
     Region          50..150
                     /region_name="TNFRSF10"
                     /note="Tumor necrosis factor receptor superfamily member
                     10 (TNFRSF10), includes TNFRSF10A (DR4), TNFRSF10B (DR5),
                     TNFRSF10C (DcR1) and TNFRSF10D (DcR2); cd10580"
                     /db_xref="CDD:276906"
     Site            order(50..52,59,61,78..79,81..84,86..87,126,146)
                     /site_type="other"
                     /note="Antibody binding [polypeptide binding]"
                     /db_xref="CDD:276906"
     Region          50..66
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276906"
     Region          69..109
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276906"
     Region          69..109
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14798.3)"
     Site            77
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (high mannose) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O14798.3)"
     Site            order(84,87,92,123..127)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:276906"
     Region          110..149
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14798.3)"
     Region          111..149
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276906"
     Site            140
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (high mannose) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O14798.3)"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (high mannose) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O14798.3)"
     Region          160..224
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14798.3)"
     Region          163..>232
                     /region_name="PRK11907"
                     /note="bifunctional 2',3'-cyclic-nucleotide
                     2'-phosphodiesterase/3'-nucleotidase"
                     /db_xref="CDD:237019"
     Region          222..236
                     /region_name="TAPE 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14798.3)"
     CDS             1..259
                     /gene="TNFRSF10C"
                     /gene_synonym="CD263; DCR1; DCR1-TNFR; LIT; TRAIL-R3;
                     TRAILR3; TRID"
                     /coded_by="NM_003841.5:202..981"
                     /db_xref="CCDS:CCDS6037.1"
                     /db_xref="GeneID:8794"
                     /db_xref="HGNC:HGNC:11906"
                     /db_xref="MIM:603613"
ORIGIN      
        1 maripktlkf vvvivavllp vlaysattar qeevpqqtva pqqqrhsfkg eecpagshrs
       61 ehtgacnpct egvdytnasn nepscfpctv cksdqkhkss ctmtrdtvcq ckegtfrnen
      121 spemcrkcsr cpsgevqvsn ctswddiqcv eefganatve tpaaeetmnt spgtpapaae
      181 etmntspgtp apaaeetmtt spgtpapaae etmttspgtp apaaeetmit spgtpasshy
      241 lsctivgiiv livllivfv
//
LOCUS       NP_001258930            2098 aa            linear   PRI 21-NOV-2025
DEFINITION  dedicator of cytokinesis protein 7 isoform 4 [Homo sapiens].
ACCESSION   NP_001258930
VERSION     NP_001258930.1
DBSOURCE    REFSEQ: accession NM_001272001.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2098)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2098)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2098)
  AUTHORS   Chen,W., Zhou,M., Guan,B., Xie,B., Liu,Y., He,J., Zhao,J., Zhao,Q.
            and Yan,D.
  TITLE     Tumour-associated macrophage-derived DOCK7-enriched extracellular
            vesicles drive tumour metastasis in colorectal cancer via the
            RAC1/ABCA1 axis
  JOURNAL   Clin Transl Med 14 (2), e1591 (2024)
   PUBMED   38385857
  REMARK    GeneRIF: Tumour-associated macrophage-derived DOCK7-enriched
            extracellular vesicles drive tumour metastasis in colorectal cancer
            via the RAC1/ABCA1 axis.
REFERENCE   4  (residues 1 to 2098)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 2098)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 2098)
  AUTHORS   Nellist,M., Burgers,P.C., van den Ouweland,A.M., Halley,D.J. and
            Luider,T.M.
  TITLE     Phosphorylation and binding partner analysis of the TSC1-TSC2
            complex
  JOURNAL   Biochem Biophys Res Commun 333 (3), 818-826 (2005)
   PUBMED   15963462
REFERENCE   7  (residues 1 to 2098)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   8  (residues 1 to 2098)
  AUTHORS   Brajenovic,M., Joberty,G., Kuster,B., Bouwmeester,T. and Drewes,G.
  TITLE     Comprehensive proteomic analysis of human Par protein complexes
            reveals an interconnected protein network
  JOURNAL   J Biol Chem 279 (13), 12804-12811 (2004)
   PUBMED   14676191
REFERENCE   9  (residues 1 to 2098)
  AUTHORS   Cote,J.F. and Vuori,K.
  TITLE     Identification of an evolutionarily conserved superfamily of
            DOCK180-related proteins with guanine nucleotide exchange activity
  JOURNAL   J Cell Sci 115 (Pt 24), 4901-4913 (2002)
   PUBMED   12432077
REFERENCE   10 (residues 1 to 2098)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC103923.2, DR002667.1,
            DQ118680.1, AL451044.7, DQ341187.1, AB051558.1, BU567903.1 and
            BG190976.1.
            
            Summary: The protein encoded by this gene is a guanine nucleotide
            exchange factor (GEF) that plays a role in axon formation and
            neuronal polarization. The encoded protein displays GEF activity
            toward RAC1 and RAC3 Rho small GTPases but not toward CDC42.
            Several transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Dec 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853560.1242.1,
                                           SRR18074969.2229148.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2098
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..2098
                     /product="dedicator of cytokinesis protein 7 isoform 4"
                     /note="dedicator of cytokinesis protein 7"
                     /calculated_mol_wt=238144
     Region          52..161
                     /region_name="DOCK_C-D_N"
                     /note="Dedicator of cytokinesis C/D, N terminal;
                     pfam11878"
                     /db_xref="CDD:463380"
     Region          560..737
                     /region_name="C2_Dock-C"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class C proteins; cd08696"
                     /db_xref="CDD:176078"
     Region          1604..2076
                     /region_name="DHR2_DOCK7"
                     /note="Dock Homology Region 2, a GEF domain, of Class C
                     Dedicator of Cytokinesis 7; cd11703"
                     /db_xref="CDD:212576"
     Site            order(1759,1769,1771..1772,1774..1775,1778..1779,
                     1781..1782,1785..1786)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:212576"
     Site            order(1799,1801,1824,1827..1830,1832..1833,1852..1854,
                     1871..1873,1901..1904,1914..1915,1918,1920,1957..1958,
                     1961,1977..1978,1980..1981,1984..1986,1989..1991,
                     1994..1995,1998,2026,2048,2051)
                     /site_type="other"
                     /note="Rac/Cdc42 binding site [polypeptide binding]"
                     /db_xref="CDD:212576"
     Site            1989..1994
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212576"
     CDS             1..2098
                     /gene="DOCK7"
                     /gene_synonym="DEE23; EIEE23; ZIR2"
                     /coded_by="NM_001272001.2:123..6419"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS81335.1"
                     /db_xref="GeneID:85440"
                     /db_xref="HGNC:HGNC:19190"
                     /db_xref="MIM:615730"
ORIGIN      
        1 maerrafaqk isrtvaaevr kqisgqysgs pqllknlniv gnishhttvp lteavdpvdl
       61 edylithpla vdsgplrdli efppddievv ysprdcrtlv savpeesemd phvrdcirsy
      121 tedwaivirk yhklgtgfnp ntldkqkerq kglpkqvfes deapdgnsyq ddqddlkrrs
      181 msiddtprgs wacsifdlkn slpdallpnl ldrtpneeid rqnddqrksn rhkelfalhp
      241 spdeeepier lsvpdipkeh fgqrllvkcl slkfeieiep ifaslalydv kekkkisenf
      301 yfdlnseqmk gllrphvppa aittlarsai fsitypsqdv flviklekvl qqgdigecae
      361 pymifkeada tknkeklekl ksqadqfcqr lgkyrmpfaw taihlmnivs sagslerdst
      421 eveistgerk gswserrnss ivgrrslert tsgddacnlt sfrpatltvt nffkqegdrl
      481 sdedlykfla dmrrpssvlr rlrpitaqlk idispapenp hycltpellq vklypdsrvr
      541 ptreilefpa rdvyvpntty rnllyiypqs lnfanrqgsa rnitvkvqfm ygedpsnamp
      601 vifgksscse fskeaytavv yhnrspdfhe eikvklpatl tdhhhllftf yhvscqqkqn
      661 tpletpvgyt wipmlqngrl ktgqfclpvs lekppqaysv lspevplpgm kwvdnhkgvf
      721 nvevvavssi htqdpyldkf falvnaldeh lfpvrigdmr imennlenel kssisalnss
      781 qlepvvrflh llldklillv irppviagqi vnlgqasfea masiinrlhk nlegnhdqhg
      841 rnsllasyih yvfrlpntyp nssspgpggl ggsvhyatma rsavrpasln lnrsrslsns
      901 npdisgtpts pddevrsiig skamdrscnr msshtetssf lqtltgrlpt kklfheelal
      961 qwvvcsgsvr esalqqawff felmvksmvh hlyfndklea prksrfperf mddiaalvst
     1021 iasdivsrfq kdtemverln tslafflndl lsvmdrgfvf slikscykqv ssklyslpnp
     1081 svlvslrldf lriicshehy vtlnlpcsll tppaspspsv ssatsqssgf stnvqdqkia
     1141 nmfelsvpfr qqhylaglvl telavildpd aeglfglhkk vinmvhnlls shdsdprysd
     1201 pqikarvaml ylpligiime tvpqlydfte thnqrgrpic iatddyeses gsmisqtvam
     1261 aiagtsvpql trpgsfllts tsgrqhttfs aessrsllic llwvlknade tvlqkwftdl
     1321 svlqlnrlld llylcvscfe ykgkkvferm nsltfkkskd mrakleeail gsigarqemv
     1381 rrsrgqlers psgsafgsqe nlrwrkdmth wrqntekldk sraeieheal idgnlatean
     1441 liildtleiv vqtvsvtesk esilggvlkv llhsmacnqs avylqhcfat qralvskfpe
     1501 llfeeeteqc adlclrllrh csssigtirs hasaslyllm rqnfeignnf arvkmqvtms
     1561 lsslvgtsqn fneeflrrsl ktiltyaeed lelrettfpd qvqdlvfnlh milsdtvkmk
     1621 ehqedpemli dlmyriakgy qtspdlrltw lqnmagkhse rsnhaeaaqc lvhsaalvae
     1681 ylsmledrky lpvgcvtfqn issnvleesa vsddvvspde egicsgkyft esglvglleq
     1741 aaasfsmagm yeavnevykv lipiheanrd akklstihgk lqeafskivh qdgkrmfgty
     1801 frvgfygtkf gdldeqefvy kepaitklae ishrlegfyg erfgedvvev ikdsnpvdkc
     1861 kldpnkayiq ityvepyfdt yemkdrityf dknynlrrfm yctpftldgr ahgelheqfk
     1921 rktilttsha fpyiktrvnv thkeeiiltp ievaiedmqk ktqelafath qdpadpkmlq
     1981 mvlqgsvgtt vnqgplevaq vflseipsdp klfrhhnklr lcfkdftkrc edalrknksl
     2041 igpdqkeyqr elernyhrlk ealqplinrk ipqlykavlp vtchrdsfsr mslrkmdl
//
LOCUS       NP_066299                151 aa            linear   PRI 21-NOV-2025
DEFINITION  myosin light polypeptide 6 isoform 1 [Homo sapiens].
ACCESSION   NP_066299 NP_524148
VERSION     NP_066299.2
DBSOURCE    REFSEQ: accession NM_021019.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 151)
  AUTHORS   Zanivan,S., Maione,F., Hein,M.Y., Hernandez-Fernaud,J.R.,
            Ostasiewicz,P., Giraudo,E. and Mann,M.
  TITLE     SILAC-based proteomics of human primary endothelial cell
            morphogenesis unveils tumor angiogenic markers
  JOURNAL   Mol Cell Proteomics 12 (12), 3599-3611 (2013)
   PUBMED   23979707
REFERENCE   6  (residues 1 to 151)
  AUTHORS   Watanabe,M., Kohri,M., Takaishi,M., Horie,R. and Higashihara,M.
  TITLE     Molecular cloning and sequencing of myosin light chains in human
            megakaryoblastic leukemia cells
  JOURNAL   J Smooth Muscle Res 37 (1), 25-38 (2001)
   PUBMED   11436981
REFERENCE   7  (residues 1 to 151)
  AUTHORS   Komiyama,M., Soldati,T., von Arx,P. and Perriard,J.C.
  TITLE     The intracompartmental sorting of myosin alkali light chain
            isoproteins reflects the sequence of developmental expression as
            determined by double epitope-tagging competition
  JOURNAL   J Cell Sci 109 (Pt 8), 2089-2099 (1996)
   PUBMED   8856505
REFERENCE   8  (residues 1 to 151)
  AUTHORS   Bora,P.S., Bora,N.S., Wu,X., Kaplan,H.J. and Lange,L.G.
  TITLE     Molecular cloning, sequencing, and characterization of smooth
            muscle myosin alkali light chain from human eye cDNA: homology with
            myocardial fatty acid ethyl ester synthase-III cDNA
  JOURNAL   Genomics 19 (1), 186-188 (1994)
   PUBMED   8188229
REFERENCE   9  (residues 1 to 151)
  AUTHORS   Hailstones,D.L. and Gunning,P.W.
  TITLE     Characterization of human myosin light chains 1sa and 3nm:
            implications for isoform evolution and function
  JOURNAL   Mol Cell Biol 10 (3), 1095-1104 (1990)
   PUBMED   2304459
REFERENCE   10 (residues 1 to 151)
  AUTHORS   Lenz,S., Lohse,P., Seidel,U. and Arnold,H.H.
  TITLE     The alkali light chains of human smooth and nonmuscle myosins are
            encoded by a single gene. Tissue-specific expression by alternative
            splicing pathways
  JOURNAL   J Biol Chem 264 (15), 9009-9015 (1989)
   PUBMED   2722814
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG283793.1, BC017455.1 and
            CA427580.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Feb 28, 2006 this sequence version replaced
            NP_524148.1, NP_066299.1.
            
            Summary: Myosin is a hexameric ATPase cellular motor protein. It is
            composed of two heavy chains, two nonphosphorylatable alkali light
            chains, and two phosphorylatable regulatory light chains. This gene
            encodes a myosin alkali light chain that is expressed in smooth
            muscle and non-muscle tissues. Genomic sequences representing
            several pseudogenes have been described and two transcript variants
            encoding different isoforms have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1), which is the major non-muscle
            transcript, represents the longer transcript and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.506614.1,
                                           SRR5189667.249246.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000550697.6/ ENSP00000446955.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.2"
     Protein         1..151
                     /product="myosin light polypeptide 6 isoform 1"
                     /note="myosin, light polypeptide 6, alkali, smooth muscle
                     and non-muscle; myosin light chain alkali 3; myosin light
                     chain A3; 17 kDa myosin light chain; myosin, light chain
                     6, alkali, smooth muscle and non-muscle"
                     /calculated_mol_wt=16799
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylcysteine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P60660.2)"
     Region          5..150
                     /region_name="PTZ00184"
                     /note="calmodulin; Provisional"
                     /db_xref="CDD:185504"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P60660.2)"
     Site            81
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P60660.2)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P60660.2)"
     CDS             1..151
                     /gene="MYL6"
                     /gene_synonym="ESMLC; LC17; LC17-GI; LC17-NM; LC17A;
                     LC17B; MLC-3; MLC1SM; MLC3NM; MLC3SM"
                     /coded_by="NM_021019.5:44..499"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8906.1"
                     /db_xref="GeneID:4637"
                     /db_xref="HGNC:HGNC:7587"
                     /db_xref="MIM:609931"
ORIGIN      
        1 mcdftedqta efkeafqlfd rtgdgkilys qcgdvmralg qnptnaevlk vlgnpksdem
       61 nvkvldfehf lpmlqtvakn kdqgtyedyv eglrvfdkeg ngtvmgaeir hvlvtlgekm
      121 teeevemlva ghedsngcin yeafvrhils g
//
LOCUS       NP_858062                446 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B
            beta isoform isoform b [Homo sapiens].
ACCESSION   NP_858062
VERSION     NP_858062.1
DBSOURCE    REFSEQ: accession NM_181676.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Shen,D. and Kang,S.
  TITLE     Comprehensive analysis of mitochondria-related genes indicates that
            PPP2R2B is a novel biomarker and promotes the progression of
            bladder cancer via Wnt signaling pathway
  JOURNAL   Biol Direct 19 (1), 17 (2024)
   PUBMED   38409085
  REMARK    GeneRIF: Comprehensive analysis of mitochondria-related genes
            indicates that PPP2R2B is a novel biomarker and promotes the
            progression of bladder cancer via Wnt signaling pathway.
            Erratum:[Biol Direct. 2024 Apr 18;19(1):27. doi:
            10.1186/s13062-024-00474-1. PMID: 38637864]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Zhou,C., Liu,H.B., Jahanbakhsh,F., Deng,L., Wu,B., Ying,M.,
            Margolis,R.L. and Li,P.P.
  TITLE     Bidirectional Transcription at the PPP2R2B Gene Locus in
            Spinocerebellar Ataxia Type 12
  JOURNAL   Mov Disord 38 (12), 2230-2240 (2023)
   PUBMED   37735923
  REMARK    GeneRIF: Bidirectional Transcription at the PPP2R2B Gene Locus in
            Spinocerebellar Ataxia Type 12.
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Ruediger,R., Brewis,N., Ohst,K. and Walter,G.
  TITLE     Increasing the ratio of PP2A core enzyme to holoenzyme inhibits
            Tat-stimulated HIV-1 transcription and virus production
  JOURNAL   Virology 238 (2), 432-443 (1997)
   PUBMED   9400615
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Tung,H.Y., De Rocquigny,H., Zhao,L.J., Cayla,X., Roques,B.P. and
            Ozon,R.
  TITLE     Direct activation of protein phosphatase-2A0 by HIV-1 encoded
            protein complex NCp7:vpr
  JOURNAL   FEBS Lett 401 (2-3), 197-201 (1997)
   PUBMED   9013886
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Schalling,M., Hudson,T.J., Buetow,K.H. and Housman,D.E.
  TITLE     Direct detection of novel expanded trinucleotide repeats in the
            human genome
  JOURNAL   Nat Genet 4 (2), 135-139 (1993)
   PUBMED   8348150
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Margolis,R.L., Holmes,S.E., Srivastava,A.K., Mukherji,M. and
            Sinha,K.K.
  TITLE     Spinocerebellar Ataxia Type 12 - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301381
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
REFERENCE   10 (residues 1 to 446)
  AUTHORS   Mayer,R.E., Hendrix,P., Cron,P., Matthies,R., Stone,S.R., Goris,J.,
            Merlevede,W., Hofsteenge,J. and Hemmings,B.A.
  TITLE     Structure of the 55-kDa regulatory subunit of protein phosphatase
            2A: evidence for a neuronal-specific isoform
  JOURNAL   Biochemistry 30 (15), 3589-3597 (1991)
   PUBMED   1849734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA522334.1, BC031790.1,
            AI621232.1 and AC008728.7.
            
            Summary: The product of this gene belongs to the phosphatase 2
            regulatory subunit B family. Protein phosphatase 2 is one of the
            four major Ser/Thr phosphatases, and it is implicated in the
            negative control of cell growth and division. It consists of a
            common heteromeric core enzyme, which is composed of a catalytic
            subunit and a constant regulatory subunit, that associates with a
            variety of regulatory subunits. The B regulatory subunit might
            modulate substrate selectivity and catalytic activity. This gene
            encodes a beta isoform of the regulatory subunit B55 subfamily.
            Defects in this gene cause autosomal dominant spinocerebellar
            ataxia 12 (SCA12), a disease caused by degeneration of the
            cerebellum, sometimes involving the brainstem and spinal cord, and
            in resulting in poor coordination of speech and body movements.
            Multiple alternatively spliced variants, which encode different
            isoforms, have been identified for this gene. The 5' UTR of some of
            these variants includes a CAG trinucleotide repeat sequence (7-28
            copies) that can be expanded to 55-78 copies in cases of SCA12.
            [provided by RefSeq, Jul 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.110249.1,
                                           SRR1803614.19829.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..446
                     /product="serine/threonine-protein phosphatase 2A 55 kDa
                     regulatory subunit B beta isoform isoform b"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase 2, regulatory subunit B, beta"
                     /calculated_mol_wt=51886
     Region          25..441
                     /region_name="CDC55"
                     /note="Serine/threonine protein phosphatase 2A, regulatory
                     subunit [Signal transduction mechanisms]; COG5170"
                     /db_xref="CDD:227498"
     Region          30..78
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          96..173
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          179..215
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          229..280
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          287..323
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          344..379
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          418..441
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..446
                     /gene="PPP2R2B"
                     /gene_synonym="B55BETA; PP2AB55BETA; PP2ABBETA; PP2APR55B;
                     PP2APR55BETA; PR2AB55BETA; PR2ABBETA; PR2APR55BETA; PR52B;
                     PR55-BETA; PR55BETA; SCA12"
                     /coded_by="NM_181676.3:219..1559"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS4283.1"
                     /db_xref="GeneID:5521"
                     /db_xref="HGNC:HGNC:9305"
                     /db_xref="MIM:604325"
ORIGIN      
        1 mkcfsrylpy ifrppntils sschteadii stvefnhtge llatgdkggr vvifqreqes
       61 knqvhrrgey nvystfqshe pefdylksle ieekinkirw lpqqnaayfl lstndktvkl
      121 wkvserdkrp egynlkdeeg rlrdpatitt lrvpvlrpmd lmveatprrv fanahtyhin
      181 sisvnsdyet ymsaddlrin lwnfeitnqs fnivdikpan meeltevita aefhphhcnt
      241 fvyssskgti rlcdmrasal cdrhtkffee pedpsnrsff seiissisdv kfshsgryim
      301 trdyltvkvw dlnmenrpie tyqvhdylrs klcslyendc ifdkfecvwn gsdsvimtgs
      361 ynnffrmfdr ntkrdvtlea srenskprai lkprkvcvgg krrkdeisvd sldfskkilh
      421 tawhpsenii avaatnnlyi fqdkvn
//
LOCUS       NP_001351753             312 aa            linear   PRI 21-NOV-2025
DEFINITION  periphilin-1 isoform 11 [Homo sapiens].
ACCESSION   NP_001351753
VERSION     NP_001351753.1
DBSOURCE    REFSEQ: accession NM_001364824.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Bloor,S., Wit,N. and Lehner,P.J.
  TITLE     RNA binding by Periphilin plays an essential role in initiating
            silencing by the HUSH complex
  JOURNAL   Nucleic Acids Res 53 (2) (2025)
   PUBMED   39658355
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Jensvold,Z.D., Flood,J.R., Christenson,A.E. and Lewis,P.W.
  TITLE     Interplay between Two Paralogous Human Silencing Hub (HuSH)
            Complexes in Regulating LINE-1 Element Silencing
  JOURNAL   Nat Commun 15 (1), 9492 (2024)
   PUBMED   39489739
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Tunbak,H., Enriquez-Gasca,R., Tie,C.H.C., Gould,P.A., Mlcochova,P.,
            Gupta,R.K., Fernandes,L., Holt,J., van der Veen,A.G.,
            Giampazolias,E., Burns,K.H., Maillard,P.V. and Rowe,H.M.
  TITLE     The HUSH complex is a gatekeeper of type I interferon through
            epigenetic regulation of LINE-1s
  JOURNAL   Nat Commun 11 (1), 5387 (2020)
   PUBMED   33144593
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Prigozhin,D.M., Douse,C.H., Farleigh,L.E., Albecka,A.,
            Tchasovnikarova,I.A., Timms,R.T., Oda,S.I., Adolf,F.,
            Freund,S.M.V., Maslen,S., Lehner,P.J. and Modis,Y.
  TITLE     Periphilin self-association underpins epigenetic silencing by the
            HUSH complex
  JOURNAL   Nucleic Acids Res 48 (18), 10313-10328 (2020)
   PUBMED   32976585
  REMARK    GeneRIF: Periphilin self-association underpins epigenetic silencing
            by the HUSH complex.
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Kurita,M., Suzuki,H., Masai,H., Mizumoto,K., Ogata,E.,
            Nishimoto,I., Aiso,S. and Matsuoka,M.
  TITLE     Overexpression of CR/periphilin downregulates Cdc7 expression and
            induces S-phase arrest
  JOURNAL   Biochem Biophys Res Commun 324 (2), 554-561 (2004)
   PUBMED   15474462
  REMARK    GeneRIF: CR (periphilin) retards S-phase progression by modifying
            expression of Cdc7 and other genes involved in progression of DNA
            replication
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Goehler,H., Lalowski,M., Stelzl,U., Waelter,S., Stroedicke,M.,
            Worm,U., Droege,A., Lindenberg,K.S., Knoblich,M., Haenig,C.,
            Herbst,M., Suopanki,J., Scherzinger,E., Abraham,C., Bauer,B.,
            Hasenbank,R., Fritzsche,A., Ludewig,A.H., Bussow,K., Coleman,S.H.,
            Gutekunst,C.A., Landwehrmeyer,B.G., Lehrach,H. and Wanker,E.E.
  TITLE     A protein interaction network links GIT1, an enhancer of huntingtin
            aggregation, to Huntington's disease
  JOURNAL   Mol Cell 15 (6), 853-865 (2004)
   PUBMED   15383276
  REMARK    Erratum:[Mol Cell. 2005 Jul 22;19(2):287. Buessow, Konrad
            [corrected to Bussow, Konrad]]
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Kazerounian,S. and Aho,S.
  TITLE     Characterization of periphilin, a widespread, highly insoluble
            nuclear protein and potential constituent of the keratinocyte
            cornified envelope
  JOURNAL   J Biol Chem 278 (38), 36707-36717 (2003)
   PUBMED   12853457
  REMARK    GeneRIF: periphilin is potentially involved in epithelial
            differentiation and contributes to epidermal integrity and barrier
            formation
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Kazerounian,S., Uitto,J. and Aho,S.
  TITLE     Unique role for the periplakin tail in intermediate filament
            association: specific binding to keratin 8 and vimentin
  JOURNAL   Exp Dermatol 11 (5), 428-438 (2002)
   PUBMED   12366696
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Line,A., Stengrevics,A., Slucka,Z., Li,G., Jankevics,E. and
            Rees,R.C.
  TITLE     Serological identification and expression analysis of gastric
            cancer-associated genes
  JOURNAL   Br J Cancer 86 (11), 1824-1830 (2002)
   PUBMED   12087473
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079684.16 and AC079601.25.
            
            Summary: The protein encoded by this gene is one of the several
            proteins that become sequentially incorporated into the cornified
            cell envelope during the terminal differentiation of keratinocyte
            at the outer layers of epidermis. This protein interacts with
            periplakin, which is known as a precursor of the cornified cell
            envelope. The cellular localization pattern and insolubility of
            this protein suggest that it may play a role in epithelial
            differentiation and contribute to epidermal integrity and barrier
            formation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2320573.1,
                                           SRR11853562.7084.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..312
                     /product="periphilin-1 isoform 11"
                     /note="gastric cancer antigen Ga50; CDC7 expression
                     repressor"
                     /calculated_mol_wt=35899
     Region          230..302
                     /region_name="periphilin-like"
                     /note="Vertebrate periphilin-1 and similar proteins;
                     cd22896"
                     /db_xref="CDD:439377"
     Site            order(235,239..240,243,246..247,250..251,254..255,258,276,
                     279..280,283..284,287..288,290..291,294..295,298)
                     /site_type="other"
                     /note="heterotrimer interface [polypeptide binding]"
                     /db_xref="CDD:439377"
     CDS             1..312
                     /gene="PPHLN1"
                     /gene_synonym="CR; HSPC206; HSPC232"
                     /coded_by="NM_001364824.2:84..1022"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:51535"
                     /db_xref="HGNC:HGNC:19369"
                     /db_xref="MIM:608150"
ORIGIN      
        1 mwsegryeye riprerappr shpsdesgyr wtrddhsasr qpeyrdmrdg frrksfyssh
       61 yarerspykr dntffrespv grkdsphsrs gssvssrsys persksysfh qsqhrksvrp
      121 gasykrqneg nperdkerpv qslktsrdts pssgsavsss kvldkpsrlt ekelaeaask
      181 waaekleksd esnlpeisey eagstaplft dqpeepesnt thgielfeds qlttrskaia
      241 sktkeieqvy rqdcetfgmv vkmliekdps leksiqfalr qnlheigerc veelkhfiae
      301 ydtstqdfge pf
//
LOCUS       NP_001265089             256 aa            linear   PRI 21-NOV-2025
DEFINITION  proline-rich AKT1 substrate 1 isoform b [Homo sapiens].
ACCESSION   NP_001265089
VERSION     NP_001265089.1
DBSOURCE    REFSEQ: accession NM_001278160.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Zhang,T., Wang,Y., Yu,H., Zhang,T., Guo,L., Xu,J., Wei,X., Wang,N.,
            Wu,Y., Wang,X. and Huang,L.
  TITLE     PGK1 represses autophagy-mediated cell death to promote the
            proliferation of liver cancer cells by phosphorylating PRAS40
  JOURNAL   Cell Death Dis 13 (1), 68 (2022)
   PUBMED   35058442
  REMARK    GeneRIF: PGK1 represses autophagy-mediated cell death to promote
            the proliferation of liver cancer cells by phosphorylating PRAS40.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Challa,S., Khulpateea,B.R., Nandu,T., Camacho,C.V., Ryu,K.W.,
            Chen,H., Peng,Y., Lea,J.S. and Kraus,W.L.
  TITLE     Ribosome ADP-ribosylation inhibits translation and maintains
            proteostasis in cancers
  JOURNAL   Cell 184 (17), 4531-4546 (2021)
   PUBMED   34314702
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Saito,A., Narasimhan,P., Hayashi,T., Okuno,S., Ferrand-Drake,M. and
            Chan,P.H.
  TITLE     Neuroprotective role of a proline-rich Akt substrate in apoptotic
            neuronal cell death after stroke: relationships with nerve growth
            factor
  JOURNAL   J Neurosci 24 (7), 1584-1593 (2004)
   PUBMED   14973226
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Kovacina,K.S., Park,G.Y., Bae,S.S., Guzzetta,A.W., Schaefer,E.,
            Birnbaum,M.J. and Roth,R.A.
  TITLE     Identification of a proline-rich Akt substrate as a 14-3-3 binding
            partner
  JOURNAL   J Biol Chem 278 (12), 10189-10194 (2003)
   PUBMED   12524439
REFERENCE   8  (residues 1 to 256)
  AUTHORS   Park,I.H., Bachmann,R., Shirazi,H. and Chen,J.
  TITLE     Regulation of ribosomal S6 kinase 2 by mammalian target of
            rapamycin
  JOURNAL   J Biol Chem 277 (35), 31423-31429 (2002)
   PUBMED   12087098
REFERENCE   9  (residues 1 to 256)
  AUTHORS   Vladimirov,S.N., Ivanov,A.V., Karpova,G.G., Musolyamov,A.K.,
            Egorov,T.A., Thiede,B., Wittmann-Liebold,B. and Otto,A.
  TITLE     Characterization of the human small-ribosomal-subunit proteins by
            N-terminal and internal sequencing, and mass spectrometry
  JOURNAL   Eur J Biochem 239 (1), 144-149 (1996)
   PUBMED   8706699
REFERENCE   10 (residues 1 to 256)
  AUTHORS   Grove,J.R., Banerjee,P., Balasubramanyam,A., Coffer,P.J.,
            Price,D.J., Avruch,J. and Woodgett,J.R.
  TITLE     Cloning and expression of two human p70 S6 kinase polypeptides
            differing only at their amino termini
  JOURNAL   Mol Cell Biol 11 (11), 5541-5550 (1991)
   PUBMED   1922062
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA476468.1 and BC051844.2.
            
            Summary: AKT1S1 is a proline-rich substrate of AKT (MIM 164730)
            that binds 14-3-3 protein (see YWHAH, MIM 113508) when
            phosphorylated (Kovacina et al., 2003 [PubMed 12524439]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (5) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (b) is
            shorter at the N-terminus compared to isoform a. Variants 2, 3, 4,
            and 5 encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1183837.1,
                                           SRR18074968.2916905.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..256
                     /product="proline-rich AKT1 substrate 1 isoform b"
                     /note="40 kDa proline-rich AKT substrate; AKT1 substrate 1
                     (proline rich)"
                     /calculated_mol_wt=27252
     Site            51
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Region          69..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D1F4; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Region          127..251
                     /region_name="PRAS"
                     /note="Proline-rich AKT1 substrate 1; pfam15798"
                     /db_xref="CDD:406279"
     Region          129..133
                     /region_name="TOS motif.
                     /evidence=ECO:0000269|PubMed:17510057"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000269|PubMed:17517883,
                     ECO:0000269|PubMed:18372248, ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Region          197..216
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000269|PubMed:18372248,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000269|PubMed:18372248; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Region          237..256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1 and DYRK3.
                     /evidence=ECO:0000269|PubMed:12524439,
                     ECO:0000269|PubMed:23415227, ECO:0000269|PubMed:29634919,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     CDS             1..256
                     /gene="AKT1S1"
                     /gene_synonym="Lobe; PRAS40"
                     /coded_by="NM_001278160.2:195..965"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS12784.1"
                     /db_xref="GeneID:84335"
                     /db_xref="HGNC:HGNC:28426"
                     /db_xref="MIM:610221"
ORIGIN      
        1 masgrpeelw eavvgaaerf rartgtelvl ltaapppppr pgpcayaahg rgalaeaarr
       61 clhdialahr aataarppap ppapqppspt pspprptlar edneededep tetetsgeql
      121 gisdngglfv mdedatlqdl ppfcesdpes tddgslseet pagpptcsvp pasalptqqy
      181 akslpvsvpv wgfkekrtea rssdeengpp sspdldriaa smralvlrea edtqvfgdlp
      241 rprlntsdfq klkrky
//
LOCUS       NP_001012632             429 aa            linear   PRI 21-NOV-2025
DEFINITION  C-terminal-binding protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001012632
VERSION     NP_001012632.1
DBSOURCE    REFSEQ: accession NM_001012614.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Kong,Y., Yang,G., Feng,X., Ji,Z., Wang,X., Shao,Y., Meng,J.,
            Yao,G., Ren,C. and Yang,G.
  TITLE     CTBP1 links metabolic syndrome to polycystic ovary syndrome through
            interruption of aromatase and SREBP1
  JOURNAL   Commun Biol 7 (1), 1174 (2024)
   PUBMED   39294274
  REMARK    GeneRIF: CTBP1 links metabolic syndrome to polycystic ovary
            syndrome through interruption of aromatase and SREBP1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Zhou,J., Yan,X., Liu,Y. and Yang,J.
  TITLE     Succinylation of CTBP1 mediated by KAT2A suppresses its inhibitory
            activity on the transcription of CDH1 to promote the progression of
            prostate cancer
  JOURNAL   Biochem Biophys Res Commun 650, 9-16 (2023)
   PUBMED   36764210
  REMARK    GeneRIF: Succinylation of CTBP1 mediated by KAT2A suppresses its
            inhibitory activity on the transcription of CDH1 to promote the
            progression of prostate cancer.
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Lou,L.Q., Zhou,W.Q., Song,X. and Chen,Z.
  TITLE     Elevation of hsa-miR-7-5p level mediated by CtBP1-p300-AP1 complex
            targets ATXN1 to trigger NF-kappaB-dependent inflammation response
  JOURNAL   J Mol Med (Berl) 101 (3), 223-235 (2023)
   PUBMED   36629882
  REMARK    GeneRIF: Elevation of hsa-miR-7-5p level mediated by CtBP1-p300-AP1
            complex targets ATXN1 to trigger NF-kappaB-dependent inflammation
            response.
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Tseng,C., Han,Y., Lv,Z., Song,Q., Wang,K., Shen,H. and Chen,Z.
  TITLE     The CRL4DCAF6 E3 ligase ubiquitinates CtBP1/2 to induce apoptotic
            signalling and promote intervertebral disc degeneration
  JOURNAL   J Mol Med (Berl) 101 (1-2), 171-181 (2023)
   PUBMED   36688959
  REMARK    GeneRIF: The CRL4[DCAF6] E3 ligase ubiquitinates CtBP1/2 to induce
            apoptotic signalling and promote intervertebral disc degeneration.
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Schaeper,U., Subramanian,T., Lim,L., Boyd,J.M. and Chinnadurai,G.
  TITLE     Interaction between a cellular protein that binds to the C-terminal
            region of adenovirus E1A (CtBP) and a novel cellular protein is
            disrupted by E1A through a conserved PLDLS motif
  JOURNAL   J Biol Chem 273 (15), 8549-8552 (1998)
   PUBMED   9535825
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Katsanis,N. and Fisher,E.M.
  TITLE     A novel C-terminal binding protein (CTBP2) is closely related to
            CTBP1, an adenovirus E1A-binding protein, and maps to human
            chromosome 21q21.3
  JOURNAL   Genomics 47 (2), 294-299 (1998)
   PUBMED   9479502
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Schaeper,U., Boyd,J.M., Verma,S., Uhlmann,E., Subramanian,T. and
            Chinnadurai,G.
  TITLE     Molecular cloning and characterization of a cellular phosphoprotein
            that interacts with a conserved C-terminal domain of adenovirus E1A
            involved in negative modulation of oncogenic transformation
  JOURNAL   Proc Natl Acad Sci U S A 92 (23), 10467-10471 (1995)
   PUBMED   7479821
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1998 Nov 24;95(24):14584]
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Boyd,J.M., Subramanian,T., Schaeper,U., La Regina,M., Bayley,S. and
            Chinnadurai,G.
  TITLE     A region in the C-terminus of adenovirus 2/5 E1a protein is
            required for association with a cellular phosphoprotein and
            important for the negative modulation of T24-ras mediated
            transformation, tumorigenesis and metastasis
  JOURNAL   EMBO J 12 (2), 469-478 (1993)
   PUBMED   8440238
REFERENCE   10 (residues 1 to 429)
  AUTHORS   Battaglia,A., Carey,J.C. and South,S.T.
  TITLE     Wolf-Hirschhorn Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301362
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092535.4, BU553431.1,
            BC053320.1, BC011655.2 and BM989059.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that binds to the C-terminus
            of adenovirus E1A proteins. This phosphoprotein is a
            transcriptional repressor and may play a role during cellular
            proliferation. This protein and the product of a second closely
            related gene, CTBP2, can dimerize. Both proteins can also interact
            with a polycomb group protein complex which participates in
            regulation of gene expression during development. Alternative
            splicing of transcripts from this gene results in multiple
            transcript variants. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.509200.1,
                                           SRR1163655.31102.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154405 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000382952.8/ ENSP00000372411.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..429
                     /product="C-terminal-binding protein 1 isoform 2"
                     /note="brefeldin A-ribosylated substrate"
                     /calculated_mol_wt=46274
     Region          17..335
                     /region_name="CtBP_dh"
                     /note="C-terminal binding protein (CtBP),
                     D-isomer-specific 2-hydroxyacid dehydrogenases related
                     repressor; cd05299"
                     /db_xref="CDD:240624"
     Site            order(86,89..90,255,304,307)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240624"
     Site            order(89,117,169..170,172..174,192..196,225..227,229,232,
                     253..255,279..280,304,306..307)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240624"
     CDS             1..429
                     /gene="CTBP1"
                     /gene_synonym="BARS; HADDTS"
                     /coded_by="NM_001012614.2:404..1693"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43203.1"
                     /db_xref="GeneID:1487"
                     /db_xref="HGNC:HGNC:2494"
                     /db_xref="MIM:602618"
ORIGIN      
        1 msgvrppimn gplhprplva lldgrdctve mpilkdvatv afcdaqstqe ihekvlneav
       61 galmyhtitl tredlekfka lriivrigsg fdnidiksag dlgiavcnvp aasveetads
      121 tlchilnlyr ratwlhqalr egtrvqsveq irevasgaar irgetlgiig lgrvgqaval
      181 rakafgfnvl fydpylsdgv eralglqrvs tlqdllfhsd cvtlhcglne hnhhlindft
      241 vkqmrqgafl vntargglvd ekalaqalke grirgaaldv hesepfsfsq gplkdapnli
      301 ctphaawyse qasiemreea areirraitg ripdslkncv nkdhltaath wasmdpavvh
      361 pelngaayry ppgvvgvapt gipaavegiv psamslshgl ppvahpphap spgqtvkpea
      421 drdhasdql
//
LOCUS       NP_067066                 81 aa            linear   PRI 21-NOV-2025
DEFINITION  costars family protein ABRACL [Homo sapiens].
ACCESSION   NP_067066 XP_371848 XP_946232
VERSION     NP_067066.1
DBSOURCE    REFSEQ: accession NM_021243.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Li,J. and Chen,H.
  TITLE     Actin-binding Rho activating C-terminal like (ABRACL)
            transcriptionally regulated by MYB proto-oncogene like 2 (MYBL2)
            promotes the proliferation, invasion, migration and
            epithelial-mesenchymal transition of breast cancer cells
  JOURNAL   Bioengineered 13 (4), 9019-9031 (2022)
   PUBMED   35341461
  REMARK    GeneRIF: Actin-binding Rho activating C-terminal like (ABRACL)
            transcriptionally regulated by MYB proto-oncogene like 2 (MYBL2)
            promotes the proliferation, invasion, migration and
            epithelial-mesenchymal transition of breast cancer cells.
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Fan,S., Chen,P. and Li,S.
  TITLE     miR-145-5p Inhibits the Proliferation, Migration, and Invasion of
            Esophageal Carcinoma Cells by Targeting ABRACL
  JOURNAL   Biomed Res Int 2021, 6692544 (2021)
   PUBMED   33728339
  REMARK    GeneRIF: miR-145-5p Inhibits the Proliferation, Migration, and
            Invasion of Esophageal Carcinoma Cells by Targeting ABRACL.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 81)
  AUTHORS   Hsiao,B.Y., Chen,C.H., Chi,H.Y., Yen,P.R., Yu,Y.Z., Lin,C.H.,
            Pang,T.L., Lin,W.C., Li,M.L., Yeh,Y.C., Chou,T.Y. and Chen,M.Y.
  TITLE     Human Costars Family Protein ABRACL Modulates Actin Dynamics and
            Cell Migration and Associates with Tumorigenic Growth
  JOURNAL   Int J Mol Sci 22 (4), 2037 (2021)
   PUBMED   33670794
  REMARK    GeneRIF: Human Costars Family Protein ABRACL Modulates Actin
            Dynamics and Cell Migration and Associates with Tumorigenic Growth.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 81)
  AUTHORS   Lin,J., Zhou,T. and Wang,J.
  TITLE     Solution structure of the human HSPC280 protein
  JOURNAL   Protein Sci 20 (1), 216-223 (2011)
   PUBMED   21082705
  REMARK    GeneRIF: Solution structure of the human HSPC280 protein
            Erratum:[Protein Sci. 2011 Sep;20(9):1644]
REFERENCE   5  (residues 1 to 81)
  AUTHORS   Pang,T.L., Chen,F.C., Weng,Y.L., Liao,H.C., Yi,Y.H., Ho,C.L.,
            Lin,C.H. and Chen,M.Y.
  TITLE     Costars, a Dictyostelium protein similar to the C-terminal domain
            of STARS, regulates the actin cytoskeleton and motility
  JOURNAL   J Cell Sci 123 (Pt 21), 3745-3755 (2010)
   PUBMED   20940261
REFERENCE   6  (residues 1 to 81)
  AUTHORS   Molina,H., Bunkenborg,J., Reddy,G.H., Muthusamy,B., Scheel,P.J. and
            Pandey,A.
  TITLE     A proteomic analysis of human hemodialysis fluid
  JOURNAL   Mol Cell Proteomics 4 (5), 637-650 (2005)
   PUBMED   15723814
REFERENCE   7  (residues 1 to 81)
  AUTHORS   Gevaert,K., Goethals,M., Martens,L., Van Damme,J., Staes,A.,
            Thomas,G.R. and Vandekerckhove,J.
  TITLE     Exploring proteomes and analyzing protein processing by mass
            spectrometric identification of sorted N-terminal peptides
  JOURNAL   Nat Biotechnol 21 (5), 566-569 (2003)
   PUBMED   12665801
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG563686.1 and AF116682.1.
            
            On or before Jul 26, 2007 this sequence version replaced
            XP_371848.5, XP_946232.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.36065.1,
                                           SRR1163658.170877.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367660.4/ ENSP00000356632.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.1"
     Protein         1..81
                     /product="costars family protein ABRACL"
                     /note="ABRA C-terminal-like protein"
                     /calculated_mol_wt=8925
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q9P1F3.1)"
     Region          2..79
                     /region_name="Costars"
                     /note="pfam14705"
                     /db_xref="CDD:464274"
     CDS             1..81
                     /gene="ABRACL"
                     /gene_synonym="C6orf115; Costars; HSPC280; PRO2013"
                     /coded_by="NM_021243.3:138..383"
                     /db_xref="CCDS:CCDS43509.1"
                     /db_xref="GeneID:58527"
                     /db_xref="HGNC:HGNC:21230"
                     /db_xref="MIM:621425"
ORIGIN      
        1 mnvdhevnll veeihrlgsk nadgklsvkf gvlfrddkca nlfealvgtl kaakrrkivt
       61 ypgelllqgv hddvdiillq d
//
LOCUS       NP_001424219            1053 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            beta isoform isoform 3 [Homo sapiens].
ACCESSION   NP_001424219 XP_047304268 XP_054202830
VERSION     NP_001424219.1
DBSOURCE    REFSEQ: accession NM_001437290.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Liu,L., Feng,X., Fan,C., Kong,D., Feng,X., Sun,C., Xu,Y., Li,B.,
            Jiang,Y. and Zheng,C.
  TITLE     PDCD4 interacting with PIK3CB and CTSZ promotes the apoptosis of
            multiple myeloma cells
  JOURNAL   FASEB J 38 (16), e70024 (2024)
   PUBMED   39190024
  REMARK    GeneRIF: PDCD4 interacting with PIK3CB and CTSZ promotes the
            apoptosis of multiple myeloma cells.
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Liu,G., Hou,Y., Jin,X., Zhang,Y., Sun,C., Huang,C., Ren,Y., Gao,J.,
            Wang,X. and Jiang,X.
  TITLE     PI3K/HSCB axis facilitates FOG1 nuclear translocation to promote
            erythropoiesis and megakaryopoiesis
  JOURNAL   Elife 13, 95815 (2024)
   PUBMED   38757931
  REMARK    GeneRIF: PI3K/HSCB axis facilitates FOG1 nuclear translocation to
            promote erythropoiesis and megakaryopoiesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1053)
  AUTHORS   Duewell,B.R., Wilson,N.E., Bailey,G.M., Peabody,S.E. and
            Hansen,S.D.
  TITLE     Molecular dissection of PI3Kbeta synergistic activation by receptor
            tyrosine kinases, GbetaGgamma, and Rho-family GTPases
  JOURNAL   Elife 12, 88991 (2024)
   PUBMED   38713746
  REMARK    GeneRIF: Molecular dissection of PI3Kbeta synergistic activation by
            receptor tyrosine kinases, GbetaGgamma, and Rho-family GTPases.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1053)
  AUTHORS   Xu,W., Chen,Y., Zhang,Z., Jiang,Y. and Wang,Z.
  TITLE     Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma
  JOURNAL   Med Oncol 40 (8), 221 (2023)
   PUBMED   37402056
  REMARK    GeneRIF: Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1053)
  AUTHORS   Milani,D., Mazzoni,M., Borgatti,P., Zauli,G., Cantley,L. and
            Capitani,S.
  TITLE     Extracellular human immunodeficiency virus type-1 Tat protein
            activates phosphatidylinositol 3-kinase in PC12 neuronal cells
  JOURNAL   J Biol Chem 271 (38), 22961-22964 (1996)
   PUBMED   8798481
REFERENCE   7  (residues 1 to 1053)
  AUTHORS   Bonnefoy-Berard,N., Liu,Y.C., von Willebrand,M., Sung,A., Elly,C.,
            Mustelin,T., Yoshida,H., Ishizaka,K. and Altman,A.
  TITLE     Inhibition of phosphatidylinositol 3-kinase activity by association
            with 14-3-3 proteins in T cells
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10142-10146 (1995)
   PUBMED   7479742
REFERENCE   8  (residues 1 to 1053)
  AUTHORS   Hu,P. and Schlessinger,J.
  TITLE     Direct association of p110 beta phosphatidylinositol 3-kinase with
            p85 is mediated by an N-terminal fragment of p110 beta
  JOURNAL   Mol Cell Biol 14 (4), 2577-2583 (1994)
   PUBMED   8139559
REFERENCE   9  (residues 1 to 1053)
  AUTHORS   Hu,P., Mondino,A., Skolnik,E.Y. and Schlessinger,J.
  TITLE     Cloning of a novel, ubiquitously expressed human
            phosphatidylinositol 3-kinase and identification of its binding
            site on p85
  JOURNAL   Mol Cell Biol 13 (12), 7677-7688 (1993)
   PUBMED   8246984
REFERENCE   10 (residues 1 to 1053)
  AUTHORS   Carpenter,C.L., Duckworth,B.C., Auger,K.R., Cohen,B.,
            Schaffhausen,B.S. and Cantley,L.C.
  TITLE     Purification and characterization of phosphoinositide 3-kinase from
            rat liver
  JOURNAL   J Biol Chem 265 (32), 19704-19711 (1990)
   PUBMED   2174051
  REMARK    GeneRIF: This paper reports the first purification of a
            phosphoinositide 3-kinase and shows that the protein is a
            heterodimer of an 85 kd regulatory subunit that mediates binding to
            phosphorylated proteins and a 110 kd catalytic subunit.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC067728.25, AC117389.5 and AC020890.22.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_047304268.1, XP_054202830.1.
            
            Summary: This gene encodes an isoform of the catalytic subunit of
            phosphoinositide 3-kinase (PI3K). These kinases are important in
            signaling pathways involving receptors on the outer membrane of
            eukaryotic cells and are named for their catalytic subunit. The
            encoded protein is the catalytic subunit for PI3Kbeta (PI3KB).
            PI3KB has been shown to be part of the activation pathway in
            neutrophils which have bound immune complexes at sites of injury or
            infection. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.23878.1,
                                           SRR14038192.368763.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..1053
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit beta isoform isoform 3"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.1.153"
                     /note="PI3-kinase p110 subunit beta; PtdIns-3-kinase p110;
                     PI3K-beta; PI3-kinase subunit beta; ptdIns-3-kinase
                     subunit beta; ptdIns-3-kinase subunit p110-beta;
                     phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa
                     catalytic subunit beta; serine/threonine protein kinase
                     PIK3CB; phosphoinositide-3-kinase, catalytic, beta
                     polypeptide"
                     /calculated_mol_wt=120945
     Region          41..118
                     /region_name="PI3K_p85B"
                     /note="PI3-kinase family, p85-binding domain; smart00143"
                     /db_xref="CDD:197539"
     Region          180..288
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, Ras-binding domain; smart00144"
                     /db_xref="CDD:197540"
     Region          324..501
                     /region_name="C2_PI3K_class_I_beta_delta"
                     /note="C2 domain present in class I beta and delta
                     phosphatidylinositol 3-kinases (PI3Ks); cd08693"
                     /db_xref="CDD:176075"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI9; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     Region          410..418
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Region          515..685
                     /region_name="PI3Ka_I"
                     /note="Phosphoinositide 3-kinase (PI3K) class I, accessory
                     domain; PIK domain is conserved in all PI3 and
                     PI4-kinases. Its role is unclear but it has been suggested
                     to be involved in substrate presentation. In general, PI3K
                     class I prefer phosphoinositol (4,5)...; cd00872"
                     /db_xref="CDD:238444"
     Region          689..1050
                     /region_name="PI3Kc_IA_beta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase beta; cd05173"
                     /db_xref="CDD:270717"
     Region          761..767
                     /region_name="G-loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(762,764..766,768,786,788,791,822,834..837,842,845,
                     907,909,919..920)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270717"
     Site            order(829..830,857..858,861,931..932,945,948,956..959,962,
                     1029,1032..1033,1035..1036)
                     /site_type="other"
                     /note="regulatory subunit interface [polypeptide binding]"
                     /db_xref="CDD:270717"
     Site            876
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270717"
     Region          899..907
                     /region_name="Catalytic loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            899..907
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270717"
     Region          918..944
                     /region_name="Activation loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(920..933,939..944)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270717"
     Site            1053
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12502714; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     CDS             1..1053
                     /gene="PIK3CB"
                     /gene_synonym="P110BETA; PI3K; PI3KBETA; PIK3C1"
                     /coded_by="NM_001437290.1:251..3412"
                     /note="isoform 3 is encoded by transcript variant 8"
                     /db_xref="GeneID:5291"
                     /db_xref="HGNC:HGNC:8976"
                     /db_xref="MIM:602925"
ORIGIN      
        1 mcfsfimppa madildiwav dsqiasdgsi pvdfllptgi yiqlevprea tisyikqmlw
       61 kqvhnypmfn llmdidsymf acvnqtavye eledetrrlc dvrpflpvlk lvtrscdpge
      121 kldskigvli gkglhefdsl kdpevnefrr kmrkfseeki lslvglswmd wlkqtyppeh
      181 epsipenled klyggkliva vhfencqdvf sfqvspnmnp ikvnelaiqk rltihgkede
      241 vspydyvlqv sgrveyvfgd hpliqfqyir ncvmnralph filvecckik kmyeqemiai
      301 eaainrnssn lplplppkkt riishvwenn npfqivlvkg nklnteetvk vhvraglfhg
      361 tellcktivs sevsgkndhi wneplefdin icdlprmarl cfavyavldk vktkkstkti
      421 npskyqtirk agkvhypvaw vntmvfdfkg qlrtgdiilh swssfpdele emlnpmgtvq
      481 tnpytenata lhvkfpenkk qpyyyppfdk srggkkflpv lkeildrdpl sqlcenemdl
      541 iwtlrqdcre ifpqslpkll lsikwnkled vaqlqallqi wpklppreal elldfnypdq
      601 yvreyavgcl rqmsdeelsq yllqlvqvlk yepfldcals rflleralgn rrigqflfwh
      661 lrsevhipav svqfgvilea ycrgsvghmk vlskqvealn klktlnslik lnavklnrak
      721 gkeamhtclk qsayrealsd lqsplnpcvi lselyvekck ymdskmkplw lvynnkvfge
      781 dsvgvifkng ddlrqdmltl qmlrlmdllw keagldlrml pygclatgdr sglievvsts
      841 etiadiqlns snvaaaaafn kdallnwlke ynsgddldra ieeftlscag ycvasyvlgi
      901 gdrhsdnimv kktgqlfhid fghilgnfks kfgikrervp filtydfihv iqqgktgnte
      961 kfgrfrqcce daylilrrhg nlfitlfalm ltaglpelts vkdiqylkds lalgkseeea
     1021 lkqfkqkfde alreswttkv nwmahtvrkd yrs
//
LOCUS       NP_001394383            2760 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform q [Homo sapiens].
ACCESSION   NP_001394383
VERSION     NP_001394383.1
DBSOURCE    REFSEQ: accession NM_001407454.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2760)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2760)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2760)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2760)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2760)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2760)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2760)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2760)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2760)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2760)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1168690.1,
                                           SRR14372079.3260071.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2760
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2760
                     /product="adenomatous polyposis coli protein isoform q"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=302136
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Region          <8..272
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          239..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          <307..365
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          389..425
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          429..470
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          433..470
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          480..512
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(503,507,511,550,554,558,595,599,603)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          520..561
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          566..606
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          570..604
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          608..648
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          612..648
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          649..936
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          953..1052
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1174..>1191
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1200..1285
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1208..1618
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1288..1310
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1554..1577
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1579..1632
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1633..1654
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1663..1756
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1790..1864
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1950..1969
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2140..2485
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2587..2760
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2760
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407454.1:60..8342"
                     /note="isoform q is encoded by transcript variant 24"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrriar iqqiekdilr irqllqsqat
      241 eaerssqnkh etgshdaerq negqgvgein matsgngqgs ttrmdhetas vlssssthsa
      301 prrltshlgt kiraycetcw ewqeahepgm dqdknpmpap vehqicpavc vlmklsfdee
      361 hrhamnelgr katrgissqe lgqglsgglq aiaellqvdc emygltndhy sitlrryagm
      421 altnltfgdv ankatlcsmk gcmralvaql ksesedlqqv iasvlrnlsw radvnskktl
      481 revgsvkalm ecalevkkes tlksvlsalw nlsahctenk adicavdgal aflvgtltyr
      541 sqtntlaiie sgggilrnvs sliatnedhr qilrennclq tllqhlkshs ltivsnacgt
      601 lwnlsarnpk dqealwdmga vsmlknlihs khkmiamgsa aalrnlmanr pakykdanim
      661 spgsslpslh vrkqkaleae ldaqhlsetf dnidnlspka shrskqrhkq slygdyvfdt
      721 nrhddnrsdn fntgnmtvls pylnttvlps ssssrgslds srsekdrsle rergiglgny
      781 hpatenpgts skrglqistt aaqiakvmee vsaihtsqed rssgsttelh cvtdernalr
      841 rssaahthsn tynftksens nrtcsmpyak leykrssnds lnsvsssdgy gkrgqmkpsi
      901 esyseddesk fcsygqypad lahkihsanh mddndgeldt pinyslkysd eqlnsgrqsp
      961 sqnerwarpk hiiedeikqs eqrqsrnqst typvytestd dkhlkfqphf gqqecvspyr
     1021 srgangsetn rvgsnhginq nvsqslcqed dyeddkptny seryseeeqh eeeerptnys
     1081 ikyneekrhv dqpidyslky atdipssqkq sfsfsksssg qssktehmss ssentstpss
     1141 nakrqnqlhp ssaqsrsgqp qkaatckvss inqetiqtyc vedtpicfsr csslsslssa
     1201 edeigcnqtt qeadsantlq iaeikekigt rsaedpvsev pavsqhprtk ssrlqgssls
     1261 sesarhkave fssgakspsk sgaqtpkspp ehyvqetplm fsrctsvssl dsfesrsias
     1321 svqsepcsgm vsgiispsdl pdspgqtmpp srsktppppp qtaqtkrevp knkaptaekr
     1381 esgpkqaavn aavqrvqvlp dadtllhfat estpdgfscs sslsalslde pfiqkdvelr
     1441 imppvqendn gneteseqpk esnenqekea ektidsekdl lddsddddie ileeciisam
     1501 ptkssrkakk paqtasklpp pvarkpsqlp vykllpsqnr lqpqkhvsft pgddmprvyc
     1561 vegtpinfst atslsdltie sppnelaage gvrggaqsge fekrdtipte grstdeaqgg
     1621 ktssvtipel ddnkaeegdi laecinsamp kgkshkpfrv kkimdqvqqa sasssapnkn
     1681 qldgkkkkpt spvkpipqnt eyrtrvrkna dsknnlnaer vfsdnkdskk qnlknnskvf
     1741 ndklpnnedr vrgsfafdsp hhytpiegtp ycfsrndsls sldfddddvd lsrekaelrk
     1801 akenkeseak vtshteltsn qqsanktqai akqpinrgqp kpilqkqstf pqsskdipdr
     1861 gaatdeklqn faientpvcf shnsslssls didqennnke nepiketepp dsqgepskpq
     1921 asgyapksfh vedtpvcfsr nsslsslsid seddllqeci ssampkkkkp srlkgdnekh
     1981 sprnmggilg edltldlkdi qrpdsehgls pdsenfdwka iqegansivs slhqaaaaac
     2041 lsrqassdsd silslksgis lgspfhltpd qeekpftsnk gprilkpgek stletkkies
     2101 eskgikggkk vykslitgkv rsnseisgqm kqplqanmps isrgrtmihi pgvrnsssst
     2161 spvskkgppl ktpaskspse gqtattsprg akpsvksels pvarqtsqig gsskapsrsg
     2221 srdstpsrpa qqplsrpiqs pgrnsispgr ngisppnkls qlprtsspst astkssgsgk
     2281 msytspgrqm sqqnltkqtg lsknassipr sesaskglnq mnngngankk velsrmsstk
     2341 ssgsesdrse rpvlvrqstf ikeapsptlr rkleesasfe slspssrpas ptrsqaqtpv
     2401 lspslpdmsl sthssvqagg wrklppnlsp tieyndgrpa krhdiarshs espsrlpinr
     2461 sgtwkrehsk hssslprvst wrrtgssssi lsassessek aksedekhvn sisgtkqske
     2521 nqvsakgtwr kikenefspt nstsqtvssg atngaesktl iyqmapavsk tedvwvried
     2581 cpinnprsgr sptgntppvi dsvsekanpn ikdskdnqak qnvgngsvpm rtvglenrln
     2641 sfiqvdapdq kgteikpgqn npvpvsetne ssivertpfs ssssskhssp sgtvaarvtp
     2701 fnynpsprks sadstsarps qiptpvnnnt kkrdsktdst essgtqspkr hsgsylvtsv
//
LOCUS       NP_001400347             317 aa            linear   PRI 21-NOV-2025
DEFINITION  alpha-tocopherol transfer protein isoform 6 [Homo sapiens].
ACCESSION   NP_001400347
VERSION     NP_001400347.1
DBSOURCE    REFSEQ: accession NM_001413418.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Jeridi,C., Rachdi,A., Nabli,F., Saied,Z., Zouari,R., Ben
            Mohamed,D., Ben Said,M., Masmoudi,S., Ben Sassi,S. and Amouri,R.
  TITLE     Genetic heterogeneity within a consanguineous family involving TTPA
            and SETX genes
  JOURNAL   J Neurogenet 37 (4), 124-130 (2023)
   PUBMED   38109176
  REMARK    GeneRIF: Genetic heterogeneity within a consanguineous family
            involving TTPA and SETX genes.
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Ulatowski,L., Ghelfi,M., West,R., Atkinson,J., Finno,C.J. and
            Manor,D.
  TITLE     The tocopherol transfer protein mediates vitamin E trafficking
            between cerebellar astrocytes and neurons
  JOURNAL   J Biol Chem 298 (3), 101712 (2022)
   PUBMED   35150738
  REMARK    GeneRIF: The tocopherol transfer protein mediates vitamin E
            trafficking between cerebellar astrocytes and neurons.
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Arai,H. and Kono,N.
  TITLE     alpha-Tocopherol transfer protein (alpha-TTP)
  JOURNAL   Free Radic Biol Med 176, 162-175 (2021)
   PUBMED   34563650
  REMARK    GeneRIF: alpha-Tocopherol transfer protein (alpha-TTP).
            Review article
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Gotoda,T., Arita,M., Arai,H., Inoue,K., Yokota,T., Fukuo,Y.,
            Yazaki,Y. and Yamada,N.
  TITLE     Adult-onset spinocerebellar dysfunction caused by a mutation in the
            gene for the alpha-tocopherol-transfer protein
  JOURNAL   N Engl J Med 333 (20), 1313-1318 (1995)
   PUBMED   7566022
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Arita,M., Sato,Y., Miyata,A., Tanabe,T., Takahashi,E., Kayden,H.J.,
            Arai,H. and Inoue,K.
  TITLE     Human alpha-tocopherol transfer protein: cDNA cloning, expression
            and chromosomal localization
  JOURNAL   Biochem J 306 (Pt 2) (Pt 2), 437-443 (1995)
   PUBMED   7887897
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Ouahchi,K., Arita,M., Kayden,H., Hentati,F., Ben Hamida,M.,
            Sokol,R., Arai,H., Inoue,K., Mandel,J.L. and Koenig,M.
  TITLE     Ataxia with isolated vitamin E deficiency is caused by mutations in
            the alpha-tocopherol transfer protein
  JOURNAL   Nat Genet 9 (2), 141-145 (1995)
   PUBMED   7719340
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Ben Hamida,C., Doerflinger,N., Belal,S., Linder,C., Reutenauer,L.,
            Dib,C., Gyapay,G., Vignal,A., Le Paslier,D., Cohen,D. et al.
  TITLE     Localization of Friedreich ataxia phenotype with selective vitamin
            E deficiency to chromosome 8q by homozygosity mapping
  JOURNAL   Nat Genet 5 (2), 195-200 (1993)
   PUBMED   8252047
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Schuelke,M.
  TITLE     Ataxia with Vitamin E Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301419
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC120042.3.
            
            Summary: This gene encodes a soluble protein that binds
            alpha-trocopherol, a form of vitamin E, with high selectivity and
            affinity. This protein plays an important role in regulating
            vitamin E levels in the body by transporting vitamin E between
            membrane vesicles and facilitating the secretion of vitamin E from
            hepatocytes to circulating lipoproteins. Mutations in this gene
            cause hereditary vitamin E deficiency (ataxia with vitamin E
            deficiency, AVED) and retinitis pigmentosa. [provided by RefSeq,
            Nov 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.119328.1,
                                           SRR6380200.121714.5 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.3"
     Protein         1..317
                     /product="alpha-tocopherol transfer protein isoform 6"
                     /note="tocopherol (alpha) transfer protein (ataxia
                     (Friedreich-like) with vitamin E deficiency); alpha-TTP"
                     /calculated_mol_wt=35543
     Region          <40..73
                     /region_name="CRAL_TRIO_N"
                     /note="CRAL/TRIO, N-terminal domain; smart01100"
                     /db_xref="CDD:215024"
     Region          159..286
                     /region_name="CRAL_TRIO"
                     /note="CRAL/TRIO domain; pfam00650"
                     /db_xref="CDD:459890"
     CDS             1..317
                     /gene="TTPA"
                     /gene_synonym="alphaTTP; ATTP; AVED; TTP1"
                     /coded_by="NM_001413418.1:33..986"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:7274"
                     /db_xref="HGNC:HGNC:12404"
                     /db_xref="MIM:600415"
ORIGIN      
        1 maearsqpsa gpqlnalpdh spllqpglaa lrrrareagv plaplpltds fllrflrard
       61 fdldlawrll knyykwraec peisadlhpr siigllkagy hgvlrsrdpt gskvliyrie
      121 scsvaqageq waisthynlc lpsssdspas asqvagttah wdpkvftayd vfrvslitse
      181 livqevetqr ngikaifdle gwqfshafqi tpsvakkiaa vltdsfplkv rgihlinepv
      241 ifhavfsmik pfltekiker ihmhgnnykq sllqhfpdil pleyggeefs medicqewtn
      301 fimksedyls sisesiq
//
LOCUS       NP_001399997             333 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001399997 XP_047278421
VERSION     NP_001399997.1
DBSOURCE    REFSEQ: accession NM_001413068.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            On Oct 25, 2022 this sequence version replaced XP_047278421.1.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.362992.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..333
                     /product="mitochondrial fission regulator 1 isoform 1
                     precursor"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=31469
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=5550
     Region          22..251
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     mat_peptide     49..333
                     /product="Mitochondrial fission regulator 1.
                     /id=PRO_0000096622"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=31469
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15390.2)"
     Region          177..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          179..304
                     /region_name="Necessary and sufficient to promote
                     mitochondrial fission. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          288..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     CDS             1..333
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001413068.1:169..1170"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsvlwsrkpy gssrsivrki gtnlsliqcp rvqfqinsha
       61 tewspshpge davasfadvg wvakeegecs arlrtevrsr pplqddllff ekapsrqisl
      121 pdlsqeepql ktpalaneea lqkicalene laalraqiak ivtqqeqqnl tagdldsttf
      181 gtipphpppp ppplpppalg lhqstsavdl ikerrekran agktlvknnp kkpempnmle
      241 ilkemnsvkl rsvkrseqdv kpkpvdatdp aaliaealkk kfayryrsds qdevekgipk
      301 seseatserv lfgphmlkpt gkmkalienv sds
//
LOCUS       NP_001400294             365 aa            linear   PRI 21-NOV-2025
DEFINITION  telomeric repeat-binding factor 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001400294 XP_011515884
VERSION     NP_001400294.1
DBSOURCE    REFSEQ: accession NM_001413365.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Hu,H., van Roon,A.M., Ghanim,G.E., Ahsan,B., Oluwole,A.O.,
            Peak-Chew,S.Y., Robinson,C.V. and Nguyen,T.H.D.
  TITLE     Structural basis of telomeric nucleosome recognition by shelterin
            factor TRF1
  JOURNAL   Sci Adv 9 (34), eadi4148 (2023)
   PUBMED   37624885
  REMARK    GeneRIF: Structural basis of telomeric nucleosome recognition by
            shelterin factor TRF1.
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Harmak,H., Redouane,S., Charoute,H., Aniq Filali,O., Barakat,A. and
            Rouba,H.
  TITLE     In silico exploration and molecular dynamics of deleterious SNPs on
            the human TERF1 protein triggering male infertility
  JOURNAL   J Biomol Struct Dyn 41 (24), 14665-14688 (2023)
   PUBMED   36995171
  REMARK    GeneRIF: In silico exploration and molecular dynamics of
            deleterious SNPs on the human TERF1 protein triggering male
            infertility.
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Abreu,P.L., Lee,Y.W. and Azzalin,C.M.
  TITLE     In Vitro Characterization of the Physical Interactions between the
            Long Noncoding RNA TERRA and the Telomeric Proteins TRF1 and TRF2
  JOURNAL   Int J Mol Sci 23 (18), 10463 (2022)
   PUBMED   36142374
  REMARK    GeneRIF: In Vitro Characterization of the Physical Interactions
            between the Long Noncoding RNA TERRA and the Telomeric Proteins
            TRF1 and TRF2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Jack,A., Kim,Y., Strom,A.R., Lee,D.S.W., Williams,B., Schaub,J.M.,
            Kellogg,E.H., Finkelstein,I.J., Ferro,L.S., Yildiz,A. and
            Brangwynne,C.P.
  TITLE     Compartmentalization of telomeres through DNA-scaffolded phase
            separation
  JOURNAL   Dev Cell 57 (2), 277-290 (2022)
   PUBMED   35077681
  REMARK    GeneRIF: Compartmentalization of telomeres through DNA-scaffolded
            phase separation.
REFERENCE   6  (residues 1 to 365)
  AUTHORS   Broccoli,D., Chong,L., Oelmann,S., Fernald,A.A., Marziliano,N., van
            Steensel,B., Kipling,D., Le Beau,M.M. and de Lange,T.
  TITLE     Comparison of the human and mouse genes encoding the telomeric
            protein, TRF1: chromosomal localization, expression and conserved
            protein domains
  JOURNAL   Hum Mol Genet 6 (1), 69-76 (1997)
   PUBMED   9002672
REFERENCE   7  (residues 1 to 365)
  AUTHORS   Lu,K.P., Hanes,S.D. and Hunter,T.
  TITLE     A human peptidyl-prolyl isomerase essential for regulation of
            mitosis
  JOURNAL   Nature 380 (6574), 544-547 (1996)
   PUBMED   8606777
REFERENCE   8  (residues 1 to 365)
  AUTHORS   Bilaud,T., Koering,C.E., Binet-Brasselet,E., Ancelin,K.,
            Pollice,A., Gasser,S.M. and Gilson,E.
  TITLE     The telobox, a Myb-related telomeric DNA binding motif found in
            proteins from yeast, plants and human
  JOURNAL   Nucleic Acids Res 24 (7), 1294-1303 (1996)
   PUBMED   8614633
REFERENCE   9  (residues 1 to 365)
  AUTHORS   Chong,L., van Steensel,B., Broccoli,D., Erdjument-Bromage,H.,
            Hanish,J., Tempst,P. and de Lange,T.
  TITLE     A human telomeric protein
  JOURNAL   Science 270 (5242), 1663-1667 (1995)
   PUBMED   7502076
REFERENCE   10 (residues 1 to 365)
  AUTHORS   Zhong,Z., Shiue,L., Kaplan,S. and de Lange,T.
  TITLE     A mammalian factor that binds telomeric TTAGGG repeats in vitro
  JOURNAL   Mol Cell Biol 12 (11), 4834-4843 (1992)
   PUBMED   1406665
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022893.6.
            
            On Oct 31, 2022 this sequence version replaced XP_011515884.1.
            
            Summary: This gene encodes a telomere specific protein which is a
            component of the telomere nucleoprotein complex. This protein is
            present at telomeres throughout the cell cycle and functions as an
            inhibitor of telomerase, acting in cis to limit the elongation of
            individual chromosome ends. The protein structure contains a
            C-terminal Myb motif, a dimerization domain near its N-terminus and
            an acidic N-terminus. Multiple transcripts of this gene are
            alternatively spliced products. [provided by RefSeq, Aug 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1070081.1,
                                           SRR3476690.649618.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.11"
     Protein         1..365
                     /product="telomeric repeat-binding factor 1 isoform 5"
                     /note="NIMA-interacting protein 2; telomeric protein
                     Pin2/TRF1; TTAGGG repeat-binding factor 1; telomeric
                     repeat binding factor (NIMA-interacting) 1"
                     /calculated_mol_wt=42256
     Region          1..160
                     /region_name="TRFH"
                     /note="Telomeric Repeat binding Factor or TTAGGG Repeat
                     binding Factor, central (dimerization) domain Homology;
                     TRFH. Telomeres are protein/DNA complexes that make up the
                     physical ends of eukaryotic linear chromosomes and are
                     essential for chromosome stability; cl02779"
                     /db_xref="CDD:413471"
     Site            order(2,5,19,23,27,37..41,49,52..53,56)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238174"
     Region          307..355
                     /region_name="SANT_TRF"
                     /note="Telomere repeat binding factor-like DNA-binding
                     domains of the SANT/myb-like family; cd11660"
                     /db_xref="CDD:212558"
     Site            order(307..309,327,329..330,341,343..345,347..349,
                     351..352)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212558"
     CDS             1..365
                     /gene="TERF1"
                     /gene_synonym="hTRF1-AS; PIN2; t-TRF1; TRBF1; TRF; TRF1"
                     /coded_by="NM_001413365.1:412..1509"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:7013"
                     /db_xref="HGNC:HGNC:11728"
                     /db_xref="MIM:600951"
ORIGIN      
        1 mftiihglss ltacqlrtiy icqfltriaa gktldaqfen deritplesa lmiwgsieke
       61 hdklheeiqn likiqaiavc mengnfkeae evferifgdp nshmpfkskl lmiisqkdtf
      121 hsffqhfsyn hmmekiksyv nyvlseksst flmkaaakvv eskrtrtits qdkpsgndve
      181 meteanldtr ksvsdkqsav tessegtvsl lrshknlfls klqhgtqqqd lnkkerrvgt
      241 pqityicltk ltmnkkegvr kglcflvllk hyrtkkkkes rratesripv sksqpvtpek
      301 hrarkrqawl weedknlrsg vrkygegnws killhykfnn rtsvmlkdrw rtmkklklis
      361 sdsed
//
LOCUS       NP_001398005            2000 aa            linear   PRI 21-NOV-2025
DEFINITION  protein TANC2 isoform 3 [Homo sapiens].
ACCESSION   NP_001398005 XP_047291692
VERSION     NP_001398005.1
DBSOURCE    REFSEQ: accession NM_001411076.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2000)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2000)
  AUTHORS   Broniarczyk,J.K., Massimi,P., Trejo-Cerro,O., Myers,M.P. and
            Banks,L.
  TITLE     HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in a
            PBM-Dependent Manner and Promotes Increased Cell Proliferation
  JOURNAL   J Virol 96 (22), e0136522 (2022)
   PUBMED   36326272
  REMARK    GeneRIF: HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in
            a PBM-Dependent Manner and Promotes Increased Cell Proliferation.
REFERENCE   3  (residues 1 to 2000)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2000)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 2000)
  AUTHORS   Kim,S.G., Lee,S., Kim,Y., Park,J., Woo,D., Kim,D., Li,Y., Shin,W.,
            Kang,H., Yook,C., Lee,M., Kim,K., Roh,J.D., Ryu,J., Jung,H.,
            Um,S.M., Yang,E., Kim,H., Han,J., Heo,W.D. and Kim,E.
  TITLE     Tanc2-mediated mTOR inhibition balances mTORC1/2 signaling in the
            developing mouse brain and human neurons
  JOURNAL   Nat Commun 12 (1), 2695 (2021)
   PUBMED   33976205
  REMARK    GeneRIF: Tanc2-mediated mTOR inhibition balances mTORC1/2 signaling
            in the developing mouse brain and human neurons.
            Erratum:[Nat Commun. 2022 Nov 1;13(1):6544. doi:
            10.1038/s41467-022-33972-9. PMID: 36319630]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2000)
  AUTHORS   Guo,H., Bettella,E., Marcogliese,P.C., Zhao,R., Andrews,J.C.,
            Nowakowski,T.J., Gillentine,M.A., Hoekzema,K., Wang,T., Wu,H.,
            Jangam,S., Liu,C., Ni,H., Willemsen,M.H., van Bon,B.W., Rinne,T.,
            Stevens,S.J.C., Kleefstra,T., Brunner,H.G., Yntema,H.G., Long,M.,
            Zhao,W., Hu,Z., Colson,C., Richard,N., Schwartz,C.E., Romano,C.,
            Castiglia,L., Bottitta,M., Dhar,S.U., Erwin,D.J., Emrick,L.,
            Keren,B., Afenjar,A., Zhu,B., Bai,B., Stankiewicz,P., Herman,K.,
            Mercimek-Andrews,S., Juusola,J., Wilfert,A.B., Abou Jamra,R.,
            Buttner,B., Mefford,H.C., Muir,A.M., Scheffer,I.E., Regan,B.M.,
            Malone,S., Gecz,J., Cobben,J., Weiss,M.M., Waisfisz,Q.,
            Bijlsma,E.K., Hoffer,M.J.V., Ruivenkamp,C.A.L., Sartori,S., Xia,F.,
            Rosenfeld,J.A., Bernier,R.A., Wangler,M.F., Yamamoto,S., Xia,K.,
            Stegmann,A.P.A., Bellen,H.J., Murgia,A. and Eichler,E.E.
  CONSRTM   University of Washington Center for Mendelian Genomics
  TITLE     Disruptive mutations in TANC2 define a neurodevelopmental syndrome
            associated with psychiatric disorders
  JOURNAL   Nat Commun 10 (1), 4679 (2019)
   PUBMED   31616000
  REMARK    GeneRIF: Pediatric patients with disruptive TANC2 mutations present
            with autism, intellectual disability, and delayed language and
            motor development. In addition to a variable degree of epilepsy and
            facial dysmorphism, we observe a pattern of more complex
            psychiatric dysfunction or behavioral problems in adult probands or
            carrier parents.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 2000)
  AUTHORS   Stucchi,R., Plucinska,G., Hummel,J.J.A., Zahavi,E.E., Guerra San
            Juan,I., Klykov,O., Scheltema,R.A., Altelaar,A.F.M. and
            Hoogenraad,C.C.
  TITLE     Regulation of KIF1A-Driven Dense Core Vesicle Transport: Ca2+/CaM
            Controls DCV Binding and Liprin-alpha/TANC2 Recruits DCVs to
            Postsynaptic Sites
  JOURNAL   Cell Rep 24 (3), 685-700 (2018)
   PUBMED   30021165
REFERENCE   8  (residues 1 to 2000)
  AUTHORS   Gasparini,A., Tosatto,S.C.E., Murgia,A. and Leonardi,E.
  TITLE     Dynamic scaffolds for neuronal signaling: in silico analysis of the
            TANC protein family
  JOURNAL   Sci Rep 7 (1), 6829 (2017)
   PUBMED   28754924
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 2000)
  AUTHORS   Mahmood,S.F., Gruel,N., Chapeaublanc,E., Lescure,A., Jones,T.,
            Reyal,F., Vincent-Salomon,A., Raynal,V., Pierron,G., Perez,F.,
            Camonis,J., Del Nery,E., Delattre,O., Radvanyi,F. and
            Bernard-Pierrot,I.
  TITLE     A siRNA screen identifies RAD21, EIF3H, CHRAC1 and TANC2 as driver
            genes within the 8q23, 8q24.3 and 17q23 amplicons in breast cancer
            with effects on cell growth, survival and transformation
  JOURNAL   Carcinogenesis 35 (3), 670-682 (2014)
   PUBMED   24148822
  REMARK    GeneRIF: -RAD21 and EIF3H, both on chromosome 8q23, CHRAC1 on
            chromosome 8q24.3 and TANC2 on chromosome 17q23-were confirmed to
            be driver genes regulating the proliferation/survival of clonogenic
            breast cancer cells
REFERENCE   10 (residues 1 to 2000)
  AUTHORS   Han,S., Nam,J., Li,Y., Kim,S., Cho,S.H., Cho,Y.S., Choi,S.Y.,
            Choi,J., Han,K., Kim,Y., Na,M., Kim,H., Bae,Y.C., Choi,S.Y. and
            Kim,E.
  TITLE     Regulation of dendritic spines, spatial memory, and embryonic
            development by the TANC family of PSD-95-interacting proteins
  JOURNAL   J Neurosci 30 (45), 15102-15112 (2010)
   PUBMED   21068316
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005972.1, AC006270.1, AC015923.8 and AC005828.1.
            
            On Aug 20, 2022 this sequence version replaced XP_047291692.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2260699.1,
                                           SRR18074969.487402.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2000
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.2-q23.3"
     Protein         1..2000
                     /product="protein TANC2 isoform 3"
                     /note="putative ankyrin-repeat containing protein; rolling
                     pebbles homolog B; protein TANC2; tetratricopeptide
                     repeat, ankyrin repeat and coiled-coil domain-containing
                     protein 2"
                     /calculated_mol_wt=220616
     Region          1..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          129..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          396..442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          846..878
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          856..>1150
                     /region_name="PHA03095"
                     /note="ankyrin-like protein; Provisional"
                     /db_xref="CDD:222980"
     Region          884..913
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          889..915
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(890..891,894..896,898..899,903,906,915,917,919,
                     923..924,927..929,931..932,936,939,948,950,952,956..957,
                     960..962,964..965,969,972)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          917..948
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          917..946
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          950..979
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          990..1019
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1026..1225
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1033..1062
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1034..1064
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1066..1097
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1066..1095
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1099..1128
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1100..1130
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1101,1105..1106,1109..1111,1113..1114,1118,1121,
                     1130,1132,1134,1138..1139,1142..1144,1146..1147,1151,1154,
                     1163,1165,1167,1171..1172,1175..1177,1179..1180,1184,1187,
                     1196)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1132..1163
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1132..1161
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1165..1196
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1165..1194
                     /region_name="ANK 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1198..1228
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1254..1287
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1257..1282
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(1258..1259,1262..1263,1265,1302,1305..1306,
                     1309..1310,1312..1313,1336,1339..1340,1343..1344,1347)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          1261..>1375
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          1287..1330
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1301..1334
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1335..1368
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1335..1363
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1382..1411
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          <1437..1666
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1440..1596
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1452
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1555
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1573
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:A2A690; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1586
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:A2A690; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1589
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1702..1728
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1732
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1793..1813
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1831..1853
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2A690; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1837
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1938
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:A2A690; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1978..2000
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     CDS             1..2000
                     /gene="TANC2"
                     /gene_synonym="IDDALDS; rols; ROLSA"
                     /coded_by="NM_001411076.1:539..6541"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92375.1"
                     /db_xref="GeneID:26115"
                     /db_xref="HGNC:HGNC:30212"
                     /db_xref="MIM:615047"
ORIGIN      
        1 mfrnslkmll tggkssrknr ssdggseepp drrqssvdsr qsrsgqggis tesdcafepd
       61 yavpplpvse gdaeqelgpp psvdeaantl mtrlgfllge kvtevqpgdq ysmevqdenq
      121 tsaitqrisp cstltsstas ppasspcstl ppistnatak dcsygavtsp tstlesrdsg
      181 iiatltsyse nvertkyage sskelgsggn ikpwqsqkss mdsclyrvde nmtastysln
      241 kipernletv lsqsvqsipl ylmprpnsva atssahledl ayldeqrhtp lrtslrmprq
      301 smggartqqd lrvrfapyrp pdislkpllf evpsittesv fvgrdwvfhe idaqlqssna
      361 svnqgvvivg nigfgktaii srlvalschg trmrqiasds phaspkhvda nrelpltqpp
      421 sahssitsgs cpgtpemrrr qeeamrrlas qvvayhycqa dnaytclvpe fvhnvaallc
      481 rspqltayre qllrephlqs mlslrscvqd pmasfrrgvl eplenlhker kipdedfiil
      541 idglneaefh kpdygdtivs flskmigkfp swlklivtvr tslqeitkll pfhrifldrl
      601 eeneaidqdl qayilhrihs sseiqnnisl ngkmdnttfg klsshlktls qgsylylklt
      661 fdliekgylv lksssykvvp vslsevyllq cnmkfptqss fdrvmpllnv avaslhpltd
      721 ehifqainag siegtlewed fqqrmenlsm flikrrdmtr mfvhpsfrew liwreegekt
      781 kflcdprsgh tllafwfsrq egklnrqqti elghhilkah ifkglskkvg vsssilqglw
      841 isysteglsm alaslrnlyt pnikvsrlli lgganinyrt evlnnapilc vqshlgytem
      901 valllefgan vdassesglt plgyaaaagy lsivvllckk rakvdhldkn gqcalvhaal
      961 rghlevvkfl iqcdwtmagq qqgvfkksha iqqaliaaas mgyteivsyl ldlpekdeee
     1021 veraqinsfd slwgetalta aagrgklevc rllleqgaav aqpnrrgavp lfstvrqghw
     1081 qivdlllthg advnmadkqg rtplmmaase ghlgtvdfll aqgasialmd kegltalswa
     1141 clkghlsvvr slvdngaatd hadkngrtpl dlaafygdae vvqflvdhga miehvdysgm
     1201 rpldravgcr ntsvvvtllk kgakigcqtl psrprgpatw amatskpdim iillsklmee
     1261 gdmfykkgkv keaaqryqya lkkfpregfg edlktfrelk vslllnlsrc rrkmndfgma
     1321 eefatkalel kpksyeayya rarakrssrq faaaledlne aiklcpnnre iqrlllrvee
     1381 ecrqmqqpqq pppppqpqqq lpeeaepepq hediysvqdi feeeyleqdv envsiglqte
     1441 arpsqglpvi qsppsspphr dsayissspl gshqvfdfrs sssvgsptrq tyqstspals
     1501 pthqnshyrp spphtspahq ggsyrfsppp vggqgkeyps pppsplrrgp qyrasppaes
     1561 msvyrsqsgs pvryqqetsv sqlpgrpksp lskmaqrpyq mpqlpvavpq qglrlqpaka
     1621 qivrsnqpsp avhsstvipt gaygqvahsm askyqssqgd igvsqsrlvy qgsiggivgd
     1681 grpvqhvqas lsagaicqhg gltkedlpqr pssayrggvr ysqtpqigrs qsasyypvch
     1741 skldlersss qlgspdvshl irrpisvnpn eikphpptpr pllhsqsvgl rfspssnsis
     1801 stsnltptfr psssiqqmei plkpayersc delspvsptq ggypseptrs rttpfmgiid
     1861 ktartqqyph lhqqnrtwav ssvdtvlspt spgnlpqpes fsppssisni afynktnnaq
     1921 nghlleddyy sphgmlangs rgdllervsq assypdvkva rtlpvaqayq dnlyrqlsrd
     1981 srqgqtspik pkrpfvesnv
//
LOCUS       NP_001427591             754 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 3 isoform 10 [Homo sapiens].
ACCESSION   NP_001427591
VERSION     NP_001427591.1
DBSOURCE    REFSEQ: accession NM_001440662.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Ghashghaei,M., Liu,Y., Ettles,J., Bombaci,G., Ramkumar,N., Liu,Z.,
            Escano,L., Miko,S.S., Kim,Y., Waldron,J.A., Do,K., MacPherson,K.,
            Yuen,K.A., Taibi,T., Yue,M., Arsalan,A., Jin,Z., Edin,G.,
            Karsan,A., Morin,G.B., Kuchenbauer,F., Perna,F., Bushell,M. and
            Vu,L.P.
  TITLE     Translation efficiency driven by CNOT3 subunit of the CCR4-NOT
            complex promotes leukemogenesis
  JOURNAL   Nat Commun 15 (1), 2340 (2024)
   PUBMED   38491013
  REMARK    GeneRIF: Translation efficiency driven by CNOT3 subunit of the
            CCR4-NOT complex promotes leukemogenesis.
            Erratum:[Nat Commun. 2024 Oct 7;15(1):8674. doi:
            10.1038/s41467-024-53071-1. PMID: 39375334]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Burgess,H.M., Grande,R., Riccio,S., Dinesh,I., Winkler,G.S.,
            Depledge,D.P. and Mohr,I.
  TITLE     CCR4-NOT differentially controls host versus virus poly(a)-tail
            length and regulates HCMV infection
  JOURNAL   EMBO Rep 24 (12), e56327 (2023)
   PUBMED   37846490
  REMARK    GeneRIF: CCR4-NOT differentially controls host versus virus
            poly(a)-tail length and regulates HCMV infection.
REFERENCE   4  (residues 1 to 754)
  AUTHORS   Zhao,P., Meng,Q., Wan,C., Lei,T., Zhang,L., Zhang,X., Tan,L.,
            Zhu,H. and He,X.
  TITLE     Clinical features of CNOT3-associated neurodevelopmental disorder
            in three Chinese patients
  JOURNAL   Neurogenetics 24 (2), 129-136 (2023)
   PUBMED   36802310
  REMARK    GeneRIF: Clinical features of CNOT3-associated neurodevelopmental
            disorder in three Chinese patients.
REFERENCE   5  (residues 1 to 754)
  AUTHORS   McLenachan,S., Zhang,D., Grainok,J., Zhang,X., Huang,Z., Chen,S.C.,
            Zaw,K., Lima,A., Jennings,L., Roshandel,D., Moon,S.Y., Heath
            Jeffery,R.C., Attia,M.S., Thompson,J.A., Lamey,T.M., McLaren,T.L.,
            De Roach,J., Fletcher,S. and Chen,F.K.
  TITLE     Determinants of Disease Penetrance in PRPF31-Associated Retinopathy
  JOURNAL   Genes (Basel) 12 (10), 1542 (2021)
   PUBMED   34680937
  REMARK    GeneRIF: Determinants of Disease Penetrance in PRPF31-Associated
            Retinopathy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 754)
  AUTHORS   Yin,X., Warner,D.R., Roberts,E.A., Pisano,M.M. and Greene,R.M.
  TITLE     Identification of novel CBP interacting proteins in embryonic
            orofacial tissue
  JOURNAL   Biochem Biophys Res Commun 329 (3), 1010-1017 (2005)
   PUBMED   15752756
REFERENCE   7  (residues 1 to 754)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 754)
  AUTHORS   Aoki,T., Okada,N., Wakamatsu,T. and Tamura,T.A.
  TITLE     TBP-interacting protein 120B, which is induced in relation to
            myogenesis, binds to NOT3
  JOURNAL   Biochem Biophys Res Commun 296 (5), 1097-1103 (2002)
   PUBMED   12207886
  REMARK    GeneRIF: TBP-interacting protein 120B binds to NOT3
REFERENCE   9  (residues 1 to 754)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
REFERENCE   10 (residues 1 to 754)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC245052.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.589479.1,
                                           SRR14038194.4123520.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..754
                     /product="CCR4-NOT transcription complex subunit 3 isoform
                     10"
                     /note="NOT3 (negative regulator of transcription 3, yeast)
                     homolog; CCR4-associated factor 3; leukocyte receptor
                     cluster member 2"
                     /calculated_mol_wt=81869
     Region          3..230
                     /region_name="Not3"
                     /note="Not1 N-terminal domain, CCR4-Not complex component;
                     pfam04065"
                     /db_xref="CDD:461155"
     Region          241..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75175.1)"
     Region          <289..660
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Region          621..746
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     Region          662..754
                     /region_name="Repressor domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O75175.1)"
     CDS             1..754
                     /gene="CNOT3"
                     /gene_synonym="IDDSADF; LENG2; NOT3; NOT3H"
                     /coded_by="NM_001440662.1:521..2785"
                     /note="isoform 10 is encoded by transcript variant 11"
                     /db_xref="GeneID:4849"
                     /db_xref="HGNC:HGNC:7879"
                     /db_xref="MIM:604910"
ORIGIN      
        1 madkrklqge idrclkkvse gveqfediwq klhnaananq kekyeadlkk eikklqrlrd
       61 qiktwvasne ikdkrqlidn rklietqmer fkvveretkt kayskeglgl aqkvdpaqke
      121 keevgqwltn tidtlnmqvd qfesevesls vqtrkkkgdk dqkqdriegl krhiekhryh
      181 vrmletilrm ldndsilvda irkikddvey yvdssqdpdf eeneflyddl dledipqalv
      241 atsppshshm edeifnqsss tptsttsssp ippspanctt enseddkkrg rstdsevsqs
      301 pakngskpvh snqhpqspav pptypsgppp aasalsttpg nngvpapaap psalgpkasp
      361 apshnsgtpa pyaqavappa psgpsttqpr ppsvqpsggg gggsggggss sssnssaggg
      421 agkqngatsy ssvvadspae valsssggnn assqalgpps gphnpppsts kepsaaaptg
      481 aggvapgsgn nsggpsllvp lpvnppsspt psfsdakaag allngppqfs tapeikapep
      541 lsslksmaer aaissgiedp vptlhlterd iilsstsapp asaqpplqls evniplslgv
      601 cplgpvpltk eqlyqqamee aawhhmphps dserirqylp rnpcptppyh hqmppphsdt
      661 vefyqrlste tlffifyyle gtkaqylaak alkkqswrfh tkymmwfqrh eepktitdef
      721 eqgtyiyfdy ekwgqrkkeg ftfeyryled rdlq
//
LOCUS       NP_001427360            2857 aa            linear   PRI 21-NOV-2025
DEFINITION  lipopolysaccharide-responsive and beige-like anchor protein isoform
            4 [Homo sapiens].
ACCESSION   NP_001427360 XP_005263431 XP_054207314
VERSION     NP_001427360.1
DBSOURCE    REFSEQ: accession NM_001440431.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2857)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2857)
  AUTHORS   Szentgyorgyi,V., Lueck,L.M., Overwijn,D., Ritz,D., Zoeller,N.,
            Schmidt,A., Hondele,M., Spang,A. and Bakhtiar,S.
  TITLE     Arf1-dependent LRBA recruitment to Rab4 endosomes is required for
            endolysosome homeostasis
  JOURNAL   J Cell Biol 223 (11) (2024)
   PUBMED   39325073
  REMARK    GeneRIF: Arf1-dependent LRBA recruitment to Rab4 endosomes is
            required for endolysosome homeostasis.
REFERENCE   3  (residues 1 to 2857)
  AUTHORS   Freund,T., Baxter,S.K., Walsh,T., Golan,H., Kapelushnik,J.,
            Abramsohn-Goldenberg,M., Benor,S., Sarid,N., Ram,R., Alcalay,Y.,
            Segel,R., Renbaum,P., Stepensky,P., King,M.C., Torgerson,T.R. and
            Hagin,D.
  TITLE     Clinically Complex LRBA Deficiency Due to a Founder Allele in the
            Georgian Jewish Population
  JOURNAL   J Clin Immunol 43 (1), 151-164 (2023)
   PUBMED   36063261
  REMARK    GeneRIF: Clinically Complex LRBA Deficiency Due to a Founder Allele
            in the Georgian Jewish Population.
REFERENCE   4  (residues 1 to 2857)
  AUTHORS   Catak,M.C., Akcam,B., Bilgic Eltan,S., Babayeva,R., Karakus,I.S.,
            Akgun,G., Baser,D., Bulutoglu,A., Bayram,F., Kasap,N., Kiykim,A.,
            Hancioglu,G., Kokcu Karadag,S.I., Kendir Demirkol,Y., Ozen,S.,
            Cekic,S., Ozcan,D., Edeer Karaca,N., Sasihuseyinoglu,A.S.,
            Cansever,M., Ozek Yucel,E., Tamay,Z., Altintas,D.U., Aydogmus,C.,
            Celmeli,F., Cokugras,H., Gulez,N., Genel,F., Metin,A., Guner,S.N.,
            Kutukculer,N., Keles,S., Reisli,I., Kilic,S.S., Yildiran,A.,
            Karakoc-Aydiner,E., Lo,B., Ozen,A. and Baris,S.
  TITLE     Comparing the levels of CTLA-4-dependent biological defects in
            patients with LRBA deficiency and CTLA-4 insufficiency
  JOURNAL   Allergy 77 (10), 3108-3123 (2022)
   PUBMED   35491430
  REMARK    GeneRIF: Comparing the levels of CTLA-4-dependent biological
            defects in patients with LRBA deficiency and CTLA-4 insufficiency.
REFERENCE   5  (residues 1 to 2857)
  AUTHORS   Yao,J., Gu,H., Mou,W., Chen,Z., Ma,J., Ma,H., Li,N., Zhang,R.,
            Wang,T., Jiang,J. and Wu,R.
  TITLE     Various phenotypes of LRBA gene with compound heterozygous
            variation: A case series report of pediatric cytopenia patients
  JOURNAL   Int J Immunopathol Pharmacol 36, 3946320221125591 (2022)
   PUBMED   36074705
  REMARK    GeneRIF: Various phenotypes of LRBA gene with compound heterozygous
            variation: A case series report of pediatric cytopenia patients.
REFERENCE   6  (residues 1 to 2857)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 2857)
  AUTHORS   Gebauer,D., Li,J., Jogl,G., Shen,Y., Myszka,D.G. and Tong,L.
  TITLE     Crystal structure of the PH-BEACH domains of human LRBA/BGL
  JOURNAL   Biochemistry 43 (47), 14873-14880 (2004)
   PUBMED   15554694
  REMARK    GeneRIF: The crystal structure of the aPH-BEACH domains of LRBA
            were studied.
REFERENCE   8  (residues 1 to 2857)
  AUTHORS   Dyomin,V.G., Chaganti,S.R., Dyomina,K., Palanisamy,N., Murty,V.V.,
            Dalla-Favera,R. and Chaganti,R.S.
  TITLE     BCL8 is a novel, evolutionarily conserved human gene family
            encoding proteins with presumptive protein kinase A anchoring
            function
  JOURNAL   Genomics 80 (2), 158-165 (2002)
   PUBMED   12160729
REFERENCE   9  (residues 1 to 2857)
  AUTHORS   Wang,J.W., Howson,J., Haller,E. and Kerr,W.G.
  TITLE     Identification of a novel lipopolysaccharide-inducible gene with
            key features of both A kinase anchor proteins and chs1/beige
            proteins
  JOURNAL   J Immunol 166 (7), 4586-4595 (2001)
   PUBMED   11254716
REFERENCE   10 (residues 1 to 2857)
  AUTHORS   Feuchter,A.E., Freeman,J.D. and Mager,D.L.
  TITLE     Strategy for detecting cellular transcripts promoted by human
            endogenous long terminal repeats: identification of a novel gene
            (CDC4L) with homology to yeast CDC4
  JOURNAL   Genomics 13 (4), 1237-1246 (1992)
   PUBMED   1505956
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104796.4, AC092544.4,
            AC110813.4, AC097373.3, AC092612.3 and AC093748.3.
            
            On or before May 20, 2025 this sequence version replaced
            XP_005263431.1, XP_054207314.1.
            
            Summary: The protein encoded by this gene is a member of the
            WDL-BEACH-WD (WBW) gene family. Its expression is induced in B
            cells and macrophages by bacterial lipopolysaccharides (LPS). The
            encoded protein associates with protein kinase A and may be
            involved in leading intracellular vesicles to activated receptor
            complexes, which aids in the secretion and/or membrane deposition
            of immune effector molecules. Defects in this gene are associated
            with the disorder common variable immunodeficiency-8 with
            autoimmunity. Two transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Dec 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.23492.1,
                                           SRR14038193.1790334.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2857
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.3"
     Protein         1..2857
                     /product="lipopolysaccharide-responsive and beige-like
                     anchor protein isoform 4"
                     /note="vesicle trafficking, beach and anchor containing;
                     lipopolysaccharide-responsive and beige-like anchor
                     protein; CDC4-like protein; LPS-responsive vesicle
                     trafficking, beach and anchor containing"
                     /calculated_mol_wt=318291
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          229..376
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
     Region          441..921
                     /region_name="DUF4704"
                     /note="Neurobeachin/BDCP, DUF4704 alpha solenoid region;
                     pfam15787"
                     /db_xref="CDD:464870"
     Region          969..1005
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            979
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1003
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1018..1039
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1161..1193
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1301..1343
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1531..1548
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          1586..1668
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1759..1789
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1770
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1880..2047
                     /region_name="DUF1088"
                     /note="Neurobeachin-like, DUF1088; pfam06469"
                     /db_xref="CDD:461925"
     Site            2053
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          2073..2170
                     /region_name="PH_BEACH"
                     /note="PH domain associated with Beige/BEACH; pfam14844"
                     /db_xref="CDD:434260"
     Region          2201..2478
                     /region_name="Beach"
                     /note="Beige/BEACH domain; smart01026"
                     /db_xref="CDD:214982"
     Site            2490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          2578..2842
                     /region_name="NBCH_WD40"
                     /note="Neurobeachin beta propeller domain; pfam20426"
                     /db_xref="CDD:466575"
     Region          2585..2627
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2594..2630
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2630..2673
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2636..2689
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2689..2729
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2694..2729
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2734..2763
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2771..2810
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2776..2810
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2813..2852
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     CDS             1..2857
                     /gene="LRBA"
                     /gene_synonym="BGL; CDC4L; CVID8; LAB300; LBA; uc.147"
                     /coded_by="NM_001440431.1:303..8876"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:987"
                     /db_xref="HGNC:HGNC:1742"
                     /db_xref="MIM:606453"
ORIGIN      
        1 masednrvps ppptgddggg ggreetpteg galslkpglp irgirmkfav ltglvevgev
       61 snrdivetvf nllvggqfdl emnfiiqege sincmvdlle kcditcqaev wsmftailkk
      121 sirnlqvcte vglvekvlgk iekvdnmiad llvdmlgvla synltvrelk lffsklqgdk
      181 grwpphagkl lsvlkhmpqk ygpdaffnfp gksaaaialp piakwpyqng ftfhtwlrmd
      241 pvnninvdkd kpylycfrts kglgysahfv ggclivtsik skgkgfqhcv kfdfkpqkwy
      301 mvtivhiynr wknselrcyv ngelasygei twfvntsdtf dkcflgsset adanrvfcgq
      361 mtavylfsea lnaaqifaiy qlglgykgtf kfkaesdlfl aehhklllyd gklssaiaft
      421 ynpratdaql clesspkdnp sifvhsphal mlqdvkavlt hsiqsamhsi ggvqvlfplf
      481 aqldyrqyls deidlticst llafimellk nsiamqeqml ackgflvigy sleksskshv
      541 sravlelcla fskylsnlqn gmpllkqlcd hvllnpaiwi htpakvqlml ytylstefig
      601 tvniyntirr vgtvllimht lkyyywavnp qdrsgitpkg ldgprpnqke mlslrafllm
      661 fikqlvmkds gvkedelqai lnylltmhed dnlmdvlqll valmsehpns mipafdqrng
      721 lrviykllas ksegirvqal kamgyflkhl apkrkaevml ghglfsllae rlmlqtnlit
      781 mttynvlfei lieqigtqvi hkqhpdpdss vkiqnpqilk viatllrnsp qcpesmevrr
      841 aflsdmiklf nnsrenrrsl lqcsvwqewm lslcyfnpkn sdeqkitemv yaifrillyh
      901 avkyewggwr vwvdtlsith skvtfeihke nlanifreqq gkvdeeiglc sstsvqaasg
      961 irrdinvsvg sqqpdtkdsp vcphfttngn enssiektss lesasnielq ttntsyeemk
     1021 aeqenqelpd egtleetltn etrnaddlev ssdiieavai ssnsfittgk dsmtvsevta
     1081 sisspseeda sempefldks iveeeedddy velkvegspt eeanlptelq dnslspaase
     1141 agekldmfgn ddklifqegk pvtekqtdte tqdskdsgiq tmtasgssam spettvsqia
     1201 vesdlgqmle egkkatnltr etklindchg svseasseqk iakldvsnva tdterlelka
     1261 spnveapqph rhvleisrqh eqpgqgiapd avngqrrdsr stvfripefn wsqmhqrllt
     1321 dllfsietdi qmwrshstkt vmdfvnssdn vifvhntihl isqvmdnmvm acggilplls
     1381 aatsathele nieptqglsi easvtflqrl islvdvlifa sslgfteiea eksmssggil
     1441 rqclrlvcav avrnclecqq hsqlktrgdk alkpmhslip lgksaakspv divtggispv
     1501 rdldrllqdm dinrlravvf rdiedskqaq flalavvyfi svlmvskyrd ilepqnerhs
     1561 qsctetgsen envslseitp aafstlttas veesestssa rrrdsgigee tatglgshve
     1621 vtphtappgv sagpdaisev lstlslevnk spetkndrgn dldtkatpsv svsknvnvkd
     1681 ilrslvnipa dgvtvdpall ppaclgalgd lsveqpvqfr sfdrsvivaa kksavspstf
     1741 ntsiptnavs vvssvdsaqa sdmggespgs rssnaklpsv ptvdsvsqdp vsnmsiterl
     1801 ehalekaapl lreifvdfap flsrtllgsh gqelliegts lvcmkssssv velvmllcsq
     1861 ewqnsiqkna glafielvne grllsqtmkd hlvrvaneae filsrqraed ihrhaefesl
     1921 caqysadkre dekmcdhlir aakyrdhvta tqliqkiini ltdkhgawgn savsrplefw
     1981 rldyweddlr rrrrfvrnpl gsthpeatlk tavehatded ilakgkqsir sqalgnqnse
     2041 neillegddd tlssvdekdl enlagpvsls tpaqlvapsv vvkgtlsvts selyfevdee
     2101 dpnfkkidpk ilayteglhg kwlfteirsi fsrryllqnt aleifmanrv avmfnfpdpa
     2161 tvkkvvnylp rvgvgtsfgl pqtrrislas prqlfkasnm tqrwqhreis nfeylmflnt
     2221 iagrsyndln qypvfpwvit nyeseeldlt lptnfrdlsk pigalnpkra affaeryesw
     2281 eddqvpkfhy gthystasfv lawllriepf ttyflnlqgg kfdhadrtfs sisrawrnsq
     2341 rdtsdikeli pefyylpemf vnfnnynlgv mddgtvvsdv elppwaktse efvhinrlal
     2401 esefvscqlh qwidlifgyk qqgpeavral nvfyyltyeg avnlnsitdp vlreaveaqi
     2461 rsfgqtpsql liephpprgs amqvylllqs plmftdkaqq dvimvlkfps nspvthvaan
     2521 tqpglatpav itvtanrlfa vnkwhnlpah qgavqdqpyq lpveidplia sntgmhrrqi
     2581 tdlldqsiqv hsqcfvitsd nryilvcgfw dksfrvystd tgrliqvvfg hwdvvtclar
     2641 sesyiggncy ilsgsrdatl llwywngkcs gigdnpgset aaprailtgh dyevtcaavc
     2701 aelglvlsgs qegpclihsm ngdllrtleg penclkpkli qasreghcvi fyenglfctf
     2761 svngklqatm etddniraiq lsrdgqyllt ggdrgvvvvr qvsdlkqlfa ypgcdagira
     2821 malsydqrci isgmasgsiv lfyndfnrwh heyqtry
//
LOCUS       NP_001139310             300 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001139310
VERSION     NP_001139310.1
DBSOURCE    REFSEQ: accession NM_001145838.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 300)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 300)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 300)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 300)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            coding region, compared to variant 1. The encoded isoform (2) is
            shorter than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2092279.1,
                                           SRR14038194.287232.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..300
                     /product="mitochondrial fission regulator 1 isoform 2"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=33069
     Region          25..218
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     CDS             1..300
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001145838.2:132..1034"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55240.1"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsinshatew spshpgedav asfadvgwva keegecsarl
       61 rtevrsrppl qddllffeka psrqislpdl sqeepqlktp alaneealqk icalenelaa
      121 lraqiakivt qqeqqnltag dldsttfgti pphppppppp lpppalglhq stsavdlike
      181 rrekranagk tlvknnpkkp empnmleilk emnsvklrsv krseqdvkpk pvdatdpaal
      241 iaealkkkfa yryrsdsqde vekgipkses eatservlfg phmlkptgkm kalienvsds
//
LOCUS       NP_001400231             280 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 3 [Homo sapiens].
ACCESSION   NP_001400231 XP_016868557
VERSION     NP_001400231.1
DBSOURCE    REFSEQ: accession NM_001413302.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 280)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 280)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 280)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC103816.2, AC027043.7, AC087368.7 and AC009901.6.
            
            On Oct 31, 2022 this sequence version replaced XP_016868557.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.500536.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..280
                     /product="RNA-binding Raly-like protein isoform 3"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=30943
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          188..>233
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     CDS             1..280
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413302.1:456..1298"
                     /note="isoform 3 is encoded by transcript variant 29"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly sgyvfdydyy
      121 rddfynrlfd yhgrvppppr aviplkrprv avtttrrgkg vfsmkggsrs tasgstgskl
      181 ksdelqtikk eltqiktkid sllgrlekie kqqkaeaeaq kkqleeslvl iqeecvseia
      241 dhsteepaeg gpdadgeemt dgieedfded gghelflqik
//
LOCUS       NP_001400303             347 aa            linear   PRI 21-NOV-2025
DEFINITION  telomeric repeat-binding factor 1 isoform 14 [Homo sapiens].
ACCESSION   NP_001400303
VERSION     NP_001400303.1
DBSOURCE    REFSEQ: accession NM_001413374.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Hu,H., van Roon,A.M., Ghanim,G.E., Ahsan,B., Oluwole,A.O.,
            Peak-Chew,S.Y., Robinson,C.V. and Nguyen,T.H.D.
  TITLE     Structural basis of telomeric nucleosome recognition by shelterin
            factor TRF1
  JOURNAL   Sci Adv 9 (34), eadi4148 (2023)
   PUBMED   37624885
  REMARK    GeneRIF: Structural basis of telomeric nucleosome recognition by
            shelterin factor TRF1.
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Harmak,H., Redouane,S., Charoute,H., Aniq Filali,O., Barakat,A. and
            Rouba,H.
  TITLE     In silico exploration and molecular dynamics of deleterious SNPs on
            the human TERF1 protein triggering male infertility
  JOURNAL   J Biomol Struct Dyn 41 (24), 14665-14688 (2023)
   PUBMED   36995171
  REMARK    GeneRIF: In silico exploration and molecular dynamics of
            deleterious SNPs on the human TERF1 protein triggering male
            infertility.
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Abreu,P.L., Lee,Y.W. and Azzalin,C.M.
  TITLE     In Vitro Characterization of the Physical Interactions between the
            Long Noncoding RNA TERRA and the Telomeric Proteins TRF1 and TRF2
  JOURNAL   Int J Mol Sci 23 (18), 10463 (2022)
   PUBMED   36142374
  REMARK    GeneRIF: In Vitro Characterization of the Physical Interactions
            between the Long Noncoding RNA TERRA and the Telomeric Proteins
            TRF1 and TRF2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Jack,A., Kim,Y., Strom,A.R., Lee,D.S.W., Williams,B., Schaub,J.M.,
            Kellogg,E.H., Finkelstein,I.J., Ferro,L.S., Yildiz,A. and
            Brangwynne,C.P.
  TITLE     Compartmentalization of telomeres through DNA-scaffolded phase
            separation
  JOURNAL   Dev Cell 57 (2), 277-290 (2022)
   PUBMED   35077681
  REMARK    GeneRIF: Compartmentalization of telomeres through DNA-scaffolded
            phase separation.
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Broccoli,D., Chong,L., Oelmann,S., Fernald,A.A., Marziliano,N., van
            Steensel,B., Kipling,D., Le Beau,M.M. and de Lange,T.
  TITLE     Comparison of the human and mouse genes encoding the telomeric
            protein, TRF1: chromosomal localization, expression and conserved
            protein domains
  JOURNAL   Hum Mol Genet 6 (1), 69-76 (1997)
   PUBMED   9002672
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Lu,K.P., Hanes,S.D. and Hunter,T.
  TITLE     A human peptidyl-prolyl isomerase essential for regulation of
            mitosis
  JOURNAL   Nature 380 (6574), 544-547 (1996)
   PUBMED   8606777
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Bilaud,T., Koering,C.E., Binet-Brasselet,E., Ancelin,K.,
            Pollice,A., Gasser,S.M. and Gilson,E.
  TITLE     The telobox, a Myb-related telomeric DNA binding motif found in
            proteins from yeast, plants and human
  JOURNAL   Nucleic Acids Res 24 (7), 1294-1303 (1996)
   PUBMED   8614633
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Chong,L., van Steensel,B., Broccoli,D., Erdjument-Bromage,H.,
            Hanish,J., Tempst,P. and de Lange,T.
  TITLE     A human telomeric protein
  JOURNAL   Science 270 (5242), 1663-1667 (1995)
   PUBMED   7502076
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Zhong,Z., Shiue,L., Kaplan,S. and de Lange,T.
  TITLE     A mammalian factor that binds telomeric TTAGGG repeats in vitro
  JOURNAL   Mol Cell Biol 12 (11), 4834-4843 (1992)
   PUBMED   1406665
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022893.6.
            
            Summary: This gene encodes a telomere specific protein which is a
            component of the telomere nucleoprotein complex. This protein is
            present at telomeres throughout the cell cycle and functions as an
            inhibitor of telomerase, acting in cis to limit the elongation of
            individual chromosome ends. The protein structure contains a
            C-terminal Myb motif, a dimerization domain near its N-terminus and
            an acidic N-terminus. Multiple transcripts of this gene are
            alternatively spliced products. [provided by RefSeq, Aug 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14243140.653577.1,
                                           SRR12514507.570958.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.11"
     Protein         1..347
                     /product="telomeric repeat-binding factor 1 isoform 14"
                     /note="NIMA-interacting protein 2; telomeric protein
                     Pin2/TRF1; TTAGGG repeat-binding factor 1; telomeric
                     repeat binding factor (NIMA-interacting) 1"
                     /calculated_mol_wt=39488
     Region          76..264
                     /region_name="TRFH"
                     /note="Telomeric Repeat binding Factor or TTAGGG Repeat
                     binding Factor, central (dimerization) domain Homology;
                     TRFH. Telomeres are protein/DNA complexes that make up the
                     physical ends of eukaryotic linear chromosomes and are
                     essential for chromosome stability; cd00280"
                     /db_xref="CDD:238174"
     Site            order(106,109,123,127,131,141..145,153,156..157,160)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238174"
     CDS             1..347
                     /gene="TERF1"
                     /gene_synonym="hTRF1-AS; PIN2; t-TRF1; TRBF1; TRF; TRF1"
                     /coded_by="NM_001413374.1:24..1067"
                     /note="isoform 14 is encoded by transcript variant 14"
                     /db_xref="GeneID:7013"
                     /db_xref="HGNC:HGNC:11728"
                     /db_xref="MIM:600951"
ORIGIN      
        1 maedvssaap sprgcadgrd adpteeqmae terndeeqfe cqellecqvq vgapeeeeee
       61 eedaglvaea eavaagwmld flclslcraf rdgrsedfrr trnsaeaiih glssltacql
      121 rtiyicqflt riaagktlda qfenderitp lesalmiwgs iekehdklhe eiqnlikiqa
      181 iavcmengnf keaeevferi fgdpnshmpf kskllmiisq kdtfhsffqh fsynhmmeki
      241 ksyvnyvlse ksstflmkaa akvveskrtr titsqdkpsg ndvemetean ldtrkrshkn
      301 lflsklqhgt qqqdlnkker rvgtpqsekk kaeeplkaey lfqrvsr
//
LOCUS       NP_001411263             194 aa            linear   PRI 21-NOV-2025
DEFINITION  protein cholesin isoform a [Homo sapiens].
ACCESSION   NP_001411263
VERSION     NP_001411263.1
DBSOURCE    REFSEQ: accession NM_001424334.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Ryk,A., Marcinkiewicz,A., Chrzanowski,J., Michalak,A.M., Drozdz,I.,
            Burzynski,J., Krejca,M. and Fendler,W.
  TITLE     Cholesin receptor signalling is active in cardiovascular
            system-associated adipose tissue and correlates with SGLT2i
            treatment in patients with diabetes
  JOURNAL   Cardiovasc Diabetol 23 (1), 211 (2024)
   PUBMED   38902687
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Hu,X., Chen,F., Jia,L., Long,A., Peng,Y., Li,X., Huang,J., Wei,X.,
            Fang,X., Gao,Z., Zhang,M., Liu,X., Chen,Y.G., Wang,Y., Zhang,H. and
            Wang,Y.
  TITLE     A gut-derived hormone regulates cholesterol metabolism
  JOURNAL   Cell 187 (7), 1685-1700 (2024)
   PUBMED   38503280
  REMARK    GeneRIF: A gut-derived hormone regulates cholesterol metabolism.
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 194)
  AUTHORS   Willer,C.J., Schmidt,E.M., Sengupta,S., Peloso,G.M., Gustafsson,S.,
            Kanoni,S., Ganna,A., Chen,J., Buchkovich,M.L., Mora,S.,
            Beckmann,J.S., Bragg-Gresham,J.L., Chang,H.Y., Demirkan,A., Den
            Hertog,H.M., Do,R., Donnelly,L.A., Ehret,G.B., Esko,T.,
            Feitosa,M.F., Ferreira,T., Fischer,K., Fontanillas,P., Fraser,R.M.,
            Freitag,D.F., Gurdasani,D., Heikkila,K., Hypponen,E., Isaacs,A.,
            Jackson,A.U., Johansson,A., Johnson,T., Kaakinen,M., Kettunen,J.,
            Kleber,M.E., Li,X., Luan,J., Lyytikainen,L.P., Magnusson,P.K.E.,
            Mangino,M., Mihailov,E., Montasser,M.E., Muller-Nurasyid,M.,
            Nolte,I.M., O'Connell,J.R., Palmer,C.D., Perola,M., Petersen,A.K.,
            Sanna,S., Saxena,R., Service,S.K., Shah,S., Shungin,D., Sidore,C.,
            Song,C., Strawbridge,R.J., Surakka,I., Tanaka,T., Teslovich,T.M.,
            Thorleifsson,G., Van den Herik,E.G., Voight,B.F., Volcik,K.A.,
            Waite,L.L., Wong,A., Wu,Y., Zhang,W., Absher,D., Asiki,G.,
            Barroso,I., Been,L.F., Bolton,J.L., Bonnycastle,L.L., Brambilla,P.,
            Burnett,M.S., Cesana,G., Dimitriou,M., Doney,A.S.F., Doring,A.,
            Elliott,P., Epstein,S.E., Ingi Eyjolfsson,G., Gigante,B.,
            Goodarzi,M.O., Grallert,H., Gravito,M.L., Groves,C.J., Hallmans,G.,
            Hartikainen,A.L., Hayward,C., Hernandez,D., Hicks,A.A., Holm,H.,
            Hung,Y.J., Illig,T., Jones,M.R., Kaleebu,P., Kastelein,J.J.P.,
            Khaw,K.T., Kim,E., Klopp,N., Komulainen,P., Kumari,M.,
            Langenberg,C., Lehtimaki,T., Lin,S.Y., Lindstrom,J., Loos,R.J.F.,
            Mach,F., McArdle,W.L., Meisinger,C., Mitchell,B.D., Muller,G.,
            Nagaraja,R., Narisu,N., Nieminen,T.V.M., Nsubuga,R.N., Olafsson,I.,
            Ong,K.K., Palotie,A., Papamarkou,T., Pomilla,C., Pouta,A.,
            Rader,D.J., Reilly,M.P., Ridker,P.M., Rivadeneira,F., Rudan,I.,
            Ruokonen,A., Samani,N., Scharnagl,H., Seeley,J., Silander,K.,
            Stancakova,A., Stirrups,K., Swift,A.J., Tiret,L.,
            Uitterlinden,A.G., van Pelt,L.J., Vedantam,S., Wainwright,N.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilsgaard,T., Wilson,J.F.,
            Young,E.H., Zhao,J.H., Adair,L.S., Arveiler,D., Assimes,T.L.,
            Bandinelli,S., Bennett,F., Bochud,M., Boehm,B.O., Boomsma,D.I.,
            Borecki,I.B., Bornstein,S.R., Bovet,P., Burnier,M., Campbell,H.,
            Chakravarti,A., Chambers,J.C., Chen,Y.I., Collins,F.S.,
            Cooper,R.S., Danesh,J., Dedoussis,G., de Faire,U., Feranil,A.B.,
            Ferrieres,J., Ferrucci,L., Freimer,N.B., Gieger,C., Groop,L.C.,
            Gudnason,V., Gyllensten,U., Hamsten,A., Harris,T.B., Hingorani,A.,
            Hirschhorn,J.N., Hofman,A., Hovingh,G.K., Hsiung,C.A.,
            Humphries,S.E., Hunt,S.C., Hveem,K., Iribarren,C., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kaprio,J., Kesaniemi,A., Kivimaki,M.,
            Kooner,J.S., Koudstaal,P.J., Krauss,R.M., Kuh,D., Kuusisto,J.,
            Kyvik,K.O., Laakso,M., Lakka,T.A., Lind,L., Lindgren,C.M.,
            Martin,N.G., Marz,W., McCarthy,M.I., McKenzie,C.A., Meneton,P.,
            Metspalu,A., Moilanen,L., Morris,A.D., Munroe,P.B., Njolstad,I.,
            Pedersen,N.L., Power,C., Pramstaller,P.P., Price,J.F., Psaty,B.M.,
            Quertermous,T., Rauramaa,R., Saleheen,D., Salomaa,V.,
            Sanghera,D.K., Saramies,J., Schwarz,P.E.H., Sheu,W.H.,
            Shuldiner,A.R., Siegbahn,A., Spector,T.D., Stefansson,K.,
            Strachan,D.P., Tayo,B.O., Tremoli,E., Tuomilehto,J., Uusitupa,M.,
            van Duijn,C.M., Vollenweider,P., Wallentin,L., Wareham,N.J.,
            Whitfield,J.B., Wolffenbuttel,B.H.R., Ordovas,J.M., Boerwinkle,E.,
            Palmer,C.N.A., Thorsteinsdottir,U., Chasman,D.I., Rotter,J.I.,
            Franks,P.W., Ripatti,S., Cupples,L.A., Sandhu,M.S., Rich,S.S.,
            Boehnke,M., Deloukas,P., Kathiresan,S., Mohlke,K.L., Ingelsson,E.
            and Abecasis,G.R.
  CONSRTM   Global Lipids Genetics Consortium
  TITLE     Discovery and refinement of loci associated with lipid levels
  JOURNAL   Nat Genet 45 (11), 1274-1283 (2013)
   PUBMED   24097068
REFERENCE   7  (residues 1 to 194)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 194)
  AUTHORS   Yashin,A.I., Wu,D., Arbeev,K.G. and Ukraintseva,S.V.
  TITLE     Joint influence of small-effect genetic variants on human longevity
  JOURNAL   Aging (Albany NY) 2 (9), 612-620 (2010)
   PUBMED   20834067
REFERENCE   9  (residues 1 to 194)
  AUTHORS   Satoh,J., Obayashi,S., Misawa,T., Sumiyoshi,K., Oosumi,K. and
            Tabunoki,H.
  TITLE     Protein microarray analysis identifies human cellular prion protein
            interactors
  JOURNAL   Neuropathol Appl Neurobiol 35 (1), 16-35 (2009)
   PUBMED   18482256
REFERENCE   10 (residues 1 to 194)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CP068271.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: ERR4368409.417512.1, ERR4352444.545047.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMN03465413 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..194
                     /product="protein cholesin isoform a"
                     /note="uncharacterized protein C7orf50; protein cholesin"
                     /calculated_mol_wt=21952
     Region          1..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Region          104..165
                     /region_name="WKF"
                     /note="WKF domain; pfam10180"
                     /db_xref="CDD:462982"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     CDS             1..194
                     /gene="CHLSN"
                     /gene_synonym="C7orf50; YCR016W"
                     /coded_by="NM_001424334.1:132..716"
                     /note="isoform a is encoded by transcript variant 27"
                     /db_xref="GeneID:84310"
                     /db_xref="HGNC:HGNC:22421"
                     /db_xref="MIM:621174"
ORIGIN      
        1 makqkrkvpe vtekknkklk kasaegpllg peaapsgega gskgeavlrp gldaepelsp
       61 eeqrvlerkl kkerkkeerq rlreaglvaq hpparrsgae laldylcrwa qkhknwrfqk
      121 trqtwlllhm ydsdkvpdeh fstllayleg lqgrareltv qkaealmrel deegsdpplp
      181 graqrirqvl qlls
//
LOCUS       NP_001400129             441 aa            linear   PRI 21-NOV-2025
DEFINITION  cyclin-T1 isoform e [Homo sapiens].
ACCESSION   NP_001400129
VERSION     NP_001400129.1
DBSOURCE    REFSEQ: accession NM_001413200.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Chen,W., Chu,J., Miao,Y., Jiang,W., Wang,F., Zhang,N., Jin,J. and
            Cai,Y.
  TITLE     MOF-mediated acetylation of CDK9 promotes global transcription by
            modulating P-TEFb complex formation
  JOURNAL   FEBS J 291 (21), 4796-4812 (2024)
   PUBMED   39250546
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Gao,G., Wu,X., Zhou,J., He,M., He,J.J. and Guo,D.
  TITLE     Inhibition of HIV-1 transcription and replication by a newly
            identified cyclin T1 splice variant
  JOURNAL   J Biol Chem 288 (20), 14297-14309 (2013)
   PUBMED   23569210
  REMARK    GeneRIF: CYCT1b is a newly identified cyclin T1 splice variant
            whose expression leads to direct inhibition of TAT-transactivated
            transcription of the HIV-1 LTR promoter
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Urano,E., Miyauchi,K., Ichikawa,R., Futahashi,Y. and Komano,J.
  TITLE     Regulation of cyclin T1 expression and function by an alternative
            splice variant that skips exon 7 and contains a premature
            termination codon
  JOURNAL   Gene 505 (1), 1-8 (2012)
   PUBMED   22692005
REFERENCE   5  (residues 1 to 441)
  AUTHORS   De Luca,A., De Falco,M., Baldi,A. and Paggi,M.G.
  TITLE     Cyclin T: three forms for different roles in physiological and
            pathological functions
  JOURNAL   J Cell Physiol 194 (2), 101-107 (2003)
   PUBMED   12494448
  REMARK    Review article
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Martin-Serrano,J., Li,K. and Bieniasz,P.D.
  TITLE     Cyclin T1 expression is mediated by a complex and constitutively
            active promoter and does not limit human immunodeficiency virus
            type 1 Tat function in unstimulated primary lymphocytes
  JOURNAL   J Virol 76 (1), 208-219 (2002)
   PUBMED   11739686
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Liu,H. and Rice,A.P.
  TITLE     Isolation and characterization of the human cyclin T1 promoter
  JOURNAL   Gene 252 (1-2), 39-49 (2000)
   PUBMED   10903436
REFERENCE   8  (residues 1 to 441)
  AUTHORS   Wei,P., Garber,M.E., Fang,S.M., Fischer,W.H. and Jones,K.A.
  TITLE     A novel CDK9-associated C-type cyclin interacts directly with HIV-1
            Tat and mediates its high-affinity, loop-specific binding to TAR
            RNA
  JOURNAL   Cell 92 (4), 451-462 (1998)
   PUBMED   9491887
REFERENCE   9  (residues 1 to 441)
  AUTHORS   Yang,X., Herrmann,C.H. and Rice,A.P.
  TITLE     The human immunodeficiency virus Tat proteins specifically
            associate with TAK in vivo and require the carboxyl-terminal domain
            of RNA polymerase II for function
  JOURNAL   J Virol 70 (7), 4576-4584 (1996)
   PUBMED   8676484
REFERENCE   10 (residues 1 to 441)
  AUTHORS   Herrmann,C.H. and Rice,A.P.
  TITLE     Lentivirus Tat proteins specifically associate with a cellular
            protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal
            domain of the large subunit of RNA polymerase II: candidate for a
            Tat cofactor
  JOURNAL   J Virol 69 (3), 1612-1620 (1995)
   PUBMED   7853496
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079951.35.
            
            Summary: This gene encodes a member of the highly conserved cyclin
            C subfamily. The encoded protein tightly associates with
            cyclin-dependent kinase 9, and is a major subunit of positive
            transcription elongation factor b (p-TEFb). In humans, there are
            multiple forms of positive transcription elongation factor b, which
            may include one of several different cyclins along with
            cyclin-dependent kinase 9. The complex containing the encoded
            cyclin and cyclin-dependent kinase 9 acts as a cofactor of human
            immunodeficiency virus type 1 (HIV-1) Tat protein, and is both
            necessary and sufficient for full activation of viral
            transcription. This cyclin and its kinase partner are also involved
            in triggering transcript elongation through phosphorylation of the
            carboxy-terminal domain of the largest RNA polymerase II subunit.
            Overexpression of this gene is implicated in tumor growth.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Apr 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.852424.1,
                                           SRR14038193.1214069.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267750, SAMN03267761
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.11-q13.12"
     Protein         1..441
                     /product="cyclin-T1 isoform e"
                     /note="human immunodeficiency virus type 1 (HIV-1)
                     expression (elevated) 1; cyclin C-related protein;
                     CDK9-associated C-type protein; MLLT10/CCNT1 fusion"
                     /calculated_mol_wt=47629
     CDS             1..441
                     /gene="CCNT1"
                     /gene_synonym="CCNT; CYCT1; HIVE1"
                     /coded_by="NM_001413200.1:390..1715"
                     /note="isoform e is encoded by transcript variant e"
                     /db_xref="GeneID:904"
                     /db_xref="HGNC:HGNC:1599"
                     /db_xref="MIM:143055"
ORIGIN      
        1 misqsssdtt iaglmsmsts ttsavpslpv seesssnlts vemlpgkrwl ssqpsfklep
       61 tqghrtsenl altgvdhslp qdgsnafisq kqnsksvpsa kvslkeyrak haeelaaqkr
      121 qlenmeanvk sqyayaaqnl lshhdshssv ilkmpiegse nperpfleka dktalkmrip
      181 vaggdkaass kpeeikmrik vhaaadkhns vedsvtksre hkekhkthps nhhhhhnhhs
      241 hkhshsqlpv gtgnkrpgdp khssqtsnla hktyslsssf ssssstrkrg pseetggavf
      301 dhpakiakst kssslnfsfp slptmgqmpg hssdtsglsf sqpscktrvp hskldkgptg
      361 anghnttqti dyqdtvnmlh sllsaqgvqp tqptafefvr pysdylnprs ggissrsgnt
      421 dkprppplps epppplpplp k
//
LOCUS       NP_001400609             344 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 13 precursor [Homo sapiens].
ACCESSION   NP_001400609
VERSION     NP_001400609.1
DBSOURCE    REFSEQ: accession NM_001413680.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 344)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 344)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 344)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1613028.1,
                                           SRR18074969.1347695.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..344
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 13 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=34835
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..312
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            277..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     CDS             1..344
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413680.1:169..1203"
                     /note="isoform 13 precursor is encoded by transcript
                     variant 16"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvsyih gssqaqfvae shiilvlnaa itmgmvllne
      301 aatskgdvgk rrrslpfpli yqdlqlpqvl rhyvfkqvns vafl
//
LOCUS       NP_001424532             427 aa            linear   PRI 21-NOV-2025
DEFINITION  sorting nexin-27 isoform 5 [Homo sapiens].
ACCESSION   NP_001424532 XP_047287245 XP_054194890
VERSION     NP_001424532.1
DBSOURCE    REFSEQ: accession NM_001437603.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Broniarczyk,J., Trejo-Cerro,O., Massimi,P., Kavcic,N., Myers,M.P.
            and Banks,L.
  TITLE     HPV-18 E6 enhances the interaction between EMILIN2 and SNX27 to
            promote WNT signaling
  JOURNAL   J Virol 98 (7), e0073524 (2024)
   PUBMED   38874360
  REMARK    GeneRIF: HPV-18 E6 enhances the interaction between EMILIN2 and
            SNX27 to promote WNT signaling.
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Xi,Y., Gai,Y., Zhang,W., Wang,M., Liu,Q. and Bi,Y.
  TITLE     Circular RNA SNX27 Facilitates Gastric Cancer Progression By
            Sponging miR-638
  JOURNAL   Turk J Gastroenterol 35 (4), 280-287 (2024)
   PUBMED   39128090
  REMARK    GeneRIF: Circular RNA SNX27 Facilitates Gastric Cancer Progression
            By Sponging miR-638.
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Broniarczyk,J.K., Massimi,P., Trejo-Cerro,O., Myers,M.P. and
            Banks,L.
  TITLE     HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in a
            PBM-Dependent Manner and Promotes Increased Cell Proliferation
  JOURNAL   J Virol 96 (22), e0136522 (2022)
   PUBMED   36326272
  REMARK    GeneRIF: HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in
            a PBM-Dependent Manner and Promotes Increased Cell Proliferation.
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 427)
  AUTHORS   MacNeil,A.J., Mansour,M. and Pohajdak,B.
  TITLE     Sorting nexin 27 interacts with the Cytohesin associated
            scaffolding protein (CASP) in lymphocytes
  JOURNAL   Biochem Biophys Res Commun 359 (4), 848-853 (2007)
   PUBMED   17577583
  REMARK    GeneRIF: These results suggest that endosomal SNX27 may recruit
            CASP to orchestrate intracellular trafficking and/or signaling
            complexes.
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Rincon,E., Santos,T., Avila-Flores,A., Albar,J.P., Lalioti,V.,
            Lei,C., Hong,W. and Merida,I.
  TITLE     Proteomics identification of sorting nexin 27 as a diacylglycerol
            kinase zeta-associated protein: new diacylglycerol kinase roles in
            endocytic recycling
  JOURNAL   Mol Cell Proteomics 6 (6), 1073-1087 (2007)
   PUBMED   17351151
  REMARK    GeneRIF: These data support a previously unreported role for
            diacylglycerol kinase zeta in the modulation of membrane
            trafficking, which may also help to define SNX27 function.
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Joubert,L., Hanson,B., Barthet,G., Sebben,M., Claeysen,S., Hong,W.,
            Marin,P., Dumuis,A. and Bockaert,J.
  TITLE     New sorting nexin (SNX27) and NHERF specifically interact with the
            5-HT4a receptor splice variant: roles in receptor targeting
  JOURNAL   J Cell Sci 117 (Pt 22), 5367-5379 (2004)
   PUBMED   15466885
  REMARK    GeneRIF: SNX27a redirects part of the 5-HT4(a)R to early endosomes.
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Worby,C.A. and Dixon,J.E.
  TITLE     Sorting out the cellular functions of sorting nexins
  JOURNAL   Nat Rev Mol Cell Biol 3 (12), 919-931 (2002)
   PUBMED   12461558
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol. 2003 Feb;4(2):156.]
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Teasdale,R.D., Loci,D., Houghton,F., Karlsson,L. and Gleeson,P.A.
  TITLE     A large family of endosome-localized proteins related to sorting
            nexin 1
  JOURNAL   Biochem J 358 (Pt 1), 7-16 (2001)
   PUBMED   11485546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL391335.32 and AL589765.19.
            
            On or before Apr 7, 2025 this sequence version replaced
            XP_047287245.1, XP_054194890.1.
            
            Summary: This gene encodes a member of the sorting nexin family, a
            diverse group of cytoplasmic and membrane-associated proteins
            involved in endocytosis of plasma membrane receptors and protein
            trafficking through these compartments. All members of this protein
            family contain a phosphoinositide binding domain (PX domain). A
            highly similar protein in mouse is responsible for the specific
            recruitment of an isoform of serotonin 5-hydroxytryptamine 4
            receptor into early endosomes, suggesting the analogous role for
            the human protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.374123.1,
                                           SRR14038196.2295994.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..427
                     /product="sorting nexin-27 isoform 5"
                     /note="methamphetamine-responsive transcript 1; sorting
                     nexin family member 27"
                     /calculated_mol_wt=48695
     Region          42..>88
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     Region          70..164
                     /region_name="PX_domain"
                     /note="The Phox Homology domain, a phosphoinositide
                     binding module; cl02563"
                     /db_xref="CDD:470617"
     Site            order(95..97,121..122,134)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132768"
     Region          172..264
                     /region_name="FERM_F1_SNX27"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F1 sub-domain, found in sorting nexin protein 27
                     (SNX27); cd01777"
                     /db_xref="CDD:340475"
     Region          324..425
                     /region_name="FERM-like_C_SNX27"
                     /note="Atypical FERM-like domain C-lobe of Sorting nexin
                     27; cd13338"
                     /db_xref="CDD:270146"
     CDS             1..427
                     /gene="SNX27"
                     /gene_synonym="MRT1; MY014"
                     /coded_by="NM_001437603.1:153..1436"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:81609"
                     /db_xref="HGNC:HGNC:20073"
                     /db_xref="MIM:611541"
ORIGIN      
        1 madedgegih psaphrnggg gggggsglhc agnggggggg prvvrivkse sgygfnvrgq
       61 vseggqlrsi ngelyaplqh vynvymagrq lcskryrefa ilhqnlkref anftfprlpg
      121 kwpfslseqq ldarrrglee ylekvcsirv igesdimqef lsesdenyng vsdvelrval
      181 pdgttvtvrv kknsttdqvy qaiaakvgmd sttvnyfalf evishsfvrk lapnefphkl
      241 yiqnytsavp gtcltirkwl ftteeeilln dndlavtyff hqavddvkkg yikaeeksyq
      301 lqklyeqrkm vmylnmlrtc egyneiifph cacdsrrkgh vitaisithf klhacteegq
      361 lenqviafew demqrwdtde egmafcfeya rgekkprwvk iftpyfnymh ecfervfcel
      421 kwrkeey
//
LOCUS       NP_001392801            1061 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001392801
VERSION     NP_001392801.1
DBSOURCE    REFSEQ: accession NM_001405872.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1061)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1061)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1061)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1061)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1061)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1061)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1061)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2000457.1,
                                           SRR18074967.2454038.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1061
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 5"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=116251
     Region          885..>947
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..1061
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405872.1:251..3436"
                     /note="isoform 5 is encoded by transcript variant 13"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankgli
      481 vlgevpppeh ttdlflplss evktdhgtdk liesvsqple nhgapiighi seslstkscg
      541 alrpvngvin tlqpvladhi pgdssdaeeq lhkkqrlnlv ssssdgtcva artrpvlsck
      601 krrlvrpnsi vplskkvhrn stirpgcdvn pscalcgsgs intmppeihy eapllerlsq
      661 ldscvhpvla fpddvptslh fqsmlksqwq nkpfdkikpp kklslkhrap mpgslpdsar
      721 kdrhklvssf lttaklshhq trpdrthrqh lddvgavpmv ervtapkaer llnppppvhd
      781 pnhskmrlrd hssersevlk hhtdmssssy laathhpphs plvrqlstss dspapassss
      841 qvtastsqqp vrrrrgessf dinnivipms vaattrvekl qykeiltpsw revdlqslkg
      901 spdeeneeie dlsdaafaal hakceemera rwlwttsvpp qrrgsrspis pelhsapltp
      961 vardtprhla sedtrcstpe lgldeqsvqp werrtfplah spqaecedql daqeraarct
     1021 rrtsgsktgr eteaaptspp ivplksrhlv aaataqrpth r
//
LOCUS       NP_001400598             291 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 4 [Homo sapiens].
ACCESSION   NP_001400598
VERSION     NP_001400598.1
DBSOURCE    REFSEQ: accession NM_001413669.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 291)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1660807.112944.1, SRR14038193.3879752.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..291
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 4"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=33182
     Region          4..286
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     CDS             1..291
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413669.1:149..1024"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mewssrrsif rmngdkfrkf ikapprnysm ivmftalqpq rqcsvcrqan eeyqilansw
       61 ryssafcnkl ffsmvdydeg tdvfqqlnmn saptfmhfpp kgrpkradtf dlqrigfaae
      121 qlakwiadrt dvhirvfrpp nysgtialal lvslvgglly lrrnnlefiy nktgwamvsl
      181 civfamtsgq mwnhirgppy ahknphngqv syihgssqaq fvaeshiilv lnaaitmgmv
      241 llneaatskg dvgkrriicl vglglvvfff sfllsifrsk yhgypysfli k
//
LOCUS       NP_001400245             291 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 2 [Homo sapiens].
ACCESSION   NP_001400245
VERSION     NP_001400245.1
DBSOURCE    REFSEQ: accession NM_001413316.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.332764.1,
                                           SRR1660809.59040.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968832 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..291
                     /product="RNA-binding Raly-like protein isoform 2"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=32199
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          171..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     Region          199..>244
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     Region          249..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     CDS             1..291
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413316.1:112..987"
                     /note="isoform 2 is encoded by transcript variant 43"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly rleskepfls
      121 vggyvfdydy yrddfynrlf dyhgrvpppp raviplkrpr vavtttrrgk gvfsmkggsr
      181 stasgstgsk lksdelqtik keltqiktki dsllgrleki ekqqkaeaea qkkqleeslv
      241 liqeecvsei adhsteepae ggpdadgeem tdgieedfde dgghelflqi k
//
LOCUS       NP_001427532             323 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform r [Homo sapiens].
ACCESSION   NP_001427532 XP_016874002 XP_054226336
VERSION     NP_001427532.1
DBSOURCE    REFSEQ: accession NM_001440603.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 323)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 323)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 323)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2.
            
            On or before May 22, 2025 this sequence version replaced
            XP_016874002.1, XP_054226336.1.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.13534.1,
                                           SRR14038193.3944217.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..323
                     /product="polycomb protein EED isoform r"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=36225
     Region          <90..222
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          96..140
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          148..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <162..>312
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          193..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          285..311
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..323
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001440603.1:478..1449"
                     /note="isoform r is encoded by transcript variant 18"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdendd avsiesgtnt erpdtptntp
       61 napgrkswgk gkwkskkcky sfkcvnslke dhnqplfgvq fnwhskegdp lvfatvgsnr
      121 vtlyechsqg eirllqsyvd adadenfytc awtydsntsh pllavagsrg iiriinpitm
      181 qcikhyvghg nainelkfhp rdpnlllsvs kdhalrlwni qtdtlvaifg gveghrdevl
      241 sascenaivc wkpgkmeddi dkikpsesnv tilgrfdysq cdiwymrfsm dfwqkmlalg
      301 nqvgklyvwd levedphkan rdh
//
LOCUS       NP_001396235            2442 aa            linear   PRI 21-NOV-2025
DEFINITION  histone-lysine N-methyltransferase, H3 lysine-36 specific isoform e
            [Homo sapiens].
ACCESSION   NP_001396235
VERSION     NP_001396235.1
DBSOURCE    REFSEQ: accession NM_001409306.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2442)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2442)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   3  (residues 1 to 2442)
  AUTHORS   Conteduca,G., Cangelosi,D., Baldo,C., Arado,A., Testa,B.,
            Wagner,R.T., Robertson,K.D., Dequiedt,F., Fitzsimmons,L.,
            Malacarne,M., Filaci,G. and Coviello,D.A.
  TITLE     Impact of NSD1 Alternative Transcripts in Actin Filament Formation
            and Cellular Division Pathways in Fibroblasts
  JOURNAL   Genes (Basel) 15 (9), 1117 (2024)
   PUBMED   39336709
  REMARK    GeneRIF: Impact of NSD1 Alternative Transcripts in Actin Filament
            Formation and Cellular Division Pathways in Fibroblasts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2442)
  AUTHORS   Ren,Z., Yue,L., Hu,H.Y., Hou,X.L., Chen,W.Q., Tan,Y., Dong,Z. and
            Zhang,J.
  TITLE     Identification of Novel NSD1 variations in four Pediatric cases
            with sotos Syndrome
  JOURNAL   BMC Med Genomics 17 (1), 116 (2024)
   PUBMED   38684994
  REMARK    GeneRIF: Identification of Novel NSD1 variations in four Pediatric
            cases with sotos Syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2442)
  AUTHORS   Wang,X., Yeh,S., Wu,G., Hsu,C.L., Wang,L., Chiang,T., Yang,Y.,
            Guo,Y. and Chang,C.
  TITLE     Identification and characterization of a novel androgen receptor
            coregulator ARA267-alpha in prostate cancer cells
  JOURNAL   J Biol Chem 276 (44), 40417-40423 (2001)
   PUBMED   11509567
REFERENCE   6  (residues 1 to 2442)
  AUTHORS   Jaju,R.J., Fidler,C., Haas,O.A., Strickson,A.J., Watkins,F.,
            Clark,K., Cross,N.C., Cheng,J.F., Aplan,P.D., Kearney,L.,
            Boultwood,J. and Wainscoat,J.S.
  TITLE     A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in
            de novo childhood acute myeloid leukemia
  JOURNAL   Blood 98 (4), 1264-1267 (2001)
   PUBMED   11493482
REFERENCE   7  (residues 1 to 2442)
  AUTHORS   Lee,D.K., Duan,H.O. and Chang,C.
  TITLE     Androgen receptor interacts with the positive elongation factor
            P-TEFb and enhances the efficiency of transcriptional elongation
  JOURNAL   J Biol Chem 276 (13), 9978-9984 (2001)
   PUBMED   11266437
REFERENCE   8  (residues 1 to 2442)
  AUTHORS   Huang,N., vom Baur,E., Garnier,J.M., Lerouge,T., Vonesch,J.L.,
            Lutz,Y., Chambon,P. and Losson,R.
  TITLE     Two distinct nuclear receptor interaction domains in NSD1, a novel
            SET protein that exhibits characteristics of both corepressors and
            coactivators
  JOURNAL   EMBO J 17 (12), 3398-3412 (1998)
   PUBMED   9628876
REFERENCE   9  (residues 1 to 2442)
  AUTHORS   Ocansey,S., Cole,T.R.P., Rahman,N. and Tatton-Brown,K.
  TITLE     Sotos Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301652
REFERENCE   10 (residues 1 to 2442)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027314.5, AC008570.6 and
            AC146507.2.
            
            Summary: This gene encodes a protein containing a SET domain, 2
            LXXLL motifs, 3 nuclear translocation signals (NLSs), 4 plant
            homeodomain (PHD) finger regions, and a proline-rich region. The
            encoded protein enhances androgen receptor (AR) transactivation,
            and this enhancement can be increased further in the presence of
            other androgen receptor associated coregulators. This protein may
            act as a nucleus-localized, basic transcriptional factor and also
            as a bifunctional transcriptional regulator. Mutations of this gene
            have been associated with Sotos syndrome and Weaver syndrome. One
            version of childhood acute myeloid leukemia is the result of a
            cryptic translocation with the breakpoints occurring within nuclear
            receptor-binding Su-var, enhancer of zeste, and trithorax domain
            protein 1 on chromosome 5 and nucleoporin, 98-kd on chromosome 11.
            Multiple transcript variants encoding distinct isoforms have been
            identified for this gene. [provided by RefSeq, Sep 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1379835.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2442
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..2442
                     /product="histone-lysine N-methyltransferase, H3 lysine-36
                     specific isoform e"
                     /EC_number="2.1.1.357"
                     /note="androgen receptor-associated coregulator 267;
                     histone-lysine N-methyltransferase, H3 lysine-36 and H4
                     lysine-20 specific; H3-K36-HMTase; H4-K20-HMTase; lysine
                     N-methyltransferase 3B; NR-binding SET domain-containing
                     protein; androgen receptor coactivator 267 kDa protein;
                     androgen receptor-associated protein of 267 kDa; nuclear
                     receptor-binding SET domain-containing protein 1; nuclear
                     receptor SET domain-containing protein 1; histone-lysine
                     N-methyltransferase, H3 lysine-36 specific"
                     /calculated_mol_wt=268791
     Region          27..142
                     /region_name="PWWP_NSD1_rpt1"
                     /note="first PWWP domain found in nuclear receptor-binding
                     SET domain-containing protein 1 (NSD1) and similar
                     proteins; cd20161"
                     /db_xref="CDD:438989"
     Site            order(43,46,77)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438989"
     Site            44..47
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438989"
     Site            order(115..117,120..121)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438989"
     Region          <1140..1296
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          1254..1296
                     /region_name="PHD1_NSD1_2"
                     /note="PHD finger 1 found in nuclear receptor-binding SET
                     domain-containing protein NSD1 and NSD2; cd15648"
                     /db_xref="CDD:277118"
     Site            order(1254,1263..1267,1272,1290)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277118"
     Region          1338..1384
                     /region_name="PHD2_NSD1"
                     /note="PHD finger 2 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15650"
                     /db_xref="CDD:277120"
     Site            order(1338,1348..1352,1358,1379)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277120"
     Region          1385..1438
                     /region_name="PHD3_NSD1"
                     /note="PHD finger 3 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15653"
                     /db_xref="CDD:277123"
     Site            order(1385,1403..1407,1411,1433)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277123"
     Region          1455..1494
                     /region_name="PHD4_NSD1"
                     /note="PHD finger 4 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15656"
                     /db_xref="CDD:277126"
     Site            order(1455,1464..1468,1472,1489)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277126"
     Region          1501..1596
                     /region_name="PWWP_NSD1_rpt2"
                     /note="second PWWP domain found in nuclear
                     receptor-binding SET domain-containing protein 1 (NSD1)
                     and similar proteins; cd20164"
                     /db_xref="CDD:438992"
     Site            order(1513,1516,1544)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438992"
     Site            1514..1517
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438992"
     Region          1647..1685
                     /region_name="AWS"
                     /note="AWS domain; pfam17907"
                     /db_xref="CDD:465559"
     Region          1687..1828
                     /region_name="SET_NSD1"
                     /note="SET domain (including post-SET domain) found in
                     nuclear receptor-binding SET domain-containing protein 1
                     (NSD1) and similar proteins; cd19210"
                     /db_xref="CDD:380987"
     Site            order(1698..1700,1717,1727,1731,1740..1746,1763..1767,
                     1774..1776,1791,1802..1812,1814..1818,1827)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380987"
     Site            order(1698..1700,1740..1743,1763..1767,1804,1811,
                     1815..1818,1827)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380987"
     Site            order(1717,1727,1731,1742..1746,1774..1776,1791,
                     1802..1806)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:380987"
     Site            order(1769,1816,1818,1823)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380987"
     Region          1866..1908
                     /region_name="PHD5_NSD1"
                     /note="PHD finger 5 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15659"
                     /db_xref="CDD:277129"
     Site            order(1866,1875..1879,1885,1903)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277129"
     Region          1907..1956
                     /region_name="C5HCH"
                     /note="NSD Cys-His rich domain; pfam17982"
                     /db_xref="CDD:465605"
     Region          <1954..2320
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..2442
                     /gene="NSD1"
                     /gene_synonym="ARA267; KMT3B; SOTOS; SOTOS1; STO"
                     /coded_by="NM_001409306.1:288..7616"
                     /note="isoform e is encoded by transcript variant 9"
                     /db_xref="GeneID:64324"
                     /db_xref="HGNC:HGNC:14234"
                     /db_xref="MIM:606681"
ORIGIN      
        1 mlelpgtsss stsqelpfcq pkkkstplky evgdliwakf krrpwwpcri csdplinths
       61 kmkvsnrrpy rqyyveafgd pserawvagk aivmfegrhq feelpvlrrr gkqkekgyrh
      121 kvpqkilskw easvglaeqy dvpkgsknrk cipgsiklds eedmpfedct ndpesehdll
      181 lngclkslaf dsehsadeke kpcaksrark ssdnpkrtsv kkghiqfeah kderrgkipe
      241 nlglnfisgd isdtqasnel sriansltgs ntapgsflfs scgkntakke fetsngdsll
      301 glpegalisk csreknkpqr slvcgskvkl cyigagdeek rsdsisictt sddgssdldp
      361 iehssesdns vleipdafdr tenmlsmqkn ekikysrfaa tntrvkakqk plisnshtdh
      421 lmgctksaep gtetsqvnls dlkastlvhk pqsdftndal spkfnlsssi ssenslikgg
      481 aanqallhsk skqpkfrsik ckhkenpvma eppvineecs lkccssdtkg splasisksg
      541 kvdglkllnn mhektrdssd ietavvkhvl selkelsyrs lgedvsdsgt skpskpllfs
      601 sassqnhipi epdykfstll mmlkdmhdsk tkeqrlmtaq nlvsyrspgr gdcstnspvg
      661 vskvlvsggs thnsekkgdg tqnsanpsps ggdsalsgel saslpgllsd krdlpasgks
      721 rsdcvtrrnc grskpssklr dafsaqmvkn tvnrkalkte rkrklnqlps vtldavlqgd
      781 rerggslrgg aedpskedpl qimghltsed gdhfsdvhfd skvkqsdpgk isekglsfen
      841 gkgpeldsvm nsendelngv nqvvpkkrwq rlnqrrtkpr krmnrfkeke nsecafrvll
      901 psdpvqegrd efpehrtpsa sileeplteq nhadcldsag prlnvcdkss asigdmekep
      961 gipsltpqae lpepavrsek krlrkpskwl leyteeydqi fapkkkqkkv qeqvhkvssr
     1021 ceeesllarg rssaqnkqvd enslistkee ppvlereapf legplaqsel ggghaelpql
     1081 tlsvpvapev sprpalesee llvktpgnye skrqrkptkk llesndldpg fmpkkgdlgl
     1141 skkcyeaghl engitescat syskdfgggt tkifdkprkr krqrhaaakm qckkvkndds
     1201 skeipgsege lmphrtatsp ketveegveh dpgmpaskkm qgergggaal kenvcqncek
     1261 lgelllceaq ccgafhlecl gltemprgkf icnecrtesc tvtrarvqwr slgnlrllgs
     1321 skspasasqv agitgihtcf vckqsgedvk rcllplcgkf yheecvqkyp ptvmqnkgfr
     1381 cslhicitch aanpanvsas kgrlmrcvrc pvayhandfc laagskilas nsiicpnhft
     1441 prrgcrnheh vnvswcfvcs eggsllccds cpaafhrecl nidipegnwy cndckagkkp
     1501 hyreivwvkv gryrwwpaei chpravpsni dkmrhdvgef pvlffgsndy lwthqarvfp
     1561 ymegdvsskd kmgkgvdgty kkalqeaaar feelkaqkel rqlqedrknd kkpppykhik
     1621 vnrpigrvqi ftadlseipr cnckatdenp cgidsecinr mllyechptv cpaggrcqnq
     1681 cfskrqypev eifrtlqrgw glrtktdikk gefvneyvge lideeecrar iryaqehdit
     1741 nfymltldkd riidagpkgn yarfmnhccq pncetqkwsv ngdtrvglfa lsdikagtel
     1801 tfnynleclg ngktvckcga pncsgflgvr pknqpiatee kskkfkkkqq gkrrtqgeit
     1861 keredecfsc gdagqlvsck kpgcpkvyha dclnltkrpa gkwecpwhqc dicgkeaasf
     1921 cemcpssfck qhregmlfis kldgrlscte hdpcgpnple pgeireyvpp pvplppgpst
     1981 hlaeqstgma aqapkmsdkp padtnqmlsl skkalagtcq rpllperple rtdsrpqpld
     2041 kvrdlagsgt ksqslvssqr pldrppavag prpqlsdkps pvtspsssps vrsqplerpl
     2101 gtadprldks igaasprpqs lektsvptgl rlpppdrlli tsspkpqtsd rptdkphasl
     2161 sqrlpppekv lsavvqtlva kekalrpvdq ntqsknraal vmdlidltpr qkeraasphq
     2221 vtpqadekmp vlessswpas kglghmprav ekgcvsdplq tsgkaaapse dpwqavkslt
     2281 qarllsqppa kaflyepttq asgrasagae qtpgplsqsp glvkqakqmv ggqqlpalaa
     2341 ksgqsfrslg kapaslptee kklvtteqsp walgkassra glwpivagqt laqscwsags
     2401 tqtlaqtcws lgrgqdpkpe qntlpalnqa psshkcaese qk
//
LOCUS       NP_001393544            1043 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 5 [Homo sapiens].
ACCESSION   NP_001393544
VERSION     NP_001393544.1
DBSOURCE    REFSEQ: accession NM_001406615.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1043)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1043)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1043)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1043)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1043)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1043)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1043)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.79665.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1043
                     /product="hamartin isoform 5"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=116145
     Region          16..598
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <587..>839
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1043
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406615.1:706..3837"
                     /note="isoform 5 is encoded by transcript variant 29"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mdtdvvvltt gvlvlitmlp mipqsgkqhl ldffdifgrl sswclkkpgh vaevylvhlh
       61 asvyalfhrl ygmypcnfvs flrshysmke nletfeevvk pmmehvrihp elvtgskdhe
      121 ldprrwkrle thdvviecak isldpteasy edgysvshqi sarfphrsad vttspyadtq
      181 nsygcatstp ystsrlmlln mpgqlpqtls spstrlitep pqatlwspsm vcgmttppts
      241 pgnvppdlsh pyskvfgtta ggkgtplgtp atspppaplc hsddyvhisl pqatvtpprk
      301 eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed siekdkeeaa
      361 isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv npeplhssld
      421 klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp trvgfgsgqp
      481 ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr liqqgadahs
      541 kelnklplps ksvdwthfgg sppsdeirtl rdqllllhnq llyerfkrqq halrnrrllr
      601 kvikaaalee hnaamkdqlk lqekdiqmwk vslqkeqary nqlqeqrdtm vtklhsqirq
      661 lqhdreefyn qsqelqtkle dcrnmiaelr ielkkannkv chtelllsqv sqklsnsesv
      721 qqqmeflnrq llvlgevnel yleqlqnkhs dttkevemmk aayrkelekn rshvlqqtqr
      781 ldtsqkrile leshlakkdh llleqkkyle dvklqargql qaaesryeaq kritqvfele
      841 ildlygrlek dgllkkleee kaeaaeaaee rldccndgcs dsmvghneea sghngetktp
      901 rpssargssg srggggssss sselstpekp phqragpfss rwettmgeas asipttvgsl
      961 pssksflgmk arelfrnkse sqcdedgmts slseslktel gkdlgveaki plnldgphps
     1021 pptpdsvgql himdynethh ehs
//
LOCUS       NP_001424951            2331 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HECTD1 isoform 6 [Homo sapiens].
ACCESSION   NP_001424951 XP_016876640 XP_054231759
VERSION     NP_001424951.1
DBSOURCE    REFSEQ: accession NM_001438022.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2331)
  AUTHORS   Oxman,E., Li,H., Wang,H.Y. and Zohn,I.E.
  TITLE     Identification and functional analysis of rare HECTD1 missense
            variants in human neural tube defects
  JOURNAL   Hum Genet 143 (3), 263-277 (2024)
   PUBMED   38451291
  REMARK    GeneRIF: Identification and functional analysis of rare HECTD1
            missense variants in human neural tube defects.
REFERENCE   2  (residues 1 to 2331)
  AUTHORS   Zhang,J., Xin,Y., Ling,X., Liang,H., Zhang,L., Fang,C. and Ma,J.
  TITLE     Nucleoporin 93, a new substrate of the E3 ubiquitin protein ligase
            HECTD1, promotes esophageal squamous cell carcinoma progression
  JOURNAL   Hum Cell 37 (1), 245-257 (2024)
   PUBMED   37993750
  REMARK    GeneRIF: Nucleoporin 93, a new substrate of the E3 ubiquitin
            protein ligase HECTD1, promotes esophageal squamous cell carcinoma
            progression.
REFERENCE   3  (residues 1 to 2331)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 2331)
  AUTHORS   Vaughan,N., Scholz,N., Lindon,C. and Licchesi,J.D.F.
  TITLE     The E3 ubiquitin ligase HECTD1 contributes to cell proliferation
            through an effect on mitosis
  JOURNAL   Sci Rep 12 (1), 13160 (2022)
   PUBMED   35915203
  REMARK    GeneRIF: The E3 ubiquitin ligase HECTD1 contributes to cell
            proliferation through an effect on mitosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2331)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 2331)
  AUTHORS   Aleidi,S.M., Yang,A., Sharpe,L.J., Rao,G., Cochran,B.J., Rye,K.A.,
            Kockx,M., Brown,A.J. and Gelissen,I.C.
  TITLE     The E3 ubiquitin ligase, HECTD1, is involved in ABCA1-mediated
            cholesterol export from macrophages
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1863 (4), 359-368 (2018)
   PUBMED   29306077
  REMARK    GeneRIF: HECTD1 may be involved in the regulation of ABCA1-mediated
            cholesterol export from unloaded macrophages to apoA-I.
REFERENCE   7  (residues 1 to 2331)
  AUTHORS   Fang,S., Guo,H., Cheng,Y., Zhou,Z., Zhang,W., Han,B., Luo,W.,
            Wang,J., Xie,W. and Chao,J.
  TITLE     circHECTD1 promotes the silica-induced pulmonary
            endothelial-mesenchymal transition via HECTD1
  JOURNAL   Cell Death Dis 9 (3), 396 (2018)
   PUBMED   29540674
  REMARK    GeneRIF: SiO2 concomitantly increased circHECTD1 expression, which,
            in turn, inhibited HECTD1 protein expression.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 2331)
  AUTHORS   Shen,X., Jia,Z., D'Alonzo,D., Wang,X., Bruder,E., Emch,F.H., De
            Geyter,C. and Zhang,H.
  TITLE     HECTD1 controls the protein level of IQGAP1 to regulate the
            dynamics of adhesive structures
  JOURNAL   Cell Commun Signal 15 (1), 2 (2017)
   PUBMED   28073378
  REMARK    GeneRIF: Hectd1 regulates the protein level of IQGAP1 through
            ubiquitination.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 2331)
  AUTHORS   Helander,S., Montecchio,M., Lemak,A., Fares,C., Almlof,J., Yi,Y.,
            Yee,A., Arrowsmith,C., DhePaganon,S. and Sunnerhagen,M.
  TITLE     Basic Tilted Helix Bundle - a new protein fold in human
            FKBP25/FKBP3 and HectD1
  JOURNAL   Biochem Biophys Res Commun 447 (1), 26-31 (2014)
   PUBMED   24667607
  REMARK    GeneRIF: our high-resolution structures show a new fold composed of
            five small helices where H3 and H4 are tilted in a novel
            arrangement; we call this fold the Basic Tilted Helix Bundle (BTHB)
            domain.
REFERENCE   10 (residues 1 to 2331)
  AUTHORS   Tran,H., Bustos,D., Yeh,R., Rubinfeld,B., Lam,C., Shriver,S.,
            Zilberleyb,I., Lee,M.W., Phu,L., Sarkar,A.A., Zohn,I.E.,
            Wertz,I.E., Kirkpatrick,D.S. and Polakis,P.
  TITLE     HectD1 E3 ligase modifies adenomatous polyposis coli (APC) with
            polyubiquitin to promote the APC-axin interaction
  JOURNAL   J Biol Chem 288 (6), 3753-3767 (2013)
   PUBMED   23277359
  REMARK    GeneRIF: HectD1 promotes the APC-Axin interaction to negatively
            regulate Wnt signaling.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136418.4, AL121808.4 and KC877516.1.
            
            On or before Apr 14, 2025 this sequence version replaced
            XP_016876640.1, XP_054231759.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2691685.1,
                                           SRR14372079.3486628.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2331
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..2331
                     /product="E3 ubiquitin-protein ligase HECTD1 isoform 6"
                     /EC_number="2.3.2.26"
                     /note="E3 ubiquitin-protein ligase HECTD1; E3 ligase for
                     inhibin receptor; HECT domain-containing protein 1; HECT
                     domain containing E3 ubiquitin protein ligase 1; HECT-type
                     E3 ubiquitin transferase HECTD1"
                     /calculated_mol_wt=260688
     Region          <366..>479
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          366..393
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          396..426
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(397,401..402,405..407,409..410,414,417,426,428,
                     432..433,436..438,440..441,445,448,457,459,461,465..466,
                     469..471,473..474,478)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          428..457
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1107..1240
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     Region          1277..>1302
                     /region_name="MIB_HERC2"
                     /note="Mib_herc2; pfam06701"
                     /db_xref="CDD:461991"
     Region          1614..1679
                     /region_name="BTHB_HectD1"
                     /note="basic tilted helix bundle (BTHB) domain found in
                     HECT domain-containing protein 1 (HectD1) and similar
                     proteins; cd21062"
                     /db_xref="CDD:439138"
     Region          1852..2329
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(1858,1887,1897,1984,2262,2294..2295,2298..2302,2322,
                     2328)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(2077,2080..2081,2083..2084,2087,2129,2131,
                     2135..2136,2138,2144,2149,2166,2170)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..2331
                     /gene="HECTD1"
                     /gene_synonym="EULIR"
                     /coded_by="NM_001438022.1:800..7795"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="GeneID:25831"
                     /db_xref="HGNC:HGNC:20157"
                     /db_xref="MIM:618649"
ORIGIN      
        1 madvdpdtll ewlqmgqgde rdmqlialeq lcmlllmsdn vdrcfetcpp rtflpalcki
       61 fldesapdnv levtaraity yldvsaectr rivgvdgaik alcnrlvvve lnnrtsrdla
      121 eqcvkvleli ctresgavfe agglncvltf irdsghlvhk dtlhsamavv srlcgkmepq
      181 dssleicves lssllkhedh qvsdgalrcf asladrftrr gvdpaplakh glteellsrm
      241 aaaggtvsgp ssackpgrst tgapsttads klsnqvstiv sllstlcrgs pvvthdllrs
      301 elpdsiesal qgdercvldt mrlvdlllvl lfegrkalpk ssagstgrip glrrldssge
      361 rshrqlidci rskdtdalid aidtgafevn fmddvgqtll nwasafgtqe mveflcerga
      421 dvnrgqrsss lhyaacfgrp qvaktllrhg anpdlrdedg ktpldkarer ghsevvailq
      481 spgdwmcpvn kgddkkkkdt nkdeeecnep kgdpemapiy lkrllpvfaq tfqqtmlpsi
      541 rkaslalirk mihfcseall kevcdsdvgh nlptilveit atvldqeddd dghllalqii
      601 rdlvdkggdi fldqlarlgv iskvstlagp ssddeneees kpekedepqe dakelqqgkp
      661 yhwrdwsiir grdclyiwsd aaalelsngs ngwfrfildg klatmyssgs peggsdsses
      721 rsefleklqr argqvkpsts sqpilsapgp tkltvgnwsl tclkegeiai hnsdgqqati
      781 lkedlpgfvf esnrgtkhsf taetslgsef vtgwtgkrgr klksklektk qkvrtmardl
      841 yddhfkaves mprgvvvtlr niatqlessw elhtnrqcie sentwrdlmk talenlivll
      901 kdentispye mcssglvqal ltvlnnsmdl dmkqdcsqlv erinvfktaf seneddesrp
      961 avalirklia vlesierlpl hlydtpgsty nlqiltrrlr frlerapget alidrtgrml
     1021 kmeplatves leqyllkmva kqwydfdrss fvfvrklreg qnfifrhqhd fdengiiywi
     1081 gtnaktayew vnpaayglvv vtssegrnlp ygrledilsr dnsalnchsn ddknawfaid
     1141 lglwvipsay tlrhargygr salrnwvfqv skdgqnwtsl ythvddcsln epgstatwpl
     1201 dppkdekqgw rhvrikqmgk nasgqthyls lsgfelygtv ngvcedqlgk aakeaeanlr
     1261 rqrrlvrsqv lkymvpgarv irgldwkwrd qdgspqgegt vtgelhnasp lmgaqsfpnl
     1321 ttpgttstvt mstssvtsss nvatattvls vgqslsntlt tsltstsses dtgqeaeysl
     1381 ydfldscras tllaelddde dlpepdeedd eneddnqedq eyeevmilrr pslqrragsr
     1441 sdvthhavts qlpqvpagag srpigeqeee eyetkggrrr twdddyvlkr qfsalvpafd
     1501 prpgrtnvqq ttdleipppg tphselleev ectpsprlal tlkvtglgtt revelpltnf
     1561 rstifyyvqk llqlscngnv ksdklrriwe ptytimyrem kdsdkekeng kmgcwsiehv
     1621 eqylgtdelp kndlitylqk nadaaflrhw kltgtnksir knrncsqlia aykdfcehgt
     1681 ksglnqgais tlqssdilnl tkeqpqakag ngqnscgved vlqllrilyi vasdpysris
     1741 qedgdeqpqf tfppdeftsk kittkilqqi eeplalasga lpdwceqlts kcpflipfet
     1801 rqlyftctaf gasraivwlq nrreatvert rttssvrrdd pgefrvgrlk hervkvprge
     1861 slmewaenvm qihadrksvl eveflgeegt glgptlefya lvaaefqrtd lgawlcddnf
     1921 pddesrhvdl ggglkppgyy vqrscglfta pfpqdsdele ritklfhflg iflakciqdn
     1981 rlvdlpiskp ffklmcmgdi ksnmskliye srgdrdlhct esqseastee ghdslsvgsf
     2041 eedsksefil dppkpkppaw fngiltwedf elvnphrarf lkeikdlaik rrqilsnkgl
     2101 sedekntklq elvlknpsgs gpplsiedlg lnfqfcpssr iygftavdlk psgedemitm
     2161 dnaeeyvdlm fdfcmhtgiq kqmeafrdgf nkvfpmekls sfsheevqmi lcgnqspswa
     2221 aediinytep klgytrdspg flrfvrvlcg mssderkafl qfttgcstlp pgglanlhpr
     2281 ltvvrkvdat dasypsvntc vhylklpeys seeimrerll aatmekgfhl n
//
LOCUS       NP_001394384            2760 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform q [Homo sapiens].
ACCESSION   NP_001394384
VERSION     NP_001394384.1
DBSOURCE    REFSEQ: accession NM_001407455.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2760)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2760)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2760)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2760)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2760)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2760)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2760)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2760)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2760)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2760)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.452703.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2760
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2760
                     /product="adenomatous polyposis coli protein isoform q"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=302136
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Region          <8..272
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          239..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          <307..365
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          389..425
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          429..470
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          433..470
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          480..512
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(503,507,511,550,554,558,595,599,603)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          520..561
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          566..606
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          570..604
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          608..648
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          612..648
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          649..936
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          953..1052
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1174..>1191
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1200..1285
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1208..1618
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1288..1310
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1554..1577
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1579..1632
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1633..1654
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1663..1756
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1790..1864
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1950..1969
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2140..2485
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2587..2760
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2760
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407455.1:168..8450"
                     /note="isoform q is encoded by transcript variant 25"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrriar iqqiekdilr irqllqsqat
      241 eaerssqnkh etgshdaerq negqgvgein matsgngqgs ttrmdhetas vlssssthsa
      301 prrltshlgt kiraycetcw ewqeahepgm dqdknpmpap vehqicpavc vlmklsfdee
      361 hrhamnelgr katrgissqe lgqglsgglq aiaellqvdc emygltndhy sitlrryagm
      421 altnltfgdv ankatlcsmk gcmralvaql ksesedlqqv iasvlrnlsw radvnskktl
      481 revgsvkalm ecalevkkes tlksvlsalw nlsahctenk adicavdgal aflvgtltyr
      541 sqtntlaiie sgggilrnvs sliatnedhr qilrennclq tllqhlkshs ltivsnacgt
      601 lwnlsarnpk dqealwdmga vsmlknlihs khkmiamgsa aalrnlmanr pakykdanim
      661 spgsslpslh vrkqkaleae ldaqhlsetf dnidnlspka shrskqrhkq slygdyvfdt
      721 nrhddnrsdn fntgnmtvls pylnttvlps ssssrgslds srsekdrsle rergiglgny
      781 hpatenpgts skrglqistt aaqiakvmee vsaihtsqed rssgsttelh cvtdernalr
      841 rssaahthsn tynftksens nrtcsmpyak leykrssnds lnsvsssdgy gkrgqmkpsi
      901 esyseddesk fcsygqypad lahkihsanh mddndgeldt pinyslkysd eqlnsgrqsp
      961 sqnerwarpk hiiedeikqs eqrqsrnqst typvytestd dkhlkfqphf gqqecvspyr
     1021 srgangsetn rvgsnhginq nvsqslcqed dyeddkptny seryseeeqh eeeerptnys
     1081 ikyneekrhv dqpidyslky atdipssqkq sfsfsksssg qssktehmss ssentstpss
     1141 nakrqnqlhp ssaqsrsgqp qkaatckvss inqetiqtyc vedtpicfsr csslsslssa
     1201 edeigcnqtt qeadsantlq iaeikekigt rsaedpvsev pavsqhprtk ssrlqgssls
     1261 sesarhkave fssgakspsk sgaqtpkspp ehyvqetplm fsrctsvssl dsfesrsias
     1321 svqsepcsgm vsgiispsdl pdspgqtmpp srsktppppp qtaqtkrevp knkaptaekr
     1381 esgpkqaavn aavqrvqvlp dadtllhfat estpdgfscs sslsalslde pfiqkdvelr
     1441 imppvqendn gneteseqpk esnenqekea ektidsekdl lddsddddie ileeciisam
     1501 ptkssrkakk paqtasklpp pvarkpsqlp vykllpsqnr lqpqkhvsft pgddmprvyc
     1561 vegtpinfst atslsdltie sppnelaage gvrggaqsge fekrdtipte grstdeaqgg
     1621 ktssvtipel ddnkaeegdi laecinsamp kgkshkpfrv kkimdqvqqa sasssapnkn
     1681 qldgkkkkpt spvkpipqnt eyrtrvrkna dsknnlnaer vfsdnkdskk qnlknnskvf
     1741 ndklpnnedr vrgsfafdsp hhytpiegtp ycfsrndsls sldfddddvd lsrekaelrk
     1801 akenkeseak vtshteltsn qqsanktqai akqpinrgqp kpilqkqstf pqsskdipdr
     1861 gaatdeklqn faientpvcf shnsslssls didqennnke nepiketepp dsqgepskpq
     1921 asgyapksfh vedtpvcfsr nsslsslsid seddllqeci ssampkkkkp srlkgdnekh
     1981 sprnmggilg edltldlkdi qrpdsehgls pdsenfdwka iqegansivs slhqaaaaac
     2041 lsrqassdsd silslksgis lgspfhltpd qeekpftsnk gprilkpgek stletkkies
     2101 eskgikggkk vykslitgkv rsnseisgqm kqplqanmps isrgrtmihi pgvrnsssst
     2161 spvskkgppl ktpaskspse gqtattsprg akpsvksels pvarqtsqig gsskapsrsg
     2221 srdstpsrpa qqplsrpiqs pgrnsispgr ngisppnkls qlprtsspst astkssgsgk
     2281 msytspgrqm sqqnltkqtg lsknassipr sesaskglnq mnngngankk velsrmsstk
     2341 ssgsesdrse rpvlvrqstf ikeapsptlr rkleesasfe slspssrpas ptrsqaqtpv
     2401 lspslpdmsl sthssvqagg wrklppnlsp tieyndgrpa krhdiarshs espsrlpinr
     2461 sgtwkrehsk hssslprvst wrrtgssssi lsassessek aksedekhvn sisgtkqske
     2521 nqvsakgtwr kikenefspt nstsqtvssg atngaesktl iyqmapavsk tedvwvried
     2581 cpinnprsgr sptgntppvi dsvsekanpn ikdskdnqak qnvgngsvpm rtvglenrln
     2641 sfiqvdapdq kgteikpgqn npvpvsetne ssivertpfs ssssskhssp sgtvaarvtp
     2701 fnynpsprks sadstsarps qiptpvnnnt kkrdsktdst essgtqspkr hsgsylvtsv
//
LOCUS       NP_001392809            1041 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 7 [Homo sapiens].
ACCESSION   NP_001392809
VERSION     NP_001392809.1
DBSOURCE    REFSEQ: accession NM_001405880.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1041)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1041)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1041)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1041)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1041)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1041)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1041)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.835507.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1041
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 7"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=113459
     Site            104
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          145..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          225..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          399..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          821..941
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..1041
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405880.1:697..3822"
                     /note="isoform 7 is encoded by transcript variant 21"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankgli
      481 vlgevpppeh ttdlflplss evktdhgtdk liesvsqple nhgapiighi seslstkscg
      541 alrpvngvin tlqpvladhi pgdssdaeeq lhkkqrlnlv ssssdgtcva artrpvlsck
      601 krrlvrpnsi vplskkvhrn stirpgcdvn pscalcgsgs intmppeihy eapllerlsq
      661 ldscvhpvla fpddvptslh fqsmlksqwq nkpfdkikpp kklslkhrap mpgslpdsar
      721 kdrhklvssf lttamlkhht dmssssylaa thhpphsplv rqlstssdsp apassssqvt
      781 astsqpvrrr rgessfdinn ivipmsvaat trveklqyke iltpswrevd lqslkgspde
      841 eneeiedlsd aafaalhakc eemerarwlw ttsvppqrrg srsyrssdgr ttpqlgsanp
      901 stpqpaspdv ssshslseys hgqsprspis pelhsapltp vardtprhla sedtrcstpe
      961 lgldeqsvqp werrtfplah spqaecedql daqeraarct rrtsgsktgr eteaaptspp
     1021 ivplksrhlv aaataqrpth r
//
LOCUS       NP_001357138             406 aa            linear   PRI 21-NOV-2025
DEFINITION  F-box/LRR-repeat protein 20 isoform 4 [Homo sapiens].
ACCESSION   NP_001357138 XP_005257804
VERSION     NP_001357138.2
DBSOURCE    REFSEQ: accession NM_001370209.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Liu,J., Zhan,W., Chen,G., Yan,S., Chen,W. and Li,R.
  TITLE     SP1-induced PROX1-AS1 contributes to tumor progression by
            regulating miR-326/FBXL20 axis in colorectal cancer
  JOURNAL   Cell Signal 101, 110503 (2023)
   PUBMED   36374774
  REMARK    GeneRIF: SP1-induced PROX1-AS1 contributes to tumor progression by
            regulating miR-326/FBXL20 axis in colorectal cancer.
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Sun,R. and Lim,S.O.
  TITLE     FBXL20-mediated ubiquitination triggers the proteasomal degradation
            of 4-1BB
  JOURNAL   FEBS J 289 (15), 4549-4563 (2022)
   PUBMED   35112462
  REMARK    GeneRIF: FBXL20-mediated ubiquitination triggers the proteasomal
            degradation of 4-1BB.
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Madduri,L.S.V., Brandquist,N.D., Palanivel,C., Talmon,G.A.,
            Baine,M.J., Zhou,S., Enke,C.A., Johnson,K.R., Ouellette,M.M. and
            Yan,Y.
  TITLE     p53/FBXL20 axis negatively regulates the protein stability of
            PR55alpha, a regulatory subunit of PP2A Ser/Thr phosphatase
  JOURNAL   Neoplasia 23 (12), 1192-1203 (2021)
   PUBMED   34731788
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Manne,R.K., Agrawal,Y., Malonia,S.K., Banday,S., Edachery,S.,
            Patel,A., Kumar,A., Shetty,P. and Santra,M.K.
  TITLE     FBXL20 promotes breast cancer malignancy by inhibiting apoptosis
            through degradation of PUMA and BAX
  JOURNAL   J Biol Chem 297 (4), 101253 (2021)
   PUBMED   34587475
  REMARK    GeneRIF: FBXL20 promotes breast cancer malignancy by inhibiting
            apoptosis through degradation of PUMA and BAX.
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Xiao,J., Zhang,T., Xu,D., Wang,H., Cai,Y., Jin,T., Liu,M., Jin,M.,
            Wu,K. and Yuan,J.
  TITLE     FBXL20-mediated Vps34 ubiquitination as a p53 controlled checkpoint
            in regulating autophagy and receptor degradation
  JOURNAL   Genes Dev 29 (2), 184-196 (2015)
   PUBMED   25593308
  REMARK    GeneRIF: which provides a signal to promote its ubiquitination and
            proteasomal degradation mediated by FBXL20 and the associated
            Skp1-Cullin1 complex, leading to inhibition of autophagy and
            receptor endocytosis
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Zhu,J., Li,K., Dong,L. and Chen,Y.
  TITLE     Role of FBXL20 in human colorectal adenocarcinoma
  JOURNAL   Oncol Rep 28 (6), 2290-2298 (2012)
   PUBMED   23023584
  REMARK    GeneRIF: study concludes FBXL20 plays an essential role in the
            carcinogenesis of colorectal adenocarcinoma and promotes
            carcinogenesis through the regulation of the Wnt signaling pathway
            and caspase activation
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Mells,G.F., Floyd,J.A., Morley,K.I., Cordell,H.J., Franklin,C.S.,
            Shin,S.Y., Heneghan,M.A., Neuberger,J.M., Donaldson,P.T., Day,D.B.,
            Ducker,S.J., Muriithi,A.W., Wheater,E.F., Hammond,C.J.,
            Dawwas,M.F., Jones,D.E., Peltonen,L., Alexander,G.J., Sandford,R.N.
            and Anderson,C.A.
  CONSRTM   UK PBC Consortium; Wellcome Trust Case Control Consortium 3
  TITLE     Genome-wide association study identifies 12 new susceptibility loci
            for primary biliary cirrhosis
  JOURNAL   Nat Genet 43 (4), 329-332 (2011)
   PUBMED   21399635
  REMARK    Erratum:[Nat Genet. 2011 Nov;43(11):1164. Richardson,Paul [added];
            Nasr, Ikram [added]; Aspinall,Richard [added]]
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005288.1 and AC015910.10.
            
            On Sep 26, 2022 this sequence version replaced NP_001357138.1.
            
            Summary: Members of the F-box protein family, such as FBXL20, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3225166.1,
                                           SRR14038194.1683796.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..406
                     /product="F-box/LRR-repeat protein 20 isoform 4"
                     /note="F-box protein FBL2"
                     /calculated_mol_wt=45001
     Region          24..68
                     /region_name="F-box_FBXL2-like"
                     /note="F-box domain found in F-box/LRR-repeat protein 2
                     (FBXL2), F-box/LRR-repeat protein 20 (FBXL20) and similar
                     proteins; cd22115"
                     /db_xref="CDD:438887"
     Site            order(24..27,29..30,33..34,37..43,46,48..55,57..58,66)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438887"
     Region          <91..259
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          95..108
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          121..140
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          141..166
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          167..192
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          190..364
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          193..218
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          219..244
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          245..270
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          271..296
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          297..319
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          326..350
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          351..376
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..406
                     /gene="FBXL20"
                     /gene_synonym="Fbl2; Fbl20"
                     /coded_by="NM_001370209.3:337..1557"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:84961"
                     /db_xref="HGNC:HGNC:24679"
                     /db_xref="MIM:609086"
ORIGIN      
        1 mapsrdrllh fgfkatmfsn sdeavinkkl pkelllrifs fldvvtlcrc aqvsrawnvl
       61 aldgsnwqri dlfdfqrdie grvveniskr cggflrklsl rgclgvgdna lrtfaqncrn
      121 ievlnlngct kttdaegcpl leqlniswcd qvtkdgiqal vrgcgglkal flkgctqled
      181 ealkyigahc pelvtlnlqt clqitdegli ticrgchklq slcasgcsni tdailnalgq
      241 ncprlrilev arcsqltdvg fttlarnche lekmdleecv qitdstliql sihcprlqvl
      301 slshcelitd dgirhlgnga cahdqlevie ldncplitda slehlkschs lerielydcq
      361 qitragikrl rthlpnikvh ayfapvtppp svggsrqrfc rcciil
//
LOCUS       NP_001424277            2549 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HECTD1 isoform 3 [Homo sapiens].
ACCESSION   NP_001424277 XP_024305295 XP_054231752
VERSION     NP_001424277.1
DBSOURCE    REFSEQ: accession NM_001437348.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2549)
  AUTHORS   Oxman,E., Li,H., Wang,H.Y. and Zohn,I.E.
  TITLE     Identification and functional analysis of rare HECTD1 missense
            variants in human neural tube defects
  JOURNAL   Hum Genet 143 (3), 263-277 (2024)
   PUBMED   38451291
  REMARK    GeneRIF: Identification and functional analysis of rare HECTD1
            missense variants in human neural tube defects.
REFERENCE   2  (residues 1 to 2549)
  AUTHORS   Zhang,J., Xin,Y., Ling,X., Liang,H., Zhang,L., Fang,C. and Ma,J.
  TITLE     Nucleoporin 93, a new substrate of the E3 ubiquitin protein ligase
            HECTD1, promotes esophageal squamous cell carcinoma progression
  JOURNAL   Hum Cell 37 (1), 245-257 (2024)
   PUBMED   37993750
  REMARK    GeneRIF: Nucleoporin 93, a new substrate of the E3 ubiquitin
            protein ligase HECTD1, promotes esophageal squamous cell carcinoma
            progression.
REFERENCE   3  (residues 1 to 2549)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 2549)
  AUTHORS   Vaughan,N., Scholz,N., Lindon,C. and Licchesi,J.D.F.
  TITLE     The E3 ubiquitin ligase HECTD1 contributes to cell proliferation
            through an effect on mitosis
  JOURNAL   Sci Rep 12 (1), 13160 (2022)
   PUBMED   35915203
  REMARK    GeneRIF: The E3 ubiquitin ligase HECTD1 contributes to cell
            proliferation through an effect on mitosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 2549)
  AUTHORS   Aleidi,S.M., Yang,A., Sharpe,L.J., Rao,G., Cochran,B.J., Rye,K.A.,
            Kockx,M., Brown,A.J. and Gelissen,I.C.
  TITLE     The E3 ubiquitin ligase, HECTD1, is involved in ABCA1-mediated
            cholesterol export from macrophages
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1863 (4), 359-368 (2018)
   PUBMED   29306077
  REMARK    GeneRIF: HECTD1 may be involved in the regulation of ABCA1-mediated
            cholesterol export from unloaded macrophages to apoA-I.
REFERENCE   7  (residues 1 to 2549)
  AUTHORS   Fang,S., Guo,H., Cheng,Y., Zhou,Z., Zhang,W., Han,B., Luo,W.,
            Wang,J., Xie,W. and Chao,J.
  TITLE     circHECTD1 promotes the silica-induced pulmonary
            endothelial-mesenchymal transition via HECTD1
  JOURNAL   Cell Death Dis 9 (3), 396 (2018)
   PUBMED   29540674
  REMARK    GeneRIF: SiO2 concomitantly increased circHECTD1 expression, which,
            in turn, inhibited HECTD1 protein expression.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 2549)
  AUTHORS   Shen,X., Jia,Z., D'Alonzo,D., Wang,X., Bruder,E., Emch,F.H., De
            Geyter,C. and Zhang,H.
  TITLE     HECTD1 controls the protein level of IQGAP1 to regulate the
            dynamics of adhesive structures
  JOURNAL   Cell Commun Signal 15 (1), 2 (2017)
   PUBMED   28073378
  REMARK    GeneRIF: Hectd1 regulates the protein level of IQGAP1 through
            ubiquitination.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 2549)
  AUTHORS   Helander,S., Montecchio,M., Lemak,A., Fares,C., Almlof,J., Yi,Y.,
            Yee,A., Arrowsmith,C., DhePaganon,S. and Sunnerhagen,M.
  TITLE     Basic Tilted Helix Bundle - a new protein fold in human
            FKBP25/FKBP3 and HectD1
  JOURNAL   Biochem Biophys Res Commun 447 (1), 26-31 (2014)
   PUBMED   24667607
  REMARK    GeneRIF: our high-resolution structures show a new fold composed of
            five small helices where H3 and H4 are tilted in a novel
            arrangement; we call this fold the Basic Tilted Helix Bundle (BTHB)
            domain.
REFERENCE   10 (residues 1 to 2549)
  AUTHORS   Tran,H., Bustos,D., Yeh,R., Rubinfeld,B., Lam,C., Shriver,S.,
            Zilberleyb,I., Lee,M.W., Phu,L., Sarkar,A.A., Zohn,I.E.,
            Wertz,I.E., Kirkpatrick,D.S. and Polakis,P.
  TITLE     HectD1 E3 ligase modifies adenomatous polyposis coli (APC) with
            polyubiquitin to promote the APC-axin interaction
  JOURNAL   J Biol Chem 288 (6), 3753-3767 (2013)
   PUBMED   23277359
  REMARK    GeneRIF: HectD1 promotes the APC-Axin interaction to negatively
            regulate Wnt signaling.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136418.4, AL121808.4 and KC877516.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_024305295.1, XP_054231752.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1328144.1,
                                           SRR14038197.500304.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..2549
                     /product="E3 ubiquitin-protein ligase HECTD1 isoform 3"
                     /EC_number="2.3.2.26"
                     /note="E3 ubiquitin-protein ligase HECTD1; E3 ligase for
                     inhibin receptor; HECT domain-containing protein 1; HECT
                     domain containing E3 ubiquitin protein ligase 1; HECT-type
                     E3 ubiquitin transferase HECTD1"
                     /calculated_mol_wt=282191
     Region          <366..>479
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          366..393
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          396..426
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(397,401..402,405..407,409..410,414,417,426,428,
                     432..433,436..438,440..441,445,448,457,459,461,465..466,
                     469..471,473..474,478)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          428..457
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1107..1240
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     Region          1277..1335
                     /region_name="MIB_HERC2"
                     /note="Mib_herc2; pfam06701"
                     /db_xref="CDD:461991"
     Region          2070..2547
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(2076,2105,2115,2202,2480,2512..2513,2516..2520,2540,
                     2546)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(2295,2298..2299,2301..2302,2305,2347,2349,
                     2353..2354,2356,2362,2367,2384,2388)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..2549
                     /gene="HECTD1"
                     /gene_synonym="EULIR"
                     /coded_by="NM_001437348.1:800..8449"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:25831"
                     /db_xref="HGNC:HGNC:20157"
                     /db_xref="MIM:618649"
ORIGIN      
        1 madvdpdtll ewlqmgqgde rdmqlialeq lcmlllmsdn vdrcfetcpp rtflpalcki
       61 fldesapdnv levtaraity yldvsaectr rivgvdgaik alcnrlvvve lnnrtsrdla
      121 eqcvkvleli ctresgavfe agglncvltf irdsghlvhk dtlhsamavv srlcgkmepq
      181 dssleicves lssllkhedh qvsdgalrcf asladrftrr gvdpaplakh glteellsrm
      241 aaaggtvsgp ssackpgrst tgapsttads klsnqvstiv sllstlcrgs pvvthdllrs
      301 elpdsiesal qgdercvldt mrlvdlllvl lfegrkalpk ssagstgrip glrrldssge
      361 rshrqlidci rskdtdalid aidtgafevn fmddvgqtll nwasafgtqe mveflcerga
      421 dvnrgqrsss lhyaacfgrp qvaktllrhg anpdlrdedg ktpldkarer ghsevvailq
      481 spgdwmcpvn kgddkkkkdt nkdeeecnep kgdpemapiy lkrllpvfaq tfqqtmlpsi
      541 rkaslalirk mihfcseall kevcdsdvgh nlptilveit atvldqeddd dghllalqii
      601 rdlvdkggdi fldqlarlgv iskvstlagp ssddeneees kpekedepqe dakelqqgkp
      661 yhwrdwsiir grdclyiwsd aaalelsngs ngwfrfildg klatmyssgs peggsdsses
      721 rsefleklqr argqvkpsts sqpilsapgp tkltvgnwsl tclkegeiai hnsdgqqati
      781 lkedlpgfvf esnrgtkhsf taetslgsef vtgwtgkrgr klksklektk qkvrtmardl
      841 yddhfkaves mprgvvvtlr niatqlessw elhtnrqcie sentwrdlmk talenlivll
      901 kdentispye mcssglvqal ltvlnnsmdl dmkqdcsqlv erinvfktaf seneddesrp
      961 avalirklia vlesierlpl hlydtpgsty nlqiltrrlr frlerapget alidrtgrml
     1021 kmeplatves leqyllkmva kqwydfdrss fvfvrklreg qnfifrhqhd fdengiiywi
     1081 gtnaktayew vnpaayglvv vtssegrnlp ygrledilsr dnsalnchsn ddknawfaid
     1141 lglwvipsay tlrhargygr salrnwvfqv skdgqnwtsl ythvddcsln epgstatwpl
     1201 dppkdekqgw rhvrikqmgk nasgqthyls lsgfelygtv ngvcedqlgk aakeaeanlr
     1261 rqrrlvrsqv lkymvpgarv irgldwkwrd qdgspqgegt vtgelhngwi dvtwdaggsn
     1321 syrmgaegkf dlklapgydp dtvaspkpvs stvsgttqsw sslvknncpd ktsaaagsss
     1381 rkgssssvcs vasssdislg stkterrsei vmehsivsga dvhepivvls saenvpqtev
     1441 gssssastst ltaetgsena erklgpdssv rtpgessais mgivsvsspd vssvseltnk
     1501 eaasqrplss sasnrlsvss llaagapmss sasvpnlssr etsslesfvr rvaniartna
     1561 tnnmnlsrss sdnntntlgr nvmstatspl mgaqsfpnlt tpgttstvtm stssvtsssn
     1621 vatattvlsv gqslsntltt sltstssesd tgqeaeysly dfldscrast llaelddded
     1681 lpepdeedde neddnqedqe yeevmilrrp slqrragsrs dvthhavtsq lpqvpagags
     1741 rpigeqeeee yetkggrrrt wdddyvlkrq fsalvpafdp rpgrtnvqqt tdleipppgt
     1801 phselleeve ctpsprlalt lkvtglgttr evelpltnfr stifyyvqkl lqlscngnvk
     1861 sdklrriwep tytimyremk dsdkekengk mdfcehgtks glnqgaistl qssdilnltk
     1921 eqpqakagng qnscgvedvl qllrilyiva sdpysrisqe dgdeqpqftf ppdeftskki
     1981 ttkilqqiee plalasgalp dwceqltskc pflipfetrq lyftctafga sraivwlqnr
     2041 reatvertrt tssvrrddpg efrvgrlkhe rvkvprgesl mewaenvmqi hadrksvlev
     2101 eflgeegtgl gptlefyalv aaefqrtdlg awlcddnfpd desrhvdlgg glkppgyyvq
     2161 rscglftapf pqdsdeleri tklfhflgif lakciqdnrl vdlpiskpff klmcmgdiks
     2221 nmskliyesr gdrdlhctes qseasteegh dslsvgsfee dsksefildp pkpkppawfn
     2281 giltwedfel vnphrarflk eikdlaikrr qilsnkglse dekntklqel vlknpsgsgp
     2341 plsiedlgln fqfcpssriy gftavdlkps gedemitmdn aeeyvdlmfd fcmhtgiqkq
     2401 meafrdgfnk vfpmeklssf sheevqmilc gnqspswaae diinytepkl gytrdspgfl
     2461 rfvrvlcgms sderkaflqf ttgcstlppg glanlhprlt vvrkvdatda sypsvntcvh
     2521 ylklpeysse eimrerllaa tmekgfhln
//
LOCUS       NP_001393994             412 aa            linear   PRI 21-NOV-2025
DEFINITION  merlin isoform 19 [Homo sapiens].
ACCESSION   NP_001393994
VERSION     NP_001393994.1
DBSOURCE    REFSEQ: accession NM_001407065.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 412)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 412)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 412)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 412)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 412)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005529.7 and AC004882.3.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3107730.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2155974
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..412
                     /product="merlin isoform 19"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=48150
     Region          <1..44
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          38..134
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(80..81,83..89,98,119,122..123,126)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(80,83..90,98,119,122..123,126)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(116,120)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            119..134
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          129..>189
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          168..287
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          340..>401
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..412
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_001407065.1:1007..2245"
                     /note="isoform 19 is encoded by transcript variant 27"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 mtpemweeri tawyaehrgr ardeaemeyl kiaqdlemyg vnyfairnkk gtelllgvda
       61 lglhiydpen rltpkisfpw neirnisysd keftikpldk kidvfkfnss klrvnklilq
      121 lcignhdlfm rrrkadslev qqmkaqaree karkqmerqr larekqmree aertrdeler
      181 rllqmkeeat manealmrse etadllaeka qiteeeakll aqkaaeaeqe mqrikatair
      241 teeekrlmeq kvleaevlal kmaeeserra keadqlkqdl qeareaerra kqklleiatk
      301 ptyppmnpip aplppdipsf nligdslsfd fkdtdmkrls meiekekvey mekskhlqeq
      361 lnelkteiea lklkeretal dilhnensdr ggsskhntik kpqaqgrrpi ci
//
LOCUS       NP_001427454             289 aa            linear   PRI 21-NOV-2025
DEFINITION  syntaxin-3 isoform 3 [Homo sapiens].
ACCESSION   NP_001427454
VERSION     NP_001427454.1
DBSOURCE    REFSEQ: accession NM_001440525.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Shinozuka,T., Kanda,M., Sato,Y., Shimizu,D., Tanaka,C., Umeda,S.,
            Inokawa,Y., Hattori,N., Hayashi,M., Nakayama,G. and Kodera,Y.
  TITLE     Increased STX3 transcript and protein levels were associated with
            poor prognosis in two independent cohorts of esophageal squamous
            cell carcinoma patients
  JOURNAL   Cancer Med 12 (24), 22185-22195 (2023)
   PUBMED   38014487
  REMARK    GeneRIF: Increased STX3 transcript and protein levels were
            associated with poor prognosis in two independent cohorts of
            esophageal squamous cell carcinoma patients.
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Janecke,A.R., Liu,X., Adam,R., Punuru,S., Viestenz,A., Strauss,V.,
            Laass,M., Sanchez,E., Adachi,R., Schatz,M.P., Saboo,U.S.,
            Mittal,N., Rohrschneider,K., Escher,J., Ganesh,A., Al Zuhaibi,S.,
            Al Murshedi,F., AlSaleem,B., Alfadhel,M., Al Sinani,S.,
            Alkuraya,F.S., Huber,L.A., Muller,T., Heidelberger,R. and Janz,R.
  TITLE     Pathogenic STX3 variants affecting the retinal and intestinal
            transcripts cause an early-onset severe retinal dystrophy in
            microvillus inclusion disease subjects
  JOURNAL   Hum Genet 140 (8), 1143-1156 (2021)
   PUBMED   33974130
  REMARK    GeneRIF: Pathogenic STX3 variants affecting the retinal and
            intestinal transcripts cause an early-onset severe retinal
            dystrophy in microvillus inclusion disease subjects.
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Low,S.H., Vasanji,A., Nanduri,J., He,M., Sharma,N., Koo,M.,
            Drazba,J. and Weimbs,T.
  TITLE     Syntaxins 3 and 4 are concentrated in separate clusters on the
            plasma membrane before the establishment of cell polarity
  JOURNAL   Mol Biol Cell 17 (2), 977-989 (2006)
   PUBMED   16339081
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Martin-Martin,B., Nabokina,S.M., Lazo,P.A. and Mollinedo,F.
  TITLE     Co-expression of several human syntaxin genes in neutrophils and
            differentiating HL-60 cells: variant isoforms and detection of
            syntaxin 1
  JOURNAL   J Leukoc Biol 65 (3), 397-406 (1999)
   PUBMED   10080545
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Steegmaier,M., Yang,B., Yoo,J.S., Huang,B., Shen,M., Yu,S., Luo,Y.
            and Scheller,R.H.
  TITLE     Three novel proteins of the syntaxin/SNAP-25 family
  JOURNAL   J Biol Chem 273 (51), 34171-34179 (1998)
   PUBMED   9852078
REFERENCE   8  (residues 1 to 289)
  AUTHORS   Riento,K., Galli,T., Jansson,S., Ehnholm,C., Lehtonen,E. and
            Olkkonen,V.M.
  TITLE     Interaction of Munc-18-2 with syntaxin 3 controls the association
            of apical SNAREs in epithelial cells
  JOURNAL   J Cell Sci 111 (Pt 17), 2681-2688 (1998)
   PUBMED   9701566
REFERENCE   9  (residues 1 to 289)
  AUTHORS   Galli,T., Zahraoui,A., Vaidyanathan,V.V., Raposo,G., Tian,J.M.,
            Karin,M., Niemann,H. and Louvard,D.
  TITLE     A novel tetanus neurotoxin-insensitive vesicle-associated membrane
            protein in SNARE complexes of the apical plasma membrane of
            epithelial cells
  JOURNAL   Mol Biol Cell 9 (6), 1437-1448 (1998)
   PUBMED   9614185
REFERENCE   10 (residues 1 to 289)
  AUTHORS   Delgrossi,M.H., Breuza,L., Mirre,C., Chavrier,P. and Le Bivic,A.
  TITLE     Human syntaxin 3 is localized apically in human intestinal cells
  JOURNAL   J Cell Sci 110 (Pt 18), 2207-2214 (1997)
   PUBMED   9378770
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000640.5.
            
            Summary: The gene is a member of the syntaxin family. The encoded
            protein is targeted to the apical membrane of epithelial cells
            where it forms clusters and is important in establishing and
            maintaining polarity necessary for protein trafficking involving
            vesicle fusion and exocytosis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4352442.434759.1,
                                           SRR18074969.393724.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN02400308, SAMN03267776
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..289
                     /product="syntaxin-3 isoform 3"
                     /note="syntaxin 3A; syntaxin 3B"
                     /calculated_mol_wt=32912
     Region          34..226
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     Region          194..260
                     /region_name="SNARE"
                     /note="SNARE motif; cl22856"
                     /db_xref="CDD:473982"
     Site            order(222,229,232)
                     /site_type="other"
                     /note="flanking leucine-zipper layers"
                     /db_xref="CDD:277192"
     Site            225
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277192"
     CDS             1..289
                     /gene="STX3"
                     /gene_synonym="DIAR12; MVID2; RDMVID; STX3A"
                     /coded_by="NM_001440525.1:231..1100"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="GeneID:6809"
                     /db_xref="HGNC:HGNC:11438"
                     /db_xref="MIM:600876"
ORIGIN      
        1 mkdrleqlka kqltqdddtd aveiaidnta fmdeffseie etrlnidkis ehveeakkly
       61 siilsapipe pktkddleql tteikkrann vrnklksmek hieedevrss adlrirksqh
      121 svlsrkfvev mtkyneaqvd frerskgriq rqleitgkkt tdeeleemle sgnpaiftsg
      181 iidsqiskqa lseiegrhkd ivrlessike lhdmfmdiam lvenqgsmid riennmdqsv
      241 gfveravadt kkavkyqsea rrkliiiivl vvvllgilal iiglsvgln
//
LOCUS       NP_001277006            1081 aa            linear   PRI 21-NOV-2025
DEFINITION  angiopoietin-1 receptor isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001277006 XP_005251619
VERSION     NP_001277006.2
DBSOURCE    REFSEQ: accession NM_001290077.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Chacon-Camacho,O.F., Ordaz-Robles,T., Cid-Garcia,M.A.,
            Hofmann-Blancas,M.E., Ledesma-Gil,J., Garcia-Huerta,M.M.,
            Prado-Larrea,C., Cortes-Gonzalez,V., Lozano-Garza,R.I.,
            Garcia-Vega,D., Kim,J., Khang,R., Lee,E. and Zenteno,J.C.
  TITLE     TEK gene-related primary congenital glaucoma: Phenotypic features
            and mutational spectrum in a Mexican cohort of 10 unrelated
            families
  JOURNAL   Am J Med Genet A 194 (10), e63716 (2024)
   PUBMED   38847211
  REMARK    GeneRIF: TEK gene-related primary congenital glaucoma: Phenotypic
            features and mutational spectrum in a Mexican cohort of 10
            unrelated families.
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Yu,J., Brelen,M.E., Chan,C.K.M., Chen,Z.J., Mohamed,S., Yam,J.C.,
            Lam,D.S.C., Pang,C.P., Tham,C.C. and Chen,L.J.
  TITLE     Genetic association of TIE2 with diabetic retinopathy and diabetic
            macular edema
  JOURNAL   Asia Pac J Ophthalmol (Phila) 13 (3), 100068 (2024)
   PUBMED   38750959
  REMARK    GeneRIF: Genetic association of TIE2 with diabetic retinopathy and
            diabetic macular edema.
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Jin,P., Zhang,J., Sumariwalla,P.F., Ni,I., Jorgensen,B.,
            Crawford,D., Phillips,S., Feldmann,M., Shepard,H.M. and
            Paleolog,E.M.
  TITLE     Novel splice variants derived from the receptor tyrosine kinase
            superfamily are potential therapeutics for rheumatoid arthritis
  JOURNAL   Arthritis Res Ther 10 (4), R73 (2008)
   PUBMED   18593464
REFERENCE   4  (residues 1 to 1081)
  AUTHORS   Park,E.H., Lee,J.M. and Pelletier,J.
  TITLE     The Tie2 5' untranslated region is inhibitory to 5' end-mediated
            translation initiation
  JOURNAL   FEBS Lett 580 (5), 1309-1319 (2006)
   PUBMED   16457819
  REMARK    GeneRIF: the uORFs within the Tie2 5' UTR serve to decrease the
            percent of ribosomes competent for reinitiation as these traverse
            the mRNA 5' UTR, thus minimizing interference with the internal
            ribosome entry site
REFERENCE   5  (residues 1 to 1081)
  AUTHORS   Park,E.H., Lee,J.M., Blais,J.D., Bell,J.C. and Pelletier,J.
  TITLE     Internal translation initiation mediated by the angiogenic factor
            Tie2
  JOURNAL   J Biol Chem 280 (22), 20945-20953 (2005)
   PUBMED   15802272
  REMARK    GeneRIF: Tie2 mediates internal translation initiation
REFERENCE   6  (residues 1 to 1081)
  AUTHORS   Huang,L., Turck,C.W., Rao,P. and Peters,K.G.
  TITLE     GRB2 and SH-PTP2: potentially important endothelial signaling
            molecules downstream of the TEK/TIE2 receptor tyrosine kinase
  JOURNAL   Oncogene 11 (10), 2097-2103 (1995)
   PUBMED   7478529
REFERENCE   7  (residues 1 to 1081)
  AUTHORS   Dumont,D.J., Anderson,L., Breitman,M.L. and Duncan,A.M.
  TITLE     Assignment of the endothelial-specific protein receptor tyrosine
            kinase gene (TEK) to human chromosome 9p21
  JOURNAL   Genomics 23 (2), 512-513 (1994)
   PUBMED   7835909
REFERENCE   8  (residues 1 to 1081)
  AUTHORS   Seront,E., Boon,L.M. and Vikkula,M.
  TITLE     TEK-Related Venous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301733
REFERENCE   9  (residues 1 to 1081)
  AUTHORS   Abu-Amero,K.K. and Edward,D.P.
  TITLE     Primary Congenital Glaucoma
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301314
REFERENCE   10 (residues 1 to 1081)
  AUTHORS   Partanen,J., Armstrong,E., Makela,T.P., Korhonen,J., Sandberg,M.,
            Renkonen,R., Knuutila,S., Huebner,K. and Alitalo,K.
  TITLE     A novel endothelial cell surface receptor tyrosine kinase with
            extracellular epidermal growth factor homology domains
  JOURNAL   Mol Cell Biol 12 (4), 1698-1707 (1992)
   PUBMED   1312667
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355432.7, AL355433.6 and
            AL133411.9.
            
            On Dec 12, 2023 this sequence version replaced NP_001277006.1.
            
            Summary: This gene encodes a receptor that belongs to the protein
            tyrosine kinase Tie2 family. The encoded protein possesses a unique
            extracellular region that contains two immunoglobulin-like domains,
            three epidermal growth factor (EGF)-like domains and three
            fibronectin type III repeats. The ligand angiopoietin-1 binds to
            this receptor and mediates a signaling pathway that functions in
            embryonic vascular development. Mutations in this gene are
            associated with inherited venous malformations of the skin and
            mucous membranes. Alternative splicing results in multiple
            transcript variants. Additional alternatively spliced transcript
            variants of this gene have been described, but their full-length
            nature is not known. [provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region compared to variant 1. The encoded
            isoform (2) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295043.1, SRR14038194.929248.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            regulatory uORF :: PMID: 16457819
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.2"
     Protein         1..1081
                     /product="angiopoietin-1 receptor isoform 2 precursor"
                     /EC_number="2.7.10.1"
                     /note="angiopoietin-1 receptor; tyrosine-protein kinase
                     receptor TEK; tunica interna endothelial cell kinase;
                     tyrosine-protein kinase receptor TIE-2; endothelial
                     tyrosine kinase; tyrosine kinase with Ig and EGF homology
                     domains-2; TEK tyrosine kinase, endothelial"
                     /calculated_mol_wt=118902
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2165
     mat_peptide     23..1081
                     /product="angiopoietin-1 receptor isoform 2"
                     /calculated_mol_wt=118902
     Region          24..118
                     /region_name="Ig_Tie2_1"
                     /note="Tie-2 Ig-like domain 1; pfam10430"
                     /db_xref="CDD:463089"
     Region          230..275
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domain;
                     laminins are the major noncollagenous components of
                     basement membranes that mediate cell adhesion, growth
                     migration, and differentiation; the laminin-type epidermal
                     growth factor-like module occurs in...; cd00055"
                     /db_xref="CDD:238012"
     Region          305..396
                     /region_name="IgI_Tie2"
                     /note="Immunoglobulin domain of Tie2 tyrosine kinase; a
                     member of the I-set of IgSF domains; cd20964"
                     /db_xref="CDD:409556"
     Region          305..309
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409556"
     Region          315..319
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409556"
     Region          322..331
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409556"
     Region          339..344
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409556"
     Region          348..350
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409556"
     Region          354..358
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409556"
     Region          361..369
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409556"
     Region          377..385
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409556"
     Region          388..396
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409556"
     Region          402..477
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Region          501..583
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(579..580,582..583)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          596..688
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(596,661,676)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(677..678,680..681)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          773..1075
                     /region_name="PTKc_Tie2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Tie2; cd05088"
                     /db_xref="CDD:133219"
     Site            order(787..791,795,810,812,829,833,836,843,859..862,
                     865..866,917,919,921,925..926,928,937..940,954..958,967,
                     1001)
                     /site_type="active"
                     /db_xref="CDD:133219"
     Site            order(787..788,790..791,795,810,812,829,833,843,859..862,
                     865..866,925..926,928,939)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:133219"
     Site            order(921,925,954..958,967,1001)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133219"
     Site            938..960
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:133219"
     CDS             1..1081
                     /gene="TEK"
                     /gene_synonym="CD202B; GLC3E; TIE-2; TIE2; VMCM; VMCM1"
                     /coded_by="NM_001290077.2:367..3612"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS75825.1"
                     /db_xref="GeneID:7010"
                     /db_xref="HGNC:HGNC:11724"
                     /db_xref="MIM:600221"
ORIGIN      
        1 mdslaslvlc gvslllsgtv egamdlilin slplvsdaet sltciasgwr phepitigrd
       61 fealmnqhqd plevtqdvtr ewakkvvwkr ekaskingay fcegrvrgea irirtmkmrq
      121 qasflpatlt mtvdkgdnvn isfkkvlike edaviykngs fihsvprhev pdilevhlph
      181 aqpqdagvys aryiggnlft saftrlivrr ceaqkwgpec nhlctacmnn gvchedtgec
      241 icppgfmgrt cekacelhtf grtckercsg qegcksyvfc lpdpygcsca tgwkglqcne
      301 giqrmtpkiv dlpdhievns gkfnpickas gwplptneem tlvkpdgtvl hpkdfnhtdh
      361 fsvaiftihr ilppdsgvwv csvntvagmv ekpfnisvkv lpkplnapnv idtghnfavi
      421 nissepyfgd gpikskklly kpvnhyeawq hiqvtneivt lnyleprtey elcvqlvrrg
      481 eggeghpgpv rrfttasigl ppprglnllp ksqttlnltw qpifpssedd fyveverrsv
      541 qksdqqnikv pgnltsvlln nlhpreqyvv rarvntkaqg ewsedltawt lsdilppqpe
      601 nikisniths saviswtild gysissitir ykvqgknedq hvdvkiknat itqyqlkgle
      661 petayqvdif aennigssnp afshelvtlp esqapadlgg gkmlliailg sagmtcltvl
      721 lafliilqlk ranvqrrmaq afqnvreepa vqfnsgtlal nrkvknnpdp tiypvldwnd
      781 ikfqdvigeg nfgqvlkari kkdglrmdaa ikrmkeyask ddhrdfagel evlcklghhp
      841 niinllgace hrgylylaie yaphgnlldf lrksrvletd pafaiansta stlssqqllh
      901 faadvargmd ylsqkqfihr dlaarnilvg enyvakiadf glsrgqevyv kktmgrlpvr
      961 wmaieslnys vyttnsdvws ygvllweivs lggtpycgmt caelyeklpq gyrlekplnc
     1021 ddevydlmrq cwrekpyerp sfaqilvsln rmleerktyv nttlyekfty agidcsaeea
     1081 a
//
LOCUS       NP_001394396            2714 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform r [Homo sapiens].
ACCESSION   NP_001394396
VERSION     NP_001394396.1
DBSOURCE    REFSEQ: accession NM_001407467.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2714)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2714)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2714)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2714)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2714)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2714)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2714)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2714)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2714)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2714)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.284493.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2714
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2714
                     /product="adenomatous polyposis coli protein isoform r"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=296950
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          <279..337
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          336..379
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(370,374,378,413,417,421,457,461,465)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          383..424
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          387..424
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          431..466
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          474..515
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          520..560
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          524..558
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          562..602
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          566..602
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          603..890
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          907..1006
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1128..>1145
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1154..1239
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1162..1572
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1242..1264
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1508..1531
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1533..1586
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1587..1608
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1617..1710
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1744..1818
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1904..1923
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2094..2439
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2541..2714
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2714
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407467.1:60..8204"
                     /note="isoform r is encoded by transcript variant 31"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrssqn khetgshdae rqnegqgvge
      241 inmatsgngq gsttrmdhet asvlssssth saprrltshl gtkiraycet cwewqeahep
      301 gmdqdknpmp apvehqicpa vcvlmklsfd eehrhamnel gglqaiaell qvdcemyglt
      361 ndhysitlrr yagmaltnlt fgdvankatl csmkgcmral vaqlksesed lqqviasvlr
      421 nlswradvns kktlrevgsv kalmecalev kkestlksvl salwnlsahc tenkadicav
      481 dgalaflvgt ltyrsqtntl aiiesgggil rnvssliatn edhrqilren nclqtllqhl
      541 kshsltivsn acgtlwnlsa rnpkdqealw dmgavsmlkn lihskhkmia mgsaaalrnl
      601 manrpakykd animspgssl pslhvrkqka leaeldaqhl setfdnidnl spkashrskq
      661 rhkqslygdy vfdtnrhddn rsdnfntgnm tvlspylntt vlpsssssrg sldssrsekd
      721 rslerergig lgnyhpaten pgtsskrglq isttaaqiak vmeevsaiht sqedrssgst
      781 telhcvtder nalrrssaah thsntynftk sensnrtcsm pyakleykrs sndslnsvss
      841 sdgygkrgqm kpsiesysed deskfcsygq ypadlahkih sanhmddndg eldtpinysl
      901 kysdeqlnsg rqspsqnerw arpkhiiede ikqseqrqsr nqsttypvyt estddkhlkf
      961 qphfgqqecv spyrsrgang setnrvgsnh ginqnvsqsl cqeddyeddk ptnyseryse
     1021 eeqheeeerp tnysikynee krhvdqpidy slkyatdips sqkqsfsfsk sssgqsskte
     1081 hmssssents tpssnakrqn qlhpssaqsr sgqpqkaatc kvssinqeti qtycvedtpi
     1141 cfsrcsslss lssaedeigc nqttqeadsa ntlqiaeike kigtrsaedp vsevpavsqh
     1201 prtkssrlqg sslssesarh kavefssgak spsksgaqtp ksppehyvqe tplmfsrcts
     1261 vssldsfesr siassvqsep csgmvsgiis psdlpdspgq tmppsrsktp ppppqtaqtk
     1321 revpknkapt aekresgpkq aavnaavqrv qvlpdadtll hfatestpdg fscssslsal
     1381 sldepfiqkd velrimppvq endngnetes eqpkesnenq ekeaektids ekdllddsdd
     1441 ddieileeci isamptkssr kakkpaqtas klpppvarkp sqlpvykllp sqnrlqpqkh
     1501 vsftpgddmp rvycvegtpi nfstatslsd ltiesppnel aagegvrgga qsgefekrdt
     1561 iptegrstde aqggktssvt ipelddnkae egdilaecin sampkgkshk pfrvkkimdq
     1621 vqqasasssa pnknqldgkk kkptspvkpi pqnteyrtrv rknadsknnl naervfsdnk
     1681 dskkqnlknn skvfndklpn nedrvrgsfa fdsphhytpi egtpycfsrn dslssldfdd
     1741 ddvdlsreka elrkakenke seakvtshte ltsnqqsank tqaiakqpin rgqpkpilqk
     1801 qstfpqsskd ipdrgaatde klqnfaient pvcfshnssl sslsdidqen nnkenepike
     1861 teppdsqgep skpqasgyap ksfhvedtpv cfsrnsslss lsidseddll qecissampk
     1921 kkkpsrlkgd nekhsprnmg gilgedltld lkdiqrpdse hglspdsenf dwkaiqegan
     1981 sivsslhqaa aaaclsrqas sdsdsilslk sgislgspfh ltpdqeekpf tsnkgprilk
     2041 pgekstletk kieseskgik ggkkvyksli tgkvrsnsei sgqmkqplqa nmpsisrgrt
     2101 mihipgvrns ssstspvskk gpplktpask spsegqtatt sprgakpsvk selspvarqt
     2161 sqiggsskap srsgsrdstp srpaqqplsr piqspgrnsi spgrngispp nklsqlprts
     2221 spstastkss gsgkmsytsp grqmsqqnlt kqtglsknas siprsesask glnqmnngng
     2281 ankkvelsrm sstkssgses drserpvlvr qstfikeaps ptlrrklees asfeslspss
     2341 rpasptrsqa qtpvlspslp dmslsthssv qaggwrklpp nlsptieynd grpakrhdia
     2401 rshsespsrl pinrsgtwkr ehskhssslp rvstwrrtgs sssilsasse ssekaksede
     2461 khvnsisgtk qskenqvsak gtwrkikene fsptnstsqt vssgatngae sktliyqmap
     2521 avsktedvwv riedcpinnp rsgrsptgnt ppvidsvsek anpnikdskd nqakqnvgng
     2581 svpmrtvgle nrlnsfiqvd apdqkgteik pgqnnpvpvs etnessiver tpfssssssk
     2641 hsspsgtvaa rvtpfnynps prkssadsts arpsqiptpv nnntkkrdsk tdstessgtq
     2701 spkrhsgsyl vtsv
//
LOCUS       NP_001393521            1164 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 1 [Homo sapiens].
ACCESSION   NP_001393521 XP_005272268
VERSION     NP_001393521.1
DBSOURCE    REFSEQ: accession NM_001406592.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1164)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1164)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1164)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1164)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1164)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1164)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1164)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            On May 18, 2022 this sequence version replaced XP_005272268.1.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1952044.1,
                                           SRR18074967.769687.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1164
                     /product="hamartin isoform 1"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=129636
     Region          7..719
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          403..787
                     /region_name="Mediates interaction with WDR45B.
                     /evidence=ECO:0000269|PubMed:28561066"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Region          439..571
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <708..>960
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1006..1085
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1131..1164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1164
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406592.1:189..3683"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS6956.1"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt aggkgtplgt patspppapl chsddyvhis lpqatvtppr
      421 keermdsarp clhrqhhlln drgseeppgs kgsvtlsdlp gflgdlasee dsiekdkeea
      481 aisrelseit taeaepvvpr ggfdspfyrd slpgsqrkth saasssqgas vnpeplhssl
      541 dklgpdtpkq aftpidlpcg sadespagdr ecqtsletsi ftpspckipp ptrvgfgsgq
      601 pppydhlfev alpktahhfv irkteellkk akgnteedgv pstspmevld rliqqgadah
      661 skelnklplp sksvdwthfg gsppsdeirt lrdqllllhn qllyerfkrq qhalrnrrll
      721 rkvikaaale ehnaamkdql klqekdiqmw kvslqkeqar ynqlqeqrdt mvtklhsqir
      781 qlqhdreefy nqsqelqtkl edcrnmiael rielkkannk vchtelllsq vsqklsnses
      841 vqqqmeflnr qllvlgevne lyleqlqnkh sdttkevemm kaayrkelek nrshvlqqtq
      901 rldtsqkril eleshlakkd hllleqkkyl edvklqargq lqaaesryea qkritqvfel
      961 eildlygrle kdgllkklee ekaeaaeaae erldccndgc sdsmvghnee asghngetkt
     1021 prpssargss gsrggggsss ssselstpek pphqragpfs srwettmgea sasipttvgs
     1081 lpssksflgm karelfrnks esqcdedgmt sslseslkte lgkdlgveak iplnldgphp
     1141 spptpdsvgq lhimdyneth hehs
//
LOCUS       NP_001424537             342 aa            linear   PRI 21-NOV-2025
DEFINITION  sorting nexin-27 isoform 10 [Homo sapiens].
ACCESSION   NP_001424537 XP_005245568 XP_054194894
VERSION     NP_001424537.1
DBSOURCE    REFSEQ: accession NM_001437608.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Broniarczyk,J., Trejo-Cerro,O., Massimi,P., Kavcic,N., Myers,M.P.
            and Banks,L.
  TITLE     HPV-18 E6 enhances the interaction between EMILIN2 and SNX27 to
            promote WNT signaling
  JOURNAL   J Virol 98 (7), e0073524 (2024)
   PUBMED   38874360
  REMARK    GeneRIF: HPV-18 E6 enhances the interaction between EMILIN2 and
            SNX27 to promote WNT signaling.
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Xi,Y., Gai,Y., Zhang,W., Wang,M., Liu,Q. and Bi,Y.
  TITLE     Circular RNA SNX27 Facilitates Gastric Cancer Progression By
            Sponging miR-638
  JOURNAL   Turk J Gastroenterol 35 (4), 280-287 (2024)
   PUBMED   39128090
  REMARK    GeneRIF: Circular RNA SNX27 Facilitates Gastric Cancer Progression
            By Sponging miR-638.
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Broniarczyk,J.K., Massimi,P., Trejo-Cerro,O., Myers,M.P. and
            Banks,L.
  TITLE     HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in a
            PBM-Dependent Manner and Promotes Increased Cell Proliferation
  JOURNAL   J Virol 96 (22), e0136522 (2022)
   PUBMED   36326272
  REMARK    GeneRIF: HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in
            a PBM-Dependent Manner and Promotes Increased Cell Proliferation.
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 342)
  AUTHORS   MacNeil,A.J., Mansour,M. and Pohajdak,B.
  TITLE     Sorting nexin 27 interacts with the Cytohesin associated
            scaffolding protein (CASP) in lymphocytes
  JOURNAL   Biochem Biophys Res Commun 359 (4), 848-853 (2007)
   PUBMED   17577583
  REMARK    GeneRIF: These results suggest that endosomal SNX27 may recruit
            CASP to orchestrate intracellular trafficking and/or signaling
            complexes.
REFERENCE   7  (residues 1 to 342)
  AUTHORS   Rincon,E., Santos,T., Avila-Flores,A., Albar,J.P., Lalioti,V.,
            Lei,C., Hong,W. and Merida,I.
  TITLE     Proteomics identification of sorting nexin 27 as a diacylglycerol
            kinase zeta-associated protein: new diacylglycerol kinase roles in
            endocytic recycling
  JOURNAL   Mol Cell Proteomics 6 (6), 1073-1087 (2007)
   PUBMED   17351151
  REMARK    GeneRIF: These data support a previously unreported role for
            diacylglycerol kinase zeta in the modulation of membrane
            trafficking, which may also help to define SNX27 function.
REFERENCE   8  (residues 1 to 342)
  AUTHORS   Joubert,L., Hanson,B., Barthet,G., Sebben,M., Claeysen,S., Hong,W.,
            Marin,P., Dumuis,A. and Bockaert,J.
  TITLE     New sorting nexin (SNX27) and NHERF specifically interact with the
            5-HT4a receptor splice variant: roles in receptor targeting
  JOURNAL   J Cell Sci 117 (Pt 22), 5367-5379 (2004)
   PUBMED   15466885
  REMARK    GeneRIF: SNX27a redirects part of the 5-HT4(a)R to early endosomes.
REFERENCE   9  (residues 1 to 342)
  AUTHORS   Worby,C.A. and Dixon,J.E.
  TITLE     Sorting out the cellular functions of sorting nexins
  JOURNAL   Nat Rev Mol Cell Biol 3 (12), 919-931 (2002)
   PUBMED   12461558
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol. 2003 Feb;4(2):156.]
REFERENCE   10 (residues 1 to 342)
  AUTHORS   Teasdale,R.D., Loci,D., Houghton,F., Karlsson,L. and Gleeson,P.A.
  TITLE     A large family of endosome-localized proteins related to sorting
            nexin 1
  JOURNAL   Biochem J 358 (Pt 1), 7-16 (2001)
   PUBMED   11485546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL391335.32 and AL589765.19.
            
            On or before May 5, 2025 this sequence version replaced
            XP_005245568.1, XP_054194894.1.
            
            Summary: This gene encodes a member of the sorting nexin family, a
            diverse group of cytoplasmic and membrane-associated proteins
            involved in endocytosis of plasma membrane receptors and protein
            trafficking through these compartments. All members of this protein
            family contain a phosphoinositide binding domain (PX domain). A
            highly similar protein in mouse is responsible for the specific
            recruitment of an isoform of serotonin 5-hydroxytryptamine 4
            receptor into early endosomes, suggesting the analogous role for
            the human protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.705318.1, BC012184.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2144835
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..342
                     /product="sorting nexin-27 isoform 10"
                     /note="methamphetamine-responsive transcript 1; sorting
                     nexin family member 27"
                     /calculated_mol_wt=40265
     Region          <1..79
                     /region_name="PX_domain"
                     /note="The Phox Homology domain, a phosphoinositide
                     binding module; cl02563"
                     /db_xref="CDD:470617"
     Site            order(10..12,36..37,49)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132796"
     Region          87..179
                     /region_name="FERM_F1_SNX27"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F1 sub-domain, found in sorting nexin protein 27
                     (SNX27); cd01777"
                     /db_xref="CDD:340475"
     Region          239..340
                     /region_name="FERM-like_C_SNX27"
                     /note="Atypical FERM-like domain C-lobe of Sorting nexin
                     27; cd13338"
                     /db_xref="CDD:270146"
     CDS             1..342
                     /gene="SNX27"
                     /gene_synonym="MRT1; MY014"
                     /coded_by="NM_001437608.1:580..1608"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:81609"
                     /db_xref="HGNC:HGNC:20073"
                     /db_xref="MIM:611541"
ORIGIN      
        1 magrqlcskr yrefailhqn lkrefanftf prlpgkwpfs lseqqldarr rgleeylekv
       61 csirvigesd imqeflsesd enyngvsdve lrvalpdgtt vtvrvkknst tdqvyqaiaa
      121 kvgmdsttvn yfalfevish sfvrklapne fphklyiqny tsavpgtclt irkwlfttee
      181 eillndndla vtyffhqavd dvkkgyikae eksyqlqkly eqrkmvmyln mlrtcegyne
      241 iifphcacds rrkghvitai sithfklhac teegqlenqv iafewdemqr wdtdeegmaf
      301 cfeyargekk prwvkiftpy fnymhecfer vfcelkwrke ey
//
LOCUS       NP_001402870             419 aa            linear   PRI 21-NOV-2025
DEFINITION  synaptotagmin-1 isoform 2 [Homo sapiens].
ACCESSION   NP_001402870 XP_005269170
VERSION     NP_001402870.1
DBSOURCE    REFSEQ: accession NM_001415941.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Stephan,G., Haddock,S., Wang,S., Erdjument-Bromage,H., Liu,W.,
            Ravn-Boess,N., Frenster,J.D., Bready,D., Cai,J., Ronnen,R.,
            Sabio-Ortiz,J., Fenyo,D., Neubert,T.A. and Placantonakis,D.G.
  TITLE     Modulation of GPR133 (ADGRD1) signaling by its intracellular
            interaction partner extended synaptotagmin 1
  JOURNAL   Cell Rep 43 (5), 114229 (2024)
   PUBMED   38758649
  REMARK    GeneRIF: Modulation of GPR133 (ADGRD1) signaling by its
            intracellular interaction partner extended synaptotagmin 1.
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Zhang,J., Ren,G., Huang,T., Sang,Y., Zhong,Y. and Yi,Y.
  TITLE     miRNA-363-3p Hinders Proliferation, Migration, Invasion and
            Autophagy of Thyroid Cancer Cells by Controlling SYT1 Transcription
            to affect NF-kappaB
  JOURNAL   Endocr Metab Immune Disord Drug Targets 24 (1), 153-162 (2024)
   PUBMED   37150983
  REMARK    GeneRIF: miRNA-363-3p Hinders Proliferation, Migration, Invasion
            and Autophagy of Thyroid Cancer Cells by Controlling SYT1
            Transcription to affect NF-kappaB.
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Yamada,K., Motohashi,S., Oikawa,T., Tago,N., Koizumi,R., Ono,M.,
            Tachibana,T., Yoshida,A., Yoshida,S., Shimoda,M., Oka,M., Yoneda,Y.
            and Yoshida,K.
  TITLE     Extended-synaptotagmin 1 engages in unconventional protein
            secretion mediated via SEC22B+ vesicle pathway in liver cancer
  JOURNAL   Proc Natl Acad Sci U S A 119 (36), e2202730119 (2022)
   PUBMED   36044553
  REMARK    GeneRIF: Extended-synaptotagmin 1 engages in unconventional protein
            secretion mediated via SEC22B(+) vesicle pathway in liver cancer.
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Thibord,F., Chan,M.V., Chen,M.H. and Johnson,A.D.
  TITLE     A year of COVID-19 GWAS results from the GRASP portal reveals
            potential genetic risk factors
  JOURNAL   HGG Adv 3 (2), 100095 (2022)
   PUBMED   35224516
REFERENCE   6  (residues 1 to 419)
  AUTHORS   McMahon,H.T., Missler,M., Li,C. and Sudhof,T.C.
  TITLE     Complexins: cytosolic proteins that regulate SNAP receptor function
  JOURNAL   Cell 83 (1), 111-119 (1995)
   PUBMED   7553862
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Chowdhury,D., Travis,G.H., Sutcliffe,J.G. and Burton,F.H.
  TITLE     Synaptotagmin I and 1B4 are identical: implications for
            synaptotagmin distribution in the primate brain
  JOURNAL   Neurosci Lett 190 (1), 9-12 (1995)
   PUBMED   7624059
REFERENCE   8  (residues 1 to 419)
  AUTHORS   Mochly-Rosen,D., Miller,K.G., Scheller,R.H., Khaner,H., Lopez,J.
            and Smith,B.L.
  TITLE     p65 fragments, homologous to the C2 region of protein kinase C,
            bind to the intracellular receptors for protein kinase C
  JOURNAL   Biochemistry 31 (35), 8120-8124 (1992)
   PUBMED   1326322
REFERENCE   9  (residues 1 to 419)
  AUTHORS   Perin,M.S., Johnston,P.A., Ozcelik,T., Jahn,R., Francke,U. and
            Sudhof,T.C.
  TITLE     Structural and functional conservation of synaptotagmin (p65) in
            Drosophila and humans
  JOURNAL   J Biol Chem 266 (1), 615-622 (1991)
   PUBMED   1840599
REFERENCE   10 (residues 1 to 419)
  AUTHORS   Blaustein,R.O., Germann,W.J., Finkelstein,A. and DasGupta,B.R.
  TITLE     The N-terminal half of the heavy chain of botulinum type A
            neurotoxin forms channels in planar phospholipid bilayers
  JOURNAL   FEBS Lett 226 (1), 115-120 (1987)
   PUBMED   2446925
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073606.19, AC073616.17,
            AC073572.19, AC078917.14 and AC027288.26.
            
            On Jan 5, 2023 this sequence version replaced XP_005269170.1.
            
            Summary: This gene encodes a member of the synaptotagmin protein
            family. The synaptotagmins are integral membrane proteins of
            synaptic vesicles that serve as calcium sensors in the process of
            vesicular trafficking and exocytosis. The encoded protein
            participates in triggering neurotransmitter release at the synapse
            in response to calcium binding. Mutations in this gene are
            associated with Baker-Gordon syndrome. [provided by RefSeq, Jan
            2023].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.80687.1,
                                           SRR1803615.65143.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.2"
     Protein         1..419
                     /product="synaptotagmin-1 isoform 2"
                     /note="sytI; synaptotagmin I"
                     /calculated_mol_wt=47130
     Region          6..113
                     /region_name="Syt1_N"
                     /note="N-terminal domain of synaptotagmin-1 (Syt1) and
                     similar proteins; cd21963"
                     /db_xref="CDD:409248"
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            order(40,43..44,46..48,50..51)
                     /site_type="other"
                     /note="Botolinum neurotoxin B binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409248"
     Site            58..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Region          133..379
                     /region_name="Phospholipid binding. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Region          140..262
                     /region_name="C2A_Synaptotagmin-1-5-6-9-10"
                     /note="C2A domain first repeat present in Synaptotagmins
                     1, 5, 6, 9, and 10; cd08385"
                     /db_xref="CDD:176031"
     Site            order(170,176,228,230,236)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176031"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P46096; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46096; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Region          271..406
                     /region_name="C2B_Synaptotagmin-1"
                     /note="C2 domain second repeat present in Synaptotagmin 1;
                     cd08402"
                     /db_xref="CDD:176047"
     Site            order(301,307,361,363,369)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176047"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21707; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21707; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     CDS             1..419
                     /gene="SYT1"
                     /gene_synonym="BAGOS; P65; SVP65; SYT"
                     /coded_by="NM_001415941.1:553..1812"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="GeneID:6857"
                     /db_xref="HGNC:HGNC:11509"
                     /db_xref="MIM:185605"
ORIGIN      
        1 mvseshheal aappvttvat vlpsnatepa spgegkedaf sklkekfmne lhkiplppwa
       61 liaiaivavl lvltccfcic kkclfkkknk kkgkekggkn ainmkdvkdl gktmkdqddd
      121 aetgltdgee keepkeeekl gklqysldyd fqnnqllvgi iqaaelpald mggtsdpyvk
      181 vfllpdkkkk fetkvhrktl npvfneqftf kvpyselggk tlvmavydfd rfskhdiige
      241 fkvpmntvdf ghvteewrdl qsaekeeqek lgdicfslry vptagkltvv ileaknlkkm
      301 dvgglsdpyv kihlmqngkr lkkkkttikk ntlnpyynes fsfevpfeqi qkvqvvvtvl
      361 dydkigknda igkvfvgyns tgaelrhwsd mlanprrpia qwhtlqveee vdamlavkk
//
LOCUS       NP_001393928             456 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform M [Homo sapiens].
ACCESSION   NP_001393928
VERSION     NP_001393928.1
DBSOURCE    REFSEQ: accession NM_001406999.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 456)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 456)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 456)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1590600.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146982, SAMEA2159931
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..456
                     /product="lamin isoform M"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=49912
     Region          <104..178
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          226..333
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     CDS             1..456
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406999.1:1053..2423"
                     /note="isoform M is encoded by transcript variant 24"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 mrpdwwrltm gssvslragw rmrcrncgps mrtrwssirr swrrlilpsw tmpgsllrgt
       61 atwwglptrs cssrasasta slpssassrs ralgsspnpp tplqlaakea klrdledsla
      121 rerdtsrrll aekeremaem rarmqqqlde yqelldikla ldmeihayrk llegeeerlr
      181 lspsptsqrs rgrasshssq tqgggsvtkk rklestesrs sfsqhartsg rvaveevdee
      241 gkfvrlrnks nedqsmgnwq ikrqngddpl ltyrfppkft lkagqvvtiw aagagathsp
      301 ptdlvwkaqn twgcgnslrt alinstgeev amrklvrsvt vveddededg ddllhhhhgs
      361 hcsssgdpae ynlrsrtvlc gtcgqpadka sasgsgaqvg gpissgssas svtvtrsyrs
      421 vggsgggsfg dnlvtrsyll gnssprtqsp qncsim
//
LOCUS       NP_001400924             337 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, NMDA 2B isoform b precursor [Homo
            sapiens].
ACCESSION   NP_001400924
VERSION     NP_001400924.1
DBSOURCE    REFSEQ: accession NM_001413995.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Korinek,M., Candelas Serra,M., Abdel Rahman,F., Dobrovolski,M.,
            Kuchtiak,V., Abramova,V., Fili,K., Tomovic,E., Hrcka Krausova,B.,
            Krusek,J., Cerny,J., Vyklicky,L., Balik,A. and Smejkalova,T.
  TITLE     Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B genes:
            Insights into NMDA Receptor Structure, Function, and
            Pathophysiology
  JOURNAL   Physiol Res 73 (Suppl 1), S413-S434 (2024)
   PUBMED   38836461
  REMARK    GeneRIF: Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B
            genes: Insights into NMDA Receptor Structure, Function, and
            Pathophysiology.
            Review article
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Raich,I., Lillo,J., Rebassa,J.B., Capo,T., Cordomi,A.,
            Reyes-Resina,I., Pallas,M. and Navarro,G.
  TITLE     Dual Role of NMDAR Containing NR2A and NR2B Subunits in Alzheimer's
            Disease
  JOURNAL   Int J Mol Sci 25 (9), 4757 (2024)
   PUBMED   38731978
  REMARK    GeneRIF: Dual Role of NMDAR Containing NR2A and NR2B Subunits in
            Alzheimer's Disease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Iacobucci,G.J. and Popescu,G.K.
  TITLE     NMDA receptors: linking physiological output to biophysical
            operation
  JOURNAL   Nat Rev Neurosci 18 (4), 236-249 (2017)
   PUBMED   28303017
  REMARK    Review article
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Hu,C., Chen,W., Myers,S.J., Yuan,H. and Traynelis,S.F.
  TITLE     Human GRIN2B variants in neurodevelopmental disorders
  JOURNAL   J Pharmacol Sci 132 (2), 115-121 (2016)
   PUBMED   27818011
  REMARK    GeneRIF: In this review, mutations in GRIN2B were described as
            distributed throughout the entire gene in patients with
            neuropsychiatric and developmental disorders.
            Review article
            Erratum:[J Pharmacol Sci. 2017 Apr;133(4):280. doi:
            10.1016/j.jphs.2017.04.001. PMID: 28434657]
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Hess,S.D., Daggett,L.P., Crona,J., Deal,C., Lu,C.C., Urrutia,A.,
            Chavez-Noriega,L., Ellis,S.B., Johnson,E.C. and Velicelebi,G.
  TITLE     Cloning and functional characterization of human heteromeric
            N-methyl-D-aspartate receptors
  JOURNAL   J Pharmacol Exp Ther 278 (2), 808-816 (1996)
   PUBMED   8768735
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Kornau,H.C., Schenker,L.T., Kennedy,M.B. and Seeburg,P.H.
  TITLE     Domain interaction between NMDA receptor subunits and the
            postsynaptic density protein PSD-95
  JOURNAL   Science 269 (5231), 1737-1740 (1995)
   PUBMED   7569905
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Magnuson,D.S., Knudsen,B.E., Geiger,J.D., Brownstone,R.M. and
            Nath,A.
  TITLE     Human immunodeficiency virus type 1 tat activates
            non-N-methyl-D-aspartate excitatory amino acid receptors and causes
            neurotoxicity
  JOURNAL   Ann Neurol 37 (3), 373-380 (1995)
   PUBMED   7695237
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Mandich,P., Schito,A.M., Bellone,E., Antonacci,R., Finelli,P.,
            Rocchi,M. and Ajmar,F.
  TITLE     Mapping of the human NMDAR2B receptor subunit gene (GRIN2B) to
            chromosome 12p12
  JOURNAL   Genomics 22 (1), 216-218 (1994)
   PUBMED   7959773
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Platzer,K. and Lemke,J.R.
  TITLE     GRIN2B-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29851452
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Monyer,H., Sprengel,R., Schoepfer,R., Herb,A., Higuchi,M.,
            Lomeli,H., Burnashev,N., Sakmann,B. and Seeburg,P.H.
  TITLE     Heteromeric NMDA receptors: molecular and functional distinction of
            subtypes
  JOURNAL   Science 256 (5060), 1217-1221 (1992)
   PUBMED   1350383
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007916.10, AC007784.7 and
            AC007397.21.
            
            Summary: This gene encodes a member of the N-methyl-D-aspartate
            (NMDA) receptor family within the ionotropic glutamate receptor
            superfamily. The encoded protein is a subunit of the NMDA receptor
            ion channel which acts as an agonist binding site for glutamate.
            The NMDA receptors mediate a slow calcium-permeable component of
            excitatory synaptic transmission in the central nervous system. The
            NMDA receptors are heterotetramers of seven genetically encoded,
            differentially expressed subunits including NR1 (GRIN1), NR2
            (GRIN2A, GRIN2B, GRIN2C, or GRIN2D) and NR3 (GRIN3A or GRIN3B). The
            early expression of this gene in development suggests a role in
            brain development, circuit formation, synaptic plasticity, and
            cellular migration and differentiation. Naturally occurring
            mutations within this gene are associated with neurodevelopmental
            disorders including autism spectrum disorder, attention deficit
            hyperactivity disorder, epilepsy, and schizophrenia. [provided by
            RefSeq, Aug 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410571.158703.1, DR000599.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.1"
     Protein         1..337
                     /product="glutamate receptor ionotropic, NMDA 2B isoform b
                     precursor"
                     /note="glutamate [NMDA] receptor subunit epsilon-2;
                     glutamate receptor subunit epsilon-2; N-methyl-D-aspartate
                     receptor subunit 3; N-methyl D-aspartate receptor subtype
                     2B; GluN2B(alt_5'UTR); glutamate receptor ionotropic, NMDA
                     2B; glutamate receptor, ionotropic, N-methyl D-aspartate
                     2B"
                     /calculated_mol_wt=34767
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2820
     Region          33..337
                     /region_name="PBP1_iGluR_NMDA_NR2"
                     /note="N-terminal leucine-isoleucine-valine-binding
                     protein (LIVBP)-like domain of the NR2 subunit of NMDA
                     receptor family; cd06378"
                     /db_xref="CDD:380601"
     Site            order(33,77..79,114,135,175,177,192,207..208,311..312)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:380601"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:26912815,
                     ECO:0007744|PDB:5EWJ, ECO:0007744|PDB:5EWL,
                     ECO:0007744|PDB:5EWM; propagated from UniProtKB/Swiss-Prot
                     (Q13224.3)"
     Site            order(75..80,82..83,118..119,175,179,206,208,311..317,
                     321..323,334)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:380601"
     CDS             1..337
                     /gene="GRIN2B"
                     /gene_synonym="DEE27; EIEE27; GluN2B; hNR3; MRD6; NMDAR2B;
                     NR2B; NR3"
                     /coded_by="NM_001413995.1:937..1950"
                     /note="isoform b precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:2904"
                     /db_xref="HGNC:HGNC:4586"
                     /db_xref="MIM:138252"
ORIGIN      
        1 mkpraeccsp kfwlvlavla vsgsrarsqk sppsigiavi lvgtsdevai kdahekddfh
       61 hlsvvprvel vamnetdpks iitricdlms drkiqgvvfa ddtdqeaiaq ildfisaqtl
      121 tpilgihggs smimadkdes smffqfgpsi eqqasvmlni meeydwyifs ivttyfpgyq
      181 dfvnkirsti ensfvgwele evllldmsld dgdskiqnql kklqspiill yctkeeatyi
      241 fevansvglt gygytwivps lvagdtdtvp aefptglisv sydewdyglp arvrdgiaii
      301 ttaasdmlse hsfipepkss cynthekriy qsnmlnr
//
LOCUS       NP_001397687             563 aa            linear   PRI 21-NOV-2025
DEFINITION  SH3 domain-containing kinase-binding protein 1 isoform m [Homo
            sapiens].
ACCESSION   NP_001397687 XP_047298005
VERSION     NP_001397687.1
DBSOURCE    REFSEQ: accession NM_001410758.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 563)
  AUTHORS   Ahmed,S.F., Buetow,L., Gabrielsen,M., Lilla,S., Sibbet,G.J.,
            Sumpton,D., Zanivan,S., Hedley,A., Clark,W. and Huang,D.T.
  TITLE     E3 ligase-inactivation rewires CBL interactome to elicit
            oncogenesis by hijacking RTK-CBL-CIN85 axis
  JOURNAL   Oncogene 40 (12), 2149-2164 (2021)
   PUBMED   33627783
  REMARK    GeneRIF: E3 ligase-inactivation rewires CBL interactome to elicit
            oncogenesis by hijacking RTK-CBL-CIN85 axis.
REFERENCE   5  (residues 1 to 563)
  AUTHORS   Soubeyran,P., Kowanetz,K., Szymkiewicz,I., Langdon,W.Y. and
            Dikic,I.
  TITLE     Cbl-CIN85-endophilin complex mediates ligand-induced downregulation
            of EGF receptors
  JOURNAL   Nature 416 (6877), 183-187 (2002)
   PUBMED   11894095
  REMARK    GeneRIF: Cbl-CIN85-endophilin complex mediates ligand-induced
            downregulation of EGF receptors
            Erratum:[Nature 2002 May 2;417(6884):102]
REFERENCE   6  (residues 1 to 563)
  AUTHORS   Narita,T., Amano,F., Yoshizaki,K., Nishimoto,N., Nishimura,T.,
            Tajima,T., Namiki,H. and Taniyama,T.
  TITLE     Assignment of SH3KBP1 to human chromosome band Xp22.1-->p21.3 by in
            situ hybridization
  JOURNAL   Cytogenet Cell Genet 93 (1-2), 133-134 (2001)
   PUBMED   11474197
REFERENCE   7  (residues 1 to 563)
  AUTHORS   Watanabe,S., Take,H., Takeda,K., Yu,Z.X., Iwata,N. and Kajigaya,S.
  TITLE     Characterization of the CIN85 adaptor protein and identification of
            components involved in CIN85 complexes
  JOURNAL   Biochem Biophys Res Commun 278 (1), 167-174 (2000)
   PUBMED   11071869
REFERENCE   8  (residues 1 to 563)
  AUTHORS   Gout,I., Middleton,G., Adu,J., Ninkina,N.N., Drobot,L.B.,
            Filonenko,V., Matsuka,G., Davies,A.M., Waterfield,M. and
            Buchman,V.L.
  TITLE     Negative regulation of PI 3-kinase by Ruk, a novel adaptor protein
  JOURNAL   EMBO J 19 (15), 4015-4025 (2000)
   PUBMED   10921882
REFERENCE   9  (residues 1 to 563)
  AUTHORS   Take,H., Watanabe,S., Takeda,K., Yu,Z.X., Iwata,N. and Kajigaya,S.
  TITLE     Cloning and characterization of a novel adaptor protein, CIN85,
            that interacts with c-Cbl
  JOURNAL   Biochem Biophys Res Commun 268 (2), 321-328 (2000)
   PUBMED   10679202
REFERENCE   10 (residues 1 to 563)
  AUTHORS   Salvatore,P., Hanash,C.R., Kido,Y., Imai,Y. and Accili,D.
  TITLE     Identification of sirm, a novel insulin-regulated SH3 binding
            protein that associates with Grb-2 and FYN
  JOURNAL   J Biol Chem 273 (12), 6989-6997 (1998)
   PUBMED   9507006
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL732325.6, AL732327.6 and
            AL732423.12.
            
            On Aug 15, 2022 this sequence version replaced XP_047298005.1.
            
            Summary: This gene encodes an adapter protein that contains one or
            more N-terminal Src homology domains, a proline rich region and a
            C-terminal coiled-coil domain. The encoded protein facilitates
            protein-protein interactions and has been implicated in numerous
            cellular processes including apoptosis, cytoskeletal rearrangement,
            cell adhesion and in the regulation of clathrin-dependent
            endocytosis. Alternate splicing results in multiple transcript
            variants encoding distinct isoforms. [provided by RefSeq, Jul
            2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.241972.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.12"
     Protein         1..563
                     /product="SH3 domain-containing kinase-binding protein 1
                     isoform m"
                     /note="Src family kinase-binding protein 1; src-related
                     kinase binding protein-1; CD2-binding protein 3;
                     migration-inducing gene 18; c-Cbl-interacting protein;
                     cbl-interacting protein of 85 kDa; SH3-domain kinase
                     binding protein 1; human Src family kinase-binding protein
                     1"
                     /calculated_mol_wt=61496
     Region          43..95
                     /region_name="SH3_CIN85_2"
                     /note="Second Src Homology 3 domain (SH3B) of
                     Cbl-interacting protein of 85 kDa; cd12055"
                     /db_xref="CDD:212988"
     Site            order(47..53,57,61..62,74..76,86..87,89,91..92)
                     /site_type="other"
                     /note="putative ubiquitin interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:212988"
     Site            order(48,50,53,57,74..76,87,89,91..92)
                     /site_type="other"
                     /note="putative peptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:212988"
     Region          212..267
                     /region_name="SH3_CIN85_3"
                     /note="Third Src Homology 3 domain (SH3C) of
                     Cbl-interacting protein of 85 kDa; cd12057"
                     /db_xref="CDD:212990"
     Site            order(216..223,225..226,230..231,244..247,257..258,260,
                     262..263,265)
                     /site_type="other"
                     /note="ubiquitin interaction site [polypeptide binding]"
                     /db_xref="CDD:212990"
     Site            order(217,219,222,226,245..247,258,260,262..263)
                     /site_type="other"
                     /note="putative peptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:212990"
     CDS             1..563
                     /gene="SH3KBP1"
                     /gene_synonym="AGMX2; CD2BP3; CIN85; GIG10; HSB-1; HSB1;
                     IMD61; MIG18"
                     /coded_by="NM_001410758.1:73..1764"
                     /note="isoform m is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS94566.1"
                     /db_xref="GeneID:30011"
                     /db_xref="HGNC:HGNC:13867"
                     /db_xref="MIM:300374"
ORIGIN      
        1 mkkdpltnka pekplhevps gnsllsseti lrtnkrgerr rrrcqvafsy lpqnddelel
       61 kvgdiievvg eveegwwegv lngktgmfps nfikelsges delgisqdeq lsksslrett
      121 gsesdggdss stksegangt vataaiqpkk vkgvgfgdif kdkpiklrpr sievendflp
      181 vektigkklp attatpdssk temdsrtksk dyckvifpye aqnddeltik egdivtlink
      241 dcidvgwweg elngrrgvfp dnfvkllppd fekegnrpkk ppppsapvik qgagtterkh
      301 eikkipperp emlpnrteek erperepkld lqkpsvpaip pkkprppktn slsrpgalpp
      361 rrperpvgpl thtrgdspki dlagsslsgi ldkdlsdrsn didlegfdsv vssteklshp
      421 ttsrpkatgr rppsqsltsv sdnkaslppk pgtmaagggg paplssaaps plssslgtag
      481 hranspslfg tegkpkmepa assqaaveel rtqvrelrsi ietmkdqqkr eikqllseld
      541 eekkirlrlq mevndikkal qsk
//
LOCUS       NP_001400345             282 aa            linear   PRI 21-NOV-2025
DEFINITION  alpha-tocopherol transfer protein isoform 4 [Homo sapiens].
ACCESSION   NP_001400345
VERSION     NP_001400345.1
DBSOURCE    REFSEQ: accession NM_001413416.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Jeridi,C., Rachdi,A., Nabli,F., Saied,Z., Zouari,R., Ben
            Mohamed,D., Ben Said,M., Masmoudi,S., Ben Sassi,S. and Amouri,R.
  TITLE     Genetic heterogeneity within a consanguineous family involving TTPA
            and SETX genes
  JOURNAL   J Neurogenet 37 (4), 124-130 (2023)
   PUBMED   38109176
  REMARK    GeneRIF: Genetic heterogeneity within a consanguineous family
            involving TTPA and SETX genes.
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Ulatowski,L., Ghelfi,M., West,R., Atkinson,J., Finno,C.J. and
            Manor,D.
  TITLE     The tocopherol transfer protein mediates vitamin E trafficking
            between cerebellar astrocytes and neurons
  JOURNAL   J Biol Chem 298 (3), 101712 (2022)
   PUBMED   35150738
  REMARK    GeneRIF: The tocopherol transfer protein mediates vitamin E
            trafficking between cerebellar astrocytes and neurons.
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Arai,H. and Kono,N.
  TITLE     alpha-Tocopherol transfer protein (alpha-TTP)
  JOURNAL   Free Radic Biol Med 176, 162-175 (2021)
   PUBMED   34563650
  REMARK    GeneRIF: alpha-Tocopherol transfer protein (alpha-TTP).
            Review article
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Gotoda,T., Arita,M., Arai,H., Inoue,K., Yokota,T., Fukuo,Y.,
            Yazaki,Y. and Yamada,N.
  TITLE     Adult-onset spinocerebellar dysfunction caused by a mutation in the
            gene for the alpha-tocopherol-transfer protein
  JOURNAL   N Engl J Med 333 (20), 1313-1318 (1995)
   PUBMED   7566022
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Arita,M., Sato,Y., Miyata,A., Tanabe,T., Takahashi,E., Kayden,H.J.,
            Arai,H. and Inoue,K.
  TITLE     Human alpha-tocopherol transfer protein: cDNA cloning, expression
            and chromosomal localization
  JOURNAL   Biochem J 306 (Pt 2) (Pt 2), 437-443 (1995)
   PUBMED   7887897
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Ouahchi,K., Arita,M., Kayden,H., Hentati,F., Ben Hamida,M.,
            Sokol,R., Arai,H., Inoue,K., Mandel,J.L. and Koenig,M.
  TITLE     Ataxia with isolated vitamin E deficiency is caused by mutations in
            the alpha-tocopherol transfer protein
  JOURNAL   Nat Genet 9 (2), 141-145 (1995)
   PUBMED   7719340
REFERENCE   8  (residues 1 to 282)
  AUTHORS   Ben Hamida,C., Doerflinger,N., Belal,S., Linder,C., Reutenauer,L.,
            Dib,C., Gyapay,G., Vignal,A., Le Paslier,D., Cohen,D. et al.
  TITLE     Localization of Friedreich ataxia phenotype with selective vitamin
            E deficiency to chromosome 8q by homozygosity mapping
  JOURNAL   Nat Genet 5 (2), 195-200 (1993)
   PUBMED   8252047
REFERENCE   9  (residues 1 to 282)
  AUTHORS   Schuelke,M.
  TITLE     Ataxia with Vitamin E Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301419
REFERENCE   10 (residues 1 to 282)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC120042.3.
            
            Summary: This gene encodes a soluble protein that binds
            alpha-trocopherol, a form of vitamin E, with high selectivity and
            affinity. This protein plays an important role in regulating
            vitamin E levels in the body by transporting vitamin E between
            membrane vesicles and facilitating the secretion of vitamin E from
            hepatocytes to circulating lipoproteins. Mutations in this gene
            cause hereditary vitamin E deficiency (ataxia with vitamin E
            deficiency, AVED) and retinitis pigmentosa. [provided by RefSeq,
            Nov 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.163149.1,
                                           SRR6380202.13266.9 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.3"
     Protein         1..282
                     /product="alpha-tocopherol transfer protein isoform 4"
                     /note="tocopherol (alpha) transfer protein (ataxia
                     (Friedreich-like) with vitamin E deficiency); alpha-TTP"
                     /calculated_mol_wt=31605
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49638.1)"
     Region          <40..73
                     /region_name="CRAL_TRIO_N"
                     /note="CRAL/TRIO, N-terminal domain; smart01100"
                     /db_xref="CDD:215024"
     Region          99..236
                     /region_name="CRAL_TRIO"
                     /note="CRAL/TRIO domain; pfam00650"
                     /db_xref="CDD:459890"
     CDS             1..282
                     /gene="TTPA"
                     /gene_synonym="alphaTTP; ATTP; AVED; TTP1"
                     /coded_by="NM_001413416.1:33..881"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:7274"
                     /db_xref="HGNC:HGNC:12404"
                     /db_xref="MIM:600415"
ORIGIN      
        1 maearsqpsa gpqlnalpdh spllqpglaa lrrrareagv plaplpltds fllrflrard
       61 fdldlawrll knyykwraec peisadlhpr siigllkagy hgvlrsrdpt gskvliyria
      121 hwdpkvftay dvfrvslits elivqevetq rngikaifdl egwqfshafq itpsvakkia
      181 avltdsfplk vrgihlinep vifhavfsmi kpfltekike rtgphfvqwh dlgslqpppp
      241 glkqssclsp psiwdyspap prpanfciff vpamlprlvl ns
//
LOCUS       NP_001427526             390 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform l [Homo sapiens].
ACCESSION   NP_001427526 XP_047283757 XP_054226335
VERSION     NP_001427526.1
DBSOURCE    REFSEQ: accession NM_001440597.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 390)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 390)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 390)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2.
            
            On or before May 22, 2025 this sequence version replaced
            XP_047283757.1, XP_054226335.1.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.4156446.1,
                                           SRR14038192.2693469.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..390
                     /product="polycomb protein EED isoform l"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=44472
     Region          1..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q921E6; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            66
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918; N6-methyllysine,
                     alternate. /evidence=ECO:0000269|PubMed:20974918;
                     propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Region          <83..269
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          96..140
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          148..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          149..303
                     /region_name="Required for interaction with the matrix
                     protein MA of HIV-1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Region          193..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            197
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918; N6-methyllysine,
                     alternate. /evidence=ECO:0000269|PubMed:20974918;
                     propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Region          240..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            268
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918; N6-methyllysine,
                     alternate. /evidence=ECO:0000269|PubMed:20974918;
                     propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Site            284
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918; N6-methyllysine,
                     alternate. /evidence=ECO:0000269|PubMed:20974918;
                     propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Region          309..357
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..390
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001440597.1:478..1650"
                     /note="isoform l is encoded by transcript variant 12"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdendd avsiesgtnt erpdtptntp
       61 napgrkswgk gkwkskkcky sfkcvnslke dhnqplfgvq fnwhskegdp lvfatvgsnr
      121 vtlyechsqg eirllqsyvd adadenfytc awtydsntsh pllavagsrg iiriinpitm
      181 qcikhyvghg nainelkfhp rdpnlllsvs kdhalrlwni qtdtlvaifg gveghrdevl
      241 sadydllgek imscgmdhsl klwrinskrm mnaikesydy npnktnrpfi sqkihfpdfs
      301 trdihrnyvd cvrwlgdlil skscenaivc wkpgkmeddi dkikpsesnv tilgrfdysq
      361 cdiwymrfsm dfwqkeyktq rnsqehrgwn
//
LOCUS       NP_001394261             284 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 32 [Homo sapiens].
ACCESSION   NP_001394261 XP_047288958
VERSION     NP_001394261.1
DBSOURCE    REFSEQ: accession NM_001407332.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            On May 31, 2022 this sequence version replaced XP_047288958.1.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY640414.1, DRR138528.627473.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..284
                     /product="tropomyosin alpha-1 chain isoform 32"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=32536
     Region          48..282
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..284
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407332.1:84..938"
                     /note="isoform 32 is encoded by transcript variant 32"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle ediaakekll rvsederdrv
       61 leelhkaeds llaaeeaaak aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegkc aeleeelktv tnnlksleaq aekysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledel yaqklkykai seeldhalnd mtsm
//
LOCUS       NP_001400680             817 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform m [Homo sapiens].
ACCESSION   NP_001400680
VERSION     NP_001400680.1
DBSOURCE    REFSEQ: accession NM_001413751.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 817)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 817)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 817)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 817)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 817)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 817)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1965009.1,
                                           SRR18074969.3203129.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..817
                     /product="polyhomeotic-like protein 1 isoform m"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=86571
     Region          641..748
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          748..816
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(766..767,801..802,805..806,809)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(777..781,783..784,787..788,792,797)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..817
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413751.1:157..2610"
                     /note="isoform m is encoded by transcript variant 15"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq asinlattsa aqlisrsqsv
      121 sspsattltq svllgnttsp plnqsqaqmy lrvnrtlgrn vplasqlilm pngavaavqq
      181 evpsaqspgv hadadqvqnl avrnqqasaq gpqmqgstqk aippgaspvs slsqassqal
      241 avaqassgat nqslnlsqag ggsgnsipgs mgpggggqah gglgqlpssg mgggscprkg
      301 tgvvqplpaa qtvtvsqgsq teaesaaakk aeadgsgqqn vgmnltrtat papsqtliss
      361 atytqiqphs liqqqqqihl qqkqvviqqq iaihhqqqfq hrqsqllhta thlqlaqqqq
      421 qqqqqqqqqq qpqattltap qppqgkpqtl avkrkadsee erddvstlgs mlpakaspva
      481 espkvmdeks slgekaesva nvnantpsse lvaltpapsv ppptlamvsr qmgdskppqa
      541 ivkpqilthi iegfviqega epfpvgcsql lkesekplqt glptgltenq sggplgvdsp
      601 saeldkkanl lkceycgkya paeqfrgskr fcsmtcakry nvscshqfrl krkkmkefqe
      661 anyarvrrrg prrsssdiar akiqgkchrg qedssrgsdn ssydealspt spgplsvrag
      721 hgerdlgnpn tapptpelhg inpvflssnp srwsveevye fiaslqgcqe iaeefrsqei
      781 dgqallllke ehlmsamnik lgpalkicak invlket
//
LOCUS       NP_001389611            1357 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform a [Homo sapiens].
ACCESSION   NP_001389611 XP_006720201
VERSION     NP_001389611.1
DBSOURCE    REFSEQ: accession NM_001402682.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1357)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1357)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1357)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1357)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1357)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1357)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1357)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1357)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1357)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1357)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            On Apr 22, 2022 this sequence version replaced XP_006720201.1.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2909739.1,
                                           SRR14038197.2607585.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1357
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1357
                     /product="kinectin isoform a"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=156145
     Site            7..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UP2.1)"
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          48..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Region          103..218
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            172
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Region          316..>532
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Site            435
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Region          448..1270
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            772
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            904
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            1055
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            1084
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            1088
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Region          <1190..>1357
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            1263
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            1313
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            1329
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     CDS             1..1357
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402682.1:303..4376"
                     /note="isoform a is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS41957.1"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqdlkqeika
      841 lkeeignvql ekaqqlsits kvqelqnllk gkeeqmntmk avleekekdl antgkwlqdl
      901 qeeneslkah vqevaqhnlk eassasqfee leivlkeken elkrleamlk eresdlsskt
      961 qllqdvqden klfksqieql kqqnyqqass fppheellkv iserekeisg lwneldslkd
     1021 avehqrkknn dlreknweam ealastekml qdkvnktske rqqqveavel eakevlkklf
     1081 pkvsvpsnls ygewlhgfek kakecmagts gseevkvleh klkeademht llqlecekyk
     1141 svlaetegil qklqrsveqe enkwkvkvde shktikqmqs sftsseqele rlrsenkdie
     1201 nlrrerehle melekaemer styvtevrel kdlltelqkk lddsyseavr qneelnllka
     1261 qlnetltklr teqnerqkva gdlhkaqqsl eliqskivka agdttviens dvspetesse
     1321 ketmsvslnq tvtqlqqllq avnqqltkek ehyqvle
//
LOCUS       NP_001392222             387 aa            linear   PRI 21-NOV-2025
DEFINITION  F-box/LRR-repeat protein 14 isoform 4 [Homo sapiens].
ACCESSION   NP_001392222 XP_016874365
VERSION     NP_001392222.1
DBSOURCE    REFSEQ: accession NM_001405293.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Pitts,S., Liu,H., Ibrahim,A., Garg,A., Felgueira,C.M., Begum,A.,
            Fan,W., Teh,S., Low,J.Y., Ford,B., Schneider,D.A., Hay,R. and
            Laiho,M.
  TITLE     Identification of an E3 ligase that targets the catalytic subunit
            of RNA Polymerase I upon transcription stress
  JOURNAL   J Biol Chem 298 (12), 102690 (2022)
   PUBMED   36372232
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Cui,Y.H., Kang,J.H., Suh,Y., Zhao,Y., Yi,J.M., Bae,I.H., Lee,H.J.,
            Park,D.W., Kim,M.J. and Lee,S.J.
  TITLE     Loss of FBXL14 promotes mesenchymal shift and radioresistance of
            non-small cell lung cancer by TWIST1 stabilization
  JOURNAL   Signal Transduct Target Ther 6 (1), 272 (2021)
   PUBMED   34285182
  REMARK    GeneRIF: Loss of FBXL14 promotes mesenchymal shift and
            radioresistance of non-small cell lung cancer by TWIST1
            stabilization.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Hauri,S., Comoglio,F., Seimiya,M., Gerstung,M., Glatter,T.,
            Hansen,K., Aebersold,R., Paro,R., Gstaiger,M. and Beisel,C.
  TITLE     A High-Density Map for Navigating the Human Polycomb Complexome
  JOURNAL   Cell Rep 17 (2), 583-595 (2016)
   PUBMED   27705803
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Zheng,H., Shen,M., Zha,Y.L., Li,W., Wei,Y., Blanco,M.A., Ren,G.,
            Zhou,T., Storz,P., Wang,H.Y. and Kang,Y.
  TITLE     PKD1 phosphorylation-dependent degradation of SNAIL by SCF-FBXO11
            regulates epithelial-mesenchymal transition and metastasis
  JOURNAL   Cancer Cell 26 (3), 358-373 (2014)
   PUBMED   25203322
REFERENCE   8  (residues 1 to 387)
  AUTHORS   Vinas-Castells,R., Beltran,M., Valls,G., Gomez,I., Garcia,J.M.,
            Montserrat-Sentis,B., Baulida,J., Bonilla,F., de Herreros,A.G. and
            Diaz,V.M.
  TITLE     The hypoxia-controlled FBXL14 ubiquitin ligase targets SNAIL1 for
            proteasome degradation
  JOURNAL   J Biol Chem 285 (6), 3794-3805 (2010)
   PUBMED   19955572
  REMARK    GeneRIF: Data show that Twist1 small interfering RNA prevents
            hypoxia-induced Fbxl14 down-regulation and SNAIL1 stabilization.
REFERENCE   9  (residues 1 to 387)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   10 (residues 1 to 387)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005182.2.
            
            On Apr 21, 2022 this sequence version replaced XP_016874365.1.
            
            Summary: Members of the F-box protein family, such as FBXL14, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HY207849.1, SRR9304713.124811.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..387
                     /product="F-box/LRR-repeat protein 14 isoform 4"
                     /note="F-box/LRR-repeat protein 14"
                     /calculated_mol_wt=42145
     Region          2..48
                     /region_name="Required for down-regulation of SNAI1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1E6.1)"
     Region          6..46
                     /region_name="F-box_FBXL14"
                     /note="F-box domain found in F-box/LRR-repeat protein 14
                     (FBXL14) and similar proteins; cd22125"
                     /db_xref="CDD:438897"
     Site            order(8,12,15..16,19..20,24,26..27,31..33,35)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438897"
     Region          90..296
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          92..118
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          119..142
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          144..163
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1E6.1)"
     Region          145..170
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          170..191
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1E6.1)"
     Region          171..203
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          203..225
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1E6.1)"
     Region          204..229
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          228..386
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          229..250
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1E6.1)"
     Region          230..254
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          254..275
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1E6.1)"
     Region          255..280
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          281..306
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          307..331
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          332..357
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          358..382
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..387
                     /gene="FBXL14"
                     /gene_synonym="Fbl14"
                     /coded_by="NM_001405293.1:777..1940"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:144699"
                     /db_xref="HGNC:HGNC:28624"
                     /db_xref="MIM:609081"
ORIGIN      
        1 methisclfp ellamifgyl dvrdkgraaq vctawrdaay hksvwrgvea klhlrranps
       61 lfpslqargi rrvqilslrr slsyviqgma nieslnlsgc ynltdnglgh afvqeigslr
      121 alnlslckqi tdsslgriaq ylkglevlel ggcsnitntg llliawglqr lkslnlrscr
      181 hlsdvgighl agmtrsaaeg clgleqltlq dcqkltdlsl khisrgltgl rllnlsfcgg
      241 isdagllhls hmgslrslnl rscdnisdtg imhlamgslr lsgldvsfcd kvgdqslayi
      301 aqgldglksl slcschisdd ginrmvrqmh glrtlnigqc vritdkglel iaehlsqltg
      361 idlygctrit krgleritql pclkgll
//
LOCUS       NP_001426090             604 aa            linear   PRI 21-NOV-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein Q isoform 11 [Homo
            sapiens].
ACCESSION   NP_001426090 XP_047274038 XP_054210014
VERSION     NP_001426090.1
DBSOURCE    REFSEQ: accession NM_001439161.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Ishtayeh,H., Galves,M., Barnatan,T.T., Berdichevsky,Y.,
            Amer-Sarsour,F., Pasmanik-Chor,M., Braverman,I., Blumen,S.C. and
            Ashkenazi,A.
  TITLE     Oculopharyngeal muscular dystrophy mutations link the RNA-binding
            protein HNRNPQ to autophagosome biogenesis
  JOURNAL   Aging Cell 22 (10), e13949 (2023)
   PUBMED   37559347
  REMARK    GeneRIF: Oculopharyngeal muscular dystrophy mutations link the
            RNA-binding protein HNRNPQ to autophagosome biogenesis.
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Semino,F., Schroter,J., Willemsen,M.H., Bast,T., Biskup,S.,
            Beck-Woedl,S., Brennenstuhl,H., Schaaf,C.P., Kolker,S.,
            Hoffmann,G.F., Haack,T.B. and Syrbe,S.
  TITLE     Further evidence for de novo variants in SYNCRIP as the cause of a
            neurodevelopmental disorder
  JOURNAL   Hum Mutat 42 (9), 1094-1100 (2021)
   PUBMED   34157790
  REMARK    GeneRIF: Further evidence for de novo variants in SYNCRIP as the
            cause of a neurodevelopmental disorder.
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Mourelatos,Z., Abel,L., Yong,J., Kataoka,N. and Dreyfuss,G.
  TITLE     SMN interacts with a novel family of hnRNP and spliceosomal
            proteins
  JOURNAL   EMBO J 20 (19), 5443-5452 (2001)
   PUBMED   11574476
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Lau,P.P., Chang,B.H. and Chan,L.
  TITLE     Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a
            component of apobec-1 editosome
  JOURNAL   Biochem Biophys Res Commun 282 (4), 977-983 (2001)
   PUBMED   11352648
REFERENCE   7  (residues 1 to 604)
  AUTHORS   Blanc,V., Navaratnam,N., Henderson,J.O., Anant,S., Kennedy,S.,
            Jarmuz,A., Scott,J. and Davidson,N.O.
  TITLE     Identification of GRY-RBP as an apolipoprotein B RNA-binding
            protein that interacts with both apobec-1 and apobec-1
            complementation factor to modulate C to U editing
  JOURNAL   J Biol Chem 276 (13), 10272-10283 (2001)
   PUBMED   11134005
REFERENCE   8  (residues 1 to 604)
  AUTHORS   Grosset,C., Chen,C.Y., Xu,N., Sonenberg,N., Jacquemin-Sablon,H. and
            Shyu,A.B.
  TITLE     A mechanism for translationally coupled mRNA turnover: interaction
            between the poly(A) tail and a c-fos RNA coding determinant via a
            protein complex
  JOURNAL   Cell 103 (1), 29-40 (2000)
   PUBMED   11051545
REFERENCE   9  (residues 1 to 604)
  AUTHORS   Mizutani,A., Fukuda,M., Ibata,K., Shiraishi,Y. and Mikoshiba,K.
  TITLE     SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear
            ribonucleoprotein R, interacts with ubiquitous synaptotagmin
            isoforms
  JOURNAL   J Biol Chem 275 (13), 9823-9831 (2000)
   PUBMED   10734137
REFERENCE   10 (residues 1 to 604)
  AUTHORS   Harris,C.E., Boden,R.A. and Astell,C.R.
  TITLE     A novel heterogeneous nuclear ribonucleoprotein-like protein
            interacts with NS1 of the minute virus of mice
  JOURNAL   J Virol 73 (1), 72-80 (1999)
   PUBMED   9847309
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136082.22.
            
            On or before Apr 28, 2025 this sequence version replaced
            XP_047274038.1, XP_054210014.1.
            
            Summary: This gene encodes a member of the cellular heterogeneous
            nuclear ribonucleoprotein (hnRNP) family. hnRNPs are RNA binding
            proteins that complex with heterogeneous nuclear RNA (hnRNA) and
            regulate alternative splicing, polyadenylation, and other aspects
            of mRNA metabolism and transport. The encoded protein plays a role
            in multiple aspects of mRNA maturation and is associated with
            several multiprotein complexes including the apoB RNA
            editing-complex and survival of motor neurons (SMN) complex.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene, and a pseudogene of this
            gene is located on the short arm of chromosome 20. [provided by
            RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2779516.1,
                                           SRR14372080.214178.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.3"
     Protein         1..604
                     /product="heterogeneous nuclear ribonucleoprotein Q
                     isoform 11"
                     /note="NS1-associated protein 1; heterogeneous nuclear
                     ribonucleoprotein Q; glycine- and tyrosine-rich
                     RNA-binding protein"
                     /calculated_mol_wt=67173
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          23..107
                     /region_name="NURR_hnRNPQ"
                     /note="NURR (N-terminal unit for RNA recognition) domain
                     found in heterogeneous nuclear ribonucleoprotein Q
                     (hnRNPQ) and similar proteins; cd21066"
                     /db_xref="CDD:410954"
     Region          103..592
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            221
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            363
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:12601080; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          400..561
                     /region_name="Interaction with APOBEC1"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            444
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          448..559
                     /region_name="8 X 3 AA repeats of R-G-G"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Region          460..488
                     /region_name="3 X 4 AA repeats of Y-Y-G-Y"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            496
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            510
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          518..549
                     /region_name="Interaction with SMN.
                     /evidence=ECO:0000269|PubMed:11574476"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            518
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            526
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            536
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            539
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          564..578
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            587
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     CDS             1..604
                     /gene="SYNCRIP"
                     /gene_synonym="GRY-RBP; GRYRBP; hnRNP-Q; HNRNPQ; HNRPQ1;
                     NSAP1; PP68"
                     /coded_by="NM_001439161.1:134..1948"
                     /note="isoform 11 is encoded by transcript variant 12"
                     /db_xref="GeneID:10492"
                     /db_xref="HGNC:HGNC:16918"
                     /db_xref="MIM:616686"
ORIGIN      
        1 matehvngng teepmdttsa vihsenfqtl ldaglpqkva ekldeiyvag lvahsdlder
       61 aiealkefne dgalavlqqf kdsdlshvqn ksaflcgvmk tyrqrekqgt kvadsskgpd
      121 eakikaller tgytldvttg qrkyggpppd svysgqqpsv gteifvgkip rdlfedelvp
      181 lfekagpiwd lrlmmdpltg lnrgyafvtf ctkeaaqeav klynnheirs gkhigvcisv
      241 annrlfvgsi pksktkeqil eefskvtegl tdvilyhqpd dkkknrgfcf leyedhktaa
      301 qarrrlmsgk vkvwgnvgtv ewadpiedpd pevmakvkvl fvrnlantvt eeilekafsq
      361 fgklervkkl kdyafihfde rdgavkamee mngkdlegen ieivfakppd qkrkerkaqr
      421 qaaknqmydd yyyygpphmp pptrgrgrgg rggygyppdy ygyedyydyy gydyhnyrgg
      481 yedpyygyed fqvgargrgg rgargaapsr grgaapprgr agysqrggpg sargvrgarg
      541 gaqqqrgrgv rgarggrggn vggkrkadgy nqpdskrrqt nnqnwgsqpi aqqplqgkrg
      601 rgrs
//
LOCUS       NP_001424536             355 aa            linear   PRI 21-NOV-2025
DEFINITION  sorting nexin-27 isoform 9 [Homo sapiens].
ACCESSION   NP_001424536 XP_024305806 XP_054194895
VERSION     NP_001424536.1
DBSOURCE    REFSEQ: accession NM_001437607.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Broniarczyk,J., Trejo-Cerro,O., Massimi,P., Kavcic,N., Myers,M.P.
            and Banks,L.
  TITLE     HPV-18 E6 enhances the interaction between EMILIN2 and SNX27 to
            promote WNT signaling
  JOURNAL   J Virol 98 (7), e0073524 (2024)
   PUBMED   38874360
  REMARK    GeneRIF: HPV-18 E6 enhances the interaction between EMILIN2 and
            SNX27 to promote WNT signaling.
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Xi,Y., Gai,Y., Zhang,W., Wang,M., Liu,Q. and Bi,Y.
  TITLE     Circular RNA SNX27 Facilitates Gastric Cancer Progression By
            Sponging miR-638
  JOURNAL   Turk J Gastroenterol 35 (4), 280-287 (2024)
   PUBMED   39128090
  REMARK    GeneRIF: Circular RNA SNX27 Facilitates Gastric Cancer Progression
            By Sponging miR-638.
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Broniarczyk,J.K., Massimi,P., Trejo-Cerro,O., Myers,M.P. and
            Banks,L.
  TITLE     HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in a
            PBM-Dependent Manner and Promotes Increased Cell Proliferation
  JOURNAL   J Virol 96 (22), e0136522 (2022)
   PUBMED   36326272
  REMARK    GeneRIF: HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in
            a PBM-Dependent Manner and Promotes Increased Cell Proliferation.
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 355)
  AUTHORS   MacNeil,A.J., Mansour,M. and Pohajdak,B.
  TITLE     Sorting nexin 27 interacts with the Cytohesin associated
            scaffolding protein (CASP) in lymphocytes
  JOURNAL   Biochem Biophys Res Commun 359 (4), 848-853 (2007)
   PUBMED   17577583
  REMARK    GeneRIF: These results suggest that endosomal SNX27 may recruit
            CASP to orchestrate intracellular trafficking and/or signaling
            complexes.
REFERENCE   7  (residues 1 to 355)
  AUTHORS   Rincon,E., Santos,T., Avila-Flores,A., Albar,J.P., Lalioti,V.,
            Lei,C., Hong,W. and Merida,I.
  TITLE     Proteomics identification of sorting nexin 27 as a diacylglycerol
            kinase zeta-associated protein: new diacylglycerol kinase roles in
            endocytic recycling
  JOURNAL   Mol Cell Proteomics 6 (6), 1073-1087 (2007)
   PUBMED   17351151
  REMARK    GeneRIF: These data support a previously unreported role for
            diacylglycerol kinase zeta in the modulation of membrane
            trafficking, which may also help to define SNX27 function.
REFERENCE   8  (residues 1 to 355)
  AUTHORS   Joubert,L., Hanson,B., Barthet,G., Sebben,M., Claeysen,S., Hong,W.,
            Marin,P., Dumuis,A. and Bockaert,J.
  TITLE     New sorting nexin (SNX27) and NHERF specifically interact with the
            5-HT4a receptor splice variant: roles in receptor targeting
  JOURNAL   J Cell Sci 117 (Pt 22), 5367-5379 (2004)
   PUBMED   15466885
  REMARK    GeneRIF: SNX27a redirects part of the 5-HT4(a)R to early endosomes.
REFERENCE   9  (residues 1 to 355)
  AUTHORS   Worby,C.A. and Dixon,J.E.
  TITLE     Sorting out the cellular functions of sorting nexins
  JOURNAL   Nat Rev Mol Cell Biol 3 (12), 919-931 (2002)
   PUBMED   12461558
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol. 2003 Feb;4(2):156.]
REFERENCE   10 (residues 1 to 355)
  AUTHORS   Teasdale,R.D., Loci,D., Houghton,F., Karlsson,L. and Gleeson,P.A.
  TITLE     A large family of endosome-localized proteins related to sorting
            nexin 1
  JOURNAL   Biochem J 358 (Pt 1), 7-16 (2001)
   PUBMED   11485546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL391335.32 and AL589765.19.
            
            On or before Apr 7, 2025 this sequence version replaced
            XP_024305806.1, XP_054194895.1.
            
            Summary: This gene encodes a member of the sorting nexin family, a
            diverse group of cytoplasmic and membrane-associated proteins
            involved in endocytosis of plasma membrane receptors and protein
            trafficking through these compartments. All members of this protein
            family contain a phosphoinositide binding domain (PX domain). A
            highly similar protein in mouse is responsible for the specific
            recruitment of an isoform of serotonin 5-hydroxytryptamine 4
            receptor into early endosomes, suggesting the analogous role for
            the human protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2543430.1,
                                           SRR14038192.2889237.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..355
                     /product="sorting nexin-27 isoform 9"
                     /note="methamphetamine-responsive transcript 1; sorting
                     nexin family member 27"
                     /calculated_mol_wt=41720
     Region          <1..79
                     /region_name="PX_domain"
                     /note="The Phox Homology domain, a phosphoinositide
                     binding module; cl02563"
                     /db_xref="CDD:470617"
     Site            order(10..12,36..37,49)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132796"
     Region          87..179
                     /region_name="FERM_F1_SNX27"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F1 sub-domain, found in sorting nexin protein 27
                     (SNX27); cd01777"
                     /db_xref="CDD:340475"
     Region          239..340
                     /region_name="FERM-like_C_SNX27"
                     /note="Atypical FERM-like domain C-lobe of Sorting nexin
                     27; cd13338"
                     /db_xref="CDD:270146"
     CDS             1..355
                     /gene="SNX27"
                     /gene_synonym="MRT1; MY014"
                     /coded_by="NM_001437607.1:479..1546"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:81609"
                     /db_xref="HGNC:HGNC:20073"
                     /db_xref="MIM:611541"
ORIGIN      
        1 magrqlcskr yrefailhqn lkrefanftf prlpgkwpfs lseqqldarr rgleeylekv
       61 csirvigesd imqeflsesd enyngvsdve lrvalpdgtt vtvrvkknst tdqvyqaiaa
      121 kvgmdsttvn yfalfevish sfvrklapne fphklyiqny tsavpgtclt irkwlfttee
      181 eillndndla vtyffhqavd dvkkgyikae eksyqlqkly eqrkmvmyln mlrtcegyne
      241 iifphcacds rrkghvitai sithfklhac teegqlenqv iafewdemqr wdtdeegmaf
      301 cfeyargekk prwvkiftpy fnymhecfer vfcelkwrke nifqmarsqq rdvat
//
LOCUS       NP_001427460             252 aa            linear   PRI 21-NOV-2025
DEFINITION  syntaxin-3 isoform 7 [Homo sapiens].
ACCESSION   NP_001427460 XP_047283458 XP_054225740
VERSION     NP_001427460.1
DBSOURCE    REFSEQ: accession NM_001440531.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Shinozuka,T., Kanda,M., Sato,Y., Shimizu,D., Tanaka,C., Umeda,S.,
            Inokawa,Y., Hattori,N., Hayashi,M., Nakayama,G. and Kodera,Y.
  TITLE     Increased STX3 transcript and protein levels were associated with
            poor prognosis in two independent cohorts of esophageal squamous
            cell carcinoma patients
  JOURNAL   Cancer Med 12 (24), 22185-22195 (2023)
   PUBMED   38014487
  REMARK    GeneRIF: Increased STX3 transcript and protein levels were
            associated with poor prognosis in two independent cohorts of
            esophageal squamous cell carcinoma patients.
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Janecke,A.R., Liu,X., Adam,R., Punuru,S., Viestenz,A., Strauss,V.,
            Laass,M., Sanchez,E., Adachi,R., Schatz,M.P., Saboo,U.S.,
            Mittal,N., Rohrschneider,K., Escher,J., Ganesh,A., Al Zuhaibi,S.,
            Al Murshedi,F., AlSaleem,B., Alfadhel,M., Al Sinani,S.,
            Alkuraya,F.S., Huber,L.A., Muller,T., Heidelberger,R. and Janz,R.
  TITLE     Pathogenic STX3 variants affecting the retinal and intestinal
            transcripts cause an early-onset severe retinal dystrophy in
            microvillus inclusion disease subjects
  JOURNAL   Hum Genet 140 (8), 1143-1156 (2021)
   PUBMED   33974130
  REMARK    GeneRIF: Pathogenic STX3 variants affecting the retinal and
            intestinal transcripts cause an early-onset severe retinal
            dystrophy in microvillus inclusion disease subjects.
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Low,S.H., Vasanji,A., Nanduri,J., He,M., Sharma,N., Koo,M.,
            Drazba,J. and Weimbs,T.
  TITLE     Syntaxins 3 and 4 are concentrated in separate clusters on the
            plasma membrane before the establishment of cell polarity
  JOURNAL   Mol Biol Cell 17 (2), 977-989 (2006)
   PUBMED   16339081
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Martin-Martin,B., Nabokina,S.M., Lazo,P.A. and Mollinedo,F.
  TITLE     Co-expression of several human syntaxin genes in neutrophils and
            differentiating HL-60 cells: variant isoforms and detection of
            syntaxin 1
  JOURNAL   J Leukoc Biol 65 (3), 397-406 (1999)
   PUBMED   10080545
REFERENCE   7  (residues 1 to 252)
  AUTHORS   Steegmaier,M., Yang,B., Yoo,J.S., Huang,B., Shen,M., Yu,S., Luo,Y.
            and Scheller,R.H.
  TITLE     Three novel proteins of the syntaxin/SNAP-25 family
  JOURNAL   J Biol Chem 273 (51), 34171-34179 (1998)
   PUBMED   9852078
REFERENCE   8  (residues 1 to 252)
  AUTHORS   Riento,K., Galli,T., Jansson,S., Ehnholm,C., Lehtonen,E. and
            Olkkonen,V.M.
  TITLE     Interaction of Munc-18-2 with syntaxin 3 controls the association
            of apical SNAREs in epithelial cells
  JOURNAL   J Cell Sci 111 (Pt 17), 2681-2688 (1998)
   PUBMED   9701566
REFERENCE   9  (residues 1 to 252)
  AUTHORS   Galli,T., Zahraoui,A., Vaidyanathan,V.V., Raposo,G., Tian,J.M.,
            Karin,M., Niemann,H. and Louvard,D.
  TITLE     A novel tetanus neurotoxin-insensitive vesicle-associated membrane
            protein in SNARE complexes of the apical plasma membrane of
            epithelial cells
  JOURNAL   Mol Biol Cell 9 (6), 1437-1448 (1998)
   PUBMED   9614185
REFERENCE   10 (residues 1 to 252)
  AUTHORS   Delgrossi,M.H., Breuza,L., Mirre,C., Chavrier,P. and Le Bivic,A.
  TITLE     Human syntaxin 3 is localized apically in human intestinal cells
  JOURNAL   J Cell Sci 110 (Pt 18), 2207-2214 (1997)
   PUBMED   9378770
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000640.5.
            
            On or before May 21, 2025 this sequence version replaced
            XP_047283458.1, XP_054225740.1.
            
            Summary: The gene is a member of the syntaxin family. The encoded
            protein is targeted to the apical membrane of epithelial cells
            where it forms clusters and is important in establishing and
            maintaining polarity necessary for protein trafficking involving
            vesicle fusion and exocytosis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.113164.1,
                                           SRR14038196.3365620.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..252
                     /product="syntaxin-3 isoform 7"
                     /note="syntaxin 3A; syntaxin 3B"
                     /calculated_mol_wt=28729
     Region          34..225
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     CDS             1..252
                     /gene="STX3"
                     /gene_synonym="DIAR12; MVID2; RDMVID; STX3A"
                     /coded_by="NM_001440531.1:231..989"
                     /note="isoform 7 is encoded by transcript variant 12"
                     /db_xref="GeneID:6809"
                     /db_xref="HGNC:HGNC:11438"
                     /db_xref="MIM:600876"
ORIGIN      
        1 mkdrleqlka kqltqdddtd aveiaidnta fmdeffseie etrlnidkis ehveeakkly
       61 siilsapipe pktkddleql tteikkrann vrnklksmek hieedevrss adlrirksqh
      121 svlsrkfvev mtkyneaqvd frerskgriq rqleitgkkt tdeeleemle sgnpaiftsg
      181 iidsqiskqa lseiegrhkd ivrlessike lhdmfmdiam lvenqkliii ivlvvvllgi
      241 laliiglsvg ln
//
LOCUS       NP_001427359            2868 aa            linear   PRI 21-NOV-2025
DEFINITION  lipopolysaccharide-responsive and beige-like anchor protein isoform
            5 [Homo sapiens].
ACCESSION   NP_001427359 XP_005263429 XP_054207311
VERSION     NP_001427359.1
DBSOURCE    REFSEQ: accession NM_001440430.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2868)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2868)
  AUTHORS   Szentgyorgyi,V., Lueck,L.M., Overwijn,D., Ritz,D., Zoeller,N.,
            Schmidt,A., Hondele,M., Spang,A. and Bakhtiar,S.
  TITLE     Arf1-dependent LRBA recruitment to Rab4 endosomes is required for
            endolysosome homeostasis
  JOURNAL   J Cell Biol 223 (11) (2024)
   PUBMED   39325073
  REMARK    GeneRIF: Arf1-dependent LRBA recruitment to Rab4 endosomes is
            required for endolysosome homeostasis.
REFERENCE   3  (residues 1 to 2868)
  AUTHORS   Freund,T., Baxter,S.K., Walsh,T., Golan,H., Kapelushnik,J.,
            Abramsohn-Goldenberg,M., Benor,S., Sarid,N., Ram,R., Alcalay,Y.,
            Segel,R., Renbaum,P., Stepensky,P., King,M.C., Torgerson,T.R. and
            Hagin,D.
  TITLE     Clinically Complex LRBA Deficiency Due to a Founder Allele in the
            Georgian Jewish Population
  JOURNAL   J Clin Immunol 43 (1), 151-164 (2023)
   PUBMED   36063261
  REMARK    GeneRIF: Clinically Complex LRBA Deficiency Due to a Founder Allele
            in the Georgian Jewish Population.
REFERENCE   4  (residues 1 to 2868)
  AUTHORS   Catak,M.C., Akcam,B., Bilgic Eltan,S., Babayeva,R., Karakus,I.S.,
            Akgun,G., Baser,D., Bulutoglu,A., Bayram,F., Kasap,N., Kiykim,A.,
            Hancioglu,G., Kokcu Karadag,S.I., Kendir Demirkol,Y., Ozen,S.,
            Cekic,S., Ozcan,D., Edeer Karaca,N., Sasihuseyinoglu,A.S.,
            Cansever,M., Ozek Yucel,E., Tamay,Z., Altintas,D.U., Aydogmus,C.,
            Celmeli,F., Cokugras,H., Gulez,N., Genel,F., Metin,A., Guner,S.N.,
            Kutukculer,N., Keles,S., Reisli,I., Kilic,S.S., Yildiran,A.,
            Karakoc-Aydiner,E., Lo,B., Ozen,A. and Baris,S.
  TITLE     Comparing the levels of CTLA-4-dependent biological defects in
            patients with LRBA deficiency and CTLA-4 insufficiency
  JOURNAL   Allergy 77 (10), 3108-3123 (2022)
   PUBMED   35491430
  REMARK    GeneRIF: Comparing the levels of CTLA-4-dependent biological
            defects in patients with LRBA deficiency and CTLA-4 insufficiency.
REFERENCE   5  (residues 1 to 2868)
  AUTHORS   Yao,J., Gu,H., Mou,W., Chen,Z., Ma,J., Ma,H., Li,N., Zhang,R.,
            Wang,T., Jiang,J. and Wu,R.
  TITLE     Various phenotypes of LRBA gene with compound heterozygous
            variation: A case series report of pediatric cytopenia patients
  JOURNAL   Int J Immunopathol Pharmacol 36, 3946320221125591 (2022)
   PUBMED   36074705
  REMARK    GeneRIF: Various phenotypes of LRBA gene with compound heterozygous
            variation: A case series report of pediatric cytopenia patients.
REFERENCE   6  (residues 1 to 2868)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 2868)
  AUTHORS   Gebauer,D., Li,J., Jogl,G., Shen,Y., Myszka,D.G. and Tong,L.
  TITLE     Crystal structure of the PH-BEACH domains of human LRBA/BGL
  JOURNAL   Biochemistry 43 (47), 14873-14880 (2004)
   PUBMED   15554694
  REMARK    GeneRIF: The crystal structure of the aPH-BEACH domains of LRBA
            were studied.
REFERENCE   8  (residues 1 to 2868)
  AUTHORS   Dyomin,V.G., Chaganti,S.R., Dyomina,K., Palanisamy,N., Murty,V.V.,
            Dalla-Favera,R. and Chaganti,R.S.
  TITLE     BCL8 is a novel, evolutionarily conserved human gene family
            encoding proteins with presumptive protein kinase A anchoring
            function
  JOURNAL   Genomics 80 (2), 158-165 (2002)
   PUBMED   12160729
REFERENCE   9  (residues 1 to 2868)
  AUTHORS   Wang,J.W., Howson,J., Haller,E. and Kerr,W.G.
  TITLE     Identification of a novel lipopolysaccharide-inducible gene with
            key features of both A kinase anchor proteins and chs1/beige
            proteins
  JOURNAL   J Immunol 166 (7), 4586-4595 (2001)
   PUBMED   11254716
REFERENCE   10 (residues 1 to 2868)
  AUTHORS   Feuchter,A.E., Freeman,J.D. and Mager,D.L.
  TITLE     Strategy for detecting cellular transcripts promoted by human
            endogenous long terminal repeats: identification of a novel gene
            (CDC4L) with homology to yeast CDC4
  JOURNAL   Genomics 13 (4), 1237-1246 (1992)
   PUBMED   1505956
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104796.4, AC092544.4,
            AC110813.4, AC097373.3, AC092612.3 and AC093748.3.
            
            On or before May 20, 2025 this sequence version replaced
            XP_005263429.1, XP_054207311.1.
            
            Summary: The protein encoded by this gene is a member of the
            WDL-BEACH-WD (WBW) gene family. Its expression is induced in B
            cells and macrophages by bacterial lipopolysaccharides (LPS). The
            encoded protein associates with protein kinase A and may be
            involved in leading intracellular vesicles to activated receptor
            complexes, which aids in the secretion and/or membrane deposition
            of immune effector molecules. Defects in this gene are associated
            with the disorder common variable immunodeficiency-8 with
            autoimmunity. Two transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Dec 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.2335904.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2868
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.3"
     Protein         1..2868
                     /product="lipopolysaccharide-responsive and beige-like
                     anchor protein isoform 5"
                     /note="vesicle trafficking, beach and anchor containing;
                     lipopolysaccharide-responsive and beige-like anchor
                     protein; CDC4-like protein; LPS-responsive vesicle
                     trafficking, beach and anchor containing"
                     /calculated_mol_wt=319609
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          229..376
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
     Region          441..921
                     /region_name="DUF4704"
                     /note="Neurobeachin/BDCP, DUF4704 alpha solenoid region;
                     pfam15787"
                     /db_xref="CDD:464870"
     Region          969..1005
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            979
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1003
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1018..1039
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1161..1193
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1301..1343
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1531..1548
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          1586..1668
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1759..1789
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1770
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1880..2058
                     /region_name="DUF1088"
                     /note="Neurobeachin-like, DUF1088; pfam06469"
                     /db_xref="CDD:461925"
     Site            2064
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          2084..2181
                     /region_name="PH_BEACH"
                     /note="PH domain associated with Beige/BEACH; pfam14844"
                     /db_xref="CDD:434260"
     Region          2212..2489
                     /region_name="Beach"
                     /note="Beige/BEACH domain; smart01026"
                     /db_xref="CDD:214982"
     Site            2501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          2589..2853
                     /region_name="NBCH_WD40"
                     /note="Neurobeachin beta propeller domain; pfam20426"
                     /db_xref="CDD:466575"
     Region          2596..2638
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2605..2641
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2641..2684
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2647..2700
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2700..2740
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2705..2740
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2745..2774
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2782..2821
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2787..2821
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2824..2863
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     CDS             1..2868
                     /gene="LRBA"
                     /gene_synonym="BGL; CDC4L; CVID8; LAB300; LBA; uc.147"
                     /coded_by="NM_001440430.1:303..8909"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:987"
                     /db_xref="HGNC:HGNC:1742"
                     /db_xref="MIM:606453"
ORIGIN      
        1 masednrvps ppptgddggg ggreetpteg galslkpglp irgirmkfav ltglvevgev
       61 snrdivetvf nllvggqfdl emnfiiqege sincmvdlle kcditcqaev wsmftailkk
      121 sirnlqvcte vglvekvlgk iekvdnmiad llvdmlgvla synltvrelk lffsklqgdk
      181 grwpphagkl lsvlkhmpqk ygpdaffnfp gksaaaialp piakwpyqng ftfhtwlrmd
      241 pvnninvdkd kpylycfrts kglgysahfv ggclivtsik skgkgfqhcv kfdfkpqkwy
      301 mvtivhiynr wknselrcyv ngelasygei twfvntsdtf dkcflgsset adanrvfcgq
      361 mtavylfsea lnaaqifaiy qlglgykgtf kfkaesdlfl aehhklllyd gklssaiaft
      421 ynpratdaql clesspkdnp sifvhsphal mlqdvkavlt hsiqsamhsi ggvqvlfplf
      481 aqldyrqyls deidlticst llafimellk nsiamqeqml ackgflvigy sleksskshv
      541 sravlelcla fskylsnlqn gmpllkqlcd hvllnpaiwi htpakvqlml ytylstefig
      601 tvniyntirr vgtvllimht lkyyywavnp qdrsgitpkg ldgprpnqke mlslrafllm
      661 fikqlvmkds gvkedelqai lnylltmhed dnlmdvlqll valmsehpns mipafdqrng
      721 lrviykllas ksegirvqal kamgyflkhl apkrkaevml ghglfsllae rlmlqtnlit
      781 mttynvlfei lieqigtqvi hkqhpdpdss vkiqnpqilk viatllrnsp qcpesmevrr
      841 aflsdmiklf nnsrenrrsl lqcsvwqewm lslcyfnpkn sdeqkitemv yaifrillyh
      901 avkyewggwr vwvdtlsith skvtfeihke nlanifreqq gkvdeeiglc sstsvqaasg
      961 irrdinvsvg sqqpdtkdsp vcphfttngn enssiektss lesasnielq ttntsyeemk
     1021 aeqenqelpd egtleetltn etrnaddlev ssdiieavai ssnsfittgk dsmtvsevta
     1081 sisspseeda sempefldks iveeeedddy velkvegspt eeanlptelq dnslspaase
     1141 agekldmfgn ddklifqegk pvtekqtdte tqdskdsgiq tmtasgssam spettvsqia
     1201 vesdlgqmle egkkatnltr etklindchg svseasseqk iakldvsnva tdterlelka
     1261 spnveapqph rhvleisrqh eqpgqgiapd avngqrrdsr stvfripefn wsqmhqrllt
     1321 dllfsietdi qmwrshstkt vmdfvnssdn vifvhntihl isqvmdnmvm acggilplls
     1381 aatsathele nieptqglsi easvtflqrl islvdvlifa sslgfteiea eksmssggil
     1441 rqclrlvcav avrnclecqq hsqlktrgdk alkpmhslip lgksaakspv divtggispv
     1501 rdldrllqdm dinrlravvf rdiedskqaq flalavvyfi svlmvskyrd ilepqnerhs
     1561 qsctetgsen envslseitp aafstlttas veesestssa rrrdsgigee tatglgshve
     1621 vtphtappgv sagpdaisev lstlslevnk spetkndrgn dldtkatpsv svsknvnvkd
     1681 ilrslvnipa dgvtvdpall ppaclgalgd lsveqpvqfr sfdrsvivaa kksavspstf
     1741 ntsiptnavs vvssvdsaqa sdmggespgs rssnaklpsv ptvdsvsqdp vsnmsiterl
     1801 ehalekaapl lreifvdfap flsrtllgsh gqelliegts lvcmkssssv velvmllcsq
     1861 ewqnsiqkna glafielvne grllsqtmkd hlvrvaneae filsrqraed ihrhaefesl
     1921 caqysadkre dekmcdhlir aakyrdhvta tqliqkiini ltdkhgawgn savsrplefw
     1981 rldyweddlr rrrrfvrnpl gsthpeatlk tavehvcifk lrenskatde dilakgkqsi
     2041 rsqalgnqns eneillegdd dtlssvdekd lenlagpvsl stpaqlvaps vvvkgtlsvt
     2101 sselyfevde edpnfkkidp kilayteglh gkwlfteirs ifsrryllqn taleifmanr
     2161 vavmfnfpdp atvkkvvnyl prvgvgtsfg lpqtrrisla sprqlfkasn mtqrwqhrei
     2221 snfeylmfln tiagrsyndl nqypvfpwvi tnyeseeldl tlptnfrdls kpigalnpkr
     2281 aaffaeryes weddqvpkfh ygthystasf vlawllriep fttyflnlqg gkfdhadrtf
     2341 ssisrawrns qrdtsdikel ipefyylpem fvnfnnynlg vmddgtvvsd velppwakts
     2401 eefvhinrla lesefvscql hqwidlifgy kqqgpeavra lnvfyyltye gavnlnsitd
     2461 pvlreaveaq irsfgqtpsq lliephpprg samqvylllq splmftdkaq qdvimvlkfp
     2521 snspvthvaa ntqpglatpa vitvtanrlf avnkwhnlpa hqgavqdqpy qlpveidpli
     2581 asntgmhrrq itdlldqsiq vhsqcfvits dnryilvcgf wdksfrvyst dtgrliqvvf
     2641 ghwdvvtcla rsesyiggnc yilsgsrdat lllwywngkc sgigdnpgse taaprailtg
     2701 hdyevtcaav caelglvlsg sqegpclihs mngdllrtle gpenclkpkl iqasreghcv
     2761 ifyenglfct fsvngklqat metddnirai qlsrdgqyll tggdrgvvvv rqvsdlkqlf
     2821 aypgcdagir amalsydqrc iisgmasgsi vlfyndfnrw hheyqtry
//
LOCUS       NP_001424221            1053 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            beta isoform isoform 3 [Homo sapiens].
ACCESSION   NP_001424221 XP_047304270 XP_054202831
VERSION     NP_001424221.1
DBSOURCE    REFSEQ: accession NM_001437292.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Liu,L., Feng,X., Fan,C., Kong,D., Feng,X., Sun,C., Xu,Y., Li,B.,
            Jiang,Y. and Zheng,C.
  TITLE     PDCD4 interacting with PIK3CB and CTSZ promotes the apoptosis of
            multiple myeloma cells
  JOURNAL   FASEB J 38 (16), e70024 (2024)
   PUBMED   39190024
  REMARK    GeneRIF: PDCD4 interacting with PIK3CB and CTSZ promotes the
            apoptosis of multiple myeloma cells.
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Liu,G., Hou,Y., Jin,X., Zhang,Y., Sun,C., Huang,C., Ren,Y., Gao,J.,
            Wang,X. and Jiang,X.
  TITLE     PI3K/HSCB axis facilitates FOG1 nuclear translocation to promote
            erythropoiesis and megakaryopoiesis
  JOURNAL   Elife 13, 95815 (2024)
   PUBMED   38757931
  REMARK    GeneRIF: PI3K/HSCB axis facilitates FOG1 nuclear translocation to
            promote erythropoiesis and megakaryopoiesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1053)
  AUTHORS   Duewell,B.R., Wilson,N.E., Bailey,G.M., Peabody,S.E. and
            Hansen,S.D.
  TITLE     Molecular dissection of PI3Kbeta synergistic activation by receptor
            tyrosine kinases, GbetaGgamma, and Rho-family GTPases
  JOURNAL   Elife 12, 88991 (2024)
   PUBMED   38713746
  REMARK    GeneRIF: Molecular dissection of PI3Kbeta synergistic activation by
            receptor tyrosine kinases, GbetaGgamma, and Rho-family GTPases.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1053)
  AUTHORS   Xu,W., Chen,Y., Zhang,Z., Jiang,Y. and Wang,Z.
  TITLE     Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma
  JOURNAL   Med Oncol 40 (8), 221 (2023)
   PUBMED   37402056
  REMARK    GeneRIF: Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1053)
  AUTHORS   Milani,D., Mazzoni,M., Borgatti,P., Zauli,G., Cantley,L. and
            Capitani,S.
  TITLE     Extracellular human immunodeficiency virus type-1 Tat protein
            activates phosphatidylinositol 3-kinase in PC12 neuronal cells
  JOURNAL   J Biol Chem 271 (38), 22961-22964 (1996)
   PUBMED   8798481
REFERENCE   7  (residues 1 to 1053)
  AUTHORS   Bonnefoy-Berard,N., Liu,Y.C., von Willebrand,M., Sung,A., Elly,C.,
            Mustelin,T., Yoshida,H., Ishizaka,K. and Altman,A.
  TITLE     Inhibition of phosphatidylinositol 3-kinase activity by association
            with 14-3-3 proteins in T cells
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10142-10146 (1995)
   PUBMED   7479742
REFERENCE   8  (residues 1 to 1053)
  AUTHORS   Hu,P. and Schlessinger,J.
  TITLE     Direct association of p110 beta phosphatidylinositol 3-kinase with
            p85 is mediated by an N-terminal fragment of p110 beta
  JOURNAL   Mol Cell Biol 14 (4), 2577-2583 (1994)
   PUBMED   8139559
REFERENCE   9  (residues 1 to 1053)
  AUTHORS   Hu,P., Mondino,A., Skolnik,E.Y. and Schlessinger,J.
  TITLE     Cloning of a novel, ubiquitously expressed human
            phosphatidylinositol 3-kinase and identification of its binding
            site on p85
  JOURNAL   Mol Cell Biol 13 (12), 7677-7688 (1993)
   PUBMED   8246984
REFERENCE   10 (residues 1 to 1053)
  AUTHORS   Carpenter,C.L., Duckworth,B.C., Auger,K.R., Cohen,B.,
            Schaffhausen,B.S. and Cantley,L.C.
  TITLE     Purification and characterization of phosphoinositide 3-kinase from
            rat liver
  JOURNAL   J Biol Chem 265 (32), 19704-19711 (1990)
   PUBMED   2174051
  REMARK    GeneRIF: This paper reports the first purification of a
            phosphoinositide 3-kinase and shows that the protein is a
            heterodimer of an 85 kd regulatory subunit that mediates binding to
            phosphorylated proteins and a 110 kd catalytic subunit.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC067728.25, AC117389.5 and AC020890.22.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_047304270.1, XP_054202831.1.
            
            Summary: This gene encodes an isoform of the catalytic subunit of
            phosphoinositide 3-kinase (PI3K). These kinases are important in
            signaling pathways involving receptors on the outer membrane of
            eukaryotic cells and are named for their catalytic subunit. The
            encoded protein is the catalytic subunit for PI3Kbeta (PI3KB).
            PI3KB has been shown to be part of the activation pathway in
            neutrophils which have bound immune complexes at sites of injury or
            infection. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2034604.1,
                                           SRR14038195.100211.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..1053
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit beta isoform isoform 3"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.1.153"
                     /note="PI3-kinase p110 subunit beta; PtdIns-3-kinase p110;
                     PI3K-beta; PI3-kinase subunit beta; ptdIns-3-kinase
                     subunit beta; ptdIns-3-kinase subunit p110-beta;
                     phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa
                     catalytic subunit beta; serine/threonine protein kinase
                     PIK3CB; phosphoinositide-3-kinase, catalytic, beta
                     polypeptide"
                     /calculated_mol_wt=120945
     Region          41..118
                     /region_name="PI3K_p85B"
                     /note="PI3-kinase family, p85-binding domain; smart00143"
                     /db_xref="CDD:197539"
     Region          180..288
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, Ras-binding domain; smart00144"
                     /db_xref="CDD:197540"
     Region          324..501
                     /region_name="C2_PI3K_class_I_beta_delta"
                     /note="C2 domain present in class I beta and delta
                     phosphatidylinositol 3-kinases (PI3Ks); cd08693"
                     /db_xref="CDD:176075"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI9; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     Region          410..418
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Region          515..685
                     /region_name="PI3Ka_I"
                     /note="Phosphoinositide 3-kinase (PI3K) class I, accessory
                     domain; PIK domain is conserved in all PI3 and
                     PI4-kinases. Its role is unclear but it has been suggested
                     to be involved in substrate presentation. In general, PI3K
                     class I prefer phosphoinositol (4,5)...; cd00872"
                     /db_xref="CDD:238444"
     Region          689..1050
                     /region_name="PI3Kc_IA_beta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase beta; cd05173"
                     /db_xref="CDD:270717"
     Region          761..767
                     /region_name="G-loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(762,764..766,768,786,788,791,822,834..837,842,845,
                     907,909,919..920)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270717"
     Site            order(829..830,857..858,861,931..932,945,948,956..959,962,
                     1029,1032..1033,1035..1036)
                     /site_type="other"
                     /note="regulatory subunit interface [polypeptide binding]"
                     /db_xref="CDD:270717"
     Site            876
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270717"
     Region          899..907
                     /region_name="Catalytic loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            899..907
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270717"
     Region          918..944
                     /region_name="Activation loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(920..933,939..944)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270717"
     Site            1053
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12502714; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     CDS             1..1053
                     /gene="PIK3CB"
                     /gene_synonym="P110BETA; PI3K; PI3KBETA; PIK3C1"
                     /coded_by="NM_001437292.1:423..3584"
                     /note="isoform 3 is encoded by transcript variant 10"
                     /db_xref="GeneID:5291"
                     /db_xref="HGNC:HGNC:8976"
                     /db_xref="MIM:602925"
ORIGIN      
        1 mcfsfimppa madildiwav dsqiasdgsi pvdfllptgi yiqlevprea tisyikqmlw
       61 kqvhnypmfn llmdidsymf acvnqtavye eledetrrlc dvrpflpvlk lvtrscdpge
      121 kldskigvli gkglhefdsl kdpevnefrr kmrkfseeki lslvglswmd wlkqtyppeh
      181 epsipenled klyggkliva vhfencqdvf sfqvspnmnp ikvnelaiqk rltihgkede
      241 vspydyvlqv sgrveyvfgd hpliqfqyir ncvmnralph filvecckik kmyeqemiai
      301 eaainrnssn lplplppkkt riishvwenn npfqivlvkg nklnteetvk vhvraglfhg
      361 tellcktivs sevsgkndhi wneplefdin icdlprmarl cfavyavldk vktkkstkti
      421 npskyqtirk agkvhypvaw vntmvfdfkg qlrtgdiilh swssfpdele emlnpmgtvq
      481 tnpytenata lhvkfpenkk qpyyyppfdk srggkkflpv lkeildrdpl sqlcenemdl
      541 iwtlrqdcre ifpqslpkll lsikwnkled vaqlqallqi wpklppreal elldfnypdq
      601 yvreyavgcl rqmsdeelsq yllqlvqvlk yepfldcals rflleralgn rrigqflfwh
      661 lrsevhipav svqfgvilea ycrgsvghmk vlskqvealn klktlnslik lnavklnrak
      721 gkeamhtclk qsayrealsd lqsplnpcvi lselyvekck ymdskmkplw lvynnkvfge
      781 dsvgvifkng ddlrqdmltl qmlrlmdllw keagldlrml pygclatgdr sglievvsts
      841 etiadiqlns snvaaaaafn kdallnwlke ynsgddldra ieeftlscag ycvasyvlgi
      901 gdrhsdnimv kktgqlfhid fghilgnfks kfgikrervp filtydfihv iqqgktgnte
      961 kfgrfrqcce daylilrrhg nlfitlfalm ltaglpelts vkdiqylkds lalgkseeea
     1021 lkqfkqkfde alreswttkv nwmahtvrkd yrs
//
LOCUS       NP_001400620             289 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 23 precursor [Homo sapiens].
ACCESSION   NP_001400620
VERSION     NP_001400620.1
DBSOURCE    REFSEQ: accession NM_001413691.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 289)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 289)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 289)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3295722.1,
                                           SRR13316199.175511.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..289
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 23 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=28624
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..287
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     CDS             1..289
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413691.1:169..1038"
                     /note="isoform 23 precursor is encoded by transcript
                     variant 27"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvsyih gssqaqfvae shiilvlts
//
LOCUS       NP_001428014            1268 aa            linear   PRI 21-NOV-2025
DEFINITION  cohesin subunit SA-2 isoform a [Homo sapiens].
ACCESSION   NP_001428014 XP_047297734 XP_054182358
VERSION     NP_001428014.1
DBSOURCE    REFSEQ: accession NM_001441085.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1268)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1268)
  AUTHORS   Fischer,A., Hernandez-Rodriguez,B., Mulet-Lazaro,R., Nuetzel,M.,
            Holzl,F., van Herk,S., Kavelaars,F.G., Stanewsky,H., Ackermann,U.,
            Niang,A.H., Diaz,N., Reuschel,E., Strieder,N., Hernandez-Lopez,I.,
            Valk,P.J.M., Vaquerizas,J.M., Rehli,M., Delwel,R. and Gebhard,C.
  TITLE     STAG2 mutations reshape the cohesin-structured spatial chromatin
            architecture to drive gene regulation in acute myeloid leukemia
  JOURNAL   Cell Rep 43 (8), 114498 (2024)
   PUBMED   39084219
  REMARK    GeneRIF: STAG2 mutations reshape the cohesin-structured spatial
            chromatin architecture to drive gene regulation in acute myeloid
            leukemia.
REFERENCE   3  (residues 1 to 1268)
  AUTHORS   Huber,J., Tanasie,N.L., Zernia,S. and Stigler,J.
  TITLE     Single-molecule imaging reveals a direct role of CTCF's zinc
            fingers in SA interaction and cluster-dependent RNA recruitment
  JOURNAL   Nucleic Acids Res 52 (11), 6490-6506 (2024)
   PUBMED   38742641
  REMARK    GeneRIF: Single-molecule imaging reveals a direct role of CTCF's
            zinc fingers in SA interaction and cluster-dependent RNA
            recruitment.
REFERENCE   4  (residues 1 to 1268)
  AUTHORS   Xu,W., Kim,J.S., Yang,T., Ya,A., Sadzewicz,L., Tallon,L.,
            Harris,B.T., Sarkaria,J., Jin,F. and Waldman,T.
  TITLE     STAG2 mutations regulate 3D genome organization, chromatin loops,
            and Polycomb signaling in glioblastoma multiforme
  JOURNAL   J Biol Chem 300 (6), 107341 (2024)
   PUBMED   38705393
  REMARK    GeneRIF: STAG2 mutations regulate 3D genome organization, chromatin
            loops, and Polycomb signaling in glioblastoma multiforme.
REFERENCE   5  (residues 1 to 1268)
  AUTHORS   Ros-Pardo,D., Gomez-Puertas,P. and Marcos-Alcalde,I.
  TITLE     STAG2: Computational Analysis of Missense Variants Involved in
            Disease
  JOURNAL   Int J Mol Sci 25 (2), 1280 (2024)
   PUBMED   38279279
  REMARK    GeneRIF: STAG2: Computational Analysis of Missense Variants
            Involved in Disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1268)
  AUTHORS   Gregson,H.C., Schmiesing,J.A., Kim,J.S., Kobayashi,T., Zhou,S. and
            Yokomori,K.
  TITLE     A potential role for human cohesin in mitotic spindle aster
            assembly
  JOURNAL   J Biol Chem 276 (50), 47575-47582 (2001)
   PUBMED   11590136
REFERENCE   7  (residues 1 to 1268)
  AUTHORS   Sumara,I., Vorlaufer,E., Gieffers,C., Peters,B.H. and Peters,J.M.
  TITLE     Characterization of vertebrate cohesin complexes and their
            regulation in prophase
  JOURNAL   J Cell Biol 151 (4), 749-762 (2000)
   PUBMED   11076961
REFERENCE   8  (residues 1 to 1268)
  AUTHORS   Carramolino,L., Lee,B.C., Zaballos,A., Peled,A., Barthelemy,I.,
            Shav-Tal,Y., Prieto,I., Carmi,P., Gothelf,Y., Gonzalez de
            Buitrago,G., Aracil,M., Marquez,G., Barbero,J.L. and Zipori,D.
  TITLE     SA-1, a nuclear protein encoded by one member of a novel gene
            family: molecular cloning and detection in hemopoietic organs
  JOURNAL   Gene 195 (2), 151-159 (1997)
   PUBMED   9305759
  REMARK    Erratum:[Gene 1998 Jan 12;206(2):283]
REFERENCE   9  (residues 1 to 1268)
  AUTHORS   Wu,C., Friedlander,P., Lamoureux,C., Zannis-Hadjopoulos,M. and
            Price,G.B.
  TITLE     cDNA clones contain autonomous replication activity
  JOURNAL   Biochim Biophys Acta 1174 (3), 241-257 (1993)
   PUBMED   7690594
REFERENCE   10 (residues 1 to 1268)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121601.13 and AL355476.12.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297734.1, XP_054182358.1.
            
            Summary: The protein encoded by this gene is a subunit of the
            cohesin complex, which regulates the separation of sister
            chromatids during cell division. Targeted inactivation of this gene
            results in chromatid cohesion defects and aneuploidy, suggesting
            that genetic disruption of cohesin is a cause of aneuploidy in
            human cancer. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2466949.1,
                                           SRR18074967.2465824.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142363, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1268
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..1268
                     /product="cohesin subunit SA-2 isoform a"
                     /note="SCC3 homolog 2; cohesin subunit SA-2; SA2
                     stromalin; sister chromatid cohesion 3 homolog B; stromal
                     antigen 2"
                     /calculated_mol_wt=145621
     Region          102..>395
                     /region_name="IRR1"
                     /note="Cohesin [Cell division and chromosome
                     partitioning]; COG5537"
                     /db_xref="CDD:227824"
     Region          157..270
                     /region_name="STAG"
                     /note="STAG domain; pfam08514"
                     /db_xref="CDD:462502"
     CDS             1..1268
                     /gene="STAG2"
                     /gene_synonym="bA517O1.1; HPE13; MKMS; NEDXCF; SA-2; SA2;
                     SCC3B"
                     /coded_by="NM_001441085.1:352..4158"
                     /note="isoform a is encoded by transcript variant 24"
                     /db_xref="GeneID:10735"
                     /db_xref="HGNC:HGNC:11355"
                     /db_xref="MIM:300826"
ORIGIN      
        1 miaapeiptd fnllqeseth fssdtdfedi egknqkqgkg ktckkgkkgp aekgkggngg
       61 gkppsgpnrm nghhqqngve nmmlfevvkm gksamqsvvd dwiesykhdr dialldlinf
      121 fiqcsgckgv vtaemfrhmq nseiirkmte efdedsgdyp ltmagpqwkk fkssfcefig
      181 vlvrqcqysi iydeymmdtv islltglsds qvrafrhtst laamklmtal vnvalnlsin
      241 mdntqrqyea ernkmigkra nerlelllqk rkelqenqde ienmmnaifk gvfvhryrda
      301 iaeiraicie eigiwmkmys daflndsylk yvgwtmhdkq gevrlkclta lqglyynkel
      361 nsklelftsr fkdrivsmtl dkeydvavqa iklltlvlqs seevltaedc envyhlvysa
      421 hrpvavaage flykklfsrr dpeedgmmkr rgrqgpnanl vktlvfffle selhehaayl
      481 vdsmwdcate llkdwecmns llleeplsge ealtdrqesa lieimlctir qaaechppvg
      541 rgtgkrvlta kekktqlddr tkitelfava lpqllakysv daekvtnllq lpqyfdleiy
      601 ttgrlekhld allrqirniv ekhtdtdvle acsktyhalc neeftifnrv disrsqlide
      661 ladkfnrlle dflqegeepd eddayqvlst lkritafhna hdlskwdlfa cnykllktgi
      721 engdmpeqiv ihalqcthyv ilwqlakite ssstkedllr lkkqmrvfcq icqhyltnvn
      781 ttvkeqafti lcdilmifsh qimsggrdml eplvytpdss lqsellsfil dhvfieqddd
      841 nnsadgqqed easkiealhk rrnllaafck livytvvemn taadifkqym kyyndygdii
      901 ketmsktrqi dkiqcaktli lslqqlfnem iqengynfdr ssstfsgike larrfaltfg
      961 ldqlktreai amlhkdgief afkepnpqge shpplnlafl dilsefsskl lrqdkrtvyv
     1021 ylekfmtfqm slrredvwlp lmsyrnslla ggdddtmsvi sgissrgstv rskkskpstg
     1081 krkvvegmql slteessssd smwlsreqtl htpvmmqtpq ltstimrepk rlrpedsfms
     1141 vypmqtehhq tpldyntqvt wmlaqrqqee arqqqeraam syvklrtnlq hairrgtslm
     1201 eddeepived vmmssegrie dlnegmdfdt mdidlppskn rrertelkpd ffdpasimde
     1261 svlgvsmf
//
LOCUS       NP_001402867             422 aa            linear   PRI 21-NOV-2025
DEFINITION  synaptotagmin-1 isoform 1 [Homo sapiens].
ACCESSION   NP_001402867 XP_011537012
VERSION     NP_001402867.1
DBSOURCE    REFSEQ: accession NM_001415938.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Stephan,G., Haddock,S., Wang,S., Erdjument-Bromage,H., Liu,W.,
            Ravn-Boess,N., Frenster,J.D., Bready,D., Cai,J., Ronnen,R.,
            Sabio-Ortiz,J., Fenyo,D., Neubert,T.A. and Placantonakis,D.G.
  TITLE     Modulation of GPR133 (ADGRD1) signaling by its intracellular
            interaction partner extended synaptotagmin 1
  JOURNAL   Cell Rep 43 (5), 114229 (2024)
   PUBMED   38758649
  REMARK    GeneRIF: Modulation of GPR133 (ADGRD1) signaling by its
            intracellular interaction partner extended synaptotagmin 1.
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Zhang,J., Ren,G., Huang,T., Sang,Y., Zhong,Y. and Yi,Y.
  TITLE     miRNA-363-3p Hinders Proliferation, Migration, Invasion and
            Autophagy of Thyroid Cancer Cells by Controlling SYT1 Transcription
            to affect NF-kappaB
  JOURNAL   Endocr Metab Immune Disord Drug Targets 24 (1), 153-162 (2024)
   PUBMED   37150983
  REMARK    GeneRIF: miRNA-363-3p Hinders Proliferation, Migration, Invasion
            and Autophagy of Thyroid Cancer Cells by Controlling SYT1
            Transcription to affect NF-kappaB.
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Yamada,K., Motohashi,S., Oikawa,T., Tago,N., Koizumi,R., Ono,M.,
            Tachibana,T., Yoshida,A., Yoshida,S., Shimoda,M., Oka,M., Yoneda,Y.
            and Yoshida,K.
  TITLE     Extended-synaptotagmin 1 engages in unconventional protein
            secretion mediated via SEC22B+ vesicle pathway in liver cancer
  JOURNAL   Proc Natl Acad Sci U S A 119 (36), e2202730119 (2022)
   PUBMED   36044553
  REMARK    GeneRIF: Extended-synaptotagmin 1 engages in unconventional protein
            secretion mediated via SEC22B(+) vesicle pathway in liver cancer.
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Thibord,F., Chan,M.V., Chen,M.H. and Johnson,A.D.
  TITLE     A year of COVID-19 GWAS results from the GRASP portal reveals
            potential genetic risk factors
  JOURNAL   HGG Adv 3 (2), 100095 (2022)
   PUBMED   35224516
REFERENCE   6  (residues 1 to 422)
  AUTHORS   McMahon,H.T., Missler,M., Li,C. and Sudhof,T.C.
  TITLE     Complexins: cytosolic proteins that regulate SNAP receptor function
  JOURNAL   Cell 83 (1), 111-119 (1995)
   PUBMED   7553862
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Chowdhury,D., Travis,G.H., Sutcliffe,J.G. and Burton,F.H.
  TITLE     Synaptotagmin I and 1B4 are identical: implications for
            synaptotagmin distribution in the primate brain
  JOURNAL   Neurosci Lett 190 (1), 9-12 (1995)
   PUBMED   7624059
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Mochly-Rosen,D., Miller,K.G., Scheller,R.H., Khaner,H., Lopez,J.
            and Smith,B.L.
  TITLE     p65 fragments, homologous to the C2 region of protein kinase C,
            bind to the intracellular receptors for protein kinase C
  JOURNAL   Biochemistry 31 (35), 8120-8124 (1992)
   PUBMED   1326322
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Perin,M.S., Johnston,P.A., Ozcelik,T., Jahn,R., Francke,U. and
            Sudhof,T.C.
  TITLE     Structural and functional conservation of synaptotagmin (p65) in
            Drosophila and humans
  JOURNAL   J Biol Chem 266 (1), 615-622 (1991)
   PUBMED   1840599
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Blaustein,R.O., Germann,W.J., Finkelstein,A. and DasGupta,B.R.
  TITLE     The N-terminal half of the heavy chain of botulinum type A
            neurotoxin forms channels in planar phospholipid bilayers
  JOURNAL   FEBS Lett 226 (1), 115-120 (1987)
   PUBMED   2446925
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073606.19, AC073572.19,
            AC078917.14 and AC027288.26.
            
            On Jan 5, 2023 this sequence version replaced XP_011537012.1.
            
            Summary: This gene encodes a member of the synaptotagmin protein
            family. The synaptotagmins are integral membrane proteins of
            synaptic vesicles that serve as calcium sensors in the process of
            vesicular trafficking and exocytosis. The encoded protein
            participates in triggering neurotransmitter release at the synapse
            in response to calcium binding. Mutations in this gene are
            associated with Baker-Gordon syndrome. [provided by RefSeq, Jan
            2023].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.161302.1,
                                           SRR1803614.108410.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.2"
     Protein         1..422
                     /product="synaptotagmin-1 isoform 1"
                     /note="sytI; synaptotagmin I"
                     /calculated_mol_wt=47442
     Region          6..113
                     /region_name="Syt1_N"
                     /note="N-terminal domain of synaptotagmin-1 (Syt1) and
                     similar proteins; cd21963"
                     /db_xref="CDD:409248"
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            order(40,43..44,46..48,50..51)
                     /site_type="other"
                     /note="Botolinum neurotoxin B binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409248"
     Site            58..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Region          113..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Region          136..382
                     /region_name="Phospholipid binding. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Region          143..265
                     /region_name="C2A_Synaptotagmin-1-5-6-9-10"
                     /note="C2A domain first repeat present in Synaptotagmins
                     1, 5, 6, 9, and 10; cd08385"
                     /db_xref="CDD:176031"
     Site            order(173,179,231,233,239)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176031"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P46096; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46096; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Region          274..409
                     /region_name="C2B_Synaptotagmin-1"
                     /note="C2 domain second repeat present in Synaptotagmin 1;
                     cd08402"
                     /db_xref="CDD:176047"
     Site            order(304,310,364,366,372)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176047"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21707; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21707; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     CDS             1..422
                     /gene="SYT1"
                     /gene_synonym="BAGOS; P65; SVP65; SYT"
                     /coded_by="NM_001415938.1:487..1755"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="GeneID:6857"
                     /db_xref="HGNC:HGNC:11509"
                     /db_xref="MIM:185605"
ORIGIN      
        1 mvseshheal aappvttvat vlpsnatepa spgegkedaf sklkekfmne lhkiplppwa
       61 liaiaivavl lvltccfcic kkclfkkknk kkgkekggkn ainmkdvkdl gktmkdqalk
      121 dddaetgltd geekeepkee eklgklqysl dydfqnnqll vgiiqaaelp aldmggtsdp
      181 yvkvfllpdk kkkfetkvhr ktlnpvfneq ftfkvpysel ggktlvmavy dfdrfskhdi
      241 igefkvpmnt vdfghvteew rdlqsaekee qeklgdicfs lryvptagkl tvvileaknl
      301 kkmdvgglsd pyvkihlmqn gkrlkkkktt ikkntlnpyy nesfsfevpf eqiqkvqvvv
      361 tvldydkigk ndaigkvfvg ynstgaelrh wsdmlanprr piaqwhtlqv eeevdamlav
      421 kk
//
LOCUS       NP_001396233            2556 aa            linear   PRI 21-NOV-2025
DEFINITION  histone-lysine N-methyltransferase, H3 lysine-36 specific isoform c
            [Homo sapiens].
ACCESSION   NP_001396233
VERSION     NP_001396233.1
DBSOURCE    REFSEQ: accession NM_001409304.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2556)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2556)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   3  (residues 1 to 2556)
  AUTHORS   Conteduca,G., Cangelosi,D., Baldo,C., Arado,A., Testa,B.,
            Wagner,R.T., Robertson,K.D., Dequiedt,F., Fitzsimmons,L.,
            Malacarne,M., Filaci,G. and Coviello,D.A.
  TITLE     Impact of NSD1 Alternative Transcripts in Actin Filament Formation
            and Cellular Division Pathways in Fibroblasts
  JOURNAL   Genes (Basel) 15 (9), 1117 (2024)
   PUBMED   39336709
  REMARK    GeneRIF: Impact of NSD1 Alternative Transcripts in Actin Filament
            Formation and Cellular Division Pathways in Fibroblasts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2556)
  AUTHORS   Ren,Z., Yue,L., Hu,H.Y., Hou,X.L., Chen,W.Q., Tan,Y., Dong,Z. and
            Zhang,J.
  TITLE     Identification of Novel NSD1 variations in four Pediatric cases
            with sotos Syndrome
  JOURNAL   BMC Med Genomics 17 (1), 116 (2024)
   PUBMED   38684994
  REMARK    GeneRIF: Identification of Novel NSD1 variations in four Pediatric
            cases with sotos Syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2556)
  AUTHORS   Wang,X., Yeh,S., Wu,G., Hsu,C.L., Wang,L., Chiang,T., Yang,Y.,
            Guo,Y. and Chang,C.
  TITLE     Identification and characterization of a novel androgen receptor
            coregulator ARA267-alpha in prostate cancer cells
  JOURNAL   J Biol Chem 276 (44), 40417-40423 (2001)
   PUBMED   11509567
REFERENCE   6  (residues 1 to 2556)
  AUTHORS   Jaju,R.J., Fidler,C., Haas,O.A., Strickson,A.J., Watkins,F.,
            Clark,K., Cross,N.C., Cheng,J.F., Aplan,P.D., Kearney,L.,
            Boultwood,J. and Wainscoat,J.S.
  TITLE     A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in
            de novo childhood acute myeloid leukemia
  JOURNAL   Blood 98 (4), 1264-1267 (2001)
   PUBMED   11493482
REFERENCE   7  (residues 1 to 2556)
  AUTHORS   Lee,D.K., Duan,H.O. and Chang,C.
  TITLE     Androgen receptor interacts with the positive elongation factor
            P-TEFb and enhances the efficiency of transcriptional elongation
  JOURNAL   J Biol Chem 276 (13), 9978-9984 (2001)
   PUBMED   11266437
REFERENCE   8  (residues 1 to 2556)
  AUTHORS   Huang,N., vom Baur,E., Garnier,J.M., Lerouge,T., Vonesch,J.L.,
            Lutz,Y., Chambon,P. and Losson,R.
  TITLE     Two distinct nuclear receptor interaction domains in NSD1, a novel
            SET protein that exhibits characteristics of both corepressors and
            coactivators
  JOURNAL   EMBO J 17 (12), 3398-3412 (1998)
   PUBMED   9628876
REFERENCE   9  (residues 1 to 2556)
  AUTHORS   Ocansey,S., Cole,T.R.P., Rahman,N. and Tatton-Brown,K.
  TITLE     Sotos Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301652
REFERENCE   10 (residues 1 to 2556)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027314.5, AC008570.6 and
            AC146507.2.
            
            Summary: This gene encodes a protein containing a SET domain, 2
            LXXLL motifs, 3 nuclear translocation signals (NLSs), 4 plant
            homeodomain (PHD) finger regions, and a proline-rich region. The
            encoded protein enhances androgen receptor (AR) transactivation,
            and this enhancement can be increased further in the presence of
            other androgen receptor associated coregulators. This protein may
            act as a nucleus-localized, basic transcriptional factor and also
            as a bifunctional transcriptional regulator. Mutations of this gene
            have been associated with Sotos syndrome and Weaver syndrome. One
            version of childhood acute myeloid leukemia is the result of a
            cryptic translocation with the breakpoints occurring within nuclear
            receptor-binding Su-var, enhancer of zeste, and trithorax domain
            protein 1 on chromosome 5 and nucleoporin, 98-kd on chromosome 11.
            Multiple transcript variants encoding distinct isoforms have been
            identified for this gene. [provided by RefSeq, Sep 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.400047.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMN03267750
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2556
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..2556
                     /product="histone-lysine N-methyltransferase, H3 lysine-36
                     specific isoform c"
                     /EC_number="2.1.1.357"
                     /note="androgen receptor-associated coregulator 267;
                     histone-lysine N-methyltransferase, H3 lysine-36 and H4
                     lysine-20 specific; H3-K36-HMTase; H4-K20-HMTase; lysine
                     N-methyltransferase 3B; NR-binding SET domain-containing
                     protein; androgen receptor coactivator 267 kDa protein;
                     androgen receptor-associated protein of 267 kDa; nuclear
                     receptor-binding SET domain-containing protein 1; nuclear
                     receptor SET domain-containing protein 1; histone-lysine
                     N-methyltransferase, H3 lysine-36 specific"
                     /calculated_mol_wt=281043
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88491; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          178..293
                     /region_name="PWWP_NSD1_rpt1"
                     /note="first PWWP domain found in nuclear receptor-binding
                     SET domain-containing protein 1 (NSD1) and similar
                     proteins; cd20161"
                     /db_xref="CDD:438989"
     Site            order(194,197,228)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438989"
     Site            195..198
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438989"
     Site            order(266..268,271..272)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438989"
     Region          <1291..1447
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          1405..1447
                     /region_name="PHD1_NSD1_2"
                     /note="PHD finger 1 found in nuclear receptor-binding SET
                     domain-containing protein NSD1 and NSD2; cd15648"
                     /db_xref="CDD:277118"
     Site            order(1405,1414..1418,1423,1441)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277118"
     Region          1452..1498
                     /region_name="PHD2_NSD1"
                     /note="PHD finger 2 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15650"
                     /db_xref="CDD:277120"
     Site            order(1452,1462..1466,1472,1493)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277120"
     Region          1499..1552
                     /region_name="PHD3_NSD1"
                     /note="PHD finger 3 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15653"
                     /db_xref="CDD:277123"
     Site            order(1499,1517..1521,1525,1547)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277123"
     Region          1569..1608
                     /region_name="PHD4_NSD1"
                     /note="PHD finger 4 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15656"
                     /db_xref="CDD:277126"
     Site            order(1569,1578..1582,1586,1603)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277126"
     Region          1615..1710
                     /region_name="PWWP_NSD1_rpt2"
                     /note="second PWWP domain found in nuclear
                     receptor-binding SET domain-containing protein 1 (NSD1)
                     and similar proteins; cd20164"
                     /db_xref="CDD:438992"
     Site            order(1627,1630,1658)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438992"
     Site            1628..1631
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438992"
     Region          1761..1799
                     /region_name="AWS"
                     /note="AWS domain; pfam17907"
                     /db_xref="CDD:465559"
     Region          1801..1942
                     /region_name="SET_NSD1"
                     /note="SET domain (including post-SET domain) found in
                     nuclear receptor-binding SET domain-containing protein 1
                     (NSD1) and similar proteins; cd19210"
                     /db_xref="CDD:380987"
     Site            order(1812..1814,1831,1841,1845,1854..1860,1877..1881,
                     1888..1890,1905,1916..1926,1928..1932,1941)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380987"
     Site            order(1812..1814,1854..1857,1877..1881,1918,1925,
                     1929..1932,1941)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380987"
     Site            order(1831,1841,1845,1856..1860,1888..1890,1905,
                     1916..1920)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:380987"
     Site            order(1883,1930,1932,1937)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380987"
     Region          1980..2022
                     /region_name="PHD5_NSD1"
                     /note="PHD finger 5 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15659"
                     /db_xref="CDD:277129"
     Site            order(1980,1989..1993,1999,2017)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277129"
     Region          2021..2070
                     /region_name="C5HCH"
                     /note="NSD Cys-His rich domain; pfam17982"
                     /db_xref="CDD:465605"
     Region          <2068..2434
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..2556
                     /gene="NSD1"
                     /gene_synonym="ARA267; KMT3B; SOTOS; SOTOS1; STO"
                     /coded_by="NM_001409304.1:155..7825"
                     /note="isoform c is encoded by transcript variant 7"
                     /db_xref="GeneID:64324"
                     /db_xref="HGNC:HGNC:14234"
                     /db_xref="MIM:606681"
ORIGIN      
        1 mdqtcelprr ncllpfsnpv nldapedkds pfgngqsnfs eplngctmql stvsgtsqna
       61 ygqdspscyi plrrlqdlas minveylngs adgsesfqdp eksdsraqtp ivctslspgg
      121 ptalamkqep scnnspelqd dpdsststlg nmlelpgtss sstsqelpfc qpkkkstplk
      181 yevgdliwak fkrrpwwpcr icsdplinth skmkvsnrrp yrqyyveafg dpserawvag
      241 kaivmfegrh qfeelpvlrr rgkqkekgyr hkvpqkilsk weasvglaeq ydvpkgsknr
      301 kcipgsikld seedmpfedc tndpesehdl llngclksla fdsehsadek ekpcaksrar
      361 kssdnpkrts vkkghiqfea hkderrgkip enlglnfisg disdtqasne lsriansltg
      421 sntapgsflf sscgkntakk efetsngdsl lglpegalis kcsreknkpq rslvcgskvk
      481 lcyigagdee krsdsisict tsddgssdld piehssesdn svleipdafd rtenmlsmqk
      541 nekikysrfa atntrvkakq kplisnshtd hlmgctksae pgtetsqvnl sdlkastlvh
      601 kpqsdftnda lspkfnlsss issenslikg gaanqallhs kskqpkfrsi kckhkenpvm
      661 aeppvineec slkccssdtk gsplasisks gkvdglklln nmhektrdss dietavvkhv
      721 lselkelsyr slgedvsdsg tskpskpllf ssassqnhip iepdykfstl lmmlkdmhds
      781 ktkeqrlmta qnlvsyrspg rgdcstnspv gvskvlvsgg sthnsekkgd gtqnsanpsp
      841 sggdsalsge lsaslpglls dkrdlpasgk srsdcvtrrn cgrskpsskl rdafsaqmvk
      901 ntvnrkalkt erkrklnqlp svtldavlqg drerggslrg gaedpskedp lqimghltse
      961 dgdhfsdvhf dskvkqsdpg kisekglsfe ngkgpeldsv mnsendelng vnqvvpkkrw
     1021 qrlnqrrtkp rkrmnrfkek ensecafrvl lpsdpvqegr defpehrtps asileeplte
     1081 qnhadcldsa gprlnvcdks sasigdmeke pgipsltpqa elpepavrse kkrlrkpskw
     1141 lleyteeydq ifapkkkqkk vqeqvhkvss rceeesllar grssaqnkqv denslistke
     1201 eppvlereap flegplaqse lggghaelpq ltlsvpvape vsprpalese ellvktpgny
     1261 eskrqrkptk kllesndldp gfmpkkgdlg lskkcyeagh lengitesca tsyskdfggg
     1321 ttkifdkprk rkrqrhaaak mqckkvkndd sskeipgseg elmphrtats pketveegve
     1381 hdpgmpaskk mqgergggaa lkenvcqnce klgelllcea qccgafhlec lgltemprgk
     1441 ficnecrtgi htcfvckqsg edvkrcllpl cgkfyheecv qkypptvmqn kgfrcslhic
     1501 itchaanpan vsaskgrlmr cvrcpvayha ndfclaagsk ilasnsiicp nhftprrgcr
     1561 nhehvnvswc fvcseggsll ccdscpaafh reclnidipe gnwycndcka gkkphyreiv
     1621 wvkvgryrww paeichprav psnidkmrhd vgefpvlffg sndylwthqa rvfpymegdv
     1681 sskdkmgkgv dgtykkalqe aaarfeelka qkelrqlqed rkndkkpppy khikvnrpig
     1741 rvqiftadls eiprcnckat denpcgidse cinrmllyec hptvcpaggr cqnqcfskrq
     1801 ypeveifrtl qrgwglrtkt dikkgefvne yvgelideee crariryaqe hditnfymlt
     1861 ldkdriidag pkgnyarfmn hccqpncetq kwsvngdtrv glfalsdika gteltfnynl
     1921 eclgngktvc kcgapncsgf lgvrpknqpi ateekskkfk kkqqgkrrtq geitkerede
     1981 cfscgdagql vsckkpgcpk vyhadclnlt krpagkwecp whqcdicgke aasfcemcps
     2041 sfckqhregm lfiskldgrl sctehdpcgp nplepgeire yvpppvplpp gpsthlaeqs
     2101 tgmaaqapkm sdkppadtnq mlslskkala gtcqrpllpe rplertdsrp qpldkvrdla
     2161 gsgtksqslv ssqrpldrpp avagprpqls dkpspvtsps sspsvrsqpl erplgtadpr
     2221 ldksigaasp rpqslektsv ptglrlpppd rllitsspkp qtsdrptdkp haslsqrlpp
     2281 pekvlsavvq tlvakekalr pvdqntqskn raalvmdlid ltprqkeraa sphqvtpqad
     2341 ekmpvlesss wpaskglghm pravekgcvs dplqtsgkaa apsedpwqav ksltqarlls
     2401 qppakaflye pttqasgras agaeqtpgpl sqspglvkqa kqmvggqqlp alaaksgqsf
     2461 rslgkapasl pteekklvtt eqspwalgka ssraglwpiv agqtlaqscw sagstqtlaq
     2521 tcwslgrgqd pkpeqntlpa lnqapsshkc aeseqk
//
LOCUS       NP_001400843             443 aa            linear   PRI 21-NOV-2025
DEFINITION  transcription factor ETV6 isoform 3 [Homo sapiens].
ACCESSION   NP_001400843
VERSION     NP_001400843.1
DBSOURCE    REFSEQ: accession NM_001413914.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Xu,W., Tian,F., Tai,X., Song,G., Liu,Y., Fan,L., Weng,X., Yang,E.,
            Wang,M., Bornhauser,M., Zhang,C., Lock,R.B., Wong,J.W.H., Wang,J.,
            Jing,D. and Mi,J.Q.
  TITLE     ETV6::ACSL6 translocation-driven super-enhancer activation leads to
            eosinophilia in acute lymphoblastic leukemia through IL-3
            overexpression
  JOURNAL   Haematologica 109 (8), 2445-2458 (2024)
   PUBMED   38356460
  REMARK    GeneRIF: ETV6::ACSL6 translocation-driven super-enhancer activation
            leads to eosinophilia in acute lymphoblastic leukemia through IL-3
            overexpression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Xue,S., Sun,H.P., Huang,X.B., Chen,X., Wang,T., Ma,W., Tian,Y.,
            Pan,Z.L., Li,L.H., Zhang,L., Liu,H.X. and Cao,X.Y.
  TITLE     Characteristics and literature review of ETV6::ABL1 fusion
            gene-positive acute myeloid leukemia
  JOURNAL   Int J Hematol 119 (5), 564-572 (2024)
   PUBMED   38441775
  REMARK    GeneRIF: Characteristics and literature review of ETV6::ABL1 fusion
            gene-positive acute myeloid leukemia.
            Review article
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Mueller,S.B., Pikman,Y., Tasian,S.K., Silverman,L.B., Harris,M.H.
            and Tsai,H.K.
  TITLE     ETV6 fusions from insertions of exons 3-5 in pediatric hematologic
            malignancies
  JOURNAL   Haematologica 108 (12), 3471-3476 (2023)
   PUBMED   37381775
  REMARK    GeneRIF: ETV6 fusions from insertions of exons 3-5 in pediatric
            hematologic malignancies.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Klubickova,N., Mosaieby,E., Ptakova,N., Trinquet,A., Lae,M.,
            Costes-Martineau,V. and Skalova,A.
  TITLE     High-grade non-intestinal type sinonasal adenocarcinoma with
            ETV6::NTRK3 fusion, distinct from secretory carcinoma by
            immunoprofile and morphology
  JOURNAL   Virchows Arch 483 (2), 187-195 (2023)
   PUBMED   37415052
  REMARK    GeneRIF: High-grade non-intestinal type sinonasal adenocarcinoma
            with ETV6::NTRK3 fusion, distinct from secretory carcinoma by
            immunoprofile and morphology.
REFERENCE   6  (residues 1 to 443)
  AUTHORS   Romana,S.P., Mauchauffe,M., Le Coniat,M., Chumakov,I., Le
            Paslier,D., Berger,R. and Bernard,O.A.
  TITLE     The t(12;21) of acute lymphoblastic leukemia results in a tel-AML1
            gene fusion
  JOURNAL   Blood 85 (12), 3662-3670 (1995)
   PUBMED   7780150
REFERENCE   7  (residues 1 to 443)
  AUTHORS   Golub,T.R., Barker,G.F., Bohlander,S.K., Hiebert,S.W., Ward,D.C.,
            Bray-Ward,P., Morgan,E., Raimondi,S.C., Rowley,J.D. and
            Gilliland,D.G.
  TITLE     Fusion of the TEL gene on 12p13 to the AML1 gene on 21q22 in acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 92 (11), 4917-4921 (1995)
   PUBMED   7761424
REFERENCE   8  (residues 1 to 443)
  AUTHORS   Buijs,A., Sherr,S., van Baal,S., van Bezouw,S., van der Plas,D.,
            Geurts van Kessel,A., Riegman,P., Lekanne Deprez,R., Zwarthoff,E.,
            Hagemeijer,A. et al.
  TITLE     Translocation (12;22) (p13;q11) in myeloproliferative disorders
            results in fusion of the ETS-like TEL gene on 12p13 to the MN1 gene
            on 22q11
  JOURNAL   Oncogene 10 (8), 1511-1519 (1995)
   PUBMED   7731705
  REMARK    Erratum:[Oncogene 1995 Aug 17;11(4):809]
REFERENCE   9  (residues 1 to 443)
  AUTHORS   Pencheva,B., Di Paola,J. and Porter,C.C.
  TITLE     ETV6-Related Thrombocytopenia and Predisposition to Leukemia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   33226740
REFERENCE   10 (residues 1 to 443)
  AUTHORS   Fainstein,E., Einat,M., Gokkel,E., Marcelle,C., Croce,C.M.,
            Gale,R.P. and Canaani,E.
  TITLE     Nucleotide sequence analysis of human abl and bcr-abl cDNAs
  JOURNAL   Oncogene 4 (12), 1477-1481 (1989)
   PUBMED   2687768
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007450.1, AC084430.13 and
            AC084358.19.
            
            Summary: This gene encodes an ETS family transcription factor. The
            product of this gene contains two functional domains: a N-terminal
            pointed (PNT) domain that is involved in protein-protein
            interactions with itself and other proteins, and a C-terminal
            DNA-binding domain. Gene knockout studies in mice suggest that it
            is required for hematopoiesis and maintenance of the developing
            vascular network. This gene is known to be involved in a large
            number of chromosomal rearrangements associated with leukemia and
            congenital fibrosarcoma. [provided by RefSeq, Sep 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4352443.353471.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..443
                     /product="transcription factor ETV6 isoform 3"
                     /note="ets variant gene 6 (TEL oncogene); TEL1 oncogene;
                     transcription factor ETV6; ETS-related protein Tel1;
                     ETV6-RUNX1 fusion protein"
                     /calculated_mol_wt=51952
     Region          47..114
                     /region_name="SAM_PNT-Tel_Yan"
                     /note="Sterile alpha motif (SAM)/Pointed domain of Tel/Yan
                     protein; cd08535"
                     /db_xref="CDD:176085"
     Site            order(54,76,79..81,83..84,87,89,91..92,95..96)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:176085"
     Site            order(66..71,98..100,102..103,106..107)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:176085"
     Region          329..415
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..443
                     /gene="ETV6"
                     /gene_synonym="TEL; TEL/ABL; THC5"
                     /coded_by="NM_001413914.1:607..1938"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:2120"
                     /db_xref="HGNC:HGNC:3495"
                     /db_xref="MIM:600618"
ORIGIN      
        1 mqqerisytp pespvpsyas stplhvpvpr alrmeedsir lpahlrlqpi ywsrddvaqw
       61 lkwaenefsl rpidsntfem ngkalllltk edfryrsphs gdvlyellqh ilkqrkpril
      121 fspffhpgns ihtqpevilh qnheedncvq rtprpsvdnv hhnpptiell hrsrspittn
      181 hrpspdpeqr plrspldnmi rrlspaeraq gprphqennh qesyplsvsp mennhcpass
      241 eshpkpsspr qestrviqlm pspimhplil nprhsvdfkq srlsedglhr egkpinlshr
      301 edlaymnhim vsvsppeeha mpigriadcr llwdyvyqll sdsryenfir wedkeskifr
      361 ivdpnglarl wgnhknrtnm tyekmsralr hyyklniirk epgqrllfrf mktpdeimsg
      421 rtdrlehles qeldeqiyqe dec
//
LOCUS       NP_001396236            2442 aa            linear   PRI 21-NOV-2025
DEFINITION  histone-lysine N-methyltransferase, H3 lysine-36 specific isoform e
            [Homo sapiens].
ACCESSION   NP_001396236
VERSION     NP_001396236.1
DBSOURCE    REFSEQ: accession NM_001409307.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2442)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2442)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   3  (residues 1 to 2442)
  AUTHORS   Conteduca,G., Cangelosi,D., Baldo,C., Arado,A., Testa,B.,
            Wagner,R.T., Robertson,K.D., Dequiedt,F., Fitzsimmons,L.,
            Malacarne,M., Filaci,G. and Coviello,D.A.
  TITLE     Impact of NSD1 Alternative Transcripts in Actin Filament Formation
            and Cellular Division Pathways in Fibroblasts
  JOURNAL   Genes (Basel) 15 (9), 1117 (2024)
   PUBMED   39336709
  REMARK    GeneRIF: Impact of NSD1 Alternative Transcripts in Actin Filament
            Formation and Cellular Division Pathways in Fibroblasts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2442)
  AUTHORS   Ren,Z., Yue,L., Hu,H.Y., Hou,X.L., Chen,W.Q., Tan,Y., Dong,Z. and
            Zhang,J.
  TITLE     Identification of Novel NSD1 variations in four Pediatric cases
            with sotos Syndrome
  JOURNAL   BMC Med Genomics 17 (1), 116 (2024)
   PUBMED   38684994
  REMARK    GeneRIF: Identification of Novel NSD1 variations in four Pediatric
            cases with sotos Syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2442)
  AUTHORS   Wang,X., Yeh,S., Wu,G., Hsu,C.L., Wang,L., Chiang,T., Yang,Y.,
            Guo,Y. and Chang,C.
  TITLE     Identification and characterization of a novel androgen receptor
            coregulator ARA267-alpha in prostate cancer cells
  JOURNAL   J Biol Chem 276 (44), 40417-40423 (2001)
   PUBMED   11509567
REFERENCE   6  (residues 1 to 2442)
  AUTHORS   Jaju,R.J., Fidler,C., Haas,O.A., Strickson,A.J., Watkins,F.,
            Clark,K., Cross,N.C., Cheng,J.F., Aplan,P.D., Kearney,L.,
            Boultwood,J. and Wainscoat,J.S.
  TITLE     A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in
            de novo childhood acute myeloid leukemia
  JOURNAL   Blood 98 (4), 1264-1267 (2001)
   PUBMED   11493482
REFERENCE   7  (residues 1 to 2442)
  AUTHORS   Lee,D.K., Duan,H.O. and Chang,C.
  TITLE     Androgen receptor interacts with the positive elongation factor
            P-TEFb and enhances the efficiency of transcriptional elongation
  JOURNAL   J Biol Chem 276 (13), 9978-9984 (2001)
   PUBMED   11266437
REFERENCE   8  (residues 1 to 2442)
  AUTHORS   Huang,N., vom Baur,E., Garnier,J.M., Lerouge,T., Vonesch,J.L.,
            Lutz,Y., Chambon,P. and Losson,R.
  TITLE     Two distinct nuclear receptor interaction domains in NSD1, a novel
            SET protein that exhibits characteristics of both corepressors and
            coactivators
  JOURNAL   EMBO J 17 (12), 3398-3412 (1998)
   PUBMED   9628876
REFERENCE   9  (residues 1 to 2442)
  AUTHORS   Ocansey,S., Cole,T.R.P., Rahman,N. and Tatton-Brown,K.
  TITLE     Sotos Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301652
REFERENCE   10 (residues 1 to 2442)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027314.5, AC008570.6 and
            AC146507.2.
            
            Summary: This gene encodes a protein containing a SET domain, 2
            LXXLL motifs, 3 nuclear translocation signals (NLSs), 4 plant
            homeodomain (PHD) finger regions, and a proline-rich region. The
            encoded protein enhances androgen receptor (AR) transactivation,
            and this enhancement can be increased further in the presence of
            other androgen receptor associated coregulators. This protein may
            act as a nucleus-localized, basic transcriptional factor and also
            as a bifunctional transcriptional regulator. Mutations of this gene
            have been associated with Sotos syndrome and Weaver syndrome. One
            version of childhood acute myeloid leukemia is the result of a
            cryptic translocation with the breakpoints occurring within nuclear
            receptor-binding Su-var, enhancer of zeste, and trithorax domain
            protein 1 on chromosome 5 and nucleoporin, 98-kd on chromosome 11.
            Multiple transcript variants encoding distinct isoforms have been
            identified for this gene. [provided by RefSeq, Sep 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2054439.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2442
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..2442
                     /product="histone-lysine N-methyltransferase, H3 lysine-36
                     specific isoform e"
                     /EC_number="2.1.1.357"
                     /note="androgen receptor-associated coregulator 267;
                     histone-lysine N-methyltransferase, H3 lysine-36 and H4
                     lysine-20 specific; H3-K36-HMTase; H4-K20-HMTase; lysine
                     N-methyltransferase 3B; NR-binding SET domain-containing
                     protein; androgen receptor coactivator 267 kDa protein;
                     androgen receptor-associated protein of 267 kDa; nuclear
                     receptor-binding SET domain-containing protein 1; nuclear
                     receptor SET domain-containing protein 1; histone-lysine
                     N-methyltransferase, H3 lysine-36 specific"
                     /calculated_mol_wt=268791
     Region          27..142
                     /region_name="PWWP_NSD1_rpt1"
                     /note="first PWWP domain found in nuclear receptor-binding
                     SET domain-containing protein 1 (NSD1) and similar
                     proteins; cd20161"
                     /db_xref="CDD:438989"
     Site            order(43,46,77)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438989"
     Site            44..47
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438989"
     Site            order(115..117,120..121)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438989"
     Region          <1140..1296
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          1254..1296
                     /region_name="PHD1_NSD1_2"
                     /note="PHD finger 1 found in nuclear receptor-binding SET
                     domain-containing protein NSD1 and NSD2; cd15648"
                     /db_xref="CDD:277118"
     Site            order(1254,1263..1267,1272,1290)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277118"
     Region          1338..1384
                     /region_name="PHD2_NSD1"
                     /note="PHD finger 2 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15650"
                     /db_xref="CDD:277120"
     Site            order(1338,1348..1352,1358,1379)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277120"
     Region          1385..1438
                     /region_name="PHD3_NSD1"
                     /note="PHD finger 3 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15653"
                     /db_xref="CDD:277123"
     Site            order(1385,1403..1407,1411,1433)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277123"
     Region          1455..1494
                     /region_name="PHD4_NSD1"
                     /note="PHD finger 4 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15656"
                     /db_xref="CDD:277126"
     Site            order(1455,1464..1468,1472,1489)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277126"
     Region          1501..1596
                     /region_name="PWWP_NSD1_rpt2"
                     /note="second PWWP domain found in nuclear
                     receptor-binding SET domain-containing protein 1 (NSD1)
                     and similar proteins; cd20164"
                     /db_xref="CDD:438992"
     Site            order(1513,1516,1544)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438992"
     Site            1514..1517
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438992"
     Region          1647..1685
                     /region_name="AWS"
                     /note="AWS domain; pfam17907"
                     /db_xref="CDD:465559"
     Region          1687..1828
                     /region_name="SET_NSD1"
                     /note="SET domain (including post-SET domain) found in
                     nuclear receptor-binding SET domain-containing protein 1
                     (NSD1) and similar proteins; cd19210"
                     /db_xref="CDD:380987"
     Site            order(1698..1700,1717,1727,1731,1740..1746,1763..1767,
                     1774..1776,1791,1802..1812,1814..1818,1827)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380987"
     Site            order(1698..1700,1740..1743,1763..1767,1804,1811,
                     1815..1818,1827)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380987"
     Site            order(1717,1727,1731,1742..1746,1774..1776,1791,
                     1802..1806)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:380987"
     Site            order(1769,1816,1818,1823)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380987"
     Region          1866..1908
                     /region_name="PHD5_NSD1"
                     /note="PHD finger 5 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15659"
                     /db_xref="CDD:277129"
     Site            order(1866,1875..1879,1885,1903)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277129"
     Region          1907..1956
                     /region_name="C5HCH"
                     /note="NSD Cys-His rich domain; pfam17982"
                     /db_xref="CDD:465605"
     Region          <1954..2320
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..2442
                     /gene="NSD1"
                     /gene_synonym="ARA267; KMT3B; SOTOS; SOTOS1; STO"
                     /coded_by="NM_001409307.1:291..7619"
                     /note="isoform e is encoded by transcript variant 10"
                     /db_xref="GeneID:64324"
                     /db_xref="HGNC:HGNC:14234"
                     /db_xref="MIM:606681"
ORIGIN      
        1 mlelpgtsss stsqelpfcq pkkkstplky evgdliwakf krrpwwpcri csdplinths
       61 kmkvsnrrpy rqyyveafgd pserawvagk aivmfegrhq feelpvlrrr gkqkekgyrh
      121 kvpqkilskw easvglaeqy dvpkgsknrk cipgsiklds eedmpfedct ndpesehdll
      181 lngclkslaf dsehsadeke kpcaksrark ssdnpkrtsv kkghiqfeah kderrgkipe
      241 nlglnfisgd isdtqasnel sriansltgs ntapgsflfs scgkntakke fetsngdsll
      301 glpegalisk csreknkpqr slvcgskvkl cyigagdeek rsdsisictt sddgssdldp
      361 iehssesdns vleipdafdr tenmlsmqkn ekikysrfaa tntrvkakqk plisnshtdh
      421 lmgctksaep gtetsqvnls dlkastlvhk pqsdftndal spkfnlsssi ssenslikgg
      481 aanqallhsk skqpkfrsik ckhkenpvma eppvineecs lkccssdtkg splasisksg
      541 kvdglkllnn mhektrdssd ietavvkhvl selkelsyrs lgedvsdsgt skpskpllfs
      601 sassqnhipi epdykfstll mmlkdmhdsk tkeqrlmtaq nlvsyrspgr gdcstnspvg
      661 vskvlvsggs thnsekkgdg tqnsanpsps ggdsalsgel saslpgllsd krdlpasgks
      721 rsdcvtrrnc grskpssklr dafsaqmvkn tvnrkalkte rkrklnqlps vtldavlqgd
      781 rerggslrgg aedpskedpl qimghltsed gdhfsdvhfd skvkqsdpgk isekglsfen
      841 gkgpeldsvm nsendelngv nqvvpkkrwq rlnqrrtkpr krmnrfkeke nsecafrvll
      901 psdpvqegrd efpehrtpsa sileeplteq nhadcldsag prlnvcdkss asigdmekep
      961 gipsltpqae lpepavrsek krlrkpskwl leyteeydqi fapkkkqkkv qeqvhkvssr
     1021 ceeesllarg rssaqnkqvd enslistkee ppvlereapf legplaqsel ggghaelpql
     1081 tlsvpvapev sprpalesee llvktpgnye skrqrkptkk llesndldpg fmpkkgdlgl
     1141 skkcyeaghl engitescat syskdfgggt tkifdkprkr krqrhaaakm qckkvkndds
     1201 skeipgsege lmphrtatsp ketveegveh dpgmpaskkm qgergggaal kenvcqncek
     1261 lgelllceaq ccgafhlecl gltemprgkf icnecrtesc tvtrarvqwr slgnlrllgs
     1321 skspasasqv agitgihtcf vckqsgedvk rcllplcgkf yheecvqkyp ptvmqnkgfr
     1381 cslhicitch aanpanvsas kgrlmrcvrc pvayhandfc laagskilas nsiicpnhft
     1441 prrgcrnheh vnvswcfvcs eggsllccds cpaafhrecl nidipegnwy cndckagkkp
     1501 hyreivwvkv gryrwwpaei chpravpsni dkmrhdvgef pvlffgsndy lwthqarvfp
     1561 ymegdvsskd kmgkgvdgty kkalqeaaar feelkaqkel rqlqedrknd kkpppykhik
     1621 vnrpigrvqi ftadlseipr cnckatdenp cgidsecinr mllyechptv cpaggrcqnq
     1681 cfskrqypev eifrtlqrgw glrtktdikk gefvneyvge lideeecrar iryaqehdit
     1741 nfymltldkd riidagpkgn yarfmnhccq pncetqkwsv ngdtrvglfa lsdikagtel
     1801 tfnynleclg ngktvckcga pncsgflgvr pknqpiatee kskkfkkkqq gkrrtqgeit
     1861 keredecfsc gdagqlvsck kpgcpkvyha dclnltkrpa gkwecpwhqc dicgkeaasf
     1921 cemcpssfck qhregmlfis kldgrlscte hdpcgpnple pgeireyvpp pvplppgpst
     1981 hlaeqstgma aqapkmsdkp padtnqmlsl skkalagtcq rpllperple rtdsrpqpld
     2041 kvrdlagsgt ksqslvssqr pldrppavag prpqlsdkps pvtspsssps vrsqplerpl
     2101 gtadprldks igaasprpqs lektsvptgl rlpppdrlli tsspkpqtsd rptdkphasl
     2161 sqrlpppekv lsavvqtlva kekalrpvdq ntqsknraal vmdlidltpr qkeraasphq
     2221 vtpqadekmp vlessswpas kglghmprav ekgcvsdplq tsgkaaapse dpwqavkslt
     2281 qarllsqppa kaflyepttq asgrasagae qtpgplsqsp glvkqakqmv ggqqlpalaa
     2341 ksgqsfrslg kapaslptee kklvtteqsp walgkassra glwpivagqt laqscwsags
     2401 tqtlaqtcws lgrgqdpkpe qntlpalnqa psshkcaese qk
//
LOCUS       NP_001400673             879 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform g [Homo sapiens].
ACCESSION   NP_001400673
VERSION     NP_001400673.1
DBSOURCE    REFSEQ: accession NM_001413744.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 879)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 879)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 879)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 879)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 879)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 879)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 879)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 879)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 879)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 879)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3721098.1,
                                           SRR14038192.908857.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2152719 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..879
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..879
                     /product="polyhomeotic-like protein 1 isoform g"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=92883
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          212..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          261..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          703..810
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          810..878
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(828..829,863..864,867..868,871)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(839..843,845..846,849..850,854,859)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..879
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413744.1:368..3007"
                     /note="isoform g is encoded by transcript variant 8"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq asinlattsa aqlisrsqsv
      121 sspsattltq svllgnttsp plnqsqaqmy lrpqlgnllq vnrtlgrnvp lasqlilmpn
      181 gavaavqqev psaqspgvha dadqvqnlav rnqqasaqgp qmqgstqkai ppgaspvssl
      241 sqassqalav aqassgatnq slnlsqaggg sgnsipgsmg pggggqahgg lgqlpssgmg
      301 ggscprkgtg vvqplpaaqt vtvsqgsqte aesaaakkae adgsgqqnvg mnltrtatpa
      361 psqtlissat ytqiqphsli qqqqqihlqq kqvviqqqia ihhqqqfqhr qsqllhtath
      421 lqlaqqqqqq qqqqqqqqqp qattltapqp pqvpptqqec pptlapgmtl apvqgtahvv
      481 kggattsspv vaqvpaafym qsvhlpgkpq tlavkrkads eeerddvstl gsmlpakasp
      541 vaespkvmde ksslgekaes vanvnantps selvaltpap svppptlamv srqmgdskpp
      601 qaivkpqilt hiiegfviqe gaepfpvgcs qllkesekpl qtglptglte nqsggplgvd
      661 spsaeldkka nllkceycgk yapaeqfrgs krfcsmtcak rynvscshqf rlkrkkmkef
      721 qeanyarvrr rgprrsssdi arakiqgkch rgqedssrgs dnssydeals ptspgplsvr
      781 aghgerdlgn pntapptpel hginpvflss npsrwsveev yefiaslqgc qeiaeefrsq
      841 eidgqallll keehlmsamn iklgpalkic akinvlket
//
LOCUS       NP_001427248             182 aa            linear   PRI 21-NOV-2025
DEFINITION  T-cell surface glycoprotein CD3 gamma chain precursor [Homo
            sapiens].
ACCESSION   NP_001427248 XP_006719004 XP_054226470
VERSION     NP_001427248.1
DBSOURCE    REFSEQ: accession NM_001440319.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Li,N., Ren,P., Wang,J., Zhu,X., Qiao,X., Zeng,Z., Ye,T., Wang,S.,
            Meng,Z., Gan,H., Liu,S., Sun,Y., Zhu,X., Dou,G. and Gu,R.
  TITLE     Immune-Related Molecules CD3G and FERMT3: Novel Biomarkers
            Associated with Sepsis
  JOURNAL   Int J Mol Sci 25 (2), 749 (2024)
   PUBMED   38255822
  REMARK    GeneRIF: Immune-Related Molecules CD3G and FERMT3: Novel Biomarkers
            Associated with Sepsis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Dong,D., Zheng,L., Lin,J., Zhang,B., Zhu,Y., Li,N., Xie,S.,
            Wang,Y., Gao,N. and Huang,Z.
  TITLE     Structural basis of assembly of the human T cell receptor-CD3
            complex
  JOURNAL   Nature 573 (7775), 546-552 (2019)
   PUBMED   31461748
  REMARK    Erratum:[Nature. 2021 Feb;590(7846):E52. doi:
            10.1038/s41586-021-03245-4. PMID: 33526937]
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Muro,R., Takayanagi,H. and Nitta,T.
  TITLE     T cell receptor signaling for gammadeltaT cell development
  JOURNAL   Inflamm Regen 39, 6 (2019)
   PUBMED   30976362
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Gaud,G., Lesourne,R. and Love,P.E.
  TITLE     Regulatory mechanisms in T cell receptor signalling
  JOURNAL   Nat Rev Immunol 18 (8), 485-497 (2018)
   PUBMED   29789755
  REMARK    Review article
REFERENCE   6  (residues 1 to 182)
  AUTHORS   Lanier,L.L., Chang,C., Spits,H. and Phillips,J.H.
  TITLE     Expression of cytoplasmic CD3 epsilon proteins in activated human
            adult natural killer (NK) cells and CD3 gamma, delta, epsilon
            complexes in fetal NK cells. Implications for the relationship of
            NK and T lymphocytes
  JOURNAL   J Immunol 149 (6), 1876-1880 (1992)
   PUBMED   1387664
REFERENCE   7  (residues 1 to 182)
  AUTHORS   Arnaiz-Villena,A., Timon,M., Corell,A., Perez-Aciego,P.,
            Martin-Villa,J.M. and Regueiro,J.R.
  TITLE     Brief report: primary immunodeficiency caused by mutations in the
            gene encoding the CD3-gamma subunit of the T-lymphocyte receptor
  JOURNAL   N Engl J Med 327 (8), 529-533 (1992)
   PUBMED   1635567
REFERENCE   8  (residues 1 to 182)
  AUTHORS   Cenciarelli,C., Hou,D., Hsu,K.C., Rellahan,B.L., Wiest,D.L.,
            Smith,H.T., Fried,V.A. and Weissman,A.M.
  TITLE     Activation-induced ubiquitination of the T cell antigen receptor
  JOURNAL   Science 257 (5071), 795-797 (1992)
   PUBMED   1323144
REFERENCE   9  (residues 1 to 182)
  AUTHORS   Letourneur,F. and Klausner,R.D.
  TITLE     A novel di-leucine motif and a tyrosine-based motif independently
            mediate lysosomal targeting and endocytosis of CD3 chains
  JOURNAL   Cell 69 (7), 1143-1157 (1992)
   PUBMED   1535555
REFERENCE   10 (residues 1 to 182)
  AUTHORS   Arnaiz-Villena,A., Perez-Aciego,P., Ballestin,C., Sotelo,T.,
            Perez-Seoane,C., Martin-Villa,J.M. and Regueiro,J.R.
  TITLE     Biochemical basis of a novel T lymphocyte receptor immunodeficiency
            by immunohistochemistry. A possible CD3 gamma abnormality
  JOURNAL   Lab Invest 64 (5), 675-681 (1991)
   PUBMED   1709425
  REMARK    GeneRIF: Protein level controlled by OTHER KINASES PROTEINS
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001582.4.
            
            On or before May 19, 2025 this sequence version replaced
            XP_006719004.1, XP_054226470.1.
            
            Summary: The protein encoded by this gene is the CD3-gamma
            polypeptide, which together with CD3-epsilon, -delta and -zeta, and
            the T-cell receptor alpha/beta and gamma/delta heterodimers, forms
            the T-cell receptor-CD3 complex. This complex plays an important
            role in coupling antigen recognition to several intracellular
            signal-transduction pathways. The genes encoding the epsilon, gamma
            and delta polypeptides are located in the same cluster on
            chromosome 11. Defects in this gene are associated with T cell
            immunodeficiency. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2589335.1,
                                           SRR14038194.2344627.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..182
                     /product="T-cell surface glycoprotein CD3 gamma chain
                     precursor"
                     /note="CD3g antigen, gamma polypeptide (TiT3 complex);
                     T-cell receptor T3 gamma chain; T-cell antigen receptor
                     complex, gamma subunit of T3; T-cell surface glycoprotein
                     CD3 gamma chain; CD3g molecule, epsilon (CD3-TCR complex);
                     CD3g molecule, gamma (CD3-TCR complex)"
                     /calculated_mol_wt=18222
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2266
     mat_peptide     23..182
                     /product="T-cell surface glycoprotein CD3 gamma chain.
                     /id=PRO_0000014615"
                     /note="propagated from UniProtKB/Swiss-Prot (P09693.1)"
                     /calculated_mol_wt=18222
     Region          35..105
                     /region_name="IgC1_CD3_gamma_delta"
                     /note="Immunoglobulin (Ig)-like domain of Cluster of
                     Differentiation (CD) 3 gamma and delta chains; member of
                     the C1-set of IgSF domains; cd07691"
                     /db_xref="CDD:409488"
     Site            order(35..36,38,84,96..98,100..104)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409488"
     Region          35..39
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409488"
     Region          41..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409488"
     Region          52..56
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409488"
     Site            52
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:8636209; propagated from
                     UniProtKB/Swiss-Prot (P09693.1)"
     Region          58..60
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409488"
     Region          62..65
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409488"
     Region          70..76
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409488"
     Region          82..88
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409488"
     Site            92
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:8636209; propagated from
                     UniProtKB/Swiss-Prot (P09693.1)"
     Region          94..102
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409488"
     Site            117..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P09693.1)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:2540970,
                     ECO:0000269|PubMed:3112151; propagated from
                     UniProtKB/Swiss-Prot (P09693.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000269|PubMed:2540970,
                     ECO:0000269|PubMed:3112151, ECO:0000269|PubMed:8187769;
                     propagated from UniProtKB/Swiss-Prot (P09693.1)"
     Region          153..154
                     /region_name="Di-leucine motif.
                     /evidence=ECO:0000269|PubMed:8187769"
                     /note="propagated from UniProtKB/Swiss-Prot (P09693.1)"
     Region          157..176
                     /region_name="ITAM"
                     /note="Immunoreceptor tyrosine-based activation motif;
                     pfam02189"
                     /db_xref="CDD:426646"
     CDS             1..182
                     /gene="CD3G"
                     /gene_synonym="CD3-GAMMA; CD3GAMMA; IMD17; T3G"
                     /coded_by="NM_001440319.1:81..629"
                     /db_xref="GeneID:917"
                     /db_xref="HGNC:HGNC:1675"
                     /db_xref="MIM:186740"
ORIGIN      
        1 meqgkglavl ilaiillqgt laqsikgnhl vkvydyqedg svlltcdaea knitwfkdgk
       61 migfltedkk kwnlgsnakd prgmyqckgs qnkskplqvy yrmcqnciel naatisgflf
      121 aeivsifvla vgvyfiagqd gvrqsrasdk qtllpndqly qplkdreddq yshlqgnqlr
      181 rn
//
LOCUS       NP_001427336             852 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 5 precursor [Homo
            sapiens].
ACCESSION   NP_001427336
VERSION     NP_001427336.1
DBSOURCE    REFSEQ: accession NM_001440407.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 852)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 852)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 852)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 852)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 852)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 852)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 852)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 852)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 852)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 852)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3, AP004147.3 and
            AP001929.5.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..852
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..852
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     5 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=93535
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..388
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Region          <388..681
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     CDS             1..852
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440407.1:191..2749"
                     /note="isoform 5 precursor is encoded by transcript
                     variant 9"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk aaelgmvsay
      241 ytyiftnlef slqrmdslvd drvnilgfsi fnqshaffqe faqslnqswq encdhvpftg
      301 palssallfd avyavvtavq elnrsqeigv kplscgsaqi wqhgtslmny lrmveleglt
      361 ghiefnskgq rsnyalkilq ftrngfrqka dlavagltit aerekvidfs kpfmtlgisi
      421 lyrvhmgrkp gyfsfldpfs pgvwlfmlla ylavscvlfl varltpyewy sphpcaqgrc
      481 nllvnqyslg nslwfpvggf mqqgstiapr alstrcvsgv wwaftliiis sytanlaafl
      541 tvqrmdvpie svddladqta ieygtihggs smtffqnsry qtyqrmwnym yskqpsvfvk
      601 steegiarvl nsnyaflles tmneyyrqrn cnltqiggll dtkgygigmp vgsvfrdefd
      661 lailqlqenn rleilkrkww eggkcpkeed hrakglgmen iggifvvlic glivaifmam
      721 leflwtlrhs eatevsvcqe mvtelrsiil cqdsihprrr raavppprpp ipeerrprgt
      781 atlsngklcg agepdqlaqr laqeaalvar gcthirvcpe crrfqglrar psparseesl
      841 ewekttnsse pe
//
LOCUS       NP_001428155             443 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 9 [Homo sapiens].
ACCESSION   NP_001428155
VERSION     NP_001428155.1
DBSOURCE    REFSEQ: accession NM_001441226.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 443)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 443)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 443)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 443)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 443)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.1586016.1,
                                           SRR14038195.183104.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..443
                     /product="calcium uptake protein 1, mitochondrial isoform
                     9"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=50454
     Region          189..408
                     /region_name="EFh_MICU1"
                     /note="EF-hand, calcium binding motif, found in calcium
                     uptake protein 1, mitochondrial (MICU1) and similar
                     proteins; cd16173"
                     /db_xref="CDD:320081"
     Region          189..218
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Site            order(191,343,346,349..350,352,370)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:320081"
     Site            order(198,200,202,209,388,390,392,399)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320081"
     Region          244..274
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          342..371
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          379..408
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     CDS             1..443
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001441226.1:136..1467"
                     /note="isoform 9 is encoded by transcript variant 13"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mmvaflgasa vtastgllwk rahaesppcv dnlksdigdk gknkdegdvc nhekktadla
       61 phpeekkkkr sgfrdrkvme yenrirayst pdkifryfat lkvisepgea evfmtpedfv
      121 rsitpnekqp ehlgldqyii krfdgkkisq erekfadegs ifytlgecgl isfsdyiflt
      181 tvlstpqrnf eiafkmfdln gdgevdmeef eqvqsiirsq tsmgmrhrdr pttgntlksg
      241 lcsalttyff gadlkgklti knflefqrkl qhdvlklefe rhdpvdgrit erqfggmlla
      301 ysgvqskklt amqrqlkkhf kegkgltfqe venfftflkn indvdtalsf yhmagasldk
      361 vtmqqvartv akvelsdhvc dvvfalfdcd gngelsnkef vsimkqrlmr glekpkdmgf
      421 trlmqamwkc aqetawdfal pkq
//
LOCUS       NP_001424296             728 aa            linear   PRI 21-NOV-2025
DEFINITION  MAP/microtubule affinity-regulating kinase 3 isoform j [Homo
            sapiens].
ACCESSION   NP_001424296 XP_016876780 XP_054232032
VERSION     NP_001424296.1
DBSOURCE    REFSEQ: accession NM_001437367.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 728)
  AUTHORS   Aparicio-Bautista,D.I., Jimenez-Ortega,R.F., Becerra-Cervera,A.,
            Aquino-Galvez,A., de Leon-Suarez,V.P., Casas-Avila,L., Salmeron,J.,
            Hidalgo-Bravo,A., Rivera-Paredez,B. and Velazquez-Cruz,R.
  TITLE     Interaction between MARK3 (rs11623869), PLCB4 (rs6086746) and
            GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women
  JOURNAL   Front Endocrinol (Lausanne) 15, 1392063 (2024)
   PUBMED   38715801
  REMARK    GeneRIF: Interaction between MARK3 (rs11623869), PLCB4 (rs6086746)
            and GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 728)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 728)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 728)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 728)
  AUTHORS   Li,M.G., Katsura,K., Nomiyama,H., Komaki,K., Ninomiya-Tsuji,J.,
            Matsumoto,K., Kobayashi,T. and Tamura,S.
  TITLE     Regulation of the interleukin-1-induced signaling pathways by a
            novel member of the protein phosphatase 2C family (PP2Cepsilon)
  JOURNAL   J Biol Chem 278 (14), 12013-12021 (2003)
   PUBMED   12556533
REFERENCE   7  (residues 1 to 728)
  AUTHORS   Sun,T.Q., Lu,B., Feng,J.J., Reinhard,C., Jan,Y.N., Fantl,W.J. and
            Williams,L.T.
  TITLE     PAR-1 is a Dishevelled-associated kinase and a positive regulator
            of Wnt signalling
  JOURNAL   Nat Cell Biol 3 (7), 628-636 (2001)
   PUBMED   11433294
REFERENCE   8  (residues 1 to 728)
  AUTHORS   Peng,C.Y., Graves,P.R., Ogg,S., Thoma,R.S., Byrnes,M.J. 3rd, Wu,Z.,
            Stephenson,M.T. and Piwnica-Worms,H.
  TITLE     C-TAK1 protein kinase phosphorylates human Cdc25C on serine 216 and
            promotes 14-3-3 protein binding
  JOURNAL   Cell Growth Differ 9 (3), 197-208 (1998)
   PUBMED   9543386
REFERENCE   9  (residues 1 to 728)
  AUTHORS   Ono,T., Kawabe,T., Sonta,S. and Okamoto,T.
  TITLE     Assignment of MARK3 alias KP78 to human chromosome band 14q32.3 by
            in situ hybridization
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 101-102 (1997)
   PUBMED   9533022
REFERENCE   10 (residues 1 to 728)
  AUTHORS   Meller,N., Liu,Y.C., Collins,T.L., Bonnefoy-Berard,N., Baier,G.,
            Isakov,N. and Altman,A.
  TITLE     Direct interaction between protein kinase C theta (PKC theta) and
            14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition
            of PKC theta translocation and function
  JOURNAL   Mol Cell Biol 16 (10), 5782-5791 (1996)
   PUBMED   8816492
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133367.4 and KF456011.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_016876780.1, XP_054232032.1.
            
            Summary: The protein encoded by this gene is activated by
            phosphorylation and in turn is involved in the phosphorylation of
            tau proteins MAP2 and MAP4. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1503283.1,
                                           SRR14038193.3535159.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.32-q32.33"
     Protein         1..728
                     /product="MAP/microtubule affinity-regulating kinase 3
                     isoform j"
                     /EC_number="2.7.11.1"
                     /note="EMK-2; C-TAK1; ELKL motif kinase 2; protein kinase
                     STK10; ser/Thr protein kinase PAR-1; cdc25C-associated
                     protein kinase 1; MAP/microtubule affinity-regulating
                     kinase 3; serine/threonine-protein kinase p78"
                     /calculated_mol_wt=81554
     Region          55..307
                     /region_name="STKc_MARK"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     MAP/microtubule affinity-regulating kinases; cd14072"
                     /db_xref="CDD:270974"
     Site            order(62..66,70,83,85,116,132..135,139,141..142,144,
                     177..178,180,182..183,185,195..196,199,212..217,219,
                     249..252,254)
                     /site_type="active"
                     /db_xref="CDD:270974"
     Site            order(62..65,70,83,85,116,132..135,139,182..183,185,
                     195..196)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270974"
     Site            order(66,139,141,177..178,180,182,199,213..217,219)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270974"
     Site            195..217
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270974"
     Region          325..367
                     /region_name="UBA_MARK3_4"
                     /note="UBA domain found in MAP/microtubule
                     affinity-regulating kinase MARK3, MARK4, and similar
                     proteins; cd14407"
                     /db_xref="CDD:270590"
     Region          629..726
                     /region_name="MARK1-3_C"
                     /note="C-terminal, kinase associated domain 1 (KA1), a
                     phospholipid binding domain, of microtubule
                     affinity-regulating kinases 1-3; cd12196"
                     /db_xref="CDD:213381"
     Site            order(631,634,704,706..707)
                     /site_type="other"
                     /note="putative phospholipid binding site [chemical
                     binding]"
                     /db_xref="CDD:213381"
     CDS             1..728
                     /gene="MARK3"
                     /gene_synonym="CTAK1; KP78; Par-1a; PAR1A; VIPB"
                     /coded_by="NM_001437367.1:616..2802"
                     /note="isoform j is encoded by transcript variant 10"
                     /db_xref="GeneID:4140"
                     /db_xref="HGNC:HGNC:6897"
                     /db_xref="MIM:602678"
ORIGIN      
        1 mstrtplptv nerdtenhts hgdgrqevts rtsrsgarcr nsiascadeq phignyrllk
       61 tigkgnfakv klarhiltgr evaikiidkt qlnptslqkl frevrimkil nhpnivklfe
      121 vietektlyl imeyasggev fdylvahgrm kekearskfr qivsavqych qkrivhrdlk
      181 aenllldadm nikiadfgfs neftvggkld tfcgsppyaa pelfqgkkyd gpevdvwslg
      241 vilytlvsgs lpfdgqnlke lrervlrgky ripfymstdc enllkrflvl npikrgtleq
      301 imkdrwinag heedelkpfv epeldisdqk ridimvgmgy sqeeiqesls kmkydeitat
      361 ylllgrksse vrpssdlnns tgqsphhkvq rsvsssqkqr rysdhagpai psvvaypkrs
      421 qtstadsdlk edgissrkss gsavggkgia paspmlgnas npnkadiper kksstvpssn
      481 tasggmtrrn tyvcsertta drhsviqngk enstipdqrt pvasthsiss aatpdrirfp
      541 rgtasrstfh gqprerrtat yngppaspsl sheatplsqt rsrgstnlfs kltskltrrl
      601 pteyerngry egssrnvsae qkdenkeakp rslrftwsmk ttssmdpgdm mreirkvlda
      661 nncdyeqrer fllfcvhgdg haenlvqwem evcklprlsl ngvrfkrisg tsiafknias
      721 kianelkl
//
LOCUS       NP_001397635             903 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 1 isoform 12 [Homo sapiens].
ACCESSION   NP_001397635 XP_005261001
VERSION     NP_001397635.1
DBSOURCE    REFSEQ: accession NM_001410706.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 903)
  AUTHORS   Chatterjee,M., Saha,S., Dutta,N., Sinha,S. and Mukhopadhyay,K.
  TITLE     Kainate receptor subunit 1 (GRIK1) risk variants and GRIK1
            deficiency were detected in the Indian ADHD probands
  JOURNAL   Sci Rep 12 (1), 18449 (2022)
   PUBMED   36323684
  REMARK    GeneRIF: Kainate receptor subunit 1 (GRIK1) risk variants and GRIK1
            deficiency were detected in the Indian ADHD probands.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 903)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   3  (residues 1 to 903)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   4  (residues 1 to 903)
  AUTHORS   Hirbec,H., Francis,J.C., Lauri,S.E., Braithwaite,S.P., Coussen,F.,
            Mulle,C., Dev,K.K., Coutinho,V., Meyer,G., Isaac,J.T.,
            Collingridge,G.L. and Henley,J.M.
  TITLE     Rapid and differential regulation of AMPA and kainate receptors at
            hippocampal mossy fibre synapses by PICK1 and GRIP
  JOURNAL   Neuron 37 (4), 625-638 (2003)
   PUBMED   12597860
  REMARK    Erratum:[Neuron. 2003 May 22;38(4):673. Couthino V [corrected to
            Coutinho V]]
REFERENCE   5  (residues 1 to 903)
  AUTHORS   Barbon,A. and Barlati,S.
  TITLE     Genomic organization, proposed alternative splicing mechanisms, and
            RNA editing structure of GRIK1
  JOURNAL   Cytogenet Cell Genet 88 (3-4), 236-239 (2000)
   PUBMED   10828597
REFERENCE   6  (residues 1 to 903)
  AUTHORS   Bortolotto,Z.A., Clarke,V.R., Delany,C.M., Parry,M.C., Smolders,I.,
            Vignes,M., Ho,K.H., Miu,P., Brinton,B.T., Fantaske,R., Ogden,A.,
            Gates,M., Ornstein,P.L., Lodge,D., Bleakman,D. and
            Collingridge,G.L.
  TITLE     Kainate receptors are involved in synaptic plasticity
  JOURNAL   Nature 402 (6759), 297-301 (1999)
   PUBMED   10580501
REFERENCE   7  (residues 1 to 903)
  AUTHORS   Clarke,V.R., Ballyk,B.A., Hoo,K.H., Mandelzys,A., Pellizzari,A.,
            Bath,C.P., Thomas,J., Sharpe,E.F., Davies,C.H., Ornstein,P.L.,
            Schoepp,D.D., Kamboj,R.K., Collingridge,G.L., Lodge,D. and
            Bleakman,D.
  TITLE     A hippocampal GluR5 kainate receptor regulating inhibitory synaptic
            transmission
  JOURNAL   Nature 389 (6651), 599-603 (1997)
   PUBMED   9335499
REFERENCE   8  (residues 1 to 903)
  AUTHORS   Nutt,S.L. and Kamboj,R.K.
  TITLE     RNA editing of human kainate receptor subunits
  JOURNAL   Neuroreport 5 (18), 2625-2629 (1994)
   PUBMED   7696618
REFERENCE   9  (residues 1 to 903)
  AUTHORS   Roche,K.W., Raymond,L.A., Blackstone,C. and Huganir,R.L.
  TITLE     Transmembrane topology of the glutamate receptor subunit GluR6
  JOURNAL   J Biol Chem 269 (16), 11679-11682 (1994)
   PUBMED   8163463
REFERENCE   10 (residues 1 to 903)
  AUTHORS   Gregor,P., O'Hara,B.F., Yang,X. and Uhl,G.R.
  TITLE     Expression and novel subunit isoforms of glutamate receptor genes
            GluR5 and GluR6
  JOURNAL   Neuroreport 4 (12), 1343-1346 (1993)
   PUBMED   8260617
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000236.2, AP000237.3,
            AP000238.2 and AP000239.2.
            
            On Aug 15, 2022 this sequence version replaced XP_005261001.1.
            
            Summary: Glutamate receptors are the predominant excitatory
            neurotransmitter receptors in the mammalian brain and are activated
            in a variety of normal neurophysiologic processes. This gene
            product belongs to the kainate family of glutamate receptors, which
            are composed of four subunits and function as ligand-activated ion
            channels. The subunit encoded by this gene is subject to RNA
            editing (CAG->CGG; Q->R) within the second transmembrane domain,
            which is thought to alter the properties of ion flow. Alternative
            splicing, resulting in transcript variants encoding different
            isoforms, has been noted for this gene. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.785558.1,
                                           SRR14372080.4462471.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            undergoes RNA editing :: PMID: 7696618, 10828597
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..903
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..903
                     /product="glutamate receptor ionotropic, kainate 1 isoform
                     12"
                     /note="excitatory amino acid receptor 3; glutamate
                     receptor 5; glutamate receptor ionotropic, kainate 1;
                     GluK1(del_e2)"
                     /calculated_mol_wt=102124
     Region          38..416
                     /region_name="PBP1_iGluR_Kainate"
                     /note="N-terminal leucine-isoleucine-valine binding
                     protein (LIVBP)-like domain of the kainate receptors;
                     cd06382"
                     /db_xref="CDD:380605"
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            order(88..90,94,125,177,180,184,187,190..191,201..204)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380605"
     Site            276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            379
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            413
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            424
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Region          431..800
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            431
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            546
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            562..582
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P39086.1)"
     Site            639..659
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P39086.1)"
     Site            710
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P39086.1)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P39086.1)"
     Site            751
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39086.1)"
     Site            820..840
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P39086.1)"
     CDS             1..903
                     /gene="GRIK1"
                     /gene_synonym="EAA3; EEA3; GLR5; GluK1; gluR-5; GLUR5"
                     /coded_by="NM_001410706.1:497..3208"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS93084.1"
                     /db_xref="GeneID:2897"
                     /db_xref="HGNC:HGNC:4579"
                     /db_xref="MIM:138245"
ORIGIN      
        1 mehgtllaqp glwtrdtswa llyflcyilp qtapqvlrig gifetvenep vnveelafkf
       61 avtsinrnrt lmpnttltyd iqrinlfdsf easrracdql algvaalfgp shsssvsavq
      121 sicnalevph iqtrwkhpsv dnkdlfyinl ypdyaaisra ildlvlyynw ktvtvvyeds
      181 tglirlqeli kapsryniki kirqlpsgnk dakpllkemk kgkefyvifd cshetaaeil
      241 kqilfmgmmt eyyhyffttl dlfaldlely rysgvnmtgf rllnidnphv ssiiekwsme
      301 rlqapprpet glldgmmtte aalmydavym vaiashrasq ltvsslqchr hkpwrlgprf
      361 mnlikearwd gltghitfnk tnglrkdfdl diislkeegt ekigiwnsns glnmtdsnkd
      421 kssnitdsla nrtlivttil eepyvmyrks dkplygndrf egycldllke lsnilgfiyd
      481 vklvpdgkyg aqndkgewng mvkelidhra dlavapltit yvrekvidfs kpfmtlgisi
      541 lyrkpngtnp gvfsflnpls pdiwmyvlla clgvscvlfv iarftpyewy nphpcnpdsd
      601 vvennftlln sfwfgvgalm qqgselmpka lstrivggiw wfftliiiss ytanlaaflt
      661 vermespids addlakqtki eygavrdgst mtffkkskis tyekmwafms srqqtalvrn
      721 sdegiqrvlt tdyallmest sieyvtqrnc nltqigglid skgygvgtpi gspyrdkiti
      781 ailqlqeegk lhmmkekwwr gngcpeednk easalgveni ggifivlaag lvlsvfvaig
      841 efiyksrknn dieqafcffy glqckqthpt nstsgttlst dlecgklire ergirkqssv
      901 htv
//
LOCUS       NP_001393920             664 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform A [Homo sapiens].
ACCESSION   NP_001393920
VERSION     NP_001393920.1
DBSOURCE    REFSEQ: accession NM_001406991.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 664)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 664)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 664)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 664)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 664)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 664)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 664)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 664)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355388.30 and AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3133649.1,
                                           SRR14038194.1003159.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154405, SAMEA2155550
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..664
                     /product="lamin isoform A"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=74009
     mat_peptide     1..661
                     /product="Prelamin-A/C. /id=PRO_0000398835"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
                     /calculated_mol_wt=73808
     mat_peptide     1..646
                     /product="Lamin-A/C. /id=PRO_0000063810"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
                     /calculated_mol_wt=72225
     Region          1..130
                     /region_name="Interaction with MLIP.
                     /evidence=ECO:0000269|PubMed:21498514"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          1..33
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          30..386
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Site            32
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          34..70
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          71..80
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            78
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          81..218
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            108
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            114
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            123
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            135
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            155
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            171
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            180
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            201
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            208
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          219..242
                     /region_name="Linker 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          243..383
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          259..331
                     /region_name="Necessary and sufficient for the interaction
                     with IFFO1. /evidence=ECO:0000269|PubMed:31548606"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            265
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            266
                     /site_type="other"
                     /note="Heptad change of phase; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            270
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATR.
                     /evidence=ECO:0000269|PubMed:37832547; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            311
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            316
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            325
                     /site_type="other"
                     /note="Stutter. /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            330
                     /site_type="other"
                     /note="Heptad change of phase; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            341
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          384..664
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          384..442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:37788673,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATR.
                     /evidence=ECO:0000269|PubMed:37788673,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:24741066, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          417..422
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            417
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          434..541
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     Site            450
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            457
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            486
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48679; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48679; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            546
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          552..576
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          598..619
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            625
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:26237509; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            628
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:26237509; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            632
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            646..647
                     /site_type="cleavage"
                     /note="Cleavage, by endoprotease; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            661
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000269|PubMed:8175923,
                     ECO:0000269|PubMed:9030603; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     CDS             1..664
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406991.1:315..2309"
                     /note="isoform A is encoded by transcript variant 9"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 metpsqrrat rsgaqasstp lsptritrlq ekedlqelnd rlavyidrvr sletenaglr
       61 lriteseevv srevsgikaa yeaelgdark tldsvakera rlqlelskvr eefkelkarn
      121 tkkegdliaa qarlkdleal lnskeaalst alsekrtleg elhdlrgqva kleaalgeak
      181 kqlqdemlrr vdaenrlqtm keeldfqkni yseelretkr rhetrlveid ngkqrefesr
      241 ladalqelra qhedqveqyk kelektysak ldnarqsaer nsnlvgaahe elqqsririd
      301 slsaqlsqlq kqlaakeakl rdledslare rdtsrrllae keremaemra rmqqqldeyq
      361 elldiklald meihayrkll egeeerlrls psptsqrsrg rasshssqtq gggsvtkkrk
      421 lestesrssf sqhartsgrv aveevdeegk fvrlrnksne dqsmgnwqik rqngddpllt
      481 yrfppkftlk agqvvtiwaa gagathsppt dlvwkaqntw gcgnslrtal instgeevam
      541 rklvrsvtvv eddededgdd llhhhhgshc sssgdpaeyn lrsrtvlcgt cgqpadkasa
      601 sgsgaqvggp issgssassv tvtrsyrsvg gsgggsfgdn lvtrsyllgn ssprtqspqn
      661 csim
//
LOCUS       NP_001400253             162 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 18 [Homo sapiens].
ACCESSION   NP_001400253
VERSION     NP_001400253.1
DBSOURCE    REFSEQ: accession NM_001413324.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 162)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 162)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 162)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 162)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 162)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 162)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 162)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.295632.1,
                                           SRR3476690.691541.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..162
                     /product="RNA-binding Raly-like protein isoform 18"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=18457
     CDS             1..162
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413324.1:98..586"
                     /note="isoform 18 is encoded by transcript variant 50"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtmykskrrh qryinmagep kpyrpkpgnk rplsalyrle skepflsvgg yvfdydyyrd
       61 dfynrlfdyh grvpppprav iplkrprvav tttrrgkgvf smkggsrsta sgstgsklks
      121 delqtikkel tqiktkidsl lgrlekiekq qkaeavstdk vi
//
LOCUS       NP_001428089             375 aa            linear   PRI 21-NOV-2025
DEFINITION  urokinase-type plasminogen activator isoform 4 preprotprotein
            precursor [Homo sapiens].
ACCESSION   NP_001428089
VERSION     NP_001428089.1
DBSOURCE    REFSEQ: accession NM_001441160.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Li,D., Ding,C., Huang,F., Chang,M., Lu,Z., Li,G., Li,Y., Gao,H. and
            Sun,F.
  TITLE     Bioinformatics Analysis of the Expression and Prognostic Value of
            PLAU Gene in Wilms' Tumor
  JOURNAL   Anticancer Res 44 (9), 3829-3842 (2024)
   PUBMED   39197889
  REMARK    GeneRIF: Bioinformatics Analysis of the Expression and Prognostic
            Value of PLAU Gene in Wilms' Tumor.
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Guo,J., Wang,H., Huang,C., Lai,C., Shang,W., Luo,S. and Chen,L.
  TITLE     PLAU, transcriptionally negatively regulated by GATA6, promotes
            lung squamous carcinoma cell proliferation and migration
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (5), 119744 (2024)
   PUBMED   38702016
  REMARK    GeneRIF: PLAU, transcriptionally negatively regulated by GATA6,
            promotes lung squamous carcinoma cell proliferation and migration.
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Cui,X., Sun,H., Liu,X., Bai,Y., Bai,Y., Cui,Y., Wang,B., Zhang,S.
            and Li,X.
  TITLE     PLAU promotes cell proliferation and migration of head and neck
            cancer via STAT3 signaling pathway
  JOURNAL   Exp Cell Res 438 (2), 114056 (2024)
   PUBMED   38663475
  REMARK    GeneRIF: PLAU promotes cell proliferation and migration of head and
            neck cancer via STAT3 signaling pathway.
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Cetinsoy,O., Anyanwu,I., Krishnanand,H., Natarajan,G.,
            Ramachandran,N., Thomas,A. and Brookes,K.J.
  TITLE     Gene Association Study of the Urokinase Plasminogen Activator and
            Its Receptor Gene in Alzheimer's Disease
  JOURNAL   J Alzheimers Dis 99 (1), 241-250 (2024)
   PUBMED   38669542
  REMARK    GeneRIF: Gene Association Study of the Urokinase Plasminogen
            Activator and Its Receptor Gene in Alzheimer's Disease.
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Mekkawy,A.H., Pourgholami,M.H. and Morris,D.L.
  TITLE     Involvement of urokinase-type plasminogen activator system in
            cancer: an overview
  JOURNAL   Med Res Rev 34 (5), 918-956 (2014)
   PUBMED   24549574
  REMARK    Review article
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Naldini,L., Tamagnone,L., Vigna,E., Sachs,M., Hartmann,G.,
            Birchmeier,W., Daikuhara,Y., Tsubouchi,H., Blasi,F. and
            Comoglio,P.M.
  TITLE     Extracellular proteolytic cleavage by urokinase is required for
            activation of hepatocyte growth factor/scatter factor
  JOURNAL   EMBO J 11 (13), 4825-4833 (1992)
   PUBMED   1334458
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Li,X., Smith,R.A. and Dobson,C.M.
  TITLE     Sequential 1H NMR assignments and secondary structure of the
            kringle domain from urokinase
  JOURNAL   Biochemistry 31 (40), 9562-9571 (1992)
   PUBMED   1327118
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Stephens,R.W., Aumailley,M., Timpl,R., Reisberg,T., Tapiovaara,H.,
            Myohanen,H., Murphy-Ullrich,J. and Vaheri,A.
  TITLE     Urokinase binding to laminin-nidogen. Structural requirements and
            interactions with heparin
  JOURNAL   Eur J Biochem 207 (3), 937-942 (1992)
   PUBMED   1499567
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Moroi,M. and Aoki,N.
  TITLE     Isolation and characterization of alpha2-plasmin inhibitor from
            human plasma. A novel proteinase inhibitor which inhibits
            activator-induced clot lysis
  JOURNAL   J Biol Chem 251 (19), 5956-5965 (1976)
   PUBMED   134998
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22.
            
            Summary: This gene encodes a secreted serine protease that converts
            plasminogen to plasmin. The encoded preproprotein is
            proteolytically processed to generate A and B polypeptide chains.
            These chains associate via a single disulfide bond to form the
            catalytically inactive high molecular weight urokinase-type
            plasminogen activator (HMW-uPA). HMW-uPA can be further processed
            into the catalytically active low molecular weight urokinase-type
            plasminogen activator (LMW-uPA). This low molecular weight form
            does not bind to the urokinase-type plasminogen activator receptor.
            Mutations in this gene may be associated with Quebec platelet
            disorder and late-onset Alzheimer's disease. Alternative splicing
            results in multiple transcript variants, at least one of which
            encodes an isoform that is proteolytically processed. [provided by
            RefSeq, Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3610020.1,
                                           SRR14038192.1139498.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..375
                     /product="urokinase-type plasminogen activator isoform 4
                     preprotprotein precursor"
                     /EC_number="3.4.21.73"
                     /note="plasminogen activator, urinary; U-plasminogen
                     activator; urokinase-type plasminogen activator"
                     /calculated_mol_wt=40290
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2158
     mat_peptide     21..177
                     /product="Urokinase-type plasminogen activator long chain
                     A. /id=PRO_0000028319"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=17849
     Region          34..57
                     /region_name="Binds urokinase plasminogen activator
                     surface receptor. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
     Site            38
                     /site_type="glycosylation"
                     /note="O-linked (Fuc) threonine.
                     /evidence=ECO:0000269|PubMed:2023947; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Region          67..152
                     /region_name="KR"
                     /note="Kringle domain; Kringle domains are believed to
                     play a role in binding mediators, such as peptides, other
                     proteins, membranes, or phospholipids. They are autonomous
                     structural domains, found in a varying number of copies,
                     in blood clotting and...; cd00108"
                     /db_xref="CDD:238056"
     Site            79
                     /site_type="active"
                     /note="putative domain interaction site [active]"
                     /db_xref="CDD:238056"
     Site            order(94,104,132,134,143)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Region          152..177
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
     mat_peptide     156..177
                     /product="Urokinase-type plasminogen activator short chain
                     A. /id=PRO_0000028320"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=2574
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9151681; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Site            177..178
                     /site_type="cleavage"
                     /note="Cleavage, during zymogen activation; propagated
                     from UniProtKB/Swiss-Prot (P00749.3)"
     Region          179..>373
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            179
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            322
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine. /id=CAR_000026;
                     propagated from UniProtKB/Swiss-Prot (P00749.3)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9151681; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     CDS             1..375
                     /gene="PLAU"
                     /gene_synonym="ATF; BDPLT5; QPD; u-PA; UPA; URK"
                     /coded_by="NM_001441160.1:119..1246"
                     /note="isoform 4 preprotprotein precursor is encoded by
                     transcript variant 10"
                     /db_xref="GeneID:5328"
                     /db_xref="HGNC:HGNC:9052"
                     /db_xref="MIM:191840"
ORIGIN      
        1 mrallarlll cvlvvsdskg snelhqvpsn cdclnggtcv snkyfsnihw cncpkkfggq
       61 hceidksktc yegnghfyrg kastdtmgrp clpwnsatvl qqtyhahrsd alqlglgkhn
      121 ycrnpdnrrr pwcyvqvglk llvqecmvhd cadgkkpssp peelkfqcgq ktlrprfkii
      181 ggefttienq pwfaaiyrrh rggsvtyvcg gslispcwvi sathcfidyp kkedyivylg
      241 rsrlnsntqg emkfevenli lhkdysadtl ahhndiallk irskegrcaq psrtiqticl
      301 psmyndpqfg tsceitgfgk enstdylype qlkmtvvkli shrecqqphy ygsevttkml
      361 caadpqwktd scqaa
//
LOCUS       NP_001394273             248 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 41 [Homo sapiens].
ACCESSION   NP_001394273 XP_005254707
VERSION     NP_001394273.1
DBSOURCE    REFSEQ: accession NM_001407344.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 248)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            On May 31, 2022 this sequence version replaced XP_005254707.1.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.585887.1,
                                           SRR14038194.2424173.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..248
                     /product="tropomyosin alpha-1 chain isoform 41"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=28588
     Region          12..246
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..248
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407344.1:88..834"
                     /note="isoform 41 is encoded by transcript variant 41"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 magsssleav rrkirslqeq adaaeeragt lqreldherk lretaeadva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkviesraqk deekmeiqei qlkeakhiae
      121 dadrkyeeva rklviiesdl eraeeraels egqvrqleeq lrimdqtlka lmaaedkysq
      181 kedryeeeik vlsdklkeae traefaersv tkleksiddl edelyaqklk ykaiseeldh
      241 alndmtsi
//
LOCUS       NP_001424668             557 aa            linear   PRI 21-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 10 [Homo sapiens].
ACCESSION   NP_001424668
VERSION     NP_001424668.1
DBSOURCE    REFSEQ: accession NM_001437739.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 557)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 557)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 557)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 557)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 557)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 557)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008641.7.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2220532.1,
                                           SRR14038192.2077354.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..557
                     /product="TNFAIP3-interacting protein 1 isoform 10"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=63147
     Region          <135..>172
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          <219..>459
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..557
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001437739.1:106..1779"
                     /note="isoform 10 is encoded by transcript variant 18"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 meatrlrqka eelvkdnell pppspslgsf dplaeltgkd snvtasptap acpsdkpapv
       61 qkppssalgp lpredgnlml hlqrlettls vcaeepdhgq lfthlgrmal efnrlaskvh
      121 kneqrtsilq tlceqlrken ealkakldkg leqrdqaaer lreenlelkk llmsngnkeg
      181 asgrpgspkm egtgkkavag qqqasvtagk vpevvalgaa ekkvkmleqq rsellevnkq
      241 wdqhfrsmkq qyeqkitelr qkladlqkqv tdleaereqk qrdfdrklll akskiemeet
      301 dkeqltaeak elrqkvkylq dqlspltrqr eyqekeiqrl nkaleealsi qtppssppta
      361 fgspegagal lrkqelvtqn ellkqqvkif eedfqrersd rermneekee lkkqveklqa
      421 qvtlsnaqlk afkdeekare alrqqkrkak asgeryhvep hpehlcgayp yayppmpamv
      481 phhgfedwsq iryppppmam ehppplpnsr lfhlpeytwr lpcggvrnpn qssqvmdppt
      541 arptepespk ndregpq
//
LOCUS       NP_001396238            2322 aa            linear   PRI 21-NOV-2025
DEFINITION  histone-lysine N-methyltransferase, H3 lysine-36 specific isoform f
            [Homo sapiens].
ACCESSION   NP_001396238
VERSION     NP_001396238.1
DBSOURCE    REFSEQ: accession NM_001409309.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2322)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2322)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   3  (residues 1 to 2322)
  AUTHORS   Conteduca,G., Cangelosi,D., Baldo,C., Arado,A., Testa,B.,
            Wagner,R.T., Robertson,K.D., Dequiedt,F., Fitzsimmons,L.,
            Malacarne,M., Filaci,G. and Coviello,D.A.
  TITLE     Impact of NSD1 Alternative Transcripts in Actin Filament Formation
            and Cellular Division Pathways in Fibroblasts
  JOURNAL   Genes (Basel) 15 (9), 1117 (2024)
   PUBMED   39336709
  REMARK    GeneRIF: Impact of NSD1 Alternative Transcripts in Actin Filament
            Formation and Cellular Division Pathways in Fibroblasts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2322)
  AUTHORS   Ren,Z., Yue,L., Hu,H.Y., Hou,X.L., Chen,W.Q., Tan,Y., Dong,Z. and
            Zhang,J.
  TITLE     Identification of Novel NSD1 variations in four Pediatric cases
            with sotos Syndrome
  JOURNAL   BMC Med Genomics 17 (1), 116 (2024)
   PUBMED   38684994
  REMARK    GeneRIF: Identification of Novel NSD1 variations in four Pediatric
            cases with sotos Syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2322)
  AUTHORS   Wang,X., Yeh,S., Wu,G., Hsu,C.L., Wang,L., Chiang,T., Yang,Y.,
            Guo,Y. and Chang,C.
  TITLE     Identification and characterization of a novel androgen receptor
            coregulator ARA267-alpha in prostate cancer cells
  JOURNAL   J Biol Chem 276 (44), 40417-40423 (2001)
   PUBMED   11509567
REFERENCE   6  (residues 1 to 2322)
  AUTHORS   Jaju,R.J., Fidler,C., Haas,O.A., Strickson,A.J., Watkins,F.,
            Clark,K., Cross,N.C., Cheng,J.F., Aplan,P.D., Kearney,L.,
            Boultwood,J. and Wainscoat,J.S.
  TITLE     A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in
            de novo childhood acute myeloid leukemia
  JOURNAL   Blood 98 (4), 1264-1267 (2001)
   PUBMED   11493482
REFERENCE   7  (residues 1 to 2322)
  AUTHORS   Lee,D.K., Duan,H.O. and Chang,C.
  TITLE     Androgen receptor interacts with the positive elongation factor
            P-TEFb and enhances the efficiency of transcriptional elongation
  JOURNAL   J Biol Chem 276 (13), 9978-9984 (2001)
   PUBMED   11266437
REFERENCE   8  (residues 1 to 2322)
  AUTHORS   Huang,N., vom Baur,E., Garnier,J.M., Lerouge,T., Vonesch,J.L.,
            Lutz,Y., Chambon,P. and Losson,R.
  TITLE     Two distinct nuclear receptor interaction domains in NSD1, a novel
            SET protein that exhibits characteristics of both corepressors and
            coactivators
  JOURNAL   EMBO J 17 (12), 3398-3412 (1998)
   PUBMED   9628876
REFERENCE   9  (residues 1 to 2322)
  AUTHORS   Ocansey,S., Cole,T.R.P., Rahman,N. and Tatton-Brown,K.
  TITLE     Sotos Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301652
REFERENCE   10 (residues 1 to 2322)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027314.5, AC008570.6 and
            AC146507.2.
            
            Summary: This gene encodes a protein containing a SET domain, 2
            LXXLL motifs, 3 nuclear translocation signals (NLSs), 4 plant
            homeodomain (PHD) finger regions, and a proline-rich region. The
            encoded protein enhances androgen receptor (AR) transactivation,
            and this enhancement can be increased further in the presence of
            other androgen receptor associated coregulators. This protein may
            act as a nucleus-localized, basic transcriptional factor and also
            as a bifunctional transcriptional regulator. Mutations of this gene
            have been associated with Sotos syndrome and Weaver syndrome. One
            version of childhood acute myeloid leukemia is the result of a
            cryptic translocation with the breakpoints occurring within nuclear
            receptor-binding Su-var, enhancer of zeste, and trithorax domain
            protein 1 on chromosome 5 and nucleoporin, 98-kd on chromosome 11.
            Multiple transcript variants encoding distinct isoforms have been
            identified for this gene. [provided by RefSeq, Sep 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.151364.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968832,
                                           SAMEA1968968 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2322
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..2322
                     /product="histone-lysine N-methyltransferase, H3 lysine-36
                     specific isoform f"
                     /EC_number="2.1.1.357"
                     /note="androgen receptor-associated coregulator 267;
                     histone-lysine N-methyltransferase, H3 lysine-36 and H4
                     lysine-20 specific; H3-K36-HMTase; H4-K20-HMTase; lysine
                     N-methyltransferase 3B; NR-binding SET domain-containing
                     protein; androgen receptor coactivator 267 kDa protein;
                     androgen receptor-associated protein of 267 kDa; nuclear
                     receptor-binding SET domain-containing protein 1; nuclear
                     receptor SET domain-containing protein 1; histone-lysine
                     N-methyltransferase, H3 lysine-36 specific"
                     /calculated_mol_wt=255922
     Region          27..142
                     /region_name="PWWP_NSD1_rpt1"
                     /note="first PWWP domain found in nuclear receptor-binding
                     SET domain-containing protein 1 (NSD1) and similar
                     proteins; cd20161"
                     /db_xref="CDD:438989"
     Site            order(43,46,77)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438989"
     Site            44..47
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438989"
     Site            order(115..117,120..121)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438989"
     Region          <1140..1296
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          1254..1296
                     /region_name="PHD1_NSD1_2"
                     /note="PHD finger 1 found in nuclear receptor-binding SET
                     domain-containing protein NSD1 and NSD2; cd15648"
                     /db_xref="CDD:277118"
     Site            order(1254,1263..1267,1272,1290)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277118"
     Region          1301..1347
                     /region_name="PHD2_NSD1"
                     /note="PHD finger 2 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15650"
                     /db_xref="CDD:277120"
     Site            order(1301,1311..1315,1321,1342)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277120"
     Region          1348..1401
                     /region_name="PHD3_NSD1"
                     /note="PHD finger 3 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15653"
                     /db_xref="CDD:277123"
     Site            order(1348,1366..1370,1374,1396)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277123"
     Region          1418..1457
                     /region_name="PHD4_NSD1"
                     /note="PHD finger 4 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15656"
                     /db_xref="CDD:277126"
     Site            order(1418,1427..1431,1435,1452)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277126"
     Region          1464..1559
                     /region_name="PWWP_NSD1_rpt2"
                     /note="second PWWP domain found in nuclear
                     receptor-binding SET domain-containing protein 1 (NSD1)
                     and similar proteins; cd20164"
                     /db_xref="CDD:438992"
     Site            order(1476,1479,1507)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438992"
     Site            1477..1480
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438992"
     Region          1610..1648
                     /region_name="AWS"
                     /note="AWS domain; pfam17907"
                     /db_xref="CDD:465559"
     Region          1650..>1716
                     /region_name="SET"
                     /note="SET (Su(var)3-9, Enhancer-of-zeste, Trithorax)
                     domain superfamily; cl40432"
                     /db_xref="CDD:394802"
     Region          1746..1788
                     /region_name="PHD5_NSD1"
                     /note="PHD finger 5 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15659"
                     /db_xref="CDD:277129"
     Site            order(1746,1755..1759,1765,1783)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277129"
     Region          1787..1836
                     /region_name="C5HCH"
                     /note="NSD Cys-His rich domain; pfam17982"
                     /db_xref="CDD:465605"
     Region          <1834..2200
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..2322
                     /gene="NSD1"
                     /gene_synonym="ARA267; KMT3B; SOTOS; SOTOS1; STO"
                     /coded_by="NM_001409309.1:186..7154"
                     /note="isoform f is encoded by transcript variant 12"
                     /db_xref="GeneID:64324"
                     /db_xref="HGNC:HGNC:14234"
                     /db_xref="MIM:606681"
ORIGIN      
        1 mlelpgtsss stsqelpfcq pkkkstplky evgdliwakf krrpwwpcri csdplinths
       61 kmkvsnrrpy rqyyveafgd pserawvagk aivmfegrhq feelpvlrrr gkqkekgyrh
      121 kvpqkilskw easvglaeqy dvpkgsknrk cipgsiklds eedmpfedct ndpesehdll
      181 lngclkslaf dsehsadeke kpcaksrark ssdnpkrtsv kkghiqfeah kderrgkipe
      241 nlglnfisgd isdtqasnel sriansltgs ntapgsflfs scgkntakke fetsngdsll
      301 glpegalisk csreknkpqr slvcgskvkl cyigagdeek rsdsisictt sddgssdldp
      361 iehssesdns vleipdafdr tenmlsmqkn ekikysrfaa tntrvkakqk plisnshtdh
      421 lmgctksaep gtetsqvnls dlkastlvhk pqsdftndal spkfnlsssi ssenslikgg
      481 aanqallhsk skqpkfrsik ckhkenpvma eppvineecs lkccssdtkg splasisksg
      541 kvdglkllnn mhektrdssd ietavvkhvl selkelsyrs lgedvsdsgt skpskpllfs
      601 sassqnhipi epdykfstll mmlkdmhdsk tkeqrlmtaq nlvsyrspgr gdcstnspvg
      661 vskvlvsggs thnsekkgdg tqnsanpsps ggdsalsgel saslpgllsd krdlpasgks
      721 rsdcvtrrnc grskpssklr dafsaqmvkn tvnrkalkte rkrklnqlps vtldavlqgd
      781 rerggslrgg aedpskedpl qimghltsed gdhfsdvhfd skvkqsdpgk isekglsfen
      841 gkgpeldsvm nsendelngv nqvvpkkrwq rlnqrrtkpr krmnrfkeke nsecafrvll
      901 psdpvqegrd efpehrtpsa sileeplteq nhadcldsag prlnvcdkss asigdmekep
      961 gipsltpqae lpepavrsek krlrkpskwl leyteeydqi fapkkkqkkv qeqvhkvssr
     1021 ceeesllarg rssaqnkqvd enslistkee ppvlereapf legplaqsel ggghaelpql
     1081 tlsvpvapev sprpalesee llvktpgnye skrqrkptkk llesndldpg fmpkkgdlgl
     1141 skkcyeaghl engitescat syskdfgggt tkifdkprkr krqrhaaakm qckkvkndds
     1201 skeipgsege lmphrtatsp ketveegveh dpgmpaskkm qgergggaal kenvcqncek
     1261 lgelllceaq ccgafhlecl gltemprgkf icnecrtgih tcfvckqsge dvkrcllplc
     1321 gkfyheecvq kypptvmqnk gfrcslhici tchaanpanv saskgrlmrc vrcpvayhan
     1381 dfclaagski lasnsiicpn hftprrgcrn hehvnvswcf vcseggsllc cdscpaafhr
     1441 eclnidipeg nwycndckag kkphyreivw vkvgryrwwp aeichpravp snidkmrhdv
     1501 gefpvlffgs ndylwthqar vfpymegdvs skdkmgkgvd gtykkalqea aarfeelkaq
     1561 kelrqlqedr kndkkpppyk hikvnrpigr vqiftadlse iprcnckatd enpcgidsec
     1621 inrmllyech ptvcpaggrc qnqcfskrqy peveifrtlq rgwglrtktd ikkgefvney
     1681 vgelideeec rariryaqeh ditnfymltl dknqpiatee kskkfkkkqq gkrrtqgeit
     1741 keredecfsc gdagqlvsck kpgcpkvyha dclnltkrpa gkwecpwhqc dicgkeaasf
     1801 cemcpssfck qhregmlfis kldgrlscte hdpcgpnple pgeireyvpp pvplppgpst
     1861 hlaeqstgma aqapkmsdkp padtnqmlsl skkalagtcq rpllperple rtdsrpqpld
     1921 kvrdlagsgt ksqslvssqr pldrppavag prpqlsdkps pvtspsssps vrsqplerpl
     1981 gtadprldks igaasprpqs lektsvptgl rlpppdrlli tsspkpqtsd rptdkphasl
     2041 sqrlpppekv lsavvqtlva kekalrpvdq ntqsknraal vmdlidltpr qkeraasphq
     2101 vtpqadekmp vlessswpas kglghmprav ekgcvsdplq tsgkaaapse dpwqavkslt
     2161 qarllsqppa kaflyepttq asgrasagae qtpgplsqsp glvkqakqmv ggqqlpalaa
     2221 ksgqsfrslg kapaslptee kklvtteqsp walgkassra glwpivagqt laqscwsags
     2281 tqtlaqtcws lgrgqdpkpe qntlpalnqa psshkcaese qk
//
LOCUS       NP_001427922             727 aa            linear   PRI 21-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 6 isoform 3 [Homo sapiens].
ACCESSION   NP_001427922 XP_005262556 XP_054184148
VERSION     NP_001427922.1
DBSOURCE    REFSEQ: accession NM_001440993.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Zheng,T., Zhou,H., Zheng,Z., Guo,Y., Liu,J., Zhang,J. and Li,S.
  TITLE     The pathological significance and potential mechanism of ARHGEF6 in
            lung adenocarcinoma
  JOURNAL   Comput Biol Med 158, 106894 (2023)
   PUBMED   37058762
  REMARK    GeneRIF: The pathological significance and potential mechanism of
            ARHGEF6 in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 727)
  AUTHORS   Li,K., Wang,H., Yang,C., Li,C., Xue,B. and Zhou,J.
  TITLE     Clinical implication and potential function of ARHGEF6 in acute
            myeloid leukemia: An in vitro study
  JOURNAL   PLoS One 18 (4), e0283934 (2023)
   PUBMED   37027440
  REMARK    GeneRIF: Clinical implication and potential function of ARHGEF6 in
            acute myeloid leukemia: An in vitro study.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 727)
  AUTHORS   Klambt,V., Buerger,F., Wang,C., Naert,T., Richter,K., Nauth,T.,
            Weiss,A.C., Sieckmann,T., Lai,E., Connaughton,D.M., Seltzsam,S.,
            Mann,N., Majmundar,A.J., Wu,C.W., Onuchic-Whitford,A.C., Shril,S.,
            Schneider,S., Schierbaum,L., Dai,R., Bekheirnia,M.R., Joosten,M.,
            Shlomovitz,O., Vivante,A., Banne,E., Mane,S., Lifton,R.P.,
            Kirschner,K.M., Kispert,A., Rosenberger,G., Fischer,K.D.,
            Lienkamp,S.S., Zegers,M.M.P. and Hildebrandt,F.
  TITLE     Genetic Variants in ARHGEF6 Cause Congenital Anomalies of the
            Kidneys and Urinary Tract in Humans, Mice, and Frogs
  JOURNAL   J Am Soc Nephrol 34 (2), 273-290 (2023)
   PUBMED   36414417
  REMARK    GeneRIF: Genetic Variants in ARHGEF6 Cause Congenital Anomalies of
            the Kidneys and Urinary Tract in Humans, Mice, and Frogs.
REFERENCE   5  (residues 1 to 727)
  AUTHORS   Wang,N., Li,Y., Zhou,X., Wang,X. and Yang,G.
  TITLE     Comprehensive analysis identifies ARHGEF6 as a potential prognostic
            and immunological biomarker in lung adenocarcinoma
  JOURNAL   Comput Biol Med 153, 106448 (2023)
   PUBMED   36586227
  REMARK    GeneRIF: Comprehensive analysis identifies ARHGEF6 as a potential
            prognostic and immunological biomarker in lung adenocarcinoma.
REFERENCE   6  (residues 1 to 727)
  AUTHORS   Yoshii,S., Tanaka,M., Otsuki,Y., Wang,D.Y., Guo,R.J., Zhu,Y.,
            Takeda,R., Hanai,H., Kaneko,E. and Sugimura,H.
  TITLE     alphaPIX nucleotide exchange factor is activated by interaction
            with phosphatidylinositol 3-kinase
  JOURNAL   Oncogene 18 (41), 5680-5690 (1999)
   PUBMED   10523848
REFERENCE   7  (residues 1 to 727)
  AUTHORS   Yntema,H.G., Hamel,B.C., Smits,A.P., van Roosmalen,T., van den
            Helm,B., Kremer,H., Ropers,H.H., Smeets,D.F. and van Bokhoven,H.
  TITLE     Localisation of a gene for non-specific X linked mental retardation
            (MRX46) to Xq25-q26
  JOURNAL   J Med Genet 35 (10), 801-805 (1998)
   PUBMED   9783701
REFERENCE   8  (residues 1 to 727)
  AUTHORS   Ebinu,J.O., Bottorff,D.A., Chan,E.Y., Stang,S.L., Dunn,R.J. and
            Stone,J.C.
  TITLE     RasGRP, a Ras guanyl nucleotide- releasing protein with calcium-
            and diacylglycerol-binding motifs
  JOURNAL   Science 280 (5366), 1082-1086 (1998)
   PUBMED   9582122
REFERENCE   9  (residues 1 to 727)
  AUTHORS   Manser,E., Loo,T.H., Koh,C.G., Zhao,Z.S., Chen,X.Q., Tan,L.,
            Tan,I., Leung,T. and Lim,L.
  TITLE     PAK kinases are directly coupled to the PIX family of nucleotide
            exchange factors
  JOURNAL   Mol Cell 1 (2), 183-192 (1998)
   PUBMED   9659915
REFERENCE   10 (residues 1 to 727)
  AUTHORS   Nomura,N., Nagase,T., Miyajima,N., Sazuka,T., Tanaka,A., Sato,S.,
            Seki,N., Kawarabayasi,Y., Ishikawa,K. and Tabata,S.
  TITLE     Prediction of the coding sequences of unidentified human genes. II.
            The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
            analysis of cDNA clones from human cell line KG-1 (supplement)
  JOURNAL   DNA Res 1 (5), 251-262 (1994)
   PUBMED   7584048
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL683813.10 and AL135783.6.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_005262556.1, XP_054184148.1.
            
            Summary: Rho GTPases play a fundamental role in numerous cellular
            processes that are initiated by extracellular stimuli that work
            through G protein coupled receptors. The encoded protein belongs to
            a family of cytoplasmic proteins that activate the Ras-like family
            of Rho proteins by exchanging bound GDP for GTP. It may form a
            complex with G proteins and stimulate Rho-dependent signals. This
            protein is activated by PI3-kinase. Mutations in this gene can
            cause X-chromosomal non-specific cognitive disability. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1453405.1,
                                           SRR1660805.131693.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.3"
     Protein         1..727
                     /product="rho guanine nucleotide exchange factor 6 isoform
                     3"
                     /note="Rac/Cdc42 guanine exchange factor (GEF) 6; rho
                     guanine nucleotide exchange factor 6; PAK-interacting
                     exchange factor, alpha; Rac/Cdc42 guanine nucleotide
                     exchange factor (GEF) 6"
                     /calculated_mol_wt=81963
     Region          1..117
                     /region_name="CH_alphaPIX"
                     /note="calponin homology (CH) domain found in alpha-Pak
                     Interactive eXchange factor; cd21265"
                     /db_xref="CDD:409114"
     Site            order(3,7,65,67..68,71..72,74,81..89,95,97..98,100..101,
                     104..105,108)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409114"
     Region          115..160
                     /region_name="RhoGEF67_u1"
                     /note="Unstructured region one on RhoGEF 6 and 7;
                     pfam16615"
                     /db_xref="CDD:465201"
     Region          162..219
                     /region_name="SH3_alphaPIX"
                     /note="Src Homology 3 domain of alpha-Pak Interactive
                     eXchange factor; cd12060"
                     /db_xref="CDD:212993"
     Site            order(169,171,174,177..178,193,195..197,208,210,212..213)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212993"
     Region          242..419
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(248,252,346,370..371,374..375,377..378,381..382,
                     385..386,389,415,419)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          450..547
                     /region_name="PH_Cool_Pix"
                     /note="Cloned out of library/PAK-interactive exchange
                     factor pleckstrin homology (PH) domain; cd01225"
                     /db_xref="CDD:269932"
     Region          <572..625
                     /region_name="RhoGEF67_u2"
                     /note="Unstructured region two on RhoGEF 6 and 7;
                     pfam16614"
                     /db_xref="CDD:465200"
     Region          636..720
                     /region_name="betaPIX_CC"
                     /note="betaPIX coiled coil; pfam16523"
                     /db_xref="CDD:465158"
     CDS             1..727
                     /gene="ARHGEF6"
                     /gene_synonym="alpha-PIX; alphaPIX; Cool-2; COOL2; MRX46;
                     PIXA"
                     /coded_by="NM_001440993.1:51..2234"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:9459"
                     /db_xref="HGNC:HGNC:685"
                     /db_xref="MIM:300267"
ORIGIN      
        1 mnpeeqivtw lislgvlesp kkticdpeef lksslkngvv lcklinrlmp gsvekfcldp
       61 qteadcinni ndflkgcatl qveifdpddl ysgvnfskvl stllavnkat edqlserpcg
      121 rssslsaant sqtnpqgavs stvsglqrqs ktvemtengs hqlivkarfn fkqtnedels
      181 vckgdiiyvt rveeggwweg tlngrtgwfp snyvreikss erplspkavk gfetapltkn
      241 yytvvlqnil dtekeyakel qsllvtylrp lqsnnnlstv evtsllgnfe evctfqqtlc
      301 qaleecskfp enqhkvggcl lslmphfksm ylaycanhps avnvltqhsd eleqfmenqg
      361 asspgililt tnlskpfmrl ekyvtllqel erhmedthpd hqdilkaiva fktlmgqcqd
      421 lrkrkqlelq ilsepiqawe gediknlgnv ifmsqvmvqy gaceekeery lmlfsnvlim
      481 lsasprmsgf iyqgkipiag tvvtrldeie gndctfeitg ntverivvhc nnnqdfqewl
      541 eqlnrlirgp ascsslskts ssscsahses skspktmkkf lhkrkterkp seeeyvirks
      601 taaleedaqi lkvieaycts anfqqghgss trkdsipqvl lpeeekliie etrsngqtim
      661 eekslvdtvy alkdevrelk qenkrmkqcl eeelksrrdl eklvrrllkq tdecirgess
      721 sktsilp
//
LOCUS       NP_001400252             326 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 17 [Homo sapiens].
ACCESSION   NP_001400252
VERSION     NP_001400252.1
DBSOURCE    REFSEQ: accession NM_001413323.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC103816.2, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.40490.1,
                                           SRR14372080.1881177.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..326
                     /product="RNA-binding Raly-like protein isoform 17"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=36288
     Region          50..132
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          234..>279
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     CDS             1..326
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413323.1:244..1224"
                     /note="isoform 17 is encoded by transcript variant 49"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mlrttllvcs ndptplrysp wrgawlhrlk qgepimtgkt qtsnvtnknd pksinsrvfi
       61 gnlntaivkk vdieaifsky gkivgcsvhk gyafvqymse rharaavage narviagqpl
      121 dinmagepkp yrpkpgnkrp lsalyrlesk epflsvggyv fdydyyrddf ynrlfdyhgr
      181 vppppravip lkrprvavtt trrgkgvfsm kggsrstasg stgsklksde lqtikkeltq
      241 iktkidsllg rlekiekqqk aeaeaqkkql eeslvliqee cvseiadhst eepaeggpda
      301 dgeemtdgie edfdedgghe lflqik
//
LOCUS       NP_001393552            1042 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 11 [Homo sapiens].
ACCESSION   NP_001393552
VERSION     NP_001393552.1
DBSOURCE    REFSEQ: accession NM_001406623.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1042)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1042)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1042)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1042)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1042)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1042)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1042)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1369110.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1042
                     /product="hamartin isoform 11"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=116074
     Region          16..597
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <586..>838
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1042
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406623.1:706..3834"
                     /note="isoform 11 is encoded by transcript variant 37"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mdtdvvvltt gvlvlitmlp mipqsgkqhl ldffdifgrl sswclkkpgh vaevylvhlh
       61 asvyalfhrl ygmypcnfvs flrshysmke nletfeevvk pmmehvrihp elvtgskdhe
      121 ldprrwkrle thdvviecak isldpteasy edgysvshqi sarfphrsad vttspyadtq
      181 nsygcatstp ystsrlmlln mpgqlpqtls spstrlitep pqatlwspsm vcgmttppts
      241 pgnvppdlsh pyskvfgttg gkgtplgtpa tspppaplch sddyvhislp qatvtpprke
      301 ermdsarpcl hrqhhllndr gseeppgskg svtlsdlpgf lgdlaseeds iekdkeeaai
      361 srelseitta eaepvvprgg fdspfyrdsl pgsqrkthsa asssqgasvn peplhssldk
      421 lgpdtpkqaf tpidlpcgsa despagdrec qtsletsift pspckipppt rvgfgsgqpp
      481 pydhlfeval pktahhfvir kteellkkak gnteedgvps tspmevldrl iqqgadahsk
      541 elnklplpsk svdwthfggs ppsdeirtlr dqllllhnql lyerfkrqqh alrnrrllrk
      601 vikaaaleeh naamkdqlkl qekdiqmwkv slqkeqaryn qlqeqrdtmv tklhsqirql
      661 qhdreefynq sqelqtkled crnmiaelri elkkannkvc htelllsqvs qklsnsesvq
      721 qqmeflnrql lvlgevnely leqlqnkhsd ttkevemmka ayrkeleknr shvlqqtqrl
      781 dtsqkrilel eshlakkdhl lleqkkyled vklqargqlq aaesryeaqk ritqvfelei
      841 ldlygrlekd gllkkleeek aeaaeaaeer ldccndgcsd smvghneeas ghngetktpr
      901 pssargssgs rggggsssss selstpekpp hqragpfssr wettmgeasa sipttvgslp
      961 ssksflgmka relfrnkses qcdedgmtss lseslktelg kdlgveakip lnldgphpsp
     1021 ptpdsvgqlh imdynethhe hs
//
LOCUS       NP_001393931             386 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform N [Homo sapiens].
ACCESSION   NP_001393931
VERSION     NP_001393931.1
DBSOURCE    REFSEQ: accession NM_001407002.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 386)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 386)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 386)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 386)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 386)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355388.30 and AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.169350.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2146982
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..386
                     /product="lamin isoform N"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=44241
     Region          <1..200
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          248..355
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     CDS             1..386
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001407002.1:955..2115"
                     /note="isoform N is encoded by transcript variant 27"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 mlrrvdaenr lqtmkeeldf qkniyseelr etkrrhetrl veidngkqre fesrladalq
       61 elraqhedqv eqykkelekt ysakldnarq saernsnlvg aaheelqqsr iridslsaql
      121 sqlqkqlaak eaklrdleds larerdtsrr llaekerema emrarmqqql deyqelldik
      181 laldmeihay rkllegeeer lrlspsptsq rsrgrasshs sqtqgggsvt kkrklestes
      241 rssfsqhart sgrvaveevd eegkfvrlrn ksnedqsmgn wqikrqngdd plltyrfppk
      301 ftlkagqvvt iwaagagath spptdlvwka qntwgcgnsl rtalinstge evamrklvrs
      361 vtvveddede dgddllhhhh vsgsrr
//
LOCUS       NP_001428012            1231 aa            linear   PRI 21-NOV-2025
DEFINITION  cohesin subunit SA-2 isoform b [Homo sapiens].
ACCESSION   NP_001428012
VERSION     NP_001428012.1
DBSOURCE    REFSEQ: accession NM_001441083.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1231)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1231)
  AUTHORS   Fischer,A., Hernandez-Rodriguez,B., Mulet-Lazaro,R., Nuetzel,M.,
            Holzl,F., van Herk,S., Kavelaars,F.G., Stanewsky,H., Ackermann,U.,
            Niang,A.H., Diaz,N., Reuschel,E., Strieder,N., Hernandez-Lopez,I.,
            Valk,P.J.M., Vaquerizas,J.M., Rehli,M., Delwel,R. and Gebhard,C.
  TITLE     STAG2 mutations reshape the cohesin-structured spatial chromatin
            architecture to drive gene regulation in acute myeloid leukemia
  JOURNAL   Cell Rep 43 (8), 114498 (2024)
   PUBMED   39084219
  REMARK    GeneRIF: STAG2 mutations reshape the cohesin-structured spatial
            chromatin architecture to drive gene regulation in acute myeloid
            leukemia.
REFERENCE   3  (residues 1 to 1231)
  AUTHORS   Huber,J., Tanasie,N.L., Zernia,S. and Stigler,J.
  TITLE     Single-molecule imaging reveals a direct role of CTCF's zinc
            fingers in SA interaction and cluster-dependent RNA recruitment
  JOURNAL   Nucleic Acids Res 52 (11), 6490-6506 (2024)
   PUBMED   38742641
  REMARK    GeneRIF: Single-molecule imaging reveals a direct role of CTCF's
            zinc fingers in SA interaction and cluster-dependent RNA
            recruitment.
REFERENCE   4  (residues 1 to 1231)
  AUTHORS   Xu,W., Kim,J.S., Yang,T., Ya,A., Sadzewicz,L., Tallon,L.,
            Harris,B.T., Sarkaria,J., Jin,F. and Waldman,T.
  TITLE     STAG2 mutations regulate 3D genome organization, chromatin loops,
            and Polycomb signaling in glioblastoma multiforme
  JOURNAL   J Biol Chem 300 (6), 107341 (2024)
   PUBMED   38705393
  REMARK    GeneRIF: STAG2 mutations regulate 3D genome organization, chromatin
            loops, and Polycomb signaling in glioblastoma multiforme.
REFERENCE   5  (residues 1 to 1231)
  AUTHORS   Ros-Pardo,D., Gomez-Puertas,P. and Marcos-Alcalde,I.
  TITLE     STAG2: Computational Analysis of Missense Variants Involved in
            Disease
  JOURNAL   Int J Mol Sci 25 (2), 1280 (2024)
   PUBMED   38279279
  REMARK    GeneRIF: STAG2: Computational Analysis of Missense Variants
            Involved in Disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1231)
  AUTHORS   Gregson,H.C., Schmiesing,J.A., Kim,J.S., Kobayashi,T., Zhou,S. and
            Yokomori,K.
  TITLE     A potential role for human cohesin in mitotic spindle aster
            assembly
  JOURNAL   J Biol Chem 276 (50), 47575-47582 (2001)
   PUBMED   11590136
REFERENCE   7  (residues 1 to 1231)
  AUTHORS   Sumara,I., Vorlaufer,E., Gieffers,C., Peters,B.H. and Peters,J.M.
  TITLE     Characterization of vertebrate cohesin complexes and their
            regulation in prophase
  JOURNAL   J Cell Biol 151 (4), 749-762 (2000)
   PUBMED   11076961
REFERENCE   8  (residues 1 to 1231)
  AUTHORS   Carramolino,L., Lee,B.C., Zaballos,A., Peled,A., Barthelemy,I.,
            Shav-Tal,Y., Prieto,I., Carmi,P., Gothelf,Y., Gonzalez de
            Buitrago,G., Aracil,M., Marquez,G., Barbero,J.L. and Zipori,D.
  TITLE     SA-1, a nuclear protein encoded by one member of a novel gene
            family: molecular cloning and detection in hemopoietic organs
  JOURNAL   Gene 195 (2), 151-159 (1997)
   PUBMED   9305759
  REMARK    Erratum:[Gene 1998 Jan 12;206(2):283]
REFERENCE   9  (residues 1 to 1231)
  AUTHORS   Wu,C., Friedlander,P., Lamoureux,C., Zannis-Hadjopoulos,M. and
            Price,G.B.
  TITLE     cDNA clones contain autonomous replication activity
  JOURNAL   Biochim Biophys Acta 1174 (3), 241-257 (1993)
   PUBMED   7690594
REFERENCE   10 (residues 1 to 1231)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121601.13 and AL355476.12.
            
            Summary: The protein encoded by this gene is a subunit of the
            cohesin complex, which regulates the separation of sister
            chromatids during cell division. Targeted inactivation of this gene
            results in chromatid cohesion defects and aneuploidy, suggesting
            that genetic disruption of cohesin is a cause of aneuploidy in
            human cancer. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3009334.1,
                                           SRR14038195.2182951.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1231
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..1231
                     /product="cohesin subunit SA-2 isoform b"
                     /note="SCC3 homolog 2; cohesin subunit SA-2; SA2
                     stromalin; sister chromatid cohesion 3 homolog B; stromal
                     antigen 2"
                     /calculated_mol_wt=141196
     Region          1..75
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Region          102..>395
                     /region_name="IRR1"
                     /note="Cohesin [Cell division and chromosome
                     partitioning]; COG5537"
                     /db_xref="CDD:227824"
     Region          157..270
                     /region_name="STAG"
                     /note="STAG domain; pfam08514"
                     /db_xref="CDD:462502"
     Site            607
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1058
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1061
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Region          1064..1083
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1064
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35638; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1065
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35638; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1112
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     CDS             1..1231
                     /gene="STAG2"
                     /gene_synonym="bA517O1.1; HPE13; MKMS; NEDXCF; SA-2; SA2;
                     SCC3B"
                     /coded_by="NM_001441083.1:530..4225"
                     /note="isoform b is encoded by transcript variant 26"
                     /db_xref="GeneID:10735"
                     /db_xref="HGNC:HGNC:11355"
                     /db_xref="MIM:300826"
ORIGIN      
        1 miaapeiptd fnllqeseth fssdtdfedi egknqkqgkg ktckkgkkgp aekgkggngg
       61 gkppsgpnrm nghhqqngve nmmlfevvkm gksamqsvvd dwiesykhdr dialldlinf
      121 fiqcsgckgv vtaemfrhmq nseiirkmte efdedsgdyp ltmagpqwkk fkssfcefig
      181 vlvrqcqysi iydeymmdtv islltglsds qvrafrhtst laamklmtal vnvalnlsin
      241 mdntqrqyea ernkmigkra nerlelllqk rkelqenqde ienmmnaifk gvfvhryrda
      301 iaeiraicie eigiwmkmys daflndsylk yvgwtmhdkq gevrlkclta lqglyynkel
      361 nsklelftsr fkdrivsmtl dkeydvavqa iklltlvlqs seevltaedc envyhlvysa
      421 hrpvavaage flykklfsrr dpeedgmmkr rgrqgpnanl vktlvfffle selhehaayl
      481 vdsmwdcate llkdwecmns llleeplsge ealtdrqesa lieimlctir qaaechppvg
      541 rgtgkrvlta kekktqlddr tkitelfava lpqllakysv daekvtnllq lpqyfdleiy
      601 ttgrlekhld allrqirniv ekhtdtdvle acsktyhalc neeftifnrv disrsqlide
      661 ladkfnrlle dflqegeepd eddayqvlst lkritafhna hdlskwdlfa cnykllktgi
      721 engdmpeqiv ihalqcthyv ilwqlakite ssstkedllr lkkqmrvfcq icqhyltnvn
      781 ttvkeqafti lcdilmifsh qimsggrdml eplvytpdss lqsellsfil dhvfieqddd
      841 nnsadgqqed easkiealhk rrnllaafck livytvvemn taadifkqym kyyndygdii
      901 ketmsktrqi dkiqcaktli lslqqlfnem iqengynfdr ssstfsgike larrfaltfg
      961 ldqlktreai amlhkdgief afkepnpqge shpplnlafl dilsefsskl lrqdkrtvyv
     1021 ylekfmtfqm slrredvwlp lmsyrnslla ggdddtmsvi sgissrgstv rskkskpstg
     1081 krkvvegmql slteessssd smwlsreqtl htpvmmqtpq ltstimrepk rlrpedsfms
     1141 vypmqtehhq tpldynrrgt slmeddeepi vedvmmsseg riedlnegmd fdtmdidlpp
     1201 sknrrertel kpdffdpasi mdesvlgvsm f
//
LOCUS       NP_001427441             590 aa            linear   PRI 21-NOV-2025
DEFINITION  radixin isoform 7 [Homo sapiens].
ACCESSION   NP_001427441
VERSION     NP_001427441.1
DBSOURCE    REFSEQ: accession NM_001440512.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 590)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 590)
  AUTHORS   Kruse,T., Benz,C., Garvanska,D.H., Lindqvist,R., Mihalic,F.,
            Coscia,F., Inturi,R., Sayadi,A., Simonetti,L., Nilsson,E., Ali,M.,
            Kliche,J., Moliner Morro,A., Mund,A., Andersson,E., McInerney,G.,
            Mann,M., Jemth,P., Davey,N.E., Overby,A.K., Nilsson,J. and
            Ivarsson,Y.
  TITLE     Large scale discovery of coronavirus-host factor protein
            interaction motifs reveals SARS-CoV-2 specific mechanisms and
            vulnerabilities
  JOURNAL   Nat Commun 12 (1), 6761 (2021)
   PUBMED   34799561
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 590)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 590)
  AUTHORS   Stemmer-Rachamimov,A.O., Gonzalez-Agosti,C., Xu,L., Burwick,J.A.,
            Beauchamp,R., Pinney,D., Louis,D.N. and Ramesh,V.
  TITLE     Expression of NF2-encoded merlin and related ERM family proteins in
            the human central nervous system
  JOURNAL   J Neuropathol Exp Neurol 56 (6), 735-742 (1997)
   PUBMED   9184664
REFERENCE   7  (residues 1 to 590)
  AUTHORS   Hirao,M., Sato,N., Kondo,T., Yonemura,S., Monden,M., Sasaki,T.,
            Takai,Y., Tsukita,S. and Tsukita,S.
  TITLE     Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma
            membrane association: possible involvement of phosphatidylinositol
            turnover and Rho-dependent signaling pathway
  JOURNAL   J Cell Biol 135 (1), 37-51 (1996)
   PUBMED   8858161
REFERENCE   8  (residues 1 to 590)
  AUTHORS   Wilgenbus,K.K., Milatovich,A., Francke,U. and Furthmayr,H.
  TITLE     Molecular cloning, cDNA sequence, and chromosomal assignment of the
            human radixin gene and two dispersed pseudogenes
  JOURNAL   Genomics 16 (1), 199-206 (1993)
   PUBMED   8486357
REFERENCE   9  (residues 1 to 590)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 590)
  AUTHORS   Sato,N., Funayama,N., Nagafuchi,A., Yonemura,S., Tsukita,S. and
            Tsukita,S.
  TITLE     A gene family consisting of ezrin, radixin and moesin. Its specific
            localization at actin filament/plasma membrane association sites
  JOURNAL   J Cell Sci 103 (Pt 1), 131-143 (1992)
   PUBMED   1429901
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002788.3 and AP000901.5.
            
            Summary: Radixin is a cytoskeletal protein that may be important in
            linking actin to the plasma membrane. It is highly similar in
            sequence to both ezrin and moesin. The radixin gene has been
            localized by fluorescence in situ hybridization to 11q23. A
            truncated version representing a pseudogene (RDXP2) was assigned to
            Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was
            mapped to 11p by Southern and PCR analyses. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR12921934.2469335.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..590
                     /product="radixin isoform 7"
                     /calculated_mol_wt=69393
     Region          7..206
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          200..303
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(249..250,252..258,267,288,291..292,295)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(249,252..259,267,288,291..292,295)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(285,289)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            288..303
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          317..337
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35241.1)"
     Region          354..463
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          383..414
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35241.1)"
     Region          469..533
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35241.1)"
     Region          514..590
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ROCK2.
                     /evidence=ECO:0000250|UniProtKB:P26043; propagated from
                     UniProtKB/Swiss-Prot (P35241.1)"
     CDS             1..590
                     /gene="RDX"
                     /gene_synonym="DFNB24"
                     /coded_by="NM_001440512.1:213..1985"
                     /note="isoform 7 is encoded by transcript variant 14"
                     /db_xref="GeneID:5962"
                     /db_xref="HGNC:HGNC:9944"
                     /db_xref="MIM:179410"
ORIGIN      
        1 mpkpinvrvt tmdaelefai qpnttgkqlf dqvvktvglr evwffglqyv dskgystwlk
       61 lnkkvtqqdv kkenplqfkf rakffpedvs eeliqeitqr lfflqvkeai lndeiycppe
      121 tavllasyav qakygdynke ihkpgyland rllpqrvleq hkltkeqwee riqnwheehr
      181 gmlredsmme ylkiaqdlem ygvnyfeikn kkgtelwlgv dalglniyeh ddkrcfhflr
      241 ltpkigfpws eirnisfndk kfvikpidkk apdfvfyapr lrinkrilal cmgnhelymr
      301 rrkpdtievq qmkaqareek hqkqleraql enekkkreia ekekeriere keelmerlkq
      361 ieeqtikaqk eleeqtrkal eldqerkrak eeaerleker raaeeaksai akqaadqmkn
      421 qeqlaaelae ftakiallee akkkkeeeat ewqhkafaaq edlektkeel ktvmsapppp
      481 ppppvippte nehdehdenn aeasaelsne gvmnhrseee rvtetqkner vkkqlqalss
      541 elaqardetk ktqndvlhae nvkagrdkyk tlrqirqgnt kqridefeam
//
LOCUS       NP_001400230             322 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 11 [Homo sapiens].
ACCESSION   NP_001400230
VERSION     NP_001400230.1
DBSOURCE    REFSEQ: accession NM_001413301.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 322)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 322)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 322)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 322)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC103816.2, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.274900.1,
                                           SRR1660809.34506.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968832 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..322
                     /product="RNA-binding Raly-like protein isoform 11"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=36041
     Region          46..128
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          230..>275
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     CDS             1..322
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413301.1:184..1152"
                     /note="isoform 11 is encoded by transcript variant 28"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mkytrkwqat tlryspwrga wlhrlkqgep imtgktqtsn vtnkndpksi nsrvfignln
       61 taivkkvdie aifskygkiv gcsvhkgyaf vqymserhar aavagenarv iagqpldinm
      121 agepkpyrpk pgnkrplsal yrleskepfl svggyvfdyd yyrddfynrl fdyhgrvppp
      181 praviplkrp rvavtttrrg kgvfsmkggs rstasgstgs klksdelqti kkeltqiktk
      241 idsllgrlek iekqqkaeae aqkkqleesl vliqeecvse iadhsteepa eggpdadgee
      301 mtdgieedfd edgghelflq ik
//
LOCUS       NP_001398022             251 aa            linear   PRI 21-NOV-2025
DEFINITION  MIF4G domain-containing protein isoform 6 [Homo sapiens].
ACCESSION   NP_001398022 XP_047292409
VERSION     NP_001398022.1
DBSOURCE    REFSEQ: accession NM_001411093.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Cakmakci,N.G., Lerner,R.S., Wagner,E.J., Zheng,L. and Marzluff,W.F.
  TITLE     SLIP1, a factor required for activation of histone mRNA translation
            by the stem-loop binding protein
  JOURNAL   Mol Cell Biol 28 (3), 1182-1194 (2008)
   PUBMED   18025107
  REMARK    GeneRIF: downregulation of endogenous SLIP1 reduces the rate of
            translation of endogenous histone mRNA and also reduces cell
            viability.
REFERENCE   8  (residues 1 to 251)
  AUTHORS   Miele,A., Medina,R., van Wijnen,A.J., Stein,G.S. and Stein,J.L.
  TITLE     The interactome of the histone gene regulatory factor HiNF-P
            suggests novel cell cycle related roles in transcriptional control
            and RNA processing
  JOURNAL   J Cell Biochem 102 (1), 136-148 (2007)
   PUBMED   17577209
REFERENCE   9  (residues 1 to 251)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 251)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022211.5.
            
            On Aug 22, 2022 this sequence version replaced XP_047292409.1.
            
            Summary: This gene encodes a protein which interacts with the
            N-terminus of the stem-loop binding protein (SLBP) and the 3' end
            of histone mRNA. This interaction facilitates the activation of
            histone mRNA translation. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jun 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14243140.9512191.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..251
                     /product="MIF4G domain-containing protein isoform 6"
                     /note="SLBP (stem loop binding protein)-interacting
                     protein 1; MIF4G domain-containing protein;
                     SLBP-interacting protein 1"
                     /calculated_mol_wt=28148
     Region          8..208
                     /region_name="MIF4G"
                     /note="MIF4G domain; cl02652"
                     /db_xref="CDD:413423"
     CDS             1..251
                     /gene="MIF4GD"
                     /gene_synonym="AD023; MIFD; SLIP1"
                     /coded_by="NM_001411093.1:340..1095"
                     /note="isoform 6 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS92391.1"
                     /db_xref="GeneID:57409"
                     /db_xref="HGNC:HGNC:24030"
                     /db_xref="MIM:612072"
ORIGIN      
        1 mgepsreeyk iqsfdaetqq llktalkdpg avdlekvanv ivdhslqdcv fskeagrmcy
       61 aiiqaeskqa gqsvfrrgll nrlqqeyqar eqlrarslqg wvcyvtficn ifdylrvnnm
      121 pmmalvnpvy dclfrlaqpd slskeeevgg pspgtstegc rmdspaqpcv splltevdcl
      181 vlqlhrvgeq lekmngqrmd elfvlirdgf llptglssla qlllleiief raagwkttpa
      241 ahkyyysevs d
//
LOCUS       NP_001424667             566 aa            linear   PRI 21-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 9 [Homo sapiens].
ACCESSION   NP_001424667
VERSION     NP_001424667.1
DBSOURCE    REFSEQ: accession NM_001437738.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 566)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 566)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 566)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 566)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 566)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008641.7.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14478891.1347000.1,
                                           SRR14038192.2926558.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..566
                     /product="TNFAIP3-interacting protein 1 isoform 9"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=64091
     Region          <161..>198
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          <245..>485
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..566
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001437738.1:106..1806"
                     /note="isoform 9 is encoded by transcript variant 17"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 meatrlrqka eelvkdnell pppspslgsf dplaeltgkd snvtasptap acpsdkpapv
       61 qkppssgtss efevvtpeeq nspessshan amalgplpre dgnlmlhlqr lettlsvcae
      121 epdhgqlfth lgrmalefnr laskvhkneq rtsilqtlce qlrkenealk akldkgleqr
      181 dqaaerlree nlelkkllms ngnkegasgr pgspkmegtg kkavagqqqa svtagkvpev
      241 valgaaekkv kmleqqrsel levnkqwdqh frsmkqqyeq kitelrqkla dlqkqvtdle
      301 aereqkqrdf drklllaksk iemeetdkeq ltaeakelrq kvkylqdqls pltrqreyqe
      361 keiqrlnkal eealsiqtpp sspptafgsp egagallrkq elvtqnellk qqvkifeedf
      421 qrersdrerm neekeelkkq veklqaqvtl snaqlkafkd eekarealrq qkrkakasge
      481 ryhvephpeh lcgaypyayp pmpamvphhg fedwsqiryp pppmamehpp plpnsrlfhl
      541 hqfcrsrntp gvypvegfei qirapk
//
LOCUS       NP_001428020             670 aa            linear   PRI 21-NOV-2025
DEFINITION  fibroblast growth factor receptor 2 isoform 21 precursor [Homo
            sapiens].
ACCESSION   NP_001428020 XP_016871414 XP_054221149
VERSION     NP_001428020.1
DBSOURCE    REFSEQ: accession NM_001441091.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 670)
  AUTHORS   Chen,C.P., Huang,J.P., Huang,K.S., Chen,Y.Y., Wu,F.T., Pan,Y.T.,
            Chiu,C.L. and Wang,W.
  TITLE     Perinatal imaging findings of a fetus with Pfeiffer syndrome and a
            heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation in FGFR2
            presenting a cloverleaf skull, craniosynostosis and short limbs on
            prenatal ultrasound mimicking thanatophoric dysplasia type II
  JOURNAL   Taiwan J Obstet Gynecol 63 (3), 387-390 (2024)
   PUBMED   38802203
  REMARK    GeneRIF: Perinatal imaging findings of a fetus with Pfeiffer
            syndrome and a heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation
            in FGFR2 presenting a cloverleaf skull, craniosynostosis and short
            limbs on prenatal ultrasound mimicking thanatophoric dysplasia type
            II.
REFERENCE   2  (residues 1 to 670)
  AUTHORS   Lian,Y., Bodian,D. and Shehu,A.
  TITLE     Elucidating the Role of Wildtype and Variant FGFR2 Structural
            Dynamics in (Dys)Function and Disorder
  JOURNAL   Int J Mol Sci 25 (8), 4523 (2024)
   PUBMED   38674107
  REMARK    GeneRIF: Elucidating the Role of Wildtype and Variant FGFR2
            Structural Dynamics in (Dys)Function and Disorder.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 670)
  AUTHORS   Xu,N., Hung,K.L., Gong,X., Fan,D., Tian,Y., Yan,M., Wei,Y. and
            Wang,S.
  TITLE     Genetic insights into the 'sandwich fusion' subtype of Klippel-Feil
            syndrome: novel FGFR2 mutations identified by 21 cases of
            whole-exome sequencing
  JOURNAL   Orphanet J Rare Dis 19 (1), 141 (2024)
   PUBMED   38561822
  REMARK    GeneRIF: Genetic insights into the 'sandwich fusion' subtype of
            Klippel-Feil syndrome: novel FGFR2 mutations identified by 21 cases
            of whole-exome sequencing.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 670)
  AUTHORS   Wenger,T.L., Hing,A.V. and Evans,K.N.
  TITLE     Apert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31145570
REFERENCE   5  (residues 1 to 670)
  AUTHORS   Wenger,T., Miller,D. and Evans,K.
  TITLE     FGFR Craniosynostosis Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301628
REFERENCE   6  (residues 1 to 670)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   7  (residues 1 to 670)
  AUTHORS   Dell,K.R. and Williams,L.T.
  TITLE     A novel form of fibroblast growth factor receptor 2. Alternative
            splicing of the third immunoglobulin-like domain confers ligand
            binding specificity
  JOURNAL   J Biol Chem 267 (29), 21225-21229 (1992)
   PUBMED   1400433
REFERENCE   8  (residues 1 to 670)
  AUTHORS   Luqmani,Y.A., Graham,M. and Coombes,R.C.
  TITLE     Expression of basic fibroblast growth factor, FGFR1 and FGFR2 in
            normal and malignant human breast, and comparison with other normal
            tissues
  JOURNAL   Br J Cancer 66 (2), 273-280 (1992)
   PUBMED   1380281
REFERENCE   9  (residues 1 to 670)
  AUTHORS   Katoh,M., Hattori,Y., Sasaki,H., Tanaka,M., Sugano,K., Yazaki,Y.,
            Sugimura,T. and Terada,M.
  TITLE     K-sam gene encodes secreted as well as transmembrane receptor
            tyrosine kinase
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 2960-2964 (1992)
   PUBMED   1313574
REFERENCE   10 (residues 1 to 670)
  AUTHORS   Miki,T., Bottaro,D.P., Fleming,T.P., Smith,C.L., Burgess,W.H.,
            Chan,A.M. and Aaronson,S.A.
  TITLE     Determination of ligand-binding specificity by alternative
            splicing: two distinct growth factor receptors encoded by a single
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 246-250 (1992)
   PUBMED   1309608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009988.12.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_016871414.1, XP_054221149.1.
            
            Summary: The protein encoded by this gene is a member of the
            fibroblast growth factor receptor family, where amino acid sequence
            is highly conserved between members and throughout evolution. FGFR
            family members differ from one another in their ligand affinities
            and tissue distribution. A full-length representative protein
            consists of an extracellular region, composed of three
            immunoglobulin-like domains, a single hydrophobic membrane-spanning
            segment and a cytoplasmic tyrosine kinase domain. The extracellular
            portion of the protein interacts with fibroblast growth factors,
            setting in motion a cascade of downstream signals, ultimately
            influencing mitogenesis and differentiation. This particular family
            member is a high-affinity receptor for acidic, basic and/or
            keratinocyte growth factor, depending on the isoform. Mutations in
            this gene are associated with Crouzon syndrome, Pfeiffer syndrome,
            Craniosynostosis, Apert syndrome, Jackson-Weiss syndrome,
            Beare-Stevenson cutis gyrata syndrome, Saethre-Chotzen syndrome,
            and syndromic craniosynostosis. Multiple alternatively spliced
            transcript variants encoding different isoforms have been noted for
            this gene. [provided by RefSeq, Jan 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.37544.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:1309608)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..670
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..670
                     /product="fibroblast growth factor receptor 2 isoform 21
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="protein tyrosine kinase, receptor like 14;
                     bacteria-expressed kinase; keratinocyte growth factor
                     receptor; BEK fibroblast growth factor receptor"
                     /calculated_mol_wt=73274
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2298
     Region          39..133
                     /region_name="IgI_2_FGFR"
                     /note="Second immunoglobulin (Ig)-like domain of
                     fibroblast growth factor (FGF) receptor; member of the
                     I-set of IgSF domains; cd05857"
                     /db_xref="CDD:409443"
     Region          39..42
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409443"
     Region          50..55
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409443"
     Site            order(51,53,55)
                     /site_type="other"
                     /note="FGF binding site [polypeptide binding]"
                     /db_xref="CDD:409443"
     Site            order(52,59..61,63)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409443"
     Region          59..67
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409443"
     Region          73..78
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409443"
     Region          81..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409443"
     Region          92..95
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409443"
     Region          99..104
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409443"
     Region          113..120
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409443"
     Region          123..133
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409443"
     Region          141..245
                     /region_name="IgI_3_FGFR2"
                     /note="Third immunoglobulin (Ig)-like domain of fibroblast
                     growth factor receptor 2 (FGFR2); member of the I-set of
                     Ig superfamily (IgSF) domains; cd05858"
                     /db_xref="CDD:409444"
     Region          141..144
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409444"
     Region          148..152
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409444"
     Region          160..167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409444"
     Site            order(165,170..172,201..202,206,210,231)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409444"
     Region          171..178
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409444"
     Region          193..198
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409444"
     Region          210..215
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409444"
     Region          223..231
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409444"
     Region          234..242
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409444"
     Region          339..651
                     /region_name="PTKc_FGFR2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Fibroblast Growth Factor Receptor 2; cd05101"
                     /db_xref="CDD:270679"
     Site            order(370..371,373,378,398,400,417,447..450,454,509,
                     513..514,516,527,545..549,558,592)
                     /site_type="active"
                     /db_xref="CDD:270679"
     Site            order(370..371,373,378,398,400,417,447..450,454,513..514,
                     516,527)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270679"
     Site            order(509,513,545..549,558,592)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270679"
     Site            526..551
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270679"
     CDS             1..670
                     /gene="FGFR2"
                     /gene_synonym="BBDS; BEK; BFR-1; CD332; CEK3; CFD1; ECT1;
                     JWS; K-SAM; KGFR; TK14; TK25"
                     /coded_by="NM_001441091.1:634..2646"
                     /note="isoform 21 precursor is encoded by transcript
                     variant 21"
                     /db_xref="GeneID:2263"
                     /db_xref="HGNC:HGNC:3689"
                     /db_xref="MIM:176943"
ORIGIN      
        1 mvswgrficl vvvtmatlsl arpsfslved ttlepegapy wtntekmekr lhavpaantv
       61 kfrcpaggnp mptmrwlkng kefkqehrig gykvrnqhws limesvvpsd kgnytcvven
      121 eygsinhtyh ldvversphr pilqaglpan astvvggdve fvckvysdaq phiqwikhve
      181 kngskygpdg lpylkvlkaa gvnttdkeie vlyirnvtfe dageytclag nsigisfhsa
      241 wltvlpapgr ekeitaspdy leiaiycigv fliacmvvtv ilcrmknttk kpdfssqpav
      301 hkltkriplr rqvsaessss mnsntplvri ttrlsstadt pmlagvseye lpedpkwefp
      361 rdkltlgkpl gegcfgqvvm aeavgidkdk pkeavtvavk mlkddatekd lsdlvsemem
      421 mkmigkhkni inllgactqd gplyviveya skgnlreylr arrppgmeys ydinrvpeeq
      481 mtfkdlvsct yqlargmeyl asqkcihrdl aarnvlvten nvmkiadfgl ardinnidyy
      541 kkttngrlpv kwmapealfd rvythqsdvw sfgvlmweif tlggspypgi pveelfkllk
      601 eghrmdkpan ctnelymmmr dcwhavpsqr ptfkqlvedl driltlttne eyldlsqple
      661 pyspcypdpr
//
LOCUS       NP_001400605             269 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 9 precursor [Homo sapiens].
ACCESSION   NP_001400605
VERSION     NP_001400605.1
DBSOURCE    REFSEQ: accession NM_001413676.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 269)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 269)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 269)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 269)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 269)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1084238.1,
                                           SRR14038197.1823711.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..269
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 9 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=26529
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..>268
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     CDS             1..269
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413676.1:169..978"
                     /note="isoform 9 precursor is encoded by transcript
                     variant 12"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvlfn
//
LOCUS       NP_001389615            1329 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform d [Homo sapiens].
ACCESSION   NP_001389615
VERSION     NP_001389615.1
DBSOURCE    REFSEQ: accession NM_001402686.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1329)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1329)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1329)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1329)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1329)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1329)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1329)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1329)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1329)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1329)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC143720.1, SRR14038197.1516214.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968968, SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1329
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1329
                     /product="kinectin isoform d"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=152857
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          316..>532
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          448..1269
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1329
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402686.1:1042..5031"
                     /note="isoform d is encoded by transcript variant 11"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqdlkqeika
      841 lkeeignvql ekaqqlsits kvqelqnllk gkeeqmntmk avleekekdl antgkwlqdl
      901 qeeneslkah vqevaqhnlk eassasqfee leivlkeken elkrleamlk eresdlsskt
      961 qllqdvqden klfksqieql kqqnyqqass fppheellkv iserekeisg lwneldslkd
     1021 avehqrkknn dlreknweam ealastekml qdkvnktske rqqqveavel eakevlkklf
     1081 pkvsvpsnls ygewlhgfek kakecmagts gseevkvleh klkeademht llqlecekyk
     1141 svlaetegil qklqrsveqe enkwkvkvde shktikqmqs sftsseqele rlrsenkdie
     1201 nlrrerehle melekaemer styvtevrel kaqlnetltk lrteqnerqk vagdlhkaqq
     1261 sleliqskiv kaagdttvie nsdvspetes seketmsvsl nqtvtqlqql lqavnqqltk
     1321 ekehyqvle
//
LOCUS       NP_001428008            1231 aa            linear   PRI 21-NOV-2025
DEFINITION  cohesin subunit SA-2 isoform b [Homo sapiens].
ACCESSION   NP_001428008 XP_047297738 XP_054182363
VERSION     NP_001428008.1
DBSOURCE    REFSEQ: accession NM_001441079.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1231)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1231)
  AUTHORS   Fischer,A., Hernandez-Rodriguez,B., Mulet-Lazaro,R., Nuetzel,M.,
            Holzl,F., van Herk,S., Kavelaars,F.G., Stanewsky,H., Ackermann,U.,
            Niang,A.H., Diaz,N., Reuschel,E., Strieder,N., Hernandez-Lopez,I.,
            Valk,P.J.M., Vaquerizas,J.M., Rehli,M., Delwel,R. and Gebhard,C.
  TITLE     STAG2 mutations reshape the cohesin-structured spatial chromatin
            architecture to drive gene regulation in acute myeloid leukemia
  JOURNAL   Cell Rep 43 (8), 114498 (2024)
   PUBMED   39084219
  REMARK    GeneRIF: STAG2 mutations reshape the cohesin-structured spatial
            chromatin architecture to drive gene regulation in acute myeloid
            leukemia.
REFERENCE   3  (residues 1 to 1231)
  AUTHORS   Huber,J., Tanasie,N.L., Zernia,S. and Stigler,J.
  TITLE     Single-molecule imaging reveals a direct role of CTCF's zinc
            fingers in SA interaction and cluster-dependent RNA recruitment
  JOURNAL   Nucleic Acids Res 52 (11), 6490-6506 (2024)
   PUBMED   38742641
  REMARK    GeneRIF: Single-molecule imaging reveals a direct role of CTCF's
            zinc fingers in SA interaction and cluster-dependent RNA
            recruitment.
REFERENCE   4  (residues 1 to 1231)
  AUTHORS   Xu,W., Kim,J.S., Yang,T., Ya,A., Sadzewicz,L., Tallon,L.,
            Harris,B.T., Sarkaria,J., Jin,F. and Waldman,T.
  TITLE     STAG2 mutations regulate 3D genome organization, chromatin loops,
            and Polycomb signaling in glioblastoma multiforme
  JOURNAL   J Biol Chem 300 (6), 107341 (2024)
   PUBMED   38705393
  REMARK    GeneRIF: STAG2 mutations regulate 3D genome organization, chromatin
            loops, and Polycomb signaling in glioblastoma multiforme.
REFERENCE   5  (residues 1 to 1231)
  AUTHORS   Ros-Pardo,D., Gomez-Puertas,P. and Marcos-Alcalde,I.
  TITLE     STAG2: Computational Analysis of Missense Variants Involved in
            Disease
  JOURNAL   Int J Mol Sci 25 (2), 1280 (2024)
   PUBMED   38279279
  REMARK    GeneRIF: STAG2: Computational Analysis of Missense Variants
            Involved in Disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1231)
  AUTHORS   Gregson,H.C., Schmiesing,J.A., Kim,J.S., Kobayashi,T., Zhou,S. and
            Yokomori,K.
  TITLE     A potential role for human cohesin in mitotic spindle aster
            assembly
  JOURNAL   J Biol Chem 276 (50), 47575-47582 (2001)
   PUBMED   11590136
REFERENCE   7  (residues 1 to 1231)
  AUTHORS   Sumara,I., Vorlaufer,E., Gieffers,C., Peters,B.H. and Peters,J.M.
  TITLE     Characterization of vertebrate cohesin complexes and their
            regulation in prophase
  JOURNAL   J Cell Biol 151 (4), 749-762 (2000)
   PUBMED   11076961
REFERENCE   8  (residues 1 to 1231)
  AUTHORS   Carramolino,L., Lee,B.C., Zaballos,A., Peled,A., Barthelemy,I.,
            Shav-Tal,Y., Prieto,I., Carmi,P., Gothelf,Y., Gonzalez de
            Buitrago,G., Aracil,M., Marquez,G., Barbero,J.L. and Zipori,D.
  TITLE     SA-1, a nuclear protein encoded by one member of a novel gene
            family: molecular cloning and detection in hemopoietic organs
  JOURNAL   Gene 195 (2), 151-159 (1997)
   PUBMED   9305759
  REMARK    Erratum:[Gene 1998 Jan 12;206(2):283]
REFERENCE   9  (residues 1 to 1231)
  AUTHORS   Wu,C., Friedlander,P., Lamoureux,C., Zannis-Hadjopoulos,M. and
            Price,G.B.
  TITLE     cDNA clones contain autonomous replication activity
  JOURNAL   Biochim Biophys Acta 1174 (3), 241-257 (1993)
   PUBMED   7690594
REFERENCE   10 (residues 1 to 1231)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121601.13 and AL355476.12.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297738.1, XP_054182363.1.
            
            Summary: The protein encoded by this gene is a subunit of the
            cohesin complex, which regulates the separation of sister
            chromatids during cell division. Targeted inactivation of this gene
            results in chromatid cohesion defects and aneuploidy, suggesting
            that genetic disruption of cohesin is a cause of aneuploidy in
            human cancer. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR11853559.34221.1, SRR14038194.2705163.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2142680, SAMEA2142853 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1231
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..1231
                     /product="cohesin subunit SA-2 isoform b"
                     /note="SCC3 homolog 2; cohesin subunit SA-2; SA2
                     stromalin; sister chromatid cohesion 3 homolog B; stromal
                     antigen 2"
                     /calculated_mol_wt=141196
     Region          1..75
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Region          102..>395
                     /region_name="IRR1"
                     /note="Cohesin [Cell division and chromosome
                     partitioning]; COG5537"
                     /db_xref="CDD:227824"
     Region          157..270
                     /region_name="STAG"
                     /note="STAG domain; pfam08514"
                     /db_xref="CDD:462502"
     Site            607
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1058
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1061
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Region          1064..1083
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1064
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35638; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1065
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35638; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1112
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     CDS             1..1231
                     /gene="STAG2"
                     /gene_synonym="bA517O1.1; HPE13; MKMS; NEDXCF; SA-2; SA2;
                     SCC3B"
                     /coded_by="NM_001441079.1:668..4363"
                     /note="isoform b is encoded by transcript variant 19"
                     /db_xref="GeneID:10735"
                     /db_xref="HGNC:HGNC:11355"
                     /db_xref="MIM:300826"
ORIGIN      
        1 miaapeiptd fnllqeseth fssdtdfedi egknqkqgkg ktckkgkkgp aekgkggngg
       61 gkppsgpnrm nghhqqngve nmmlfevvkm gksamqsvvd dwiesykhdr dialldlinf
      121 fiqcsgckgv vtaemfrhmq nseiirkmte efdedsgdyp ltmagpqwkk fkssfcefig
      181 vlvrqcqysi iydeymmdtv islltglsds qvrafrhtst laamklmtal vnvalnlsin
      241 mdntqrqyea ernkmigkra nerlelllqk rkelqenqde ienmmnaifk gvfvhryrda
      301 iaeiraicie eigiwmkmys daflndsylk yvgwtmhdkq gevrlkclta lqglyynkel
      361 nsklelftsr fkdrivsmtl dkeydvavqa iklltlvlqs seevltaedc envyhlvysa
      421 hrpvavaage flykklfsrr dpeedgmmkr rgrqgpnanl vktlvfffle selhehaayl
      481 vdsmwdcate llkdwecmns llleeplsge ealtdrqesa lieimlctir qaaechppvg
      541 rgtgkrvlta kekktqlddr tkitelfava lpqllakysv daekvtnllq lpqyfdleiy
      601 ttgrlekhld allrqirniv ekhtdtdvle acsktyhalc neeftifnrv disrsqlide
      661 ladkfnrlle dflqegeepd eddayqvlst lkritafhna hdlskwdlfa cnykllktgi
      721 engdmpeqiv ihalqcthyv ilwqlakite ssstkedllr lkkqmrvfcq icqhyltnvn
      781 ttvkeqafti lcdilmifsh qimsggrdml eplvytpdss lqsellsfil dhvfieqddd
      841 nnsadgqqed easkiealhk rrnllaafck livytvvemn taadifkqym kyyndygdii
      901 ketmsktrqi dkiqcaktli lslqqlfnem iqengynfdr ssstfsgike larrfaltfg
      961 ldqlktreai amlhkdgief afkepnpqge shpplnlafl dilsefsskl lrqdkrtvyv
     1021 ylekfmtfqm slrredvwlp lmsyrnslla ggdddtmsvi sgissrgstv rskkskpstg
     1081 krkvvegmql slteessssd smwlsreqtl htpvmmqtpq ltstimrepk rlrpedsfms
     1141 vypmqtehhq tpldynrrgt slmeddeepi vedvmmsseg riedlnegmd fdtmdidlpp
     1201 sknrrertel kpdffdpasi mdesvlgvsm f
//
LOCUS       NP_001389613            1330 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 6 [Homo sapiens].
ACCESSION   NP_001389613
VERSION     NP_001389613.1
DBSOURCE    REFSEQ: accession NM_001402684.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1330)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1330)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1330)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1330)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1330)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1330)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1330)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1330)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1330)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1330)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1837682.1,
                                           SRR14038196.1656410.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1330
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1330
                     /product="kinectin isoform 6"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=152956
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          316..>532
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          448..1270
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1330
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402684.1:303..4295"
                     /note="isoform 6 is encoded by transcript variant 9"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqdlkqeika
      841 lkeeignvql ekaqqlsits kvqelqnllk gkeeqmntmk avleekekdl antgkwlqdl
      901 qeeneslkah vqevaqhnlk eassasqfee leivlkeken elkrleamlk eresdlsskt
      961 qllqdvqden klfksqieql kqqnyqqass fppheellkv iserekeisg lwneldslkd
     1021 avehqrkknn dlreknweam ealastekml qdkvnktskv erqqqveave leakevlkkl
     1081 fpkvsvpsnl sygewlhgfe kkakecmagt sgseevkvle hklkeademh tllqleceky
     1141 ksvlaetegi lqklqrsveq eenkwkvkvd eshktikqmq ssftsseqel erlrsenkdi
     1201 enlrrerehl emelekaeme rstyvtevre lkaqlnetlt klrteqnerq kvagdlhkaq
     1261 qsleliqski vkaagdttvi ensdvspete sseketmsvs lnqtvtqlqq llqavnqqlt
     1321 kekehyqvle
//
LOCUS       NP_001393982             557 aa            linear   PRI 21-NOV-2025
DEFINITION  merlin isoform 9 [Homo sapiens].
ACCESSION   NP_001393982
VERSION     NP_001393982.1
DBSOURCE    REFSEQ: accession NM_001407053.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 557)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 557)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 557)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 557)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 557)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 557)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005529.7 and AC004882.3.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2221399.1,
                                           SRR14038196.1739903.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMN03267772
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..557
                     /product="merlin isoform 9"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=65264
     Region          1..184
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          178..274
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(220..221,223..229,238,259,262..263,266)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(220,223..230,238,259,262..263,266)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(256,260)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            259..274
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          269..>329
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          308..427
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          480..557
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..557
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_001407053.1:597..2270"
                     /note="isoform 9 is encoded by transcript variant 14"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 mkwkgkdlfd lvcrtlglre twffglqyti kdtvawlkmd kkvldhdvsk eepvtfhfla
       61 kfypenaeee lvqeitqhlf flqvkkqild ekiycppeas vllasyavqa kygdydpsvh
      121 krgflaqeel lpkrvinlyq mtpemweeri tawyaehrgr ardeaemeyl kiaqdlemyg
      181 vnyfairnkk gtelllgvda lglhiydpen rltpkisfpw neirnisysd keftikpldk
      241 kidvfkfnss klrvnklilq lcignhdlfm rrrkadslev qqmkaqaree karkqmerqr
      301 larekqmree aertrdeler rllqmkeeat manealmrse etadllaeka qiteeeakll
      361 aqkaaeaeqe mqrikatair teeekrlmeq kvleaevlal kmaeeserra keadqlkqdl
      421 qeareaerra kqklleiatk ptyppmnpip aplppdipsf nligdslsfd fkdtdmkrls
      481 meiekekvey mekskhlqeq lnelkteiea lklkeretal dilhnensdr ggsskhntik
      541 kltlqsaksr vaffeel
//
LOCUS       NP_001394271             251 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 40 [Homo sapiens].
ACCESSION   NP_001394271 XP_047288961
VERSION     NP_001394271.1
DBSOURCE    REFSEQ: accession NM_001407342.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 251)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 251)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 251)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            On May 31, 2022 this sequence version replaced XP_047288961.1.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.725733.1,
                                           SRR18074967.1172064.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..251
                     /product="tropomyosin alpha-1 chain isoform 40"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=28831
     Region          12..223
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..251
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407342.1:88..843"
                     /note="isoform 40 is encoded by transcript variant 40"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 magsssleav rrkirslqeq adaaeeragt lqreldherk lretaeadva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkviesraqk deekmeiqei qlkeakhiae
      121 dadrkyeeva rklviiesdl eraeeraels egqvrqleeq lrimdqtlka lmaaedkysq
      181 kedryeeeik vlsdklkeae traefaersv tkleksiddl edkflcftsp ktpssswmsh
      241 lselciclfs s
//
LOCUS       NP_001427617             307 aa            linear   PRI 21-NOV-2025
DEFINITION  dual specificity mitogen-activated protein kinase kinase 2 isoform
            2 [Homo sapiens].
ACCESSION   NP_001427617 XP_006722862 XP_054177439
VERSION     NP_001427617.1
DBSOURCE    REFSEQ: accession NM_001440688.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Wan,Y., Zhao,Y., Cao,M., Wang,J., Tran,S.V., Song,Z., Hsueh,B.W.
            and Wang,S.E.
  TITLE     Lung Fibroblasts Take up Breast Cancer Cell-derived Extracellular
            Vesicles Partially Through MEK2-dependent Macropinocytosis
  JOURNAL   Cancer Res Commun 4 (1), 170-181 (2024)
   PUBMED   38259097
  REMARK    GeneRIF: Lung Fibroblasts Take up Breast Cancer Cell-derived
            Extracellular Vesicles Partially Through MEK2-dependent
            Macropinocytosis.
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Gong,K.Q., Mikacenic,C., Long,M.E., Frevert,C.W., Birkland,T.P.,
            Charron,J., Gharib,S.A. and Manicone,A.M.
  TITLE     MAP2K2 Delays Recovery in Murine Models of Acute Lung Injury and
            Associates with Acute Respiratory Distress Syndrome Outcome
  JOURNAL   Am J Respir Cell Mol Biol 66 (5), 555-563 (2022)
   PUBMED   35157553
  REMARK    GeneRIF: MAP2K2 Delays Recovery in Murine Models of Acute Lung
            Injury and Associates with Acute Respiratory Distress Syndrome
            Outcome.
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 307)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   7  (residues 1 to 307)
  AUTHORS   Derijard,B., Raingeaud,J., Barrett,T., Wu,I.H., Han,J.,
            Ulevitch,R.J. and Davis,R.J.
  TITLE     Independent human MAP-kinase signal transduction pathways defined
            by MEK and MKK isoforms
  JOURNAL   Science 267 (5198), 682-685 (1995)
   PUBMED   7839144
  REMARK    Erratum:[Science 1995 Jul 7;269(5220):17]
REFERENCE   8  (residues 1 to 307)
  AUTHORS   Alessi,D.R., Saito,Y., Campbell,D.G., Cohen,P., Sithanandam,G.,
            Rapp,U., Ashworth,A., Marshall,C.J. and Cowley,S.
  TITLE     Identification of the sites in MAP kinase kinase-1 phosphorylated
            by p74raf-1
  JOURNAL   EMBO J 13 (7), 1610-1619 (1994)
   PUBMED   8157000
REFERENCE   9  (residues 1 to 307)
  AUTHORS   Charest,D.L., Mordret,G., Harder,K.W., Jirik,F. and Pelech,S.L.
  TITLE     Molecular cloning, expression, and characterization of the human
            mitogen-activated protein kinase p44erk1
  JOURNAL   Mol Cell Biol 13 (8), 4679-4690 (1993)
   PUBMED   7687743
REFERENCE   10 (residues 1 to 307)
  AUTHORS   Rauen,K.A.
  TITLE     Cardiofaciocutaneous Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301365
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016586.9.
            
            On or before May 23, 2025 this sequence version replaced
            XP_006722862.1, XP_054177439.1.
            
            Summary: The protein encoded by this gene is a dual specificity
            protein kinase that belongs to the MAP kinase kinase family. This
            kinase is known to play a critical role in mitogen growth factor
            signal transduction. It phosphorylates and thus activates
            MAPK1/ERK2 and MAPK2/ERK3. The activation of this kinase itself is
            dependent on the Ser/Thr phosphorylation by MAP kinase kinase
            kinases. Mutations in this gene cause cardiofaciocutaneous syndrome
            (CFC syndrome), a disease characterized by heart defects, cognitive
            disability, and distinctive facial features similar to those found
            in Noonan syndrome. The inhibition or degradation of this kinase is
            also found to be involved in the pathogenesis of Yersinia and
            anthrax. A pseudogene, which is located on chromosome 7, has been
            identified for this gene. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138524.942531.1,
                                           ERR4352444.324782.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..307
                     /product="dual specificity mitogen-activated protein
                     kinase kinase 2 isoform 2"
                     /EC_number="2.7.12.2"
                     /note="MAP kinase kinase 2; MAPK/ERK kinase 2; dual
                     specificity mitogen-activated protein kinase kinase 2; ERK
                     activator kinase 2; mitogen-activated protein kinase
                     kinase 2, p45"
                     /calculated_mol_wt=34095
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P36507.1)"
     Site            10..11
                     /site_type="cleavage"
                     /note="Cleavage, by anthrax lethal factor; propagated from
                     UniProtKB/Swiss-Prot (P36507.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P36507.1)"
     Region          70..294
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(78..81,84,86,99,101,131,147..150,194,198..199,201,
                     211..212)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:132946"
     Site            222
                     /site_type="acetylation"
                     /note="(Microbial infection) O-acetylserine, by Yersinia
                     YopJ, alternate. /evidence=ECO:0000269|PubMed:17116858;
                     propagated from UniProtKB/Swiss-Prot (P36507.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RAF, alternate.
                     /evidence=ECO:0000269|PubMed:10409742,
                     ECO:0000269|PubMed:17116858; propagated from
                     UniProtKB/Swiss-Prot (P36507.1)"
     Site            226
                     /site_type="acetylation"
                     /note="(Microbial infection) O-acetylserine, by Yersinia
                     YopJ, alternate. /evidence=ECO:0000269|PubMed:17116858;
                     propagated from UniProtKB/Swiss-Prot (P36507.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0000269|PubMed:17116858; propagated from
                     UniProtKB/Swiss-Prot (P36507.1)"
     CDS             1..307
                     /gene="MAP2K2"
                     /gene_synonym="CFC4; MAPKK2; MEK2; MKK2; PRKMK2"
                     /coded_by="NM_001440688.1:248..1171"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:5605"
                     /db_xref="HGNC:HGNC:6842"
                     /db_xref="MIM:601263"
ORIGIN      
        1 mlarrkpvlp altinptiae gpsptsegas eanlvdlqkk leeleldeqq kkrleafltq
       61 kakvgelkdd dferiselga gnggvvtkvq hrpsglimar klihleikpa irnqiirelq
      121 vlhecnspyi vgfygafysd geisicmehm dggsldqvlk eakripeeil gkvsiavlrg
      181 laylrekhqi mhrdvkpsni lvnsrgeikl cdfgvsgqli dsmansfvgt rsymapppkl
      241 pngvftpdfq efvnkclikn paeradlkml tnhtfikrse veevdfagwl cktlrlnqpg
      301 tptrtav
//
LOCUS       NP_001389638            1093 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 18 [Homo sapiens].
ACCESSION   NP_001389638
VERSION     NP_001389638.1
DBSOURCE    REFSEQ: accession NM_001402709.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1093)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1093)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1093)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1093)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1093)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1093)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1093)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1093)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.152713.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1093
                     /product="kinectin isoform 18"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=125936
     Region          132..>348
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          274..1033
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1093
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402709.1:178..3459"
                     /note="isoform 18 is encoded by transcript variant 32"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mvpskrqeal plhqetkqes gsgkkkassk kqktenvfvd eplihattyi plmdnadssp
       61 vvdkrevidl lkpdqvegiq ksgtkklkte tdkenaevkf kdfllslktm mfsedealcv
      121 vdllkeksgv iqdalkkssk gelttlihql qekdkllaav kedaaatkdr ckqltqemmt
      181 ekersnvvit rmkdrigtle kehnvfqnki hvsyqetqqm qmkfqqvreq meaeiahlkq
      241 engilrdavs nttnqleskq saelnklrqd yarlvnelte ktgklqqeev qkknaeqaat
      301 qlkvqlqeae rrweevqsyi rkrtaeheaa qqdlqskfva kenevqslhs kltdtlvskq
      361 qleqrlmqlm eseqkrvnke eslqmqvqdi leqnealkaq iqqfhsqiaa qtsasvlaee
      421 lhkviaekdk qikqtedsla serdrltske eelkdiqnmn fllkaevqkl qalaneqaaa
      481 ahelekmqqs vyvkddkirl leeqlqheis nkmeefkiln dqnkalksev qklqtlvseq
      541 pnkdvveqme kciqekdekl ktveelletg liqvatkeee lnairtenss ltkevqdlka
      601 kqndqvsfas lveelkkvih ekdgkiksve elleaellkv ankektvqls itskvqelqn
      661 llkgkeeqmn tmkavleeke kdlantgkwl qdlqeenesl kahvqevaqh nlkeassasq
      721 feeleivlke kenelkrlea mlkeresdls sktqllqdvq denklfksqi eqlkqqnyqq
      781 assfppheel lkvisereke isglwnelds lkdavehqrk knnerqqqve aveleakevl
      841 kklfpkvsvp snlsygewlh gfekkakecm agtsgseevk vlehklkead emhtllqlec
      901 ekyksvlaet egilqklqrs veqeenkwkv kvdeshktik qmqssftsse qelerlrsen
      961 kdienlrrer ehlemeleka emerstyvte vrelkaqlne tltklrteqn erqkvagdlh
     1021 kaqqsleliq skivkaagdt tviensdvsp etesseketm svslnqtvtq lqqllqavnq
     1081 qltkekehyq vle
//
LOCUS       NP_001424259             959 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, NMDA 1 isoform 6 precursor [Homo
            sapiens].
ACCESSION   NP_001424259 XP_005266130 XP_054218781
VERSION     NP_001424259.1
DBSOURCE    REFSEQ: accession NM_001437330.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Korinek,M., Candelas Serra,M., Abdel Rahman,F., Dobrovolski,M.,
            Kuchtiak,V., Abramova,V., Fili,K., Tomovic,E., Hrcka Krausova,B.,
            Krusek,J., Cerny,J., Vyklicky,L., Balik,A. and Smejkalova,T.
  TITLE     Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B genes:
            Insights into NMDA Receptor Structure, Function, and
            Pathophysiology
  JOURNAL   Physiol Res 73 (Suppl 1), S413-S434 (2024)
   PUBMED   38836461
  REMARK    GeneRIF: Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B
            genes: Insights into NMDA Receptor Structure, Function, and
            Pathophysiology.
            Review article
REFERENCE   2  (residues 1 to 959)
  AUTHORS   Michalski,K. and Furukawa,H.
  TITLE     Structure and function of GluN1-3A NMDA receptor excitatory glycine
            receptor channel
  JOURNAL   Sci Adv 10 (15), eadl5952 (2024)
   PUBMED   38598639
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Xu,Y., Song,R., Perszyk,R.E., Chen,W., Kim,S., Park,K.L.,
            Allen,J.P., Nocilla,K.A., Zhang,J., XiangWei,W., Tankovic,A.,
            McDaniels,E.D., Sheikh,R., Mizu,R.K., Karamchandani,M.M., Hu,C.,
            Kusumoto,H., Pecha,J., Cappuccio,G., Gaitanis,J., Sullivan,J.,
            Shashi,V., Petrovski,S., Jauss,R.T., Lee,H.K., Bozarth,X.,
            Lynch,D.R., Helbig,I., Pierson,T.M., Boerkoel,C.F., Myers,S.J.,
            Lemke,J.R., Benke,T.A., Yuan,H. and Traynelis,S.F.
  TITLE     De novo GRIN variants in M3 helix associated with neurological
            disorders control channel gating of NMDA receptor
  JOURNAL   Cell Mol Life Sci 81 (1), 153 (2024)
   PUBMED   38538865
  REMARK    GeneRIF: De novo GRIN variants in M3 helix associated with
            neurological disorders control channel gating of NMDA receptor.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 959)
  AUTHORS   Ragnarsson,L., Zhang,Z., Das,S.S., Tran,P., Andersson,A., des
            Portes,V., Desmettre Altuzarra,C., Remerand,G., Labalme,A.,
            Chatron,N., Sanlaville,D., Lesca,G., Anggono,V., Vetter,I. and
            Keramidas,A.
  TITLE     GRIN1 variants associated with neurodevelopmental disorders reveal
            channel gating pathomechanisms
  JOURNAL   Epilepsia 64 (12), 3377-3388 (2023)
   PUBMED   37734923
  REMARK    GeneRIF: GRIN1 variants associated with neurodevelopmental
            disorders reveal channel gating pathomechanisms.
REFERENCE   5  (residues 1 to 959)
  AUTHORS   McNearney,T.A. and Westlund,K.N.
  TITLE     Pluripotential GluN1 (NMDA NR1): Functional Significance in
            Cellular Nuclei in Pain/Nociception
  JOURNAL   Int J Mol Sci 24 (17), 13196 (2023)
   PUBMED   37686003
  REMARK    GeneRIF: Pluripotential GluN1 (NMDA NR1): Functional Significance
            in Cellular Nuclei in Pain/Nociception.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 959)
  AUTHORS   Zimmer,M., Fink,T.M., Franke,Y., Lichter,P. and Spiess,J.
  TITLE     Cloning and structure of the gene encoding the human
            N-methyl-D-aspartate receptor (NMDAR1)
  JOURNAL   Gene 159 (2), 219-223 (1995)
   PUBMED   7622053
REFERENCE   7  (residues 1 to 959)
  AUTHORS   Younkin,D.P., Tang,C.M., Hardy,M., Reddy,U.R., Shi,Q.Y.,
            Pleasure,S.J., Lee,V.M. and Pleasure,D.
  TITLE     Inducible expression of neuronal glutamate receptor channels in the
            NT2 human cell line
  JOURNAL   Proc Natl Acad Sci U S A 90 (6), 2174-2178 (1993)
   PUBMED   7681588
REFERENCE   8  (residues 1 to 959)
  AUTHORS   Karp,S.J., Masu,M., Eki,T., Ozawa,K. and Nakanishi,S.
  TITLE     Molecular cloning and chromosomal localization of the key subunit
            of the human N-methyl-D-aspartate receptor
  JOURNAL   J Biol Chem 268 (5), 3728-3733 (1993)
   PUBMED   7679115
REFERENCE   9  (residues 1 to 959)
  AUTHORS   Platzer,K. and Lemke,J.R.
  TITLE     GRIN1-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31219694
REFERENCE   10 (residues 1 to 959)
  AUTHORS   Monyer,H., Sprengel,R., Schoepfer,R., Herb,A., Higuchi,M.,
            Lomeli,H., Burnashev,N., Sakmann,B. and Seeburg,P.H.
  TITLE     Heteromeric NMDA receptors: molecular and functional distinction of
            subtypes
  JOURNAL   Science 256 (5060), 1217-1221 (1992)
   PUBMED   1350383
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL929554.20.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_005266130.1, XP_054218781.1.
            
            Summary: The protein encoded by this gene is a critical subunit of
            N-methyl-D-aspartate receptors, members of the glutamate receptor
            channel superfamily which are heteromeric protein complexes with
            multiple subunits arranged to form a ligand-gated ion channel.
            These subunits play a key role in the plasticity of synapses, which
            is believed to underlie memory and learning. Cell-specific factors
            are thought to control expression of different isoforms, possibly
            contributing to the functional diversity of the subunits.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2145743,
                              SAMEA2154665 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..959
                     /product="glutamate receptor ionotropic, NMDA 1 isoform 6
                     precursor"
                     /note="N-methyl-D-aspartate receptor channel, subunit
                     zeta-1; glutamate [NMDA] receptor subunit zeta-1;
                     N-methyl-D-aspartate receptor subunit NR1; glutamate
                     receptor ionotropic, NMDA 1; glutamate receptor,
                     ionotropic, N-methyl D-aspartate 1; putative
                     NMDtranscript(altAcc_e2)"
                     /calculated_mol_wt=105742
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2185
     Region          25..404
                     /region_name="PBP1_iGluR_NMDA_NR1"
                     /note="N-terminal leucine-isoleucine-valine-binding
                     protein (LIVBP)-like domain of the NR1, an essential
                     channel-forming subunit of the NMDA receptor; cd06379"
                     /db_xref="CDD:380602"
     Site            order(69..72,76,79,113,340,344,363)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:380602"
     Site            order(69..73,75..76,79..80,113..114,131,135,329..331,
                     340..341,343..344)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:380602"
     Region          416..820
                     /region_name="PBP2_iGluR_NMDA_Nr1"
                     /note="The ligand-binding domain of the NR1 subunit of
                     ionotropic NMDA (N-methyl-D-aspartate) glutamate
                     receptors, a member of the type 2 periplasmic binding fold
                     protein superfamily; cd13719"
                     /db_xref="CDD:270437"
     Site            order(537..540,542,544..546,689,708..709,713,753,774..776,
                     779,785,801..804,807)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270437"
     Site            order(537..539,544,708..710,752..753)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270437"
     Region          856..884
                     /region_name="CaM_bdg_C0"
                     /note="Calmodulin-binding domain C0 of NMDA receptor NR1
                     subunit; pfam10562"
                     /db_xref="CDD:402271"
     CDS             1..959
                     /gene="GRIN1"
                     /gene_synonym="DEE101; GluN1; hNR1; MRD8; NDHMSD; NDHMSR;
                     NMD-R1; NMDA1; NMDAR1; NR1"
                     /coded_by="NM_001437330.1:334..3213"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:2902"
                     /db_xref="HGNC:HGNC:4584"
                     /db_xref="MIM:138249"
ORIGIN      
        1 mstmrlltla llfscsvara acdpkivnig avlstrkheq mfreavnqan krhgswkiql
       61 natsvthkpn aiqmalsvce dlissqvyai lvshpptpnd hftptpvsyt agfyripvlg
      121 lttrmsiysd ksihlsflrt vppyshqssv wfemmrvysw nhiillvsdd hegraaqkrl
      181 etlleeresk skkrnyenld qlsydnkrgp kaekvlqfdp gtknvtallm eakelearvi
      241 ilsaseddaa tvyraaamln mtgsgyvwlv gereisgnal ryapdgilgl qlingknesa
      301 hisdavgvva qavhelleke nitdpprgcv gntniwktgp lfkrvlmssk yadgvtgrve
      361 fnedgdrkfa nysimnlqnr klvqvgiyng thvipndrki iwpggetekp rgyqmstrlk
      421 ivtihqepfv yvkptlsdgt ckeeftvngd pvkkvictgp ndtspgsprh tvpqccygfc
      481 idlliklart mnftyevhlv adgkfgtqer vnnsnkkewn gmmgellsgq admivaplti
      541 nneraqyief skpfkyqglt ilvkkeiprs tldsfmqpfq stlwllvgls vhvvavmlyl
      601 ldrfspfgrf kvnseeeeed altlssamwf swgvllnsgi gegaprsfsa rilgmvwagf
      661 amiivasyta nlaaflvldr peeritgind prlrnpsdkf iyatvkqssv diyfrrqvel
      721 stmyrhmekh nyesaaeaiq avrdnklhaf iwdsavlefe asqkcdlvtt gelffrsgfg
      781 igmrkdspwk qnvslsilks hengfmedld ktwvryqecd srsnapatlt fenmagvfml
      841 vaggivagif lifieiaykr hkdarrkqmq lafaavnvwr knlqdrksgr aepdpkkkat
      901 fraitstlas sfkrrrsskd tstgggrgal qnqkdtvlpr raiereegql qlcsrhres
//
LOCUS       NP_001425601             740 aa            linear   PRI 21-NOV-2025
DEFINITION  dipeptidyl peptidase 8 isoform 10 [Homo sapiens].
ACCESSION   NP_001425601 XP_047288723 XP_054234287
VERSION     NP_001425601.1
DBSOURCE    REFSEQ: accession NM_001438672.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Li,K., Zhang,Y., Zhao,W., Wang,R., Li,Y., Wei,L., Wang,L., Chen,X.,
            Chen,Z., Liu,P., Nie,N., Tian,X. and Fu,R.
  TITLE     DPP8/9 inhibition attenuates the TGF-beta1-induced excessive
            deposition of extracellular matrix (ECM) in human mesangial cells
            via Smad and Akt signaling pathways
  JOURNAL   Toxicol Lett 395, 1-10 (2024)
   PUBMED   38458339
  REMARK    GeneRIF: DPP8/9 inhibition attenuates the TGF-beta1-induced
            excessive deposition of extracellular matrix (ECM) in human
            mesangial cells via Smad and Akt signaling pathways.
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Zhang,Y., Li,K., Li,Y., Zhao,W., Wang,L., Chen,Z., Ma,X., Yao,T.,
            Wang,J., Dong,W., Li,X., Tian,X. and Fu,R.
  TITLE     Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the
            proximal renal tubule epithelial cells
  JOURNAL   Pharmacol Res 169, 105630 (2021)
   PUBMED   33932609
  REMARK    GeneRIF: Profibrotic mechanisms of DPP8 and DPP9 highly expressed
            in the proximal renal tubule epithelial cells.
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 740)
  AUTHORS   Hollingsworth,L.R., Sharif,H., Griswold,A.R., Fontana,P.,
            Mintseris,J., Dagbay,K.B., Paulo,J.A., Gygi,S.P., Bachovchin,D.A.
            and Wu,H.
  TITLE     DPP9 sequesters the C terminus of NLRP1 to repress inflammasome
            activation
  JOURNAL   Nature 592 (7856), 778-783 (2021)
   PUBMED   33731932
REFERENCE   6  (residues 1 to 740)
  AUTHORS   Chen,Y.S., Chien,C.H., Goparaju,C.M., Hsu,J.T., Liang,P.H. and
            Chen,X.
  TITLE     Purification and characterization of human prolyl dipeptidase DPP8
            in Sf9 insect cells
  JOURNAL   Protein Expr Purif 35 (1), 142-146 (2004)
   PUBMED   15039077
REFERENCE   7  (residues 1 to 740)
  AUTHORS   Shu,H., Chen,S., Bi,Q., Mumby,M. and Brekken,D.L.
  TITLE     Identification of phosphoproteins and their phosphorylation sites
            in the WEHI-231 B lymphoma cell line
  JOURNAL   Mol Cell Proteomics 3 (3), 279-286 (2004)
   PUBMED   14729942
REFERENCE   8  (residues 1 to 740)
  AUTHORS   Qi,S.Y., Riviere,P.J., Trojnar,J., Junien,J.L. and Akinsanya,K.O.
  TITLE     Cloning and characterization of dipeptidyl peptidase 10, a new
            member of an emerging subgroup of serine proteases
  JOURNAL   Biochem J 373 (Pt 1), 179-189 (2003)
   PUBMED   12662155
REFERENCE   9  (residues 1 to 740)
  AUTHORS   Ajami,K., Abbott,C.A., Obradovic,M., Gysbers,V., Kahne,T.,
            McCaughan,G.W. and Gorrell,M.D.
  TITLE     Structural requirements for catalysis, expression, and dimerization
            in the CD26/DPIV gene family
  JOURNAL   Biochemistry 42 (3), 694-701 (2003)
   PUBMED   12534281
REFERENCE   10 (residues 1 to 740)
  AUTHORS   Abbott,C.A., Yu,D.M., Woollatt,E., Sutherland,G.R., McCaughan,G.W.
            and Gorrell,M.D.
  TITLE     Cloning, expression and chromosomal localization of a novel human
            dipeptidyl peptidase (DPP) IV homolog, DPP8
  JOURNAL   Eur J Biochem 267 (20), 6140-6150 (2000)
   PUBMED   11012666
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011846.16 and AC105129.4.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047288723.1, XP_054234287.1.
            
            Summary: This gene encodes a member of the peptidase S9B family, a
            small family of dipeptidyl peptidases that are able to cleave
            peptide substrates at a prolyl bond. The encoded protein shares
            similarity with dipeptidyl peptidase IV in that it is ubiquitously
            expressed, and hydrolyzes the same substrates. These similarities
            suggest that, like dipeptidyl peptidase IV, this protein may play a
            role in T-cell activation and immune function. Alternatively
            spliced transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.2955637.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..740
                     /product="dipeptidyl peptidase 8 isoform 10"
                     /EC_number="3.4.14.5"
                     /note="prolyl dipeptidase DPP8; dipeptidyl peptidase VIII;
                     DPP VIII; dipeptidyl peptidase IV-related protein 1"
                     /calculated_mol_wt=85299
     Region          8..143
                     /region_name="Dpp_8_9_N"
                     /note="Dipeptidyl peptidase 8 and 9 N-terminal; pfam19520"
                     /db_xref="CDD:466112"
     Region          142..537
                     /region_name="DPPIV_N"
                     /note="Dipeptidyl peptidase IV (DPP IV) N-terminal region;
                     pfam00930"
                     /db_xref="CDD:395744"
     Region          <615..733
                     /region_name="Peptidase_S9"
                     /note="Prolyl oligopeptidase family; pfam00326"
                     /db_xref="CDD:459761"
     CDS             1..740
                     /gene="DPP8"
                     /gene_synonym="DP8; DPRP-1; DPRP1; MST097; MSTP097;
                     MSTP135; MSTP141"
                     /coded_by="NM_001438672.1:169..2391"
                     /note="isoform 10 is encoded by transcript variant 14"
                     /db_xref="GeneID:54878"
                     /db_xref="HGNC:HGNC:16490"
                     /db_xref="MIM:606819"
ORIGIN      
        1 mwkrseqmki ksgkcnmaaa meteqlgvei fetadceeni esqdrpklep fyveryswsq
       61 lkklladtrk yhgymmakap hdfmfvkrnd pdgphsdriy ylamsgenre ntlfyseipk
      121 tinraavlml swkplldlfq qqplrpnlve tscpnirmdp klcpadpdwi afihsndiwi
      181 snivtreerr ltyvhnelan meedarsagv atfvlqeefd rysgywwcpk aettpsggki
      241 lrilyeende seveiihvts pmletrrads frypktgtan pkvtfkmsei midaegriid
      301 vidkeliqpf eilfegveyi aragwtpegk yawsilldrs qtrlqivlis pelfipvedd
      361 vmerqrlies vpdsvtplii yeettdiwin ihdifhvfpq sheeeiefif asecktgfrh
      421 lykitsilke skykrssggl papsdfkcpi keeiaitsge wevlgrhgsn iqvdevrrlv
      481 yfegtkdspl ehhlyvvsyv npgevtrltd rgyshsccis qhcdffisky snqknphcvs
      541 lyklsspedd ptcktkefwa tildsagplp dytppeifsf esttgftlyg mlykphdlqp
      601 gkkyptvlfi yggpqvaiag apvtlwifyd tgyterymgh pdqneqgyyl gsvamqaekf
      661 psepnrllll hgfldenvhf ahtsillsfl vragkpydlq iypqerhsir vpesgehyel
      721 hllhylqenl gsriaalkvi
//
LOCUS       NP_001397697            1144 aa            linear   PRI 21-NOV-2025
DEFINITION  voltage-dependent calcium channel subunit alpha-2/delta-2 isoform e
            precursor [Homo sapiens].
ACCESSION   NP_001397697 XP_005265638
VERSION     NP_001397697.1
DBSOURCE    REFSEQ: accession NM_001410768.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1144)
  AUTHORS   Westhoff,M. and Dixon,R.E.
  TITLE     Mechanisms and Regulation of Cardiac CaV1.2 Trafficking
  JOURNAL   Int J Mol Sci 22 (11), 5927 (2021)
   PUBMED   34072954
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1144)
  AUTHORS   Dolphin,A.C.
  TITLE     Voltage-gated calcium channels and their auxiliary subunits:
            physiology and pathophysiology and pharmacology
  JOURNAL   J Physiol 594 (19), 5369-5390 (2016)
   PUBMED   27273705
  REMARK    Review article
REFERENCE   3  (residues 1 to 1144)
  AUTHORS   Warnier,M., Roudbaraki,M., Derouiche,S., Delcourt,P., Bokhobza,A.,
            Prevarskaya,N. and Mariot,P.
  TITLE     CACNA2D2 promotes tumorigenesis by stimulating cell proliferation
            and angiogenesis
  JOURNAL   Oncogene 34 (42), 5383-5394 (2015)
   PUBMED   25619833
  REMARK    GeneRIF: show that the action of alpha2delta2 on tumor development
            occurs not only through a stimulation of proliferation
REFERENCE   4  (residues 1 to 1144)
  AUTHORS   Pippucci,T., Parmeggiani,A., Palombo,F., Maresca,A., Angius,A.,
            Crisponi,L., Cucca,F., Liguori,R., Valentino,M.L., Seri,M. and
            Carelli,V.
  TITLE     A novel null homozygous mutation confirms CACNA2D2 as a gene
            mutated in epileptic encephalopathy
  JOURNAL   PLoS One 8 (12), e82154 (2013)
   PUBMED   24358150
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1144)
  AUTHORS   Rhodin,A., Gronbladh,A., Ginya,H., Nilsson,K.W., Rosenblad,A.,
            Zhou,Q., Enlund,M., Hallberg,M., Gordh,T. and Nyberg,F.
  TITLE     Combined analysis of circulating beta-endorphin with gene
            polymorphisms in OPRM1, CACNAD2 and ABCB1 reveals correlation with
            pain, opioid sensitivity and opioid-related side effects
  JOURNAL   Mol Brain 6, 8 (2013)
   PUBMED   23402298
  REMARK    GeneRIF: The investigation of single nucleotide polymorphisms in
            three genes that have a functional impact on the opioid response:
            OPRM1, ABCB1 and the calcium channel complex subunit CACNA2D2, is
            reported.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1144)
  AUTHORS   Edvardson,S., Oz,S., Abulhijaa,F.A., Taher,F.B., Shaag,A.,
            Zenvirt,S., Dascal,N. and Elpeleg,O.
  TITLE     Early infantile epileptic encephalopathy associated with a high
            voltage gated calcium channelopathy
  JOURNAL   J Med Genet 50 (2), 118-123 (2013)
   PUBMED   23339110
REFERENCE   7  (residues 1 to 1144)
  AUTHORS   Angeloni,D., Duh,F.M., Wei,M.F., Johnson,B.E. and Lerman,M.I.
  TITLE     A G-to-A single nucleotide polymorphism in intron 2 of the human
            CACNA2D2 gene that maps at 3p21.3
  JOURNAL   Mol Cell Probes 15 (2), 125-127 (2001)
   PUBMED   11292331
REFERENCE   8  (residues 1 to 1144)
  AUTHORS   Lerman,M.I. and Minna,J.D.
  TITLE     The 630-kb lung cancer homozygous deletion region on human
            chromosome 3p21.3: identification and evaluation of the resident
            candidate tumor suppressor genes. The International Lung Cancer
            Chromosome 3p21.3 Tumor Suppressor Gene Consortium
  JOURNAL   Cancer Res 60 (21), 6116-6133 (2000)
   PUBMED   11085536
REFERENCE   9  (residues 1 to 1144)
  AUTHORS   Gao,B., Sekido,Y., Maximov,A., Saad,M., Forgacs,E., Latif,F.,
            Wei,M.H., Lerman,M., Lee,J.H., Perez-Reyes,E., Bezprozvanny,I. and
            Minna,J.D.
  TITLE     Functional properties of a new voltage-dependent calcium channel
            alpha(2)delta auxiliary subunit gene (CACNA2D2)
  JOURNAL   J Biol Chem 275 (16), 12237-12242 (2000)
   PUBMED   10766861
REFERENCE   10 (residues 1 to 1144)
  AUTHORS   Hobom,M., Dai,S., Marais,E., Lacinova,L., Hofmann,F. and
            Klugbauer,N.
  TITLE     Neuronal distribution and functional characterization of the
            calcium channel alpha2delta-2 subunit
  JOURNAL   Eur J Neurosci 12 (4), 1217-1226 (2000)
   PUBMED   10762351
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL450422.2, Z84494.1, Z75743.1,
            Z75742.1 and Z84492.2.
            
            On Aug 15, 2022 this sequence version replaced XP_005265638.1.
            
            Summary: Calcium channels mediate the entry of calcium ions into
            the cell upon membrane polarization. This gene encodes the
            alpha-2/delta subunit of the voltage-dependent calcium channel
            complex. The complex consists of the main channel-forming subunit
            alpha-1, and auxiliary subunits alpha-2/delta, beta, and gamma. The
            auxiliary subunits function in the assembly and membrane
            localization of the complex, and modulate calcium currents and
            channel activation/inactivation kinetics. The subunit encoded by
            this gene undergoes post-translational cleavage to yield the
            extracellular alpha2 peptide and a membrane-anchored delta
            polypeptide. This subunit is a receptor for the antiepileptic drug,
            gabapentin. Mutations in this gene are associated with early
            infantile epileptic encephalopathy. Single nucleotide polymorphisms
            in this gene are correlated with increased sensitivity to opioid
            drugs. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Mar 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1588828.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1144
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1144
                     /product="voltage-dependent calcium channel subunit
                     alpha-2/delta-2 isoform e precursor"
                     /note="gene 26; alpha 2 delta calcium channel subunit;
                     voltage-gated calcium channel subunit alpha-2/delta-2;
                     calcium channel, voltage-dependent, alpha 2/delta subunit
                     2; alpha2delta-2"
                     /calculated_mol_wt=127433
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NY47.2)"
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NY47.2)"
                     /calculated_mol_wt=1799
     Region          141..265
                     /region_name="VWA_N"
                     /note="VWA N-terminal; pfam08399"
                     /db_xref="CDD:462464"
     Region          277..456
                     /region_name="vWA_VGCC_like"
                     /note="VWA Voltage gated Calcium channel like:
                     Voltage-gated calcium channels are a complex of five
                     proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The
                     alpha 2 and delta subunits result from proteolytic
                     processing of a single gene product and carries at...;
                     cd01463"
                     /db_xref="CDD:238740"
     Site            order(297,299,301,369,401)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238740"
     Region          297..301
                     /region_name="MIDAS-like motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NY47.2)"
     Site            386
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q9NY47.2)"
     Site            418
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NY47.2)"
     Region          <448..531
                     /region_name="HK_sensor"
                     /note="Sensor domains of Histidine Kinase receptors;
                     cl38916"
                     /db_xref="CDD:365792"
     Site            507
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NY47.2)"
     Region          533..642
                     /region_name="HK_sensor"
                     /note="Sensor domains of Histidine Kinase receptors;
                     cl38916"
                     /db_xref="CDD:365792"
     Site            540
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NY47.2)"
     Site            624
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NY47.2)"
     Region          662..1105
                     /region_name="VGCC_alpha2"
                     /note="Neuronal voltage-dependent calcium channel alpha
                     2acd; pfam08473"
                     /db_xref="CDD:462488"
     Site            854
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NY47.2)"
     mat_peptide     996..1144
                     /product="Voltage-dependent calcium channel subunit
                     delta-2. /evidence=ECO:0000255. /id=PRO_0000304639"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NY47.2)"
                     /calculated_mol_wt=16537
     Site            1108..1128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NY47.2)"
     CDS             1..1144
                     /gene="CACNA2D2"
                     /gene_synonym="CACNA2D; CASVDD"
                     /coded_by="NM_001410768.1:212..3646"
                     /note="isoform e precursor is encoded by transcript
                     variant 5"
                     /db_xref="CCDS:CCDS93278.1"
                     /db_xref="GeneID:9254"
                     /db_xref="HGNC:HGNC:1400"
                     /db_xref="MIM:607082"
ORIGIN      
        1 mavpartcga srpgpartar pwpgcgphpg pgtrrptsgp prplwlllpl lpllaapgas
       61 aysfpqqhtm qhwarrleqe vdgvmrifgg vqqlreiykd nrnlfevqen epqklvekva
      121 gdieslldrk vqalkrlada aenfqkahrw qdnikeediv yydakadael ddpesedver
      181 gskastlrld fiedpnfknk vnysyaavqi ptdiykgstv ilnelnwtea lenvfmenrr
      241 qdptllwqvf gsatgvtryy patpwrapkk idlydvrrrp wyiqgasspk dmviivdvsg
      301 svsgltlklm ktsvcemldt lsdddyvnva sfnekaqpvs cfthlvqanv rnkkvfkeav
      361 qgmvakgttg ykagfeyafd qlqnsnitra ncnkmimmft dggedrvqdv fekynwpnrt
      421 vrvftfsvgq hnydvtplqw macankgyyf eipsigairi ntqeyldvlg rpmvlagkea
      481 kqvqwtnvye dalglglvvt gtlpvfnltq dgpgekknql ilgvmgidva lndikrltpn
      541 ytlgangyvf aidlngyvll hpnlkpqttn frepvtldfl daeledenke eirrsmidgn
      601 kghkqirtlv kslderyide vtrnytwvpi rstnyslglv lppystfylq anlsdqilqv
      661 kyfefllpss feseghvfia preyckdlna sdnnteflkn fielmekvtp dskqcnnfll
      721 hnlildtgit qqlvervwrd qdlntyslla vfaatdggit rvfpnkaaed wtenpepfna
      781 sfyrrsldnh gyvfkpphqd allrplelen dtvgilvsta velslgrrtl rpavvgvkld
      841 leawaekfkv lasnrthqdq pqkqcgpnsh cemdcevnne dllcvliddg gflvlsnqnh
      901 qwdqvgrffs evdanlmlal ynnsfytrke sydyqaacap qppgnlgaap rgvfvptvad
      961 flnlawwtsa aawslfqqll ygliyhswfq adpaeaegsp etresscvmk qtqyyfgsvn
     1021 asynaiidcg ncsrlfhaqr ltntnllfvv aekplcsqce agrllqketh sdgpeqcelv
     1081 qrpryrrgph icfdynated tsdcgrgasf ppslgvlvsl qlllllglpp rpqpqvlvha
     1141 srrl
//
LOCUS       NP_001428158             344 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 12 [Homo sapiens].
ACCESSION   NP_001428158
VERSION     NP_001428158.1
DBSOURCE    REFSEQ: accession NM_001441229.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 344)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 344)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 344)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.100432.1,
                                           SRR14038191.1420890.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..344
                     /product="calcium uptake protein 1, mitochondrial isoform
                     12"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=35465
     transit_peptide 1..33
                     /note="Mitochondrion. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:26387864; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
                     /calculated_mol_wt=3784
     Region          68..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          99..110
                     /region_name="Polybasic region.
                     /evidence=ECO:0000269|PubMed:27099988"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCX5; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          126..129
                     /region_name="K/R-ring.
                     /evidence=ECO:0000269|PubMed:32494073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          <232..309
                     /region_name="EFh_MICU"
                     /note="EF-hand, calcium binding motif, found in
                     mitochondrial calcium uptake proteins MICU1, MICU2, MICU3,
                     and similar proteins; cl28896"
                     /db_xref="CDD:333716"
     Region          243..272
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320080"
     Region          280..309
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320080"
     CDS             1..344
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001441229.1:72..1106"
                     /note="isoform 12 is encoded by transcript variant 16"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mfrlnslsal aelavgsrwy hggsqpiqir rrlmmvaflg asavtastgl lwkrahaesp
       61 pcvdnlksdi gdkgknkdeg dvcnhekkta dlaphpeekk kkrsgfrdrk vmeyenrira
      121 ystpdkifry fatlkvisep geaevfmtpe dfvrsitpne kqpehlgldq yiikrfdgkf
      181 erhdpvdgri terqfggmll aysgvqskkl tamqrqlkkh fkegkgltfq evenfftflk
      241 nindvdtals fyhmagasld kvtmqqvart vakvelsdhv cdvvfalfdc dgngelsnke
      301 fvsimkqrlm rglekpkdmg ftrlmqamwk caqetawdfa lpkq
//
LOCUS       NP_001337542             294 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/arginine-rich splicing factor 11 isoform 7 [Homo sapiens].
ACCESSION   NP_001337542 XP_016858315
VERSION     NP_001337542.1
DBSOURCE    REFSEQ: accession NM_001350613.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Oh,J., Oh,J.M. and Cho,S.Y.
  TITLE     METTL3-mediated downregulation of splicing factor SRSF11 is
            associated with carcinogenesis and poor survival of cancer patients
  JOURNAL   Eur Rev Med Pharmacol Sci 27 (6), 2561-2570 (2023)
   PUBMED   37013774
  REMARK    GeneRIF: METTL3-mediated downregulation of splicing factor SRSF11
            is associated with carcinogenesis and poor survival of cancer
            patients.
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Pan,Y.J., Huo,F.C., Kang,M.J., Liu,B.W., Wu,M.D. and Pei,D.S.
  TITLE     Alternative splicing of HSPA12A pre-RNA by SRSF11 contributes to
            metastasis potential of colorectal cancer
  JOURNAL   Clin Transl Med 12 (11), e1113 (2022)
   PUBMED   36394206
  REMARK    GeneRIF: Alternative splicing of HSPA12A pre-RNA by SRSF11
            contributes to metastasis potential of colorectal cancer.
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Manley,J.L. and Krainer,A.R.
  TITLE     A rational nomenclature for serine/arginine-rich protein splicing
            factors (SR proteins)
  JOURNAL   Genes Dev 24 (11), 1073-1074 (2010)
   PUBMED   20516191
REFERENCE   7  (residues 1 to 294)
  AUTHORS   Page-McCaw,P.S., Amonlirdviman,K. and Sharp,P.A.
  TITLE     PUF60: a novel U2AF65-related splicing activity
  JOURNAL   RNA 5 (12), 1548-1560 (1999)
   PUBMED   10606266
REFERENCE   8  (residues 1 to 294)
  AUTHORS   Straub,T., Grue,P., Uhse,A., Lisby,M., Knudsen,B.R., Tange,T.O.,
            Westergaard,O. and Boege,F.
  TITLE     The RNA-splicing factor PSF/p54 controls DNA-topoisomerase I
            activity by a direct interaction
  JOURNAL   J Biol Chem 273 (41), 26261-26264 (1998)
   PUBMED   9756848
REFERENCE   9  (residues 1 to 294)
  AUTHORS   Zhang,W.J. and Wu,J.Y.
  TITLE     Functional properties of p54, a novel SR protein active in
            constitutive and alternative splicing
  JOURNAL   Mol Cell Biol 16 (10), 5400-5408 (1996)
   PUBMED   8816452
REFERENCE   10 (residues 1 to 294)
  AUTHORS   Chaudhary,N., McMahon,C. and Blobel,G.
  TITLE     Primary structure of a human arginine-rich nuclear protein that
            colocalizes with spliceosome components
  JOURNAL   Proc Natl Acad Sci U S A 88 (18), 8189-8193 (1991)
   PUBMED   1896467
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC415520.1, DA157431.1,
            AL353771.8, DA581964.1, AL532192.3, BM716576.1, CA417788.1,
            BG494115.1, CN294419.1, BF680379.1 and AI002238.1.
            
            On Apr 20, 2017 this sequence version replaced XP_016858315.1.
            
            Summary: This gene encodes 54-kD nuclear protein that contains an
            arginine/serine-rich region similar to segments found in pre-mRNA
            splicing factors. Although the function of this protein is not yet
            known, structure and immunolocalization data suggest that it may
            play a role in pre-mRNA processing. Alternative splicing results in
            multiple transcript variants encoding different proteins. In
            addition, a pseudogene of this gene has been found on chromosome
            12.[provided by RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1549643.1,
                                           SRR1660805.226307.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.1"
     Protein         1..294
                     /product="serine/arginine-rich splicing factor 11 isoform
                     7"
                     /note="splicing factor, arginine/serine-rich 11; SR
                     splicing factor 11; arginine-rich 54 kDa nuclear protein;
                     splicing factor p54; serine/arginine-rich splicing factor
                     11"
                     /calculated_mol_wt=34671
     CDS             1..294
                     /gene="SRSF11"
                     /gene_synonym="dJ677H15.2; NET2; p54; SFRS11"
                     /coded_by="NM_001350613.2:945..1829"
                     /note="isoform 7 is encoded by transcript variant 11"
                     /db_xref="GeneID:9295"
                     /db_xref="HGNC:HGNC:10782"
                     /db_xref="MIM:602010"
ORIGIN      
        1 mstvdpklnh vaaglvspsl ksdtsskeie eamkrvreaq slisaaiepd kkeekrrhsr
       61 srsrsrrrrt psssrhrrsr srsrrrshsk srsrrrsksp rrrrshsrer grrsrstskt
      121 rdkkkedkek krsktppksy starrsrsas rerrrrrsrs gtrspkkprs pkrklsrsps
      181 prrhkkekkk dkdkersrde rerstskkkk skdkekdrer ksesdkdvkq vtrdydeeeq
      241 gydsekekke ekkpietgsp ktkecsvekg tgdslreskv ngddhheedm dmsd
//
LOCUS       NP_001393983             554 aa            linear   PRI 21-NOV-2025
DEFINITION  merlin isoform 10 [Homo sapiens].
ACCESSION   NP_001393983
VERSION     NP_001393983.1
DBSOURCE    REFSEQ: accession NM_001407054.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 554)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 554)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 554)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 554)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 554)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 554)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 554)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005529.7 and AC004882.3.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2524981.1,
                                           SRR14038191.2508649.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..554
                     /product="merlin isoform 10"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=64659
     Region          23..181
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          175..271
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(217..218,220..226,235,256,259..260,263)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(217,220..227,235,256,259..260,263)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(253,257)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            256..271
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          266..>326
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          305..424
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          477..554
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..554
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_001407054.1:367..2031"
                     /note="isoform 10 is encoded by transcript variant 16"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 magaiasrms fsslkrkqpk tftvrivtmd aemefncemk wkgkdlfdlv crtlglretw
       61 ffglqytikd tvawlkmdkk vkkqildeki ycppeasvll asyavqakyg dydpsvhkrg
      121 flaqeellpk rvinlyqmtp emweeritaw yaehrgrard eaemeylkia qdlemygvny
      181 fairnkkgte lllgvdalgl hiydpenrlt pkisfpwnei rnisysdkef tikpldkkid
      241 vfkfnssklr vnklilqlci gnhdlfmrrr kadslevqqm kaqareekar kqmerqrlar
      301 ekqmreeaer trdelerrll qmkeeatman ealmrseeta dllaekaqit eeeakllaqk
      361 aaeaeqemqr ikatairtee ekrlmeqkvl eaevlalkma eeserrakea dqlkqdlqea
      421 reaerrakqk lleiatkpty ppmnpipapl ppdipsfnli gdslsfdfkd tdmkrlsmei
      481 ekekveymek skhlqeqlne lkteiealkl keretaldil hnensdrggs skhntikklt
      541 lqsaksrvaf feel
//
LOCUS       NP_001400617             290 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 21 precursor [Homo sapiens].
ACCESSION   NP_001400617
VERSION     NP_001400617.1
DBSOURCE    REFSEQ: accession NM_001413688.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 290)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 290)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 290)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC100850.2.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR3218372.761384.1,
                                           SRR14038195.919726.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..290
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 21 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=28662
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..>264
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     CDS             1..290
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413688.1:169..1041"
                     /note="isoform 21 precursor is encoded by transcript
                     variant 24"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvtgss pvaqagvqwr dhsllltsks
//
LOCUS       NP_001397876            1288 aa            linear   PRI 21-NOV-2025
DEFINITION  synaptojanin-2 isoform 3 [Homo sapiens].
ACCESSION   NP_001397876 XP_047275427
VERSION     NP_001397876.1
DBSOURCE    REFSEQ: accession NM_001410947.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1288)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1288)
  AUTHORS   Hou,W., Li,G.S., Gao,L., Lu,H.P., Zhou,H.F., Kong,J.L., Chen,G.,
            Xia,S. and Wei,H.Y.
  TITLE     SYNJ2 is a novel and potential biomarker for the prediction and
            treatment of cancers: from lung squamous cell carcinoma to
            pan-cancer
  JOURNAL   BMC Med Genomics 15 (1), 114 (2022)
   PUBMED   35581615
  REMARK    GeneRIF: SYNJ2 is a novel and potential biomarker for the
            prediction and treatment of cancers: from lung squamous cell
            carcinoma to pan-cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1288)
  AUTHORS   Zhang,R., Mo,W.J., Huang,L.S., Chen,J.T., Wu,W.Z., He,W.Y. and
            Feng,Z.B.
  TITLE     Identifying the Prognostic Risk Factors of Synaptojanin 2 and Its
            Underlying Perturbations Pathways in Hepatocellular Carcinoma
  JOURNAL   Bioengineered 12 (1), 855-874 (2021)
   PUBMED   33641617
  REMARK    GeneRIF: Identifying the Prognostic Risk Factors of Synaptojanin 2
            and Its Underlying Perturbations Pathways in Hepatocellular
            Carcinoma.
REFERENCE   4  (residues 1 to 1288)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1288)
  AUTHORS   Kennedy,S.A., Jarboui,M.A., Srihari,S., Raso,C., Bryan,K.,
            Dernayka,L., Charitou,T., Bernal-Llinares,M., Herrera-Montavez,C.,
            Krstic,A., Matallanas,D., Kotlyar,M., Jurisica,I., Curak,J.,
            Wong,V., Stagljar,I., LeBihan,T., Imrie,L., Pillai,P., Lynn,M.A.,
            Fasterius,E., Al-Khalili Szigyarto,C., Breen,J., Kiel,C.,
            Serrano,L., Rauch,N., Rukhlenko,O., Kholodenko,B.N.,
            Iglesias-Martinez,L.F., Ryan,C.J., Pilkington,R., Cammareri,P.,
            Sansom,O., Shave,S., Auer,M., Horn,N., Klose,F., Ueffing,M.,
            Boldt,K., Lynn,D.J. and Kolch,W.
  TITLE     Extensive rewiring of the EGFR network in colorectal cancer cells
            expressing transforming levels of KRASG13D
  JOURNAL   Nat Commun 11 (1), 499 (2020)
   PUBMED   31980649
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1288)
  AUTHORS   Spaenij-Dekking,E.H., Van Delft,J., Van Der Meijden,E.,
            Hiemstra,H.S., Falkenburg,J.H., Koning,F., Drijfhout,J.W. and
            Kluin-Nelemans,J.C.
  TITLE     Synaptojanin 2 is recognized by HLA class II-restricted hairy cell
            leukemia-specific T cells
  JOURNAL   Leukemia 17 (12), 2467-2473 (2003)
   PUBMED   14562116
  REMARK    GeneRIF: Since Syn 2 is a phosphatidylinositol 4,5-biphosphatase
            involved in cell growth and rearrangement of actin filaments, the
            increased Syn 2 expression may correlate with the hairy cell
            leukemia etiology or the characteristic morphologic alterations.
REFERENCE   7  (residues 1 to 1288)
  AUTHORS   Zhong,R. and Ye,Z.H.
  TITLE     The SAC domain-containing protein gene family in Arabidopsis
  JOURNAL   Plant Physiol 132 (2), 544-555 (2003)
   PUBMED   12805586
REFERENCE   8  (residues 1 to 1288)
  AUTHORS   Rusk,N., Le,P.U., Mariggio,S., Guay,G., Lurisci,C., Nabi,I.R.,
            Corda,D. and Symons,M.
  TITLE     Synaptojanin 2 functions at an early step of clathrin-mediated
            endocytosis
  JOURNAL   Curr Biol 13 (8), 659-663 (2003)
   PUBMED   12699622
  REMARK    Erratum:[Curr Biol. 2003 Sep 30;13(19):1746]
REFERENCE   9  (residues 1 to 1288)
  AUTHORS   Nemoto,Y., Wenk,M.R., Watanabe,M., Daniell,L., Murakami,T.,
            Ringstad,N., Yamada,H., Takei,K. and De Camilli,P.
  TITLE     Identification and characterization of a synaptojanin 2 splice
            isoform predominantly expressed in nerve terminals
  JOURNAL   J Biol Chem 276 (44), 41133-41142 (2001)
   PUBMED   11498538
REFERENCE   10 (residues 1 to 1288)
  AUTHORS   Malecz,N., McCabe,P.C., Spaargaren,C., Qiu,R., Chuang,Y. and
            Symons,M.
  TITLE     Synaptojanin 2, a novel Rac1 effector that regulates
            clathrin-mediated endocytosis
  JOURNAL   Curr Biol 10 (21), 1383-1386 (2000)
   PUBMED   11084340
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139330.17.
            
            On Aug 18, 2022 this sequence version replaced XP_047275427.1.
            
            Summary: The gene is a member of the inositol-polyphosphate
            5-phosphatase family. The encoded protein interacts with the
            ras-related C3 botulinum toxin substrate 1, which causes
            translocation of the encoded protein to the plasma membrane where
            it inhibits clathrin-mediated endocytosis. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, May
            2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1936723.1,
                                           SRR14038191.3765756.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..1288
                     /product="synaptojanin-2 isoform 3"
                     /EC_number="3.1.3.36"
                     /note="inositol phosphate 5'-phosphatase 2; synaptic
                     inositol 1,4,5-trisphosphate 5-phosphatase 2;
                     phosphoinositide 5-phosphatase; inositol
                     polyphosphate-5-phosphatase H"
                     /calculated_mol_wt=143315
     Region          13..485
                     /region_name="COG5329"
                     /note="Phosphoinositide polyphosphatase (Sac family)
                     [Signal transduction mechanisms]"
                     /db_xref="CDD:227637"
     Region          530..861
                     /region_name="EEP"
                     /note="Exonuclease-Endonuclease-Phosphatase (EEP) domain
                     superfamily; cl00490"
                     /db_xref="CDD:469791"
     Site            order(538,587,685,726,728,802,854..855)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197306"
     Site            order(587,854)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197306"
     Site            order(685,728,855)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197306"
     Region          872..1008
                     /region_name="DUF1866"
                     /note="Domain of unknown function (DUF1866); pfam08952"
                     /db_xref="CDD:286093"
     Region          1027..1073
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15056.3)"
     Region          1085..1166
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15056.3)"
     Site            1124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15056.3)"
     Site            1191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O15056.3)"
     CDS             1..1288
                     /gene="SYNJ2"
                     /gene_synonym="INPP5H"
                     /coded_by="NM_001410947.1:100..3966"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS94025.1"
                     /db_xref="GeneID:8871"
                     /db_xref="HGNC:HGNC:11504"
                     /db_xref="MIM:609410"
ORIGIN      
        1 malskglrll grlgaegdcs vlleargrdd cllfeagtva tlapeekevi kgqygkltda
       61 ygclgelrlk sggtslsflv lvtgctsvgr ipdaeiykit atdfyplqee akeeerlial
      121 kkilssgvfy fswpndgsrf dltvrtqkqg ddssewgnsf fwnqllhvpl rqhqvsccdw
      181 llkiicgvvt irtvyashkq akaclvsrvs certgtrfht rgvnddghvs nfveteqmiy
      241 mddgvssfvq irgsvplfwe qpglqvgshh lrlhrglean apafdrhmvl lkeqygqqvv
      301 vnllgsrgge evlnrafkkl lwaschagdt pminfdfhqf akggklekle tllrpqlklh
      361 wedfdvftkg envsprfqkg tlrmncldcl drtntvqsfi alevlhlqlk tlglsskpiv
      421 drfvesfkam wslnghslsk vftgsraleg kakvgklkdg arsmsrtiqs nffdgvkqea
      481 iklllvgdvy geevadkggm lldstallvt prilkamter qseftnfkri riamgtwnvn
      541 ggkqfrsnvl rtaeltdwll dspqlsgatd sqddsspadi favgfeemve lsagnivnas
      601 ttnkkmwgeq lqkaisrshr yilltsaqlv gvclyifvrp yhvpfirdva idtvktgmgg
      661 kagnkgavgi rfqfhstsfc ficshltagq sqvkernedy keitqklcfp mgrnvfshdy
      721 vfwcgdfnyr idltyeevfy fvkrqdwkkl lefdqlqlqk ssgkifkdfh egainfgpty
      781 kydvgsaayd tsdkcrtpaw tdrvlwwrkk hpfdktagel nlldsdldvd tkvrhtwspg
      841 alqyygrael qasdhrpvla ivevevqevd vgarervfqe vssfqgplda tvvvnlqspt
      901 leeknefped lrtelmqtlg sygtivlvri nqgqmlvtfa dshsalsvld vdgmkvkgra
      961 vkirpktkdw lkglreeiir krdsmapvsp tansclleen fdftsldyes egdiledded
     1021 ylvdefnqpg vsdselggdd lsdvpgptal appskspalt kkkqhptykd dadlvelkre
     1081 leavgefrhr spsrslsvpn rprppqppqr pppptglmvk ksasdasiss gthgqysilq
     1141 tarllpgapq qppkartgis kpynvkqikt tnaqeaeaai rclleargga seealsavap
     1201 rdleassepe ptpgaakpet pqappllprr ppprvpaikk ptlrrtgkiv fcsrsqasqp
     1261 clllqrhefv rtvaaqrlas vdtsgssv
//
LOCUS       NP_001411262             194 aa            linear   PRI 21-NOV-2025
DEFINITION  protein cholesin isoform a [Homo sapiens].
ACCESSION   NP_001411262 XP_054215197
VERSION     NP_001411262.1
DBSOURCE    REFSEQ: accession NM_001424333.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Ryk,A., Marcinkiewicz,A., Chrzanowski,J., Michalak,A.M., Drozdz,I.,
            Burzynski,J., Krejca,M. and Fendler,W.
  TITLE     Cholesin receptor signalling is active in cardiovascular
            system-associated adipose tissue and correlates with SGLT2i
            treatment in patients with diabetes
  JOURNAL   Cardiovasc Diabetol 23 (1), 211 (2024)
   PUBMED   38902687
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Hu,X., Chen,F., Jia,L., Long,A., Peng,Y., Li,X., Huang,J., Wei,X.,
            Fang,X., Gao,Z., Zhang,M., Liu,X., Chen,Y.G., Wang,Y., Zhang,H. and
            Wang,Y.
  TITLE     A gut-derived hormone regulates cholesterol metabolism
  JOURNAL   Cell 187 (7), 1685-1700 (2024)
   PUBMED   38503280
  REMARK    GeneRIF: A gut-derived hormone regulates cholesterol metabolism.
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 194)
  AUTHORS   Willer,C.J., Schmidt,E.M., Sengupta,S., Peloso,G.M., Gustafsson,S.,
            Kanoni,S., Ganna,A., Chen,J., Buchkovich,M.L., Mora,S.,
            Beckmann,J.S., Bragg-Gresham,J.L., Chang,H.Y., Demirkan,A., Den
            Hertog,H.M., Do,R., Donnelly,L.A., Ehret,G.B., Esko,T.,
            Feitosa,M.F., Ferreira,T., Fischer,K., Fontanillas,P., Fraser,R.M.,
            Freitag,D.F., Gurdasani,D., Heikkila,K., Hypponen,E., Isaacs,A.,
            Jackson,A.U., Johansson,A., Johnson,T., Kaakinen,M., Kettunen,J.,
            Kleber,M.E., Li,X., Luan,J., Lyytikainen,L.P., Magnusson,P.K.E.,
            Mangino,M., Mihailov,E., Montasser,M.E., Muller-Nurasyid,M.,
            Nolte,I.M., O'Connell,J.R., Palmer,C.D., Perola,M., Petersen,A.K.,
            Sanna,S., Saxena,R., Service,S.K., Shah,S., Shungin,D., Sidore,C.,
            Song,C., Strawbridge,R.J., Surakka,I., Tanaka,T., Teslovich,T.M.,
            Thorleifsson,G., Van den Herik,E.G., Voight,B.F., Volcik,K.A.,
            Waite,L.L., Wong,A., Wu,Y., Zhang,W., Absher,D., Asiki,G.,
            Barroso,I., Been,L.F., Bolton,J.L., Bonnycastle,L.L., Brambilla,P.,
            Burnett,M.S., Cesana,G., Dimitriou,M., Doney,A.S.F., Doring,A.,
            Elliott,P., Epstein,S.E., Ingi Eyjolfsson,G., Gigante,B.,
            Goodarzi,M.O., Grallert,H., Gravito,M.L., Groves,C.J., Hallmans,G.,
            Hartikainen,A.L., Hayward,C., Hernandez,D., Hicks,A.A., Holm,H.,
            Hung,Y.J., Illig,T., Jones,M.R., Kaleebu,P., Kastelein,J.J.P.,
            Khaw,K.T., Kim,E., Klopp,N., Komulainen,P., Kumari,M.,
            Langenberg,C., Lehtimaki,T., Lin,S.Y., Lindstrom,J., Loos,R.J.F.,
            Mach,F., McArdle,W.L., Meisinger,C., Mitchell,B.D., Muller,G.,
            Nagaraja,R., Narisu,N., Nieminen,T.V.M., Nsubuga,R.N., Olafsson,I.,
            Ong,K.K., Palotie,A., Papamarkou,T., Pomilla,C., Pouta,A.,
            Rader,D.J., Reilly,M.P., Ridker,P.M., Rivadeneira,F., Rudan,I.,
            Ruokonen,A., Samani,N., Scharnagl,H., Seeley,J., Silander,K.,
            Stancakova,A., Stirrups,K., Swift,A.J., Tiret,L.,
            Uitterlinden,A.G., van Pelt,L.J., Vedantam,S., Wainwright,N.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilsgaard,T., Wilson,J.F.,
            Young,E.H., Zhao,J.H., Adair,L.S., Arveiler,D., Assimes,T.L.,
            Bandinelli,S., Bennett,F., Bochud,M., Boehm,B.O., Boomsma,D.I.,
            Borecki,I.B., Bornstein,S.R., Bovet,P., Burnier,M., Campbell,H.,
            Chakravarti,A., Chambers,J.C., Chen,Y.I., Collins,F.S.,
            Cooper,R.S., Danesh,J., Dedoussis,G., de Faire,U., Feranil,A.B.,
            Ferrieres,J., Ferrucci,L., Freimer,N.B., Gieger,C., Groop,L.C.,
            Gudnason,V., Gyllensten,U., Hamsten,A., Harris,T.B., Hingorani,A.,
            Hirschhorn,J.N., Hofman,A., Hovingh,G.K., Hsiung,C.A.,
            Humphries,S.E., Hunt,S.C., Hveem,K., Iribarren,C., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kaprio,J., Kesaniemi,A., Kivimaki,M.,
            Kooner,J.S., Koudstaal,P.J., Krauss,R.M., Kuh,D., Kuusisto,J.,
            Kyvik,K.O., Laakso,M., Lakka,T.A., Lind,L., Lindgren,C.M.,
            Martin,N.G., Marz,W., McCarthy,M.I., McKenzie,C.A., Meneton,P.,
            Metspalu,A., Moilanen,L., Morris,A.D., Munroe,P.B., Njolstad,I.,
            Pedersen,N.L., Power,C., Pramstaller,P.P., Price,J.F., Psaty,B.M.,
            Quertermous,T., Rauramaa,R., Saleheen,D., Salomaa,V.,
            Sanghera,D.K., Saramies,J., Schwarz,P.E.H., Sheu,W.H.,
            Shuldiner,A.R., Siegbahn,A., Spector,T.D., Stefansson,K.,
            Strachan,D.P., Tayo,B.O., Tremoli,E., Tuomilehto,J., Uusitupa,M.,
            van Duijn,C.M., Vollenweider,P., Wallentin,L., Wareham,N.J.,
            Whitfield,J.B., Wolffenbuttel,B.H.R., Ordovas,J.M., Boerwinkle,E.,
            Palmer,C.N.A., Thorsteinsdottir,U., Chasman,D.I., Rotter,J.I.,
            Franks,P.W., Ripatti,S., Cupples,L.A., Sandhu,M.S., Rich,S.S.,
            Boehnke,M., Deloukas,P., Kathiresan,S., Mohlke,K.L., Ingelsson,E.
            and Abecasis,G.R.
  CONSRTM   Global Lipids Genetics Consortium
  TITLE     Discovery and refinement of loci associated with lipid levels
  JOURNAL   Nat Genet 45 (11), 1274-1283 (2013)
   PUBMED   24097068
REFERENCE   7  (residues 1 to 194)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 194)
  AUTHORS   Yashin,A.I., Wu,D., Arbeev,K.G. and Ukraintseva,S.V.
  TITLE     Joint influence of small-effect genetic variants on human longevity
  JOURNAL   Aging (Albany NY) 2 (9), 612-620 (2010)
   PUBMED   20834067
REFERENCE   9  (residues 1 to 194)
  AUTHORS   Satoh,J., Obayashi,S., Misawa,T., Sumiyoshi,K., Oosumi,K. and
            Tabunoki,H.
  TITLE     Protein microarray analysis identifies human cellular prion protein
            interactors
  JOURNAL   Neuropathol Appl Neurobiol 35 (1), 16-35 (2009)
   PUBMED   18482256
REFERENCE   10 (residues 1 to 194)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CP068271.2.
            
            On Sep 21, 2023 this sequence version replaced XP_054215197.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BQ049678.1, BM464700.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465413 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..194
                     /product="protein cholesin isoform a"
                     /note="uncharacterized protein C7orf50; protein cholesin"
                     /calculated_mol_wt=21952
     Region          1..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Region          104..165
                     /region_name="WKF"
                     /note="WKF domain; pfam10180"
                     /db_xref="CDD:462982"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     CDS             1..194
                     /gene="CHLSN"
                     /gene_synonym="C7orf50; YCR016W"
                     /coded_by="NM_001424333.1:42..626"
                     /note="isoform a is encoded by transcript variant 26"
                     /db_xref="GeneID:84310"
                     /db_xref="HGNC:HGNC:22421"
                     /db_xref="MIM:621174"
ORIGIN      
        1 makqkrkvpe vtekknkklk kasaegpllg peaapsgega gskgeavlrp gldaepelsp
       61 eeqrvlerkl kkerkkeerq rlreaglvaq hpparrsgae laldylcrwa qkhknwrfqk
      121 trqtwlllhm ydsdkvpdeh fstllayleg lqgrareltv qkaealmrel deegsdpplp
      181 graqrirqvl qlls
//
LOCUS       NP_001424674             566 aa            linear   PRI 21-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 9 [Homo sapiens].
ACCESSION   NP_001424674
VERSION     NP_001424674.1
DBSOURCE    REFSEQ: accession NM_001437745.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 566)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 566)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 566)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 566)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 566)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008641.7.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1867787.1,
                                           SRR14038192.605942.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..566
                     /product="TNFAIP3-interacting protein 1 isoform 9"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=64091
     Region          <161..>198
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          <245..>485
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..566
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001437745.1:179..1879"
                     /note="isoform 9 is encoded by transcript variant 25"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 meatrlrqka eelvkdnell pppspslgsf dplaeltgkd snvtasptap acpsdkpapv
       61 qkppssgtss efevvtpeeq nspessshan amalgplpre dgnlmlhlqr lettlsvcae
      121 epdhgqlfth lgrmalefnr laskvhkneq rtsilqtlce qlrkenealk akldkgleqr
      181 dqaaerlree nlelkkllms ngnkegasgr pgspkmegtg kkavagqqqa svtagkvpev
      241 valgaaekkv kmleqqrsel levnkqwdqh frsmkqqyeq kitelrqkla dlqkqvtdle
      301 aereqkqrdf drklllaksk iemeetdkeq ltaeakelrq kvkylqdqls pltrqreyqe
      361 keiqrlnkal eealsiqtpp sspptafgsp egagallrkq elvtqnellk qqvkifeedf
      421 qrersdrerm neekeelkkq veklqaqvtl snaqlkafkd eekarealrq qkrkakasge
      481 ryhvephpeh lcgaypyayp pmpamvphhg fedwsqiryp pppmamehpp plpnsrlfhl
      541 hqfcrsrntp gvypvegfei qirapk
//
LOCUS       NP_001425898             725 aa            linear   PRI 21-NOV-2025
DEFINITION  transcriptional repressor CTCF isoform 3 [Homo sapiens].
ACCESSION   NP_001425898 XP_005255832 XP_054235374
VERSION     NP_001425898.1
DBSOURCE    REFSEQ: accession NM_001438969.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 725)
  AUTHORS   Ma,D.B., Zhang,H., Wang,X.L. and Wu,Q.G.
  TITLE     METTL3 aggravates cell damage induced by Streptococcus pneumoniae
            via the NEAT1/CTCF/MUC19 axis
  JOURNAL   Kaohsiung J Med Sci 40 (8), 722-731 (2024)
   PUBMED   38757482
  REMARK    GeneRIF: METTL3 aggravates cell damage induced by Streptococcus
            pneumoniae via the NEAT1/CTCF/MUC19 axis.
REFERENCE   3  (residues 1 to 725)
  AUTHORS   Zhang,J., Hu,G., Lu,Y., Ren,H., Huang,Y., Wen,Y., Ji,B., Wang,D.,
            Wang,H., Liu,H., Ma,N., Zhang,L., Pan,G., Qu,Y., Wang,H., Zhang,W.,
            Miao,Z. and Yao,H.
  TITLE     CTCF mutation at R567 causes developmental disorders via 3D genome
            rearrangement and abnormal neurodevelopment
  JOURNAL   Nat Commun 15 (1), 5524 (2024)
   PUBMED   38951485
  REMARK    GeneRIF: CTCF mutation at R567 causes developmental disorders via
            3D genome rearrangement and abnormal neurodevelopment.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 725)
  AUTHORS   Pandey,A., Kakani,P. and Shukla,S.
  TITLE     CTCF and BORIS-mediated autophagy regulation via alternative
            splicing of BNIP3L in breast cancer
  JOURNAL   J Biol Chem 300 (7), 107416 (2024)
   PUBMED   38810696
  REMARK    GeneRIF: CTCF and BORIS-mediated autophagy regulation via
            alternative splicing of BNIP3L in breast cancer.
REFERENCE   5  (residues 1 to 725)
  AUTHORS   He,T., You,M., Zhu,H., Chen,P. and Fang,S.
  TITLE     CCCTC-binding factor suppresses alpha-2-macroglobulin transcription
            to improve vascular endothelial cell functions in lower extremity
            arteriosclerosis obliterans
  JOURNAL   Gen Physiol Biophys 43 (3), 231-242 (2024)
   PUBMED   38774923
  REMARK    GeneRIF: CCCTC-binding factor suppresses alpha-2-macroglobulin
            transcription to improve vascular endothelial cell functions in
            lower extremity arteriosclerosis obliterans.
REFERENCE   6  (residues 1 to 725)
  AUTHORS   Bell,A.C., West,A.G. and Felsenfeld,G.
  TITLE     The protein CTCF is required for the enhancer blocking activity of
            vertebrate insulators
  JOURNAL   Cell 98 (3), 387-396 (1999)
   PUBMED   10458613
REFERENCE   7  (residues 1 to 725)
  AUTHORS   Filippova,G.N., Lindblom,A., Meincke,L.J., Klenova,E.M.,
            Neiman,P.E., Collins,S.J., Doggett,N.A. and Lobanenkov,V.V.
  TITLE     A widely expressed transcription factor with multiple DNA sequence
            specificity, CTCF, is localized at chromosome segment 16q22.1
            within one of the smallest regions of overlap for common deletions
            in breast and prostate cancers
  JOURNAL   Genes Chromosomes Cancer 22 (1), 26-36 (1998)
   PUBMED   9591631
REFERENCE   8  (residues 1 to 725)
  AUTHORS   Vostrov,A.A. and Quitschke,W.W.
  TITLE     The zinc finger protein CTCF binds to the APBbeta domain of the
            amyloid beta-protein precursor promoter. Evidence for a role in
            transcriptional activation
  JOURNAL   J Biol Chem 272 (52), 33353-33359 (1997)
   PUBMED   9407128
REFERENCE   9  (residues 1 to 725)
  AUTHORS   Filippova,G.N., Fagerlie,S., Klenova,E.M., Myers,C., Dehner,Y.,
            Goodwin,G., Neiman,P.E., Collins,S.J. and Lobanenkov,V.V.
  TITLE     An exceptionally conserved transcriptional repressor, CTCF, employs
            different combinations of zinc fingers to bind diverged promoter
            sequences of avian and mammalian c-myc oncogenes
  JOURNAL   Mol Cell Biol 16 (6), 2802-2813 (1996)
   PUBMED   8649389
REFERENCE   10 (residues 1 to 725)
  AUTHORS   Valverde de Morales,H.G., Wang,H.L., Garber,K., Corces,V. and Li,H.
  TITLE     CTCF-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   38662876
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027682.10 and AC009095.7.
            
            On or before Apr 25, 2025 this sequence version replaced
            XP_005255832.1, XP_054235374.1.
            
            Summary: This gene is a member of the BORIS + CTCF gene family and
            encodes a transcriptional regulator protein with 11 highly
            conserved zinc finger (ZF) domains. This nuclear protein is able to
            use different combinations of the ZF domains to bind different DNA
            target sequences and proteins. Depending upon the context of the
            site, the protein can bind a histone acetyltransferase
            (HAT)-containing complex and function as a transcriptional
            activator or bind a histone deacetylase (HDAC)-containing complex
            and function as a transcriptional repressor. If the protein is
            bound to a transcriptional insulator element, it can block
            communication between enhancers and upstream promoters, thereby
            regulating imprinted expression. Mutations in this gene have been
            associated with invasive breast cancers, prostate cancers, and
            Wilms' tumors. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.2064361.1,
                                           SRR14038196.134643.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..725
                     /product="transcriptional repressor CTCF isoform 3"
                     /note="transcriptional repressor CTCF; CTCFL paralog;
                     11-zinc finger protein; 11 zinc finger transcriptional
                     repressor; CCCTC-binding factor (zinc finger protein)"
                     /calculated_mol_wt=82483
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P49711.1)"
     Region          180..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49711.1)"
     Region          266..289
                     /region_name="zf-H2C2_5"
                     /note="C2H2-type zinc-finger domain; pfam13909"
                     /db_xref="CDD:404746"
     Region          268..288
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(273,275,277,279..280,283..284,287,301,303,307..308,
                     311..312,315,329,331,333,335..336,339..340,346)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          280..305
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P49711.1)"
     Region          296..316
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          309..333
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P49711.1)"
     Region          324..347
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          351..375
                     /region_name="zf-H2C2_5"
                     /note="C2H2-type zinc-finger domain; pfam13909"
                     /db_xref="CDD:404746"
     Region          353..373
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <366..500
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P49711.1)"
     Region          381..401
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P49711.1)"
     Region          409..426
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          439..457
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          469..489
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(474,476,478,480..481,484..485,488,502,504,508..509,
                     512..513,516,530,532,534,536..537,540..541,545)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          497..517
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          509..534
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          525..546
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          557..573
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            609
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P49711.1)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P49711.1)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P49711.1)"
     Region          687..715
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49711.1)"
     CDS             1..725
                     /gene="CTCF"
                     /gene_synonym="CFAP108; FAP108; MRD21"
                     /coded_by="NM_001438969.1:326..2503"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:10664"
                     /db_xref="HGNC:HGNC:13723"
                     /db_xref="MIM:604167"
ORIGIN      
        1 megdaveaiv eesetfikgk erktyqrrre ggqeedachl pqnqtdggev vqdvnssvqm
       61 vmmeqldptl lqmktevmeg tvapeaeaav ddtqiitlqv vnmeeqpini gelqlvqvpv
      121 pvtvpvatts veelqgayen evskeglaes epmichtlpl pegfqvvkvg angevetleq
      181 gelppqedps wqkdpdyqpp akktkktkks klryteegkd vdvsvydfee eqqegllsev
      241 naekvvgnmk ppkptkikkk gvkktfqcel csytcprrsn ldrhmkshtd erphkchlcg
      301 rafrtvtllr nhlnthtgtr phkcpdcdma fvtsgelvrh rrykhthekp fkcsmcdyas
      361 vevsklkrhi rshtgerpfq cslcsyasrd tyklkrhmrt hsgekpyecy icharftqsg
      421 tmkmhilqkh tenvakfhcp hcdtviarks dlgvhlrkqh syieqgkkcr ycdavfhery
      481 aliqhqkshk nekrfkcdqc dyacrqerhm imhkrthtge kpyacshcdk tfrqkqlldm
      541 hfkryhdpnf vpaafvcskc gktftrrntm arhadncagp dgvegengge tkkskrgrkr
      601 kmrskkedss dsenaepdld dnedeeepav eiepepepqp vtpapppakk rrgrppgrtn
      661 qpkqnqpiiq vedqntgaie niivevkkep daepaegeee eaqpaatdap ngdltpemil
      721 smmdr
//
LOCUS       NP_001401583             531 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 2 isoform c [Homo sapiens].
ACCESSION   NP_001401583 XP_047284837
VERSION     NP_001401583.1
DBSOURCE    REFSEQ: accession NM_001414654.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Jung,J.H., Lee,D., Ko,H.M. and Jang,H.J.
  TITLE     Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in Colorectal
            Cancer Cells by Activating p53
  JOURNAL   Biomolecules 11 (10), 1492 (2021)
   PUBMED   34680125
  REMARK    GeneRIF: Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in
            Colorectal Cancer Cells by Activating p53.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Royer-Bertrand,B., Cisarova,K., Niel Butschi,F., Foletti,G.,
            Guinchat,V., Tran,C., Superti-Furga,A. and Good,J.M.
  TITLE     CNOT2 haploinsufficiency in a 40-year-old man with intellectual
            disability, autism, and seizures
  JOURNAL   Am J Med Genet A 185 (8), 2602-2606 (2021)
   PUBMED   34018673
  REMARK    GeneRIF: CNOT2 haploinsufficiency in a 40-year-old man with
            intellectual disability, autism, and seizures.
            Review article
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Jayne,S., Zwartjes,C.G., van Schaik,F.M. and Timmers,H.T.
  TITLE     Involvement of the SMRT/NCoR-HDAC3 complex in transcriptional
            repression by the CNOT2 subunit of the human Ccr4-Not complex
  JOURNAL   Biochem J 398 (3), 461-467 (2006)
   PUBMED   16712523
  REMARK    GeneRIF: This study shows that SMRT/NCoR-HDAC3 complex is a
            cofactor of CNOT2-mediated repression and suggests that
            transcriptional regulation by the Ccr4-Not complex involves
            regulation of chromatin modification.
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Winkler,G.S., Mulder,K.W., Bardwell,V.J., Kalkhoven,E. and
            Timmers,H.T.
  TITLE     Human Ccr4-Not complex is a ligand-dependent repressor of nuclear
            receptor-mediated transcription
  JOURNAL   EMBO J 25 (13), 3089-3099 (2006)
   PUBMED   16778766
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Shi,J. and Nelson,M.A.
  TITLE     The cyclin-dependent kinase 11 interacts with NOT2
  JOURNAL   Biochem Biophys Res Commun 334 (4), 1310-1316 (2005)
   PUBMED   16039607
  REMARK    GeneRIF: These findings suggest that CDK11 may contribute to
            apoptosis by regulating the activity of NOT2 independent of its
            kinase activity.
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Zwartjes,C.G., Jayne,S., van den Berg,D.L. and Timmers,H.T.
  TITLE     Repression of promoter activity by CNOT2, a subunit of the
            transcription regulatory Ccr4-not complex
  JOURNAL   J Biol Chem 279 (12), 10848-10854 (2004)
   PUBMED   14707134
  REMARK    GeneRIF: major repression function of CNOT2 is localized in a
            specialized protein motif, the Not-Box
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Denis,C.L. and Chen,J.
  TITLE     The CCR4-NOT complex plays diverse roles in mRNA metabolism
  JOURNAL   Prog Nucleic Acid Res Mol Biol 73, 221-250 (2003)
   PUBMED   12882519
  REMARK    Review article
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092881.8 and AC025569.37.
            
            On Feb 21, 2023 this sequence version replaced XP_047284837.1.
            
            Summary: This gene encodes a subunit of the multi-component
            CCR4-NOT complex. The CCR4-NOT complex regulates mRNA synthesis and
            degradation and is also thought to be involved in mRNA splicing,
            transport and localization. The encoded protein interacts with
            histone deacetylases and functions as a repressor of polymerase II
            transcription. Alternatively spliced transcript variants have been
            observed for this gene. [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.3745826.1,
                                           SRR14038194.4050049.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..531
                     /product="CCR4-NOT transcription complex subunit 2 isoform
                     c"
                     /note="negative regulator of transcription 2;
                     CCR4-associated factor 2; CC chemokine receptor 4-negative
                     regulator of transcription 2"
                     /calculated_mol_wt=58490
     Region          387..510
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..531
                     /gene="CNOT2"
                     /gene_synonym="CDC36; HSPC131; IDNADFS; NOT2; NOT2H"
                     /coded_by="NM_001414654.1:229..1824"
                     /note="isoform c is encoded by transcript variant 8"
                     /db_xref="GeneID:4848"
                     /db_xref="HGNC:HGNC:7878"
                     /db_xref="MIM:604909"
ORIGIN      
        1 mlkevaqvtn smfgasrkkf vegvdsdyhd enmyysqssm fphrsekdml aspstsgqls
       61 qfgaslygqq salglpmrgm snntpqlnrs lsqgtqlpsh vtpttgvptm slhtppspsr
      121 gilpmnprnm mnhsqvgqgi gipsrtnsms ssglgspnrs spsiicmpkq qpsrqpftvn
      181 smsgfgmnrn qafgmnnsls snifngtdgs envtgldlsd fpaladrnrr egsgnptpli
      241 nplagrapyv gmvtkpaneq sqdfsihned fpalpgssyk dptssnddsk snlntsgktt
      301 sstdgpkfpg dkssttqnnn qqkkgiqvlp dgrvtnipqg mvtdqfgmig lltfiraaet
      361 dpgmvhlalg sdlttlglnl nspenlypkf aspwasspcr pqdidfhvps eyltnihird
      421 klaaiklgry gedllfylyy mnggdvlqll aavelfnrdw ryhkeervwi trapgmeptm
      481 ktntyergty yffdclnwrk vakefhleyd kleerphlps tfnynpaqqa f
//
LOCUS       NP_001394253             326 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 25 [Homo sapiens].
ACCESSION   NP_001394253
VERSION     NP_001394253.1
DBSOURCE    REFSEQ: accession NM_001407324.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2351770.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..326
                     /product="tropomyosin alpha-1 chain isoform 25"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=37312
     Region          2..>159
                     /region_name="EmrA"
                     /note="Multidrug resistance efflux pump EmrA [Defense
                     mechanisms]; COG1566"
                     /db_xref="CDD:441174"
     Region          90..324
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..326
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407324.1:84..1064"
                     /note="isoform 25 is encoded by transcript variant 25"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle ediaakekll rvsederdrv
       61 leelhkaeds llaaeeaaak ledelvslqk klkgtedeld kysealkdaq eklelaekka
      121 tdaeadvasl nrriqlveee ldraqerlat alqkleeaek aadesergmk viesraqkde
      181 ekmeiqeiql keakhiaeda drkyeevark lviiesdler aeeraelseg kcaeleeelk
      241 tvtnnlksle aqaekysqke dryeeeikvl sdklkeaetr aefaersvtk leksiddled
      301 elyaqklkyk aiseeldhal ndmtsm
//
LOCUS       NP_001427442             572 aa            linear   PRI 21-NOV-2025
DEFINITION  radixin isoform 8 [Homo sapiens].
ACCESSION   NP_001427442
VERSION     NP_001427442.1
DBSOURCE    REFSEQ: accession NM_001440513.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Kruse,T., Benz,C., Garvanska,D.H., Lindqvist,R., Mihalic,F.,
            Coscia,F., Inturi,R., Sayadi,A., Simonetti,L., Nilsson,E., Ali,M.,
            Kliche,J., Moliner Morro,A., Mund,A., Andersson,E., McInerney,G.,
            Mann,M., Jemth,P., Davey,N.E., Overby,A.K., Nilsson,J. and
            Ivarsson,Y.
  TITLE     Large scale discovery of coronavirus-host factor protein
            interaction motifs reveals SARS-CoV-2 specific mechanisms and
            vulnerabilities
  JOURNAL   Nat Commun 12 (1), 6761 (2021)
   PUBMED   34799561
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Stemmer-Rachamimov,A.O., Gonzalez-Agosti,C., Xu,L., Burwick,J.A.,
            Beauchamp,R., Pinney,D., Louis,D.N. and Ramesh,V.
  TITLE     Expression of NF2-encoded merlin and related ERM family proteins in
            the human central nervous system
  JOURNAL   J Neuropathol Exp Neurol 56 (6), 735-742 (1997)
   PUBMED   9184664
REFERENCE   7  (residues 1 to 572)
  AUTHORS   Hirao,M., Sato,N., Kondo,T., Yonemura,S., Monden,M., Sasaki,T.,
            Takai,Y., Tsukita,S. and Tsukita,S.
  TITLE     Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma
            membrane association: possible involvement of phosphatidylinositol
            turnover and Rho-dependent signaling pathway
  JOURNAL   J Cell Biol 135 (1), 37-51 (1996)
   PUBMED   8858161
REFERENCE   8  (residues 1 to 572)
  AUTHORS   Wilgenbus,K.K., Milatovich,A., Francke,U. and Furthmayr,H.
  TITLE     Molecular cloning, cDNA sequence, and chromosomal assignment of the
            human radixin gene and two dispersed pseudogenes
  JOURNAL   Genomics 16 (1), 199-206 (1993)
   PUBMED   8486357
REFERENCE   9  (residues 1 to 572)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 572)
  AUTHORS   Sato,N., Funayama,N., Nagafuchi,A., Yonemura,S., Tsukita,S. and
            Tsukita,S.
  TITLE     A gene family consisting of ezrin, radixin and moesin. Its specific
            localization at actin filament/plasma membrane association sites
  JOURNAL   J Cell Sci 103 (Pt 1), 131-143 (1992)
   PUBMED   1429901
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002788.3 and AP000901.5.
            
            Summary: Radixin is a cytoskeletal protein that may be important in
            linking actin to the plasma membrane. It is highly similar in
            sequence to both ezrin and moesin. The radixin gene has been
            localized by fluorescence in situ hybridization to 11q23. A
            truncated version representing a pseudogene (RDXP2) was assigned to
            Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was
            mapped to 11p by Southern and PCR analyses. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.4085433.1,
                                           SRR14038195.2097085.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267755 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..572
                     /product="radixin isoform 8"
                     /calculated_mol_wt=67195
     Region          5..195
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          189..285
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(231..232,234..240,249,270,273..274,277)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(231,234..241,249,270,273..274,277)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(267,271)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            270..285
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          336..445
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          496..572
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..572
                     /gene="RDX"
                     /gene_synonym="DFNB24"
                     /coded_by="NM_001440513.1:170..1888"
                     /note="isoform 8 is encoded by transcript variant 15"
                     /db_xref="GeneID:5962"
                     /db_xref="HGNC:HGNC:9944"
                     /db_xref="MIM:179410"
ORIGIN      
        1 mdaelefaiq pnttgkqlfd qvvktvglre vwffglqyvd skgystwlkl nkkvtqqdvk
       61 kenplqfkfr akffpedvse eliqeitqrl fflqvkeail ndeiycppet avllasyavq
      121 akygdynkei hkpgylandr llpqrvleqh kltkeqweer iqnwheehrg mlredsmmey
      181 lkiaqdlemy gvnyfeiknk kgtelwlgvd alglniyehd dkltpkigfp wseirnisfn
      241 dkkfvikpid kkapdfvfya prlrinkril alcmgnhely mrrrkpdtie vqqmkaqare
      301 ekhqkqlera qlenekkkre iaekekerie rekeelmerl kqieeqtika qkeleeqtrk
      361 aleldqerkr akeeaerlek erraaeeaks aiakqaadqm knqeqlaael aeftakiall
      421 eeakkkkeee atewqhkafa aqedlektke elktvmsapp ppppppvipp tenehdehde
      481 nnaeasaels negvmnhrse eervtetqkn ervkkqlqal sselaqarde tkktqndvlh
      541 aenvkagrdk yktlrqirqg ntkqridefe am
//
LOCUS       NP_001427983            4359 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HUWE1 isoform 3 [Homo sapiens].
ACCESSION   NP_001427983 XP_047297696 XP_054182292
VERSION     NP_001427983.1
DBSOURCE    REFSEQ: accession NM_001441054.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4359)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 4359)
  AUTHORS   Lee,C., Park,S.H. and Yoon,S.K.
  TITLE     The E3 ligase HUWE1 increases the sensitivity of CRC to oxaliplatin
            through TOMM20 degradation
  JOURNAL   Oncogene 43 (9), 636-649 (2024)
   PUBMED   38184713
  REMARK    GeneRIF: The E3 ligase HUWE1 increases the sensitivity of CRC to
            oxaliplatin through TOMM20 degradation.
REFERENCE   3  (residues 1 to 4359)
  AUTHORS   Li,X.X., Xu,J.K., Su,W.J., Wu,H.L., Zhao,K., Zhang,C.M., Chen,X.K.
            and Yang,L.X.
  TITLE     The role of KDM4A-mediated histone methylation on temozolomide
            resistance in glioma cells through the HUWE1/ROCK2 axis
  JOURNAL   Kaohsiung J Med Sci 40 (2), 161-174 (2024)
   PUBMED   37873881
  REMARK    GeneRIF: The role of KDM4A-mediated histone methylation on
            temozolomide resistance in glioma cells through the HUWE1/ROCK2
            axis.
REFERENCE   4  (residues 1 to 4359)
  AUTHORS   Bernassola,F., Karin,M., Ciechanover,A. and Melino,G.
  TITLE     The HECT family of E3 ubiquitin ligases: multiple players in cancer
            development
  JOURNAL   Cancer Cell 14 (1), 10-21 (2008)
   PUBMED   18598940
  REMARK    Review article
REFERENCE   5  (residues 1 to 4359)
  AUTHORS   Zhong,Q., Gao,W., Du,F. and Wang,X.
  TITLE     Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the
            polyubiquitination of Mcl-1 and regulates apoptosis
  JOURNAL   Cell 121 (7), 1085-1095 (2005)
   PUBMED   15989957
  REMARK    GeneRIF: Mule is both required and sufficient for the
            polyubiquitination of Mcl-1; Mule is a unique BH3-containing E3
            ubiquitin ligase apical to Bcl-2 family proteins during DNA
            damage-induced apoptosis
            GeneRIF: Mule (HUWE1) poly-ubiquitinates anti-apoptotic gene Mcl-1.
REFERENCE   6  (residues 1 to 4359)
  AUTHORS   Chen,D., Kon,N., Li,M., Zhang,W., Qin,J. and Gu,W.
  TITLE     ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
  JOURNAL   Cell 121 (7), 1071-1083 (2005)
   PUBMED   15989956
  REMARK    GeneRIF: study modifies the current view of ARF-mediated p53
            activation and reveals that ARF-BP1 is a critical mediator of both
            the p53-independent and p53-dependent tumor suppressor functions of
            ARF
            GeneRIF: Ubiquitin ligase activity of ARF-BP1 (HUWE1) is inhibited
            by Arf.
REFERENCE   7  (residues 1 to 4359)
  AUTHORS   Liu,Z., Oughtred,R. and Wing,S.S.
  TITLE     Characterization of E3Histone, a novel testis ubiquitin protein
            ligase which ubiquitinates histones
  JOURNAL   Mol Cell Biol 25 (7), 2819-2831 (2005)
   PUBMED   15767685
REFERENCE   8  (residues 1 to 4359)
  AUTHORS   Gu,J., Dubner,R., Fornace,A.J. Jr. and Iadarola,M.J.
  TITLE     UREB1, a tyrosine phosphorylated nuclear protein, inhibits p53
            transactivation
  JOURNAL   Oncogene 11 (10), 2175-2178 (1995)
   PUBMED   7478539
REFERENCE   9  (residues 1 to 4359)
  AUTHORS   Turner,G., Gedeon,A. and Mulley,J.
  TITLE     X-linked mental retardation with heterozygous expression and
            macrocephaly: pericentromeric gene localization
  JOURNAL   Am J Med Genet 51 (4), 575-580 (1994)
   PUBMED   7943042
REFERENCE   10 (residues 1 to 4359)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX323845.7 and AC231658.3.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297696.1, XP_054182292.1.
            
            Summary: This gene encodes a protein containing a C-terminal HECT
            (E6AP type E3 ubiquitin protein ligase) domain that functions as an
            E3 ubiquitin ligase. The encoded protein is required for the
            ubiquitination and subsequent degradation of the anti-apoptotic
            protein Mcl1 (myeloid cell leukemia sequence 1 (BCL2-related)).
            This protein also ubiquitinates the p53 tumor suppressor, core
            histones, and DNA polymerase beta. Mutations in this gene are
            associated with Turner type X-linked syndromic cognitive
            disability. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3494325.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..4359
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..4359
                     /product="E3 ubiquitin-protein ligase HUWE1 isoform 3"
                     /EC_number="2.3.2.26"
                     /note="Mcl-1 ubiquitin ligase E3; BJ-HCC-24 tumor antigen;
                     HECT domain protein LASU1; ARF-binding protein 1;
                     URE-binding protein 1; large structure of UREB1; upstream
                     regulatory element-binding protein 1; homologous to E6AP
                     carboxyl terminus homologous protein 9; HECT-type E3
                     ubiquitin transferase HUWE1; HECT, UBA and WWE domain
                     containing 1, E3 ubiquitin protein ligase"
                     /calculated_mol_wt=480025
     Region          92..367
                     /region_name="DUF908"
                     /note="Domain of Unknown Function (DUF908); pfam06012"
                     /db_xref="CDD:428721"
     Region          431..814
                     /region_name="DUF913"
                     /note="Domain of Unknown Function (DUF913); pfam06025"
                     /db_xref="CDD:461803"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          706..759
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          978..1001
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1014..1037
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1084
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1291..1320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1317..1356
                     /region_name="UBA_HUWE1"
                     /note="UBA domain found in eukaryotic E3 ubiquitin-protein
                     ligase HUWE1 and similar proteins; cd14288"
                     /db_xref="CDD:270474"
     Site            1368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1396..1415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1617..1678
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          1689..1735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1722
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1907
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2018..2065
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2035
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2262..2342
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2267
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2356..2480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2554
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2595
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2694..2970
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          <2735..3066
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            2751
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2826
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2833
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2835
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2861
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2887
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2888
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2889
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2918
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3010..3043
                     /region_name="UBM"
                     /note="Ubiquitin binding region; pfam14377"
                     /db_xref="CDD:464159"
     Region          3036..3059
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3149
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3245..3267
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3404..3424
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3471..3512
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3537..3568
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3555
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3737..3758
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3752
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3757
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3760
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3793
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3801
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3812
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3815
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3879..3916
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3891
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3904
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3909
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3912
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          4004..4357
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(4008,4038,4049,4110,4284,4320..4321,4324..4328,4348,
                     4356)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(4138,4141..4142,4144..4145,4148,4155,4157,
                     4161..4162,4164,4169,4174,4191,4195)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     Site            4256
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P51593; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     CDS             1..4359
                     /gene="HUWE1"
                     /gene_synonym="ARF-BP1; HECTH9; HSPC272; Ib772; LASU1;
                     MRXST; MULE; URE-B1; UREB1"
                     /coded_by="NM_001441054.1:426..13505"
                     /note="isoform 3 is encoded by transcript variant 8"
                     /db_xref="GeneID:10075"
                     /db_xref="HGNC:HGNC:30892"
                     /db_xref="MIM:300697"
ORIGIN      
        1 mkvdrtklkk tpteapadcr alidklkvcn deqlllelqq iktwnigkce lyhwvdlldr
       61 fdgiladagq tvenmswmlv cdrpereqlk mlllavlnft allieysfsr hlyssiehlt
      121 tllassdmqv vlavlnllyv fskrsnyitr lgsdkrtpll trlqhlaesw ggkengfgla
      181 eccrdlhmmk yppsattlhf efyadpgaev kiekrttsnt lhyihieqld kisespseim
      241 esltkmysip kdkqmllfth irlahgfsnh rkrlqavqar lhaisilvys nalqesansi
      301 lynglieelv dvlqitdkql meikaaslrt ltsivhlert pklssiidct gtasyhgflp
      361 vlvrnciqam idpsmdpyph qfatalfsfl yhlasydagg ealvscgmme allkvikflg
      421 deqdqitfvt ravrvvdlit nldmaafqsh sglsifiyrl ehevdlcrke cpfvikpkiq
      481 rpnttqegee metdmdgvqc ipqraallks mlnflkkaiq dpafsdgirh vmdgslptsl
      541 khiisnaeyy gpslfllate vvtvfvfqep sllsslqdng ltdvmlhall ikdvpatrev
      601 lgslpnvfsa lclnarglqs fvqcqpferl fkvllspdyl pamrrrrssd plgdtasnlg
      661 savdelmrhq ptlktdatta iiklleeicn lgrdpkyicq kpsiqkadgt atappprsnh
      721 aaeeassede eeeevqamqs fnstqqnete pnqqvvgtee ripiplmdyi lnvmkfvesi
      781 lsnnttddhc qefvnqkgll plvtilglpn lpidfptsaa cqavagvcks iltlshepkv
      841 lqegllqlds ilssleplhr piespggsvl lrelacagnv adatlsaqat pllhaltaah
      901 ayimmfvhtc rvgqseirsi svnqwgsqlg lsvlsklsql ycslvwestv llslctpnsl
      961 psgcefgqad mqklvpkdek agttqggkrs dgeqdgaags mdastqglle gigldgdtla
     1021 pmetdeptas dskgkskitp amaarikqik pllsassrlg ralaelfgll vklcvgspvr
     1081 qrrshhaast ttaptpaars tasaltkllt kglswqpppy tptprfrltf ficsvgftsp
     1141 mlfderkypy hlmlqkflcs gghnalfetf nwalsmggkv pvseglehsd lpdgtgefld
     1201 awlmlvekmv npttvlesph slpaklpggv qnfpqfsalr flvvtqkaaf tciknlwnrk
     1261 plkvyggrma esmlailchi lrgepvirer lskekegsrg eedtgqeegg srrepqvnqq
     1321 qlqqlmdmgf trehameall ntstmeqate yllthpppim ggvvrdlsms eedqmmraia
     1381 mslgqdipmd qraespeeva crkeeeerka rekqeeeeak clekfqdadp leqdelhtft
     1441 dtmlpgcfhl ldelpdtvyr vcdlimtaik rngadyrdmi lkqvvnqvwe aadvlikaal
     1501 plttsdtktv sewisqmatl pqasnlatri llltllfeel klpcawvves sgilnvlikl
     1561 levvqpclqa akeqkevqtp kwitpvllli dfyektaiss krraqmtkyl qsnsnnwrwf
     1621 ddrsgrwcsy sasnnstids awksgetsvr ftagrrrytv qfttmvqvne etgnrrpvml
     1681 tllrvprlnk nsknsngqel ektleeskem dikrkenkgn dtplalestn teketsleet
     1741 kigeiliqgl tedmvtvlir acvsmlgvpv dpdtlhatlr lclrltrdhk yammfaelks
     1801 trmilnltqs sgfngftplv tlllrhiied pctlrhtmek vvrsaatsga gsttsgvvsg
     1861 slgsreinyi lrvlgpaacr npdiftevan ccirialpap rgsgtasdde fenlrikgpn
     1921 avqlvkttpl kpsplpvipd tikeviydml nalaayhape eadksdpkpg vmtqevgqll
     1981 qdmgddvyqq yrsltrqssd fdtqsgfsin sqvfaadgas tetsasgtsq geastpeesr
     2041 dgkkdkegdr aseegkqkgk gskplmptst ilrllaelvr syvgiatlia nysytvgqse
     2101 likedcsvla fvldhllpht qnaedkdtpa larlflasla aagsgtdaqv alvnevkaal
     2161 gralamaest ekharlqavm ciistimesc pstssfyssa taktqhngmn niirlflkkg
     2221 lvndlarvph sldlsspnma ntvnaalkpl etlsrivnqp sslfgsksas sknkseqdaq
     2281 gasqdsssnq qdpgepgeae vqeedhdvtq tevadgdimd geaetdsvvi agqpevlssq
     2341 emqveneled lidellerdg gsgnstiivs rsgedesqed vlmdeapsnl sqastlqanr
     2401 edsmnildpe deeehtqeed ssgsnededd sqdeeeeeee deeddqedde geegdedddd
     2461 dgsemelded ypdmnasplv rferfdredd liiefdnmfs satdippspg niptthplmv
     2521 rhadhssltl gsgssttrlt qgigrsqrtl rqltantght ihvhypgnrq pnpplilqrl
     2581 lgpsaaadil qlssslplqs rgrarllvgn ddvhiiarsd dellddffhd qstatsqagt
     2641 lssiptaltr wteeckvlda esmhdcvsvv kvsivnhlef lrdeeleerr ekrrkqlaee
     2701 etkitdkgke dkenrdqsaq ctasksndst eqnlsdgtpm pdsypttpss tdaatseske
     2761 tlgtlqssqq qptlptppal gevpqelqsp ageggsstql lmpvepeelg ptrpsgeaet
     2821 tqmelspapt itslsperae dsdaltavss qlegspmdts slasctleea vgdtsaagss
     2881 eqpragsstp gdappavaev qgrsdgsges aqppedsspp assessstrd savaisgads
     2941 rgileeplps tsseeedpla gislpegvdp sflaalpddi rrevlqnqlg irpptrtaps
     3001 tnssapavvg npgvtevspe flaalppaiq eevlaqqrae qqrrelaqna ssdtpmdpvt
     3061 fiqtlpsdlr rsvledmeds vlavmppdia aeaqalrreq earqrqlmhe rlfghsstsa
     3121 lsailrspaf tsrlsgnrgv qytrlavqrg gtfqmggsss hnrpsgsnvd tllrlrgrll
     3181 ldhealscll vllfvdepkl ntsrlhrvlr nlcyhaqtrh wvirsllsil qrsseselci
     3241 etpklttsee kgkksskscg ssshenrpld llhkmeskss nqlswlsvsm daalgcrtni
     3301 fqiqrsggrk htekhasggs tvhihpqaap vvcrhvldtl iqlakvfpsh ftqqrtketn
     3361 cesdrergnk acspcssqss ssgictdfwd llvkldnmnv srkgknsvks vpvsaggege
     3421 tspysleasp lgqlmnmlsh pvirrssllt ekllrllsli sialpenkvs eaqansgsga
     3481 sstttatstt stttttaast tptpptaptp vtsapalvaa taistivvaa sttvttptta
     3541 tttvsisptt kgskspakvs dggssstdfk mvssgltenq lqlsvevlts hscseegled
     3601 aanvllqlsr gdsgtrdtvl klllngarhl gytlckqigt llaelreynl eqqrraqcet
     3661 lspdglpeeq pqttklkgkm qsrfdmaenv vivasqkrpl ggrelqlpsm smltsktstq
     3721 kfflrvlqvi iqlrddtrra nkkakqtgrl gssglgsass iqaavrqlea eadaiiqmse
     3781 ssqseasvrr eespmdvdqp spsaqdtqsi asdgtpqgek ekeerppelp llseqlslde
     3841 lwdmlgeclk eleeshdqha vlvlqpavea fflvhatere skppvrdtre sqlahikdep
     3901 pplspapltp atpssldpff srepssmhis sslppdtqkf lrfaethrtv lnqilrqstt
     3961 hladgpfavl vdyirvldfd vkrkyfrqel erldeglrke dmavhvrrdh vfedsyrelh
     4021 rkspeemknr lyivfegeeg qdaggllrew ymiisremfn pmyalfrtsp gdrvtytinp
     4081 sshcnpnhls yfkfvgriva kavydnrlle cyftrsfykh ilgksvrytd mesedyhfyq
     4141 glvyllendv stlgydltfs tevqefgvce vrdlkpngan ilvteenkke yvhlvcqmrm
     4201 tgairkqlaa flegfyeiip krlisifteq elellisglp tididdlksn teyhkyqsns
     4261 iqiqwfwral rsfdqadrak flqfvtgtsk vplqgfaale gmngiqkfqi hrddrstdrl
     4321 psahtcfnql dlpayesfek lrhmlllaiq ecsegfgla
//
LOCUS       NP_001394389            2742 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform j [Homo sapiens].
ACCESSION   NP_001394389
VERSION     NP_001394389.1
DBSOURCE    REFSEQ: accession NM_001407460.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2742)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2742)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2742)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2742)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2742)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2742)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2742)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2742)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2742)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2742)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2829910.1,
                                           SRR18074969.2900725.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2742
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2742
                     /product="adenomatous polyposis coli protein isoform j"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=300309
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Region          <8..272
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          <307..365
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          364..407
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(398,402,406,441,445,449,485,489,493)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          411..452
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          415..452
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          459..494
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          502..543
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          548..588
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          552..586
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          590..630
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          594..630
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          631..918
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          935..1034
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1156..>1173
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1182..1267
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1190..1600
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1270..1292
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1536..1559
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1561..1614
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1615..1636
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1645..1738
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1772..1846
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1932..1951
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2122..2467
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2569..2742
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2742
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407460.1:404..8632"
                     /note="isoform j is encoded by transcript variant 30"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrriar iqqiekdilr irqllqsqat
      241 eaerssqnkh etgshdaerq negqgvgein matsgngqgs ttrmdhetas vlssssthsa
      301 prrltshlgt kiraycetcw ewqeahepgm dqdknpmpap vehqicpavc vlmklsfdee
      361 hrhamnelgg lqaiaellqv dcemygltnd hysitlrrya gmaltnltfg dvankatlcs
      421 mkgcmralva qlksesedlq qviasvlrnl swradvnskk tlrevgsvka lmecalevkk
      481 estlksvlsa lwnlsahcte nkadicavdg alaflvgtlt yrsqtntlai iesgggilrn
      541 vssliatned hrqilrennc lqtllqhlks hsltivsnac gtlwnlsarn pkdqealwdm
      601 gavsmlknli hskhkmiamg saaalrnlma nrpakykdan imspgsslps lhvrkqkale
      661 aeldaqhlse tfdnidnlsp kashrskqrh kqslygdyvf dtnrhddnrs dnfntgnmtv
      721 lspylnttvl psssssrgsl dssrsekdrs lerergiglg nyhpatenpg tsskrglqis
      781 ttaaqiakvm eevsaihtsq edrssgstte lhcvtderna lrrssaahth sntynftkse
      841 nsnrtcsmpy akleykrssn dslnsvsssd gygkrgqmkp siesysedde skfcsygqyp
      901 adlahkihsa nhmddndgel dtpinyslky sdeqlnsgrq spsqnerwar pkhiiedeik
      961 qseqrqsrnq sttypvytes tddkhlkfqp hfgqqecvsp yrsrgangse tnrvgsnhgi
     1021 nqnvsqslcq eddyeddkpt nyseryseee qheeeerptn ysikyneekr hvdqpidysl
     1081 kyatdipssq kqsfsfskss sgqssktehm ssssentstp ssnakrqnql hpssaqsrsg
     1141 qpqkaatckv ssinqetiqt ycvedtpicf srcsslssls saedeigcnq ttqeadsant
     1201 lqiaeikeki gtrsaedpvs evpavsqhpr tkssrlqgss lssesarhka vefssgaksp
     1261 sksgaqtpks ppehyvqetp lmfsrctsvs sldsfesrsi assvqsepcs gmvsgiisps
     1321 dlpdspgqtm ppsrsktppp ppqtaqtkre vpknkaptae kresgpkqaa vnaavqrvqv
     1381 lpdadtllhf atestpdgfs cssslsalsl depfiqkdve lrimppvqen dngneteseq
     1441 pkesnenqek eaektidsek dllddsdddd ieileeciis amptkssrka kkpaqtaskl
     1501 pppvarkpsq lpvykllpsq nrlqpqkhvs ftpgddmprv ycvegtpinf statslsdlt
     1561 iesppnelaa gegvrggaqs gefekrdtip tegrstdeaq ggktssvtip elddnkaeeg
     1621 dilaecinsa mpkgkshkpf rvkkimdqvq qasasssapn knqldgkkkk ptspvkpipq
     1681 nteyrtrvrk nadsknnlna ervfsdnkds kkqnlknnsk vfndklpnne drvrgsfafd
     1741 sphhytpieg tpycfsrnds lssldfdddd vdlsrekael rkakenkese akvtshtelt
     1801 snqqsanktq aiakqpinrg qpkpilqkqs tfpqsskdip drgaatdekl qnfaientpv
     1861 cfshnsslss lsdidqennn kenepikete ppdsqgepsk pqasgyapks fhvedtpvcf
     1921 srnsslssls idseddllqe cissampkkk kpsrlkgdne khsprnmggi lgedltldlk
     1981 diqrpdsehg lspdsenfdw kaiqegansi vsslhqaaaa aclsrqassd sdsilslksg
     2041 islgspfhlt pdqeekpfts nkgprilkpg ekstletkki eseskgikgg kkvykslitg
     2101 kvrsnseisg qmkqplqanm psisrgrtmi hipgvrnsss stspvskkgp plktpasksp
     2161 segqtattsp rgakpsvkse lspvarqtsq iggsskapsr sgsrdstpsr paqqplsrpi
     2221 qspgrnsisp grngisppnk lsqlprtssp stastkssgs gkmsytspgr qmsqqnltkq
     2281 tglsknassi prsesaskgl nqmnngngan kkvelsrmss tkssgsesdr serpvlvrqs
     2341 tfikeapspt lrrkleesas feslspssrp asptrsqaqt pvlspslpdm slsthssvqa
     2401 ggwrklppnl sptieyndgr pakrhdiars hsespsrlpi nrsgtwkreh skhssslprv
     2461 stwrrtgsss silsassess ekaksedekh vnsisgtkqs kenqvsakgt wrkikenefs
     2521 ptnstsqtvs sgatngaesk tliyqmapav sktedvwvri edcpinnprs grsptgntpp
     2581 vidsvsekan pnikdskdnq akqnvgngsv pmrtvglenr lnsfiqvdap dqkgteikpg
     2641 qnnpvpvset nessivertp fsssssskhs spsgtvaarv tpfnynpspr kssadstsar
     2701 psqiptpvnn ntkkrdsktd stessgtqsp krhsgsylvt sv
//
LOCUS       NP_075259                822 aa            linear   PRI 21-NOV-2025
DEFINITION  fibroblast growth factor receptor 2 isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_075259 NP_075258
VERSION     NP_075259.4
DBSOURCE    REFSEQ: accession NM_022970.4
KEYWORDS    RefSeq; MANE Plus Clinical.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Chen,C.P., Huang,J.P., Huang,K.S., Chen,Y.Y., Wu,F.T., Pan,Y.T.,
            Chiu,C.L. and Wang,W.
  TITLE     Perinatal imaging findings of a fetus with Pfeiffer syndrome and a
            heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation in FGFR2
            presenting a cloverleaf skull, craniosynostosis and short limbs on
            prenatal ultrasound mimicking thanatophoric dysplasia type II
  JOURNAL   Taiwan J Obstet Gynecol 63 (3), 387-390 (2024)
   PUBMED   38802203
  REMARK    GeneRIF: Perinatal imaging findings of a fetus with Pfeiffer
            syndrome and a heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation
            in FGFR2 presenting a cloverleaf skull, craniosynostosis and short
            limbs on prenatal ultrasound mimicking thanatophoric dysplasia type
            II.
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Lian,Y., Bodian,D. and Shehu,A.
  TITLE     Elucidating the Role of Wildtype and Variant FGFR2 Structural
            Dynamics in (Dys)Function and Disorder
  JOURNAL   Int J Mol Sci 25 (8), 4523 (2024)
   PUBMED   38674107
  REMARK    GeneRIF: Elucidating the Role of Wildtype and Variant FGFR2
            Structural Dynamics in (Dys)Function and Disorder.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Xu,N., Hung,K.L., Gong,X., Fan,D., Tian,Y., Yan,M., Wei,Y. and
            Wang,S.
  TITLE     Genetic insights into the 'sandwich fusion' subtype of Klippel-Feil
            syndrome: novel FGFR2 mutations identified by 21 cases of
            whole-exome sequencing
  JOURNAL   Orphanet J Rare Dis 19 (1), 141 (2024)
   PUBMED   38561822
  REMARK    GeneRIF: Genetic insights into the 'sandwich fusion' subtype of
            Klippel-Feil syndrome: novel FGFR2 mutations identified by 21 cases
            of whole-exome sequencing.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Wenger,T.L., Hing,A.V. and Evans,K.N.
  TITLE     Apert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31145570
REFERENCE   5  (residues 1 to 822)
  AUTHORS   Wenger,T., Miller,D. and Evans,K.
  TITLE     FGFR Craniosynostosis Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301628
REFERENCE   6  (residues 1 to 822)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   7  (residues 1 to 822)
  AUTHORS   Dell,K.R. and Williams,L.T.
  TITLE     A novel form of fibroblast growth factor receptor 2. Alternative
            splicing of the third immunoglobulin-like domain confers ligand
            binding specificity
  JOURNAL   J Biol Chem 267 (29), 21225-21229 (1992)
   PUBMED   1400433
REFERENCE   8  (residues 1 to 822)
  AUTHORS   Luqmani,Y.A., Graham,M. and Coombes,R.C.
  TITLE     Expression of basic fibroblast growth factor, FGFR1 and FGFR2 in
            normal and malignant human breast, and comparison with other normal
            tissues
  JOURNAL   Br J Cancer 66 (2), 273-280 (1992)
   PUBMED   1380281
REFERENCE   9  (residues 1 to 822)
  AUTHORS   Katoh,M., Hattori,Y., Sasaki,H., Tanaka,M., Sugano,K., Yazaki,Y.,
            Sugimura,T. and Terada,M.
  TITLE     K-sam gene encodes secreted as well as transmembrane receptor
            tyrosine kinase
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 2960-2964 (1992)
   PUBMED   1313574
REFERENCE   10 (residues 1 to 822)
  AUTHORS   Miki,T., Bottaro,D.P., Fleming,T.P., Smith,C.L., Burgess,W.H.,
            Chan,A.M. and Aaronson,S.A.
  TITLE     Determination of ligand-binding specificity by alternative
            splicing: two distinct growth factor receptors encoded by a single
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 246-250 (1992)
   PUBMED   1309608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009988.12.
            
            On Jan 24, 2009 this sequence version replaced NP_075259.3.
            
            Summary: The protein encoded by this gene is a member of the
            fibroblast growth factor receptor family, where amino acid sequence
            is highly conserved between members and throughout evolution. FGFR
            family members differ from one another in their ligand affinities
            and tissue distribution. A full-length representative protein
            consists of an extracellular region, composed of three
            immunoglobulin-like domains, a single hydrophobic membrane-spanning
            segment and a cytoplasmic tyrosine kinase domain. The extracellular
            portion of the protein interacts with fibroblast growth factors,
            setting in motion a cascade of downstream signals, ultimately
            influencing mitogenesis and differentiation. This particular family
            member is a high-affinity receptor for acidic, basic and/or
            keratinocyte growth factor, depending on the isoform. Mutations in
            this gene are associated with Crouzon syndrome, Pfeiffer syndrome,
            Craniosynostosis, Apert syndrome, Jackson-Weiss syndrome,
            Beare-Stevenson cutis gyrata syndrome, Saethre-Chotzen syndrome,
            and syndromic craniosynostosis. Multiple alternatively spliced
            transcript variants encoding different isoforms have been noted for
            this gene. [provided by RefSeq, Jan 2009].
            
            Transcript Variant: This variant (2) uses an alternate internal
            in-frame coding exon compared to transcript variant 1, resulting in
            an isoform (2, also known as isoform K-sam-IIH1, IIIb, and BFR-1)
            with a different, 1 aa longer protein segment in the mid-region
            compared to isoform 1.
            
            Sequence Note: A downstream AUG translation start codon is selected
            for this RefSeq based on the presence of a strong Kozak consensus
            signal, a strong community standard for the use of the downstream
            start codon, and on a higher probability of an N-terminal signal
            peptide being present in the resulting protein. The use of an
            alternative in-frame upstream AUG start codon would result in a
            protein that is 19 aa longer at the N-terminus. Translation from
            the annotated downstream start codon is likely to occur via leaky
            scanning and/or reinitiation.
            
            CCDS Note: A downstream AUG translation start codon is selected for
            this CCDS representation based on a strong community standard for
            its use, and on a higher probability of a signal peptide being
            present in the protein N-terminus. The use of an alternative
            upstream AUG start codon would result in a protein that is 19 aa
            longer at the N-terminus. The upstream AUG has a weak Kozak signal
            while the downstream AUG has a strong Kozak signal. Due to leaky
            scanning by ribosomes, it is possible that some ribosomes may
            initiate translation from the downstream AUG codon while others
            start from the upstream AUG. The presence of multiple upstream ORFs
            suggests that a combination of leaky scanning and translational
            reinitiation may be necessary to achieve translation of the
            annotated ORF.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M97193.1, M80634.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: community standard (PMID:
                                                15863034)
            MANE Ensembl match               :: ENST00000457416.7/
                                                ENSP00000410294.2
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..822
                     /product="fibroblast growth factor receptor 2 isoform 2
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="protein tyrosine kinase, receptor like 14;
                     bacteria-expressed kinase; keratinocyte growth factor
                     receptor; BEK fibroblast growth factor receptor"
                     /calculated_mol_wt=89839
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2298
     mat_peptide     22..822
                     /product="fibroblast growth factor receptor 2 isoform 2"
                     /calculated_mol_wt=89839
     Region          31..124
                     /region_name="IgI_1_FGFR"
                     /note="First immunoglobulin (Ig)-like domain of fibroblast
                     growth factor receptor (FGFR); member of the I-set of Ig
                     superfamily (IgSF) domains; cd04973"
                     /db_xref="CDD:409362"
     Region          31..34
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409362"
     Region          47..53
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409362"
     Region          56..66
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409362"
     Region          69..74
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409362"
     Region          77..79
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409362"
     Region          84..88
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409362"
     Region          91..96
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409362"
     Region          102..111
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409362"
     Region          114..124
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409362"
     Region          154..248
                     /region_name="IgI_2_FGFR"
                     /note="Second immunoglobulin (Ig)-like domain of
                     fibroblast growth factor (FGF) receptor; member of the
                     I-set of IgSF domains; cd05857"
                     /db_xref="CDD:409443"
     Region          154..157
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409443"
     Region          165..170
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409443"
     Site            order(166,168,170)
                     /site_type="other"
                     /note="FGF binding site [polypeptide binding]"
                     /db_xref="CDD:409443"
     Site            order(167,174..176,178)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409443"
     Region          174..182
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409443"
     Region          188..193
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409443"
     Region          196..198
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409443"
     Region          207..210
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409443"
     Region          214..219
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409443"
     Region          228..235
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409443"
     Region          238..248
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409443"
     Region          256..358
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          274..278
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          287..291
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          323..327
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          337..342
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          350..353
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          457..769
                     /region_name="PTKc_FGFR2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Fibroblast Growth Factor Receptor 2; cd05101"
                     /db_xref="CDD:270679"
     Site            order(488..489,491,496,516,518,535,565..568,572,627,
                     631..632,634,645,663..667,676,710)
                     /site_type="active"
                     /db_xref="CDD:270679"
     Site            order(488..489,491,496,516,518,535,565..568,572,631..632,
                     634,645)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270679"
     Site            order(627,631,663..667,676,710)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270679"
     Site            644..669
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270679"
     CDS             1..822
                     /gene="FGFR2"
                     /gene_synonym="BBDS; BEK; BFR-1; CD332; CEK3; CFD1; ECT1;
                     JWS; K-SAM; KGFR; TK14; TK25"
                     /coded_by="NM_022970.4:634..3102"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS7620.2"
                     /db_xref="GeneID:2263"
                     /db_xref="HGNC:HGNC:3689"
                     /db_xref="MIM:176943"
ORIGIN      
        1 mvswgrficl vvvtmatlsl arpsfslved ttlepeeppt kyqisqpevy vaapgeslev
       61 rcllkdaavi swtkdgvhlg pnnrtvlige ylqikgatpr dsglyactas rtvdsetwyf
      121 mvnvtdaiss gddeddtdga edfvsensnn krapywtnte kmekrlhavp aantvkfrcp
      181 aggnpmptmr wlkngkefkq ehriggykvr nqhwslimes vvpsdkgnyt cvveneygsi
      241 nhtyhldvve rsphrpilqa glpanastvv ggdvefvckv ysdaqphiqw ikhvekngsk
      301 ygpdglpylk vlkhsginss naevlalfnv teadageyic kvsnyigqan qsawltvlpk
      361 qqapgrekei taspdyleia iycigvflia cmvvtvilcr mknttkkpdf ssqpavhklt
      421 kriplrrqvt vsaessssmn sntplvritt rlsstadtpm lagvseyelp edpkwefprd
      481 kltlgkplge gcfgqvvmae avgidkdkpk eavtvavkml kddatekdls dlvsememmk
      541 migkhkniin llgactqdgp lyviveyask gnlreylrar rppgmeysyd inrvpeeqmt
      601 fkdlvsctyq largmeylas qkcihrdlaa rnvlvtennv mkiadfglar dinnidyykk
      661 ttngrlpvkw mapealfdrv ythqsdvwsf gvlmweiftl ggspypgipv eelfkllkeg
      721 hrmdkpanct nelymmmrdc whavpsqrpt fkqlvedldr iltlttneey ldlsqpleqy
      781 spsypdtrss cssgddsvfs pdpmpyepcl pqyphingsv kt
//
LOCUS       NP_001397911             575 aa            linear   PRI 21-NOV-2025
DEFINITION  tectonic-3 isoform c precursor [Homo sapiens].
ACCESSION   NP_001397911 XP_024303703
VERSION     NP_001397911.1
DBSOURCE    REFSEQ: accession NM_001410982.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 575)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 575)
  AUTHORS   Hussain,S., Nawaz,S., Khan,H., Acharya,A., Schrauwen,I., Ahmad,W.
            and Leal,S.M.
  TITLE     A splice site variant in TCTN3 underlies an atypical form of
            orofaciodigital syndrome IV
  JOURNAL   Ann Hum Genet 86 (6), 291-296 (2022)
   PUBMED   36039988
  REMARK    GeneRIF: A splice site variant in TCTN3 underlies an atypical form
            of orofaciodigital syndrome IV.
REFERENCE   3  (residues 1 to 575)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 575)
  AUTHORS   Chen,H.X., Yang,Z.Y., Hou,H.T., Wang,J., Wang,X.L., Yang,Q., Liu,L.
            and He,G.W.
  TITLE     Novel mutations of TCTN3/LTBP2 with cellular function changes in
            congenital heart disease associated with polydactyly
  JOURNAL   J Cell Mol Med 24 (23), 13751-13762 (2020)
   PUBMED   33098376
  REMARK    GeneRIF: Novel mutations of TCTN3/LTBP2 with cellular function
            changes in congenital heart disease associated with polydactyly.
REFERENCE   5  (residues 1 to 575)
  AUTHORS   Thomas,S., Legendre,M., Saunier,S., Bessieres,B., Alby,C.,
            Bonniere,M., Toutain,A., Loeuillet,L., Szymanska,K., Jossic,F.,
            Gaillard,D., Yacoubi,M.T., Mougou-Zerelli,S., David,A.,
            Barthez,M.A., Ville,Y., Bole-Feysot,C., Nitschke,P., Lyonnet,S.,
            Munnich,A., Johnson,C.A., Encha-Razavi,F., Cormier-Daire,V.,
            Thauvin-Robinet,C., Vekemans,M. and Attie-Bitach,T.
  TITLE     TCTN3 mutations cause Mohr-Majewski syndrome
  JOURNAL   Am J Hum Genet 91 (2), 372-378 (2012)
   PUBMED   22883145
  REMARK    GeneRIF: TCTN3 mutations cause Mohr-Majewski syndrome.
REFERENCE   6  (residues 1 to 575)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 575)
  AUTHORS   Park,K.M., Kang,E., Jeon,Y.J., Kim,N., Kim,N.S., Yoo,H.S.,
            Yeom,Y.I. and Kim,S.J.
  TITLE     Identification of novel regulators of apoptosis using a
            high-throughput cell-based screen
  JOURNAL   Mol Cells 23 (2), 170-174 (2007)
   PUBMED   17464193
REFERENCE   8  (residues 1 to 575)
  AUTHORS   Reiter,J.F. and Skarnes,W.C.
  TITLE     Tectonic, a novel regulator of the Hedgehog pathway required for
            both activation and inhibition
  JOURNAL   Genes Dev 20 (1), 22-27 (2006)
   PUBMED   16357211
REFERENCE   9  (residues 1 to 575)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 575)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL356632.12.
            
            On Aug 18, 2022 this sequence version replaced XP_024303703.2.
            
            Summary: This gene encodes a member of the tectonic gene family
            which functions in Hedgehog signal transduction and development of
            the neural tube. Mutations in this gene have been associated with
            Orofaciodigital Syndrome IV and Joubert Syndrom 18. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed for this gene. [provided by RefSeq, Sep 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3305662.1,
                                           SRR14038196.1920431.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..575
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.1"
     Protein         1..575
                     /product="tectonic-3 isoform c precursor"
                     /calculated_mol_wt=60248
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2545
     Region          90..363
                     /region_name="TCTN_DUF1619"
                     /note="Tectonic domain DUF1619; pfam07773"
                     /db_xref="CDD:462260"
     CDS             1..575
                     /gene="TCTN3"
                     /gene_synonym="C10orf61; JBTS18; OFD4; TECT3"
                     /coded_by="NM_001410982.1:29..1756"
                     /note="isoform c precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS91309.1"
                     /db_xref="GeneID:26123"
                     /db_xref="HGNC:HGNC:24519"
                     /db_xref="MIM:613847"
ORIGIN      
        1 mrtpqlallq vfflvfpdgv rpqpssspsg avptslelqr gtdggtlqsp seatatrpav
       61 pglptvvptl vtpsapgnrt vdlfpvlpic vcdltpgacd incccdrdcy llhprtvfsf
      121 clpgsvrsss wvcvdnsvif rsnspfpsrv fmdsngirqf cvhvnnsnln yfqklqkvna
      181 tnfqalaaef ggesftstfq tqsppsfyra gdpiltyfpk wsvisllrqp agvgagglca
      241 esnpagfles ksttctrffk nlassctlds alnaasyynf tvlkvprsmt dpqnmevtye
      301 ietngtfgiq kvsvslgqtn ltvepgaslq qhfilrfraf qqstaaslts prsgnpgyiv
      361 gkpllaltdd isyssqgngs csvkrhevqf gvnaisgckl rlkkadcshl qqeiyqtlhg
      421 rprpeyvaif gnadpaqkgg wtrilnrhcs isainctscc lipvsleiqv lwayvgllsn
      481 pqahvsgvrf lyqcqsiqds qqvtevsltt lvnfvditqk pqpprgqpkm dwkwpfdffp
      541 fkvafsrgvf sqkcsvspil ilcllllgvl nletm
//
LOCUS       NP_001427518             425 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform g [Homo sapiens].
ACCESSION   NP_001427518
VERSION     NP_001427518.1
DBSOURCE    REFSEQ: accession NM_001440589.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 425)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 425)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 425)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138512.398753.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..425
                     /product="polycomb protein EED isoform g"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=48257
     Region          96..140
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          148..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          150..423
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          193..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          240..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          309..382
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          390..416
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..425
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001440589.1:478..1755"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdendd avsiesgtnt erpdtptntp
       61 napgrkswgk gkwkskkcky sfkcvnslke dhnqplfgvq fnwhskegdp lvfatvgsnr
      121 vtlyechsqg eirllqsyvd adadenfytc awtydsntsh pllavagsrg iiriinpitm
      181 qcikhyvghg nainelkfhp rdpnlllsvs kdhalrlwni qtdtlvaifg gveghrdevl
      241 sadydllgek imscgmdhsl klwrinskrm mnaikesydy npnktnrpfi sqkihfpdfs
      301 trdihrnyvd cvrwlgdlil sksgrailhs hqqcmrdpvs pnlrqhlsce naivcwkpgk
      361 meddidkikp sesnvtilgr fdysqcdiwy mrfsmdfwqk mlalgnqvgk lyvwdleved
      421 phkak
//
LOCUS       NP_001392806            1042 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 6 [Homo sapiens].
ACCESSION   NP_001392806
VERSION     NP_001392806.1
DBSOURCE    REFSEQ: accession NM_001405877.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1042)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1042)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1042)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1042)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1042)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1042)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1042)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.13237.1,
                                           SRR14038196.3585527.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1042
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 6"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=113587
     Site            104
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          145..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          225..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          399..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          822..942
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..1042
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405877.1:697..3825"
                     /note="isoform 6 is encoded by transcript variant 18"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankgli
      481 vlgevpppeh ttdlflplss evktdhgtdk liesvsqple nhgapiighi seslstkscg
      541 alrpvngvin tlqpvladhi pgdssdaeeq lhkkqrlnlv ssssdgtcva artrpvlsck
      601 krrlvrpnsi vplskkvhrn stirpgcdvn pscalcgsgs intmppeihy eapllerlsq
      661 ldscvhpvla fpddvptslh fqsmlksqwq nkpfdkikpp kklslkhrap mpgslpdsar
      721 kdrhklvssf lttamlkhht dmssssylaa thhpphsplv rqlstssdsp apassssqvt
      781 astsqqpvrr rrgessfdin nivipmsvaa ttrveklqyk eiltpswrev dlqslkgspd
      841 eeneeiedls daafaalhak ceemerarwl wttsvppqrr gsrsyrssdg rttpqlgsan
      901 pstpqpaspd vssshslsey shgqsprspi spelhsaplt pvardtprhl asedtrcstp
      961 elgldeqsvq pwerrtfpla hspqaecedq ldaqeraarc trrtsgsktg reteaaptsp
     1021 pivplksrhl vaaataqrpt hr
//
LOCUS       NP_001428152             476 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 2 [Homo sapiens].
ACCESSION   NP_001428152
VERSION     NP_001428152.1
DBSOURCE    REFSEQ: accession NM_001441223.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3397896.1,
                                           SRR18074967.798124.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..476
                     /product="calcium uptake protein 1, mitochondrial isoform
                     2"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=50585
     transit_peptide 1..33
                     /note="Mitochondrion. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:26387864; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
                     /calculated_mol_wt=3784
     mat_peptide     34..476
                     /product="Calcium uptake protein 1, mitochondrial.
                     /id=PRO_0000322990"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
                     /calculated_mol_wt=50585
     Region          68..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          99..110
                     /region_name="Polybasic region.
                     /evidence=ECO:0000269|PubMed:27099988"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCX5; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          126..129
                     /region_name="K/R-ring.
                     /evidence=ECO:0000269|PubMed:32494073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          222..441
                     /region_name="EFh_MICU1"
                     /note="EF-hand, calcium binding motif, found in calcium
                     uptake protein 1, mitochondrial (MICU1) and similar
                     proteins; cd16173"
                     /db_xref="CDD:320081"
     Region          222..251
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Site            order(224,376,379,382..383,385,403)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:320081"
     Site            order(231,233,235,242,421,423,425,432)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320081"
     Region          259..263
                     /region_name="K/R-ring.
                     /evidence=ECO:0000269|PubMed:32494073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          277..307
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          375..404
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          412..441
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          455..465
                     /region_name="C-helix region.
                     /evidence=ECO:0000269|PubMed:24514027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Site            455
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:27642082; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
     CDS             1..476
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001441223.1:170..1600"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mfrlnslsal aelavgsrwy hggsqpiqir rrlmmvaflg asavtastgl lwkrahaesp
       61 pcvdnlksdi gdkgknkdeg dvcnhekkta dlaphpeekk kkrsgfrdrk vmeyenrira
      121 ystpdkifry fatlkvisep geaevfmtpe dfvrsitpne kqpehlgldq yiikrfdgkk
      181 isqerekfad egsifytlge cglisfsdyi flttvlstpq rnfeiafkmf dlngdgevdm
      241 eefeqvqsii rsqtsmgmrh rdrpttgntl ksglcsaltt yffgadlkgk ltiknflefq
      301 rklqhdvlkl eferhdpvdg riterqfggm llaysgvqsk kltamqrqlk khfkegkglt
      361 fqevenfftf lknindvdta lsfyhmagas ldkvtmqqva rtvakvelsd hvcdvvfalf
      421 dcdgngelsn kefvsimkqr lmrglekpkd mgftrlmqam wkcaqetawd falpkq
//
LOCUS       NP_001427450             552 aa            linear   PRI 21-NOV-2025
DEFINITION  plasma kallikrein isoform 4 precursor [Homo sapiens].
ACCESSION   NP_001427450 XP_016863672 XP_054205940
VERSION     NP_001427450.1
DBSOURCE    REFSEQ: accession NM_001440521.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Longhurst,H.J., Lindsay,K., Petersen,R.S., Fijen,L.M., Gurugama,P.,
            Maag,D., Butler,J.S., Shah,M.Y., Golden,A., Xu,Y., Boiselle,C.,
            Vogel,J.D., Abdelhady,A.M., Maitland,M.L., McKee,M.D., Seitzer,J.,
            Han,B.W., Soukamneuth,S., Leonard,J., Sepp-Lorenzino,L.,
            Clark,E.D., Lebwohl,D. and Cohn,D.M.
  TITLE     CRISPR-Cas9 In Vivo Gene Editing of KLKB1 for Hereditary Angioedema
  JOURNAL   N Engl J Med 390 (5), 432-441 (2024)
   PUBMED   38294975
  REMARK    GeneRIF: CRISPR-Cas9 In Vivo Gene Editing of KLKB1 for Hereditary
            Angioedema.
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Schachtl-Riess,J.F., Schonherr,S., Lamina,C., Forer,L., Coassin,S.,
            Streiter,G., Kheirkhah,A., Li,Y., Meiselbach,H., Di Maio,S.,
            Eckardt,K.U., Kottgen,A. and Kronenberg,F.
  CONSRTM   GCKD investigators
  TITLE     KLKB1 and CLSTN2 are associated with HDL-mediated cholesterol
            efflux capacity in a genome-wide association study
  JOURNAL   Atherosclerosis 368, 1-11 (2023)
   PUBMED   36812656
  REMARK    GeneRIF: KLKB1 and CLSTN2 are associated with HDL-mediated
            cholesterol efflux capacity in a genome-wide association study.
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Feng,L., Liu,Y., Chen,M. and Hu,Y.
  TITLE     [Matrix metalloproteinase 14 and plasma kallikrein 1 may be
            potential biomarkers in the diagnosis and treatment of sepsis: a
            proteomics and bioinformatics analysis]
  JOURNAL   Zhonghua Wei Zhong Bing Ji Jiu Yi Xue 34 (7), 676-681 (2022)
   PUBMED   36100402
  REMARK    GeneRIF: [Matrix metalloproteinase 14 and plasma kallikrein 1 may
            be potential biomarkers in the diagnosis and treatment of sepsis: a
            proteomics and bioinformatics analysis].
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Wan,J., Vadaq,N., Konings,J., Jaeger,M., Kumar,V., de Laat,B.,
            Joosten,L., Netea,M.G., van der Ven,A.J., de Groot,P.G., de Mast,Q.
            and Roest,M.
  TITLE     Kallikrein augments the anticoagulant function of the protein C
            system in thrombin generation
  JOURNAL   J Thromb Haemost 20 (1), 48-57 (2022)
   PUBMED   34532976
  REMARK    GeneRIF: Kallikrein augments the anticoagulant function of the
            protein C system in thrombin generation.
REFERENCE   5  (residues 1 to 552)
  AUTHORS   Beaubien,G., Rosinski-Chupin,I., Mattei,M.G., Mbikay,M.,
            Chretien,M. and Seidah,N.G.
  TITLE     Gene structure and chromosomal localization of plasma kallikrein
  JOURNAL   Biochemistry 30 (6), 1628-1635 (1991)
   PUBMED   1993180
REFERENCE   6  (residues 1 to 552)
  AUTHORS   Chung,D.W., Fujikawa,K., McMullen,B.A. and Davie,E.W.
  TITLE     Human plasma prekallikrein, a zymogen to a serine protease that
            contains four tandem repeats
  JOURNAL   Biochemistry 25 (9), 2410-2417 (1986)
   PUBMED   3521732
REFERENCE   7  (residues 1 to 552)
  AUTHORS   Thompson,R.E., Mandle,R. Jr. and Kaplan,A.P.
  TITLE     Studies of binding of prekallikrein and Factor XI to high molecular
            weight kininogen and its light chain
  JOURNAL   Proc Natl Acad Sci U S A 76 (10), 4862-4866 (1979)
   PUBMED   291905
REFERENCE   8  (residues 1 to 552)
  AUTHORS   Mandle,R.J. Jr. and Kaplan,A.P.
  TITLE     Hageman-factor-dependent fibrinolysis: generation of fibrinolytic
            activity by the interaction of human activated factor XI and
            plasminogen
  JOURNAL   Blood 54 (4), 850-862 (1979)
   PUBMED   89876
REFERENCE   9  (residues 1 to 552)
  AUTHORS   Aznar,J.A., Espana,F., Aznar,J., Tascon,A. and Jimenez,C.
  TITLE     Fletcher factor deficiency: report of a new family
  JOURNAL   Scand J Haematol 21 (2), 94-98 (1978)
   PUBMED   694428
REFERENCE   10 (residues 1 to 552)
  AUTHORS   Meier,H.L., Pierce,J.V., Colman,R.W. and Kaplan,A.P.
  TITLE     Activation and function of human Hageman factor. The role of high
            molecular weight kininogen and prekallikrein
  JOURNAL   J Clin Invest 60 (1), 18-31 (1977)
   PUBMED   874082
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC110771.3.
            
            On or before May 21, 2025 this sequence version replaced
            XP_016863672.1, XP_054205940.1.
            
            Summary: This gene encodes a glycoprotein that participates in the
            surface-dependent activation of blood coagulation, fibrinolysis,
            kinin generation and inflammation. The encoded preproprotein
            present in plasma as a non-covalent complex with high molecular
            weight kininogen undergoes proteolytic processing mediated by
            activated coagulation factor XII to generate a disulfide-linked,
            heterodimeric serine protease comprised of heavy and light chains.
            Certain mutations in this gene cause prekallikrein deficiency.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2145122,
                              SAMEA2155590 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q35.2"
     Protein         1..552
                     /product="plasma kallikrein isoform 4 precursor"
                     /EC_number="3.4.21.34"
                     /note="kallikrein B, plasma (Fletcher factor) 1;
                     kininogenin; plasma prekallikrein; plasma kallikrein"
                     /calculated_mol_wt=59674
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2184
     Region          21..104
                     /region_name="APPLE"
                     /note="APPLE domain; smart00223"
                     /db_xref="CDD:128519"
     Site            order(37,39,50)
                     /site_type="active"
                     /note="putative binding site [active]"
                     /db_xref="CDD:238533"
     Region          111..194
                     /region_name="APPLE"
                     /note="APPLE domain; smart00223"
                     /db_xref="CDD:128519"
     Site            order(127,129,140)
                     /site_type="active"
                     /note="putative binding site [active]"
                     /db_xref="CDD:238533"
     Site            127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:3521732; propagated from
                     UniProtKB/Swiss-Prot (P03952.2)"
     Region          201..284
                     /region_name="APPLE"
                     /note="APPLE domain; smart00223"
                     /db_xref="CDD:128519"
     Site            order(217,219,230)
                     /site_type="active"
                     /note="putative binding site [active]"
                     /db_xref="CDD:238533"
     Region          292..375
                     /region_name="APPLE"
                     /note="APPLE domain; smart00223"
                     /db_xref="CDD:128519"
     Site            order(308,310,321)
                     /site_type="active"
                     /note="putative binding site [active]"
                     /db_xref="CDD:238533"
     Site            308
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3521732;
                     propagated from UniProtKB/Swiss-Prot (P03952.2)"
     Region          391..>538
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            391
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            396
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3521732;
                     propagated from UniProtKB/Swiss-Prot (P03952.2)"
     Site            453
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:3521732; propagated from
                     UniProtKB/Swiss-Prot (P03952.2)"
     Site            494
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3521732;
                     propagated from UniProtKB/Swiss-Prot (P03952.2)"
     CDS             1..552
                     /gene="KLKB1"
                     /gene_synonym="KLK3; PKK; PKKD; PPK"
                     /coded_by="NM_001440521.1:83..1741"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:3818"
                     /db_xref="HGNC:HGNC:6371"
                     /db_xref="MIM:229000"
ORIGIN      
        1 milfkqatyf islfatvscg cltqlyenaf frggdvasmy tpnaqycqmr ctfhprcllf
       61 sflpassind mekrfgcflk dsvtgtlpkv hrtgavsghs lkqcghqisa chrdiykgvd
      121 mrgvnfnvsk vssveecqkr ctsnircqff syatqtfhka eyrnncllky spggtptaik
      181 vlsnvesgfs lkpcalseig chmnifqhla fsdvdvarvl tpdafvcrti ctyhpnclff
      241 tfytnvwkie sqrnvcllkt sesgtpssst pqentisgys lltckrtlpe pchskiypgv
      301 dfggeelnvt fvkgvnvcqe tctkmircqf ftysllpedc keekckcflr lsmdgsptri
      361 aygtqgssgy slrlcntgdn svcttktstr ivggtnsswg ewpwqvslqv kltaqrhlcg
      421 gslighqwvl taahcfdglp lqdvwriysg ilnlsditkd tpfsqikeii ihqnykvseg
      481 nhdialiklq aplnytefqk piclpskgdt stiytncwvt gwgfskekgr frwslslqtq
      541 wnvafgghhq lg
//
LOCUS       NP_001424663             636 aa            linear   PRI 21-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001424663
VERSION     NP_001424663.1
DBSOURCE    REFSEQ: accession NM_001437734.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 636)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 636)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 636)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 636)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 636)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 636)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 636)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 636)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008641.7.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1140445.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..636
                     /product="TNFAIP3-interacting protein 1 isoform 3"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=71733
     Region          14..>149
                     /region_name="Speriolin_N"
                     /note="Speriolin N terminus; pfam15058"
                     /db_xref="CDD:434426"
     Region          61..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          94..412
                     /region_name="Interaction with Nef"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Region          <214..>251
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          252..283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          <298..>538
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          351..367
                     /region_name="Interaction with Shigella flexneri ipah9.8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          431..588
                     /region_name="Required for inhibitory activity of
                     TNF-induced NF-kappa-B activation. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          452..510
                     /region_name="Ubiquitin-binding domain (UBD)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Region          524..530
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            552
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17632516; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            571
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9WUU8; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            599
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          603..636
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            627
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     CDS             1..636
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001437734.1:115..2025"
                     /note="isoform 3 is encoded by transcript variant 13"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 megrgpyriy dpggsvpsge asaaferlvk ensrlkekmq gikmlgelle esqmeatrlr
       61 qkaeelvkdn ellpppspsl gsfdplaelt gkdsnvtasp tapacpsdkp apvqkppssg
      121 tssefevvtp eeqnspesss hanamalgpl predgnlmlh lqrlettlsv caeepdhgql
      181 fthlgrmale fnrlaskvhk neqrtsilqt lceqlrkene alkakldkgl eqrdqaaerl
      241 reenlelkkl lmsngnkega sgrpgspkme gtgkkavagq qqasvtagkv pevvalgaae
      301 kkvkmleqqr sellevnkqw dqhfrsmkqq yeqkitelrq kladlqkqvt dleaereqkq
      361 rdfdrkllla kskiemeetd keqltaeake lrqkvkylqd qlspltrqre yqekeiqrln
      421 kaleealsiq tppsspptaf gspegagall rkqelvtqne llkqqvkife edfqrersdr
      481 ermneekeel kkqveklqaq vtlsnaqlka fkdeekarea lrqqkrkaka sgeryhveph
      541 pehlcgaypy ayppmpamvp hhgfedwsqi ryppppmame hppplpnsrl fhlpeytwrl
      601 pcggvrnpnq ssqvmdppta rptepespkn dregpq
//
LOCUS       NP_001007538             333 aa            linear   PRI 21-NOV-2025
DEFINITION  complement C1q and tumor necrosis factor-related protein 9B
            precursor [Homo sapiens].
ACCESSION   NP_001007538 XP_370715
VERSION     NP_001007538.1
DBSOURCE    REFSEQ: accession NM_001007537.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Dong,F., Jiang,M., Zhang,Z., Li,F. and Lian,Y.
  TITLE     C1q/TNF-related protein-9 suppresses inflammation in synovial cells
            from patients with osteoarthritis
  JOURNAL   Scand J Rheumatol 51 (5), 368-373 (2022)
   PUBMED   34514937
  REMARK    GeneRIF: C1q/TNF-related protein-9 suppresses inflammation in
            synovial cells from patients with osteoarthritis.
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Li,Z., Du,Y., Jia,L., Fan,J., Guo,R., Ma,X., Wang,X., Nie,S. and
            Wei,Y.
  TITLE     Association of C1q/TNF-Related Protein-9 (CTRP9) Level with
            Obstructive Sleep Apnea in Patients with Coronary Artery Disease
  JOURNAL   Mediators Inflamm 2020, 7281391 (2020)
   PUBMED   32831639
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Du,Y., Zhang,S., Yu,H., Wu,Y., Cao,N., Wang,W., Xu,W., Li,Y. and
            Liu,H.
  TITLE     Autoantibodies Against beta1-Adrenoceptor Exaggerated Ventricular
            Remodeling by Inhibiting CTRP9 Expression
  JOURNAL   J Am Heart Assoc 8 (4), e010475 (2019)
   PUBMED   30764693
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Shi,Y., Qu,J., Zhang,D., Zhao,P., Zhang,Q., Tam,P.O.S., Sun,L.,
            Zuo,X., Zhou,X., Xiao,X., Hu,J., Li,Y., Cai,L., Liu,X., Lu,F.,
            Liao,S., Chen,B., He,F., Gong,B., Lin,H., Ma,S., Cheng,J.,
            Zhang,J., Chen,Y., Zhao,F., Yang,X., Chen,Y., Yang,C., Lam,D.S.C.,
            Li,X., Shi,F., Wu,Z., Lin,Y., Yang,J., Li,S., Ren,Y., Xue,A.,
            Fan,Y., Li,D., Pang,C.P., Zhang,X. and Yang,Z.
  TITLE     Genetic variants at 13q12.12 are associated with high myopia in the
            Han Chinese population
  JOURNAL   Am J Hum Genet 88 (6), 805-813 (2011)
   PUBMED   21640322
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Peterson,J.M., Wei,Z. and Wong,G.W.
  TITLE     CTRP8 and CTRP9B are novel proteins that hetero-oligomerize with
            C1q/TNF family members
  JOURNAL   Biochem Biophys Res Commun 388 (2), 360-365 (2009)
   PUBMED   19666007
  REMARK    GeneRIF: two novel human C1q/TNF family members, designated as
            CTRP8 and CTRP9B were described.
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Ghai,R., Waters,P., Roumenina,L.T., Gadjeva,M., Kojouharova,M.S.,
            Reid,K.B., Sim,R.B. and Kishore,U.
  TITLE     C1q and its growing family
  JOURNAL   Immunobiology 212 (4-5), 253-266 (2007)
   PUBMED   17544811
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445985.10.
            
            On Dec 31, 2004 this sequence version replaced XP_370715.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the protein.
            
            ##Evidence-Data-START##
            CDS exon combination :: EL734395.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2147596, SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000713589.1/ ENSP00000518885.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.12"
     Protein         1..333
                     /product="complement C1q and tumor necrosis factor-related
                     protein 9B precursor"
                     /note="collagen triple helix repeat-containing;
                     C1q/TNF-related protein 9B; complement C1q and tumor
                     necrosis factor-related protein 9B; C1q and tumor necrosis
                     factor related protein 9B"
                     /calculated_mol_wt=32484
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2247
     mat_peptide     20..333
                     /product="Complement C1q and tumor necrosis factor-related
                     protein 9B. /id=PRO_0000348424"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RNN3.1)"
                     /calculated_mol_wt=32484
     Region          24..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B2RNN3.1)"
     Region          <35..>194
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          203..329
                     /region_name="C1q"
                     /note="C1q domain; pfam00386"
                     /db_xref="CDD:395310"
     CDS             1..333
                     /gene="C1QTNF9B"
                     /gene_synonym="CTRP9B"
                     /coded_by="NM_001007537.3:211..1212"
                     /db_xref="CCDS:CCDS31947.1"
                     /db_xref="GeneID:387911"
                     /db_xref="HGNC:HGNC:34072"
                     /db_xref="MIM:614148"
ORIGIN      
        1 mriwwlllai eictgninsq dtcrqghpgi pgnpghnglp grdgrdgakg dkgdagepgc
       61 pgspgkdgts gekgergadg kveakgikgd qgsrgspgkh gpkglagpmg ekglrgetgp
      121 qgqkgnkgdv gptgpegprg nigplgptgl pgpmgpigkp gpkgeagptg pqgepgvrgi
      181 rgwkgdrgek gkigetlvlp ksaftvgltv lskfpssdvp ikfdkilyne fnhydtavgk
      241 ftchiagvyy ftyhitvfsr nvqvslvkng vkilhtrday vssedqasgs ivlqlklgde
      301 mwlqvtgger fnglfadedd dttftgfllf ssq
//
LOCUS       NP_001393549            1042 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 11 [Homo sapiens].
ACCESSION   NP_001393549
VERSION     NP_001393549.1
DBSOURCE    REFSEQ: accession NM_001406620.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1042)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1042)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1042)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1042)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1042)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1042)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1042)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR18074969.863504.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1042
                     /product="hamartin isoform 11"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=116074
     Region          16..597
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <586..>838
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1042
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406620.1:262..3390"
                     /note="isoform 11 is encoded by transcript variant 34"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mdtdvvvltt gvlvlitmlp mipqsgkqhl ldffdifgrl sswclkkpgh vaevylvhlh
       61 asvyalfhrl ygmypcnfvs flrshysmke nletfeevvk pmmehvrihp elvtgskdhe
      121 ldprrwkrle thdvviecak isldpteasy edgysvshqi sarfphrsad vttspyadtq
      181 nsygcatstp ystsrlmlln mpgqlpqtls spstrlitep pqatlwspsm vcgmttppts
      241 pgnvppdlsh pyskvfgttg gkgtplgtpa tspppaplch sddyvhislp qatvtpprke
      301 ermdsarpcl hrqhhllndr gseeppgskg svtlsdlpgf lgdlaseeds iekdkeeaai
      361 srelseitta eaepvvprgg fdspfyrdsl pgsqrkthsa asssqgasvn peplhssldk
      421 lgpdtpkqaf tpidlpcgsa despagdrec qtsletsift pspckipppt rvgfgsgqpp
      481 pydhlfeval pktahhfvir kteellkkak gnteedgvps tspmevldrl iqqgadahsk
      541 elnklplpsk svdwthfggs ppsdeirtlr dqllllhnql lyerfkrqqh alrnrrllrk
      601 vikaaaleeh naamkdqlkl qekdiqmwkv slqkeqaryn qlqeqrdtmv tklhsqirql
      661 qhdreefynq sqelqtkled crnmiaelri elkkannkvc htelllsqvs qklsnsesvq
      721 qqmeflnrql lvlgevnely leqlqnkhsd ttkevemmka ayrkeleknr shvlqqtqrl
      781 dtsqkrilel eshlakkdhl lleqkkyled vklqargqlq aaesryeaqk ritqvfelei
      841 ldlygrlekd gllkkleeek aeaaeaaeer ldccndgcsd smvghneeas ghngetktpr
      901 pssargssgs rggggsssss selstpekpp hqragpfssr wettmgeasa sipttvgslp
      961 ssksflgmka relfrnkses qcdedgmtss lseslktelg kdlgveakip lnldgphpsp
     1021 ptpdsvgqlh imdynethhe hs
//
LOCUS       NP_001426088             506 aa            linear   PRI 21-NOV-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein Q isoform 10 [Homo
            sapiens].
ACCESSION   NP_001426088 XP_047274039 XP_054210018
VERSION     NP_001426088.1
DBSOURCE    REFSEQ: accession NM_001439159.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Ishtayeh,H., Galves,M., Barnatan,T.T., Berdichevsky,Y.,
            Amer-Sarsour,F., Pasmanik-Chor,M., Braverman,I., Blumen,S.C. and
            Ashkenazi,A.
  TITLE     Oculopharyngeal muscular dystrophy mutations link the RNA-binding
            protein HNRNPQ to autophagosome biogenesis
  JOURNAL   Aging Cell 22 (10), e13949 (2023)
   PUBMED   37559347
  REMARK    GeneRIF: Oculopharyngeal muscular dystrophy mutations link the
            RNA-binding protein HNRNPQ to autophagosome biogenesis.
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Semino,F., Schroter,J., Willemsen,M.H., Bast,T., Biskup,S.,
            Beck-Woedl,S., Brennenstuhl,H., Schaaf,C.P., Kolker,S.,
            Hoffmann,G.F., Haack,T.B. and Syrbe,S.
  TITLE     Further evidence for de novo variants in SYNCRIP as the cause of a
            neurodevelopmental disorder
  JOURNAL   Hum Mutat 42 (9), 1094-1100 (2021)
   PUBMED   34157790
  REMARK    GeneRIF: Further evidence for de novo variants in SYNCRIP as the
            cause of a neurodevelopmental disorder.
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 506)
  AUTHORS   Mourelatos,Z., Abel,L., Yong,J., Kataoka,N. and Dreyfuss,G.
  TITLE     SMN interacts with a novel family of hnRNP and spliceosomal
            proteins
  JOURNAL   EMBO J 20 (19), 5443-5452 (2001)
   PUBMED   11574476
REFERENCE   6  (residues 1 to 506)
  AUTHORS   Lau,P.P., Chang,B.H. and Chan,L.
  TITLE     Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a
            component of apobec-1 editosome
  JOURNAL   Biochem Biophys Res Commun 282 (4), 977-983 (2001)
   PUBMED   11352648
REFERENCE   7  (residues 1 to 506)
  AUTHORS   Blanc,V., Navaratnam,N., Henderson,J.O., Anant,S., Kennedy,S.,
            Jarmuz,A., Scott,J. and Davidson,N.O.
  TITLE     Identification of GRY-RBP as an apolipoprotein B RNA-binding
            protein that interacts with both apobec-1 and apobec-1
            complementation factor to modulate C to U editing
  JOURNAL   J Biol Chem 276 (13), 10272-10283 (2001)
   PUBMED   11134005
REFERENCE   8  (residues 1 to 506)
  AUTHORS   Grosset,C., Chen,C.Y., Xu,N., Sonenberg,N., Jacquemin-Sablon,H. and
            Shyu,A.B.
  TITLE     A mechanism for translationally coupled mRNA turnover: interaction
            between the poly(A) tail and a c-fos RNA coding determinant via a
            protein complex
  JOURNAL   Cell 103 (1), 29-40 (2000)
   PUBMED   11051545
REFERENCE   9  (residues 1 to 506)
  AUTHORS   Mizutani,A., Fukuda,M., Ibata,K., Shiraishi,Y. and Mikoshiba,K.
  TITLE     SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear
            ribonucleoprotein R, interacts with ubiquitous synaptotagmin
            isoforms
  JOURNAL   J Biol Chem 275 (13), 9823-9831 (2000)
   PUBMED   10734137
REFERENCE   10 (residues 1 to 506)
  AUTHORS   Harris,C.E., Boden,R.A. and Astell,C.R.
  TITLE     A novel heterogeneous nuclear ribonucleoprotein-like protein
            interacts with NS1 of the minute virus of mice
  JOURNAL   J Virol 73 (1), 72-80 (1999)
   PUBMED   9847309
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136082.22.
            
            On or before Apr 28, 2025 this sequence version replaced
            XP_047274039.1, XP_054210018.1.
            
            Summary: This gene encodes a member of the cellular heterogeneous
            nuclear ribonucleoprotein (hnRNP) family. hnRNPs are RNA binding
            proteins that complex with heterogeneous nuclear RNA (hnRNA) and
            regulate alternative splicing, polyadenylation, and other aspects
            of mRNA metabolism and transport. The encoded protein plays a role
            in multiple aspects of mRNA maturation and is associated with
            several multiprotein complexes including the apoB RNA
            editing-complex and survival of motor neurons (SMN) complex.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene, and a pseudogene of this
            gene is located on the short arm of chromosome 20. [provided by
            RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.591082.1,
                                           SRR14372080.2427920.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.3"
     Protein         1..506
                     /product="heterogeneous nuclear ribonucleoprotein Q
                     isoform 10"
                     /note="NS1-associated protein 1; heterogeneous nuclear
                     ribonucleoprotein Q; glycine- and tyrosine-rich
                     RNA-binding protein"
                     /calculated_mol_wt=56564
     Region          5..494
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     CDS             1..506
                     /gene="SYNCRIP"
                     /gene_synonym="GRY-RBP; GRYRBP; hnRNP-Q; HNRNPQ; HNRPQ1;
                     NSAP1; PP68"
                     /coded_by="NM_001439159.1:237..1757"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:10492"
                     /db_xref="HGNC:HGNC:16918"
                     /db_xref="MIM:616686"
ORIGIN      
        1 mktyrqrekq gtkvadsskg pdeakikall ertgytldvt tgqrkyggpp pdsvysgqqp
       61 svgteifvgk iprdlfedel vplfekagpi wdlrlmmdpl tglnrgyafv tfctkeaaqe
      121 avklynnhei rsgkhigvci svannrlfvg sipksktkeq ileefskvte gltdvilyhq
      181 pddkkknrgf cfleyedhkt aaqarrrlms gkvkvwgnvg tvewadpied pdpevmakvk
      241 vlfvrnlant vteeilekaf sqfgklervk klkdyafihf derdgavkam eemngkdleg
      301 enieivfakp pdqkrkerka qrqaaknqmy ddyyyygpph mppptrgrgr ggrggygypp
      361 dyygyedyyd yygydyhnyr ggyedpyygy edfqvgargr ggrgargaap srgrgaappr
      421 gragysqrgg pgsargvrga rggaqqqrgr gvrgarggrg gnvggkrkad gynqpdskrr
      481 qtnnqnwgsq piaqqplqgk rgrgrs
//
LOCUS       NP_001427877             935 aa            linear   PRI 21-NOV-2025
DEFINITION  centriole and centriolar satellite protein OFD1 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001427877 XP_047298546 XP_054183984
VERSION     NP_001427877.1
DBSOURCE    REFSEQ: accession NM_001440948.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 935)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 935)
  AUTHORS   Kim,N.H., Lee,C.H. and Lee,A.Y.
  TITLE     Extraciliary OFD1 Is Involved in Melanocyte Survival through Cell
            Adhesion to ECM via Paxillin
  JOURNAL   Int J Mol Sci 24 (24), 17528 (2023)
   PUBMED   38139355
  REMARK    GeneRIF: Extraciliary OFD1 Is Involved in Melanocyte Survival
            through Cell Adhesion to ECM via Paxillin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 935)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 935)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   5  (residues 1 to 935)
  AUTHORS   Alitalo,T., Francis,F., Kere,J., Lehrach,H., Schlessinger,D. and
            Willard,H.F.
  TITLE     A 6-Mb YAC contig in Xp22.1-p22.2 spanning the DXS69E, XE59, GLRA2,
            PIGA, GRPR, CALB3, and PHKA2 genes
  JOURNAL   Genomics 25 (3), 691-700 (1995)
   PUBMED   7759104
REFERENCE   6  (residues 1 to 935)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   7  (residues 1 to 935)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   8  (residues 1 to 935)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
REFERENCE   9  (residues 1 to 935)
  AUTHORS   Franco,B., Bruel,A.L. and Thauvin-Robinet,C.
  TITLE     Oral-Facial-Digital Syndrome Type I
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301367
REFERENCE   10 (residues 1 to 935)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC003037.1.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047298546.1, XP_054183984.1.
            
            Summary: This gene is located on the X chromosome and encodes a
            centrosomal protein. A knockout mouse model has been used to study
            the effect of mutations in this gene. The mouse gene is also
            located on the X chromosome, however, unlike the human gene it is
            not subject to X inactivation. Mutations in this gene are
            associated with oral-facial-digital syndrome type I and
            Simpson-Golabi-Behmel syndrome type 2. Many pseudogenes have been
            identified; a single pseudogene is found on chromosome 5 while as
            many as fifteen have been found on the Y chromosome. [provided by
            RefSeq, Aug 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2912249.1,
                                           SRR14038195.905603.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..935
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..935
                     /product="centriole and centriolar satellite protein OFD1
                     isoform 5"
                     /note="oral-facial-digital syndrome 1 protein; protein
                     71-7A; Joubert syndrome type 10; centriole and centriolar
                     satellite protein OFD1"
                     /calculated_mol_wt=107913
     Region          75..101
                     /region_name="LisH_2"
                     /note="pfam16045"
                     /db_xref="CDD:464992"
     Region          191..>914
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          205..>516
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..935
                     /gene="OFD1"
                     /gene_synonym="71-7A; CXorf5; JBTS10; RP23; SGBS2"
                     /coded_by="NM_001440948.1:325..3132"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:8481"
                     /db_xref="HGNC:HGNC:2567"
                     /db_xref="MIM:300170"
ORIGIN      
        1 mmaqsnmftv advlsqdelr kklyqtfkdr gildtlktql rnqlihelmh pvlsgelqpr
       61 sisvegssll igasnslvad hlqrcgyeys lsvffpesgl akekvftmqd llqlikinpt
      121 sslykslvsg sdkenqkgfl mhflkelaey hqakescnme tqtsstfnrd slaeklqlid
      181 dqfadaypqr ikfesleikl neykreieeq lraemcqklk ffkdteiaki kmeakkkyek
      241 eltmfqndfe kacqakseal vlrekstler ihkhqeietk eiyaqrqlll kdmdllrgre
      301 aelkqrveaf elyqlelkdd yiirtnrlie derknkekav hlqeeliain skkeelnqsv
      361 nrvkelelel esvkaqslai tkqnhmlnek vkemsdysll keeklellaq nkllkqqlee
      421 srnenlrlln rlaqpapela vfqkelrkae kaivveheef escrqalhkq lqdeiehsaq
      481 lkaqilgyka svkslttqva dlklqlkqtq talenevycn pkqsvidrsv nglingnvvp
      541 cngeisgdfl nnpfkqenvl armvasritn yptawvegss pdsdlefvan tkarvkelqq
      601 eaerlekafr syhrrvikns aksplaaksp pslhlleafk nitsssperh ifgedrvvse
      661 qpqvgtleer ndvvealtgs aasrlrggts srrlsstplp kakrslesem yleglgrshi
      721 aspspcpdrm plpsptesrh slsippvssp peqkvglyrr qtelqdksef sdvdklafkd
      781 neefessfec vdqkqieeqk eeekireqqv kerrqreerr qsnlqevler erreleklyq
      841 erkmieeslk ikikkeleme nelemsnqei kdksahsenp lekymkiiqq eqdqesadks
      901 skkmvqegsl vdtlqssdkv esltgfshee lddsw
//
LOCUS       NP_001276325            1590 aa            linear   PRI 21-NOV-2025
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily A member 2 isoform a [Homo sapiens].
ACCESSION   NP_001276325 XP_005251614
VERSION     NP_001276325.1
DBSOURCE    REFSEQ: accession NM_001289396.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1590)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1590)
  AUTHORS   Zhang,Z., Li,Q., Sun,S., Li,Z., Cui,Z., Liu,Q., Zhang,Y., Xiong,S.
            and Zhang,S.
  TITLE     Expression of SMARCA2 and SMARCA4 in gastric adenocarcinoma and
            construction of a nomogram prognostic model
  JOURNAL   Int J Clin Oncol 28 (11), 1487-1500 (2023)
   PUBMED   37634210
  REMARK    GeneRIF: Expression of SMARCA2 and SMARCA4 in gastric
            adenocarcinoma and construction of a nomogram prognostic model.
REFERENCE   3  (residues 1 to 1590)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1590)
  AUTHORS   Zhang,Z., Li,Q., Sun,S., Li,Z., Cui,Z.G., Zhang,M., Liu,Q.,
            Zhang,Y., Xiong,S. and Zhang,S.
  TITLE     Clinicopathological and prognostic significance of SWI/SNF complex
            subunits in undifferentiated gastric carcinoma
  JOURNAL   World J Surg Oncol 20 (1), 383 (2022)
   PUBMED   36464671
  REMARK    GeneRIF: Clinicopathological and prognostic significance of SWI/SNF
            complex subunits in undifferentiated gastric carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1590)
  AUTHORS   Zhang,X., Chen,H., Song,Y., Chen,Z., Liu,X., Rong,P. and Ma,R.
  TITLE     Ten-year follow-up of Nicolaides-Baraitser syndrome with a de novo
            mutation and analysis of 58 gene loci of SMARCA2-associated NCBRS
  JOURNAL   Mol Genet Genomic Med 10 (9), e2009 (2022)
   PUBMED   35811451
  REMARK    GeneRIF: Ten-year follow-up of Nicolaides-Baraitser syndrome with a
            de novo mutation and analysis of 58 gene loci of SMARCA2-associated
            NCBRS.
REFERENCE   6  (residues 1 to 1590)
  AUTHORS   Aves,S.J., Hindley,J., Phear,G.A. and Tongue,N.
  TITLE     A fission yeast gene mapping close to suc1 encodes a protein
            containing two bromodomains
  JOURNAL   Mol Gen Genet 248 (4), 491-498 (1995)
   PUBMED   7565614
REFERENCE   7  (residues 1 to 1590)
  AUTHORS   Chiba,H., Muramatsu,M., Nomoto,A. and Kato,H.
  TITLE     Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and
            Drosophila brahma are transcriptional coactivators cooperating with
            the estrogen receptor and the retinoic acid receptor
  JOURNAL   Nucleic Acids Res 22 (10), 1815-1820 (1994)
   PUBMED   8208605
REFERENCE   8  (residues 1 to 1590)
  AUTHORS   Muchardt,C., Yaniv,M. and Mattei,M.G.
  TITLE     Assignment of HBRM, the human homolog of S. cerevisiae SNF2/SWI2
            and Drosophila brm genes, to chromosome region 9p23-p24, by in situ
            hybridization
  JOURNAL   Mamm Genome 5 (4), 241-243 (1994)
   PUBMED   8012116
REFERENCE   9  (residues 1 to 1590)
  AUTHORS   Muchardt,C. and Yaniv,M.
  TITLE     A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and
            Drosophila brm genes potentiates transcriptional activation by the
            glucocorticoid receptor
  JOURNAL   EMBO J 12 (11), 4279-4290 (1993)
   PUBMED   8223438
REFERENCE   10 (residues 1 to 1590)
  AUTHORS   Abdul-Rahman,O. and May,F.
  TITLE     SMARCA2-Related Nicolaides-Baraitser Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26468571
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359076.16 and AL138755.13.
            
            On Jan 17, 2014 this sequence version replaced XP_005251614.1.
            
            Summary: The protein encoded by this gene is a member of the
            SWI/SNF family of proteins and is highly similar to the brahma
            protein of Drosophila. Members of this family have helicase and
            ATPase activities and are thought to regulate transcription of
            certain genes by altering the chromatin structure around those
            genes. The encoded protein is part of the large ATP-dependent
            chromatin remodeling complex SNF/SWI, which is required for
            transcriptional activation of genes normally repressed by
            chromatin. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene, which contains a
            trinucleotide repeat (CAG) length polymorphism. [provided by
            RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X72889.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1590
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.3"
     Protein         1..1590
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily A member
                     2 isoform a"
                     /note="global transcription activator homologous sequence;
                     SNF2-alpha; sucrose nonfermenting 2-like protein 2;
                     SNF2/SWI2-like protein 2; SWI/SNF-related
                     matrix-associated actin-dependent regulator of chromatin
                     a2; brahma homolog; probable global transcription
                     activator SNF2L2; BAF190B; protein brahma homolog;
                     BRG1-associated factor 190B; ATP-dependent helicase
                     SMARCA2; putative global transcription activator SNF2L2;
                     SWI/SNF related, matrix associated, actin dependent
                     regulator of chromatin, subfamily a, member 2"
                     /calculated_mol_wt=181149
     Region          1..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Region          <46..>450
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          95..176
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          173..207
                     /region_name="QLQ"
                     /note="pfam08880"
                     /db_xref="CDD:462622"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            190
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P51532; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          212..334
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6DIC0; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Region          436..508
                     /region_name="HSA"
                     /note="domain in helicases and associated with SANT
                     domains; smart00573"
                     /db_xref="CDD:214727"
     Region          551..592
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51532; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          589..632
                     /region_name="BRK"
                     /note="BRK domain; pfam07533"
                     /db_xref="CDD:462196"
     Site            591
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            604
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6DIC0; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          627..672
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            670
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51532; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          701..951
                     /region_name="DEXHc_SMARCA2"
                     /note="DEXH-box helicase domain of SMARCA2; cd18063"
                     /db_xref="CDD:350821"
     Region          720..>1202
                     /region_name="PLN03142"
                     /note="Probable chromatin-remodeling complex ATPase chain;
                     Provisional"
                     /db_xref="CDD:215601"
     Site            order(751..757,791,851..852)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350821"
     Region          851..854
                     /region_name="DEGH box"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            997
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            999
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          1259..1326
                     /region_name="SnAC"
                     /note="Snf2-ATP coupling, chromatin remodelling complex;
                     pfam14619"
                     /db_xref="CDD:464219"
     Region          1333..>1419
                     /region_name="Bromodomain"
                     /note="Bromodomains are found in many chromatin-associated
                     proteins and in nuclear histone acetyltransferases. They
                     interact specifically with acetylated lysine; cl02556"
                     /db_xref="CDD:445827"
     Region          1344..1383
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            order(1361,1370,1373,1415,1419)
                     /site_type="active"
                     /note="acetyllysine binding site [active]"
                     /db_xref="CDD:99926"
     Site            1377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          1382..1506
                     /region_name="Bromo_SNF2L2"
                     /note="Bromodomain, SNF2L2-like subfamily, specific to
                     animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related
                     matrix-associated actin-dependent regulator of chromatin
                     subfamily A member 2 is a global transcriptional
                     activator, which cooperates with nuclear hormone...;
                     cd05516"
                     /db_xref="CDD:99947"
     Site            order(1431,1436,1439,1478,1482,1488)
                     /site_type="active"
                     /note="acetyllysine binding site [active]"
                     /db_xref="CDD:99947"
     Region          1506..1590
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            1512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            1516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            1528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            1568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            1572
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     CDS             1..1590
                     /gene="SMARCA2"
                     /gene_synonym="BAF190; BIS; BRM; hBRM; hSNF2a; NCBRS;
                     SAMRCA2; SNF2; SNF2L2; SNF2LA; Sth1p; SWI2"
                     /coded_by="NM_001289396.2:210..4982"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS34977.1"
                     /db_xref="GeneID:6595"
                     /db_xref="HGNC:HGNC:11098"
                     /db_xref="MIM:600014"
ORIGIN      
        1 mstptdpgam phpgpspgpg pspgpilgps pgpgpspgsv hsmmgpspgp psvshpmptm
       61 gstdfpqegm hqmhkpidgi hdkgivedih cgsmkgtgmr pphpgmgppq spmdqhsqgy
      121 msphpsplga pehvsspmsg ggptppqmpp sqpgalipgd pqamsqpnrg pspfspvqlh
      181 qlraqilayk mlargqplpe tlqlavqgkr tlpglqqqqq qqqqqqqqqq qqqqqqqqpq
      241 qqppqpqtqq qqqpalvnyn rpsgpgpels gpstpqklpv papggrpspa ppaaaqppaa
      301 avpgpsvpqp apgqpspvlq lqqkqsrisp iqkpqgldpv eilqereyrl qariahriqe
      361 lenlpgslpp dlrtkatvel kalrllnfqr qlrqevvacm rrdttletal nskaykrskr
      421 qtlrearmte klekqqkieq erkrrqkhqe ylnsilqhak dfkeyhrsva gkiqklskav
      481 atwhantere qkketeriek ermrrlmaed eegyrklidq kkdrrlayll qqtdeyvanl
      541 tnlvwehkqa qaakekkkrr rrkkkaeena eggesalgpd gepidessqm sdlpvkvtht
      601 etgkvlfgpe apkasqldaw lemnpgyeva prsdseesds dyeeedeeee ssrqeteeki
      661 lldpnseevs ekdakqiiet akqdvddeys mqysargsqs yytvahaise rvekqsalli
      721 ngtlkhyqlq glewmvslyn nnlngilade mglgktiqti alitylmehk rlngpyliiv
      781 plstlsnwty efdkwapsvv kisykgtpam rrslvpqlrs gkfnvlltty eyiikdkhil
      841 akirwkymiv deghrmknhh ckltqvlnth yvaprrillt gtplqnklpe lwallnfllp
      901 tifkscstfe qwfnapfamt gervdlneee tiliirrlhk vlrpfllrrl kkevesqlpe
      961 kveyvikcdm salqkilyrh mqakgilltd gsekdkkgkg gaktlmntim qlrkicnhpy
     1021 mfqhieesfa ehlgysngvi ngaelyrasg kfelldrilp klratnhrvl lfcqmtslmt
     1081 imedyfafrn flylrldgtt ksedraallk kfnepgsqyf ifllstragg lglnlqaadt
     1141 vvifdsdwnp hqdlqaqdra hrigqqnevr vlrlctvnsv eekilaaaky klnvdqkviq
     1201 agmfdqksss herraflqai leheeeneee devpddetln qmiarreeef dlfmrmdmdr
     1261 rredarnpkr kprlmeedel pswiikddae verltceeee ekifgrgsrq rrdvdysdal
     1321 tekqwlraie dgnleemeee vrlkkrkrrr nvdkdpaked vekakkrrgr ppaeklspnp
     1381 pkltkqmnai idtvinykdr cnvekvpsns qleiegnssg rqlsevfiql psrkelpeyy
     1441 elirkpvdfk kikerirnhk yrslgdlekd vmllchnaqt fnlegsqiye dsivlqsvfk
     1501 sarqkiakee esedesneee eeedeeeses eaksvkvkik lnkkddkgrd kgkgkkrpnr
     1561 gkakpvvsdf dsdeeqdere qsegsgtdde
//
LOCUS       NP_001397696             615 aa            linear   PRI 21-NOV-2025
DEFINITION  WD and tetratricopeptide repeats protein 1 isoform c [Homo
            sapiens].
ACCESSION   NP_001397696 XP_047305720
VERSION     NP_001397696.1
DBSOURCE    REFSEQ: accession NM_001410767.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Wang,X., Cai,Q., Ping,J., Diaz-Zabala,H., Xia,Y. and Guo,X.
  TITLE     The putative oncogenic role of WDTC1 in colorectal cancer
  JOURNAL   Carcinogenesis 43 (6), 594-600 (2022)
   PUBMED   35238908
  REMARK    GeneRIF: The putative oncogenic role of WDTC1 in colorectal cancer.
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 615)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 615)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 615)
  AUTHORS   Li,T., Robert,E.I., van Breugel,P.C., Strubin,M. and Zheng,N.
  TITLE     A promiscuous alpha-helical motif anchors viral hijackers and
            substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery
  JOURNAL   Nat Struct Mol Biol 17 (1), 105-111 (2010)
   PUBMED   19966799
REFERENCE   7  (residues 1 to 615)
  AUTHORS   Lai,C.Q., Parnell,L.D., Arnett,D.K., Garcia-Bailo,B., Tsai,M.Y.,
            Kabagambe,E.K., Straka,R.J., Province,M.A., An,P., Borecki,I.B.,
            Tucker,K.L. and Ordovas,J.M.
  TITLE     WDTC1, the ortholog of Drosophila adipose gene, associates with
            human obesity, modulated by MUFA intake
  JOURNAL   Obesity (Silver Spring) 17 (3), 593-600 (2009)
   PUBMED   19238144
  REMARK    GeneRIF: WDTC1 variation may be an important risk factor
            contributing to obesity in both Puerto Rican and white populations.
            GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   8  (residues 1 to 615)
  AUTHORS   Angers,S., Li,T., Yi,X., MacCoss,M.J., Moon,R.T. and Zheng,N.
  TITLE     Molecular architecture and assembly of the DDB1-CUL4A ubiquitin
            ligase machinery
  JOURNAL   Nature 443 (7111), 590-593 (2006)
   PUBMED   16964240
REFERENCE   9  (residues 1 to 615)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 615)
  AUTHORS   Hader,T., Muller,S., Aguilera,M., Eulenberg,K.G., Steuernagel,A.,
            Ciossek,T., Kuhnlein,R.P., Lemaire,L., Fritsch,R., Dohrmann,C.,
            Vetter,I.R., Jackle,H., Doane,W.W. and Bronner,G.
  TITLE     Control of triglyceride storage by a WD40/TPR-domain protein
  JOURNAL   EMBO Rep 4 (5), 511-516 (2003)
   PUBMED   12717455
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL590640.19 and FO393419.1.
            
            On Aug 16, 2022 this sequence version replaced XP_047305720.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1579306.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..615
                     /product="WD and tetratricopeptide repeats protein 1
                     isoform c"
                     /note="DDB1 and CUL4 associated factor 9; adipose homolog;
                     WD and tetratricopeptide repeats protein 1"
                     /calculated_mol_wt=68935
     Region          <39..215
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          45..84
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          51..88
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          88..129
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          93..131
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          132..172
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          138..178
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          182..222
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          236..271
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          265..305
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          362..395
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Site            order(366..367,370..371,373,397,400..401,404..405,
                     407..408,434,437..438,441..442,445)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          366..390
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <377..>457
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          395..428
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          397..432
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          433..457
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          487..509
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     CDS             1..615
                     /gene="WDTC1"
                     /gene_synonym="ADP; DCAF9"
                     /coded_by="NM_001410767.1:153..2000"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS90895.1"
                     /db_xref="GeneID:23038"
                     /db_xref="HGNC:HGNC:29175"
                     /db_xref="MIM:619763"
ORIGIN      
        1 makvnitrdl irrqikerga lsferryhvt dpfirrlgle aelqghsgcv nclewnekgd
       61 llasgsddqh tivwdplhhk kllsmhtght anifsvkflp hagdrilitg aadskvhvhd
      121 ltvketihmf gdhtnrvkri atapmwpntf wsaaedglir qydlrenskh sevlidltey
      181 cgqlveakcl tvnpqdnncl avgasgpfvr lydirmihnh rksmkqspsa gvhtfcdrqk
      241 plpdgaaqyy vaghlpvklp dynnrlrvlv atyvtfspng tellvnmgge qvylfdltyk
      301 qrpytfllpr kchssgevqn gkmstngvsn gvsnglhlhs ngfrlpesrg hvspqvelpp
      361 ylervkqqan eafacqqwtq aiqlyskavq raphnamlyg nraaaymkrk wdgdhydalr
      421 dclkaislnp chlkahfrla rclfelkyva ealeclddfk gkfpeqahss acdalgrdit
      481 aalfskndge ekkgpgggap vrlrstsrkd sisedemvlr ersydyqfry cghcntttdi
      541 keanffgrrp ptwsvcskgm splstacsht pataswppva sillcgsgtp dqrvktsqae
      601 swkiwrvlhr ptsga
//
LOCUS       NP_001392807            1042 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 6 [Homo sapiens].
ACCESSION   NP_001392807
VERSION     NP_001392807.1
DBSOURCE    REFSEQ: accession NM_001405878.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1042)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1042)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1042)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1042)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1042)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1042)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1042)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4310049.1,
                                           SRR18074967.1658314.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1042
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 6"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=113587
     Site            104
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          145..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          225..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          399..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          822..942
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..1042
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405878.1:391..3519"
                     /note="isoform 6 is encoded by transcript variant 19"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankgli
      481 vlgevpppeh ttdlflplss evktdhgtdk liesvsqple nhgapiighi seslstkscg
      541 alrpvngvin tlqpvladhi pgdssdaeeq lhkkqrlnlv ssssdgtcva artrpvlsck
      601 krrlvrpnsi vplskkvhrn stirpgcdvn pscalcgsgs intmppeihy eapllerlsq
      661 ldscvhpvla fpddvptslh fqsmlksqwq nkpfdkikpp kklslkhrap mpgslpdsar
      721 kdrhklvssf lttamlkhht dmssssylaa thhpphsplv rqlstssdsp apassssqvt
      781 astsqqpvrr rrgessfdin nivipmsvaa ttrveklqyk eiltpswrev dlqslkgspd
      841 eeneeiedls daafaalhak ceemerarwl wttsvppqrr gsrsyrssdg rttpqlgsan
      901 pstpqpaspd vssshslsey shgqsprspi spelhsaplt pvardtprhl asedtrcstp
      961 elgldeqsvq pwerrtfpla hspqaecedq ldaqeraarc trrtsgsktg reteaaptsp
     1021 pivplksrhl vaaataqrpt hr
//
LOCUS       NP_001428100             628 aa            linear   PRI 21-NOV-2025
DEFINITION  PHD finger protein 21A isoform g [Homo sapiens].
ACCESSION   NP_001428100 XP_047283065 XP_054225075
VERSION     NP_001428100.1
DBSOURCE    REFSEQ: accession NM_001441171.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Mustafa,S., Abbas,S., Mahmood,A., Khan,A.Z., Zeb,S., Khan,A. and
            Umair,M.
  TITLE     A novel de novo variant in the PHF21A causes craniofacial
            abnormalities, intellectual disability and skeletal manifestations
  JOURNAL   Clin Genet 104 (1), 142-144 (2023)
   PUBMED   36843358
  REMARK    GeneRIF: A novel de novo variant in the PHF21A causes craniofacial
            abnormalities, intellectual disability and skeletal manifestations.
REFERENCE   3  (residues 1 to 628)
  AUTHORS   Huang,J.Q., Ji,L.C., Jing,Q.A., He,Y.C., Ma,Y.Y. and Tong,X.M.
  TITLE     PHF21A expression as a biomarker of hepatocellular carcinoma
            progression and prognosis
  JOURNAL   Neoplasma 69 (6), 1349-1358 (2022)
   PUBMED   36305691
  REMARK    GeneRIF: PHF21A expression as a biomarker of hepatocellular
            carcinoma progression and prognosis.
REFERENCE   4  (residues 1 to 628)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 628)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 628)
  AUTHORS   Hailesellasse Sene,K., Porter,C.J., Palidwor,G., Perez-Iratxeta,C.,
            Muro,E.M., Campbell,P.A., Rudnicki,M.A. and Andrade-Navarro,M.A.
  TITLE     Gene function in early mouse embryonic stem cell differentiation
  JOURNAL   BMC Genomics 8, 85 (2007)
   PUBMED   17394647
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 628)
  AUTHORS   Shi,Y.J., Matson,C., Lan,F., Iwase,S., Baba,T. and Shi,Y.
  TITLE     Regulation of LSD1 histone demethylase activity by its associated
            factors
  JOURNAL   Mol Cell 19 (6), 857-864 (2005)
   PUBMED   16140033
REFERENCE   8  (residues 1 to 628)
  AUTHORS   Iwase,S., Januma,A., Miyamoto,K., Shono,N., Honda,A., Yanagisawa,J.
            and Baba,T.
  TITLE     Characterization of BHC80 in BRAF-HDAC complex, involved in
            neuron-specific gene repression
  JOURNAL   Biochem Biophys Res Commun 322 (2), 601-608 (2004)
   PUBMED   15325272
  REMARK    GeneRIF: Presumably serves as a scaffold protein in BHC in neuronal
            as well as non-neuronal cells. Possible role in spermatogenesis.
REFERENCE   9  (residues 1 to 628)
  AUTHORS   Hakimi,M.A., Dong,Y., Lane,W.S., Speicher,D.W. and Shiekhattar,R.
  TITLE     A candidate X-linked mental retardation gene is a component of a
            new family of histone deacetylase-containing complexes
  JOURNAL   J Biol Chem 278 (9), 7234-7239 (2003)
   PUBMED   12493763
REFERENCE   10 (residues 1 to 628)
  AUTHORS   Hakimi,M.A., Bochar,D.A., Chenoweth,J., Lane,W.S., Mandel,G. and
            Shiekhattar,R.
  TITLE     A core-BRAF35 complex containing histone deacetylase mediates
            repression of neuronal-specific genes
  JOURNAL   Proc Natl Acad Sci U S A 99 (11), 7420-7425 (2002)
   PUBMED   12032298
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC024475.15 and AC068385.9.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_047283065.1, XP_054225075.1.
            
            Summary: The PHF21A gene encodes BHC80, a component of a BRAF35
            (MIM 605535)/histone deacetylase (HDAC; see MIM 601241) complex
            (BHC) that mediates repression of neuron-specific genes through the
            cis-regulatory element known as repressor element-1 (RE1) or neural
            restrictive silencer (NRS) (Hakimi et al., 2002 [PubMed
            12032298]).[supplied by OMIM, Nov 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038193.3363772.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..628
                     /product="PHD finger protein 21A isoform g"
                     /note="BRAF35/HDAC2 complex (80 kDa); BHC80a; BRAF35-HDAC
                     complex protein BHC80"
                     /calculated_mol_wt=68784
     CDS             1..628
                     /gene="PHF21A"
                     /gene_synonym="BHC80; BM-006; IDDBCS; NEDMS"
                     /coded_by="NM_001441171.1:645..2531"
                     /note="isoform g is encoded by transcript variant 17"
                     /db_xref="GeneID:51317"
                     /db_xref="HGNC:HGNC:24156"
                     /db_xref="MIM:608325"
ORIGIN      
        1 melqtlqeal kveiqvhqkl vaqmkqdpqn adlkkqlhel qakitalsek qkrvveqlrk
       61 nlivkqeqpd kfqiqplpqs enklqtaqqq plqqlqqqqq yhhhhaqqsa aaspnltasq
      121 ktvttasmit tktlplvlka atatmpasvv gqrptiamvt ainsqkavls tdvqntpvnl
      181 qtsskvtgpg aeavqivakn tvtlvqatpp qpikvpqfip pprltprpnf lpqvrpkpva
      241 qnnipiapap ppmlaapqli qrpvmltkft pttlptsqns ihpvrvvngq tatiaktfpm
      301 aqltsiviat pgtrlagpqt vqlskpslek qtvkshtetd ekqtesrtit ppaapkpkre
      361 enpqklafmv slglvthdhl eeiqskrqer krrttanpvy sgavfeperk ksavtylnst
      421 mhpgtrkrgr ppkynavlgf galtptspqs shpdspenek tettftfpap vqpvslpspt
      481 stdmlkkeea ipwpgtlaiv hsyiaykaak eeekqkllkw ssdlkqereq leqkvkqlsn
      541 siskcmemkn tilarqkemh sslekvkqli rlihgidlsk pvdseatvga isngpdctpp
      601 anaatstpap spssqsctan cnqgeetk
//
LOCUS       NP_001397640             675 aa            linear   PRI 21-NOV-2025
DEFINITION  interleukin-17 receptor C isoform 10 precursor [Homo sapiens].
ACCESSION   NP_001397640 XP_047305032
VERSION     NP_001397640.1
DBSOURCE    REFSEQ: accession NM_001410711.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 675)
  AUTHORS   Arikan,S., Ozturk,O., Duygulu,S., Atalay,E.O. and Atalay,A.
  TITLE     Associations of IL-17 and IL-17 receptor polymorphisms with
            Behcet's disease in Denizli Province of Turkey
  JOURNAL   Immunol Res 71 (4), 600-608 (2023)
   PUBMED   36701075
  REMARK    GeneRIF: Associations of IL-17 and IL-17 receptor polymorphisms
            with Behcet's disease in Denizli Province of Turkey.
REFERENCE   2  (residues 1 to 675)
  AUTHORS   Kang,J.H., Park,S., Rho,J., Hong,E.J., Cho,Y.E., Won,Y.S. and
            Kwon,H.J.
  TITLE     IL-17A promotes Helicobacter pylori-induced gastric carcinogenesis
            via interactions with IL-17RC
  JOURNAL   Gastric Cancer 26 (1), 82-94 (2023)
   PUBMED   36125689
  REMARK    GeneRIF: IL-17A promotes Helicobacter pylori-induced gastric
            carcinogenesis via interactions with IL-17RC.
REFERENCE   3  (residues 1 to 675)
  AUTHORS   Goepfert,A., Barske,C., Lehmann,S., Wirth,E., Willemsen,J.,
            Gudjonsson,J.E., Ward,N.L., Sarkar,M.K., Hemmig,R., Kolbinger,F.
            and Rondeau,J.M.
  TITLE     IL-17-induced dimerization of IL-17RA drives the formation of the
            IL-17 signalosome to potentiate signaling
  JOURNAL   Cell Rep 41 (3), 111489 (2022)
   PUBMED   36260993
REFERENCE   4  (residues 1 to 675)
  AUTHORS   Huang,X., Li,Z., Shen,X., Nie,N. and Shen,Y.
  TITLE     IL-17 upregulates MCP-1 expression via Act1 / TRAF6 / TAK1 in
            experimental autoimmune myocarditis
  JOURNAL   Cytokine 152, 155823 (2022)
   PUBMED   35183823
  REMARK    Erratum:[Cytokine. 2022 Jun;154:155879. doi:
            10.1016/j.cyto.2022.155879. PMID: 35413623]
REFERENCE   5  (residues 1 to 675)
  AUTHORS   Schmidt,T., Luebbe,J., Kilian,C., Riedel,J.H., Hiekmann,S.,
            Asada,N., Ginsberg,P., Robben,L., Song,N., Kaffke,A., Peters,A.,
            Borchers,A., Flavell,R.A., Gagliani,N., Pelzcar,P., Huber,S.,
            Huber,T.B., Turner,J.E., Paust,H.J., Krebs,C.F. and Panzer,U.
  TITLE     IL-17 Receptor C Signaling Controls CD4+ TH17 Immune Responses and
            Tissue Injury in Immune-Mediated Kidney Diseases
  JOURNAL   J Am Soc Nephrol 32 (12), 3081-3098 (2021)
   PUBMED   35167487
  REMARK    GeneRIF: IL-17 Receptor C Signaling Controls CD4(+) TH17 Immune
            Responses and Tissue Injury in Immune-Mediated Kidney Diseases.
REFERENCE   6  (residues 1 to 675)
  AUTHORS   Haudenschild,D.R., Curtiss,S.B., Moseley,T.A. and Reddi,A.H.
  TITLE     Generation of interleukin-17 receptor-like protein (IL-17RL) in
            prostate by alternative splicing of RNA
  JOURNAL   Prostate 66 (12), 1268-1274 (2006)
   PUBMED   16688746
  REMARK    GeneRIF: IL-17RL exists as multiple isoforms due to extensive
            alternative splicing. Changes in RNA IL-17RL splicing occur in
            advanced cancers.
REFERENCE   7  (residues 1 to 675)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   8  (residues 1 to 675)
  AUTHORS   Gerritsen,M.E., Tomlinson,J.E., Zlot,C., Ziman,M. and Hwang,S.
  TITLE     Using gene expression profiling to identify the molecular basis of
            the synergistic actions of hepatocyte growth factor and vascular
            endothelial growth factor in human endothelial cells
  JOURNAL   Br J Pharmacol 140 (4), 595-610 (2003)
   PUBMED   14504135
  REMARK    Review article
REFERENCE   9  (residues 1 to 675)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 675)
  AUTHORS   Haudenschild,D., Moseley,T., Rose,L. and Reddi,A.H.
  TITLE     Soluble and transmembrane isoforms of novel interleukin-17
            receptor-like protein by RNA splicing and expression in prostate
            cancer
  JOURNAL   J Biol Chem 277 (6), 4309-4316 (2002)
   PUBMED   11706037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018809.5.
            
            On Aug 15, 2022 this sequence version replaced XP_047305032.1.
            
            Summary: This gene encodes a single-pass type I membrane protein
            that shares similarity with the interleukin-17 receptor (IL-17RA).
            Unlike IL-17RA, which is predominantly expressed in hemopoietic
            cells, and binds with high affinity to only IL-17A, this protein is
            expressed in nonhemopoietic tissues, and binds both IL-17A and
            IL-17F with similar affinities. The proinflammatory cytokines,
            IL-17A and IL-17F, have been implicated in the progression of
            inflammatory and autoimmune diseases. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            detected for this gene, and it has been proposed that soluble,
            secreted proteins lacking transmembrane and intracellular domains
            may function as extracellular antagonists to cytokine signaling.
            [provided by RefSeq, Feb 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3352282.1,
                                           SRR14038193.3007768.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..675
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3"
     Protein         1..675
                     /product="interleukin-17 receptor C isoform 10 precursor"
                     /note="IL17F receptor; IL-17RL; IL17Rhom; zcytoR14; IL-17
                     receptor C; interleukin-17 receptor homolog;
                     interleukin-17 receptor-like protein"
                     /calculated_mol_wt=71351
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2183
     Region          71..427
                     /region_name="IL17_R_N"
                     /note="Interleukin-17 receptor extracellular region;
                     pfam15037"
                     /db_xref="CDD:464460"
     Region          474..621
                     /region_name="SEFIR"
                     /note="SEFIR domain; pfam08357"
                     /db_xref="CDD:254756"
     CDS             1..675
                     /gene="IL17RC"
                     /gene_synonym="CANDF9; IL17-RL; IL17RL"
                     /coded_by="NM_001410711.1:219..2246"
                     /note="isoform 10 precursor is encoded by transcript
                     variant 11"
                     /db_xref="CCDS:CCDS93203.1"
                     /db_xref="GeneID:84818"
                     /db_xref="HGNC:HGNC:18358"
                     /db_xref="MIM:610925"
ORIGIN      
        1 mpvpwfllsl algrspvvls lerlvgpqda thcspglscr lwdsdilclp gdivpapgpv
       61 lapthlqtel vlrcqketdc dlclrvavhl avhghweepe deekfggaad sgveeprnas
      121 lqaqvvlsfq ayptarcvll evqvpaalvq fgqsvgsvvy dcfeaalgse vriwsytqpr
      181 yekelnhtqq lpalpwlnvs adgdnvhlvl nvseeqhfgl slywnqvqgp pkprwhknlt
      241 gpqiitlnht dlvpclciqv wplepdsvrt nicpfredpr ahqnlwqaar lqlltlqswl
      301 ldapcslpae aalcwrapgg dpcqplvppl swenvtvdvn sseklqlqec lwadslgplk
      361 ddvllletrg pqdnrslcal epsgctslps kastraarlg eyllqdlqsg qclqlwdddl
      421 galwacpmdk yihkrwalvw lacllfaaal slilllkkdh akaaargraa lllysaddsg
      481 ferlvgalas alcqlplrva vdlwsrrels aqgpvawfha qrrqtlqegg vvvllfspga
      541 valcsewlqd gvsgpgahgp hdafraslsc vlpdflqgra pgsyvgacfd rllhpdavpa
      601 lfrtvpvftl psqlpdflga lqqpraprsg rlqeraeqvs ralqpaldsy fhppgtpapg
      661 rgvgpgagpg agdgt
//
LOCUS       NP_001394270             275 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 39 [Homo sapiens].
ACCESSION   NP_001394270
VERSION     NP_001394270.1
DBSOURCE    REFSEQ: accession NM_001407341.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4178994.1,
                                           SRR14038192.2148470.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..275
                     /product="tropomyosin alpha-1 chain isoform 39"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=31483
     Region          12..226
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..275
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407341.1:88..915"
                     /note="isoform 39 is encoded by transcript variant 39"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 magsssleav rrkirslqeq adaaeeragt lqreldherk lretaeadva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkviesraqk deekmeiqei qlkeakhiae
      121 dadrkyeeva rklviiesdl eraeeraels egkcaeleee lktvtnnlks leaqaekysq
      181 kedryeeeik vlsdklkeae traefaersv tkleksiddl egkilssvfs lilmveyqpg
      241 ktifqfkgih idtllctctf flcvlwgfsl wllns
//
LOCUS       NP_001412007             417 aa            linear   PRI 21-NOV-2025
DEFINITION  coatomer subunit delta isoform 8 [Homo sapiens].
ACCESSION   NP_001412007 XP_005271599 XP_054224671
VERSION     NP_001412007.1
DBSOURCE    REFSEQ: accession NM_001425078.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   O'Donoghue,L., Comer,S.P., Hiebner,D.W., Schoen,I., von
            Kriegsheim,A. and Smolenski,A.
  TITLE     RhoGAP6 interacts with COPI to regulate protein transport
  JOURNAL   Biochem J 480 (14), 1109-1127 (2023)
   PUBMED   37409526
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Li,W., Liang,J., Outeda,P., Turner,S., Wakimoto,B.T. and Watnick,T.
  TITLE     A genetic screen in Drosophila reveals an unexpected role for the
            KIP1 ubiquitination-promoting complex in male fertility
  JOURNAL   PLoS Genet 16 (12), e1009217 (2020)
   PUBMED   33378371
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Tidwell,T., Deshotel,M., Palumbos,J., Miller,C., Bayrak-Toydemir,P.
            and Carey,J.C.
  TITLE     Novel de novo ARCN1 intronic variant causes rhizomelic short
            stature with microretrognathia and developmental delay
  JOURNAL   Cold Spring Harb Mol Case Stud 6 (6), a005728 (2020)
   PUBMED   33154040
  REMARK    GeneRIF: Novel de novo ARCN1 intronic variant causes rhizomelic
            short stature with microretrognathia and developmental delay.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Schekman,R. and Orci,L.
  TITLE     Coat proteins and vesicle budding
  JOURNAL   Science 271 (5255), 1526-1533 (1996)
   PUBMED   8599108
  REMARK    Review article
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Cukierman,E., Huber,I., Rotman,M. and Cassel,D.
  TITLE     The ARF1 GTPase-activating protein: zinc finger motif and Golgi
            complex localization
  JOURNAL   Science 270 (5244), 1999-2002 (1995)
   PUBMED   8533093
REFERENCE   8  (residues 1 to 417)
  AUTHORS   Radice,P., Pensotti,V., Jones,C., Perry,H., Pierotti,M.A. and
            Tunnacliffe,A.
  TITLE     The human archain gene, ARCN1, has highly conserved homologs in
            rice and Drosophila
  JOURNAL   Genomics 26 (1), 101-106 (1995)
   PUBMED   7782067
REFERENCE   9  (residues 1 to 417)
  AUTHORS   Orcl,L., Palmer,D.J., Amherdt,M. and Rothman,J.E.
  TITLE     Coated vesicle assembly in the Golgi requires only coatomer and ARF
            proteins from the cytosol
  JOURNAL   Nature 364 (6439), 732-734 (1993)
   PUBMED   8355790
REFERENCE   10 (residues 1 to 417)
  AUTHORS   Waters,M.G., Serafini,T. and Rothman,J.E.
  TITLE     'Coatomer': a cytosolic protein complex containing subunits of
            non-clathrin-coated Golgi transport vesicles
  JOURNAL   Nature 349 (6306), 248-251 (1991)
   PUBMED   1898986
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000941.6.
            
            On or before Oct 25, 2023 this sequence version replaced
            XP_005271599.1, XP_054224671.1.
            
            Summary: This gene maps in a region, which include the mixed
            lineage leukemia and Friend leukemia virus integration 1 genes,
            where multiple disease-associated chromosome translocations occur.
            It is an intracellular protein. Archain sequences are well
            conserved among eukaryotes and this protein may play a fundamental
            role in eukaryotic cell biology. It has similarities to heat shock
            proteins and clathrin-associated proteins, and may be involved in
            vesicle structure or trafficking. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853561.5910.1,
                                           SRR11853567.6244.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..417
                     /product="coatomer subunit delta isoform 8"
                     /note="coatomer protein delta-COP; coatomer protein
                     complex, subunit delta; archain vesicle transport protein
                     1; coatomer delta subunit; delta-coat protein; COPI coat
                     complex subunit delta"
                     /calculated_mol_wt=46636
     Region          4..133
                     /region_name="Delta_COP_N"
                     /note="delta subunit of the F-COPI complex, N-terminal
                     domain; cd14830"
                     /db_xref="CDD:341434"
     Region          168..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48444.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q5XJY5; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Region          272..>414
                     /region_name="AP_delta-COPI_MHD"
                     /note="Mu homology domain (MHD) of adaptor protein (AP)
                     coat protein I (COPI) delta subunit; cd09254"
                     /db_xref="CDD:271162"
     Site            309
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            351
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q5XJY5; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     CDS             1..417
                     /gene="ARCN1"
                     /gene_synonym="COPD; SRMMD; SSMG"
                     /coded_by="NM_001425078.1:140..1393"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:372"
                     /db_xref="HGNC:HGNC:649"
                     /db_xref="MIM:600820"
ORIGIN      
        1 mvllaaavct kagkaivsrq fvemtrtrie gllaafpklm ntgkqhtfve tesvryvyqp
       61 meklymvlit tknsniledl etlrlfsrvi peycraleen eisehcfdli fafdeivalg
      121 yrenvnlaqi rtftemdshe ekvfravret qereakaemr rkakelqqar rdaerqgkka
      181 pgfggfgssa vsggstaami tetiietdkp kvapaparps gpskalklga kgkevdnfvd
      241 klksegetim sssmgkrtse atkmhappin mesvhmkiee kitltcgrdg glqnmelhgm
      301 imlrisddky grirlhvene dkkgvqlqth pnvdkklfta esliglknpe ksfpvnsdvg
      361 vlkwrlqtte esfipltinc wpsesgngcd vnieyelqed nlelndvvit iplplpk
//
LOCUS       NP_001393553            1029 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 12 [Homo sapiens].
ACCESSION   NP_001393553
VERSION     NP_001393553.1
DBSOURCE    REFSEQ: accession NM_001406624.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1029)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1029)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1029)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1029)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1029)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1029)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1029)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2221598.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1029
                     /product="hamartin isoform 12"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=114578
     Region          16..598
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <584..>821
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1029
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406624.1:673..3762"
                     /note="isoform 12 is encoded by transcript variant 38"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mdtdvvvltt gvlvlitmlp mipqsgkqhl ldffdifgrl sswclkkpgh vaevylvhlh
       61 asvyalfhrl ygmypcnfvs flrshysmke nletfeevvk pmmehvrihp elvtgskdhe
      121 ldprrwkrle thdvviecak isldpteasy edgysvshqi sarfphrsad vttspyadtq
      181 nsygcatstp ystsrlmlln mpgqlpqtls spstrlitep pqatlwspsm vcgmttppts
      241 pgnvppdlsh pyskvfgtta ggkgtplgtp atspppaplc hsddyvhisl pqatvtpprk
      301 eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed siekdkeeaa
      361 isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv npeplhssld
      421 klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp trvgfgsgqp
      481 ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr liqqgadahs
      541 kelnklplps ksvdwthfgg sppsdeirtl rdqllllhnq llyerfkrqq halrnrrllr
      601 kvikaaalee hnaamkdqlk lqekdiqmwk vslqkeqary nqlqeqrdtm vtklhsqirq
      661 lqhdreefyn qsqelqtkle dcrnmiaelr ielkkannkl snsesvqqqm eflnrqllvl
      721 gevnelyleq lqnkhsdttk evemmkaayr keleknrshv lqqtqrldts qkrilelesh
      781 lakkdhllle qkkyledvkl qargqlqaae sryeaqkrit qvfeleildl ygrlekdgll
      841 kkleeekaea aeaaeerldc cndgcsdsmv ghneeasghn getktprpss argssgsrgg
      901 ggssssssel stpekpphqr agpfssrwet tmgeasasip ttvgslpssk sflgmkarel
      961 frnksesqcd edgmtsslse slktelgkdl gveakiplnl dgphpspptp dsvgqlhimd
     1021 ynethhehs
//
LOCUS       NP_001428164            1620 aa            linear   PRI 21-NOV-2025
DEFINITION  THO complex subunit 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001428164 XP_047298226 XP_054183399
VERSION     NP_001428164.1
DBSOURCE    REFSEQ: accession NM_001441235.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1620)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1620)
  AUTHORS   Zhou,X., Liu,X., Zhang,G., Zhang,Q., Chen,H., Wang,Y., Fang,F. and
            Sun,J.
  TITLE     Knockdown THOC2 suppresses the proliferation and invasion of
            melanoma
  JOURNAL   Bioengineered 10 (1), 635-645 (2019)
   PUBMED   31680623
  REMARK    GeneRIF: THOC2 reduction repressed melanoma cell proliferation and
            invasion, and induced cell apoptosis.
REFERENCE   3  (residues 1 to 1620)
  AUTHORS   Kumar,R., Gardner,A., Homan,C.C., Douglas,E., Mefford,H.,
            Wieczorek,D., Ludecke,H.J., Stark,Z., Sadedin,S., Nowak,C.B.,
            Douglas,J., Parsons,G., Mark,P., Loidi,L., Herman,G.E., Mihalic
            Mosher,T., Gillespie,M.K., Brady,L., Tarnopolsky,M., Madrigal,I.,
            Eiris,J., Domenech Salgado,L., Rabionet,R., Strom,T.M.,
            Ishihara,N., Inagaki,H., Kurahashi,H., Dudding-Byth,T.,
            Palmer,E.E., Field,M. and Gecz,J.
  CONSRTM   Broad CMG
  TITLE     Severe neurocognitive and growth disorders due to variation in
            THOC2, an essential component of nuclear mRNA export machinery
  JOURNAL   Hum Mutat 39 (8), 1126-1138 (2018)
   PUBMED   29851191
  REMARK    GeneRIF: Study presents detailed clinical assessment and functional
            studies on a de novo variant in a female with an epileptic
            encephalopathy and discuss an additional four families with rare
            variants in THOC2 with supportive evidence for pathogenicity.
REFERENCE   4  (residues 1 to 1620)
  AUTHORS   Kumar,R., Corbett,M.A., van Bon,B.W., Woenig,J.A., Weir,L.,
            Douglas,E., Friend,K.L., Gardner,A., Shaw,M., Jolly,L.A., Tan,C.,
            Hunter,M.F., Hackett,A., Field,M., Palmer,E.E., Leffler,M.,
            Rogers,C., Boyle,J., Bienek,M., Jensen,C., Van Buggenhout,G., Van
            Esch,H., Hoffmann,K., Raynaud,M., Zhao,H., Reed,R., Hu,H.,
            Haas,S.A., Haan,E., Kalscheuer,V.M. and Gecz,J.
  TITLE     THOC2 Mutations Implicate mRNA-Export Pathway in X-Linked
            Intellectual Disability
  JOURNAL   Am J Hum Genet 97 (2), 302-310 (2015)
   PUBMED   26166480
  REMARK    GeneRIF: THOC2 mutations implicate mRNA-export pathway in X-linked
            intellectual disability.
REFERENCE   5  (residues 1 to 1620)
  AUTHORS   Grolimund,L., Aeby,E., Hamelin,R., Armand,F., Chiappe,D.,
            Moniatte,M. and Lingner,J.
  TITLE     A quantitative telomeric chromatin isolation protocol identifies
            different telomeric states
  JOURNAL   Nat Commun 4, 2848 (2013)
   PUBMED   24270157
REFERENCE   6  (residues 1 to 1620)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   7  (residues 1 to 1620)
  AUTHORS   Strasser,K., Masuda,S., Mason,P., Pfannstiel,J., Oppizzi,M.,
            Rodriguez-Navarro,S., Rondon,A.G., Aguilera,A., Struhl,K., Reed,R.
            and Hurt,E.
  TITLE     TREX is a conserved complex coupling transcription with messenger
            RNA export
  JOURNAL   Nature 417 (6886), 304-308 (2002)
   PUBMED   11979277
REFERENCE   8  (residues 1 to 1620)
  AUTHORS   Coffey,A.J., Brooksbank,R.A., Brandau,O., Oohashi,T., Howell,G.R.,
            Bye,J.M., Cahn,A.P., Durham,J., Heath,P., Wray,P., Pavitt,R.,
            Wilkinson,J., Leversha,M., Huckle,E., Shaw-Smith,C.J., Dunham,A.,
            Rhodes,S., Schuster,V., Porta,G., Yin,L., Serafini,P., Sylla,B.,
            Zollo,M., Franco,B., Bolino,A., Seri,M., Lanyi,A., Davis,J.R.,
            Webster,D., Harris,A., Lenoir,G., de St Basile,G., Jones,A.,
            Behloradsky,B.H., Achatz,H., Murken,J., Fassler,R., Sumegi,J.,
            Romeo,G., Vaudin,M., Ross,M.T., Meindl,A. and Bentley,D.R.
  TITLE     Host response to EBV infection in X-linked lymphoproliferative
            disease results from mutations in an SH2-domain encoding gene
  JOURNAL   Nat Genet 20 (2), 129-135 (1998)
   PUBMED   9771704
REFERENCE   9  (residues 1 to 1620)
  AUTHORS   Gu,X.X., Decorte,R., Marynen,P., Fryns,J.P., Cassiman,J.J. and
            Raeymaekers,P.
  TITLE     Localisation of a new gene for non-specific mental retardation to
            Xq22-q26 (MRX35)
  JOURNAL   J Med Genet 33 (1), 52-55 (1996)
   PUBMED   8825049
REFERENCE   10 (residues 1 to 1620)
  AUTHORS   Mulley,J.C., Kerr,B., Stevenson,R. and Lubs,H.
  TITLE     Nomenclature guidelines for X-linked mental retardation
  JOURNAL   Am J Med Genet 43 (1-2), 383-391 (1992)
   PUBMED   1605216
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL023575.1, Z82901.1 and
            AL030996.1.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_047298226.1, XP_054183399.1.
            
            Summary: The TREX multiprotein complex binds specifically to
            spliced mRNAs to facilitate mRNA export. The protein encoded by
            this gene is a member of the THO complex, a subset of the TREX
            complex. The encoded protein interacts with the THOC1
            protein.[provided by RefSeq, Jun 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.298303.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1620
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..1620
                     /product="THO complex subunit 2 isoform 2"
                     /note="THO complex 2"
                     /calculated_mol_wt=185508
     Region          1..163
                     /region_name="Anchor domain, interaction with THOC5 and
                     THOC7. /evidence=ECO:0000269|PubMed:33191911,
                     ECO:0007744|PDB:7APK"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          11..566
                     /region_name="THOC2_N"
                     /note="THO complex subunit 2 N-terminus; pfam16134"
                     /db_xref="CDD:465032"
     Region          164..534
                     /region_name="Bow domain, interaction with THOC1 dock
                     domain and THOC3. /evidence=ECO:0000269|PubMed:33191911,
                     ECO:0007744|PDB:7APK"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          322..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          535..686
                     /region_name="MIF4G domain, interaction with THOC3 and
                     DDX39B. /evidence=ECO:0000269|PubMed:33191911,
                     ECO:0007744|PDB:7APK"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          568..642
                     /region_name="Thoc2"
                     /note="Transcription- and export-related complex subunit;
                     pfam11732"
                     /db_xref="CDD:463334"
     Region          687..1174
                     /region_name="Stern domain.
                     /evidence=ECO:0000269|PubMed:33191911"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          874..1173
                     /region_name="Tho2"
                     /note="Transcription factor/nuclear export subunit protein
                     2; pfam11262"
                     /db_xref="CDD:463251"
     Region          923..928
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B1AZI6; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1385
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1470
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          1475..>1583
                     /region_name="U2AF_lg"
                     /note="U2 snRNP auxilliary factor, large subunit, splicing
                     factor; TIGR01642"
                     /db_xref="CDD:273727"
     Site            1477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1513
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     CDS             1..1620
                     /gene="THOC2"
                     /gene_synonym="AMC7; CXorf3; dJ506G2.1; hTREX120; MRX12;
                     MRX35; THO2; XLID12"
                     /coded_by="NM_001441235.1:31..4893"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:57187"
                     /db_xref="HGNC:HGNC:19073"
                     /db_xref="MIM:300395"
ORIGIN      
        1 maaaavvvpa ewiknweksg rgeflhlcri lsenkshdss tyrdfqqaly elsyhvikgn
       61 lkheqasnvl sdisefredm psiladvfci ldietnclee kskrdyftql vlaclylvsd
      121 tvlkerldpe tleslglikq sqqfnqksvk iktklfykqq kfnllreene gyakliaelg
      181 qdlsgsitsd lileniksli gcfnldpnrv ldvilevfec rpehddffis llesymsmce
      241 pqtlchilgf kfkfyqepng etpsslyrva avllqfnlid lddlyvhllp adncimdehk
      301 reiaeakqiv rkltmvvlss ekmderekek ekeeekvekp pdnqklglle allkigdwqh
      361 aqnimdqmpp yyaashklia laicklihit ieplyrrvgv pkgakgspvn alqnkrapkq
      421 aesfedlrrd vfnmfcylgp hlshdpilfa kvvrigksfm kefqsdgskq edkektevil
      481 scllsitdqv llpslslmdc nacmseelwg mfktfpyqhr yrlygqwkne tynshpllvk
      541 vkaqtidrak yimkrltken vkpsgrqigk lshsnptilf dyilsqiqky dnlitpvvds
      601 lkyltslnyd vlayciieal anpekermkh ddttisswlq slasfcgavf rkypidlagl
      661 lqyvanqlka gksfdllilk evvqkmagie iteemtmeql eamtggeqlk aeggyfgqir
      721 ntkkssqrlk dalldhdlal plcllmaqqr ngvifqegge khlklvgkly dqchdtlvqf
      781 ggflasnlst edyikrvpsi dvlcnefhtp hdaafflsrp myahhissky delkksekgs
      841 kqqhkvhkyi tscemvmapv heavvslhvs kvwddispqf yatfwsltmy dlavphtsye
      901 revnklkvqm kaiddnqemp pnkkkkeker ctalqdklle eekkqmehvq rvlqrlklek
      961 dnwllakstk netitkflql cifprcifsa idavycarfv elvhqqktpn fstllcydrv
     1021 fsdiiytvas cteneasryg rflccmletv trwhsdraty ekecgnypgf ltilratgfd
     1081 ggnkadqldy enfrhvvhkw hykltkasvh cletgeythi rnilivltki lpwypkvlnl
     1141 gqalerrvhk icqeekekrp dlyalamgys gqlksrksym ipenefhhkd ppprnavasv
     1201 qngpgggpss ssigsasksd essteetdks rersqcgvka vnkassttpk gnssngnsgs
     1261 nsnkavkend kekgkekeke kkektpattp earvlgkdgk ekpkeerpnk dekaretker
     1321 tpksdkekek fkkeekakde kfkttvpnae skstqerere kepsrerdia kemkskenvk
     1381 ggektpvsgs lkspvprsdi pepereqkrr kidthpspsh sstvkvtail pkvplgseny
     1441 asspvisihf lqdslielke ssaklyinht ppplsksker emdkkdldks rersrerekk
     1501 dekdrkerkr dhsnndrevp pdltkrrkee ngtmgvskhk sespcespyp nekdkeknks
     1561 kssgkekgsd sfksekmdki ssggkkesrh dkekiekkek rdssggkeek khhkssdkhr
//
LOCUS       NP_001401617             510 aa            linear   PRI 21-NOV-2025
DEFINITION  nucleolar complex protein 4 homolog isoform 2 [Homo sapiens].
ACCESSION   NP_001401617
VERSION     NP_001401617.1
DBSOURCE    REFSEQ: accession NM_001414688.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Talebi,A., Shahidsales,S., Aliakbarian,M., Pezeshki Rad,M. and
            Kerachian,M.A.
  TITLE     Oncogenic fusion transcript analysis identified ADAP1-NOC4L,
            potentially associated with metastatic colorectal cancer
  JOURNAL   Cancer Med 12 (1), 525-540 (2023)
   PUBMED   35702822
  REMARK    GeneRIF: Oncogenic fusion transcript analysis identified
            ADAP1-NOC4L, potentially associated with metastatic colorectal
            cancer.
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Qin,Y., Li,H., Jia,L., Yan,J., Gao,G.F. and Li,X.
  TITLE     Targeted disruption of Noc4l leads to preimplantation embryonic
            lethality in mice
  JOURNAL   Protein Cell 8 (3), 230-235 (2017)
   PUBMED   28012024
  REMARK    GeneRIF: The results provide the first in vivo genetic evidence
            that Noc4l plays important roles in early embryogenesis in mice.
REFERENCE   5  (residues 1 to 510)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 510)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 510)
  AUTHORS   Bernstein,K.A., Gallagher,J.E., Mitchell,B.M., Granneman,S. and
            Baserga,S.J.
  TITLE     The small-subunit processome is a ribosome assembly intermediate
  JOURNAL   Eukaryot Cell 3 (6), 1619-1626 (2004)
   PUBMED   15590835
REFERENCE   8  (residues 1 to 510)
  AUTHORS   Milkereit,P., Strauss,D., Bassler,J., Gadal,O., Kuhn,H., Schutz,S.,
            Gas,N., Lechner,J., Hurt,E. and Tschochner,H.
  TITLE     A Noc complex specifically involved in the formation and nuclear
            export of ribosomal 40 S subunits
  JOURNAL   J Biol Chem 278 (6), 4072-4081 (2003)
   PUBMED   12446671
REFERENCE   9  (residues 1 to 510)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC138466.12.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1965299, SAMEA1966682
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.33"
     Protein         1..510
                     /product="nucleolar complex protein 4 homolog isoform 2"
                     /note="nucleolar complex protein 4 homolog; NOC4-like
                     protein; NOC4 protein homolog; nucleolar
                     complex-associated protein 4-like protein"
                     /calculated_mol_wt=57554
     Site            291..311
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVI4.1)"
     Region          304..446
                     /region_name="CBF"
                     /note="CBF/Mak21 family; pfam03914"
                     /db_xref="CDD:461090"
     Site            341..361
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVI4.1)"
     Site            369..389
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVI4.1)"
     CDS             1..510
                     /gene="NOC4L"
                     /gene_synonym="NET49; NOC4; UTP19"
                     /coded_by="NM_001414688.1:33..1565"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:79050"
                     /db_xref="HGNC:HGNC:28461"
                     /db_xref="MIM:612819"
ORIGIN      
        1 merepgaagv rralgrrlea vlasrseana vfdilavlqs edqeeiqeav rtcsrlfgal
       61 lergelfvgq lpseemvmtg sqgatrkykv wmrhryhscc nrlgellghp sfqvkelals
      121 allkfvqleg ahplekskwe gnylfprelf klvvggllsp eedqslllsq freyldyddt
      181 ryhtmqaavd avarvtgqhp evppafwnna ftllsavslp rreptvssfy vkravwtplq
      241 ehrrvfqamw lsflkhklpl slykkvlliv hdailpqlaq ptlmidfltr acdlggalsl
      301 lalnglfili hkhnleypdf yrklyglldp svfhvkyrar ffhladlfls sshlpaylva
      361 afakrlarla ltappeallm vlpficnllr rhpacrvlvh rphgpeldad pydpgeedpa
      421 qsralesslw elqalqrhyh pevskaasvi nqalsmpevs iaplleltay eiferdlkkk
      481 gpepvplefi paqgllgrpg elcaqhftls
//
LOCUS       NP_001400005             328 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001400005
VERSION     NP_001400005.1
DBSOURCE    REFSEQ: accession NM_001413076.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.2788964.1,
                                           SRR14038193.286678.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..328
                     /product="mitochondrial fission regulator 1 isoform 4
                     precursor"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=30859
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=5550
     Region          22..251
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15390.2)"
     Region          177..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          179..304
                     /region_name="Necessary and sufficient to promote
                     mitochondrial fission. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     CDS             1..328
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001413076.1:132..1118"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 11"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsvlwsrkpy gssrsivrki gtnlsliqcp rvqfqinsha
       61 tewspshpge davasfadvg wvakeegecs arlrtevrsr pplqddllff ekapsrqisl
      121 pdlsqeepql ktpalaneea lqkicalene laalraqiak ivtqqeqqnl tagdldsttf
      181 gtipphpppp ppplpppalg lhqstsavdl ikerrekran agktlvknnp kkpempnmle
      241 ilkemnsvkl rsvkrseqdv kpkpvdatdp aaliaealkk kfayryrsds qdevekgipk
      301 seseatserv lslpagfiqp hvskhclg
//
LOCUS       NP_001394097              78 aa            linear   PRI 21-NOV-2025
DEFINITION  retinoblastoma-associated protein isoform 5 [Homo sapiens].
ACCESSION   NP_001394097
VERSION     NP_001394097.1
DBSOURCE    REFSEQ: accession NM_001407168.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Castro,A., Ruiz Rivera,A., Moorman,C.C., Wolf-Saxon,E.R.,
            Mims,H.N., Vasquez Meza,V.I., Rangel,M.A., Loera,M.M., Bond,I.C.,
            Buchanan,S.B., Villarreal,E., Tripathi,S., Rubin,S.M. and
            Burke,J.R.
  TITLE     Structural and functional analysis of cancer-associated missense
            variants in the retinoblastoma protein pocket domain
  JOURNAL   J Biol Chem 301 (3), 108284 (2025)
   PUBMED   39938803
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Zhang,S., Valenzuela,L.F., Zatulovskiy,E., Mangiante,L., Curtis,C.
            and Skotheim,J.M.
  TITLE     The G1-S transition is promoted by Rb degradation via the E3 ligase
            UBR5
  JOURNAL   Sci Adv 10 (43), eadq6858 (2024)
   PUBMED   39441926
  REMARK    GeneRIF: The G1-S transition is promoted by Rb degradation via the
            E3 ligase UBR5.
REFERENCE   4  (residues 1 to 78)
  AUTHORS   Schwartz,C.J., Marra,A., Selenica,P., Gazzo,A., Tan,K., Ross,D.,
            Razavi,P., Chandarlapaty,S., Weigelt,B., Reis-Filho,J.S., Brogi,E.,
            Pareja,F. and Wen,H.Y.
  TITLE     RB1 Genetic Alterations in Estrogen Receptor-Positive Breast
            Carcinomas: Correlation With Neuroendocrine Differentiation
  JOURNAL   Mod Pathol 37 (8), 100541 (2024)
   PUBMED   38897452
  REMARK    GeneRIF: RB1 Genetic Alterations in Estrogen Receptor-Positive
            Breast Carcinomas: Correlation With Neuroendocrine Differentiation.
REFERENCE   5  (residues 1 to 78)
  AUTHORS   Konagaya,Y., Rosenthal,D., Ratnayeke,N., Fan,Y. and Meyer,T.
  TITLE     An intermediate Rb-E2F activity state safeguards proliferation
            commitment
  JOURNAL   Nature 631 (8020), 424-431 (2024)
   PUBMED   38926571
  REMARK    GeneRIF: An intermediate Rb-E2F activity state safeguards
            proliferation commitment.
REFERENCE   6  (residues 1 to 78)
  AUTHORS   Lohmann,D.R. and Gallie,B.L.
  TITLE     Retinoblastoma
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301625
REFERENCE   7  (residues 1 to 78)
  AUTHORS   Dyson,N., Guida,P., Munger,K. and Harlow,E.
  TITLE     Homologous sequences in adenovirus E1A and human papillomavirus E7
            proteins mediate interaction with the same set of cellular proteins
  JOURNAL   J Virol 66 (12), 6893-6902 (1992)
   PUBMED   1331501
REFERENCE   8  (residues 1 to 78)
  AUTHORS   Huang,S., Shin,E., Sheppard,K.A., Chokroverty,L., Shan,B.,
            Qian,Y.W., Lee,E.Y. and Yee,A.S.
  TITLE     The retinoblastoma protein region required for interaction with the
            E2F transcription factor includes the T/E1A binding and
            carboxy-terminal sequences
  JOURNAL   DNA Cell Biol 11 (7), 539-548 (1992)
   PUBMED   1388726
REFERENCE   9  (residues 1 to 78)
  AUTHORS   Onadim,Z., Hogg,A., Baird,P.N. and Cowell,J.K.
  TITLE     Oncogenic point mutations in exon 20 of the RB1 gene in families
            showing incomplete penetrance and mild expression of the
            retinoblastoma phenotype
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 6177-6181 (1992)
   PUBMED   1352883
REFERENCE   10 (residues 1 to 78)
  AUTHORS   Hogg,A., Onadim,Z., Baird,P.N. and Cowell,J.K.
  TITLE     Detection of heterozygous mutations in the RB1 gene in
            retinoblastoma patients using single-strand conformation
            polymorphism analysis and polymerase chain reaction sequencing
  JOURNAL   Oncogene 7 (7), 1445-1451 (1992)
   PUBMED   1352398
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136960.4.
            
            Summary: The protein encoded by this gene is a negative regulator
            of the cell cycle and was the first tumor suppressor gene found.
            The encoded protein also stabilizes constitutive heterochromatin to
            maintain the overall chromatin structure. The active,
            hypophosphorylated form of the protein binds transcription factor
            E2F1. Defects in this gene are a cause of childhood cancer
            retinoblastoma (RB), bladder cancer, and osteogenic sarcoma.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1911532.1,
                                           SRR14038191.3079486.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.2"
     Protein         1..78
                     /product="retinoblastoma-associated protein isoform 5"
                     /note="retinoblastoma-associated protein;
                     prepro-retinoblastoma-associated protein; protein
                     phosphatase 1, regulatory subunit 130; retinoblastoma
                     suspectibility protein; retinoblastoma 1"
                     /calculated_mol_wt=8727
     Region          <1..75
                     /region_name="Rb_C"
                     /note="Rb C-terminal domain; pfam08934"
                     /db_xref="CDD:462639"
     CDS             1..78
                     /gene="RB1"
                     /gene_synonym="OSRC; p105-Rb; p110-RB1; pp110; PPP1R130;
                     pRb; RB"
                     /coded_by="NM_001407168.1:104..340"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:5925"
                     /db_xref="HGNC:HGNC:9884"
                     /db_xref="MIM:614041"
ORIGIN      
        1 mvcnsdrvlk rsaegsnppk plkklrfdie gsdeadgskh lpgeskfqqk laemtstrtr
       61 mqkqkmndsm dtsnkeek
//
LOCUS       NP_001394252             326 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 24 [Homo sapiens].
ACCESSION   NP_001394252
VERSION     NP_001394252.1
DBSOURCE    REFSEQ: accession NM_001407323.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2232089.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2145313
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..326
                     /product="tropomyosin alpha-1 chain isoform 24"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=37451
     Region          2..>159
                     /region_name="EmrA"
                     /note="Multidrug resistance efflux pump EmrA [Defense
                     mechanisms]; COG1566"
                     /db_xref="CDD:441174"
     Region          90..324
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..326
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407323.1:84..1064"
                     /note="isoform 24 is encoded by transcript variant 24"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle ediaakekll rvsederdrv
       61 leelhkaeds llaaeeaaak ledelvslqk klkgtedeld kysealkdaq eklelaekka
      121 tdaeadvasl nrriqlveee ldraqerlat alqkleeaek aadesergmk viesraqkde
      181 ekmeiqeiql keakhiaeda drkyeevark lviiesdler aeeraelseg qvrqleeqlr
      241 imdqtlkalm aaedkysqke dryeeeikvl sdklkeaetr aefaersvtk leksiddled
      301 elyaqklkyk aiseeldhal ndmtsm
//
LOCUS       NP_001428088             345 aa            linear   PRI 21-NOV-2025
DEFINITION  urokinase-type plasminogen activator isoform 3 [Homo sapiens].
ACCESSION   NP_001428088
VERSION     NP_001428088.1
DBSOURCE    REFSEQ: accession NM_001441159.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Li,D., Ding,C., Huang,F., Chang,M., Lu,Z., Li,G., Li,Y., Gao,H. and
            Sun,F.
  TITLE     Bioinformatics Analysis of the Expression and Prognostic Value of
            PLAU Gene in Wilms' Tumor
  JOURNAL   Anticancer Res 44 (9), 3829-3842 (2024)
   PUBMED   39197889
  REMARK    GeneRIF: Bioinformatics Analysis of the Expression and Prognostic
            Value of PLAU Gene in Wilms' Tumor.
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Guo,J., Wang,H., Huang,C., Lai,C., Shang,W., Luo,S. and Chen,L.
  TITLE     PLAU, transcriptionally negatively regulated by GATA6, promotes
            lung squamous carcinoma cell proliferation and migration
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (5), 119744 (2024)
   PUBMED   38702016
  REMARK    GeneRIF: PLAU, transcriptionally negatively regulated by GATA6,
            promotes lung squamous carcinoma cell proliferation and migration.
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Cui,X., Sun,H., Liu,X., Bai,Y., Bai,Y., Cui,Y., Wang,B., Zhang,S.
            and Li,X.
  TITLE     PLAU promotes cell proliferation and migration of head and neck
            cancer via STAT3 signaling pathway
  JOURNAL   Exp Cell Res 438 (2), 114056 (2024)
   PUBMED   38663475
  REMARK    GeneRIF: PLAU promotes cell proliferation and migration of head and
            neck cancer via STAT3 signaling pathway.
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Cetinsoy,O., Anyanwu,I., Krishnanand,H., Natarajan,G.,
            Ramachandran,N., Thomas,A. and Brookes,K.J.
  TITLE     Gene Association Study of the Urokinase Plasminogen Activator and
            Its Receptor Gene in Alzheimer's Disease
  JOURNAL   J Alzheimers Dis 99 (1), 241-250 (2024)
   PUBMED   38669542
  REMARK    GeneRIF: Gene Association Study of the Urokinase Plasminogen
            Activator and Its Receptor Gene in Alzheimer's Disease.
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Mekkawy,A.H., Pourgholami,M.H. and Morris,D.L.
  TITLE     Involvement of urokinase-type plasminogen activator system in
            cancer: an overview
  JOURNAL   Med Res Rev 34 (5), 918-956 (2014)
   PUBMED   24549574
  REMARK    Review article
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Naldini,L., Tamagnone,L., Vigna,E., Sachs,M., Hartmann,G.,
            Birchmeier,W., Daikuhara,Y., Tsubouchi,H., Blasi,F. and
            Comoglio,P.M.
  TITLE     Extracellular proteolytic cleavage by urokinase is required for
            activation of hepatocyte growth factor/scatter factor
  JOURNAL   EMBO J 11 (13), 4825-4833 (1992)
   PUBMED   1334458
REFERENCE   8  (residues 1 to 345)
  AUTHORS   Li,X., Smith,R.A. and Dobson,C.M.
  TITLE     Sequential 1H NMR assignments and secondary structure of the
            kringle domain from urokinase
  JOURNAL   Biochemistry 31 (40), 9562-9571 (1992)
   PUBMED   1327118
REFERENCE   9  (residues 1 to 345)
  AUTHORS   Stephens,R.W., Aumailley,M., Timpl,R., Reisberg,T., Tapiovaara,H.,
            Myohanen,H., Murphy-Ullrich,J. and Vaheri,A.
  TITLE     Urokinase binding to laminin-nidogen. Structural requirements and
            interactions with heparin
  JOURNAL   Eur J Biochem 207 (3), 937-942 (1992)
   PUBMED   1499567
REFERENCE   10 (residues 1 to 345)
  AUTHORS   Moroi,M. and Aoki,N.
  TITLE     Isolation and characterization of alpha2-plasmin inhibitor from
            human plasma. A novel proteinase inhibitor which inhibits
            activator-induced clot lysis
  JOURNAL   J Biol Chem 251 (19), 5956-5965 (1976)
   PUBMED   134998
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22.
            
            Summary: This gene encodes a secreted serine protease that converts
            plasminogen to plasmin. The encoded preproprotein is
            proteolytically processed to generate A and B polypeptide chains.
            These chains associate via a single disulfide bond to form the
            catalytically inactive high molecular weight urokinase-type
            plasminogen activator (HMW-uPA). HMW-uPA can be further processed
            into the catalytically active low molecular weight urokinase-type
            plasminogen activator (LMW-uPA). This low molecular weight form
            does not bind to the urokinase-type plasminogen activator receptor.
            Mutations in this gene may be associated with Quebec platelet
            disorder and late-onset Alzheimer's disease. Alternative splicing
            results in multiple transcript variants, at least one of which
            encodes an isoform that is proteolytically processed. [provided by
            RefSeq, Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3562088.1,
                                           SRR14038192.1561694.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154529, SAMEA2163459
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..345
                     /product="urokinase-type plasminogen activator isoform 3"
                     /EC_number="3.4.21.73"
                     /note="plasminogen activator, urinary; U-plasminogen
                     activator; urokinase-type plasminogen activator"
                     /calculated_mol_wt=38910
     Region          <1..66
                     /region_name="KR"
                     /note="Kringle domain; Kringle domains are believed to
                     play a role in binding mediators, such as peptides, other
                     proteins, membranes, or phospholipids. They are autonomous
                     structural domains, found in a varying number of copies,
                     in blood clotting and...; cd00108"
                     /db_xref="CDD:238056"
     Site            order(8,18,46,48,57)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Region          93..336
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            93
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(138,189,290)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            order(284,309,311)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..345
                     /gene="PLAU"
                     /gene_synonym="ATF; BDPLT5; QPD; u-PA; UPA; URK"
                     /coded_by="NM_001441159.1:372..1409"
                     /note="isoform 3 is encoded by transcript variant 9"
                     /db_xref="GeneID:5328"
                     /db_xref="HGNC:HGNC:9052"
                     /db_xref="MIM:191840"
ORIGIN      
        1 mgrpclpwns atvlqqtyha hrsdalqlgl gkhnycrnpd nrrrpwcyvq vglkllvqec
       61 mvhdcadgkk pssppeelkf qcgqktlrpr fkiiggeftt ienqpwfaai yrrhrggsvt
      121 yvcggslisp cwvisathcf idypkkedyi vylgrsrlns ntqgemkfev enlilhkdys
      181 adtlahhndi allkirskeg rcaqpsrtiq ticlpsmynd pqfgtsceit gfgkenstdy
      241 lypeqlkmtv vklishrecq qphyygsevt tkmlcaadpq wktdscqgds ggplvcslqg
      301 rmtltgivsw grgcalkdkp gvytrvshfl pwirshtkee nglal
//
LOCUS       NP_001424298             664 aa            linear   PRI 21-NOV-2025
DEFINITION  MAP/microtubule affinity-regulating kinase 3 isoform l [Homo
            sapiens].
ACCESSION   NP_001424298 XP_016876788 XP_054232047
VERSION     NP_001424298.1
DBSOURCE    REFSEQ: accession NM_001437369.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Aparicio-Bautista,D.I., Jimenez-Ortega,R.F., Becerra-Cervera,A.,
            Aquino-Galvez,A., de Leon-Suarez,V.P., Casas-Avila,L., Salmeron,J.,
            Hidalgo-Bravo,A., Rivera-Paredez,B. and Velazquez-Cruz,R.
  TITLE     Interaction between MARK3 (rs11623869), PLCB4 (rs6086746) and
            GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women
  JOURNAL   Front Endocrinol (Lausanne) 15, 1392063 (2024)
   PUBMED   38715801
  REMARK    GeneRIF: Interaction between MARK3 (rs11623869), PLCB4 (rs6086746)
            and GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 664)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 664)
  AUTHORS   Li,M.G., Katsura,K., Nomiyama,H., Komaki,K., Ninomiya-Tsuji,J.,
            Matsumoto,K., Kobayashi,T. and Tamura,S.
  TITLE     Regulation of the interleukin-1-induced signaling pathways by a
            novel member of the protein phosphatase 2C family (PP2Cepsilon)
  JOURNAL   J Biol Chem 278 (14), 12013-12021 (2003)
   PUBMED   12556533
REFERENCE   7  (residues 1 to 664)
  AUTHORS   Sun,T.Q., Lu,B., Feng,J.J., Reinhard,C., Jan,Y.N., Fantl,W.J. and
            Williams,L.T.
  TITLE     PAR-1 is a Dishevelled-associated kinase and a positive regulator
            of Wnt signalling
  JOURNAL   Nat Cell Biol 3 (7), 628-636 (2001)
   PUBMED   11433294
REFERENCE   8  (residues 1 to 664)
  AUTHORS   Peng,C.Y., Graves,P.R., Ogg,S., Thoma,R.S., Byrnes,M.J. 3rd, Wu,Z.,
            Stephenson,M.T. and Piwnica-Worms,H.
  TITLE     C-TAK1 protein kinase phosphorylates human Cdc25C on serine 216 and
            promotes 14-3-3 protein binding
  JOURNAL   Cell Growth Differ 9 (3), 197-208 (1998)
   PUBMED   9543386
REFERENCE   9  (residues 1 to 664)
  AUTHORS   Ono,T., Kawabe,T., Sonta,S. and Okamoto,T.
  TITLE     Assignment of MARK3 alias KP78 to human chromosome band 14q32.3 by
            in situ hybridization
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 101-102 (1997)
   PUBMED   9533022
REFERENCE   10 (residues 1 to 664)
  AUTHORS   Meller,N., Liu,Y.C., Collins,T.L., Bonnefoy-Berard,N., Baier,G.,
            Isakov,N. and Altman,A.
  TITLE     Direct interaction between protein kinase C theta (PKC theta) and
            14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition
            of PKC theta translocation and function
  JOURNAL   Mol Cell Biol 16 (10), 5782-5791 (1996)
   PUBMED   8816492
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133367.4 and KF456011.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_016876788.1, XP_054232047.1.
            
            Summary: The protein encoded by this gene is activated by
            phosphorylation and in turn is involved in the phosphorylation of
            tau proteins MAP2 and MAP4. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.267898.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.32-q32.33"
     Protein         1..664
                     /product="MAP/microtubule affinity-regulating kinase 3
                     isoform l"
                     /EC_number="2.7.11.1"
                     /note="EMK-2; C-TAK1; ELKL motif kinase 2; protein kinase
                     STK10; ser/Thr protein kinase PAR-1; cdc25C-associated
                     protein kinase 1; MAP/microtubule affinity-regulating
                     kinase 3; serine/threonine-protein kinase p78"
                     /calculated_mol_wt=74527
     Region          18..243
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          261..303
                     /region_name="UBA_MARK3_4"
                     /note="UBA domain found in MAP/microtubule
                     affinity-regulating kinase MARK3, MARK4, and similar
                     proteins; cd14407"
                     /db_xref="CDD:270590"
     Region          565..662
                     /region_name="MARK1-3_C"
                     /note="C-terminal, kinase associated domain 1 (KA1), a
                     phospholipid binding domain, of microtubule
                     affinity-regulating kinases 1-3; cd12196"
                     /db_xref="CDD:213381"
     Site            order(567,570,640,642..643)
                     /site_type="other"
                     /note="putative phospholipid binding site [chemical
                     binding]"
                     /db_xref="CDD:213381"
     CDS             1..664
                     /gene="MARK3"
                     /gene_synonym="CTAK1; KP78; Par-1a; PAR1A; VIPB"
                     /coded_by="NM_001437369.1:616..2610"
                     /note="isoform l is encoded by transcript variant 12"
                     /db_xref="GeneID:4140"
                     /db_xref="HGNC:HGNC:6897"
                     /db_xref="MIM:602678"
ORIGIN      
        1 mstrtplptv nerdtenvai kiidktqlnp tslqklfrev rimkilnhpn ivklfeviet
       61 ektlylimey asggevfdyl vahgrmkeke arskfrqivs avqychqkri vhrdlkaenl
      121 lldadmniki adfgfsneft vggkldtfcg sppyaapelf qgkkydgpev dvwslgvily
      181 tlvsgslpfd gqnlkelrer vlrgkyripf ymstdcenll krflvlnpik rgtleqimkd
      241 rwinagheed elkpfvepel disdqkridi mvgmgysqee iqeslskmky deitatylll
      301 grkssevrps sdlnnstgqs phhkvqrsvs ssqkqrrysd hagpaipsvv aypkrsqtst
      361 adsdlkedgi ssrkssgsav ggkgiapasp mlgnasnpnk adiperkkss tvpssntasg
      421 gmtrrntyvc serttadrhs viqngkenst ipdqrtpvas thsissaatp drirfprgta
      481 srstfhgqpr errtatyngp paspslshea tplsqtrsrg stnlfsklts kltrrlptey
      541 erngryegss rnvsaeqkde nkeakprslr ftwsmkttss mdpgdmmrei rkvldanncd
      601 yeqrerfllf cvhgdghaen lvqwemevck lprlslngvr fkrisgtsia fkniaskian
      661 elkl
//
LOCUS       NP_001394737            1233 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 4 precursor
            [Homo sapiens].
ACCESSION   NP_001394737
VERSION     NP_001394737.1
DBSOURCE    REFSEQ: accession NM_001407808.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1233)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1233)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1233)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1233)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1233)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1233)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1233)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1233)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1233)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1233)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1422853.1,
                                           SRR14038196.1179716.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1233
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1233
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 4 precursor"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=134914
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O00411.2)"
                     /calculated_mol_wt=4109
     Region          18..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          95..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          261..290
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          296..323
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          432..704
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          731..750
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          831..1233
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1233
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407808.1:26..3727"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 msalcwgrga aglkralrpc grpglpgkeg taggvcgprr sssaspqeqd qdrrkdwghv
       61 ellevlqarv rqlqaesvse vvvnrvdvar lpecgsgdgs lqpprkvqmg akdatpvpcg
      121 rwakilekdk rtqqmrmqrl kaklqmpfqs gefkaltrrl qveprllskq magcledctr
      181 qapespweeq larllqeapg klsldveqap sgqhsqaqls gqqqrllaff kcclltdqlp
      241 lahhllvvhh gqrqkrkllt ldmynavmlg warqgafkel vyvlfmvkda gltpdllsya
      301 aalqcmgrqd qdagtiercl eqmsqeglkl qalftavlls eedratvlka vhkvkptfsl
      361 ppqlpppvnt skllrdvyak dgrvsypklh lplktlqclf ekqlhmelas rvcvvsvekp
      421 tlpskevkha rktlktlrdq wekalcralr etknrlerev yegrfslypf lcllderevv
      481 rmllqvlqal paqgesfttl arelsartfs rhvvqrqrvs gqvqalqnhy rkylcllasd
      541 aevpepclpr qyweelgape alreqpwplp vqmelgklla emlvqatqmp csldkphrss
      601 rlvpvlyhvy sfrnvqqigi lkphpayvql lekaaeptlt feavdvpmlc pplpwtsphs
      661 gafllsptkl mrtvegatqh qelletcppt alhgaldalt qlgncawrvn grvldlvlql
      721 fqakgcpqlg vpappseapq ppeahlphsa aparkaelrr elahcqkvar emhslraeal
      781 yrlslaqhlr drvfwlphnm dfrgrtypcp phfnhlgsdv arallefaqg rplgphgldw
      841 lkihlvnltg lkkreplrkr lafaeevmdd ildsadqplt grkwwmgaee pwqtlaccme
      901 vanavrasdp aayvshlpvh qdgscnglqh yaalgrdsvg aasvnlepsd vpqdvysgva
      961 aqvevfrrqd aqrgmrvaqv legfitrkvv kqtvmtvvyg vtryggrlqi ekrlrelsdf
     1021 pqvrqefvwe ashylvrqvf kslqemfsgt raiqhwltes arlishmgsv vewvtplgvp
     1081 viqpyrldsk vkqigggiqs itythngdis rkpntrkqkn gfppnfihsl dsshmmltal
     1141 hcyrkgltfv svhdcywtha advsvmnqvc reqfvrlhse pilqdlsrfl vkrfcsepqk
     1201 ileasqlket lqavpkpgaf dleqvkrsty ffs
//
LOCUS       NP_001389620            1306 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform b [Homo sapiens].
ACCESSION   NP_001389620
VERSION     NP_001389620.1
DBSOURCE    REFSEQ: accession NM_001402691.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1306)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1306)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1306)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1306)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1306)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1306)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1306)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1306)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1306)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1306)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.126597.1,
                                           SRR1803611.91609.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1306
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1306
                     /product="kinectin isoform b"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=150222
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          <326..>584
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          458..1246
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1306
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402691.1:179..4099"
                     /note="isoform b is encoded by transcript variant 16"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqlsitskvq
      841 elqnllkgke eqmntmkavl eekekdlant gkwlqdlqee neslkahvqe vaqhnlkeas
      901 sasqfeelei vlkekenelk rleamlkere sdlssktqll qdvqdenklf ksqieqlkqq
      961 nyqqassfpp heellkvise rekeisglwn eldslkdave hqrkknndlr eknweameal
     1021 astekmlqdk vnktskerqq qveaveleak evlkklfpkv svpsnlsyge wlhgfekkak
     1081 ecmagtsgse evkvlehklk eademhtllq lecekyksvl aetegilqkl qrsveqeenk
     1141 wkvkvdeshk tikqmqssft sseqelerlr senkdienlr rerehlemel ekaemersty
     1201 vtevrelkaq lnetltklrt eqnerqkvag dlhkaqqsle liqskivkaa gdttviensd
     1261 vspetessek etmsvslnqt vtqlqqllqa vnqqltkeke hyqvle
//
LOCUS       NP_001397750             268 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase III subunit RPC6 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001397750 XP_016883085
VERSION     NP_001397750.1
DBSOURCE    REFSEQ: accession NM_001410821.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Hu,P., Wu,S., Sun,Y., Yuan,C.C., Kobayashi,R., Myers,M.P. and
            Hernandez,N.
  TITLE     Characterization of human RNA polymerase III identifies orthologues
            for Saccharomyces cerevisiae RNA polymerase III subunits
  JOURNAL   Mol Cell Biol 22 (22), 8044-8055 (2002)
   PUBMED   12391170
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Mertens,C., Hofmann,I., Wang,Z., Teichmann,M., Sepehri Chong,S.,
            Schnolzer,M. and Franke,W.W.
  TITLE     Nuclear particles containing RNA polymerase III complexes
            associated with the junctional plaque protein plakophilin 2
  JOURNAL   Proc Natl Acad Sci U S A 98 (14), 7795-7800 (2001)
   PUBMED   11416169
REFERENCE   8  (residues 1 to 268)
  AUTHORS   Jones,E., Kimura,H., Vigneron,M., Wang,Z., Roeder,R.G. and
            Cook,P.R.
  TITLE     Isolation and characterization of monoclonal antibodies directed
            against subunits of human RNA polymerases I, II, and III
  JOURNAL   Exp Cell Res 254 (1), 163-172 (2000)
   PUBMED   10623476
REFERENCE   9  (residues 1 to 268)
  AUTHORS   Hsieh,Y.J., Kundu,T.K., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     The TFIIIC90 subunit of TFIIIC interacts with multiple components
            of the RNA polymerase III machinery and contains a histone-specific
            acetyltransferase activity
  JOURNAL   Mol Cell Biol 19 (11), 7697-7704 (1999)
   PUBMED   10523658
REFERENCE   10 (residues 1 to 268)
  AUTHORS   Wang,Z. and Roeder,R.G.
  TITLE     Three human RNA polymerase III-specific subunits form a subcomplex
            with a selective function in specific transcription initiation
  JOURNAL   Genes Dev 11 (10), 1315-1326 (1997)
   PUBMED   9171375
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121893.21.
            
            On Aug 16, 2022 this sequence version replaced XP_016883085.1.
            
            Summary: The protein encoded by this gene is one of more than a
            dozen subunits forming eukaryotic RNA polymerase III (RNA Pol III),
            which transcribes 5S ribosomal RNA and tRNA genes. This protein has
            been shown to bind both TFIIIB90 and TBP, two subunits of RNA
            polymerase III transcription initiation factor IIIB (TFIIIB).
            Unlike most of the other RNA Pol III subunits, the encoded protein
            is unique to this polymerase. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1901347.1,
                                           SRR14038191.3822833.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.23"
     Protein         1..268
                     /product="DNA-directed RNA polymerase III subunit RPC6
                     isoform 3"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerase III subunit RPC6;
                     polymerase (RNA) III (DNA directed) polypeptide F, 39 kDa;
                     RNA polymerase III C39 subunit; RNA polymerase III subunit
                     C6; polymerase (RNA) III subunit F"
                     /calculated_mol_wt=29917
     Region          12..267
                     /region_name="RNA_pol_Rpc34"
                     /note="RNA polymerase Rpc34 subunit; pfam05158"
                     /db_xref="CDD:398703"
     CDS             1..268
                     /gene="POLR3F"
                     /gene_synonym="C34; IMD101; RPC39; RPC6"
                     /coded_by="NM_001410821.1:118..924"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS93015.1"
                     /db_xref="GeneID:10621"
                     /db_xref="HGNC:HGNC:15763"
                     /db_xref="MIM:617455"
ORIGIN      
        1 maevkvkvqp pdadpveien riielchqfp hgitdqviqn emphieaqqr avainrllsm
       61 gqldllrsnt gllyrikdsq nagkmkgsdn qeklvyqiie dagnkgiwsr diryksnlpl
      121 teinkilknl eskklikavk svaaetares kqnpmiqrns sfasshevwk yicelgiskv
      181 elsmedieti lntliydgkv emtiiaakeg tvgsvdghmk lyravnpiip ptglvrapcg
      241 lcpvfddche ggeispsnci ymtewlef
//
LOCUS       NP_001393523            1164 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 1 [Homo sapiens].
ACCESSION   NP_001393523 XP_016870585
VERSION     NP_001393523.1
DBSOURCE    REFSEQ: accession NM_001406594.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1164)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1164)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1164)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1164)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1164)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1164)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1164)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            On May 18, 2022 this sequence version replaced XP_016870585.1.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2148336.1,
                                           SRR14038191.3284522.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1164
                     /product="hamartin isoform 1"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=129636
     Region          7..719
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          403..787
                     /region_name="Mediates interaction with WDR45B.
                     /evidence=ECO:0000269|PubMed:28561066"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Region          439..571
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <708..>960
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1006..1085
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1131..1164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1164
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406594.1:437..3931"
                     /note="isoform 1 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS6956.1"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt aggkgtplgt patspppapl chsddyvhis lpqatvtppr
      421 keermdsarp clhrqhhlln drgseeppgs kgsvtlsdlp gflgdlasee dsiekdkeea
      481 aisrelseit taeaepvvpr ggfdspfyrd slpgsqrkth saasssqgas vnpeplhssl
      541 dklgpdtpkq aftpidlpcg sadespagdr ecqtsletsi ftpspckipp ptrvgfgsgq
      601 pppydhlfev alpktahhfv irkteellkk akgnteedgv pstspmevld rliqqgadah
      661 skelnklplp sksvdwthfg gsppsdeirt lrdqllllhn qllyerfkrq qhalrnrrll
      721 rkvikaaale ehnaamkdql klqekdiqmw kvslqkeqar ynqlqeqrdt mvtklhsqir
      781 qlqhdreefy nqsqelqtkl edcrnmiael rielkkannk vchtelllsq vsqklsnses
      841 vqqqmeflnr qllvlgevne lyleqlqnkh sdttkevemm kaayrkelek nrshvlqqtq
      901 rldtsqkril eleshlakkd hllleqkkyl edvklqargq lqaaesryea qkritqvfel
      961 eildlygrle kdgllkklee ekaeaaeaae erldccndgc sdsmvghnee asghngetkt
     1021 prpssargss gsrggggsss ssselstpek pphqragpfs srwettmgea sasipttvgs
     1081 lpssksflgm karelfrnks esqcdedgmt sslseslkte lgkdlgveak iplnldgphp
     1141 spptpdsvgq lhimdyneth hehs
//
LOCUS       NP_001392591            1171 aa            linear   PRI 21-NOV-2025
DEFINITION  phospholipid-transporting ATPase IH isoform d [Homo sapiens].
ACCESSION   NP_001392591 XP_005268357
VERSION     NP_001392591.1
DBSOURCE    REFSEQ: accession NM_001405662.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1171)
  AUTHORS   Higuchi,T., Oka,S., Furukawa,H., Shimada,K., Tsunoda,S., Ito,S.,
            Okamoto,A., Fujimori,M., Nakamura,T., Katayama,M., Saisho,K.,
            Shinohara,S., Matsui,T., Migita,K., Nagaoka,S. and Tohma,S.
  TITLE     Association of a Single Nucleotide Variant in TERT with Airway
            Disease in Japanese Rheumatoid Arthritis Patients
  JOURNAL   Genes (Basel) 14 (11), 2084 (2023)
   PUBMED   38003027
  REMARK    GeneRIF: Association of a Single Nucleotide Variant in TERT with
            Airway Disease in Japanese Rheumatoid Arthritis Patients.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1171)
  AUTHORS   Chepurwar,S., von Loh,S.M., Wigger,D.C., Neef,J., Frommolt,P.,
            Beutner,D., Lang-Roth,R., Kubisch,C., Strenzke,N. and Volk,A.E.
  TITLE     A mutation in ATP11A causes autosomal-dominant auditory neuropathy
            type 2
  JOURNAL   Hum Mol Genet 32 (7), 1083-1089 (2023)
   PUBMED   36300302
  REMARK    GeneRIF: A mutation in ATP11A causes autosomal-dominant auditory
            neuropathy type 2.
REFERENCE   3  (residues 1 to 1171)
  AUTHORS   Miyata,Y., Yamada,K., Nagata,S. and Segawa,K.
  TITLE     Two types of type IV P-type ATPases independently re-establish the
            asymmetrical distribution of phosphatidylserine in plasma membranes
  JOURNAL   J Biol Chem 298 (11), 102527 (2022)
   PUBMED   36162506
REFERENCE   4  (residues 1 to 1171)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   5  (residues 1 to 1171)
  AUTHORS   Pater,J.A., Penney,C., O'Rielly,D.D., Griffin,A., Kamal,L.,
            Brownstein,Z., Vona,B., Vinkler,C., Shohat,M., Barel,O.,
            French,C.R., Singh,S., Werdyani,S., Burt,T., Abdelfatah,N.,
            Houston,J., Doucette,L.P., Squires,J., Glaser,F., Roslin,N.M.,
            Vincent,D., Marquis,P., Woodland,G., Benoukraf,T., Hawkey-Noble,A.,
            Avraham,K.B., Stanton,S.G. and Young,T.L.
  TITLE     Autosomal dominant non-syndromic hearing loss maps to DFNA33
            (13q34) and co-segregates with splice and frameshift variants in
            ATP11A, a phospholipid flippase gene
  JOURNAL   Hum Genet 141 (3-4), 431-444 (2022)
   PUBMED   35278131
  REMARK    GeneRIF: Autosomal dominant non-syndromic hearing loss maps to
            DFNA33 (13q34) and co-segregates with splice and frameshift
            variants in ATP11A, a phospholipid flippase gene.
REFERENCE   6  (residues 1 to 1171)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 1171)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   8  (residues 1 to 1171)
  AUTHORS   Andrew Nesbit,M., Bowl,M.R., Harding,B., Schlessinger,D.,
            Whyte,M.P. and Thakker,R.V.
  TITLE     X-linked hypoparathyroidism region on Xq27 is evolutionarily
            conserved with regions on 3q26 and 13q34 and contains a novel
            P-type ATPase
  JOURNAL   Genomics 84 (6), 1060-1070 (2004)
   PUBMED   15533723
REFERENCE   9  (residues 1 to 1171)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
REFERENCE   10 (residues 1 to 1171)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139384.17, AL356752.13 and
            AL356740.19.
            
            On Apr 29, 2022 this sequence version replaced XP_005268357.1.
            
            Summary: The protein encoded by this gene is an integral membrane
            ATPase. The encoded protein is probably phosphorylated in its
            intermediate state and likely drives the transport of ions such as
            calcium across membranes. [provided by RefSeq, Apr 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1367676.1,
                                           SRR14038196.2695241.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1171
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..1171
                     /product="phospholipid-transporting ATPase IH isoform d"
                     /EC_number="7.6.2.1"
                     /note="probable phospholipid-transporting ATPase IH;
                     potential phospholipid-transporting ATPase IH;
                     phospholipid-translocating ATPase; P4-ATPase flippase
                     complex alpha subunit ATP11A; ATPase, class VI, type 11A"
                     /calculated_mol_wt=133530
     Region          47..983
                     /region_name="P-type_ATPase_APLT_Dnf-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2,
                     -10D, -11B, -11C; cd02073"
                     /db_xref="CDD:319770"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            89..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            297..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            350..372
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            order(414..416,553,576..578,640,687..689,798,801,804,825,
                     828)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     Site            457..458
                     /site_type="cleavage"
                     /note="Cleavage, by CASP3.
                     /evidence=ECO:0000269|PubMed:26567335; propagated from
                     UniProtKB/Swiss-Prot (P98196.3)"
     Site            490..491
                     /site_type="cleavage"
                     /note="Cleavage, by CASP3.
                     /evidence=ECO:0000269|PubMed:26567335; propagated from
                     UniProtKB/Swiss-Prot (P98196.3)"
     Site            738
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P98196.3)"
     Site            882..902
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            915..934
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Region          <965..1061
                     /region_name="RDD"
                     /note="RDD family; cl00746"
                     /db_xref="CDD:469900"
     Site            965..986
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            1001..1023
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            1030..1050
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            1069..1093
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     CDS             1..1171
                     /gene="ATP11A"
                     /gene_synonym="ATPIH; ATPIS; AUNA2; DFNA84; HLD24"
                     /coded_by="NM_001405662.1:380..3895"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:23250"
                     /db_xref="HGNC:HGNC:13552"
                     /db_xref="MIM:605868"
ORIGIN      
        1 mdcslvrtlv hrycageenw vdsrtiyvgh repppgaeay ipqrypdnri vsskytfwnf
       61 ipknlfeqfr rvanfyflii flvqliidtp tspvtsglpl ffvitvtaik qgyedwlrhk
      121 adnamnqcpv hfiqhgklvr kqsrklrvgd ivmvkedetf pcdliflssn rgdgtchvtt
      181 asldgesshk thyavqdtkg fhteediggl hatieceqpq pdlykfvgri nvysdlndpv
      241 vrplgsenll lrgatlknte kifgvaiytg metkmalnyq sksqkrsave ksmnaflivy
      301 lciliskali ntvlkymwqs epfrdepwyn qkteserqrn lflkaftdfl afmvlfnyii
      361 pvsmyvtvem qkflgsyfit wdedmfdeet gegplvntsd lneelgqvey iftdktgtlt
      421 ennmefkecc ieghvyvphv icngqvlpes sgidmidssp svngrereel ffralclcht
      481 vqvkdddsvd gprkspdggk scvyissspd evalvegvqr lgftylrlkd nymeilnren
      541 hierfellei lsfdsvrrrm svivksatge iylfckgads sifprviegk vdqirarver
      601 naveglrtlc vaykrliqee yegickllqa akvalqdrek klaeayeqie kdltllgata
      661 vedrlqekaa dtiealqkag ikvwvltgdk metaaatcya cklfrrntql lelttkriee
      721 qslhdvlfel sktvlrhsgs ltrdnlsgls admqdyglii dgaalslimk predgssgny
      781 relfleicrs csavlccrma plqkaqivkl ikfskehpit laigdgandv smileahvgi
      841 gvigkegrqa arnsdyaipk fkhlkkmllv hghfyyiris elvqyffykn vcfifpqfly
      901 qffcgfsqqt lydtayltly nisftslpil lyslmeqhvg idvlkrdptl yrdvaknall
      961 rwrvfiywtl lglfdalvff fgayfvfent tvtsngqifg nwtfgtlvft vmvftvtlkl
     1021 aldthywtwi nhfviwgsll fyvvfsllwg gviwpflnyq rmyyvfiqml ssgpawlaiv
     1081 llvtisllpd vlkkvlcrql wptatervqs pgyqstcpsa awysshsqqv tlaawkekvs
     1141 tepppilggs hhhcssipsh scprsrvgml v
//
LOCUS       NP_001427924             780 aa            linear   PRI 21-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 6 isoform 5 [Homo sapiens].
ACCESSION   NP_001427924 XP_011529715 XP_054184145
VERSION     NP_001427924.1
DBSOURCE    REFSEQ: accession NM_001440995.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Zheng,T., Zhou,H., Zheng,Z., Guo,Y., Liu,J., Zhang,J. and Li,S.
  TITLE     The pathological significance and potential mechanism of ARHGEF6 in
            lung adenocarcinoma
  JOURNAL   Comput Biol Med 158, 106894 (2023)
   PUBMED   37058762
  REMARK    GeneRIF: The pathological significance and potential mechanism of
            ARHGEF6 in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 780)
  AUTHORS   Li,K., Wang,H., Yang,C., Li,C., Xue,B. and Zhou,J.
  TITLE     Clinical implication and potential function of ARHGEF6 in acute
            myeloid leukemia: An in vitro study
  JOURNAL   PLoS One 18 (4), e0283934 (2023)
   PUBMED   37027440
  REMARK    GeneRIF: Clinical implication and potential function of ARHGEF6 in
            acute myeloid leukemia: An in vitro study.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 780)
  AUTHORS   Klambt,V., Buerger,F., Wang,C., Naert,T., Richter,K., Nauth,T.,
            Weiss,A.C., Sieckmann,T., Lai,E., Connaughton,D.M., Seltzsam,S.,
            Mann,N., Majmundar,A.J., Wu,C.W., Onuchic-Whitford,A.C., Shril,S.,
            Schneider,S., Schierbaum,L., Dai,R., Bekheirnia,M.R., Joosten,M.,
            Shlomovitz,O., Vivante,A., Banne,E., Mane,S., Lifton,R.P.,
            Kirschner,K.M., Kispert,A., Rosenberger,G., Fischer,K.D.,
            Lienkamp,S.S., Zegers,M.M.P. and Hildebrandt,F.
  TITLE     Genetic Variants in ARHGEF6 Cause Congenital Anomalies of the
            Kidneys and Urinary Tract in Humans, Mice, and Frogs
  JOURNAL   J Am Soc Nephrol 34 (2), 273-290 (2023)
   PUBMED   36414417
  REMARK    GeneRIF: Genetic Variants in ARHGEF6 Cause Congenital Anomalies of
            the Kidneys and Urinary Tract in Humans, Mice, and Frogs.
REFERENCE   5  (residues 1 to 780)
  AUTHORS   Wang,N., Li,Y., Zhou,X., Wang,X. and Yang,G.
  TITLE     Comprehensive analysis identifies ARHGEF6 as a potential prognostic
            and immunological biomarker in lung adenocarcinoma
  JOURNAL   Comput Biol Med 153, 106448 (2023)
   PUBMED   36586227
  REMARK    GeneRIF: Comprehensive analysis identifies ARHGEF6 as a potential
            prognostic and immunological biomarker in lung adenocarcinoma.
REFERENCE   6  (residues 1 to 780)
  AUTHORS   Yoshii,S., Tanaka,M., Otsuki,Y., Wang,D.Y., Guo,R.J., Zhu,Y.,
            Takeda,R., Hanai,H., Kaneko,E. and Sugimura,H.
  TITLE     alphaPIX nucleotide exchange factor is activated by interaction
            with phosphatidylinositol 3-kinase
  JOURNAL   Oncogene 18 (41), 5680-5690 (1999)
   PUBMED   10523848
REFERENCE   7  (residues 1 to 780)
  AUTHORS   Yntema,H.G., Hamel,B.C., Smits,A.P., van Roosmalen,T., van den
            Helm,B., Kremer,H., Ropers,H.H., Smeets,D.F. and van Bokhoven,H.
  TITLE     Localisation of a gene for non-specific X linked mental retardation
            (MRX46) to Xq25-q26
  JOURNAL   J Med Genet 35 (10), 801-805 (1998)
   PUBMED   9783701
REFERENCE   8  (residues 1 to 780)
  AUTHORS   Ebinu,J.O., Bottorff,D.A., Chan,E.Y., Stang,S.L., Dunn,R.J. and
            Stone,J.C.
  TITLE     RasGRP, a Ras guanyl nucleotide- releasing protein with calcium-
            and diacylglycerol-binding motifs
  JOURNAL   Science 280 (5366), 1082-1086 (1998)
   PUBMED   9582122
REFERENCE   9  (residues 1 to 780)
  AUTHORS   Manser,E., Loo,T.H., Koh,C.G., Zhao,Z.S., Chen,X.Q., Tan,L.,
            Tan,I., Leung,T. and Lim,L.
  TITLE     PAK kinases are directly coupled to the PIX family of nucleotide
            exchange factors
  JOURNAL   Mol Cell 1 (2), 183-192 (1998)
   PUBMED   9659915
REFERENCE   10 (residues 1 to 780)
  AUTHORS   Nomura,N., Nagase,T., Miyajima,N., Sazuka,T., Tanaka,A., Sato,S.,
            Seki,N., Kawarabayasi,Y., Ishikawa,K. and Tabata,S.
  TITLE     Prediction of the coding sequences of unidentified human genes. II.
            The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
            analysis of cDNA clones from human cell line KG-1 (supplement)
  JOURNAL   DNA Res 1 (5), 251-262 (1994)
   PUBMED   7584048
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL683813.10 and AL135783.6.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_011529715.1, XP_054184145.1.
            
            Summary: Rho GTPases play a fundamental role in numerous cellular
            processes that are initiated by extracellular stimuli that work
            through G protein coupled receptors. The encoded protein belongs to
            a family of cytoplasmic proteins that activate the Ras-like family
            of Rho proteins by exchanging bound GDP for GTP. It may form a
            complex with G proteins and stimulate Rho-dependent signals. This
            protein is activated by PI3-kinase. Mutations in this gene can
            cause X-chromosomal non-specific cognitive disability. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3040803.1,
                                           SRR14038195.1335670.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.3"
     Protein         1..780
                     /product="rho guanine nucleotide exchange factor 6 isoform
                     5"
                     /note="Rac/Cdc42 guanine exchange factor (GEF) 6; rho
                     guanine nucleotide exchange factor 6; PAK-interacting
                     exchange factor, alpha; Rac/Cdc42 guanine nucleotide
                     exchange factor (GEF) 6"
                     /calculated_mol_wt=87832
     Region          1..117
                     /region_name="CH_alphaPIX"
                     /note="calponin homology (CH) domain found in alpha-Pak
                     Interactive eXchange factor; cd21265"
                     /db_xref="CDD:409114"
     Site            order(3,7,65,67..68,71..72,74,81..89,95,97..98,100..101,
                     104..105,108)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409114"
     Region          115..160
                     /region_name="RhoGEF67_u1"
                     /note="Unstructured region one on RhoGEF 6 and 7;
                     pfam16615"
                     /db_xref="CDD:465201"
     Region          115..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15052.2)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15052.2)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15052.2)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15052.2)"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15052.2)"
     Region          162..219
                     /region_name="SH3_alphaPIX"
                     /note="Src Homology 3 domain of alpha-Pak Interactive
                     eXchange factor; cd12060"
                     /db_xref="CDD:212993"
     Site            order(169,171,174,177..178,193,195..197,208,210,212..213)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212993"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15052.2)"
     Region          242..419
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(248,252,346,370..371,374..375,377..378,381..382,
                     385..386,389,415,419)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          450..547
                     /region_name="PH_Cool_Pix"
                     /note="Cloned out of library/PAK-interactive exchange
                     factor pleckstrin homology (PH) domain; cd01225"
                     /db_xref="CDD:269932"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K4I3; propagated from
                     UniProtKB/Swiss-Prot (Q15052.2)"
     Region          580..678
                     /region_name="RhoGEF67_u2"
                     /note="Unstructured region two on RhoGEF 6 and 7;
                     pfam16614"
                     /db_xref="CDD:465200"
     Site            644
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15052.2)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15052.2)"
     Region          689..773
                     /region_name="betaPIX_CC"
                     /note="betaPIX coiled coil; pfam16523"
                     /db_xref="CDD:465158"
     CDS             1..780
                     /gene="ARHGEF6"
                     /gene_synonym="alpha-PIX; alphaPIX; Cool-2; COOL2; MRX46;
                     PIXA"
                     /coded_by="NM_001440995.1:51..2393"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:9459"
                     /db_xref="HGNC:HGNC:685"
                     /db_xref="MIM:300267"
ORIGIN      
        1 mnpeeqivtw lislgvlesp kkticdpeef lksslkngvv lcklinrlmp gsvekfcldp
       61 qteadcinni ndflkgcatl qveifdpddl ysgvnfskvl stllavnkat edqlserpcg
      121 rssslsaant sqtnpqgavs stvsglqrqs ktvemtengs hqlivkarfn fkqtnedels
      181 vckgdiiyvt rveeggwweg tlngrtgwfp snyvreikss erplspkavk gfetapltkn
      241 yytvvlqnil dtekeyakel qsllvtylrp lqsnnnlstv evtsllgnfe evctfqqtlc
      301 qaleecskfp enqhkvggcl lslmphfksm ylaycanhps avnvltqhsd eleqfmenqg
      361 asspgililt tnlskpfmrl ekyvtllqel erhmedthpd hqdilkaiva fktlmgqcqd
      421 lrkrkqlelq ilsepiqawe gediknlgnv ifmsqvmvqy gaceekeery lmlfsnvlim
      481 lsasprmsgf iyqgkipiag tvvtrldeie gndctfeitg ntverivvhc nnnqdfqewl
      541 eqlnrlirgp ascsslskts ssscsahstf sqsfsstgqp rgpleppqii kpwslsclrp
      601 applrpsaal gykermsyil kesskspktm kkflhkrkte rkpseeeyvi rkstaaleed
      661 aqilkvieay ctsanfqqgh gsstrkdsip qvllpeeekl iieetrsngq timeekslvd
      721 tvyalkdevr elkqenkrmk qcleeelksr rdleklvrrl lkqtdecirg esssktsilp
//
LOCUS       NP_001400616             316 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 20 precursor [Homo sapiens].
ACCESSION   NP_001400616
VERSION     NP_001400616.1
DBSOURCE    REFSEQ: accession NM_001413687.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 316)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 316)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 316)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 316)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 316)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7 and AC010656.7.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3349739.1,
                                           SRR14372079.2953178.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..316
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 20 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=32125
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..>264
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     CDS             1..316
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413687.1:169..1119"
                     /note="isoform 20 precursor is encoded by transcript
                     variant 23"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvdngl qlhpycckgh efilfygciv fpvvyvphfl
      301 yphcgwtpql lpylwy
//
LOCUS       NP_001394196             354 aa            linear   PRI 21-NOV-2025
DEFINITION  cellular tumor antigen p53 isoform g [Homo sapiens].
ACCESSION   NP_001394196
VERSION     NP_001394196.1
DBSOURCE    REFSEQ: accession NM_001407267.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Mirgayazova,R., Khadiullina,R., Chasov,V., Mingaleeva,R.,
            Miftakhova,R., Rizvanov,A. and Bulatov,E.
  TITLE     Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an Option?
  JOURNAL   Genes (Basel) 11 (6), 704 (2020)
   PUBMED   32630614
  REMARK    GeneRIF: Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an
            Option?
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Flynt,E., Bisht,K., Sridharan,V., Ortiz,M., Towfic,F. and
            Thakurta,A.
  TITLE     Prognosis, Biology, and Targeting of TP53 Dysregulation in Multiple
            Myeloma
  JOURNAL   Cells 9 (2), 287 (2020)
   PUBMED   31991614
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Barnoud,T., Parris,J.L.D. and Murphy,M.E.
  TITLE     Common genetic variants in the TP53 pathway and their impact on
            cancer
  JOURNAL   J Mol Cell Biol 11 (7), 578-585 (2019)
   PUBMED   31152665
  REMARK    GeneRIF: Common genetic variants in the TP53 pathway and their
            impact on cancer.
            Review article
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Hu,W., Chen,S., Thorne,R.F. and Wu,M.
  TITLE     TP53, TP53 Target Genes (DRAM, TIGAR), and Autophagy
  JOURNAL   Adv Exp Med Biol 1206, 127-149 (2019)
   PUBMED   31776983
  REMARK    Review article
REFERENCE   5  (residues 1 to 354)
  AUTHORS   Baugh,E.H., Ke,H., Levine,A.J., Bonneau,R.A. and Chan,C.S.
  TITLE     Why are there hotspot mutations in the TP53 gene in human cancers?
  JOURNAL   Cell Death Differ 25 (1), 154-160 (2018)
   PUBMED   29099487
  REMARK    GeneRIF: TP53 missense mutant alleles that occur in human cancers
            are discussed in the context of high resolution models of these p53
            mutant protein structures to determine the structural features of
            mutations (review).
            Review article
REFERENCE   6  (residues 1 to 354)
  AUTHORS   Aubrey,B.J., Strasser,A. and Kelly,G.L.
  TITLE     Tumor-Suppressor Functions of the TP53 Pathway
  JOURNAL   Cold Spring Harb Perspect Med 6 (5), a026062 (2016)
   PUBMED   27141080
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 354)
  AUTHORS   Soussi,T. and Wiman,K.G.
  TITLE     TP53: an oncogene in disguise
  JOURNAL   Cell Death Differ 22 (8), 1239-1249 (2015)
   PUBMED   26024390
  REMARK    Review article
REFERENCE   8  (residues 1 to 354)
  AUTHORS   Soussi,T.
  TITLE     The TP53 gene network in a postgenomic era
  JOURNAL   Hum Mutat 35 (6), 641-642 (2014)
   PUBMED   24753184
  REMARK    GeneRIF: Recommendations and guidelines for reporting and
            annotating TP53 variants are also provided, to help researchers
            generate standardized data that are easy to understand, analyze,
            and exchange across various cancer variant databases
            Review article
REFERENCE   9  (residues 1 to 354)
  AUTHORS   Anczukow,O., Ware,M.D., Buisson,M., Zetoune,A.B.,
            Stoppa-Lyonnet,D., Sinilnikova,O.M. and Mazoyer,S.
  TITLE     Does the nonsense-mediated mRNA decay mechanism prevent the
            synthesis of truncated BRCA1, CHK2, and p53 proteins?
  JOURNAL   Hum Mutat 29 (1), 65-73 (2008)
   PUBMED   17694537
  REMARK    GeneRIF: the p53 protein encoded by the 770delT allele is as
            abundant as the wild-type protein, as removal of the C-terminal p53
            domain leads to a stabilized mutant protein, whose abundance is
            markedly increased when NMD is inhibited.
REFERENCE   10 (residues 1 to 354)
  AUTHORS   Bourdon,J.C.
  TITLE     p53 Family isoforms
  JOURNAL   Curr Pharm Biotechnol 8 (6), 332-336 (2007)
   PUBMED   18289041
  REMARK    Review article
REFERENCE   11 (residues 1 to 354)
  AUTHORS   Candeias,M.M., Powell,D.J., Roubalova,E., Apcher,S., Bourougaa,K.,
            Vojtesek,B., Bruzzoni-Giovanelli,H. and Fahraeus,R.
  TITLE     Expression of p53 and p53/47 are controlled by alternative
            mechanisms of messenger RNA translation initiation
  JOURNAL   Oncogene 25 (52), 6936-6947 (2006)
   PUBMED   16983332
  REMARK    GeneRIF: harbouring alternative translation initiation sites, the
            p53 mRNA gives rise to different levels of the p53 isoforms which
            help to orchestrate the cell biological outcome of p53 activation
REFERENCE   12 (residues 1 to 354)
  AUTHORS   Murray-Zmijewski,F., Lane,D.P. and Bourdon,J.C.
  TITLE     p53/p63/p73 isoforms: an orchestra of isoforms to harmonise cell
            differentiation and response to stress
  JOURNAL   Cell Death Differ 13 (6), 962-972 (2006)
   PUBMED   16601753
  REMARK    Review article
REFERENCE   13 (residues 1 to 354)
  AUTHORS   Bourdon,J.C., Fernandes,K., Murray-Zmijewski,F., Liu,G., Diot,A.,
            Xirodimas,D.P., Saville,M.K. and Lane,D.P.
  TITLE     p53 isoforms can regulate p53 transcriptional activity
  JOURNAL   Genes Dev 19 (18), 2122-2137 (2005)
   PUBMED   16131611
  REMARK    GeneRIF: p53 isoforms can regulate p53 transcriptional activity.
REFERENCE   14 (residues 1 to 354)
  AUTHORS   Ghosh,A., Stewart,D. and Matlashewski,G.
  TITLE     Regulation of human p53 activity and cell localization by
            alternative splicing
  JOURNAL   Mol Cell Biol 24 (18), 7987-7997 (2004)
   PUBMED   15340061
  REMARK    GeneRIF: mechanism of p53 regulation originating through
            alternative splicing of the human p53 gene resulting in the
            expression of a novel p53 mRNA
REFERENCE   15 (residues 1 to 354)
  AUTHORS   Flaman,J.M., Waridel,F., Estreicher,A., Vannier,A., Limacher,J.M.,
            Gilbert,D., Iggo,R. and Frebourg,T.
  TITLE     The human tumour suppressor gene p53 is alternatively spliced in
            normal cells
  JOURNAL   Oncogene 12 (4), 813-818 (1996)
   PUBMED   8632903
REFERENCE   16 (residues 1 to 354)
  AUTHORS   Schneider,K., Zelley,K., Nichols,K.E., Schwartz Levine,A. and
            Garber,J.
  TITLE     Li-Fraumeni Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301488
REFERENCE   17 (residues 1 to 354)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   18 (residues 1 to 354)
  AUTHORS   Lamb,P. and Crawford,L.
  TITLE     Characterization of the human p53 gene
  JOURNAL   Mol Cell Biol 6 (5), 1379-1385 (1986)
   PUBMED   2946935
REFERENCE   19 (residues 1 to 354)
  AUTHORS   Isobe,M., Emanuel,B.S., Givol,D., Oren,M. and Croce,C.M.
  TITLE     Localization of gene for human p53 tumour antigen to band 17p13
  JOURNAL   Nature 320 (6057), 84-85 (1986)
   PUBMED   3456488
REFERENCE   20 (residues 1 to 354)
  AUTHORS   Benchimol,S., Lamb,P., Crawford,L.V., Sheer,D., Shows,T.B.,
            Bruns,G.A. and Peacock,J.
  TITLE     Transformation associated p53 protein is encoded by a gene on human
            chromosome 17
  JOURNAL   Somat Cell Mol Genet 11 (5), 505-510 (1985)
   PUBMED   2994241
REFERENCE   21 (residues 1 to 354)
  AUTHORS   Harlow,E., Williamson,N.M., Ralston,R., Helfman,D.M. and Adams,T.E.
  TITLE     Molecular cloning and in vitro expression of a cDNA clone for human
            cellular tumor antigen p53
  JOURNAL   Mol Cell Biol 5 (7), 1601-1610 (1985)
   PUBMED   3894933
REFERENCE   22 (residues 1 to 354)
  AUTHORS   Zakut-Houri,R., Bienz-Tadmor,B., Givol,D. and Oren,M.
  TITLE     Human p53 cellular tumor antigen: cDNA sequence and expression in
            COS cells
  JOURNAL   EMBO J 4 (5), 1251-1255 (1985)
   PUBMED   4006916
REFERENCE   23 (residues 1 to 354)
  AUTHORS   Matlashewski,G., Lamb,P., Pim,D., Peacock,J., Crawford,L. and
            Benchimol,S.
  TITLE     Isolation and characterization of a human p53 cDNA clone:
            expression of the human p53 gene
  JOURNAL   EMBO J 3 (13), 3257-3262 (1984)
   PUBMED   6396087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087388.9 and AC007421.13.
            
            Summary: This gene encodes a tumor suppressor protein containing
            transcriptional activation, DNA binding, and oligomerization
            domains. The encoded protein responds to diverse cellular stresses
            to regulate expression of target genes, thereby inducing cell cycle
            arrest, apoptosis, senescence, DNA repair, or changes in
            metabolism. Mutations in this gene are associated with a variety of
            human cancers, including hereditary cancers such as Li-Fraumeni
            syndrome. Alternative splicing of this gene and the use of
            alternate promoters result in multiple transcript variants and
            isoforms. Additional isoforms have also been shown to result from
            the use of alternate translation initiation codons from identical
            transcript variants (PMIDs: 12032546, 20937277). [provided by
            RefSeq, Dec 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.139836.1,
                                           SRR14038195.336928.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:2946935)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..354
                     /product="cellular tumor antigen p53 isoform g"
                     /note="tumor protein 53; mutant tumor protein 53; cellular
                     tumor antigen p53; phosphoprotein p53;
                     transformation-related protein 53; antigen NY-CO-13; tumor
                     supressor p53"
                     /calculated_mol_wt=39189
     Region          1..20
                     /region_name="TAD2"
                     /note="Transactivation domain 2; pfam18521"
                     /db_xref="CDD:375947"
     Region          70..249
                     /region_name="P53"
                     /note="P53 DNA-binding domain; cd08367"
                     /db_xref="CDD:176262"
     Site            order(137,140,199,203)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:176262"
     Site            order(138..140,142)
                     /site_type="other"
                     /note="dimerization site [polypeptide binding]"
                     /db_xref="CDD:176262"
     Site            order(200,202,209,234,236..238,241)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176262"
     Region          280..319
                     /region_name="P53_tetramer"
                     /note="P53 tetramerization motif; pfam07710"
                     /db_xref="CDD:462238"
     CDS             1..354
                     /gene="TP53"
                     /gene_synonym="BCC7; BMFS5; LFS1; P53; TRP53"
                     /coded_by="NM_001407267.1:273..1337"
                     /note="isoform g is encoded by transcript variant 11"
                     /db_xref="GeneID:7157"
                     /db_xref="HGNC:HGNC:11998"
                     /db_xref="MIM:191170"
ORIGIN      
        1 mddlmlspdd ieqwftedpg pdeaprmpea appvapapaa ptpaapapap swplsssvps
       61 qktyqgsygf rlgflhsgta ksvtctyspa lnkmfcqlak tcpvqlwvds tpppgtrvra
      121 maiykqsqhm tevvrrcphh ercsdsdgla ppqhlirveg nlrveylddr ntfrhsvvvp
      181 yeppevgsdc ttihynymcn sscmggmnrr piltiitled ssgnllgrns fevrvcacpg
      241 rdrrteeenl rkkgephhel ppgstkralp nntssspqpk kkpldgeyft lqirgrerfe
      301 mfrelneale lkdaqagkep ggsrahsshl kskkgqstsr hkklmfkteg pdsd
//
LOCUS       NP_001277007             976 aa            linear   PRI 21-NOV-2025
DEFINITION  angiopoietin-1 receptor isoform 3 precursor [Homo sapiens].
ACCESSION   NP_001277007
VERSION     NP_001277007.2
DBSOURCE    REFSEQ: accession NM_001290078.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 976)
  AUTHORS   Chacon-Camacho,O.F., Ordaz-Robles,T., Cid-Garcia,M.A.,
            Hofmann-Blancas,M.E., Ledesma-Gil,J., Garcia-Huerta,M.M.,
            Prado-Larrea,C., Cortes-Gonzalez,V., Lozano-Garza,R.I.,
            Garcia-Vega,D., Kim,J., Khang,R., Lee,E. and Zenteno,J.C.
  TITLE     TEK gene-related primary congenital glaucoma: Phenotypic features
            and mutational spectrum in a Mexican cohort of 10 unrelated
            families
  JOURNAL   Am J Med Genet A 194 (10), e63716 (2024)
   PUBMED   38847211
  REMARK    GeneRIF: TEK gene-related primary congenital glaucoma: Phenotypic
            features and mutational spectrum in a Mexican cohort of 10
            unrelated families.
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Yu,J., Brelen,M.E., Chan,C.K.M., Chen,Z.J., Mohamed,S., Yam,J.C.,
            Lam,D.S.C., Pang,C.P., Tham,C.C. and Chen,L.J.
  TITLE     Genetic association of TIE2 with diabetic retinopathy and diabetic
            macular edema
  JOURNAL   Asia Pac J Ophthalmol (Phila) 13 (3), 100068 (2024)
   PUBMED   38750959
  REMARK    GeneRIF: Genetic association of TIE2 with diabetic retinopathy and
            diabetic macular edema.
REFERENCE   3  (residues 1 to 976)
  AUTHORS   Jin,P., Zhang,J., Sumariwalla,P.F., Ni,I., Jorgensen,B.,
            Crawford,D., Phillips,S., Feldmann,M., Shepard,H.M. and
            Paleolog,E.M.
  TITLE     Novel splice variants derived from the receptor tyrosine kinase
            superfamily are potential therapeutics for rheumatoid arthritis
  JOURNAL   Arthritis Res Ther 10 (4), R73 (2008)
   PUBMED   18593464
REFERENCE   4  (residues 1 to 976)
  AUTHORS   Park,E.H., Lee,J.M. and Pelletier,J.
  TITLE     The Tie2 5' untranslated region is inhibitory to 5' end-mediated
            translation initiation
  JOURNAL   FEBS Lett 580 (5), 1309-1319 (2006)
   PUBMED   16457819
  REMARK    GeneRIF: the uORFs within the Tie2 5' UTR serve to decrease the
            percent of ribosomes competent for reinitiation as these traverse
            the mRNA 5' UTR, thus minimizing interference with the internal
            ribosome entry site
REFERENCE   5  (residues 1 to 976)
  AUTHORS   Park,E.H., Lee,J.M., Blais,J.D., Bell,J.C. and Pelletier,J.
  TITLE     Internal translation initiation mediated by the angiogenic factor
            Tie2
  JOURNAL   J Biol Chem 280 (22), 20945-20953 (2005)
   PUBMED   15802272
  REMARK    GeneRIF: Tie2 mediates internal translation initiation
REFERENCE   6  (residues 1 to 976)
  AUTHORS   Huang,L., Turck,C.W., Rao,P. and Peters,K.G.
  TITLE     GRB2 and SH-PTP2: potentially important endothelial signaling
            molecules downstream of the TEK/TIE2 receptor tyrosine kinase
  JOURNAL   Oncogene 11 (10), 2097-2103 (1995)
   PUBMED   7478529
REFERENCE   7  (residues 1 to 976)
  AUTHORS   Dumont,D.J., Anderson,L., Breitman,M.L. and Duncan,A.M.
  TITLE     Assignment of the endothelial-specific protein receptor tyrosine
            kinase gene (TEK) to human chromosome 9p21
  JOURNAL   Genomics 23 (2), 512-513 (1994)
   PUBMED   7835909
REFERENCE   8  (residues 1 to 976)
  AUTHORS   Seront,E., Boon,L.M. and Vikkula,M.
  TITLE     TEK-Related Venous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301733
REFERENCE   9  (residues 1 to 976)
  AUTHORS   Abu-Amero,K.K. and Edward,D.P.
  TITLE     Primary Congenital Glaucoma
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301314
REFERENCE   10 (residues 1 to 976)
  AUTHORS   Partanen,J., Armstrong,E., Makela,T.P., Korhonen,J., Sandberg,M.,
            Renkonen,R., Knuutila,S., Huebner,K. and Alitalo,K.
  TITLE     A novel endothelial cell surface receptor tyrosine kinase with
            extracellular epidermal growth factor homology domains
  JOURNAL   Mol Cell Biol 12 (4), 1698-1707 (1992)
   PUBMED   1312667
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355432.7, AL355433.6 and
            AL133411.9.
            
            On Dec 12, 2023 this sequence version replaced NP_001277007.1.
            
            Summary: This gene encodes a receptor that belongs to the protein
            tyrosine kinase Tie2 family. The encoded protein possesses a unique
            extracellular region that contains two immunoglobulin-like domains,
            three epidermal growth factor (EGF)-like domains and three
            fibronectin type III repeats. The ligand angiopoietin-1 binds to
            this receptor and mediates a signaling pathway that functions in
            embryonic vascular development. Mutations in this gene are
            associated with inherited venous malformations of the skin and
            mucous membranes. Alternative splicing results in multiple
            transcript variants. Additional alternatively spliced transcript
            variants of this gene have been described, but their full-length
            nature is not known. [provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (3) lacks two alternate in-frame
            exons and uses an alternate in-frame splice site in the coding
            region compared to variant 1. The encoded isoform (3) is shorter
            than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK294887.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153031 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            regulatory uORF :: PMID: 16457819
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.2"
     Protein         1..976
                     /product="angiopoietin-1 receptor isoform 3 precursor"
                     /EC_number="2.7.10.1"
                     /note="angiopoietin-1 receptor; tyrosine-protein kinase
                     receptor TEK; tunica interna endothelial cell kinase;
                     tyrosine-protein kinase receptor TIE-2; endothelial
                     tyrosine kinase; tyrosine kinase with Ig and EGF homology
                     domains-2; TEK tyrosine kinase, endothelial"
                     /calculated_mol_wt=106536
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2623
     mat_peptide     27..976
                     /product="angiopoietin-1 receptor isoform 3"
                     /calculated_mol_wt=106536
     Region          126..171
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domain;
                     laminins are the major noncollagenous components of
                     basement membranes that mediate cell adhesion, growth
                     migration, and differentiation; the laminin-type epidermal
                     growth factor-like module occurs in...; cd00055"
                     /db_xref="CDD:238012"
     Region          201..292
                     /region_name="IgI_Tie2"
                     /note="Immunoglobulin domain of Tie2 tyrosine kinase; a
                     member of the I-set of IgSF domains; cd20964"
                     /db_xref="CDD:409556"
     Region          201..205
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409556"
     Region          211..215
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409556"
     Region          218..227
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409556"
     Region          235..240
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409556"
     Region          244..246
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409556"
     Region          250..254
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409556"
     Region          257..265
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409556"
     Region          273..281
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409556"
     Region          284..292
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409556"
     Region          298..373
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Region          397..479
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(475..476,478..479)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          492..584
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(492,557,572)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(573..574,576..577)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          668..970
                     /region_name="PTKc_Tie2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Tie2; cd05088"
                     /db_xref="CDD:133219"
     Site            order(682..686,690,705,707,724,728,731,738,754..757,
                     760..761,812,814,816,820..821,823,832..835,849..853,862,
                     896)
                     /site_type="active"
                     /db_xref="CDD:133219"
     Site            order(682..683,685..686,690,705,707,724,728,738,754..757,
                     760..761,820..821,823,834)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:133219"
     Site            order(816,820,849..853,862,896)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133219"
     Site            833..855
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:133219"
     CDS             1..976
                     /gene="TEK"
                     /gene_synonym="CD202B; GLC3E; TIE-2; TIE2; VMCM; VMCM1"
                     /coded_by="NM_001290078.2:367..3297"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS78389.1"
                     /db_xref="GeneID:7010"
                     /db_xref="HGNC:HGNC:11724"
                     /db_xref="MIM:600221"
ORIGIN      
        1 mdslaslvlc gvslllsasf lpatltmtvd kgdnvnisfk kvlikeedav iykngsfihs
       61 vprhevpdil evhlphaqpq dagvysaryi ggnlftsaft rlivrrceaq kwgpecnhlc
      121 tacmnngvch edtgecicpp gfmgrtceka celhtfgrtc kercsgqegc ksyvfclpdp
      181 ygcscatgwk glqcnegiqr mtpkivdlpd hievnsgkfn pickasgwpl ptneemtlvk
      241 pdgtvlhpkd fnhtdhfsva iftihrilpp dsgvwvcsvn tvagmvekpf nisvkvlpkp
      301 lnapnvidtg hnfaviniss epyfgdgpik skkllykpvn hyeawqhiqv tneivtlnyl
      361 eprteyelcv qlvrrgegge ghpgpvrrft tasiglpppr glnllpksqt tlnltwqpif
      421 psseddfyve verrsvqksd qqnikvpgnl tsvllnnlhp reqyvvrarv ntkaqgewse
      481 dltawtlsdi lppqpeniki snithssavi swtildgysi ssitirykvq gknedqhvdv
      541 kiknatitqy qlkglepeta yqvdifaenn igssnpafsh elvtlpesqa padlgggkml
      601 liailgsagm tcltvllafl iilqlkranv qrrmaqafqn reepavqfns gtlalnrkvk
      661 nnpdptiypv ldwndikfqd vigegnfgqv lkarikkdgl rmdaaikrmk eyaskddhrd
      721 fagelevlck lghhpniinl lgacehrgyl ylaieyaphg nlldflrksr vletdpafai
      781 anstastlss qqllhfaadv argmdylsqk qfihrdlaar nilvgenyva kiadfglsrg
      841 qevyvkktmg rlpvrwmaie slnysvyttn sdvwsygvll weivslggtp ycgmtcaely
      901 eklpqgyrle kplncddevy dlmrqcwrek pyerpsfaqi lvslnrmlee rktyvnttly
      961 ekftyagidc saeeaa
//
LOCUS       NP_001400599             327 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 5 [Homo sapiens].
ACCESSION   NP_001400599
VERSION     NP_001400599.1
DBSOURCE    REFSEQ: accession NM_001413670.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 327)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 327)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 327)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..327
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 5"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=37306
     Region          34..322
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     CDS             1..327
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413670.1:134..1117"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mlyrlvtnsw alvihptrpp kvlglqnlla ekveqlmews srrsifrmng dkfrkfikap
       61 prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss afcnklffsm vdydegtdvf
      121 qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak wiadrtdvhi rvfrppnysg
      181 tialallvsl vggllylrrn nlefiynktg wamvslcivf amtsgqmwnh irgppyahkn
      241 phngqvsyih gssqaqfvae shiilvlnaa itmgmvllne aatskgdvgk rriiclvglg
      301 lvvfffsfll sifrskyhgy pysflik
//
LOCUS       NP_001428165            1593 aa            linear   PRI 21-NOV-2025
DEFINITION  THO complex subunit 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001428165 XP_047298232 XP_054183406
VERSION     NP_001428165.1
DBSOURCE    REFSEQ: accession NM_001441236.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1593)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1593)
  AUTHORS   Zhou,X., Liu,X., Zhang,G., Zhang,Q., Chen,H., Wang,Y., Fang,F. and
            Sun,J.
  TITLE     Knockdown THOC2 suppresses the proliferation and invasion of
            melanoma
  JOURNAL   Bioengineered 10 (1), 635-645 (2019)
   PUBMED   31680623
  REMARK    GeneRIF: THOC2 reduction repressed melanoma cell proliferation and
            invasion, and induced cell apoptosis.
REFERENCE   3  (residues 1 to 1593)
  AUTHORS   Kumar,R., Gardner,A., Homan,C.C., Douglas,E., Mefford,H.,
            Wieczorek,D., Ludecke,H.J., Stark,Z., Sadedin,S., Nowak,C.B.,
            Douglas,J., Parsons,G., Mark,P., Loidi,L., Herman,G.E., Mihalic
            Mosher,T., Gillespie,M.K., Brady,L., Tarnopolsky,M., Madrigal,I.,
            Eiris,J., Domenech Salgado,L., Rabionet,R., Strom,T.M.,
            Ishihara,N., Inagaki,H., Kurahashi,H., Dudding-Byth,T.,
            Palmer,E.E., Field,M. and Gecz,J.
  CONSRTM   Broad CMG
  TITLE     Severe neurocognitive and growth disorders due to variation in
            THOC2, an essential component of nuclear mRNA export machinery
  JOURNAL   Hum Mutat 39 (8), 1126-1138 (2018)
   PUBMED   29851191
  REMARK    GeneRIF: Study presents detailed clinical assessment and functional
            studies on a de novo variant in a female with an epileptic
            encephalopathy and discuss an additional four families with rare
            variants in THOC2 with supportive evidence for pathogenicity.
REFERENCE   4  (residues 1 to 1593)
  AUTHORS   Kumar,R., Corbett,M.A., van Bon,B.W., Woenig,J.A., Weir,L.,
            Douglas,E., Friend,K.L., Gardner,A., Shaw,M., Jolly,L.A., Tan,C.,
            Hunter,M.F., Hackett,A., Field,M., Palmer,E.E., Leffler,M.,
            Rogers,C., Boyle,J., Bienek,M., Jensen,C., Van Buggenhout,G., Van
            Esch,H., Hoffmann,K., Raynaud,M., Zhao,H., Reed,R., Hu,H.,
            Haas,S.A., Haan,E., Kalscheuer,V.M. and Gecz,J.
  TITLE     THOC2 Mutations Implicate mRNA-Export Pathway in X-Linked
            Intellectual Disability
  JOURNAL   Am J Hum Genet 97 (2), 302-310 (2015)
   PUBMED   26166480
  REMARK    GeneRIF: THOC2 mutations implicate mRNA-export pathway in X-linked
            intellectual disability.
REFERENCE   5  (residues 1 to 1593)
  AUTHORS   Grolimund,L., Aeby,E., Hamelin,R., Armand,F., Chiappe,D.,
            Moniatte,M. and Lingner,J.
  TITLE     A quantitative telomeric chromatin isolation protocol identifies
            different telomeric states
  JOURNAL   Nat Commun 4, 2848 (2013)
   PUBMED   24270157
REFERENCE   6  (residues 1 to 1593)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   7  (residues 1 to 1593)
  AUTHORS   Strasser,K., Masuda,S., Mason,P., Pfannstiel,J., Oppizzi,M.,
            Rodriguez-Navarro,S., Rondon,A.G., Aguilera,A., Struhl,K., Reed,R.
            and Hurt,E.
  TITLE     TREX is a conserved complex coupling transcription with messenger
            RNA export
  JOURNAL   Nature 417 (6886), 304-308 (2002)
   PUBMED   11979277
REFERENCE   8  (residues 1 to 1593)
  AUTHORS   Coffey,A.J., Brooksbank,R.A., Brandau,O., Oohashi,T., Howell,G.R.,
            Bye,J.M., Cahn,A.P., Durham,J., Heath,P., Wray,P., Pavitt,R.,
            Wilkinson,J., Leversha,M., Huckle,E., Shaw-Smith,C.J., Dunham,A.,
            Rhodes,S., Schuster,V., Porta,G., Yin,L., Serafini,P., Sylla,B.,
            Zollo,M., Franco,B., Bolino,A., Seri,M., Lanyi,A., Davis,J.R.,
            Webster,D., Harris,A., Lenoir,G., de St Basile,G., Jones,A.,
            Behloradsky,B.H., Achatz,H., Murken,J., Fassler,R., Sumegi,J.,
            Romeo,G., Vaudin,M., Ross,M.T., Meindl,A. and Bentley,D.R.
  TITLE     Host response to EBV infection in X-linked lymphoproliferative
            disease results from mutations in an SH2-domain encoding gene
  JOURNAL   Nat Genet 20 (2), 129-135 (1998)
   PUBMED   9771704
REFERENCE   9  (residues 1 to 1593)
  AUTHORS   Gu,X.X., Decorte,R., Marynen,P., Fryns,J.P., Cassiman,J.J. and
            Raeymaekers,P.
  TITLE     Localisation of a new gene for non-specific mental retardation to
            Xq22-q26 (MRX35)
  JOURNAL   J Med Genet 33 (1), 52-55 (1996)
   PUBMED   8825049
REFERENCE   10 (residues 1 to 1593)
  AUTHORS   Mulley,J.C., Kerr,B., Stevenson,R. and Lubs,H.
  TITLE     Nomenclature guidelines for X-linked mental retardation
  JOURNAL   Am J Med Genet 43 (1-2), 383-391 (1992)
   PUBMED   1605216
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL023575.1, Z82901.1 and
            AL030996.1.
            
            On or before Jun 5, 2025 this sequence version replaced
            XP_047298232.1, XP_054183406.1.
            
            Summary: The TREX multiprotein complex binds specifically to
            spliced mRNAs to facilitate mRNA export. The protein encoded by
            this gene is a member of the THO complex, a subset of the TREX
            complex. The encoded protein interacts with the THOC1
            protein.[provided by RefSeq, Jun 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1961588.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1593
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..1593
                     /product="THO complex subunit 2 isoform 1"
                     /note="THO complex 2"
                     /calculated_mol_wt=182644
     Region          1..163
                     /region_name="Anchor domain, interaction with THOC5 and
                     THOC7. /evidence=ECO:0000269|PubMed:33191911,
                     ECO:0007744|PDB:7APK"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          11..566
                     /region_name="THOC2_N"
                     /note="THO complex subunit 2 N-terminus; pfam16134"
                     /db_xref="CDD:465032"
     Region          164..534
                     /region_name="Bow domain, interaction with THOC1 dock
                     domain and THOC3. /evidence=ECO:0000269|PubMed:33191911,
                     ECO:0007744|PDB:7APK"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          322..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          535..686
                     /region_name="MIF4G domain, interaction with THOC3 and
                     DDX39B. /evidence=ECO:0000269|PubMed:33191911,
                     ECO:0007744|PDB:7APK"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          568..642
                     /region_name="Thoc2"
                     /note="Transcription- and export-related complex subunit;
                     pfam11732"
                     /db_xref="CDD:463334"
     Region          687..1174
                     /region_name="Stern domain.
                     /evidence=ECO:0000269|PubMed:33191911"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          874..1173
                     /region_name="Tho2"
                     /note="Transcription factor/nuclear export subunit protein
                     2; pfam11262"
                     /db_xref="CDD:463251"
     Region          923..928
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          1175..1593
                     /region_name="Charged domain.
                     /evidence=ECO:0000269|PubMed:33191911"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          1184..1593
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B1AZI6; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          <1291..1593
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            1385
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1443
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          1448..>1556
                     /region_name="U2AF_lg"
                     /note="U2 snRNP auxilliary factor, large subunit, splicing
                     factor; TIGR01642"
                     /db_xref="CDD:273727"
     Site            1450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     CDS             1..1593
                     /gene="THOC2"
                     /gene_synonym="AMC7; CXorf3; dJ506G2.1; hTREX120; MRX12;
                     MRX35; THO2; XLID12"
                     /coded_by="NM_001441236.1:31..4812"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:57187"
                     /db_xref="HGNC:HGNC:19073"
                     /db_xref="MIM:300395"
ORIGIN      
        1 maaaavvvpa ewiknweksg rgeflhlcri lsenkshdss tyrdfqqaly elsyhvikgn
       61 lkheqasnvl sdisefredm psiladvfci ldietnclee kskrdyftql vlaclylvsd
      121 tvlkerldpe tleslglikq sqqfnqksvk iktklfykqq kfnllreene gyakliaelg
      181 qdlsgsitsd lileniksli gcfnldpnrv ldvilevfec rpehddffis llesymsmce
      241 pqtlchilgf kfkfyqepng etpsslyrva avllqfnlid lddlyvhllp adncimdehk
      301 reiaeakqiv rkltmvvlss ekmderekek ekeeekvekp pdnqklglle allkigdwqh
      361 aqnimdqmpp yyaashklia laicklihit ieplyrrvgv pkgakgspvn alqnkrapkq
      421 aesfedlrrd vfnmfcylgp hlshdpilfa kvvrigksfm kefqsdgskq edkektevil
      481 scllsitdqv llpslslmdc nacmseelwg mfktfpyqhr yrlygqwkne tynshpllvk
      541 vkaqtidrak yimkrltken vkpsgrqigk lshsnptilf dyilsqiqky dnlitpvvds
      601 lkyltslnyd vlayciieal anpekermkh ddttisswlq slasfcgavf rkypidlagl
      661 lqyvanqlka gksfdllilk evvqkmagie iteemtmeql eamtggeqlk aeggyfgqir
      721 ntkkssqrlk dalldhdlal plcllmaqqr ngvifqegge khlklvgkly dqchdtlvqf
      781 ggflasnlst edyikrvpsi dvlcnefhtp hdaafflsrp myahhissky delkksekgs
      841 kqqhkvhkyi tscemvmapv heavvslhvs kvwddispqf yatfwsltmy dlavphtsye
      901 revnklkvqm kaiddnqemp pnkkkkeker ctalqdklle eekkqmehvq rvlqrlklek
      961 dnwllakstk netitkflql cifprcifsa idavycarfv elvhqqktpn fstllcydrv
     1021 fsdiiytvas cteneasryg rflccmletv trwhsdraty ekecgnypgf ltilratgfd
     1081 ggnkadqldy enfrhvvhkw hykltkasvh cletgeythi rnilivltki lpwypkvlnl
     1141 gqalerrvhk icqeekekrp dlyalamgys gqlksrksym ipenefhhkd ppprnavasv
     1201 qngpgggpss ssigsasksd essteetdks rersqcgvka vnkassttpk gnssngnsgs
     1261 nsnkavkend kekgkekeke kkektpattp earvlgkdgk ekpkeerpnk dekaretker
     1321 tpksdkekek fkkeekakde kfkttvpnae skstqerere kepsrerdia kemkskenvk
     1381 ggektpvsgs lkspvprsdi pepereqkrr kidthpspsh sstvkdslie lkessaklyi
     1441 nhtppplsks keremdkkdl dksrersrer ekkdekdrke rkrdhsnndr evppdltkrr
     1501 keengtmgvs khksespces pypnekdkek nkskssgkek gsdsfksekm dkissggkke
     1561 srhdkekiek kekrdssggk eekkhhkssd khr
//
LOCUS       NP_001426202             612 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA replication licensing factor MCM7 isoform 3 [Homo sapiens].
ACCESSION   NP_001426202
VERSION     NP_001426202.1
DBSOURCE    REFSEQ: accession NM_001439273.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Sun,Q., Sui,Y., Li,S., Zhou,R., Fu,Z., Luo,J. and Zhao,W.
  TITLE     RNF8-mediated multi-ubiquitination of MCM7: Linking disassembly of
            the CMG helicase with DNA damage response in human cells
  JOURNAL   Life Sci 353, 122912 (2024)
   PUBMED   39004272
  REMARK    GeneRIF: RNF8-mediated multi-ubiquitination of MCM7: Linking
            disassembly of the CMG helicase with DNA damage response in human
            cells.
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Wang,J., Amin,A., Cheung,M.H., Shi,L. and Liang,C.
  TITLE     Targeted inhibition of the expression of both MCM5 and MCM7 by
            miRNA-214 impedes DNA replication and tumorigenesis in
            hepatocellular carcinoma cells
  JOURNAL   Cancer Lett 539, 215677 (2022)
   PUBMED   35490917
  REMARK    GeneRIF: Targeted inhibition of the expression of both MCM5 and
            MCM7 by miRNA-214 impedes DNA replication and tumorigenesis in
            hepatocellular carcinoma cells.
REFERENCE   4  (residues 1 to 612)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 612)
  AUTHORS   Su,D.
  TITLE     MCM7 affects the cisplatin resistance of liver cancer cells and the
            development of liver cancer by regulating the PI3K/Akt signaling
            pathway
  JOURNAL   Immunopharmacol Immunotoxicol 44 (1), 17-27 (2022)
   PUBMED   34821526
  REMARK    GeneRIF: MCM7 affects the cisplatin resistance of liver cancer
            cells and the development of liver cancer by regulating the
            PI3K/Akt signaling pathway.
REFERENCE   6  (residues 1 to 612)
  AUTHORS   Suzuki,S., Adachi,A., Hiraiwa,A., Ohashi,M., Ishibashi,M. and
            Kiyono,T.
  TITLE     Cloning and characterization of human MCM7 promoter
  JOURNAL   Gene 216 (1), 85-91 (1998)
   PUBMED   9714754
REFERENCE   7  (residues 1 to 612)
  AUTHORS   Fujita,M., Kiyono,T., Hayashi,Y. and Ishibashi,M.
  TITLE     hCDC47, a human member of the MCM family. Dissociation of the
            nucleus-bound form during S phase
  JOURNAL   J Biol Chem 271 (8), 4349-4354 (1996)
   PUBMED   8626784
REFERENCE   8  (residues 1 to 612)
  AUTHORS   Musahl,C., Schulte,D., Burkhart,R. and Knippers,R.
  TITLE     A human homologue of the yeast replication protein Cdc21.
            Interactions with other Mcm proteins
  JOURNAL   Eur J Biochem 230 (3), 1096-1101 (1995)
   PUBMED   7601140
REFERENCE   9  (residues 1 to 612)
  AUTHORS   Nakatsuru,S., Sudo,K. and Nakamura,Y.
  TITLE     Isolation and mapping of a human gene (MCM2) encoding a product
            homologous to yeast proteins involved in DNA replication
  JOURNAL   Cytogenet Cell Genet 68 (3-4), 226-230 (1995)
   PUBMED   7842741
REFERENCE   10 (residues 1 to 612)
  AUTHORS   Hu,B., Burkhart,R., Schulte,D., Musahl,C. and Knippers,R.
  TITLE     The P1 family: a new class of nuclear mammalian proteins related to
            the yeast Mcm replication proteins
  JOURNAL   Nucleic Acids Res 21 (23), 5289-5293 (1993)
   PUBMED   8265339
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073842.5.
            
            Summary: The protein encoded by this gene is one of the highly
            conserved mini-chromosome maintenance proteins (MCM) that are
            essential for the initiation of eukaryotic genome replication. The
            hexameric protein complex formed by the MCM proteins is a key
            component of the pre-replication complex (pre_RC) and may be
            involved in the formation of replication forks and in the
            recruitment of other DNA replication related proteins. The MCM
            complex consisting of this protein and MCM2, 4 and 6 proteins
            possesses DNA helicase activity, and may act as a DNA unwinding
            enzyme. Cyclin D1-dependent kinase, CDK4, is found to associate
            with this protein, and may regulate the binding of this protein
            with the tumorsuppressor protein RB1/RB. Alternatively spliced
            transcript variants encoding distinct isoforms have been reported.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3379116.1,
                                           SRR1803616.109717.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..612
                     /product="DNA replication licensing factor MCM7 isoform 3"
                     /EC_number="3.6.4.12"
                     /note="minichromosome maintenance deficient 7; DNA
                     replication licensing factor MCM7; homolog of S.
                     cerevisiae Cdc47; CDC47 homolog; protein phosphatase 1,
                     regulatory subunit 104"
                     /calculated_mol_wt=68485
     Region          38..534
                     /region_name="MCM"
                     /note="minichromosome maintenance proteins; smart00350"
                     /db_xref="CDD:214631"
     Site            order(236,260..262,276,281..282,285,289,296,298,300,302,
                     305..306,313,316,319..320,322,324,331,339,342,345,349,
                     352..353,356,361..365,368..369,371..372,374,386..387,403,
                     406,416,418,420,423..424,427,430..431,434..435,437,449,
                     465..468,471,475,478..479,482..483,495..497,503)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:350664"
     Site            order(236..238,276..282,407,430,497)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350664"
     Site            order(305,364..365)
                     /site_type="other"
                     /note="nucleic acid binding site [nucleotide binding]"
                     /db_xref="CDD:350664"
     CDS             1..612
                     /gene="MCM7"
                     /gene_synonym="CDC47; MCM2; P1.1-MCM3; P1CDC47; P85MCM;
                     PNAS146; PPP1R104"
                     /coded_by="NM_001439273.1:502..2340"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="GeneID:4176"
                     /db_xref="HGNC:HGNC:6950"
                     /db_xref="MIM:600592"
ORIGIN      
        1 mmeqrsrdpg mvrspqnqyp aelmrrfely fqgpssnkpr virevradsv gklvtvrgiv
       61 trvsevkpkm vvatytcdqc gaetyqpiqs ptfmplimcp sqecqtnrsg grlylqtrgs
      121 rfikfqemkm qehsdqvpvg niprsitvlv egentriaqp gdhvsvtgif lpilrtgfrq
      181 vvqgllsety leahrivkmn kseddesgag eltreelrqi aeedfyekla asiapeiygh
      241 edvkkallll lvggvdqspr gmkirgnini clmgdpgvak sqllsyidrl aprsqyttgr
      301 gssgvgltaa vlrdsvsgel tleggalvla dqgvccidef dkmaeadrta ihevmeqqti
      361 siakagiltt lnarcsilaa anpaygrynp rrsleqniql paallsrfdl lwliqdrpdr
      421 dndlrlaqhi tyvhqhsrqp psqfepldmk lmrryiamcr ekqpmvpesl adyitaayve
      481 mrreawaskd atytsartll ailrlstala rlrmvdvvek edvneairlm emskdsllgd
      541 kgqtartqrp advifatvre lvsggrsvrf seaeqrcvsr gftpaqfqaa ldeyeelnvw
      601 qvnasrtrit fv
//
LOCUS       NP_001392805            1042 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 6 [Homo sapiens].
ACCESSION   NP_001392805 XP_047291755
VERSION     NP_001392805.1
DBSOURCE    REFSEQ: accession NM_001405876.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1042)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1042)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1042)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1042)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1042)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1042)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1042)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            On May 5, 2022 this sequence version replaced XP_047291755.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.1487963.1,
                                           ERR4643830.5416377.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1042
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 6"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=113587
     Site            104
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          145..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          225..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          399..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          822..942
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..1042
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405876.1:454..3582"
                     /note="isoform 6 is encoded by transcript variant 17"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankgli
      481 vlgevpppeh ttdlflplss evktdhgtdk liesvsqple nhgapiighi seslstkscg
      541 alrpvngvin tlqpvladhi pgdssdaeeq lhkkqrlnlv ssssdgtcva artrpvlsck
      601 krrlvrpnsi vplskkvhrn stirpgcdvn pscalcgsgs intmppeihy eapllerlsq
      661 ldscvhpvla fpddvptslh fqsmlksqwq nkpfdkikpp kklslkhrap mpgslpdsar
      721 kdrhklvssf lttamlkhht dmssssylaa thhpphsplv rqlstssdsp apassssqvt
      781 astsqqpvrr rrgessfdin nivipmsvaa ttrveklqyk eiltpswrev dlqslkgspd
      841 eeneeiedls daafaalhak ceemerarwl wttsvppqrr gsrsyrssdg rttpqlgsan
      901 pstpqpaspd vssshslsey shgqsprspi spelhsaplt pvardtprhl asedtrcstp
      961 elgldeqsvq pwerrtfpla hspqaecedq ldaqeraarc trrtsgsktg reteaaptsp
     1021 pivplksrhl vaaataqrpt hr
//
LOCUS       NP_001158287            1301 aa            linear   PRI 21-NOV-2025
DEFINITION  apoptotic chromatin condensation inducer in the nucleus isoform 3
            [Homo sapiens].
ACCESSION   NP_001158287
VERSION     NP_001158287.2
DBSOURCE    REFSEQ: accession NM_001164815.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1301)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1301)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1301)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1301)
  AUTHORS   Chen,Y.S., Liu,C.W., Lin,Y.C., Tsai,C.Y., Yang,C.H. and Lin,J.C.
  TITLE     The SRSF3-MBNL1-Acin1 circuit constitutes an emerging axis to
            lessen DNA fragmentation in colorectal cancer via an alternative
            splicing mechanism
  JOURNAL   Neoplasia 22 (12), 702-713 (2020)
   PUBMED   33142236
  REMARK    GeneRIF: The SRSF3-MBNL1-Acin1 circuit constitutes an emerging axis
            to lessen DNA fragmentation in colorectal cancer via an alternative
            splicing mechanism.
REFERENCE   5  (residues 1 to 1301)
  AUTHORS   Xue,L., Xie,L., Song,X. and Song,X.
  TITLE     [Expression and Significance of ACIN1 mRNA in Platelets of Lung
            Cancer]
  JOURNAL   Zhongguo Fei Ai Za Zhi 21 (9), 677-681 (2018)
   PUBMED   30201066
  REMARK    GeneRIF: ACIN1 mRNA was highly expressed in platelets of lung
            cancer patients
REFERENCE   6  (residues 1 to 1301)
  AUTHORS   Hu,Y., Yao,J., Liu,Z., Liu,X., Fu,H. and Ye,K.
  TITLE     Akt phosphorylates acinus and inhibits its proteolytic cleavage,
            preventing chromatin condensation
  JOURNAL   EMBO J 24 (20), 3543-3554 (2005)
   PUBMED   16177823
  REMARK    GeneRIF: Akt phosphorylation of acinus on serine 422 and 573
            results in its resistance to caspase cleavage in the nucleus and
            the inhibition of acinus-dependent chromatin condensation.
REFERENCE   7  (residues 1 to 1301)
  AUTHORS   Schwerk,C., Prasad,J., Degenhardt,K., Erdjument-Bromage,H.,
            White,E., Tempst,P., Kidd,V.J., Manley,J.L., Lahti,J.M. and
            Reinberg,D.
  TITLE     ASAP, a novel protein complex involved in RNA processing and
            apoptosis
  JOURNAL   Mol Cell Biol 23 (8), 2981-2990 (2003)
   PUBMED   12665594
REFERENCE   8  (residues 1 to 1301)
  AUTHORS   Sordet,O., Rebe,C., Plenchette,S., Zermati,Y., Hermine,O.,
            Vainchenker,W., Garrido,C., Solary,E. and Dubrez-Daloz,L.
  TITLE     Specific involvement of caspases in the differentiation of
            monocytes into macrophages
  JOURNAL   Blood 100 (13), 4446-4453 (2002)
   PUBMED   12393560
REFERENCE   9  (residues 1 to 1301)
  AUTHORS   Zermati,Y., Garrido,C., Amsellem,S., Fishelson,S., Bouscary,D.,
            Valensi,F., Varet,B., Solary,E. and Hermine,O.
  TITLE     Caspase activation is required for terminal erythroid
            differentiation
  JOURNAL   J Exp Med 193 (2), 247-254 (2001)
   PUBMED   11208865
REFERENCE   10 (residues 1 to 1301)
  AUTHORS   Sahara,S., Aoto,M., Eguchi,Y., Imamoto,N., Yoneda,Y. and
            Tsujimoto,Y.
  TITLE     Acinus is a caspase-3-activated protein required for apoptotic
            chromatin condensation
  JOURNAL   Nature 401 (6749), 168-173 (1999)
   PUBMED   10490026
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL117258.4 and AL132780.5.
            
            On Dec 12, 2023 this sequence version replaced NP_001158287.1.
            
            Summary: Apoptosis is defined by several morphologic nuclear
            changes, including chromatin condensation and nuclear
            fragmentation. This gene encodes a nuclear protein that induces
            apoptotic chromatin condensation after activation by caspase-3,
            without inducing DNA fragmentation. This protein has also been
            shown to be a component of a splicing-dependent multiprotein exon
            junction complex (EJC) that is deposited at splice junctions on
            mRNAs, as a consequence of pre-mRNA splicing. It may thus be
            involved in mRNA metabolism associated with splicing. Alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1. This results
            in a shorter protein (isoform 3), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3104862.1,
                                           SRR14038197.1631425.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1301
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..1301
                     /product="apoptotic chromatin condensation inducer in the
                     nucleus isoform 3"
                     /note="apoptotic chromatin condensation inducer in the
                     nucleus; functional spliceosome-associated protein 152"
                     /calculated_mol_wt=147232
     Region          72..106
                     /region_name="SAP"
                     /note="Putative DNA-binding (bihelical) motif predicted to
                     be involved in chromosomal organisation; smart00513"
                     /db_xref="CDD:128789"
     Region          <141..373
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          971..1057
                     /region_name="RRM_ACINU"
                     /note="RNA recognition motif (RRM) found in apoptotic
                     chromatin condensation inducer in the nucleus (acinus) and
                     similar proteins; cd12432"
                     /db_xref="CDD:409866"
     Region          <1166..1196
                     /region_name="RSB_motif"
                     /note="RNSP1-SAP18 binding (RSB) motif; pfam16294"
                     /db_xref="CDD:465085"
     CDS             1..1301
                     /gene="ACIN1"
                     /gene_synonym="ACINUS; ACN; fSAP152"
                     /coded_by="NM_001164815.2:186..4091"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS53889.1"
                     /db_xref="GeneID:22985"
                     /db_xref="HGNC:HGNC:17066"
                     /db_xref="MIM:604562"
ORIGIN      
        1 mwrrkhprts ggtrgvlsgn rgveygsgrg hlgtfegrwr klpkmpeavg tdpstsrkma
       61 eleevtldgk plqalrvtdl kaaleqrgla ksgqksalvk rlkgalmlen lqkhstphaa
      121 fqpnsqigee msqnsfikqy lekqqellrq rlereareaa elegksssis eekgdsddek
      181 prkgerrssr vrqaraakls egsqpaeeee dqetpsrnlr vradrnlkte eeeeeeeeee
      241 eddeeeegdd egqksreapi lkefkeegee iprvkpeemm derpktrsqe qevlerggrf
      301 trsqeearks hlarqqqeke mkttspleee ereikssqgl kekskspspp rltedrkkas
      361 lvalpeqtas eeetpppllt keassppphp qlhseeeiep megpapavli qlsppntdad
      421 trellvsqht vqlvgglspl sspsdtkaes paekvpeesv lplvqkstla dysaqkdlep
      481 esdrsaqplp lkieelalak giteeclkqp sleqkegrra shtllpshrl kqsadssssr
      541 sssssssssr srsrspdssg srshsplrsk qrdvaqarth anprgrpkmg srstsesrsr
      601 srsrsrsass nsrkslspgv srdsstsyte tkdpssgqev atppvpqlqv cepkertsts
      661 sssvqarrls qpesaekhvt qrlqpergsp kkceaeeaep paatqpqtse tqtshlpese
      721 rihhtveeke evtmdtsenr pendvpeppm piadqvsndd rpegsvedee kkesslpksf
      781 krkisvvsat kgvpagnsdt eggqpgrkrr wgastattqk kpsisittes lkslipdikp
      841 lagqeavvdl haddsrised eterngddgt hdkglkicrt vtqvvpaegq engqreeeee
      901 ekepeaeppv ppqvsveval pppaehevkk vtlgdtltrr sisqqksgvs itiddpvrta
      961 qvpspprgki snivhisnlv rpftlgqlke llgrtgtlve eafwidkiks hcfvtystve
     1021 eavatrtalh gvkwpqsnpk flcadyaeqd eldyhrgllv drpsetktee qgiprplhpp
     1081 ppppvqppqh praeqreqer avreqwaere remerrertr serewdrdkv regprsrsrs
     1141 rdrrrkerak skekksekke kaqeeppakl lddlfrktka apciywlplt dsqivqkeae
     1201 raerakerek rrkeqeeeeq kerekeaere rnrqlerekr rehsrerdre rerererdrg
     1261 drdrdrerdr ergrerdrrd tkrhsrsrsr stpvrdrggr r
//
LOCUS       NP_001393921             572 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform C [Homo sapiens].
ACCESSION   NP_001393921
VERSION     NP_001393921.1
DBSOURCE    REFSEQ: accession NM_001406992.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 572)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 572)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 572)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 572)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 572)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 572)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355388.30 and AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.132578.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154405, SAMEA2155550
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..572
                     /product="lamin isoform C"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=65004
     Region          1..130
                     /region_name="Interaction with MLIP.
                     /evidence=ECO:0000269|PubMed:21498514"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          1..33
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          30..386
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Site            32
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          34..70
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          71..80
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            78
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          81..218
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            108
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            114
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            123
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            135
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            155
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            171
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            180
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            201
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            208
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          219..242
                     /region_name="Linker 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          243..383
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          259..331
                     /region_name="Necessary and sufficient for the interaction
                     with IFFO1. /evidence=ECO:0000269|PubMed:31548606"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            265
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            266
                     /site_type="other"
                     /note="Heptad change of phase; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            270
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATR.
                     /evidence=ECO:0000269|PubMed:37832547; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            311
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            316
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            325
                     /site_type="other"
                     /note="Stutter. /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            330
                     /site_type="other"
                     /note="Heptad change of phase; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            341
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          384..442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:37788673,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATR.
                     /evidence=ECO:0000269|PubMed:37788673,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:24741066, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          417..422
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            417
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          434..541
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     Site            450
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            457
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            486
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48679; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48679; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            546
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     CDS             1..572
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406992.1:315..2033"
                     /note="isoform C is encoded by transcript variant 11"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 metpsqrrat rsgaqasstp lsptritrlq ekedlqelnd rlavyidrvr sletenaglr
       61 lriteseevv srevsgikaa yeaelgdark tldsvakera rlqlelskvr eefkelkarn
      121 tkkegdliaa qarlkdleal lnskeaalst alsekrtleg elhdlrgqva kleaalgeak
      181 kqlqdemlrr vdaenrlqtm keeldfqkni yseelretkr rhetrlveid ngkqrefesr
      241 ladalqelra qhedqveqyk kelektysak ldnarqsaer nsnlvgaahe elqqsririd
      301 slsaqlsqlq kqlaakeakl rdledslare rdtsrrllae keremaemra rmqqqldeyq
      361 elldiklald meihayrkll egeeerlrls psptsqrsrg rasshssqtq gggsvtkkrk
      421 lestesrssf sqhartsgrv aveevdeegk fvrlrnksne dqsmgnwqik rqngddpllt
      481 yrfppkftlk agqvvtiwaa gagathsppt dlvwkaqntw gcgnslrtal instgeevam
      541 rklvrsvtvv eddededgdd llhhhhvsgs rr
//
LOCUS       NP_001397748             872 aa            linear   PRI 21-NOV-2025
DEFINITION  MICAL-like protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001397748 XP_005261848
VERSION     NP_001397748.1
DBSOURCE    REFSEQ: accession NM_001410819.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 872)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 872)
  AUTHORS   Frisby,D., Murakonda,A.B., Ashraf,B., Dhawan,K., Almeida-Souza,L.,
            Naslavsky,N. and Caplan,S.
  TITLE     Endosomal actin branching, fission, and receptor recycling require
            FCHSD2 recruitment by MICAL-L1
  JOURNAL   Mol Biol Cell 35 (11), ar144 (2024)
   PUBMED   39382837
  REMARK    GeneRIF: Endosomal actin branching, fission, and receptor recycling
            require FCHSD2 recruitment by MICAL-L1.
REFERENCE   3  (residues 1 to 872)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 872)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 872)
  AUTHORS   Sikora,R., Bun,P., Danglot,L., Alqabandi,M., Bassereau,P.,
            Niedergang,F., Galli,T. and Zahraoui,A.
  TITLE     MICAL-L1 is required for cargo protein delivery to the cell surface
  JOURNAL   Biol Open 10 (6) (2021)
   PUBMED   34100897
  REMARK    GeneRIF: MICAL-L1 is required for cargo protein delivery to the
            cell surface.
REFERENCE   6  (residues 1 to 872)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 872)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   8  (residues 1 to 872)
  AUTHORS   Weide,T., Teuber,J., Bayer,M. and Barnekow,A.
  TITLE     MICAL-1 isoforms, novel rab1 interacting proteins
  JOURNAL   Biochem Biophys Res Commun 306 (1), 79-86 (2003)
   PUBMED   12788069
REFERENCE   9  (residues 1 to 872)
  AUTHORS   Terman,J.R., Mao,T., Pasterkamp,R.J., Yu,H.H. and Kolodkin,A.L.
  TITLE     MICALs, a family of conserved flavoprotein oxidoreductases,
            function in plexin-mediated axonal repulsion
  JOURNAL   Cell 109 (7), 887-900 (2002)
   PUBMED   12110185
REFERENCE   10 (residues 1 to 872)
  AUTHORS   Marzesco,A.M., Dunia,I., Pandjaitan,R., Recouvreur,M., Dauzonne,D.,
            Benedetti,E.L., Louvard,D. and Zahraoui,A.
  TITLE     The small GTPase Rab13 regulates assembly of functional tight
            junctions in epithelial cells
  JOURNAL   Mol Biol Cell 13 (6), 1819-1831 (2002)
   PUBMED   12058051
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL022311.5.
            
            On Aug 16, 2022 this sequence version replaced XP_005261848.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.284951.1,
                                           SRR14038196.755472.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..872
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..872
                     /product="MICAL-like protein 1 isoform 2"
                     /note="molecule interacting with Rab13; MICAL-like protein
                     1"
                     /calculated_mol_wt=94124
     Region          4..110
                     /region_name="CH_MICALL1"
                     /note="calponin homology (CH) domain found in MICAL-like
                     protein 1; cd21252"
                     /db_xref="CDD:409101"
     Site            order(4,8,58,60..61,64..65,67,76..84,92,94..95,97..98,
                     101..102,105)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409101"
     Region          119..162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Region          164..218
                     /region_name="LIM_Mical_like_1"
                     /note="This domain belongs to the LIM domain family which
                     are found on Mical (molecule interacting with CasL) like
                     proteins; cd09444"
                     /db_xref="CDD:188828"
     Site            order(164,167,185,188,191,194,214,217)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188828"
     Region          224..670
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Region          <246..667
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Region          425..427
                     /region_name="NPF1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            467
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            578
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Region          633..635
                     /region_name="NPF2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Region          687..808
                     /region_name="bMERB_dom"
                     /note="Bivalent Mical/EHBP Rab binding domain; pfam12130"
                     /db_xref="CDD:463467"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BGT6; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     CDS             1..872
                     /gene="MICALL1"
                     /gene_synonym="MICAL-L1; MIRAB13"
                     /coded_by="NM_001410819.1:127..2745"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS93163.1"
                     /db_xref="GeneID:85377"
                     /db_xref="HGNC:HGNC:29804"
                     /db_xref="MIM:619563"
ORIGIN      
        1 magprgalla wcrrqcegyr gveirdlsss frdglafcai lhrhrpdlld fdslskdnvf
       61 ennrlafeva ekelgipall dpndmvsmsv pdclsimtyv sqyynhfcsp gqagvspprk
      121 glapcsppsv aptpvepedv aqgeelssgs lseqgtgqtp sstcaacqqh vhlvqrylad
      181 grlyhrhcfr crrcsstllp gayengpeeg tfvcaehcar lgpgtrsgtr pgpfsqpkqq
      241 hqqqlaedak dvpgggpsss apagaeadgp kaspearpqi ptkprvpgkl qelasppagr
      301 ptpaprkase sttpapptpr prsslqqenl veqagssslv ngrlhelpvp kprgtpkpse
      361 gtpaprkdpp witlvqaepk kkpaplppss spgppsqdsr qvenggteev aqpsptasle
      421 skpynpfeee eedkeeeapa apslatspal ghpestpksl hpwygitpts spktkkrpap
      481 rapsasplal hasrlshsep psatpspals veslssesas qtagaellep pavpksssep
      541 avhapgtpgn pvslstnssl assgelvepr veqmpqaspg laprtrgssg pqpakpcsga
      601 tptplllvgd rspvpspgss spqlqvkssc kenpfnrkps paaspatkka tkgskpvrpp
      661 apghgfplik rkvqadqyip eedihgemdt ierrldaleh rgvlleeklr gglnegredd
      721 mlvdwfklih ekhllvrres eliyvfkqqn leqrqadvey elrcllnkpe kdwteedrar
      781 ekvlmqelvt lieqrnaiin cldedrqree eedkmleami kkkgealagd eaefqreaep
      841 egkkkgkfkt mkmlkllgnk rdaksksprd ks
//
LOCUS       NP_001424190             749 aa            linear   PRI 21-NOV-2025
DEFINITION  protein lin-54 homolog isoform a [Homo sapiens].
ACCESSION   NP_001424190 XP_005262807 XP_054204888
VERSION     NP_001424190.1
DBSOURCE    REFSEQ: accession NM_001437261.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 749)
  AUTHORS   Marceau,A.H., Felthousen,J.G., Goetsch,P.D., Iness,A.N., Lee,H.W.,
            Tripathi,S.M., Strome,S., Litovchick,L. and Rubin,S.M.
  TITLE     Structural basis for LIN54 recognition of CHR elements in cell
            cycle-regulated promoters
  JOURNAL   Nat Commun 7, 12301 (2016)
   PUBMED   27465258
  REMARK    GeneRIF: the DNA-binding properties of LIN54 and the structural
            basis for recognition of a cell cycle genes homology region
            sequence, are described.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 749)
  AUTHORS   Sadasivam,S. and DeCaprio,J.A.
  TITLE     The DREAM complex: master coordinator of cell cycle-dependent gene
            expression
  JOURNAL   Nat Rev Cancer 13 (8), 585-595 (2013)
   PUBMED   23842645
  REMARK    Review article
            Erratum:[Nat Rev Cancer. 2013 Oct;13(10):752]
REFERENCE   4  (residues 1 to 749)
  AUTHORS   Matsuo,T., Kuramoto,H., Kumazaki,T., Mitsui,Y. and Takahashi,T.
  TITLE     LIN54 harboring a mutation in CHC domain is localized to the
            cytoplasm and inhibits cell cycle progression
  JOURNAL   Cell Cycle 11 (17), 3227-3236 (2012)
   PUBMED   22895175
  REMARK    GeneRIF: LIN54 harboring a mutation in CHC domain is localized to
            the cytoplasm and inhibits cell cycle progression.
REFERENCE   5  (residues 1 to 749)
  AUTHORS   Sadasivam,S., Duan,S. and DeCaprio,J.A.
  TITLE     The MuvB complex sequentially recruits B-Myb and FoxM1 to promote
            mitotic gene expression
  JOURNAL   Genes Dev 26 (5), 474-489 (2012)
   PUBMED   22391450
REFERENCE   6  (residues 1 to 749)
  AUTHORS   Litovchick,L., Florens,L.A., Swanson,S.K., Washburn,M.P. and
            DeCaprio,J.A.
  TITLE     DYRK1A protein kinase promotes quiescence and senescence through
            DREAM complex assembly
  JOURNAL   Genes Dev 25 (8), 801-813 (2011)
   PUBMED   21498570
REFERENCE   7  (residues 1 to 749)
  AUTHORS   Schmit,F., Cremer,S. and Gaubatz,S.
  TITLE     LIN54 is an essential core subunit of the DREAM/LINC complex that
            binds to the cdc2 promoter in a sequence-specific manner
  JOURNAL   FEBS J 276 (19), 5703-5716 (2009)
   PUBMED   19725879
  REMARK    GeneRIF: the cysteine-rich CXC domain of LIN54 is a novel
            DNA-binding domain that binds to the cdc2 promoter in a
            sequence-specific manner
REFERENCE   8  (residues 1 to 749)
  AUTHORS   Litovchick,L., Sadasivam,S., Florens,L., Zhu,X., Swanson,S.K.,
            Velmurugan,S., Chen,R., Washburn,M.P., Liu,X.S. and DeCaprio,J.A.
  TITLE     Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein
            complex represses human cell cycle-dependent genes in quiescence
  JOURNAL   Mol Cell 26 (4), 539-551 (2007)
   PUBMED   17531812
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC021105.13.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_005262807.1, XP_054204888.1.
            
            Summary: LIN54 is a component of the LIN, or DREAM, complex, an
            essential regulator of cell cycle genes (Schmit et al., 2009
            [PubMed 19725879]).[supplied by OMIM, Dec 2010].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1535266.1,
                                           SRR18074968.2286914.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..749
                     /product="protein lin-54 homolog isoform a"
                     /note="protein lin-54 homolog; CXC domain-containing
                     protein 1"
                     /calculated_mol_wt=79363
     Region          214..>461
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Site            244
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q6MZP7.3)"
     Site            249
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q6MZP7.3)"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6MZP7.3)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6MZP7.3)"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6MZP7.3)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6MZP7.3)"
     Region          369..388
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MZP7.3)"
     Region          522..>545
                     /region_name="TCR"
                     /note="Tesmin/TSO1-like CXC domain, cysteine-rich domain;
                     pfam03638"
                     /db_xref="CDD:461001"
     Region          523..536
                     /region_name="DNA-binding.
                     /evidence=ECO:0000269|PubMed:27465258"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MZP7.3)"
     Site            536
                     /site_type="other"
                     /note="Critical for interaction with target DNA.
                     /evidence=ECO:0000269|PubMed:27465258; propagated from
                     UniProtKB/Swiss-Prot (Q6MZP7.3)"
     Site            574
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000269|PubMed:27465258; propagated from
                     UniProtKB/Swiss-Prot (Q6MZP7.3)"
     Region          583..596
                     /region_name="Linker.
                     /evidence=ECO:0000269|PubMed:27465258"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MZP7.3)"
     Region          596..631
                     /region_name="TCR"
                     /note="Tesmin/TSO1-like CXC domain, cysteine-rich domain;
                     pfam03638"
                     /db_xref="CDD:461001"
     Region          599..612
                     /region_name="DNA-binding.
                     /evidence=ECO:0000269|PubMed:27465258"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6MZP7.3)"
     Site            610
                     /site_type="other"
                     /note="Critical for interaction with target DNA.
                     /evidence=ECO:0000269|PubMed:27465258; propagated from
                     UniProtKB/Swiss-Prot (Q6MZP7.3)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6MZP7.3)"
     CDS             1..749
                     /gene="LIN54"
                     /gene_synonym="CXCDC1; JC8.6; MIP120; TCX1"
                     /coded_by="NM_001437261.1:183..2432"
                     /note="isoform a is encoded by transcript variant 8"
                     /db_xref="GeneID:132660"
                     /db_xref="HGNC:HGNC:25397"
                     /db_xref="MIM:613367"
ORIGIN      
        1 mevvpaevns llpeeimdtg itlvdddsie avivsspipm eteleeivni nstgdstatp
       61 istepitvys nhtnqvavnt titkadsntt vkpafpsglq klgaqtpvti sanqiilnkv
      121 sqtsdlklgn qtlkpdgqkl ilttlgksgs pivlalphsq lpqaqkvttq aqsgdaklpp
      181 qqikvvtigg rpevkpvigv saltpgsqli ntttqpsvlq tqqlktvqia kkprtptsgp
      241 vitklifakp inskavtgqt tqvsppviag rvlsqstpgt psktitises gvigstlnst
      301 tqtpnkiais plkspnkavk stvqtitvgg vstsqfktii platapnvqq iqvpgskfhy
      361 vrlvtatsas sstqpvsqnp stntqplqqa kpvvvnttpv rmsvpivsaq avkqvvpkpi
      421 nptsqivtts qpqqrlimpa tplpqiqpnl tnlppgtvla papgtgnvgy avlpaqyvtq
      481 lqqssyvsia snstftgtsg iqtqarlpfn giipsesasr prkpcnctks lclklycdcf
      541 angefcnncn ctncynnleh enerqkaika cldrnpeafk pkigkgkege sdrrhskgcn
      601 ckrsgclkny cecyeakimc ssickcigck nfeesperkt lmhladaaev rvqqqtaakt
      661 klssqisdll trptpalnsg ggklpftfvt kevaeatcnc llaqaeqadk kgkskaaaer
      721 mileefgrcl msvinsagka ksdpcamnc
//
LOCUS       NP_001399056             895 aa            linear   PRI 21-NOV-2025
DEFINITION  protein PTHB1 isoform 15 [Homo sapiens].
ACCESSION   NP_001399056
VERSION     NP_001399056.1
DBSOURCE    REFSEQ: accession NM_001412127.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 895)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 895)
  AUTHORS   Zhang,Y., Xu,M., Zhang,M., Yang,G. and Li,X.
  TITLE     A Novel BBS9 Mutation Identified via Whole-Exome Sequencing in a
            Chinese Family with Bardet-Biedl Syndrome
  JOURNAL   Biomed Res Int 2021, 4514967 (2021)
   PUBMED   34692830
  REMARK    GeneRIF: A Novel BBS9 Mutation Identified via Whole-Exome
            Sequencing in a Chinese Family with Bardet-Biedl Syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 895)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 895)
  AUTHORS   Jeziorny,K., Antosik,K., Jakiel,P., Mlynarski,W., Borowiec,M. and
            Zmyslowska,A.
  TITLE     Next-Generation Sequencing in the Diagnosis of Patients with
            Bardet-Biedl Syndrome-New Variants and Relationship with
            Hyperglycemia and Insulin Resistance
  JOURNAL   Genes (Basel) 11 (11), 1283 (2020)
   PUBMED   33138063
  REMARK    GeneRIF: Next-Generation Sequencing in the Diagnosis of Patients
            with Bardet-Biedl Syndrome-New Variants and Relationship with
            Hyperglycemia and Insulin Resistance.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 895)
  AUTHORS   Nachury,M.V., Loktev,A.V., Zhang,Q., Westlake,C.J., Peranen,J.,
            Merdes,A., Slusarski,D.C., Scheller,R.H., Bazan,J.F.,
            Sheffield,V.C. and Jackson,P.K.
  TITLE     A core complex of BBS proteins cooperates with the GTPase Rab8 to
            promote ciliary membrane biogenesis
  JOURNAL   Cell 129 (6), 1201-1213 (2007)
   PUBMED   17574030
REFERENCE   6  (residues 1 to 895)
  AUTHORS   Nishimura,D.Y., Swiderski,R.E., Searby,C.C., Berg,E.M.,
            Ferguson,A.L., Hennekam,R., Merin,S., Weleber,R.G., Biesecker,L.G.,
            Stone,E.M. and Sheffield,V.C.
  TITLE     Comparative genomics and gene expression analysis identifies BBS9,
            a new Bardet-Biedl syndrome gene
  JOURNAL   Am J Hum Genet 77 (6), 1021-1033 (2005)
   PUBMED   16380913
  REMARK    GeneRIF: Comparative genomics and gene expression analysis
            identifies PHTB1 protein as BBS9, a new Bardet-Biedl syndrome gene.
REFERENCE   7  (residues 1 to 895)
  AUTHORS   Vernon,E.G., Malik,K., Reynolds,P., Powlesland,R., Dallosso,A.R.,
            Jackson,S., Henthorn,K., Green,E.D. and Brown,K.W.
  TITLE     The parathyroid hormone-responsive B1 gene is interrupted by a
            t(1;7)(q42;p15) breakpoint associated with Wilms' tumour
  JOURNAL   Oncogene 22 (9), 1371-1380 (2003)
   PUBMED   12618763
  REMARK    GeneRIF: gene is interrupted by a t(1;7)(q42;p15) breakpoint
            associated with Wilms' tumour; new alternately spliced isoforms
            were found in a wide range of adult and foetal tissues
REFERENCE   8  (residues 1 to 895)
  AUTHORS   Adams,A.E., Rosenblatt,M. and Suva,L.J.
  TITLE     Identification of a novel parathyroid hormone-responsive gene in
            human osteoblastic cells
  JOURNAL   Bone 24 (4), 305-313 (1999)
   PUBMED   10221542
REFERENCE   9  (residues 1 to 895)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 895)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CP068271.2.
            
            Summary: This gene is downregulated by parathyroid hormone in
            osteoblastic cells, and therefore is thought to be involved in
            parathyroid hormone action in bones. The exact function of this
            gene has not yet been determined. Alternatively spliced transcript
            variants encoding different isoforms have been identified.
            [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (20) uses the same exon
            combination as variant 10 but represents the allele encoded by the
            T2T-CHM13v2.0 genome assembly. The encoded isoform (15) has a
            frameshifted C-terminus compared to isoform 9.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1968189 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.3"
     Protein         1..895
                     /product="protein PTHB1 isoform 15"
                     /note="protein PTHB1; PTH-responsive osteosarcoma B1
                     protein; bardet-Biedl syndrome 9 protein; parathyroid
                     hormone-responsive B1 gene protein"
                     /calculated_mol_wt=100239
     Region          1..418
                     /region_name="PHTB1_N"
                     /note="PTHB1 N-terminus; pfam14727"
                     /db_xref="CDD:464284"
     Region          1..407
                     /region_name="Seven-bladed beta-propeller.
                     /evidence=ECO:0000269|PubMed:26085087"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SYG4.1)"
     Site            141
                     /site_type="other"
                     /note="Critical for protein stability.
                     /evidence=ECO:0000269|PubMed:26085087; propagated from
                     UniProtKB/Swiss-Prot (Q3SYG4.1)"
     Region          441..819
                     /region_name="PHTB1_C"
                     /note="PTHB1 C-terminus; pfam14728"
                     /db_xref="CDD:464285"
     Region          685..765
                     /region_name="Interaction with LZTL1.
                     /evidence=ECO:0000269|PubMed:22072986"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SYG4.1)"
     CDS             1..895
                     /gene="BBS9"
                     /gene_synonym="B1; C18; D1; PTHB1"
                     /coded_by="NM_001412127.2:490..3177"
                     /note="isoform 15 is encoded by transcript variant 20"
                     /db_xref="GeneID:27241"
                     /db_xref="HGNC:HGNC:30000"
                     /db_xref="MIM:607968"
ORIGIN      
        1 mslfkardww stilgdkeef dqgclclanv dnsgngqdki ivgsfmgylr ifsphpaktg
       61 dgaqaedlll evdlrdpvlq vevgkfvsgt emlhlavlhs rklcvysvsg tlgnvehgnq
      121 cqmklmyehn lqrtacnmty gsfggvkgrd liciqsmdgm lmvfeqesya fgrflpgfll
      181 pgplayssrt dsfltvsscq qvesykyqvl afatdadkrq eteqqklgsg krlvvdwtln
      241 igeqaldici vsfnqsassv fvlgernffc lkdngqirfm kkldwspscf lpycsvsegt
      301 intlignhnn mlhiyqdvtl kwatqlphip vavrvgclhd lkgvivtlsd dghlqcsylg
      361 tdpslfqapn vqsrelnyde ldvemkelqk iikdvnksqg vwpmteredd lnvsvvvspn
      421 fdsvsqatdv evgtdlvpsv tvkvtlqnrv ilqkaklsvy vqppleltcd qftfefmtpd
      481 ltrtvsfsvy lkrsytpsel egnavvsysr ptdrnpdgip rviqckfrlp lkliclpgqp
      541 sktashkiti dtnkspvsll slfpgfasqs dddqvnvmgf hflggaritv lasktsqryr
      601 iqseqfedlw litnelilrl qeyfekqgvk dfacsfsgsi plqeyfelid hhfelringe
      661 kleellsera vqfraiqrrl larfkdktpa plqhldtlld gtykqviala daveenqgnl
      721 fqsftrlksa thlvillial wqklsadqva ileaaflplq edtqelgwee tvdaaishll
      781 ktclsksske qalnlnsqln ipkdtsqlkk hitllcdrls kggrlclstd aaapqtmvmp
      841 ggcttipesd leersveqds telftnhrhl taetprpdpr tgqrieawtl riphs
//
LOCUS       NP_001427986            4374 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HUWE1 isoform 1 [Homo sapiens].
ACCESSION   NP_001427986 XP_047297687 XP_054182281
VERSION     NP_001427986.1
DBSOURCE    REFSEQ: accession NM_001441057.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4374)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 4374)
  AUTHORS   Lee,C., Park,S.H. and Yoon,S.K.
  TITLE     The E3 ligase HUWE1 increases the sensitivity of CRC to oxaliplatin
            through TOMM20 degradation
  JOURNAL   Oncogene 43 (9), 636-649 (2024)
   PUBMED   38184713
  REMARK    GeneRIF: The E3 ligase HUWE1 increases the sensitivity of CRC to
            oxaliplatin through TOMM20 degradation.
REFERENCE   3  (residues 1 to 4374)
  AUTHORS   Li,X.X., Xu,J.K., Su,W.J., Wu,H.L., Zhao,K., Zhang,C.M., Chen,X.K.
            and Yang,L.X.
  TITLE     The role of KDM4A-mediated histone methylation on temozolomide
            resistance in glioma cells through the HUWE1/ROCK2 axis
  JOURNAL   Kaohsiung J Med Sci 40 (2), 161-174 (2024)
   PUBMED   37873881
  REMARK    GeneRIF: The role of KDM4A-mediated histone methylation on
            temozolomide resistance in glioma cells through the HUWE1/ROCK2
            axis.
REFERENCE   4  (residues 1 to 4374)
  AUTHORS   Bernassola,F., Karin,M., Ciechanover,A. and Melino,G.
  TITLE     The HECT family of E3 ubiquitin ligases: multiple players in cancer
            development
  JOURNAL   Cancer Cell 14 (1), 10-21 (2008)
   PUBMED   18598940
  REMARK    Review article
REFERENCE   5  (residues 1 to 4374)
  AUTHORS   Zhong,Q., Gao,W., Du,F. and Wang,X.
  TITLE     Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the
            polyubiquitination of Mcl-1 and regulates apoptosis
  JOURNAL   Cell 121 (7), 1085-1095 (2005)
   PUBMED   15989957
  REMARK    GeneRIF: Mule is both required and sufficient for the
            polyubiquitination of Mcl-1; Mule is a unique BH3-containing E3
            ubiquitin ligase apical to Bcl-2 family proteins during DNA
            damage-induced apoptosis
            GeneRIF: Mule (HUWE1) poly-ubiquitinates anti-apoptotic gene Mcl-1.
REFERENCE   6  (residues 1 to 4374)
  AUTHORS   Chen,D., Kon,N., Li,M., Zhang,W., Qin,J. and Gu,W.
  TITLE     ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
  JOURNAL   Cell 121 (7), 1071-1083 (2005)
   PUBMED   15989956
  REMARK    GeneRIF: study modifies the current view of ARF-mediated p53
            activation and reveals that ARF-BP1 is a critical mediator of both
            the p53-independent and p53-dependent tumor suppressor functions of
            ARF
            GeneRIF: Ubiquitin ligase activity of ARF-BP1 (HUWE1) is inhibited
            by Arf.
REFERENCE   7  (residues 1 to 4374)
  AUTHORS   Liu,Z., Oughtred,R. and Wing,S.S.
  TITLE     Characterization of E3Histone, a novel testis ubiquitin protein
            ligase which ubiquitinates histones
  JOURNAL   Mol Cell Biol 25 (7), 2819-2831 (2005)
   PUBMED   15767685
REFERENCE   8  (residues 1 to 4374)
  AUTHORS   Gu,J., Dubner,R., Fornace,A.J. Jr. and Iadarola,M.J.
  TITLE     UREB1, a tyrosine phosphorylated nuclear protein, inhibits p53
            transactivation
  JOURNAL   Oncogene 11 (10), 2175-2178 (1995)
   PUBMED   7478539
REFERENCE   9  (residues 1 to 4374)
  AUTHORS   Turner,G., Gedeon,A. and Mulley,J.
  TITLE     X-linked mental retardation with heterozygous expression and
            macrocephaly: pericentromeric gene localization
  JOURNAL   Am J Med Genet 51 (4), 575-580 (1994)
   PUBMED   7943042
REFERENCE   10 (residues 1 to 4374)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX323845.7 and AC231658.3.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297687.1, XP_054182281.1.
            
            Summary: This gene encodes a protein containing a C-terminal HECT
            (E6AP type E3 ubiquitin protein ligase) domain that functions as an
            E3 ubiquitin ligase. The encoded protein is required for the
            ubiquitination and subsequent degradation of the anti-apoptotic
            protein Mcl1 (myeloid cell leukemia sequence 1 (BCL2-related)).
            This protein also ubiquitinates the p53 tumor suppressor, core
            histones, and DNA polymerase beta. Mutations in this gene are
            associated with Turner type X-linked syndromic cognitive
            disability. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1137366.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..4374
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..4374
                     /product="E3 ubiquitin-protein ligase HUWE1 isoform 1"
                     /EC_number="2.3.2.26"
                     /note="Mcl-1 ubiquitin ligase E3; BJ-HCC-24 tumor antigen;
                     HECT domain protein LASU1; ARF-binding protein 1;
                     URE-binding protein 1; large structure of UREB1; upstream
                     regulatory element-binding protein 1; homologous to E6AP
                     carboxyl terminus homologous protein 9; HECT-type E3
                     ubiquitin transferase HUWE1; HECT, UBA and WWE domain
                     containing 1, E3 ubiquitin protein ligase"
                     /calculated_mol_wt=481762
     Region          92..367
                     /region_name="DUF908"
                     /note="Domain of Unknown Function (DUF908); pfam06012"
                     /db_xref="CDD:428721"
     Region          431..814
                     /region_name="DUF913"
                     /note="Domain of Unknown Function (DUF913); pfam06025"
                     /db_xref="CDD:461803"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          706..759
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          978..1001
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1014..1037
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1084
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1291..1320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1317..1356
                     /region_name="UBA_HUWE1"
                     /note="UBA domain found in eukaryotic E3 ubiquitin-protein
                     ligase HUWE1 and similar proteins; cd14288"
                     /db_xref="CDD:270474"
     Site            1368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1396..1415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1617..1678
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          1689..1735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1722
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1907
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2018..2065
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2035
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2262..2342
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2267
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2356..2480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2554
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2595
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2694..2970
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          <2735..3066
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            2751
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2826
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2833
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2835
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2861
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2887
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2888
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2889
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2918
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3010..3043
                     /region_name="UBM"
                     /note="Ubiquitin binding region; pfam14377"
                     /db_xref="CDD:464159"
     Region          3036..3059
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3149
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3245..3267
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3404..3424
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3471..3512
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3537..3568
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3555
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3737..3758
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3752
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3757
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3760
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3781..3848
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3808
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3816
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3827
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3830
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3894..3931
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3906
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3919
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3924
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3927
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          4019..4372
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(4023,4053,4064,4125,4299,4335..4336,4339..4343,4363,
                     4371)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(4153,4156..4157,4159..4160,4163,4170,4172,
                     4176..4177,4179,4184,4189,4206,4210)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     Site            4271
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P51593; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     CDS             1..4374
                     /gene="HUWE1"
                     /gene_synonym="ARF-BP1; HECTH9; HSPC272; Ib772; LASU1;
                     MRXST; MULE; URE-B1; UREB1"
                     /coded_by="NM_001441057.1:291..13415"
                     /note="isoform 1 is encoded by transcript variant 11"
                     /db_xref="GeneID:10075"
                     /db_xref="HGNC:HGNC:30892"
                     /db_xref="MIM:300697"
ORIGIN      
        1 mkvdrtklkk tpteapadcr alidklkvcn deqlllelqq iktwnigkce lyhwvdlldr
       61 fdgiladagq tvenmswmlv cdrpereqlk mlllavlnft allieysfsr hlyssiehlt
      121 tllassdmqv vlavlnllyv fskrsnyitr lgsdkrtpll trlqhlaesw ggkengfgla
      181 eccrdlhmmk yppsattlhf efyadpgaev kiekrttsnt lhyihieqld kisespseim
      241 esltkmysip kdkqmllfth irlahgfsnh rkrlqavqar lhaisilvys nalqesansi
      301 lynglieelv dvlqitdkql meikaaslrt ltsivhlert pklssiidct gtasyhgflp
      361 vlvrnciqam idpsmdpyph qfatalfsfl yhlasydagg ealvscgmme allkvikflg
      421 deqdqitfvt ravrvvdlit nldmaafqsh sglsifiyrl ehevdlcrke cpfvikpkiq
      481 rpnttqegee metdmdgvqc ipqraallks mlnflkkaiq dpafsdgirh vmdgslptsl
      541 khiisnaeyy gpslfllate vvtvfvfqep sllsslqdng ltdvmlhall ikdvpatrev
      601 lgslpnvfsa lclnarglqs fvqcqpferl fkvllspdyl pamrrrrssd plgdtasnlg
      661 savdelmrhq ptlktdatta iiklleeicn lgrdpkyicq kpsiqkadgt atappprsnh
      721 aaeeassede eeeevqamqs fnstqqnete pnqqvvgtee ripiplmdyi lnvmkfvesi
      781 lsnnttddhc qefvnqkgll plvtilglpn lpidfptsaa cqavagvcks iltlshepkv
      841 lqegllqlds ilssleplhr piespggsvl lrelacagnv adatlsaqat pllhaltaah
      901 ayimmfvhtc rvgqseirsi svnqwgsqlg lsvlsklsql ycslvwestv llslctpnsl
      961 psgcefgqad mqklvpkdek agttqggkrs dgeqdgaags mdastqglle gigldgdtla
     1021 pmetdeptas dskgkskitp amaarikqik pllsassrlg ralaelfgll vklcvgspvr
     1081 qrrshhaast ttaptpaars tasaltkllt kglswqpppy tptprfrltf ficsvgftsp
     1141 mlfderkypy hlmlqkflcs gghnalfetf nwalsmggkv pvseglehsd lpdgtgefld
     1201 awlmlvekmv npttvlesph slpaklpggv qnfpqfsalr flvvtqkaaf tciknlwnrk
     1261 plkvyggrma esmlailchi lrgepvirer lskekegsrg eedtgqeegg srrepqvnqq
     1321 qlqqlmdmgf trehameall ntstmeqate yllthpppim ggvvrdlsms eedqmmraia
     1381 mslgqdipmd qraespeeva crkeeeerka rekqeeeeak clekfqdadp leqdelhtft
     1441 dtmlpgcfhl ldelpdtvyr vcdlimtaik rngadyrdmi lkqvvnqvwe aadvlikaal
     1501 plttsdtktv sewisqmatl pqasnlatri llltllfeel klpcawvves sgilnvlikl
     1561 levvqpclqa akeqkevqtp kwitpvllli dfyektaiss krraqmtkyl qsnsnnwrwf
     1621 ddrsgrwcsy sasnnstids awksgetsvr ftagrrrytv qfttmvqvne etgnrrpvml
     1681 tllrvprlnk nsknsngqel ektleeskem dikrkenkgn dtplalestn teketsleet
     1741 kigeiliqgl tedmvtvlir acvsmlgvpv dpdtlhatlr lclrltrdhk yammfaelks
     1801 trmilnltqs sgfngftplv tlllrhiied pctlrhtmek vvrsaatsga gsttsgvvsg
     1861 slgsreinyi lrvlgpaacr npdiftevan ccirialpap rgsgtasdde fenlrikgpn
     1921 avqlvkttpl kpsplpvipd tikeviydml nalaayhape eadksdpkpg vmtqevgqll
     1981 qdmgddvyqq yrsltrqssd fdtqsgfsin sqvfaadgas tetsasgtsq geastpeesr
     2041 dgkkdkegdr aseegkqkgk gskplmptst ilrllaelvr syvgiatlia nysytvgqse
     2101 likedcsvla fvldhllpht qnaedkdtpa larlflasla aagsgtdaqv alvnevkaal
     2161 gralamaest ekharlqavm ciistimesc pstssfyssa taktqhngmn niirlflkkg
     2221 lvndlarvph sldlsspnma ntvnaalkpl etlsrivnqp sslfgsksas sknkseqdaq
     2281 gasqdsssnq qdpgepgeae vqeedhdvtq tevadgdimd geaetdsvvi agqpevlssq
     2341 emqveneled lidellerdg gsgnstiivs rsgedesqed vlmdeapsnl sqastlqanr
     2401 edsmnildpe deeehtqeed ssgsnededd sqdeeeeeee deeddqedde geegdedddd
     2461 dgsemelded ypdmnasplv rferfdredd liiefdnmfs satdippspg niptthplmv
     2521 rhadhssltl gsgssttrlt qgigrsqrtl rqltantght ihvhypgnrq pnpplilqrl
     2581 lgpsaaadil qlssslplqs rgrarllvgn ddvhiiarsd dellddffhd qstatsqagt
     2641 lssiptaltr wteeckvlda esmhdcvsvv kvsivnhlef lrdeeleerr ekrrkqlaee
     2701 etkitdkgke dkenrdqsaq ctasksndst eqnlsdgtpm pdsypttpss tdaatseske
     2761 tlgtlqssqq qptlptppal gevpqelqsp ageggsstql lmpvepeelg ptrpsgeaet
     2821 tqmelspapt itslsperae dsdaltavss qlegspmdts slasctleea vgdtsaagss
     2881 eqpragsstp gdappavaev qgrsdgsges aqppedsspp assessstrd savaisgads
     2941 rgileeplps tsseeedpla gislpegvdp sflaalpddi rrevlqnqlg irpptrtaps
     3001 tnssapavvg npgvtevspe flaalppaiq eevlaqqrae qqrrelaqna ssdtpmdpvt
     3061 fiqtlpsdlr rsvledmeds vlavmppdia aeaqalrreq earqrqlmhe rlfghsstsa
     3121 lsailrspaf tsrlsgnrgv qytrlavqrg gtfqmggsss hnrpsgsnvd tllrlrgrll
     3181 ldhealscll vllfvdepkl ntsrlhrvlr nlcyhaqtrh wvirsllsil qrsseselci
     3241 etpklttsee kgkksskscg ssshenrpld llhkmeskss nqlswlsvsm daalgcrtni
     3301 fqiqrsggrk htekhasggs tvhihpqaap vvcrhvldtl iqlakvfpsh ftqqrtketn
     3361 cesdrergnk acspcssqss ssgictdfwd llvkldnmnv srkgknsvks vpvsaggege
     3421 tspysleasp lgqlmnmlsh pvirrssllt ekllrllsli sialpenkvs eaqansgsga
     3481 sstttatstt stttttaast tptpptaptp vtsapalvaa taistivvaa sttvttptta
     3541 tttvsisptt kgskspakvs dggssstdfk mvssgltenq lqlsvevlts hscseegled
     3601 aanvllqlsr gdsgtrdtvl klllngarhl gytlckqigt llaelreynl eqqrraqcet
     3661 lspdglpeeq pqttklkgkm qsrfdmaenv vivasqkrpl ggrelqlpsm smltsktstq
     3721 kfflrvlqvi iqlrddtrra nkkakqtgrl gssglgsass iqaavrqlea eadaiiqmvr
     3781 egqrarrqqq aatsessqse asvrreespm dvdqpspsaq dtqsiasdgt pqgekekeer
     3841 ppelpllseq lsldelwdml geclkelees hdqhavlvlq paveafflvh atereskppv
     3901 rdtresqlah ikdeppplsp apltpatpss ldpffsreps smhissslpp dtqkflrfae
     3961 thrtvlnqil rqstthladg pfavlvdyir vldfdvkrky frqelerlde glrkedmavh
     4021 vrrdhvfeds yrelhrkspe emknrlyivf egeegqdagg llrewymiis remfnpmyal
     4081 frtspgdrvt ytinpsshcn pnhlsyfkfv grivakavyd nrllecyftr sfykhilgks
     4141 vrytdmesed yhfyqglvyl lendvstlgy dltfstevqe fgvcevrdlk pnganilvte
     4201 enkkeyvhlv cqmrmtgair kqlaaflegf yeiipkrlis ifteqelell isglptidid
     4261 dlksnteyhk yqsnsiqiqw fwralrsfdq adrakflqfv tgtskvplqg faalegmngi
     4321 qkfqihrddr stdrlpsaht cfnqldlpay esfeklrhml llaiqecseg fgla
//
LOCUS       NP_001424556            1283 aa            linear   PRI 21-NOV-2025
DEFINITION  ras GTPase-activating protein nGAP isoform 5 [Homo sapiens].
ACCESSION   NP_001424556 XP_047290793 XP_054195667
VERSION     NP_001424556.1
DBSOURCE    REFSEQ: accession NM_001437627.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1283)
  AUTHORS   Zhang,Y., Yang,Y., Hu,X., Wei,B., Shen,Q., Shi,C. and Chen,P.
  TITLE     RAS protein activator-like 2 (RASAL2) initiates peritubular
            capillary rarefaction in hypoxic renal interstitial fibrosis
  JOURNAL   Transl Res 269, 14-30 (2024)
   PUBMED   38453052
  REMARK    GeneRIF: RAS protein activator-like 2 (RASAL2) initiates
            peritubular capillary rarefaction in hypoxic renal interstitial
            fibrosis.
REFERENCE   2  (residues 1 to 1283)
  AUTHORS   Singharajkomron,N., Yodsurang,V., Limprasutr,V., Wattanathamsan,O.,
            Iksen,I., Hayakawa,Y. and Pongrakhananon,V.
  TITLE     CAMSAP2 enhances lung cancer cell metastasis by mediating RASAL2
            degradation
  JOURNAL   Life Sci 338, 122391 (2024)
   PUBMED   38159595
  REMARK    GeneRIF: CAMSAP2 enhances lung cancer cell metastasis by mediating
            RASAL2 degradation.
REFERENCE   3  (residues 1 to 1283)
  AUTHORS   Wills,C., Watts,K., Maughan,T.S., Fisher,D., Al-Tassan,N.A.,
            Houlston,R.S., Escott-Price,V. and Cheadle,J.P.
  TITLE     Germline variation in RASAL2 may predict survival in patients with
            RAS-activated colorectal cancer
  JOURNAL   Genes Chromosomes Cancer 62 (6), 332-341 (2023)
   PUBMED   36790221
  REMARK    GeneRIF: Germline variation in RASAL2 may predict survival in
            patients with RAS-activated colorectal cancer.
REFERENCE   4  (residues 1 to 1283)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 1283)
  AUTHORS   Yue,Y., Wu,K., Qian,W., Zhu,Z., Zhang,S., Zhang,W., Zhang,W.,
            Wu,S., Li,L., Wu,Z., Ma,Q., Xie,K. and Wang,Z.
  TITLE     RASAL2 mediated the enhancement of YAP1/TIAM1 signaling promotes
            malignant phenotypes of pancreatic ductal adenocarcinoma
  JOURNAL   Int J Biol Sci 18 (10), 4245-4259 (2022)
   PUBMED   35844783
  REMARK    GeneRIF: RASAL2 mediated the enhancement of YAP1/TIAM1 signaling
            promotes malignant phenotypes of pancreatic ductal adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1283)
  AUTHORS   Melen,E., Himes,B.E., Brehm,J.M., Boutaoui,N., Klanderman,B.J.,
            Sylvia,J.S. and Lasky-Su,J.
  TITLE     Analyses of shared genetic factors between asthma and obesity in
            children
  JOURNAL   J Allergy Clin Immunol 126 (3), 631-7 (2010)
   PUBMED   20816195
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1283)
  AUTHORS   Shibui,T., Kobayashi,T. and Shiratori,M.
  TITLE     Isolation of cross-reacting antigen candidates by mRNA-display
            using a mixed cDNA library
  JOURNAL   Biotechnol Lett 30 (12), 2037-2043 (2008)
   PUBMED   18633578
REFERENCE   8  (residues 1 to 1283)
  AUTHORS   de Chassey,B., Navratil,V., Tafforeau,L., Hiet,M.S., Aublin-Gex,A.,
            Agaugue,S., Meiffren,G., Pradezynski,F., Faria,B.F., Chantier,T.,
            Le Breton,M., Pellet,J., Davoust,N., Mangeot,P.E., Chaboud,A.,
            Penin,F., Jacob,Y., Vidalain,P.O., Vidal,M., Andre,P.,
            Rabourdin-Combe,C. and Lotteau,V.
  TITLE     Hepatitis C virus infection protein network
  JOURNAL   Mol Syst Biol 4, 230 (2008)
   PUBMED   18985028
REFERENCE   9  (residues 1 to 1283)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 1283)
  AUTHORS   Noto,S., Maeda,T., Hattori,S., Inazawa,J., Imamura,M., Asaka,M. and
            Hatakeyama,M.
  TITLE     A novel human RasGAP-like gene that maps within the prostate cancer
            susceptibility locus at chromosome 1q25
  JOURNAL   FEBS Lett 441 (1), 127-131 (1998)
   PUBMED   9877179
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160281.17, AL499617.16,
            AL365357.12 and AL035702.7.
            
            On or before Apr 7, 2025 this sequence version replaced
            XP_047290793.1, XP_054195667.1.
            
            Summary: This gene encodes a protein that contains the GAP-related
            domain (GRD), a characteristic domain of GTPase-activating proteins
            (GAPs). GAPs function as activators of Ras superfamily of small
            GTPases. The protein encoded by this gene is able to complement the
            defective RasGAP function in a yeast system. Two alternatively
            spliced transcript variants of this gene encoding distinct isoforms
            have been reported. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2304293.1,
                                           SRR18074967.1727982.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1283
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..1283
                     /product="ras GTPase-activating protein nGAP isoform 5"
                     /note="Ras protein activator like 1; ras GTPase-activating
                     protein nGAP; RASAL2/ACVR1 fusion"
                     /calculated_mol_wt=144149
     Region          184..321
                     /region_name="PH_nGAP"
                     /note="Neuronal growth-associated proteins Pleckstrin
                     homology (PH) domain; cd13373"
                     /db_xref="CDD:270176"
     Region          307..446
                     /region_name="C2_SynGAP_like"
                     /note="C2 domain present in Ras GTPase activating protein
                     (GAP) family; cd04013"
                     /db_xref="CDD:175980"
     Region          437..760
                     /region_name="RasGAP_DAB2IP"
                     /note="Ras-GTPase Activating Domain of DAB2IP and similar
                     proteins; cd05136"
                     /db_xref="CDD:213338"
     Site            order(476,513,515,517..518,520,523,527,619,627..628,
                     631..632,635,656,659..660,663,667,669,674..675)
                     /site_type="other"
                     /note="putative RAS interface [polypeptide binding]"
                     /db_xref="CDD:213338"
     Region          750..1226
                     /region_name="DUF3498"
                     /note="Domain of unknown function (DUF3498); pfam12004"
                     /db_xref="CDD:463427"
     CDS             1..1283
                     /gene="RASAL2"
                     /gene_synonym="NGAP"
                     /coded_by="NM_001437627.1:390..4241"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:9462"
                     /db_xref="HGNC:HGNC:9874"
                     /db_xref="MIM:606136"
ORIGIN      
        1 melspssgga aealswpemf palesdsplp pedldavvpv sgavaggmld rillesvcqq
       61 qswvrvydvk gppthrlscg qspytetttw erkyciltds qlvllnkeke ipveggqeqq
      121 tdstkgrclr rtvsvpsegq fpeyppegat klevpaersp rrrsisgtst sekpnsmdta
      181 ntspfkvpgf fskrlkgsik rtksqskldr ntsfrlpslr stddrsrglp klkesrshes
      241 llspcstvec ldlgrgepvs vkplhssilg qdfcfevtyl sgskcfscns aserdkwmen
      301 lrrtvqpnkd ncrraenvlr lwiieakdla pkkkyfcelc lddtlfartt sktkadnifw
      361 gehfeffslp plhsitvhiy kdvekkkkkd knnyvglvni ptasvtgrqf vekwypvstp
      421 tpnkgktggp siriksrfqt itilpmeqyk efaefvtsny tmlcsvlepv isvrnkeela
      481 calvhilqst grakdfltdl vmsevdrcge hdvlifrent iatksieeyl klvgqqylhd
      541 algefikaly esdencevdp skcssselid hqsnlkmcce lafckiinsy cvfprelkev
      601 faswkqqcln rgkqdiserl isaslflrfl cpaimspslf nlmqeypddr tsrtltliak
      661 viqnlanfak fgnkeeymaf mndflehewg gmkrflleis npdtisntpg fdgyidlgre
      721 lsvlhsllwe vvsqldkatv aklgplprvl aditksltnp tpiqqqlrrf tehnsspnvs
      781 gslssglqki fedptdsdlh klkspsqdnt dsyfrgktll lvqqassqsm tysekderes
      841 slpngrsvsl mdlqdthaaq vehasvmldv pirltgsqls itqvasikql retqstpqsa
      901 pqvrrplhpa lnqpgglqpl sfqnpvyhln npipampkas idsslenlst assrsqsnse
      961 dfklsgpsns smedftkrst qsedfsrrht vpdrhiplal prqnstgqaq irkvdqgglg
     1021 arakappslp hsaslrstgs msvvsaalva epvqngsrsr qqssssresp vpkvraiqrq
     1081 qtqqvqspvd satmspvert aawvlnngqy eedveeteqn ldeakhaeky eqeitklker
     1141 lrvssrrlee yerrllvqeq qmqkllleyk arledseerl rrqqeekdsq mksiisrlma
     1201 veeelkkdha emqavidakq kiidaqving deiiqtgktd rvpgfsqhqt deradpsega
     1261 vqhagpqwhl phqphqafhh gew
//
LOCUS       NP_001415241             326 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb complex protein BMI-1 [Homo sapiens].
ACCESSION   NP_001415241
VERSION     NP_001415241.1
DBSOURCE    REFSEQ: accession NM_001428312.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Szustka,A. and Krzeslak,A.
  TITLE     BMI-1 in Breast Cancer - Biological Role and Clinical Implications
  JOURNAL   Cell Physiol Biochem 58 (5), 584-596 (2024)
   PUBMED   39429016
  REMARK    GeneRIF: BMI-1 in Breast Cancer - Biological Role and Clinical
            Implications.
            Review article
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Hsu,Y.C., Luo,C.W., Chang,S.J., Lai,C.Y., Yang,Y.T., Chen,Y.Z.,
            Liu,W.T., Wu,C.C., Sun,C.K., Hou,M.F. and Pan,M.R.
  TITLE     Targeting Bmi1 for Enhancing Anoikis Sensitivity and Inhibiting
            Metastasis in Colorectal Cancer
  JOURNAL   Cancer Genomics Proteomics 21 (5), 523-532 (2024)
   PUBMED   39191496
  REMARK    GeneRIF: Targeting Bmi1 for Enhancing Anoikis Sensitivity and
            Inhibiting Metastasis in Colorectal Cancer.
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Li,Q., Fu,T., Wei,N., Wang,Q. and Zhang,X.
  TITLE     Bmi-1 promotes the proliferation, migration and invasion, and
            inhibits cell apoptosis of human retinoblastoma cells via RKIP
  JOURNAL   Sci Rep 14 (1), 14544 (2024)
   PUBMED   38914697
  REMARK    GeneRIF: Bmi-1 promotes the proliferation, migration and invasion,
            and inhibits cell apoptosis of human retinoblastoma cells via RKIP.
            Erratum:[Sci Rep. 2025 Aug 5;15(1):28521. doi:
            10.1038/s41598-025-11879-x. PMID: 40764337]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Park,I.K., Qian,D., Kiel,M., Becker,M.W., Pihalja,M.,
            Weissman,I.L., Morrison,S.J. and Clarke,M.F.
  TITLE     Bmi-1 is required for maintenance of adult self-renewing
            haematopoietic stem cells
  JOURNAL   Nature 423 (6937), 302-305 (2003)
   PUBMED   12714971
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Satijn,D.P. and Otte,A.P.
  TITLE     RING1 interacts with multiple Polycomb-group proteins and displays
            tumorigenic activity
  JOURNAL   Mol Cell Biol 19 (1), 57-68 (1999)
   PUBMED   9858531
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Alkema,M.J., Jacobs,J., Voncken,J.W., Jenkins,N.A., Copeland,N.G.,
            Satijn,D.P., Otte,A.P., Berns,A. and van Lohuizen,M.
  TITLE     MPc2, a new murine homolog of the Drosophila polycomb protein is a
            member of the mouse polycomb transcriptional repressor complex
  JOURNAL   J Mol Biol 273 (5), 993-1003 (1997)
   PUBMED   9367786
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Alkema,M.J., Bronk,M., Verhoeven,E., Otte,A., van 't Veer,L.J.,
            Berns,A. and van Lohuizen,M.
  TITLE     Identification of Bmi1-interacting proteins as constituents of a
            multimeric mammalian polycomb complex
  JOURNAL   Genes Dev 11 (2), 226-240 (1997)
   PUBMED   9009205
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Alkema,M.J., Wiegant,J., Raap,A.K., Berns,A. and van Lohuizen,M.
  TITLE     Characterization and chromosomal localization of the human
            proto-oncogene BMI-1
  JOURNAL   Hum Mol Genet 2 (10), 1597-1603 (1993)
   PUBMED   8268912
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158211.29.
            
            Summary: This gene encodes a ring finger protein that is major
            component of the polycomb group complex 1 (PRC1). This complex
            functions through chromatin remodeling as an essential epigenetic
            repressor of multiple regulatory genes involved in embryonic
            development and self-renewal in somatic stem cells. This protein
            also plays a central role in DNA damage repair. This gene is an
            oncogene and aberrant expression is associated with numerous
            cancers and is associated with resistance to certain
            chemotherapies. A pseudogene of this gene is found on chromosome X.
            Read-through transcription also exists between this gene and the
            upstream COMM domain containing 3 (COMMD3) gene. [provided by
            RefSeq, Sep 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.215303.1,
                                           SRR1803612.110042.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.2"
     Protein         1..326
                     /product="polycomb complex protein BMI-1"
                     /note="murine leukemia viral (bmi-1) oncogene homolog; B
                     lymphoma Mo-MLV insertion region 1 homolog; ring finger
                     protein 51; polycomb group protein Bmi1; polycomb group
                     RING finger protein 4; BMI1 polycomb ring finger oncogene;
                     BMI1 polycomb ring finger proto-oncogene"
                     /calculated_mol_wt=36818
     Region          5..101
                     /region_name="RING-HC_PCGF4"
                     /note="RING finger found in polycomb group RING finger
                     protein 4 (PCGF4) and similar proteins; cd16736"
                     /db_xref="CDD:438394"
     Site            order(5..13,15,17,21,23..24,26..27,29..30,32..36,39..42,
                     44..45,66,69..72,74,78,81..82,84,86,89..90,93..94,97)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438394"
     Region          81..95
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     Region          130..226
                     /region_name="RAWUL_PCGF4"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in polycomb group RING finger protein
                     4 (PCGF4); cd17165"
                     /db_xref="CDD:340685"
     Region          162..182
                     /region_name="Interaction with PHC2.
                     /evidence=ECO:0000269|PubMed:27827373"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     Region          164..228
                     /region_name="Interaction with E4F1.
                     /evidence=ECO:0000269|PubMed:16882984"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     Region          236..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     CDS             1..326
                     /gene="BMI1"
                     /gene_synonym="flvi-2/bmi-1; FLVI2/BMI1; PCGF4; RNF51"
                     /coded_by="NM_001428312.1:270..1250"
                     /db_xref="GeneID:648"
                     /db_xref="HGNC:HGNC:1066"
                     /db_xref="MIM:164831"
ORIGIN      
        1 mhrttrikit elnphlmcvl cggyfidatt iieclhsfck tcivrylets kycpicdvqv
       61 hktrpllnir sdktlqdivy klvpglfkne mkrrrdfyaa hpsadaangs nedrgevade
      121 dkriitddei islsieffdq nrldrkvnkd kekskeevnd krylrcpaam tvmhlrkflr
      181 skmdipntfq idvmyeeepl kdyytlmdia yiytwrrngp lplkyrvrpt ckrmkishqr
      241 dgltnagele sdsgsdkans paggipstss clpspstpvq sphpqfphis stmngtsnsp
      301 sgnhqssfan rprkssvngs satssg
//
LOCUS       NP_001427456             287 aa            linear   PRI 21-NOV-2025
DEFINITION  syntaxin-3 isoform 5 [Homo sapiens].
ACCESSION   NP_001427456
VERSION     NP_001427456.1
DBSOURCE    REFSEQ: accession NM_001440527.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Shinozuka,T., Kanda,M., Sato,Y., Shimizu,D., Tanaka,C., Umeda,S.,
            Inokawa,Y., Hattori,N., Hayashi,M., Nakayama,G. and Kodera,Y.
  TITLE     Increased STX3 transcript and protein levels were associated with
            poor prognosis in two independent cohorts of esophageal squamous
            cell carcinoma patients
  JOURNAL   Cancer Med 12 (24), 22185-22195 (2023)
   PUBMED   38014487
  REMARK    GeneRIF: Increased STX3 transcript and protein levels were
            associated with poor prognosis in two independent cohorts of
            esophageal squamous cell carcinoma patients.
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Janecke,A.R., Liu,X., Adam,R., Punuru,S., Viestenz,A., Strauss,V.,
            Laass,M., Sanchez,E., Adachi,R., Schatz,M.P., Saboo,U.S.,
            Mittal,N., Rohrschneider,K., Escher,J., Ganesh,A., Al Zuhaibi,S.,
            Al Murshedi,F., AlSaleem,B., Alfadhel,M., Al Sinani,S.,
            Alkuraya,F.S., Huber,L.A., Muller,T., Heidelberger,R. and Janz,R.
  TITLE     Pathogenic STX3 variants affecting the retinal and intestinal
            transcripts cause an early-onset severe retinal dystrophy in
            microvillus inclusion disease subjects
  JOURNAL   Hum Genet 140 (8), 1143-1156 (2021)
   PUBMED   33974130
  REMARK    GeneRIF: Pathogenic STX3 variants affecting the retinal and
            intestinal transcripts cause an early-onset severe retinal
            dystrophy in microvillus inclusion disease subjects.
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Low,S.H., Vasanji,A., Nanduri,J., He,M., Sharma,N., Koo,M.,
            Drazba,J. and Weimbs,T.
  TITLE     Syntaxins 3 and 4 are concentrated in separate clusters on the
            plasma membrane before the establishment of cell polarity
  JOURNAL   Mol Biol Cell 17 (2), 977-989 (2006)
   PUBMED   16339081
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Martin-Martin,B., Nabokina,S.M., Lazo,P.A. and Mollinedo,F.
  TITLE     Co-expression of several human syntaxin genes in neutrophils and
            differentiating HL-60 cells: variant isoforms and detection of
            syntaxin 1
  JOURNAL   J Leukoc Biol 65 (3), 397-406 (1999)
   PUBMED   10080545
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Steegmaier,M., Yang,B., Yoo,J.S., Huang,B., Shen,M., Yu,S., Luo,Y.
            and Scheller,R.H.
  TITLE     Three novel proteins of the syntaxin/SNAP-25 family
  JOURNAL   J Biol Chem 273 (51), 34171-34179 (1998)
   PUBMED   9852078
REFERENCE   8  (residues 1 to 287)
  AUTHORS   Riento,K., Galli,T., Jansson,S., Ehnholm,C., Lehtonen,E. and
            Olkkonen,V.M.
  TITLE     Interaction of Munc-18-2 with syntaxin 3 controls the association
            of apical SNAREs in epithelial cells
  JOURNAL   J Cell Sci 111 (Pt 17), 2681-2688 (1998)
   PUBMED   9701566
REFERENCE   9  (residues 1 to 287)
  AUTHORS   Galli,T., Zahraoui,A., Vaidyanathan,V.V., Raposo,G., Tian,J.M.,
            Karin,M., Niemann,H. and Louvard,D.
  TITLE     A novel tetanus neurotoxin-insensitive vesicle-associated membrane
            protein in SNARE complexes of the apical plasma membrane of
            epithelial cells
  JOURNAL   Mol Biol Cell 9 (6), 1437-1448 (1998)
   PUBMED   9614185
REFERENCE   10 (residues 1 to 287)
  AUTHORS   Delgrossi,M.H., Breuza,L., Mirre,C., Chavrier,P. and Le Bivic,A.
  TITLE     Human syntaxin 3 is localized apically in human intestinal cells
  JOURNAL   J Cell Sci 110 (Pt 18), 2207-2214 (1997)
   PUBMED   9378770
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000640.5.
            
            Summary: The gene is a member of the syntaxin family. The encoded
            protein is targeted to the apical membrane of epithelial cells
            where it forms clusters and is important in establishing and
            maintaining polarity necessary for protein trafficking involving
            vesicle fusion and exocytosis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA2145743, SAMN03465402
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..287
                     /product="syntaxin-3 isoform 5"
                     /note="syntaxin 3A; syntaxin 3B"
                     /calculated_mol_wt=32810
     Region          34..226
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     Region          194..260
                     /region_name="SNARE"
                     /note="SNARE motif; cl22856"
                     /db_xref="CDD:473982"
     Site            order(222,229,232)
                     /site_type="other"
                     /note="flanking leucine-zipper layers"
                     /db_xref="CDD:277192"
     Site            225
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277192"
     CDS             1..287
                     /gene="STX3"
                     /gene_synonym="DIAR12; MVID2; RDMVID; STX3A"
                     /coded_by="NM_001440527.1:231..1094"
                     /note="isoform 5 is encoded by transcript variant 8"
                     /db_xref="GeneID:6809"
                     /db_xref="HGNC:HGNC:11438"
                     /db_xref="MIM:600876"
ORIGIN      
        1 mkdrleqlka kqltqdddtd aveiaidnta fmdeffseie etrlnidkis ehveeakkly
       61 siilsapipe pktkddleql tteikkrann vrnklksmek hieedevrss adlrirksqh
      121 svlsrkfvev mtkyneaqvd frerskgriq rqleitgkkt tdeeleemle sgnpaiftsg
      181 iidsqiskqa lseiegrhkd ivrlessike lhdmfmdiam lvenqgsmid riennmdqsv
      241 gfveravadt kkavkyqsea rrkkimimic ciilaiilas tigsifa
//
LOCUS       NP_001393932             386 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform N [Homo sapiens].
ACCESSION   NP_001393932
VERSION     NP_001393932.1
DBSOURCE    REFSEQ: accession NM_001407003.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 386)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 386)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 386)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 386)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 386)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355388.30 and AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1363725.1,
                                           SRR1163655.450397.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..386
                     /product="lamin isoform N"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=44241
     Region          <1..200
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          248..355
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     CDS             1..386
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001407003.1:311..1471"
                     /note="isoform N is encoded by transcript variant 28"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 mlrrvdaenr lqtmkeeldf qkniyseelr etkrrhetrl veidngkqre fesrladalq
       61 elraqhedqv eqykkelekt ysakldnarq saernsnlvg aaheelqqsr iridslsaql
      121 sqlqkqlaak eaklrdleds larerdtsrr llaekerema emrarmqqql deyqelldik
      181 laldmeihay rkllegeeer lrlspsptsq rsrgrasshs sqtqgggsvt kkrklestes
      241 rssfsqhart sgrvaveevd eegkfvrlrn ksnedqsmgn wqikrqngdd plltyrfppk
      301 ftlkagqvvt iwaagagath spptdlvwka qntwgcgnsl rtalinstge evamrklvrs
      361 vtvveddede dgddllhhhh vsgsrr
//
LOCUS       NP_001393924             478 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform K [Homo sapiens].
ACCESSION   NP_001393924
VERSION     NP_001393924.1
DBSOURCE    REFSEQ: accession NM_001406995.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 478)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 478)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853562.2224.1,
                                           SRR14038192.4070665.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..478
                     /product="lamin isoform K"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=53246
     Region          <1..200
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          248..355
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     CDS             1..478
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406995.1:610..2046"
                     /note="isoform K is encoded by transcript variant 20"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 mlrrvdaenr lqtmkeeldf qkniyseelr etkrrhetrl veidngkqre fesrladalq
       61 elraqhedqv eqykkelekt ysakldnarq saernsnlvg aaheelqqsr iridslsaql
      121 sqlqkqlaak eaklrdleds larerdtsrr llaekerema emrarmqqql deyqelldik
      181 laldmeihay rkllegeeer lrlspsptsq rsrgrasshs sqtqgggsvt kkrklestes
      241 rssfsqhart sgrvaveevd eegkfvrlrn ksnedqsmgn wqikrqngdd plltyrfppk
      301 ftlkagqvvt iwaagagath spptdlvwka qntwgcgnsl rtalinstge evamrklvrs
      361 vtvveddede dgddllhhhh gshcsssgdp aeynlrsrtv lcgtcgqpad kasasgsgaq
      421 vggpissgss assvtvtrsy rsvggsgggs fgdnlvtrsy llgnssprtq spqncsim
//
LOCUS       NP_001425414            2342 aa            linear   PRI 21-NOV-2025
DEFINITION  AT-rich interactive domain-containing protein 1B isoform 7 [Homo
            sapiens].
ACCESSION   NP_001425414 XP_047275098 XP_054212020
VERSION     NP_001425414.1
DBSOURCE    REFSEQ: accession NM_001438485.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2342)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2342)
  AUTHORS   Bosch,E., Guse,E., Kirchner,P., Winterpacht,A., Walther,M.,
            Alders,M., Kerkhof,J., Ekici,A.B., Sticht,H., Sadikovic,B., Reis,A.
            and Vasileiou,G.
  TITLE     The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation
  JOURNAL   Hum Genet 143 (8), 965-978 (2024)
   PUBMED   39028335
  REMARK    GeneRIF: The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation.
REFERENCE   3  (residues 1 to 2342)
  AUTHORS   Huang,X., Li,H., Yang,S., Ma,M., Lian,Y., Wu,X., Qi,X., Wang,X.,
            Rong,W. and Sheng,X.
  TITLE     De novo variation in ARID1B gene causes Coffin-Siris syndrome 1 in
            a Chinese family with excessive early-onset high myopia
  JOURNAL   BMC Med Genomics 17 (1), 142 (2024)
   PUBMED   38790056
  REMARK    GeneRIF: De novo variation in ARID1B gene causes Coffin-Siris
            syndrome 1 in a Chinese family with excessive early-onset high
            myopia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2342)
  AUTHORS   Hurlstone,A.F., Olave,I.A., Barker,N., van Noort,M. and Clevers,H.
  TITLE     Cloning and characterization of hELD/OSA1, a novel BRG1 interacting
            protein
  JOURNAL   Biochem J 364 (Pt 1), 255-264 (2002)
   PUBMED   11988099
  REMARK    GeneRIF: Cloning and characterization of hELD/OSA1, a novel BRG1
            interacting protein.
REFERENCE   5  (residues 1 to 2342)
  AUTHORS   Phelan,M.L., Sif,S., Narlikar,G.J. and Kingston,R.E.
  TITLE     Reconstitution of a core chromatin remodeling complex from SWI/SNF
            subunits
  JOURNAL   Mol Cell 3 (2), 247-253 (1999)
   PUBMED   10078207
REFERENCE   6  (residues 1 to 2342)
  AUTHORS   Imbert,G., Saudou,F., Yvert,G., Devys,D., Trottier,Y.,
            Garnier,J.M., Weber,C., Mandel,J.L., Cancel,G., Abbas,N., Durr,A.,
            Didierjean,O., Stevanin,G., Agid,Y. and Brice,A.
  TITLE     Cloning of the gene for spinocerebellar ataxia 2 reveals a locus
            with high sensitivity to expanded CAG/glutamine repeats
  JOURNAL   Nat Genet 14 (3), 285-291 (1996)
   PUBMED   8896557
REFERENCE   7  (residues 1 to 2342)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
REFERENCE   8  (residues 1 to 2342)
  AUTHORS   Vergano,S.A., van der Sluijs,P.J. and Santen,G.
  TITLE     ARID1B-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31132234
REFERENCE   9  (residues 1 to 2342)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
REFERENCE   10 (residues 1 to 2342)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355297.20, AL162578.13,
            AL049820.23 and AL591545.6.
            
            On or before Apr 21, 2025 this sequence version replaced
            XP_047275098.1, XP_054212020.1.
            
            Summary: This locus encodes an AT-rich DNA interacting
            domain-containing protein. The encoded protein is a component of
            the SWI/SNF chromatin remodeling complex and may play a role in
            cell-cycle activation. The protein encoded by this locus is similar
            to AT-rich interactive domain-containing protein 1A. These two
            proteins function as alternative, mutually exclusive ARID-subunits
            of the SWI/SNF complex. The associated complexes play opposing
            roles. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.171981.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2342
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..2342
                     /product="AT-rich interactive domain-containing protein 1B
                     isoform 7"
                     /note="BRG1-binding protein ELD/OSA1; ELD (eyelid)/OSA
                     protein; BRG1-associated factor 250b; ARID
                     domain-containing protein 1B; AT rich interactive domain
                     1B (SWI1-like)"
                     /calculated_mol_wt=246024
     Region          758..>1099
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     Region          1160..1252
                     /region_name="ARID_ARID1B"
                     /note="ARID/BRIGHT DNA binding domain of AT-rich
                     interactive domain-containing protein 1B (ARID1B) and
                     similar proteins; cd16877"
                     /db_xref="CDD:350641"
     Site            order(1182..1188,1213,1215..1216,1219,1229,1231..1233,
                     1235)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350641"
     Region          1273..>1653
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          2033..2288
                     /region_name="BAF250_C"
                     /note="SWI/SNF-like complex subunit BAF250/Osa; pfam12031"
                     /db_xref="CDD:463439"
     CDS             1..2342
                     /gene="ARID1B"
                     /gene_synonym="6A3-5; BAF250B; BRIGHT; CSS1; DAN15;
                     ELD/OSA1; MRD12; OSA2; P250R; SMARCF2"
                     /coded_by="NM_001438485.1:304..7332"
                     /note="isoform 7 is encoded by transcript variant 8"
                     /db_xref="GeneID:57492"
                     /db_xref="HGNC:HGNC:18040"
                     /db_xref="MIM:614556"
ORIGIN      
        1 maaraaaaaa aaaararara gsgerrappg prpapgardl eagargaaaa aaapgpmlgg
       61 ggdgggglns vhhhpllprh elnmahnaga aaaagthsak sggseaalke ggsaaalsss
      121 ssssaaaaaa ssssssgpgs ametgllpnh klktvgeapa apphqqhhhh hhahhhhhha
      181 hhlhhhhalq qqlnqfqqqq qqqqqqqqqq qqqqhpisnn nslggaggga pqpgpdmeqp
      241 qhggakdsaa ggqadppgpp llskpgdedd appkmgepag gryehpglga lgtqqppvav
      301 pgggggpaav pefnnyygsa apasggpggr agpcfdqhgg qqspgmgmmh sasaaaagap
      361 gsmdplqnsh egypnsqcnh ypgysrpgag gggggggggg ggsggggggg gagaggagag
      421 avaaaaaaaa aaaggggggg yggssagygv lssprqqggg mmmgpgggga aslskaaags
      481 aaggfqrfag qnqhpsgatp tlnqlltsps pmmrsyggsy peysspsapp pppsqpqsqa
      541 aaagaaaggq qaaagmglgk dmgaqyaaas pawaaaqqrs hpamspgtpg ptmgrsqgsp
      601 mdpmvmkrpq lygmgsnphs qpqqsspypg gsygppgpqr ypigiqgrtp gamagmqypq
      661 qqmppqygqq gvsgycqqgq qpyysqqpqp phlppqaqyl psqsqqryqp qqdmsqegyg
      721 trsqpplapg kpnhedlnli qqerpsslpd lsgsiddlpt gteatlssav sasgstssqg
      781 dqsnpaqspf sphasphlss ipggpspspv gspvgsnqsr sgpispasip gfmagtqrnp
      841 qmaqygpqqt gpsmsphpsp ggqmhagiss fqqsnssgty gpqmsqygpq gnysrppays
      901 gvpsasysgp gpgmgisann qmhgqgpsqp cgavplgrmp sagmqnrpfp gnmssmtpss
      961 pgmsqqggpg mgppmptvnr kaqeaaaavm qaaansaqsr qgsfpgmnqs glmassspys
     1021 qpmnnssslm ntqappysma pamvnssaas vgladmmspg esklplplka dgkeegtpqp
     1081 eskskdsyss qgisqpptpg nlpvpspmsp ssasissfhg desdsisspg wpktpsspks
     1141 ssstttgeki tkvyelgnep erklwvdryl tfmeergspv sslpavgkkp ldlfrlyvcv
     1201 keigglaqvn knkkwrelat nlnvgtsssa asslkkqyiq ylfafeckie rgeepppevf
     1261 stgdtkkqpk lqppspansg slqgpqtpqs tgsnsmaevp gdlkpptpas tphgqmtpmq
     1321 ggrsstisvh dpfsdvsdss fpkrnsmtpn apyqqgmsmp dvmgrmpyep nkdpfggmrk
     1381 vpgssepfmt qgqmpnssmq dmynqspsga msnlgmgqrq qfpygasydr rhepygqqyp
     1441 gqgppsgqpp ygghqpglyp qqpnykrhmd gmygppakrh egdmynmqys sqqqemynqy
     1501 ggsysgpdrr piqgqypypy srermqgpgq iqthgippqm mggplqssss egpqqnmwaa
     1561 rndmpypyqn rqgpggptqa ppypgmnrtd dmmvpdqrin hesqwpshvs qrqpymsssa
     1621 smqpitrppq psyqtppslp nhisrapspa sfqrslenrm spskspflps mkmqkvmptv
     1681 ptsqvtgppp qpppirreit fppgsveasq pvlkqrrkit skdivtpeaw rvmmslksgl
     1741 laestwaldt inillyddst vatfnlsqls gflellveyf rkclidifgi lmeyevgdps
     1801 qkaldhnaar kddsqsladd sgkeeedaec idddeedeed eeedsektes dekssialta
     1861 pdaaadpkek pkqaskfdkl pikivkknnl fvvdrsdklg rvqefnsgll hwqlgggdtt
     1921 ehiqthfesk meipprrrpp pplssagrkk eqegkgdsee qqeksiiati ddvlsarpga
     1981 lpedanpgpq tesskfpfgi qqakshrnik lledeprsrd etplctiahw qdslakrcic
     2041 vsnivrslsf vpgndaemsk hpglvlilgk lillhhehpe rkrapqtyek eededkgvac
     2101 skdewwwdcl evlrdntlvt lanisgqldl saytesiclp ildgllhwmv cpsaeaqdpf
     2161 ptvgpnsvls pqrlvletlc klsiqdnnvd lilatppfsr qekfyatlvr yvgdrknpvc
     2221 remsmallsn laqgdalaar aiavqkgsig nlisfledgv tmaqyqqsqh nlmhmqpppl
     2281 eppsvdmmcr aakallamar vdenrsefll hegrlldisi savlnslvas vicdvlfqig
     2341 ql
//
LOCUS       NP_001400670             967 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform d [Homo sapiens].
ACCESSION   NP_001400670
VERSION     NP_001400670.1
DBSOURCE    REFSEQ: accession NM_001413741.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 967)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 967)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 967)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 967)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 967)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 967)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 967)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 967)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 967)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 967)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.143395.1,
                                           SRR18074967.1400355.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..967
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..967
                     /product="polyhomeotic-like protein 1 isoform d"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=101199
     Region          <437..633
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          791..898
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          898..966
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(916..917,951..952,955..956,959)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(927..931,933..934,937..938,942,947)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..967
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413741.1:368..3271"
                     /note="isoform d is encoded by transcript variant 5"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqat iaasrqassp ntsttqqqtt
       61 ttqasinlat tsaaqlisrs qsvsspsatt ltqsvllgnt tspplnqsqa qmylrpqlgn
      121 llqvnrtlgr nvplasqlil mpngavaavq qevpsaqspg vhadadqvqn lavrnqqasa
      181 qgpqmqgstq kaippgaspv sslsqassqa lavaqassga tnqslnlsqa gggsgnsipg
      241 smgpggggqa hgglgqlpss gmgggscprk gtgvvqplpa aqtvtvsqgs qteaesaaak
      301 kaeadgsgqq nvgmnltrta tpapsqtlis satytqiqph sliqqqqqih lqqkqvviqq
      361 qiaihhqqqf qhrqsqllht athlqlaqqq qqqqqqqqqq qqpqattlta pqppqvpptq
      421 qvppsqsqqq aqtlvvqpml qssplslppd aapkppipiq skppvapikp pqlgaakmsa
      481 aqqppphipv qvvgtrqpgt aqaqalglaq laaavptsrg mpgtvqsgqa hlassppssq
      541 apgalqecpp tlapgmtlap vqgtahvvkg gattsspvva qvpaafymqs vhlpgkpqtl
      601 avkrkadsee erddvstlgs mlpakaspva espkvmdeks slgekaesva nvnantpsse
      661 lvaltpapsv ppptlamvsr qmgdskppqa ivkpqilthi iegfviqega epfpvgcsql
      721 lkesekplqt glptgltenq sggplgvdsp saeldkkanl lkceycgkya paeqfrgskr
      781 fcsmtcakry nvscshqfrl krkkmkefqe anyarvrrrg prrsssdiar akiqgkchrg
      841 qedssrgsdn ssydealspt spgplsvrag hgerdlgnpn tapptpelhg inpvflssnp
      901 srwsveevye fiaslqgcqe iaeefrsqei dgqallllke ehlmsamnik lgpalkicak
      961 invlket
//
LOCUS       NP_001425495             159 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding protein with multiple splicing isoform E [Homo
            sapiens].
ACCESSION   NP_001425495 XP_047277235
VERSION     NP_001425495.1
DBSOURCE    REFSEQ: accession NM_001438566.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Gan,P., Wang,Z., Bezprozvannaya,S., McAnally,J.R., Tan,W., Li,H.,
            Bassel-Duby,R., Liu,N. and Olson,E.N.
  TITLE     RBPMS regulates cardiomyocyte contraction and cardiac function
            through RNA alternative splicing
  JOURNAL   Cardiovasc Res 120 (1), 56-68 (2024)
   PUBMED   37890031
  REMARK    GeneRIF: RBPMS regulates cardiomyocyte contraction and cardiac
            function through RNA alternative splicing.
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Gong,T.T., Liu,F.H., Xiao,Q., Li,Y.Z., Wei,Y.F., Xu,H.L., Cao,F.,
            Sun,M.L., Jiang,F.L., Tao,T., Ma,Q.P., Qin,X., Song,Y., Gao,S.,
            Wu,L., Zhao,Y.H., Huang,D.H. and Wu,Q.J.
  TITLE     SH3RF2 contributes to cisplatin resistance in ovarian cancer cells
            by promoting RBPMS degradation
  JOURNAL   Commun Biol 7 (1), 67 (2024)
   PUBMED   38195842
  REMARK    GeneRIF: SH3RF2 contributes to cisplatin resistance in ovarian
            cancer cells by promoting RBPMS degradation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Yang,Y., Lee,G.C., Nakagaki-Silva,E., Huang,Y., Peacey,M.,
            Partridge,R., Gooding,C. and Smith,C.W.J.
  TITLE     Cell-type specific regulator RBPMS switches alternative splicing
            via higher-order oligomerization and heterotypic interactions with
            other splicing regulators
  JOURNAL   Nucleic Acids Res 51 (18), 9961-9982 (2023)
   PUBMED   37548402
  REMARK    GeneRIF: Cell-type specific regulator RBPMS switches alternative
            splicing via higher-order oligomerization and heterotypic
            interactions with other splicing regulators.
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Bartsch,D., Kalamkar,K., Ahuja,G., Lackmann,J.W., Hescheler,J.,
            Weber,T., Bazzi,H., Clamer,M., Mendjan,S., Papantonis,A. and
            Kurian,L.
  TITLE     mRNA translational specialization by RBPMS presets the competence
            for cardiac commitment in hESCs
  JOURNAL   Sci Adv 9 (13), eade1792 (2023)
   PUBMED   36989351
  REMARK    GeneRIF: mRNA translational specialization by RBPMS presets the
            competence for cardiac commitment in hESCs.
REFERENCE   6  (residues 1 to 159)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   7  (residues 1 to 159)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 159)
  AUTHORS   Sun,Y., Ding,L., Zhang,H., Han,J., Yang,X., Yan,J., Zhu,Y., Li,J.,
            Song,H. and Ye,Q.
  TITLE     Potentiation of Smad-mediated transcriptional activation by the
            RNA-binding protein RBPMS
  JOURNAL   Nucleic Acids Res 34 (21), 6314-6326 (2006)
   PUBMED   17099224
REFERENCE   9  (residues 1 to 159)
  AUTHORS   Hillman,R.T., Green,R.E. and Brenner,S.E.
  TITLE     An unappreciated role for RNA surveillance
  JOURNAL   Genome Biol 5 (2), R8 (2004)
   PUBMED   14759258
REFERENCE   10 (residues 1 to 159)
  AUTHORS   Shimamoto,A., Kitao,S., Ichikawa,K., Suzuki,N., Yamabe,Y.,
            Imamura,O., Tokutake,Y., Satoh,M., Matsumoto,T., Kuromitsu,J.,
            Kataoka,H., Sugawara,K., Sugawara,M., Sugimoto,M., Goto,M. and
            Furuichi,Y.
  TITLE     A unique human gene that spans over 230 kb in the human chromosome
            8p11-12 and codes multiple family proteins sharing RNA-binding
            motifs
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 10913-10917 (1996)
   PUBMED   8855282
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC109329.8, AC011204.6 and
            AC102945.2.
            
            On Apr 22, 2025 this sequence version replaced XP_047277235.1.
            
            Summary: This gene encodes a member of the RNA recognition motif
            family of RNA-binding proteins. The RNA recognition motif is
            between 80-100 amino acids in length and family members contain one
            to four copies of the motif. The RNA recognition motif consists of
            two short stretches of conserved sequence, as well as a few highly
            conserved hydrophobic residues. The encoded protein has a single,
            putative RNA recognition motif in its N-terminus. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Jun 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14243140.964748.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p12"
     Protein         1..159
                     /product="RNA-binding protein with multiple splicing
                     isoform E"
                     /note="heart and RRM expressed sequence; RNA binding
                     protein with multiple splicing"
                     /calculated_mol_wt=17448
     Region          <14..40
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     CDS             1..159
                     /gene="RBPMS"
                     /gene_synonym="HERMES"
                     /coded_by="NM_001438566.1:553..1032"
                     /note="isoform E is encoded by transcript variant 6"
                     /db_xref="GeneID:11030"
                     /db_xref="HGNC:HGNC:19097"
                     /db_xref="MIM:601558"
ORIGIN      
        1 mnnggkaeke ntpseanlqe eegirfdpei pqtlrlefak antkmaknkl vgtpnpstpl
       61 pntvpqfiar epyeltvpal ypsspevwap yplypaelap alpppaftyp aslhaqcfsp
      121 eakpntpvfc pllqqirfvs gnvfvtyqpt adqqrelpc
//
LOCUS       NP_001401106             444 aa            linear   PRI 21-NOV-2025
DEFINITION  lymphocyte activation gene 3 protein isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_001401106 XP_011519258
VERSION     NP_001401106.1
DBSOURCE    REFSEQ: accession NM_001414177.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Du,J., Chen,H., You,J., Hu,W., Liu,J., Lu,Q., Zhang,Y., Gao,J.,
            Lin,M.J., Foster,C.J.R., Rao,E., Cammer,M., Yin,W., Koide,S.,
            Lu,C.P., Chen,W., Lou,J. and Wang,J.
  TITLE     Proximity between LAG-3 and the T cell receptor guides suppression
            of T cell activation and autoimmunity
  JOURNAL   Cell 188 (15), 4025-4042 (2025)
   PUBMED   40592325
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Jiang,Y., Dai,A., Huang,Y., Li,H., Cui,J., Yang,H., Si,L., Jiao,T.,
            Ren,Z., Zhang,Z., Mou,S., Zhu,H., Guo,W., Huang,Q., Li,Y., Xue,M.,
            Jiang,J., Wang,F., Li,L., Zhong,Q., Wang,K., Liu,B., Wang,J.,
            Fan,G., Guo,J., Chen,L., Workman,C.J., Shen,Z., Kong,Y.,
            Vignali,D.A.A., Xu,C. and Wang,H.
  TITLE     Ligand-induced ubiquitination unleashes LAG3 immune checkpoint
            function by hindering membrane sequestration of signaling motifs
  JOURNAL   Cell 188 (9), 2354-2371 (2025)
   PUBMED   40101708
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Wakamatsu,E., Machiyama,H., Toyota,H., Takeuchi,A., Hashimoto,R.,
            Kozono,H. and Yokosuka,T.
  TITLE     Indirect suppression of CD4 T cell activation through
            LAG-3-mediated trans-endocytosis of MHC class II
  JOURNAL   Cell Rep 43 (9), 114655 (2024)
   PUBMED   39191259
  REMARK    GeneRIF: Indirect suppression of CD4 T cell activation through
            LAG-3-mediated trans-endocytosis of MHC class II.
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Perales,O., Jilaveanu,L., Adeniran,A., Su,D.G., Hurwitz,M.,
            Braun,D.A., Kluger,H.M. and Schoenfeld,D.A.
  TITLE     TIGIT expression in renal cell carcinoma infiltrating T cells is
            variable and inversely correlated with PD-1 and LAG3
  JOURNAL   Cancer Immunol Immunother 73 (10), 192 (2024)
   PUBMED   39105820
  REMARK    GeneRIF: TIGIT expression in renal cell carcinoma infiltrating T
            cells is variable and inversely correlated with PD-1 and LAG3.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Saevarsdottir,S., Bjarnadottir,K., Markusson,T., Berglund,J.,
            Olafsdottir,T.A., Halldorsson,G.H., Rutsdottir,G.,
            Gunnarsdottir,K., Arnthorsson,A.O., Lund,S.H., Stefansdottir,L.,
            Gudmundsson,J., Johannesson,A.J., Sturluson,A., Oddsson,A.,
            Halldorsson,B., Ludviksson,B.R., Ferkingstad,E., Ivarsdottir,E.V.,
            Sveinbjornsson,G., Grondal,G., Masson,G., Eldjarn,G.H.,
            Thorisson,G.A., Kristjansdottir,K., Knowlton,K.U., Moore,K.H.S.,
            Gudjonsson,S.A., Rognvaldsson,S., Knight,S., Nadauld,L.D., Holm,H.,
            Magnusson,O.T., Sulem,P., Gudbjartsson,D.F., Rafnar,T.,
            Thorleifsson,G., Melsted,P., Norddahl,G.L., Jonsdottir,I. and
            Stefansson,K.
  TITLE     Start codon variant in LAG3 is associated with decreased LAG-3
            expression and increased risk of autoimmune thyroid disease
  JOURNAL   Nat Commun 15 (1), 5748 (2024)
   PUBMED   38982041
  REMARK    GeneRIF: Start codon variant in LAG3 is associated with decreased
            LAG-3 expression and increased risk of autoimmune thyroid disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Huard,B., Mastrangeli,R., Prigent,P., Bruniquel,D., Donini,S.,
            El-Tayar,N., Maigret,B., Dreano,M. and Triebel,F.
  TITLE     Characterization of the major histocompatibility complex class II
            binding site on LAG-3 protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (11), 5744-5749 (1997)
   PUBMED   9159144
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Bruniquel,D., Borie,N. and Triebel,F.
  TITLE     Genomic organization of the human LAG-3/CD4 locus
  JOURNAL   Immunogenetics 47 (1), 96-98 (1997)
   PUBMED   9382927
REFERENCE   8  (residues 1 to 444)
  AUTHORS   Blum,M.D., Wong,G.T., Higgins,K.M., Sunshine,M.J. and Lacy,E.
  TITLE     Reconstitution of the subclass-specific expression of CD4 in
            thymocytes and peripheral T cells of transgenic mice:
            identification of a human CD4 enhancer
  JOURNAL   J Exp Med 177 (5), 1343-1358 (1993)
   PUBMED   8097522
REFERENCE   9  (residues 1 to 444)
  AUTHORS   Baixeras,E., Huard,B., Miossec,C., Jitsukawa,S., Martin,M.,
            Hercend,T., Auffray,C., Triebel,F. and Piatier-Tonneau,D.
  TITLE     Characterization of the lymphocyte activation gene 3-encoded
            protein. A new ligand for human leukocyte antigen class II antigens
  JOURNAL   J Exp Med 176 (2), 327-337 (1992)
   PUBMED   1380059
REFERENCE   10 (residues 1 to 444)
  AUTHORS   Triebel,F., Jitsukawa,S., Baixeras,E., Roman-Roman,S., Genevee,C.,
            Viegas-Pequignot,E. and Hercend,T.
  TITLE     LAG-3, a novel lymphocyte activation gene closely related to CD4
  JOURNAL   J Exp Med 171 (5), 1393-1405 (1990)
   PUBMED   1692078
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC125494.2.
            
            On Nov 15, 2022 this sequence version replaced XP_011519258.1.
            
            Summary: Lymphocyte-activation protein 3 belongs to Ig superfamily
            and contains 4 extracellular Ig-like domains. The LAG3 gene
            contains 8 exons.  The sequence data, exon/intron organization, and
            chromosomal localization all indicate a close relationship of LAG3
            to CD4. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.369177.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..444
                     /product="lymphocyte activation gene 3 protein isoform 3
                     precursor"
                     /note="lymphocyte activation gene 3 protein;
                     lymphocyte-activation gene 3"
                     /calculated_mol_wt=46010
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2584
     Region          <22..151
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          185..252
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cd00096"
                     /db_xref="CDD:409353"
     Region          185..189
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          199..203
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          224..228
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          238..243
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          267..348
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     CDS             1..444
                     /gene="LAG3"
                     /gene_synonym="CD223"
                     /coded_by="NM_001414177.1:334..1668"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:3902"
                     /db_xref="HGNC:HGNC:6476"
                     /db_xref="MIM:153337"
ORIGIN      
        1 mweaqflgll flqplwvapv kplqpgaevp vvwaqegapa qlpcsptipl qdlsllrrag
       61 vtwqhqpdsg ppaaapghpl apgphpaaps swgprprryt vlsvgpgglr sgrlplqprv
      121 qldergrqrg dfslwlrpar radageyraa vhlrdralsc rlrlrlgqas mtasppgslr
      181 asdwvilncs fsrpdrpasv hwfrnrgqgr vpvresphhh laesflflpq vspmdsgpwg
      241 ciltyrdgfn vsimynltvl glepptpltv yagagsrvgl pcrlpagvgt rsfltakwtp
      301 pgggpdllvt gdngdftlrl edvsqaqagt ytchihlqeq qlnatvtlai itgaqrsgra
      361 pgalpaghll lflilgvlsl lllvtgafgf hlwrrqwrpr rfsaleqgih ppqaqskiee
      421 leqepepepe pepepepepe peql
//
LOCUS       NP_001393535            1150 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 7 [Homo sapiens].
ACCESSION   NP_001393535 XP_047279790
VERSION     NP_001393535.1
DBSOURCE    REFSEQ: accession NM_001406606.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1150)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1150)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1150)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1150)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1150)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1150)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1150)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1150)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1150)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1150)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            On May 18, 2022 this sequence version replaced XP_047279790.1.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1458056.1,
                                           SRR14372079.958400.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1150
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1150
                     /product="hamartin isoform 7"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=128069
     Region          7..719
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          403..787
                     /region_name="Mediates interaction with WDR45B.
                     /evidence=ECO:0000269|PubMed:28561066"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Region          439..571
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <705..>942
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          992..1071
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1086
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1117..1150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1150
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406606.1:189..3641"
                     /note="isoform 7 is encoded by transcript variant 20"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt aggkgtplgt patspppapl chsddyvhis lpqatvtppr
      421 keermdsarp clhrqhhlln drgseeppgs kgsvtlsdlp gflgdlasee dsiekdkeea
      481 aisrelseit taeaepvvpr ggfdspfyrd slpgsqrkth saasssqgas vnpeplhssl
      541 dklgpdtpkq aftpidlpcg sadespagdr ecqtsletsi ftpspckipp ptrvgfgsgq
      601 pppydhlfev alpktahhfv irkteellkk akgnteedgv pstspmevld rliqqgadah
      661 skelnklplp sksvdwthfg gsppsdeirt lrdqllllhn qllyerfkrq qhalrnrrll
      721 rkvikaaale ehnaamkdql klqekdiqmw kvslqkeqar ynqlqeqrdt mvtklhsqir
      781 qlqhdreefy nqsqelqtkl edcrnmiael rielkkannk lsnsesvqqq meflnrqllv
      841 lgevnelyle qlqnkhsdtt kevemmkaay rkeleknrsh vlqqtqrldt sqkrileles
      901 hlakkdhlll eqkkyledvk lqargqlqaa esryeaqkri tqvfeleild lygrlekdgl
      961 lkkleeekae aaeaaeerld ccndgcsdsm vghneeasgh ngetktprps sargssgsrg
     1021 gggsssssse lstpekpphq ragpfssrwe ttmgeasasi pttvgslpss ksflgmkare
     1081 lfrnksesqc dedgmtssls eslktelgkd lgveakipln ldgphpsppt pdsvgqlhim
     1141 dynethhehs
//
LOCUS       NP_001428222             513 aa            linear   PRI 21-NOV-2025
DEFINITION  dynamin-binding protein isoform h [Homo sapiens].
ACCESSION   NP_001428222
VERSION     NP_001428222.1
DBSOURCE    REFSEQ: accession NM_001441293.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Ouyang,C., Mu,J., Lu,Q., Li,J., Zhu,H., Wang,Q., Zou,M.H. and
            Xie,Z.
  TITLE     Autophagic degradation of KAT2A/GCN5 promotes directional migration
            of vascular smooth muscle cells by reducing TUBA/alpha-tubulin
            acetylation
  JOURNAL   Autophagy 16 (10), 1753-1770 (2020)
   PUBMED   31878840
  REMARK    GeneRIF: Autophagic degradation of KAT2A/GCN5 promotes directional
            migration of vascular smooth muscle cells by reducing
            TUBA/alpha-tubulin acetylation.
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Ansar,M., Chung,H.L., Taylor,R.L., Nazir,A., Imtiaz,S.,
            Sarwar,M.T., Manousopoulou,A., Makrythanasis,P., Saeed,S.,
            Falconnet,E., Guipponi,M., Pournaras,C.J., Ansari,M.A., Ranza,E.,
            Santoni,F.A., Ahmed,J., Shah,I., Gul,K., Black,G.C., Bellen,H.J.
            and Antonarakis,S.E.
  TITLE     Bi-allelic Loss-of-Function Variants in DNMBP Cause Infantile
            Cataracts
  JOURNAL   Am J Hum Genet 103 (4), 568-578 (2018)
   PUBMED   30290152
  REMARK    GeneRIF: DNMBP loss-of-function variants cause infantile-onset
            cataracts in humans.
REFERENCE   6  (residues 1 to 513)
  AUTHORS   Minster,R.L., DeKosky,S.T. and Kamboh,M.I.
  TITLE     No association of dynamin binding protein (DNMBP) gene SNPs and
            Alzheimer's disease
  JOURNAL   Neurobiol Aging 29 (10), 1602-1604 (2008)
   PUBMED   17442457
  REMARK    GeneRIF: We observed no association of statistical significance in
            either the total sample or the APOE*4 non-carriers for any of the
            SNPs of Dynamin Binding Protein.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 513)
  AUTHORS   Otani,T., Ichii,T., Aono,S. and Takeichi,M.
  TITLE     Cdc42 GEF Tuba regulates the junctional configuration of simple
            epithelial cells
  JOURNAL   J Cell Biol 175 (1), 135-146 (2006)
   PUBMED   17015620
  REMARK    GeneRIF: Tuba controls the shaping of cell junctions through the
            local activation of Cdc42 and its effectors.
REFERENCE   8  (residues 1 to 513)
  AUTHORS   Kuwano,R., Miyashita,A., Arai,H., Asada,T., Imagawa,M., Shoji,M.,
            Higuchi,S., Urakami,K., Kakita,A., Takahashi,H., Tsukie,T.,
            Toyabe,S., Akazawa,K., Kanazawa,I. and Ihara,Y.
  CONSRTM   Japanese Genetic Study Consortium for Alzeheimer's Disease
  TITLE     Dynamin-binding protein gene on chromosome 10q is associated with
            late-onset Alzheimer's disease
  JOURNAL   Hum Mol Genet 15 (13), 2170-2182 (2006)
   PUBMED   16740596
  REMARK    GeneRIF: Results confirmed DNMBP may be one of the susceptibility
            genes for Alzheimer's disease.
            GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   9  (residues 1 to 513)
  AUTHORS   Cestra,G., Kwiatkowski,A., Salazar,M., Gertler,F. and De Camilli,P.
  TITLE     Tuba, a GEF for CDC42, links dynamin to actin regulatory proteins
  JOURNAL   Methods Enzymol 404, 537-545 (2005)
   PUBMED   16413298
REFERENCE   10 (residues 1 to 513)
  AUTHORS   Salazar,M.A., Kwiatkowski,A.V., Pellegrini,L., Cestra,G.,
            Butler,M.H., Rossman,K.L., Serna,D.M., Sondek,J., Gertler,F.B. and
            De Camilli,P.
  TITLE     Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl
            homology domains, links dynamin to regulation of the actin
            cytoskeleton
  JOURNAL   J Biol Chem 278 (49), 49031-49043 (2003)
   PUBMED   14506234
  REMARK    GeneRIF: functions to bring together dynamin with actin regulatory
            proteins
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL627434.4 and AL392107.17.
            
            Summary: This gene encodes a protein belonging to the guanine
            nucleotide exchange factor family, and which regulates the
            configuration of cell junctions. It contains multiple binding sites
            for dynamin and thus links dynamin to actin regulatory proteins.
            Polymorphisms in this gene have been linked to Alzheimer's disease
            in some populations, though there are conflicting reports of such
            linkages in other populations. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2066260.1,
                                           SRR14372079.2215544.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.2"
     Protein         1..513
                     /product="dynamin-binding protein isoform h"
                     /note="scaffold protein TUBA"
                     /calculated_mol_wt=57766
     Region          <1..144
                     /region_name="BAR_DNMBP"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin
                     Binding Protein; cd07589"
                     /db_xref="CDD:153273"
     Region          225..281
                     /region_name="SH3_DNMBP_C1"
                     /note="First C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11798"
                     /db_xref="CDD:212732"
     Site            order(230,232,235,239,261..262,275,277..278)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212732"
     Region          453..509
                     /region_name="SH3_DNMBP_C2"
                     /note="Second C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba, and similar domains;
                     cd12141"
                     /db_xref="CDD:213017"
     Site            order(458,460,463,467,489..490,503,505..506)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213017"
     CDS             1..513
                     /gene="DNMBP"
                     /gene_synonym="ARHGEF36; CTRCT48; TUBA"
                     /coded_by="NM_001441293.1:1118..2659"
                     /note="isoform h is encoded by transcript variant 9"
                     /db_xref="GeneID:23268"
                     /db_xref="HGNC:HGNC:30373"
                     /db_xref="MIM:611282"
ORIGIN      
        1 mwdvcmergh rdleqfervh ryisdqlftn fkerterlvi splnqllsmf tgphklvqkr
       61 fdklldfync teraeklkdk ktleelqsar nnyealnaql ldelpkfhqy aqglftncvh
      121 gyaeahcdfv hqaleqlkpl lsllkvagre gnliaifhee hsrvlqqlqv ftffpeslpa
      181 tkkpferkti drqsarkpll glpsymlqse elrasllary ppeklfqaer nfnaaqdldv
      241 sllegdlvgv ikkkdpmgsq nrwlidngvt kgfvyssflk pynprrshsd asvgshsste
      301 sehgsssprf prqnsgstlt fnpssmavsf tsgscqkqpq daspppkecd qgtlsaslnp
      361 snsesspsrc psdpdstsqp rsgdsadvar dvkqptatpr syrnfrhpei vgysvpgrng
      421 qsqdlvkgca rtaqapedrs tepdgseaeg nqvyfavytf karnpnelsv sanqklkile
      481 fkdvtgntew wlaevngkkg yvpsnyirkt eyt
//
LOCUS       NP_001424213             750 aa            linear   PRI 21-NOV-2025
DEFINITION  signal transducer and activator of transcription 1-alpha/beta
            isoform alpha [Homo sapiens].
ACCESSION   NP_001424213 XP_006712781 XP_054199535
VERSION     NP_001424213.1
DBSOURCE    REFSEQ: accession NM_001437284.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 750)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 750)
  AUTHORS   Wang,Y., Song,Q., Huang,W., Lin,Y., Wang,X., Wang,C., Willard,B.,
            Zhao,C., Nan,J., Holvey-Bates,E., Wang,Z., Taylor,D., Yang,J. and
            Stark,G.R.
  TITLE     A virus-induced conformational switch of STAT1-STAT2 dimers boosts
            antiviral defenses
  JOURNAL   Cell Res 31 (2), 206-218 (2021)
   PUBMED   32759968
REFERENCE   3  (residues 1 to 750)
  AUTHORS   Decker,T. and Kovarik,P.
  TITLE     Serine phosphorylation of STATs
  JOURNAL   Oncogene 19 (21), 2628-2637 (2000)
   PUBMED   10851062
  REMARK    Review article
REFERENCE   4  (residues 1 to 750)
  AUTHORS   Bowman,T., Garcia,R., Turkson,J. and Jove,R.
  TITLE     STATs in oncogenesis
  JOURNAL   Oncogene 19 (21), 2474-2488 (2000)
   PUBMED   10851046
  REMARK    Review article
REFERENCE   5  (residues 1 to 750)
  AUTHORS   Haddad,B., Pabon-Pena,C.R., Young,H. and Sun,W.H.
  TITLE     Assignment1 of STAT1 to human chromosome 2q32 by FISH and radiation
            hybrids
  JOURNAL   Cytogenet Cell Genet 83 (1-2), 58-59 (1998)
   PUBMED   9925928
REFERENCE   6  (residues 1 to 750)
  AUTHORS   Yan,R., Qureshi,S., Zhong,Z., Wen,Z. and Darnell,J.E. Jr.
  TITLE     The genomic structure of the STAT genes: multiple exons in
            coincident sites in Stat1 and Stat2
  JOURNAL   Nucleic Acids Res 23 (3), 459-463 (1995)
   PUBMED   7885841
REFERENCE   7  (residues 1 to 750)
  AUTHORS   Igarashi,K., Garotta,G., Ozmen,L., Ziemiecki,A., Wilks,A.F.,
            Harpur,A.G., Larner,A.C. and Finbloom,D.S.
  TITLE     Interferon-gamma induces tyrosine phosphorylation of
            interferon-gamma receptor and regulated association of protein
            tyrosine kinases, Jak1 and Jak2, with its receptor
  JOURNAL   J Biol Chem 269 (20), 14333-14336 (1994)
   PUBMED   7514165
REFERENCE   8  (residues 1 to 750)
  AUTHORS   Shuai,K., Horvath,C.M., Huang,L.H., Qureshi,S.A., Cowburn,D. and
            Darnell,J.E. Jr.
  TITLE     Interferon activation of the transcription factor Stat91 involves
            dimerization through SH2-phosphotyrosyl peptide interactions
  JOURNAL   Cell 76 (5), 821-828 (1994)
   PUBMED   7510216
REFERENCE   9  (residues 1 to 750)
  AUTHORS   Schindler,C., Fu,X.Y., Improta,T., Aebersold,R. and Darnell,J.E.
            Jr.
  TITLE     Proteins of transcription factor ISGF-3: one gene encodes the
            91-and 84-kDa ISGF-3 proteins that are activated by interferon
            alpha
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7836-7839 (1992)
   PUBMED   1502203
REFERENCE   10 (residues 1 to 750)
  AUTHORS   Schindler,C., Shuai,K., Prezioso,V.R. and Darnell,J.E. Jr.
  TITLE     Interferon-dependent tyrosine phosphorylation of a latent
            cytoplasmic transcription factor
  JOURNAL   Science 257 (5071), 809-813 (1992)
   PUBMED   1496401
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC067945.4.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_006712781.1, XP_054199535.1.
            
            Summary: The protein encoded by this gene is a member of the STAT
            protein family. In response to cytokines and growth factors, STAT
            family members are phosphorylated by the receptor associated
            kinases, and then form homo- or heterodimers that translocate to
            the cell nucleus where they act as transcription activators. The
            protein encoded by this gene can be activated by various ligands
            including interferon-alpha, interferon-gamma, EGF, PDGF and IL6.
            This protein mediates the expression of a variety of genes, which
            is thought to be important for cell viability in response to
            different cell stimuli and pathogens. The protein plays an
            important role in immune responses to viral, fungal and
            mycobacterial pathogens. Mutations in this gene are associated with
            Immunodeficiency 31B, 31A, and 31C. [provided by RefSeq, Jun 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1230515.1,
                                           SRR18074967.2617002.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..750
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.2"
     Protein         1..750
                     /product="signal transducer and activator of transcription
                     1-alpha/beta isoform alpha"
                     /note="transcription factor ISGF-3 components p91/p84;
                     signal transducer and activator of transcription
                     1-alpha/beta; signal transducer and activator of
                     transcription 1, 91kD; signal transducer and activator of
                     transcription 1, 91kDa"
                     /calculated_mol_wt=87204
     Region          2..121
                     /region_name="STAT_int"
                     /note="STAT protein, protein interaction domain;
                     smart00964"
                     /db_xref="CDD:214942"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            114
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Region          138..313
                     /region_name="STAT1_CCD"
                     /note="Coiled-coil domain of Signal Transducer and
                     Activator of Transcription 1 (STAT1); cd16851"
                     /db_xref="CDD:341076"
     Site            order(164..165,168..169,172,175..176,179,232,236,239..241,
                     243..244,256..257,259..260,263..264,267,271,274,306,
                     309..311)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:341076"
     Site            175
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            order(239..241,243..244,256..257,260,263..264,267,271,274,
                     302,306,309..310)
                     /site_type="other"
                     /note="CCD-DBD interface [polypeptide binding]"
                     /db_xref="CDD:341076"
     Site            296
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Region          317..477
                     /region_name="STAT1_DBD"
                     /note="DNA-binding domain of Signal Transducer and
                     Activator of Transcription 1 (STAT1); cd16845"
                     /db_xref="CDD:341083"
     Site            order(336,340,378,411,413,426..427,459..460,463)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:341083"
     Site            366
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            525
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Region          557..707
                     /region_name="SH2_STAT1"
                     /note="Src homology 2 (SH2) domain found in signal
                     transducer and activator of transcription (STAT) 1
                     proteins; cd10372"
                     /db_xref="CDD:198235"
     Site            order(584,602,630,632)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198235"
     Site            order(631,647)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198235"
     Site            637
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            order(641..642,706)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:198235"
     Site            665
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:28753426; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            701
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK1, JAK2 or TYK2.
                     /evidence=ECO:0000269|PubMed:17561467,
                     ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:21135090,
                     ECO:0000269|PubMed:22065572, ECO:0000269|PubMed:26479788,
                     ECO:0000269|PubMed:27796300, ECO:0000269|PubMed:28753426,
                     ECO:0000269|PubMed:38621137, ECO:0000269|PubMed:7657660;
                     propagated from UniProtKB/Swiss-Prot (P42224.2)"
     Site            708
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKE.
                     /evidence=ECO:0000269|PubMed:22065572; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Region          715..739
                     /region_name="STAT1_TAZ2bind"
                     /note="STAT1 TAZ2 binding domain; pfam12162"
                     /db_xref="CDD:432372"
     Site            724
                     /site_type="other"
                     /note="Required for recruitment of EP300/p300.
                     /evidence=ECO:0000269|PubMed:16257975; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            727
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CAMK2 and MAPK14.
                     /evidence=ECO:0000269|PubMed:11972023,
                     ECO:0000269|PubMed:15322115, ECO:0000269|PubMed:16257975,
                     ECO:0000269|PubMed:17897103, ECO:0000269|PubMed:21135090,
                     ECO:0000269|PubMed:22065572, ECO:0000269|PubMed:26479788,
                     ECO:0000269|PubMed:38621137, ECO:0000269|PubMed:7543024,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            745
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKE.
                     /evidence=ECO:0000250|UniProtKB:P42225; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     Site            749
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by IKKB.
                     /evidence=ECO:0000269|PubMed:32209697,
                     ECO:0000269|PubMed:38621137; propagated from
                     UniProtKB/Swiss-Prot (P42224.2)"
     CDS             1..750
                     /gene="STAT1"
                     /gene_synonym="CANDF7; IMD31A; IMD31B; IMD31C; ISGF-3;
                     STAT91"
                     /coded_by="NM_001437284.1:156..2408"
                     /note="isoform alpha is encoded by transcript variant 13"
                     /db_xref="GeneID:6772"
                     /db_xref="HGNC:HGNC:11362"
                     /db_xref="MIM:600555"
ORIGIN      
        1 msqwyelqql dskfleqvhq lyddsfpmei rqylaqwlek qdwehaandv sfatirfhdl
       61 lsqlddqysr fslennfllq hnirkskrnl qdnfqedpiq msmiiysclk eerkilenaq
      121 rfnqaqsgni qstvmldkqk eldskvrnvk dkvmciehei ksledlqdey dfkcktlqnr
      181 ehetngvaks dqkqeqlllk kmylmldnkr kevvhkiiel lnvteltqna lindelvewk
      241 rrqqsacigg ppnacldqlq nwftivaesl qqvrqqlkkl eeleqkytye hdpitknkqv
      301 lwdrtfslfq qliqssfvve rqpcmpthpq rplvlktgvq ftvklrllvk lqelnynlkv
      361 kvlfdkdvne rntvkgfrkf nilgthtkvm nmeestngsl aaefrhlqlk eqknagtrtn
      421 egplivteel hslsfetqlc qpglvidlet tslpvvvisn vsqlpsgwas ilwynmlvae
      481 prnlsffltp pcarwaqlse vlswqfssvt krglnvdqln mlgekllgpn aspdglipwt
      541 rfckenindk nfpfwlwies ilelikkhll plwndgcimg fiskereral lkdqqpgtfl
      601 lrfsessreg aitftwvers qnggepdfha vepytkkels avtfpdiirn ykvmaaenip
      661 enplkylypn idkdhafgky ysrpkeapep meldgpkgtg yiktelisvs evhpsrlqtt
      721 dnllpmspee fdevsrivgs vefdsmmntv
//
LOCUS       NP_001425387             589 aa            linear   PRI 21-NOV-2025
DEFINITION  excitatory amino acid transporter 1 isoform 6 [Homo sapiens].
ACCESSION   NP_001425387
VERSION     NP_001425387.1
DBSOURCE    REFSEQ: accession NM_001438458.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Albury,C.L., Sutherland,H.G., Lam,A.W.Y., Tran,N.K., Lea,R.A.,
            Haupt,L.M. and Griffiths,L.R.
  TITLE     Identification of Polymorphisms in EAAT1 Glutamate Transporter Gene
            SLC1A3 Associated with Reduced Migraine Risk
  JOURNAL   Genes (Basel) 15 (6), 797 (2024)
   PUBMED   38927733
  REMARK    GeneRIF: Identification of Polymorphisms in EAAT1 Glutamate
            Transporter Gene SLC1A3 Associated with Reduced Migraine Risk.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Welby,E. and Ebert,A.D.
  TITLE     Diminished motor neuron activity driven by abnormal astrocytic
            EAAT1 glutamate transporter activity in spinal muscular atrophy is
            not fully restored after lentiviral SMN delivery
  JOURNAL   Glia 71 (5), 1311-1332 (2023)
   PUBMED   36655314
  REMARK    GeneRIF: Diminished motor neuron activity driven by abnormal
            astrocytic EAAT1 glutamate transporter activity in spinal muscular
            atrophy is not fully restored after lentiviral SMN delivery.
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 589)
  AUTHORS   Pant,S., Wu,Q., Ryan,R. and Tajkhorshid,E.
  TITLE     Microscopic Characterization of the Chloride Permeation Pathway in
            the Human Excitatory Amino Acid Transporter 1 (EAAT1)
  JOURNAL   ACS Chem Neurosci 13 (6), 776-785 (2022)
   PUBMED   35192345
  REMARK    GeneRIF: Microscopic Characterization of the Chloride Permeation
            Pathway in the Human Excitatory Amino Acid Transporter 1 (EAAT1).
REFERENCE   5  (residues 1 to 589)
  AUTHORS   Lee,A., Anderson,A.R., Beasley,S.J., Barnett,N.L., Poronnik,P. and
            Pow,D.V.
  TITLE     A new splice variant of the glutamate-aspartate transporter:
            cloning and immunolocalization of GLAST1c in rat, pig and human
            brains
  JOURNAL   J Chem Neuroanat 43 (1), 52-63 (2012)
   PUBMED   22026960
REFERENCE   6  (residues 1 to 589)
  AUTHORS   Vallejo-Illarramendi,A., Domercq,M. and Matute,C.
  TITLE     A novel alternative splicing form of excitatory amino acid
            transporter 1 is a negative regulator of glutamate uptake
  JOURNAL   J Neurochem 95 (2), 341-348 (2005)
   PUBMED   16042756
  REMARK    GeneRIF: EAAT1ex9skip splice variant is a negative regulator of
            full-length EAAT1 function in the human brain
REFERENCE   7  (residues 1 to 589)
  AUTHORS   Takai,S., Yamada,K., Kawakami,H., Tanaka,K. and Nakamura,S.
  TITLE     Localization of the gene (SLC1A3) encoding human glutamate
            transporter (GluT-1) to 5p13 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 209-210 (1995)
   PUBMED   7698014
REFERENCE   8  (residues 1 to 589)
  AUTHORS   Shashidharan,P., Huntley,G.W., Meyer,T., Morrison,J.H. and
            Plaitakis,A.
  TITLE     Neuron-specific human glutamate transporter: molecular cloning,
            characterization and expression in human brain
  JOURNAL   Brain Res 662 (1-2), 245-250 (1994)
   PUBMED   7859077
REFERENCE   9  (residues 1 to 589)
  AUTHORS   Arriza,J.L., Fairman,W.A., Wadiche,J.I., Murdoch,G.H.,
            Kavanaugh,M.P. and Amara,S.G.
  TITLE     Functional comparisons of three glutamate transporter subtypes
            cloned from human motor cortex
  JOURNAL   J Neurosci 14 (9), 5559-5569 (1994)
   PUBMED   7521911
REFERENCE   10 (residues 1 to 589)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010631.6 and AC008957.7.
            
            Summary: This gene encodes a member of a member of a high affinity
            glutamate transporter family. This gene functions in the
            termination of excitatory neurotransmission in central nervous
            system. Mutations are associated with episodic ataxia, Type 6.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.175920.1,
                                           SRR14038196.1464821.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..589
                     /product="excitatory amino acid transporter 1 isoform 6"
                     /note="excitatory amino acid transporter 1; GLAST-1;
                     sodium-dependent glutamate/aspartate transporter 1; solute
                     carrier family 1 (glial high affinity glutamate
                     transporter), member 3"
                     /calculated_mol_wt=64954
     Region          46..543
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     CDS             1..589
                     /gene="SLC1A3"
                     /gene_synonym="EA6; EAAT1; GLAST; GLAST1"
                     /coded_by="NM_001438458.1:226..1995"
                     /note="isoform 6 is encoded by transcript variant 10"
                     /db_xref="GeneID:6507"
                     /db_xref="HGNC:HGNC:10941"
                     /db_xref="MIM:600111"
ORIGIN      
        1 mtksngeepk mggrmerfqq gvrkrtllak kkvqnitked vksylfrnaf vlltvtaviv
       61 gtilgftlrp yrmsyrevky fsfpgellmr mlqmlvlpli isslvtgmaa ldskasgkmg
      121 mravvyymtt tiiavvigii iviiihpgkg tkenmhregk ivrvtaadaf ldlirnmfpp
      181 nlveacfkqf ktnyekrsfk vpiqanetlv gavinnvsea metltritee lvpvpgsvng
      241 vnalglvvfs mcfgfvignm keqgqalref fdslneaimr lvavimwskr ktlcprails
      301 egkarfcknq gkfiftkekk evhsfckkrs pqflyapvgi lfliagkive medmgviggq
      361 lamytvtviv gllihavivl pllyflvtrk npwvfiggll qalitalgts sssatlpitf
      421 kcleenngvd krvtrfvlpv gatinmdgta lyealaaifi aqvnnfelnf gqiitisita
      481 taasigaagi pqaglvtmvi vltsvglptd ditliiavdw fldrlrtttn vlgdslgagi
      541 vehlsrhelk nrdvemgnsv ieenemkkpy qliaqdnete kpidsetkm
//
LOCUS       NP_001397655             410 aa            linear   PRI 21-NOV-2025
DEFINITION  Golgi reassembly-stacking protein 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001397655 XP_016862539
VERSION     NP_001397655.1
DBSOURCE    REFSEQ: accession NM_001410726.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Ahat,E., Song,Y., Xia,K., Reid,W., Li,J., Bui,S., Zhang,F.,
            Linhardt,R.J. and Wang,Y.
  TITLE     GRASP depletion-mediated Golgi fragmentation impairs
            glycosaminoglycan synthesis, sulfation, and secretion
  JOURNAL   Cell Mol Life Sci 79 (4), 199 (2022)
   PUBMED   35312866
  REMARK    GeneRIF: GRASP depletion-mediated Golgi fragmentation impairs
            glycosaminoglycan synthesis, sulfation, and secretion.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Zhang,Y. and Seemann,J.
  TITLE     Rapid degradation of GRASP55 and GRASP65 reveals their immediate
            impact on the Golgi structure
  JOURNAL   J Cell Biol 220 (1) (2021)
   PUBMED   33301566
  REMARK    GeneRIF: Rapid degradation of GRASP55 and GRASP65 reveals their
            immediate impact on the Golgi structure.
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Sutterlin,C., Lin,C.Y., Feng,Y., Ferris,D.K., Erikson,R.L. and
            Malhotra,V.
  TITLE     Polo-like kinase is required for the fragmentation of
            pericentriolar Golgi stacks during mitosis
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 9128-9132 (2001)
   PUBMED   11447294
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Moyer,B.D., Allan,B.B. and Balch,W.E.
  TITLE     Rab1 interaction with a GM130 effector complex regulates COPII
            vesicle cis--Golgi tethering
  JOURNAL   Traffic 2 (4), 268-276 (2001)
   PUBMED   11285137
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Lin,C.Y., Madsen,M.L., Yarm,F.R., Jang,Y.J., Liu,X. and
            Erikson,R.L.
  TITLE     Peripheral Golgi protein GRASP65 is a target of mitotic polo-like
            kinase (Plk) and Cdc2
  JOURNAL   Proc Natl Acad Sci U S A 97 (23), 12589-12594 (2000)
   PUBMED   11050165
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Barr,F.A., Nakamura,N. and Warren,G.
  TITLE     Mapping the interaction between GRASP65 and GM130, components of a
            protein complex involved in the stacking of Golgi cisternae
  JOURNAL   EMBO J 17 (12), 3258-3268 (1998)
   PUBMED   9628863
  REMARK    GeneRIF: A study showing that GRASP65 binds directly to the
            coiled-coil vesicle tethering factor GM130, and targets it to Golgi
            membranes.
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Barr,F.A., Puype,M., Vandekerckhove,J. and Warren,G.
  TITLE     GRASP65, a protein involved in the stacking of Golgi cisternae
  JOURNAL   Cell 91 (2), 253-262 (1997)
   PUBMED   9346242
  REMARK    GeneRIF: Identification of GRASP65, and demonstration that it
            functions in the formation of stacked Golgi cisternae.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC138124.2.
            
            On Aug 15, 2022 this sequence version replaced XP_016862539.1.
            
            Summary: The Golgi complex plays a key role in the sorting and
            modification of proteins exported from the endoplasmic reticulum.
            The protein encoded by this gene is a membrane protein involved in
            establishing the stacked structure of the Golgi apparatus. It is a
            caspase-3 substrate, and cleavage of this encoded protein
            contributes to Golgi fragmentation in apoptosis. This encoded
            protein can form a complex with the Golgi matrix protein GOLGA2,
            and this complex binds to the vesicle docking protein p115.
            Alternative splicing results in multiple transcript variants of
            this gene. [provided by RefSeq, Jul 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.838845.1,
                                           SRR14038192.968511.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.2"
     Protein         1..410
                     /product="Golgi reassembly-stacking protein 1 isoform 4"
                     /note="Golgi reassembly and stacking protein 1; Golgi
                     phosphoprotein 5; Golgi peripheral membrane protein p65;
                     golgi reassembly-stacking protein of 65 kDa; golgi
                     reassembly stacking protein 1, 65kDa; Golgi
                     reassembly-stacking protein 1"
                     /calculated_mol_wt=43294
     Region          3..100
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     Region          69..>175
                     /region_name="GRASP55_65"
                     /note="GRASP55/65 PDZ-like domain; pfam04495"
                     /db_xref="CDD:427981"
     Region          <95..265
                     /region_name="GRH1"
                     /note="Peripheral Golgi membrane protein [Intracellular
                     trafficking and secretion]; COG5233"
                     /db_xref="CDD:227558"
     CDS             1..410
                     /gene="GORASP1"
                     /gene_synonym="GOLPH5; GRASP65; P65"
                     /coded_by="NM_001410726.1:87..1319"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS93246.1"
                     /db_xref="GeneID:64689"
                     /db_xref="HGNC:HGNC:16769"
                     /db_xref="MIM:606867"
ORIGIN      
        1 mglgvsaeqp aggaegfhlh gvqenspaqq aglepyfdfi itighsrlnk endtlkallk
       61 anvekpvkle vfnmktmrvr evevvpsnmw ggqgllgasv rfcsfrrase qvwhvldvep
      121 sspaalaglr pytdyvvgsd qilqesedff tlieshegkp lklmvynsks dscreppsyh
      181 kkppgtppps alplgapppd alppgptped spsletgsrq sdymeallqa pgssmedplp
      241 gpgspshsap dpdglphfme tplqppppvq rvmdpgfldv sgislldnsn asvwpslpss
      301 teltttavst sgpedicsss ssherggeat wsgsefevsf ldspgaqaqa dhlpqltlpd
      361 sltsaasped glsaelleaq aeeepasteg ldtgteaegl dsqaqistte
//
LOCUS       NP_001427683             515 aa            linear   PRI 21-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform p [Homo sapiens].
ACCESSION   NP_001427683 XP_011535343 XP_054232486
VERSION     NP_001427683.1
DBSOURCE    REFSEQ: accession NM_001440754.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 515)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 515)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 515)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 515)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 515)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 515)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            On or before May 28, 2025 this sequence version replaced
            XP_011535343.1, XP_054232486.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3785118.1,
                                           SRR18074967.1879449.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..515
                     /product="lysosomal cobalamin transporter ABCD4 isoform p"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=56891
     Region          <100..512
                     /region_name="YddA"
                     /note="ABC-type uncharacterized transport system, permease
                     and ATPase components [General function prediction only];
                     COG4178"
                     /db_xref="CDD:443337"
     CDS             1..515
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_001440754.1:23..1570"
                     /note="isoform p is encoded by transcript variant 37"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 mavagpapga garprldlqf lqrflqilkv lfpswssqna lmfltllclt llgtsasart
       61 wsdsagssaa wpassssprs pssttltsas kgwlgpvsif gyfilgtvvn ktlmgpivmk
      121 lvhqeklegd frfkhmqirv naepaafyra ghvehmrtdr rlqrllqtqr elmskelwly
      181 igintfdylg silsyvviai pifsgvygdl spaelstlvs knafvciyli scftqlidls
      241 ttlsdvagyt hrigqlretl ldmslksqdc eilgesewgl dtppgwpaae padtafller
      301 vsisapssdk plikdlslki segqsllitg ntgtgktsll rvlgglwtst rgsvqmltdf
      361 gphgvlflpq kpfftdgtlr eqviyplkev ypdsgsadde rilrflelag lsnlvarteg
      421 ldqqvdwnwy dvlspgemqr lsfarlfylq pkyavldeat salteevese lyrigqqlgm
      481 tfisvghrqs lekfhslvlk lcgggrwelm rikve
//
LOCUS       NP_001427434             604 aa            linear   PRI 21-NOV-2025
DEFINITION  radixin isoform 1 [Homo sapiens].
ACCESSION   NP_001427434
VERSION     NP_001427434.1
DBSOURCE    REFSEQ: accession NM_001440505.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Kruse,T., Benz,C., Garvanska,D.H., Lindqvist,R., Mihalic,F.,
            Coscia,F., Inturi,R., Sayadi,A., Simonetti,L., Nilsson,E., Ali,M.,
            Kliche,J., Moliner Morro,A., Mund,A., Andersson,E., McInerney,G.,
            Mann,M., Jemth,P., Davey,N.E., Overby,A.K., Nilsson,J. and
            Ivarsson,Y.
  TITLE     Large scale discovery of coronavirus-host factor protein
            interaction motifs reveals SARS-CoV-2 specific mechanisms and
            vulnerabilities
  JOURNAL   Nat Commun 12 (1), 6761 (2021)
   PUBMED   34799561
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Stemmer-Rachamimov,A.O., Gonzalez-Agosti,C., Xu,L., Burwick,J.A.,
            Beauchamp,R., Pinney,D., Louis,D.N. and Ramesh,V.
  TITLE     Expression of NF2-encoded merlin and related ERM family proteins in
            the human central nervous system
  JOURNAL   J Neuropathol Exp Neurol 56 (6), 735-742 (1997)
   PUBMED   9184664
REFERENCE   7  (residues 1 to 604)
  AUTHORS   Hirao,M., Sato,N., Kondo,T., Yonemura,S., Monden,M., Sasaki,T.,
            Takai,Y., Tsukita,S. and Tsukita,S.
  TITLE     Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma
            membrane association: possible involvement of phosphatidylinositol
            turnover and Rho-dependent signaling pathway
  JOURNAL   J Cell Biol 135 (1), 37-51 (1996)
   PUBMED   8858161
REFERENCE   8  (residues 1 to 604)
  AUTHORS   Wilgenbus,K.K., Milatovich,A., Francke,U. and Furthmayr,H.
  TITLE     Molecular cloning, cDNA sequence, and chromosomal assignment of the
            human radixin gene and two dispersed pseudogenes
  JOURNAL   Genomics 16 (1), 199-206 (1993)
   PUBMED   8486357
REFERENCE   9  (residues 1 to 604)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 604)
  AUTHORS   Sato,N., Funayama,N., Nagafuchi,A., Yonemura,S., Tsukita,S. and
            Tsukita,S.
  TITLE     A gene family consisting of ezrin, radixin and moesin. Its specific
            localization at actin filament/plasma membrane association sites
  JOURNAL   J Cell Sci 103 (Pt 1), 131-143 (1992)
   PUBMED   1429901
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002788.3 and AP000901.5.
            
            Summary: Radixin is a cytoskeletal protein that may be important in
            linking actin to the plasma membrane. It is highly similar in
            sequence to both ezrin and moesin. The radixin gene has been
            localized by fluorescence in situ hybridization to 11q23. A
            truncated version representing a pseudogene (RDXP2) was assigned to
            Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was
            mapped to 11p by Southern and PCR analyses. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.4284254.1,
                                           SRR14038194.1208700.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..604
                     /product="radixin isoform 1"
                     /calculated_mol_wt=70918
     Region          7..206
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          200..296
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(242..243,245..251,260,281,284..285,288)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(242,245..252,260,281,284..285,288)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(278,282)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            281..296
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          310..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35241.1)"
     Region          347..456
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          376..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35241.1)"
     Region          462..526
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35241.1)"
     Region          507..583
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ROCK2.
                     /evidence=ECO:0000250|UniProtKB:P26043; propagated from
                     UniProtKB/Swiss-Prot (P35241.1)"
     CDS             1..604
                     /gene="RDX"
                     /gene_synonym="DFNB24"
                     /coded_by="NM_001440505.1:213..2027"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="GeneID:5962"
                     /db_xref="HGNC:HGNC:9944"
                     /db_xref="MIM:179410"
ORIGIN      
        1 mpkpinvrvt tmdaelefai qpnttgkqlf dqvvktvglr evwffglqyv dskgystwlk
       61 lnkkvtqqdv kkenplqfkf rakffpedvs eeliqeitqr lfflqvkeai lndeiycppe
      121 tavllasyav qakygdynke ihkpgyland rllpqrvleq hkltkeqwee riqnwheehr
      181 gmlredsmme ylkiaqdlem ygvnyfeikn kkgtelwlgv dalglniyeh ddkltpkigf
      241 pwseirnisf ndkkfvikpi dkkapdfvfy aprlrinkri lalcmgnhel ymrrrkpdti
      301 evqqmkaqar eekhqkqler aqlenekkkr eiaekekeri erekeelmer lkqieeqtik
      361 aqkeleeqtr kaleldqerk rakeeaerle kerraaeeak saiakqaadq mknqeqlaae
      421 laeftakial leeakkkkee eatewqhkaf aaqedlektk eelktvmsap pppppppvip
      481 ptenehdehd ennaeasael snegvmnhrs eeervtetqk nervkkqlqa lsselaqard
      541 etkktqndvl haenvkagrd kyktlrqirq gntkqridef eamwgpklya lfqmrscqss
      601 ikqm
//
LOCUS       NP_001426075             567 aa            linear   PRI 21-NOV-2025
DEFINITION  tyrosine-protein kinase Lck isoform c [Homo sapiens].
ACCESSION   NP_001426075 XP_024302814 XP_054192534
VERSION     NP_001426075.1
DBSOURCE    REFSEQ: accession NM_001439146.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Du,J., Chen,H., You,J., Hu,W., Liu,J., Lu,Q., Zhang,Y., Gao,J.,
            Lin,M.J., Foster,C.J.R., Rao,E., Cammer,M., Yin,W., Koide,S.,
            Lu,C.P., Chen,W., Lou,J. and Wang,J.
  TITLE     Proximity between LAG-3 and the T cell receptor guides suppression
            of T cell activation and autoimmunity
  JOURNAL   Cell 188 (15), 4025-4042 (2025)
   PUBMED   40592325
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Deng,S., Zhang,Y., Wang,H., Liang,W., Xie,L., Li,N., Fang,Y.,
            Wang,Y., Liu,J., Chi,H., Sun,Y., Ye,R., Shan,L., Shi,J., Shen,Z.,
            Wang,Y., Wang,S., Brosseau,J.P., Wang,F., Liu,G., Quan,Y. and Xu,J.
  TITLE     ITPRIPL1 binds CD3epsilon to impede T cell activation and enable
            tumor immune evasion
  JOURNAL   Cell 187 (9), 2305-2323 (2024)
   PUBMED   38614099
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Jaeger-Ruckstuhl,C.A., Lo,Y., Fulton,E., Waltner,O.G.,
            Shabaneh,T.B., Simon,S., Muthuraman,P.V., Correnti,C.E.,
            Newsom,O.J., Engstrom,I.A., Kanaan,S.B., Bhise,S.S.,
            Peralta,J.M.C., Ruff,R., Price,J.P., Stull,S.M., Stevens,A.R.,
            Bugos,G., Kluesner,M.G., Voillet,V., Muhunthan,V., Morrish,F.,
            Olson,J.M., Gottardo,R., Sarthy,J.F., Henikoff,S., Sullivan,L.B.,
            Furlan,S.N. and Riddell,S.R.
  TITLE     Signaling via a CD27-TRAF2-SHP-1 axis during naive T cell
            activation promotes memory-associated gene regulatory networks
  JOURNAL   Immunity 57 (2), 287-302 (2024)
   PUBMED   38354704
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Keller,B., Kfir-Erenfeld,S., Matusewicz,P., Hartl,F., Lev,A.,
            Lee,Y.N., Simon,A.J., Stauber,T., Elpeleg,O., Somech,R.,
            Stepensky,P., Minguet,S., Schraven,B. and Warnatz,K.
  TITLE     Combined Immunodeficiency Caused by a Novel Nonsense Mutation in
            LCK
  JOURNAL   J Clin Immunol 44 (1), 4 (2023)
   PUBMED   38112969
  REMARK    GeneRIF: Combined Immunodeficiency Caused by a Novel Nonsense
            Mutation in LCK.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 567)
  AUTHORS   Lanz,A.L., Erdem,S., Ozcan,A., Ceylaner,G., Cansever,M.,
            Ceylaner,S., Conca,R., Magg,T., Acuto,O., Latour,S., Klein,C.,
            Patiroglu,T., Unal,E., Eken,A. and Hauck,F.
  TITLE     A Novel Biallelic LCK Variant Resulting in Profound T-Cell Immune
            Deficiency and Review of the Literature
  JOURNAL   J Clin Immunol 44 (1), 1 (2023)
   PUBMED   38100037
  REMARK    GeneRIF: A Novel Biallelic LCK Variant Resulting in Profound T-Cell
            Immune Deficiency and Review of the Literature.
            Review article
            Erratum:[J Clin Immunol. 2024 Jan 16;44(1):41. doi:
            10.1007/s10875-024-01654-4. PMID: 38225415]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 567)
  AUTHORS   Shenoy-Scaria,A.M., Kwong,J., Fujita,T., Olszowy,M.W., Shaw,A.S.
            and Lublin,D.M.
  TITLE     Signal transduction through decay-accelerating factor. Interaction
            of glycosyl-phosphatidylinositol anchor and protein tyrosine
            kinases p56lck and p59fyn 1
  JOURNAL   J Immunol 149 (11), 3535-3541 (1992)
   PUBMED   1385527
REFERENCE   7  (residues 1 to 567)
  AUTHORS   Alai,M., Mui,A.L., Cutler,R.L., Bustelo,X.R., Barbacid,M. and
            Krystal,G.
  TITLE     Steel factor stimulates the tyrosine phosphorylation of the
            proto-oncogene product, p95vav, in human hemopoietic cells
  JOURNAL   J Biol Chem 267 (25), 18021-18025 (1992)
   PUBMED   1381360
REFERENCE   8  (residues 1 to 567)
  AUTHORS   Weber,J.R., Bell,G.M., Han,M.Y., Pawson,T. and Imboden,J.B.
  TITLE     Association of the tyrosine kinase LCK with phospholipase C-gamma 1
            after stimulation of the T cell antigen receptor
  JOURNAL   J Exp Med 176 (2), 373-379 (1992)
   PUBMED   1500851
REFERENCE   9  (residues 1 to 567)
  AUTHORS   Molina,T.J., Kishihara,K., Siderovski,D.P., van Ewijk,W.,
            Narendran,A., Timms,E., Wakeham,A., Paige,C.J., Hartmann,K.U.,
            Veillette,A. et al.
  TITLE     Profound block in thymocyte development in mice lacking p56lck
  JOURNAL   Nature 357 (6374), 161-164 (1992)
   PUBMED   1579166
REFERENCE   10 (residues 1 to 567)
  AUTHORS   Levinson,A.D., Oppermann,H., Levintow,L., Varmus,H.E. and
            Bishop,J.M.
  TITLE     Evidence that the transforming gene of avian sarcoma virus encodes
            a protein kinase associated with a phosphoprotein
  JOURNAL   Cell 15 (2), 561-572 (1978)
   PUBMED   214242
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121991.50 and AL109945.15.
            
            On or before Apr 28, 2025 this sequence version replaced
            XP_024302814.1, XP_054192534.1.
            
            Summary: This gene is a member of the Src family of protein
            tyrosine kinases (PTKs). The encoded protein is a key signaling
            molecule in the selection and maturation of developing T-cells. It
            contains N-terminal sites for myristylation and palmitylation, a
            PTK domain, and SH2 and SH3 domains which are involved in mediating
            protein-protein interactions with phosphotyrosine-containing and
            proline-rich motifs, respectively. The protein localizes to the
            plasma membrane and pericentrosomal vesicles, and binds to cell
            surface receptors, including CD4 and CD8, and other signaling
            molecules. Multiple alternatively spliced variants encoding
            different isoforms have been described. [provided by RefSeq, Aug
            2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.4037056.1,
                                           SRR14038196.96757.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.2"
     Protein         1..567
                     /product="tyrosine-protein kinase Lck isoform c"
                     /EC_number="2.7.10.2"
                     /note="T-lymphocyte specific protein tyrosine kinase
                     p56lck; p56(LSTRA) protein-tyrosine kinase; proto-oncogene
                     tyrosine-protein kinase LCK; leukocyte C-terminal Src
                     kinase; t cell-specific protein-tyrosine kinase;
                     lymphocyte cell-specific protein-tyrosine kinase"
                     /calculated_mol_wt=64073
     Region          123..176
                     /region_name="SH3_Lck"
                     /note="Src homology 3 domain of Lck Protein Tyrosine
                     Kinase; cd12005"
                     /db_xref="CDD:212938"
     Site            order(128,130,133..134,137,153..155,168,170,172..173)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212938"
     Region          181..281
                     /region_name="SH2_Src_Lck"
                     /note="Src homology 2 (SH2) domain in lymphocyte cell
                     kinase (Lck); cd10362"
                     /db_xref="CDD:198225"
     Site            order(192,212,214..217,222,238,240,273)
                     /site_type="other"
                     /note="autoinhibitory site [polypeptide binding]"
                     /db_xref="CDD:198225"
     Site            order(192,212,214..216,222,238..240)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198225"
     Site            order(239,251..252,254,267,272..274)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198225"
     Region          295..558
                     /region_name="PTKc_Lck_Blk"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Lymphocyte-specific kinase and Blk; cd05067"
                     /db_xref="CDD:270652"
     Site            order(309,311..313,317,329,331,346,374..377,381,422,
                     426..427,429,440,457..461,470,504)
                     /site_type="active"
                     /db_xref="CDD:270652"
     Site            order(309,312,317,329,331,346,374..377,381,422,424,427,
                     429,440)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270652"
     Site            order(323,325,357,360,362,375,401,405,433,553)
                     /site_type="other"
                     /note="SH3/SH2 domain interface [polypeptide binding]"
                     /db_xref="CDD:270652"
     Site            order(411,414..415,478,540..542,544,546..547,550,554,
                     557..558)
                     /site_type="other"
                     /note="CSK binding interface [polypeptide binding]"
                     /db_xref="CDD:270652"
     Site            order(422,426,457..461,470,504)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270652"
     Site            order(439..448,450..463)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270652"
     CDS             1..567
                     /gene="LCK"
                     /gene_synonym="IMD22; LSK; p56lck; pp58lck; YT16"
                     /coded_by="NM_001439146.1:113..1816"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="GeneID:3932"
                     /db_xref="HGNC:HGNC:6524"
                     /db_xref="MIM:153390"
ORIGIN      
        1 mgcgcsshpe ddwmenidvc enchypivpl dgkgtllirn gsevrdplvt yegsnppasp
       61 lqgdprqqgl kdkacgslav gfhlsptyfl pglaflvphp vtpgflpipa rfslmplvft
      121 dnlvialhsy epshdgdlgf ekgeqlrile qsgewwkaqs lttgqegfip fnfvakansl
      181 epepwffknl srkdaerqll apgnthgsfl iresestags fslsvrdfdq nqgevvkhyk
      241 irnldnggfy ispritfpgl helvrhytna sdglctrlsr pcqtqkpqkp wwedewevpr
      301 etlklverlg agqfgevwmg yynghtkvav kslkqgsmsp daflaeanlm kqlqhqrlvr
      361 lyavvtqepi yiiteymeng slvdflktps gikltinkll dmaaqiaegm afieernyih
      421 rdlraanilv sdtlsckiad fglarliedn eytaregakf pikwtapeai nygtftiksd
      481 vwsfgillte ivthgripyp gmtnpeviqn lergyrmvrp dncpeelyql mrlcwkerpe
      541 drptfdylrs vledfftate gqyqpqp
//
LOCUS       NP_001393914             686 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform F [Homo sapiens].
ACCESSION   NP_001393914
VERSION     NP_001393914.1
DBSOURCE    REFSEQ: accession NM_001406985.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 686)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 686)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 686)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 686)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 686)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 686)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 686)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 686)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 686)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853562.2232.1,
                                           SRR14038191.41124.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..686
                     /product="lamin isoform F"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=76594
     mat_peptide     1..661
                     /product="Prelamin-A/C. /id=PRO_0000398835"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
                     /calculated_mol_wt=73808
     mat_peptide     1..646
                     /product="Lamin-A/C. /id=PRO_0000063810"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
                     /calculated_mol_wt=72225
     Region          1..130
                     /region_name="Interaction with MLIP.
                     /evidence=ECO:0000269|PubMed:21498514"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          1..33
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          30..386
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Site            32
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          34..70
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          71..80
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            78
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          81..218
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            108
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            114
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            123
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            135
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            155
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            171
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            180
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            201
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            208
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          219..242
                     /region_name="Linker 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          243..383
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          259..331
                     /region_name="Necessary and sufficient for the interaction
                     with IFFO1. /evidence=ECO:0000269|PubMed:31548606"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            265
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            266
                     /site_type="other"
                     /note="Heptad change of phase; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            270
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATR.
                     /evidence=ECO:0000269|PubMed:37832547; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            311
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            316
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            325
                     /site_type="other"
                     /note="Stutter. /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            330
                     /site_type="other"
                     /note="Heptad change of phase; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            341
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          384..664
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          384..442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:37788673,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATR.
                     /evidence=ECO:0000269|PubMed:37788673,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:24741066, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          417..422
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            417
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          434..541
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     Site            450
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            457
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            486
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48679; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48679; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            546
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          552..576
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          598..619
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            625
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:26237509; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            628
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:26237509; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            632
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            646..647
                     /site_type="cleavage"
                     /note="Cleavage, by endoprotease; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            661
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000269|PubMed:8175923,
                     ECO:0000269|PubMed:9030603; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     CDS             1..686
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406985.1:209..2269"
                     /note="isoform F is encoded by transcript variant 12"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 metpsqrrat rsgaqasstp lsptritrlq ekedlqelnd rlavyidrvr sletenaglr
       61 lriteseevv srevsgikaa yeaelgdark tldsvakera rlqlelskvr eefkelkarn
      121 tkkegdliaa qarlkdleal lnskeaalst alsekrtleg elhdlrgqva kleaalgeak
      181 kqlqdemlrr vdaenrlqtm keeldfqkni yseelretkr rhetrlveid ngkqrefesr
      241 ladalqelra qhedqveqyk kelektysak ldnarqsaer nsnlvgaahe elqqsririd
      301 slsaqlsqlq kqlaakeakl rdledslare rdtsrrllae keremaemra rmqqqldeyq
      361 elldiklald meihayrkll egeeerlrls psptsqrsrg rasshssqtq gggsvtkkrk
      421 lestesrssf sqhartsgrv aveevdeegk fvrlrnksne dqsmgnwqik rqngddpllt
      481 yrfppkftlk agqvvtiwaa gagathsppt dlvwkaqntw gcgnslrtal instgeevam
      541 rklvrsvtvv eddededgdd llhhhhgshc sssgdpaeyn lrsrtvlcgt cgqpadkasa
      601 sgsgaqvggp issgssassv tvtrsyrsvg gsgggsfgdn lvtrsyllgn ssprtqspqn
      661 csiiqemgmr weveegrrkv slsclp
//
LOCUS       NP_001424297             673 aa            linear   PRI 21-NOV-2025
DEFINITION  MAP/microtubule affinity-regulating kinase 3 isoform k [Homo
            sapiens].
ACCESSION   NP_001424297 XP_016876786 XP_054232044
VERSION     NP_001424297.1
DBSOURCE    REFSEQ: accession NM_001437368.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Aparicio-Bautista,D.I., Jimenez-Ortega,R.F., Becerra-Cervera,A.,
            Aquino-Galvez,A., de Leon-Suarez,V.P., Casas-Avila,L., Salmeron,J.,
            Hidalgo-Bravo,A., Rivera-Paredez,B. and Velazquez-Cruz,R.
  TITLE     Interaction between MARK3 (rs11623869), PLCB4 (rs6086746) and
            GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women
  JOURNAL   Front Endocrinol (Lausanne) 15, 1392063 (2024)
   PUBMED   38715801
  REMARK    GeneRIF: Interaction between MARK3 (rs11623869), PLCB4 (rs6086746)
            and GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 673)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 673)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 673)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 673)
  AUTHORS   Li,M.G., Katsura,K., Nomiyama,H., Komaki,K., Ninomiya-Tsuji,J.,
            Matsumoto,K., Kobayashi,T. and Tamura,S.
  TITLE     Regulation of the interleukin-1-induced signaling pathways by a
            novel member of the protein phosphatase 2C family (PP2Cepsilon)
  JOURNAL   J Biol Chem 278 (14), 12013-12021 (2003)
   PUBMED   12556533
REFERENCE   7  (residues 1 to 673)
  AUTHORS   Sun,T.Q., Lu,B., Feng,J.J., Reinhard,C., Jan,Y.N., Fantl,W.J. and
            Williams,L.T.
  TITLE     PAR-1 is a Dishevelled-associated kinase and a positive regulator
            of Wnt signalling
  JOURNAL   Nat Cell Biol 3 (7), 628-636 (2001)
   PUBMED   11433294
REFERENCE   8  (residues 1 to 673)
  AUTHORS   Peng,C.Y., Graves,P.R., Ogg,S., Thoma,R.S., Byrnes,M.J. 3rd, Wu,Z.,
            Stephenson,M.T. and Piwnica-Worms,H.
  TITLE     C-TAK1 protein kinase phosphorylates human Cdc25C on serine 216 and
            promotes 14-3-3 protein binding
  JOURNAL   Cell Growth Differ 9 (3), 197-208 (1998)
   PUBMED   9543386
REFERENCE   9  (residues 1 to 673)
  AUTHORS   Ono,T., Kawabe,T., Sonta,S. and Okamoto,T.
  TITLE     Assignment of MARK3 alias KP78 to human chromosome band 14q32.3 by
            in situ hybridization
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 101-102 (1997)
   PUBMED   9533022
REFERENCE   10 (residues 1 to 673)
  AUTHORS   Meller,N., Liu,Y.C., Collins,T.L., Bonnefoy-Berard,N., Baier,G.,
            Isakov,N. and Altman,A.
  TITLE     Direct interaction between protein kinase C theta (PKC theta) and
            14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition
            of PKC theta translocation and function
  JOURNAL   Mol Cell Biol 16 (10), 5782-5791 (1996)
   PUBMED   8816492
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133367.4 and KF456011.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_016876786.1, XP_054232044.1.
            
            Summary: The protein encoded by this gene is activated by
            phosphorylation and in turn is involved in the phosphorylation of
            tau proteins MAP2 and MAP4. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.17654.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.32-q32.33"
     Protein         1..673
                     /product="MAP/microtubule affinity-regulating kinase 3
                     isoform k"
                     /EC_number="2.7.11.1"
                     /note="EMK-2; C-TAK1; ELKL motif kinase 2; protein kinase
                     STK10; ser/Thr protein kinase PAR-1; cdc25C-associated
                     protein kinase 1; MAP/microtubule affinity-regulating
                     kinase 3; serine/threonine-protein kinase p78"
                     /calculated_mol_wt=75707
     Region          18..243
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          261..303
                     /region_name="UBA_MARK3_4"
                     /note="UBA domain found in MAP/microtubule
                     affinity-regulating kinase MARK3, MARK4, and similar
                     proteins; cd14407"
                     /db_xref="CDD:270590"
     Region          574..671
                     /region_name="MARK1-3_C"
                     /note="C-terminal, kinase associated domain 1 (KA1), a
                     phospholipid binding domain, of microtubule
                     affinity-regulating kinases 1-3; cd12196"
                     /db_xref="CDD:213381"
     Site            order(576,579,649,651..652)
                     /site_type="other"
                     /note="putative phospholipid binding site [chemical
                     binding]"
                     /db_xref="CDD:213381"
     CDS             1..673
                     /gene="MARK3"
                     /gene_synonym="CTAK1; KP78; Par-1a; PAR1A; VIPB"
                     /coded_by="NM_001437368.1:616..2637"
                     /note="isoform k is encoded by transcript variant 11"
                     /db_xref="GeneID:4140"
                     /db_xref="HGNC:HGNC:6897"
                     /db_xref="MIM:602678"
ORIGIN      
        1 mstrtplptv nerdtenvai kiidktqlnp tslqklfrev rimkilnhpn ivklfeviet
       61 ektlylimey asggevfdyl vahgrmkeke arskfrqivs avqychqkri vhrdlkaenl
      121 lldadmniki adfgfsneft vggkldtfcg sppyaapelf qgkkydgpev dvwslgvily
      181 tlvsgslpfd gqnlkelrer vlrgkyripf ymstdcenll krflvlnpik rgtleqimkd
      241 rwinagheed elkpfvepel disdqkridi mvgmgysqee iqeslskmky deitatylll
      301 grkssevrps sdlnnstgqs phhkvqrsvs ssqkqrrysd hagpaipsvv aypkrsqtst
      361 adsdlkedgi ssrkssgsav ggkgiapasp mlgnasnpnk adiperkkss tvpssntasg
      421 gmtrrntyvc serttadrhs viqngkenst ipdqrtpvas thsissaatp drirfprgta
      481 srstfhgqpr errtatyngp paspslshea tplsqtrsrg stnlfsklts kltrrnmsfr
      541 fikrlpteye rngryegssr nvsaeqkden keakprslrf twsmkttssm dpgdmmreir
      601 kvldanncdy eqrerfllfc vhgdghaenl vqwemevckl prlslngvrf krisgtsiaf
      661 kniaskiane lkl
//
LOCUS       NP_001397645             266 aa            linear   PRI 21-NOV-2025
DEFINITION  microtubule-associated protein RP/EB family member 3 isoform 2
            [Homo sapiens].
ACCESSION   NP_001397645 XP_006712030
VERSION     NP_001397645.1
DBSOURCE    REFSEQ: accession NM_001410716.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Zhang,Y., Liu,F., Zheng,J., Jiang,K., Ai,H., Liu,L. and Mao,D.
  TITLE     MAPRE3 as an epigenetic target of EZH2 restricts ovarian cancer
            proliferation in vitro and in vivo
  JOURNAL   Exp Cell Res 435 (1), 113913 (2024)
   PUBMED   38199479
  REMARK    GeneRIF: MAPRE3 as an epigenetic target of EZH2 restricts ovarian
            cancer proliferation in vitro and in vivo.
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 266)
  AUTHORS   Bu,W. and Su,L.K.
  TITLE     Characterization of functional domains of human EB1 family proteins
  JOURNAL   J Biol Chem 278 (50), 49721-49731 (2003)
   PUBMED   14514668
  REMARK    GeneRIF: neither APC nor p150glued binding domain is necessary for
            EB1 or EBF3 to induce microtubule bundling
REFERENCE   7  (residues 1 to 266)
  AUTHORS   Su,L.K. and Qi,Y.
  TITLE     Characterization of human MAPRE genes and their proteins
  JOURNAL   Genomics 71 (2), 142-149 (2001)
   PUBMED   11161807
REFERENCE   8  (residues 1 to 266)
  AUTHORS   Nakagawa,H., Koyama,K., Murata,Y., Morito,M., Akiyama,T. and
            Nakamura,Y.
  TITLE     EB3, a novel member of the EB1 family preferentially expressed in
            the central nervous system, binds to a CNS-specific APC homologue
  JOURNAL   Oncogene 19 (2), 210-216 (2000)
   PUBMED   10644998
REFERENCE   9  (residues 1 to 266)
  AUTHORS   Juwana,J.P., Henderikx,P., Mischo,A., Wadle,A., Fadle,N.,
            Gerlach,K., Arends,J.W., Hoogenboom,H., Pfreundschuh,M. and
            Renner,C.
  TITLE     EB/RP gene family encodes tubulin binding proteins
  JOURNAL   Int J Cancer 81 (2), 275-284 (1999)
   PUBMED   10188731
REFERENCE   10 (residues 1 to 266)
  AUTHORS   Renner,C., Pfitzenmeier,J.P., Gerlach,K., Held,G., Ohnesorge,S.,
            Sahin,U., Bauer,S. and Pfreundschuh,M.
  TITLE     RP1, a new member of the adenomatous polyposis coli-binding
            EB1-like gene family, is differentially expressed in activated T
            cells
  JOURNAL   J Immunol 159 (3), 1276-1283 (1997)
   PUBMED   9233623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC013472.8.
            
            On Aug 15, 2022 this sequence version replaced XP_006712030.1.
            
            Summary:  The protein encoded by this gene is a member of the RP/EB
            family of genes.  The protein localizes to the cytoplasmic
            microtubule network and binds APCL, a homolog of the adenomatous
            polyposis coli tumor suppressor gene. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853562.18660.1,
                                           SRR11853559.18051.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..266
                     /product="microtubule-associated protein RP/EB family
                     member 3 isoform 2"
                     /note="APC binding protein; end-binding protein 3; EB1
                     protein family member 3"
                     /calculated_mol_wt=30249
     Region          16..264
                     /region_name="BIM1"
                     /note="Microtubule-binding protein involved in cell cycle
                     control [Cell division and chromosome partitioning /
                     Cytoskeleton]; COG5217"
                     /db_xref="CDD:227542"
     CDS             1..266
                     /gene="MAPRE3"
                     /gene_synonym="EB3; EBF3; EBF3-S; RP3"
                     /coded_by="NM_001410716.1:174..974"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92722.1"
                     /db_xref="GeneID:22924"
                     /db_xref="HGNC:HGNC:6892"
                     /db_xref="MIM:605788"
ORIGIN      
        1 mavnvystsv tsenlsrhdm lawvndslhl nytkieqlcs gaaycqfmdm lfpgcvhlrk
       61 vkfqaklehe yihnfkvlqa afkkmgvdki ipveklvkgk fqdnfefiqw fkkffdanyd
      121 gkdynpllar qgqdvapppn pvpqrtsptg pknmqtsgrl snvappcilr knppsarngg
      181 hetdaqilel nqqlvdlklt vdglekerdf yfsklrdiel icqehesens pvisgiigil
      241 yateegfapp eddeieehqq edqdey
//
LOCUS       NP_001422925             763 aa            linear   PRI 21-NOV-2025
DEFINITION  histone deacetylase 4 isoform 6 [Homo sapiens].
ACCESSION   NP_001422925
VERSION     NP_001422925.1
DBSOURCE    REFSEQ: accession NM_001435996.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 763)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 763)
  AUTHORS   Liu,W. and Luo,G.
  TITLE     NEDD9 is transcriptionally regulated by HDAC4 and promotes breast
            cancer metastasis and macrophage M2 polarization via the
            FAK/NF-kappaB signaling pathway
  JOURNAL   Neoplasia 57, 101059 (2024)
   PUBMED   39326322
  REMARK    GeneRIF: NEDD9 is transcriptionally regulated by HDAC4 and promotes
            breast cancer metastasis and macrophage M2 polarization via the
            FAK/NF-kappaB signaling pathway.
REFERENCE   3  (residues 1 to 763)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 763)
  AUTHORS   Di Giorgio,E., Dalla,E., Tolotto,V., D'Este,F., Paluvai,H.,
            Ranzino,L. and Brancolini,C.
  TITLE     HDAC4 influences the DNA damage response and counteracts senescence
            by assembling with HDAC1/HDAC2 to control H2BK120 acetylation and
            homology-directed repair
  JOURNAL   Nucleic Acids Res 52 (14), 8218-8240 (2024)
   PUBMED   38874468
  REMARK    GeneRIF: HDAC4 influences the DNA damage response and counteracts
            senescence by assembling with HDAC1/HDAC2 to control H2BK120
            acetylation and homology-directed repair.
REFERENCE   5  (residues 1 to 763)
  AUTHORS   Chen,Q. and Lao,J.
  TITLE     Interference with Histone Deacetylase 4 Regulates c-Jun N-terminal
            Kinase/Activating Protein-1 Signaling to Ameliorate Sepsis-induced
            Alveolar Epithelial Cell Injury
  JOURNAL   J Physiol Investig 67 (4), 174-186 (2024)
   PUBMED   39133038
  REMARK    GeneRIF: Interference with Histone Deacetylase 4 Regulates c-Jun
            N-terminal Kinase/Activating Protein-1 Signaling to Ameliorate
            Sepsis-induced Alveolar Epithelial Cell Injury.
REFERENCE   6  (residues 1 to 763)
  AUTHORS   Pazin,M.J. and Kadonaga,J.T.
  TITLE     What's up and down with histone deacetylation and transcription?
  JOURNAL   Cell 89 (3), 325-328 (1997)
   PUBMED   9150131
  REMARK    Review article
REFERENCE   7  (residues 1 to 763)
  AUTHORS   Wolffe,A.P.
  TITLE     Transcriptional control. Sinful repression
  JOURNAL   Nature 387 (6628), 16-17 (1997)
   PUBMED   9139815
REFERENCE   8  (residues 1 to 763)
  AUTHORS   Ohara,O., Nagase,T., Ishikawa,K., Nakajima,D., Ohira,M., Seki,N.
            and Nomura,N.
  TITLE     Construction and characterization of human brain cDNA libraries
            suitable for analysis of cDNA clones encoding relatively large
            proteins
  JOURNAL   DNA Res 4 (1), 53-59 (1997)
   PUBMED   9179496
REFERENCE   9  (residues 1 to 763)
  AUTHORS   Wilson,L.C., Leverton,K., Oude Luttikhuis,M.E., Oley,C.A.,
            Flint,J., Wolstenholme,J., Duckett,D.P., Barrow,M.A., Leonard,J.V.,
            Read,A.P. et al.
  TITLE     Brachydactyly and mental retardation: an Albright hereditary
            osteodystrophy-like syndrome localized to 2q37
  JOURNAL   Am J Hum Genet 56 (2), 400-407 (1995)
   PUBMED   7847374
REFERENCE   10 (residues 1 to 763)
  AUTHORS   Doherty,E.S. and Lacbawan,F.L.
  TITLE     2q37 Microdeletion Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301337
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC062017.6 and AC017028.11.
            
            Summary: Histones play a critical role in transcriptional
            regulation, cell cycle progression, and developmental events.
            Histone acetylation/deacetylation alters chromosome structure and
            affects transcription factor access to DNA. The protein encoded by
            this gene belongs to class II of the histone deacetylase/acuc/apha
            family. It possesses histone deacetylase activity and represses
            transcription when tethered to a promoter. This protein does not
            bind DNA directly, but through transcription factors MEF2C and
            MEF2D. It seems to interact in a multiprotein complex with RbAp48
            and HDAC3. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303368.1, SRR14038193.3603233.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..763
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..763
                     /product="histone deacetylase 4 isoform 6"
                     /EC_number="3.5.1.98"
                     /note="histone deacetylase A"
                     /calculated_mol_wt=84759
     Region          <86..147
                     /region_name="ClassIIa_HDAC4_Gln-rich-N"
                     /note="Glutamine-rich N-terminal helical domain of HDAC4,
                     a Class IIa histone deacetylase; cd10162"
                     /db_xref="CDD:197398"
     Site            order(88,92,103..104,107,114,118..119)
                     /site_type="other"
                     /note="dimer interface A, B [polypeptide binding]"
                     /db_xref="CDD:197398"
     Region          649..>756
                     /region_name="Arginase_HDAC"
                     /note="Arginase-like and histone-like hydrolases; cl17011"
                     /db_xref="CDD:450134"
     CDS             1..763
                     /gene="HDAC4"
                     /gene_synonym="AHO3; BDMR; HA6116; HD4; HDAC-4; HDAC-A;
                     HDACA; NEDCHF; NEDCHID"
                     /coded_by="NM_001435996.1:359..2650"
                     /note="isoform 6 is encoded by transcript variant 10"
                     /db_xref="GeneID:9759"
                     /db_xref="HGNC:HGNC:14063"
                     /db_xref="MIM:605314"
ORIGIN      
        1 mfdglsgrdq pvellnparv nhmpstvdva talplqvaps avpmdlrldh qfslpvaepa
       61 lreqqlqqel lalkqkqqiq rqiliaefqr qheqlsrqhe aqlhehikqq qemlamkhqq
      121 ellehqrkle rhrqeqelek qhreqklqql knkekgkesa vastevkmkl qefvlnkkka
      181 lahrnlnhci ssdprywygk tqhssldqss ppqsgvstsy nhpvlgmyda kddfplrkta
      241 sepnlklrsr lkqkvaerrs spllrrkdgp vvtalkkrpl dvtdsacssa pgsgpsspnn
      301 ssgsvsaeng iapavpsipa etslahrlva regsaaplpl ytspslpnit lglpatgpsa
      361 gtagqqdaer ltlpalqqrl slfpgthltp ylstsplerd ggaahspllq hmvlleqppa
      421 qaplvtdwyl sglgalplha qslvgadrvs psihklrqhr plgrtqsapl pqnaqalqhl
      481 viqqqhqqfl ekhkqqfqqq qlqmnkiipk pseparqpes hpeeteeelr ehqalldepy
      541 ldrlpgqkea haqagvqvkq epiesdeeea epprevepgq rqpseqellf rqqallleqq
      601 rihqlrnyqa smeaagipvs fgghrplsra qsspasatfp vsvqepptkp rfttglvydt
      661 lmlkhqctcg sssshpehag riqsiwsrlq etglrgkcec irgrkatlee lqtvhseaht
      721 llygtnplnr qkldskkllg slasvfvrlp cggvgvsvpl mck
//
LOCUS       NP_001394380            2836 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform o [Homo sapiens].
ACCESSION   NP_001394380
VERSION     NP_001394380.1
DBSOURCE    REFSEQ: accession NM_001407451.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2836)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2836)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2836)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2836)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2836)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2836)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2836)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2836)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2836)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2836)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.337850.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2836
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2836
                     /product="adenomatous polyposis coli protein isoform o"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=310606
     Region          102..182
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          315..367
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          368..441
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          465..501
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          505..546
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          509..546
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          556..588
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(579,583,587,626,630,634,671,675,679)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          596..637
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          642..682
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          646..680
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          684..724
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          688..724
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          725..1012
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          1029..1128
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1250..>1267
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1276..1361
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1284..1694
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1630..1653
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1655..1708
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1709..1730
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1739..1832
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1866..1940
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          2026..2045
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2216..2561
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2663..2836
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2836
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407451.1:90..8600"
                     /note="isoform o is encoded by transcript variant 21"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 madvnlvera tgderkrrrq evlkqlqgsi edeamassgq idllerlkel nldssnfpgv
       61 klrskmslrs ygsregsvss rsgecspvpm gsfprrgfvn gsrestgyle elekerslll
      121 adldkeekek dwyyaqlqnl tkridslplt enfslqtdmt rrqleyearq irvameeqlg
      181 tcqdmekraq rriariqqie kdilrirqll qsqateaers sqnkhetgsh daerqnegqg
      241 vgeinmatsg ngqgsttrmd hetasvlsss sthsaprrlt shlgtkvemv ysllsmlgth
      301 dkddmsrtll amsssqdsci smrqsgclpl liqllhgndk dsvllgnsrg skeararasa
      361 alhniihsqp ddkrgrreir vlhlleqira ycetcwewqe ahepgmdqdk npmpapvehq
      421 icpavcvlmk lsfdeehrha mnelgrkatr gissqelgqg lsgglqaiae llqvdcemyg
      481 ltndhysitl rryagmaltn ltfgdvanka tlcsmkgcmr alvaqlkses edlqqviasv
      541 lrnlswradv nskktlrevg svkalmecal evkkestlks vlsalwnlsa hctenkadic
      601 avdgalaflv gtltyrsqtn tlaiiesggg ilrnvsslia tnedhrqilr ennclqtllq
      661 hlkshsltiv snacgtlwnl sarnpkdqea lwdmgavsml knlihskhkm iamgsaaalr
      721 nlmanrpaky kdanimspgs slpslhvrkq kaleaeldaq hlsetfdnid nlspkashrs
      781 kqrhkqslyg dyvfdtnrhd dnrsdnfntg nmtvlspyln ttvlpsssss rgsldssrse
      841 kdrslererg iglgnyhpat enpgtsskrg lqisttaaqi akvmeevsai htsqedrssg
      901 sttelhcvtd ernalrrssa ahthsntynf tksensnrtc smpyakleyk rssndslnsv
      961 sssdgygkrg qmkpsiesys eddeskfcsy gqypadlahk ihsanhmddn dgeldtpiny
     1021 slkysdeqln sgrqspsqne rwarpkhiie deikqseqrq srnqsttypv ytestddkhl
     1081 kfqphfgqqe cvspyrsrga ngsetnrvgs nhginqnvsq slcqeddyed dkptnysery
     1141 seeeqheeee rptnysikyn eekrhvdqpi dyslkyatdi pssqkqsfsf sksssgqssk
     1201 tehmssssen tstpssnakr qnqlhpssaq srsgqpqkaa tckvssinqe tiqtycvedt
     1261 picfsrcssl sslssaedei gcnqttqead santlqiaei kekigtrsae dpvsevpavs
     1321 qhprtkssrl qgsslssesa rhkavefssg akspsksgaq tpksppehyv qetplmfsrc
     1381 tsvssldsfe srsiassvqs epcsgmvsgi ispsdlpdsp gqtmppsrsk tpppppqtaq
     1441 tkrevpknka ptaekresgp kqaavnaavq rvqvlpdadt llhfatestp dgfscsssls
     1501 alsldepfiq kdvelrimpp vqendngnet eseqpkesne nqekeaekti dsekdlldds
     1561 ddddieilee ciisamptks srkakkpaqt asklpppvar kpsqlpvykl lpsqnrlqpq
     1621 khvsftpgdd mprvycvegt pinfstatsl sdltiesppn elaagegvrg gaqsgefekr
     1681 dtiptegrst deaqggktss vtipelddnk aeegdilaec insampkgks hkpfrvkkim
     1741 dqvqqasass sapnknqldg kkkkptspvk pipqnteyrt rvrknadskn nlnaervfsd
     1801 nkdskkqnlk nnskvfndkl pnnedrvrgs fafdsphhyt piegtpycfs rndslssldf
     1861 ddddvdlsre kaelrkaken keseakvtsh teltsnqqsa nktqaiakqp inrgqpkpil
     1921 qkqstfpqss kdipdrgaat deklqnfaie ntpvcfshns slsslsdidq ennnkenepi
     1981 keteppdsqg epskpqasgy apksfhvedt pvcfsrnssl sslsidsedd llqecissam
     2041 pkkkkpsrlk gdnekhsprn mggilgedlt ldlkdiqrpd sehglspdse nfdwkaiqeg
     2101 ansivsslhq aaaaaclsrq assdsdsils lksgislgsp fhltpdqeek pftsnkgpri
     2161 lkpgekstle tkkieseskg ikggkkvyks litgkvrsns eisgqmkqpl qanmpsisrg
     2221 rtmihipgvr nsssstspvs kkgpplktpa skspsegqta ttsprgakps vkselspvar
     2281 qtsqiggssk apsrsgsrds tpsrpaqqpl srpiqspgrn sispgrngis ppnklsqlpr
     2341 tsspstastk ssgsgkmsyt spgrqmsqqn ltkqtglskn assiprsesa skglnqmnng
     2401 ngankkvels rmsstkssgs esdrserpvl vrqstfikea psptlrrkle esasfeslsp
     2461 ssrpasptrs qaqtpvlsps lpdmslsths svqaggwrkl ppnlsptiey ndgrpakrhd
     2521 iarshsesps rlpinrsgtw krehskhsss lprvstwrrt gssssilsas sessekakse
     2581 dekhvnsisg tkqskenqvs akgtwrkike nefsptnsts qtvssgatng aesktliyqm
     2641 apavsktedv wvriedcpin nprsgrsptg ntppvidsvs ekanpnikds kdnqakqnvg
     2701 ngsvpmrtvg lenrlnsfiq vdapdqkgte ikpgqnnpvp vsetnessiv ertpfsssss
     2761 skhsspsgtv aarvtpfnyn psprkssads tsarpsqipt pvnnntkkrd sktdstessg
     2821 tqspkrhsgs ylvtsv
//
LOCUS       NP_001401241             278 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 3 isoform 12
            precursor [Homo sapiens].
ACCESSION   NP_001401241
VERSION     NP_001401241.1
DBSOURCE    REFSEQ: accession NM_001414312.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Tang,Q., Yuan,Y., Li,L., Xu,Y., Ji,W., Xiao,S., Han,Y., Miao,W.,
            Cai,J., You,P., Chen,M., Ding,S., Li,Z., Qi,Z., Hou,W. and Luo,H.
  TITLE     Comprehensive analysis reveals that LTBR is a immune-related
            biomarker for glioma
  JOURNAL   Comput Biol Med 174, 108457 (2024)
   PUBMED   38599071
  REMARK    GeneRIF: Comprehensive analysis reveals that LTBR is a
            immune-related biomarker for glioma.
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Wu,Y., Zhao,S., Guo,W., Liu,Y., Requena Mullor,M.D.M.,
            Rodriguez,R.A. and Wei,R.
  TITLE     Systematic analysis of the prognostic value and immunological
            function of LTBR in human cancer
  JOURNAL   Aging (Albany NY) 16 (1), 129-152 (2024)
   PUBMED   38175686
  REMARK    GeneRIF: Systematic analysis of the prognostic value and
            immunological function of LTBR in human cancer.
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Shuptrine,C.W., Perez,V.M., Selitsky,S.R., Schreiber,T.H. and
            Fromm,G.
  TITLE     Shining a LIGHT on myeloid cell targeted immunotherapy
  JOURNAL   Eur J Cancer 187, 147-160 (2023)
   PUBMED   37167762
  REMARK    Review article
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Abudukeyoumu,A., Lai,Z.Z., Lu,J.J., Zhang,X., Hou,D.Y., Dong,J.,
            Wu,J.N., Li,M.Q. and Xie,F.
  TITLE     A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion
  JOURNAL   J Reprod Immunol 153, 103693 (2022)
   PUBMED   35987137
  REMARK    GeneRIF: A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion.
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Remouchamps,C., Boutaffala,L., Ganeff,C. and Dejardin,E.
  TITLE     Biology and signal transduction pathways of the
            Lymphotoxin-alphabeta/LTbetaR system
  JOURNAL   Cytokine Growth Factor Rev 22 (5-6), 301-310 (2011)
   PUBMED   22152226
  REMARK    Review article
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Nakano,H., Oshima,H., Chung,W., Williams-Abbott,L., Ware,C.F.,
            Yagita,H. and Okumura,K.
  TITLE     TRAF5, an activator of NF-kappaB and putative signal transducer for
            the lymphotoxin-beta receptor
  JOURNAL   J Biol Chem 271 (25), 14661-14664 (1996)
   PUBMED   8663299
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Browning,J.L., Miatkowski,K., Sizing,I., Griffiths,D., Zafari,M.,
            Benjamin,C.D., Meier,W. and Mackay,F.
  TITLE     Signaling through the lymphotoxin beta receptor induces the death
            of some adenocarcinoma tumor lines
  JOURNAL   J Exp Med 183 (3), 867-878 (1996)
   PUBMED   8642291
REFERENCE   8  (residues 1 to 278)
  AUTHORS   Baens,M., Aerssens,J., van Zand,K., Van den Berghe,H. and
            Marynen,P.
  TITLE     Isolation and regional assignment of human chromosome 12p cDNAs
  JOURNAL   Genomics 29 (1), 44-52 (1995)
   PUBMED   8530100
REFERENCE   9  (residues 1 to 278)
  AUTHORS   Crowe,P.D., VanArsdale,T.L., Walter,B.N., Ware,C.F., Hession,C.,
            Ehrenfels,B., Browning,J.L., Din,W.S., Goodwin,R.G. and Smith,C.A.
  TITLE     A lymphotoxin-beta-specific receptor
  JOURNAL   Science 264 (5159), 707-710 (1994)
   PUBMED   8171323
REFERENCE   10 (residues 1 to 278)
  AUTHORS   Baens,M., Chaffanet,M., Cassiman,J.J., van den Berghe,H. and
            Marynen,P.
  TITLE     Construction and evaluation of a hncDNA library of human 12p
            transcribed sequences derived from a somatic cell hybrid
  JOURNAL   Genomics 16 (1), 214-218 (1993)
   PUBMED   8486360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005840.2.
            
            Summary: This gene encodes a member of the tumor necrosis factor
            receptor superfamily. The major ligands of this receptor include
            lymphotoxin alpha/beta and tumor necrosis factor ligand superfamily
            member 14. The encoded protein plays a role in signalling during
            the development of lymphoid and other organs, lipid metabolism,
            immune response, and programmed cell death. Activity of this
            receptor has also been linked to carcinogenesis. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853560.6392.1,
                                           SRR14038192.1011810.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..278
                     /product="tumor necrosis factor receptor superfamily
                     member 3 isoform 12 precursor"
                     /note="tumor necrosis factor C receptor; lymphotoxin B
                     receptor; tumor necrosis factor receptor type III;
                     lymphotoxin beta receptor (TNFR superfamily, member 3);
                     tumor necrosis factor receptor 2-related protein"
                     /calculated_mol_wt=27378
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3049
     Region          11..168
                     /region_name="TNFRSF3"
                     /note="Tumor necrosis factor receptor superfamily member 3
                     (TNFRSF3), also known as lymphotoxin beta receptor (LTBR);
                     cd10578"
                     /db_xref="CDD:276904"
     Region          22..80
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276904"
     Region          83..124
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276904"
     Region          126..167
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276904"
     Region          148..>210
                     /region_name="TNFRSF"
                     /note="Tumor necrosis factor receptor superfamily
                     (TNFRSF); cl22855"
                     /db_xref="CDD:473981"
     Region          170..210
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276924"
     CDS             1..278
                     /gene="LTBR"
                     /gene_synonym="D12S370; LT-BETA-R; TNF-R-III; TNFCR;
                     TNFR-RP; TNFR2-RP; TNFR3; TNFRSF3"
                     /coded_by="NM_001414312.1:198..1034"
                     /note="isoform 12 precursor is encoded by transcript
                     variant 12"
                     /db_xref="GeneID:4055"
                     /db_xref="HGNC:HGNC:6718"
                     /db_xref="MIM:600979"
ORIGIN      
        1 mllpwatsap glawgplvlg lfgllaasqp qavppyasen qtcrdqekey yepqhriccs
       61 rcppgtyvsa kcsrirdtvc atcaensyne hwnylticql crpcdpvmgl eeiapctskr
      121 ktqcrcqpgm fcaawalect hcellsdcpp gteaelkdev gkgnnhcvpc kaghfqntss
      181 psarcqphtr cenqglveaa pgtaqsdttc knpleplppe msgtmlmlav llplafflll
      241 atvfsciwks hpslcrklgs llkrrpqvpm afmspagl
//
LOCUS       NP_065918               1066 aa            linear   PRI 21-NOV-2025
DEFINITION  ubiquitin-associated protein 2 isoform 7 [Homo sapiens].
ACCESSION   NP_065918
VERSION     NP_065918.1
DBSOURCE    REFSEQ: accession NM_020867.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Lv,Z., Shi,Y., Wu,H., Cao,K., Liu,X. and Wang,C.
  TITLE     Novel Circular RNA CircUBAP2 Drives Tumor Progression by Regulating
            the miR-143/TFAP2B Axis in Prostate Cancer
  JOURNAL   Protein Pept Lett 31 (1), 61-73 (2024)
   PUBMED   37962045
  REMARK    GeneRIF: Novel Circular RNA CircUBAP2 Drives Tumor Progression by
            Regulating the miR-143/TFAP2B Axis in Prostate Cancer.
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Chou,M.C., Wang,Y.H., Chen,F.Y., Kung,C.Y., Wu,K.P., Kuo,J.C.,
            Chan,S.J., Cheng,M.L., Lin,C.Y., Chou,Y.C., Ho,M.C., Firestine,S.,
            Huang,J.R. and Chen,R.H.
  TITLE     PAICS ubiquitination recruits UBAP2 to trigger phase separation for
            purinosome assembly
  JOURNAL   Mol Cell 83 (22), 4123-4140 (2023)
   PUBMED   37848033
  REMARK    GeneRIF: PAICS ubiquitination recruits UBAP2 to trigger phase
            separation for purinosome assembly.
REFERENCE   4  (residues 1 to 1066)
  AUTHORS   Herlihy,A.E., Boeing,S., Weems,J.C., Walker,J.,
            Dirac-Svejstrup,A.B., Lehner,M.H., Conaway,R.C., Conaway,J.W. and
            Svejstrup,J.Q.
  TITLE     UBAP2/UBAP2L regulate UV-induced ubiquitylation of RNA polymerase
            II and are the human orthologues of yeast Def1
  JOURNAL   DNA Repair (Amst) 115, 103343 (2022)
   PUBMED   35633597
  REMARK    GeneRIF: UBAP2/UBAP2L regulate UV-induced ubiquitylation of RNA
            polymerase II and are the human orthologues of yeast Def1.
REFERENCE   5  (residues 1 to 1066)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 1066)
  AUTHORS   Zuo,L., Saba,L., Wang,K., Zhang,X., Krystal,J.H., Tabakoff,B. and
            Luo,X.
  TITLE     Exome-wide association study of replicable nonsynonymous variants
            conferring risk for alcohol dependence
  JOURNAL   J Stud Alcohol Drugs 74 (4), 622-625 (2013)
   PUBMED   23739027
  REMARK    GeneRIF: By incorporating the information from bioinformatics and
            RNA expression analyses, we identified at least two of the most
            promising risk genes for alcohol dependence: APOER2 and UBAP2
REFERENCE   7  (residues 1 to 1066)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 1066)
  AUTHORS   Venturelli,E., Villa,C., Fenoglio,C., Clerici,F., Marcone,A.,
            Benussi,L., Ghidoni,R., Gallone,S., Scalabrini,D., Cortini,F.,
            Fumagalli,G., Cappa,S., Binetti,G., Franceschi,M., Rainero,I.,
            Giordana,M.T., Mariani,C., Bresolin,N., Scarpini,E. and
            Galimberti,D.
  TITLE     Is KIF24 a genetic risk factor for Frontotemporal Lobar
            Degeneration?
  JOURNAL   Neurosci Lett 482 (3), 240-244 (2010)
   PUBMED   20670673
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1066)
  AUTHORS   Dieci,G., Preti,M. and Montanini,B.
  TITLE     Eukaryotic snoRNAs: a paradigm for gene expression flexibility
  JOURNAL   Genomics 94 (2), 83-88 (2009)
   PUBMED   19446021
  REMARK    GeneRIF: UBAP2 serves as a host gene for snoRNAs
            Review article
REFERENCE   10 (residues 1 to 1066)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The UBA domain: a sequence motif present in multiple enzyme classes
            of the ubiquitination pathway
  JOURNAL   Trends Biochem Sci 21 (5), 172-173 (1996)
   PUBMED   8871400
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354989.13 and AL139113.21.
            
            Summary: The protein encoded by this gene contains a UBA (ubiquitin
            associated) domain, which is characteristic of proteins that
            function in the ubiquitination pathway. This gene may show
            increased expression in the adrenal gland and lymphatic tissues.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2356809.1,
                                           SRR14038194.1692137.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..1066
                     /product="ubiquitin-associated protein 2 isoform 7"
                     /note="AD-012 protein; RNA polymerase II degradation
                     factor UBAP2"
                     /calculated_mol_wt=111558
     Region          53..90
                     /region_name="UBA_UBP2_like"
                     /note="UBA domain found in ubiquitin-associated protein 2
                     (UBAP-2) like proteins; cd14277"
                     /db_xref="CDD:270463"
     Region          459..488
                     /region_name="DUF3697"
                     /note="Ubiquitin-associated protein 2; pfam12478"
                     /db_xref="CDD:372135"
     CDS             1..1066
                     /gene="UBAP2"
                     /gene_synonym="UBAP-2"
                     /coded_by="NM_020867.2:297..3497"
                     /note="isoform 7 is encoded by transcript variant 12"
                     /db_xref="GeneID:55833"
                     /db_xref="HGNC:HGNC:14185"
ORIGIN      
        1 mmtsvssdhc rgarekpqis aaqstqpqkq vvqataeqmr laqvifdknd sdfeakvkql
       61 mevtgknqde civalhdcng dvnkainill egnsdttswe tvgckkknfa kensenkenr
      121 ekksekessr grgnnnrkgr ggnrgrefrg eengidcnqv dkpsdrgkra rgrelasnth
      181 niaqdlsnks syglkgawkn sveewttedw tedlsetkvf tassapaenh ilpgqsidlv
      241 allqkpvphs qaseansfet sqqqgfgqal vftnsqhnnq mapgtgssta vnscspqsls
      301 svlgsgfgel appkmanits sqildqlkap slgqftttps tqqnstshpt tttswdlkpp
      361 tsqssvlshl dfksqpepsp vlsqlsqrqq hqsqavtvpp pglesfpsqa klrestpgds
      421 pstvnkllql psttienisv svhqpqpkhi klakrrippa skipasavem pgsadvtgln
      481 vqfgalefgs epslsefgsa pssensnqip islyskslse plntslsmts avqnstytts
      541 vitscsltss slnsaspvam sssydqssvh nripyqspvs ssesapgtim nghgggrsqq
      601 tldtpkttgp psalpsvssl psttsctall pstsqhtgdl tssplsqlss slsshqssls
      661 ahaalsssts hthasvesas shqssatfst aatsvsssas sgaslsssmn tanslclggt
      721 pasasssssr aaplvtsgka ppnlpqgvpp llhnqylvgp ggllpaypiy gydelqmlqs
      781 rlpvdyygip faaptalasr dgslannpyp gdvtkfgrgd saspapattp aqpqqsqsqt
      841 hhtaqqpfvn palppgysyt glpyytgmps afqygptmfv ppasakqhgv nlstptppfq
      901 qasgygqhgy stgyddltqg taagdyskgg yagssqapnk sagsgpgkgv svsssttglp
      961 dmtgsvynkt qtfdkqgfha gtpppfslps vlgstgplas gaapgyappp flhilpahqq
     1021 phsqllhhhl pqdaqsgsgq rsqpsslqpk sqaskpaygn spywtn
//
LOCUS       NP_001425608            1634 aa            linear   PRI 21-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4 gamma 3 isoform 17 [Homo
            sapiens].
ACCESSION   NP_001425608 XP_047289218 XP_054195341
VERSION     NP_001425608.1
DBSOURCE    REFSEQ: accession NM_001438679.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1634)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1634)
  AUTHORS   Kang,J.Y., Wen,Z., Pan,D., Zhang,Y., Li,Q., Zhong,A., Yu,X.,
            Wu,Y.C., Chen,Y., Zhang,X., Kou,P.C., Geng,J., Wang,Y.Y., Hua,M.M.,
            Zong,R., Li,B., Shi,H.J., Li,D., Fu,X.D., Li,J., Nelson,D.L.,
            Guo,X., Zhou,Y., Gou,L.T., Huang,Y. and Liu,M.F.
  TITLE     LLPS of FXR1 drives spermiogenesis by activating translation of
            stored mRNAs
  JOURNAL   Science 377 (6607), eabj6647 (2022)
   PUBMED   35951695
REFERENCE   3  (residues 1 to 1634)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1634)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 1634)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1634)
  AUTHORS   Waskiewicz,A.J., Johnson,J.C., Penn,B., Mahalingam,M., Kimball,S.R.
            and Cooper,J.A.
  TITLE     Phosphorylation of the cap-binding protein eukaryotic translation
            initiation factor 4E by protein kinase Mnk1 in vivo
  JOURNAL   Mol Cell Biol 19 (3), 1871-1880 (1999)
   PUBMED   10022874
REFERENCE   7  (residues 1 to 1634)
  AUTHORS   Pyronnet,S., Imataka,H., Gingras,A.C., Fukunaga,R., Hunter,T. and
            Sonenberg,N.
  TITLE     Human eukaryotic translation initiation factor 4G (eIF4G) recruits
            mnk1 to phosphorylate eIF4E
  JOURNAL   EMBO J 18 (1), 270-279 (1999)
   PUBMED   9878069
REFERENCE   8  (residues 1 to 1634)
  AUTHORS   Gingras,A.C., Raught,B. and Sonenberg,N.
  TITLE     eIF4 initiation factors: effectors of mRNA recruitment to ribosomes
            and regulators of translation
  JOURNAL   Annu Rev Biochem 68, 913-963 (1999)
   PUBMED   10872469
  REMARK    Review article
REFERENCE   9  (residues 1 to 1634)
  AUTHORS   Imataka,H., Gradi,A. and Sonenberg,N.
  TITLE     A newly identified N-terminal amino acid sequence of human eIF4G
            binds poly(A)-binding protein and functions in poly(A)-dependent
            translation
  JOURNAL   EMBO J 17 (24), 7480-7489 (1998)
   PUBMED   9857202
REFERENCE   10 (residues 1 to 1634)
  AUTHORS   Gradi,A., Imataka,H., Svitkin,Y.V., Rom,E., Raught,B., Morino,S.
            and Sonenberg,N.
  TITLE     A novel functional human eukaryotic translation initiation factor
            4G
  JOURNAL   Mol Cell Biol 18 (1), 334-342 (1998)
   PUBMED   9418880
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031005.2, AL627311.16,
            AL358392.19 and AL606477.11.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047289218.1, XP_054195341.1.
            
            Summary: The protein encoded by this gene is thought to be part of
            the eIF4F protein complex, which is involved in mRNA cap
            recognition and transport of mRNAs to the ribosome. Interestingly,
            a microRNA (miR-520c-3p) has been found that negatively regulates
            synthesis of the encoded protein, and this leads to a global
            decrease in protein translation and cell proliferation. Therefore,
            this protein is a key component of the anti-tumor activity of
            miR-520c-3p. [provided by RefSeq, May 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.656657.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1634
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     Protein         1..1634
                     /product="eukaryotic translation initiation factor 4 gamma
                     3 isoform 17"
                     /note="eIF-4-gamma 3; eIF-4-gamma II"
                     /calculated_mol_wt=182230
     Region          <2..276
                     /region_name="PHA03378"
                     /note="EBNA-3B; Provisional"
                     /db_xref="CDD:223065"
     Region          <166..390
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          804..1032
                     /region_name="MIF4G"
                     /note="MIF4G domain; pfam02854"
                     /db_xref="CDD:397130"
     Region          1271..1383
                     /region_name="MA3"
                     /note="MA3 domain; pfam02847"
                     /db_xref="CDD:397128"
     Region          1477..1605
                     /region_name="W2_eIF4G1_like"
                     /note="C-terminal W2 domain of eukaryotic translation
                     initiation factor 4 gamma 1 and similar proteins; cd11559"
                     /db_xref="CDD:211397"
     Region          <1584..1630
                     /region_name="W2"
                     /note="C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon;
                     cl17013"
                     /db_xref="CDD:473053"
     CDS             1..1634
                     /gene="EIF4G3"
                     /gene_synonym="eIF-4G 3; eIF4G 3; eIF4GII"
                     /coded_by="NM_001438679.1:326..5230"
                     /note="isoform 17 is encoded by transcript variant 23"
                     /db_xref="GeneID:8672"
                     /db_xref="HGNC:HGNC:3298"
                     /db_xref="MIM:603929"
ORIGIN      
        1 mnsqpqtrsp psrtvpihct dnwkrrkvle qtpvyrslag rgwikycifa agprpphhqf
       61 fqrpqiqppr atipnsspsi rpgaqtptav yqanqhimmv nhlpmpypvp qgpqycipqy
      121 rhsgppyvgp pqqypvqppg pgpfypgpgp gdfpnaygtp fypsqpvyqs apiivptqqq
      181 pppakrekkt irirdpnqgg kditeeimsg ggsrnptppi grptstptpp qqlpsqvpeh
      241 spvvygtves ahlaastpvt aasdqkqeek pkpdpvlksp spvlrlvlsg ekkeqegqts
      301 ettaivsiae lplppspttv ssvarstiaa ptssalssqp ifttaiddrc elsspredti
      361 pipsltscte tsdplptnen dddickkpcs vapndiplvs stnlineing vseklsates
      421 iveivkqevl pltleleile nppeemklec ipapitpstv psfpptpptp paspphtpvi
      481 vpaaattvss psaaitvqrv leedesirtc lsedakeiqn kieveadgqt eeildsqnln
      541 srrspvpaqi aitvpktwkk pkdrtrttee mleaelelka eeelsidkvl eseqdkmsqg
      601 fhperdpsdl kkvkaveeng eeaepvrnga esvsegegid ansgstdssg dgvtfpfkpe
      661 swkptdtegk kqydreflld fqfmpaciqk peglppisdv vldkinqpkl pmrtldpril
      721 prgpdftpaf adfgrqtpgg rgvpllnvgs rrsqpgqrre prkiitvsvk edvhlkkaen
      781 awkpsqkrds qaddpenikt qelfrkvrsi lnkltpqmfn qlmkqvsglt vdteerlkgv
      841 idlvfekaid epsfsvayan mcrclvtlkv pmadkpgntv nfrklllnrc qkefekdkad
      901 ddvfekkqke leaasapeer trlhdeleea kdkarrrsig nikfigelfk lkmlteaimh
      961 dcvvkllknh deesleclcr llttigkdld fekakprmdq yfnqmekivk erktssrirf
     1021 mlqdvidlrl cnwvsrradq gpktieqihk eakieeqeeq rkvqqlmtke krrpgvqrvd
     1081 eggwntvqga knsrvldpsk flkitkptid ekiqlvpkaq lgswgkgssg gakasetdal
     1141 rssasslnrf salqppapsg stpstpvefd srrtltsrgs mgrekndkpl psatarpntf
     1201 mrggsskdll dnqsqeeqrr emletvkqlt ggvdvernst eaernktres akpeisamsa
     1261 hdkaalseee lerksksiid eflhindfke amqcveelna qgllhvfvrv gvestlersq
     1321 itrdhmgqll yqlvqsekls kqdffkgfse tleladdmai diphiwlyla elvtpmlkeg
     1381 gismreltie fskpllpvgr agvllseilh llckqmshkk vgalwreadl swkdflpege
     1441 dvhnflleqk ldfiesdspc ssealskkel saeelykrle kliiedkand eqifdwvean
     1501 ldeiqmsspt flralmtavc kaaiiadsst frvdtavikq rvpillkyld sdtekelqal
     1561 yalqasivkl dqpanllrmf fdclydeevi sedafykwes skdpaeqngk gvalksvtaf
     1621 ftwlreaeee sedn
//
LOCUS       NP_001356                767 aa            linear   PRI 21-NOV-2025
DEFINITION  disks large homolog 4 isoform 1 [Homo sapiens].
ACCESSION   NP_001356
VERSION     NP_001356.1
DBSOURCE    REFSEQ: accession NM_001365.5
KEYWORDS    RefSeq; MANE Plus Clinical.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 767)
  AUTHORS   Fadahunsi,N., Petersen,J., Metz,S., Jakobsen,A., Vad Mathiesen,C.,
            Silke Buch-Rasmussen,A., Kurgan,N., Kjaergaard Larsen,J.,
            Andersen,R.C., Topilko,T., Svendsen,C., Apuschkin,M., Skovbjerg,G.,
            Hendrik Schmidt,J., Houser,G., Elgaard Jager,S., Bach,A.,
            Deshmukh,A.S., Kilpelainen,T.O., Stromgaard,K., Madsen,K.L. and
            Clemmensen,C.
  TITLE     Targeting postsynaptic glutamate receptor scaffolding proteins
            PSD-95 and PICK1 for obesity treatment
  JOURNAL   Sci Adv 10 (9), eadg2636 (2024)
   PUBMED   38427737
  REMARK    GeneRIF: Targeting postsynaptic glutamate receptor scaffolding
            proteins PSD-95 and PICK1 for obesity treatment.
REFERENCE   2  (residues 1 to 767)
  AUTHORS   Shen,Z., Sun,D., Savastano,A., Varga,S.J., Cima-Omori,M.S.,
            Becker,S., Honigmann,A. and Zweckstetter,M.
  TITLE     Multivalent Tau/PSD-95 interactions arrest in vitro condensates and
            clusters mimicking the postsynaptic density
  JOURNAL   Nat Commun 14 (1), 6839 (2023)
   PUBMED   37891164
  REMARK    GeneRIF: Multivalent Tau/PSD-95 interactions arrest in vitro
            condensates and clusters mimicking the postsynaptic density.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 767)
  AUTHORS   Shimizu,H. and Hohjoh,H.
  TITLE     FMRP, FXR1 protein and Dlg4 mRNA, which are associated with fragile
            X syndrome, are involved in the ubiquitin-proteasome system
  JOURNAL   Sci Rep 13 (1), 1956 (2023)
   PUBMED   36732356
  REMARK    GeneRIF: FMRP, FXR1 protein and Dlg4 mRNA, which are associated
            with fragile X syndrome, are involved in the ubiquitin-proteasome
            system.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 767)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 767)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 767)
  AUTHORS   Niethammer,M., Kim,E. and Sheng,M.
  TITLE     Interaction between the C terminus of NMDA receptor subunits and
            multiple members of the PSD-95 family of membrane-associated
            guanylate kinases
  JOURNAL   J Neurosci 16 (7), 2157-2163 (1996)
   PUBMED   8601796
REFERENCE   7  (residues 1 to 767)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   8  (residues 1 to 767)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 767)
  AUTHORS   Kornau,H.C., Schenker,L.T., Kennedy,M.B. and Seeburg,P.H.
  TITLE     Domain interaction between NMDA receptor subunits and the
            postsynaptic density protein PSD-95
  JOURNAL   Science 269 (5231), 1737-1740 (1995)
   PUBMED   7569905
REFERENCE   10 (residues 1 to 767)
  AUTHORS   Tumer,Z., Dye,T.J., Prada,C., White-Brown,A.M., MacKenzie,A. and
            Levy,A.M.
  TITLE     DLG4-Related Synaptopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37347881
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC120057.9.
            
            Summary: This gene encodes a member of the membrane-associated
            guanylate kinase (MAGUK) family. It heteromultimerizes with another
            MAGUK protein, DLG2, and is recruited into NMDA receptor and
            potassium channel clusters. These two MAGUK proteins may interact
            at postsynaptic sites to form a multimeric scaffold for the
            clustering of receptors, ion channels, and associated signaling
            proteins. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U83192.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match :: ENST00000648172.9/ ENSP00000497806.3
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..767
                     /product="disks large homolog 4 isoform 1"
                     /note="disks large homolog 4; Tax interaction protein 15;
                     post-synaptic density protein 95; synapse-associated
                     protein 90; discs large homolog 4"
                     /calculated_mol_wt=85299
     Region          <26..49
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          54..107
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          106..194
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(117..123,140,143,173,177,180..181)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          203..287
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(212..218,235,238,268,272,275..276)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          288..355
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          353..443
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(365..371,382,385,415,419,422..423)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          473..538
                     /region_name="SH3_DLG4"
                     /note="Src Homology 3 domain of Disks Large homolog 4;
                     cd12030"
                     /db_xref="CDD:212963"
     Site            order(477,499)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212963"
     Site            order(480,482,485,494,512..513,532,534..535)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212963"
     Region          576..754
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..767
                     /gene="DLG4"
                     /gene_synonym="MRD62; PSD95; SAP-90; SAP90"
                     /coded_by="NM_001365.5:988..3291"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45599.1"
                     /db_xref="GeneID:1742"
                     /db_xref="HGNC:HGNC:2903"
                     /db_xref="MIM:602887"
ORIGIN      
        1 msqrpraprs alwllappll rwapplltvl hsdlfqalld ildyyeasls esqkyryqde
       61 dtpplehspa hlpnqanspp vivntdtlea pgyelqvngt egemeyeeit lergnsglgf
      121 siaggtdnph igddpsifit kiipggaaaq dgrlrvndsi lfvnevdvre vthsaaveal
      181 keagsivrly vmrrkppaek vmeiklikgp kglgfsiagg vgnqhipgdn siyvtkiieg
      241 gaahkdgrlq igdkilavns vgledvmhed avaalkntyd vvylkvakps naylsdsyap
      301 pdittsysqh ldneishssy lgtdyptamt ptsprryspv akdllgeedi preprrivih
      361 rgstglgfni vggedgegif isfilaggpa dlsgelrkgd qilsvngvdl rnasheqaai
      421 alknagqtvt iiaqykpeey srfeakihdl reqlmnsslg sgtaslrsnp krgfyiralf
      481 dydktkdcgf lsqalsfrfg dvlhvidasd eewwqarrvh sdsetddigf ipskrrverr
      541 ewsrlkakdw gsssgsqgre dsvlsyetvt qmevhyarpi iilgptkdra nddllsefpd
      601 kfgscvphtt rpkreyeidg rdyhfvssre kmekdiqahk fieagqynsh lygtsvqsvr
      661 evaeqgkhci ldvsanavrr lqaahlhpia ifirprslen vleinkrite eqarkafdra
      721 tkleqeftec fsaivegdsf eeiyhkvkrv iedlsgpyiw vparerl
//
LOCUS       NP_001427446             551 aa            linear   PRI 21-NOV-2025
DEFINITION  radixin isoform 10 [Homo sapiens].
ACCESSION   NP_001427446
VERSION     NP_001427446.1
DBSOURCE    REFSEQ: accession NM_001440517.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Kruse,T., Benz,C., Garvanska,D.H., Lindqvist,R., Mihalic,F.,
            Coscia,F., Inturi,R., Sayadi,A., Simonetti,L., Nilsson,E., Ali,M.,
            Kliche,J., Moliner Morro,A., Mund,A., Andersson,E., McInerney,G.,
            Mann,M., Jemth,P., Davey,N.E., Overby,A.K., Nilsson,J. and
            Ivarsson,Y.
  TITLE     Large scale discovery of coronavirus-host factor protein
            interaction motifs reveals SARS-CoV-2 specific mechanisms and
            vulnerabilities
  JOURNAL   Nat Commun 12 (1), 6761 (2021)
   PUBMED   34799561
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Stemmer-Rachamimov,A.O., Gonzalez-Agosti,C., Xu,L., Burwick,J.A.,
            Beauchamp,R., Pinney,D., Louis,D.N. and Ramesh,V.
  TITLE     Expression of NF2-encoded merlin and related ERM family proteins in
            the human central nervous system
  JOURNAL   J Neuropathol Exp Neurol 56 (6), 735-742 (1997)
   PUBMED   9184664
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Hirao,M., Sato,N., Kondo,T., Yonemura,S., Monden,M., Sasaki,T.,
            Takai,Y., Tsukita,S. and Tsukita,S.
  TITLE     Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma
            membrane association: possible involvement of phosphatidylinositol
            turnover and Rho-dependent signaling pathway
  JOURNAL   J Cell Biol 135 (1), 37-51 (1996)
   PUBMED   8858161
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Wilgenbus,K.K., Milatovich,A., Francke,U. and Furthmayr,H.
  TITLE     Molecular cloning, cDNA sequence, and chromosomal assignment of the
            human radixin gene and two dispersed pseudogenes
  JOURNAL   Genomics 16 (1), 199-206 (1993)
   PUBMED   8486357
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Sato,N., Funayama,N., Nagafuchi,A., Yonemura,S., Tsukita,S. and
            Tsukita,S.
  TITLE     A gene family consisting of ezrin, radixin and moesin. Its specific
            localization at actin filament/plasma membrane association sites
  JOURNAL   J Cell Sci 103 (Pt 1), 131-143 (1992)
   PUBMED   1429901
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002788.3 and AP000901.5.
            
            Summary: Radixin is a cytoskeletal protein that may be important in
            linking actin to the plasma membrane. It is highly similar in
            sequence to both ezrin and moesin. The radixin gene has been
            localized by fluorescence in situ hybridization to 11q23. A
            truncated version representing a pseudogene (RDXP2) was assigned to
            Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was
            mapped to 11p by Southern and PCR analyses. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2105209.1,
                                           SRR18074967.3264354.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..551
                     /product="radixin isoform 10"
                     /calculated_mol_wt=64661
     Region          7..174
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          168..264
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(210..211,213..219,228,249,252..253,256)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(210,213..220,228,249,252..253,256)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(246,250)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            249..264
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          315..424
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          475..551
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..551
                     /gene="RDX"
                     /gene_synonym="DFNB24"
                     /coded_by="NM_001440517.1:213..1868"
                     /note="isoform 10 is encoded by transcript variant 19"
                     /db_xref="GeneID:5962"
                     /db_xref="HGNC:HGNC:9944"
                     /db_xref="MIM:179410"
ORIGIN      
        1 mpkpinvrvt tmdaelefai qpnttgkqlf dqvtqqdvkk enplqfkfra kffpedvsee
       61 liqeitqrlf flqvkeailn deiycppeta vllasyavqa kygdynkeih kpgylandrl
      121 lpqrvleqhk ltkeqweeri qnwheehrgm lredsmmeyl kiaqdlemyg vnyfeiknkk
      181 gtelwlgvda lglniyehdd kltpkigfpw seirnisfnd kkfvikpidk kapdfvfyap
      241 rlrinkrila lcmgnhelym rrrkpdtiev qqmkaqaree khqkqleraq lenekkkrei
      301 aekekerier ekeelmerlk qieeqtikaq keleeqtrka leldqerkra keeaerleke
      361 rraaeeaksa iakqaadqmk nqeqlaaela eftakialle eakkkkeeea tewqhkafaa
      421 qedlektkee lktvmsappp pppppvippt enehdehden naeasaelsn egvmnhrsee
      481 ervtetqkne rvkkqlqals selaqardet kktqndvlha envkagrdky ktlrqirqgn
      541 tkqridefea m
//
LOCUS       NP_001427443             572 aa            linear   PRI 21-NOV-2025
DEFINITION  radixin isoform 8 [Homo sapiens].
ACCESSION   NP_001427443
VERSION     NP_001427443.1
DBSOURCE    REFSEQ: accession NM_001440514.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Kruse,T., Benz,C., Garvanska,D.H., Lindqvist,R., Mihalic,F.,
            Coscia,F., Inturi,R., Sayadi,A., Simonetti,L., Nilsson,E., Ali,M.,
            Kliche,J., Moliner Morro,A., Mund,A., Andersson,E., McInerney,G.,
            Mann,M., Jemth,P., Davey,N.E., Overby,A.K., Nilsson,J. and
            Ivarsson,Y.
  TITLE     Large scale discovery of coronavirus-host factor protein
            interaction motifs reveals SARS-CoV-2 specific mechanisms and
            vulnerabilities
  JOURNAL   Nat Commun 12 (1), 6761 (2021)
   PUBMED   34799561
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Stemmer-Rachamimov,A.O., Gonzalez-Agosti,C., Xu,L., Burwick,J.A.,
            Beauchamp,R., Pinney,D., Louis,D.N. and Ramesh,V.
  TITLE     Expression of NF2-encoded merlin and related ERM family proteins in
            the human central nervous system
  JOURNAL   J Neuropathol Exp Neurol 56 (6), 735-742 (1997)
   PUBMED   9184664
REFERENCE   7  (residues 1 to 572)
  AUTHORS   Hirao,M., Sato,N., Kondo,T., Yonemura,S., Monden,M., Sasaki,T.,
            Takai,Y., Tsukita,S. and Tsukita,S.
  TITLE     Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma
            membrane association: possible involvement of phosphatidylinositol
            turnover and Rho-dependent signaling pathway
  JOURNAL   J Cell Biol 135 (1), 37-51 (1996)
   PUBMED   8858161
REFERENCE   8  (residues 1 to 572)
  AUTHORS   Wilgenbus,K.K., Milatovich,A., Francke,U. and Furthmayr,H.
  TITLE     Molecular cloning, cDNA sequence, and chromosomal assignment of the
            human radixin gene and two dispersed pseudogenes
  JOURNAL   Genomics 16 (1), 199-206 (1993)
   PUBMED   8486357
REFERENCE   9  (residues 1 to 572)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 572)
  AUTHORS   Sato,N., Funayama,N., Nagafuchi,A., Yonemura,S., Tsukita,S. and
            Tsukita,S.
  TITLE     A gene family consisting of ezrin, radixin and moesin. Its specific
            localization at actin filament/plasma membrane association sites
  JOURNAL   J Cell Sci 103 (Pt 1), 131-143 (1992)
   PUBMED   1429901
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002788.3 and AP000901.5.
            
            Summary: Radixin is a cytoskeletal protein that may be important in
            linking actin to the plasma membrane. It is highly similar in
            sequence to both ezrin and moesin. The radixin gene has been
            localized by fluorescence in situ hybridization to 11q23. A
            truncated version representing a pseudogene (RDXP2) was assigned to
            Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was
            mapped to 11p by Southern and PCR analyses. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.774573.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2144333,
                                           SAMEA2467144 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..572
                     /product="radixin isoform 8"
                     /calculated_mol_wt=67195
     Region          5..195
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          189..285
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(231..232,234..240,249,270,273..274,277)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(231,234..241,249,270,273..274,277)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(267,271)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            270..285
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          336..445
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          496..572
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..572
                     /gene="RDX"
                     /gene_synonym="DFNB24"
                     /coded_by="NM_001440514.1:608..2326"
                     /note="isoform 8 is encoded by transcript variant 16"
                     /db_xref="GeneID:5962"
                     /db_xref="HGNC:HGNC:9944"
                     /db_xref="MIM:179410"
ORIGIN      
        1 mdaelefaiq pnttgkqlfd qvvktvglre vwffglqyvd skgystwlkl nkkvtqqdvk
       61 kenplqfkfr akffpedvse eliqeitqrl fflqvkeail ndeiycppet avllasyavq
      121 akygdynkei hkpgylandr llpqrvleqh kltkeqweer iqnwheehrg mlredsmmey
      181 lkiaqdlemy gvnyfeiknk kgtelwlgvd alglniyehd dkltpkigfp wseirnisfn
      241 dkkfvikpid kkapdfvfya prlrinkril alcmgnhely mrrrkpdtie vqqmkaqare
      301 ekhqkqlera qlenekkkre iaekekerie rekeelmerl kqieeqtika qkeleeqtrk
      361 aleldqerkr akeeaerlek erraaeeaks aiakqaadqm knqeqlaael aeftakiall
      421 eeakkkkeee atewqhkafa aqedlektke elktvmsapp ppppppvipp tenehdehde
      481 nnaeasaels negvmnhrse eervtetqkn ervkkqlqal sselaqarde tkktqndvlh
      541 aenvkagrdk yktlrqirqg ntkqridefe am
//
LOCUS       NP_001357137             438 aa            linear   PRI 21-NOV-2025
DEFINITION  F-box/LRR-repeat protein 20 isoform 3 [Homo sapiens].
ACCESSION   NP_001357137 XP_005257803
VERSION     NP_001357137.2
DBSOURCE    REFSEQ: accession NM_001370208.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Liu,J., Zhan,W., Chen,G., Yan,S., Chen,W. and Li,R.
  TITLE     SP1-induced PROX1-AS1 contributes to tumor progression by
            regulating miR-326/FBXL20 axis in colorectal cancer
  JOURNAL   Cell Signal 101, 110503 (2023)
   PUBMED   36374774
  REMARK    GeneRIF: SP1-induced PROX1-AS1 contributes to tumor progression by
            regulating miR-326/FBXL20 axis in colorectal cancer.
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Sun,R. and Lim,S.O.
  TITLE     FBXL20-mediated ubiquitination triggers the proteasomal degradation
            of 4-1BB
  JOURNAL   FEBS J 289 (15), 4549-4563 (2022)
   PUBMED   35112462
  REMARK    GeneRIF: FBXL20-mediated ubiquitination triggers the proteasomal
            degradation of 4-1BB.
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Madduri,L.S.V., Brandquist,N.D., Palanivel,C., Talmon,G.A.,
            Baine,M.J., Zhou,S., Enke,C.A., Johnson,K.R., Ouellette,M.M. and
            Yan,Y.
  TITLE     p53/FBXL20 axis negatively regulates the protein stability of
            PR55alpha, a regulatory subunit of PP2A Ser/Thr phosphatase
  JOURNAL   Neoplasia 23 (12), 1192-1203 (2021)
   PUBMED   34731788
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Manne,R.K., Agrawal,Y., Malonia,S.K., Banday,S., Edachery,S.,
            Patel,A., Kumar,A., Shetty,P. and Santra,M.K.
  TITLE     FBXL20 promotes breast cancer malignancy by inhibiting apoptosis
            through degradation of PUMA and BAX
  JOURNAL   J Biol Chem 297 (4), 101253 (2021)
   PUBMED   34587475
  REMARK    GeneRIF: FBXL20 promotes breast cancer malignancy by inhibiting
            apoptosis through degradation of PUMA and BAX.
REFERENCE   6  (residues 1 to 438)
  AUTHORS   Xiao,J., Zhang,T., Xu,D., Wang,H., Cai,Y., Jin,T., Liu,M., Jin,M.,
            Wu,K. and Yuan,J.
  TITLE     FBXL20-mediated Vps34 ubiquitination as a p53 controlled checkpoint
            in regulating autophagy and receptor degradation
  JOURNAL   Genes Dev 29 (2), 184-196 (2015)
   PUBMED   25593308
  REMARK    GeneRIF: which provides a signal to promote its ubiquitination and
            proteasomal degradation mediated by FBXL20 and the associated
            Skp1-Cullin1 complex, leading to inhibition of autophagy and
            receptor endocytosis
REFERENCE   7  (residues 1 to 438)
  AUTHORS   Zhu,J., Li,K., Dong,L. and Chen,Y.
  TITLE     Role of FBXL20 in human colorectal adenocarcinoma
  JOURNAL   Oncol Rep 28 (6), 2290-2298 (2012)
   PUBMED   23023584
  REMARK    GeneRIF: study concludes FBXL20 plays an essential role in the
            carcinogenesis of colorectal adenocarcinoma and promotes
            carcinogenesis through the regulation of the Wnt signaling pathway
            and caspase activation
REFERENCE   8  (residues 1 to 438)
  AUTHORS   Mells,G.F., Floyd,J.A., Morley,K.I., Cordell,H.J., Franklin,C.S.,
            Shin,S.Y., Heneghan,M.A., Neuberger,J.M., Donaldson,P.T., Day,D.B.,
            Ducker,S.J., Muriithi,A.W., Wheater,E.F., Hammond,C.J.,
            Dawwas,M.F., Jones,D.E., Peltonen,L., Alexander,G.J., Sandford,R.N.
            and Anderson,C.A.
  CONSRTM   UK PBC Consortium; Wellcome Trust Case Control Consortium 3
  TITLE     Genome-wide association study identifies 12 new susceptibility loci
            for primary biliary cirrhosis
  JOURNAL   Nat Genet 43 (4), 329-332 (2011)
   PUBMED   21399635
  REMARK    Erratum:[Nat Genet. 2011 Nov;43(11):1164. Richardson,Paul [added];
            Nasr, Ikram [added]; Aspinall,Richard [added]]
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 438)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   10 (residues 1 to 438)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005288.1 and AC015910.10.
            
            On Sep 26, 2022 this sequence version replaced NP_001357137.1.
            
            Summary: Members of the F-box protein family, such as FBXL20, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853565.12429.1,
                                           SRR14038194.2665581.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..438
                     /product="F-box/LRR-repeat protein 20 isoform 3"
                     /note="F-box protein FBL2"
                     /calculated_mol_wt=48445
     Region          24..68
                     /region_name="F-box_FBXL2-like"
                     /note="F-box domain found in F-box/LRR-repeat protein 2
                     (FBXL2), F-box/LRR-repeat protein 20 (FBXL20) and similar
                     proteins; cd22115"
                     /db_xref="CDD:438887"
     Site            order(24..27,29..30,33..34,37..43,46,48..55,57..58,66)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438887"
     Region          67..94
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          95..291
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          95..114
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          121..146
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          147..172
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          173..198
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          199..224
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          222..396
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          225..250
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          251..276
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          277..302
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          303..328
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          329..357
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          358..382
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          383..408
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..438
                     /gene="FBXL20"
                     /gene_synonym="Fbl2; Fbl20"
                     /coded_by="NM_001370208.3:337..1653"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:84961"
                     /db_xref="HGNC:HGNC:24679"
                     /db_xref="MIM:609086"
ORIGIN      
        1 mapsrdrllh fgfkatmfsn sdeavinkkl pkelllrifs fldvvtlcrc aqvsrawnvl
       61 aldgsnwqri dlfdfqrdie grvveniskr cggflrklsl rgclgvgdna lrtfaqncrn
      121 ievlnlngct kttdatctsl skfcsklrhl dlasctsitn mslkalsegc plleqlnisw
      181 cdqvtkdgiq alvrgcgglk alflkgctql edealkyiga hcpelvtlnl qtclqitdeg
      241 liticrgchk lqslcasgcs nitdailnal gqncprlril evarcsqltd vgfttlarnc
      301 helekmdlee cvqitdstli qlsihcprlq vlslshceli tddgirhlgn gacahdqlev
      361 ieldncplit daslehlksc hslerielyd cqqitragik rlrthlpnik vhayfapvtp
      421 ppsvggsrqr fcrcciil
//
LOCUS       NP_001428219             822 aa            linear   PRI 21-NOV-2025
DEFINITION  dynamin-binding protein isoform e [Homo sapiens].
ACCESSION   NP_001428219
VERSION     NP_001428219.1
DBSOURCE    REFSEQ: accession NM_001441290.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Ouyang,C., Mu,J., Lu,Q., Li,J., Zhu,H., Wang,Q., Zou,M.H. and
            Xie,Z.
  TITLE     Autophagic degradation of KAT2A/GCN5 promotes directional migration
            of vascular smooth muscle cells by reducing TUBA/alpha-tubulin
            acetylation
  JOURNAL   Autophagy 16 (10), 1753-1770 (2020)
   PUBMED   31878840
  REMARK    GeneRIF: Autophagic degradation of KAT2A/GCN5 promotes directional
            migration of vascular smooth muscle cells by reducing
            TUBA/alpha-tubulin acetylation.
REFERENCE   5  (residues 1 to 822)
  AUTHORS   Ansar,M., Chung,H.L., Taylor,R.L., Nazir,A., Imtiaz,S.,
            Sarwar,M.T., Manousopoulou,A., Makrythanasis,P., Saeed,S.,
            Falconnet,E., Guipponi,M., Pournaras,C.J., Ansari,M.A., Ranza,E.,
            Santoni,F.A., Ahmed,J., Shah,I., Gul,K., Black,G.C., Bellen,H.J.
            and Antonarakis,S.E.
  TITLE     Bi-allelic Loss-of-Function Variants in DNMBP Cause Infantile
            Cataracts
  JOURNAL   Am J Hum Genet 103 (4), 568-578 (2018)
   PUBMED   30290152
  REMARK    GeneRIF: DNMBP loss-of-function variants cause infantile-onset
            cataracts in humans.
REFERENCE   6  (residues 1 to 822)
  AUTHORS   Minster,R.L., DeKosky,S.T. and Kamboh,M.I.
  TITLE     No association of dynamin binding protein (DNMBP) gene SNPs and
            Alzheimer's disease
  JOURNAL   Neurobiol Aging 29 (10), 1602-1604 (2008)
   PUBMED   17442457
  REMARK    GeneRIF: We observed no association of statistical significance in
            either the total sample or the APOE*4 non-carriers for any of the
            SNPs of Dynamin Binding Protein.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 822)
  AUTHORS   Otani,T., Ichii,T., Aono,S. and Takeichi,M.
  TITLE     Cdc42 GEF Tuba regulates the junctional configuration of simple
            epithelial cells
  JOURNAL   J Cell Biol 175 (1), 135-146 (2006)
   PUBMED   17015620
  REMARK    GeneRIF: Tuba controls the shaping of cell junctions through the
            local activation of Cdc42 and its effectors.
REFERENCE   8  (residues 1 to 822)
  AUTHORS   Kuwano,R., Miyashita,A., Arai,H., Asada,T., Imagawa,M., Shoji,M.,
            Higuchi,S., Urakami,K., Kakita,A., Takahashi,H., Tsukie,T.,
            Toyabe,S., Akazawa,K., Kanazawa,I. and Ihara,Y.
  CONSRTM   Japanese Genetic Study Consortium for Alzeheimer's Disease
  TITLE     Dynamin-binding protein gene on chromosome 10q is associated with
            late-onset Alzheimer's disease
  JOURNAL   Hum Mol Genet 15 (13), 2170-2182 (2006)
   PUBMED   16740596
  REMARK    GeneRIF: Results confirmed DNMBP may be one of the susceptibility
            genes for Alzheimer's disease.
            GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   9  (residues 1 to 822)
  AUTHORS   Cestra,G., Kwiatkowski,A., Salazar,M., Gertler,F. and De Camilli,P.
  TITLE     Tuba, a GEF for CDC42, links dynamin to actin regulatory proteins
  JOURNAL   Methods Enzymol 404, 537-545 (2005)
   PUBMED   16413298
REFERENCE   10 (residues 1 to 822)
  AUTHORS   Salazar,M.A., Kwiatkowski,A.V., Pellegrini,L., Cestra,G.,
            Butler,M.H., Rossman,K.L., Serna,D.M., Sondek,J., Gertler,F.B. and
            De Camilli,P.
  TITLE     Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl
            homology domains, links dynamin to regulation of the actin
            cytoskeleton
  JOURNAL   J Biol Chem 278 (49), 49031-49043 (2003)
   PUBMED   14506234
  REMARK    GeneRIF: functions to bring together dynamin with actin regulatory
            proteins
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL627434.4 and AL392107.17.
            
            Summary: This gene encodes a protein belonging to the guanine
            nucleotide exchange factor family, and which regulates the
            configuration of cell junctions. It contains multiple binding sites
            for dynamin and thus links dynamin to actin regulatory proteins.
            Polymorphisms in this gene have been linked to Alzheimer's disease
            in some populations, though there are conflicting reports of such
            linkages in other populations. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3755266.1,
                                           SRR18074967.3247872.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.2"
     Protein         1..822
                     /product="dynamin-binding protein isoform e"
                     /note="scaffold protein TUBA"
                     /calculated_mol_wt=93239
     Region          31..211
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(37,41,130,162..163,166..167,169..170,173..174,
                     177..178,181,207,211)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          263..453
                     /region_name="BAR_DNMBP"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin
                     Binding Protein; cd07589"
                     /db_xref="CDD:153273"
     Site            order(275,278..279,283,285..286,289..290,292..293,
                     307..308,310..311,314..315,317..318,321,327,330..331,414,
                     417..418,420,425,428..429,431..432,435..436,439..440,
                     442..443,446..447,449..450)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153273"
     Region          534..590
                     /region_name="SH3_DNMBP_C1"
                     /note="First C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11798"
                     /db_xref="CDD:212732"
     Site            order(539,541,544,548,570..571,584,586..587)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212732"
     Region          762..818
                     /region_name="SH3_DNMBP_C2"
                     /note="Second C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba, and similar domains;
                     cd12141"
                     /db_xref="CDD:213017"
     Site            order(767,769,772,776,798..799,812,814..815)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213017"
     CDS             1..822
                     /gene="DNMBP"
                     /gene_synonym="ARHGEF36; CTRCT48; TUBA"
                     /coded_by="NM_001441290.1:87..2555"
                     /note="isoform e is encoded by transcript variant 6"
                     /db_xref="GeneID:23268"
                     /db_xref="HGNC:HGNC:30373"
                     /db_xref="MIM:611282"
ORIGIN      
        1 mtllssqsss lvapsgsvsa enpeqrmlek rakvieellq terdyirdle mcierimvpm
       61 qqaqvpnidf eglfgnmqmv ikvskqllaa leisdavgpv flghrdeleg tykiycqnhd
      121 eaialleiye kdekiqkhlq dsladlksly newgctnyin lgsflikpvq rvmryplllm
      181 ellnstpesh pdkvpltnav lavkeinvni neykrrkdlv lkyrkgdeds lmekisklni
      241 hsiikksnrv sshlkhltgf apqikdevfe eteknfrmqe rliksfirdl slylqhires
      301 acvkvvaavs mwdvcmergh rdleqfervh ryisdqlftn ferterlvis plnqllsmft
      361 gphklvqkrf dklldfynct eraeklkdkk tleelqsarn nyealnaqll delpkfhqya
      421 qglftncvhg yaeahcdfvh qaleqlkpll sllkvagreg nliaifheeh srvlqqlqvf
      481 tffpeslpat kkpferktid rqsarkpllg lpsymlqsee lrasllaryp peklfqaern
      541 fnaaqdldvs llegdlvgvi kkkdpmgsqn rwlidngvtk gfvyssflkp ynprrshsda
      601 svgshsstes ehgsssprfp rqnsgstltf npssmavsft sgscqkqpqd aspppkecdq
      661 gtlsaslnps nsesspsrcp sdpdstsqpr sgdsadvard vkqptatprs yrnfrhpeiv
      721 gysvpgrngq sqdlvkgcar taqapedrst epdgseaegn qvyfavytfk arnpnelsvs
      781 anqklkilef kdvtgnteww laevngkkgy vpsnyirkte yt
//
LOCUS       NP_001425420             759 aa            linear   PRI 21-NOV-2025
DEFINITION  AT-rich interactive domain-containing protein 1B isoform 13 [Homo
            sapiens].
ACCESSION   NP_001425420
VERSION     NP_001425420.1
DBSOURCE    REFSEQ: accession NM_001438491.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Bosch,E., Guse,E., Kirchner,P., Winterpacht,A., Walther,M.,
            Alders,M., Kerkhof,J., Ekici,A.B., Sticht,H., Sadikovic,B., Reis,A.
            and Vasileiou,G.
  TITLE     The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation
  JOURNAL   Hum Genet 143 (8), 965-978 (2024)
   PUBMED   39028335
  REMARK    GeneRIF: The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation.
REFERENCE   3  (residues 1 to 759)
  AUTHORS   Huang,X., Li,H., Yang,S., Ma,M., Lian,Y., Wu,X., Qi,X., Wang,X.,
            Rong,W. and Sheng,X.
  TITLE     De novo variation in ARID1B gene causes Coffin-Siris syndrome 1 in
            a Chinese family with excessive early-onset high myopia
  JOURNAL   BMC Med Genomics 17 (1), 142 (2024)
   PUBMED   38790056
  REMARK    GeneRIF: De novo variation in ARID1B gene causes Coffin-Siris
            syndrome 1 in a Chinese family with excessive early-onset high
            myopia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 759)
  AUTHORS   Hurlstone,A.F., Olave,I.A., Barker,N., van Noort,M. and Clevers,H.
  TITLE     Cloning and characterization of hELD/OSA1, a novel BRG1 interacting
            protein
  JOURNAL   Biochem J 364 (Pt 1), 255-264 (2002)
   PUBMED   11988099
  REMARK    GeneRIF: Cloning and characterization of hELD/OSA1, a novel BRG1
            interacting protein.
REFERENCE   5  (residues 1 to 759)
  AUTHORS   Phelan,M.L., Sif,S., Narlikar,G.J. and Kingston,R.E.
  TITLE     Reconstitution of a core chromatin remodeling complex from SWI/SNF
            subunits
  JOURNAL   Mol Cell 3 (2), 247-253 (1999)
   PUBMED   10078207
REFERENCE   6  (residues 1 to 759)
  AUTHORS   Imbert,G., Saudou,F., Yvert,G., Devys,D., Trottier,Y.,
            Garnier,J.M., Weber,C., Mandel,J.L., Cancel,G., Abbas,N., Durr,A.,
            Didierjean,O., Stevanin,G., Agid,Y. and Brice,A.
  TITLE     Cloning of the gene for spinocerebellar ataxia 2 reveals a locus
            with high sensitivity to expanded CAG/glutamine repeats
  JOURNAL   Nat Genet 14 (3), 285-291 (1996)
   PUBMED   8896557
REFERENCE   7  (residues 1 to 759)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
REFERENCE   8  (residues 1 to 759)
  AUTHORS   Vergano,S.A., van der Sluijs,P.J. and Santen,G.
  TITLE     ARID1B-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31132234
REFERENCE   9  (residues 1 to 759)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
REFERENCE   10 (residues 1 to 759)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355297.20, AL162578.13 and
            AL136091.6.
            
            Summary: This locus encodes an AT-rich DNA interacting
            domain-containing protein. The encoded protein is a component of
            the SWI/SNF chromatin remodeling complex and may play a role in
            cell-cycle activation. The protein encoded by this locus is similar
            to AT-rich interactive domain-containing protein 1A. These two
            proteins function as alternative, mutually exclusive ARID-subunits
            of the SWI/SNF complex. The associated complexes play opposing
            roles. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410571.141809.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..759
                     /product="AT-rich interactive domain-containing protein 1B
                     isoform 13"
                     /note="BRG1-binding protein ELD/OSA1; ELD (eyelid)/OSA
                     protein; BRG1-associated factor 250b; ARID
                     domain-containing protein 1B; AT rich interactive domain
                     1B (SWI1-like)"
                     /calculated_mol_wt=74414
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          155..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          321..414
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          487..546
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            487
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4N7; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          502..506
                     /region_name="LXXLL"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            608
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4N7; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            640
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     CDS             1..759
                     /gene="ARID1B"
                     /gene_synonym="6A3-5; BAF250B; BRIGHT; CSS1; DAN15;
                     ELD/OSA1; MRD12; OSA2; P250R; SMARCF2"
                     /coded_by="NM_001438491.1:304..2583"
                     /note="isoform 13 is encoded by transcript variant 14"
                     /db_xref="GeneID:57492"
                     /db_xref="HGNC:HGNC:18040"
                     /db_xref="MIM:614556"
ORIGIN      
        1 maaraaaaaa aaaararara gsgerrappg prpapgardl eagargaaaa aaapgpmlgg
       61 ggdgggglns vhhhpllprh elnmahnaga aaaagthsak sggseaalke ggsaaalsss
      121 ssssaaaaaa ssssssgpgs ametgllpnh klktvgeapa apphqqhhhh hhahhhhhha
      181 hhlhhhhalq qqlnqfqqqq qqqqqqqqqq qqqqhpisnn nslggaggga pqpgpdmeqp
      241 qhggakdsaa ggqadppgpp llskpgdedd appkmgepag gryehpglga lgtqqppvav
      301 pgggggpaav pefnnyygsa apasggpggr agpcfdqhgg qqspgmgmmh sasaaaagap
      361 gsmdplqnsh egypnsqcnh ypgysrpgag gggggggggg ggsggggggg gagaggagag
      421 avaaaaaaaa aaaggggggg yggssagygv lssprqqggg mmmgpgggga aslskaaags
      481 aaggfqrfag qnqhpsgatp tlnqlltsps pmmrsyggsy peysspsapp pppsqpqsqa
      541 aaagaaaggq qaaagmglgk dmgaqyaaas pawaaaqqrs hpamspgtpg ptmgrsqgsp
      601 mdpmvmkrpq lygmgsnphs qpqqsspypg gsygppgpqr ypigiqgrtp gamagmqypq
      661 qqmppqygqq gvsgycqqgq qpyysqqpqp phlppqaqyl psqsqqryqp qqdmsqegyg
      721 trsqpplapg kpnhedlnli qqerpsslpl llgplhist
//
LOCUS       NP_001394256             287 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 28 [Homo sapiens].
ACCESSION   NP_001394256 XP_005254696
VERSION     NP_001394256.1
DBSOURCE    REFSEQ: accession NM_001407327.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 287)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 287)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 287)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            On May 31, 2022 this sequence version replaced XP_005254696.3.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3065281.1,
                                           SRR18074969.3405900.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..287
                     /product="tropomyosin alpha-1 chain isoform 28"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=32960
     Region          48..259
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..287
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407327.1:84..947"
                     /note="isoform 28 is encoded by transcript variant 28"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle delvslqkkl kgtedeldky
       61 sealkdaqek lelaekkatd aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegqv rqleeqlrim dqtlkalmaa edkysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledkf lcftspktps sswmshlsel ciclfss
//
LOCUS       NP_001425830             336 aa            linear   PRI 21-NOV-2025
DEFINITION  STAM-binding protein isoform 5 [Homo sapiens].
ACCESSION   NP_001425830 XP_011530787 XP_054196183
VERSION     NP_001425830.1
DBSOURCE    REFSEQ: accession NM_001438901.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Zhang,W., Xu,Z., Du,Y., Liu,T., Xiong,Z., Hu,J., Chen,L., Peng,X.
            and Zhou,F.
  TITLE     Identification of STAM-binding protein as a target for the
            treatment of gemcitabine resistance pancreatic cancer in a
            nutrient-poor microenvironment
  JOURNAL   Cell Death Dis 15 (9), 657 (2024)
   PUBMED   39242557
  REMARK    GeneRIF: Identification of STAM-binding protein as a target for the
            treatment of gemcitabine resistance pancreatic cancer in a
            nutrient-poor microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Li,L., Yang,X., He,M., Xu,X., Xuan,X., Zhang,J., Zhang,L., Xu,H.
            and Li,D.
  TITLE     The expression and clinical significance of STAMBP in breast cancer
  JOURNAL   Mol Biol Rep 50 (1), 899-906 (2023)
   PUBMED   36309616
  REMARK    GeneRIF: The expression and clinical significance of STAMBP in
            breast cancer.
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Yang,Q., Yan,D., Zou,C., Xue,Q., Lin,S., Huang,Q., Li,X., Tang,D.,
            Chen,X. and Liu,J.
  TITLE     The deubiquitinating enzyme STAMBP is a newly discovered driver of
            triple-negative breast cancer progression that maintains RAI14
            protein stability
  JOURNAL   Exp Mol Med 54 (11), 2047-2059 (2022)
   PUBMED   36434041
  REMARK    GeneRIF: The deubiquitinating enzyme STAMBP is a newly discovered
            driver of triple-negative breast cancer progression that maintains
            RAI14 protein stability.
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Yu,S., E,C. and Yang,J.
  TITLE     STAM binding protein regulated by hsa_circ_0007334 exerts oncogenic
            potential in pancreatic cancer
  JOURNAL   Pancreatology 22 (7), 1003-1012 (2022)
   PUBMED   36089485
  REMARK    GeneRIF: STAM binding protein regulated by hsa_circ_0007334 exerts
            oncogenic potential in pancreatic cancer.
REFERENCE   6  (residues 1 to 336)
  AUTHORS   Itoh,F., Asao,H., Sugamura,K., Heldin,C.H., ten Dijke,P. and
            Itoh,S.
  TITLE     Promoting bone morphogenetic protein signaling through negative
            regulation of inhibitory Smads
  JOURNAL   EMBO J 20 (15), 4132-4142 (2001)
   PUBMED   11483516
REFERENCE   7  (residues 1 to 336)
  AUTHORS   Endo,K., Takeshita,T., Kasai,H., Sasaki,Y., Tanaka,N., Asao,H.,
            Kikuchi,K., Yamada,M., Chenb,M., O'Shea,J.J. and Sugamura,K.
  TITLE     STAM2, a new member of the STAM family, binding to the Janus
            kinases
  JOURNAL   FEBS Lett 477 (1-2), 55-61 (2000)
   PUBMED   10899310
REFERENCE   8  (residues 1 to 336)
  AUTHORS   Tanaka,N., Kaneko,K., Asao,H., Kasai,H., Endo,Y., Fujita,T.,
            Takeshita,T. and Sugamura,K.
  TITLE     Possible involvement of a novel STAM-associated molecule 'AMSH' in
            intracellular signal transduction mediated by cytokines
  JOURNAL   J Biol Chem 274 (27), 19129-19135 (1999)
   PUBMED   10383417
REFERENCE   9  (residues 1 to 336)
  AUTHORS   Asada,H., Ishii,N., Sasaki,Y., Endo,K., Kasai,H., Tanaka,N.,
            Takeshita,T., Tsuchiya,S., Konno,T. and Sugamura,K.
  TITLE     Grf40, A novel Grb2 family member, is involved in T cell signaling
            through interaction with SLP-76 and LAT
  JOURNAL   J Exp Med 189 (9), 1383-1390 (1999)
   PUBMED   10224278
REFERENCE   10 (residues 1 to 336)
  AUTHORS   Carter,M.T., Mirzaa,G., McDonell,L.M. and Boycott,K.M.
  TITLE     Microcephaly-Capillary Malformation Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24354023
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073046.7.
            
            On or before Apr 25, 2025 this sequence version replaced
            XP_011530787.1, XP_054196183.1.
            
            Summary: Cytokine-mediated signal transduction in the JAK-STAT
            cascade requires the involvement of adaptor molecules. One such
            signal-transducing adaptor molecule contains an SH3 domain that is
            required for induction of MYC and cell growth. The protein encoded
            by this gene binds to the SH3 domain of the signal-transducing
            adaptor molecule, and plays a critical role in cytokine-mediated
            signaling for MYC induction and cell cycle progression. Multiple
            alternatively spliced transcript variants encoding the same protein
            isoform have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.852824.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..336
                     /product="STAM-binding protein isoform 5"
                     /EC_number="3.1.2.15"
                     /note="associated molecule with the SH3 domain of STAM;
                     endosome-associated ubiquitin isopeptidase; testicular
                     secretory protein Li 54"
                     /calculated_mol_wt=38074
     Region          1..127
                     /region_name="Interaction with CHMP3.
                     /evidence=ECO:0000269|PubMed:17146056"
                     /note="propagated from UniProtKB/Swiss-Prot (O95630.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          13..117
                     /region_name="USP8_dimer"
                     /note="USP8 dimerization domain; pfam08969"
                     /db_xref="CDD:462647"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          227..231
                     /region_name="Interaction with STAM.
                     /evidence=ECO:0000269|PubMed:10383417"
                     /note="propagated from UniProtKB/Swiss-Prot (O95630.1)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          254..>335
                     /region_name="MPN"
                     /note="Mpr1p, Pad1p N-terminal (MPN) domains; cl13996"
                     /db_xref="CDD:472685"
     Site            280
                     /site_type="other"
                     /note="Indirect zinc-binding.
                     /evidence=ECO:0000250|UniProtKB:Q96FJ0; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     CDS             1..336
                     /gene="STAMBP"
                     /gene_synonym="AMSH; MICCAP"
                     /coded_by="NM_001438901.1:229..1239"
                     /note="isoform 5 is encoded by transcript variant 19"
                     /db_xref="GeneID:10617"
                     /db_xref="HGNC:HGNC:16950"
                     /db_xref="MIM:606247"
ORIGIN      
        1 msdhgdvslp pedrvralsq lgsavevned ipprryfrsg veiirmasiy seegniehaf
       61 ilynkyitlf ieklpkhrdy ksavipekkd tvkklkeiaf pkaeelkael lkrytkeyte
      121 yneekkkeae elarnmaiqq elekekqrva qqkqqqleqe qfhafeemir nqelekerlk
      181 ivqefgkvdp glggplvpdl ekpsldvfpt ltvssiqpsd chttvrpakp pvvdrslkpg
      241 alsnsesipt idglrhvvvp grlcpqflql asantargve tcgilcgklm rneftithvl
      301 ipkqsagsdy cnteneeelf liqdqqglit lgwiha
//
LOCUS       NP_001427914             600 aa            linear   PRI 21-NOV-2025
DEFINITION  complement factor I isoform 14 precursor [Homo sapiens].
ACCESSION   NP_001427914
VERSION     NP_001427914.1
DBSOURCE    REFSEQ: accession NM_001440985.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Moreno,R. and Broderick,L.
  TITLE     Complement factor I deficiency: Diverse phenotypes
  JOURNAL   J Allergy Clin Immunol 156 (2), 305-307 (2025)
   PUBMED   40127737
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Schwotzer,N., Fakhouri,F., Martins,P.V., Delmas,Y., Caillard,S.,
            Zuber,J., Moranne,O., Mesnard,L., Fremeaux-Bacchi,V. and
            El-Sissy,C.
  TITLE     Hot Spot of Complement Factor I Rare Variant p.Ile357Met in
            Patients With Hemolytic Uremic Syndrome
  JOURNAL   Am J Kidney Dis 84 (2), 244-249 (2024)
   PUBMED   38423159
  REMARK    GeneRIF: Hot Spot of Complement Factor I Rare Variant p.Ile357Met
            in Patients With Hemolytic Uremic Syndrome.
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Felberg,A., Bienkowski,M., Stokowy,T., Myszczynski,K.,
            Polakiewicz,Z., Kitowska,K., Sadej,R., Mohlin,F., Kuzniewska,A.,
            Kowalska,D., Stasilojc,G., Jongerius,I., Spaapen,R.,
            Mesa-Guzman,M., Montuenga,L.M., Blom,A.M., Pio,R. and Okroj,M.
  TITLE     Elevated expression of complement factor I in lung cancer cells
            associates with shorter survival-Potentially via non-canonical
            mechanism
  JOURNAL   Transl Res 269, 1-13 (2024)
   PUBMED   38395390
  REMARK    GeneRIF: Elevated expression of complement factor I in lung cancer
            cells associates with shorter survival-Potentially via
            non-canonical mechanism.
REFERENCE   4  (residues 1 to 600)
  AUTHORS   Massey,V., Nguyen,C.E., Francois,T., De Bruycker,J.J., Bonnefoy,A.,
            Lapeyraque,A.L. and Decaluwe,H.
  TITLE     CNS Inflammation as the First Sign of Complement Factor I
            Deficiency: A Severe Myelitis Treated With Intense Immunotherapy
            and Eculizumab
  JOURNAL   Neurol Neuroimmunol Neuroinflamm 11 (2), e200191 (2024)
   PUBMED   38134378
  REMARK    GeneRIF: CNS Inflammation as the First Sign of Complement Factor I
            Deficiency.
REFERENCE   5  (residues 1 to 600)
  AUTHORS   van de Ven,J.P., Nilsson,S.C., Tan,P.L., Buitendijk,G.H.,
            Ristau,T., Mohlin,F.C., Nabuurs,S.B., Schoenmaker-Koller,F.E.,
            Smailhodzic,D., Campochiaro,P.A., Zack,D.J., Duvvari,M.R.,
            Bakker,B., Paun,C.C., Boon,C.J., Uitterlinden,A.G., Liakopoulos,S.,
            Klevering,B.J., Fauser,S., Daha,M.R., Katsanis,N., Klaver,C.C.,
            Blom,A.M., Hoyng,C.B. and den Hollander,A.I.
  TITLE     A functional variant in the CFI gene confers a high risk of
            age-related macular degeneration
  JOURNAL   Nat Genet 45 (7), 813-817 (2013)
   PUBMED   23685748
  REMARK    GeneRIF: these findings demonstrate that rare, highly penetrant
            mutations in CFI contribute to the genetic burden of age-related
            macular degeneration.
REFERENCE   6  (residues 1 to 600)
  AUTHORS   Martin,B. and Smith,R.J.H.
  TITLE     C3 Glomerulopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301598
REFERENCE   7  (residues 1 to 600)
  AUTHORS   Noris,M., Bresin,E., Mele,C. and Remuzzi,G.
  TITLE     Genetic Atypical Hemolytic-Uremic Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301541
REFERENCE   8  (residues 1 to 600)
  AUTHORS   DiScipio,R.G.
  TITLE     Ultrastructures and interactions of complement factors H and I
  JOURNAL   J Immunol 149 (8), 2592-2599 (1992)
   PUBMED   1401896
REFERENCE   9  (residues 1 to 600)
  AUTHORS   Shiang,R., Murray,J.C., Morton,C.C., Buetow,K.H., Wasmuth,J.J.,
            Olney,A.H., Sanger,W.G. and Goldberger,G.
  TITLE     Mapping of the human complement factor I gene to 4q25
  JOURNAL   Genomics 4 (1), 82-86 (1989)
   PUBMED   2563353
REFERENCE   10 (residues 1 to 600)
  AUTHORS   Catterall,C.F., Lyons,A., Sim,R.B., Day,A.J. and Harris,T.J.
  TITLE     Characterization of primary amino acid sequence of human complement
            control protein factor I from an analysis of cDNA clones
  JOURNAL   Biochem J 242 (3), 849-856 (1987)
   PUBMED   2954545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC126283.3 and AC004067.1.
            
            Summary: This gene encodes a serine proteinase that is essential
            for regulating the complement cascade. The encoded preproprotein is
            cleaved to produce both heavy and light chains, which are linked by
            disulfide bonds to form a heterodimeric glycoprotein. This
            heterodimer can cleave and inactivate the complement components C4b
            and C3b, and it prevents the assembly of the C3 and C5 convertase
            enzymes. Defects in this gene cause complement factor I deficiency,
            an autosomal recessive disease associated with a susceptibility to
            pyogenic infections. Mutations in this gene have been associated
            with a predisposition to atypical hemolytic uremic syndrome, a
            disease characterized by acute renal failure, microangiopathic
            hemolytic anemia and thrombocytopenia. Primary glomerulonephritis
            with immune deposits and age-related macular degeneration are other
            conditions associated with mutations of this gene. [provided by
            RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.249403.1,
                                           SRR14038194.1215525.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..600
                     /product="complement factor I isoform 14 precursor"
                     /EC_number="3.4.21.45"
                     /note="C3b-inactivator; Konglutinogen-activating factor;
                     complement factor I heavy chain; complement component I;
                     C3B/C4B inactivator; complement control protein factor I;
                     light chain of factor I"
                     /calculated_mol_wt=65574
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2281
     Region          43..108
                     /region_name="FIMAC"
                     /note="factor I membrane attack complex; smart00057"
                     /db_xref="CDD:214493"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Region          114..215
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     Region          224..256
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(227,235,246..247)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(239,242,246,252..253)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            249..253
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          257..293
                     /region_name="Ldl_recept_a"
                     /note="Low-density lipoprotein receptor domain class A;
                     pfam00057"
                     /db_xref="CDD:395011"
     Site            order(264,272,283..284)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(276,279,283,289..290)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            286..290
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          347..>518
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            347
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            471
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Site            501
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     CDS             1..600
                     /gene="CFI"
                     /gene_synonym="AHUS3; ARMD13; C3b-INA; C3BINA; FI; IF;
                     KAF"
                     /coded_by="NM_001440985.1:29..1831"
                     /note="isoform 14 precursor is encoded by transcript
                     variant 14"
                     /db_xref="GeneID:3426"
                     /db_xref="HGNC:HGNC:5394"
                     /db_xref="MIM:217030"
ORIGIN      
        1 mkllhvfllf lcfhlrfckv tytsqedlve kkclakkyth lscdkvfcqp wqrciegtcv
       61 cklpyqcpkn gtavcatnrr sfptycqqks leclhpgtkf lnngtctaeg kfsvslkhgn
      121 tdsegivevk lvdqdktmfi cksswsmrea nvacldlgfq qgadtqrrfk lsdlsinste
      181 clhvhcrgle tslaectftk rrtmgyqdfa dvvcytqkad spmddffqcv ngkyisqmka
      241 cdgindcgdq sdelcckacq gkgfhcksgv cipsqyqcng evdcitgede vgcaarhpti
      301 qgfasvtqee teiltadmda errriksllp klscgvknrm hirrkrivgg kraqlgdlpw
      361 qvaikdasgi tcggiyiggc wiltaahclr askthryqiw ttvvdwihpd lkrivieyvd
      421 riifhenyna gtyqndiali emkkdgnkkd celprsipac vpwspylfqp ndtcivsgwg
      481 rekdnervfs lqwgevklis ncskfygnrf yekemecadc csvaqagvqw hdlsslqppp
      541 prfkqfscls lpsswdyrhl pprpesrsvp qagvqwcnls slqhpstswv qvillppppe
//
LOCUS       NP_001427341             321 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 7 precursor [Homo
            sapiens].
ACCESSION   NP_001427341
VERSION     NP_001427341.1
DBSOURCE    REFSEQ: accession NM_001440412.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 321)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3 and AP004147.3.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.2122941.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..321
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     7 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=33613
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..>302
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            286
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     CDS             1..321
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440412.1:296..1261"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 14"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk aaelgmvsay
      241 ytyiftnlef slqrmdslvd drvnilgfsi fnqshaffqe faqslnqswq encdhvpftg
      301 pagilvtvks ghvalldkwg n
//
LOCUS       NP_001427991             762 aa            linear   PRI 21-NOV-2025
DEFINITION  inhibitor of nuclear factor kappa-B kinase subunit alpha isoform 3
            [Homo sapiens].
ACCESSION   NP_001427991
VERSION     NP_001427991.1
DBSOURCE    REFSEQ: accession NM_001441062.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 762)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 762)
  AUTHORS   Chen,X., Wu,W., Jeong,J.H., Rokavec,M., Wei,R., Feng,S.,
            Schroth,W., Brauch,H., Zhong,S. and Luo,J.L.
  TITLE     Cytokines-activated nuclear IKKalpha-FAT10 pathway induces breast
            cancer tamoxifen-resistance
  JOURNAL   Sci China Life Sci 67 (7), 1413-1426 (2024)
   PUBMED   38565741
  REMARK    GeneRIF: Cytokines-activated nuclear IKKalpha-FAT10 pathway induces
            breast cancer tamoxifen-resistance.
REFERENCE   3  (residues 1 to 762)
  AUTHORS   Chang,X., Guo,Y., Zhang,Q., Zheng,X., Cui,X., Hu,J., Zhang,Z.,
            Zhang,F. and Wang,X.
  TITLE     GRP78 recognizes EV-F 3D protein and activates NF-kappaB to repress
            virus replication by interacting with CHUK/IKBKB
  JOURNAL   J Virol 98 (6), e0026824 (2024)
   PUBMED   38775480
  REMARK    GeneRIF: GRP78 recognizes EV-F 3D protein and activates NF-kappaB
            to repress virus replication by interacting with CHUK/IKBKB.
REFERENCE   4  (residues 1 to 762)
  AUTHORS   McIntosh,K., Khalaf,Y.H., Craig,R., West,C., McCulloch,A.,
            Waghmare,A., Lawson,C., Chan,E.Y.W., Mackay,S., Paul,A. and
            Plevin,R.
  TITLE     IL-1beta stimulates a novel, IKKalpha -dependent, NIK -independent
            activation of non-canonical NFkappaB signalling
  JOURNAL   Cell Signal 107, 110684 (2023)
   PUBMED   37080443
  REMARK    GeneRIF: IL-1beta stimulates a novel, IKKalpha -dependent, NIK
            -independent activation of non-canonical NFkappaB signalling.
REFERENCE   5  (residues 1 to 762)
  AUTHORS   Yang,H., Espada,C.E., Phillips,S., Martinez,N., Kenney,A.D.,
            Yount,J.S., Xiong,Y. and Wu,L.
  TITLE     The host antiviral protein SAMHD1 suppresses NF-kappaB activation
            by interacting with the IKK complex during inflammatory responses
            and viral infection
  JOURNAL   J Biol Chem 299 (6), 104750 (2023)
   PUBMED   37100289
  REMARK    GeneRIF: The host antiviral protein SAMHD1 suppresses NF-kappaB
            activation by interacting with the IKK complex during inflammatory
            responses and viral infection.
REFERENCE   6  (residues 1 to 762)
  AUTHORS   Scherer,D.C., Brockman,J.A., Chen,Z., Maniatis,T. and Ballard,D.W.
  TITLE     Signal-induced degradation of I kappa B alpha requires
            site-specific ubiquitination
  JOURNAL   Proc Natl Acad Sci U S A 92 (24), 11259-11263 (1995)
   PUBMED   7479976
REFERENCE   7  (residues 1 to 762)
  AUTHORS   Mock,B.A., Connelly,M.A., McBride,O.W., Kozak,C.A. and Marcu,K.B.
  TITLE     CHUK, a conserved helix-loop-helix ubiquitous kinase, maps to human
            chromosome 10 and mouse chromosome 19
  JOURNAL   Genomics 27 (2), 348-351 (1995)
   PUBMED   7558004
REFERENCE   8  (residues 1 to 762)
  AUTHORS   Connelly,M.A. and Marcu,K.B.
  TITLE     CHUK, a new member of the helix-loop-helix and leucine zipper
            families of interacting proteins, contains a serine-threonine
            kinase catalytic domain
  JOURNAL   Cell Mol Biol Res 41 (6), 537-549 (1995)
   PUBMED   8777433
REFERENCE   9  (residues 1 to 762)
  AUTHORS   Ganchi,P.A., Sun,S.C., Greene,W.C. and Ballard,D.W.
  TITLE     A novel NF-kappa B complex containing p65 homodimers: implications
            for transcriptional control at the level of subunit dimerization
  JOURNAL   Mol Cell Biol 13 (12), 7826-7835 (1993)
   PUBMED   8246997
REFERENCE   10 (residues 1 to 762)
  AUTHORS   Ganchi,P.A., Sun,S.C., Greene,W.C. and Ballard,D.W.
  TITLE     I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B
            p65 and requires the transactivation domain to inhibit NF-kappa B
            p65 DNA binding
  JOURNAL   Mol Biol Cell 3 (12), 1339-1352 (1992)
   PUBMED   1493333
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138921.14.
            
            Summary: This gene encodes a member of the serine/threonine protein
            kinase family. The encoded protein, a component of a
            cytokine-activated protein complex that is an inhibitor of the
            essential transcription factor NF-kappa-B complex, phosphorylates
            sites that trigger the degradation of the inhibitor via the
            ubiquination pathway, thereby activating the transcription factor.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.3960370.1,
                                           SRR14038192.632938.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.31"
     Protein         1..762
                     /product="inhibitor of nuclear factor kappa-B kinase
                     subunit alpha isoform 3"
                     /EC_number="2.7.11.10"
                     /note="I-kappa-B kinase-alpha; I-kappa-B kinase 1; Nuclear
                     factor NFkappaB inhibitor kinase alpha; IKK-a kinase; IkB
                     kinase alpha subunit; inhibitor of nuclear factor kappa-B
                     kinase subunit alpha; conserved helix-loop-helix
                     ubiquitous kinase; transcription factor 16"
                     /calculated_mol_wt=86492
     Region          21..309
                     /region_name="STKc_IKK_alpha"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha;
                     cd14039"
                     /db_xref="CDD:270941"
     Site            order(21..25,29,42,44,74,95..98,102,104,144,146,148..149,
                     151,165,168,183..186)
                     /site_type="active"
                     /db_xref="CDD:270941"
     Site            order(21..25,29,42,44,74,95..98,102,144,146,148..149,151,
                     165)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270941"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1 and SGK1.
                     /evidence=ECO:0000269|PubMed:10485710,
                     ECO:0000269|PubMed:19088076; propagated from
                     UniProtKB/Swiss-Prot (O15111.2)"
     Site            order(25,102,104,144,146,148,168,183..186)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270941"
     Site            order(108,110,114,117,218,223,251..252,254,260..263)
                     /site_type="other"
                     /note="putative SDD interface [polypeptide binding]"
                     /db_xref="CDD:270941"
     Site            164..186
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270941"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAP3K14.
                     /evidence=ECO:0000269|PubMed:9520446; propagated from
                     UniProtKB/Swiss-Prot (O15111.2)"
     Site            179
                     /site_type="acetylation"
                     /note="(Microbial infection) O-acetylthreonine, by
                     Yersinia YopJ. /evidence=ECO:0000269|PubMed:17116858;
                     propagated from UniProtKB/Swiss-Prot (O15111.2)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by SGK1.
                     /evidence=ECO:0000269|PubMed:19088076; propagated from
                     UniProtKB/Swiss-Prot (O15111.2)"
     Region          311..387
                     /region_name="Ubl_IKKA_like"
                     /note="ubiquitin-like (Ubl) domain found in inhibitor of
                     nuclear factor kappa-B kinases, IKK-alpha and IKK-beta,
                     and similar proteins; cd17046"
                     /db_xref="CDD:340566"
     Region          386..659
                     /region_name="IKBKB_SDD"
                     /note="IQBAL scaffold dimerization domain; pfam18397"
                     /db_xref="CDD:465745"
     Region          455..476
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (O15111.2)"
     Region          707..737
                     /region_name="IKKbetaNEMObind"
                     /note="I-kappa-kinase-beta NEMO binding domain; pfam12179"
                     /db_xref="CDD:463485"
     CDS             1..762
                     /gene="CHUK"
                     /gene_synonym="BPS2; IKBKA; IKK-1; IKK-alpha; IKK1; IKKA;
                     NFKBIKA; TCF16"
                     /coded_by="NM_001441062.1:65..2353"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:1147"
                     /db_xref="HGNC:HGNC:1974"
                     /db_xref="MIM:600664"
ORIGIN      
        1 merppglrpg aggpwemrer lgtggfgnvc lyqhreldlk iaikscrlel stknrerwch
       61 eiqimkklnh anvvkacdvp eelnilihdv pllameycsg gdlrkllnkp enccglkesq
      121 ilsllsdigs girylhenki ihrdlkpeni vlqdvggkii hkiidlgyak dvdqgslcts
      181 fvgtlqylap elfenkpyta tvdywsfgtm vfeciagyrp flhhlqpftw hekikkkdpk
      241 cifaceemsg evrfsshlpq pnslcslvve pmenwlqlml nwdpqqrggp vdltlkqprc
      301 fvlmdhilnl kivhilnmts akiisfllpp deslhslqsr ieretgintg sqellsetgi
      361 sldprkpasq cvldgvrgcd symvylfdks ktvyegpfas rslsdcvnyi vqdskiqlpi
      421 iqlrkvwaea vhyvsglked ysrlfqgqra amlsllryna nltkmkntli sasqqlkakl
      481 effhksiqld leryseqmty gissekmlka wkemeekaih yaevgvigyl edqimslhae
      541 imelqkspyg rrqgdlmesl eqraidlykq lkhrpsdhsy sdstemvkii vhtvqsqdrv
      601 lkelfghlsk llgckqkiid llpkvevals nikeadntvm fmqgkrqkei whllkiactq
      661 ssarslvgss legavtpqts awlpptsaeh dhslscvvtp qdgetsaqmi eenlnclghl
      721 stiiheanee qgnsmmtsvn grngyeqklh fyydqknmil qv
//
LOCUS       NP_001425596             855 aa            linear   PRI 21-NOV-2025
DEFINITION  dipeptidyl peptidase 8 isoform 5 [Homo sapiens].
ACCESSION   NP_001425596 XP_047288715 XP_054234275
VERSION     NP_001425596.1
DBSOURCE    REFSEQ: accession NM_001438667.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 855)
  AUTHORS   Li,K., Zhang,Y., Zhao,W., Wang,R., Li,Y., Wei,L., Wang,L., Chen,X.,
            Chen,Z., Liu,P., Nie,N., Tian,X. and Fu,R.
  TITLE     DPP8/9 inhibition attenuates the TGF-beta1-induced excessive
            deposition of extracellular matrix (ECM) in human mesangial cells
            via Smad and Akt signaling pathways
  JOURNAL   Toxicol Lett 395, 1-10 (2024)
   PUBMED   38458339
  REMARK    GeneRIF: DPP8/9 inhibition attenuates the TGF-beta1-induced
            excessive deposition of extracellular matrix (ECM) in human
            mesangial cells via Smad and Akt signaling pathways.
REFERENCE   3  (residues 1 to 855)
  AUTHORS   Zhang,Y., Li,K., Li,Y., Zhao,W., Wang,L., Chen,Z., Ma,X., Yao,T.,
            Wang,J., Dong,W., Li,X., Tian,X. and Fu,R.
  TITLE     Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the
            proximal renal tubule epithelial cells
  JOURNAL   Pharmacol Res 169, 105630 (2021)
   PUBMED   33932609
  REMARK    GeneRIF: Profibrotic mechanisms of DPP8 and DPP9 highly expressed
            in the proximal renal tubule epithelial cells.
REFERENCE   4  (residues 1 to 855)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 855)
  AUTHORS   Hollingsworth,L.R., Sharif,H., Griswold,A.R., Fontana,P.,
            Mintseris,J., Dagbay,K.B., Paulo,J.A., Gygi,S.P., Bachovchin,D.A.
            and Wu,H.
  TITLE     DPP9 sequesters the C terminus of NLRP1 to repress inflammasome
            activation
  JOURNAL   Nature 592 (7856), 778-783 (2021)
   PUBMED   33731932
REFERENCE   6  (residues 1 to 855)
  AUTHORS   Chen,Y.S., Chien,C.H., Goparaju,C.M., Hsu,J.T., Liang,P.H. and
            Chen,X.
  TITLE     Purification and characterization of human prolyl dipeptidase DPP8
            in Sf9 insect cells
  JOURNAL   Protein Expr Purif 35 (1), 142-146 (2004)
   PUBMED   15039077
REFERENCE   7  (residues 1 to 855)
  AUTHORS   Shu,H., Chen,S., Bi,Q., Mumby,M. and Brekken,D.L.
  TITLE     Identification of phosphoproteins and their phosphorylation sites
            in the WEHI-231 B lymphoma cell line
  JOURNAL   Mol Cell Proteomics 3 (3), 279-286 (2004)
   PUBMED   14729942
REFERENCE   8  (residues 1 to 855)
  AUTHORS   Qi,S.Y., Riviere,P.J., Trojnar,J., Junien,J.L. and Akinsanya,K.O.
  TITLE     Cloning and characterization of dipeptidyl peptidase 10, a new
            member of an emerging subgroup of serine proteases
  JOURNAL   Biochem J 373 (Pt 1), 179-189 (2003)
   PUBMED   12662155
REFERENCE   9  (residues 1 to 855)
  AUTHORS   Ajami,K., Abbott,C.A., Obradovic,M., Gysbers,V., Kahne,T.,
            McCaughan,G.W. and Gorrell,M.D.
  TITLE     Structural requirements for catalysis, expression, and dimerization
            in the CD26/DPIV gene family
  JOURNAL   Biochemistry 42 (3), 694-701 (2003)
   PUBMED   12534281
REFERENCE   10 (residues 1 to 855)
  AUTHORS   Abbott,C.A., Yu,D.M., Woollatt,E., Sutherland,G.R., McCaughan,G.W.
            and Gorrell,M.D.
  TITLE     Cloning, expression and chromosomal localization of a novel human
            dipeptidyl peptidase (DPP) IV homolog, DPP8
  JOURNAL   Eur J Biochem 267 (20), 6140-6150 (2000)
   PUBMED   11012666
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011846.16 and AC105129.4.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047288715.1, XP_054234275.1.
            
            Summary: This gene encodes a member of the peptidase S9B family, a
            small family of dipeptidyl peptidases that are able to cleave
            peptide substrates at a prolyl bond. The encoded protein shares
            similarity with dipeptidyl peptidase IV in that it is ubiquitously
            expressed, and hydrolyzes the same substrates. These similarities
            suggest that, like dipeptidyl peptidase IV, this protein may play a
            role in T-cell activation and immune function. Alternatively
            spliced transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2296040.1,
                                           SRR14038195.2590759.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..855
                     /product="dipeptidyl peptidase 8 isoform 5"
                     /EC_number="3.4.14.5"
                     /note="prolyl dipeptidase DPP8; dipeptidyl peptidase VIII;
                     DPP VIII; dipeptidyl peptidase IV-related protein 1"
                     /calculated_mol_wt=98296
     Region          8..162
                     /region_name="Dpp_8_9_N"
                     /note="Dipeptidyl peptidase 8 and 9 N-terminal; pfam19520"
                     /db_xref="CDD:466112"
     Region          175..552
                     /region_name="DPPIV_N"
                     /note="Dipeptidyl peptidase IV (DPP IV) N-terminal region;
                     pfam00930"
                     /db_xref="CDD:395744"
     Region          644..848
                     /region_name="Peptidase_S9"
                     /note="Prolyl oligopeptidase family; pfam00326"
                     /db_xref="CDD:459761"
     CDS             1..855
                     /gene="DPP8"
                     /gene_synonym="DP8; DPRP-1; DPRP1; MST097; MSTP097;
                     MSTP135; MSTP141"
                     /coded_by="NM_001438667.1:304..2871"
                     /note="isoform 5 is encoded by transcript variant 9"
                     /db_xref="GeneID:54878"
                     /db_xref="HGNC:HGNC:16490"
                     /db_xref="MIM:606819"
ORIGIN      
        1 mwkrseqmki ksgkcnmaaa meteqlgvei fetadceeni esqdrpklep fyveryswsq
       61 lkklladtrk yhgymmakap hdfmfvkrnd pdgphsdriy ylamsgenre ntlfyseipk
      121 tinraavlml swkplldlfq atldygmysr eeellrerkr igtvgiasyd yhqgsgtflf
      181 qagsgiyhvk dggpqgftqq plrpnlvets cpnirmdpkl cpadpdwiaf ihsndiwisn
      241 ivtreerrlt yvhnelanme edarsagvat fvlqeefdry sgywwcpkae tstanpkvtf
      301 kmseimidae griidvidke liqpfeilfe gveyiaragw tpegkyawsi lldrsqtrlq
      361 ivlispelfi pveddvmerq rliesvpdsv tpliiyeett diwinihdif hvfpqsheee
      421 iefifaseck tgfrhlykit silkeskykr ssgglpapsd fkcpikeeia itsgewevlg
      481 rhgsniqvde vrrlvyfegt kdsplehhly vvsyvnpgev trltdrgysh sccisqhcdf
      541 fiskysnqkn phcvslykls speddptckt kefwatilds agplpdytpp eifsfesttg
      601 ftlygmlykp hdlqpgkkyp tvlfiyggpq vqlvnnrfkg vkyfrlntla slgyvvvvid
      661 nrgschrglk fegafkykmg qieiddqveg lqylasrydf idldrvgihg wsyggylslm
      721 almqrsdifr vaiagapvtl wifydtgyte rymghpdqne qgyylgsvam qaekfpsepn
      781 rllllhgfld envhfahtsi llsflvragk pydlqiypqe rhsirvpesg ehyelhllhy
      841 lqenlgsria alkvi
//
LOCUS       NP_001428085             431 aa            linear   PRI 21-NOV-2025
DEFINITION  urokinase-type plasminogen activator isoform 1 preproprotein [Homo
            sapiens].
ACCESSION   NP_001428085
VERSION     NP_001428085.1
DBSOURCE    REFSEQ: accession NM_001441156.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Li,D., Ding,C., Huang,F., Chang,M., Lu,Z., Li,G., Li,Y., Gao,H. and
            Sun,F.
  TITLE     Bioinformatics Analysis of the Expression and Prognostic Value of
            PLAU Gene in Wilms' Tumor
  JOURNAL   Anticancer Res 44 (9), 3829-3842 (2024)
   PUBMED   39197889
  REMARK    GeneRIF: Bioinformatics Analysis of the Expression and Prognostic
            Value of PLAU Gene in Wilms' Tumor.
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Guo,J., Wang,H., Huang,C., Lai,C., Shang,W., Luo,S. and Chen,L.
  TITLE     PLAU, transcriptionally negatively regulated by GATA6, promotes
            lung squamous carcinoma cell proliferation and migration
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (5), 119744 (2024)
   PUBMED   38702016
  REMARK    GeneRIF: PLAU, transcriptionally negatively regulated by GATA6,
            promotes lung squamous carcinoma cell proliferation and migration.
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Cui,X., Sun,H., Liu,X., Bai,Y., Bai,Y., Cui,Y., Wang,B., Zhang,S.
            and Li,X.
  TITLE     PLAU promotes cell proliferation and migration of head and neck
            cancer via STAT3 signaling pathway
  JOURNAL   Exp Cell Res 438 (2), 114056 (2024)
   PUBMED   38663475
  REMARK    GeneRIF: PLAU promotes cell proliferation and migration of head and
            neck cancer via STAT3 signaling pathway.
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Cetinsoy,O., Anyanwu,I., Krishnanand,H., Natarajan,G.,
            Ramachandran,N., Thomas,A. and Brookes,K.J.
  TITLE     Gene Association Study of the Urokinase Plasminogen Activator and
            Its Receptor Gene in Alzheimer's Disease
  JOURNAL   J Alzheimers Dis 99 (1), 241-250 (2024)
   PUBMED   38669542
  REMARK    GeneRIF: Gene Association Study of the Urokinase Plasminogen
            Activator and Its Receptor Gene in Alzheimer's Disease.
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Mekkawy,A.H., Pourgholami,M.H. and Morris,D.L.
  TITLE     Involvement of urokinase-type plasminogen activator system in
            cancer: an overview
  JOURNAL   Med Res Rev 34 (5), 918-956 (2014)
   PUBMED   24549574
  REMARK    Review article
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Naldini,L., Tamagnone,L., Vigna,E., Sachs,M., Hartmann,G.,
            Birchmeier,W., Daikuhara,Y., Tsubouchi,H., Blasi,F. and
            Comoglio,P.M.
  TITLE     Extracellular proteolytic cleavage by urokinase is required for
            activation of hepatocyte growth factor/scatter factor
  JOURNAL   EMBO J 11 (13), 4825-4833 (1992)
   PUBMED   1334458
REFERENCE   8  (residues 1 to 431)
  AUTHORS   Li,X., Smith,R.A. and Dobson,C.M.
  TITLE     Sequential 1H NMR assignments and secondary structure of the
            kringle domain from urokinase
  JOURNAL   Biochemistry 31 (40), 9562-9571 (1992)
   PUBMED   1327118
REFERENCE   9  (residues 1 to 431)
  AUTHORS   Stephens,R.W., Aumailley,M., Timpl,R., Reisberg,T., Tapiovaara,H.,
            Myohanen,H., Murphy-Ullrich,J. and Vaheri,A.
  TITLE     Urokinase binding to laminin-nidogen. Structural requirements and
            interactions with heparin
  JOURNAL   Eur J Biochem 207 (3), 937-942 (1992)
   PUBMED   1499567
REFERENCE   10 (residues 1 to 431)
  AUTHORS   Moroi,M. and Aoki,N.
  TITLE     Isolation and characterization of alpha2-plasmin inhibitor from
            human plasma. A novel proteinase inhibitor which inhibits
            activator-induced clot lysis
  JOURNAL   J Biol Chem 251 (19), 5956-5965 (1976)
   PUBMED   134998
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22.
            
            Summary: This gene encodes a secreted serine protease that converts
            plasminogen to plasmin. The encoded preproprotein is
            proteolytically processed to generate A and B polypeptide chains.
            These chains associate via a single disulfide bond to form the
            catalytically inactive high molecular weight urokinase-type
            plasminogen activator (HMW-uPA). HMW-uPA can be further processed
            into the catalytically active low molecular weight urokinase-type
            plasminogen activator (LMW-uPA). This low molecular weight form
            does not bind to the urokinase-type plasminogen activator receptor.
            Mutations in this gene may be associated with Quebec platelet
            disorder and late-onset Alzheimer's disease. Alternative splicing
            results in multiple transcript variants, at least one of which
            encodes an isoform that is proteolytically processed. [provided by
            RefSeq, Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.734152.1,
                                           SRR18074969.2163091.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147596, SAMEA2152474
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..431
                     /product="urokinase-type plasminogen activator isoform 1
                     preproprotein"
                     /EC_number="3.4.21.73"
                     /note="plasminogen activator, urinary; U-plasminogen
                     activator; urokinase-type plasminogen activator"
                     /calculated_mol_wt=46384
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2158
     mat_peptide     21..431
                     /product="Urokinase-type plasminogen activator.
                     /id=PRO_0000028318"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=46384
     mat_peptide     21..177
                     /product="Urokinase-type plasminogen activator long chain
                     A. /id=PRO_0000028319"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=17849
     Region          34..57
                     /region_name="Binds urokinase plasminogen activator
                     surface receptor. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
     Site            38
                     /site_type="glycosylation"
                     /note="O-linked (Fuc) threonine.
                     /evidence=ECO:0000269|PubMed:2023947; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Region          67..152
                     /region_name="KR"
                     /note="Kringle domain; Kringle domains are believed to
                     play a role in binding mediators, such as peptides, other
                     proteins, membranes, or phospholipids. They are autonomous
                     structural domains, found in a varying number of copies,
                     in blood clotting and...; cd00108"
                     /db_xref="CDD:238056"
     Site            79
                     /site_type="active"
                     /note="putative domain interaction site [active]"
                     /db_xref="CDD:238056"
     Site            order(94,104,132,134,143)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Region          152..177
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
     mat_peptide     156..177
                     /product="Urokinase-type plasminogen activator short chain
                     A. /id=PRO_0000028320"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=2574
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9151681; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Site            177..178
                     /site_type="cleavage"
                     /note="Cleavage, during zymogen activation; propagated
                     from UniProtKB/Swiss-Prot (P00749.3)"
     mat_peptide     179..431
                     /product="Urokinase-type plasminogen activator chain B.
                     /id=PRO_0000028321"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=28425
     Region          179..422
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            179
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(224,275,376)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            322
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine. /id=CAR_000026;
                     propagated from UniProtKB/Swiss-Prot (P00749.3)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9151681; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Site            order(370,395,397)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..431
                     /gene="PLAU"
                     /gene_synonym="ATF; BDPLT5; QPD; u-PA; UPA; URK"
                     /coded_by="NM_001441156.1:172..1467"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:5328"
                     /db_xref="HGNC:HGNC:9052"
                     /db_xref="MIM:191840"
ORIGIN      
        1 mrallarlll cvlvvsdskg snelhqvpsn cdclnggtcv snkyfsnihw cncpkkfggq
       61 hceidksktc yegnghfyrg kastdtmgrp clpwnsatvl qqtyhahrsd alqlglgkhn
      121 ycrnpdnrrr pwcyvqvglk llvqecmvhd cadgkkpssp peelkfqcgq ktlrprfkii
      181 ggefttienq pwfaaiyrrh rggsvtyvcg gslispcwvi sathcfidyp kkedyivylg
      241 rsrlnsntqg emkfevenli lhkdysadtl ahhndiallk irskegrcaq psrtiqticl
      301 psmyndpqfg tsceitgfgk enstdylype qlkmtvvkli shrecqqphy ygsevttkml
      361 caadpqwktd scqgdsggpl vcslqgrmtl tgivswgrgc alkdkpgvyt rvshflpwir
      421 shtkeengla l
//
LOCUS       NP_001393670             952 aa            linear   PRI 21-NOV-2025
DEFINITION  lysosomal alpha-glucosidase preproprotein [Homo sapiens].
ACCESSION   NP_001393670 XP_005257250
VERSION     NP_001393670.1
DBSOURCE    REFSEQ: accession NM_001406741.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 952)
  AUTHORS   Colella,P.
  TITLE     Advances in Pompe Disease Treatment: From Enzyme Replacement to
            Gene Therapy
  JOURNAL   Mol Diagn Ther 28 (6), 703-719 (2024)
   PUBMED   39134822
  REMARK    Review article
REFERENCE   2  (residues 1 to 952)
  AUTHORS   Ruiz-Saavedra,S., Salazar,N., Suarez,A., Diaz,Y., Gonzalez Del
            Rey,C., Gonzalez,S. and de Los Reyes-Gavilan,C.G.
  TITLE     Human fecal alpha-glucosidase activity and its relationship with
            gut microbiota profiles and early stages of intestinal mucosa
            damage
  JOURNAL   Anaerobe 87, 102853 (2024)
   PUBMED   38614290
  REMARK    GeneRIF: Human fecal alpha-glucosidase activity and its
            relationship with gut microbiota profiles and early stages of
            intestinal mucosa damage.
REFERENCE   3  (residues 1 to 952)
  AUTHORS   Schoser,B., Raben,N., Varfaj,F., Walzer,M. and Toscano,A.
  TITLE     Acid alpha-glucosidase (GAA) activity and glycogen content in
            muscle biopsy specimens of patients with Pompe disease: A
            systematic review
  JOURNAL   Mol Genet Metab Rep 39, 101085 (2024)
   PUBMED   38698877
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 952)
  AUTHORS   Lim,J.A., Li,L. and Raben,N.
  TITLE     Pompe disease: from pathophysiology to therapy and back again
  JOURNAL   Front Aging Neurosci 6, 177 (2014)
   PUBMED   25183957
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 952)
  AUTHORS   Moreland,R.J., Jin,X., Zhang,X.K., Decker,R.W., Albee,K.L.,
            Lee,K.L., Cauthron,R.D., Brewer,K., Edmunds,T. and Canfield,W.M.
  TITLE     Lysosomal acid alpha-glucosidase consists of four different
            peptides processed from a single chain precursor
  JOURNAL   J Biol Chem 280 (8), 6780-6791 (2005)
   PUBMED   15520017
  REMARK    GeneRIF: data show that the mature forms of GAA characterized by
            polypeptides of 76 or 70 kDa are in fact larger molecular mass
            multicomponent enzyme complexes; peptides released during
            proteolytic processing remained tightly associated with the major
            species
REFERENCE   6  (residues 1 to 952)
  AUTHORS   Sperry,E., Leslie,N., Berry,L. and Pena,L.
  TITLE     Pompe Disease
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301438
REFERENCE   7  (residues 1 to 952)
  AUTHORS   Martiniuk,F., Mehler,M., Bodkin,M., Tzall,S., Hirschhorn,K.,
            Zhong,N. and Hirschhorn,R.
  TITLE     Identification of a missense mutation in an adult-onset patient
            with glycogenosis type II expressing only one allele
  JOURNAL   DNA Cell Biol 10 (9), 681-687 (1991)
   PUBMED   1684505
REFERENCE   8  (residues 1 to 952)
  AUTHORS   Zhong,N., Martiniuk,F., Tzall,S. and Hirschhorn,R.
  TITLE     Identification of a missense mutation in one allele of a patient
            with Pompe disease, and use of endonuclease digestion of
            PCR-amplified RNA to demonstrate lack of mRNA expression from the
            second allele
  JOURNAL   Am J Hum Genet 49 (3), 635-645 (1991)
   PUBMED   1652892
REFERENCE   9  (residues 1 to 952)
  AUTHORS   Hoefsloot,L.H., Hoogeveen-Westerveld,M., Kroos,M.A., van
            Beeumen,J., Reuser,A.J. and Oostra,B.A.
  TITLE     Primary structure and processing of lysosomal alpha-glucosidase;
            homology with the intestinal sucrase-isomaltase complex
  JOURNAL   EMBO J 7 (6), 1697-1704 (1988)
   PUBMED   3049072
REFERENCE   10 (residues 1 to 952)
  AUTHORS   Murray,A.K., Brown,B.I. and Brown,D.H.
  TITLE     The molecular heterogeneity of purified human liver lysosomal
            alpha-glucosidase (acid alpha-glucosidase)
  JOURNAL   Arch Biochem Biophys 185 (2), 511-524 (1978)
   PUBMED   24417
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087741.18.
            
            On May 20, 2022 this sequence version replaced XP_005257250.1.
            
            Summary: This gene encodes lysosomal alpha-glucosidase, which is
            essential for the degradation of glycogen to glucose in lysosomes.
            The encoded preproprotein is proteolytically processed to generate
            multiple intermediate forms and the mature form of the enzyme.
            Defects in this gene are the cause of glycogen storage disease II,
            also known as Pompe's disease, which is an autosomal recessive
            disorder with a broad clinical spectrum. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jan
            2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1381455.1,
                                           SRR14038191.2153984.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..952
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..952
                     /product="lysosomal alpha-glucosidase preproprotein"
                     /EC_number="3.2.1.20"
                     /note="lysosomal alpha-glucosidase; acid maltase;
                     aglucosidase alfa; glucosidase alpha, acid"
                     /calculated_mol_wt=102542
     sig_peptide     1..27
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10253.4)"
                     /calculated_mol_wt=2800
     Region          47..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10253.4)"
     mat_peptide     70..952
                     /product="Lysosomal alpha-glucosidase. /id=PRO_0000018566"
                     /note="propagated from UniProtKB/Swiss-Prot (P10253.4)"
                     /calculated_mol_wt=98009
     Region          81..132
                     /region_name="PD"
                     /note="P or trefoil or TFF domain; smart00018"
                     /db_xref="CDD:197472"
     Site            order(95,125..126)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:238059"
     Site            order(111,125)
                     /site_type="active"
                     /note="putative binding specificity loop [active]"
                     /db_xref="CDD:238059"
     mat_peptide     123..952
                     /product="76 kDa lysosomal alpha-glucosidase.
                     /id=PRO_0000018567"
                     /note="propagated from UniProtKB/Swiss-Prot (P10253.4)"
                     /calculated_mol_wt=92314
     Site            140
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:8435067,
                     ECO:0000269|Ref.19, ECO:0007744|PDB:5KZW,
                     ECO:0007744|PDB:5NN3; propagated from UniProtKB/Swiss-Prot
                     (P10253.4)"
     Region          159..254
                     /region_name="NtCtMGAM_N"
                     /note="N-terminal barrel of NtMGAM and CtMGAM,
                     maltase-glucoamylase; pfam16863"
                     /db_xref="CDD:465286"
     mat_peptide     204..952
                     /product="70 kDa lysosomal alpha-glucosidase.
                     /id=PRO_0000018568"
                     /note="propagated from UniProtKB/Swiss-Prot (P10253.4)"
                     /calculated_mol_wt=82826
     Site            233
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29061980,
                     ECO:0000269|PubMed:8435067, ECO:0000269|Ref.19,
                     ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5NN3; propagated
                     from UniProtKB/Swiss-Prot (P10253.4)"
     Region          246..359
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            282
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          340..824
                     /region_name="Glyco_hydro_31"
                     /note="Glycosyl hydrolases family 31; pfam01055"
                     /db_xref="CDD:460044"
     Site            390
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:8435067,
                     ECO:0000269|Ref.19, ECO:0007744|PDB:5KZW,
                     ECO:0007744|PDB:5NN3; propagated from UniProtKB/Swiss-Prot
                     (P10253.4)"
     Site            470
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:29061980,
                     ECO:0000269|PubMed:8435067, ECO:0000269|Ref.19,
                     ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5NN3; propagated
                     from UniProtKB/Swiss-Prot (P10253.4)"
     Site            652
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29061980,
                     ECO:0000269|PubMed:8435067, ECO:0000269|Ref.19,
                     ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5NN3; propagated
                     from UniProtKB/Swiss-Prot (P10253.4)"
     Site            882
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:8435067,
                     ECO:0000269|Ref.19, ECO:0007744|PDB:5KZW,
                     ECO:0007744|PDB:5NN3; propagated from UniProtKB/Swiss-Prot
                     (P10253.4)"
     Site            925
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:8435067; propagated from
                     UniProtKB/Swiss-Prot (P10253.4)"
     CDS             1..952
                     /gene="GAA"
                     /gene_synonym="IOPD; LOPD; LYAG"
                     /coded_by="NM_001406741.1:253..3111"
                     /db_xref="CCDS:CCDS32760.1"
                     /db_xref="GeneID:2548"
                     /db_xref="HGNC:HGNC:4065"
                     /db_xref="MIM:606800"
ORIGIN      
        1 mgvrhppcsh rllavcalvs lataallghi llhdfllvpr elsgsspvle ethpahqqga
       61 srpgprdaqa hpgrpravpt qcdvppnsrf dcapdkaitq eqceargccy ipakqglqga
      121 qmgqpwcffp psypsyklen lsssemgyta tltrttptff pkdiltlrld vmmetenrlh
      181 ftikdpanrr yevpletphv hsrapsplys vefseepfgv ivrrqldgrv llnttvaplf
      241 fadqflqlst slpsqyitgl aehlsplmls tswtritlwn rdlaptpgan lygshpfyla
      301 ledggsahgv fllnsnamdv vlqpspalsw rstggildvy iflgpepksv vqqyldvvgy
      361 pfmppywglg fhlcrwgyss taitrqvven mtrahfpldv qwndldymds rrdftfnkdg
      421 frdfpamvqe lhqggrrymm ivdpaisssg pagsyrpyde glrrgvfitn etgqpligkv
      481 wpgstafpdf tnptalawwe dmvaefhdqv pfdgmwidmn epsnfirgse dgcpnnelen
      541 ppyvpgvvgg tlqaaticas shqflsthyn lhnlygltea iashralvka rgtrpfvisr
      601 stfaghgrya ghwtgdvwss weqlassvpe ilqfnllgvp lvgadvcgfl gntseelcvr
      661 wtqlgafypf mrnhnsllsl pqepysfsep aqqamrkalt lryallphly tlfhqahvag
      721 etvarplfle fpkdsstwtv dhqllwgeal litpvlqagk aevtgyfplg twydlqtvpv
      781 ealgslpppp aaprepaihs egqwvtlpap ldtinvhlra gyiiplqgpg ltttesrqqp
      841 malavaltkg geargelfwd dgeslevler gaytqvifla rnntivnelv rvtsegaglq
      901 lqkvtvlgva tapqqvlsng vpvsnftysp dtkvldicvs llmgeqflvs wc
//
LOCUS       NP_001411265             225 aa            linear   PRI 21-NOV-2025
DEFINITION  protein cholesin isoform e [Homo sapiens].
ACCESSION   NP_001411265 XP_016868209 XP_054215195
VERSION     NP_001411265.1
DBSOURCE    REFSEQ: accession NM_001424336.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Ryk,A., Marcinkiewicz,A., Chrzanowski,J., Michalak,A.M., Drozdz,I.,
            Burzynski,J., Krejca,M. and Fendler,W.
  TITLE     Cholesin receptor signalling is active in cardiovascular
            system-associated adipose tissue and correlates with SGLT2i
            treatment in patients with diabetes
  JOURNAL   Cardiovasc Diabetol 23 (1), 211 (2024)
   PUBMED   38902687
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Hu,X., Chen,F., Jia,L., Long,A., Peng,Y., Li,X., Huang,J., Wei,X.,
            Fang,X., Gao,Z., Zhang,M., Liu,X., Chen,Y.G., Wang,Y., Zhang,H. and
            Wang,Y.
  TITLE     A gut-derived hormone regulates cholesterol metabolism
  JOURNAL   Cell 187 (7), 1685-1700 (2024)
   PUBMED   38503280
  REMARK    GeneRIF: A gut-derived hormone regulates cholesterol metabolism.
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 225)
  AUTHORS   Willer,C.J., Schmidt,E.M., Sengupta,S., Peloso,G.M., Gustafsson,S.,
            Kanoni,S., Ganna,A., Chen,J., Buchkovich,M.L., Mora,S.,
            Beckmann,J.S., Bragg-Gresham,J.L., Chang,H.Y., Demirkan,A., Den
            Hertog,H.M., Do,R., Donnelly,L.A., Ehret,G.B., Esko,T.,
            Feitosa,M.F., Ferreira,T., Fischer,K., Fontanillas,P., Fraser,R.M.,
            Freitag,D.F., Gurdasani,D., Heikkila,K., Hypponen,E., Isaacs,A.,
            Jackson,A.U., Johansson,A., Johnson,T., Kaakinen,M., Kettunen,J.,
            Kleber,M.E., Li,X., Luan,J., Lyytikainen,L.P., Magnusson,P.K.E.,
            Mangino,M., Mihailov,E., Montasser,M.E., Muller-Nurasyid,M.,
            Nolte,I.M., O'Connell,J.R., Palmer,C.D., Perola,M., Petersen,A.K.,
            Sanna,S., Saxena,R., Service,S.K., Shah,S., Shungin,D., Sidore,C.,
            Song,C., Strawbridge,R.J., Surakka,I., Tanaka,T., Teslovich,T.M.,
            Thorleifsson,G., Van den Herik,E.G., Voight,B.F., Volcik,K.A.,
            Waite,L.L., Wong,A., Wu,Y., Zhang,W., Absher,D., Asiki,G.,
            Barroso,I., Been,L.F., Bolton,J.L., Bonnycastle,L.L., Brambilla,P.,
            Burnett,M.S., Cesana,G., Dimitriou,M., Doney,A.S.F., Doring,A.,
            Elliott,P., Epstein,S.E., Ingi Eyjolfsson,G., Gigante,B.,
            Goodarzi,M.O., Grallert,H., Gravito,M.L., Groves,C.J., Hallmans,G.,
            Hartikainen,A.L., Hayward,C., Hernandez,D., Hicks,A.A., Holm,H.,
            Hung,Y.J., Illig,T., Jones,M.R., Kaleebu,P., Kastelein,J.J.P.,
            Khaw,K.T., Kim,E., Klopp,N., Komulainen,P., Kumari,M.,
            Langenberg,C., Lehtimaki,T., Lin,S.Y., Lindstrom,J., Loos,R.J.F.,
            Mach,F., McArdle,W.L., Meisinger,C., Mitchell,B.D., Muller,G.,
            Nagaraja,R., Narisu,N., Nieminen,T.V.M., Nsubuga,R.N., Olafsson,I.,
            Ong,K.K., Palotie,A., Papamarkou,T., Pomilla,C., Pouta,A.,
            Rader,D.J., Reilly,M.P., Ridker,P.M., Rivadeneira,F., Rudan,I.,
            Ruokonen,A., Samani,N., Scharnagl,H., Seeley,J., Silander,K.,
            Stancakova,A., Stirrups,K., Swift,A.J., Tiret,L.,
            Uitterlinden,A.G., van Pelt,L.J., Vedantam,S., Wainwright,N.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilsgaard,T., Wilson,J.F.,
            Young,E.H., Zhao,J.H., Adair,L.S., Arveiler,D., Assimes,T.L.,
            Bandinelli,S., Bennett,F., Bochud,M., Boehm,B.O., Boomsma,D.I.,
            Borecki,I.B., Bornstein,S.R., Bovet,P., Burnier,M., Campbell,H.,
            Chakravarti,A., Chambers,J.C., Chen,Y.I., Collins,F.S.,
            Cooper,R.S., Danesh,J., Dedoussis,G., de Faire,U., Feranil,A.B.,
            Ferrieres,J., Ferrucci,L., Freimer,N.B., Gieger,C., Groop,L.C.,
            Gudnason,V., Gyllensten,U., Hamsten,A., Harris,T.B., Hingorani,A.,
            Hirschhorn,J.N., Hofman,A., Hovingh,G.K., Hsiung,C.A.,
            Humphries,S.E., Hunt,S.C., Hveem,K., Iribarren,C., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kaprio,J., Kesaniemi,A., Kivimaki,M.,
            Kooner,J.S., Koudstaal,P.J., Krauss,R.M., Kuh,D., Kuusisto,J.,
            Kyvik,K.O., Laakso,M., Lakka,T.A., Lind,L., Lindgren,C.M.,
            Martin,N.G., Marz,W., McCarthy,M.I., McKenzie,C.A., Meneton,P.,
            Metspalu,A., Moilanen,L., Morris,A.D., Munroe,P.B., Njolstad,I.,
            Pedersen,N.L., Power,C., Pramstaller,P.P., Price,J.F., Psaty,B.M.,
            Quertermous,T., Rauramaa,R., Saleheen,D., Salomaa,V.,
            Sanghera,D.K., Saramies,J., Schwarz,P.E.H., Sheu,W.H.,
            Shuldiner,A.R., Siegbahn,A., Spector,T.D., Stefansson,K.,
            Strachan,D.P., Tayo,B.O., Tremoli,E., Tuomilehto,J., Uusitupa,M.,
            van Duijn,C.M., Vollenweider,P., Wallentin,L., Wareham,N.J.,
            Whitfield,J.B., Wolffenbuttel,B.H.R., Ordovas,J.M., Boerwinkle,E.,
            Palmer,C.N.A., Thorsteinsdottir,U., Chasman,D.I., Rotter,J.I.,
            Franks,P.W., Ripatti,S., Cupples,L.A., Sandhu,M.S., Rich,S.S.,
            Boehnke,M., Deloukas,P., Kathiresan,S., Mohlke,K.L., Ingelsson,E.
            and Abecasis,G.R.
  CONSRTM   Global Lipids Genetics Consortium
  TITLE     Discovery and refinement of loci associated with lipid levels
  JOURNAL   Nat Genet 45 (11), 1274-1283 (2013)
   PUBMED   24097068
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Yashin,A.I., Wu,D., Arbeev,K.G. and Ukraintseva,S.V.
  TITLE     Joint influence of small-effect genetic variants on human longevity
  JOURNAL   Aging (Albany NY) 2 (9), 612-620 (2010)
   PUBMED   20834067
REFERENCE   9  (residues 1 to 225)
  AUTHORS   Satoh,J., Obayashi,S., Misawa,T., Sumiyoshi,K., Oosumi,K. and
            Tabunoki,H.
  TITLE     Protein microarray analysis identifies human cellular prion protein
            interactors
  JOURNAL   Neuropathol Appl Neurobiol 35 (1), 16-35 (2009)
   PUBMED   18482256
REFERENCE   10 (residues 1 to 225)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CP068271.2.
            
            On or before Sep 21, 2023 this sequence version replaced
            XP_016868209.1, XP_054215195.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..225
                     /product="protein cholesin isoform e"
                     /note="uncharacterized protein C7orf50; protein cholesin"
                     /calculated_mol_wt=25056
     Region          1..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Region          104..165
                     /region_name="WKF"
                     /note="WKF domain; pfam10180"
                     /db_xref="CDD:462982"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     CDS             1..225
                     /gene="CHLSN"
                     /gene_synonym="C7orf50; YCR016W"
                     /coded_by="NM_001424336.1:42..719"
                     /note="isoform e is encoded by transcript variant 29"
                     /db_xref="GeneID:84310"
                     /db_xref="HGNC:HGNC:22421"
                     /db_xref="MIM:621174"
ORIGIN      
        1 makqkrkvpe vtekknkklk kasaegpllg peaapsgega gskgeavlrp gldaepelsp
       61 eeqrvlerkl kkerkkeerq rlreaglvaq hpparrsgae laldylcrwa qkhknwrfqk
      121 trqtwlllhm ydsdkvpdeh fstllayleg lqgrareltv qkaealmrel deegsdpplp
      181 graqrirqdt cavdpaamlw gspaarrgah vegnpgprnr gqast
//
LOCUS       NP_001427449             219 aa            linear   PRI 21-NOV-2025
DEFINITION  beta-sarcoglycan isoform 3 [Homo sapiens].
ACCESSION   NP_001427449 XP_047272031 XP_054206690
VERSION     NP_001427449.1
DBSOURCE    REFSEQ: accession NM_001440520.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Sanga,S., Chakraborty,S., Bardhan,M., Polavarapu,K., Kumar,V.P.,
            Bhattacharya,C., Nashi,S., Vengalil,S., Geetha,T.S., Ramprasad,V.,
            Nalini,A., Basu,A. and Acharya,M.
  TITLE     Identification of a shared, common haplotype segregating with an
            SGCB c.544 T > G mutation in Indian patients affected with
            sarcoglycanopathy
  JOURNAL   Sci Rep 13 (1), 15095 (2023)
   PUBMED   37699968
  REMARK    GeneRIF: Identification of a shared, common haplotype segregating
            with an SGCB c.544 T > G mutation in Indian patients affected with
            sarcoglycanopathy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Li,C., Wilborn,J., Pittman,S., Daw,J., Alonso-Perez,J.,
            Diaz-Manera,J., Weihl,C.C. and Haller,G.
  TITLE     Comprehensive functional characterization of SGCB coding variants
            predicts pathogenicity in limb-girdle muscular dystrophy type R4/2E
  JOURNAL   J Clin Invest 133 (12), e168156 (2023)
   PUBMED   37317968
  REMARK    GeneRIF: Comprehensive functional characterization of SGCB coding
            variants predicts pathogenicity in limb-girdle muscular dystrophy
            type R4/2E.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Bardhan,M., Anjanappa,R.M., Polavarapu,K., Preethish-Kumar,V.,
            Vengalil,S., Nashi,S., Sanga,S., Padmanabh,H., Valasani,R.K.,
            Nishadham,V., Keerthipriya,M., Geetha,T.S., Ramprasad,V.,
            Arunachal,G., Thomas,P.T., Acharya,M. and Nalini,A.
  TITLE     Clinical, genetic profile and disease progression of
            sarcoglycanopathies in a large cohort from India: high prevalence
            of SGCB c.544A > C
  JOURNAL   Neurogenetics 23 (3), 187-202 (2022)
   PUBMED   35416532
  REMARK    GeneRIF: Clinical, genetic profile and disease progression of
            sarcoglycanopathies in a large cohort from India: high prevalence
            of SGCB c.544A > C.
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Alavi,A., Esmaeili,S., Nilipour,Y., Nafissi,S., Tonekaboni,S.H.,
            Zamani,G., Ashrafi,M.R., Kahrizi,K., Najmabadi,H. and Jazayeri,F.
  TITLE     LGMD2E is the most common type of sarcoglycanopathies in the
            Iranian population
  JOURNAL   J Neurogenet 31 (3), 161-169 (2017)
   PUBMED   28687063
  REMARK    GeneRIF: This study demonstrated that LGMD2E is the most common
            type of sarcoglycanopathies in the Iranian population.
REFERENCE   6  (residues 1 to 219)
  AUTHORS   Bonnemann,C.G., Passos-Bueno,M.R., McNally,E.M., Vainzof,M., de Sa
            Moreira,E., Marie,S.K., Pavanello,R.C., Noguchi,S., Ozawa,E.,
            Zatz,M. and Kunkel,L.M.
  TITLE     Genomic screening for beta-sarcoglycan gene mutations: missense
            mutations may cause severe limb-girdle muscular dystrophy type 2E
            (LGMD 2E)
  JOURNAL   Hum Mol Genet 5 (12), 1953-1961 (1996)
   PUBMED   8968749
REFERENCE   7  (residues 1 to 219)
  AUTHORS   Bonnemann,C.G., Modi,R., Noguchi,S., Mizuno,Y., Yoshida,M.,
            Gussoni,E., McNally,E.M., Duggan,D.J., Angelini,C. and Hoffman,E.P.
  TITLE     Beta-sarcoglycan (A3b) mutations cause autosomal recessive muscular
            dystrophy with loss of the sarcoglycan complex
  JOURNAL   Nat Genet 11 (3), 266-273 (1995)
   PUBMED   7581449
  REMARK    Erratum:[Nat Genet 1996 Jan;12(1):110]
REFERENCE   8  (residues 1 to 219)
  AUTHORS   Lim,L.E., Duclos,F., Broux,O., Bourg,N., Sunada,Y., Allamand,V.,
            Meyer,J., Richard,I., Moomaw,C., Slaughter,C. et al.
  TITLE     Beta-sarcoglycan: characterization and role in limb-girdle muscular
            dystrophy linked to 4q12
  JOURNAL   Nat Genet 11 (3), 257-265 (1995)
   PUBMED   7581448
REFERENCE   9  (residues 1 to 219)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   10 (residues 1 to 219)
  AUTHORS   Yoshida,M. and Ozawa,E.
  TITLE     Glycoprotein complex anchoring dystrophin to sarcolemma
  JOURNAL   J Biochem 108 (5), 748-752 (1990)
   PUBMED   2081733
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093858.2.
            
            On or before May 21, 2025 this sequence version replaced
            XP_047272031.1, XP_054206690.1.
            
            Summary: This gene encodes a member of the sarcoglycan family.
            Sarcoglycans are transmembrane components in the
            dystrophin-glycoprotein complex which help stabilize the muscle
            fiber membranes and link the muscle cytoskeleton to the
            extracellular matrix. Mutations in this gene have been associated
            with limb-girdle muscular dystrophy.[provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.25229.1,
                                           SRR11853561.22168.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..219
                     /product="beta-sarcoglycan isoform 3"
                     /note="beta-sarcoglycan; beta-sarcoglycan(43kD
                     dystrophin-associated glycoprotein); limb girdle muscular
                     dystrophy 2E (non-linked families); 43DAG; beta-SG; 43 kDa
                     dystrophin-associated glycoprotein; sarcoglycan, beta
                     (43kDa dystrophin-associated glycoprotein)"
                     /calculated_mol_wt=23926
     Region          1..204
                     /region_name="Sarcoglycan_1"
                     /note="Sarcoglycan complex subunit protein; pfam04790"
                     /db_xref="CDD:461428"
     CDS             1..219
                     /gene="SGCB"
                     /gene_synonym="A3b; LGMD2E; LGMDR4; SGC"
                     /coded_by="NM_001440520.1:448..1107"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:6443"
                     /db_xref="HGNC:HGNC:10806"
                     /db_xref="MIM:600900"
ORIGIN      
        1 mefhesgllr fkqvsdmgvi hplykstvgg rrnenlvitg nnqpivfqqg ttklsvennk
       61 tsitsdigmq ffdprtqnil fstdyethef hlpsgvksln vqkasterit snatsdlnik
      121 vdgraivrgn egvfimgkti efhmggnmel kaensiilng svmvsttrlp ssssgdqlgs
      181 gdwvryklcm cadgtlfkvq vtsqnmgcqi sdnpcgnth
//
LOCUS       NP_001427582             771 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 3 isoform 2 [Homo sapiens].
ACCESSION   NP_001427582 XP_005278336 XP_054177055 XP_054185659 XP_054186154
            XP_054186451 XP_054186703 XP_054186934 XP_054187215 XP_054187490
            XP_054189530 XP_054189632
VERSION     NP_001427582.1
DBSOURCE    REFSEQ: accession NM_001440653.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 771)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 771)
  AUTHORS   Ghashghaei,M., Liu,Y., Ettles,J., Bombaci,G., Ramkumar,N., Liu,Z.,
            Escano,L., Miko,S.S., Kim,Y., Waldron,J.A., Do,K., MacPherson,K.,
            Yuen,K.A., Taibi,T., Yue,M., Arsalan,A., Jin,Z., Edin,G.,
            Karsan,A., Morin,G.B., Kuchenbauer,F., Perna,F., Bushell,M. and
            Vu,L.P.
  TITLE     Translation efficiency driven by CNOT3 subunit of the CCR4-NOT
            complex promotes leukemogenesis
  JOURNAL   Nat Commun 15 (1), 2340 (2024)
   PUBMED   38491013
  REMARK    GeneRIF: Translation efficiency driven by CNOT3 subunit of the
            CCR4-NOT complex promotes leukemogenesis.
            Erratum:[Nat Commun. 2024 Oct 7;15(1):8674. doi:
            10.1038/s41467-024-53071-1. PMID: 39375334]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 771)
  AUTHORS   Burgess,H.M., Grande,R., Riccio,S., Dinesh,I., Winkler,G.S.,
            Depledge,D.P. and Mohr,I.
  TITLE     CCR4-NOT differentially controls host versus virus poly(a)-tail
            length and regulates HCMV infection
  JOURNAL   EMBO Rep 24 (12), e56327 (2023)
   PUBMED   37846490
  REMARK    GeneRIF: CCR4-NOT differentially controls host versus virus
            poly(a)-tail length and regulates HCMV infection.
REFERENCE   4  (residues 1 to 771)
  AUTHORS   Zhao,P., Meng,Q., Wan,C., Lei,T., Zhang,L., Zhang,X., Tan,L.,
            Zhu,H. and He,X.
  TITLE     Clinical features of CNOT3-associated neurodevelopmental disorder
            in three Chinese patients
  JOURNAL   Neurogenetics 24 (2), 129-136 (2023)
   PUBMED   36802310
  REMARK    GeneRIF: Clinical features of CNOT3-associated neurodevelopmental
            disorder in three Chinese patients.
REFERENCE   5  (residues 1 to 771)
  AUTHORS   McLenachan,S., Zhang,D., Grainok,J., Zhang,X., Huang,Z., Chen,S.C.,
            Zaw,K., Lima,A., Jennings,L., Roshandel,D., Moon,S.Y., Heath
            Jeffery,R.C., Attia,M.S., Thompson,J.A., Lamey,T.M., McLaren,T.L.,
            De Roach,J., Fletcher,S. and Chen,F.K.
  TITLE     Determinants of Disease Penetrance in PRPF31-Associated Retinopathy
  JOURNAL   Genes (Basel) 12 (10), 1542 (2021)
   PUBMED   34680937
  REMARK    GeneRIF: Determinants of Disease Penetrance in PRPF31-Associated
            Retinopathy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 771)
  AUTHORS   Yin,X., Warner,D.R., Roberts,E.A., Pisano,M.M. and Greene,R.M.
  TITLE     Identification of novel CBP interacting proteins in embryonic
            orofacial tissue
  JOURNAL   Biochem Biophys Res Commun 329 (3), 1010-1017 (2005)
   PUBMED   15752756
REFERENCE   7  (residues 1 to 771)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 771)
  AUTHORS   Aoki,T., Okada,N., Wakamatsu,T. and Tamura,T.A.
  TITLE     TBP-interacting protein 120B, which is induced in relation to
            myogenesis, binds to NOT3
  JOURNAL   Biochem Biophys Res Commun 296 (5), 1097-1103 (2002)
   PUBMED   12207886
  REMARK    GeneRIF: TBP-interacting protein 120B binds to NOT3
REFERENCE   9  (residues 1 to 771)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
REFERENCE   10 (residues 1 to 771)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC245052.3.
            
            On or before May 23, 2025 this sequence version replaced
            XP_054186154.1, XP_054189632.1, XP_054189530.1, XP_054187215.1,
            XP_054186451.1, XP_054187490.1, XP_005278336.1, XP_054185659.1,
            XP_054186703.1, XP_054186934.1, XP_054177055.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853565.15841.1,
                                           SRR18074968.4244221.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..771
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..771
                     /product="CCR4-NOT transcription complex subunit 3 isoform
                     2"
                     /note="NOT3 (negative regulator of transcription 3, yeast)
                     homolog; CCR4-associated factor 3; leukocyte receptor
                     cluster member 2"
                     /calculated_mol_wt=83683
     Region          3..230
                     /region_name="Not3"
                     /note="Not1 N-terminal domain, CCR4-Not complex component;
                     pfam04065"
                     /db_xref="CDD:461155"
     Region          <289..660
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          621..763
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..771
                     /gene="CNOT3"
                     /gene_synonym="IDDSADF; LENG2; NOT3; NOT3H"
                     /coded_by="NM_001440653.1:283..2598"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:4849"
                     /db_xref="HGNC:HGNC:7879"
                     /db_xref="MIM:604910"
ORIGIN      
        1 madkrklqge idrclkkvse gveqfediwq klhnaananq kekyeadlkk eikklqrlrd
       61 qiktwvasne ikdkrqlidn rklietqmer fkvveretkt kayskeglgl aqkvdpaqke
      121 keevgqwltn tidtlnmqvd qfesevesls vqtrkkkgdk dqkqdriegl krhiekhryh
      181 vrmletilrm ldndsilvda irkikddvey yvdssqdpdf eeneflyddl dledipqalv
      241 atsppshshm edeifnqsss tptsttsssp ippspanctt enseddkkrg rstdsevsqs
      301 pakngskpvh snqhpqspav pptypsgppp aasalsttpg nngvpapaap psalgpkasp
      361 apshnsgtpa pyaqavappa psgpsttqpr ppsvqpsggg gggsggggss sssnssaggg
      421 agkqngatsy ssvvadspae valsssggnn assqalgpps gphnpppsts kepsaaaptg
      481 aggvapgsgn nsggpsllvp lpvnppsspt psfsdakaag allngppqfs tapeikapep
      541 lsslksmaer aaissgiedp vptlhlterd iilsstsapp asaqpplqls evniplslgv
      601 cplgpvpltk eqlyqqamee aawhhmphps dserirqylp rnpcptppyh hqmppphsdt
      661 vefyqrlste tlffifyyle gtkaqylaak alkkqswrfh tkymmwfqrh eepktitdef
      721 eqipdhllvh sltafspgqg tyiyfdyekw gqrkkegftf eyryledrdl q
//
LOCUS       NP_001392221             404 aa            linear   PRI 21-NOV-2025
DEFINITION  F-box/LRR-repeat protein 14 isoform 3 [Homo sapiens].
ACCESSION   NP_001392221 XP_016874364
VERSION     NP_001392221.1
DBSOURCE    REFSEQ: accession NM_001405292.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Pitts,S., Liu,H., Ibrahim,A., Garg,A., Felgueira,C.M., Begum,A.,
            Fan,W., Teh,S., Low,J.Y., Ford,B., Schneider,D.A., Hay,R. and
            Laiho,M.
  TITLE     Identification of an E3 ligase that targets the catalytic subunit
            of RNA Polymerase I upon transcription stress
  JOURNAL   J Biol Chem 298 (12), 102690 (2022)
   PUBMED   36372232
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Cui,Y.H., Kang,J.H., Suh,Y., Zhao,Y., Yi,J.M., Bae,I.H., Lee,H.J.,
            Park,D.W., Kim,M.J. and Lee,S.J.
  TITLE     Loss of FBXL14 promotes mesenchymal shift and radioresistance of
            non-small cell lung cancer by TWIST1 stabilization
  JOURNAL   Signal Transduct Target Ther 6 (1), 272 (2021)
   PUBMED   34285182
  REMARK    GeneRIF: Loss of FBXL14 promotes mesenchymal shift and
            radioresistance of non-small cell lung cancer by TWIST1
            stabilization.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Hauri,S., Comoglio,F., Seimiya,M., Gerstung,M., Glatter,T.,
            Hansen,K., Aebersold,R., Paro,R., Gstaiger,M. and Beisel,C.
  TITLE     A High-Density Map for Navigating the Human Polycomb Complexome
  JOURNAL   Cell Rep 17 (2), 583-595 (2016)
   PUBMED   27705803
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Zheng,H., Shen,M., Zha,Y.L., Li,W., Wei,Y., Blanco,M.A., Ren,G.,
            Zhou,T., Storz,P., Wang,H.Y. and Kang,Y.
  TITLE     PKD1 phosphorylation-dependent degradation of SNAIL by SCF-FBXO11
            regulates epithelial-mesenchymal transition and metastasis
  JOURNAL   Cancer Cell 26 (3), 358-373 (2014)
   PUBMED   25203322
REFERENCE   8  (residues 1 to 404)
  AUTHORS   Vinas-Castells,R., Beltran,M., Valls,G., Gomez,I., Garcia,J.M.,
            Montserrat-Sentis,B., Baulida,J., Bonilla,F., de Herreros,A.G. and
            Diaz,V.M.
  TITLE     The hypoxia-controlled FBXL14 ubiquitin ligase targets SNAIL1 for
            proteasome degradation
  JOURNAL   J Biol Chem 285 (6), 3794-3805 (2010)
   PUBMED   19955572
  REMARK    GeneRIF: Data show that Twist1 small interfering RNA prevents
            hypoxia-induced Fbxl14 down-regulation and SNAIL1 stabilization.
REFERENCE   9  (residues 1 to 404)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   10 (residues 1 to 404)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005182.2 and AC004671.1.
            
            On Apr 21, 2022 this sequence version replaced XP_016874364.1.
            
            Summary: Members of the F-box protein family, such as FBXL14, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853564.6158.1,
                                           SRR14038192.1634647.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..404
                     /product="F-box/LRR-repeat protein 14 isoform 3"
                     /note="F-box/LRR-repeat protein 14"
                     /calculated_mol_wt=44139
     Region          6..46
                     /region_name="F-box_FBXL14"
                     /note="F-box domain found in F-box/LRR-repeat protein 14
                     (FBXL14) and similar proteins; cd22125"
                     /db_xref="CDD:438897"
     Site            order(8,12,15..16,19..20,24,26..27,31..33,35)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438897"
     Region          90..296
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          92..118
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          119..142
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          145..170
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          171..203
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          204..229
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          228..404
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          230..254
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          255..280
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          281..306
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          307..331
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          332..357
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          358..382
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..404
                     /gene="FBXL14"
                     /gene_synonym="Fbl14"
                     /coded_by="NM_001405292.1:777..1991"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:144699"
                     /db_xref="HGNC:HGNC:28624"
                     /db_xref="MIM:609081"
ORIGIN      
        1 methisclfp ellamifgyl dvrdkgraaq vctawrdaay hksvwrgvea klhlrranps
       61 lfpslqargi rrvqilslrr slsyviqgma nieslnlsgc ynltdnglgh afvqeigslr
      121 alnlslckqi tdsslgriaq ylkglevlel ggcsnitntg llliawglqr lkslnlrscr
      181 hlsdvgighl agmtrsaaeg clgleqltlq dcqkltdlsl khisrgltgl rllnlsfcgg
      241 isdagllhls hmgslrslnl rscdnisdtg imhlamgslr lsgldvsfcd kvgdqslayi
      301 aqgldglksl slcschisdd ginrmvrqmh glrtlnigqc vritdkglel iaehlsqltg
      361 idlygctrit krgleritql pclkeargdf splftvrtrg ssrr
//
LOCUS       NP_001427284             736 aa            linear   PRI 21-NOV-2025
DEFINITION  general transcription and DNA repair factor IIH helicase subunit
            XPD isoform 3 [Homo sapiens].
ACCESSION   NP_001427284
VERSION     NP_001427284.1
DBSOURCE    REFSEQ: accession NM_001440355.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Barbour,J.A., Ou,T., Yang,H., Fang,H., Yue,N.C., Zhu,X.,
            Wong-Brown,M.W., Wong,Y.T., Bowden,N.A., Wu,S. and Wong,J.W.H.
  TITLE     ERCC2 mutations alter the genomic distribution pattern of somatic
            mutations and are independently prognostic in bladder cancer
  JOURNAL   Cell Genom 4 (8), 100627 (2024)
   PUBMED   39096913
  REMARK    GeneRIF: ERCC2 mutations alter the genomic distribution pattern of
            somatic mutations and are independently prognostic in bladder
            cancer.
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Zeng,W., Xu,W. and Long,W.
  TITLE     The association between XPD rs13181 and rs1799793 polymorphism and
            oral cancer risk: evidence from a meta-analysis
  JOURNAL   BMC Cancer 24 (1), 738 (2024)
   PUBMED   38879503
  REMARK    GeneRIF: The association between XPD rs13181 and rs1799793
            polymorphism and oral cancer risk: evidence from a meta-analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Gudur,A.K., Kale,S.R., Gudur,R.A., Bhosale,S.J. and Datkhile,K.D.
  TITLE     Genetic Polymorphisms of XPC, XPD, XPG Genes and their Association
            with Radiotherapy Induced Toxicity among Head and Neck Cancer
            Patients: A Hospital Based Study from Maharashtra
  JOURNAL   Asian Pac J Cancer Prev 25 (1), 191-199 (2024)
   PUBMED   38285784
  REMARK    GeneRIF: Genetic Polymorphisms of XPC, XPD, XPG Genes and their
            Association with Radiotherapy Induced Toxicity among Head and Neck
            Cancer Patients: A Hospital Based Study from Maharashtra.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 736)
  AUTHORS   Fu,I., Geacintov,N.E. and Broyde,S.
  TITLE     Differing structures and dynamics of two photolesions portray
            verification differences by the human XPD helicase
  JOURNAL   Nucleic Acids Res 51 (22), 12261-12274 (2023)
   PUBMED   37933861
  REMARK    GeneRIF: Differing structures and dynamics of two photolesions
            portray verification differences by the human XPD helicase.
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Sun,G.F. and Ding,H.
  TITLE     NOP2-mediated m5C methylation of XPD is associated with
            hepatocellular carcinoma progression
  JOURNAL   Neoplasma 70 (3), 340-349 (2023)
   PUBMED   37498063
  REMARK    GeneRIF: NOP2-mediated m5C methylation of XPD is associated with
            hepatocellular carcinoma progression.
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Flejter,W.L., McDaniel,L.D., Johns,D., Friedberg,E.C. and
            Schultz,R.A.
  TITLE     Correction of xeroderma pigmentosum complementation group D mutant
            cell phenotypes by chromosome and gene transfer: involvement of the
            human ERCC2 DNA repair gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 261-265 (1992)
   PUBMED   1729695
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Weber,C.A., Salazar,E.P., Stewart,S.A. and Thompson,L.H.
  TITLE     ERCC2: cDNA cloning and molecular characterization of a human
            nucleotide excision repair gene with high homology to yeast RAD3
  JOURNAL   EMBO J 9 (5), 1437-1447 (1990)
   PUBMED   2184031
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from L47234.2.
            
            Summary: The nucleotide excision repair pathway is a mechanism to
            repair damage to DNA. The protein encoded by this gene is involved
            in transcription-coupled nucleotide excision repair and is an
            integral member of the basal transcription factor BTF2/TFIIH
            complex. The gene product has ATP-dependent DNA helicase activity
            and belongs to the RAD3/XPD subfamily of helicases. Defects in this
            gene can result in three different disorders, the cancer-prone
            syndrome xeroderma pigmentosum complementation group D,
            trichothiodystrophy, and Cockayne syndrome. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4417532.1,
                                           SRR14038195.2680125.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..736
                     /product="general transcription and DNA repair factor IIH
                     helicase subunit XPD isoform 3"
                     /EC_number="5.6.2.3"
                     /note="xeroderma pigmentosum complementary group D; TFIIH
                     basal transcription factor complex helicase XPD subunit;
                     TFIIH subunit XPD; DNA 5'-3' helicase XPD; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 2; xeroderma pigmentosum group
                     D-complementing protein; TFIIH basal transcription factor
                     complex 80 kDa subunit; BTF2 p80; TFIIH p80; TFIIH 80 kDa
                     subunit; DNA excision repair protein ERCC-2; DNA repair
                     protein complementing XP-D cells; basic transcription
                     factor 2 80 kDa subunit; excision repair
                     cross-complementation group 2; general transcription and
                     DNA repair factor IIH helicase subunit XPD"
                     /calculated_mol_wt=83818
     Region          1..684
                     /region_name="rad3"
                     /note="DNA repair helicase (rad3); TIGR00604"
                     /db_xref="CDD:273169"
     CDS             1..736
                     /gene="ERCC2"
                     /gene_synonym="COFS2; CXPD; EM9; TFIIH; TTD; TTD1; XPD"
                     /coded_by="NM_001440355.1:171..2381"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:2068"
                     /db_xref="HGNC:HGNC:3434"
                     /db_xref="MIM:126340"
ORIGIN      
        1 mrelkrtlda kghgvlemps gtgktvslla limayqrayp levtkliycs rtvpeiekvi
       61 eelrkllnfy ekqegeklpf lglalssrkn lcihpevtpl rfgkdvdgkc hsltasyvra
      121 qyqhdtslph crfyeefdah grevplpagi ynlddlkalg rrqgwcpyfl arysilhanv
      181 vvysyhylld pkiadlvske larkavvvfd eahnidnvci dsmsvnltrr tldrcqgnle
      241 tlqktvlrik etdeqrlrde yrrlveglre asaaretdah lanpvlpdev lqeavpgsir
      301 taehflgflr rlleyvkwrl rvqhvvqesp paflsglaqr vciqrkplrf caerlrsllh
      361 tleitdladf spltllanfa tlvstyakgf tiiiepfddr tptianpilh fscmdaslai
      421 kpvferfqsv iitsgtlspl diypkildfh pvtmatftmt larvclcpmi igrgndqvai
      481 sskfetredi avirnygnll lemsavvpdg ivafftsyqy mestvaswye qgileniqrn
      541 kllfietqdg aetsvaleky qeacengrga illsvargkv segidfvhhy gravimfgvp
      601 yvytqsrilk arleylrdqf qirendfltf damrhaaqcv grairgktdy glmvfadkrf
      661 argdkrgklp rwiqehltda nlnltvdegv qvakyflrqm aqpfhredql glsllsleql
      721 eseetlkrie qiaqql
//
LOCUS       NP_001428150             476 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 2 [Homo sapiens].
ACCESSION   NP_001428150
VERSION     NP_001428150.1
DBSOURCE    REFSEQ: accession NM_001441221.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1975747.1,
                                           SRR14038194.3684918.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..476
                     /product="calcium uptake protein 1, mitochondrial isoform
                     2"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=50585
     transit_peptide 1..33
                     /note="Mitochondrion. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:26387864; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
                     /calculated_mol_wt=3784
     mat_peptide     34..476
                     /product="Calcium uptake protein 1, mitochondrial.
                     /id=PRO_0000322990"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
                     /calculated_mol_wt=50585
     Region          68..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          99..110
                     /region_name="Polybasic region.
                     /evidence=ECO:0000269|PubMed:27099988"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCX5; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          126..129
                     /region_name="K/R-ring.
                     /evidence=ECO:0000269|PubMed:32494073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          222..441
                     /region_name="EFh_MICU1"
                     /note="EF-hand, calcium binding motif, found in calcium
                     uptake protein 1, mitochondrial (MICU1) and similar
                     proteins; cd16173"
                     /db_xref="CDD:320081"
     Region          222..251
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Site            order(224,376,379,382..383,385,403)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:320081"
     Site            order(231,233,235,242,421,423,425,432)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320081"
     Region          259..263
                     /region_name="K/R-ring.
                     /evidence=ECO:0000269|PubMed:32494073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          277..307
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          375..404
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          412..441
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          455..465
                     /region_name="C-helix region.
                     /evidence=ECO:0000269|PubMed:24514027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Site            455
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:27642082; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
     CDS             1..476
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001441221.1:206..1636"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mfrlnslsal aelavgsrwy hggsqpiqir rrlmmvaflg asavtastgl lwkrahaesp
       61 pcvdnlksdi gdkgknkdeg dvcnhekkta dlaphpeekk kkrsgfrdrk vmeyenrira
      121 ystpdkifry fatlkvisep geaevfmtpe dfvrsitpne kqpehlgldq yiikrfdgkk
      181 isqerekfad egsifytlge cglisfsdyi flttvlstpq rnfeiafkmf dlngdgevdm
      241 eefeqvqsii rsqtsmgmrh rdrpttgntl ksglcsaltt yffgadlkgk ltiknflefq
      301 rklqhdvlkl eferhdpvdg riterqfggm llaysgvqsk kltamqrqlk khfkegkglt
      361 fqevenfftf lknindvdta lsfyhmagas ldkvtmqqva rtvakvelsd hvcdvvfalf
      421 dcdgngelsn kefvsimkqr lmrglekpkd mgftrlmqam wkcaqetawd falpkq
//
LOCUS       NP_001411260             233 aa            linear   PRI 21-NOV-2025
DEFINITION  bcl-2-like protein 1 isoform Bcl-X(L) [Homo sapiens].
ACCESSION   NP_001411260
VERSION     NP_001411260.1
DBSOURCE    REFSEQ: accession NM_001424331.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Nguyen,T.T., Torrini,C., Shang,E., Shu,C., Mun,J.Y., Gao,Q.,
            Humala,N., Akman,H.O., Zhang,G., Westhoff,M.A., Karpel-Massler,G.,
            Bruce,J.N., Canoll,P. and Siegelin,M.D.
  TITLE     OGDH and Bcl-xL loss causes synthetic lethality in glioblastoma
  JOURNAL   JCI Insight 9 (8), e172565 (2024)
   PUBMED   38483541
  REMARK    GeneRIF: OGDH and Bcl-xL loss causes synthetic lethality in
            glioblastoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Li,S., Wang,Y., Chen,Y., Zhang,H., Shen,K. and Guan,H.
  TITLE     PTEN hinders the formation of scars by regulating the levels of
            proteins in the extracellular matrix and promoting the apoptosis of
            dermal fibroblasts through Bcl-xL
  JOURNAL   Arch Biochem Biophys 753, 109912 (2024)
   PUBMED   38325773
  REMARK    GeneRIF: PTEN hinders the formation of scars by regulating the
            levels of proteins in the extracellular matrix and promoting the
            apoptosis of dermal fibroblasts through Bcl-xL.
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Dou,Z., Lei,H., Su,W., Zhang,T., Chen,X., Yu,B., Zhen,X., Si,J.,
            Sun,C., Zhang,H. and Di,C.
  TITLE     Modification of BCLX pre-mRNA splicing has antitumor efficacy alone
            or in combination with radiotherapy in human glioblastoma cells
  JOURNAL   Cell Death Dis 15 (2), 160 (2024)
   PUBMED   38383492
  REMARK    GeneRIF: Modification of BCLX pre-mRNA splicing has antitumor
            efficacy alone or in combination with radiotherapy in human
            glioblastoma cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Yin,L., Hu,X., Pei,G., Tang,M., Zhou,Y., Zhang,H., Huang,M., Li,S.,
            Zhang,J., Citu,C., Zhao,Z., Debeb,B.G., Feng,X. and Chen,J.
  TITLE     Genome-wide CRISPR screen reveals the synthetic lethality between
            BCL2L1 inhibition and radiotherapy
  JOURNAL   Life Sci Alliance 7 (4), e202302353 (2024)
   PUBMED   38316463
  REMARK    GeneRIF: Genome-wide CRISPR screen reveals the synthetic lethality
            between BCL2L1 inhibition and radiotherapy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 233)
  AUTHORS   Broome,H.E., Dargan,C.M., Krajewski,S. and Reed,J.C.
  TITLE     Expression of Bcl-2, Bcl-x, and Bax after T cell activation and
            IL-2 withdrawal
  JOURNAL   J Immunol 155 (5), 2311-2317 (1995)
   PUBMED   7650367
REFERENCE   7  (residues 1 to 233)
  AUTHORS   Sedlak,T.W., Oltvai,Z.N., Yang,E., Wang,K., Boise,L.H.,
            Thompson,C.B. and Korsmeyer,S.J.
  TITLE     Multiple Bcl-2 family members demonstrate selective dimerizations
            with Bax
  JOURNAL   Proc Natl Acad Sci U S A 92 (17), 7834-7838 (1995)
   PUBMED   7644501
REFERENCE   8  (residues 1 to 233)
  AUTHORS   Jaattela,M., Benedict,M., Tewari,M., Shayman,J.A. and Dixit,V.M.
  TITLE     Bcl-x and Bcl-2 inhibit TNF and Fas-induced apoptosis and
            activation of phospholipase A2 in breast carcinoma cells
  JOURNAL   Oncogene 10 (12), 2297-2305 (1995)
   PUBMED   7540278
REFERENCE   9  (residues 1 to 233)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
REFERENCE   10 (residues 1 to 233)
  AUTHORS   Boise,L.H., Gonzalez-Garcia,M., Postema,C.E., Ding,L., Lindsten,T.,
            Turka,L.A., Mao,X., Nunez,G. and Thompson,C.B.
  TITLE     bcl-x, a bcl-2-related gene that functions as a dominant regulator
            of apoptotic cell death
  JOURNAL   Cell 74 (4), 597-608 (1993)
   PUBMED   8358789
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160175.5 and AL117381.32.
            
            Summary: The protein encoded by this gene belongs to the BCL-2
            protein family. BCL-2 family members form hetero- or homodimers and
            act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. The proteins encoded by this
            gene are located at the outer mitochondrial membrane, and have been
            shown to regulate outer mitochondrial membrane channel (VDAC)
            opening. VDAC regulates mitochondrial membrane potential, and thus
            controls the production of reactive oxygen species and release of
            cytochrome C by mitochondria, both of which are the potent inducers
            of cell apoptosis. Alternative splicing results in multiple
            transcript variants encoding two different isoforms. The longer
            isoform acts as an apoptotic inhibitor and the shorter isoform acts
            as an apoptotic activator. [provided by RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853562.21055.1,
                                           SRR14038196.3096896.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..233
                     /product="bcl-2-like protein 1 isoform Bcl-X(L)"
                     /note="bcl-2-like protein 1; apoptosis regulator Bcl-X;
                     protein phosphatase 1, regulatory subunit 52"
                     /calculated_mol_wt=25918
     Region          1..233
                     /region_name="bcl-2"
                     /note="apoptosis regulator; TIGR00865"
                     /db_xref="CDD:273308"
     Region          4..24
                     /region_name="BH4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Region          28..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000269|PubMed:21840391; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Site            61..62
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-1; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:19917720; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Region          86..100
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            90..98
                     /site_type="active"
                     /note="BH3 [active]"
                     /db_xref="CDD:132900"
     Site            order(93..94,96..97,101,104..105,121..122,125..126,
                     129..130,136,138..139,141..142,146,150,194)
                     /site_type="active"
                     /note="BH3-homology region binding site [active]"
                     /db_xref="CDD:132900"
     Region          129..148
                     /region_name="BH1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            order(129..131,135..147)
                     /site_type="active"
                     /note="BH1 [active]"
                     /db_xref="CDD:132900"
     Region          180..195
                     /region_name="BH2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            180..194
                     /site_type="active"
                     /note="BH2 [active]"
                     /db_xref="CDD:132900"
     Site            210..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     CDS             1..233
                     /gene="BCL2L1"
                     /gene_synonym="Bcl-X; BCL-XL/S; BCL2L; BCLX; PPP1R52"
                     /coded_by="NM_001424331.1:170..871"
                     /note="isoform Bcl-X(L) is encoded by transcript variant
                     10"
                     /db_xref="GeneID:598"
                     /db_xref="HGNC:HGNC:992"
                     /db_xref="MIM:600039"
ORIGIN      
        1 msqsnrelvv dflsyklsqk gyswsqfsdv eenrteapeg tesemetpsa ingnpswhla
       61 dspavngatg hsssldarev ipmaavkqal reagdefelr yrrafsdlts qlhitpgtay
      121 qsfeqvvnel frdgvnwgri vaffsfggal cvesvdkemq vlvsriaawm atylndhlep
      181 wiqenggwdt fvelygnnaa aesrkgqerf nrwfltgmtv agvvllgslf srk
//
LOCUS       NP_001393524            1164 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 1 [Homo sapiens].
ACCESSION   NP_001393524 XP_016870586
VERSION     NP_001393524.1
DBSOURCE    REFSEQ: accession NM_001406595.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1164)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1164)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1164)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1164)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1164)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1164)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1164)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            On May 20, 2022 this sequence version replaced XP_016870586.1.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138524.178266.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1164
                     /product="hamartin isoform 1"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=129636
     Region          7..719
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          403..787
                     /region_name="Mediates interaction with WDR45B.
                     /evidence=ECO:0000269|PubMed:28561066"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Region          439..571
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <708..>960
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1006..1085
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1131..1164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1164
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406595.1:408..3902"
                     /note="isoform 1 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS6956.1"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt aggkgtplgt patspppapl chsddyvhis lpqatvtppr
      421 keermdsarp clhrqhhlln drgseeppgs kgsvtlsdlp gflgdlasee dsiekdkeea
      481 aisrelseit taeaepvvpr ggfdspfyrd slpgsqrkth saasssqgas vnpeplhssl
      541 dklgpdtpkq aftpidlpcg sadespagdr ecqtsletsi ftpspckipp ptrvgfgsgq
      601 pppydhlfev alpktahhfv irkteellkk akgnteedgv pstspmevld rliqqgadah
      661 skelnklplp sksvdwthfg gsppsdeirt lrdqllllhn qllyerfkrq qhalrnrrll
      721 rkvikaaale ehnaamkdql klqekdiqmw kvslqkeqar ynqlqeqrdt mvtklhsqir
      781 qlqhdreefy nqsqelqtkl edcrnmiael rielkkannk vchtelllsq vsqklsnses
      841 vqqqmeflnr qllvlgevne lyleqlqnkh sdttkevemm kaayrkelek nrshvlqqtq
      901 rldtsqkril eleshlakkd hllleqkkyl edvklqargq lqaaesryea qkritqvfel
      961 eildlygrle kdgllkklee ekaeaaeaae erldccndgc sdsmvghnee asghngetkt
     1021 prpssargss gsrggggsss ssselstpek pphqragpfs srwettmgea sasipttvgs
     1081 lpssksflgm karelfrnks esqcdedgmt sslseslkte lgkdlgveak iplnldgphp
     1141 spptpdsvgq lhimdyneth hehs
//
LOCUS       NP_001428256            1785 aa            linear   PRI 21-NOV-2025
DEFINITION  BCL-6 corepressor-like protein 1 isoform 1a [Homo sapiens].
ACCESSION   NP_001428256 XP_016885210 XP_054183518
VERSION     NP_001428256.1
DBSOURCE    REFSEQ: accession NM_001441327.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1785)
  AUTHORS   Luo,C., Chen,Z., Meng,L., Tan,C., He,W., Tu,C., Du,J., Lu,G.X.,
            Lin,G., Tan,Y.Q. and Hu,T.Y.
  TITLE     A hemizygous loss-of-function variant in BCORL1 is associated with
            male infertility and oligoasthenoteratozoospermia
  JOURNAL   Clin Genet 106 (1), 27-36 (2024)
   PUBMED   38342987
  REMARK    GeneRIF: A hemizygous loss-of-function variant in BCORL1 is
            associated with male infertility and oligoasthenoteratozoospermia.
REFERENCE   2  (residues 1 to 1785)
  AUTHORS   Kommoss,F.K.F., Chiang,S., Kobel,M., Koelsche,C., Chang,K.T.,
            Irving,J.A., Dickson,B., Thiryayi,S., Rouzbahman,M., Rasty,G., von
            Deimling,A., Lee,C.H. and Turashvili,G.
  TITLE     Endometrial Stromal Sarcomas With BCOR Internal Tandem Duplication
            and Variant BCOR/BCORL1 Rearrangements Resemble High-grade
            Endometrial Stromal Sarcomas With Recurrent CDK4 Pathway
            Alterations and MDM2 Amplifications
  JOURNAL   Am J Surg Pathol 46 (8), 1142-1152 (2022)
   PUBMED   35499168
  REMARK    GeneRIF: Endometrial Stromal Sarcomas With BCOR Internal Tandem
            Duplication and Variant BCOR/BCORL1 Rearrangements Resemble
            High-grade Endometrial Stromal Sarcomas With Recurrent CDK4 Pathway
            Alterations and MDM2 Amplifications.
REFERENCE   3  (residues 1 to 1785)
  AUTHORS   Schaefer,E.J., Wang,H.C., Karp,H.Q., Meyer,C.A., Cejas,P.,
            Gearhart,M.D., Adelman,E.R., Fares,I., Apffel,A., Lim,K., Xie,Y.,
            Gibson,C.J., Schenone,M., Murdock,H.M., Wang,E.S., Gondek,L.P.,
            Carroll,M.P., Vedula,R.S., Winer,E.S., Garcia,J.S., Stone,R.M.,
            Luskin,M.R., Carr,S.A., Long,H.W., Bardwell,V.J., Figueroa,M.E. and
            Lindsley,R.C.
  TITLE     BCOR and BCORL1 Mutations Drive Epigenetic Reprogramming and
            Oncogenic Signaling by Unlinking PRC1.1 from Target Genes
  JOURNAL   Blood Cancer Discov 3 (2), 116-135 (2022)
   PUBMED   35015684
  REMARK    GeneRIF: BCOR and BCORL1 Mutations Drive Epigenetic Reprogramming
            and Oncogenic Signaling by Unlinking PRC1.1 from Target Genes.
REFERENCE   4  (residues 1 to 1785)
  AUTHORS   Gafner,M., Michelson,M., Argilli,E., Yosovich,K., Sherr,E.H.,
            Parks,K.C., England,E.M., Hady-Cohen,R., Leibovitz,Z., Lev,D.,
            Michaeli-Yosef,Y., Lerman-Sagie,T. and Blumkin,L.
  TITLE     Major brain malformations: corpus callosum dysgenesis, agenesis of
            septum pellucidum and polymicrogyria in patients with
            BCORL1-related disorders
  JOURNAL   J Hum Genet 67 (2), 95-101 (2022)
   PUBMED   34400773
  REMARK    GeneRIF: Major brain malformations: corpus callosum dysgenesis,
            agenesis of septum pellucidum and polymicrogyria in patients with
            BCORL1-related disorders.
REFERENCE   5  (residues 1 to 1785)
  AUTHORS   Junco,S.E., Wang,R., Gaipa,J.C., Taylor,A.B., Schirf,V.,
            Gearhart,M.D., Bardwell,V.J., Demeler,B., Hart,P.J. and Kim,C.A.
  TITLE     Structure of the polycomb group protein PCGF1 in complex with BCOR
            reveals basis for binding selectivity of PCGF homologs
  JOURNAL   Structure 21 (4), 665-671 (2013)
   PUBMED   23523425
REFERENCE   6  (residues 1 to 1785)
  AUTHORS   Shaffer,J.R., Feingold,E., Wang,X., Lee,M., Tcuenco,K., Weeks,D.E.,
            Weyant,R.J., Crout,R., McNeil,D.W. and Marazita,M.L.
  TITLE     GWAS of dental caries patterns in the permanent dentition
  JOURNAL   J Dent Res 92 (1), 38-44 (2013)
   PUBMED   23064961
REFERENCE   7  (residues 1 to 1785)
  AUTHORS   Gao,Z., Zhang,J., Bonasio,R., Strino,F., Sawai,A., Parisi,F.,
            Kluger,Y. and Reinberg,D.
  TITLE     PCGF homologs, CBX proteins, and RYBP define functionally distinct
            PRC1 family complexes
  JOURNAL   Mol Cell 45 (3), 344-356 (2012)
   PUBMED   22325352
REFERENCE   8  (residues 1 to 1785)
  AUTHORS   Li,M., Collins,R., Jiao,Y., Ouillette,P., Bixby,D., Erba,H.,
            Vogelstein,B., Kinzler,K.W., Papadopoulos,N. and Malek,S.N.
  TITLE     Somatic mutations in the transcriptional corepressor gene BCORL1 in
            adult acute myelogenous leukemia
  JOURNAL   Blood 118 (22), 5914-5917 (2011)
   PUBMED   21989985
  REMARK    GeneRIF: BCORL1 by genetic criteria is a novel candidate tumor
            suppressor gene, joining the growing list of genes recurrently
            mutated in acute myelogenous leukemia.
REFERENCE   9  (residues 1 to 1785)
  AUTHORS   Pagan,J.K., Arnold,J., Hanchard,K.J., Kumar,R., Bruno,T.,
            Jones,M.J., Richard,D.J., Forrest,A., Spurdle,A., Verdin,E.,
            Crossley,M., Fanciulli,M., Chenevix-Trench,G., Young,D.B. and
            Khanna,K.K.
  TITLE     A novel corepressor, BCoR-L1, represses transcription through an
            interaction with CtBP
  JOURNAL   J Biol Chem 282 (20), 15248-15257 (2007)
   PUBMED   17379597
REFERENCE   10 (residues 1 to 1785)
  AUTHORS   Lose,F., Arnold,J., Young,D.B., Brown,C.J., Mann,G.J., Pupo,G.M.,
            Khanna,K.K., Chenevix-Trench,G. and Spurdle,A.B.
  CONSRTM   Kathleen Cuningham Foundation Consortium for Research into Familial
            Breast Cancer
  TITLE     BCoR-L1 variation and breast cancer
  JOURNAL   Breast Cancer Res 9 (4), R54 (2007)
   PUBMED   17697391
  REMARK    GeneRIF: Dysregulated BCoR-L1 expression is associated with breast
            cancer
            Erratum:[Breast Cancer Res. 2008;10(5):406]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL034405.16, Z82208.1,
            KF459400.1 and AL136450.8.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_016885210.1, XP_054183518.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            corepressor that is found tethered to promoter regions by
            DNA-binding proteins. The encoded protein can interact with several
            different class II histone deacetylases to repress transcription.
            Two transcript variants encoding different isoforms have been found
            for this gene. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1265791.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1785
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.1"
     Protein         1..1785
                     /product="BCL-6 corepressor-like protein 1 isoform 1a"
                     /note="BCoR-like protein 1"
                     /calculated_mol_wt=190431
     Region          65..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          113..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          <198..636
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          343..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          527..550
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          562..646
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          753..781
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          876..901
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          937..977
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1029
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1033
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1107..1293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1312..1487
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1328..1336
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          <1494..>1603
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1496..1527
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1497,1501..1502,1505..1507,1509..1510,1514,1517,
                     1527,1529,1531,1535..1536,1539..1541,1543..1544,1548,1551,
                     1560,1562,1564,1568..1569,1572..1574,1576..1577,1581,1584)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1529..1560
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1529..1558
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1562..1591
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1562..1591
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1595..1623
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1666..1779
                     /region_name="PUFD_like_1"
                     /note="PCGF Ub-like fold discriminator of BCOR-like 1;
                     cd14260"
                     /db_xref="CDD:271223"
     Region          1668..1785
                     /region_name="PCGF Ub-like fold domain (PUFD), required
                     for the interaction with the KDM2B-SKP1 heterodimeric
                     complex. /evidence=ECO:0000269|PubMed:27568929"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            order(1668,1670..1680,1682,1684,1693..1695,1697,
                     1738..1739,1741,1744,1766,1777,1779)
                     /site_type="other"
                     /note="RAWUL domain interface [polypeptide binding]"
                     /db_xref="CDD:271223"
     CDS             1..1785
                     /gene="BCORL1"
                     /gene_synonym="BCoR-L1; CXorf10; SHUVER"
                     /coded_by="NM_001441327.1:511..5868"
                     /note="isoform 1a is encoded by transcript variant 5"
                     /db_xref="GeneID:63035"
                     /db_xref="HGNC:HGNC:25657"
                     /db_xref="MIM:300688"
ORIGIN      
        1 mistaplysg vhnwtssdri rmcgineerr aplsdeestt gdcqhfgsqe fcvsssfskv
       61 eltavgsgsn argadpdgsa teklghksed kpddpqpkmd yagnvaeaeg llvplsspgd
      121 glklpasdsa easnsradcs wtplntqmsk qvdcspagvk aldsrqgvge kntfilatlg
      181 tgvpvegtlp lvttnfsplp apicppapgs asvphsvpda fqvplsvpap vphsglvpvq
      241 vatsvpapsp plapvpalap appsvptlis dsnplsvsas vlvpvpasap psgpvplsap
      301 apaplsvpvs applaliqap vppsaptlvl apvptpvlap mpastppaap appsvpmptp
      361 tpssgppstp tlipafaptp vpaptpapif tpaptpmpaa tpaaiptsap ipasfslsrv
      421 cfpaaqapam qkvplsfqpg tvltpsqplv yipppscgqp lsvatlpttl gvsstltlpv
      481 lpsylqdrcl pgvlaspelr sypyafsvar pltsdsklvs levnrlpcts psgstttqpa
      541 pdgvpgplad tslvtasakv lptpqpllpa psgssapphp akmpsgteqq tegtsvtfsp
      601 lksppqlere masppecsem pldlssksnr qklplpnqrk tppmpvltpv htsskallst
      661 vlsrsqrttq aaggnvtscl gstsspfvif peivrngdps twvknstali stipgtyvgv
      721 anpvpaslll nkdpnlglnr dprhlpkqep isiidqgepk gtgatcgkkg sqagaegqps
      781 tvkrytpari apglpgcqtk elslwkptgp aniyprcsvn gkptstqvlp vgwspyhqas
      841 llsigissag qltpsqgapi rptsvvsefs gvpslsssea vhglpegqpr pggsfvpeqd
      901 pvtknktcri aakpyeeqvn pvlltlspqt gtlalsvqps ggdirmnqgp eeseshlcsd
      961 stpkmegpqg acglklagdt kpknqvlaty mshelvlatp qnlpkmpelp llphdshpke
     1021 lildvvpssr rgssterpql gsqvdlgrvk mekvdgdvvf nlatcfradg lpvapqrgqa
     1081 evrakagqar vkqesvgvfa cknkwqpddv teslppkkmk cgkekdseeq qlqpqakavv
     1141 rsshrpkcrk lpsdpqestk ksprgasdsg kehngvrgkh khrkptkpes qspgkradsh
     1201 eegslekkak ssfrdfipvv lstrtrsqsg sicssfagma dsdmgsqevf pteeeeevtp
     1261 tpakrrkvrk tqrdtqyrsh haqdksllsq grrhlwrare mpwrteaarq mwdtneeeee
     1321 eeeegllkrk krrrqksrky qtgeylteqe deqrrkgrad lkarkqktss sqslehrlrn
     1381 rnlllpnkvq gisdspngfl pnnleepacl ensekpsgkr kcktkhmatv seeakgkgrw
     1441 sqqktrspks ptpvkptepc tpsksrsass eeasesptar qippearrli vnknagetll
     1501 qraarlgykd vvlyclqkds edvnhrdnag ytalheacsr gwtdilnill ehganvncsa
     1561 qdgtrpvhda vvndnletiw lllsygadpt latysgqtam klassdtmkr flsdhlsdlq
     1621 graegdpgvs wdfysssvle ekdgfacdll hnppgssdqe gddpmeeddf mfelsdkpll
     1681 pcynlqvsvs rgpcnwflfs dvlkrlklss rifqarfphf eittmpkaef yrqvassqll
     1741 tpaerpggld drsppgsset velvryepdl lrllgsevef qscns
//
LOCUS       NP_001411261             233 aa            linear   PRI 21-NOV-2025
DEFINITION  bcl-2-like protein 1 isoform Bcl-X(L) [Homo sapiens].
ACCESSION   NP_001411261
VERSION     NP_001411261.1
DBSOURCE    REFSEQ: accession NM_001424332.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Nguyen,T.T., Torrini,C., Shang,E., Shu,C., Mun,J.Y., Gao,Q.,
            Humala,N., Akman,H.O., Zhang,G., Westhoff,M.A., Karpel-Massler,G.,
            Bruce,J.N., Canoll,P. and Siegelin,M.D.
  TITLE     OGDH and Bcl-xL loss causes synthetic lethality in glioblastoma
  JOURNAL   JCI Insight 9 (8), e172565 (2024)
   PUBMED   38483541
  REMARK    GeneRIF: OGDH and Bcl-xL loss causes synthetic lethality in
            glioblastoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Li,S., Wang,Y., Chen,Y., Zhang,H., Shen,K. and Guan,H.
  TITLE     PTEN hinders the formation of scars by regulating the levels of
            proteins in the extracellular matrix and promoting the apoptosis of
            dermal fibroblasts through Bcl-xL
  JOURNAL   Arch Biochem Biophys 753, 109912 (2024)
   PUBMED   38325773
  REMARK    GeneRIF: PTEN hinders the formation of scars by regulating the
            levels of proteins in the extracellular matrix and promoting the
            apoptosis of dermal fibroblasts through Bcl-xL.
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Dou,Z., Lei,H., Su,W., Zhang,T., Chen,X., Yu,B., Zhen,X., Si,J.,
            Sun,C., Zhang,H. and Di,C.
  TITLE     Modification of BCLX pre-mRNA splicing has antitumor efficacy alone
            or in combination with radiotherapy in human glioblastoma cells
  JOURNAL   Cell Death Dis 15 (2), 160 (2024)
   PUBMED   38383492
  REMARK    GeneRIF: Modification of BCLX pre-mRNA splicing has antitumor
            efficacy alone or in combination with radiotherapy in human
            glioblastoma cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Yin,L., Hu,X., Pei,G., Tang,M., Zhou,Y., Zhang,H., Huang,M., Li,S.,
            Zhang,J., Citu,C., Zhao,Z., Debeb,B.G., Feng,X. and Chen,J.
  TITLE     Genome-wide CRISPR screen reveals the synthetic lethality between
            BCL2L1 inhibition and radiotherapy
  JOURNAL   Life Sci Alliance 7 (4), e202302353 (2024)
   PUBMED   38316463
  REMARK    GeneRIF: Genome-wide CRISPR screen reveals the synthetic lethality
            between BCL2L1 inhibition and radiotherapy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 233)
  AUTHORS   Broome,H.E., Dargan,C.M., Krajewski,S. and Reed,J.C.
  TITLE     Expression of Bcl-2, Bcl-x, and Bax after T cell activation and
            IL-2 withdrawal
  JOURNAL   J Immunol 155 (5), 2311-2317 (1995)
   PUBMED   7650367
REFERENCE   7  (residues 1 to 233)
  AUTHORS   Sedlak,T.W., Oltvai,Z.N., Yang,E., Wang,K., Boise,L.H.,
            Thompson,C.B. and Korsmeyer,S.J.
  TITLE     Multiple Bcl-2 family members demonstrate selective dimerizations
            with Bax
  JOURNAL   Proc Natl Acad Sci U S A 92 (17), 7834-7838 (1995)
   PUBMED   7644501
REFERENCE   8  (residues 1 to 233)
  AUTHORS   Jaattela,M., Benedict,M., Tewari,M., Shayman,J.A. and Dixit,V.M.
  TITLE     Bcl-x and Bcl-2 inhibit TNF and Fas-induced apoptosis and
            activation of phospholipase A2 in breast carcinoma cells
  JOURNAL   Oncogene 10 (12), 2297-2305 (1995)
   PUBMED   7540278
REFERENCE   9  (residues 1 to 233)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
REFERENCE   10 (residues 1 to 233)
  AUTHORS   Boise,L.H., Gonzalez-Garcia,M., Postema,C.E., Ding,L., Lindsten,T.,
            Turka,L.A., Mao,X., Nunez,G. and Thompson,C.B.
  TITLE     bcl-x, a bcl-2-related gene that functions as a dominant regulator
            of apoptotic cell death
  JOURNAL   Cell 74 (4), 597-608 (1993)
   PUBMED   8358789
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160175.5 and AL117381.32.
            
            Summary: The protein encoded by this gene belongs to the BCL-2
            protein family. BCL-2 family members form hetero- or homodimers and
            act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. The proteins encoded by this
            gene are located at the outer mitochondrial membrane, and have been
            shown to regulate outer mitochondrial membrane channel (VDAC)
            opening. VDAC regulates mitochondrial membrane potential, and thus
            controls the production of reactive oxygen species and release of
            cytochrome C by mitochondria, both of which are the potent inducers
            of cell apoptosis. Alternative splicing results in multiple
            transcript variants encoding two different isoforms. The longer
            isoform acts as an apoptotic inhibitor and the shorter isoform acts
            as an apoptotic activator. [provided by RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1658048.1,
                                           SRR14038194.4077229.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..233
                     /product="bcl-2-like protein 1 isoform Bcl-X(L)"
                     /note="bcl-2-like protein 1; apoptosis regulator Bcl-X;
                     protein phosphatase 1, regulatory subunit 52"
                     /calculated_mol_wt=25918
     Region          1..233
                     /region_name="bcl-2"
                     /note="apoptosis regulator; TIGR00865"
                     /db_xref="CDD:273308"
     Region          4..24
                     /region_name="BH4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Region          28..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000269|PubMed:21840391; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Site            61..62
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-1; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:19917720; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Region          86..100
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            90..98
                     /site_type="active"
                     /note="BH3 [active]"
                     /db_xref="CDD:132900"
     Site            order(93..94,96..97,101,104..105,121..122,125..126,
                     129..130,136,138..139,141..142,146,150,194)
                     /site_type="active"
                     /note="BH3-homology region binding site [active]"
                     /db_xref="CDD:132900"
     Region          129..148
                     /region_name="BH1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            order(129..131,135..147)
                     /site_type="active"
                     /note="BH1 [active]"
                     /db_xref="CDD:132900"
     Region          180..195
                     /region_name="BH2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            180..194
                     /site_type="active"
                     /note="BH2 [active]"
                     /db_xref="CDD:132900"
     Site            210..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     CDS             1..233
                     /gene="BCL2L1"
                     /gene_synonym="Bcl-X; BCL-XL/S; BCL2L; BCLX; PPP1R52"
                     /coded_by="NM_001424332.1:188..889"
                     /note="isoform Bcl-X(L) is encoded by transcript variant
                     11"
                     /db_xref="GeneID:598"
                     /db_xref="HGNC:HGNC:992"
                     /db_xref="MIM:600039"
ORIGIN      
        1 msqsnrelvv dflsyklsqk gyswsqfsdv eenrteapeg tesemetpsa ingnpswhla
       61 dspavngatg hsssldarev ipmaavkqal reagdefelr yrrafsdlts qlhitpgtay
      121 qsfeqvvnel frdgvnwgri vaffsfggal cvesvdkemq vlvsriaawm atylndhlep
      181 wiqenggwdt fvelygnnaa aesrkgqerf nrwfltgmtv agvvllgslf srk
//
LOCUS       NP_001393993             460 aa            linear   PRI 21-NOV-2025
DEFINITION  merlin isoform 18 [Homo sapiens].
ACCESSION   NP_001393993
VERSION     NP_001393993.1
DBSOURCE    REFSEQ: accession NM_001407064.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 460)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 460)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 460)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 460)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 460)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 460)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005529.7 and AC004882.3.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2295697.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437, SAMN03267761
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..460
                     /product="merlin isoform 18"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=53398
     Region          20..>41
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     Region          <37..139
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          133..229
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(175..176,178..184,193,214,217..218,221)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(175,178..185,193,214,217..218,221)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(211,215)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            214..229
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          224..>284
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          263..382
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     CDS             1..460
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_001407064.1:367..1749"
                     /note="isoform 18 is encoded by transcript variant 26"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 magaiasrms fsslkrkqpk tftvrivtmd aemefncevk kqildekiyc ppeasvllas
       61 yavqakygdy dpsvhkrgfl aqeellpkrv inlyqmtpem weeritawya ehrgrardea
      121 emeylkiaqd lemygvnyfa irnkkgtell lgvdalglhi ydpenrltpk isfpwneirn
      181 isysdkefti kpldkkidvf kfnssklrvn klilqlcign hdlfmrrrka dslevqqmka
      241 qareekarkq merqrlarek qmreeaertr delerrllqm keeatmanea lmrseetadl
      301 laekaqitee eakllaqkaa eaeqemqrik atairteeek rlmeqkvlea evlalkmaee
      361 serrakeadq lkqdlqeare aerrakqkll eiatkptypp mnpipaplpp dipsfnligd
      421 slsfdfkdtd mkrlsmeiek enspcrapsp ewpslksssr
//
LOCUS       NP_001393546            1043 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 5 [Homo sapiens].
ACCESSION   NP_001393546
VERSION     NP_001393546.1
DBSOURCE    REFSEQ: accession NM_001406617.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1043)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1043)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1043)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1043)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1043)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1043)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1043)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2094190.1,
                                           SRR14372079.2015062.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1043
                     /product="hamartin isoform 5"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=116145
     Region          16..598
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <587..>839
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1043
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406617.1:448..3579"
                     /note="isoform 5 is encoded by transcript variant 31"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mdtdvvvltt gvlvlitmlp mipqsgkqhl ldffdifgrl sswclkkpgh vaevylvhlh
       61 asvyalfhrl ygmypcnfvs flrshysmke nletfeevvk pmmehvrihp elvtgskdhe
      121 ldprrwkrle thdvviecak isldpteasy edgysvshqi sarfphrsad vttspyadtq
      181 nsygcatstp ystsrlmlln mpgqlpqtls spstrlitep pqatlwspsm vcgmttppts
      241 pgnvppdlsh pyskvfgtta ggkgtplgtp atspppaplc hsddyvhisl pqatvtpprk
      301 eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed siekdkeeaa
      361 isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv npeplhssld
      421 klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp trvgfgsgqp
      481 ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr liqqgadahs
      541 kelnklplps ksvdwthfgg sppsdeirtl rdqllllhnq llyerfkrqq halrnrrllr
      601 kvikaaalee hnaamkdqlk lqekdiqmwk vslqkeqary nqlqeqrdtm vtklhsqirq
      661 lqhdreefyn qsqelqtkle dcrnmiaelr ielkkannkv chtelllsqv sqklsnsesv
      721 qqqmeflnrq llvlgevnel yleqlqnkhs dttkevemmk aayrkelekn rshvlqqtqr
      781 ldtsqkrile leshlakkdh llleqkkyle dvklqargql qaaesryeaq kritqvfele
      841 ildlygrlek dgllkkleee kaeaaeaaee rldccndgcs dsmvghneea sghngetktp
      901 rpssargssg srggggssss sselstpekp phqragpfss rwettmgeas asipttvgsl
      961 pssksflgmk arelfrnkse sqcdedgmts slseslktel gkdlgveaki plnldgphps
     1021 pptpdsvgql himdynethh ehs
//
LOCUS       NP_001393987             549 aa            linear   PRI 21-NOV-2025
DEFINITION  merlin isoform 6 [Homo sapiens].
ACCESSION   NP_001393987
VERSION     NP_001393987.1
DBSOURCE    REFSEQ: accession NM_001407058.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 549)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 549)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 549)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 549)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 549)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005529.7 and AC004882.3.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1536504.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..549
                     /product="merlin isoform 6"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=64058
     Region          23..181
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          175..271
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(217..218,220..226,235,256,259..260,263)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(217,220..227,235,256,259..260,263)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(253,257)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            256..271
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          266..>326
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          305..424
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          477..>538
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..549
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_001407058.1:367..2016"
                     /note="isoform 6 is encoded by transcript variant 20"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 magaiasrms fsslkrkqpk tftvrivtmd aemefncemk wkgkdlfdlv crtlglretw
       61 ffglqytikd tvawlkmdkk vkkqildeki ycppeasvll asyavqakyg dydpsvhkrg
      121 flaqeellpk rvinlyqmtp emweeritaw yaehrgrard eaemeylkia qdlemygvny
      181 fairnkkgte lllgvdalgl hiydpenrlt pkisfpwnei rnisysdkef tikpldkkid
      241 vfkfnssklr vnklilqlci gnhdlfmrrr kadslevqqm kaqareekar kqmerqrlar
      301 ekqmreeaer trdelerrll qmkeeatman ealmrseeta dllaekaqit eeeakllaqk
      361 aaeaeqemqr ikatairtee ekrlmeqkvl eaevlalkma eeserrakea dqlkqdlqea
      421 reaerrakqk lleiatkpty ppmnpipapl ppdipsfnli gdslsfdfkd tdmkrlsmei
      481 ekekveymek skhlqeqlne lkteiealkl keretaldil hnensdrggs skhntikkpq
      541 aqgrrpici
//
LOCUS       NP_001392590            1192 aa            linear   PRI 21-NOV-2025
DEFINITION  phospholipid-transporting ATPase IH isoform c [Homo sapiens].
ACCESSION   NP_001392590 XP_005268356
VERSION     NP_001392590.1
DBSOURCE    REFSEQ: accession NM_001405661.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1192)
  AUTHORS   Higuchi,T., Oka,S., Furukawa,H., Shimada,K., Tsunoda,S., Ito,S.,
            Okamoto,A., Fujimori,M., Nakamura,T., Katayama,M., Saisho,K.,
            Shinohara,S., Matsui,T., Migita,K., Nagaoka,S. and Tohma,S.
  TITLE     Association of a Single Nucleotide Variant in TERT with Airway
            Disease in Japanese Rheumatoid Arthritis Patients
  JOURNAL   Genes (Basel) 14 (11), 2084 (2023)
   PUBMED   38003027
  REMARK    GeneRIF: Association of a Single Nucleotide Variant in TERT with
            Airway Disease in Japanese Rheumatoid Arthritis Patients.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1192)
  AUTHORS   Chepurwar,S., von Loh,S.M., Wigger,D.C., Neef,J., Frommolt,P.,
            Beutner,D., Lang-Roth,R., Kubisch,C., Strenzke,N. and Volk,A.E.
  TITLE     A mutation in ATP11A causes autosomal-dominant auditory neuropathy
            type 2
  JOURNAL   Hum Mol Genet 32 (7), 1083-1089 (2023)
   PUBMED   36300302
  REMARK    GeneRIF: A mutation in ATP11A causes autosomal-dominant auditory
            neuropathy type 2.
REFERENCE   3  (residues 1 to 1192)
  AUTHORS   Miyata,Y., Yamada,K., Nagata,S. and Segawa,K.
  TITLE     Two types of type IV P-type ATPases independently re-establish the
            asymmetrical distribution of phosphatidylserine in plasma membranes
  JOURNAL   J Biol Chem 298 (11), 102527 (2022)
   PUBMED   36162506
REFERENCE   4  (residues 1 to 1192)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   5  (residues 1 to 1192)
  AUTHORS   Pater,J.A., Penney,C., O'Rielly,D.D., Griffin,A., Kamal,L.,
            Brownstein,Z., Vona,B., Vinkler,C., Shohat,M., Barel,O.,
            French,C.R., Singh,S., Werdyani,S., Burt,T., Abdelfatah,N.,
            Houston,J., Doucette,L.P., Squires,J., Glaser,F., Roslin,N.M.,
            Vincent,D., Marquis,P., Woodland,G., Benoukraf,T., Hawkey-Noble,A.,
            Avraham,K.B., Stanton,S.G. and Young,T.L.
  TITLE     Autosomal dominant non-syndromic hearing loss maps to DFNA33
            (13q34) and co-segregates with splice and frameshift variants in
            ATP11A, a phospholipid flippase gene
  JOURNAL   Hum Genet 141 (3-4), 431-444 (2022)
   PUBMED   35278131
  REMARK    GeneRIF: Autosomal dominant non-syndromic hearing loss maps to
            DFNA33 (13q34) and co-segregates with splice and frameshift
            variants in ATP11A, a phospholipid flippase gene.
REFERENCE   6  (residues 1 to 1192)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 1192)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   8  (residues 1 to 1192)
  AUTHORS   Andrew Nesbit,M., Bowl,M.R., Harding,B., Schlessinger,D.,
            Whyte,M.P. and Thakker,R.V.
  TITLE     X-linked hypoparathyroidism region on Xq27 is evolutionarily
            conserved with regions on 3q26 and 13q34 and contains a novel
            P-type ATPase
  JOURNAL   Genomics 84 (6), 1060-1070 (2004)
   PUBMED   15533723
REFERENCE   9  (residues 1 to 1192)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
REFERENCE   10 (residues 1 to 1192)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139384.17, AL356752.13 and
            AL356740.19.
            
            On Apr 29, 2022 this sequence version replaced XP_005268356.1.
            
            Summary: The protein encoded by this gene is an integral membrane
            ATPase. The encoded protein is probably phosphorylated in its
            intermediate state and likely drives the transport of ions such as
            calcium across membranes. [provided by RefSeq, Apr 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1135590.1,
                                           SRR14038196.834525.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..1192
                     /product="phospholipid-transporting ATPase IH isoform c"
                     /EC_number="7.6.2.1"
                     /note="probable phospholipid-transporting ATPase IH;
                     potential phospholipid-transporting ATPase IH;
                     phospholipid-translocating ATPase; P4-ATPase flippase
                     complex alpha subunit ATP11A; ATPase, class VI, type 11A"
                     /calculated_mol_wt=135845
     Region          47..983
                     /region_name="P-type_ATPase_APLT_Dnf-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2,
                     -10D, -11B, -11C; cd02073"
                     /db_xref="CDD:319770"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            89..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            297..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            350..372
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            order(414..416,553,576..578,640,687..689,798,801,804,825,
                     828)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     Site            457..458
                     /site_type="cleavage"
                     /note="Cleavage, by CASP3.
                     /evidence=ECO:0000269|PubMed:26567335; propagated from
                     UniProtKB/Swiss-Prot (P98196.3)"
     Site            490..491
                     /site_type="cleavage"
                     /note="Cleavage, by CASP3.
                     /evidence=ECO:0000269|PubMed:26567335; propagated from
                     UniProtKB/Swiss-Prot (P98196.3)"
     Site            738
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P98196.3)"
     Site            882..902
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            915..934
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Region          <965..1061
                     /region_name="RDD"
                     /note="RDD family; cl00746"
                     /db_xref="CDD:469900"
     Site            965..986
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            1001..1023
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            1030..1050
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            1069..1093
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     CDS             1..1192
                     /gene="ATP11A"
                     /gene_synonym="ATPIH; ATPIS; AUNA2; DFNA84; HLD24"
                     /coded_by="NM_001405661.1:380..3958"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:23250"
                     /db_xref="HGNC:HGNC:13552"
                     /db_xref="MIM:605868"
ORIGIN      
        1 mdcslvrtlv hrycageenw vdsrtiyvgh repppgaeay ipqrypdnri vsskytfwnf
       61 ipknlfeqfr rvanfyflii flvqliidtp tspvtsglpl ffvitvtaik qgyedwlrhk
      121 adnamnqcpv hfiqhgklvr kqsrklrvgd ivmvkedetf pcdliflssn rgdgtchvtt
      181 asldgesshk thyavqdtkg fhteediggl hatieceqpq pdlykfvgri nvysdlndpv
      241 vrplgsenll lrgatlknte kifgvaiytg metkmalnyq sksqkrsave ksmnaflivy
      301 lciliskali ntvlkymwqs epfrdepwyn qkteserqrn lflkaftdfl afmvlfnyii
      361 pvsmyvtvem qkflgsyfit wdedmfdeet gegplvntsd lneelgqvey iftdktgtlt
      421 ennmefkecc ieghvyvphv icngqvlpes sgidmidssp svngrereel ffralclcht
      481 vqvkdddsvd gprkspdggk scvyissspd evalvegvqr lgftylrlkd nymeilnren
      541 hierfellei lsfdsvrrrm svivksatge iylfckgads sifprviegk vdqirarver
      601 naveglrtlc vaykrliqee yegickllqa akvalqdrek klaeayeqie kdltllgata
      661 vedrlqekaa dtiealqkag ikvwvltgdk metaaatcya cklfrrntql lelttkriee
      721 qslhdvlfel sktvlrhsgs ltrdnlsgls admqdyglii dgaalslimk predgssgny
      781 relfleicrs csavlccrma plqkaqivkl ikfskehpit laigdgandv smileahvgi
      841 gvigkegrqa arnsdyaipk fkhlkkmllv hghfyyiris elvqyffykn vcfifpqfly
      901 qffcgfsqqt lydtayltly nisftslpil lyslmeqhvg idvlkrdptl yrdvaknall
      961 rwrvfiywtl lglfdalvff fgayfvfent tvtsngqifg nwtfgtlvft vmvftvtlkl
     1021 aldthywtwi nhfviwgsll fyvvfsllwg gviwpflnyq rmyyvfiqml ssgpawlaiv
     1081 llvtisllpd vlkkvlcrql wptatervqq ngcaqprdrd seftplaslq spgyqstcps
     1141 aawysshsqq vtlaawkekv stepppilgg shhhcssips hscprsrvgm lv
//
LOCUS       NP_001393989             543 aa            linear   PRI 21-NOV-2025
DEFINITION  merlin isoform 15 [Homo sapiens].
ACCESSION   NP_001393989
VERSION     NP_001393989.1
DBSOURCE    REFSEQ: accession NM_001407060.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 543)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 543)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 543)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 543)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 543)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 543)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005529.7 and AC004882.3.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2146625.1,
                                           SRR14038192.292284.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..543
                     /product="merlin isoform 15"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=63391
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35240.1)"
     Region          23..222
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          216..312
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(258..259,261..267,276,297,300..301,304)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(258,261..268,276,297,300..301,304)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(294,298)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            297..312
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          307..>367
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          346..465
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PAK.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (P35240.1)"
     CDS             1..543
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_001407060.1:367..1998"
                     /note="isoform 15 is encoded by transcript variant 22"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 magaiasrms fsslkrkqpk tftvrivtmd aemefncemk wkgkdlfdlv crtlglretw
       61 ffglqytikd tvawlkmdkk vldhdvskee pvtfhflakf ypenaeeelv qeitqhlffl
      121 qvkkqildek iycppeasvl lasyavqaky gdydpsvhkr gflaqeellp krvinlyqmt
      181 pemweerita wyaehrgrar deaemeylki aqdlemygvn yfairnkkgt elllgvdalg
      241 lhiydpenrl tpkisfpwne irnisysdke ftikpldkki dvfkfnsskl rvnklilqlc
      301 ignhdlfmrr rkadslevqq mkaqareeka rkqmerqrla rekqmreeae rtrdelerrl
      361 lqmkeeatma nealmrseet adllaekaqi teeeakllaq kaaeaeqemq rikatairte
      421 eekrlmeqkv leaevlalkm aeeserrake adqlkqdlqe areaerrakq klleiatkpt
      481 yppmnpipap lppdipsfnl igdslsfdfk dtdmkrlsme iekenspcra pspewpslks
      541 ssr
//
LOCUS       NP_001397668            1727 aa            linear   PRI 21-NOV-2025
DEFINITION  intraflagellar transport protein 172 homolog isoform 2 [Homo
            sapiens].
ACCESSION   NP_001397668 XP_005264311
VERSION     NP_001397668.1
DBSOURCE    REFSEQ: accession NM_001410739.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1727)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1727)
  AUTHORS   Neroldova,M., Ciara,E., Slatinska,J., Frankova,S., Liskova,P.,
            Kotalova,R., Globinovska,J., Safarikova,M., Pfeiferova,L.,
            Zunova,H., Mrazova,L., Stranecky,V., Vrbacka,A., Fabian,O.,
            Sticova,E., Skanderova,D., Sperl,J., Kalousova,M., Zima,T.,
            Macek,M., Pawlowska,J., Knisely,A.S., Kmoch,S. and Jirsa,M.
  TITLE     Exome sequencing reveals IFT172 variants in patients with
            non-syndromic cholestatic liver disease
  JOURNAL   PLoS One 18 (7), e0288907 (2023)
   PUBMED   37471416
  REMARK    GeneRIF: Exome sequencing reveals IFT172 variants in patients with
            non-syndromic cholestatic liver disease.
            Erratum:[PLoS One. 2025 Jan 30;20(1):e0318705. doi:
            10.1371/journal.pone.0318705. PMID: 39883651]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1727)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1727)
  AUTHORS   O'Seaghdha,C.M., Yang,Q., Glazer,N.L., Leak,T.S., Dehghan,A.,
            Smith,A.V., Kao,W.H., Lohman,K., Hwang,S.J., Johnson,A.D.,
            Hofman,A., Uitterlinden,A.G., Chen,Y.D., Brown,E.M.,
            Siscovick,D.S., Harris,T.B., Psaty,B.M., Coresh,J., Gudnason,V.,
            Witteman,J.C., Liu,Y.M., Kestenbaum,B.R., Fox,C.S. and Kottgen,A.
  CONSRTM   GEFOS Consortium
  TITLE     Common variants in the calcium-sensing receptor gene are associated
            with total serum calcium levels
  JOURNAL   Hum Mol Genet 19 (21), 4296-4303 (2010)
   PUBMED   20705733
REFERENCE   5  (residues 1 to 1727)
  AUTHORS   Kottgen,A., Pattaro,C., Boger,C.A., Fuchsberger,C., Olden,M.,
            Glazer,N.L., Parsa,A., Gao,X., Yang,Q., Smith,A.V., O'Connell,J.R.,
            Li,M., Schmidt,H., Tanaka,T., Isaacs,A., Ketkar,S., Hwang,S.J.,
            Johnson,A.D., Dehghan,A., Teumer,A., Pare,G., Atkinson,E.J.,
            Zeller,T., Lohman,K., Cornelis,M.C., Probst-Hensch,N.M.,
            Kronenberg,F., Tonjes,A., Hayward,C., Aspelund,T., Eiriksdottir,G.,
            Launer,L.J., Harris,T.B., Rampersaud,E., Mitchell,B.D.,
            Arking,D.E., Boerwinkle,E., Struchalin,M., Cavalieri,M.,
            Singleton,A., Giallauria,F., Metter,J., de Boer,I.H.,
            Haritunians,T., Lumley,T., Siscovick,D., Psaty,B.M.,
            Zillikens,M.C., Oostra,B.A., Feitosa,M., Province,M., de
            Andrade,M., Turner,S.T., Schillert,A., Ziegler,A., Wild,P.S.,
            Schnabel,R.B., Wilde,S., Munzel,T.F., Leak,T.S., Illig,T.,
            Klopp,N., Meisinger,C., Wichmann,H.E., Koenig,W., Zgaga,L.,
            Zemunik,T., Kolcic,I., Minelli,C., Hu,F.B., Johansson,A., Igl,W.,
            Zaboli,G., Wild,S.H., Wright,A.F., Campbell,H., Ellinghaus,D.,
            Schreiber,S., Aulchenko,Y.S., Felix,J.F., Rivadeneira,F.,
            Uitterlinden,A.G., Hofman,A., Imboden,M., Nitsch,D.,
            Brandstatter,A., Kollerits,B., Kedenko,L., Magi,R., Stumvoll,M.,
            Kovacs,P., Boban,M., Campbell,S., Endlich,K., Volzke,H.,
            Kroemer,H.K., Nauck,M., Volker,U., Polasek,O., Vitart,V.,
            Badola,S., Parker,A.N., Ridker,P.M., Kardia,S.L., Blankenberg,S.,
            Liu,Y., Curhan,G.C., Franke,A., Rochat,T., Paulweber,B.,
            Prokopenko,I., Wang,W., Gudnason,V., Shuldiner,A.R., Coresh,J.,
            Schmidt,R., Ferrucci,L., Shlipak,M.G., van Duijn,C.M., Borecki,I.,
            Kramer,B.K., Rudan,I., Gyllensten,U., Wilson,J.F., Witteman,J.C.,
            Pramstaller,P.P., Rettig,R., Hastie,N., Chasman,D.I., Kao,W.H.,
            Heid,I.M. and Fox,C.S.
  TITLE     New loci associated with kidney function and chronic kidney disease
  JOURNAL   Nat Genet 42 (5), 376-384 (2010)
   PUBMED   20383146
REFERENCE   6  (residues 1 to 1727)
  AUTHORS   Howard,P.W. and Maurer,R.A.
  TITLE     Identification of a conserved protein that interacts with specific
            LIM homeodomain transcription factors
  JOURNAL   J Biol Chem 275 (18), 13336-13342 (2000)
   PUBMED   10788441
REFERENCE   7  (residues 1 to 1727)
  AUTHORS   Stokman,M., Lilien,M. and Knoers,N.
  TITLE     Nephronophthisis-Related Ciliopathies
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27336129
REFERENCE   8  (residues 1 to 1727)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   9  (residues 1 to 1727)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
REFERENCE   10 (residues 1 to 1727)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC074117.7.
            
            On Aug 15, 2022 this sequence version replaced XP_005264311.1.
            
            Summary: This gene encodes a subunit of the intraflagellar
            transport subcomplex IFT-B. Subcomplexes IFT-A and IFT-B are
            necessary for ciliary assembly and maintenance. Mutations in this
            gene have been associated with skeletal ciliopathies, with or
            without polydactyly, such as such short-rib thoracic dysplasias 1,
            9 or 10. [provided by RefSeq, Mar 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.554180.1,
                                           SRR14038194.1704896.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1727
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..1727
                     /product="intraflagellar transport protein 172 homolog
                     isoform 2"
                     /note="wimple homolog; selective LIM binding factor
                     homolog; intraflagellar transport protein 172 homolog;
                     intraflagellar transport 172 homolog"
                     /calculated_mol_wt=194824
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:20388717; propagated from
                     UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          14..53
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          17..318
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          20..64
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(33,37,43..44,55..56,83,87,93,98,111,127,132,
                     138..139,151,168,173,181..182,195..196,212,216,222..223,
                     234..235,256,261,266..267,276..277,303,314)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          64..103
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          69..110
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          110..148
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          116..148
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          150..191
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          155..194
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          195..233
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          200..248
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          238..278
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          284..323
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          571..602
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Site            650
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6VH22; propagated from
                     UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          670..703
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          786..>972
                     /region_name="SNAP"
                     /note="Soluble N-ethylmaleimide-sensitive factor (NSF)
                     Attachment Protein family; cl24038"
                     /db_xref="CDD:451671"
     Region          787..820
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          789..844
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276937"
     Region          832..865
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          848..884
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276937"
     Region          887..932
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276937"
     Region          890..923
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          925..948
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          949..982
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          1010..>1170
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          1020..1053
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          1120..1153
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          1133..>1266
                     /region_name="HemYx"
                     /note="Uncharacterized protein HemY, contains HemY_N
                     domain and TPR repeats (unrelated to protoporphyrinogen
                     oxidase HemY) [Function unknown]; COG3071"
                     /db_xref="CDD:442305"
     Region          1254..1287
                     /region_name="TPR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          1323..1356
                     /region_name="TPR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          1389..1423
                     /region_name="TPR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          1425..1455
                     /region_name="TPR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          1552..1585
                     /region_name="TPR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     CDS             1..1727
                     /gene="IFT172"
                     /gene_synonym="BBS20; NPHP17; osm-1; RP71; SLB; SRTD10;
                     wim"
                     /coded_by="NM_001410739.1:91..5274"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS92725.1"
                     /db_xref="GeneID:26160"
                     /db_xref="HGNC:HGNC:30391"
                     /db_xref="MIM:607386"
ORIGIN      
        1 mhlkhlrtll spqdgaakvt cmawsqnnak favctvdrvv llydehgerr dkfstkpadm
       61 kygrksymvk gmafspdstk iaigqtdnii yvykigedwg dkkvicnkfi qtsavtclqw
      121 paeyiivfgl aegkvrlant ktnksstiyg tesyvvsltt ncsgkgilsg hadgtivryf
      181 fddegsgesq gklvnhpcpp yalawatnsi vaagcdrkiv aygkeghmlq tfdysrdpqe
      241 refttavssp ggqsvvlgsy drlrvfnwip rrsiweeakp keitnlytit alawkrdgsr
      301 lcvgtlcggv eqfdcclrrs iyknkfelty vgpsqvivkn lssgtrvvlk shygyeveev
      361 kilgkerylv ahtsetlllg dlntnrlsei awqgsggnek yffenenvcm ifnageltlv
      421 eygnndtlgs vrtefmnphl isvrinercq rgtednkkla ylidiktiai vdliggynig
      481 tvshesrvdw lelnetghkl lfrdrklrwv pgsdvlvaqn rnslcvwyni eapervtmft
      541 irgdvigler gggktevmvm egvttvaytl degliefgta iddgnyirat afletlemtp
      601 eteamwktls klalearqlh iaercfsalg qvakarflhe tneiadqvsr eyggegtdfy
      661 qvrarlamle knyklaemif leqnaveeam gmyqelhrwd eciavaeakg hpaleklrrs
      721 yyqwlmdtqq eeragelqes qgdglaaisl ylkaglpaka arlvltreel lantelvehi
      781 taalikgely eragdlfeki hnpqkalecy rkgnafmkav elarlafpve vvkleeawgd
      841 hlvqqkqlda ainhyiearc sikaieaalg arqwkkaiyi ldlqdrntas kyyplvaqhy
      901 aslqeyeiae elytkgdrtk daidmytqag rweqahklam kcmrpedvsv lyitqaqeme
      961 kqgkyreaer lyvtvqepdl aitmykkhkl yddmirlvgk hhpdllsdth lhlgkeleae
     1021 grlqeaeyhy leaqewkatv nmyrasglwe eayrvartqg ganahkhvay lwakslggea
     1081 avrllnklgl leaavdhaad ncsfefafel srlalkhktp evhlkyamfl edegkfeeae
     1141 aefiragkpk eavlmfvhnq dweaaqrvae ahdpdsvaev lvgqargale ekdfqkaegl
     1201 llraqrpgla lnyykeaglw sdalrickdy vpsqlealqe eyereatkkg argvegfveq
     1261 arhweqagey sravdcylkv rdsgnsglae kcwmkaaels ikflppqrnm evvlavgpql
     1321 igigkhsaaa elylnldlvk eaidafiege ewnkakrvak eldpryedyv dqhykeflkn
     1381 qgkvdslvgv dviaaldlyv eqgqwdkcie tatkqnykil hkyvalyath liregssaqa
     1441 lalyvqhgap anpqnfniyk riftdmvssp gtncaeayhs wadlrdvlfn lcenlvksse
     1501 anspaheefk tmlliahyya trsaaqsvkq letvaarlsv sllrhtqllp vdkafyeagi
     1561 aakavgwdnm afiflnrfld ltdaieegtl dgldhsdfqd tdipfevplp akqhvpeaer
     1621 eevrdwvltv smdqrleqvl prdergayea slvaastgvr alpclitgyp ilrnkiefkr
     1681 pgkaankdnw nkflmaikts hspvcqdvlk fisqwcgglp stsfsfq
//
LOCUS       NP_001397768             893 aa            linear   PRI 21-NOV-2025
DEFINITION  splicing regulator ARVCF isoform 2 [Homo sapiens].
ACCESSION   NP_001397768 XP_047297330
VERSION     NP_001397768.1
DBSOURCE    REFSEQ: accession NM_001410839.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 893)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 893)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 893)
  AUTHORS   Suzuki,N., Idogawa,M., Tange,S., Ohashi,T., Sasaki,Y., Nakase,H.
            and Tokino,T.
  TITLE     p53-induced ARVCF modulates the splicing landscape and supports the
            tumor suppressive function of p53
  JOURNAL   Oncogene 39 (10), 2202-2211 (2020)
   PUBMED   31827232
  REMARK    GeneRIF: p53-induced ARVCF modulates the splicing landscape and
            supports the tumor suppressive function of p53.
REFERENCE   5  (residues 1 to 893)
  AUTHORS   Zhang,D., Tang,N., Liu,Y. and Wang,E.H.
  TITLE     ARVCF expression is significantly correlated with the malignant
            phenotype of non-small cell lung cancer
  JOURNAL   Mol Carcinog 54 Suppl 1, E185-E191 (2015)
   PUBMED   25683624
  REMARK    GeneRIF: observed ARVCF-dependent changes in small GTPase (mainly
            RhoA) activity in lung cancer cells. We confirmed that ARVCF plays
            an important role in the malignant phenotype
REFERENCE   6  (residues 1 to 893)
  AUTHORS   Mariner,D.J., Wang,J. and Reynolds,A.B.
  TITLE     ARVCF localizes to the nucleus and adherens junction and is
            mutually exclusive with p120(ctn) in E-cadherin complexes
  JOURNAL   J Cell Sci 113 (Pt 8), 1481-1490 (2000)
   PUBMED   10725230
REFERENCE   7  (residues 1 to 893)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   8  (residues 1 to 893)
  AUTHORS   Sirotkin,H., Morrow,B., Saint-Jore,B., Puech,A., Das Gupta,R.,
            Patanjali,S.R., Skoultchi,A., Weissman,S.M. and Kucherlapati,R.
  TITLE     Identification, characterization, and precise mapping of a human
            gene encoding a novel membrane-spanning protein from the 22q11
            region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 42 (2), 245-251 (1997)
   PUBMED   9192844
REFERENCE   9  (residues 1 to 893)
  AUTHORS   Sirotkin,H., O'Donnell,H., DasGupta,R., Halford,S., St Jore,B.,
            Puech,A., Parimoo,S., Morrow,B., Skoultchi,A., Weissman,S.M.,
            Scambler,P. and Kucherlapati,R.
  TITLE     Identification of a new human catenin gene family member (ARVCF)
            from the region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 41 (1), 75-83 (1997)
   PUBMED   9126485
REFERENCE   10 (residues 1 to 893)
  AUTHORS   Lindsay,E.A., Goldberg,R., Jurecic,V., Morrow,B., Carlson,C.,
            Kucherlapati,R.S., Shprintzen,R.J. and Baldini,A.
  TITLE     Velo-cardio-facial syndrome: frequency and extent of 22q11
            deletions
  JOURNAL   Am J Med Genet 57 (3), 514-522 (1995)
   PUBMED   7677167
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005663.2.
            
            On Aug 16, 2022 this sequence version replaced XP_047297330.1.
            
            Summary: Armadillo Repeat gene deleted in Velo-Cardio-Facial
            syndrome (ARVCF) is a member of the catenin family. This family
            plays an important role in the formation of adherens junction
            complexes, which are thought to facilitate communication between
            the inside and outside environments of a cell. The ARVCF gene was
            isolated in the search for the genetic defect responsible for the
            autosomal dominant Velo-Cardio-Facial syndrome (VCFS), a relatively
            common human disorder with phenotypic features including cleft
            palate, conotruncal heart defects and facial dysmorphology. The
            ARVCF gene encodes a protein containing two motifs, a coiled coil
            domain in the N-terminus and a 10 armadillo repeat sequence in the
            midregion. Since these sequences can facilitate protein-protein
            interactions ARVCF is thought to function in a protein complex. In
            addition, ARVCF contains a predicted nuclear-targeting sequence
            suggesting that it may have a function as a nuclear protein.
            [provided by RefSeq, Jun 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2721477.1,
                                           SRR14372080.3145931.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..893
                     /product="splicing regulator ARVCF isoform 2"
                     /note="armadillo repeat protein deleted in
                     velo-cardio-facial syndrome; armadillo repeat gene deleted
                     in velocardiofacial syndrome; splicing regulator ARVCF"
                     /calculated_mol_wt=96697
     Region          297..322
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(313,317,321,355,359,363,398,403,407)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          326..365
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          330..366
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          369..410
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          373..408
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          415..466
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          587..623
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          587..623
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          633..668
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          633..667
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          674..719
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          725..757
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     CDS             1..893
                     /gene="ARVCF"
                     /coded_by="NM_001410839.1:104..2785"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS93120.1"
                     /db_xref="GeneID:421"
                     /db_xref="HGNC:HGNC:728"
                     /db_xref="MIM:602269"
ORIGIN      
        1 mpaelrqeqs pgsqaslatm peapdvleet vtveedpgtp tshvsivtse dgttrrtetk
       61 vtktvktvtt rtvrqvpvgp dglplldggp plgpfadgal drhfllrggg pvatlsrayl
      121 ssgggfpegp eprdspsygs lsrglgmrpp ragplgpgpg dgcftlpghr eafpvgpepg
      181 ppggrslper fqaepygled dtrslaadde ggpelepdyg tatrrrpecg rglhtrayed
      241 taddggelad erpafpmvta plaqpergsm gsldrlvrrs psvdsarkep rwrdpelpev
      301 lamlrhpvdp vkanaaaylq hlcfenegvk rrvrqlrglp llvalldhpr aevrrracga
      361 lrnlsygrdt dnkaairdcg gvpalvrllr aardnevrel vtgtlwnlss yeplkmviid
      421 hglqtlthev ivphsgwere pnedskprda ewttvfknts gclrnvssdg aearrrlrec
      481 eglvdallha lqsavgrkdt dnksvencvc imrnlsyhvh kevpgadryq eaepgplgsa
      541 vgsqrrrrdd ascfggkkak gkkdgemdrn fdtldlpkrt eaakgfelly qpevvrlyls
      601 lltesrnfnt leaaagalqn lsagnwmwat yiratvrker glpvlvellq setdkvvrav
      661 aialrnlsld rrnkdligsy amaelvrnvr naqapprpga cleedtvvav lntiheivsd
      721 sldnarsllq argvpalval vassqsvrea kaashvlqtv wsykelrgtl qkdgwtkarf
      781 qsaaatakgp kgalspggfd dstlplvdks legektgsrd vipmdalgpd gystvdrrer
      841 rprgassage asekeplkld psrkapppgp srpavrlvda vgdakpqpvd swv
//
LOCUS       NP_001401589             520 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 2 isoform e [Homo sapiens].
ACCESSION   NP_001401589 XP_011536702
VERSION     NP_001401589.1
DBSOURCE    REFSEQ: accession NM_001414660.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Jung,J.H., Lee,D., Ko,H.M. and Jang,H.J.
  TITLE     Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in Colorectal
            Cancer Cells by Activating p53
  JOURNAL   Biomolecules 11 (10), 1492 (2021)
   PUBMED   34680125
  REMARK    GeneRIF: Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in
            Colorectal Cancer Cells by Activating p53.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Royer-Bertrand,B., Cisarova,K., Niel Butschi,F., Foletti,G.,
            Guinchat,V., Tran,C., Superti-Furga,A. and Good,J.M.
  TITLE     CNOT2 haploinsufficiency in a 40-year-old man with intellectual
            disability, autism, and seizures
  JOURNAL   Am J Med Genet A 185 (8), 2602-2606 (2021)
   PUBMED   34018673
  REMARK    GeneRIF: CNOT2 haploinsufficiency in a 40-year-old man with
            intellectual disability, autism, and seizures.
            Review article
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Jayne,S., Zwartjes,C.G., van Schaik,F.M. and Timmers,H.T.
  TITLE     Involvement of the SMRT/NCoR-HDAC3 complex in transcriptional
            repression by the CNOT2 subunit of the human Ccr4-Not complex
  JOURNAL   Biochem J 398 (3), 461-467 (2006)
   PUBMED   16712523
  REMARK    GeneRIF: This study shows that SMRT/NCoR-HDAC3 complex is a
            cofactor of CNOT2-mediated repression and suggests that
            transcriptional regulation by the Ccr4-Not complex involves
            regulation of chromatin modification.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Winkler,G.S., Mulder,K.W., Bardwell,V.J., Kalkhoven,E. and
            Timmers,H.T.
  TITLE     Human Ccr4-Not complex is a ligand-dependent repressor of nuclear
            receptor-mediated transcription
  JOURNAL   EMBO J 25 (13), 3089-3099 (2006)
   PUBMED   16778766
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Shi,J. and Nelson,M.A.
  TITLE     The cyclin-dependent kinase 11 interacts with NOT2
  JOURNAL   Biochem Biophys Res Commun 334 (4), 1310-1316 (2005)
   PUBMED   16039607
  REMARK    GeneRIF: These findings suggest that CDK11 may contribute to
            apoptosis by regulating the activity of NOT2 independent of its
            kinase activity.
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Zwartjes,C.G., Jayne,S., van den Berg,D.L. and Timmers,H.T.
  TITLE     Repression of promoter activity by CNOT2, a subunit of the
            transcription regulatory Ccr4-not complex
  JOURNAL   J Biol Chem 279 (12), 10848-10854 (2004)
   PUBMED   14707134
  REMARK    GeneRIF: major repression function of CNOT2 is localized in a
            specialized protein motif, the Not-Box
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Denis,C.L. and Chen,J.
  TITLE     The CCR4-NOT complex plays diverse roles in mRNA metabolism
  JOURNAL   Prog Nucleic Acid Res Mol Biol 73, 221-250 (2003)
   PUBMED   12882519
  REMARK    Review article
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092881.8 and AC025569.37.
            
            On Feb 21, 2023 this sequence version replaced XP_011536702.1.
            
            Summary: This gene encodes a subunit of the multi-component
            CCR4-NOT complex. The CCR4-NOT complex regulates mRNA synthesis and
            degradation and is also thought to be involved in mRNA splicing,
            transport and localization. The encoded protein interacts with
            histone deacetylases and functions as a repressor of polymerase II
            transcription. Alternatively spliced transcript variants have been
            observed for this gene. [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1841942.1,
                                           SRR14038192.4048380.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..520
                     /product="CCR4-NOT transcription complex subunit 2 isoform
                     e"
                     /note="negative regulator of transcription 2;
                     CCR4-associated factor 2; CC chemokine receptor 4-negative
                     regulator of transcription 2"
                     /calculated_mol_wt=57288
     Region          376..499
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..520
                     /gene="CNOT2"
                     /gene_synonym="CDC36; HSPC131; IDNADFS; NOT2; NOT2H"
                     /coded_by="NM_001414660.1:391..1953"
                     /note="isoform e is encoded by transcript variant 14"
                     /db_xref="GeneID:4848"
                     /db_xref="HGNC:HGNC:7878"
                     /db_xref="MIM:604909"
ORIGIN      
        1 mfgasrkkfv egvdsdyhde nmyysqssmf phrsekdmla spstsgqlsq fgaslygqqs
       61 alglpmrgms nntpqlnrsl sqgtqlpshv tpttgvptms lhtppspsrg ilpmnprnmm
      121 nhsqvgqgig ipsrtnsmss sglgspnrss psiicmpkqq psrqpftvns msgfgmnrnq
      181 afgmnnslss nifngtdgse nvtgldlsdf paladrnrre gsgnptplin plagrapyvg
      241 mvtkpaneqs qdfsihnedf palpgssykd ptssnddsks nlntsgktts stdgpkfpgd
      301 kssttqnnnq qkkgiqvlpd grvtnipqgm vtdqfgmigl ltfiraaetd pgmvhlalgs
      361 dlttlglnln spenlypkfa spwasspcrp qdidfhvpse yltnihirdk laaiklgryg
      421 edllfylyym nggdvlqlla avelfnrdwr yhkeervwit rapgmeptmk tntyergtyy
      481 ffdclnwrkv akefhleydk leerphlpst fnynpaqqaf
//
LOCUS       NP_001403223             754 aa            linear   PRI 21-NOV-2025
DEFINITION  oxysterol-binding protein-related protein 9 isoform j [Homo
            sapiens].
ACCESSION   NP_001403223
VERSION     NP_001403223.1
DBSOURCE    REFSEQ: accession NM_001416294.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Cabukusta,B., Borst Pauwels,S., Akkermans,J.J.L.L., Blomberg,N.,
            Mulder,A.A., Koning,R.I., Giera,M. and Neefjes,J.
  TITLE     The ORP9-ORP11 dimer promotes sphingomyelin synthesis
  JOURNAL   Elife 12, 91345 (2024)
   PUBMED   39106189
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 754)
  AUTHORS   He,R., Liu,F., Wang,H., Huang,S., Xu,K., Zhang,C., Liu,Y. and Yu,H.
  TITLE     ORP9 and ORP10 form a heterocomplex to transfer
            phosphatidylinositol 4-phosphate at ER-TGN contact sites
  JOURNAL   Cell Mol Life Sci 80 (3), 77 (2023)
   PUBMED   36853333
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Tan,J.X. and Finkel,T.
  TITLE     A phosphoinositide signalling pathway mediates rapid lysosomal
            repair
  JOURNAL   Nature 609 (7928), 815-821 (2022)
   PUBMED   36071159
REFERENCE   4  (residues 1 to 754)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 754)
  AUTHORS   Hacker,B., Schultheiss,C., Doring,M. and Kurzik-Dumke,U.
  TITLE     Molecular partners of hNOT/ALG3, the human counterpart of the
            Drosophila NOT and yeast ALG3 gene, suggest its involvement in
            distinct cellular processes relevant to congenital disorders of
            glycosylation, cancer, neurodegeneration and a variety of further
            pathologies
  JOURNAL   Hum Mol Genet 27 (11), 1858-1878 (2018)
   PUBMED   29547901
REFERENCE   6  (residues 1 to 754)
  AUTHORS   Gauci,S., Helbig,A.O., Slijper,M., Krijgsveld,J., Heck,A.J. and
            Mohammed,S.
  TITLE     Lys-N and trypsin cover complementary parts of the phosphoproteome
            in a refined SCX-based approach
  JOURNAL   Anal Chem 81 (11), 4493-4501 (2009)
   PUBMED   19413330
  REMARK    GeneRIF: Includes data showing N-alpha terminal acetylation of this
            protein (OSBL9_HUMAN), which begins with nASIMEGPLSK following
            cleavage of the initiating Met-1 residue.
REFERENCE   7  (residues 1 to 754)
  AUTHORS   Lessmann,E., Ngo,M., Leitges,M., Minguet,S., Ridgway,N.D. and
            Huber,M.
  TITLE     Oxysterol-binding protein-related protein (ORP) 9 is a PDK-2
            substrate and regulates Akt phosphorylation
  JOURNAL   Cell Signal 19 (2), 384-392 (2007)
   PUBMED   16962287
  REMARK    GeneRIF: Furthermore, mammalian target of rapamycin was implicated
            in ORP9L phosphorylation in HEK293 cells. These studies identify
            ORP9 as a PDK-2 substrate and negative regulator of Akt
            phosphorylation at the PDK-2 site.
REFERENCE   8  (residues 1 to 754)
  AUTHORS   Wyles,J.P. and Ridgway,N.D.
  TITLE     VAMP-associated protein-A regulates partitioning of
            oxysterol-binding protein-related protein-9 between the endoplasmic
            reticulum and Golgi apparatus
  JOURNAL   Exp Cell Res 297 (2), 533-547 (2004)
   PUBMED   15212954
REFERENCE   9  (residues 1 to 754)
  AUTHORS   Jaworski,C.J., Moreira,E., Li,A., Lee,R. and Rodriguez,I.R.
  TITLE     A family of 12 human genes containing oxysterol-binding domains
  JOURNAL   Genomics 78 (3), 185-196 (2001)
   PUBMED   11735225
REFERENCE   10 (residues 1 to 754)
  AUTHORS   Lehto,M., Laitinen,S., Chinetti,G., Johansson,M., Ehnholm,C.,
            Staels,B., Ikonen,E. and Olkkonen,V.M.
  TITLE     The OSBP-related protein family in humans
  JOURNAL   J Lipid Res 42 (8), 1203-1213 (2001)
   PUBMED   11483621
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104170.2, AL772260.3,
            AL831767.8 and AL050343.17.
            
            Summary: This gene encodes a member of the oxysterol-binding
            protein (OSBP) family, a group of intracellular lipid receptors.
            Most members contain an N-terminal pleckstrin homology domain and a
            highly conserved C-terminal OSBP-like sterol-binding domain,
            although some members contain only the sterol-binding domain. This
            family member functions as a cholesterol transfer protein that
            regulates Golgi structure and function. Multiple transcript
            variants, most of which encode distinct isoforms, have been
            identified. Related pseudogenes have been identified on chromosomes
            3, 11 and 12. [provided by RefSeq, Jul 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2154228.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..754
                     /product="oxysterol-binding protein-related protein 9
                     isoform j"
                     /note="oxysterol-binding protein-related protein 9;
                     OSBP-related protein 9"
                     /calculated_mol_wt=85052
     Region          23..124
                     /region_name="PH_ORP9"
                     /note="Human Oxysterol binding protein related protein 9
                     Pleckstrin homology (PH) domain; cd13290"
                     /db_xref="CDD:241444"
     Region          395..741
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     CDS             1..754
                     /gene="OSBPL9"
                     /gene_synonym="ORP-9; ORP9"
                     /coded_by="NM_001416294.1:756..3020"
                     /note="isoform j is encoded by transcript variant 15"
                     /db_xref="GeneID:114883"
                     /db_xref="HGNC:HGNC:16386"
                     /db_xref="MIM:606737"
ORIGIN      
        1 mpyrrvtsgr llslaapkma simegplskw tnvmkgwqyr wfvldynagl lsyytskdkm
       61 mrgsrrgcvr lrgavigidd eddstftitv dqktfhfqar daderekwih aleetilrht
      121 lqlqgldsgf vpsvqdfdkk lteadaylqi lieqlklfdd klqnckedeq rkkietlket
      181 tnsmvesikh civllqiakd qsnaekhadg mistinpvda iyqpsplepv istmpsqtvl
      241 ppepvqlcks eqrpsslpvg pvlatlghhq tptpnstgsg hsppssslts pshvnlspnt
      301 vpefsyssse defydadefh qsgsspkrli dssgsasvlt hsssgnslkr pdtteslnss
      361 lsngtsdadl fdshddrddd aeagsveehk svimhllsqv rlgmdltkvv lptfilerrs
      421 llemyadffa hpdlfvsisd qkdpkdrmvq vvkwylsafh agrkgsvakk pynpilgeif
      481 qchwtlpndt eentelvseg pvpwvsknsv tfvaeqvshh ppisafyaec fnkkiqfnah
      541 iwtkskflgm sigvhnigqg cvscldydeh yiltfpngyg rsiltvpwve lggecnincs
      601 ktgysaniif htkpfyggkk hritaeifsp ndkksfcsie gewngvmyak yatgentvfv
      661 dtkklpiikk kvrkledqne yesrslwkdv tfnlkirdid aateakhrle erqraearer
      721 kekeiqwetr lfhedgecwv ydepllkrlg aakh
//
LOCUS       NP_001392784            1105 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001392784
VERSION     NP_001392784.1
DBSOURCE    REFSEQ: accession NM_001405855.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1105)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1105)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1105)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1105)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1105)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1105)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1105)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1652571.1,
                                           SRR18074969.2634780.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1105
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 1"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=120835
     Site            104
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          145..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          225..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          399..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          733..857
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          850..882
                     /region_name="Required for activation of KAT8 histone
                     acetyltransferase activity"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          885..1005
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     Region          910..928
                     /region_name="Interaction with KAT8 HAT domain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01397"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          938..1034
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            991
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            994
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            1003
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            1045
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          1058..1105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     CDS             1..1105
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405855.1:391..3708"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankgli
      481 vlgevpppeh ttdlflplss evktdhgtdk liesvsqple nhgapiighi seslstkscg
      541 alrpvngvin tlqpvladhi pgdssdaeeq lhkkqrlnlv ssssdgtcva artrpvlsck
      601 krrlvrpnsi vplskkvhrn stirpgcdvn pscalcgsgs intmppeihy eapllerlsq
      661 ldscvhpvla fpddvptslh fqsmlksqwq nkpfdkikpp kklslkhrap mpgslpdsar
      721 kdrhklvssf lttaklshhq trpdrthrqh lddvgavpmv ervtapkaer llnppppvhd
      781 pnhskmrlrd hssersevlk hhtdmssssy laathhpphs plvrqlstss dspapassss
      841 qvtastsqqp vrrrrgessf dinnivipms vaattrvekl qykeiltpsw revdlqslkg
      901 spdeeneeie dlsdaafaal hakceemera rwlwttsvpp qrrgsrsyrs sdgrttpqlg
      961 sanpstpqpa spdvssshsl seyshgqspr spispelhsa pltpvardtp rhlasedtrc
     1021 stpelgldeq svqpwerrtf plahspqaec edqldaqera arctrrtsgs ktgreteaap
     1081 tsppivplks rhlvaaataq rpthr
//
LOCUS       NP_001400606             203 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 10 [Homo sapiens].
ACCESSION   NP_001400606
VERSION     NP_001400606.1
DBSOURCE    REFSEQ: accession NM_001413677.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 203)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 203)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 203)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 203)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 203)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 203)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.2974711.1,
                                           SRR14038192.1979619.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..203
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 10"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=22645
     Region          <1..198
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     CDS             1..203
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413677.1:483..1094"
                     /note="isoform 10 is encoded by transcript variant 13"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mnsaptfmhf ppkgrpkrad tfdlqrigfa aeqlakwiad rtdvhirvfr ppnysgtial
       61 allvslvggl lylrrnnlef iynktgwamv slcivfamts gqmwnhirgp pyahknphng
      121 qvsyihgssq aqfvaeshii lvlnaaitmg mvllneaats kgdvgkrrii clvglglvvf
      181 ffsfllsifr skyhgypysf lik
//
LOCUS       NP_001397812             650 aa            linear   PRI 21-NOV-2025
DEFINITION  ran-binding protein 10 isoform 5 [Homo sapiens].
ACCESSION   NP_001397812 XP_005256127
VERSION     NP_001397812.1
DBSOURCE    REFSEQ: accession NM_001410883.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 650)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 650)
  AUTHORS   Maitland,M.E.R., Lajoie,G.A., Shaw,G.S. and Schild-Poulter,C.
  TITLE     Structural and Functional Insights into GID/CTLH E3 Ligase
            Complexes
  JOURNAL   Int J Mol Sci 23 (11), 5863 (2022)
   PUBMED   35682545
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 650)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 650)
  AUTHORS   Hou,J., Liu,Y., Huang,P., Wang,Y., Pei,D., Tan,R., Zhang,Y. and
            Cui,H.
  TITLE     RANBP10 promotes glioblastoma progression by regulating the
            FBXW7/c-Myc pathway
  JOURNAL   Cell Death Dis 12 (11), 967 (2021)
   PUBMED   34671019
  REMARK    GeneRIF: RANBP10 promotes glioblastoma progression by regulating
            the FBXW7/c-Myc pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 650)
  AUTHORS   Lai,K.Y., Rizzato,M., Aydin,I., Villalonga-Planells,R.,
            Drexler,H.C.A. and Schelhaas,M.
  TITLE     A Ran-binding protein facilitates nuclear import of human
            papillomavirus type 16
  JOURNAL   PLoS Pathog 17 (5), e1009580 (2021)
   PUBMED   33974675
  REMARK    GeneRIF: A Ran-binding protein facilitates nuclear import of human
            papillomavirus type 16.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 650)
  AUTHORS   Hosono,K., Noda,S., Shimizu,A., Nakanishi,N., Ohtsubo,M.,
            Shimizu,N. and Minoshima,S.
  TITLE     YPEL5 protein of the YPEL gene family is involved in the cell cycle
            progression by interacting with two distinct proteins RanBPM and
            RanBP10
  JOURNAL   Genomics 96 (2), 102-111 (2010)
   PUBMED   20580816
REFERENCE   7  (residues 1 to 650)
  AUTHORS   Rex,E.B., Rankin,M.L., Yang,Y., Lu,Q., Gerfen,C.R., Jose,P.A. and
            Sibley,D.R.
  TITLE     Identification of RanBP 9/10 as interacting partners for protein
            kinase C (PKC) gamma/delta and the D1 dopamine receptor: regulation
            of PKC-mediated receptor phosphorylation
  JOURNAL   Mol Pharmacol 78 (1), 69-80 (2010)
   PUBMED   20395553
  REMARK    GeneRIF: data support the idea that RanBP9 and RanBP10 may function
            as signaling integrators and dictate the efficient regulation of
            D(1) receptor signaling by PKCdelta and PKCgamma
REFERENCE   8  (residues 1 to 650)
  AUTHORS   Schulze,H., Dose,M., Korpal,M., Meyer,I., Italiano,J.E. Jr. and
            Shivdasani,R.A.
  TITLE     RanBP10 is a cytoplasmic guanine nucleotide exchange factor that
            modulates noncentrosomal microtubules
  JOURNAL   J Biol Chem 283 (20), 14109-14119 (2008)
   PUBMED   18347012
  REMARK    GeneRIF: RanBP10 might serve as a molecular link between Ran and
            noncentrosomal microtubules
REFERENCE   9  (residues 1 to 650)
  AUTHORS   Woo,J.S., Imm,J.H., Min,C.K., Kim,K.J., Cha,S.S. and Oh,B.H.
  TITLE     Structural and functional insights into the B30.2/SPRY domain
  JOURNAL   EMBO J 25 (6), 1353-1363 (2006)
   PUBMED   16498413
REFERENCE   10 (residues 1 to 650)
  AUTHORS   Wang,D., Li,Z., Schoen,S.R., Messing,E.M. and Wu,G.
  TITLE     A novel MET-interacting protein shares high sequence similarity
            with RanBPM, but fails to stimulate MET-induced Ras/Erk signaling
  JOURNAL   Biochem Biophys Res Commun 313 (2), 320-326 (2004)
   PUBMED   14684163
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC040162.5 and AC010530.8.
            
            On Aug 17, 2022 this sequence version replaced XP_005256127.1.
            
            Summary: RAN is a small GTPase involved in the assembly of
            microtubules to form mitotic spindles. The protein encoded by this
            gene is a cytoplasmic guanine nucleotide exchange factor (GEF) that
            binds beta-tubulin and has GEF activity toward RAN. The encoded
            protein plays a role in the formation of noncentrosomal
            microtubules. In addition, this protein may be involved in the
            regulation of D(1) receptor signaling by protein kinase C delta and
            protein kinase C gamma. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Feb 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.12769.1,
                                           SRR11853561.11458.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..650
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..650
                     /product="ran-binding protein 10 isoform 5"
                     /note="Ran-binding protein 10"
                     /calculated_mol_wt=70354
     Region          77..219
                     /region_name="SPRY_RanBP9_10"
                     /note="SPRY domain in Ran binding proteins 9 and 10;
                     cd12909"
                     /db_xref="CDD:293966"
     Region          257..284
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          291..>345
                     /region_name="CTLH"
                     /note="CTLH/CRA C-terminal to LisH motif domain;
                     pfam10607"
                     /db_xref="CDD:402305"
     Region          537..634
                     /region_name="CRA"
                     /note="CT11-RanBPM; smart00757"
                     /db_xref="CDD:214806"
     CDS             1..650
                     /gene="RANBP10"
                     /coded_by="NM_001410883.1:25..1977"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS92180.1"
                     /db_xref="GeneID:57610"
                     /db_xref="HGNC:HGNC:29285"
                     /db_xref="MIM:614031"
ORIGIN      
        1 maaatadpga gnpqpgdssg ggaggglpsp geqelsrrlq rlypavnqqe tplprswspk
       61 dkynyiglsq gnlrvhykgh gknhkdaasv rathpipaac giyyfevkiv skgrdgymgi
      121 glsaqgvnmn rlpgwdkhsy gyhgddghsf cssgtgqpyg ptfttgdvig ccvnlingtc
      181 fytknghslg iaftdlpanl yptvglqtpg eivdanfgqq pflfdiedym rewrakvqgt
      241 vhcfpisarl gewqavlqnm vssylvhhgy catatafarm tetpiqeeqa siknrqkiqk
      301 lvlegrvgea iettqrfypg llehnpnllf mlkcrqfvem vngtdsevrs lssrspksqd
      361 sypgspslsp rhgpssshmh ntgadspscs ngvastkskq nhskypapss ssssssssss
      421 sspssvnyse snstdstksq hhsstsnqet snpwlqlerr pnqaapttpp gptptstpph
      481 sdsememeae hypngvlgsm strivngayk hedlqtdess mddrhprrql cggnqaater
      541 iilfgrelqa lseqlgreyg knlahtemlq dafsllaysd pwscpvgqql dpiqrepvca
      601 alnsailesq nlpkqpplml algqaseclr lmaraglgsc sfarvddylh
//
LOCUS       NP_001397986             309 aa            linear   PRI 21-NOV-2025
DEFINITION  glucose-induced degradation protein 4 homolog isoform 2 [Homo
            sapiens].
ACCESSION   NP_001397986 XP_005256856
VERSION     NP_001397986.1
DBSOURCE    REFSEQ: accession NM_001411057.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Bagci,H., Winkler,M., Gradel,B., Uliana,F., Boulais,J.,
            Mohamed,W.I., Park,S.L., Cote,J.F., Pertz,O. and Peter,M.
  TITLE     The hGIDGID4 E3 ubiquitin ligase complex targets ARHGAP11A to
            regulate cell migration
  JOURNAL   Life Sci Alliance 7 (12), e202403046 (2024)
   PUBMED   39389782
  REMARK    GeneRIF: The hGID[GID4] E3 ubiquitin ligase complex targets
            ARHGAP11A to regulate cell migration.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Maitland,M.E.R., Lajoie,G.A., Shaw,G.S. and Schild-Poulter,C.
  TITLE     Structural and Functional Insights into GID/CTLH E3 Ligase
            Complexes
  JOURNAL   Int J Mol Sci 23 (11), 5863 (2022)
   PUBMED   35682545
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 309)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   9  (residues 1 to 309)
  AUTHORS   Bi,W., Yan,J., Stankiewicz,P., Park,S.S., Walz,K., Boerkoel,C.F.,
            Potocki,L., Shaffer,L.G., Devriendt,K., Nowaczyk,M.J., Inoue,K. and
            Lupski,J.R.
  TITLE     Genes in a refined Smith-Magenis syndrome critical deletion
            interval on chromosome 17p11.2 and the syntenic region of the mouse
  JOURNAL   Genome Res 12 (5), 713-728 (2002)
   PUBMED   11997338
REFERENCE   10 (residues 1 to 309)
  AUTHORS   Lucas,R.E., Vlangos,C.N., Das,P., Patel,P.I. and Elsea,S.H.
  TITLE     Genomic organisation of the approximately 1.5 Mb Smith-Magenis
            syndrome critical interval: transcription map, genomic contig, and
            candidate gene analysis
  JOURNAL   Eur J Hum Genet 9 (12), 892-902 (2001)
   PUBMED   11840190
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC087164.9.
            
            On Aug 20, 2022 this sequence version replaced XP_005256856.1.
            
            Summary: The multiprotein Mediator complex is a coactivator
            required for activation of RNA polymerase II transcription by DNA
            bound transcription factors. The protein encoded by this gene is
            thought to be a subunit of the Mediator complex. This gene is
            located within the Smith-Magenis syndrome region on chromosome 17.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.217561.1,
                                           SRR14038193.425304.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..309
                     /product="glucose-induced degradation protein 4 homolog
                     isoform 2"
                     /note="vacuolar import and degradation 24; vacuolar import
                     and degradation protein 24 homolog; glucose-induced
                     degradation protein 4 homolog; GID complex subunit 4,
                     VID24 homolog"
                     /calculated_mol_wt=34239
     Region          121..>202
                     /region_name="Vac_ImportDeg"
                     /note="Vacuolar import and degradation protein; pfam09783"
                     /db_xref="CDD:462897"
     CDS             1..309
                     /gene="GID4"
                     /gene_synonym="C17orf39; VID2; VID24"
                     /coded_by="NM_001411057.1:58..987"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS92267.1"
                     /db_xref="GeneID:79018"
                     /db_xref="HGNC:HGNC:28453"
                     /db_xref="MIM:617699"
ORIGIN      
        1 mcargqvgrg tqlrtgrpcs qvpgsrwrpe rllrrqragg rpsrphpara rpglslpatl
       61 lgsraaaavp lplppalapg dpampvrtec pppagasaas aaslippppi ntqqpgvats
      121 llysgskfrg hqkskgnsyd vevvlqhvdt gnsylcgylk ikglteeypt lttffegeii
      181 skkhpfltrk wdadedvdrk hwnigryldl qtlldwtetf wvreelrrpp lvlacevwls
      241 qgaepmecfl lqqfvaafvv lsispnfhhs wrtprfprgt pgalyctwvc lrftmsntlh
      301 lgchffiin
//
LOCUS       NP_001389618            1328 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 7 [Homo sapiens].
ACCESSION   NP_001389618
VERSION     NP_001389618.1
DBSOURCE    REFSEQ: accession NM_001402689.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1328)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1328)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1328)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1328)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1328)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1328)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1328)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1328)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1328)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1328)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038193.173341.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2146236, SAMEA2159607 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1328
                     /product="kinectin isoform 7"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=152768
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          316..>532
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          448..1268
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1328
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402689.1:299..4285"
                     /note="isoform 7 is encoded by transcript variant 14"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqdlkqeika
      841 lkeeignvql ekaqqlsits kvqelqnllk gkeeqmntmk avleekekdl antgkwlqdl
      901 qeeneslkah vqevaqhnlk eassasqfee leivlkeken elkrleamlk eresdlsskt
      961 qllqdvqden klfksqieql kqqnyqqass fppheellkv iserekeisg lwneldslkd
     1021 avehqrkknn erqqqveave leakevlkkl fpkvsvpsnl sygewlhgfe kkakecmagt
     1081 sgseevkvle hklkeademh tllqleceky ksvlaetegi lqklqrsveq eenkwkvkvd
     1141 eshktikqmq ssftsseqel erlrsenkdi enlrrerehl emelekaeme rstyvtevre
     1201 lkdlltelqk klddsyseav rqneelnllk aqlnetltkl rteqnerqkv agdlhkaqqs
     1261 leliqskivk aagdttvien sdvspetess eketmsvsln qtvtqlqqll qavnqqltke
     1321 kehyqvle
//
LOCUS       NP_001427689            1248 aa            linear   PRI 21-NOV-2025
DEFINITION  collagen alpha-6(IV) chain isoform 7 precursor [Homo sapiens].
ACCESSION   NP_001427689 XP_047297773 XP_054182424
VERSION     NP_001427689.1
DBSOURCE    REFSEQ: accession NM_001440760.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1248)
  AUTHORS   O'Brien,A., Aw,W.Y., Tee,H.Y., Naegeli,K.M., Bademci,G., Tekin,M.,
            Arnos,K. and Pandya,A.
  TITLE     Confirmation of COL4A6 variants in X-linked nonsyndromic hearing
            loss and its clinical implications
  JOURNAL   Eur J Hum Genet 30 (1), 7-12 (2022)
   PUBMED   33840813
  REMARK    GeneRIF: Confirmation of COL4A6 variants in X-linked nonsyndromic
            hearing loss and its clinical implications.
REFERENCE   2  (residues 1 to 1248)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 1248)
  AUTHORS   Komori,T., Ono,M., Hara,E.S., Ueda,J., Nguyen,H.T.T., Nguyen,H.T.,
            Yonezawa,T., Maeba,T., Kimura-Ono,A., Takarada,T., Momota,R.,
            Maekawa,K., Kuboki,T. and Oohashi,T.
  TITLE     Type IV collagen alpha6 chain is a regulator of keratin 10 in
            keratinization of oral mucosal epithelium
  JOURNAL   Sci Rep 8 (1), 2612 (2018)
   PUBMED   29422532
  REMARK    GeneRIF: These findings indicate that alpha112:alpha556 (IV)
            network, which is the only network that includes the alpha6(IV)
            chain, is one regulator of KRT10 expression in keratinization of
            oral mucosal epithelium.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1248)
  AUTHORS   Holmes,D.F., Lu,Y., Starborg,T. and Kadler,K.E.
  TITLE     Collagen Fibril Assembly and Function
  JOURNAL   Curr Top Dev Biol 130, 107-142 (2018)
   PUBMED   29853175
  REMARK    Review article
REFERENCE   5  (residues 1 to 1248)
  AUTHORS   Naba,A., Pearce,O.M.T., Del Rosario,A., Ma,D., Ding,H., Rajeeve,V.,
            Cutillas,P.R., Balkwill,F.R. and Hynes,R.O.
  TITLE     Characterization of the Extracellular Matrix of Normal and Diseased
            Tissues Using Proteomics
  JOURNAL   J Proteome Res 16 (8), 3083-3091 (2017)
   PUBMED   28675934
REFERENCE   6  (residues 1 to 1248)
  AUTHORS   Ghebrehiwet,B., Peerschke,E.I., Hong,Y., Munoz,P. and Gorevic,P.D.
  TITLE     Short amino acid sequences derived from C1q receptor (C1q-R) show
            homology with the alpha chains of fibronectin and vitronectin
            receptors and collagen type IV
  JOURNAL   J Leukoc Biol 51 (6), 546-556 (1992)
   PUBMED   1377218
REFERENCE   7  (residues 1 to 1248)
  AUTHORS   Gupta,S., Batchu,R.B. and Datta,K.
  TITLE     Purification, partial characterization of rat kidney hyaluronic
            acid binding protein and its localization on the cell surface
  JOURNAL   Eur J Cell Biol 56 (1), 58-67 (1991)
   PUBMED   1724753
REFERENCE   8  (residues 1 to 1248)
  AUTHORS   Hernandez,M.R., Igoe,F. and Neufeld,A.H.
  TITLE     Extracellular matrix of the human optic nerve head
  JOURNAL   Am J Ophthalmol 102 (2), 139-148 (1986)
   PUBMED   2426947
REFERENCE   9  (residues 1 to 1248)
  AUTHORS   Glant,T.T., Hadhazy,C., Mikecz,K. and Sipos,A.
  TITLE     Appearance and persistence of fibronectin in cartilage. Specific
            interaction of fibronectin with collagen type II
  JOURNAL   Histochemistry 82 (2), 149-158 (1985)
   PUBMED   3997552
REFERENCE   10 (residues 1 to 1248)
  AUTHORS   Matsubara,T., Trueb,B., Fehr,K., Ruttner,J.R. and Odermatt,B.F.
  TITLE     The localization and secretion of type IV collagen in synovial
            capillaries by immunohistochemistry using a monoclonal antibody
            against human type IV collagen
  JOURNAL   Exp Cell Biol 52 (3), 159-169 (1984)
   PUBMED   6386565
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL034369.1, AL109943.18,
            AL136080.6 and AL031177.1.
            
            On or before May 28, 2025 this sequence version replaced
            XP_047297773.1, XP_054182424.1.
            
            Summary: This gene encodes one of the six subunits of type IV
            collagen, the major structural component of basement membranes.
            Like the other members of the type IV collagen gene family, this
            gene is organized in a head-to-head conformation with another type
            IV collagen gene, alpha 5 type IV collagen, so that the gene pair
            shares a common promoter. Deletions in the alpha 5 gene that extend
            into the alpha 6 gene result in diffuse leiomyomatosis accompanying
            the X-linked Alport syndrome caused by the deletion in the alpha 5
            gene. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.278505.1,
                                           SRR14038193.629678.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.3"
     Protein         1..1248
                     /product="collagen alpha-6(IV) chain isoform 7 precursor"
                     /note="collagen of basement membrane, alpha-6; collagen
                     IV, alpha-6 polypeptide; collagen alpha-6(IV) chain;
                     dJ889N15.4 (Collagen Alpha 6(IV)); collagen, type IV,
                     alpha 6"
                     /calculated_mol_wt=116486
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2295
     Region          <44..374
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <296..>547
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <515..>750
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <638..>871
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          891..946
                     /region_name="Collagen"
                     /note="Collagen triple helix repeat (20 copies);
                     pfam01391"
                     /db_xref="CDD:460189"
     Region          <926..>1164
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     CDS             1..1248
                     /gene="COL4A6"
                     /gene_synonym="CXDELq22.3; DELXq22.3; DFNX6"
                     /coded_by="NM_001440760.1:227..3973"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:1288"
                     /db_xref="HGNC:HGNC:2208"
                     /db_xref="MIM:303631"
ORIGIN      
        1 mhpglwlllv tlclteelaa ageksygkpc ggqdcsgscq cfpekgargr pgpigiqgpt
       61 gpqgftgstg lsglkgergf pgllgpygpk gdkgpmgvpg flgingipgh pgqpgprgpp
      121 gldgcngtqg avgfpgpdgy pgllgppglp gqkgskgdpv lapgsfkgmk gdpglpgldg
      181 itgpqgapgf pgavgpagpp glqgppgppg plgpdgnmgl gfqgekgvkg dvglpgpagp
      241 ppstgelefm gfpkgkkgsk gepgpkgfpg isgppgfpgl gttgekgekg ekgipglpgp
      301 rgpmgsegvq gppgqqgkkg tlgfpglngf qgiegqkgdi glpgpdvfid idgavisgnp
      361 gdpgvpglpg lkgdegiqgl rgpsgvpglp alsgvpgalg pqgfpglkgd qgnpgrttig
      421 aaglpgrdgl pgppgppgpp spefetetlh nkesgfpglr geqgpkgnlg lkgikgdsgf
      481 cacdggvpnt gppgepgppg pwgliglpgl kgargdrgsg gaqgpagapg lvgplgpsgp
      541 kgkkgepils tiqgmpgdrg dsgsqgfrgv igepgkdgvp glpglpglpg dggqgfpgek
      601 glpglpgekg hpgppglpgn glpglpgprg lpgdkgkdgl pgqqglpgsk gitlpciipg
      661 sygpsgfpgt pgfpgpkgsr glpgtpgqpg ssgskgepgs pglvhlpelp gfpgprgekg
      721 lpgfpglpgk dglpgmigsp glpgskgatg difgaengap geqglqgltg hkgflgdsgl
      781 pglkgvhgkp gllgpkgerg spgtpgqvgq pgtpgssgpy gikgksglpg apgfpgisgh
      841 pgkkgtrgkk gppgsivkkg lpglkglpgn pglvglkgsp gspgvaglpa lsgpkgekgs
      901 vgfvgfpgip glpgipgtrg lkgipgstgk mgpsgragtp gekgdrgnpg pvgipsprrp
      961 msnlwlkgdk gsqgsagsng fpgprgdkge agrpgppglp gapglpgiik gvsgkpgppg
     1021 fmgirglpgl kgssgitgfp gmpgesgsqg irgspglpga sglpglkgdn gqtveisgsp
     1081 gpkgqpgesg fkgtkgrdgl ignigfpgnk gedgkvgvsg dvglpgapgf pgvagmrgep
     1141 glpgssghqg aigplgspgl igpkgfpgfp glhglnglpg tkgthgtpgp sitgvpgpag
     1201 lpgpkgekgy pgigigapgk pglrgqkgdr dfypgdkeky fkgspnqk
//
LOCUS       NP_001400006             328 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001400006
VERSION     NP_001400006.1
DBSOURCE    REFSEQ: accession NM_001413077.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4012744.1,
                                           SRR14038192.267249.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..328
                     /product="mitochondrial fission regulator 1 isoform 4
                     precursor"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=30859
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=5550
     Region          22..251
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15390.2)"
     Region          177..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          179..304
                     /region_name="Necessary and sufficient to promote
                     mitochondrial fission. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     CDS             1..328
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001413077.1:132..1118"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 12"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsvlwsrkpy gssrsivrki gtnlsliqcp rvqfqinsha
       61 tewspshpge davasfadvg wvakeegecs arlrtevrsr pplqddllff ekapsrqisl
      121 pdlsqeepql ktpalaneea lqkicalene laalraqiak ivtqqeqqnl tagdldsttf
      181 gtipphpppp ppplpppalg lhqstsavdl ikerrekran agktlvknnp kkpempnmle
      241 ilkemnsvkl rsvkrseqdv kpkpvdatdp aaliaealkk kfayryrsds qdevekgipk
      301 seseatserv lslpagfiqp hvskhclg
//
LOCUS       NP_001309042             541 aa            linear   PRI 21-NOV-2025
DEFINITION  2-hydroxyacylsphingosine 1-beta-galactosyltransferase precursor
            [Homo sapiens].
ACCESSION   NP_001309042 XP_006714365
VERSION     NP_001309042.2
DBSOURCE    REFSEQ: accession NM_001322113.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Ji,J., Xie,M., Qian,Q., Xu,Y., Shi,W., Chen,Z., Ren,D., Liu,W.,
            He,X., Lv,M., Ma,J., Liu,W., Li,A. and Liu,B.
  TITLE     SOX9-mediated UGT8 expression promotes glycolysis and maintains the
            malignancy of non-small cell lung cancer
  JOURNAL   Biochem Biophys Res Commun 587, 139-145 (2022)
   PUBMED   34872002
  REMARK    GeneRIF: SOX9-mediated UGT8 expression promotes glycolysis and
            maintains the malignancy of non-small cell lung cancer.
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Reza,S., Ugorski,M. and Suchanski,J.
  TITLE     Glucosylceramide and galactosylceramide, small glycosphingolipids
            with significant impact on health and disease
  JOURNAL   Glycobiology 31 (11), 1416-1434 (2021)
   PUBMED   34080016
  REMARK    Review article
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Lemay,A.M., Courtemanche,O., Couttas,T.A., Jamsari,G., Gagne,A.,
            Bosse,Y., Joubert,P., Don,A.S. and Marsolais,D.
  TITLE     High FA2H and UGT8 transcript levels predict hydroxylated
            hexosylceramide accumulation in lung adenocarcinoma
  JOURNAL   J Lipid Res 60 (10), 1776-1786 (2019)
   PUBMED   31409741
  REMARK    GeneRIF: High FA2H and UGT8 transcript levels predict hydroxylated
            hexosylceramide accumulation in lung adenocarcinoma
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Cao,Q., Chen,X., Wu,X., Liao,R., Huang,P., Tan,Y., Wang,L., Ren,G.,
            Huang,J. and Dong,C.
  TITLE     Inhibition of UGT8 suppresses basal-like breast cancer progression
            by attenuating sulfatide-alphaVbeta5 axis
  JOURNAL   J Exp Med 215 (6), 1679-1692 (2018)
   PUBMED   29728441
  REMARK    GeneRIF: UGT8 is a potential prognostic indicator and druggable
            target of basal-like breast cancer.
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Tencomnao,T., Kapitonov,D., Bieberich,E. and Yu,R.K.
  TITLE     Transcriptional regulation of the human UDP-galactose:ceramide
            galactosyltransferase (hCGT) gene expression: functional role of
            GC-box and CRE
  JOURNAL   Glycoconj J 20 (5), 339-351 (2004)
   PUBMED   15229398
  REMARK    GeneRIF: the GC-box and CRE function cooperatively, and that the
            CRE regulates the cell-specific expression of the hCGT gene
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Sprong,H., Degroote,S., Nilsson,T., Kawakita,M., Ishida,N., van der
            Sluijs,P. and van Meer,G.
  TITLE     Association of the Golgi UDP-galactose transporter with
            UDP-galactose:ceramide galactosyltransferase allows UDP-galactose
            import in the endoplasmic reticulum
  JOURNAL   Mol Biol Cell 14 (8), 3482-3493 (2003)
   PUBMED   12925779
  REMARK    Erratum:[Mol Biol Cell. 2003 Sep;14(9):preceding table of contents]
REFERENCE   7  (residues 1 to 541)
  AUTHORS   Iida,A., Saito,S., Sekine,A., Mishima,C., Kitamura,Y., Kondo,K.,
            Harigae,S., Osawa,S. and Nakamura,Y.
  TITLE     Catalog of 86 single-nucleotide polymorphisms (SNPs) in three
            uridine diphosphate glycosyltransferase genes: UGT2A1, UGT2B15, and
            UGT8
  JOURNAL   J Hum Genet 47 (10), 505-510 (2002)
   PUBMED   12376738
  REMARK    GeneRIF: Single-nucleotide polymorphisms (SNPs) were found in UGT8
            gene
REFERENCE   8  (residues 1 to 541)
  AUTHORS   Sprong,H., Kruithof,B., Leijendekker,R., Slot,J.W., van Meer,G. and
            van der Sluijs,P.
  TITLE     UDP-galactose:ceramide galactosyltransferase is a class I integral
            membrane protein of the endoplasmic reticulum
  JOURNAL   J Biol Chem 273 (40), 25880-25888 (1998)
   PUBMED   9748263
REFERENCE   9  (residues 1 to 541)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Cloning, characterization, and expression of human ceramide
            galactosyltransferase cDNA
  JOURNAL   Biochem Biophys Res Commun 232 (2), 449-453 (1997)
   PUBMED   9125199
REFERENCE   10 (residues 1 to 541)
  AUTHORS   Bosio,A., Binczek,E., Le Beau,M.M., Fernald,A.A. and Stoffel,W.
  TITLE     The human gene CGT encoding the UDP-galactose ceramide galactosyl
            transferase (cerebroside synthase): cloning, characterization, and
            assignment to human chromosome 4, band q26
  JOURNAL   Genomics 34 (1), 69-75 (1996)
   PUBMED   8661025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC127386.5 and AC122938.3.
            
            On Feb 23, 2022 this sequence version replaced NP_001309042.1.
            
            Summary: The protein encoded by this gene belongs to the
            UDP-glycosyltransferase family. It catalyzes the transfer of
            galactose to ceramide, a key enzymatic step in the biosynthesis of
            galactocerebrosides, which are abundant sphingolipids of the myelin
            membrane of the central and peripheral nervous systems.
            Alternatively spliced transcript variants have been found for this
            gene. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (4) uses an alternate donor splice
            site at the 5' non-coding exon compared to variant 1. Variants 1-5
            encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.1294039.1,
                                           SRR11853561.22540.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..541
                     /product="2-hydroxyacylsphingosine
                     1-beta-galactosyltransferase precursor"
                     /EC_number="2.4.1.47"
                     /note="cerebroside synthase; 2-hydroxyacylsphingosine
                     1-beta-galactosyltransferase; uridine diphosphate
                     glycosyltransferase 8; ceramide UDP-galactosyltransferase;
                     UDP-galactose-ceramide galactosyltransferase"
                     /calculated_mol_wt=59196
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2260
     mat_peptide     21..541
                     /product="2-hydroxyacylsphingosine
                     1-beta-galactosyltransferase. /id=PRO_0000036064"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16880.2)"
                     /calculated_mol_wt=59196
     Region          21..502
                     /region_name="Glycosyltransferase_GTB-type"
                     /note="glycosyltransferase family 1 and related proteins
                     with GTB topology; cl10013"
                     /db_xref="CDD:471961"
     Site            order(33..34,36,186,189..190,194,221,295,358,360,362..363,
                     366)
                     /site_type="active"
                     /db_xref="CDD:340817"
     Site            order(33,295,358,360,362..363)
                     /site_type="active"
                     /note="TDP-binding site [active]"
                     /db_xref="CDD:340817"
     Site            34
                     /site_type="active"
                     /note="acceptor substrate-binding pocket [active]"
                     /db_xref="CDD:340817"
     Site            78
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16880.2)"
     Site            333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16880.2)"
     Site            442
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16880.2)"
     Site            472..492
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16880.2)"
     CDS             1..541
                     /gene="UGT8"
                     /gene_synonym="CGT; UGT4"
                     /coded_by="NM_001322113.2:659..2284"
                     /db_xref="CCDS:CCDS3705.1"
                     /db_xref="GeneID:7368"
                     /db_xref="HGNC:HGNC:12555"
                     /db_xref="MIM:601291"
ORIGIN      
        1 mksytpyfil lwsavgiaka akiiivppim feshmyifkt lasalhergh htvfllsegr
       61 diapsnhysl qrypgifnst tsdaflqskm rnifsgrlta ielfdildhy tkncdlmvgn
      121 haliqglkke kfdlllvdpn dmcgfviahl lgvkyavfst glwypaevga paplayvpef
      181 nslltdrmnl lqrmkntgvy lisrlgvsfl vlpkyerimq kynllpeksm ydlvhgsslw
      241 mlctdvalef prptlpnvvy vggiltkpas plpedlqrwv nganehgfvl vsfgagvkyl
      301 sedianklag algrlpqkvi wrfsgpkpkn lgnntkliew lpqndllghs kikaflshgg
      361 lnsifetiyh gvpvvgiplf gdhydtmtrv qakgmgille wktvtekely ealvkvinnp
      421 syrqraqkls eihkdqpghp vnrtiywidy iirhngahhl raavhqisfc qyflldiafv
      481 lllgaallyf llswvtkfiy rkikslwsrn khstvnghyh ngilngkykr nghikhekkv
      541 k
//
LOCUS       NP_001392790            1070 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001392790 XP_047291753
VERSION     NP_001392790.1
DBSOURCE    REFSEQ: accession NM_001405861.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1070)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1070)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1070)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1070)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1070)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1070)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1070)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            On May 5, 2022 this sequence version replaced XP_047291753.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1119552.1,
                                           SRR11853563.14353.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1070
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 4"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=117069
     Region          850..970
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..1070
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405861.1:251..3463"
                     /note="isoform 4 is encoded by transcript variant 12"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankies
      481 vsqplenhga piighisesl stkscgalrp vngvintlqp vladhipgds sdaeeqlhkk
      541 qrlnlvssss dgtcvaartr pvlsckkrrl vrpnsivpls kkvhrnstir pgcdvnpsca
      601 lcgsgsintm ppeihyeapl lerlsqldsc vhpvlafpdd vptslhfqsm lksqwqnkpf
      661 dkikppkkls lkhrapmpgs lpdsarkdrh klvssfltta klshhqtrpd rthrqhlddv
      721 gavpmvervt apkaerllnp pppvhdpnhs kmrlrdhsse rsevlkhhtd mssssylaat
      781 hhpphsplvr qlstssdspa passssqvta stsqpvrrrr gessfdinni vipmsvaatt
      841 rveklqykei ltpswrevdl qslkgspdee neeiedlsda afaalhakce emerarwlwt
      901 tsvppqrrgs rsyrssdgrt tpqlgsanps tpqpaspdvs sshslseysh gqsprspisp
      961 elhsapltpv ardtprhlas edtrcstpel gldeqsvqpw errtfplahs pqaecedqld
     1021 aqeraarctr rtsgsktgre teaaptsppi vplksrhlva aataqrpthr
//
LOCUS       NP_001427740            1058 aa            linear   PRI 21-NOV-2025
DEFINITION  ubiquitin-like modifier-activating enzyme 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001427740
VERSION     NP_001427740.1
DBSOURCE    REFSEQ: accession NM_001440811.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Sirenko,M., Bernard,E., Creignou,M., Domenico,D., Farina,A., Arango
            Ossa,J.E., Kosmider,O., Hasserjian,R., Jadersten,M., Germing,U.,
            Sanz,G., van de Loosdrecht,A.A., Gurnari,C., Follo,M.Y., Thol,F.,
            Zamora,L., Pinheiro,R.F., Pellagatti,A., Elias,H.K., Haase,D.,
            Sander,B., Orna,E., Zoldan,K., Eder,L.N., Sperr,W.R.,
            Thalhammer,R., Ganster,C., Ades,L., Tobiasson,M., Palomo,L., Della
            Porta,M.G., Huberman,K., Fenaux,P., Belickova,M., Savona,M.R.,
            Klimek,V.M., Santos,F.P.S., Boultwood,J., Kotsianidis,I.,
            Santini,V., Sole,F., Platzbecker,U., Heuser,M., Valent,P.,
            Finelli,C., Voso,M.T., Shih,L.Y., Ogawa,S., Fontenay,M.,
            Jansen,J.H., Cervera,J., Ebert,B.L., Bejar,R., Greenberg,P.L.,
            Gattermann,N., Malcovati,L., Cazzola,M., Beck,D.B.,
            Hellstrom-Lindberg,E. and Papaemmanuil,E.
  TITLE     Molecular and clinical presentation of UBA1-mutated myelodysplastic
            syndromes
  JOURNAL   Blood 144 (11), 1221-1229 (2024)
   PUBMED   38687605
  REMARK    GeneRIF: Molecular and clinical presentation of UBA1-mutated
            myelodysplastic syndromes.
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Chen,C., Li,Y., Chen,Z., Shi,P., Li,Y. and Qian,S.
  TITLE     A comprehensive prognostic and immune infiltration analysis of UBA1
            in pan-cancer: A computational analysis and in vitro experiments
  JOURNAL   J Cell Mol Med 28 (16), e70037 (2024)
   PUBMED   39183260
  REMARK    GeneRIF: A comprehensive prognostic and immune infiltration
            analysis of UBA1 in pan-cancer: A computational analysis and in
            vitro experiments.
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Corty,R.W., Brogan,J., Byram,K., Springer,J., Grayson,P.C. and
            Bick,A.G.
  TITLE     VEXAS-Defining UBA1 Somatic Variants in 245,368 Diverse Individuals
            in the NIH All Of Us Cohort
  JOURNAL   Arthritis Rheumatol 76 (6), 942-948 (2024)
   PUBMED   38225170
  REMARK    GeneRIF: VEXAS-Defining UBA1 Somatic Variants in 245,368 Diverse
            Individuals in the NIH All Of Us Cohort.
REFERENCE   4  (residues 1 to 1058)
  AUTHORS   Collins,J.C., Magaziner,S.J., English,M., Hassan,B., Chen,X.,
            Balanda,N., Anderson,M., Lam,A., Fernandez-Pol,S., Kwong,B.,
            Greenberg,P.L., Terrier,B., Likhite,M.E., Kosmider,O., Wang,Y.,
            Samara,N.L., Walters,K.J., Beck,D.B. and Werner,A.
  TITLE     Shared and distinct mechanisms of UBA1 inactivation across
            different diseases
  JOURNAL   EMBO J 43 (10), 1919-1946 (2024)
   PUBMED   38360993
  REMARK    GeneRIF: Shared and distinct mechanisms of UBA1 inactivation across
            different diseases.
REFERENCE   5  (residues 1 to 1058)
  AUTHORS   Hadjadj,J. and Beck,D.
  TITLE     VEXAS Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   40373178
REFERENCE   6  (residues 1 to 1058)
  AUTHORS   Baumbach-Reardon,L., Hunter,J.M., Ahearn,M.E. and Pfautsch,M.
  TITLE     Spinal Muscular Atrophy, X-Linked Infantile
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301739
REFERENCE   7  (residues 1 to 1058)
  AUTHORS   Schwartz,A.L., Trausch,J.S., Ciechanover,A., Slot,J.W. and Geuze,H.
  TITLE     Immunoelectron microscopic localization of the ubiquitin-activating
            enzyme E1 in HepG2 cells
  JOURNAL   Proc Natl Acad Sci U S A 89 (12), 5542-5546 (1992)
   PUBMED   1376922
REFERENCE   8  (residues 1 to 1058)
  AUTHORS   Ayusawa,D., Kaneda,S., Itoh,Y., Yasuda,H., Murakami,Y.,
            Sugasawa,K., Hanaoka,F. and Seno,T.
  TITLE     Complementation by a cloned human ubiquitin-activating enzyme E1 of
            the S-phase-arrested mouse FM3A cell mutant with thermolabile E1
  JOURNAL   Cell Struct Funct 17 (2), 113-122 (1992)
   PUBMED   1606621
REFERENCE   9  (residues 1 to 1058)
  AUTHORS   Takahashi,E., Ayusawa,D., Kaneda,S., Itoh,Y., Seno,T. and Hori,T.
  TITLE     The human ubiquitin-activating enzyme E1 gene (UBE1) mapped to band
            Xp11.3----p11.23 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 59 (4), 268-269 (1992)
   PUBMED   1544321
REFERENCE   10 (residues 1 to 1058)
  AUTHORS   Kudo,M., Sugasawa,K., Hori,T., Enomoto,T., Hanaoka,F. and Ui,M.
  TITLE     Human ubiquitin-activating enzyme (E1): compensation for
            heat-labile mouse E1 and its gene localization on the X chromosome
  JOURNAL   Exp Cell Res 192 (1), 110-117 (1991)
   PUBMED   1845793
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513366.11.
            
            Summary: The protein encoded by this gene catalyzes the first step
            in ubiquitin conjugation to mark cellular proteins for degradation.
            This gene complements an X-linked mouse temperature-sensitive
            defect in DNA synthesis, and thus may function in DNA repair. It is
            part of a gene cluster on chromosome Xp11.23. Alternatively spliced
            transcript variants that encode the same protein have been
            described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1579881.1,
                                           SRR14038191.917313.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.3"
     Protein         1..1058
                     /product="ubiquitin-like modifier-activating enzyme 1
                     isoform 1"
                     /EC_number="6.2.1.45"
                     /note="POC20 centriolar protein homolog; UBA1,
                     ubiquitin-activating enzyme E1 homolog A; A1S9T and BN75
                     temperature sensitivity complementing; testicular
                     secretory protein Li 63"
                     /calculated_mol_wt=117718
     Region          1..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22314.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9099746; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Region          5..11
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P22314.3)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02053; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02053; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P22314.3)"
     Region          49..1055
                     /region_name="Ube1"
                     /note="ubiquitin-activating enzyme E1; TIGR01408"
                     /db_xref="CDD:273603"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q02053; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Region          63..611
                     /region_name="2 approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P22314.3)"
     Site            671
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            800
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            810
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            816
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02053; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            820
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            835
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            980
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     CDS             1..1058
                     /gene="UBA1"
                     /gene_synonym="A1S9; A1S9T; A1ST; AMCX1; CFAP124; GXP1;
                     POC20; SMAX2; UBA1A; UBE1; UBE1X; VEXAS"
                     /coded_by="NM_001440811.1:311..3487"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:7317"
                     /db_xref="HGNC:HGNC:12469"
                     /db_xref="MIM:314370"
ORIGIN      
        1 msssplskkr rvsgpdpkpg sncspaqsvl sevpsvptng makngseadi deglysrqly
       61 vlgheamkrl qtssvlvsgl rglgveiakn iilggvkavt lhdqgtaqwa dlssqfylre
      121 edigknraev sqprlaelns yvpvtaytgp lvedflsgfq vvvltntple dqlrvgefch
      181 nrgiklvvad trglfgqlfc dfgeemiltd sngeqplsam vsmvtkdnpg vvtcldearh
      241 gfesgdfvsf sevqgmveln gnqpmeikvl gpytfsicdt snfsdyirgg ivsqvkvpkk
      301 isfkslvasl aepdfvvtdf akfsrpaqlh igfqalhqfc aqhgrpprpr needaaelva
      361 laqavnaral pavqqnnlde dlirklayva agdlapinaf igglaaqevm kacsgkfmpi
      421 mqwlyfdale clpedkevlt edkclqrqnr ydgqvavfgs dlqeklgkqk yflvgagaig
      481 cellknfami glgcgeggei ivtdmdtiek snlnrqflfr pwdvtklksd taaaavrqmn
      541 phirvtshqn rvgpdteriy dddffqnldg vanaldnvda rmymdrrcvy yrkpllesgt
      601 lgtkgnvqvv ipfltesyss sqdppeksip ictlknfpna iehtlqward efeglfkqpa
      661 envnqyltdp kfvertlrla gtqplevlea vqrslvlqrp qtwadcvtwa chhwhtqysn
      721 nirqllhnfp pdqltssgap fwsgpkrcph pltfdvnnpl hldyvmaaan lfaqtygltg
      781 sqdraavatf lqsvqvpeft pksgvkihvs dqelqsanas vddsrleelk atlpspdklp
      841 gfkmypidfe kdddsnfhmd fivaasnlra enydipsadr hkskliagki ipaiatttaa
      901 vvglvclely kvvqghrqld sykngflnla lpffgfsepl aaprhqyynq ewtlwdrfev
      961 qglqpngeem tlkqfldyfk tehkleitml sqgvsmlysf fmpaaklker ldqpmteivs
     1021 rvskrklgrh vralvlelcc ndesgedvev pyvrytir
//
LOCUS       NP_001400302             371 aa            linear   PRI 21-NOV-2025
DEFINITION  telomeric repeat-binding factor 1 isoform 13 [Homo sapiens].
ACCESSION   NP_001400302
VERSION     NP_001400302.1
DBSOURCE    REFSEQ: accession NM_001413373.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Hu,H., van Roon,A.M., Ghanim,G.E., Ahsan,B., Oluwole,A.O.,
            Peak-Chew,S.Y., Robinson,C.V. and Nguyen,T.H.D.
  TITLE     Structural basis of telomeric nucleosome recognition by shelterin
            factor TRF1
  JOURNAL   Sci Adv 9 (34), eadi4148 (2023)
   PUBMED   37624885
  REMARK    GeneRIF: Structural basis of telomeric nucleosome recognition by
            shelterin factor TRF1.
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Harmak,H., Redouane,S., Charoute,H., Aniq Filali,O., Barakat,A. and
            Rouba,H.
  TITLE     In silico exploration and molecular dynamics of deleterious SNPs on
            the human TERF1 protein triggering male infertility
  JOURNAL   J Biomol Struct Dyn 41 (24), 14665-14688 (2023)
   PUBMED   36995171
  REMARK    GeneRIF: In silico exploration and molecular dynamics of
            deleterious SNPs on the human TERF1 protein triggering male
            infertility.
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Abreu,P.L., Lee,Y.W. and Azzalin,C.M.
  TITLE     In Vitro Characterization of the Physical Interactions between the
            Long Noncoding RNA TERRA and the Telomeric Proteins TRF1 and TRF2
  JOURNAL   Int J Mol Sci 23 (18), 10463 (2022)
   PUBMED   36142374
  REMARK    GeneRIF: In Vitro Characterization of the Physical Interactions
            between the Long Noncoding RNA TERRA and the Telomeric Proteins
            TRF1 and TRF2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Jack,A., Kim,Y., Strom,A.R., Lee,D.S.W., Williams,B., Schaub,J.M.,
            Kellogg,E.H., Finkelstein,I.J., Ferro,L.S., Yildiz,A. and
            Brangwynne,C.P.
  TITLE     Compartmentalization of telomeres through DNA-scaffolded phase
            separation
  JOURNAL   Dev Cell 57 (2), 277-290 (2022)
   PUBMED   35077681
  REMARK    GeneRIF: Compartmentalization of telomeres through DNA-scaffolded
            phase separation.
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Broccoli,D., Chong,L., Oelmann,S., Fernald,A.A., Marziliano,N., van
            Steensel,B., Kipling,D., Le Beau,M.M. and de Lange,T.
  TITLE     Comparison of the human and mouse genes encoding the telomeric
            protein, TRF1: chromosomal localization, expression and conserved
            protein domains
  JOURNAL   Hum Mol Genet 6 (1), 69-76 (1997)
   PUBMED   9002672
REFERENCE   7  (residues 1 to 371)
  AUTHORS   Lu,K.P., Hanes,S.D. and Hunter,T.
  TITLE     A human peptidyl-prolyl isomerase essential for regulation of
            mitosis
  JOURNAL   Nature 380 (6574), 544-547 (1996)
   PUBMED   8606777
REFERENCE   8  (residues 1 to 371)
  AUTHORS   Bilaud,T., Koering,C.E., Binet-Brasselet,E., Ancelin,K.,
            Pollice,A., Gasser,S.M. and Gilson,E.
  TITLE     The telobox, a Myb-related telomeric DNA binding motif found in
            proteins from yeast, plants and human
  JOURNAL   Nucleic Acids Res 24 (7), 1294-1303 (1996)
   PUBMED   8614633
REFERENCE   9  (residues 1 to 371)
  AUTHORS   Chong,L., van Steensel,B., Broccoli,D., Erdjument-Bromage,H.,
            Hanish,J., Tempst,P. and de Lange,T.
  TITLE     A human telomeric protein
  JOURNAL   Science 270 (5242), 1663-1667 (1995)
   PUBMED   7502076
REFERENCE   10 (residues 1 to 371)
  AUTHORS   Zhong,Z., Shiue,L., Kaplan,S. and de Lange,T.
  TITLE     A mammalian factor that binds telomeric TTAGGG repeats in vitro
  JOURNAL   Mol Cell Biol 12 (11), 4834-4843 (1992)
   PUBMED   1406665
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022893.6.
            
            Summary: This gene encodes a telomere specific protein which is a
            component of the telomere nucleoprotein complex. This protein is
            present at telomeres throughout the cell cycle and functions as an
            inhibitor of telomerase, acting in cis to limit the elongation of
            individual chromosome ends. The protein structure contains a
            C-terminal Myb motif, a dimerization domain near its N-terminus and
            an acidic N-terminus. Multiple transcripts of this gene are
            alternatively spliced products. [provided by RefSeq, Aug 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4310460.1,
                                           SRR18074969.325707.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.11"
     Protein         1..371
                     /product="telomeric repeat-binding factor 1 isoform 13"
                     /note="NIMA-interacting protein 2; telomeric protein
                     Pin2/TRF1; TTAGGG repeat-binding factor 1; telomeric
                     repeat binding factor (NIMA-interacting) 1"
                     /calculated_mol_wt=42177
     Region          76..264
                     /region_name="TRFH"
                     /note="Telomeric Repeat binding Factor or TTAGGG Repeat
                     binding Factor, central (dimerization) domain Homology;
                     TRFH. Telomeres are protein/DNA complexes that make up the
                     physical ends of eukaryotic linear chromosomes and are
                     essential for chromosome stability; cd00280"
                     /db_xref="CDD:238174"
     Site            order(106,109,123,127,131,141..145,153,156..157,160)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238174"
     CDS             1..371
                     /gene="TERF1"
                     /gene_synonym="hTRF1-AS; PIN2; t-TRF1; TRBF1; TRF; TRF1"
                     /coded_by="NM_001413373.1:24..1139"
                     /note="isoform 13 is encoded by transcript variant 13"
                     /db_xref="GeneID:7013"
                     /db_xref="HGNC:HGNC:11728"
                     /db_xref="MIM:600951"
ORIGIN      
        1 maedvssaap sprgcadgrd adpteeqmae terndeeqfe cqellecqvq vgapeeeeee
       61 eedaglvaea eavaagwmld flclslcraf rdgrsedfrr trnsaeaiih glssltacql
      121 rtiyicqflt riaagktlda qfenderitp lesalmiwgs iekehdklhe eiqnlikiqa
      181 iavcmengnf keaeevferi fgdpnshmpf kskllmiisq kdtfhsffqh fsynhmmeki
      241 ksyvnyvlse ksstflmkaa akvveskrtr titsqdkpsg ndvemetean ldtrkrshkn
      301 lflsklqhgt qqqdlnkker rvgtpqstkk kkesrrates ripvsksqpv tpekhrarkr
      361 qgssvkrvff t
//
LOCUS       NP_001425937            1023 aa            linear   PRI 21-NOV-2025
DEFINITION  2-oxoglutarate dehydrogenase complex component E1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001425937 XP_047276383 XP_054214285
VERSION     NP_001425937.1
DBSOURCE    REFSEQ: accession NM_001439008.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Nguyen,T.T., Torrini,C., Shang,E., Shu,C., Mun,J.Y., Gao,Q.,
            Humala,N., Akman,H.O., Zhang,G., Westhoff,M.A., Karpel-Massler,G.,
            Bruce,J.N., Canoll,P. and Siegelin,M.D.
  TITLE     OGDH and Bcl-xL loss causes synthetic lethality in glioblastoma
  JOURNAL   JCI Insight 9 (8), e172565 (2024)
   PUBMED   38483541
  REMARK    GeneRIF: OGDH and Bcl-xL loss causes synthetic lethality in
            glioblastoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Hevler,J.F., Albanese,P., Cabrera-Orefice,A., Potter,A.,
            Jankevics,A., Misic,J., Scheltema,R.A., Brandt,U., Arnold,S. and
            Heck,A.J.R.
  TITLE     MRPS36 provides a structural link in the eukaryotic 2-oxoglutarate
            dehydrogenase complex
  JOURNAL   Open Biol 13 (3), 220363 (2023)
   PUBMED   36854377
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Whittle,E.F., Chilian,M., Karimiani,E.G., Progri,H., Buhas,D.,
            Kose,M., Ganetzky,R.D., Toosi,M.B., Torbati,P.N., Badv,R.S.,
            Shelihan,I., Yang,H., Elloumi,H.Z., Lee,S., Jamshidi,Y.,
            Pittman,A.M., Houlden,H., Ignatius,E., Rahman,S., Maroofian,R.,
            Yoon,W.H. and Carroll,C.J.
  TITLE     Biallelic variants in OGDH encoding oxoglutarate dehydrogenase lead
            to a neurodevelopmental disorder characterized by global
            developmental delay, movement disorder, and metabolic abnormalities
  JOURNAL   Genet Med 25 (2), 100332 (2023)
   PUBMED   36520152
  REMARK    GeneRIF: Biallelic variants in OGDH encoding oxoglutarate
            dehydrogenase lead to a neurodevelopmental disorder characterized
            by global developmental delay, movement disorder, and metabolic
            abnormalities.
REFERENCE   4  (residues 1 to 1023)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 1023)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 1023)
  AUTHORS   McCartney,R.G., Rice,J.E., Sanderson,S.J., Bunik,V., Lindsay,H. and
            Lindsay,J.G.
  TITLE     Subunit interactions in the mammalian alpha-ketoglutarate
            dehydrogenase complex. Evidence for direct association of the
            alpha-ketoglutarate dehydrogenase and dihydrolipoamide
            dehydrogenase components
  JOURNAL   J Biol Chem 273 (37), 24158-24164 (1998)
   PUBMED   9727038
REFERENCE   7  (residues 1 to 1023)
  AUTHORS   Koike,K.
  TITLE     The gene encoding human 2-oxoglutarate dehydrogenase: structural
            organization and mapping to chromosome 7p13-p14
  JOURNAL   Gene 159 (2), 261-266 (1995)
   PUBMED   7622061
REFERENCE   8  (residues 1 to 1023)
  AUTHORS   Szabo,P., Cai,X., Ali,G. and Blass,J.P.
  TITLE     Localization of the gene (OGDH) coding for the E1k component of the
            alpha-ketoglutarate dehydrogenase complex to chromosome 7p13-p11.2
  JOURNAL   Genomics 20 (2), 324-326 (1994)
   PUBMED   8020988
REFERENCE   9  (residues 1 to 1023)
  AUTHORS   Koike,K., Urata,Y. and Goto,S.
  TITLE     Cloning and nucleotide sequence of the cDNA encoding human
            2-oxoglutarate dehydrogenase (lipoamide)
  JOURNAL   Proc Natl Acad Sci U S A 89 (5), 1963-1967 (1992)
   PUBMED   1542694
REFERENCE   10 (residues 1 to 1023)
  AUTHORS   Reed,L.J. and Hackert,M.L.
  TITLE     Structure-function relationships in dihydrolipoamide
            acyltransferases
  JOURNAL   J Biol Chem 265 (16), 8971-8974 (1990)
   PUBMED   2188967
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011894.3 and AC004859.3.
            
            On or before Apr 25, 2025 this sequence version replaced
            XP_047276383.1, XP_054214285.1.
            
            Summary: This gene encodes one subunit of the 2-oxoglutarate
            dehydrogenase complex. This complex catalyzes the overall
            conversion of 2-oxoglutarate (alpha-ketoglutarate) to succinyl-CoA
            and CO(2) during the Krebs cycle. The protein is located in the
            mitochondrial matrix and uses thiamine pyrophosphate as a cofactor.
            A congenital deficiency in 2-oxoglutarate dehydrogenase activity is
            believed to lead to hypotonia, metabolic acidosis, and
            hyperlactatemia. Alternative splicing results in multiple
            transcript variants encoding distinct isoforms.[provided by RefSeq,
            Sep 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2124573.1,
                                           SRR14038197.1111124.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..1023
                     /product="2-oxoglutarate dehydrogenase complex component
                     E1 isoform 1"
                     /EC_number="1.2.4.2"
                     /note="oxoglutarate dehydrogenase (succinyl-transferring);
                     oxoglutarate (alpha-ketoglutarate) dehydrogenase
                     (lipoamide); 2-oxoglutarate dehydrogenase, mitochondrial;
                     oxoglutarate decarboxylase; OGDC-E1; 2-oxoglutarate
                     dehydrogenase complex component E1; testicular tissue
                     protein Li 131; alpha-KGDH-E1; thiamine diphosphate
                     (ThDP)-dependent 2-oxoglutarate dehydrogenase"
                     /calculated_mol_wt=111340
     transit_peptide 1..40
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q02218.3)"
                     /calculated_mol_wt=4613
     mat_peptide     41..1023
                     /product="2-oxoglutarate dehydrogenase complex component
                     E1. /id=PRO_0000020432"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02218.3)"
                     /calculated_mol_wt=111340
     Region          49..1016
                     /region_name="SucA"
                     /note="2-oxoglutarate dehydrogenase complex, dehydrogenase
                     (E1) component, and related enzymes [Energy production and
                     conversion]; COG0567"
                     /db_xref="CDD:440333"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60597; propagated from
                     UniProtKB/Swiss-Prot (Q02218.3)"
     Site            401
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60597; propagated from
                     UniProtKB/Swiss-Prot (Q02218.3)"
     Site            970
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q02218.3)"
     CDS             1..1023
                     /gene="OGDH"
                     /gene_synonym="AKGDH; E1k; E1o; HsOGDH; KGD1; OGDC;
                     OGDH-E1; OGDH2; OGDHD"
                     /coded_by="NM_001439008.1:166..3237"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="GeneID:4967"
                     /db_xref="HGNC:HGNC:8124"
                     /db_xref="MIM:613022"
ORIGIN      
        1 mfhlrtcaak lrpltasqtv ktfsqnrpaa artfqqircy sapvaaepfl sgtssnyvee
       61 mycawlenpk svhkswdiff rntnagappg tayqsplpls rgslaavaha qslveaqpnv
      121 dklvedhlav qslirayqir ghhvaqldpl gildadldss vpadiisstd klgfygldes
      181 dldkvfhlpt ttfiggqesa lplreiirrl emaycqhigv efmfindleq cqwirqkfet
      241 pgimqftnee krtllarlvr strfeeflqr kwssekrfgl egcevlipal ktiidkssen
      301 gvdyvimgmp hrgrlnvlan virkeleqif cqfdskleaa degsgdvkyh lgmyhrrinr
      361 vtdrnitlsl vanpshleaa dpvvmgktka eqfycgdteg kkvmsillhg daafagqgiv
      421 yetfhlsdlp sytthgtvhv vvnnqigftt dprmarsspy ptdvarvvna pifhvnsddp
      481 eavmyvckva aewrstfhkd vvvdlvcyrr nghnemdepm ftqplmykqi rkqkpvlqky
      541 aellvsqgvv nqpeyeeeis kydkiceeaf arskdekilh ikhwldspwp gfftldgqpr
      601 smscpstglt edilthignv assvpvenft ihgglsrilk trgemvknrt vdwalaeyma
      661 fgsllkegih irlsgqdver gtfshrhhvl hdqnvdkrtc ipmnhlwpnq apytvcnssl
      721 seygvlgfel gfamaspnal vlweaqfgdf hntaqciidq ficpgqakwv rqngivlllp
      781 hgmegmgpeh ssarperflq mcnddpdvlp dlkeanfdin qlydcnwvvv ncstpgnffh
      841 vlrrqillpf rkpliiftpk sllrhpears sfdemlpgth fqrvipedgp aaqnpenvkr
      901 llfctgkvyy dltrerkard mvgqvaitri eqlspfpfdl llkevqkypn aelawcqeeh
      961 knqgyydyvk prlrttisra kpvwyagrdp aaapatgnkk thltelqrll dtafdldvfk
     1021 nfs
//
LOCUS       NP_001424533             425 aa            linear   PRI 21-NOV-2025
DEFINITION  sorting nexin-27 isoform 6 [Homo sapiens].
ACCESSION   NP_001424533 XP_047287246 XP_054194891
VERSION     NP_001424533.1
DBSOURCE    REFSEQ: accession NM_001437604.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Broniarczyk,J., Trejo-Cerro,O., Massimi,P., Kavcic,N., Myers,M.P.
            and Banks,L.
  TITLE     HPV-18 E6 enhances the interaction between EMILIN2 and SNX27 to
            promote WNT signaling
  JOURNAL   J Virol 98 (7), e0073524 (2024)
   PUBMED   38874360
  REMARK    GeneRIF: HPV-18 E6 enhances the interaction between EMILIN2 and
            SNX27 to promote WNT signaling.
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Xi,Y., Gai,Y., Zhang,W., Wang,M., Liu,Q. and Bi,Y.
  TITLE     Circular RNA SNX27 Facilitates Gastric Cancer Progression By
            Sponging miR-638
  JOURNAL   Turk J Gastroenterol 35 (4), 280-287 (2024)
   PUBMED   39128090
  REMARK    GeneRIF: Circular RNA SNX27 Facilitates Gastric Cancer Progression
            By Sponging miR-638.
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Broniarczyk,J.K., Massimi,P., Trejo-Cerro,O., Myers,M.P. and
            Banks,L.
  TITLE     HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in a
            PBM-Dependent Manner and Promotes Increased Cell Proliferation
  JOURNAL   J Virol 96 (22), e0136522 (2022)
   PUBMED   36326272
  REMARK    GeneRIF: HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in
            a PBM-Dependent Manner and Promotes Increased Cell Proliferation.
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 425)
  AUTHORS   MacNeil,A.J., Mansour,M. and Pohajdak,B.
  TITLE     Sorting nexin 27 interacts with the Cytohesin associated
            scaffolding protein (CASP) in lymphocytes
  JOURNAL   Biochem Biophys Res Commun 359 (4), 848-853 (2007)
   PUBMED   17577583
  REMARK    GeneRIF: These results suggest that endosomal SNX27 may recruit
            CASP to orchestrate intracellular trafficking and/or signaling
            complexes.
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Rincon,E., Santos,T., Avila-Flores,A., Albar,J.P., Lalioti,V.,
            Lei,C., Hong,W. and Merida,I.
  TITLE     Proteomics identification of sorting nexin 27 as a diacylglycerol
            kinase zeta-associated protein: new diacylglycerol kinase roles in
            endocytic recycling
  JOURNAL   Mol Cell Proteomics 6 (6), 1073-1087 (2007)
   PUBMED   17351151
  REMARK    GeneRIF: These data support a previously unreported role for
            diacylglycerol kinase zeta in the modulation of membrane
            trafficking, which may also help to define SNX27 function.
REFERENCE   8  (residues 1 to 425)
  AUTHORS   Joubert,L., Hanson,B., Barthet,G., Sebben,M., Claeysen,S., Hong,W.,
            Marin,P., Dumuis,A. and Bockaert,J.
  TITLE     New sorting nexin (SNX27) and NHERF specifically interact with the
            5-HT4a receptor splice variant: roles in receptor targeting
  JOURNAL   J Cell Sci 117 (Pt 22), 5367-5379 (2004)
   PUBMED   15466885
  REMARK    GeneRIF: SNX27a redirects part of the 5-HT4(a)R to early endosomes.
REFERENCE   9  (residues 1 to 425)
  AUTHORS   Worby,C.A. and Dixon,J.E.
  TITLE     Sorting out the cellular functions of sorting nexins
  JOURNAL   Nat Rev Mol Cell Biol 3 (12), 919-931 (2002)
   PUBMED   12461558
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol. 2003 Feb;4(2):156.]
REFERENCE   10 (residues 1 to 425)
  AUTHORS   Teasdale,R.D., Loci,D., Houghton,F., Karlsson,L. and Gleeson,P.A.
  TITLE     A large family of endosome-localized proteins related to sorting
            nexin 1
  JOURNAL   Biochem J 358 (Pt 1), 7-16 (2001)
   PUBMED   11485546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL391335.32 and AL589765.19.
            
            On or before Apr 7, 2025 this sequence version replaced
            XP_047287246.1, XP_054194891.1.
            
            Summary: This gene encodes a member of the sorting nexin family, a
            diverse group of cytoplasmic and membrane-associated proteins
            involved in endocytosis of plasma membrane receptors and protein
            trafficking through these compartments. All members of this protein
            family contain a phosphoinositide binding domain (PX domain). A
            highly similar protein in mouse is responsible for the specific
            recruitment of an isoform of serotonin 5-hydroxytryptamine 4
            receptor into early endosomes, suggesting the analogous role for
            the human protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2229279.1,
                                           SRR14038195.2341411.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..425
                     /product="sorting nexin-27 isoform 6"
                     /note="methamphetamine-responsive transcript 1; sorting
                     nexin family member 27"
                     /calculated_mol_wt=49631
     Region          <2..31
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     Region          57..162
                     /region_name="PX_SNX27"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 27; cd06886"
                     /db_xref="CDD:132796"
     Site            order(93..95,118..119,132)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132796"
     Region          170..262
                     /region_name="FERM_F1_SNX27"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F1 sub-domain, found in sorting nexin protein 27
                     (SNX27); cd01777"
                     /db_xref="CDD:340475"
     Region          322..423
                     /region_name="FERM-like_C_SNX27"
                     /note="Atypical FERM-like domain C-lobe of Sorting nexin
                     27; cd13338"
                     /db_xref="CDD:270146"
     CDS             1..425
                     /gene="SNX27"
                     /gene_synonym="MRT1; MY014"
                     /coded_by="NM_001437604.1:391..1668"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:81609"
                     /db_xref="HGNC:HGNC:20073"
                     /db_xref="MIM:611541"
ORIGIN      
        1 mnhvnvegat hkqvvdlira gekeliltvl svppheadnl dpsddslgqs fydytekqav
       61 pisvprykhv eqngekfvvy nvymagrqlc skryrefail hqnlkrefan ftfprlpgkw
      121 pfslseqqld arrrgleeyl ekvcsirvig esdimqefls esdenyngvs dvelrvalpd
      181 gttvtvrvkk nsttdqvyqa iaakvgmdst tvnyfalfev ishsfvrkla pnefphklyi
      241 qnytsavpgt cltirkwlft teeeillndn dlavtyffhq avddvkkgyi kaeeksyqlq
      301 klyeqrkmvm ylnmlrtceg yneiifphca cdsrrkghvi taisithfkl hacteegqle
      361 nqviafewde mqrwdtdeeg mafcfeyarg ekkprwvkif tpyfnymhec fervfcelkw
      421 rkeey
//
LOCUS       NP_001428156             435 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 10 [Homo sapiens].
ACCESSION   NP_001428156
VERSION     NP_001428156.1
DBSOURCE    REFSEQ: accession NM_001441227.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 435)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 435)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 435)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR12921934.3389039.1,
                                           SRR1660805.28607.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..435
                     /product="calcium uptake protein 1, mitochondrial isoform
                     10"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=49603
     Region          181..400
                     /region_name="EFh_MICU1"
                     /note="EF-hand, calcium binding motif, found in calcium
                     uptake protein 1, mitochondrial (MICU1) and similar
                     proteins; cd16173"
                     /db_xref="CDD:320081"
     Region          181..210
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Site            order(183,335,338,341..342,344,362)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:320081"
     Site            order(190,192,194,201,380,382,384,391)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320081"
     Region          236..266
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          334..363
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          371..400
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     CDS             1..435
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001441227.1:72..1379"
                     /note="isoform 10 is encoded by transcript variant 14"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mfrlnslsal aelavgsrwy hggsqpiqir rrlmmvaflg asavtastgl lwkrahaesp
       61 pcvdnlksdi gdkgknkdeg dvcnhekkta dlaphpeekk kkrsgfrdrk vmeyenrira
      121 ystpdkifry fatlkvisep geaevfmtpe dfvrsitpne kqpehlgldq yiikrfdgkr
      181 nfeiafkmfd lngdgevdme efeqvqsiir sqtsmgmrhr drpttgntlk sglcsaltty
      241 ffgadlkgkl tiknflefqr klqhdvlkle ferhdpvdgr iterqfggml laysgvqskk
      301 ltamqrqlkk hfkegkgltf qevenfftfl knindvdtal sfyhmagasl dkvtmqqvar
      361 tvakvelsdh vcdvvfalfd cdgngelsnk efvsimkqrl mrglekpkdm gftrlmqamw
      421 kcaqetawdf alpkq
//
LOCUS       NP_001389619            1306 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 21 [Homo sapiens].
ACCESSION   NP_001389619
VERSION     NP_001389619.1
DBSOURCE    REFSEQ: accession NM_001402690.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1306)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1306)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1306)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1306)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1306)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1306)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1306)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1306)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1306)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1306)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1735813.1,
                                           SRR14038191.2007851.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1306
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1306
                     /product="kinectin isoform 21"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=150251
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          <326..>568
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          453..1246
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1306
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402690.1:179..4099"
                     /note="isoform 21 is encoded by transcript variant 15"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqtsasvlae elhkviaekd kqikqtedsl
      601 aserdrltsk eeelkdiqnm nfllkaevqk lqalaneqaa aahelekmqq svyvkddkir
      661 lleeqlqhei snkmeefkil ndqnkalkse vqklqtlvse qpnkdvveqm ekciqekdek
      721 lktveellet gliqvatkee elnairtens sltkevqdlk akqndqvsfa slveelkkvi
      781 hekdgkiksv eelleaellk vankektvqd lkqeikalke eignvqleka qqlsitskvq
      841 elqnllkgke eqmntmkavl eekekdlant gkwlqdlqee neslkahvqe vaqhnlkeas
      901 sasqfeelei vlkekenelk rleamlkere sdlssktqll qdvqdenklf ksqieqlkqq
      961 nyqqassfpp heellkvise rekeisglwn eldslkdave hqrkknndlr eknweameal
     1021 astekmlqdk vnktskerqq qveaveleak evlkklfpkv svpsnlsyge wlhgfekkak
     1081 ecmagtsgse evkvlehklk eademhtllq lecekyksvl aetegilqkl qrsveqeenk
     1141 wkvkvdeshk tikqmqssft sseqelerlr senkdienlr rerehlemel ekaemersty
     1201 vtevrelkaq lnetltklrt eqnerqkvag dlhkaqqsle liqskivkaa gdttviensd
     1261 vspetessek etmsvslnqt vtqlqqllqa vnqqltkeke hyqvle
//
LOCUS       NP_001393988             545 aa            linear   PRI 21-NOV-2025
DEFINITION  merlin isoform 14 [Homo sapiens].
ACCESSION   NP_001393988
VERSION     NP_001393988.1
DBSOURCE    REFSEQ: accession NM_001407059.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 545)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 545)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 545)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 545)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 545)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005529.7 and AC004882.3.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.3788067.1,
                                           SRR14038194.3171274.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145313, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..545
                     /product="merlin isoform 14"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=63791
     Region          23..222
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          216..267
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          262..>322
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          301..420
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          473..>534
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..545
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_001407059.1:367..2004"
                     /note="isoform 14 is encoded by transcript variant 21"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 magaiasrms fsslkrkqpk tftvrivtmd aemefncemk wkgkdlfdlv crtlglretw
       61 ffglqytikd tvawlkmdkk vldhdvskee pvtfhflakf ypenaeeelv qeitqhlffl
      121 qvkkqildek iycppeasvl lasyavqaky gdydpsvhkr gflaqeellp krvinlyqmt
      181 pemweerita wyaehrgrar deaemeylki aqdlemygvn yfairftikp ldkkidvfkf
      241 nssklrvnkl ilqlcignhd lfmrrrkads levqqmkaqa reekarkqme rqrlarekqm
      301 reeaertrde lerrllqmke eatmanealm rseetadlla ekaqiteeea kllaqkaaea
      361 eqemqrikat airteeekrl meqkvleaev lalkmaeese rrakeadqlk qdlqeareae
      421 rrakqkllei atkptyppmn pipaplppdi psfnligdsl sfdfkdtdmk rlsmeiekek
      481 veymekskhl qeqlnelkte iealklkere taldilhnen sdrggsskhn tikkpqaqgr
      541 rpici
//
LOCUS       NP_001424266            1254 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase NEDD4-like isoform 8 [Homo sapiens].
ACCESSION   NP_001424266 XP_005266717 XP_054174358
VERSION     NP_001424266.1
DBSOURCE    REFSEQ: accession NM_001437337.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1254)
  AUTHORS   Chen,G., Pei,Y., Ye,Q., Xie,Z., Gyawali,L. and Liang,X.
  TITLE     NEDD4L-mediated RASGRP2 suppresses high-glucose and oxLDL-induced
            vascular endothelial cell dysfunctions by activating Rap1 and R-Ras
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (8), 119844 (2024)
   PUBMED   39260747
  REMARK    GeneRIF: NEDD4L-mediated RASGRP2 suppresses high-glucose and
            oxLDL-induced vascular endothelial cell dysfunctions by activating
            Rap1 and R-Ras.
REFERENCE   3  (residues 1 to 1254)
  AUTHORS   Wang,R., Wang,R., Zhou,S., Liu,T., Dang,J., Chen,Q., Chen,J. and
            Wang,Z.
  TITLE     Ubiquitination of angiotensin-converting enzyme 2 contributes to
            the development of pulmonary arterial hypertension mediated by
            neural precursor cell-expressed developmentally down-regulated gene
            4-Like
  JOURNAL   Respir Res 25 (1), 326 (2024)
   PUBMED   39210401
  REMARK    GeneRIF: Ubiquitination of angiotensin-converting enzyme 2
            contributes to the development of pulmonary arterial hypertension
            mediated by neural precursor cell-expressed developmentally
            down-regulated gene 4-Like.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1254)
  AUTHORS   Yang,B. and Kumar,S.
  TITLE     Nedd4 and Nedd4-2: closely related ubiquitin-protein ligases with
            distinct physiological functions
  JOURNAL   Cell Death Differ 17 (1), 68-77 (2010)
   PUBMED   19557014
  REMARK    Review article
REFERENCE   5  (residues 1 to 1254)
  AUTHORS   Russo,C.J., Melista,E., Cui,J., DeStefano,A.L., Bakris,G.L.,
            Manolis,A.J., Gavras,H. and Baldwin,C.T.
  TITLE     Association of NEDD4L ubiquitin ligase with essential hypertension
  JOURNAL   Hypertension 46 (3), 488-491 (2005)
   PUBMED   16103266
  REMARK    GeneRIF: Significant association between several SNPs and
            hypertension in US whites, Greek whites, and African-Americans.
            Genetic variation in NEDD4L may play role in development or
            progression of some forms of hypertension.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 1254)
  AUTHORS   Qi,H., Grenier,J., Fournier,A. and Labrie,C.
  TITLE     Androgens differentially regulate the expression of NEDD4L
            transcripts in LNCaP human prostate cancer cells
  JOURNAL   Mol Cell Endocrinol 210 (1-2), 51-62 (2003)
   PUBMED   14615060
  REMARK    GeneRIF: Results describe the isolation of three new NEDD4L
            transcripts designated NEDD4Lf, NEDD4Lg and NEDD4Lh, which encode
            different forms of the NEDD4L protein.
REFERENCE   7  (residues 1 to 1254)
  AUTHORS   Itani,O.A., Campbell,J.R., Herrero,J., Snyder,P.M. and Thomas,C.P.
  TITLE     Alternate promoters and variable splicing lead to hNedd4-2 isoforms
            with a C2 domain and varying number of WW domains
  JOURNAL   Am J Physiol Renal Physiol 285 (5), F916-F929 (2003)
   PUBMED   12876068
  REMARK    GeneRIF: Alternate transcripts of Nedd4-2 may interact with ENaC
            differently. hNedd4-2 has role in regulation of ENaC. Protein
            domains are important for Nedd4-2 function.
            GeneRIF: Identification of multiple splice forms and 5' variants of
            Nedd4l.  5' variants inhibit ENaC-mediated Na+ transport when
            reconstituted in FRT epithelia.  Other splice forms encode Nedd4L
            isoforms with 2 to 4 WW domains having varying affinity for ENaC.
REFERENCE   8  (residues 1 to 1254)
  AUTHORS   Chen,H., Ross,C.A., Wang,N., Huo,Y., MacKinnon,D.F., Potash,J.B.,
            Simpson,S.G., McMahon,F.J., DePaulo,J.R. Jr. and McInnis,M.G.
  TITLE     NEDD4L on human chromosome 18q21 has multiple forms of transcripts
            and is a homologue of the mouse Nedd4-2 gene
  JOURNAL   Eur J Hum Genet 9 (12), 922-930 (2001)
   PUBMED   11840194
  REMARK    GeneRIF: Candidate gene for autosomal dominant orthostatic
            hypotensive disorder.
REFERENCE   9  (residues 1 to 1254)
  AUTHORS   Winberg,G., Matskova,L., Chen,F., Plant,P., Rotin,D., Gish,G.,
            Ingham,R., Ernberg,I. and Pawson,T.
  TITLE     Latent membrane protein 2A of Epstein-Barr virus binds WW domain E3
            protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases
  JOURNAL   Mol Cell Biol 20 (22), 8526-8535 (2000)
   PUBMED   11046148
REFERENCE   10 (residues 1 to 1254)
  AUTHORS   Nuber,U., Schwarz,S., Kaiser,P., Schneider,R. and Scheffner,M.
  TITLE     Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7
            (E2-F1) and characterization of their interaction with E6-AP and
            RSP5
  JOURNAL   J Biol Chem 271 (5), 2795-2800 (1996)
   PUBMED   8576257
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC090236.4.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_005266717.3, XP_054174358.1.
            
            Summary: This gene encodes a member of the Nedd4 family of HECT
            domain E3 ubiquitin ligases. HECT domain E3 ubiquitin ligases
            transfer ubiquitin from E2 ubiquitin-conjugating enzymes to protein
            substrates, thus targeting specific proteins for lysosomal
            degradation. The encoded protein mediates the ubiquitination of
            multiple target substrates and plays a critical role in epithelial
            sodium transport by regulating the cell surface expression of the
            epithelial sodium channel, ENaC. Single nucleotide polymorphisms in
            this gene may be associated with essential hypertension.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene. [provided by RefSeq, Mar
            2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1067047.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144835
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.31"
     Protein         1..1254
                     /product="E3 ubiquitin-protein ligase NEDD4-like isoform
                     8"
                     /EC_number="2.3.2.26"
                     /EC_number="2.3.2.36"
                     /note="ubiquitin-protein ligase Rsp5; HECT-type E3
                     ubiquitin transferase NED4L; neural precursor cell
                     expressed, developmentally down-regulated 4-like, E3
                     ubiquitin protein ligase"
                     /calculated_mol_wt=140688
     Region          <79..404
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <379..432
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Region          477..503
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          666..695
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          779..809
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(793,804)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          828..860
                     /region_name="WW"
                     /note="Domain with 2 conserved Trp (W) residues;
                     smart00456"
                     /db_xref="CDD:197736"
     Site            order(844,855)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Site            order(903,934,945,1007,1180,1215..1216,1219..1223,1243,
                     1250)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Region          921..1250
                     /region_name="HECTc"
                     /note="Domain Homologous to E6-AP Carboxyl Terminus with;
                     smart00119"
                     /db_xref="CDD:214523"
     Site            order(1035,1038..1039,1041..1042,1045,1050,1052,
                     1056..1057,1059,1064,1069,1086,1090)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..1254
                     /gene="NEDD4L"
                     /gene_synonym="hNEDD4-2; NEDD4-2; NEDD4.2; PVNH7; RSP5"
                     /coded_by="NM_001437337.1:126..3890"
                     /note="isoform 8 is encoded by transcript variant m"
                     /db_xref="GeneID:23327"
                     /db_xref="HGNC:HGNC:7728"
                     /db_xref="MIM:606384"
ORIGIN      
        1 mahrlrfhfg sgrsntapes dildqeredd ffmafhtlpr rssphpfaqn ggedgggglq
       61 ggvgalkrss smfipqllts idarptcsss vqislqrkat dgatdgcgpp egaddgppca
      121 tpdprdqasa tattraspqs gsrepsprdt pgssppraar dpglqvngtc grrvrcsgpv
      181 dcaeeaapgl riqhrassad vrqvrllplg pdgqggpaaa eprrwslqhv pdasgssgkr
      241 cfvfqlqqpq qgasgpgsdl nfgftgtkgd rlvryprirl erstsyptqp rsergspted
      301 rgaleaspra grmapeirrt nsaertpqgq gctfkirqdq nagqqhfril vtrgpeeapq
      361 npeeksaksp vstgadtttr ddflgqvdvp lshlptedpt merpytfkdf llrprshksr
      421 vkgflrlkma ympknggqde ensdqrddme hgwevvdsnd sasqhqeelp ppplppgwee
      481 kvdnlgrtyy vnhnnrttqw hrpslmdvss esdnnirqin qeaahrrfrs rrhisedlep
      541 epseggdvpe pwetiseevn iagdslglal ppppaspgsr tspqelseel srrlqitpds
      601 ngeqfssliq repssrlrsc svtdavaeqg hlpppsapag rarsstvtgg eeptpsvayv
      661 httpglpsgw eerkdakgrt yyvnhnnrtt twtrpimqla edgasgsatn snnhliepqi
      721 rrprslsspt vtlsaplega kdspvrravk dtlsnpqspq pspynspkpq hkvtqsflpp
      781 gwemriapng rpffidhntk tttwedprlk fpvhmrskts lnpndlgplp pgweerihld
      841 grtfyidhns kitqwedprl qnpaitgpav pysrefkqky dyfrkklkkp adipnrfemk
      901 lhrnnifees yrrimsvkrp dvlkarlwie fesekgldyg gvarewffll skemfnpyyg
      961 lfeysatdny tlqinpnsgl cnedhlsyft figrvaglav fhgklldgff irpfykmmlg
     1021 kqitlndmes vdseyynslk wilendptel dlmfcideen fgqtyqvdlk pngseimvtn
     1081 enkreyidlv iqwrfvnrvq kqmnaflegf tellpidlik ifdenelell mcglgdvdvn
     1141 dwrqhsiykn gycpnhpviq wfwkavllmd aekrirllqf vtgtsrvpmn gfaelygsng
     1201 pqlftieqwg speklpraht cfnrldlppy etfedlrekl lmavenaqgf egvd
//
LOCUS       NP_001400298             316 aa            linear   PRI 21-NOV-2025
DEFINITION  telomeric repeat-binding factor 1 isoform 9 [Homo sapiens].
ACCESSION   NP_001400298
VERSION     NP_001400298.1
DBSOURCE    REFSEQ: accession NM_001413369.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Hu,H., van Roon,A.M., Ghanim,G.E., Ahsan,B., Oluwole,A.O.,
            Peak-Chew,S.Y., Robinson,C.V. and Nguyen,T.H.D.
  TITLE     Structural basis of telomeric nucleosome recognition by shelterin
            factor TRF1
  JOURNAL   Sci Adv 9 (34), eadi4148 (2023)
   PUBMED   37624885
  REMARK    GeneRIF: Structural basis of telomeric nucleosome recognition by
            shelterin factor TRF1.
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Harmak,H., Redouane,S., Charoute,H., Aniq Filali,O., Barakat,A. and
            Rouba,H.
  TITLE     In silico exploration and molecular dynamics of deleterious SNPs on
            the human TERF1 protein triggering male infertility
  JOURNAL   J Biomol Struct Dyn 41 (24), 14665-14688 (2023)
   PUBMED   36995171
  REMARK    GeneRIF: In silico exploration and molecular dynamics of
            deleterious SNPs on the human TERF1 protein triggering male
            infertility.
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Abreu,P.L., Lee,Y.W. and Azzalin,C.M.
  TITLE     In Vitro Characterization of the Physical Interactions between the
            Long Noncoding RNA TERRA and the Telomeric Proteins TRF1 and TRF2
  JOURNAL   Int J Mol Sci 23 (18), 10463 (2022)
   PUBMED   36142374
  REMARK    GeneRIF: In Vitro Characterization of the Physical Interactions
            between the Long Noncoding RNA TERRA and the Telomeric Proteins
            TRF1 and TRF2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Jack,A., Kim,Y., Strom,A.R., Lee,D.S.W., Williams,B., Schaub,J.M.,
            Kellogg,E.H., Finkelstein,I.J., Ferro,L.S., Yildiz,A. and
            Brangwynne,C.P.
  TITLE     Compartmentalization of telomeres through DNA-scaffolded phase
            separation
  JOURNAL   Dev Cell 57 (2), 277-290 (2022)
   PUBMED   35077681
  REMARK    GeneRIF: Compartmentalization of telomeres through DNA-scaffolded
            phase separation.
REFERENCE   6  (residues 1 to 316)
  AUTHORS   Broccoli,D., Chong,L., Oelmann,S., Fernald,A.A., Marziliano,N., van
            Steensel,B., Kipling,D., Le Beau,M.M. and de Lange,T.
  TITLE     Comparison of the human and mouse genes encoding the telomeric
            protein, TRF1: chromosomal localization, expression and conserved
            protein domains
  JOURNAL   Hum Mol Genet 6 (1), 69-76 (1997)
   PUBMED   9002672
REFERENCE   7  (residues 1 to 316)
  AUTHORS   Lu,K.P., Hanes,S.D. and Hunter,T.
  TITLE     A human peptidyl-prolyl isomerase essential for regulation of
            mitosis
  JOURNAL   Nature 380 (6574), 544-547 (1996)
   PUBMED   8606777
REFERENCE   8  (residues 1 to 316)
  AUTHORS   Bilaud,T., Koering,C.E., Binet-Brasselet,E., Ancelin,K.,
            Pollice,A., Gasser,S.M. and Gilson,E.
  TITLE     The telobox, a Myb-related telomeric DNA binding motif found in
            proteins from yeast, plants and human
  JOURNAL   Nucleic Acids Res 24 (7), 1294-1303 (1996)
   PUBMED   8614633
REFERENCE   9  (residues 1 to 316)
  AUTHORS   Chong,L., van Steensel,B., Broccoli,D., Erdjument-Bromage,H.,
            Hanish,J., Tempst,P. and de Lange,T.
  TITLE     A human telomeric protein
  JOURNAL   Science 270 (5242), 1663-1667 (1995)
   PUBMED   7502076
REFERENCE   10 (residues 1 to 316)
  AUTHORS   Zhong,Z., Shiue,L., Kaplan,S. and de Lange,T.
  TITLE     A mammalian factor that binds telomeric TTAGGG repeats in vitro
  JOURNAL   Mol Cell Biol 12 (11), 4834-4843 (1992)
   PUBMED   1406665
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022893.6.
            
            Summary: This gene encodes a telomere specific protein which is a
            component of the telomere nucleoprotein complex. This protein is
            present at telomeres throughout the cell cycle and functions as an
            inhibitor of telomerase, acting in cis to limit the elongation of
            individual chromosome ends. The protein structure contains a
            C-terminal Myb motif, a dimerization domain near its N-terminus and
            an acidic N-terminus. Multiple transcripts of this gene are
            alternatively spliced products. [provided by RefSeq, Aug 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.78042.1,
                                           SRR14038191.3148030.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2161674 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.11"
     Protein         1..316
                     /product="telomeric repeat-binding factor 1 isoform 9"
                     /note="NIMA-interacting protein 2; telomeric protein
                     Pin2/TRF1; TTAGGG repeat-binding factor 1; telomeric
                     repeat binding factor (NIMA-interacting) 1"
                     /calculated_mol_wt=36295
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54274.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P54274.3)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P54274.3)"
     Region          76..259
                     /region_name="TRFH"
                     /note="Telomeric Repeat binding Factor or TTAGGG Repeat
                     binding Factor, central (dimerization) domain Homology;
                     TRFH. Telomeres are protein/DNA complexes that make up the
                     physical ends of eukaryotic linear chromosomes and are
                     essential for chromosome stability; cd00280"
                     /db_xref="CDD:238174"
     Site            order(106,109,123,127,131,141..145,153,156..157,160)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238174"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000269|PubMed:11375976; propagated from
                     UniProtKB/Swiss-Prot (P54274.3)"
     Region          258..306
                     /region_name="SANT_TRF"
                     /note="Telomere repeat binding factor-like DNA-binding
                     domains of the SANT/myb-like family; cd11660"
                     /db_xref="CDD:212558"
     Site            order(258..260,278,280..281,292,294..296,298..300,
                     302..303)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212558"
     CDS             1..316
                     /gene="TERF1"
                     /gene_synonym="hTRF1-AS; PIN2; t-TRF1; TRBF1; TRF; TRF1"
                     /coded_by="NM_001413369.1:24..974"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:7013"
                     /db_xref="HGNC:HGNC:11728"
                     /db_xref="MIM:600951"
ORIGIN      
        1 maedvssaap sprgcadgrd adpteeqmae terndeeqfe cqellecqvq vgapeeeeee
       61 eedaglvaea eavaagwmld flclslcraf rdgrsedfrr trnsaeaiih glssltacql
      121 rtiyicqflt riaagktlda qfenderitp lesalmiwgs iekehdklhe eiqnlikiqa
      181 iavcmengnf keaeevferi fgdpnshmpf kskllmiisq kdtfhsffqh fsynhmmeki
      241 ksyvnyvlse ksstflmkaw lweedknlrs gvrkygegnw skillhykfn nrtsvmlkdr
      301 wrtmkklkli ssdsed
//
LOCUS       NP_001427521             413 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform i [Homo sapiens].
ACCESSION   NP_001427521
VERSION     NP_001427521.1
DBSOURCE    REFSEQ: accession NM_001440592.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 413)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 413)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 413)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 413)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 413)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1965299, SAMEA1966682
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..413
                     /product="polycomb protein EED isoform i"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=46592
     Region          96..140
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          148..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <162..410
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          193..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          240..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          309..340
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          385..409
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..413
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001440592.1:478..1719"
                     /note="isoform i is encoded by transcript variant 9"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdendd avsiesgtnt erpdtptntp
       61 napgrkswgk gkwkskkcky sfkcvnslke dhnqplfgvq fnwhskegdp lvfatvgsnr
      121 vtlyechsqg eirllqsyvd adadenfytc awtydsntsh pllavagsrg iiriinpitm
      181 qcikhyvghg nainelkfhp rdpnlllsvs kdhalrlwni qtdtlvaifg gveghrdevl
      241 sadydllgek imscgmdhsl klwrinskrm mnaikesydy npnktnrpfi sqkihfpdfs
      301 trdihrnyvd cvrwlgdlil sksgrailhs hqqcmrdpvs pnlrqhlmla lgnqvgklyv
      361 wdlevedphk akcttlthhk cgaairqtsf srdssiliav cddasiwrwd rlr
//
LOCUS       NP_001425598             839 aa            linear   PRI 21-NOV-2025
DEFINITION  dipeptidyl peptidase 8 isoform 7 [Homo sapiens].
ACCESSION   NP_001425598 XP_016877864 XP_054234278
VERSION     NP_001425598.1
DBSOURCE    REFSEQ: accession NM_001438669.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 839)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 839)
  AUTHORS   Li,K., Zhang,Y., Zhao,W., Wang,R., Li,Y., Wei,L., Wang,L., Chen,X.,
            Chen,Z., Liu,P., Nie,N., Tian,X. and Fu,R.
  TITLE     DPP8/9 inhibition attenuates the TGF-beta1-induced excessive
            deposition of extracellular matrix (ECM) in human mesangial cells
            via Smad and Akt signaling pathways
  JOURNAL   Toxicol Lett 395, 1-10 (2024)
   PUBMED   38458339
  REMARK    GeneRIF: DPP8/9 inhibition attenuates the TGF-beta1-induced
            excessive deposition of extracellular matrix (ECM) in human
            mesangial cells via Smad and Akt signaling pathways.
REFERENCE   3  (residues 1 to 839)
  AUTHORS   Zhang,Y., Li,K., Li,Y., Zhao,W., Wang,L., Chen,Z., Ma,X., Yao,T.,
            Wang,J., Dong,W., Li,X., Tian,X. and Fu,R.
  TITLE     Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the
            proximal renal tubule epithelial cells
  JOURNAL   Pharmacol Res 169, 105630 (2021)
   PUBMED   33932609
  REMARK    GeneRIF: Profibrotic mechanisms of DPP8 and DPP9 highly expressed
            in the proximal renal tubule epithelial cells.
REFERENCE   4  (residues 1 to 839)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 839)
  AUTHORS   Hollingsworth,L.R., Sharif,H., Griswold,A.R., Fontana,P.,
            Mintseris,J., Dagbay,K.B., Paulo,J.A., Gygi,S.P., Bachovchin,D.A.
            and Wu,H.
  TITLE     DPP9 sequesters the C terminus of NLRP1 to repress inflammasome
            activation
  JOURNAL   Nature 592 (7856), 778-783 (2021)
   PUBMED   33731932
REFERENCE   6  (residues 1 to 839)
  AUTHORS   Chen,Y.S., Chien,C.H., Goparaju,C.M., Hsu,J.T., Liang,P.H. and
            Chen,X.
  TITLE     Purification and characterization of human prolyl dipeptidase DPP8
            in Sf9 insect cells
  JOURNAL   Protein Expr Purif 35 (1), 142-146 (2004)
   PUBMED   15039077
REFERENCE   7  (residues 1 to 839)
  AUTHORS   Shu,H., Chen,S., Bi,Q., Mumby,M. and Brekken,D.L.
  TITLE     Identification of phosphoproteins and their phosphorylation sites
            in the WEHI-231 B lymphoma cell line
  JOURNAL   Mol Cell Proteomics 3 (3), 279-286 (2004)
   PUBMED   14729942
REFERENCE   8  (residues 1 to 839)
  AUTHORS   Qi,S.Y., Riviere,P.J., Trojnar,J., Junien,J.L. and Akinsanya,K.O.
  TITLE     Cloning and characterization of dipeptidyl peptidase 10, a new
            member of an emerging subgroup of serine proteases
  JOURNAL   Biochem J 373 (Pt 1), 179-189 (2003)
   PUBMED   12662155
REFERENCE   9  (residues 1 to 839)
  AUTHORS   Ajami,K., Abbott,C.A., Obradovic,M., Gysbers,V., Kahne,T.,
            McCaughan,G.W. and Gorrell,M.D.
  TITLE     Structural requirements for catalysis, expression, and dimerization
            in the CD26/DPIV gene family
  JOURNAL   Biochemistry 42 (3), 694-701 (2003)
   PUBMED   12534281
REFERENCE   10 (residues 1 to 839)
  AUTHORS   Abbott,C.A., Yu,D.M., Woollatt,E., Sutherland,G.R., McCaughan,G.W.
            and Gorrell,M.D.
  TITLE     Cloning, expression and chromosomal localization of a novel human
            dipeptidyl peptidase (DPP) IV homolog, DPP8
  JOURNAL   Eur J Biochem 267 (20), 6140-6150 (2000)
   PUBMED   11012666
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011846.16 and AC105129.4.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_016877864.1, XP_054234278.1.
            
            Summary: This gene encodes a member of the peptidase S9B family, a
            small family of dipeptidyl peptidases that are able to cleave
            peptide substrates at a prolyl bond. The encoded protein shares
            similarity with dipeptidyl peptidase IV in that it is ubiquitously
            expressed, and hydrolyzes the same substrates. These similarities
            suggest that, like dipeptidyl peptidase IV, this protein may play a
            role in T-cell activation and immune function. Alternatively
            spliced transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853566.9357.1,
                                           SRR14038196.3392637.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..839
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..839
                     /product="dipeptidyl peptidase 8 isoform 7"
                     /EC_number="3.4.14.5"
                     /note="prolyl dipeptidase DPP8; dipeptidyl peptidase VIII;
                     DPP VIII; dipeptidyl peptidase IV-related protein 1"
                     /calculated_mol_wt=96360
     Region          1..146
                     /region_name="Dpp_8_9_N"
                     /note="Dipeptidyl peptidase 8 and 9 N-terminal; pfam19520"
                     /db_xref="CDD:466112"
     Region          159..536
                     /region_name="DPPIV_N"
                     /note="Dipeptidyl peptidase IV (DPP IV) N-terminal region;
                     pfam00930"
                     /db_xref="CDD:395744"
     Region          628..832
                     /region_name="Peptidase_S9"
                     /note="Prolyl oligopeptidase family; pfam00326"
                     /db_xref="CDD:459761"
     CDS             1..839
                     /gene="DPP8"
                     /gene_synonym="DP8; DPRP-1; DPRP1; MST097; MSTP097;
                     MSTP135; MSTP141"
                     /coded_by="NM_001438669.1:216..2735"
                     /note="isoform 7 is encoded by transcript variant 11"
                     /db_xref="GeneID:54878"
                     /db_xref="HGNC:HGNC:16490"
                     /db_xref="MIM:606819"
ORIGIN      
        1 maaameteql gveifetadc eeniesqdrp klepfyvery swsqlkklla dtrkyhgymm
       61 akaphdfmfv krndpdgphs driyylamsg enrentlfys eipktinraa vlmlswkpll
      121 dlfqatldyg mysreeellr erkrigtvgi asydyhqgsg tflfqagsgi yhvkdggpqg
      181 ftqqplrpnl vetscpnirm dpklcpadpd wiafihsndi wisnivtree rrltyvhnel
      241 anmeedarsa gvatfvlqee fdrysgywwc pkaetstanp kvtfkmseim idaegriidv
      301 idkeliqpfe ilfegveyia ragwtpegky awsilldrsq trlqivlisp elfipveddv
      361 merqrliesv pdsvtpliiy eettdiwini hdifhvfpqs heeeiefifa secktgfrhl
      421 ykitsilkes kykrssgglp apsdfkcpik eeiaitsgew evlgrhgsni qvdevrrlvy
      481 fegtkdsple hhlyvvsyvn pgevtrltdr gyshsccisq hcdffiskys nqknphcvsl
      541 yklsspeddp tcktkefwat ildsagplpd ytppeifsfe sttgftlygm lykphdlqpg
      601 kkyptvlfiy ggpqvqlvnn rfkgvkyfrl ntlaslgyvv vvidnrgsch rglkfegafk
      661 ykmgqieidd qveglqylas rydfidldrv gihgwsyggy lslmalmqrs difrvaiaga
      721 pvtlwifydt gyterymghp dqneqgyylg svamqaekfp sepnrllllh gfldenvhfa
      781 htsillsflv ragkpydlqi ypqerhsirv pesgehyelh llhylqenlg sriaalkvi
//
LOCUS       NP_001422920            1062 aa            linear   PRI 21-NOV-2025
DEFINITION  histone deacetylase 4 isoform 3 [Homo sapiens].
ACCESSION   NP_001422920 XP_047302444 XP_054200732
VERSION     NP_001422920.1
DBSOURCE    REFSEQ: accession NM_001435991.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Liu,W. and Luo,G.
  TITLE     NEDD9 is transcriptionally regulated by HDAC4 and promotes breast
            cancer metastasis and macrophage M2 polarization via the
            FAK/NF-kappaB signaling pathway
  JOURNAL   Neoplasia 57, 101059 (2024)
   PUBMED   39326322
  REMARK    GeneRIF: NEDD9 is transcriptionally regulated by HDAC4 and promotes
            breast cancer metastasis and macrophage M2 polarization via the
            FAK/NF-kappaB signaling pathway.
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1062)
  AUTHORS   Di Giorgio,E., Dalla,E., Tolotto,V., D'Este,F., Paluvai,H.,
            Ranzino,L. and Brancolini,C.
  TITLE     HDAC4 influences the DNA damage response and counteracts senescence
            by assembling with HDAC1/HDAC2 to control H2BK120 acetylation and
            homology-directed repair
  JOURNAL   Nucleic Acids Res 52 (14), 8218-8240 (2024)
   PUBMED   38874468
  REMARK    GeneRIF: HDAC4 influences the DNA damage response and counteracts
            senescence by assembling with HDAC1/HDAC2 to control H2BK120
            acetylation and homology-directed repair.
REFERENCE   5  (residues 1 to 1062)
  AUTHORS   Chen,Q. and Lao,J.
  TITLE     Interference with Histone Deacetylase 4 Regulates c-Jun N-terminal
            Kinase/Activating Protein-1 Signaling to Ameliorate Sepsis-induced
            Alveolar Epithelial Cell Injury
  JOURNAL   J Physiol Investig 67 (4), 174-186 (2024)
   PUBMED   39133038
  REMARK    GeneRIF: Interference with Histone Deacetylase 4 Regulates c-Jun
            N-terminal Kinase/Activating Protein-1 Signaling to Ameliorate
            Sepsis-induced Alveolar Epithelial Cell Injury.
REFERENCE   6  (residues 1 to 1062)
  AUTHORS   Pazin,M.J. and Kadonaga,J.T.
  TITLE     What's up and down with histone deacetylation and transcription?
  JOURNAL   Cell 89 (3), 325-328 (1997)
   PUBMED   9150131
  REMARK    Review article
REFERENCE   7  (residues 1 to 1062)
  AUTHORS   Wolffe,A.P.
  TITLE     Transcriptional control. Sinful repression
  JOURNAL   Nature 387 (6628), 16-17 (1997)
   PUBMED   9139815
REFERENCE   8  (residues 1 to 1062)
  AUTHORS   Ohara,O., Nagase,T., Ishikawa,K., Nakajima,D., Ohira,M., Seki,N.
            and Nomura,N.
  TITLE     Construction and characterization of human brain cDNA libraries
            suitable for analysis of cDNA clones encoding relatively large
            proteins
  JOURNAL   DNA Res 4 (1), 53-59 (1997)
   PUBMED   9179496
REFERENCE   9  (residues 1 to 1062)
  AUTHORS   Wilson,L.C., Leverton,K., Oude Luttikhuis,M.E., Oley,C.A.,
            Flint,J., Wolstenholme,J., Duckett,D.P., Barrow,M.A., Leonard,J.V.,
            Read,A.P. et al.
  TITLE     Brachydactyly and mental retardation: an Albright hereditary
            osteodystrophy-like syndrome localized to 2q37
  JOURNAL   Am J Hum Genet 56 (2), 400-407 (1995)
   PUBMED   7847374
REFERENCE   10 (residues 1 to 1062)
  AUTHORS   Doherty,E.S. and Lacbawan,F.L.
  TITLE     2q37 Microdeletion Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301337
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC062017.6 and AC017028.11.
            
            On or before Jan 22, 2025 this sequence version replaced
            XP_047302444.1, XP_054200732.1.
            
            Summary: Histones play a critical role in transcriptional
            regulation, cell cycle progression, and developmental events.
            Histone acetylation/deacetylation alters chromosome structure and
            affects transcription factor access to DNA. The protein encoded by
            this gene belongs to class II of the histone deacetylase/acuc/apha
            family. It possesses histone deacetylase activity and represses
            transcription when tethered to a promoter. This protein does not
            bind DNA directly, but through transcription factors MEF2C and
            MEF2D. It seems to interact in a multiprotein complex with RbAp48
            and HDAC3. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1436928.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..1062
                     /product="histone deacetylase 4 isoform 3"
                     /EC_number="3.5.1.98"
                     /note="histone deacetylase A"
                     /calculated_mol_wt=116650
     Region          <64..125
                     /region_name="ClassIIa_HDAC4_Gln-rich-N"
                     /note="Glutamine-rich N-terminal helical domain of HDAC4,
                     a Class IIa histone deacetylase; cd10162"
                     /db_xref="CDD:197398"
     Site            order(66,70,81..82,85,92,96..97)
                     /site_type="other"
                     /note="dimer interface A, B [polypeptide binding]"
                     /db_xref="CDD:197398"
     Region          627..1035
                     /region_name="HDAC4"
                     /note="Histone deacetylase 4; cd10006"
                     /db_xref="CDD:212530"
     Site            order(780..781,789..790,818,820,912,952)
                     /site_type="active"
                     /db_xref="CDD:212530"
     CDS             1..1062
                     /gene="HDAC4"
                     /gene_synonym="AHO3; BDMR; HA6116; HD4; HDAC-4; HDAC-A;
                     HDACA; NEDCHF; NEDCHID"
                     /coded_by="NM_001435991.1:320..3508"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="GeneID:9759"
                     /db_xref="HGNC:HGNC:14063"
                     /db_xref="MIM:605314"
ORIGIN      
        1 mpstvdvata lplqvapsav pmdlrldhqf slpvaepalr eqqlqqella lkqkqqiqrq
       61 iliaefqrqh eqlsrqheaq lhehikqqqe mlamkhqqel lehqrklerh rqeqelekqh
      121 reqklqqlkn kekgkesava stevkmklqe fvlnkkkala hrnlnhciss dprywygktq
      181 hssldqsspp qsgvstsynh pvlgmydakd dfplrktase pnlklrsrlk qkvaerrssp
      241 llrrkdgpvv talkkrpldv tdsacssapg sgpsspnnss gsvsaengia pavpsipaet
      301 slahrlvare gsaaplplyt spslpnitlg lpatgpsagt agqqdaerlt lpalqqrlsl
      361 fpgthltpyl stsplerdgg aahspllqhm vlleqppaqa plvtdwylsg lgalplhaqs
      421 lvgadrvsps ihklrqhrpl grtqsaplpq naqalqhlvi qqqhqqflek hkqqfqqqql
      481 qmnkiipkps eparqpeshp eeteeelreh qalldepyld rlpgqkeaha qagvqvkqep
      541 iesdeeeaep prevepgqrq pseqellfrq qallleqqri hqlrnyqasm eaagipvsfg
      601 ghrplsraqs spasatfpvs vqepptkprf ttglvydtlm lkhqctcgss sshpehagri
      661 qsiwsrlqet glrgkcecir grkatleelq tvhseahtll ygtnplnrqk ldskkllgsl
      721 asvfvrlpcg gvgvdsdtiw nevhsagaar lavgcvvelv fkvatgelkn gfavvrppgh
      781 haeestpmgf cyfnsvavaa kllqqrlsvs kilivdwdvh hgngtqqafy sdpsvlymsl
      841 hryddgnffp gsgapdevgt gpgvgfnvnm aftggldppm gdaeylaafr tvvmpiasef
      901 apdvvlvssg fdaveghptp lggynlsarc fgyltkqlmg laggrivlal egghdltaic
      961 daseacvsal lgneldplpe kvlqqrpnan avrsmekvme ihskywrclq rttstagrsl
     1021 ieaqtcenee aetvtamasl svgvkpaekr pdeepmeeep pl
//
LOCUS       NP_001400614             321 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 18 precursor [Homo sapiens].
ACCESSION   NP_001400614
VERSION     NP_001400614.1
DBSOURCE    REFSEQ: accession NM_001413685.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 321)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..321
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 18 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=32106
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..312
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            277..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     CDS             1..321
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413685.1:169..1134"
                     /note="isoform 18 precursor is encoded by transcript
                     variant 21"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvsyih gssqaqfvae shiilvlnaa itmgmvllne
      301 aatskgdvgk rrneetlire v
//
LOCUS       NP_001393926             478 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform K [Homo sapiens].
ACCESSION   NP_001393926
VERSION     NP_001393926.1
DBSOURCE    REFSEQ: accession NM_001406997.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 478)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 478)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1965465.1,
                                           SRR12921934.1750030.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..478
                     /product="lamin isoform K"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=53246
     Region          <1..200
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          248..355
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     CDS             1..478
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406997.1:300..1736"
                     /note="isoform K is encoded by transcript variant 22"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 mlrrvdaenr lqtmkeeldf qkniyseelr etkrrhetrl veidngkqre fesrladalq
       61 elraqhedqv eqykkelekt ysakldnarq saernsnlvg aaheelqqsr iridslsaql
      121 sqlqkqlaak eaklrdleds larerdtsrr llaekerema emrarmqqql deyqelldik
      181 laldmeihay rkllegeeer lrlspsptsq rsrgrasshs sqtqgggsvt kkrklestes
      241 rssfsqhart sgrvaveevd eegkfvrlrn ksnedqsmgn wqikrqngdd plltyrfppk
      301 ftlkagqvvt iwaagagath spptdlvwka qntwgcgnsl rtalinstge evamrklvrs
      361 vtvveddede dgddllhhhh gshcsssgdp aeynlrsrtv lcgtcgqpad kasasgsgaq
      421 vggpissgss assvtvtrsy rsvggsgggs fgdnlvtrsy llgnssprtq spqncsim
//
LOCUS       NP_001400000             333 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001400000
VERSION     NP_001400000.1
DBSOURCE    REFSEQ: accession NM_001413071.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.576143.1,
                                           SRR18074967.735237.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..333
                     /product="mitochondrial fission regulator 1 isoform 1
                     precursor"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=31469
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=5550
     Region          22..251
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     mat_peptide     49..333
                     /product="Mitochondrial fission regulator 1.
                     /id=PRO_0000096622"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=31469
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15390.2)"
     Region          177..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          179..304
                     /region_name="Necessary and sufficient to promote
                     mitochondrial fission. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          288..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     CDS             1..333
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001413071.1:154..1155"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsvlwsrkpy gssrsivrki gtnlsliqcp rvqfqinsha
       61 tewspshpge davasfadvg wvakeegecs arlrtevrsr pplqddllff ekapsrqisl
      121 pdlsqeepql ktpalaneea lqkicalene laalraqiak ivtqqeqqnl tagdldsttf
      181 gtipphpppp ppplpppalg lhqstsavdl ikerrekran agktlvknnp kkpempnmle
      241 ilkemnsvkl rsvkrseqdv kpkpvdatdp aaliaealkk kfayryrsds qdevekgipk
      301 seseatserv lfgphmlkpt gkmkalienv sds
//
LOCUS       NP_001411254             225 aa            linear   PRI 21-NOV-2025
DEFINITION  protein cholesin isoform d [Homo sapiens].
ACCESSION   NP_001411254
VERSION     NP_001411254.1
DBSOURCE    REFSEQ: accession NM_001424325.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Ryk,A., Marcinkiewicz,A., Chrzanowski,J., Michalak,A.M., Drozdz,I.,
            Burzynski,J., Krejca,M. and Fendler,W.
  TITLE     Cholesin receptor signalling is active in cardiovascular
            system-associated adipose tissue and correlates with SGLT2i
            treatment in patients with diabetes
  JOURNAL   Cardiovasc Diabetol 23 (1), 211 (2024)
   PUBMED   38902687
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Hu,X., Chen,F., Jia,L., Long,A., Peng,Y., Li,X., Huang,J., Wei,X.,
            Fang,X., Gao,Z., Zhang,M., Liu,X., Chen,Y.G., Wang,Y., Zhang,H. and
            Wang,Y.
  TITLE     A gut-derived hormone regulates cholesterol metabolism
  JOURNAL   Cell 187 (7), 1685-1700 (2024)
   PUBMED   38503280
  REMARK    GeneRIF: A gut-derived hormone regulates cholesterol metabolism.
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 225)
  AUTHORS   Willer,C.J., Schmidt,E.M., Sengupta,S., Peloso,G.M., Gustafsson,S.,
            Kanoni,S., Ganna,A., Chen,J., Buchkovich,M.L., Mora,S.,
            Beckmann,J.S., Bragg-Gresham,J.L., Chang,H.Y., Demirkan,A., Den
            Hertog,H.M., Do,R., Donnelly,L.A., Ehret,G.B., Esko,T.,
            Feitosa,M.F., Ferreira,T., Fischer,K., Fontanillas,P., Fraser,R.M.,
            Freitag,D.F., Gurdasani,D., Heikkila,K., Hypponen,E., Isaacs,A.,
            Jackson,A.U., Johansson,A., Johnson,T., Kaakinen,M., Kettunen,J.,
            Kleber,M.E., Li,X., Luan,J., Lyytikainen,L.P., Magnusson,P.K.E.,
            Mangino,M., Mihailov,E., Montasser,M.E., Muller-Nurasyid,M.,
            Nolte,I.M., O'Connell,J.R., Palmer,C.D., Perola,M., Petersen,A.K.,
            Sanna,S., Saxena,R., Service,S.K., Shah,S., Shungin,D., Sidore,C.,
            Song,C., Strawbridge,R.J., Surakka,I., Tanaka,T., Teslovich,T.M.,
            Thorleifsson,G., Van den Herik,E.G., Voight,B.F., Volcik,K.A.,
            Waite,L.L., Wong,A., Wu,Y., Zhang,W., Absher,D., Asiki,G.,
            Barroso,I., Been,L.F., Bolton,J.L., Bonnycastle,L.L., Brambilla,P.,
            Burnett,M.S., Cesana,G., Dimitriou,M., Doney,A.S.F., Doring,A.,
            Elliott,P., Epstein,S.E., Ingi Eyjolfsson,G., Gigante,B.,
            Goodarzi,M.O., Grallert,H., Gravito,M.L., Groves,C.J., Hallmans,G.,
            Hartikainen,A.L., Hayward,C., Hernandez,D., Hicks,A.A., Holm,H.,
            Hung,Y.J., Illig,T., Jones,M.R., Kaleebu,P., Kastelein,J.J.P.,
            Khaw,K.T., Kim,E., Klopp,N., Komulainen,P., Kumari,M.,
            Langenberg,C., Lehtimaki,T., Lin,S.Y., Lindstrom,J., Loos,R.J.F.,
            Mach,F., McArdle,W.L., Meisinger,C., Mitchell,B.D., Muller,G.,
            Nagaraja,R., Narisu,N., Nieminen,T.V.M., Nsubuga,R.N., Olafsson,I.,
            Ong,K.K., Palotie,A., Papamarkou,T., Pomilla,C., Pouta,A.,
            Rader,D.J., Reilly,M.P., Ridker,P.M., Rivadeneira,F., Rudan,I.,
            Ruokonen,A., Samani,N., Scharnagl,H., Seeley,J., Silander,K.,
            Stancakova,A., Stirrups,K., Swift,A.J., Tiret,L.,
            Uitterlinden,A.G., van Pelt,L.J., Vedantam,S., Wainwright,N.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilsgaard,T., Wilson,J.F.,
            Young,E.H., Zhao,J.H., Adair,L.S., Arveiler,D., Assimes,T.L.,
            Bandinelli,S., Bennett,F., Bochud,M., Boehm,B.O., Boomsma,D.I.,
            Borecki,I.B., Bornstein,S.R., Bovet,P., Burnier,M., Campbell,H.,
            Chakravarti,A., Chambers,J.C., Chen,Y.I., Collins,F.S.,
            Cooper,R.S., Danesh,J., Dedoussis,G., de Faire,U., Feranil,A.B.,
            Ferrieres,J., Ferrucci,L., Freimer,N.B., Gieger,C., Groop,L.C.,
            Gudnason,V., Gyllensten,U., Hamsten,A., Harris,T.B., Hingorani,A.,
            Hirschhorn,J.N., Hofman,A., Hovingh,G.K., Hsiung,C.A.,
            Humphries,S.E., Hunt,S.C., Hveem,K., Iribarren,C., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kaprio,J., Kesaniemi,A., Kivimaki,M.,
            Kooner,J.S., Koudstaal,P.J., Krauss,R.M., Kuh,D., Kuusisto,J.,
            Kyvik,K.O., Laakso,M., Lakka,T.A., Lind,L., Lindgren,C.M.,
            Martin,N.G., Marz,W., McCarthy,M.I., McKenzie,C.A., Meneton,P.,
            Metspalu,A., Moilanen,L., Morris,A.D., Munroe,P.B., Njolstad,I.,
            Pedersen,N.L., Power,C., Pramstaller,P.P., Price,J.F., Psaty,B.M.,
            Quertermous,T., Rauramaa,R., Saleheen,D., Salomaa,V.,
            Sanghera,D.K., Saramies,J., Schwarz,P.E.H., Sheu,W.H.,
            Shuldiner,A.R., Siegbahn,A., Spector,T.D., Stefansson,K.,
            Strachan,D.P., Tayo,B.O., Tremoli,E., Tuomilehto,J., Uusitupa,M.,
            van Duijn,C.M., Vollenweider,P., Wallentin,L., Wareham,N.J.,
            Whitfield,J.B., Wolffenbuttel,B.H.R., Ordovas,J.M., Boerwinkle,E.,
            Palmer,C.N.A., Thorsteinsdottir,U., Chasman,D.I., Rotter,J.I.,
            Franks,P.W., Ripatti,S., Cupples,L.A., Sandhu,M.S., Rich,S.S.,
            Boehnke,M., Deloukas,P., Kathiresan,S., Mohlke,K.L., Ingelsson,E.
            and Abecasis,G.R.
  CONSRTM   Global Lipids Genetics Consortium
  TITLE     Discovery and refinement of loci associated with lipid levels
  JOURNAL   Nat Genet 45 (11), 1274-1283 (2013)
   PUBMED   24097068
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Yashin,A.I., Wu,D., Arbeev,K.G. and Ukraintseva,S.V.
  TITLE     Joint influence of small-effect genetic variants on human longevity
  JOURNAL   Aging (Albany NY) 2 (9), 612-620 (2010)
   PUBMED   20834067
REFERENCE   9  (residues 1 to 225)
  AUTHORS   Satoh,J., Obayashi,S., Misawa,T., Sumiyoshi,K., Oosumi,K. and
            Tabunoki,H.
  TITLE     Protein microarray analysis identifies human cellular prion protein
            interactors
  JOURNAL   Neuropathol Appl Neurobiol 35 (1), 16-35 (2009)
   PUBMED   18482256
REFERENCE   10 (residues 1 to 225)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091729.4 and AC073957.7.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3485593.1,
                                           SRR14478891.1397768.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..225
                     /product="protein cholesin isoform d"
                     /note="uncharacterized protein C7orf50; protein cholesin"
                     /calculated_mol_wt=25056
     Region          1..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Region          104..165
                     /region_name="WKF"
                     /note="WKF domain; pfam10180"
                     /db_xref="CDD:462982"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     CDS             1..225
                     /gene="CHLSN"
                     /gene_synonym="C7orf50; YCR016W"
                     /coded_by="NM_001424325.1:61..738"
                     /note="isoform d is encoded by transcript variant 15"
                     /db_xref="GeneID:84310"
                     /db_xref="HGNC:HGNC:22421"
                     /db_xref="MIM:621174"
ORIGIN      
        1 makqkrkvpe vtekknkklk kasaegpllg peaapsgega gskgeavlrp gldaepelsp
       61 eeqrvlerkl kkerkkeerq rlreaglvaq hpparrsgae laldylcrwa qkhknwrfqk
      121 trqtwlllhm ydsdkvpdeh fstllayleg lqgrareltv qkaealmrel deegsdpplp
      181 graqrirqdt cavdpaamlw gspaarrgah vegnpgprnr gqast
//
LOCUS       NP_001425391             435 aa            linear   PRI 21-NOV-2025
DEFINITION  excitatory amino acid transporter 1 isoform 9 [Homo sapiens].
ACCESSION   NP_001425391 XP_047273496 XP_054209166
VERSION     NP_001425391.1
DBSOURCE    REFSEQ: accession NM_001438462.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Albury,C.L., Sutherland,H.G., Lam,A.W.Y., Tran,N.K., Lea,R.A.,
            Haupt,L.M. and Griffiths,L.R.
  TITLE     Identification of Polymorphisms in EAAT1 Glutamate Transporter Gene
            SLC1A3 Associated with Reduced Migraine Risk
  JOURNAL   Genes (Basel) 15 (6), 797 (2024)
   PUBMED   38927733
  REMARK    GeneRIF: Identification of Polymorphisms in EAAT1 Glutamate
            Transporter Gene SLC1A3 Associated with Reduced Migraine Risk.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Welby,E. and Ebert,A.D.
  TITLE     Diminished motor neuron activity driven by abnormal astrocytic
            EAAT1 glutamate transporter activity in spinal muscular atrophy is
            not fully restored after lentiviral SMN delivery
  JOURNAL   Glia 71 (5), 1311-1332 (2023)
   PUBMED   36655314
  REMARK    GeneRIF: Diminished motor neuron activity driven by abnormal
            astrocytic EAAT1 glutamate transporter activity in spinal muscular
            atrophy is not fully restored after lentiviral SMN delivery.
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Pant,S., Wu,Q., Ryan,R. and Tajkhorshid,E.
  TITLE     Microscopic Characterization of the Chloride Permeation Pathway in
            the Human Excitatory Amino Acid Transporter 1 (EAAT1)
  JOURNAL   ACS Chem Neurosci 13 (6), 776-785 (2022)
   PUBMED   35192345
  REMARK    GeneRIF: Microscopic Characterization of the Chloride Permeation
            Pathway in the Human Excitatory Amino Acid Transporter 1 (EAAT1).
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Lee,A., Anderson,A.R., Beasley,S.J., Barnett,N.L., Poronnik,P. and
            Pow,D.V.
  TITLE     A new splice variant of the glutamate-aspartate transporter:
            cloning and immunolocalization of GLAST1c in rat, pig and human
            brains
  JOURNAL   J Chem Neuroanat 43 (1), 52-63 (2012)
   PUBMED   22026960
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Vallejo-Illarramendi,A., Domercq,M. and Matute,C.
  TITLE     A novel alternative splicing form of excitatory amino acid
            transporter 1 is a negative regulator of glutamate uptake
  JOURNAL   J Neurochem 95 (2), 341-348 (2005)
   PUBMED   16042756
  REMARK    GeneRIF: EAAT1ex9skip splice variant is a negative regulator of
            full-length EAAT1 function in the human brain
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Takai,S., Yamada,K., Kawakami,H., Tanaka,K. and Nakamura,S.
  TITLE     Localization of the gene (SLC1A3) encoding human glutamate
            transporter (GluT-1) to 5p13 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 209-210 (1995)
   PUBMED   7698014
REFERENCE   8  (residues 1 to 435)
  AUTHORS   Shashidharan,P., Huntley,G.W., Meyer,T., Morrison,J.H. and
            Plaitakis,A.
  TITLE     Neuron-specific human glutamate transporter: molecular cloning,
            characterization and expression in human brain
  JOURNAL   Brain Res 662 (1-2), 245-250 (1994)
   PUBMED   7859077
REFERENCE   9  (residues 1 to 435)
  AUTHORS   Arriza,J.L., Fairman,W.A., Wadiche,J.I., Murdoch,G.H.,
            Kavanaugh,M.P. and Amara,S.G.
  TITLE     Functional comparisons of three glutamate transporter subtypes
            cloned from human motor cortex
  JOURNAL   J Neurosci 14 (9), 5559-5569 (1994)
   PUBMED   7521911
REFERENCE   10 (residues 1 to 435)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010631.6 and AC008957.7.
            
            On or before Apr 21, 2025 this sequence version replaced
            XP_047273496.1, XP_054209166.1.
            
            Summary: This gene encodes a member of a member of a high affinity
            glutamate transporter family. This gene functions in the
            termination of excitatory neurotransmission in central nervous
            system. Mutations are associated with episodic ataxia, Type 6.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2451085.1,
                                           SRR11853566.22036.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..435
                     /product="excitatory amino acid transporter 1 isoform 9"
                     /note="excitatory amino acid transporter 1; GLAST-1;
                     sodium-dependent glutamate/aspartate transporter 1; solute
                     carrier family 1 (glial high affinity glutamate
                     transporter), member 3"
                     /calculated_mol_wt=47153
     Region          5..389
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     CDS             1..435
                     /gene="SLC1A3"
                     /gene_synonym="EA6; EAAT1; GLAST; GLAST1"
                     /coded_by="NM_001438462.1:649..1956"
                     /note="isoform 9 is encoded by transcript variant 14"
                     /db_xref="GeneID:6507"
                     /db_xref="HGNC:HGNC:10941"
                     /db_xref="MIM:600111"
ORIGIN      
        1 maaldskasg kmgmravvyy mtttiiavvi giiiviiihp gkgtkenmhr egkivrvtaa
       61 dafldlirnm fppnlveacf kqfktnyekr sfkvpiqane tlvgavinnv seametltri
      121 teelvpvpgs vngvnalglv vfsmcfgfvi gnmkeqgqal reffdslnea imrlvavimw
      181 yapvgilfli agkivemedm gviggqlamy tvtvivglli havivlplly flvtrknpwv
      241 figgllqali talgtssssa tlpitfkcle enngvdkrvt rfvlpvgati nmdgtalyea
      301 laaifiaqvn nfelnfgqii tisitataas igaagipqag lvtmvivlts vglptdditl
      361 iiavdwfldr lrtttnvlgd slgagivehl srhelknrdv emgnsvieen emkkpyqlia
      421 qdnetekpid setkm
//
LOCUS       NP_001394255             294 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 27 [Homo sapiens].
ACCESSION   NP_001394255
VERSION     NP_001394255.1
DBSOURCE    REFSEQ: accession NM_001407326.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 294)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 294)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 294)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 294)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3780878.1,
                                           SRR14372079.3232146.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2144835
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..294
                     /product="tropomyosin alpha-1 chain isoform 27"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=33846
     Region          48..282
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..294
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407326.1:84..968"
                     /note="isoform 27 is encoded by transcript variant 27"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle delvslqkkl kgtedeldky
       61 sealkdaqek lelaekkatd aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegqv rqleeqlrim dqtlkalmaa edkysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledel yaqklkykai seeldhalnd mtsiesgscq rrkp
//
LOCUS       NP_075418                732 aa            linear   PRI 21-NOV-2025
DEFINITION  fibroblast growth factor receptor 2 isoform 11 precursor [Homo
            sapiens].
ACCESSION   NP_075418 XP_024303655 XP_054221144
VERSION     NP_075418.1
DBSOURCE    REFSEQ: accession NM_023029.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Chen,C.P., Huang,J.P., Huang,K.S., Chen,Y.Y., Wu,F.T., Pan,Y.T.,
            Chiu,C.L. and Wang,W.
  TITLE     Perinatal imaging findings of a fetus with Pfeiffer syndrome and a
            heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation in FGFR2
            presenting a cloverleaf skull, craniosynostosis and short limbs on
            prenatal ultrasound mimicking thanatophoric dysplasia type II
  JOURNAL   Taiwan J Obstet Gynecol 63 (3), 387-390 (2024)
   PUBMED   38802203
  REMARK    GeneRIF: Perinatal imaging findings of a fetus with Pfeiffer
            syndrome and a heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation
            in FGFR2 presenting a cloverleaf skull, craniosynostosis and short
            limbs on prenatal ultrasound mimicking thanatophoric dysplasia type
            II.
REFERENCE   2  (residues 1 to 732)
  AUTHORS   Lian,Y., Bodian,D. and Shehu,A.
  TITLE     Elucidating the Role of Wildtype and Variant FGFR2 Structural
            Dynamics in (Dys)Function and Disorder
  JOURNAL   Int J Mol Sci 25 (8), 4523 (2024)
   PUBMED   38674107
  REMARK    GeneRIF: Elucidating the Role of Wildtype and Variant FGFR2
            Structural Dynamics in (Dys)Function and Disorder.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 732)
  AUTHORS   Xu,N., Hung,K.L., Gong,X., Fan,D., Tian,Y., Yan,M., Wei,Y. and
            Wang,S.
  TITLE     Genetic insights into the 'sandwich fusion' subtype of Klippel-Feil
            syndrome: novel FGFR2 mutations identified by 21 cases of
            whole-exome sequencing
  JOURNAL   Orphanet J Rare Dis 19 (1), 141 (2024)
   PUBMED   38561822
  REMARK    GeneRIF: Genetic insights into the 'sandwich fusion' subtype of
            Klippel-Feil syndrome: novel FGFR2 mutations identified by 21 cases
            of whole-exome sequencing.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 732)
  AUTHORS   Wenger,T.L., Hing,A.V. and Evans,K.N.
  TITLE     Apert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31145570
REFERENCE   5  (residues 1 to 732)
  AUTHORS   Wenger,T., Miller,D. and Evans,K.
  TITLE     FGFR Craniosynostosis Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301628
REFERENCE   6  (residues 1 to 732)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   7  (residues 1 to 732)
  AUTHORS   Dell,K.R. and Williams,L.T.
  TITLE     A novel form of fibroblast growth factor receptor 2. Alternative
            splicing of the third immunoglobulin-like domain confers ligand
            binding specificity
  JOURNAL   J Biol Chem 267 (29), 21225-21229 (1992)
   PUBMED   1400433
REFERENCE   8  (residues 1 to 732)
  AUTHORS   Luqmani,Y.A., Graham,M. and Coombes,R.C.
  TITLE     Expression of basic fibroblast growth factor, FGFR1 and FGFR2 in
            normal and malignant human breast, and comparison with other normal
            tissues
  JOURNAL   Br J Cancer 66 (2), 273-280 (1992)
   PUBMED   1380281
REFERENCE   9  (residues 1 to 732)
  AUTHORS   Katoh,M., Hattori,Y., Sasaki,H., Tanaka,M., Sugano,K., Yazaki,Y.,
            Sugimura,T. and Terada,M.
  TITLE     K-sam gene encodes secreted as well as transmembrane receptor
            tyrosine kinase
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 2960-2964 (1992)
   PUBMED   1313574
REFERENCE   10 (residues 1 to 732)
  AUTHORS   Miki,T., Bottaro,D.P., Fleming,T.P., Smith,C.L., Burgess,W.H.,
            Chan,A.M. and Aaronson,S.A.
  TITLE     Determination of ligand-binding specificity by alternative
            splicing: two distinct growth factor receptors encoded by a single
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 246-250 (1992)
   PUBMED   1309608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009988.12.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_024303655.1, XP_054221144.1.
            
            Summary: The protein encoded by this gene is a member of the
            fibroblast growth factor receptor family, where amino acid sequence
            is highly conserved between members and throughout evolution. FGFR
            family members differ from one another in their ligand affinities
            and tissue distribution. A full-length representative protein
            consists of an extracellular region, composed of three
            immunoglobulin-like domains, a single hydrophobic membrane-spanning
            segment and a cytoplasmic tyrosine kinase domain. The extracellular
            portion of the protein interacts with fibroblast growth factors,
            setting in motion a cascade of downstream signals, ultimately
            influencing mitogenesis and differentiation. This particular family
            member is a high-affinity receptor for acidic, basic and/or
            keratinocyte growth factor, depending on the isoform. Mutations in
            this gene are associated with Crouzon syndrome, Pfeiffer syndrome,
            Craniosynostosis, Apert syndrome, Jackson-Weiss syndrome,
            Beare-Stevenson cutis gyrata syndrome, Saethre-Chotzen syndrome,
            and syndromic craniosynostosis. Multiple alternatively spliced
            transcript variants encoding different isoforms have been noted for
            this gene. [provided by RefSeq, Jan 2009].
            
            Transcript Variant: This variant (11) lacks an in-frame coding exon
            in the 5' region, compared to variant 1. This results in a shorter
            isoform (11) lacking an internal protein segment compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: EF057068.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: community standard (PMID:
                                                15863034)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..732
                     /product="fibroblast growth factor receptor 2 isoform 11
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="protein tyrosine kinase, receptor like 14;
                     bacteria-expressed kinase; keratinocyte growth factor
                     receptor; BEK fibroblast growth factor receptor"
                     /calculated_mol_wt=79946
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2298
     mat_peptide     22..732
                     /product="fibroblast growth factor receptor 2 isoform 11"
                     /calculated_mol_wt=79946
     Region          65..159
                     /region_name="IgI_2_FGFR"
                     /note="Second immunoglobulin (Ig)-like domain of
                     fibroblast growth factor (FGF) receptor; member of the
                     I-set of IgSF domains; cd05857"
                     /db_xref="CDD:409443"
     Region          65..68
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409443"
     Region          76..81
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409443"
     Site            order(77,79,81)
                     /site_type="other"
                     /note="FGF binding site [polypeptide binding]"
                     /db_xref="CDD:409443"
     Site            order(78,85..87,89)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409443"
     Region          85..93
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409443"
     Region          99..104
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409443"
     Region          107..109
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409443"
     Region          118..121
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409443"
     Region          125..130
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409443"
     Region          139..146
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409443"
     Region          149..159
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409443"
     Region          167..271
                     /region_name="IgI_3_FGFR2"
                     /note="Third immunoglobulin (Ig)-like domain of fibroblast
                     growth factor receptor 2 (FGFR2); member of the I-set of
                     Ig superfamily (IgSF) domains; cd05858"
                     /db_xref="CDD:409444"
     Region          167..170
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409444"
     Region          174..178
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409444"
     Region          186..193
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409444"
     Site            order(191,196..198,227..228,232,236,257)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409444"
     Region          197..204
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409444"
     Region          219..224
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409444"
     Region          236..241
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409444"
     Region          249..257
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409444"
     Region          260..268
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409444"
     Region          367..679
                     /region_name="PTKc_FGFR2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Fibroblast Growth Factor Receptor 2; cd05101"
                     /db_xref="CDD:270679"
     Site            order(398..399,401,406,426,428,445,475..478,482,537,
                     541..542,544,555,573..577,586,620)
                     /site_type="active"
                     /db_xref="CDD:270679"
     Site            order(398..399,401,406,426,428,445,475..478,482,541..542,
                     544,555)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270679"
     Site            order(537,541,573..577,586,620)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270679"
     Site            554..579
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270679"
     CDS             1..732
                     /gene="FGFR2"
                     /gene_synonym="BBDS; BEK; BFR-1; CD332; CEK3; CFD1; ECT1;
                     JWS; K-SAM; KGFR; TK14; TK25"
                     /coded_by="NM_023029.3:634..2832"
                     /note="isoform 11 precursor is encoded by transcript
                     variant 11"
                     /db_xref="CCDS:CCDS73210.1"
                     /db_xref="GeneID:2263"
                     /db_xref="HGNC:HGNC:3689"
                     /db_xref="MIM:176943"
ORIGIN      
        1 mvswgrficl vvvtmatlsl arpsfslved ttlepedais sgddeddtdg aedfvsensn
       61 nkrapywtnt ekmekrlhav paantvkfrc paggnpmptm rwlkngkefk qehriggykv
      121 rnqhwslime svvpsdkgny tcvveneygs inhtyhldvv ersphrpilq aglpanastv
      181 vggdvefvck vysdaqphiq wikhvekngs kygpdglpyl kvlkaagvnt tdkeievlyi
      241 rnvtfedage ytclagnsig isfhsawltv lpapgrekei taspdyleia iycigvflia
      301 cmvvtvilcr mknttkkpdf ssqpavhklt kriplrrqvt vsaessssmn sntplvritt
      361 rlsstadtpm lagvseyelp edpkwefprd kltlgkplge gcfgqvvmae avgidkdkpk
      421 eavtvavkml kddatekdls dlvsememmk migkhkniin llgactqdgp lyviveyask
      481 gnlreylrar rppgmeysyd inrvpeeqmt fkdlvsctyq largmeylas qkcihrdlaa
      541 rnvlvtennv mkiadfglar dinnidyykk ttngrlpvkw mapealfdrv ythqsdvwsf
      601 gvlmweiftl ggspypgipv eelfkllkeg hrmdkpanct nelymmmrdc whavpsqrpt
      661 fkqlvedldr iltlttneey ldlsqpleqy spsypdtrss cssgddsvfs pdpmpyepcl
      721 pqyphingsv kt
//
LOCUS       NP_001389631            1270 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 12 [Homo sapiens].
ACCESSION   NP_001389631 XP_047287318
VERSION     NP_001389631.1
DBSOURCE    REFSEQ: accession NM_001402702.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1270)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1270)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1270)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1270)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1270)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1270)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1270)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1270)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1270)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1270)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            On Apr 22, 2022 this sequence version replaced XP_047287318.1.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2987616.1,
                                           SRR14038195.2082763.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1270
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1270
                     /product="kinectin isoform 12"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=146061
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          <326..>584
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          480..>1210
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1270
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402702.1:303..4115"
                     /note="isoform 12 is encoded by transcript variant 25"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqdlkqeika
      841 lkeeignvql ekaqqlsits kvqelqnllk gkeeqmntmk avleekekdl antgkwlqdl
      901 qeeneslkah vqevaqhnlk eassasqfee leivlkeken elkrleamlk eresdlsskt
      961 qllqdvqden klfksqieql kqqnyqqass fppheellkv iserekeisg lwneldslkd
     1021 avehqrkknn sygewlhgfe kkakecmagt sgseevkvle hklkeademh tllqleceky
     1081 ksvlaetegi lqklqrsveq eenkwkvkvd eshktikqmq ssftsseqel erlrsenkdi
     1141 enlrrerehl emelekaeme rstyvtevre lkaqlnetlt klrteqnerq kvagdlhkaq
     1201 qsleliqski vkaagdttvi ensdvspete sseketmsvs lnqtvtqlqq llqavnqqlt
     1261 kekehyqvle
//
LOCUS       NP_001392802            1061 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001392802
VERSION     NP_001392802.1
DBSOURCE    REFSEQ: accession NM_001405873.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1061)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1061)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1061)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1061)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1061)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1061)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1061)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.321033.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1061
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 5"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=116251
     Region          885..>947
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..1061
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405873.1:697..3882"
                     /note="isoform 5 is encoded by transcript variant 14"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankgli
      481 vlgevpppeh ttdlflplss evktdhgtdk liesvsqple nhgapiighi seslstkscg
      541 alrpvngvin tlqpvladhi pgdssdaeeq lhkkqrlnlv ssssdgtcva artrpvlsck
      601 krrlvrpnsi vplskkvhrn stirpgcdvn pscalcgsgs intmppeihy eapllerlsq
      661 ldscvhpvla fpddvptslh fqsmlksqwq nkpfdkikpp kklslkhrap mpgslpdsar
      721 kdrhklvssf lttaklshhq trpdrthrqh lddvgavpmv ervtapkaer llnppppvhd
      781 pnhskmrlrd hssersevlk hhtdmssssy laathhpphs plvrqlstss dspapassss
      841 qvtastsqqp vrrrrgessf dinnivipms vaattrvekl qykeiltpsw revdlqslkg
      901 spdeeneeie dlsdaafaal hakceemera rwlwttsvpp qrrgsrspis pelhsapltp
      961 vardtprhla sedtrcstpe lgldeqsvqp werrtfplah spqaecedql daqeraarct
     1021 rrtsgsktgr eteaaptspp ivplksrhlv aaataqrpth r
//
LOCUS       NP_001393984             553 aa            linear   PRI 21-NOV-2025
DEFINITION  merlin isoform 11 [Homo sapiens].
ACCESSION   NP_001393984
VERSION     NP_001393984.1
DBSOURCE    REFSEQ: accession NM_001407055.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 553)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 553)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 553)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 553)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 553)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 553)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005529.7 and AC004882.3.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3428532.1,
                                           SRR18074967.646021.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..553
                     /product="merlin isoform 11"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=64466
     Region          <38..180
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          174..270
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(216..217,219..225,234,255,258..259,262)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(216,219..226,234,255,258..259,262)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(252,256)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            255..270
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          265..>325
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          304..423
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          476..553
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..553
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_001407055.1:367..2028"
                     /note="isoform 11 is encoded by transcript variant 17"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 magaiasrms fsslkrkqpk tftvrivtmd aemefncevl dhdvskeepv tfhflakfyp
       61 enaeeelvqe itqhlfflqv kkqildekiy cppeasvlla syavqakygd ydpsvhkrgf
      121 laqeellpkr vinlyqmtpe mweeritawy aehrgrarde aemeylkiaq dlemygvnyf
      181 airnkkgtel llgvdalglh iydpenrltp kisfpwneir nisysdkeft ikpldkkidv
      241 fkfnssklrv nklilqlcig nhdlfmrrrk adslevqqmk aqareekark qmerqrlare
      301 kqmreeaert rdelerrllq mkeeatmane almrseetad llaekaqite eeakllaqka
      361 aeaeqemqri katairteee krlmeqkvle aevlalkmae eserrakead qlkqdlqear
      421 eaerrakqkl leiatkptyp pmnpipaplp pdipsfnlig dslsfdfkdt dmkrlsmeie
      481 kekveymeks khlqeqlnel kteiealklk eretaldilh nensdrggss khntikkltl
      541 qsaksrvaff eel
//
LOCUS       NP_001427982            4358 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HUWE1 isoform 2 [Homo sapiens].
ACCESSION   NP_001427982 XP_047297699 XP_054182295
VERSION     NP_001427982.1
DBSOURCE    REFSEQ: accession NM_001441053.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4358)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 4358)
  AUTHORS   Lee,C., Park,S.H. and Yoon,S.K.
  TITLE     The E3 ligase HUWE1 increases the sensitivity of CRC to oxaliplatin
            through TOMM20 degradation
  JOURNAL   Oncogene 43 (9), 636-649 (2024)
   PUBMED   38184713
  REMARK    GeneRIF: The E3 ligase HUWE1 increases the sensitivity of CRC to
            oxaliplatin through TOMM20 degradation.
REFERENCE   3  (residues 1 to 4358)
  AUTHORS   Li,X.X., Xu,J.K., Su,W.J., Wu,H.L., Zhao,K., Zhang,C.M., Chen,X.K.
            and Yang,L.X.
  TITLE     The role of KDM4A-mediated histone methylation on temozolomide
            resistance in glioma cells through the HUWE1/ROCK2 axis
  JOURNAL   Kaohsiung J Med Sci 40 (2), 161-174 (2024)
   PUBMED   37873881
  REMARK    GeneRIF: The role of KDM4A-mediated histone methylation on
            temozolomide resistance in glioma cells through the HUWE1/ROCK2
            axis.
REFERENCE   4  (residues 1 to 4358)
  AUTHORS   Bernassola,F., Karin,M., Ciechanover,A. and Melino,G.
  TITLE     The HECT family of E3 ubiquitin ligases: multiple players in cancer
            development
  JOURNAL   Cancer Cell 14 (1), 10-21 (2008)
   PUBMED   18598940
  REMARK    Review article
REFERENCE   5  (residues 1 to 4358)
  AUTHORS   Zhong,Q., Gao,W., Du,F. and Wang,X.
  TITLE     Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the
            polyubiquitination of Mcl-1 and regulates apoptosis
  JOURNAL   Cell 121 (7), 1085-1095 (2005)
   PUBMED   15989957
  REMARK    GeneRIF: Mule is both required and sufficient for the
            polyubiquitination of Mcl-1; Mule is a unique BH3-containing E3
            ubiquitin ligase apical to Bcl-2 family proteins during DNA
            damage-induced apoptosis
            GeneRIF: Mule (HUWE1) poly-ubiquitinates anti-apoptotic gene Mcl-1.
REFERENCE   6  (residues 1 to 4358)
  AUTHORS   Chen,D., Kon,N., Li,M., Zhang,W., Qin,J. and Gu,W.
  TITLE     ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
  JOURNAL   Cell 121 (7), 1071-1083 (2005)
   PUBMED   15989956
  REMARK    GeneRIF: study modifies the current view of ARF-mediated p53
            activation and reveals that ARF-BP1 is a critical mediator of both
            the p53-independent and p53-dependent tumor suppressor functions of
            ARF
            GeneRIF: Ubiquitin ligase activity of ARF-BP1 (HUWE1) is inhibited
            by Arf.
REFERENCE   7  (residues 1 to 4358)
  AUTHORS   Liu,Z., Oughtred,R. and Wing,S.S.
  TITLE     Characterization of E3Histone, a novel testis ubiquitin protein
            ligase which ubiquitinates histones
  JOURNAL   Mol Cell Biol 25 (7), 2819-2831 (2005)
   PUBMED   15767685
REFERENCE   8  (residues 1 to 4358)
  AUTHORS   Gu,J., Dubner,R., Fornace,A.J. Jr. and Iadarola,M.J.
  TITLE     UREB1, a tyrosine phosphorylated nuclear protein, inhibits p53
            transactivation
  JOURNAL   Oncogene 11 (10), 2175-2178 (1995)
   PUBMED   7478539
REFERENCE   9  (residues 1 to 4358)
  AUTHORS   Turner,G., Gedeon,A. and Mulley,J.
  TITLE     X-linked mental retardation with heterozygous expression and
            macrocephaly: pericentromeric gene localization
  JOURNAL   Am J Med Genet 51 (4), 575-580 (1994)
   PUBMED   7943042
REFERENCE   10 (residues 1 to 4358)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX323845.7 and AC231658.3.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297699.1, XP_054182295.1.
            
            Summary: This gene encodes a protein containing a C-terminal HECT
            (E6AP type E3 ubiquitin protein ligase) domain that functions as an
            E3 ubiquitin ligase. The encoded protein is required for the
            ubiquitination and subsequent degradation of the anti-apoptotic
            protein Mcl1 (myeloid cell leukemia sequence 1 (BCL2-related)).
            This protein also ubiquitinates the p53 tumor suppressor, core
            histones, and DNA polymerase beta. Mutations in this gene are
            associated with Turner type X-linked syndromic cognitive
            disability. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2114570.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..4358
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..4358
                     /product="E3 ubiquitin-protein ligase HUWE1 isoform 2"
                     /EC_number="2.3.2.26"
                     /note="Mcl-1 ubiquitin ligase E3; BJ-HCC-24 tumor antigen;
                     HECT domain protein LASU1; ARF-binding protein 1;
                     URE-binding protein 1; large structure of UREB1; upstream
                     regulatory element-binding protein 1; homologous to E6AP
                     carboxyl terminus homologous protein 9; HECT-type E3
                     ubiquitin transferase HUWE1; HECT, UBA and WWE domain
                     containing 1, E3 ubiquitin protein ligase"
                     /calculated_mol_wt=479954
     Region          92..367
                     /region_name="DUF908"
                     /note="Domain of Unknown Function (DUF908); pfam06012"
                     /db_xref="CDD:428721"
     Region          431..814
                     /region_name="DUF913"
                     /note="Domain of Unknown Function (DUF913); pfam06025"
                     /db_xref="CDD:461803"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          706..759
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          978..1001
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1014..1037
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1084
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1291..1320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1317..1356
                     /region_name="UBA_HUWE1"
                     /note="UBA domain found in eukaryotic E3 ubiquitin-protein
                     ligase HUWE1 and similar proteins; cd14288"
                     /db_xref="CDD:270474"
     Site            1368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1396..1415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1617..1678
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          1689..1735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1722
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1907
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2017..2064
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2034
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2261..2341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2266
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2355..2479
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2534
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2553
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2594
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2618
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2693..2969
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          <2734..3065
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            2750
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2825
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2832
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2860
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2886
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2887
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2888
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2917
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3009..3042
                     /region_name="UBM"
                     /note="Ubiquitin binding region; pfam14377"
                     /db_xref="CDD:464159"
     Region          3035..3058
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3148
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3244..3266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3403..3423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3470..3511
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3536..3567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3736..3757
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3751
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3792
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3800
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3811
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3814
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3878..3915
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3890
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3903
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3908
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3911
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          4003..4356
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(4007,4037,4048,4109,4283,4319..4320,4323..4327,4347,
                     4355)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(4137,4140..4141,4143..4144,4147,4154,4156,
                     4160..4161,4163,4168,4173,4190,4194)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     Site            4255
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P51593; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     CDS             1..4358
                     /gene="HUWE1"
                     /gene_synonym="ARF-BP1; HECTH9; HSPC272; Ib772; LASU1;
                     MRXST; MULE; URE-B1; UREB1"
                     /coded_by="NM_001441053.1:426..13502"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:10075"
                     /db_xref="HGNC:HGNC:30892"
                     /db_xref="MIM:300697"
ORIGIN      
        1 mkvdrtklkk tpteapadcr alidklkvcn deqlllelqq iktwnigkce lyhwvdlldr
       61 fdgiladagq tvenmswmlv cdrpereqlk mlllavlnft allieysfsr hlyssiehlt
      121 tllassdmqv vlavlnllyv fskrsnyitr lgsdkrtpll trlqhlaesw ggkengfgla
      181 eccrdlhmmk yppsattlhf efyadpgaev kiekrttsnt lhyihieqld kisespseim
      241 esltkmysip kdkqmllfth irlahgfsnh rkrlqavqar lhaisilvys nalqesansi
      301 lynglieelv dvlqitdkql meikaaslrt ltsivhlert pklssiidct gtasyhgflp
      361 vlvrnciqam idpsmdpyph qfatalfsfl yhlasydagg ealvscgmme allkvikflg
      421 deqdqitfvt ravrvvdlit nldmaafqsh sglsifiyrl ehevdlcrke cpfvikpkiq
      481 rpnttqegee metdmdgvqc ipqraallks mlnflkkaiq dpafsdgirh vmdgslptsl
      541 khiisnaeyy gpslfllate vvtvfvfqep sllsslqdng ltdvmlhall ikdvpatrev
      601 lgslpnvfsa lclnarglqs fvqcqpferl fkvllspdyl pamrrrrssd plgdtasnlg
      661 savdelmrhq ptlktdatta iiklleeicn lgrdpkyicq kpsiqkadgt atappprsnh
      721 aaeeassede eeeevqamqs fnstqqnete pnqqvvgtee ripiplmdyi lnvmkfvesi
      781 lsnnttddhc qefvnqkgll plvtilglpn lpidfptsaa cqavagvcks iltlshepkv
      841 lqegllqlds ilssleplhr piespggsvl lrelacagnv adatlsaqat pllhaltaah
      901 ayimmfvhtc rvgqseirsi svnqwgsqlg lsvlsklsql ycslvwestv llslctpnsl
      961 psgcefgqad mqklvpkdek agttqggkrs dgeqdgaags mdastqglle gigldgdtla
     1021 pmetdeptas dskgkskitp amaarikqik pllsassrlg ralaelfgll vklcvgspvr
     1081 qrrshhaast ttaptpaars tasaltkllt kglswqpppy tptprfrltf ficsvgftsp
     1141 mlfderkypy hlmlqkflcs gghnalfetf nwalsmggkv pvseglehsd lpdgtgefld
     1201 awlmlvekmv npttvlesph slpaklpggv qnfpqfsalr flvvtqkaaf tciknlwnrk
     1261 plkvyggrma esmlailchi lrgepvirer lskekegsrg eedtgqeegg srrepqvnqq
     1321 qlqqlmdmgf trehameall ntstmeqate yllthpppim ggvvrdlsms eedqmmraia
     1381 mslgqdipmd qraespeeva crkeeeerka rekqeeeeak clekfqdadp leqdelhtft
     1441 dtmlpgcfhl ldelpdtvyr vcdlimtaik rngadyrdmi lkqvvnqvwe aadvlikaal
     1501 plttsdtktv sewisqmatl pqasnlatri llltllfeel klpcawvves sgilnvlikl
     1561 levvqpclqa akeqkevqtp kwitpvllli dfyektaiss krraqmtkyl qsnsnnwrwf
     1621 ddrsgrwcsy sasnnstids awksgetsvr ftagrrrytv qfttmvqvne etgnrrpvml
     1681 tllrvprlnk nsknsngqel ektleeskem dikrkenkgn dtplalestn teketsleet
     1741 kigeiliqgl tedmvtvlir acvsmlgvpv dpdtlhatlr lclrltrdhk yammfaelks
     1801 trmilnltqs sgfngftplv tlllrhiied pctlrhtmek vvrsaatsga gsttsgvvsg
     1861 slgsreinyi lrvlgpaacr npdiftevan ccirialpap rgsgtasdde fenlrikgpn
     1921 avqlvkttpl kpsplpvipd tikeviydml nalaayhape edksdpkpgv mtqevgqllq
     1981 dmgddvyqqy rsltrqssdf dtqsgfsins qvfaadgast etsasgtsqg eastpeesrd
     2041 gkkdkegdra seegkqkgkg skplmptsti lrllaelvrs yvgiatlian ysytvgqsel
     2101 ikedcsvlaf vldhllphtq naedkdtpal arlflaslaa agsgtdaqva lvnevkaalg
     2161 ralamaeste kharlqavmc iistimescp stssfyssat aktqhngmnn iirlflkkgl
     2221 vndlarvphs ldlsspnman tvnaalkple tlsrivnqps slfgsksass knkseqdaqg
     2281 asqdsssnqq dpgepgeaev qeedhdvtqt evadgdimdg eaetdsvvia gqpevlssqe
     2341 mqveneledl idellerdgg sgnstiivsr sgedesqedv lmdeapsnls qastlqanre
     2401 dsmnildped eeehtqeeds sgsnededds qdeeeeeeed eeddqeddeg eegdeddddd
     2461 gsemeldedy pdmnasplvr ferfdreddl iiefdnmfss atdippspgn iptthplmvr
     2521 hadhssltlg sgssttrltq gigrsqrtlr qltantghti hvhypgnrqp npplilqrll
     2581 gpsaaadilq lssslplqsr grarllvgnd dvhiiarsdd ellddffhdq statsqagtl
     2641 ssiptaltrw teeckvldae smhdcvsvvk vsivnhlefl rdeeleerre krrkqlaeee
     2701 tkitdkgked kenrdqsaqc tasksndste qnlsdgtpmp dsypttpsst daatsesket
     2761 lgtlqssqqq ptlptppalg evpqelqspa geggsstqll mpvepeelgp trpsgeaett
     2821 qmelspapti tslsperaed sdaltavssq legspmdtss lasctleeav gdtsaagsse
     2881 qpragsstpg dappavaevq grsdgsgesa qppedssppa ssessstrds avaisgadsr
     2941 gileeplpst sseeedplag islpegvdps flaalpddir revlqnqlgi rpptrtapst
     3001 nssapavvgn pgvtevspef laalppaiqe evlaqqraeq qrrelaqnas sdtpmdpvtf
     3061 iqtlpsdlrr svledmedsv lavmppdiaa eaqalrreqe arqrqlmher lfghsstsal
     3121 sailrspaft srlsgnrgvq ytrlavqrgg tfqmggsssh nrpsgsnvdt llrlrgrlll
     3181 dhealscllv llfvdepkln tsrlhrvlrn lcyhaqtrhw virsllsilq rsseselcie
     3241 tpklttseek gkksskscgs sshenrpldl lhkmeskssn qlswlsvsmd aalgcrtnif
     3301 qiqrsggrkh tekhasggst vhihpqaapv vcrhvldtli qlakvfpshf tqqrtketnc
     3361 esdrergnka cspcssqsss sgictdfwdl lvkldnmnvs rkgknsvksv pvsaggeget
     3421 spysleaspl gqlmnmlshp virrssllte kllrllslis ialpenkvse aqansgsgas
     3481 stttatstts tttttaastt ptpptaptpv tsapalvaat aistivvaas ttvttpttat
     3541 ttvsispttk gskspakvsd ggssstdfkm vssgltenql qlsvevltsh scseegleda
     3601 anvllqlsrg dsgtrdtvlk lllngarhlg ytlckqigtl laelreynle qqrraqcetl
     3661 spdglpeeqp qttklkgkmq srfdmaenvv ivasqkrplg grelqlpsms mltsktstqk
     3721 fflrvlqvii qlrddtrran kkakqtgrlg ssglgsassi qaavrqleae adaiiqmses
     3781 sqseasvrre espmdvdqps psaqdtqsia sdgtpqgeke keerppelpl lseqlsldel
     3841 wdmlgeclke leeshdqhav lvlqpaveaf flvhateres kppvrdtres qlahikdepp
     3901 plspapltpa tpssldpffs repssmhiss slppdtqkfl rfaethrtvl nqilrqstth
     3961 ladgpfavlv dyirvldfdv krkyfrqele rldeglrked mavhvrrdhv fedsyrelhr
     4021 kspeemknrl yivfegeegq daggllrewy miisremfnp myalfrtspg drvtytinps
     4081 shcnpnhlsy fkfvgrivak avydnrllec yftrsfykhi lgksvrytdm esedyhfyqg
     4141 lvyllendvs tlgydltfst evqefgvcev rdlkpngani lvteenkkey vhlvcqmrmt
     4201 gairkqlaaf legfyeiipk rlisifteqe lellisglpt ididdlksnt eyhkyqsnsi
     4261 qiqwfwralr sfdqadrakf lqfvtgtskv plqgfaaleg mngiqkfqih rddrstdrlp
     4321 sahtcfnqld lpayesfekl rhmlllaiqe csegfgla
//
LOCUS       NP_001424926             999 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 3 isoform 7 [Homo sapiens].
ACCESSION   NP_001424926 XP_006713816 XP_054203919
VERSION     NP_001424926.1
DBSOURCE    REFSEQ: accession NM_001437997.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Wang,H., Lan,S., Wang,L., Zhao,J., Jia,X., Xu,J., Sun,G., Liu,L.,
            Gong,S., Wang,N., Shan,B., Zhang,F. and Zhang,Z.
  TITLE     Expression of circ-PHC3 enhances ovarian cancer progression via
            regulation of the miR-497-5p/SOX9 pathway
  JOURNAL   J Ovarian Res 16 (1), 142 (2023)
   PUBMED   37468993
  REMARK    GeneRIF: Expression of circ-PHC3 enhances ovarian cancer
            progression via regulation of the miR-497-5p/SOX9 pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 999)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 999)
  AUTHORS   Crea,F., Di Paolo,A., Liu,H.H., Polillo,M., Clermont,P.L.,
            Guerrini,F., Ciabatti,E., Ricci,F., Barate,C., Fontanelli,G.,
            Barsotti,S., Morganti,R., Danesi,R., Wang,Y., Petrini,M.,
            Galimberti,S. and Helgason,C.D.
  TITLE     Polycomb genes are associated with response to imatinib in chronic
            myeloid leukemia
  JOURNAL   Epigenomics 7 (5), 757-765 (2015)
   PUBMED   26343356
  REMARK    GeneRIF: Data show that polycomb-group proteins BMI1, PHC3, CBX6
            and CBX7 expression was significantly increased during imatinib
            treatment.
REFERENCE   6  (residues 1 to 999)
  AUTHORS   Deshpande,A.M., Akunowicz,J.D., Reveles,X.T., Patel,B.B.,
            Saria,E.A., Gorlick,R.G., Naylor,S.L., Leach,R.J. and Hansen,M.F.
  TITLE     PHC3, a component of the hPRC-H complex, associates with E2F6
            during G0 and is lost in osteosarcoma tumors
  JOURNAL   Oncogene 26 (12), 1714-1722 (2007)
   PUBMED   17001316
  REMARK    GeneRIF: loss of PHC3 may favor tumorigenesis by potentially
            disrupting the ability of cells to remain in G(0)
REFERENCE   7  (residues 1 to 999)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   8  (residues 1 to 999)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 999)
  AUTHORS   Tonkin,E., Hagan,D.M., Li,W. and Strachan,T.
  TITLE     Identification and characterisation of novel mammalian homologues
            of Drosophila polyhomeoticpermits new insights into relationships
            between members of the polyhomeotic family
  JOURNAL   Hum Genet 111 (4-5), 435-442 (2002)
   PUBMED   12384788
REFERENCE   10 (residues 1 to 999)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC023891.28 and AC008040.7.
            
            On or before Apr 14, 2025 this sequence version replaced
            XP_006713816.1, XP_054203919.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.383379.1,
                                           SRR14038193.1705396.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.2"
     Protein         1..999
                     /product="polyhomeotic-like protein 3 isoform 7"
                     /note="early development regulator 3; polyhomeotic-like
                     protein 3; homolog of polyhomeotic 3; early development
                     regulatory protein 3; polyhomeotic like 3"
                     /calculated_mol_wt=107905
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          103..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          225..283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          313..332
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          339..410
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          344..>584
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          477..509
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          617..636
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Site            625
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Site            630
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Site            632
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          707..736
                     /region_name="HD1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Site            777
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Site            778
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          843..863
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          880..905
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          930..998
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(948..949,983..984,987..988,991)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(959..963,965..966,969..970,974,979)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..999
                     /gene="PHC3"
                     /gene_synonym="EDR3; HPH3"
                     /coded_by="NM_001437997.1:70..3069"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:80012"
                     /db_xref="HGNC:HGNC:15682"
                     /db_xref="MIM:620031"
ORIGIN      
        1 mdtepnpgts svstttsstt tttittsssr mqqpqisvys gsdrhavqvi qqalhrppss
       61 aaqylqqmya aqqqhlmlht aalqqqhlss sqlqslaavq aslssgrpst sptgsvtqqs
      121 smsqtsinls tsptpaqlis rsqassstsg sitqqtmllg stsptltasq aqmylraqml
      181 iftpattvaa vqsdipvvss ssssscqsaa tqvqnltlrs qklgvlsssq ngppkstsqt
      241 qsltichnkt tvtsskisqr dpspesnkkg espslesrst avtrtssihq liapasyspi
      301 qphslikhqq iplhsppskv shhqlilqqq qqqiqpitlq nstqdpppsq hciplqnhgl
      361 ppapsnaqsq hcspiqshps pltvspnqsq saqqsvvvsp ppphspsqsp tiiihpqali
      421 qphplvssal qpgpnlqqst anqvqataql nlpshlplpa spvvhigpvq qsalvspgqq
      481 ivspshqqys slqsspipia sppqmstspp aqipplplqs mqslqvqpei lsqgqvlvqn
      541 alvseeelpa aealvqlpfq tlpppqtvav nlqvqppapv dppvgmhlnq chlhkvfslk
      601 vyqvedvcee empeesdecv rmdrtppppt lspaaitvgr gedltsehpl leqvelpava
      661 svsasviksp sdpshvsvpp pplllpaatt rsnstsmhss ipsienkppq aivkpqilth
      721 viegfviqeg lepfpvsrss llieqpvkkr plldnqvins vcvqpelqnn tkhadnssdt
      781 emedmiaeet leemdsellk cefcgkmgya neflrskrfc tmscakrynv scskkfalsr
      841 wnrkpdnqsl ghrgrrpsgp dgaarehilr qlpitypsae edlashedsv psamttrlrr
      901 qserererel rdvrirkmpe nsdllpvaqt epsiwtvddv wafihslpgc qdiadefraq
      961 eidgqallll kedhlmsamn iklgpalkic arinslkes
//
LOCUS       NP_001400233             291 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 2 [Homo sapiens].
ACCESSION   NP_001400233
VERSION     NP_001400233.1
DBSOURCE    REFSEQ: accession NM_001413304.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.167830.1,
                                           SRR1660809.177079.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..291
                     /product="RNA-binding Raly-like protein isoform 2"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=32199
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          171..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     Region          199..>244
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     Region          249..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     CDS             1..291
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413304.1:424..1299"
                     /note="isoform 2 is encoded by transcript variant 31"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly rleskepfls
      121 vggyvfdydy yrddfynrlf dyhgrvpppp raviplkrpr vavtttrrgk gvfsmkggsr
      181 stasgstgsk lksdelqtik keltqiktki dsllgrleki ekqqkaeaea qkkqleeslv
      241 liqeecvsei adhsteepae ggpdadgeem tdgieedfde dgghelflqi k
//
LOCUS       NP_001400667            1004 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform a [Homo sapiens].
ACCESSION   NP_001400667
VERSION     NP_001400667.1
DBSOURCE    REFSEQ: accession NM_001413738.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1004)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1004)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 1004)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 1004)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 1004)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 1004)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 1004)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.988529.1,
                                           SRR14038191.793635.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..1004
                     /product="polyhomeotic-like protein 1 isoform a"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=105403
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          212..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          261..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          432..512
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          <474..670
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          556..589
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          636..672
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P78364.3)"
     Region          828..935
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          848..928
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Site            898
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P78364.3)"
     Site            922
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P78364.3)"
     Region          935..1003
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(953..954,988..989,992..993,996)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(964..968,970..971,974..975,979,984)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..1004
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413738.1:157..3171"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq asinlattsa aqlisrsqsv
      121 sspsattltq svllgnttsp plnqsqaqmy lrpqlgnllq vnrtlgrnvp lasqlilmpn
      181 gavaavqqev psaqspgvha dadqvqnlav rnqqasaqgp qmqgstqkai ppgaspvssl
      241 sqassqalav aqassgatnq slnlsqaggg sgnsipgsmg pggggqahgg lgqlpssgmg
      301 ggscprkgtg vvqplpaaqt vtvsqgsqte aesaaakkae adgsgqqnvg mnltrtatpa
      361 psqtlissat ytqiqphsli qqqqqihlqq kqvviqqqia ihhqqqfqhr qsqllhtath
      421 lqlaqqqqqq qqqqqqqqqp qattltapqp pqvpptqqvp psqsqqqaqt lvvqpmlqss
      481 plslppdaap kppipiqskp pvapikppql gaakmsaaqq ppphipvqvv gtrqpgtaqa
      541 qalglaqlaa avptsrgmpg tvqsgqahla ssppssqapg alqecpptla pgmtlapvqg
      601 tahvvkggat tsspvvaqvp aafymqsvhl pgkpqtlavk rkadseeerd dvstlgsmlp
      661 akaspvaesp kvmdeksslg ekaesvanvn antpsselva ltpapsvppp tlamvsrqmg
      721 dskppqaivk pqilthiieg fviqegaepf pvgcsqllke sekplqtglp tgltenqsgg
      781 plgvdspsae ldkkanllkc eycgkyapae qfrgskrfcs mtcakrynvs cshqfrlkrk
      841 kmkefqeany arvrrrgprr sssdiaraki qgkchrgqed ssrgsdnssy dealsptspg
      901 plsvraghge rdlgnpntap ptpelhginp vflssnpsrw sveevyefia slqgcqeiae
      961 efrsqeidgq allllkeehl msamniklgp alkicakinv lket
//
LOCUS       NP_001397771             865 aa            linear   PRI 21-NOV-2025
DEFINITION  N-alpha-acetyltransferase 15, NatA auxiliary subunit isoform 2
            [Homo sapiens].
ACCESSION   NP_001397771 XP_005263293
VERSION     NP_001397771.1
DBSOURCE    REFSEQ: accession NM_001410842.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 865)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 865)
  AUTHORS   Lyon,G.J., Vedaie,M., Beisheim,T., Park,A., Marchi,E., Gottlieb,L.,
            Hsieh,T.C., Klinkhammer,H., Sandomirsky,K., Cheng,H., Starr,L.J.,
            Preddy,I., Tseng,M., Li,Q., Hu,Y., Wang,K., Carvalho,A.,
            Martinez,F., Caro-Llopis,A., Gavin,M., Amble,K., Krawitz,P.,
            Marmorstein,R. and Herr-Israel,E.
  TITLE     Expanding the phenotypic spectrum of NAA10-related
            neurodevelopmental syndrome and NAA15-related neurodevelopmental
            syndrome
  JOURNAL   Eur J Hum Genet 31 (7), 824-833 (2023)
   PUBMED   37130971
  REMARK    GeneRIF: Expanding the phenotypic spectrum of NAA10-related
            neurodevelopmental syndrome and NAA15-related neurodevelopmental
            syndrome.
REFERENCE   3  (residues 1 to 865)
  AUTHORS   Tian,Y., Xie,H., Yang,S., Shangguan,S., Wang,J., Jin,C., Zhang,Y.,
            Cui,X., Lyu,Y., Chen,X. and Wang,L.
  TITLE     Possible Catch-Up Developmental Trajectories for Children with Mild
            Developmental Delay Caused by NAA15 Pathogenic Variants
  JOURNAL   Genes (Basel) 13 (3), 536 (2022)
   PUBMED   35328089
  REMARK    GeneRIF: Possible Catch-Up Developmental Trajectories for Children
            with Mild Developmental Delay Caused by NAA15 Pathogenic Variants.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 865)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 865)
  AUTHORS   Ward,T., Tai,W., Morton,S., Impens,F., Van Damme,P., Van Haver,D.,
            Timmerman,E., Venturini,G., Zhang,K., Jang,M.Y., Willcox,J.A.L.,
            Haghighi,A., Gelb,B.D., Chung,W.K., Goldmuntz,E., Porter,G.A. Jr.,
            Lifton,R.P., Brueckner,M., Yost,H.J., Bruneau,B.G., Gorham,J.,
            Kim,Y., Pereira,A., Homsy,J., Benson,C.C., DePalma,S.R.,
            Varland,S., Chen,C.S., Arnesen,T., Gevaert,K., Seidman,C. and
            Seidman,J.G.
  TITLE     Mechanisms of Congenital Heart Disease Caused by NAA15
            Haploinsufficiency
  JOURNAL   Circ Res 128 (8), 1156-1169 (2021)
   PUBMED   33557580
  REMARK    GeneRIF: Mechanisms of Congenital Heart Disease Caused by NAA15
            Haploinsufficiency.
REFERENCE   6  (residues 1 to 865)
  AUTHORS   Fluge,O., Bruland,O., Akslen,L.A., Varhaug,J.E. and Lillehaug,J.R.
  TITLE     NATH, a novel gene overexpressed in papillary thyroid carcinomas
  JOURNAL   Oncogene 21 (33), 5056-5068 (2002)
   PUBMED   12140756
  REMARK    GeneRIF: NATH, a novel gene overexpressed in papillary thyroid
            carcinomas.
REFERENCE   7  (residues 1 to 865)
  AUTHORS   Line,A., Stengrevics,A., Slucka,Z., Li,G., Jankevics,E. and
            Rees,R.C.
  TITLE     Serological identification and expression analysis of gastric
            cancer-associated genes
  JOURNAL   Br J Cancer 86 (11), 1824-1830 (2002)
   PUBMED   12087473
REFERENCE   8  (residues 1 to 865)
  AUTHORS   He,Y.G., Xie,Y.F., Chen,Y., Qian,W., Lai,J.H. and Tan,D.Y.
  TITLE     [Cloning and analysis of a novel gene encoding N-terminal
            acetyltransferase subunit]
  JOURNAL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 34 (3),
            353-357 (2002)
   PUBMED   12019451
REFERENCE   9  (residues 1 to 865)
  AUTHORS   Gendron,R.L., Good,W.V., Adams,L.C. and Paradis,H.
  TITLE     Suppressed expression of tubedown-1 in retinal neovascularization
            of proliferative diabetic retinopathy
  JOURNAL   Invest Ophthalmol Vis Sci 42 (12), 3000-3007 (2001)
   PUBMED   11687548
REFERENCE   10 (residues 1 to 865)
  AUTHORS   Choi,S.C., Chang,J.Y. and Han,J.K.
  TITLE     A novel Xenopus acetyltransferase with a dynamic expression in
            early development
  JOURNAL   Biochem Biophys Res Commun 285 (5), 1338-1343 (2001)
   PUBMED   11478804
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC097376.3.
            
            On Aug 16, 2022 this sequence version replaced XP_005263293.1.
            
            Summary: N-alpha-acetylation is among the most common
            post-translational protein modifications in eukaryotic cells. This
            process involves the transfer of an acetyl group from
            acetyl-coenzyme A to the alpha-amino group on a nascent polypeptide
            and is essential for normal cell function. This gene encodes the
            auxillary subunit of the N-terminal acetyltransferase A (NatA)
            complex. [provided by RefSeq, Jan 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.25817.1,
                                           SRR14372080.3326707.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..865
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.1"
     Protein         1..865
                     /product="N-alpha-acetyltransferase 15, NatA auxiliary
                     subunit isoform 2"
                     /note="transcriptional coactivator tubedown-100; NMDA
                     receptor regulated 1; NMDA receptor-regulated protein 1;
                     gastric cancer antigen Ga19; protein tubedown-1;
                     N-terminal acetyltransferase"
                     /calculated_mol_wt=101071
     Region          12..38
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          44..283
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          46..79
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Region          47..74
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          80..113
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Region          82..108
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(84..85,88..89,91,115,118..119,122..123,125..126,149,
                     152..153,156..157,160)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          113..143
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          148..184
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Region          148..173
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          187..698
                     /region_name="NatA_aux_su"
                     /note="N-terminal acetyltransferase A, auxiliary subunit;
                     pfam12569"
                     /db_xref="CDD:463630"
     Region          224..257
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            262
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Region          374..407
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            order(378..379,382..383,385,409,412..413,416..417,
                     419..420,443,446..447,450..451,454)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          378..402
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          407..437
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          409..441
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Region          442..467
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          485..518
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Region          579..642
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Region          612..629
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            734
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            755
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            854
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     Site            855
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BXJ9.1)"
     CDS             1..865
                     /gene="NAA15"
                     /gene_synonym="Ga19; MRD50; NARG1; NAT1P; NATH; TBDN;
                     TBDN100"
                     /coded_by="NM_001410842.1:274..2871"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS93635.1"
                     /db_xref="GeneID:80155"
                     /db_xref="HGNC:HGNC:30782"
                     /db_xref="MIM:608000"
ORIGIN      
        1 mpavslppke nalfkrilrc yehkqyrngl kfckqilsnp kfaehgetla mkgltlnclg
       61 kkeeayelvr rglrndlksh vcwhvygllq rsdkkydeai kcyrnalkwd kdnlqilrdl
      121 sllqiqmrdl egyretryql lqlrpaqras wigyaiayhl ledyemaaki leefrktqqt
      181 spdkvdyeys elllyqnqvl reaglyreal ehlctyekqi cdklaveetk gelllqlcrl
      241 edaadvyrgl qernpenway ykglekalkp anmlerlkiy eeawtkyprg lvprrlplnf
      301 lsgekfkecl dkflrmnfsk gcppvfntlr slykdkekva iieelvvgye tslkscrlfn
      361 pnddgkeepp ttllwvqyyl aqhydkigqp sialeyinta iestptliel flvkakiykh
      421 agnikeaarw mdeaqaldta drfinskcak ymlkanlike aeemcskftr egtsavenln
      481 emqcmwfqte caqaykamnk fgealkkche ierhfieitd dqfdfhtycm rkitlrsyvd
      541 llkledvlrq hpfyfkaari aieiylklhd npltdenkeh eadtanmsdk elkklrnkqr
      601 raqkkaqiee ekknaekekq qrnqkkkkdd ddeeiggpke elipeklakv etpleeaikf
      661 ltplknlvkn kiethlfafe iyfrkekfll mlqsvkrafa idsshpwlhe cmirlfntvc
      721 eskdlsdtvr tvlkqemnrl fgatnpknfn etflkrnsds lphrlsaakm vyyldpssqk
      781 raielattld esltnrnlqt cmevlealyd gslgdckeaa eiyranchkl fpyalafmpp
      841 gyeedmkitv ngdssaeaee lanei
//
LOCUS       NP_001426087             605 aa            linear   PRI 21-NOV-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein Q isoform 9 [Homo sapiens].
ACCESSION   NP_001426087 XP_016865665 XP_054210011
VERSION     NP_001426087.1
DBSOURCE    REFSEQ: accession NM_001439158.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 605)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 605)
  AUTHORS   Ishtayeh,H., Galves,M., Barnatan,T.T., Berdichevsky,Y.,
            Amer-Sarsour,F., Pasmanik-Chor,M., Braverman,I., Blumen,S.C. and
            Ashkenazi,A.
  TITLE     Oculopharyngeal muscular dystrophy mutations link the RNA-binding
            protein HNRNPQ to autophagosome biogenesis
  JOURNAL   Aging Cell 22 (10), e13949 (2023)
   PUBMED   37559347
  REMARK    GeneRIF: Oculopharyngeal muscular dystrophy mutations link the
            RNA-binding protein HNRNPQ to autophagosome biogenesis.
REFERENCE   3  (residues 1 to 605)
  AUTHORS   Semino,F., Schroter,J., Willemsen,M.H., Bast,T., Biskup,S.,
            Beck-Woedl,S., Brennenstuhl,H., Schaaf,C.P., Kolker,S.,
            Hoffmann,G.F., Haack,T.B. and Syrbe,S.
  TITLE     Further evidence for de novo variants in SYNCRIP as the cause of a
            neurodevelopmental disorder
  JOURNAL   Hum Mutat 42 (9), 1094-1100 (2021)
   PUBMED   34157790
  REMARK    GeneRIF: Further evidence for de novo variants in SYNCRIP as the
            cause of a neurodevelopmental disorder.
REFERENCE   4  (residues 1 to 605)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 605)
  AUTHORS   Mourelatos,Z., Abel,L., Yong,J., Kataoka,N. and Dreyfuss,G.
  TITLE     SMN interacts with a novel family of hnRNP and spliceosomal
            proteins
  JOURNAL   EMBO J 20 (19), 5443-5452 (2001)
   PUBMED   11574476
REFERENCE   6  (residues 1 to 605)
  AUTHORS   Lau,P.P., Chang,B.H. and Chan,L.
  TITLE     Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a
            component of apobec-1 editosome
  JOURNAL   Biochem Biophys Res Commun 282 (4), 977-983 (2001)
   PUBMED   11352648
REFERENCE   7  (residues 1 to 605)
  AUTHORS   Blanc,V., Navaratnam,N., Henderson,J.O., Anant,S., Kennedy,S.,
            Jarmuz,A., Scott,J. and Davidson,N.O.
  TITLE     Identification of GRY-RBP as an apolipoprotein B RNA-binding
            protein that interacts with both apobec-1 and apobec-1
            complementation factor to modulate C to U editing
  JOURNAL   J Biol Chem 276 (13), 10272-10283 (2001)
   PUBMED   11134005
REFERENCE   8  (residues 1 to 605)
  AUTHORS   Grosset,C., Chen,C.Y., Xu,N., Sonenberg,N., Jacquemin-Sablon,H. and
            Shyu,A.B.
  TITLE     A mechanism for translationally coupled mRNA turnover: interaction
            between the poly(A) tail and a c-fos RNA coding determinant via a
            protein complex
  JOURNAL   Cell 103 (1), 29-40 (2000)
   PUBMED   11051545
REFERENCE   9  (residues 1 to 605)
  AUTHORS   Mizutani,A., Fukuda,M., Ibata,K., Shiraishi,Y. and Mikoshiba,K.
  TITLE     SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear
            ribonucleoprotein R, interacts with ubiquitous synaptotagmin
            isoforms
  JOURNAL   J Biol Chem 275 (13), 9823-9831 (2000)
   PUBMED   10734137
REFERENCE   10 (residues 1 to 605)
  AUTHORS   Harris,C.E., Boden,R.A. and Astell,C.R.
  TITLE     A novel heterogeneous nuclear ribonucleoprotein-like protein
            interacts with NS1 of the minute virus of mice
  JOURNAL   J Virol 73 (1), 72-80 (1999)
   PUBMED   9847309
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136082.22.
            
            On or before Apr 28, 2025 this sequence version replaced
            XP_016865665.1, XP_054210011.1.
            
            Summary: This gene encodes a member of the cellular heterogeneous
            nuclear ribonucleoprotein (hnRNP) family. hnRNPs are RNA binding
            proteins that complex with heterogeneous nuclear RNA (hnRNA) and
            regulate alternative splicing, polyadenylation, and other aspects
            of mRNA metabolism and transport. The encoded protein plays a role
            in multiple aspects of mRNA maturation and is associated with
            several multiprotein complexes including the apoB RNA
            editing-complex and survival of motor neurons (SMN) complex.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene, and a pseudogene of this
            gene is located on the short arm of chromosome 20. [provided by
            RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.640022.1,
                                           SRR14372080.3290573.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..605
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.3"
     Protein         1..605
                     /product="heterogeneous nuclear ribonucleoprotein Q
                     isoform 9"
                     /note="NS1-associated protein 1; heterogeneous nuclear
                     ribonucleoprotein Q; glycine- and tyrosine-rich
                     RNA-binding protein"
                     /calculated_mol_wt=67245
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          23..107
                     /region_name="NURR_hnRNPQ"
                     /note="NURR (N-terminal unit for RNA recognition) domain
                     found in heterogeneous nuclear ribonucleoprotein Q
                     (hnRNPQ) and similar proteins; cd21066"
                     /db_xref="CDD:410954"
     Region          103..592
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            221
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            363
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:12601080; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          400..561
                     /region_name="Interaction with APOBEC1"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            444
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          448..559
                     /region_name="8 X 3 AA repeats of R-G-G"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Region          460..488
                     /region_name="3 X 4 AA repeats of Y-Y-G-Y"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            496
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            510
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          518..549
                     /region_name="Interaction with SMN.
                     /evidence=ECO:0000269|PubMed:11574476"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            518
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            526
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            536
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            539
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          564..578
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            587
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     CDS             1..605
                     /gene="SYNCRIP"
                     /gene_synonym="GRY-RBP; GRYRBP; hnRNP-Q; HNRNPQ; HNRPQ1;
                     NSAP1; PP68"
                     /coded_by="NM_001439158.1:103..1920"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:10492"
                     /db_xref="HGNC:HGNC:16918"
                     /db_xref="MIM:616686"
ORIGIN      
        1 matehvngng teepmdttsa vihsenfqtl ldaglpqkva ekldeiyvag lvahsdlder
       61 aiealkefne dgalavlqqf kdsdlshvqn ksaflcgvmk tyrqrekqgt kvadsskgpd
      121 eakikaller tgytldvttg qrkyggpppd svysgqqpsv gteifvgkip rdlfedelvp
      181 lfekagpiwd lrlmmdpltg lnrgyafvtf ctkeaaqeav klynnheirs gkhigvcisv
      241 annrlfvgsi pksktkeqil eefskvtegl tdvilyhqpd dkkknrgfcf leyedhktaa
      301 qarrrlmsgk vkvwgnvgtv ewadpiedpd pevmakvkvl fvrnlantvt eeilekafsq
      361 fgklervkkl kdyafihfde rdgavkamee mngkdlegen ieivfakppd qkrkerkaqr
      421 qaaknqmydd yyyygpphmp pptrgrgrgg rggygyppdy ygyedyydyy gydyhnyrgg
      481 yedpyygyed fqvgargrgg rgargaapsr grgaapprgr agysqrggpg sargvrgarg
      541 gaqqqrgrgv rgarggrggn vggkrkadgy nqpdskrrqt nnqnwgsqpi aqqplqagkr
      601 grgrs
//
LOCUS       NP_001422921            1062 aa            linear   PRI 21-NOV-2025
DEFINITION  histone deacetylase 4 isoform 3 [Homo sapiens].
ACCESSION   NP_001422921 XP_024309025 XP_054200719
VERSION     NP_001422921.1
DBSOURCE    REFSEQ: accession NM_001435992.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Liu,W. and Luo,G.
  TITLE     NEDD9 is transcriptionally regulated by HDAC4 and promotes breast
            cancer metastasis and macrophage M2 polarization via the
            FAK/NF-kappaB signaling pathway
  JOURNAL   Neoplasia 57, 101059 (2024)
   PUBMED   39326322
  REMARK    GeneRIF: NEDD9 is transcriptionally regulated by HDAC4 and promotes
            breast cancer metastasis and macrophage M2 polarization via the
            FAK/NF-kappaB signaling pathway.
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1062)
  AUTHORS   Di Giorgio,E., Dalla,E., Tolotto,V., D'Este,F., Paluvai,H.,
            Ranzino,L. and Brancolini,C.
  TITLE     HDAC4 influences the DNA damage response and counteracts senescence
            by assembling with HDAC1/HDAC2 to control H2BK120 acetylation and
            homology-directed repair
  JOURNAL   Nucleic Acids Res 52 (14), 8218-8240 (2024)
   PUBMED   38874468
  REMARK    GeneRIF: HDAC4 influences the DNA damage response and counteracts
            senescence by assembling with HDAC1/HDAC2 to control H2BK120
            acetylation and homology-directed repair.
REFERENCE   5  (residues 1 to 1062)
  AUTHORS   Chen,Q. and Lao,J.
  TITLE     Interference with Histone Deacetylase 4 Regulates c-Jun N-terminal
            Kinase/Activating Protein-1 Signaling to Ameliorate Sepsis-induced
            Alveolar Epithelial Cell Injury
  JOURNAL   J Physiol Investig 67 (4), 174-186 (2024)
   PUBMED   39133038
  REMARK    GeneRIF: Interference with Histone Deacetylase 4 Regulates c-Jun
            N-terminal Kinase/Activating Protein-1 Signaling to Ameliorate
            Sepsis-induced Alveolar Epithelial Cell Injury.
REFERENCE   6  (residues 1 to 1062)
  AUTHORS   Pazin,M.J. and Kadonaga,J.T.
  TITLE     What's up and down with histone deacetylation and transcription?
  JOURNAL   Cell 89 (3), 325-328 (1997)
   PUBMED   9150131
  REMARK    Review article
REFERENCE   7  (residues 1 to 1062)
  AUTHORS   Wolffe,A.P.
  TITLE     Transcriptional control. Sinful repression
  JOURNAL   Nature 387 (6628), 16-17 (1997)
   PUBMED   9139815
REFERENCE   8  (residues 1 to 1062)
  AUTHORS   Ohara,O., Nagase,T., Ishikawa,K., Nakajima,D., Ohira,M., Seki,N.
            and Nomura,N.
  TITLE     Construction and characterization of human brain cDNA libraries
            suitable for analysis of cDNA clones encoding relatively large
            proteins
  JOURNAL   DNA Res 4 (1), 53-59 (1997)
   PUBMED   9179496
REFERENCE   9  (residues 1 to 1062)
  AUTHORS   Wilson,L.C., Leverton,K., Oude Luttikhuis,M.E., Oley,C.A.,
            Flint,J., Wolstenholme,J., Duckett,D.P., Barrow,M.A., Leonard,J.V.,
            Read,A.P. et al.
  TITLE     Brachydactyly and mental retardation: an Albright hereditary
            osteodystrophy-like syndrome localized to 2q37
  JOURNAL   Am J Hum Genet 56 (2), 400-407 (1995)
   PUBMED   7847374
REFERENCE   10 (residues 1 to 1062)
  AUTHORS   Doherty,E.S. and Lacbawan,F.L.
  TITLE     2q37 Microdeletion Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301337
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC062017.6 and AC017028.11.
            
            On or before Jan 22, 2025 this sequence version replaced
            XP_024309025.1, XP_054200719.1.
            
            Summary: Histones play a critical role in transcriptional
            regulation, cell cycle progression, and developmental events.
            Histone acetylation/deacetylation alters chromosome structure and
            affects transcription factor access to DNA. The protein encoded by
            this gene belongs to class II of the histone deacetylase/acuc/apha
            family. It possesses histone deacetylase activity and represses
            transcription when tethered to a promoter. This protein does not
            bind DNA directly, but through transcription factors MEF2C and
            MEF2D. It seems to interact in a multiprotein complex with RbAp48
            and HDAC3. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853565.17890.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..1062
                     /product="histone deacetylase 4 isoform 3"
                     /EC_number="3.5.1.98"
                     /note="histone deacetylase A"
                     /calculated_mol_wt=116650
     Region          <64..125
                     /region_name="ClassIIa_HDAC4_Gln-rich-N"
                     /note="Glutamine-rich N-terminal helical domain of HDAC4,
                     a Class IIa histone deacetylase; cd10162"
                     /db_xref="CDD:197398"
     Site            order(66,70,81..82,85,92,96..97)
                     /site_type="other"
                     /note="dimer interface A, B [polypeptide binding]"
                     /db_xref="CDD:197398"
     Region          627..1035
                     /region_name="HDAC4"
                     /note="Histone deacetylase 4; cd10006"
                     /db_xref="CDD:212530"
     Site            order(780..781,789..790,818,820,912,952)
                     /site_type="active"
                     /db_xref="CDD:212530"
     CDS             1..1062
                     /gene="HDAC4"
                     /gene_synonym="AHO3; BDMR; HA6116; HD4; HDAC-4; HDAC-A;
                     HDACA; NEDCHF; NEDCHID"
                     /coded_by="NM_001435992.1:234..3422"
                     /note="isoform 3 is encoded by transcript variant 7"
                     /db_xref="GeneID:9759"
                     /db_xref="HGNC:HGNC:14063"
                     /db_xref="MIM:605314"
ORIGIN      
        1 mpstvdvata lplqvapsav pmdlrldhqf slpvaepalr eqqlqqella lkqkqqiqrq
       61 iliaefqrqh eqlsrqheaq lhehikqqqe mlamkhqqel lehqrklerh rqeqelekqh
      121 reqklqqlkn kekgkesava stevkmklqe fvlnkkkala hrnlnhciss dprywygktq
      181 hssldqsspp qsgvstsynh pvlgmydakd dfplrktase pnlklrsrlk qkvaerrssp
      241 llrrkdgpvv talkkrpldv tdsacssapg sgpsspnnss gsvsaengia pavpsipaet
      301 slahrlvare gsaaplplyt spslpnitlg lpatgpsagt agqqdaerlt lpalqqrlsl
      361 fpgthltpyl stsplerdgg aahspllqhm vlleqppaqa plvtdwylsg lgalplhaqs
      421 lvgadrvsps ihklrqhrpl grtqsaplpq naqalqhlvi qqqhqqflek hkqqfqqqql
      481 qmnkiipkps eparqpeshp eeteeelreh qalldepyld rlpgqkeaha qagvqvkqep
      541 iesdeeeaep prevepgqrq pseqellfrq qallleqqri hqlrnyqasm eaagipvsfg
      601 ghrplsraqs spasatfpvs vqepptkprf ttglvydtlm lkhqctcgss sshpehagri
      661 qsiwsrlqet glrgkcecir grkatleelq tvhseahtll ygtnplnrqk ldskkllgsl
      721 asvfvrlpcg gvgvdsdtiw nevhsagaar lavgcvvelv fkvatgelkn gfavvrppgh
      781 haeestpmgf cyfnsvavaa kllqqrlsvs kilivdwdvh hgngtqqafy sdpsvlymsl
      841 hryddgnffp gsgapdevgt gpgvgfnvnm aftggldppm gdaeylaafr tvvmpiasef
      901 apdvvlvssg fdaveghptp lggynlsarc fgyltkqlmg laggrivlal egghdltaic
      961 daseacvsal lgneldplpe kvlqqrpnan avrsmekvme ihskywrclq rttstagrsl
     1021 ieaqtcenee aetvtamasl svgvkpaekr pdeepmeeep pl
//
LOCUS       NP_079066               1221 aa            linear   PRI 21-NOV-2025
DEFINITION  centrosome and spindle pole-associated protein 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_079066
VERSION     NP_079066.5
DBSOURCE    REFSEQ: accession NM_024790.7
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1221)
  AUTHORS   van den Berg,C.M., Volkov,V.A., Schnorrenberg,S., Huang,Z.,
            Stecker,K.E., Grigoriev,I., Gilani,S., Frikstad,K.M., Patzke,S.,
            Zimmermann,T., Dogterom,M. and Akhmanova,A.
  TITLE     CSPP1 stabilizes growing microtubule ends and damaged lattices from
            the luminal side
  JOURNAL   J Cell Biol 222 (4) (2023)
   PUBMED   36752787
  REMARK    GeneRIF: CSPP1 stabilizes growing microtubule ends and damaged
            lattices from the luminal side.
REFERENCE   2  (residues 1 to 1221)
  AUTHORS   Odabasi,E., Conkar,D., Deretic,J., Batman,U., Frikstad,K.M.,
            Patzke,S. and Firat-Karalar,E.N.
  TITLE     CCDC66 regulates primary cilium length and signaling via
            interactions with transition zone and axonemal proteins
  JOURNAL   J Cell Sci 136 (3) (2023)
   PUBMED   36606424
REFERENCE   3  (residues 1 to 1221)
  AUTHORS   Zhang,L., Yang,S.T., Wang,C., Zhang,L.C., Zhang,X., Li,F.C.,
            Wang,S.Y. and Ma,K.
  TITLE     Circle RNA circCSPP1 promotes human osteosarcoma cell proliferation
            and increases glucose metabolism by suppressing miR-200c maturation
  JOURNAL   Hum Exp Toxicol 41, 9603271221097364 (2022)
   PUBMED   35713481
  REMARK    GeneRIF: Circle RNA circCSPP1 promotes human osteosarcoma cell
            proliferation and increases glucose metabolism by suppressing
            miR-200c maturation.
REFERENCE   4  (residues 1 to 1221)
  AUTHORS   Latour,B.L., Van De Weghe,J.C., Rusterholz,T.D., Letteboer,S.J.,
            Gomez,A., Shaheen,R., Gesemann,M., Karamzade,A., Asadollahi,M.,
            Barroso-Gil,M., Chitre,M., Grout,M.E., van Reeuwijk,J., van
            Beersum,S.E., Miller,C.V., Dempsey,J.C., Morsy,H., Bamshad,M.J.,
            Nickerson,D.A., Neuhauss,S.C., Boldt,K., Ueffing,M.,
            Keramatipour,M., Sayer,J.A., Alkuraya,F.S., Bachmann-Gagescu,R.,
            Roepman,R. and Doherty,D.
  CONSRTM   University of Washington Center for Mendelian Genomics; Genomics
            England Research Consortium
  TITLE     Dysfunction of the ciliary ARMC9/TOGARAM1 protein module causes
            Joubert syndrome
  JOURNAL   J Clin Invest 130 (8), 4423-4439 (2020)
   PUBMED   32453716
REFERENCE   5  (residues 1 to 1221)
  AUTHORS   Xue,Y.F., Li,M., Li,W., Lin,Q., Yu,B.X., Zhu,Q.B. and Chen,H.J.
  TITLE     Roles of circ-CSPP1 on the proliferation and metastasis of glioma
            cancer
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (10), 5519-5525 (2020)
   PUBMED   32495924
  REMARK    GeneRIF: Roles of circ-CSPP1 on the proliferation and metastasis of
            glioma cancer.
REFERENCE   6  (residues 1 to 1221)
  AUTHORS   Patzke,S., Redick,S., Warsame,A., Murga-Zamalloa,C.A., Khanna,H.,
            Doxsey,S. and Stokke,T.
  TITLE     CSPP is a ciliary protein interacting with Nephrocystin 8 and
            required for cilia formation
  JOURNAL   Mol Biol Cell 21 (15), 2555-2567 (2010)
   PUBMED   20519441
  REMARK    GeneRIF: CSPP isoforms require their common C-terminal domain to
            interact with Nephrocystin 8 (NPHP8/RPGRIP1L) and to form a ternary
            complex with NPHP8 and NPHP4.
REFERENCE   7  (residues 1 to 1221)
  AUTHORS   Asiedu,M., Wu,D., Matsumura,F. and Wei,Q.
  TITLE     Centrosome/spindle pole-associated protein regulates cytokinesis
            via promoting the recruitment of MyoGEF to the central spindle
  JOURNAL   Mol Biol Cell 20 (5), 1428-1440 (2009)
   PUBMED   19129481
  REMARK    GeneRIF: CSPP interacts with and recruits MyoGEF to the central
            spindle, where MyoGEF contributes to the spatiotemporal regulation
            of cytokinesis.
REFERENCE   8  (residues 1 to 1221)
  AUTHORS   Patzke,S., Stokke,T. and Aasheim,H.C.
  TITLE     CSPP and CSPP-L associate with centrosomes and microtubules and
            differently affect microtubule organization
  JOURNAL   J Cell Physiol 209 (1), 199-210 (2006)
   PUBMED   16826565
  REMARK    GeneRIF: Taken together, CSPP and CSPP-L interact with centrosomes
            and microtubules and can differently affect microtubule
            organization.
REFERENCE   9  (residues 1 to 1221)
  AUTHORS   Patzke,S., Hauge,H., Sioud,M., Finne,E.F., Sivertsen,E.A.,
            Delabie,J., Stokke,T. and Aasheim,H.C.
  TITLE     Identification of a novel centrosome/microtubule-associated
            coiled-coil protein involved in cell-cycle progression and spindle
            organization
  JOURNAL   Oncogene 24 (7), 1159-1173 (2005)
   PUBMED   15580290
  REMARK    GeneRIF: Novel centrosome/microtubule-associated coiled-coil
            protein (CSPP)is associated with centrosomes and microtubules and
            may play a role in the regulation of G(1)/S-phase progression and
            spindle assembly [CSPP].
REFERENCE   10 (residues 1 to 1221)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC109335.5 and AC087359.13.
            
            On Oct 14, 2006 this sequence version replaced NP_079066.4.
            
            Summary: This gene encodes a centrosome and spindle pole associated
            protein. The encoded protein plays a role in cell-cycle progression
            and spindle organization, regulates cytokinesis, interacts with
            Nephrocystin 8 and is required for cilia formation. Mutations in
            this gene result in primary cilia abnormalities and classical
            Joubert syndrome. Alternatively spliced transcript variants
            encoding distinct isoforms have been found for this gene. [provided
            by RefSeq, Apr 2014].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1, also known as CSPP-L).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AM156947.1, BX649147.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1221
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1-q13.2"
     Protein         1..1221
                     /product="centrosome and spindle pole-associated protein 1
                     isoform 1"
                     /calculated_mol_wt=141692
     CDS             1..1221
                     /gene="CSPP1"
                     /gene_synonym="CSPP; CSPP-L; JBTS21"
                     /coded_by="NM_024790.7:8..3673"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43744.1"
                     /db_xref="GeneID:79848"
                     /db_xref="HGNC:HGNC:26193"
                     /db_xref="MIM:611654"
ORIGIN      
        1 mlfplqvaav tssvrddple hcvsprtrar speickmadn ldefieeqka rlaedkaele
       61 sdppymemkg klsaklsens kilismaken ippnsqqtrg slgidyglsl plgedyerkk
      121 hklkeelrqd yrryltqerl klernkeynq flrgkeesse kfrqvekste pksqrnkkpi
      181 gqvkpdltsq iqtscenseg prkdvltpse ayeellnqrr leedryrqld deielrnrri
      241 ikkaneevgi snlkhqrfas kagipdrrfh rfnedrvfdr ryhrpdqdpe vseemderfr
      301 yesdfdrrls rvytndrmhr nkrgnmppme hdgdvieqsn irissaenks apdnetsksa
      361 nqdtcspfag mlfggedrel iqrrkekyrl elleqmaeqq rnkrrekdle lrvaasgaqd
      421 pekspdrlkq fsvaprhfee mipperpria fqtplpplsa psvppipsvh pvpsqnedlr
      481 sglssalgem vspriaplpp ppllpplatn yrtpyddayy fygsrntfdp slayygsgmm
      541 gvqpaayvsa pvthqlaqpv vntvgqnelk itsdqvinsg lifedkpkps kqslqsyqea
      601 lqqqireree rrkkereeke eyeakleaem rtynpwgkgg ggaplrdakg nlitdlnrmh
      661 rqnidayhnp dartyedkra vvsldpnlat snaenledaa nkssghmqtq sspfargnvf
      721 gepptelqik qqelyknflr fqieekkqre eaererlria eekeerrlae qrariqqeye
      781 eeqekkreke eeqrlkneeh irlaeerqke aerkkkeeee kynlqlqhyc erdnligeet
      841 khmrqpspiv palqnkiask lqrppsvdsi irsfihessm sraqsppvpa rknqlraeee
      901 kknvimelse mrkqlrseer rlqerllhmd sddeipirkk ernpmdifdm arhrlqapvr
      961 rqspkgldaa tfqnvhdfne lkdrdsetrv dlkfmyldpp rdhhtleiqq qallreqqkr
     1021 lnrikmqega kvdldaipsa kvreqrmprd dtsdflknsl lesdsafiga ygetypaied
     1081 dvlpppsqlp sarerrrnkw kgldidssrp nvapdglslk sissvnvdel rvrneermrr
     1141 lnefhnkpin tddesslvdp ddimkhigdd gsnsvatepw lrpgtsetlk rfmaeqlnqe
     1201 qqqipgkpgt ftwqglstah g
//
LOCUS       NP_001397984             726 aa            linear   PRI 21-NOV-2025
DEFINITION  MAP/microtubule affinity-regulating kinase 3 isoform f [Homo
            sapiens].
ACCESSION   NP_001397984 XP_047287336
VERSION     NP_001397984.1
DBSOURCE    REFSEQ: accession NM_001411055.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 726)
  AUTHORS   Aparicio-Bautista,D.I., Jimenez-Ortega,R.F., Becerra-Cervera,A.,
            Aquino-Galvez,A., de Leon-Suarez,V.P., Casas-Avila,L., Salmeron,J.,
            Hidalgo-Bravo,A., Rivera-Paredez,B. and Velazquez-Cruz,R.
  TITLE     Interaction between MARK3 (rs11623869), PLCB4 (rs6086746) and
            GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women
  JOURNAL   Front Endocrinol (Lausanne) 15, 1392063 (2024)
   PUBMED   38715801
  REMARK    GeneRIF: Interaction between MARK3 (rs11623869), PLCB4 (rs6086746)
            and GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 726)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 726)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 726)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 726)
  AUTHORS   Li,M.G., Katsura,K., Nomiyama,H., Komaki,K., Ninomiya-Tsuji,J.,
            Matsumoto,K., Kobayashi,T. and Tamura,S.
  TITLE     Regulation of the interleukin-1-induced signaling pathways by a
            novel member of the protein phosphatase 2C family (PP2Cepsilon)
  JOURNAL   J Biol Chem 278 (14), 12013-12021 (2003)
   PUBMED   12556533
REFERENCE   7  (residues 1 to 726)
  AUTHORS   Sun,T.Q., Lu,B., Feng,J.J., Reinhard,C., Jan,Y.N., Fantl,W.J. and
            Williams,L.T.
  TITLE     PAR-1 is a Dishevelled-associated kinase and a positive regulator
            of Wnt signalling
  JOURNAL   Nat Cell Biol 3 (7), 628-636 (2001)
   PUBMED   11433294
REFERENCE   8  (residues 1 to 726)
  AUTHORS   Peng,C.Y., Graves,P.R., Ogg,S., Thoma,R.S., Byrnes,M.J. 3rd, Wu,Z.,
            Stephenson,M.T. and Piwnica-Worms,H.
  TITLE     C-TAK1 protein kinase phosphorylates human Cdc25C on serine 216 and
            promotes 14-3-3 protein binding
  JOURNAL   Cell Growth Differ 9 (3), 197-208 (1998)
   PUBMED   9543386
REFERENCE   9  (residues 1 to 726)
  AUTHORS   Ono,T., Kawabe,T., Sonta,S. and Okamoto,T.
  TITLE     Assignment of MARK3 alias KP78 to human chromosome band 14q32.3 by
            in situ hybridization
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 101-102 (1997)
   PUBMED   9533022
REFERENCE   10 (residues 1 to 726)
  AUTHORS   Meller,N., Liu,Y.C., Collins,T.L., Bonnefoy-Berard,N., Baier,G.,
            Isakov,N. and Altman,A.
  TITLE     Direct interaction between protein kinase C theta (PKC theta) and
            14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition
            of PKC theta translocation and function
  JOURNAL   Mol Cell Biol 16 (10), 5782-5791 (1996)
   PUBMED   8816492
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133367.4 and KF456011.1.
            
            On Aug 20, 2022 this sequence version replaced XP_047287336.1.
            
            Summary: The protein encoded by this gene is activated by
            phosphorylation and in turn is involved in the phosphorylation of
            tau proteins MAP2 and MAP4. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.21916.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.32-q32.33"
     Protein         1..726
                     /product="MAP/microtubule affinity-regulating kinase 3
                     isoform f"
                     /EC_number="2.7.11.1"
                     /note="EMK-2; C-TAK1; ELKL motif kinase 2; protein kinase
                     STK10; ser/Thr protein kinase PAR-1; cdc25C-associated
                     protein kinase 1; MAP/microtubule affinity-regulating
                     kinase 3; serine/threonine-protein kinase p78"
                     /calculated_mol_wt=81125
     Region          55..289
                     /region_name="STKc_MARK"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     MAP/microtubule affinity-regulating kinases; cd14072"
                     /db_xref="CDD:270974"
     Site            order(62..66,70,98,114..117,121,123..124,126,159..160,162,
                     164..165,167,177..178,181,194..199,201,231..234,236)
                     /site_type="active"
                     /db_xref="CDD:270974"
     Site            order(62..65,70,98,114..117,121,164..165,167,177..178)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270974"
     Site            order(66,121,123,159..160,162,164,181,195..199,201)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270974"
     Site            177..199
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270974"
     Region          307..349
                     /region_name="UBA_MARK3_4"
                     /note="UBA domain found in MAP/microtubule
                     affinity-regulating kinase MARK3, MARK4, and similar
                     proteins; cd14407"
                     /db_xref="CDD:270590"
     Region          627..724
                     /region_name="MARK1-3_C"
                     /note="C-terminal, kinase associated domain 1 (KA1), a
                     phospholipid binding domain, of microtubule
                     affinity-regulating kinases 1-3; cd12196"
                     /db_xref="CDD:213381"
     Site            order(629,632,702,704..705)
                     /site_type="other"
                     /note="putative phospholipid binding site [chemical
                     binding]"
                     /db_xref="CDD:213381"
     CDS             1..726
                     /gene="MARK3"
                     /gene_synonym="CTAK1; KP78; Par-1a; PAR1A; VIPB"
                     /coded_by="NM_001411055.1:616..2796"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS91938.1"
                     /db_xref="GeneID:4140"
                     /db_xref="HGNC:HGNC:6897"
                     /db_xref="MIM:602678"
ORIGIN      
        1 mstrtplptv nerdtenhts hgdgrqevts rtsrsgarcr nsiascadeq phignyrllk
       61 tigkgnfakv klarhiltgr elfrevrimk ilnhpnivkl fevietektl ylimeyasgg
      121 evfdylvahg rmkekearsk frqivsavqy chqkrivhrd lkaenlllda dmnikiadfg
      181 fsneftvggk ldtfcgsppy aapelfqgkk ydgpevdvws lgvilytlvs gslpfdgqnl
      241 kelrervlrg kyripfymst dcenllkrfl vlnpikrgtl eqimkdrwin agheedelkp
      301 fvepeldisd qkridimvgm gysqeeiqes lskmkydeit atylllgrks seldasdsss
      361 ssnlslakvr pssdlnnstg qsphhkvqrs vsssqkqrry sdhagpaips vvaypkrsqt
      421 stadsdlked gissrkssgs avggkgiapa spmlgnasnp nkadiperkk sstvpssnta
      481 sggmtrrnty vcserttadr hsviqngken stipdqrtpv asthsissaa tpdrirfprg
      541 tasrstfhgq prerrtatyn gppaspslsh eatplsqtrs rgstnlfskl tskltrrlpt
      601 eyerngryeg ssrnvsaeqk denkeakprs lrftwsmktt ssmdpgdmmr eirkvldann
      661 cdyeqrerfl lfcvhgdgha enlvqwemev cklprlslng vrfkrisgts iafkniaski
      721 anelkl
//
LOCUS       NP_001425418             764 aa            linear   PRI 21-NOV-2025
DEFINITION  AT-rich interactive domain-containing protein 1B isoform 11 [Homo
            sapiens].
ACCESSION   NP_001425418
VERSION     NP_001425418.1
DBSOURCE    REFSEQ: accession NM_001438489.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Bosch,E., Guse,E., Kirchner,P., Winterpacht,A., Walther,M.,
            Alders,M., Kerkhof,J., Ekici,A.B., Sticht,H., Sadikovic,B., Reis,A.
            and Vasileiou,G.
  TITLE     The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation
  JOURNAL   Hum Genet 143 (8), 965-978 (2024)
   PUBMED   39028335
  REMARK    GeneRIF: The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation.
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Huang,X., Li,H., Yang,S., Ma,M., Lian,Y., Wu,X., Qi,X., Wang,X.,
            Rong,W. and Sheng,X.
  TITLE     De novo variation in ARID1B gene causes Coffin-Siris syndrome 1 in
            a Chinese family with excessive early-onset high myopia
  JOURNAL   BMC Med Genomics 17 (1), 142 (2024)
   PUBMED   38790056
  REMARK    GeneRIF: De novo variation in ARID1B gene causes Coffin-Siris
            syndrome 1 in a Chinese family with excessive early-onset high
            myopia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Hurlstone,A.F., Olave,I.A., Barker,N., van Noort,M. and Clevers,H.
  TITLE     Cloning and characterization of hELD/OSA1, a novel BRG1 interacting
            protein
  JOURNAL   Biochem J 364 (Pt 1), 255-264 (2002)
   PUBMED   11988099
  REMARK    GeneRIF: Cloning and characterization of hELD/OSA1, a novel BRG1
            interacting protein.
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Phelan,M.L., Sif,S., Narlikar,G.J. and Kingston,R.E.
  TITLE     Reconstitution of a core chromatin remodeling complex from SWI/SNF
            subunits
  JOURNAL   Mol Cell 3 (2), 247-253 (1999)
   PUBMED   10078207
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Imbert,G., Saudou,F., Yvert,G., Devys,D., Trottier,Y.,
            Garnier,J.M., Weber,C., Mandel,J.L., Cancel,G., Abbas,N., Durr,A.,
            Didierjean,O., Stevanin,G., Agid,Y. and Brice,A.
  TITLE     Cloning of the gene for spinocerebellar ataxia 2 reveals a locus
            with high sensitivity to expanded CAG/glutamine repeats
  JOURNAL   Nat Genet 14 (3), 285-291 (1996)
   PUBMED   8896557
REFERENCE   7  (residues 1 to 764)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
REFERENCE   8  (residues 1 to 764)
  AUTHORS   Vergano,S.A., van der Sluijs,P.J. and Santen,G.
  TITLE     ARID1B-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31132234
REFERENCE   9  (residues 1 to 764)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
REFERENCE   10 (residues 1 to 764)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355297.20, AL162578.13 and
            AL049820.23.
            
            Summary: This locus encodes an AT-rich DNA interacting
            domain-containing protein. The encoded protein is a component of
            the SWI/SNF chromatin remodeling complex and may play a role in
            cell-cycle activation. The protein encoded by this locus is similar
            to AT-rich interactive domain-containing protein 1A. These two
            proteins function as alternative, mutually exclusive ARID-subunits
            of the SWI/SNF complex. The associated complexes play opposing
            roles. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.464119.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..764
                     /product="AT-rich interactive domain-containing protein 1B
                     isoform 11"
                     /note="BRG1-binding protein ELD/OSA1; ELD (eyelid)/OSA
                     protein; BRG1-associated factor 250b; ARID
                     domain-containing protein 1B; AT rich interactive domain
                     1B (SWI1-like)"
                     /calculated_mol_wt=74902
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          155..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          321..414
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          487..546
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            487
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4N7; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          502..506
                     /region_name="LXXLL"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            608
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4N7; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            640
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     CDS             1..764
                     /gene="ARID1B"
                     /gene_synonym="6A3-5; BAF250B; BRIGHT; CSS1; DAN15;
                     ELD/OSA1; MRD12; OSA2; P250R; SMARCF2"
                     /coded_by="NM_001438489.1:304..2598"
                     /note="isoform 11 is encoded by transcript variant 12"
                     /db_xref="GeneID:57492"
                     /db_xref="HGNC:HGNC:18040"
                     /db_xref="MIM:614556"
ORIGIN      
        1 maaraaaaaa aaaararara gsgerrappg prpapgardl eagargaaaa aaapgpmlgg
       61 ggdgggglns vhhhpllprh elnmahnaga aaaagthsak sggseaalke ggsaaalsss
      121 ssssaaaaaa ssssssgpgs ametgllpnh klktvgeapa apphqqhhhh hhahhhhhha
      181 hhlhhhhalq qqlnqfqqqq qqqqqqqqqq qqqqhpisnn nslggaggga pqpgpdmeqp
      241 qhggakdsaa ggqadppgpp llskpgdedd appkmgepag gryehpglga lgtqqppvav
      301 pgggggpaav pefnnyygsa apasggpggr agpcfdqhgg qqspgmgmmh sasaaaagap
      361 gsmdplqnsh egypnsqcnh ypgysrpgag gggggggggg ggsggggggg gagaggagag
      421 avaaaaaaaa aaaggggggg yggssagygv lssprqqggg mmmgpgggga aslskaaags
      481 aaggfqrfag qnqhpsgatp tlnqlltsps pmmrsyggsy peysspsapp pppsqpqsqa
      541 aaagaaaggq qaaagmglgk dmgaqyaaas pawaaaqqrs hpamspgtpg ptmgrsqgsp
      601 mdpmvmkrpq lygmgsnphs qpqqsspypg gsygppgpqr ypigiqgrtp gamagmqypq
      661 qqmppqygqq gvsgycqqgq qpyysqqpqp phlppqaqyl psqsqqryqp qqdmsqegyg
      721 trsqpplapg kpnhedlnli qqerpsslpv evlasedaaf glkc
//
LOCUS       NP_001428153             472 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 7 [Homo sapiens].
ACCESSION   NP_001428153
VERSION     NP_001428153.1
DBSOURCE    REFSEQ: accession NM_001441224.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 472)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 472)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 472)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 472)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 472)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 472)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.703510.1,
                                           SRR1803616.92687.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..472
                     /product="calcium uptake protein 1, mitochondrial isoform
                     7"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=50129
     transit_peptide 1..33
                     /note="Mitochondrion. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:26387864; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
                     /calculated_mol_wt=3784
     Region          68..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          99..110
                     /region_name="Polybasic region.
                     /evidence=ECO:0000269|PubMed:27099988"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCX5; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          126..129
                     /region_name="K/R-ring.
                     /evidence=ECO:0000269|PubMed:32494073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          218..437
                     /region_name="EFh_MICU1"
                     /note="EF-hand, calcium binding motif, found in calcium
                     uptake protein 1, mitochondrial (MICU1) and similar
                     proteins; cd16173"
                     /db_xref="CDD:320081"
     Region          218..247
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Site            order(220,372,375,378..379,381,399)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:320081"
     Site            order(227,229,231,238,417,419,421,428)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320081"
     Region          255..259
                     /region_name="K/R-ring.
                     /evidence=ECO:0000269|PubMed:32494073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          273..303
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          371..400
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          408..437
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          451..461
                     /region_name="C-helix region.
                     /evidence=ECO:0000269|PubMed:24514027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Site            451
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:27642082; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
     CDS             1..472
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001441224.1:72..1490"
                     /note="isoform 7 is encoded by transcript variant 11"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mfrlnslsal aelavgsrwy hggsqpiqir rrlmmvaflg asavtastgl lwkrahaesp
       61 pcvdnlksdi gdkgknkdeg dvcnhekkta dlaphpeekk kkrsgfrdrk vmeyenrira
      121 ystpdkifry fatlkvisep geaevfmtpe dfvrsitpne kqpehlgldq yiikrfdgke
      181 rekfadegsi fytlgecgli sfsdyifltt vlstpqrnfe iafkmfdlng dgevdmeefe
      241 qvqsiirsqt smgmrhrdrp ttgntlksgl csalttyffg adlkgkltik nflefqrklq
      301 hdvlklefer hdpvdgrite rqfggmllay sgvqskklta mqrqlkkhfk egkgltfqev
      361 enfftflkni ndvdtalsfy hmagasldkv tmqqvartva kvelsdhvcd vvfalfdcdg
      421 ngelsnkefv simkqrlmrg lekpkdmgft rlmqamwkca qetawdfalp kq
//
LOCUS       NP_001400344             145 aa            linear   PRI 21-NOV-2025
DEFINITION  alpha-tocopherol transfer protein isoform 3 [Homo sapiens].
ACCESSION   NP_001400344
VERSION     NP_001400344.1
DBSOURCE    REFSEQ: accession NM_001413415.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Jeridi,C., Rachdi,A., Nabli,F., Saied,Z., Zouari,R., Ben
            Mohamed,D., Ben Said,M., Masmoudi,S., Ben Sassi,S. and Amouri,R.
  TITLE     Genetic heterogeneity within a consanguineous family involving TTPA
            and SETX genes
  JOURNAL   J Neurogenet 37 (4), 124-130 (2023)
   PUBMED   38109176
  REMARK    GeneRIF: Genetic heterogeneity within a consanguineous family
            involving TTPA and SETX genes.
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Ulatowski,L., Ghelfi,M., West,R., Atkinson,J., Finno,C.J. and
            Manor,D.
  TITLE     The tocopherol transfer protein mediates vitamin E trafficking
            between cerebellar astrocytes and neurons
  JOURNAL   J Biol Chem 298 (3), 101712 (2022)
   PUBMED   35150738
  REMARK    GeneRIF: The tocopherol transfer protein mediates vitamin E
            trafficking between cerebellar astrocytes and neurons.
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Arai,H. and Kono,N.
  TITLE     alpha-Tocopherol transfer protein (alpha-TTP)
  JOURNAL   Free Radic Biol Med 176, 162-175 (2021)
   PUBMED   34563650
  REMARK    GeneRIF: alpha-Tocopherol transfer protein (alpha-TTP).
            Review article
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 145)
  AUTHORS   Gotoda,T., Arita,M., Arai,H., Inoue,K., Yokota,T., Fukuo,Y.,
            Yazaki,Y. and Yamada,N.
  TITLE     Adult-onset spinocerebellar dysfunction caused by a mutation in the
            gene for the alpha-tocopherol-transfer protein
  JOURNAL   N Engl J Med 333 (20), 1313-1318 (1995)
   PUBMED   7566022
REFERENCE   6  (residues 1 to 145)
  AUTHORS   Arita,M., Sato,Y., Miyata,A., Tanabe,T., Takahashi,E., Kayden,H.J.,
            Arai,H. and Inoue,K.
  TITLE     Human alpha-tocopherol transfer protein: cDNA cloning, expression
            and chromosomal localization
  JOURNAL   Biochem J 306 (Pt 2) (Pt 2), 437-443 (1995)
   PUBMED   7887897
REFERENCE   7  (residues 1 to 145)
  AUTHORS   Ouahchi,K., Arita,M., Kayden,H., Hentati,F., Ben Hamida,M.,
            Sokol,R., Arai,H., Inoue,K., Mandel,J.L. and Koenig,M.
  TITLE     Ataxia with isolated vitamin E deficiency is caused by mutations in
            the alpha-tocopherol transfer protein
  JOURNAL   Nat Genet 9 (2), 141-145 (1995)
   PUBMED   7719340
REFERENCE   8  (residues 1 to 145)
  AUTHORS   Ben Hamida,C., Doerflinger,N., Belal,S., Linder,C., Reutenauer,L.,
            Dib,C., Gyapay,G., Vignal,A., Le Paslier,D., Cohen,D. et al.
  TITLE     Localization of Friedreich ataxia phenotype with selective vitamin
            E deficiency to chromosome 8q by homozygosity mapping
  JOURNAL   Nat Genet 5 (2), 195-200 (1993)
   PUBMED   8252047
REFERENCE   9  (residues 1 to 145)
  AUTHORS   Schuelke,M.
  TITLE     Ataxia with Vitamin E Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301419
REFERENCE   10 (residues 1 to 145)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC120042.3.
            
            Summary: This gene encodes a soluble protein that binds
            alpha-trocopherol, a form of vitamin E, with high selectivity and
            affinity. This protein plays an important role in regulating
            vitamin E levels in the body by transporting vitamin E between
            membrane vesicles and facilitating the secretion of vitamin E from
            hepatocytes to circulating lipoproteins. Mutations in this gene
            cause hereditary vitamin E deficiency (ataxia with vitamin E
            deficiency, AVED) and retinitis pigmentosa. [provided by RefSeq,
            Nov 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.241803.1,
                                           SRR1660805.201278.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.3"
     Protein         1..145
                     /product="alpha-tocopherol transfer protein isoform 3"
                     /note="tocopherol (alpha) transfer protein (ataxia
                     (Friedreich-like) with vitamin E deficiency); alpha-TTP"
                     /calculated_mol_wt=16243
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49638.1)"
     Region          <40..73
                     /region_name="CRAL_TRIO_N"
                     /note="CRAL/TRIO, N-terminal domain; smart01100"
                     /db_xref="CDD:215024"
     CDS             1..145
                     /gene="TTPA"
                     /gene_synonym="alphaTTP; ATTP; AVED; TTP1"
                     /coded_by="NM_001413415.1:33..470"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:7274"
                     /db_xref="HGNC:HGNC:12404"
                     /db_xref="MIM:600415"
ORIGIN      
        1 maearsqpsa gpqlnalpdh spllqpglaa lrrrareagv plaplpltds fllrflrard
       61 fdldlawrll knyykwraec peisadlhpr siigllkagy hgvlrsrdpt gskvliyrid
      121 shaweqlqtk lasafprhss sgiww
//
LOCUS       NP_001423776             564 aa            linear   PRI 21-NOV-2025
DEFINITION  semaphorin-4F isoform 5 precursor [Homo sapiens].
ACCESSION   NP_001423776 XP_047298885 XP_054196170
VERSION     NP_001423776.1
DBSOURCE    REFSEQ: accession NM_001436847.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Fan,Q., Barathi,V.A., Cheng,C.Y., Zhou,X., Meguro,A., Nakata,I.,
            Khor,C.C., Goh,L.K., Li,Y.J., Lim,W., Ho,C.E., Hawthorne,F.,
            Zheng,Y., Chua,D., Inoko,H., Yamashiro,K., Ohno-Matsui,K.,
            Matsuo,K., Matsuda,F., Vithana,E., Seielstad,M., Mizuki,N.,
            Beuerman,R.W., Tai,E.S., Yoshimura,N., Aung,T., Young,T.L.,
            Wong,T.Y., Teo,Y.Y. and Saw,S.M.
  TITLE     Genetic variants on chromosome 1q41 influence ocular axial length
            and high myopia
  JOURNAL   PLoS Genet 8 (6), e1002753 (2012)
   PUBMED   22685421
REFERENCE   5  (residues 1 to 564)
  AUTHORS   Parrinello,S., Noon,L.A., Harrisingh,M.C., Wingfield Digby,P.,
            Rosenberg,L.H., Cremona,C.A., Echave,P., Flanagan,A.M., Parada,L.F.
            and Lloyd,A.C.
  TITLE     NF1 loss disrupts Schwann cell-axonal interactions: a novel role
            for semaphorin 4F
  JOURNAL   Genes Dev 22 (23), 3335-3348 (2008)
   PUBMED   19056885
  REMARK    GeneRIF: Sema4F levels were strongly reduced in a panel of human
            neurofibromas, confirming the relevance of these findings to the
            human disease.
REFERENCE   6  (residues 1 to 564)
  AUTHORS   Ayala,G.E., Dai,H., Powell,M., Li,R., Ding,Y., Wheeler,T.M.,
            Shine,D., Kadmon,D., Thompson,T., Miles,B.J., Ittmann,M.M. and
            Rowley,D.
  TITLE     Cancer-related axonogenesis and neurogenesis in prostate cancer
  JOURNAL   Clin Cancer Res 14 (23), 7593-7603 (2008)
   PUBMED   19047084
REFERENCE   7  (residues 1 to 564)
  AUTHORS   Park,Y.D., Park,D., Bhak,J. and Yang,J.M.
  TITLE     Proteomic approaches to the analysis of atopic dermatitis and new
            insights from interactomics
  JOURNAL   Proteomics Clin Appl 2 (3), 290-300 (2008)
   PUBMED   21136834
REFERENCE   8  (residues 1 to 564)
  AUTHORS   Francks,C., Fisher,S.E., Olson,R.K., Pennington,B.F., Smith,S.D.,
            DeFries,J.C. and Monaco,A.P.
  TITLE     Fine mapping of the chromosome 2p12-16 dyslexia susceptibility
            locus: quantitative association analysis and positional candidate
            genes SEMA4F and OTX1
  JOURNAL   Psychiatr Genet 12 (1), 35-41 (2002)
   PUBMED   11901358
  REMARK    GeneRIF: Fine mapping of the chromosome 2p12-16 dyslexia
            susceptibility candidate gene
REFERENCE   9  (residues 1 to 564)
  AUTHORS   Schultze,W., Eulenburg,V., Lessmann,V., Herrmann,L., Dittmar,T.,
            Gundelfinger,E.D., Heumann,R. and Erdmann,K.S.
  TITLE     Semaphorin4F interacts with the synapse-associated protein
            SAP90/PSD-95
  JOURNAL   J Neurochem 78 (3), 482-489 (2001)
   PUBMED   11483650
REFERENCE   10 (residues 1 to 564)
  AUTHORS   Encinas,J.A., Kikuchi,K., Chedotal,A., de Castro,F., Goodman,C.S.
            and Kimura,T.
  TITLE     Cloning, expression, and genetic mapping of Sema W, a member of the
            semaphorin family
  JOURNAL   Proc Natl Acad Sci U S A 96 (5), 2491-2496 (1999)
   PUBMED   10051670
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007387.4.
            
            On or before Mar 24, 2025 this sequence version replaced
            XP_047298885.1, XP_054196170.1.
            
            Summary: This gene encodes a transmembrane class IV semaphorin
            family protein, which plays a role in neural development. This gene
            may be involved in neurogenesis in prostate cancer, the development
            of neurofibromas, and breast cancer tumorigenesis. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Nov 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.1288183.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMEA2159912
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..564
                     /product="semaphorin-4F isoform 5 precursor"
                     /note="semaphorin M; semaphorin-4F; semaphorin-W; sema
                     domain immunoglobulin domain transmembrane domain (TM) and
                     short cytoplasmic domain (semaphorin) 4F; sema domain,
                     immunoglobulin domain (Ig), transmembrane domain (TM) and
                     short cytoplasmic domain, (semaphorin) 4F"
                     /calculated_mol_wt=58974
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3311
     Region          52..478
                     /region_name="Sema_4F"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 4F (Sema4F); cd11261"
                     /db_xref="CDD:200522"
     Site            order(114..116,139,160,162..163,165,181,184,186,191,223,
                     247..251,253,332..333,369,373,376)
                     /site_type="other"
                     /note="plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200522"
     Site            order(224..225,227,230..232,266,269..271,273,275,299..301,
                     305..306,382,397)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200522"
     Region          479..530
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     CDS             1..564
                     /gene="SEMA4F"
                     /gene_synonym="M-SEMA; m-Sema-M; PRO2353; S4F; SEMAM;
                     SEMAW"
                     /coded_by="NM_001436847.1:131..1825"
                     /note="isoform 5 precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:10505"
                     /db_xref="HGNC:HGNC:10734"
                     /db_xref="MIM:603706"
ORIGIN      
        1 mpasaarprp gpgqptaspf pllllavlsg pvsgrvprsv prtslpisea dscltrfavp
       61 htynysvllv dpashtlyvg ardtifalsl pfsgerprri dwmvpeahrq ncrkkgkked
      121 vsrfqqverl esgrgkcpfe paqrsaavma ggvlyaatvk nylgtepiit ravgraedwi
      181 rtdtlpswln apafvaaval spaewgdedg ddeiyfffte tsrafdsyer ikvprvarvc
      241 agdlggrktl qqrwttflka dllcpgpehg rassvlqdva vlrpelgagt pifygifssq
      301 wegatisavc afrpqdirtv lngpfrelkh dcnrglpvvd ndvpqprpge citnnmklrh
      361 fgsslslpdr vltfirdhpl mdrpvfpadg hpllvttdta ylrvvahrvt slsgkeydvl
      421 ylgtedghlh ravrigaqls vledlalfpe pqpvenmkly hswllvgsrt evtqvnttnc
      481 grlqscseci laqdpvcaws frldecvaha gehrglvqdi esadvsslcp kepggkrpwk
      541 kgnmnlqdss qqnklstcyl ykgl
//
LOCUS       NP_001394095             568 aa            linear   PRI 21-NOV-2025
DEFINITION  retinoblastoma-associated protein isoform 3 [Homo sapiens].
ACCESSION   NP_001394095
VERSION     NP_001394095.1
DBSOURCE    REFSEQ: accession NM_001407166.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Castro,A., Ruiz Rivera,A., Moorman,C.C., Wolf-Saxon,E.R.,
            Mims,H.N., Vasquez Meza,V.I., Rangel,M.A., Loera,M.M., Bond,I.C.,
            Buchanan,S.B., Villarreal,E., Tripathi,S., Rubin,S.M. and
            Burke,J.R.
  TITLE     Structural and functional analysis of cancer-associated missense
            variants in the retinoblastoma protein pocket domain
  JOURNAL   J Biol Chem 301 (3), 108284 (2025)
   PUBMED   39938803
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Zhang,S., Valenzuela,L.F., Zatulovskiy,E., Mangiante,L., Curtis,C.
            and Skotheim,J.M.
  TITLE     The G1-S transition is promoted by Rb degradation via the E3 ligase
            UBR5
  JOURNAL   Sci Adv 10 (43), eadq6858 (2024)
   PUBMED   39441926
  REMARK    GeneRIF: The G1-S transition is promoted by Rb degradation via the
            E3 ligase UBR5.
REFERENCE   4  (residues 1 to 568)
  AUTHORS   Schwartz,C.J., Marra,A., Selenica,P., Gazzo,A., Tan,K., Ross,D.,
            Razavi,P., Chandarlapaty,S., Weigelt,B., Reis-Filho,J.S., Brogi,E.,
            Pareja,F. and Wen,H.Y.
  TITLE     RB1 Genetic Alterations in Estrogen Receptor-Positive Breast
            Carcinomas: Correlation With Neuroendocrine Differentiation
  JOURNAL   Mod Pathol 37 (8), 100541 (2024)
   PUBMED   38897452
  REMARK    GeneRIF: RB1 Genetic Alterations in Estrogen Receptor-Positive
            Breast Carcinomas: Correlation With Neuroendocrine Differentiation.
REFERENCE   5  (residues 1 to 568)
  AUTHORS   Konagaya,Y., Rosenthal,D., Ratnayeke,N., Fan,Y. and Meyer,T.
  TITLE     An intermediate Rb-E2F activity state safeguards proliferation
            commitment
  JOURNAL   Nature 631 (8020), 424-431 (2024)
   PUBMED   38926571
  REMARK    GeneRIF: An intermediate Rb-E2F activity state safeguards
            proliferation commitment.
REFERENCE   6  (residues 1 to 568)
  AUTHORS   Lohmann,D.R. and Gallie,B.L.
  TITLE     Retinoblastoma
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301625
REFERENCE   7  (residues 1 to 568)
  AUTHORS   Dyson,N., Guida,P., Munger,K. and Harlow,E.
  TITLE     Homologous sequences in adenovirus E1A and human papillomavirus E7
            proteins mediate interaction with the same set of cellular proteins
  JOURNAL   J Virol 66 (12), 6893-6902 (1992)
   PUBMED   1331501
REFERENCE   8  (residues 1 to 568)
  AUTHORS   Huang,S., Shin,E., Sheppard,K.A., Chokroverty,L., Shan,B.,
            Qian,Y.W., Lee,E.Y. and Yee,A.S.
  TITLE     The retinoblastoma protein region required for interaction with the
            E2F transcription factor includes the T/E1A binding and
            carboxy-terminal sequences
  JOURNAL   DNA Cell Biol 11 (7), 539-548 (1992)
   PUBMED   1388726
REFERENCE   9  (residues 1 to 568)
  AUTHORS   Onadim,Z., Hogg,A., Baird,P.N. and Cowell,J.K.
  TITLE     Oncogenic point mutations in exon 20 of the RB1 gene in families
            showing incomplete penetrance and mild expression of the
            retinoblastoma phenotype
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 6177-6181 (1992)
   PUBMED   1352883
REFERENCE   10 (residues 1 to 568)
  AUTHORS   Hogg,A., Onadim,Z., Baird,P.N. and Cowell,J.K.
  TITLE     Detection of heterozygous mutations in the RB1 gene in
            retinoblastoma patients using single-strand conformation
            polymorphism analysis and polymerase chain reaction sequencing
  JOURNAL   Oncogene 7 (7), 1445-1451 (1992)
   PUBMED   1352398
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL392048.9.
            
            Summary: The protein encoded by this gene is a negative regulator
            of the cell cycle and was the first tumor suppressor gene found.
            The encoded protein also stabilizes constitutive heterochromatin to
            maintain the overall chromatin structure. The active,
            hypophosphorylated form of the protein binds transcription factor
            E2F1. Defects in this gene are a cause of childhood cancer
            retinoblastoma (RB), bladder cancer, and osteogenic sarcoma.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1125763.1,
                                           SRR14038197.131273.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.2"
     Protein         1..568
                     /product="retinoblastoma-associated protein isoform 3"
                     /note="retinoblastoma-associated protein;
                     prepro-retinoblastoma-associated protein; protein
                     phosphatase 1, regulatory subunit 130; retinoblastoma
                     suspectibility protein; retinoblastoma 1"
                     /calculated_mol_wt=64743
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            2
                     /site_type="methylation"
                     /note="N,N-dimethylproline.
                     /evidence=ECO:0000250|UniProtKB:P13405; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Region          114..227
                     /region_name="DUF3452"
                     /note="Domain of unknown function (DUF3452); pfam11934"
                     /db_xref="CDD:463402"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:1756735,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:1756735,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Region          373..568
                     /region_name="RB_A"
                     /note="Retinoblastoma-associated protein A domain;
                     pfam01858"
                     /db_xref="CDD:460364"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:1756735,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK2.
                     /evidence=ECO:0000269|PubMed:10499802; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     CDS             1..568
                     /gene="RB1"
                     /gene_synonym="OSRC; p105-Rb; p110-RB1; pp110; PPP1R130;
                     pRb; RB"
                     /coded_by="NM_001407166.1:163..1869"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:5925"
                     /db_xref="HGNC:HGNC:9884"
                     /db_xref="MIM:614041"
ORIGIN      
        1 mppktprkta ataaaaaaep papppppppe edpeqdsgpe dlplvrlefe eteepdftal
       61 cqklkipdhv rerawltwek vssvdgvlgg yiqkkkelwg icifiaavdl demsftftel
      121 qknieisvhk ffnllkeidt stkvdnamsr llkkydvlfa lfsklertce liyltqpsss
      181 isteinsalv lkvswitfll akgevlqmed dlvisfqlml cvldyfikls ppmllkepyk
      241 tavipingsp rtprrgqnrs ariakqlend triievlcke hecnidevkn vyfknfipfm
      301 nslglvtsng lpevenlskr yeeiylknkd ldarlfldhd ktlqtdsids fetqrtprks
      361 nldeevnvip phtpvrtvmn tiqqlmmiln sasdqpsenl isyfnnctvn pkesilkrvk
      421 digyifkekf akavgqgcve igsqryklgv rlyyrvmesm lkseeerlsi qnfskllndn
      481 ifhmsllaca levvmatysr stsqnldsgt dlsfpwilnv lnlkafdfyk viesfikaeg
      541 nltremikhl ercehrimes lawlsvss
//
LOCUS       NP_001428250             262 aa            linear   PRI 21-NOV-2025
DEFINITION  dnaJ homolog subfamily B member 13 isoform 3 [Homo sapiens].
ACCESSION   NP_001428250 XP_005274041 XP_054224691
VERSION     NP_001428250.1
DBSOURCE    REFSEQ: accession NM_001441321.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Zhang,X., Xiao,Z., Zhang,J., Xu,C., Liu,S., Cheng,L., Zhou,S.,
            Zhao,S., Zhang,Y., Wu,J., Wang,Y. and Liu,M.
  TITLE     Differential requirements of IQUB for the assembly of radial spoke
            1 and the motility of mouse cilia and flagella
  JOURNAL   Cell Rep 41 (8), 111683 (2022)
   PUBMED   36417862
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Liu,M., Li,J., Jiang,C., Zhou,Y., Sun,Y., Yang,Y. and Shen,Y.
  TITLE     A novel homozygous mutation in DNAJB13-a gene associated with the
            sperm axoneme-leads to teratozoospermia
  JOURNAL   J Assist Reprod Genet 39 (3), 757-764 (2022)
   PUBMED   35166991
  REMARK    GeneRIF: A novel homozygous mutation in DNAJB13-a gene associated
            with the sperm axoneme-leads to teratozoospermia.
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Li,W.N., Zhu,L., Jia,M.M., Yin,S.L., Lu,G.X. and Liu,G.
  TITLE     Missense mutation in DNAJB13 gene correlated with male fertility in
            asthenozoospermia
  JOURNAL   Andrology 8 (2), 299-306 (2020)
   PUBMED   31342671
  REMARK    GeneRIF: Missense mutation in DNAJB13 gene correlated with male
            fertility in asthenozoospermia.
REFERENCE   5  (residues 1 to 262)
  AUTHORS   El Khouri,E., Thomas,L., Jeanson,L., Bequignon,E., Vallette,B.,
            Duquesnoy,P., Montantin,G., Copin,B., Dastot-Le Moal,F.,
            Blanchon,S., Papon,J.F., Lores,P., Yuan,L., Collot,N., Tissier,S.,
            Faucon,C., Gacon,G., Patrat,C., Wolf,J.P., Dulioust,E.,
            Crestani,B., Escudier,E., Coste,A., Legendre,M., Toure,A. and
            Amselem,S.
  TITLE     Mutations in DNAJB13, Encoding an HSP40 Family Member, Cause
            Primary Ciliary Dyskinesia and Male Infertility
  JOURNAL   Am J Hum Genet 99 (2), 489-500 (2016)
   PUBMED   27486783
  REMARK    GeneRIF: this study, which establishes mutations in DNAJB13 as a
            cause of PCD, unveils the key role played by DNAJB13 in the proper
            formation and function of ciliary and flagellar axonemes in humans
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Li,W. and Liu,G.
  TITLE     DNAJB13, a type II HSP40 family member, localizes to the spermatids
            and spermatozoa during mouse spermatogenesis
  JOURNAL   BMC Dev Biol 14, 38 (2014)
   PUBMED   25233908
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Toure,A., Rode,B., Hunnicutt,G.R., Escalier,D. and Gacon,G.
  TITLE     Septins at the annulus of mammalian sperm
  JOURNAL   Biol Chem 392 (8-9), 799-803 (2011)
   PUBMED   21740329
  REMARK    Review article
REFERENCE   8  (residues 1 to 262)
  AUTHORS   Liu,G., Lu,G.X. and Xing,X.W.
  TITLE     Molecular cloning of TSARG6 gene related to apoptosis in human
            spermatogenic cells
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 36 (2), 93-98 (2004)
   PUBMED   14970903
  REMARK    GeneRIF: TSARG6 is specifically expressed in adult testis with a
            transcript of 1.8 kb, which has a role in spermatogenesis and
            apoptosis
REFERENCE   9  (residues 1 to 262)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003717.3.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_005274041.1, XP_054224691.1.
            
            Summary: This gene encodes a member of the heat shock protein 40
            co-chaperone family which is produced in large amounts in the
            testis and is located on the radial spokes of the axoneme in human
            sperm flagella and other flagellar structures. The encoded protein
            associates with the sperm annulus, as part of the septin complex,
            through direct interaction with septin 4, during sperm terminal
            differentiation. Naturally occurring mutations in this gene are
            associated with primary ciliary dyskinesia and male infertility.
            [provided by RefSeq, Apr 2017].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14243140.9625697.1,
                                           DRR138516.109164.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..262
                     /product="dnaJ homolog subfamily B member 13 isoform 3"
                     /note="DnaJ (Hsp40) related, subfamily B, member 13;
                     radial spoke 16 homolog A; dnaJ homolog subfamily B member
                     13; DnaJ-like protein; testis and spermatogenesis
                     cell-related protein 6; testis spermatocyte
                     apoptosis-related gene 6 protein; testis spermatogenesis
                     apoptosis-related gene 3 protein; testis spermatogenesis
                     apoptosis-related gene 6 protein; DnaJ (Hsp40) homolog,
                     subfamily B, member 13"
                     /calculated_mol_wt=29940
     Region          5..257
                     /region_name="PTZ00037"
                     /note="DnaJ_C chaperone protein; Provisional"
                     /db_xref="CDD:240236"
     CDS             1..262
                     /gene="DNAJB13"
                     /gene_synonym="CILD34; RSPH16A; TSARG5; TSARG6"
                     /coded_by="NM_001441321.1:45..833"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:374407"
                     /db_xref="HGNC:HGNC:30718"
                     /db_xref="MIM:610263"
ORIGIN      
        1 mgqdyysvlg itrnsedaqi kqayrrlalk hhplksneps saeifrqiae aydvlsdqff
       61 daegsevdln fgglqgrgvk kqdpqverdl ylsledlffg ctkkikisrr vlnedgysst
      121 ikdkiltidv kpgwrqgtri tfekegdqgp niipadiifi vkeklhprfr rendnlffvn
      181 piplgkaltc ctvevrtldd rllnipindi ihpkyfkkvp gegmplpedp tkkgdlfiff
      241 diqfptrltp qkkqmlrqal lt
//
LOCUS       NP_001400604             322 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 8 precursor [Homo sapiens].
ACCESSION   NP_001400604
VERSION     NP_001400604.1
DBSOURCE    REFSEQ: accession NM_001413675.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 322)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 322)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 322)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 322)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 322)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3132195.1,
                                           SRR14038196.116470.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..322
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 8 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=32733
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..291
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     CDS             1..322
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413675.1:169..1137"
                     /note="isoform 8 precursor is encoded by transcript
                     variant 11"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvsyih gssqaqfvae shiilvlsil lryrriekgk
      301 lklhvfkltf flavniktfk rh
//
LOCUS       NP_001400842             451 aa            linear   PRI 21-NOV-2025
DEFINITION  transcription factor ETV6 isoform 2 [Homo sapiens].
ACCESSION   NP_001400842 XP_011518909
VERSION     NP_001400842.1
DBSOURCE    REFSEQ: accession NM_001413913.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Xu,W., Tian,F., Tai,X., Song,G., Liu,Y., Fan,L., Weng,X., Yang,E.,
            Wang,M., Bornhauser,M., Zhang,C., Lock,R.B., Wong,J.W.H., Wang,J.,
            Jing,D. and Mi,J.Q.
  TITLE     ETV6::ACSL6 translocation-driven super-enhancer activation leads to
            eosinophilia in acute lymphoblastic leukemia through IL-3
            overexpression
  JOURNAL   Haematologica 109 (8), 2445-2458 (2024)
   PUBMED   38356460
  REMARK    GeneRIF: ETV6::ACSL6 translocation-driven super-enhancer activation
            leads to eosinophilia in acute lymphoblastic leukemia through IL-3
            overexpression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Xue,S., Sun,H.P., Huang,X.B., Chen,X., Wang,T., Ma,W., Tian,Y.,
            Pan,Z.L., Li,L.H., Zhang,L., Liu,H.X. and Cao,X.Y.
  TITLE     Characteristics and literature review of ETV6::ABL1 fusion
            gene-positive acute myeloid leukemia
  JOURNAL   Int J Hematol 119 (5), 564-572 (2024)
   PUBMED   38441775
  REMARK    GeneRIF: Characteristics and literature review of ETV6::ABL1 fusion
            gene-positive acute myeloid leukemia.
            Review article
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Mueller,S.B., Pikman,Y., Tasian,S.K., Silverman,L.B., Harris,M.H.
            and Tsai,H.K.
  TITLE     ETV6 fusions from insertions of exons 3-5 in pediatric hematologic
            malignancies
  JOURNAL   Haematologica 108 (12), 3471-3476 (2023)
   PUBMED   37381775
  REMARK    GeneRIF: ETV6 fusions from insertions of exons 3-5 in pediatric
            hematologic malignancies.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Klubickova,N., Mosaieby,E., Ptakova,N., Trinquet,A., Lae,M.,
            Costes-Martineau,V. and Skalova,A.
  TITLE     High-grade non-intestinal type sinonasal adenocarcinoma with
            ETV6::NTRK3 fusion, distinct from secretory carcinoma by
            immunoprofile and morphology
  JOURNAL   Virchows Arch 483 (2), 187-195 (2023)
   PUBMED   37415052
  REMARK    GeneRIF: High-grade non-intestinal type sinonasal adenocarcinoma
            with ETV6::NTRK3 fusion, distinct from secretory carcinoma by
            immunoprofile and morphology.
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Romana,S.P., Mauchauffe,M., Le Coniat,M., Chumakov,I., Le
            Paslier,D., Berger,R. and Bernard,O.A.
  TITLE     The t(12;21) of acute lymphoblastic leukemia results in a tel-AML1
            gene fusion
  JOURNAL   Blood 85 (12), 3662-3670 (1995)
   PUBMED   7780150
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Golub,T.R., Barker,G.F., Bohlander,S.K., Hiebert,S.W., Ward,D.C.,
            Bray-Ward,P., Morgan,E., Raimondi,S.C., Rowley,J.D. and
            Gilliland,D.G.
  TITLE     Fusion of the TEL gene on 12p13 to the AML1 gene on 21q22 in acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 92 (11), 4917-4921 (1995)
   PUBMED   7761424
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Buijs,A., Sherr,S., van Baal,S., van Bezouw,S., van der Plas,D.,
            Geurts van Kessel,A., Riegman,P., Lekanne Deprez,R., Zwarthoff,E.,
            Hagemeijer,A. et al.
  TITLE     Translocation (12;22) (p13;q11) in myeloproliferative disorders
            results in fusion of the ETS-like TEL gene on 12p13 to the MN1 gene
            on 22q11
  JOURNAL   Oncogene 10 (8), 1511-1519 (1995)
   PUBMED   7731705
  REMARK    Erratum:[Oncogene 1995 Aug 17;11(4):809]
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Pencheva,B., Di Paola,J. and Porter,C.C.
  TITLE     ETV6-Related Thrombocytopenia and Predisposition to Leukemia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   33226740
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Fainstein,E., Einat,M., Gokkel,E., Marcelle,C., Croce,C.M.,
            Gale,R.P. and Canaani,E.
  TITLE     Nucleotide sequence analysis of human abl and bcr-abl cDNAs
  JOURNAL   Oncogene 4 (12), 1477-1481 (1989)
   PUBMED   2687768
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007450.1, AC084430.13 and
            AC084358.19.
            
            On Nov 9, 2022 this sequence version replaced XP_011518909.1.
            
            Summary: This gene encodes an ETS family transcription factor. The
            product of this gene contains two functional domains: a N-terminal
            pointed (PNT) domain that is involved in protein-protein
            interactions with itself and other proteins, and a C-terminal
            DNA-binding domain. Gene knockout studies in mice suggest that it
            is required for hematopoiesis and maintenance of the developing
            vascular network. This gene is known to be involved in a large
            number of chromosomal rearrangements associated with leukemia and
            congenital fibrosarcoma. [provided by RefSeq, Sep 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2163077.1,
                                           SRR14038194.3369903.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..451
                     /product="transcription factor ETV6 isoform 2"
                     /note="ets variant gene 6 (TEL oncogene); TEL1 oncogene;
                     transcription factor ETV6; ETS-related protein Tel1;
                     ETV6-RUNX1 fusion protein"
                     /calculated_mol_wt=52741
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12435397,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            53..54
                     /site_type="other"
                     /note="Breakpoint for translocation to form ETV6-MDS2 in
                     MDS; propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            54..55
                     /site_type="other"
                     /note="Breakpoint for translocation to form PAX5-ETV6;
                     propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Region          55..122
                     /region_name="SAM_PNT-Tel_Yan"
                     /note="Sterile alpha motif (SAM)/Pointed domain of Tel/Yan
                     protein; cd08535"
                     /db_xref="CDD:176085"
     Site            order(62,84,87..89,91..92,95,97,99..100,103..104)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:176085"
     Site            order(74..79,106..108,110..111,114..115)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:176085"
     Region          157..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97360; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14.
                     /evidence=ECO:0000269|PubMed:12435397; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            301
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97360; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            335..336
                     /site_type="other"
                     /note="Breakpoint for translocation to form ETV6-AML1 in
                     ALL; propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Region          337..423
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..451
                     /gene="ETV6"
                     /gene_synonym="TEL; TEL/ABL; THC5"
                     /coded_by="NM_001413913.1:455..1810"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:2120"
                     /db_xref="HGNC:HGNC:3495"
                     /db_xref="MIM:600618"
ORIGIN      
        1 msetpaqcsi kerisytppe spvpsyasst plhvpvpral rmeedsirlp ahlrlqpiyw
       61 srddvaqwlk waenefslrp idsntfemng kalllltked fryrsphsgd vlyellqhil
      121 kqrkprilfs pffhpgnsih tqpevilhqn heedncvqrt prpsvdnvhh npptiellhr
      181 srspittnhr pspdpeqrpl rspldnmirr lspaeraqgp rphqennhqe syplsvspme
      241 nnhcpasses hpkpssprqe strviqlmps pimhplilnp rhsvdfkqsr lsedglhreg
      301 kpinlshred laymnhimvs vsppeehamp igriadcrll wdyvyqllsd sryenfirwe
      361 dkeskifriv dpnglarlwg nhknrtnmty ekmsralrhy yklniirkep gqrllfrfmk
      421 tpdeimsgrt drlehlesqe ldeqiyqede c
//
LOCUS       NP_001422922            1036 aa            linear   PRI 21-NOV-2025
DEFINITION  histone deacetylase 4 isoform 4 [Homo sapiens].
ACCESSION   NP_001422922
VERSION     NP_001422922.1
DBSOURCE    REFSEQ: accession NM_001435993.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Liu,W. and Luo,G.
  TITLE     NEDD9 is transcriptionally regulated by HDAC4 and promotes breast
            cancer metastasis and macrophage M2 polarization via the
            FAK/NF-kappaB signaling pathway
  JOURNAL   Neoplasia 57, 101059 (2024)
   PUBMED   39326322
  REMARK    GeneRIF: NEDD9 is transcriptionally regulated by HDAC4 and promotes
            breast cancer metastasis and macrophage M2 polarization via the
            FAK/NF-kappaB signaling pathway.
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1036)
  AUTHORS   Di Giorgio,E., Dalla,E., Tolotto,V., D'Este,F., Paluvai,H.,
            Ranzino,L. and Brancolini,C.
  TITLE     HDAC4 influences the DNA damage response and counteracts senescence
            by assembling with HDAC1/HDAC2 to control H2BK120 acetylation and
            homology-directed repair
  JOURNAL   Nucleic Acids Res 52 (14), 8218-8240 (2024)
   PUBMED   38874468
  REMARK    GeneRIF: HDAC4 influences the DNA damage response and counteracts
            senescence by assembling with HDAC1/HDAC2 to control H2BK120
            acetylation and homology-directed repair.
REFERENCE   5  (residues 1 to 1036)
  AUTHORS   Chen,Q. and Lao,J.
  TITLE     Interference with Histone Deacetylase 4 Regulates c-Jun N-terminal
            Kinase/Activating Protein-1 Signaling to Ameliorate Sepsis-induced
            Alveolar Epithelial Cell Injury
  JOURNAL   J Physiol Investig 67 (4), 174-186 (2024)
   PUBMED   39133038
  REMARK    GeneRIF: Interference with Histone Deacetylase 4 Regulates c-Jun
            N-terminal Kinase/Activating Protein-1 Signaling to Ameliorate
            Sepsis-induced Alveolar Epithelial Cell Injury.
REFERENCE   6  (residues 1 to 1036)
  AUTHORS   Pazin,M.J. and Kadonaga,J.T.
  TITLE     What's up and down with histone deacetylation and transcription?
  JOURNAL   Cell 89 (3), 325-328 (1997)
   PUBMED   9150131
  REMARK    Review article
REFERENCE   7  (residues 1 to 1036)
  AUTHORS   Wolffe,A.P.
  TITLE     Transcriptional control. Sinful repression
  JOURNAL   Nature 387 (6628), 16-17 (1997)
   PUBMED   9139815
REFERENCE   8  (residues 1 to 1036)
  AUTHORS   Ohara,O., Nagase,T., Ishikawa,K., Nakajima,D., Ohira,M., Seki,N.
            and Nomura,N.
  TITLE     Construction and characterization of human brain cDNA libraries
            suitable for analysis of cDNA clones encoding relatively large
            proteins
  JOURNAL   DNA Res 4 (1), 53-59 (1997)
   PUBMED   9179496
REFERENCE   9  (residues 1 to 1036)
  AUTHORS   Wilson,L.C., Leverton,K., Oude Luttikhuis,M.E., Oley,C.A.,
            Flint,J., Wolstenholme,J., Duckett,D.P., Barrow,M.A., Leonard,J.V.,
            Read,A.P. et al.
  TITLE     Brachydactyly and mental retardation: an Albright hereditary
            osteodystrophy-like syndrome localized to 2q37
  JOURNAL   Am J Hum Genet 56 (2), 400-407 (1995)
   PUBMED   7847374
REFERENCE   10 (residues 1 to 1036)
  AUTHORS   Doherty,E.S. and Lacbawan,F.L.
  TITLE     2q37 Microdeletion Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301337
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC062017.6 and AC017028.11.
            
            Summary: Histones play a critical role in transcriptional
            regulation, cell cycle progression, and developmental events.
            Histone acetylation/deacetylation alters chromosome structure and
            affects transcription factor access to DNA. The protein encoded by
            this gene belongs to class II of the histone deacetylase/acuc/apha
            family. It possesses histone deacetylase activity and represses
            transcription when tethered to a promoter. This protein does not
            bind DNA directly, but through transcription factors MEF2C and
            MEF2D. It seems to interact in a multiprotein complex with RbAp48
            and HDAC3. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1029935.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..1036
                     /product="histone deacetylase 4 isoform 4"
                     /EC_number="3.5.1.98"
                     /note="histone deacetylase A"
                     /calculated_mol_wt=113938
     Region          15..104
                     /region_name="ClassIIa_HDAC4_Gln-rich-N"
                     /note="Glutamine-rich N-terminal helical domain of HDAC4,
                     a Class IIa histone deacetylase; cd10162"
                     /db_xref="CDD:197398"
     Site            order(16..17,19..20,23,27,30..31,34..35,37..38,41..42,
                     44..45,48..50,52..54,56..57,59..61,63..64,67,70..71,
                     74..76)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:197398"
     Site            order(16..17,19..20,23,27,30,34,37,41..42,44..45,48..49,
                     52,56,59,63,70,74)
                     /site_type="other"
                     /note="dimer interface A, C [polypeptide binding]"
                     /db_xref="CDD:197398"
     Site            order(27,31,35,38,42,45,49..50,53..54,57,61,64)
                     /site_type="other"
                     /note="dimer interface A, D [polypeptide binding]"
                     /db_xref="CDD:197398"
     Site            order(45,49,60..61,64,71,75..76)
                     /site_type="other"
                     /note="dimer interface A, B [polypeptide binding]"
                     /db_xref="CDD:197398"
     Region          601..1009
                     /region_name="HDAC4"
                     /note="Histone deacetylase 4; cd10006"
                     /db_xref="CDD:212530"
     Site            order(754..755,763..764,792,794,886,926)
                     /site_type="active"
                     /db_xref="CDD:212530"
     Site            order(792,794,886)
                     /site_type="other"
                     /note="Zn binding site 1 [ion binding]"
                     /db_xref="CDD:212530"
     CDS             1..1036
                     /gene="HDAC4"
                     /gene_synonym="AHO3; BDMR; HA6116; HD4; HDAC-4; HDAC-A;
                     HDACA; NEDCHF; NEDCHID"
                     /coded_by="NM_001435993.1:225..3335"
                     /note="isoform 4 is encoded by transcript variant 8"
                     /db_xref="GeneID:9759"
                     /db_xref="HGNC:HGNC:14063"
                     /db_xref="MIM:605314"
ORIGIN      
        1 mdlrldhqfs lpvaepalre qqlqqellal kqkqqiqrqi liaefqrqhe qlsrqheaql
       61 hehikqqqem lamkhqqell ehqrklerhr qeqelekqhr eqklqqlknk ekgkesavas
      121 tevkmklqef vlnkkkalah rnlnhcissd prywygktqh ssldqssppq sgvstsynhp
      181 vlgmydakdd fplrktasep nlklrsrlkq kvaerrsspl lrrkdgpvvt alkkrpldvt
      241 dsacssapgs gpsspnnssg svsaengiap avpsipaets lahrlvareg saaplplyts
      301 pslpnitlgl patgpsagta gqqdaerltl palqqrlslf pgthltpyls tsplerdgga
      361 ahspllqhmv lleqppaqap lvtglgalpl haqslvgadr vspsihklrq hrplgrtqsa
      421 plpqnaqalq hlviqqqhqq flekhkqqfq qqqlqmnkii pkpseparqp eshpeeteee
      481 lrehqallde pyldrlpgqk eahaqagvqv kqepiesdee eaepprevep gqrqpseqel
      541 lfrqqallle qqrihqlrny qasmeaagip vsfgghrpls raqsspasat fpvsvqeppt
      601 kprfttglvy dtlmlkhqct cgsssshpeh agriqsiwsr lqetglrgkc ecirgrkatl
      661 eelqtvhsea htllygtnpl nrqkldskkl lgslasvfvr lpcggvgvds dtiwnevhsa
      721 gaarlavgcv velvfkvatg elkngfavvr ppghhaeest pmgfcyfnsv avaakllqqr
      781 lsvskilivd wdvhhgngtq qafysdpsvl ymslhryddg nffpgsgapd evgtgpgvgf
      841 nvnmaftggl dppmgdaeyl aafrtvvmpi asefapdvvl vssgfdaveg hptplggynl
      901 sarcfgyltk qlmglaggri vlalegghdl taicdaseac vsallgneld plpekvlqqr
      961 pnanavrsme kvmeihskyw rclqrttsta grslieaqtc eneeaetvta maslsvgvkp
     1021 aekrpdeepm eeeppl
//
LOCUS       NP_001400923             337 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, NMDA 2B isoform b precursor [Homo
            sapiens].
ACCESSION   NP_001400923
VERSION     NP_001400923.1
DBSOURCE    REFSEQ: accession NM_001413994.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Korinek,M., Candelas Serra,M., Abdel Rahman,F., Dobrovolski,M.,
            Kuchtiak,V., Abramova,V., Fili,K., Tomovic,E., Hrcka Krausova,B.,
            Krusek,J., Cerny,J., Vyklicky,L., Balik,A. and Smejkalova,T.
  TITLE     Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B genes:
            Insights into NMDA Receptor Structure, Function, and
            Pathophysiology
  JOURNAL   Physiol Res 73 (Suppl 1), S413-S434 (2024)
   PUBMED   38836461
  REMARK    GeneRIF: Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B
            genes: Insights into NMDA Receptor Structure, Function, and
            Pathophysiology.
            Review article
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Raich,I., Lillo,J., Rebassa,J.B., Capo,T., Cordomi,A.,
            Reyes-Resina,I., Pallas,M. and Navarro,G.
  TITLE     Dual Role of NMDAR Containing NR2A and NR2B Subunits in Alzheimer's
            Disease
  JOURNAL   Int J Mol Sci 25 (9), 4757 (2024)
   PUBMED   38731978
  REMARK    GeneRIF: Dual Role of NMDAR Containing NR2A and NR2B Subunits in
            Alzheimer's Disease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Iacobucci,G.J. and Popescu,G.K.
  TITLE     NMDA receptors: linking physiological output to biophysical
            operation
  JOURNAL   Nat Rev Neurosci 18 (4), 236-249 (2017)
   PUBMED   28303017
  REMARK    Review article
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Hu,C., Chen,W., Myers,S.J., Yuan,H. and Traynelis,S.F.
  TITLE     Human GRIN2B variants in neurodevelopmental disorders
  JOURNAL   J Pharmacol Sci 132 (2), 115-121 (2016)
   PUBMED   27818011
  REMARK    GeneRIF: In this review, mutations in GRIN2B were described as
            distributed throughout the entire gene in patients with
            neuropsychiatric and developmental disorders.
            Review article
            Erratum:[J Pharmacol Sci. 2017 Apr;133(4):280. doi:
            10.1016/j.jphs.2017.04.001. PMID: 28434657]
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Hess,S.D., Daggett,L.P., Crona,J., Deal,C., Lu,C.C., Urrutia,A.,
            Chavez-Noriega,L., Ellis,S.B., Johnson,E.C. and Velicelebi,G.
  TITLE     Cloning and functional characterization of human heteromeric
            N-methyl-D-aspartate receptors
  JOURNAL   J Pharmacol Exp Ther 278 (2), 808-816 (1996)
   PUBMED   8768735
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Kornau,H.C., Schenker,L.T., Kennedy,M.B. and Seeburg,P.H.
  TITLE     Domain interaction between NMDA receptor subunits and the
            postsynaptic density protein PSD-95
  JOURNAL   Science 269 (5231), 1737-1740 (1995)
   PUBMED   7569905
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Magnuson,D.S., Knudsen,B.E., Geiger,J.D., Brownstone,R.M. and
            Nath,A.
  TITLE     Human immunodeficiency virus type 1 tat activates
            non-N-methyl-D-aspartate excitatory amino acid receptors and causes
            neurotoxicity
  JOURNAL   Ann Neurol 37 (3), 373-380 (1995)
   PUBMED   7695237
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Mandich,P., Schito,A.M., Bellone,E., Antonacci,R., Finelli,P.,
            Rocchi,M. and Ajmar,F.
  TITLE     Mapping of the human NMDAR2B receptor subunit gene (GRIN2B) to
            chromosome 12p12
  JOURNAL   Genomics 22 (1), 216-218 (1994)
   PUBMED   7959773
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Platzer,K. and Lemke,J.R.
  TITLE     GRIN2B-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29851452
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Monyer,H., Sprengel,R., Schoepfer,R., Herb,A., Higuchi,M.,
            Lomeli,H., Burnashev,N., Sakmann,B. and Seeburg,P.H.
  TITLE     Heteromeric NMDA receptors: molecular and functional distinction of
            subtypes
  JOURNAL   Science 256 (5060), 1217-1221 (1992)
   PUBMED   1350383
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007916.10, AC007784.7 and
            AC007397.21.
            
            Summary: This gene encodes a member of the N-methyl-D-aspartate
            (NMDA) receptor family within the ionotropic glutamate receptor
            superfamily. The encoded protein is a subunit of the NMDA receptor
            ion channel which acts as an agonist binding site for glutamate.
            The NMDA receptors mediate a slow calcium-permeable component of
            excitatory synaptic transmission in the central nervous system. The
            NMDA receptors are heterotetramers of seven genetically encoded,
            differentially expressed subunits including NR1 (GRIN1), NR2
            (GRIN2A, GRIN2B, GRIN2C, or GRIN2D) and NR3 (GRIN3A or GRIN3B). The
            early expression of this gene in development suggests a role in
            brain development, circuit formation, synaptic plasticity, and
            cellular migration and differentiation. Naturally occurring
            mutations within this gene are associated with neurodevelopmental
            disorders including autism spectrum disorder, attention deficit
            hyperactivity disorder, epilepsy, and schizophrenia. [provided by
            RefSeq, Aug 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410571.158682.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.1"
     Protein         1..337
                     /product="glutamate receptor ionotropic, NMDA 2B isoform b
                     precursor"
                     /note="glutamate [NMDA] receptor subunit epsilon-2;
                     glutamate receptor subunit epsilon-2; N-methyl-D-aspartate
                     receptor subunit 3; N-methyl D-aspartate receptor subtype
                     2B; GluN2B(alt_5'UTR); glutamate receptor ionotropic, NMDA
                     2B; glutamate receptor, ionotropic, N-methyl D-aspartate
                     2B"
                     /calculated_mol_wt=34767
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2820
     Region          33..337
                     /region_name="PBP1_iGluR_NMDA_NR2"
                     /note="N-terminal leucine-isoleucine-valine-binding
                     protein (LIVBP)-like domain of the NR2 subunit of NMDA
                     receptor family; cd06378"
                     /db_xref="CDD:380601"
     Site            order(33,77..79,114,135,175,177,192,207..208,311..312)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:380601"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:26912815,
                     ECO:0007744|PDB:5EWJ, ECO:0007744|PDB:5EWL,
                     ECO:0007744|PDB:5EWM; propagated from UniProtKB/Swiss-Prot
                     (Q13224.3)"
     Site            order(75..80,82..83,118..119,175,179,206,208,311..317,
                     321..323,334)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:380601"
     CDS             1..337
                     /gene="GRIN2B"
                     /gene_synonym="DEE27; EIEE27; GluN2B; hNR3; MRD6; NMDAR2B;
                     NR2B; NR3"
                     /coded_by="NM_001413994.1:709..1722"
                     /note="isoform b precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:2904"
                     /db_xref="HGNC:HGNC:4586"
                     /db_xref="MIM:138252"
ORIGIN      
        1 mkpraeccsp kfwlvlavla vsgsrarsqk sppsigiavi lvgtsdevai kdahekddfh
       61 hlsvvprvel vamnetdpks iitricdlms drkiqgvvfa ddtdqeaiaq ildfisaqtl
      121 tpilgihggs smimadkdes smffqfgpsi eqqasvmlni meeydwyifs ivttyfpgyq
      181 dfvnkirsti ensfvgwele evllldmsld dgdskiqnql kklqspiill yctkeeatyi
      241 fevansvglt gygytwivps lvagdtdtvp aefptglisv sydewdyglp arvrdgiaii
      301 ttaasdmlse hsfipepkss cynthekriy qsnmlnr
//
LOCUS       NP_001427725             173 aa            linear   PRI 21-NOV-2025
DEFINITION  translocon-associated protein subunit delta isoform 2 precursor
            [Homo sapiens].
ACCESSION   NP_001427725 XP_047298346 XP_054183598
VERSION     NP_001427725.1
DBSOURCE    REFSEQ: accession NM_001440796.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Gemmer,M., Chaillet,M.L., van Loenhout,J., Cuevas Arenas,R.,
            Vismpas,D., Grollers-Mulderij,M., Koh,F.A., Albanese,P.,
            Scheltema,R.A., Howes,S.C., Kotecha,A., Fedry,J. and Forster,F.
  TITLE     Visualization of translation and protein biogenesis at the ER
            membrane
  JOURNAL   Nature 614 (7946), 160-167 (2023)
   PUBMED   36697828
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Castiglioni,C., Feillet,F., Barnerias,C., Wiedemann,A., Muchart,J.,
            Cortes,F., Hernando-Davalillo,C., Montero,R., Dupre,T., Bruneel,A.,
            Seta,N., Vuillaumier-Barrot,S. and Serrano,M.
  TITLE     Expanding the phenotype of X-linked SSR4-CDG: Connective tissue
            implications
  JOURNAL   Hum Mutat 42 (2), 142-149 (2021)
   PUBMED   33300232
  REMARK    GeneRIF: Expanding the phenotype of X-linked SSR4-CDG: Connective
            tissue implications.
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Ng,B.G., Raymond,K., Kircher,M., Buckingham,K.J., Wood,T.,
            Shendure,J., Nickerson,D.A., Bamshad,M.J., Wong,J.T.,
            Monteiro,F.P., Graham,B.H., Jackson,S., Sparkes,R., Scheuerle,A.E.,
            Cathey,S., Kok,F., Gibson,J.B. and Freeze,H.H.
  CONSRTM   University of Washington Center for Mendelian Genomics
  TITLE     Expanding the Molecular and Clinical Phenotype of SSR4-CDG
  JOURNAL   Hum Mutat 36 (11), 1048-1051 (2015)
   PUBMED   26264460
  REMARK    GeneRIF: We now report eight affected males with either de novo (4)
            or inherited (4) loss of function mutations in SSR4.
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   5  (residues 1 to 173)
  AUTHORS   Wang,Z. and VandeBerg,J.L.
  TITLE     Cloning and molecular characterization of a human ortholog of
            Monodelphis TRAPD in ultraviolet B-induced melanoma
  JOURNAL   Melanoma Res 14 (2), 107-114 (2004)
   PUBMED   15057039
  REMARK    GeneRIF: results of this study implicate TRAPD as a candidate gene
            with potential functions that might be associated with
            ultraviolet-induced melanomagenesis and metastasis
REFERENCE   6  (residues 1 to 173)
  AUTHORS   Dodson,G. and Steiner,D.
  TITLE     The role of assembly in insulin's biosynthesis
  JOURNAL   Curr Opin Struct Biol 8 (2), 189-194 (1998)
   PUBMED   9631292
  REMARK    Review article
REFERENCE   7  (residues 1 to 173)
  AUTHORS   Brenner,V., Nyakatura,G., Rosenthal,A. and Platzer,M.
  TITLE     Genomic organization of two novel genes on human Xq28: compact head
            to head arrangement of IDH gamma and TRAP delta is conserved in rat
            and mouse
  JOURNAL   Genomics 44 (1), 8-14 (1997)
   PUBMED   9286695
REFERENCE   8  (residues 1 to 173)
  AUTHORS   Holthuis,J.C., van Riel,M.C. and Martens,G.J.
  TITLE     Translocon-associated protein TRAP delta and a novel TRAP-like
            protein are coordinately expressed with pro-opiomelanocortin in
            Xenopus intermediate pituitary
  JOURNAL   Biochem J 312 (Pt 1) (Pt 1), 205-213 (1995)
   PUBMED   7492314
REFERENCE   9  (residues 1 to 173)
  AUTHORS   Hartmann,E., Gorlich,D., Kostka,S., Otto,A., Kraft,R., Knespel,S.,
            Burger,E., Rapoport,T.A. and Prehn,S.
  TITLE     A tetrameric complex of membrane proteins in the endoplasmic
            reticulum
  JOURNAL   Eur J Biochem 214 (2), 375-381 (1993)
   PUBMED   7916687
REFERENCE   10 (residues 1 to 173)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U52111.3.
            
            On or before May 30, 2025 this sequence version replaced
            XP_047298346.1, XP_054183598.1.
            
            Summary: This gene encodes the delta subunit of the
            translocon-associated protein complex which is involved in
            translocating proteins across the endoplasmic reticulum membrane.
            The encoded protein is located in the Xq28 region and is arranged
            in a compact head-to-head manner with the isocitrate dehydrogenase
            3 (NAD+) gamma gene and both genes are driven by a CpG-embedded
            bidirectional promoter. Alternate splicing results in multiple
            transcript variants.[provided by RefSeq, Mar 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2719450.1,
                                           ERR4368409.186436.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..173
                     /product="translocon-associated protein subunit delta
                     isoform 2 precursor"
                     /note="translocon-associated protein subunit delta;
                     SSR-delta; TRAP-delta; signal sequence receptor, delta"
                     /calculated_mol_wt=16766
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2251
     Region          24..172
                     /region_name="TRAP-delta"
                     /note="Translocon-associated protein, delta subunit
                     precursor (TRAP-delta); pfam05404"
                     /db_xref="CDD:398850"
     Site            145..165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51571.1)"
     CDS             1..173
                     /gene="SSR4"
                     /gene_synonym="CDG1Y; TRAPD"
                     /coded_by="NM_001440796.1:279..800"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:6748"
                     /db_xref="HGNC:HGNC:11326"
                     /db_xref="MIM:300090"
ORIGIN      
        1 maamaslgal allllsslsr csaeaclepq itpsyyttsd avistetvfi veisltcknr
       61 vqnmalyadv ggkqfpvtrg qdvgryqvsw sldhksahag tyevrffdee sysllrkaqr
      121 nnedisiipp lftvsvdhrg twngpwvste vlaaaiglvi yylafsaksh iqa
//
LOCUS       NP_001428160             278 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 14 [Homo sapiens].
ACCESSION   NP_001428160
VERSION     NP_001428160.1
DBSOURCE    REFSEQ: accession NM_001441231.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 278)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 278)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 278)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1259410.1,
                                           SRR1803616.23687.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..278
                     /product="calcium uptake protein 1, mitochondrial isoform
                     14"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=31800
     Region          24..243
                     /region_name="EFh_MICU1"
                     /note="EF-hand, calcium binding motif, found in calcium
                     uptake protein 1, mitochondrial (MICU1) and similar
                     proteins; cd16173"
                     /db_xref="CDD:320081"
     Region          24..53
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Site            order(26,178,181,184..185,187,205)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:320081"
     Site            order(33,35,37,44,223,225,227,234)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320081"
     Region          79..109
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          177..206
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          214..243
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     CDS             1..278
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001441231.1:777..1613"
                     /note="isoform 14 is encoded by transcript variant 18"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mvslkaklnh lrqsmlkqka pqrnfeiafk mfdlngdgev dmeefeqvqs iirsqtsmgm
       61 rhrdrpttgn tlksglcsal ttyffgadlk gkltiknfle fqrklqhdvl kleferhdpv
      121 dgriterqfg gmllaysgvq skkltamqrq lkkhfkegkg ltfqevenff tflknindvd
      181 talsfyhmag asldkvtmqq vartvakvel sdhvcdvvfa lfdcdgngel snkefvsimk
      241 qrlmrglekp kdmgftrlmq amwkcaqeta wdfalpkq
//
LOCUS       NP_001425619             929 aa            linear   PRI 21-NOV-2025
DEFINITION  splicing regulator ARVCF isoform 6 [Homo sapiens].
ACCESSION   NP_001425619 XP_005261301 XP_054181608
VERSION     NP_001425619.1
DBSOURCE    REFSEQ: accession NM_001438690.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 929)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 929)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 929)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 929)
  AUTHORS   Suzuki,N., Idogawa,M., Tange,S., Ohashi,T., Sasaki,Y., Nakase,H.
            and Tokino,T.
  TITLE     p53-induced ARVCF modulates the splicing landscape and supports the
            tumor suppressive function of p53
  JOURNAL   Oncogene 39 (10), 2202-2211 (2020)
   PUBMED   31827232
  REMARK    GeneRIF: p53-induced ARVCF modulates the splicing landscape and
            supports the tumor suppressive function of p53.
REFERENCE   5  (residues 1 to 929)
  AUTHORS   Zhang,D., Tang,N., Liu,Y. and Wang,E.H.
  TITLE     ARVCF expression is significantly correlated with the malignant
            phenotype of non-small cell lung cancer
  JOURNAL   Mol Carcinog 54 Suppl 1, E185-E191 (2015)
   PUBMED   25683624
  REMARK    GeneRIF: observed ARVCF-dependent changes in small GTPase (mainly
            RhoA) activity in lung cancer cells. We confirmed that ARVCF plays
            an important role in the malignant phenotype
REFERENCE   6  (residues 1 to 929)
  AUTHORS   Mariner,D.J., Wang,J. and Reynolds,A.B.
  TITLE     ARVCF localizes to the nucleus and adherens junction and is
            mutually exclusive with p120(ctn) in E-cadherin complexes
  JOURNAL   J Cell Sci 113 (Pt 8), 1481-1490 (2000)
   PUBMED   10725230
REFERENCE   7  (residues 1 to 929)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   8  (residues 1 to 929)
  AUTHORS   Sirotkin,H., Morrow,B., Saint-Jore,B., Puech,A., Das Gupta,R.,
            Patanjali,S.R., Skoultchi,A., Weissman,S.M. and Kucherlapati,R.
  TITLE     Identification, characterization, and precise mapping of a human
            gene encoding a novel membrane-spanning protein from the 22q11
            region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 42 (2), 245-251 (1997)
   PUBMED   9192844
REFERENCE   9  (residues 1 to 929)
  AUTHORS   Sirotkin,H., O'Donnell,H., DasGupta,R., Halford,S., St Jore,B.,
            Puech,A., Parimoo,S., Morrow,B., Skoultchi,A., Weissman,S.M.,
            Scambler,P. and Kucherlapati,R.
  TITLE     Identification of a new human catenin gene family member (ARVCF)
            from the region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 41 (1), 75-83 (1997)
   PUBMED   9126485
REFERENCE   10 (residues 1 to 929)
  AUTHORS   Lindsay,E.A., Goldberg,R., Jurecic,V., Morrow,B., Carlson,C.,
            Kucherlapati,R.S., Shprintzen,R.J. and Baldini,A.
  TITLE     Velo-cardio-facial syndrome: frequency and extent of 22q11
            deletions
  JOURNAL   Am J Med Genet 57 (3), 514-522 (1995)
   PUBMED   7677167
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005663.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_005261301.1, XP_054181608.1.
            
            Summary: Armadillo Repeat gene deleted in Velo-Cardio-Facial
            syndrome (ARVCF) is a member of the catenin family. This family
            plays an important role in the formation of adherens junction
            complexes, which are thought to facilitate communication between
            the inside and outside environments of a cell. The ARVCF gene was
            isolated in the search for the genetic defect responsible for the
            autosomal dominant Velo-Cardio-Facial syndrome (VCFS), a relatively
            common human disorder with phenotypic features including cleft
            palate, conotruncal heart defects and facial dysmorphology. The
            ARVCF gene encodes a protein containing two motifs, a coiled coil
            domain in the N-terminus and a 10 armadillo repeat sequence in the
            midregion. Since these sequences can facilitate protein-protein
            interactions ARVCF is thought to function in a protein complex. In
            addition, ARVCF contains a predicted nuclear-targeting sequence
            suggesting that it may have a function as a nuclear protein.
            [provided by RefSeq, Jun 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.393620.1,
                                           SRR14038192.3637749.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..929
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..929
                     /product="splicing regulator ARVCF isoform 6"
                     /note="armadillo repeat protein deleted in
                     velo-cardio-facial syndrome; armadillo repeat gene deleted
                     in velocardiofacial syndrome; splicing regulator ARVCF"
                     /calculated_mol_wt=100653
     Region          95..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            170
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P98203; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          186..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          266..290
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          348..387
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          360..385
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(376,380,384,418,422,426,461,466,470)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          389..428
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          390..429
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          393..429
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          432..473
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          433..467
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          436..471
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          468..508
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          478..529
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          526..565
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          575..622
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          590..614
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          607..623
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          640..680
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          650..686
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          650..686
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          693..732
                     /region_name="ARM 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          696..731
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          696..730
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          733..775
                     /region_name="ARM 9"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          737..782
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          788..820
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            858
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            865
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            866
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            909
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     CDS             1..929
                     /gene="ARVCF"
                     /coded_by="NM_001438690.1:308..3097"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="GeneID:421"
                     /db_xref="HGNC:HGNC:728"
                     /db_xref="MIM:602269"
ORIGIN      
        1 medcnvhsaa silasvkeqe arferltral eqerrhvalq leraqqpgmv sggmgsgqpl
       61 pmawqqlvlq eqspgsqasl atmpeapdvl eetvtveedp gtptshvsiv tsedgttrrt
      121 etkvtktvkt vttrtvrqvp vgpdglplld ggpplgpfad galdrhfllr gggpvatlsr
      181 aylssgggfp egpeprdsps ygslsrglgm rppragplgp gpgdgcftlp ghreafpvgp
      241 epgppggrsl perfqaepyg leddtrslaa ddeggpelep dygtatrrrp ecgrglhtra
      301 yedtaddgge laderpafpm vtaplaqper gsmgsldrlv rrspsvdsar keprwrdpel
      361 pevlamlrhp vdpvkanaaa ylqhlcfene gvkrrvrqlr glpllvalld hpraevrrra
      421 cgalrnlsyg rdtdnkaair dcggvpalvr llraardnev relvtgtlwn lssyeplkmv
      481 iidhglqtlt hevivphsgw erepnedskp rdaewttvfk ntsgclrnvs sdgaearrrl
      541 receglvdal lhalqsavgr kdtdnksven cvcimrnlsy hvhkevpgad ryqeaepgpl
      601 gsavgsqrrr rddascfggk kakgkkdgem drnfdtldlp krteaakgfe llyqpevvrl
      661 ylslltesrn fntleaaaga lqnlsagnwm watyiratvr kerglpvlve llqsetdkvv
      721 ravaialrnl sldrrnkdli gsyamaelvr nvrnaqappr pgacleedtv vavlntihei
      781 vsdsldnars llqargvpal valvassqsv reakaashvl qtvwsykelr gtlqkdgwtk
      841 arfqsaaata kgpkgalspg gfddstlplv dkslegektg srdvipmdal gpdgystvdr
      901 rerrprgass ageasekepl kgpgpascs
//
LOCUS       NP_001400844             364 aa            linear   PRI 21-NOV-2025
DEFINITION  transcription factor ETV6 isoform 4 [Homo sapiens].
ACCESSION   NP_001400844 XP_011518913
VERSION     NP_001400844.1
DBSOURCE    REFSEQ: accession NM_001413915.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Xu,W., Tian,F., Tai,X., Song,G., Liu,Y., Fan,L., Weng,X., Yang,E.,
            Wang,M., Bornhauser,M., Zhang,C., Lock,R.B., Wong,J.W.H., Wang,J.,
            Jing,D. and Mi,J.Q.
  TITLE     ETV6::ACSL6 translocation-driven super-enhancer activation leads to
            eosinophilia in acute lymphoblastic leukemia through IL-3
            overexpression
  JOURNAL   Haematologica 109 (8), 2445-2458 (2024)
   PUBMED   38356460
  REMARK    GeneRIF: ETV6::ACSL6 translocation-driven super-enhancer activation
            leads to eosinophilia in acute lymphoblastic leukemia through IL-3
            overexpression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Xue,S., Sun,H.P., Huang,X.B., Chen,X., Wang,T., Ma,W., Tian,Y.,
            Pan,Z.L., Li,L.H., Zhang,L., Liu,H.X. and Cao,X.Y.
  TITLE     Characteristics and literature review of ETV6::ABL1 fusion
            gene-positive acute myeloid leukemia
  JOURNAL   Int J Hematol 119 (5), 564-572 (2024)
   PUBMED   38441775
  REMARK    GeneRIF: Characteristics and literature review of ETV6::ABL1 fusion
            gene-positive acute myeloid leukemia.
            Review article
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Mueller,S.B., Pikman,Y., Tasian,S.K., Silverman,L.B., Harris,M.H.
            and Tsai,H.K.
  TITLE     ETV6 fusions from insertions of exons 3-5 in pediatric hematologic
            malignancies
  JOURNAL   Haematologica 108 (12), 3471-3476 (2023)
   PUBMED   37381775
  REMARK    GeneRIF: ETV6 fusions from insertions of exons 3-5 in pediatric
            hematologic malignancies.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Klubickova,N., Mosaieby,E., Ptakova,N., Trinquet,A., Lae,M.,
            Costes-Martineau,V. and Skalova,A.
  TITLE     High-grade non-intestinal type sinonasal adenocarcinoma with
            ETV6::NTRK3 fusion, distinct from secretory carcinoma by
            immunoprofile and morphology
  JOURNAL   Virchows Arch 483 (2), 187-195 (2023)
   PUBMED   37415052
  REMARK    GeneRIF: High-grade non-intestinal type sinonasal adenocarcinoma
            with ETV6::NTRK3 fusion, distinct from secretory carcinoma by
            immunoprofile and morphology.
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Romana,S.P., Mauchauffe,M., Le Coniat,M., Chumakov,I., Le
            Paslier,D., Berger,R. and Bernard,O.A.
  TITLE     The t(12;21) of acute lymphoblastic leukemia results in a tel-AML1
            gene fusion
  JOURNAL   Blood 85 (12), 3662-3670 (1995)
   PUBMED   7780150
REFERENCE   7  (residues 1 to 364)
  AUTHORS   Golub,T.R., Barker,G.F., Bohlander,S.K., Hiebert,S.W., Ward,D.C.,
            Bray-Ward,P., Morgan,E., Raimondi,S.C., Rowley,J.D. and
            Gilliland,D.G.
  TITLE     Fusion of the TEL gene on 12p13 to the AML1 gene on 21q22 in acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 92 (11), 4917-4921 (1995)
   PUBMED   7761424
REFERENCE   8  (residues 1 to 364)
  AUTHORS   Buijs,A., Sherr,S., van Baal,S., van Bezouw,S., van der Plas,D.,
            Geurts van Kessel,A., Riegman,P., Lekanne Deprez,R., Zwarthoff,E.,
            Hagemeijer,A. et al.
  TITLE     Translocation (12;22) (p13;q11) in myeloproliferative disorders
            results in fusion of the ETS-like TEL gene on 12p13 to the MN1 gene
            on 22q11
  JOURNAL   Oncogene 10 (8), 1511-1519 (1995)
   PUBMED   7731705
  REMARK    Erratum:[Oncogene 1995 Aug 17;11(4):809]
REFERENCE   9  (residues 1 to 364)
  AUTHORS   Pencheva,B., Di Paola,J. and Porter,C.C.
  TITLE     ETV6-Related Thrombocytopenia and Predisposition to Leukemia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   33226740
REFERENCE   10 (residues 1 to 364)
  AUTHORS   Fainstein,E., Einat,M., Gokkel,E., Marcelle,C., Croce,C.M.,
            Gale,R.P. and Canaani,E.
  TITLE     Nucleotide sequence analysis of human abl and bcr-abl cDNAs
  JOURNAL   Oncogene 4 (12), 1477-1481 (1989)
   PUBMED   2687768
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007450.1 and AC084358.19.
            
            On Nov 9, 2022 this sequence version replaced XP_011518913.1.
            
            Summary: This gene encodes an ETS family transcription factor. The
            product of this gene contains two functional domains: a N-terminal
            pointed (PNT) domain that is involved in protein-protein
            interactions with itself and other proteins, and a C-terminal
            DNA-binding domain. Gene knockout studies in mice suggest that it
            is required for hematopoiesis and maintenance of the developing
            vascular network. This gene is known to be involved in a large
            number of chromosomal rearrangements associated with leukemia and
            congenital fibrosarcoma. [provided by RefSeq, Sep 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.4180776.1,
                                           SRR1163658.341894.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..364
                     /product="transcription factor ETV6 isoform 4"
                     /note="ets variant gene 6 (TEL oncogene); TEL1 oncogene;
                     transcription factor ETV6; ETS-related protein Tel1;
                     ETV6-RUNX1 fusion protein"
                     /calculated_mol_wt=42691
     Region          <1..35
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     Region          250..336
                     /region_name="ETS"
                     /note="erythroblast transformation specific domain;
                     smart00413"
                     /db_xref="CDD:197710"
     CDS             1..364
                     /gene="ETV6"
                     /gene_synonym="TEL; TEL/ABL; THC5"
                     /coded_by="NM_001413915.1:589..1683"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:2120"
                     /db_xref="HGNC:HGNC:3495"
                     /db_xref="MIM:600618"
ORIGIN      
        1 mngkallllt kedfryrsph sgdvlyellq hilkqrkpri lfspffhpgn sihtqpevil
       61 hqnheedncv qrtprpsvdn vhhnpptiel lhrsrspitt nhrpspdpeq rplrspldnm
      121 irrlspaera qgprphqenn hqesyplsvs pmennhcpas seshpkpssp rqestrviql
      181 mpspimhpli lnprhsvdfk qsrlsedglh regkpinlsh redlaymnhi mvsvsppeeh
      241 ampigriadc rllwdyvyql lsdsryenfi rwedkeskif rivdpnglar lwgnhknrtn
      301 mtyekmsral rhyyklniir kepgqrllfr fmktpdeims grtdrlehle sqeldeqiyq
      361 edec
//
LOCUS       NP_001397857             449 aa            linear   PRI 21-NOV-2025
DEFINITION  telomeric repeat-binding factor 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001397857 XP_005251349
VERSION     NP_001397857.1
DBSOURCE    REFSEQ: accession NM_001410928.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Hu,H., van Roon,A.M., Ghanim,G.E., Ahsan,B., Oluwole,A.O.,
            Peak-Chew,S.Y., Robinson,C.V. and Nguyen,T.H.D.
  TITLE     Structural basis of telomeric nucleosome recognition by shelterin
            factor TRF1
  JOURNAL   Sci Adv 9 (34), eadi4148 (2023)
   PUBMED   37624885
  REMARK    GeneRIF: Structural basis of telomeric nucleosome recognition by
            shelterin factor TRF1.
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Harmak,H., Redouane,S., Charoute,H., Aniq Filali,O., Barakat,A. and
            Rouba,H.
  TITLE     In silico exploration and molecular dynamics of deleterious SNPs on
            the human TERF1 protein triggering male infertility
  JOURNAL   J Biomol Struct Dyn 41 (24), 14665-14688 (2023)
   PUBMED   36995171
  REMARK    GeneRIF: In silico exploration and molecular dynamics of
            deleterious SNPs on the human TERF1 protein triggering male
            infertility.
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Abreu,P.L., Lee,Y.W. and Azzalin,C.M.
  TITLE     In Vitro Characterization of the Physical Interactions between the
            Long Noncoding RNA TERRA and the Telomeric Proteins TRF1 and TRF2
  JOURNAL   Int J Mol Sci 23 (18), 10463 (2022)
   PUBMED   36142374
  REMARK    GeneRIF: In Vitro Characterization of the Physical Interactions
            between the Long Noncoding RNA TERRA and the Telomeric Proteins
            TRF1 and TRF2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Jack,A., Kim,Y., Strom,A.R., Lee,D.S.W., Williams,B., Schaub,J.M.,
            Kellogg,E.H., Finkelstein,I.J., Ferro,L.S., Yildiz,A. and
            Brangwynne,C.P.
  TITLE     Compartmentalization of telomeres through DNA-scaffolded phase
            separation
  JOURNAL   Dev Cell 57 (2), 277-290 (2022)
   PUBMED   35077681
  REMARK    GeneRIF: Compartmentalization of telomeres through DNA-scaffolded
            phase separation.
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Broccoli,D., Chong,L., Oelmann,S., Fernald,A.A., Marziliano,N., van
            Steensel,B., Kipling,D., Le Beau,M.M. and de Lange,T.
  TITLE     Comparison of the human and mouse genes encoding the telomeric
            protein, TRF1: chromosomal localization, expression and conserved
            protein domains
  JOURNAL   Hum Mol Genet 6 (1), 69-76 (1997)
   PUBMED   9002672
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Lu,K.P., Hanes,S.D. and Hunter,T.
  TITLE     A human peptidyl-prolyl isomerase essential for regulation of
            mitosis
  JOURNAL   Nature 380 (6574), 544-547 (1996)
   PUBMED   8606777
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Bilaud,T., Koering,C.E., Binet-Brasselet,E., Ancelin,K.,
            Pollice,A., Gasser,S.M. and Gilson,E.
  TITLE     The telobox, a Myb-related telomeric DNA binding motif found in
            proteins from yeast, plants and human
  JOURNAL   Nucleic Acids Res 24 (7), 1294-1303 (1996)
   PUBMED   8614633
REFERENCE   9  (residues 1 to 449)
  AUTHORS   Chong,L., van Steensel,B., Broccoli,D., Erdjument-Bromage,H.,
            Hanish,J., Tempst,P. and de Lange,T.
  TITLE     A human telomeric protein
  JOURNAL   Science 270 (5242), 1663-1667 (1995)
   PUBMED   7502076
REFERENCE   10 (residues 1 to 449)
  AUTHORS   Zhong,Z., Shiue,L., Kaplan,S. and de Lange,T.
  TITLE     A mammalian factor that binds telomeric TTAGGG repeats in vitro
  JOURNAL   Mol Cell Biol 12 (11), 4834-4843 (1992)
   PUBMED   1406665
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022893.6.
            
            On Aug 18, 2022 this sequence version replaced XP_005251349.1.
            
            Summary: This gene encodes a telomere specific protein which is a
            component of the telomere nucleoprotein complex. This protein is
            present at telomeres throughout the cell cycle and functions as an
            inhibitor of telomerase, acting in cis to limit the elongation of
            individual chromosome ends. The protein structure contains a
            C-terminal Myb motif, a dimerization domain near its N-terminus and
            an acidic N-terminus. Multiple transcripts of this gene are
            alternatively spliced products. [provided by RefSeq, Aug 2022].
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longest isoform (3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.74651.1,
                                           SRR18074967.1841595.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.11"
     Protein         1..449
                     /product="telomeric repeat-binding factor 1 isoform 3"
                     /note="NIMA-interacting protein 2; telomeric protein
                     Pin2/TRF1; TTAGGG repeat-binding factor 1; telomeric
                     repeat binding factor (NIMA-interacting) 1"
                     /calculated_mol_wt=51687
     Region          76..264
                     /region_name="TRFH"
                     /note="Telomeric Repeat binding Factor or TTAGGG Repeat
                     binding Factor, central (dimerization) domain Homology;
                     TRFH. Telomeres are protein/DNA complexes that make up the
                     physical ends of eukaryotic linear chromosomes and are
                     essential for chromosome stability; cd00280"
                     /db_xref="CDD:238174"
     Site            order(106,109,123,127,131,141..145,153,156..157,160)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238174"
     Region          391..439
                     /region_name="SANT_TRF"
                     /note="Telomere repeat binding factor-like DNA-binding
                     domains of the SANT/myb-like family; cd11660"
                     /db_xref="CDD:212558"
     Site            order(391..393,411,413..414,425,427..429,431..433,
                     435..436)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212558"
     CDS             1..449
                     /gene="TERF1"
                     /gene_synonym="hTRF1-AS; PIN2; t-TRF1; TRBF1; TRF; TRF1"
                     /coded_by="NM_001410928.1:24..1373"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS94314.1"
                     /db_xref="GeneID:7013"
                     /db_xref="HGNC:HGNC:11728"
                     /db_xref="MIM:600951"
ORIGIN      
        1 maedvssaap sprgcadgrd adpteeqmae terndeeqfe cqellecqvq vgapeeeeee
       61 eedaglvaea eavaagwmld flclslcraf rdgrsedfrr trnsaeaiih glssltacql
      121 rtiyicqflt riaagktlda qfenderitp lesalmiwgs iekehdklhe eiqnlikiqa
      181 iavcmengnf keaeevferi fgdpnshmpf kskllmiisq kdtfhsffqh fsynhmmeki
      241 ksyvnyvlse ksstflmkaa akvveskrtr titsqdkpsg ndvemetean ldtrkrshkn
      301 lflsklqhgt qqqdlnkker rvgtpqityi cltkltmnkk egvrkglcfl vllkhyrtkk
      361 kkesrrates ripvsksqpv tpekhrarkr qawlweedkn lrsgvrkyge gnwskillhy
      421 kfnnrtsvml kdrwrtmkkl klissdsed
//
LOCUS       NP_001393522            1164 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 1 [Homo sapiens].
ACCESSION   NP_001393522 XP_006717334
VERSION     NP_001393522.1
DBSOURCE    REFSEQ: accession NM_001406593.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1164)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1164)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1164)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1164)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1164)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1164)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1164)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            On May 18, 2022 this sequence version replaced XP_006717334.1.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3798727.1,
                                           SRR14038191.1796580.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1164
                     /product="hamartin isoform 1"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=129636
     Region          7..719
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          403..787
                     /region_name="Mediates interaction with WDR45B.
                     /evidence=ECO:0000269|PubMed:28561066"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Region          439..571
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <708..>960
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1006..1085
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1131..1164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1164
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406593.1:214..3708"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS6956.1"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt aggkgtplgt patspppapl chsddyvhis lpqatvtppr
      421 keermdsarp clhrqhhlln drgseeppgs kgsvtlsdlp gflgdlasee dsiekdkeea
      481 aisrelseit taeaepvvpr ggfdspfyrd slpgsqrkth saasssqgas vnpeplhssl
      541 dklgpdtpkq aftpidlpcg sadespagdr ecqtsletsi ftpspckipp ptrvgfgsgq
      601 pppydhlfev alpktahhfv irkteellkk akgnteedgv pstspmevld rliqqgadah
      661 skelnklplp sksvdwthfg gsppsdeirt lrdqllllhn qllyerfkrq qhalrnrrll
      721 rkvikaaale ehnaamkdql klqekdiqmw kvslqkeqar ynqlqeqrdt mvtklhsqir
      781 qlqhdreefy nqsqelqtkl edcrnmiael rielkkannk vchtelllsq vsqklsnses
      841 vqqqmeflnr qllvlgevne lyleqlqnkh sdttkevemm kaayrkelek nrshvlqqtq
      901 rldtsqkril eleshlakkd hllleqkkyl edvklqargq lqaaesryea qkritqvfel
      961 eildlygrle kdgllkklee ekaeaaeaae erldccndgc sdsmvghnee asghngetkt
     1021 prpssargss gsrggggsss ssselstpek pphqragpfs srwettmgea sasipttvgs
     1081 lpssksflgm karelfrnks esqcdedgmt sslseslkte lgkdlgveak iplnldgphp
     1141 spptpdsvgq lhimdyneth hehs
//
LOCUS       NP_001400921            1484 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, NMDA 2B isoform a precursor [Homo
            sapiens].
ACCESSION   NP_001400921 XP_011518931
VERSION     NP_001400921.1
DBSOURCE    REFSEQ: accession NM_001413992.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1484)
  AUTHORS   Korinek,M., Candelas Serra,M., Abdel Rahman,F., Dobrovolski,M.,
            Kuchtiak,V., Abramova,V., Fili,K., Tomovic,E., Hrcka Krausova,B.,
            Krusek,J., Cerny,J., Vyklicky,L., Balik,A. and Smejkalova,T.
  TITLE     Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B genes:
            Insights into NMDA Receptor Structure, Function, and
            Pathophysiology
  JOURNAL   Physiol Res 73 (Suppl 1), S413-S434 (2024)
   PUBMED   38836461
  REMARK    GeneRIF: Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B
            genes: Insights into NMDA Receptor Structure, Function, and
            Pathophysiology.
            Review article
REFERENCE   2  (residues 1 to 1484)
  AUTHORS   Raich,I., Lillo,J., Rebassa,J.B., Capo,T., Cordomi,A.,
            Reyes-Resina,I., Pallas,M. and Navarro,G.
  TITLE     Dual Role of NMDAR Containing NR2A and NR2B Subunits in Alzheimer's
            Disease
  JOURNAL   Int J Mol Sci 25 (9), 4757 (2024)
   PUBMED   38731978
  REMARK    GeneRIF: Dual Role of NMDAR Containing NR2A and NR2B Subunits in
            Alzheimer's Disease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1484)
  AUTHORS   Iacobucci,G.J. and Popescu,G.K.
  TITLE     NMDA receptors: linking physiological output to biophysical
            operation
  JOURNAL   Nat Rev Neurosci 18 (4), 236-249 (2017)
   PUBMED   28303017
  REMARK    Review article
REFERENCE   4  (residues 1 to 1484)
  AUTHORS   Hu,C., Chen,W., Myers,S.J., Yuan,H. and Traynelis,S.F.
  TITLE     Human GRIN2B variants in neurodevelopmental disorders
  JOURNAL   J Pharmacol Sci 132 (2), 115-121 (2016)
   PUBMED   27818011
  REMARK    GeneRIF: In this review, mutations in GRIN2B were described as
            distributed throughout the entire gene in patients with
            neuropsychiatric and developmental disorders.
            Review article
            Erratum:[J Pharmacol Sci. 2017 Apr;133(4):280. doi:
            10.1016/j.jphs.2017.04.001. PMID: 28434657]
REFERENCE   5  (residues 1 to 1484)
  AUTHORS   Hess,S.D., Daggett,L.P., Crona,J., Deal,C., Lu,C.C., Urrutia,A.,
            Chavez-Noriega,L., Ellis,S.B., Johnson,E.C. and Velicelebi,G.
  TITLE     Cloning and functional characterization of human heteromeric
            N-methyl-D-aspartate receptors
  JOURNAL   J Pharmacol Exp Ther 278 (2), 808-816 (1996)
   PUBMED   8768735
REFERENCE   6  (residues 1 to 1484)
  AUTHORS   Kornau,H.C., Schenker,L.T., Kennedy,M.B. and Seeburg,P.H.
  TITLE     Domain interaction between NMDA receptor subunits and the
            postsynaptic density protein PSD-95
  JOURNAL   Science 269 (5231), 1737-1740 (1995)
   PUBMED   7569905
REFERENCE   7  (residues 1 to 1484)
  AUTHORS   Magnuson,D.S., Knudsen,B.E., Geiger,J.D., Brownstone,R.M. and
            Nath,A.
  TITLE     Human immunodeficiency virus type 1 tat activates
            non-N-methyl-D-aspartate excitatory amino acid receptors and causes
            neurotoxicity
  JOURNAL   Ann Neurol 37 (3), 373-380 (1995)
   PUBMED   7695237
REFERENCE   8  (residues 1 to 1484)
  AUTHORS   Mandich,P., Schito,A.M., Bellone,E., Antonacci,R., Finelli,P.,
            Rocchi,M. and Ajmar,F.
  TITLE     Mapping of the human NMDAR2B receptor subunit gene (GRIN2B) to
            chromosome 12p12
  JOURNAL   Genomics 22 (1), 216-218 (1994)
   PUBMED   7959773
REFERENCE   9  (residues 1 to 1484)
  AUTHORS   Platzer,K. and Lemke,J.R.
  TITLE     GRIN2B-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29851452
REFERENCE   10 (residues 1 to 1484)
  AUTHORS   Monyer,H., Sprengel,R., Schoepfer,R., Herb,A., Higuchi,M.,
            Lomeli,H., Burnashev,N., Sakmann,B. and Seeburg,P.H.
  TITLE     Heteromeric NMDA receptors: molecular and functional distinction of
            subtypes
  JOURNAL   Science 256 (5060), 1217-1221 (1992)
   PUBMED   1350383
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007916.10, AC007784.7,
            AC007397.21, AC007535.3 and AC007527.6.
            
            On Nov 14, 2022 this sequence version replaced XP_011518931.1.
            
            Summary: This gene encodes a member of the N-methyl-D-aspartate
            (NMDA) receptor family within the ionotropic glutamate receptor
            superfamily. The encoded protein is a subunit of the NMDA receptor
            ion channel which acts as an agonist binding site for glutamate.
            The NMDA receptors mediate a slow calcium-permeable component of
            excitatory synaptic transmission in the central nervous system. The
            NMDA receptors are heterotetramers of seven genetically encoded,
            differentially expressed subunits including NR1 (GRIN1), NR2
            (GRIN2A, GRIN2B, GRIN2C, or GRIN2D) and NR3 (GRIN3A or GRIN3B). The
            early expression of this gene in development suggests a role in
            brain development, circuit formation, synaptic plasticity, and
            cellular migration and differentiation. Naturally occurring
            mutations within this gene are associated with neurodevelopmental
            disorders including autism spectrum disorder, attention deficit
            hyperactivity disorder, epilepsy, and schizophrenia. [provided by
            RefSeq, Aug 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK014585.1, SRR14038196.762666.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1484
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.1"
     Protein         1..1484
                     /product="glutamate receptor ionotropic, NMDA 2B isoform a
                     precursor"
                     /note="glutamate [NMDA] receptor subunit epsilon-2;
                     glutamate receptor subunit epsilon-2; N-methyl-D-aspartate
                     receptor subunit 3; N-methyl D-aspartate receptor subtype
                     2B; GluN2B(alt_5'UTR); glutamate receptor ionotropic, NMDA
                     2B; glutamate receptor, ionotropic, N-methyl D-aspartate
                     2B"
                     /calculated_mol_wt=163566
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2820
     mat_peptide     27..1484
                     /product="Glutamate receptor ionotropic, NMDA 2B.
                     /id=PRO_0000011577"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13224.3)"
                     /calculated_mol_wt=163566
     Region          33..388
                     /region_name="PBP1_iGluR_NMDA_NR2"
                     /note="N-terminal leucine-isoleucine-valine-binding
                     protein (LIVBP)-like domain of the NR2 subunit of NMDA
                     receptor family; cd06378"
                     /db_xref="CDD:380601"
     Site            order(33,77..79,114,135,175,177,192,207..208,311..312)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:380601"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:26912815,
                     ECO:0007744|PDB:5EWJ, ECO:0007744|PDB:5EWL,
                     ECO:0007744|PDB:5EWM; propagated from UniProtKB/Swiss-Prot
                     (Q13224.3)"
     Site            order(75..80,82..83,118..119,175,179,206,208,311..317,
                     321..323,334)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:380601"
     Site            341
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:26912815,
                     ECO:0000269|PubMed:34321660, ECO:0007744|PDB:5EWJ,
                     ECO:0007744|PDB:5EWL, ECO:0007744|PDB:5EWM,
                     ECO:0007744|PDB:7EU8; propagated from UniProtKB/Swiss-Prot
                     (Q13224.3)"
     Site            348
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Region          403..803
                     /region_name="PBP2_iGluR_NMDA_Nr2"
                     /note="The ligand-binding domain of the NR2 subunit of
                     ionotropic NMDA (N-methyl-D-aspartate) glutamate
                     receptors, a member of the type 2 periplasmic binding fold
                     protein superfamily; cd13718"
                     /db_xref="CDD:270436"
     Site            444
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Site            491
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Site            order(512..515,517,519..521,667,689..690,694,732,757..759,
                     762,768,784..787,790)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:270436"
     Site            order(512..514,519,689..691,731..732)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270436"
     Site            542
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:34321660,
                     ECO:0007744|PDB:7EU8; propagated from UniProtKB/Swiss-Prot
                     (Q13224.3)"
     Site            556..576
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13224.3)"
     Region          604..623
                     /region_name="Pore-forming.
                     /evidence=ECO:0000250|UniProtKB:A7XY94"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13224.3)"
     Site            615
                     /site_type="other"
                     /note="Functional determinant of NMDA receptors.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Site            628..647
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13224.3)"
     Site            688
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:34321660,
                     ECO:0007744|PDB:7EU8; propagated from UniProtKB/Swiss-Prot
                     (Q13224.3)"
     Site            820..835
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13224.3)"
     Region          840..1484
                     /region_name="NMDAR2_C"
                     /note="N-methyl D-aspartate receptor 2B3 C-terminus;
                     pfam10565"
                     /db_xref="CDD:463148"
     Site            882
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01097; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q00960; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Site            917
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01097; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Site            920
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01097; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Site            962
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q01097; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Site            1039
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q01097; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Site            1058
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01097; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Site            1061
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01097; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Site            1064
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01097; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Region          1074..1097
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13224.3)"
     Site            1109
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q01097; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Site            1133
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q01097; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Site            1143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01097; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Site            1155
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q01097; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Region          1161..1194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13224.3)"
     Site            1255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01097; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Site            1259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q01097; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Region          1271..1301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13224.3)"
     Region          1292..1304
                     /region_name="Interaction with DAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q01097"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13224.3)"
     Site            1303
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by DAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q01097; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Site            1474
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q01097; propagated from
                     UniProtKB/Swiss-Prot (Q13224.3)"
     Region          1482..1484
                     /region_name="PDZ-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13224.3)"
     CDS             1..1484
                     /gene="GRIN2B"
                     /gene_synonym="DEE27; EIEE27; GluN2B; hNR3; MRD6; NMDAR2B;
                     NR2B; NR3"
                     /coded_by="NM_001413992.1:902..5356"
                     /note="isoform a precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:2904"
                     /db_xref="HGNC:HGNC:4586"
                     /db_xref="MIM:138252"
ORIGIN      
        1 mkpraeccsp kfwlvlavla vsgsrarsqk sppsigiavi lvgtsdevai kdahekddfh
       61 hlsvvprvel vamnetdpks iitricdlms drkiqgvvfa ddtdqeaiaq ildfisaqtl
      121 tpilgihggs smimadkdes smffqfgpsi eqqasvmlni meeydwyifs ivttyfpgyq
      181 dfvnkirsti ensfvgwele evllldmsld dgdskiqnql kklqspiill yctkeeatyi
      241 fevansvglt gygytwivps lvagdtdtvp aefptglisv sydewdyglp arvrdgiaii
      301 ttaasdmlse hsfipepkss cynthekriy qsnmlnryli nvtfegrnls fsedgyqmhp
      361 klviillnke rkwervgkwk dkslqmkyyv wprmcpetee qeddhlsivt leeapfvive
      421 svdplsgtcm rntvpcqkri vtenktdeep gyikkcckgf cidilkkisk svkftydlyl
      481 vtngkhgkki ngtwngmige vvmkraymav gsltineers evvdfsvpfi etgisvmvsr
      541 sngtvspsaf lepfsadvwv mmfvmllivs avavfvfeyf spvgynrcla dgrepggpsf
      601 tigkaiwllw glvfnnsvpv qnpkgttski mvsvwaffav iflasytanl aafmiqeeyv
      661 dqvsglsdkk fqrpndfspp frfgtvpngs ternirnnya emhaymgkfn qrgvddalls
      721 lktgkldafi ydaavlnyma grdegcklvt igsgkvfast gygiaiqkds gwkrqvdlai
      781 lqlfgdgeme elealwltgi chneknevms sqldidnmag vfymlgaama lslitficeh
      841 lfywqfrhcf mgvcsgkpgm vfsisrgiys cihgvaieer qsvmnsptat mnnthsnilr
      901 llrtaknman lsgvngspqs aldfirress vydisehrrs fthsdcksyn nppceenlfs
      961 dyisevertf gnlqlkdsnv yqdhyhhhhr phsigsassi dglydcdnpp fttqsrsisk
     1021 kpldiglpss khsqlsdlyg kfsfksdrys ghddlirsdv sdisthtvty gniegnaakr
     1081 rkqqykdslk krpasaksrr efdeielayr rrpprspdhk ryfrdkeglr dfyldqfrtk
     1141 ensphwehvd ltdiykersd dfkrdsvsgg gpctnrshik hgtgdkhgvv sgvpapwekn
     1201 ltnvewedrs ggnfcrscps klhnysttvt gqnsgrqaci rceackkagn lydisednsl
     1261 qeldqpaapv avtsnasttk ypqsptnska qkknrnklrr qhsydtfvdl qkeeaalapr
     1321 svslkdkgrf mdgspyahmf emsagestfa nnkssvptag hhhhnnpggg ymlskslypd
     1381 rvtqnpfipt fgddqcllhg sksyffrqpt vagaskarpd fralvtnkpv vsalhgavpa
     1441 rfqkdicign qsnpcvpnnk nprafngssn ghvyeklssi esdv
//
LOCUS       NP_001427339             656 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 6 precursor [Homo
            sapiens].
ACCESSION   NP_001427339
VERSION     NP_001427339.1
DBSOURCE    REFSEQ: accession NM_001440410.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 656)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 656)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 656)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 656)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 656)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 656)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3, AP004147.3 and
            AP001929.5.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.219548.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..656
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     6 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=71193
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          28..293
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Region          306..654
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     CDS             1..656
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440410.1:191..2161"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 12"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslrivcq ilpkgvvavl gpssspasss iisnicgeke
       61 vphfkvapee fvkfqfqrft tlnlhpsntd isvavagiln ffncttacli cakaecllnl
      121 ekllrqflis kdtlsvrmld dtrdptpllk eirddktati iihanasmsh tillkaaelg
      181 mvsayytyif tnllssallf davyavvtav qelnrsqeig vkplscgsaq iwqhgtslmn
      241 ylrmvelegl tghiefnskg qrsnyalkil qftrngfrqi gqwhvaegls mdshlyasni
      301 sdtlfnttlv vttilenpyl mlkgnhqeme gndryegfcv dmlkelaeil rfnykirlvg
      361 dgvygvpean gtwtgmvgel iarkadlava gltitaerek vidfskpfmt lgisilyrvh
      421 mgrkpgyfsf ldpfspgvwl fmllaylavs cvlflvarlt pyewysphpc aqgrcnllvn
      481 qyslgnslwf pvggfmqqgs tiapralstr cvsgvwwaft liiissytan laafltvqrm
      541 dvpiesvddl adqtaieygt ihggssmtff qnsryqtyqr mwnymyskqp svfvksteeg
      601 iarvlnsnya fllestmney yrqrncnltq igglldtkgy gigmpvgmre rnslfg
//
LOCUS       NP_001393555             847 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 14 [Homo sapiens].
ACCESSION   NP_001393555
VERSION     NP_001393555.1
DBSOURCE    REFSEQ: accession NM_001406626.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 847)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 847)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 847)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 847)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 847)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 847)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 847)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 847)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.242373.1,
                                           SRR14038196.500396.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..847
                     /product="hamartin isoform 14"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=93769
     Region          <1..402
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <391..>643
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..847
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406626.1:1095..3638"
                     /note="isoform 14 is encoded by transcript variant 40"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mllnmpgqlp qtlsspstrl iteppqatlw spsmvcgmtt pptspgnvpp dlshpyskvf
       61 gttaggkgtp lgtpatsppp aplchsddyv hislpqatvt pprkeermds arpclhrqhh
      121 llndrgseep pgskgsvtls dlpgflgdla seedsiekdk eeaaisrels eittaeaepv
      181 vprggfdspf yrdslpgsqr kthsaasssq gasvnpeplh ssldklgpdt pkqaftpidl
      241 pcgsadespa gdrecqtsle tsiftpspck ippptrvgfg sgqpppydhl fevalpktah
      301 hfvirkteel lkkakgntee dgvpstspme vldrliqqga dahskelnkl plpsksvdwt
      361 hfggsppsde irtlrdqlll lhnqllyerf krqqhalrnr rllrkvikaa aleehnaamk
      421 dqlklqekdi qmwkvslqke qarynqlqeq rdtmvtklhs qirqlqhdre efynqsqelq
      481 tkledcrnmi aelrielkka nnkvchtell lsqvsqklsn sesvqqqmef lnrqllvlge
      541 vnelyleqlq nkhsdttkev emmkaayrke leknrshvlq qtqrldtsqk rileleshla
      601 kkdhllleqk kyledvklqa rgqlqaaesr yeaqkritqv feleildlyg rlekdgllkk
      661 leeekaeaae aaeerldccn dgcsdsmvgh neeasghnge tktprpssar gssgsrgggg
      721 sssssselst pekpphqrag pfssrwettm geasasiptt vgslpssksf lgmkarelfr
      781 nksesqcded gmtsslsesl ktelgkdlgv eakiplnldg phpspptpds vgqlhimdyn
      841 ethhehs
//
LOCUS       NP_001427234             407 aa            linear   PRI 21-NOV-2025
DEFINITION  G1/S-specific cyclin-E1 isoform 6 [Homo sapiens].
ACCESSION   NP_001427234 XP_011525742 XP_054178472
VERSION     NP_001427234.1
DBSOURCE    REFSEQ: accession NM_001440305.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Lee,S.J., Jeon,S.H., Cho,S., Kim,C.M., Yoo,J.K., Oh,S.H., Kim,J.H.,
            Yang,Y.D. and Kim,J.K.
  TITLE     hsa-miR-CHA2, a novel microRNA, exhibits anticancer effects by
            suppressing cyclin E1 in human non-small cell lung cancer cells
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (6), 167250 (2024)
   PUBMED   38763409
  REMARK    GeneRIF: hsa-miR-CHA2, a novel microRNA, exhibits anticancer
            effects by suppressing cyclin E1 in human non-small cell lung
            cancer cells.
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Rustgi,N., Wu,S., Samec,T., Walker,P., Xiu,J., Lou,E., Goel,S.,
            Saeed,A. and Moy,R.H.
  TITLE     Molecular Landscape and Clinical Implication of CCNE1-amplified
            Esophagogastric Cancer
  JOURNAL   Cancer Res Commun 4 (6), 1399-1409 (2024)
   PUBMED   38717153
  REMARK    GeneRIF: Molecular Landscape and Clinical Implication of
            CCNE1-amplified Esophagogastric Cancer.
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Audrey,A., Kok,Y.P., Yu,S., de Haan,L., van de Kooij,B., van den
            Tempel,N., Chen,M., de Boer,H.R., van der Vegt,B. and van
            Vugt,M.A.T.M.
  TITLE     RAD52-dependent mitotic DNA synthesis is required for genome
            stability in Cyclin E1-overexpressing cells
  JOURNAL   Cell Rep 43 (4), 114116 (2024)
   PUBMED   38625790
  REMARK    GeneRIF: RAD52-dependent mitotic DNA synthesis is required for
            genome stability in Cyclin E1-overexpressing cells.
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Mumberg,D., Wick,M., Burger,C., Haas,K., Funk,M. and Muller,R.
  TITLE     Cyclin ET, a new splice variant of human cyclin E with a unique
            expression pattern during cell cycle progression and
            differentiation
  JOURNAL   Nucleic Acids Res 25 (11), 2098-2105 (1997)
   PUBMED   9153308
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Sewing,A., Ronicke,V., Burger,C., Funk,M. and Muller,R.
  TITLE     Alternative splicing of human cyclin E
  JOURNAL   J Cell Sci 107 (Pt 2), 581-588 (1994)
   PUBMED   8207080
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Koff,A., Giordano,A., Desai,D., Yamashita,K., Harper,J.W.,
            Elledge,S., Nishimoto,T., Morgan,D.O., Franza,B.R. and Roberts,J.M.
  TITLE     Formation and activation of a cyclin E-cdk2 complex during the G1
            phase of the human cell cycle
  JOURNAL   Science 257 (5077), 1689-1694 (1992)
   PUBMED   1388288
REFERENCE   8  (residues 1 to 407)
  AUTHORS   Hinds,P.W., Mittnacht,S., Dulic,V., Arnold,A., Reed,S.I. and
            Weinberg,R.A.
  TITLE     Regulation of retinoblastoma protein functions by ectopic
            expression of human cyclins
  JOURNAL   Cell 70 (6), 993-1006 (1992)
   PUBMED   1388095
REFERENCE   9  (residues 1 to 407)
  AUTHORS   Koff,A., Cross,F., Fisher,A., Schumacher,J., Leguellec,K.,
            Philippe,M. and Roberts,J.M.
  TITLE     Human cyclin E, a new cyclin that interacts with two members of the
            CDC2 gene family
  JOURNAL   Cell 66 (6), 1217-1228 (1991)
   PUBMED   1833068
REFERENCE   10 (residues 1 to 407)
  AUTHORS   Lew,D.J., Dulic,V. and Reed,S.I.
  TITLE     Isolation of three novel human cyclins by rescue of G1 cyclin (Cln)
            function in yeast
  JOURNAL   Cell 66 (6), 1197-1206 (1991)
   PUBMED   1833066
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008798.10.
            
            On or before May 19, 2025 this sequence version replaced
            XP_011525742.1, XP_054178472.1.
            
            Summary: The protein encoded by this gene belongs to the highly
            conserved cyclin family, whose members are characterized by a
            dramatic periodicity in protein abundance through the cell cycle.
            Cyclins function as regulators of CDK kinases. Different cyclins
            exhibit distinct expression and degradation patterns which
            contribute to the temporal coordination of each mitotic event. This
            cyclin forms a complex with and functions as a regulatory subunit
            of CDK2, whose activity is required for cell cycle G1/S transition.
            This protein accumulates at the G1-S phase boundary and is degraded
            as cells progress through S phase. Overexpression of this gene has
            been observed in many tumors, which results in chromosome
            instability, and thus may contribute to tumorigenesis. This protein
            was found to associate with, and be involved in, the
            phosphorylation of NPAT protein (nuclear protein mapped to the ATM
            locus), which participates in cell-cycle regulated histone gene
            expression and plays a critical role in promoting cell-cycle
            progression in the absence of pRB. [provided by RefSeq, Apr 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.100590.1,
                                           SRR14038194.3630116.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..407
                     /product="G1/S-specific cyclin-E1 isoform 6"
                     /note="G1/S-specific cyclin-E1"
                     /calculated_mol_wt=46558
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P24864.2)"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14536078,
                     ECO:0000269|PubMed:17434132; propagated from
                     UniProtKB/Swiss-Prot (P24864.2)"
     Region          100..236
                     /region_name="CYCLIN_CCNE1_rpt1"
                     /note="first cyclin box found in G1/S-specific cyclin-E1
                     (CCNE1); cd20579"
                     /db_xref="CDD:410282"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P24864.2)"
     Site            order(106..107,109,112..113,116..117,120,124,159,194,
                     198..202,206..207,224,227..228,231..232,235..236)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410282"
     Region          240..353
                     /region_name="CYCLIN_CCNE1_rpt2"
                     /note="second cyclin box found in G1/S-specific cyclin-E1
                     (CCNE1); cd20581"
                     /db_xref="CDD:410284"
     Site            order(241,248..249,252,261..265,267,352..353)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410284"
     Region          375..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P24864.2)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14536078,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P24864.2)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by GSK3.
                     /evidence=ECO:0000269|PubMed:14536078,
                     ECO:0000269|PubMed:17434132, ECO:0000269|PubMed:8861947,
                     ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P24864.2)"
     Site            396
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK2.
                     /evidence=ECO:0000269|PubMed:14536078,
                     ECO:0000269|PubMed:17434132; propagated from
                     UniProtKB/Swiss-Prot (P24864.2)"
     CDS             1..407
                     /gene="CCNE1"
                     /gene_synonym="CCNE; pCCNE1"
                     /coded_by="NM_001440305.1:187..1410"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:898"
                     /db_xref="HGNC:HGNC:1589"
                     /db_xref="MIM:123837"
ORIGIN      
        1 mprerrerda kerdtmkedg gaefsarsrk rkanvtvdpd eemakidrta rdqcgsqpwd
       61 nnavcadpcs liptpdkedd drvypnstck priiapsrgs plpvlswanr eevwkimlnk
      121 ektylrdqhf leqhpllqpk mrailldwlm evcevyklhr etfylaqdff drymatqenv
      181 vktllqligi sslfiaakle eiyppklhqf ayvtdgacsg deiltmelmi mkalkwrlsp
      241 ltivswlnvy mqvaylndlh evllpqypqq ifiqiaelld lcvldvdcle fpygilaasa
      301 lyhfssselm qkvsgyqwcd iencvkwmvp famviretgs sklkhfrgva dedahniqth
      361 rdsldlldka rakkamlseq nrasplpsgl ltppqsgkkq ssgpema
//
LOCUS       NP_001424535             407 aa            linear   PRI 21-NOV-2025
DEFINITION  sorting nexin-27 isoform 8 [Homo sapiens].
ACCESSION   NP_001424535 XP_016857906 XP_054194893
VERSION     NP_001424535.1
DBSOURCE    REFSEQ: accession NM_001437606.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Broniarczyk,J., Trejo-Cerro,O., Massimi,P., Kavcic,N., Myers,M.P.
            and Banks,L.
  TITLE     HPV-18 E6 enhances the interaction between EMILIN2 and SNX27 to
            promote WNT signaling
  JOURNAL   J Virol 98 (7), e0073524 (2024)
   PUBMED   38874360
  REMARK    GeneRIF: HPV-18 E6 enhances the interaction between EMILIN2 and
            SNX27 to promote WNT signaling.
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Xi,Y., Gai,Y., Zhang,W., Wang,M., Liu,Q. and Bi,Y.
  TITLE     Circular RNA SNX27 Facilitates Gastric Cancer Progression By
            Sponging miR-638
  JOURNAL   Turk J Gastroenterol 35 (4), 280-287 (2024)
   PUBMED   39128090
  REMARK    GeneRIF: Circular RNA SNX27 Facilitates Gastric Cancer Progression
            By Sponging miR-638.
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Broniarczyk,J.K., Massimi,P., Trejo-Cerro,O., Myers,M.P. and
            Banks,L.
  TITLE     HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in a
            PBM-Dependent Manner and Promotes Increased Cell Proliferation
  JOURNAL   J Virol 96 (22), e0136522 (2022)
   PUBMED   36326272
  REMARK    GeneRIF: HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in
            a PBM-Dependent Manner and Promotes Increased Cell Proliferation.
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 407)
  AUTHORS   MacNeil,A.J., Mansour,M. and Pohajdak,B.
  TITLE     Sorting nexin 27 interacts with the Cytohesin associated
            scaffolding protein (CASP) in lymphocytes
  JOURNAL   Biochem Biophys Res Commun 359 (4), 848-853 (2007)
   PUBMED   17577583
  REMARK    GeneRIF: These results suggest that endosomal SNX27 may recruit
            CASP to orchestrate intracellular trafficking and/or signaling
            complexes.
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Rincon,E., Santos,T., Avila-Flores,A., Albar,J.P., Lalioti,V.,
            Lei,C., Hong,W. and Merida,I.
  TITLE     Proteomics identification of sorting nexin 27 as a diacylglycerol
            kinase zeta-associated protein: new diacylglycerol kinase roles in
            endocytic recycling
  JOURNAL   Mol Cell Proteomics 6 (6), 1073-1087 (2007)
   PUBMED   17351151
  REMARK    GeneRIF: These data support a previously unreported role for
            diacylglycerol kinase zeta in the modulation of membrane
            trafficking, which may also help to define SNX27 function.
REFERENCE   8  (residues 1 to 407)
  AUTHORS   Joubert,L., Hanson,B., Barthet,G., Sebben,M., Claeysen,S., Hong,W.,
            Marin,P., Dumuis,A. and Bockaert,J.
  TITLE     New sorting nexin (SNX27) and NHERF specifically interact with the
            5-HT4a receptor splice variant: roles in receptor targeting
  JOURNAL   J Cell Sci 117 (Pt 22), 5367-5379 (2004)
   PUBMED   15466885
  REMARK    GeneRIF: SNX27a redirects part of the 5-HT4(a)R to early endosomes.
REFERENCE   9  (residues 1 to 407)
  AUTHORS   Worby,C.A. and Dixon,J.E.
  TITLE     Sorting out the cellular functions of sorting nexins
  JOURNAL   Nat Rev Mol Cell Biol 3 (12), 919-931 (2002)
   PUBMED   12461558
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol. 2003 Feb;4(2):156.]
REFERENCE   10 (residues 1 to 407)
  AUTHORS   Teasdale,R.D., Loci,D., Houghton,F., Karlsson,L. and Gleeson,P.A.
  TITLE     A large family of endosome-localized proteins related to sorting
            nexin 1
  JOURNAL   Biochem J 358 (Pt 1), 7-16 (2001)
   PUBMED   11485546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL391335.32 and AL589765.19.
            
            On or before Apr 7, 2025 this sequence version replaced
            XP_016857906.1, XP_054194893.1.
            
            Summary: This gene encodes a member of the sorting nexin family, a
            diverse group of cytoplasmic and membrane-associated proteins
            involved in endocytosis of plasma membrane receptors and protein
            trafficking through these compartments. All members of this protein
            family contain a phosphoinositide binding domain (PX domain). A
            highly similar protein in mouse is responsible for the specific
            recruitment of an isoform of serotonin 5-hydroxytryptamine 4
            receptor into early endosomes, suggesting the analogous role for
            the human protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1163616.1,
                                           SRR14038193.2407983.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..407
                     /product="sorting nexin-27 isoform 8"
                     /note="methamphetamine-responsive transcript 1; sorting
                     nexin family member 27"
                     /calculated_mol_wt=46545
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L92.2)"
     Region          42..>61
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96L92.2)"
     Region          <61..144
                     /region_name="PX_domain"
                     /note="The Phox Homology domain, a phosphoinositide
                     binding module; cl02563"
                     /db_xref="CDD:470617"
     Site            order(75..77,101..102,114)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132796"
     Region          152..244
                     /region_name="FERM_F1_SNX27"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F1 sub-domain, found in sorting nexin protein 27
                     (SNX27); cd01777"
                     /db_xref="CDD:340475"
     Region          304..405
                     /region_name="FERM-like_C_SNX27"
                     /note="Atypical FERM-like domain C-lobe of Sorting nexin
                     27; cd13338"
                     /db_xref="CDD:270146"
     CDS             1..407
                     /gene="SNX27"
                     /gene_synonym="MRT1; MY014"
                     /coded_by="NM_001437606.1:153..1376"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:81609"
                     /db_xref="HGNC:HGNC:20073"
                     /db_xref="MIM:611541"
ORIGIN      
        1 madedgegih psaphrnggg gggggsglhc agnggggggg prvvrivkse sgygfnvrgq
       61 vynvymagrq lcskryrefa ilhqnlkref anftfprlpg kwpfslseqq ldarrrglee
      121 ylekvcsirv igesdimqef lsesdenyng vsdvelrval pdgttvtvrv kknsttdqvy
      181 qaiaakvgmd sttvnyfalf evishsfvrk lapnefphkl yiqnytsavp gtcltirkwl
      241 ftteeeilln dndlavtyff hqavddvkkg yikaeeksyq lqklyeqrkm vmylnmlrtc
      301 egyneiifph cacdsrrkgh vitaisithf klhacteegq lenqviafew demqrwdtde
      361 egmafcfeya rgekkprwvk iftpyfnymh ecfervfcel kwrkeey
//
LOCUS       NP_001401392             237 aa            linear   PRI 21-NOV-2025
DEFINITION  bax inhibitor 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001401392 XP_024304940
VERSION     NP_001401392.1
DBSOURCE    REFSEQ: accession NM_001414463.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Zhang,X., Chen,Q., He,Y., Shi,Q., Yin,C., Xie,Y., Yu,H., Bao,Y.,
            Wang,X., Tang,C. and Dong,Z.
  TITLE     STRIP2 motivates non-small cell lung cancer progression by
            modulating the TMBIM6 stability through IGF2BP3 dependent
  JOURNAL   J Exp Clin Cancer Res 42 (1), 19 (2023)
   PUBMED   36639675
  REMARK    GeneRIF: STRIP2 motivates non-small cell lung cancer progression by
            modulating the TMBIM6 stability through IGF2BP3 dependent.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Liao,Y., Qiu,Z. and Bai,L.
  TITLE     miR-302d-3p regulates the viability, migration and apoptosis of
            breast cancer cells through regulating the TMBIM6-mediated ERK
            signaling pathway
  JOURNAL   Mol Med Rep 24 (6) (2021)
   PUBMED   34651659
  REMARK    GeneRIF: miR302d3p regulates the viability, migration and apoptosis
            of breast cancer cells through regulating the TMBIM6mediated ERK
            signaling pathway.
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Bhattarai,K.R., Kim,H.K., Chaudhary,M., Ur Rashid,M.M., Kim,J.,
            Kim,H.R. and Chae,H.J.
  TITLE     TMBIM6 regulates redox-associated posttranslational modifications
            of IRE1alpha and ER stress response failure in aging mice and
            humans
  JOURNAL   Redox Biol 47, 102128 (2021)
   PUBMED   34562874
  REMARK    GeneRIF: TMBIM6 regulates redox-associated posttranslational
            modifications of IRE1alpha and ER stress response failure in aging
            mice and humans.
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 237)
  AUTHORS   Grzmil,M., Thelen,P., Hemmerlein,B., Schweyer,S., Voigt,S., Mury,D.
            and Burfeind,P.
  TITLE     Bax inhibitor-1 is overexpressed in prostate cancer and its
            specific down-regulation by RNA interference leads to cell death in
            human prostate carcinoma cells
  JOURNAL   Am J Pathol 163 (2), 543-552 (2003)
   PUBMED   12875974
  REMARK    GeneRIF: Results indicate that the human Bax inhibitor-1 gene may
            serve as a prostate cancer expression marker based on its
            overexpression in prostate carcinoma and prostate cancer cell
            lines.
REFERENCE   7  (residues 1 to 237)
  AUTHORS   Jean,J.C., Oakes,S.M. and Joyce-Brady,M.
  TITLE     The Bax inhibitor-1 gene is differentially regulated in adult
            testis and developing lung by two alternative TATA-less promoters
  JOURNAL   Genomics 57 (2), 201-208 (1999)
   PUBMED   10198159
REFERENCE   8  (residues 1 to 237)
  AUTHORS   Cowling,R.T. and Birnboim,H.C.
  TITLE     Preliminary characterization of the protein encoded by human
            testis-enhanced gene transcript (TEGT)
  JOURNAL   Mol Membr Biol 15 (4), 177-187 (1998)
   PUBMED   10087504
REFERENCE   9  (residues 1 to 237)
  AUTHORS   Xu,Q. and Reed,J.C.
  TITLE     Bax inhibitor-1, a mammalian apoptosis suppressor identified by
            functional screening in yeast
  JOURNAL   Mol Cell 1 (3), 337-346 (1998)
   PUBMED   9660918
REFERENCE   10 (residues 1 to 237)
  AUTHORS   Walter,L., Marynen,P., Szpirer,J., Levan,G. and Gunther,E.
  TITLE     Identification of a novel conserved human gene, TEGT
  JOURNAL   Genomics 28 (2), 301-304 (1995)
   PUBMED   8530040
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC084037.35 and AC131157.4.
            
            On Feb 21, 2023 this sequence version replaced XP_024304940.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2540938.1,
                                           SRR14038193.1442415.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..237
                     /product="bax inhibitor 1 isoform 1"
                     /note="BAX inhibitor 1; testis-enhanced gene transcript
                     protein; transmembrane BAX inhibitor motif-containing
                     protein 6; testis enhanced gene transcript"
                     /calculated_mol_wt=26407
     Region          16..228
                     /region_name="BI-1"
                     /note="BAX inhibitor (BI)-1; cd10430"
                     /db_xref="CDD:198412"
     Site            30..50
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            53..73
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            87..107
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            140..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            167..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     CDS             1..237
                     /gene="TMBIM6"
                     /gene_synonym="BAXI1; BI-1; TEGT"
                     /coded_by="NM_001414463.1:415..1128"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:7009"
                     /db_xref="HGNC:HGNC:11723"
                     /db_xref="MIM:600748"
ORIGIN      
        1 mnifdrkinf dallkfshit pstqqhlkkv yasfalcmfv aaagayvhmv thfiqaglls
       61 algslilmiw lmatphshet eqkrlgllag fafltgvglg palefciavn psilptafmg
      121 tamiftcftl salyarrrsy lflggilmsa lsllllsslg nvffgsiwlf qanlyvglvv
      181 mcgfvlfdtq liiekaehgd qdyiwhcidl fldfitvfrk lmmilamnek dkkkekk
//
LOCUS       NP_001389616            1328 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 7 [Homo sapiens].
ACCESSION   NP_001389616 XP_006720203
VERSION     NP_001389616.1
DBSOURCE    REFSEQ: accession NM_001402687.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1328)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1328)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1328)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1328)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1328)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1328)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1328)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1328)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1328)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1328)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            On Apr 22, 2022 this sequence version replaced XP_006720203.1.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1526409.1,
                                           SRR14038194.2375973.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1328
                     /product="kinectin isoform 7"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=152768
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          316..>532
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          448..1268
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1328
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402687.1:179..4165"
                     /note="isoform 7 is encoded by transcript variant 12"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqdlkqeika
      841 lkeeignvql ekaqqlsits kvqelqnllk gkeeqmntmk avleekekdl antgkwlqdl
      901 qeeneslkah vqevaqhnlk eassasqfee leivlkeken elkrleamlk eresdlsskt
      961 qllqdvqden klfksqieql kqqnyqqass fppheellkv iserekeisg lwneldslkd
     1021 avehqrkknn erqqqveave leakevlkkl fpkvsvpsnl sygewlhgfe kkakecmagt
     1081 sgseevkvle hklkeademh tllqleceky ksvlaetegi lqklqrsveq eenkwkvkvd
     1141 eshktikqmq ssftsseqel erlrsenkdi enlrrerehl emelekaeme rstyvtevre
     1201 lkdlltelqk klddsyseav rqneelnllk aqlnetltkl rteqnerqkv agdlhkaqqs
     1261 leliqskivk aagdttvien sdvspetess eketmsvsln qtvtqlqqll qavnqqltke
     1321 kehyqvle
//
LOCUS       NP_001411255             225 aa            linear   PRI 21-NOV-2025
DEFINITION  protein cholesin isoform e [Homo sapiens].
ACCESSION   NP_001411255 XP_011513885
VERSION     NP_001411255.1
DBSOURCE    REFSEQ: accession NM_001424326.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Ryk,A., Marcinkiewicz,A., Chrzanowski,J., Michalak,A.M., Drozdz,I.,
            Burzynski,J., Krejca,M. and Fendler,W.
  TITLE     Cholesin receptor signalling is active in cardiovascular
            system-associated adipose tissue and correlates with SGLT2i
            treatment in patients with diabetes
  JOURNAL   Cardiovasc Diabetol 23 (1), 211 (2024)
   PUBMED   38902687
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Hu,X., Chen,F., Jia,L., Long,A., Peng,Y., Li,X., Huang,J., Wei,X.,
            Fang,X., Gao,Z., Zhang,M., Liu,X., Chen,Y.G., Wang,Y., Zhang,H. and
            Wang,Y.
  TITLE     A gut-derived hormone regulates cholesterol metabolism
  JOURNAL   Cell 187 (7), 1685-1700 (2024)
   PUBMED   38503280
  REMARK    GeneRIF: A gut-derived hormone regulates cholesterol metabolism.
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 225)
  AUTHORS   Willer,C.J., Schmidt,E.M., Sengupta,S., Peloso,G.M., Gustafsson,S.,
            Kanoni,S., Ganna,A., Chen,J., Buchkovich,M.L., Mora,S.,
            Beckmann,J.S., Bragg-Gresham,J.L., Chang,H.Y., Demirkan,A., Den
            Hertog,H.M., Do,R., Donnelly,L.A., Ehret,G.B., Esko,T.,
            Feitosa,M.F., Ferreira,T., Fischer,K., Fontanillas,P., Fraser,R.M.,
            Freitag,D.F., Gurdasani,D., Heikkila,K., Hypponen,E., Isaacs,A.,
            Jackson,A.U., Johansson,A., Johnson,T., Kaakinen,M., Kettunen,J.,
            Kleber,M.E., Li,X., Luan,J., Lyytikainen,L.P., Magnusson,P.K.E.,
            Mangino,M., Mihailov,E., Montasser,M.E., Muller-Nurasyid,M.,
            Nolte,I.M., O'Connell,J.R., Palmer,C.D., Perola,M., Petersen,A.K.,
            Sanna,S., Saxena,R., Service,S.K., Shah,S., Shungin,D., Sidore,C.,
            Song,C., Strawbridge,R.J., Surakka,I., Tanaka,T., Teslovich,T.M.,
            Thorleifsson,G., Van den Herik,E.G., Voight,B.F., Volcik,K.A.,
            Waite,L.L., Wong,A., Wu,Y., Zhang,W., Absher,D., Asiki,G.,
            Barroso,I., Been,L.F., Bolton,J.L., Bonnycastle,L.L., Brambilla,P.,
            Burnett,M.S., Cesana,G., Dimitriou,M., Doney,A.S.F., Doring,A.,
            Elliott,P., Epstein,S.E., Ingi Eyjolfsson,G., Gigante,B.,
            Goodarzi,M.O., Grallert,H., Gravito,M.L., Groves,C.J., Hallmans,G.,
            Hartikainen,A.L., Hayward,C., Hernandez,D., Hicks,A.A., Holm,H.,
            Hung,Y.J., Illig,T., Jones,M.R., Kaleebu,P., Kastelein,J.J.P.,
            Khaw,K.T., Kim,E., Klopp,N., Komulainen,P., Kumari,M.,
            Langenberg,C., Lehtimaki,T., Lin,S.Y., Lindstrom,J., Loos,R.J.F.,
            Mach,F., McArdle,W.L., Meisinger,C., Mitchell,B.D., Muller,G.,
            Nagaraja,R., Narisu,N., Nieminen,T.V.M., Nsubuga,R.N., Olafsson,I.,
            Ong,K.K., Palotie,A., Papamarkou,T., Pomilla,C., Pouta,A.,
            Rader,D.J., Reilly,M.P., Ridker,P.M., Rivadeneira,F., Rudan,I.,
            Ruokonen,A., Samani,N., Scharnagl,H., Seeley,J., Silander,K.,
            Stancakova,A., Stirrups,K., Swift,A.J., Tiret,L.,
            Uitterlinden,A.G., van Pelt,L.J., Vedantam,S., Wainwright,N.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilsgaard,T., Wilson,J.F.,
            Young,E.H., Zhao,J.H., Adair,L.S., Arveiler,D., Assimes,T.L.,
            Bandinelli,S., Bennett,F., Bochud,M., Boehm,B.O., Boomsma,D.I.,
            Borecki,I.B., Bornstein,S.R., Bovet,P., Burnier,M., Campbell,H.,
            Chakravarti,A., Chambers,J.C., Chen,Y.I., Collins,F.S.,
            Cooper,R.S., Danesh,J., Dedoussis,G., de Faire,U., Feranil,A.B.,
            Ferrieres,J., Ferrucci,L., Freimer,N.B., Gieger,C., Groop,L.C.,
            Gudnason,V., Gyllensten,U., Hamsten,A., Harris,T.B., Hingorani,A.,
            Hirschhorn,J.N., Hofman,A., Hovingh,G.K., Hsiung,C.A.,
            Humphries,S.E., Hunt,S.C., Hveem,K., Iribarren,C., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kaprio,J., Kesaniemi,A., Kivimaki,M.,
            Kooner,J.S., Koudstaal,P.J., Krauss,R.M., Kuh,D., Kuusisto,J.,
            Kyvik,K.O., Laakso,M., Lakka,T.A., Lind,L., Lindgren,C.M.,
            Martin,N.G., Marz,W., McCarthy,M.I., McKenzie,C.A., Meneton,P.,
            Metspalu,A., Moilanen,L., Morris,A.D., Munroe,P.B., Njolstad,I.,
            Pedersen,N.L., Power,C., Pramstaller,P.P., Price,J.F., Psaty,B.M.,
            Quertermous,T., Rauramaa,R., Saleheen,D., Salomaa,V.,
            Sanghera,D.K., Saramies,J., Schwarz,P.E.H., Sheu,W.H.,
            Shuldiner,A.R., Siegbahn,A., Spector,T.D., Stefansson,K.,
            Strachan,D.P., Tayo,B.O., Tremoli,E., Tuomilehto,J., Uusitupa,M.,
            van Duijn,C.M., Vollenweider,P., Wallentin,L., Wareham,N.J.,
            Whitfield,J.B., Wolffenbuttel,B.H.R., Ordovas,J.M., Boerwinkle,E.,
            Palmer,C.N.A., Thorsteinsdottir,U., Chasman,D.I., Rotter,J.I.,
            Franks,P.W., Ripatti,S., Cupples,L.A., Sandhu,M.S., Rich,S.S.,
            Boehnke,M., Deloukas,P., Kathiresan,S., Mohlke,K.L., Ingelsson,E.
            and Abecasis,G.R.
  CONSRTM   Global Lipids Genetics Consortium
  TITLE     Discovery and refinement of loci associated with lipid levels
  JOURNAL   Nat Genet 45 (11), 1274-1283 (2013)
   PUBMED   24097068
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Yashin,A.I., Wu,D., Arbeev,K.G. and Ukraintseva,S.V.
  TITLE     Joint influence of small-effect genetic variants on human longevity
  JOURNAL   Aging (Albany NY) 2 (9), 612-620 (2010)
   PUBMED   20834067
REFERENCE   9  (residues 1 to 225)
  AUTHORS   Satoh,J., Obayashi,S., Misawa,T., Sumiyoshi,K., Oosumi,K. and
            Tabunoki,H.
  TITLE     Protein microarray analysis identifies human cellular prion protein
            interactors
  JOURNAL   Neuropathol Appl Neurobiol 35 (1), 16-35 (2009)
   PUBMED   18482256
REFERENCE   10 (residues 1 to 225)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091729.4 and AC073957.7.
            
            On Sep 22, 2023 this sequence version replaced XP_011513885.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3104662.1,
                                           SRR14038193.3696447.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..225
                     /product="protein cholesin isoform e"
                     /note="uncharacterized protein C7orf50; protein cholesin"
                     /calculated_mol_wt=25056
     Region          1..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Region          104..165
                     /region_name="WKF"
                     /note="WKF domain; pfam10180"
                     /db_xref="CDD:462982"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     CDS             1..225
                     /gene="CHLSN"
                     /gene_synonym="C7orf50; YCR016W"
                     /coded_by="NM_001424326.1:51..728"
                     /note="isoform e is encoded by transcript variant 16"
                     /db_xref="GeneID:84310"
                     /db_xref="HGNC:HGNC:22421"
                     /db_xref="MIM:621174"
ORIGIN      
        1 makqkrkvpe vtekknkklk kasaegpllg peaapsgega gskgeavlrp gldaepelsp
       61 eeqrvlerkl kkerkkeerq rlreaglvaq hpparrsgae laldylcrwa qkhknwrfqk
      121 trqtwlllhm ydsdkvpdeh fstllayleg lqgrareltv qkaealmrel deegsdpplp
      181 graqrirqdt cavdpaamlw gspaarrgah vegnpgprnr gqast
//
LOCUS       NP_001427448             248 aa            linear   PRI 21-NOV-2025
DEFINITION  beta-sarcoglycan isoform 2 [Homo sapiens].
ACCESSION   NP_001427448 XP_047272030 XP_054206689
VERSION     NP_001427448.1
DBSOURCE    REFSEQ: accession NM_001440519.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Sanga,S., Chakraborty,S., Bardhan,M., Polavarapu,K., Kumar,V.P.,
            Bhattacharya,C., Nashi,S., Vengalil,S., Geetha,T.S., Ramprasad,V.,
            Nalini,A., Basu,A. and Acharya,M.
  TITLE     Identification of a shared, common haplotype segregating with an
            SGCB c.544 T > G mutation in Indian patients affected with
            sarcoglycanopathy
  JOURNAL   Sci Rep 13 (1), 15095 (2023)
   PUBMED   37699968
  REMARK    GeneRIF: Identification of a shared, common haplotype segregating
            with an SGCB c.544 T > G mutation in Indian patients affected with
            sarcoglycanopathy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Li,C., Wilborn,J., Pittman,S., Daw,J., Alonso-Perez,J.,
            Diaz-Manera,J., Weihl,C.C. and Haller,G.
  TITLE     Comprehensive functional characterization of SGCB coding variants
            predicts pathogenicity in limb-girdle muscular dystrophy type R4/2E
  JOURNAL   J Clin Invest 133 (12), e168156 (2023)
   PUBMED   37317968
  REMARK    GeneRIF: Comprehensive functional characterization of SGCB coding
            variants predicts pathogenicity in limb-girdle muscular dystrophy
            type R4/2E.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Bardhan,M., Anjanappa,R.M., Polavarapu,K., Preethish-Kumar,V.,
            Vengalil,S., Nashi,S., Sanga,S., Padmanabh,H., Valasani,R.K.,
            Nishadham,V., Keerthipriya,M., Geetha,T.S., Ramprasad,V.,
            Arunachal,G., Thomas,P.T., Acharya,M. and Nalini,A.
  TITLE     Clinical, genetic profile and disease progression of
            sarcoglycanopathies in a large cohort from India: high prevalence
            of SGCB c.544A > C
  JOURNAL   Neurogenetics 23 (3), 187-202 (2022)
   PUBMED   35416532
  REMARK    GeneRIF: Clinical, genetic profile and disease progression of
            sarcoglycanopathies in a large cohort from India: high prevalence
            of SGCB c.544A > C.
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Alavi,A., Esmaeili,S., Nilipour,Y., Nafissi,S., Tonekaboni,S.H.,
            Zamani,G., Ashrafi,M.R., Kahrizi,K., Najmabadi,H. and Jazayeri,F.
  TITLE     LGMD2E is the most common type of sarcoglycanopathies in the
            Iranian population
  JOURNAL   J Neurogenet 31 (3), 161-169 (2017)
   PUBMED   28687063
  REMARK    GeneRIF: This study demonstrated that LGMD2E is the most common
            type of sarcoglycanopathies in the Iranian population.
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Bonnemann,C.G., Passos-Bueno,M.R., McNally,E.M., Vainzof,M., de Sa
            Moreira,E., Marie,S.K., Pavanello,R.C., Noguchi,S., Ozawa,E.,
            Zatz,M. and Kunkel,L.M.
  TITLE     Genomic screening for beta-sarcoglycan gene mutations: missense
            mutations may cause severe limb-girdle muscular dystrophy type 2E
            (LGMD 2E)
  JOURNAL   Hum Mol Genet 5 (12), 1953-1961 (1996)
   PUBMED   8968749
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Bonnemann,C.G., Modi,R., Noguchi,S., Mizuno,Y., Yoshida,M.,
            Gussoni,E., McNally,E.M., Duggan,D.J., Angelini,C. and Hoffman,E.P.
  TITLE     Beta-sarcoglycan (A3b) mutations cause autosomal recessive muscular
            dystrophy with loss of the sarcoglycan complex
  JOURNAL   Nat Genet 11 (3), 266-273 (1995)
   PUBMED   7581449
  REMARK    Erratum:[Nat Genet 1996 Jan;12(1):110]
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Lim,L.E., Duclos,F., Broux,O., Bourg,N., Sunada,Y., Allamand,V.,
            Meyer,J., Richard,I., Moomaw,C., Slaughter,C. et al.
  TITLE     Beta-sarcoglycan: characterization and role in limb-girdle muscular
            dystrophy linked to 4q12
  JOURNAL   Nat Genet 11 (3), 257-265 (1995)
   PUBMED   7581448
REFERENCE   9  (residues 1 to 248)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Yoshida,M. and Ozawa,E.
  TITLE     Glycoprotein complex anchoring dystrophin to sarcolemma
  JOURNAL   J Biochem 108 (5), 748-752 (1990)
   PUBMED   2081733
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093858.2.
            
            On or before May 21, 2025 this sequence version replaced
            XP_047272030.1, XP_054206689.1.
            
            Summary: This gene encodes a member of the sarcoglycan family.
            Sarcoglycans are transmembrane components in the
            dystrophin-glycoprotein complex which help stabilize the muscle
            fiber membranes and link the muscle cytoskeleton to the
            extracellular matrix. Mutations in this gene have been associated
            with limb-girdle muscular dystrophy.[provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853564.20889.1,
                                           SRR11853561.22170.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..248
                     /product="beta-sarcoglycan isoform 2"
                     /note="beta-sarcoglycan; beta-sarcoglycan(43kD
                     dystrophin-associated glycoprotein); limb girdle muscular
                     dystrophy 2E (non-linked families); 43DAG; beta-SG; 43 kDa
                     dystrophin-associated glycoprotein; sarcoglycan, beta
                     (43kDa dystrophin-associated glycoprotein)"
                     /calculated_mol_wt=26792
     Region          12..233
                     /region_name="Sarcoglycan_1"
                     /note="Sarcoglycan complex subunit protein; pfam04790"
                     /db_xref="CDD:461428"
     CDS             1..248
                     /gene="SGCB"
                     /gene_synonym="A3b; LGMD2E; LGMDR4; SGC"
                     /coded_by="NM_001440519.1:41..787"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:6443"
                     /db_xref="HGNC:HGNC:10806"
                     /db_xref="MIM:600900"
ORIGIN      
        1 maaaaaaaae qitlviwavi rigpngcdsm efhesgllrf kqvsdmgvih plykstvggr
       61 rnenlvitgn nqpivfqqgt tklsvennkt sitsdigmqf fdprtqnilf stdyethefh
      121 lpsgvkslnv qkasterits natsdlnikv dgraivrgne gvfimgktie fhmggnmelk
      181 aensiilngs vmvsttrlps sssgdqlgsg dwvryklcmc adgtlfkvqv tsqnmgcqis
      241 dnpcgnth
//
LOCUS       NP_001397685             709 aa            linear   PRI 21-NOV-2025
DEFINITION  SH3 domain-containing kinase-binding protein 1 isoform k [Homo
            sapiens].
ACCESSION   NP_001397685 XP_011543800
VERSION     NP_001397685.1
DBSOURCE    REFSEQ: accession NM_001410756.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   3  (residues 1 to 709)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 709)
  AUTHORS   Ahmed,S.F., Buetow,L., Gabrielsen,M., Lilla,S., Sibbet,G.J.,
            Sumpton,D., Zanivan,S., Hedley,A., Clark,W. and Huang,D.T.
  TITLE     E3 ligase-inactivation rewires CBL interactome to elicit
            oncogenesis by hijacking RTK-CBL-CIN85 axis
  JOURNAL   Oncogene 40 (12), 2149-2164 (2021)
   PUBMED   33627783
  REMARK    GeneRIF: E3 ligase-inactivation rewires CBL interactome to elicit
            oncogenesis by hijacking RTK-CBL-CIN85 axis.
REFERENCE   5  (residues 1 to 709)
  AUTHORS   Soubeyran,P., Kowanetz,K., Szymkiewicz,I., Langdon,W.Y. and
            Dikic,I.
  TITLE     Cbl-CIN85-endophilin complex mediates ligand-induced downregulation
            of EGF receptors
  JOURNAL   Nature 416 (6877), 183-187 (2002)
   PUBMED   11894095
  REMARK    GeneRIF: Cbl-CIN85-endophilin complex mediates ligand-induced
            downregulation of EGF receptors
            Erratum:[Nature 2002 May 2;417(6884):102]
REFERENCE   6  (residues 1 to 709)
  AUTHORS   Narita,T., Amano,F., Yoshizaki,K., Nishimoto,N., Nishimura,T.,
            Tajima,T., Namiki,H. and Taniyama,T.
  TITLE     Assignment of SH3KBP1 to human chromosome band Xp22.1-->p21.3 by in
            situ hybridization
  JOURNAL   Cytogenet Cell Genet 93 (1-2), 133-134 (2001)
   PUBMED   11474197
REFERENCE   7  (residues 1 to 709)
  AUTHORS   Watanabe,S., Take,H., Takeda,K., Yu,Z.X., Iwata,N. and Kajigaya,S.
  TITLE     Characterization of the CIN85 adaptor protein and identification of
            components involved in CIN85 complexes
  JOURNAL   Biochem Biophys Res Commun 278 (1), 167-174 (2000)
   PUBMED   11071869
REFERENCE   8  (residues 1 to 709)
  AUTHORS   Gout,I., Middleton,G., Adu,J., Ninkina,N.N., Drobot,L.B.,
            Filonenko,V., Matsuka,G., Davies,A.M., Waterfield,M. and
            Buchman,V.L.
  TITLE     Negative regulation of PI 3-kinase by Ruk, a novel adaptor protein
  JOURNAL   EMBO J 19 (15), 4015-4025 (2000)
   PUBMED   10921882
REFERENCE   9  (residues 1 to 709)
  AUTHORS   Take,H., Watanabe,S., Takeda,K., Yu,Z.X., Iwata,N. and Kajigaya,S.
  TITLE     Cloning and characterization of a novel adaptor protein, CIN85,
            that interacts with c-Cbl
  JOURNAL   Biochem Biophys Res Commun 268 (2), 321-328 (2000)
   PUBMED   10679202
REFERENCE   10 (residues 1 to 709)
  AUTHORS   Salvatore,P., Hanash,C.R., Kido,Y., Imai,Y. and Accili,D.
  TITLE     Identification of sirm, a novel insulin-regulated SH3 binding
            protein that associates with Grb-2 and FYN
  JOURNAL   J Biol Chem 273 (12), 6989-6997 (1998)
   PUBMED   9507006
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL772197.12, AL732325.6,
            AL732327.6 and AL732423.12.
            
            On Aug 15, 2022 this sequence version replaced XP_011543800.1.
            
            Summary: This gene encodes an adapter protein that contains one or
            more N-terminal Src homology domains, a proline rich region and a
            C-terminal coiled-coil domain. The encoded protein facilitates
            protein-protein interactions and has been implicated in numerous
            cellular processes including apoptosis, cytoskeletal rearrangement,
            cell adhesion and in the regulation of clathrin-dependent
            endocytosis. Alternate splicing results in multiple transcript
            variants encoding distinct isoforms. [provided by RefSeq, Jul
            2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.8112.1,
                                           SRR1660807.143130.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.12"
     Protein         1..709
                     /product="SH3 domain-containing kinase-binding protein 1
                     isoform k"
                     /note="Src family kinase-binding protein 1; src-related
                     kinase binding protein-1; CD2-binding protein 3;
                     migration-inducing gene 18; c-Cbl-interacting protein;
                     cbl-interacting protein of 85 kDa; SH3-domain kinase
                     binding protein 1; human Src family kinase-binding protein
                     1"
                     /calculated_mol_wt=77788
     Region          3..55
                     /region_name="SH3_CIN85_1"
                     /note="First Src Homology 3 domain (SH3A) of
                     Cbl-interacting protein of 85 kDa; cd12052"
                     /db_xref="CDD:212985"
     Site            order(7..13,17,21..22,34..36,46..47,49,51..52)
                     /site_type="other"
                     /note="putative ubiquitin interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:212985"
     Site            order(8,10,13..14,16..17,34,36,47,51..52,54)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212985"
     Region          102..154
                     /region_name="SH3_CIN85_2"
                     /note="Second Src Homology 3 domain (SH3B) of
                     Cbl-interacting protein of 85 kDa; cd12055"
                     /db_xref="CDD:212988"
     Site            order(106..112,116,120..121,133..135,145..146,148,
                     150..151)
                     /site_type="other"
                     /note="putative ubiquitin interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:212988"
     Site            order(107,109,112,116,133..135,146,148,150..151)
                     /site_type="other"
                     /note="putative peptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:212988"
     Region          315..370
                     /region_name="SH3_CIN85_3"
                     /note="Third Src Homology 3 domain (SH3C) of
                     Cbl-interacting protein of 85 kDa; cd12057"
                     /db_xref="CDD:212990"
     Site            order(319..326,328..329,333..334,347..350,360..361,363,
                     365..366,368)
                     /site_type="other"
                     /note="ubiquitin interaction site [polypeptide binding]"
                     /db_xref="CDD:212990"
     Site            order(320,322,325,329,348..350,361,363,365..366)
                     /site_type="other"
                     /note="putative peptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:212990"
     CDS             1..709
                     /gene="SH3KBP1"
                     /gene_synonym="AGMX2; CD2BP3; CIN85; GIG10; HSB-1; HSB1;
                     IMD61; MIG18"
                     /coded_by="NM_001410756.1:291..2420"
                     /note="isoform k is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS94575.1"
                     /db_xref="GeneID:30011"
                     /db_xref="HGNC:HGNC:13867"
                     /db_xref="MIM:300374"
ORIGIN      
        1 mveaivefdy qaqhddelti svgeiitnir kedggwwegq ingrrglfpd nfvreikkem
       61 kkdpltnkap ekplhevpsg nsllssetil rtnkrgerrr rrcqvafsyl pqnddelelk
      121 vgdiievvge veegwwegvl ngktgmfpsn fikelsgesd elgisqdeql sksrpeglpp
      181 asllpfpahg akgkttfegt ilyraapgkt eghrryyslr ettgsesdgg dssstksega
      241 ngtvataaiq pkkvkgvgfg difkdkpikl rprsievend flpvektigk klpattatpd
      301 ssktemdsrt kskdyckvif pyeaqnddel tikegdivtl inkdcidvgw wegelngrrg
      361 vfpdnfvkll ppdfekegnr pkkppppsap vikqgagtte rkheikkipp erpemlpnrt
      421 eekerperep kldlqkpsvp aippkkprpp ktnslsrpga lpprrperpv gplthtrgds
      481 pkidlagssl sgildkdlsd rsndidlegf dsvvsstekl shpttsrpka tgrrppsqsl
      541 tssslsspdi fdspspeedk eehislahrg vdaskktskt vtisqvsdnk aslppkpgtm
      601 aaggggpapl ssaapsplss slgtaghran spslfgtegk pkmepaassq aaveelrtqv
      661 relrsiietm kdqqkreikq llseldeekk irlrlqmevn dikkalqsk
//
LOCUS       NP_001401620             496 aa            linear   PRI 21-NOV-2025
DEFINITION  nucleolar complex protein 4 homolog isoform 5 [Homo sapiens].
ACCESSION   NP_001401620
VERSION     NP_001401620.1
DBSOURCE    REFSEQ: accession NM_001414691.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Talebi,A., Shahidsales,S., Aliakbarian,M., Pezeshki Rad,M. and
            Kerachian,M.A.
  TITLE     Oncogenic fusion transcript analysis identified ADAP1-NOC4L,
            potentially associated with metastatic colorectal cancer
  JOURNAL   Cancer Med 12 (1), 525-540 (2023)
   PUBMED   35702822
  REMARK    GeneRIF: Oncogenic fusion transcript analysis identified
            ADAP1-NOC4L, potentially associated with metastatic colorectal
            cancer.
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Qin,Y., Li,H., Jia,L., Yan,J., Gao,G.F. and Li,X.
  TITLE     Targeted disruption of Noc4l leads to preimplantation embryonic
            lethality in mice
  JOURNAL   Protein Cell 8 (3), 230-235 (2017)
   PUBMED   28012024
  REMARK    GeneRIF: The results provide the first in vivo genetic evidence
            that Noc4l plays important roles in early embryogenesis in mice.
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 496)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 496)
  AUTHORS   Bernstein,K.A., Gallagher,J.E., Mitchell,B.M., Granneman,S. and
            Baserga,S.J.
  TITLE     The small-subunit processome is a ribosome assembly intermediate
  JOURNAL   Eukaryot Cell 3 (6), 1619-1626 (2004)
   PUBMED   15590835
REFERENCE   8  (residues 1 to 496)
  AUTHORS   Milkereit,P., Strauss,D., Bassler,J., Gadal,O., Kuhn,H., Schutz,S.,
            Gas,N., Lechner,J., Hurt,E. and Tschochner,H.
  TITLE     A Noc complex specifically involved in the formation and nuclear
            export of ribosomal 40 S subunits
  JOURNAL   J Biol Chem 278 (6), 4072-4081 (2003)
   PUBMED   12446671
REFERENCE   9  (residues 1 to 496)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC138466.12.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.358538.1,
                                           SRR14038193.3613607.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.33"
     Protein         1..496
                     /product="nucleolar complex protein 4 homolog isoform 5"
                     /note="nucleolar complex protein 4 homolog; NOC4-like
                     protein; NOC4 protein homolog; nucleolar
                     complex-associated protein 4-like protein"
                     /calculated_mol_wt=56081
     Region          290..432
                     /region_name="CBF"
                     /note="CBF/Mak21 family; pfam03914"
                     /db_xref="CDD:461090"
     CDS             1..496
                     /gene="NOC4L"
                     /gene_synonym="NET49; NOC4; UTP19"
                     /coded_by="NM_001414691.1:33..1523"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:79050"
                     /db_xref="HGNC:HGNC:28461"
                     /db_xref="MIM:612819"
ORIGIN      
        1 merepgaagv rralgrrlea vlasrseana vfdilavlqs edqeeiqeav rtcsrlfgal
       61 lergelfvgq lpseemvmtg sqgatrkykv wmrhryhscc nrlgellghp sfqvkelals
      121 allkfvqleg ahplekskwe gnylfprelf klvvggllsp eedqslllsq freyldyddt
      181 ryhtmqaavd avarvtgqhp evppafwnna ftllsavslp rreptvssfy vkraelwdtw
      241 kvahlkehrr vfqamwlsfl khklaqptlm idfltracdl ggalsllaln glfilihkhn
      301 leypdfyrkl yglldpsvfh vkyrarffhl adlflssshl paylvaafak rlarlaltap
      361 peallmvlpf icnllrrhpa crvlvhrphg peldadpydp geedpaqsra lesslwelqa
      421 lqrhyhpevs kaasvinqal smpevsiapl leltayeife rdlkkkgpep vplefipaqg
      481 llgrpgelca qhftls
//
LOCUS       NP_001394398            2714 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform r [Homo sapiens].
ACCESSION   NP_001394398
VERSION     NP_001394398.1
DBSOURCE    REFSEQ: accession NM_001407469.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2714)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2714)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2714)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2714)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2714)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2714)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2714)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2714)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2714)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2714)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2458089.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2714
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2714
                     /product="adenomatous polyposis coli protein isoform r"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=296950
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          <279..337
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          336..379
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(370,374,378,413,417,421,457,461,465)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          383..424
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          387..424
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          431..466
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          474..515
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          520..560
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          524..558
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          562..602
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          566..602
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          603..890
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          907..1006
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1128..>1145
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1154..1239
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1162..1572
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1242..1264
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1508..1531
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1533..1586
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1587..1608
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1617..1710
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1744..1818
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1904..1923
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2094..2439
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2541..2714
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2714
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407469.1:404..8548"
                     /note="isoform r is encoded by transcript variant 32"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrssqn khetgshdae rqnegqgvge
      241 inmatsgngq gsttrmdhet asvlssssth saprrltshl gtkiraycet cwewqeahep
      301 gmdqdknpmp apvehqicpa vcvlmklsfd eehrhamnel gglqaiaell qvdcemyglt
      361 ndhysitlrr yagmaltnlt fgdvankatl csmkgcmral vaqlksesed lqqviasvlr
      421 nlswradvns kktlrevgsv kalmecalev kkestlksvl salwnlsahc tenkadicav
      481 dgalaflvgt ltyrsqtntl aiiesgggil rnvssliatn edhrqilren nclqtllqhl
      541 kshsltivsn acgtlwnlsa rnpkdqealw dmgavsmlkn lihskhkmia mgsaaalrnl
      601 manrpakykd animspgssl pslhvrkqka leaeldaqhl setfdnidnl spkashrskq
      661 rhkqslygdy vfdtnrhddn rsdnfntgnm tvlspylntt vlpsssssrg sldssrsekd
      721 rslerergig lgnyhpaten pgtsskrglq isttaaqiak vmeevsaiht sqedrssgst
      781 telhcvtder nalrrssaah thsntynftk sensnrtcsm pyakleykrs sndslnsvss
      841 sdgygkrgqm kpsiesysed deskfcsygq ypadlahkih sanhmddndg eldtpinysl
      901 kysdeqlnsg rqspsqnerw arpkhiiede ikqseqrqsr nqsttypvyt estddkhlkf
      961 qphfgqqecv spyrsrgang setnrvgsnh ginqnvsqsl cqeddyeddk ptnyseryse
     1021 eeqheeeerp tnysikynee krhvdqpidy slkyatdips sqkqsfsfsk sssgqsskte
     1081 hmssssents tpssnakrqn qlhpssaqsr sgqpqkaatc kvssinqeti qtycvedtpi
     1141 cfsrcsslss lssaedeigc nqttqeadsa ntlqiaeike kigtrsaedp vsevpavsqh
     1201 prtkssrlqg sslssesarh kavefssgak spsksgaqtp ksppehyvqe tplmfsrcts
     1261 vssldsfesr siassvqsep csgmvsgiis psdlpdspgq tmppsrsktp ppppqtaqtk
     1321 revpknkapt aekresgpkq aavnaavqrv qvlpdadtll hfatestpdg fscssslsal
     1381 sldepfiqkd velrimppvq endngnetes eqpkesnenq ekeaektids ekdllddsdd
     1441 ddieileeci isamptkssr kakkpaqtas klpppvarkp sqlpvykllp sqnrlqpqkh
     1501 vsftpgddmp rvycvegtpi nfstatslsd ltiesppnel aagegvrgga qsgefekrdt
     1561 iptegrstde aqggktssvt ipelddnkae egdilaecin sampkgkshk pfrvkkimdq
     1621 vqqasasssa pnknqldgkk kkptspvkpi pqnteyrtrv rknadsknnl naervfsdnk
     1681 dskkqnlknn skvfndklpn nedrvrgsfa fdsphhytpi egtpycfsrn dslssldfdd
     1741 ddvdlsreka elrkakenke seakvtshte ltsnqqsank tqaiakqpin rgqpkpilqk
     1801 qstfpqsskd ipdrgaatde klqnfaient pvcfshnssl sslsdidqen nnkenepike
     1861 teppdsqgep skpqasgyap ksfhvedtpv cfsrnsslss lsidseddll qecissampk
     1921 kkkpsrlkgd nekhsprnmg gilgedltld lkdiqrpdse hglspdsenf dwkaiqegan
     1981 sivsslhqaa aaaclsrqas sdsdsilslk sgislgspfh ltpdqeekpf tsnkgprilk
     2041 pgekstletk kieseskgik ggkkvyksli tgkvrsnsei sgqmkqplqa nmpsisrgrt
     2101 mihipgvrns ssstspvskk gpplktpask spsegqtatt sprgakpsvk selspvarqt
     2161 sqiggsskap srsgsrdstp srpaqqplsr piqspgrnsi spgrngispp nklsqlprts
     2221 spstastkss gsgkmsytsp grqmsqqnlt kqtglsknas siprsesask glnqmnngng
     2281 ankkvelsrm sstkssgses drserpvlvr qstfikeaps ptlrrklees asfeslspss
     2341 rpasptrsqa qtpvlspslp dmslsthssv qaggwrklpp nlsptieynd grpakrhdia
     2401 rshsespsrl pinrsgtwkr ehskhssslp rvstwrrtgs sssilsasse ssekaksede
     2461 khvnsisgtk qskenqvsak gtwrkikene fsptnstsqt vssgatngae sktliyqmap
     2521 avsktedvwv riedcpinnp rsgrsptgnt ppvidsvsek anpnikdskd nqakqnvgng
     2581 svpmrtvgle nrlnsfiqvd apdqkgteik pgqnnpvpvs etnessiver tpfssssssk
     2641 hsspsgtvaa rvtpfnynps prkssadsts arpsqiptpv nnntkkrdsk tdstessgtq
     2701 spkrhsgsyl vtsv
//
LOCUS       NP_001393525            1164 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 1 [Homo sapiens].
ACCESSION   NP_001393525
VERSION     NP_001393525.1
DBSOURCE    REFSEQ: accession NM_001406596.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1164)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1164)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1164)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1164)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1164)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1164)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1164)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1548504.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1164
                     /product="hamartin isoform 1"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=129636
     Region          7..719
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          403..787
                     /region_name="Mediates interaction with WDR45B.
                     /evidence=ECO:0000269|PubMed:28561066"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Region          439..571
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <708..>960
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1006..1085
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1131..1164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1164
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406596.1:155..3649"
                     /note="isoform 1 is encoded by transcript variant 10"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt aggkgtplgt patspppapl chsddyvhis lpqatvtppr
      421 keermdsarp clhrqhhlln drgseeppgs kgsvtlsdlp gflgdlasee dsiekdkeea
      481 aisrelseit taeaepvvpr ggfdspfyrd slpgsqrkth saasssqgas vnpeplhssl
      541 dklgpdtpkq aftpidlpcg sadespagdr ecqtsletsi ftpspckipp ptrvgfgsgq
      601 pppydhlfev alpktahhfv irkteellkk akgnteedgv pstspmevld rliqqgadah
      661 skelnklplp sksvdwthfg gsppsdeirt lrdqllllhn qllyerfkrq qhalrnrrll
      721 rkvikaaale ehnaamkdql klqekdiqmw kvslqkeqar ynqlqeqrdt mvtklhsqir
      781 qlqhdreefy nqsqelqtkl edcrnmiael rielkkannk vchtelllsq vsqklsnses
      841 vqqqmeflnr qllvlgevne lyleqlqnkh sdttkevemm kaayrkelek nrshvlqqtq
      901 rldtsqkril eleshlakkd hllleqkkyl edvklqargq lqaaesryea qkritqvfel
      961 eildlygrle kdgllkklee ekaeaaeaae erldccndgc sdsmvghnee asghngetkt
     1021 prpssargss gsrggggsss ssselstpek pphqragpfs srwettmgea sasipttvgs
     1081 lpssksflgm karelfrnks esqcdedgmt sslseslkte lgkdlgveak iplnldgphp
     1141 spptpdsvgq lhimdyneth hehs
//
LOCUS       NP_001394184             404 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase STK11 isoform 2 [Homo sapiens].
ACCESSION   NP_001394184
VERSION     NP_001394184.1
DBSOURCE    REFSEQ: accession NM_001407255.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Hou,J., Mei,K., Wang,D., Ke,S., Chen,X., Shang,J., Li,G., Gao,Y.,
            Xiong,H., Zhang,H., Chen,L., Zhang,W., Deng,Y., Hong,X., Liu,D.A.,
            Hu,T., Guo,W. and Zhan,Y.Y.
  TITLE     TGM1/3-mediated transamidation of Exo70 promotes tumor metastasis
            upon LKB1 inactivation
  JOURNAL   Cell Rep 43 (8), 114604 (2024)
   PUBMED   39146185
  REMARK    GeneRIF: TGM1/3-mediated transamidation of Exo70 promotes tumor
            metastasis upon LKB1 inactivation.
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Principe,D.R., Pasquinelli,M.M., Nguyen,R.H., Munshi,H.G.,
            Hulbert,A., Aissa,A.F. and Weinberg,F.
  TITLE     Loss of STK11 Suppresses Lipid Metabolism and Attenuates
            KRAS-Induced Immunogenicity in Patients with Non-Small Cell Lung
            Cancer
  JOURNAL   Cancer Res Commun 4 (8), 2282-2294 (2024)
   PUBMED   39113608
  REMARK    GeneRIF: Loss of STK11 Suppresses Lipid Metabolism and Attenuates
            KRAS-Induced Immunogenicity in Patients with Non-Small Cell Lung
            Cancer.
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Wang,X., Li,Y., Zhang,J., Liu,C., Deng,A. and Li,J.
  TITLE     Genetic variation at a splicing branch point in intron 7 of STK11:
            a rare variant decreasing its expression in a Chinese family with
            Peutz-Jeghers syndrome
  JOURNAL   World J Surg Oncol 22 (1), 202 (2024)
   PUBMED   39080663
  REMARK    GeneRIF: Genetic variation at a splicing branch point in intron 7
            of STK11: a rare variant decreasing its expression in a Chinese
            family with Peutz-Jeghers syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Liu,M., Gu,L., Zhang,Y., Li,Y., Zhang,L., Xin,Y., Wang,Y. and
            Xu,Z.X.
  TITLE     LKB1 inhibits telomerase activity resulting in cellular senescence
            through histone lactylation in lung adenocarcinoma
  JOURNAL   Cancer Lett 595, 217025 (2024)
   PUBMED   38844063
  REMARK    GeneRIF: LKB1 inhibits telomerase activity resulting in cellular
            senescence through histone lactylation in lung adenocarcinoma.
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Bignell,G.R., Barfoot,R., Seal,S., Collins,N., Warren,W. and
            Stratton,M.R.
  TITLE     Low frequency of somatic mutations in the LKB1/Peutz-Jeghers
            syndrome gene in sporadic breast cancer
  JOURNAL   Cancer Res 58 (7), 1384-1386 (1998)
   PUBMED   9537235
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Hemminki,A., Markie,D., Tomlinson,I., Avizienyte,E., Roth,S.,
            Loukola,A., Bignell,G., Warren,W., Aminoff,M., Hoglund,P.,
            Jarvinen,H., Kristo,P., Pelin,K., Ridanpaa,M., Salovaara,R.,
            Toro,T., Bodmer,W., Olschwang,S., Olsen,A.S., Stratton,M.R., de la
            Chapelle,A. and Aaltonen,L.A.
  TITLE     A serine/threonine kinase gene defective in Peutz-Jeghers syndrome
  JOURNAL   Nature 391 (6663), 184-187 (1998)
   PUBMED   9428765
REFERENCE   8  (residues 1 to 404)
  AUTHORS   Jenne,D.E., Reimann,H., Nezu,J., Friedel,W., Loff,S., Jeschke,R.,
            Muller,O., Back,W. and Zimmer,M.
  TITLE     Peutz-Jeghers syndrome is caused by mutations in a novel serine
            threonine kinase
  JOURNAL   Nat Genet 18 (1), 38-43 (1998)
   PUBMED   9425897
REFERENCE   9  (residues 1 to 404)
  AUTHORS   Hemminki,A., Tomlinson,I., Markie,D., Jarvinen,H., Sistonen,P.,
            Bjorkqvist,A.M., Knuutila,S., Salovaara,R., Bodmer,W., Shibata,D.,
            de la Chapelle,A. and Aaltonen,L.A.
  TITLE     Localization of a susceptibility locus for Peutz-Jeghers syndrome
            to 19p using comparative genomic hybridization and targeted linkage
            analysis
  JOURNAL   Nat Genet 15 (1), 87-90 (1997)
   PUBMED   8988175
REFERENCE   10 (residues 1 to 404)
  AUTHORS   McGarrity,T.J., Amos,C.I. and Baker,M.J.
  TITLE     Peutz-Jeghers Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301443
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011544.6.
            
            Summary: The protein encoded by this gene is a serine/threonine
            kinase that regulates cell polarity and energy metabolism and
            functions as a tumor suppressor. Mutations in this gene have been
            associated with the autosomal dominant Peutz-Jeghers syndrome, as
            well as with skin, pancreatic, and testicular cancers. [provided by
            RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR9304713.255619.1,
                                           SRR14038193.3379081.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..404
                     /product="serine/threonine-protein kinase STK11 isoform 2"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase 11;
                     polarization-related protein LKB1; renal carcinoma antigen
                     NY-REN-19; serine/threonine-protein kinase LKB1; liver
                     kinase B1; serine/threonine-protein kinase STK11"
                     /calculated_mol_wt=45256
     Region          55..309
                     /region_name="STKc_LKB1"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Liver Kinase B1; cd14119"
                     /db_xref="CDD:271021"
     Site            order(55..59,63,76,78,111,129..132,136,138,176,178,
                     180..181,183,194,197,215..218)
                     /site_type="active"
                     /db_xref="CDD:271021"
     Site            order(55..59,63,76,78,111,129..132,136,176,178,180..181,
                     183,194)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271021"
     Site            order(59,136,138,176,178,180,197,215..218)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271021"
     Site            order(70..74,106,186..187)
                     /site_type="other"
                     /note="STRAD interface [polypeptide binding]"
                     /db_xref="CDD:271021"
     Site            order(100,165,168..169,171,201..207,301,307)
                     /site_type="other"
                     /note="MO25 interface [polypeptide binding]"
                     /db_xref="CDD:271021"
     Site            193..218
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271021"
     CDS             1..404
                     /gene="STK11"
                     /gene_synonym="hLKB1; LKB1; PJS"
                     /coded_by="NM_001407255.1:1137..2351"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:6794"
                     /db_xref="HGNC:HGNC:11389"
                     /db_xref="MIM:602216"
ORIGIN      
        1 mevvdpqqlg mftegelmsv gmdtfihrid steviyqprr krakligkyl mgdllgegsy
       61 gkvkevldse tlcrravkil kkkklrripn geanvkkeiq llrrlrhknv iqlvdvlyne
      121 ekqkmymvme ycvcgmqeml dsvpekrfpv cqahgyfcql idgleylhsq givhkdikpg
      181 nlllttggtl kisdlgvaea lhpfaaddtc rtsqgspafq ppeiangldt fsgfkvdiws
      241 agvtlynitt glypfegdni yklfenigkg syaipgdcgp plsdllkgml eyepakrfsi
      301 rqirqhswfr kkhppaeapv pippspdtkd rwrsmtvvpy ledlhgaded edlfdieddi
      361 iytqdftvpg geeaseaglr aerglqkseg sdlsgeeasr papq
//
LOCUS       NP_001394385            2760 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform q [Homo sapiens].
ACCESSION   NP_001394385
VERSION     NP_001394385.1
DBSOURCE    REFSEQ: accession NM_001407456.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2760)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2760)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2760)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2760)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2760)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2760)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2760)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2760)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2760)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2760)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3285704.1,
                                           SRR14372079.834321.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2760
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2760
                     /product="adenomatous polyposis coli protein isoform q"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=302136
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Region          <8..272
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          239..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          <307..365
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          389..425
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          429..470
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          433..470
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          480..512
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(503,507,511,550,554,558,595,599,603)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          520..561
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          566..606
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          570..604
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          608..648
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          612..648
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          649..936
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          953..1052
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1174..>1191
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1200..1285
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1208..1618
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1288..1310
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1554..1577
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1579..1632
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1633..1654
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1663..1756
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1790..1864
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1950..1969
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2140..2485
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2587..2760
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2760
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407456.1:404..8686"
                     /note="isoform q is encoded by transcript variant 26"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrriar iqqiekdilr irqllqsqat
      241 eaerssqnkh etgshdaerq negqgvgein matsgngqgs ttrmdhetas vlssssthsa
      301 prrltshlgt kiraycetcw ewqeahepgm dqdknpmpap vehqicpavc vlmklsfdee
      361 hrhamnelgr katrgissqe lgqglsgglq aiaellqvdc emygltndhy sitlrryagm
      421 altnltfgdv ankatlcsmk gcmralvaql ksesedlqqv iasvlrnlsw radvnskktl
      481 revgsvkalm ecalevkkes tlksvlsalw nlsahctenk adicavdgal aflvgtltyr
      541 sqtntlaiie sgggilrnvs sliatnedhr qilrennclq tllqhlkshs ltivsnacgt
      601 lwnlsarnpk dqealwdmga vsmlknlihs khkmiamgsa aalrnlmanr pakykdanim
      661 spgsslpslh vrkqkaleae ldaqhlsetf dnidnlspka shrskqrhkq slygdyvfdt
      721 nrhddnrsdn fntgnmtvls pylnttvlps ssssrgslds srsekdrsle rergiglgny
      781 hpatenpgts skrglqistt aaqiakvmee vsaihtsqed rssgsttelh cvtdernalr
      841 rssaahthsn tynftksens nrtcsmpyak leykrssnds lnsvsssdgy gkrgqmkpsi
      901 esyseddesk fcsygqypad lahkihsanh mddndgeldt pinyslkysd eqlnsgrqsp
      961 sqnerwarpk hiiedeikqs eqrqsrnqst typvytestd dkhlkfqphf gqqecvspyr
     1021 srgangsetn rvgsnhginq nvsqslcqed dyeddkptny seryseeeqh eeeerptnys
     1081 ikyneekrhv dqpidyslky atdipssqkq sfsfsksssg qssktehmss ssentstpss
     1141 nakrqnqlhp ssaqsrsgqp qkaatckvss inqetiqtyc vedtpicfsr csslsslssa
     1201 edeigcnqtt qeadsantlq iaeikekigt rsaedpvsev pavsqhprtk ssrlqgssls
     1261 sesarhkave fssgakspsk sgaqtpkspp ehyvqetplm fsrctsvssl dsfesrsias
     1321 svqsepcsgm vsgiispsdl pdspgqtmpp srsktppppp qtaqtkrevp knkaptaekr
     1381 esgpkqaavn aavqrvqvlp dadtllhfat estpdgfscs sslsalslde pfiqkdvelr
     1441 imppvqendn gneteseqpk esnenqekea ektidsekdl lddsddddie ileeciisam
     1501 ptkssrkakk paqtasklpp pvarkpsqlp vykllpsqnr lqpqkhvsft pgddmprvyc
     1561 vegtpinfst atslsdltie sppnelaage gvrggaqsge fekrdtipte grstdeaqgg
     1621 ktssvtipel ddnkaeegdi laecinsamp kgkshkpfrv kkimdqvqqa sasssapnkn
     1681 qldgkkkkpt spvkpipqnt eyrtrvrkna dsknnlnaer vfsdnkdskk qnlknnskvf
     1741 ndklpnnedr vrgsfafdsp hhytpiegtp ycfsrndsls sldfddddvd lsrekaelrk
     1801 akenkeseak vtshteltsn qqsanktqai akqpinrgqp kpilqkqstf pqsskdipdr
     1861 gaatdeklqn faientpvcf shnsslssls didqennnke nepiketepp dsqgepskpq
     1921 asgyapksfh vedtpvcfsr nsslsslsid seddllqeci ssampkkkkp srlkgdnekh
     1981 sprnmggilg edltldlkdi qrpdsehgls pdsenfdwka iqegansivs slhqaaaaac
     2041 lsrqassdsd silslksgis lgspfhltpd qeekpftsnk gprilkpgek stletkkies
     2101 eskgikggkk vykslitgkv rsnseisgqm kqplqanmps isrgrtmihi pgvrnsssst
     2161 spvskkgppl ktpaskspse gqtattsprg akpsvksels pvarqtsqig gsskapsrsg
     2221 srdstpsrpa qqplsrpiqs pgrnsispgr ngisppnkls qlprtsspst astkssgsgk
     2281 msytspgrqm sqqnltkqtg lsknassipr sesaskglnq mnngngankk velsrmsstk
     2341 ssgsesdrse rpvlvrqstf ikeapsptlr rkleesasfe slspssrpas ptrsqaqtpv
     2401 lspslpdmsl sthssvqagg wrklppnlsp tieyndgrpa krhdiarshs espsrlpinr
     2461 sgtwkrehsk hssslprvst wrrtgssssi lsassessek aksedekhvn sisgtkqske
     2521 nqvsakgtwr kikenefspt nstsqtvssg atngaesktl iyqmapavsk tedvwvried
     2581 cpinnprsgr sptgntppvi dsvsekanpn ikdskdnqak qnvgngsvpm rtvglenrln
     2641 sfiqvdapdq kgteikpgqn npvpvsetne ssivertpfs ssssskhssp sgtvaarvtp
     2701 fnynpsprks sadstsarps qiptpvnnnt kkrdsktdst essgtqspkr hsgsylvtsv
//
LOCUS       NP_001424554            1290 aa            linear   PRI 21-NOV-2025
DEFINITION  ras GTPase-activating protein nGAP isoform 3 [Homo sapiens].
ACCESSION   NP_001424554 XP_011508468 XP_054195665
VERSION     NP_001424554.1
DBSOURCE    REFSEQ: accession NM_001437625.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1290)
  AUTHORS   Zhang,Y., Yang,Y., Hu,X., Wei,B., Shen,Q., Shi,C. and Chen,P.
  TITLE     RAS protein activator-like 2 (RASAL2) initiates peritubular
            capillary rarefaction in hypoxic renal interstitial fibrosis
  JOURNAL   Transl Res 269, 14-30 (2024)
   PUBMED   38453052
  REMARK    GeneRIF: RAS protein activator-like 2 (RASAL2) initiates
            peritubular capillary rarefaction in hypoxic renal interstitial
            fibrosis.
REFERENCE   2  (residues 1 to 1290)
  AUTHORS   Singharajkomron,N., Yodsurang,V., Limprasutr,V., Wattanathamsan,O.,
            Iksen,I., Hayakawa,Y. and Pongrakhananon,V.
  TITLE     CAMSAP2 enhances lung cancer cell metastasis by mediating RASAL2
            degradation
  JOURNAL   Life Sci 338, 122391 (2024)
   PUBMED   38159595
  REMARK    GeneRIF: CAMSAP2 enhances lung cancer cell metastasis by mediating
            RASAL2 degradation.
REFERENCE   3  (residues 1 to 1290)
  AUTHORS   Wills,C., Watts,K., Maughan,T.S., Fisher,D., Al-Tassan,N.A.,
            Houlston,R.S., Escott-Price,V. and Cheadle,J.P.
  TITLE     Germline variation in RASAL2 may predict survival in patients with
            RAS-activated colorectal cancer
  JOURNAL   Genes Chromosomes Cancer 62 (6), 332-341 (2023)
   PUBMED   36790221
  REMARK    GeneRIF: Germline variation in RASAL2 may predict survival in
            patients with RAS-activated colorectal cancer.
REFERENCE   4  (residues 1 to 1290)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 1290)
  AUTHORS   Yue,Y., Wu,K., Qian,W., Zhu,Z., Zhang,S., Zhang,W., Zhang,W.,
            Wu,S., Li,L., Wu,Z., Ma,Q., Xie,K. and Wang,Z.
  TITLE     RASAL2 mediated the enhancement of YAP1/TIAM1 signaling promotes
            malignant phenotypes of pancreatic ductal adenocarcinoma
  JOURNAL   Int J Biol Sci 18 (10), 4245-4259 (2022)
   PUBMED   35844783
  REMARK    GeneRIF: RASAL2 mediated the enhancement of YAP1/TIAM1 signaling
            promotes malignant phenotypes of pancreatic ductal adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1290)
  AUTHORS   Melen,E., Himes,B.E., Brehm,J.M., Boutaoui,N., Klanderman,B.J.,
            Sylvia,J.S. and Lasky-Su,J.
  TITLE     Analyses of shared genetic factors between asthma and obesity in
            children
  JOURNAL   J Allergy Clin Immunol 126 (3), 631-7 (2010)
   PUBMED   20816195
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1290)
  AUTHORS   Shibui,T., Kobayashi,T. and Shiratori,M.
  TITLE     Isolation of cross-reacting antigen candidates by mRNA-display
            using a mixed cDNA library
  JOURNAL   Biotechnol Lett 30 (12), 2037-2043 (2008)
   PUBMED   18633578
REFERENCE   8  (residues 1 to 1290)
  AUTHORS   de Chassey,B., Navratil,V., Tafforeau,L., Hiet,M.S., Aublin-Gex,A.,
            Agaugue,S., Meiffren,G., Pradezynski,F., Faria,B.F., Chantier,T.,
            Le Breton,M., Pellet,J., Davoust,N., Mangeot,P.E., Chaboud,A.,
            Penin,F., Jacob,Y., Vidalain,P.O., Vidal,M., Andre,P.,
            Rabourdin-Combe,C. and Lotteau,V.
  TITLE     Hepatitis C virus infection protein network
  JOURNAL   Mol Syst Biol 4, 230 (2008)
   PUBMED   18985028
REFERENCE   9  (residues 1 to 1290)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 1290)
  AUTHORS   Noto,S., Maeda,T., Hattori,S., Inazawa,J., Imamura,M., Asaka,M. and
            Hatakeyama,M.
  TITLE     A novel human RasGAP-like gene that maps within the prostate cancer
            susceptibility locus at chromosome 1q25
  JOURNAL   FEBS Lett 441 (1), 127-131 (1998)
   PUBMED   9877179
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160281.17, AL499617.16,
            AL365357.12 and AL035702.7.
            
            On or before Apr 7, 2025 this sequence version replaced
            XP_011508468.1, XP_054195665.1.
            
            Summary: This gene encodes a protein that contains the GAP-related
            domain (GRD), a characteristic domain of GTPase-activating proteins
            (GAPs). GAPs function as activators of Ras superfamily of small
            GTPases. The protein encoded by this gene is able to complement the
            defective RasGAP function in a yeast system. Two alternatively
            spliced transcript variants of this gene encoding distinct isoforms
            have been reported. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.742888.1,
                                           SRR14372079.872448.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1290
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..1290
                     /product="ras GTPase-activating protein nGAP isoform 3"
                     /note="Ras protein activator like 1; ras GTPase-activating
                     protein nGAP; RASAL2/ACVR1 fusion"
                     /calculated_mol_wt=144925
     Region          184..321
                     /region_name="PH_nGAP"
                     /note="Neuronal growth-associated proteins Pleckstrin
                     homology (PH) domain; cd13373"
                     /db_xref="CDD:270176"
     Region          307..446
                     /region_name="C2_SynGAP_like"
                     /note="C2 domain present in Ras GTPase activating protein
                     (GAP) family; cd04013"
                     /db_xref="CDD:175980"
     Region          437..767
                     /region_name="RasGAP_DAB2IP"
                     /note="Ras-GTPase Activating Domain of DAB2IP and similar
                     proteins; cd05136"
                     /db_xref="CDD:213338"
     Site            order(476,513,515,517..518,520,523,527,619,627..628,
                     631..632,635,656,659..660,663,667,669,674..675)
                     /site_type="other"
                     /note="putative RAS interface [polypeptide binding]"
                     /db_xref="CDD:213338"
     Region          757..1233
                     /region_name="DUF3498"
                     /note="Domain of unknown function (DUF3498); pfam12004"
                     /db_xref="CDD:463427"
     CDS             1..1290
                     /gene="RASAL2"
                     /gene_synonym="NGAP"
                     /coded_by="NM_001437625.1:390..4262"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:9462"
                     /db_xref="HGNC:HGNC:9874"
                     /db_xref="MIM:606136"
ORIGIN      
        1 melspssgga aealswpemf palesdsplp pedldavvpv sgavaggmld rillesvcqq
       61 qswvrvydvk gppthrlscg qspytetttw erkyciltds qlvllnkeke ipveggqeqq
      121 tdstkgrclr rtvsvpsegq fpeyppegat klevpaersp rrrsisgtst sekpnsmdta
      181 ntspfkvpgf fskrlkgsik rtksqskldr ntsfrlpslr stddrsrglp klkesrshes
      241 llspcstvec ldlgrgepvs vkplhssilg qdfcfevtyl sgskcfscns aserdkwmen
      301 lrrtvqpnkd ncrraenvlr lwiieakdla pkkkyfcelc lddtlfartt sktkadnifw
      361 gehfeffslp plhsitvhiy kdvekkkkkd knnyvglvni ptasvtgrqf vekwypvstp
      421 tpnkgktggp siriksrfqt itilpmeqyk efaefvtsny tmlcsvlepv isvrnkeela
      481 calvhilqst grakdfltdl vmsevdrcge hdvlifrent iatksieeyl klvgqqylhd
      541 algefikaly esdencevdp skcssselid hqsnlkmcce lafckiinsy cvfprelkev
      601 faswkqqcln rgkqdiserl isaslflrfl cpaimspslf nlmqeypddr tsrtltliak
      661 viqnlanfak fgnkeeymaf mndflehewg gmkrflleis npdtisntpg fdgyidlgre
      721 lsvlhsllwe vvsqldkgen sflqatvakl gplprvladi tksltnptpi qqqlrrfteh
      781 nsspnvsgsl ssglqkifed ptdsdlhklk spsqdntdsy frgktlllvq qassqsmtys
      841 ekderesslp ngrsvslmdl qdthaaqveh asvmldvpir ltgsqlsitq vasikqlret
      901 qstpqsapqv rrplhpalnq pgglqplsfq npvyhlnnpi pampkasids slenlstass
      961 rsqsnsedfk lsgpsnssme dftkrstqse dfsrrhtvpd rhiplalprq nstgqaqirk
     1021 vdqgglgara kappslphsa slrstgsmsv vsaalvaepv qngsrsrqqs sssrespvpk
     1081 vraiqrqqtq qvqspvdsat mspvertaaw vlnngqyeed veeteqnlde akhaekyeqe
     1141 itklkerlrv ssrrleeyer rllvqeqqmq kllleykarl edseerlrrq qeekdsqmks
     1201 iisrlmavee elkkdhaemq avidakqkii daqvingdei iqtgktdrvp gfsqhqtder
     1261 adpsegavqh agpqwhlphq phqafhhgew
//
LOCUS       NP_001427915             590 aa            linear   PRI 21-NOV-2025
DEFINITION  complement factor I isoform 15 precursor [Homo sapiens].
ACCESSION   NP_001427915 XP_054205914
VERSION     NP_001427915.1
DBSOURCE    REFSEQ: accession NM_001440986.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Moreno,R. and Broderick,L.
  TITLE     Complement factor I deficiency: Diverse phenotypes
  JOURNAL   J Allergy Clin Immunol 156 (2), 305-307 (2025)
   PUBMED   40127737
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Schwotzer,N., Fakhouri,F., Martins,P.V., Delmas,Y., Caillard,S.,
            Zuber,J., Moranne,O., Mesnard,L., Fremeaux-Bacchi,V. and
            El-Sissy,C.
  TITLE     Hot Spot of Complement Factor I Rare Variant p.Ile357Met in
            Patients With Hemolytic Uremic Syndrome
  JOURNAL   Am J Kidney Dis 84 (2), 244-249 (2024)
   PUBMED   38423159
  REMARK    GeneRIF: Hot Spot of Complement Factor I Rare Variant p.Ile357Met
            in Patients With Hemolytic Uremic Syndrome.
REFERENCE   3  (residues 1 to 590)
  AUTHORS   Felberg,A., Bienkowski,M., Stokowy,T., Myszczynski,K.,
            Polakiewicz,Z., Kitowska,K., Sadej,R., Mohlin,F., Kuzniewska,A.,
            Kowalska,D., Stasilojc,G., Jongerius,I., Spaapen,R.,
            Mesa-Guzman,M., Montuenga,L.M., Blom,A.M., Pio,R. and Okroj,M.
  TITLE     Elevated expression of complement factor I in lung cancer cells
            associates with shorter survival-Potentially via non-canonical
            mechanism
  JOURNAL   Transl Res 269, 1-13 (2024)
   PUBMED   38395390
  REMARK    GeneRIF: Elevated expression of complement factor I in lung cancer
            cells associates with shorter survival-Potentially via
            non-canonical mechanism.
REFERENCE   4  (residues 1 to 590)
  AUTHORS   Massey,V., Nguyen,C.E., Francois,T., De Bruycker,J.J., Bonnefoy,A.,
            Lapeyraque,A.L. and Decaluwe,H.
  TITLE     CNS Inflammation as the First Sign of Complement Factor I
            Deficiency: A Severe Myelitis Treated With Intense Immunotherapy
            and Eculizumab
  JOURNAL   Neurol Neuroimmunol Neuroinflamm 11 (2), e200191 (2024)
   PUBMED   38134378
  REMARK    GeneRIF: CNS Inflammation as the First Sign of Complement Factor I
            Deficiency.
REFERENCE   5  (residues 1 to 590)
  AUTHORS   van de Ven,J.P., Nilsson,S.C., Tan,P.L., Buitendijk,G.H.,
            Ristau,T., Mohlin,F.C., Nabuurs,S.B., Schoenmaker-Koller,F.E.,
            Smailhodzic,D., Campochiaro,P.A., Zack,D.J., Duvvari,M.R.,
            Bakker,B., Paun,C.C., Boon,C.J., Uitterlinden,A.G., Liakopoulos,S.,
            Klevering,B.J., Fauser,S., Daha,M.R., Katsanis,N., Klaver,C.C.,
            Blom,A.M., Hoyng,C.B. and den Hollander,A.I.
  TITLE     A functional variant in the CFI gene confers a high risk of
            age-related macular degeneration
  JOURNAL   Nat Genet 45 (7), 813-817 (2013)
   PUBMED   23685748
  REMARK    GeneRIF: these findings demonstrate that rare, highly penetrant
            mutations in CFI contribute to the genetic burden of age-related
            macular degeneration.
REFERENCE   6  (residues 1 to 590)
  AUTHORS   Martin,B. and Smith,R.J.H.
  TITLE     C3 Glomerulopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301598
REFERENCE   7  (residues 1 to 590)
  AUTHORS   Noris,M., Bresin,E., Mele,C. and Remuzzi,G.
  TITLE     Genetic Atypical Hemolytic-Uremic Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301541
REFERENCE   8  (residues 1 to 590)
  AUTHORS   DiScipio,R.G.
  TITLE     Ultrastructures and interactions of complement factors H and I
  JOURNAL   J Immunol 149 (8), 2592-2599 (1992)
   PUBMED   1401896
REFERENCE   9  (residues 1 to 590)
  AUTHORS   Shiang,R., Murray,J.C., Morton,C.C., Buetow,K.H., Wasmuth,J.J.,
            Olney,A.H., Sanger,W.G. and Goldberger,G.
  TITLE     Mapping of the human complement factor I gene to 4q25
  JOURNAL   Genomics 4 (1), 82-86 (1989)
   PUBMED   2563353
REFERENCE   10 (residues 1 to 590)
  AUTHORS   Catterall,C.F., Lyons,A., Sim,R.B., Day,A.J. and Harris,T.J.
  TITLE     Characterization of primary amino acid sequence of human complement
            control protein factor I from an analysis of cDNA clones
  JOURNAL   Biochem J 242 (3), 849-856 (1987)
   PUBMED   2954545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC126283.3.
            
            On Jun 4, 2025 this sequence version replaced XP_054205914.1.
            
            Summary: This gene encodes a serine proteinase that is essential
            for regulating the complement cascade. The encoded preproprotein is
            cleaved to produce both heavy and light chains, which are linked by
            disulfide bonds to form a heterodimeric glycoprotein. This
            heterodimer can cleave and inactivate the complement components C4b
            and C3b, and it prevents the assembly of the C3 and C5 convertase
            enzymes. Defects in this gene cause complement factor I deficiency,
            an autosomal recessive disease associated with a susceptibility to
            pyogenic infections. Mutations in this gene have been associated
            with a predisposition to atypical hemolytic uremic syndrome, a
            disease characterized by acute renal failure, microangiopathic
            hemolytic anemia and thrombocytopenia. Primary glomerulonephritis
            with immune deposits and age-related macular degeneration are other
            conditions associated with mutations of this gene. [provided by
            RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2151473.1,
                                           SRR14038192.1613329.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..590
                     /product="complement factor I isoform 15 precursor"
                     /EC_number="3.4.21.45"
                     /note="C3b-inactivator; Konglutinogen-activating factor;
                     complement factor I heavy chain; complement component I;
                     C3B/C4B inactivator; complement control protein factor I;
                     light chain of factor I"
                     /calculated_mol_wt=64292
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2281
     Region          43..108
                     /region_name="FIMAC"
                     /note="factor I membrane attack complex; smart00057"
                     /db_xref="CDD:214493"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Region          114..215
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     Region          224..256
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(227,235,246..247)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(239,242,246,252..253)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            249..253
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          257..293
                     /region_name="Ldl_recept_a"
                     /note="Low-density lipoprotein receptor domain class A;
                     pfam00057"
                     /db_xref="CDD:395011"
     Site            order(264,272,283..284)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(276,279,283,289..290)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            286..290
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          347..579
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            347
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(387,436,532)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            471
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Site            501
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Site            order(526,552,554)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     Site            543
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     CDS             1..590
                     /gene="CFI"
                     /gene_synonym="AHUS3; ARMD13; C3b-INA; C3BINA; FI; IF;
                     KAF"
                     /coded_by="NM_001440986.1:29..1801"
                     /note="isoform 15 precursor is encoded by transcript
                     variant 15"
                     /db_xref="GeneID:3426"
                     /db_xref="HGNC:HGNC:5394"
                     /db_xref="MIM:217030"
ORIGIN      
        1 mkllhvfllf lcfhlrfckv tytsqedlve kkclakkyth lscdkvfcqp wqrciegtcv
       61 cklpyqcpkn gtavcatnrr sfptycqqks leclhpgtkf lnngtctaeg kfsvslkhgn
      121 tdsegivevk lvdqdktmfi cksswsmrea nvacldlgfq qgadtqrrfk lsdlsinste
      181 clhvhcrgle tslaectftk rrtmgyqdfa dvvcytqkad spmddffqcv ngkyisqmka
      241 cdgindcgdq sdelcckacq gkgfhcksgv cipsqyqcng evdcitgede vgcaarhpti
      301 qgfasvtqee teiltadmda errriksllp klscgvknrm hirrkrivgg kraqlgdlpw
      361 qvaikdasgi tcggiyiggc wiltaahclr askthryqiw ttvvdwihpd lkrivieyvd
      421 riifhenyna gtyqndiali emkkdgnkkd celprsipac vpwspylfqp ndtcivsgwg
      481 rekdnervfs lqwgevklis ncskfygnrf yekemecagt ydgsidackg dsggplvcmd
      541 annvtyvwgv vswgencgkp efpgvytkva nyfdwisyhv grpfisqynv
//
LOCUS       NP_001392220             411 aa            linear   PRI 21-NOV-2025
DEFINITION  F-box/LRR-repeat protein 14 isoform 2 [Homo sapiens].
ACCESSION   NP_001392220
VERSION     NP_001392220.1
DBSOURCE    REFSEQ: accession NM_001405291.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Pitts,S., Liu,H., Ibrahim,A., Garg,A., Felgueira,C.M., Begum,A.,
            Fan,W., Teh,S., Low,J.Y., Ford,B., Schneider,D.A., Hay,R. and
            Laiho,M.
  TITLE     Identification of an E3 ligase that targets the catalytic subunit
            of RNA Polymerase I upon transcription stress
  JOURNAL   J Biol Chem 298 (12), 102690 (2022)
   PUBMED   36372232
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Cui,Y.H., Kang,J.H., Suh,Y., Zhao,Y., Yi,J.M., Bae,I.H., Lee,H.J.,
            Park,D.W., Kim,M.J. and Lee,S.J.
  TITLE     Loss of FBXL14 promotes mesenchymal shift and radioresistance of
            non-small cell lung cancer by TWIST1 stabilization
  JOURNAL   Signal Transduct Target Ther 6 (1), 272 (2021)
   PUBMED   34285182
  REMARK    GeneRIF: Loss of FBXL14 promotes mesenchymal shift and
            radioresistance of non-small cell lung cancer by TWIST1
            stabilization.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Hauri,S., Comoglio,F., Seimiya,M., Gerstung,M., Glatter,T.,
            Hansen,K., Aebersold,R., Paro,R., Gstaiger,M. and Beisel,C.
  TITLE     A High-Density Map for Navigating the Human Polycomb Complexome
  JOURNAL   Cell Rep 17 (2), 583-595 (2016)
   PUBMED   27705803
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Zheng,H., Shen,M., Zha,Y.L., Li,W., Wei,Y., Blanco,M.A., Ren,G.,
            Zhou,T., Storz,P., Wang,H.Y. and Kang,Y.
  TITLE     PKD1 phosphorylation-dependent degradation of SNAIL by SCF-FBXO11
            regulates epithelial-mesenchymal transition and metastasis
  JOURNAL   Cancer Cell 26 (3), 358-373 (2014)
   PUBMED   25203322
REFERENCE   8  (residues 1 to 411)
  AUTHORS   Vinas-Castells,R., Beltran,M., Valls,G., Gomez,I., Garcia,J.M.,
            Montserrat-Sentis,B., Baulida,J., Bonilla,F., de Herreros,A.G. and
            Diaz,V.M.
  TITLE     The hypoxia-controlled FBXL14 ubiquitin ligase targets SNAIL1 for
            proteasome degradation
  JOURNAL   J Biol Chem 285 (6), 3794-3805 (2010)
   PUBMED   19955572
  REMARK    GeneRIF: Data show that Twist1 small interfering RNA prevents
            hypoxia-induced Fbxl14 down-regulation and SNAIL1 stabilization.
REFERENCE   9  (residues 1 to 411)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   10 (residues 1 to 411)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005182.2 and AC004671.1.
            
            Summary: Members of the F-box protein family, such as FBXL14, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.181036.1,
                                           SRR14038196.246649.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..411
                     /product="F-box/LRR-repeat protein 14 isoform 2"
                     /note="F-box/LRR-repeat protein 14"
                     /calculated_mol_wt=45087
     Region          2..48
                     /region_name="Required for down-regulation of SNAI1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1E6.1)"
     Region          6..46
                     /region_name="F-box_FBXL14"
                     /note="F-box domain found in F-box/LRR-repeat protein 14
                     (FBXL14) and similar proteins; cd22125"
                     /db_xref="CDD:438897"
     Site            order(8,12,15..16,19..20,24,26..27,31..33,35)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438897"
     Region          90..296
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          92..118
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          119..142
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          144..163
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1E6.1)"
     Region          145..170
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          170..191
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1E6.1)"
     Region          171..203
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          203..225
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1E6.1)"
     Region          204..229
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          228..395
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          229..250
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1E6.1)"
     Region          230..254
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          254..275
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1E6.1)"
     Region          255..280
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          281..306
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          307..331
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          332..357
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          358..382
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..411
                     /gene="FBXL14"
                     /gene_synonym="Fbl14"
                     /coded_by="NM_001405291.1:777..2012"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:144699"
                     /db_xref="HGNC:HGNC:28624"
                     /db_xref="MIM:609081"
ORIGIN      
        1 methisclfp ellamifgyl dvrdkgraaq vctawrdaay hksvwrgvea klhlrranps
       61 lfpslqargi rrvqilslrr slsyviqgma nieslnlsgc ynltdnglgh afvqeigslr
      121 alnlslckqi tdsslgriaq ylkglevlel ggcsnitntg llliawglqr lkslnlrscr
      181 hlsdvgighl agmtrsaaeg clgleqltlq dcqkltdlsl khisrgltgl rllnlsfcgg
      241 isdagllhls hmgslrslnl rscdnisdtg imhlamgslr lsgldvsfcd kvgdqslayi
      301 aqgldglksl slcschisdd ginrmvrqmh glrtlnigqc vritdkglel iaehlsqltg
      361 idlygctrit krgleritql pclkvlnlgl wqmtdsekvr rhegiflhys l
//
LOCUS       NP_001424954             564 aa            linear   PRI 21-NOV-2025
DEFINITION  proto-oncogene c-Rel isoform 3 [Homo sapiens].
ACCESSION   NP_001424954 XP_016860116 XP_054199242
VERSION     NP_001424954.1
DBSOURCE    REFSEQ: accession NM_001438025.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   5  (residues 1 to 564)
  AUTHORS   Neumann,M., Tsapos,K., Scheppler,J.A., Ross,J. and Franza,B.R. Jr.
  TITLE     Identification of complex formation between two intracellular
            tyrosine kinase substrates: human c-Rel and the p105 precursor of
            p50 NF-kappa B
  JOURNAL   Oncogene 7 (11), 2095-2104 (1992)
   PUBMED   1437141
REFERENCE   6  (residues 1 to 564)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
REFERENCE   7  (residues 1 to 564)
  AUTHORS   Ruben,S.M., Klement,J.F., Coleman,T.A., Maher,M., Chen,C.H. and
            Rosen,C.A.
  TITLE     I-Rel: a novel rel-related protein that inhibits NF-kappa B
            transcriptional activity
  JOURNAL   Genes Dev 6 (5), 745-760 (1992)
   PUBMED   1577270
REFERENCE   8  (residues 1 to 564)
  AUTHORS   Kochel,T. and Rice,N.R.
  TITLE     v-rel- and c-rel-protein complexes bind to the NF-kappa B site in
            vitro
  JOURNAL   Oncogene 7 (3), 567-572 (1992)
   PUBMED   1549370
REFERENCE   9  (residues 1 to 564)
  AUTHORS   Brownell,E., Mittereder,N. and Rice,N.R.
  TITLE     A human rel proto-oncogene cDNA containing an Alu fragment as a
            potential coding exon
  JOURNAL   Oncogene 4 (7), 935-942 (1989)
   PUBMED   2666912
REFERENCE   10 (residues 1 to 564)
  AUTHORS   Brownell,E., Kozak,C.A., Fowle,J.R. 3rd, Modi,W.S., Rice,N.R. and
            O'Brien,S.J.
  TITLE     Comparative genetic mapping of cellular rel sequences in man,
            mouse, and the domestic cat
  JOURNAL   Am J Hum Genet 39 (2), 194-202 (1986)
   PUBMED   3529946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010733.8.
            
            On or before Apr 15, 2025 this sequence version replaced
            XP_016860116.1, XP_054199242.1.
            
            Summary: This gene encodes a protein that belongs to the Rel
            homology domain/immunoglobulin-like fold, plexin, transcription
            factor (RHD/IPT) family. Members of this family regulate genes
            involved in apoptosis, inflammation, the immune response, and
            oncogenic processes. This proto-oncogene plays a role in the
            survival and proliferation of B lymphocytes. Mutation or
            amplification of this gene is associated with B-cell lymphomas,
            including Hodgkin's lymphoma. Single nucleotide polymorphisms in
            this gene are associated with susceptibility to ulcerative colitis
            and rheumatoid arthritis. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Apr 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3279964.1,
                                           SRR11853567.16678.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.1"
     Protein         1..564
                     /product="proto-oncogene c-Rel isoform 3"
                     /note="proto-oncogene c-Rel; oncogene REL, avian
                     reticuloendotheliosis; v-rel avian reticuloendotheliosis
                     viral oncogene homolog"
                     /calculated_mol_wt=62494
     Region          8..179
                     /region_name="RHD-n_c-Rel"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of c-Rel; cd07933"
                     /db_xref="CDD:143649"
     Site            order(22,24..25,27..28,31,111..112,179)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143649"
     Region          186..281
                     /region_name="IPT_NFkappaB"
                     /note="IPT domain of the transcription factor NFkappaB and
                     related transcription factors. NFkappaB is considered a
                     central regulator of stress responses, activated by
                     different stressful conditions, including physical stress,
                     oxidative stress, and exposure to...; cd01177"
                     /db_xref="CDD:238582"
     Site            order(187,189..191,193..195,230..232,245,256,275,278,280)
                     /site_type="other"
                     /note="ankyrin protein binding site [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(189..190,192,205,207,209,237..238,241,243)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(210,212,238..239)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238582"
     CDS             1..564
                     /gene="REL"
                     /gene_synonym="C-Rel; HIVEN86A; IMD92"
                     /coded_by="NM_001438025.1:268..1962"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:5966"
                     /db_xref="HGNC:HGNC:9954"
                     /db_xref="MIM:164910"
ORIGIN      
        1 masgaynpyi eiieqprqrg mrfrykcegr sagsipgehs tdnnrtypsi qimnyygkgk
       61 vritlvtknd pykphphdlv gkdcrdgyye aefgqerrpl ffqnlgircv kkkevkeaii
      121 trikaginpf nvpekqlndi edcdlnvvrl cfqvflpdeh gnlttalppv vsnpiydnra
      181 pntaelricr vnkncgsvrg gdeifllcdk vqkddievrf vlndweakgi fsqadvhrqv
      241 aivfktppyc kaitepvtvk mqlrrpsdqe vsesmdfryl pdekdtygnk akkqkttllf
      301 qklcqdhepn lfshdavvre mptgvssqae syypspgpis sglshhasma plpssswssv
      361 ahptprsgnt nplssfstrt lpsnsqgipp flripvgndl nasnaciynn addivgmeas
      421 smpsadlygi sdpnmlsncs vnmmttssds mgetdnprll smnlenpscn svldprdlrq
      481 lhqmssssms agansnttvf vsqsdafegs dfscadnsmi nesgpsnstn pnshgfvqds
      541 qysgigsmqn eqlsdsfpye ffqv
//
LOCUS       NP_001392592            1139 aa            linear   PRI 21-NOV-2025
DEFINITION  phospholipid-transporting ATPase IH isoform e [Homo sapiens].
ACCESSION   NP_001392592
VERSION     NP_001392592.1
DBSOURCE    REFSEQ: accession NM_001405663.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1139)
  AUTHORS   Higuchi,T., Oka,S., Furukawa,H., Shimada,K., Tsunoda,S., Ito,S.,
            Okamoto,A., Fujimori,M., Nakamura,T., Katayama,M., Saisho,K.,
            Shinohara,S., Matsui,T., Migita,K., Nagaoka,S. and Tohma,S.
  TITLE     Association of a Single Nucleotide Variant in TERT with Airway
            Disease in Japanese Rheumatoid Arthritis Patients
  JOURNAL   Genes (Basel) 14 (11), 2084 (2023)
   PUBMED   38003027
  REMARK    GeneRIF: Association of a Single Nucleotide Variant in TERT with
            Airway Disease in Japanese Rheumatoid Arthritis Patients.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1139)
  AUTHORS   Chepurwar,S., von Loh,S.M., Wigger,D.C., Neef,J., Frommolt,P.,
            Beutner,D., Lang-Roth,R., Kubisch,C., Strenzke,N. and Volk,A.E.
  TITLE     A mutation in ATP11A causes autosomal-dominant auditory neuropathy
            type 2
  JOURNAL   Hum Mol Genet 32 (7), 1083-1089 (2023)
   PUBMED   36300302
  REMARK    GeneRIF: A mutation in ATP11A causes autosomal-dominant auditory
            neuropathy type 2.
REFERENCE   3  (residues 1 to 1139)
  AUTHORS   Miyata,Y., Yamada,K., Nagata,S. and Segawa,K.
  TITLE     Two types of type IV P-type ATPases independently re-establish the
            asymmetrical distribution of phosphatidylserine in plasma membranes
  JOURNAL   J Biol Chem 298 (11), 102527 (2022)
   PUBMED   36162506
REFERENCE   4  (residues 1 to 1139)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   5  (residues 1 to 1139)
  AUTHORS   Pater,J.A., Penney,C., O'Rielly,D.D., Griffin,A., Kamal,L.,
            Brownstein,Z., Vona,B., Vinkler,C., Shohat,M., Barel,O.,
            French,C.R., Singh,S., Werdyani,S., Burt,T., Abdelfatah,N.,
            Houston,J., Doucette,L.P., Squires,J., Glaser,F., Roslin,N.M.,
            Vincent,D., Marquis,P., Woodland,G., Benoukraf,T., Hawkey-Noble,A.,
            Avraham,K.B., Stanton,S.G. and Young,T.L.
  TITLE     Autosomal dominant non-syndromic hearing loss maps to DFNA33
            (13q34) and co-segregates with splice and frameshift variants in
            ATP11A, a phospholipid flippase gene
  JOURNAL   Hum Genet 141 (3-4), 431-444 (2022)
   PUBMED   35278131
  REMARK    GeneRIF: Autosomal dominant non-syndromic hearing loss maps to
            DFNA33 (13q34) and co-segregates with splice and frameshift
            variants in ATP11A, a phospholipid flippase gene.
REFERENCE   6  (residues 1 to 1139)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 1139)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   8  (residues 1 to 1139)
  AUTHORS   Andrew Nesbit,M., Bowl,M.R., Harding,B., Schlessinger,D.,
            Whyte,M.P. and Thakker,R.V.
  TITLE     X-linked hypoparathyroidism region on Xq27 is evolutionarily
            conserved with regions on 3q26 and 13q34 and contains a novel
            P-type ATPase
  JOURNAL   Genomics 84 (6), 1060-1070 (2004)
   PUBMED   15533723
REFERENCE   9  (residues 1 to 1139)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
REFERENCE   10 (residues 1 to 1139)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139384.17, AL356752.13 and
            AL356740.19.
            
            Summary: The protein encoded by this gene is an integral membrane
            ATPase. The encoded protein is probably phosphorylated in its
            intermediate state and likely drives the transport of ions such as
            calcium across membranes. [provided by RefSeq, Apr 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3007954.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1139
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..1139
                     /product="phospholipid-transporting ATPase IH isoform e"
                     /EC_number="7.6.2.1"
                     /note="probable phospholipid-transporting ATPase IH;
                     potential phospholipid-transporting ATPase IH;
                     phospholipid-translocating ATPase; P4-ATPase flippase
                     complex alpha subunit ATP11A; ATPase, class VI, type 11A"
                     /calculated_mol_wt=130223
     Region          47..983
                     /region_name="P-type_ATPase_APLT_Dnf-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2,
                     -10D, -11B, -11C; cd02073"
                     /db_xref="CDD:319770"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            89..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            297..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            350..372
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            order(414..416,553,576..578,640,687..689,798,801,804,825,
                     828)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     Site            457..458
                     /site_type="cleavage"
                     /note="Cleavage, by CASP3.
                     /evidence=ECO:0000269|PubMed:26567335; propagated from
                     UniProtKB/Swiss-Prot (P98196.3)"
     Site            490..491
                     /site_type="cleavage"
                     /note="Cleavage, by CASP3.
                     /evidence=ECO:0000269|PubMed:26567335; propagated from
                     UniProtKB/Swiss-Prot (P98196.3)"
     Site            738
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P98196.3)"
     Site            882..902
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            915..934
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            965..986
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            1001..1023
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            1030..1050
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     Site            1069..1093
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98196.3)"
     CDS             1..1139
                     /gene="ATP11A"
                     /gene_synonym="ATPIH; ATPIS; AUNA2; DFNA84; HLD24"
                     /coded_by="NM_001405663.1:380..3799"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="GeneID:23250"
                     /db_xref="HGNC:HGNC:13552"
                     /db_xref="MIM:605868"
ORIGIN      
        1 mdcslvrtlv hrycageenw vdsrtiyvgh repppgaeay ipqrypdnri vsskytfwnf
       61 ipknlfeqfr rvanfyflii flvqliidtp tspvtsglpl ffvitvtaik qgyedwlrhk
      121 adnamnqcpv hfiqhgklvr kqsrklrvgd ivmvkedetf pcdliflssn rgdgtchvtt
      181 asldgesshk thyavqdtkg fhteediggl hatieceqpq pdlykfvgri nvysdlndpv
      241 vrplgsenll lrgatlknte kifgvaiytg metkmalnyq sksqkrsave ksmnaflivy
      301 lciliskali ntvlkymwqs epfrdepwyn qkteserqrn lflkaftdfl afmvlfnyii
      361 pvsmyvtvem qkflgsyfit wdedmfdeet gegplvntsd lneelgqvey iftdktgtlt
      421 ennmefkecc ieghvyvphv icngqvlpes sgidmidssp svngrereel ffralclcht
      481 vqvkdddsvd gprkspdggk scvyissspd evalvegvqr lgftylrlkd nymeilnren
      541 hierfellei lsfdsvrrrm svivksatge iylfckgads sifprviegk vdqirarver
      601 naveglrtlc vaykrliqee yegickllqa akvalqdrek klaeayeqie kdltllgata
      661 vedrlqekaa dtiealqkag ikvwvltgdk metaaatcya cklfrrntql lelttkriee
      721 qslhdvlfel sktvlrhsgs ltrdnlsgls admqdyglii dgaalslimk predgssgny
      781 relfleicrs csavlccrma plqkaqivkl ikfskehpit laigdgandv smileahvgi
      841 gvigkegrqa arnsdyaipk fkhlkkmllv hghfyyiris elvqyffykn vcfifpqfly
      901 qffcgfsqqt lydtayltly nisftslpil lyslmeqhvg idvlkrdptl yrdvaknall
      961 rwrvfiywtl lglfdalvff fgayfvfent tvtsngqifg nwtfgtlvft vmvftvtlkl
     1021 aldthywtwi nhfviwgsll fyvvfsllwg gviwpflnyq rmyyvfiqml ssgpawlaiv
     1081 llvtisllpd vlkkvlcrql wptatervqr gvkhkapvqa aqssdgpllk dllrrprrs
//
LOCUS       NP_001427978            4359 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HUWE1 isoform 3 [Homo sapiens].
ACCESSION   NP_001427978 XP_047297697 XP_054182293
VERSION     NP_001427978.1
DBSOURCE    REFSEQ: accession NM_001441049.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4359)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 4359)
  AUTHORS   Lee,C., Park,S.H. and Yoon,S.K.
  TITLE     The E3 ligase HUWE1 increases the sensitivity of CRC to oxaliplatin
            through TOMM20 degradation
  JOURNAL   Oncogene 43 (9), 636-649 (2024)
   PUBMED   38184713
  REMARK    GeneRIF: The E3 ligase HUWE1 increases the sensitivity of CRC to
            oxaliplatin through TOMM20 degradation.
REFERENCE   3  (residues 1 to 4359)
  AUTHORS   Li,X.X., Xu,J.K., Su,W.J., Wu,H.L., Zhao,K., Zhang,C.M., Chen,X.K.
            and Yang,L.X.
  TITLE     The role of KDM4A-mediated histone methylation on temozolomide
            resistance in glioma cells through the HUWE1/ROCK2 axis
  JOURNAL   Kaohsiung J Med Sci 40 (2), 161-174 (2024)
   PUBMED   37873881
  REMARK    GeneRIF: The role of KDM4A-mediated histone methylation on
            temozolomide resistance in glioma cells through the HUWE1/ROCK2
            axis.
REFERENCE   4  (residues 1 to 4359)
  AUTHORS   Bernassola,F., Karin,M., Ciechanover,A. and Melino,G.
  TITLE     The HECT family of E3 ubiquitin ligases: multiple players in cancer
            development
  JOURNAL   Cancer Cell 14 (1), 10-21 (2008)
   PUBMED   18598940
  REMARK    Review article
REFERENCE   5  (residues 1 to 4359)
  AUTHORS   Zhong,Q., Gao,W., Du,F. and Wang,X.
  TITLE     Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the
            polyubiquitination of Mcl-1 and regulates apoptosis
  JOURNAL   Cell 121 (7), 1085-1095 (2005)
   PUBMED   15989957
  REMARK    GeneRIF: Mule is both required and sufficient for the
            polyubiquitination of Mcl-1; Mule is a unique BH3-containing E3
            ubiquitin ligase apical to Bcl-2 family proteins during DNA
            damage-induced apoptosis
            GeneRIF: Mule (HUWE1) poly-ubiquitinates anti-apoptotic gene Mcl-1.
REFERENCE   6  (residues 1 to 4359)
  AUTHORS   Chen,D., Kon,N., Li,M., Zhang,W., Qin,J. and Gu,W.
  TITLE     ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
  JOURNAL   Cell 121 (7), 1071-1083 (2005)
   PUBMED   15989956
  REMARK    GeneRIF: study modifies the current view of ARF-mediated p53
            activation and reveals that ARF-BP1 is a critical mediator of both
            the p53-independent and p53-dependent tumor suppressor functions of
            ARF
            GeneRIF: Ubiquitin ligase activity of ARF-BP1 (HUWE1) is inhibited
            by Arf.
REFERENCE   7  (residues 1 to 4359)
  AUTHORS   Liu,Z., Oughtred,R. and Wing,S.S.
  TITLE     Characterization of E3Histone, a novel testis ubiquitin protein
            ligase which ubiquitinates histones
  JOURNAL   Mol Cell Biol 25 (7), 2819-2831 (2005)
   PUBMED   15767685
REFERENCE   8  (residues 1 to 4359)
  AUTHORS   Gu,J., Dubner,R., Fornace,A.J. Jr. and Iadarola,M.J.
  TITLE     UREB1, a tyrosine phosphorylated nuclear protein, inhibits p53
            transactivation
  JOURNAL   Oncogene 11 (10), 2175-2178 (1995)
   PUBMED   7478539
REFERENCE   9  (residues 1 to 4359)
  AUTHORS   Turner,G., Gedeon,A. and Mulley,J.
  TITLE     X-linked mental retardation with heterozygous expression and
            macrocephaly: pericentromeric gene localization
  JOURNAL   Am J Med Genet 51 (4), 575-580 (1994)
   PUBMED   7943042
REFERENCE   10 (residues 1 to 4359)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX323845.7 and AC231658.3.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297697.1, XP_054182293.1.
            
            Summary: This gene encodes a protein containing a C-terminal HECT
            (E6AP type E3 ubiquitin protein ligase) domain that functions as an
            E3 ubiquitin ligase. The encoded protein is required for the
            ubiquitination and subsequent degradation of the anti-apoptotic
            protein Mcl1 (myeloid cell leukemia sequence 1 (BCL2-related)).
            This protein also ubiquitinates the p53 tumor suppressor, core
            histones, and DNA polymerase beta. Mutations in this gene are
            associated with Turner type X-linked syndromic cognitive
            disability. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1197174.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..4359
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..4359
                     /product="E3 ubiquitin-protein ligase HUWE1 isoform 3"
                     /EC_number="2.3.2.26"
                     /note="Mcl-1 ubiquitin ligase E3; BJ-HCC-24 tumor antigen;
                     HECT domain protein LASU1; ARF-binding protein 1;
                     URE-binding protein 1; large structure of UREB1; upstream
                     regulatory element-binding protein 1; homologous to E6AP
                     carboxyl terminus homologous protein 9; HECT-type E3
                     ubiquitin transferase HUWE1; HECT, UBA and WWE domain
                     containing 1, E3 ubiquitin protein ligase"
                     /calculated_mol_wt=480025
     Region          92..367
                     /region_name="DUF908"
                     /note="Domain of Unknown Function (DUF908); pfam06012"
                     /db_xref="CDD:428721"
     Region          431..814
                     /region_name="DUF913"
                     /note="Domain of Unknown Function (DUF913); pfam06025"
                     /db_xref="CDD:461803"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          706..759
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          978..1001
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1014..1037
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1084
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1291..1320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1317..1356
                     /region_name="UBA_HUWE1"
                     /note="UBA domain found in eukaryotic E3 ubiquitin-protein
                     ligase HUWE1 and similar proteins; cd14288"
                     /db_xref="CDD:270474"
     Site            1368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1396..1415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1617..1678
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          1689..1735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1722
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1907
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2018..2065
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2035
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2262..2342
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2267
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2356..2480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2554
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2595
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2694..2970
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          <2735..3066
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            2751
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2826
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2833
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2835
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2861
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2887
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2888
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2889
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2918
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3010..3043
                     /region_name="UBM"
                     /note="Ubiquitin binding region; pfam14377"
                     /db_xref="CDD:464159"
     Region          3036..3059
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3149
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3245..3267
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3404..3424
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3471..3512
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3537..3568
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3555
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3737..3758
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3752
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3757
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3760
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3793
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3801
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3812
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3815
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3879..3916
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3891
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3904
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3909
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3912
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          4004..4357
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(4008,4038,4049,4110,4284,4320..4321,4324..4328,4348,
                     4356)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(4138,4141..4142,4144..4145,4148,4155,4157,
                     4161..4162,4164,4169,4174,4191,4195)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     Site            4256
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P51593; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     CDS             1..4359
                     /gene="HUWE1"
                     /gene_synonym="ARF-BP1; HECTH9; HSPC272; Ib772; LASU1;
                     MRXST; MULE; URE-B1; UREB1"
                     /coded_by="NM_001441049.1:394..13473"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:10075"
                     /db_xref="HGNC:HGNC:30892"
                     /db_xref="MIM:300697"
ORIGIN      
        1 mkvdrtklkk tpteapadcr alidklkvcn deqlllelqq iktwnigkce lyhwvdlldr
       61 fdgiladagq tvenmswmlv cdrpereqlk mlllavlnft allieysfsr hlyssiehlt
      121 tllassdmqv vlavlnllyv fskrsnyitr lgsdkrtpll trlqhlaesw ggkengfgla
      181 eccrdlhmmk yppsattlhf efyadpgaev kiekrttsnt lhyihieqld kisespseim
      241 esltkmysip kdkqmllfth irlahgfsnh rkrlqavqar lhaisilvys nalqesansi
      301 lynglieelv dvlqitdkql meikaaslrt ltsivhlert pklssiidct gtasyhgflp
      361 vlvrnciqam idpsmdpyph qfatalfsfl yhlasydagg ealvscgmme allkvikflg
      421 deqdqitfvt ravrvvdlit nldmaafqsh sglsifiyrl ehevdlcrke cpfvikpkiq
      481 rpnttqegee metdmdgvqc ipqraallks mlnflkkaiq dpafsdgirh vmdgslptsl
      541 khiisnaeyy gpslfllate vvtvfvfqep sllsslqdng ltdvmlhall ikdvpatrev
      601 lgslpnvfsa lclnarglqs fvqcqpferl fkvllspdyl pamrrrrssd plgdtasnlg
      661 savdelmrhq ptlktdatta iiklleeicn lgrdpkyicq kpsiqkadgt atappprsnh
      721 aaeeassede eeeevqamqs fnstqqnete pnqqvvgtee ripiplmdyi lnvmkfvesi
      781 lsnnttddhc qefvnqkgll plvtilglpn lpidfptsaa cqavagvcks iltlshepkv
      841 lqegllqlds ilssleplhr piespggsvl lrelacagnv adatlsaqat pllhaltaah
      901 ayimmfvhtc rvgqseirsi svnqwgsqlg lsvlsklsql ycslvwestv llslctpnsl
      961 psgcefgqad mqklvpkdek agttqggkrs dgeqdgaags mdastqglle gigldgdtla
     1021 pmetdeptas dskgkskitp amaarikqik pllsassrlg ralaelfgll vklcvgspvr
     1081 qrrshhaast ttaptpaars tasaltkllt kglswqpppy tptprfrltf ficsvgftsp
     1141 mlfderkypy hlmlqkflcs gghnalfetf nwalsmggkv pvseglehsd lpdgtgefld
     1201 awlmlvekmv npttvlesph slpaklpggv qnfpqfsalr flvvtqkaaf tciknlwnrk
     1261 plkvyggrma esmlailchi lrgepvirer lskekegsrg eedtgqeegg srrepqvnqq
     1321 qlqqlmdmgf trehameall ntstmeqate yllthpppim ggvvrdlsms eedqmmraia
     1381 mslgqdipmd qraespeeva crkeeeerka rekqeeeeak clekfqdadp leqdelhtft
     1441 dtmlpgcfhl ldelpdtvyr vcdlimtaik rngadyrdmi lkqvvnqvwe aadvlikaal
     1501 plttsdtktv sewisqmatl pqasnlatri llltllfeel klpcawvves sgilnvlikl
     1561 levvqpclqa akeqkevqtp kwitpvllli dfyektaiss krraqmtkyl qsnsnnwrwf
     1621 ddrsgrwcsy sasnnstids awksgetsvr ftagrrrytv qfttmvqvne etgnrrpvml
     1681 tllrvprlnk nsknsngqel ektleeskem dikrkenkgn dtplalestn teketsleet
     1741 kigeiliqgl tedmvtvlir acvsmlgvpv dpdtlhatlr lclrltrdhk yammfaelks
     1801 trmilnltqs sgfngftplv tlllrhiied pctlrhtmek vvrsaatsga gsttsgvvsg
     1861 slgsreinyi lrvlgpaacr npdiftevan ccirialpap rgsgtasdde fenlrikgpn
     1921 avqlvkttpl kpsplpvipd tikeviydml nalaayhape eadksdpkpg vmtqevgqll
     1981 qdmgddvyqq yrsltrqssd fdtqsgfsin sqvfaadgas tetsasgtsq geastpeesr
     2041 dgkkdkegdr aseegkqkgk gskplmptst ilrllaelvr syvgiatlia nysytvgqse
     2101 likedcsvla fvldhllpht qnaedkdtpa larlflasla aagsgtdaqv alvnevkaal
     2161 gralamaest ekharlqavm ciistimesc pstssfyssa taktqhngmn niirlflkkg
     2221 lvndlarvph sldlsspnma ntvnaalkpl etlsrivnqp sslfgsksas sknkseqdaq
     2281 gasqdsssnq qdpgepgeae vqeedhdvtq tevadgdimd geaetdsvvi agqpevlssq
     2341 emqveneled lidellerdg gsgnstiivs rsgedesqed vlmdeapsnl sqastlqanr
     2401 edsmnildpe deeehtqeed ssgsnededd sqdeeeeeee deeddqedde geegdedddd
     2461 dgsemelded ypdmnasplv rferfdredd liiefdnmfs satdippspg niptthplmv
     2521 rhadhssltl gsgssttrlt qgigrsqrtl rqltantght ihvhypgnrq pnpplilqrl
     2581 lgpsaaadil qlssslplqs rgrarllvgn ddvhiiarsd dellddffhd qstatsqagt
     2641 lssiptaltr wteeckvlda esmhdcvsvv kvsivnhlef lrdeeleerr ekrrkqlaee
     2701 etkitdkgke dkenrdqsaq ctasksndst eqnlsdgtpm pdsypttpss tdaatseske
     2761 tlgtlqssqq qptlptppal gevpqelqsp ageggsstql lmpvepeelg ptrpsgeaet
     2821 tqmelspapt itslsperae dsdaltavss qlegspmdts slasctleea vgdtsaagss
     2881 eqpragsstp gdappavaev qgrsdgsges aqppedsspp assessstrd savaisgads
     2941 rgileeplps tsseeedpla gislpegvdp sflaalpddi rrevlqnqlg irpptrtaps
     3001 tnssapavvg npgvtevspe flaalppaiq eevlaqqrae qqrrelaqna ssdtpmdpvt
     3061 fiqtlpsdlr rsvledmeds vlavmppdia aeaqalrreq earqrqlmhe rlfghsstsa
     3121 lsailrspaf tsrlsgnrgv qytrlavqrg gtfqmggsss hnrpsgsnvd tllrlrgrll
     3181 ldhealscll vllfvdepkl ntsrlhrvlr nlcyhaqtrh wvirsllsil qrsseselci
     3241 etpklttsee kgkksskscg ssshenrpld llhkmeskss nqlswlsvsm daalgcrtni
     3301 fqiqrsggrk htekhasggs tvhihpqaap vvcrhvldtl iqlakvfpsh ftqqrtketn
     3361 cesdrergnk acspcssqss ssgictdfwd llvkldnmnv srkgknsvks vpvsaggege
     3421 tspysleasp lgqlmnmlsh pvirrssllt ekllrllsli sialpenkvs eaqansgsga
     3481 sstttatstt stttttaast tptpptaptp vtsapalvaa taistivvaa sttvttptta
     3541 tttvsisptt kgskspakvs dggssstdfk mvssgltenq lqlsvevlts hscseegled
     3601 aanvllqlsr gdsgtrdtvl klllngarhl gytlckqigt llaelreynl eqqrraqcet
     3661 lspdglpeeq pqttklkgkm qsrfdmaenv vivasqkrpl ggrelqlpsm smltsktstq
     3721 kfflrvlqvi iqlrddtrra nkkakqtgrl gssglgsass iqaavrqlea eadaiiqmse
     3781 ssqseasvrr eespmdvdqp spsaqdtqsi asdgtpqgek ekeerppelp llseqlslde
     3841 lwdmlgeclk eleeshdqha vlvlqpavea fflvhatere skppvrdtre sqlahikdep
     3901 pplspapltp atpssldpff srepssmhis sslppdtqkf lrfaethrtv lnqilrqstt
     3961 hladgpfavl vdyirvldfd vkrkyfrqel erldeglrke dmavhvrrdh vfedsyrelh
     4021 rkspeemknr lyivfegeeg qdaggllrew ymiisremfn pmyalfrtsp gdrvtytinp
     4081 sshcnpnhls yfkfvgriva kavydnrlle cyftrsfykh ilgksvrytd mesedyhfyq
     4141 glvyllendv stlgydltfs tevqefgvce vrdlkpngan ilvteenkke yvhlvcqmrm
     4201 tgairkqlaa flegfyeiip krlisifteq elellisglp tididdlksn teyhkyqsns
     4261 iqiqwfwral rsfdqadrak flqfvtgtsk vplqgfaale gmngiqkfqi hrddrstdrl
     4321 psahtcfnql dlpayesfek lrhmlllaiq ecsegfgla
//
LOCUS       NP_001401621             425 aa            linear   PRI 21-NOV-2025
DEFINITION  nucleolar complex protein 4 homolog isoform 6 [Homo sapiens].
ACCESSION   NP_001401621
VERSION     NP_001401621.1
DBSOURCE    REFSEQ: accession NM_001414692.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Talebi,A., Shahidsales,S., Aliakbarian,M., Pezeshki Rad,M. and
            Kerachian,M.A.
  TITLE     Oncogenic fusion transcript analysis identified ADAP1-NOC4L,
            potentially associated with metastatic colorectal cancer
  JOURNAL   Cancer Med 12 (1), 525-540 (2023)
   PUBMED   35702822
  REMARK    GeneRIF: Oncogenic fusion transcript analysis identified
            ADAP1-NOC4L, potentially associated with metastatic colorectal
            cancer.
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Qin,Y., Li,H., Jia,L., Yan,J., Gao,G.F. and Li,X.
  TITLE     Targeted disruption of Noc4l leads to preimplantation embryonic
            lethality in mice
  JOURNAL   Protein Cell 8 (3), 230-235 (2017)
   PUBMED   28012024
  REMARK    GeneRIF: The results provide the first in vivo genetic evidence
            that Noc4l plays important roles in early embryogenesis in mice.
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Bernstein,K.A., Gallagher,J.E., Mitchell,B.M., Granneman,S. and
            Baserga,S.J.
  TITLE     The small-subunit processome is a ribosome assembly intermediate
  JOURNAL   Eukaryot Cell 3 (6), 1619-1626 (2004)
   PUBMED   15590835
REFERENCE   8  (residues 1 to 425)
  AUTHORS   Milkereit,P., Strauss,D., Bassler,J., Gadal,O., Kuhn,H., Schutz,S.,
            Gas,N., Lechner,J., Hurt,E. and Tschochner,H.
  TITLE     A Noc complex specifically involved in the formation and nuclear
            export of ribosomal 40 S subunits
  JOURNAL   J Biol Chem 278 (6), 4072-4081 (2003)
   PUBMED   12446671
REFERENCE   9  (residues 1 to 425)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC138466.12.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4470835.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.33"
     Protein         1..425
                     /product="nucleolar complex protein 4 homolog isoform 6"
                     /note="nucleolar complex protein 4 homolog; NOC4-like
                     protein; NOC4 protein homolog; nucleolar
                     complex-associated protein 4-like protein"
                     /calculated_mol_wt=48287
     Region          219..361
                     /region_name="CBF"
                     /note="CBF/Mak21 family; pfam03914"
                     /db_xref="CDD:461090"
     CDS             1..425
                     /gene="NOC4L"
                     /gene_synonym="NET49; NOC4; UTP19"
                     /coded_by="NM_001414692.1:185..1462"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:79050"
                     /db_xref="HGNC:HGNC:28461"
                     /db_xref="MIM:612819"
ORIGIN      
        1 mrhryhsccn rlgellghps fqvkelalsa llkfvqlega hplekskweg nylfprelfk
       61 lvvggllspe edqslllsqf reyldyddtr yhtmqaavda varvtgqhpe vppafwnnaf
      121 tllsavslpr reptvssfyv kraelwdtwk vahlkehrrv fqamwlsflk hklplslykk
      181 vllivhdail pqlaqptlmi dfltracdlg galsllalng lfilihkhnl eypdfyrkly
      241 glldpsvfhv kyrarffhla dlflssshlp aylvaafakr larlaltapp eallmvlpfi
      301 cnllrrhpac rvlvhrphgp eldadpydpg eedpaqsral esslwelqal qrhyhpevsk
      361 aasvinqals mpevsiapll eltayeifer dlkkkgpepv plefipaqgl lgrpgelcaq
      421 hftls
//
LOCUS       NP_001425720             567 aa            linear   PRI 21-NOV-2025
DEFINITION  semaphorin-4F isoform 7 precursor [Homo sapiens].
ACCESSION   NP_001425720 XP_047298884 XP_054196169
VERSION     NP_001425720.1
DBSOURCE    REFSEQ: accession NM_001438791.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Fan,Q., Barathi,V.A., Cheng,C.Y., Zhou,X., Meguro,A., Nakata,I.,
            Khor,C.C., Goh,L.K., Li,Y.J., Lim,W., Ho,C.E., Hawthorne,F.,
            Zheng,Y., Chua,D., Inoko,H., Yamashiro,K., Ohno-Matsui,K.,
            Matsuo,K., Matsuda,F., Vithana,E., Seielstad,M., Mizuki,N.,
            Beuerman,R.W., Tai,E.S., Yoshimura,N., Aung,T., Young,T.L.,
            Wong,T.Y., Teo,Y.Y. and Saw,S.M.
  TITLE     Genetic variants on chromosome 1q41 influence ocular axial length
            and high myopia
  JOURNAL   PLoS Genet 8 (6), e1002753 (2012)
   PUBMED   22685421
REFERENCE   5  (residues 1 to 567)
  AUTHORS   Parrinello,S., Noon,L.A., Harrisingh,M.C., Wingfield Digby,P.,
            Rosenberg,L.H., Cremona,C.A., Echave,P., Flanagan,A.M., Parada,L.F.
            and Lloyd,A.C.
  TITLE     NF1 loss disrupts Schwann cell-axonal interactions: a novel role
            for semaphorin 4F
  JOURNAL   Genes Dev 22 (23), 3335-3348 (2008)
   PUBMED   19056885
  REMARK    GeneRIF: Sema4F levels were strongly reduced in a panel of human
            neurofibromas, confirming the relevance of these findings to the
            human disease.
REFERENCE   6  (residues 1 to 567)
  AUTHORS   Ayala,G.E., Dai,H., Powell,M., Li,R., Ding,Y., Wheeler,T.M.,
            Shine,D., Kadmon,D., Thompson,T., Miles,B.J., Ittmann,M.M. and
            Rowley,D.
  TITLE     Cancer-related axonogenesis and neurogenesis in prostate cancer
  JOURNAL   Clin Cancer Res 14 (23), 7593-7603 (2008)
   PUBMED   19047084
REFERENCE   7  (residues 1 to 567)
  AUTHORS   Park,Y.D., Park,D., Bhak,J. and Yang,J.M.
  TITLE     Proteomic approaches to the analysis of atopic dermatitis and new
            insights from interactomics
  JOURNAL   Proteomics Clin Appl 2 (3), 290-300 (2008)
   PUBMED   21136834
REFERENCE   8  (residues 1 to 567)
  AUTHORS   Francks,C., Fisher,S.E., Olson,R.K., Pennington,B.F., Smith,S.D.,
            DeFries,J.C. and Monaco,A.P.
  TITLE     Fine mapping of the chromosome 2p12-16 dyslexia susceptibility
            locus: quantitative association analysis and positional candidate
            genes SEMA4F and OTX1
  JOURNAL   Psychiatr Genet 12 (1), 35-41 (2002)
   PUBMED   11901358
  REMARK    GeneRIF: Fine mapping of the chromosome 2p12-16 dyslexia
            susceptibility candidate gene
REFERENCE   9  (residues 1 to 567)
  AUTHORS   Schultze,W., Eulenburg,V., Lessmann,V., Herrmann,L., Dittmar,T.,
            Gundelfinger,E.D., Heumann,R. and Erdmann,K.S.
  TITLE     Semaphorin4F interacts with the synapse-associated protein
            SAP90/PSD-95
  JOURNAL   J Neurochem 78 (3), 482-489 (2001)
   PUBMED   11483650
REFERENCE   10 (residues 1 to 567)
  AUTHORS   Encinas,J.A., Kikuchi,K., Chedotal,A., de Castro,F., Goodman,C.S.
            and Kimura,T.
  TITLE     Cloning, expression, and genetic mapping of Sema W, a member of the
            semaphorin family
  JOURNAL   Proc Natl Acad Sci U S A 96 (5), 2491-2496 (1999)
   PUBMED   10051670
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007387.4.
            
            On or before Apr 24, 2025 this sequence version replaced
            XP_047298884.1, XP_054196169.1.
            
            Summary: This gene encodes a transmembrane class IV semaphorin
            family protein, which plays a role in neural development. This gene
            may be involved in neurogenesis in prostate cancer, the development
            of neurofibromas, and breast cancer tumorigenesis. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Nov 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1552592.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..567
                     /product="semaphorin-4F isoform 7 precursor"
                     /note="semaphorin M; semaphorin-4F; semaphorin-W; sema
                     domain immunoglobulin domain transmembrane domain (TM) and
                     short cytoplasmic domain (semaphorin) 4F; sema domain,
                     immunoglobulin domain (Ig), transmembrane domain (TM) and
                     short cytoplasmic domain, (semaphorin) 4F"
                     /calculated_mol_wt=59261
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3311
     Region          52..478
                     /region_name="Sema_4F"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 4F (Sema4F); cd11261"
                     /db_xref="CDD:200522"
     Site            order(114..116,139,160,162..163,165,181,184,186,191,223,
                     247..251,253,332..333,369,373,376)
                     /site_type="other"
                     /note="plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200522"
     Site            order(224..225,227,230..232,266,269..271,273,275,299..301,
                     305..306,382,397)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200522"
     Region          479..530
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     CDS             1..567
                     /gene="SEMA4F"
                     /gene_synonym="M-SEMA; m-Sema-M; PRO2353; S4F; SEMAM;
                     SEMAW"
                     /coded_by="NM_001438791.1:131..1834"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 9"
                     /db_xref="GeneID:10505"
                     /db_xref="HGNC:HGNC:10734"
                     /db_xref="MIM:603706"
ORIGIN      
        1 mpasaarprp gpgqptaspf pllllavlsg pvsgrvprsv prtslpisea dscltrfavp
       61 htynysvllv dpashtlyvg ardtifalsl pfsgerprri dwmvpeahrq ncrkkgkked
      121 vsrfqqverl esgrgkcpfe paqrsaavma ggvlyaatvk nylgtepiit ravgraedwi
      181 rtdtlpswln apafvaaval spaewgdedg ddeiyfffte tsrafdsyer ikvprvarvc
      241 agdlggrktl qqrwttflka dllcpgpehg rassvlqdva vlrpelgagt pifygifssq
      301 wegatisavc afrpqdirtv lngpfrelkh dcnrglpvvd ndvpqprpge citnnmklrh
      361 fgsslslpdr vltfirdhpl mdrpvfpadg hpllvttdta ylrvvahrvt slsgkeydvl
      421 ylgtedghlh ravrigaqls vledlalfpe pqpvenmkly hswllvgsrt evtqvnttnc
      481 grlqscseci laqdpvcaws frldecvaha gehrglvqdi esadvsslcp kepggkrpwk
      541 kgnmnlqdss qqnklstcyl ykegggr
//
LOCUS       NP_001425935            1282 aa            linear   PRI 21-NOV-2025
DEFINITION  receptor tyrosine-protein kinase erbB-4 isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001425935 XP_005246434 XP_054196999
VERSION     NP_001425935.1
DBSOURCE    REFSEQ: accession NM_001439006.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1282)
  AUTHORS   Li,X., Zhang,H., Li,W., Tuo,H., He,B. and Jiang,H.
  TITLE     The role and mechanism of NRG1/ErbB4 in inducing the
            differentiation of induced pluripotent stem cells into
            cardiomyocytes
  JOURNAL   BMC Cardiovasc Disord 24 (1), 559 (2024)
   PUBMED   39407109
  REMARK    GeneRIF: The role and mechanism of NRG1/ErbB4 in inducing the
            differentiation of induced pluripotent stem cells into
            cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1282)
  AUTHORS   Singh,P.K., Kim,S. and Smith,A.W.
  TITLE     HER4 is a high-affinity dimerization partner for all EGFR/HER/ErbB
            family proteins
  JOURNAL   Protein Sci 33 (10), e5171 (2024)
   PUBMED   39276020
  REMARK    GeneRIF: HER4 is a high-affinity dimerization partner for all
            EGFR/HER/ErbB family proteins.
REFERENCE   3  (residues 1 to 1282)
  AUTHORS   Adashek,J.J., Pandya,C., Maragakis,N.J., De,P., Cohen,P.R., Kato,S.
            and Kurzrock,R.
  TITLE     Neuregulin-1 and ALS19 (ERBB4): at the crossroads of amyotrophic
            lateral sclerosis and cancer
  JOURNAL   BMC Med 22 (1), 74 (2024)
   PUBMED   38369520
  REMARK    GeneRIF: Neuregulin-1 and ALS19 (ERBB4): at the crossroads of
            amyotrophic lateral sclerosis and cancer.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1282)
  AUTHORS   Li,R., Wang,Y., Yang,L., Zhong,P., Huang,G., Liang,Q. and Yu,X.
  TITLE     Genetic variants of ERBB4 gene and risk of gestational diabetes
            mellitus: a susceptibility and diagnostic nomogram study
  JOURNAL   Front Endocrinol (Lausanne) 14, 1283539 (2023)
   PUBMED   38149095
  REMARK    GeneRIF: Genetic variants of ERBB4 gene and risk of gestational
            diabetes mellitus: a susceptibility and diagnostic nomogram study.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1282)
  AUTHORS   Tang,R., Cui,H., Dou,R., Tao,L., Tan,L., Guo,T. and Luo,D.
  TITLE     ErbB4 affects Th1/Th17 cell differentiation and promotes psoriasis
            progression
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (12), 1-5 (2023)
   PUBMED   38063127
  REMARK    GeneRIF: ErbB4 affects Th1/Th17 cell differentiation and promotes
            psoriasis progression.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1282)
  AUTHORS   Barbacci,E.G., Guarino,B.C., Stroh,J.G., Singleton,D.H.,
            Rosnack,K.J., Moyer,J.D. and Andrews,G.C.
  TITLE     The structural basis for the specificity of epidermal growth factor
            and heregulin binding
  JOURNAL   J Biol Chem 270 (16), 9585-9589 (1995)
   PUBMED   7721889
  REMARK    Erratum:[J Biol Chem 1995 Nov 24;270(47):28494]
REFERENCE   7  (residues 1 to 1282)
  AUTHORS   Zimonjic,D.B., Alimandi,M., Miki,T., Popescu,N.C. and Kraus,M.H.
  TITLE     Localization of the human HER4/erbB-4 gene to chromosome 2
  JOURNAL   Oncogene 10 (6), 1235-1237 (1995)
   PUBMED   7700649
REFERENCE   8  (residues 1 to 1282)
  AUTHORS   Nagata,K., Kohda,D., Hatanaka,H., Ichikawa,S., Matsuda,S.,
            Yamamoto,T., Suzuki,A. and Inagaki,F.
  TITLE     Solution structure of the epidermal growth factor-like domain of
            heregulin-alpha, a ligand for p180erbB-4
  JOURNAL   EMBO J 13 (15), 3517-3523 (1994)
   PUBMED   8062828
REFERENCE   9  (residues 1 to 1282)
  AUTHORS   Culouscou,J.M., Plowman,G.D., Carlton,G.W., Green,J.M. and
            Shoyab,M.
  TITLE     Characterization of a breast cancer cell differentiation factor
            that specifically activates the HER4/p180erbB4 receptor
  JOURNAL   J Biol Chem 268 (25), 18407-18410 (1993)
   PUBMED   7689552
REFERENCE   10 (residues 1 to 1282)
  AUTHORS   Siddique,N. and Siddique,T.
  TITLE     Amyotrophic Lateral Sclerosis Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC096765.3, AC096547.1,
            AC093823.2, AC105921.5, AC068970.6 and AC012069.10.
            
            On or before Apr 25, 2025 this sequence version replaced
            XP_005246434.1, XP_054196999.1.
            
            Summary: This gene is a member of the Tyr protein kinase family and
            the epidermal growth factor receptor subfamily. It encodes a
            single-pass type I membrane protein with multiple cysteine rich
            domains, a transmembrane domain, a tyrosine kinase domain, a
            phosphotidylinositol-3 kinase binding site and a PDZ domain binding
            motif. The protein binds to and is activated by neuregulins and
            other factors and induces a variety of cellular responses including
            mitogenesis and differentiation. Multiple proteolytic events allow
            for the release of a cytoplasmic fragment and an extracellular
            fragment. Mutations in this gene have been associated with cancer.
            Alternatively spliced variants which encode different protein
            isoforms have been described; however, not all variants have been
            fully characterized. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143749.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1282
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..1282
                     /product="receptor tyrosine-protein kinase erbB-4 isoform
                     4 precursor"
                     /EC_number="2.7.10.1"
                     /note="receptor tyrosine-protein kinase erbB-4; tyrosine
                     kinase-type cell surface receptor HER4; avian
                     erythroblastic leukemia viral (v-erb-b2) oncogene homolog
                     4; proto-oncogene-like protein c-ErbB-4; v-erb-a
                     erythroblastic leukemia viral oncogene homolog 4; v-erb-b2
                     avian erythroblastic leukemia viral oncogene homolog 4;
                     human epidermal growth factor receptor 4"
                     /calculated_mol_wt=141662
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2325
     Region          55..167
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Region          186..332
                     /region_name="Furin-like"
                     /note="Furin-like cysteine rich region; pfam00757"
                     /db_xref="CDD:395614"
     Region          358..478
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Region          502..634
                     /region_name="GF_recep_IV"
                     /note="Growth factor receptor domain IV; pfam14843"
                     /db_xref="CDD:464344"
     Region          632..675
                     /region_name="TM_ErbB4"
                     /note="Transmembrane domain of ErbB4, a Protein Tyrosine
                     Kinase; cd12092"
                     /db_xref="CDD:213053"
     Site            order(632..633,635..638,641..642,645..646,649..650,
                     653..654,657,661)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:213053"
     Region          700..1002
                     /region_name="PTKc_HER4"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     HER4; cd05110"
                     /db_xref="CDD:173655"
     Site            order(714..715,722,739,741,762,784,786..787,789,837..838,
                     840,851,872..876,881,885)
                     /site_type="active"
                     /db_xref="CDD:173655"
     Site            order(714..715,722,739,741,762,784,786..787,789,837..838,
                     840,851)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173655"
     Site            850..875
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173655"
     Site            order(872..876,881,885)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173655"
     CDS             1..1282
                     /gene="ERBB4"
                     /gene_synonym="ALS19; HER4; p180erbB4"
                     /coded_by="NM_001439006.1:273..4121"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:2066"
                     /db_xref="HGNC:HGNC:3432"
                     /db_xref="MIM:600543"
ORIGIN      
        1 mkpatglwvw vsllvaagtv qpsdsqsvca gtenklssls dleqqyralr kyyencevvm
       61 gnleitsieh nrdlsflrsv revtgyvlva lnqfrylple nlriirgtkl yedryalaif
      121 lnyrkdgnfg lqelglknlt eilnggvyvd qnkflcyadt ihwqdivrnp wpsnltlvst
      181 ngssgcgrch ksctgrcwgp tenhcqtltr tvcaeqcdgr cygpyvsdcc hrecaggcsg
      241 pkdtdcfacm nfndsgacvt qcpqtfvynp ttfqlehnfn akytygafcv kkcphnfvvd
      301 ssscvracps skmeveengi kmckpctdic pkacdgigtg slmsaqtvds snidkfinct
      361 kingnliflv tgihgdpyna ieaidpekln vfrtvreitg flniqswppn mtdfsvfsnl
      421 vtiggrvlys glsllilkqq gitslqfqsl keisagniyi tdnsnlcyyh tinwttlfst
      481 inqrivirdn rkaenctaeg mvcnhlcssd gcwgpgpdqc lscrrfsrgr iciescnlyd
      541 gefrefengs icvecdpqce kmedglltch gpgpdnctkc shfkdgpncv ekcpdglqga
      601 nsfifkyadp drechpchpn ctqgcigssi edciglmdrt pliaagvigg lfilvivglt
      661 favyvrrksi kkkralrrfl etelvepltp sgtapnqaql rilketelkr vkvlgsgafg
      721 tvykgiwvpe getvkipvai kilnettgpk anvefmdeal imasmdhphl vrllgvclsp
      781 tiqlvtqlmp hgclleyvhe hkdnigsqll lnwcvqiakg mmyleerrlv hrdlaarnvl
      841 vkspnhvkit dfglarlleg dekeynadgg kmpikwmale cihyrkfthq sdvwsygvti
      901 welmtfggkp ydgiptreip dllekgerlp qppictidvy mvmvkcwmid adsrpkfkel
      961 aaefsrmard pqrylviqgd drmklpspnd skffqnllde edledmmdae eylvpqafni
     1021 pppiytsrar idsnrnqfvy rdggfaaeqg vsvpyrapts tipeapvaqg ataeifddsc
     1081 cngtlrkpva phvqedsstq rysadptvfa persprgeld eegymtpmrd kpkqeylnpv
     1141 eenpfvsrrk ngdlqaldnp eyhnasngpp kaedeyvnep lylntfantl gkaeylknni
     1201 lsmpekakka fdnpdywnhs lpprstlqhp dylqeystky fykqngrirp ivaenpeyls
     1261 efslkpgtvl ppppyrhrnt vv
//
LOCUS       NP_001427682             528 aa            linear   PRI 21-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform o [Homo sapiens].
ACCESSION   NP_001427682 XP_047287593 XP_054232485
VERSION     NP_001427682.1
DBSOURCE    REFSEQ: accession NM_001440753.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 528)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 528)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 528)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 528)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 528)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 528)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            On or before May 28, 2025 this sequence version replaced
            XP_047287593.1, XP_054232485.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3398148.1,
                                           SRR18074967.1839401.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..528
                     /product="lysosomal cobalamin transporter ABCD4 isoform o"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=59404
     Region          27..294
                     /region_name="ABC_membrane_2"
                     /note="ABC transporter transmembrane region 2; pfam06472"
                     /db_xref="CDD:399466"
     Site            43..63
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Site            76..96
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Site            190..210
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Site            279..299
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Site            314..334
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Region          387..>488
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            421..428
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213190"
     Site            458..461
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213190"
     CDS             1..528
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_001440753.1:23..1609"
                     /note="isoform o is encoded by transcript variant 36"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 mavagpapga garprldlqf lqrflqilkv lfpswssqna lmfltllclt lleqfviyqv
       61 glipsqyygv lgnkdlegfk tltflavmli vlnstlksfd qftcnllyvs wrkdltehlh
      121 rlyfrgrayy tlnvlrddid npdqrisqdv erfcrqlssm askliispft lvyytyqcfq
      181 stgwlgpvsi fgyfilgtvv nktlmgpivm klvhqekleg dfrfkhmqir vnaepaafyr
      241 aghvehmrtd rrlqrllqtq relmskelwl yigintfdyl gsilsyvvia ipifsgvygd
      301 lspaelstlv sknafvciyl iscftqlidl sttlsdvagy thrigqlret lldmslksqd
      361 ceilgesewg ldtppgwpaa epadtaflle rvsisapssd kplikdlslk isegqsllit
      421 gntgtgktsl lrvlgglwts trgsvqmltd fgphgvlflp qkpfftdgtl reqviyplke
      481 vypdsgempt gtrkvmpsft hpfpyedlqp vvskpspsil rppplhhp
//
LOCUS       NP_001337426             298 aa            linear   PRI 21-NOV-2025
DEFINITION  cyclin-L2 isoform C [Homo sapiens].
ACCESSION   NP_001337426 XP_011540523
VERSION     NP_001337426.1
DBSOURCE    REFSEQ: accession NM_001350497.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Wang,C., Xu,L., Du,C., Yun,H., Wang,K., Liu,H., Ye,M., Fan,J.,
            Zhou,Y. and Cheng,H.
  TITLE     CDK11 requires a critical activator SAP30BP to regulate pre-mRNA
            splicing
  JOURNAL   EMBO J 42 (24), e114051 (2023)
   PUBMED   38059508
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Hluchy,M., Gajduskova,P., Ruiz de Los Mozos,I., Rajecky,M.,
            Kluge,M., Berger,B.T., Slaba,Z., Potesil,D., Weiss,E., Ule,J.,
            Zdrahal,Z., Knapp,S., Paruch,K., Friedel,C.C. and Blazek,D.
  TITLE     CDK11 regulates pre-mRNA splicing by phosphorylation of SF3B1
  JOURNAL   Nature 609 (7928), 829-834 (2022)
   PUBMED   36104565
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Wu,C., Zhu,Q., Yao,Y., Shi,Z., Jin,C. and Chen,L.
  TITLE     Exosome miR-23a-3p from Osteoblast Alleviates Spinal Cord
            Ischemia/Reperfusion Injury by Down-Regulating KLF3-Activated CCNL2
            Transcription
  JOURNAL   Dev Neurosci 44 (3), 121-130 (2022)
   PUBMED   34937039
  REMARK    GeneRIF: Exosome miR-23a-3p from Osteoblast Alleviates Spinal Cord
            Ischemia/Reperfusion Injury by Down-Regulating KLF3-Activated CCNL2
            Transcription.
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 298)
  AUTHORS   Loyer,P., Trembley,J.H., Grenet,J.A., Busson,A., Corlu,A., Zhao,W.,
            Kocak,M., Kidd,V.J. and Lahti,J.M.
  TITLE     Characterization of cyclin L1 and L2 interactions with CDK11 and
            splicing factors: influence of cyclin L isoforms on splice site
            selection
  JOURNAL   J Biol Chem 283 (12), 7721-7732 (2008)
   PUBMED   18216018
  REMARK    GeneRIF: CDK11(p110) interacts physically and functionally with
            cyclin Lalpha and -beta isoforms and SR proteins to regulate
            splicing.
REFERENCE   7  (residues 1 to 298)
  AUTHORS   de Graaf,K., Hekerman,P., Spelten,O., Herrmann,A., Packman,L.C.,
            Bussow,K., Muller-Newen,G. and Becker,W.
  TITLE     Characterization of cyclin L2, a novel cyclin with an
            arginine/serine-rich domain: phosphorylation by DYRK1A and
            colocalization with splicing factors
  JOURNAL   J Biol Chem 279 (6), 4612-4624 (2004)
   PUBMED   14623875
  REMARK    GeneRIF: characterize cyclin L2 as a highly mobile component of
            nuclear speckles and suggest that DYRK1A may regulate splicing by
            phosphorylation of cyclin L2
REFERENCE   8  (residues 1 to 298)
  AUTHORS   Edelheit,S. and Meiri,N.
  TITLE     Cyclin S: a new member of the cyclin family plays a role in
            long-term memory
  JOURNAL   Eur J Neurosci 19 (2), 365-375 (2004)
   PUBMED   14725631
REFERENCE   9  (residues 1 to 298)
  AUTHORS   Cheng,H. and Bjerknes,M.
  TITLE     Patterns of gene expression along the crypt-villus axis in mouse
            jejunal epithelium
  JOURNAL   Anat Rec 244 (1), 78-94 (1996)
   PUBMED   8838426
REFERENCE   10 (residues 1 to 298)
  AUTHORS   Bunnell,B.A., Heath,L.S., Adams,D.E., Lahti,J.M. and Kidd,V.J.
  TITLE     Increased expression of a 58-kDa protein kinase leads to changes in
            the CHO cell cycle
  JOURNAL   Proc Natl Acad Sci U S A 87 (19), 7467-7471 (1990)
   PUBMED   2217177
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1991 Mar 15;88(6):2612]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL391244.11 and CR628411.1.
            
            On Apr 15, 2017 this sequence version replaced XP_011540523.1.
            
            Summary: The protein encoded by this gene belongs to the cyclin
            family. Through its interaction with several proteins, such as RNA
            polymerase II, splicing factors, and cyclin-dependent kinases, this
            protein functions as a regulator of the pre-mRNA splicing process,
            as well as in inducing apoptosis by modulating the expression of
            apoptotic and antiapoptotic proteins. Alternatively spliced
            transcript variants encoding different isoforms have been described
            for this gene. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (6) has multiple differences,
            compared to variant 1. These differences cause translation
            initiation at a downstream start codon, compared to variant 1. The
            resulting isoform (C) is shorter at the N-terminus compared to
            isoform A. Variants 3, 4, 6, and 7 encode the same isoform (C).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3690242.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154405 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.33"
     Protein         1..298
                     /product="cyclin-L2 isoform C"
                     /note="cyclin M; paneth cell-enhanced expression protein;
                     cyclin S"
                     /calculated_mol_wt=33708
     Region          <1..95
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cl40454"
                     /db_xref="CDD:477360"
     CDS             1..298
                     /gene="CCNL2"
                     /gene_synonym="ANIA-6B; CCNM; CCNS; HCLA-ISO; HLA-ISO;
                     PCEE; SB138"
                     /coded_by="NM_001350497.2:844..1740"
                     /note="isoform C is encoded by transcript variant 6"
                     /db_xref="GeneID:81669"
                     /db_xref="HGNC:HGNC:20570"
                     /db_xref="MIM:613482"
ORIGIN      
        1 mndslrtdvf vrfqpesiac aciylaartl eiplpnrphw fllfgateee iqeiclkilq
       61 lyarkkvdlt hlegevekrk haieeakaqa rgllpggtqv ldgtsgfspa pklvespkeg
      121 kgskpsplsv kntkrrlega kkakadspvn glpkgresrs rsrsreqsys rspsrsaspk
      181 rrksdsgsts ggsksqsrsr srsdspprqa prsapykgse irgsrkskdc kypqkphksr
      241 srsssrsrsr sreradnpgk ykkkshyyrd qrrersrsye rtgrryerdh pghsrhrr
//
LOCUS       NP_001393919             500 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform J [Homo sapiens].
ACCESSION   NP_001393919
VERSION     NP_001393919.1
DBSOURCE    REFSEQ: accession NM_001406990.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 500)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 500)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 500)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 500)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 500)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 500)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 500)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 500)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1362093.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..500
                     /product="lamin isoform J"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=55831
     Region          <1..200
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          248..355
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     CDS             1..500
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406990.1:610..2112"
                     /note="isoform J is encoded by transcript variant 17"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 mlrrvdaenr lqtmkeeldf qkniyseelr etkrrhetrl veidngkqre fesrladalq
       61 elraqhedqv eqykkelekt ysakldnarq saernsnlvg aaheelqqsr iridslsaql
      121 sqlqkqlaak eaklrdleds larerdtsrr llaekerema emrarmqqql deyqelldik
      181 laldmeihay rkllegeeer lrlspsptsq rsrgrasshs sqtqgggsvt kkrklestes
      241 rssfsqhart sgrvaveevd eegkfvrlrn ksnedqsmgn wqikrqngdd plltyrfppk
      301 ftlkagqvvt iwaagagath spptdlvwka qntwgcgnsl rtalinstge evamrklvrs
      361 vtvveddede dgddllhhhh gshcsssgdp aeynlrsrtv lcgtcgqpad kasasgsgaq
      421 vggpissgss assvtvtrsy rsvggsgggs fgdnlvtrsy llgnssprtq spqncsiiqe
      481 mgmrweveeg rrkvslsclp
//
LOCUS       NP_001424676             519 aa            linear   PRI 21-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 11 [Homo sapiens].
ACCESSION   NP_001424676
VERSION     NP_001424676.1
DBSOURCE    REFSEQ: accession NM_001437747.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 519)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 519)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 519)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 519)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 519)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 519)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008641.7.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.2089579.1,
                                           SRR14038191.3166610.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..519
                     /product="TNFAIP3-interacting protein 1 isoform 11"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=58516
     Region          <161..>198
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          <245..>476
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..519
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001437747.1:179..1738"
                     /note="isoform 11 is encoded by transcript variant 27"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 meatrlrqka eelvkdnell pppspslgsf dplaeltgkd snvtasptap acpsdkpapv
       61 qkppssgtss efevvtpeeq nspessshan amalgplpre dgnlmlhlqr lettlsvcae
      121 epdhgqlfth lgrmalefnr laskvhkneq rtsilqtlce qlrkenealk akldkgleqr
      181 dqaaerlree nlelkkllms ngnkegasgr pgspkmegtg kkavagqqqa svtagkvpev
      241 valgaaekkv kmleqqrsel levnkqwdqh frsmkqqyeq kitelrqkla dlqkqvtdle
      301 aereqkqrdf drklllaksk iemeetdkeq ltaeakelrq kvkylqdqls pltrqreyqe
      361 keiqrlnkal eealsiqtpp sspptafgsp egagallrkq elvtqnellk qqvkifeedf
      421 qrersdrerm neekeelkkq veklqaqvtl snaqlkafkd eekarealrq qkrkakpeyt
      481 wrlpcggvrn pnqssqvmdp ptarptepes pkndregpq
//
LOCUS       NP_001394257             287 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 29 [Homo sapiens].
ACCESSION   NP_001394257 XP_047288956
VERSION     NP_001394257.1
DBSOURCE    REFSEQ: accession NM_001407328.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 287)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 287)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 287)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            On May 31, 2022 this sequence version replaced XP_047288956.1.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR13170464.102611.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..287
                     /product="tropomyosin alpha-1 chain isoform 29"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=32762
     Region          48..259
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..287
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407328.1:84..947"
                     /note="isoform 29 is encoded by transcript variant 29"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle ediaakekll rvsederdrv
       61 leelhkaeds llaaeeaaak aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegkc aeleeelktv tnnlksleaq aekysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledkf lcftspktps sswmshlsel ciclfss
//
LOCUS       NP_001428017             731 aa            linear   PRI 21-NOV-2025
DEFINITION  fibroblast growth factor receptor 2 isoform 18 precursor [Homo
            sapiens].
ACCESSION   NP_001428017 XP_024303656 XP_054221145
VERSION     NP_001428017.1
DBSOURCE    REFSEQ: accession NM_001441088.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Chen,C.P., Huang,J.P., Huang,K.S., Chen,Y.Y., Wu,F.T., Pan,Y.T.,
            Chiu,C.L. and Wang,W.
  TITLE     Perinatal imaging findings of a fetus with Pfeiffer syndrome and a
            heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation in FGFR2
            presenting a cloverleaf skull, craniosynostosis and short limbs on
            prenatal ultrasound mimicking thanatophoric dysplasia type II
  JOURNAL   Taiwan J Obstet Gynecol 63 (3), 387-390 (2024)
   PUBMED   38802203
  REMARK    GeneRIF: Perinatal imaging findings of a fetus with Pfeiffer
            syndrome and a heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation
            in FGFR2 presenting a cloverleaf skull, craniosynostosis and short
            limbs on prenatal ultrasound mimicking thanatophoric dysplasia type
            II.
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Lian,Y., Bodian,D. and Shehu,A.
  TITLE     Elucidating the Role of Wildtype and Variant FGFR2 Structural
            Dynamics in (Dys)Function and Disorder
  JOURNAL   Int J Mol Sci 25 (8), 4523 (2024)
   PUBMED   38674107
  REMARK    GeneRIF: Elucidating the Role of Wildtype and Variant FGFR2
            Structural Dynamics in (Dys)Function and Disorder.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 731)
  AUTHORS   Xu,N., Hung,K.L., Gong,X., Fan,D., Tian,Y., Yan,M., Wei,Y. and
            Wang,S.
  TITLE     Genetic insights into the 'sandwich fusion' subtype of Klippel-Feil
            syndrome: novel FGFR2 mutations identified by 21 cases of
            whole-exome sequencing
  JOURNAL   Orphanet J Rare Dis 19 (1), 141 (2024)
   PUBMED   38561822
  REMARK    GeneRIF: Genetic insights into the 'sandwich fusion' subtype of
            Klippel-Feil syndrome: novel FGFR2 mutations identified by 21 cases
            of whole-exome sequencing.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 731)
  AUTHORS   Wenger,T.L., Hing,A.V. and Evans,K.N.
  TITLE     Apert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31145570
REFERENCE   5  (residues 1 to 731)
  AUTHORS   Wenger,T., Miller,D. and Evans,K.
  TITLE     FGFR Craniosynostosis Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301628
REFERENCE   6  (residues 1 to 731)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   7  (residues 1 to 731)
  AUTHORS   Dell,K.R. and Williams,L.T.
  TITLE     A novel form of fibroblast growth factor receptor 2. Alternative
            splicing of the third immunoglobulin-like domain confers ligand
            binding specificity
  JOURNAL   J Biol Chem 267 (29), 21225-21229 (1992)
   PUBMED   1400433
REFERENCE   8  (residues 1 to 731)
  AUTHORS   Luqmani,Y.A., Graham,M. and Coombes,R.C.
  TITLE     Expression of basic fibroblast growth factor, FGFR1 and FGFR2 in
            normal and malignant human breast, and comparison with other normal
            tissues
  JOURNAL   Br J Cancer 66 (2), 273-280 (1992)
   PUBMED   1380281
REFERENCE   9  (residues 1 to 731)
  AUTHORS   Katoh,M., Hattori,Y., Sasaki,H., Tanaka,M., Sugano,K., Yazaki,Y.,
            Sugimura,T. and Terada,M.
  TITLE     K-sam gene encodes secreted as well as transmembrane receptor
            tyrosine kinase
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 2960-2964 (1992)
   PUBMED   1313574
REFERENCE   10 (residues 1 to 731)
  AUTHORS   Miki,T., Bottaro,D.P., Fleming,T.P., Smith,C.L., Burgess,W.H.,
            Chan,A.M. and Aaronson,S.A.
  TITLE     Determination of ligand-binding specificity by alternative
            splicing: two distinct growth factor receptors encoded by a single
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 246-250 (1992)
   PUBMED   1309608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009988.12.
            
            On or before Jun 5, 2025 this sequence version replaced
            XP_024303656.1, XP_054221145.1.
            
            Summary: The protein encoded by this gene is a member of the
            fibroblast growth factor receptor family, where amino acid sequence
            is highly conserved between members and throughout evolution. FGFR
            family members differ from one another in their ligand affinities
            and tissue distribution. A full-length representative protein
            consists of an extracellular region, composed of three
            immunoglobulin-like domains, a single hydrophobic membrane-spanning
            segment and a cytoplasmic tyrosine kinase domain. The extracellular
            portion of the protein interacts with fibroblast growth factors,
            setting in motion a cascade of downstream signals, ultimately
            influencing mitogenesis and differentiation. This particular family
            member is a high-affinity receptor for acidic, basic and/or
            keratinocyte growth factor, depending on the isoform. Mutations in
            this gene are associated with Crouzon syndrome, Pfeiffer syndrome,
            Craniosynostosis, Apert syndrome, Jackson-Weiss syndrome,
            Beare-Stevenson cutis gyrata syndrome, Saethre-Chotzen syndrome,
            and syndromic craniosynostosis. Multiple alternatively spliced
            transcript variants encoding different isoforms have been noted for
            this gene. [provided by RefSeq, Jan 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.4531.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:1309608)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..731
                     /product="fibroblast growth factor receptor 2 isoform 18
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="protein tyrosine kinase, receptor like 14;
                     bacteria-expressed kinase; keratinocyte growth factor
                     receptor; BEK fibroblast growth factor receptor"
                     /calculated_mol_wt=79838
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2298
     Region          65..159
                     /region_name="IgI_2_FGFR"
                     /note="Second immunoglobulin (Ig)-like domain of
                     fibroblast growth factor (FGF) receptor; member of the
                     I-set of IgSF domains; cd05857"
                     /db_xref="CDD:409443"
     Region          65..68
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409443"
     Region          76..81
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409443"
     Site            order(77,79,81)
                     /site_type="other"
                     /note="FGF binding site [polypeptide binding]"
                     /db_xref="CDD:409443"
     Site            order(78,85..87,89)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409443"
     Region          85..93
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409443"
     Region          99..104
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409443"
     Region          107..109
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409443"
     Region          118..121
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409443"
     Region          125..130
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409443"
     Region          139..146
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409443"
     Region          149..159
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409443"
     Region          167..269
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          185..189
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          198..202
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          234..238
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          248..253
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          261..264
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          366..678
                     /region_name="PTKc_FGFR2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Fibroblast Growth Factor Receptor 2; cd05101"
                     /db_xref="CDD:270679"
     Site            order(397..398,400,405,425,427,444,474..477,481,536,
                     540..541,543,554,572..576,585,619)
                     /site_type="active"
                     /db_xref="CDD:270679"
     Site            order(397..398,400,405,425,427,444,474..477,481,540..541,
                     543,554)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270679"
     Site            order(536,540,572..576,585,619)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270679"
     Site            553..578
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270679"
     CDS             1..731
                     /gene="FGFR2"
                     /gene_synonym="BBDS; BEK; BFR-1; CD332; CEK3; CFD1; ECT1;
                     JWS; K-SAM; KGFR; TK14; TK25"
                     /coded_by="NM_001441088.1:634..2829"
                     /note="isoform 18 precursor is encoded by transcript
                     variant 18"
                     /db_xref="GeneID:2263"
                     /db_xref="HGNC:HGNC:3689"
                     /db_xref="MIM:176943"
ORIGIN      
        1 mvswgrficl vvvtmatlsl arpsfslved ttlepedais sgddeddtdg aedfvsensn
       61 nkrapywtnt ekmekrlhav paantvkfrc paggnpmptm rwlkngkefk qehriggykv
      121 rnqhwslime svvpsdkgny tcvveneygs inhtyhldvv ersphrpilq aglpanastv
      181 vggdvefvck vysdaqphiq wikhvekngs kygpdglpyl kvlkhsgins snaevlalfn
      241 vteadageyi ckvsnyigqa nqsawltvlp kqqapgreke itaspdylei aiycigvfli
      301 acmvvtvilc rmknttkkpd fssqpavhkl tkriplrrqv saessssmns ntplvrittr
      361 lsstadtpml agvseyelpe dpkwefprdk ltlgkplgeg cfgqvvmaea vgidkdkpke
      421 avtvavkmlk ddatekdlsd lvsememmkm igkhkniinl lgactqdgpl yviveyaskg
      481 nlreylrarr ppgmeysydi nrvpeeqmtf kdlvsctyql argmeylasq kcihrdlaar
      541 nvlvtennvm kiadfglard innidyykkt tngrlpvkwm apealfdrvy thqsdvwsfg
      601 vlmweiftlg gspypgipve elfkllkegh rmdkpanctn elymmmrdcw havpsqrptf
      661 kqlvedldri ltlttneeyl dlsqpleqys psypdtrssc ssgddsvfsp dpmpyepclp
      721 qyphingsvk t
//
LOCUS       NP_001399998             333 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001399998
VERSION     NP_001399998.1
DBSOURCE    REFSEQ: accession NM_001413069.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.892128.1,
                                           SRR14038192.1919983.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..333
                     /product="mitochondrial fission regulator 1 isoform 1
                     precursor"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=31469
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=5550
     Region          22..251
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     mat_peptide     49..333
                     /product="Mitochondrial fission regulator 1.
                     /id=PRO_0000096622"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=31469
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15390.2)"
     Region          177..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          179..304
                     /region_name="Necessary and sufficient to promote
                     mitochondrial fission. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          288..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     CDS             1..333
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001413069.1:392..1393"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsvlwsrkpy gssrsivrki gtnlsliqcp rvqfqinsha
       61 tewspshpge davasfadvg wvakeegecs arlrtevrsr pplqddllff ekapsrqisl
      121 pdlsqeepql ktpalaneea lqkicalene laalraqiak ivtqqeqqnl tagdldsttf
      181 gtipphpppp ppplpppalg lhqstsavdl ikerrekran agktlvknnp kkpempnmle
      241 ilkemnsvkl rsvkrseqdv kpkpvdatdp aaliaealkk kfayryrsds qdevekgipk
      301 seseatserv lfgphmlkpt gkmkalienv sds
//
LOCUS       NP_001424391            1273 aa            linear   PRI 21-NOV-2025
DEFINITION  paired amphipathic helix protein Sin3a [Homo sapiens].
ACCESSION   NP_001424391 XP_006720529 XP_054233664
VERSION     NP_001424391.1
DBSOURCE    REFSEQ: accession NM_001437462.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1273)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1273)
  AUTHORS   Coenen-van der Spek,J., Relator,R., Kerkhof,J., McConkey,H.,
            Levy,M.A., Tedder,M.L., Louie,R.J., Fletcher,R.S., Moore,H.W.,
            Childers,A., Farrelly,E.R., Champaigne,N.L., Lyons,M.J.,
            Everman,D.B., Rogers,R.C., Skinner,S.A., Renck,A., Matalon,D.R.,
            Dills,S.K., Monteleone,B., Demirdas,S., Dingemans,A.J.M., Donker
            Kaat,L., Kolk,S.M., Pfundt,R., Rump,P., Sadikovic,B., Kleefstra,T.
            and Butler,K.M.
  TITLE     DNA methylation episignature for Witteveen-Kolk syndrome due to
            SIN3A haploinsufficiency
  JOURNAL   Genet Med 25 (1), 63-75 (2023)
   PUBMED   36399132
  REMARK    GeneRIF: DNA methylation episignature for Witteveen-Kolk syndrome
            due to SIN3A haploinsufficiency.
REFERENCE   3  (residues 1 to 1273)
  AUTHORS   Soukar,I., Amarasinghe,A. and Pile,L.A.
  TITLE     Coordination of cross-talk between metabolism and epigenetic
            regulation by the SIN3 complex
  JOURNAL   Enzymes 53, 33-68 (2023)
   PUBMED   37748836
  REMARK    GeneRIF: Coordination of cross-talk between metabolism and
            epigenetic regulation by the SIN3 complex.
            Review article
REFERENCE   4  (residues 1 to 1273)
  AUTHORS   Dahiya,N.R., Leibovitch,B.A., Kadamb,R., Bansal,N. and Waxman,S.
  TITLE     The Sin3A/MAD1 Complex, through Its PAH2 Domain, Acts as a Second
            Repressor of Retinoic Acid Receptor Beta Expression in Breast
            Cancer Cells
  JOURNAL   Cells 11 (7), 1179 (2022)
   PUBMED   35406744
  REMARK    GeneRIF: The Sin3A/MAD1 Complex, through Its PAH2 Domain, Acts as a
            Second Repressor of Retinoic Acid Receptor Beta Expression in
            Breast Cancer Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1273)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1273)
  AUTHORS   Laherty,C.D., Yang,W.M., Sun,J.M., Davie,J.R., Seto,E. and
            Eisenman,R.N.
  TITLE     Histone deacetylases associated with the mSin3 corepressor mediate
            mad transcriptional repression
  JOURNAL   Cell 89 (3), 349-356 (1997)
   PUBMED   9150134
  REMARK    GeneRIF: mSin3A interacts with HDAC2 via the HDAC-interacting
            domain (HID) of mSin3A.
            GeneRIF: The transcriptional repressor mSin3A associates with
            histone deacetylase 1 forming a co-repressor complex. See also PMID
            (PubMed identifier) 9150133.
REFERENCE   7  (residues 1 to 1273)
  AUTHORS   Hassig,C.A., Fleischer,T.C., Billin,A.N., Schreiber,S.L. and
            Ayer,D.E.
  TITLE     Histone deacetylase activity is required for full transcriptional
            repression by mSin3A
  JOURNAL   Cell 89 (3), 341-347 (1997)
   PUBMED   9150133
REFERENCE   8  (residues 1 to 1273)
  AUTHORS   Hurlin,P.J., Queva,C., Koskinen,P.J., Steingrimsson,E., Ayer,D.E.,
            Copeland,N.G., Jenkins,N.A. and Eisenman,R.N.
  TITLE     Mad3 and Mad4: novel Max-interacting transcriptional repressors
            that suppress c-myc dependent transformation and are expressed
            during neural and epidermal differentiation
  JOURNAL   EMBO J 14 (22), 5646-5659 (1995)
   PUBMED   8521822
  REMARK    Erratum:[EMBO J. 1996 Apr 15;15(8):2030. PMID: 8617250]
REFERENCE   9  (residues 1 to 1273)
  AUTHORS   Halleck,M.S., Pownall,S., Harder,K.W., Duncan,A.M., Jirik,F.R. and
            Schlegel,R.A.
  TITLE     A widely distributed putative mammalian transcriptional regulator
            containing multiple paired amphipathic helices, with similarity to
            yeast SIN3
  JOURNAL   Genomics 26 (2), 403-406 (1995)
   PUBMED   7601471
REFERENCE   10 (residues 1 to 1273)
  AUTHORS   Ayer,D.E., Lawrence,Q.A. and Eisenman,R.N.
  TITLE     Mad-Max transcriptional repression is mediated by ternary complex
            formation with mammalian homologs of yeast repressor Sin3
  JOURNAL   Cell 80 (5), 767-776 (1995)
   PUBMED   7889570
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC105137.18 and AC068338.14.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_006720529.1, XP_054233664.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            regulatory protein. It contains paired amphipathic helix (PAH)
            domains, which are important for protein-protein interactions and
            may mediate repression by the Mad-Max complex. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1471012.1,
                                           SRR18074969.3005638.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.2"
     Protein         1..1273
                     /product="paired amphipathic helix protein Sin3a"
                     /note="transcriptional co-repressor Sin3A; histone
                     deacetylase complex subunit Sin3a; transcriptional
                     corepressor Sin3a; transcriptional regulator, SIN3A; SIN3
                     homolog A, transcription regulator"
                     /calculated_mol_wt=145045
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          5..1213
                     /region_name="Sin3"
                     /note="Histone deacetylase complex, regulatory component
                     SIN3 [Chromatin structure and dynamics]; COG5602"
                     /db_xref="CDD:227889"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          87..110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          119..196
                     /region_name="Interaction with HCFC1.
                     /evidence=ECO:0000269|PubMed:12670868"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          205..480
                     /region_name="Interaction with REST.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          205..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q60520; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          398..446
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          458..525
                     /region_name="Interaction with SAP30.
                     /evidence=ECO:0000250|UniProtKB:Q60520"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            469
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          523..850
                     /region_name="Interaction with NCOR1.
                     /evidence=ECO:0000250|UniProtKB:Q60520"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          524..659
                     /region_name="Interaction with SUDS3 and SAP130.
                     /evidence=ECO:0000269|PubMed:12724404"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          687..829
                     /region_name="Interaction with HDAC1 and ARID4B.
                     /evidence=ECO:0000269|PubMed:12724404"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            832
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            860
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            865
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60520; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            875
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60520; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          888..967
                     /region_name="Interaction with OGT.
                     /evidence=ECO:0000269|PubMed:12150998"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            940
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            1089
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            1112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          1136..1156
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     CDS             1..1273
                     /gene="SIN3A"
                     /gene_synonym="CHR15DELq24; DEL15Q24; WITKOS"
                     /coded_by="NM_001437462.1:400..4221"
                     /db_xref="GeneID:25942"
                     /db_xref="HGNC:HGNC:19353"
                     /db_xref="MIM:607776"
ORIGIN      
        1 mkrrlddqes pvyaaqqrri pgsteafphq hrvlapappv yeavsetmqs atgiqysvtp
       61 syqvsampqs sgshgpaiaa vhsshhhpta vqphggqvvq shahpappva pvqgqqqfqr
      121 lkvedalsyl dqvklqfgsq pqvyndfldi mkefksqsid tpgvisrvsq lfkghpdlim
      181 gfntflppgy kievqtndmv nvttpgqvhq ipthgiqpqp qpppqhpsqp saqsapapaq
      241 papqpppakv skpsqlqaht pasqqtpplp pyasprsppv qphtpvtisl gtapslqnnq
      301 pvefnhainy vnkiknrfqg qpdiykafle ilhtyqkeqr nakeaggnyt palteqevya
      361 qvarlfknqe dllsefgqfl pdanssvlls kttaekvdsv rndhggtvkk pqlnnkpqrp
      421 sqngcqirrh ptgttppvkk kpkllnlkds smadaskhgg gteslffdkv rkalrsaeay
      481 enflrclvif nqevisrael vqlvspflgk fpelfnwfkn flgykesvhl etypkerate
      541 giameidyas ckrlgssyra lpksyqqpkc tgrtplckev lndtwvsfps wsedstfvss
      601 kktqyeehiy rcederfeld vvletnlati rvleaiqkkl srlsaeeqak frldntlggt
      661 sevihrkalq riyadkaadi idglrknpsi avpivlkrlk mkeeewreaq rgfnkvwreq
      721 nekyylksld hqginfkqnd tkvlrsksll neiesiyder qeqateenag vpvgphlsla
      781 yedkqileda aaliihhvkr qtgiqkedky kikqimhhfi pdllfaqrgd lsdveeeeee
      841 emdvdeatga vkkhngvggs ppkskllfsn taaqklrgmd evynlfyvnn nwyifmrlhq
      901 ilclrllric sqaerqieee nrerewerev lgikrdksds paiqlrlkep mdvdvedyyp
      961 afldmvrsll dgnidssqye dslremftih ayiaftmdkl iqsivrqlqh ivsdeicvqv
     1021 tdlylaennn gatggqlntq nsrsllesty qrkaeqlmsd encfklmfiq sqgqvqltie
     1081 lldteeensd dpveaerwsd yverymnsdt tspelrehla qkpvflprnl rrirkcqrgr
     1141 eqqekegkeg nskktmenvd sldklecrfk lnsykmvyvi ksedymyrrt allrahqshe
     1201 rvskrlhqrf qawvdkwtke hvpremaaet skwlmgegle glvpctttcd tetlhfvsin
     1261 kyrvkygtvf kap
//
LOCUS       NP_001400600             292 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 3 [Homo sapiens].
ACCESSION   NP_001400600
VERSION     NP_001400600.1
DBSOURCE    REFSEQ: accession NM_001413671.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 292)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 292)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 292)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803614.115591.1, SRR1660803.180098.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..292
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 3"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=33300
     Region          4..286
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     CDS             1..292
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413671.1:149..1027"
                     /note="isoform 3 is encoded by transcript variant 7"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mewssrrsif rmngdkfrkf ikapprnysm ivmftalqpq rqcsvcrqan eeyqilansw
       61 ryssafcnkl ffsmvdydeg tdvfqqlnmn saptfmhfpp kgrpkradtf dlqrigfaae
      121 qlakwiadrt dvhirvfrpp nysgtialal lvslvgglly lrrnnlefiy nktgwamvsl
      181 civfamtsgq mwnhirgppy ahknphngqv syihgssqaq fvaeshiilv lnaaitmgmv
      241 llneaatskg dvgkrriicl vglglvvfff sfllsifrsk yhgypysdld fe
//
LOCUS       NP_001427348             250 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 8 precursor [Homo
            sapiens].
ACCESSION   NP_001427348
VERSION     NP_001427348.1
DBSOURCE    REFSEQ: accession NM_001440419.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 250)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 250)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 250)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3 and AP004147.3.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA2157437 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..250
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     8 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=25325
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..>230
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     CDS             1..250
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440419.1:603..1355"
                     /note="isoform 8 precursor is encoded by transcript
                     variant 21"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk vgaslspppp
      241 aelhpppslp
//
LOCUS       NP_001116855            1721 aa            linear   PRI 21-NOV-2025
DEFINITION  BCL-6 corepressor isoform a [Homo sapiens].
ACCESSION   NP_001116855
VERSION     NP_001116855.1
DBSOURCE    REFSEQ: accession NM_001123383.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1721)
  AUTHORS   Batkova,M., Havlovicova,M., Nocar,A., Dudakova,L., Macek,M.,
            Liskova,P. and Dostalova,T.
  TITLE     Dental abnormalities observed in the oculo-facio-cardio-dental
            (OFCD) syndrome present in two Czech families bearing novel de novo
            BCOR pathogenic variants
  JOURNAL   BMC Oral Health 24 (1), 1264 (2024)
   PUBMED   39438869
  REMARK    GeneRIF: Dental abnormalities observed in the
            oculo-facio-cardio-dental (OFCD) syndrome present in two Czech
            families bearing novel de novo BCOR pathogenic variants.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1721)
  AUTHORS   Giner,F., Medina-Ceballos,E., Lopez-Reig,R., Machado,I.,
            Lopez-Guerrero,J.A., Navarro,S., Rubio-Martinez,L.A., Espino,M.,
            Mayordomo-Aranda,E. and Llombart-Bosch,A.
  TITLE     The Combined Immunohistochemical Expression of GLI1 and BCOR in
            Synovial Sarcomas for the Identification of Three Risk Groups and
            Their Prognostic Outcomes: A Study of 52 Patients
  JOURNAL   Int J Mol Sci 25 (14), 7615 (2024)
   PUBMED   39062853
  REMARK    GeneRIF: The Combined Immunohistochemical Expression of GLI1 and
            BCOR in Synovial Sarcomas for the Identification of Three Risk
            Groups and Their Prognostic Outcomes: A Study of 52 Patients.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1721)
  AUTHORS   Mavridou,E., Lema Fernandez,A.G., Nardelli,C., Pierini,V.,
            Quintini,M., Arniani,S., Di Giacomo,D., Crescenzi,B., Matteucci,C.,
            Sambani,C. and Mecucci,C.
  TITLE     A novel t(X;21)(p11.4;q22.12) translocation adds to the role of
            BCOR and RUNX1 in myelodysplastic syndromes and acute myeloid
            leukemias
  JOURNAL   Genes Chromosomes Cancer 63 (4), e23235 (2024)
   PUBMED   38656651
  REMARK    GeneRIF: A novel t(X;21)(p11.4;q22.12) translocation adds to the
            role of BCOR and RUNX1 in myelodysplastic syndromes and acute
            myeloid leukemias.
REFERENCE   4  (residues 1 to 1721)
  AUTHORS   Pierron,G., Tirode,F., Lucchesi,C., Reynaud,S., Ballet,S.,
            Cohen-Gogo,S., Perrin,V., Coindre,J.M. and Delattre,O.
  TITLE     A new subtype of bone sarcoma defined by BCOR-CCNB3 gene fusion
  JOURNAL   Nat Genet 44 (4), 461-466 (2012)
   PUBMED   22387997
  REMARK    GeneRIF: A new fusion was observed between BCOR (encoding the BCL6
            co-repressor) and CCNB3 (encoding the testis-specific cyclin B3) on
            the X chromosome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1721)
  AUTHORS   Tomsig,J.L., Snyder,S.L. and Creutz,C.E.
  TITLE     Identification of targets for calcium signaling through the copine
            family of proteins. Characterization of a coiled-coil
            copine-binding motif
  JOURNAL   J Biol Chem 278 (12), 10048-10054 (2003)
   PUBMED   12522145
REFERENCE   6  (residues 1 to 1721)
  AUTHORS   Ng,D., Hadley,D.W., Tifft,C.J. and Biesecker,L.G.
  TITLE     Genetic heterogeneity of syndromic X-linked recessive
            microphthalmia-anophthalmia: is Lenz microphthalmia a single
            disorder?
  JOURNAL   Am J Med Genet 110 (4), 308-314 (2002)
   PUBMED   12116202
REFERENCE   7  (residues 1 to 1721)
  AUTHORS   Tang,T.T., Dowbenko,D., Jackson,A., Toney,L., Lewin,D.A., Dent,A.L.
            and Lasky,L.A.
  TITLE     The forkhead transcription factor AFX activates apoptosis by
            induction of the BCL-6 transcriptional repressor
  JOURNAL   J Biol Chem 277 (16), 14255-14265 (2002)
   PUBMED   11777915
  REMARK    GeneRIF: The forkhead transcription factor AFX activates apoptosis
            by induction of the BCL-6 transcriptional repressor.
REFERENCE   8  (residues 1 to 1721)
  AUTHORS   Huynh,K.D., Fischle,W., Verdin,E. and Bardwell,V.J.
  TITLE     BCoR, a novel corepressor involved in BCL-6 repression
  JOURNAL   Genes Dev 14 (14), 1810-1823 (2000)
   PUBMED   10898795
  REMARK    GeneRIF: Function:BCoR is a transcriptional corepressor for BCL-6.
            Nomenclature:BCoR (BCL-6 corepressor)
REFERENCE   9  (residues 1 to 1721)
  AUTHORS   Ng,D.
  TITLE     Lenz Microphthalmia Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301694
REFERENCE   10 (residues 1 to 1721)
  AUTHORS   Bardakjian,T., Weiss,A. and Schneider,A.
  TITLE     Microphthalmia/Anophthalmia/Coloboma Spectrum - RETIRED CHAPTER,
            FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301552
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091806.4 and AC092198.5.
            
            Summary: The protein encoded by this gene was identified as an
            interacting corepressor of BCL6, a POZ/zinc finger transcription
            repressor that is required for germinal center formation and may
            influence apoptosis. This protein selectively interacts with the
            POZ domain of BCL6, but not with eight other POZ proteins. Specific
            class I and II histone deacetylases (HDACs) have been shown to
            interact with this protein, which suggests a possible link between
            the two classes of HDACs. Several transcript variants encoding
            different isoforms have been found for this gene. A pseudogene of
            this gene is found on chromosome Y.[provided by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and uses
            an alternate in-frame splice site compared to variant 5. The
            resulting isoform (a) has the same N- and C-termini but is shorter
            compared to isoform c. Variants 1 and 3 both encode the same
            isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1941133.1,
                                           SRR14038192.446815.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1721
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.4"
     Protein         1..1721
                     /product="BCL-6 corepressor isoform a"
                     /note="BCL-6 interacting corepressor; BCL6 interacting
                     corepressor; BCL-6 coreceptor"
                     /calculated_mol_wt=188072
     Region          <257..673
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          309..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          388..438
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            392
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          498..514
                     /region_name="Interaction with BCL6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          557..641
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          737..760
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          773..794
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          815..844
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGN4; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1168..1380
                     /region_name="BCOR"
                     /note="BCL-6 co-repressor, non-ankyrin-repeat region;
                     pfam15808"
                     /db_xref="CDD:434953"
     Region          1186..1294
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGN4; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1376
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1396..1417
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          <1427..1559
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1428..1461
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1429..1460
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1430,1434..1435,1438..1440,1442..1443,1447,1450,
                     1460,1462,1464,1468..1469,1472..1474,1476..1477,1481,1484,
                     1493,1495,1497,1501..1502,1505..1507,1509..1510,1514,1517)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1462..1493
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1462..1491
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1495..1524
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1495..1524
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1600..1714
                     /region_name="Necessary and sufficient for interaction
                     with PCGF1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1600..1713
                     /region_name="PUFD"
                     /note="BCORL-PCGF1-binding domain; pfam16553"
                     /db_xref="CDD:465171"
     Site            order(1602..1603,1605..1609,1611..1613,1615,1617,1626,
                     1628,1670..1672,1674..1675,1677..1678,1695,1706,1708,
                     1710..1712)
                     /site_type="other"
                     /note="RAWUL domain interface [polypeptide binding]"
                     /db_xref="CDD:271224"
     CDS             1..1721
                     /gene="BCOR"
                     /gene_synonym="ANOP2; MAA2; MCOPS2"
                     /coded_by="NM_001123383.2:312..5477"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS14250.1"
                     /db_xref="GeneID:54880"
                     /db_xref="HGNC:HGNC:20893"
                     /db_xref="MIM:300485"
ORIGIN      
        1 mlsatplygn vhswmnserv rmcgasedrk ilvndgdask arlelreenp lnhnvvdast
       61 ahridglaal smdrtglire glrvpgnivy sslcglgsek greaatstlg glgfssernp
      121 emqfkpntpe tveasavsgk ppngfsaiyk tppgiqksav ataealgldr pasdkqspln
      181 ingasylrlp wvnpymegat paiypfldsp nkyslnmyka llpqqsysla qplyspvctn
      241 gerflylppp hyvgphipss laspmrlstp saspaipplv hcadkslpwk mgvspgnpvd
      301 shayphiqns kqprvpsaka vtsglpgdta lllppsprps prvhlptqpa adtysefhkh
      361 yaristspsv alskpymtvs sefpaarlsn gkypkapegg egaqpvpgha rktavqdrkd
      421 gssppllekq tvtkdvtdkp ldlsskvvdv daskadhmkk maptvlvhsr agsglvlsgs
      481 eipketlspp gngcaiyrse iistapsswv vpgpspneen ngksmslknk aldwaipqqr
      541 ssscprmggt davitnvsgs vssagrpasa spapnanadg tktsrssvet tpsviqhvgq
      601 ppatpakhss stsskgakas npepsfkane nglppssifl spneafrspp ipyprsylpy
      661 papegiavsp lslhgkgpvy phpvllpngs lfpghlapkp glpyglptgr pefvtyqdal
      721 glgmvhpmli phtpieitke ekperrsrsh eraryedptl rnrfseilet sstklhpdvp
      781 tdknlkpnpn wnqgktvvks dklvyvdllr eepdaktdtn vskpsfaaes vgqsaeppkp
      841 svepalqqhr dfialreelg risdfhetyt fkqpvftvsk dsvlagtnke nlglpvstpf
      901 lepplgsdgp avtfgktqed pkpfcvgsap psvdvtptyt kdgadeaesn dgkvlkpkps
      961 klakriansa gyvgdrfkcv ttelyadssq lsreqralqm eglqedsilc lpaayceram
     1021 mrfselemke regghpatkd semckfspad werlkgnqdk kpksvtleea iaeqneserc
     1081 eysvgnkhrd pfeapedkdl pvekyfverq pvseppadqv asdmphsptl rvdrkrkvsg
     1141 dsshtettae evpedpllka krrrvskglh pkkqrhllhl rerweqqvsa adgkpgrqsr
     1201 kevtqatqpe aipqgtnite ekpgrkraea kgnrswsees lkpsdneqgl pvfsgsppmk
     1261 slsstsaggk kqaqpscapa srppakqqki kenqktdvlc adeeedcqaa sllqkytdns
     1321 ekpsgkrlck tkhlipqesr rglpltgeyy venadgkvtv rrfrkrpeps sdydlspakq
     1381 epkpfdrlqq llpasqstql pcssspqett qsrpmppear rlivnknage tllqraarlg
     1441 yeevvlycle nkicdvnhrd nagycalhea cargwlnivr hlleygadvn csaqdgtrpl
     1501 hdavendhle ivrlllsyga dptlatysgr timkmthsel mekfltdyln dlqgrnddda
     1561 sgtwdfygss vcepddesgy dvlanppgpe dqdddddays dvfefefset pllpcyniqv
     1621 svaqgprnwl llsdvlkklk mssrifrcnf pnveivtiae aefyrqvsas llfscskdle
     1681 afnpeskell dlveftneiq tllgssvewl hpsdlasdny w
//
LOCUS       NP_001427592             719 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 3 isoform 11 [Homo sapiens].
ACCESSION   NP_001427592
VERSION     NP_001427592.1
DBSOURCE    REFSEQ: accession NM_001440663.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 719)
  AUTHORS   Ghashghaei,M., Liu,Y., Ettles,J., Bombaci,G., Ramkumar,N., Liu,Z.,
            Escano,L., Miko,S.S., Kim,Y., Waldron,J.A., Do,K., MacPherson,K.,
            Yuen,K.A., Taibi,T., Yue,M., Arsalan,A., Jin,Z., Edin,G.,
            Karsan,A., Morin,G.B., Kuchenbauer,F., Perna,F., Bushell,M. and
            Vu,L.P.
  TITLE     Translation efficiency driven by CNOT3 subunit of the CCR4-NOT
            complex promotes leukemogenesis
  JOURNAL   Nat Commun 15 (1), 2340 (2024)
   PUBMED   38491013
  REMARK    GeneRIF: Translation efficiency driven by CNOT3 subunit of the
            CCR4-NOT complex promotes leukemogenesis.
            Erratum:[Nat Commun. 2024 Oct 7;15(1):8674. doi:
            10.1038/s41467-024-53071-1. PMID: 39375334]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 719)
  AUTHORS   Burgess,H.M., Grande,R., Riccio,S., Dinesh,I., Winkler,G.S.,
            Depledge,D.P. and Mohr,I.
  TITLE     CCR4-NOT differentially controls host versus virus poly(a)-tail
            length and regulates HCMV infection
  JOURNAL   EMBO Rep 24 (12), e56327 (2023)
   PUBMED   37846490
  REMARK    GeneRIF: CCR4-NOT differentially controls host versus virus
            poly(a)-tail length and regulates HCMV infection.
REFERENCE   4  (residues 1 to 719)
  AUTHORS   Zhao,P., Meng,Q., Wan,C., Lei,T., Zhang,L., Zhang,X., Tan,L.,
            Zhu,H. and He,X.
  TITLE     Clinical features of CNOT3-associated neurodevelopmental disorder
            in three Chinese patients
  JOURNAL   Neurogenetics 24 (2), 129-136 (2023)
   PUBMED   36802310
  REMARK    GeneRIF: Clinical features of CNOT3-associated neurodevelopmental
            disorder in three Chinese patients.
REFERENCE   5  (residues 1 to 719)
  AUTHORS   McLenachan,S., Zhang,D., Grainok,J., Zhang,X., Huang,Z., Chen,S.C.,
            Zaw,K., Lima,A., Jennings,L., Roshandel,D., Moon,S.Y., Heath
            Jeffery,R.C., Attia,M.S., Thompson,J.A., Lamey,T.M., McLaren,T.L.,
            De Roach,J., Fletcher,S. and Chen,F.K.
  TITLE     Determinants of Disease Penetrance in PRPF31-Associated Retinopathy
  JOURNAL   Genes (Basel) 12 (10), 1542 (2021)
   PUBMED   34680937
  REMARK    GeneRIF: Determinants of Disease Penetrance in PRPF31-Associated
            Retinopathy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 719)
  AUTHORS   Yin,X., Warner,D.R., Roberts,E.A., Pisano,M.M. and Greene,R.M.
  TITLE     Identification of novel CBP interacting proteins in embryonic
            orofacial tissue
  JOURNAL   Biochem Biophys Res Commun 329 (3), 1010-1017 (2005)
   PUBMED   15752756
REFERENCE   7  (residues 1 to 719)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 719)
  AUTHORS   Aoki,T., Okada,N., Wakamatsu,T. and Tamura,T.A.
  TITLE     TBP-interacting protein 120B, which is induced in relation to
            myogenesis, binds to NOT3
  JOURNAL   Biochem Biophys Res Commun 296 (5), 1097-1103 (2002)
   PUBMED   12207886
  REMARK    GeneRIF: TBP-interacting protein 120B binds to NOT3
REFERENCE   9  (residues 1 to 719)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
REFERENCE   10 (residues 1 to 719)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC245052.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3003586.1,
                                           SRR14372079.441612.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..719
                     /product="CCR4-NOT transcription complex subunit 3 isoform
                     11"
                     /note="NOT3 (negative regulator of transcription 3, yeast)
                     homolog; CCR4-associated factor 3; leukocyte receptor
                     cluster member 2"
                     /calculated_mol_wt=76566
     Region          3..230
                     /region_name="Not3"
                     /note="Not1 N-terminal domain, CCR4-Not complex component;
                     pfam04065"
                     /db_xref="CDD:461155"
     Region          241..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75175.1)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Region          621..>685
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; cl02384"
                     /db_xref="CDD:470561"
     CDS             1..719
                     /gene="CNOT3"
                     /gene_synonym="IDDSADF; LENG2; NOT3; NOT3H"
                     /coded_by="NM_001440663.1:283..2442"
                     /note="isoform 11 is encoded by transcript variant 12"
                     /db_xref="GeneID:4849"
                     /db_xref="HGNC:HGNC:7879"
                     /db_xref="MIM:604910"
ORIGIN      
        1 madkrklqge idrclkkvse gveqfediwq klhnaananq kekyeadlkk eikklqrlrd
       61 qiktwvasne ikdkrqlidn rklietqmer fkvveretkt kayskeglgl aqkvdpaqke
      121 keevgqwltn tidtlnmqvd qfesevesls vqtrkkkgdk dqkqdriegl krhiekhryh
      181 vrmletilrm ldndsilvda irkikddvey yvdssqdpdf eeneflyddl dledipqalv
      241 atsppshshm edeifnqsss tptsttsssp ippspanctt enseddkkrg rstdsevsqs
      301 pakngskpvh snqhpqspav pptypsgppp aasalsttpg nngvpapaap psalgpkasp
      361 apshnsgtpa pyaqavappa psgpsttqpr ppsvqpsggg gggsggggss sssnssaggg
      421 agkqngatsy ssvvadspae valsssggnn assqalgpps gphnpppsts kepsaaaptg
      481 aggvapgsgn nsggpsllvp lpvnppsspt psfsdakaag allngppqfs tapeikapep
      541 lsslksmaer aaissgiedp vptlhlterd iilsstsapp asaqpplqls evniplslgv
      601 cplgpvpltk eqlyqqamee aawhhmphps dserirqylp rnpcptppyh hqmppphsdt
      661 vefyqrlste tlffifyyle vqqgprgslg ppgfaataav ppraggvral rhsiwqprp
//
LOCUS       NP_001424250             852 aa            linear   PRI 21-NOV-2025
DEFINITION  ephrin type-A receptor 5 isoform j [Homo sapiens].
ACCESSION   NP_001424250 XP_016863369 XP_054205165
VERSION     NP_001424250.1
DBSOURCE    REFSEQ: accession NM_001437321.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 852)
  AUTHORS   Han,X., Liu,T., Zhai,J., Liu,C., Wang,W., Nie,C., Wang,Q., Zhu,X.,
            Zhou,H. and Tian,W.
  TITLE     Association between EPHA5 methylation status in peripheral blood
            leukocytes and the risk and prognosis of gastric cancer
  JOURNAL   PeerJ 10, e13774 (2022)
   PUBMED   36164608
  REMARK    GeneRIF: Association between EPHA5 methylation status in peripheral
            blood leukocytes and the risk and prognosis of gastric cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 852)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   3  (residues 1 to 852)
  AUTHORS   Liu,C., He,Y., Feng,X., Li,J. and Wang,J.
  TITLE     Expression of EPHA5 in lung adenocarcinoma is associated with lymph
            node metastasis and EGFR mutation
  JOURNAL   APMIS 130 (6), 338-345 (2022)
   PUBMED   35332588
  REMARK    GeneRIF: Expression of EPHA5 in lung adenocarcinoma is associated
            with lymph node metastasis and EGFR mutation.
REFERENCE   4  (residues 1 to 852)
  AUTHORS   Abouhashem,N., Harb,O., Elwan,A., Zaitoun,M. and Saraya,Y.
  TITLE     Immunohistochemical evaluation of forkhead box A1 and EphA5 markers
            in serous ovarian carcinomas, and their impact on the clinical
            outcome of patients
  JOURNAL   Pol J Pathol 73 (2), 120-133 (2022)
   PUBMED   36345952
  REMARK    GeneRIF: Immunohistochemical evaluation of forkhead box A1 and
            EphA5 markers in serous ovarian carcinomas, and their impact on the
            clinical outcome of patients.
REFERENCE   5  (residues 1 to 852)
  AUTHORS   Zhou,R.
  TITLE     Regulation of topographic projection by the Eph family receptor Bsk
            (EphA5) and its ligands
  JOURNAL   Cell Tissue Res 290 (2), 251-259 (1997)
   PUBMED   9321686
  REMARK    Review article
REFERENCE   6  (residues 1 to 852)
  AUTHORS   Miescher,G.C., Taylor,V., Olivieri,G., Mindermann,T., Schrock,E.
            and Steck,A.J.
  TITLE     Extensive splice variation and localization of the EHK-1 receptor
            tyrosine kinase in adult human brain and glial tumors
  JOURNAL   Brain Res Mol Brain Res 46 (1-2), 17-24 (1997)
   PUBMED   9191074
REFERENCE   7  (residues 1 to 852)
  AUTHORS   Gale,N.W., Holland,S.J., Valenzuela,D.M., Flenniken,A., Pan,L.,
            Ryan,T.E., Henkemeyer,M., Strebhardt,K., Hirai,H., Wilkinson,D.G.,
            Pawson,T., Davis,S. and Yancopoulos,G.D.
  TITLE     Eph receptors and ligands comprise two major specificity subclasses
            and are reciprocally compartmentalized during embryogenesis
  JOURNAL   Neuron 17 (1), 9-19 (1996)
   PUBMED   8755474
REFERENCE   8  (residues 1 to 852)
  AUTHORS   Winslow,J.W., Moran,P., Valverde,J., Shih,A., Yuan,J.Q., Wong,S.C.,
            Tsai,S.P., Goddard,A., Henzel,W.J., Hefti,F. et al.
  TITLE     Cloning of AL-1, a ligand for an Eph-related tyrosine kinase
            receptor involved in axon bundle formation
  JOURNAL   Neuron 14 (5), 973-981 (1995)
   PUBMED   7748564
REFERENCE   9  (residues 1 to 852)
  AUTHORS   Fox,G.M., Holst,P.L., Chute,H.T., Lindberg,R.A., Janssen,A.M.,
            Basu,R. and Welcher,A.A.
  TITLE     cDNA cloning and tissue distribution of five human EPH-like
            receptor protein-tyrosine kinases
  JOURNAL   Oncogene 10 (5), 897-905 (1995)
   PUBMED   7898931
REFERENCE   10 (residues 1 to 852)
  AUTHORS   Spritz,R.A., Strunk,K.M., Lee,S.T., Lu-Kuo,J.M., Ward,D.C., Le
            Paslier,D., Altherr,M.R., Dorman,T.E. and Moir,D.T.
  TITLE     A YAC contig spanning a cluster of human type III receptor protein
            tyrosine kinase genes (PDGFRA-KIT-KDR) in chromosome segment 4q12
  JOURNAL   Genomics 22 (2), 431-436 (1994)
   PUBMED   7528718
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104137.5, AC105923.6 and
            AC018683.4.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_016863369.1, XP_054205165.1.
            
            Summary: This gene belongs to the ephrin receptor subfamily of the
            protein-tyrosine kinase family. EPH and EPH-related receptors have
            been implicated in mediating developmental events, particularly in
            the nervous system. Receptors in the EPH subfamily typically have a
            single kinase domain and an extracellular region containing a
            Cys-rich domain and 2 fibronectin type III repeats. The ephrin
            receptors are divided into 2 groups based on the similarity of
            their extracellular domain sequences and their affinities for
            binding ephrin-A and ephrin-B ligands. Alternatively spliced
            transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2685512.1,
                                           SRR14038194.1310067.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..852
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q13.1-q13.2"
     Protein         1..852
                     /product="ephrin type-A receptor 5 isoform j"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-A receptor 5; receptor protein-tyrosine
                     kinase HEK7; tyrosine-protein kinase receptor EHK-1;
                     EPH-like kinase 7; EPH homology kinase 1; brain-specific
                     kinase; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=94572
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54756.3)"
     Region          60..232
                     /region_name="EphR_LBD_A5"
                     /note="Ligand Binding Domain of Ephrin type-A Receptor 5;
                     cd10483"
                     /db_xref="CDD:198451"
     Site            order(84,86..90,97..98,100,102,133,135,140..141,183,
                     187..188,191..193,220..222,224)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198451"
     Site            264
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54756.3)"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54756.3)"
     Region          305..395
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(305,368,383)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(384..385,387..388)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          412..487
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Region          485..751
                     /region_name="PTKc_EphR_A"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphA Ephrin Receptors; cd05066"
                     /db_xref="CDD:270651"
     Site            order(496,498..500,504,520,522,568..569,571,615,619..620,
                     622,633,652..656,665,699)
                     /site_type="active"
                     /db_xref="CDD:270651"
     Site            order(496..500,504,520,522,568..571,574..575,619..620,622,
                     633)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270651"
     Site            order(615,619,652..656,665,699)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270651"
     Site            632..658
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270651"
     Region          780..845
                     /region_name="SAM_EPH-A5"
                     /note="SAM domain of EPH-A5 subfamily of tyrosine kinase
                     receptors; cd09546"
                     /db_xref="CDD:188945"
     Site            order(797,830)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188945"
     CDS             1..852
                     /gene="EPHA5"
                     /gene_synonym="CEK7; EHK-1; EHK1; EK7; HEK7; TYRO4"
                     /coded_by="NM_001437321.1:748..3306"
                     /note="isoform j is encoded by transcript variant 10"
                     /db_xref="GeneID:2044"
                     /db_xref="HGNC:HGNC:3389"
                     /db_xref="MIM:600004"
ORIGIN      
        1 mrgsgprgag rrrppsgggd tpitpaslag cysaprrapl wtclllcaal rtllaspsne
       61 vnlldsrtvm gdlgwiafpk ngweeigevd enyapihtyq vckvmeqnqn nwlltswisn
      121 egasrifiel kftlrdcnsl pgglgtcket fnmyyfesdd qngrnikenq yikidtiaad
      181 esfteldlgd rvmklntevr dvgplskkgf ylafqdvgac ialvsvrvyy kkcpsvvrhl
      241 avfpdtitga dssqllevsg scvnhsvtde ppkmhcsaeg ewlvpigkcm ckagyeekng
      301 tcqapspvtn vkkgkiakns islswqepdr pngiileyei kyfekdqets ytiikskett
      361 itaeglkpas vyvfqirart aagygvfsrr fefettpvsv aassdqsqip viavsvtvgv
      421 illavvigvl lsgrrcgysk akqdpeeekm hfhnghiklp gvrtyidpht yedpnqavhe
      481 fakeieasci tiervigage fgevcsgrlk lpgkrelpva iktlkvgyte kqrrdflgea
      541 simgqfdhpn iihlegvvtk skpvmivtey mengsldtfl kkndgqftvi qlvgmlrgis
      601 agmkylsdmg yvhrdlaarn ilinsnlvck vsdfglsrvl eddpeaaytt rggkipirwt
      661 apeaiafrkf tsasdvwsyg ivmwevvsyg erpywemtnq dvikaveegy rlpspmdcpa
      721 alyqlmldcw qkernsrpkf deivnmldkl irnpsslktl vnascrvsnl laehsplgsg
      781 ayrsvgewle aikmgrytei fmengyssmd avaqvtledl rrlgvtlvgh qkkimnslqe
      841 mkvqlvngmv pl
//
LOCUS       NP_001393930             456 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform M [Homo sapiens].
ACCESSION   NP_001393930
VERSION     NP_001393930.1
DBSOURCE    REFSEQ: accession NM_001407001.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 456)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 456)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 456)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2939050.1,
                                           SRR14038191.1879957.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..456
                     /product="lamin isoform M"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=49912
     Region          <104..178
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          226..333
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     CDS             1..456
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001407001.1:716..2086"
                     /note="isoform M is encoded by transcript variant 26"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 mrpdwwrltm gssvslragw rmrcrncgps mrtrwssirr swrrlilpsw tmpgsllrgt
       61 atwwglptrs cssrasasta slpssassrs ralgsspnpp tplqlaakea klrdledsla
      121 rerdtsrrll aekeremaem rarmqqqlde yqelldikla ldmeihayrk llegeeerlr
      181 lspsptsqrs rgrasshssq tqgggsvtkk rklestesrs sfsqhartsg rvaveevdee
      241 gkfvrlrnks nedqsmgnwq ikrqngddpl ltyrfppkft lkagqvvtiw aagagathsp
      301 ptdlvwkaqn twgcgnslrt alinstgeev amrklvrsvt vveddededg ddllhhhhgs
      361 hcsssgdpae ynlrsrtvlc gtcgqpadka sasgsgaqvg gpissgssas svtvtrsyrs
      421 vggsgggsfg dnlvtrsyll gnssprtqsp qncsim
//
LOCUS       NP_001427354             667 aa            linear   PRI 21-NOV-2025
DEFINITION  interleukin-12 receptor subunit beta-1 isoform 6 precursor [Homo
            sapiens].
ACCESSION   NP_001427354 XP_047294728 XP_054176857
VERSION     NP_001427354.1
DBSOURCE    REFSEQ: accession NM_001440425.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Chen,H., Ge,X., Li,C., Zeng,J. and Wang,X.
  TITLE     Structure and assembly of the human IL-12 signaling complex
  JOURNAL   Structure 32 (10), 1640-1651 (2024)
   PUBMED   39111304
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Huang,J., He,Q., Huang,L., Liu,L., Yang,P. and Chen,M.
  TITLE     Discovering the link between IL12RB1 gene polymorphisms and
            tuberculosis susceptibility: a comprehensive meta-analysis
  JOURNAL   Front Public Health 12, 1249880 (2024)
   PUBMED   38317798
  REMARK    GeneRIF: Discovering the link between IL12RB1 gene polymorphisms
            and tuberculosis susceptibility: a comprehensive meta-analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 667)
  AUTHORS   Rosas Mejia,O., Claeys,T.A., Williams,A., Zafar,A. and
            Robinson,R.T.
  TITLE     IL12RB1 allele bias in human TH cells is regulated by functional
            SNPs in its 3'UTR
  JOURNAL   Cytokine 158, 155993 (2022)
   PUBMED   36007427
  REMARK    GeneRIF: IL12RB1 allele bias in human TH cells is regulated by
            functional SNPs in its 3'UTR.
REFERENCE   4  (residues 1 to 667)
  AUTHORS   Khattak,F.A., Akbar,N.U., Riaz,M., Hussain,M., Rehman,K., Khan,S.N.
            and Khan,T.A.
  TITLE     Novel IL-12Rbeta1 deficiency-mediates recurrent cutaneous
            leishmaniasis
  JOURNAL   Int J Infect Dis 112, 338-345 (2021)
   PUBMED   34438084
  REMARK    GeneRIF: Novel IL-12Rbeta1 deficiency-mediates recurrent cutaneous
            leishmaniasis.
REFERENCE   5  (residues 1 to 667)
  AUTHORS   Yamamoto,K., Kobayashi,H., Miura,O., Hirosawa,S. and Miyasaka,N.
  TITLE     Assignment of IL12RB1 and IL12RB2, interleukin-12 receptor beta 1
            and beta 2 chains, to human chromosome 19 band p13.1 and chromosome
            1 band p31.2, respectively, by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 77 (3-4), 257-258 (1997)
   PUBMED   9284929
REFERENCE   6  (residues 1 to 667)
  AUTHORS   Bacon,C.M., Petricoin,E.F. 3rd, Ortaldo,J.R., Rees,R.C.,
            Larner,A.C., Johnston,J.A. and O'Shea,J.J.
  TITLE     Interleukin 12 induces tyrosine phosphorylation and activation of
            STAT4 in human lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 92 (16), 7307-7311 (1995)
   PUBMED   7638186
REFERENCE   7  (residues 1 to 667)
  AUTHORS   Bacon,C.M., McVicar,D.W., Ortaldo,J.R., Rees,R.C., O'Shea,J.J. and
            Johnston,J.A.
  TITLE     Interleukin 12 (IL-12) induces tyrosine phosphorylation of JAK2 and
            TYK2: differential use of Janus family tyrosine kinases by IL-2 and
            IL-12
  JOURNAL   J Exp Med 181 (1), 399-404 (1995)
   PUBMED   7528775
REFERENCE   8  (residues 1 to 667)
  AUTHORS   Ling,P., Gately,M.K., Gubler,U., Stern,A.S., Lin,P., Hollfelder,K.,
            Su,C., Pan,Y.C. and Hakimi,J.
  TITLE     Human IL-12 p40 homodimer binds to the IL-12 receptor but does not
            mediate biologic activity
  JOURNAL   J Immunol 154 (1), 116-127 (1995)
   PUBMED   7527811
REFERENCE   9  (residues 1 to 667)
  AUTHORS   Gillessen,S., Carvajal,D., Ling,P., Podlaski,F.J., Stremlo,D.L.,
            Familletti,P.C., Gubler,U., Presky,D.H., Stern,A.S. and Gately,M.K.
  TITLE     Mouse interleukin-12 (IL-12) p40 homodimer: a potent IL-12
            antagonist
  JOURNAL   Eur J Immunol 25 (1), 200-206 (1995)
   PUBMED   7843232
REFERENCE   10 (residues 1 to 667)
  AUTHORS   Chua,A.O., Chizzonite,R., Desai,B.B., Truitt,T.P., Nunes,P.,
            Minetti,L.J., Warrier,R.R., Presky,D.H., Levine,J.F., Gately,M.K.
            et al.
  TITLE     Expression cloning of a human IL-12 receptor component. A new
            member of the cytokine receptor superfamily with strong homology to
            gp130
  JOURNAL   J Immunol 153 (1), 128-136 (1994)
   PUBMED   7911493
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020904.7.
            
            On or before May 20, 2025 this sequence version replaced
            XP_047294728.1, XP_054176857.1.
            
            Summary: The protein encoded by this gene is a type I transmembrane
            protein that belongs to the hemopoietin receptor superfamily. This
            protein binds to interleukine 12 (IL12) with a low affinity, and is
            thought to be a part of IL12 receptor complex. This protein forms a
            disulfide-linked oligomer, which is required for its IL12 binding
            activity. The coexpression of this and IL12RB2 proteins was shown
            to lead to the formation of high-affinity IL12 binding sites and
            reconstitution of IL12 dependent signaling. Mutations in this gene
            impair the development of interleukin-17-producing T lymphocytes
            and result in increased susceptibility to mycobacterial and
            Salmonella infections. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.3284543.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..667
                     /product="interleukin-12 receptor subunit beta-1 isoform 6
                     precursor"
                     /note="IL-12 receptor beta component; interleukin-12
                     receptor beta-1 chain; IL-12R subunit beta-1; IL-12
                     receptor subunit beta-1; cluster of differentiation 212;
                     interleukin 12 receptor, beta 1"
                     /calculated_mol_wt=71004
     sig_peptide     1..23
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
                     /calculated_mol_wt=2601
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
     Region          222..226
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P42701.1)"
     Site            336
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
     Site            353
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
     Site            359
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
     Site            449
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
     Region          454..544
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            463
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
     Site            order(535..536,538..539)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            553..577
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P42701.1)"
     Region          584..592
                     /region_name="Box 1 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P42701.1)"
     Region          633..655
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42701.1)"
     CDS             1..667
                     /gene="IL12RB1"
                     /gene_synonym="CD212; IL-12R-BETA1; IL12RB; IMD30"
                     /coded_by="NM_001440425.1:112..2115"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:3594"
                     /db_xref="HGNC:HGNC:5971"
                     /db_xref="MIM:601604"
ORIGIN      
        1 meplvtwvvp llflfllsrq gaacrtsecc fqdppypdad sgsasgprdl rcyrissdry
       61 ecswqyegpt agvshflrcc lssgrccyfa agsatrlqfs dqagvsvlyt vtlwveswar
      121 nqtekspevt lqlynsvkye pplgdikvsk lagqlrmewe tpdnqvgaev qfrhrtpssp
      181 wklgdcgpqd ddtesclcpl emnvaqefql rrrqlgsqgs swskwsspvc vppvglvlia
      241 enppqpqvrf sveqlgqdgr rrltlkeqpt qlelpegcqg lapgtevtyr lqlhmlscpc
      301 kakatrtlhl gkmpylsgaa ynvavissnq fgpglnqtwh ipadthtepv alnisvgtng
      361 ttmywparaq smtyciewqp vgqdgglatc sltapqdpdp agmatyswsr esgamgqekc
      421 yyitifasah pekltlwstv lstyhfggna saagtphhvs vknhsldsvs vdwapsllst
      481 cpgvlkeyvv rcrdedskqv sehpvqptet qvtlsglrag vaytvqvrad tawlrgvwsq
      541 pqrfsievqv sdwliffasl gsflsillvg vlgylglnra arhlcpplpt pcassaiefp
      601 ggketwqwin pvdfqeeasl qealvvemsw dkgerteple ktelpegape laldtelsle
      661 dgdrcdr
//
LOCUS       NP_001401587             520 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 2 isoform e [Homo sapiens].
ACCESSION   NP_001401587
VERSION     NP_001401587.1
DBSOURCE    REFSEQ: accession NM_001414658.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Jung,J.H., Lee,D., Ko,H.M. and Jang,H.J.
  TITLE     Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in Colorectal
            Cancer Cells by Activating p53
  JOURNAL   Biomolecules 11 (10), 1492 (2021)
   PUBMED   34680125
  REMARK    GeneRIF: Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in
            Colorectal Cancer Cells by Activating p53.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Royer-Bertrand,B., Cisarova,K., Niel Butschi,F., Foletti,G.,
            Guinchat,V., Tran,C., Superti-Furga,A. and Good,J.M.
  TITLE     CNOT2 haploinsufficiency in a 40-year-old man with intellectual
            disability, autism, and seizures
  JOURNAL   Am J Med Genet A 185 (8), 2602-2606 (2021)
   PUBMED   34018673
  REMARK    GeneRIF: CNOT2 haploinsufficiency in a 40-year-old man with
            intellectual disability, autism, and seizures.
            Review article
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Jayne,S., Zwartjes,C.G., van Schaik,F.M. and Timmers,H.T.
  TITLE     Involvement of the SMRT/NCoR-HDAC3 complex in transcriptional
            repression by the CNOT2 subunit of the human Ccr4-Not complex
  JOURNAL   Biochem J 398 (3), 461-467 (2006)
   PUBMED   16712523
  REMARK    GeneRIF: This study shows that SMRT/NCoR-HDAC3 complex is a
            cofactor of CNOT2-mediated repression and suggests that
            transcriptional regulation by the Ccr4-Not complex involves
            regulation of chromatin modification.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Winkler,G.S., Mulder,K.W., Bardwell,V.J., Kalkhoven,E. and
            Timmers,H.T.
  TITLE     Human Ccr4-Not complex is a ligand-dependent repressor of nuclear
            receptor-mediated transcription
  JOURNAL   EMBO J 25 (13), 3089-3099 (2006)
   PUBMED   16778766
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Shi,J. and Nelson,M.A.
  TITLE     The cyclin-dependent kinase 11 interacts with NOT2
  JOURNAL   Biochem Biophys Res Commun 334 (4), 1310-1316 (2005)
   PUBMED   16039607
  REMARK    GeneRIF: These findings suggest that CDK11 may contribute to
            apoptosis by regulating the activity of NOT2 independent of its
            kinase activity.
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Zwartjes,C.G., Jayne,S., van den Berg,D.L. and Timmers,H.T.
  TITLE     Repression of promoter activity by CNOT2, a subunit of the
            transcription regulatory Ccr4-not complex
  JOURNAL   J Biol Chem 279 (12), 10848-10854 (2004)
   PUBMED   14707134
  REMARK    GeneRIF: major repression function of CNOT2 is localized in a
            specialized protein motif, the Not-Box
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Denis,C.L. and Chen,J.
  TITLE     The CCR4-NOT complex plays diverse roles in mRNA metabolism
  JOURNAL   Prog Nucleic Acid Res Mol Biol 73, 221-250 (2003)
   PUBMED   12882519
  REMARK    Review article
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092881.8 and AC025569.37.
            
            Summary: This gene encodes a subunit of the multi-component
            CCR4-NOT complex. The CCR4-NOT complex regulates mRNA synthesis and
            degradation and is also thought to be involved in mRNA splicing,
            transport and localization. The encoded protein interacts with
            histone deacetylases and functions as a repressor of polymerase II
            transcription. Alternatively spliced transcript variants have been
            observed for this gene. [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.12663.1,
                                           SRR14038194.2203.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145774, SAMEA2145893
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..520
                     /product="CCR4-NOT transcription complex subunit 2 isoform
                     e"
                     /note="negative regulator of transcription 2;
                     CCR4-associated factor 2; CC chemokine receptor 4-negative
                     regulator of transcription 2"
                     /calculated_mol_wt=57288
     Region          376..499
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..520
                     /gene="CNOT2"
                     /gene_synonym="CDC36; HSPC131; IDNADFS; NOT2; NOT2H"
                     /coded_by="NM_001414658.1:61..1623"
                     /note="isoform e is encoded by transcript variant 12"
                     /db_xref="GeneID:4848"
                     /db_xref="HGNC:HGNC:7878"
                     /db_xref="MIM:604909"
ORIGIN      
        1 mfgasrkkfv egvdsdyhde nmyysqssmf phrsekdmla spstsgqlsq fgaslygqqs
       61 alglpmrgms nntpqlnrsl sqgtqlpshv tpttgvptms lhtppspsrg ilpmnprnmm
      121 nhsqvgqgig ipsrtnsmss sglgspnrss psiicmpkqq psrqpftvns msgfgmnrnq
      181 afgmnnslss nifngtdgse nvtgldlsdf paladrnrre gsgnptplin plagrapyvg
      241 mvtkpaneqs qdfsihnedf palpgssykd ptssnddsks nlntsgktts stdgpkfpgd
      301 kssttqnnnq qkkgiqvlpd grvtnipqgm vtdqfgmigl ltfiraaetd pgmvhlalgs
      361 dlttlglnln spenlypkfa spwasspcrp qdidfhvpse yltnihirdk laaiklgryg
      421 edllfylyym nggdvlqlla avelfnrdwr yhkeervwit rapgmeptmk tntyergtyy
      481 ffdclnwrkv akefhleydk leerphlpst fnynpaqqaf
//
LOCUS       NP_001393548            1043 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 5 [Homo sapiens].
ACCESSION   NP_001393548
VERSION     NP_001393548.1
DBSOURCE    REFSEQ: accession NM_001406619.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1043)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1043)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1043)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1043)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1043)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1043)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1043)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3745975.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1043
                     /product="hamartin isoform 5"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=116145
     Region          16..598
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <587..>839
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1043
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406619.1:473..3604"
                     /note="isoform 5 is encoded by transcript variant 33"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mdtdvvvltt gvlvlitmlp mipqsgkqhl ldffdifgrl sswclkkpgh vaevylvhlh
       61 asvyalfhrl ygmypcnfvs flrshysmke nletfeevvk pmmehvrihp elvtgskdhe
      121 ldprrwkrle thdvviecak isldpteasy edgysvshqi sarfphrsad vttspyadtq
      181 nsygcatstp ystsrlmlln mpgqlpqtls spstrlitep pqatlwspsm vcgmttppts
      241 pgnvppdlsh pyskvfgtta ggkgtplgtp atspppaplc hsddyvhisl pqatvtpprk
      301 eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed siekdkeeaa
      361 isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv npeplhssld
      421 klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp trvgfgsgqp
      481 ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr liqqgadahs
      541 kelnklplps ksvdwthfgg sppsdeirtl rdqllllhnq llyerfkrqq halrnrrllr
      601 kvikaaalee hnaamkdqlk lqekdiqmwk vslqkeqary nqlqeqrdtm vtklhsqirq
      661 lqhdreefyn qsqelqtkle dcrnmiaelr ielkkannkv chtelllsqv sqklsnsesv
      721 qqqmeflnrq llvlgevnel yleqlqnkhs dttkevemmk aayrkelekn rshvlqqtqr
      781 ldtsqkrile leshlakkdh llleqkkyle dvklqargql qaaesryeaq kritqvfele
      841 ildlygrlek dgllkkleee kaeaaeaaee rldccndgcs dsmvghneea sghngetktp
      901 rpssargssg srggggssss sselstpekp phqragpfss rwettmgeas asipttvgsl
      961 pssksflgmk arelfrnkse sqcdedgmts slseslktel gkdlgveaki plnldgphps
     1021 pptpdsvgql himdynethh ehs
//
LOCUS       NP_001424927             991 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 3 isoform 8 [Homo sapiens].
ACCESSION   NP_001424927 XP_047304939 XP_054203922
VERSION     NP_001424927.1
DBSOURCE    REFSEQ: accession NM_001437998.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Wang,H., Lan,S., Wang,L., Zhao,J., Jia,X., Xu,J., Sun,G., Liu,L.,
            Gong,S., Wang,N., Shan,B., Zhang,F. and Zhang,Z.
  TITLE     Expression of circ-PHC3 enhances ovarian cancer progression via
            regulation of the miR-497-5p/SOX9 pathway
  JOURNAL   J Ovarian Res 16 (1), 142 (2023)
   PUBMED   37468993
  REMARK    GeneRIF: Expression of circ-PHC3 enhances ovarian cancer
            progression via regulation of the miR-497-5p/SOX9 pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 991)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 991)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 991)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 991)
  AUTHORS   Crea,F., Di Paolo,A., Liu,H.H., Polillo,M., Clermont,P.L.,
            Guerrini,F., Ciabatti,E., Ricci,F., Barate,C., Fontanelli,G.,
            Barsotti,S., Morganti,R., Danesi,R., Wang,Y., Petrini,M.,
            Galimberti,S. and Helgason,C.D.
  TITLE     Polycomb genes are associated with response to imatinib in chronic
            myeloid leukemia
  JOURNAL   Epigenomics 7 (5), 757-765 (2015)
   PUBMED   26343356
  REMARK    GeneRIF: Data show that polycomb-group proteins BMI1, PHC3, CBX6
            and CBX7 expression was significantly increased during imatinib
            treatment.
REFERENCE   6  (residues 1 to 991)
  AUTHORS   Deshpande,A.M., Akunowicz,J.D., Reveles,X.T., Patel,B.B.,
            Saria,E.A., Gorlick,R.G., Naylor,S.L., Leach,R.J. and Hansen,M.F.
  TITLE     PHC3, a component of the hPRC-H complex, associates with E2F6
            during G0 and is lost in osteosarcoma tumors
  JOURNAL   Oncogene 26 (12), 1714-1722 (2007)
   PUBMED   17001316
  REMARK    GeneRIF: loss of PHC3 may favor tumorigenesis by potentially
            disrupting the ability of cells to remain in G(0)
REFERENCE   7  (residues 1 to 991)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   8  (residues 1 to 991)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 991)
  AUTHORS   Tonkin,E., Hagan,D.M., Li,W. and Strachan,T.
  TITLE     Identification and characterisation of novel mammalian homologues
            of Drosophila polyhomeoticpermits new insights into relationships
            between members of the polyhomeotic family
  JOURNAL   Hum Genet 111 (4-5), 435-442 (2002)
   PUBMED   12384788
REFERENCE   10 (residues 1 to 991)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC023891.28 and AC008040.7.
            
            On or before Apr 14, 2025 this sequence version replaced
            XP_047304939.1, XP_054203922.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2314630.1,
                                           SRR14038194.1924647.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.2"
     Protein         1..991
                     /product="polyhomeotic-like protein 3 isoform 8"
                     /note="early development regulator 3; polyhomeotic-like
                     protein 3; homolog of polyhomeotic 3; early development
                     regulatory protein 3; polyhomeotic like 3"
                     /calculated_mol_wt=106881
     Region          <354..>514
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     Region          922..990
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(940..941,975..976,979..980,983)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(951..955,957..958,961..962,966,971)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..991
                     /gene="PHC3"
                     /gene_synonym="EDR3; HPH3"
                     /coded_by="NM_001437998.1:19..2994"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:80012"
                     /db_xref="HGNC:HGNC:15682"
                     /db_xref="MIM:620031"
ORIGIN      
        1 maeaefkdhs tamdtepnpg tssvstttss tttttittss srmqqpqisv ysgsdrhavq
       61 alhrppssaa qylqqmyaaq qqhlmlhtaa lqqqhlsssq lqslaavqas lssgrpstsp
      121 tgsvtqqssm sqtsinlsts ptpaqlisrs qassstsgsi tqqtmllgst sptltasqaq
      181 mylraqmlif tpattvaavq sdipvvssss ssscqsaatq vqnltlrsqk lgvlsssqng
      241 ppkstsqtqs ltichnkttv tsskisqrdp spesnkkges pslesrstav trtssihqli
      301 apasyspiqp hslikhqqip lhsppskvsh hqlilqqqqq qiqpitlqns tqdpppsqhc
      361 iplqnhglpp apsnaqsqhc spiqshpspl tvspnqsqsa qqsvvvsppp phspsqspti
      421 iihpqaliqp hplvssalqp gpnlqqstan qvqataqlnl pshlplpasp vvhigpvqqs
      481 alvspgqqiv spshqqyssl qsspipiasp pqmstsppaq ipplplqsmq slqvqpeils
      541 qgqvlvqnal vseeelpaae alvqlpfqtl pppqtvavnl qvqppapvdp pvvyqvedvc
      601 eeempeesde cvrmdrtppp ptlspaaitv grgedltseh plleqvelpa vasvsasvik
      661 spsdpshvsv pppplllpaa ttrsnstsmh ssipsienkp pqaivkpqil thviegfviq
      721 eglepfpvsr ssllieqpvk krplldnqvi nsvcvqpelq nntkhadnss dtemedmiae
      781 etleemdsel lkcefcgkmg yaneflrskr fctmscakry nvscskkfal srwnrkpdnq
      841 slghrgrrps gpdgaarehi lrqlpityps aeedlashed svpsamttrl rrqsererer
      901 elrdvrirkm pensdllpva qtepsiwtvd dvwafihslp gcqdiadefr aqeidgqall
      961 llkedhlmsa mniklgpalk icarinslke s
//
LOCUS       NP_001397934            1163 aa            linear   PRI 21-NOV-2025
DEFINITION  phospholipid-transporting ATPase IB isoform 3 [Homo sapiens].
ACCESSION   NP_001397934 XP_011533405
VERSION     NP_001397934.1
DBSOURCE    REFSEQ: accession NM_001411005.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1163)
  AUTHORS   Matsell,E., Mazaheri,M., Andersen,J.P. and Molday,R.S.
  TITLE     Structural and functional properties of the N- and C-terminal
            segments of the P4-ATPase phospholipid flippase ATP8A2
  JOURNAL   J Biol Chem 301 (1), 108065 (2025)
   PUBMED   39662833
REFERENCE   2  (residues 1 to 1163)
  AUTHORS   Matsell,E., Andersen,J.P. and Molday,R.S.
  TITLE     Functional and in silico analysis of ATP8A2 and other P4-ATPase
            variants associated with human genetic diseases
  JOURNAL   Dis Model Mech 17 (6) (2024)
   PUBMED   38436085
  REMARK    GeneRIF: Functional and in silico analysis of ATP8A2 and other
            P4-ATPase variants associated with human genetic diseases.
REFERENCE   3  (residues 1 to 1163)
  AUTHORS   Mogensen,L.S., Mikkelsen,S.A., Tadini-Buoninsegni,F., Holm,R.,
            Matsell,E., Vilsen,B., Molday,R.S. and Andersen,J.P.
  TITLE     On the track of the lipid transport pathway of the phospholipid
            flippase ATP8A2 - Mutation analysis of residues of the
            transmembrane segments M1, M2, M3 and M4
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (1), 119570 (2024)
   PUBMED   37678495
  REMARK    GeneRIF: On the track of the lipid transport pathway of the
            phospholipid flippase ATP8A2 - Mutation analysis of residues of the
            transmembrane segments M1, M2, M3 and M4.
            Review article
REFERENCE   4  (residues 1 to 1163)
  AUTHORS   van der Mark,V.A., Elferink,R.P. and Paulusma,C.C.
  TITLE     P4 ATPases: flippases in health and disease
  JOURNAL   Int J Mol Sci 14 (4), 7897-7922 (2013)
   PUBMED   23579954
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1163)
  AUTHORS   Coleman,J.A. and Molday,R.S.
  TITLE     Critical role of the beta-subunit CDC50A in the stable expression,
            assembly, subcellular localization, and lipid transport activity of
            the P4-ATPase ATP8A2
  JOURNAL   J Biol Chem 286 (19), 17205-17216 (2011)
   PUBMED   21454556
  REMARK    GeneRIF: CDC50A is the beta-subunit of ATP8A2 and is crucial for
            the correct folding, stable expression, export from endoplasmic
            reticulum, and phosphatidylserine flippase activity of ATP8A2
REFERENCE   6  (residues 1 to 1163)
  AUTHORS   van der Velden,L.M., Wichers,C.G., van Breevoort,A.E.,
            Coleman,J.A., Molday,R.S., Berger,R., Klomp,L.W. and van de
            Graaf,S.F.
  TITLE     Heteromeric interactions required for abundance and subcellular
            localization of human CDC50 proteins and class 1 P4-ATPases
  JOURNAL   J Biol Chem 285 (51), 40088-40096 (2010)
   PUBMED   20947505
REFERENCE   7  (residues 1 to 1163)
  AUTHORS   Cacciagli,P., Haddad,M.R., Mignon-Ravix,C., El-Waly,B., Moncla,A.,
            Missirian,C., Chabrol,B. and Villard,L.
  TITLE     Disruption of the ATP8A2 gene in a patient with a t(10;13) de novo
            balanced translocation and a severe neurological phenotype
  JOURNAL   Eur J Hum Genet 18 (12), 1360-1363 (2010)
   PUBMED   20683487
REFERENCE   8  (residues 1 to 1163)
  AUTHORS   Coleman,J.A., Kwok,M.C. and Molday,R.S.
  TITLE     Localization, purification, and functional reconstitution of the
            P4-ATPase Atp8a2, a phosphatidylserine flippase in photoreceptor
            disc membranes
  JOURNAL   J Biol Chem 284 (47), 32670-32679 (2009)
   PUBMED   19778899
  REMARK    GeneRIF: P4-ATPase Atp8a2 is a phosphatidylserine flippase in
            photoreceptor disc membranes
REFERENCE   9  (residues 1 to 1163)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1163)
  AUTHORS   Sun,X.L., Li,D., Fang,J., Noyes,I., Casto,B., Theil,K., Shuler,C.
            and Milo,G.E.
  TITLE     Changes in levels of normal ML-1 gene transcripts associated with
            the conversion of human nontumorigenic to tumorigenic phenotypes
  JOURNAL   Gene Expr 8 (2), 129-139 (1999)
   PUBMED   10551800
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138958.18, AL356316.18,
            AL669971.2, AL136438.10, AL157366.12, AL138815.6 and AL139004.11.
            
            On Aug 20, 2022 this sequence version replaced XP_011533405.1.
            
            Summary: The protein encoded by this gene is a member of the P4
            ATPase family of proteins, which are thought to be involved in a
            process called lipid flipping, whereby phospholipids are
            translocated inwards from the exoplasmic leaflet to the cytosolic
            leaflet of the cell membrane, which aids in generating and
            maintaining asymmetry in membrane lipids. This protein is predicted
            to contain an E1 E2 ATPase, a haloacid dehalogenase-like hydrolase
            (HAD) domain, and multiple transmembrane domains. Associations
            between this protein and cell cycle control protein 50A are
            important for translocation of phosphatidylserine across membranes.
            Mutations in this gene have been associated with a syndrome
            (CAMRQ4) characterized by cerebellar ataxia and cognitive
            disabilities. In addition, a translocation breakpoint within this
            gene was observed in an individual with neurological dysfunction.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Jul 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.228684.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.13"
     Protein         1..1163
                     /product="phospholipid-transporting ATPase IB isoform 3"
                     /EC_number="7.6.2.1"
                     /note="ATPase, aminophospholipid transporter-like, class
                     I, type 8A, member 2; probable phospholipid-transporting
                     ATPase IB; P4-ATPase flippase complex alpha subunit
                     ATP8A2; ATPase, aminophospholipid transporter, class I,
                     type 8A, member 2"
                     /calculated_mol_wt=130506
     Region          68..1081
                     /region_name="ATPase-Plipid"
                     /note="phospholipid-translocating P-type ATPase, flippase;
                     TIGR01652"
                     /db_xref="CDD:273734"
     Site            order(428..430,569,592..594,658,705..707,795,798,801,821,
                     824)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     CDS             1..1163
                     /gene="ATP8A2"
                     /gene_synonym="ATP; ATPIB; CAMRQ4; IB; ML-1"
                     /coded_by="NM_001411005.1:240..3731"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS91793.1"
                     /db_xref="GeneID:51761"
                     /db_xref="HGNC:HGNC:13533"
                     /db_xref="MIM:605870"
ORIGIN      
        1 mlngagldka lkmslprrsr irssvgpvrs slgykkaede msratsvgdq leapartiyl
       61 nqphlnkfrd nqistakysv ltflprflye qirraanaff lfiallqqip dvsptgrytt
      121 lvpliiilti agikeivedf krhkadnavn kkktivlrng mwhtimwkev avgdivkvvn
      181 gqylpadvvl lsssepqamc yvetanldge tnlkirqgls htadmqtrev lmklsgtiec
      241 egpnrhlydf tgnlnldgks lvalgpdqil lrgtqlrntq wvfgivvytg hdtklmqnst
      301 kaplkrsnve kvtnvqilvl fgillvmalv ssagalywnr shgeknwyik kmdttsdnfg
      361 ynlltfiily nnlipisllv tlevvkytqa lfinwdtdmy yigndtpama rtsnlneelg
      421 qvkylfsdkt gtltcnimnf kkcsiagvty ghfpelarep ssddfcrmpp pcsdscdfdd
      481 prllkniedr hptapciqef ltllavchtv vpekdgdnii yqasspdeaa lvkgakklgf
      541 vftartpfsv iieamgqeqt fgilnvlefs sdrkrmsviv rtpsgrlrly ckgadnvife
      601 rlskdskyme etlchleyfa teglrtlcva yadlseneye ewlkvyqeas tilkdraqrl
      661 eecyeiiekn llllgataie drlqagvpet iatllkaeik iwvltgdkqe tainigyscr
      721 lvsqnmalil lkedsldatr aaitqhctdl gnllgkendv aliidghtlk yalsfevrrs
      781 fldlalscka viccrvsplq kseivdvvkk rvkaitlaig dgandvgmiq tahvgvgisg
      841 negmqatnns dyaiaqfsyl eklllvhgaw synrvtkcil ycfyknvvly iieiftalpp
      901 ftlgifersc tqesmlrfpq lykitqngeg fntkvfwghc inalvhslil fwfpmkaleh
      961 dtvltsghat dylfvgnivy tyvvvtvclk aglettawtk fshlavwgsm ltwlvffgiy
     1021 stiwptipia pdmrgqatmv lssahfwlgl flvptaclie dvawraakht ckktlleevq
     1081 eletksrvlg kavlrdsngk rlnerdrlik rlgrktpptl frgsslqqgv phgyafsqee
     1141 hgavsqeevi raydttkkks rkk
//
LOCUS       NP_001427363            1280 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 isoform 1
            [Homo sapiens].
ACCESSION   NP_001427363
VERSION     NP_001427363.1
DBSOURCE    REFSEQ: accession NM_001440434.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1280)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1280)
  AUTHORS   Ji,X., Wu,Q., Cao,X., Liu,S., Zhang,J., Chen,S., Shan,J., Zhang,Y.,
            Li,B. and Zhao,H.
  TITLE     Helicobacter pylori East Asian type CagA hijacks more SHIP2 by its
            EPIYA-D motif to potentiate the oncogenicity
  JOURNAL   Virulence 15 (1), 2375549 (2024)
   PUBMED   38982595
  REMARK    GeneRIF: Helicobacter pylori East Asian type CagA hijacks more
            SHIP2 by its EPIYA-D motif to potentiate the oncogenicity.
REFERENCE   3  (residues 1 to 1280)
  AUTHORS   Ando,K., Kucukali,F., Doeraene,E., Nagaraj,S., Antonelli,E.M.,
            Thazin Htut,M., Yilmaz,Z., Kosa,A.C., Lopez-Guitierrez,L.,
            Quintanilla-Sanchez,C., Aydin,E., Ramos,A.R., Mansour,S.,
            Turbant,S., Schurmans,S., Sleegers,K., Erneux,C., Brion,J.P. and
            Leroy,K.
  CONSRTM   Brain Bank NeuroCEB Neuropathology Network
  TITLE     Alteration of gene expression and protein solubility of the PI
            5-phosphatase SHIP2 are correlated with Alzheimer's disease
            pathology progression
  JOURNAL   Acta Neuropathol 147 (1), 94 (2024)
   PUBMED   38833073
  REMARK    GeneRIF: Alteration of gene expression and protein solubility of
            the PI 5-phosphatase SHIP2 are correlated with Alzheimer's disease
            pathology progression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1280)
  AUTHORS   Bradshaw,W.J., Kennedy,E.C., Moreira,T., Smith,L.A., Chalk,R.,
            Katis,V.L., Benesch,J.L.P., Brennan,P.E., Murphy,E.J. and
            Gileadi,O.
  TITLE     Regulation of inositol 5-phosphatase activity by the C2 domain of
            SHIP1 and SHIP2
  JOURNAL   Structure 32 (4), 453-466 (2024)
   PUBMED   38309262
  REMARK    GeneRIF: Regulation of inositol 5-phosphatase activity by the C2
            domain of SHIP1 and SHIP2.
REFERENCE   5  (residues 1 to 1280)
  AUTHORS   Habib,T., Hejna,J.A., Moses,R.E. and Decker,S.J.
  TITLE     Growth factors and insulin stimulate tyrosine phosphorylation of
            the 51C/SHIP2 protein
  JOURNAL   J Biol Chem 273 (29), 18605-18609 (1998)
   PUBMED   9660833
REFERENCE   6  (residues 1 to 1280)
  AUTHORS   Le Drean,E., Vely,F., Olcese,L., Cambiaggi,A., Guia,S., Krystal,G.,
            Gervois,N., Moretta,A., Jotereau,F. and Vivier,E.
  TITLE     Inhibition of antigen-induced T cell response and antibody-induced
            NK cell cytotoxicity by NKG2A: association of NKG2A with SHP-1 and
            SHP-2 protein-tyrosine phosphatases
  JOURNAL   Eur J Immunol 28 (1), 264-276 (1998)
   PUBMED   9485206
  REMARK    Erratum:[Eur J Immunol 1998 Mar;28(3):1122]
REFERENCE   7  (residues 1 to 1280)
  AUTHORS   Pesesse,X., Deleu,S., De Smedt,F., Drayer,L. and Erneux,C.
  TITLE     Identification of a second SH2-domain-containing protein closely
            related to the phosphatidylinositol polyphosphate 5-phosphatase
            SHIP
  JOURNAL   Biochem Biophys Res Commun 239 (3), 697-700 (1997)
   PUBMED   9367831
REFERENCE   8  (residues 1 to 1280)
  AUTHORS   Hejna,J.A., Saito,H., Merkens,L.S., Tittle,T.V., Jakobs,P.M.,
            Whitney,M.A., Grompe,M., Friedberg,A.S. and Moses,R.E.
  TITLE     Cloning and characterization of a human cDNA (INPPL1) sharing
            homology with inositol polyphosphate phosphatases
  JOURNAL   Genomics 29 (1), 285-287 (1995)
   PUBMED   8530088
REFERENCE   9  (residues 1 to 1280)
  AUTHORS   Huang,S., Earl,D. and White,K.
  TITLE     INPPL1-Related Opsismodysplasia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   40504975
REFERENCE   10 (residues 1 to 1280)
  AUTHORS   Slama,V. and Dudek,J.
  TITLE     [Stability of diluted solutions of peracetic acid]
  JOURNAL   Cesk Farm 17 (1), 40-41 (1968)
   PUBMED   5668240
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000593.4.
            
            Summary: The protein encoded by this gene is an SH2-containing
            5'-inositol phosphatase that is involved in the regulation of
            insulin function. The encoded protein also plays a role in the
            regulation of epidermal growth factor receptor turnover and actin
            remodelling. Additionally, this gene supports metastatic growth in
            breast cancer and is a valuable biomarker for breast cancer.
            [provided by RefSeq, Jan 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1280
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..1280
                     /product="phosphatidylinositol 3,4,5-trisphosphate
                     5-phosphatase 2 isoform 1"
                     /EC_number="3.1.3.86"
                     /note="SH2 domain-containing inositol-5'-phosphatase 2;
                     51C protein; protein 51C; phosphatidylinositol
                     3,4,5-trisphosphate 5-phosphatase 2"
                     /calculated_mol_wt=140825
     Region          17..119
                     /region_name="SH2_SHIP"
                     /note="Src homology 2 (SH2) domain found in SH2-containing
                     inositol-5'-phosphatase (SHIP) and SLAM-associated protein
                     (SAP); cd10343"
                     /db_xref="CDD:198206"
     Site            order(28,47,68,70)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198206"
     Site            order(68..69,81..82,87,90,106..108)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198206"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          446..749
                     /region_name="INPP5c_SHIP2-INPPL1"
                     /note="Catalytic inositol polyphosphate 5-phosphatase
                     (INPP5c) domain of SH2 domain containing inositol
                     5-phosphatase-2 and related proteins; cd09101"
                     /db_xref="CDD:197335"
     Site            order(454,456,495,562..563,583,586..587,629,631,633,
                     683..684,706,712,739..740)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197335"
     Site            order(454,495,583,629,631,712,739..740)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197335"
     Site            order(495,562..563,583,586..587,633,683..684,706,739)
                     /site_type="other"
                     /note="putative PI/IP binding site [chemical binding]"
                     /db_xref="CDD:197335"
     Site            order(495,739)
                     /site_type="other"
                     /note="putative Mg binding site [ion binding]"
                     /db_xref="CDD:197335"
     Site            order(583,631,740)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197335"
     Site            908
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            912
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          919..1140
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Region          <921..1236
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          966..971
                     /region_name="SH3-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Site            980
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17219406,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          1005..1008
                     /region_name="NPXY motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Site            1008
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:11349134,
                     ECO:0000269|PubMed:12235291; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            1153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            1157
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            1184
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:11687594,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          1216..1278
                     /region_name="SAM_Ship2"
                     /note="SAM domain of Ship2 lipid phosphatase proteins;
                     cd09491"
                     /db_xref="CDD:188890"
     Site            order(1244..1246,1248..1249,1252,1257)
                     /site_type="other"
                     /note="heterodimer interface ML [polypeptide binding]"
                     /db_xref="CDD:188890"
     Site            1279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     CDS             1..1280
                     /gene="INPPL1"
                     /gene_synonym="OPSMD; SHIP2"
                     /coded_by="NM_001440434.1:219..4061"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:3636"
                     /db_xref="HGNC:HGNC:6080"
                     /db_xref="MIM:600829"
ORIGIN      
        1 masacgapgp ggalgsqaps wyhrdlsraa aeellaragr dgsflvrdse svagafalcv
       61 lyqkhvhtyr ilpdgedfla vqtsqgvpvr rfqtlgelig lyaqpnqglv calllpvege
      121 repdppddrd asdgedekpp lpprsgstsi saptgpsspl papetptapa aerdgaevlg
      181 qvsrtstdfl tppqsapngl stvshdylkg sygldleavr ggashlphlt rtlatscrrl
      241 hsevdkvlsg leilskvfdq qsspmvtrll qqqnlpqtge qeleslvlkl svlkdflsgi
      301 qkkalkalqd msstappapq pstrkaktip vqafevkldv tlgdltkigk sqkftlsvdv
      361 eggrlvllrr qrdsqedwtt fthdrirqli ksqrvqnklg vvfekekdrt qrkdfifvsa
      421 rkreafcqll qlmknkhskq depdmisvfi gtwnmgsvpp pknvtswfts kglgktldev
      481 tvtiphdiyv fgtqensvgd rewldllrgg lkeltdldyr piamqslwni kvavlvkpeh
      541 enrishvsts svktgiantl gnkgavgvsf mfngtsfgfv nchltsgnek tarrnqnyld
      601 ilrllslgdr qlnafdislr fthlfwfgdl nyrldmdiqe ilnyisrkef epllrvdqln
      661 lerekhkvfl rfseeeisfp ptyryergsr dtyawhkqkp tgvrtnvpsw cdrilwksyp
      721 ethiicnsyg ctddivtsdh spvfgtfevg vtsqfiskkg lsktsdqayi efesieaivk
      781 tasrtkffie fystcleeyk ksfendaqss dninflkvqw ssrqlptlkp iladieylqd
      841 qhllltvksm dgyesygecv valksmigst aqqfltflsh rgeetgnirg smkvrvpter
      901 lgtrerlyew isidkdeaga kskapsvsrg sqeprsgsrk pafteascpl srlfeepekp
      961 pptgrppapp raapreeplt prlkpegape pegvaapppk nsfnnpayyv legvphqllp
     1021 peppsparap vpsatknkva itvpapqlgh hrhprvgegs ssdeesggtl pppdfppppl
     1081 pdsaiflpps ldplpgpvvr grggaeargp pppkahprpp lppgpspast flgevasgdd
     1141 rscsvlqmak tlsevdyapa gparsallpg plelqpprgl psdygrplsf pppriresiq
     1201 edlaeeapcl qggrasglge agmsawlrai gleryeeglv hngwddlefl sditeedlee
     1261 agvqdpahkr llldtlqlsk
//
LOCUS       NP_001397682             810 aa            linear   PRI 21-NOV-2025
DEFINITION  mitogen-activated protein kinase kinase kinase kinase 3 isoform 3
            [Homo sapiens].
ACCESSION   NP_001397682 XP_047302049
VERSION     NP_001397682.1
DBSOURCE    REFSEQ: accession NM_001410753.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 810)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 810)
  AUTHORS   Chuang,H.C., Hung,W.T., Chen,Y.M., Hsu,P.M., Yen,J.H., Lan,J.L. and
            Tan,T.H.
  TITLE     Genomic sequencing and functional analyses identify MAP4K3/GLK
            germline and somatic variants associated with systemic lupus
            erythematosus
  JOURNAL   Ann Rheum Dis 81 (2), 243-254 (2022)
   PUBMED   34610951
  REMARK    GeneRIF: Genomic sequencing and functional analyses identify
            MAP4K3/GLK germline and somatic variants associated with systemic
            lupus erythematosus.
REFERENCE   3  (residues 1 to 810)
  AUTHORS   Song,Y., Zhang,F., Li,L., Song,B., Xu,J., Wang,G. and Zheng,Z.
  TITLE     MiR-338-3p inhibits growth of glioblastoma through targeting MAP4K3
  JOURNAL   Minerva Med 112 (4), 531-533 (2021)
   PUBMED   31578840
  REMARK    GeneRIF: MiR-338-3p inhibits growth of glioblastoma through
            targeting MAP4K3.
REFERENCE   4  (residues 1 to 810)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 810)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   6  (residues 1 to 810)
  AUTHORS   Bandyopadhyay,S., Chiang,C.Y., Srivastava,J., Gersten,M., White,S.,
            Bell,R., Kurschner,C., Martin,C., Smoot,M., Sahasrabudhe,S.,
            Barber,D.L., Chanda,S.K. and Ideker,T.
  TITLE     A human MAP kinase interactome
  JOURNAL   Nat Methods 7 (10), 801-805 (2010)
   PUBMED   20936779
REFERENCE   7  (residues 1 to 810)
  AUTHORS   Yan,L., Mieulet,V., Burgess,D., Findlay,G.M., Sully,K., Procter,J.,
            Goris,J., Janssens,V., Morrice,N.A. and Lamb,R.F.
  TITLE     PP2A T61 epsilon is an inhibitor of MAP4K3 in nutrient signaling to
            mTOR
  JOURNAL   Mol Cell 37 (5), 633-642 (2010)
   PUBMED   20227368
  REMARK    GeneRIF: Amino acid sufficiency phosphorylates MAP4K3/Ser170,
            activating mTORC1, but amino acid restriction causes MAP4K3 to
            interact with PP2A(T61 epsilon), promoting dephosphorylation of
            Ser170, MAP4K3 inhibition, and, inhibition of mTORC1 signaling.
REFERENCE   8  (residues 1 to 810)
  AUTHORS   Lam,D. and Martins,L.M.
  TITLE     MAP4K3 enhances the expression of the BH3-only protein BID
  JOURNAL   Cell Cycle 8 (20), 3248-3249 (2009)
   PUBMED   19806019
REFERENCE   9  (residues 1 to 810)
  AUTHORS   Lam,D., Dickens,D., Reid,E.B., Loh,S.H., Moisoi,N. and Martins,L.M.
  TITLE     MAP4K3 modulates cell death via the post-transcriptional regulation
            of BH3-only proteins
  JOURNAL   Proc Natl Acad Sci U S A 106 (29), 11978-11983 (2009)
   PUBMED   19587239
  REMARK    GeneRIF: MAP4K3 orchestrates activation of BAX via the concerted
            posttranscriptional modulation of PUMA, BAD, and BIM.
REFERENCE   10 (residues 1 to 810)
  AUTHORS   Diener,K., Wang,X.S., Chen,C., Meyer,C.F., Keesler,G., Zukowski,M.,
            Tan,T.H. and Yao,Z.
  TITLE     Activation of the c-Jun N-terminal kinase pathway by a novel
            protein kinase related to human germinal center kinase
  JOURNAL   Proc Natl Acad Sci U S A 94 (18), 9687-9692 (1997)
   PUBMED   9275185
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007684.3 and AC079615.6.
            
            On Aug 15, 2022 this sequence version replaced XP_047302049.1.
            
            Summary: This gene encodes a member of the mitogen-activated
            protein kinase kinase kinase kinase family. The encoded protein
            activates key effectors in cell signalling, among them c-Jun.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Jul 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1654137.1,
                                           SRR18074967.1912228.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..810
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.1"
     Protein         1..810
                     /product="mitogen-activated protein kinase kinase kinase
                     kinase 3 isoform 3"
                     /EC_number="2.7.11.1"
                     /note="germinal center kinase-related protein kinase;
                     germinal center kinase-like kinase; MEK kinase kinase 3;
                     MAPK/ERK kinase kinase kinase 3"
                     /calculated_mol_wt=91790
     Region          1..210
                     /region_name="STKc_MAP4K3_like"
                     /note="Catalytic domain of Mitogen-activated protein
                     kinase kinase kinase kinase (MAP4K) 3-like
                     Serine/Threonine Kinases; cd06613"
                     /db_xref="CDD:270788"
     Site            order(73,75..77,94,108..111,113,143,152)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270788"
     Site            order(90..101,104..113)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270788"
     Region          477..790
                     /region_name="CNH"
                     /note="Domain found in NIK1-like kinases, mouse citron and
                     yeast ROM1, ROM2; smart00036"
                     /db_xref="CDD:214481"
     CDS             1..810
                     /gene="MAP4K3"
                     /gene_synonym="GLK; MAPKKKK3; MEKKK 3; MEKKK3; RAB8IPL1"
                     /coded_by="NM_001410753.1:430..2862"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92741.1"
                     /db_xref="GeneID:8491"
                     /db_xref="HGNC:HGNC:6865"
                     /db_xref="MIM:604921"
ORIGIN      
        1 mmkdckhpni vayfgsylrr dklwicmefc gggslqdiyh vtgplselqi ayvsretlqg
       61 lyylhskgkm hrdikganil ltdnghvkla dfgvsaqita tiakrksfig tpywmapeva
      121 averkggynq lcdlwavgit aielaelqpp mfdlhpmral flmtksnfqp pklkdkmkws
      181 nsfhhfvkma ltknpkkrpt aekllqhpfv tqhltrslai elldkvnnpd hstyhdfddd
      241 dpeplvavph rihstsrnvr eektrseitf gqvkfdpplr ketephheld lqleygqghq
      301 ggyflganks llksveeelh qrghvahled degdddeskh stlkakippp lppkpksifi
      361 pqemhstede nqgtikrcpm sgspakpsqv pprpppprlp phkpvalgng mssfqlnger
      421 dgslcqqqne hrgtnlsrke kkdvpkpisn glpptpkvhm gacfskvfng cplkihcass
      481 winpdtrdqy lifgaeegiy tlnlnelhet smeqlfprrc twlyvmnncl lsisgkasql
      541 yshnlpglfd yarqmqklpv aipahklpdr ilprkfsvsa kipetkwcqk ccvvrnpytg
      601 hkylcgalqt sivllewvep mqkfmlikhi dfpipcplrm femlvvpeqe yplvcvgvsr
      661 grdfnqvvrf etvnpnstss wftesdtpqt nvthvtqler dtilvcldcc ikivnlqgrl
      721 kssrklssel tfdfqiesiv clqdsvlafw khgmqgrsfr snevtqeisd strifrllgs
      781 drvvvlesrp tdnptansnl yilaghensy
//
LOCUS       NP_001400668            1002 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform b [Homo sapiens].
ACCESSION   NP_001400668
VERSION     NP_001400668.1
DBSOURCE    REFSEQ: accession NM_001413739.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1002)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1002)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1002)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1002)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1002)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 1002)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 1002)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 1002)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 1002)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 1002)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4454476.1,
                                           SRR18074969.2705467.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1002
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..1002
                     /product="polyhomeotic-like protein 1 isoform b"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=105178
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          210..239
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          259..353
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          430..510
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          <472..668
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          554..587
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          634..670
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P78364.3)"
     Region          826..933
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          846..926
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Site            896
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P78364.3)"
     Site            920
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P78364.3)"
     Region          933..1001
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(951..952,986..987,990..991,994)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(962..966,968..969,972..973,977,982)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..1002
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413739.1:368..3376"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq asinlattsa aqlisrsqsv
      121 sspsattltq svllgnttsp plnqsqaqmy lrlgnllqvn rtlgrnvpla sqlilmpnga
      181 vaavqqevps aqspgvhada dqvqnlavrn qqasaqgpqm qgstqkaipp gaspvsslsq
      241 assqalavaq assgatnqsl nlsqagggsg nsipgsmgpg gggqahgglg qlpssgmggg
      301 scprkgtgvv qplpaaqtvt vsqgsqteae saaakkaead gsgqqnvgmn ltrtatpaps
      361 qtlissatyt qiqphsliqq qqqihlqqkq vviqqqiaih hqqqfqhrqs qllhtathlq
      421 laqqqqqqqq qqqqqqqpqa ttltapqppq vpptqqvpps qsqqqaqtlv vqpmlqsspl
      481 slppdaapkp pipiqskppv apikppqlga akmsaaqqpp phipvqvvgt rqpgtaqaqa
      541 lglaqlaaav ptsrgmpgtv qsgqahlass ppssqapgal qecpptlapg mtlapvqgta
      601 hvvkggatts spvvaqvpaa fymqsvhlpg kpqtlavkrk adseeerddv stlgsmlpak
      661 aspvaespkv mdeksslgek aesvanvnan tpsselvalt papsvppptl amvsrqmgds
      721 kppqaivkpq ilthiiegfv iqegaepfpv gcsqllkese kplqtglptg ltenqsggpl
      781 gvdspsaeld kkanllkcey cgkyapaeqf rgskrfcsmt cakrynvscs hqfrlkrkkm
      841 kefqeanyar vrrrgprrss sdiarakiqg kchrgqedss rgsdnssyde alsptspgpl
      901 svraghgerd lgnpntappt pelhginpvf lssnpsrwsv eevyefiasl qgcqeiaeef
      961 rsqeidgqal lllkeehlms amniklgpal kicakinvlk et
//
LOCUS       NP_001425597             840 aa            linear   PRI 21-NOV-2025
DEFINITION  dipeptidyl peptidase 8 isoform 6 [Homo sapiens].
ACCESSION   NP_001425597 XP_047288716 XP_054234277
VERSION     NP_001425597.1
DBSOURCE    REFSEQ: accession NM_001438668.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 840)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 840)
  AUTHORS   Li,K., Zhang,Y., Zhao,W., Wang,R., Li,Y., Wei,L., Wang,L., Chen,X.,
            Chen,Z., Liu,P., Nie,N., Tian,X. and Fu,R.
  TITLE     DPP8/9 inhibition attenuates the TGF-beta1-induced excessive
            deposition of extracellular matrix (ECM) in human mesangial cells
            via Smad and Akt signaling pathways
  JOURNAL   Toxicol Lett 395, 1-10 (2024)
   PUBMED   38458339
  REMARK    GeneRIF: DPP8/9 inhibition attenuates the TGF-beta1-induced
            excessive deposition of extracellular matrix (ECM) in human
            mesangial cells via Smad and Akt signaling pathways.
REFERENCE   3  (residues 1 to 840)
  AUTHORS   Zhang,Y., Li,K., Li,Y., Zhao,W., Wang,L., Chen,Z., Ma,X., Yao,T.,
            Wang,J., Dong,W., Li,X., Tian,X. and Fu,R.
  TITLE     Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the
            proximal renal tubule epithelial cells
  JOURNAL   Pharmacol Res 169, 105630 (2021)
   PUBMED   33932609
  REMARK    GeneRIF: Profibrotic mechanisms of DPP8 and DPP9 highly expressed
            in the proximal renal tubule epithelial cells.
REFERENCE   4  (residues 1 to 840)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 840)
  AUTHORS   Hollingsworth,L.R., Sharif,H., Griswold,A.R., Fontana,P.,
            Mintseris,J., Dagbay,K.B., Paulo,J.A., Gygi,S.P., Bachovchin,D.A.
            and Wu,H.
  TITLE     DPP9 sequesters the C terminus of NLRP1 to repress inflammasome
            activation
  JOURNAL   Nature 592 (7856), 778-783 (2021)
   PUBMED   33731932
REFERENCE   6  (residues 1 to 840)
  AUTHORS   Chen,Y.S., Chien,C.H., Goparaju,C.M., Hsu,J.T., Liang,P.H. and
            Chen,X.
  TITLE     Purification and characterization of human prolyl dipeptidase DPP8
            in Sf9 insect cells
  JOURNAL   Protein Expr Purif 35 (1), 142-146 (2004)
   PUBMED   15039077
REFERENCE   7  (residues 1 to 840)
  AUTHORS   Shu,H., Chen,S., Bi,Q., Mumby,M. and Brekken,D.L.
  TITLE     Identification of phosphoproteins and their phosphorylation sites
            in the WEHI-231 B lymphoma cell line
  JOURNAL   Mol Cell Proteomics 3 (3), 279-286 (2004)
   PUBMED   14729942
REFERENCE   8  (residues 1 to 840)
  AUTHORS   Qi,S.Y., Riviere,P.J., Trojnar,J., Junien,J.L. and Akinsanya,K.O.
  TITLE     Cloning and characterization of dipeptidyl peptidase 10, a new
            member of an emerging subgroup of serine proteases
  JOURNAL   Biochem J 373 (Pt 1), 179-189 (2003)
   PUBMED   12662155
REFERENCE   9  (residues 1 to 840)
  AUTHORS   Ajami,K., Abbott,C.A., Obradovic,M., Gysbers,V., Kahne,T.,
            McCaughan,G.W. and Gorrell,M.D.
  TITLE     Structural requirements for catalysis, expression, and dimerization
            in the CD26/DPIV gene family
  JOURNAL   Biochemistry 42 (3), 694-701 (2003)
   PUBMED   12534281
REFERENCE   10 (residues 1 to 840)
  AUTHORS   Abbott,C.A., Yu,D.M., Woollatt,E., Sutherland,G.R., McCaughan,G.W.
            and Gorrell,M.D.
  TITLE     Cloning, expression and chromosomal localization of a novel human
            dipeptidyl peptidase (DPP) IV homolog, DPP8
  JOURNAL   Eur J Biochem 267 (20), 6140-6150 (2000)
   PUBMED   11012666
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011846.16 and AC105129.4.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047288716.1, XP_054234277.1.
            
            Summary: This gene encodes a member of the peptidase S9B family, a
            small family of dipeptidyl peptidases that are able to cleave
            peptide substrates at a prolyl bond. The encoded protein shares
            similarity with dipeptidyl peptidase IV in that it is ubiquitously
            expressed, and hydrolyzes the same substrates. These similarities
            suggest that, like dipeptidyl peptidase IV, this protein may play a
            role in T-cell activation and immune function. Alternatively
            spliced transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3011806.1,
                                           SRR14038196.1838341.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..840
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..840
                     /product="dipeptidyl peptidase 8 isoform 6"
                     /EC_number="3.4.14.5"
                     /note="prolyl dipeptidase DPP8; dipeptidyl peptidase VIII;
                     DPP VIII; dipeptidyl peptidase IV-related protein 1"
                     /calculated_mol_wt=96814
     Region          8..143
                     /region_name="Dpp_8_9_N"
                     /note="Dipeptidyl peptidase 8 and 9 N-terminal; pfam19520"
                     /db_xref="CDD:466112"
     Region          142..537
                     /region_name="DPPIV_N"
                     /note="Dipeptidyl peptidase IV (DPP IV) N-terminal region;
                     pfam00930"
                     /db_xref="CDD:395744"
     Region          629..833
                     /region_name="Peptidase_S9"
                     /note="Prolyl oligopeptidase family; pfam00326"
                     /db_xref="CDD:459761"
     CDS             1..840
                     /gene="DPP8"
                     /gene_synonym="DP8; DPRP-1; DPRP1; MST097; MSTP097;
                     MSTP135; MSTP141"
                     /coded_by="NM_001438668.1:304..2826"
                     /note="isoform 6 is encoded by transcript variant 10"
                     /db_xref="GeneID:54878"
                     /db_xref="HGNC:HGNC:16490"
                     /db_xref="MIM:606819"
ORIGIN      
        1 mwkrseqmki ksgkcnmaaa meteqlgvei fetadceeni esqdrpklep fyveryswsq
       61 lkklladtrk yhgymmakap hdfmfvkrnd pdgphsdriy ylamsgenre ntlfyseipk
      121 tinraavlml swkplldlfq qqplrpnlve tscpnirmdp klcpadpdwi afihsndiwi
      181 snivtreerr ltyvhnelan meedarsagv atfvlqeefd rysgywwcpk aettpsggki
      241 lrilyeende seveiihvts pmletrrads frypktgtan pkvtfkmsei midaegriid
      301 vidkeliqpf eilfegveyi aragwtpegk yawsilldrs qtrlqivlis pelfipvedd
      361 vmerqrlies vpdsvtplii yeettdiwin ihdifhvfpq sheeeiefif asecktgfrh
      421 lykitsilke skykrssggl papsdfkcpi keeiaitsge wevlgrhgsn iqvdevrrlv
      481 yfegtkdspl ehhlyvvsyv npgevtrltd rgyshsccis qhcdffisky snqknphcvs
      541 lyklsspedd ptcktkefwa tildsagplp dytppeifsf esttgftlyg mlykphdlqp
      601 gkkyptvlfi yggpqvqlvn nrfkgvkyfr lntlaslgyv vvvidnrgsc hrglkfegaf
      661 kykmgqieid dqveglqyla srydfidldr vgihgwsygg ylslmalmqr sdifrvaiag
      721 apvtlwifyd tgyterymgh pdqneqgyyl gsvamqaekf psepnrllll hgfldenvhf
      781 ahtsillsfl vragkpydlq iypqerhsir vpesgehyel hllhylqenl gsriaalkvi
//
LOCUS       NP_001425344            1466 aa            linear   PRI 21-NOV-2025
DEFINITION  GTPase-activating protein and VPS9 domain-containing protein 1
            isoform 9 [Homo sapiens].
ACCESSION   NP_001425344 XP_047279140 XP_054218644
VERSION     NP_001425344.1
DBSOURCE    REFSEQ: accession NM_001438415.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1466)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1466)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1466)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1466)
  AUTHORS   Khademi,B., Khorrami,M., Ayromlou,H., Rikhtegar,R., Moghadam,E.A.,
            Tahmasebivand,M., Mousavi,S.R., Kheirollahi,M., Fakhr,F.,
            Alizadeh-Ghodsi,M. and Emamalizadeh,B.
  TITLE     An interdependence between GAPVD1 gene polymorphism, expression
            level and response to interferon beta in patients with multiple
            sclerosis
  JOURNAL   J Neuroimmunol 353, 577507 (2021)
   PUBMED   33548618
  REMARK    GeneRIF: An interdependence between GAPVD1 gene polymorphism,
            expression level and response to interferon beta in patients with
            multiple sclerosis.
REFERENCE   5  (residues 1 to 1466)
  AUTHORS   Ibrahim,H., Reus,P., Mundorf,A.K., Grothoff,A.L., Rudenko,V.,
            Buschhaus,C., Stefanski,A., Berleth,N., Stork,B., Stuhler,K.,
            Kalfalah,F. and Reinke,H.
  TITLE     Phosphorylation of GAPVD1 Is Regulated by the PER Complex and
            Linked to GAPVD1 Degradation
  JOURNAL   Int J Mol Sci 22 (7), 3787 (2021)
   PUBMED   33917494
  REMARK    GeneRIF: Phosphorylation of GAPVD1 Is Regulated by the PER Complex
            and Linked to GAPVD1 Degradation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1466)
  AUTHORS   Kim,H., Oh,H., Oh,Y.S., Bae,J., Hong,N.H., Park,S.J., Ahn,S.,
            Lee,M., Rhee,S., Lee,S.H., Jun,Y., Kim,S.H., Huh,Y.H. and Song,W.K.
  TITLE     SPIN90, an adaptor protein, alters the proximity between Rab5 and
            Gapex5 and facilitates Rab5 activation during EGF endocytosis
  JOURNAL   Exp Mol Med 51 (7), 1-14 (2019)
   PUBMED   31358736
  REMARK    GeneRIF: The findings suggest that SPIN90, as an adaptor protein,
            simultaneously binds inactive Rab5 and Gapex5, thereby altering
            their spatial proximity and facilitating Rab5 activation.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1466)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1466)
  AUTHORS   Su,X., Kong,C. and Stahl,P.D.
  TITLE     GAPex-5 mediates ubiquitination, trafficking, and degradation of
            epidermal growth factor receptor
  JOURNAL   J Biol Chem 282 (29), 21278-21284 (2007)
   PUBMED   17545148
  REMARK    GeneRIF: EGF-stimulated receptor ubiquitination and trafficking are
            mediated via GAPex-5: GAPex-5-mediated EGFR ubiquitination is
            independent of Rab5 activation
REFERENCE   9  (residues 1 to 1466)
  AUTHORS   Hunker,C.M., Galvis,A., Kruk,I., Giambini,H., Veisaga,M.L. and
            Barbieri,M.A.
  TITLE     Rab5-activating protein 6, a novel endosomal protein with a role in
            endocytosis
  JOURNAL   Biochem Biophys Res Commun 340 (3), 967-975 (2006)
   PUBMED   16410077
REFERENCE   10 (residues 1 to 1466)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL354710.17 and AL627223.23.
            
            On or before Apr 18, 2025 this sequence version replaced
            XP_047279140.1, XP_054218644.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2149947.1,
                                           SRR18074967.2771735.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1466
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..1466
                     /product="GTPase-activating protein and VPS9
                     domain-containing protein 1 isoform 9"
                     /note="GTPase-activating protein and VPS9
                     domain-containing protein 1; Rab5-activating protein 6;
                     Rab5 exchange factor"
                     /calculated_mol_wt=163746
     Region          84..449
                     /region_name="RasGAP_RAP6"
                     /note="Ras-GTPase Activating Domain of Rab5-activating
                     protein 6; cd05129"
                     /db_xref="CDD:213331"
     Site            order(129,168,170,172..173,179,182,186,304,312..313,
                     316..317,320,342,345..346,349,353,355,359..360)
                     /site_type="other"
                     /note="putative Rab5 interface [polypeptide binding]"
                     /db_xref="CDD:213331"
     Region          1251..1314
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          1362..1463
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..1466
                     /gene="GAPVD1"
                     /gene_synonym="GAPex-5; GAPEX5; RAP6"
                     /coded_by="NM_001438415.1:167..4567"
                     /note="isoform 9 is encoded by transcript variant 19"
                     /db_xref="GeneID:26130"
                     /db_xref="HGNC:HGNC:23375"
                     /db_xref="MIM:611714"
ORIGIN      
        1 mvkldihtla hhlkqerlyv nsekqliqrl nadvlktaek lyrtawiakq qrinldrlii
       61 tsaeaspaec cqhakiledt qfvdgykqlg fqetaygefl srlrenprli asslvagekl
      121 nqentqsviy tvftslygnc imqedesyll qvlryliefe lkesdnprrl lrrgtcafsi
      181 lfklfseglf saklfltatl hepimqllve dedhletdpn klierfspsq qeklfgekgs
      241 drfrqkvqem vesneaklva lvnkfigylk qntycfphsl rwivsqmykt lscvdrlevg
      301 evramctdll lacficpavv npeqygiisd apinevarfn lmqvgrllqq lamtgseegd
      361 prtksslgkf dkscvaafld vviggravet pplssvnlle glsrtvvyit ysqlitlvnf
      421 mksvmsgdql redrmaldnl lanlppakpg kssslemtpy ntpqlspatt pankknrlpi
      481 atrsrsrtnm lmdlhmdheg ssqetiqevq peevlvislg tgpqltpgmm senevlnmql
      541 sdggqgdvpv denklhgpsn rsnsvssldl egesvselga gpsgsngvea lqlleheqat
      601 tqdnlddklr kfeirdmmgl tddrdisetv setwstdvlg sdfdpnided rlqeiagaaa
      661 enmlgsllcl pgsgsvlldp ctgstisett seawsvevlp sdseapdlkq eerlqelesc
      721 sglgstsddt dvrevssrps tpglsvvsgi satsedipnk iedlrsecss dfggkdsvts
      781 pdmdeithdf lyilqpkqhf qhieaeadmr iqlsssahql tsppsqsesl lamfdplssh
      841 egasavvrpk vhyarpshpp pdppilegav ggnearlpnf gshvltpaem eafkqrhsyp
      901 erlvrsrssd ivssvrrpms dpswnrrpgn eerelppaaa igatslvaap hssssspskd
      961 ssrgeteerk dsddeksdrn rpwwrkrfvs ampkapipfr kkekqekdkd dlgpdrfstl
     1021 tddpsprlsa qaqvaedild kyrnaikrts psdgamanye stevmgdges ahdsprdeal
     1081 qnisaddlpd sasqaahpqd safsyrdakk klrlalcsad svafpvlths trnglpdhtd
     1141 pedneivcfl kvqiaeainl qdknlmaqlq etmrcvcrfd nrtcrkllas iaedyrkrap
     1201 yiayltrcrq glqttqahle rllqrvlrdk evanryfttv cvrllleske kkirefiqdf
     1261 qkltaaddkt aqvedflqfl ygamaqdviw qnaseeqlqd aqlaiersvm nrifklafyp
     1321 nqdgdilrdq vlhehiqrls kvvtanhral qipevylrea pwpsaqseir tisayktprd
     1381 kvqcilrmcs timnllslan edsvpgaddf vpvlvfvlik anppcllstv qyissfyasc
     1441 lsgeesywwm qftaavefik tiddrk
//
LOCUS       NP_001394269             275 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 38 [Homo sapiens].
ACCESSION   NP_001394269 XP_005254703
VERSION     NP_001394269.1
DBSOURCE    REFSEQ: accession NM_001407340.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            On May 31, 2022 this sequence version replaced XP_005254703.1.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.818031.1,
                                           SRR14038197.79511.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..275
                     /product="tropomyosin alpha-1 chain isoform 38"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=31622
     Region          12..226
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..275
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407340.1:88..915"
                     /note="isoform 38 is encoded by transcript variant 38"
                     /db_xref="CCDS:CCDS92011.1"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 magsssleav rrkirslqeq adaaeeragt lqreldherk lretaeadva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkviesraqk deekmeiqei qlkeakhiae
      121 dadrkyeeva rklviiesdl eraeeraels egqvrqleeq lrimdqtlka lmaaedkysq
      181 kedryeeeik vlsdklkeae traefaersv tkleksiddl egkilssvfs lilmveyqpg
      241 ktifqfkgih idtllctctf flcvlwgfsl wllns
//
LOCUS       NP_001427984            4366 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HUWE1 isoform 4 [Homo sapiens].
ACCESSION   NP_001427984 XP_047297694 XP_054182290
VERSION     NP_001427984.1
DBSOURCE    REFSEQ: accession NM_001441055.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4366)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 4366)
  AUTHORS   Lee,C., Park,S.H. and Yoon,S.K.
  TITLE     The E3 ligase HUWE1 increases the sensitivity of CRC to oxaliplatin
            through TOMM20 degradation
  JOURNAL   Oncogene 43 (9), 636-649 (2024)
   PUBMED   38184713
  REMARK    GeneRIF: The E3 ligase HUWE1 increases the sensitivity of CRC to
            oxaliplatin through TOMM20 degradation.
REFERENCE   3  (residues 1 to 4366)
  AUTHORS   Li,X.X., Xu,J.K., Su,W.J., Wu,H.L., Zhao,K., Zhang,C.M., Chen,X.K.
            and Yang,L.X.
  TITLE     The role of KDM4A-mediated histone methylation on temozolomide
            resistance in glioma cells through the HUWE1/ROCK2 axis
  JOURNAL   Kaohsiung J Med Sci 40 (2), 161-174 (2024)
   PUBMED   37873881
  REMARK    GeneRIF: The role of KDM4A-mediated histone methylation on
            temozolomide resistance in glioma cells through the HUWE1/ROCK2
            axis.
REFERENCE   4  (residues 1 to 4366)
  AUTHORS   Bernassola,F., Karin,M., Ciechanover,A. and Melino,G.
  TITLE     The HECT family of E3 ubiquitin ligases: multiple players in cancer
            development
  JOURNAL   Cancer Cell 14 (1), 10-21 (2008)
   PUBMED   18598940
  REMARK    Review article
REFERENCE   5  (residues 1 to 4366)
  AUTHORS   Zhong,Q., Gao,W., Du,F. and Wang,X.
  TITLE     Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the
            polyubiquitination of Mcl-1 and regulates apoptosis
  JOURNAL   Cell 121 (7), 1085-1095 (2005)
   PUBMED   15989957
  REMARK    GeneRIF: Mule is both required and sufficient for the
            polyubiquitination of Mcl-1; Mule is a unique BH3-containing E3
            ubiquitin ligase apical to Bcl-2 family proteins during DNA
            damage-induced apoptosis
            GeneRIF: Mule (HUWE1) poly-ubiquitinates anti-apoptotic gene Mcl-1.
REFERENCE   6  (residues 1 to 4366)
  AUTHORS   Chen,D., Kon,N., Li,M., Zhang,W., Qin,J. and Gu,W.
  TITLE     ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
  JOURNAL   Cell 121 (7), 1071-1083 (2005)
   PUBMED   15989956
  REMARK    GeneRIF: study modifies the current view of ARF-mediated p53
            activation and reveals that ARF-BP1 is a critical mediator of both
            the p53-independent and p53-dependent tumor suppressor functions of
            ARF
            GeneRIF: Ubiquitin ligase activity of ARF-BP1 (HUWE1) is inhibited
            by Arf.
REFERENCE   7  (residues 1 to 4366)
  AUTHORS   Liu,Z., Oughtred,R. and Wing,S.S.
  TITLE     Characterization of E3Histone, a novel testis ubiquitin protein
            ligase which ubiquitinates histones
  JOURNAL   Mol Cell Biol 25 (7), 2819-2831 (2005)
   PUBMED   15767685
REFERENCE   8  (residues 1 to 4366)
  AUTHORS   Gu,J., Dubner,R., Fornace,A.J. Jr. and Iadarola,M.J.
  TITLE     UREB1, a tyrosine phosphorylated nuclear protein, inhibits p53
            transactivation
  JOURNAL   Oncogene 11 (10), 2175-2178 (1995)
   PUBMED   7478539
REFERENCE   9  (residues 1 to 4366)
  AUTHORS   Turner,G., Gedeon,A. and Mulley,J.
  TITLE     X-linked mental retardation with heterozygous expression and
            macrocephaly: pericentromeric gene localization
  JOURNAL   Am J Med Genet 51 (4), 575-580 (1994)
   PUBMED   7943042
REFERENCE   10 (residues 1 to 4366)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX323845.7 and AC231658.3.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297694.1, XP_054182290.1.
            
            Summary: This gene encodes a protein containing a C-terminal HECT
            (E6AP type E3 ubiquitin protein ligase) domain that functions as an
            E3 ubiquitin ligase. The encoded protein is required for the
            ubiquitination and subsequent degradation of the anti-apoptotic
            protein Mcl1 (myeloid cell leukemia sequence 1 (BCL2-related)).
            This protein also ubiquitinates the p53 tumor suppressor, core
            histones, and DNA polymerase beta. Mutations in this gene are
            associated with Turner type X-linked syndromic cognitive
            disability. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1544394.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..4366
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..4366
                     /product="E3 ubiquitin-protein ligase HUWE1 isoform 4"
                     /EC_number="2.3.2.26"
                     /note="Mcl-1 ubiquitin ligase E3; BJ-HCC-24 tumor antigen;
                     HECT domain protein LASU1; ARF-binding protein 1;
                     URE-binding protein 1; large structure of UREB1; upstream
                     regulatory element-binding protein 1; homologous to E6AP
                     carboxyl terminus homologous protein 9; HECT-type E3
                     ubiquitin transferase HUWE1; HECT, UBA and WWE domain
                     containing 1, E3 ubiquitin protein ligase"
                     /calculated_mol_wt=480773
     Region          92..374
                     /region_name="DUF908"
                     /note="Domain of Unknown Function (DUF908); pfam06012"
                     /db_xref="CDD:428721"
     Region          438..821
                     /region_name="DUF913"
                     /note="Domain of Unknown Function (DUF913); pfam06025"
                     /db_xref="CDD:461803"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            656
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          713..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            747
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          985..1008
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1021..1044
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1091
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1298..1327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1324..1363
                     /region_name="UBA_HUWE1"
                     /note="UBA domain found in eukaryotic E3 ubiquitin-protein
                     ligase HUWE1 and similar proteins; cd14288"
                     /db_xref="CDD:270474"
     Site            1375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1403..1422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1624..1685
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          1696..1742
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1729
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1914
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2025..2072
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2042
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2269..2349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2274
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2363..2487
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2534
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2561
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2591
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2602
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2701..2977
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          <2742..3073
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            2758
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2833
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2840
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2842
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2868
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2894
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2895
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2896
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2925
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3017..3050
                     /region_name="UBM"
                     /note="Ubiquitin binding region; pfam14377"
                     /db_xref="CDD:464159"
     Region          3043..3066
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3156
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3252..3274
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3411..3431
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3478..3519
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3544..3575
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3562
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3669
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3744..3765
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3764
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3800
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3808
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3819
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3822
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3886..3923
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3898
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3911
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3916
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3919
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          4011..4364
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(4015,4045,4056,4117,4291,4327..4328,4331..4335,4355,
                     4363)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(4145,4148..4149,4151..4152,4155,4162,4164,
                     4168..4169,4171,4176,4181,4198,4202)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     Site            4263
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P51593; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     CDS             1..4366
                     /gene="HUWE1"
                     /gene_synonym="ARF-BP1; HECTH9; HSPC272; Ib772; LASU1;
                     MRXST; MULE; URE-B1; UREB1"
                     /coded_by="NM_001441055.1:426..13526"
                     /note="isoform 4 is encoded by transcript variant 9"
                     /db_xref="GeneID:10075"
                     /db_xref="HGNC:HGNC:30892"
                     /db_xref="MIM:300697"
ORIGIN      
        1 mkvdrtklkk tpteapadcr alidklkvcn deqlllelqq iktwnigkce lyhwvdlldr
       61 fdgiladagq tvenmswmlv cdrpereqlk mlllavlnft allieysfsr hlyssiehlt
      121 tllassdmqv vlavlnllyv fskrsnyitr lgsdkrtpll trlqhlaesw ggkengfgla
      181 eccrdlhmmk yppsattlhf efyadpgaev kiekrttsnt lhyihieqld kisespseim
      241 esltkmysip kdkqmllfth irlahgfsnh rkrlqavqar lhaisilvfv spfavysnal
      301 qesansilyn glieelvdvl qitdkqlmei kaaslrtlts ivhlertpkl ssiidctgta
      361 syhgflpvlv rnciqamidp smdpyphqfa talfsflyhl asydaggeal vscgmmeall
      421 kvikflgdeq dqitfvtrav rvvdlitnld maafqshsgl sifiyrlehe vdlcrkecpf
      481 vikpkiqrpn ttqegeemet dmdgvqcipq raallksmln flkkaiqdpa fsdgirhvmd
      541 gslptslkhi isnaeyygps lfllatevvt vfvfqepsll sslqdngltd vmlhallikd
      601 vpatrevlgs lpnvfsalcl narglqsfvq cqpferlfkv llspdylpam rrrrssdplg
      661 dtasnlgsav delmrhqptl ktdattaiik lleeicnlgr dpkyicqkps iqkadgtata
      721 ppprsnhaae eassedeeee evqamqsfns tqqnetepnq qvvgteerip iplmdyilnv
      781 mkfvesilsn nttddhcqef vnqkgllplv tilglpnlpi dfptsaacqa vagvcksilt
      841 lshepkvlqe gllqldsils sleplhrpie spggsvllre lacagnvada tlsaqatpll
      901 haltaahayi mmfvhtcrvg qseirsisvn qwgsqlglsv lsklsqlycs lvwestvlls
      961 lctpnslpsg cefgqadmqk lvpkdekagt tqggkrsdge qdgaagsmda stqgllegig
     1021 ldgdtlapme tdeptasdsk gkskitpama arikqikpll sassrlgral aelfgllvkl
     1081 cvgspvrqrr shhaasttta ptpaarstas altklltkgl swqpppytpt prfrltffic
     1141 svgftspmlf derkypyhlm lqkflcsggh nalfetfnwa lsmggkvpvs eglehsdlpd
     1201 gtgefldawl mlvekmvnpt tvlesphslp aklpggvqnf pqfsalrflv vtqkaaftci
     1261 knlwnrkplk vyggrmaesm lailchilrg epvirerlsk ekegsrgeed tgqeeggsrr
     1321 epqvnqqqlq qlmdmgftre hameallnts tmeqateyll thpppimggv vrdlsmseed
     1381 qmmraiamsl gqdipmdqra espeevacrk eeeerkarek qeeeeakcle kfqdadpleq
     1441 delhtftdtm lpgcfhllde lpdtvyrvcd limtaikrng adyrdmilkq vvnqvweaad
     1501 vlikaalplt tsdtktvsew isqmatlpqa snlatrilll tllfeelklp cawvvessgi
     1561 lnvlikllev vqpclqaake qkevqtpkwi tpvlllidfy ektaisskrr aqmtkylqsn
     1621 snnwrwfddr sgrwcsysas nnstidsawk sgetsvrfta grrrytvqft tmvqvneetg
     1681 nrrpvmltll rvprlnknsk nsngqelekt leeskemdik rkenkgndtp lalestntek
     1741 etsleetkig eiliqglted mvtvliracv smlgvpvdpd tlhatlrlcl rltrdhkyam
     1801 mfaelkstrm ilnltqssgf ngftplvtll lrhiiedpct lrhtmekvvr saatsgagst
     1861 tsgvvsgslg sreinyilrv lgpaacrnpd iftevancci rialpaprgs gtasddefen
     1921 lrikgpnavq lvkttplkps plpvipdtik eviydmlnal aayhapeead ksdpkpgvmt
     1981 qevgqllqdm gddvyqqyrs ltrqssdfdt qsgfsinsqv faadgastet sasgtsqgea
     2041 stpeesrdgk kdkegdrase egkqkgkgsk plmptstilr llaelvrsyv giatlianys
     2101 ytvgqselik edcsvlafvl dhllphtqna edkdtpalar lflaslaaag sgtdaqvalv
     2161 nevkaalgra lamaestekh arlqavmcii stimescpst ssfyssatak tqhngmnnii
     2221 rlflkkglvn dlarvphsld lsspnmantv naalkpletl srivnqpssl fgsksasskn
     2281 kseqdaqgas qdsssnqqdp gepgeaevqe edhdvtqtev adgdimdgea etdsvviagq
     2341 pevlssqemq veneledlid ellerdggsg nstiivsrsg edesqedvlm deapsnlsqa
     2401 stlqanreds mnildpedee ehtqeedssg snededdsqd eeeeeeedee ddqeddegee
     2461 gdedddddgs emeldedypd mnasplvrfe rfdreddlii efdnmfssat dippspgnip
     2521 tthplmvrha dhssltlgsg ssttrltqgi grsqrtlrql tantghtihv hypgnrqpnp
     2581 plilqrllgp saaadilqls sslplqsrgr arllvgnddv hiiarsddel lddffhdqst
     2641 atsqagtlss iptaltrwte eckvldaesm hdcvsvvkvs ivnhleflrd eeleerrekr
     2701 rkqlaeeetk itdkgkedke nrdqsaqcta sksndsteqn lsdgtpmpds ypttpsstda
     2761 atsesketlg tlqssqqqpt lptppalgev pqelqspage ggsstqllmp vepeelgptr
     2821 psgeaettqm elspaptits lsperaedsd altavssqle gspmdtssla sctleeavgd
     2881 tsaagsseqp ragsstpgda ppavaevqgr sdgsgesaqp pedssppass essstrdsav
     2941 aisgadsrgi leeplpstss eeedplagis lpegvdpsfl aalpddirre vlqnqlgirp
     3001 ptrtapstns sapavvgnpg vtevspefla alppaiqeev laqqraeqqr relaqnassd
     3061 tpmdpvtfiq tlpsdlrrsv ledmedsvla vmppdiaaea qalrreqear qrqlmherlf
     3121 ghsstsalsa ilrspaftsr lsgnrgvqyt rlavqrggtf qmggssshnr psgsnvdtll
     3181 rlrgrllldh ealscllvll fvdepklnts rlhrvlrnlc yhaqtrhwvi rsllsilqrs
     3241 seselcietp klttseekgk ksskscgsss henrpldllh kmeskssnql swlsvsmdaa
     3301 lgcrtnifqi qrsggrkhte khasggstvh ihpqaapvvc rhvldtliql akvfpshftq
     3361 qrtketnces drergnkacs pcssqssssg ictdfwdllv kldnmnvsrk gknsvksvpv
     3421 saggegetsp ysleasplgq lmnmlshpvi rrsslltekl lrllslisia lpenkvseaq
     3481 ansgsgasst ttatsttstt tttaasttpt pptaptpvts apalvaatai stivvaastt
     3541 vttpttattt vsispttkgs kspakvsdgg ssstdfkmvs sgltenqlql svevltshsc
     3601 seegledaan vllqlsrgds gtrdtvlkll lngarhlgyt lckqigtlla elreynleqq
     3661 rraqcetlsp dglpeeqpqt tklkgkmqsr fdmaenvviv asqkrplggr elqlpsmsml
     3721 tsktstqkff lrvlqviiql rddtrrankk akqtgrlgss glgsassiqa avrqleaead
     3781 aiiqmsessq seasvrrees pmdvdqpsps aqdtqsiasd gtpqgekeke erppelplls
     3841 eqlsldelwd mlgeclkele eshdqhavlv lqpaveaffl vhatereskp pvrdtresql
     3901 ahikdepppl spapltpatp ssldpffsre pssmhisssl ppdtqkflrf aethrtvlnq
     3961 ilrqstthla dgpfavlvdy irvldfdvkr kyfrqelerl deglrkedma vhvrrdhvfe
     4021 dsyrelhrks peemknrlyi vfegeegqda ggllrewymi isremfnpmy alfrtspgdr
     4081 vtytinpssh cnpnhlsyfk fvgrivakav ydnrllecyf trsfykhilg ksvrytdmes
     4141 edyhfyqglv yllendvstl gydltfstev qefgvcevrd lkpnganilv teenkkeyvh
     4201 lvcqmrmtga irkqlaafle gfyeiipkrl isifteqele llisglptid iddlksntey
     4261 hkyqsnsiqi qwfwralrsf dqadrakflq fvtgtskvpl qgfaalegmn giqkfqihrd
     4321 drstdrlpsa htcfnqldlp ayesfeklrh mlllaiqecs egfgla
//
LOCUS       NP_001424931             909 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 3 isoform 5 [Homo sapiens].
ACCESSION   NP_001424931 XP_016862727 XP_054203929
VERSION     NP_001424931.1
DBSOURCE    REFSEQ: accession NM_001438002.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 909)
  AUTHORS   Wang,H., Lan,S., Wang,L., Zhao,J., Jia,X., Xu,J., Sun,G., Liu,L.,
            Gong,S., Wang,N., Shan,B., Zhang,F. and Zhang,Z.
  TITLE     Expression of circ-PHC3 enhances ovarian cancer progression via
            regulation of the miR-497-5p/SOX9 pathway
  JOURNAL   J Ovarian Res 16 (1), 142 (2023)
   PUBMED   37468993
  REMARK    GeneRIF: Expression of circ-PHC3 enhances ovarian cancer
            progression via regulation of the miR-497-5p/SOX9 pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 909)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 909)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 909)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 909)
  AUTHORS   Crea,F., Di Paolo,A., Liu,H.H., Polillo,M., Clermont,P.L.,
            Guerrini,F., Ciabatti,E., Ricci,F., Barate,C., Fontanelli,G.,
            Barsotti,S., Morganti,R., Danesi,R., Wang,Y., Petrini,M.,
            Galimberti,S. and Helgason,C.D.
  TITLE     Polycomb genes are associated with response to imatinib in chronic
            myeloid leukemia
  JOURNAL   Epigenomics 7 (5), 757-765 (2015)
   PUBMED   26343356
  REMARK    GeneRIF: Data show that polycomb-group proteins BMI1, PHC3, CBX6
            and CBX7 expression was significantly increased during imatinib
            treatment.
REFERENCE   6  (residues 1 to 909)
  AUTHORS   Deshpande,A.M., Akunowicz,J.D., Reveles,X.T., Patel,B.B.,
            Saria,E.A., Gorlick,R.G., Naylor,S.L., Leach,R.J. and Hansen,M.F.
  TITLE     PHC3, a component of the hPRC-H complex, associates with E2F6
            during G0 and is lost in osteosarcoma tumors
  JOURNAL   Oncogene 26 (12), 1714-1722 (2007)
   PUBMED   17001316
  REMARK    GeneRIF: loss of PHC3 may favor tumorigenesis by potentially
            disrupting the ability of cells to remain in G(0)
REFERENCE   7  (residues 1 to 909)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   8  (residues 1 to 909)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 909)
  AUTHORS   Tonkin,E., Hagan,D.M., Li,W. and Strachan,T.
  TITLE     Identification and characterisation of novel mammalian homologues
            of Drosophila polyhomeoticpermits new insights into relationships
            between members of the polyhomeotic family
  JOURNAL   Hum Genet 111 (4-5), 435-442 (2002)
   PUBMED   12384788
REFERENCE   10 (residues 1 to 909)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC023891.28 and AC008040.7.
            
            On or before Apr 14, 2025 this sequence version replaced
            XP_016862727.1, XP_054203929.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.239957.1,
                                           SRR18074969.1987362.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..909
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.2"
     Protein         1..909
                     /product="polyhomeotic-like protein 3 isoform 5"
                     /note="early development regulator 3; polyhomeotic-like
                     protein 3; homolog of polyhomeotic 3; early development
                     regulatory protein 3; polyhomeotic like 3"
                     /calculated_mol_wt=98612
     Region          116..>444
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          <272..>432
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     Region          840..908
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(858..859,893..894,897..898,901)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(869..873,875..876,879..880,884,889)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..909
                     /gene="PHC3"
                     /gene_synonym="EDR3; HPH3"
                     /coded_by="NM_001438002.1:19..2748"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:80012"
                     /db_xref="HGNC:HGNC:15682"
                     /db_xref="MIM:620031"
ORIGIN      
        1 maeaefkdhs tamdtepnpg tssvstttss tttttittss srmqqpqisv ysgsdrhavq
       61 viqqalhrpp ssaaqylqqm yaaqqqhlml htaalqqqhl sssqlqslaa vqaslssgrp
      121 stsptgsvtq qssmsqtsvq nltlrsqklg vlsssqngpp kstsqtqslt ichnkttvts
      181 skisqrdpsp esnkkgesps lesrstavtr tssihqliap asyspiqphs likhqqiplh
      241 sppskvshhq lilqqqqqqi qpitlqnstq dpppsqhcip lqnhglppap snaqsqhcsp
      301 iqshpspltv spnqsqsaqq svvvspppph spsqsptiii hpqaliqphp lvssalqpgp
      361 nlqqstanqv qataqlnlps hlplpaspvv higpvqqsal vspgqqivsp shqqysslqs
      421 spipiasppq mstsppaqip plplqsmqsl qvqpeilsqg qvlvqnalvs eeelpaaeal
      481 vqlpfqtlpp pqtvavnlqv qppapvdppv vyqvedvcee empeesdecv rmdrtppppt
      541 lspaaitvgr gedltsehpl leqvelpava svsasviksp sdpshvsvpp pplllpaatt
      601 rsnstsmhss ipsienkppq aivkpqilth viegfviqeg lepfpvsrss llieqpvkkr
      661 plldnqvins vcvqpelqnn tkhadnssdt emedmiaeet leemdsellk cefcgkmgya
      721 neflrskrfc tmscakrynv scskkfalsr wnrkpdnqsl ghrgrrpsgp dgaarehilr
      781 qlpitypsae edlashedsv psamttrlrr qserererel rdvrirkmpe nsdllpvaqt
      841 epsiwtvddv wafihslpgc qdiadefraq eidgqallll kedhlmsamn iklgpalkic
      901 arinslkes
//
LOCUS       NP_001400601             291 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 4 [Homo sapiens].
ACCESSION   NP_001400601
VERSION     NP_001400601.1
DBSOURCE    REFSEQ: accession NM_001413672.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 291)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1660807.112944.1, SRR14038193.3879752.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..291
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 4"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=33182
     Region          4..286
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     CDS             1..291
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413672.1:247..1122"
                     /note="isoform 4 is encoded by transcript variant 8"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mewssrrsif rmngdkfrkf ikapprnysm ivmftalqpq rqcsvcrqan eeyqilansw
       61 ryssafcnkl ffsmvdydeg tdvfqqlnmn saptfmhfpp kgrpkradtf dlqrigfaae
      121 qlakwiadrt dvhirvfrpp nysgtialal lvslvgglly lrrnnlefiy nktgwamvsl
      181 civfamtsgq mwnhirgppy ahknphngqv syihgssqaq fvaeshiilv lnaaitmgmv
      241 llneaatskg dvgkrriicl vglglvvfff sfllsifrsk yhgypysfli k
//
LOCUS       NP_001424278            2547 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HECTD1 isoform 4 [Homo sapiens].
ACCESSION   NP_001424278 XP_047287159 XP_054231753
VERSION     NP_001424278.1
DBSOURCE    REFSEQ: accession NM_001437349.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2547)
  AUTHORS   Oxman,E., Li,H., Wang,H.Y. and Zohn,I.E.
  TITLE     Identification and functional analysis of rare HECTD1 missense
            variants in human neural tube defects
  JOURNAL   Hum Genet 143 (3), 263-277 (2024)
   PUBMED   38451291
  REMARK    GeneRIF: Identification and functional analysis of rare HECTD1
            missense variants in human neural tube defects.
REFERENCE   2  (residues 1 to 2547)
  AUTHORS   Zhang,J., Xin,Y., Ling,X., Liang,H., Zhang,L., Fang,C. and Ma,J.
  TITLE     Nucleoporin 93, a new substrate of the E3 ubiquitin protein ligase
            HECTD1, promotes esophageal squamous cell carcinoma progression
  JOURNAL   Hum Cell 37 (1), 245-257 (2024)
   PUBMED   37993750
  REMARK    GeneRIF: Nucleoporin 93, a new substrate of the E3 ubiquitin
            protein ligase HECTD1, promotes esophageal squamous cell carcinoma
            progression.
REFERENCE   3  (residues 1 to 2547)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 2547)
  AUTHORS   Vaughan,N., Scholz,N., Lindon,C. and Licchesi,J.D.F.
  TITLE     The E3 ubiquitin ligase HECTD1 contributes to cell proliferation
            through an effect on mitosis
  JOURNAL   Sci Rep 12 (1), 13160 (2022)
   PUBMED   35915203
  REMARK    GeneRIF: The E3 ubiquitin ligase HECTD1 contributes to cell
            proliferation through an effect on mitosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2547)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 2547)
  AUTHORS   Aleidi,S.M., Yang,A., Sharpe,L.J., Rao,G., Cochran,B.J., Rye,K.A.,
            Kockx,M., Brown,A.J. and Gelissen,I.C.
  TITLE     The E3 ubiquitin ligase, HECTD1, is involved in ABCA1-mediated
            cholesterol export from macrophages
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1863 (4), 359-368 (2018)
   PUBMED   29306077
  REMARK    GeneRIF: HECTD1 may be involved in the regulation of ABCA1-mediated
            cholesterol export from unloaded macrophages to apoA-I.
REFERENCE   7  (residues 1 to 2547)
  AUTHORS   Fang,S., Guo,H., Cheng,Y., Zhou,Z., Zhang,W., Han,B., Luo,W.,
            Wang,J., Xie,W. and Chao,J.
  TITLE     circHECTD1 promotes the silica-induced pulmonary
            endothelial-mesenchymal transition via HECTD1
  JOURNAL   Cell Death Dis 9 (3), 396 (2018)
   PUBMED   29540674
  REMARK    GeneRIF: SiO2 concomitantly increased circHECTD1 expression, which,
            in turn, inhibited HECTD1 protein expression.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 2547)
  AUTHORS   Shen,X., Jia,Z., D'Alonzo,D., Wang,X., Bruder,E., Emch,F.H., De
            Geyter,C. and Zhang,H.
  TITLE     HECTD1 controls the protein level of IQGAP1 to regulate the
            dynamics of adhesive structures
  JOURNAL   Cell Commun Signal 15 (1), 2 (2017)
   PUBMED   28073378
  REMARK    GeneRIF: Hectd1 regulates the protein level of IQGAP1 through
            ubiquitination.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 2547)
  AUTHORS   Helander,S., Montecchio,M., Lemak,A., Fares,C., Almlof,J., Yi,Y.,
            Yee,A., Arrowsmith,C., DhePaganon,S. and Sunnerhagen,M.
  TITLE     Basic Tilted Helix Bundle - a new protein fold in human
            FKBP25/FKBP3 and HectD1
  JOURNAL   Biochem Biophys Res Commun 447 (1), 26-31 (2014)
   PUBMED   24667607
  REMARK    GeneRIF: our high-resolution structures show a new fold composed of
            five small helices where H3 and H4 are tilted in a novel
            arrangement; we call this fold the Basic Tilted Helix Bundle (BTHB)
            domain.
REFERENCE   10 (residues 1 to 2547)
  AUTHORS   Tran,H., Bustos,D., Yeh,R., Rubinfeld,B., Lam,C., Shriver,S.,
            Zilberleyb,I., Lee,M.W., Phu,L., Sarkar,A.A., Zohn,I.E.,
            Wertz,I.E., Kirkpatrick,D.S. and Polakis,P.
  TITLE     HectD1 E3 ligase modifies adenomatous polyposis coli (APC) with
            polyubiquitin to promote the APC-axin interaction
  JOURNAL   J Biol Chem 288 (6), 3753-3767 (2013)
   PUBMED   23277359
  REMARK    GeneRIF: HectD1 promotes the APC-Axin interaction to negatively
            regulate Wnt signaling.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136418.4, AL121808.4 and KC877516.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_047287159.1, XP_054231753.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4378894.1,
                                           SRR14038191.211214.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2547
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..2547
                     /product="E3 ubiquitin-protein ligase HECTD1 isoform 4"
                     /EC_number="2.3.2.26"
                     /note="E3 ubiquitin-protein ligase HECTD1; E3 ligase for
                     inhibin receptor; HECT domain-containing protein 1; HECT
                     domain containing E3 ubiquitin protein ligase 1; HECT-type
                     E3 ubiquitin transferase HECTD1"
                     /calculated_mol_wt=281960
     Region          <366..>479
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          366..393
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          396..426
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(397,401..402,405..407,409..410,414,417,426,428,
                     432..433,436..438,440..441,445,448,457,459,461,465..466,
                     469..471,473..474,478)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          428..457
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1107..1240
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     Region          1277..1335
                     /region_name="MIB_HERC2"
                     /note="Mib_herc2; pfam06701"
                     /db_xref="CDD:461991"
     Region          2068..2545
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(2074,2103,2113,2200,2478,2510..2511,2514..2518,2538,
                     2544)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(2293,2296..2297,2299..2300,2303,2345,2347,
                     2351..2352,2354,2360,2365,2382,2386)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..2547
                     /gene="HECTD1"
                     /gene_synonym="EULIR"
                     /coded_by="NM_001437349.1:800..8443"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:25831"
                     /db_xref="HGNC:HGNC:20157"
                     /db_xref="MIM:618649"
ORIGIN      
        1 madvdpdtll ewlqmgqgde rdmqlialeq lcmlllmsdn vdrcfetcpp rtflpalcki
       61 fldesapdnv levtaraity yldvsaectr rivgvdgaik alcnrlvvve lnnrtsrdla
      121 eqcvkvleli ctresgavfe agglncvltf irdsghlvhk dtlhsamavv srlcgkmepq
      181 dssleicves lssllkhedh qvsdgalrcf asladrftrr gvdpaplakh glteellsrm
      241 aaaggtvsgp ssackpgrst tgapsttads klsnqvstiv sllstlcrgs pvvthdllrs
      301 elpdsiesal qgdercvldt mrlvdlllvl lfegrkalpk ssagstgrip glrrldssge
      361 rshrqlidci rskdtdalid aidtgafevn fmddvgqtll nwasafgtqe mveflcerga
      421 dvnrgqrsss lhyaacfgrp qvaktllrhg anpdlrdedg ktpldkarer ghsevvailq
      481 spgdwmcpvn kgddkkkkdt nkdeeecnep kgdpemapiy lkrllpvfaq tfqqtmlpsi
      541 rkaslalirk mihfcseall kevcdsdvgh nlptilveit atvldqeddd dghllalqii
      601 rdlvdkggdi fldqlarlgv iskvstlagp ssddeneees kpekedepqe dakelqqgkp
      661 yhwrdwsiir grdclyiwsd aaalelsngs ngwfrfildg klatmyssgs peggsdsses
      721 rsefleklqr argqvkpsts sqpilsapgp tkltvgnwsl tclkegeiai hnsdgqqati
      781 lkedlpgfvf esnrgtkhsf taetslgsef vtgwtgkrgr klksklektk qkvrtmardl
      841 yddhfkaves mprgvvvtlr niatqlessw elhtnrqcie sentwrdlmk talenlivll
      901 kdentispye mcssglvqal ltvlnnsmdl dmkqdcsqlv erinvfktaf seneddesrp
      961 avalirklia vlesierlpl hlydtpgsty nlqiltrrlr frlerapget alidrtgrml
     1021 kmeplatves leqyllkmva kqwydfdrss fvfvrklreg qnfifrhqhd fdengiiywi
     1081 gtnaktayew vnpaayglvv vtssegrnlp ygrledilsr dnsalnchsn ddknawfaid
     1141 lglwvipsay tlrhargygr salrnwvfqv skdgqnwtsl ythvddcsln epgstatwpl
     1201 dppkdekqgw rhvrikqmgk nasgqthyls lsgfelygtv ngvcedqlgk aakeaeanlr
     1261 rqrrlvrsqv lkymvpgarv irgldwkwrd qdgspqgegt vtgelhngwi dvtwdaggsn
     1321 syrmgaegkf dlklapgydp dtvaspkpvs stvsgttqsw sslvknncpd ktsaaagsss
     1381 rkgssssvcs vasssdislg stkterrsei vmehsivsga dvhepivvls saenvpqtev
     1441 gssssastst ltaetgsena erklgpdssv rtpgessais mgivsvsspd vssvseltnk
     1501 eaasqrplss sasnrlsvss llaagapmss sasvpnlssr etsslesfvr rvaniartna
     1561 tnnmnlsrss sdnntntlgr nvmstatspl mgaqsfpnlt tpgttstvtm stssvtsssn
     1621 vatattvlsv gqslsntltt sltstssesd tgqeaeysly dfldscrast llaelddded
     1681 lpepdeedde neddnqedqe yeeilrrpsl qrragsrsdv thhavtsqlp qvpagagsrp
     1741 igeqeeeeye tkggrrrtwd ddyvlkrqfs alvpafdprp grtnvqqttd leipppgtph
     1801 selleevect psprlaltlk vtglgttrev elpltnfrst ifyyvqkllq lscngnvksd
     1861 klrriwepty timyremkds dkekengkmd fcehgtksgl nqgaistlqs sdilnltkeq
     1921 pqakagngqn scgvedvlql lrilyivasd pysrisqedg deqpqftfpp deftskkitt
     1981 kilqqieepl alasgalpdw ceqltskcpf lipfetrqly ftctafgasr aivwlqnrre
     2041 atvertrtts svrrddpgef rvgrlkherv kvprgeslme waenvmqiha drksvlevef
     2101 lgeegtglgp tlefyalvaa efqrtdlgaw lcddnfpdde srhvdlgggl kppgyyvqrs
     2161 cglftapfpq dsdeleritk lfhflgifla kciqdnrlvd lpiskpffkl mcmgdiksnm
     2221 skliyesrgd rdlhctesqs easteeghds lsvgsfeeds ksefildppk pkppawfngi
     2281 ltwedfelvn phrarflkei kdlaikrrqi lsnkglsede kntklqelvl knpsgsgppl
     2341 siedlglnfq fcpssriygf tavdlkpsge demitmdnae eyvdlmfdfc mhtgiqkqme
     2401 afrdgfnkvf pmeklssfsh eevqmilcgn qspswaaedi inytepklgy trdspgflrf
     2461 vrvlcgmssd erkaflqftt gcstlppggl anlhprltvv rkvdatdasy psvntcvhyl
     2521 klpeysseei mrerllaatm ekgfhln
//
LOCUS       NP_001428016             820 aa            linear   PRI 21-NOV-2025
DEFINITION  fibroblast growth factor receptor 2 isoform 17 precursor [Homo
            sapiens].
ACCESSION   NP_001428016 XP_006717771 XP_054221139
VERSION     NP_001428016.1
DBSOURCE    REFSEQ: accession NM_001441087.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Chen,C.P., Huang,J.P., Huang,K.S., Chen,Y.Y., Wu,F.T., Pan,Y.T.,
            Chiu,C.L. and Wang,W.
  TITLE     Perinatal imaging findings of a fetus with Pfeiffer syndrome and a
            heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation in FGFR2
            presenting a cloverleaf skull, craniosynostosis and short limbs on
            prenatal ultrasound mimicking thanatophoric dysplasia type II
  JOURNAL   Taiwan J Obstet Gynecol 63 (3), 387-390 (2024)
   PUBMED   38802203
  REMARK    GeneRIF: Perinatal imaging findings of a fetus with Pfeiffer
            syndrome and a heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation
            in FGFR2 presenting a cloverleaf skull, craniosynostosis and short
            limbs on prenatal ultrasound mimicking thanatophoric dysplasia type
            II.
REFERENCE   2  (residues 1 to 820)
  AUTHORS   Lian,Y., Bodian,D. and Shehu,A.
  TITLE     Elucidating the Role of Wildtype and Variant FGFR2 Structural
            Dynamics in (Dys)Function and Disorder
  JOURNAL   Int J Mol Sci 25 (8), 4523 (2024)
   PUBMED   38674107
  REMARK    GeneRIF: Elucidating the Role of Wildtype and Variant FGFR2
            Structural Dynamics in (Dys)Function and Disorder.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 820)
  AUTHORS   Xu,N., Hung,K.L., Gong,X., Fan,D., Tian,Y., Yan,M., Wei,Y. and
            Wang,S.
  TITLE     Genetic insights into the 'sandwich fusion' subtype of Klippel-Feil
            syndrome: novel FGFR2 mutations identified by 21 cases of
            whole-exome sequencing
  JOURNAL   Orphanet J Rare Dis 19 (1), 141 (2024)
   PUBMED   38561822
  REMARK    GeneRIF: Genetic insights into the 'sandwich fusion' subtype of
            Klippel-Feil syndrome: novel FGFR2 mutations identified by 21 cases
            of whole-exome sequencing.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 820)
  AUTHORS   Wenger,T.L., Hing,A.V. and Evans,K.N.
  TITLE     Apert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31145570
REFERENCE   5  (residues 1 to 820)
  AUTHORS   Wenger,T., Miller,D. and Evans,K.
  TITLE     FGFR Craniosynostosis Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301628
REFERENCE   6  (residues 1 to 820)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   7  (residues 1 to 820)
  AUTHORS   Dell,K.R. and Williams,L.T.
  TITLE     A novel form of fibroblast growth factor receptor 2. Alternative
            splicing of the third immunoglobulin-like domain confers ligand
            binding specificity
  JOURNAL   J Biol Chem 267 (29), 21225-21229 (1992)
   PUBMED   1400433
REFERENCE   8  (residues 1 to 820)
  AUTHORS   Luqmani,Y.A., Graham,M. and Coombes,R.C.
  TITLE     Expression of basic fibroblast growth factor, FGFR1 and FGFR2 in
            normal and malignant human breast, and comparison with other normal
            tissues
  JOURNAL   Br J Cancer 66 (2), 273-280 (1992)
   PUBMED   1380281
REFERENCE   9  (residues 1 to 820)
  AUTHORS   Katoh,M., Hattori,Y., Sasaki,H., Tanaka,M., Sugano,K., Yazaki,Y.,
            Sugimura,T. and Terada,M.
  TITLE     K-sam gene encodes secreted as well as transmembrane receptor
            tyrosine kinase
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 2960-2964 (1992)
   PUBMED   1313574
REFERENCE   10 (residues 1 to 820)
  AUTHORS   Miki,T., Bottaro,D.P., Fleming,T.P., Smith,C.L., Burgess,W.H.,
            Chan,A.M. and Aaronson,S.A.
  TITLE     Determination of ligand-binding specificity by alternative
            splicing: two distinct growth factor receptors encoded by a single
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 246-250 (1992)
   PUBMED   1309608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009988.12.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_006717771.1, XP_054221139.1.
            
            Summary: The protein encoded by this gene is a member of the
            fibroblast growth factor receptor family, where amino acid sequence
            is highly conserved between members and throughout evolution. FGFR
            family members differ from one another in their ligand affinities
            and tissue distribution. A full-length representative protein
            consists of an extracellular region, composed of three
            immunoglobulin-like domains, a single hydrophobic membrane-spanning
            segment and a cytoplasmic tyrosine kinase domain. The extracellular
            portion of the protein interacts with fibroblast growth factors,
            setting in motion a cascade of downstream signals, ultimately
            influencing mitogenesis and differentiation. This particular family
            member is a high-affinity receptor for acidic, basic and/or
            keratinocyte growth factor, depending on the isoform. Mutations in
            this gene are associated with Crouzon syndrome, Pfeiffer syndrome,
            Craniosynostosis, Apert syndrome, Jackson-Weiss syndrome,
            Beare-Stevenson cutis gyrata syndrome, Saethre-Chotzen syndrome,
            and syndromic craniosynostosis. Multiple alternatively spliced
            transcript variants encoding different isoforms have been noted for
            this gene. [provided by RefSeq, Jan 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853562.4561.1,
                                           SRR7346977.1921846.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:1309608)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..820
                     /product="fibroblast growth factor receptor 2 isoform 17
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="protein tyrosine kinase, receptor like 14;
                     bacteria-expressed kinase; keratinocyte growth factor
                     receptor; BEK fibroblast growth factor receptor"
                     /calculated_mol_wt=89638
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2298
     Region          31..124
                     /region_name="IgI_1_FGFR"
                     /note="First immunoglobulin (Ig)-like domain of fibroblast
                     growth factor receptor (FGFR); member of the I-set of Ig
                     superfamily (IgSF) domains; cd04973"
                     /db_xref="CDD:409362"
     Region          31..34
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409362"
     Region          47..53
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409362"
     Region          56..66
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409362"
     Region          69..74
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409362"
     Region          77..79
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409362"
     Region          84..88
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409362"
     Region          91..96
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409362"
     Region          102..111
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409362"
     Region          114..124
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409362"
     Region          154..248
                     /region_name="IgI_2_FGFR"
                     /note="Second immunoglobulin (Ig)-like domain of
                     fibroblast growth factor (FGF) receptor; member of the
                     I-set of IgSF domains; cd05857"
                     /db_xref="CDD:409443"
     Region          154..157
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409443"
     Region          165..170
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409443"
     Site            order(166,168,170)
                     /site_type="other"
                     /note="FGF binding site [polypeptide binding]"
                     /db_xref="CDD:409443"
     Site            order(167,174..176,178)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409443"
     Region          174..182
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409443"
     Region          188..193
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409443"
     Region          196..198
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409443"
     Region          207..210
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409443"
     Region          214..219
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409443"
     Region          228..235
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409443"
     Region          238..248
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409443"
     Region          256..358
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          274..278
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409444"
     Region          287..291
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409444"
     Region          323..327
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409444"
     Region          337..342
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409444"
     Region          350..353
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409444"
     Region          455..767
                     /region_name="PTKc_FGFR2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Fibroblast Growth Factor Receptor 2; cd05101"
                     /db_xref="CDD:270679"
     Site            order(486..487,489,494,514,516,533,563..566,570,625,
                     629..630,632,643,661..665,674,708)
                     /site_type="active"
                     /db_xref="CDD:270679"
     Site            order(486..487,489,494,514,516,533,563..566,570,629..630,
                     632,643)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270679"
     Site            order(625,629,661..665,674,708)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270679"
     Site            642..667
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270679"
     CDS             1..820
                     /gene="FGFR2"
                     /gene_synonym="BBDS; BEK; BFR-1; CD332; CEK3; CFD1; ECT1;
                     JWS; K-SAM; KGFR; TK14; TK25"
                     /coded_by="NM_001441087.1:634..3096"
                     /note="isoform 17 precursor is encoded by transcript
                     variant 17"
                     /db_xref="GeneID:2263"
                     /db_xref="HGNC:HGNC:3689"
                     /db_xref="MIM:176943"
ORIGIN      
        1 mvswgrficl vvvtmatlsl arpsfslved ttlepeeppt kyqisqpevy vaapgeslev
       61 rcllkdaavi swtkdgvhlg pnnrtvlige ylqikgatpr dsglyactas rtvdsetwyf
      121 mvnvtdaiss gddeddtdga edfvsensnn krapywtnte kmekrlhavp aantvkfrcp
      181 aggnpmptmr wlkngkefkq ehriggykvr nqhwslimes vvpsdkgnyt cvveneygsi
      241 nhtyhldvve rsphrpilqa glpanastvv ggdvefvckv ysdaqphiqw ikhvekngsk
      301 ygpdglpylk vlkhsginss naevlalfnv teadageyic kvsnyigqan qsawltvlpk
      361 qqapgrekei taspdyleia iycigvflia cmvvtvilcr mknttkkpdf ssqpavhklt
      421 kriplrrqvs aessssmnsn tplvrittrl sstadtpmla gvseyelped pkwefprdkl
      481 tlgkplgegc fgqvvmaeav gidkdkpkea vtvavkmlkd datekdlsdl vsememmkmi
      541 gkhkniinll gactqdgply viveyaskgn lreylrarrp pgmeysydin rvpeeqmtfk
      601 dlvsctyqla rgmeylasqk cihrdlaarn vlvtennvmk iadfglardi nnidyykktt
      661 ngrlpvkwma pealfdrvyt hqsdvwsfgv lmweiftlgg spypgipvee lfkllkeghr
      721 mdkpanctne lymmmrdcwh avpsqrptfk qlvedldril tlttneeyld lsqpleqysp
      781 sypdtrsscs sgddsvfspd pmpyepclpq yphingsvkt
//
LOCUS       NP_001427333             898 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001427333 XP_016873110 XP_054224544
VERSION     NP_001427333.1
DBSOURCE    REFSEQ: accession NM_001440404.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 898)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 898)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 898)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 898)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 898)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 898)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 898)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3, AP004147.3 and
            AP001929.5.
            
            On or before May 20, 2025 this sequence version replaced
            XP_016873110.1, XP_054224544.1.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1099934.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..898
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     4 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=98772
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..402
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Region          415..727
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     CDS             1..898
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440404.1:299..2995"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk aaelgmvsay
      241 ytyiftnlef slqrmdslvd drvnilgfsi fnqshaffqe faqslnqswq encdhvpftg
      301 palssallfd avyavvtavq elnrsqeigv kplscgsaqi wqhgtslmny lrmveleglt
      361 ghiefnskgq rsnyalkilq ftrngfrqig qwhvaeglsm dshlyasnis dtlfnttlvv
      421 ttilenpylm lkgnhqemeg ndryegfcvd mlkelaeilr fnykirlvgd gvygvpeang
      481 twtgmvgeli arkadlavag ltitaerekv idfskpfmtl gisilyrvhm grkpgyfsfl
      541 dpfspgvwlf mllaylavsc vlflvarwaf tliiissyta nlaafltvqr mdvpiesvdd
      601 ladqtaieyg tihggssmtf fqnsryqtyq rmwnymyskq psvfvkstee giarvlnsny
      661 afllestmne yyrqrncnlt qigglldtkg ygigmpvgsv frdefdlail qlqennrlei
      721 lkrkwweggk cpkeedhrak glgmeniggi fvvlicgliv aifmamlefl wtlrhseate
      781 vsvcqemvte lrsiilcqds ihprrrraav ppprppipee rrprgtatls ngklcgagep
      841 dqlaqrlaqe aalvargcth irvcpecrrf qglrarpspa rseeslewek ttnssepe
//
LOCUS       NP_001415208             443 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B
            beta isoform isoform e [Homo sapiens].
ACCESSION   NP_001415208 NP_001120853
VERSION     NP_001415208.1
DBSOURCE    REFSEQ: accession NM_001428279.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Shen,D. and Kang,S.
  TITLE     Comprehensive analysis of mitochondria-related genes indicates that
            PPP2R2B is a novel biomarker and promotes the progression of
            bladder cancer via Wnt signaling pathway
  JOURNAL   Biol Direct 19 (1), 17 (2024)
   PUBMED   38409085
  REMARK    GeneRIF: Comprehensive analysis of mitochondria-related genes
            indicates that PPP2R2B is a novel biomarker and promotes the
            progression of bladder cancer via Wnt signaling pathway.
            Erratum:[Biol Direct. 2024 Apr 18;19(1):27. doi:
            10.1186/s13062-024-00474-1. PMID: 38637864]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Zhou,C., Liu,H.B., Jahanbakhsh,F., Deng,L., Wu,B., Ying,M.,
            Margolis,R.L. and Li,P.P.
  TITLE     Bidirectional Transcription at the PPP2R2B Gene Locus in
            Spinocerebellar Ataxia Type 12
  JOURNAL   Mov Disord 38 (12), 2230-2240 (2023)
   PUBMED   37735923
  REMARK    GeneRIF: Bidirectional Transcription at the PPP2R2B Gene Locus in
            Spinocerebellar Ataxia Type 12.
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Ruediger,R., Brewis,N., Ohst,K. and Walter,G.
  TITLE     Increasing the ratio of PP2A core enzyme to holoenzyme inhibits
            Tat-stimulated HIV-1 transcription and virus production
  JOURNAL   Virology 238 (2), 432-443 (1997)
   PUBMED   9400615
REFERENCE   6  (residues 1 to 443)
  AUTHORS   Tung,H.Y., De Rocquigny,H., Zhao,L.J., Cayla,X., Roques,B.P. and
            Ozon,R.
  TITLE     Direct activation of protein phosphatase-2A0 by HIV-1 encoded
            protein complex NCp7:vpr
  JOURNAL   FEBS Lett 401 (2-3), 197-201 (1997)
   PUBMED   9013886
REFERENCE   7  (residues 1 to 443)
  AUTHORS   Schalling,M., Hudson,T.J., Buetow,K.H. and Housman,D.E.
  TITLE     Direct detection of novel expanded trinucleotide repeats in the
            human genome
  JOURNAL   Nat Genet 4 (2), 135-139 (1993)
   PUBMED   8348150
REFERENCE   8  (residues 1 to 443)
  AUTHORS   Margolis,R.L., Holmes,S.E., Srivastava,A.K., Mukherji,M. and
            Sinha,K.K.
  TITLE     Spinocerebellar Ataxia Type 12 - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301381
REFERENCE   9  (residues 1 to 443)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
REFERENCE   10 (residues 1 to 443)
  AUTHORS   Mayer,R.E., Hendrix,P., Cron,P., Matthies,R., Stone,S.R., Goris,J.,
            Merlevede,W., Hofsteenge,J. and Hemmings,B.A.
  TITLE     Structure of the 55-kDa regulatory subunit of protein phosphatase
            2A: evidence for a neuronal-specific isoform
  JOURNAL   Biochemistry 30 (15), 3589-3597 (1991)
   PUBMED   1849734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011386.6, AC009186.7 and
            AC008728.7.
            
            Summary: The product of this gene belongs to the phosphatase 2
            regulatory subunit B family. Protein phosphatase 2 is one of the
            four major Ser/Thr phosphatases, and it is implicated in the
            negative control of cell growth and division. It consists of a
            common heteromeric core enzyme, which is composed of a catalytic
            subunit and a constant regulatory subunit, that associates with a
            variety of regulatory subunits. The B regulatory subunit might
            modulate substrate selectivity and catalytic activity. This gene
            encodes a beta isoform of the regulatory subunit B55 subfamily.
            Defects in this gene cause autosomal dominant spinocerebellar
            ataxia 12 (SCA12), a disease caused by degeneration of the
            cerebellum, sometimes involving the brainstem and spinal cord, and
            in resulting in poor coordination of speech and body movements.
            Multiple alternatively spliced variants, which encode different
            isoforms, have been identified for this gene. The 5' UTR of some of
            these variants includes a CAG trinucleotide repeat sequence (7-28
            copies) that can be expanded to 55-78 copies in cases of SCA12.
            [provided by RefSeq, Jul 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3102017.1,
                                           SRR14372079.2330119.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..443
                     /product="serine/threonine-protein phosphatase 2A 55 kDa
                     regulatory subunit B beta isoform isoform e"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase 2, regulatory subunit B, beta"
                     /calculated_mol_wt=51579
     Region          22..438
                     /region_name="CDC55"
                     /note="Serine/threonine protein phosphatase 2A, regulatory
                     subunit [Signal transduction mechanisms]; COG5170"
                     /db_xref="CDD:227498"
     Region          22..61
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00005.1)"
     Region          27..75
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          87..128
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00005.1)"
     Region          93..170
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          171..209
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00005.1)"
     Region          176..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          220..260
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00005.1)"
     Region          226..277
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P36877; propagated from
                     UniProtKB/Swiss-Prot (Q00005.1)"
     Region          279..317
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00005.1)"
     Region          284..320
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P36877; propagated from
                     UniProtKB/Swiss-Prot (Q00005.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P36877; propagated from
                     UniProtKB/Swiss-Prot (Q00005.1)"
     Region          334..375
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00005.1)"
     Region          341..376
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          410..442
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00005.1)"
     Region          415..438
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..443
                     /gene="PPP2R2B"
                     /gene_synonym="B55BETA; PP2AB55BETA; PP2ABBETA; PP2APR55B;
                     PP2APR55BETA; PR2AB55BETA; PR2ABBETA; PR2APR55BETA; PR52B;
                     PR55-BETA; PR55BETA; SCA12"
                     /coded_by="NM_001428279.1:182..1513"
                     /note="isoform e is encoded by transcript variant 12"
                     /db_xref="GeneID:5521"
                     /db_xref="HGNC:HGNC:9305"
                     /db_xref="MIM:604325"
ORIGIN      
        1 meedidtrki nnsflrdhsy ateadiistv efnhtgella tgdkggrvvi fqreqesknq
       61 vhrrgeynvy stfqshepef dylksleiee kinkirwlpq qnaayfllst ndktvklwkv
      121 serdkrpegy nlkdeegrlr dpatittlrv pvlrpmdlmv eatprrvfan ahtyhinsis
      181 vnsdyetyms addlrinlwn feitnqsfni vdikpanmee ltevitaaef hphhcntfvy
      241 ssskgtirlc dmrasalcdr htkffeeped psnrsffsei issisdvkfs hsgryimtrd
      301 yltvkvwdln menrpietyq vhdylrsklc slyendcifd kfecvwngsd svimtgsynn
      361 ffrmfdrntk rdvtleasre nskprailkp rkvcvggkrr kdeisvdsld fskkilhtaw
      421 hpseniiava atnnlyifqd kvn
//
LOCUS       NP_001400678             825 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform k [Homo sapiens].
ACCESSION   NP_001400678
VERSION     NP_001400678.1
DBSOURCE    REFSEQ: accession NM_001413749.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 825)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 825)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 825)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 825)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 825)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.757155.1,
                                           SRR14038192.2385297.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..825
                     /product="polyhomeotic-like protein 1 isoform k"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=87435
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          212..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          261..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          649..756
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          756..824
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(774..775,809..810,813..814,817)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(785..789,791..792,795..796,800,805)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..825
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413749.1:368..2845"
                     /note="isoform k is encoded by transcript variant 13"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq asinlattsa aqlisrsqsv
      121 sspsattltq svllgnttsp plnqsqaqmy lrpqlgnllq vnrtlgrnvp lasqlilmpn
      181 gavaavqqev psaqspgvha dadqvqnlav rnqqasaqgp qmqgstqkai ppgaspvssl
      241 sqassqalav aqassgatnq slnlsqaggg sgnsipgsmg pggggqahgg lgqlpssgmg
      301 ggscprkgtg vvqplpaaqt vtvsqgsqte aesaaakkae adgsgqqnvg mnltrtatpa
      361 psqtlissat ytqiqphsli qqqqqihlqq kqvviqqqia ihhqqqfqhr qsqllhtath
      421 lqlaqqqqqq qqqqqqqqqp qattltapqp pqgkpqtlav krkadseeer ddvstlgsml
      481 pakaspvaes pkvmdekssl gekaesvanv nantpsselv altpapsvpp ptlamvsrqm
      541 gdskppqaiv kpqilthiie gfviqegaep fpvgcsqllk esekplqtgl ptgltenqsg
      601 gplgvdspsa eldkkanllk ceycgkyapa eqfrgskrfc smtcakrynv scshqfrlkr
      661 kkmkefqean yarvrrrgpr rsssdiarak iqgkchrgqe dssrgsdnss ydealsptsp
      721 gplsvraghg erdlgnpnta pptpelhgin pvflssnpsr wsveevyefi aslqgcqeia
      781 eefrsqeidg qallllkeeh lmsamniklg palkicakin vlket
//
LOCUS       NP_001427523             410 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform j [Homo sapiens].
ACCESSION   NP_001427523
VERSION     NP_001427523.1
DBSOURCE    REFSEQ: accession NM_001440594.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 410)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2421273.1,
                                           SRR14038193.2500087.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..410
                     /product="polycomb protein EED isoform j"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=46558
     Region          <90..408
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          117..157
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          162..199
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          209..271
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          278..326
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          334..374
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          382..406
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..410
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001440594.1:478..1710"
                     /note="isoform j is encoded by transcript variant 10"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdendd avsiesgtnt erpdtptntp
       61 napgrkswgk gkwkskkcky sfkcvnslkv tlyechsqge irllqsyvda dadenfytca
      121 wtydsntshp llavagsrgi iriinpitmq cikhyvghgn ainelkfhpr dpnlllsvsk
      181 dhalrlwniq tdtlvaifgg veghrdevls adydllgeki mscgmdhslk lwrinskrmm
      241 naikesydyn pnktnrpfis qkihfpdfst rdihrnyvdc vrwlgdlils kscenaivcw
      301 kpgkmeddid kikpsesnvt ilgrfdysqc diwymrfsmd fwqkmlalgn qvgklyvwdl
      361 evedphkakc ttlthhkcga airqtsfsrd ssiliavcdd asiwrwdrlr
//
LOCUS       NP_001393995             590 aa            linear   PRI 21-NOV-2025
DEFINITION  merlin isoform 2 [Homo sapiens].
ACCESSION   NP_001393995
VERSION     NP_001393995.1
DBSOURCE    REFSEQ: accession NM_001407066.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 590)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 590)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 590)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 590)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 590)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 590)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 590)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 590)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005529.7 and AC004882.3.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1106070.1,
                                           SRR14038193.2190099.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333, SAMEA2147975
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..590
                     /product="merlin isoform 2"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=68959
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35240.1)"
     Region          23..222
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          216..312
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(258..259,261..267,276,297,300..301,304)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(258,261..268,276,297,300..301,304)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(294,298)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            297..312
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          307..>367
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          346..465
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          518..>579
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PAK.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (P35240.1)"
     CDS             1..590
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_001407066.1:367..2139"
                     /note="isoform 2 is encoded by transcript variant 15"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 magaiasrms fsslkrkqpk tftvrivtmd aemefncemk wkgkdlfdlv crtlglretw
       61 ffglqytikd tvawlkmdkk vldhdvskee pvtfhflakf ypenaeeelv qeitqhlffl
      121 qvkkqildek iycppeasvl lasyavqaky gdydpsvhkr gflaqeellp krvinlyqmt
      181 pemweerita wyaehrgrar deaemeylki aqdlemygvn yfairnkkgt elllgvdalg
      241 lhiydpenrl tpkisfpwne irnisysdke ftikpldkki dvfkfnsskl rvnklilqlc
      301 ignhdlfmrr rkadslevqq mkaqareeka rkqmerqrla rekqmreeae rtrdelerrl
      361 lqmkeeatma nealmrseet adllaekaqi teeeakllaq kaaeaeqemq rikatairte
      421 eekrlmeqkv leaevlalkm aeeserrake adqlkqdlqe areaerrakq klleiatkpt
      481 yppmnpipap lppdipsfnl igdslsfdfk dtdmkrlsme iekekveyme kskhlqeqln
      541 elkteiealk lkeretaldi lhnensdrgg sskhntikkp qaqgrrpici
//
LOCUS       NP_001415240             326 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb complex protein BMI-1 [Homo sapiens].
ACCESSION   NP_001415240
VERSION     NP_001415240.1
DBSOURCE    REFSEQ: accession NM_001428311.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Szustka,A. and Krzeslak,A.
  TITLE     BMI-1 in Breast Cancer - Biological Role and Clinical Implications
  JOURNAL   Cell Physiol Biochem 58 (5), 584-596 (2024)
   PUBMED   39429016
  REMARK    GeneRIF: BMI-1 in Breast Cancer - Biological Role and Clinical
            Implications.
            Review article
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Hsu,Y.C., Luo,C.W., Chang,S.J., Lai,C.Y., Yang,Y.T., Chen,Y.Z.,
            Liu,W.T., Wu,C.C., Sun,C.K., Hou,M.F. and Pan,M.R.
  TITLE     Targeting Bmi1 for Enhancing Anoikis Sensitivity and Inhibiting
            Metastasis in Colorectal Cancer
  JOURNAL   Cancer Genomics Proteomics 21 (5), 523-532 (2024)
   PUBMED   39191496
  REMARK    GeneRIF: Targeting Bmi1 for Enhancing Anoikis Sensitivity and
            Inhibiting Metastasis in Colorectal Cancer.
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Li,Q., Fu,T., Wei,N., Wang,Q. and Zhang,X.
  TITLE     Bmi-1 promotes the proliferation, migration and invasion, and
            inhibits cell apoptosis of human retinoblastoma cells via RKIP
  JOURNAL   Sci Rep 14 (1), 14544 (2024)
   PUBMED   38914697
  REMARK    GeneRIF: Bmi-1 promotes the proliferation, migration and invasion,
            and inhibits cell apoptosis of human retinoblastoma cells via RKIP.
            Erratum:[Sci Rep. 2025 Aug 5;15(1):28521. doi:
            10.1038/s41598-025-11879-x. PMID: 40764337]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Park,I.K., Qian,D., Kiel,M., Becker,M.W., Pihalja,M.,
            Weissman,I.L., Morrison,S.J. and Clarke,M.F.
  TITLE     Bmi-1 is required for maintenance of adult self-renewing
            haematopoietic stem cells
  JOURNAL   Nature 423 (6937), 302-305 (2003)
   PUBMED   12714971
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Satijn,D.P. and Otte,A.P.
  TITLE     RING1 interacts with multiple Polycomb-group proteins and displays
            tumorigenic activity
  JOURNAL   Mol Cell Biol 19 (1), 57-68 (1999)
   PUBMED   9858531
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Alkema,M.J., Jacobs,J., Voncken,J.W., Jenkins,N.A., Copeland,N.G.,
            Satijn,D.P., Otte,A.P., Berns,A. and van Lohuizen,M.
  TITLE     MPc2, a new murine homolog of the Drosophila polycomb protein is a
            member of the mouse polycomb transcriptional repressor complex
  JOURNAL   J Mol Biol 273 (5), 993-1003 (1997)
   PUBMED   9367786
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Alkema,M.J., Bronk,M., Verhoeven,E., Otte,A., van 't Veer,L.J.,
            Berns,A. and van Lohuizen,M.
  TITLE     Identification of Bmi1-interacting proteins as constituents of a
            multimeric mammalian polycomb complex
  JOURNAL   Genes Dev 11 (2), 226-240 (1997)
   PUBMED   9009205
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Alkema,M.J., Wiegant,J., Raap,A.K., Berns,A. and van Lohuizen,M.
  TITLE     Characterization and chromosomal localization of the human
            proto-oncogene BMI-1
  JOURNAL   Hum Mol Genet 2 (10), 1597-1603 (1993)
   PUBMED   8268912
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158211.29.
            
            Summary: This gene encodes a ring finger protein that is major
            component of the polycomb group complex 1 (PRC1). This complex
            functions through chromatin remodeling as an essential epigenetic
            repressor of multiple regulatory genes involved in embryonic
            development and self-renewal in somatic stem cells. This protein
            also plays a central role in DNA damage repair. This gene is an
            oncogene and aberrant expression is associated with numerous
            cancers and is associated with resistance to certain
            chemotherapies. A pseudogene of this gene is found on chromosome X.
            Read-through transcription also exists between this gene and the
            upstream COMM domain containing 3 (COMMD3) gene. [provided by
            RefSeq, Sep 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1685366.1,
                                           SRR11853567.3414.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.2"
     Protein         1..326
                     /product="polycomb complex protein BMI-1"
                     /note="murine leukemia viral (bmi-1) oncogene homolog; B
                     lymphoma Mo-MLV insertion region 1 homolog; ring finger
                     protein 51; polycomb group protein Bmi1; polycomb group
                     RING finger protein 4; BMI1 polycomb ring finger oncogene;
                     BMI1 polycomb ring finger proto-oncogene"
                     /calculated_mol_wt=36818
     Region          5..101
                     /region_name="RING-HC_PCGF4"
                     /note="RING finger found in polycomb group RING finger
                     protein 4 (PCGF4) and similar proteins; cd16736"
                     /db_xref="CDD:438394"
     Site            order(5..13,15,17,21,23..24,26..27,29..30,32..36,39..42,
                     44..45,66,69..72,74,78,81..82,84,86,89..90,93..94,97)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438394"
     Region          81..95
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     Region          130..226
                     /region_name="RAWUL_PCGF4"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in polycomb group RING finger protein
                     4 (PCGF4); cd17165"
                     /db_xref="CDD:340685"
     Region          162..182
                     /region_name="Interaction with PHC2.
                     /evidence=ECO:0000269|PubMed:27827373"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     Region          164..228
                     /region_name="Interaction with E4F1.
                     /evidence=ECO:0000269|PubMed:16882984"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     Region          236..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     CDS             1..326
                     /gene="BMI1"
                     /gene_synonym="flvi-2/bmi-1; FLVI2/BMI1; PCGF4; RNF51"
                     /coded_by="NM_001428311.1:181..1161"
                     /db_xref="GeneID:648"
                     /db_xref="HGNC:HGNC:1066"
                     /db_xref="MIM:164831"
ORIGIN      
        1 mhrttrikit elnphlmcvl cggyfidatt iieclhsfck tcivrylets kycpicdvqv
       61 hktrpllnir sdktlqdivy klvpglfkne mkrrrdfyaa hpsadaangs nedrgevade
      121 dkriitddei islsieffdq nrldrkvnkd kekskeevnd krylrcpaam tvmhlrkflr
      181 skmdipntfq idvmyeeepl kdyytlmdia yiytwrrngp lplkyrvrpt ckrmkishqr
      241 dgltnagele sdsgsdkans paggipstss clpspstpvq sphpqfphis stmngtsnsp
      301 sgnhqssfan rprkssvngs satssg
//
LOCUS       NP_001424222            1070 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            beta isoform isoform 1 [Homo sapiens].
ACCESSION   NP_001424222 XP_016862108 XP_054202828
VERSION     NP_001424222.1
DBSOURCE    REFSEQ: accession NM_001437293.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Liu,L., Feng,X., Fan,C., Kong,D., Feng,X., Sun,C., Xu,Y., Li,B.,
            Jiang,Y. and Zheng,C.
  TITLE     PDCD4 interacting with PIK3CB and CTSZ promotes the apoptosis of
            multiple myeloma cells
  JOURNAL   FASEB J 38 (16), e70024 (2024)
   PUBMED   39190024
  REMARK    GeneRIF: PDCD4 interacting with PIK3CB and CTSZ promotes the
            apoptosis of multiple myeloma cells.
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Liu,G., Hou,Y., Jin,X., Zhang,Y., Sun,C., Huang,C., Ren,Y., Gao,J.,
            Wang,X. and Jiang,X.
  TITLE     PI3K/HSCB axis facilitates FOG1 nuclear translocation to promote
            erythropoiesis and megakaryopoiesis
  JOURNAL   Elife 13, 95815 (2024)
   PUBMED   38757931
  REMARK    GeneRIF: PI3K/HSCB axis facilitates FOG1 nuclear translocation to
            promote erythropoiesis and megakaryopoiesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1070)
  AUTHORS   Duewell,B.R., Wilson,N.E., Bailey,G.M., Peabody,S.E. and
            Hansen,S.D.
  TITLE     Molecular dissection of PI3Kbeta synergistic activation by receptor
            tyrosine kinases, GbetaGgamma, and Rho-family GTPases
  JOURNAL   Elife 12, 88991 (2024)
   PUBMED   38713746
  REMARK    GeneRIF: Molecular dissection of PI3Kbeta synergistic activation by
            receptor tyrosine kinases, GbetaGgamma, and Rho-family GTPases.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1070)
  AUTHORS   Xu,W., Chen,Y., Zhang,Z., Jiang,Y. and Wang,Z.
  TITLE     Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma
  JOURNAL   Med Oncol 40 (8), 221 (2023)
   PUBMED   37402056
  REMARK    GeneRIF: Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1070)
  AUTHORS   Milani,D., Mazzoni,M., Borgatti,P., Zauli,G., Cantley,L. and
            Capitani,S.
  TITLE     Extracellular human immunodeficiency virus type-1 Tat protein
            activates phosphatidylinositol 3-kinase in PC12 neuronal cells
  JOURNAL   J Biol Chem 271 (38), 22961-22964 (1996)
   PUBMED   8798481
REFERENCE   7  (residues 1 to 1070)
  AUTHORS   Bonnefoy-Berard,N., Liu,Y.C., von Willebrand,M., Sung,A., Elly,C.,
            Mustelin,T., Yoshida,H., Ishizaka,K. and Altman,A.
  TITLE     Inhibition of phosphatidylinositol 3-kinase activity by association
            with 14-3-3 proteins in T cells
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10142-10146 (1995)
   PUBMED   7479742
REFERENCE   8  (residues 1 to 1070)
  AUTHORS   Hu,P. and Schlessinger,J.
  TITLE     Direct association of p110 beta phosphatidylinositol 3-kinase with
            p85 is mediated by an N-terminal fragment of p110 beta
  JOURNAL   Mol Cell Biol 14 (4), 2577-2583 (1994)
   PUBMED   8139559
REFERENCE   9  (residues 1 to 1070)
  AUTHORS   Hu,P., Mondino,A., Skolnik,E.Y. and Schlessinger,J.
  TITLE     Cloning of a novel, ubiquitously expressed human
            phosphatidylinositol 3-kinase and identification of its binding
            site on p85
  JOURNAL   Mol Cell Biol 13 (12), 7677-7688 (1993)
   PUBMED   8246984
REFERENCE   10 (residues 1 to 1070)
  AUTHORS   Carpenter,C.L., Duckworth,B.C., Auger,K.R., Cohen,B.,
            Schaffhausen,B.S. and Cantley,L.C.
  TITLE     Purification and characterization of phosphoinositide 3-kinase from
            rat liver
  JOURNAL   J Biol Chem 265 (32), 19704-19711 (1990)
   PUBMED   2174051
  REMARK    GeneRIF: This paper reports the first purification of a
            phosphoinositide 3-kinase and shows that the protein is a
            heterodimer of an 85 kd regulatory subunit that mediates binding to
            phosphorylated proteins and a 110 kd catalytic subunit.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC067728.25, AC117389.5 and AC020890.22.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_016862108.1, XP_054202828.1.
            
            Summary: This gene encodes an isoform of the catalytic subunit of
            phosphoinositide 3-kinase (PI3K). These kinases are important in
            signaling pathways involving receptors on the outer membrane of
            eukaryotic cells and are named for their catalytic subunit. The
            encoded protein is the catalytic subunit for PI3Kbeta (PI3KB).
            PI3KB has been shown to be part of the activation pathway in
            neutrophils which have bound immune complexes at sites of injury or
            infection. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.955432.1,
                                           SRR11853561.21286.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..1070
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit beta isoform isoform 1"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.1.153"
                     /note="PI3-kinase p110 subunit beta; PtdIns-3-kinase p110;
                     PI3K-beta; PI3-kinase subunit beta; ptdIns-3-kinase
                     subunit beta; ptdIns-3-kinase subunit p110-beta;
                     phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa
                     catalytic subunit beta; serine/threonine protein kinase
                     PIK3CB; phosphoinositide-3-kinase, catalytic, beta
                     polypeptide"
                     /calculated_mol_wt=122632
     Region          41..118
                     /region_name="PI3K_p85B"
                     /note="PI3-kinase family, p85-binding domain; smart00143"
                     /db_xref="CDD:197539"
     Region          180..288
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, Ras-binding domain; smart00144"
                     /db_xref="CDD:197540"
     Region          324..501
                     /region_name="C2_PI3K_class_I_beta_delta"
                     /note="C2 domain present in class I beta and delta
                     phosphatidylinositol 3-kinases (PI3Ks); cd08693"
                     /db_xref="CDD:176075"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI9; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     Region          410..418
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Region          532..702
                     /region_name="PI3Ka_I"
                     /note="Phosphoinositide 3-kinase (PI3K) class I, accessory
                     domain; PIK domain is conserved in all PI3 and
                     PI4-kinases. Its role is unclear but it has been suggested
                     to be involved in substrate presentation. In general, PI3K
                     class I prefer phosphoinositol (4,5)...; cd00872"
                     /db_xref="CDD:238444"
     Region          706..1067
                     /region_name="PI3Kc_IA_beta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase beta; cd05173"
                     /db_xref="CDD:270717"
     Region          778..784
                     /region_name="G-loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(779,781..783,785,803,805,808,839,851..854,859,862,
                     924,926,936..937)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270717"
     Site            order(846..847,874..875,878,948..949,962,965,973..976,979,
                     1046,1049..1050,1052..1053)
                     /site_type="other"
                     /note="regulatory subunit interface [polypeptide binding]"
                     /db_xref="CDD:270717"
     Site            893
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270717"
     Region          916..924
                     /region_name="Catalytic loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            916..924
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270717"
     Region          935..961
                     /region_name="Activation loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(937..950,956..961)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270717"
     Site            1070
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12502714; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     CDS             1..1070
                     /gene="PIK3CB"
                     /gene_synonym="P110BETA; PI3K; PI3KBETA; PIK3C1"
                     /coded_by="NM_001437293.1:478..3690"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="GeneID:5291"
                     /db_xref="HGNC:HGNC:8976"
                     /db_xref="MIM:602925"
ORIGIN      
        1 mcfsfimppa madildiwav dsqiasdgsi pvdfllptgi yiqlevprea tisyikqmlw
       61 kqvhnypmfn llmdidsymf acvnqtavye eledetrrlc dvrpflpvlk lvtrscdpge
      121 kldskigvli gkglhefdsl kdpevnefrr kmrkfseeki lslvglswmd wlkqtyppeh
      181 epsipenled klyggkliva vhfencqdvf sfqvspnmnp ikvnelaiqk rltihgkede
      241 vspydyvlqv sgrveyvfgd hpliqfqyir ncvmnralph filvecckik kmyeqemiai
      301 eaainrnssn lplplppkkt riishvwenn npfqivlvkg nklnteetvk vhvraglfhg
      361 tellcktivs sevsgkndhi wneplefdin icdlprmarl cfavyavldk vktkkstkti
      421 npskyqtirk agkvhypvaw vntmvfdfkg qlrtgdiilh swssfpdele emlnpmgtvq
      481 tnpytenata lhvkfpenkk qpyyyppfdk iiekaaeias sdsanvssrg gkkflpvlke
      541 ildrdplsql cenemdliwt lrqdcreifp qslpklllsi kwnkledvaq lqallqiwpk
      601 lpprealell dfnypdqyvr eyavgclrqm sdeelsqyll qlvqvlkyep fldcalsrfl
      661 leralgnrri gqflfwhlrs evhipavsvq fgvileaycr gsvghmkvls kqvealnklk
      721 tlnsliklna vklnrakgke amhtclkqsa yrealsdlqs plnpcvilse lyvekckymd
      781 skmkplwlvy nnkvfgedsv gvifkngddl rqdmltlqml rlmdllwkea gldlrmlpyg
      841 clatgdrsgl ievvstseti adiqlnssnv aaaaafnkda llnwlkeyns gddldraiee
      901 ftlscagycv asyvlgigdr hsdnimvkkt gqlfhidfgh ilgnfkskfg ikrervpfil
      961 tydfihviqq gktgntekfg rfrqcceday lilrrhgnlf itlfalmlta glpeltsvkd
     1021 iqylkdslal gkseeealkq fkqkfdealr eswttkvnwm ahtvrkdyrs
//
LOCUS       NP_001396234            2445 aa            linear   PRI 21-NOV-2025
DEFINITION  histone-lysine N-methyltransferase, H3 lysine-36 specific isoform d
            [Homo sapiens].
ACCESSION   NP_001396234
VERSION     NP_001396234.1
DBSOURCE    REFSEQ: accession NM_001409305.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2445)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2445)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   3  (residues 1 to 2445)
  AUTHORS   Conteduca,G., Cangelosi,D., Baldo,C., Arado,A., Testa,B.,
            Wagner,R.T., Robertson,K.D., Dequiedt,F., Fitzsimmons,L.,
            Malacarne,M., Filaci,G. and Coviello,D.A.
  TITLE     Impact of NSD1 Alternative Transcripts in Actin Filament Formation
            and Cellular Division Pathways in Fibroblasts
  JOURNAL   Genes (Basel) 15 (9), 1117 (2024)
   PUBMED   39336709
  REMARK    GeneRIF: Impact of NSD1 Alternative Transcripts in Actin Filament
            Formation and Cellular Division Pathways in Fibroblasts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2445)
  AUTHORS   Ren,Z., Yue,L., Hu,H.Y., Hou,X.L., Chen,W.Q., Tan,Y., Dong,Z. and
            Zhang,J.
  TITLE     Identification of Novel NSD1 variations in four Pediatric cases
            with sotos Syndrome
  JOURNAL   BMC Med Genomics 17 (1), 116 (2024)
   PUBMED   38684994
  REMARK    GeneRIF: Identification of Novel NSD1 variations in four Pediatric
            cases with sotos Syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2445)
  AUTHORS   Wang,X., Yeh,S., Wu,G., Hsu,C.L., Wang,L., Chiang,T., Yang,Y.,
            Guo,Y. and Chang,C.
  TITLE     Identification and characterization of a novel androgen receptor
            coregulator ARA267-alpha in prostate cancer cells
  JOURNAL   J Biol Chem 276 (44), 40417-40423 (2001)
   PUBMED   11509567
REFERENCE   6  (residues 1 to 2445)
  AUTHORS   Jaju,R.J., Fidler,C., Haas,O.A., Strickson,A.J., Watkins,F.,
            Clark,K., Cross,N.C., Cheng,J.F., Aplan,P.D., Kearney,L.,
            Boultwood,J. and Wainscoat,J.S.
  TITLE     A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in
            de novo childhood acute myeloid leukemia
  JOURNAL   Blood 98 (4), 1264-1267 (2001)
   PUBMED   11493482
REFERENCE   7  (residues 1 to 2445)
  AUTHORS   Lee,D.K., Duan,H.O. and Chang,C.
  TITLE     Androgen receptor interacts with the positive elongation factor
            P-TEFb and enhances the efficiency of transcriptional elongation
  JOURNAL   J Biol Chem 276 (13), 9978-9984 (2001)
   PUBMED   11266437
REFERENCE   8  (residues 1 to 2445)
  AUTHORS   Huang,N., vom Baur,E., Garnier,J.M., Lerouge,T., Vonesch,J.L.,
            Lutz,Y., Chambon,P. and Losson,R.
  TITLE     Two distinct nuclear receptor interaction domains in NSD1, a novel
            SET protein that exhibits characteristics of both corepressors and
            coactivators
  JOURNAL   EMBO J 17 (12), 3398-3412 (1998)
   PUBMED   9628876
REFERENCE   9  (residues 1 to 2445)
  AUTHORS   Ocansey,S., Cole,T.R.P., Rahman,N. and Tatton-Brown,K.
  TITLE     Sotos Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301652
REFERENCE   10 (residues 1 to 2445)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027314.5, AC008570.6 and
            AC146507.2.
            
            Summary: This gene encodes a protein containing a SET domain, 2
            LXXLL motifs, 3 nuclear translocation signals (NLSs), 4 plant
            homeodomain (PHD) finger regions, and a proline-rich region. The
            encoded protein enhances androgen receptor (AR) transactivation,
            and this enhancement can be increased further in the presence of
            other androgen receptor associated coregulators. This protein may
            act as a nucleus-localized, basic transcriptional factor and also
            as a bifunctional transcriptional regulator. Mutations of this gene
            have been associated with Sotos syndrome and Weaver syndrome. One
            version of childhood acute myeloid leukemia is the result of a
            cryptic translocation with the breakpoints occurring within nuclear
            receptor-binding Su-var, enhancer of zeste, and trithorax domain
            protein 1 on chromosome 5 and nucleoporin, 98-kd on chromosome 11.
            Multiple transcript variants encoding distinct isoforms have been
            identified for this gene. [provided by RefSeq, Sep 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2665806.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2445
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..2445
                     /product="histone-lysine N-methyltransferase, H3 lysine-36
                     specific isoform d"
                     /EC_number="2.1.1.357"
                     /note="androgen receptor-associated coregulator 267;
                     histone-lysine N-methyltransferase, H3 lysine-36 and H4
                     lysine-20 specific; H3-K36-HMTase; H4-K20-HMTase; lysine
                     N-methyltransferase 3B; NR-binding SET domain-containing
                     protein; androgen receptor coactivator 267 kDa protein;
                     androgen receptor-associated protein of 267 kDa; nuclear
                     receptor-binding SET domain-containing protein 1; nuclear
                     receptor SET domain-containing protein 1; histone-lysine
                     N-methyltransferase, H3 lysine-36 specific"
                     /calculated_mol_wt=269016
     Region          27..182
                     /region_name="PWWP_NSD1_rpt1"
                     /note="first PWWP domain found in nuclear receptor-binding
                     SET domain-containing protein 1 (NSD1) and similar
                     proteins; cd20161"
                     /db_xref="CDD:438989"
     Site            order(43,46,117)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438989"
     Site            44..47
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438989"
     Site            order(155..157,160..161)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438989"
     Region          <1180..1336
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          1294..1336
                     /region_name="PHD1_NSD1_2"
                     /note="PHD finger 1 found in nuclear receptor-binding SET
                     domain-containing protein NSD1 and NSD2; cd15648"
                     /db_xref="CDD:277118"
     Site            order(1294,1303..1307,1312,1330)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277118"
     Region          1341..1387
                     /region_name="PHD2_NSD1"
                     /note="PHD finger 2 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15650"
                     /db_xref="CDD:277120"
     Site            order(1341,1351..1355,1361,1382)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277120"
     Region          1388..1441
                     /region_name="PHD3_NSD1"
                     /note="PHD finger 3 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15653"
                     /db_xref="CDD:277123"
     Site            order(1388,1406..1410,1414,1436)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277123"
     Region          1458..1497
                     /region_name="PHD4_NSD1"
                     /note="PHD finger 4 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15656"
                     /db_xref="CDD:277126"
     Site            order(1458,1467..1471,1475,1492)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277126"
     Region          1504..1599
                     /region_name="PWWP_NSD1_rpt2"
                     /note="second PWWP domain found in nuclear
                     receptor-binding SET domain-containing protein 1 (NSD1)
                     and similar proteins; cd20164"
                     /db_xref="CDD:438992"
     Site            order(1516,1519,1547)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438992"
     Site            1517..1520
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438992"
     Region          1650..1688
                     /region_name="AWS"
                     /note="AWS domain; pfam17907"
                     /db_xref="CDD:465559"
     Region          1690..1831
                     /region_name="SET_NSD1"
                     /note="SET domain (including post-SET domain) found in
                     nuclear receptor-binding SET domain-containing protein 1
                     (NSD1) and similar proteins; cd19210"
                     /db_xref="CDD:380987"
     Site            order(1701..1703,1720,1730,1734,1743..1749,1766..1770,
                     1777..1779,1794,1805..1815,1817..1821,1830)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380987"
     Site            order(1701..1703,1743..1746,1766..1770,1807,1814,
                     1818..1821,1830)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380987"
     Site            order(1720,1730,1734,1745..1749,1777..1779,1794,
                     1805..1809)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:380987"
     Site            order(1772,1819,1821,1826)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380987"
     Region          1869..1911
                     /region_name="PHD5_NSD1"
                     /note="PHD finger 5 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15659"
                     /db_xref="CDD:277129"
     Site            order(1869,1878..1882,1888,1906)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277129"
     Region          1910..1959
                     /region_name="C5HCH"
                     /note="NSD Cys-His rich domain; pfam17982"
                     /db_xref="CDD:465605"
     Region          <1957..2323
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..2445
                     /gene="NSD1"
                     /gene_synonym="ARA267; KMT3B; SOTOS; SOTOS1; STO"
                     /coded_by="NM_001409305.1:288..7625"
                     /note="isoform d is encoded by transcript variant 8"
                     /db_xref="GeneID:64324"
                     /db_xref="HGNC:HGNC:14234"
                     /db_xref="MIM:606681"
ORIGIN      
        1 mlelpgtsss stsqelpfcq pkkkstplky evgdliwakf krrpwwpcri csdplinths
       61 kmkdgvslls rlecsggisa hcnprllsss dshasasqva witvsnrrpy rqyyveafgd
      121 pserawvagk aivmfegrhq feelpvlrrr gkqkekgyrh kvpqkilskw easvglaeqy
      181 dvpkgsknrk cipgsiklds eedmpfedct ndpesehdll lngclkslaf dsehsadeke
      241 kpcaksrark ssdnpkrtsv kkghiqfeah kderrgkipe nlglnfisgd isdtqasnel
      301 sriansltgs ntapgsflfs scgkntakke fetsngdsll glpegalisk csreknkpqr
      361 slvcgskvkl cyigagdeek rsdsisictt sddgssdldp iehssesdns vleipdafdr
      421 tenmlsmqkn ekikysrfaa tntrvkakqk plisnshtdh lmgctksaep gtetsqvnls
      481 dlkastlvhk pqsdftndal spkfnlsssi ssenslikgg aanqallhsk skqpkfrsik
      541 ckhkenpvma eppvineecs lkccssdtkg splasisksg kvdglkllnn mhektrdssd
      601 ietavvkhvl selkelsyrs lgedvsdsgt skpskpllfs sassqnhipi epdykfstll
      661 mmlkdmhdsk tkeqrlmtaq nlvsyrspgr gdcstnspvg vskvlvsggs thnsekkgdg
      721 tqnsanpsps ggdsalsgel saslpgllsd krdlpasgks rsdcvtrrnc grskpssklr
      781 dafsaqmvkn tvnrkalkte rkrklnqlps vtldavlqgd rerggslrgg aedpskedpl
      841 qimghltsed gdhfsdvhfd skvkqsdpgk isekglsfen gkgpeldsvm nsendelngv
      901 nqvvpkkrwq rlnqrrtkpr krmnrfkeke nsecafrvll psdpvqegrd efpehrtpsa
      961 sileeplteq nhadcldsag prlnvcdkss asigdmekep gipsltpqae lpepavrsek
     1021 krlrkpskwl leyteeydqi fapkkkqkkv qeqvhkvssr ceeesllarg rssaqnkqvd
     1081 enslistkee ppvlereapf legplaqsel ggghaelpql tlsvpvapev sprpalesee
     1141 llvktpgnye skrqrkptkk llesndldpg fmpkkgdlgl skkcyeaghl engitescat
     1201 syskdfgggt tkifdkprkr krqrhaaakm qckkvkndds skeipgsege lmphrtatsp
     1261 ketveegveh dpgmpaskkm qgergggaal kenvcqncek lgelllceaq ccgafhlecl
     1321 gltemprgkf icnecrtgih tcfvckqsge dvkrcllplc gkfyheecvq kypptvmqnk
     1381 gfrcslhici tchaanpanv saskgrlmrc vrcpvayhan dfclaagski lasnsiicpn
     1441 hftprrgcrn hehvnvswcf vcseggsllc cdscpaafhr eclnidipeg nwycndckag
     1501 kkphyreivw vkvgryrwwp aeichpravp snidkmrhdv gefpvlffgs ndylwthqar
     1561 vfpymegdvs skdkmgkgvd gtykkalqea aarfeelkaq kelrqlqedr kndkkpppyk
     1621 hikvnrpigr vqiftadlse iprcnckatd enpcgidsec inrmllyech ptvcpaggrc
     1681 qnqcfskrqy peveifrtlq rgwglrtktd ikkgefvney vgelideeec rariryaqeh
     1741 ditnfymltl dkdriidagp kgnyarfmnh ccqpncetqk wsvngdtrvg lfalsdikag
     1801 teltfnynle clgngktvck cgapncsgfl gvrpknqpia teekskkfkk kqqgkrrtqg
     1861 eitkeredec fscgdagqlv sckkpgcpkv yhadclnltk rpagkwecpw hqcdicgkea
     1921 asfcemcpss fckqhregml fiskldgrls ctehdpcgpn plepgeirey vpppvplppg
     1981 psthlaeqst gmaaqapkms dkppadtnqm lslskkalag tcqrpllper plertdsrpq
     2041 pldkvrdlag sgtksqslvs sqrpldrppa vagprpqlsd kpspvtspss spsvrsqple
     2101 rplgtadprl dksigaaspr pqslektsvp tglrlpppdr llitsspkpq tsdrptdkph
     2161 aslsqrlppp ekvlsavvqt lvakekalrp vdqntqsknr aalvmdlidl tprqkeraas
     2221 phqvtpqade kmpvlesssw paskglghmp ravekgcvsd plqtsgkaaa psedpwqavk
     2281 sltqarllsq ppakaflyep ttqasgrasa gaeqtpgpls qspglvkqak qmvggqqlpa
     2341 laaksgqsfr slgkapaslp teekklvtte qspwalgkas sraglwpiva gqtlaqscws
     2401 agstqtlaqt cwslgrgqdp kpeqntlpal nqapsshkca eseqk
//
LOCUS       NP_001427352             429 aa            linear   PRI 21-NOV-2025
DEFINITION  interleukin-10 receptor subunit alpha isoform 2 [Homo sapiens].
ACCESSION   NP_001427352
VERSION     NP_001427352.1
DBSOURCE    REFSEQ: accession NM_001440423.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Grk,M., Miskovic,R., Jeremic,I., Basaric,M., Dusanovic Pjevic,M.,
            Jekic,B., Miljanovic,D., Lazarevic,I., Despotovic,A., Cirkovic,A.
            and Banko,A.
  TITLE     Association of IL10RA, IL10RB, and IL22RA Polymorphisms/Haplotypes
            with Susceptibility to and Clinical Manifestations of SLE
  JOURNAL   Int J Mol Sci 24 (14), 11292 (2023)
   PUBMED   37511050
  REMARK    GeneRIF: Association of IL10RA, IL10RB, and IL22RA
            Polymorphisms/Haplotypes with Susceptibility to and Clinical
            Manifestations of SLE.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Hanna,B.S., Llao-Cid,L., Iskar,M., Roessner,P.M., Klett,L.C.,
            Wong,J.K.L., Paul,Y., Ioannou,N., Ozturk,S., Mack,N., Kalter,V.,
            Colomer,D., Campo,E., Bloehdorn,J., Stilgenbauer,S., Dietrich,S.,
            Schmidt,M., Gabriel,R., Rippe,K., Feuerer,M., Ramsay,A.G.,
            Lichter,P., Zapatka,M. and Seiffert,M.
  TITLE     Interleukin-10 receptor signaling promotes the maintenance of a
            PD-1int TCF-1+ CD8+ T cell population that sustains anti-tumor
            immunity
  JOURNAL   Immunity 54 (12), 2825-2841 (2021)
   PUBMED   34879221
  REMARK    GeneRIF: Interleukin-10 receptor signaling promotes the maintenance
            of a PD-1(int) TCF-1(+) CD8(+) T cell population that sustains
            anti-tumor immunity.
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Nedelkopoulou,N., Taparkou,A., Agakidis,C., Mavroudi,A., Xinias,I.
            and Farmaki,E.
  TITLE     IL-10 receptor expression on lymphocytes and monocytes in children
            with food allergy
  JOURNAL   Pediatr Allergy Immunol 32 (5), 1108-1111 (2021)
   PUBMED   33595140
  REMARK    GeneRIF: IL-10 receptor expression on lymphocytes and monocytes in
            children with food allergy.
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Tang,Z., Zhang,P., Ji,M., Yin,C., Zhao,R., Huang,Z. and Huang,Y.
  TITLE     Characterization of novel and large fragment deletions in exon 1 of
            the IL10RA gene in Chinese children with very early onset
            inflammatory bowel diseases
  JOURNAL   BMC Gastroenterol 21 (1), 167 (2021)
   PUBMED   33849446
  REMARK    GeneRIF: Characterization of novel and large fragment deletions in
            exon 1 of the IL10RA gene in Chinese children with very early onset
            inflammatory bowel diseases.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Saxton,R.A., Tsutsumi,N., Su,L.L., Abhiraman,G.C., Mohan,K.,
            Henneberg,L.T., Aduri,N.G., Gati,C. and Garcia,K.C.
  TITLE     Structure-based decoupling of the pro- and anti-inflammatory
            functions of interleukin-10
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33737461
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Finbloom,D.S. and Winestock,K.D.
  TITLE     IL-10 induces the tyrosine phosphorylation of tyk2 and Jak1 and the
            differential assembly of STAT1 alpha and STAT3 complexes in human T
            cells and monocytes
  JOURNAL   J Immunol 155 (3), 1079-1090 (1995)
   PUBMED   7543512
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Carson,W.E., Lindemann,M.J., Baiocchi,R., Linett,M., Tan,J.C.,
            Chou,C.C., Narula,S. and Caligiuri,M.A.
  TITLE     The functional characterization of interleukin-10 receptor
            expression on human natural killer cells
  JOURNAL   Blood 85 (12), 3577-3585 (1995)
   PUBMED   7540068
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Tan,J.C., Braun,S., Rong,H., DiGiacomo,R., Dolphin,E., Baldwin,S.,
            Narula,S.K., Zavodny,P.J. and Chou,C.C.
  TITLE     Characterization of recombinant extracellular domain of human
            interleukin-10 receptor
  JOURNAL   J Biol Chem 270 (21), 12906-12911 (1995)
   PUBMED   7759550
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Taniyama,T., Takai,S., Miyazaki,E., Fukumura,R., Sato,J.,
            Kobayashi,Y., Hirakawa,T., Moore,K.W. and Yamada,K.
  TITLE     The human interleukin-10 receptor gene maps to chromosome 11q23.3
  JOURNAL   Hum Genet 95 (1), 99-101 (1995)
   PUBMED   7814035
REFERENCE   10 (residues 1 to 429)
  AUTHORS   Liu,Y., Wei,S.H., Ho,A.S., de Waal Malefyt,R. and Moore,K.W.
  TITLE     Expression cloning and characterization of a human IL-10 receptor
  JOURNAL   J Immunol 152 (4), 1821-1829 (1994)
   PUBMED   8120391
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002962.2.
            
            Summary: The protein encoded by this gene is a receptor for
            interleukin 10. This protein is structurally related to interferon
            receptors. It has been shown to mediate the immunosuppressive
            signal of interleukin 10, and thus inhibits the synthesis of
            proinflammatory cytokines. This receptor is reported to promote
            survival of progenitor myeloid cells through the insulin receptor
            substrate-2/PI 3-kinase/AKT pathway. Activation of this receptor
            leads to tyrosine phosphorylation of JAK1 and TYK2 kinases. Two
            transcript variants, one protein-coding and the other not
            protein-coding, have been found for this gene. [provided by RefSeq,
            Jan 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038195.703141.1, SRR18074968.660908.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1966682, SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..429
                     /product="interleukin-10 receptor subunit alpha isoform 2"
                     /note="interleukin-10 receptor alpha chain; IL-10R subunit
                     1; IL-10R subunit alpha; IL-10 receptor subunit alpha;
                     interleukin-10 receptor subunit 1; interleukin 10
                     receptor, alpha"
                     /calculated_mol_wt=46211
     Region          113..154
                     /region_name="JAK1bd_box_IFNLR1-like"
                     /note="JAK1 binding box domain found in interferon lambda
                     receptor 1 (IFNLR1), interleukin-10 receptor subunit alpha
                     (IL10RA) and similar proteins; cl45915"
                     /db_xref="CDD:459260"
     Site            order(113,116..124,126,128,130..134,136,138..139,141..149)
                     /site_type="other"
                     /note="JAK1 binding site [polypeptide binding]"
                     /db_xref="CDD:439313"
     CDS             1..429
                     /gene="IL10RA"
                     /gene_synonym="CD210; CD210a; CDW210A; HIL-10R; IL-10R1;
                     IL10R"
                     /coded_by="NM_001440423.1:215..1504"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:3587"
                     /db_xref="HGNC:HGNC:5964"
                     /db_xref="MIM:146933"
ORIGIN      
        1 mapandtyes ifshfreyei airkvpgnft fthkkvkhen fslltsgevg efcvqvkpsv
       61 asrsnkgmws keecisltrq yftvtnviif fafvlllsga layclalqly vrrrkklpsv
      121 llfkkpspfi fisqrpspet qdtihpldee aflkvspelk nldlhgstds gfgstkpslq
      181 teepqfllpd phpqadrtlg nreppvlgds cssgssnstd sgiclqepsl spstgptweq
      241 qvgsnsrgqd dsgidlvqns egragdtqgg salghhsppe pevpgeedpa avafqgylrq
      301 trcaeekatk tgcleeespl tdglgpkfgr clvdeaglhp palakgylkq dplemtlass
      361 gaptgqwnqp teewsllals scsdlgisdw sfahdlaplg cvaapggllg sfnsdlvtlp
      421 lisslqsse
//
LOCUS       NP_001394096             103 aa            linear   PRI 21-NOV-2025
DEFINITION  retinoblastoma-associated protein isoform 4 [Homo sapiens].
ACCESSION   NP_001394096
VERSION     NP_001394096.1
DBSOURCE    REFSEQ: accession NM_001407167.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Castro,A., Ruiz Rivera,A., Moorman,C.C., Wolf-Saxon,E.R.,
            Mims,H.N., Vasquez Meza,V.I., Rangel,M.A., Loera,M.M., Bond,I.C.,
            Buchanan,S.B., Villarreal,E., Tripathi,S., Rubin,S.M. and
            Burke,J.R.
  TITLE     Structural and functional analysis of cancer-associated missense
            variants in the retinoblastoma protein pocket domain
  JOURNAL   J Biol Chem 301 (3), 108284 (2025)
   PUBMED   39938803
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Zhang,S., Valenzuela,L.F., Zatulovskiy,E., Mangiante,L., Curtis,C.
            and Skotheim,J.M.
  TITLE     The G1-S transition is promoted by Rb degradation via the E3 ligase
            UBR5
  JOURNAL   Sci Adv 10 (43), eadq6858 (2024)
   PUBMED   39441926
  REMARK    GeneRIF: The G1-S transition is promoted by Rb degradation via the
            E3 ligase UBR5.
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Schwartz,C.J., Marra,A., Selenica,P., Gazzo,A., Tan,K., Ross,D.,
            Razavi,P., Chandarlapaty,S., Weigelt,B., Reis-Filho,J.S., Brogi,E.,
            Pareja,F. and Wen,H.Y.
  TITLE     RB1 Genetic Alterations in Estrogen Receptor-Positive Breast
            Carcinomas: Correlation With Neuroendocrine Differentiation
  JOURNAL   Mod Pathol 37 (8), 100541 (2024)
   PUBMED   38897452
  REMARK    GeneRIF: RB1 Genetic Alterations in Estrogen Receptor-Positive
            Breast Carcinomas: Correlation With Neuroendocrine Differentiation.
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Konagaya,Y., Rosenthal,D., Ratnayeke,N., Fan,Y. and Meyer,T.
  TITLE     An intermediate Rb-E2F activity state safeguards proliferation
            commitment
  JOURNAL   Nature 631 (8020), 424-431 (2024)
   PUBMED   38926571
  REMARK    GeneRIF: An intermediate Rb-E2F activity state safeguards
            proliferation commitment.
REFERENCE   6  (residues 1 to 103)
  AUTHORS   Lohmann,D.R. and Gallie,B.L.
  TITLE     Retinoblastoma
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301625
REFERENCE   7  (residues 1 to 103)
  AUTHORS   Dyson,N., Guida,P., Munger,K. and Harlow,E.
  TITLE     Homologous sequences in adenovirus E1A and human papillomavirus E7
            proteins mediate interaction with the same set of cellular proteins
  JOURNAL   J Virol 66 (12), 6893-6902 (1992)
   PUBMED   1331501
REFERENCE   8  (residues 1 to 103)
  AUTHORS   Huang,S., Shin,E., Sheppard,K.A., Chokroverty,L., Shan,B.,
            Qian,Y.W., Lee,E.Y. and Yee,A.S.
  TITLE     The retinoblastoma protein region required for interaction with the
            E2F transcription factor includes the T/E1A binding and
            carboxy-terminal sequences
  JOURNAL   DNA Cell Biol 11 (7), 539-548 (1992)
   PUBMED   1388726
REFERENCE   9  (residues 1 to 103)
  AUTHORS   Onadim,Z., Hogg,A., Baird,P.N. and Cowell,J.K.
  TITLE     Oncogenic point mutations in exon 20 of the RB1 gene in families
            showing incomplete penetrance and mild expression of the
            retinoblastoma phenotype
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 6177-6181 (1992)
   PUBMED   1352883
REFERENCE   10 (residues 1 to 103)
  AUTHORS   Hogg,A., Onadim,Z., Baird,P.N. and Cowell,J.K.
  TITLE     Detection of heterozygous mutations in the RB1 gene in
            retinoblastoma patients using single-strand conformation
            polymorphism analysis and polymerase chain reaction sequencing
  JOURNAL   Oncogene 7 (7), 1445-1451 (1992)
   PUBMED   1352398
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL392048.9.
            
            Summary: The protein encoded by this gene is a negative regulator
            of the cell cycle and was the first tumor suppressor gene found.
            The encoded protein also stabilizes constitutive heterochromatin to
            maintain the overall chromatin structure. The active,
            hypophosphorylated form of the protein binds transcription factor
            E2F1. Defects in this gene are a cause of childhood cancer
            retinoblastoma (RB), bladder cancer, and osteogenic sarcoma.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4487405.1,
                                           SRR14038192.1192638.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.2"
     Protein         1..103
                     /product="retinoblastoma-associated protein isoform 4"
                     /note="retinoblastoma-associated protein;
                     prepro-retinoblastoma-associated protein; protein
                     phosphatase 1, regulatory subunit 130; retinoblastoma
                     suspectibility protein; retinoblastoma 1"
                     /calculated_mol_wt=11230
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            2
                     /site_type="methylation"
                     /note="N,N-dimethylproline.
                     /evidence=ECO:0000250|UniProtKB:P13405; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P06400.2)"
     CDS             1..103
                     /gene="RB1"
                     /gene_synonym="OSRC; p105-Rb; p110-RB1; pp110; PPP1R130;
                     pRb; RB"
                     /coded_by="NM_001407167.1:163..474"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:5925"
                     /db_xref="HGNC:HGNC:9884"
                     /db_xref="MIM:614041"
ORIGIN      
        1 mppktprkta ataaaaaaep papppppppe edpeqdsgpe dlplvrlefe eteepdftal
       61 cqklkipdhv rerawltwek vssvdgvlvl rspvfkpwlt mgn
//
LOCUS       NP_001397794             679 aa            linear   PRI 21-NOV-2025
DEFINITION  IQ domain-containing protein E isoform 7 [Homo sapiens].
ACCESSION   NP_001397794 XP_047276038
VERSION     NP_001397794.1
DBSOURCE    REFSEQ: accession NM_001410865.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 679)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 679)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 679)
  AUTHORS   Estrada-Cuzcano,A., Etard,C., Delvallee,C., Stoetzel,C.,
            Schaefer,E., Scheidecker,S., Geoffroy,V., Schneider,A., Studer,F.,
            Mattioli,F., Chennen,K., Sigaudy,S., Plassard,D., Poch,O.,
            Piton,A., Strahle,U., Muller,J. and Dollfus,H.
  TITLE     Novel IQCE variations confirm its role in postaxial polydactyly and
            cause ciliary defect phenotype in zebrafish
  JOURNAL   Hum Mutat 41 (1), 240-254 (2020)
   PUBMED   31549751
  REMARK    GeneRIF: Novel IQCE variations confirm its role in postaxial
            polydactyly and cause ciliary defect phenotype in zebrafish.
REFERENCE   5  (residues 1 to 679)
  AUTHORS   Umair,M., Shah,K., Alhaddad,B., Haack,T.B., Graf,E., Strom,T.M.,
            Meitinger,T. and Ahmad,W.
  TITLE     Exome sequencing revealed a splice site variant in the IQCE gene
            underlying post-axial polydactyly type A restricted to lower limb
  JOURNAL   Eur J Hum Genet 25 (8), 960-965 (2017)
   PUBMED   28488682
  REMARK    GeneRIF: Frameshift and a premature stop codon 22 in IQCE
            completely co-segregated with post-axial polydactyly phenotype
            within the family.
REFERENCE   6  (residues 1 to 679)
  AUTHORS   Corominas,R., Yang,X., Lin,G.N., Kang,S., Shen,Y., Ghamsari,L.,
            Broly,M., Rodriguez,M., Tam,S., Wanamaker,S.A., Fan,C., Yi,S.,
            Tasan,M., Lemmens,I., Kuang,X., Zhao,N., Malhotra,D.,
            Michaelson,J.J., Vacic,V., Calderwood,M.A., Roth,F.P.,
            Tavernier,J., Horvath,S., Salehi-Ashtiani,K., Korkin,D., Sebat,J.,
            Hill,D.E., Hao,T., Vidal,M. and Iakoucheva,L.M.
  TITLE     Protein interaction network of alternatively spliced isoforms from
            brain links genetic risk factors for autism
  JOURNAL   Nat Commun 5, 3650 (2014)
   PUBMED   24722188
  REMARK    Erratum:[Nat Commun. 2023 Feb 2;14(1):569. doi:
            10.1038/s41467-023-36264-y. PMID: 36732511]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 679)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092488.3 and AC073462.8.
            
            On Aug 17, 2022 this sequence version replaced XP_047276038.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4167306.1,
                                           SRR14372080.494636.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..679
                     /product="IQ domain-containing protein E isoform 7"
                     /note="IQ domain-containing protein E"
                     /calculated_mol_wt=75527
     Region          <125..456
                     /region_name="Mplasa_alph_rch"
                     /note="helix-rich Mycoplasma protein; TIGR04523"
                     /db_xref="CDD:275316"
     CDS             1..679
                     /gene="IQCE"
                     /gene_synonym="1700028P05Rik; PAPA7"
                     /coded_by="NM_001410865.1:204..2243"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS94047.1"
                     /db_xref="GeneID:23288"
                     /db_xref="HGNC:HGNC:29171"
                     /db_xref="MIM:617631"
ORIGIN      
        1 mflgtgepal dtkakrkafh kppptspksp ylskprkvas wrslrtagsm plggrasltp
       61 qklwlgtakp gsltqalnsp ltwehawtgv pggtpdcltd tfrvkrphlr rsasnghvpg
      121 tpvyrekedm ydeiielkks lhvqksdvdl mrtklrrlee ensrkdrqie qlldpsrgtd
      181 fvrtlaekrp daswvinglk qrilkleqqc kekdgtiskl qtdmkttnle emriametyy
      241 eevhrlqtll assettgkkp lgekktgakr qkkmgsalls lsrsvqelte enqslkedld
      301 rvlstsptis ktqgyvewsk prllrrivel ekklsvmess kshaaepvrs hppaclasss
      361 alhrqprgdr nkdherlrga vrdlkeerta lqeqllqrdl evkqllqaka dlekelecar
      421 egeeerrere evlreeiqtl tsklqelqem kkeekedcpe vphkaqelpa ptpssrhceq
      481 dwppdsseeg lprprspcsd grrdaaarvl qaqwkvykhk kkkavldeaa vvlqaafrgh
      541 ltrtkllask ahgseppsvp glpdqsspvp rvpspiaqat gspvqeeaiv iiqsalrahl
      601 ararhsatgk rtttaastrr rsasathgda ssppflaalp dpspsgpqal aplpgddvns
      661 ddsddiviap slptknfpv
//
LOCUS       NP_001401163             272 aa            linear   PRI 21-NOV-2025
DEFINITION  L-lactate dehydrogenase B chain isoform 4 [Homo sapiens].
ACCESSION   NP_001401163
VERSION     NP_001401163.1
DBSOURCE    REFSEQ: accession NM_001414234.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Zhang,P., Wan,Y., Ma,J., Gong,J., Zhong,Z., Cui,Y., Zhang,H.,
            Da,Y., Ma,J., Li,C., Liu,L., Gong,T., Tan,Y. and Zhang,C.
  TITLE     Epigenetic silencing of LDHB promotes hepatocellular carcinoma by
            remodeling the tumor microenvironment
  JOURNAL   Cancer Immunol Immunother 73 (7), 127 (2024)
   PUBMED   38739169
  REMARK    GeneRIF: Epigenetic silencing of LDHB promotes hepatocellular
            carcinoma by remodeling the tumor microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Shi,F., Zhang,G., Li,J., Shu,L., Yu,C., Ren,D., Zhang,Y. and
            Zheng,P.
  TITLE     Integrated analysis of single cell-RNA sequencing and Mendelian
            randomization identifies lactate dehydrogenase B as a target of
            melatonin in ischemic stroke
  JOURNAL   CNS Neurosci Ther 30 (5), e14741 (2024)
   PUBMED   38702940
  REMARK    GeneRIF: Integrated analysis of single cell-RNA sequencing and
            Mendelian randomization identifies lactate dehydrogenase B as a
            target of melatonin in ischemic stroke.
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Stiebler,A.C., Freitag,J., Schink,K.O., Stehlik,T., Tillmann,B.A.,
            Ast,J. and Bolker,M.
  TITLE     Ribosomal readthrough at a short UGA stop codon context triggers
            dual localization of metabolic enzymes in Fungi and animals
  JOURNAL   PLoS Genet 10 (10), e1004685 (2014)
   PUBMED   25340584
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Schueren,F., Lingner,T., George,R., Hofhuis,J., Dickel,C.,
            Gartner,J. and Thoms,S.
  TITLE     Peroxisomal lactate dehydrogenase is generated by translational
            readthrough in mammals
  JOURNAL   Elife 3, e03640 (2014)
   PUBMED   25247702
  REMARK    GeneRIF: The readthrough-extended lactate dehydrogenase subunit
            LDHBx can also co-import LDHA, the other LDH subunit, into
            peroxisomes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
REFERENCE   7  (residues 1 to 272)
  AUTHORS   Takeno,T. and Li,S.S.
  TITLE     Structure of the human lactate dehydrogenase B gene
  JOURNAL   Biochem J 257 (3), 921-924 (1989)
   PUBMED   2930497
REFERENCE   8  (residues 1 to 272)
  AUTHORS   Sakai,I., Sharief,F.S., Pan,Y.C. and Li,S.S.
  TITLE     The cDNA and protein sequences of human lactate dehydrogenase B
  JOURNAL   Biochem J 248 (3), 933-936 (1987)
   PUBMED   3435492
REFERENCE   9  (residues 1 to 272)
  AUTHORS   Law,M.L. and Kao,F.T.
  TITLE     Regional assignment of human genes TPI1, GAPDH, LDHB, SHMT, and
            PEPB on chromosome 12
  JOURNAL   Cytogenet Cell Genet 24 (2), 102-114 (1979)
   PUBMED   477403
REFERENCE   10 (residues 1 to 272)
  AUTHORS   Rethore,M.O., Kaplan,J.C., Junien,C., Cruveiller,J., Dutrillaux,B.,
            Aurias,A., Carpentier,S., Lafourcade,J. and Lejeune.
  TITLE     [Increase of the LDH-B activity in a boy with 12p trisomy by
            malsegregation of a maternal translocation t(12;14) (q12;p11)]
  JOURNAL   Ann Genet 18 (2), 81-87 (1975)
   PUBMED   1081369
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010197.7.
            
            Summary: This gene encodes the B subunit of lactate dehydrogenase
            enzyme, which catalyzes the interconversion of pyruvate and lactate
            with concomitant interconversion of NADH and NAD+ in a
            post-glycolysis process. Alternatively spliced transcript variants
            have been found for this gene. Recent studies have shown that a
            C-terminally extended isoform is produced by use of an alternative
            in-frame translation termination codon via a stop codon readthrough
            mechanism, and that this isoform is localized in the peroxisomes.
            Mutations in this gene are associated with lactate dehydrogenase B
            deficiency. Pseudogenes have been identified on chromosomes X, 5
            and 13. [provided by RefSeq, Feb 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.40181.1,
                                           SRR18074967.3597223.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267756, SAMN03267763
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..272
                     /product="L-lactate dehydrogenase B chain isoform 4"
                     /EC_number="1.1.1.27"
                     /note="L-lactate dehydrogenase B chain; LDH heart subunit;
                     renal carcinoma antigen NY-REN-46; lactate dehydrogenase H
                     chain; epididymis secretory protein Li 281; testicular
                     secretory protein Li 25"
                     /calculated_mol_wt=30091
     Region          1..268
                     /region_name="LDH_1"
                     /note="A subgroup of L-lactate dehydrogenases; cd05293"
                     /db_xref="CDD:133429"
     Site            order(39,45,77,108,132,177,187)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133429"
     Site            order(120,123,125,142,147,204..206,209,236..237,240,
                     242..244)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:133429"
     CDS             1..272
                     /gene="LDHB"
                     /gene_synonym="HEL-S-281; LDH-B; LDH-H; LDHBD; TRG-5"
                     /coded_by="NM_001414234.1:150..968"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:3945"
                     /db_xref="HGNC:HGNC:6541"
                     /db_xref="MIM:150100"
ORIGIN      
        1 mmdlqhgslf lqtpkivadk dysvtanski vvvtagvrqq egesrlnlvq rnvnvfkfii
       61 pqivkyspdc iiivvsnpvd iltyvtwkls glpkhrvigs gcnldsarfr ylmaeklgih
      121 psschgwilg ehgdssvavw sgvnvagvsl qelnpemgtd ndsenwkevh kmvvesayev
      181 iklkgytnwa iglsvadlie smlknlsrih pvstmvkgmy gienevflsl pcilnarglt
      241 svinqklkdd evaqlkksad tlwdiqkdlk dl
//
LOCUS       NP_001427530             359 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform p [Homo sapiens].
ACCESSION   NP_001427530
VERSION     NP_001427530.1
DBSOURCE    REFSEQ: accession NM_001440601.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 359)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 359)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 359)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 359)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 359)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2238539.1,
                                           SRR14038192.3513115.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..359
                     /product="polycomb protein EED isoform p"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=40932
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Region          <23..357
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q921E6; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Region          66..106
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          111..148
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          158..220
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          227..275
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          283..323
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          331..355
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..359
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001440601.1:478..1557"
                     /note="isoform p is encoded by transcript variant 16"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdenvt lyechsqgei rllqsyvdad
       61 adenfytcaw tydsntshpl lavagsrgii riinpitmqc ikhyvghgna inelkfhprd
      121 pnlllsvskd halrlwniqt dtlvaifggv eghrdevlsa dydllgekim scgmdhslkl
      181 wrinskrmmn aikesydynp nktnrpfisq kihfpdfstr dihrnyvdcv rwlgdlilsk
      241 scenaivcwk pgkmeddidk ikpsesnvti lgrfdysqcd iwymrfsmdf wqkmlalgnq
      301 vgklyvwdle vedphkakct tlthhkcgaa irqtsfsrds siliavcdda siwrwdrlr
//
LOCUS       NP_001394387            2742 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform j [Homo sapiens].
ACCESSION   NP_001394387
VERSION     NP_001394387.1
DBSOURCE    REFSEQ: accession NM_001407458.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2742)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2742)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2742)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2742)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2742)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2742)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2742)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2742)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2742)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2742)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2679019.1,
                                           SRR18074967.1179438.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2742
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2742
                     /product="adenomatous polyposis coli protein isoform j"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=300309
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Region          <8..272
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          <307..365
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          364..407
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(398,402,406,441,445,449,485,489,493)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          411..452
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          415..452
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          459..494
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          502..543
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          548..588
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          552..586
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          590..630
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          594..630
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          631..918
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          935..1034
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1156..>1173
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1182..1267
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1190..1600
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1270..1292
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1536..1559
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1561..1614
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1615..1636
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1645..1738
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1772..1846
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1932..1951
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2122..2467
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2569..2742
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2742
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407458.1:171..8399"
                     /note="isoform j is encoded by transcript variant 28"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrriar iqqiekdilr irqllqsqat
      241 eaerssqnkh etgshdaerq negqgvgein matsgngqgs ttrmdhetas vlssssthsa
      301 prrltshlgt kiraycetcw ewqeahepgm dqdknpmpap vehqicpavc vlmklsfdee
      361 hrhamnelgg lqaiaellqv dcemygltnd hysitlrrya gmaltnltfg dvankatlcs
      421 mkgcmralva qlksesedlq qviasvlrnl swradvnskk tlrevgsvka lmecalevkk
      481 estlksvlsa lwnlsahcte nkadicavdg alaflvgtlt yrsqtntlai iesgggilrn
      541 vssliatned hrqilrennc lqtllqhlks hsltivsnac gtlwnlsarn pkdqealwdm
      601 gavsmlknli hskhkmiamg saaalrnlma nrpakykdan imspgsslps lhvrkqkale
      661 aeldaqhlse tfdnidnlsp kashrskqrh kqslygdyvf dtnrhddnrs dnfntgnmtv
      721 lspylnttvl psssssrgsl dssrsekdrs lerergiglg nyhpatenpg tsskrglqis
      781 ttaaqiakvm eevsaihtsq edrssgstte lhcvtderna lrrssaahth sntynftkse
      841 nsnrtcsmpy akleykrssn dslnsvsssd gygkrgqmkp siesysedde skfcsygqyp
      901 adlahkihsa nhmddndgel dtpinyslky sdeqlnsgrq spsqnerwar pkhiiedeik
      961 qseqrqsrnq sttypvytes tddkhlkfqp hfgqqecvsp yrsrgangse tnrvgsnhgi
     1021 nqnvsqslcq eddyeddkpt nyseryseee qheeeerptn ysikyneekr hvdqpidysl
     1081 kyatdipssq kqsfsfskss sgqssktehm ssssentstp ssnakrqnql hpssaqsrsg
     1141 qpqkaatckv ssinqetiqt ycvedtpicf srcsslssls saedeigcnq ttqeadsant
     1201 lqiaeikeki gtrsaedpvs evpavsqhpr tkssrlqgss lssesarhka vefssgaksp
     1261 sksgaqtpks ppehyvqetp lmfsrctsvs sldsfesrsi assvqsepcs gmvsgiisps
     1321 dlpdspgqtm ppsrsktppp ppqtaqtkre vpknkaptae kresgpkqaa vnaavqrvqv
     1381 lpdadtllhf atestpdgfs cssslsalsl depfiqkdve lrimppvqen dngneteseq
     1441 pkesnenqek eaektidsek dllddsdddd ieileeciis amptkssrka kkpaqtaskl
     1501 pppvarkpsq lpvykllpsq nrlqpqkhvs ftpgddmprv ycvegtpinf statslsdlt
     1561 iesppnelaa gegvrggaqs gefekrdtip tegrstdeaq ggktssvtip elddnkaeeg
     1621 dilaecinsa mpkgkshkpf rvkkimdqvq qasasssapn knqldgkkkk ptspvkpipq
     1681 nteyrtrvrk nadsknnlna ervfsdnkds kkqnlknnsk vfndklpnne drvrgsfafd
     1741 sphhytpieg tpycfsrnds lssldfdddd vdlsrekael rkakenkese akvtshtelt
     1801 snqqsanktq aiakqpinrg qpkpilqkqs tfpqsskdip drgaatdekl qnfaientpv
     1861 cfshnsslss lsdidqennn kenepikete ppdsqgepsk pqasgyapks fhvedtpvcf
     1921 srnsslssls idseddllqe cissampkkk kpsrlkgdne khsprnmggi lgedltldlk
     1981 diqrpdsehg lspdsenfdw kaiqegansi vsslhqaaaa aclsrqassd sdsilslksg
     2041 islgspfhlt pdqeekpfts nkgprilkpg ekstletkki eseskgikgg kkvykslitg
     2101 kvrsnseisg qmkqplqanm psisrgrtmi hipgvrnsss stspvskkgp plktpasksp
     2161 segqtattsp rgakpsvkse lspvarqtsq iggsskapsr sgsrdstpsr paqqplsrpi
     2221 qspgrnsisp grngisppnk lsqlprtssp stastkssgs gkmsytspgr qmsqqnltkq
     2281 tglsknassi prsesaskgl nqmnngngan kkvelsrmss tkssgsesdr serpvlvrqs
     2341 tfikeapspt lrrkleesas feslspssrp asptrsqaqt pvlspslpdm slsthssvqa
     2401 ggwrklppnl sptieyndgr pakrhdiars hsespsrlpi nrsgtwkreh skhssslprv
     2461 stwrrtgsss silsassess ekaksedekh vnsisgtkqs kenqvsakgt wrkikenefs
     2521 ptnstsqtvs sgatngaesk tliyqmapav sktedvwvri edcpinnprs grsptgntpp
     2581 vidsvsekan pnikdskdnq akqnvgngsv pmrtvglenr lnsfiqvdap dqkgteikpg
     2641 qnnpvpvset nessivertp fsssssskhs spsgtvaarv tpfnynpspr kssadstsar
     2701 psqiptpvnn ntkkrdsktd stessgtqsp krhsgsylvt sv
//
LOCUS       NP_001393991             509 aa            linear   PRI 21-NOV-2025
DEFINITION  merlin isoform 17 [Homo sapiens].
ACCESSION   NP_001393991
VERSION     NP_001393991.1
DBSOURCE    REFSEQ: accession NM_001407062.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 509)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 509)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 509)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 509)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 509)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 509)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005529.7 and AC004882.3.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3022454.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465405, SAMN03465406
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..509
                     /product="merlin isoform 17"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=59491
     Region          23..181
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          175..226
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          221..>281
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          260..379
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          432..509
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..509
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_001407062.1:367..1896"
                     /note="isoform 17 is encoded by transcript variant 24"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 magaiasrms fsslkrkqpk tftvrivtmd aemefncemk wkgkdlfdlv crtlglretw
       61 ffglqytikd tvawlkmdkk vkkqildeki ycppeasvll asyavqakyg dydpsvhkrg
      121 flaqeellpk rvinlyqmtp emweeritaw yaehrgrard eaemeylkia qdlemygvny
      181 fairftikpl dkkidvfkfn ssklrvnkli lqlcignhdl fmrrrkadsl evqqmkaqar
      241 eekarkqmer qrlarekqmr eeaertrdel errllqmkee atmanealmr seetadllae
      301 kaqiteeeak llaqkaaeae qemqrikata irteeekrlm eqkvleaevl alkmaeeser
      361 rakeadqlkq dlqeareaer rakqklleia tkptyppmnp ipaplppdip sfnligdsls
      421 fdfkdtdmkr lsmeiekekv eymekskhlq eqlnelktei ealklkeret aldilhnens
      481 drggsskhnt ikkltlqsak srvaffeel
//
LOCUS       NP_001428099             681 aa            linear   PRI 21-NOV-2025
DEFINITION  PHD finger protein 21A isoform c [Homo sapiens].
ACCESSION   NP_001428099 XP_005253022 XP_054225048
VERSION     NP_001428099.1
DBSOURCE    REFSEQ: accession NM_001441170.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 681)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 681)
  AUTHORS   Mustafa,S., Abbas,S., Mahmood,A., Khan,A.Z., Zeb,S., Khan,A. and
            Umair,M.
  TITLE     A novel de novo variant in the PHF21A causes craniofacial
            abnormalities, intellectual disability and skeletal manifestations
  JOURNAL   Clin Genet 104 (1), 142-144 (2023)
   PUBMED   36843358
  REMARK    GeneRIF: A novel de novo variant in the PHF21A causes craniofacial
            abnormalities, intellectual disability and skeletal manifestations.
REFERENCE   3  (residues 1 to 681)
  AUTHORS   Huang,J.Q., Ji,L.C., Jing,Q.A., He,Y.C., Ma,Y.Y. and Tong,X.M.
  TITLE     PHF21A expression as a biomarker of hepatocellular carcinoma
            progression and prognosis
  JOURNAL   Neoplasma 69 (6), 1349-1358 (2022)
   PUBMED   36305691
  REMARK    GeneRIF: PHF21A expression as a biomarker of hepatocellular
            carcinoma progression and prognosis.
REFERENCE   4  (residues 1 to 681)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 681)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 681)
  AUTHORS   Hailesellasse Sene,K., Porter,C.J., Palidwor,G., Perez-Iratxeta,C.,
            Muro,E.M., Campbell,P.A., Rudnicki,M.A. and Andrade-Navarro,M.A.
  TITLE     Gene function in early mouse embryonic stem cell differentiation
  JOURNAL   BMC Genomics 8, 85 (2007)
   PUBMED   17394647
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 681)
  AUTHORS   Shi,Y.J., Matson,C., Lan,F., Iwase,S., Baba,T. and Shi,Y.
  TITLE     Regulation of LSD1 histone demethylase activity by its associated
            factors
  JOURNAL   Mol Cell 19 (6), 857-864 (2005)
   PUBMED   16140033
REFERENCE   8  (residues 1 to 681)
  AUTHORS   Iwase,S., Januma,A., Miyamoto,K., Shono,N., Honda,A., Yanagisawa,J.
            and Baba,T.
  TITLE     Characterization of BHC80 in BRAF-HDAC complex, involved in
            neuron-specific gene repression
  JOURNAL   Biochem Biophys Res Commun 322 (2), 601-608 (2004)
   PUBMED   15325272
  REMARK    GeneRIF: Presumably serves as a scaffold protein in BHC in neuronal
            as well as non-neuronal cells. Possible role in spermatogenesis.
REFERENCE   9  (residues 1 to 681)
  AUTHORS   Hakimi,M.A., Dong,Y., Lane,W.S., Speicher,D.W. and Shiekhattar,R.
  TITLE     A candidate X-linked mental retardation gene is a component of a
            new family of histone deacetylase-containing complexes
  JOURNAL   J Biol Chem 278 (9), 7234-7239 (2003)
   PUBMED   12493763
REFERENCE   10 (residues 1 to 681)
  AUTHORS   Hakimi,M.A., Bochar,D.A., Chenoweth,J., Lane,W.S., Mandel,G. and
            Shiekhattar,R.
  TITLE     A core-BRAF35 complex containing histone deacetylase mediates
            repression of neuronal-specific genes
  JOURNAL   Proc Natl Acad Sci U S A 99 (11), 7420-7425 (2002)
   PUBMED   12032298
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC024475.15 and AC068385.9.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_005253022.1, XP_054225048.1.
            
            Summary: The PHF21A gene encodes BHC80, a component of a BRAF35
            (MIM 605535)/histone deacetylase (HDAC; see MIM 601241) complex
            (BHC) that mediates repression of neuron-specific genes through the
            cis-regulatory element known as repressor element-1 (RE1) or neural
            restrictive silencer (NRS) (Hakimi et al., 2002 [PubMed
            12032298]).[supplied by OMIM, Nov 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.2356354.1,
                                           SRR14038195.988442.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..681
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..681
                     /product="PHD finger protein 21A isoform c"
                     /note="BRAF35/HDAC2 complex (80 kDa); BHC80a; BRAF35-HDAC
                     complex protein BHC80"
                     /calculated_mol_wt=74851
     Region          82..118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          319..364
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          <375..537
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          441..464
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96BD5.1)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          487..681
                     /region_name="Required for transcriptional repression"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          491..533
                     /region_name="PHD_PHF21A"
                     /note="PHD finger found in PHD finger protein 21A
                     (PHF21A); cd15523"
                     /db_xref="CDD:276998"
     Site            order(491,498..503,523..526,528)
                     /site_type="other"
                     /note="histone H3 binding site [polypeptide binding]"
                     /db_xref="CDD:276998"
     Region          640..681
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     CDS             1..681
                     /gene="PHF21A"
                     /gene_synonym="BHC80; BM-006; IDDBCS; NEDMS"
                     /coded_by="NM_001441170.1:290..2335"
                     /note="isoform c is encoded by transcript variant 16"
                     /db_xref="GeneID:51317"
                     /db_xref="HGNC:HGNC:24156"
                     /db_xref="MIM:608325"
ORIGIN      
        1 melqtlqeal kveiqvhqkl vaqmkqdpqn adlkkqlhel qakitalsek qkrvveqlrk
       61 nlivkqeqpd kfqiqplpqs enklqtaqqq plqqlqqqqq yhhhhaqqsa aaspnltasq
      121 ktvttasmit tktlplvlka atatmpasvv gqrptiamvt ainsqkavls tdvqntpvnl
      181 qtsskvtgpg aeavqivakn tvtlqvqatp pqpikvpqfi ppprltprpn flpqvrpkpv
      241 aqnnipiapa pppmlaapql iqrpvmltkf tpttlptsqn sihpvrvvng qtatiaktfp
      301 maqltsivia tpgtrlagpq tvqlskpsle kqtvkshtet dekqtesrti tppaapkpkr
      361 eenpqklafm vslglvthdh leeiqskrqe rkrrttanpv ysgavfeper kksavtylns
      421 tmhpgtrkrg rppkynavlg fgaltptspq sshpdspene ktettftfpa pvqpvslpsp
      481 tstdgdihed fcsvcrksgq llmcdtcsrv yhldcldppl ktipkgmwic prcqdqmlkk
      541 eeaipwpgtl aivhsyiayk aakeeekqkl lkwssdlkqe reqleqkvkq lsnsiskcme
      601 mkntilarqk emhsslekvk qlirlihgid lskpvdseat vgaisngpdc tppanaatst
      661 papspssqsc tancnqgeet k
//
LOCUS       NP_001400602             359 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 6 precursor [Homo sapiens].
ACCESSION   NP_001400602
VERSION     NP_001400602.1
DBSOURCE    REFSEQ: accession NM_001413673.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 359)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 359)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 359)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 359)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 359)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1909562.1,
                                           SRR14038193.2701533.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..359
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 6 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=36559
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..342
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            277..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            313..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     CDS             1..359
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413673.1:169..1248"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 9"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvsyih gssqaqfvae shiilvlnaa itmgmvllne
      301 aatskgdvgk rriiclvglg lvvfffsfll sifrskyhgy pyrekssdkn vyqktdtws
//
LOCUS       NP_001427356             421 aa            linear   PRI 21-NOV-2025
DEFINITION  interleukin-12 receptor subunit beta-1 isoform 8 [Homo sapiens].
ACCESSION   NP_001427356 XP_011526279 XP_054176863
VERSION     NP_001427356.1
DBSOURCE    REFSEQ: accession NM_001440427.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Chen,H., Ge,X., Li,C., Zeng,J. and Wang,X.
  TITLE     Structure and assembly of the human IL-12 signaling complex
  JOURNAL   Structure 32 (10), 1640-1651 (2024)
   PUBMED   39111304
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Huang,J., He,Q., Huang,L., Liu,L., Yang,P. and Chen,M.
  TITLE     Discovering the link between IL12RB1 gene polymorphisms and
            tuberculosis susceptibility: a comprehensive meta-analysis
  JOURNAL   Front Public Health 12, 1249880 (2024)
   PUBMED   38317798
  REMARK    GeneRIF: Discovering the link between IL12RB1 gene polymorphisms
            and tuberculosis susceptibility: a comprehensive meta-analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Rosas Mejia,O., Claeys,T.A., Williams,A., Zafar,A. and
            Robinson,R.T.
  TITLE     IL12RB1 allele bias in human TH cells is regulated by functional
            SNPs in its 3'UTR
  JOURNAL   Cytokine 158, 155993 (2022)
   PUBMED   36007427
  REMARK    GeneRIF: IL12RB1 allele bias in human TH cells is regulated by
            functional SNPs in its 3'UTR.
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Khattak,F.A., Akbar,N.U., Riaz,M., Hussain,M., Rehman,K., Khan,S.N.
            and Khan,T.A.
  TITLE     Novel IL-12Rbeta1 deficiency-mediates recurrent cutaneous
            leishmaniasis
  JOURNAL   Int J Infect Dis 112, 338-345 (2021)
   PUBMED   34438084
  REMARK    GeneRIF: Novel IL-12Rbeta1 deficiency-mediates recurrent cutaneous
            leishmaniasis.
REFERENCE   5  (residues 1 to 421)
  AUTHORS   Yamamoto,K., Kobayashi,H., Miura,O., Hirosawa,S. and Miyasaka,N.
  TITLE     Assignment of IL12RB1 and IL12RB2, interleukin-12 receptor beta 1
            and beta 2 chains, to human chromosome 19 band p13.1 and chromosome
            1 band p31.2, respectively, by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 77 (3-4), 257-258 (1997)
   PUBMED   9284929
REFERENCE   6  (residues 1 to 421)
  AUTHORS   Bacon,C.M., Petricoin,E.F. 3rd, Ortaldo,J.R., Rees,R.C.,
            Larner,A.C., Johnston,J.A. and O'Shea,J.J.
  TITLE     Interleukin 12 induces tyrosine phosphorylation and activation of
            STAT4 in human lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 92 (16), 7307-7311 (1995)
   PUBMED   7638186
REFERENCE   7  (residues 1 to 421)
  AUTHORS   Bacon,C.M., McVicar,D.W., Ortaldo,J.R., Rees,R.C., O'Shea,J.J. and
            Johnston,J.A.
  TITLE     Interleukin 12 (IL-12) induces tyrosine phosphorylation of JAK2 and
            TYK2: differential use of Janus family tyrosine kinases by IL-2 and
            IL-12
  JOURNAL   J Exp Med 181 (1), 399-404 (1995)
   PUBMED   7528775
REFERENCE   8  (residues 1 to 421)
  AUTHORS   Ling,P., Gately,M.K., Gubler,U., Stern,A.S., Lin,P., Hollfelder,K.,
            Su,C., Pan,Y.C. and Hakimi,J.
  TITLE     Human IL-12 p40 homodimer binds to the IL-12 receptor but does not
            mediate biologic activity
  JOURNAL   J Immunol 154 (1), 116-127 (1995)
   PUBMED   7527811
REFERENCE   9  (residues 1 to 421)
  AUTHORS   Gillessen,S., Carvajal,D., Ling,P., Podlaski,F.J., Stremlo,D.L.,
            Familletti,P.C., Gubler,U., Presky,D.H., Stern,A.S. and Gately,M.K.
  TITLE     Mouse interleukin-12 (IL-12) p40 homodimer: a potent IL-12
            antagonist
  JOURNAL   Eur J Immunol 25 (1), 200-206 (1995)
   PUBMED   7843232
REFERENCE   10 (residues 1 to 421)
  AUTHORS   Chua,A.O., Chizzonite,R., Desai,B.B., Truitt,T.P., Nunes,P.,
            Minetti,L.J., Warrier,R.R., Presky,D.H., Levine,J.F., Gately,M.K.
            et al.
  TITLE     Expression cloning of a human IL-12 receptor component. A new
            member of the cytokine receptor superfamily with strong homology to
            gp130
  JOURNAL   J Immunol 153 (1), 128-136 (1994)
   PUBMED   7911493
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020904.7.
            
            On or before May 20, 2025 this sequence version replaced
            XP_011526279.1, XP_054176863.1.
            
            Summary: The protein encoded by this gene is a type I transmembrane
            protein that belongs to the hemopoietin receptor superfamily. This
            protein binds to interleukine 12 (IL12) with a low affinity, and is
            thought to be a part of IL12 receptor complex. This protein forms a
            disulfide-linked oligomer, which is required for its IL12 binding
            activity. The coexpression of this and IL12RB2 proteins was shown
            to lead to the formation of high-affinity IL12 binding sites and
            reconstitution of IL12 dependent signaling. Mutations in this gene
            impair the development of interleukin-17-producing T lymphocytes
            and result in increased susceptibility to mycobacterial and
            Salmonella infections. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1329669.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..421
                     /product="interleukin-12 receptor subunit beta-1 isoform
                     8"
                     /note="IL-12 receptor beta component; interleukin-12
                     receptor beta-1 chain; IL-12R subunit beta-1; IL-12
                     receptor subunit beta-1; cluster of differentiation 212;
                     interleukin 12 receptor, beta 1"
                     /calculated_mol_wt=46603
     CDS             1..421
                     /gene="IL12RB1"
                     /gene_synonym="CD212; IL-12R-BETA1; IL12RB; IMD30"
                     /coded_by="NM_001440427.1:163..1428"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:3594"
                     /db_xref="HGNC:HGNC:5971"
                     /db_xref="MIM:601604"
ORIGIN      
        1 mfvglfslls fnvfrsgdgv aeprrwqrgs pgavglyvdp meplvtwvvp llflfllsrq
       61 gaacrtsecc fqdppypdad sgsasgprdl rcyrissdry ecswqyegpt agvshflrcc
      121 lssgrccyfa agsatrlqfs dqagvsvlyt vtlwveswar nqtekspevt lqlynsvkye
      181 pplgdikvsk lagqlrmewe tpdnqvgaev qfrhrtpssp wklgdcgpqd ddtesclcpl
      241 emnvaqefql rrrqlgsqgs swskwsspvc vppenppqpq vrfsveqlgq dgrrrltlke
      301 qptqlelpeg cqglapgtev tyrlqlhmls cpckakatrt lhlgkmpyls gaaynvavis
      361 snqfgpglnq twhipadtht dgmisahcnl rlpdsrdspa sasrvagitg ichhtrlily
      421 f
//
LOCUS       NP_001428084             431 aa            linear   PRI 21-NOV-2025
DEFINITION  urokinase-type plasminogen activator isoform 1 preproprotein [Homo
            sapiens].
ACCESSION   NP_001428084
VERSION     NP_001428084.1
DBSOURCE    REFSEQ: accession NM_001441155.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Li,D., Ding,C., Huang,F., Chang,M., Lu,Z., Li,G., Li,Y., Gao,H. and
            Sun,F.
  TITLE     Bioinformatics Analysis of the Expression and Prognostic Value of
            PLAU Gene in Wilms' Tumor
  JOURNAL   Anticancer Res 44 (9), 3829-3842 (2024)
   PUBMED   39197889
  REMARK    GeneRIF: Bioinformatics Analysis of the Expression and Prognostic
            Value of PLAU Gene in Wilms' Tumor.
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Guo,J., Wang,H., Huang,C., Lai,C., Shang,W., Luo,S. and Chen,L.
  TITLE     PLAU, transcriptionally negatively regulated by GATA6, promotes
            lung squamous carcinoma cell proliferation and migration
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (5), 119744 (2024)
   PUBMED   38702016
  REMARK    GeneRIF: PLAU, transcriptionally negatively regulated by GATA6,
            promotes lung squamous carcinoma cell proliferation and migration.
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Cui,X., Sun,H., Liu,X., Bai,Y., Bai,Y., Cui,Y., Wang,B., Zhang,S.
            and Li,X.
  TITLE     PLAU promotes cell proliferation and migration of head and neck
            cancer via STAT3 signaling pathway
  JOURNAL   Exp Cell Res 438 (2), 114056 (2024)
   PUBMED   38663475
  REMARK    GeneRIF: PLAU promotes cell proliferation and migration of head and
            neck cancer via STAT3 signaling pathway.
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Cetinsoy,O., Anyanwu,I., Krishnanand,H., Natarajan,G.,
            Ramachandran,N., Thomas,A. and Brookes,K.J.
  TITLE     Gene Association Study of the Urokinase Plasminogen Activator and
            Its Receptor Gene in Alzheimer's Disease
  JOURNAL   J Alzheimers Dis 99 (1), 241-250 (2024)
   PUBMED   38669542
  REMARK    GeneRIF: Gene Association Study of the Urokinase Plasminogen
            Activator and Its Receptor Gene in Alzheimer's Disease.
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Mekkawy,A.H., Pourgholami,M.H. and Morris,D.L.
  TITLE     Involvement of urokinase-type plasminogen activator system in
            cancer: an overview
  JOURNAL   Med Res Rev 34 (5), 918-956 (2014)
   PUBMED   24549574
  REMARK    Review article
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Naldini,L., Tamagnone,L., Vigna,E., Sachs,M., Hartmann,G.,
            Birchmeier,W., Daikuhara,Y., Tsubouchi,H., Blasi,F. and
            Comoglio,P.M.
  TITLE     Extracellular proteolytic cleavage by urokinase is required for
            activation of hepatocyte growth factor/scatter factor
  JOURNAL   EMBO J 11 (13), 4825-4833 (1992)
   PUBMED   1334458
REFERENCE   8  (residues 1 to 431)
  AUTHORS   Li,X., Smith,R.A. and Dobson,C.M.
  TITLE     Sequential 1H NMR assignments and secondary structure of the
            kringle domain from urokinase
  JOURNAL   Biochemistry 31 (40), 9562-9571 (1992)
   PUBMED   1327118
REFERENCE   9  (residues 1 to 431)
  AUTHORS   Stephens,R.W., Aumailley,M., Timpl,R., Reisberg,T., Tapiovaara,H.,
            Myohanen,H., Murphy-Ullrich,J. and Vaheri,A.
  TITLE     Urokinase binding to laminin-nidogen. Structural requirements and
            interactions with heparin
  JOURNAL   Eur J Biochem 207 (3), 937-942 (1992)
   PUBMED   1499567
REFERENCE   10 (residues 1 to 431)
  AUTHORS   Moroi,M. and Aoki,N.
  TITLE     Isolation and characterization of alpha2-plasmin inhibitor from
            human plasma. A novel proteinase inhibitor which inhibits
            activator-induced clot lysis
  JOURNAL   J Biol Chem 251 (19), 5956-5965 (1976)
   PUBMED   134998
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22.
            
            Summary: This gene encodes a secreted serine protease that converts
            plasminogen to plasmin. The encoded preproprotein is
            proteolytically processed to generate A and B polypeptide chains.
            These chains associate via a single disulfide bond to form the
            catalytically inactive high molecular weight urokinase-type
            plasminogen activator (HMW-uPA). HMW-uPA can be further processed
            into the catalytically active low molecular weight urokinase-type
            plasminogen activator (LMW-uPA). This low molecular weight form
            does not bind to the urokinase-type plasminogen activator receptor.
            Mutations in this gene may be associated with Quebec platelet
            disorder and late-onset Alzheimer's disease. Alternative splicing
            results in multiple transcript variants, at least one of which
            encodes an isoform that is proteolytically processed. [provided by
            RefSeq, Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2229725.1,
                                           SRR14038192.2031826.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2156266, SAMEA2162946
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..431
                     /product="urokinase-type plasminogen activator isoform 1
                     preproprotein"
                     /EC_number="3.4.21.73"
                     /note="plasminogen activator, urinary; U-plasminogen
                     activator; urokinase-type plasminogen activator"
                     /calculated_mol_wt=46384
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2158
     mat_peptide     21..431
                     /product="Urokinase-type plasminogen activator.
                     /id=PRO_0000028318"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=46384
     mat_peptide     21..177
                     /product="Urokinase-type plasminogen activator long chain
                     A. /id=PRO_0000028319"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=17849
     Region          34..57
                     /region_name="Binds urokinase plasminogen activator
                     surface receptor. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
     Site            38
                     /site_type="glycosylation"
                     /note="O-linked (Fuc) threonine.
                     /evidence=ECO:0000269|PubMed:2023947; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Region          67..152
                     /region_name="KR"
                     /note="Kringle domain; Kringle domains are believed to
                     play a role in binding mediators, such as peptides, other
                     proteins, membranes, or phospholipids. They are autonomous
                     structural domains, found in a varying number of copies,
                     in blood clotting and...; cd00108"
                     /db_xref="CDD:238056"
     Site            79
                     /site_type="active"
                     /note="putative domain interaction site [active]"
                     /db_xref="CDD:238056"
     Site            order(94,104,132,134,143)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Region          152..177
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
     mat_peptide     156..177
                     /product="Urokinase-type plasminogen activator short chain
                     A. /id=PRO_0000028320"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=2574
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9151681; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Site            177..178
                     /site_type="cleavage"
                     /note="Cleavage, during zymogen activation; propagated
                     from UniProtKB/Swiss-Prot (P00749.3)"
     mat_peptide     179..431
                     /product="Urokinase-type plasminogen activator chain B.
                     /id=PRO_0000028321"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=28425
     Region          179..422
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            179
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(224,275,376)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            322
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine. /id=CAR_000026;
                     propagated from UniProtKB/Swiss-Prot (P00749.3)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9151681; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Site            order(370,395,397)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..431
                     /gene="PLAU"
                     /gene_synonym="ATF; BDPLT5; QPD; u-PA; UPA; URK"
                     /coded_by="NM_001441155.1:248..1543"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:5328"
                     /db_xref="HGNC:HGNC:9052"
                     /db_xref="MIM:191840"
ORIGIN      
        1 mrallarlll cvlvvsdskg snelhqvpsn cdclnggtcv snkyfsnihw cncpkkfggq
       61 hceidksktc yegnghfyrg kastdtmgrp clpwnsatvl qqtyhahrsd alqlglgkhn
      121 ycrnpdnrrr pwcyvqvglk llvqecmvhd cadgkkpssp peelkfqcgq ktlrprfkii
      181 ggefttienq pwfaaiyrrh rggsvtyvcg gslispcwvi sathcfidyp kkedyivylg
      241 rsrlnsntqg emkfevenli lhkdysadtl ahhndiallk irskegrcaq psrtiqticl
      301 psmyndpqfg tsceitgfgk enstdylype qlkmtvvkli shrecqqphy ygsevttkml
      361 caadpqwktd scqgdsggpl vcslqgrmtl tgivswgrgc alkdkpgvyt rvshflpwir
      421 shtkeengla l
//
LOCUS       NP_001171511             277 aa            linear   PRI 21-NOV-2025
DEFINITION  syntaxin-3 isoform 2 [Homo sapiens].
ACCESSION   NP_001171511
VERSION     NP_001171511.1
DBSOURCE    REFSEQ: accession NM_001178040.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Shinozuka,T., Kanda,M., Sato,Y., Shimizu,D., Tanaka,C., Umeda,S.,
            Inokawa,Y., Hattori,N., Hayashi,M., Nakayama,G. and Kodera,Y.
  TITLE     Increased STX3 transcript and protein levels were associated with
            poor prognosis in two independent cohorts of esophageal squamous
            cell carcinoma patients
  JOURNAL   Cancer Med 12 (24), 22185-22195 (2023)
   PUBMED   38014487
  REMARK    GeneRIF: Increased STX3 transcript and protein levels were
            associated with poor prognosis in two independent cohorts of
            esophageal squamous cell carcinoma patients.
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Janecke,A.R., Liu,X., Adam,R., Punuru,S., Viestenz,A., Strauss,V.,
            Laass,M., Sanchez,E., Adachi,R., Schatz,M.P., Saboo,U.S.,
            Mittal,N., Rohrschneider,K., Escher,J., Ganesh,A., Al Zuhaibi,S.,
            Al Murshedi,F., AlSaleem,B., Alfadhel,M., Al Sinani,S.,
            Alkuraya,F.S., Huber,L.A., Muller,T., Heidelberger,R. and Janz,R.
  TITLE     Pathogenic STX3 variants affecting the retinal and intestinal
            transcripts cause an early-onset severe retinal dystrophy in
            microvillus inclusion disease subjects
  JOURNAL   Hum Genet 140 (8), 1143-1156 (2021)
   PUBMED   33974130
  REMARK    GeneRIF: Pathogenic STX3 variants affecting the retinal and
            intestinal transcripts cause an early-onset severe retinal
            dystrophy in microvillus inclusion disease subjects.
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Low,S.H., Vasanji,A., Nanduri,J., He,M., Sharma,N., Koo,M.,
            Drazba,J. and Weimbs,T.
  TITLE     Syntaxins 3 and 4 are concentrated in separate clusters on the
            plasma membrane before the establishment of cell polarity
  JOURNAL   Mol Biol Cell 17 (2), 977-989 (2006)
   PUBMED   16339081
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Martin-Martin,B., Nabokina,S.M., Lazo,P.A. and Mollinedo,F.
  TITLE     Co-expression of several human syntaxin genes in neutrophils and
            differentiating HL-60 cells: variant isoforms and detection of
            syntaxin 1
  JOURNAL   J Leukoc Biol 65 (3), 397-406 (1999)
   PUBMED   10080545
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Steegmaier,M., Yang,B., Yoo,J.S., Huang,B., Shen,M., Yu,S., Luo,Y.
            and Scheller,R.H.
  TITLE     Three novel proteins of the syntaxin/SNAP-25 family
  JOURNAL   J Biol Chem 273 (51), 34171-34179 (1998)
   PUBMED   9852078
REFERENCE   8  (residues 1 to 277)
  AUTHORS   Riento,K., Galli,T., Jansson,S., Ehnholm,C., Lehtonen,E. and
            Olkkonen,V.M.
  TITLE     Interaction of Munc-18-2 with syntaxin 3 controls the association
            of apical SNAREs in epithelial cells
  JOURNAL   J Cell Sci 111 (Pt 17), 2681-2688 (1998)
   PUBMED   9701566
REFERENCE   9  (residues 1 to 277)
  AUTHORS   Galli,T., Zahraoui,A., Vaidyanathan,V.V., Raposo,G., Tian,J.M.,
            Karin,M., Niemann,H. and Louvard,D.
  TITLE     A novel tetanus neurotoxin-insensitive vesicle-associated membrane
            protein in SNARE complexes of the apical plasma membrane of
            epithelial cells
  JOURNAL   Mol Biol Cell 9 (6), 1437-1448 (1998)
   PUBMED   9614185
REFERENCE   10 (residues 1 to 277)
  AUTHORS   Delgrossi,M.H., Breuza,L., Mirre,C., Chavrier,P. and Le Bivic,A.
  TITLE     Human syntaxin 3 is localized apically in human intestinal cells
  JOURNAL   J Cell Sci 110 (Pt 18), 2207-2214 (1997)
   PUBMED   9378770
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000640.5.
            
            Summary: The gene is a member of the syntaxin family. The encoded
            protein is targeted to the apical membrane of epithelial cells
            where it forms clusters and is important in establishing and
            maintaining polarity necessary for protein trafficking involving
            vesicle fusion and exocytosis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.466292.1,
                                           SRR11853561.5012.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..277
                     /product="syntaxin-3 isoform 2"
                     /note="syntaxin 3A; syntaxin 3B"
                     /calculated_mol_wt=31887
     Region          34..226
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     Region          227..>265
                     /region_name="SNARE"
                     /note="SNARE domain; pfam05739"
                     /db_xref="CDD:461727"
     CDS             1..277
                     /gene="STX3"
                     /gene_synonym="DIAR12; MVID2; RDMVID; STX3A"
                     /coded_by="NM_001178040.3:231..1064"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS53637.1"
                     /db_xref="GeneID:6809"
                     /db_xref="HGNC:HGNC:11438"
                     /db_xref="MIM:600876"
ORIGIN      
        1 mkdrleqlka kqltqdddtd aveiaidnta fmdeffseie etrlnidkis ehveeakkly
       61 siilsapipe pktkddleql tteikkrann vrnklksmek hieedevrss adlrirksqh
      121 svlsrkfvev mtkyneaqvd frerskgriq rqleitgkkt tdeeleemle sgnpaiftsg
      181 iidsqiskqa lseiegrhkd ivrlessike lhdmfmdiam lvenqgemld nielnvmhtv
      241 dhvekardet kkavkyqsqa rkklislqtg vatlvfr
//
LOCUS       NP_001400672             952 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform f [Homo sapiens].
ACCESSION   NP_001400672
VERSION     NP_001400672.1
DBSOURCE    REFSEQ: accession NM_001413743.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 952)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 952)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 952)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 952)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 952)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 952)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 952)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 952)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 952)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 952)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.714377.1,
                                           SRR18074969.1970718.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..952
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..952
                     /product="polyhomeotic-like protein 1 isoform f"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=99961
     Region          <422..618
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          776..883
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          883..951
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(901..902,936..937,940..941,944)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(912..916,918..919,922..923,927,932)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..952
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413743.1:368..3226"
                     /note="isoform f is encoded by transcript variant 7"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq aslgnllqvn rtlgrnvpla
      121 sqlilmpnga vaavqqevps aqspgvhada dqvqnlavrn qqasaqgpqm qgstqkaipp
      181 gaspvsslsq assqalavaq assgatnqsl nlsqagggsg nsipgsmgpg gggqahgglg
      241 qlpssgmggg scprkgtgvv qplpaaqtvt vsqgsqteae saaakkaead gsgqqnvgmn
      301 ltrtatpaps qtlissatyt qiqphsliqq qqqihlqqkq vviqqqiaih hqqqfqhrqs
      361 qllhtathlq laqqqqqqqq qqqqqqqpqa ttltapqppq vpptqqvpps qsqqqaqtlv
      421 vqpmlqsspl slppdaapkp pipiqskppv apikppqlga akmsaaqqpp phipvqvvgt
      481 rqpgtaqaqa lglaqlaaav ptsrgmpgtv qsgqahlass ppssqapgal qecpptlapg
      541 mtlapvqgta hvvkggatts spvvaqvpaa fymqsvhlpg kpqtlavkrk adseeerddv
      601 stlgsmlpak aspvaespkv mdeksslgek aesvanvnan tpsselvalt papsvppptl
      661 amvsrqmgds kppqaivkpq ilthiiegfv iqegaepfpv gcsqllkese kplqtglptg
      721 ltenqsggpl gvdspsaeld kkanllkcey cgkyapaeqf rgskrfcsmt cakrynvscs
      781 hqfrlkrkkm kefqeanyar vrrrgprrss sdiarakiqg kchrgqedss rgsdnssyde
      841 alsptspgpl svraghgerd lgnpntappt pelhginpvf lssnpsrwsv eevyefiasl
      901 qgcqeiaeef rsqeidgqal lllkeehlms amniklgpal kicakinvlk et
//
LOCUS       NP_001424248             903 aa            linear   PRI 21-NOV-2025
DEFINITION  ephrin type-A receptor 5 isoform h [Homo sapiens].
ACCESSION   NP_001424248 XP_047305718 XP_054205162
VERSION     NP_001424248.1
DBSOURCE    REFSEQ: accession NM_001437319.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 903)
  AUTHORS   Han,X., Liu,T., Zhai,J., Liu,C., Wang,W., Nie,C., Wang,Q., Zhu,X.,
            Zhou,H. and Tian,W.
  TITLE     Association between EPHA5 methylation status in peripheral blood
            leukocytes and the risk and prognosis of gastric cancer
  JOURNAL   PeerJ 10, e13774 (2022)
   PUBMED   36164608
  REMARK    GeneRIF: Association between EPHA5 methylation status in peripheral
            blood leukocytes and the risk and prognosis of gastric cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 903)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   3  (residues 1 to 903)
  AUTHORS   Liu,C., He,Y., Feng,X., Li,J. and Wang,J.
  TITLE     Expression of EPHA5 in lung adenocarcinoma is associated with lymph
            node metastasis and EGFR mutation
  JOURNAL   APMIS 130 (6), 338-345 (2022)
   PUBMED   35332588
  REMARK    GeneRIF: Expression of EPHA5 in lung adenocarcinoma is associated
            with lymph node metastasis and EGFR mutation.
REFERENCE   4  (residues 1 to 903)
  AUTHORS   Abouhashem,N., Harb,O., Elwan,A., Zaitoun,M. and Saraya,Y.
  TITLE     Immunohistochemical evaluation of forkhead box A1 and EphA5 markers
            in serous ovarian carcinomas, and their impact on the clinical
            outcome of patients
  JOURNAL   Pol J Pathol 73 (2), 120-133 (2022)
   PUBMED   36345952
  REMARK    GeneRIF: Immunohistochemical evaluation of forkhead box A1 and
            EphA5 markers in serous ovarian carcinomas, and their impact on the
            clinical outcome of patients.
REFERENCE   5  (residues 1 to 903)
  AUTHORS   Zhou,R.
  TITLE     Regulation of topographic projection by the Eph family receptor Bsk
            (EphA5) and its ligands
  JOURNAL   Cell Tissue Res 290 (2), 251-259 (1997)
   PUBMED   9321686
  REMARK    Review article
REFERENCE   6  (residues 1 to 903)
  AUTHORS   Miescher,G.C., Taylor,V., Olivieri,G., Mindermann,T., Schrock,E.
            and Steck,A.J.
  TITLE     Extensive splice variation and localization of the EHK-1 receptor
            tyrosine kinase in adult human brain and glial tumors
  JOURNAL   Brain Res Mol Brain Res 46 (1-2), 17-24 (1997)
   PUBMED   9191074
REFERENCE   7  (residues 1 to 903)
  AUTHORS   Gale,N.W., Holland,S.J., Valenzuela,D.M., Flenniken,A., Pan,L.,
            Ryan,T.E., Henkemeyer,M., Strebhardt,K., Hirai,H., Wilkinson,D.G.,
            Pawson,T., Davis,S. and Yancopoulos,G.D.
  TITLE     Eph receptors and ligands comprise two major specificity subclasses
            and are reciprocally compartmentalized during embryogenesis
  JOURNAL   Neuron 17 (1), 9-19 (1996)
   PUBMED   8755474
REFERENCE   8  (residues 1 to 903)
  AUTHORS   Winslow,J.W., Moran,P., Valverde,J., Shih,A., Yuan,J.Q., Wong,S.C.,
            Tsai,S.P., Goddard,A., Henzel,W.J., Hefti,F. et al.
  TITLE     Cloning of AL-1, a ligand for an Eph-related tyrosine kinase
            receptor involved in axon bundle formation
  JOURNAL   Neuron 14 (5), 973-981 (1995)
   PUBMED   7748564
REFERENCE   9  (residues 1 to 903)
  AUTHORS   Fox,G.M., Holst,P.L., Chute,H.T., Lindberg,R.A., Janssen,A.M.,
            Basu,R. and Welcher,A.A.
  TITLE     cDNA cloning and tissue distribution of five human EPH-like
            receptor protein-tyrosine kinases
  JOURNAL   Oncogene 10 (5), 897-905 (1995)
   PUBMED   7898931
REFERENCE   10 (residues 1 to 903)
  AUTHORS   Spritz,R.A., Strunk,K.M., Lee,S.T., Lu-Kuo,J.M., Ward,D.C., Le
            Paslier,D., Altherr,M.R., Dorman,T.E. and Moir,D.T.
  TITLE     A YAC contig spanning a cluster of human type III receptor protein
            tyrosine kinase genes (PDGFRA-KIT-KDR) in chromosome segment 4q12
  JOURNAL   Genomics 22 (2), 431-436 (1994)
   PUBMED   7528718
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104137.5, AC105923.6 and
            AC018683.4.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_047305718.1, XP_054205162.1.
            
            Summary: This gene belongs to the ephrin receptor subfamily of the
            protein-tyrosine kinase family. EPH and EPH-related receptors have
            been implicated in mediating developmental events, particularly in
            the nervous system. Receptors in the EPH subfamily typically have a
            single kinase domain and an extracellular region containing a
            Cys-rich domain and 2 fibronectin type III repeats. The ephrin
            receptors are divided into 2 groups based on the similarity of
            their extracellular domain sequences and their affinities for
            binding ephrin-A and ephrin-B ligands. Alternatively spliced
            transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1625321.1,
                                           SRR14038191.1804936.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..903
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q13.1-q13.2"
     Protein         1..903
                     /product="ephrin type-A receptor 5 isoform h"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-A receptor 5; receptor protein-tyrosine
                     kinase HEK7; tyrosine-protein kinase receptor EHK-1;
                     EPH-like kinase 7; EPH homology kinase 1; brain-specific
                     kinase; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=100368
     Region          60..232
                     /region_name="EphR_LBD_A5"
                     /note="Ligand Binding Domain of Ephrin type-A Receptor 5;
                     cd10483"
                     /db_xref="CDD:198451"
     Site            order(84,86..90,97..98,100,102,133,135,140..141,183,
                     187..188,191..193,220..222,224)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198451"
     Region          357..447
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(357,420,435)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(436..437,439..440)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          463..538
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Region          536..802
                     /region_name="PTKc_EphR_A"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphA Ephrin Receptors; cd05066"
                     /db_xref="CDD:270651"
     Site            order(547,549..551,555,571,573,619..620,622,666,670..671,
                     673,684,703..707,716,750)
                     /site_type="active"
                     /db_xref="CDD:270651"
     Site            order(547..551,555,571,573,619..622,625..626,670..671,673,
                     684)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270651"
     Site            order(666,670,703..707,716,750)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270651"
     Site            683..709
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270651"
     Region          831..896
                     /region_name="SAM_EPH-A5"
                     /note="SAM domain of EPH-A5 subfamily of tyrosine kinase
                     receptors; cd09546"
                     /db_xref="CDD:188945"
     Site            order(848,881)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188945"
     CDS             1..903
                     /gene="EPHA5"
                     /gene_synonym="CEK7; EHK-1; EHK1; EK7; HEK7; TYRO4"
                     /coded_by="NM_001437319.1:748..3459"
                     /note="isoform h is encoded by transcript variant 8"
                     /db_xref="GeneID:2044"
                     /db_xref="HGNC:HGNC:3389"
                     /db_xref="MIM:600004"
ORIGIN      
        1 mrgsgprgag rrrppsgggd tpitpaslag cysaprrapl wtclllcaal rtllaspsne
       61 vnlldsrtvm gdlgwiafpk ngweeigevd enyapihtyq vckvmeqnqn nwlltswisn
      121 egasrifiel kftlrdcnsl pgglgtcket fnmyyfesdd qngrnikenq yikidtiaad
      181 esfteldlgd rvmklntevr dvgplskkgf ylafqdvgac ialvsvrvyy kkcpsvvrhl
      241 avfpdtitga dssqllevsg scvnhsvtde ppkmhcsaeg ewlvpigkcm ckagyeekng
      301 tcqvcrpgff kasphiqscg kcpphsythe eastscvcek dyfrresdpp tmacttpspv
      361 tnvkkgkiak nsislswqep drpngiiley eikyfekdqe tsytiikske ttitaeglkp
      421 asvyvfqira rtaagygvfs rrfefettpv faassdqsqi pviavsvtvg villavvigv
      481 llsgrrcgys kakqdpeeek mhfhnghikl pgvrtyidph tyedpnqavh efakeieasc
      541 itiervigag efgevcsgrl klpgkrelpv aiktlkvgyt ekqrrdflge asimgqfdhp
      601 niihlegvvt kskpvmivte ymengsldtf lkkndgqftv iqlvgmlrgi sagmkylsdm
      661 gyvhrdlaar nilinsnlvc kvsdfglsrv leddpeaayt trggkipirw tapeaiafrk
      721 ftsasdvwsy givmwevvsy gerpywemtn qdvikaveeg yrlpspmdcp aalyqlmldc
      781 wqkernsrpk fdeivnmldk lirnpsslkt lvnascrvsn llaehsplgs gayrsvgewl
      841 eaikmgryte ifmengyssm davaqvtled lrrlgvtlvg hqkkimnslq emkvqlvngm
      901 vpl
//
LOCUS       NP_001389639            1086 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 19 [Homo sapiens].
ACCESSION   NP_001389639
VERSION     NP_001389639.1
DBSOURCE    REFSEQ: accession NM_001402710.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1086)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1086)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1086)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1086)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1086)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1086)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1086)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2678291.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1086
                     /product="kinectin isoform 19"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=125152
     Region          <142..>400
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          296..>1026
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1086
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402710.1:178..3438"
                     /note="isoform 19 is encoded by transcript variant 33"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mvpskrqeal plhqetkqes gsgkkkassk kqktenvfvd eplihattyi plmdnadssp
       61 vvdkrevidl lkpdqvegiq ksgtkklkte tdkenaevkf kdfllslktm mfsedealcv
      121 vdllkeksgv iqdalkkssk gelttlihql qekdkllaav kedaaatkdr ckqltqemmt
      181 ekersnvvit rmkdrigtle kehnvfqnki hvsyqetqqm qmkfqqvreq meaeiahlkq
      241 engilrdavs nttnqleskq saelnklrqd yarlvnelte ktgklqqeev qkknaeqaat
      301 qlkvqlqeae rrweevqsyi rkrtaeheaa qqdlqskfva kenevqslhs kltdtlvskq
      361 qleqrlmqlm eseqkrvnke eslqmqvqdi leqnealkaq iqqfhsqiaa qtsasvlaee
      421 lhkviaekdk qikqtedsla serdrltske eelkdiqnmn fllkaevqkl qalaneqaaa
      481 ahelekmqqs vyvkddkirl leeqlqheis nkmeefkiln dqnkalksev qklqtlvseq
      541 pnkdvveqme kciqekdekl ktveelletg liqvatkeee lnairtenss ltkevqdlka
      601 kqndqvsfas lveelkkvih ekdgkiksve elleaellkv ankektvqdl kqeikalkee
      661 ignvqlekaq qlsitskvqe lqnllkgkee qmntmkavle ekekdlantg kwlqdlqeen
      721 eslkahvqev aqhnlkeass asqfeeleiv lkekenelkr leamlkeres dlssktqllq
      781 dvqdenklfk sqieqlkqqn yqqassfpph eellkviser ekeisglwne ldslkdaveh
      841 qrkknnsyge wlhgfekkak ecmagtsgse evkvlehklk eademhtllq lecekyksvl
      901 aetegilqkl qrsveqeenk wkvkvdeshk tikqmqssft sseqelerlr senkdienlr
      961 rerehlemel ekaemersty vtevrelkaq lnetltklrt eqnerqkvag dlhkaqqsle
     1021 liqskivkaa gdttviensd vspetessek etmsvslnqt vtqlqqllqa vnqqltkeke
     1081 hyqvle
//
LOCUS       NP_001427457             287 aa            linear   PRI 21-NOV-2025
DEFINITION  syntaxin-3 isoform 4 [Homo sapiens].
ACCESSION   NP_001427457
VERSION     NP_001427457.1
DBSOURCE    REFSEQ: accession NM_001440528.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Shinozuka,T., Kanda,M., Sato,Y., Shimizu,D., Tanaka,C., Umeda,S.,
            Inokawa,Y., Hattori,N., Hayashi,M., Nakayama,G. and Kodera,Y.
  TITLE     Increased STX3 transcript and protein levels were associated with
            poor prognosis in two independent cohorts of esophageal squamous
            cell carcinoma patients
  JOURNAL   Cancer Med 12 (24), 22185-22195 (2023)
   PUBMED   38014487
  REMARK    GeneRIF: Increased STX3 transcript and protein levels were
            associated with poor prognosis in two independent cohorts of
            esophageal squamous cell carcinoma patients.
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Janecke,A.R., Liu,X., Adam,R., Punuru,S., Viestenz,A., Strauss,V.,
            Laass,M., Sanchez,E., Adachi,R., Schatz,M.P., Saboo,U.S.,
            Mittal,N., Rohrschneider,K., Escher,J., Ganesh,A., Al Zuhaibi,S.,
            Al Murshedi,F., AlSaleem,B., Alfadhel,M., Al Sinani,S.,
            Alkuraya,F.S., Huber,L.A., Muller,T., Heidelberger,R. and Janz,R.
  TITLE     Pathogenic STX3 variants affecting the retinal and intestinal
            transcripts cause an early-onset severe retinal dystrophy in
            microvillus inclusion disease subjects
  JOURNAL   Hum Genet 140 (8), 1143-1156 (2021)
   PUBMED   33974130
  REMARK    GeneRIF: Pathogenic STX3 variants affecting the retinal and
            intestinal transcripts cause an early-onset severe retinal
            dystrophy in microvillus inclusion disease subjects.
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Low,S.H., Vasanji,A., Nanduri,J., He,M., Sharma,N., Koo,M.,
            Drazba,J. and Weimbs,T.
  TITLE     Syntaxins 3 and 4 are concentrated in separate clusters on the
            plasma membrane before the establishment of cell polarity
  JOURNAL   Mol Biol Cell 17 (2), 977-989 (2006)
   PUBMED   16339081
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Martin-Martin,B., Nabokina,S.M., Lazo,P.A. and Mollinedo,F.
  TITLE     Co-expression of several human syntaxin genes in neutrophils and
            differentiating HL-60 cells: variant isoforms and detection of
            syntaxin 1
  JOURNAL   J Leukoc Biol 65 (3), 397-406 (1999)
   PUBMED   10080545
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Steegmaier,M., Yang,B., Yoo,J.S., Huang,B., Shen,M., Yu,S., Luo,Y.
            and Scheller,R.H.
  TITLE     Three novel proteins of the syntaxin/SNAP-25 family
  JOURNAL   J Biol Chem 273 (51), 34171-34179 (1998)
   PUBMED   9852078
REFERENCE   8  (residues 1 to 287)
  AUTHORS   Riento,K., Galli,T., Jansson,S., Ehnholm,C., Lehtonen,E. and
            Olkkonen,V.M.
  TITLE     Interaction of Munc-18-2 with syntaxin 3 controls the association
            of apical SNAREs in epithelial cells
  JOURNAL   J Cell Sci 111 (Pt 17), 2681-2688 (1998)
   PUBMED   9701566
REFERENCE   9  (residues 1 to 287)
  AUTHORS   Galli,T., Zahraoui,A., Vaidyanathan,V.V., Raposo,G., Tian,J.M.,
            Karin,M., Niemann,H. and Louvard,D.
  TITLE     A novel tetanus neurotoxin-insensitive vesicle-associated membrane
            protein in SNARE complexes of the apical plasma membrane of
            epithelial cells
  JOURNAL   Mol Biol Cell 9 (6), 1437-1448 (1998)
   PUBMED   9614185
REFERENCE   10 (residues 1 to 287)
  AUTHORS   Delgrossi,M.H., Breuza,L., Mirre,C., Chavrier,P. and Le Bivic,A.
  TITLE     Human syntaxin 3 is localized apically in human intestinal cells
  JOURNAL   J Cell Sci 110 (Pt 18), 2207-2214 (1997)
   PUBMED   9378770
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000640.5.
            
            Summary: The gene is a member of the syntaxin family. The encoded
            protein is targeted to the apical membrane of epithelial cells
            where it forms clusters and is important in establishing and
            maintaining polarity necessary for protein trafficking involving
            vesicle fusion and exocytosis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4175852.1,
                                           ERR4352443.206042.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155984 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..287
                     /product="syntaxin-3 isoform 4"
                     /note="syntaxin 3A; syntaxin 3B"
                     /calculated_mol_wt=32768
     Region          32..224
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     Region          192..258
                     /region_name="SNARE"
                     /note="SNARE motif; cl22856"
                     /db_xref="CDD:473982"
     Site            order(220,227,230)
                     /site_type="other"
                     /note="flanking leucine-zipper layers"
                     /db_xref="CDD:277192"
     Site            223
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277192"
     Site            262..282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13277.3)"
     CDS             1..287
                     /gene="STX3"
                     /gene_synonym="DIAR12; MVID2; RDMVID; STX3A"
                     /coded_by="NM_001440528.1:231..1094"
                     /note="isoform 4 is encoded by transcript variant 9"
                     /db_xref="GeneID:6809"
                     /db_xref="HGNC:HGNC:11438"
                     /db_xref="MIM:600876"
ORIGIN      
        1 mkdrleqlka ltqdddtdav eiaidntafm deffseieet rlnidkiseh veeakklysi
       61 ilsapipepk tkddleqltt eikkrannvr nklksmekhi eedevrssad lrirksqhsv
      121 lsrkfvevmt kyneaqvdfr erskgriqrq leitgkkttd eeleemlesg npaiftsgii
      181 dsqiskqals eiegrhkdiv rlessikelh dmfmdiamlv enqgemldni elnvmhtvdh
      241 vekardetkk avkyqsqark kliiiivlvv vllgilalii glsvgln
//
LOCUS       NP_001424218            1053 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            beta isoform isoform 3 [Homo sapiens].
ACCESSION   NP_001424218 XP_047304267 XP_054202829
VERSION     NP_001424218.1
DBSOURCE    REFSEQ: accession NM_001437289.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Liu,L., Feng,X., Fan,C., Kong,D., Feng,X., Sun,C., Xu,Y., Li,B.,
            Jiang,Y. and Zheng,C.
  TITLE     PDCD4 interacting with PIK3CB and CTSZ promotes the apoptosis of
            multiple myeloma cells
  JOURNAL   FASEB J 38 (16), e70024 (2024)
   PUBMED   39190024
  REMARK    GeneRIF: PDCD4 interacting with PIK3CB and CTSZ promotes the
            apoptosis of multiple myeloma cells.
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Liu,G., Hou,Y., Jin,X., Zhang,Y., Sun,C., Huang,C., Ren,Y., Gao,J.,
            Wang,X. and Jiang,X.
  TITLE     PI3K/HSCB axis facilitates FOG1 nuclear translocation to promote
            erythropoiesis and megakaryopoiesis
  JOURNAL   Elife 13, 95815 (2024)
   PUBMED   38757931
  REMARK    GeneRIF: PI3K/HSCB axis facilitates FOG1 nuclear translocation to
            promote erythropoiesis and megakaryopoiesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1053)
  AUTHORS   Duewell,B.R., Wilson,N.E., Bailey,G.M., Peabody,S.E. and
            Hansen,S.D.
  TITLE     Molecular dissection of PI3Kbeta synergistic activation by receptor
            tyrosine kinases, GbetaGgamma, and Rho-family GTPases
  JOURNAL   Elife 12, 88991 (2024)
   PUBMED   38713746
  REMARK    GeneRIF: Molecular dissection of PI3Kbeta synergistic activation by
            receptor tyrosine kinases, GbetaGgamma, and Rho-family GTPases.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1053)
  AUTHORS   Xu,W., Chen,Y., Zhang,Z., Jiang,Y. and Wang,Z.
  TITLE     Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma
  JOURNAL   Med Oncol 40 (8), 221 (2023)
   PUBMED   37402056
  REMARK    GeneRIF: Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1053)
  AUTHORS   Milani,D., Mazzoni,M., Borgatti,P., Zauli,G., Cantley,L. and
            Capitani,S.
  TITLE     Extracellular human immunodeficiency virus type-1 Tat protein
            activates phosphatidylinositol 3-kinase in PC12 neuronal cells
  JOURNAL   J Biol Chem 271 (38), 22961-22964 (1996)
   PUBMED   8798481
REFERENCE   7  (residues 1 to 1053)
  AUTHORS   Bonnefoy-Berard,N., Liu,Y.C., von Willebrand,M., Sung,A., Elly,C.,
            Mustelin,T., Yoshida,H., Ishizaka,K. and Altman,A.
  TITLE     Inhibition of phosphatidylinositol 3-kinase activity by association
            with 14-3-3 proteins in T cells
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10142-10146 (1995)
   PUBMED   7479742
REFERENCE   8  (residues 1 to 1053)
  AUTHORS   Hu,P. and Schlessinger,J.
  TITLE     Direct association of p110 beta phosphatidylinositol 3-kinase with
            p85 is mediated by an N-terminal fragment of p110 beta
  JOURNAL   Mol Cell Biol 14 (4), 2577-2583 (1994)
   PUBMED   8139559
REFERENCE   9  (residues 1 to 1053)
  AUTHORS   Hu,P., Mondino,A., Skolnik,E.Y. and Schlessinger,J.
  TITLE     Cloning of a novel, ubiquitously expressed human
            phosphatidylinositol 3-kinase and identification of its binding
            site on p85
  JOURNAL   Mol Cell Biol 13 (12), 7677-7688 (1993)
   PUBMED   8246984
REFERENCE   10 (residues 1 to 1053)
  AUTHORS   Carpenter,C.L., Duckworth,B.C., Auger,K.R., Cohen,B.,
            Schaffhausen,B.S. and Cantley,L.C.
  TITLE     Purification and characterization of phosphoinositide 3-kinase from
            rat liver
  JOURNAL   J Biol Chem 265 (32), 19704-19711 (1990)
   PUBMED   2174051
  REMARK    GeneRIF: This paper reports the first purification of a
            phosphoinositide 3-kinase and shows that the protein is a
            heterodimer of an 85 kd regulatory subunit that mediates binding to
            phosphorylated proteins and a 110 kd catalytic subunit.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC067728.25, AC117389.5 and AC020890.22.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_047304267.1, XP_054202829.1.
            
            Summary: This gene encodes an isoform of the catalytic subunit of
            phosphoinositide 3-kinase (PI3K). These kinases are important in
            signaling pathways involving receptors on the outer membrane of
            eukaryotic cells and are named for their catalytic subunit. The
            encoded protein is the catalytic subunit for PI3Kbeta (PI3KB).
            PI3KB has been shown to be part of the activation pathway in
            neutrophils which have bound immune complexes at sites of injury or
            infection. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.269331.1,
                                           SRR14038196.1991134.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..1053
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit beta isoform isoform 3"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.1.153"
                     /note="PI3-kinase p110 subunit beta; PtdIns-3-kinase p110;
                     PI3K-beta; PI3-kinase subunit beta; ptdIns-3-kinase
                     subunit beta; ptdIns-3-kinase subunit p110-beta;
                     phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa
                     catalytic subunit beta; serine/threonine protein kinase
                     PIK3CB; phosphoinositide-3-kinase, catalytic, beta
                     polypeptide"
                     /calculated_mol_wt=120945
     Region          41..118
                     /region_name="PI3K_p85B"
                     /note="PI3-kinase family, p85-binding domain; smart00143"
                     /db_xref="CDD:197539"
     Region          180..288
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, Ras-binding domain; smart00144"
                     /db_xref="CDD:197540"
     Region          324..501
                     /region_name="C2_PI3K_class_I_beta_delta"
                     /note="C2 domain present in class I beta and delta
                     phosphatidylinositol 3-kinases (PI3Ks); cd08693"
                     /db_xref="CDD:176075"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI9; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     Region          410..418
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Region          515..685
                     /region_name="PI3Ka_I"
                     /note="Phosphoinositide 3-kinase (PI3K) class I, accessory
                     domain; PIK domain is conserved in all PI3 and
                     PI4-kinases. Its role is unclear but it has been suggested
                     to be involved in substrate presentation. In general, PI3K
                     class I prefer phosphoinositol (4,5)...; cd00872"
                     /db_xref="CDD:238444"
     Region          689..1050
                     /region_name="PI3Kc_IA_beta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase beta; cd05173"
                     /db_xref="CDD:270717"
     Region          761..767
                     /region_name="G-loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(762,764..766,768,786,788,791,822,834..837,842,845,
                     907,909,919..920)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270717"
     Site            order(829..830,857..858,861,931..932,945,948,956..959,962,
                     1029,1032..1033,1035..1036)
                     /site_type="other"
                     /note="regulatory subunit interface [polypeptide binding]"
                     /db_xref="CDD:270717"
     Site            876
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270717"
     Region          899..907
                     /region_name="Catalytic loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            899..907
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270717"
     Region          918..944
                     /region_name="Activation loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(920..933,939..944)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270717"
     Site            1053
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12502714; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     CDS             1..1053
                     /gene="PIK3CB"
                     /gene_synonym="P110BETA; PI3K; PI3KBETA; PIK3C1"
                     /coded_by="NM_001437289.1:356..3517"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:5291"
                     /db_xref="HGNC:HGNC:8976"
                     /db_xref="MIM:602925"
ORIGIN      
        1 mcfsfimppa madildiwav dsqiasdgsi pvdfllptgi yiqlevprea tisyikqmlw
       61 kqvhnypmfn llmdidsymf acvnqtavye eledetrrlc dvrpflpvlk lvtrscdpge
      121 kldskigvli gkglhefdsl kdpevnefrr kmrkfseeki lslvglswmd wlkqtyppeh
      181 epsipenled klyggkliva vhfencqdvf sfqvspnmnp ikvnelaiqk rltihgkede
      241 vspydyvlqv sgrveyvfgd hpliqfqyir ncvmnralph filvecckik kmyeqemiai
      301 eaainrnssn lplplppkkt riishvwenn npfqivlvkg nklnteetvk vhvraglfhg
      361 tellcktivs sevsgkndhi wneplefdin icdlprmarl cfavyavldk vktkkstkti
      421 npskyqtirk agkvhypvaw vntmvfdfkg qlrtgdiilh swssfpdele emlnpmgtvq
      481 tnpytenata lhvkfpenkk qpyyyppfdk srggkkflpv lkeildrdpl sqlcenemdl
      541 iwtlrqdcre ifpqslpkll lsikwnkled vaqlqallqi wpklppreal elldfnypdq
      601 yvreyavgcl rqmsdeelsq yllqlvqvlk yepfldcals rflleralgn rrigqflfwh
      661 lrsevhipav svqfgvilea ycrgsvghmk vlskqvealn klktlnslik lnavklnrak
      721 gkeamhtclk qsayrealsd lqsplnpcvi lselyvekck ymdskmkplw lvynnkvfge
      781 dsvgvifkng ddlrqdmltl qmlrlmdllw keagldlrml pygclatgdr sglievvsts
      841 etiadiqlns snvaaaaafn kdallnwlke ynsgddldra ieeftlscag ycvasyvlgi
      901 gdrhsdnimv kktgqlfhid fghilgnfks kfgikrervp filtydfihv iqqgktgnte
      961 kfgrfrqcce daylilrrhg nlfitlfalm ltaglpelts vkdiqylkds lalgkseeea
     1021 lkqfkqkfde alreswttkv nwmahtvrkd yrs
//
LOCUS       NP_001389627            1298 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 10 [Homo sapiens].
ACCESSION   NP_001389627 XP_006720204
VERSION     NP_001389627.1
DBSOURCE    REFSEQ: accession NM_001402698.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1298)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1298)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1298)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1298)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1298)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1298)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1298)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1298)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1298)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1298)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            On Apr 22, 2022 this sequence version replaced XP_006720204.1.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.24249.1,
                                           SRR14372080.2140186.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1298
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1298
                     /product="kinectin isoform 10"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=149349
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          <326..>584
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          480..1251
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1298
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402698.1:179..4075"
                     /note="isoform 10 is encoded by transcript variant 21"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqdlkqeika
      841 lkeeignvql ekaqqlsits kvqelqnllk gkeeqmntmk avleekekdl antgkwlqdl
      901 qeeneslkah vqevaqhnlk eassasqfee leivlkeken elkrleamlk eresdlsskt
      961 qllqdvqden klfksqieql kqqnyqqass fppheellkv iserekeisg lwneldslkd
     1021 avehqrkknn sygewlhgfe kkakecmagt sgseevkvle hklkeademh tllqleceky
     1081 ksvlaetegi lqklqrsveq eenkwkvkvd eshktikqmq ssftsseqel erlrsenkdi
     1141 enlrrerehl emelekaeme rstyvtevre lkdlltelqk klddsyseav rqneelnllk
     1201 aqlnetltkl rteqnerqkv agdlhkaqqs leliqskivk aagdttvien sdvspetess
     1261 eketmsvsln qtvtqlqqll qavnqqltke kehyqvle
//
LOCUS       NP_001428151             476 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 2 [Homo sapiens].
ACCESSION   NP_001428151
VERSION     NP_001428151.1
DBSOURCE    REFSEQ: accession NM_001441222.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2141007.1,
                                           SRR14038194.3755757.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..476
                     /product="calcium uptake protein 1, mitochondrial isoform
                     2"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=50585
     transit_peptide 1..33
                     /note="Mitochondrion. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:26387864; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
                     /calculated_mol_wt=3784
     mat_peptide     34..476
                     /product="Calcium uptake protein 1, mitochondrial.
                     /id=PRO_0000322990"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
                     /calculated_mol_wt=50585
     Region          68..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          99..110
                     /region_name="Polybasic region.
                     /evidence=ECO:0000269|PubMed:27099988"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCX5; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          126..129
                     /region_name="K/R-ring.
                     /evidence=ECO:0000269|PubMed:32494073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          222..441
                     /region_name="EFh_MICU1"
                     /note="EF-hand, calcium binding motif, found in calcium
                     uptake protein 1, mitochondrial (MICU1) and similar
                     proteins; cd16173"
                     /db_xref="CDD:320081"
     Region          222..251
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Site            order(224,376,379,382..383,385,403)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:320081"
     Site            order(231,233,235,242,421,423,425,432)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320081"
     Region          259..263
                     /region_name="K/R-ring.
                     /evidence=ECO:0000269|PubMed:32494073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          277..307
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          375..404
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          412..441
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          455..465
                     /region_name="C-helix region.
                     /evidence=ECO:0000269|PubMed:24514027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Site            455
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:27642082; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
     CDS             1..476
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001441222.1:166..1596"
                     /note="isoform 2 is encoded by transcript variant 9"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mfrlnslsal aelavgsrwy hggsqpiqir rrlmmvaflg asavtastgl lwkrahaesp
       61 pcvdnlksdi gdkgknkdeg dvcnhekkta dlaphpeekk kkrsgfrdrk vmeyenrira
      121 ystpdkifry fatlkvisep geaevfmtpe dfvrsitpne kqpehlgldq yiikrfdgkk
      181 isqerekfad egsifytlge cglisfsdyi flttvlstpq rnfeiafkmf dlngdgevdm
      241 eefeqvqsii rsqtsmgmrh rdrpttgntl ksglcsaltt yffgadlkgk ltiknflefq
      301 rklqhdvlkl eferhdpvdg riterqfggm llaysgvqsk kltamqrqlk khfkegkglt
      361 fqevenfftf lknindvdta lsfyhmagas ldkvtmqqva rtvakvelsd hvcdvvfalf
      421 dcdgngelsn kefvsimkqr lmrglekpkd mgftrlmqam wkcaqetawd falpkq
//
LOCUS       NP_001427917             555 aa            linear   PRI 21-NOV-2025
DEFINITION  complement factor I isoform 11 precursor [Homo sapiens].
ACCESSION   NP_001427917 XP_011530222 XP_054205915
VERSION     NP_001427917.1
DBSOURCE    REFSEQ: accession NM_001440988.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Moreno,R. and Broderick,L.
  TITLE     Complement factor I deficiency: Diverse phenotypes
  JOURNAL   J Allergy Clin Immunol 156 (2), 305-307 (2025)
   PUBMED   40127737
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Schwotzer,N., Fakhouri,F., Martins,P.V., Delmas,Y., Caillard,S.,
            Zuber,J., Moranne,O., Mesnard,L., Fremeaux-Bacchi,V. and
            El-Sissy,C.
  TITLE     Hot Spot of Complement Factor I Rare Variant p.Ile357Met in
            Patients With Hemolytic Uremic Syndrome
  JOURNAL   Am J Kidney Dis 84 (2), 244-249 (2024)
   PUBMED   38423159
  REMARK    GeneRIF: Hot Spot of Complement Factor I Rare Variant p.Ile357Met
            in Patients With Hemolytic Uremic Syndrome.
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Felberg,A., Bienkowski,M., Stokowy,T., Myszczynski,K.,
            Polakiewicz,Z., Kitowska,K., Sadej,R., Mohlin,F., Kuzniewska,A.,
            Kowalska,D., Stasilojc,G., Jongerius,I., Spaapen,R.,
            Mesa-Guzman,M., Montuenga,L.M., Blom,A.M., Pio,R. and Okroj,M.
  TITLE     Elevated expression of complement factor I in lung cancer cells
            associates with shorter survival-Potentially via non-canonical
            mechanism
  JOURNAL   Transl Res 269, 1-13 (2024)
   PUBMED   38395390
  REMARK    GeneRIF: Elevated expression of complement factor I in lung cancer
            cells associates with shorter survival-Potentially via
            non-canonical mechanism.
REFERENCE   4  (residues 1 to 555)
  AUTHORS   Massey,V., Nguyen,C.E., Francois,T., De Bruycker,J.J., Bonnefoy,A.,
            Lapeyraque,A.L. and Decaluwe,H.
  TITLE     CNS Inflammation as the First Sign of Complement Factor I
            Deficiency: A Severe Myelitis Treated With Intense Immunotherapy
            and Eculizumab
  JOURNAL   Neurol Neuroimmunol Neuroinflamm 11 (2), e200191 (2024)
   PUBMED   38134378
  REMARK    GeneRIF: CNS Inflammation as the First Sign of Complement Factor I
            Deficiency.
REFERENCE   5  (residues 1 to 555)
  AUTHORS   van de Ven,J.P., Nilsson,S.C., Tan,P.L., Buitendijk,G.H.,
            Ristau,T., Mohlin,F.C., Nabuurs,S.B., Schoenmaker-Koller,F.E.,
            Smailhodzic,D., Campochiaro,P.A., Zack,D.J., Duvvari,M.R.,
            Bakker,B., Paun,C.C., Boon,C.J., Uitterlinden,A.G., Liakopoulos,S.,
            Klevering,B.J., Fauser,S., Daha,M.R., Katsanis,N., Klaver,C.C.,
            Blom,A.M., Hoyng,C.B. and den Hollander,A.I.
  TITLE     A functional variant in the CFI gene confers a high risk of
            age-related macular degeneration
  JOURNAL   Nat Genet 45 (7), 813-817 (2013)
   PUBMED   23685748
  REMARK    GeneRIF: these findings demonstrate that rare, highly penetrant
            mutations in CFI contribute to the genetic burden of age-related
            macular degeneration.
REFERENCE   6  (residues 1 to 555)
  AUTHORS   Martin,B. and Smith,R.J.H.
  TITLE     C3 Glomerulopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301598
REFERENCE   7  (residues 1 to 555)
  AUTHORS   Noris,M., Bresin,E., Mele,C. and Remuzzi,G.
  TITLE     Genetic Atypical Hemolytic-Uremic Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301541
REFERENCE   8  (residues 1 to 555)
  AUTHORS   DiScipio,R.G.
  TITLE     Ultrastructures and interactions of complement factors H and I
  JOURNAL   J Immunol 149 (8), 2592-2599 (1992)
   PUBMED   1401896
REFERENCE   9  (residues 1 to 555)
  AUTHORS   Shiang,R., Murray,J.C., Morton,C.C., Buetow,K.H., Wasmuth,J.J.,
            Olney,A.H., Sanger,W.G. and Goldberger,G.
  TITLE     Mapping of the human complement factor I gene to 4q25
  JOURNAL   Genomics 4 (1), 82-86 (1989)
   PUBMED   2563353
REFERENCE   10 (residues 1 to 555)
  AUTHORS   Catterall,C.F., Lyons,A., Sim,R.B., Day,A.J. and Harris,T.J.
  TITLE     Characterization of primary amino acid sequence of human complement
            control protein factor I from an analysis of cDNA clones
  JOURNAL   Biochem J 242 (3), 849-856 (1987)
   PUBMED   2954545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC126283.3 and AC004067.1.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_011530222.1, XP_054205915.1.
            
            Summary: This gene encodes a serine proteinase that is essential
            for regulating the complement cascade. The encoded preproprotein is
            cleaved to produce both heavy and light chains, which are linked by
            disulfide bonds to form a heterodimeric glycoprotein. This
            heterodimer can cleave and inactivate the complement components C4b
            and C3b, and it prevents the assembly of the C3 and C5 convertase
            enzymes. Defects in this gene cause complement factor I deficiency,
            an autosomal recessive disease associated with a susceptibility to
            pyogenic infections. Mutations in this gene have been associated
            with a predisposition to atypical hemolytic uremic syndrome, a
            disease characterized by acute renal failure, microangiopathic
            hemolytic anemia and thrombocytopenia. Primary glomerulonephritis
            with immune deposits and age-related macular degeneration are other
            conditions associated with mutations of this gene. [provided by
            RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2674245.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..555
                     /product="complement factor I isoform 11 precursor"
                     /EC_number="3.4.21.45"
                     /note="C3b-inactivator; Konglutinogen-activating factor;
                     complement factor I heavy chain; complement component I;
                     C3B/C4B inactivator; complement control protein factor I;
                     light chain of factor I"
                     /calculated_mol_wt=60427
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2281
     Region          43..108
                     /region_name="FIMAC"
                     /note="factor I membrane attack complex; smart00057"
                     /db_xref="CDD:214493"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Region          114..215
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     Region          224..256
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(227,235,246..247)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(239,242,246,252..253)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            249..253
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          257..293
                     /region_name="Ldl_recept_a"
                     /note="Low-density lipoprotein receptor domain class A;
                     pfam00057"
                     /db_xref="CDD:395011"
     Site            order(264,272,283..284)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(276,279,283,289..290)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            286..290
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          347..>519
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; smart00020"
                     /db_xref="CDD:214473"
     Site            348
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            472
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Site            502
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     CDS             1..555
                     /gene="CFI"
                     /gene_synonym="AHUS3; ARMD13; C3b-INA; C3BINA; FI; IF;
                     KAF"
                     /coded_by="NM_001440988.1:29..1696"
                     /note="isoform 11 precursor is encoded by transcript
                     variant 16"
                     /db_xref="GeneID:3426"
                     /db_xref="HGNC:HGNC:5394"
                     /db_xref="MIM:217030"
ORIGIN      
        1 mkllhvfllf lcfhlrfckv tytsqedlve kkclakkyth lscdkvfcqp wqrciegtcv
       61 cklpyqcpkn gtavcatnrr sfptycqqks leclhpgtkf lnngtctaeg kfsvslkhgn
      121 tdsegivevk lvdqdktmfi cksswsmrea nvacldlgfq qgadtqrrfk lsdlsinste
      181 clhvhcrgle tslaectftk rrtmgyqdfa dvvcytqkad spmddffqcv ngkyisqmka
      241 cdgindcgdq sdelcckacq gkgfhcksgv cipsqyqcng evdcitgede vgcaaarhpt
      301 iqgfasvtqe eteiltadmd aerrriksll pklscgvknr mhirrkrivg gkraqlgdlp
      361 wqvaikdasg itcggiyigg cwiltaahcl raskthryqi wttvvdwihp dlkrivieyv
      421 driifhenyn agtyqndial iemkkdgnkk dcelprsipa cvpwspylfq pndtcivsgw
      481 grekdnervf slqwgevkli sncskfygnr fyekemecae srsvpqagvq wcnlsslqhp
      541 stswvqvill ppppe
//
LOCUS       NP_001425419             764 aa            linear   PRI 21-NOV-2025
DEFINITION  AT-rich interactive domain-containing protein 1B isoform 12 [Homo
            sapiens].
ACCESSION   NP_001425419
VERSION     NP_001425419.1
DBSOURCE    REFSEQ: accession NM_001438490.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Bosch,E., Guse,E., Kirchner,P., Winterpacht,A., Walther,M.,
            Alders,M., Kerkhof,J., Ekici,A.B., Sticht,H., Sadikovic,B., Reis,A.
            and Vasileiou,G.
  TITLE     The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation
  JOURNAL   Hum Genet 143 (8), 965-978 (2024)
   PUBMED   39028335
  REMARK    GeneRIF: The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation.
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Huang,X., Li,H., Yang,S., Ma,M., Lian,Y., Wu,X., Qi,X., Wang,X.,
            Rong,W. and Sheng,X.
  TITLE     De novo variation in ARID1B gene causes Coffin-Siris syndrome 1 in
            a Chinese family with excessive early-onset high myopia
  JOURNAL   BMC Med Genomics 17 (1), 142 (2024)
   PUBMED   38790056
  REMARK    GeneRIF: De novo variation in ARID1B gene causes Coffin-Siris
            syndrome 1 in a Chinese family with excessive early-onset high
            myopia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Hurlstone,A.F., Olave,I.A., Barker,N., van Noort,M. and Clevers,H.
  TITLE     Cloning and characterization of hELD/OSA1, a novel BRG1 interacting
            protein
  JOURNAL   Biochem J 364 (Pt 1), 255-264 (2002)
   PUBMED   11988099
  REMARK    GeneRIF: Cloning and characterization of hELD/OSA1, a novel BRG1
            interacting protein.
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Phelan,M.L., Sif,S., Narlikar,G.J. and Kingston,R.E.
  TITLE     Reconstitution of a core chromatin remodeling complex from SWI/SNF
            subunits
  JOURNAL   Mol Cell 3 (2), 247-253 (1999)
   PUBMED   10078207
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Imbert,G., Saudou,F., Yvert,G., Devys,D., Trottier,Y.,
            Garnier,J.M., Weber,C., Mandel,J.L., Cancel,G., Abbas,N., Durr,A.,
            Didierjean,O., Stevanin,G., Agid,Y. and Brice,A.
  TITLE     Cloning of the gene for spinocerebellar ataxia 2 reveals a locus
            with high sensitivity to expanded CAG/glutamine repeats
  JOURNAL   Nat Genet 14 (3), 285-291 (1996)
   PUBMED   8896557
REFERENCE   7  (residues 1 to 764)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
REFERENCE   8  (residues 1 to 764)
  AUTHORS   Vergano,S.A., van der Sluijs,P.J. and Santen,G.
  TITLE     ARID1B-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31132234
REFERENCE   9  (residues 1 to 764)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
REFERENCE   10 (residues 1 to 764)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355297.20, AL162578.13,
            AL049820.23 and KF458335.1.
            
            Summary: This locus encodes an AT-rich DNA interacting
            domain-containing protein. The encoded protein is a component of
            the SWI/SNF chromatin remodeling complex and may play a role in
            cell-cycle activation. The protein encoded by this locus is similar
            to AT-rich interactive domain-containing protein 1A. These two
            proteins function as alternative, mutually exclusive ARID-subunits
            of the SWI/SNF complex. The associated complexes play opposing
            roles. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3322821.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146982, SAMEA2147596
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..764
                     /product="AT-rich interactive domain-containing protein 1B
                     isoform 12"
                     /note="BRG1-binding protein ELD/OSA1; ELD (eyelid)/OSA
                     protein; BRG1-associated factor 250b; ARID
                     domain-containing protein 1B; AT rich interactive domain
                     1B (SWI1-like)"
                     /calculated_mol_wt=74946
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          155..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          321..414
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          487..546
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            487
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4N7; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          502..506
                     /region_name="LXXLL"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            608
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4N7; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            640
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     CDS             1..764
                     /gene="ARID1B"
                     /gene_synonym="6A3-5; BAF250B; BRIGHT; CSS1; DAN15;
                     ELD/OSA1; MRD12; OSA2; P250R; SMARCF2"
                     /coded_by="NM_001438490.1:304..2598"
                     /note="isoform 12 is encoded by transcript variant 13"
                     /db_xref="GeneID:57492"
                     /db_xref="HGNC:HGNC:18040"
                     /db_xref="MIM:614556"
ORIGIN      
        1 maaraaaaaa aaaararara gsgerrappg prpapgardl eagargaaaa aaapgpmlgg
       61 ggdgggglns vhhhpllprh elnmahnaga aaaagthsak sggseaalke ggsaaalsss
      121 ssssaaaaaa ssssssgpgs ametgllpnh klktvgeapa apphqqhhhh hhahhhhhha
      181 hhlhhhhalq qqlnqfqqqq qqqqqqqqqq qqqqhpisnn nslggaggga pqpgpdmeqp
      241 qhggakdsaa ggqadppgpp llskpgdedd appkmgepag gryehpglga lgtqqppvav
      301 pgggggpaav pefnnyygsa apasggpggr agpcfdqhgg qqspgmgmmh sasaaaagap
      361 gsmdplqnsh egypnsqcnh ypgysrpgag gggggggggg ggsggggggg gagaggagag
      421 avaaaaaaaa aaaggggggg yggssagygv lssprqqggg mmmgpgggga aslskaaags
      481 aaggfqrfag qnqhpsgatp tlnqlltsps pmmrsyggsy peysspsapp pppsqpqsqa
      541 aaagaaaggq qaaagmglgk dmgaqyaaas pawaaaqqrs hpamspgtpg ptmgrsqgsp
      601 mdpmvmkrpq lygmgsnphs qpqqsspypg gsygppgpqr ypigiqgrtp gamagmqypq
      661 qqmppqygqq gvsgycqqgq qpyysqqpqp phlppqaqyl psqsqqryqp qqdmsqegyg
      721 trsqpplapg kpnhedlnli qqerpsslpv evlasedaaf glkf
//
LOCUS       NP_001400008             320 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001400008
VERSION     NP_001400008.1
DBSOURCE    REFSEQ: accession NM_001413079.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 320)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 320)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 320)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.812060.1,
                                           SRR14372079.109974.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..320
                     /product="mitochondrial fission regulator 1 isoform 5"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=35191
     Region          45..238
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     CDS             1..320
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001413079.1:307..1269"
                     /note="isoform 5 is encoded by transcript variant 14"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mpykllsvig fkisinyrih clgndsvktk scsrtgpcwe psinshatew spshpgedav
       61 asfadvgwva keegecsarl rtevrsrppl qddllffeka psrqislpdl sqeepqlktp
      121 alaneealqk icalenelaa lraqiakivt qqeqqnltag dldsttfgti pphppppppp
      181 lpppalglhq stsavdlike rrekranagk tlvknnpkkp empnmleilk emnsvklrsv
      241 krseqdvkpk pvdatdpaal iaealkkkfa yryrsdsqde vekgipkses eatservlfg
      301 phmlkptgkm kalienvsds
//
LOCUS       NP_001425343            1412 aa            linear   PRI 21-NOV-2025
DEFINITION  GTPase-activating protein and VPS9 domain-containing protein 1
            isoform 5 [Homo sapiens].
ACCESSION   NP_001425343 XP_047279162 XP_054218669
VERSION     NP_001425343.1
DBSOURCE    REFSEQ: accession NM_001438414.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1412)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1412)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1412)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1412)
  AUTHORS   Khademi,B., Khorrami,M., Ayromlou,H., Rikhtegar,R., Moghadam,E.A.,
            Tahmasebivand,M., Mousavi,S.R., Kheirollahi,M., Fakhr,F.,
            Alizadeh-Ghodsi,M. and Emamalizadeh,B.
  TITLE     An interdependence between GAPVD1 gene polymorphism, expression
            level and response to interferon beta in patients with multiple
            sclerosis
  JOURNAL   J Neuroimmunol 353, 577507 (2021)
   PUBMED   33548618
  REMARK    GeneRIF: An interdependence between GAPVD1 gene polymorphism,
            expression level and response to interferon beta in patients with
            multiple sclerosis.
REFERENCE   5  (residues 1 to 1412)
  AUTHORS   Ibrahim,H., Reus,P., Mundorf,A.K., Grothoff,A.L., Rudenko,V.,
            Buschhaus,C., Stefanski,A., Berleth,N., Stork,B., Stuhler,K.,
            Kalfalah,F. and Reinke,H.
  TITLE     Phosphorylation of GAPVD1 Is Regulated by the PER Complex and
            Linked to GAPVD1 Degradation
  JOURNAL   Int J Mol Sci 22 (7), 3787 (2021)
   PUBMED   33917494
  REMARK    GeneRIF: Phosphorylation of GAPVD1 Is Regulated by the PER Complex
            and Linked to GAPVD1 Degradation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1412)
  AUTHORS   Kim,H., Oh,H., Oh,Y.S., Bae,J., Hong,N.H., Park,S.J., Ahn,S.,
            Lee,M., Rhee,S., Lee,S.H., Jun,Y., Kim,S.H., Huh,Y.H. and Song,W.K.
  TITLE     SPIN90, an adaptor protein, alters the proximity between Rab5 and
            Gapex5 and facilitates Rab5 activation during EGF endocytosis
  JOURNAL   Exp Mol Med 51 (7), 1-14 (2019)
   PUBMED   31358736
  REMARK    GeneRIF: The findings suggest that SPIN90, as an adaptor protein,
            simultaneously binds inactive Rab5 and Gapex5, thereby altering
            their spatial proximity and facilitating Rab5 activation.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1412)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1412)
  AUTHORS   Su,X., Kong,C. and Stahl,P.D.
  TITLE     GAPex-5 mediates ubiquitination, trafficking, and degradation of
            epidermal growth factor receptor
  JOURNAL   J Biol Chem 282 (29), 21278-21284 (2007)
   PUBMED   17545148
  REMARK    GeneRIF: EGF-stimulated receptor ubiquitination and trafficking are
            mediated via GAPex-5: GAPex-5-mediated EGFR ubiquitination is
            independent of Rab5 activation
REFERENCE   9  (residues 1 to 1412)
  AUTHORS   Hunker,C.M., Galvis,A., Kruk,I., Giambini,H., Veisaga,M.L. and
            Barbieri,M.A.
  TITLE     Rab5-activating protein 6, a novel endosomal protein with a role in
            endocytosis
  JOURNAL   Biochem Biophys Res Commun 340 (3), 967-975 (2006)
   PUBMED   16410077
REFERENCE   10 (residues 1 to 1412)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL354710.17 and AL627223.23.
            
            On or before Apr 18, 2025 this sequence version replaced
            XP_047279162.1, XP_054218669.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1875556.1,
                                           SRR14038196.484690.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1412
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..1412
                     /product="GTPase-activating protein and VPS9
                     domain-containing protein 1 isoform 5"
                     /note="GTPase-activating protein and VPS9
                     domain-containing protein 1; Rab5-activating protein 6;
                     Rab5 exchange factor"
                     /calculated_mol_wt=157333
     Region          84..449
                     /region_name="RasGAP_RAP6"
                     /note="Ras-GTPase Activating Domain of Rab5-activating
                     protein 6; cd05129"
                     /db_xref="CDD:213331"
     Site            order(129,168,170,172..173,179,182,186,304,312..313,
                     316..317,320,342,345..346,349,353,355,359..360)
                     /site_type="other"
                     /note="putative Rab5 interface [polypeptide binding]"
                     /db_xref="CDD:213331"
     Region          1197..1260
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          1308..1409
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..1412
                     /gene="GAPVD1"
                     /gene_synonym="GAPex-5; GAPEX5; RAP6"
                     /coded_by="NM_001438414.1:167..4405"
                     /note="isoform 5 is encoded by transcript variant 18"
                     /db_xref="GeneID:26130"
                     /db_xref="HGNC:HGNC:23375"
                     /db_xref="MIM:611714"
ORIGIN      
        1 mvkldihtla hhlkqerlyv nsekqliqrl nadvlktaek lyrtawiakq qrinldrlii
       61 tsaeaspaec cqhakiledt qfvdgykqlg fqetaygefl srlrenprli asslvagekl
      121 nqentqsviy tvftslygnc imqedesyll qvlryliefe lkesdnprrl lrrgtcafsi
      181 lfklfseglf saklfltatl hepimqllve dedhletdpn klierfspsq qeklfgekgs
      241 drfrqkvqem vesneaklva lvnkfigylk qntycfphsl rwivsqmykt lscvdrlevg
      301 evramctdll lacficpavv npeqygiisd apinevarfn lmqvgrllqq lamtgseegd
      361 prtksslgkf dkscvaafld vviggravet pplssvnlle glsrtvvyit ysqlitlvnf
      421 mksvmsgdql redrmaldnl lanlppakpg kssslemtpy ntpqlspatt pankknrlpi
      481 atrsrsrtnm lmdlhmdheg ssqetiqevq peevlvislg tgpqltpgmm senevlnmql
      541 sdggqgdvpv denklhgpsn rsnsvssldl egesvselga gpsgsngvea lqlleheqat
      601 tqdnlddklr kfeirdmmgl tddrdisetv setwstdvlg sdfdpnided rlqeiagaaa
      661 enmlgsllcl pgsgsvlldp ctgstisett seawsvevlp sdseapdlkq eerlqelesc
      721 sglgstsddt dvrevssrps tpglsvvsgi satsedipnk iedlrsecss dfggkdsvts
      781 pdmdeithga hqltsppsqs esllamfdpl sshegasavv rpkvhyarps hpppdppile
      841 gavggnearl pnfgshvltp aemeafkqrh syperlvrsr ssdivssvrr pmsdpswnrr
      901 pgneerelpp aaaigatslv aaphsssssp skdssrgete erkdsddeks drnrpwwrkr
      961 fvsampkddp sprlsaqaqv aedildkyrn aikrtspsdg amanyestev mgdgesahds
     1021 prdealqnis addlpdsasq aahpqdsafs yrdakkklrl alcsadsvaf pvlthstrng
     1081 lpdhtdpedn eivcflkvqi aeainlqdkn lmaqlqetmr cvcrfdnrtc rkllasiaed
     1141 yrkrapyiay ltrcrqglqt tqahlerllq rvlrdkevan ryfttvcvrl lleskekkir
     1201 efiqdfqklt aaddktaqve dflqflygam aqdviwqnas eeqlqdaqla iersvmnrif
     1261 klafypnqdg dilrdqvlhe hiqrlskvvt anhralqipe vylreapwps aqseirtisa
     1321 yktprdkvqc ilrmcstimn llslanedsv pgaddfvpvl vfvlikanpp cllstvqyis
     1381 sfyasclsge esywwmqfta avefiktidd rk
//
LOCUS       NP_001425205             335 aa            linear   PRI 21-NOV-2025
DEFINITION  protein GNAS isoform h [Homo sapiens].
ACCESSION   NP_001425205 XP_024307641 XP_054179349
VERSION     NP_001425205.1
DBSOURCE    REFSEQ: accession NM_001438276.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lin,J., Nie,Q., Cheng,J., Zhong,Y.N., Zhang,T., Zhang,X., Ge,X.,
            Ding,Y., Niu,C., Gao,Y., Wang,K., Gao,M., Wang,X., Chen,W., Yun,C.,
            Ye,C., Xu,J., Shaoyong,W., Zhang,L., Shang,P., Luo,X., Zhang,Z.,
            Zheng,X., Sha,X., Zhang,J., Nie,S., Zhang,X., Ren,F., Liu,H.,
            Dong,E., Yu,X., Ji,L., Pang,Y., Sun,J.P. and Jiang,C.
  TITLE     A microbial amino-acid-conjugated bile acid, tryptophan-cholic
            acid, improves glucose homeostasis via the orphan receptor MRGPRE
  JOURNAL   Cell 188 (17), 4530-4548 (2025)
   PUBMED   40446798
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Crane,J.L., Shamblott,M.J., Axelman,J., Hsu,S., Levine,M.A. and
            Germain-Lee,E.L.
  TITLE     Imprinting status of Galpha(s), NESP55, and XLalphas in cell
            cultures derived from human embryonic germ cells: GNAS imprinting
            in human embryonic germ cells
  JOURNAL   Clin Transl Sci 2 (5), 355-360 (2009)
   PUBMED   20443919
  REMARK    GeneRIF: analysis of the imprinting Status of Galpha(s), NESP55,
            and XLalphas in cell cultures derived from human embryonic germ
            cells
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Bastepe,M.
  TITLE     The GNAS Locus: Quintessential Complex Gene Encoding Gsalpha,
            XLalphas, and other Imprinted Transcripts
  JOURNAL   Curr Genomics 8 (6), 398-414 (2007)
   PUBMED   19412439
  REMARK    GeneRIF: GNAS locus has a highly complex imprinted expression
            pattern, giving rise to transcripts (including non-coding) that are
            maternally, paternally, or biallelically expressed.
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Jakobsen,A.M., Ahlman,H., Kolby,L., Abrahamsson,J.,
            Fischer-Colbrie,R. and Nilsson,O.
  TITLE     NESP55, a novel chromogranin-like peptide, is expressed in
            endocrine tumours of the pancreas and adrenal medulla but not in
            ileal carcinoids
  JOURNAL   Br J Cancer 88 (11), 1746-1754 (2003)
   PUBMED   12771991
  REMARK    GeneRIF: Neuroendocrine secretory protein 55 is found in a subset
            of neuroendocrine tumours showing differentiation towards adrenal
            chromaffin cells and pancreatic islets cells and not in ileal
            carcinoids
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Freson,K., Jaeken,J., Van Helvoirt,M., de Zegher,F.,
            Wittevrongel,C., Thys,C., Hoylaerts,M.F., Vermylen,J. and Van
            Geet,C.
  TITLE     Functional polymorphisms in the paternally expressed XLalphas and
            its cofactor ALEX decrease their mutual interaction and enhance
            receptor-mediated cAMP formation
  JOURNAL   Hum Mol Genet 12 (10), 1121-1130 (2003)
   PUBMED   12719376
REFERENCE   6  (residues 1 to 335)
  AUTHORS   Weiss,U., Ischia,R., Eder,S., Lovisetti-Scamihorn,P., Bauer,R. and
            Fischer-Colbrie,R.
  TITLE     Neuroendocrine secretory protein 55 (NESP55): alternative splicing
            onto transcripts of the GNAS gene and posttranslational processing
            of a maternally expressed protein
  JOURNAL   Neuroendocrinology 71 (3), 177-186 (2000)
   PUBMED   10729789
REFERENCE   7  (residues 1 to 335)
  AUTHORS   Ischia,R., Lovisetti-Scamihorn,P., Hogue-Angeletti,R.,
            Wolkersdorfer,M., Winkler,H. and Fischer-Colbrie,R.
  TITLE     Molecular cloning and characterization of NESP55, a novel
            chromogranin-like precursor of a peptide with 5-HT1B receptor
            antagonist activity
  JOURNAL   J Biol Chem 272 (17), 11657-11662 (1997)
   PUBMED   9111083
REFERENCE   8  (residues 1 to 335)
  AUTHORS   Haldeman-Englert,C.R., Hurst,A.C.E. and Levine,M.A.
  TITLE     Disorders of GNAS Inactivation
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29072892
REFERENCE   9  (residues 1 to 335)
  AUTHORS   Szymczuk,V., Florenzano,P., de Castro,L.F., Collins,M.T. and
            Boyce,A.M.
  TITLE     Fibrous Dysplasia / McCune-Albright Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719192
REFERENCE   10 (residues 1 to 335)
  AUTHORS   Weinstein,L.S., Gejman,P.V., de Mazancourt,P., American,N. and
            Spiegel,A.M.
  TITLE     A heterozygous 4-bp deletion mutation in the Gs alpha gene (GNAS1)
            in a patient with Albright hereditary osteodystrophy
  JOURNAL   Genomics 13 (4), 1319-1321 (1992)
   PUBMED   1505964
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121917.20 and AL109840.24.
            
            On or before Apr 17, 2025 this sequence version replaced
            XP_024307641.1, XP_054179349.1.
            
            Summary: This locus has a highly complex imprinted expression
            pattern. It gives rise to maternally, paternally, and biallelically
            expressed transcripts that are derived from four alternative
            promoters and 5' exons. Some transcripts contain a differentially
            methylated region (DMR) at their 5' exons, and this DMR is commonly
            found in imprinted genes and correlates with transcript expression.
            An antisense transcript is produced from an overlapping locus on
            the opposite strand. One of the transcripts produced from this
            locus, and the antisense transcript, are paternally expressed
            noncoding RNAs, and may regulate imprinting in this region. In
            addition, one of the transcripts contains a second overlapping ORF,
            which encodes a structurally unrelated protein - Alex. Alternative
            splicing of downstream exons is also observed, which results in
            different forms of the stimulatory G-protein alpha subunit, a key
            element of the classical signal transduction pathway linking
            receptor-ligand interactions with the activation of adenylyl
            cyclase and a variety of cellular reponses. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            Mutations in this gene result in pseudohypoparathyroidism type 1a,
            pseudohypoparathyroidism type 1b, Albright hereditary
            osteodystrophy, pseudopseudohypoparathyroidism, McCune-Albright
            syndrome, progressive osseus heteroplasia, polyostotic fibrous
            dysplasia of bone, and some pituitary tumors. [provided by RefSeq,
            Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3036583.1,
                                           SRR14038194.3028822.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 19412439
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.32"
     Protein         1..335
                     /product="protein GNAS isoform h"
                     /note="secretogranin VI; G protein subunit alpha S;
                     guanine nucleotide binding protein (G protein), alpha
                     stimulating activity polypeptide 1; guanine nucleotide
                     regulatory protein; adenylate cyclase-stimulating G alpha
                     protein; protein ALEX; extra large alphas protein;
                     alternative gene product encoded by XL-exon"
                     /calculated_mol_wt=38867
     Region          1..329
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Site            order(34,38,42,45,48..49,69,72,113,142,167,175,179)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Site            140..148
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            145
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(146,148,150,161,163,167..169,171,174..175,177..180)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(148,173,176..177,180)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            164..167
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            165..181
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Site            233..236
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(298..309,311..314)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Site            306..308
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..335
                     /gene="GNAS"
                     /gene_synonym="AHO; AIMAH1; C20orf45; GNAS1; GPSA; GSA;
                     GSP; NESP; PITA3; POH; SCG6; SgVI"
                     /coded_by="NM_001438276.1:86..1093"
                     /note="isoform h is encoded by transcript variant 20"
                     /db_xref="GeneID:2778"
                     /db_xref="HGNC:HGNC:4392"
                     /db_xref="MIM:139320"
ORIGIN      
        1 mrilhvngfn geggeedpqa arsnsdgeka tkvqdiknnl keaietivaa msnlvppvel
       61 anpenqfrvd yilsvmnvpd fdfppefyeh akalwedegv racyersney qlidcaqyfl
      121 dkidvikqad yvpsdqdllr crvltsgife tkfqvdkvnf hmfdvggqrd errkwiqcfn
      181 dvtaiifvva sssynmvire dnqtnrlqea lnlfksiwnn rwlrtisvil flnkqdllae
      241 kvlagkskie dyfpefaryt tpedatpepg edprvtraky firdeflris tasgdgrhyc
      301 yphftcavdt enirrvfndc rdiiqrmhlr qyell
//
LOCUS       NP_001401240             350 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 3 isoform 11
            precursor [Homo sapiens].
ACCESSION   NP_001401240
VERSION     NP_001401240.1
DBSOURCE    REFSEQ: accession NM_001414311.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Tang,Q., Yuan,Y., Li,L., Xu,Y., Ji,W., Xiao,S., Han,Y., Miao,W.,
            Cai,J., You,P., Chen,M., Ding,S., Li,Z., Qi,Z., Hou,W. and Luo,H.
  TITLE     Comprehensive analysis reveals that LTBR is a immune-related
            biomarker for glioma
  JOURNAL   Comput Biol Med 174, 108457 (2024)
   PUBMED   38599071
  REMARK    GeneRIF: Comprehensive analysis reveals that LTBR is a
            immune-related biomarker for glioma.
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Wu,Y., Zhao,S., Guo,W., Liu,Y., Requena Mullor,M.D.M.,
            Rodriguez,R.A. and Wei,R.
  TITLE     Systematic analysis of the prognostic value and immunological
            function of LTBR in human cancer
  JOURNAL   Aging (Albany NY) 16 (1), 129-152 (2024)
   PUBMED   38175686
  REMARK    GeneRIF: Systematic analysis of the prognostic value and
            immunological function of LTBR in human cancer.
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Shuptrine,C.W., Perez,V.M., Selitsky,S.R., Schreiber,T.H. and
            Fromm,G.
  TITLE     Shining a LIGHT on myeloid cell targeted immunotherapy
  JOURNAL   Eur J Cancer 187, 147-160 (2023)
   PUBMED   37167762
  REMARK    Review article
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Abudukeyoumu,A., Lai,Z.Z., Lu,J.J., Zhang,X., Hou,D.Y., Dong,J.,
            Wu,J.N., Li,M.Q. and Xie,F.
  TITLE     A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion
  JOURNAL   J Reprod Immunol 153, 103693 (2022)
   PUBMED   35987137
  REMARK    GeneRIF: A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion.
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Remouchamps,C., Boutaffala,L., Ganeff,C. and Dejardin,E.
  TITLE     Biology and signal transduction pathways of the
            Lymphotoxin-alphabeta/LTbetaR system
  JOURNAL   Cytokine Growth Factor Rev 22 (5-6), 301-310 (2011)
   PUBMED   22152226
  REMARK    Review article
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Nakano,H., Oshima,H., Chung,W., Williams-Abbott,L., Ware,C.F.,
            Yagita,H. and Okumura,K.
  TITLE     TRAF5, an activator of NF-kappaB and putative signal transducer for
            the lymphotoxin-beta receptor
  JOURNAL   J Biol Chem 271 (25), 14661-14664 (1996)
   PUBMED   8663299
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Browning,J.L., Miatkowski,K., Sizing,I., Griffiths,D., Zafari,M.,
            Benjamin,C.D., Meier,W. and Mackay,F.
  TITLE     Signaling through the lymphotoxin beta receptor induces the death
            of some adenocarcinoma tumor lines
  JOURNAL   J Exp Med 183 (3), 867-878 (1996)
   PUBMED   8642291
REFERENCE   8  (residues 1 to 350)
  AUTHORS   Baens,M., Aerssens,J., van Zand,K., Van den Berghe,H. and
            Marynen,P.
  TITLE     Isolation and regional assignment of human chromosome 12p cDNAs
  JOURNAL   Genomics 29 (1), 44-52 (1995)
   PUBMED   8530100
REFERENCE   9  (residues 1 to 350)
  AUTHORS   Crowe,P.D., VanArsdale,T.L., Walter,B.N., Ware,C.F., Hession,C.,
            Ehrenfels,B., Browning,J.L., Din,W.S., Goodwin,R.G. and Smith,C.A.
  TITLE     A lymphotoxin-beta-specific receptor
  JOURNAL   Science 264 (5159), 707-710 (1994)
   PUBMED   8171323
REFERENCE   10 (residues 1 to 350)
  AUTHORS   Baens,M., Chaffanet,M., Cassiman,J.J., van den Berghe,H. and
            Marynen,P.
  TITLE     Construction and evaluation of a hncDNA library of human 12p
            transcribed sequences derived from a somatic cell hybrid
  JOURNAL   Genomics 16 (1), 214-218 (1993)
   PUBMED   8486360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005840.2.
            
            Summary: This gene encodes a member of the tumor necrosis factor
            receptor superfamily. The major ligands of this receptor include
            lymphotoxin alpha/beta and tumor necrosis factor ligand superfamily
            member 14. The encoded protein plays a role in signalling during
            the development of lymphoid and other organs, lipid metabolism,
            immune response, and programmed cell death. Activity of this
            receptor has also been linked to carcinogenesis. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279829.43.1,
                                           SRR14243140.2256086.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004, SAMEA2155770
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..350
                     /product="tumor necrosis factor receptor superfamily
                     member 3 isoform 11 precursor"
                     /note="tumor necrosis factor C receptor; lymphotoxin B
                     receptor; tumor necrosis factor receptor type III;
                     lymphotoxin beta receptor (TNFR superfamily, member 3);
                     tumor necrosis factor receptor 2-related protein"
                     /calculated_mol_wt=34737
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3049
     Region          11..168
                     /region_name="TNFRSF3"
                     /note="Tumor necrosis factor receptor superfamily member 3
                     (TNFRSF3), also known as lymphotoxin beta receptor (LTBR);
                     cd10578"
                     /db_xref="CDD:276904"
     Region          22..80
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276904"
     Region          83..124
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276904"
     Region          126..167
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276904"
     Region          148..>210
                     /region_name="TNFRSF"
                     /note="Tumor necrosis factor receptor superfamily
                     (TNFRSF); cl22855"
                     /db_xref="CDD:473981"
     Region          170..210
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276924"
     CDS             1..350
                     /gene="LTBR"
                     /gene_synonym="D12S370; LT-BETA-R; TNF-R-III; TNFCR;
                     TNFR-RP; TNFR2-RP; TNFR3; TNFRSF3"
                     /coded_by="NM_001414311.1:198..1250"
                     /note="isoform 11 precursor is encoded by transcript
                     variant 11"
                     /db_xref="GeneID:4055"
                     /db_xref="HGNC:HGNC:6718"
                     /db_xref="MIM:600979"
ORIGIN      
        1 mllpwatsap glawgplvlg lfgllaasqp qavppyasen qtcrdqekey yepqhriccs
       61 rcppgtyvsa kcsrirdtvc atcaensyne hwnylticql crpcdpvmgl eeiapctskr
      121 ktqcrcqpgm fcaawalect hcellsdcpp gteaelkdev gkgnnhcvpc kaghfqntss
      181 psarcqphtr cenqglveaa pgtaqsdttc knpleplppe msgtmlmlav llplafflll
      241 atvfsciwks hpslcrklgt ngihvtggsm titgniyiyn gpvlggppgp gdlpatpepp
      301 ypipeegdpg ppglstphqe dgkawhlaet ehcgatpsnr gprnqfithd
//
LOCUS       NP_001397826             427 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial carrier homolog 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001397826 XP_005249035
VERSION     NP_001397826.1
DBSOURCE    REFSEQ: accession NM_001410897.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Xie,L., Shu,Y., Ye,M. and Li,Y.
  TITLE     Identification of MTCH1 as a novel prognostic indicator and
            therapeutic target in hepatocellular carcinoma
  JOURNAL   Pathol Res Pract 259, 155358 (2024)
   PUBMED   38820930
  REMARK    GeneRIF: Identification of MTCH1 as a novel prognostic indicator
            and therapeutic target in hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Wang,X., Ji,Y., Qi,J., Zhou,S., Wan,S., Fan,C., Gu,Z., An,P.,
            Luo,Y. and Luo,J.
  TITLE     Mitochondrial carrier 1 (MTCH1) governs ferroptosis by triggering
            the FoxO1-GPX4 axis-mediated retrograde signaling in cervical
            cancer cells
  JOURNAL   Cell Death Dis 14 (8), 508 (2023)
   PUBMED   37550282
  REMARK    GeneRIF: Mitochondrial carrier 1 (MTCH1) governs ferroptosis by
            triggering the FoxO1-GPX4 axis-mediated retrograde signaling in
            cervical cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Guna,A., Stevens,T.A., Inglis,A.J., Replogle,J.M., Esantsi,T.K.,
            Muthukumar,G., Shaffer,K.C.L., Wang,M.L., Pogson,A.N., Jones,J.J.,
            Lomenick,B., Chou,T.F., Weissman,J.S. and Voorhees,R.M.
  TITLE     MTCH2 is a mitochondrial outer membrane protein insertase
  JOURNAL   Science 378 (6617), 317-322 (2022)
   PUBMED   36264797
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Lamarca,V., Marzo,I., Sanz-Clemente,A. and Carrodeguas,J.A.
  TITLE     Exposure of any of two proapoptotic domains of presenilin
            1-associated protein/mitochondrial carrier homolog 1 on the surface
            of mitochondria is sufficient for induction of apoptosis in a
            Bax/Bak-independent manner
  JOURNAL   Eur J Cell Biol 87 (5), 325-334 (2008)
   PUBMED   18375015
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Mao,G., Tan,J., Gao,W., Shi,Y., Cui,M.Z. and Xu,X.
  TITLE     Both the N-terminal fragment and the protein-protein interaction
            domain (PDZ domain) are required for the pro-apoptotic activity of
            presenilin-associated protein PSAP
  JOURNAL   Biochim Biophys Acta 1780 (4), 696-708 (2008)
   PUBMED   18291114
  REMARK    GeneRIF: Data show that all PSAP splicing isoforms are localized in
            the mitochondria and are pro-apoptotic.
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Lamarca,V., Sanz-Clemente,A., Perez-Pe,R., Martinez-Lorenzo,M.J.,
            Halaihel,N., Muniesa,P. and Carrodeguas,J.A.
  TITLE     Two isoforms of PSAP/MTCH1 share two proapoptotic domains and
            multiple internal signals for import into the mitochondrial outer
            membrane
  JOURNAL   Am J Physiol Cell Physiol 293 (4), C1347-C1361 (2007)
   PUBMED   17670888
  REMARK    GeneRIF: PSAP has two proapoptotic isoforms generated by
            alternative splicing, and both proteins are imported into the
            mitochondrial outer membrane using multiple internal targeting
            signals, and both contain two proapoptotic domains.
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Xu,X., Shi,Y.C., Gao,W., Mao,G., Zhao,G., Agrawal,S., Chisolm,G.M.,
            Sui,D. and Cui,M.Z.
  TITLE     The novel presenilin-1-associated protein is a proapoptotic
            mitochondrial protein
  JOURNAL   J Biol Chem 277 (50), 48913-48922 (2002)
   PUBMED   12377771
  REMARK    GeneRIF: mitochondrial localization and proapoptotic activity of
            PSAP suggest that it is an important regulator of apoptosis
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Xu,X., Shi,Yc., Wu,X., Gambetti,P., Sui,D. and Cui,M.Z.
  TITLE     Identification of a novel PSD-95/Dlg/ZO-1 (PDZ)-like protein
            interacting with the C terminus of presenilin-1
  JOURNAL   J Biol Chem 274 (46), 32543-32546 (1999)
   PUBMED   10551805
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL122034.29.
            
            On Aug 17, 2022 this sequence version replaced XP_005249035.1.
            
            Summary: This gene encodes a member of the mitochondrial carrier
            family. The encoded protein is localized to the mitochondrion inner
            membrane and induces apoptosis independent of the proapoptotic
            proteins Bax and Bak. Pseudogenes on chromosomes 6 and 11 have been
            identified for this gene. Alternatively spliced transcript variants
            encoding multiple isoforms have been observed. [provided by RefSeq,
            Oct 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC040659.1, SRR18074968.173643.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..427
                     /product="mitochondrial carrier homolog 1 isoform 3"
                     /note="presenilin-associated protein; cell
                     proliferation-inducing protein 60; mitochondrial carrier
                     homolog 1; solute carrier family 25, member 49"
                     /calculated_mol_wt=46169
     Region          1..76
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Site            29
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Region          76..173
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Region          81..176
                     /region_name="Solcar 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Site            94..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Site            156..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Region          192..280
                     /region_name="Solcar 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Region          206..>264
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Site            210..229
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Site            255..279
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     Site            323..342
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZJ7.1)"
     CDS             1..427
                     /gene="MTCH1"
                     /gene_synonym="CGI-64; PIG60; PSAP; SLC25A49"
                     /coded_by="NM_001410897.1:334..1617"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS93905.1"
                     /db_xref="GeneID:23787"
                     /db_xref="HGNC:HGNC:17586"
                     /db_xref="MIM:610449"
ORIGIN      
        1 mgasdpevap warggaagma gagagagarg gaaagveara rdpppahrah prhprpaaqp
       61 sarrmdggsg glgsgdnapt tealfvalga gvtalshpll yvklliqvgh epmpptlgtn
      121 vlgrkvlylp sfftyakyiv qvdgkiglfr glsprlmsna lstvtrgsmk kvfppdeieq
      181 vsnkddmkts lkkvvketsy emmmqcvsrm lahplhvism rcmvqfvgre akysgvlssi
      241 gkifkeegll gffvgliphl lgdvvflwgc nllahfinay lvddsvsdtp gglgndqnpg
      301 sqfsqalair sytkfvmgia vsmltypfll vgdlmavnnc glqaglppys pvfkswihcw
      361 kylsvqvskh wtaeafpvlc yilqlkwfcg cfiackdkwf hgiqyceeil giykafkfss
      421 yiiseri
//
LOCUS       NP_001400241             224 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 12 [Homo sapiens].
ACCESSION   NP_001400241
VERSION     NP_001400241.1
DBSOURCE    REFSEQ: accession NM_001413312.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 224)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 224)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 224)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 224)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 224)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.7486.1,
                                           SRR3476690.837482.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..224
                     /product="RNA-binding Raly-like protein isoform 12"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=24742
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     CDS             1..224
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413312.1:1175..1849"
                     /note="isoform 12 is encoded by transcript variant 39"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly sgyvfdydyy
      121 rddfynrlfd yhgrvppppr aviplkrprv avtttrrgkg vfsmkggsrs tasgstgskl
      181 ksdelqtikk eltqiktkid sllgrlekie kqqkaeavst dkvi
//
LOCUS       NP_001424215            1070 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            beta isoform isoform 1 [Homo sapiens].
ACCESSION   NP_001424215 XP_006713722 XP_054202825
VERSION     NP_001424215.1
DBSOURCE    REFSEQ: accession NM_001437286.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Liu,L., Feng,X., Fan,C., Kong,D., Feng,X., Sun,C., Xu,Y., Li,B.,
            Jiang,Y. and Zheng,C.
  TITLE     PDCD4 interacting with PIK3CB and CTSZ promotes the apoptosis of
            multiple myeloma cells
  JOURNAL   FASEB J 38 (16), e70024 (2024)
   PUBMED   39190024
  REMARK    GeneRIF: PDCD4 interacting with PIK3CB and CTSZ promotes the
            apoptosis of multiple myeloma cells.
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Liu,G., Hou,Y., Jin,X., Zhang,Y., Sun,C., Huang,C., Ren,Y., Gao,J.,
            Wang,X. and Jiang,X.
  TITLE     PI3K/HSCB axis facilitates FOG1 nuclear translocation to promote
            erythropoiesis and megakaryopoiesis
  JOURNAL   Elife 13, 95815 (2024)
   PUBMED   38757931
  REMARK    GeneRIF: PI3K/HSCB axis facilitates FOG1 nuclear translocation to
            promote erythropoiesis and megakaryopoiesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1070)
  AUTHORS   Duewell,B.R., Wilson,N.E., Bailey,G.M., Peabody,S.E. and
            Hansen,S.D.
  TITLE     Molecular dissection of PI3Kbeta synergistic activation by receptor
            tyrosine kinases, GbetaGgamma, and Rho-family GTPases
  JOURNAL   Elife 12, 88991 (2024)
   PUBMED   38713746
  REMARK    GeneRIF: Molecular dissection of PI3Kbeta synergistic activation by
            receptor tyrosine kinases, GbetaGgamma, and Rho-family GTPases.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1070)
  AUTHORS   Xu,W., Chen,Y., Zhang,Z., Jiang,Y. and Wang,Z.
  TITLE     Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma
  JOURNAL   Med Oncol 40 (8), 221 (2023)
   PUBMED   37402056
  REMARK    GeneRIF: Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1070)
  AUTHORS   Milani,D., Mazzoni,M., Borgatti,P., Zauli,G., Cantley,L. and
            Capitani,S.
  TITLE     Extracellular human immunodeficiency virus type-1 Tat protein
            activates phosphatidylinositol 3-kinase in PC12 neuronal cells
  JOURNAL   J Biol Chem 271 (38), 22961-22964 (1996)
   PUBMED   8798481
REFERENCE   7  (residues 1 to 1070)
  AUTHORS   Bonnefoy-Berard,N., Liu,Y.C., von Willebrand,M., Sung,A., Elly,C.,
            Mustelin,T., Yoshida,H., Ishizaka,K. and Altman,A.
  TITLE     Inhibition of phosphatidylinositol 3-kinase activity by association
            with 14-3-3 proteins in T cells
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10142-10146 (1995)
   PUBMED   7479742
REFERENCE   8  (residues 1 to 1070)
  AUTHORS   Hu,P. and Schlessinger,J.
  TITLE     Direct association of p110 beta phosphatidylinositol 3-kinase with
            p85 is mediated by an N-terminal fragment of p110 beta
  JOURNAL   Mol Cell Biol 14 (4), 2577-2583 (1994)
   PUBMED   8139559
REFERENCE   9  (residues 1 to 1070)
  AUTHORS   Hu,P., Mondino,A., Skolnik,E.Y. and Schlessinger,J.
  TITLE     Cloning of a novel, ubiquitously expressed human
            phosphatidylinositol 3-kinase and identification of its binding
            site on p85
  JOURNAL   Mol Cell Biol 13 (12), 7677-7688 (1993)
   PUBMED   8246984
REFERENCE   10 (residues 1 to 1070)
  AUTHORS   Carpenter,C.L., Duckworth,B.C., Auger,K.R., Cohen,B.,
            Schaffhausen,B.S. and Cantley,L.C.
  TITLE     Purification and characterization of phosphoinositide 3-kinase from
            rat liver
  JOURNAL   J Biol Chem 265 (32), 19704-19711 (1990)
   PUBMED   2174051
  REMARK    GeneRIF: This paper reports the first purification of a
            phosphoinositide 3-kinase and shows that the protein is a
            heterodimer of an 85 kd regulatory subunit that mediates binding to
            phosphorylated proteins and a 110 kd catalytic subunit.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC067728.25, AC117389.5 and AC020890.22.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_006713722.1, XP_054202825.1.
            
            Summary: This gene encodes an isoform of the catalytic subunit of
            phosphoinositide 3-kinase (PI3K). These kinases are important in
            signaling pathways involving receptors on the outer membrane of
            eukaryotic cells and are named for their catalytic subunit. The
            encoded protein is the catalytic subunit for PI3Kbeta (PI3KB).
            PI3KB has been shown to be part of the activation pathway in
            neutrophils which have bound immune complexes at sites of injury or
            infection. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853559.23777.1,
                                           SRR14038197.2133225.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..1070
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit beta isoform isoform 1"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.1.153"
                     /note="PI3-kinase p110 subunit beta; PtdIns-3-kinase p110;
                     PI3K-beta; PI3-kinase subunit beta; ptdIns-3-kinase
                     subunit beta; ptdIns-3-kinase subunit p110-beta;
                     phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa
                     catalytic subunit beta; serine/threonine protein kinase
                     PIK3CB; phosphoinositide-3-kinase, catalytic, beta
                     polypeptide"
                     /calculated_mol_wt=122632
     Region          41..118
                     /region_name="PI3K_p85B"
                     /note="PI3-kinase family, p85-binding domain; smart00143"
                     /db_xref="CDD:197539"
     Region          180..288
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, Ras-binding domain; smart00144"
                     /db_xref="CDD:197540"
     Region          324..501
                     /region_name="C2_PI3K_class_I_beta_delta"
                     /note="C2 domain present in class I beta and delta
                     phosphatidylinositol 3-kinases (PI3Ks); cd08693"
                     /db_xref="CDD:176075"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI9; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     Region          410..418
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Region          532..702
                     /region_name="PI3Ka_I"
                     /note="Phosphoinositide 3-kinase (PI3K) class I, accessory
                     domain; PIK domain is conserved in all PI3 and
                     PI4-kinases. Its role is unclear but it has been suggested
                     to be involved in substrate presentation. In general, PI3K
                     class I prefer phosphoinositol (4,5)...; cd00872"
                     /db_xref="CDD:238444"
     Region          706..1067
                     /region_name="PI3Kc_IA_beta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase beta; cd05173"
                     /db_xref="CDD:270717"
     Region          778..784
                     /region_name="G-loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(779,781..783,785,803,805,808,839,851..854,859,862,
                     924,926,936..937)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270717"
     Site            order(846..847,874..875,878,948..949,962,965,973..976,979,
                     1046,1049..1050,1052..1053)
                     /site_type="other"
                     /note="regulatory subunit interface [polypeptide binding]"
                     /db_xref="CDD:270717"
     Site            893
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270717"
     Region          916..924
                     /region_name="Catalytic loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            916..924
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270717"
     Region          935..961
                     /region_name="Activation loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(937..950,956..961)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270717"
     Site            1070
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12502714; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     CDS             1..1070
                     /gene="PIK3CB"
                     /gene_synonym="P110BETA; PI3K; PI3KBETA; PIK3C1"
                     /coded_by="NM_001437286.1:251..3463"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:5291"
                     /db_xref="HGNC:HGNC:8976"
                     /db_xref="MIM:602925"
ORIGIN      
        1 mcfsfimppa madildiwav dsqiasdgsi pvdfllptgi yiqlevprea tisyikqmlw
       61 kqvhnypmfn llmdidsymf acvnqtavye eledetrrlc dvrpflpvlk lvtrscdpge
      121 kldskigvli gkglhefdsl kdpevnefrr kmrkfseeki lslvglswmd wlkqtyppeh
      181 epsipenled klyggkliva vhfencqdvf sfqvspnmnp ikvnelaiqk rltihgkede
      241 vspydyvlqv sgrveyvfgd hpliqfqyir ncvmnralph filvecckik kmyeqemiai
      301 eaainrnssn lplplppkkt riishvwenn npfqivlvkg nklnteetvk vhvraglfhg
      361 tellcktivs sevsgkndhi wneplefdin icdlprmarl cfavyavldk vktkkstkti
      421 npskyqtirk agkvhypvaw vntmvfdfkg qlrtgdiilh swssfpdele emlnpmgtvq
      481 tnpytenata lhvkfpenkk qpyyyppfdk iiekaaeias sdsanvssrg gkkflpvlke
      541 ildrdplsql cenemdliwt lrqdcreifp qslpklllsi kwnkledvaq lqallqiwpk
      601 lpprealell dfnypdqyvr eyavgclrqm sdeelsqyll qlvqvlkyep fldcalsrfl
      661 leralgnrri gqflfwhlrs evhipavsvq fgvileaycr gsvghmkvls kqvealnklk
      721 tlnsliklna vklnrakgke amhtclkqsa yrealsdlqs plnpcvilse lyvekckymd
      781 skmkplwlvy nnkvfgedsv gvifkngddl rqdmltlqml rlmdllwkea gldlrmlpyg
      841 clatgdrsgl ievvstseti adiqlnssnv aaaaafnkda llnwlkeyns gddldraiee
      901 ftlscagycv asyvlgigdr hsdnimvkkt gqlfhidfgh ilgnfkskfg ikrervpfil
      961 tydfihviqq gktgntekfg rfrqcceday lilrrhgnlf itlfalmlta glpeltsvkd
     1021 iqylkdslal gkseeealkq fkqkfdealr eswttkvnwm ahtvrkdyrs
//
LOCUS       NP_001400295             345 aa            linear   PRI 21-NOV-2025
DEFINITION  telomeric repeat-binding factor 1 isoform 6 [Homo sapiens].
ACCESSION   NP_001400295 XP_047278121
VERSION     NP_001400295.1
DBSOURCE    REFSEQ: accession NM_001413366.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Hu,H., van Roon,A.M., Ghanim,G.E., Ahsan,B., Oluwole,A.O.,
            Peak-Chew,S.Y., Robinson,C.V. and Nguyen,T.H.D.
  TITLE     Structural basis of telomeric nucleosome recognition by shelterin
            factor TRF1
  JOURNAL   Sci Adv 9 (34), eadi4148 (2023)
   PUBMED   37624885
  REMARK    GeneRIF: Structural basis of telomeric nucleosome recognition by
            shelterin factor TRF1.
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Harmak,H., Redouane,S., Charoute,H., Aniq Filali,O., Barakat,A. and
            Rouba,H.
  TITLE     In silico exploration and molecular dynamics of deleterious SNPs on
            the human TERF1 protein triggering male infertility
  JOURNAL   J Biomol Struct Dyn 41 (24), 14665-14688 (2023)
   PUBMED   36995171
  REMARK    GeneRIF: In silico exploration and molecular dynamics of
            deleterious SNPs on the human TERF1 protein triggering male
            infertility.
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Abreu,P.L., Lee,Y.W. and Azzalin,C.M.
  TITLE     In Vitro Characterization of the Physical Interactions between the
            Long Noncoding RNA TERRA and the Telomeric Proteins TRF1 and TRF2
  JOURNAL   Int J Mol Sci 23 (18), 10463 (2022)
   PUBMED   36142374
  REMARK    GeneRIF: In Vitro Characterization of the Physical Interactions
            between the Long Noncoding RNA TERRA and the Telomeric Proteins
            TRF1 and TRF2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Jack,A., Kim,Y., Strom,A.R., Lee,D.S.W., Williams,B., Schaub,J.M.,
            Kellogg,E.H., Finkelstein,I.J., Ferro,L.S., Yildiz,A. and
            Brangwynne,C.P.
  TITLE     Compartmentalization of telomeres through DNA-scaffolded phase
            separation
  JOURNAL   Dev Cell 57 (2), 277-290 (2022)
   PUBMED   35077681
  REMARK    GeneRIF: Compartmentalization of telomeres through DNA-scaffolded
            phase separation.
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Broccoli,D., Chong,L., Oelmann,S., Fernald,A.A., Marziliano,N., van
            Steensel,B., Kipling,D., Le Beau,M.M. and de Lange,T.
  TITLE     Comparison of the human and mouse genes encoding the telomeric
            protein, TRF1: chromosomal localization, expression and conserved
            protein domains
  JOURNAL   Hum Mol Genet 6 (1), 69-76 (1997)
   PUBMED   9002672
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Lu,K.P., Hanes,S.D. and Hunter,T.
  TITLE     A human peptidyl-prolyl isomerase essential for regulation of
            mitosis
  JOURNAL   Nature 380 (6574), 544-547 (1996)
   PUBMED   8606777
REFERENCE   8  (residues 1 to 345)
  AUTHORS   Bilaud,T., Koering,C.E., Binet-Brasselet,E., Ancelin,K.,
            Pollice,A., Gasser,S.M. and Gilson,E.
  TITLE     The telobox, a Myb-related telomeric DNA binding motif found in
            proteins from yeast, plants and human
  JOURNAL   Nucleic Acids Res 24 (7), 1294-1303 (1996)
   PUBMED   8614633
REFERENCE   9  (residues 1 to 345)
  AUTHORS   Chong,L., van Steensel,B., Broccoli,D., Erdjument-Bromage,H.,
            Hanish,J., Tempst,P. and de Lange,T.
  TITLE     A human telomeric protein
  JOURNAL   Science 270 (5242), 1663-1667 (1995)
   PUBMED   7502076
REFERENCE   10 (residues 1 to 345)
  AUTHORS   Zhong,Z., Shiue,L., Kaplan,S. and de Lange,T.
  TITLE     A mammalian factor that binds telomeric TTAGGG repeats in vitro
  JOURNAL   Mol Cell Biol 12 (11), 4834-4843 (1992)
   PUBMED   1406665
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022893.6.
            
            On Oct 31, 2022 this sequence version replaced XP_047278121.1.
            
            Summary: This gene encodes a telomere specific protein which is a
            component of the telomere nucleoprotein complex. This protein is
            present at telomeres throughout the cell cycle and functions as an
            inhibitor of telomerase, acting in cis to limit the elongation of
            individual chromosome ends. The protein structure contains a
            C-terminal Myb motif, a dimerization domain near its N-terminus and
            an acidic N-terminus. Multiple transcripts of this gene are
            alternatively spliced products. [provided by RefSeq, Aug 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1514659.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.11"
     Protein         1..345
                     /product="telomeric repeat-binding factor 1 isoform 6"
                     /note="NIMA-interacting protein 2; telomeric protein
                     Pin2/TRF1; TTAGGG repeat-binding factor 1; telomeric
                     repeat binding factor (NIMA-interacting) 1"
                     /calculated_mol_wt=40250
     Region          1..160
                     /region_name="TRFH"
                     /note="Telomeric Repeat binding Factor or TTAGGG Repeat
                     binding Factor, central (dimerization) domain Homology;
                     TRFH. Telomeres are protein/DNA complexes that make up the
                     physical ends of eukaryotic linear chromosomes and are
                     essential for chromosome stability; cl02779"
                     /db_xref="CDD:413471"
     Site            order(2,5,19,23,27,37..41,49,52..53,56)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238174"
     Region          287..335
                     /region_name="SANT_TRF"
                     /note="Telomere repeat binding factor-like DNA-binding
                     domains of the SANT/myb-like family; cd11660"
                     /db_xref="CDD:212558"
     Site            order(287..289,307,309..310,321,323..325,327..329,
                     331..332)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212558"
     CDS             1..345
                     /gene="TERF1"
                     /gene_synonym="hTRF1-AS; PIN2; t-TRF1; TRBF1; TRF; TRF1"
                     /coded_by="NM_001413366.1:412..1449"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:7013"
                     /db_xref="HGNC:HGNC:11728"
                     /db_xref="MIM:600951"
ORIGIN      
        1 mftiihglss ltacqlrtiy icqfltriaa gktldaqfen deritplesa lmiwgsieke
       61 hdklheeiqn likiqaiavc mengnfkeae evferifgdp nshmpfkskl lmiisqkdtf
      121 hsffqhfsyn hmmekiksyv nyvlseksst flmkaaakvv eskrtrtits qdkpsgndve
      181 meteanldtr krshknlfls klqhgtqqqd lnkkerrvgt pqityicltk ltmnkkegvr
      241 kglcflvllk hyrtkkkkes rratesripv sksqpvtpek hrarkrqawl weedknlrsg
      301 vrkygegnws killhykfnn rtsvmlkdrw rtmkklklis sdsed
//
LOCUS       NP_001401237             430 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 3 isoform 8
            precursor [Homo sapiens].
ACCESSION   NP_001401237
VERSION     NP_001401237.1
DBSOURCE    REFSEQ: accession NM_001414308.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Tang,Q., Yuan,Y., Li,L., Xu,Y., Ji,W., Xiao,S., Han,Y., Miao,W.,
            Cai,J., You,P., Chen,M., Ding,S., Li,Z., Qi,Z., Hou,W. and Luo,H.
  TITLE     Comprehensive analysis reveals that LTBR is a immune-related
            biomarker for glioma
  JOURNAL   Comput Biol Med 174, 108457 (2024)
   PUBMED   38599071
  REMARK    GeneRIF: Comprehensive analysis reveals that LTBR is a
            immune-related biomarker for glioma.
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Wu,Y., Zhao,S., Guo,W., Liu,Y., Requena Mullor,M.D.M.,
            Rodriguez,R.A. and Wei,R.
  TITLE     Systematic analysis of the prognostic value and immunological
            function of LTBR in human cancer
  JOURNAL   Aging (Albany NY) 16 (1), 129-152 (2024)
   PUBMED   38175686
  REMARK    GeneRIF: Systematic analysis of the prognostic value and
            immunological function of LTBR in human cancer.
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Shuptrine,C.W., Perez,V.M., Selitsky,S.R., Schreiber,T.H. and
            Fromm,G.
  TITLE     Shining a LIGHT on myeloid cell targeted immunotherapy
  JOURNAL   Eur J Cancer 187, 147-160 (2023)
   PUBMED   37167762
  REMARK    Review article
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Abudukeyoumu,A., Lai,Z.Z., Lu,J.J., Zhang,X., Hou,D.Y., Dong,J.,
            Wu,J.N., Li,M.Q. and Xie,F.
  TITLE     A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion
  JOURNAL   J Reprod Immunol 153, 103693 (2022)
   PUBMED   35987137
  REMARK    GeneRIF: A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion.
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Remouchamps,C., Boutaffala,L., Ganeff,C. and Dejardin,E.
  TITLE     Biology and signal transduction pathways of the
            Lymphotoxin-alphabeta/LTbetaR system
  JOURNAL   Cytokine Growth Factor Rev 22 (5-6), 301-310 (2011)
   PUBMED   22152226
  REMARK    Review article
REFERENCE   6  (residues 1 to 430)
  AUTHORS   Nakano,H., Oshima,H., Chung,W., Williams-Abbott,L., Ware,C.F.,
            Yagita,H. and Okumura,K.
  TITLE     TRAF5, an activator of NF-kappaB and putative signal transducer for
            the lymphotoxin-beta receptor
  JOURNAL   J Biol Chem 271 (25), 14661-14664 (1996)
   PUBMED   8663299
REFERENCE   7  (residues 1 to 430)
  AUTHORS   Browning,J.L., Miatkowski,K., Sizing,I., Griffiths,D., Zafari,M.,
            Benjamin,C.D., Meier,W. and Mackay,F.
  TITLE     Signaling through the lymphotoxin beta receptor induces the death
            of some adenocarcinoma tumor lines
  JOURNAL   J Exp Med 183 (3), 867-878 (1996)
   PUBMED   8642291
REFERENCE   8  (residues 1 to 430)
  AUTHORS   Baens,M., Aerssens,J., van Zand,K., Van den Berghe,H. and
            Marynen,P.
  TITLE     Isolation and regional assignment of human chromosome 12p cDNAs
  JOURNAL   Genomics 29 (1), 44-52 (1995)
   PUBMED   8530100
REFERENCE   9  (residues 1 to 430)
  AUTHORS   Crowe,P.D., VanArsdale,T.L., Walter,B.N., Ware,C.F., Hession,C.,
            Ehrenfels,B., Browning,J.L., Din,W.S., Goodwin,R.G. and Smith,C.A.
  TITLE     A lymphotoxin-beta-specific receptor
  JOURNAL   Science 264 (5159), 707-710 (1994)
   PUBMED   8171323
REFERENCE   10 (residues 1 to 430)
  AUTHORS   Baens,M., Chaffanet,M., Cassiman,J.J., van den Berghe,H. and
            Marynen,P.
  TITLE     Construction and evaluation of a hncDNA library of human 12p
            transcribed sequences derived from a somatic cell hybrid
  JOURNAL   Genomics 16 (1), 214-218 (1993)
   PUBMED   8486360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005840.2.
            
            Summary: This gene encodes a member of the tumor necrosis factor
            receptor superfamily. The major ligands of this receptor include
            lymphotoxin alpha/beta and tumor necrosis factor ligand superfamily
            member 14. The encoded protein plays a role in signalling during
            the development of lymphoid and other organs, lipid metabolism,
            immune response, and programmed cell death. Activity of this
            receptor has also been linked to carcinogenesis. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2121337.1,
                                           SRR14038191.3349832.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..430
                     /product="tumor necrosis factor receptor superfamily
                     member 3 isoform 8 precursor"
                     /note="tumor necrosis factor C receptor; lymphotoxin B
                     receptor; tumor necrosis factor receptor type III;
                     lymphotoxin beta receptor (TNFR superfamily, member 3);
                     tumor necrosis factor receptor 2-related protein"
                     /calculated_mol_wt=43171
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3049
     CDS             1..430
                     /gene="LTBR"
                     /gene_synonym="D12S370; LT-BETA-R; TNF-R-III; TNFCR;
                     TNFR-RP; TNFR2-RP; TNFR3; TNFRSF3"
                     /coded_by="NM_001414308.1:198..1490"
                     /note="isoform 8 precursor is encoded by transcript
                     variant 8"
                     /db_xref="GeneID:4055"
                     /db_xref="HGNC:HGNC:6718"
                     /db_xref="MIM:600979"
ORIGIN      
        1 mllpwatsap glawgplvlg lfgllaasqp qavppyasen qtcrdqekey yepqhriccs
       61 rcppakcsri rdtvcatcae nsynehwnyl ticqlcrpcd pvmgleeiap ctskrktqcr
      121 cqpgmfcaaw alecthcell sdcppgteae lkdevgkgnn hcvpckaghf qntsspsarc
      181 qphtrcenqg lveaapgtaq sdttcknple plppemsgtm lmlavllpla fflllatvfs
      241 ciwkshpslc rklgsllkrr pqgegpnpva gsweppkahp yfpdlvqpll pisgdvspvs
      301 tglpaapvle agvpqqqspl dltrepqlep geqsqvahgt ngihvtggsm titgniyiyn
      361 gpvlggppgp gdlpatpepp ypipeegdpg ppglstphqe dgkawhlaet ehcgatpsnr
      421 gprnqfithd
//
LOCUS       NP_001427688            1249 aa            linear   PRI 21-NOV-2025
DEFINITION  collagen alpha-6(IV) chain isoform 6 precursor [Homo sapiens].
ACCESSION   NP_001427688 XP_047297772 XP_054182423
VERSION     NP_001427688.1
DBSOURCE    REFSEQ: accession NM_001440759.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1249)
  AUTHORS   O'Brien,A., Aw,W.Y., Tee,H.Y., Naegeli,K.M., Bademci,G., Tekin,M.,
            Arnos,K. and Pandya,A.
  TITLE     Confirmation of COL4A6 variants in X-linked nonsyndromic hearing
            loss and its clinical implications
  JOURNAL   Eur J Hum Genet 30 (1), 7-12 (2022)
   PUBMED   33840813
  REMARK    GeneRIF: Confirmation of COL4A6 variants in X-linked nonsyndromic
            hearing loss and its clinical implications.
REFERENCE   2  (residues 1 to 1249)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 1249)
  AUTHORS   Komori,T., Ono,M., Hara,E.S., Ueda,J., Nguyen,H.T.T., Nguyen,H.T.,
            Yonezawa,T., Maeba,T., Kimura-Ono,A., Takarada,T., Momota,R.,
            Maekawa,K., Kuboki,T. and Oohashi,T.
  TITLE     Type IV collagen alpha6 chain is a regulator of keratin 10 in
            keratinization of oral mucosal epithelium
  JOURNAL   Sci Rep 8 (1), 2612 (2018)
   PUBMED   29422532
  REMARK    GeneRIF: These findings indicate that alpha112:alpha556 (IV)
            network, which is the only network that includes the alpha6(IV)
            chain, is one regulator of KRT10 expression in keratinization of
            oral mucosal epithelium.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1249)
  AUTHORS   Holmes,D.F., Lu,Y., Starborg,T. and Kadler,K.E.
  TITLE     Collagen Fibril Assembly and Function
  JOURNAL   Curr Top Dev Biol 130, 107-142 (2018)
   PUBMED   29853175
  REMARK    Review article
REFERENCE   5  (residues 1 to 1249)
  AUTHORS   Naba,A., Pearce,O.M.T., Del Rosario,A., Ma,D., Ding,H., Rajeeve,V.,
            Cutillas,P.R., Balkwill,F.R. and Hynes,R.O.
  TITLE     Characterization of the Extracellular Matrix of Normal and Diseased
            Tissues Using Proteomics
  JOURNAL   J Proteome Res 16 (8), 3083-3091 (2017)
   PUBMED   28675934
REFERENCE   6  (residues 1 to 1249)
  AUTHORS   Ghebrehiwet,B., Peerschke,E.I., Hong,Y., Munoz,P. and Gorevic,P.D.
  TITLE     Short amino acid sequences derived from C1q receptor (C1q-R) show
            homology with the alpha chains of fibronectin and vitronectin
            receptors and collagen type IV
  JOURNAL   J Leukoc Biol 51 (6), 546-556 (1992)
   PUBMED   1377218
REFERENCE   7  (residues 1 to 1249)
  AUTHORS   Gupta,S., Batchu,R.B. and Datta,K.
  TITLE     Purification, partial characterization of rat kidney hyaluronic
            acid binding protein and its localization on the cell surface
  JOURNAL   Eur J Cell Biol 56 (1), 58-67 (1991)
   PUBMED   1724753
REFERENCE   8  (residues 1 to 1249)
  AUTHORS   Hernandez,M.R., Igoe,F. and Neufeld,A.H.
  TITLE     Extracellular matrix of the human optic nerve head
  JOURNAL   Am J Ophthalmol 102 (2), 139-148 (1986)
   PUBMED   2426947
REFERENCE   9  (residues 1 to 1249)
  AUTHORS   Glant,T.T., Hadhazy,C., Mikecz,K. and Sipos,A.
  TITLE     Appearance and persistence of fibronectin in cartilage. Specific
            interaction of fibronectin with collagen type II
  JOURNAL   Histochemistry 82 (2), 149-158 (1985)
   PUBMED   3997552
REFERENCE   10 (residues 1 to 1249)
  AUTHORS   Matsubara,T., Trueb,B., Fehr,K., Ruttner,J.R. and Odermatt,B.F.
  TITLE     The localization and secretion of type IV collagen in synovial
            capillaries by immunohistochemistry using a monoclonal antibody
            against human type IV collagen
  JOURNAL   Exp Cell Biol 52 (3), 159-169 (1984)
   PUBMED   6386565
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL034369.1, AL109943.18,
            AL136080.6 and AL031177.1.
            
            On or before May 28, 2025 this sequence version replaced
            XP_047297772.1, XP_054182423.1.
            
            Summary: This gene encodes one of the six subunits of type IV
            collagen, the major structural component of basement membranes.
            Like the other members of the type IV collagen gene family, this
            gene is organized in a head-to-head conformation with another type
            IV collagen gene, alpha 5 type IV collagen, so that the gene pair
            shares a common promoter. Deletions in the alpha 5 gene that extend
            into the alpha 6 gene result in diffuse leiomyomatosis accompanying
            the X-linked Alport syndrome caused by the deletion in the alpha 5
            gene. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3122906.1,
                                           SRR14038197.1316612.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2147975
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1249
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.3"
     Protein         1..1249
                     /product="collagen alpha-6(IV) chain isoform 6 precursor"
                     /note="collagen of basement membrane, alpha-6; collagen
                     IV, alpha-6 polypeptide; collagen alpha-6(IV) chain;
                     dJ889N15.4 (Collagen Alpha 6(IV)); collagen, type IV,
                     alpha 6"
                     /calculated_mol_wt=116486
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2472
     Region          23..46
                     /region_name="7S domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14031.3)"
     Region          <45..375
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          108..338
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14031.3)"
     Site            127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14031.3)"
     Region          <297..>548
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          404..473
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14031.3)"
     Region          486..881
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14031.3)"
     Region          515..517
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14031.3)"
     Region          <516..>751
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          560..562
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14031.3)"
     Region          <639..>872
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          892..947
                     /region_name="Collagen"
                     /note="Collagen triple helix repeat (20 copies);
                     pfam01391"
                     /db_xref="CDD:460189"
     Region          915..1099
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14031.3)"
     Region          <927..>1165
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          986..988
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14031.3)"
     CDS             1..1249
                     /gene="COL4A6"
                     /gene_synonym="CXDELq22.3; DELXq22.3; DFNX6"
                     /coded_by="NM_001440759.1:88..3837"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:1288"
                     /db_xref="HGNC:HGNC:2208"
                     /db_xref="MIM:303631"
ORIGIN      
        1 mlinklwlll vtlclteela aageksygkp cggqdcsgsc qcfpekgarg rpgpigiqgp
       61 tgpqgftgst glsglkgerg fpgllgpygp kgdkgpmgvp gflgingipg hpgqpgprgp
      121 pgldgcngtq gavgfpgpdg ypgllgppgl pgqkgskgdp vlapgsfkgm kgdpglpgld
      181 gitgpqgapg fpgavgpagp pglqgppgpp gplgpdgnmg lgfqgekgvk gdvglpgpag
      241 pppstgelef mgfpkgkkgs kgepgpkgfp gisgppgfpg lgttgekgek gekgipglpg
      301 prgpmgsegv qgppgqqgkk gtlgfpglng fqgiegqkgd iglpgpdvfi didgavisgn
      361 pgdpgvpglp glkgdegiqg lrgpsgvpgl palsgvpgal gpqgfpglkg dqgnpgrtti
      421 gaaglpgrdg lpgppgppgp pspefetetl hnkesgfpgl rgeqgpkgnl glkgikgdsg
      481 fcacdggvpn tgppgepgpp gpwgliglpg lkgargdrgs ggaqgpagap glvgplgpsg
      541 pkgkkgepil stiqgmpgdr gdsgsqgfrg vigepgkdgv pglpglpglp gdggqgfpge
      601 kglpglpgek ghpgppglpg nglpglpgpr glpgdkgkdg lpgqqglpgs kgitlpciip
      661 gsygpsgfpg tpgfpgpkgs rglpgtpgqp gssgskgepg spglvhlpel pgfpgprgek
      721 glpgfpglpg kdglpgmigs pglpgskgat gdifgaenga pgeqglqglt ghkgflgdsg
      781 lpglkgvhgk pgllgpkger gspgtpgqvg qpgtpgssgp ygikgksglp gapgfpgisg
      841 hpgkkgtrgk kgppgsivkk glpglkglpg npglvglkgs pgspgvaglp alsgpkgekg
      901 svgfvgfpgi pglpgipgtr glkgipgstg kmgpsgragt pgekgdrgnp gpvgipsprr
      961 pmsnlwlkgd kgsqgsagsn gfpgprgdkg eagrpgppgl pgapglpgii kgvsgkpgpp
     1021 gfmgirglpg lkgssgitgf pgmpgesgsq girgspglpg asglpglkgd ngqtveisgs
     1081 pgpkgqpges gfkgtkgrdg lignigfpgn kgedgkvgvs gdvglpgapg fpgvagmrge
     1141 pglpgssghq gaigplgspg ligpkgfpgf pglhglnglp gtkgthgtpg psitgvpgpa
     1201 glpgpkgekg ypgigigapg kpglrgqkgd rdfypgdkek yfkgspnqk
//
LOCUS       NP_001397854             375 aa            linear   PRI 21-NOV-2025
DEFINITION  pleckstrin homology domain-containing family A member 2 isoform 2
            [Homo sapiens].
ACCESSION   NP_001397854 XP_016869208
VERSION     NP_001397854.1
DBSOURCE    REFSEQ: accession NM_001410925.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Li,H., Hou,S., Wu,X., Nandagopal,S., Lin,F., Kung,S. and
            Marshall,A.J.
  TITLE     The tandem PH domain-containing protein 2 (TAPP2) regulates
            chemokine-induced cytoskeletal reorganization and malignant B cell
            migration
  JOURNAL   PLoS One 8 (2), e57809 (2013)
   PUBMED   23460911
  REMARK    GeneRIF: This study identified TAPP2 as a novel regulator of
            malignant B cell migration.
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Costantini,J.L., Cheung,S.M., Hou,S., Li,H., Kung,S.K.,
            Johnston,J.B., Wilkins,J.A., Gibson,S.B. and Marshall,A.J.
  TITLE     TAPP2 links phosphoinositide 3-kinase signaling to B-cell adhesion
            through interaction with the cytoskeletal protein utrophin:
            expression of a novel cell adhesion-promoting complex in B-cell
            leukemia
  JOURNAL   Blood 114 (21), 4703-4712 (2009)
   PUBMED   19786618
  REMARK    GeneRIF: These findings identify TAPP2 as a novel link between PI3K
            signaling and the cytoskeleton with potential relevance for
            leukemia progression.
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Nusbaum,C., Mikkelsen,T.S., Zody,M.C., Asakawa,S., Taudien,S.,
            Garber,M., Kodira,C.D., Schueler,M.G., Shimizu,A., Whittaker,C.A.,
            Chang,J.L., Cuomo,C.A., Dewar,K., FitzGerald,M.G., Yang,X.,
            Allen,N.R., Anderson,S., Asakawa,T., Blechschmidt,K., Bloom,T.,
            Borowsky,M.L., Butler,J., Cook,A., Corum,B., DeArellano,K.,
            DeCaprio,D., Dooley,K.T., Dorris,L. 3rd, Engels,R., Glockner,G.,
            Hafez,N., Hagopian,D.S., Hall,J.L., Ishikawa,S.K., Jaffe,D.B.,
            Kamat,A., Kudoh,J., Lehmann,R., Lokitsang,T., Macdonald,P.,
            Major,J.E., Matthews,C.D., Mauceli,E., Menzel,U., Mihalev,A.H.,
            Minoshima,S., Murayama,Y., Naylor,J.W., Nicol,R., Nguyen,C.,
            O'Leary,S.B., O'Neill,K., Parker,S.C., Polley,A., Raymond,C.K.,
            Reichwald,K., Rodriguez,J., Sasaki,T., Schilhabel,M., Siddiqui,R.,
            Smith,C.L., Sneddon,T.P., Talamas,J.A., Tenzin,P., Topham,K.,
            Venkataraman,V., Wen,G., Yamazaki,S., Young,S.K., Zeng,Q.,
            Zimmer,A.R., Rosenthal,A., Birren,B.W., Platzer,M., Shimizu,N. and
            Lander,E.S.
  TITLE     DNA sequence and analysis of human chromosome 8
  JOURNAL   Nature 439 (7074), 331-335 (2006)
   PUBMED   16421571
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Kimber,W.A., Deak,M., Prescott,A.R. and Alessi,D.R.
  TITLE     Interaction of the protein tyrosine phosphatase PTPL1 with the
            PtdIns(3,4)P2-binding adaptor protein TAPP1
  JOURNAL   Biochem J 376 (Pt 2), 525-535 (2003)
   PUBMED   14516276
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Dowler,S., Currie,R.A., Campbell,D.G., Deak,M., Kular,G.,
            Downes,C.P. and Alessi,D.R.
  TITLE     Identification of pleckstrin-homology-domain-containing proteins
            with novel phosphoinositide-binding specificities
  JOURNAL   Biochem J 351 (Pt 1), 19-31 (2000)
   PUBMED   11001876
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC067817.10, AC108863.4 and KF495718.1.
            
            On Aug 18, 2022 this sequence version replaced XP_016869208.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.4309436.1,
                                           SRR14038196.1944914.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.22"
     Protein         1..375
                     /product="pleckstrin homology domain-containing family A
                     member 2 isoform 2"
                     /note="tandem PH Domain containing protein-2; pleckstrin
                     homology domain-containing family A member 2; TAPP-2;
                     tandem PH domain-containing protein 2; PH
                     domain-containing family A member 2; pleckstrin homology
                     domain containing, family A (phosphoinositide binding
                     specific) member 2"
                     /calculated_mol_wt=41079
     Region          <1..69
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          142..257
                     /region_name="PH2_TAPP1_2"
                     /note="Tandem PH-domain-containing proteins 1 and 2
                     Pleckstrin homology (PH) domain, C-terminal repeat;
                     cd13271"
                     /db_xref="CDD:270090"
     Site            order(157,159..160,168,179,189..190,224)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270090"
     CDS             1..375
                     /gene="PLEKHA2"
                     /gene_synonym="TAPP2"
                     /coded_by="NM_001410925.1:139..1266"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS94287.1"
                     /db_xref="GeneID:59339"
                     /db_xref="HGNC:HGNC:14336"
                     /db_xref="MIM:607773"
ORIGIN      
        1 mgagavgalq ltyiskvsia tpkqkpktpf cfvinalsqr yflqandqkd mkdwvealnq
       61 askitvpkgg glpmttevlk slaappalek kpqvayktei iggvvvhtpi sqnggdgqeg
      121 sepgshtilr rsqsyiptsg crastgppli ksgycvkqgn vrkswkrrff alddfticyf
      181 kceqdreplr tiflkdvlkt heclvksgdl lmrdnlfeii tssrtfyvqa dspedmhswi
      241 keigaavqal kchpretsfs rsisltrpgs sslssgpnsi lcrgrpplee kkalckapsv
      301 asswqpwtpv pqagekllpp gdtsedslft prpgegsapg vlpssrirhr sepqhpkekp
      361 fmfnlddeni rtsdv
//
LOCUS       NP_001350845             725 aa            linear   PRI 21-NOV-2025
DEFINITION  transcriptional repressor CTCF isoform 3 [Homo sapiens].
ACCESSION   NP_001350845 XP_016878358
VERSION     NP_001350845.1
DBSOURCE    REFSEQ: accession NM_001363916.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 725)
  AUTHORS   Ma,D.B., Zhang,H., Wang,X.L. and Wu,Q.G.
  TITLE     METTL3 aggravates cell damage induced by Streptococcus pneumoniae
            via the NEAT1/CTCF/MUC19 axis
  JOURNAL   Kaohsiung J Med Sci 40 (8), 722-731 (2024)
   PUBMED   38757482
  REMARK    GeneRIF: METTL3 aggravates cell damage induced by Streptococcus
            pneumoniae via the NEAT1/CTCF/MUC19 axis.
REFERENCE   3  (residues 1 to 725)
  AUTHORS   Zhang,J., Hu,G., Lu,Y., Ren,H., Huang,Y., Wen,Y., Ji,B., Wang,D.,
            Wang,H., Liu,H., Ma,N., Zhang,L., Pan,G., Qu,Y., Wang,H., Zhang,W.,
            Miao,Z. and Yao,H.
  TITLE     CTCF mutation at R567 causes developmental disorders via 3D genome
            rearrangement and abnormal neurodevelopment
  JOURNAL   Nat Commun 15 (1), 5524 (2024)
   PUBMED   38951485
  REMARK    GeneRIF: CTCF mutation at R567 causes developmental disorders via
            3D genome rearrangement and abnormal neurodevelopment.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 725)
  AUTHORS   Pandey,A., Kakani,P. and Shukla,S.
  TITLE     CTCF and BORIS-mediated autophagy regulation via alternative
            splicing of BNIP3L in breast cancer
  JOURNAL   J Biol Chem 300 (7), 107416 (2024)
   PUBMED   38810696
  REMARK    GeneRIF: CTCF and BORIS-mediated autophagy regulation via
            alternative splicing of BNIP3L in breast cancer.
REFERENCE   5  (residues 1 to 725)
  AUTHORS   He,T., You,M., Zhu,H., Chen,P. and Fang,S.
  TITLE     CCCTC-binding factor suppresses alpha-2-macroglobulin transcription
            to improve vascular endothelial cell functions in lower extremity
            arteriosclerosis obliterans
  JOURNAL   Gen Physiol Biophys 43 (3), 231-242 (2024)
   PUBMED   38774923
  REMARK    GeneRIF: CCCTC-binding factor suppresses alpha-2-macroglobulin
            transcription to improve vascular endothelial cell functions in
            lower extremity arteriosclerosis obliterans.
REFERENCE   6  (residues 1 to 725)
  AUTHORS   Bell,A.C., West,A.G. and Felsenfeld,G.
  TITLE     The protein CTCF is required for the enhancer blocking activity of
            vertebrate insulators
  JOURNAL   Cell 98 (3), 387-396 (1999)
   PUBMED   10458613
REFERENCE   7  (residues 1 to 725)
  AUTHORS   Filippova,G.N., Lindblom,A., Meincke,L.J., Klenova,E.M.,
            Neiman,P.E., Collins,S.J., Doggett,N.A. and Lobanenkov,V.V.
  TITLE     A widely expressed transcription factor with multiple DNA sequence
            specificity, CTCF, is localized at chromosome segment 16q22.1
            within one of the smallest regions of overlap for common deletions
            in breast and prostate cancers
  JOURNAL   Genes Chromosomes Cancer 22 (1), 26-36 (1998)
   PUBMED   9591631
REFERENCE   8  (residues 1 to 725)
  AUTHORS   Vostrov,A.A. and Quitschke,W.W.
  TITLE     The zinc finger protein CTCF binds to the APBbeta domain of the
            amyloid beta-protein precursor promoter. Evidence for a role in
            transcriptional activation
  JOURNAL   J Biol Chem 272 (52), 33353-33359 (1997)
   PUBMED   9407128
REFERENCE   9  (residues 1 to 725)
  AUTHORS   Filippova,G.N., Fagerlie,S., Klenova,E.M., Myers,C., Dehner,Y.,
            Goodwin,G., Neiman,P.E., Collins,S.J. and Lobanenkov,V.V.
  TITLE     An exceptionally conserved transcriptional repressor, CTCF, employs
            different combinations of zinc fingers to bind diverged promoter
            sequences of avian and mammalian c-myc oncogenes
  JOURNAL   Mol Cell Biol 16 (6), 2802-2813 (1996)
   PUBMED   8649389
REFERENCE   10 (residues 1 to 725)
  AUTHORS   Valverde de Morales,H.G., Wang,H.L., Garber,K., Corces,V. and Li,H.
  TITLE     CTCF-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   38662876
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027682.10 and AC009095.7.
            
            On Jun 3, 2018 this sequence version replaced XP_016878358.1.
            
            Summary: This gene is a member of the BORIS + CTCF gene family and
            encodes a transcriptional regulator protein with 11 highly
            conserved zinc finger (ZF) domains. This nuclear protein is able to
            use different combinations of the ZF domains to bind different DNA
            target sequences and proteins. Depending upon the context of the
            site, the protein can bind a histone acetyltransferase
            (HAT)-containing complex and function as a transcriptional
            activator or bind a histone deacetylase (HDAC)-containing complex
            and function as a transcriptional repressor. If the protein is
            bound to a transcriptional insulator element, it can block
            communication between enhancers and upstream promoters, thereby
            regulating imprinted expression. Mutations in this gene have been
            associated with invasive breast cancers, prostate cancers, and
            Wilms' tumors. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2010].
            
            Sequence Note:.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.765999.1,
                                           SRR1803617.216220.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2149876
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..725
                     /product="transcriptional repressor CTCF isoform 3"
                     /note="transcriptional repressor CTCF; CTCFL paralog;
                     11-zinc finger protein; 11 zinc finger transcriptional
                     repressor; CCCTC-binding factor (zinc finger protein)"
                     /calculated_mol_wt=82483
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P49711.1)"
     Region          180..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49711.1)"
     Region          266..289
                     /region_name="zf-H2C2_5"
                     /note="C2H2-type zinc-finger domain; pfam13909"
                     /db_xref="CDD:404746"
     Region          268..288
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(273,275,277,279..280,283..284,287,301,303,307..308,
                     311..312,315,329,331,333,335..336,339..340,346)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          280..305
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P49711.1)"
     Region          296..316
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          309..333
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P49711.1)"
     Region          324..347
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          351..375
                     /region_name="zf-H2C2_5"
                     /note="C2H2-type zinc-finger domain; pfam13909"
                     /db_xref="CDD:404746"
     Region          353..373
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <366..500
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P49711.1)"
     Region          381..401
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P49711.1)"
     Region          409..426
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          439..457
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          469..489
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(474,476,478,480..481,484..485,488,502,504,508..509,
                     512..513,516,530,532,534,536..537,540..541,545)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          497..517
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          509..534
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          525..546
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          557..573
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            609
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P49711.1)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P49711.1)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P49711.1)"
     Region          687..715
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49711.1)"
     CDS             1..725
                     /gene="CTCF"
                     /gene_synonym="CFAP108; FAP108; MRD21"
                     /coded_by="NM_001363916.2:205..2382"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS86536.1"
                     /db_xref="GeneID:10664"
                     /db_xref="HGNC:HGNC:13723"
                     /db_xref="MIM:604167"
ORIGIN      
        1 megdaveaiv eesetfikgk erktyqrrre ggqeedachl pqnqtdggev vqdvnssvqm
       61 vmmeqldptl lqmktevmeg tvapeaeaav ddtqiitlqv vnmeeqpini gelqlvqvpv
      121 pvtvpvatts veelqgayen evskeglaes epmichtlpl pegfqvvkvg angevetleq
      181 gelppqedps wqkdpdyqpp akktkktkks klryteegkd vdvsvydfee eqqegllsev
      241 naekvvgnmk ppkptkikkk gvkktfqcel csytcprrsn ldrhmkshtd erphkchlcg
      301 rafrtvtllr nhlnthtgtr phkcpdcdma fvtsgelvrh rrykhthekp fkcsmcdyas
      361 vevsklkrhi rshtgerpfq cslcsyasrd tyklkrhmrt hsgekpyecy icharftqsg
      421 tmkmhilqkh tenvakfhcp hcdtviarks dlgvhlrkqh syieqgkkcr ycdavfhery
      481 aliqhqkshk nekrfkcdqc dyacrqerhm imhkrthtge kpyacshcdk tfrqkqlldm
      541 hfkryhdpnf vpaafvcskc gktftrrntm arhadncagp dgvegengge tkkskrgrkr
      601 kmrskkedss dsenaepdld dnedeeepav eiepepepqp vtpapppakk rrgrppgrtn
      661 qpkqnqpiiq vedqntgaie niivevkkep daepaegeee eaqpaatdap ngdltpemil
      721 smmdr
//
LOCUS       NP_001427347             250 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 8 precursor [Homo
            sapiens].
ACCESSION   NP_001427347
VERSION     NP_001427347.1
DBSOURCE    REFSEQ: accession NM_001440418.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 250)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 250)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 250)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3 and AP004147.3.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN03465404
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..250
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     8 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=25325
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..>230
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     CDS             1..250
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440418.1:296..1048"
                     /note="isoform 8 precursor is encoded by transcript
                     variant 20"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk vgaslspppp
      241 aelhpppslp
//
LOCUS       NP_001394265             281 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 35 [Homo sapiens].
ACCESSION   NP_001394265 XP_047288960
VERSION     NP_001394265.1
DBSOURCE    REFSEQ: accession NM_001407336.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            On May 31, 2022 this sequence version replaced XP_047288960.1.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1069804.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..281
                     /product="tropomyosin alpha-1 chain isoform 35"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=32463
     Region          48..280
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..281
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407336.1:84..929"
                     /note="isoform 35 is encoded by transcript variant 35"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle ediaakekll rvsederdrv
       61 leelhkaeds llaaeeaaak aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegqv rqleeqlrim dqtlkalmaa edkysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledql yqqleqnrrl tnelklalne d
//
LOCUS       NP_001338319             549 aa            linear   PRI 21-NOV-2025
DEFINITION  dystrobrevin beta isoform 24 [Homo sapiens].
ACCESSION   NP_001338319
VERSION     NP_001338319.1
DBSOURCE    REFSEQ: accession NM_001351390.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Prokopenko,D., Lee,S., Hecker,J., Mullin,K., Morgan,S.,
            Katsumata,Y., Weiner,M.W., Fardo,D.W., Laird,N., Bertram,L.,
            Hide,W., Lange,C. and Tanzi,R.E.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative (ADNI)
  TITLE     Region-based analysis of rare genomic variants in whole-genome
            sequencing datasets reveal two novel Alzheimer's disease-associated
            genes: DTNB and DLG2
  JOURNAL   Mol Psychiatry 27 (4), 1963-1969 (2022)
   PUBMED   35246634
  REMARK    GeneRIF: Region-based analysis of rare genomic variants in
            whole-genome sequencing datasets reveal two novel Alzheimer's
            disease-associated genes: DTNB and DLG2.
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Piluso,G., Mirabella,M., Ricci,E., Belsito,A., Abbondanza,C.,
            Servidei,S., Puca,A.A., Tonali,P., Puca,G.A. and Nigro,V.
  TITLE     Gamma1- and gamma2-syntrophins, two novel dystrophin-binding
            proteins localized in neuronal cells
  JOURNAL   J Biol Chem 275 (21), 15851-15860 (2000)
   PUBMED   10747910
REFERENCE   7  (residues 1 to 549)
  AUTHORS   Blake,D.J., Hawkes,R., Benson,M.A. and Beesley,P.W.
  TITLE     Different dystrophin-like complexes are expressed in neurons and
            glia
  JOURNAL   J Cell Biol 147 (3), 645-658 (1999)
   PUBMED   10545507
REFERENCE   8  (residues 1 to 549)
  AUTHORS   Puca,A.A., Nigro,V., Piluso,G., Belsito,A., Sampaolo,S.,
            Quaderi,N., Rossi,E., Di Iorio,G., Ballabio,A. and Franco,B.
  TITLE     Identification and characterization of a novel member of the
            dystrobrevin gene family
  JOURNAL   FEBS Lett 425 (1), 7-13 (1998)
   PUBMED   9540997
REFERENCE   9  (residues 1 to 549)
  AUTHORS   Peters,M.F., O'Brien,K.F., Sadoulet-Puccio,H.M., Kunkel,L.M.,
            Adams,M.E. and Froehner,S.C.
  TITLE     beta-dystrobrevin, a new member of the dystrophin family.
            Identification, cloning, and protein associations
  JOURNAL   J Biol Chem 272 (50), 31561-31569 (1997)
   PUBMED   9395493
REFERENCE   10 (residues 1 to 549)
  AUTHORS   Straub,V. and Campbell,K.P.
  TITLE     Muscular dystrophies and the dystrophin-glycoprotein complex
  JOURNAL   Curr Opin Neurol 10 (2), 168-175 (1997)
   PUBMED   9146999
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010150.3, AC019144.9,
            AC104699.2 and AC012074.9.
            
            Summary: This gene encodes dystrobrevin beta, a component of the
            dystrophin-associated protein complex (DPC). The DPC consists of
            dystrophin and several integral and peripheral membrane proteins,
            including dystroglycans, sarcoglycans, syntrophins and dystrobrevin
            alpha and beta. The DPC localizes to the sarcolemma and its
            disruption is associated with various forms of muscular dystrophy.
            Dystrobrevin beta is thought to interact with syntrophin and the
            DP71 short form of dystrophin. [provided by RefSeq, Mar 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.199587.1,
                                           SRR1803616.265312.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..549
                     /product="dystrobrevin beta isoform 24"
                     /note="DTN-B; beta-dystrobrevin"
                     /calculated_mol_wt=62411
     Region          54..214
                     /region_name="EFh_DTN"
                     /note="EF-hand-like motif found in dystrobrevins and
                     similar proteins; cd16244"
                     /db_xref="CDD:320002"
     Region          54..95
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320002"
     Region          104..138
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320002"
     Region          144..180
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320002"
     Region          191..214
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320002"
     Region          241..289
                     /region_name="ZZ_dystrophin"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     dystrophin and dystrobrevin. The ZZ motif coordinates two
                     zinc ions and most likely participates in ligand binding
                     or molecular scaffolding. Dystrophin attaches actin
                     filaments to an integral membrane...; cd02334"
                     /db_xref="CDD:239074"
     Site            order(243,246,258,261,267,270,280,284)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(243,246,267,270)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(244,255,257,263,265)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(256,271,286,289)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(258,261,280,284)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239074"
     Region          <370..>519
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     CDS             1..549
                     /gene="DTNB"
                     /coded_by="NM_001351390.2:194..1843"
                     /note="isoform 24 is encoded by transcript variant 24"
                     /db_xref="GeneID:1838"
                     /db_xref="HGNC:HGNC:3058"
                     /db_xref="MIM:602415"
ORIGIN      
        1 mieesgnkrk tmaekrqlfi emraqnfdvi rlstyrtack lrfvqkrcnl hlvdiwnmie
       61 afrdnglntl dhtteisvsr letvissiyy qlnkrlpsth qisveqsisl llnfmiaayd
      121 segrgkltvf svkamlatmc ggkmldklry vfsqmsdsng lmifskfdqf lkevlklpta
      181 vfegpsfgyt ehsvrtcfpq qrkimlnmfl dtmmadpppq clvwlplmhr lahvenvfhp
      241 vecsycrces mmgfryrcqq chnyqlcqnc fwrghaggph snqhqmkehs swkspakkls
      301 haiskslgcv ptrepphpvf peqpekpldl ahivpprplt nmndtmvshm ssgvptptks
      361 vldspsrlde ehrliaryaa rlaaeagnvt rpptdlsfnf dankqqrqli aelenknrei
      421 lqeiqrlrle heqasqptpe kaqqnptlla elrllrqrkd eleqrmsalq esrrelmvql
      481 eelmkllkee eqkqaaqatg sphtspthgg grpmpmpvrs tsagstpthc pqdslsgvgg
      541 dvqeafaqg
//
LOCUS       NP_001400239             275 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 15 [Homo sapiens].
ACCESSION   NP_001400239
VERSION     NP_001400239.1
DBSOURCE    REFSEQ: accession NM_001413310.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.159668.1,
                                           SRR1803616.241806.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..275
                     /product="RNA-binding Raly-like protein isoform 15"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=30046
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          183..>228
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     CDS             1..275
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413310.1:329..1156"
                     /note="isoform 15 is encoded by transcript variant 37"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly rleskepfls
      121 vglfdyhgrv ppppravipl krprvavttt rrgkgvfsmk ggsrstasgs tgsklksdel
      181 qtikkeltqi ktkidsllgr lekiekqqka eaeaqkkqle eslvliqeec vseiadhste
      241 epaeggpdad geemtdgiee dfdedgghel flqik
//
LOCUS       NP_001394764            1109 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 20 [Homo
            sapiens].
ACCESSION   NP_001394764
VERSION     NP_001394764.1
DBSOURCE    REFSEQ: accession NM_001407835.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1109)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1109)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1109)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1109)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1109)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1109)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1109)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.3339024.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1109
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 20"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=125307
     Region          153..182
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          188..215
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          324..596
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          723..1109
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1109
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407835.1:575..3904"
                     /note="isoform 20 is encoded by transcript variant 20"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 mgakdatpvp cgrwakilek dkrtqqmrmq rlkaklqmpf qsgefkaltr rlqveprlls
       61 kqmagcledc trqapespwe eqlarllqea pgklsldveq apsgqhsqaq lsgqqqrlla
      121 ffkcclltdq lplahhllvv hhgqrqkrkl ltldmynavm lgwarqgafk elvyvlfmvk
      181 dagltpdlls yaaalqcmgr qdqdagtier cleqmsqegl klqalftavl lseedratvl
      241 kavhkvkptf slppqlpppv ntskllrdvy akdgrvsypk lhlplktlqc lfekqlhmel
      301 asrvcvvsve kptlpskevk harktlktlr dqwekalcra lretknrler evyegrfsly
      361 pflclldere vvrmllqvlq alpaqgesft tlarelsart fsrhvvqrqr vsgqvqalqn
      421 hyrkylclla sdaevpepcl prqyweelga pealreqpwp lpvqmelgkl laemlvqatq
      481 mpcsldkphr ssrlvpvlyh vysfrnvqqi gilkphpayv qllekaaept ltfeavdvpm
      541 lcpplpwtsp hsgafllspt klmrtvegat qhqelletcp ptalhgalda ltqlgncawr
      601 vngrvldlvl qlfqakgcpq lgvpappsea pqppeahlph saaparkael rrelahcqkv
      661 aremhslrae alyrlslaqh lrdrvfwlph nmdfrgrtyp cpphfnhlgs dvarallefa
      721 qgrplgphgl dwlkihlvnl tglkkreplr krlafaeevm ddildsadqp ltgrkwwmga
      781 eepwqtlacc mevanavras dpaayvshlp vhqdgscngl qhyaalgrds vgaasvnlep
      841 sdvpqdvysg vaaqvevfrr qdaqrgmrva qvlegfitrk vvkqtvmtvv ygvtryggrl
      901 qiekrlrels dfpqvfkslq emfsgtraiq hwltesarli shmgsvvewv tplgvpviqp
      961 yrldskvkqi gggiqsityt hngdisrkpn trkqkngfpp nfihsldssh mmltalhcyr
     1021 kgltfvsvhd cywthaadvs vmnqvcreqf vrlhsepilq dlsrflvkrf csepqkilea
     1081 sqlketlqav pkpgafdleq vkrstyffs
//
LOCUS       NP_001392812             682 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 10 [Homo sapiens].
ACCESSION   NP_001392812
VERSION     NP_001392812.1
DBSOURCE    REFSEQ: accession NM_001405883.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 682)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 682)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 682)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 682)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 682)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 682)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 682)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 682)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1131318.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..682
                     /product="KAT8 regulatory NSL complex subunit 1 isoform
                     10"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=75478
     Region          462..582
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..682
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405883.1:139..2187"
                     /note="isoform 10 is encoded by transcript variant 24"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 mllgcllrrr rsewkwaadr aaivsrwnwl qahvsdleyr irqqtdiykq irankglivl
       61 gevpppehtt dlflplssev ktdhgtdkli esvsqplenh gapiighise slstkscgal
      121 rpvngvintl qpvladhipg dssdaeeqlh kkqrlnlvss ssdgtcvaar trpvlsckkr
      181 rlvrpnsivp lskkvhrnst irpgcdvnps calcgsgsin tmppeihyea pllerlsqld
      241 scvhpvlafp ddvptslhfq smlksqwqnk pfdkikppkk lslkhrapmp gslpdsarkd
      301 rhklvssflt taklshhqtr pdrthrqhld dvgavpmver vtapkaerll nppppvhdpn
      361 hskmrlrdhs sersevlkhh tdmssssyla athhpphspl vrqlstssds papassssqv
      421 tastsqpvrr rrgessfdin nivipmsvaa ttrveklqyk eiltpswrev dlqslkgspd
      481 eeneeiedls daafaalhak ceemerarwl wttsvppqrr gsrsyrssdg rttpqlgsan
      541 pstpqpaspd vssshslsey shgqsprspi spelhsaplt pvardtprhl asedtrcstp
      601 elgldeqsvq pwerrtfpla hspqaecedq ldaqeraarc trrtsgsktg reteaaptsp
      661 pivplksrhl vaaataqrpt hr
//
LOCUS       NP_001427353             669 aa            linear   PRI 21-NOV-2025
DEFINITION  interleukin-12 receptor subunit beta-1 isoform 5 precursor [Homo
            sapiens].
ACCESSION   NP_001427353 XP_047294727 XP_054176856
VERSION     NP_001427353.1
DBSOURCE    REFSEQ: accession NM_001440424.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Chen,H., Ge,X., Li,C., Zeng,J. and Wang,X.
  TITLE     Structure and assembly of the human IL-12 signaling complex
  JOURNAL   Structure 32 (10), 1640-1651 (2024)
   PUBMED   39111304
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Huang,J., He,Q., Huang,L., Liu,L., Yang,P. and Chen,M.
  TITLE     Discovering the link between IL12RB1 gene polymorphisms and
            tuberculosis susceptibility: a comprehensive meta-analysis
  JOURNAL   Front Public Health 12, 1249880 (2024)
   PUBMED   38317798
  REMARK    GeneRIF: Discovering the link between IL12RB1 gene polymorphisms
            and tuberculosis susceptibility: a comprehensive meta-analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Rosas Mejia,O., Claeys,T.A., Williams,A., Zafar,A. and
            Robinson,R.T.
  TITLE     IL12RB1 allele bias in human TH cells is regulated by functional
            SNPs in its 3'UTR
  JOURNAL   Cytokine 158, 155993 (2022)
   PUBMED   36007427
  REMARK    GeneRIF: IL12RB1 allele bias in human TH cells is regulated by
            functional SNPs in its 3'UTR.
REFERENCE   4  (residues 1 to 669)
  AUTHORS   Khattak,F.A., Akbar,N.U., Riaz,M., Hussain,M., Rehman,K., Khan,S.N.
            and Khan,T.A.
  TITLE     Novel IL-12Rbeta1 deficiency-mediates recurrent cutaneous
            leishmaniasis
  JOURNAL   Int J Infect Dis 112, 338-345 (2021)
   PUBMED   34438084
  REMARK    GeneRIF: Novel IL-12Rbeta1 deficiency-mediates recurrent cutaneous
            leishmaniasis.
REFERENCE   5  (residues 1 to 669)
  AUTHORS   Yamamoto,K., Kobayashi,H., Miura,O., Hirosawa,S. and Miyasaka,N.
  TITLE     Assignment of IL12RB1 and IL12RB2, interleukin-12 receptor beta 1
            and beta 2 chains, to human chromosome 19 band p13.1 and chromosome
            1 band p31.2, respectively, by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 77 (3-4), 257-258 (1997)
   PUBMED   9284929
REFERENCE   6  (residues 1 to 669)
  AUTHORS   Bacon,C.M., Petricoin,E.F. 3rd, Ortaldo,J.R., Rees,R.C.,
            Larner,A.C., Johnston,J.A. and O'Shea,J.J.
  TITLE     Interleukin 12 induces tyrosine phosphorylation and activation of
            STAT4 in human lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 92 (16), 7307-7311 (1995)
   PUBMED   7638186
REFERENCE   7  (residues 1 to 669)
  AUTHORS   Bacon,C.M., McVicar,D.W., Ortaldo,J.R., Rees,R.C., O'Shea,J.J. and
            Johnston,J.A.
  TITLE     Interleukin 12 (IL-12) induces tyrosine phosphorylation of JAK2 and
            TYK2: differential use of Janus family tyrosine kinases by IL-2 and
            IL-12
  JOURNAL   J Exp Med 181 (1), 399-404 (1995)
   PUBMED   7528775
REFERENCE   8  (residues 1 to 669)
  AUTHORS   Ling,P., Gately,M.K., Gubler,U., Stern,A.S., Lin,P., Hollfelder,K.,
            Su,C., Pan,Y.C. and Hakimi,J.
  TITLE     Human IL-12 p40 homodimer binds to the IL-12 receptor but does not
            mediate biologic activity
  JOURNAL   J Immunol 154 (1), 116-127 (1995)
   PUBMED   7527811
REFERENCE   9  (residues 1 to 669)
  AUTHORS   Gillessen,S., Carvajal,D., Ling,P., Podlaski,F.J., Stremlo,D.L.,
            Familletti,P.C., Gubler,U., Presky,D.H., Stern,A.S. and Gately,M.K.
  TITLE     Mouse interleukin-12 (IL-12) p40 homodimer: a potent IL-12
            antagonist
  JOURNAL   Eur J Immunol 25 (1), 200-206 (1995)
   PUBMED   7843232
REFERENCE   10 (residues 1 to 669)
  AUTHORS   Chua,A.O., Chizzonite,R., Desai,B.B., Truitt,T.P., Nunes,P.,
            Minetti,L.J., Warrier,R.R., Presky,D.H., Levine,J.F., Gately,M.K.
            et al.
  TITLE     Expression cloning of a human IL-12 receptor component. A new
            member of the cytokine receptor superfamily with strong homology to
            gp130
  JOURNAL   J Immunol 153 (1), 128-136 (1994)
   PUBMED   7911493
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020904.7.
            
            On or before May 20, 2025 this sequence version replaced
            XP_047294727.1, XP_054176856.1.
            
            Summary: The protein encoded by this gene is a type I transmembrane
            protein that belongs to the hemopoietin receptor superfamily. This
            protein binds to interleukine 12 (IL12) with a low affinity, and is
            thought to be a part of IL12 receptor complex. This protein forms a
            disulfide-linked oligomer, which is required for its IL12 binding
            activity. The coexpression of this and IL12RB2 proteins was shown
            to lead to the formation of high-affinity IL12 binding sites and
            reconstitution of IL12 dependent signaling. Mutations in this gene
            impair the development of interleukin-17-producing T lymphocytes
            and result in increased susceptibility to mycobacterial and
            Salmonella infections. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1862957.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..669
                     /product="interleukin-12 receptor subunit beta-1 isoform 5
                     precursor"
                     /note="IL-12 receptor beta component; interleukin-12
                     receptor beta-1 chain; IL-12R subunit beta-1; IL-12
                     receptor subunit beta-1; cluster of differentiation 212;
                     interleukin 12 receptor, beta 1"
                     /calculated_mol_wt=71192
     sig_peptide     1..23
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
                     /calculated_mol_wt=2601
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
     Region          222..226
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P42701.1)"
     Site            336
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
     Site            353
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
     Site            359
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
     Site            449
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
     Region          454..544
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            463
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
     Site            order(535..536,538..539)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            553..577
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P42701.1)"
     Region          584..592
                     /region_name="Box 1 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P42701.1)"
     Region          633..655
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42701.1)"
     CDS             1..669
                     /gene="IL12RB1"
                     /gene_synonym="CD212; IL-12R-BETA1; IL12RB; IMD30"
                     /coded_by="NM_001440424.1:112..2121"
                     /note="isoform 5 precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:3594"
                     /db_xref="HGNC:HGNC:5971"
                     /db_xref="MIM:601604"
ORIGIN      
        1 meplvtwvvp llflfllsrq gaacrtsecc fqdppypdad sgsasgprdl rcyrissdry
       61 ecswqyegpt agvshflrcc lssgrccyfa agsatrlqfs dqagvsvlyt vtlwveswar
      121 nqtekspevt lqlynsvkye pplgdikvsk lagqlrmewe tpdnqvgaev qfrhrtpssp
      181 wklgdcgpqd ddtesclcpl emnvaqefql rrrqlgsqgs swskwsspvc vppvglvlia
      241 enppqpqvrf sveqlgqdgr rrltlkeqpt qlelpegcqg lapgtevtyr lqlhmlscpc
      301 kakatrtlhl gkmpylsgaa ynvavissnq fgpglnqtwh ipadthtepv alnisvgtng
      361 ttmywparaq smtyciewqp vgqdgglatc sltapqdpdp agmatyswsr esgamgqekc
      421 yyitifasah pekltlwstv lstyhfggna saagtphhvs vknhsldsvs vdwapsllst
      481 cpgvlkeyvv rcrdedskqv sehpvqptet qvtlsglrag vaytvqvrad tawlrgvwsq
      541 pqrfsievqv sdwliffasl gsflsillvg vlgylglnra arhlcpplpt pcassaiefp
      601 ggketwqwin pvdfqeeasl qealvvemsw dkgerteple ktelpegape laldtelsle
      661 dgdrckakm
//
LOCUS       NP_001425259            1170 aa            linear   PRI 21-NOV-2025
DEFINITION  centrosome and spindle pole-associated protein 1 isoform 9 [Homo
            sapiens].
ACCESSION   NP_001425259 XP_047278208
VERSION     NP_001425259.1
DBSOURCE    REFSEQ: accession NM_001438330.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1170)
  AUTHORS   van den Berg,C.M., Volkov,V.A., Schnorrenberg,S., Huang,Z.,
            Stecker,K.E., Grigoriev,I., Gilani,S., Frikstad,K.M., Patzke,S.,
            Zimmermann,T., Dogterom,M. and Akhmanova,A.
  TITLE     CSPP1 stabilizes growing microtubule ends and damaged lattices from
            the luminal side
  JOURNAL   J Cell Biol 222 (4) (2023)
   PUBMED   36752787
  REMARK    GeneRIF: CSPP1 stabilizes growing microtubule ends and damaged
            lattices from the luminal side.
REFERENCE   2  (residues 1 to 1170)
  AUTHORS   Odabasi,E., Conkar,D., Deretic,J., Batman,U., Frikstad,K.M.,
            Patzke,S. and Firat-Karalar,E.N.
  TITLE     CCDC66 regulates primary cilium length and signaling via
            interactions with transition zone and axonemal proteins
  JOURNAL   J Cell Sci 136 (3) (2023)
   PUBMED   36606424
REFERENCE   3  (residues 1 to 1170)
  AUTHORS   Zhang,L., Yang,S.T., Wang,C., Zhang,L.C., Zhang,X., Li,F.C.,
            Wang,S.Y. and Ma,K.
  TITLE     Circle RNA circCSPP1 promotes human osteosarcoma cell proliferation
            and increases glucose metabolism by suppressing miR-200c maturation
  JOURNAL   Hum Exp Toxicol 41, 9603271221097364 (2022)
   PUBMED   35713481
  REMARK    GeneRIF: Circle RNA circCSPP1 promotes human osteosarcoma cell
            proliferation and increases glucose metabolism by suppressing
            miR-200c maturation.
REFERENCE   4  (residues 1 to 1170)
  AUTHORS   Latour,B.L., Van De Weghe,J.C., Rusterholz,T.D., Letteboer,S.J.,
            Gomez,A., Shaheen,R., Gesemann,M., Karamzade,A., Asadollahi,M.,
            Barroso-Gil,M., Chitre,M., Grout,M.E., van Reeuwijk,J., van
            Beersum,S.E., Miller,C.V., Dempsey,J.C., Morsy,H., Bamshad,M.J.,
            Nickerson,D.A., Neuhauss,S.C., Boldt,K., Ueffing,M.,
            Keramatipour,M., Sayer,J.A., Alkuraya,F.S., Bachmann-Gagescu,R.,
            Roepman,R. and Doherty,D.
  CONSRTM   University of Washington Center for Mendelian Genomics; Genomics
            England Research Consortium
  TITLE     Dysfunction of the ciliary ARMC9/TOGARAM1 protein module causes
            Joubert syndrome
  JOURNAL   J Clin Invest 130 (8), 4423-4439 (2020)
   PUBMED   32453716
REFERENCE   5  (residues 1 to 1170)
  AUTHORS   Xue,Y.F., Li,M., Li,W., Lin,Q., Yu,B.X., Zhu,Q.B. and Chen,H.J.
  TITLE     Roles of circ-CSPP1 on the proliferation and metastasis of glioma
            cancer
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (10), 5519-5525 (2020)
   PUBMED   32495924
  REMARK    GeneRIF: Roles of circ-CSPP1 on the proliferation and metastasis of
            glioma cancer.
REFERENCE   6  (residues 1 to 1170)
  AUTHORS   Patzke,S., Redick,S., Warsame,A., Murga-Zamalloa,C.A., Khanna,H.,
            Doxsey,S. and Stokke,T.
  TITLE     CSPP is a ciliary protein interacting with Nephrocystin 8 and
            required for cilia formation
  JOURNAL   Mol Biol Cell 21 (15), 2555-2567 (2010)
   PUBMED   20519441
  REMARK    GeneRIF: CSPP isoforms require their common C-terminal domain to
            interact with Nephrocystin 8 (NPHP8/RPGRIP1L) and to form a ternary
            complex with NPHP8 and NPHP4.
REFERENCE   7  (residues 1 to 1170)
  AUTHORS   Asiedu,M., Wu,D., Matsumura,F. and Wei,Q.
  TITLE     Centrosome/spindle pole-associated protein regulates cytokinesis
            via promoting the recruitment of MyoGEF to the central spindle
  JOURNAL   Mol Biol Cell 20 (5), 1428-1440 (2009)
   PUBMED   19129481
  REMARK    GeneRIF: CSPP interacts with and recruits MyoGEF to the central
            spindle, where MyoGEF contributes to the spatiotemporal regulation
            of cytokinesis.
REFERENCE   8  (residues 1 to 1170)
  AUTHORS   Patzke,S., Stokke,T. and Aasheim,H.C.
  TITLE     CSPP and CSPP-L associate with centrosomes and microtubules and
            differently affect microtubule organization
  JOURNAL   J Cell Physiol 209 (1), 199-210 (2006)
   PUBMED   16826565
  REMARK    GeneRIF: Taken together, CSPP and CSPP-L interact with centrosomes
            and microtubules and can differently affect microtubule
            organization.
REFERENCE   9  (residues 1 to 1170)
  AUTHORS   Patzke,S., Hauge,H., Sioud,M., Finne,E.F., Sivertsen,E.A.,
            Delabie,J., Stokke,T. and Aasheim,H.C.
  TITLE     Identification of a novel centrosome/microtubule-associated
            coiled-coil protein involved in cell-cycle progression and spindle
            organization
  JOURNAL   Oncogene 24 (7), 1159-1173 (2005)
   PUBMED   15580290
  REMARK    GeneRIF: Novel centrosome/microtubule-associated coiled-coil
            protein (CSPP)is associated with centrosomes and microtubules and
            may play a role in the regulation of G(1)/S-phase progression and
            spindle assembly [CSPP].
REFERENCE   10 (residues 1 to 1170)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC109335.5 and AC087359.13.
            
            On Apr 17, 2025 this sequence version replaced XP_047278208.1.
            
            Summary: This gene encodes a centrosome and spindle pole associated
            protein. The encoded protein plays a role in cell-cycle progression
            and spindle organization, regulates cytokinesis, interacts with
            Nephrocystin 8 and is required for cilia formation. Mutations in
            this gene result in primary cilia abnormalities and classical
            Joubert syndrome. Alternatively spliced transcript variants
            encoding distinct isoforms have been found for this gene. [provided
            by RefSeq, Apr 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.953906.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1170
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1-q13.2"
     Protein         1..1170
                     /product="centrosome and spindle pole-associated protein 1
                     isoform 9"
                     /calculated_mol_wt=135997
     CDS             1..1170
                     /gene="CSPP1"
                     /gene_synonym="CSPP; CSPP-L; JBTS21"
                     /coded_by="NM_001438330.1:8..3520"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:79848"
                     /db_xref="HGNC:HGNC:26193"
                     /db_xref="MIM:611654"
ORIGIN      
        1 mlfplqvaav tssvrddple hcvsprtrar speickmadn ldefieeqka rlaedkaele
       61 sdppymemkg klsaklsens kilismaken ippnsqqtrg slgidyglsl plgedyerkk
      121 hklkeelrqd yrryltqerl klernkeynq flrgkeesse kfrqvekste pksqrnkkpi
      181 gqvkpdltsq iqtscenseg prkdvltpse ayeellnqrr leedryrqld deielrnrri
      241 ikkaneevgi snlkhqrfas kagipdrrfh rfnedrvfdr ryhrpdqdpe vseemderfr
      301 yesdfdrrls rvytndrmhr nkrgnmppme hdgdvieqsn irissaenks apdnetsksa
      361 nqdtcspfag mlfggedrel iqrrkekyrl elleqmaeqq rnkrrekdle lrvaasgaqd
      421 pekspdrlkq fsvaprhfee mipperpria fqtplpplsa psvppipsvh pvpsqnedlr
      481 sglssalgem vspriaplpp ppllpplatn yrtpyddayy fygsrntfdp slayygsgmm
      541 gvqpaayvsa pvthqlaqpv vntvgqnelk itsdqvinsg lifedkpkps kqslqsyqea
      601 lqqqireree rrkkereeke eyeakleaem rtynpwgkgg ggaplrdakg nlishmqtqs
      661 spfargnvfg epptelqikq qelyknflrf qieekkqree aererlriae ekeerrlaeq
      721 rariqqeyee eqekkrekee eqrlkneehi rlaeerqkea erkkkeeeek ynlqlqhyce
      781 rdnligeetk hmrqpspivp alqnkiaskl qrppsvdsii rsfihessms raqsppvpar
      841 knqlraeeek knvimelsem rkqlrseerr lqerllhmds ddeipirkke rnpmdifdma
      901 rhrlqapvrr qspkgldaat fqnvhdfnel kdrdsetrvd lkfmyldppr dhhtleiqqq
      961 allreqqkrl nrikmqegak vdldaipsak vreqrmprdd tsdflknsll esdsafigay
     1021 getypaiedd vlpppsqlps arerrrnkwk gldidssrpn vapdglslks issvnvdelr
     1081 vrneermrrl nefhnkpint ddesslvdpd dimkhigddg snsvatepwl rpgtsetlkr
     1141 fmaeqlnqeq qqipgkpgtf twqglstahg
//
LOCUS       NP_001424534             420 aa            linear   PRI 21-NOV-2025
DEFINITION  sorting nexin-27 isoform 7 [Homo sapiens].
ACCESSION   NP_001424534 XP_011508327 XP_054194892
VERSION     NP_001424534.1
DBSOURCE    REFSEQ: accession NM_001437605.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Broniarczyk,J., Trejo-Cerro,O., Massimi,P., Kavcic,N., Myers,M.P.
            and Banks,L.
  TITLE     HPV-18 E6 enhances the interaction between EMILIN2 and SNX27 to
            promote WNT signaling
  JOURNAL   J Virol 98 (7), e0073524 (2024)
   PUBMED   38874360
  REMARK    GeneRIF: HPV-18 E6 enhances the interaction between EMILIN2 and
            SNX27 to promote WNT signaling.
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Xi,Y., Gai,Y., Zhang,W., Wang,M., Liu,Q. and Bi,Y.
  TITLE     Circular RNA SNX27 Facilitates Gastric Cancer Progression By
            Sponging miR-638
  JOURNAL   Turk J Gastroenterol 35 (4), 280-287 (2024)
   PUBMED   39128090
  REMARK    GeneRIF: Circular RNA SNX27 Facilitates Gastric Cancer Progression
            By Sponging miR-638.
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Broniarczyk,J.K., Massimi,P., Trejo-Cerro,O., Myers,M.P. and
            Banks,L.
  TITLE     HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in a
            PBM-Dependent Manner and Promotes Increased Cell Proliferation
  JOURNAL   J Virol 96 (22), e0136522 (2022)
   PUBMED   36326272
  REMARK    GeneRIF: HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in
            a PBM-Dependent Manner and Promotes Increased Cell Proliferation.
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 420)
  AUTHORS   MacNeil,A.J., Mansour,M. and Pohajdak,B.
  TITLE     Sorting nexin 27 interacts with the Cytohesin associated
            scaffolding protein (CASP) in lymphocytes
  JOURNAL   Biochem Biophys Res Commun 359 (4), 848-853 (2007)
   PUBMED   17577583
  REMARK    GeneRIF: These results suggest that endosomal SNX27 may recruit
            CASP to orchestrate intracellular trafficking and/or signaling
            complexes.
REFERENCE   7  (residues 1 to 420)
  AUTHORS   Rincon,E., Santos,T., Avila-Flores,A., Albar,J.P., Lalioti,V.,
            Lei,C., Hong,W. and Merida,I.
  TITLE     Proteomics identification of sorting nexin 27 as a diacylglycerol
            kinase zeta-associated protein: new diacylglycerol kinase roles in
            endocytic recycling
  JOURNAL   Mol Cell Proteomics 6 (6), 1073-1087 (2007)
   PUBMED   17351151
  REMARK    GeneRIF: These data support a previously unreported role for
            diacylglycerol kinase zeta in the modulation of membrane
            trafficking, which may also help to define SNX27 function.
REFERENCE   8  (residues 1 to 420)
  AUTHORS   Joubert,L., Hanson,B., Barthet,G., Sebben,M., Claeysen,S., Hong,W.,
            Marin,P., Dumuis,A. and Bockaert,J.
  TITLE     New sorting nexin (SNX27) and NHERF specifically interact with the
            5-HT4a receptor splice variant: roles in receptor targeting
  JOURNAL   J Cell Sci 117 (Pt 22), 5367-5379 (2004)
   PUBMED   15466885
  REMARK    GeneRIF: SNX27a redirects part of the 5-HT4(a)R to early endosomes.
REFERENCE   9  (residues 1 to 420)
  AUTHORS   Worby,C.A. and Dixon,J.E.
  TITLE     Sorting out the cellular functions of sorting nexins
  JOURNAL   Nat Rev Mol Cell Biol 3 (12), 919-931 (2002)
   PUBMED   12461558
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol. 2003 Feb;4(2):156.]
REFERENCE   10 (residues 1 to 420)
  AUTHORS   Teasdale,R.D., Loci,D., Houghton,F., Karlsson,L. and Gleeson,P.A.
  TITLE     A large family of endosome-localized proteins related to sorting
            nexin 1
  JOURNAL   Biochem J 358 (Pt 1), 7-16 (2001)
   PUBMED   11485546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL391335.32 and AL589765.19.
            
            On or before Apr 7, 2025 this sequence version replaced
            XP_011508327.1, XP_054194892.1.
            
            Summary: This gene encodes a member of the sorting nexin family, a
            diverse group of cytoplasmic and membrane-associated proteins
            involved in endocytosis of plasma membrane receptors and protein
            trafficking through these compartments. All members of this protein
            family contain a phosphoinositide binding domain (PX domain). A
            highly similar protein in mouse is responsible for the specific
            recruitment of an isoform of serotonin 5-hydroxytryptamine 4
            receptor into early endosomes, suggesting the analogous role for
            the human protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3319678.1,
                                           SRR14038195.740717.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..420
                     /product="sorting nexin-27 isoform 7"
                     /note="methamphetamine-responsive transcript 1; sorting
                     nexin family member 27"
                     /calculated_mol_wt=48000
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L92.2)"
     Region          42..>61
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96L92.2)"
     Region          <61..144
                     /region_name="PX_domain"
                     /note="The Phox Homology domain, a phosphoinositide
                     binding module; cl02563"
                     /db_xref="CDD:470617"
     Site            order(75..77,101..102,114)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132768"
     Region          152..244
                     /region_name="FERM_F1_SNX27"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F1 sub-domain, found in sorting nexin protein 27
                     (SNX27); cd01777"
                     /db_xref="CDD:340475"
     Region          304..405
                     /region_name="FERM-like_C_SNX27"
                     /note="Atypical FERM-like domain C-lobe of Sorting nexin
                     27; cd13338"
                     /db_xref="CDD:270146"
     CDS             1..420
                     /gene="SNX27"
                     /gene_synonym="MRT1; MY014"
                     /coded_by="NM_001437605.1:153..1415"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:81609"
                     /db_xref="HGNC:HGNC:20073"
                     /db_xref="MIM:611541"
ORIGIN      
        1 madedgegih psaphrnggg gggggsglhc agnggggggg prvvrivkse sgygfnvrgq
       61 vynvymagrq lcskryrefa ilhqnlkref anftfprlpg kwpfslseqq ldarrrglee
      121 ylekvcsirv igesdimqef lsesdenyng vsdvelrval pdgttvtvrv kknsttdqvy
      181 qaiaakvgmd sttvnyfalf evishsfvrk lapnefphkl yiqnytsavp gtcltirkwl
      241 ftteeeilln dndlavtyff hqavddvkkg yikaeeksyq lqklyeqrkm vmylnmlrtc
      301 egyneiifph cacdsrrkgh vitaisithf klhacteegq lenqviafew demqrwdtde
      361 egmafcfeya rgekkprwvk iftpyfnymh ecfervfcel kwrkenifqm arsqqrdvat
//
LOCUS       NP_001403222             754 aa            linear   PRI 21-NOV-2025
DEFINITION  oxysterol-binding protein-related protein 9 isoform j [Homo
            sapiens].
ACCESSION   NP_001403222
VERSION     NP_001403222.1
DBSOURCE    REFSEQ: accession NM_001416293.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Cabukusta,B., Borst Pauwels,S., Akkermans,J.J.L.L., Blomberg,N.,
            Mulder,A.A., Koning,R.I., Giera,M. and Neefjes,J.
  TITLE     The ORP9-ORP11 dimer promotes sphingomyelin synthesis
  JOURNAL   Elife 12, 91345 (2024)
   PUBMED   39106189
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 754)
  AUTHORS   He,R., Liu,F., Wang,H., Huang,S., Xu,K., Zhang,C., Liu,Y. and Yu,H.
  TITLE     ORP9 and ORP10 form a heterocomplex to transfer
            phosphatidylinositol 4-phosphate at ER-TGN contact sites
  JOURNAL   Cell Mol Life Sci 80 (3), 77 (2023)
   PUBMED   36853333
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Tan,J.X. and Finkel,T.
  TITLE     A phosphoinositide signalling pathway mediates rapid lysosomal
            repair
  JOURNAL   Nature 609 (7928), 815-821 (2022)
   PUBMED   36071159
REFERENCE   4  (residues 1 to 754)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 754)
  AUTHORS   Hacker,B., Schultheiss,C., Doring,M. and Kurzik-Dumke,U.
  TITLE     Molecular partners of hNOT/ALG3, the human counterpart of the
            Drosophila NOT and yeast ALG3 gene, suggest its involvement in
            distinct cellular processes relevant to congenital disorders of
            glycosylation, cancer, neurodegeneration and a variety of further
            pathologies
  JOURNAL   Hum Mol Genet 27 (11), 1858-1878 (2018)
   PUBMED   29547901
REFERENCE   6  (residues 1 to 754)
  AUTHORS   Gauci,S., Helbig,A.O., Slijper,M., Krijgsveld,J., Heck,A.J. and
            Mohammed,S.
  TITLE     Lys-N and trypsin cover complementary parts of the phosphoproteome
            in a refined SCX-based approach
  JOURNAL   Anal Chem 81 (11), 4493-4501 (2009)
   PUBMED   19413330
  REMARK    GeneRIF: Includes data showing N-alpha terminal acetylation of this
            protein (OSBL9_HUMAN), which begins with nASIMEGPLSK following
            cleavage of the initiating Met-1 residue.
REFERENCE   7  (residues 1 to 754)
  AUTHORS   Lessmann,E., Ngo,M., Leitges,M., Minguet,S., Ridgway,N.D. and
            Huber,M.
  TITLE     Oxysterol-binding protein-related protein (ORP) 9 is a PDK-2
            substrate and regulates Akt phosphorylation
  JOURNAL   Cell Signal 19 (2), 384-392 (2007)
   PUBMED   16962287
  REMARK    GeneRIF: Furthermore, mammalian target of rapamycin was implicated
            in ORP9L phosphorylation in HEK293 cells. These studies identify
            ORP9 as a PDK-2 substrate and negative regulator of Akt
            phosphorylation at the PDK-2 site.
REFERENCE   8  (residues 1 to 754)
  AUTHORS   Wyles,J.P. and Ridgway,N.D.
  TITLE     VAMP-associated protein-A regulates partitioning of
            oxysterol-binding protein-related protein-9 between the endoplasmic
            reticulum and Golgi apparatus
  JOURNAL   Exp Cell Res 297 (2), 533-547 (2004)
   PUBMED   15212954
REFERENCE   9  (residues 1 to 754)
  AUTHORS   Jaworski,C.J., Moreira,E., Li,A., Lee,R. and Rodriguez,I.R.
  TITLE     A family of 12 human genes containing oxysterol-binding domains
  JOURNAL   Genomics 78 (3), 185-196 (2001)
   PUBMED   11735225
REFERENCE   10 (residues 1 to 754)
  AUTHORS   Lehto,M., Laitinen,S., Chinetti,G., Johansson,M., Ehnholm,C.,
            Staels,B., Ikonen,E. and Olkkonen,V.M.
  TITLE     The OSBP-related protein family in humans
  JOURNAL   J Lipid Res 42 (8), 1203-1213 (2001)
   PUBMED   11483621
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104170.2, AL772260.3,
            AL831767.8 and AL050343.17.
            
            Summary: This gene encodes a member of the oxysterol-binding
            protein (OSBP) family, a group of intracellular lipid receptors.
            Most members contain an N-terminal pleckstrin homology domain and a
            highly conserved C-terminal OSBP-like sterol-binding domain,
            although some members contain only the sterol-binding domain. This
            family member functions as a cholesterol transfer protein that
            regulates Golgi structure and function. Multiple transcript
            variants, most of which encode distinct isoforms, have been
            identified. Related pseudogenes have been identified on chromosomes
            3, 11 and 12. [provided by RefSeq, Jul 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.995.1,
                                           SRR14038191.1467841.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..754
                     /product="oxysterol-binding protein-related protein 9
                     isoform j"
                     /note="oxysterol-binding protein-related protein 9;
                     OSBP-related protein 9"
                     /calculated_mol_wt=85052
     Region          23..124
                     /region_name="PH_ORP9"
                     /note="Human Oxysterol binding protein related protein 9
                     Pleckstrin homology (PH) domain; cd13290"
                     /db_xref="CDD:241444"
     Region          395..741
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     CDS             1..754
                     /gene="OSBPL9"
                     /gene_synonym="ORP-9; ORP9"
                     /coded_by="NM_001416293.1:641..2905"
                     /note="isoform j is encoded by transcript variant 14"
                     /db_xref="GeneID:114883"
                     /db_xref="HGNC:HGNC:16386"
                     /db_xref="MIM:606737"
ORIGIN      
        1 mpyrrvtsgr llslaapkma simegplskw tnvmkgwqyr wfvldynagl lsyytskdkm
       61 mrgsrrgcvr lrgavigidd eddstftitv dqktfhfqar daderekwih aleetilrht
      121 lqlqgldsgf vpsvqdfdkk lteadaylqi lieqlklfdd klqnckedeq rkkietlket
      181 tnsmvesikh civllqiakd qsnaekhadg mistinpvda iyqpsplepv istmpsqtvl
      241 ppepvqlcks eqrpsslpvg pvlatlghhq tptpnstgsg hsppssslts pshvnlspnt
      301 vpefsyssse defydadefh qsgsspkrli dssgsasvlt hsssgnslkr pdtteslnss
      361 lsngtsdadl fdshddrddd aeagsveehk svimhllsqv rlgmdltkvv lptfilerrs
      421 llemyadffa hpdlfvsisd qkdpkdrmvq vvkwylsafh agrkgsvakk pynpilgeif
      481 qchwtlpndt eentelvseg pvpwvsknsv tfvaeqvshh ppisafyaec fnkkiqfnah
      541 iwtkskflgm sigvhnigqg cvscldydeh yiltfpngyg rsiltvpwve lggecnincs
      601 ktgysaniif htkpfyggkk hritaeifsp ndkksfcsie gewngvmyak yatgentvfv
      661 dtkklpiikk kvrkledqne yesrslwkdv tfnlkirdid aateakhrle erqraearer
      721 kekeiqwetr lfhedgecwv ydepllkrlg aakh
//
LOCUS       NP_001412003             510 aa            linear   PRI 21-NOV-2025
DEFINITION  coatomer subunit delta isoform 4 [Homo sapiens].
ACCESSION   NP_001412003
VERSION     NP_001412003.1
DBSOURCE    REFSEQ: accession NM_001425074.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   O'Donoghue,L., Comer,S.P., Hiebner,D.W., Schoen,I., von
            Kriegsheim,A. and Smolenski,A.
  TITLE     RhoGAP6 interacts with COPI to regulate protein transport
  JOURNAL   Biochem J 480 (14), 1109-1127 (2023)
   PUBMED   37409526
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Li,W., Liang,J., Outeda,P., Turner,S., Wakimoto,B.T. and Watnick,T.
  TITLE     A genetic screen in Drosophila reveals an unexpected role for the
            KIP1 ubiquitination-promoting complex in male fertility
  JOURNAL   PLoS Genet 16 (12), e1009217 (2020)
   PUBMED   33378371
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Tidwell,T., Deshotel,M., Palumbos,J., Miller,C., Bayrak-Toydemir,P.
            and Carey,J.C.
  TITLE     Novel de novo ARCN1 intronic variant causes rhizomelic short
            stature with microretrognathia and developmental delay
  JOURNAL   Cold Spring Harb Mol Case Stud 6 (6), a005728 (2020)
   PUBMED   33154040
  REMARK    GeneRIF: Novel de novo ARCN1 intronic variant causes rhizomelic
            short stature with microretrognathia and developmental delay.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 510)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 510)
  AUTHORS   Schekman,R. and Orci,L.
  TITLE     Coat proteins and vesicle budding
  JOURNAL   Science 271 (5255), 1526-1533 (1996)
   PUBMED   8599108
  REMARK    Review article
REFERENCE   7  (residues 1 to 510)
  AUTHORS   Cukierman,E., Huber,I., Rotman,M. and Cassel,D.
  TITLE     The ARF1 GTPase-activating protein: zinc finger motif and Golgi
            complex localization
  JOURNAL   Science 270 (5244), 1999-2002 (1995)
   PUBMED   8533093
REFERENCE   8  (residues 1 to 510)
  AUTHORS   Radice,P., Pensotti,V., Jones,C., Perry,H., Pierotti,M.A. and
            Tunnacliffe,A.
  TITLE     The human archain gene, ARCN1, has highly conserved homologs in
            rice and Drosophila
  JOURNAL   Genomics 26 (1), 101-106 (1995)
   PUBMED   7782067
REFERENCE   9  (residues 1 to 510)
  AUTHORS   Orcl,L., Palmer,D.J., Amherdt,M. and Rothman,J.E.
  TITLE     Coated vesicle assembly in the Golgi requires only coatomer and ARF
            proteins from the cytosol
  JOURNAL   Nature 364 (6439), 732-734 (1993)
   PUBMED   8355790
REFERENCE   10 (residues 1 to 510)
  AUTHORS   Waters,M.G., Serafini,T. and Rothman,J.E.
  TITLE     'Coatomer': a cytosolic protein complex containing subunits of
            non-clathrin-coated Golgi transport vesicles
  JOURNAL   Nature 349 (6306), 248-251 (1991)
   PUBMED   1898986
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000941.6.
            
            Summary: This gene maps in a region, which include the mixed
            lineage leukemia and Friend leukemia virus integration 1 genes,
            where multiple disease-associated chromosome translocations occur.
            It is an intracellular protein. Archain sequences are well
            conserved among eukaryotes and this protein may play a fundamental
            role in eukaryotic cell biology. It has similarities to heat shock
            proteins and clathrin-associated proteins, and may be involved in
            vesicle structure or trafficking. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4643856.39731.1,
                                           ERR4643930.16156.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN02400308 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..510
                     /product="coatomer subunit delta isoform 4"
                     /note="coatomer protein delta-COP; coatomer protein
                     complex, subunit delta; archain vesicle transport protein
                     1; coatomer delta subunit; delta-coat protein; COPI coat
                     complex subunit delta"
                     /calculated_mol_wt=56980
     Region          4..132
                     /region_name="Delta_COP_N"
                     /note="delta subunit of the F-COPI complex, N-terminal
                     domain; cd14830"
                     /db_xref="CDD:341434"
     Region          167..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48444.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            232
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            240
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q5XJY5; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Region          271..507
                     /region_name="AP_delta-COPI_MHD"
                     /note="Mu homology domain (MHD) of adaptor protein (AP)
                     coat protein I (COPI) delta subunit; cd09254"
                     /db_xref="CDD:271162"
     Site            308
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            350
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q5XJY5; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P48444.1)"
     CDS             1..510
                     /gene="ARCN1"
                     /gene_synonym="COPD; SRMMD; SSMG"
                     /coded_by="NM_001425074.1:140..1672"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:372"
                     /db_xref="HGNC:HGNC:649"
                     /db_xref="MIM:600820"
ORIGIN      
        1 mvllaaavct kagkaivsrq fvemtrtrie gllaafpklm ntgkqhtfve tesvryvyqp
       61 meklymvlit tknsniledl etlrlfsrip eycraleene isehcfdlif afdeivalgy
      121 renvnlaqir tftemdshee kvfravretq ereakaemrr kakelqqarr daerqgkkap
      181 gfggfgssav sggstaamit etiietdkpk vapaparpsg pskalklgak gkevdnfvdk
      241 lksegetims ssmgkrtsea tkmhappinm esvhmkieek itltcgrdgg lqnmelhgmi
      301 mlrisddkyg rirlhvened kkgvqlqthp nvdkklftae sliglknpek sfpvnsdvgv
      361 lkwrlqttee sfipltincw psesgngcdv nieyelqedn lelndvviti plpsgvgapv
      421 igeidgeyrh dsrrntlewc lpvidaknks gslefsiagq pndffpvqvs fvskknycni
      481 qvtkvtqvdg nspvrfstet tflvdkyeil
//
LOCUS       NP_001397945             897 aa            linear   PRI 21-NOV-2025
DEFINITION  echinoderm microtubule-associated protein-like 3 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001397945 XP_005273935
VERSION     NP_001397945.1
DBSOURCE    REFSEQ: accession NM_001411016.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 897)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 897)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 897)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   4  (residues 1 to 897)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 897)
  AUTHORS   Luo,J., Yang,B., Xin,G., Sun,M., Zhang,B., Guo,X., Jiang,Q. and
            Zhang,C.
  TITLE     The microtubule-associated protein EML3 regulates mitotic spindle
            assembly by recruiting the Augmin complex to spindle microtubules
  JOURNAL   J Biol Chem 294 (14), 5643-5656 (2019)
   PUBMED   30723163
  REMARK    GeneRIF: results indicate that EML3 regulates mitotic spindle
            assembly and the kinetochore-MT connection by regulating MT-based
            MT nucleation and recruiting Augmin/gamma-TuRC to MTs.
REFERENCE   6  (residues 1 to 897)
  AUTHORS   Richards,M.W., O'Regan,L., Roth,D., Montgomery,J.M., Straube,A.,
            Fry,A.M. and Bayliss,R.
  TITLE     Microtubule association of EML proteins and the EML4-ALK variant 3
            oncoprotein require an N-terminal trimerization domain
  JOURNAL   Biochem J 467 (3), 529-536 (2015)
   PUBMED   25740311
REFERENCE   7  (residues 1 to 897)
  AUTHORS   Tegha-Dunghu,J., Neumann,B., Reber,S., Krause,R., Erfle,H.,
            Walter,T., Held,M., Rogers,P., Hupfeld,K., Ruppert,T., Ellenberg,J.
            and Gruss,O.J.
  TITLE     EML3 is a nuclear microtubule-binding protein required for the
            correct alignment of chromosomes in metaphase
  JOURNAL   J Cell Sci 121 (Pt 10), 1718-1726 (2008)
   PUBMED   18445686
  REMARK    GeneRIF: Functional analysis of EML3 demonstrates an important role
            for EML3 in correct metaphase chromosome alignment.
REFERENCE   8  (residues 1 to 897)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   9  (residues 1 to 897)
  AUTHORS   O'Connor,V., Houtman,S.H., De Zeeuw,C.I., Bliss,T.V. and
            French,P.J.
  TITLE     Eml5, a novel WD40 domain protein expressed in rat brain
  JOURNAL   Gene 336 (1), 127-137 (2004)
   PUBMED   15225882
REFERENCE   10 (residues 1 to 897)
  AUTHORS   Pozuelo Rubio,M., Geraghty,K.M., Wong,B.H., Wood,N.T.,
            Campbell,D.G., Morrice,N. and Mackintosh,C.
  TITLE     14-3-3-affinity purification of over 200 human phosphoproteins
            reveals new links to regulation of cellular metabolism,
            proliferation and trafficking
  JOURNAL   Biochem J 379 (Pt 2), 395-408 (2004)
   PUBMED   14744259
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001458.6.
            
            On Aug 20, 2022 this sequence version replaced XP_005273935.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853566.4859.1,
                                           SRR14038196.3250565.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..897
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..897
                     /product="echinoderm microtubule-associated protein-like 3
                     isoform 4"
                     /note="EMAP-3; echinoderm microtubule associated protein
                     like 3"
                     /calculated_mol_wt=95153
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          6..>37
                     /region_name="TD_EMAP-like"
                     /note="trimerization domain of the echinoderm
                     microtubule-associated protein-like family; cl41737"
                     /db_xref="CDD:425368"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q32P44.1)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q32P44.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          218..286
                     /region_name="HELP"
                     /note="HELP motif; pfam03451"
                     /db_xref="CDD:460922"
     Region          235..287
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          296..345
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          <300..626
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          309..356
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          351..393
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          364..403
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          399..435
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          409..449
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          449..488
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          464..513
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          505..544
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          506..870
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          518..556
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          550..585
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          562..596
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          590..627
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          630..668
                     /region_name="WD 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          634..678
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          675..710
                     /region_name="WD 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          684..724
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          717..756
                     /region_name="WD 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          730..756
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          766..824
                     /region_name="WD 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          798..835
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          831..870
                     /region_name="WD 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Region          843..870
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          877..897
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q32P44.1)"
     Site            882
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:30723163,
                     ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q32P44.1)"
     Site            884
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q32P44.1)"
     CDS             1..897
                     /gene="EML3"
                     /gene_synonym="ELP95; EMAP3; EMAP95"
                     /coded_by="NM_001411016.1:319..3012"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS91491.1"
                     /db_xref="GeneID:256364"
                     /db_xref="HGNC:HGNC:26666"
                     /db_xref="MIM:618118"
ORIGIN      
        1 mdgaagpgdg parealqsls qrlrvqeqem elvkaalaea lrllrlqvpp sslqgsgtpa
       61 ppgdsslaap pglpptctps lvsrgtqtet evelksspgp pglsngppap qgaseepsgt
      121 qsegggssss gagspgppgi lrplqppqra dtprrnssss sspserprqk lsrkaissan
      181 llvrsgstes rggkdplssp ggpgsrrsny nlegisvkmf lrgrpitmyi psgirsleel
      241 psgpppetls ldwvygyrgr dsrsnlfvlr sgevvyfiac vvvlyrpggg pggpggggqr
      301 hyrghtdcvr clavhpdgvr vasgqtagvd kdgkplqpvv hiwdsetllk lqeiglgafe
      361 rgvgalafsa adqgaflcvv ddsnehmlsv wdcsrgmkla eikstndsvl avgfnprdss
      421 civtsgkshv hfwnwsggvg vpgngtltrk qgvfgkykkp kfipcfvflp dgdiltgdse
      481 gniltwgrsp sdsktpgrgg aketygivaq ahahegsifa lclrrdgtvl sgggrdrrlv
      541 qwgpglvalq eaeipehfga vraiaeglgs ellvgttkna llrgdlaqgf spviqghtde
      601 lwglcthpsq nrfltcghdr qlclwdgesh alawsidlke tglcadfhps gavvavglnt
      661 grwlvldtet reivsdvidg neqlsvvrys pdglylaigs hdnviyiysv ssdgakssrf
      721 grcmghssfi thldwskdgn fimsnsgdye ilywdvaggc kqlknryesr drewatytcv
      781 lgfhvygvwp dgsdgtdins lcrshnervv avaddfckvh lfqypcarak apsrmygghg
      841 shvtsvrfth ddshlvslgg kdasifqwrv lgaggagpap atpsrtpsls passldv
//
LOCUS       NP_001229468            1070 aa            linear   PRI 21-NOV-2025
DEFINITION  nuclear receptor coactivator 6 isoform 2 [Homo sapiens].
ACCESSION   NP_001229468 XP_016883240 XP_054179249
VERSION     NP_001229468.1
DBSOURCE    REFSEQ: accession NM_001242539.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Lee,K.G., Hong,B.K., Lee,S., Lee,N., Kim,S.W., Kim,D. and Kim,W.U.
  TITLE     Nuclear receptor coactivator 6 is a critical regulator of NLRP3
            inflammasome activation and gouty arthritis
  JOURNAL   Cell Mol Immunol 21 (3), 227-244 (2024)
   PUBMED   38195836
  REMARK    GeneRIF: Nuclear receptor coactivator 6 is a critical regulator of
            NLRP3 inflammasome activation and gouty arthritis.
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Fang,Y., Xu,Y., Liao,W., Ji,T., Yu,L., Li,L., Pan,M. and Yang,D.
  TITLE     Multiomics analyses and machine learning of nuclear receptor
            coactivator 6 reveal its essential role in hepatocellular carcinoma
  JOURNAL   Cancer Sci 114 (1), 75-90 (2023)
   PUBMED   36086920
  REMARK    GeneRIF: Multiomics analyses and machine learning of nuclear
            receptor coactivator 6 reveal its essential role in hepatocellular
            carcinoma.
REFERENCE   4  (residues 1 to 1070)
  AUTHORS   Watanabe,N., Kawagoe,J., Sugiyama,A., Takehara,I., Ohta,T. and
            Nagase,S.
  TITLE     Nuclear receptor coactivator-6 is essential for the morphological
            change of human uterine stromal cell decidualization via regulating
            actin fiber reorganization
  JOURNAL   Mol Reprod Dev 89 (4), 165-174 (2022)
   PUBMED   35384116
  REMARK    GeneRIF: Nuclear receptor coactivator-6 is essential for the
            morphological change of human uterine stromal cell decidualization
            via regulating actin fiber reorganization.
REFERENCE   5  (residues 1 to 1070)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 1070)
  AUTHORS   Caira,F., Antonson,P., Pelto-Huikko,M., Treuter,E. and
            Gustafsson,J.A.
  TITLE     Cloning and characterization of RAP250, a novel nuclear receptor
            coactivator
  JOURNAL   J Biol Chem 275 (8), 5308-5317 (2000)
   PUBMED   10681503
REFERENCE   7  (residues 1 to 1070)
  AUTHORS   Lee,S.K., Anzick,S.L., Choi,J.E., Bubendorf,L., Guan,X.Y.,
            Jung,Y.K., Kallioniemi,O.P., Kononen,J., Trent,J.M., Azorsa,D.,
            Jhun,B.H., Cheong,J.H., Lee,Y.C., Meltzer,P.S. and Lee,J.W.
  TITLE     A nuclear factor, ASC-2, as a cancer-amplified transcriptional
            coactivator essential for ligand-dependent transactivation by
            nuclear receptors in vivo
  JOURNAL   J Biol Chem 274 (48), 34283-34293 (1999)
   PUBMED   10567404
REFERENCE   8  (residues 1 to 1070)
  AUTHORS   Guan,X.Y., Xu,J., Anzick,S.L., Zhang,H., Trent,J.M. and
            Meltzer,P.S.
  TITLE     Hybrid selection of transcribed sequences from microdissected DNA:
            isolation of genes within amplified region at 20q11-q13.2 in breast
            cancer
  JOURNAL   Cancer Res 56 (15), 3446-3450 (1996)
   PUBMED   8758910
REFERENCE   9  (residues 1 to 1070)
  AUTHORS   Carney,J.P., McKnight,C., VanEpps,S. and Kelley,M.R.
  TITLE     Random rapid amplification of cDNA ends (RRACE) allows for cloning
            of multiple novel human cDNA fragments containing (CAG)n repeats
  JOURNAL   Gene 155 (2), 289-292 (1995)
   PUBMED   7536696
REFERENCE   10 (residues 1 to 1070)
  AUTHORS   Estey,A., Kemp,M., Allison,S. and Lamb,C.
  TITLE     Evaluation of a patient information booklet
  JOURNAL   J Nurs Staff Dev 9 (6), 278-282 (1993)
   PUBMED   8263591
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049709.18 and AL109824.24.
            
            On or before Apr 16, 2025 this sequence version replaced
            XP_016883240.1, XP_054179249.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            coactivator that can interact with nuclear hormone receptors to
            enhance their transcriptional activator functions. This protein has
            been shown to be involved in the hormone-dependent coactivation of
            several receptors, including prostanoid, retinoid, vitamin D3,
            thyroid hormone, and steroid receptors. Alternatively spliced
            transcript variants encoding different isoforms have been described
            for this gene. [provided by RefSeq, Jun 2011].
            
            Transcript Variant: This variant (2) lacks an in-frame coding exon
            in the central coding region, compared to variant 3. The encoded
            isoform (2, also known as NCOA6-beta) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1678932.1,
                                           SRR14038192.3457895.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..1070
                     /product="nuclear receptor coactivator 6 isoform 2"
                     /note="amplified in breast cancer-3 protein; activating
                     signal cointegrator-2; nuclear receptor coactivator
                     RAP250; peroxisome proliferator-activated receptor
                     interacting protein; thyroid hormone receptor binding
                     protein; NRC RAP250; PPAR-interacting protein; amplified
                     in breast cancer protein 3; nuclear receptor-activating
                     protein, 250 kDa; cancer-amplified transcriptional
                     coactivator ASC-2"
                     /calculated_mol_wt=115209
     Region          1..928
                     /region_name="TBP/GTF2A-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          48..190
                     /region_name="Nucleic_acid_bd"
                     /note="Putative nucleic acid-binding region; pfam13820"
                     /db_xref="CDD:463988"
     Site            95
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          <152..544
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          184..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          281..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          520..>838
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          773..927
                     /region_name="NCOA6IP-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          789..811
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            884
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK, in vitro.
                     /evidence=ECO:0000269|PubMed:11773444; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          887..891
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     CDS             1..1070
                     /gene="NCOA6"
                     /gene_synonym="AIB3; ASC2; NRC; PRIP; RAP250; TRBP"
                     /coded_by="NM_001242539.3:344..3556"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS74720.1"
                     /db_xref="GeneID:23054"
                     /db_xref="HGNC:HGNC:15936"
                     /db_xref="MIM:605299"
ORIGIN      
        1 mvlddlpnle diytslcsst medsemdfds gledddtksd siledstifv afkgniddkd
       61 fkwkldailk nvpnllhmes sklkvqkvep wnsvrvtfni preaaerlri laqsnnqqlr
      121 dlgilsvqie gegainlala qnrsqdvrmn gpmgagnsvr meagfpmasg pgiirmnnpa
      181 tvmippggnv sssmmapgpn pelqprtprp asqsdamdpl lsglhiqqqs hpsgslapph
      241 hpmqpvsvnr qmnpanfpql qqqqqqqqqq qqqqqqqqqq qqqqqlqarp pqqhqqqqpq
      301 girpqftapt qvpvppgwnq lpsgalqppp aqgslgtmta nqgwkkaplp gpmqqqlqar
      361 pslatvqtps hppppypfgs qqasqahtnf pqmsnpgqft apqmkslqgg psrvptplqq
      421 phltnkspas spssfqqgsp assptvnqtq qqmgprppqn nplpqgfqqp vsspgrnpmv
      481 qqgnvppnfm vmqqqppnqg pqslhpglgg mpkrlppgfs agqanpnfmq gqvpsttatt
      541 pgnsgapqlq anqnvqhagg qgagppqnqm qvshgppnmm qpslmgihgn mnnqqagtsg
      601 vpqvnlsnmq gqpqqgppsq lmgmhqqivp sqgqmvqqqg tlnpqnpmil sraqlmpqgq
      661 mmvnppsqnl gpspqrmtpp kqmlsqqgpq mmaphnqmmg pqgqvllqqn pmieqimtnq
      721 mqgnkqqfnt qnqsnvmpgp aqimrgptpn mqgnmvqftg qmsgqmlpqq gpvnnspsqv
      781 mgiqgqvlrp pgpsphmaqq hgdpattann dvslsqmmpd vsiqqtnmvp phvqamqgns
      841 asgnhfsghg msfnapfsga pngnqmscgq npgfpvnkdv tltspllvnl lqsdisaghf
      901 gvnnkqnntn ankpkkkkpp rkkknsqqdl ntpdtrpagl eeadqpplpg eqginldnsg
      961 pklpefsnrp papsqnlvsk etsttalqas varpelevna aivsgqssep keivekskip
     1021 grrnsrteep tvasesveng hrkrssrpas assstkdits avqskrrksk
//
LOCUS       NP_001427439             593 aa            linear   PRI 21-NOV-2025
DEFINITION  radixin isoform 6 [Homo sapiens].
ACCESSION   NP_001427439
VERSION     NP_001427439.1
DBSOURCE    REFSEQ: accession NM_001440510.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 593)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 593)
  AUTHORS   Kruse,T., Benz,C., Garvanska,D.H., Lindqvist,R., Mihalic,F.,
            Coscia,F., Inturi,R., Sayadi,A., Simonetti,L., Nilsson,E., Ali,M.,
            Kliche,J., Moliner Morro,A., Mund,A., Andersson,E., McInerney,G.,
            Mann,M., Jemth,P., Davey,N.E., Overby,A.K., Nilsson,J. and
            Ivarsson,Y.
  TITLE     Large scale discovery of coronavirus-host factor protein
            interaction motifs reveals SARS-CoV-2 specific mechanisms and
            vulnerabilities
  JOURNAL   Nat Commun 12 (1), 6761 (2021)
   PUBMED   34799561
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 593)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 593)
  AUTHORS   Stemmer-Rachamimov,A.O., Gonzalez-Agosti,C., Xu,L., Burwick,J.A.,
            Beauchamp,R., Pinney,D., Louis,D.N. and Ramesh,V.
  TITLE     Expression of NF2-encoded merlin and related ERM family proteins in
            the human central nervous system
  JOURNAL   J Neuropathol Exp Neurol 56 (6), 735-742 (1997)
   PUBMED   9184664
REFERENCE   7  (residues 1 to 593)
  AUTHORS   Hirao,M., Sato,N., Kondo,T., Yonemura,S., Monden,M., Sasaki,T.,
            Takai,Y., Tsukita,S. and Tsukita,S.
  TITLE     Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma
            membrane association: possible involvement of phosphatidylinositol
            turnover and Rho-dependent signaling pathway
  JOURNAL   J Cell Biol 135 (1), 37-51 (1996)
   PUBMED   8858161
REFERENCE   8  (residues 1 to 593)
  AUTHORS   Wilgenbus,K.K., Milatovich,A., Francke,U. and Furthmayr,H.
  TITLE     Molecular cloning, cDNA sequence, and chromosomal assignment of the
            human radixin gene and two dispersed pseudogenes
  JOURNAL   Genomics 16 (1), 199-206 (1993)
   PUBMED   8486357
REFERENCE   9  (residues 1 to 593)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 593)
  AUTHORS   Sato,N., Funayama,N., Nagafuchi,A., Yonemura,S., Tsukita,S. and
            Tsukita,S.
  TITLE     A gene family consisting of ezrin, radixin and moesin. Its specific
            localization at actin filament/plasma membrane association sites
  JOURNAL   J Cell Sci 103 (Pt 1), 131-143 (1992)
   PUBMED   1429901
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002788.3 and AP000901.5.
            
            Summary: Radixin is a cytoskeletal protein that may be important in
            linking actin to the plasma membrane. It is highly similar in
            sequence to both ezrin and moesin. The radixin gene has been
            localized by fluorescence in situ hybridization to 11q23. A
            truncated version representing a pseudogene (RDXP2) was assigned to
            Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was
            mapped to 11p by Southern and PCR analyses. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.919617.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..593
                     /product="radixin isoform 6"
                     /calculated_mol_wt=69680
     Region          5..195
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          189..285
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(231..232,234..240,249,270,273..274,277)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(231,234..241,249,270,273..274,277)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(267,271)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            270..285
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          336..445
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          496..572
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..593
                     /gene="RDX"
                     /gene_synonym="DFNB24"
                     /coded_by="NM_001440510.1:170..1951"
                     /note="isoform 6 is encoded by transcript variant 12"
                     /db_xref="GeneID:5962"
                     /db_xref="HGNC:HGNC:9944"
                     /db_xref="MIM:179410"
ORIGIN      
        1 mdaelefaiq pnttgkqlfd qvvktvglre vwffglqyvd skgystwlkl nkkvtqqdvk
       61 kenplqfkfr akffpedvse eliqeitqrl fflqvkeail ndeiycppet avllasyavq
      121 akygdynkei hkpgylandr llpqrvleqh kltkeqweer iqnwheehrg mlredsmmey
      181 lkiaqdlemy gvnyfeiknk kgtelwlgvd alglniyehd dkltpkigfp wseirnisfn
      241 dkkfvikpid kkapdfvfya prlrinkril alcmgnhely mrrrkpdtie vqqmkaqare
      301 ekhqkqlera qlenekkkre iaekekerie rekeelmerl kqieeqtika qkeleeqtrk
      361 aleldqerkr akeeaerlek erraaeeaks aiakqaadqm knqeqlaael aeftakiall
      421 eeakkkkeee atewqhkafa aqedlektke elktvmsapp ppppppvipp tenehdehde
      481 nnaeasaels negvmnhrse eervtetqkn ervkkqlqal sselaqarde tkktqndvlh
      541 aenvkagrdk yktlrqirqg ntkqridefe amwgpklyal fqmrscqssi kqm
//
LOCUS       NP_001392785            1104 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001392785 XP_047291751
VERSION     NP_001392785.1
DBSOURCE    REFSEQ: accession NM_001405856.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1104)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1104)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1104)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1104)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1104)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1104)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1104)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            On May 5, 2022 this sequence version replaced XP_047291751.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3418512.1,
                                           SRR14372080.587022.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1104
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 2"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=120707
     Site            104
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          145..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          225..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          399..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          849..881
                     /region_name="Required for activation of KAT8 histone
                     acetyltransferase activity"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          884..1004
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     Region          909..927
                     /region_name="Interaction with KAT8 HAT domain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01397"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          937..1033
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            990
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            993
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            1002
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            1044
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          1057..1104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     CDS             1..1104
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405856.1:454..3768"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS74084.1"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankgli
      481 vlgevpppeh ttdlflplss evktdhgtdk liesvsqple nhgapiighi seslstkscg
      541 alrpvngvin tlqpvladhi pgdssdaeeq lhkkqrlnlv ssssdgtcva artrpvlsck
      601 krrlvrpnsi vplskkvhrn stirpgcdvn pscalcgsgs intmppeihy eapllerlsq
      661 ldscvhpvla fpddvptslh fqsmlksqwq nkpfdkikpp kklslkhrap mpgslpdsar
      721 kdrhklvssf lttaklshhq trpdrthrqh lddvgavpmv ervtapkaer llnppppvhd
      781 pnhskmrlrd hssersevlk hhtdmssssy laathhpphs plvrqlstss dspapassss
      841 qvtastsqpv rrrrgessfd innivipmsv aattrveklq ykeiltpswr evdlqslkgs
      901 pdeeneeied lsdaafaalh akceemerar wlwttsvppq rrgsrsyrss dgrttpqlgs
      961 anpstpqpas pdvssshsls eyshgqsprs pispelhsap ltpvardtpr hlasedtrcs
     1021 tpelgldeqs vqpwerrtfp lahspqaece dqldaqeraa rctrrtsgsk tgreteaapt
     1081 sppivplksr hlvaaataqr pthr
//
LOCUS       NP_001397985             674 aa            linear   PRI 21-NOV-2025
DEFINITION  MAP/microtubule affinity-regulating kinase 3 isoform g [Homo
            sapiens].
ACCESSION   NP_001397985 XP_016876785
VERSION     NP_001397985.1
DBSOURCE    REFSEQ: accession NM_001411056.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 674)
  AUTHORS   Aparicio-Bautista,D.I., Jimenez-Ortega,R.F., Becerra-Cervera,A.,
            Aquino-Galvez,A., de Leon-Suarez,V.P., Casas-Avila,L., Salmeron,J.,
            Hidalgo-Bravo,A., Rivera-Paredez,B. and Velazquez-Cruz,R.
  TITLE     Interaction between MARK3 (rs11623869), PLCB4 (rs6086746) and
            GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women
  JOURNAL   Front Endocrinol (Lausanne) 15, 1392063 (2024)
   PUBMED   38715801
  REMARK    GeneRIF: Interaction between MARK3 (rs11623869), PLCB4 (rs6086746)
            and GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 674)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 674)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 674)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 674)
  AUTHORS   Li,M.G., Katsura,K., Nomiyama,H., Komaki,K., Ninomiya-Tsuji,J.,
            Matsumoto,K., Kobayashi,T. and Tamura,S.
  TITLE     Regulation of the interleukin-1-induced signaling pathways by a
            novel member of the protein phosphatase 2C family (PP2Cepsilon)
  JOURNAL   J Biol Chem 278 (14), 12013-12021 (2003)
   PUBMED   12556533
REFERENCE   7  (residues 1 to 674)
  AUTHORS   Sun,T.Q., Lu,B., Feng,J.J., Reinhard,C., Jan,Y.N., Fantl,W.J. and
            Williams,L.T.
  TITLE     PAR-1 is a Dishevelled-associated kinase and a positive regulator
            of Wnt signalling
  JOURNAL   Nat Cell Biol 3 (7), 628-636 (2001)
   PUBMED   11433294
REFERENCE   8  (residues 1 to 674)
  AUTHORS   Peng,C.Y., Graves,P.R., Ogg,S., Thoma,R.S., Byrnes,M.J. 3rd, Wu,Z.,
            Stephenson,M.T. and Piwnica-Worms,H.
  TITLE     C-TAK1 protein kinase phosphorylates human Cdc25C on serine 216 and
            promotes 14-3-3 protein binding
  JOURNAL   Cell Growth Differ 9 (3), 197-208 (1998)
   PUBMED   9543386
REFERENCE   9  (residues 1 to 674)
  AUTHORS   Ono,T., Kawabe,T., Sonta,S. and Okamoto,T.
  TITLE     Assignment of MARK3 alias KP78 to human chromosome band 14q32.3 by
            in situ hybridization
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 101-102 (1997)
   PUBMED   9533022
REFERENCE   10 (residues 1 to 674)
  AUTHORS   Meller,N., Liu,Y.C., Collins,T.L., Bonnefoy-Berard,N., Baier,G.,
            Isakov,N. and Altman,A.
  TITLE     Direct interaction between protein kinase C theta (PKC theta) and
            14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition
            of PKC theta translocation and function
  JOURNAL   Mol Cell Biol 16 (10), 5782-5791 (1996)
   PUBMED   8816492
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133367.4 and KF456011.1.
            
            On Aug 20, 2022 this sequence version replaced XP_016876785.1.
            
            Summary: The protein encoded by this gene is activated by
            phosphorylation and in turn is involved in the phosphorylation of
            tau proteins MAP2 and MAP4. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.267927.1,
                                           SRR14038191.4530151.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.32-q32.33"
     Protein         1..674
                     /product="MAP/microtubule affinity-regulating kinase 3
                     isoform g"
                     /EC_number="2.7.11.1"
                     /note="EMK-2; C-TAK1; ELKL motif kinase 2; protein kinase
                     STK10; ser/Thr protein kinase PAR-1; cdc25C-associated
                     protein kinase 1; MAP/microtubule affinity-regulating
                     kinase 3; serine/threonine-protein kinase p78"
                     /calculated_mol_wt=75462
     Region          18..243
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          261..303
                     /region_name="UBA_MARK3_4"
                     /note="UBA domain found in MAP/microtubule
                     affinity-regulating kinase MARK3, MARK4, and similar
                     proteins; cd14407"
                     /db_xref="CDD:270590"
     Region          575..672
                     /region_name="MARK1-3_C"
                     /note="C-terminal, kinase associated domain 1 (KA1), a
                     phospholipid binding domain, of microtubule
                     affinity-regulating kinases 1-3; cd12196"
                     /db_xref="CDD:213381"
     Site            order(577,580,650,652..653)
                     /site_type="other"
                     /note="putative phospholipid binding site [chemical
                     binding]"
                     /db_xref="CDD:213381"
     CDS             1..674
                     /gene="MARK3"
                     /gene_synonym="CTAK1; KP78; Par-1a; PAR1A; VIPB"
                     /coded_by="NM_001411056.1:616..2640"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS91940.1"
                     /db_xref="GeneID:4140"
                     /db_xref="HGNC:HGNC:6897"
                     /db_xref="MIM:602678"
ORIGIN      
        1 mstrtplptv nerdtenvai kiidktqlnp tslqklfrev rimkilnhpn ivklfeviet
       61 ektlylimey asggevfdyl vahgrmkeke arskfrqivs avqychqkri vhrdlkaenl
      121 lldadmniki adfgfsneft vggkldtfcg sppyaapelf qgkkydgpev dvwslgvily
      181 tlvsgslpfd gqnlkelrer vlrgkyripf ymstdcenll krflvlnpik rgtleqimkd
      241 rwinagheed elkpfvepel disdqkridi mvgmgysqee iqeslskmky deitatylll
      301 grksseldas dsssssnlsl akvrpssdln nstgqsphhk vqrsvsssqk qrrysdhagp
      361 aipsvvaypk rsqtstadsd lkedgissrk ssgsavggkg iapaspmlgn asnpnkadip
      421 erkksstvps sntasggmtr rntyvcsert tadrhsviqn gkenstipdq rtpvasthsi
      481 ssaatpdrir fprgtasrst fhgqprerrt atyngppasp slsheatpls qtrsrgstnl
      541 fskltskltr rnmsfrfiks rnvsaeqkde nkeakprslr ftwsmkttss mdpgdmmrei
      601 rkvldanncd yeqrerfllf cvhgdghaen lvqwemevck lprlslngvr fkrisgtsia
      661 fkniaskian elkl
//
LOCUS       NP_001397749             861 aa            linear   PRI 21-NOV-2025
DEFINITION  MICAL-like protein 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001397749 XP_047297509
VERSION     NP_001397749.1
DBSOURCE    REFSEQ: accession NM_001410820.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 861)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 861)
  AUTHORS   Frisby,D., Murakonda,A.B., Ashraf,B., Dhawan,K., Almeida-Souza,L.,
            Naslavsky,N. and Caplan,S.
  TITLE     Endosomal actin branching, fission, and receptor recycling require
            FCHSD2 recruitment by MICAL-L1
  JOURNAL   Mol Biol Cell 35 (11), ar144 (2024)
   PUBMED   39382837
  REMARK    GeneRIF: Endosomal actin branching, fission, and receptor recycling
            require FCHSD2 recruitment by MICAL-L1.
REFERENCE   3  (residues 1 to 861)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 861)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 861)
  AUTHORS   Sikora,R., Bun,P., Danglot,L., Alqabandi,M., Bassereau,P.,
            Niedergang,F., Galli,T. and Zahraoui,A.
  TITLE     MICAL-L1 is required for cargo protein delivery to the cell surface
  JOURNAL   Biol Open 10 (6) (2021)
   PUBMED   34100897
  REMARK    GeneRIF: MICAL-L1 is required for cargo protein delivery to the
            cell surface.
REFERENCE   6  (residues 1 to 861)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 861)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   8  (residues 1 to 861)
  AUTHORS   Weide,T., Teuber,J., Bayer,M. and Barnekow,A.
  TITLE     MICAL-1 isoforms, novel rab1 interacting proteins
  JOURNAL   Biochem Biophys Res Commun 306 (1), 79-86 (2003)
   PUBMED   12788069
REFERENCE   9  (residues 1 to 861)
  AUTHORS   Terman,J.R., Mao,T., Pasterkamp,R.J., Yu,H.H. and Kolodkin,A.L.
  TITLE     MICALs, a family of conserved flavoprotein oxidoreductases,
            function in plexin-mediated axonal repulsion
  JOURNAL   Cell 109 (7), 887-900 (2002)
   PUBMED   12110185
REFERENCE   10 (residues 1 to 861)
  AUTHORS   Marzesco,A.M., Dunia,I., Pandjaitan,R., Recouvreur,M., Dauzonne,D.,
            Benedetti,E.L., Louvard,D. and Zahraoui,A.
  TITLE     The small GTPase Rab13 regulates assembly of functional tight
            junctions in epithelial cells
  JOURNAL   Mol Biol Cell 13 (6), 1819-1831 (2002)
   PUBMED   12058051
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL022311.5.
            
            On Aug 16, 2022 this sequence version replaced XP_047297509.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1376968.1,
                                           SRR14038194.73579.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..861
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..861
                     /product="MICAL-like protein 1 isoform 4"
                     /note="molecule interacting with Rab13; MICAL-like protein
                     1"
                     /calculated_mol_wt=93083
     Region          4..110
                     /region_name="CH_MICALL1"
                     /note="calponin homology (CH) domain found in MICAL-like
                     protein 1; cd21252"
                     /db_xref="CDD:409101"
     Site            order(4,8,58,60..61,64..65,67,76..84,92,94..95,97..98,
                     101..102,105)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409101"
     Region          119..162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Region          164..218
                     /region_name="LIM_Mical_like_1"
                     /note="This domain belongs to the LIM domain family which
                     are found on Mical (molecule interacting with CasL) like
                     proteins; cd09444"
                     /db_xref="CDD:188828"
     Site            order(164,167,185,188,191,194,214,217)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188828"
     Region          <245..660
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Region          425..427
                     /region_name="NPF1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            467
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            578
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Region          631..633
                     /region_name="NPF2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Region          650..861
                     /region_name="Mediates the interaction with RAB13 and
                     RAB35 and intramolecular interaction with the CH domain.
                     /evidence=ECO:0000269|PubMed:21795389,
                     ECO:0000269|PubMed:21951725"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Region          685..806
                     /region_name="bMERB_dom"
                     /note="Bivalent Mical/EHBP Rab binding domain; pfam12130"
                     /db_xref="CDD:463467"
     Region          698..861
                     /region_name="Necessary and sufficient to associate with
                     tubular recycling endosome membranes, mediate phosphatidic
                     acid-binding and membrane tubulation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            738
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BGT6; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     CDS             1..861
                     /gene="MICALL1"
                     /gene_synonym="MICAL-L1; MIRAB13"
                     /coded_by="NM_001410820.1:127..2712"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS93162.1"
                     /db_xref="GeneID:85377"
                     /db_xref="HGNC:HGNC:29804"
                     /db_xref="MIM:619563"
ORIGIN      
        1 magprgalla wcrrqcegyr gveirdlsss frdglafcai lhrhrpdlld fdslskdnvf
       61 ennrlafeva ekelgipall dpndmvsmsv pdclsimtyv sqyynhfcsp gqagvspprk
      121 glapcsppsv aptpvepedv aqgeelssgs lseqgtgqtp sstcaacqqh vhlvqrylad
      181 grlyhrhcfr crrcsstllp gayengpeeg tfvcaehcar lgpgtrsgtr pgpfsqpkqq
      241 hqqqlaedak dvpgggpsss apagaeadgp kaspearpqi ptkprvpgkl qelasppagr
      301 ptpaprkase sttpapptpr prsslqqenl veqagssslv ngrlhelpvp kprgtpkpse
      361 gtpaprkdpp witlvqaepk kkpaplppss spgppsqdsr qvenggteev aqpsptasle
      421 skpynpfeee eedkeeeapa apslatspal ghpestpksl hpwygitpts spktkkrpap
      481 rapsasplal hasrlshsep psatpspals veslssesas qtagaellep pavpksssep
      541 avhapgtpgn pvslstnssl assgelvepr veqmpqaspg laprtrgssg pqpakpcsga
      601 tptplllvgd rspvpspgss spqlqsscke npfnrkpspa aspatkkatk gskpvrppap
      661 ghgfplikrk vqadqyipee dihgemdtie rrldalehrg vlleeklrgg lnegreddml
      721 vdwfklihek hllvrresel iyvfkqqnle qrqadveyel rcllnkpekd wteedrarek
      781 vlmqelvtli eqrnaiincl dedrqreeee dkmleamikk kefqreaepe gkkkgkfktm
      841 kmlkllgnkr daksksprdk s
//
LOCUS       NP_001397862             284 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase E3D isoform 4 [Homo sapiens].
ACCESSION   NP_001397862 XP_047275460
VERSION     NP_001397862.1
DBSOURCE    REFSEQ: accession NM_001410933.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Lin,M.H., Jensen,M.K., Elrod,N.D., Chu,H.F., Haseley,M., Beam,A.C.,
            Huang,K.L., Chiang,W., Russell,W.K., Williams,K., Proschel,C.,
            Wagner,E.J. and Tong,L.
  TITLE     Cytoplasmic binding partners of the Integrator endonuclease INTS11
            and its paralog CPSF73 are required for their nuclear function
  JOURNAL   Mol Cell 84 (15), 2900-2917 (2024)
   PUBMED   39032490
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Offenbacher,S., Divaris,K., Barros,S.P., Moss,K.L., Marchesan,J.T.,
            Morelli,T., Zhang,S., Kim,S., Sun,L., Beck,J.D., Laudes,M.,
            Munz,M., Schaefer,A.S. and North,K.E.
  TITLE     Genome-wide association study of biologically informed periodontal
            complex traits offers novel insights into the genetic basis of
            periodontal disease
  JOURNAL   Hum Mol Genet 25 (10), 2113-2129 (2016)
   PUBMED   26962152
  REMARK    GeneRIF: With the exception of associations of BEGAIN with severe
            and UBE3D with moderate chronic periodontitis (CP) , no other loci
            were associated with CP in ARIC or aggressive periodontitis in the
            German sample.
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Huang,L.Z., Li,Y.J., Xie,X.F., Zhang,J.J., Cheng,C.Y.,
            Yamashiro,K., Chen,L.J., Ma,X.Y., Cheung,C.M., Wang,Y.S.,
            Zhang,C.F., Bai,Y.J., Hou,J., Chen,X.L., Qi,Y., Li,S.S., Sun,Y.Y.,
            Mei,J.P., Cheng,Y., Yu,W.Z., Hu,X.B., Zhuang,F.F., Fan,L., Lu,Y.,
            Sun,X.H., Zhu,X.J., Shen,D.F., Chan,C.C., Zhao,M.W., Yoshimura,N.,
            Pang,C.P., Wong,T.Y., Khor,C.C., Zhang,K., Zhou,P. and Li,X.X.
  TITLE     Whole-exome sequencing implicates UBE3D in age-related macular
            degeneration in East Asian populations
  JOURNAL   Nat Commun 6, 6687 (2015)
   PUBMED   25872646
  REMARK    GeneRIF: A novel missense SNV, rs7739323, is strongly associated
            with age-related macular degeneration in an East Asian population.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Kobirumaki,F., Miyauchi,Y., Fukami,K. and Tanaka,H.
  TITLE     A novel UbcH10-binding protein facilitates the ubiquitinylation of
            cyclin B in vitro
  JOURNAL   J Biochem 137 (2), 133-139 (2005)
   PUBMED   15749827
  REMARK    GeneRIF: The carboxyl terminal half of H10BH was able to bind
            cyclin B and ubiquitinylate cyclin B in vitro.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL139333.10 and AL357121.30.
            
            On Aug 18, 2022 this sequence version replaced XP_047275460.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2536819.1,
                                           SRR14038197.2108235.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467147 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..284
                     /product="E3 ubiquitin-protein ligase E3D isoform 4"
                     /EC_number="2.3.2.26"
                     /note="UBCH10 binding protein with a hect-like domain;
                     ubiquitin-conjugating enzyme E2C-binding protein; E3
                     ubiquitin-protein ligase E3D; ubcH10-binding protein with
                     a HECT-like domain; HECT-type E3 ubiquitin transferase
                     E3D"
                     /calculated_mol_wt=31715
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6J8.2)"
     Region          13..>275
                     /region_name="HECT_2"
                     /note="HECT-like Ubiquitin-conjugating enzyme
                     (E2)-binding; pfam09814"
                     /db_xref="CDD:462911"
     Region          129..159
                     /region_name="BRAT1-like motif.
                     /evidence=ECO:0000305|PubMed:39032490"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6J8.2)"
     Region          235..257
                     /region_name="Interaction with UBE2C.
                     /evidence=ECO:0000269|PubMed:15749827"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6J8.2)"
     CDS             1..284
                     /gene="UBE3D"
                     /gene_synonym="C6orf157; H10BH; UBE2CBP; YJR141W"
                     /coded_by="NM_001410933.1:124..978"
                     /note="isoform 4 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS93953.1"
                     /db_xref="GeneID:90025"
                     /db_xref="HGNC:HGNC:21381"
                     /db_xref="MIM:612495"
ORIGIN      
        1 maasaaetrv flevrgqlqs allilgepke ggmpmnisim psslqmktpe gcteiqlpae
       61 vrlvpsscrg lqfvvgdglh lrlqtqaklg tklismfnqs sqtqecctfy cqscgeviik
      121 drkllrvlpl psenwgalvg ewcchpdpfa nkslhpqend cfigdsfflv nlrtslwqqr
      181 pelspvemcc vssdnhckle pkantkvick rckvmlgetv ssettkfymt eiiiqssers
      241 fpiiprswfv qsviaqclvq lssarstfrf tiqamafkfr qfgd
//
LOCUS       NP_001427994             651 aa            linear   PRI 21-NOV-2025
DEFINITION  inhibitor of nuclear factor kappa-B kinase subunit alpha isoform 7
            [Homo sapiens].
ACCESSION   NP_001427994
VERSION     NP_001427994.1
DBSOURCE    REFSEQ: accession NM_001441065.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Chen,X., Wu,W., Jeong,J.H., Rokavec,M., Wei,R., Feng,S.,
            Schroth,W., Brauch,H., Zhong,S. and Luo,J.L.
  TITLE     Cytokines-activated nuclear IKKalpha-FAT10 pathway induces breast
            cancer tamoxifen-resistance
  JOURNAL   Sci China Life Sci 67 (7), 1413-1426 (2024)
   PUBMED   38565741
  REMARK    GeneRIF: Cytokines-activated nuclear IKKalpha-FAT10 pathway induces
            breast cancer tamoxifen-resistance.
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Chang,X., Guo,Y., Zhang,Q., Zheng,X., Cui,X., Hu,J., Zhang,Z.,
            Zhang,F. and Wang,X.
  TITLE     GRP78 recognizes EV-F 3D protein and activates NF-kappaB to repress
            virus replication by interacting with CHUK/IKBKB
  JOURNAL   J Virol 98 (6), e0026824 (2024)
   PUBMED   38775480
  REMARK    GeneRIF: GRP78 recognizes EV-F 3D protein and activates NF-kappaB
            to repress virus replication by interacting with CHUK/IKBKB.
REFERENCE   4  (residues 1 to 651)
  AUTHORS   McIntosh,K., Khalaf,Y.H., Craig,R., West,C., McCulloch,A.,
            Waghmare,A., Lawson,C., Chan,E.Y.W., Mackay,S., Paul,A. and
            Plevin,R.
  TITLE     IL-1beta stimulates a novel, IKKalpha -dependent, NIK -independent
            activation of non-canonical NFkappaB signalling
  JOURNAL   Cell Signal 107, 110684 (2023)
   PUBMED   37080443
  REMARK    GeneRIF: IL-1beta stimulates a novel, IKKalpha -dependent, NIK
            -independent activation of non-canonical NFkappaB signalling.
REFERENCE   5  (residues 1 to 651)
  AUTHORS   Yang,H., Espada,C.E., Phillips,S., Martinez,N., Kenney,A.D.,
            Yount,J.S., Xiong,Y. and Wu,L.
  TITLE     The host antiviral protein SAMHD1 suppresses NF-kappaB activation
            by interacting with the IKK complex during inflammatory responses
            and viral infection
  JOURNAL   J Biol Chem 299 (6), 104750 (2023)
   PUBMED   37100289
  REMARK    GeneRIF: The host antiviral protein SAMHD1 suppresses NF-kappaB
            activation by interacting with the IKK complex during inflammatory
            responses and viral infection.
REFERENCE   6  (residues 1 to 651)
  AUTHORS   Scherer,D.C., Brockman,J.A., Chen,Z., Maniatis,T. and Ballard,D.W.
  TITLE     Signal-induced degradation of I kappa B alpha requires
            site-specific ubiquitination
  JOURNAL   Proc Natl Acad Sci U S A 92 (24), 11259-11263 (1995)
   PUBMED   7479976
REFERENCE   7  (residues 1 to 651)
  AUTHORS   Mock,B.A., Connelly,M.A., McBride,O.W., Kozak,C.A. and Marcu,K.B.
  TITLE     CHUK, a conserved helix-loop-helix ubiquitous kinase, maps to human
            chromosome 10 and mouse chromosome 19
  JOURNAL   Genomics 27 (2), 348-351 (1995)
   PUBMED   7558004
REFERENCE   8  (residues 1 to 651)
  AUTHORS   Connelly,M.A. and Marcu,K.B.
  TITLE     CHUK, a new member of the helix-loop-helix and leucine zipper
            families of interacting proteins, contains a serine-threonine
            kinase catalytic domain
  JOURNAL   Cell Mol Biol Res 41 (6), 537-549 (1995)
   PUBMED   8777433
REFERENCE   9  (residues 1 to 651)
  AUTHORS   Ganchi,P.A., Sun,S.C., Greene,W.C. and Ballard,D.W.
  TITLE     A novel NF-kappa B complex containing p65 homodimers: implications
            for transcriptional control at the level of subunit dimerization
  JOURNAL   Mol Cell Biol 13 (12), 7826-7835 (1993)
   PUBMED   8246997
REFERENCE   10 (residues 1 to 651)
  AUTHORS   Ganchi,P.A., Sun,S.C., Greene,W.C. and Ballard,D.W.
  TITLE     I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B
            p65 and requires the transactivation domain to inhibit NF-kappa B
            p65 DNA binding
  JOURNAL   Mol Biol Cell 3 (12), 1339-1352 (1992)
   PUBMED   1493333
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138921.14.
            
            Summary: This gene encodes a member of the serine/threonine protein
            kinase family. The encoded protein, a component of a
            cytokine-activated protein complex that is an inhibitor of the
            essential transcription factor NF-kappa-B complex, phosphorylates
            sites that trigger the degradation of the inhibitor via the
            ubiquination pathway, thereby activating the transcription factor.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.29142.1,
                                           SRR14372079.496152.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.31"
     Protein         1..651
                     /product="inhibitor of nuclear factor kappa-B kinase
                     subunit alpha isoform 7"
                     /EC_number="2.7.11.10"
                     /note="I-kappa-B kinase-alpha; I-kappa-B kinase 1; Nuclear
                     factor NFkappaB inhibitor kinase alpha; IKK-a kinase; IkB
                     kinase alpha subunit; inhibitor of nuclear factor kappa-B
                     kinase subunit alpha; conserved helix-loop-helix
                     ubiquitous kinase; transcription factor 16"
                     /calculated_mol_wt=73815
     Region          <1..215
                     /region_name="PKc_like"
                     /note="Protein Kinases, catalytic domain; cl21453"
                     /db_xref="CDD:473864"
     Region          217..293
                     /region_name="Ubl_IKKA_like"
                     /note="ubiquitin-like (Ubl) domain found in inhibitor of
                     nuclear factor kappa-B kinases, IKK-alpha and IKK-beta,
                     and similar proteins; cd17046"
                     /db_xref="CDD:340566"
     Region          292..565
                     /region_name="IKBKB_SDD"
                     /note="IQBAL scaffold dimerization domain; pfam18397"
                     /db_xref="CDD:465745"
     Region          613..649
                     /region_name="IKKbetaNEMObind"
                     /note="I-kappa-kinase-beta NEMO binding domain; pfam12179"
                     /db_xref="CDD:463485"
     CDS             1..651
                     /gene="CHUK"
                     /gene_synonym="BPS2; IKBKA; IKK-1; IKK-alpha; IKK1; IKKA;
                     NFKBIKA; TCF16"
                     /coded_by="NM_001441065.1:252..2207"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:1147"
                     /db_xref="HGNC:HGNC:1974"
                     /db_xref="MIM:600664"
ORIGIN      
        1 meycsggdlr kllnkpencc glkesqilsl lsdigsgiry lhenkiihrd lkpenivlqd
       61 vggkiihkii dlgyakdvdq gslctsfvgt lqylapelfe nkpytatvdy wsfgtmvfec
      121 iagyrpflhh lqpftwheki kkkdpkcifa ceemsgevrf sshlpqpnsl cslvvepmen
      181 wlqlmlnwdp qqrggpvdlt lkqprcfvlm dhilnlkivh ilnmtsakii sfllppdesl
      241 hslqsriere tgintgsqel lsetgisldp rkpasqcvld gvrgcdsymv ylfdksktvy
      301 egpfasrsls dcvnyivqds kiqlpiiqlr kvwaeavhyv sglkedysrl fqgqraamls
      361 llrynanltk mkntlisasq qlkakleffh ksiqldlery seqmtygiss ekmlkawkem
      421 eekaihyaev gvigyledqi mslhaeimel qkspygrrqg dlmesleqra idlykqlkhr
      481 psdhsysdst emvkiivhtv qsqdrvlkel fghlskllgc kqkiidllpk vevalsnike
      541 adntvmfmqg krqkeiwhll kiactqssar slvgsslega vtpqtsawlp ptsaehdhsl
      601 scvvtpqdge tsaqmieenl nclghlstii heaneeqgns mmnldwswlt e
//
LOCUS       NP_001401162             276 aa            linear   PRI 21-NOV-2025
DEFINITION  L-lactate dehydrogenase B chain isoform 3 [Homo sapiens].
ACCESSION   NP_001401162
VERSION     NP_001401162.1
DBSOURCE    REFSEQ: accession NM_001414233.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Zhang,P., Wan,Y., Ma,J., Gong,J., Zhong,Z., Cui,Y., Zhang,H.,
            Da,Y., Ma,J., Li,C., Liu,L., Gong,T., Tan,Y. and Zhang,C.
  TITLE     Epigenetic silencing of LDHB promotes hepatocellular carcinoma by
            remodeling the tumor microenvironment
  JOURNAL   Cancer Immunol Immunother 73 (7), 127 (2024)
   PUBMED   38739169
  REMARK    GeneRIF: Epigenetic silencing of LDHB promotes hepatocellular
            carcinoma by remodeling the tumor microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Shi,F., Zhang,G., Li,J., Shu,L., Yu,C., Ren,D., Zhang,Y. and
            Zheng,P.
  TITLE     Integrated analysis of single cell-RNA sequencing and Mendelian
            randomization identifies lactate dehydrogenase B as a target of
            melatonin in ischemic stroke
  JOURNAL   CNS Neurosci Ther 30 (5), e14741 (2024)
   PUBMED   38702940
  REMARK    GeneRIF: Integrated analysis of single cell-RNA sequencing and
            Mendelian randomization identifies lactate dehydrogenase B as a
            target of melatonin in ischemic stroke.
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Stiebler,A.C., Freitag,J., Schink,K.O., Stehlik,T., Tillmann,B.A.,
            Ast,J. and Bolker,M.
  TITLE     Ribosomal readthrough at a short UGA stop codon context triggers
            dual localization of metabolic enzymes in Fungi and animals
  JOURNAL   PLoS Genet 10 (10), e1004685 (2014)
   PUBMED   25340584
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Schueren,F., Lingner,T., George,R., Hofhuis,J., Dickel,C.,
            Gartner,J. and Thoms,S.
  TITLE     Peroxisomal lactate dehydrogenase is generated by translational
            readthrough in mammals
  JOURNAL   Elife 3, e03640 (2014)
   PUBMED   25247702
  REMARK    GeneRIF: The readthrough-extended lactate dehydrogenase subunit
            LDHBx can also co-import LDHA, the other LDH subunit, into
            peroxisomes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
REFERENCE   7  (residues 1 to 276)
  AUTHORS   Takeno,T. and Li,S.S.
  TITLE     Structure of the human lactate dehydrogenase B gene
  JOURNAL   Biochem J 257 (3), 921-924 (1989)
   PUBMED   2930497
REFERENCE   8  (residues 1 to 276)
  AUTHORS   Sakai,I., Sharief,F.S., Pan,Y.C. and Li,S.S.
  TITLE     The cDNA and protein sequences of human lactate dehydrogenase B
  JOURNAL   Biochem J 248 (3), 933-936 (1987)
   PUBMED   3435492
REFERENCE   9  (residues 1 to 276)
  AUTHORS   Law,M.L. and Kao,F.T.
  TITLE     Regional assignment of human genes TPI1, GAPDH, LDHB, SHMT, and
            PEPB on chromosome 12
  JOURNAL   Cytogenet Cell Genet 24 (2), 102-114 (1979)
   PUBMED   477403
REFERENCE   10 (residues 1 to 276)
  AUTHORS   Rethore,M.O., Kaplan,J.C., Junien,C., Cruveiller,J., Dutrillaux,B.,
            Aurias,A., Carpentier,S., Lafourcade,J. and Lejeune.
  TITLE     [Increase of the LDH-B activity in a boy with 12p trisomy by
            malsegregation of a maternal translocation t(12;14) (q12;p11)]
  JOURNAL   Ann Genet 18 (2), 81-87 (1975)
   PUBMED   1081369
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010197.7.
            
            Summary: This gene encodes the B subunit of lactate dehydrogenase
            enzyme, which catalyzes the interconversion of pyruvate and lactate
            with concomitant interconversion of NADH and NAD+ in a
            post-glycolysis process. Alternatively spliced transcript variants
            have been found for this gene. Recent studies have shown that a
            C-terminally extended isoform is produced by use of an alternative
            in-frame translation termination codon via a stop codon readthrough
            mechanism, and that this isoform is localized in the peroxisomes.
            Mutations in this gene are associated with lactate dehydrogenase B
            deficiency. Pseudogenes have been identified on chromosomes X, 5
            and 13. [provided by RefSeq, Feb 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14243140.5158954.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968968,
                                           SAMEA2144333 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..276
                     /product="L-lactate dehydrogenase B chain isoform 3"
                     /EC_number="1.1.1.27"
                     /note="L-lactate dehydrogenase B chain; LDH heart subunit;
                     renal carcinoma antigen NY-REN-46; lactate dehydrogenase H
                     chain; epididymis secretory protein Li 281; testicular
                     secretory protein Li 25"
                     /calculated_mol_wt=30065
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.4;
                     propagated from UniProtKB/Swiss-Prot (P07195.2)"
     Site            7
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P07195.2)"
     Region          20..272
                     /region_name="LDH_1"
                     /note="A subgroup of L-lactate dehydrogenases; cd05293"
                     /db_xref="CDD:133429"
     Site            order(21,124,127,129,146,151,208..210,213,240..241,244,
                     246..248)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:133429"
     Site            order(34,39,61..62,65,67..68,112,114..115,121,187..188,
                     191..194)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133429"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P07195.2)"
     Site            58
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P07195.2)"
     CDS             1..276
                     /gene="LDHB"
                     /gene_synonym="HEL-S-281; LDH-B; LDH-H; LDHBD; TRG-5"
                     /coded_by="NM_001414233.1:99..929"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:3945"
                     /db_xref="HGNC:HGNC:6541"
                     /db_xref="MIM:150100"
ORIGIN      
        1 matlkeklia pvaeeeatvp nnkitvvgvg qvgmacaisi lgksladela lvdvledklk
       61 gemmdlqhgs lflqtpkiva dkvdiltyvt wklsglpkhr vigsgcnlds arfrylmaek
      121 lgihpsschg wilgehgdss vavwsgvnva gvslqelnpe mgtdndsenw kevhkmvves
      181 ayeviklkgy tnwaiglsva dliesmlknl srihpvstmv kgmygienev flslpcilna
      241 rgltsvinqk lkddevaqlk ksadtlwdiq kdlkdl
//
LOCUS       NP_001415185              94 aa            linear   PRI 21-NOV-2025
DEFINITION  oocyte-expressed protein homolog isoform 2 [Homo sapiens].
ACCESSION   NP_001415185
VERSION     NP_001415185.1
DBSOURCE    REFSEQ: accession NM_001428256.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Chi,P., Ou,G., Liu,S., Ma,Q., Lu,Y., Li,J., Li,J., Qi,Q., Han,Z.,
            Zhang,Z., Liu,Q., Guo,L., Chen,J., Wang,X., Huang,W., Li,L. and
            Deng,D.
  TITLE     Cryo-EM structure of the human subcortical maternal complex and the
            associated discovery of infertility-associated variants
  JOURNAL   Nat Struct Mol Biol 31 (11), 1798-1807 (2024)
   PUBMED   39379527
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Tong,X., Jin,J., Hu,Z., Zhang,Y., Fan,H.Y., Zhang,Y.L. and Zhang,S.
  TITLE     Mutations in OOEP and NLRP5 identified in infertile patients with
            early embryonic arrest
  JOURNAL   Hum Mutat 43 (12), 1909-1920 (2022)
   PUBMED   35946397
  REMARK    GeneRIF: Mutations in OOEP and NLRP5 identified in infertile
            patients with early embryonic arrest.
REFERENCE   3  (residues 1 to 94)
  AUTHORS   Liu,J., Tan,Z., He,J., Jin,T., Han,Y., Hu,L. and Huang,S.
  TITLE     Two novel mutations in PADI6 and TLE6 genes cause female
            infertility due to arrest in embryonic development
  JOURNAL   J Assist Reprod Genet 38 (6), 1551-1559 (2021)
   PUBMED   34036456
REFERENCE   4  (residues 1 to 94)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 94)
  AUTHORS   Bebbere,D., Masala,L., Albertini,D.F. and Ledda,S.
  TITLE     The subcortical maternal complex: multiple functions for one
            biological structure?
  JOURNAL   J Assist Reprod Genet 33 (11), 1431-1438 (2016)
   PUBMED   27525657
  REMARK    Review article
REFERENCE   6  (residues 1 to 94)
  AUTHORS   Alazami,A.M., Awad,S.M., Coskun,S., Al-Hassan,S., Hijazi,H.,
            Abdulwahab,F.M., Poizat,C. and Alkuraya,F.S.
  TITLE     TLE6 mutation causes the earliest known human embryonic lethality
  JOURNAL   Genome Biol 16, 240 (2015)
   PUBMED   26537248
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 94)
  AUTHORS   Zhu,K., Yan,L., Zhang,X., Lu,X., Wang,T., Yan,J., Liu,X., Qiao,J.
            and Li,L.
  TITLE     Identification of a human subcortical maternal complex
  JOURNAL   Mol Hum Reprod 21 (4), 320-329 (2015)
   PUBMED   25542835
REFERENCE   8  (residues 1 to 94)
  AUTHORS   Pierre,A., Gautier,M., Callebaut,I., Bontoux,M., Jeanpierre,E.,
            Pontarotti,P. and Monget,P.
  TITLE     Atypical structure and phylogenomic evolution of the new eutherian
            oocyte- and embryo-expressed KHDC1/DPPA5/ECAT1/OOEP gene family
  JOURNAL   Genomics 90 (5), 583-594 (2007)
   PUBMED   17913455
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019205.4 and KF459597.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.257662.1,
                                           SRR14372080.137378.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149178, SAMEA2161674
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..94
                     /product="oocyte-expressed protein homolog isoform 2"
                     /note="KH homology domain containing 2; oocyte and embryo
                     protein 19; oocyte-expressed protein homolog; oocyte- and
                     embryo-specific protein 19; KH homology domain-containing
                     protein 2; oocyte expressed protein homolog (dog)"
                     /calculated_mol_wt=10592
     Region          <9..77
                     /region_name="FILIA_N_like"
                     /note="FILIA-N KH-like domain; cd12795"
                     /db_xref="CDD:240613"
     Site            order(14,16..18,21..23,46..47,50,54,57..58,61)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:240613"
     CDS             1..94
                     /gene="OOEP"
                     /gene_synonym="C6orf156; FLOPED; HOEP19; KHDC2"
                     /coded_by="NM_001428256.1:794..1078"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:441161"
                     /db_xref="HGNC:HGNC:21382"
                     /db_xref="MIM:611689"
ORIGIN      
        1 mfstvthkgp draiipemew tsqalltvdi vdsgnlveit vfgrprvqnr vksmllclaw
       61 fhrehrarae kmkhleknlk ahasdphspq dpva
//
LOCUS       NP_001411256             115 aa            linear   PRI 21-NOV-2025
DEFINITION  protein cholesin isoform f [Homo sapiens].
ACCESSION   NP_001411256
VERSION     NP_001411256.1
DBSOURCE    REFSEQ: accession NM_001424327.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Ryk,A., Marcinkiewicz,A., Chrzanowski,J., Michalak,A.M., Drozdz,I.,
            Burzynski,J., Krejca,M. and Fendler,W.
  TITLE     Cholesin receptor signalling is active in cardiovascular
            system-associated adipose tissue and correlates with SGLT2i
            treatment in patients with diabetes
  JOURNAL   Cardiovasc Diabetol 23 (1), 211 (2024)
   PUBMED   38902687
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Hu,X., Chen,F., Jia,L., Long,A., Peng,Y., Li,X., Huang,J., Wei,X.,
            Fang,X., Gao,Z., Zhang,M., Liu,X., Chen,Y.G., Wang,Y., Zhang,H. and
            Wang,Y.
  TITLE     A gut-derived hormone regulates cholesterol metabolism
  JOURNAL   Cell 187 (7), 1685-1700 (2024)
   PUBMED   38503280
  REMARK    GeneRIF: A gut-derived hormone regulates cholesterol metabolism.
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Willer,C.J., Schmidt,E.M., Sengupta,S., Peloso,G.M., Gustafsson,S.,
            Kanoni,S., Ganna,A., Chen,J., Buchkovich,M.L., Mora,S.,
            Beckmann,J.S., Bragg-Gresham,J.L., Chang,H.Y., Demirkan,A., Den
            Hertog,H.M., Do,R., Donnelly,L.A., Ehret,G.B., Esko,T.,
            Feitosa,M.F., Ferreira,T., Fischer,K., Fontanillas,P., Fraser,R.M.,
            Freitag,D.F., Gurdasani,D., Heikkila,K., Hypponen,E., Isaacs,A.,
            Jackson,A.U., Johansson,A., Johnson,T., Kaakinen,M., Kettunen,J.,
            Kleber,M.E., Li,X., Luan,J., Lyytikainen,L.P., Magnusson,P.K.E.,
            Mangino,M., Mihailov,E., Montasser,M.E., Muller-Nurasyid,M.,
            Nolte,I.M., O'Connell,J.R., Palmer,C.D., Perola,M., Petersen,A.K.,
            Sanna,S., Saxena,R., Service,S.K., Shah,S., Shungin,D., Sidore,C.,
            Song,C., Strawbridge,R.J., Surakka,I., Tanaka,T., Teslovich,T.M.,
            Thorleifsson,G., Van den Herik,E.G., Voight,B.F., Volcik,K.A.,
            Waite,L.L., Wong,A., Wu,Y., Zhang,W., Absher,D., Asiki,G.,
            Barroso,I., Been,L.F., Bolton,J.L., Bonnycastle,L.L., Brambilla,P.,
            Burnett,M.S., Cesana,G., Dimitriou,M., Doney,A.S.F., Doring,A.,
            Elliott,P., Epstein,S.E., Ingi Eyjolfsson,G., Gigante,B.,
            Goodarzi,M.O., Grallert,H., Gravito,M.L., Groves,C.J., Hallmans,G.,
            Hartikainen,A.L., Hayward,C., Hernandez,D., Hicks,A.A., Holm,H.,
            Hung,Y.J., Illig,T., Jones,M.R., Kaleebu,P., Kastelein,J.J.P.,
            Khaw,K.T., Kim,E., Klopp,N., Komulainen,P., Kumari,M.,
            Langenberg,C., Lehtimaki,T., Lin,S.Y., Lindstrom,J., Loos,R.J.F.,
            Mach,F., McArdle,W.L., Meisinger,C., Mitchell,B.D., Muller,G.,
            Nagaraja,R., Narisu,N., Nieminen,T.V.M., Nsubuga,R.N., Olafsson,I.,
            Ong,K.K., Palotie,A., Papamarkou,T., Pomilla,C., Pouta,A.,
            Rader,D.J., Reilly,M.P., Ridker,P.M., Rivadeneira,F., Rudan,I.,
            Ruokonen,A., Samani,N., Scharnagl,H., Seeley,J., Silander,K.,
            Stancakova,A., Stirrups,K., Swift,A.J., Tiret,L.,
            Uitterlinden,A.G., van Pelt,L.J., Vedantam,S., Wainwright,N.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilsgaard,T., Wilson,J.F.,
            Young,E.H., Zhao,J.H., Adair,L.S., Arveiler,D., Assimes,T.L.,
            Bandinelli,S., Bennett,F., Bochud,M., Boehm,B.O., Boomsma,D.I.,
            Borecki,I.B., Bornstein,S.R., Bovet,P., Burnier,M., Campbell,H.,
            Chakravarti,A., Chambers,J.C., Chen,Y.I., Collins,F.S.,
            Cooper,R.S., Danesh,J., Dedoussis,G., de Faire,U., Feranil,A.B.,
            Ferrieres,J., Ferrucci,L., Freimer,N.B., Gieger,C., Groop,L.C.,
            Gudnason,V., Gyllensten,U., Hamsten,A., Harris,T.B., Hingorani,A.,
            Hirschhorn,J.N., Hofman,A., Hovingh,G.K., Hsiung,C.A.,
            Humphries,S.E., Hunt,S.C., Hveem,K., Iribarren,C., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kaprio,J., Kesaniemi,A., Kivimaki,M.,
            Kooner,J.S., Koudstaal,P.J., Krauss,R.M., Kuh,D., Kuusisto,J.,
            Kyvik,K.O., Laakso,M., Lakka,T.A., Lind,L., Lindgren,C.M.,
            Martin,N.G., Marz,W., McCarthy,M.I., McKenzie,C.A., Meneton,P.,
            Metspalu,A., Moilanen,L., Morris,A.D., Munroe,P.B., Njolstad,I.,
            Pedersen,N.L., Power,C., Pramstaller,P.P., Price,J.F., Psaty,B.M.,
            Quertermous,T., Rauramaa,R., Saleheen,D., Salomaa,V.,
            Sanghera,D.K., Saramies,J., Schwarz,P.E.H., Sheu,W.H.,
            Shuldiner,A.R., Siegbahn,A., Spector,T.D., Stefansson,K.,
            Strachan,D.P., Tayo,B.O., Tremoli,E., Tuomilehto,J., Uusitupa,M.,
            van Duijn,C.M., Vollenweider,P., Wallentin,L., Wareham,N.J.,
            Whitfield,J.B., Wolffenbuttel,B.H.R., Ordovas,J.M., Boerwinkle,E.,
            Palmer,C.N.A., Thorsteinsdottir,U., Chasman,D.I., Rotter,J.I.,
            Franks,P.W., Ripatti,S., Cupples,L.A., Sandhu,M.S., Rich,S.S.,
            Boehnke,M., Deloukas,P., Kathiresan,S., Mohlke,K.L., Ingelsson,E.
            and Abecasis,G.R.
  CONSRTM   Global Lipids Genetics Consortium
  TITLE     Discovery and refinement of loci associated with lipid levels
  JOURNAL   Nat Genet 45 (11), 1274-1283 (2013)
   PUBMED   24097068
REFERENCE   7  (residues 1 to 115)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 115)
  AUTHORS   Yashin,A.I., Wu,D., Arbeev,K.G. and Ukraintseva,S.V.
  TITLE     Joint influence of small-effect genetic variants on human longevity
  JOURNAL   Aging (Albany NY) 2 (9), 612-620 (2010)
   PUBMED   20834067
REFERENCE   9  (residues 1 to 115)
  AUTHORS   Satoh,J., Obayashi,S., Misawa,T., Sumiyoshi,K., Oosumi,K. and
            Tabunoki,H.
  TITLE     Protein microarray analysis identifies human cellular prion protein
            interactors
  JOURNAL   Neuropathol Appl Neurobiol 35 (1), 16-35 (2009)
   PUBMED   18482256
REFERENCE   10 (residues 1 to 115)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073957.7.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.707871.1,
                                           ERR4352442.150439.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..115
                     /product="protein cholesin isoform f"
                     /note="uncharacterized protein C7orf50; protein cholesin"
                     /calculated_mol_wt=12817
     Region          <1..36
                     /region_name="WKF"
                     /note="WKF domain; pfam10180"
                     /db_xref="CDD:462982"
     CDS             1..115
                     /gene="CHLSN"
                     /gene_synonym="C7orf50; YCR016W"
                     /coded_by="NM_001424327.1:371..718"
                     /note="isoform f is encoded by transcript variant 17"
                     /db_xref="GeneID:84310"
                     /db_xref="HGNC:HGNC:22421"
                     /db_xref="MIM:621174"
ORIGIN      
        1 mydsdkvpde hfstllayle glqgrarelt vqkaealmre ldeegsdppl pgraqrirqe
       61 glwsspfvtq ssrgqkpcll ippvefhgtl lqctrdppdi kkelslgsvt rfpei
//
LOCUS       NP_001401584             531 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 2 isoform c [Homo sapiens].
ACCESSION   NP_001401584 XP_016874838
VERSION     NP_001401584.1
DBSOURCE    REFSEQ: accession NM_001414655.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Jung,J.H., Lee,D., Ko,H.M. and Jang,H.J.
  TITLE     Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in Colorectal
            Cancer Cells by Activating p53
  JOURNAL   Biomolecules 11 (10), 1492 (2021)
   PUBMED   34680125
  REMARK    GeneRIF: Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in
            Colorectal Cancer Cells by Activating p53.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Royer-Bertrand,B., Cisarova,K., Niel Butschi,F., Foletti,G.,
            Guinchat,V., Tran,C., Superti-Furga,A. and Good,J.M.
  TITLE     CNOT2 haploinsufficiency in a 40-year-old man with intellectual
            disability, autism, and seizures
  JOURNAL   Am J Med Genet A 185 (8), 2602-2606 (2021)
   PUBMED   34018673
  REMARK    GeneRIF: CNOT2 haploinsufficiency in a 40-year-old man with
            intellectual disability, autism, and seizures.
            Review article
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Jayne,S., Zwartjes,C.G., van Schaik,F.M. and Timmers,H.T.
  TITLE     Involvement of the SMRT/NCoR-HDAC3 complex in transcriptional
            repression by the CNOT2 subunit of the human Ccr4-Not complex
  JOURNAL   Biochem J 398 (3), 461-467 (2006)
   PUBMED   16712523
  REMARK    GeneRIF: This study shows that SMRT/NCoR-HDAC3 complex is a
            cofactor of CNOT2-mediated repression and suggests that
            transcriptional regulation by the Ccr4-Not complex involves
            regulation of chromatin modification.
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Winkler,G.S., Mulder,K.W., Bardwell,V.J., Kalkhoven,E. and
            Timmers,H.T.
  TITLE     Human Ccr4-Not complex is a ligand-dependent repressor of nuclear
            receptor-mediated transcription
  JOURNAL   EMBO J 25 (13), 3089-3099 (2006)
   PUBMED   16778766
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Shi,J. and Nelson,M.A.
  TITLE     The cyclin-dependent kinase 11 interacts with NOT2
  JOURNAL   Biochem Biophys Res Commun 334 (4), 1310-1316 (2005)
   PUBMED   16039607
  REMARK    GeneRIF: These findings suggest that CDK11 may contribute to
            apoptosis by regulating the activity of NOT2 independent of its
            kinase activity.
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Zwartjes,C.G., Jayne,S., van den Berg,D.L. and Timmers,H.T.
  TITLE     Repression of promoter activity by CNOT2, a subunit of the
            transcription regulatory Ccr4-not complex
  JOURNAL   J Biol Chem 279 (12), 10848-10854 (2004)
   PUBMED   14707134
  REMARK    GeneRIF: major repression function of CNOT2 is localized in a
            specialized protein motif, the Not-Box
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Denis,C.L. and Chen,J.
  TITLE     The CCR4-NOT complex plays diverse roles in mRNA metabolism
  JOURNAL   Prog Nucleic Acid Res Mol Biol 73, 221-250 (2003)
   PUBMED   12882519
  REMARK    Review article
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092881.8 and AC025569.37.
            
            On Feb 21, 2023 this sequence version replaced XP_016874838.1.
            
            Summary: This gene encodes a subunit of the multi-component
            CCR4-NOT complex. The CCR4-NOT complex regulates mRNA synthesis and
            degradation and is also thought to be involved in mRNA splicing,
            transport and localization. The encoded protein interacts with
            histone deacetylases and functions as a repressor of polymerase II
            transcription. Alternatively spliced transcript variants have been
            observed for this gene. [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4239917.1,
                                           SRR1660809.248721.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..531
                     /product="CCR4-NOT transcription complex subunit 2 isoform
                     c"
                     /note="negative regulator of transcription 2;
                     CCR4-associated factor 2; CC chemokine receptor 4-negative
                     regulator of transcription 2"
                     /calculated_mol_wt=58490
     Region          387..510
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..531
                     /gene="CNOT2"
                     /gene_synonym="CDC36; HSPC131; IDNADFS; NOT2; NOT2H"
                     /coded_by="NM_001414655.1:582..2177"
                     /note="isoform c is encoded by transcript variant 9"
                     /db_xref="GeneID:4848"
                     /db_xref="HGNC:HGNC:7878"
                     /db_xref="MIM:604909"
ORIGIN      
        1 mlkevaqvtn smfgasrkkf vegvdsdyhd enmyysqssm fphrsekdml aspstsgqls
       61 qfgaslygqq salglpmrgm snntpqlnrs lsqgtqlpsh vtpttgvptm slhtppspsr
      121 gilpmnprnm mnhsqvgqgi gipsrtnsms ssglgspnrs spsiicmpkq qpsrqpftvn
      181 smsgfgmnrn qafgmnnsls snifngtdgs envtgldlsd fpaladrnrr egsgnptpli
      241 nplagrapyv gmvtkpaneq sqdfsihned fpalpgssyk dptssnddsk snlntsgktt
      301 sstdgpkfpg dkssttqnnn qqkkgiqvlp dgrvtnipqg mvtdqfgmig lltfiraaet
      361 dpgmvhlalg sdlttlglnl nspenlypkf aspwasspcr pqdidfhvps eyltnihird
      421 klaaiklgry gedllfylyy mnggdvlqll aavelfnrdw ryhkeervwi trapgmeptm
      481 ktntyergty yffdclnwrk vakefhleyd kleerphlps tfnynpaqqa f
//
LOCUS       NP_001425991            2500 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HECTD1 isoform 10 [Homo sapiens].
ACCESSION   NP_001425991 XP_047287163 XP_054231757
VERSION     NP_001425991.1
DBSOURCE    REFSEQ: accession NM_001439062.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2500)
  AUTHORS   Oxman,E., Li,H., Wang,H.Y. and Zohn,I.E.
  TITLE     Identification and functional analysis of rare HECTD1 missense
            variants in human neural tube defects
  JOURNAL   Hum Genet 143 (3), 263-277 (2024)
   PUBMED   38451291
  REMARK    GeneRIF: Identification and functional analysis of rare HECTD1
            missense variants in human neural tube defects.
REFERENCE   2  (residues 1 to 2500)
  AUTHORS   Zhang,J., Xin,Y., Ling,X., Liang,H., Zhang,L., Fang,C. and Ma,J.
  TITLE     Nucleoporin 93, a new substrate of the E3 ubiquitin protein ligase
            HECTD1, promotes esophageal squamous cell carcinoma progression
  JOURNAL   Hum Cell 37 (1), 245-257 (2024)
   PUBMED   37993750
  REMARK    GeneRIF: Nucleoporin 93, a new substrate of the E3 ubiquitin
            protein ligase HECTD1, promotes esophageal squamous cell carcinoma
            progression.
REFERENCE   3  (residues 1 to 2500)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 2500)
  AUTHORS   Vaughan,N., Scholz,N., Lindon,C. and Licchesi,J.D.F.
  TITLE     The E3 ubiquitin ligase HECTD1 contributes to cell proliferation
            through an effect on mitosis
  JOURNAL   Sci Rep 12 (1), 13160 (2022)
   PUBMED   35915203
  REMARK    GeneRIF: The E3 ubiquitin ligase HECTD1 contributes to cell
            proliferation through an effect on mitosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2500)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 2500)
  AUTHORS   Aleidi,S.M., Yang,A., Sharpe,L.J., Rao,G., Cochran,B.J., Rye,K.A.,
            Kockx,M., Brown,A.J. and Gelissen,I.C.
  TITLE     The E3 ubiquitin ligase, HECTD1, is involved in ABCA1-mediated
            cholesterol export from macrophages
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1863 (4), 359-368 (2018)
   PUBMED   29306077
  REMARK    GeneRIF: HECTD1 may be involved in the regulation of ABCA1-mediated
            cholesterol export from unloaded macrophages to apoA-I.
REFERENCE   7  (residues 1 to 2500)
  AUTHORS   Fang,S., Guo,H., Cheng,Y., Zhou,Z., Zhang,W., Han,B., Luo,W.,
            Wang,J., Xie,W. and Chao,J.
  TITLE     circHECTD1 promotes the silica-induced pulmonary
            endothelial-mesenchymal transition via HECTD1
  JOURNAL   Cell Death Dis 9 (3), 396 (2018)
   PUBMED   29540674
  REMARK    GeneRIF: SiO2 concomitantly increased circHECTD1 expression, which,
            in turn, inhibited HECTD1 protein expression.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 2500)
  AUTHORS   Shen,X., Jia,Z., D'Alonzo,D., Wang,X., Bruder,E., Emch,F.H., De
            Geyter,C. and Zhang,H.
  TITLE     HECTD1 controls the protein level of IQGAP1 to regulate the
            dynamics of adhesive structures
  JOURNAL   Cell Commun Signal 15 (1), 2 (2017)
   PUBMED   28073378
  REMARK    GeneRIF: Hectd1 regulates the protein level of IQGAP1 through
            ubiquitination.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 2500)
  AUTHORS   Helander,S., Montecchio,M., Lemak,A., Fares,C., Almlof,J., Yi,Y.,
            Yee,A., Arrowsmith,C., DhePaganon,S. and Sunnerhagen,M.
  TITLE     Basic Tilted Helix Bundle - a new protein fold in human
            FKBP25/FKBP3 and HectD1
  JOURNAL   Biochem Biophys Res Commun 447 (1), 26-31 (2014)
   PUBMED   24667607
  REMARK    GeneRIF: our high-resolution structures show a new fold composed of
            five small helices where H3 and H4 are tilted in a novel
            arrangement; we call this fold the Basic Tilted Helix Bundle (BTHB)
            domain.
REFERENCE   10 (residues 1 to 2500)
  AUTHORS   Tran,H., Bustos,D., Yeh,R., Rubinfeld,B., Lam,C., Shriver,S.,
            Zilberleyb,I., Lee,M.W., Phu,L., Sarkar,A.A., Zohn,I.E.,
            Wertz,I.E., Kirkpatrick,D.S. and Polakis,P.
  TITLE     HectD1 E3 ligase modifies adenomatous polyposis coli (APC) with
            polyubiquitin to promote the APC-axin interaction
  JOURNAL   J Biol Chem 288 (6), 3753-3767 (2013)
   PUBMED   23277359
  REMARK    GeneRIF: HectD1 promotes the APC-Axin interaction to negatively
            regulate Wnt signaling.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136418.4, AL121808.4 and KC877516.1.
            
            On or before Apr 25, 2025 this sequence version replaced
            XP_047287163.1, XP_054231757.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3505180.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2500
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..2500
                     /product="E3 ubiquitin-protein ligase HECTD1 isoform 10"
                     /EC_number="2.3.2.26"
                     /note="E3 ubiquitin-protein ligase HECTD1; E3 ligase for
                     inhibin receptor; HECT domain-containing protein 1; HECT
                     domain containing E3 ubiquitin protein ligase 1; HECT-type
                     E3 ubiquitin transferase HECTD1"
                     /calculated_mol_wt=277047
     Region          <366..>479
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          366..393
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          396..426
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(397,401..402,405..407,409..410,414,417,426,428,
                     432..433,436..438,440..441,445,448,457,459,461,465..466,
                     469..471,473..474,478)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          428..457
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1107..1240
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     Region          1277..>1321
                     /region_name="MIB_HERC2"
                     /note="Mib_herc2; pfam06701"
                     /db_xref="CDD:461991"
     Region          2021..2498
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(2027,2056,2066,2153,2431,2463..2464,2467..2471,2491,
                     2497)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(2246,2249..2250,2252..2253,2256,2298,2300,
                     2304..2305,2307,2313,2318,2335,2339)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..2500
                     /gene="HECTD1"
                     /gene_synonym="EULIR"
                     /coded_by="NM_001439062.1:800..8302"
                     /note="isoform 10 is encoded by transcript variant 11"
                     /db_xref="GeneID:25831"
                     /db_xref="HGNC:HGNC:20157"
                     /db_xref="MIM:618649"
ORIGIN      
        1 madvdpdtll ewlqmgqgde rdmqlialeq lcmlllmsdn vdrcfetcpp rtflpalcki
       61 fldesapdnv levtaraity yldvsaectr rivgvdgaik alcnrlvvve lnnrtsrdla
      121 eqcvkvleli ctresgavfe agglncvltf irdsghlvhk dtlhsamavv srlcgkmepq
      181 dssleicves lssllkhedh qvsdgalrcf asladrftrr gvdpaplakh glteellsrm
      241 aaaggtvsgp ssackpgrst tgapsttads klsnqvstiv sllstlcrgs pvvthdllrs
      301 elpdsiesal qgdercvldt mrlvdlllvl lfegrkalpk ssagstgrip glrrldssge
      361 rshrqlidci rskdtdalid aidtgafevn fmddvgqtll nwasafgtqe mveflcerga
      421 dvnrgqrsss lhyaacfgrp qvaktllrhg anpdlrdedg ktpldkarer ghsevvailq
      481 spgdwmcpvn kgddkkkkdt nkdeeecnep kgdpemapiy lkrllpvfaq tfqqtmlpsi
      541 rkaslalirk mihfcseall kevcdsdvgh nlptilveit atvldqeddd dghllalqii
      601 rdlvdkggdi fldqlarlgv iskvstlagp ssddeneees kpekedepqe dakelqqgkp
      661 yhwrdwsiir grdclyiwsd aaalelsngs ngwfrfildg klatmyssgs peggsdsses
      721 rsefleklqr argqvkpsts sqpilsapgp tkltvgnwsl tclkegeiai hnsdgqqati
      781 lkedlpgfvf esnrgtkhsf taetslgsef vtgwtgkrgr klksklektk qkvrtmardl
      841 yddhfkaves mprgvvvtlr niatqlessw elhtnrqcie sentwrdlmk talenlivll
      901 kdentispye mcssglvqal ltvlnnsmdl dmkqdcsqlv erinvfktaf seneddesrp
      961 avalirklia vlesierlpl hlydtpgsty nlqiltrrlr frlerapget alidrtgrml
     1021 kmeplatves leqyllkmva kqwydfdrss fvfvrklreg qnfifrhqhd fdengiiywi
     1081 gtnaktayew vnpaayglvv vtssegrnlp ygrledilsr dnsalnchsn ddknawfaid
     1141 lglwvipsay tlrhargygr salrnwvfqv skdgqnwtsl ythvddcsln epgstatwpl
     1201 dppkdekqgw rhvrikqmgk nasgqthyls lsgfelygtv ngvcedqlgk aakeaeanlr
     1261 rqrrlvrsqv lkymvpgarv irgldwkwrd qdgspqgegt vtgelhngtt qswsslvknn
     1321 cpdktsaaag sssrkgssss vcsvasssdi slgstkterr seivmehsiv sgadvhepiv
     1381 vlssaenvpq tevgssssas tstltaetgs enaerklgpd ssvrtpgess aismgivsvs
     1441 spdvssvsel tnkeaasqrp lsssasnrls vssllaagap msssasvpnl ssretssles
     1501 fvrrvaniar tnatnnmnls rsssdnntnt lgrnvmstat splmgaqsfp nlttpgttst
     1561 vtmstssvts ssnvatattv lsvgqslsnt lttsltstss esdtgqeaey slydfldscr
     1621 astllaeldd dedlpepdee ddeneddnqe dqeyeeilrr pslqrragsr sdvthhavts
     1681 qlpqvpagag srpigeqeee eyetkggrrr twdddyvlkr qfsalvpafd prpgrtnvqq
     1741 ttdleipppg tphselleev ectpsprlal tlkvtglgtt revelpltnf rstifyyvqk
     1801 llqlscngnv ksdklrriwe ptytimyrem kdsdkekeng kmdfcehgtk sglnqgaist
     1861 lqssdilnlt keqpqakagn gqnscgvedv lqllrilyiv asdpysrisq edgdeqpqft
     1921 fppdeftskk ittkilqqie eplalasgal pdwceqltsk cpflipfetr qlyftctafg
     1981 asraivwlqn rreatvertr ttssvrrddp gefrvgrlkh ervkvprges lmewaenvmq
     2041 ihadrksvle veflgeegtg lgptlefyal vaaefqrtdl gawlcddnfp ddesrhvdlg
     2101 gglkppgyyv qrscglftap fpqdsdeler itklfhflgi flakciqdnr lvdlpiskpf
     2161 fklmcmgdik snmskliyes rgdrdlhcte sqseasteeg hdslsvgsfe edsksefild
     2221 ppkpkppawf ngiltwedfe lvnphrarfl keikdlaikr rqilsnkgls edekntklqe
     2281 lvlknpsgsg pplsiedlgl nfqfcpssri ygftavdlkp sgedemitmd naeeyvdlmf
     2341 dfcmhtgiqk qmeafrdgfn kvfpmeklss fsheevqmil cgnqspswaa ediinytepk
     2401 lgytrdspgf lrfvrvlcgm ssderkaflq fttgcstlpp gglanlhprl tvvrkvdatd
     2461 asypsvntcv hylklpeyss eeimrerlla atmekgfhln
//
LOCUS       NP_001427980            4373 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HUWE1 isoform 5 [Homo sapiens].
ACCESSION   NP_001427980 XP_047297690 XP_054182285
VERSION     NP_001427980.1
DBSOURCE    REFSEQ: accession NM_001441051.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4373)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 4373)
  AUTHORS   Lee,C., Park,S.H. and Yoon,S.K.
  TITLE     The E3 ligase HUWE1 increases the sensitivity of CRC to oxaliplatin
            through TOMM20 degradation
  JOURNAL   Oncogene 43 (9), 636-649 (2024)
   PUBMED   38184713
  REMARK    GeneRIF: The E3 ligase HUWE1 increases the sensitivity of CRC to
            oxaliplatin through TOMM20 degradation.
REFERENCE   3  (residues 1 to 4373)
  AUTHORS   Li,X.X., Xu,J.K., Su,W.J., Wu,H.L., Zhao,K., Zhang,C.M., Chen,X.K.
            and Yang,L.X.
  TITLE     The role of KDM4A-mediated histone methylation on temozolomide
            resistance in glioma cells through the HUWE1/ROCK2 axis
  JOURNAL   Kaohsiung J Med Sci 40 (2), 161-174 (2024)
   PUBMED   37873881
  REMARK    GeneRIF: The role of KDM4A-mediated histone methylation on
            temozolomide resistance in glioma cells through the HUWE1/ROCK2
            axis.
REFERENCE   4  (residues 1 to 4373)
  AUTHORS   Bernassola,F., Karin,M., Ciechanover,A. and Melino,G.
  TITLE     The HECT family of E3 ubiquitin ligases: multiple players in cancer
            development
  JOURNAL   Cancer Cell 14 (1), 10-21 (2008)
   PUBMED   18598940
  REMARK    Review article
REFERENCE   5  (residues 1 to 4373)
  AUTHORS   Zhong,Q., Gao,W., Du,F. and Wang,X.
  TITLE     Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the
            polyubiquitination of Mcl-1 and regulates apoptosis
  JOURNAL   Cell 121 (7), 1085-1095 (2005)
   PUBMED   15989957
  REMARK    GeneRIF: Mule is both required and sufficient for the
            polyubiquitination of Mcl-1; Mule is a unique BH3-containing E3
            ubiquitin ligase apical to Bcl-2 family proteins during DNA
            damage-induced apoptosis
            GeneRIF: Mule (HUWE1) poly-ubiquitinates anti-apoptotic gene Mcl-1.
REFERENCE   6  (residues 1 to 4373)
  AUTHORS   Chen,D., Kon,N., Li,M., Zhang,W., Qin,J. and Gu,W.
  TITLE     ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
  JOURNAL   Cell 121 (7), 1071-1083 (2005)
   PUBMED   15989956
  REMARK    GeneRIF: study modifies the current view of ARF-mediated p53
            activation and reveals that ARF-BP1 is a critical mediator of both
            the p53-independent and p53-dependent tumor suppressor functions of
            ARF
            GeneRIF: Ubiquitin ligase activity of ARF-BP1 (HUWE1) is inhibited
            by Arf.
REFERENCE   7  (residues 1 to 4373)
  AUTHORS   Liu,Z., Oughtred,R. and Wing,S.S.
  TITLE     Characterization of E3Histone, a novel testis ubiquitin protein
            ligase which ubiquitinates histones
  JOURNAL   Mol Cell Biol 25 (7), 2819-2831 (2005)
   PUBMED   15767685
REFERENCE   8  (residues 1 to 4373)
  AUTHORS   Gu,J., Dubner,R., Fornace,A.J. Jr. and Iadarola,M.J.
  TITLE     UREB1, a tyrosine phosphorylated nuclear protein, inhibits p53
            transactivation
  JOURNAL   Oncogene 11 (10), 2175-2178 (1995)
   PUBMED   7478539
REFERENCE   9  (residues 1 to 4373)
  AUTHORS   Turner,G., Gedeon,A. and Mulley,J.
  TITLE     X-linked mental retardation with heterozygous expression and
            macrocephaly: pericentromeric gene localization
  JOURNAL   Am J Med Genet 51 (4), 575-580 (1994)
   PUBMED   7943042
REFERENCE   10 (residues 1 to 4373)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX323845.7 and AC231658.3.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297690.1, XP_054182285.1.
            
            Summary: This gene encodes a protein containing a C-terminal HECT
            (E6AP type E3 ubiquitin protein ligase) domain that functions as an
            E3 ubiquitin ligase. The encoded protein is required for the
            ubiquitination and subsequent degradation of the anti-apoptotic
            protein Mcl1 (myeloid cell leukemia sequence 1 (BCL2-related)).
            This protein also ubiquitinates the p53 tumor suppressor, core
            histones, and DNA polymerase beta. Mutations in this gene are
            associated with Turner type X-linked syndromic cognitive
            disability. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2504699.1,
                                           SRR14038197.1658932.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..4373
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..4373
                     /product="E3 ubiquitin-protein ligase HUWE1 isoform 5"
                     /EC_number="2.3.2.26"
                     /note="Mcl-1 ubiquitin ligase E3; BJ-HCC-24 tumor antigen;
                     HECT domain protein LASU1; ARF-binding protein 1;
                     URE-binding protein 1; large structure of UREB1; upstream
                     regulatory element-binding protein 1; homologous to E6AP
                     carboxyl terminus homologous protein 9; HECT-type E3
                     ubiquitin transferase HUWE1; HECT, UBA and WWE domain
                     containing 1, E3 ubiquitin protein ligase"
                     /calculated_mol_wt=481691
     Region          92..367
                     /region_name="DUF908"
                     /note="Domain of Unknown Function (DUF908); pfam06012"
                     /db_xref="CDD:428721"
     Region          431..814
                     /region_name="DUF913"
                     /note="Domain of Unknown Function (DUF913); pfam06025"
                     /db_xref="CDD:461803"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          706..759
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          978..1001
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1014..1037
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1084
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1291..1320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1317..1356
                     /region_name="UBA_HUWE1"
                     /note="UBA domain found in eukaryotic E3 ubiquitin-protein
                     ligase HUWE1 and similar proteins; cd14288"
                     /db_xref="CDD:270474"
     Site            1368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1396..1415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1617..1678
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          1689..1735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1722
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1907
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2017..2064
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2034
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2261..2341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2266
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2355..2479
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2534
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2553
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2594
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2618
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2693..2969
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          <2734..3065
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            2750
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2825
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2832
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2860
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2886
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2887
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2888
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2917
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3009..3042
                     /region_name="UBM"
                     /note="Ubiquitin binding region; pfam14377"
                     /db_xref="CDD:464159"
     Region          3035..3058
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3148
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3244..3266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3403..3423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3470..3511
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3536..3567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3736..3757
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3751
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3780..3847
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3807
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3815
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3826
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3829
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3893..3930
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3905
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3918
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3923
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3926
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          4018..4371
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(4022,4052,4063,4124,4298,4334..4335,4338..4342,4362,
                     4370)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(4152,4155..4156,4158..4159,4162,4169,4171,
                     4175..4176,4178,4183,4188,4205,4209)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     Site            4270
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P51593; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     CDS             1..4373
                     /gene="HUWE1"
                     /gene_synonym="ARF-BP1; HECTH9; HSPC272; Ib772; LASU1;
                     MRXST; MULE; URE-B1; UREB1"
                     /coded_by="NM_001441051.1:394..13515"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:10075"
                     /db_xref="HGNC:HGNC:30892"
                     /db_xref="MIM:300697"
ORIGIN      
        1 mkvdrtklkk tpteapadcr alidklkvcn deqlllelqq iktwnigkce lyhwvdlldr
       61 fdgiladagq tvenmswmlv cdrpereqlk mlllavlnft allieysfsr hlyssiehlt
      121 tllassdmqv vlavlnllyv fskrsnyitr lgsdkrtpll trlqhlaesw ggkengfgla
      181 eccrdlhmmk yppsattlhf efyadpgaev kiekrttsnt lhyihieqld kisespseim
      241 esltkmysip kdkqmllfth irlahgfsnh rkrlqavqar lhaisilvys nalqesansi
      301 lynglieelv dvlqitdkql meikaaslrt ltsivhlert pklssiidct gtasyhgflp
      361 vlvrnciqam idpsmdpyph qfatalfsfl yhlasydagg ealvscgmme allkvikflg
      421 deqdqitfvt ravrvvdlit nldmaafqsh sglsifiyrl ehevdlcrke cpfvikpkiq
      481 rpnttqegee metdmdgvqc ipqraallks mlnflkkaiq dpafsdgirh vmdgslptsl
      541 khiisnaeyy gpslfllate vvtvfvfqep sllsslqdng ltdvmlhall ikdvpatrev
      601 lgslpnvfsa lclnarglqs fvqcqpferl fkvllspdyl pamrrrrssd plgdtasnlg
      661 savdelmrhq ptlktdatta iiklleeicn lgrdpkyicq kpsiqkadgt atappprsnh
      721 aaeeassede eeeevqamqs fnstqqnete pnqqvvgtee ripiplmdyi lnvmkfvesi
      781 lsnnttddhc qefvnqkgll plvtilglpn lpidfptsaa cqavagvcks iltlshepkv
      841 lqegllqlds ilssleplhr piespggsvl lrelacagnv adatlsaqat pllhaltaah
      901 ayimmfvhtc rvgqseirsi svnqwgsqlg lsvlsklsql ycslvwestv llslctpnsl
      961 psgcefgqad mqklvpkdek agttqggkrs dgeqdgaags mdastqglle gigldgdtla
     1021 pmetdeptas dskgkskitp amaarikqik pllsassrlg ralaelfgll vklcvgspvr
     1081 qrrshhaast ttaptpaars tasaltkllt kglswqpppy tptprfrltf ficsvgftsp
     1141 mlfderkypy hlmlqkflcs gghnalfetf nwalsmggkv pvseglehsd lpdgtgefld
     1201 awlmlvekmv npttvlesph slpaklpggv qnfpqfsalr flvvtqkaaf tciknlwnrk
     1261 plkvyggrma esmlailchi lrgepvirer lskekegsrg eedtgqeegg srrepqvnqq
     1321 qlqqlmdmgf trehameall ntstmeqate yllthpppim ggvvrdlsms eedqmmraia
     1381 mslgqdipmd qraespeeva crkeeeerka rekqeeeeak clekfqdadp leqdelhtft
     1441 dtmlpgcfhl ldelpdtvyr vcdlimtaik rngadyrdmi lkqvvnqvwe aadvlikaal
     1501 plttsdtktv sewisqmatl pqasnlatri llltllfeel klpcawvves sgilnvlikl
     1561 levvqpclqa akeqkevqtp kwitpvllli dfyektaiss krraqmtkyl qsnsnnwrwf
     1621 ddrsgrwcsy sasnnstids awksgetsvr ftagrrrytv qfttmvqvne etgnrrpvml
     1681 tllrvprlnk nsknsngqel ektleeskem dikrkenkgn dtplalestn teketsleet
     1741 kigeiliqgl tedmvtvlir acvsmlgvpv dpdtlhatlr lclrltrdhk yammfaelks
     1801 trmilnltqs sgfngftplv tlllrhiied pctlrhtmek vvrsaatsga gsttsgvvsg
     1861 slgsreinyi lrvlgpaacr npdiftevan ccirialpap rgsgtasdde fenlrikgpn
     1921 avqlvkttpl kpsplpvipd tikeviydml nalaayhape edksdpkpgv mtqevgqllq
     1981 dmgddvyqqy rsltrqssdf dtqsgfsins qvfaadgast etsasgtsqg eastpeesrd
     2041 gkkdkegdra seegkqkgkg skplmptsti lrllaelvrs yvgiatlian ysytvgqsel
     2101 ikedcsvlaf vldhllphtq naedkdtpal arlflaslaa agsgtdaqva lvnevkaalg
     2161 ralamaeste kharlqavmc iistimescp stssfyssat aktqhngmnn iirlflkkgl
     2221 vndlarvphs ldlsspnman tvnaalkple tlsrivnqps slfgsksass knkseqdaqg
     2281 asqdsssnqq dpgepgeaev qeedhdvtqt evadgdimdg eaetdsvvia gqpevlssqe
     2341 mqveneledl idellerdgg sgnstiivsr sgedesqedv lmdeapsnls qastlqanre
     2401 dsmnildped eeehtqeeds sgsnededds qdeeeeeeed eeddqeddeg eegdeddddd
     2461 gsemeldedy pdmnasplvr ferfdreddl iiefdnmfss atdippspgn iptthplmvr
     2521 hadhssltlg sgssttrltq gigrsqrtlr qltantghti hvhypgnrqp npplilqrll
     2581 gpsaaadilq lssslplqsr grarllvgnd dvhiiarsdd ellddffhdq statsqagtl
     2641 ssiptaltrw teeckvldae smhdcvsvvk vsivnhlefl rdeeleerre krrkqlaeee
     2701 tkitdkgked kenrdqsaqc tasksndste qnlsdgtpmp dsypttpsst daatsesket
     2761 lgtlqssqqq ptlptppalg evpqelqspa geggsstqll mpvepeelgp trpsgeaett
     2821 qmelspapti tslsperaed sdaltavssq legspmdtss lasctleeav gdtsaagsse
     2881 qpragsstpg dappavaevq grsdgsgesa qppedssppa ssessstrds avaisgadsr
     2941 gileeplpst sseeedplag islpegvdps flaalpddir revlqnqlgi rpptrtapst
     3001 nssapavvgn pgvtevspef laalppaiqe evlaqqraeq qrrelaqnas sdtpmdpvtf
     3061 iqtlpsdlrr svledmedsv lavmppdiaa eaqalrreqe arqrqlmher lfghsstsal
     3121 sailrspaft srlsgnrgvq ytrlavqrgg tfqmggsssh nrpsgsnvdt llrlrgrlll
     3181 dhealscllv llfvdepkln tsrlhrvlrn lcyhaqtrhw virsllsilq rsseselcie
     3241 tpklttseek gkksskscgs sshenrpldl lhkmeskssn qlswlsvsmd aalgcrtnif
     3301 qiqrsggrkh tekhasggst vhihpqaapv vcrhvldtli qlakvfpshf tqqrtketnc
     3361 esdrergnka cspcssqsss sgictdfwdl lvkldnmnvs rkgknsvksv pvsaggeget
     3421 spysleaspl gqlmnmlshp virrssllte kllrllslis ialpenkvse aqansgsgas
     3481 stttatstts tttttaastt ptpptaptpv tsapalvaat aistivvaas ttvttpttat
     3541 ttvsispttk gskspakvsd ggssstdfkm vssgltenql qlsvevltsh scseegleda
     3601 anvllqlsrg dsgtrdtvlk lllngarhlg ytlckqigtl laelreynle qqrraqcetl
     3661 spdglpeeqp qttklkgkmq srfdmaenvv ivasqkrplg grelqlpsms mltsktstqk
     3721 fflrvlqvii qlrddtrran kkakqtgrlg ssglgsassi qaavrqleae adaiiqmvre
     3781 gqrarrqqqa atsessqsea svrreespmd vdqpspsaqd tqsiasdgtp qgekekeerp
     3841 pelpllseql sldelwdmlg eclkeleesh dqhavlvlqp aveafflvha tereskppvr
     3901 dtresqlahi kdeppplspa pltpatpssl dpffsrepss mhissslppd tqkflrfaet
     3961 hrtvlnqilr qstthladgp favlvdyirv ldfdvkrkyf rqelerldeg lrkedmavhv
     4021 rrdhvfedsy relhrkspee mknrlyivfe geegqdaggl lrewymiisr emfnpmyalf
     4081 rtspgdrvty tinpsshcnp nhlsyfkfvg rivakavydn rllecyftrs fykhilgksv
     4141 rytdmesedy hfyqglvyll endvstlgyd ltfstevqef gvcevrdlkp nganilvtee
     4201 nkkeyvhlvc qmrmtgairk qlaaflegfy eiipkrlisi fteqelelli sglptididd
     4261 lksnteyhky qsnsiqiqwf wralrsfdqa drakflqfvt gtskvplqgf aalegmngiq
     4321 kfqihrddrs tdrlpsahtc fnqldlpaye sfeklrhmll laiqecsegf gla
//
LOCUS       NP_001392803            1061 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001392803
VERSION     NP_001392803.1
DBSOURCE    REFSEQ: accession NM_001405874.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1061)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1061)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1061)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1061)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1061)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1061)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1061)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1808272.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1061
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 5"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=116251
     Region          885..>947
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..1061
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405874.1:391..3576"
                     /note="isoform 5 is encoded by transcript variant 15"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankgli
      481 vlgevpppeh ttdlflplss evktdhgtdk liesvsqple nhgapiighi seslstkscg
      541 alrpvngvin tlqpvladhi pgdssdaeeq lhkkqrlnlv ssssdgtcva artrpvlsck
      601 krrlvrpnsi vplskkvhrn stirpgcdvn pscalcgsgs intmppeihy eapllerlsq
      661 ldscvhpvla fpddvptslh fqsmlksqwq nkpfdkikpp kklslkhrap mpgslpdsar
      721 kdrhklvssf lttaklshhq trpdrthrqh lddvgavpmv ervtapkaer llnppppvhd
      781 pnhskmrlrd hssersevlk hhtdmssssy laathhpphs plvrqlstss dspapassss
      841 qvtastsqqp vrrrrgessf dinnivipms vaattrvekl qykeiltpsw revdlqslkg
      901 spdeeneeie dlsdaafaal hakceemera rwlwttsvpp qrrgsrspis pelhsapltp
      961 vardtprhla sedtrcstpe lgldeqsvqp werrtfplah spqaecedql daqeraarct
     1021 rrtsgsktgr eteaaptspp ivplksrhlv aaataqrpth r
//
LOCUS       NP_001425829             424 aa            linear   PRI 21-NOV-2025
DEFINITION  STAM-binding protein isoform 1 [Homo sapiens].
ACCESSION   NP_001425829 XP_047298924 XP_054196180
VERSION     NP_001425829.1
DBSOURCE    REFSEQ: accession NM_001438900.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Zhang,W., Xu,Z., Du,Y., Liu,T., Xiong,Z., Hu,J., Chen,L., Peng,X.
            and Zhou,F.
  TITLE     Identification of STAM-binding protein as a target for the
            treatment of gemcitabine resistance pancreatic cancer in a
            nutrient-poor microenvironment
  JOURNAL   Cell Death Dis 15 (9), 657 (2024)
   PUBMED   39242557
  REMARK    GeneRIF: Identification of STAM-binding protein as a target for the
            treatment of gemcitabine resistance pancreatic cancer in a
            nutrient-poor microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Li,L., Yang,X., He,M., Xu,X., Xuan,X., Zhang,J., Zhang,L., Xu,H.
            and Li,D.
  TITLE     The expression and clinical significance of STAMBP in breast cancer
  JOURNAL   Mol Biol Rep 50 (1), 899-906 (2023)
   PUBMED   36309616
  REMARK    GeneRIF: The expression and clinical significance of STAMBP in
            breast cancer.
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Yang,Q., Yan,D., Zou,C., Xue,Q., Lin,S., Huang,Q., Li,X., Tang,D.,
            Chen,X. and Liu,J.
  TITLE     The deubiquitinating enzyme STAMBP is a newly discovered driver of
            triple-negative breast cancer progression that maintains RAI14
            protein stability
  JOURNAL   Exp Mol Med 54 (11), 2047-2059 (2022)
   PUBMED   36434041
  REMARK    GeneRIF: The deubiquitinating enzyme STAMBP is a newly discovered
            driver of triple-negative breast cancer progression that maintains
            RAI14 protein stability.
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Yu,S., E,C. and Yang,J.
  TITLE     STAM binding protein regulated by hsa_circ_0007334 exerts oncogenic
            potential in pancreatic cancer
  JOURNAL   Pancreatology 22 (7), 1003-1012 (2022)
   PUBMED   36089485
  REMARK    GeneRIF: STAM binding protein regulated by hsa_circ_0007334 exerts
            oncogenic potential in pancreatic cancer.
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Itoh,F., Asao,H., Sugamura,K., Heldin,C.H., ten Dijke,P. and
            Itoh,S.
  TITLE     Promoting bone morphogenetic protein signaling through negative
            regulation of inhibitory Smads
  JOURNAL   EMBO J 20 (15), 4132-4142 (2001)
   PUBMED   11483516
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Endo,K., Takeshita,T., Kasai,H., Sasaki,Y., Tanaka,N., Asao,H.,
            Kikuchi,K., Yamada,M., Chenb,M., O'Shea,J.J. and Sugamura,K.
  TITLE     STAM2, a new member of the STAM family, binding to the Janus
            kinases
  JOURNAL   FEBS Lett 477 (1-2), 55-61 (2000)
   PUBMED   10899310
REFERENCE   8  (residues 1 to 424)
  AUTHORS   Tanaka,N., Kaneko,K., Asao,H., Kasai,H., Endo,Y., Fujita,T.,
            Takeshita,T. and Sugamura,K.
  TITLE     Possible involvement of a novel STAM-associated molecule 'AMSH' in
            intracellular signal transduction mediated by cytokines
  JOURNAL   J Biol Chem 274 (27), 19129-19135 (1999)
   PUBMED   10383417
REFERENCE   9  (residues 1 to 424)
  AUTHORS   Asada,H., Ishii,N., Sasaki,Y., Endo,K., Kasai,H., Tanaka,N.,
            Takeshita,T., Tsuchiya,S., Konno,T. and Sugamura,K.
  TITLE     Grf40, A novel Grb2 family member, is involved in T cell signaling
            through interaction with SLP-76 and LAT
  JOURNAL   J Exp Med 189 (9), 1383-1390 (1999)
   PUBMED   10224278
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Carter,M.T., Mirzaa,G., McDonell,L.M. and Boycott,K.M.
  TITLE     Microcephaly-Capillary Malformation Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24354023
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073046.7.
            
            On or before Apr 25, 2025 this sequence version replaced
            XP_047298924.1, XP_054196180.1.
            
            Summary: Cytokine-mediated signal transduction in the JAK-STAT
            cascade requires the involvement of adaptor molecules. One such
            signal-transducing adaptor molecule contains an SH3 domain that is
            required for induction of MYC and cell growth. The protein encoded
            by this gene binds to the SH3 domain of the signal-transducing
            adaptor molecule, and plays a critical role in cytokine-mediated
            signaling for MYC induction and cell cycle progression. Multiple
            alternatively spliced transcript variants encoding the same protein
            isoform have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.397304.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..424
                     /product="STAM-binding protein isoform 1"
                     /EC_number="3.1.2.15"
                     /note="associated molecule with the SH3 domain of STAM;
                     endosome-associated ubiquitin isopeptidase; testicular
                     secretory protein Li 54"
                     /calculated_mol_wt=47946
     Region          1..127
                     /region_name="Interaction with CHMP3.
                     /evidence=ECO:0000269|PubMed:17146056"
                     /note="propagated from UniProtKB/Swiss-Prot (O95630.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          13..117
                     /region_name="USP8_dimer"
                     /note="USP8 dimerization domain; pfam08969"
                     /db_xref="CDD:462647"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          227..231
                     /region_name="Interaction with STAM.
                     /evidence=ECO:0000269|PubMed:10383417"
                     /note="propagated from UniProtKB/Swiss-Prot (O95630.1)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          254..424
                     /region_name="MPN_AMSH_like"
                     /note="Mov34/MPN/PAD-1 family; cd08066"
                     /db_xref="CDD:163697"
     Site            order(280,335,337,345,348)
                     /site_type="active"
                     /note="MPN+ (JAMM) motif [active]"
                     /db_xref="CDD:163697"
     Site            280
                     /site_type="other"
                     /note="Indirect zinc-binding.
                     /evidence=ECO:0000250|UniProtKB:Q96FJ0; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Site            order(282..284,309..313,316..317,320,323,329..330,333,335,
                     337,345,347..348,350..351,354..355,357..358,395)
                     /site_type="other"
                     /note="Distal ubiquitin recognition interface [polypeptide
                     binding]"
                     /db_xref="CDD:163697"
     Site            order(309,337,340..341,343,345..346,395..397)
                     /site_type="active"
                     /note="Proximal ubiquitin recognition interface [active]"
                     /db_xref="CDD:163697"
     Region          335..348
                     /region_name="JAMM motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01182"
                     /note="propagated from UniProtKB/Swiss-Prot (O95630.1)"
     Site            order(335,337,348)
                     /site_type="other"
                     /note="Zinc-binding site [ion binding]"
                     /db_xref="CDD:163697"
     CDS             1..424
                     /gene="STAMBP"
                     /gene_synonym="AMSH; MICCAP"
                     /coded_by="NM_001438900.1:49..1323"
                     /note="isoform 1 is encoded by transcript variant 18"
                     /db_xref="GeneID:10617"
                     /db_xref="HGNC:HGNC:16950"
                     /db_xref="MIM:606247"
ORIGIN      
        1 msdhgdvslp pedrvralsq lgsavevned ipprryfrsg veiirmasiy seegniehaf
       61 ilynkyitlf ieklpkhrdy ksavipekkd tvkklkeiaf pkaeelkael lkrytkeyte
      121 yneekkkeae elarnmaiqq elekekqrva qqkqqqleqe qfhafeemir nqelekerlk
      181 ivqefgkvdp glggplvpdl ekpsldvfpt ltvssiqpsd chttvrpakp pvvdrslkpg
      241 alsnsesipt idglrhvvvp grlcpqflql asantargve tcgilcgklm rneftithvl
      301 ipkqsagsdy cnteneeelf liqdqqglit lgwihthptq taflssvdlh thcsyqmmlp
      361 esvaivcspk fqetgffklt dhgleeissc rqkgfhphsk dpplfcscsh vtvvdravti
      421 tdlr
//
LOCUS       NP_001394094             923 aa            linear   PRI 21-NOV-2025
DEFINITION  retinoblastoma-associated protein isoform 2 [Homo sapiens].
ACCESSION   NP_001394094
VERSION     NP_001394094.1
DBSOURCE    REFSEQ: accession NM_001407165.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 923)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 923)
  AUTHORS   Castro,A., Ruiz Rivera,A., Moorman,C.C., Wolf-Saxon,E.R.,
            Mims,H.N., Vasquez Meza,V.I., Rangel,M.A., Loera,M.M., Bond,I.C.,
            Buchanan,S.B., Villarreal,E., Tripathi,S., Rubin,S.M. and
            Burke,J.R.
  TITLE     Structural and functional analysis of cancer-associated missense
            variants in the retinoblastoma protein pocket domain
  JOURNAL   J Biol Chem 301 (3), 108284 (2025)
   PUBMED   39938803
REFERENCE   3  (residues 1 to 923)
  AUTHORS   Zhang,S., Valenzuela,L.F., Zatulovskiy,E., Mangiante,L., Curtis,C.
            and Skotheim,J.M.
  TITLE     The G1-S transition is promoted by Rb degradation via the E3 ligase
            UBR5
  JOURNAL   Sci Adv 10 (43), eadq6858 (2024)
   PUBMED   39441926
  REMARK    GeneRIF: The G1-S transition is promoted by Rb degradation via the
            E3 ligase UBR5.
REFERENCE   4  (residues 1 to 923)
  AUTHORS   Schwartz,C.J., Marra,A., Selenica,P., Gazzo,A., Tan,K., Ross,D.,
            Razavi,P., Chandarlapaty,S., Weigelt,B., Reis-Filho,J.S., Brogi,E.,
            Pareja,F. and Wen,H.Y.
  TITLE     RB1 Genetic Alterations in Estrogen Receptor-Positive Breast
            Carcinomas: Correlation With Neuroendocrine Differentiation
  JOURNAL   Mod Pathol 37 (8), 100541 (2024)
   PUBMED   38897452
  REMARK    GeneRIF: RB1 Genetic Alterations in Estrogen Receptor-Positive
            Breast Carcinomas: Correlation With Neuroendocrine Differentiation.
REFERENCE   5  (residues 1 to 923)
  AUTHORS   Konagaya,Y., Rosenthal,D., Ratnayeke,N., Fan,Y. and Meyer,T.
  TITLE     An intermediate Rb-E2F activity state safeguards proliferation
            commitment
  JOURNAL   Nature 631 (8020), 424-431 (2024)
   PUBMED   38926571
  REMARK    GeneRIF: An intermediate Rb-E2F activity state safeguards
            proliferation commitment.
REFERENCE   6  (residues 1 to 923)
  AUTHORS   Lohmann,D.R. and Gallie,B.L.
  TITLE     Retinoblastoma
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301625
REFERENCE   7  (residues 1 to 923)
  AUTHORS   Dyson,N., Guida,P., Munger,K. and Harlow,E.
  TITLE     Homologous sequences in adenovirus E1A and human papillomavirus E7
            proteins mediate interaction with the same set of cellular proteins
  JOURNAL   J Virol 66 (12), 6893-6902 (1992)
   PUBMED   1331501
REFERENCE   8  (residues 1 to 923)
  AUTHORS   Huang,S., Shin,E., Sheppard,K.A., Chokroverty,L., Shan,B.,
            Qian,Y.W., Lee,E.Y. and Yee,A.S.
  TITLE     The retinoblastoma protein region required for interaction with the
            E2F transcription factor includes the T/E1A binding and
            carboxy-terminal sequences
  JOURNAL   DNA Cell Biol 11 (7), 539-548 (1992)
   PUBMED   1388726
REFERENCE   9  (residues 1 to 923)
  AUTHORS   Onadim,Z., Hogg,A., Baird,P.N. and Cowell,J.K.
  TITLE     Oncogenic point mutations in exon 20 of the RB1 gene in families
            showing incomplete penetrance and mild expression of the
            retinoblastoma phenotype
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 6177-6181 (1992)
   PUBMED   1352883
REFERENCE   10 (residues 1 to 923)
  AUTHORS   Hogg,A., Onadim,Z., Baird,P.N. and Cowell,J.K.
  TITLE     Detection of heterozygous mutations in the RB1 gene in
            retinoblastoma patients using single-strand conformation
            polymorphism analysis and polymerase chain reaction sequencing
  JOURNAL   Oncogene 7 (7), 1445-1451 (1992)
   PUBMED   1352398
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL392048.9 and AL136960.4.
            
            Summary: The protein encoded by this gene is a negative regulator
            of the cell cycle and was the first tumor suppressor gene found.
            The encoded protein also stabilizes constitutive heterochromatin to
            maintain the overall chromatin structure. The active,
            hypophosphorylated form of the protein binds transcription factor
            E2F1. Defects in this gene are a cause of childhood cancer
            retinoblastoma (RB), bladder cancer, and osteogenic sarcoma.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.762946.1,
                                           SRR14038196.1098966.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..923
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.2"
     Protein         1..923
                     /product="retinoblastoma-associated protein isoform 2"
                     /note="retinoblastoma-associated protein;
                     prepro-retinoblastoma-associated protein; protein
                     phosphatase 1, regulatory subunit 130; retinoblastoma
                     suspectibility protein; retinoblastoma 1"
                     /calculated_mol_wt=105323
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            2
                     /site_type="methylation"
                     /note="N,N-dimethylproline.
                     /evidence=ECO:0000250|UniProtKB:P13405; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Region          114..227
                     /region_name="DUF3452"
                     /note="Domain of unknown function (DUF3452); pfam11934"
                     /db_xref="CDD:463402"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:1756735,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:1756735,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Region          373..771
                     /region_name="Pocket, binds T and E1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Region          373..579
                     /region_name="Domain A"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Region          373..573
                     /region_name="RB_A"
                     /note="Retinoblastoma-associated protein A domain;
                     pfam01858"
                     /db_xref="CDD:460364"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:1756735,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK2.
                     /evidence=ECO:0000269|PubMed:10499802; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Region          580..639
                     /region_name="Spacer"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13405; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Region          610..632
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CHEK2 and CHEK1.
                     /evidence=ECO:0000269|PubMed:17380128,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Region          640..771
                     /region_name="Domain B"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Region          645..771
                     /region_name="CYCLIN_RB"
                     /note="cyclin box found in retinoblastoma-associated
                     protein (RB) and similar proteins; cd20599"
                     /db_xref="CDD:410302"
     Site            order(645,649,652..653,656,660)
                     /site_type="other"
                     /note="E2F transcription factor binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410302"
     Site            order(709,713..714,720..721,753,756..757,761)
                     /site_type="other"
                     /note="LxCxE peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410302"
     Region          768..904
                     /region_name="Rb_C"
                     /note="Rb C-terminal domain; pfam08934"
                     /db_xref="CDD:462639"
     Site            780
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            788
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            795
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            807
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1 and CDK3.
                     /evidence=ECO:0000269|PubMed:15084261,
                     ECO:0000269|PubMed:1756735, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            810
                     /site_type="methylation"
                     /note="N6-methyllysine, by SMYD2.
                     /evidence=ECO:0000269|PubMed:22787429; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            811
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1 and CDK3.
                     /evidence=ECO:0000269|PubMed:15084261,
                     ECO:0000269|PubMed:1756735, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK6.
                     /evidence=ECO:0000269|PubMed:15809340,
                     ECO:0000269|PubMed:16360038, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            823
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            826
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK4.
                     /evidence=ECO:0000269|PubMed:15809340,
                     ECO:0000269|PubMed:16360038, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            841
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            855
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Region          860..876
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:P13405"
                     /note="propagated from UniProtKB/Swiss-Prot (P06400.2)"
     Site            860
                     /site_type="methylation"
                     /note="N6-methyllysine, by SMYD2.
                     /evidence=ECO:0000269|PubMed:20870719; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            873
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by PCAF.
                     /evidence=ECO:0000269|PubMed:20940255; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     Site            874
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by PCAF.
                     /evidence=ECO:0000269|PubMed:20940255; propagated from
                     UniProtKB/Swiss-Prot (P06400.2)"
     CDS             1..923
                     /gene="RB1"
                     /gene_synonym="OSRC; p105-Rb; p110-RB1; pp110; PPP1R130;
                     pRb; RB"
                     /coded_by="NM_001407165.1:163..2934"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:5925"
                     /db_xref="HGNC:HGNC:9884"
                     /db_xref="MIM:614041"
ORIGIN      
        1 mppktprkta ataaaaaaep papppppppe edpeqdsgpe dlplvrlefe eteepdftal
       61 cqklkipdhv rerawltwek vssvdgvlgg yiqkkkelwg icifiaavdl demsftftel
      121 qknieisvhk ffnllkeidt stkvdnamsr llkkydvlfa lfsklertce liyltqpsss
      181 isteinsalv lkvswitfll akgevlqmed dlvisfqlml cvldyfikls ppmllkepyk
      241 tavipingsp rtprrgqnrs ariakqlend triievlcke hecnidevkn vyfknfipfm
      301 nslglvtsng lpevenlskr yeeiylknkd ldarlfldhd ktlqtdsids fetqrtprks
      361 nldeevnvip phtpvrtvmn tiqqlmmiln sasdqpsenl isyfnnctvn pkesilkrvk
      421 digyifkekf akavgqgcve igsqryklgv rlyyrvmesm lkseeerlsi qnfskllndn
      481 ifhmsllaca levvmatysr stsqnldsgt dlsfpwilnv lnlkafdfyk viesfikaeg
      541 nltremikhl ercehrimes lawlsdsplf dlikqskdre gptdhlesac plnlplqnnh
      601 taadmylspv rspkkkgstt rvnstanaet qatsafqtqk plkstslslf ykkvyrlayl
      661 rlntlcerll sehpelehii wtlfqhtlqn eyelmrdrhl dqimmcsmyg ickvknidlk
      721 fkiivtaykd lphavqetfk rvlikeeeyd siivfynsvf mqrlktnilq yastrpptls
      781 piphiprspy kfpssplrip ggniyisplk spykiseglp tptkmtprsr ilvsigesfg
      841 tsekfqkinq mvcnsdrvlk rsaegsnppk plkklrfdie gsdeadgskh lpgeskfqqk
      901 laemilhpfs sfysntnaka ene
//
LOCUS       NP_001393529            1163 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 3 [Homo sapiens].
ACCESSION   NP_001393529 XP_047279788
VERSION     NP_001393529.1
DBSOURCE    REFSEQ: accession NM_001406600.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1163)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1163)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1163)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1163)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1163)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1163)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1163)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1163)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1163)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1163)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            On May 18, 2022 this sequence version replaced XP_047279788.1.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3283444.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1163
                     /product="hamartin isoform 3"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=129565
     Region          7..718
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          402..786
                     /region_name="Mediates interaction with WDR45B.
                     /evidence=ECO:0000269|PubMed:28561066"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Region          438..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <707..>959
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1005..1084
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1099
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1130..1163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1163
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406600.1:408..3899"
                     /note="isoform 3 is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS87703.1"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt ggkgtplgtp atspppaplc hsddyvhisl pqatvtpprk
      421 eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed siekdkeeaa
      481 isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv npeplhssld
      541 klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp trvgfgsgqp
      601 ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr liqqgadahs
      661 kelnklplps ksvdwthfgg sppsdeirtl rdqllllhnq llyerfkrqq halrnrrllr
      721 kvikaaalee hnaamkdqlk lqekdiqmwk vslqkeqary nqlqeqrdtm vtklhsqirq
      781 lqhdreefyn qsqelqtkle dcrnmiaelr ielkkannkv chtelllsqv sqklsnsesv
      841 qqqmeflnrq llvlgevnel yleqlqnkhs dttkevemmk aayrkelekn rshvlqqtqr
      901 ldtsqkrile leshlakkdh llleqkkyle dvklqargql qaaesryeaq kritqvfele
      961 ildlygrlek dgllkkleee kaeaaeaaee rldccndgcs dsmvghneea sghngetktp
     1021 rpssargssg srggggssss sselstpekp phqragpfss rwettmgeas asipttvgsl
     1081 pssksflgmk arelfrnkse sqcdedgmts slseslktel gkdlgveaki plnldgphps
     1141 pptpdsvgql himdynethh ehs
//
LOCUS       NP_001411268             229 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 5 isoform 7
            precursor [Homo sapiens].
ACCESSION   NP_001411268 XP_005260676 XP_054180219
VERSION     NP_001411268.1
DBSOURCE    REFSEQ: accession NM_001424339.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Ahmed,H.A., Abdelkreem,E., Hamed,E.O., Abo Elmahassen,N.M. and
            Younis,M.A.A.
  TITLE     Frequency of CD40-1C>T polymorphism (rs1883832) and association
            with response to treatment in children with primary immune
            thrombocytopenia
  JOURNAL   Pediatr Blood Cancer 71 (12), e31356 (2024)
   PUBMED   39350313
  REMARK    GeneRIF: Frequency of CD40-1C>T polymorphism (rs1883832) and
            association with response to treatment in children with primary
            immune thrombocytopenia.
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Meng,H., Li,L., Nan,M., Ding,Y., Li,Y. and Zhang,M.
  TITLE     ZG16 enhances the maturation of dendritic cells via induction of
            CD40 and contributes to the antitumor immunity in pancreatic cancer
  JOURNAL   Oncogene 43 (43), 3184-3196 (2024)
   PUBMED   39261658
  REMARK    GeneRIF: ZG16 enhances the maturation of dendritic cells via
            induction of CD40 and contributes to the antitumor immunity in
            pancreatic cancer.
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Aydin,S., Darko,K., Detchou,D. and Barrie,U.
  TITLE     A call for clinical trials in glioblastoma multiforme for
            interleukin 4, interleukin 6, interleukin 13 and CD40
  JOURNAL   Neurosurg Rev 47 (1), 571 (2024)
   PUBMED   39242402
  REMARK    GeneRIF: A call for clinical trials in glioblastoma multiforme for
            interleukin 4, interleukin 6, interleukin 13 and CD40.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Naseri,S., Cordova,M.M., Wenthe,J., Lovgren,T., Eriksson,E.,
            Loskog,A. and Ullenhag,G.J.
  TITLE     CD40 stimulation via CD40 ligand enhances adenovirus-mediated
            tumour immunogenicity including 'find-me', 'eat-me', and 'kill-me'
            signalling
  JOURNAL   J Cell Mol Med 28 (7), e18162 (2024)
   PUBMED   38494863
REFERENCE   6  (residues 1 to 229)
  AUTHORS   Foy,T.M., Laman,J.D., Ledbetter,J.A., Aruffo,A., Claassen,E. and
            Noelle,R.J.
  TITLE     gp39-CD40 interactions are essential for germinal center formation
            and the development of B cell memory
  JOURNAL   J Exp Med 180 (1), 157-163 (1994)
   PUBMED   7516405
REFERENCE   7  (residues 1 to 229)
  AUTHORS   Banchereau,J., Bazan,F., Blanchard,D., Briere,F., Galizzi,J.P., van
            Kooten,C., Liu,Y.J., Rousset,F. and Saeland,S.
  TITLE     The CD40 antigen and its ligand
  JOURNAL   Annu Rev Immunol 12, 881-922 (1994)
   PUBMED   7516669
  REMARK    Review article
REFERENCE   8  (residues 1 to 229)
  AUTHORS   Stamenkovic,I., Clark,E.A. and Seed,B.
  TITLE     A B-lymphocyte activation molecule related to the nerve growth
            factor receptor and induced by cytokines in carcinomas
  JOURNAL   EMBO J 8 (5), 1403-1410 (1989)
   PUBMED   2475341
REFERENCE   9  (residues 1 to 229)
  AUTHORS   Clark,E.A. and Ledbetter,J.A.
  TITLE     Activation of human B cells mediated through two distinct cell
            surface differentiation antigens, Bp35 and Bp50
  JOURNAL   Proc Natl Acad Sci U S A 83 (12), 4494-4498 (1986)
   PUBMED   3487090
REFERENCE   10 (residues 1 to 229)
  AUTHORS   Paulie,S., Ehlin-Henriksson,B., Mellstedt,H., Koho,H., Ben-Aissa,H.
            and Perlmann,P.
  TITLE     A p50 surface antigen restricted to human urinary bladder
            carcinomas and B lymphocytes
  JOURNAL   Cancer Immunol Immunother 20 (1), 23-28 (1985)
   PUBMED   2998589
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL035662.65.
            
            On or before Sep 22, 2023 this sequence version replaced
            XP_005260676.1, XP_054180219.1.
            
            Summary: This gene is a member of the TNF-receptor superfamily. The
            encoded protein is a receptor on antigen-presenting cells of the
            immune system and is essential for mediating a broad variety of
            immune and inflammatory responses including T cell-dependent
            immunoglobulin class switching, memory B cell development, and
            germinal center formation. AT-hook transcription factor AKNA is
            reported to coordinately regulate the expression of this receptor
            and its ligand, which may be important for homotypic cell
            interactions. Adaptor protein TNFR2 interacts with this receptor
            and serves as a mediator of the signal transduction. The
            interaction of this receptor and its ligand is found to be
            necessary for amyloid-beta-induced microglial activation, and thus
            is thought to be an early event in Alzheimer disease pathogenesis.
            Mutations affecting this gene are the cause of autosomal recessive
            hyper-IgM immunodeficiency type 3 (HIGM3). Multiple alternatively
            spliced transcript variants of this gene encoding distinct isoforms
            have been reported. [provided by RefSeq, Nov 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.3706306.1,
                                           DRR138524.502031.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..229
                     /product="tumor necrosis factor receptor superfamily
                     member 5 isoform 7 precursor"
                     /note="CD40L receptor; B cell-associated molecule; B cell
                     surface antigen CD40; tumor necrosis factor receptor
                     superfamily member 5; CD40 molecule, TNF receptor
                     superfamily member 5"
                     /calculated_mol_wt=23258
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2250
     Region          26..>135
                     /region_name="TNFRSF"
                     /note="Tumor necrosis factor receptor superfamily
                     (TNFRSF); cl22855"
                     /db_xref="CDD:473981"
     Region          62..103
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276912"
     CDS             1..229
                     /gene="CD40"
                     /gene_synonym="Bp50; CDW40; p50; TNFRSF5"
                     /coded_by="NM_001424339.1:31..720"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 9"
                     /db_xref="GeneID:958"
                     /db_xref="HGNC:HGNC:11919"
                     /db_xref="MIM:109535"
ORIGIN      
        1 mvrlplqcvl wgclltavhp epptacrekq ylinsqccsl cqpgqklvsd cteftetecl
       61 pcgesefldt wnrethchqh kycdpnlglr vqqkgtsetd tictceegwh ctseacescv
      121 lhrscspgfg vkqigpqdrl ralvvipiif gilfaillvl vfisessekv akkptnkaph
      181 pkqepqeinf pddlpgsnta apvqetlhgc qpvtqedgke srisvqerq
//
LOCUS       NP_001394765            1096 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 21 [Homo
            sapiens].
ACCESSION   NP_001394765
VERSION     NP_001394765.1
DBSOURCE    REFSEQ: accession NM_001407836.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1096)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1096)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1096)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1096)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1096)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1096)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1096)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1096)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1096)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1096)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3496888.1,
                                           SRR14038191.4255764.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1096
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1096
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 21"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=123880
     Region          153..182
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          188..215
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          324..596
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          723..1096
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1096
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407836.1:575..3865"
                     /note="isoform 21 is encoded by transcript variant 21"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 mgakdatpvp cgrwakilek dkrtqqmrmq rlkaklqmpf qsgefkaltr rlqveprlls
       61 kqmagcledc trqapespwe eqlarllqea pgklsldveq apsgqhsqaq lsgqqqrlla
      121 ffkcclltdq lplahhllvv hhgqrqkrkl ltldmynavm lgwarqgafk elvyvlfmvk
      181 dagltpdlls yaaalqcmgr qdqdagtier cleqmsqegl klqalftavl lseedratvl
      241 kavhkvkptf slppqlpppv ntskllrdvy akdgrvsypk lhlplktlqc lfekqlhmel
      301 asrvcvvsve kptlpskevk harktlktlr dqwekalcra lretknrler evyegrfsly
      361 pflclldere vvrmllqvlq alpaqgesft tlarelsart fsrhvvqrqr vsgqvqalqn
      421 hyrkylclla sdaevpepcl prqyweelga pealreqpwp lpvqmelgkl laemlvqatq
      481 mpcsldkphr ssrlvpvlyh vysfrnvqqi gilkphpayv qllekaaept ltfeavdvpm
      541 lcpplpwtsp hsgafllspt klmrtvegat qhqelletcp ptalhgalda ltqlgncawr
      601 vngrvldlvl qlfqakgcpq lgvpappsea pqppeahlph saaparkael rrelahcqkv
      661 aremhslrae alyrlslaqh lrdrvfwlph nmdfrgrtyp cpphfnhlgs dvarallefa
      721 qgrplgphgl dwlkihlvnl tglkkreplr krlafaeevm ddildsadqp ltgrkwwmga
      781 eepwqtlacc mevanavras dpaayvshlp vhqdgscngl qhyaalgrds vgaasvnlep
      841 sdvpqdvysg vaaqvvkqtv mtvvygvtry ggrlqiekrl relsdfpqef vweashylvr
      901 qvfkslqemf sgtraiqhwl tesarlishm gsvvewvtpl gvpviqpyrl dskvkqiggg
      961 iqsitythng disrkpntrk qkngfppnfi hsldsshmml talhcyrkgl tfvsvhdcyw
     1021 thaadvsvmn qvcreqfvrl hsepilqdls rflvkrfcse pqkileasql ketlqavpkp
     1081 gafdleqvkr styffs
//
LOCUS       NP_001424440            1659 aa            linear   PRI 21-NOV-2025
DEFINITION  BCL-6 corepressor isoform d [Homo sapiens].
ACCESSION   NP_001424440 XP_016885105 XP_054183310
VERSION     NP_001424440.1
DBSOURCE    REFSEQ: accession NM_001437511.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1659)
  AUTHORS   Batkova,M., Havlovicova,M., Nocar,A., Dudakova,L., Macek,M.,
            Liskova,P. and Dostalova,T.
  TITLE     Dental abnormalities observed in the oculo-facio-cardio-dental
            (OFCD) syndrome present in two Czech families bearing novel de novo
            BCOR pathogenic variants
  JOURNAL   BMC Oral Health 24 (1), 1264 (2024)
   PUBMED   39438869
  REMARK    GeneRIF: Dental abnormalities observed in the
            oculo-facio-cardio-dental (OFCD) syndrome present in two Czech
            families bearing novel de novo BCOR pathogenic variants.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1659)
  AUTHORS   Giner,F., Medina-Ceballos,E., Lopez-Reig,R., Machado,I.,
            Lopez-Guerrero,J.A., Navarro,S., Rubio-Martinez,L.A., Espino,M.,
            Mayordomo-Aranda,E. and Llombart-Bosch,A.
  TITLE     The Combined Immunohistochemical Expression of GLI1 and BCOR in
            Synovial Sarcomas for the Identification of Three Risk Groups and
            Their Prognostic Outcomes: A Study of 52 Patients
  JOURNAL   Int J Mol Sci 25 (14), 7615 (2024)
   PUBMED   39062853
  REMARK    GeneRIF: The Combined Immunohistochemical Expression of GLI1 and
            BCOR in Synovial Sarcomas for the Identification of Three Risk
            Groups and Their Prognostic Outcomes: A Study of 52 Patients.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1659)
  AUTHORS   Mavridou,E., Lema Fernandez,A.G., Nardelli,C., Pierini,V.,
            Quintini,M., Arniani,S., Di Giacomo,D., Crescenzi,B., Matteucci,C.,
            Sambani,C. and Mecucci,C.
  TITLE     A novel t(X;21)(p11.4;q22.12) translocation adds to the role of
            BCOR and RUNX1 in myelodysplastic syndromes and acute myeloid
            leukemias
  JOURNAL   Genes Chromosomes Cancer 63 (4), e23235 (2024)
   PUBMED   38656651
  REMARK    GeneRIF: A novel t(X;21)(p11.4;q22.12) translocation adds to the
            role of BCOR and RUNX1 in myelodysplastic syndromes and acute
            myeloid leukemias.
REFERENCE   4  (residues 1 to 1659)
  AUTHORS   Pierron,G., Tirode,F., Lucchesi,C., Reynaud,S., Ballet,S.,
            Cohen-Gogo,S., Perrin,V., Coindre,J.M. and Delattre,O.
  TITLE     A new subtype of bone sarcoma defined by BCOR-CCNB3 gene fusion
  JOURNAL   Nat Genet 44 (4), 461-466 (2012)
   PUBMED   22387997
  REMARK    GeneRIF: A new fusion was observed between BCOR (encoding the BCL6
            co-repressor) and CCNB3 (encoding the testis-specific cyclin B3) on
            the X chromosome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1659)
  AUTHORS   Tomsig,J.L., Snyder,S.L. and Creutz,C.E.
  TITLE     Identification of targets for calcium signaling through the copine
            family of proteins. Characterization of a coiled-coil
            copine-binding motif
  JOURNAL   J Biol Chem 278 (12), 10048-10054 (2003)
   PUBMED   12522145
REFERENCE   6  (residues 1 to 1659)
  AUTHORS   Ng,D., Hadley,D.W., Tifft,C.J. and Biesecker,L.G.
  TITLE     Genetic heterogeneity of syndromic X-linked recessive
            microphthalmia-anophthalmia: is Lenz microphthalmia a single
            disorder?
  JOURNAL   Am J Med Genet 110 (4), 308-314 (2002)
   PUBMED   12116202
REFERENCE   7  (residues 1 to 1659)
  AUTHORS   Tang,T.T., Dowbenko,D., Jackson,A., Toney,L., Lewin,D.A., Dent,A.L.
            and Lasky,L.A.
  TITLE     The forkhead transcription factor AFX activates apoptosis by
            induction of the BCL-6 transcriptional repressor
  JOURNAL   J Biol Chem 277 (16), 14255-14265 (2002)
   PUBMED   11777915
  REMARK    GeneRIF: The forkhead transcription factor AFX activates apoptosis
            by induction of the BCL-6 transcriptional repressor.
REFERENCE   8  (residues 1 to 1659)
  AUTHORS   Huynh,K.D., Fischle,W., Verdin,E. and Bardwell,V.J.
  TITLE     BCoR, a novel corepressor involved in BCL-6 repression
  JOURNAL   Genes Dev 14 (14), 1810-1823 (2000)
   PUBMED   10898795
  REMARK    GeneRIF: Function:BCoR is a transcriptional corepressor for BCL-6.
            Nomenclature:BCoR (BCL-6 corepressor)
REFERENCE   9  (residues 1 to 1659)
  AUTHORS   Ng,D.
  TITLE     Lenz Microphthalmia Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301694
REFERENCE   10 (residues 1 to 1659)
  AUTHORS   Bardakjian,T., Weiss,A. and Schneider,A.
  TITLE     Microphthalmia/Anophthalmia/Coloboma Spectrum - RETIRED CHAPTER,
            FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301552
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL591802.28 and AC092198.5.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_016885105.1, XP_054183310.1.
            
            Summary: The protein encoded by this gene was identified as an
            interacting corepressor of BCL6, a POZ/zinc finger transcription
            repressor that is required for germinal center formation and may
            influence apoptosis. This protein selectively interacts with the
            POZ domain of BCL6, but not with eight other POZ proteins. Specific
            class I and II histone deacetylases (HDACs) have been shown to
            interact with this protein, which suggests a possible link between
            the two classes of HDACs. Several transcript variants encoding
            different isoforms have been found for this gene. A pseudogene of
            this gene is found on chromosome Y.[provided by RefSeq, Jun 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1305272.1,
                                           SRR14372079.3565227.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1659
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.4"
     Protein         1..1659
                     /product="BCL-6 corepressor isoform d"
                     /note="BCL-6 interacting corepressor; BCL6 interacting
                     corepressor; BCL-6 coreceptor"
                     /calculated_mol_wt=180978
     Region          <257..673
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          309..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          388..438
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            392
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          498..514
                     /region_name="Interaction with BCL6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          557..641
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          737..760
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          773..794
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          815..844
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1071..1187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGN4; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1202..1414
                     /region_name="BCOR"
                     /note="BCL-6 co-repressor, non-ankyrin-repeat region;
                     pfam15808"
                     /db_xref="CDD:434953"
     Region          1220..1328
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGN4; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1430..1451
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          <1461..1593
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1462..1495
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1463..1494
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1464,1468..1469,1472..1474,1476..1477,1481,1484,
                     1494,1496,1498,1502..1503,1506..1508,1510..1511,1515,1518,
                     1527,1529,1531,1535..1536,1539..1541,1543..1544,1548,1551)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1496..1527
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1496..1525
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1529..1558
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1529..1558
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1634..>1659
                     /region_name="PUFD_like"
                     /note="PCGF Ub-like fold discriminator and related
                     domains; cl21640"
                     /db_xref="CDD:473927"
     CDS             1..1659
                     /gene="BCOR"
                     /gene_synonym="ANOP2; MAA2; MCOPS2"
                     /coded_by="NM_001437511.1:785..5764"
                     /note="isoform d is encoded by transcript variant 8"
                     /db_xref="GeneID:54880"
                     /db_xref="HGNC:HGNC:20893"
                     /db_xref="MIM:300485"
ORIGIN      
        1 mlsatplygn vhswmnserv rmcgasedrk ilvndgdask arlelreenp lnhnvvdast
       61 ahridglaal smdrtglire glrvpgnivy sslcglgsek greaatstlg glgfssernp
      121 emqfkpntpe tveasavsgk ppngfsaiyk tppgiqksav ataealgldr pasdkqspln
      181 ingasylrlp wvnpymegat paiypfldsp nkyslnmyka llpqqsysla qplyspvctn
      241 gerflylppp hyvgphipss laspmrlstp saspaipplv hcadkslpwk mgvspgnpvd
      301 shayphiqns kqprvpsaka vtsglpgdta lllppsprps prvhlptqpa adtysefhkh
      361 yaristspsv alskpymtvs sefpaarlsn gkypkapegg egaqpvpgha rktavqdrkd
      421 gssppllekq tvtkdvtdkp ldlsskvvdv daskadhmkk maptvlvhsr agsglvlsgs
      481 eipketlspp gngcaiyrse iistapsswv vpgpspneen ngksmslknk aldwaipqqr
      541 ssscprmggt davitnvsgs vssagrpasa spapnanadg tktsrssvet tpsviqhvgq
      601 ppatpakhss stsskgakas npepsfkane nglppssifl spneafrspp ipyprsylpy
      661 papegiavsp lslhgkgpvy phpvllpngs lfpghlapkp glpyglptgr pefvtyqdal
      721 glgmvhpmli phtpieitke ekperrsrsh eraryedptl rnrfseilet sstklhpdvp
      781 tdknlkpnpn wnqgktvvks dklvyvdllr eepdaktdtn vskpsfaaes vgqsaeppkp
      841 svepalqqhr dfialreelg risdfhetyt fkqpvftvsk dsvlagtnke nlglpvstpf
      901 lepplgsdgp avtfgktqed pkpfcvgsap psvdvtptyt kdgadeaesn dgkvlkpkps
      961 klakriansa gyvgdrfkcv ttelyadssq lsreqralqm eglqedsilc lpaayceram
     1021 mrfselemke regghpatkd semckfspad werlkgnqdk kpksvtleea iaeqneserc
     1081 eysvgnkhrd pfeapedkdl pvekyfverq pvseppadqv asdmphsptl rvdrkrkvsg
     1141 dsshtettae evpedpllka krrrvskddw peremtnsss nhledphyse ltnlkvciel
     1201 tglhpkkqrh llhlrerweq qvsaadgkpg rqsrkevtqa tqpeaipqgt niteekpgrk
     1261 raeakgnrsw seeslkpsdn eqglpvfsgs ppmkslssts aggkkqaqps capasrppak
     1321 qqkikenqkt dvlcadeeed cqaasllqky tdnsekpsgk rlcktkhlip qesrrglplt
     1381 geyyvenadg kvtvrrfrkr pepssdydls pakqepkpfd rlqqllpasq stqlpcsssp
     1441 qettqsrpmp pearrlivnk nagetllqra arlgyeevvl yclenkicdv nhrdnagyca
     1501 lheacargwl nivrhlleyg advncsaqdg trplhdaven dhleivrlll sygadptlat
     1561 ysgrtimkmt hselmekflt dylndlqgrn dddasgtwdf ygssvcepdd esgydvlanp
     1621 pgpedqdddd daysdvfefe fsetpllpcy niqvsvaqg
//
LOCUS       NP_001424531             438 aa            linear   PRI 21-NOV-2025
DEFINITION  sorting nexin-27 isoform 4 [Homo sapiens].
ACCESSION   NP_001424531 XP_005245567 XP_054194889
VERSION     NP_001424531.1
DBSOURCE    REFSEQ: accession NM_001437602.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Broniarczyk,J., Trejo-Cerro,O., Massimi,P., Kavcic,N., Myers,M.P.
            and Banks,L.
  TITLE     HPV-18 E6 enhances the interaction between EMILIN2 and SNX27 to
            promote WNT signaling
  JOURNAL   J Virol 98 (7), e0073524 (2024)
   PUBMED   38874360
  REMARK    GeneRIF: HPV-18 E6 enhances the interaction between EMILIN2 and
            SNX27 to promote WNT signaling.
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Xi,Y., Gai,Y., Zhang,W., Wang,M., Liu,Q. and Bi,Y.
  TITLE     Circular RNA SNX27 Facilitates Gastric Cancer Progression By
            Sponging miR-638
  JOURNAL   Turk J Gastroenterol 35 (4), 280-287 (2024)
   PUBMED   39128090
  REMARK    GeneRIF: Circular RNA SNX27 Facilitates Gastric Cancer Progression
            By Sponging miR-638.
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Broniarczyk,J.K., Massimi,P., Trejo-Cerro,O., Myers,M.P. and
            Banks,L.
  TITLE     HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in a
            PBM-Dependent Manner and Promotes Increased Cell Proliferation
  JOURNAL   J Virol 96 (22), e0136522 (2022)
   PUBMED   36326272
  REMARK    GeneRIF: HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in
            a PBM-Dependent Manner and Promotes Increased Cell Proliferation.
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 438)
  AUTHORS   MacNeil,A.J., Mansour,M. and Pohajdak,B.
  TITLE     Sorting nexin 27 interacts with the Cytohesin associated
            scaffolding protein (CASP) in lymphocytes
  JOURNAL   Biochem Biophys Res Commun 359 (4), 848-853 (2007)
   PUBMED   17577583
  REMARK    GeneRIF: These results suggest that endosomal SNX27 may recruit
            CASP to orchestrate intracellular trafficking and/or signaling
            complexes.
REFERENCE   7  (residues 1 to 438)
  AUTHORS   Rincon,E., Santos,T., Avila-Flores,A., Albar,J.P., Lalioti,V.,
            Lei,C., Hong,W. and Merida,I.
  TITLE     Proteomics identification of sorting nexin 27 as a diacylglycerol
            kinase zeta-associated protein: new diacylglycerol kinase roles in
            endocytic recycling
  JOURNAL   Mol Cell Proteomics 6 (6), 1073-1087 (2007)
   PUBMED   17351151
  REMARK    GeneRIF: These data support a previously unreported role for
            diacylglycerol kinase zeta in the modulation of membrane
            trafficking, which may also help to define SNX27 function.
REFERENCE   8  (residues 1 to 438)
  AUTHORS   Joubert,L., Hanson,B., Barthet,G., Sebben,M., Claeysen,S., Hong,W.,
            Marin,P., Dumuis,A. and Bockaert,J.
  TITLE     New sorting nexin (SNX27) and NHERF specifically interact with the
            5-HT4a receptor splice variant: roles in receptor targeting
  JOURNAL   J Cell Sci 117 (Pt 22), 5367-5379 (2004)
   PUBMED   15466885
  REMARK    GeneRIF: SNX27a redirects part of the 5-HT4(a)R to early endosomes.
REFERENCE   9  (residues 1 to 438)
  AUTHORS   Worby,C.A. and Dixon,J.E.
  TITLE     Sorting out the cellular functions of sorting nexins
  JOURNAL   Nat Rev Mol Cell Biol 3 (12), 919-931 (2002)
   PUBMED   12461558
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol. 2003 Feb;4(2):156.]
REFERENCE   10 (residues 1 to 438)
  AUTHORS   Teasdale,R.D., Loci,D., Houghton,F., Karlsson,L. and Gleeson,P.A.
  TITLE     A large family of endosome-localized proteins related to sorting
            nexin 1
  JOURNAL   Biochem J 358 (Pt 1), 7-16 (2001)
   PUBMED   11485546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL391335.32 and AL589765.19.
            
            On or before Apr 7, 2025 this sequence version replaced
            XP_005245567.1, XP_054194889.1.
            
            Summary: This gene encodes a member of the sorting nexin family, a
            diverse group of cytoplasmic and membrane-associated proteins
            involved in endocytosis of plasma membrane receptors and protein
            trafficking through these compartments. All members of this protein
            family contain a phosphoinositide binding domain (PX domain). A
            highly similar protein in mouse is responsible for the specific
            recruitment of an isoform of serotonin 5-hydroxytryptamine 4
            receptor into early endosomes, suggesting the analogous role for
            the human protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2006503.1,
                                           SRR14038194.970378.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..438
                     /product="sorting nexin-27 isoform 4"
                     /note="methamphetamine-responsive transcript 1; sorting
                     nexin family member 27"
                     /calculated_mol_wt=51085
     Region          <2..31
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     Region          57..162
                     /region_name="PX_SNX27"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 27; cd06886"
                     /db_xref="CDD:132796"
     Site            order(93..95,118..119,132)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132796"
     Region          170..262
                     /region_name="FERM_F1_SNX27"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F1 sub-domain, found in sorting nexin protein 27
                     (SNX27); cd01777"
                     /db_xref="CDD:340475"
     Region          322..423
                     /region_name="FERM-like_C_SNX27"
                     /note="Atypical FERM-like domain C-lobe of Sorting nexin
                     27; cd13338"
                     /db_xref="CDD:270146"
     CDS             1..438
                     /gene="SNX27"
                     /gene_synonym="MRT1; MY014"
                     /coded_by="NM_001437602.1:391..1707"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:81609"
                     /db_xref="HGNC:HGNC:20073"
                     /db_xref="MIM:611541"
ORIGIN      
        1 mnhvnvegat hkqvvdlira gekeliltvl svppheadnl dpsddslgqs fydytekqav
       61 pisvprykhv eqngekfvvy nvymagrqlc skryrefail hqnlkrefan ftfprlpgkw
      121 pfslseqqld arrrgleeyl ekvcsirvig esdimqefls esdenyngvs dvelrvalpd
      181 gttvtvrvkk nsttdqvyqa iaakvgmdst tvnyfalfev ishsfvrkla pnefphklyi
      241 qnytsavpgt cltirkwlft teeeillndn dlavtyffhq avddvkkgyi kaeeksyqlq
      301 klyeqrkmvm ylnmlrtceg yneiifphca cdsrrkghvi taisithfkl hacteegqle
      361 nqviafewde mqrwdtdeeg mafcfeyarg ekkprwvkif tpyfnymhec fervfcelkw
      421 rkenifqmar sqqrdvat
//
LOCUS       NP_001427925             769 aa            linear   PRI 21-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 6 isoform 6 [Homo sapiens].
ACCESSION   NP_001427925 XP_047298628 XP_054184146
VERSION     NP_001427925.1
DBSOURCE    REFSEQ: accession NM_001440996.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Zheng,T., Zhou,H., Zheng,Z., Guo,Y., Liu,J., Zhang,J. and Li,S.
  TITLE     The pathological significance and potential mechanism of ARHGEF6 in
            lung adenocarcinoma
  JOURNAL   Comput Biol Med 158, 106894 (2023)
   PUBMED   37058762
  REMARK    GeneRIF: The pathological significance and potential mechanism of
            ARHGEF6 in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 769)
  AUTHORS   Li,K., Wang,H., Yang,C., Li,C., Xue,B. and Zhou,J.
  TITLE     Clinical implication and potential function of ARHGEF6 in acute
            myeloid leukemia: An in vitro study
  JOURNAL   PLoS One 18 (4), e0283934 (2023)
   PUBMED   37027440
  REMARK    GeneRIF: Clinical implication and potential function of ARHGEF6 in
            acute myeloid leukemia: An in vitro study.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 769)
  AUTHORS   Klambt,V., Buerger,F., Wang,C., Naert,T., Richter,K., Nauth,T.,
            Weiss,A.C., Sieckmann,T., Lai,E., Connaughton,D.M., Seltzsam,S.,
            Mann,N., Majmundar,A.J., Wu,C.W., Onuchic-Whitford,A.C., Shril,S.,
            Schneider,S., Schierbaum,L., Dai,R., Bekheirnia,M.R., Joosten,M.,
            Shlomovitz,O., Vivante,A., Banne,E., Mane,S., Lifton,R.P.,
            Kirschner,K.M., Kispert,A., Rosenberger,G., Fischer,K.D.,
            Lienkamp,S.S., Zegers,M.M.P. and Hildebrandt,F.
  TITLE     Genetic Variants in ARHGEF6 Cause Congenital Anomalies of the
            Kidneys and Urinary Tract in Humans, Mice, and Frogs
  JOURNAL   J Am Soc Nephrol 34 (2), 273-290 (2023)
   PUBMED   36414417
  REMARK    GeneRIF: Genetic Variants in ARHGEF6 Cause Congenital Anomalies of
            the Kidneys and Urinary Tract in Humans, Mice, and Frogs.
REFERENCE   5  (residues 1 to 769)
  AUTHORS   Wang,N., Li,Y., Zhou,X., Wang,X. and Yang,G.
  TITLE     Comprehensive analysis identifies ARHGEF6 as a potential prognostic
            and immunological biomarker in lung adenocarcinoma
  JOURNAL   Comput Biol Med 153, 106448 (2023)
   PUBMED   36586227
  REMARK    GeneRIF: Comprehensive analysis identifies ARHGEF6 as a potential
            prognostic and immunological biomarker in lung adenocarcinoma.
REFERENCE   6  (residues 1 to 769)
  AUTHORS   Yoshii,S., Tanaka,M., Otsuki,Y., Wang,D.Y., Guo,R.J., Zhu,Y.,
            Takeda,R., Hanai,H., Kaneko,E. and Sugimura,H.
  TITLE     alphaPIX nucleotide exchange factor is activated by interaction
            with phosphatidylinositol 3-kinase
  JOURNAL   Oncogene 18 (41), 5680-5690 (1999)
   PUBMED   10523848
REFERENCE   7  (residues 1 to 769)
  AUTHORS   Yntema,H.G., Hamel,B.C., Smits,A.P., van Roosmalen,T., van den
            Helm,B., Kremer,H., Ropers,H.H., Smeets,D.F. and van Bokhoven,H.
  TITLE     Localisation of a gene for non-specific X linked mental retardation
            (MRX46) to Xq25-q26
  JOURNAL   J Med Genet 35 (10), 801-805 (1998)
   PUBMED   9783701
REFERENCE   8  (residues 1 to 769)
  AUTHORS   Ebinu,J.O., Bottorff,D.A., Chan,E.Y., Stang,S.L., Dunn,R.J. and
            Stone,J.C.
  TITLE     RasGRP, a Ras guanyl nucleotide- releasing protein with calcium-
            and diacylglycerol-binding motifs
  JOURNAL   Science 280 (5366), 1082-1086 (1998)
   PUBMED   9582122
REFERENCE   9  (residues 1 to 769)
  AUTHORS   Manser,E., Loo,T.H., Koh,C.G., Zhao,Z.S., Chen,X.Q., Tan,L.,
            Tan,I., Leung,T. and Lim,L.
  TITLE     PAK kinases are directly coupled to the PIX family of nucleotide
            exchange factors
  JOURNAL   Mol Cell 1 (2), 183-192 (1998)
   PUBMED   9659915
REFERENCE   10 (residues 1 to 769)
  AUTHORS   Nomura,N., Nagase,T., Miyajima,N., Sazuka,T., Tanaka,A., Sato,S.,
            Seki,N., Kawarabayasi,Y., Ishikawa,K. and Tabata,S.
  TITLE     Prediction of the coding sequences of unidentified human genes. II.
            The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
            analysis of cDNA clones from human cell line KG-1 (supplement)
  JOURNAL   DNA Res 1 (5), 251-262 (1994)
   PUBMED   7584048
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL683813.10 and AL135783.6.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047298628.1, XP_054184146.1.
            
            Summary: Rho GTPases play a fundamental role in numerous cellular
            processes that are initiated by extracellular stimuli that work
            through G protein coupled receptors. The encoded protein belongs to
            a family of cytoplasmic proteins that activate the Ras-like family
            of Rho proteins by exchanging bound GDP for GTP. It may form a
            complex with G proteins and stimulate Rho-dependent signals. This
            protein is activated by PI3-kinase. Mutations in this gene can
            cause X-chromosomal non-specific cognitive disability. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.4126396.1,
                                           SRR14038193.3122973.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.3"
     Protein         1..769
                     /product="rho guanine nucleotide exchange factor 6 isoform
                     6"
                     /note="Rac/Cdc42 guanine exchange factor (GEF) 6; rho
                     guanine nucleotide exchange factor 6; PAK-interacting
                     exchange factor, alpha; Rac/Cdc42 guanine nucleotide
                     exchange factor (GEF) 6"
                     /calculated_mol_wt=86476
     Region          1..117
                     /region_name="CH_alphaPIX"
                     /note="calponin homology (CH) domain found in alpha-Pak
                     Interactive eXchange factor; cd21265"
                     /db_xref="CDD:409114"
     Site            order(3,7,65,67..68,71..72,74,81..89,95,97..98,100..101,
                     104..105,108)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409114"
     Region          115..160
                     /region_name="RhoGEF67_u1"
                     /note="Unstructured region one on RhoGEF 6 and 7;
                     pfam16615"
                     /db_xref="CDD:465201"
     Region          115..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15052.2)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15052.2)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15052.2)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15052.2)"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15052.2)"
     Region          162..219
                     /region_name="SH3_alphaPIX"
                     /note="Src Homology 3 domain of alpha-Pak Interactive
                     eXchange factor; cd12060"
                     /db_xref="CDD:212993"
     Site            order(169,171,174,177..178,193,195..197,208,210,212..213)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212993"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15052.2)"
     Region          242..419
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(248,252,346,370..371,374..375,377..378,381..382,
                     385..386,389,415,419)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          450..547
                     /region_name="PH_Cool_Pix"
                     /note="Cloned out of library/PAK-interactive exchange
                     factor pleckstrin homology (PH) domain; cd01225"
                     /db_xref="CDD:269932"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K4I3; propagated from
                     UniProtKB/Swiss-Prot (Q15052.2)"
     Region          561..581
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15052.2)"
     Region          576..667
                     /region_name="RhoGEF67_u2"
                     /note="Unstructured region two on RhoGEF 6 and 7;
                     pfam16614"
                     /db_xref="CDD:465200"
     Site            633
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15052.2)"
     Site            677
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15052.2)"
     Region          678..762
                     /region_name="betaPIX_CC"
                     /note="betaPIX coiled coil; pfam16523"
                     /db_xref="CDD:465158"
     CDS             1..769
                     /gene="ARHGEF6"
                     /gene_synonym="alpha-PIX; alphaPIX; Cool-2; COOL2; MRX46;
                     PIXA"
                     /coded_by="NM_001440996.1:51..2360"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:9459"
                     /db_xref="HGNC:HGNC:685"
                     /db_xref="MIM:300267"
ORIGIN      
        1 mnpeeqivtw lislgvlesp kkticdpeef lksslkngvv lcklinrlmp gsvekfcldp
       61 qteadcinni ndflkgcatl qveifdpddl ysgvnfskvl stllavnkat edqlserpcg
      121 rssslsaant sqtnpqgavs stvsglqrqs ktvemtengs hqlivkarfn fkqtnedels
      181 vckgdiiyvt rveeggwweg tlngrtgwfp snyvreikss erplspkavk gfetapltkn
      241 yytvvlqnil dtekeyakel qsllvtylrp lqsnnnlstv evtsllgnfe evctfqqtlc
      301 qaleecskfp enqhkvggcl lslmphfksm ylaycanhps avnvltqhsd eleqfmenqg
      361 asspgililt tnlskpfmrl ekyvtllqel erhmedthpd hqdilkaiva fktlmgqcqd
      421 lrkrkqlelq ilsepiqawe gediknlgnv ifmsqvmvqy gaceekeery lmlfsnvlim
      481 lsasprmsgf iyqgkipiag tvvtrldeie gndctfeitg ntverivvhc nnnqdfqewl
      541 eqlnrlirgp ascsslskts ssscsahssf sstgqprgpl eppqiikpws lsclrpappl
      601 rpsaalgyke esskspktmk kflhkrkter kpseeeyvir kstaaleeda qilkvieayc
      661 tsanfqqghg sstrkdsipq vllpeeekli ieetrsngqt imeekslvdt vyalkdevre
      721 lkqenkrmkq cleeelksrr dleklvrrll kqtdecirge sssktsilp
//
LOCUS       NP_001427584             757 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 3 isoform 4 [Homo sapiens].
ACCESSION   NP_001427584 XP_047294825 XP_054177063 XP_054185665
VERSION     NP_001427584.1
DBSOURCE    REFSEQ: accession NM_001440655.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 757)
  AUTHORS   Ghashghaei,M., Liu,Y., Ettles,J., Bombaci,G., Ramkumar,N., Liu,Z.,
            Escano,L., Miko,S.S., Kim,Y., Waldron,J.A., Do,K., MacPherson,K.,
            Yuen,K.A., Taibi,T., Yue,M., Arsalan,A., Jin,Z., Edin,G.,
            Karsan,A., Morin,G.B., Kuchenbauer,F., Perna,F., Bushell,M. and
            Vu,L.P.
  TITLE     Translation efficiency driven by CNOT3 subunit of the CCR4-NOT
            complex promotes leukemogenesis
  JOURNAL   Nat Commun 15 (1), 2340 (2024)
   PUBMED   38491013
  REMARK    GeneRIF: Translation efficiency driven by CNOT3 subunit of the
            CCR4-NOT complex promotes leukemogenesis.
            Erratum:[Nat Commun. 2024 Oct 7;15(1):8674. doi:
            10.1038/s41467-024-53071-1. PMID: 39375334]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 757)
  AUTHORS   Burgess,H.M., Grande,R., Riccio,S., Dinesh,I., Winkler,G.S.,
            Depledge,D.P. and Mohr,I.
  TITLE     CCR4-NOT differentially controls host versus virus poly(a)-tail
            length and regulates HCMV infection
  JOURNAL   EMBO Rep 24 (12), e56327 (2023)
   PUBMED   37846490
  REMARK    GeneRIF: CCR4-NOT differentially controls host versus virus
            poly(a)-tail length and regulates HCMV infection.
REFERENCE   4  (residues 1 to 757)
  AUTHORS   Zhao,P., Meng,Q., Wan,C., Lei,T., Zhang,L., Zhang,X., Tan,L.,
            Zhu,H. and He,X.
  TITLE     Clinical features of CNOT3-associated neurodevelopmental disorder
            in three Chinese patients
  JOURNAL   Neurogenetics 24 (2), 129-136 (2023)
   PUBMED   36802310
  REMARK    GeneRIF: Clinical features of CNOT3-associated neurodevelopmental
            disorder in three Chinese patients.
REFERENCE   5  (residues 1 to 757)
  AUTHORS   McLenachan,S., Zhang,D., Grainok,J., Zhang,X., Huang,Z., Chen,S.C.,
            Zaw,K., Lima,A., Jennings,L., Roshandel,D., Moon,S.Y., Heath
            Jeffery,R.C., Attia,M.S., Thompson,J.A., Lamey,T.M., McLaren,T.L.,
            De Roach,J., Fletcher,S. and Chen,F.K.
  TITLE     Determinants of Disease Penetrance in PRPF31-Associated Retinopathy
  JOURNAL   Genes (Basel) 12 (10), 1542 (2021)
   PUBMED   34680937
  REMARK    GeneRIF: Determinants of Disease Penetrance in PRPF31-Associated
            Retinopathy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 757)
  AUTHORS   Yin,X., Warner,D.R., Roberts,E.A., Pisano,M.M. and Greene,R.M.
  TITLE     Identification of novel CBP interacting proteins in embryonic
            orofacial tissue
  JOURNAL   Biochem Biophys Res Commun 329 (3), 1010-1017 (2005)
   PUBMED   15752756
REFERENCE   7  (residues 1 to 757)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 757)
  AUTHORS   Aoki,T., Okada,N., Wakamatsu,T. and Tamura,T.A.
  TITLE     TBP-interacting protein 120B, which is induced in relation to
            myogenesis, binds to NOT3
  JOURNAL   Biochem Biophys Res Commun 296 (5), 1097-1103 (2002)
   PUBMED   12207886
  REMARK    GeneRIF: TBP-interacting protein 120B binds to NOT3
REFERENCE   9  (residues 1 to 757)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
REFERENCE   10 (residues 1 to 757)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC245052.3.
            
            On or before May 23, 2025 this sequence version replaced
            XP_047294825.1, XP_054185665.1, XP_054177063.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2557133.1,
                                           SRR14038193.275957.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..757
                     /product="CCR4-NOT transcription complex subunit 3 isoform
                     4"
                     /note="NOT3 (negative regulator of transcription 3, yeast)
                     homolog; CCR4-associated factor 3; leukocyte receptor
                     cluster member 2"
                     /calculated_mol_wt=81396
     Region          3..230
                     /region_name="Not3"
                     /note="Not1 N-terminal domain, CCR4-Not complex component;
                     pfam04065"
                     /db_xref="CDD:461155"
     Region          241..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75175.1)"
     Region          <289..660
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Region          621..722
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..757
                     /gene="CNOT3"
                     /gene_synonym="IDDSADF; LENG2; NOT3; NOT3H"
                     /coded_by="NM_001440655.1:286..2559"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:4849"
                     /db_xref="HGNC:HGNC:7879"
                     /db_xref="MIM:604910"
ORIGIN      
        1 madkrklqge idrclkkvse gveqfediwq klhnaananq kekyeadlkk eikklqrlrd
       61 qiktwvasne ikdkrqlidn rklietqmer fkvveretkt kayskeglgl aqkvdpaqke
      121 keevgqwltn tidtlnmqvd qfesevesls vqtrkkkgdk dqkqdriegl krhiekhryh
      181 vrmletilrm ldndsilvda irkikddvey yvdssqdpdf eeneflyddl dledipqalv
      241 atsppshshm edeifnqsss tptsttsssp ippspanctt enseddkkrg rstdsevsqs
      301 pakngskpvh snqhpqspav pptypsgppp aasalsttpg nngvpapaap psalgpkasp
      361 apshnsgtpa pyaqavappa psgpsttqpr ppsvqpsggg gggsggggss sssnssaggg
      421 agkqngatsy ssvvadspae valsssggnn assqalgpps gphnpppsts kepsaaaptg
      481 aggvapgsgn nsggpsllvp lpvnppsspt psfsdakaag allngppqfs tapeikapep
      541 lsslksmaer aaissgiedp vptlhlterd iilsstsapp asaqpplqls evniplslgv
      601 cplgpvpltk eqlyqqamee aawhhmphps dserirqylp rnpcptppyh hqmppphsdt
      661 vefyqrlste tlffifyyle gtkaqylaak alkkqswrfh tkymmwfqrh eepktitdef
      721 eqlaqslslt kysslwlsaq pgtppshppl gqllgll
//
LOCUS       NP_001403224             741 aa            linear   PRI 21-NOV-2025
DEFINITION  oxysterol-binding protein-related protein 9 isoform k [Homo
            sapiens].
ACCESSION   NP_001403224
VERSION     NP_001403224.1
DBSOURCE    REFSEQ: accession NM_001416295.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Cabukusta,B., Borst Pauwels,S., Akkermans,J.J.L.L., Blomberg,N.,
            Mulder,A.A., Koning,R.I., Giera,M. and Neefjes,J.
  TITLE     The ORP9-ORP11 dimer promotes sphingomyelin synthesis
  JOURNAL   Elife 12, 91345 (2024)
   PUBMED   39106189
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 741)
  AUTHORS   He,R., Liu,F., Wang,H., Huang,S., Xu,K., Zhang,C., Liu,Y. and Yu,H.
  TITLE     ORP9 and ORP10 form a heterocomplex to transfer
            phosphatidylinositol 4-phosphate at ER-TGN contact sites
  JOURNAL   Cell Mol Life Sci 80 (3), 77 (2023)
   PUBMED   36853333
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 741)
  AUTHORS   Tan,J.X. and Finkel,T.
  TITLE     A phosphoinositide signalling pathway mediates rapid lysosomal
            repair
  JOURNAL   Nature 609 (7928), 815-821 (2022)
   PUBMED   36071159
REFERENCE   4  (residues 1 to 741)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 741)
  AUTHORS   Hacker,B., Schultheiss,C., Doring,M. and Kurzik-Dumke,U.
  TITLE     Molecular partners of hNOT/ALG3, the human counterpart of the
            Drosophila NOT and yeast ALG3 gene, suggest its involvement in
            distinct cellular processes relevant to congenital disorders of
            glycosylation, cancer, neurodegeneration and a variety of further
            pathologies
  JOURNAL   Hum Mol Genet 27 (11), 1858-1878 (2018)
   PUBMED   29547901
REFERENCE   6  (residues 1 to 741)
  AUTHORS   Gauci,S., Helbig,A.O., Slijper,M., Krijgsveld,J., Heck,A.J. and
            Mohammed,S.
  TITLE     Lys-N and trypsin cover complementary parts of the phosphoproteome
            in a refined SCX-based approach
  JOURNAL   Anal Chem 81 (11), 4493-4501 (2009)
   PUBMED   19413330
  REMARK    GeneRIF: Includes data showing N-alpha terminal acetylation of this
            protein (OSBL9_HUMAN), which begins with nASIMEGPLSK following
            cleavage of the initiating Met-1 residue.
REFERENCE   7  (residues 1 to 741)
  AUTHORS   Lessmann,E., Ngo,M., Leitges,M., Minguet,S., Ridgway,N.D. and
            Huber,M.
  TITLE     Oxysterol-binding protein-related protein (ORP) 9 is a PDK-2
            substrate and regulates Akt phosphorylation
  JOURNAL   Cell Signal 19 (2), 384-392 (2007)
   PUBMED   16962287
  REMARK    GeneRIF: Furthermore, mammalian target of rapamycin was implicated
            in ORP9L phosphorylation in HEK293 cells. These studies identify
            ORP9 as a PDK-2 substrate and negative regulator of Akt
            phosphorylation at the PDK-2 site.
REFERENCE   8  (residues 1 to 741)
  AUTHORS   Wyles,J.P. and Ridgway,N.D.
  TITLE     VAMP-associated protein-A regulates partitioning of
            oxysterol-binding protein-related protein-9 between the endoplasmic
            reticulum and Golgi apparatus
  JOURNAL   Exp Cell Res 297 (2), 533-547 (2004)
   PUBMED   15212954
REFERENCE   9  (residues 1 to 741)
  AUTHORS   Jaworski,C.J., Moreira,E., Li,A., Lee,R. and Rodriguez,I.R.
  TITLE     A family of 12 human genes containing oxysterol-binding domains
  JOURNAL   Genomics 78 (3), 185-196 (2001)
   PUBMED   11735225
REFERENCE   10 (residues 1 to 741)
  AUTHORS   Lehto,M., Laitinen,S., Chinetti,G., Johansson,M., Ehnholm,C.,
            Staels,B., Ikonen,E. and Olkkonen,V.M.
  TITLE     The OSBP-related protein family in humans
  JOURNAL   J Lipid Res 42 (8), 1203-1213 (2001)
   PUBMED   11483621
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104170.2, AL772260.3,
            AL831767.8 and AL050343.17.
            
            Summary: This gene encodes a member of the oxysterol-binding
            protein (OSBP) family, a group of intracellular lipid receptors.
            Most members contain an N-terminal pleckstrin homology domain and a
            highly conserved C-terminal OSBP-like sterol-binding domain,
            although some members contain only the sterol-binding domain. This
            family member functions as a cholesterol transfer protein that
            regulates Golgi structure and function. Multiple transcript
            variants, most of which encode distinct isoforms, have been
            identified. Related pseudogenes have been identified on chromosomes
            3, 11 and 12. [provided by RefSeq, Jul 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.3350813.1,
                                           SRR18074968.371918.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..741
                     /product="oxysterol-binding protein-related protein 9
                     isoform k"
                     /note="oxysterol-binding protein-related protein 9;
                     OSBP-related protein 9"
                     /calculated_mol_wt=83655
     Region          23..124
                     /region_name="PH_ORP9"
                     /note="Human Oxysterol binding protein related protein 9
                     Pleckstrin homology (PH) domain; cd13290"
                     /db_xref="CDD:241444"
     Region          382..728
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     CDS             1..741
                     /gene="OSBPL9"
                     /gene_synonym="ORP-9; ORP9"
                     /coded_by="NM_001416295.1:499..2724"
                     /note="isoform k is encoded by transcript variant 17"
                     /db_xref="GeneID:114883"
                     /db_xref="HGNC:HGNC:16386"
                     /db_xref="MIM:606737"
ORIGIN      
        1 mpyrrvtsgr llslaapkma simegplskw tnvmkgwqyr wfvldynagl lsyytskdkm
       61 mrgsrrgcvr lrgavigidd eddstftitv dqktfhfqar daderekwih aleetilrht
      121 lqlqgldsgf vpsvqdfdkk lteadaylqi lieqlklfdd klqnckedeq rkkietlket
      181 tnsmvesikh civllqiaks tinpvdaiyq psplepvist mpsqtvlppe pvqlckseqr
      241 psslpvgpvl atlghhqtpt pnstgsghsp psssltspsh vnlspntvpe fsysssedef
      301 ydadefhqsg sspkrlidss gsasvlthss sgnslkrpdt teslnsslsn gtsdadlfds
      361 hddrdddaea gsveehksvi mhllsqvrlg mdltkvvlpt filerrslle myadffahpd
      421 lfvsisdqkd pkdrmvqvvk wylsafhagr kgsvakkpyn pilgeifqch wtlpndteen
      481 telvsegpvp wvsknsvtfv aeqvshhppi safyaecfnk kiqfnahiwt kskflgmsig
      541 vhnigqgcvs cldydehyil tfpngygrsi ltvpwvelgg ecnincsktg ysaniifhtk
      601 pfyggkkhri taeifspndk ksfcsiegew ngvmyakyat gentvfvdtk klpiikkkvr
      661 kledqneyes rslwkdvtfn lkirdidaat eakhrleerq raearerkek eiqwetrlfh
      721 edgecwvyde pllkrlgaak h
//
LOCUS       NP_001358593             285 aa            linear   PRI 21-NOV-2025
DEFINITION  ribosome biogenesis protein WDR12 isoform 2 [Homo sapiens].
ACCESSION   NP_001358593
VERSION     NP_001358593.1
DBSOURCE    REFSEQ: accession NM_001371664.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Yin,L., Li,L., Gao,M., Qi,Y., Xu,L. and Peng,J.
  TITLE     circMIRIAF aggravates myocardial ischemia-reperfusion injury via
            targeting miR-544/WDR12 axis
  JOURNAL   Redox Biol 73, 103175 (2024)
   PUBMED   38795544
  REMARK    GeneRIF: circMIRIAF aggravates myocardial ischemia-reperfusion
            injury via targeting miR-544/WDR12 axis.
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Holzel,M., Rohrmoser,M., Schlee,M., Grimm,T., Harasim,T.,
            Malamoussi,A., Gruber-Eber,A., Kremmer,E., Hiddemann,W.,
            Bornkamm,G.W. and Eick,D.
  TITLE     Mammalian WDR12 is a novel member of the Pes1-Bop1 complex and is
            required for ribosome biogenesis and cell proliferation
  JOURNAL   J Cell Biol 170 (3), 367-378 (2005)
   PUBMED   16043514
  REMARK    GeneRIF: WDR12 triggers accumulation of p53 in a p19ARF-independent
            manner in proliferating cells but not in quiescent cells.
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   8  (residues 1 to 285)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   9  (residues 1 to 285)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   10 (residues 1 to 285)
  AUTHORS   Nal,B., Mohr,E., Silva,M.I., Tagett,R., Navarro,C., Carroll,P.,
            Depetris,D., Verthuy,C., Jordan,B.R. and Ferrier,P.
  TITLE     Wdr12, a mouse gene encoding a novel WD-Repeat Protein with a
            notchless-like amino-terminal domain
  JOURNAL   Genomics 79 (1), 77-86 (2002)
   PUBMED   11827460
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010900.12.
            
            Summary: This gene encodes a member of the WD repeat protein
            family. WD repeats are minimally conserved regions of approximately
            40 amino acids typically bracketed by gly-his and trp-asp (GH-WD),
            which may facilitate formation of heterotrimeric or multiprotein
            complexes. Members of this family are involved in a variety of
            cellular processes, including cell cycle progression, signal
            transduction, apoptosis, and gene regulation. This protein is
            highly similar to the mouse WD repeat domain 12 protein at the
            amino acid level. The protein encoded by this gene is a component
            of a nucleolar protein complex that affects maturation of the large
            ribosomal subunit.[provided by RefSeq, Dec 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1525021.1,
                                           SRR18074967.2729158.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..285
                     /product="ribosome biogenesis protein WDR12 isoform 2"
                     /note="ribosome biogenesis protein WDR12; WD
                     repeat-containing protein 12"
                     /calculated_mol_wt=31466
     Region          <26..272
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          55..117
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          122..157
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          163..200
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          207..245
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..285
                     /gene="WDR12"
                     /gene_synonym="YTM1"
                     /coded_by="NM_001371664.1:496..1353"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:55759"
                     /db_xref="HGNC:HGNC:14098"
                     /db_xref="MIM:616620"
ORIGIN      
        1 mmtgsvqlkg qrndslscll lsasmdqtil lwewnvernk vkalhccrgh agsvdsiavd
       61 gsgtkfcsgs wdkmlkiwst vptdeedeme estnrprkkq kteqlgltrt pivtlsghme
      121 avssvlwsda eeicsaswdh tirvwdvesg slkstltgnk vfncisyspl ckrlasgstd
      181 rhirlwdprt kdgslvslsl tshtgwvtsv kwsptheqql isgsldnivk lwdtrsckap
      241 lydlaahedk vlsvdwtdtg lllsggadnk lysyrysptt shvga
//
LOCUS       NP_001400250             291 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 2 [Homo sapiens].
ACCESSION   NP_001400250
VERSION     NP_001400250.1
DBSOURCE    REFSEQ: accession NM_001413321.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.204267.1,
                                           SRR1803615.249498.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968832 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..291
                     /product="RNA-binding Raly-like protein isoform 2"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=32199
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          171..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     Region          199..>244
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     Region          249..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     CDS             1..291
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413321.1:317..1192"
                     /note="isoform 2 is encoded by transcript variant 47"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly rleskepfls
      121 vggyvfdydy yrddfynrlf dyhgrvpppp raviplkrpr vavtttrrgk gvfsmkggsr
      181 stasgstgsk lksdelqtik keltqiktki dsllgrleki ekqqkaeaea qkkqleeslv
      241 liqeecvsei adhsteepae ggpdadgeem tdgieedfde dgghelflqi k
//
LOCUS       NP_001394761            1122 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 17 precursor
            [Homo sapiens].
ACCESSION   NP_001394761
VERSION     NP_001394761.1
DBSOURCE    REFSEQ: accession NM_001407832.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1122)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1122)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1122)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1122)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1122)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1122)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1122)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1122)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1122)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1122)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.2261528.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1122
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1122
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 17 precursor"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=121970
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O00411.2)"
                     /calculated_mol_wt=4109
     Region          18..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          95..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          261..290
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          296..323
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          432..629
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          756..1122
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1122
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407832.1:26..3394"
                     /note="isoform 17 precursor is encoded by transcript
                     variant 17"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 msalcwgrga aglkralrpc grpglpgkeg taggvcgprr sssaspqeqd qdrrkdwghv
       61 ellevlqarv rqlqaesvse vvvnrvdvar lpecgsgdgs lqpprkvqmg akdatpvpcg
      121 rwakilekdk rtqqmrmqrl kaklqmpfqs gefkaltrrl qveprllskq magcledctr
      181 qapespweeq larllqeapg klsldveqap sgqhsqaqls gqqqrllaff kcclltdqlp
      241 lahhllvvhh gqrqkrkllt ldmynavmlg warqgafkel vyvlfmvkda gltpdllsya
      301 aalqcmgrqd qdagtiercl eqmsqeglkl qalftavlls eedratvlka vhkvkptfsl
      361 ppqlpppvnt skllrdvyak dgrvsypklh lplktlqclf ekqlhmelas rvcvvsvekp
      421 tlpskevkha rktlktlrdq wekalcralr etknrlerev yegrfslypf lcllderevv
      481 rmllqvlqal paqgesfttl arelsartfs rhvvqrqrvs gqvqalqnhy rkylcllasd
      541 aeigilkphp ayvqllekaa eptltfeavd vpmlcpplpw tsphsgafll sptklmrtve
      601 gatqhqelle tcpptalhga ldaltqlgnc awrvngrvld lvlqlfqakg cpqlgvpapp
      661 seapqppeah lphsaapark aelrrelahc qkvaremhsl raealyrlsl aqhlrdrvfw
      721 lphnmdfrgr typcpphfnh lgsdvarall efaqgrplgp hgldwlkihl vnltglkkre
      781 plrkrlafae evmddildsa dqpltgrkww mgaeepwqtl accmevanav rasdpaayvs
      841 hlpvhqdgsc nglqhyaalg rdsvgaasvn lepsdvpqdv ysgvaaqvev frrqdaqrgm
      901 rvaqvlegfi trkvvkqtvm tvvygvtryg grlqiekrlr elsdfpqefv weashylvrq
      961 vfkslqemfs gtraiqhwlt esarlishmg svvewvtplg vpviqpyrld skvkqigggi
     1021 qsitythngd isrkgltfvs vhdcywthaa dvsvmnqvcr eqfvrlhsep ilqdlsrflv
     1081 krfcsepqki leasqlketl qavpkpgafd leqvkrstyf fs
//
LOCUS       NP_001425593             638 aa            linear   PRI 21-NOV-2025
DEFINITION  TRPM8 channel-associated factor 2 isoform G [Homo sapiens].
ACCESSION   NP_001425593
VERSION     NP_001425593.1
DBSOURCE    REFSEQ: accession NM_001438664.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Yun,D., Liang,J., Wang,X., Fan,J., Wang,X., Li,J., Ren,X., Liu,J.,
            Ren,X., Zhang,H., Shang,G., Jin,W., Chen,L., Li,T., Zhang,C., Yu,S.
            and Yang,X.
  TITLE     TCAF2 drives glioma cellular migratory/invasion properties through
            STAT3 signaling
  JOURNAL   Mol Cell Biochem 479 (7), 1801-1815 (2024)
   PUBMED   38019450
  REMARK    GeneRIF: TCAF2 drives glioma cellular migratory/invasion properties
            through STAT3 signaling.
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Li,Y., Li,J., Chen,H., Lu,B., Lu,F., Chen,H., Liu,H. and Qian,C.
  TITLE     TCAF2 is associated with the immune microenvironment, promotes
            pathogenesis, and impairs prognosis in glioma
  JOURNAL   Gene 883, 147667 (2023)
   PUBMED   37506986
  REMARK    GeneRIF: TCAF2 is associated with the immune microenvironment,
            promotes pathogenesis, and impairs prognosis in glioma.
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Li,X., Qi,Q., Li,Y., Miao,Q., Yin,W., Pan,J., Zhao,Z., Chen,X.,
            Yang,F., Zhou,X., Huang,M., Wang,C., Deng,L., Huang,D., Qi,M.,
            Fan,S., Zhang,Y., Qiu,S., Deng,W., Liu,T., Chen,M., Ye,W. and
            Zhang,D.
  TITLE     TCAF2 in Pericytes Promotes Colorectal Cancer Liver Metastasis via
            Inhibiting Cold-Sensing TRPM8 Channel
  JOURNAL   Adv Sci (Weinh) 10 (30), e2302717 (2023)
   PUBMED   37635201
  REMARK    GeneRIF: TCAF2 in Pericytes Promotes Colorectal Cancer Liver
            Metastasis via Inhibiting Cold-Sensing TRPM8 Channel.
REFERENCE   5  (residues 1 to 638)
  AUTHORS   Hsieh,P., Dang,V., Vollger,M.R., Mao,Y., Huang,T.H., Dishuck,P.C.,
            Baker,C., Cantsilieris,S., Lewis,A.P., Munson,K.M., Sorensen,M.,
            Welch,A.E., Underwood,J.G. and Eichler,E.E.
  TITLE     Evidence for opposing selective forces operating on human-specific
            duplicated TCAF genes in Neanderthals and humans
  JOURNAL   Nat Commun 12 (1), 5118 (2021)
   PUBMED   34433829
  REMARK    GeneRIF: Evidence for opposing selective forces operating on
            human-specific duplicated TCAF genes in Neanderthals and humans.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 638)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 638)
  AUTHORS   Gkika,D., Lemonnier,L., Shapovalov,G., Gordienko,D., Poux,C.,
            Bernardini,M., Bokhobza,A., Bidaux,G., Degerny,C., Verreman,K.,
            Guarmit,B., Benahmed,M., de Launoit,Y., Bindels,R.J., Fiorio Pla,A.
            and Prevarskaya,N.
  TITLE     TRP channel-associated factors are a novel protein family that
            regulates TRPM8 trafficking and activity
  JOURNAL   J Cell Biol 208 (1), 89-107 (2015)
   PUBMED   25559186
  REMARK    GeneRIF: Report novel TRP channel-associated factors that modulate
            TRPM8 activity.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073264.5 and AC106862.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853566.26042.1,
                                           SRR14038191.2576246.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q35"
     Protein         1..638
                     /product="TRPM8 channel-associated factor 2 isoform G"
                     /note="family with sequence similarity 139, member A;
                     protein FAM115C; family with sequence similarity 115,
                     member C; TRP channel-associated factor 2"
                     /calculated_mol_wt=70865
     Region          241..351
                     /region_name="M60-like_N"
                     /note="N-terminal domain of M60-like peptidases;
                     pfam17291"
                     /db_xref="CDD:435844"
     Region          352..608
                     /region_name="Peptidase_M60"
                     /note="Peptidase M60, enhancin and enhancin-like;
                     pfam13402"
                     /db_xref="CDD:433178"
     CDS             1..638
                     /gene="TCAF2"
                     /gene_synonym="FAM115C; FAM139A; GATD9; GATD9B"
                     /coded_by="NM_001438664.1:268..2184"
                     /note="isoform G is encoded by transcript variant 11"
                     /db_xref="GeneID:285966"
                     /db_xref="HGNC:HGNC:26878"
                     /db_xref="MIM:616252"
ORIGIN      
        1 mgpfllnavr wlargqtgkv gvntnlkdlc pllsehglqc slephlnsdl cvycckaysd
       61 keakqlqefv aeggglligg qawwwasqnp ghcplagfpg niilncfgls ilpqtlkagc
      121 fpvptpemrs yhfrkalsqf qailnhengn leksclaklr vdgaaflqip aegvpayisl
      181 hrllrkmlrg sglpavsren pvasdsyeaa vlslatglah sgtdcsqlaq glgtwtcsss
      241 lypskhpitv einginpgnn dcwvstglyl legqnaevsl seaaasaglr vqigchtddl
      301 tkarklsrap vvthqcwmdr tersvsclwg gllyvivpkg sqlgpvpvti rgavpapyyk
      361 lgktsleewk rqmqenlapw gelatdniil tvpttnlqal kdpepvlrlw demmqavarl
      421 aaepfpfrrp erivadvqis agwmhsgypi mchlesvkei inemdmrsrg vwgpihelgh
      481 nqqrhgwefp phtteatcnl wsvyvhetvl gipraqahea lsppererri kahlgkgapl
      541 cdwnvwtale tylqlqeafg wepftqlfae yqtlshlpkd ntgrmnlwvk kfsekvkknl
      601 vpffeawgwp iqkevadsla slpewqenpm qvylrark
//
LOCUS       NP_001394199             341 aa            linear   PRI 21-NOV-2025
DEFINITION  cellular tumor antigen p53 isoform b [Homo sapiens].
ACCESSION   NP_001394199
VERSION     NP_001394199.1
DBSOURCE    REFSEQ: accession NM_001407270.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Mirgayazova,R., Khadiullina,R., Chasov,V., Mingaleeva,R.,
            Miftakhova,R., Rizvanov,A. and Bulatov,E.
  TITLE     Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an Option?
  JOURNAL   Genes (Basel) 11 (6), 704 (2020)
   PUBMED   32630614
  REMARK    GeneRIF: Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an
            Option?
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Flynt,E., Bisht,K., Sridharan,V., Ortiz,M., Towfic,F. and
            Thakurta,A.
  TITLE     Prognosis, Biology, and Targeting of TP53 Dysregulation in Multiple
            Myeloma
  JOURNAL   Cells 9 (2), 287 (2020)
   PUBMED   31991614
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Barnoud,T., Parris,J.L.D. and Murphy,M.E.
  TITLE     Common genetic variants in the TP53 pathway and their impact on
            cancer
  JOURNAL   J Mol Cell Biol 11 (7), 578-585 (2019)
   PUBMED   31152665
  REMARK    GeneRIF: Common genetic variants in the TP53 pathway and their
            impact on cancer.
            Review article
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Hu,W., Chen,S., Thorne,R.F. and Wu,M.
  TITLE     TP53, TP53 Target Genes (DRAM, TIGAR), and Autophagy
  JOURNAL   Adv Exp Med Biol 1206, 127-149 (2019)
   PUBMED   31776983
  REMARK    Review article
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Baugh,E.H., Ke,H., Levine,A.J., Bonneau,R.A. and Chan,C.S.
  TITLE     Why are there hotspot mutations in the TP53 gene in human cancers?
  JOURNAL   Cell Death Differ 25 (1), 154-160 (2018)
   PUBMED   29099487
  REMARK    GeneRIF: TP53 missense mutant alleles that occur in human cancers
            are discussed in the context of high resolution models of these p53
            mutant protein structures to determine the structural features of
            mutations (review).
            Review article
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Aubrey,B.J., Strasser,A. and Kelly,G.L.
  TITLE     Tumor-Suppressor Functions of the TP53 Pathway
  JOURNAL   Cold Spring Harb Perspect Med 6 (5), a026062 (2016)
   PUBMED   27141080
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Soussi,T. and Wiman,K.G.
  TITLE     TP53: an oncogene in disguise
  JOURNAL   Cell Death Differ 22 (8), 1239-1249 (2015)
   PUBMED   26024390
  REMARK    Review article
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Soussi,T.
  TITLE     The TP53 gene network in a postgenomic era
  JOURNAL   Hum Mutat 35 (6), 641-642 (2014)
   PUBMED   24753184
  REMARK    GeneRIF: Recommendations and guidelines for reporting and
            annotating TP53 variants are also provided, to help researchers
            generate standardized data that are easy to understand, analyze,
            and exchange across various cancer variant databases
            Review article
REFERENCE   9  (residues 1 to 341)
  AUTHORS   Anczukow,O., Ware,M.D., Buisson,M., Zetoune,A.B.,
            Stoppa-Lyonnet,D., Sinilnikova,O.M. and Mazoyer,S.
  TITLE     Does the nonsense-mediated mRNA decay mechanism prevent the
            synthesis of truncated BRCA1, CHK2, and p53 proteins?
  JOURNAL   Hum Mutat 29 (1), 65-73 (2008)
   PUBMED   17694537
  REMARK    GeneRIF: the p53 protein encoded by the 770delT allele is as
            abundant as the wild-type protein, as removal of the C-terminal p53
            domain leads to a stabilized mutant protein, whose abundance is
            markedly increased when NMD is inhibited.
REFERENCE   10 (residues 1 to 341)
  AUTHORS   Bourdon,J.C.
  TITLE     p53 Family isoforms
  JOURNAL   Curr Pharm Biotechnol 8 (6), 332-336 (2007)
   PUBMED   18289041
  REMARK    Review article
REFERENCE   11 (residues 1 to 341)
  AUTHORS   Candeias,M.M., Powell,D.J., Roubalova,E., Apcher,S., Bourougaa,K.,
            Vojtesek,B., Bruzzoni-Giovanelli,H. and Fahraeus,R.
  TITLE     Expression of p53 and p53/47 are controlled by alternative
            mechanisms of messenger RNA translation initiation
  JOURNAL   Oncogene 25 (52), 6936-6947 (2006)
   PUBMED   16983332
  REMARK    GeneRIF: harbouring alternative translation initiation sites, the
            p53 mRNA gives rise to different levels of the p53 isoforms which
            help to orchestrate the cell biological outcome of p53 activation
REFERENCE   12 (residues 1 to 341)
  AUTHORS   Murray-Zmijewski,F., Lane,D.P. and Bourdon,J.C.
  TITLE     p53/p63/p73 isoforms: an orchestra of isoforms to harmonise cell
            differentiation and response to stress
  JOURNAL   Cell Death Differ 13 (6), 962-972 (2006)
   PUBMED   16601753
  REMARK    Review article
REFERENCE   13 (residues 1 to 341)
  AUTHORS   Bourdon,J.C., Fernandes,K., Murray-Zmijewski,F., Liu,G., Diot,A.,
            Xirodimas,D.P., Saville,M.K. and Lane,D.P.
  TITLE     p53 isoforms can regulate p53 transcriptional activity
  JOURNAL   Genes Dev 19 (18), 2122-2137 (2005)
   PUBMED   16131611
  REMARK    GeneRIF: p53 isoforms can regulate p53 transcriptional activity.
REFERENCE   14 (residues 1 to 341)
  AUTHORS   Ghosh,A., Stewart,D. and Matlashewski,G.
  TITLE     Regulation of human p53 activity and cell localization by
            alternative splicing
  JOURNAL   Mol Cell Biol 24 (18), 7987-7997 (2004)
   PUBMED   15340061
  REMARK    GeneRIF: mechanism of p53 regulation originating through
            alternative splicing of the human p53 gene resulting in the
            expression of a novel p53 mRNA
REFERENCE   15 (residues 1 to 341)
  AUTHORS   Flaman,J.M., Waridel,F., Estreicher,A., Vannier,A., Limacher,J.M.,
            Gilbert,D., Iggo,R. and Frebourg,T.
  TITLE     The human tumour suppressor gene p53 is alternatively spliced in
            normal cells
  JOURNAL   Oncogene 12 (4), 813-818 (1996)
   PUBMED   8632903
REFERENCE   16 (residues 1 to 341)
  AUTHORS   Schneider,K., Zelley,K., Nichols,K.E., Schwartz Levine,A. and
            Garber,J.
  TITLE     Li-Fraumeni Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301488
REFERENCE   17 (residues 1 to 341)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   18 (residues 1 to 341)
  AUTHORS   Lamb,P. and Crawford,L.
  TITLE     Characterization of the human p53 gene
  JOURNAL   Mol Cell Biol 6 (5), 1379-1385 (1986)
   PUBMED   2946935
REFERENCE   19 (residues 1 to 341)
  AUTHORS   Isobe,M., Emanuel,B.S., Givol,D., Oren,M. and Croce,C.M.
  TITLE     Localization of gene for human p53 tumour antigen to band 17p13
  JOURNAL   Nature 320 (6057), 84-85 (1986)
   PUBMED   3456488
REFERENCE   20 (residues 1 to 341)
  AUTHORS   Benchimol,S., Lamb,P., Crawford,L.V., Sheer,D., Shows,T.B.,
            Bruns,G.A. and Peacock,J.
  TITLE     Transformation associated p53 protein is encoded by a gene on human
            chromosome 17
  JOURNAL   Somat Cell Mol Genet 11 (5), 505-510 (1985)
   PUBMED   2994241
REFERENCE   21 (residues 1 to 341)
  AUTHORS   Harlow,E., Williamson,N.M., Ralston,R., Helfman,D.M. and Adams,T.E.
  TITLE     Molecular cloning and in vitro expression of a cDNA clone for human
            cellular tumor antigen p53
  JOURNAL   Mol Cell Biol 5 (7), 1601-1610 (1985)
   PUBMED   3894933
REFERENCE   22 (residues 1 to 341)
  AUTHORS   Zakut-Houri,R., Bienz-Tadmor,B., Givol,D. and Oren,M.
  TITLE     Human p53 cellular tumor antigen: cDNA sequence and expression in
            COS cells
  JOURNAL   EMBO J 4 (5), 1251-1255 (1985)
   PUBMED   4006916
REFERENCE   23 (residues 1 to 341)
  AUTHORS   Matlashewski,G., Lamb,P., Pim,D., Peacock,J., Crawford,L. and
            Benchimol,S.
  TITLE     Isolation and characterization of a human p53 cDNA clone:
            expression of the human p53 gene
  JOURNAL   EMBO J 3 (13), 3257-3262 (1984)
   PUBMED   6396087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087388.9 and AC007421.13.
            
            Summary: This gene encodes a tumor suppressor protein containing
            transcriptional activation, DNA binding, and oligomerization
            domains. The encoded protein responds to diverse cellular stresses
            to regulate expression of target genes, thereby inducing cell cycle
            arrest, apoptosis, senescence, DNA repair, or changes in
            metabolism. Mutations in this gene are associated with a variety of
            human cancers, including hereditary cancers such as Li-Fraumeni
            syndrome. Alternative splicing of this gene and the use of
            alternate promoters result in multiple transcript variants and
            isoforms. Additional isoforms have also been shown to result from
            the use of alternate translation initiation codons from identical
            transcript variants (PMIDs: 12032546, 20937277). [provided by
            RefSeq, Dec 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2758179.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            NMD candidate                    :: PMID: 16131611, 16601753,
                                                18289041
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..341
                     /product="cellular tumor antigen p53 isoform b"
                     /note="tumor protein 53; mutant tumor protein 53; cellular
                     tumor antigen p53; phosphoprotein p53;
                     transformation-related protein 53; antigen NY-CO-13; tumor
                     supressor p53"
                     /calculated_mol_wt=37695
     Region          1..320
                     /region_name="Interaction with CCAR2.
                     /evidence=ECO:0000269|PubMed:25732823"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          1..83
                     /region_name="Interaction with HRMT1L2.
                     /evidence=ECO:0000269|PubMed:15186775"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          1..44
                     /region_name="Transcription activation (acidic)"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          6..30
                     /region_name="P53_TAD"
                     /note="P53 transactivation motif; pfam08563"
                     /db_xref="CDD:462520"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by HIPK4.
                     /evidence=ECO:0000269|PubMed:18022393; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5, PRPK, AMPK, NUAK1 and ATM.
                     /evidence=ECO:0000269|PubMed:10570149,
                     ECO:0000269|PubMed:11554766, ECO:0000269|PubMed:15866171,
                     ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:17591690,
                     ECO:0000269|PubMed:17967874, ECO:0000269|PubMed:21317932,
                     ECO:0000269|PubMed:28842590; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          17..25
                     /region_name="TADI"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK1, VRK1 and VRK2.
                     /evidence=ECO:0000269|PubMed:10606744,
                     ECO:0000269|PubMed:10951572, ECO:0000269|PubMed:16704422,
                     ECO:0000269|PubMed:31527692; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CHEK2, CK1 and PLK3.
                     /evidence=ECO:0000269|PubMed:10570149,
                     ECO:0000269|PubMed:11447225, ECO:0000269|PubMed:11551930,
                     ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:20041275;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5 and CDK7.
                     /evidence=ECO:0000269|PubMed:17591690,
                     ECO:0000269|PubMed:9372954; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          35..59
                     /region_name="TAD2"
                     /note="Transactivation domain 2; pfam18521"
                     /db_xref="CDD:375947"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK5.
                     /evidence=ECO:0000269|PubMed:17254968; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5, DYRK2, HIPK2 and PKC/PRKCG.
                     /evidence=ECO:0000269|PubMed:11740489,
                     ECO:0000269|PubMed:11780126, ECO:0000269|PubMed:16377624,
                     ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:17591690;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          48..56
                     /region_name="TADII"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          50..96
                     /region_name="Disordered.
                     /evidence=ECO:0000269|PubMed:31953488"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by TAF1 and GRK5.
                     /evidence=ECO:0000269|PubMed:15053879,
                     ECO:0000269|PubMed:20124405; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          66..110
                     /region_name="Interaction with WWOX"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          100..300
                     /region_name="Required for interaction with ZNF385A.
                     /evidence=ECO:0000269|PubMed:17719541"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          109..288
                     /region_name="P53"
                     /note="P53 DNA-binding domain; cd08367"
                     /db_xref="CDD:176262"
     Region          113..236
                     /region_name="Required for interaction with FBXO42.
                     /evidence=ECO:0000269|PubMed:19509332"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          116..292
                     /region_name="Interaction with AXIN1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            120
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000269|PubMed:16793544,
                     ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            120
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:17189187,
                     ECO:0000269|PubMed:19854137, ECO:0000269|PubMed:23431171;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            order(176,179,238,242)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:176262"
     Site            order(177..179,181)
                     /site_type="other"
                     /note="dimerization site [polypeptide binding]"
                     /db_xref="CDD:176262"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB.
                     /evidence=ECO:0000269|PubMed:20959462; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            order(239,241,248,273,275..277,280)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176262"
     Region          241..248
                     /region_name="Interaction with the 53BP2 SH3 domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          256..294
                     /region_name="Interaction with E4F1.
                     /evidence=ECO:0000269|PubMed:10644996"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB.
                     /evidence=ECO:0000269|PubMed:20959462; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          273..280
                     /region_name="Interaction with DNA"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          282..325
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AURKB.
                     /evidence=ECO:0000269|PubMed:20959462; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          305..321
                     /region_name="Bipartite nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            305
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:12724314; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKA, CDK1 and CDK2.
                     /evidence=ECO:0000269|PubMed:10884347,
                     ECO:0000269|PubMed:14702041; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            321
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P02340; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     CDS             1..341
                     /gene="TP53"
                     /gene_synonym="BCC7; BMFS5; LFS1; P53; TRP53"
                     /coded_by="NM_001407270.1:156..1181"
                     /note="isoform b is encoded by transcript variant 13"
                     /db_xref="GeneID:7157"
                     /db_xref="HGNC:HGNC:11998"
                     /db_xref="MIM:191170"
ORIGIN      
        1 meepqsdpsv epplsqetfs dlwkllpenn vlsplpsqam ddlmlspddi eqwftedpgp
       61 deaprmpeaa ppvapapaap tpaapapaps wplsssvpsq ktyqgsygfr lgflhsgtak
      121 svtctyspal nkmfcqlakt cpvqlwvdst pppgtrvram aiykqsqhmt evvrrcphhe
      181 rcsdsdglap pqhlirvegn lrveylddrn tfrhsvvvpy eppevgsdct tihynymcns
      241 scmggmnrrp iltiitleds sgnllgrnsf evrvcacpgr drrteeenlr kkgephhelp
      301 pgstkralpn ntssspqpkk kpldgeyftl qdqtsfqken c
//
LOCUS       NP_001427593             718 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 3 isoform 12 [Homo sapiens].
ACCESSION   NP_001427593
VERSION     NP_001427593.1
DBSOURCE    REFSEQ: accession NM_001440664.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 718)
  AUTHORS   Ghashghaei,M., Liu,Y., Ettles,J., Bombaci,G., Ramkumar,N., Liu,Z.,
            Escano,L., Miko,S.S., Kim,Y., Waldron,J.A., Do,K., MacPherson,K.,
            Yuen,K.A., Taibi,T., Yue,M., Arsalan,A., Jin,Z., Edin,G.,
            Karsan,A., Morin,G.B., Kuchenbauer,F., Perna,F., Bushell,M. and
            Vu,L.P.
  TITLE     Translation efficiency driven by CNOT3 subunit of the CCR4-NOT
            complex promotes leukemogenesis
  JOURNAL   Nat Commun 15 (1), 2340 (2024)
   PUBMED   38491013
  REMARK    GeneRIF: Translation efficiency driven by CNOT3 subunit of the
            CCR4-NOT complex promotes leukemogenesis.
            Erratum:[Nat Commun. 2024 Oct 7;15(1):8674. doi:
            10.1038/s41467-024-53071-1. PMID: 39375334]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 718)
  AUTHORS   Burgess,H.M., Grande,R., Riccio,S., Dinesh,I., Winkler,G.S.,
            Depledge,D.P. and Mohr,I.
  TITLE     CCR4-NOT differentially controls host versus virus poly(a)-tail
            length and regulates HCMV infection
  JOURNAL   EMBO Rep 24 (12), e56327 (2023)
   PUBMED   37846490
  REMARK    GeneRIF: CCR4-NOT differentially controls host versus virus
            poly(a)-tail length and regulates HCMV infection.
REFERENCE   4  (residues 1 to 718)
  AUTHORS   Zhao,P., Meng,Q., Wan,C., Lei,T., Zhang,L., Zhang,X., Tan,L.,
            Zhu,H. and He,X.
  TITLE     Clinical features of CNOT3-associated neurodevelopmental disorder
            in three Chinese patients
  JOURNAL   Neurogenetics 24 (2), 129-136 (2023)
   PUBMED   36802310
  REMARK    GeneRIF: Clinical features of CNOT3-associated neurodevelopmental
            disorder in three Chinese patients.
REFERENCE   5  (residues 1 to 718)
  AUTHORS   McLenachan,S., Zhang,D., Grainok,J., Zhang,X., Huang,Z., Chen,S.C.,
            Zaw,K., Lima,A., Jennings,L., Roshandel,D., Moon,S.Y., Heath
            Jeffery,R.C., Attia,M.S., Thompson,J.A., Lamey,T.M., McLaren,T.L.,
            De Roach,J., Fletcher,S. and Chen,F.K.
  TITLE     Determinants of Disease Penetrance in PRPF31-Associated Retinopathy
  JOURNAL   Genes (Basel) 12 (10), 1542 (2021)
   PUBMED   34680937
  REMARK    GeneRIF: Determinants of Disease Penetrance in PRPF31-Associated
            Retinopathy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 718)
  AUTHORS   Yin,X., Warner,D.R., Roberts,E.A., Pisano,M.M. and Greene,R.M.
  TITLE     Identification of novel CBP interacting proteins in embryonic
            orofacial tissue
  JOURNAL   Biochem Biophys Res Commun 329 (3), 1010-1017 (2005)
   PUBMED   15752756
REFERENCE   7  (residues 1 to 718)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 718)
  AUTHORS   Aoki,T., Okada,N., Wakamatsu,T. and Tamura,T.A.
  TITLE     TBP-interacting protein 120B, which is induced in relation to
            myogenesis, binds to NOT3
  JOURNAL   Biochem Biophys Res Commun 296 (5), 1097-1103 (2002)
   PUBMED   12207886
  REMARK    GeneRIF: TBP-interacting protein 120B binds to NOT3
REFERENCE   9  (residues 1 to 718)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
REFERENCE   10 (residues 1 to 718)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC245052.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK300434.1, SRR14038197.609634.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..718
                     /product="CCR4-NOT transcription complex subunit 3 isoform
                     12"
                     /note="NOT3 (negative regulator of transcription 3, yeast)
                     homolog; CCR4-associated factor 3; leukocyte receptor
                     cluster member 2"
                     /calculated_mol_wt=76438
     Region          3..229
                     /region_name="Not3"
                     /note="Not1 N-terminal domain, CCR4-Not complex component;
                     pfam04065"
                     /db_xref="CDD:461155"
     Region          240..534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75175.1)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Region          620..>684
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; cl02384"
                     /db_xref="CDD:470561"
     CDS             1..718
                     /gene="CNOT3"
                     /gene_synonym="IDDSADF; LENG2; NOT3; NOT3H"
                     /coded_by="NM_001440664.1:283..2439"
                     /note="isoform 12 is encoded by transcript variant 13"
                     /db_xref="GeneID:4849"
                     /db_xref="HGNC:HGNC:7879"
                     /db_xref="MIM:604910"
ORIGIN      
        1 madkrklqge idrclkkvse gveqfediwq klhnaananq kekyeadlkk eikklqrlrd
       61 qiktwvasne ikdkrqlidn rklietqmer fkvveretkt kayskeglgl aqkvdpaqke
      121 keevgqwltn tidtlnmqvd qfesevesls vqtrkkkgdk dkqdrieglk rhiekhryhv
      181 rmletilrml dndsilvdai rkikddveyy vdssqdpdfe eneflyddld ledipqalva
      241 tsppshshme deifnqssst ptsttssspi ppspanctte nseddkkrgr stdsevsqsp
      301 akngskpvhs nqhpqspavp ptypsgpppa asalsttpgn ngvpapaapp salgpkaspa
      361 pshnsgtpap yaqavappap sgpsttqprp psvqpsgggg ggsggggsss ssnssaggga
      421 gkqngatsys svvadspaev alsssggnna ssqalgppsg phnpppstsk epsaaaptga
      481 ggvapgsgnn sggpsllvpl pvnppssptp sfsdakaaga llngppqfst apeikapepl
      541 sslksmaera aissgiedpv ptlhlterdi ilsstsappa saqpplqlse vniplslgvc
      601 plgpvpltke qlyqqameea awhhmphpsd serirqylpr npcptppyhh qmppphsdtv
      661 efyqrlstet lffifyylev qqgprgslgp pgfaataavp praggvralr hsiwqprp
//
LOCUS       NP_057728                281 aa            linear   PRI 21-NOV-2025
DEFINITION  protein Largen isoform 2 [Homo sapiens].
ACCESSION   NP_057728
VERSION     NP_057728.1
DBSOURCE    REFSEQ: accession NM_016644.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Thiebaut,R., Esmiol,S., Lecine,P., Mahfouz,B., Hermant,A.,
            Nicoletti,C., Parnis,S., Perroy,J., Borg,J.P., Pascoe,L.,
            Hugot,J.P. and Ollendorff,V.
  TITLE     Characterization and Genetic Analyses of New Genes Coding for NOD2
            Interacting Proteins
  JOURNAL   PLoS One 11 (11), e0165420 (2016)
   PUBMED   27812135
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Scannell Bryan,M., Argos,M., Pierce,B., Tong,L., Rakibuz-Zaman,M.,
            Ahmed,A., Rahman,M., Islam,T., Yunus,M., Parvez,F., Roy,S.,
            Jasmine,F., Baron,J.A., Kibriya,M.G. and Ahsan,H.
  TITLE     Genome-wide association studies and heritability estimates of body
            mass index related phenotypes in Bangladeshi adults
  JOURNAL   PLoS One 9 (8), e105062 (2014)
   PUBMED   25133637
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Yamamoto,K., Gandin,V., Sasaki,M., McCracken,S., Li,W.,
            Silvester,J.L., Elia,A.J., Wang,F., Wakutani,Y., Alexandrova,R.,
            Oo,Y.D., Mullen,P.J., Inoue,S., Itsumi,M., Lapin,V., Haight,J.,
            Wakeham,A., Shahinian,A., Ikura,M., Topisirovic,I., Sonenberg,N.
            and Mak,T.W.
  TITLE     Largen: a molecular regulator of mammalian cell size control
  JOURNAL   Mol Cell 53 (6), 904-915 (2014)
   PUBMED   24656129
  REMARK    GeneRIF: Largen, the product of a gene PRR16, increases cell size
            upon overexpression in human cells.
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Wang,H., St Julien,K.R., Stevenson,D.K., Hoffmann,T.J., Witte,J.S.,
            Lazzeroni,L.C., Krasnow,M.A., Quaintance,C.C., Oehlert,J.W.,
            Jelliffe-Pawlowski,L.L., Gould,J.B., Shaw,G.M. and O'Brodovich,H.M.
  TITLE     A genome-wide association study (GWAS) for bronchopulmonary
            dysplasia
  JOURNAL   Pediatrics 132 (2), 290-297 (2013)
   PUBMED   23897914
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Kennedy,R.B., Ovsyannikova,I.G., Pankratz,V.S., Haralambieva,I.H.,
            Vierkant,R.A. and Poland,G.A.
  TITLE     Genome-wide analysis of polymorphisms associated with cytokine
            responses in smallpox vaccine recipients
  JOURNAL   Hum Genet 131 (9), 1403-1421 (2012)
   PUBMED   22610502
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Sakai,Y., Shaw,C.A., Dawson,B.C., Dugas,D.V., Al-Mohtaseb,Z.,
            Hill,D.E. and Zoghbi,H.Y.
  TITLE     Protein interactome reveals converging molecular pathways among
            autism disorders
  JOURNAL   Sci Transl Med 3 (86), 86ra49 (2011)
   PUBMED   21653829
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Barberi,T., Willis,L.M., Socci,N.D. and Studer,L.
  TITLE     Derivation of multipotent mesenchymal precursors from human
            embryonic stem cells
  JOURNAL   PLoS Med 2 (6), e161 (2005)
   PUBMED   15971941
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC113418.2, AC104110.2 and AC093301.3.
            
            Transcript Variant: This variant (2) contains an additional exon in
            the 5' region, and it thus differs in the 5' UTR and initiates
            translation at an alternate start codon, compared to variant 1. The
            encoded isoform (2) has a distinct N-terminus and is shorter than
            isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF242769.1, SRR14038193.4388743.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968189,
                                           SAMEA2142670 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q23.1"
     Protein         1..281
                     /product="protein Largen isoform 2"
                     /note="mesenchymal stem cell protein DSC54; proline-rich
                     protein 16; protein Largen"
                     /calculated_mol_wt=30256
     Region          31..281
                     /region_name="DUF4589"
                     /note="Domain of unknown function (DUF4589); pfam15252"
                     /db_xref="CDD:464592"
     CDS             1..281
                     /gene="PRR16"
                     /gene_synonym="DSC54; LARGEN"
                     /coded_by="NM_016644.3:382..1227"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4127.1"
                     /db_xref="GeneID:51334"
                     /db_xref="HGNC:HGNC:29654"
                     /db_xref="MIM:615931"
ORIGIN      
        1 maqsgltats asqvqaillp qpasvrhyaw vvdqidtlts dlqledemtd ssktdtlnss
       61 ssgttassle kikvqanapl ikppahpsai ltvlrkpnpp pppprltpvk cedpkrvvpt
      121 anpvktngtl lrngglpggp nkipngdicc ipnsnldkap vqllmhrpek drcpqagpre
      181 rvrfnekvqy hgycpdcdtr yniknrevhl hsepvhppgk iphqgpplpp tphlppfple
      241 nggmgishsn sfppirpatv ppptapkpqk tilrkstttt v
//
LOCUS       NP_001393537            1149 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 8 [Homo sapiens].
ACCESSION   NP_001393537 XP_047279792
VERSION     NP_001393537.1
DBSOURCE    REFSEQ: accession NM_001406608.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1149)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1149)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1149)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1149)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1149)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1149)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1149)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1149)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1149)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1149)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            On May 18, 2022 this sequence version replaced XP_047279792.1.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2910018.1,
                                           SRR18074969.2669839.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1149
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1149
                     /product="hamartin isoform 8"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=127998
     Region          7..718
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          402..786
                     /region_name="Mediates interaction with WDR45B.
                     /evidence=ECO:0000269|PubMed:28561066"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Region          438..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <704..>941
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          991..1070
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1085
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1116..1149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1149
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406608.1:218..3667"
                     /note="isoform 8 is encoded by transcript variant 22"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt ggkgtplgtp atspppaplc hsddyvhisl pqatvtpprk
      421 eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed siekdkeeaa
      481 isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv npeplhssld
      541 klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp trvgfgsgqp
      601 ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr liqqgadahs
      661 kelnklplps ksvdwthfgg sppsdeirtl rdqllllhnq llyerfkrqq halrnrrllr
      721 kvikaaalee hnaamkdqlk lqekdiqmwk vslqkeqary nqlqeqrdtm vtklhsqirq
      781 lqhdreefyn qsqelqtkle dcrnmiaelr ielkkannkl snsesvqqqm eflnrqllvl
      841 gevnelyleq lqnkhsdttk evemmkaayr keleknrshv lqqtqrldts qkrilelesh
      901 lakkdhllle qkkyledvkl qargqlqaae sryeaqkrit qvfeleildl ygrlekdgll
      961 kkleeekaea aeaaeerldc cndgcsdsmv ghneeasghn getktprpss argssgsrgg
     1021 ggssssssel stpekpphqr agpfssrwet tmgeasasip ttvgslpssk sflgmkarel
     1081 frnksesqcd edgmtsslse slktelgkdl gveakiplnl dgphpspptp dsvgqlhimd
     1141 ynethhehs
//
LOCUS       NP_001427527             384 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform m [Homo sapiens].
ACCESSION   NP_001427527
VERSION     NP_001427527.1
DBSOURCE    REFSEQ: accession NM_001440598.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 384)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 384)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 384)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 384)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 384)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 384)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 384)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.17109.1,
                                           SRR5189667.176797.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..384
                     /product="polycomb protein EED isoform m"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=43795
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q921E6; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Region          66..106
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          68..381
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(83,87,93..94,106..107,126,130,136..137,152..153,170,
                     175,181..182,223,238,248..249,266,268,274,282,301..302,
                     321,326,332..333,349..350,370,374,380..381)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          111..148
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          158..220
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          227..300
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          308..348
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          356..380
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..384
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001440598.1:478..1632"
                     /note="isoform m is encoded by transcript variant 13"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdenvt lyechsqgei rllqsyvdad
       61 adenfytcaw tydsntshpl lavagsrgii riinpitmqc ikhyvghgna inelkfhprd
      121 pnlllsvskd halrlwniqt dtlvaifggv eghrdevlsa dydllgekim scgmdhslkl
      181 wrinskrmmn aikesydynp nktnrpfisq kihfpdfstr dihrnyvdcv rwlgdlilsk
      241 sgrailhshq qcmrdpvspn lrqhlscena ivcwkpgkme ddidkikpse snvtilgrfd
      301 ysqcdiwymr fsmdfwqkml algnqvgkly vwdlevedph kakcttlthh kcgaairqts
      361 fsrdssilia vcddasiwrw drlr
//
LOCUS       NP_001424952             689 aa            linear   PRI 21-NOV-2025
DEFINITION  MAP/microtubule affinity-regulating kinase 3 isoform m [Homo
            sapiens].
ACCESSION   NP_001424952 XP_016876783 XP_054232042
VERSION     NP_001424952.1
DBSOURCE    REFSEQ: accession NM_001438023.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 689)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 689)
  AUTHORS   Aparicio-Bautista,D.I., Jimenez-Ortega,R.F., Becerra-Cervera,A.,
            Aquino-Galvez,A., de Leon-Suarez,V.P., Casas-Avila,L., Salmeron,J.,
            Hidalgo-Bravo,A., Rivera-Paredez,B. and Velazquez-Cruz,R.
  TITLE     Interaction between MARK3 (rs11623869), PLCB4 (rs6086746) and
            GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women
  JOURNAL   Front Endocrinol (Lausanne) 15, 1392063 (2024)
   PUBMED   38715801
  REMARK    GeneRIF: Interaction between MARK3 (rs11623869), PLCB4 (rs6086746)
            and GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 689)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 689)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 689)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 689)
  AUTHORS   Li,M.G., Katsura,K., Nomiyama,H., Komaki,K., Ninomiya-Tsuji,J.,
            Matsumoto,K., Kobayashi,T. and Tamura,S.
  TITLE     Regulation of the interleukin-1-induced signaling pathways by a
            novel member of the protein phosphatase 2C family (PP2Cepsilon)
  JOURNAL   J Biol Chem 278 (14), 12013-12021 (2003)
   PUBMED   12556533
REFERENCE   7  (residues 1 to 689)
  AUTHORS   Sun,T.Q., Lu,B., Feng,J.J., Reinhard,C., Jan,Y.N., Fantl,W.J. and
            Williams,L.T.
  TITLE     PAR-1 is a Dishevelled-associated kinase and a positive regulator
            of Wnt signalling
  JOURNAL   Nat Cell Biol 3 (7), 628-636 (2001)
   PUBMED   11433294
REFERENCE   8  (residues 1 to 689)
  AUTHORS   Peng,C.Y., Graves,P.R., Ogg,S., Thoma,R.S., Byrnes,M.J. 3rd, Wu,Z.,
            Stephenson,M.T. and Piwnica-Worms,H.
  TITLE     C-TAK1 protein kinase phosphorylates human Cdc25C on serine 216 and
            promotes 14-3-3 protein binding
  JOURNAL   Cell Growth Differ 9 (3), 197-208 (1998)
   PUBMED   9543386
REFERENCE   9  (residues 1 to 689)
  AUTHORS   Ono,T., Kawabe,T., Sonta,S. and Okamoto,T.
  TITLE     Assignment of MARK3 alias KP78 to human chromosome band 14q32.3 by
            in situ hybridization
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 101-102 (1997)
   PUBMED   9533022
REFERENCE   10 (residues 1 to 689)
  AUTHORS   Meller,N., Liu,Y.C., Collins,T.L., Bonnefoy-Berard,N., Baier,G.,
            Isakov,N. and Altman,A.
  TITLE     Direct interaction between protein kinase C theta (PKC theta) and
            14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition
            of PKC theta translocation and function
  JOURNAL   Mol Cell Biol 16 (10), 5782-5791 (1996)
   PUBMED   8816492
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133367.4 and KF456011.1.
            
            On or before Apr 14, 2025 this sequence version replaced
            XP_016876783.1, XP_054232042.1.
            
            Summary: The protein encoded by this gene is activated by
            phosphorylation and in turn is involved in the phosphorylation of
            tau proteins MAP2 and MAP4. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.258470.1,
                                           SRR14038194.3332504.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..689
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.32-q32.33"
     Protein         1..689
                     /product="MAP/microtubule affinity-regulating kinase 3
                     isoform m"
                     /EC_number="2.7.11.1"
                     /note="EMK-2; C-TAK1; ELKL motif kinase 2; protein kinase
                     STK10; ser/Thr protein kinase PAR-1; cdc25C-associated
                     protein kinase 1; MAP/microtubule affinity-regulating
                     kinase 3; serine/threonine-protein kinase p78"
                     /calculated_mol_wt=77271
     Region          18..243
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          261..303
                     /region_name="UBA_MARK3_4"
                     /note="UBA domain found in MAP/microtubule
                     affinity-regulating kinase MARK3, MARK4, and similar
                     proteins; cd14407"
                     /db_xref="CDD:270590"
     Region          590..687
                     /region_name="MARK1-3_C"
                     /note="C-terminal, kinase associated domain 1 (KA1), a
                     phospholipid binding domain, of microtubule
                     affinity-regulating kinases 1-3; cd12196"
                     /db_xref="CDD:213381"
     Site            order(592,595,665,667..668)
                     /site_type="other"
                     /note="putative phospholipid binding site [chemical
                     binding]"
                     /db_xref="CDD:213381"
     CDS             1..689
                     /gene="MARK3"
                     /gene_synonym="CTAK1; KP78; Par-1a; PAR1A; VIPB"
                     /coded_by="NM_001438023.1:616..2685"
                     /note="isoform m is encoded by transcript variant 13"
                     /db_xref="GeneID:4140"
                     /db_xref="HGNC:HGNC:6897"
                     /db_xref="MIM:602678"
ORIGIN      
        1 mstrtplptv nerdtenvai kiidktqlnp tslqklfrev rimkilnhpn ivklfeviet
       61 ektlylimey asggevfdyl vahgrmkeke arskfrqivs avqychqkri vhrdlkaenl
      121 lldadmniki adfgfsneft vggkldtfcg sppyaapelf qgkkydgpev dvwslgvily
      181 tlvsgslpfd gqnlkelrer vlrgkyripf ymstdcenll krflvlnpik rgtleqimkd
      241 rwinagheed elkpfvepel disdqkridi mvgmgysqee iqeslskmky deitatylll
      301 grksseldas dsssssnlsl akvrpssdln nstgqsphhk vqrsvsssqk qrrysdhagp
      361 aipsvvaypk rsqtstadsd lkedgissrk ssgsavggkg iapaspmlgn asnpnkadip
      421 erkksstvps sntasggmtr rntyvcsert tadrhsviqn gkenstipdq rtpvasthsi
      481 ssaatpdrir fprgtasrst fhgqprerrt atyngppasp slsheatpls qtrsrgstnl
      541 fskltskltr rnmsfrfikr lpteyerngr yegssrnvsa eqkdenkeak prslrftwsm
      601 kttssmdpgd mmreirkvld anncdyeqre rfllfcvhgd ghaenlvqwe mevcklprls
      661 lngvrfkris gtsiafknia skianelkl
//
LOCUS       NP_001425421             751 aa            linear   PRI 21-NOV-2025
DEFINITION  AT-rich interactive domain-containing protein 1B isoform 14 [Homo
            sapiens].
ACCESSION   NP_001425421
VERSION     NP_001425421.1
DBSOURCE    REFSEQ: accession NM_001438492.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 751)
  AUTHORS   Bosch,E., Guse,E., Kirchner,P., Winterpacht,A., Walther,M.,
            Alders,M., Kerkhof,J., Ekici,A.B., Sticht,H., Sadikovic,B., Reis,A.
            and Vasileiou,G.
  TITLE     The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation
  JOURNAL   Hum Genet 143 (8), 965-978 (2024)
   PUBMED   39028335
  REMARK    GeneRIF: The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation.
REFERENCE   3  (residues 1 to 751)
  AUTHORS   Huang,X., Li,H., Yang,S., Ma,M., Lian,Y., Wu,X., Qi,X., Wang,X.,
            Rong,W. and Sheng,X.
  TITLE     De novo variation in ARID1B gene causes Coffin-Siris syndrome 1 in
            a Chinese family with excessive early-onset high myopia
  JOURNAL   BMC Med Genomics 17 (1), 142 (2024)
   PUBMED   38790056
  REMARK    GeneRIF: De novo variation in ARID1B gene causes Coffin-Siris
            syndrome 1 in a Chinese family with excessive early-onset high
            myopia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 751)
  AUTHORS   Hurlstone,A.F., Olave,I.A., Barker,N., van Noort,M. and Clevers,H.
  TITLE     Cloning and characterization of hELD/OSA1, a novel BRG1 interacting
            protein
  JOURNAL   Biochem J 364 (Pt 1), 255-264 (2002)
   PUBMED   11988099
  REMARK    GeneRIF: Cloning and characterization of hELD/OSA1, a novel BRG1
            interacting protein.
REFERENCE   5  (residues 1 to 751)
  AUTHORS   Phelan,M.L., Sif,S., Narlikar,G.J. and Kingston,R.E.
  TITLE     Reconstitution of a core chromatin remodeling complex from SWI/SNF
            subunits
  JOURNAL   Mol Cell 3 (2), 247-253 (1999)
   PUBMED   10078207
REFERENCE   6  (residues 1 to 751)
  AUTHORS   Imbert,G., Saudou,F., Yvert,G., Devys,D., Trottier,Y.,
            Garnier,J.M., Weber,C., Mandel,J.L., Cancel,G., Abbas,N., Durr,A.,
            Didierjean,O., Stevanin,G., Agid,Y. and Brice,A.
  TITLE     Cloning of the gene for spinocerebellar ataxia 2 reveals a locus
            with high sensitivity to expanded CAG/glutamine repeats
  JOURNAL   Nat Genet 14 (3), 285-291 (1996)
   PUBMED   8896557
REFERENCE   7  (residues 1 to 751)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
REFERENCE   8  (residues 1 to 751)
  AUTHORS   Vergano,S.A., van der Sluijs,P.J. and Santen,G.
  TITLE     ARID1B-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31132234
REFERENCE   9  (residues 1 to 751)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
REFERENCE   10 (residues 1 to 751)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355297.20 and AL162578.13.
            
            Summary: This locus encodes an AT-rich DNA interacting
            domain-containing protein. The encoded protein is a component of
            the SWI/SNF chromatin remodeling complex and may play a role in
            cell-cycle activation. The protein encoded by this locus is similar
            to AT-rich interactive domain-containing protein 1A. These two
            proteins function as alternative, mutually exclusive ARID-subunits
            of the SWI/SNF complex. The associated complexes play opposing
            roles. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR13170464.234338.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..751
                     /product="AT-rich interactive domain-containing protein 1B
                     isoform 14"
                     /note="BRG1-binding protein ELD/OSA1; ELD (eyelid)/OSA
                     protein; BRG1-associated factor 250b; ARID
                     domain-containing protein 1B; AT rich interactive domain
                     1B (SWI1-like)"
                     /calculated_mol_wt=73626
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          155..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          321..414
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          487..546
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            487
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4N7; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          502..506
                     /region_name="LXXLL"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            608
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4N7; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            640
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     CDS             1..751
                     /gene="ARID1B"
                     /gene_synonym="6A3-5; BAF250B; BRIGHT; CSS1; DAN15;
                     ELD/OSA1; MRD12; OSA2; P250R; SMARCF2"
                     /coded_by="NM_001438492.1:304..2559"
                     /note="isoform 14 is encoded by transcript variant 15"
                     /db_xref="GeneID:57492"
                     /db_xref="HGNC:HGNC:18040"
                     /db_xref="MIM:614556"
ORIGIN      
        1 maaraaaaaa aaaararara gsgerrappg prpapgardl eagargaaaa aaapgpmlgg
       61 ggdgggglns vhhhpllprh elnmahnaga aaaagthsak sggseaalke ggsaaalsss
      121 ssssaaaaaa ssssssgpgs ametgllpnh klktvgeapa apphqqhhhh hhahhhhhha
      181 hhlhhhhalq qqlnqfqqqq qqqqqqqqqq qqqqhpisnn nslggaggga pqpgpdmeqp
      241 qhggakdsaa ggqadppgpp llskpgdedd appkmgepag gryehpglga lgtqqppvav
      301 pgggggpaav pefnnyygsa apasggpggr agpcfdqhgg qqspgmgmmh sasaaaagap
      361 gsmdplqnsh egypnsqcnh ypgysrpgag gggggggggg ggsggggggg gagaggagag
      421 avaaaaaaaa aaaggggggg yggssagygv lssprqqggg mmmgpgggga aslskaaags
      481 aaggfqrfag qnqhpsgatp tlnqlltsps pmmrsyggsy peysspsapp pppsqpqsqa
      541 aaagaaaggq qaaagmglgk dmgaqyaaas pawaaaqqrs hpamspgtpg ptmgrsqgsp
      601 mdpmvmkrpq lygmgsnphs qpqqsspypg gsygppgpqr ypigiqgrtp gamagmqypq
      661 qqmppqygqq gvsgycqqgq qpyysqqpqp phlppqaqyl psqsqqryqp qqdmsqegyg
      721 trsqpplapg kpnhedlnli qqerpsslpr t
//
LOCUS       NP_001427345             250 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 8 precursor [Homo
            sapiens].
ACCESSION   NP_001427345
VERSION     NP_001427345.1
DBSOURCE    REFSEQ: accession NM_001440416.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 250)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 250)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 250)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3 and AP004147.3.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2122572.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..250
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     8 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=25325
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..>230
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     CDS             1..250
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440416.1:711..1463"
                     /note="isoform 8 precursor is encoded by transcript
                     variant 18"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk vgaslspppp
      241 aelhpppslp
//
LOCUS       NP_036366                228 aa            linear   PRI 21-NOV-2025
DEFINITION  RING1 and YY1-binding protein [Homo sapiens].
ACCESSION   NP_036366
VERSION     NP_036366.3
DBSOURCE    REFSEQ: accession NM_012234.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Chen,X., Liu,W., Li,T., Xia,W. and Chen,D.
  TITLE     Glucose-induced RYBP suppresses tumor cell aerobic glycolysis and
            migration
  JOURNAL   Biochem Biophys Res Commun 719, 150089 (2024)
   PUBMED   38735205
  REMARK    GeneRIF: Glucose-induced RYBP suppresses tumor cell aerobic
            glycolysis and migration.
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Ciapponi,M., Karlukova,E., Schkolziger,S., Benda,C. and Muller,J.
  TITLE     Structural basis of the histone ubiquitination read-write mechanism
            of RYBP-PRC1
  JOURNAL   Nat Struct Mol Biol 31 (7), 1023-1027 (2024)
   PUBMED   38528151
  REMARK    GeneRIF: Structural basis of the histone ubiquitination read-write
            mechanism of RYBP-PRC1.
            Erratum:[Nat Struct Mol Biol. 2025 Sep;32(9):1840. doi:
            10.1038/s41594-025-01674-7. PMID: 40866579]
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Araujo-Abad,S., Rizzuti,B., Vidal,M., Abian,O., Farez-Vidal,M.E.,
            Velazquez-Campoy,A., de Juan Romero,C. and Neira,J.L.
  TITLE     Unveiling the Binding between the Armadillo-Repeat Domain of
            Plakophilin 1 and the Intrinsically Disordered Transcriptional
            Repressor RYBP
  JOURNAL   Biomolecules 14 (5), 561 (2024)
   PUBMED   38785968
  REMARK    GeneRIF: Unveiling the Binding between the Armadillo-Repeat Domain
            of Plakophilin 1 and the Intrinsically Disordered Transcriptional
            Repressor RYBP.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 228)
  AUTHORS   Cui,W., Huang,Z., Jin,S.G., Johnson,J., Lau,K.H., Hostetter,G. and
            Pfeifer,G.P.
  TITLE     Deficiency of the Polycomb Protein RYBP and TET Methylcytosine
            Oxidases Promotes Extensive CpG Island Hypermethylation and
            Malignant Transformation
  JOURNAL   Cancer Res 83 (15), 2480-2495 (2023)
   PUBMED   37272752
  REMARK    GeneRIF: Deficiency of the Polycomb Protein RYBP and TET
            Methylcytosine Oxidases Promotes Extensive CpG Island
            Hypermethylation and Malignant Transformation.
REFERENCE   6  (residues 1 to 228)
  AUTHORS   Schlisio,S., Halperin,T., Vidal,M. and Nevins,J.R.
  TITLE     Interaction of YY1 with E2Fs, mediated by RYBP, provides a
            mechanism for specificity of E2F function
  JOURNAL   EMBO J 21 (21), 5775-5786 (2002)
   PUBMED   12411495
  REMARK    GeneRIF: interacts specifically with the E2F2 and E2F3 family
            members, dependent on the marked box domain in these proteins
REFERENCE   7  (residues 1 to 228)
  AUTHORS   Sawa,C., Yoshikawa,T., Matsuda-Suzuki,F., Delehouzee,S., Goto,M.,
            Watanabe,H., Sawada,J., Kataoka,K. and Handa,H.
  TITLE     YEAF1/RYBP and YAF-2 are functionally distinct members of a
            cofactor family for the YY1 and E4TF1/hGABP transcription factors
  JOURNAL   J Biol Chem 277 (25), 22484-22490 (2002)
   PUBMED   11953439
  REMARK    GeneRIF: YEAF1/RYBP and YAF-2 are functionally distinct members of
            a cofactor family for the YY1 and E4TF1/hGABP transcription
            factors.
REFERENCE   8  (residues 1 to 228)
  AUTHORS   Zheng,L., Schickling,O., Peter,M.E. and Lenardo,M.J.
  TITLE     The death effector domain-associated factor plays distinct
            regulatory roles in the nucleus and cytoplasm
  JOURNAL   J Biol Chem 276 (34), 31945-31952 (2001)
   PUBMED   11395500
REFERENCE   9  (residues 1 to 228)
  AUTHORS   Trimarchi,J.M., Fairchild,B., Wen,J. and Lees,J.A.
  TITLE     The E2F6 transcription factor is a component of the mammalian
            Bmi1-containing polycomb complex
  JOURNAL   Proc Natl Acad Sci U S A 98 (4), 1519-1524 (2001)
   PUBMED   11171983
REFERENCE   10 (residues 1 to 228)
  AUTHORS   Garcia,E., Marcos-Gutierrez,C., del Mar Lorente,M., Moreno,J.C. and
            Vidal,M.
  TITLE     RYBP, a new repressor protein that interacts with components of the
            mammalian Polycomb complex, and with the transcription factor YY1
  JOURNAL   EMBO J 18 (12), 3404-3418 (1999)
   PUBMED   10369680
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC255560.1.
            
            On Aug 16, 2006 this sequence version replaced NP_036366.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN03267754
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000643872.4/ ENSP00000493835.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..228
                     /product="RING1 and YY1-binding protein"
                     /note="YY1 and E4TF1 associated factor 1; death effector
                     domain-associated factor; ring1 interactor RYBP;
                     apoptin-associating protein 1; DED-associated factor"
                     /calculated_mol_wt=24690
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N488.2)"
     Region          22..45
                     /region_name="zf-RanBP"
                     /note="Zn-finger in Ran binding protein and others;
                     pfam00641"
                     /db_xref="CDD:395516"
     Region          25..44
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275376"
     Region          65..156
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N488.2)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N488.2)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N488.2)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N488.2)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N488.2)"
     Region          143..226
                     /region_name="Interaction with GABPB1 and FANK1.
                     /evidence=ECO:0000269|PubMed:11953439,
                     ECO:0000269|PubMed:27060496"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N488.2)"
     Region          145..176
                     /region_name="YAF2_RYBP"
                     /note="Yaf2/RYBP C-terminal binding motif; pfam17219"
                     /db_xref="CDD:465386"
     Region          172..228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N488.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8N488.2)"
     CDS             1..228
                     /gene="RYBP"
                     /gene_synonym="AAP1; APAP-1; DEDAF; YEAF1"
                     /coded_by="NM_012234.7:184..870"
                     /db_xref="GeneID:23429"
                     /db_xref="HGNC:HGNC:10480"
                     /db_xref="MIM:607535"
ORIGIN      
        1 mtmgdkkspt rpkrqakpaa degfwdcsvc tfrnsaeafk csicdvrkgt strkprinsq
       61 lvaqqvaqqy atppppkkek kekvekqdke kpekdkeisp svtkkntnkk tkpksdilkd
      121 ppseansiqs anattktset nhtsrprlkn vdrstaqqla vtvgnvtvii tdfkektrss
      181 stssstvtss agseqqnqss sgsestdkgs srsstpkgdm savndesf
//
LOCUS       NP_001400611             332 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 15 precursor [Homo sapiens].
ACCESSION   NP_001400611
VERSION     NP_001400611.1
DBSOURCE    REFSEQ: accession NM_001413682.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 332)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 332)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 332)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.700343.1,
                                           SRR14038196.1291667.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..332
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 15 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=33070
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..312
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            277..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     CDS             1..332
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413682.1:169..1167"
                     /note="isoform 15 precursor is encoded by transcript
                     variant 18"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvsyih gssqaqfvae shiilvlnaa itmgmvllne
      301 aatskgdvgk rrsvvshvaa vvpliiinps lh
//
LOCUS       NP_001400242             275 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 15 [Homo sapiens].
ACCESSION   NP_001400242
VERSION     NP_001400242.1
DBSOURCE    REFSEQ: accession NM_001413313.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.122613.1,
                                           SRR14372080.3958765.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMN03267753
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..275
                     /product="RNA-binding Raly-like protein isoform 15"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=30046
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          183..>228
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     CDS             1..275
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413313.1:1175..2002"
                     /note="isoform 15 is encoded by transcript variant 40"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly rleskepfls
      121 vglfdyhgrv ppppravipl krprvavttt rrgkgvfsmk ggsrstasgs tgsklksdel
      181 qtikkeltqi ktkidsllgr lekiekqqka eaeaqkkqle eslvliqeec vseiadhste
      241 epaeggpdad geemtdgiee dfdedgghel flqik
//
LOCUS       NP_001402869             422 aa            linear   PRI 21-NOV-2025
DEFINITION  synaptotagmin-1 isoform 1 [Homo sapiens].
ACCESSION   NP_001402869
VERSION     NP_001402869.1
DBSOURCE    REFSEQ: accession NM_001415940.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Stephan,G., Haddock,S., Wang,S., Erdjument-Bromage,H., Liu,W.,
            Ravn-Boess,N., Frenster,J.D., Bready,D., Cai,J., Ronnen,R.,
            Sabio-Ortiz,J., Fenyo,D., Neubert,T.A. and Placantonakis,D.G.
  TITLE     Modulation of GPR133 (ADGRD1) signaling by its intracellular
            interaction partner extended synaptotagmin 1
  JOURNAL   Cell Rep 43 (5), 114229 (2024)
   PUBMED   38758649
  REMARK    GeneRIF: Modulation of GPR133 (ADGRD1) signaling by its
            intracellular interaction partner extended synaptotagmin 1.
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Zhang,J., Ren,G., Huang,T., Sang,Y., Zhong,Y. and Yi,Y.
  TITLE     miRNA-363-3p Hinders Proliferation, Migration, Invasion and
            Autophagy of Thyroid Cancer Cells by Controlling SYT1 Transcription
            to affect NF-kappaB
  JOURNAL   Endocr Metab Immune Disord Drug Targets 24 (1), 153-162 (2024)
   PUBMED   37150983
  REMARK    GeneRIF: miRNA-363-3p Hinders Proliferation, Migration, Invasion
            and Autophagy of Thyroid Cancer Cells by Controlling SYT1
            Transcription to affect NF-kappaB.
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Yamada,K., Motohashi,S., Oikawa,T., Tago,N., Koizumi,R., Ono,M.,
            Tachibana,T., Yoshida,A., Yoshida,S., Shimoda,M., Oka,M., Yoneda,Y.
            and Yoshida,K.
  TITLE     Extended-synaptotagmin 1 engages in unconventional protein
            secretion mediated via SEC22B+ vesicle pathway in liver cancer
  JOURNAL   Proc Natl Acad Sci U S A 119 (36), e2202730119 (2022)
   PUBMED   36044553
  REMARK    GeneRIF: Extended-synaptotagmin 1 engages in unconventional protein
            secretion mediated via SEC22B(+) vesicle pathway in liver cancer.
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Thibord,F., Chan,M.V., Chen,M.H. and Johnson,A.D.
  TITLE     A year of COVID-19 GWAS results from the GRASP portal reveals
            potential genetic risk factors
  JOURNAL   HGG Adv 3 (2), 100095 (2022)
   PUBMED   35224516
REFERENCE   6  (residues 1 to 422)
  AUTHORS   McMahon,H.T., Missler,M., Li,C. and Sudhof,T.C.
  TITLE     Complexins: cytosolic proteins that regulate SNAP receptor function
  JOURNAL   Cell 83 (1), 111-119 (1995)
   PUBMED   7553862
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Chowdhury,D., Travis,G.H., Sutcliffe,J.G. and Burton,F.H.
  TITLE     Synaptotagmin I and 1B4 are identical: implications for
            synaptotagmin distribution in the primate brain
  JOURNAL   Neurosci Lett 190 (1), 9-12 (1995)
   PUBMED   7624059
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Mochly-Rosen,D., Miller,K.G., Scheller,R.H., Khaner,H., Lopez,J.
            and Smith,B.L.
  TITLE     p65 fragments, homologous to the C2 region of protein kinase C,
            bind to the intracellular receptors for protein kinase C
  JOURNAL   Biochemistry 31 (35), 8120-8124 (1992)
   PUBMED   1326322
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Perin,M.S., Johnston,P.A., Ozcelik,T., Jahn,R., Francke,U. and
            Sudhof,T.C.
  TITLE     Structural and functional conservation of synaptotagmin (p65) in
            Drosophila and humans
  JOURNAL   J Biol Chem 266 (1), 615-622 (1991)
   PUBMED   1840599
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Blaustein,R.O., Germann,W.J., Finkelstein,A. and DasGupta,B.R.
  TITLE     The N-terminal half of the heavy chain of botulinum type A
            neurotoxin forms channels in planar phospholipid bilayers
  JOURNAL   FEBS Lett 226 (1), 115-120 (1987)
   PUBMED   2446925
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073606.19, AC090709.6,
            AC073616.17, AC073572.19, AC078917.14 and AC027288.26.
            
            Summary: This gene encodes a member of the synaptotagmin protein
            family. The synaptotagmins are integral membrane proteins of
            synaptic vesicles that serve as calcium sensors in the process of
            vesicular trafficking and exocytosis. The encoded protein
            participates in triggering neurotransmitter release at the synapse
            in response to calcium binding. Mutations in this gene are
            associated with Baker-Gordon syndrome. [provided by RefSeq, Jan
            2023].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.10145.1,
                                           SRR1803611.50481.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968189,
                                           SAMEA1968968 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.2"
     Protein         1..422
                     /product="synaptotagmin-1 isoform 1"
                     /note="sytI; synaptotagmin I"
                     /calculated_mol_wt=47442
     Region          6..113
                     /region_name="Syt1_N"
                     /note="N-terminal domain of synaptotagmin-1 (Syt1) and
                     similar proteins; cd21963"
                     /db_xref="CDD:409248"
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            order(40,43..44,46..48,50..51)
                     /site_type="other"
                     /note="Botolinum neurotoxin B binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409248"
     Site            58..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Region          113..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Region          136..382
                     /region_name="Phospholipid binding. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Region          143..265
                     /region_name="C2A_Synaptotagmin-1-5-6-9-10"
                     /note="C2A domain first repeat present in Synaptotagmins
                     1, 5, 6, 9, and 10; cd08385"
                     /db_xref="CDD:176031"
     Site            order(173,179,231,233,239)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176031"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P46096; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46096; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Region          274..409
                     /region_name="C2B_Synaptotagmin-1"
                     /note="C2 domain second repeat present in Synaptotagmin 1;
                     cd08402"
                     /db_xref="CDD:176047"
     Site            order(304,310,364,366,372)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176047"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21707; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21707; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     CDS             1..422
                     /gene="SYT1"
                     /gene_synonym="BAGOS; P65; SVP65; SYT"
                     /coded_by="NM_001415940.1:642..1910"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="GeneID:6857"
                     /db_xref="HGNC:HGNC:11509"
                     /db_xref="MIM:185605"
ORIGIN      
        1 mvseshheal aappvttvat vlpsnatepa spgegkedaf sklkekfmne lhkiplppwa
       61 liaiaivavl lvltccfcic kkclfkkknk kkgkekggkn ainmkdvkdl gktmkdqalk
      121 dddaetgltd geekeepkee eklgklqysl dydfqnnqll vgiiqaaelp aldmggtsdp
      181 yvkvfllpdk kkkfetkvhr ktlnpvfneq ftfkvpysel ggktlvmavy dfdrfskhdi
      241 igefkvpmnt vdfghvteew rdlqsaekee qeklgdicfs lryvptagkl tvvileaknl
      301 kkmdvgglsd pyvkihlmqn gkrlkkkktt ikkntlnpyy nesfsfevpf eqiqkvqvvv
      361 tvldydkigk ndaigkvfvg ynstgaelrh wsdmlanprr piaqwhtlqv eeevdamlav
      421 kk
//
LOCUS       NP_001393551            1042 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 11 [Homo sapiens].
ACCESSION   NP_001393551
VERSION     NP_001393551.1
DBSOURCE    REFSEQ: accession NM_001406622.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1042)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1042)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1042)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1042)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1042)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1042)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1042)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4352443.839460.1,
                                           SRR18074969.1430239.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1042
                     /product="hamartin isoform 11"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=116074
     Region          16..597
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <586..>838
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1042
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406622.1:477..3605"
                     /note="isoform 11 is encoded by transcript variant 36"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mdtdvvvltt gvlvlitmlp mipqsgkqhl ldffdifgrl sswclkkpgh vaevylvhlh
       61 asvyalfhrl ygmypcnfvs flrshysmke nletfeevvk pmmehvrihp elvtgskdhe
      121 ldprrwkrle thdvviecak isldpteasy edgysvshqi sarfphrsad vttspyadtq
      181 nsygcatstp ystsrlmlln mpgqlpqtls spstrlitep pqatlwspsm vcgmttppts
      241 pgnvppdlsh pyskvfgttg gkgtplgtpa tspppaplch sddyvhislp qatvtpprke
      301 ermdsarpcl hrqhhllndr gseeppgskg svtlsdlpgf lgdlaseeds iekdkeeaai
      361 srelseitta eaepvvprgg fdspfyrdsl pgsqrkthsa asssqgasvn peplhssldk
      421 lgpdtpkqaf tpidlpcgsa despagdrec qtsletsift pspckipppt rvgfgsgqpp
      481 pydhlfeval pktahhfvir kteellkkak gnteedgvps tspmevldrl iqqgadahsk
      541 elnklplpsk svdwthfggs ppsdeirtlr dqllllhnql lyerfkrqqh alrnrrllrk
      601 vikaaaleeh naamkdqlkl qekdiqmwkv slqkeqaryn qlqeqrdtmv tklhsqirql
      661 qhdreefynq sqelqtkled crnmiaelri elkkannkvc htelllsqvs qklsnsesvq
      721 qqmeflnrql lvlgevnely leqlqnkhsd ttkevemmka ayrkeleknr shvlqqtqrl
      781 dtsqkrilel eshlakkdhl lleqkkyled vklqargqlq aaesryeaqk ritqvfelei
      841 ldlygrlekd gllkkleeek aeaaeaaeer ldccndgcsd smvghneeas ghngetktpr
      901 pssargssgs rggggsssss selstpekpp hqragpfssr wettmgeasa sipttvgslp
      961 ssksflgmka relfrnkses qcdedgmtss lseslktelg kdlgveakip lnldgphpsp
     1021 ptpdsvgqlh imdynethhe hs
//
LOCUS       NP_001427583             770 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 3 isoform 3 [Homo sapiens].
ACCESSION   NP_001427583 XP_005278338 XP_054177058 XP_054185661 XP_054186157
            XP_054186454 XP_054186705 XP_054186936 XP_054187218 XP_054187493
            XP_054189532 XP_054189634
VERSION     NP_001427583.1
DBSOURCE    REFSEQ: accession NM_001440654.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 770)
  AUTHORS   Ghashghaei,M., Liu,Y., Ettles,J., Bombaci,G., Ramkumar,N., Liu,Z.,
            Escano,L., Miko,S.S., Kim,Y., Waldron,J.A., Do,K., MacPherson,K.,
            Yuen,K.A., Taibi,T., Yue,M., Arsalan,A., Jin,Z., Edin,G.,
            Karsan,A., Morin,G.B., Kuchenbauer,F., Perna,F., Bushell,M. and
            Vu,L.P.
  TITLE     Translation efficiency driven by CNOT3 subunit of the CCR4-NOT
            complex promotes leukemogenesis
  JOURNAL   Nat Commun 15 (1), 2340 (2024)
   PUBMED   38491013
  REMARK    GeneRIF: Translation efficiency driven by CNOT3 subunit of the
            CCR4-NOT complex promotes leukemogenesis.
            Erratum:[Nat Commun. 2024 Oct 7;15(1):8674. doi:
            10.1038/s41467-024-53071-1. PMID: 39375334]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 770)
  AUTHORS   Burgess,H.M., Grande,R., Riccio,S., Dinesh,I., Winkler,G.S.,
            Depledge,D.P. and Mohr,I.
  TITLE     CCR4-NOT differentially controls host versus virus poly(a)-tail
            length and regulates HCMV infection
  JOURNAL   EMBO Rep 24 (12), e56327 (2023)
   PUBMED   37846490
  REMARK    GeneRIF: CCR4-NOT differentially controls host versus virus
            poly(a)-tail length and regulates HCMV infection.
REFERENCE   4  (residues 1 to 770)
  AUTHORS   Zhao,P., Meng,Q., Wan,C., Lei,T., Zhang,L., Zhang,X., Tan,L.,
            Zhu,H. and He,X.
  TITLE     Clinical features of CNOT3-associated neurodevelopmental disorder
            in three Chinese patients
  JOURNAL   Neurogenetics 24 (2), 129-136 (2023)
   PUBMED   36802310
  REMARK    GeneRIF: Clinical features of CNOT3-associated neurodevelopmental
            disorder in three Chinese patients.
REFERENCE   5  (residues 1 to 770)
  AUTHORS   McLenachan,S., Zhang,D., Grainok,J., Zhang,X., Huang,Z., Chen,S.C.,
            Zaw,K., Lima,A., Jennings,L., Roshandel,D., Moon,S.Y., Heath
            Jeffery,R.C., Attia,M.S., Thompson,J.A., Lamey,T.M., McLaren,T.L.,
            De Roach,J., Fletcher,S. and Chen,F.K.
  TITLE     Determinants of Disease Penetrance in PRPF31-Associated Retinopathy
  JOURNAL   Genes (Basel) 12 (10), 1542 (2021)
   PUBMED   34680937
  REMARK    GeneRIF: Determinants of Disease Penetrance in PRPF31-Associated
            Retinopathy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 770)
  AUTHORS   Yin,X., Warner,D.R., Roberts,E.A., Pisano,M.M. and Greene,R.M.
  TITLE     Identification of novel CBP interacting proteins in embryonic
            orofacial tissue
  JOURNAL   Biochem Biophys Res Commun 329 (3), 1010-1017 (2005)
   PUBMED   15752756
REFERENCE   7  (residues 1 to 770)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 770)
  AUTHORS   Aoki,T., Okada,N., Wakamatsu,T. and Tamura,T.A.
  TITLE     TBP-interacting protein 120B, which is induced in relation to
            myogenesis, binds to NOT3
  JOURNAL   Biochem Biophys Res Commun 296 (5), 1097-1103 (2002)
   PUBMED   12207886
  REMARK    GeneRIF: TBP-interacting protein 120B binds to NOT3
REFERENCE   9  (residues 1 to 770)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
REFERENCE   10 (residues 1 to 770)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC245052.3.
            
            On or before May 23, 2025 this sequence version replaced
            XP_054186157.1, XP_054189634.1, XP_054189532.1, XP_054187218.1,
            XP_054186454.1, XP_054187493.1, XP_005278338.1, XP_054185661.1,
            XP_054186705.1, XP_054186936.1, XP_054177058.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2147686.1,
                                           SRR14038192.1447391.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..770
                     /product="CCR4-NOT transcription complex subunit 3 isoform
                     3"
                     /note="NOT3 (negative regulator of transcription 3, yeast)
                     homolog; CCR4-associated factor 3; leukocyte receptor
                     cluster member 2"
                     /calculated_mol_wt=83555
     Region          3..229
                     /region_name="Not3"
                     /note="Not1 N-terminal domain, CCR4-Not complex component;
                     pfam04065"
                     /db_xref="CDD:461155"
     Region          <288..659
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          620..762
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..770
                     /gene="CNOT3"
                     /gene_synonym="IDDSADF; LENG2; NOT3; NOT3H"
                     /coded_by="NM_001440654.1:283..2595"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:4849"
                     /db_xref="HGNC:HGNC:7879"
                     /db_xref="MIM:604910"
ORIGIN      
        1 madkrklqge idrclkkvse gveqfediwq klhnaananq kekyeadlkk eikklqrlrd
       61 qiktwvasne ikdkrqlidn rklietqmer fkvveretkt kayskeglgl aqkvdpaqke
      121 keevgqwltn tidtlnmqvd qfesevesls vqtrkkkgdk dkqdrieglk rhiekhryhv
      181 rmletilrml dndsilvdai rkikddveyy vdssqdpdfe eneflyddld ledipqalva
      241 tsppshshme deifnqssst ptsttssspi ppspanctte nseddkkrgr stdsevsqsp
      301 akngskpvhs nqhpqspavp ptypsgpppa asalsttpgn ngvpapaapp salgpkaspa
      361 pshnsgtpap yaqavappap sgpsttqprp psvqpsgggg ggsggggsss ssnssaggga
      421 gkqngatsys svvadspaev alsssggnna ssqalgppsg phnpppstsk epsaaaptga
      481 ggvapgsgnn sggpsllvpl pvnppssptp sfsdakaaga llngppqfst apeikapepl
      541 sslksmaera aissgiedpv ptlhlterdi ilsstsappa saqpplqlse vniplslgvc
      601 plgpvpltke qlyqqameea awhhmphpsd serirqylpr npcptppyhh qmppphsdtv
      661 efyqrlstet lffifyyleg tkaqylaaka lkkqswrfht kymmwfqrhe epktitdefe
      721 qipdhllvhs ltafspgqgt yiyfdyekwg qrkkegftfe yryledrdlq
//
LOCUS       NP_001394759            1155 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 15 precursor
            [Homo sapiens].
ACCESSION   NP_001394759
VERSION     NP_001394759.1
DBSOURCE    REFSEQ: accession NM_001407830.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1155)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1155)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1155)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1155)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1155)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1155)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1155)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1155)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1155)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1155)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1547162.1,
                                           SRR14038196.3516634.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1155
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1155
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 15 precursor"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=125822
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O00411.2)"
                     /calculated_mol_wt=4109
     Region          18..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          95..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          261..290
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          296..323
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          432..629
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          756..1155
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1155
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407830.1:26..3493"
                     /note="isoform 15 precursor is encoded by transcript
                     variant 15"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 msalcwgrga aglkralrpc grpglpgkeg taggvcgprr sssaspqeqd qdrrkdwghv
       61 ellevlqarv rqlqaesvse vvvnrvdvar lpecgsgdgs lqpprkvqmg akdatpvpcg
      121 rwakilekdk rtqqmrmqrl kaklqmpfqs gefkaltrrl qveprllskq magcledctr
      181 qapespweeq larllqeapg klsldveqap sgqhsqaqls gqqqrllaff kcclltdqlp
      241 lahhllvvhh gqrqkrkllt ldmynavmlg warqgafkel vyvlfmvkda gltpdllsya
      301 aalqcmgrqd qdagtiercl eqmsqeglkl qalftavlls eedratvlka vhkvkptfsl
      361 ppqlpppvnt skllrdvyak dgrvsypklh lplktlqclf ekqlhmelas rvcvvsvekp
      421 tlpskevkha rktlktlrdq wekalcralr etknrlerev yegrfslypf lcllderevv
      481 rmllqvlqal paqgesfttl arelsartfs rhvvqrqrvs gqvqalqnhy rkylcllasd
      541 aeigilkphp ayvqllekaa eptltfeavd vpmlcpplpw tsphsgafll sptklmrtve
      601 gatqhqelle tcpptalhga ldaltqlgnc awrvngrvld lvlqlfqakg cpqlgvpapp
      661 seapqppeah lphsaapark aelrrelahc qkvaremhsl raealyrlsl aqhlrdrvfw
      721 lphnmdfrgr typcpphfnh lgsdvarall efaqgrplgp hgldwlkihl vnltglkkre
      781 plrkrlafae evmddildsa dqpltgrkww mgaeepwqtl accmevanav rasdpaayvs
      841 hlpvhqdgsc nglqhyaalg rdsvgaasvn lepsdvpqdv ysgvaaqvev frrqdaqrgm
      901 rvaqvlegfi trkvvkqtvm tvvygvtryg grlqiekrlr elsdfpqefv weashylvrq
      961 vfkslqemfs gtraiqhwlt esarlishmg svvewvtplg vpviqpyrld skvkqigggi
     1021 qsitythngd isrkpntrkq kngfppnfih sldsshmmlt alhcyrkglt fvsvhdcywt
     1081 haadvsvmnq vcreqfvrlh sepilqdlsr flvkrfcsep qkileasqlk etlqavpkpg
     1141 afdleqvkrs tyffs
//
LOCUS       NP_001397827             173 aa            linear   PRI 21-NOV-2025
DEFINITION  BTB/POZ domain-containing adapter for CUL3-mediated RhoA
            degradation protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001397827 XP_016878595
VERSION     NP_001397827.1
DBSOURCE    REFSEQ: accession NM_001410898.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Seth,A., Rivera,A., Chahdi,A., Choi,I.S., Medina-Martinez,O.,
            Lewis,S., O'Neill,M., Ridgeway,A., Moore,J., Jorgez,C. and
            Lamb,D.J.
  TITLE     Gene dosage changes in KCTD13 result in penile and testicular
            anomalies via diminished androgen receptor function
  JOURNAL   FASEB J 36 (11), e22567 (2022)
   PUBMED   36196997
  REMARK    GeneRIF: Gene dosage changes in KCTD13 result in penile and
            testicular anomalies via diminished androgen receptor function.
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 173)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 173)
  AUTHORS   Tomaru,T., Satoh,T., Yoshino,S., Ishizuka,T., Hashimoto,K.,
            Monden,T., Yamada,M. and Mori,M.
  TITLE     Isolation and characterization of a transcriptional cofactor and
            its novel isoform that bind the deoxyribonucleic acid-binding
            domain of peroxisome proliferator-activated receptor-gamma
  JOURNAL   Endocrinology 147 (1), 377-388 (2006)
   PUBMED   16239304
  REMARK    GeneRIF: PDIP1 mRNA was expressed in 3T3-L1 adipocytes and THP-1
            macrophages
REFERENCE   7  (residues 1 to 173)
  AUTHORS   Zhou,J., Hu,X., Xiong,X., Liu,X., Liu,Y., Ren,K., Jiang,T., Hu,X.
            and Zhang,J.
  TITLE     Cloning of two rat PDIP1 related genes and their interactions with
            proliferating cell nuclear antigen
  JOURNAL   J Exp Zool A Comp Exp Biol 303 (3), 227-240 (2005)
   PUBMED   15726626
REFERENCE   8  (residues 1 to 173)
  AUTHORS   Wan,D., Gong,Y., Qin,W., Zhang,P., Li,J., Wei,L., Zhou,X., Li,H.,
            Qiu,X., Zhong,F., He,L., Yu,J., Yao,G., Jiang,H., Qian,L., Yu,Y.,
            Shu,H., Chen,X., Xu,H., Guo,M., Pan,Z., Chen,Y., Ge,C., Yang,S. and
            Gu,J.
  TITLE     Large-scale cDNA transfection screening for genes related to cancer
            development and progression
  JOURNAL   Proc Natl Acad Sci U S A 101 (44), 15724-15729 (2004)
   PUBMED   15498874
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 Dec 14:101(50):17565]
REFERENCE   9  (residues 1 to 173)
  AUTHORS   Kutsenko,A.S., Gizatullin,R.Z., Al-Amin,A.N., Wang,F., Kvasha,S.M.,
            Podowski,R.M., Matushkin,Y.G., Gyanchandani,A., Muravenko,O.V.,
            Levitsky,V.G., Kolchanov,N.A., Protopopov,A.I., Kashuba,V.I.,
            Kisselev,L.L., Wasserman,W., Wahlestedt,C. and Zabarovsky,E.R.
  TITLE     NotI flanking sequences: a tool for gene discovery and verification
            of the human genome
  JOURNAL   Nucleic Acids Res 30 (14), 3163-3170 (2002)
   PUBMED   12136098
REFERENCE   10 (residues 1 to 173)
  AUTHORS   He,H., Tan,C.K., Downey,K.M. and So,A.G.
  TITLE     A tumor necrosis factor alpha- and interleukin 6-inducible protein
            that interacts with the small subunit of DNA polymerase delta and
            proliferating cell nuclear antigen
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11979-11984 (2001)
   PUBMED   11593007
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC120114.2 and KF459558.1.
            
            On Aug 17, 2022 this sequence version replaced XP_016878595.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.457322.1,
                                           SRR14372080.3423576.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..173
                     /product="BTB/POZ domain-containing adapter for
                     CUL3-mediated RhoA degradation protein 1 isoform 2"
                     /note="BTB/POZ domain-containing protein KCTD13;
                     polymerase delta-interacting protein 1; BTB/POZ
                     domain-containing adapter for CUL3-mediated RhoA
                     degradation protein 1; TNFAIP1-like protein; potassium
                     channel tetramerisation domain containing 13;
                     CTD-2574D22.4"
                     /calculated_mol_wt=18281
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WZ19.1)"
     Region          40..138
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     CDS             1..173
                     /gene="KCTD13"
                     /gene_synonym="BACURD1; FKSG86; hBACURD1; PDIP1; POLDIP1"
                     /coded_by="NM_001410898.1:194..715"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92133.1"
                     /db_xref="GeneID:253980"
                     /db_xref="HGNC:HGNC:22234"
                     /db_xref="MIM:608947"
ORIGIN      
        1 msaeasgpaa aaapsleapk psglepgpaa yglkpltpns kyvklnvggs lhyttlrtlt
       61 gqdtmlkamf sgrvevltda ggwvlidrsg rhfgtilnyl rdgsvplpes trelgellge
      121 aryylvqgli edcqlalqsl svaqagvqwr dlgspqplpp rfkqfsclsl pss
//
LOCUS       NP_001427342             321 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 7 precursor [Homo
            sapiens].
ACCESSION   NP_001427342
VERSION     NP_001427342.1
DBSOURCE    REFSEQ: accession NM_001440413.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 321)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3 and AP004147.3.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803613.173970.1, SRR1660809.214206.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..321
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     7 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=33613
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..>302
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            286
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     CDS             1..321
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440413.1:708..1673"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 15"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk aaelgmvsay
      241 ytyiftnlef slqrmdslvd drvnilgfsi fnqshaffqe faqslnqswq encdhvpftg
      301 pagilvtvks ghvalldkwg n
//
LOCUS       NP_001427569             207 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol N-acetylglucosaminyltransferase subunit H
            isoform 3 [Homo sapiens].
ACCESSION   NP_001427569 XP_011535140 XP_054232198
VERSION     NP_001427569.1
DBSOURCE    REFSEQ: accession NM_001440640.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Wegner,J., Zillinger,T., Schlee-Guimaraes,T.M., Bartok,E. and
            Schlee,M.
  TITLE     An epigenetic GPI anchor defect impairs TLR4 signaling in the B
            cell transdifferentiation model for primary human monocytes BLaER1
  JOURNAL   Sci Rep 11 (1), 14983 (2021)
   PUBMED   34294787
  REMARK    GeneRIF: An epigenetic GPI anchor defect impairs TLR4 signaling in
            the B cell transdifferentiation model for primary human monocytes
            BLaER1.
            Erratum:[Sci Rep. 2021 Aug 30;11(1):17661. doi:
            10.1038/s41598-021-97277-5. PMID: 34462520]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Tremblay-Laganiere,C., Kaiyrzhanov,R., Maroofian,R., Nguyen,T.T.M.,
            Salayev,K., Chilton,I.T., Chung,W.K., Madden,J.A., Phornphutkul,C.,
            Agrawal,P.B., Houlden,H. and Campeau,P.M.
  TITLE     PIGH deficiency can be associated with severe neurodevelopmental
            and skeletal manifestations
  JOURNAL   Clin Genet 99 (2), 313-317 (2021)
   PUBMED   33156547
  REMARK    GeneRIF: PIGH deficiency can be associated with severe
            neurodevelopmental and skeletal manifestations.
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Loeff,F.C., Rijs,K., van Egmond,E.H.M., Zoutman,W.H., Qiao,X.,
            Kroes,W.G.M., Veld,S.A.J., Griffioen,M., Vermeer,M.H., Neefjes,J.,
            Frederik Falkenburg,J.H., Halkes,C.J.M. and Jedema,I.
  TITLE     Loss of the GPI-anchor in B-lymphoblastic leukemia by epigenetic
            downregulation of PIGH expression
  JOURNAL   Am J Hematol 94 (1), 93-102 (2019)
   PUBMED   30370942
  REMARK    GeneRIF: The GPI-anchor negative phenotype results from loss of
            mRNA expression of the PIGH gene, which is involved in the first
            step of GPI-anchor synthesis. Loss of PIGH mRNA expression within
            these B-ALL cells follows epigenetic silencing rather than gene
            mutation or deletion.
REFERENCE   6  (residues 1 to 207)
  AUTHORS   Watanabe,R., Murakami,Y., Marmor,M.D., Inoue,N., Maeda,Y., Hino,J.,
            Kangawa,K., Julius,M. and Kinoshita,T.
  TITLE     Initial enzyme for glycosylphosphatidylinositol biosynthesis
            requires PIG-P and is regulated by DPM2
  JOURNAL   EMBO J 19 (16), 4402-4411 (2000)
   PUBMED   10944123
REFERENCE   7  (residues 1 to 207)
  AUTHORS   Watanabe,R., Inoue,N., Westfall,B., Taron,C.H., Orlean,P.,
            Takeda,J. and Kinoshita,T.
  TITLE     The first step of glycosylphosphatidylinositol biosynthesis is
            mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1
  JOURNAL   EMBO J 17 (4), 877-885 (1998)
   PUBMED   9463366
REFERENCE   8  (residues 1 to 207)
  AUTHORS   Watanabe,R., Kinoshita,T., Masaki,R., Yamamoto,A., Takeda,J. and
            Inoue,N.
  TITLE     PIG-A and PIG-H, which participate in glycosylphosphatidylinositol
            anchor biosynthesis, form a protein complex in the endoplasmic
            reticulum
  JOURNAL   J Biol Chem 271 (43), 26868-26875 (1996)
   PUBMED   8900170
REFERENCE   9  (residues 1 to 207)
  AUTHORS   Ware,R.E., Howard,T.A., Kamitani,T., Chang,H.-M., Yeh,E.T.H. and
            Seldin,M.F.
  TITLE     Chromosomal assignment of genes involved in
            glycosylphosphatidylinositol anchor biosynthesis: implications for
            the pathogenesis of paroxysmal nocturnal hemoglobinuria
  JOURNAL   Blood 83 (12), 3753-3757 (1994)
   PUBMED   8204896
REFERENCE   10 (residues 1 to 207)
  AUTHORS   Kamitani,T., Chang,H.M., Rollins,C., Waneck,G.L. and Yeh,E.T.
  TITLE     Correction of the class H defect in glycosylphosphatidylinositol
            anchor biosynthesis in Ltk- cells by a human cDNA clone
  JOURNAL   J Biol Chem 268 (28), 20733-20736 (1993)
   PUBMED   8407896
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL132640.4.
            
            On or before May 23, 2025 this sequence version replaced
            XP_011535140.1, XP_054232198.1.
            
            Summary: This gene encodes an endoplasmic reticulum associated
            protein that is involved in glycosylphosphatidylinositol
            (GPI)-anchor biosynthesis. The GPI anchor is a glycolipid found on
            many blood cells and which serves to anchor proteins to the cell
            surface. The protein encoded by this gene is a subunit of the GPI
            N-acetylglucosaminyl (GlcNAc) transferase that transfers GlcNAc to
            phosphatidylinositol (PI) on the cytoplasmic side of the
            endoplasmic reticulum. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2611395.1,
                                           SRR14038192.4124296.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.1"
     Protein         1..207
                     /product="phosphatidylinositol
                     N-acetylglucosaminyltransferase subunit H isoform 3"
                     /EC_number="2.4.1.198"
                     /note="phosphatidylinositol
                     N-acetylglucosaminyltransferase subunit H;
                     phosphatidylinositol-glycan biosynthesis, class H protein"
                     /calculated_mol_wt=23217
     Region          89..158
                     /region_name="PIG-H"
                     /note="GPI-GlcNAc transferase complex, PIG-H component;
                     pfam10181"
                     /db_xref="CDD:462983"
     CDS             1..207
                     /gene="PIGH"
                     /gene_synonym="GPI-H"
                     /coded_by="NM_001440640.1:66..689"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:5283"
                     /db_xref="HGNC:HGNC:8964"
                     /db_xref="MIM:600154"
ORIGIN      
        1 medersfsdi cggrlalqrr yyspscrefc lscprlslrs ltavtctvwl aayglftlce
       61 nsmilsaaif itllgllgyl hfvkidqetl liidslgiqm tssyasgkes ttfiemgkvk
      121 divineaiym qkviyylcil lkdpvephgi sqvvpvfqrq sltlsprlec sdnhhslqpp
      181 pprlkksscl sllrtwdyrv pspgwta
//
LOCUS       NP_001393559             813 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 16 [Homo sapiens].
ACCESSION   NP_001393559
VERSION     NP_001393559.1
DBSOURCE    REFSEQ: accession NM_001406630.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 813)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 813)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 813)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 813)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 813)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 813)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 813)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 813)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1806632.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..813
                     /product="hamartin isoform 16"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=90122
     Region          <1..368
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <357..>609
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..813
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406630.1:1311..3752"
                     /note="isoform 16 is encoded by transcript variant 44"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mvcgmttppt spgnvppdls hpyskvfgtt ggkgtplgtp atspppaplc hsddyvhisl
       61 pqatvtpprk eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed
      121 siekdkeeaa isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv
      181 npeplhssld klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp
      241 trvgfgsgqp ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr
      301 liqqgadahs kelnklplps ksvdwthfgg sppsdeirtl rdqllllhnq llyerfkrqq
      361 halrnrrllr kvikaaalee hnaamkdqlk lqekdiqmwk vslqkeqary nqlqeqrdtm
      421 vtklhsqirq lqhdreefyn qsqelqtkle dcrnmiaelr ielkkannkv chtelllsqv
      481 sqklsnsesv qqqmeflnrq llvlgevnel yleqlqnkhs dttkevemmk aayrkelekn
      541 rshvlqqtqr ldtsqkrile leshlakkdh llleqkkyle dvklqargql qaaesryeaq
      601 kritqvfele ildlygrlek dgllkkleee kaeaaeaaee rldccndgcs dsmvghneea
      661 sghngetktp rpssargssg srggggssss sselstpekp phqragpfss rwettmgeas
      721 asipttvgsl pssksflgmk arelfrnkse sqcdedgmts slseslktel gkdlgveaki
      781 plnldgphps pptpdsvgql himdynethh ehs
//
LOCUS       NP_001276328             276 aa            linear   PRI 21-NOV-2025
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily A member 2 isoform e precursor [Homo sapiens].
ACCESSION   NP_001276328
VERSION     NP_001276328.1
DBSOURCE    REFSEQ: accession NM_001289399.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Zhang,Z., Li,Q., Sun,S., Li,Z., Cui,Z., Liu,Q., Zhang,Y., Xiong,S.
            and Zhang,S.
  TITLE     Expression of SMARCA2 and SMARCA4 in gastric adenocarcinoma and
            construction of a nomogram prognostic model
  JOURNAL   Int J Clin Oncol 28 (11), 1487-1500 (2023)
   PUBMED   37634210
  REMARK    GeneRIF: Expression of SMARCA2 and SMARCA4 in gastric
            adenocarcinoma and construction of a nomogram prognostic model.
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Zhang,Z., Li,Q., Sun,S., Li,Z., Cui,Z.G., Zhang,M., Liu,Q.,
            Zhang,Y., Xiong,S. and Zhang,S.
  TITLE     Clinicopathological and prognostic significance of SWI/SNF complex
            subunits in undifferentiated gastric carcinoma
  JOURNAL   World J Surg Oncol 20 (1), 383 (2022)
   PUBMED   36464671
  REMARK    GeneRIF: Clinicopathological and prognostic significance of SWI/SNF
            complex subunits in undifferentiated gastric carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Zhang,X., Chen,H., Song,Y., Chen,Z., Liu,X., Rong,P. and Ma,R.
  TITLE     Ten-year follow-up of Nicolaides-Baraitser syndrome with a de novo
            mutation and analysis of 58 gene loci of SMARCA2-associated NCBRS
  JOURNAL   Mol Genet Genomic Med 10 (9), e2009 (2022)
   PUBMED   35811451
  REMARK    GeneRIF: Ten-year follow-up of Nicolaides-Baraitser syndrome with a
            de novo mutation and analysis of 58 gene loci of SMARCA2-associated
            NCBRS.
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Aves,S.J., Hindley,J., Phear,G.A. and Tongue,N.
  TITLE     A fission yeast gene mapping close to suc1 encodes a protein
            containing two bromodomains
  JOURNAL   Mol Gen Genet 248 (4), 491-498 (1995)
   PUBMED   7565614
REFERENCE   7  (residues 1 to 276)
  AUTHORS   Chiba,H., Muramatsu,M., Nomoto,A. and Kato,H.
  TITLE     Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and
            Drosophila brahma are transcriptional coactivators cooperating with
            the estrogen receptor and the retinoic acid receptor
  JOURNAL   Nucleic Acids Res 22 (10), 1815-1820 (1994)
   PUBMED   8208605
REFERENCE   8  (residues 1 to 276)
  AUTHORS   Muchardt,C., Yaniv,M. and Mattei,M.G.
  TITLE     Assignment of HBRM, the human homolog of S. cerevisiae SNF2/SWI2
            and Drosophila brm genes, to chromosome region 9p23-p24, by in situ
            hybridization
  JOURNAL   Mamm Genome 5 (4), 241-243 (1994)
   PUBMED   8012116
REFERENCE   9  (residues 1 to 276)
  AUTHORS   Muchardt,C. and Yaniv,M.
  TITLE     A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and
            Drosophila brm genes potentiates transcriptional activation by the
            glucocorticoid receptor
  JOURNAL   EMBO J 12 (11), 4279-4290 (1993)
   PUBMED   8223438
REFERENCE   10 (residues 1 to 276)
  AUTHORS   Abdul-Rahman,O. and May,F.
  TITLE     SMARCA2-Related Nicolaides-Baraitser Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26468571
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138755.13.
            
            Summary: The protein encoded by this gene is a member of the
            SWI/SNF family of proteins and is highly similar to the brahma
            protein of Drosophila. Members of this family have helicase and
            ATPase activities and are thought to regulate transcription of
            certain genes by altering the chromatin structure around those
            genes. The encoded protein is part of the large ATP-dependent
            chromatin remodeling complex SNF/SWI, which is required for
            transcriptional activation of genes normally repressed by
            chromatin. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene, which contains a
            trinucleotide repeat (CAG) length polymorphism. [provided by
            RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK298045.1, SRR1803614.188633.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.3"
     Protein         1..276
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily A member
                     2 isoform e precursor"
                     /note="global transcription activator homologous sequence;
                     SNF2-alpha; sucrose nonfermenting 2-like protein 2;
                     SNF2/SWI2-like protein 2; SWI/SNF-related
                     matrix-associated actin-dependent regulator of chromatin
                     a2; brahma homolog; probable global transcription
                     activator SNF2L2; BAF190B; protein brahma homolog;
                     BRG1-associated factor 190B; ATP-dependent helicase
                     SMARCA2; putative global transcription activator SNF2L2;
                     SWI/SNF related, matrix associated, actin dependent
                     regulator of chromatin, subfamily a, member 2"
                     /calculated_mol_wt=29379
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2374
     Region          37..>99
                     /region_name="Bromodomain"
                     /note="Bromodomains are found in many chromatin-associated
                     proteins and in nuclear histone acetyltransferases. They
                     interact specifically with acetylated lysine; cl02556"
                     /db_xref="CDD:445827"
     Region          86..192
                     /region_name="Bromo_SNF2L2"
                     /note="Bromodomain, SNF2L2-like subfamily, specific to
                     animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related
                     matrix-associated actin-dependent regulator of chromatin
                     subfamily A member 2 is a global transcriptional
                     activator, which cooperates with nuclear hormone...;
                     cd05516"
                     /db_xref="CDD:99947"
     Site            order(117,122,125,164,168,174)
                     /site_type="active"
                     /note="acetyllysine binding site [active]"
                     /db_xref="CDD:99947"
     CDS             1..276
                     /gene="SMARCA2"
                     /gene_synonym="BAF190; BIS; BRM; hBRM; hSNF2a; NCBRS;
                     SAMRCA2; SNF2; SNF2L2; SNF2LA; Sth1p; SWI2"
                     /coded_by="NM_001289399.2:94..924"
                     /note="isoform e precursor is encoded by transcript
                     variant 6"
                     /db_xref="CCDS:CCDS83339.1"
                     /db_xref="GeneID:6595"
                     /db_xref="HGNC:HGNC:11098"
                     /db_xref="MIM:600014"
ORIGIN      
        1 mkrlaarcfa gllilspltv isdsrpadsg kaiedgnlee meeevrlkkr krrrnvdkdp
       61 akedvekakk rrgrppaekl spnppkltkq mnaiidtvin ykdssgrqls evfiqlpsrk
      121 elpeyyelir kpvdfkkike rirnhkyrsl gdlekdvmll chnaqtfnle gsqiyedsiv
      181 lqsvfksarq kiakeeesed esneeeeeed eeeseseaks vkvkiklnkk ddkgrdkgkg
      241 kkrpnrgkak pvvsdfdsde eqdereqseg sgtdde
//
LOCUS       NP_001424279            2329 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HECTD1 isoform 5 [Homo sapiens].
ACCESSION   NP_001424279 XP_016876641 XP_054231760
VERSION     NP_001424279.1
DBSOURCE    REFSEQ: accession NM_001437350.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2329)
  AUTHORS   Oxman,E., Li,H., Wang,H.Y. and Zohn,I.E.
  TITLE     Identification and functional analysis of rare HECTD1 missense
            variants in human neural tube defects
  JOURNAL   Hum Genet 143 (3), 263-277 (2024)
   PUBMED   38451291
  REMARK    GeneRIF: Identification and functional analysis of rare HECTD1
            missense variants in human neural tube defects.
REFERENCE   2  (residues 1 to 2329)
  AUTHORS   Zhang,J., Xin,Y., Ling,X., Liang,H., Zhang,L., Fang,C. and Ma,J.
  TITLE     Nucleoporin 93, a new substrate of the E3 ubiquitin protein ligase
            HECTD1, promotes esophageal squamous cell carcinoma progression
  JOURNAL   Hum Cell 37 (1), 245-257 (2024)
   PUBMED   37993750
  REMARK    GeneRIF: Nucleoporin 93, a new substrate of the E3 ubiquitin
            protein ligase HECTD1, promotes esophageal squamous cell carcinoma
            progression.
REFERENCE   3  (residues 1 to 2329)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 2329)
  AUTHORS   Vaughan,N., Scholz,N., Lindon,C. and Licchesi,J.D.F.
  TITLE     The E3 ubiquitin ligase HECTD1 contributes to cell proliferation
            through an effect on mitosis
  JOURNAL   Sci Rep 12 (1), 13160 (2022)
   PUBMED   35915203
  REMARK    GeneRIF: The E3 ubiquitin ligase HECTD1 contributes to cell
            proliferation through an effect on mitosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2329)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 2329)
  AUTHORS   Aleidi,S.M., Yang,A., Sharpe,L.J., Rao,G., Cochran,B.J., Rye,K.A.,
            Kockx,M., Brown,A.J. and Gelissen,I.C.
  TITLE     The E3 ubiquitin ligase, HECTD1, is involved in ABCA1-mediated
            cholesterol export from macrophages
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1863 (4), 359-368 (2018)
   PUBMED   29306077
  REMARK    GeneRIF: HECTD1 may be involved in the regulation of ABCA1-mediated
            cholesterol export from unloaded macrophages to apoA-I.
REFERENCE   7  (residues 1 to 2329)
  AUTHORS   Fang,S., Guo,H., Cheng,Y., Zhou,Z., Zhang,W., Han,B., Luo,W.,
            Wang,J., Xie,W. and Chao,J.
  TITLE     circHECTD1 promotes the silica-induced pulmonary
            endothelial-mesenchymal transition via HECTD1
  JOURNAL   Cell Death Dis 9 (3), 396 (2018)
   PUBMED   29540674
  REMARK    GeneRIF: SiO2 concomitantly increased circHECTD1 expression, which,
            in turn, inhibited HECTD1 protein expression.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 2329)
  AUTHORS   Shen,X., Jia,Z., D'Alonzo,D., Wang,X., Bruder,E., Emch,F.H., De
            Geyter,C. and Zhang,H.
  TITLE     HECTD1 controls the protein level of IQGAP1 to regulate the
            dynamics of adhesive structures
  JOURNAL   Cell Commun Signal 15 (1), 2 (2017)
   PUBMED   28073378
  REMARK    GeneRIF: Hectd1 regulates the protein level of IQGAP1 through
            ubiquitination.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 2329)
  AUTHORS   Helander,S., Montecchio,M., Lemak,A., Fares,C., Almlof,J., Yi,Y.,
            Yee,A., Arrowsmith,C., DhePaganon,S. and Sunnerhagen,M.
  TITLE     Basic Tilted Helix Bundle - a new protein fold in human
            FKBP25/FKBP3 and HectD1
  JOURNAL   Biochem Biophys Res Commun 447 (1), 26-31 (2014)
   PUBMED   24667607
  REMARK    GeneRIF: our high-resolution structures show a new fold composed of
            five small helices where H3 and H4 are tilted in a novel
            arrangement; we call this fold the Basic Tilted Helix Bundle (BTHB)
            domain.
REFERENCE   10 (residues 1 to 2329)
  AUTHORS   Tran,H., Bustos,D., Yeh,R., Rubinfeld,B., Lam,C., Shriver,S.,
            Zilberleyb,I., Lee,M.W., Phu,L., Sarkar,A.A., Zohn,I.E.,
            Wertz,I.E., Kirkpatrick,D.S. and Polakis,P.
  TITLE     HectD1 E3 ligase modifies adenomatous polyposis coli (APC) with
            polyubiquitin to promote the APC-axin interaction
  JOURNAL   J Biol Chem 288 (6), 3753-3767 (2013)
   PUBMED   23277359
  REMARK    GeneRIF: HectD1 promotes the APC-Axin interaction to negatively
            regulate Wnt signaling.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136418.4, AL121808.4 and KC877516.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_016876641.1, XP_054231760.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.902116.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2329
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..2329
                     /product="E3 ubiquitin-protein ligase HECTD1 isoform 5"
                     /EC_number="2.3.2.26"
                     /note="E3 ubiquitin-protein ligase HECTD1; E3 ligase for
                     inhibin receptor; HECT domain-containing protein 1; HECT
                     domain containing E3 ubiquitin protein ligase 1; HECT-type
                     E3 ubiquitin transferase HECTD1"
                     /calculated_mol_wt=260458
     Region          <366..>479
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          366..393
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          396..426
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(397,401..402,405..407,409..410,414,417,426,428,
                     432..433,436..438,440..441,445,448,457,459,461,465..466,
                     469..471,473..474,478)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          428..457
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1107..1240
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     Region          1277..>1302
                     /region_name="MIB_HERC2"
                     /note="Mib_herc2; pfam06701"
                     /db_xref="CDD:461991"
     Region          1612..1677
                     /region_name="BTHB_HectD1"
                     /note="basic tilted helix bundle (BTHB) domain found in
                     HECT domain-containing protein 1 (HectD1) and similar
                     proteins; cd21062"
                     /db_xref="CDD:439138"
     Region          1850..2327
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(1856,1885,1895,1982,2260,2292..2293,2296..2300,2320,
                     2326)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(2075,2078..2079,2081..2082,2085,2127,2129,
                     2133..2134,2136,2142,2147,2164,2168)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..2329
                     /gene="HECTD1"
                     /gene_synonym="EULIR"
                     /coded_by="NM_001437350.1:800..7789"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:25831"
                     /db_xref="HGNC:HGNC:20157"
                     /db_xref="MIM:618649"
ORIGIN      
        1 madvdpdtll ewlqmgqgde rdmqlialeq lcmlllmsdn vdrcfetcpp rtflpalcki
       61 fldesapdnv levtaraity yldvsaectr rivgvdgaik alcnrlvvve lnnrtsrdla
      121 eqcvkvleli ctresgavfe agglncvltf irdsghlvhk dtlhsamavv srlcgkmepq
      181 dssleicves lssllkhedh qvsdgalrcf asladrftrr gvdpaplakh glteellsrm
      241 aaaggtvsgp ssackpgrst tgapsttads klsnqvstiv sllstlcrgs pvvthdllrs
      301 elpdsiesal qgdercvldt mrlvdlllvl lfegrkalpk ssagstgrip glrrldssge
      361 rshrqlidci rskdtdalid aidtgafevn fmddvgqtll nwasafgtqe mveflcerga
      421 dvnrgqrsss lhyaacfgrp qvaktllrhg anpdlrdedg ktpldkarer ghsevvailq
      481 spgdwmcpvn kgddkkkkdt nkdeeecnep kgdpemapiy lkrllpvfaq tfqqtmlpsi
      541 rkaslalirk mihfcseall kevcdsdvgh nlptilveit atvldqeddd dghllalqii
      601 rdlvdkggdi fldqlarlgv iskvstlagp ssddeneees kpekedepqe dakelqqgkp
      661 yhwrdwsiir grdclyiwsd aaalelsngs ngwfrfildg klatmyssgs peggsdsses
      721 rsefleklqr argqvkpsts sqpilsapgp tkltvgnwsl tclkegeiai hnsdgqqati
      781 lkedlpgfvf esnrgtkhsf taetslgsef vtgwtgkrgr klksklektk qkvrtmardl
      841 yddhfkaves mprgvvvtlr niatqlessw elhtnrqcie sentwrdlmk talenlivll
      901 kdentispye mcssglvqal ltvlnnsmdl dmkqdcsqlv erinvfktaf seneddesrp
      961 avalirklia vlesierlpl hlydtpgsty nlqiltrrlr frlerapget alidrtgrml
     1021 kmeplatves leqyllkmva kqwydfdrss fvfvrklreg qnfifrhqhd fdengiiywi
     1081 gtnaktayew vnpaayglvv vtssegrnlp ygrledilsr dnsalnchsn ddknawfaid
     1141 lglwvipsay tlrhargygr salrnwvfqv skdgqnwtsl ythvddcsln epgstatwpl
     1201 dppkdekqgw rhvrikqmgk nasgqthyls lsgfelygtv ngvcedqlgk aakeaeanlr
     1261 rqrrlvrsqv lkymvpgarv irgldwkwrd qdgspqgegt vtgelhnasp lmgaqsfpnl
     1321 ttpgttstvt mstssvtsss nvatattvls vgqslsntlt tsltstsses dtgqeaeysl
     1381 ydfldscras tllaelddde dlpepdeedd eneddnqedq eyeeilrrps lqrragsrsd
     1441 vthhavtsql pqvpagagsr pigeqeeeey etkggrrrtw dddyvlkrqf salvpafdpr
     1501 pgrtnvqqtt dleipppgtp hselleevec tpsprlaltl kvtglgttre velpltnfrs
     1561 tifyyvqkll qlscngnvks dklrriwept ytimyremkd sdkekengkm gcwsiehveq
     1621 ylgtdelpkn dlitylqkna daaflrhwkl tgtnksirkn rncsqliaay kdfcehgtks
     1681 glnqgaistl qssdilnltk eqpqakagng qnscgvedvl qllrilyiva sdpysrisqe
     1741 dgdeqpqftf ppdeftskki ttkilqqiee plalasgalp dwceqltskc pflipfetrq
     1801 lyftctafga sraivwlqnr reatvertrt tssvrrddpg efrvgrlkhe rvkvprgesl
     1861 mewaenvmqi hadrksvlev eflgeegtgl gptlefyalv aaefqrtdlg awlcddnfpd
     1921 desrhvdlgg glkppgyyvq rscglftapf pqdsdeleri tklfhflgif lakciqdnrl
     1981 vdlpiskpff klmcmgdiks nmskliyesr gdrdlhctes qseasteegh dslsvgsfee
     2041 dsksefildp pkpkppawfn giltwedfel vnphrarflk eikdlaikrr qilsnkglse
     2101 dekntklqel vlknpsgsgp plsiedlgln fqfcpssriy gftavdlkps gedemitmdn
     2161 aeeyvdlmfd fcmhtgiqkq meafrdgfnk vfpmeklssf sheevqmilc gnqspswaae
     2221 diinytepkl gytrdspgfl rfvrvlcgms sderkaflqf ttgcstlppg glanlhprlt
     2281 vvrkvdatda sypsvntcvh ylklpeysse eimrerllaa tmekgfhln
//
LOCUS       NP_001427738            1064 aa            linear   PRI 21-NOV-2025
DEFINITION  ubiquitin-like modifier-activating enzyme 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001427738 XP_005272706 XP_054183668
VERSION     NP_001427738.1
DBSOURCE    REFSEQ: accession NM_001440809.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Sirenko,M., Bernard,E., Creignou,M., Domenico,D., Farina,A., Arango
            Ossa,J.E., Kosmider,O., Hasserjian,R., Jadersten,M., Germing,U.,
            Sanz,G., van de Loosdrecht,A.A., Gurnari,C., Follo,M.Y., Thol,F.,
            Zamora,L., Pinheiro,R.F., Pellagatti,A., Elias,H.K., Haase,D.,
            Sander,B., Orna,E., Zoldan,K., Eder,L.N., Sperr,W.R.,
            Thalhammer,R., Ganster,C., Ades,L., Tobiasson,M., Palomo,L., Della
            Porta,M.G., Huberman,K., Fenaux,P., Belickova,M., Savona,M.R.,
            Klimek,V.M., Santos,F.P.S., Boultwood,J., Kotsianidis,I.,
            Santini,V., Sole,F., Platzbecker,U., Heuser,M., Valent,P.,
            Finelli,C., Voso,M.T., Shih,L.Y., Ogawa,S., Fontenay,M.,
            Jansen,J.H., Cervera,J., Ebert,B.L., Bejar,R., Greenberg,P.L.,
            Gattermann,N., Malcovati,L., Cazzola,M., Beck,D.B.,
            Hellstrom-Lindberg,E. and Papaemmanuil,E.
  TITLE     Molecular and clinical presentation of UBA1-mutated myelodysplastic
            syndromes
  JOURNAL   Blood 144 (11), 1221-1229 (2024)
   PUBMED   38687605
  REMARK    GeneRIF: Molecular and clinical presentation of UBA1-mutated
            myelodysplastic syndromes.
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Chen,C., Li,Y., Chen,Z., Shi,P., Li,Y. and Qian,S.
  TITLE     A comprehensive prognostic and immune infiltration analysis of UBA1
            in pan-cancer: A computational analysis and in vitro experiments
  JOURNAL   J Cell Mol Med 28 (16), e70037 (2024)
   PUBMED   39183260
  REMARK    GeneRIF: A comprehensive prognostic and immune infiltration
            analysis of UBA1 in pan-cancer: A computational analysis and in
            vitro experiments.
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Corty,R.W., Brogan,J., Byram,K., Springer,J., Grayson,P.C. and
            Bick,A.G.
  TITLE     VEXAS-Defining UBA1 Somatic Variants in 245,368 Diverse Individuals
            in the NIH All Of Us Cohort
  JOURNAL   Arthritis Rheumatol 76 (6), 942-948 (2024)
   PUBMED   38225170
  REMARK    GeneRIF: VEXAS-Defining UBA1 Somatic Variants in 245,368 Diverse
            Individuals in the NIH All Of Us Cohort.
REFERENCE   4  (residues 1 to 1064)
  AUTHORS   Collins,J.C., Magaziner,S.J., English,M., Hassan,B., Chen,X.,
            Balanda,N., Anderson,M., Lam,A., Fernandez-Pol,S., Kwong,B.,
            Greenberg,P.L., Terrier,B., Likhite,M.E., Kosmider,O., Wang,Y.,
            Samara,N.L., Walters,K.J., Beck,D.B. and Werner,A.
  TITLE     Shared and distinct mechanisms of UBA1 inactivation across
            different diseases
  JOURNAL   EMBO J 43 (10), 1919-1946 (2024)
   PUBMED   38360993
  REMARK    GeneRIF: Shared and distinct mechanisms of UBA1 inactivation across
            different diseases.
REFERENCE   5  (residues 1 to 1064)
  AUTHORS   Hadjadj,J. and Beck,D.
  TITLE     VEXAS Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   40373178
REFERENCE   6  (residues 1 to 1064)
  AUTHORS   Baumbach-Reardon,L., Hunter,J.M., Ahearn,M.E. and Pfautsch,M.
  TITLE     Spinal Muscular Atrophy, X-Linked Infantile
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301739
REFERENCE   7  (residues 1 to 1064)
  AUTHORS   Schwartz,A.L., Trausch,J.S., Ciechanover,A., Slot,J.W. and Geuze,H.
  TITLE     Immunoelectron microscopic localization of the ubiquitin-activating
            enzyme E1 in HepG2 cells
  JOURNAL   Proc Natl Acad Sci U S A 89 (12), 5542-5546 (1992)
   PUBMED   1376922
REFERENCE   8  (residues 1 to 1064)
  AUTHORS   Ayusawa,D., Kaneda,S., Itoh,Y., Yasuda,H., Murakami,Y.,
            Sugasawa,K., Hanaoka,F. and Seno,T.
  TITLE     Complementation by a cloned human ubiquitin-activating enzyme E1 of
            the S-phase-arrested mouse FM3A cell mutant with thermolabile E1
  JOURNAL   Cell Struct Funct 17 (2), 113-122 (1992)
   PUBMED   1606621
REFERENCE   9  (residues 1 to 1064)
  AUTHORS   Takahashi,E., Ayusawa,D., Kaneda,S., Itoh,Y., Seno,T. and Hori,T.
  TITLE     The human ubiquitin-activating enzyme E1 gene (UBE1) mapped to band
            Xp11.3----p11.23 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 59 (4), 268-269 (1992)
   PUBMED   1544321
REFERENCE   10 (residues 1 to 1064)
  AUTHORS   Kudo,M., Sugasawa,K., Hori,T., Enomoto,T., Hanaoka,F. and Ui,M.
  TITLE     Human ubiquitin-activating enzyme (E1): compensation for
            heat-labile mouse E1 and its gene localization on the X chromosome
  JOURNAL   Exp Cell Res 192 (1), 110-117 (1991)
   PUBMED   1845793
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513366.11.
            
            On or before May 30, 2025 this sequence version replaced
            XP_005272706.1, XP_054183668.1.
            
            Summary: The protein encoded by this gene catalyzes the first step
            in ubiquitin conjugation to mark cellular proteins for degradation.
            This gene complements an X-linked mouse temperature-sensitive
            defect in DNA synthesis, and thus may function in DNA repair. It is
            part of a gene cluster on chromosome Xp11.23. Alternatively spliced
            transcript variants that encode the same protein have been
            described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1779307.1,
                                           SRR11853562.33405.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.3"
     Protein         1..1064
                     /product="ubiquitin-like modifier-activating enzyme 1
                     isoform 2"
                     /EC_number="6.2.1.45"
                     /note="POC20 centriolar protein homolog; UBA1,
                     ubiquitin-activating enzyme E1 homolog A; A1S9T and BN75
                     temperature sensitivity complementing; testicular
                     secretory protein Li 63"
                     /calculated_mol_wt=118431
     Region          55..1061
                     /region_name="Ube1"
                     /note="ubiquitin-activating enzyme E1; TIGR01408"
                     /db_xref="CDD:273603"
     CDS             1..1064
                     /gene="UBA1"
                     /gene_synonym="A1S9; A1S9T; A1ST; AMCX1; CFAP124; GXP1;
                     POC20; SMAX2; UBA1A; UBE1; UBE1X; VEXAS"
                     /coded_by="NM_001440809.1:257..3451"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:7317"
                     /db_xref="HGNC:HGNC:12469"
                     /db_xref="MIM:314370"
ORIGIN      
        1 mrslpqmsss plskkrrvsg pdpkpgsncs paqsvlsevp svptngmakn gseadidegl
       61 ysrqlyvlgh eamkrlqtss vlvsglrglg veiakniilg gvkavtlhdq gtaqwadlss
      121 qfylreedig knraevsqpr laelnsyvpv taytgplved flsgfqvvvl tntpledqlr
      181 vgefchnrgi klvvadtrgl fgqlfcdfge emiltdsnge qplsamvsmv tkdnpgvvtc
      241 ldearhgfes gdfvsfsevq gmvelngnqp meikvlgpyt fsicdtsnfs dyirggivsq
      301 vkvpkkisfk slvaslaepd fvvtdfakfs rpaqlhigfq alhqfcaqhg rpprprneed
      361 aaelvalaqa vnaralpavq qnnldedlir klayvaagdl apinafiggl aaqevmkacs
      421 gkfmpimqwl yfdaleclpe dkevltedkc lqrqnrydgq vavfgsdlqe klgkqkyflv
      481 gagaigcell knfamiglgc geggeiivtd mdtieksnln rqflfrpwdv tklksdtaaa
      541 avrqmnphir vtshqnrvgp dteriydddf fqnldgvana ldnvdarmym drrcvyyrkp
      601 llesgtlgtk gnvqvvipfl tesysssqdp peksipictl knfpnaieht lqwardefeg
      661 lfkqpaenvn qyltdpkfve rtlrlagtqp levleavqrs lvlqrpqtwa dcvtwachhw
      721 htqysnnirq llhnfppdql tssgapfwsg pkrcphpltf dvnnplhldy vmaaanlfaq
      781 tygltgsqdr aavatflqsv qvpeftpksg vkihvsdqel qsanasvdds rleelkatlp
      841 spdklpgfkm ypidfekddd snfhmdfiva asnlraenyd ipsadrhksk liagkiipai
      901 atttaavvgl vclelykvvq ghrqldsykn gflnlalpff gfseplaapr hqyynqewtl
      961 wdrfevqglq pngeemtlkq fldyfktehk leitmlsqgv smlysffmpa aklkerldqp
     1021 mteivsrvsk rklgrhvral vlelccndes gedvevpyvr ytir
//
LOCUS       NP_001427586             736 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 3 isoform 6 [Homo sapiens].
ACCESSION   NP_001427586
VERSION     NP_001427586.1
DBSOURCE    REFSEQ: accession NM_001440657.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Ghashghaei,M., Liu,Y., Ettles,J., Bombaci,G., Ramkumar,N., Liu,Z.,
            Escano,L., Miko,S.S., Kim,Y., Waldron,J.A., Do,K., MacPherson,K.,
            Yuen,K.A., Taibi,T., Yue,M., Arsalan,A., Jin,Z., Edin,G.,
            Karsan,A., Morin,G.B., Kuchenbauer,F., Perna,F., Bushell,M. and
            Vu,L.P.
  TITLE     Translation efficiency driven by CNOT3 subunit of the CCR4-NOT
            complex promotes leukemogenesis
  JOURNAL   Nat Commun 15 (1), 2340 (2024)
   PUBMED   38491013
  REMARK    GeneRIF: Translation efficiency driven by CNOT3 subunit of the
            CCR4-NOT complex promotes leukemogenesis.
            Erratum:[Nat Commun. 2024 Oct 7;15(1):8674. doi:
            10.1038/s41467-024-53071-1. PMID: 39375334]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Burgess,H.M., Grande,R., Riccio,S., Dinesh,I., Winkler,G.S.,
            Depledge,D.P. and Mohr,I.
  TITLE     CCR4-NOT differentially controls host versus virus poly(a)-tail
            length and regulates HCMV infection
  JOURNAL   EMBO Rep 24 (12), e56327 (2023)
   PUBMED   37846490
  REMARK    GeneRIF: CCR4-NOT differentially controls host versus virus
            poly(a)-tail length and regulates HCMV infection.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   Zhao,P., Meng,Q., Wan,C., Lei,T., Zhang,L., Zhang,X., Tan,L.,
            Zhu,H. and He,X.
  TITLE     Clinical features of CNOT3-associated neurodevelopmental disorder
            in three Chinese patients
  JOURNAL   Neurogenetics 24 (2), 129-136 (2023)
   PUBMED   36802310
  REMARK    GeneRIF: Clinical features of CNOT3-associated neurodevelopmental
            disorder in three Chinese patients.
REFERENCE   5  (residues 1 to 736)
  AUTHORS   McLenachan,S., Zhang,D., Grainok,J., Zhang,X., Huang,Z., Chen,S.C.,
            Zaw,K., Lima,A., Jennings,L., Roshandel,D., Moon,S.Y., Heath
            Jeffery,R.C., Attia,M.S., Thompson,J.A., Lamey,T.M., McLaren,T.L.,
            De Roach,J., Fletcher,S. and Chen,F.K.
  TITLE     Determinants of Disease Penetrance in PRPF31-Associated Retinopathy
  JOURNAL   Genes (Basel) 12 (10), 1542 (2021)
   PUBMED   34680937
  REMARK    GeneRIF: Determinants of Disease Penetrance in PRPF31-Associated
            Retinopathy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Yin,X., Warner,D.R., Roberts,E.A., Pisano,M.M. and Greene,R.M.
  TITLE     Identification of novel CBP interacting proteins in embryonic
            orofacial tissue
  JOURNAL   Biochem Biophys Res Commun 329 (3), 1010-1017 (2005)
   PUBMED   15752756
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Aoki,T., Okada,N., Wakamatsu,T. and Tamura,T.A.
  TITLE     TBP-interacting protein 120B, which is induced in relation to
            myogenesis, binds to NOT3
  JOURNAL   Biochem Biophys Res Commun 296 (5), 1097-1103 (2002)
   PUBMED   12207886
  REMARK    GeneRIF: TBP-interacting protein 120B binds to NOT3
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC245052.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3350289.1,
                                           SRR14038197.1840466.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..736
                     /product="CCR4-NOT transcription complex subunit 3 isoform
                     6"
                     /note="NOT3 (negative regulator of transcription 3, yeast)
                     homolog; CCR4-associated factor 3; leukocyte receptor
                     cluster member 2"
                     /calculated_mol_wt=79171
     Region          3..230
                     /region_name="Not3"
                     /note="Not1 N-terminal domain, CCR4-Not complex component;
                     pfam04065"
                     /db_xref="CDD:461155"
     Region          241..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75175.1)"
     Region          <289..660
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Region          621..722
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..736
                     /gene="CNOT3"
                     /gene_synonym="IDDSADF; LENG2; NOT3; NOT3H"
                     /coded_by="NM_001440657.1:283..2493"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:4849"
                     /db_xref="HGNC:HGNC:7879"
                     /db_xref="MIM:604910"
ORIGIN      
        1 madkrklqge idrclkkvse gveqfediwq klhnaananq kekyeadlkk eikklqrlrd
       61 qiktwvasne ikdkrqlidn rklietqmer fkvveretkt kayskeglgl aqkvdpaqke
      121 keevgqwltn tidtlnmqvd qfesevesls vqtrkkkgdk dqkqdriegl krhiekhryh
      181 vrmletilrm ldndsilvda irkikddvey yvdssqdpdf eeneflyddl dledipqalv
      241 atsppshshm edeifnqsss tptsttsssp ippspanctt enseddkkrg rstdsevsqs
      301 pakngskpvh snqhpqspav pptypsgppp aasalsttpg nngvpapaap psalgpkasp
      361 apshnsgtpa pyaqavappa psgpsttqpr ppsvqpsggg gggsggggss sssnssaggg
      421 agkqngatsy ssvvadspae valsssggnn assqalgpps gphnpppsts kepsaaaptg
      481 aggvapgsgn nsggpsllvp lpvnppsspt psfsdakaag allngppqfs tapeikapep
      541 lsslksmaer aaissgiedp vptlhlterd iilsstsapp asaqpplqls evniplslgv
      601 cplgpvpltk eqlyqqamee aawhhmphps dserirqylp rnpcptppyh hqmppphsdt
      661 vefyqrlste tlffifyyle gtkaqylaak alkkqswrfh tkymmwfqrh eepktitdef
      721 eqvrappplf pllglg
//
LOCUS       NP_001427734            1243 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphorylase b kinase regulatory subunit alpha, liver isoform
            isoform 7 [Homo sapiens].
ACCESSION   NP_001427734 XP_006724559 XP_054183175
VERSION     NP_001427734.1
DBSOURCE    REFSEQ: accession NM_001440805.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1243)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1243)
  AUTHORS   Dong,R., Wei,X., Zhang,K., Song,F., Lv,Y., Gao,M., Wang,D., Ma,J.,
            Gai,Z. and Liu,Y.
  TITLE     Genotypic and phenotypic characteristics of 12 chinese children
            with glycogen storage diseases
  JOURNAL   Front Genet 13, 932760 (2022)
   PUBMED   36105079
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1243)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1243)
  AUTHORS   Benner,A., Alhaidan,Y., Lines,M.A., Brusgaard,K., De Leon,D.D.,
            Sparkes,R., Frederiksen,A.L. and Christesen,H.T.
  TITLE     PHKA2 variants expand the phenotype of phosphorylase B kinase
            deficiency to include patients with ketotic hypoglycemia only
  JOURNAL   Am J Med Genet A 185 (10), 2959-2975 (2021)
   PUBMED   34117828
  REMARK    GeneRIF: PHKA2 variants expand the phenotype of phosphorylase B
            kinase deficiency to include patients with ketotic hypoglycemia
            only.
REFERENCE   5  (residues 1 to 1243)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1243)
  AUTHORS   Herbert,M., Goldstein,J.L., Rehder,C., Austin,S., Kishnani,P.S. and
            Bali,D.S.
  TITLE     Phosphorylase Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21634085
REFERENCE   7  (residues 1 to 1243)
  AUTHORS   Davidson,J.J., Ozcelik,T., Hamacher,C., Willems,P.J., Francke,U.
            and Kilimann,M.W.
  TITLE     cDNA cloning of a liver isoform of the phosphorylase kinase alpha
            subunit and mapping of the gene to Xp22.2-p22.1, the region of
            human X-linked liver glycogenosis
  JOURNAL   Proc Natl Acad Sci U S A 89 (6), 2096-2100 (1992)
   PUBMED   1372435
REFERENCE   8  (residues 1 to 1243)
  AUTHORS   Wauters,J.G., Bossuyt,P.J., Davidson,J., Hendrickx,J.,
            Kilimann,M.W. and Willems,P.J.
  TITLE     Regional mapping of a liver alpha-subunit gene of phosphorylase
            kinase (PHKA) to the distal region of human chromosome Xp
  JOURNAL   Cytogenet Cell Genet 60 (3-4), 194-196 (1992)
   PUBMED   1505214
REFERENCE   9  (residues 1 to 1243)
  AUTHORS   Willems,P.
  TITLE     Families with X-linked liver glycogenosis due to phosphorylase
            kinase deficiency
  JOURNAL   Clin Genet 38 (1), 80 (1990)
   PUBMED   2387090
REFERENCE   10 (residues 1 to 1243)
  AUTHORS   Willems,P.J., Gerver,W.J., Berger,R. and Fernandes,J.
  TITLE     The natural history of liver glycogenosis due to phosphorylase
            kinase deficiency: a longitudinal study of 41 patients
  JOURNAL   Eur J Pediatr 149 (4), 268-271 (1990)
   PUBMED   2303074
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL732509.4 and AL096700.14.
            
            On or before May 30, 2025 this sequence version replaced
            XP_006724559.1, XP_054183175.1.
            
            Summary: Phosphorylase kinase is a polymer of 16 subunits, four
            each of alpha, beta, gamma and delta. The alpha subunit includes
            the skeletal muscle and hepatic isoforms, and the hepatic isoform
            is encoded by this gene. The beta subunit is the same in both the
            muscle and hepatic isoforms, and encoded by one gene. The gamma
            subunit also includes the skeletal muscle and hepatic isoforms,
            which are encoded by two different genes. The delta subunit is a
            calmodulin and can be encoded by three different genes. The gamma
            subunits contain the active site of the enzyme, whereas the alpha
            and beta subunits have regulatory functions controlled by
            phosphorylation. The delta subunit mediates the dependence of the
            enzyme on calcium concentration. Mutations in this gene cause
            glycogen storage disease type 9A, also known as X-linked liver
            glycogenosis. Alternatively spliced transcript variants have been
            reported, but the full-length nature of these variants has not been
            determined.[provided by RefSeq, Feb 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.28822.1,
                                           SRR14038194.356366.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.13"
     Protein         1..1243
                     /product="phosphorylase b kinase regulatory subunit alpha,
                     liver isoform isoform 7"
                     /EC_number="2.7.11.19"
                     /note="phosphorylase kinase alpha L subunit; phosphorylase
                     kinase alpha-subunit"
                     /calculated_mol_wt=139212
     Region          8..>439
                     /region_name="Glyco_hydro_15"
                     /note="Glycosyl hydrolases family 15; pfam00723"
                     /db_xref="CDD:395586"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46019.1)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P46019.1)"
     Site            735
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46019.1)"
     Region          <802..919
                     /region_name="Bac_rhamnosid6H"
                     /note="Bacterial alpha-L-rhamnosidase 6 hairpin
                     glycosidase domain; cl46875"
                     /db_xref="CDD:481215"
     Region          807..837
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P46019.1)"
     Region          972..998
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46019.1)"
     Site            983
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P46019.1)"
     Site            1015
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46019.1)"
     Site            1052
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P46019.1)"
     Region          1067..1107
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P46019.1)"
     Region          <1070..>1155
                     /region_name="KPBB_C"
                     /note="Phosphorylase b kinase C-terminal domain;
                     pfam19292"
                     /db_xref="CDD:437124"
     CDS             1..1243
                     /gene="PHKA2"
                     /gene_synonym="GSD9A; PHK; PYK; PYKL; XLG; XLG2"
                     /coded_by="NM_001440805.1:183..3914"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:5256"
                     /db_xref="HGNC:HGNC:8926"
                     /db_xref="MIM:300798"
ORIGIN      
        1 mrsrsnsgvr ldgyarlvqq tilcyqnpvt gllsasheqk dawvrdniys ilavwglgma
       61 yrknadrded kakayeleqn vvklmrgllq cmmrqvakve kfkhtqstkd slhakyntat
      121 cgtvvgddqw ghlqvdatsl fllflaqmta sglriiftld evafiqnlvf yieaaykvad
      181 ygmwergdkt nqgipelnas svgmakaale aideldlfga hggrksvihv lpdevehcqs
      241 ilfsmlpras tskeidagll siisfpafav edvnlvnvtk neiisklqgr ygccrflrdg
      301 yktpredpnr lhydpaelkl feniecewpv fwtyfiidgv fsgdavqvqe yrealegili
      361 rgkngirlvp elyavppnkv deeyknphtv drvpmgkvph lwgqslyils sllaegflaa
      421 geidplnrrf stsvkpdvvv qvtvlaennh ikdllrkhgv nvqsiadihp iqvqpgrils
      481 hiyaklgrnk nmnlsgrpyr higvlgtskl yvirnqiftf tpqftdqhhf ylaldnemiv
      541 emlrielayl ctcwrmtgrp tltfpisrtm ltndgsdihs avlstirkle dgyfggarvk
      601 lgnlsefltt sfytyltfld pdcdeklfdn asegtfspds dsdlvgyled tcnqesqdel
      661 dhyinhllqs tslrsylppl ckntedrhvf saihstrdil svmakakgle vpfvpmtlpt
      721 kvlsahrksl nlvdspqpll ekvpesdfqw prddhgdvdc eklveqlkdc snlqdqadil
      781 yilyvikgps wdtnlsgqhg vtvqnllgel ygkaglnqew gliryisgll rkkvevlaea
      841 ctdllshqkq ltvglppepr ekiisaplpp eeltkliyea sgqdisiavl tqeivvylam
      901 yvraqpslfv emlrlrigli iqvmatelar slncsgeeas eslmnlspfd mknllhhils
      961 gkefgversv rpihsstssp tisihevght gvtktersgi nrlrsemkqm trrfsadeqf
     1021 fsvgqaasss ahssksavtv prdycrsstp ssptgtsssd sgghhigwge rqgqwlrrrr
     1081 ldgainrvpv gfyqrvwkil qkchglsidg yvlpssttre mtpheikfav hvesvlnrvp
     1141 qpeyrqllve aimvltllsd temtsiggii hvdqivqmas qlflqdqvsi gamdtlekdq
     1201 atgichffyd sapsgaygtm tyltravasy lqellpnsgc qmq
//
LOCUS       NP_001427355             428 aa            linear   PRI 21-NOV-2025
DEFINITION  interleukin-12 receptor subunit beta-1 isoform 7 [Homo sapiens].
ACCESSION   NP_001427355 XP_047294730 XP_054176861
VERSION     NP_001427355.1
DBSOURCE    REFSEQ: accession NM_001440426.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Chen,H., Ge,X., Li,C., Zeng,J. and Wang,X.
  TITLE     Structure and assembly of the human IL-12 signaling complex
  JOURNAL   Structure 32 (10), 1640-1651 (2024)
   PUBMED   39111304
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Huang,J., He,Q., Huang,L., Liu,L., Yang,P. and Chen,M.
  TITLE     Discovering the link between IL12RB1 gene polymorphisms and
            tuberculosis susceptibility: a comprehensive meta-analysis
  JOURNAL   Front Public Health 12, 1249880 (2024)
   PUBMED   38317798
  REMARK    GeneRIF: Discovering the link between IL12RB1 gene polymorphisms
            and tuberculosis susceptibility: a comprehensive meta-analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Rosas Mejia,O., Claeys,T.A., Williams,A., Zafar,A. and
            Robinson,R.T.
  TITLE     IL12RB1 allele bias in human TH cells is regulated by functional
            SNPs in its 3'UTR
  JOURNAL   Cytokine 158, 155993 (2022)
   PUBMED   36007427
  REMARK    GeneRIF: IL12RB1 allele bias in human TH cells is regulated by
            functional SNPs in its 3'UTR.
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Khattak,F.A., Akbar,N.U., Riaz,M., Hussain,M., Rehman,K., Khan,S.N.
            and Khan,T.A.
  TITLE     Novel IL-12Rbeta1 deficiency-mediates recurrent cutaneous
            leishmaniasis
  JOURNAL   Int J Infect Dis 112, 338-345 (2021)
   PUBMED   34438084
  REMARK    GeneRIF: Novel IL-12Rbeta1 deficiency-mediates recurrent cutaneous
            leishmaniasis.
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Yamamoto,K., Kobayashi,H., Miura,O., Hirosawa,S. and Miyasaka,N.
  TITLE     Assignment of IL12RB1 and IL12RB2, interleukin-12 receptor beta 1
            and beta 2 chains, to human chromosome 19 band p13.1 and chromosome
            1 band p31.2, respectively, by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 77 (3-4), 257-258 (1997)
   PUBMED   9284929
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Bacon,C.M., Petricoin,E.F. 3rd, Ortaldo,J.R., Rees,R.C.,
            Larner,A.C., Johnston,J.A. and O'Shea,J.J.
  TITLE     Interleukin 12 induces tyrosine phosphorylation and activation of
            STAT4 in human lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 92 (16), 7307-7311 (1995)
   PUBMED   7638186
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Bacon,C.M., McVicar,D.W., Ortaldo,J.R., Rees,R.C., O'Shea,J.J. and
            Johnston,J.A.
  TITLE     Interleukin 12 (IL-12) induces tyrosine phosphorylation of JAK2 and
            TYK2: differential use of Janus family tyrosine kinases by IL-2 and
            IL-12
  JOURNAL   J Exp Med 181 (1), 399-404 (1995)
   PUBMED   7528775
REFERENCE   8  (residues 1 to 428)
  AUTHORS   Ling,P., Gately,M.K., Gubler,U., Stern,A.S., Lin,P., Hollfelder,K.,
            Su,C., Pan,Y.C. and Hakimi,J.
  TITLE     Human IL-12 p40 homodimer binds to the IL-12 receptor but does not
            mediate biologic activity
  JOURNAL   J Immunol 154 (1), 116-127 (1995)
   PUBMED   7527811
REFERENCE   9  (residues 1 to 428)
  AUTHORS   Gillessen,S., Carvajal,D., Ling,P., Podlaski,F.J., Stremlo,D.L.,
            Familletti,P.C., Gubler,U., Presky,D.H., Stern,A.S. and Gately,M.K.
  TITLE     Mouse interleukin-12 (IL-12) p40 homodimer: a potent IL-12
            antagonist
  JOURNAL   Eur J Immunol 25 (1), 200-206 (1995)
   PUBMED   7843232
REFERENCE   10 (residues 1 to 428)
  AUTHORS   Chua,A.O., Chizzonite,R., Desai,B.B., Truitt,T.P., Nunes,P.,
            Minetti,L.J., Warrier,R.R., Presky,D.H., Levine,J.F., Gately,M.K.
            et al.
  TITLE     Expression cloning of a human IL-12 receptor component. A new
            member of the cytokine receptor superfamily with strong homology to
            gp130
  JOURNAL   J Immunol 153 (1), 128-136 (1994)
   PUBMED   7911493
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020904.7.
            
            On or before May 20, 2025 this sequence version replaced
            XP_047294730.1, XP_054176861.1.
            
            Summary: The protein encoded by this gene is a type I transmembrane
            protein that belongs to the hemopoietin receptor superfamily. This
            protein binds to interleukine 12 (IL12) with a low affinity, and is
            thought to be a part of IL12 receptor complex. This protein forms a
            disulfide-linked oligomer, which is required for its IL12 binding
            activity. The coexpression of this and IL12RB2 proteins was shown
            to lead to the formation of high-affinity IL12 binding sites and
            reconstitution of IL12 dependent signaling. Mutations in this gene
            impair the development of interleukin-17-producing T lymphocytes
            and result in increased susceptibility to mycobacterial and
            Salmonella infections. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.2083558.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..428
                     /product="interleukin-12 receptor subunit beta-1 isoform
                     7"
                     /note="IL-12 receptor beta component; interleukin-12
                     receptor beta-1 chain; IL-12R subunit beta-1; IL-12
                     receptor subunit beta-1; cluster of differentiation 212;
                     interleukin 12 receptor, beta 1"
                     /calculated_mol_wt=47269
     CDS             1..428
                     /gene="IL12RB1"
                     /gene_synonym="CD212; IL-12R-BETA1; IL12RB; IMD30"
                     /coded_by="NM_001440426.1:163..1449"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:3594"
                     /db_xref="HGNC:HGNC:5971"
                     /db_xref="MIM:601604"
ORIGIN      
        1 mfvglfslls fnvfrsgdgv aeprrwqrgs pgavglyvdp meplvtwvvp llflfllsrq
       61 gaacrtsecc fqdppypdad sgsasgprdl rcyrissdry ecswqyegpt agvshflrcc
      121 lssgrccyfa agsatrlqfs dqagvsvlyt vtlwveswar nqtekspevt lqlynsvkye
      181 pplgdikvsk lagqlrmewe tpdnqvgaev qfrhrtpssp wklgdcgpqd ddtesclcpl
      241 emnvaqefql rrrqlgsqgs swskwsspvc vppvglvlia enppqpqvrf sveqlgqdgr
      301 rrltlkeqpt qlelpegcqg lapgtevtyr lqlhmlscpc kakatrtlhl gkmpylsgaa
      361 ynvavissnq fgpglnqtwh ipadthtdgm isahcnlrlp dsrdspasas rvagitgich
      421 htrlilyf
//
LOCUS       NP_001412002             532 aa            linear   PRI 21-NOV-2025
DEFINITION  coatomer subunit delta isoform 3 [Homo sapiens].
ACCESSION   NP_001412002
VERSION     NP_001412002.1
DBSOURCE    REFSEQ: accession NM_001425073.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   O'Donoghue,L., Comer,S.P., Hiebner,D.W., Schoen,I., von
            Kriegsheim,A. and Smolenski,A.
  TITLE     RhoGAP6 interacts with COPI to regulate protein transport
  JOURNAL   Biochem J 480 (14), 1109-1127 (2023)
   PUBMED   37409526
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Li,W., Liang,J., Outeda,P., Turner,S., Wakimoto,B.T. and Watnick,T.
  TITLE     A genetic screen in Drosophila reveals an unexpected role for the
            KIP1 ubiquitination-promoting complex in male fertility
  JOURNAL   PLoS Genet 16 (12), e1009217 (2020)
   PUBMED   33378371
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Tidwell,T., Deshotel,M., Palumbos,J., Miller,C., Bayrak-Toydemir,P.
            and Carey,J.C.
  TITLE     Novel de novo ARCN1 intronic variant causes rhizomelic short
            stature with microretrognathia and developmental delay
  JOURNAL   Cold Spring Harb Mol Case Stud 6 (6), a005728 (2020)
   PUBMED   33154040
  REMARK    GeneRIF: Novel de novo ARCN1 intronic variant causes rhizomelic
            short stature with microretrognathia and developmental delay.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 532)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 532)
  AUTHORS   Schekman,R. and Orci,L.
  TITLE     Coat proteins and vesicle budding
  JOURNAL   Science 271 (5255), 1526-1533 (1996)
   PUBMED   8599108
  REMARK    Review article
REFERENCE   7  (residues 1 to 532)
  AUTHORS   Cukierman,E., Huber,I., Rotman,M. and Cassel,D.
  TITLE     The ARF1 GTPase-activating protein: zinc finger motif and Golgi
            complex localization
  JOURNAL   Science 270 (5244), 1999-2002 (1995)
   PUBMED   8533093
REFERENCE   8  (residues 1 to 532)
  AUTHORS   Radice,P., Pensotti,V., Jones,C., Perry,H., Pierotti,M.A. and
            Tunnacliffe,A.
  TITLE     The human archain gene, ARCN1, has highly conserved homologs in
            rice and Drosophila
  JOURNAL   Genomics 26 (1), 101-106 (1995)
   PUBMED   7782067
REFERENCE   9  (residues 1 to 532)
  AUTHORS   Orcl,L., Palmer,D.J., Amherdt,M. and Rothman,J.E.
  TITLE     Coated vesicle assembly in the Golgi requires only coatomer and ARF
            proteins from the cytosol
  JOURNAL   Nature 364 (6439), 732-734 (1993)
   PUBMED   8355790
REFERENCE   10 (residues 1 to 532)
  AUTHORS   Waters,M.G., Serafini,T. and Rothman,J.E.
  TITLE     'Coatomer': a cytosolic protein complex containing subunits of
            non-clathrin-coated Golgi transport vesicles
  JOURNAL   Nature 349 (6306), 248-251 (1991)
   PUBMED   1898986
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000941.6.
            
            Summary: This gene maps in a region, which include the mixed
            lineage leukemia and Friend leukemia virus integration 1 genes,
            where multiple disease-associated chromosome translocations occur.
            It is an intracellular protein. Archain sequences are well
            conserved among eukaryotes and this protein may play a fundamental
            role in eukaryotic cell biology. It has similarities to heat shock
            proteins and clathrin-associated proteins, and may be involved in
            vesicle structure or trafficking. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4256135.1,
                                           SRR11853564.5949.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..532
                     /product="coatomer subunit delta isoform 3"
                     /note="coatomer protein delta-COP; coatomer protein
                     complex, subunit delta; archain vesicle transport protein
                     1; coatomer delta subunit; delta-coat protein; COPI coat
                     complex subunit delta"
                     /calculated_mol_wt=59395
     Region          4..133
                     /region_name="Delta_COP_N"
                     /note="delta subunit of the F-COPI complex, N-terminal
                     domain; cd14830"
                     /db_xref="CDD:341434"
     Region          272..529
                     /region_name="AP_delta-COPI_MHD"
                     /note="Mu homology domain (MHD) of adaptor protein (AP)
                     coat protein I (COPI) delta subunit; cd09254"
                     /db_xref="CDD:271162"
     CDS             1..532
                     /gene="ARCN1"
                     /gene_synonym="COPD; SRMMD; SSMG"
                     /coded_by="NM_001425073.1:140..1738"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:372"
                     /db_xref="HGNC:HGNC:649"
                     /db_xref="MIM:600820"
ORIGIN      
        1 mvllaaavct kagkaivsrq fvemtrtrie gllaafpklm ntgkqhtfve tesvryvyqp
       61 meklymvlit tknsniledl etlrlfsrvi peycraleen eisehcfdli fafdeivalg
      121 yrenvnlaqi rtftemdshe ekvfravret qereakaemr rkakelqqar rdaerqgkka
      181 pgfggfgssa vsggstaami tetiietdkp kvapaparps gpskalklga kgkevdnfvd
      241 klksegetim sssmgkrtse atkmhappin mesvhmkiee kitltcgrdg glqnmelhgm
      301 imlrisddky grirlhvene dkkgvqlqth pnvdkklfta esliglknpe ksfpvnsdvg
      361 vlkwrlqtte esfipltinc wpsesgngcd vnieyelqed nlelndvvit iplptgtkig
      421 tiqrrlawal ckadmsgvga pvigeidgey rhdsrrntle wclpvidakn ksgslefsia
      481 gqpndffpvq vsfvskknyc niqvtkvtqv dgnspvrfst ettflvdkye il
//
LOCUS       NP_001427992             746 aa            linear   PRI 21-NOV-2025
DEFINITION  inhibitor of nuclear factor kappa-B kinase subunit alpha isoform 5
            [Homo sapiens].
ACCESSION   NP_001427992 XP_047280496 XP_054220630
VERSION     NP_001427992.1
DBSOURCE    REFSEQ: accession NM_001441063.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 746)
  AUTHORS   Chen,X., Wu,W., Jeong,J.H., Rokavec,M., Wei,R., Feng,S.,
            Schroth,W., Brauch,H., Zhong,S. and Luo,J.L.
  TITLE     Cytokines-activated nuclear IKKalpha-FAT10 pathway induces breast
            cancer tamoxifen-resistance
  JOURNAL   Sci China Life Sci 67 (7), 1413-1426 (2024)
   PUBMED   38565741
  REMARK    GeneRIF: Cytokines-activated nuclear IKKalpha-FAT10 pathway induces
            breast cancer tamoxifen-resistance.
REFERENCE   3  (residues 1 to 746)
  AUTHORS   Chang,X., Guo,Y., Zhang,Q., Zheng,X., Cui,X., Hu,J., Zhang,Z.,
            Zhang,F. and Wang,X.
  TITLE     GRP78 recognizes EV-F 3D protein and activates NF-kappaB to repress
            virus replication by interacting with CHUK/IKBKB
  JOURNAL   J Virol 98 (6), e0026824 (2024)
   PUBMED   38775480
  REMARK    GeneRIF: GRP78 recognizes EV-F 3D protein and activates NF-kappaB
            to repress virus replication by interacting with CHUK/IKBKB.
REFERENCE   4  (residues 1 to 746)
  AUTHORS   McIntosh,K., Khalaf,Y.H., Craig,R., West,C., McCulloch,A.,
            Waghmare,A., Lawson,C., Chan,E.Y.W., Mackay,S., Paul,A. and
            Plevin,R.
  TITLE     IL-1beta stimulates a novel, IKKalpha -dependent, NIK -independent
            activation of non-canonical NFkappaB signalling
  JOURNAL   Cell Signal 107, 110684 (2023)
   PUBMED   37080443
  REMARK    GeneRIF: IL-1beta stimulates a novel, IKKalpha -dependent, NIK
            -independent activation of non-canonical NFkappaB signalling.
REFERENCE   5  (residues 1 to 746)
  AUTHORS   Yang,H., Espada,C.E., Phillips,S., Martinez,N., Kenney,A.D.,
            Yount,J.S., Xiong,Y. and Wu,L.
  TITLE     The host antiviral protein SAMHD1 suppresses NF-kappaB activation
            by interacting with the IKK complex during inflammatory responses
            and viral infection
  JOURNAL   J Biol Chem 299 (6), 104750 (2023)
   PUBMED   37100289
  REMARK    GeneRIF: The host antiviral protein SAMHD1 suppresses NF-kappaB
            activation by interacting with the IKK complex during inflammatory
            responses and viral infection.
REFERENCE   6  (residues 1 to 746)
  AUTHORS   Scherer,D.C., Brockman,J.A., Chen,Z., Maniatis,T. and Ballard,D.W.
  TITLE     Signal-induced degradation of I kappa B alpha requires
            site-specific ubiquitination
  JOURNAL   Proc Natl Acad Sci U S A 92 (24), 11259-11263 (1995)
   PUBMED   7479976
REFERENCE   7  (residues 1 to 746)
  AUTHORS   Mock,B.A., Connelly,M.A., McBride,O.W., Kozak,C.A. and Marcu,K.B.
  TITLE     CHUK, a conserved helix-loop-helix ubiquitous kinase, maps to human
            chromosome 10 and mouse chromosome 19
  JOURNAL   Genomics 27 (2), 348-351 (1995)
   PUBMED   7558004
REFERENCE   8  (residues 1 to 746)
  AUTHORS   Connelly,M.A. and Marcu,K.B.
  TITLE     CHUK, a new member of the helix-loop-helix and leucine zipper
            families of interacting proteins, contains a serine-threonine
            kinase catalytic domain
  JOURNAL   Cell Mol Biol Res 41 (6), 537-549 (1995)
   PUBMED   8777433
REFERENCE   9  (residues 1 to 746)
  AUTHORS   Ganchi,P.A., Sun,S.C., Greene,W.C. and Ballard,D.W.
  TITLE     A novel NF-kappa B complex containing p65 homodimers: implications
            for transcriptional control at the level of subunit dimerization
  JOURNAL   Mol Cell Biol 13 (12), 7826-7835 (1993)
   PUBMED   8246997
REFERENCE   10 (residues 1 to 746)
  AUTHORS   Ganchi,P.A., Sun,S.C., Greene,W.C. and Ballard,D.W.
  TITLE     I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B
            p65 and requires the transactivation domain to inhibit NF-kappa B
            p65 DNA binding
  JOURNAL   Mol Biol Cell 3 (12), 1339-1352 (1992)
   PUBMED   1493333
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138921.14.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047280496.1, XP_054220630.1.
            
            Summary: This gene encodes a member of the serine/threonine protein
            kinase family. The encoded protein, a component of a
            cytokine-activated protein complex that is an inhibitor of the
            essential transcription factor NF-kappa-B complex, phosphorylates
            sites that trigger the degradation of the inhibitor via the
            ubiquination pathway, thereby activating the transcription factor.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2079188.1,
                                           SRR14038196.1224942.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.31"
     Protein         1..746
                     /product="inhibitor of nuclear factor kappa-B kinase
                     subunit alpha isoform 5"
                     /EC_number="2.7.11.10"
                     /note="I-kappa-B kinase-alpha; I-kappa-B kinase 1; Nuclear
                     factor NFkappaB inhibitor kinase alpha; IKK-a kinase; IkB
                     kinase alpha subunit; inhibitor of nuclear factor kappa-B
                     kinase subunit alpha; conserved helix-loop-helix
                     ubiquitous kinase; transcription factor 16"
                     /calculated_mol_wt=84531
     Region          21..309
                     /region_name="STKc_IKK_alpha"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha;
                     cd14039"
                     /db_xref="CDD:270941"
     Site            order(21..25,29,42,44,74,95..98,102,104,144,146,148..149,
                     151,165,168,183..186)
                     /site_type="active"
                     /db_xref="CDD:270941"
     Site            order(21..25,29,42,44,74,95..98,102,144,146,148..149,151,
                     165)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270941"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1 and SGK1.
                     /evidence=ECO:0000269|PubMed:10485710,
                     ECO:0000269|PubMed:19088076; propagated from
                     UniProtKB/Swiss-Prot (O15111.2)"
     Site            order(25,102,104,144,146,148,168,183..186)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270941"
     Site            order(108,110,114,117,218,223,251..252,254,260..263)
                     /site_type="other"
                     /note="putative SDD interface [polypeptide binding]"
                     /db_xref="CDD:270941"
     Site            164..186
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270941"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAP3K14.
                     /evidence=ECO:0000269|PubMed:9520446; propagated from
                     UniProtKB/Swiss-Prot (O15111.2)"
     Site            179
                     /site_type="acetylation"
                     /note="(Microbial infection) O-acetylthreonine, by
                     Yersinia YopJ. /evidence=ECO:0000269|PubMed:17116858;
                     propagated from UniProtKB/Swiss-Prot (O15111.2)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by SGK1.
                     /evidence=ECO:0000269|PubMed:19088076; propagated from
                     UniProtKB/Swiss-Prot (O15111.2)"
     Region          311..387
                     /region_name="Ubl_IKKA_like"
                     /note="ubiquitin-like (Ubl) domain found in inhibitor of
                     nuclear factor kappa-B kinases, IKK-alpha and IKK-beta,
                     and similar proteins; cd17046"
                     /db_xref="CDD:340566"
     Region          386..659
                     /region_name="IKBKB_SDD"
                     /note="IQBAL scaffold dimerization domain; pfam18397"
                     /db_xref="CDD:465745"
     Region          455..476
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (O15111.2)"
     Region          707..738
                     /region_name="IKKbetaNEMObind"
                     /note="I-kappa-kinase-beta NEMO binding domain; pfam12179"
                     /db_xref="CDD:463485"
     CDS             1..746
                     /gene="CHUK"
                     /gene_synonym="BPS2; IKBKA; IKK-1; IKK-alpha; IKK1; IKKA;
                     NFKBIKA; TCF16"
                     /coded_by="NM_001441063.1:65..2305"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:1147"
                     /db_xref="HGNC:HGNC:1974"
                     /db_xref="MIM:600664"
ORIGIN      
        1 merppglrpg aggpwemrer lgtggfgnvc lyqhreldlk iaikscrlel stknrerwch
       61 eiqimkklnh anvvkacdvp eelnilihdv pllameycsg gdlrkllnkp enccglkesq
      121 ilsllsdigs girylhenki ihrdlkpeni vlqdvggkii hkiidlgyak dvdqgslcts
      181 fvgtlqylap elfenkpyta tvdywsfgtm vfeciagyrp flhhlqpftw hekikkkdpk
      241 cifaceemsg evrfsshlpq pnslcslvve pmenwlqlml nwdpqqrggp vdltlkqprc
      301 fvlmdhilnl kivhilnmts akiisfllpp deslhslqsr ieretgintg sqellsetgi
      361 sldprkpasq cvldgvrgcd symvylfdks ktvyegpfas rslsdcvnyi vqdskiqlpi
      421 iqlrkvwaea vhyvsglked ysrlfqgqra amlsllryna nltkmkntli sasqqlkakl
      481 effhksiqld leryseqmty gissekmlka wkemeekaih yaevgvigyl edqimslhae
      541 imelqkspyg rrqgdlmesl eqraidlykq lkhrpsdhsy sdstemvkii vhtvqsqdrv
      601 lkelfghlsk llgckqkiid llpkvevals nikeadntvm fmqgkrqkei whllkiactq
      661 ssarslvgss legavtpqts awlpptsaeh dhslscvvtp qdgetsaqmi eenlnclghl
      721 stiiheanee qgnsmmhfic nkfscs
//
LOCUS       NP_001427343             321 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 7 precursor [Homo
            sapiens].
ACCESSION   NP_001427343
VERSION     NP_001427343.1
DBSOURCE    REFSEQ: accession NM_001440414.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 321)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3 and AP004147.3.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.168062.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159931 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..321
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     7 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=33613
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..>302
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            286
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     CDS             1..321
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440414.1:451..1416"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 16"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk aaelgmvsay
      241 ytyiftnlef slqrmdslvd drvnilgfsi fnqshaffqe faqslnqswq encdhvpftg
      301 pagilvtvks ghvalldkwg n
//
LOCUS       NP_001427286             719 aa            linear   PRI 21-NOV-2025
DEFINITION  general transcription and DNA repair factor IIH helicase subunit
            XPD isoform 5 [Homo sapiens].
ACCESSION   NP_001427286
VERSION     NP_001427286.1
DBSOURCE    REFSEQ: accession NM_001440357.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   Barbour,J.A., Ou,T., Yang,H., Fang,H., Yue,N.C., Zhu,X.,
            Wong-Brown,M.W., Wong,Y.T., Bowden,N.A., Wu,S. and Wong,J.W.H.
  TITLE     ERCC2 mutations alter the genomic distribution pattern of somatic
            mutations and are independently prognostic in bladder cancer
  JOURNAL   Cell Genom 4 (8), 100627 (2024)
   PUBMED   39096913
  REMARK    GeneRIF: ERCC2 mutations alter the genomic distribution pattern of
            somatic mutations and are independently prognostic in bladder
            cancer.
REFERENCE   2  (residues 1 to 719)
  AUTHORS   Zeng,W., Xu,W. and Long,W.
  TITLE     The association between XPD rs13181 and rs1799793 polymorphism and
            oral cancer risk: evidence from a meta-analysis
  JOURNAL   BMC Cancer 24 (1), 738 (2024)
   PUBMED   38879503
  REMARK    GeneRIF: The association between XPD rs13181 and rs1799793
            polymorphism and oral cancer risk: evidence from a meta-analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 719)
  AUTHORS   Gudur,A.K., Kale,S.R., Gudur,R.A., Bhosale,S.J. and Datkhile,K.D.
  TITLE     Genetic Polymorphisms of XPC, XPD, XPG Genes and their Association
            with Radiotherapy Induced Toxicity among Head and Neck Cancer
            Patients: A Hospital Based Study from Maharashtra
  JOURNAL   Asian Pac J Cancer Prev 25 (1), 191-199 (2024)
   PUBMED   38285784
  REMARK    GeneRIF: Genetic Polymorphisms of XPC, XPD, XPG Genes and their
            Association with Radiotherapy Induced Toxicity among Head and Neck
            Cancer Patients: A Hospital Based Study from Maharashtra.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 719)
  AUTHORS   Fu,I., Geacintov,N.E. and Broyde,S.
  TITLE     Differing structures and dynamics of two photolesions portray
            verification differences by the human XPD helicase
  JOURNAL   Nucleic Acids Res 51 (22), 12261-12274 (2023)
   PUBMED   37933861
  REMARK    GeneRIF: Differing structures and dynamics of two photolesions
            portray verification differences by the human XPD helicase.
REFERENCE   5  (residues 1 to 719)
  AUTHORS   Sun,G.F. and Ding,H.
  TITLE     NOP2-mediated m5C methylation of XPD is associated with
            hepatocellular carcinoma progression
  JOURNAL   Neoplasma 70 (3), 340-349 (2023)
   PUBMED   37498063
  REMARK    GeneRIF: NOP2-mediated m5C methylation of XPD is associated with
            hepatocellular carcinoma progression.
REFERENCE   6  (residues 1 to 719)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
REFERENCE   7  (residues 1 to 719)
  AUTHORS   Flejter,W.L., McDaniel,L.D., Johns,D., Friedberg,E.C. and
            Schultz,R.A.
  TITLE     Correction of xeroderma pigmentosum complementation group D mutant
            cell phenotypes by chromosome and gene transfer: involvement of the
            human ERCC2 DNA repair gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 261-265 (1992)
   PUBMED   1729695
REFERENCE   8  (residues 1 to 719)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 719)
  AUTHORS   Weber,C.A., Salazar,E.P., Stewart,S.A. and Thompson,L.H.
  TITLE     ERCC2: cDNA cloning and molecular characterization of a human
            nucleotide excision repair gene with high homology to yeast RAD3
  JOURNAL   EMBO J 9 (5), 1437-1447 (1990)
   PUBMED   2184031
REFERENCE   10 (residues 1 to 719)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from L47234.2.
            
            Summary: The nucleotide excision repair pathway is a mechanism to
            repair damage to DNA. The protein encoded by this gene is involved
            in transcription-coupled nucleotide excision repair and is an
            integral member of the basal transcription factor BTF2/TFIIH
            complex. The gene product has ATP-dependent DNA helicase activity
            and belongs to the RAD3/XPD subfamily of helicases. Defects in this
            gene can result in three different disorders, the cancer-prone
            syndrome xeroderma pigmentosum complementation group D,
            trichothiodystrophy, and Cockayne syndrome. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1440426.1,
                                           SRR14038191.1733809.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..719
                     /product="general transcription and DNA repair factor IIH
                     helicase subunit XPD isoform 5"
                     /EC_number="5.6.2.3"
                     /note="xeroderma pigmentosum complementary group D; TFIIH
                     basal transcription factor complex helicase XPD subunit;
                     TFIIH subunit XPD; DNA 5'-3' helicase XPD; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 2; xeroderma pigmentosum group
                     D-complementing protein; TFIIH basal transcription factor
                     complex 80 kDa subunit; BTF2 p80; TFIIH p80; TFIIH 80 kDa
                     subunit; DNA excision repair protein ERCC-2; DNA repair
                     protein complementing XP-D cells; basic transcription
                     factor 2 80 kDa subunit; excision repair
                     cross-complementation group 2; general transcription and
                     DNA repair factor IIH helicase subunit XPD"
                     /calculated_mol_wt=81883
     Region          1..667
                     /region_name="rad3"
                     /note="DNA repair helicase (rad3); TIGR00604"
                     /db_xref="CDD:273169"
     CDS             1..719
                     /gene="ERCC2"
                     /gene_synonym="COFS2; CXPD; EM9; TFIIH; TTD; TTD1; XPD"
                     /coded_by="NM_001440357.1:57..2216"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:2068"
                     /db_xref="HGNC:HGNC:3434"
                     /db_xref="MIM:126340"
ORIGIN      
        1 mpsgtgktvs llalimayqr ayplevtkli ycsrtvpeie kvieelrkll nfyekqegek
       61 lpflglalss rknlcihpev tplrfgkdvd gkchsltasy vraqyqhdts lphcrfyeef
      121 dahgrevplp agiynlddlk algrrqgwcp yflarysilh anvvvysyhy lldpkiadlv
      181 skelarkavv vfdeahnidn vcidsmsvnl trrtldrcqg nletlqktvl riketdeqrl
      241 rdeyrrlveg lreasaaret dahlanpvlp devlqeavpg sirtaehflg flrrlleyvk
      301 wrlrvqhvvq esppaflsgl aqrvciqrkp lrfcaerlrs llhtleitdl adfspltlla
      361 nfatlvstya kgftiiiepf ddrtptianp ilhfscmdas laikpvferf qsviitsgtl
      421 spldiypkil dfhpvtmatf tmtlarvclc pmiigrgndq vaisskfetr ediavirnyg
      481 nlllemsavv pdgivaffts yqymestvas wyeqgileni qrnkllfiet qdgaetsval
      541 ekyqeaceng rgaillsvar gkvsegidfv hhygravimf gvpyvytqsr ilkarleylr
      601 dqfqirendf ltfdamrhaa qcvgrairgk tdyglmvfad krfargdkrg klprwiqehl
      661 tdanlnltvd egvqvakyfl rqmaqpfhre dqlglsllsl eqleseetlk rieqiaqql
//
LOCUS       NP_006717               2863 aa            linear   PRI 21-NOV-2025
DEFINITION  lipopolysaccharide-responsive and beige-like anchor protein isoform
            2 [Homo sapiens].
ACCESSION   NP_006717
VERSION     NP_006717.2
DBSOURCE    REFSEQ: accession NM_006726.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2863)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2863)
  AUTHORS   Szentgyorgyi,V., Lueck,L.M., Overwijn,D., Ritz,D., Zoeller,N.,
            Schmidt,A., Hondele,M., Spang,A. and Bakhtiar,S.
  TITLE     Arf1-dependent LRBA recruitment to Rab4 endosomes is required for
            endolysosome homeostasis
  JOURNAL   J Cell Biol 223 (11) (2024)
   PUBMED   39325073
  REMARK    GeneRIF: Arf1-dependent LRBA recruitment to Rab4 endosomes is
            required for endolysosome homeostasis.
REFERENCE   3  (residues 1 to 2863)
  AUTHORS   Freund,T., Baxter,S.K., Walsh,T., Golan,H., Kapelushnik,J.,
            Abramsohn-Goldenberg,M., Benor,S., Sarid,N., Ram,R., Alcalay,Y.,
            Segel,R., Renbaum,P., Stepensky,P., King,M.C., Torgerson,T.R. and
            Hagin,D.
  TITLE     Clinically Complex LRBA Deficiency Due to a Founder Allele in the
            Georgian Jewish Population
  JOURNAL   J Clin Immunol 43 (1), 151-164 (2023)
   PUBMED   36063261
  REMARK    GeneRIF: Clinically Complex LRBA Deficiency Due to a Founder Allele
            in the Georgian Jewish Population.
REFERENCE   4  (residues 1 to 2863)
  AUTHORS   Catak,M.C., Akcam,B., Bilgic Eltan,S., Babayeva,R., Karakus,I.S.,
            Akgun,G., Baser,D., Bulutoglu,A., Bayram,F., Kasap,N., Kiykim,A.,
            Hancioglu,G., Kokcu Karadag,S.I., Kendir Demirkol,Y., Ozen,S.,
            Cekic,S., Ozcan,D., Edeer Karaca,N., Sasihuseyinoglu,A.S.,
            Cansever,M., Ozek Yucel,E., Tamay,Z., Altintas,D.U., Aydogmus,C.,
            Celmeli,F., Cokugras,H., Gulez,N., Genel,F., Metin,A., Guner,S.N.,
            Kutukculer,N., Keles,S., Reisli,I., Kilic,S.S., Yildiran,A.,
            Karakoc-Aydiner,E., Lo,B., Ozen,A. and Baris,S.
  TITLE     Comparing the levels of CTLA-4-dependent biological defects in
            patients with LRBA deficiency and CTLA-4 insufficiency
  JOURNAL   Allergy 77 (10), 3108-3123 (2022)
   PUBMED   35491430
  REMARK    GeneRIF: Comparing the levels of CTLA-4-dependent biological
            defects in patients with LRBA deficiency and CTLA-4 insufficiency.
REFERENCE   5  (residues 1 to 2863)
  AUTHORS   Yao,J., Gu,H., Mou,W., Chen,Z., Ma,J., Ma,H., Li,N., Zhang,R.,
            Wang,T., Jiang,J. and Wu,R.
  TITLE     Various phenotypes of LRBA gene with compound heterozygous
            variation: A case series report of pediatric cytopenia patients
  JOURNAL   Int J Immunopathol Pharmacol 36, 3946320221125591 (2022)
   PUBMED   36074705
  REMARK    GeneRIF: Various phenotypes of LRBA gene with compound heterozygous
            variation: A case series report of pediatric cytopenia patients.
REFERENCE   6  (residues 1 to 2863)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 2863)
  AUTHORS   Gebauer,D., Li,J., Jogl,G., Shen,Y., Myszka,D.G. and Tong,L.
  TITLE     Crystal structure of the PH-BEACH domains of human LRBA/BGL
  JOURNAL   Biochemistry 43 (47), 14873-14880 (2004)
   PUBMED   15554694
  REMARK    GeneRIF: The crystal structure of the aPH-BEACH domains of LRBA
            were studied.
REFERENCE   8  (residues 1 to 2863)
  AUTHORS   Dyomin,V.G., Chaganti,S.R., Dyomina,K., Palanisamy,N., Murty,V.V.,
            Dalla-Favera,R. and Chaganti,R.S.
  TITLE     BCL8 is a novel, evolutionarily conserved human gene family
            encoding proteins with presumptive protein kinase A anchoring
            function
  JOURNAL   Genomics 80 (2), 158-165 (2002)
   PUBMED   12160729
REFERENCE   9  (residues 1 to 2863)
  AUTHORS   Wang,J.W., Howson,J., Haller,E. and Kerr,W.G.
  TITLE     Identification of a novel lipopolysaccharide-inducible gene with
            key features of both A kinase anchor proteins and chs1/beige
            proteins
  JOURNAL   J Immunol 166 (7), 4586-4595 (2001)
   PUBMED   11254716
REFERENCE   10 (residues 1 to 2863)
  AUTHORS   Feuchter,A.E., Freeman,J.D. and Mager,D.L.
  TITLE     Strategy for detecting cellular transcripts promoted by human
            endogenous long terminal repeats: identification of a novel gene
            (CDC4L) with homology to yeast CDC4
  JOURNAL   Genomics 13 (4), 1237-1246 (1992)
   PUBMED   1505956
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079794.6, AC104796.4,
            AC092544.4, AC110813.4, AC097373.3, AC092612.3 and AC093748.3.
            
            On May 23, 2007 this sequence version replaced NP_006717.1.
            
            Summary: The protein encoded by this gene is a member of the
            WDL-BEACH-WD (WBW) gene family. Its expression is induced in B
            cells and macrophages by bacterial lipopolysaccharides (LPS). The
            encoded protein associates with protein kinase A and may be
            involved in leading intracellular vesicles to activated receptor
            complexes, which aids in the secretion and/or membrane deposition
            of immune effector molecules. Defects in this gene are associated
            with the disorder common variable immunodeficiency-8 with
            autoimmunity. Two transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (2) encodes the longer isoform
            (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF216648.2, SRR14038197.1297637.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2863
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.3"
     Protein         1..2863
                     /product="lipopolysaccharide-responsive and beige-like
                     anchor protein isoform 2"
                     /note="vesicle trafficking, beach and anchor containing;
                     lipopolysaccharide-responsive and beige-like anchor
                     protein; CDC4-like protein; LPS-responsive vesicle
                     trafficking, beach and anchor containing"
                     /calculated_mol_wt=318978
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          229..376
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
     Region          441..921
                     /region_name="DUF4704"
                     /note="Neurobeachin/BDCP, DUF4704 alpha solenoid region;
                     pfam15787"
                     /db_xref="CDD:464870"
     Region          969..1005
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            979
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1003
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1018..1039
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1161..1193
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1301..1343
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1531..1548
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          1586..1668
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1759..1789
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1770
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1880..2058
                     /region_name="DUF1088"
                     /note="Neurobeachin-like, DUF1088; pfam06469"
                     /db_xref="CDD:461925"
     Site            2064
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          2084..2181
                     /region_name="PH_BEACH"
                     /note="PH domain associated with Beige/BEACH; pfam14844"
                     /db_xref="CDD:434260"
     Region          2212..2489
                     /region_name="Beach"
                     /note="Beige/BEACH domain; smart01026"
                     /db_xref="CDD:214982"
     Site            2496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          2584..2848
                     /region_name="NBCH_WD40"
                     /note="Neurobeachin beta propeller domain; pfam20426"
                     /db_xref="CDD:466575"
     Region          2591..2633
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2600..2636
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2636..2679
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2642..2695
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2695..2735
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2700..2735
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2740..2769
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2777..2816
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2782..2816
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2819..2858
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     CDS             1..2863
                     /gene="LRBA"
                     /gene_synonym="BGL; CDC4L; CVID8; LAB300; LBA; uc.147"
                     /coded_by="NM_006726.5:475..9066"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3773.1"
                     /db_xref="GeneID:987"
                     /db_xref="HGNC:HGNC:1742"
                     /db_xref="MIM:606453"
ORIGIN      
        1 masednrvps ppptgddggg ggreetpteg galslkpglp irgirmkfav ltglvevgev
       61 snrdivetvf nllvggqfdl emnfiiqege sincmvdlle kcditcqaev wsmftailkk
      121 sirnlqvcte vglvekvlgk iekvdnmiad llvdmlgvla synltvrelk lffsklqgdk
      181 grwpphagkl lsvlkhmpqk ygpdaffnfp gksaaaialp piakwpyqng ftfhtwlrmd
      241 pvnninvdkd kpylycfrts kglgysahfv ggclivtsik skgkgfqhcv kfdfkpqkwy
      301 mvtivhiynr wknselrcyv ngelasygei twfvntsdtf dkcflgsset adanrvfcgq
      361 mtavylfsea lnaaqifaiy qlglgykgtf kfkaesdlfl aehhklllyd gklssaiaft
      421 ynpratdaql clesspkdnp sifvhsphal mlqdvkavlt hsiqsamhsi ggvqvlfplf
      481 aqldyrqyls deidlticst llafimellk nsiamqeqml ackgflvigy sleksskshv
      541 sravlelcla fskylsnlqn gmpllkqlcd hvllnpaiwi htpakvqlml ytylstefig
      601 tvniyntirr vgtvllimht lkyyywavnp qdrsgitpkg ldgprpnqke mlslrafllm
      661 fikqlvmkds gvkedelqai lnylltmhed dnlmdvlqll valmsehpns mipafdqrng
      721 lrviykllas ksegirvqal kamgyflkhl apkrkaevml ghglfsllae rlmlqtnlit
      781 mttynvlfei lieqigtqvi hkqhpdpdss vkiqnpqilk viatllrnsp qcpesmevrr
      841 aflsdmiklf nnsrenrrsl lqcsvwqewm lslcyfnpkn sdeqkitemv yaifrillyh
      901 avkyewggwr vwvdtlsith skvtfeihke nlanifreqq gkvdeeiglc sstsvqaasg
      961 irrdinvsvg sqqpdtkdsp vcphfttngn enssiektss lesasnielq ttntsyeemk
     1021 aeqenqelpd egtleetltn etrnaddlev ssdiieavai ssnsfittgk dsmtvsevta
     1081 sisspseeda sempefldks iveeeedddy velkvegspt eeanlptelq dnslspaase
     1141 agekldmfgn ddklifqegk pvtekqtdte tqdskdsgiq tmtasgssam spettvsqia
     1201 vesdlgqmle egkkatnltr etklindchg svseasseqk iakldvsnva tdterlelka
     1261 spnveapqph rhvleisrqh eqpgqgiapd avngqrrdsr stvfripefn wsqmhqrllt
     1321 dllfsietdi qmwrshstkt vmdfvnssdn vifvhntihl isqvmdnmvm acggilplls
     1381 aatsathele nieptqglsi easvtflqrl islvdvlifa sslgfteiea eksmssggil
     1441 rqclrlvcav avrnclecqq hsqlktrgdk alkpmhslip lgksaakspv divtggispv
     1501 rdldrllqdm dinrlravvf rdiedskqaq flalavvyfi svlmvskyrd ilepqnerhs
     1561 qsctetgsen envslseitp aafstlttas veesestssa rrrdsgigee tatglgshve
     1621 vtphtappgv sagpdaisev lstlslevnk spetkndrgn dldtkatpsv svsknvnvkd
     1681 ilrslvnipa dgvtvdpall ppaclgalgd lsveqpvqfr sfdrsvivaa kksavspstf
     1741 ntsiptnavs vvssvdsaqa sdmggespgs rssnaklpsv ptvdsvsqdp vsnmsiterl
     1801 ehalekaapl lreifvdfap flsrtllgsh gqelliegts lvcmkssssv velvmllcsq
     1861 ewqnsiqkna glafielvne grllsqtmkd hlvrvaneae filsrqraed ihrhaefesl
     1921 caqysadkre dekmcdhlir aakyrdhvta tqliqkiini ltdkhgawgn savsrplefw
     1981 rldyweddlr rrrrfvrnpl gsthpeatlk tavehvcifk lrenskatde dilakgkqsi
     2041 rsqalgnqns eneillegdd dtlssvdekd lenlagpvsl stpaqlvaps vvvkgtlsvt
     2101 sselyfevde edpnfkkidp kilayteglh gkwlfteirs ifsrryllqn taleifmanr
     2161 vavmfnfpdp atvkkvvnyl prvgvgtsfg lpqtrrisla sprqlfkasn mtqrwqhrei
     2221 snfeylmfln tiagrsyndl nqypvfpwvi tnyeseeldl tlptnfrdls kpigalnpkr
     2281 aaffaeryes weddqvpkfh ygthystasf vlawllriep fttyflnlqg gkfdhadrtf
     2341 ssisrawrns qrdtsdikel ipefyylpem fvnfnnynlg vmddgtvvsd velppwakts
     2401 eefvhinrla lesefvscql hqwidlifgy kqqgpeavra lnvfyyltye gavnlnsitd
     2461 pvlreaveaq irsfgqtpsq lliephpprg samqvsplmf tdkaqqdvim vlkfpsnspv
     2521 thvaantqpg latpavitvt anrlfavnkw hnlpahqgav qdqpyqlpve idpliasntg
     2581 mhrrqitdll dqsiqvhsqc fvitsdnryi lvcgfwdksf rvystdtgrl iqvvfghwdv
     2641 vtclarsesy iggncyilsg srdatlllwy wngkcsgigd npgsetaapr ailtghdyev
     2701 tcaavcaelg lvlsgsqegp clihsmngdl lrtlegpenc lkpkliqasr eghcvifyen
     2761 glfctfsvng klqatmetdd niraiqlsrd gqylltggdr gvvvvrqvsd lkqlfaypgc
     2821 dagiramals ydqrciisgm asgsivlfyn dfnrwhheyq try
//
LOCUS       NP_001425136            1737 aa            linear   PRI 21-NOV-2025
DEFINITION  BCL-6 corepressor isoform e [Homo sapiens].
ACCESSION   NP_001425136 XP_047298158 XP_054183281
VERSION     NP_001425136.1
DBSOURCE    REFSEQ: accession NM_001438207.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1737)
  AUTHORS   Batkova,M., Havlovicova,M., Nocar,A., Dudakova,L., Macek,M.,
            Liskova,P. and Dostalova,T.
  TITLE     Dental abnormalities observed in the oculo-facio-cardio-dental
            (OFCD) syndrome present in two Czech families bearing novel de novo
            BCOR pathogenic variants
  JOURNAL   BMC Oral Health 24 (1), 1264 (2024)
   PUBMED   39438869
  REMARK    GeneRIF: Dental abnormalities observed in the
            oculo-facio-cardio-dental (OFCD) syndrome present in two Czech
            families bearing novel de novo BCOR pathogenic variants.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1737)
  AUTHORS   Giner,F., Medina-Ceballos,E., Lopez-Reig,R., Machado,I.,
            Lopez-Guerrero,J.A., Navarro,S., Rubio-Martinez,L.A., Espino,M.,
            Mayordomo-Aranda,E. and Llombart-Bosch,A.
  TITLE     The Combined Immunohistochemical Expression of GLI1 and BCOR in
            Synovial Sarcomas for the Identification of Three Risk Groups and
            Their Prognostic Outcomes: A Study of 52 Patients
  JOURNAL   Int J Mol Sci 25 (14), 7615 (2024)
   PUBMED   39062853
  REMARK    GeneRIF: The Combined Immunohistochemical Expression of GLI1 and
            BCOR in Synovial Sarcomas for the Identification of Three Risk
            Groups and Their Prognostic Outcomes: A Study of 52 Patients.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1737)
  AUTHORS   Mavridou,E., Lema Fernandez,A.G., Nardelli,C., Pierini,V.,
            Quintini,M., Arniani,S., Di Giacomo,D., Crescenzi,B., Matteucci,C.,
            Sambani,C. and Mecucci,C.
  TITLE     A novel t(X;21)(p11.4;q22.12) translocation adds to the role of
            BCOR and RUNX1 in myelodysplastic syndromes and acute myeloid
            leukemias
  JOURNAL   Genes Chromosomes Cancer 63 (4), e23235 (2024)
   PUBMED   38656651
  REMARK    GeneRIF: A novel t(X;21)(p11.4;q22.12) translocation adds to the
            role of BCOR and RUNX1 in myelodysplastic syndromes and acute
            myeloid leukemias.
REFERENCE   4  (residues 1 to 1737)
  AUTHORS   Pierron,G., Tirode,F., Lucchesi,C., Reynaud,S., Ballet,S.,
            Cohen-Gogo,S., Perrin,V., Coindre,J.M. and Delattre,O.
  TITLE     A new subtype of bone sarcoma defined by BCOR-CCNB3 gene fusion
  JOURNAL   Nat Genet 44 (4), 461-466 (2012)
   PUBMED   22387997
  REMARK    GeneRIF: A new fusion was observed between BCOR (encoding the BCL6
            co-repressor) and CCNB3 (encoding the testis-specific cyclin B3) on
            the X chromosome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1737)
  AUTHORS   Tomsig,J.L., Snyder,S.L. and Creutz,C.E.
  TITLE     Identification of targets for calcium signaling through the copine
            family of proteins. Characterization of a coiled-coil
            copine-binding motif
  JOURNAL   J Biol Chem 278 (12), 10048-10054 (2003)
   PUBMED   12522145
REFERENCE   6  (residues 1 to 1737)
  AUTHORS   Ng,D., Hadley,D.W., Tifft,C.J. and Biesecker,L.G.
  TITLE     Genetic heterogeneity of syndromic X-linked recessive
            microphthalmia-anophthalmia: is Lenz microphthalmia a single
            disorder?
  JOURNAL   Am J Med Genet 110 (4), 308-314 (2002)
   PUBMED   12116202
REFERENCE   7  (residues 1 to 1737)
  AUTHORS   Tang,T.T., Dowbenko,D., Jackson,A., Toney,L., Lewin,D.A., Dent,A.L.
            and Lasky,L.A.
  TITLE     The forkhead transcription factor AFX activates apoptosis by
            induction of the BCL-6 transcriptional repressor
  JOURNAL   J Biol Chem 277 (16), 14255-14265 (2002)
   PUBMED   11777915
  REMARK    GeneRIF: The forkhead transcription factor AFX activates apoptosis
            by induction of the BCL-6 transcriptional repressor.
REFERENCE   8  (residues 1 to 1737)
  AUTHORS   Huynh,K.D., Fischle,W., Verdin,E. and Bardwell,V.J.
  TITLE     BCoR, a novel corepressor involved in BCL-6 repression
  JOURNAL   Genes Dev 14 (14), 1810-1823 (2000)
   PUBMED   10898795
  REMARK    GeneRIF: Function:BCoR is a transcriptional corepressor for BCL-6.
            Nomenclature:BCoR (BCL-6 corepressor)
REFERENCE   9  (residues 1 to 1737)
  AUTHORS   Ng,D.
  TITLE     Lenz Microphthalmia Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301694
REFERENCE   10 (residues 1 to 1737)
  AUTHORS   Bardakjian,T., Weiss,A. and Schneider,A.
  TITLE     Microphthalmia/Anophthalmia/Coloboma Spectrum - RETIRED CHAPTER,
            FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301552
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091806.4 and AC092198.5.
            
            On or before Apr 16, 2025 this sequence version replaced
            XP_047298158.1, XP_054183281.1.
            
            Summary: The protein encoded by this gene was identified as an
            interacting corepressor of BCL6, a POZ/zinc finger transcription
            repressor that is required for germinal center formation and may
            influence apoptosis. This protein selectively interacts with the
            POZ domain of BCL6, but not with eight other POZ proteins. Specific
            class I and II histone deacetylases (HDACs) have been shown to
            interact with this protein, which suggests a possible link between
            the two classes of HDACs. Several transcript variants encoding
            different isoforms have been found for this gene. A pseudogene of
            this gene is found on chromosome Y.[provided by RefSeq, Jun 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.6148.1,
                                           SRR14038197.2650723.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1737
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.4"
     Protein         1..1737
                     /product="BCL-6 corepressor isoform e"
                     /note="BCL-6 interacting corepressor; BCL6 interacting
                     corepressor; BCL-6 coreceptor"
                     /calculated_mol_wt=190091
     Region          <257..673
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          309..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          388..438
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            392
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          498..514
                     /region_name="Interaction with BCL6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          557..641
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          737..760
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          773..794
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          815..844
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1053..1169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGN4; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1184..1396
                     /region_name="BCOR"
                     /note="BCL-6 co-repressor, non-ankyrin-repeat region;
                     pfam15808"
                     /db_xref="CDD:434953"
     Region          1202..1310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGN4; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1412..1433
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          <1443..1575
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1444..1477
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1445..1476
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1446,1450..1451,1454..1456,1458..1459,1463,1466,
                     1476,1478,1480,1484..1485,1488..1490,1492..1493,1497,1500,
                     1509,1511,1513,1517..1518,1521..1523,1525..1526,1530,1533)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1478..1509
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1478..1507
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1511..1540
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1511..1540
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1616..1730
                     /region_name="Necessary and sufficient for interaction
                     with PCGF1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1616..1729
                     /region_name="PUFD"
                     /note="BCORL-PCGF1-binding domain; pfam16553"
                     /db_xref="CDD:465171"
     Site            order(1618..1619,1621..1625,1627..1629,1631,1633,1642,
                     1644,1686..1688,1690..1691,1693..1694,1711,1722,1724,
                     1726..1728)
                     /site_type="other"
                     /note="RAWUL domain interface [polypeptide binding]"
                     /db_xref="CDD:271224"
     CDS             1..1737
                     /gene="BCOR"
                     /gene_synonym="ANOP2; MAA2; MCOPS2"
                     /coded_by="NM_001438207.1:312..5525"
                     /note="isoform e is encoded by transcript variant 9"
                     /db_xref="GeneID:54880"
                     /db_xref="HGNC:HGNC:20893"
                     /db_xref="MIM:300485"
ORIGIN      
        1 mlsatplygn vhswmnserv rmcgasedrk ilvndgdask arlelreenp lnhnvvdast
       61 ahridglaal smdrtglire glrvpgnivy sslcglgsek greaatstlg glgfssernp
      121 emqfkpntpe tveasavsgk ppngfsaiyk tppgiqksav ataealgldr pasdkqspln
      181 ingasylrlp wvnpymegat paiypfldsp nkyslnmyka llpqqsysla qplyspvctn
      241 gerflylppp hyvgphipss laspmrlstp saspaipplv hcadkslpwk mgvspgnpvd
      301 shayphiqns kqprvpsaka vtsglpgdta lllppsprps prvhlptqpa adtysefhkh
      361 yaristspsv alskpymtvs sefpaarlsn gkypkapegg egaqpvpgha rktavqdrkd
      421 gssppllekq tvtkdvtdkp ldlsskvvdv daskadhmkk maptvlvhsr agsglvlsgs
      481 eipketlspp gngcaiyrse iistapsswv vpgpspneen ngksmslknk aldwaipqqr
      541 ssscprmggt davitnvsgs vssagrpasa spapnanadg tktsrssvet tpsviqhvgq
      601 ppatpakhss stsskgakas npepsfkane nglppssifl spneafrspp ipyprsylpy
      661 papegiavsp lslhgkgpvy phpvllpngs lfpghlapkp glpyglptgr pefvtyqdal
      721 glgmvhpmli phtpieitke ekperrsrsh eraryedptl rnrfseilet sstklhpdvp
      781 tdknlkpnpn wnqgktvvks dklvyvdllr eepdaktdtn vskpsfaaes vgqsaeppkp
      841 svepalqqhr dfialreelg risdfhetyt fkqpvftvsk dsvlagtnke nlglpvstpf
      901 lepplgsdgp avtfgktqed pkpfcvgsap psvdvtptyt kdgadeaesn dgkvlkpkps
      961 klakriansa gyvgdrfkcv ttelyadssq lsreqralqr ammrfselem keregghpat
     1021 kdsemckfsp adwerlkgnq dkkpksvtle eaiaeqnese rceysvgnkh rdpfeapedk
     1081 dlpvekyfve rqpvseppad qvasdmphsp tlrvdrkrkv sgdsshtett aeevpedpll
     1141 kakrrrvskd dwperemtns ssnhledphy seltnlkvci eltglhpkkq rhllhlrerw
     1201 eqqvsaadgk pgrqsrkevt qatqpeaipq gtniteekpg rkraeakgnr swseeslkps
     1261 dneqglpvfs gsppmkslss tsaggkkqaq pscapasrpp akqqkikenq ktdvlcadee
     1321 edcqaasllq kytdnsekps gkrlcktkhl ipqesrrglp ltgeyyvena dgkvtvrrfr
     1381 krpepssdyd lspakqepkp fdrlqqllpa sqstqlpcss spqettqsrp mppearrliv
     1441 nknagetllq raarlgyeev vlyclenkic dvnhrdnagy calheacarg wlnivrhlle
     1501 ygadvncsaq dgtrplhdav endhleivrl llsygadptl atysgrtimk mthselmekf
     1561 ltdylndlqg rndddasgtw dfygssvcep ddesgydvla nppgpedqdd dddaysdvfe
     1621 fefsetpllp cyniqvsvaq gprnwlllsd vlkklkmssr ifrcnfpnve ivtiaeaefy
     1681 rqvsasllfs cskdleafnp eskelldlve ftneiqtllg ssvewlhpsd lasdnyw
//
LOCUS       NP_001415239             326 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb complex protein BMI-1 [Homo sapiens].
ACCESSION   NP_001415239
VERSION     NP_001415239.1
DBSOURCE    REFSEQ: accession NM_001428310.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Szustka,A. and Krzeslak,A.
  TITLE     BMI-1 in Breast Cancer - Biological Role and Clinical Implications
  JOURNAL   Cell Physiol Biochem 58 (5), 584-596 (2024)
   PUBMED   39429016
  REMARK    GeneRIF: BMI-1 in Breast Cancer - Biological Role and Clinical
            Implications.
            Review article
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Hsu,Y.C., Luo,C.W., Chang,S.J., Lai,C.Y., Yang,Y.T., Chen,Y.Z.,
            Liu,W.T., Wu,C.C., Sun,C.K., Hou,M.F. and Pan,M.R.
  TITLE     Targeting Bmi1 for Enhancing Anoikis Sensitivity and Inhibiting
            Metastasis in Colorectal Cancer
  JOURNAL   Cancer Genomics Proteomics 21 (5), 523-532 (2024)
   PUBMED   39191496
  REMARK    GeneRIF: Targeting Bmi1 for Enhancing Anoikis Sensitivity and
            Inhibiting Metastasis in Colorectal Cancer.
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Li,Q., Fu,T., Wei,N., Wang,Q. and Zhang,X.
  TITLE     Bmi-1 promotes the proliferation, migration and invasion, and
            inhibits cell apoptosis of human retinoblastoma cells via RKIP
  JOURNAL   Sci Rep 14 (1), 14544 (2024)
   PUBMED   38914697
  REMARK    GeneRIF: Bmi-1 promotes the proliferation, migration and invasion,
            and inhibits cell apoptosis of human retinoblastoma cells via RKIP.
            Erratum:[Sci Rep. 2025 Aug 5;15(1):28521. doi:
            10.1038/s41598-025-11879-x. PMID: 40764337]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Park,I.K., Qian,D., Kiel,M., Becker,M.W., Pihalja,M.,
            Weissman,I.L., Morrison,S.J. and Clarke,M.F.
  TITLE     Bmi-1 is required for maintenance of adult self-renewing
            haematopoietic stem cells
  JOURNAL   Nature 423 (6937), 302-305 (2003)
   PUBMED   12714971
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Satijn,D.P. and Otte,A.P.
  TITLE     RING1 interacts with multiple Polycomb-group proteins and displays
            tumorigenic activity
  JOURNAL   Mol Cell Biol 19 (1), 57-68 (1999)
   PUBMED   9858531
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Alkema,M.J., Jacobs,J., Voncken,J.W., Jenkins,N.A., Copeland,N.G.,
            Satijn,D.P., Otte,A.P., Berns,A. and van Lohuizen,M.
  TITLE     MPc2, a new murine homolog of the Drosophila polycomb protein is a
            member of the mouse polycomb transcriptional repressor complex
  JOURNAL   J Mol Biol 273 (5), 993-1003 (1997)
   PUBMED   9367786
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Alkema,M.J., Bronk,M., Verhoeven,E., Otte,A., van 't Veer,L.J.,
            Berns,A. and van Lohuizen,M.
  TITLE     Identification of Bmi1-interacting proteins as constituents of a
            multimeric mammalian polycomb complex
  JOURNAL   Genes Dev 11 (2), 226-240 (1997)
   PUBMED   9009205
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Alkema,M.J., Wiegant,J., Raap,A.K., Berns,A. and van Lohuizen,M.
  TITLE     Characterization and chromosomal localization of the human
            proto-oncogene BMI-1
  JOURNAL   Hum Mol Genet 2 (10), 1597-1603 (1993)
   PUBMED   8268912
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158211.29.
            
            Summary: This gene encodes a ring finger protein that is major
            component of the polycomb group complex 1 (PRC1). This complex
            functions through chromatin remodeling as an essential epigenetic
            repressor of multiple regulatory genes involved in embryonic
            development and self-renewal in somatic stem cells. This protein
            also plays a central role in DNA damage repair. This gene is an
            oncogene and aberrant expression is associated with numerous
            cancers and is associated with resistance to certain
            chemotherapies. A pseudogene of this gene is found on chromosome X.
            Read-through transcription also exists between this gene and the
            upstream COMM domain containing 3 (COMMD3) gene. [provided by
            RefSeq, Sep 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.926852.1,
                                           SRR11853561.3349.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.2"
     Protein         1..326
                     /product="polycomb complex protein BMI-1"
                     /note="murine leukemia viral (bmi-1) oncogene homolog; B
                     lymphoma Mo-MLV insertion region 1 homolog; ring finger
                     protein 51; polycomb group protein Bmi1; polycomb group
                     RING finger protein 4; BMI1 polycomb ring finger oncogene;
                     BMI1 polycomb ring finger proto-oncogene"
                     /calculated_mol_wt=36818
     Region          5..101
                     /region_name="RING-HC_PCGF4"
                     /note="RING finger found in polycomb group RING finger
                     protein 4 (PCGF4) and similar proteins; cd16736"
                     /db_xref="CDD:438394"
     Site            order(5..13,15,17,21,23..24,26..27,29..30,32..36,39..42,
                     44..45,66,69..72,74,78,81..82,84,86,89..90,93..94,97)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438394"
     Region          81..95
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     Region          130..226
                     /region_name="RAWUL_PCGF4"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in polycomb group RING finger protein
                     4 (PCGF4); cd17165"
                     /db_xref="CDD:340685"
     Region          162..182
                     /region_name="Interaction with PHC2.
                     /evidence=ECO:0000269|PubMed:27827373"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     Region          164..228
                     /region_name="Interaction with E4F1.
                     /evidence=ECO:0000269|PubMed:16882984"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     Region          236..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     CDS             1..326
                     /gene="BMI1"
                     /gene_synonym="flvi-2/bmi-1; FLVI2/BMI1; PCGF4; RNF51"
                     /coded_by="NM_001428310.1:119..1099"
                     /db_xref="GeneID:648"
                     /db_xref="HGNC:HGNC:1066"
                     /db_xref="MIM:164831"
ORIGIN      
        1 mhrttrikit elnphlmcvl cggyfidatt iieclhsfck tcivrylets kycpicdvqv
       61 hktrpllnir sdktlqdivy klvpglfkne mkrrrdfyaa hpsadaangs nedrgevade
      121 dkriitddei islsieffdq nrldrkvnkd kekskeevnd krylrcpaam tvmhlrkflr
      181 skmdipntfq idvmyeeepl kdyytlmdia yiytwrrngp lplkyrvrpt ckrmkishqr
      241 dgltnagele sdsgsdkans paggipstss clpspstpvq sphpqfphis stmngtsnsp
      301 sgnhqssfan rprkssvngs satssg
//
LOCUS       NP_001400009             333 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001400009
VERSION     NP_001400009.1
DBSOURCE    REFSEQ: accession NM_001413080.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2308711.1,
                                           SRR14038196.93278.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..333
                     /product="mitochondrial fission regulator 1 isoform 1
                     precursor"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=31469
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=5550
     Region          22..251
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     mat_peptide     49..333
                     /product="Mitochondrial fission regulator 1.
                     /id=PRO_0000096622"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=31469
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15390.2)"
     Region          177..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          179..304
                     /region_name="Necessary and sufficient to promote
                     mitochondrial fission. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          288..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     CDS             1..333
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001413080.1:432..1433"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 15"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsvlwsrkpy gssrsivrki gtnlsliqcp rvqfqinsha
       61 tewspshpge davasfadvg wvakeegecs arlrtevrsr pplqddllff ekapsrqisl
      121 pdlsqeepql ktpalaneea lqkicalene laalraqiak ivtqqeqqnl tagdldsttf
      181 gtipphpppp ppplpppalg lhqstsavdl ikerrekran agktlvknnp kkpempnmle
      241 ilkemnsvkl rsvkrseqdv kpkpvdatdp aaliaealkk kfayryrsds qdevekgipk
      301 seseatserv lfgphmlkpt gkmkalienv sds
//
LOCUS       NP_001400236             280 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 3 [Homo sapiens].
ACCESSION   NP_001400236
VERSION     NP_001400236.1
DBSOURCE    REFSEQ: accession NM_001413307.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 280)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 280)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 280)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC103816.2, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.34170.1,
                                           SRR1803617.161536.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..280
                     /product="RNA-binding Raly-like protein isoform 3"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=30943
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          188..>233
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     CDS             1..280
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413307.1:1313..2155"
                     /note="isoform 3 is encoded by transcript variant 34"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly sgyvfdydyy
      121 rddfynrlfd yhgrvppppr aviplkrprv avtttrrgkg vfsmkggsrs tasgstgskl
      181 ksdelqtikk eltqiktkid sllgrlekie kqqkaeaeaq kkqleeslvl iqeecvseia
      241 dhsteepaeg gpdadgeemt dgieedfded gghelflqik
//
LOCUS       NP_001397811             574 aa            linear   PRI 21-NOV-2025
DEFINITION  voltage-dependent L-type calcium channel subunit beta-2 isoform 11
            [Homo sapiens].
ACCESSION   NP_001397811 XP_005252645
VERSION     NP_001397811.1
DBSOURCE    REFSEQ: accession NM_001410882.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Zhong,R., Zhang,F., Yang,Z., Li,Y., Xu,Q., Lan,H., Cyganek,L.,
            El-Battrawy,I., Zhou,X., Akin,I. and Borggrefe,M.
  TITLE     Epigenetic mechanism of L-type calcium channel beta-subunit
            downregulation in short QT human induced pluripotent stem
            cell-derived cardiomyocytes with CACNB2 mutation
  JOURNAL   Europace 24 (12), 2028-2036 (2022)
   PUBMED   35894107
  REMARK    GeneRIF: Epigenetic mechanism of L-type calcium channel
            beta-subunit downregulation in short QT human induced pluripotent
            stem cell-derived cardiomyocytes with CACNB2 mutation.
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Xin,Q., Xin,G., Li,L., Sun,W., Jiang,W., Wang,J., Luan,Y.,
            Zhang,Y., Cheng,L., Duan,S., Hong,F., Ji,Q. and Ma,W.
  TITLE     Association study of hypertension susceptibility genes ITGA9,
            MOV10, and CACNB2 with preeclampsia in Chinese Han population
  JOURNAL   J Matern Fetal Neonatal Med 35 (25), 5227-5235 (2022)
   PUBMED   33491517
  REMARK    GeneRIF: Association study of hypertension susceptibility genes
            ITGA9, MOV10, and CACNB2 with preeclampsia in Chinese Han
            population.
REFERENCE   3  (residues 1 to 574)
  AUTHORS   Martins,H.C., Gilardi,C., Sungur,A.O., Winterer,J., Pelzl,M.A.,
            Bicker,S., Gross,F., Kisko,T.M., Malikowska-Racia,N., Braun,M.D.,
            Brosch,K., Nenadic,I., Stein,F., Meinert,S., Schwarting,R.K.W.,
            Dannlowski,U., Kircher,T., Wohr,M. and Schratt,G.
  TITLE     Bipolar-associated miR-499-5p controls neuroplasticity by
            downregulating the Cav1.2 subunit CACNB2
  JOURNAL   EMBO Rep 23 (10), e54420 (2022)
   PUBMED   35969184
  REMARK    GeneRIF: Bipolar-associated miR-499-5p controls neuroplasticity by
            downregulating the Cav1.2 subunit CACNB2.
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Zhong,R., Schimanski,T., Zhang,F., Lan,H., Hohn,A., Xu,Q.,
            Huang,M., Liao,Z., Qiao,L., Yang,Z., Li,Y., Zhao,Z., Li,X.,
            Rose,L., Albers,S., Maywald,L., Muller,J., Dinkel,H., Saguner,A.,
            Janssen,J.W.G., Swamy,N., Xi,Y., Lang,S., Kleinsorge,M., Duru,F.,
            Zhou,X., Diecke,S., Cyganek,L., Akin,I. and El-Battrawy,I.
  TITLE     A Preclinical Study on Brugada Syndrome with a CACNB2 Variant Using
            Human Cardiomyocytes from Induced Pluripotent Stem Cells
  JOURNAL   Int J Mol Sci 23 (15), 8313 (2022)
   PUBMED   35955449
  REMARK    GeneRIF: A Preclinical Study on Brugada Syndrome with a CACNB2
            Variant Using Human Cardiomyocytes from Induced Pluripotent Stem
            Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 574)
  AUTHORS   Westhoff,M. and Dixon,R.E.
  TITLE     Mechanisms and Regulation of Cardiac CaV1.2 Trafficking
  JOURNAL   Int J Mol Sci 22 (11), 5927 (2021)
   PUBMED   34072954
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 574)
  AUTHORS   Brust,P.F., Simerson,S., McCue,A.F., Deal,C.R., Schoonmaker,S.,
            Williams,M.E., Velicelebi,G., Johnson,E.C., Harpold,M.M. and
            Ellis,S.B.
  TITLE     Human neuronal voltage-dependent calcium channels: studies on
            subunit structure and role in channel assembly
  JOURNAL   Neuropharmacology 32 (11), 1089-1102 (1993)
   PUBMED   8107964
REFERENCE   7  (residues 1 to 574)
  AUTHORS   Rosenfeld,M.R., Wong,E., Dalmau,J., Manley,G., Egan,D.,
            Posner,J.B., Sher,E. and Furneaux,H.M.
  TITLE     Sera from patients with Lambert-Eaton myasthenic syndrome recognize
            the beta-subunit of Ca2+ channel complexes
  JOURNAL   Ann N Y Acad Sci 681, 408-411 (1993)
   PUBMED   8395157
REFERENCE   8  (residues 1 to 574)
  AUTHORS   Rosenfeld,M.R., Wong,E., Dalmau,J., Manley,G., Posner,J.B., Sher,E.
            and Furneaux,H.M.
  TITLE     Cloning and characterization of a Lambert-Eaton myasthenic syndrome
            antigen
  JOURNAL   Ann Neurol 33 (1), 113-120 (1993)
   PUBMED   8494331
REFERENCE   9  (residues 1 to 574)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   10 (residues 1 to 574)
  AUTHORS   Williams,M.E., Feldman,D.H., McCue,A.F., Brenner,R., Velicelebi,G.,
            Ellis,S.B. and Harpold,M.M.
  TITLE     Structure and functional expression of alpha 1, alpha 2, and beta
            subunits of a novel human neuronal calcium channel subtype
  JOURNAL   Neuron 8 (1), 71-84 (1992)
   PUBMED   1309651
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139814.13, AL450364.12 and
            AL450384.34.
            
            On Aug 17, 2022 this sequence version replaced XP_005252645.1.
            
            Summary: This gene encodes a subunit of a voltage-dependent calcium
            channel protein that is a member of the voltage-gated calcium
            channel superfamily. The gene product was originally identified as
            an antigen target in Lambert-Eaton myasthenic syndrome, an
            autoimmune disorder. Mutations in this gene are associated with
            Brugada syndrome. Alternatively spliced variants encoding different
            isoforms have been described. [provided by RefSeq, Feb 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293937.1, SRR1660807.188352.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.33-p12.31"
     Protein         1..574
                     /product="voltage-dependent L-type calcium channel subunit
                     beta-2 isoform 11"
                     /note="voltage-dependent L-type calcium channel subunit
                     beta-2; myasthenic (Lambert-Eaton) syndrome antigen B;
                     lambert-Eaton myasthenic syndrome antigen B; calcium
                     channel voltage-dependent subunit beta 2; calcium channel,
                     voltage-dependent, beta 2 subunit"
                     /calculated_mol_wt=64575
     Region          24..65
                     /region_name="VGCC_beta4Aa_N"
                     /note="Voltage gated calcium channel subunit beta domain
                     4Aa N terminal; pfam12052"
                     /db_xref="CDD:463445"
     Region          64..132
                     /region_name="SH3_CACNB2"
                     /note="Src Homology 3 domain of Voltage-dependent L-type
                     calcium channel subunit beta2; cd12040"
                     /db_xref="CDD:212973"
     Site            order(75,77,80,91,109..110,126,128..129)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212973"
     Region          194..374
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     Region          <452..>545
                     /region_name="Innate_immun"
                     /note="Invertebrate innate immunity transcript family;
                     pfam12782"
                     /db_xref="CDD:432781"
     CDS             1..574
                     /gene="CACNB2"
                     /gene_synonym="CAB2; CACNLB2; CAVB2; MYSB"
                     /coded_by="NM_001410882.1:458..2182"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS91220.1"
                     /db_xref="GeneID:783"
                     /db_xref="HGNC:HGNC:1402"
                     /db_xref="MIM:600003"
ORIGIN      
        1 mkatwirllk rakggrlkns dicgsadsyt srpsdsdvsl eedreavrre aerqaqaqle
       61 kaktkpvafa vrtnvsysaa heddvpvpgm aisfeakdfl hvkekfnndw wigrlvkegc
      121 eigfipspvk lenmrlqheq rakqgkfyss ksggnssssl gdivpssrks tppssakqkq
      181 kstehtppyd vvpsmrpvvl vgpslkgyev tdmmqkalfd flkhrfegri sitrvtadis
      241 lakrsvlnnp skhaiiersn trsslaevqs eierifelar tlqlvvldad tinhpaqlsk
      301 tslapiivyv kisspkvlqr liksrgksqa khlnvqmvaa dklaqcppel fdvildenql
      361 edacehlady leaywkathp pssslpnpll srtlatsslp lsptlasnsq gsqgdqrtdr
      421 sapirsasqa eeepsvepvk ksqhrssssa phhnhrsgts rglsrqetfd setqesrdsa
      481 yvepkedysh dhvdhyashr dhnhrdethg ssdhrhresr hrsrdvdreq dhnecnkqrs
      541 rhkskdryce kdgeviskkr neagewnrdv yirq
//
LOCUS       NP_001400618             348 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001400618
VERSION     NP_001400618.1
DBSOURCE    REFSEQ: accession NM_001413689.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 348)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 348)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 348)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.1853615.1,
                                           ERR4368410.730713.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..348
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 1 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=35211
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     mat_peptide     42..348
                     /product="Dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3. /id=PRO_0000215300"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
                     /calculated_mol_wt=35211
     Region          54..342
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            277..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            313..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     CDS             1..348
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413689.1:169..1215"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 25"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvsyih gssqaqfvae shiilvlnaa itmgmvllne
      301 aatskgdvgk rriiclvglg lvvfffsfll sifrskyhgy pysdldfe
//
LOCUS       NP_001394743            1211 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 11 precursor
            [Homo sapiens].
ACCESSION   NP_001394743
VERSION     NP_001394743.1
DBSOURCE    REFSEQ: accession NM_001407814.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1211)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1211)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1211)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1211)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1211)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1211)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1211)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1211)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1211)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1211)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1929765.1,
                                           SRR12514507.819468.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1211
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 11 precursor"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=136208
     Region          261..290
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          296..323
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          432..704
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          831..1211
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1211
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407814.1:26..3661"
                     /note="isoform 11 precursor is encoded by transcript
                     variant 11"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 msalcwgrga aglkralrpc grpglpgkeg taggvcgprr sssaspqeqd qdrrkdwghv
       61 ellevlqarv rqlqaesvse vvvnrvdvar lpecgsgdgs lqpprkvqmg akdatpvpcg
      121 rwakilekdk rtqqmrmqrl kaklqmpfqs gefkaltrrl qveprllskq magcledctr
      181 qapespweeq larllqeapg klsldveqap sgqhsqaqls gqqqrllaff kcclltdqlp
      241 lahhllvvhh gqrqkrkllt ldmynavmlg warqgafkel vyvlfmvkda gltpdllsya
      301 aalqcmgrqd qdagtiercl eqmsqeglkl qalftavlls eedratvlka vhkvkptfsl
      361 ppqlpppvnt skllrdvyak dgrvsypklh lplktlqclf ekqlhmelas rvcvvsvekp
      421 tlpskevkha rktlktlrdq wekalcralr etknrlerev yegrfslypf lcllderevv
      481 rmllqvlqal paqgesfttl arelsartfs rhvvqrqrvs gqvqalqnhy rkylcllasd
      541 aevpepclpr qyweelgape alreqpwplp vqmelgklla emlvqatqmp csldkphrss
      601 rlvpvlyhvy sfrnvqqigi lkphpayvql lekaaeptlt feavdvpmlc pplpwtsphs
      661 gafllsptkl mrtvegatqh qelletcppt alhgaldalt qlgncawrvn grvldlvlql
      721 fqakgcpqlg vpappseapq ppeahlphsa aparkaelrr elahcqkvar emhslraeal
      781 yrlslaqhlr drvfwlphnm dfrgrtypcp phfnhlgsdv arallefaqg rplgphgldw
      841 lkihlvnltg lkkreplrkr lafaeevmdd ildsadqplt grkwwmgaee pwqtlaccme
      901 vanavrasdp aayvshlpvh qdgscnglqh yaalgrdsvg aasvnlepsd vpqdvysgva
      961 aqvvkqtvmt vvygvtrygg rlqiekrlre lsdfpqefvw eashylvrqv fkslqemfsg
     1021 traiqhwlte sarlishmgs vvewvtplgv pviqpyrlds kvkqigggiq sitythngdi
     1081 srkpntrkqk ngfppnfihs ldsshmmlta lhcyrspplc hrkgltfvsv hdcywthaad
     1141 vsvmnqvcre qfvrlhsepi lqdlsrflvk rfcsepqkil easqlketlq avpkpgafdl
     1201 eqvkrstyff s
//
LOCUS       NP_001427344             321 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 7 precursor [Homo
            sapiens].
ACCESSION   NP_001427344
VERSION     NP_001427344.1
DBSOURCE    REFSEQ: accession NM_001440415.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 321)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3 and AP004147.3.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1817878.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..321
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     7 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=33613
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..>302
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            286
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     CDS             1..321
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440415.1:863..1828"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 17"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk aaelgmvsay
      241 ytyiftnlef slqrmdslvd drvnilgfsi fnqshaffqe faqslnqswq encdhvpftg
      301 pagilvtvks ghvalldkwg n
//
LOCUS       NP_001427367            1184 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 isoform 4
            [Homo sapiens].
ACCESSION   NP_001427367
VERSION     NP_001427367.1
DBSOURCE    REFSEQ: accession NM_001440438.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1184)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1184)
  AUTHORS   Ji,X., Wu,Q., Cao,X., Liu,S., Zhang,J., Chen,S., Shan,J., Zhang,Y.,
            Li,B. and Zhao,H.
  TITLE     Helicobacter pylori East Asian type CagA hijacks more SHIP2 by its
            EPIYA-D motif to potentiate the oncogenicity
  JOURNAL   Virulence 15 (1), 2375549 (2024)
   PUBMED   38982595
  REMARK    GeneRIF: Helicobacter pylori East Asian type CagA hijacks more
            SHIP2 by its EPIYA-D motif to potentiate the oncogenicity.
REFERENCE   3  (residues 1 to 1184)
  AUTHORS   Ando,K., Kucukali,F., Doeraene,E., Nagaraj,S., Antonelli,E.M.,
            Thazin Htut,M., Yilmaz,Z., Kosa,A.C., Lopez-Guitierrez,L.,
            Quintanilla-Sanchez,C., Aydin,E., Ramos,A.R., Mansour,S.,
            Turbant,S., Schurmans,S., Sleegers,K., Erneux,C., Brion,J.P. and
            Leroy,K.
  CONSRTM   Brain Bank NeuroCEB Neuropathology Network
  TITLE     Alteration of gene expression and protein solubility of the PI
            5-phosphatase SHIP2 are correlated with Alzheimer's disease
            pathology progression
  JOURNAL   Acta Neuropathol 147 (1), 94 (2024)
   PUBMED   38833073
  REMARK    GeneRIF: Alteration of gene expression and protein solubility of
            the PI 5-phosphatase SHIP2 are correlated with Alzheimer's disease
            pathology progression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1184)
  AUTHORS   Bradshaw,W.J., Kennedy,E.C., Moreira,T., Smith,L.A., Chalk,R.,
            Katis,V.L., Benesch,J.L.P., Brennan,P.E., Murphy,E.J. and
            Gileadi,O.
  TITLE     Regulation of inositol 5-phosphatase activity by the C2 domain of
            SHIP1 and SHIP2
  JOURNAL   Structure 32 (4), 453-466 (2024)
   PUBMED   38309262
  REMARK    GeneRIF: Regulation of inositol 5-phosphatase activity by the C2
            domain of SHIP1 and SHIP2.
REFERENCE   5  (residues 1 to 1184)
  AUTHORS   Habib,T., Hejna,J.A., Moses,R.E. and Decker,S.J.
  TITLE     Growth factors and insulin stimulate tyrosine phosphorylation of
            the 51C/SHIP2 protein
  JOURNAL   J Biol Chem 273 (29), 18605-18609 (1998)
   PUBMED   9660833
REFERENCE   6  (residues 1 to 1184)
  AUTHORS   Le Drean,E., Vely,F., Olcese,L., Cambiaggi,A., Guia,S., Krystal,G.,
            Gervois,N., Moretta,A., Jotereau,F. and Vivier,E.
  TITLE     Inhibition of antigen-induced T cell response and antibody-induced
            NK cell cytotoxicity by NKG2A: association of NKG2A with SHP-1 and
            SHP-2 protein-tyrosine phosphatases
  JOURNAL   Eur J Immunol 28 (1), 264-276 (1998)
   PUBMED   9485206
  REMARK    Erratum:[Eur J Immunol 1998 Mar;28(3):1122]
REFERENCE   7  (residues 1 to 1184)
  AUTHORS   Pesesse,X., Deleu,S., De Smedt,F., Drayer,L. and Erneux,C.
  TITLE     Identification of a second SH2-domain-containing protein closely
            related to the phosphatidylinositol polyphosphate 5-phosphatase
            SHIP
  JOURNAL   Biochem Biophys Res Commun 239 (3), 697-700 (1997)
   PUBMED   9367831
REFERENCE   8  (residues 1 to 1184)
  AUTHORS   Hejna,J.A., Saito,H., Merkens,L.S., Tittle,T.V., Jakobs,P.M.,
            Whitney,M.A., Grompe,M., Friedberg,A.S. and Moses,R.E.
  TITLE     Cloning and characterization of a human cDNA (INPPL1) sharing
            homology with inositol polyphosphate phosphatases
  JOURNAL   Genomics 29 (1), 285-287 (1995)
   PUBMED   8530088
REFERENCE   9  (residues 1 to 1184)
  AUTHORS   Huang,S., Earl,D. and White,K.
  TITLE     INPPL1-Related Opsismodysplasia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   40504975
REFERENCE   10 (residues 1 to 1184)
  AUTHORS   Slama,V. and Dudek,J.
  TITLE     [Stability of diluted solutions of peracetic acid]
  JOURNAL   Cesk Farm 17 (1), 40-41 (1968)
   PUBMED   5668240
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000593.4.
            
            Summary: The protein encoded by this gene is an SH2-containing
            5'-inositol phosphatase that is involved in the regulation of
            insulin function. The encoded protein also plays a role in the
            regulation of epidermal growth factor receptor turnover and actin
            remodelling. Additionally, this gene supports metastatic growth in
            breast cancer and is a valuable biomarker for breast cancer.
            [provided by RefSeq, Jan 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038193.3398233.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968189, SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..1184
                     /product="phosphatidylinositol 3,4,5-trisphosphate
                     5-phosphatase 2 isoform 4"
                     /EC_number="3.1.3.86"
                     /note="SH2 domain-containing inositol-5'-phosphatase 2;
                     51C protein; protein 51C; phosphatidylinositol
                     3,4,5-trisphosphate 5-phosphatase 2"
                     /calculated_mol_wt=130393
     Region          17..119
                     /region_name="SH2_SHIP"
                     /note="Src homology 2 (SH2) domain found in SH2-containing
                     inositol-5'-phosphatase (SHIP) and SLAM-associated protein
                     (SAP); cd10343"
                     /db_xref="CDD:198206"
     Site            order(28,47,68,70)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198206"
     Site            order(68..69,81..82,87,90,106..108)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198206"
     Region          119..180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          424..727
                     /region_name="INPP5c_SHIP2-INPPL1"
                     /note="Catalytic inositol polyphosphate 5-phosphatase
                     (INPP5c) domain of SH2 domain containing inositol
                     5-phosphatase-2 and related proteins; cd09101"
                     /db_xref="CDD:197335"
     Site            order(432,434,473,540..541,561,564..565,607,609,611,
                     661..662,684,690,717..718)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197335"
     Site            order(432,473,561,607,609,690,717..718)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197335"
     Site            order(473,540..541,561,564..565,611,661..662,684,717)
                     /site_type="other"
                     /note="putative PI/IP binding site [chemical binding]"
                     /db_xref="CDD:197335"
     Site            order(473,717)
                     /site_type="other"
                     /note="putative Mg binding site [ion binding]"
                     /db_xref="CDD:197335"
     Site            order(561,609,718)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197335"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            890
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          897..1118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Region          944..949
                     /region_name="SH3-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Region          958..>1176
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            958
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17219406,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          983..986
                     /region_name="NPXY motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Site            986
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:11349134,
                     ECO:0000269|PubMed:12235291; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            1131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            1135
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:11687594,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     CDS             1..1184
                     /gene="INPPL1"
                     /gene_synonym="OPSMD; SHIP2"
                     /coded_by="NM_001440438.1:497..4051"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:3636"
                     /db_xref="HGNC:HGNC:6080"
                     /db_xref="MIM:600829"
ORIGIN      
        1 masacgapgp ggalgsqaps wyhrdlsraa aeellaragr dgsflvrdse svagafalcv
       61 lyqkhvhtyr ilpdgedfla vqtsqgvpvr rfqtlgelig lyaqpnqglv calllpvege
      121 repdppddrd asdgedekpp lpprsgstsi saptgpsspl papetptapa aesapnglst
      181 vshdylkgsy gldleavrgg ashlphltrt latscrrlhs evdkvlsgle ilskvfdqqs
      241 spmvtrllqq qnlpqtgeqe leslvlklsv lkdflsgiqk kalkalqdms stappapqps
      301 trkaktipvq afevkldvtl gdltkigksq kftlsvdveg grlvllrrqr dsqedwttft
      361 hdrirqliks qrvqnklgvv fekekdrtqr kdfifvsark reafcqllql mknkhskqde
      421 pdmisvfigt wnmgsvpppk nvtswftskg lgktldevtv tiphdiyvfg tqensvgdre
      481 wldllrgglk eltdldyrpi amqslwnikv avlvkpehen rishvstssv ktgiantlgn
      541 kgavgvsfmf ngtsfgfvnc hltsgnekta rrnqnyldil rllslgdrql nafdislrft
      601 hlfwfgdlny rldmdiqeil nyisrkefep llrvdqlnle rekhkvflrf seeeisfppt
      661 yryergsrdt yawhkqkptg vrtnvpswcd rilwksypet hiicnsygct ddivtsdhsp
      721 vfgtfevgvt sqfiskkgls ktsdqayief esieaivkta srtkffiefy stcleeykks
      781 fendaqssdn inflkvqwss rqlptlkpil adieylqdqh llltvksmdg yesygecvva
      841 lksmigstaq qfltflshrg eetgnirgsm kvrvpterlg trerlyewis idkdeagaks
      901 kapsvsrgsq eprsgsrkpa fteascplsr lfeepekppp tgrppappra apreepltpr
      961 lkpegapepe gvaapppkns fnnpayyvle gvphqllppe ppsparapvp satknkvait
     1021 vpapqlghhr hprvgegsss deesggtlpp pdfpppplpd saiflppsld plpgpvvrgr
     1081 ggaeargppp pkahprpplp pgpspastfl gevasgddrs csvlqmaktl sevdyapagp
     1141 arsallpgpl elqpprglps dygrplsfpp priresiqed laee
//
LOCUS       NP_001428257            1785 aa            linear   PRI 21-NOV-2025
DEFINITION  BCL-6 corepressor-like protein 1 isoform 1a [Homo sapiens].
ACCESSION   NP_001428257 XP_005262512 XP_054183515
VERSION     NP_001428257.1
DBSOURCE    REFSEQ: accession NM_001441328.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1785)
  AUTHORS   Luo,C., Chen,Z., Meng,L., Tan,C., He,W., Tu,C., Du,J., Lu,G.X.,
            Lin,G., Tan,Y.Q. and Hu,T.Y.
  TITLE     A hemizygous loss-of-function variant in BCORL1 is associated with
            male infertility and oligoasthenoteratozoospermia
  JOURNAL   Clin Genet 106 (1), 27-36 (2024)
   PUBMED   38342987
  REMARK    GeneRIF: A hemizygous loss-of-function variant in BCORL1 is
            associated with male infertility and oligoasthenoteratozoospermia.
REFERENCE   2  (residues 1 to 1785)
  AUTHORS   Kommoss,F.K.F., Chiang,S., Kobel,M., Koelsche,C., Chang,K.T.,
            Irving,J.A., Dickson,B., Thiryayi,S., Rouzbahman,M., Rasty,G., von
            Deimling,A., Lee,C.H. and Turashvili,G.
  TITLE     Endometrial Stromal Sarcomas With BCOR Internal Tandem Duplication
            and Variant BCOR/BCORL1 Rearrangements Resemble High-grade
            Endometrial Stromal Sarcomas With Recurrent CDK4 Pathway
            Alterations and MDM2 Amplifications
  JOURNAL   Am J Surg Pathol 46 (8), 1142-1152 (2022)
   PUBMED   35499168
  REMARK    GeneRIF: Endometrial Stromal Sarcomas With BCOR Internal Tandem
            Duplication and Variant BCOR/BCORL1 Rearrangements Resemble
            High-grade Endometrial Stromal Sarcomas With Recurrent CDK4 Pathway
            Alterations and MDM2 Amplifications.
REFERENCE   3  (residues 1 to 1785)
  AUTHORS   Schaefer,E.J., Wang,H.C., Karp,H.Q., Meyer,C.A., Cejas,P.,
            Gearhart,M.D., Adelman,E.R., Fares,I., Apffel,A., Lim,K., Xie,Y.,
            Gibson,C.J., Schenone,M., Murdock,H.M., Wang,E.S., Gondek,L.P.,
            Carroll,M.P., Vedula,R.S., Winer,E.S., Garcia,J.S., Stone,R.M.,
            Luskin,M.R., Carr,S.A., Long,H.W., Bardwell,V.J., Figueroa,M.E. and
            Lindsley,R.C.
  TITLE     BCOR and BCORL1 Mutations Drive Epigenetic Reprogramming and
            Oncogenic Signaling by Unlinking PRC1.1 from Target Genes
  JOURNAL   Blood Cancer Discov 3 (2), 116-135 (2022)
   PUBMED   35015684
  REMARK    GeneRIF: BCOR and BCORL1 Mutations Drive Epigenetic Reprogramming
            and Oncogenic Signaling by Unlinking PRC1.1 from Target Genes.
REFERENCE   4  (residues 1 to 1785)
  AUTHORS   Gafner,M., Michelson,M., Argilli,E., Yosovich,K., Sherr,E.H.,
            Parks,K.C., England,E.M., Hady-Cohen,R., Leibovitz,Z., Lev,D.,
            Michaeli-Yosef,Y., Lerman-Sagie,T. and Blumkin,L.
  TITLE     Major brain malformations: corpus callosum dysgenesis, agenesis of
            septum pellucidum and polymicrogyria in patients with
            BCORL1-related disorders
  JOURNAL   J Hum Genet 67 (2), 95-101 (2022)
   PUBMED   34400773
  REMARK    GeneRIF: Major brain malformations: corpus callosum dysgenesis,
            agenesis of septum pellucidum and polymicrogyria in patients with
            BCORL1-related disorders.
REFERENCE   5  (residues 1 to 1785)
  AUTHORS   Junco,S.E., Wang,R., Gaipa,J.C., Taylor,A.B., Schirf,V.,
            Gearhart,M.D., Bardwell,V.J., Demeler,B., Hart,P.J. and Kim,C.A.
  TITLE     Structure of the polycomb group protein PCGF1 in complex with BCOR
            reveals basis for binding selectivity of PCGF homologs
  JOURNAL   Structure 21 (4), 665-671 (2013)
   PUBMED   23523425
REFERENCE   6  (residues 1 to 1785)
  AUTHORS   Shaffer,J.R., Feingold,E., Wang,X., Lee,M., Tcuenco,K., Weeks,D.E.,
            Weyant,R.J., Crout,R., McNeil,D.W. and Marazita,M.L.
  TITLE     GWAS of dental caries patterns in the permanent dentition
  JOURNAL   J Dent Res 92 (1), 38-44 (2013)
   PUBMED   23064961
REFERENCE   7  (residues 1 to 1785)
  AUTHORS   Gao,Z., Zhang,J., Bonasio,R., Strino,F., Sawai,A., Parisi,F.,
            Kluger,Y. and Reinberg,D.
  TITLE     PCGF homologs, CBX proteins, and RYBP define functionally distinct
            PRC1 family complexes
  JOURNAL   Mol Cell 45 (3), 344-356 (2012)
   PUBMED   22325352
REFERENCE   8  (residues 1 to 1785)
  AUTHORS   Li,M., Collins,R., Jiao,Y., Ouillette,P., Bixby,D., Erba,H.,
            Vogelstein,B., Kinzler,K.W., Papadopoulos,N. and Malek,S.N.
  TITLE     Somatic mutations in the transcriptional corepressor gene BCORL1 in
            adult acute myelogenous leukemia
  JOURNAL   Blood 118 (22), 5914-5917 (2011)
   PUBMED   21989985
  REMARK    GeneRIF: BCORL1 by genetic criteria is a novel candidate tumor
            suppressor gene, joining the growing list of genes recurrently
            mutated in acute myelogenous leukemia.
REFERENCE   9  (residues 1 to 1785)
  AUTHORS   Pagan,J.K., Arnold,J., Hanchard,K.J., Kumar,R., Bruno,T.,
            Jones,M.J., Richard,D.J., Forrest,A., Spurdle,A., Verdin,E.,
            Crossley,M., Fanciulli,M., Chenevix-Trench,G., Young,D.B. and
            Khanna,K.K.
  TITLE     A novel corepressor, BCoR-L1, represses transcription through an
            interaction with CtBP
  JOURNAL   J Biol Chem 282 (20), 15248-15257 (2007)
   PUBMED   17379597
REFERENCE   10 (residues 1 to 1785)
  AUTHORS   Lose,F., Arnold,J., Young,D.B., Brown,C.J., Mann,G.J., Pupo,G.M.,
            Khanna,K.K., Chenevix-Trench,G. and Spurdle,A.B.
  CONSRTM   Kathleen Cuningham Foundation Consortium for Research into Familial
            Breast Cancer
  TITLE     BCoR-L1 variation and breast cancer
  JOURNAL   Breast Cancer Res 9 (4), R54 (2007)
   PUBMED   17697391
  REMARK    GeneRIF: Dysregulated BCoR-L1 expression is associated with breast
            cancer
            Erratum:[Breast Cancer Res. 2008;10(5):406]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL034405.16, Z82208.1,
            KF459400.1 and AL136450.8.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_005262512.2, XP_054183515.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            corepressor that is found tethered to promoter regions by
            DNA-binding proteins. The encoded protein can interact with several
            different class II histone deacetylases to repress transcription.
            Two transcript variants encoding different isoforms have been found
            for this gene. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2163363.1,
                                           SRR14038193.1552557.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1785
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.1"
     Protein         1..1785
                     /product="BCL-6 corepressor-like protein 1 isoform 1a"
                     /note="BCoR-like protein 1"
                     /calculated_mol_wt=190431
     Region          65..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          113..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          <198..636
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          343..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          527..550
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          562..646
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          753..781
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          876..901
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          937..977
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1029
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1033
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1107..1293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1312..1487
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1328..1336
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          <1494..>1603
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1496..1527
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1497,1501..1502,1505..1507,1509..1510,1514,1517,
                     1527,1529,1531,1535..1536,1539..1541,1543..1544,1548,1551,
                     1560,1562,1564,1568..1569,1572..1574,1576..1577,1581,1584)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1529..1560
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1529..1558
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1562..1591
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1562..1591
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1595..1623
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1666..1779
                     /region_name="PUFD_like_1"
                     /note="PCGF Ub-like fold discriminator of BCOR-like 1;
                     cd14260"
                     /db_xref="CDD:271223"
     Region          1668..1785
                     /region_name="PCGF Ub-like fold domain (PUFD), required
                     for the interaction with the KDM2B-SKP1 heterodimeric
                     complex. /evidence=ECO:0000269|PubMed:27568929"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            order(1668,1670..1680,1682,1684,1693..1695,1697,
                     1738..1739,1741,1744,1766,1777,1779)
                     /site_type="other"
                     /note="RAWUL domain interface [polypeptide binding]"
                     /db_xref="CDD:271223"
     CDS             1..1785
                     /gene="BCORL1"
                     /gene_synonym="BCoR-L1; CXorf10; SHUVER"
                     /coded_by="NM_001441328.1:89..5446"
                     /note="isoform 1a is encoded by transcript variant 6"
                     /db_xref="GeneID:63035"
                     /db_xref="HGNC:HGNC:25657"
                     /db_xref="MIM:300688"
ORIGIN      
        1 mistaplysg vhnwtssdri rmcgineerr aplsdeestt gdcqhfgsqe fcvsssfskv
       61 eltavgsgsn argadpdgsa teklghksed kpddpqpkmd yagnvaeaeg llvplsspgd
      121 glklpasdsa easnsradcs wtplntqmsk qvdcspagvk aldsrqgvge kntfilatlg
      181 tgvpvegtlp lvttnfsplp apicppapgs asvphsvpda fqvplsvpap vphsglvpvq
      241 vatsvpapsp plapvpalap appsvptlis dsnplsvsas vlvpvpasap psgpvplsap
      301 apaplsvpvs applaliqap vppsaptlvl apvptpvlap mpastppaap appsvpmptp
      361 tpssgppstp tlipafaptp vpaptpapif tpaptpmpaa tpaaiptsap ipasfslsrv
      421 cfpaaqapam qkvplsfqpg tvltpsqplv yipppscgqp lsvatlpttl gvsstltlpv
      481 lpsylqdrcl pgvlaspelr sypyafsvar pltsdsklvs levnrlpcts psgstttqpa
      541 pdgvpgplad tslvtasakv lptpqpllpa psgssapphp akmpsgteqq tegtsvtfsp
      601 lksppqlere masppecsem pldlssksnr qklplpnqrk tppmpvltpv htsskallst
      661 vlsrsqrttq aaggnvtscl gstsspfvif peivrngdps twvknstali stipgtyvgv
      721 anpvpaslll nkdpnlglnr dprhlpkqep isiidqgepk gtgatcgkkg sqagaegqps
      781 tvkrytpari apglpgcqtk elslwkptgp aniyprcsvn gkptstqvlp vgwspyhqas
      841 llsigissag qltpsqgapi rptsvvsefs gvpslsssea vhglpegqpr pggsfvpeqd
      901 pvtknktcri aakpyeeqvn pvlltlspqt gtlalsvqps ggdirmnqgp eeseshlcsd
      961 stpkmegpqg acglklagdt kpknqvlaty mshelvlatp qnlpkmpelp llphdshpke
     1021 lildvvpssr rgssterpql gsqvdlgrvk mekvdgdvvf nlatcfradg lpvapqrgqa
     1081 evrakagqar vkqesvgvfa cknkwqpddv teslppkkmk cgkekdseeq qlqpqakavv
     1141 rsshrpkcrk lpsdpqestk ksprgasdsg kehngvrgkh khrkptkpes qspgkradsh
     1201 eegslekkak ssfrdfipvv lstrtrsqsg sicssfagma dsdmgsqevf pteeeeevtp
     1261 tpakrrkvrk tqrdtqyrsh haqdksllsq grrhlwrare mpwrteaarq mwdtneeeee
     1321 eeeegllkrk krrrqksrky qtgeylteqe deqrrkgrad lkarkqktss sqslehrlrn
     1381 rnlllpnkvq gisdspngfl pnnleepacl ensekpsgkr kcktkhmatv seeakgkgrw
     1441 sqqktrspks ptpvkptepc tpsksrsass eeasesptar qippearrli vnknagetll
     1501 qraarlgykd vvlyclqkds edvnhrdnag ytalheacsr gwtdilnill ehganvncsa
     1561 qdgtrpvhda vvndnletiw lllsygadpt latysgqtam klassdtmkr flsdhlsdlq
     1621 graegdpgvs wdfysssvle ekdgfacdll hnppgssdqe gddpmeeddf mfelsdkpll
     1681 pcynlqvsvs rgpcnwflfs dvlkrlklss rifqarfphf eittmpkaef yrqvassqll
     1741 tpaerpggld drsppgsset velvryepdl lrllgsevef qscns
//
LOCUS       NP_001400244             280 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 3 [Homo sapiens].
ACCESSION   NP_001400244 XP_024302835
VERSION     NP_001400244.1
DBSOURCE    REFSEQ: accession NM_001413315.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 280)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 280)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 280)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            On Oct 31, 2022 this sequence version replaced XP_024302835.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.261139.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162841, SAMN03267755
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..280
                     /product="RNA-binding Raly-like protein isoform 3"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=30943
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          188..>233
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     CDS             1..280
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413315.1:112..954"
                     /note="isoform 3 is encoded by transcript variant 42"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly sgyvfdydyy
      121 rddfynrlfd yhgrvppppr aviplkrprv avtttrrgkg vfsmkggsrs tasgstgskl
      181 ksdelqtikk eltqiktkid sllgrlekie kqqkaeaeaq kkqleeslvl iqeecvseia
      241 dhsteepaeg gpdadgeemt dgieedfded gghelflqik
//
LOCUS       NP_001397939            2563 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HECTD1 isoform 2 [Homo sapiens].
ACCESSION   NP_001397939 XP_047287156
VERSION     NP_001397939.1
DBSOURCE    REFSEQ: accession NM_001411010.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2563)
  AUTHORS   Oxman,E., Li,H., Wang,H.Y. and Zohn,I.E.
  TITLE     Identification and functional analysis of rare HECTD1 missense
            variants in human neural tube defects
  JOURNAL   Hum Genet 143 (3), 263-277 (2024)
   PUBMED   38451291
  REMARK    GeneRIF: Identification and functional analysis of rare HECTD1
            missense variants in human neural tube defects.
REFERENCE   2  (residues 1 to 2563)
  AUTHORS   Zhang,J., Xin,Y., Ling,X., Liang,H., Zhang,L., Fang,C. and Ma,J.
  TITLE     Nucleoporin 93, a new substrate of the E3 ubiquitin protein ligase
            HECTD1, promotes esophageal squamous cell carcinoma progression
  JOURNAL   Hum Cell 37 (1), 245-257 (2024)
   PUBMED   37993750
  REMARK    GeneRIF: Nucleoporin 93, a new substrate of the E3 ubiquitin
            protein ligase HECTD1, promotes esophageal squamous cell carcinoma
            progression.
REFERENCE   3  (residues 1 to 2563)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 2563)
  AUTHORS   Vaughan,N., Scholz,N., Lindon,C. and Licchesi,J.D.F.
  TITLE     The E3 ubiquitin ligase HECTD1 contributes to cell proliferation
            through an effect on mitosis
  JOURNAL   Sci Rep 12 (1), 13160 (2022)
   PUBMED   35915203
  REMARK    GeneRIF: The E3 ubiquitin ligase HECTD1 contributes to cell
            proliferation through an effect on mitosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2563)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 2563)
  AUTHORS   Aleidi,S.M., Yang,A., Sharpe,L.J., Rao,G., Cochran,B.J., Rye,K.A.,
            Kockx,M., Brown,A.J. and Gelissen,I.C.
  TITLE     The E3 ubiquitin ligase, HECTD1, is involved in ABCA1-mediated
            cholesterol export from macrophages
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1863 (4), 359-368 (2018)
   PUBMED   29306077
  REMARK    GeneRIF: HECTD1 may be involved in the regulation of ABCA1-mediated
            cholesterol export from unloaded macrophages to apoA-I.
REFERENCE   7  (residues 1 to 2563)
  AUTHORS   Fang,S., Guo,H., Cheng,Y., Zhou,Z., Zhang,W., Han,B., Luo,W.,
            Wang,J., Xie,W. and Chao,J.
  TITLE     circHECTD1 promotes the silica-induced pulmonary
            endothelial-mesenchymal transition via HECTD1
  JOURNAL   Cell Death Dis 9 (3), 396 (2018)
   PUBMED   29540674
  REMARK    GeneRIF: SiO2 concomitantly increased circHECTD1 expression, which,
            in turn, inhibited HECTD1 protein expression.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 2563)
  AUTHORS   Shen,X., Jia,Z., D'Alonzo,D., Wang,X., Bruder,E., Emch,F.H., De
            Geyter,C. and Zhang,H.
  TITLE     HECTD1 controls the protein level of IQGAP1 to regulate the
            dynamics of adhesive structures
  JOURNAL   Cell Commun Signal 15 (1), 2 (2017)
   PUBMED   28073378
  REMARK    GeneRIF: Hectd1 regulates the protein level of IQGAP1 through
            ubiquitination.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 2563)
  AUTHORS   Helander,S., Montecchio,M., Lemak,A., Fares,C., Almlof,J., Yi,Y.,
            Yee,A., Arrowsmith,C., DhePaganon,S. and Sunnerhagen,M.
  TITLE     Basic Tilted Helix Bundle - a new protein fold in human
            FKBP25/FKBP3 and HectD1
  JOURNAL   Biochem Biophys Res Commun 447 (1), 26-31 (2014)
   PUBMED   24667607
  REMARK    GeneRIF: our high-resolution structures show a new fold composed of
            five small helices where H3 and H4 are tilted in a novel
            arrangement; we call this fold the Basic Tilted Helix Bundle (BTHB)
            domain.
REFERENCE   10 (residues 1 to 2563)
  AUTHORS   Tran,H., Bustos,D., Yeh,R., Rubinfeld,B., Lam,C., Shriver,S.,
            Zilberleyb,I., Lee,M.W., Phu,L., Sarkar,A.A., Zohn,I.E.,
            Wertz,I.E., Kirkpatrick,D.S. and Polakis,P.
  TITLE     HectD1 E3 ligase modifies adenomatous polyposis coli (APC) with
            polyubiquitin to promote the APC-axin interaction
  JOURNAL   J Biol Chem 288 (6), 3753-3767 (2013)
   PUBMED   23277359
  REMARK    GeneRIF: HectD1 promotes the APC-Axin interaction to negatively
            regulate Wnt signaling.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136418.4, AL121808.4 and KC877516.1.
            
            On Aug 20, 2022 this sequence version replaced XP_047287156.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1892216.1,
                                           SRR14038194.2261023.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2563
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..2563
                     /product="E3 ubiquitin-protein ligase HECTD1 isoform 2"
                     /EC_number="2.3.2.26"
                     /note="E3 ubiquitin-protein ligase HECTD1; E3 ligase for
                     inhibin receptor; HECT domain-containing protein 1; HECT
                     domain containing E3 ubiquitin protein ligase 1; HECT-type
                     E3 ubiquitin transferase HECTD1"
                     /calculated_mol_wt=284325
     Region          246..269
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          <366..>479
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          366..393
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          395..424
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          396..426
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(397,401..402,405..407,409..410,414,417,426,428,
                     432..433,436..438,440..441,445,448,457,459,461,465..466,
                     469..471,473..474,478)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          426..455
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          428..457
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          459..491
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          489..513
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          579..612
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          627..657
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZR2; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          707..748
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1107..1240
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     Region          1277..>1321
                     /region_name="MIB_HERC2"
                     /note="Mib_herc2; pfam06701"
                     /db_xref="CDD:461991"
     Site            1337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZR2; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1386..1436
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1449..1468
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZR2; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1545..1564
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1627..1710
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1713
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1725
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1730..1750
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1846..1911
                     /region_name="BTHB_HectD1"
                     /note="basic tilted helix bundle (BTHB) domain found in
                     HECT domain-containing protein 1 (HectD1) and similar
                     proteins; cd21062"
                     /db_xref="CDD:439138"
     Region          1982..2056
                     /region_name="K-box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          2084..2561
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(2090,2119,2129,2216,2494,2526..2527,2530..2534,2554,
                     2560)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Region          2250..2271
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            2271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            order(2309,2312..2313,2315..2316,2319,2361,2363,
                     2367..2368,2370,2376,2381,2398,2402)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..2563
                     /gene="HECTD1"
                     /gene_synonym="EULIR"
                     /coded_by="NM_001411010.1:425..8116"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS91860.1"
                     /db_xref="GeneID:25831"
                     /db_xref="HGNC:HGNC:20157"
                     /db_xref="MIM:618649"
ORIGIN      
        1 madvdpdtll ewlqmgqgde rdmqlialeq lcmlllmsdn vdrcfetcpp rtflpalcki
       61 fldesapdnv levtaraity yldvsaectr rivgvdgaik alcnrlvvve lnnrtsrdla
      121 eqcvkvleli ctresgavfe agglncvltf irdsghlvhk dtlhsamavv srlcgkmepq
      181 dssleicves lssllkhedh qvsdgalrcf asladrftrr gvdpaplakh glteellsrm
      241 aaaggtvsgp ssackpgrst tgapsttads klsnqvstiv sllstlcrgs pvvthdllrs
      301 elpdsiesal qgdercvldt mrlvdlllvl lfegrkalpk ssagstgrip glrrldssge
      361 rshrqlidci rskdtdalid aidtgafevn fmddvgqtll nwasafgtqe mveflcerga
      421 dvnrgqrsss lhyaacfgrp qvaktllrhg anpdlrdedg ktpldkarer ghsevvailq
      481 spgdwmcpvn kgddkkkkdt nkdeeecnep kgdpemapiy lkrllpvfaq tfqqtmlpsi
      541 rkaslalirk mihfcseall kevcdsdvgh nlptilveit atvldqeddd dghllalqii
      601 rdlvdkggdi fldqlarlgv iskvstlagp ssddeneees kpekedepqe dakelqqgkp
      661 yhwrdwsiir grdclyiwsd aaalelsngs ngwfrfildg klatmyssgs peggsdsses
      721 rsefleklqr argqvkpsts sqpilsapgp tkltvgnwsl tclkegeiai hnsdgqqati
      781 lkedlpgfvf esnrgtkhsf taetslgsef vtgwtgkrgr klksklektk qkvrtmardl
      841 yddhfkaves mprgvvvtlr niatqlessw elhtnrqcie sentwrdlmk talenlivll
      901 kdentispye mcssglvqal ltvlnnsmdl dmkqdcsqlv erinvfktaf seneddesrp
      961 avalirklia vlesierlpl hlydtpgsty nlqiltrrlr frlerapget alidrtgrml
     1021 kmeplatves leqyllkmva kqwydfdrss fvfvrklreg qnfifrhqhd fdengiiywi
     1081 gtnaktayew vnpaayglvv vtssegrnlp ygrledilsr dnsalnchsn ddknawfaid
     1141 lglwvipsay tlrhargygr salrnwvfqv skdgqnwtsl ythvddcsln epgstatwpl
     1201 dppkdekqgw rhvrikqmgk nasgqthyls lsgfelygtv ngvcedqlgk aakeaeanlr
     1261 rqrrlvrsqv lkymvpgarv irgldwkwrd qdgspqgegt vtgelhngtt qswsslvknn
     1321 cpdktsaaag sssrkgssss vcsvasssdi slgstkterr seivmehsiv sgadvhepiv
     1381 vlssaenvpq tevgssssas tstltaetgs enaerklgpd ssvrtpgess aismgivsvs
     1441 spdvssvsel tnkeaasqrp lsssasnrls vssllaagap msssasvpnl ssretssles
     1501 fvrrvaniar tnatnnmnls rsssdnntnt lgrnvmstat splmgaqsfp nlttpgttst
     1561 vtmstssvts ssnvatattv lsvgqslsnt lttsltstss esdtgqeaey slydfldscr
     1621 astllaeldd dedlpepdee ddeneddnqe dqeyeevmil rrpslqrrag srsdvthhav
     1681 tsqlpqvpag agsrpigeqe eeeyetkggr rrtwdddyvl krqfsalvpa fdprpgrtnv
     1741 qqttdleipp pgtphselle evectpsprl altlkvtglg ttrevelplt nfrstifyyv
     1801 qkllqlscng nvksdklrri weptytimyr emkdsdkeke ngkmgcwsie hveqylgtde
     1861 lpkndlityl qknadaaflr hwkltgtnks irknrncsql iaaykdfceh gtksglnqga
     1921 istlqssdil nltkeqpqak agngqnscgv edvlqllril yivasdpysr isqedgdeqp
     1981 qftfppdeft skkittkilq qieeplalas galpdwceql tskcpflipf etrqlyftct
     2041 afgasraivw lqnrreatve rtrttssvrr ddpgefrvgr lkhervkvpr geslmewaen
     2101 vmqihadrks vleveflgee gtglgptlef yalvaaefqr tdlgawlcdd nfpddesrhv
     2161 dlggglkppg yyvqrscglf tapfpqdsde leritklfhf lgiflakciq dnrlvdlpis
     2221 kpffklmcmg diksnmskli yesrgdrdlh ctesqseast eeghdslsvg sfeedsksef
     2281 ildppkpkpp awfngiltwe dfelvnphra rflkeikdla ikrrqilsnk glsedekntk
     2341 lqelvlknps gsgpplsied lglnfqfcps sriygftavd lkpsgedemi tmdnaeeyvd
     2401 lmfdfcmhtg iqkqmeafrd gfnkvfpmek lssfsheevq milcgnqsps waaediinyt
     2461 epklgytrds pgflrfvrvl cgmssderka flqfttgcst lppgglanlh prltvvrkvd
     2521 atdasypsvn tcvhylklpe ysseeimrer llaatmekgf hln
//
LOCUS       NP_001425602             778 aa            linear   PRI 21-NOV-2025
DEFINITION  dipeptidyl peptidase 8 isoform 11 [Homo sapiens].
ACCESSION   NP_001425602 XP_047288721 XP_054234285
VERSION     NP_001425602.1
DBSOURCE    REFSEQ: accession NM_001438673.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Li,K., Zhang,Y., Zhao,W., Wang,R., Li,Y., Wei,L., Wang,L., Chen,X.,
            Chen,Z., Liu,P., Nie,N., Tian,X. and Fu,R.
  TITLE     DPP8/9 inhibition attenuates the TGF-beta1-induced excessive
            deposition of extracellular matrix (ECM) in human mesangial cells
            via Smad and Akt signaling pathways
  JOURNAL   Toxicol Lett 395, 1-10 (2024)
   PUBMED   38458339
  REMARK    GeneRIF: DPP8/9 inhibition attenuates the TGF-beta1-induced
            excessive deposition of extracellular matrix (ECM) in human
            mesangial cells via Smad and Akt signaling pathways.
REFERENCE   3  (residues 1 to 778)
  AUTHORS   Zhang,Y., Li,K., Li,Y., Zhao,W., Wang,L., Chen,Z., Ma,X., Yao,T.,
            Wang,J., Dong,W., Li,X., Tian,X. and Fu,R.
  TITLE     Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the
            proximal renal tubule epithelial cells
  JOURNAL   Pharmacol Res 169, 105630 (2021)
   PUBMED   33932609
  REMARK    GeneRIF: Profibrotic mechanisms of DPP8 and DPP9 highly expressed
            in the proximal renal tubule epithelial cells.
REFERENCE   4  (residues 1 to 778)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 778)
  AUTHORS   Hollingsworth,L.R., Sharif,H., Griswold,A.R., Fontana,P.,
            Mintseris,J., Dagbay,K.B., Paulo,J.A., Gygi,S.P., Bachovchin,D.A.
            and Wu,H.
  TITLE     DPP9 sequesters the C terminus of NLRP1 to repress inflammasome
            activation
  JOURNAL   Nature 592 (7856), 778-783 (2021)
   PUBMED   33731932
REFERENCE   6  (residues 1 to 778)
  AUTHORS   Chen,Y.S., Chien,C.H., Goparaju,C.M., Hsu,J.T., Liang,P.H. and
            Chen,X.
  TITLE     Purification and characterization of human prolyl dipeptidase DPP8
            in Sf9 insect cells
  JOURNAL   Protein Expr Purif 35 (1), 142-146 (2004)
   PUBMED   15039077
REFERENCE   7  (residues 1 to 778)
  AUTHORS   Shu,H., Chen,S., Bi,Q., Mumby,M. and Brekken,D.L.
  TITLE     Identification of phosphoproteins and their phosphorylation sites
            in the WEHI-231 B lymphoma cell line
  JOURNAL   Mol Cell Proteomics 3 (3), 279-286 (2004)
   PUBMED   14729942
REFERENCE   8  (residues 1 to 778)
  AUTHORS   Qi,S.Y., Riviere,P.J., Trojnar,J., Junien,J.L. and Akinsanya,K.O.
  TITLE     Cloning and characterization of dipeptidyl peptidase 10, a new
            member of an emerging subgroup of serine proteases
  JOURNAL   Biochem J 373 (Pt 1), 179-189 (2003)
   PUBMED   12662155
REFERENCE   9  (residues 1 to 778)
  AUTHORS   Ajami,K., Abbott,C.A., Obradovic,M., Gysbers,V., Kahne,T.,
            McCaughan,G.W. and Gorrell,M.D.
  TITLE     Structural requirements for catalysis, expression, and dimerization
            in the CD26/DPIV gene family
  JOURNAL   Biochemistry 42 (3), 694-701 (2003)
   PUBMED   12534281
REFERENCE   10 (residues 1 to 778)
  AUTHORS   Abbott,C.A., Yu,D.M., Woollatt,E., Sutherland,G.R., McCaughan,G.W.
            and Gorrell,M.D.
  TITLE     Cloning, expression and chromosomal localization of a novel human
            dipeptidyl peptidase (DPP) IV homolog, DPP8
  JOURNAL   Eur J Biochem 267 (20), 6140-6150 (2000)
   PUBMED   11012666
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011846.16 and AC105129.4.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047288721.1, XP_054234285.1.
            
            Summary: This gene encodes a member of the peptidase S9B family, a
            small family of dipeptidyl peptidases that are able to cleave
            peptide substrates at a prolyl bond. The encoded protein shares
            similarity with dipeptidyl peptidase IV in that it is ubiquitously
            expressed, and hydrolyzes the same substrates. These similarities
            suggest that, like dipeptidyl peptidase IV, this protein may play a
            role in T-cell activation and immune function. Alternatively
            spliced transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3582851.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..778
                     /product="dipeptidyl peptidase 8 isoform 11"
                     /EC_number="3.4.14.5"
                     /note="prolyl dipeptidase DPP8; dipeptidyl peptidase VIII;
                     DPP VIII; dipeptidyl peptidase IV-related protein 1"
                     /calculated_mol_wt=89326
     Region          8..162
                     /region_name="Dpp_8_9_N"
                     /note="Dipeptidyl peptidase 8 and 9 N-terminal; pfam19520"
                     /db_xref="CDD:466112"
     Region          175..595
                     /region_name="DPPIV_N"
                     /note="Dipeptidyl peptidase IV (DPP IV) N-terminal region;
                     pfam00930"
                     /db_xref="CDD:395744"
     Region          637..>766
                     /region_name="DAP2"
                     /note="Dipeptidyl aminopeptidase/acylaminoacyl peptidase
                     [Amino acid transport and metabolism]; COG1506"
                     /db_xref="CDD:441115"
     CDS             1..778
                     /gene="DPP8"
                     /gene_synonym="DP8; DPRP-1; DPRP1; MST097; MSTP097;
                     MSTP135; MSTP141"
                     /coded_by="NM_001438673.1:304..2640"
                     /note="isoform 11 is encoded by transcript variant 15"
                     /db_xref="GeneID:54878"
                     /db_xref="HGNC:HGNC:16490"
                     /db_xref="MIM:606819"
ORIGIN      
        1 mwkrseqmki ksgkcnmaaa meteqlgvei fetadceeni esqdrpklep fyveryswsq
       61 lkklladtrk yhgymmakap hdfmfvkrnd pdgphsdriy ylamsgenre ntlfyseipk
      121 tinraavlml swkplldlfq atldygmysr eeellrerkr igtvgiasyd yhqgsgtflf
      181 qagsgiyhvk dggpqgftqq plrpnlvets cpnirmdpkl cpadpdwiaf ihsndiwisn
      241 ivtreerrlt yvhnelanme edarsagvat fvlqeefdry sgywwcpkae ttpsggkilr
      301 ilyeendese veiihvtspm letrradsfr ypktgtanpk vtfkmseimi daegriidvi
      361 dkeliqpfei lfegveyiar agwtpegkya wsilldrsqt rlqivlispe lfipveddvm
      421 erqrliesvp dsvtpliiye ettdiwinih difhvfpqsh eeeiefifas ecktgfrhly
      481 kitsilkesk ykrssgglpa psdfkcpike eiaitsgewe vlgrhgsniq vdevrrlvyf
      541 egtkdspleh hlyvvsyvnp gevtrltdrg yshsccisqh cdffiskysn qknphcvsly
      601 klsspeddpt cktkefwati ldsagplpdy tppeifsfes ttgftlygml ykphdlqpgk
      661 kyptvlfiyg gpqvqlvnnr fkgvkyfrln tlaslgyvvv vidnrgschr glkfegafky
      721 kmvaiagapv tlwifydtgy terymghpdq neqgyylgsv amqaekfpse silrrdta
//
LOCUS       NP_001424392            1273 aa            linear   PRI 21-NOV-2025
DEFINITION  paired amphipathic helix protein Sin3a [Homo sapiens].
ACCESSION   NP_001424392 XP_006720528 XP_054233663
VERSION     NP_001424392.1
DBSOURCE    REFSEQ: accession NM_001437463.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1273)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1273)
  AUTHORS   Coenen-van der Spek,J., Relator,R., Kerkhof,J., McConkey,H.,
            Levy,M.A., Tedder,M.L., Louie,R.J., Fletcher,R.S., Moore,H.W.,
            Childers,A., Farrelly,E.R., Champaigne,N.L., Lyons,M.J.,
            Everman,D.B., Rogers,R.C., Skinner,S.A., Renck,A., Matalon,D.R.,
            Dills,S.K., Monteleone,B., Demirdas,S., Dingemans,A.J.M., Donker
            Kaat,L., Kolk,S.M., Pfundt,R., Rump,P., Sadikovic,B., Kleefstra,T.
            and Butler,K.M.
  TITLE     DNA methylation episignature for Witteveen-Kolk syndrome due to
            SIN3A haploinsufficiency
  JOURNAL   Genet Med 25 (1), 63-75 (2023)
   PUBMED   36399132
  REMARK    GeneRIF: DNA methylation episignature for Witteveen-Kolk syndrome
            due to SIN3A haploinsufficiency.
REFERENCE   3  (residues 1 to 1273)
  AUTHORS   Soukar,I., Amarasinghe,A. and Pile,L.A.
  TITLE     Coordination of cross-talk between metabolism and epigenetic
            regulation by the SIN3 complex
  JOURNAL   Enzymes 53, 33-68 (2023)
   PUBMED   37748836
  REMARK    GeneRIF: Coordination of cross-talk between metabolism and
            epigenetic regulation by the SIN3 complex.
            Review article
REFERENCE   4  (residues 1 to 1273)
  AUTHORS   Dahiya,N.R., Leibovitch,B.A., Kadamb,R., Bansal,N. and Waxman,S.
  TITLE     The Sin3A/MAD1 Complex, through Its PAH2 Domain, Acts as a Second
            Repressor of Retinoic Acid Receptor Beta Expression in Breast
            Cancer Cells
  JOURNAL   Cells 11 (7), 1179 (2022)
   PUBMED   35406744
  REMARK    GeneRIF: The Sin3A/MAD1 Complex, through Its PAH2 Domain, Acts as a
            Second Repressor of Retinoic Acid Receptor Beta Expression in
            Breast Cancer Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1273)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1273)
  AUTHORS   Laherty,C.D., Yang,W.M., Sun,J.M., Davie,J.R., Seto,E. and
            Eisenman,R.N.
  TITLE     Histone deacetylases associated with the mSin3 corepressor mediate
            mad transcriptional repression
  JOURNAL   Cell 89 (3), 349-356 (1997)
   PUBMED   9150134
  REMARK    GeneRIF: mSin3A interacts with HDAC2 via the HDAC-interacting
            domain (HID) of mSin3A.
            GeneRIF: The transcriptional repressor mSin3A associates with
            histone deacetylase 1 forming a co-repressor complex. See also PMID
            (PubMed identifier) 9150133.
REFERENCE   7  (residues 1 to 1273)
  AUTHORS   Hassig,C.A., Fleischer,T.C., Billin,A.N., Schreiber,S.L. and
            Ayer,D.E.
  TITLE     Histone deacetylase activity is required for full transcriptional
            repression by mSin3A
  JOURNAL   Cell 89 (3), 341-347 (1997)
   PUBMED   9150133
REFERENCE   8  (residues 1 to 1273)
  AUTHORS   Hurlin,P.J., Queva,C., Koskinen,P.J., Steingrimsson,E., Ayer,D.E.,
            Copeland,N.G., Jenkins,N.A. and Eisenman,R.N.
  TITLE     Mad3 and Mad4: novel Max-interacting transcriptional repressors
            that suppress c-myc dependent transformation and are expressed
            during neural and epidermal differentiation
  JOURNAL   EMBO J 14 (22), 5646-5659 (1995)
   PUBMED   8521822
  REMARK    Erratum:[EMBO J. 1996 Apr 15;15(8):2030. PMID: 8617250]
REFERENCE   9  (residues 1 to 1273)
  AUTHORS   Halleck,M.S., Pownall,S., Harder,K.W., Duncan,A.M., Jirik,F.R. and
            Schlegel,R.A.
  TITLE     A widely distributed putative mammalian transcriptional regulator
            containing multiple paired amphipathic helices, with similarity to
            yeast SIN3
  JOURNAL   Genomics 26 (2), 403-406 (1995)
   PUBMED   7601471
REFERENCE   10 (residues 1 to 1273)
  AUTHORS   Ayer,D.E., Lawrence,Q.A. and Eisenman,R.N.
  TITLE     Mad-Max transcriptional repression is mediated by ternary complex
            formation with mammalian homologs of yeast repressor Sin3
  JOURNAL   Cell 80 (5), 767-776 (1995)
   PUBMED   7889570
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC105137.18 and AC068338.14.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_006720528.1, XP_054233663.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            regulatory protein. It contains paired amphipathic helix (PAH)
            domains, which are important for protein-protein interactions and
            may mediate repression by the Mad-Max complex. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.11568.1,
                                           SRR18074969.2393589.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.2"
     Protein         1..1273
                     /product="paired amphipathic helix protein Sin3a"
                     /note="transcriptional co-repressor Sin3A; histone
                     deacetylase complex subunit Sin3a; transcriptional
                     corepressor Sin3a; transcriptional regulator, SIN3A; SIN3
                     homolog A, transcription regulator"
                     /calculated_mol_wt=145045
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          5..1213
                     /region_name="Sin3"
                     /note="Histone deacetylase complex, regulatory component
                     SIN3 [Chromatin structure and dynamics]; COG5602"
                     /db_xref="CDD:227889"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          87..110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          119..196
                     /region_name="Interaction with HCFC1.
                     /evidence=ECO:0000269|PubMed:12670868"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          205..480
                     /region_name="Interaction with REST.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          205..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q60520; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          398..446
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          458..525
                     /region_name="Interaction with SAP30.
                     /evidence=ECO:0000250|UniProtKB:Q60520"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            469
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          523..850
                     /region_name="Interaction with NCOR1.
                     /evidence=ECO:0000250|UniProtKB:Q60520"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          524..659
                     /region_name="Interaction with SUDS3 and SAP130.
                     /evidence=ECO:0000269|PubMed:12724404"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          687..829
                     /region_name="Interaction with HDAC1 and ARID4B.
                     /evidence=ECO:0000269|PubMed:12724404"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            832
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            860
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            865
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60520; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            875
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60520; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          888..967
                     /region_name="Interaction with OGT.
                     /evidence=ECO:0000269|PubMed:12150998"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            940
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            1089
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            1112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          1136..1156
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     CDS             1..1273
                     /gene="SIN3A"
                     /gene_synonym="CHR15DELq24; DEL15Q24; WITKOS"
                     /coded_by="NM_001437463.1:62..3883"
                     /db_xref="GeneID:25942"
                     /db_xref="HGNC:HGNC:19353"
                     /db_xref="MIM:607776"
ORIGIN      
        1 mkrrlddqes pvyaaqqrri pgsteafphq hrvlapappv yeavsetmqs atgiqysvtp
       61 syqvsampqs sgshgpaiaa vhsshhhpta vqphggqvvq shahpappva pvqgqqqfqr
      121 lkvedalsyl dqvklqfgsq pqvyndfldi mkefksqsid tpgvisrvsq lfkghpdlim
      181 gfntflppgy kievqtndmv nvttpgqvhq ipthgiqpqp qpppqhpsqp saqsapapaq
      241 papqpppakv skpsqlqaht pasqqtpplp pyasprsppv qphtpvtisl gtapslqnnq
      301 pvefnhainy vnkiknrfqg qpdiykafle ilhtyqkeqr nakeaggnyt palteqevya
      361 qvarlfknqe dllsefgqfl pdanssvlls kttaekvdsv rndhggtvkk pqlnnkpqrp
      421 sqngcqirrh ptgttppvkk kpkllnlkds smadaskhgg gteslffdkv rkalrsaeay
      481 enflrclvif nqevisrael vqlvspflgk fpelfnwfkn flgykesvhl etypkerate
      541 giameidyas ckrlgssyra lpksyqqpkc tgrtplckev lndtwvsfps wsedstfvss
      601 kktqyeehiy rcederfeld vvletnlati rvleaiqkkl srlsaeeqak frldntlggt
      661 sevihrkalq riyadkaadi idglrknpsi avpivlkrlk mkeeewreaq rgfnkvwreq
      721 nekyylksld hqginfkqnd tkvlrsksll neiesiyder qeqateenag vpvgphlsla
      781 yedkqileda aaliihhvkr qtgiqkedky kikqimhhfi pdllfaqrgd lsdveeeeee
      841 emdvdeatga vkkhngvggs ppkskllfsn taaqklrgmd evynlfyvnn nwyifmrlhq
      901 ilclrllric sqaerqieee nrerewerev lgikrdksds paiqlrlkep mdvdvedyyp
      961 afldmvrsll dgnidssqye dslremftih ayiaftmdkl iqsivrqlqh ivsdeicvqv
     1021 tdlylaennn gatggqlntq nsrsllesty qrkaeqlmsd encfklmfiq sqgqvqltie
     1081 lldteeensd dpveaerwsd yverymnsdt tspelrehla qkpvflprnl rrirkcqrgr
     1141 eqqekegkeg nskktmenvd sldklecrfk lnsykmvyvi ksedymyrrt allrahqshe
     1201 rvskrlhqrf qawvdkwtke hvpremaaet skwlmgegle glvpctttcd tetlhfvsin
     1261 kyrvkygtvf kap
//
LOCUS       NP_001427995             536 aa            linear   PRI 21-NOV-2025
DEFINITION  inhibitor of nuclear factor kappa-B kinase subunit alpha isoform 8
            [Homo sapiens].
ACCESSION   NP_001427995
VERSION     NP_001427995.1
DBSOURCE    REFSEQ: accession NM_001441066.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Chen,X., Wu,W., Jeong,J.H., Rokavec,M., Wei,R., Feng,S.,
            Schroth,W., Brauch,H., Zhong,S. and Luo,J.L.
  TITLE     Cytokines-activated nuclear IKKalpha-FAT10 pathway induces breast
            cancer tamoxifen-resistance
  JOURNAL   Sci China Life Sci 67 (7), 1413-1426 (2024)
   PUBMED   38565741
  REMARK    GeneRIF: Cytokines-activated nuclear IKKalpha-FAT10 pathway induces
            breast cancer tamoxifen-resistance.
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Chang,X., Guo,Y., Zhang,Q., Zheng,X., Cui,X., Hu,J., Zhang,Z.,
            Zhang,F. and Wang,X.
  TITLE     GRP78 recognizes EV-F 3D protein and activates NF-kappaB to repress
            virus replication by interacting with CHUK/IKBKB
  JOURNAL   J Virol 98 (6), e0026824 (2024)
   PUBMED   38775480
  REMARK    GeneRIF: GRP78 recognizes EV-F 3D protein and activates NF-kappaB
            to repress virus replication by interacting with CHUK/IKBKB.
REFERENCE   4  (residues 1 to 536)
  AUTHORS   McIntosh,K., Khalaf,Y.H., Craig,R., West,C., McCulloch,A.,
            Waghmare,A., Lawson,C., Chan,E.Y.W., Mackay,S., Paul,A. and
            Plevin,R.
  TITLE     IL-1beta stimulates a novel, IKKalpha -dependent, NIK -independent
            activation of non-canonical NFkappaB signalling
  JOURNAL   Cell Signal 107, 110684 (2023)
   PUBMED   37080443
  REMARK    GeneRIF: IL-1beta stimulates a novel, IKKalpha -dependent, NIK
            -independent activation of non-canonical NFkappaB signalling.
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Yang,H., Espada,C.E., Phillips,S., Martinez,N., Kenney,A.D.,
            Yount,J.S., Xiong,Y. and Wu,L.
  TITLE     The host antiviral protein SAMHD1 suppresses NF-kappaB activation
            by interacting with the IKK complex during inflammatory responses
            and viral infection
  JOURNAL   J Biol Chem 299 (6), 104750 (2023)
   PUBMED   37100289
  REMARK    GeneRIF: The host antiviral protein SAMHD1 suppresses NF-kappaB
            activation by interacting with the IKK complex during inflammatory
            responses and viral infection.
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Scherer,D.C., Brockman,J.A., Chen,Z., Maniatis,T. and Ballard,D.W.
  TITLE     Signal-induced degradation of I kappa B alpha requires
            site-specific ubiquitination
  JOURNAL   Proc Natl Acad Sci U S A 92 (24), 11259-11263 (1995)
   PUBMED   7479976
REFERENCE   7  (residues 1 to 536)
  AUTHORS   Mock,B.A., Connelly,M.A., McBride,O.W., Kozak,C.A. and Marcu,K.B.
  TITLE     CHUK, a conserved helix-loop-helix ubiquitous kinase, maps to human
            chromosome 10 and mouse chromosome 19
  JOURNAL   Genomics 27 (2), 348-351 (1995)
   PUBMED   7558004
REFERENCE   8  (residues 1 to 536)
  AUTHORS   Connelly,M.A. and Marcu,K.B.
  TITLE     CHUK, a new member of the helix-loop-helix and leucine zipper
            families of interacting proteins, contains a serine-threonine
            kinase catalytic domain
  JOURNAL   Cell Mol Biol Res 41 (6), 537-549 (1995)
   PUBMED   8777433
REFERENCE   9  (residues 1 to 536)
  AUTHORS   Ganchi,P.A., Sun,S.C., Greene,W.C. and Ballard,D.W.
  TITLE     A novel NF-kappa B complex containing p65 homodimers: implications
            for transcriptional control at the level of subunit dimerization
  JOURNAL   Mol Cell Biol 13 (12), 7826-7835 (1993)
   PUBMED   8246997
REFERENCE   10 (residues 1 to 536)
  AUTHORS   Ganchi,P.A., Sun,S.C., Greene,W.C. and Ballard,D.W.
  TITLE     I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B
            p65 and requires the transactivation domain to inhibit NF-kappa B
            p65 DNA binding
  JOURNAL   Mol Biol Cell 3 (12), 1339-1352 (1992)
   PUBMED   1493333
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138921.14.
            
            Summary: This gene encodes a member of the serine/threonine protein
            kinase family. The encoded protein, a component of a
            cytokine-activated protein complex that is an inhibitor of the
            essential transcription factor NF-kappa-B complex, phosphorylates
            sites that trigger the degradation of the inhibitor via the
            ubiquination pathway, thereby activating the transcription factor.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2404286.1,
                                           SRR14038193.2177087.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.31"
     Protein         1..536
                     /product="inhibitor of nuclear factor kappa-B kinase
                     subunit alpha isoform 8"
                     /EC_number="2.7.11.10"
                     /note="I-kappa-B kinase-alpha; I-kappa-B kinase 1; Nuclear
                     factor NFkappaB inhibitor kinase alpha; IKK-a kinase; IkB
                     kinase alpha subunit; inhibitor of nuclear factor kappa-B
                     kinase subunit alpha; conserved helix-loop-helix
                     ubiquitous kinase; transcription factor 16"
                     /calculated_mol_wt=60971
     Region          <21..100
                     /region_name="PKc_like"
                     /note="Protein Kinases, catalytic domain; cl21453"
                     /db_xref="CDD:473864"
     Region          102..178
                     /region_name="Ubl_IKKA_like"
                     /note="ubiquitin-like (Ubl) domain found in inhibitor of
                     nuclear factor kappa-B kinases, IKK-alpha and IKK-beta,
                     and similar proteins; cd17046"
                     /db_xref="CDD:340566"
     Region          177..450
                     /region_name="IKBKB_SDD"
                     /note="IQBAL scaffold dimerization domain; pfam18397"
                     /db_xref="CDD:465745"
     Region          498..534
                     /region_name="IKKbetaNEMObind"
                     /note="I-kappa-kinase-beta NEMO binding domain; pfam12179"
                     /db_xref="CDD:463485"
     CDS             1..536
                     /gene="CHUK"
                     /gene_synonym="BPS2; IKBKA; IKK-1; IKK-alpha; IKK1; IKKA;
                     NFKBIKA; TCF16"
                     /coded_by="NM_001441066.1:567..2177"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:1147"
                     /db_xref="HGNC:HGNC:1974"
                     /db_xref="MIM:600664"
ORIGIN      
        1 mpkmlikevc vhllwehcsi whekikkkdp kcifaceems gevrfsshlp qpnslcslvv
       61 epmenwlqlm lnwdpqqrgg pvdltlkqpr cfvlmdhiln lkivhilnmt sakiisfllp
      121 pdeslhslqs rieretgint gsqellsetg isldprkpas qcvldgvrgc dsymvylfdk
      181 sktvyegpfa srslsdcvny ivqdskiqlp iiqlrkvwae avhyvsglke dysrlfqgqr
      241 aamlsllryn anltkmkntl isasqqlkak leffhksiql dleryseqmt ygissekmlk
      301 awkemeekai hyaevgvigy ledqimslha eimelqkspy grrqgdlmes leqraidlyk
      361 qlkhrpsdhs ysdstemvki ivhtvqsqdr vlkelfghls kllgckqkii dllpkveval
      421 snikeadntv mfmqgkrqke iwhllkiact qssarslvgs slegavtpqt sawlpptsae
      481 hdhslscvvt pqdgetsaqm ieenlnclgh lstiiheane eqgnsmmnld wswlte
//
LOCUS       NP_001400251             280 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 3 [Homo sapiens].
ACCESSION   NP_001400251
VERSION     NP_001400251.1
DBSOURCE    REFSEQ: accession NM_001413322.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 280)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 280)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 280)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.57501.1,
                                           SRR1660803.95412.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..280
                     /product="RNA-binding Raly-like protein isoform 3"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=30943
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          188..>233
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     CDS             1..280
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413322.1:317..1159"
                     /note="isoform 3 is encoded by transcript variant 48"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly sgyvfdydyy
      121 rddfynrlfd yhgrvppppr aviplkrprv avtttrrgkg vfsmkggsrs tasgstgskl
      181 ksdelqtikk eltqiktkid sllgrlekie kqqkaeaeaq kkqleeslvl iqeecvseia
      241 dhsteepaeg gpdadgeemt dgieedfded gghelflqik
//
LOCUS       NP_055792               1341 aa            linear   PRI 21-NOV-2025
DEFINITION  apoptotic chromatin condensation inducer in the nucleus isoform 1
            [Homo sapiens].
ACCESSION   NP_055792
VERSION     NP_055792.2
DBSOURCE    REFSEQ: accession NM_014977.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1341)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1341)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1341)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1341)
  AUTHORS   Chen,Y.S., Liu,C.W., Lin,Y.C., Tsai,C.Y., Yang,C.H. and Lin,J.C.
  TITLE     The SRSF3-MBNL1-Acin1 circuit constitutes an emerging axis to
            lessen DNA fragmentation in colorectal cancer via an alternative
            splicing mechanism
  JOURNAL   Neoplasia 22 (12), 702-713 (2020)
   PUBMED   33142236
  REMARK    GeneRIF: The SRSF3-MBNL1-Acin1 circuit constitutes an emerging axis
            to lessen DNA fragmentation in colorectal cancer via an alternative
            splicing mechanism.
REFERENCE   5  (residues 1 to 1341)
  AUTHORS   Xue,L., Xie,L., Song,X. and Song,X.
  TITLE     [Expression and Significance of ACIN1 mRNA in Platelets of Lung
            Cancer]
  JOURNAL   Zhongguo Fei Ai Za Zhi 21 (9), 677-681 (2018)
   PUBMED   30201066
  REMARK    GeneRIF: ACIN1 mRNA was highly expressed in platelets of lung
            cancer patients
REFERENCE   6  (residues 1 to 1341)
  AUTHORS   Hu,Y., Yao,J., Liu,Z., Liu,X., Fu,H. and Ye,K.
  TITLE     Akt phosphorylates acinus and inhibits its proteolytic cleavage,
            preventing chromatin condensation
  JOURNAL   EMBO J 24 (20), 3543-3554 (2005)
   PUBMED   16177823
  REMARK    GeneRIF: Akt phosphorylation of acinus on serine 422 and 573
            results in its resistance to caspase cleavage in the nucleus and
            the inhibition of acinus-dependent chromatin condensation.
REFERENCE   7  (residues 1 to 1341)
  AUTHORS   Schwerk,C., Prasad,J., Degenhardt,K., Erdjument-Bromage,H.,
            White,E., Tempst,P., Kidd,V.J., Manley,J.L., Lahti,J.M. and
            Reinberg,D.
  TITLE     ASAP, a novel protein complex involved in RNA processing and
            apoptosis
  JOURNAL   Mol Cell Biol 23 (8), 2981-2990 (2003)
   PUBMED   12665594
REFERENCE   8  (residues 1 to 1341)
  AUTHORS   Sordet,O., Rebe,C., Plenchette,S., Zermati,Y., Hermine,O.,
            Vainchenker,W., Garrido,C., Solary,E. and Dubrez-Daloz,L.
  TITLE     Specific involvement of caspases in the differentiation of
            monocytes into macrophages
  JOURNAL   Blood 100 (13), 4446-4453 (2002)
   PUBMED   12393560
REFERENCE   9  (residues 1 to 1341)
  AUTHORS   Zermati,Y., Garrido,C., Amsellem,S., Fishelson,S., Bouscary,D.,
            Valensi,F., Varet,B., Solary,E. and Hermine,O.
  TITLE     Caspase activation is required for terminal erythroid
            differentiation
  JOURNAL   J Exp Med 193 (2), 247-254 (2001)
   PUBMED   11208865
REFERENCE   10 (residues 1 to 1341)
  AUTHORS   Sahara,S., Aoto,M., Eguchi,Y., Imamoto,N., Yoneda,Y. and
            Tsujimoto,Y.
  TITLE     Acinus is a caspase-3-activated protein required for apoptotic
            chromatin condensation
  JOURNAL   Nature 401 (6749), 168-173 (1999)
   PUBMED   10490026
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL117258.4 and AL132780.5.
            
            On Dec 12, 2023 this sequence version replaced NP_055792.1.
            
            Summary: Apoptosis is defined by several morphologic nuclear
            changes, including chromatin condensation and nuclear
            fragmentation. This gene encodes a nuclear protein that induces
            apoptotic chromatin condensation after activation by caspase-3,
            without inducing DNA fragmentation. This protein has also been
            shown to be a component of a splicing-dependent multiprotein exon
            junction complex (EJC) that is deposited at splice junctions on
            mRNAs, as a consequence of pre-mRNA splicing. It may thus be
            involved in mRNA metabolism associated with splicing. Alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1), also known as
            ACINUS-L.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF124726.1, AB014570.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..1341
                     /product="apoptotic chromatin condensation inducer in the
                     nucleus isoform 1"
                     /note="apoptotic chromatin condensation inducer in the
                     nucleus; functional spliceosome-associated protein 152"
                     /calculated_mol_wt=151731
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          72..106
                     /region_name="SAP"
                     /note="Putative DNA-binding (bihelical) motif predicted to
                     be involved in chromosomal organisation; smart00513"
                     /db_xref="CDD:128789"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          159..460
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          <210..413
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            388
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            453
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          475..530
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          548..865
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            561
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            654
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, by EHMT2, alternate.
                     /evidence=ECO:0000269|PubMed:18438403;
                     N6,N6-dimethyllysine, by EHMT2, alternate.
                     /evidence=ECO:0000269|PubMed:18438403; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            682
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            710
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            714
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            717
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            825
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     Phosphoserine. /evidence=ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            838
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            861
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9JIX8; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          892..953
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            895
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            898
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            976
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            987
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            990
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            1004
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          1011..1097
                     /region_name="RRM_ACINU"
                     /note="RNA recognition motif (RRM) found in apoptotic
                     chromatin condensation inducer in the nucleus (acinus) and
                     similar proteins; cd12432"
                     /db_xref="CDD:409866"
     Site            1093..1094
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          1098..1341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            1180
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by SRPK2 and PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:18559500; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          <1206..1236
                     /region_name="RSB_motif"
                     /note="RNSP1-SAP18 binding (RSB) motif; pfam16294"
                     /db_xref="CDD:465085"
     Region          1210..1237
                     /region_name="Sufficient for interaction with RNPS1 and
                     SAP18 and formation of the ASAP complex.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     CDS             1..1341
                     /gene="ACIN1"
                     /gene_synonym="ACINUS; ACN; fSAP152"
                     /coded_by="NM_014977.4:186..4211"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9587.1"
                     /db_xref="GeneID:22985"
                     /db_xref="HGNC:HGNC:17066"
                     /db_xref="MIM:604562"
ORIGIN      
        1 mwrrkhprts ggtrgvlsgn rgveygsgrg hlgtfegrwr klpkmpeavg tdpstsrkma
       61 eleevtldgk plqalrvtdl kaaleqrgla ksgqksalvk rlkgalmlen lqkhstphaa
      121 fqpnsqigee msqnsfikqy lekqqellrq rlereareaa eleeasaese demihpegva
      181 sllppdfqss lerpelelsr hsprksssis eekgdsddek prkgerrssr vrqaraakls
      241 egsqpaeeee dqetpsrnlr vradrnlkte eeeeeeeeee eddeeeegdd egqksreapi
      301 lkefkeegee iprvkpeemm derpktrsqe qevlerggrf trsqeearks hlarqqqeke
      361 mkttspleee ereikssqgl kekskspspp rltedrkkas lvalpeqtas eeetpppllt
      421 keassppphp qlhseeeiep megpapavli qlsppntdad trellvsqht vqlvgglspl
      481 sspsdtkaes paekvpeesv lplvqkstla dysaqkdlep esdrsaqplp lkieelalak
      541 giteeclkqp sleqkegrra shtllpshrl kqsadssssr sssssssssr srsrspdssg
      601 srshsplrsk qrdvaqarth anprgrpkmg srstsesrsr srsrsrsass nsrkslspgv
      661 srdsstsyte tkdpssgqev atppvpqlqv cepkertsts sssvqarrls qpesaekhvt
      721 qrlqpergsp kkceaeeaep paatqpqtse tqtshlpese rihhtveeke evtmdtsenr
      781 pendvpeppm piadqvsndd rpegsvedee kkesslpksf krkisvvsat kgvpagnsdt
      841 eggqpgrkrr wgastattqk kpsisittes lkslipdikp lagqeavvdl haddsrised
      901 eterngddgt hdkglkicrt vtqvvpaegq engqreeeee ekepeaeppv ppqvsveval
      961 pppaehevkk vtlgdtltrr sisqqksgvs itiddpvrta qvpspprgki snivhisnlv
     1021 rpftlgqlke llgrtgtlve eafwidkiks hcfvtystve eavatrtalh gvkwpqsnpk
     1081 flcadyaeqd eldyhrgllv drpsetktee qgiprplhpp ppppvqppqh praeqreqer
     1141 avreqwaere remerrertr serewdrdkv regprsrsrs rdrrrkerak skekksekke
     1201 kaqeeppakl lddlfrktka apciywlplt dsqivqkeae raerakerek rrkeqeeeeq
     1261 kerekeaere rnrqlerekr rehsrerdre rerererdrg drdrdrerdr ergrerdrrd
     1321 tkrhsrsrsr stpvrdrggr r
//
LOCUS       NP_001394266             281 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 36 [Homo sapiens].
ACCESSION   NP_001394266 XP_016878028
VERSION     NP_001394266.1
DBSOURCE    REFSEQ: accession NM_001407337.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            On May 31, 2022 this sequence version replaced XP_016878028.2.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1409698.1,
                                           SRR18074967.3947174.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..281
                     /product="tropomyosin alpha-1 chain isoform 36"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=32522
     Region          48..280
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..281
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407337.1:84..929"
                     /note="isoform 36 is encoded by transcript variant 36"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle delvslqkkl kgtedeldky
       61 sealkdaqek lelaekkatd aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegqv rqleeqlrim dqtlkalmaa edkysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledql yqqleqnrrl tnelklalne d
//
LOCUS       NP_001401581             537 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 2 isoform b [Homo sapiens].
ACCESSION   NP_001401581
VERSION     NP_001401581.1
DBSOURCE    REFSEQ: accession NM_001414652.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Jung,J.H., Lee,D., Ko,H.M. and Jang,H.J.
  TITLE     Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in Colorectal
            Cancer Cells by Activating p53
  JOURNAL   Biomolecules 11 (10), 1492 (2021)
   PUBMED   34680125
  REMARK    GeneRIF: Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in
            Colorectal Cancer Cells by Activating p53.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Royer-Bertrand,B., Cisarova,K., Niel Butschi,F., Foletti,G.,
            Guinchat,V., Tran,C., Superti-Furga,A. and Good,J.M.
  TITLE     CNOT2 haploinsufficiency in a 40-year-old man with intellectual
            disability, autism, and seizures
  JOURNAL   Am J Med Genet A 185 (8), 2602-2606 (2021)
   PUBMED   34018673
  REMARK    GeneRIF: CNOT2 haploinsufficiency in a 40-year-old man with
            intellectual disability, autism, and seizures.
            Review article
REFERENCE   4  (residues 1 to 537)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 537)
  AUTHORS   Jayne,S., Zwartjes,C.G., van Schaik,F.M. and Timmers,H.T.
  TITLE     Involvement of the SMRT/NCoR-HDAC3 complex in transcriptional
            repression by the CNOT2 subunit of the human Ccr4-Not complex
  JOURNAL   Biochem J 398 (3), 461-467 (2006)
   PUBMED   16712523
  REMARK    GeneRIF: This study shows that SMRT/NCoR-HDAC3 complex is a
            cofactor of CNOT2-mediated repression and suggests that
            transcriptional regulation by the Ccr4-Not complex involves
            regulation of chromatin modification.
REFERENCE   6  (residues 1 to 537)
  AUTHORS   Winkler,G.S., Mulder,K.W., Bardwell,V.J., Kalkhoven,E. and
            Timmers,H.T.
  TITLE     Human Ccr4-Not complex is a ligand-dependent repressor of nuclear
            receptor-mediated transcription
  JOURNAL   EMBO J 25 (13), 3089-3099 (2006)
   PUBMED   16778766
REFERENCE   7  (residues 1 to 537)
  AUTHORS   Shi,J. and Nelson,M.A.
  TITLE     The cyclin-dependent kinase 11 interacts with NOT2
  JOURNAL   Biochem Biophys Res Commun 334 (4), 1310-1316 (2005)
   PUBMED   16039607
  REMARK    GeneRIF: These findings suggest that CDK11 may contribute to
            apoptosis by regulating the activity of NOT2 independent of its
            kinase activity.
REFERENCE   8  (residues 1 to 537)
  AUTHORS   Zwartjes,C.G., Jayne,S., van den Berg,D.L. and Timmers,H.T.
  TITLE     Repression of promoter activity by CNOT2, a subunit of the
            transcription regulatory Ccr4-not complex
  JOURNAL   J Biol Chem 279 (12), 10848-10854 (2004)
   PUBMED   14707134
  REMARK    GeneRIF: major repression function of CNOT2 is localized in a
            specialized protein motif, the Not-Box
REFERENCE   9  (residues 1 to 537)
  AUTHORS   Denis,C.L. and Chen,J.
  TITLE     The CCR4-NOT complex plays diverse roles in mRNA metabolism
  JOURNAL   Prog Nucleic Acid Res Mol Biol 73, 221-250 (2003)
   PUBMED   12882519
  REMARK    Review article
REFERENCE   10 (residues 1 to 537)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092881.8 and AC025569.37.
            
            Summary: This gene encodes a subunit of the multi-component
            CCR4-NOT complex. The CCR4-NOT complex regulates mRNA synthesis and
            degradation and is also thought to be involved in mRNA splicing,
            transport and localization. The encoded protein interacts with
            histone deacetylases and functions as a repressor of polymerase II
            transcription. Alternatively spliced transcript variants have been
            observed for this gene. [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR12921934.2991684.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..537
                     /product="CCR4-NOT transcription complex subunit 2 isoform
                     b"
                     /note="negative regulator of transcription 2;
                     CCR4-associated factor 2; CC chemokine receptor 4-negative
                     regulator of transcription 2"
                     /calculated_mol_wt=59308
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Region          96..126
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C5L3; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C5L3; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Region          276..342
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Region          396..516
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..537
                     /gene="CNOT2"
                     /gene_synonym="CDC36; HSPC131; IDNADFS; NOT2; NOT2H"
                     /coded_by="NM_001414652.1:144..1757"
                     /note="isoform b is encoded by transcript variant 6"
                     /db_xref="GeneID:4848"
                     /db_xref="HGNC:HGNC:7878"
                     /db_xref="MIM:604909"
ORIGIN      
        1 mvrtdghtls ekrnyqvtns mfgasrkkfv egvdsdyhde nmyysqssmf phrsekdmla
       61 spstsgqlsq fgaslygqqs alglpmrgms nntpqlnrsl sqgtqlpshv tpttgvptms
      121 lhtppspsrg ilpmnprnmm nhsqvgqgig ipsrtnsmss sglgspnrss psiicmpkqq
      181 psrqpftvns msgfgmnrnq afgmnnslss nifngtdgse nvtgldlsdf paladrnrre
      241 gsgnptplin plagrapyvg mvtkpaneqs qdfsihnedf palpgssykd ptssnddsks
      301 nlntsgktts stdgpkfpgd kssttqnnnq qkkgiqvlpd grvtnipqgm vtdqfgmigl
      361 ltfiraaetd pgmvhlalgs dlttlglnln spenlypkfa spwasspcrp qdidfhvpse
      421 yltnihirdk laaiklgryg edllfylyym nggdvlqlla avelfnrdwr yhkeervwit
      481 rapgmeptmk tntyergtyy ffdclnwrke fhleydklee rphlpstfny npaqqaf
//
LOCUS       NP_001392786            1104 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001392786
VERSION     NP_001392786.1
DBSOURCE    REFSEQ: accession NM_001405857.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1104)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1104)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1104)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1104)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1104)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1104)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1104)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2453416.1,
                                           ERR4352444.783792.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1104
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 2"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=120707
     Site            104
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          145..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          225..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          399..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          849..881
                     /region_name="Required for activation of KAT8 histone
                     acetyltransferase activity"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          884..1004
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     Region          909..927
                     /region_name="Interaction with KAT8 HAT domain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01397"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          937..1033
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            990
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            993
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            1002
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            1044
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          1057..1104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     CDS             1..1104
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405857.1:697..4011"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankgli
      481 vlgevpppeh ttdlflplss evktdhgtdk liesvsqple nhgapiighi seslstkscg
      541 alrpvngvin tlqpvladhi pgdssdaeeq lhkkqrlnlv ssssdgtcva artrpvlsck
      601 krrlvrpnsi vplskkvhrn stirpgcdvn pscalcgsgs intmppeihy eapllerlsq
      661 ldscvhpvla fpddvptslh fqsmlksqwq nkpfdkikpp kklslkhrap mpgslpdsar
      721 kdrhklvssf lttaklshhq trpdrthrqh lddvgavpmv ervtapkaer llnppppvhd
      781 pnhskmrlrd hssersevlk hhtdmssssy laathhpphs plvrqlstss dspapassss
      841 qvtastsqpv rrrrgessfd innivipmsv aattrveklq ykeiltpswr evdlqslkgs
      901 pdeeneeied lsdaafaalh akceemerar wlwttsvppq rrgsrsyrss dgrttpqlgs
      961 anpstpqpas pdvssshsls eyshgqsprs pispelhsap ltpvardtpr hlasedtrcs
     1021 tpelgldeqs vqpwerrtfp lahspqaece dqldaqeraa rctrrtsgsk tgreteaapt
     1081 sppivplksr hlvaaataqr pthr
//
LOCUS       NP_001393556             846 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 15 [Homo sapiens].
ACCESSION   NP_001393556
VERSION     NP_001393556.1
DBSOURCE    REFSEQ: accession NM_001406627.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 846)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 846)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 846)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 846)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 846)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 846)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 846)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 846)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3457895.1,
                                           SRR14038191.3862643.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..846
                     /product="hamartin isoform 15"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=93697
     Region          <1..401
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <390..>642
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..846
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406627.1:1066..3606"
                     /note="isoform 15 is encoded by transcript variant 41"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mllnmpgqlp qtlsspstrl iteppqatlw spsmvcgmtt pptspgnvpp dlshpyskvf
       61 gttggkgtpl gtpatspppa plchsddyvh islpqatvtp prkeermdsa rpclhrqhhl
      121 lndrgseepp gskgsvtlsd lpgflgdlas eedsiekdke eaaisrelse ittaeaepvv
      181 prggfdspfy rdslpgsqrk thsaasssqg asvnpeplhs sldklgpdtp kqaftpidlp
      241 cgsadespag drecqtslet siftpspcki ppptrvgfgs gqpppydhlf evalpktahh
      301 fvirkteell kkakgnteed gvpstspmev ldrliqqgad ahskelnklp lpsksvdwth
      361 fggsppsdei rtlrdqllll hnqllyerfk rqqhalrnrr llrkvikaaa leehnaamkd
      421 qlklqekdiq mwkvslqkeq arynqlqeqr dtmvtklhsq irqlqhdree fynqsqelqt
      481 kledcrnmia elrielkkan nkvchtelll sqvsqklsns esvqqqmefl nrqllvlgev
      541 nelyleqlqn khsdttkeve mmkaayrkel eknrshvlqq tqrldtsqkr ileleshlak
      601 kdhllleqkk yledvklqar gqlqaaesry eaqkritqvf eleildlygr lekdgllkkl
      661 eeekaeaaea aeerldccnd gcsdsmvghn eeasghnget ktprpssarg ssgsrggggs
      721 ssssselstp ekpphqragp fssrwettmg easasipttv gslpssksfl gmkarelfrn
      781 ksesqcdedg mtsslseslk telgkdlgve akiplnldgp hpspptpdsv gqlhimdyne
      841 thhehs
//
LOCUS       NP_001400615             351 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 19 precursor [Homo sapiens].
ACCESSION   NP_001400615
VERSION     NP_001400615.1
DBSOURCE    REFSEQ: accession NM_001413686.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 351)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 351)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 351)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 351)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 351)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 351)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2142207.1,
                                           SRR14038191.1997583.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..351
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 19 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=35491
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..342
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            277..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            313..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     CDS             1..351
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413686.1:169..1224"
                     /note="isoform 19 precursor is encoded by transcript
                     variant 22"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvsyih gssqaqfvae shiilvlnaa itmgmvllne
      301 aatskgdvgk rriiclvglg lvvfffsfll sifrskyhgy pyssvfkdha d
//
LOCUS       NP_001427451             289 aa            linear   PRI 21-NOV-2025
DEFINITION  syntaxin-3 isoform 1 [Homo sapiens].
ACCESSION   NP_001427451 XP_005274252 XP_054225737
VERSION     NP_001427451.1
DBSOURCE    REFSEQ: accession NM_001440522.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Shinozuka,T., Kanda,M., Sato,Y., Shimizu,D., Tanaka,C., Umeda,S.,
            Inokawa,Y., Hattori,N., Hayashi,M., Nakayama,G. and Kodera,Y.
  TITLE     Increased STX3 transcript and protein levels were associated with
            poor prognosis in two independent cohorts of esophageal squamous
            cell carcinoma patients
  JOURNAL   Cancer Med 12 (24), 22185-22195 (2023)
   PUBMED   38014487
  REMARK    GeneRIF: Increased STX3 transcript and protein levels were
            associated with poor prognosis in two independent cohorts of
            esophageal squamous cell carcinoma patients.
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Janecke,A.R., Liu,X., Adam,R., Punuru,S., Viestenz,A., Strauss,V.,
            Laass,M., Sanchez,E., Adachi,R., Schatz,M.P., Saboo,U.S.,
            Mittal,N., Rohrschneider,K., Escher,J., Ganesh,A., Al Zuhaibi,S.,
            Al Murshedi,F., AlSaleem,B., Alfadhel,M., Al Sinani,S.,
            Alkuraya,F.S., Huber,L.A., Muller,T., Heidelberger,R. and Janz,R.
  TITLE     Pathogenic STX3 variants affecting the retinal and intestinal
            transcripts cause an early-onset severe retinal dystrophy in
            microvillus inclusion disease subjects
  JOURNAL   Hum Genet 140 (8), 1143-1156 (2021)
   PUBMED   33974130
  REMARK    GeneRIF: Pathogenic STX3 variants affecting the retinal and
            intestinal transcripts cause an early-onset severe retinal
            dystrophy in microvillus inclusion disease subjects.
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Low,S.H., Vasanji,A., Nanduri,J., He,M., Sharma,N., Koo,M.,
            Drazba,J. and Weimbs,T.
  TITLE     Syntaxins 3 and 4 are concentrated in separate clusters on the
            plasma membrane before the establishment of cell polarity
  JOURNAL   Mol Biol Cell 17 (2), 977-989 (2006)
   PUBMED   16339081
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Martin-Martin,B., Nabokina,S.M., Lazo,P.A. and Mollinedo,F.
  TITLE     Co-expression of several human syntaxin genes in neutrophils and
            differentiating HL-60 cells: variant isoforms and detection of
            syntaxin 1
  JOURNAL   J Leukoc Biol 65 (3), 397-406 (1999)
   PUBMED   10080545
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Steegmaier,M., Yang,B., Yoo,J.S., Huang,B., Shen,M., Yu,S., Luo,Y.
            and Scheller,R.H.
  TITLE     Three novel proteins of the syntaxin/SNAP-25 family
  JOURNAL   J Biol Chem 273 (51), 34171-34179 (1998)
   PUBMED   9852078
REFERENCE   8  (residues 1 to 289)
  AUTHORS   Riento,K., Galli,T., Jansson,S., Ehnholm,C., Lehtonen,E. and
            Olkkonen,V.M.
  TITLE     Interaction of Munc-18-2 with syntaxin 3 controls the association
            of apical SNAREs in epithelial cells
  JOURNAL   J Cell Sci 111 (Pt 17), 2681-2688 (1998)
   PUBMED   9701566
REFERENCE   9  (residues 1 to 289)
  AUTHORS   Galli,T., Zahraoui,A., Vaidyanathan,V.V., Raposo,G., Tian,J.M.,
            Karin,M., Niemann,H. and Louvard,D.
  TITLE     A novel tetanus neurotoxin-insensitive vesicle-associated membrane
            protein in SNARE complexes of the apical plasma membrane of
            epithelial cells
  JOURNAL   Mol Biol Cell 9 (6), 1437-1448 (1998)
   PUBMED   9614185
REFERENCE   10 (residues 1 to 289)
  AUTHORS   Delgrossi,M.H., Breuza,L., Mirre,C., Chavrier,P. and Le Bivic,A.
  TITLE     Human syntaxin 3 is localized apically in human intestinal cells
  JOURNAL   J Cell Sci 110 (Pt 18), 2207-2214 (1997)
   PUBMED   9378770
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000640.5.
            
            On or before May 21, 2025 this sequence version replaced
            XP_005274252.1, XP_054225737.1.
            
            Summary: The gene is a member of the syntaxin family. The encoded
            protein is targeted to the apical membrane of epithelial cells
            where it forms clusters and is important in establishing and
            maintaining polarity necessary for protein trafficking involving
            vesicle fusion and exocytosis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1177605.1,
                                           SRR14038195.1408733.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..289
                     /product="syntaxin-3 isoform 1"
                     /note="syntaxin 3A; syntaxin 3B"
                     /calculated_mol_wt=33024
     Region          34..226
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     Region          194..260
                     /region_name="SNARE"
                     /note="SNARE motif; cl22856"
                     /db_xref="CDD:473982"
     Site            order(222,229,232)
                     /site_type="other"
                     /note="flanking leucine-zipper layers"
                     /db_xref="CDD:277192"
     Site            225
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277192"
     Site            264..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13277.3)"
     CDS             1..289
                     /gene="STX3"
                     /gene_synonym="DIAR12; MVID2; RDMVID; STX3A"
                     /coded_by="NM_001440522.1:231..1100"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:6809"
                     /db_xref="HGNC:HGNC:11438"
                     /db_xref="MIM:600876"
ORIGIN      
        1 mkdrleqlka kqltqdddtd aveiaidnta fmdeffseie etrlnidkis ehveeakkly
       61 siilsapipe pktkddleql tteikkrann vrnklksmek hieedevrss adlrirksqh
      121 svlsrkfvev mtkyneaqvd frerskgriq rqleitgkkt tdeeleemle sgnpaiftsg
      181 iidsqiskqa lseiegrhkd ivrlessike lhdmfmdiam lvenqgemld nielnvmhtv
      241 dhvekardet kkavkyqsqa rkkliiiivl vvvllgilal iiglsvgln
//
LOCUS       NP_001171110             895 aa            linear   PRI 21-NOV-2025
DEFINITION  dystroglycan 1 preproprotein [Homo sapiens].
ACCESSION   NP_001171110
VERSION     NP_001171110.2
DBSOURCE    REFSEQ: accession NM_001177639.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 895)
  AUTHORS   Traverso,M., Baratto,S., Iacomino,M., Di Duca,M., Panicucci,C.,
            Casalini,S., Grandis,M., Falace,A., Torella,A., Picillo,E.,
            Onore,M.E., Politano,L., Nigro,V., Innes,A.M., Barresi,R.,
            Bruno,C., Zara,F., Fiorillo,C. and Scala,M.
  TITLE     DAG1 haploinsufficiency is associated with sporadic and familial
            isolated or pauci-symptomatic hyperCKemia
  JOURNAL   Eur J Hum Genet 32 (3), 342-349 (2024)
   PUBMED   38177406
  REMARK    GeneRIF: DAG1 haploinsufficiency is associated with sporadic and
            familial isolated or pauci-symptomatic hyperCKemia.
REFERENCE   2  (residues 1 to 895)
  AUTHORS   Shareef,S.H., Amin,K. and Janson,C.
  TITLE     The Association Between beta-Dystroglycan in Airway Smooth Muscle
            and Eosinophils in Allergic Asthma
  JOURNAL   Inflammation 44 (3), 1060-1068 (2021)
   PUBMED   33566255
  REMARK    GeneRIF: The Association Between beta-Dystroglycan in Airway Smooth
            Muscle and Eosinophils in Allergic Asthma.
REFERENCE   3  (residues 1 to 895)
  AUTHORS   Ortiz-Cordero,C., Magli,A., Dhoke,N.R., Kuebler,T., Selvaraj,S.,
            Oliveira,N.A., Zhou,H., Sham,Y.Y., Bang,A.G. and Perlingeiro,R.C.
  TITLE     NAD+ enhances ribitol and ribose rescue of alpha-dystroglycan
            functional glycosylation in human FKRP-mutant myotubes
  JOURNAL   Elife 10, e65443 (2021)
   PUBMED   33513091
  REMARK    GeneRIF: NAD+ enhances ribitol and ribose rescue of
            alpha-dystroglycan functional glycosylation in human FKRP-mutant
            myotubes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 895)
  AUTHORS   Gomez-Monsivais,W.L., Monterrubio-Ledezma,F., Huerta-Cantillo,J.,
            Mondragon-Gonzalez,R., Alamillo-Iniesta,A., Garcia-Aguirre,I.,
            Azuara-Medina,P.M., Arguello-Garcia,R., Rivera-Monroy,J.E.,
            Holaska,J.M., Hernandez-Mendez,J.M.E., Garrido,E., Magana,J.J.,
            Winder,S.J., Brancaccio,A., Martinez-Vieyra,I., Navarro-Garcia,F.
            and Cisneros,B.
  TITLE     The Molecular Basis and Biologic Significance of the
            beta-Dystroglycan-Emerin Interaction
  JOURNAL   Int J Mol Sci 21 (17), 5944 (2020)
   PUBMED   32824881
  REMARK    GeneRIF: The Molecular Basis and Biologic Significance of the
            beta-Dystroglycan-Emerin Interaction.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 895)
  AUTHORS   Beltran,D., Anderson,M.E., Bharathy,N., Settelmeyer,T.P.,
            Svalina,M.N., Bajwa,Z., Shern,J.F., Gultekin,S.H., Cuellar,M.A.,
            Yonekawa,T., Keller,C. and Campbell,K.P.
  TITLE     Exogenous expression of the glycosyltransferase LARGE1 restores
            alpha-dystroglycan matriglycan and laminin binding in
            rhabdomyosarcoma
  JOURNAL   Skelet Muscle 9 (1), 11 (2019)
   PUBMED   31054580
  REMARK    GeneRIF: findings demonstrate that a lack of matriglycan on
            alpha-dystroglycan is a common feature in rhabdomyosarcoma due to
            the downregulation of LARGE1, and that ectopic expression of LARGE1
            can restore matriglycan modifications and the ability of
            alpha-dystroglycan to function as an extracellular matrix receptor
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 895)
  AUTHORS   Apel,E.D., Roberds,S.L., Campbell,K.P. and Merlie,J.P.
  TITLE     Rapsyn may function as a link between the acetylcholine receptor
            and the agrin-binding dystrophin-associated glycoprotein complex
  JOURNAL   Neuron 15 (1), 115-126 (1995)
   PUBMED   7619516
REFERENCE   7  (residues 1 to 895)
  AUTHORS   Yang,B., Jung,D., Motto,D., Meyer,J., Koretzky,G. and Campbell,K.P.
  TITLE     SH3 domain-mediated interaction of dystroglycan and Grb2
  JOURNAL   J Biol Chem 270 (20), 11711-11714 (1995)
   PUBMED   7744812
REFERENCE   8  (residues 1 to 895)
  AUTHORS   Skynner,M.J., Gangadharan,U., Coulton,G.R., Mason,R.M.,
            Nikitopoulou,A., Brown,S.D. and Blanco,G.
  TITLE     Genetic mapping of the mouse neuromuscular mutation kyphoscoliosis
  JOURNAL   Genomics 25 (1), 207-213 (1995)
   PUBMED   7774920
REFERENCE   9  (residues 1 to 895)
  AUTHORS   Matsumura,K., Tome,F.M., Collin,H., Azibi,K., Chaouch,M.,
            Kaplan,J.C., Fardeau,M. and Campbell,K.P.
  TITLE     Deficiency of the 50K dystrophin-associated glycoprotein in severe
            childhood autosomal recessive muscular dystrophy
  JOURNAL   Nature 359 (6393), 320-322 (1992)
   PUBMED   1406935
REFERENCE   10 (residues 1 to 895)
  AUTHORS   Ibraghimov-Beskrovnaya,O., Ervasti,J.M., Leveille,C.J.,
            Slaughter,C.A., Sernett,S.W. and Campbell,K.P.
  TITLE     Primary structure of dystrophin-associated glycoproteins linking
            dystrophin to the extracellular matrix
  JOURNAL   Nature 355 (6362), 696-702 (1992)
   PUBMED   1741056
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104452.2.
            
            On Feb 23, 2022 this sequence version replaced NP_001171110.1.
            
            Summary: This gene encodes dystroglycan, a central component of
            dystrophin-glycoprotein complex that links the extracellular matrix
            and the cytoskeleton in the skeletal muscle. The encoded
            preproprotein undergoes O- and N-glycosylation, and proteolytic
            processing to generate alpha and beta subunits. Certain mutations
            in this gene are known to cause distinct forms of muscular
            dystrophy. Alternative splicing results in multiple transcript
            variants, all encoding the same protein. [provided by RefSeq, Nov
            2015].
            
            Transcript Variant: This variant (8) differs in the 5' UTR compared
            to variant 1. All variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1537833.1,
                                           SRR14038194.4340530.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..895
                     /product="dystroglycan 1 preproprotein"
                     /note="dystroglycan 1 (dystrophin-associated glycoprotein
                     1)"
                     /calculated_mol_wt=94326
     sig_peptide     1..29
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
                     /calculated_mol_wt=3134
     proprotein      30..895
                     /product="dystroglycan 1 proprotein"
                     /calculated_mol_wt=94326
     mat_peptide     30..653
                     /product="Alpha-dystroglycan. /id=PRO_0000021065"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14118.2)"
                     /calculated_mol_wt=67787
     Region          30..408
                     /region_name="Required for laminin recognition"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14118.2)"
     Region          62..163
                     /region_name="Dystroglycan_repeat"
                     /note="Cadherin-like repeat domain of alpha dystroglycan;
                     cd11303"
                     /db_xref="CDD:206636"
     Site            63
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:23234360; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     Site            141
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     Region          169..200
                     /region_name="O-glycosylated at one site"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14118.2)"
     Region          182..304
                     /region_name="a_DG1_N2"
                     /note="Alpha-Dystroglycan N-terminal domain 2; pfam18424"
                     /db_xref="CDD:465761"
     Site            order(199..200,204..205,207..208,211,222..228)
                     /site_type="other"
                     /note="CA-like domain interface [polypeptide binding]"
                     /db_xref="CDD:206765"
     Region          <303..>404
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          316..485
                     /region_name="Mucin-like domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14118.2)"
     Site            317
                     /site_type="glycosylation"
                     /note="O-linked (Man6P...) threonine.
                     /evidence=ECO:0000269|PubMed:21987822,
                     ECO:0000269|PubMed:24256719; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     Site            319
                     /site_type="glycosylation"
                     /note="O-linked (Man6P...) threonine.
                     /evidence=ECO:0000269|PubMed:21987822,
                     ECO:0000269|PubMed:24256719; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     Site            367
                     /site_type="glycosylation"
                     /note="O-linked (Hex...) threonine.
                     /evidence=ECO:0000269|PubMed:20507882; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     Site            369
                     /site_type="glycosylation"
                     /note="O-linked (Hex...) threonine.
                     /evidence=ECO:0000269|PubMed:20507882; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     Site            372
                     /site_type="glycosylation"
                     /note="O-linked (Hex...) threonine.
                     /evidence=ECO:0000269|PubMed:20507882; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     Site            379
                     /site_type="glycosylation"
                     /note="O-linked (Man6P...) threonine.
                     /evidence=ECO:0000269|PubMed:20044576,
                     ECO:0000269|PubMed:23723439; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     Region          381..460
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14118.2)"
     Site            381
                     /site_type="glycosylation"
                     /note="O-linked (Hex...) threonine.
                     /evidence=ECO:0000269|PubMed:20044576; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     Site            388
                     /site_type="glycosylation"
                     /note="O-linked (Hex...) threonine.
                     /evidence=ECO:0000269|PubMed:20044576; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     Site            455
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:20507882; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     Region          463..485
                     /region_name="O-glycosylated at seven sites with GalNAc"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14118.2)"
     Region          478..498
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14118.2)"
     Region          498..602
                     /region_name="Dystroglycan_repeat"
                     /note="Cadherin-like repeat domain of alpha dystroglycan;
                     cd11303"
                     /db_xref="CDD:206636"
     Region          606..895
                     /region_name="DAG1"
                     /note="Dystroglycan (Dystrophin-associated glycoprotein
                     1); pfam05454"
                     /db_xref="CDD:461655"
     Site            641
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     Site            649
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     Site            653..654
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:17905726; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     mat_peptide     654..895
                     /product="Beta-dystroglycan. /id=PRO_0000021066"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14118.2)"
                     /calculated_mol_wt=26558
     Site            661
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:18764929; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     Site            715..716
                     /site_type="cleavage"
                     /note="Cleavage, by MMP9.
                     /evidence=ECO:0000269|PubMed:19946898; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     Region          724..746
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14118.2)"
     Site            750..775
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14118.2)"
     Region          776..782
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:20512930"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14118.2)"
     Site            790
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14118.2)"
     Region          819..895
                     /region_name="Required for interaction with CAV3.
                     /evidence=ECO:0000269|PubMed:10988290"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14118.2)"
     Region          823..895
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14118.2)"
     Region          880..895
                     /region_name="Required for binding DMD and UTRN"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14118.2)"
     Region          889..892
                     /region_name="PPXY motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14118.2)"
     Site            892
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:11495720,
                     ECO:0000269|PubMed:12795607, ECO:0000269|PubMed:20512930;
                     propagated from UniProtKB/Swiss-Prot (Q14118.2)"
     CDS             1..895
                     /gene="DAG1"
                     /gene_synonym="156DAG; A3a; AGRNR; DAG; LGMDR16; MDDGA9;
                     MDDGC7; MDDGC9"
                     /coded_by="NM_001177639.3:125..2812"
                     /db_xref="CCDS:CCDS2799.1"
                     /db_xref="GeneID:1605"
                     /db_xref="HGNC:HGNC:2666"
                     /db_xref="MIM:128239"
ORIGIN      
        1 mrmsvglsll lplsgrtfll llsvvmaqsh wpsepseavr dwenqleasm hsvlsdlhea
       61 vptvvgipdg tavvgrsfrv tiptdliass gdiikvsaag kealpswlhw dsqshtlegl
      121 pldtdkgvhy isvsatrlga ngshipqtss vfsievyped hselqsvrta spdpgevvss
      181 acaadepvtv ltvildadlt kmtpkqridl lhrmrsfsev elhnmklvpv vnnrlfdmsa
      241 fmagpgnakk vvengallsw klgcslnqns vpdihgveap aregamsaql gypvvgwhia
      301 nkkpplpkrv rrqihatptp vtaigpptta iqeppsrivp tptspaiapp tetmappvrd
      361 pvpgkptvti rtrgaiiqtp tlgpiqptrv seagttvpgq irptmtipgy veptavatpp
      421 ttttkkprvs tpkpatpstd stttttrrpt kkprtprpvp rvttkvsitr letaspptri
      481 rtttsgvprg gepnqrpelk nhidrvdawv gtyfevkips dtfydhedtt tdklkltlkl
      541 reqqlvgeks wvqfnsnsql myglpdsshv gkheyfmhat dkgglsavda feihvhrrpq
      601 gdraparfka kfvgdpalvl ndihkkialv kklafafgdr ncstitlqni trgsivvewt
      661 nntlplepcp keqiaglsrr iaeddgkprp afsnalepdf katsitvtgs gscrhlqfip
      721 vvpprrvpse apptevpdrd peksseddvy lhtvipavvv aailliagii amicyrkkrk
      781 gkltledqat fikkgvpiif adelddskpp psssmplilq eekaplpppe ypnqsvpett
      841 plnqdtmgey tplrdedpna ppyqppppft apmegkgsrp knmtpyrspp pyvpp
//
LOCUS       NP_001153147             588 aa            linear   PRI 21-NOV-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein Q isoform 4 [Homo sapiens].
ACCESSION   NP_001153147
VERSION     NP_001153147.1
DBSOURCE    REFSEQ: accession NM_001159675.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Ishtayeh,H., Galves,M., Barnatan,T.T., Berdichevsky,Y.,
            Amer-Sarsour,F., Pasmanik-Chor,M., Braverman,I., Blumen,S.C. and
            Ashkenazi,A.
  TITLE     Oculopharyngeal muscular dystrophy mutations link the RNA-binding
            protein HNRNPQ to autophagosome biogenesis
  JOURNAL   Aging Cell 22 (10), e13949 (2023)
   PUBMED   37559347
  REMARK    GeneRIF: Oculopharyngeal muscular dystrophy mutations link the
            RNA-binding protein HNRNPQ to autophagosome biogenesis.
REFERENCE   3  (residues 1 to 588)
  AUTHORS   Semino,F., Schroter,J., Willemsen,M.H., Bast,T., Biskup,S.,
            Beck-Woedl,S., Brennenstuhl,H., Schaaf,C.P., Kolker,S.,
            Hoffmann,G.F., Haack,T.B. and Syrbe,S.
  TITLE     Further evidence for de novo variants in SYNCRIP as the cause of a
            neurodevelopmental disorder
  JOURNAL   Hum Mutat 42 (9), 1094-1100 (2021)
   PUBMED   34157790
  REMARK    GeneRIF: Further evidence for de novo variants in SYNCRIP as the
            cause of a neurodevelopmental disorder.
REFERENCE   4  (residues 1 to 588)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 588)
  AUTHORS   Mourelatos,Z., Abel,L., Yong,J., Kataoka,N. and Dreyfuss,G.
  TITLE     SMN interacts with a novel family of hnRNP and spliceosomal
            proteins
  JOURNAL   EMBO J 20 (19), 5443-5452 (2001)
   PUBMED   11574476
REFERENCE   6  (residues 1 to 588)
  AUTHORS   Lau,P.P., Chang,B.H. and Chan,L.
  TITLE     Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a
            component of apobec-1 editosome
  JOURNAL   Biochem Biophys Res Commun 282 (4), 977-983 (2001)
   PUBMED   11352648
REFERENCE   7  (residues 1 to 588)
  AUTHORS   Blanc,V., Navaratnam,N., Henderson,J.O., Anant,S., Kennedy,S.,
            Jarmuz,A., Scott,J. and Davidson,N.O.
  TITLE     Identification of GRY-RBP as an apolipoprotein B RNA-binding
            protein that interacts with both apobec-1 and apobec-1
            complementation factor to modulate C to U editing
  JOURNAL   J Biol Chem 276 (13), 10272-10283 (2001)
   PUBMED   11134005
REFERENCE   8  (residues 1 to 588)
  AUTHORS   Grosset,C., Chen,C.Y., Xu,N., Sonenberg,N., Jacquemin-Sablon,H. and
            Shyu,A.B.
  TITLE     A mechanism for translationally coupled mRNA turnover: interaction
            between the poly(A) tail and a c-fos RNA coding determinant via a
            protein complex
  JOURNAL   Cell 103 (1), 29-40 (2000)
   PUBMED   11051545
REFERENCE   9  (residues 1 to 588)
  AUTHORS   Mizutani,A., Fukuda,M., Ibata,K., Shiraishi,Y. and Mikoshiba,K.
  TITLE     SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear
            ribonucleoprotein R, interacts with ubiquitous synaptotagmin
            isoforms
  JOURNAL   J Biol Chem 275 (13), 9823-9831 (2000)
   PUBMED   10734137
REFERENCE   10 (residues 1 to 588)
  AUTHORS   Harris,C.E., Boden,R.A. and Astell,C.R.
  TITLE     A novel heterogeneous nuclear ribonucleoprotein-like protein
            interacts with NS1 of the minute virus of mice
  JOURNAL   J Virol 73 (1), 72-80 (1999)
   PUBMED   9847309
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136082.22.
            
            Summary: This gene encodes a member of the cellular heterogeneous
            nuclear ribonucleoprotein (hnRNP) family. hnRNPs are RNA binding
            proteins that complex with heterogeneous nuclear RNA (hnRNA) and
            regulate alternative splicing, polyadenylation, and other aspects
            of mRNA metabolism and transport. The encoded protein plays a role
            in multiple aspects of mRNA maturation and is associated with
            several multiprotein complexes including the apoB RNA
            editing-complex and survival of motor neurons (SMN) complex.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene, and a pseudogene of this
            gene is located on the short arm of chromosome 20. [provided by
            RefSeq, Dec 2011].
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            coding region compared to variant 1. The resulting isoform (4) is
            shorter, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1001345.1,
                                           SRR18074967.2603744.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.3"
     Protein         1..588
                     /product="heterogeneous nuclear ribonucleoprotein Q
                     isoform 4"
                     /note="NS1-associated protein 1; heterogeneous nuclear
                     ribonucleoprotein Q; glycine- and tyrosine-rich
                     RNA-binding protein"
                     /calculated_mol_wt=65551
     Region          23..107
                     /region_name="NURR_hnRNPQ"
                     /note="NURR (N-terminal unit for RNA recognition) domain
                     found in heterogeneous nuclear ribonucleoprotein Q
                     (hnRNPQ) and similar proteins; cd21066"
                     /db_xref="CDD:410954"
     Region          103..580
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     CDS             1..588
                     /gene="SYNCRIP"
                     /gene_synonym="GRY-RBP; GRYRBP; hnRNP-Q; HNRNPQ; HNRPQ1;
                     NSAP1; PP68"
                     /coded_by="NM_001159675.2:103..1869"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS93967.1"
                     /db_xref="GeneID:10492"
                     /db_xref="HGNC:HGNC:16918"
                     /db_xref="MIM:616686"
ORIGIN      
        1 matehvngng teepmdttsa vihsenfqtl ldaglpqkva ekldeiyvag lvahsdlder
       61 aiealkefne dgalavlqqf kdsdlshvqn ksaflcgvmk tyrqrekqgt kvadsskgpd
      121 eakikaller tgytldvttg qrkyggpppd svysgqqpsv gteifvgkip rdlfedelvp
      181 lfekagpiwd lrlmmdpltg lnrgyafvtf ctkeaaqeav klynnheirs gkhigvcisv
      241 annrlfvgsi pksktkeqil eefskvtegl tdvilyhqpd dkkknrgfcf leyedhktaa
      301 qvkvlfvrnl antvteeile kafsqfgkle rvkklkdyaf ihfderdgav kameemngkd
      361 legenieivf akppdqkrke rkaqrqaakn qmyddyyyyg pphmppptrg rgrggrggyg
      421 yppdyygyed yydyygydyh nyrggyedpy ygyedfqvga rgrggrgarg aapsrgrgaa
      481 pprgragysq rggpgsargv rgarggaqqq rgrgvrgarg grggnvggkr kadgynqpds
      541 krrqtnnqnw gsqpiaqqpl qggdhsgnyg yksenqefyq dtfgqqwk
//
LOCUS       NP_001428149             476 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 2 [Homo sapiens].
ACCESSION   NP_001428149
VERSION     NP_001428149.1
DBSOURCE    REFSEQ: accession NM_001441220.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.2830180.1,
                                           SRR14038192.1028745.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..476
                     /product="calcium uptake protein 1, mitochondrial isoform
                     2"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=54220
     Region          68..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          99..110
                     /region_name="Polybasic region.
                     /evidence=ECO:0000269|PubMed:27099988"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCX5; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          126..129
                     /region_name="K/R-ring.
                     /evidence=ECO:0000269|PubMed:32494073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          222..441
                     /region_name="EFh_MICU1"
                     /note="EF-hand, calcium binding motif, found in calcium
                     uptake protein 1, mitochondrial (MICU1) and similar
                     proteins; cd16173"
                     /db_xref="CDD:320081"
     Region          222..251
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Site            order(224,376,379,382..383,385,403)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:320081"
     Site            order(231,233,235,242,421,423,425,432)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320081"
     Region          259..263
                     /region_name="K/R-ring.
                     /evidence=ECO:0000269|PubMed:32494073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          277..307
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          375..404
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          412..441
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          455..465
                     /region_name="C-helix region.
                     /evidence=ECO:0000269|PubMed:24514027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Site            455
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:27642082; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
     CDS             1..476
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001441220.1:188..1618"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mfrlnslsal aelavgsrwy hggsqpiqir rrlmmvaflg asavtastgl lwkrahaesp
       61 pcvdnlksdi gdkgknkdeg dvcnhekkta dlaphpeekk kkrsgfrdrk vmeyenrira
      121 ystpdkifry fatlkvisep geaevfmtpe dfvrsitpne kqpehlgldq yiikrfdgkk
      181 isqerekfad egsifytlge cglisfsdyi flttvlstpq rnfeiafkmf dlngdgevdm
      241 eefeqvqsii rsqtsmgmrh rdrpttgntl ksglcsaltt yffgadlkgk ltiknflefq
      301 rklqhdvlkl eferhdpvdg riterqfggm llaysgvqsk kltamqrqlk khfkegkglt
      361 fqevenfftf lknindvdta lsfyhmagas ldkvtmqqva rtvakvelsd hvcdvvfalf
      421 dcdgngelsn kefvsimkqr lmrglekpkd mgftrlmqam wkcaqetawd falpkq
//
LOCUS       NP_001393542            1098 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 10 [Homo sapiens].
ACCESSION   NP_001393542
VERSION     NP_001393542.1
DBSOURCE    REFSEQ: accession NM_001406613.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1098)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1098)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1098)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1098)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1098)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1098)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1098)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1098)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1098)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1098)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.469754.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1098
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1098
                     /product="hamartin isoform 10"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=122246
     Region          7..667
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <653..>890
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1098
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406613.1:189..3485"
                     /note="isoform 10 is encoded by transcript variant 27"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk mdtdvvvltt gvlvlitmlp mipqsgkqhl ldffdifgrl sswclkkpgh
      121 vaevylvhlh asvyalfhrl ygmypcnfvs flrshysmke nletfeevvk pmmehvrihp
      181 elvtgskdhe ldprrwkrle thdvviecak isldpteasy edgysvshqi sarfphrsad
      241 vttspyadtq nsygcatstp ystsrlmlln mpgqlpqtls spstrlitep pqatlwspsm
      301 vcgmttppts pgnvppdlsh pyskvfgttg gkgtplgtpa tspppaplch sddyvhislp
      361 qatvtpprke ermdsarpcl hrqhhllndr gseeppgskg svtlsdlpgf lgdlaseeds
      421 iekdkeeaai srelseitta eaepvvprgg fdspfyrdsl pgsqrkthsa asssqgasvn
      481 peplhssldk lgpdtpkqaf tpidlpcgsa despagdrec qtsletsift pspckipppt
      541 rvgfgsgqpp pydhlfeval pktahhfvir kteellkkak gnteedgvps tspmevldrl
      601 iqqgadahsk elnklplpsk svdwthfggs ppsdeirtlr dqllllhnql lyerfkrqqh
      661 alrnrrllrk vikaaaleeh naamkdqlkl qekdiqmwkv slqkeqaryn qlqeqrdtmv
      721 tklhsqirql qhdreefynq sqelqtkled crnmiaelri elkkannkls nsesvqqqme
      781 flnrqllvlg evnelyleql qnkhsdttke vemmkaayrk eleknrshvl qqtqrldtsq
      841 krileleshl akkdhllleq kkyledvklq argqlqaaes ryeaqkritq vfeleildly
      901 grlekdgllk kleeekaeaa eaaeerldcc ndgcsdsmvg hneeasghng etktprpssa
      961 rgssgsrggg gssssssels tpekpphqra gpfssrwett mgeasasipt tvgslpssks
     1021 flgmkarelf rnksesqcde dgmtsslses lktelgkdlg veakiplnld gphpspptpd
     1081 svgqlhimdy nethhehs
//
LOCUS       NP_001427458             287 aa            linear   PRI 21-NOV-2025
DEFINITION  syntaxin-3 isoform 5 [Homo sapiens].
ACCESSION   NP_001427458
VERSION     NP_001427458.1
DBSOURCE    REFSEQ: accession NM_001440529.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Shinozuka,T., Kanda,M., Sato,Y., Shimizu,D., Tanaka,C., Umeda,S.,
            Inokawa,Y., Hattori,N., Hayashi,M., Nakayama,G. and Kodera,Y.
  TITLE     Increased STX3 transcript and protein levels were associated with
            poor prognosis in two independent cohorts of esophageal squamous
            cell carcinoma patients
  JOURNAL   Cancer Med 12 (24), 22185-22195 (2023)
   PUBMED   38014487
  REMARK    GeneRIF: Increased STX3 transcript and protein levels were
            associated with poor prognosis in two independent cohorts of
            esophageal squamous cell carcinoma patients.
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Janecke,A.R., Liu,X., Adam,R., Punuru,S., Viestenz,A., Strauss,V.,
            Laass,M., Sanchez,E., Adachi,R., Schatz,M.P., Saboo,U.S.,
            Mittal,N., Rohrschneider,K., Escher,J., Ganesh,A., Al Zuhaibi,S.,
            Al Murshedi,F., AlSaleem,B., Alfadhel,M., Al Sinani,S.,
            Alkuraya,F.S., Huber,L.A., Muller,T., Heidelberger,R. and Janz,R.
  TITLE     Pathogenic STX3 variants affecting the retinal and intestinal
            transcripts cause an early-onset severe retinal dystrophy in
            microvillus inclusion disease subjects
  JOURNAL   Hum Genet 140 (8), 1143-1156 (2021)
   PUBMED   33974130
  REMARK    GeneRIF: Pathogenic STX3 variants affecting the retinal and
            intestinal transcripts cause an early-onset severe retinal
            dystrophy in microvillus inclusion disease subjects.
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Low,S.H., Vasanji,A., Nanduri,J., He,M., Sharma,N., Koo,M.,
            Drazba,J. and Weimbs,T.
  TITLE     Syntaxins 3 and 4 are concentrated in separate clusters on the
            plasma membrane before the establishment of cell polarity
  JOURNAL   Mol Biol Cell 17 (2), 977-989 (2006)
   PUBMED   16339081
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Martin-Martin,B., Nabokina,S.M., Lazo,P.A. and Mollinedo,F.
  TITLE     Co-expression of several human syntaxin genes in neutrophils and
            differentiating HL-60 cells: variant isoforms and detection of
            syntaxin 1
  JOURNAL   J Leukoc Biol 65 (3), 397-406 (1999)
   PUBMED   10080545
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Steegmaier,M., Yang,B., Yoo,J.S., Huang,B., Shen,M., Yu,S., Luo,Y.
            and Scheller,R.H.
  TITLE     Three novel proteins of the syntaxin/SNAP-25 family
  JOURNAL   J Biol Chem 273 (51), 34171-34179 (1998)
   PUBMED   9852078
REFERENCE   8  (residues 1 to 287)
  AUTHORS   Riento,K., Galli,T., Jansson,S., Ehnholm,C., Lehtonen,E. and
            Olkkonen,V.M.
  TITLE     Interaction of Munc-18-2 with syntaxin 3 controls the association
            of apical SNAREs in epithelial cells
  JOURNAL   J Cell Sci 111 (Pt 17), 2681-2688 (1998)
   PUBMED   9701566
REFERENCE   9  (residues 1 to 287)
  AUTHORS   Galli,T., Zahraoui,A., Vaidyanathan,V.V., Raposo,G., Tian,J.M.,
            Karin,M., Niemann,H. and Louvard,D.
  TITLE     A novel tetanus neurotoxin-insensitive vesicle-associated membrane
            protein in SNARE complexes of the apical plasma membrane of
            epithelial cells
  JOURNAL   Mol Biol Cell 9 (6), 1437-1448 (1998)
   PUBMED   9614185
REFERENCE   10 (residues 1 to 287)
  AUTHORS   Delgrossi,M.H., Breuza,L., Mirre,C., Chavrier,P. and Le Bivic,A.
  TITLE     Human syntaxin 3 is localized apically in human intestinal cells
  JOURNAL   J Cell Sci 110 (Pt 18), 2207-2214 (1997)
   PUBMED   9378770
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000640.5.
            
            Summary: The gene is a member of the syntaxin family. The encoded
            protein is targeted to the apical membrane of epithelial cells
            where it forms clusters and is important in establishing and
            maintaining polarity necessary for protein trafficking involving
            vesicle fusion and exocytosis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: MW273340.1, SRR1660807.97423.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..287
                     /product="syntaxin-3 isoform 5"
                     /note="syntaxin 3A; syntaxin 3B"
                     /calculated_mol_wt=32810
     Region          34..226
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     Region          194..260
                     /region_name="SNARE"
                     /note="SNARE motif; cl22856"
                     /db_xref="CDD:473982"
     Site            order(222,229,232)
                     /site_type="other"
                     /note="flanking leucine-zipper layers"
                     /db_xref="CDD:277192"
     Site            225
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277192"
     CDS             1..287
                     /gene="STX3"
                     /gene_synonym="DIAR12; MVID2; RDMVID; STX3A"
                     /coded_by="NM_001440529.1:231..1094"
                     /note="isoform 5 is encoded by transcript variant 10"
                     /db_xref="GeneID:6809"
                     /db_xref="HGNC:HGNC:11438"
                     /db_xref="MIM:600876"
ORIGIN      
        1 mkdrleqlka kqltqdddtd aveiaidnta fmdeffseie etrlnidkis ehveeakkly
       61 siilsapipe pktkddleql tteikkrann vrnklksmek hieedevrss adlrirksqh
      121 svlsrkfvev mtkyneaqvd frerskgriq rqleitgkkt tdeeleemle sgnpaiftsg
      181 iidsqiskqa lseiegrhkd ivrlessike lhdmfmdiam lvenqgsmid riennmdqsv
      241 gfveravadt kkavkyqsea rrkkimimic ciilaiilas tigsifa
//
LOCUS       NP_001425737            1038 aa            linear   PRI 21-NOV-2025
DEFINITION  NHS-like protein 2 isoform 5 [Homo sapiens].
ACCESSION   NP_001425737 XP_011529236 XP_054182942
VERSION     NP_001425737.1
DBSOURCE    REFSEQ: accession NM_001438808.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1038)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1038)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL929401.8 and BX119917.9.
            
            On or before Apr 24, 2025 this sequence version replaced
            XP_011529236.1, XP_054182942.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2153307,
                              SAMEA2156670 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..1038
                     /product="NHS-like protein 2 isoform 5"
                     /note="NHS-like protein 2; TPT1-like protein"
                     /calculated_mol_wt=111842
     Region          <338..568
                     /region_name="NHS"
                     /note="NHS-like; pfam15273"
                     /db_xref="CDD:464606"
     Region          <534..768
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1038
                     /gene="NHSL2"
                     /coded_by="NM_001438808.1:466..3582"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:340527"
                     /db_xref="HGNC:HGNC:33737"
                     /db_xref="MIM:301093"
ORIGIN      
        1 mptkrqlsed etttqgvrap easlslstta dkqtawnslf plpileekrw pqlcstqsdi
       61 vpinisgqqf dkhaslrhsl fntetavnpk stlrrrrtii gfsnfsqrdq ghsnspagsv
      121 ahsttsdirp shsvpegvhg rvavgqdarf psltspvlrt pssepdephq arsgpnppgm
      181 esmgmvysvp sscngptest fstswkgdaf tymtpsatsq snqvnengkn pscgnswvsl
      241 nkvpplvpke aatllvardn pagcsgsagy perliqqrhm perpskigll tsgtsrletg
      301 pggasrfrer slsvptdsgt tdvdydeeqk aneacalpfa stssegsnsa dniaslsaqq
      361 eaqhrrqrsk sislrkakkk pspptrsvsl vkdepgllpe ggsalpkdqr pkslclsleh
      421 qghhsshpda qghpaipnhk dpestqfshh wyltdwksgd tyqslsssst atgttviect
      481 qvqgssesla spstsrattp sqlsievear eisspgrppg lmspssgyss qsetptptvs
      541 msltlghlpp psssvrvrpv vperksslpp tspmekfpks rlsfdlplts spnldlsgms
      601 isirsktkvs rhhsetnfgv klaqktnpnq pimpmvtqsd lrsvrlrsvs ksepeddies
      661 peyaeeprae evftlperkt kppvaekppv arrppslvhk ppsvpeeyal tsptlamppr
      721 ssiqharplp qdsytvvrkp kpssfpdgrs pgestapssl vftpfasssd affsgtqqpp
      781 qgsvedegpk vrvlperisl qsqeeaekkk gkipppvpkk psvlylplts ptaqmeayva
      841 eprlplspii tleedtkcpa tgddlqslgq rvtstpqads ereasplgss vepgteeksl
      901 isdktaewia eddddvfvas rttedlftvi hrskrkllgw kepgeafvgg rtsshspikn
      961 taespisest atagsgssan ldagrnddfk allqkkgska tprsrpsaae llkttnplar
     1021 riiaqfskdy ettdnpst
//
LOCUS       NP_001400674             863 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform h [Homo sapiens].
ACCESSION   NP_001400674
VERSION     NP_001400674.1
DBSOURCE    REFSEQ: accession NM_001413745.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 863)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 863)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 863)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 863)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 863)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 863)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 863)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 863)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 863)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 863)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1537721.1,
                                           SRR18074969.2280621.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149178, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..863
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..863
                     /product="polyhomeotic-like protein 1 isoform h"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=91276
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          212..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          261..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          687..794
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          794..862
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(812..813,847..848,851..852,855)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(823..827,829..830,833..834,838,843)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..863
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413745.1:368..2959"
                     /note="isoform h is encoded by transcript variant 9"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq asinlattsa aqlisrsqsv
      121 sspsattltq svllgnttsp plnqsqaqmy lrpqlgnllq vnrtlgrnvp lasqlilmpn
      181 gavaavqqev psaqspgvha dadqvqnlav rnqqasaqgp qmqgstqkai ppgaspvssl
      241 sqassqalav aqassgatnq slnlsqaggg sgnsipgsmg pggggqahgg lgqlpssgmg
      301 ggscprkgtg vvqplpaaqt vtvsqgsqte aesaaakkae adgsgqqnvg mnltrtatpa
      361 psqtlissat ytqiqphsli qqqqqihlqq kqvviqqqia ihhqqqfqhr qsqllhtath
      421 lqlaqqqqqq qqqqqqqqqp qattltapqp pqvpptqqgt ahvvkggatt sspvvaqvpa
      481 afymqsvhlp gkpqtlavkr kadseeerdd vstlgsmlpa kaspvaespk vmdeksslge
      541 kaesvanvna ntpsselval tpapsvpppt lamvsrqmgd skppqaivkp qilthiiegf
      601 viqegaepfp vgcsqllkes ekplqtglpt gltenqsggp lgvdspsael dkkanllkce
      661 ycgkyapaeq frgskrfcsm tcakrynvsc shqfrlkrkk mkefqeanya rvrrrgprrs
      721 ssdiarakiq gkchrgqeds srgsdnssyd ealsptspgp lsvraghger dlgnpntapp
      781 tpelhginpv flssnpsrws veevyefias lqgcqeiaee frsqeidgqa llllkeehlm
      841 samniklgpa lkicakinvl ket
//
LOCUS       NP_001389629            1277 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 11 [Homo sapiens].
ACCESSION   NP_001389629
VERSION     NP_001389629.1
DBSOURCE    REFSEQ: accession NM_001402700.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1277)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1277)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1277)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1277)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1277)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1277)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1277)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1277)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1277)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1277)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.951351.1,
                                           SRR1660809.105595.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1277
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1277
                     /product="kinectin isoform 11"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=146845
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          316..>532
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          458..1217
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1277
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402700.1:179..4012"
                     /note="isoform 11 is encoded by transcript variant 23"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqlsitskvq
      841 elqnllkgke eqmntmkavl eekekdlant gkwlqdlqee neslkahvqe vaqhnlkeas
      901 sasqfeelei vlkekenelk rleamlkere sdlssktqll qdvqdenklf ksqieqlkqq
      961 nyqqassfpp heellkvise rekeisglwn eldslkdave hqrkknnerq qqveavelea
     1021 kevlkklfpk vsvpsnlsyg ewlhgfekka kecmagtsgs eevkvlehkl keademhtll
     1081 qlecekyksv laetegilqk lqrsveqeen kwkvkvdesh ktikqmqssf tsseqelerl
     1141 rsenkdienl rrerehleme lekaemerst yvtevrelka qlnetltklr teqnerqkva
     1201 gdlhkaqqsl eliqskivka agdttviens dvspetesse ketmsvslnq tvtqlqqllq
     1261 avnqqltkek ehyqvle
//
LOCUS       NP_001400293             469 aa            linear   PRI 21-NOV-2025
DEFINITION  telomeric repeat-binding factor 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001400293 XP_005251348
VERSION     NP_001400293.1
DBSOURCE    REFSEQ: accession NM_001413364.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Hu,H., van Roon,A.M., Ghanim,G.E., Ahsan,B., Oluwole,A.O.,
            Peak-Chew,S.Y., Robinson,C.V. and Nguyen,T.H.D.
  TITLE     Structural basis of telomeric nucleosome recognition by shelterin
            factor TRF1
  JOURNAL   Sci Adv 9 (34), eadi4148 (2023)
   PUBMED   37624885
  REMARK    GeneRIF: Structural basis of telomeric nucleosome recognition by
            shelterin factor TRF1.
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Harmak,H., Redouane,S., Charoute,H., Aniq Filali,O., Barakat,A. and
            Rouba,H.
  TITLE     In silico exploration and molecular dynamics of deleterious SNPs on
            the human TERF1 protein triggering male infertility
  JOURNAL   J Biomol Struct Dyn 41 (24), 14665-14688 (2023)
   PUBMED   36995171
  REMARK    GeneRIF: In silico exploration and molecular dynamics of
            deleterious SNPs on the human TERF1 protein triggering male
            infertility.
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Abreu,P.L., Lee,Y.W. and Azzalin,C.M.
  TITLE     In Vitro Characterization of the Physical Interactions between the
            Long Noncoding RNA TERRA and the Telomeric Proteins TRF1 and TRF2
  JOURNAL   Int J Mol Sci 23 (18), 10463 (2022)
   PUBMED   36142374
  REMARK    GeneRIF: In Vitro Characterization of the Physical Interactions
            between the Long Noncoding RNA TERRA and the Telomeric Proteins
            TRF1 and TRF2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 469)
  AUTHORS   Jack,A., Kim,Y., Strom,A.R., Lee,D.S.W., Williams,B., Schaub,J.M.,
            Kellogg,E.H., Finkelstein,I.J., Ferro,L.S., Yildiz,A. and
            Brangwynne,C.P.
  TITLE     Compartmentalization of telomeres through DNA-scaffolded phase
            separation
  JOURNAL   Dev Cell 57 (2), 277-290 (2022)
   PUBMED   35077681
  REMARK    GeneRIF: Compartmentalization of telomeres through DNA-scaffolded
            phase separation.
REFERENCE   6  (residues 1 to 469)
  AUTHORS   Broccoli,D., Chong,L., Oelmann,S., Fernald,A.A., Marziliano,N., van
            Steensel,B., Kipling,D., Le Beau,M.M. and de Lange,T.
  TITLE     Comparison of the human and mouse genes encoding the telomeric
            protein, TRF1: chromosomal localization, expression and conserved
            protein domains
  JOURNAL   Hum Mol Genet 6 (1), 69-76 (1997)
   PUBMED   9002672
REFERENCE   7  (residues 1 to 469)
  AUTHORS   Lu,K.P., Hanes,S.D. and Hunter,T.
  TITLE     A human peptidyl-prolyl isomerase essential for regulation of
            mitosis
  JOURNAL   Nature 380 (6574), 544-547 (1996)
   PUBMED   8606777
REFERENCE   8  (residues 1 to 469)
  AUTHORS   Bilaud,T., Koering,C.E., Binet-Brasselet,E., Ancelin,K.,
            Pollice,A., Gasser,S.M. and Gilson,E.
  TITLE     The telobox, a Myb-related telomeric DNA binding motif found in
            proteins from yeast, plants and human
  JOURNAL   Nucleic Acids Res 24 (7), 1294-1303 (1996)
   PUBMED   8614633
REFERENCE   9  (residues 1 to 469)
  AUTHORS   Chong,L., van Steensel,B., Broccoli,D., Erdjument-Bromage,H.,
            Hanish,J., Tempst,P. and de Lange,T.
  TITLE     A human telomeric protein
  JOURNAL   Science 270 (5242), 1663-1667 (1995)
   PUBMED   7502076
REFERENCE   10 (residues 1 to 469)
  AUTHORS   Zhong,Z., Shiue,L., Kaplan,S. and de Lange,T.
  TITLE     A mammalian factor that binds telomeric TTAGGG repeats in vitro
  JOURNAL   Mol Cell Biol 12 (11), 4834-4843 (1992)
   PUBMED   1406665
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022893.6.
            
            On Oct 31, 2022 this sequence version replaced XP_005251348.1.
            
            Summary: This gene encodes a telomere specific protein which is a
            component of the telomere nucleoprotein complex. This protein is
            present at telomeres throughout the cell cycle and functions as an
            inhibitor of telomerase, acting in cis to limit the elongation of
            individual chromosome ends. The protein structure contains a
            C-terminal Myb motif, a dimerization domain near its N-terminus and
            an acidic N-terminus. Multiple transcripts of this gene are
            alternatively spliced products. [provided by RefSeq, Aug 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2117425.1,
                                           SRR18074967.172580.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.11"
     Protein         1..469
                     /product="telomeric repeat-binding factor 1 isoform 4"
                     /note="NIMA-interacting protein 2; telomeric protein
                     Pin2/TRF1; TTAGGG repeat-binding factor 1; telomeric
                     repeat binding factor (NIMA-interacting) 1"
                     /calculated_mol_wt=53693
     Region          76..264
                     /region_name="TRFH"
                     /note="Telomeric Repeat binding Factor or TTAGGG Repeat
                     binding Factor, central (dimerization) domain Homology;
                     TRFH. Telomeres are protein/DNA complexes that make up the
                     physical ends of eukaryotic linear chromosomes and are
                     essential for chromosome stability; cd00280"
                     /db_xref="CDD:238174"
     Site            order(106,109,123,127,131,141..145,153,156..157,160)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238174"
     Region          411..459
                     /region_name="SANT_TRF"
                     /note="Telomere repeat binding factor-like DNA-binding
                     domains of the SANT/myb-like family; cd11660"
                     /db_xref="CDD:212558"
     Site            order(411..413,431,433..434,445,447..449,451..453,
                     455..456)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212558"
     CDS             1..469
                     /gene="TERF1"
                     /gene_synonym="hTRF1-AS; PIN2; t-TRF1; TRBF1; TRF; TRF1"
                     /coded_by="NM_001413364.1:24..1433"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:7013"
                     /db_xref="HGNC:HGNC:11728"
                     /db_xref="MIM:600951"
ORIGIN      
        1 maedvssaap sprgcadgrd adpteeqmae terndeeqfe cqellecqvq vgapeeeeee
       61 eedaglvaea eavaagwmld flclslcraf rdgrsedfrr trnsaeaiih glssltacql
      121 rtiyicqflt riaagktlda qfenderitp lesalmiwgs iekehdklhe eiqnlikiqa
      181 iavcmengnf keaeevferi fgdpnshmpf kskllmiisq kdtfhsffqh fsynhmmeki
      241 ksyvnyvlse ksstflmkaa akvveskrtr titsqdkpsg ndvemetean ldtrksvsdk
      301 qsavtesseg tvsllrshkn lflsklqhgt qqqdlnkker rvgtpqityi cltkltmnkk
      361 egvrkglcfl vllkhyrtkk kkesrrates ripvsksqpv tpekhrarkr qawlweedkn
      421 lrsgvrkyge gnwskillhy kfnnrtsvml kdrwrtmkkl klissdsed
//
LOCUS       NP_001394745            1197 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 13 precursor
            [Homo sapiens].
ACCESSION   NP_001394745
VERSION     NP_001394745.1
DBSOURCE    REFSEQ: accession NM_001407816.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1197)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1197)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1197)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1197)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1197)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1197)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1197)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1197)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1197)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1197)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.5884.1,
                                           SRR18074967.2588914.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1197
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1197
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 13 precursor"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=134637
     Region          261..290
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          296..323
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          432..704
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          831..1197
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1197
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407816.1:26..3619"
                     /note="isoform 13 precursor is encoded by transcript
                     variant 13"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 msalcwgrga aglkralrpc grpglpgkeg taggvcgprr sssaspqeqd qdrrkdwghv
       61 ellevlqarv rqlqaesvse vvvnrvdvar lpecgsgdgs lqpprkvqmg akdatpvpcg
      121 rwakilekdk rtqqmrmqrl kaklqmpfqs gefkaltrrl qveprllskq magcledctr
      181 qapespweeq larllqeapg klsldveqap sgqhsqaqls gqqqrllaff kcclltdqlp
      241 lahhllvvhh gqrqkrkllt ldmynavmlg warqgafkel vyvlfmvkda gltpdllsya
      301 aalqcmgrqd qdagtiercl eqmsqeglkl qalftavlls eedratvlka vhkvkptfsl
      361 ppqlpppvnt skllrdvyak dgrvsypklh lplktlqclf ekqlhmelas rvcvvsvekp
      421 tlpskevkha rktlktlrdq wekalcralr etknrlerev yegrfslypf lcllderevv
      481 rmllqvlqal paqgesfttl arelsartfs rhvvqrqrvs gqvqalqnhy rkylcllasd
      541 aevpepclpr qyweelgape alreqpwplp vqmelgklla emlvqatqmp csldkphrss
      601 rlvpvlyhvy sfrnvqqigi lkphpayvql lekaaeptlt feavdvpmlc pplpwtsphs
      661 gafllsptkl mrtvegatqh qelletcppt alhgaldalt qlgncawrvn grvldlvlql
      721 fqakgcpqlg vpappseapq ppeahlphsa aparkaelrr elahcqkvar emhslraeal
      781 yrlslaqhlr drvfwlphnm dfrgrtypcp phfnhlgsdv arallefaqg rplgphgldw
      841 lkihlvnltg lkkreplrkr lafaeevmdd ildsadqplt grkwwmgaee pwqtlaccme
      901 vanavrasdp aayvshlpvh qdgscnglqh yaalgrdsvg aasvnlepsd vpqdvysgva
      961 aqvevfrrqd aqrgmrvaqv legfitrkvv kqtvmtvvyg vtryggrlqi ekrlrelsdf
     1021 pqefvweash ylvrqvfksl qemfsgtrai qhwltesarl ishmgsvvew vtplgvpviq
     1081 pyrldskvkq igggiqsity thngdisrkg ltfvsvhdcy wthaadvsvm nqvcreqfvr
     1141 lhsepilqdl srflvkrfcs epqkileasq lketlqavpk pgafdleqvk rstyffs
//
LOCUS       NP_001407088             838 aa            linear   PRI 21-NOV-2025
DEFINITION  protein enabled homolog isoform f [Homo sapiens].
ACCESSION   NP_001407088 XP_047280870 XP_054193577
VERSION     NP_001407088.1
DBSOURCE    REFSEQ: accession NM_001420159.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 838)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 838)
  AUTHORS   Yin,X., Wang,J., Shen,Z., Jia,Q., Bian,Y., Yang,Z., Liu,Y., Li,Y.
            and Zhang,H.
  TITLE     ENAH transcriptionally activated by YY1 promotes growth and
            invasion of laryngocarcinoma cells through PI3K/AKT signaling
  JOURNAL   Eur J Pharmacol 983, 176991 (2024)
   PUBMED   39265883
  REMARK    GeneRIF: ENAH transcriptionally activated by YY1 promotes growth
            and invasion of laryngocarcinoma cells through PI3K/AKT signaling.
REFERENCE   3  (residues 1 to 838)
  AUTHORS   Cui,H., Liang,X., Zhu,Y., Elayah,S.A., Qi,H., Xie,L., Guo,Z.,
            Siya,F., Ming,Y., Yuxin,G., Tu,J. and Na,S.
  TITLE     Mena as a key enhancer factor of EMT to promote metastasis of human
            tongue squamous cell carcinoma
  JOURNAL   Oral Dis 30 (4), 2084-2096 (2024)
   PUBMED   37203597
  REMARK    GeneRIF: Mena as a key enhancer factor of EMT to promote metastasis
            of human tongue squamous cell carcinoma.
REFERENCE   4  (residues 1 to 838)
  AUTHORS   He,L., She,C., Jiang,S., Qi,Z., Deng,Z., Ji,L., Cui,Y. and Wu,J.
  TITLE     Mammalian enabled protein enhances tamoxifen sensitivity of the
            hormone receptor-positive breast cancer patients by suppressing the
            AKT signaling pathway
  JOURNAL   Biol Direct 19 (1), 21 (2024)
   PUBMED   38459605
  REMARK    GeneRIF: Mammalian enabled protein enhances tamoxifen sensitivity
            of the hormone receptor-positive breast cancer patients by
            suppressing the AKT signaling pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 838)
  AUTHORS   Liu,R., Miao,K., Gao,L. and He,L.
  TITLE     TRIM67 interacts with ENAH to regulate the apoptosis and autophagy
            of lung cancer cells
  JOURNAL   Gen Physiol Biophys 43 (2), 163-173 (2024)
   PUBMED   38477606
  REMARK    GeneRIF: TRIM67 interacts with ENAH to regulate the apoptosis and
            autophagy of lung cancer cells.
REFERENCE   6  (residues 1 to 838)
  AUTHORS   Urbanelli,L., Massini,C., Emiliani,C., Orlacchio,A., Bernardi,G.
            and Orlacchio,A.
  TITLE     Characterization of human Enah gene
  JOURNAL   Biochim Biophys Acta 1759 (1-2), 99-107 (2006)
   PUBMED   16494957
REFERENCE   7  (residues 1 to 838)
  AUTHORS   Mammoto,A., Sasaki,T., Asakura,T., Hotta,I., Imamura,H.,
            Takahashi,K., Matsuura,Y., Shirao,T. and Takai,Y.
  TITLE     Interactions of drebrin and gephyrin with profilin
  JOURNAL   Biochem Biophys Res Commun 243 (1), 86-89 (1998)
   PUBMED   9473484
REFERENCE   8  (residues 1 to 838)
  AUTHORS   Ermekova,K.S., Zambrano,N., Linn,H., Minopoli,G., Gertler,F.,
            Russo,T. and Sudol,M.
  TITLE     The WW domain of neural protein FE65 interacts with proline-rich
            motifs in Mena, the mammalian homolog of Drosophila enabled
  JOURNAL   J Biol Chem 272 (52), 32869-32877 (1997)
   PUBMED   9407065
REFERENCE   9  (residues 1 to 838)
  AUTHORS   Niebuhr,K., Ebel,F., Frank,R., Reinhard,M., Domann,E., Carl,U.D.,
            Walter,U., Gertler,F.B., Wehland,J. and Chakraborty,T.
  TITLE     A novel proline-rich motif present in ActA of Listeria
            monocytogenes and cytoskeletal proteins is the ligand for the EVH1
            domain, a protein module present in the Ena/VASP family
  JOURNAL   EMBO J 16 (17), 5433-5444 (1997)
   PUBMED   9312002
REFERENCE   10 (residues 1 to 838)
  AUTHORS   Sazuka,T., Tomooka,Y., Kathju,S., Ikawa,Y., Noda,M. and Kumar,S.
  TITLE     Identification of a developmentally regulated gene in the mouse
            central nervous system which encodes a novel proline rich protein
  JOURNAL   Biochim Biophys Acta 1132 (3), 240-248 (1992)
   PUBMED   1420303
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL591380.21, AL356216.13 and
            AC092811.2.
            
            On or before Apr 26, 2023 this sequence version replaced
            XP_047280870.1, XP_054193577.1.
            
            Summary: This gene encodes a member of the enabled/
            vasodilator-stimulated phosphoprotein. Members of this gene family
            are involved in actin-based motility. This protein is involved in
            regulating the assembly of actin filaments and modulates cell
            adhesion and motility. Alternate splice variants of this gene have
            been correlated with tumor invasiveness in certain tissues and
            these variants may serve as prognostic markers. A pseudogene of
            this gene is found on chromosome 3. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3766012.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..838
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.12"
     Protein         1..838
                     /product="protein enabled homolog isoform f"
                     /note="protein enabled homolog; Mena delta 11a"
                     /calculated_mol_wt=91401
     Region          5..112
                     /region_name="EVH1_Ena_VASP-like"
                     /note="Enabled/VASP family EVH1 domain; cd01207"
                     /db_xref="CDD:269918"
     Site            order(16,23,69,71,77,79,81)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269918"
     Region          <348..583
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          632..658
                     /region_name="WH2_hVASP-like"
                     /note="Wiskott-Aldrich syndrome protein (WASP)-homology
                     domain 2 (WH2) of human Vasodilator-stimulated
                     phosphoprotein and related proteins; cd22185"
                     /db_xref="CDD:409225"
     Site            order(639..640,642..643,646,648..652)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409225"
     Region          648..651
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409225"
     Region          800..834
                     /region_name="VASP_tetra"
                     /note="VASP tetramerization domain; pfam08776"
                     /db_xref="CDD:462599"
     CDS             1..838
                     /gene="ENAH"
                     /gene_synonym="ENA; MENA; NDPP1"
                     /coded_by="NM_001420159.1:434..2950"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="GeneID:55740"
                     /db_xref="HGNC:HGNC:18271"
                     /db_xref="MIM:609061"
ORIGIN      
        1 mseqsicqar aavmvyddan kkwvpaggst gfsrvhiyhh tgnntfrvvg rkiqdhqvvi
       61 ncaipkglky nqatqtfhqw rdarqvygln fgskedanvf asammhalev lnsqetaqsk
      121 vtatqdstnl rcifcgptlp rqnsqlpaqv qngpsqeele iqrrqlqeqq rqkelererl
      181 erermererl ererlererl ererleqeql ererqererq erlerqerle rqerlerqer
      241 ldrerqerqe rerlerlere rqererqeql ereqlewere rrissaapss dsslynaplp
      301 eysscqppsa pppsyakvis apvsdatpdy avvtalppts tpptpplrhs atrfatslgs
      361 afhpvlphya tvprplnkns rpsspvntps sqppatkpca wstsnfsplp psppimissp
      421 pgkatgprpv lpvcvsspvp qmppsptapn glvdsvtypv sppptsgpaa pppppplpsl
      481 aslshcgsqa spppstpias tpsskpsvlp spsaaapasv etplnsvlgd ssasepglqa
      541 asqpaetpsq qgivlgplap ppppplppgp aqasvalppp pgpppppplp stgppppppp
      601 pplpnqvppp pppppapplp asgfflasms ednrpltgla aaiagaklrk vsrmedtsfp
      661 sggnaigvns assktdtgrg ngplplggsg lmeemsalla rrrriaekgs tieteqkedk
      721 gedsepvtsk asststpept rkpwertntm ngskspvisr rdsprknqiv fdnrsydslh
      781 rpkstplsqp sangvqtegl dydrlkqdil demrkeltkl keelidairq elsksnta
//
LOCUS       NP_001425415            2333 aa            linear   PRI 21-NOV-2025
DEFINITION  AT-rich interactive domain-containing protein 1B isoform 8 [Homo
            sapiens].
ACCESSION   NP_001425415 XP_047275099 XP_054212022
VERSION     NP_001425415.1
DBSOURCE    REFSEQ: accession NM_001438486.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2333)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2333)
  AUTHORS   Bosch,E., Guse,E., Kirchner,P., Winterpacht,A., Walther,M.,
            Alders,M., Kerkhof,J., Ekici,A.B., Sticht,H., Sadikovic,B., Reis,A.
            and Vasileiou,G.
  TITLE     The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation
  JOURNAL   Hum Genet 143 (8), 965-978 (2024)
   PUBMED   39028335
  REMARK    GeneRIF: The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation.
REFERENCE   3  (residues 1 to 2333)
  AUTHORS   Huang,X., Li,H., Yang,S., Ma,M., Lian,Y., Wu,X., Qi,X., Wang,X.,
            Rong,W. and Sheng,X.
  TITLE     De novo variation in ARID1B gene causes Coffin-Siris syndrome 1 in
            a Chinese family with excessive early-onset high myopia
  JOURNAL   BMC Med Genomics 17 (1), 142 (2024)
   PUBMED   38790056
  REMARK    GeneRIF: De novo variation in ARID1B gene causes Coffin-Siris
            syndrome 1 in a Chinese family with excessive early-onset high
            myopia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2333)
  AUTHORS   Hurlstone,A.F., Olave,I.A., Barker,N., van Noort,M. and Clevers,H.
  TITLE     Cloning and characterization of hELD/OSA1, a novel BRG1 interacting
            protein
  JOURNAL   Biochem J 364 (Pt 1), 255-264 (2002)
   PUBMED   11988099
  REMARK    GeneRIF: Cloning and characterization of hELD/OSA1, a novel BRG1
            interacting protein.
REFERENCE   5  (residues 1 to 2333)
  AUTHORS   Phelan,M.L., Sif,S., Narlikar,G.J. and Kingston,R.E.
  TITLE     Reconstitution of a core chromatin remodeling complex from SWI/SNF
            subunits
  JOURNAL   Mol Cell 3 (2), 247-253 (1999)
   PUBMED   10078207
REFERENCE   6  (residues 1 to 2333)
  AUTHORS   Imbert,G., Saudou,F., Yvert,G., Devys,D., Trottier,Y.,
            Garnier,J.M., Weber,C., Mandel,J.L., Cancel,G., Abbas,N., Durr,A.,
            Didierjean,O., Stevanin,G., Agid,Y. and Brice,A.
  TITLE     Cloning of the gene for spinocerebellar ataxia 2 reveals a locus
            with high sensitivity to expanded CAG/glutamine repeats
  JOURNAL   Nat Genet 14 (3), 285-291 (1996)
   PUBMED   8896557
REFERENCE   7  (residues 1 to 2333)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
REFERENCE   8  (residues 1 to 2333)
  AUTHORS   Vergano,S.A., van der Sluijs,P.J. and Santen,G.
  TITLE     ARID1B-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31132234
REFERENCE   9  (residues 1 to 2333)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
REFERENCE   10 (residues 1 to 2333)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355297.20, AL162578.13,
            AL049820.23 and AL591545.6.
            
            On or before Apr 21, 2025 this sequence version replaced
            XP_047275099.1, XP_054212022.1.
            
            Summary: This locus encodes an AT-rich DNA interacting
            domain-containing protein. The encoded protein is a component of
            the SWI/SNF chromatin remodeling complex and may play a role in
            cell-cycle activation. The protein encoded by this locus is similar
            to AT-rich interactive domain-containing protein 1A. These two
            proteins function as alternative, mutually exclusive ARID-subunits
            of the SWI/SNF complex. The associated complexes play opposing
            roles. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4055391.1,
                                           SRR14038194.2735511.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..2333
                     /product="AT-rich interactive domain-containing protein 1B
                     isoform 8"
                     /note="BRG1-binding protein ELD/OSA1; ELD (eyelid)/OSA
                     protein; BRG1-associated factor 250b; ARID
                     domain-containing protein 1B; AT rich interactive domain
                     1B (SWI1-like)"
                     /calculated_mol_wt=245244
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          155..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          321..414
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          487..546
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            487
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4N7; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          502..506
                     /region_name="LXXLL"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            608
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4N7; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            640
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          774..>974
                     /region_name="Enamelin"
                     /note="pfam15362"
                     /db_xref="CDD:464672"
     Region          1099..1143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          1151..1243
                     /region_name="ARID_ARID1B"
                     /note="ARID/BRIGHT DNA binding domain of AT-rich
                     interactive domain-containing protein 1B (ARID1B) and
                     similar proteins; cd16877"
                     /db_xref="CDD:350641"
     Site            order(1173..1179,1204,1206..1207,1210,1220,1222..1224,
                     1226)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350641"
     Region          1244..1348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          1264..>1644
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          1360..1457
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          1455..1474
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:O14497"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          1489..1661
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            1639
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            1652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            1656
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          1796..1866
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            1812
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Site            1874
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          1918..1955
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          1968..1987
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     Region          2024..2279
                     /region_name="BAF250_C"
                     /note="SWI/SNF-like complex subunit BAF250/Osa; pfam12031"
                     /db_xref="CDD:463439"
     Region          2133..2137
                     /region_name="LXXLL"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFD5.3)"
     CDS             1..2333
                     /gene="ARID1B"
                     /gene_synonym="6A3-5; BAF250B; BRIGHT; CSS1; DAN15;
                     ELD/OSA1; MRD12; OSA2; P250R; SMARCF2"
                     /coded_by="NM_001438486.1:304..7305"
                     /note="isoform 8 is encoded by transcript variant 9"
                     /db_xref="GeneID:57492"
                     /db_xref="HGNC:HGNC:18040"
                     /db_xref="MIM:614556"
ORIGIN      
        1 maaraaaaaa aaaararara gsgerrappg prpapgardl eagargaaaa aaapgpmlgg
       61 ggdgggglns vhhhpllprh elnmahnaga aaaagthsak sggseaalke ggsaaalsss
      121 ssssaaaaaa ssssssgpgs ametgllpnh klktvgeapa apphqqhhhh hhahhhhhha
      181 hhlhhhhalq qqlnqfqqqq qqqqqqqqqq qqqqhpisnn nslggaggga pqpgpdmeqp
      241 qhggakdsaa ggqadppgpp llskpgdedd appkmgepag gryehpglga lgtqqppvav
      301 pgggggpaav pefnnyygsa apasggpggr agpcfdqhgg qqspgmgmmh sasaaaagap
      361 gsmdplqnsh egypnsqcnh ypgysrpgag gggggggggg ggsggggggg gagaggagag
      421 avaaaaaaaa aaaggggggg yggssagygv lssprqqggg mmmgpgggga aslskaaags
      481 aaggfqrfag qnqhpsgatp tlnqlltsps pmmrsyggsy peysspsapp pppsqpqsqa
      541 aaagaaaggq qaaagmglgk dmgaqyaaas pawaaaqqrs hpamspgtpg ptmgrsqgsp
      601 mdpmvmkrpq lygmgsnphs qpqqsspypg gsygppgpqr ypigiqgrtp gamagmqypq
      661 qqmppqygqq gvsgycqqgq qpyysqqpqp phlppqaqyl psqsqqryqp qqdmsqegyg
      721 trsqpplapg kpnhedlnli qqerpsslpv evlasedaaf glkdlsgsid dlptgteatl
      781 ssavsasgst ssqgdqsnpa qspfsphasp hlssipggps pspvgspvgs nqsrsgpisp
      841 asipgsqmpp qppgsqsess shpalsqspm pqergfmagt qrnpqmaqyg pqqtgpsmsp
      901 hpspggqmha gissfqqsns sgtygpqmsq ygpqgnysrp paysgvpsas ysgpgpgmgi
      961 sannqmhgqg psqpcgavpl grmpsagmqn rpfpgnmssm tpsspgmsqq ggpgmgppmp
     1021 tvnrkaqeaa aavmqaaans aqsrqgsfpg mnqsglmass spysqpmnns sslmntqapp
     1081 ysmapamvns saasvgladm mspgesklpl plkadgkeeg tpqpeskskk sssstttgek
     1141 itkvyelgne perklwvdry ltfmeergsp vsslpavgkk pldlfrlyvc vkeigglaqv
     1201 nknkkwrela tnlnvgtsss aasslkkqyi qylfafecki ergeepppev fstgdtkkqp
     1261 klqppspans gslqgpqtpq stgsnsmaev pgdlkpptpa stphgqmtpm qggrsstisv
     1321 hdpfsdvsds sfpkrnsmtp napyqqgmsm pdvmgrmpye pnkdpfggmr kvpgssepfm
     1381 tqgqmpnssm qdmynqspsg amsnlgmgqr qqfpygasyd rrhepygqqy pgqgppsgqp
     1441 pygghqpgly pqqpnykrhm dgmygppakr hegdmynmqy ssqqqemynq yggsysgpdr
     1501 rpiqgqypyp ysrermqgpg qiqthgippq mmggplqsss segpqqnmwa arndmpypyq
     1561 nrqgpggptq appypgmnrt ddmmvpdqri nhesqwpshv sqrqpymsss asmqpitrpp
     1621 qpsyqtppsl pnhisrapsp asfqrslenr mspskspflp smkmqkvmpt vptsqvtgpp
     1681 pqpppirrei tfppgsveas qpvlkqrrki tskdivtpea wrvmmslksg llaestwald
     1741 tinillydds tvatfnlsql sgflellvey frkclidifg ilmeyevgdp sqkaldhnaa
     1801 rkddsqslad dsgkeeedae cidddeedee deeedsekte sdekssialt apdaaadpke
     1861 kpkqaskfdk lpikivkknn lfvvdrsdkl grvqefnsgl lhwqlgggdt tehiqthfes
     1921 kmeipprrrp ppplssagrk keqegkgdse eqqeksiiat iddvlsarpg alpedanpgp
     1981 qtesskfpfg iqqakshrni klledeprsr detplctiah wqdslakrci cvsnivrsls
     2041 fvpgndaems khpglvlilg klillhhehp erkrapqtye keededkgva cskdewwwdc
     2101 levlrdntlv tlanisgqld lsaytesicl pildgllhwm vcpsaeaqdp fptvgpnsvl
     2161 spqrlvletl cklsiqdnnv dlilatppfs rqekfyatlv ryvgdrknpv cremsmalls
     2221 nlaqgdalaa raiavqkgsi gnlisfledg vtmaqyqqsq hnlmhmqppp leppsvdmmc
     2281 raakallama rvdenrsefl lhegrlldis isavlnslva svicdvlfqi gql
//
LOCUS       NP_001427235             362 aa            linear   PRI 21-NOV-2025
DEFINITION  G1/S-specific cyclin-E1 isoform 7 [Homo sapiens].
ACCESSION   NP_001427235 XP_047295562 XP_054178473
VERSION     NP_001427235.1
DBSOURCE    REFSEQ: accession NM_001440306.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Lee,S.J., Jeon,S.H., Cho,S., Kim,C.M., Yoo,J.K., Oh,S.H., Kim,J.H.,
            Yang,Y.D. and Kim,J.K.
  TITLE     hsa-miR-CHA2, a novel microRNA, exhibits anticancer effects by
            suppressing cyclin E1 in human non-small cell lung cancer cells
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (6), 167250 (2024)
   PUBMED   38763409
  REMARK    GeneRIF: hsa-miR-CHA2, a novel microRNA, exhibits anticancer
            effects by suppressing cyclin E1 in human non-small cell lung
            cancer cells.
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Rustgi,N., Wu,S., Samec,T., Walker,P., Xiu,J., Lou,E., Goel,S.,
            Saeed,A. and Moy,R.H.
  TITLE     Molecular Landscape and Clinical Implication of CCNE1-amplified
            Esophagogastric Cancer
  JOURNAL   Cancer Res Commun 4 (6), 1399-1409 (2024)
   PUBMED   38717153
  REMARK    GeneRIF: Molecular Landscape and Clinical Implication of
            CCNE1-amplified Esophagogastric Cancer.
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Audrey,A., Kok,Y.P., Yu,S., de Haan,L., van de Kooij,B., van den
            Tempel,N., Chen,M., de Boer,H.R., van der Vegt,B. and van
            Vugt,M.A.T.M.
  TITLE     RAD52-dependent mitotic DNA synthesis is required for genome
            stability in Cyclin E1-overexpressing cells
  JOURNAL   Cell Rep 43 (4), 114116 (2024)
   PUBMED   38625790
  REMARK    GeneRIF: RAD52-dependent mitotic DNA synthesis is required for
            genome stability in Cyclin E1-overexpressing cells.
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Mumberg,D., Wick,M., Burger,C., Haas,K., Funk,M. and Muller,R.
  TITLE     Cyclin ET, a new splice variant of human cyclin E with a unique
            expression pattern during cell cycle progression and
            differentiation
  JOURNAL   Nucleic Acids Res 25 (11), 2098-2105 (1997)
   PUBMED   9153308
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Sewing,A., Ronicke,V., Burger,C., Funk,M. and Muller,R.
  TITLE     Alternative splicing of human cyclin E
  JOURNAL   J Cell Sci 107 (Pt 2), 581-588 (1994)
   PUBMED   8207080
REFERENCE   7  (residues 1 to 362)
  AUTHORS   Koff,A., Giordano,A., Desai,D., Yamashita,K., Harper,J.W.,
            Elledge,S., Nishimoto,T., Morgan,D.O., Franza,B.R. and Roberts,J.M.
  TITLE     Formation and activation of a cyclin E-cdk2 complex during the G1
            phase of the human cell cycle
  JOURNAL   Science 257 (5077), 1689-1694 (1992)
   PUBMED   1388288
REFERENCE   8  (residues 1 to 362)
  AUTHORS   Hinds,P.W., Mittnacht,S., Dulic,V., Arnold,A., Reed,S.I. and
            Weinberg,R.A.
  TITLE     Regulation of retinoblastoma protein functions by ectopic
            expression of human cyclins
  JOURNAL   Cell 70 (6), 993-1006 (1992)
   PUBMED   1388095
REFERENCE   9  (residues 1 to 362)
  AUTHORS   Koff,A., Cross,F., Fisher,A., Schumacher,J., Leguellec,K.,
            Philippe,M. and Roberts,J.M.
  TITLE     Human cyclin E, a new cyclin that interacts with two members of the
            CDC2 gene family
  JOURNAL   Cell 66 (6), 1217-1228 (1991)
   PUBMED   1833068
REFERENCE   10 (residues 1 to 362)
  AUTHORS   Lew,D.J., Dulic,V. and Reed,S.I.
  TITLE     Isolation of three novel human cyclins by rescue of G1 cyclin (Cln)
            function in yeast
  JOURNAL   Cell 66 (6), 1197-1206 (1991)
   PUBMED   1833066
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008798.10.
            
            On or before May 19, 2025 this sequence version replaced
            XP_047295562.1, XP_054178473.1.
            
            Summary: The protein encoded by this gene belongs to the highly
            conserved cyclin family, whose members are characterized by a
            dramatic periodicity in protein abundance through the cell cycle.
            Cyclins function as regulators of CDK kinases. Different cyclins
            exhibit distinct expression and degradation patterns which
            contribute to the temporal coordination of each mitotic event. This
            cyclin forms a complex with and functions as a regulatory subunit
            of CDK2, whose activity is required for cell cycle G1/S transition.
            This protein accumulates at the G1-S phase boundary and is degraded
            as cells progress through S phase. Overexpression of this gene has
            been observed in many tumors, which results in chromosome
            instability, and thus may contribute to tumorigenesis. This protein
            was found to associate with, and be involved in, the
            phosphorylation of NPAT protein (nuclear protein mapped to the ATM
            locus), which participates in cell-cycle regulated histone gene
            expression and plays a critical role in promoting cell-cycle
            progression in the absence of pRB. [provided by RefSeq, Apr 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.977228.1,
                                           SRR14038191.3746282.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..362
                     /product="G1/S-specific cyclin-E1 isoform 7"
                     /note="G1/S-specific cyclin-E1"
                     /calculated_mol_wt=41219
     Region          100..235
                     /region_name="CYCLIN_CCNE1_rpt1"
                     /note="first cyclin box found in G1/S-specific cyclin-E1
                     (CCNE1); cd20579"
                     /db_xref="CDD:410282"
     Site            order(106..107,109,112..113,116..117,120,124,159,194,
                     198..202,206..207,224,227..228,231..232,235)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410282"
     Region          <230..308
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cl40454"
                     /db_xref="CDD:477360"
     CDS             1..362
                     /gene="CCNE1"
                     /gene_synonym="CCNE; pCCNE1"
                     /coded_by="NM_001440306.1:187..1275"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:898"
                     /db_xref="HGNC:HGNC:1589"
                     /db_xref="MIM:123837"
ORIGIN      
        1 mprerrerda kerdtmkedg gaefsarsrk rkanvtvdpd eemakidrta rdqcgsqpwd
       61 nnavcadpcs liptpdkedd drvypnstck priiapsrgs plpvlswanr eevwkimlnk
      121 ektylrdqhf leqhpllqpk mrailldwlm evcevyklhr etfylaqdff drymatqenv
      181 vktllqligi sslfiaakle eiyppklhqf ayvtdgacsg deiltmelmi mklldlcvld
      241 vdclefpygi laasalyhfs sselmqkvsg yqwcdiencv kwmvpfamvi retgssklkh
      301 frgvadedah niqthrdsld lldkarakka mlseqnrasp lpsglltppq sgkkqssgpe
      361 ma
//
LOCUS       NP_001427923             803 aa            linear   PRI 21-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 6 isoform 4 [Homo sapiens].
ACCESSION   NP_001427923 XP_011529714 XP_054184144
VERSION     NP_001427923.1
DBSOURCE    REFSEQ: accession NM_001440994.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 803)
  AUTHORS   Zheng,T., Zhou,H., Zheng,Z., Guo,Y., Liu,J., Zhang,J. and Li,S.
  TITLE     The pathological significance and potential mechanism of ARHGEF6 in
            lung adenocarcinoma
  JOURNAL   Comput Biol Med 158, 106894 (2023)
   PUBMED   37058762
  REMARK    GeneRIF: The pathological significance and potential mechanism of
            ARHGEF6 in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 803)
  AUTHORS   Li,K., Wang,H., Yang,C., Li,C., Xue,B. and Zhou,J.
  TITLE     Clinical implication and potential function of ARHGEF6 in acute
            myeloid leukemia: An in vitro study
  JOURNAL   PLoS One 18 (4), e0283934 (2023)
   PUBMED   37027440
  REMARK    GeneRIF: Clinical implication and potential function of ARHGEF6 in
            acute myeloid leukemia: An in vitro study.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 803)
  AUTHORS   Klambt,V., Buerger,F., Wang,C., Naert,T., Richter,K., Nauth,T.,
            Weiss,A.C., Sieckmann,T., Lai,E., Connaughton,D.M., Seltzsam,S.,
            Mann,N., Majmundar,A.J., Wu,C.W., Onuchic-Whitford,A.C., Shril,S.,
            Schneider,S., Schierbaum,L., Dai,R., Bekheirnia,M.R., Joosten,M.,
            Shlomovitz,O., Vivante,A., Banne,E., Mane,S., Lifton,R.P.,
            Kirschner,K.M., Kispert,A., Rosenberger,G., Fischer,K.D.,
            Lienkamp,S.S., Zegers,M.M.P. and Hildebrandt,F.
  TITLE     Genetic Variants in ARHGEF6 Cause Congenital Anomalies of the
            Kidneys and Urinary Tract in Humans, Mice, and Frogs
  JOURNAL   J Am Soc Nephrol 34 (2), 273-290 (2023)
   PUBMED   36414417
  REMARK    GeneRIF: Genetic Variants in ARHGEF6 Cause Congenital Anomalies of
            the Kidneys and Urinary Tract in Humans, Mice, and Frogs.
REFERENCE   5  (residues 1 to 803)
  AUTHORS   Wang,N., Li,Y., Zhou,X., Wang,X. and Yang,G.
  TITLE     Comprehensive analysis identifies ARHGEF6 as a potential prognostic
            and immunological biomarker in lung adenocarcinoma
  JOURNAL   Comput Biol Med 153, 106448 (2023)
   PUBMED   36586227
  REMARK    GeneRIF: Comprehensive analysis identifies ARHGEF6 as a potential
            prognostic and immunological biomarker in lung adenocarcinoma.
REFERENCE   6  (residues 1 to 803)
  AUTHORS   Yoshii,S., Tanaka,M., Otsuki,Y., Wang,D.Y., Guo,R.J., Zhu,Y.,
            Takeda,R., Hanai,H., Kaneko,E. and Sugimura,H.
  TITLE     alphaPIX nucleotide exchange factor is activated by interaction
            with phosphatidylinositol 3-kinase
  JOURNAL   Oncogene 18 (41), 5680-5690 (1999)
   PUBMED   10523848
REFERENCE   7  (residues 1 to 803)
  AUTHORS   Yntema,H.G., Hamel,B.C., Smits,A.P., van Roosmalen,T., van den
            Helm,B., Kremer,H., Ropers,H.H., Smeets,D.F. and van Bokhoven,H.
  TITLE     Localisation of a gene for non-specific X linked mental retardation
            (MRX46) to Xq25-q26
  JOURNAL   J Med Genet 35 (10), 801-805 (1998)
   PUBMED   9783701
REFERENCE   8  (residues 1 to 803)
  AUTHORS   Ebinu,J.O., Bottorff,D.A., Chan,E.Y., Stang,S.L., Dunn,R.J. and
            Stone,J.C.
  TITLE     RasGRP, a Ras guanyl nucleotide- releasing protein with calcium-
            and diacylglycerol-binding motifs
  JOURNAL   Science 280 (5366), 1082-1086 (1998)
   PUBMED   9582122
REFERENCE   9  (residues 1 to 803)
  AUTHORS   Manser,E., Loo,T.H., Koh,C.G., Zhao,Z.S., Chen,X.Q., Tan,L.,
            Tan,I., Leung,T. and Lim,L.
  TITLE     PAK kinases are directly coupled to the PIX family of nucleotide
            exchange factors
  JOURNAL   Mol Cell 1 (2), 183-192 (1998)
   PUBMED   9659915
REFERENCE   10 (residues 1 to 803)
  AUTHORS   Nomura,N., Nagase,T., Miyajima,N., Sazuka,T., Tanaka,A., Sato,S.,
            Seki,N., Kawarabayasi,Y., Ishikawa,K. and Tabata,S.
  TITLE     Prediction of the coding sequences of unidentified human genes. II.
            The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
            analysis of cDNA clones from human cell line KG-1 (supplement)
  JOURNAL   DNA Res 1 (5), 251-262 (1994)
   PUBMED   7584048
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL683813.10 and AL135783.6.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_011529714.1, XP_054184144.1.
            
            Summary: Rho GTPases play a fundamental role in numerous cellular
            processes that are initiated by extracellular stimuli that work
            through G protein coupled receptors. The encoded protein belongs to
            a family of cytoplasmic proteins that activate the Ras-like family
            of Rho proteins by exchanging bound GDP for GTP. It may form a
            complex with G proteins and stimulate Rho-dependent signals. This
            protein is activated by PI3-kinase. Mutations in this gene can
            cause X-chromosomal non-specific cognitive disability. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3018923.1,
                                           SRR14038194.101602.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.3"
     Protein         1..803
                     /product="rho guanine nucleotide exchange factor 6 isoform
                     4"
                     /note="Rac/Cdc42 guanine exchange factor (GEF) 6; rho
                     guanine nucleotide exchange factor 6; PAK-interacting
                     exchange factor, alpha; Rac/Cdc42 guanine nucleotide
                     exchange factor (GEF) 6"
                     /calculated_mol_wt=90037
     Region          1..117
                     /region_name="CH_alphaPIX"
                     /note="calponin homology (CH) domain found in alpha-Pak
                     Interactive eXchange factor; cd21265"
                     /db_xref="CDD:409114"
     Site            order(3,7,65,67..68,71..72,74,81..89,95,97..98,100..101,
                     104..105,108)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409114"
     Region          115..160
                     /region_name="RhoGEF67_u1"
                     /note="Unstructured region one on RhoGEF 6 and 7;
                     pfam16615"
                     /db_xref="CDD:465201"
     Region          162..219
                     /region_name="SH3_alphaPIX"
                     /note="Src Homology 3 domain of alpha-Pak Interactive
                     eXchange factor; cd12060"
                     /db_xref="CDD:212993"
     Site            order(169,171,174,177..178,193,195..197,208,210,212..213)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212993"
     Region          269..446
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(275,279,373,397..398,401..402,404..405,408..409,
                     412..413,416,442,446)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          477..574
                     /region_name="PH_Cool_Pix"
                     /note="Cloned out of library/PAK-interactive exchange
                     factor pleckstrin homology (PH) domain; cd01225"
                     /db_xref="CDD:269932"
     Region          603..701
                     /region_name="RhoGEF67_u2"
                     /note="Unstructured region two on RhoGEF 6 and 7;
                     pfam16614"
                     /db_xref="CDD:465200"
     Region          712..796
                     /region_name="betaPIX_CC"
                     /note="betaPIX coiled coil; pfam16523"
                     /db_xref="CDD:465158"
     CDS             1..803
                     /gene="ARHGEF6"
                     /gene_synonym="alpha-PIX; alphaPIX; Cool-2; COOL2; MRX46;
                     PIXA"
                     /coded_by="NM_001440994.1:51..2462"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:9459"
                     /db_xref="HGNC:HGNC:685"
                     /db_xref="MIM:300267"
ORIGIN      
        1 mnpeeqivtw lislgvlesp kkticdpeef lksslkngvv lcklinrlmp gsvekfcldp
       61 qteadcinni ndflkgcatl qveifdpddl ysgvnfskvl stllavnkat edqlserpcg
      121 rssslsaant sqtnpqgavs stvsglqrqs ktvemtengs hqlivkarfn fkqtnedels
      181 vckgdiiyvt rveeggwweg tlngrtgwfp snyvreikss dgvslllpgl ecngaisahh
      241 nlclpgskrp lspkavkgfe tapltknyyt vvlqnildte keyakelqsl lvtylrplqs
      301 nnnlstvevt sllgnfeevc tfqqtlcqal eecskfpenq hkvggcllsl mphfksmyla
      361 ycanhpsavn vltqhsdele qfmenqgass pgililttnl skpfmrleky vtllqelerh
      421 medthpdhqd ilkaivafkt lmgqcqdlrk rkqlelqils epiqaweged iknlgnvifm
      481 sqvmvqygac eekeerylml fsnvlimlsa sprmsgfiyq gkipiagtvv trldeiegnd
      541 ctfeitgntv erivvhcnnn qdfqewleql nrlirgpasc sslsktssss csahssfsst
      601 gqprgplepp qiikpwslsc lrpapplrps aalgykerms yilkessksp ktmkkflhkr
      661 kterkpseee yvirkstaal eedaqilkvi eayctsanfq qghgsstrkd sipqvllpee
      721 ekliieetrs ngqtimeeks lvdtvyalkd evrelkqenk rmkqcleeel ksrrdleklv
      781 rrllkqtdec irgessskts ilp
//
LOCUS       NP_001397935            1105 aa            linear   PRI 21-NOV-2025
DEFINITION  phospholipid-transporting ATPase IB isoform 4 [Homo sapiens].
ACCESSION   NP_001397935 XP_011533408
VERSION     NP_001397935.1
DBSOURCE    REFSEQ: accession NM_001411006.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Matsell,E., Mazaheri,M., Andersen,J.P. and Molday,R.S.
  TITLE     Structural and functional properties of the N- and C-terminal
            segments of the P4-ATPase phospholipid flippase ATP8A2
  JOURNAL   J Biol Chem 301 (1), 108065 (2025)
   PUBMED   39662833
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Matsell,E., Andersen,J.P. and Molday,R.S.
  TITLE     Functional and in silico analysis of ATP8A2 and other P4-ATPase
            variants associated with human genetic diseases
  JOURNAL   Dis Model Mech 17 (6) (2024)
   PUBMED   38436085
  REMARK    GeneRIF: Functional and in silico analysis of ATP8A2 and other
            P4-ATPase variants associated with human genetic diseases.
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Mogensen,L.S., Mikkelsen,S.A., Tadini-Buoninsegni,F., Holm,R.,
            Matsell,E., Vilsen,B., Molday,R.S. and Andersen,J.P.
  TITLE     On the track of the lipid transport pathway of the phospholipid
            flippase ATP8A2 - Mutation analysis of residues of the
            transmembrane segments M1, M2, M3 and M4
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (1), 119570 (2024)
   PUBMED   37678495
  REMARK    GeneRIF: On the track of the lipid transport pathway of the
            phospholipid flippase ATP8A2 - Mutation analysis of residues of the
            transmembrane segments M1, M2, M3 and M4.
            Review article
REFERENCE   4  (residues 1 to 1105)
  AUTHORS   van der Mark,V.A., Elferink,R.P. and Paulusma,C.C.
  TITLE     P4 ATPases: flippases in health and disease
  JOURNAL   Int J Mol Sci 14 (4), 7897-7922 (2013)
   PUBMED   23579954
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1105)
  AUTHORS   Coleman,J.A. and Molday,R.S.
  TITLE     Critical role of the beta-subunit CDC50A in the stable expression,
            assembly, subcellular localization, and lipid transport activity of
            the P4-ATPase ATP8A2
  JOURNAL   J Biol Chem 286 (19), 17205-17216 (2011)
   PUBMED   21454556
  REMARK    GeneRIF: CDC50A is the beta-subunit of ATP8A2 and is crucial for
            the correct folding, stable expression, export from endoplasmic
            reticulum, and phosphatidylserine flippase activity of ATP8A2
REFERENCE   6  (residues 1 to 1105)
  AUTHORS   van der Velden,L.M., Wichers,C.G., van Breevoort,A.E.,
            Coleman,J.A., Molday,R.S., Berger,R., Klomp,L.W. and van de
            Graaf,S.F.
  TITLE     Heteromeric interactions required for abundance and subcellular
            localization of human CDC50 proteins and class 1 P4-ATPases
  JOURNAL   J Biol Chem 285 (51), 40088-40096 (2010)
   PUBMED   20947505
REFERENCE   7  (residues 1 to 1105)
  AUTHORS   Cacciagli,P., Haddad,M.R., Mignon-Ravix,C., El-Waly,B., Moncla,A.,
            Missirian,C., Chabrol,B. and Villard,L.
  TITLE     Disruption of the ATP8A2 gene in a patient with a t(10;13) de novo
            balanced translocation and a severe neurological phenotype
  JOURNAL   Eur J Hum Genet 18 (12), 1360-1363 (2010)
   PUBMED   20683487
REFERENCE   8  (residues 1 to 1105)
  AUTHORS   Coleman,J.A., Kwok,M.C. and Molday,R.S.
  TITLE     Localization, purification, and functional reconstitution of the
            P4-ATPase Atp8a2, a phosphatidylserine flippase in photoreceptor
            disc membranes
  JOURNAL   J Biol Chem 284 (47), 32670-32679 (2009)
   PUBMED   19778899
  REMARK    GeneRIF: P4-ATPase Atp8a2 is a phosphatidylserine flippase in
            photoreceptor disc membranes
REFERENCE   9  (residues 1 to 1105)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1105)
  AUTHORS   Sun,X.L., Li,D., Fang,J., Noyes,I., Casto,B., Theil,K., Shuler,C.
            and Milo,G.E.
  TITLE     Changes in levels of normal ML-1 gene transcripts associated with
            the conversion of human nontumorigenic to tumorigenic phenotypes
  JOURNAL   Gene Expr 8 (2), 129-139 (1999)
   PUBMED   10551800
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138958.18, AL356316.18,
            AL669971.2, AL136438.10, AL157366.12 and AL138815.6.
            
            On Aug 20, 2022 this sequence version replaced XP_011533408.1.
            
            Summary: The protein encoded by this gene is a member of the P4
            ATPase family of proteins, which are thought to be involved in a
            process called lipid flipping, whereby phospholipids are
            translocated inwards from the exoplasmic leaflet to the cytosolic
            leaflet of the cell membrane, which aids in generating and
            maintaining asymmetry in membrane lipids. This protein is predicted
            to contain an E1 E2 ATPase, a haloacid dehalogenase-like hydrolase
            (HAD) domain, and multiple transmembrane domains. Associations
            between this protein and cell cycle control protein 50A are
            important for translocation of phosphatidylserine across membranes.
            Mutations in this gene have been associated with a syndrome
            (CAMRQ4) characterized by cerebellar ataxia and cognitive
            disabilities. In addition, a translocation breakpoint within this
            gene was observed in an individual with neurological dysfunction.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Jul 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.165970.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.13"
     Protein         1..1105
                     /product="phospholipid-transporting ATPase IB isoform 4"
                     /EC_number="7.6.2.1"
                     /note="ATPase, aminophospholipid transporter-like, class
                     I, type 8A, member 2; probable phospholipid-transporting
                     ATPase IB; P4-ATPase flippase complex alpha subunit
                     ATP8A2; ATPase, aminophospholipid transporter, class I,
                     type 8A, member 2"
                     /calculated_mol_wt=123489
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P98200; propagated from
                     UniProtKB/Swiss-Prot (Q9NTI2.3)"
     Region          68..1051
                     /region_name="ATPase-Plipid"
                     /note="phospholipid-translocating P-type ATPase, flippase;
                     TIGR01652"
                     /db_xref="CDD:273734"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTI2.3)"
     Site            120..140
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTI2.3)"
     Site            317..337
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTI2.3)"
     Site            365..385
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTI2.3)"
     Site            371
                     /site_type="other"
                     /note="Involved in the recognition of the lipid substrate
                     on the exoplasmic side.
                     /evidence=ECO:0000250|UniProtKB:C7EXK4; propagated from
                     UniProtKB/Swiss-Prot (Q9NTI2.3)"
     Site            376
                     /site_type="other"
                     /note="Involved in the release of the transported lipid
                     into the cytosolic leaflet.
                     /evidence=ECO:0000250|UniProtKB:C7EXK4; propagated from
                     UniProtKB/Swiss-Prot (Q9NTI2.3)"
     Site            order(428..430,569,592..594,658,705..707,795,798,801,821,
                     824)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     Site            888..908
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTI2.3)"
     Site            911..931
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTI2.3)"
     Site            960..980
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTI2.3)"
     Site            998..1018
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTI2.3)"
     Site            1029..1049
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTI2.3)"
     CDS             1..1105
                     /gene="ATP8A2"
                     /gene_synonym="ATP; ATPIB; CAMRQ4; IB; ML-1"
                     /coded_by="NM_001411006.1:240..3557"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS91792.1"
                     /db_xref="GeneID:51761"
                     /db_xref="HGNC:HGNC:13533"
                     /db_xref="MIM:605870"
ORIGIN      
        1 mlngagldka lkmslprrsr irssvgpvrs slgykkaede msratsvgdq leapartiyl
       61 nqphlnkfrd nqistakysv ltflprflye qirraanaff lfiallqqip dvsptgrytt
      121 lvpliiilti agikeivedf krhkadnavn kkktivlrng mwhtimwkev avgdivkvvn
      181 gqylpadvvl lsssepqamc yvetanldge tnlkirqgls htadmqtrev lmklsgtiec
      241 egpnrhlydf tgnlnldgks lvalgpdqil lrgtqlrntq wvfgivvytg hdtklmqnst
      301 kaplkrsnve kvtnvqilvl fgillvmalv ssagalywnr shgeknwyik kmdttsdnfg
      361 ynlltfiily nnlipisllv tlevvkytqa lfinwdtdmy yigndtpama rtsnlneelg
      421 qvkylfsdkt gtltcnimnf kkcsiagvty ghfpelarep ssddfcrmpp pcsdscdfdd
      481 prllkniedr hptapciqef ltllavchtv vpekdgdnii yqasspdeaa lvkgakklgf
      541 vftartpfsv iieamgqeqt fgilnvlefs sdrkrmsviv rtpsgrlrly ckgadnvife
      601 rlskdskyme etlchleyfa teglrtlcva yadlseneye ewlkvyqeas tilkdraqrl
      661 eecyeiiekn llllgataie drlqagvpet iatllkaeik iwvltgdkqe tainigyscr
      721 lvsqnmalil lkedsldatr aaitqhctdl gnllgkendv aliidghtlk yalsfevrrs
      781 fldlalscka viccrvsplq kseivdvvkk rvkaitlaig dgandvgmiq tahvgvgisg
      841 negmqatnns dyaiaqfsyl eklllvhgaw synrvtkcil ycfyknvvly iielwfafvn
      901 gfsgqilfer wciglynvif talppftlgi fersctqesm lrfpqlykit qngegfntkv
      961 fwghcinalv hslilfwfpm kalehdtvlt sghatdylfv gnivytyvvv tvclkaglet
     1021 tawtkfshla vwgsmltwlv ffgiystiwp tipiapdmrg qltcmvcpdt stqtlagycp
     1081 pcctagpcap ephsssaaph tgnci
//
LOCUS       NP_001425616             935 aa            linear   PRI 21-NOV-2025
DEFINITION  splicing regulator ARVCF isoform 5 [Homo sapiens].
ACCESSION   NP_001425616 XP_006724308 XP_054181606
VERSION     NP_001425616.1
DBSOURCE    REFSEQ: accession NM_001438687.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 935)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 935)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 935)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 935)
  AUTHORS   Suzuki,N., Idogawa,M., Tange,S., Ohashi,T., Sasaki,Y., Nakase,H.
            and Tokino,T.
  TITLE     p53-induced ARVCF modulates the splicing landscape and supports the
            tumor suppressive function of p53
  JOURNAL   Oncogene 39 (10), 2202-2211 (2020)
   PUBMED   31827232
  REMARK    GeneRIF: p53-induced ARVCF modulates the splicing landscape and
            supports the tumor suppressive function of p53.
REFERENCE   5  (residues 1 to 935)
  AUTHORS   Zhang,D., Tang,N., Liu,Y. and Wang,E.H.
  TITLE     ARVCF expression is significantly correlated with the malignant
            phenotype of non-small cell lung cancer
  JOURNAL   Mol Carcinog 54 Suppl 1, E185-E191 (2015)
   PUBMED   25683624
  REMARK    GeneRIF: observed ARVCF-dependent changes in small GTPase (mainly
            RhoA) activity in lung cancer cells. We confirmed that ARVCF plays
            an important role in the malignant phenotype
REFERENCE   6  (residues 1 to 935)
  AUTHORS   Mariner,D.J., Wang,J. and Reynolds,A.B.
  TITLE     ARVCF localizes to the nucleus and adherens junction and is
            mutually exclusive with p120(ctn) in E-cadherin complexes
  JOURNAL   J Cell Sci 113 (Pt 8), 1481-1490 (2000)
   PUBMED   10725230
REFERENCE   7  (residues 1 to 935)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   8  (residues 1 to 935)
  AUTHORS   Sirotkin,H., Morrow,B., Saint-Jore,B., Puech,A., Das Gupta,R.,
            Patanjali,S.R., Skoultchi,A., Weissman,S.M. and Kucherlapati,R.
  TITLE     Identification, characterization, and precise mapping of a human
            gene encoding a novel membrane-spanning protein from the 22q11
            region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 42 (2), 245-251 (1997)
   PUBMED   9192844
REFERENCE   9  (residues 1 to 935)
  AUTHORS   Sirotkin,H., O'Donnell,H., DasGupta,R., Halford,S., St Jore,B.,
            Puech,A., Parimoo,S., Morrow,B., Skoultchi,A., Weissman,S.M.,
            Scambler,P. and Kucherlapati,R.
  TITLE     Identification of a new human catenin gene family member (ARVCF)
            from the region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 41 (1), 75-83 (1997)
   PUBMED   9126485
REFERENCE   10 (residues 1 to 935)
  AUTHORS   Lindsay,E.A., Goldberg,R., Jurecic,V., Morrow,B., Carlson,C.,
            Kucherlapati,R.S., Shprintzen,R.J. and Baldini,A.
  TITLE     Velo-cardio-facial syndrome: frequency and extent of 22q11
            deletions
  JOURNAL   Am J Med Genet 57 (3), 514-522 (1995)
   PUBMED   7677167
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005663.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_006724308.1, XP_054181606.1.
            
            Summary: Armadillo Repeat gene deleted in Velo-Cardio-Facial
            syndrome (ARVCF) is a member of the catenin family. This family
            plays an important role in the formation of adherens junction
            complexes, which are thought to facilitate communication between
            the inside and outside environments of a cell. The ARVCF gene was
            isolated in the search for the genetic defect responsible for the
            autosomal dominant Velo-Cardio-Facial syndrome (VCFS), a relatively
            common human disorder with phenotypic features including cleft
            palate, conotruncal heart defects and facial dysmorphology. The
            ARVCF gene encodes a protein containing two motifs, a coiled coil
            domain in the N-terminus and a 10 armadillo repeat sequence in the
            midregion. Since these sequences can facilitate protein-protein
            interactions ARVCF is thought to function in a protein complex. In
            addition, ARVCF contains a predicted nuclear-targeting sequence
            suggesting that it may have a function as a nuclear protein.
            [provided by RefSeq, Jun 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..935
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..935
                     /product="splicing regulator ARVCF isoform 5"
                     /note="armadillo repeat protein deleted in
                     velo-cardio-facial syndrome; armadillo repeat gene deleted
                     in velocardiofacial syndrome; splicing regulator ARVCF"
                     /calculated_mol_wt=101510
     Region          95..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            170
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P98203; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          186..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          266..290
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          348..387
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          360..385
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(376,380,384,418,422,426,461,466,470)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          389..428
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          390..429
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          393..429
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          432..473
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          433..467
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          436..471
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          468..508
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          478..529
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          526..565
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          575..622
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          590..614
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          607..623
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            642
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          646..686
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          656..692
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          656..692
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          699..738
                     /region_name="ARM 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          702..737
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          702..736
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          739..781
                     /region_name="ARM 9"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          743..788
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          794..826
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            864
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            871
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            872
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            915
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     CDS             1..935
                     /gene="ARVCF"
                     /coded_by="NM_001438687.1:308..3115"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:421"
                     /db_xref="HGNC:HGNC:728"
                     /db_xref="MIM:602269"
ORIGIN      
        1 medcnvhsaa silasvkeqe arferltral eqerrhvalq leraqqpgmv sggmgsgqpl
       61 pmawqqlvlq eqspgsqasl atmpeapdvl eetvtveedp gtptshvsiv tsedgttrrt
      121 etkvtktvkt vttrtvrqvp vgpdglplld ggpplgpfad galdrhfllr gggpvatlsr
      181 aylssgggfp egpeprdsps ygslsrglgm rppragplgp gpgdgcftlp ghreafpvgp
      241 epgppggrsl perfqaepyg leddtrslaa ddeggpelep dygtatrrrp ecgrglhtra
      301 yedtaddgge laderpafpm vtaplaqper gsmgsldrlv rrspsvdsar keprwrdpel
      361 pevlamlrhp vdpvkanaaa ylqhlcfene gvkrrvrqlr glpllvalld hpraevrrra
      421 cgalrnlsyg rdtdnkaair dcggvpalvr llraardnev relvtgtlwn lssyeplkmv
      481 iidhglqtlt hevivphsgw erepnedskp rdaewttvfk ntsgclrnvs sdgaearrrl
      541 receglvdal lhalqsavgr kdtdnksven cvcimrnlsy hvhkevpgad ryqeaepgpl
      601 gsavgsqrrr rddascfggk kakeewfhqg kkdgemdrnf dtldlpkrte aakgfellyq
      661 pevvrlylsl ltesrnfntl eaaagalqnl sagnwmwaty iratvrkerg lpvlvellqs
      721 etdkvvrava ialrnlsldr rnkdligsya maelvrnvrn aqapprpgac leedtvvavl
      781 ntiheivsds ldnarsllqa rgvpalvalv assqsvreak aashvlqtvw sykelrgtlq
      841 kdgwtkarfq saaatakgpk galspggfdd stlplvdksl egektgsrdv ipmdalgpdg
      901 ystvdrrerr prgassagea sekeplkgpg pascs
//
LOCUS       NP_001425988            2608 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HECTD1 isoform 7 [Homo sapiens].
ACCESSION   NP_001425988 XP_024305294 XP_054231746
VERSION     NP_001425988.1
DBSOURCE    REFSEQ: accession NM_001439059.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2608)
  AUTHORS   Oxman,E., Li,H., Wang,H.Y. and Zohn,I.E.
  TITLE     Identification and functional analysis of rare HECTD1 missense
            variants in human neural tube defects
  JOURNAL   Hum Genet 143 (3), 263-277 (2024)
   PUBMED   38451291
  REMARK    GeneRIF: Identification and functional analysis of rare HECTD1
            missense variants in human neural tube defects.
REFERENCE   2  (residues 1 to 2608)
  AUTHORS   Zhang,J., Xin,Y., Ling,X., Liang,H., Zhang,L., Fang,C. and Ma,J.
  TITLE     Nucleoporin 93, a new substrate of the E3 ubiquitin protein ligase
            HECTD1, promotes esophageal squamous cell carcinoma progression
  JOURNAL   Hum Cell 37 (1), 245-257 (2024)
   PUBMED   37993750
  REMARK    GeneRIF: Nucleoporin 93, a new substrate of the E3 ubiquitin
            protein ligase HECTD1, promotes esophageal squamous cell carcinoma
            progression.
REFERENCE   3  (residues 1 to 2608)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 2608)
  AUTHORS   Vaughan,N., Scholz,N., Lindon,C. and Licchesi,J.D.F.
  TITLE     The E3 ubiquitin ligase HECTD1 contributes to cell proliferation
            through an effect on mitosis
  JOURNAL   Sci Rep 12 (1), 13160 (2022)
   PUBMED   35915203
  REMARK    GeneRIF: The E3 ubiquitin ligase HECTD1 contributes to cell
            proliferation through an effect on mitosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2608)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 2608)
  AUTHORS   Aleidi,S.M., Yang,A., Sharpe,L.J., Rao,G., Cochran,B.J., Rye,K.A.,
            Kockx,M., Brown,A.J. and Gelissen,I.C.
  TITLE     The E3 ubiquitin ligase, HECTD1, is involved in ABCA1-mediated
            cholesterol export from macrophages
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1863 (4), 359-368 (2018)
   PUBMED   29306077
  REMARK    GeneRIF: HECTD1 may be involved in the regulation of ABCA1-mediated
            cholesterol export from unloaded macrophages to apoA-I.
REFERENCE   7  (residues 1 to 2608)
  AUTHORS   Fang,S., Guo,H., Cheng,Y., Zhou,Z., Zhang,W., Han,B., Luo,W.,
            Wang,J., Xie,W. and Chao,J.
  TITLE     circHECTD1 promotes the silica-induced pulmonary
            endothelial-mesenchymal transition via HECTD1
  JOURNAL   Cell Death Dis 9 (3), 396 (2018)
   PUBMED   29540674
  REMARK    GeneRIF: SiO2 concomitantly increased circHECTD1 expression, which,
            in turn, inhibited HECTD1 protein expression.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 2608)
  AUTHORS   Shen,X., Jia,Z., D'Alonzo,D., Wang,X., Bruder,E., Emch,F.H., De
            Geyter,C. and Zhang,H.
  TITLE     HECTD1 controls the protein level of IQGAP1 to regulate the
            dynamics of adhesive structures
  JOURNAL   Cell Commun Signal 15 (1), 2 (2017)
   PUBMED   28073378
  REMARK    GeneRIF: Hectd1 regulates the protein level of IQGAP1 through
            ubiquitination.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 2608)
  AUTHORS   Helander,S., Montecchio,M., Lemak,A., Fares,C., Almlof,J., Yi,Y.,
            Yee,A., Arrowsmith,C., DhePaganon,S. and Sunnerhagen,M.
  TITLE     Basic Tilted Helix Bundle - a new protein fold in human
            FKBP25/FKBP3 and HectD1
  JOURNAL   Biochem Biophys Res Commun 447 (1), 26-31 (2014)
   PUBMED   24667607
  REMARK    GeneRIF: our high-resolution structures show a new fold composed of
            five small helices where H3 and H4 are tilted in a novel
            arrangement; we call this fold the Basic Tilted Helix Bundle (BTHB)
            domain.
REFERENCE   10 (residues 1 to 2608)
  AUTHORS   Tran,H., Bustos,D., Yeh,R., Rubinfeld,B., Lam,C., Shriver,S.,
            Zilberleyb,I., Lee,M.W., Phu,L., Sarkar,A.A., Zohn,I.E.,
            Wertz,I.E., Kirkpatrick,D.S. and Polakis,P.
  TITLE     HectD1 E3 ligase modifies adenomatous polyposis coli (APC) with
            polyubiquitin to promote the APC-axin interaction
  JOURNAL   J Biol Chem 288 (6), 3753-3767 (2013)
   PUBMED   23277359
  REMARK    GeneRIF: HectD1 promotes the APC-Axin interaction to negatively
            regulate Wnt signaling.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136418.4, AL121808.4 and KC877516.1.
            
            On or before Apr 25, 2025 this sequence version replaced
            XP_024305294.1, XP_054231746.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2608258.1,
                                           SRR14038194.1490007.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2608
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..2608
                     /product="E3 ubiquitin-protein ligase HECTD1 isoform 7"
                     /EC_number="2.3.2.26"
                     /note="E3 ubiquitin-protein ligase HECTD1; E3 ligase for
                     inhibin receptor; HECT domain-containing protein 1; HECT
                     domain containing E3 ubiquitin protein ligase 1; HECT-type
                     E3 ubiquitin transferase HECTD1"
                     /calculated_mol_wt=289008
     Region          246..269
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          <366..>479
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          366..393
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          395..424
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          396..426
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(397,401..402,405..407,409..410,414,417,426,428,
                     432..433,436..438,440..441,445,448,457,459,461,465..466,
                     469..471,473..474,478)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          426..455
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          428..457
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          459..491
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          489..513
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          579..612
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          627..657
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZR2; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          707..748
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1107..1240
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     Region          1277..1335
                     /region_name="MIB_HERC2"
                     /note="Mib_herc2; pfam06701"
                     /db_xref="CDD:461991"
     Region          1343..1406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZR2; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1433..1483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1496..1515
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZR2; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1592..1611
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1758
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1770
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1775..1795
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1891..1956
                     /region_name="BTHB_HectD1"
                     /note="basic tilted helix bundle (BTHB) domain found in
                     HECT domain-containing protein 1 (HectD1) and similar
                     proteins; cd21062"
                     /db_xref="CDD:439138"
     Region          2027..2101
                     /region_name="K-box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          2129..2606
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(2135,2164,2174,2261,2539,2571..2572,2575..2579,2599,
                     2605)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Region          2295..2316
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            2316
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            order(2354,2357..2358,2360..2361,2364,2406,2408,
                     2412..2413,2415,2421,2426,2443,2447)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..2608
                     /gene="HECTD1"
                     /gene_synonym="EULIR"
                     /coded_by="NM_001439059.1:800..8626"
                     /note="isoform 7 is encoded by transcript variant 8"
                     /db_xref="GeneID:25831"
                     /db_xref="HGNC:HGNC:20157"
                     /db_xref="MIM:618649"
ORIGIN      
        1 madvdpdtll ewlqmgqgde rdmqlialeq lcmlllmsdn vdrcfetcpp rtflpalcki
       61 fldesapdnv levtaraity yldvsaectr rivgvdgaik alcnrlvvve lnnrtsrdla
      121 eqcvkvleli ctresgavfe agglncvltf irdsghlvhk dtlhsamavv srlcgkmepq
      181 dssleicves lssllkhedh qvsdgalrcf asladrftrr gvdpaplakh glteellsrm
      241 aaaggtvsgp ssackpgrst tgapsttads klsnqvstiv sllstlcrgs pvvthdllrs
      301 elpdsiesal qgdercvldt mrlvdlllvl lfegrkalpk ssagstgrip glrrldssge
      361 rshrqlidci rskdtdalid aidtgafevn fmddvgqtll nwasafgtqe mveflcerga
      421 dvnrgqrsss lhyaacfgrp qvaktllrhg anpdlrdedg ktpldkarer ghsevvailq
      481 spgdwmcpvn kgddkkkkdt nkdeeecnep kgdpemapiy lkrllpvfaq tfqqtmlpsi
      541 rkaslalirk mihfcseall kevcdsdvgh nlptilveit atvldqeddd dghllalqii
      601 rdlvdkggdi fldqlarlgv iskvstlagp ssddeneees kpekedepqe dakelqqgkp
      661 yhwrdwsiir grdclyiwsd aaalelsngs ngwfrfildg klatmyssgs peggsdsses
      721 rsefleklqr argqvkpsts sqpilsapgp tkltvgnwsl tclkegeiai hnsdgqqati
      781 lkedlpgfvf esnrgtkhsf taetslgsef vtgwtgkrgr klksklektk qkvrtmardl
      841 yddhfkaves mprgvvvtlr niatqlessw elhtnrqcie sentwrdlmk talenlivll
      901 kdentispye mcssglvqal ltvlnnsmdl dmkqdcsqlv erinvfktaf seneddesrp
      961 avalirklia vlesierlpl hlydtpgsty nlqiltrrlr frlerapget alidrtgrml
     1021 kmeplatves leqyllkmva kqwydfdrss fvfvrklreg qnfifrhqhd fdengiiywi
     1081 gtnaktayew vnpaayglvv vtssegrnlp ygrledilsr dnsalnchsn ddknawfaid
     1141 lglwvipsay tlrhargygr salrnwvfqv skdgqnwtsl ythvddcsln epgstatwpl
     1201 dppkdekqgw rhvrikqmgk nasgqthyls lsgfelygtv ngvcedqlgk aakeaeanlr
     1261 rqrrlvrsqv lkymvpgarv irgldwkwrd qdgspqgegt vtgelhngwi dvtwdaggsn
     1321 syrmgaegkf dlklapgydp dtvaspkpvs stvsgttqsw sslvknncpd ktsaaagsss
     1381 rkgssssvcs vasssdislg stkterrsei vmehsivsga dvhepivvls saenvpqtev
     1441 gssssastst ltaetgsena erklgpdssv rtpgessais mgivsvsspd vssvseltnk
     1501 eaasqrplss sasnrlsvss llaagapmss sasvpnlssr etsslesfvr rvaniartna
     1561 tnnmnlsrss sdnntntlgr nvmstatspl mgaqsfpnlt tpgttstvtm stssvtsssn
     1621 vatattvlsv gqslsntltt sltstssesd tgqeaeysly dfldscrast llaelddded
     1681 lpepdeedde neddnqedqe yeeilrrpsl qrragsrsdv thhavtsqlp qvpagagsrp
     1741 igeqeeeeye tkggrrrtwd ddyvlkrqfs alvpafdprp grtnvqqttd leipppgtph
     1801 selleevect psprlaltlk vtglgttrev elpltnfrst ifyyvqkllq lscngnvksd
     1861 klrriwepty timyremkds dkekengkmg cwsiehveqy lgtdelpknd litylqknad
     1921 aaflrhwklt gtnksirknr ncsqliaayk dfcehgtksg lnqgaistlq ssdilnltke
     1981 qpqakagngq nscgvedvlq llrilyivas dpysrisqed gdeqpqftfp pdeftskkit
     2041 tkilqqieep lalasgalpd wceqltskcp flipfetrql yftctafgas raivwlqnrr
     2101 eatvertrtt ssvrrddpge frvgrlkher vkvprgeslm ewaenvmqih adrksvleve
     2161 flgeegtglg ptlefyalva aefqrtdlga wlcddnfpdd esrhvdlggg lkppgyyvqr
     2221 scglftapfp qdsdelerit klfhflgifl akciqdnrlv dlpiskpffk lmcmgdiksn
     2281 mskliyesrg drdlhctesq seasteeghd slsvgsfeed sksefildpp kpkppawfng
     2341 iltwedfelv nphrarflke ikdlaikrrq ilsnkglsed ekntklqelv lknpsgsgpp
     2401 lsiedlglnf qfcpssriyg ftavdlkpsg edemitmdna eeyvdlmfdf cmhtgiqkqm
     2461 eafrdgfnkv fpmeklssfs heevqmilcg nqspswaaed iinytepklg ytrdspgflr
     2521 fvrvlcgmss derkaflqft tgcstlppgg lanlhprltv vrkvdatdas ypsvntcvhy
     2581 lklpeyssee imrerllaat mekgfhln
//
LOCUS       NP_001400007             333 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001400007
VERSION     NP_001400007.1
DBSOURCE    REFSEQ: accession NM_001413078.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3369054.1,
                                           SRR14038191.4144450.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..333
                     /product="mitochondrial fission regulator 1 isoform 1
                     precursor"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=31469
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=5550
     Region          22..251
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     mat_peptide     49..333
                     /product="Mitochondrial fission regulator 1.
                     /id=PRO_0000096622"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=31469
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15390.2)"
     Region          177..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          179..304
                     /region_name="Necessary and sufficient to promote
                     mitochondrial fission. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          288..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     CDS             1..333
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001413078.1:442..1443"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 13"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsvlwsrkpy gssrsivrki gtnlsliqcp rvqfqinsha
       61 tewspshpge davasfadvg wvakeegecs arlrtevrsr pplqddllff ekapsrqisl
      121 pdlsqeepql ktpalaneea lqkicalene laalraqiak ivtqqeqqnl tagdldsttf
      181 gtipphpppp ppplpppalg lhqstsavdl ikerrekran agktlvknnp kkpempnmle
      241 ilkemnsvkl rsvkrseqdv kpkpvdatdp aaliaealkk kfayryrsds qdevekgipk
      301 seseatserv lfgphmlkpt gkmkalienv sds
//
LOCUS       NP_001397904            1656 aa            linear   PRI 21-NOV-2025
DEFINITION  alsin isoform 3 [Homo sapiens].
ACCESSION   NP_001397904 XP_016860058
VERSION     NP_001397904.1
DBSOURCE    REFSEQ: accession NM_001410975.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1656)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1656)
  AUTHORS   Miceli,M., Cannariato,M., Tortarolo,R., Pallante,L., Zizzi,E.A. and
            Deriu,M.A.
  TITLE     Conformational Dynamics and Molecular Characterization of Alsin
            MORN Monomer and Dimeric Assemblies
  JOURNAL   Proteins 92 (11), 1343-1353 (2024)
   PUBMED   39023312
  REMARK    GeneRIF: Conformational Dynamics and Molecular Characterization of
            Alsin MORN Monomer and Dimeric Assemblies.
REFERENCE   3  (residues 1 to 1656)
  AUTHORS   Silva,P., Hernandez,N., Tapia,H., Gaete-Ramirez,B., Torres,P.,
            Flores,T., Herrera,D., Caceres-Verschae,A., Acuna,R.A.,
            Varas-Godoy,M. and Torres,V.A.
  TITLE     Tumor-derived hypoxic small extracellular vesicles promote
            endothelial cell migration and tube formation via
            ALS2/Rab5/beta-catenin signaling
  JOURNAL   FASEB J 38 (11), e23716 (2024)
   PUBMED   38847490
  REMARK    GeneRIF: Tumor-derived hypoxic small extracellular vesicles promote
            endothelial cell migration and tube formation via
            ALS2/Rab5/beta-catenin signaling.
REFERENCE   4  (residues 1 to 1656)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 1656)
  AUTHORS   Hadano,S., Hand,C.K., Osuga,H., Yanagisawa,Y., Otomo,A.,
            Devon,R.S., Miyamoto,N., Showguchi-Miyata,J., Okada,Y.,
            Singaraja,R., Figlewicz,D.A., Kwiatkowski,T., Hosler,B.A.,
            Sagie,T., Skaug,J., Nasir,J., Brown,R.H. Jr., Scherer,S.W.,
            Rouleau,G.A., Hayden,M.R. and Ikeda,J.E.
  TITLE     A gene encoding a putative GTPase regulator is mutated in familial
            amyotrophic lateral sclerosis 2
  JOURNAL   Nat Genet 29 (2), 166-173 (2001)
   PUBMED   11586298
REFERENCE   6  (residues 1 to 1656)
  AUTHORS   Yang,Y., Hentati,A., Deng,H.X., Dabbagh,O., Sasaki,T., Hirano,M.,
            Hung,W.Y., Ouahchi,K., Yan,J., Azim,A.C., Cole,N., Gascon,G.,
            Yagmour,A., Ben-Hamida,M., Pericak-Vance,M., Hentati,F. and
            Siddique,T.
  TITLE     The gene encoding alsin, a protein with three guanine-nucleotide
            exchange factor domains, is mutated in a form of recessive
            amyotrophic lateral sclerosis
  JOURNAL   Nat Genet 29 (2), 160-165 (2001)
   PUBMED   11586297
REFERENCE   7  (residues 1 to 1656)
  AUTHORS   Hadano,S., Nichol,K., Brinkman,R.R., Nasir,J., Martindale,D.,
            Koop,B.F., Nicholson,D.W., Scherer,S.W., Ikeda,J.E. and Hayden,M.R.
  TITLE     A yeast artificial chromosome-based physical map of the juvenile
            amyotrophic lateral sclerosis (ALS2) critical region on human
            chromosome 2q33-q34
  JOURNAL   Genomics 55 (1), 106-112 (1999)
   PUBMED   9889004
REFERENCE   8  (residues 1 to 1656)
  AUTHORS   Hosler,B.A., Sapp,P.C., Berger,R., O'Neill,G., Bejaoui,K.,
            Hamida,M.B., Hentati,F., Chin,W., McKenna-Yasek,D., Haines,J.L.,
            Patterson,D., Horvitz,H.R., Brown,R.H. Jr. and Day,C.B.
  TITLE     Refined mapping and characterization of the recessive familial
            amyotrophic lateral sclerosis locus (ALS2) on chromosome 2q33
  JOURNAL   Neurogenetics 2 (1), 34-42 (1998)
   PUBMED   9933298
REFERENCE   9  (residues 1 to 1656)
  AUTHORS   Siddique,N. and Siddique,T.
  TITLE     Amyotrophic Lateral Sclerosis Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301623
REFERENCE   10 (residues 1 to 1656)
  AUTHORS   Orrell,R.W.
  TITLE     ALS2-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301421
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007242.3 and AC007279.4.
            
            On Aug 18, 2022 this sequence version replaced XP_016860058.1.
            
            Summary: The protein encoded by this gene contains an
            ATS1/RCC1-like domain, a RhoGEF domain, and a vacuolar protein
            sorting 9 (VPS9) domain, all of which are guanine-nucleotide
            exchange factors that activate members of the Ras superfamily of
            GTPases. The protein functions as a guanine nucleotide exchange
            factor for the small GTPase RAB5. The protein localizes with RAB5
            on early endosomal compartments, and functions as a modulator for
            endosomal dynamics. Mutations in this gene result in several forms
            of juvenile lateral sclerosis and infantile-onset ascending spastic
            paralysis. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3643868.1,
                                           SRR11853558.15057.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1656
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..1656
                     /product="alsin isoform 3"
                     /note="alsin; amyotrophic lateral sclerosis 2 protein;
                     ALS2, alsin Rho guanine nucleotide exchange factor;
                     amyotrophic lateral sclerosis 2 chromosomal region
                     candidate gene 6 protein; amyotrophic lateral sclerosis 2
                     (juvenile)"
                     /calculated_mol_wt=183313
     Region          <39..219
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
     Region          59..108
                     /region_name="RCC1 1. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q42.2)"
     Region          109..167
                     /region_name="RCC1 2. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q42.2)"
     Region          169..218
                     /region_name="RCC1 3. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q42.2)"
     Region          432..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q42.2)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96Q42.2)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96Q42.2)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96Q42.2)"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96Q42.2)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P0C5Y8; propagated from
                     UniProtKB/Swiss-Prot (Q96Q42.2)"
     Region          525..576
                     /region_name="RCC1 4. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q42.2)"
     Region          <527..>683
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
     Site            533
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96Q42.2)"
     Region          578..627
                     /region_name="RCC1 5. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q42.2)"
     Region          695..879
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cl02571"
                     /db_xref="CDD:470622"
     Site            order(697,701,802,834..835,838..839,841..842,845..846,
                     850..851,879)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          905..1010
                     /region_name="PH_alsin"
                     /note="Alsin Pleckstrin homology (PH) domain; cd13269"
                     /db_xref="CDD:241423"
     Region          <1049..1249
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
     Region          1049..1071
                     /region_name="MORN 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q42.2)"
     Region          1072..1094
                     /region_name="MORN 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q42.2)"
     Region          1100..1122
                     /region_name="MORN 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q42.2)"
     Region          1123..1145
                     /region_name="MORN 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q42.2)"
     Region          1151..1173
                     /region_name="MORN 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q42.2)"
     Region          1175..1197
                     /region_name="MORN 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q42.2)"
     Region          1198..1220
                     /region_name="MORN 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q42.2)"
     Region          1221..1244
                     /region_name="MORN 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q42.2)"
     Site            1334
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P0C5Y8; propagated from
                     UniProtKB/Swiss-Prot (Q96Q42.2)"
     Region          1553..1655
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..1656
                     /gene="ALS2"
                     /gene_synonym="ALS2CR6; ALSJ; IAHSP; PLSJ"
                     /coded_by="NM_001410975.1:118..5088"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92925.1"
                     /db_xref="GeneID:57679"
                     /db_xref="HGNC:HGNC:443"
                     /db_xref="MIM:606352"
ORIGIN      
        1 mdskkrsste aegskerglv hiwqagsfpi tperlpgwgg ktvlqaalgv khgvlltedg
       61 evysfgtlpw rsgpveicps spilenalvg qyvitvatgs fhsgavtdng vaymwgensa
      121 gqcavanqqy vpepnpvsia dseaspllav rilqlacgee htlalsisre iwawgtgcql
      181 glittafpvt kpqkvehlag rvvlqvacga fhslalvqcl psqdlkpvpe rcnqcsqlli
      241 tmtdkedhvi isdshccplg vtltesqaen hastalspst etldrqeevf entlvandqs
      301 vatelnavsa qitssdamss qqnvmgttei ssarnipsyp dtqavneylr klsdhsvred
      361 sehgekpvps qplleeaipn lhsppttsts alnslvvsca savgvrvaat yeagalslkk
      421 vmnfysttpc etgaqagssa igpeglkdsr eeqvkqesmq gkkssslvdi reeeteggsr
      481 rlslpgllsq vsprllrkaa rvktrtvvlt ptysgeadal lpslrtevwt wgkgkegqlg
      541 hgdvlprlqp lcvkcldgke vihleaggyh slaltaksqv yswgsntfgq lghsdfpttv
      601 prlakissen gvwsiaagrd yslflvdted fqpglyysgr qdptegdnlp enhsgsktpv
      661 llscsklgyi srvtagkdsy lalvdknimg yiaslhelat terrfyskls diksqilrpl
      721 lslenlgttt tvqllqevas rfsklcylig qhgaslssfl hgvkearslv ilkhsslfld
      781 syteyctsit nflvmggfql lakpaidfln knqellqdls evndentqlm eilntlfflp
      841 irrlhnyakv llklatcfev aspeyqklqd ssscyeclal hlgrkrkeae ytlgfwktfp
      901 gkmtdslrkp errllcessn ralslqhagr fsvnwfilfn dalvhaqfst hhvfplatlw
      961 aeplseeagg vnglkittpe eqftlisstp qektkwlrai sqavdqalrg msdlppygsg
     1021 ssvqrqeppi srsakytfyk dprlkdatyd grwlsgkphg rgvlkwpdgk mysgmfrngl
     1081 edgygeyrip nkamnkedhy vghwkegkmc gqgvysyasg evfegcfqdn mrhghgllrs
     1141 gkltssspsm figqwvmdkk agygvfddit rgekymgmwq ddvcqgngvv vtqfglyyeg
     1201 nfhlnkmmgn gvllseddti yegefsddwt lsgkgtltmp ngdyiegyfs gewgsgikit
     1261 gtyfkpslye sdkdrpkvlk lgnlavpade kwkavfdecw rqlgcegpgq gevwkawdni
     1321 avalttsrrq hrdspeilsr sqtqtlesle fipqhvgafs vekyddirky likacdtplh
     1381 plgrlvetlv avyrmtyvgv ganrrllqea vkeiksylkr ifqlvrflfp elpeegstip
     1441 lsaplpterk sfctgksdsr sespepgyvv tssglllpvl lprlypplfm lyaldndree
     1501 diywecvlrl nkqpdiallg flgvqrkfwp atlsilgesk kvlpttkdac fasaveclqq
     1561 isttftpsdk lkviqqtfee isqsvlaslh edflwsmddl fpvflyvvlr arirnlgsev
     1621 hliedlmdpy lqhgeqgimf ttlkacyyqi qrekln
//
LOCUS       NP_001400610             284 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 14 precursor [Homo sapiens].
ACCESSION   NP_001400610
VERSION     NP_001400610.1
DBSOURCE    REFSEQ: accession NM_001413681.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 284)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC100850.2.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.572097.1,
                                           DRR138508.7112.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..284
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 14 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=28219
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..>264
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     CDS             1..284
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413681.1:169..1023"
                     /note="isoform 14 precursor is encoded by transcript
                     variant 17"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvglll wprlefsgvi tayf
//
LOCUS       NP_001401236             433 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 3 isoform 7
            precursor [Homo sapiens].
ACCESSION   NP_001401236
VERSION     NP_001401236.1
DBSOURCE    REFSEQ: accession NM_001414307.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Tang,Q., Yuan,Y., Li,L., Xu,Y., Ji,W., Xiao,S., Han,Y., Miao,W.,
            Cai,J., You,P., Chen,M., Ding,S., Li,Z., Qi,Z., Hou,W. and Luo,H.
  TITLE     Comprehensive analysis reveals that LTBR is a immune-related
            biomarker for glioma
  JOURNAL   Comput Biol Med 174, 108457 (2024)
   PUBMED   38599071
  REMARK    GeneRIF: Comprehensive analysis reveals that LTBR is a
            immune-related biomarker for glioma.
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Wu,Y., Zhao,S., Guo,W., Liu,Y., Requena Mullor,M.D.M.,
            Rodriguez,R.A. and Wei,R.
  TITLE     Systematic analysis of the prognostic value and immunological
            function of LTBR in human cancer
  JOURNAL   Aging (Albany NY) 16 (1), 129-152 (2024)
   PUBMED   38175686
  REMARK    GeneRIF: Systematic analysis of the prognostic value and
            immunological function of LTBR in human cancer.
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Shuptrine,C.W., Perez,V.M., Selitsky,S.R., Schreiber,T.H. and
            Fromm,G.
  TITLE     Shining a LIGHT on myeloid cell targeted immunotherapy
  JOURNAL   Eur J Cancer 187, 147-160 (2023)
   PUBMED   37167762
  REMARK    Review article
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Abudukeyoumu,A., Lai,Z.Z., Lu,J.J., Zhang,X., Hou,D.Y., Dong,J.,
            Wu,J.N., Li,M.Q. and Xie,F.
  TITLE     A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion
  JOURNAL   J Reprod Immunol 153, 103693 (2022)
   PUBMED   35987137
  REMARK    GeneRIF: A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion.
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Remouchamps,C., Boutaffala,L., Ganeff,C. and Dejardin,E.
  TITLE     Biology and signal transduction pathways of the
            Lymphotoxin-alphabeta/LTbetaR system
  JOURNAL   Cytokine Growth Factor Rev 22 (5-6), 301-310 (2011)
   PUBMED   22152226
  REMARK    Review article
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Nakano,H., Oshima,H., Chung,W., Williams-Abbott,L., Ware,C.F.,
            Yagita,H. and Okumura,K.
  TITLE     TRAF5, an activator of NF-kappaB and putative signal transducer for
            the lymphotoxin-beta receptor
  JOURNAL   J Biol Chem 271 (25), 14661-14664 (1996)
   PUBMED   8663299
REFERENCE   7  (residues 1 to 433)
  AUTHORS   Browning,J.L., Miatkowski,K., Sizing,I., Griffiths,D., Zafari,M.,
            Benjamin,C.D., Meier,W. and Mackay,F.
  TITLE     Signaling through the lymphotoxin beta receptor induces the death
            of some adenocarcinoma tumor lines
  JOURNAL   J Exp Med 183 (3), 867-878 (1996)
   PUBMED   8642291
REFERENCE   8  (residues 1 to 433)
  AUTHORS   Baens,M., Aerssens,J., van Zand,K., Van den Berghe,H. and
            Marynen,P.
  TITLE     Isolation and regional assignment of human chromosome 12p cDNAs
  JOURNAL   Genomics 29 (1), 44-52 (1995)
   PUBMED   8530100
REFERENCE   9  (residues 1 to 433)
  AUTHORS   Crowe,P.D., VanArsdale,T.L., Walter,B.N., Ware,C.F., Hession,C.,
            Ehrenfels,B., Browning,J.L., Din,W.S., Goodwin,R.G. and Smith,C.A.
  TITLE     A lymphotoxin-beta-specific receptor
  JOURNAL   Science 264 (5159), 707-710 (1994)
   PUBMED   8171323
REFERENCE   10 (residues 1 to 433)
  AUTHORS   Baens,M., Chaffanet,M., Cassiman,J.J., van den Berghe,H. and
            Marynen,P.
  TITLE     Construction and evaluation of a hncDNA library of human 12p
            transcribed sequences derived from a somatic cell hybrid
  JOURNAL   Genomics 16 (1), 214-218 (1993)
   PUBMED   8486360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005840.2.
            
            Summary: This gene encodes a member of the tumor necrosis factor
            receptor superfamily. The major ligands of this receptor include
            lymphotoxin alpha/beta and tumor necrosis factor ligand superfamily
            member 14. The encoded protein plays a role in signalling during
            the development of lymphoid and other organs, lipid metabolism,
            immune response, and programmed cell death. Activity of this
            receptor has also been linked to carcinogenesis. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR12921934.828590.1,
                                           DRR138522.1292249.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..433
                     /product="tumor necrosis factor receptor superfamily
                     member 3 isoform 7 precursor"
                     /note="tumor necrosis factor C receptor; lymphotoxin B
                     receptor; tumor necrosis factor receptor type III;
                     lymphotoxin beta receptor (TNFR superfamily, member 3);
                     tumor necrosis factor receptor 2-related protein"
                     /calculated_mol_wt=43340
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3049
     Region          11..168
                     /region_name="TNFRSF3"
                     /note="Tumor necrosis factor receptor superfamily member 3
                     (TNFRSF3), also known as lymphotoxin beta receptor (LTBR);
                     cd10578"
                     /db_xref="CDD:276904"
     Region          22..80
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276904"
     Region          83..124
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276904"
     Region          126..167
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276904"
     Region          148..>210
                     /region_name="TNFRSF"
                     /note="Tumor necrosis factor receptor superfamily
                     (TNFRSF); cl22855"
                     /db_xref="CDD:473981"
     Region          170..210
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276924"
     CDS             1..433
                     /gene="LTBR"
                     /gene_synonym="D12S370; LT-BETA-R; TNF-R-III; TNFCR;
                     TNFR-RP; TNFR2-RP; TNFR3; TNFRSF3"
                     /coded_by="NM_001414307.1:198..1499"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:4055"
                     /db_xref="HGNC:HGNC:6718"
                     /db_xref="MIM:600979"
ORIGIN      
        1 mllpwatsap glawgplvlg lfgllaasqp qavppyasen qtcrdqekey yepqhriccs
       61 rcppgtyvsa kcsrirdtvc atcaensyne hwnylticql crpcdpvmgl eeiapctskr
      121 ktqcrcqpgm fcaawalect hcellsdcpp gteaelkdev gkgnnhcvpc kaghfqntss
      181 psarcqphtr cenqglveaa pgtaqsdttc knpleplppe msgtmlmlav llplafflll
      241 atvfsciwks hpslcrklgr kgldagegpn pvagsweppk ahpyfpdlvq pllpisgdvs
      301 pvstglpaap vleagvpqqq spldltrepq lepgeqsqva hgtngihvtg gsmtitgniy
      361 iyngpvlggp pgpgdlpatp eppypipeeg dpgppglstp hqedgkawhl aetehcgatp
      421 snrgprnqfi thd
//
LOCUS       NP_001427362             756 aa            linear   PRI 21-NOV-2025
DEFINITION  lipopolysaccharide-responsive and beige-like anchor protein isoform
            7 [Homo sapiens].
ACCESSION   NP_001427362 XP_016864363 XP_054207317
VERSION     NP_001427362.1
DBSOURCE    REFSEQ: accession NM_001440433.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Szentgyorgyi,V., Lueck,L.M., Overwijn,D., Ritz,D., Zoeller,N.,
            Schmidt,A., Hondele,M., Spang,A. and Bakhtiar,S.
  TITLE     Arf1-dependent LRBA recruitment to Rab4 endosomes is required for
            endolysosome homeostasis
  JOURNAL   J Cell Biol 223 (11) (2024)
   PUBMED   39325073
  REMARK    GeneRIF: Arf1-dependent LRBA recruitment to Rab4 endosomes is
            required for endolysosome homeostasis.
REFERENCE   3  (residues 1 to 756)
  AUTHORS   Freund,T., Baxter,S.K., Walsh,T., Golan,H., Kapelushnik,J.,
            Abramsohn-Goldenberg,M., Benor,S., Sarid,N., Ram,R., Alcalay,Y.,
            Segel,R., Renbaum,P., Stepensky,P., King,M.C., Torgerson,T.R. and
            Hagin,D.
  TITLE     Clinically Complex LRBA Deficiency Due to a Founder Allele in the
            Georgian Jewish Population
  JOURNAL   J Clin Immunol 43 (1), 151-164 (2023)
   PUBMED   36063261
  REMARK    GeneRIF: Clinically Complex LRBA Deficiency Due to a Founder Allele
            in the Georgian Jewish Population.
REFERENCE   4  (residues 1 to 756)
  AUTHORS   Catak,M.C., Akcam,B., Bilgic Eltan,S., Babayeva,R., Karakus,I.S.,
            Akgun,G., Baser,D., Bulutoglu,A., Bayram,F., Kasap,N., Kiykim,A.,
            Hancioglu,G., Kokcu Karadag,S.I., Kendir Demirkol,Y., Ozen,S.,
            Cekic,S., Ozcan,D., Edeer Karaca,N., Sasihuseyinoglu,A.S.,
            Cansever,M., Ozek Yucel,E., Tamay,Z., Altintas,D.U., Aydogmus,C.,
            Celmeli,F., Cokugras,H., Gulez,N., Genel,F., Metin,A., Guner,S.N.,
            Kutukculer,N., Keles,S., Reisli,I., Kilic,S.S., Yildiran,A.,
            Karakoc-Aydiner,E., Lo,B., Ozen,A. and Baris,S.
  TITLE     Comparing the levels of CTLA-4-dependent biological defects in
            patients with LRBA deficiency and CTLA-4 insufficiency
  JOURNAL   Allergy 77 (10), 3108-3123 (2022)
   PUBMED   35491430
  REMARK    GeneRIF: Comparing the levels of CTLA-4-dependent biological
            defects in patients with LRBA deficiency and CTLA-4 insufficiency.
REFERENCE   5  (residues 1 to 756)
  AUTHORS   Yao,J., Gu,H., Mou,W., Chen,Z., Ma,J., Ma,H., Li,N., Zhang,R.,
            Wang,T., Jiang,J. and Wu,R.
  TITLE     Various phenotypes of LRBA gene with compound heterozygous
            variation: A case series report of pediatric cytopenia patients
  JOURNAL   Int J Immunopathol Pharmacol 36, 3946320221125591 (2022)
   PUBMED   36074705
  REMARK    GeneRIF: Various phenotypes of LRBA gene with compound heterozygous
            variation: A case series report of pediatric cytopenia patients.
REFERENCE   6  (residues 1 to 756)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 756)
  AUTHORS   Gebauer,D., Li,J., Jogl,G., Shen,Y., Myszka,D.G. and Tong,L.
  TITLE     Crystal structure of the PH-BEACH domains of human LRBA/BGL
  JOURNAL   Biochemistry 43 (47), 14873-14880 (2004)
   PUBMED   15554694
  REMARK    GeneRIF: The crystal structure of the aPH-BEACH domains of LRBA
            were studied.
REFERENCE   8  (residues 1 to 756)
  AUTHORS   Dyomin,V.G., Chaganti,S.R., Dyomina,K., Palanisamy,N., Murty,V.V.,
            Dalla-Favera,R. and Chaganti,R.S.
  TITLE     BCL8 is a novel, evolutionarily conserved human gene family
            encoding proteins with presumptive protein kinase A anchoring
            function
  JOURNAL   Genomics 80 (2), 158-165 (2002)
   PUBMED   12160729
REFERENCE   9  (residues 1 to 756)
  AUTHORS   Wang,J.W., Howson,J., Haller,E. and Kerr,W.G.
  TITLE     Identification of a novel lipopolysaccharide-inducible gene with
            key features of both A kinase anchor proteins and chs1/beige
            proteins
  JOURNAL   J Immunol 166 (7), 4586-4595 (2001)
   PUBMED   11254716
REFERENCE   10 (residues 1 to 756)
  AUTHORS   Feuchter,A.E., Freeman,J.D. and Mager,D.L.
  TITLE     Strategy for detecting cellular transcripts promoted by human
            endogenous long terminal repeats: identification of a novel gene
            (CDC4L) with homology to yeast CDC4
  JOURNAL   Genomics 13 (4), 1237-1246 (1992)
   PUBMED   1505956
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC110813.4, AC097373.3,
            AC092612.3 and AC093748.3.
            
            On or before May 20, 2025 this sequence version replaced
            XP_016864363.1, XP_054207317.1.
            
            Summary: The protein encoded by this gene is a member of the
            WDL-BEACH-WD (WBW) gene family. Its expression is induced in B
            cells and macrophages by bacterial lipopolysaccharides (LPS). The
            encoded protein associates with protein kinase A and may be
            involved in leading intracellular vesicles to activated receptor
            complexes, which aids in the secretion and/or membrane deposition
            of immune effector molecules. Defects in this gene are associated
            with the disorder common variable immunodeficiency-8 with
            autoimmunity. Two transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Dec 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.3095028.1,
                                           SRR14372079.615876.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.3"
     Protein         1..756
                     /product="lipopolysaccharide-responsive and beige-like
                     anchor protein isoform 7"
                     /note="vesicle trafficking, beach and anchor containing;
                     lipopolysaccharide-responsive and beige-like anchor
                     protein; CDC4-like protein; LPS-responsive vesicle
                     trafficking, beach and anchor containing"
                     /calculated_mol_wt=85496
     Region          <11..69
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          101..377
                     /region_name="Beach"
                     /note="Beige/BEACH domain; pfam02138"
                     /db_xref="CDD:460459"
     Region          477..741
                     /region_name="NBCH_WD40"
                     /note="Neurobeachin beta propeller domain; pfam20426"
                     /db_xref="CDD:466575"
     Region          493..529
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          535..588
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          593..628
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          633..662
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          675..709
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..756
                     /gene="LRBA"
                     /gene_synonym="BGL; CDC4L; CVID8; LAB300; LBA; uc.147"
                     /coded_by="NM_001440433.1:42..2312"
                     /note="isoform 7 is encoded by transcript variant 8"
                     /db_xref="GeneID:987"
                     /db_xref="HGNC:HGNC:1742"
                     /db_xref="MIM:606453"
ORIGIN      
        1 marpatlpri layteglhgk wlfteirsif srryllqnta leifmanrva vmfnfpdpat
       61 vkkvvnylpr vgvgtsfglp qtrrislasp rqlfkasnmt qrwqhreisn feylmflnti
      121 agrsyndlnq ypvfpwvitn yeseeldltl ptnfrdlskp igalnpkraa ffaeryeswe
      181 ddqvpkfhyg thystasfvl awllriepft tyflnlqggk fdhadrtfss israwrnsqr
      241 dtsdikelip efyylpemfv nfnnynlgvm ddgtvvsdve lppwaktsee fvhinrlale
      301 sefvscqlhq widlifgykq qgpeavraln vfyyltyega vnlnsitdpv lreaveaqir
      361 sfgqtpsqll iephpprgsa mqvylllqsp lmftdkaqqd vimvlkfpsn spvthvaant
      421 qpglatpavi tvtanrlfav nkwhnlpahq gavqdqpyql pveidplias ntgmhrrqit
      481 dlldqsiqvh sqcfvitsdn ryilvcgfwd ksfrvystdt grliqvvfgh wdvvtclars
      541 esyiggncyi lsgsrdatll lwywngkcsg igdnpgseta aprailtghd yevtcaavca
      601 elglvlsgsq egpclihsmn gdllrtlegp enclkpkliq asreghcvif yenglfctfs
      661 vngklqatme tddniraiql srdgqylltg gdrgvvvvrq vsdlkqlfay pgcdagiram
      721 alsydqrcii sgmasgsivl fyndfnrwhh eyqtry
//
LOCUS       NP_001425897             727 aa            linear   PRI 21-NOV-2025
DEFINITION  transcriptional repressor CTCF isoform 1 [Homo sapiens].
ACCESSION   NP_001425897 XP_016878357 XP_054235373
VERSION     NP_001425897.1
DBSOURCE    REFSEQ: accession NM_001438968.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Ma,D.B., Zhang,H., Wang,X.L. and Wu,Q.G.
  TITLE     METTL3 aggravates cell damage induced by Streptococcus pneumoniae
            via the NEAT1/CTCF/MUC19 axis
  JOURNAL   Kaohsiung J Med Sci 40 (8), 722-731 (2024)
   PUBMED   38757482
  REMARK    GeneRIF: METTL3 aggravates cell damage induced by Streptococcus
            pneumoniae via the NEAT1/CTCF/MUC19 axis.
REFERENCE   3  (residues 1 to 727)
  AUTHORS   Zhang,J., Hu,G., Lu,Y., Ren,H., Huang,Y., Wen,Y., Ji,B., Wang,D.,
            Wang,H., Liu,H., Ma,N., Zhang,L., Pan,G., Qu,Y., Wang,H., Zhang,W.,
            Miao,Z. and Yao,H.
  TITLE     CTCF mutation at R567 causes developmental disorders via 3D genome
            rearrangement and abnormal neurodevelopment
  JOURNAL   Nat Commun 15 (1), 5524 (2024)
   PUBMED   38951485
  REMARK    GeneRIF: CTCF mutation at R567 causes developmental disorders via
            3D genome rearrangement and abnormal neurodevelopment.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 727)
  AUTHORS   Pandey,A., Kakani,P. and Shukla,S.
  TITLE     CTCF and BORIS-mediated autophagy regulation via alternative
            splicing of BNIP3L in breast cancer
  JOURNAL   J Biol Chem 300 (7), 107416 (2024)
   PUBMED   38810696
  REMARK    GeneRIF: CTCF and BORIS-mediated autophagy regulation via
            alternative splicing of BNIP3L in breast cancer.
REFERENCE   5  (residues 1 to 727)
  AUTHORS   He,T., You,M., Zhu,H., Chen,P. and Fang,S.
  TITLE     CCCTC-binding factor suppresses alpha-2-macroglobulin transcription
            to improve vascular endothelial cell functions in lower extremity
            arteriosclerosis obliterans
  JOURNAL   Gen Physiol Biophys 43 (3), 231-242 (2024)
   PUBMED   38774923
  REMARK    GeneRIF: CCCTC-binding factor suppresses alpha-2-macroglobulin
            transcription to improve vascular endothelial cell functions in
            lower extremity arteriosclerosis obliterans.
REFERENCE   6  (residues 1 to 727)
  AUTHORS   Bell,A.C., West,A.G. and Felsenfeld,G.
  TITLE     The protein CTCF is required for the enhancer blocking activity of
            vertebrate insulators
  JOURNAL   Cell 98 (3), 387-396 (1999)
   PUBMED   10458613
REFERENCE   7  (residues 1 to 727)
  AUTHORS   Filippova,G.N., Lindblom,A., Meincke,L.J., Klenova,E.M.,
            Neiman,P.E., Collins,S.J., Doggett,N.A. and Lobanenkov,V.V.
  TITLE     A widely expressed transcription factor with multiple DNA sequence
            specificity, CTCF, is localized at chromosome segment 16q22.1
            within one of the smallest regions of overlap for common deletions
            in breast and prostate cancers
  JOURNAL   Genes Chromosomes Cancer 22 (1), 26-36 (1998)
   PUBMED   9591631
REFERENCE   8  (residues 1 to 727)
  AUTHORS   Vostrov,A.A. and Quitschke,W.W.
  TITLE     The zinc finger protein CTCF binds to the APBbeta domain of the
            amyloid beta-protein precursor promoter. Evidence for a role in
            transcriptional activation
  JOURNAL   J Biol Chem 272 (52), 33353-33359 (1997)
   PUBMED   9407128
REFERENCE   9  (residues 1 to 727)
  AUTHORS   Filippova,G.N., Fagerlie,S., Klenova,E.M., Myers,C., Dehner,Y.,
            Goodwin,G., Neiman,P.E., Collins,S.J. and Lobanenkov,V.V.
  TITLE     An exceptionally conserved transcriptional repressor, CTCF, employs
            different combinations of zinc fingers to bind diverged promoter
            sequences of avian and mammalian c-myc oncogenes
  JOURNAL   Mol Cell Biol 16 (6), 2802-2813 (1996)
   PUBMED   8649389
REFERENCE   10 (residues 1 to 727)
  AUTHORS   Valverde de Morales,H.G., Wang,H.L., Garber,K., Corces,V. and Li,H.
  TITLE     CTCF-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   38662876
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027682.10 and AC009095.7.
            
            On or before Apr 25, 2025 this sequence version replaced
            XP_016878357.1, XP_054235373.1.
            
            Summary: This gene is a member of the BORIS + CTCF gene family and
            encodes a transcriptional regulator protein with 11 highly
            conserved zinc finger (ZF) domains. This nuclear protein is able to
            use different combinations of the ZF domains to bind different DNA
            target sequences and proteins. Depending upon the context of the
            site, the protein can bind a histone acetyltransferase
            (HAT)-containing complex and function as a transcriptional
            activator or bind a histone deacetylase (HDAC)-containing complex
            and function as a transcriptional repressor. If the protein is
            bound to a transcriptional insulator element, it can block
            communication between enhancers and upstream promoters, thereby
            regulating imprinted expression. Mutations in this gene have been
            associated with invasive breast cancers, prostate cancers, and
            Wilms' tumors. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4089831.1,
                                           SRR1803616.237792.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2149876
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..727
                     /product="transcriptional repressor CTCF isoform 1"
                     /note="transcriptional repressor CTCF; CTCFL paralog;
                     11-zinc finger protein; 11 zinc finger transcriptional
                     repressor; CCCTC-binding factor (zinc finger protein)"
                     /calculated_mol_wt=82655
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P49711.1)"
     Region          180..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49711.1)"
     Region          266..289
                     /region_name="zf-H2C2_5"
                     /note="C2H2-type zinc-finger domain; pfam13909"
                     /db_xref="CDD:404746"
     Region          268..288
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(273,275,277,279..280,283..284,287,301,303,307..308,
                     311..312,315,329,331,333,335..336,339..340,346)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          280..305
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P49711.1)"
     Region          296..316
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          309..333
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P49711.1)"
     Region          324..347
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          351..375
                     /region_name="zf-H2C2_5"
                     /note="C2H2-type zinc-finger domain; pfam13909"
                     /db_xref="CDD:404746"
     Region          353..373
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <366..500
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P49711.1)"
     Region          381..401
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P49711.1)"
     Region          409..426
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          439..457
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          469..489
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(474,476,478,480..481,484..485,488,502,504,508..509,
                     512..513,516,530,532,534,536..537,540..541,545)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          497..517
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          509..534
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          525..546
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          557..573
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          573..677
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49711.1)"
     Site            609
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P49711.1)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P49711.1)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P49711.1)"
     Region          689..717
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49711.1)"
     CDS             1..727
                     /gene="CTCF"
                     /gene_synonym="CFAP108; FAP108; MRD21"
                     /coded_by="NM_001438968.1:205..2388"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:10664"
                     /db_xref="HGNC:HGNC:13723"
                     /db_xref="MIM:604167"
ORIGIN      
        1 megdaveaiv eesetfikgk erktyqrrre ggqeedachl pqnqtdggev vqdvnssvqm
       61 vmmeqldptl lqmktevmeg tvapeaeaav ddtqiitlqv vnmeeqpini gelqlvqvpv
      121 pvtvpvatts veelqgayen evskeglaes epmichtlpl pegfqvvkvg angevetleq
      181 gelppqedps wqkdpdyqpp akktkktkks klryteegkd vdvsvydfee eqqegllsev
      241 naekvvgnmk ppkptkikkk gvkktfqcel csytcprrsn ldrhmkshtd erphkchlcg
      301 rafrtvtllr nhlnthtgtr phkcpdcdma fvtsgelvrh rrykhthekp fkcsmcdyas
      361 vevsklkrhi rshtgerpfq cslcsyasrd tyklkrhmrt hsgekpyecy icharftqsg
      421 tmkmhilqkh tenvakfhcp hcdtviarks dlgvhlrkqh syieqgkkcr ycdavfhery
      481 aliqhqkshk nekrfkcdqc dyacrqerhm imhkrthtge kpyacshcdk tfrqkqlldm
      541 hfkryhdpnf vpaafvcskc gktftrrntm arhadncagp dgvegengge tkkskrgrkr
      601 kmrskkedss dsenaepdld dnedeeepav eiepepepqp vtpapppakk rrgrppgrtn
      661 qpkqnqptai iqvedqntga ieniivevkk epdaepaege eeeaqpaatd apngdltpem
      721 ilsmmdr
//
LOCUS       NP_001394378            2861 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform c [Homo sapiens].
ACCESSION   NP_001394378
VERSION     NP_001394378.1
DBSOURCE    REFSEQ: accession NM_001407449.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2861)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2861)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2861)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2861)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2861)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2861)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2861)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2861)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2861)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2861)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2174587.1,
                                           SRR18074969.3772534.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2861
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2861
                     /product="adenomatous polyposis coli protein isoform c"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=313343
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Region          <8..272
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          239..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          340..392
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          393..466
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          490..526
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          523..565
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          530..571
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          534..571
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          566..609
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          581..613
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(604,608,612,651,655,659,696,700,704)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          610..656
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          621..662
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          657..701
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          667..707
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          671..705
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          702..743
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          709..749
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          713..749
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          744..785
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          750..1037
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Site            762
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            798
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          846..896
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            926
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          941..961
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          976..1005
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          978..1355
                     /region_name="Responsible for down-regulation through a
                     process mediated by direct ubiquitination"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1005
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1038..1187
                     /region_name="Interaction with catenins.
                     /evidence=ECO:0000269|PubMed:8259519"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1054..1153
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Site            1056
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1060
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1117..1187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1208..1262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1275..>1292
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1301..1386
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1309..1719
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1329..1394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1421..1493
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1456
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1544..1587
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1601..1629
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1655..1678
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1680..1733
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1682..1735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1734..1755
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1747..1854
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1764..1857
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Site            1792
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1879
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1881
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1882
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1884..1911
                     /region_name="Highly charged"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1891..1965
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1899..1968
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1983..2029
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1989
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1991
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2051..2070
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2053..2077
                     /region_name="Interaction with AXIN1.
                     /evidence=ECO:0000269|PubMed:10811618"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2061..2090
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2165..2653
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2169
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2185..2692
                     /region_name="Basic region.
                     /evidence=ECO:0000269|PubMed:17293347"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2241..2586
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Site            2278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2491
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2493..2861
                     /region_name="Interaction with DLG1.
                     /evidence=ECO:0000269|PubMed:8638125"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2553
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2587
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2685..2732
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2688..2861
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     Site            2689
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2692..2861
                     /region_name="Interaction with MAPRE1.
                     /evidence=ECO:0000269|PubMed:17293347"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2697
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2728
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2742
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2747..2861
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2807
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2821..2824
                     /region_name="Microtubule tip localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2859..2861
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     CDS             1..2861
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407449.1:168..8753"
                     /note="isoform c is encoded by transcript variant 19"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrriar iqqiekdilr irqllqsqat
      241 eaerssqnkh etgshdaerq negqgvgein matsgngqgs ttrmdhetas vlssssthsa
      301 prrltshlgt kvemvyslls mlgthdkddm srtllamsss qdscismrqs gclplliqll
      361 hgndkdsvll gnsrgskear arasaalhni ihsqpddkrg rreirvlhll eqiraycetc
      421 wewqeahepg mdqdknpmpa pvehqicpav cvlmklsfde ehrhamnelg rkatrgissq
      481 elgqglsggl qaiaellqvd cemygltndh ysitlrryag maltnltfgd vankatlcsm
      541 kgcmralvaq lksesedlqq viasvlrnls wradvnskkt lrevgsvkal mecalevkke
      601 stlksvlsal wnlsahcten kadicavdga laflvgtlty rsqtntlaii esgggilrnv
      661 ssliatnedh rqilrenncl qtllqhlksh sltivsnacg tlwnlsarnp kdqealwdmg
      721 avsmlknlih skhkmiamgs aaalrnlman rpakykdani mspgsslpsl hvrkqkalea
      781 eldaqhlset fdnidnlspk ashrskqrhk qslygdyvfd tnrhddnrsd nfntgnmtvl
      841 spylnttvlp sssssrgsld ssrsekdrsl erergiglgn yhpatenpgt sskrglqist
      901 taaqiakvme evsaihtsqe drssgsttel hcvtdernal rrssaahths ntynftksen
      961 snrtcsmpya kleykrssnd slnsvsssdg ygkrgqmkps iesyseddes kfcsygqypa
     1021 dlahkihsan hmddndgeld tpinyslkys deqlnsgrqs psqnerwarp khiiedeikq
     1081 seqrqsrnqs ttypvytest ddkhlkfqph fgqqecvspy rsrgangset nrvgsnhgin
     1141 qnvsqslcqe ddyeddkptn yseryseeeq heeeerptny sikyneekrh vdqpidyslk
     1201 yatdipssqk qsfsfsksss gqssktehms sssentstps snakrqnqlh pssaqsrsgq
     1261 pqkaatckvs sinqetiqty cvedtpicfs rcsslsslss aedeigcnqt tqeadsantl
     1321 qiaeikekig trsaedpvse vpavsqhprt kssrlqgssl ssesarhkav efssgaksps
     1381 ksgaqtpksp pehyvqetpl mfsrctsvss ldsfesrsia ssvqsepcsg mvsgiispsd
     1441 lpdspgqtmp psrsktpppp pqtaqtkrev pknkaptaek resgpkqaav naavqrvqvl
     1501 pdadtllhfa testpdgfsc ssslsalsld epfiqkdvel rimppvqend ngneteseqp
     1561 kesnenqeke aektidsekd llddsddddi eileeciisa mptkssrkak kpaqtasklp
     1621 ppvarkpsql pvykllpsqn rlqpqkhvsf tpgddmprvy cvegtpinfs tatslsdlti
     1681 esppnelaag egvrggaqsg efekrdtipt egrstdeaqg gktssvtipe lddnkaeegd
     1741 ilaecinsam pkgkshkpfr vkkimdqvqq asasssapnk nqldgkkkkp tspvkpipqn
     1801 teyrtrvrkn adsknnlnae rvfsdnkdsk kqnlknnskv fndklpnned rvrgsfafds
     1861 phhytpiegt pycfsrndsl ssldfddddv dlsrekaelr kakenkesea kvtshtelts
     1921 nqqsanktqa iakqpinrgq pkpilqkqst fpqsskdipd rgaatdeklq nfaientpvc
     1981 fshnsslssl sdidqennnk enepiketep pdsqgepskp qasgyapksf hvedtpvcfs
     2041 rnsslsslsi dseddllqec issampkkkk psrlkgdnek hsprnmggil gedltldlkd
     2101 iqrpdsehgl spdsenfdwk aiqegansiv sslhqaaaaa clsrqassds dsilslksgi
     2161 slgspfhltp dqeekpftsn kgprilkpge kstletkkie seskgikggk kvykslitgk
     2221 vrsnseisgq mkqplqanmp sisrgrtmih ipgvrnssss tspvskkgpp lktpasksps
     2281 egqtattspr gakpsvksel spvarqtsqi ggsskapsrs gsrdstpsrp aqqplsrpiq
     2341 spgrnsispg rngisppnkl sqlprtssps tastkssgsg kmsytspgrq msqqnltkqt
     2401 glsknassip rsesaskgln qmnngngank kvelsrmsst kssgsesdrs erpvlvrqst
     2461 fikeapsptl rrkleesasf eslspssrpa sptrsqaqtp vlspslpdms lsthssvqag
     2521 gwrklppnls ptieyndgrp akrhdiarsh sespsrlpin rsgtwkrehs khssslprvs
     2581 twrrtgssss ilsassesse kaksedekhv nsisgtkqsk enqvsakgtw rkikenefsp
     2641 tnstsqtvss gatngaeskt liyqmapavs ktedvwvrie dcpinnprsg rsptgntppv
     2701 idsvsekanp nikdskdnqa kqnvgngsvp mrtvglenrl nsfiqvdapd qkgteikpgq
     2761 nnpvpvsetn essivertpf sssssskhss psgtvaarvt pfnynpsprk ssadstsarp
     2821 sqiptpvnnn tkkrdsktds tessgtqspk rhsgsylvts v
//
LOCUS       NP_001276953             702 aa            linear   PRI 21-NOV-2025
DEFINITION  interleukin-12 receptor subunit beta-1 isoform 4 [Homo sapiens].
ACCESSION   NP_001276953
VERSION     NP_001276953.1
DBSOURCE    REFSEQ: accession NM_001290024.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Chen,H., Ge,X., Li,C., Zeng,J. and Wang,X.
  TITLE     Structure and assembly of the human IL-12 signaling complex
  JOURNAL   Structure 32 (10), 1640-1651 (2024)
   PUBMED   39111304
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Huang,J., He,Q., Huang,L., Liu,L., Yang,P. and Chen,M.
  TITLE     Discovering the link between IL12RB1 gene polymorphisms and
            tuberculosis susceptibility: a comprehensive meta-analysis
  JOURNAL   Front Public Health 12, 1249880 (2024)
   PUBMED   38317798
  REMARK    GeneRIF: Discovering the link between IL12RB1 gene polymorphisms
            and tuberculosis susceptibility: a comprehensive meta-analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 702)
  AUTHORS   Rosas Mejia,O., Claeys,T.A., Williams,A., Zafar,A. and
            Robinson,R.T.
  TITLE     IL12RB1 allele bias in human TH cells is regulated by functional
            SNPs in its 3'UTR
  JOURNAL   Cytokine 158, 155993 (2022)
   PUBMED   36007427
  REMARK    GeneRIF: IL12RB1 allele bias in human TH cells is regulated by
            functional SNPs in its 3'UTR.
REFERENCE   4  (residues 1 to 702)
  AUTHORS   Khattak,F.A., Akbar,N.U., Riaz,M., Hussain,M., Rehman,K., Khan,S.N.
            and Khan,T.A.
  TITLE     Novel IL-12Rbeta1 deficiency-mediates recurrent cutaneous
            leishmaniasis
  JOURNAL   Int J Infect Dis 112, 338-345 (2021)
   PUBMED   34438084
  REMARK    GeneRIF: Novel IL-12Rbeta1 deficiency-mediates recurrent cutaneous
            leishmaniasis.
REFERENCE   5  (residues 1 to 702)
  AUTHORS   Yamamoto,K., Kobayashi,H., Miura,O., Hirosawa,S. and Miyasaka,N.
  TITLE     Assignment of IL12RB1 and IL12RB2, interleukin-12 receptor beta 1
            and beta 2 chains, to human chromosome 19 band p13.1 and chromosome
            1 band p31.2, respectively, by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 77 (3-4), 257-258 (1997)
   PUBMED   9284929
REFERENCE   6  (residues 1 to 702)
  AUTHORS   Bacon,C.M., Petricoin,E.F. 3rd, Ortaldo,J.R., Rees,R.C.,
            Larner,A.C., Johnston,J.A. and O'Shea,J.J.
  TITLE     Interleukin 12 induces tyrosine phosphorylation and activation of
            STAT4 in human lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 92 (16), 7307-7311 (1995)
   PUBMED   7638186
REFERENCE   7  (residues 1 to 702)
  AUTHORS   Bacon,C.M., McVicar,D.W., Ortaldo,J.R., Rees,R.C., O'Shea,J.J. and
            Johnston,J.A.
  TITLE     Interleukin 12 (IL-12) induces tyrosine phosphorylation of JAK2 and
            TYK2: differential use of Janus family tyrosine kinases by IL-2 and
            IL-12
  JOURNAL   J Exp Med 181 (1), 399-404 (1995)
   PUBMED   7528775
REFERENCE   8  (residues 1 to 702)
  AUTHORS   Ling,P., Gately,M.K., Gubler,U., Stern,A.S., Lin,P., Hollfelder,K.,
            Su,C., Pan,Y.C. and Hakimi,J.
  TITLE     Human IL-12 p40 homodimer binds to the IL-12 receptor but does not
            mediate biologic activity
  JOURNAL   J Immunol 154 (1), 116-127 (1995)
   PUBMED   7527811
REFERENCE   9  (residues 1 to 702)
  AUTHORS   Gillessen,S., Carvajal,D., Ling,P., Podlaski,F.J., Stremlo,D.L.,
            Familletti,P.C., Gubler,U., Presky,D.H., Stern,A.S. and Gately,M.K.
  TITLE     Mouse interleukin-12 (IL-12) p40 homodimer: a potent IL-12
            antagonist
  JOURNAL   Eur J Immunol 25 (1), 200-206 (1995)
   PUBMED   7843232
REFERENCE   10 (residues 1 to 702)
  AUTHORS   Chua,A.O., Chizzonite,R., Desai,B.B., Truitt,T.P., Nunes,P.,
            Minetti,L.J., Warrier,R.R., Presky,D.H., Levine,J.F., Gately,M.K.
            et al.
  TITLE     Expression cloning of a human IL-12 receptor component. A new
            member of the cytokine receptor superfamily with strong homology to
            gp130
  JOURNAL   J Immunol 153 (1), 128-136 (1994)
   PUBMED   7911493
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020904.7.
            
            Summary: The protein encoded by this gene is a type I transmembrane
            protein that belongs to the hemopoietin receptor superfamily. This
            protein binds to interleukine 12 (IL12) with a low affinity, and is
            thought to be a part of IL12 receptor complex. This protein forms a
            disulfide-linked oligomer, which is required for its IL12 binding
            activity. The coexpression of this and IL12RB2 proteins was shown
            to lead to the formation of high-affinity IL12 binding sites and
            reconstitution of IL12 dependent signaling. Mutations in this gene
            impair the development of interleukin-17-producing T lymphocytes
            and result in increased susceptibility to mycobacterial and
            Salmonella infections. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (4) encodes the longest isoform
            (4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647221.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..702
                     /product="interleukin-12 receptor subunit beta-1 isoform
                     4"
                     /note="IL-12 receptor beta component; interleukin-12
                     receptor beta-1 chain; IL-12R subunit beta-1; IL-12
                     receptor subunit beta-1; cluster of differentiation 212;
                     interleukin 12 receptor, beta 1"
                     /calculated_mol_wt=77346
     Region          487..577
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(568..569,571..572)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     CDS             1..702
                     /gene="IL12RB1"
                     /gene_synonym="CD212; IL-12R-BETA1; IL12RB; IMD30"
                     /coded_by="NM_001290024.2:163..2271"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:3594"
                     /db_xref="HGNC:HGNC:5971"
                     /db_xref="MIM:601604"
ORIGIN      
        1 mfvglfslls fnvfrsgdgv aeprrwqrgs pgavglyvdp meplvtwvvp llflfllsrq
       61 gaacrtsecc fqdppypdad sgsasgprdl rcyrissdry ecswqyegpt agvshflrcc
      121 lssgrccyfa agsatrlqfs dqagvsvlyt vtlwveswar nqtekspevt lqlynsvkye
      181 pplgdikvsk lagqlrmewe tpdnqvgaev qfrhrtpssp wklgdcgpqd ddtesclcpl
      241 emnvaqefql rrrqlgsqgs swskwsspvc vppenppqpq vrfsveqlgq dgrrrltlke
      301 qptqlelpeg cqglapgtev tyrlqlhmls cpckakatrt lhlgkmpyls gaaynvavis
      361 snqfgpglnq twhipadtht epvalnisvg tngttmywpa raqsmtycie wqpvgqdggl
      421 atcsltapqd pdpagmatys wsresgamgq ekcyyitifa sahpekltlw stvlstyhfg
      481 gnasaagtph hvsvknhsld svsvdwapsl lstcpgvlke yvvrcrdeds kqvsehpvqp
      541 tetqvtlsgl ragvaytvqv radtawlrgv wsqpqrfsie vqvsdwliff aslgsflsil
      601 lvgvlgylgl nraarhlcpp lptpcassai efpggketwq winpvdfqee aslqealvve
      661 mswdkgerte plektelpeg apelaldtel sledgdrcka km
//
LOCUS       NP_001393528            1163 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 3 [Homo sapiens].
ACCESSION   NP_001393528 XP_047279787
VERSION     NP_001393528.1
DBSOURCE    REFSEQ: accession NM_001406599.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1163)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1163)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1163)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1163)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1163)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1163)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1163)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1163)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1163)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1163)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            On May 18, 2022 this sequence version replaced XP_047279787.1.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3152682.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1163
                     /product="hamartin isoform 3"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=129565
     Region          7..718
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          402..786
                     /region_name="Mediates interaction with WDR45B.
                     /evidence=ECO:0000269|PubMed:28561066"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Region          438..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <707..>959
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1005..1084
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1099
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1130..1163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1163
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406599.1:437..3928"
                     /note="isoform 3 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS87703.1"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt ggkgtplgtp atspppaplc hsddyvhisl pqatvtpprk
      421 eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed siekdkeeaa
      481 isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv npeplhssld
      541 klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp trvgfgsgqp
      601 ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr liqqgadahs
      661 kelnklplps ksvdwthfgg sppsdeirtl rdqllllhnq llyerfkrqq halrnrrllr
      721 kvikaaalee hnaamkdqlk lqekdiqmwk vslqkeqary nqlqeqrdtm vtklhsqirq
      781 lqhdreefyn qsqelqtkle dcrnmiaelr ielkkannkv chtelllsqv sqklsnsesv
      841 qqqmeflnrq llvlgevnel yleqlqnkhs dttkevemmk aayrkelekn rshvlqqtqr
      901 ldtsqkrile leshlakkdh llleqkkyle dvklqargql qaaesryeaq kritqvfele
      961 ildlygrlek dgllkkleee kaeaaeaaee rldccndgcs dsmvghneea sghngetktp
     1021 rpssargssg srggggssss sselstpekp phqragpfss rwettmgeas asipttvgsl
     1081 pssksflgmk arelfrnkse sqcdedgmts slseslktel gkdlgveaki plnldgphps
     1141 pptpdsvgql himdynethh ehs
//
LOCUS       NP_001407090             798 aa            linear   PRI 21-NOV-2025
DEFINITION  protein enabled homolog isoform h [Homo sapiens].
ACCESSION   NP_001407090 XP_047280896 XP_054193585
VERSION     NP_001407090.1
DBSOURCE    REFSEQ: accession NM_001420161.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Yin,X., Wang,J., Shen,Z., Jia,Q., Bian,Y., Yang,Z., Liu,Y., Li,Y.
            and Zhang,H.
  TITLE     ENAH transcriptionally activated by YY1 promotes growth and
            invasion of laryngocarcinoma cells through PI3K/AKT signaling
  JOURNAL   Eur J Pharmacol 983, 176991 (2024)
   PUBMED   39265883
  REMARK    GeneRIF: ENAH transcriptionally activated by YY1 promotes growth
            and invasion of laryngocarcinoma cells through PI3K/AKT signaling.
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Cui,H., Liang,X., Zhu,Y., Elayah,S.A., Qi,H., Xie,L., Guo,Z.,
            Siya,F., Ming,Y., Yuxin,G., Tu,J. and Na,S.
  TITLE     Mena as a key enhancer factor of EMT to promote metastasis of human
            tongue squamous cell carcinoma
  JOURNAL   Oral Dis 30 (4), 2084-2096 (2024)
   PUBMED   37203597
  REMARK    GeneRIF: Mena as a key enhancer factor of EMT to promote metastasis
            of human tongue squamous cell carcinoma.
REFERENCE   4  (residues 1 to 798)
  AUTHORS   He,L., She,C., Jiang,S., Qi,Z., Deng,Z., Ji,L., Cui,Y. and Wu,J.
  TITLE     Mammalian enabled protein enhances tamoxifen sensitivity of the
            hormone receptor-positive breast cancer patients by suppressing the
            AKT signaling pathway
  JOURNAL   Biol Direct 19 (1), 21 (2024)
   PUBMED   38459605
  REMARK    GeneRIF: Mammalian enabled protein enhances tamoxifen sensitivity
            of the hormone receptor-positive breast cancer patients by
            suppressing the AKT signaling pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Liu,R., Miao,K., Gao,L. and He,L.
  TITLE     TRIM67 interacts with ENAH to regulate the apoptosis and autophagy
            of lung cancer cells
  JOURNAL   Gen Physiol Biophys 43 (2), 163-173 (2024)
   PUBMED   38477606
  REMARK    GeneRIF: TRIM67 interacts with ENAH to regulate the apoptosis and
            autophagy of lung cancer cells.
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Urbanelli,L., Massini,C., Emiliani,C., Orlacchio,A., Bernardi,G.
            and Orlacchio,A.
  TITLE     Characterization of human Enah gene
  JOURNAL   Biochim Biophys Acta 1759 (1-2), 99-107 (2006)
   PUBMED   16494957
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Mammoto,A., Sasaki,T., Asakura,T., Hotta,I., Imamura,H.,
            Takahashi,K., Matsuura,Y., Shirao,T. and Takai,Y.
  TITLE     Interactions of drebrin and gephyrin with profilin
  JOURNAL   Biochem Biophys Res Commun 243 (1), 86-89 (1998)
   PUBMED   9473484
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Ermekova,K.S., Zambrano,N., Linn,H., Minopoli,G., Gertler,F.,
            Russo,T. and Sudol,M.
  TITLE     The WW domain of neural protein FE65 interacts with proline-rich
            motifs in Mena, the mammalian homolog of Drosophila enabled
  JOURNAL   J Biol Chem 272 (52), 32869-32877 (1997)
   PUBMED   9407065
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Niebuhr,K., Ebel,F., Frank,R., Reinhard,M., Domann,E., Carl,U.D.,
            Walter,U., Gertler,F.B., Wehland,J. and Chakraborty,T.
  TITLE     A novel proline-rich motif present in ActA of Listeria
            monocytogenes and cytoskeletal proteins is the ligand for the EVH1
            domain, a protein module present in the Ena/VASP family
  JOURNAL   EMBO J 16 (17), 5433-5444 (1997)
   PUBMED   9312002
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Sazuka,T., Tomooka,Y., Kathju,S., Ikawa,Y., Noda,M. and Kumar,S.
  TITLE     Identification of a developmentally regulated gene in the mouse
            central nervous system which encodes a novel proline rich protein
  JOURNAL   Biochim Biophys Acta 1132 (3), 240-248 (1992)
   PUBMED   1420303
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL591380.21, AL356216.13 and
            AC092811.2.
            
            On or before Apr 27, 2023 this sequence version replaced
            XP_047280896.1, XP_054193585.1.
            
            Summary: This gene encodes a member of the enabled/
            vasodilator-stimulated phosphoprotein. Members of this gene family
            are involved in actin-based motility. This protein is involved in
            regulating the assembly of actin filaments and modulates cell
            adhesion and motility. Alternate splice variants of this gene have
            been correlated with tumor invasiveness in certain tissues and
            these variants may serve as prognostic markers. A pseudogene of
            this gene is found on chromosome 3. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853560.2952.1,
                                           SRR18074967.2266051.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.12"
     Protein         1..798
                     /product="protein enabled homolog isoform h"
                     /note="protein enabled homolog; Mena delta 11a"
                     /calculated_mol_wt=86747
     Region          5..112
                     /region_name="EVH1_Ena_VASP-like"
                     /note="Enabled/VASP family EVH1 domain; cd01207"
                     /db_xref="CDD:269918"
     Site            order(16,23,69,71,77,79,81)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269918"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N8S7.2)"
     Region          <329..564
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          613..639
                     /region_name="WH2_hVASP-like"
                     /note="Wiskott-Aldrich syndrome protein (WASP)-homology
                     domain 2 (WH2) of human Vasodilator-stimulated
                     phosphoprotein and related proteins; cd22185"
                     /db_xref="CDD:409225"
     Site            order(620..621,623..624,627,629..633)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409225"
     Region          629..632
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409225"
     Region          760..794
                     /region_name="VASP_tetra"
                     /note="VASP tetramerization domain; pfam08776"
                     /db_xref="CDD:462599"
     CDS             1..798
                     /gene="ENAH"
                     /gene_synonym="ENA; MENA; NDPP1"
                     /coded_by="NM_001420161.1:434..2830"
                     /note="isoform h is encoded by transcript variant 8"
                     /db_xref="GeneID:55740"
                     /db_xref="HGNC:HGNC:18271"
                     /db_xref="MIM:609061"
ORIGIN      
        1 mseqsicqar aavmvyddan kkwvpaggst gfsrvhiyhh tgnntfrvvg rkiqdhqvvi
       61 ncaipkglky nqatqtfhqw rdarqvygln fgskedanvf asammhalev lnsqetgptl
      121 prqnsqlpaq vqngpsqeel eiqrrqlqeq qrqkelerer lerermerer lererlerer
      181 lererleqeq lererqerer qerlerqerl erqerlerqe rldrerqerq ererlerler
      241 erqererqeq lereqlewer errissaaps sdsslynapl peysscqpps apppsyakvi
      301 sapvsdatpd yavvtalppt stpptpplrh satrfatslg safhpvlphy atvprplnkn
      361 srpsspvntp ssqppatkpc awstsnfspl ppsppimiss ppgkatgprp vlpvcvsspv
      421 pqmppsptap nglvdsvtyp vsppptsgpa apppppplps laslshcgsq aspppstpia
      481 stpsskpsvl pspsaaapas vetplnsvlg dssasepglq aasqpaetps qqgivlgpla
      541 pppppplppg paqasvalpp ppgppppppl pstgpppppp ppplpnqvpp ppppppappl
      601 pasgfflasm sednrpltgl aaaiagaklr kvsrmedtsf psggnaigvn sassktdtgr
      661 gngplplggs glmeemsall arrrriaekg stieteqked kgedsepvts kasststpep
      721 trkpwertnt mngskspvis rpkstplsqp sangvqtegl dydrlkqdil demrkeltkl
      781 keelidairq elsksnta
//
LOCUS       NP_001400681             817 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform m [Homo sapiens].
ACCESSION   NP_001400681
VERSION     NP_001400681.1
DBSOURCE    REFSEQ: accession NM_001413752.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 817)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 817)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 817)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 817)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 817)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 817)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2135167.1,
                                           SRR18074967.3754646.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..817
                     /product="polyhomeotic-like protein 1 isoform m"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=86571
     Region          641..748
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          748..816
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(766..767,801..802,805..806,809)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(777..781,783..784,787..788,792,797)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..817
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413752.1:368..2821"
                     /note="isoform m is encoded by transcript variant 16"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq asinlattsa aqlisrsqsv
      121 sspsattltq svllgnttsp plnqsqaqmy lrvnrtlgrn vplasqlilm pngavaavqq
      181 evpsaqspgv hadadqvqnl avrnqqasaq gpqmqgstqk aippgaspvs slsqassqal
      241 avaqassgat nqslnlsqag ggsgnsipgs mgpggggqah gglgqlpssg mgggscprkg
      301 tgvvqplpaa qtvtvsqgsq teaesaaakk aeadgsgqqn vgmnltrtat papsqtliss
      361 atytqiqphs liqqqqqihl qqkqvviqqq iaihhqqqfq hrqsqllhta thlqlaqqqq
      421 qqqqqqqqqq qpqattltap qppqgkpqtl avkrkadsee erddvstlgs mlpakaspva
      481 espkvmdeks slgekaesva nvnantpsse lvaltpapsv ppptlamvsr qmgdskppqa
      541 ivkpqilthi iegfviqega epfpvgcsql lkesekplqt glptgltenq sggplgvdsp
      601 saeldkkanl lkceycgkya paeqfrgskr fcsmtcakry nvscshqfrl krkkmkefqe
      661 anyarvrrrg prrsssdiar akiqgkchrg qedssrgsdn ssydealspt spgplsvrag
      721 hgerdlgnpn tapptpelhg inpvflssnp srwsveevye fiaslqgcqe iaeefrsqei
      781 dgqallllke ehlmsamnik lgpalkicak invlket
//
LOCUS       NP_001394192             354 aa            linear   PRI 21-NOV-2025
DEFINITION  cellular tumor antigen p53 isoform g [Homo sapiens].
ACCESSION   NP_001394192
VERSION     NP_001394192.1
DBSOURCE    REFSEQ: accession NM_001407263.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Mirgayazova,R., Khadiullina,R., Chasov,V., Mingaleeva,R.,
            Miftakhova,R., Rizvanov,A. and Bulatov,E.
  TITLE     Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an Option?
  JOURNAL   Genes (Basel) 11 (6), 704 (2020)
   PUBMED   32630614
  REMARK    GeneRIF: Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an
            Option?
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Flynt,E., Bisht,K., Sridharan,V., Ortiz,M., Towfic,F. and
            Thakurta,A.
  TITLE     Prognosis, Biology, and Targeting of TP53 Dysregulation in Multiple
            Myeloma
  JOURNAL   Cells 9 (2), 287 (2020)
   PUBMED   31991614
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Barnoud,T., Parris,J.L.D. and Murphy,M.E.
  TITLE     Common genetic variants in the TP53 pathway and their impact on
            cancer
  JOURNAL   J Mol Cell Biol 11 (7), 578-585 (2019)
   PUBMED   31152665
  REMARK    GeneRIF: Common genetic variants in the TP53 pathway and their
            impact on cancer.
            Review article
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Hu,W., Chen,S., Thorne,R.F. and Wu,M.
  TITLE     TP53, TP53 Target Genes (DRAM, TIGAR), and Autophagy
  JOURNAL   Adv Exp Med Biol 1206, 127-149 (2019)
   PUBMED   31776983
  REMARK    Review article
REFERENCE   5  (residues 1 to 354)
  AUTHORS   Baugh,E.H., Ke,H., Levine,A.J., Bonneau,R.A. and Chan,C.S.
  TITLE     Why are there hotspot mutations in the TP53 gene in human cancers?
  JOURNAL   Cell Death Differ 25 (1), 154-160 (2018)
   PUBMED   29099487
  REMARK    GeneRIF: TP53 missense mutant alleles that occur in human cancers
            are discussed in the context of high resolution models of these p53
            mutant protein structures to determine the structural features of
            mutations (review).
            Review article
REFERENCE   6  (residues 1 to 354)
  AUTHORS   Aubrey,B.J., Strasser,A. and Kelly,G.L.
  TITLE     Tumor-Suppressor Functions of the TP53 Pathway
  JOURNAL   Cold Spring Harb Perspect Med 6 (5), a026062 (2016)
   PUBMED   27141080
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 354)
  AUTHORS   Soussi,T. and Wiman,K.G.
  TITLE     TP53: an oncogene in disguise
  JOURNAL   Cell Death Differ 22 (8), 1239-1249 (2015)
   PUBMED   26024390
  REMARK    Review article
REFERENCE   8  (residues 1 to 354)
  AUTHORS   Soussi,T.
  TITLE     The TP53 gene network in a postgenomic era
  JOURNAL   Hum Mutat 35 (6), 641-642 (2014)
   PUBMED   24753184
  REMARK    GeneRIF: Recommendations and guidelines for reporting and
            annotating TP53 variants are also provided, to help researchers
            generate standardized data that are easy to understand, analyze,
            and exchange across various cancer variant databases
            Review article
REFERENCE   9  (residues 1 to 354)
  AUTHORS   Anczukow,O., Ware,M.D., Buisson,M., Zetoune,A.B.,
            Stoppa-Lyonnet,D., Sinilnikova,O.M. and Mazoyer,S.
  TITLE     Does the nonsense-mediated mRNA decay mechanism prevent the
            synthesis of truncated BRCA1, CHK2, and p53 proteins?
  JOURNAL   Hum Mutat 29 (1), 65-73 (2008)
   PUBMED   17694537
  REMARK    GeneRIF: the p53 protein encoded by the 770delT allele is as
            abundant as the wild-type protein, as removal of the C-terminal p53
            domain leads to a stabilized mutant protein, whose abundance is
            markedly increased when NMD is inhibited.
REFERENCE   10 (residues 1 to 354)
  AUTHORS   Bourdon,J.C.
  TITLE     p53 Family isoforms
  JOURNAL   Curr Pharm Biotechnol 8 (6), 332-336 (2007)
   PUBMED   18289041
  REMARK    Review article
REFERENCE   11 (residues 1 to 354)
  AUTHORS   Candeias,M.M., Powell,D.J., Roubalova,E., Apcher,S., Bourougaa,K.,
            Vojtesek,B., Bruzzoni-Giovanelli,H. and Fahraeus,R.
  TITLE     Expression of p53 and p53/47 are controlled by alternative
            mechanisms of messenger RNA translation initiation
  JOURNAL   Oncogene 25 (52), 6936-6947 (2006)
   PUBMED   16983332
  REMARK    GeneRIF: harbouring alternative translation initiation sites, the
            p53 mRNA gives rise to different levels of the p53 isoforms which
            help to orchestrate the cell biological outcome of p53 activation
REFERENCE   12 (residues 1 to 354)
  AUTHORS   Murray-Zmijewski,F., Lane,D.P. and Bourdon,J.C.
  TITLE     p53/p63/p73 isoforms: an orchestra of isoforms to harmonise cell
            differentiation and response to stress
  JOURNAL   Cell Death Differ 13 (6), 962-972 (2006)
   PUBMED   16601753
  REMARK    Review article
REFERENCE   13 (residues 1 to 354)
  AUTHORS   Bourdon,J.C., Fernandes,K., Murray-Zmijewski,F., Liu,G., Diot,A.,
            Xirodimas,D.P., Saville,M.K. and Lane,D.P.
  TITLE     p53 isoforms can regulate p53 transcriptional activity
  JOURNAL   Genes Dev 19 (18), 2122-2137 (2005)
   PUBMED   16131611
  REMARK    GeneRIF: p53 isoforms can regulate p53 transcriptional activity.
REFERENCE   14 (residues 1 to 354)
  AUTHORS   Ghosh,A., Stewart,D. and Matlashewski,G.
  TITLE     Regulation of human p53 activity and cell localization by
            alternative splicing
  JOURNAL   Mol Cell Biol 24 (18), 7987-7997 (2004)
   PUBMED   15340061
  REMARK    GeneRIF: mechanism of p53 regulation originating through
            alternative splicing of the human p53 gene resulting in the
            expression of a novel p53 mRNA
REFERENCE   15 (residues 1 to 354)
  AUTHORS   Flaman,J.M., Waridel,F., Estreicher,A., Vannier,A., Limacher,J.M.,
            Gilbert,D., Iggo,R. and Frebourg,T.
  TITLE     The human tumour suppressor gene p53 is alternatively spliced in
            normal cells
  JOURNAL   Oncogene 12 (4), 813-818 (1996)
   PUBMED   8632903
REFERENCE   16 (residues 1 to 354)
  AUTHORS   Schneider,K., Zelley,K., Nichols,K.E., Schwartz Levine,A. and
            Garber,J.
  TITLE     Li-Fraumeni Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301488
REFERENCE   17 (residues 1 to 354)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   18 (residues 1 to 354)
  AUTHORS   Lamb,P. and Crawford,L.
  TITLE     Characterization of the human p53 gene
  JOURNAL   Mol Cell Biol 6 (5), 1379-1385 (1986)
   PUBMED   2946935
REFERENCE   19 (residues 1 to 354)
  AUTHORS   Isobe,M., Emanuel,B.S., Givol,D., Oren,M. and Croce,C.M.
  TITLE     Localization of gene for human p53 tumour antigen to band 17p13
  JOURNAL   Nature 320 (6057), 84-85 (1986)
   PUBMED   3456488
REFERENCE   20 (residues 1 to 354)
  AUTHORS   Benchimol,S., Lamb,P., Crawford,L.V., Sheer,D., Shows,T.B.,
            Bruns,G.A. and Peacock,J.
  TITLE     Transformation associated p53 protein is encoded by a gene on human
            chromosome 17
  JOURNAL   Somat Cell Mol Genet 11 (5), 505-510 (1985)
   PUBMED   2994241
REFERENCE   21 (residues 1 to 354)
  AUTHORS   Harlow,E., Williamson,N.M., Ralston,R., Helfman,D.M. and Adams,T.E.
  TITLE     Molecular cloning and in vitro expression of a cDNA clone for human
            cellular tumor antigen p53
  JOURNAL   Mol Cell Biol 5 (7), 1601-1610 (1985)
   PUBMED   3894933
REFERENCE   22 (residues 1 to 354)
  AUTHORS   Zakut-Houri,R., Bienz-Tadmor,B., Givol,D. and Oren,M.
  TITLE     Human p53 cellular tumor antigen: cDNA sequence and expression in
            COS cells
  JOURNAL   EMBO J 4 (5), 1251-1255 (1985)
   PUBMED   4006916
REFERENCE   23 (residues 1 to 354)
  AUTHORS   Matlashewski,G., Lamb,P., Pim,D., Peacock,J., Crawford,L. and
            Benchimol,S.
  TITLE     Isolation and characterization of a human p53 cDNA clone:
            expression of the human p53 gene
  JOURNAL   EMBO J 3 (13), 3257-3262 (1984)
   PUBMED   6396087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087388.9 and AC007421.13.
            
            Summary: This gene encodes a tumor suppressor protein containing
            transcriptional activation, DNA binding, and oligomerization
            domains. The encoded protein responds to diverse cellular stresses
            to regulate expression of target genes, thereby inducing cell cycle
            arrest, apoptosis, senescence, DNA repair, or changes in
            metabolism. Mutations in this gene are associated with a variety of
            human cancers, including hereditary cancers such as Li-Fraumeni
            syndrome. Alternative splicing of this gene and the use of
            alternate promoters result in multiple transcript variants and
            isoforms. Additional isoforms have also been shown to result from
            the use of alternate translation initiation codons from identical
            transcript variants (PMIDs: 12032546, 20937277). [provided by
            RefSeq, Dec 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.663221.1,
                                           SRR14038195.421116.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:2946935)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..354
                     /product="cellular tumor antigen p53 isoform g"
                     /note="tumor protein 53; mutant tumor protein 53; cellular
                     tumor antigen p53; phosphoprotein p53;
                     transformation-related protein 53; antigen NY-CO-13; tumor
                     supressor p53"
                     /calculated_mol_wt=39189
     Region          1..20
                     /region_name="TAD2"
                     /note="Transactivation domain 2; pfam18521"
                     /db_xref="CDD:375947"
     Region          70..249
                     /region_name="P53"
                     /note="P53 DNA-binding domain; cd08367"
                     /db_xref="CDD:176262"
     Site            order(137,140,199,203)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:176262"
     Site            order(138..140,142)
                     /site_type="other"
                     /note="dimerization site [polypeptide binding]"
                     /db_xref="CDD:176262"
     Site            order(200,202,209,234,236..238,241)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176262"
     Region          280..319
                     /region_name="P53_tetramer"
                     /note="P53 tetramerization motif; pfam07710"
                     /db_xref="CDD:462238"
     CDS             1..354
                     /gene="TP53"
                     /gene_synonym="BCC7; BMFS5; LFS1; P53; TRP53"
                     /coded_by="NM_001407263.1:363..1427"
                     /note="isoform g is encoded by transcript variant 9"
                     /db_xref="GeneID:7157"
                     /db_xref="HGNC:HGNC:11998"
                     /db_xref="MIM:191170"
ORIGIN      
        1 mddlmlspdd ieqwftedpg pdeaprmpea appvapapaa ptpaapapap swplsssvps
       61 qktyqgsygf rlgflhsgta ksvtctyspa lnkmfcqlak tcpvqlwvds tpppgtrvra
      121 maiykqsqhm tevvrrcphh ercsdsdgla ppqhlirveg nlrveylddr ntfrhsvvvp
      181 yeppevgsdc ttihynymcn sscmggmnrr piltiitled ssgnllgrns fevrvcacpg
      241 rdrrteeenl rkkgephhel ppgstkralp nntssspqpk kkpldgeyft lqirgrerfe
      301 mfrelneale lkdaqagkep ggsrahsshl kskkgqstsr hkklmfkteg pdsd
//
LOCUS       NP_001393929             456 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform M [Homo sapiens].
ACCESSION   NP_001393929
VERSION     NP_001393929.1
DBSOURCE    REFSEQ: accession NM_001407000.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 456)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 456)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 456)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1702734.1,
                                           SRR14038196.2878842.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..456
                     /product="lamin isoform M"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=49912
     Region          <104..178
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          226..333
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     CDS             1..456
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001407000.1:873..2243"
                     /note="isoform M is encoded by transcript variant 25"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 mrpdwwrltm gssvslragw rmrcrncgps mrtrwssirr swrrlilpsw tmpgsllrgt
       61 atwwglptrs cssrasasta slpssassrs ralgsspnpp tplqlaakea klrdledsla
      121 rerdtsrrll aekeremaem rarmqqqlde yqelldikla ldmeihayrk llegeeerlr
      181 lspsptsqrs rgrasshssq tqgggsvtkk rklestesrs sfsqhartsg rvaveevdee
      241 gkfvrlrnks nedqsmgnwq ikrqngddpl ltyrfppkft lkagqvvtiw aagagathsp
      301 ptdlvwkaqn twgcgnslrt alinstgeev amrklvrsvt vveddededg ddllhhhhgs
      361 hcsssgdpae ynlrsrtvlc gtcgqpadka sasgsgaqvg gpissgssas svtvtrsyrs
      421 vggsgggsfg dnlvtrsyll gnssprtqsp qncsim
//
LOCUS       NP_001398003             655 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase tousled-like 2 isoform F [Homo
            sapiens].
ACCESSION   NP_001398003 XP_047291144
VERSION     NP_001398003.1
DBSOURCE    REFSEQ: accession NM_001411074.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Liang,B., Yin,J.J., Zhang,S.N., Zhang,C., Hu,Z.L. and Wang,Y.
  TITLE     [Effect of TLK2 Expression Regulated by MiR-21 on Proliferation and
            Apoptosis of Acute Myeloid Leukemia Cells]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 32 (3), 658-662 (2024)
   PUBMED   38926950
  REMARK    GeneRIF: [Effect of TLK2 Expression Regulated by MiR-21 on
            Proliferation and Apoptosis of Acute Myeloid Leukemia Cells].
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Ronald,S., Sunavala-Dossabhoy,G., Adams,L., Williams,B. and De
            Benedetti,A.
  TITLE     The expression of Tousled kinases in CaP cell lines and its
            relation to radiation response and DSB repair
  JOURNAL   Prostate 71 (13), 1367-1373 (2011)
   PUBMED   21647934
  REMARK    GeneRIF: TLKs appear to be intimately linked to the pattern of
            resistance to DNA damage, and specifically double-strand breaks.
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Couch,F.J., Wang,X., Bamlet,W.R., de Andrade,M., Petersen,G.M. and
            McWilliams,R.R.
  TITLE     Association of mitotic regulation pathway polymorphisms with
            pancreatic cancer risk and outcome
  JOURNAL   Cancer Epidemiol Biomarkers Prev 19 (1), 251-257 (2010)
   PUBMED   20056645
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   5  (residues 1 to 655)
  AUTHORS   Pilyugin,M., Demmers,J., Verrijzer,C.P., Karch,F. and Moshkin,Y.M.
  TITLE     Phosphorylation-mediated control of histone chaperone ASF1 levels
            by Tousled-like kinases
  JOURNAL   PLoS One 4 (12), e8328 (2009)
   PUBMED   20016786
  REMARK    GeneRIF: ASF1 cellular levels are tightly controlled by distinct
            pathways and provide a molecular mechanism for post-translational
            regulation of dASF1 and hASF1a by TLK kinases.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Groth,A., Lukas,J., Nigg,E.A., Sillje,H.H., Wernstedt,C., Bartek,J.
            and Hansen,K.
  TITLE     Human Tousled like kinases are targeted by an ATM- and
            Chk1-dependent DNA damage checkpoint
  JOURNAL   EMBO J 22 (7), 1676-1687 (2003)
   PUBMED   12660173
REFERENCE   7  (residues 1 to 655)
  AUTHORS   Sillje,H.H. and Nigg,E.A.
  TITLE     Identification of human Asf1 chromatin assembly factors as
            substrates of Tousled-like kinases
  JOURNAL   Curr Biol 11 (13), 1068-1073 (2001)
   PUBMED   11470414
REFERENCE   8  (residues 1 to 655)
  AUTHORS   Sillje,H.H., Takahashi,K., Tanaka,K., Van Houwe,G. and Nigg,E.A.
  TITLE     Mammalian homologues of the plant Tousled gene code for
            cell-cycle-regulated kinases with maximal activities linked to
            ongoing DNA replication
  JOURNAL   EMBO J 18 (20), 5691-5702 (1999)
   PUBMED   10523312
REFERENCE   9  (residues 1 to 655)
  AUTHORS   Zhang,S., Xing,H. and Muslin,A.J.
  TITLE     Nuclear localization of protein kinase U-alpha is regulated by
            14-3-3
  JOURNAL   J Biol Chem 274 (35), 24865-24872 (1999)
   PUBMED   10455159
REFERENCE   10 (residues 1 to 655)
  AUTHORS   Yamakawa,A., Kameoka,Y., Hashimoto,K., Yoshitake,Y., Nishikawa,K.,
            Tanihara,K. and Date,T.
  TITLE     cDNA cloning and chromosomal mapping of genes encoding novel
            protein kinases termed PKU-alpha and PKU-beta, which have nuclear
            localization signal
  JOURNAL   Gene 202 (1-2), 193-201 (1997)
   PUBMED   9427565
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008026.7 and AC080038.5.
            
            On Aug 20, 2022 this sequence version replaced XP_047291144.1.
            
            Summary: This gene encodes a nuclear serine/threonine kinase that
            was first identified in Arabidopsis. The encoded protein is thought
            to function in the regulation of chromatin assembly in the S phase
            of the cell cycle by regulating the levels of a histone H3/H4
            chaperone. This protein is associated with double-strand break
            repair of DNA damage caused by radiation. Pseudogenes of this gene
            are present on chromosomes 10 and 17. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.10170.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.2"
     Protein         1..655
                     /product="serine/threonine-protein kinase tousled-like 2
                     isoform F"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase tousled-like 2"
                     /calculated_mol_wt=75280
     Region          338..646
                     /region_name="STKc_TLK2"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Tousled-Like Kinase 2; cd14041"
                     /db_xref="CDD:270943"
     Site            order(351..355,359,372,374,410,427..430,434,436,475,477,
                     479..480,482,496,499,522..525)
                     /site_type="active"
                     /db_xref="CDD:270943"
     Site            order(351..355,359,372,374,410,427..430,434,475,477,
                     479..480,482,496)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270943"
     Site            order(355,434,436,475,477,479,499,522..525)
                     /site_type="other"
                     /note="polypeptide substrate binding site"
                     /db_xref="CDD:270943"
     Site            order(495..501,522..525)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270943"
     CDS             1..655
                     /gene="TLK2"
                     /gene_synonym="HsHPK; MRD57; PKU-ALPHA"
                     /coded_by="NM_001411074.1:469..2436"
                     /note="isoform F is encoded by transcript variant J"
                     /db_xref="CCDS:CCDS92374.1"
                     /db_xref="GeneID:11011"
                     /db_xref="HGNC:HGNC:11842"
                     /db_xref="MIM:608439"
ORIGIN      
        1 mmeelhsldp rrqellearf tgvgvskgpl nsessnqslc svgslsdkev etpekkqndq
       61 rnrkrkaepy etsqgkgtpr ghkisdyfer rveqplygld gsaakeatee qsalptlmsv
      121 mlakprldte qlaqrgaglc ftfvsancdl rrqideqqkm lekykerlnr cvtmskklli
      181 ekskqekmac rdksmqdrlr lghfttvrhg asfteqwtdg yafqnlikqq erinsqreei
      241 erqrkmlakr kppamgqapp atneqkqrks ktngaenetl tlaeyheqee ifklrlghlk
      301 keeaeiqael erlervrnlh irelkrihne dnsqfkdhpt lndrylllhl lgrggfsevy
      361 kafdlteqry vavkihqlnk nwrdekkeny hkhacreyri hkeldhpriv klydyfsldt
      421 dsfctvleyc egndldfylk qhklmsekea rsiimqivna lkylneikpp iihydlkpgn
      481 illvngtacg eikitdfgls kimdddsyns vdgmeltsqg agtywylppe cfvvgkeppk
      541 isnkvdvwsv gvifyqclyg rkpfghnqsq qdilqentil katevqfppk pvvtpeakaf
      601 irrclayrke dridvqqlac dpyllphirk svstsspaga aiastsgasn nsssn
//
LOCUS       NP_001425164            2052 aa            linear   PRI 21-NOV-2025
DEFINITION  nuclear receptor coactivator 6 isoform 5 [Homo sapiens].
ACCESSION   NP_001425164 XP_047296008 XP_054179232
VERSION     NP_001425164.1
DBSOURCE    REFSEQ: accession NM_001438235.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2052)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2052)
  AUTHORS   Lee,K.G., Hong,B.K., Lee,S., Lee,N., Kim,S.W., Kim,D. and Kim,W.U.
  TITLE     Nuclear receptor coactivator 6 is a critical regulator of NLRP3
            inflammasome activation and gouty arthritis
  JOURNAL   Cell Mol Immunol 21 (3), 227-244 (2024)
   PUBMED   38195836
  REMARK    GeneRIF: Nuclear receptor coactivator 6 is a critical regulator of
            NLRP3 inflammasome activation and gouty arthritis.
REFERENCE   3  (residues 1 to 2052)
  AUTHORS   Fang,Y., Xu,Y., Liao,W., Ji,T., Yu,L., Li,L., Pan,M. and Yang,D.
  TITLE     Multiomics analyses and machine learning of nuclear receptor
            coactivator 6 reveal its essential role in hepatocellular carcinoma
  JOURNAL   Cancer Sci 114 (1), 75-90 (2023)
   PUBMED   36086920
  REMARK    GeneRIF: Multiomics analyses and machine learning of nuclear
            receptor coactivator 6 reveal its essential role in hepatocellular
            carcinoma.
REFERENCE   4  (residues 1 to 2052)
  AUTHORS   Watanabe,N., Kawagoe,J., Sugiyama,A., Takehara,I., Ohta,T. and
            Nagase,S.
  TITLE     Nuclear receptor coactivator-6 is essential for the morphological
            change of human uterine stromal cell decidualization via regulating
            actin fiber reorganization
  JOURNAL   Mol Reprod Dev 89 (4), 165-174 (2022)
   PUBMED   35384116
  REMARK    GeneRIF: Nuclear receptor coactivator-6 is essential for the
            morphological change of human uterine stromal cell decidualization
            via regulating actin fiber reorganization.
REFERENCE   5  (residues 1 to 2052)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 2052)
  AUTHORS   Caira,F., Antonson,P., Pelto-Huikko,M., Treuter,E. and
            Gustafsson,J.A.
  TITLE     Cloning and characterization of RAP250, a novel nuclear receptor
            coactivator
  JOURNAL   J Biol Chem 275 (8), 5308-5317 (2000)
   PUBMED   10681503
REFERENCE   7  (residues 1 to 2052)
  AUTHORS   Lee,S.K., Anzick,S.L., Choi,J.E., Bubendorf,L., Guan,X.Y.,
            Jung,Y.K., Kallioniemi,O.P., Kononen,J., Trent,J.M., Azorsa,D.,
            Jhun,B.H., Cheong,J.H., Lee,Y.C., Meltzer,P.S. and Lee,J.W.
  TITLE     A nuclear factor, ASC-2, as a cancer-amplified transcriptional
            coactivator essential for ligand-dependent transactivation by
            nuclear receptors in vivo
  JOURNAL   J Biol Chem 274 (48), 34283-34293 (1999)
   PUBMED   10567404
REFERENCE   8  (residues 1 to 2052)
  AUTHORS   Guan,X.Y., Xu,J., Anzick,S.L., Zhang,H., Trent,J.M. and
            Meltzer,P.S.
  TITLE     Hybrid selection of transcribed sequences from microdissected DNA:
            isolation of genes within amplified region at 20q11-q13.2 in breast
            cancer
  JOURNAL   Cancer Res 56 (15), 3446-3450 (1996)
   PUBMED   8758910
REFERENCE   9  (residues 1 to 2052)
  AUTHORS   Carney,J.P., McKnight,C., VanEpps,S. and Kelley,M.R.
  TITLE     Random rapid amplification of cDNA ends (RRACE) allows for cloning
            of multiple novel human cDNA fragments containing (CAG)n repeats
  JOURNAL   Gene 155 (2), 289-292 (1995)
   PUBMED   7536696
REFERENCE   10 (residues 1 to 2052)
  AUTHORS   Estey,A., Kemp,M., Allison,S. and Lamb,C.
  TITLE     Evaluation of a patient information booklet
  JOURNAL   J Nurs Staff Dev 9 (6), 278-282 (1993)
   PUBMED   8263591
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049709.18 and AL109824.24.
            
            On or before Apr 16, 2025 this sequence version replaced
            XP_047296008.1, XP_054179232.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            coactivator that can interact with nuclear hormone receptors to
            enhance their transcriptional activator functions. This protein has
            been shown to be involved in the hormone-dependent coactivation of
            several receptors, including prostanoid, retinoid, vitamin D3,
            thyroid hormone, and steroid receptors. Alternatively spliced
            transcript variants encoding different isoforms have been described
            for this gene. [provided by RefSeq, Jun 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853560.18259.1,
                                           SRR14038197.2224021.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2052
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..2052
                     /product="nuclear receptor coactivator 6 isoform 5"
                     /note="amplified in breast cancer-3 protein; activating
                     signal cointegrator-2; nuclear receptor coactivator
                     RAP250; peroxisome proliferator-activated receptor
                     interacting protein; thyroid hormone receptor binding
                     protein; NRC RAP250; PPAR-interacting protein; amplified
                     in breast cancer protein 3; nuclear receptor-activating
                     protein, 250 kDa; cancer-amplified transcriptional
                     coactivator ASC-2"
                     /calculated_mol_wt=217847
     Region          48..190
                     /region_name="Nucleic_acid_bd"
                     /note="Putative nucleic acid-binding region; pfam13820"
                     /db_xref="CDD:463988"
     Site            95
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          184..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          <185..492
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          513..>827
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          762..916
                     /region_name="NCOA6IP-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          778..800
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            873
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK, in vitro.
                     /evidence=ECO:0000269|PubMed:11773444; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          876..880
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          888..1267
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1036
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          <1045..1291
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1047
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1085
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1299..1342
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1437..1463
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1480..1484
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1630..2052
                     /region_name="EP300/CRSP3-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1727..1809
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1808
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1811
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1826..1897
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1984..2052
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            2007
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     CDS             1..2052
                     /gene="NCOA6"
                     /gene_synonym="AIB3; ASC2; NRC; PRIP; RAP250; TRBP"
                     /coded_by="NM_001438235.1:344..6502"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:23054"
                     /db_xref="HGNC:HGNC:15936"
                     /db_xref="MIM:605299"
ORIGIN      
        1 mvlddlpnle diytslcsst medsemdfds gledddtksd siledstifv afkgniddkd
       61 fkwkldailk nvpnllhmes sklkvqkvep wnsvrvtfni preaaerlri laqsnnqqlr
      121 dlgilsvqie gegainlala qnrsqdvrmn gpmgagnsvr meagfpmasg pgiirmnnpa
      181 tvmippggnv sssmmapgpn pelqprtprp asqsdamdpl lsglhiqqqs hpsgslapph
      241 hpmqpvsvnr qmnpanfpql qqqqqqqqqq qqqqqqqqqq qqqqqlqarp pqqhqqqqpq
      301 girpqftapt qvpvppgwnq lpsgalqppp aqgslgtmta nqgwkkaplp gpmqqqlqar
      361 pslatvqtps hppppypfgs qqasqahtnf pqmsnpgqft apqmkslqgg psrvptplqq
      421 phltnkspas spssfqqgsp assptvnqtq qqmgprppqn nplpqgfqqp vsspgrnpmv
      481 qqgnvppnfm vmqqqppnqg pqslhpglga gqanpnfmqg qvpsttattp gnsgapqlqa
      541 nqnvqhaggq gagppqnqmq vshgppnmmq pslmgihgnm nnqqagtsgv pqvnlsnmqg
      601 qpqqgppsql mgmhqqivps qgqmvqqqgt lnpqnpmils raqlmpqgqm mvnppsqnlg
      661 pspqrmtppk qmlsqqgpqm maphnqmmgp qgqvllqqnp mieqimtnqm qgnkqqfntq
      721 nqsnvmpgpa qimrgptpnm qgnmvqftgq msgqmlpqqg pvnnspsqvm giqgqvlrpp
      781 gpsphmaqqh gdpattannd vslsqmmpdv siqqtnmvpp hvqamqgnsa sgnhfsghgm
      841 sfnapfsgap ngnqmscgqn pgfpvnkdvt ltspllvnll qsdisaghfg vnnkqnntna
      901 nkpkkkkppr kkknsqqdln tpdtrpagle eadqpplpge qginldnsgp klpefsnrpp
      961 gypsqpveqr plqqmppqlm qhvapppqpp qqqpqpqlpq qqqppppsqp qsqqqqqqqq
     1021 qmmmmlmmqq dpksvrlpvs qnvhpprgpl npdsqrmpmq qsgsvpvmvs lqgpasvpps
     1081 pdkqrmpmpv ntplgsnsrk mvyqespqnp sssplaemas lpeasgseap svpggpnnmp
     1141 shvvlpqnql mmtgpkpgps plsatqgatp qqppvnslps shghhfpnva aptqtsrpkt
     1201 pnrasprpyy pqtpnnrpps tepseislsp erlnasiagl fppqiniplp prpnlnrgfd
     1261 qqglnpttlk aigqapsnlt mnpsnfatpq thkldsvvvn sgkqsnsgat kraspsnsrr
     1321 sspgssrktt pspgrqnska pkltlasqtn aallqnvelp rnvlvsptpl anppvpgsfp
     1381 nnsglnpqns tvsvaavggv vednkeslnv pqdsdcqnsq srkeqvniel kavpaqevkm
     1441 vvpedqskkd gqpsdpnklp sveenknlvs pamreaptsl sqlldnsgap nvtikppglt
     1501 dlevtppvvs gedlkkasvi ptlqdlsssk epsnslnlph snelcsslvh pelsevssnv
     1561 apsippvmsr pvssssistp lppnqitvfv tsnpittsan tsaalpthlq salmstvvtm
     1621 pnagskvmvs egqsaaqsna rpqfitpvfi nsssiiqvmk gsqpstipaa plttnsglmp
     1681 psvavvgplh ipqnikfssa pvppnalsss papniqtgrp lvlssratpv qlpsppctss
     1741 pvvpshppvq qvkelnpdea spqvntsadq ntlpssqstt mvsplltnsp gssgnrrspv
     1801 ssskgkgkvd kigqilltka ckkvtgslek geeqygadge tegqgldtta pglmgteqls
     1861 teldsktptp paptllkmts spvgpgtasa gpslpggalp tsvrsivttl vpselisavp
     1921 ttksnhggia seslagglve ekvgshpell psiapsqnlv sketsttalq asvarpelev
     1981 naaivsgqss epkeiveksk ipgrrnsrte eptvasesve nghrkrssrp asassstkdi
     2041 tsavqskrrk sk
//
LOCUS       NP_001401238             414 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 3 isoform 9 [Homo
            sapiens].
ACCESSION   NP_001401238
VERSION     NP_001401238.1
DBSOURCE    REFSEQ: accession NM_001414309.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Tang,Q., Yuan,Y., Li,L., Xu,Y., Ji,W., Xiao,S., Han,Y., Miao,W.,
            Cai,J., You,P., Chen,M., Ding,S., Li,Z., Qi,Z., Hou,W. and Luo,H.
  TITLE     Comprehensive analysis reveals that LTBR is a immune-related
            biomarker for glioma
  JOURNAL   Comput Biol Med 174, 108457 (2024)
   PUBMED   38599071
  REMARK    GeneRIF: Comprehensive analysis reveals that LTBR is a
            immune-related biomarker for glioma.
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Wu,Y., Zhao,S., Guo,W., Liu,Y., Requena Mullor,M.D.M.,
            Rodriguez,R.A. and Wei,R.
  TITLE     Systematic analysis of the prognostic value and immunological
            function of LTBR in human cancer
  JOURNAL   Aging (Albany NY) 16 (1), 129-152 (2024)
   PUBMED   38175686
  REMARK    GeneRIF: Systematic analysis of the prognostic value and
            immunological function of LTBR in human cancer.
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Shuptrine,C.W., Perez,V.M., Selitsky,S.R., Schreiber,T.H. and
            Fromm,G.
  TITLE     Shining a LIGHT on myeloid cell targeted immunotherapy
  JOURNAL   Eur J Cancer 187, 147-160 (2023)
   PUBMED   37167762
  REMARK    Review article
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Abudukeyoumu,A., Lai,Z.Z., Lu,J.J., Zhang,X., Hou,D.Y., Dong,J.,
            Wu,J.N., Li,M.Q. and Xie,F.
  TITLE     A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion
  JOURNAL   J Reprod Immunol 153, 103693 (2022)
   PUBMED   35987137
  REMARK    GeneRIF: A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion.
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Remouchamps,C., Boutaffala,L., Ganeff,C. and Dejardin,E.
  TITLE     Biology and signal transduction pathways of the
            Lymphotoxin-alphabeta/LTbetaR system
  JOURNAL   Cytokine Growth Factor Rev 22 (5-6), 301-310 (2011)
   PUBMED   22152226
  REMARK    Review article
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Nakano,H., Oshima,H., Chung,W., Williams-Abbott,L., Ware,C.F.,
            Yagita,H. and Okumura,K.
  TITLE     TRAF5, an activator of NF-kappaB and putative signal transducer for
            the lymphotoxin-beta receptor
  JOURNAL   J Biol Chem 271 (25), 14661-14664 (1996)
   PUBMED   8663299
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Browning,J.L., Miatkowski,K., Sizing,I., Griffiths,D., Zafari,M.,
            Benjamin,C.D., Meier,W. and Mackay,F.
  TITLE     Signaling through the lymphotoxin beta receptor induces the death
            of some adenocarcinoma tumor lines
  JOURNAL   J Exp Med 183 (3), 867-878 (1996)
   PUBMED   8642291
REFERENCE   8  (residues 1 to 414)
  AUTHORS   Baens,M., Aerssens,J., van Zand,K., Van den Berghe,H. and
            Marynen,P.
  TITLE     Isolation and regional assignment of human chromosome 12p cDNAs
  JOURNAL   Genomics 29 (1), 44-52 (1995)
   PUBMED   8530100
REFERENCE   9  (residues 1 to 414)
  AUTHORS   Crowe,P.D., VanArsdale,T.L., Walter,B.N., Ware,C.F., Hession,C.,
            Ehrenfels,B., Browning,J.L., Din,W.S., Goodwin,R.G. and Smith,C.A.
  TITLE     A lymphotoxin-beta-specific receptor
  JOURNAL   Science 264 (5159), 707-710 (1994)
   PUBMED   8171323
REFERENCE   10 (residues 1 to 414)
  AUTHORS   Baens,M., Chaffanet,M., Cassiman,J.J., van den Berghe,H. and
            Marynen,P.
  TITLE     Construction and evaluation of a hncDNA library of human 12p
            transcribed sequences derived from a somatic cell hybrid
  JOURNAL   Genomics 16 (1), 214-218 (1993)
   PUBMED   8486360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005840.2.
            
            Summary: This gene encodes a member of the tumor necrosis factor
            receptor superfamily. The major ligands of this receptor include
            lymphotoxin alpha/beta and tumor necrosis factor ligand superfamily
            member 14. The encoded protein plays a role in signalling during
            the development of lymphoid and other organs, lipid metabolism,
            immune response, and programmed cell death. Activity of this
            receptor has also been linked to carcinogenesis. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.712349.1,
                                           SRR14038192.553167.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..414
                     /product="tumor necrosis factor receptor superfamily
                     member 3 isoform 9"
                     /note="tumor necrosis factor C receptor; lymphotoxin B
                     receptor; tumor necrosis factor receptor type III;
                     lymphotoxin beta receptor (TNFR superfamily, member 3);
                     tumor necrosis factor receptor 2-related protein"
                     /calculated_mol_wt=44435
     Region          4..147
                     /region_name="TNFRSF3"
                     /note="Tumor necrosis factor receptor superfamily member 3
                     (TNFRSF3), also known as lymphotoxin beta receptor (LTBR);
                     cd10578"
                     /db_xref="CDD:276904"
     Region          4..61
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276904"
     Region          64..105
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276904"
     Region          107..146
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276904"
     Region          129..>189
                     /region_name="TNFRSF"
                     /note="Tumor necrosis factor receptor superfamily
                     (TNFRSF); cl22855"
                     /db_xref="CDD:473981"
     Region          149..189
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276900"
     CDS             1..414
                     /gene="LTBR"
                     /gene_synonym="D12S370; LT-BETA-R; TNF-R-III; TNFCR;
                     TNFR-RP; TNFR2-RP; TNFR3; TNFRSF3"
                     /coded_by="NM_001414309.1:397..1641"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:4055"
                     /db_xref="HGNC:HGNC:6718"
                     /db_xref="MIM:600979"
ORIGIN      
        1 meatgislas qlkvppyase nqtcrdqeke yyepqhricc srcppgtyvs akcsrirdtv
       61 catcaensyn ehwnylticq lcrpcdpvmg leeiapctsk rktqcrcqpg mfcaawalec
      121 thcellsdcp pgteaelkvg kgnnhcvpck aghfqntssp sarcqphtrc enqglveaap
      181 gtaqsdttck npleplppem sgtmlmlavl lplaffllla tvfsciwksh pslcrklgsl
      241 lkrrpqgegp npvagswepp kahpyfpdlv qpllpisgdv spvstglpaa pvleagvpqq
      301 qspldltrep qlepgeqsqv ahgtngihvt ggsmtitgni yiyngpvlgg ppgpgdlpat
      361 peppypipee gdpgppglst phqedgkawh laetehcgat psnrgprnqf ithd
//
LOCUS       NP_001425607            1634 aa            linear   PRI 21-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4 gamma 3 isoform 17 [Homo
            sapiens].
ACCESSION   NP_001425607
VERSION     NP_001425607.1
DBSOURCE    REFSEQ: accession NM_001438678.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1634)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1634)
  AUTHORS   Kang,J.Y., Wen,Z., Pan,D., Zhang,Y., Li,Q., Zhong,A., Yu,X.,
            Wu,Y.C., Chen,Y., Zhang,X., Kou,P.C., Geng,J., Wang,Y.Y., Hua,M.M.,
            Zong,R., Li,B., Shi,H.J., Li,D., Fu,X.D., Li,J., Nelson,D.L.,
            Guo,X., Zhou,Y., Gou,L.T., Huang,Y. and Liu,M.F.
  TITLE     LLPS of FXR1 drives spermiogenesis by activating translation of
            stored mRNAs
  JOURNAL   Science 377 (6607), eabj6647 (2022)
   PUBMED   35951695
REFERENCE   3  (residues 1 to 1634)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1634)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 1634)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1634)
  AUTHORS   Waskiewicz,A.J., Johnson,J.C., Penn,B., Mahalingam,M., Kimball,S.R.
            and Cooper,J.A.
  TITLE     Phosphorylation of the cap-binding protein eukaryotic translation
            initiation factor 4E by protein kinase Mnk1 in vivo
  JOURNAL   Mol Cell Biol 19 (3), 1871-1880 (1999)
   PUBMED   10022874
REFERENCE   7  (residues 1 to 1634)
  AUTHORS   Pyronnet,S., Imataka,H., Gingras,A.C., Fukunaga,R., Hunter,T. and
            Sonenberg,N.
  TITLE     Human eukaryotic translation initiation factor 4G (eIF4G) recruits
            mnk1 to phosphorylate eIF4E
  JOURNAL   EMBO J 18 (1), 270-279 (1999)
   PUBMED   9878069
REFERENCE   8  (residues 1 to 1634)
  AUTHORS   Gingras,A.C., Raught,B. and Sonenberg,N.
  TITLE     eIF4 initiation factors: effectors of mRNA recruitment to ribosomes
            and regulators of translation
  JOURNAL   Annu Rev Biochem 68, 913-963 (1999)
   PUBMED   10872469
  REMARK    Review article
REFERENCE   9  (residues 1 to 1634)
  AUTHORS   Imataka,H., Gradi,A. and Sonenberg,N.
  TITLE     A newly identified N-terminal amino acid sequence of human eIF4G
            binds poly(A)-binding protein and functions in poly(A)-dependent
            translation
  JOURNAL   EMBO J 17 (24), 7480-7489 (1998)
   PUBMED   9857202
REFERENCE   10 (residues 1 to 1634)
  AUTHORS   Gradi,A., Imataka,H., Svitkin,Y.V., Rom,E., Raught,B., Morino,S.
            and Sonenberg,N.
  TITLE     A novel functional human eukaryotic translation initiation factor
            4G
  JOURNAL   Mol Cell Biol 18 (1), 334-342 (1998)
   PUBMED   9418880
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031005.2, AL627311.16,
            AL358392.19 and AL606477.11.
            
            Summary: The protein encoded by this gene is thought to be part of
            the eIF4F protein complex, which is involved in mRNA cap
            recognition and transport of mRNAs to the ribosome. Interestingly,
            a microRNA (miR-520c-3p) has been found that negatively regulates
            synthesis of the encoded protein, and this leads to a global
            decrease in protein translation and cell proliferation. Therefore,
            this protein is a key component of the anti-tumor activity of
            miR-520c-3p. [provided by RefSeq, May 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.194828.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1634
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     Protein         1..1634
                     /product="eukaryotic translation initiation factor 4 gamma
                     3 isoform 17"
                     /note="eIF-4-gamma 3; eIF-4-gamma II"
                     /calculated_mol_wt=182230
     Region          <2..276
                     /region_name="PHA03378"
                     /note="EBNA-3B; Provisional"
                     /db_xref="CDD:223065"
     Region          <166..390
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          804..1032
                     /region_name="MIF4G"
                     /note="MIF4G domain; pfam02854"
                     /db_xref="CDD:397130"
     Region          1271..1383
                     /region_name="MA3"
                     /note="MA3 domain; pfam02847"
                     /db_xref="CDD:397128"
     Region          1477..1605
                     /region_name="W2_eIF4G1_like"
                     /note="C-terminal W2 domain of eukaryotic translation
                     initiation factor 4 gamma 1 and similar proteins; cd11559"
                     /db_xref="CDD:211397"
     Region          <1584..1630
                     /region_name="W2"
                     /note="C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon;
                     cl17013"
                     /db_xref="CDD:473053"
     CDS             1..1634
                     /gene="EIF4G3"
                     /gene_synonym="eIF-4G 3; eIF4G 3; eIF4GII"
                     /coded_by="NM_001438678.1:509..5413"
                     /note="isoform 17 is encoded by transcript variant 22"
                     /db_xref="GeneID:8672"
                     /db_xref="HGNC:HGNC:3298"
                     /db_xref="MIM:603929"
ORIGIN      
        1 mnsqpqtrsp psrtvpihct dnwkrrkvle qtpvyrslag rgwikycifa agprpphhqf
       61 fqrpqiqppr atipnsspsi rpgaqtptav yqanqhimmv nhlpmpypvp qgpqycipqy
      121 rhsgppyvgp pqqypvqppg pgpfypgpgp gdfpnaygtp fypsqpvyqs apiivptqqq
      181 pppakrekkt irirdpnqgg kditeeimsg ggsrnptppi grptstptpp qqlpsqvpeh
      241 spvvygtves ahlaastpvt aasdqkqeek pkpdpvlksp spvlrlvlsg ekkeqegqts
      301 ettaivsiae lplppspttv ssvarstiaa ptssalssqp ifttaiddrc elsspredti
      361 pipsltscte tsdplptnen dddickkpcs vapndiplvs stnlineing vseklsates
      421 iveivkqevl pltleleile nppeemklec ipapitpstv psfpptpptp paspphtpvi
      481 vpaaattvss psaaitvqrv leedesirtc lsedakeiqn kieveadgqt eeildsqnln
      541 srrspvpaqi aitvpktwkk pkdrtrttee mleaelelka eeelsidkvl eseqdkmsqg
      601 fhperdpsdl kkvkaveeng eeaepvrnga esvsegegid ansgstdssg dgvtfpfkpe
      661 swkptdtegk kqydreflld fqfmpaciqk peglppisdv vldkinqpkl pmrtldpril
      721 prgpdftpaf adfgrqtpgg rgvpllnvgs rrsqpgqrre prkiitvsvk edvhlkkaen
      781 awkpsqkrds qaddpenikt qelfrkvrsi lnkltpqmfn qlmkqvsglt vdteerlkgv
      841 idlvfekaid epsfsvayan mcrclvtlkv pmadkpgntv nfrklllnrc qkefekdkad
      901 ddvfekkqke leaasapeer trlhdeleea kdkarrrsig nikfigelfk lkmlteaimh
      961 dcvvkllknh deesleclcr llttigkdld fekakprmdq yfnqmekivk erktssrirf
     1021 mlqdvidlrl cnwvsrradq gpktieqihk eakieeqeeq rkvqqlmtke krrpgvqrvd
     1081 eggwntvqga knsrvldpsk flkitkptid ekiqlvpkaq lgswgkgssg gakasetdal
     1141 rssasslnrf salqppapsg stpstpvefd srrtltsrgs mgrekndkpl psatarpntf
     1201 mrggsskdll dnqsqeeqrr emletvkqlt ggvdvernst eaernktres akpeisamsa
     1261 hdkaalseee lerksksiid eflhindfke amqcveelna qgllhvfvrv gvestlersq
     1321 itrdhmgqll yqlvqsekls kqdffkgfse tleladdmai diphiwlyla elvtpmlkeg
     1381 gismreltie fskpllpvgr agvllseilh llckqmshkk vgalwreadl swkdflpege
     1441 dvhnflleqk ldfiesdspc ssealskkel saeelykrle kliiedkand eqifdwvean
     1501 ldeiqmsspt flralmtavc kaaiiadsst frvdtavikq rvpillkyld sdtekelqal
     1561 yalqasivkl dqpanllrmf fdclydeevi sedafykwes skdpaeqngk gvalksvtaf
     1621 ftwlreaeee sedn
//
LOCUS       NP_001427531             330 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform q [Homo sapiens].
ACCESSION   NP_001427531
VERSION     NP_001427531.1
DBSOURCE    REFSEQ: accession NM_001440602.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 330)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 330)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 330)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 330)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 330)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1125257.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..330
                     /product="polycomb protein EED isoform q"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=36995
     Region          <90..>327
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          117..157
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          162..199
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          254..294
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          302..326
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..330
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001440602.1:478..1470"
                     /note="isoform q is encoded by transcript variant 17"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdendd avsiesgtnt erpdtptntp
       61 napgrkswgk gkwkskkcky sfkcvnslkv tlyechsqge irllqsyvda dadenfytca
      121 wtydsntshp llavagsrgi iriinpitmq cikhyvghgn ainelkfhpr dpnlllsvsk
      181 dhalrlwniq tdtlvaifgg veghrdevls ascenaivcw kpgkmeddid kikpsesnvt
      241 ilgrfdysqc diwymrfsmd fwqkmlalgn qvgklyvwdl evedphkakc ttlthhkcga
      301 airqtsfsrd ssiliavcdd asiwrwdrlr
//
LOCUS       NP_001427453             289 aa            linear   PRI 21-NOV-2025
DEFINITION  syntaxin-3 isoform 1 [Homo sapiens].
ACCESSION   NP_001427453
VERSION     NP_001427453.1
DBSOURCE    REFSEQ: accession NM_001440524.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Shinozuka,T., Kanda,M., Sato,Y., Shimizu,D., Tanaka,C., Umeda,S.,
            Inokawa,Y., Hattori,N., Hayashi,M., Nakayama,G. and Kodera,Y.
  TITLE     Increased STX3 transcript and protein levels were associated with
            poor prognosis in two independent cohorts of esophageal squamous
            cell carcinoma patients
  JOURNAL   Cancer Med 12 (24), 22185-22195 (2023)
   PUBMED   38014487
  REMARK    GeneRIF: Increased STX3 transcript and protein levels were
            associated with poor prognosis in two independent cohorts of
            esophageal squamous cell carcinoma patients.
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Janecke,A.R., Liu,X., Adam,R., Punuru,S., Viestenz,A., Strauss,V.,
            Laass,M., Sanchez,E., Adachi,R., Schatz,M.P., Saboo,U.S.,
            Mittal,N., Rohrschneider,K., Escher,J., Ganesh,A., Al Zuhaibi,S.,
            Al Murshedi,F., AlSaleem,B., Alfadhel,M., Al Sinani,S.,
            Alkuraya,F.S., Huber,L.A., Muller,T., Heidelberger,R. and Janz,R.
  TITLE     Pathogenic STX3 variants affecting the retinal and intestinal
            transcripts cause an early-onset severe retinal dystrophy in
            microvillus inclusion disease subjects
  JOURNAL   Hum Genet 140 (8), 1143-1156 (2021)
   PUBMED   33974130
  REMARK    GeneRIF: Pathogenic STX3 variants affecting the retinal and
            intestinal transcripts cause an early-onset severe retinal
            dystrophy in microvillus inclusion disease subjects.
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Low,S.H., Vasanji,A., Nanduri,J., He,M., Sharma,N., Koo,M.,
            Drazba,J. and Weimbs,T.
  TITLE     Syntaxins 3 and 4 are concentrated in separate clusters on the
            plasma membrane before the establishment of cell polarity
  JOURNAL   Mol Biol Cell 17 (2), 977-989 (2006)
   PUBMED   16339081
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Martin-Martin,B., Nabokina,S.M., Lazo,P.A. and Mollinedo,F.
  TITLE     Co-expression of several human syntaxin genes in neutrophils and
            differentiating HL-60 cells: variant isoforms and detection of
            syntaxin 1
  JOURNAL   J Leukoc Biol 65 (3), 397-406 (1999)
   PUBMED   10080545
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Steegmaier,M., Yang,B., Yoo,J.S., Huang,B., Shen,M., Yu,S., Luo,Y.
            and Scheller,R.H.
  TITLE     Three novel proteins of the syntaxin/SNAP-25 family
  JOURNAL   J Biol Chem 273 (51), 34171-34179 (1998)
   PUBMED   9852078
REFERENCE   8  (residues 1 to 289)
  AUTHORS   Riento,K., Galli,T., Jansson,S., Ehnholm,C., Lehtonen,E. and
            Olkkonen,V.M.
  TITLE     Interaction of Munc-18-2 with syntaxin 3 controls the association
            of apical SNAREs in epithelial cells
  JOURNAL   J Cell Sci 111 (Pt 17), 2681-2688 (1998)
   PUBMED   9701566
REFERENCE   9  (residues 1 to 289)
  AUTHORS   Galli,T., Zahraoui,A., Vaidyanathan,V.V., Raposo,G., Tian,J.M.,
            Karin,M., Niemann,H. and Louvard,D.
  TITLE     A novel tetanus neurotoxin-insensitive vesicle-associated membrane
            protein in SNARE complexes of the apical plasma membrane of
            epithelial cells
  JOURNAL   Mol Biol Cell 9 (6), 1437-1448 (1998)
   PUBMED   9614185
REFERENCE   10 (residues 1 to 289)
  AUTHORS   Delgrossi,M.H., Breuza,L., Mirre,C., Chavrier,P. and Le Bivic,A.
  TITLE     Human syntaxin 3 is localized apically in human intestinal cells
  JOURNAL   J Cell Sci 110 (Pt 18), 2207-2214 (1997)
   PUBMED   9378770
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000640.5.
            
            Summary: The gene is a member of the syntaxin family. The encoded
            protein is targeted to the apical membrane of epithelial cells
            where it forms clusters and is important in establishing and
            maintaining polarity necessary for protein trafficking involving
            vesicle fusion and exocytosis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.375882.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162823 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..289
                     /product="syntaxin-3 isoform 1"
                     /note="syntaxin 3A; syntaxin 3B"
                     /calculated_mol_wt=33024
     Region          34..226
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     Region          194..260
                     /region_name="SNARE"
                     /note="SNARE motif; cl22856"
                     /db_xref="CDD:473982"
     Site            order(222,229,232)
                     /site_type="other"
                     /note="flanking leucine-zipper layers"
                     /db_xref="CDD:277192"
     Site            225
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277192"
     Site            264..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13277.3)"
     CDS             1..289
                     /gene="STX3"
                     /gene_synonym="DIAR12; MVID2; RDMVID; STX3A"
                     /coded_by="NM_001440524.1:231..1100"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="GeneID:6809"
                     /db_xref="HGNC:HGNC:11438"
                     /db_xref="MIM:600876"
ORIGIN      
        1 mkdrleqlka kqltqdddtd aveiaidnta fmdeffseie etrlnidkis ehveeakkly
       61 siilsapipe pktkddleql tteikkrann vrnklksmek hieedevrss adlrirksqh
      121 svlsrkfvev mtkyneaqvd frerskgriq rqleitgkkt tdeeleemle sgnpaiftsg
      181 iidsqiskqa lseiegrhkd ivrlessike lhdmfmdiam lvenqgemld nielnvmhtv
      241 dhvekardet kkavkyqsqa rkkliiiivl vvvllgilal iiglsvgln
//
LOCUS       NP_001400240             291 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 2 [Homo sapiens].
ACCESSION   NP_001400240
VERSION     NP_001400240.1
DBSOURCE    REFSEQ: accession NM_001413311.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC103816.2, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.220453.1,
                                           SRR1803613.175574.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968832 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..291
                     /product="RNA-binding Raly-like protein isoform 2"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=32199
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          171..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     Region          199..>244
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     Region          249..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     CDS             1..291
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413311.1:1313..2188"
                     /note="isoform 2 is encoded by transcript variant 38"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly rleskepfls
      121 vggyvfdydy yrddfynrlf dyhgrvpppp raviplkrpr vavtttrrgk gvfsmkggsr
      181 stasgstgsk lksdelqtik keltqiktki dsllgrleki ekqqkaeaea qkkqleeslv
      241 liqeecvsei adhsteepae ggpdadgeem tdgieedfde dgghelflqi k
//
LOCUS       NP_001427732            1184 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphorylase b kinase regulatory subunit alpha, liver isoform
            isoform 5 [Homo sapiens].
ACCESSION   NP_001427732 XP_047298120 XP_054183180
VERSION     NP_001427732.1
DBSOURCE    REFSEQ: accession NM_001440803.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1184)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1184)
  AUTHORS   Dong,R., Wei,X., Zhang,K., Song,F., Lv,Y., Gao,M., Wang,D., Ma,J.,
            Gai,Z. and Liu,Y.
  TITLE     Genotypic and phenotypic characteristics of 12 chinese children
            with glycogen storage diseases
  JOURNAL   Front Genet 13, 932760 (2022)
   PUBMED   36105079
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1184)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1184)
  AUTHORS   Benner,A., Alhaidan,Y., Lines,M.A., Brusgaard,K., De Leon,D.D.,
            Sparkes,R., Frederiksen,A.L. and Christesen,H.T.
  TITLE     PHKA2 variants expand the phenotype of phosphorylase B kinase
            deficiency to include patients with ketotic hypoglycemia only
  JOURNAL   Am J Med Genet A 185 (10), 2959-2975 (2021)
   PUBMED   34117828
  REMARK    GeneRIF: PHKA2 variants expand the phenotype of phosphorylase B
            kinase deficiency to include patients with ketotic hypoglycemia
            only.
REFERENCE   5  (residues 1 to 1184)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1184)
  AUTHORS   Herbert,M., Goldstein,J.L., Rehder,C., Austin,S., Kishnani,P.S. and
            Bali,D.S.
  TITLE     Phosphorylase Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21634085
REFERENCE   7  (residues 1 to 1184)
  AUTHORS   Davidson,J.J., Ozcelik,T., Hamacher,C., Willems,P.J., Francke,U.
            and Kilimann,M.W.
  TITLE     cDNA cloning of a liver isoform of the phosphorylase kinase alpha
            subunit and mapping of the gene to Xp22.2-p22.1, the region of
            human X-linked liver glycogenosis
  JOURNAL   Proc Natl Acad Sci U S A 89 (6), 2096-2100 (1992)
   PUBMED   1372435
REFERENCE   8  (residues 1 to 1184)
  AUTHORS   Wauters,J.G., Bossuyt,P.J., Davidson,J., Hendrickx,J.,
            Kilimann,M.W. and Willems,P.J.
  TITLE     Regional mapping of a liver alpha-subunit gene of phosphorylase
            kinase (PHKA) to the distal region of human chromosome Xp
  JOURNAL   Cytogenet Cell Genet 60 (3-4), 194-196 (1992)
   PUBMED   1505214
REFERENCE   9  (residues 1 to 1184)
  AUTHORS   Willems,P.
  TITLE     Families with X-linked liver glycogenosis due to phosphorylase
            kinase deficiency
  JOURNAL   Clin Genet 38 (1), 80 (1990)
   PUBMED   2387090
REFERENCE   10 (residues 1 to 1184)
  AUTHORS   Willems,P.J., Gerver,W.J., Berger,R. and Fernandes,J.
  TITLE     The natural history of liver glycogenosis due to phosphorylase
            kinase deficiency: a longitudinal study of 41 patients
  JOURNAL   Eur J Pediatr 149 (4), 268-271 (1990)
   PUBMED   2303074
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL732509.4 and AL096700.14.
            
            On or before May 30, 2025 this sequence version replaced
            XP_047298120.1, XP_054183180.1.
            
            Summary: Phosphorylase kinase is a polymer of 16 subunits, four
            each of alpha, beta, gamma and delta. The alpha subunit includes
            the skeletal muscle and hepatic isoforms, and the hepatic isoform
            is encoded by this gene. The beta subunit is the same in both the
            muscle and hepatic isoforms, and encoded by one gene. The gamma
            subunit also includes the skeletal muscle and hepatic isoforms,
            which are encoded by two different genes. The delta subunit is a
            calmodulin and can be encoded by three different genes. The gamma
            subunits contain the active site of the enzyme, whereas the alpha
            and beta subunits have regulatory functions controlled by
            phosphorylation. The delta subunit mediates the dependence of the
            enzyme on calcium concentration. Mutations in this gene cause
            glycogen storage disease type 9A, also known as X-linked liver
            glycogenosis. Alternatively spliced transcript variants have been
            reported, but the full-length nature of these variants has not been
            determined.[provided by RefSeq, Feb 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2764157.1,
                                           SRR14038193.775441.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.13"
     Protein         1..1184
                     /product="phosphorylase b kinase regulatory subunit alpha,
                     liver isoform isoform 5"
                     /EC_number="2.7.11.19"
                     /note="phosphorylase kinase alpha L subunit; phosphorylase
                     kinase alpha-subunit"
                     /calculated_mol_wt=132988
     Region          8..>406
                     /region_name="Glyco_hydro_15"
                     /note="Glycosyl hydrolases family 15; pfam00723"
                     /db_xref="CDD:395586"
     Region          <769..886
                     /region_name="Bac_rhamnosid6H"
                     /note="Bacterial alpha-L-rhamnosidase 6 hairpin
                     glycosidase domain; cl46875"
                     /db_xref="CDD:481215"
     Region          897..>1096
                     /region_name="KPBB_C"
                     /note="Phosphorylase b kinase C-terminal domain;
                     pfam19292"
                     /db_xref="CDD:437124"
     CDS             1..1184
                     /gene="PHKA2"
                     /gene_synonym="GSD9A; PHK; PYK; PYKL; XLG; XLG2"
                     /coded_by="NM_001440803.1:183..3737"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:5256"
                     /db_xref="HGNC:HGNC:8926"
                     /db_xref="MIM:300798"
ORIGIN      
        1 mrsrsnsgvr ldgyarlvqq tilcyqnpvt gllsasheqk dawvrdniys ilavwglgma
       61 yrknadrded kakayeleqn vvklmrgllq cmmrqvakve kfkhtqstkd slhakyntat
      121 cgtvvgddqw ghlqvdatsl fllflaqmta sglriiftld evafiqnlvf yieaaykvad
      181 ygmwergdkt nqgipelnas svgmaksilf smlprastsk eidagllsii sfpafavedv
      241 nlvnvtknei isklqgrygc crflrdgykt predpnrlhy dpaelklfen iecewpvfwt
      301 yfiidgvfsg davqvqeyre alegilirgk ngirlvpely avppnkvdee yknphtvdrv
      361 pmgkvphlwg qslyilssll aegflaagei dplnrrfsts vkpdvvvqvt vlaennhikd
      421 llrkhgvnvq siadihpiqv qpgrilshiy aklgrnknmn lsgrpyrhig vlgtsklyvi
      481 rnqiftftpq ftdqhhfyla ldnemiveml rielaylctc wrmtgrptlt fpisrtmltn
      541 dgsdihsavl stirkledgy fggarvklgn lseflttsfy tyltfldpdc deklfdnase
      601 gtfspdsdsd lvgyledtcn qesqdeldhy inhllqstsl rsylpplckn tedrhvfsai
      661 hstrdilsvm akakglevpf vpmtlptkvl sahrkslnlv dspqpllekv pesdfqwprd
      721 dhgdvdcekl veqlkdcsnl qdqadilyil yvikgpswdt nlsgqhgvtv qnllgelygk
      781 aglnqewgli ryisgllrkk vevlaeactd llshqkqltv glppepreki isaplppeel
      841 tkliyeasgq disiavltqe ivvylamyvr aqpslfveml rlrigliiqv matelarsln
      901 csgeeasesl mnlspfdmkn llhhilsgke fgversvrpi hsstssptis ihevghtgvt
      961 ktersginrl rsemkqmtrr fsadeqrsst pssptgtsss dsgghhigwg erqgqwlrrr
     1021 rldgainrvp vgfyqrvwki lqkchglsid gyvlpssttr emtpheikfa vhvesvlnrv
     1081 pqpeyrqllv eaimvltlls dtemtsiggi ihvdqivqma sqlflqdqvs igamdtlekd
     1141 qatgichffy dsapsgaygt mtyltravas ylqellpnsg cqmq
//
LOCUS       NP_001426200             612 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA replication licensing factor MCM7 isoform 3 [Homo sapiens].
ACCESSION   NP_001426200 XP_005250405 XP_054214227
VERSION     NP_001426200.1
DBSOURCE    REFSEQ: accession NM_001439271.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Sun,Q., Sui,Y., Li,S., Zhou,R., Fu,Z., Luo,J. and Zhao,W.
  TITLE     RNF8-mediated multi-ubiquitination of MCM7: Linking disassembly of
            the CMG helicase with DNA damage response in human cells
  JOURNAL   Life Sci 353, 122912 (2024)
   PUBMED   39004272
  REMARK    GeneRIF: RNF8-mediated multi-ubiquitination of MCM7: Linking
            disassembly of the CMG helicase with DNA damage response in human
            cells.
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Wang,J., Amin,A., Cheung,M.H., Shi,L. and Liang,C.
  TITLE     Targeted inhibition of the expression of both MCM5 and MCM7 by
            miRNA-214 impedes DNA replication and tumorigenesis in
            hepatocellular carcinoma cells
  JOURNAL   Cancer Lett 539, 215677 (2022)
   PUBMED   35490917
  REMARK    GeneRIF: Targeted inhibition of the expression of both MCM5 and
            MCM7 by miRNA-214 impedes DNA replication and tumorigenesis in
            hepatocellular carcinoma cells.
REFERENCE   4  (residues 1 to 612)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 612)
  AUTHORS   Su,D.
  TITLE     MCM7 affects the cisplatin resistance of liver cancer cells and the
            development of liver cancer by regulating the PI3K/Akt signaling
            pathway
  JOURNAL   Immunopharmacol Immunotoxicol 44 (1), 17-27 (2022)
   PUBMED   34821526
  REMARK    GeneRIF: MCM7 affects the cisplatin resistance of liver cancer
            cells and the development of liver cancer by regulating the
            PI3K/Akt signaling pathway.
REFERENCE   6  (residues 1 to 612)
  AUTHORS   Suzuki,S., Adachi,A., Hiraiwa,A., Ohashi,M., Ishibashi,M. and
            Kiyono,T.
  TITLE     Cloning and characterization of human MCM7 promoter
  JOURNAL   Gene 216 (1), 85-91 (1998)
   PUBMED   9714754
REFERENCE   7  (residues 1 to 612)
  AUTHORS   Fujita,M., Kiyono,T., Hayashi,Y. and Ishibashi,M.
  TITLE     hCDC47, a human member of the MCM family. Dissociation of the
            nucleus-bound form during S phase
  JOURNAL   J Biol Chem 271 (8), 4349-4354 (1996)
   PUBMED   8626784
REFERENCE   8  (residues 1 to 612)
  AUTHORS   Musahl,C., Schulte,D., Burkhart,R. and Knippers,R.
  TITLE     A human homologue of the yeast replication protein Cdc21.
            Interactions with other Mcm proteins
  JOURNAL   Eur J Biochem 230 (3), 1096-1101 (1995)
   PUBMED   7601140
REFERENCE   9  (residues 1 to 612)
  AUTHORS   Nakatsuru,S., Sudo,K. and Nakamura,Y.
  TITLE     Isolation and mapping of a human gene (MCM2) encoding a product
            homologous to yeast proteins involved in DNA replication
  JOURNAL   Cytogenet Cell Genet 68 (3-4), 226-230 (1995)
   PUBMED   7842741
REFERENCE   10 (residues 1 to 612)
  AUTHORS   Hu,B., Burkhart,R., Schulte,D., Musahl,C. and Knippers,R.
  TITLE     The P1 family: a new class of nuclear mammalian proteins related to
            the yeast Mcm replication proteins
  JOURNAL   Nucleic Acids Res 21 (23), 5289-5293 (1993)
   PUBMED   8265339
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073842.5.
            
            On or before Apr 29, 2025 this sequence version replaced
            XP_005250405.1, XP_054214227.1.
            
            Summary: The protein encoded by this gene is one of the highly
            conserved mini-chromosome maintenance proteins (MCM) that are
            essential for the initiation of eukaryotic genome replication. The
            hexameric protein complex formed by the MCM proteins is a key
            component of the pre-replication complex (pre_RC) and may be
            involved in the formation of replication forks and in the
            recruitment of other DNA replication related proteins. The MCM
            complex consisting of this protein and MCM2, 4 and 6 proteins
            possesses DNA helicase activity, and may act as a DNA unwinding
            enzyme. Cyclin D1-dependent kinase, CDK4, is found to associate
            with this protein, and may regulate the binding of this protein
            with the tumorsuppressor protein RB1/RB. Alternatively spliced
            transcript variants encoding distinct isoforms have been reported.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853561.26327.1,
                                           SRR11853558.22251.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..612
                     /product="DNA replication licensing factor MCM7 isoform 3"
                     /EC_number="3.6.4.12"
                     /note="minichromosome maintenance deficient 7; DNA
                     replication licensing factor MCM7; homolog of S.
                     cerevisiae Cdc47; CDC47 homolog; protein phosphatase 1,
                     regulatory subunit 104"
                     /calculated_mol_wt=68485
     Region          38..534
                     /region_name="MCM"
                     /note="minichromosome maintenance proteins; smart00350"
                     /db_xref="CDD:214631"
     Site            order(236,260..262,276,281..282,285,289,296,298,300,302,
                     305..306,313,316,319..320,322,324,331,339,342,345,349,
                     352..353,356,361..365,368..369,371..372,374,386..387,403,
                     406,416,418,420,423..424,427,430..431,434..435,437,449,
                     465..468,471,475,478..479,482..483,495..497,503)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:350664"
     Site            order(236..238,276..282,407,430,497)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350664"
     Site            order(305,364..365)
                     /site_type="other"
                     /note="nucleic acid binding site [nucleotide binding]"
                     /db_xref="CDD:350664"
     CDS             1..612
                     /gene="MCM7"
                     /gene_synonym="CDC47; MCM2; P1.1-MCM3; P1CDC47; P85MCM;
                     PNAS146; PPP1R104"
                     /coded_by="NM_001439271.1:608..2446"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:4176"
                     /db_xref="HGNC:HGNC:6950"
                     /db_xref="MIM:600592"
ORIGIN      
        1 mmeqrsrdpg mvrspqnqyp aelmrrfely fqgpssnkpr virevradsv gklvtvrgiv
       61 trvsevkpkm vvatytcdqc gaetyqpiqs ptfmplimcp sqecqtnrsg grlylqtrgs
      121 rfikfqemkm qehsdqvpvg niprsitvlv egentriaqp gdhvsvtgif lpilrtgfrq
      181 vvqgllsety leahrivkmn kseddesgag eltreelrqi aeedfyekla asiapeiygh
      241 edvkkallll lvggvdqspr gmkirgnini clmgdpgvak sqllsyidrl aprsqyttgr
      301 gssgvgltaa vlrdsvsgel tleggalvla dqgvccidef dkmaeadrta ihevmeqqti
      361 siakagiltt lnarcsilaa anpaygrynp rrsleqniql paallsrfdl lwliqdrpdr
      421 dndlrlaqhi tyvhqhsrqp psqfepldmk lmrryiamcr ekqpmvpesl adyitaayve
      481 mrreawaskd atytsartll ailrlstala rlrmvdvvek edvneairlm emskdsllgd
      541 kgqtartqrp advifatvre lvsggrsvrf seaeqrcvsr gftpaqfqaa ldeyeelnvw
      601 qvnasrtrit fv
//
LOCUS       NP_001394401            2459 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform s [Homo sapiens].
ACCESSION   NP_001394401
VERSION     NP_001394401.1
DBSOURCE    REFSEQ: accession NM_001407472.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2459)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2459)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2459)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2459)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2459)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2459)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2459)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2459)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2459)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2459)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.791950.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2161674, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2459
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2459
                     /product="adenomatous polyposis coli protein isoform s"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=268202
     Region          <24..82
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          81..124
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(115,119,123,158,162,166,202,206,210)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          128..169
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          132..169
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          176..211
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          219..260
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          265..305
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          269..303
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          307..347
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          311..347
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          348..635
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          652..751
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          873..>890
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          899..984
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <919..1317
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          987..1009
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1253..1276
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1278..1331
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1332..1353
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1362..1455
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1489..1563
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1649..1668
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1839..2184
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2286..2459
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2459
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407472.1:1439..8818"
                     /note="isoform s is encoded by transcript variant 35"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 mdhetasvls sssthsaprr ltshlgtkir aycetcwewq eahepgmdqd knpmpapveh
       61 qicpavcvlm klsfdeehrh amnelgglqa iaellqvdce mygltndhys itlrryagma
      121 ltnltfgdva nkatlcsmkg cmralvaqlk sesedlqqvi asvlrnlswr advnskktlr
      181 evgsvkalme calevkkest lksvlsalwn lsahctenka dicavdgala flvgtltyrs
      241 qtntlaiies gggilrnvss liatnedhrq ilrennclqt llqhlkshsl tivsnacgtl
      301 wnlsarnpkd qealwdmgav smlknlihsk hkmiamgsaa alrnlmanrp akykdanims
      361 pgsslpslhv rkqkaleael daqhlsetfd nidnlspkas hrskqrhkqs lygdyvfdtn
      421 rhddnrsdnf ntgnmtvlsp ylnttvlpss sssrgsldss rsekdrsler ergiglgnyh
      481 patenpgtss krglqistta aqiakvmeev saihtsqedr ssgsttelhc vtdernalrr
      541 ssaahthsnt ynftksensn rtcsmpyakl eykrssndsl nsvsssdgyg krgqmkpsie
      601 syseddeskf csygqypadl ahkihsanhm ddndgeldtp inyslkysde qlnsgrqsps
      661 qnerwarpkh iiedeikqse qrqsrnqstt ypvytestdd khlkfqphfg qqecvspyrs
      721 rgangsetnr vgsnhginqn vsqslcqedd yeddkptnys eryseeeqhe eeerptnysi
      781 kyneekrhvd qpidyslkya tdipssqkqs fsfsksssgq ssktehmsss sentstpssn
      841 akrqnqlhps saqsrsgqpq kaatckvssi nqetiqtycv edtpicfsrc sslsslssae
      901 deigcnqttq eadsantlqi aeikekigtr saedpvsevp avsqhprtks srlqgsslss
      961 esarhkavef ssgakspsks gaqtpksppe hyvqetplmf srctsvssld sfesrsiass
     1021 vqsepcsgmv sgiispsdlp dspgqtmpps rsktpppppq taqtkrevpk nkaptaekre
     1081 sgpkqaavna avqrvqvlpd adtllhfate stpdgfscss slsalsldep fiqkdvelri
     1141 mppvqendng neteseqpke snenqekeae ktidsekdll ddsddddiei leeciisamp
     1201 tkssrkakkp aqtasklppp varkpsqlpv ykllpsqnrl qpqkhvsftp gddmprvycv
     1261 egtpinfsta tslsdlties ppnelaageg vrggaqsgef ekrdtipteg rstdeaqggk
     1321 tssvtipeld dnkaeegdil aecinsampk gkshkpfrvk kimdqvqqas asssapnknq
     1381 ldgkkkkpts pvkpipqnte yrtrvrknad sknnlnaerv fsdnkdskkq nlknnskvfn
     1441 dklpnnedrv rgsfafdsph hytpiegtpy cfsrndslss ldfddddvdl srekaelrka
     1501 kenkeseakv tshteltsnq qsanktqaia kqpinrgqpk pilqkqstfp qsskdipdrg
     1561 aatdeklqnf aientpvcfs hnsslsslsd idqennnken epiketeppd sqgepskpqa
     1621 sgyapksfhv edtpvcfsrn sslsslsids eddllqecis sampkkkkps rlkgdnekhs
     1681 prnmggilge dltldlkdiq rpdsehglsp dsenfdwkai qegansivss lhqaaaaacl
     1741 srqassdsds ilslksgisl gspfhltpdq eekpftsnkg prilkpgeks tletkkiese
     1801 skgikggkkv ykslitgkvr snseisgqmk qplqanmpsi srgrtmihip gvrnssssts
     1861 pvskkgpplk tpaskspseg qtattsprga kpsvkselsp varqtsqigg sskapsrsgs
     1921 rdstpsrpaq qplsrpiqsp grnsispgrn gisppnklsq lprtsspsta stkssgsgkm
     1981 sytspgrqms qqnltkqtgl sknassiprs esaskglnqm nngngankkv elsrmsstks
     2041 sgsesdrser pvlvrqstfi keapsptlrr kleesasfes lspssrpasp trsqaqtpvl
     2101 spslpdmsls thssvqaggw rklppnlspt ieyndgrpak rhdiarshse spsrlpinrs
     2161 gtwkrehskh ssslprvstw rrtgssssil sassesseka ksedekhvns isgtkqsken
     2221 qvsakgtwrk ikenefsptn stsqtvssga tngaesktli yqmapavskt edvwvriedc
     2281 pinnprsgrs ptgntppvid svsekanpni kdskdnqakq nvgngsvpmr tvglenrlns
     2341 fiqvdapdqk gteikpgqnn pvpvsetnes sivertpfss sssskhssps gtvaarvtpf
     2401 nynpsprkss adstsarpsq iptpvnnntk krdsktdste ssgtqspkrh sgsylvtsv
//
LOCUS       NP_001393558             813 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 16 [Homo sapiens].
ACCESSION   NP_001393558
VERSION     NP_001393558.1
DBSOURCE    REFSEQ: accession NM_001406629.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 813)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 813)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 813)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 813)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 813)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 813)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 813)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 813)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 813)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 813)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.418732.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..813
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..813
                     /product="hamartin isoform 16"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=90122
     Region          <1..368
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <357..>609
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..813
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406629.1:1208..3649"
                     /note="isoform 16 is encoded by transcript variant 43"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mvcgmttppt spgnvppdls hpyskvfgtt ggkgtplgtp atspppaplc hsddyvhisl
       61 pqatvtpprk eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed
      121 siekdkeeaa isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv
      181 npeplhssld klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp
      241 trvgfgsgqp ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr
      301 liqqgadahs kelnklplps ksvdwthfgg sppsdeirtl rdqllllhnq llyerfkrqq
      361 halrnrrllr kvikaaalee hnaamkdqlk lqekdiqmwk vslqkeqary nqlqeqrdtm
      421 vtklhsqirq lqhdreefyn qsqelqtkle dcrnmiaelr ielkkannkv chtelllsqv
      481 sqklsnsesv qqqmeflnrq llvlgevnel yleqlqnkhs dttkevemmk aayrkelekn
      541 rshvlqqtqr ldtsqkrile leshlakkdh llleqkkyle dvklqargql qaaesryeaq
      601 kritqvfele ildlygrlek dgllkkleee kaeaaeaaee rldccndgcs dsmvghneea
      661 sghngetktp rpssargssg srggggssss sselstpekp phqragpfss rwettmgeas
      721 asipttvgsl pssksflgmk arelfrnkse sqcdedgmts slseslktel gkdlgveaki
      781 plnldgphps pptpdsvgql himdynethh ehs
//
LOCUS       NP_001425832             336 aa            linear   PRI 21-NOV-2025
DEFINITION  STAM-binding protein isoform 5 [Homo sapiens].
ACCESSION   NP_001425832 XP_047298929 XP_054196185
VERSION     NP_001425832.1
DBSOURCE    REFSEQ: accession NM_001438903.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Zhang,W., Xu,Z., Du,Y., Liu,T., Xiong,Z., Hu,J., Chen,L., Peng,X.
            and Zhou,F.
  TITLE     Identification of STAM-binding protein as a target for the
            treatment of gemcitabine resistance pancreatic cancer in a
            nutrient-poor microenvironment
  JOURNAL   Cell Death Dis 15 (9), 657 (2024)
   PUBMED   39242557
  REMARK    GeneRIF: Identification of STAM-binding protein as a target for the
            treatment of gemcitabine resistance pancreatic cancer in a
            nutrient-poor microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Li,L., Yang,X., He,M., Xu,X., Xuan,X., Zhang,J., Zhang,L., Xu,H.
            and Li,D.
  TITLE     The expression and clinical significance of STAMBP in breast cancer
  JOURNAL   Mol Biol Rep 50 (1), 899-906 (2023)
   PUBMED   36309616
  REMARK    GeneRIF: The expression and clinical significance of STAMBP in
            breast cancer.
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Yang,Q., Yan,D., Zou,C., Xue,Q., Lin,S., Huang,Q., Li,X., Tang,D.,
            Chen,X. and Liu,J.
  TITLE     The deubiquitinating enzyme STAMBP is a newly discovered driver of
            triple-negative breast cancer progression that maintains RAI14
            protein stability
  JOURNAL   Exp Mol Med 54 (11), 2047-2059 (2022)
   PUBMED   36434041
  REMARK    GeneRIF: The deubiquitinating enzyme STAMBP is a newly discovered
            driver of triple-negative breast cancer progression that maintains
            RAI14 protein stability.
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Yu,S., E,C. and Yang,J.
  TITLE     STAM binding protein regulated by hsa_circ_0007334 exerts oncogenic
            potential in pancreatic cancer
  JOURNAL   Pancreatology 22 (7), 1003-1012 (2022)
   PUBMED   36089485
  REMARK    GeneRIF: STAM binding protein regulated by hsa_circ_0007334 exerts
            oncogenic potential in pancreatic cancer.
REFERENCE   6  (residues 1 to 336)
  AUTHORS   Itoh,F., Asao,H., Sugamura,K., Heldin,C.H., ten Dijke,P. and
            Itoh,S.
  TITLE     Promoting bone morphogenetic protein signaling through negative
            regulation of inhibitory Smads
  JOURNAL   EMBO J 20 (15), 4132-4142 (2001)
   PUBMED   11483516
REFERENCE   7  (residues 1 to 336)
  AUTHORS   Endo,K., Takeshita,T., Kasai,H., Sasaki,Y., Tanaka,N., Asao,H.,
            Kikuchi,K., Yamada,M., Chenb,M., O'Shea,J.J. and Sugamura,K.
  TITLE     STAM2, a new member of the STAM family, binding to the Janus
            kinases
  JOURNAL   FEBS Lett 477 (1-2), 55-61 (2000)
   PUBMED   10899310
REFERENCE   8  (residues 1 to 336)
  AUTHORS   Tanaka,N., Kaneko,K., Asao,H., Kasai,H., Endo,Y., Fujita,T.,
            Takeshita,T. and Sugamura,K.
  TITLE     Possible involvement of a novel STAM-associated molecule 'AMSH' in
            intracellular signal transduction mediated by cytokines
  JOURNAL   J Biol Chem 274 (27), 19129-19135 (1999)
   PUBMED   10383417
REFERENCE   9  (residues 1 to 336)
  AUTHORS   Asada,H., Ishii,N., Sasaki,Y., Endo,K., Kasai,H., Tanaka,N.,
            Takeshita,T., Tsuchiya,S., Konno,T. and Sugamura,K.
  TITLE     Grf40, A novel Grb2 family member, is involved in T cell signaling
            through interaction with SLP-76 and LAT
  JOURNAL   J Exp Med 189 (9), 1383-1390 (1999)
   PUBMED   10224278
REFERENCE   10 (residues 1 to 336)
  AUTHORS   Carter,M.T., Mirzaa,G., McDonell,L.M. and Boycott,K.M.
  TITLE     Microcephaly-Capillary Malformation Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24354023
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073046.7.
            
            On or before Apr 25, 2025 this sequence version replaced
            XP_047298929.1, XP_054196185.1.
            
            Summary: Cytokine-mediated signal transduction in the JAK-STAT
            cascade requires the involvement of adaptor molecules. One such
            signal-transducing adaptor molecule contains an SH3 domain that is
            required for induction of MYC and cell growth. The protein encoded
            by this gene binds to the SH3 domain of the signal-transducing
            adaptor molecule, and plays a critical role in cytokine-mediated
            signaling for MYC induction and cell cycle progression. Multiple
            alternatively spliced transcript variants encoding the same protein
            isoform have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14243140.9535107.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..336
                     /product="STAM-binding protein isoform 5"
                     /EC_number="3.1.2.15"
                     /note="associated molecule with the SH3 domain of STAM;
                     endosome-associated ubiquitin isopeptidase; testicular
                     secretory protein Li 54"
                     /calculated_mol_wt=38074
     Region          1..127
                     /region_name="Interaction with CHMP3.
                     /evidence=ECO:0000269|PubMed:17146056"
                     /note="propagated from UniProtKB/Swiss-Prot (O95630.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          13..117
                     /region_name="USP8_dimer"
                     /note="USP8 dimerization domain; pfam08969"
                     /db_xref="CDD:462647"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          227..231
                     /region_name="Interaction with STAM.
                     /evidence=ECO:0000269|PubMed:10383417"
                     /note="propagated from UniProtKB/Swiss-Prot (O95630.1)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          254..>335
                     /region_name="MPN"
                     /note="Mpr1p, Pad1p N-terminal (MPN) domains; cl13996"
                     /db_xref="CDD:472685"
     Site            280
                     /site_type="other"
                     /note="Indirect zinc-binding.
                     /evidence=ECO:0000250|UniProtKB:Q96FJ0; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     CDS             1..336
                     /gene="STAMBP"
                     /gene_synonym="AMSH; MICCAP"
                     /coded_by="NM_001438903.1:123..1133"
                     /note="isoform 5 is encoded by transcript variant 21"
                     /db_xref="GeneID:10617"
                     /db_xref="HGNC:HGNC:16950"
                     /db_xref="MIM:606247"
ORIGIN      
        1 msdhgdvslp pedrvralsq lgsavevned ipprryfrsg veiirmasiy seegniehaf
       61 ilynkyitlf ieklpkhrdy ksavipekkd tvkklkeiaf pkaeelkael lkrytkeyte
      121 yneekkkeae elarnmaiqq elekekqrva qqkqqqleqe qfhafeemir nqelekerlk
      181 ivqefgkvdp glggplvpdl ekpsldvfpt ltvssiqpsd chttvrpakp pvvdrslkpg
      241 alsnsesipt idglrhvvvp grlcpqflql asantargve tcgilcgklm rneftithvl
      301 ipkqsagsdy cnteneeelf liqdqqglit lgwiha
//
LOCUS       NP_001427618             210 aa            linear   PRI 21-NOV-2025
DEFINITION  dual specificity mitogen-activated protein kinase kinase 2 isoform
            3 [Homo sapiens].
ACCESSION   NP_001427618 XP_047295056 XP_054177440
VERSION     NP_001427618.1
DBSOURCE    REFSEQ: accession NM_001440689.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Wan,Y., Zhao,Y., Cao,M., Wang,J., Tran,S.V., Song,Z., Hsueh,B.W.
            and Wang,S.E.
  TITLE     Lung Fibroblasts Take up Breast Cancer Cell-derived Extracellular
            Vesicles Partially Through MEK2-dependent Macropinocytosis
  JOURNAL   Cancer Res Commun 4 (1), 170-181 (2024)
   PUBMED   38259097
  REMARK    GeneRIF: Lung Fibroblasts Take up Breast Cancer Cell-derived
            Extracellular Vesicles Partially Through MEK2-dependent
            Macropinocytosis.
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Gong,K.Q., Mikacenic,C., Long,M.E., Frevert,C.W., Birkland,T.P.,
            Charron,J., Gharib,S.A. and Manicone,A.M.
  TITLE     MAP2K2 Delays Recovery in Murine Models of Acute Lung Injury and
            Associates with Acute Respiratory Distress Syndrome Outcome
  JOURNAL   Am J Respir Cell Mol Biol 66 (5), 555-563 (2022)
   PUBMED   35157553
  REMARK    GeneRIF: MAP2K2 Delays Recovery in Murine Models of Acute Lung
            Injury and Associates with Acute Respiratory Distress Syndrome
            Outcome.
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 210)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   7  (residues 1 to 210)
  AUTHORS   Derijard,B., Raingeaud,J., Barrett,T., Wu,I.H., Han,J.,
            Ulevitch,R.J. and Davis,R.J.
  TITLE     Independent human MAP-kinase signal transduction pathways defined
            by MEK and MKK isoforms
  JOURNAL   Science 267 (5198), 682-685 (1995)
   PUBMED   7839144
  REMARK    Erratum:[Science 1995 Jul 7;269(5220):17]
REFERENCE   8  (residues 1 to 210)
  AUTHORS   Alessi,D.R., Saito,Y., Campbell,D.G., Cohen,P., Sithanandam,G.,
            Rapp,U., Ashworth,A., Marshall,C.J. and Cowley,S.
  TITLE     Identification of the sites in MAP kinase kinase-1 phosphorylated
            by p74raf-1
  JOURNAL   EMBO J 13 (7), 1610-1619 (1994)
   PUBMED   8157000
REFERENCE   9  (residues 1 to 210)
  AUTHORS   Charest,D.L., Mordret,G., Harder,K.W., Jirik,F. and Pelech,S.L.
  TITLE     Molecular cloning, expression, and characterization of the human
            mitogen-activated protein kinase p44erk1
  JOURNAL   Mol Cell Biol 13 (8), 4679-4690 (1993)
   PUBMED   7687743
REFERENCE   10 (residues 1 to 210)
  AUTHORS   Rauen,K.A.
  TITLE     Cardiofaciocutaneous Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301365
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016586.9.
            
            On or before May 23, 2025 this sequence version replaced
            XP_047295056.1, XP_054177440.1.
            
            Summary: The protein encoded by this gene is a dual specificity
            protein kinase that belongs to the MAP kinase kinase family. This
            kinase is known to play a critical role in mitogen growth factor
            signal transduction. It phosphorylates and thus activates
            MAPK1/ERK2 and MAPK2/ERK3. The activation of this kinase itself is
            dependent on the Ser/Thr phosphorylation by MAP kinase kinase
            kinases. Mutations in this gene cause cardiofaciocutaneous syndrome
            (CFC syndrome), a disease characterized by heart defects, cognitive
            disability, and distinctive facial features similar to those found
            in Noonan syndrome. The inhibition or degradation of this kinase is
            also found to be involved in the pathogenesis of Yersinia and
            anthrax. A pseudogene, which is located on chromosome 7, has been
            identified for this gene. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279839.914.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..210
                     /product="dual specificity mitogen-activated protein
                     kinase kinase 2 isoform 3"
                     /EC_number="2.7.12.2"
                     /note="MAP kinase kinase 2; MAPK/ERK kinase 2; dual
                     specificity mitogen-activated protein kinase kinase 2; ERK
                     activator kinase 2; mitogen-activated protein kinase
                     kinase 2, p45"
                     /calculated_mol_wt=23163
     Region          <1..206
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     CDS             1..210
                     /gene="MAP2K2"
                     /gene_synonym="CFC4; MAPKK2; MEK2; MKK2; PRKMK2"
                     /coded_by="NM_001440689.1:511..1143"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:5605"
                     /db_xref="HGNC:HGNC:6842"
                     /db_xref="MIM:601263"
ORIGIN      
        1 mhrdvkpsni lvnsrgeikl cdfgvsgqli dsmansfvgt rsymaperlq gthysvqsdi
       61 wsmglslvel avgrypippp dakeleaifg rpvvdgeege phsisprprp pgrpvsghgm
      121 dsrpamaife lldyivnepp pklpngvftp dfqefvnkcl iknpaeradl kmltnhtfik
      181 rseveevdfa gwlcktlrln qpgtptrtav
//
LOCUS       NP_001393912             664 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform A [Homo sapiens].
ACCESSION   NP_001393912
VERSION     NP_001393912.1
DBSOURCE    REFSEQ: accession NM_001406983.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 664)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 664)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 664)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 664)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 664)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 664)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 664)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 664)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355388.30 and AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3588445.1,
                                           SRR14038193.3664413.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155371 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..664
                     /product="lamin isoform A"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=74009
     mat_peptide     1..661
                     /product="Prelamin-A/C. /id=PRO_0000398835"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
                     /calculated_mol_wt=73808
     mat_peptide     1..646
                     /product="Lamin-A/C. /id=PRO_0000063810"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
                     /calculated_mol_wt=72225
     Region          1..130
                     /region_name="Interaction with MLIP.
                     /evidence=ECO:0000269|PubMed:21498514"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          1..33
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          30..386
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Site            32
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          34..70
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          71..80
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            78
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          81..218
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            108
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            114
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            123
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            135
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            155
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            171
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            180
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            201
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            208
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          219..242
                     /region_name="Linker 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          243..383
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          259..331
                     /region_name="Necessary and sufficient for the interaction
                     with IFFO1. /evidence=ECO:0000269|PubMed:31548606"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            265
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            266
                     /site_type="other"
                     /note="Heptad change of phase; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            270
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATR.
                     /evidence=ECO:0000269|PubMed:37832547; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            311
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            316
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            325
                     /site_type="other"
                     /note="Stutter. /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            330
                     /site_type="other"
                     /note="Heptad change of phase; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            341
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          384..664
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          384..442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:37788673,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATR.
                     /evidence=ECO:0000269|PubMed:37788673,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:24741066, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          417..422
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            417
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          434..541
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     Site            450
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            457
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            486
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48679; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48679; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            546
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          552..576
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          598..619
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            625
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:26237509; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            628
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:26237509; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            632
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            646..647
                     /site_type="cleavage"
                     /note="Cleavage, by endoprotease; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            661
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000269|PubMed:8175923,
                     ECO:0000269|PubMed:9030603; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     CDS             1..664
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406983.1:535..2529"
                     /note="isoform A is encoded by transcript variant 8"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 metpsqrrat rsgaqasstp lsptritrlq ekedlqelnd rlavyidrvr sletenaglr
       61 lriteseevv srevsgikaa yeaelgdark tldsvakera rlqlelskvr eefkelkarn
      121 tkkegdliaa qarlkdleal lnskeaalst alsekrtleg elhdlrgqva kleaalgeak
      181 kqlqdemlrr vdaenrlqtm keeldfqkni yseelretkr rhetrlveid ngkqrefesr
      241 ladalqelra qhedqveqyk kelektysak ldnarqsaer nsnlvgaahe elqqsririd
      301 slsaqlsqlq kqlaakeakl rdledslare rdtsrrllae keremaemra rmqqqldeyq
      361 elldiklald meihayrkll egeeerlrls psptsqrsrg rasshssqtq gggsvtkkrk
      421 lestesrssf sqhartsgrv aveevdeegk fvrlrnksne dqsmgnwqik rqngddpllt
      481 yrfppkftlk agqvvtiwaa gagathsppt dlvwkaqntw gcgnslrtal instgeevam
      541 rklvrsvtvv eddededgdd llhhhhgshc sssgdpaeyn lrsrtvlcgt cgqpadkasa
      601 sgsgaqvggp issgssassv tvtrsyrsvg gsgggsfgdn lvtrsyllgn ssprtqspqn
      661 csim
//
LOCUS       NP_001424915             617 aa            linear   PRI 21-NOV-2025
DEFINITION  nuclear protein localization protein 4 homolog isoform 3 [Homo
            sapiens].
ACCESSION   NP_001424915 XP_011523281 XP_054172603
VERSION     NP_001424915.1
DBSOURCE    REFSEQ: accession NM_001437986.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Bekkari,H., Benmakhlouf,Y., Nourouti,N.G., Barakat,A. and
            Mechita,M.B.
  TITLE     Study of Clinical Characteristics of Intellectual Disability in
            Morocco
  JOURNAL   Innov Clin Neurosci 21 (7-9), 10-14 (2024)
   PUBMED   39329031
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Wang,N., Zhu,D., Liu,Y., Wu,J., Wang,M., Jin,S., Fu,F., Li,B.,
            Ji,H., Du,C. and Zheng,Z.
  TITLE     NPLOC4 is a potential target and a poor prognostic signature in
            lung squamous cell carcinoma
  JOURNAL   Sci Rep 13 (1), 20430 (2023)
   PUBMED   37993584
  REMARK    GeneRIF: NPLOC4 is a potential target and a poor prognostic
            signature in lung squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 617)
  AUTHORS   Tsioras,K., Smith,K.C., Edassery,S.L., Garjani,M., Li,Y.,
            Williams,C., McKenna,E.D., Guo,W., Wilen,A.P., Hark,T.J.,
            Marklund,S.L., Ostrow,L.W., Gilthorpe,J.D., Ichida,J.K., Kalb,R.G.,
            Savas,J.N. and Kiskinis,E.
  TITLE     Analysis of proteome-wide degradation dynamics in ALS SOD1
            iPSC-derived patient neurons reveals disrupted VCP homeostasis
  JOURNAL   Cell Rep 42 (10), 113160 (2023)
   PUBMED   37776851
REFERENCE   4  (residues 1 to 617)
  AUTHORS   Nguyen,T.Q., My Le,L.T., Kim,D.H., Ko,K.S., Lee,H.T., Kim
            Nguyen,Y.T., Kim,H.S., Han,B.W., Kang,W. and Yang,J.K.
  TITLE     Structural basis for the interaction between human Npl4 and
            Npl4-binding motif of human Ufd1
  JOURNAL   Structure 30 (11), 1530-1537 (2022)
   PUBMED   36087575
  REMARK    GeneRIF: Structural basis for the interaction between human Npl4
            and Npl4-binding motif of human Ufd1.
REFERENCE   5  (residues 1 to 617)
  AUTHORS   Fujisawa,R., Polo Rivera,C. and Labib,K.P.M.
  TITLE     Multiple UBX proteins reduce the ubiquitin threshold of the
            mammalian p97-UFD1-NPL4 unfoldase
  JOURNAL   Elife 11, e76763 (2022)
   PUBMED   35920641
  REMARK    GeneRIF: Multiple UBX proteins reduce the ubiquitin threshold of
            the mammalian p97-UFD1-NPL4 unfoldase.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 617)
  AUTHORS   McConnell,E., Lass,A. and Wojcik,C.
  TITLE     Ufd1-Npl4 is a negative regulator of cholera toxin
            retrotranslocation
  JOURNAL   Biochem Biophys Res Commun 355 (4), 1087-1090 (2007)
   PUBMED   17331469
  REMARK    GeneRIF: Ufd1-Npl4 is a negative regulator of retrotranslocation,
            delaying the retrotranslocation of endoplasmic reticulum-associated
            degradation substrates independently of its association with VCP
REFERENCE   7  (residues 1 to 617)
  AUTHORS   Arrigoni,R., Alam,S.L., Wamstad,J.A., Bardwell,V.J., Sundquist,W.I.
            and Schreiber-Agus,N.
  TITLE     The Polycomb-associated protein Rybp is a ubiquitin binding protein
  JOURNAL   FEBS Lett 580 (26), 6233-6241 (2006)
   PUBMED   17070805
  REMARK    Erratum:[FEBS Lett. 2006 Dec 11;580(28-29):6754]
REFERENCE   8  (residues 1 to 617)
  AUTHORS   Gevaert,K., Goethals,M., Martens,L., Van Damme,J., Staes,A.,
            Thomas,G.R. and Vandekerckhove,J.
  TITLE     Exploring proteomes and analyzing protein processing by mass
            spectrometric identification of sorted N-terminal peptides
  JOURNAL   Nat Biotechnol 21 (5), 566-569 (2003)
   PUBMED   12665801
REFERENCE   9  (residues 1 to 617)
  AUTHORS   Botta,A., Tandoi,C., Fini,G., Calabrese,G., Dallapiccola,B. and
            Novelli,G.
  TITLE     Cloning and characterization of the gene encoding human NPL4, a
            protein interacting with the ubiquitin fusion-degradation protein
            (UFD1L)
  JOURNAL   Gene 275 (1), 39-46 (2001)
   PUBMED   11574150
REFERENCE   10 (residues 1 to 617)
  AUTHORS   Meyer,H.H., Shorter,J.G., Seemann,J., Pappin,D. and Warren,G.
  TITLE     A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to
            ubiquitin and nuclear transport pathways
  JOURNAL   EMBO J 19 (10), 2181-2192 (2000)
   PUBMED   10811609
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC139530.3 and AC137896.5.
            
            On or before Apr 14, 2025 this sequence version replaced
            XP_011523281.1, XP_054172603.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3334923.1,
                                           SRR7346977.2363242.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..617
                     /product="nuclear protein localization protein 4 homolog
                     isoform 3"
                     /note="nuclear protein localization protein 4 homolog;
                     nuclear protein localization 4 homolog; NPLOC4 ubiquitin
                     recognition factor"
                     /calculated_mol_wt=69330
     Region          1..80
                     /region_name="UN_NPL4"
                     /note="Nuclear pore localization protein NPL4; pfam11543"
                     /db_xref="CDD:431926"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q8TAT6.3)"
     Region          105..245
                     /region_name="zf-NPL4"
                     /note="NPL4 family, putative zinc binding region;
                     pfam05020"
                     /db_xref="CDD:461523"
     Site            179
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60670; propagated from
                     UniProtKB/Swiss-Prot (Q8TAT6.3)"
     Region          249..555
                     /region_name="NPL4"
                     /note="NPL4 family; pfam05021"
                     /db_xref="CDD:461524"
     CDS             1..617
                     /gene="NPLOC4"
                     /gene_synonym="NPL4"
                     /coded_by="NM_001437986.1:183..2036"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:55666"
                     /db_xref="HGNC:HGNC:18261"
                     /db_xref="MIM:606590"
ORIGIN      
        1 maesiiirvq spdgvkrita tkretaatfl kkvakefgfq nngfsvyinr nktgeitass
       61 nkslnllkik hgdllflfps slagpsseme tsvppgfkvf gapnvvedei dqylskqdgk
      121 iyrsrdpqlc rhgplgkcvh cvplepfded ylnhleppvk hmsfhayirk ltggadkgkf
      181 valeniscki ksgceghlpw pngictkcqp saitlnrqky rhvdnimfen htvadrfldf
      241 wrktgnqhfg ylygrytehk diplgiraev aaiyeppqig tqnslelled pkaevvdeia
      301 aklglrkvgw iftdlvsedt rkgtvrysrn kdtyflssee citagdfqnk hpnmcrlspd
      361 ghfgskfvta vatggpdnqv hfegyqvsnq cmalvrdecl lpckdapelg yakessseqy
      421 vpdvfykdvd kfgneitqla rplpveylii ditttfpkdp vytfsisqnp fpienrdvlg
      481 etqdfhslat ylsqntssvf ldtisdfhll lflvtnevmp lqdsisllle avrtrneela
      541 qtwkrseqwa tieqlcseyp hplprhpvag ageqptlhss plpvvpwiph paaswqvpsa
      601 mqrvetrppc qargrlr
//
LOCUS       NP_001400669             996 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform c [Homo sapiens].
ACCESSION   NP_001400669 XP_005253391
VERSION     NP_001400669.1
DBSOURCE    REFSEQ: accession NM_001413740.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 996)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 996)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 996)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 996)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 996)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 996)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 996)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 996)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 996)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 996)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            On Nov 8, 2022 this sequence version replaced XP_005253391.1.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1173594.1,
                                           SRR14038192.150198.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..996
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..996
                     /product="polyhomeotic-like protein 1 isoform c"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=104539
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          204..233
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          253..347
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          424..504
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          <466..662
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          548..581
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          628..664
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Site            637
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P78364.3)"
     Region          820..927
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          840..920
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Site            890
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P78364.3)"
     Site            914
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P78364.3)"
     Region          927..995
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(945..946,980..981,984..985,988)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(956..960,962..963,966..967,971,976)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..996
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413740.1:368..3358"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq asinlattsa aqlisrsqsv
      121 sspsattltq svllgnttsp plnqsqaqmy lrvnrtlgrn vplasqlilm pngavaavqq
      181 evpsaqspgv hadadqvqnl avrnqqasaq gpqmqgstqk aippgaspvs slsqassqal
      241 avaqassgat nqslnlsqag ggsgnsipgs mgpggggqah gglgqlpssg mgggscprkg
      301 tgvvqplpaa qtvtvsqgsq teaesaaakk aeadgsgqqn vgmnltrtat papsqtliss
      361 atytqiqphs liqqqqqihl qqkqvviqqq iaihhqqqfq hrqsqllhta thlqlaqqqq
      421 qqqqqqqqqq qpqattltap qppqvpptqq vppsqsqqqa qtlvvqpmlq ssplslppda
      481 apkppipiqs kppvapikpp qlgaakmsaa qqppphipvq vvgtrqpgta qaqalglaql
      541 aaavptsrgm pgtvqsgqah lassppssqa pgalqecppt lapgmtlapv qgtahvvkgg
      601 attsspvvaq vpaafymqsv hlpgkpqtla vkrkadseee rddvstlgsm lpakaspvae
      661 spkvmdekss lgekaesvan vnantpssel valtpapsvp pptlamvsrq mgdskppqai
      721 vkpqilthii egfviqegae pfpvgcsqll kesekplqtg lptgltenqs ggplgvdsps
      781 aeldkkanll kceycgkyap aeqfrgskrf csmtcakryn vscshqfrlk rkkmkefqea
      841 nyarvrrrgp rrsssdiara kiqgkchrgq edssrgsdns sydealspts pgplsvragh
      901 gerdlgnpnt apptpelhgi npvflssnps rwsveevyef iaslqgcqei aeefrsqeid
      961 gqallllkee hlmsamnikl gpalkicaki nvlket
//
LOCUS       NP_001428883             740 aa            linear   PRI 21-NOV-2025
DEFINITION  protein zyg-11 homolog B isoform 2 [Homo sapiens].
ACCESSION   NP_001428883 XP_006710961 XP_054194721
VERSION     NP_001428883.1
DBSOURCE    REFSEQ: accession NM_001441954.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Duan,B., Zhang,H., Zhu,Z., Yan,X., Ji,Z. and Li,J.
  TITLE     LncRNA LINC01871 sponging miR-142-3p to modulate ZYG11B promotes
            the chemoresistance of colorectal cancer cells by inducing
            autophagy
  JOURNAL   Anticancer Drugs 34 (7), 827-836 (2023)
   PUBMED   36847071
  REMARK    GeneRIF: LncRNA LINC01871 sponging miR-142-3p to modulate ZYG11B
            promotes the chemoresistance of colorectal cancer cells by inducing
            autophagy.
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Zhang,B., Li,Y., Feng,Q., Song,L., Dong,C. and Yan,X.
  TITLE     Structural insights into ORF10 recognition by ZYG11B
  JOURNAL   Biochem Biophys Res Commun 616, 14-18 (2022)
   PUBMED   35636250
  REMARK    GeneRIF: Structural insights into ORF10 recognition by ZYG11B.
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Fonseca,B.F. and Chakrabarti,L.A.
  TITLE     A close shave: How SARS-CoV-2 induces the loss of cilia
  JOURNAL   J Cell Biol 221 (7) (2022)
   PUBMED   35695891
  REMARK    GeneRIF: A close shave: How SARS-CoV-2 induces the loss of cilia.
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Yan,X., Li,Y., Wang,G., Zhou,Z., Song,G., Feng,Q., Zhao,Y., Mi,W.,
            Ma,Z. and Dong,C.
  TITLE     Molecular basis for recognition of Gly/N-degrons by CRL2ZYG11B and
            CRL2ZER1
  JOURNAL   Mol Cell 81 (16), 3262-3274 (2021)
   PUBMED   34214466
  REMARK    GeneRIF: Molecular basis for recognition of Gly/N-degrons by
            CRL2(ZYG11B) and CRL2(ZER1).
REFERENCE   5  (residues 1 to 740)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 740)
  AUTHORS   Timms,R.T., Zhang,Z., Rhee,D.Y., Harper,J.W., Koren,I. and
            Elledge,S.J.
  TITLE     A glycine-specific N-degron pathway mediates the quality control of
            protein N-myristoylation
  JOURNAL   Science 365 (6448) (2019)
   PUBMED   31273098
REFERENCE   7  (residues 1 to 740)
  AUTHORS   Balachandran,R.S., Heighington,C.S., Starostina,N.G.,
            Anderson,J.W., Owen,D.L., Vasudevan,S. and Kipreos,E.T.
  TITLE     The ubiquitin ligase CRL2ZYG11 targets cyclin B1 for degradation in
            a conserved pathway that facilitates mitotic slippage
  JOURNAL   J Cell Biol 215 (2), 151-166 (2016)
   PUBMED   27810909
  REMARK    GeneRIF: the ubiquitin ligase CRL2(ZYG-11) redundantly targets the
            degradation of cyclin B1 in Caenorhabditis elegans and human cells.
REFERENCE   8  (residues 1 to 740)
  AUTHORS   Okumura,F., Matsuzaki,M., Nakatsukasa,K. and Kamura,T.
  TITLE     The Role of Elongin BC-Containing Ubiquitin Ligases
  JOURNAL   Front Oncol 2, 10 (2012)
   PUBMED   22649776
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 740)
  AUTHORS   Bennett,E.J., Rush,J., Gygi,S.P. and Harper,J.W.
  TITLE     Dynamics of cullin-RING ubiquitin ligase network revealed by
            systematic quantitative proteomics
  JOURNAL   Cell 143 (6), 951-965 (2010)
   PUBMED   21145461
REFERENCE   10 (residues 1 to 740)
  AUTHORS   Vasudevan,S., Starostina,N.G. and Kipreos,E.T.
  TITLE     The Caenorhabditis elegans cell-cycle regulator ZYG-11 defines a
            conserved family of CUL-2 complex components
  JOURNAL   EMBO Rep 8 (3), 279-286 (2007)
   PUBMED   17304241
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099784.2 and AL139255.9.
            
            On or before Jul 14, 2025 this sequence version replaced
            XP_006710961.1, XP_054194721.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.222804.1,
                                           SRR14038191.637719.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..740
                     /product="protein zyg-11 homolog B isoform 2"
                     /note="protein zyg-11 homolog B"
                     /calculated_mol_wt=83637
     Region          103..132
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          <124..>271
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          134..159
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          160..178
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          184..209
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          210..234
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          235..263
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          264..289
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..740
                     /gene="ZYG11B"
                     /gene_synonym="ZYG11"
                     /coded_by="NM_001441954.1:332..2554"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:79699"
                     /db_xref="HGNC:HGNC:25820"
                     /db_xref="MIM:618673"
ORIGIN      
        1 mrhhtweeas pyslldicln fltthlekfc sarqdgtlcl qepgvfpqev adrllrtmaf
       61 hgllndgtvg ifrgnqmrlk racirkakis avafrkafch hklveldatg vnadititdi
      121 isglgsnkwi qqnlqclvln sltlsledpy ercfsrlsgl ralsitnvlf ynedlaevas
      181 lprlesldis ntsitdital lackdrlksl tmhhlkclkm tttqildvvr elkhlnhldi
      241 sddkqftsdi alrlleqkdi lpnlvsldvs grkhvtdkav eafiqqrpsm qfvgllatda
      301 gysefltgeg hlkvsgeane tqiaealkry seraffvrea lfhlfslthv mektkpeilk
      361 lvvtgmrnhp mnlpvqlaas acvfnltkqd laagmpvrll advthlllka mehfpnhqql
      421 qkncllslcs drilqdvpfn rfeaaklvmq wlcnhedqnm qrmavaiisi laaklsteqt
      481 aqlgtelfiv rqllqivkqk tnqnsvdttl kftlsalwnl tdespttcrh fienqglelf
      541 mrvlesfpte ssiqqkvlgl lnniaevqel hselmwkdfi dhissllhsv evevsyfaag
      601 iiahlisrge qawtlsrsqr nsllddlhsa ilkwptpece mvayrsfnpf fpllgcfttp
      661 gvqlwavwam qhvcsknpsr ycsmlieegg lqhlynikdh ehtdphvqqi availdslek
      721 hivrhgrppp ckkqpqarln
//
LOCUS       NP_001428096             688 aa            linear   PRI 21-NOV-2025
DEFINITION  PHD finger protein 21A isoform e [Homo sapiens].
ACCESSION   NP_001428096 XP_011518459 XP_054225037
VERSION     NP_001428096.1
DBSOURCE    REFSEQ: accession NM_001441167.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Mustafa,S., Abbas,S., Mahmood,A., Khan,A.Z., Zeb,S., Khan,A. and
            Umair,M.
  TITLE     A novel de novo variant in the PHF21A causes craniofacial
            abnormalities, intellectual disability and skeletal manifestations
  JOURNAL   Clin Genet 104 (1), 142-144 (2023)
   PUBMED   36843358
  REMARK    GeneRIF: A novel de novo variant in the PHF21A causes craniofacial
            abnormalities, intellectual disability and skeletal manifestations.
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Huang,J.Q., Ji,L.C., Jing,Q.A., He,Y.C., Ma,Y.Y. and Tong,X.M.
  TITLE     PHF21A expression as a biomarker of hepatocellular carcinoma
            progression and prognosis
  JOURNAL   Neoplasma 69 (6), 1349-1358 (2022)
   PUBMED   36305691
  REMARK    GeneRIF: PHF21A expression as a biomarker of hepatocellular
            carcinoma progression and prognosis.
REFERENCE   4  (residues 1 to 688)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 688)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 688)
  AUTHORS   Hailesellasse Sene,K., Porter,C.J., Palidwor,G., Perez-Iratxeta,C.,
            Muro,E.M., Campbell,P.A., Rudnicki,M.A. and Andrade-Navarro,M.A.
  TITLE     Gene function in early mouse embryonic stem cell differentiation
  JOURNAL   BMC Genomics 8, 85 (2007)
   PUBMED   17394647
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 688)
  AUTHORS   Shi,Y.J., Matson,C., Lan,F., Iwase,S., Baba,T. and Shi,Y.
  TITLE     Regulation of LSD1 histone demethylase activity by its associated
            factors
  JOURNAL   Mol Cell 19 (6), 857-864 (2005)
   PUBMED   16140033
REFERENCE   8  (residues 1 to 688)
  AUTHORS   Iwase,S., Januma,A., Miyamoto,K., Shono,N., Honda,A., Yanagisawa,J.
            and Baba,T.
  TITLE     Characterization of BHC80 in BRAF-HDAC complex, involved in
            neuron-specific gene repression
  JOURNAL   Biochem Biophys Res Commun 322 (2), 601-608 (2004)
   PUBMED   15325272
  REMARK    GeneRIF: Presumably serves as a scaffold protein in BHC in neuronal
            as well as non-neuronal cells. Possible role in spermatogenesis.
REFERENCE   9  (residues 1 to 688)
  AUTHORS   Hakimi,M.A., Dong,Y., Lane,W.S., Speicher,D.W. and Shiekhattar,R.
  TITLE     A candidate X-linked mental retardation gene is a component of a
            new family of histone deacetylase-containing complexes
  JOURNAL   J Biol Chem 278 (9), 7234-7239 (2003)
   PUBMED   12493763
REFERENCE   10 (residues 1 to 688)
  AUTHORS   Hakimi,M.A., Bochar,D.A., Chenoweth,J., Lane,W.S., Mandel,G. and
            Shiekhattar,R.
  TITLE     A core-BRAF35 complex containing histone deacetylase mediates
            repression of neuronal-specific genes
  JOURNAL   Proc Natl Acad Sci U S A 99 (11), 7420-7425 (2002)
   PUBMED   12032298
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC024475.15 and AC068385.9.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_011518459.1, XP_054225037.1.
            
            Summary: The PHF21A gene encodes BHC80, a component of a BRAF35
            (MIM 605535)/histone deacetylase (HDAC; see MIM 601241) complex
            (BHC) that mediates repression of neuron-specific genes through the
            cis-regulatory element known as repressor element-1 (RE1) or neural
            restrictive silencer (NRS) (Hakimi et al., 2002 [PubMed
            12032298]).[supplied by OMIM, Nov 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.775095.1,
                                           SRR14038192.87542.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..688
                     /product="PHD finger protein 21A isoform e"
                     /note="BRAF35/HDAC2 complex (80 kDa); BHC80a; BRAF35-HDAC
                     complex protein BHC80"
                     /calculated_mol_wt=75701
     Region          89..125
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          326..371
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          <382..544
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          448..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96BD5.1)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          494..688
                     /region_name="Required for transcriptional repression"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          498..540
                     /region_name="PHD_PHF21A"
                     /note="PHD finger found in PHD finger protein 21A
                     (PHF21A); cd15523"
                     /db_xref="CDD:276998"
     Site            order(498,505..510,530..533,535)
                     /site_type="other"
                     /note="histone H3 binding site [polypeptide binding]"
                     /db_xref="CDD:276998"
     Region          647..688
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     CDS             1..688
                     /gene="PHF21A"
                     /gene_synonym="BHC80; BM-006; IDDBCS; NEDMS"
                     /coded_by="NM_001441167.1:645..2711"
                     /note="isoform e is encoded by transcript variant 13"
                     /db_xref="GeneID:51317"
                     /db_xref="HGNC:HGNC:24156"
                     /db_xref="MIM:608325"
ORIGIN      
        1 melqtlqeal kveiqvhqkl vaqmkqdpqi fflsnqnadl kkqlhelqak italsekqkr
       61 vveqlrknli vkqeqpdkfq iqplpqsenk lqtaqqqplq qlqqqqqyhh hhaqqsaaas
      121 pnltasqktv ttasmittkt lplvlkaata tmpasvvgqr ptiamvtain sqkavlstdv
      181 qntpvnlqts skvtgpgaea vqivakntvt lqvqatppqp ikvpqfippp rltprpnflp
      241 qvrpkpvaqn nipiapappp mlaapqliqr pvmltkftpt tlptsqnsih pvrvvngqta
      301 tiaktfpmaq ltsiviatpg trlagpqtvq lskpslekqt vkshtetdek qtesrtitpp
      361 aapkpkreen pqklafmvsl glvthdhlee iqskrqerkr rttanpvysg avfeperkks
      421 avtylnstmh pgtrkrgrpp kynavlgfga ltptspqssh pdspenekte ttftfpapvq
      481 pvslpsptst dgdihedfcs vcrksgqllm cdtcsrvyhl dcldpplkti pkgmwicprc
      541 qdqmlkkeea ipwpgtlaiv hsyiaykaak eeekqkllkw ssdlkqereq leqkvkqlsn
      601 siskcmemkn tilarqkemh sslekvkqli rlihgidlsk pvdseatvga isngpdctpp
      661 anaatstpap spssqsctan cnqgeetk
//
LOCUS       NP_001399999             333 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001399999
VERSION     NP_001399999.1
DBSOURCE    REFSEQ: accession NM_001413070.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3231799.1,
                                           SRR18074969.3074670.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..333
                     /product="mitochondrial fission regulator 1 isoform 1
                     precursor"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=31469
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=5550
     Region          22..251
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     mat_peptide     49..333
                     /product="Mitochondrial fission regulator 1.
                     /id=PRO_0000096622"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=31469
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15390.2)"
     Region          177..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          179..304
                     /region_name="Necessary and sufficient to promote
                     mitochondrial fission. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          288..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     CDS             1..333
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001413070.1:476..1477"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 20"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsvlwsrkpy gssrsivrki gtnlsliqcp rvqfqinsha
       61 tewspshpge davasfadvg wvakeegecs arlrtevrsr pplqddllff ekapsrqisl
      121 pdlsqeepql ktpalaneea lqkicalene laalraqiak ivtqqeqqnl tagdldsttf
      181 gtipphpppp ppplpppalg lhqstsavdl ikerrekran agktlvknnp kkpempnmle
      241 ilkemnsvkl rsvkrseqdv kpkpvdatdp aaliaealkk kfayryrsds qdevekgipk
      301 seseatserv lfgphmlkpt gkmkalienv sds
//
LOCUS       NP_001425383             542 aa            linear   PRI 21-NOV-2025
DEFINITION  excitatory amino acid transporter 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001425383 XP_005248399 XP_054209164
VERSION     NP_001425383.1
DBSOURCE    REFSEQ: accession NM_001438454.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Albury,C.L., Sutherland,H.G., Lam,A.W.Y., Tran,N.K., Lea,R.A.,
            Haupt,L.M. and Griffiths,L.R.
  TITLE     Identification of Polymorphisms in EAAT1 Glutamate Transporter Gene
            SLC1A3 Associated with Reduced Migraine Risk
  JOURNAL   Genes (Basel) 15 (6), 797 (2024)
   PUBMED   38927733
  REMARK    GeneRIF: Identification of Polymorphisms in EAAT1 Glutamate
            Transporter Gene SLC1A3 Associated with Reduced Migraine Risk.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Welby,E. and Ebert,A.D.
  TITLE     Diminished motor neuron activity driven by abnormal astrocytic
            EAAT1 glutamate transporter activity in spinal muscular atrophy is
            not fully restored after lentiviral SMN delivery
  JOURNAL   Glia 71 (5), 1311-1332 (2023)
   PUBMED   36655314
  REMARK    GeneRIF: Diminished motor neuron activity driven by abnormal
            astrocytic EAAT1 glutamate transporter activity in spinal muscular
            atrophy is not fully restored after lentiviral SMN delivery.
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Pant,S., Wu,Q., Ryan,R. and Tajkhorshid,E.
  TITLE     Microscopic Characterization of the Chloride Permeation Pathway in
            the Human Excitatory Amino Acid Transporter 1 (EAAT1)
  JOURNAL   ACS Chem Neurosci 13 (6), 776-785 (2022)
   PUBMED   35192345
  REMARK    GeneRIF: Microscopic Characterization of the Chloride Permeation
            Pathway in the Human Excitatory Amino Acid Transporter 1 (EAAT1).
REFERENCE   5  (residues 1 to 542)
  AUTHORS   Lee,A., Anderson,A.R., Beasley,S.J., Barnett,N.L., Poronnik,P. and
            Pow,D.V.
  TITLE     A new splice variant of the glutamate-aspartate transporter:
            cloning and immunolocalization of GLAST1c in rat, pig and human
            brains
  JOURNAL   J Chem Neuroanat 43 (1), 52-63 (2012)
   PUBMED   22026960
REFERENCE   6  (residues 1 to 542)
  AUTHORS   Vallejo-Illarramendi,A., Domercq,M. and Matute,C.
  TITLE     A novel alternative splicing form of excitatory amino acid
            transporter 1 is a negative regulator of glutamate uptake
  JOURNAL   J Neurochem 95 (2), 341-348 (2005)
   PUBMED   16042756
  REMARK    GeneRIF: EAAT1ex9skip splice variant is a negative regulator of
            full-length EAAT1 function in the human brain
REFERENCE   7  (residues 1 to 542)
  AUTHORS   Takai,S., Yamada,K., Kawakami,H., Tanaka,K. and Nakamura,S.
  TITLE     Localization of the gene (SLC1A3) encoding human glutamate
            transporter (GluT-1) to 5p13 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 209-210 (1995)
   PUBMED   7698014
REFERENCE   8  (residues 1 to 542)
  AUTHORS   Shashidharan,P., Huntley,G.W., Meyer,T., Morrison,J.H. and
            Plaitakis,A.
  TITLE     Neuron-specific human glutamate transporter: molecular cloning,
            characterization and expression in human brain
  JOURNAL   Brain Res 662 (1-2), 245-250 (1994)
   PUBMED   7859077
REFERENCE   9  (residues 1 to 542)
  AUTHORS   Arriza,J.L., Fairman,W.A., Wadiche,J.I., Murdoch,G.H.,
            Kavanaugh,M.P. and Amara,S.G.
  TITLE     Functional comparisons of three glutamate transporter subtypes
            cloned from human motor cortex
  JOURNAL   J Neurosci 14 (9), 5559-5569 (1994)
   PUBMED   7521911
REFERENCE   10 (residues 1 to 542)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010631.6 and AC008957.7.
            
            On or before Apr 21, 2025 this sequence version replaced
            XP_005248399.1, XP_054209164.1.
            
            Summary: This gene encodes a member of a member of a high affinity
            glutamate transporter family. This gene functions in the
            termination of excitatory neurotransmission in central nervous
            system. Mutations are associated with episodic ataxia, Type 6.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853560.22915.1,
                                           SRR11853566.22038.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..542
                     /product="excitatory amino acid transporter 1 isoform 1"
                     /note="excitatory amino acid transporter 1; GLAST-1;
                     sodium-dependent glutamate/aspartate transporter 1; solute
                     carrier family 1 (glial high affinity glutamate
                     transporter), member 3"
                     /calculated_mol_wt=59441
     Region          46..496
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            87..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            123..145
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            237..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            270..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            319..340
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            386..412
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            473..494
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P43003.1)"
     CDS             1..542
                     /gene="SLC1A3"
                     /gene_synonym="EA6; EAAT1; GLAST; GLAST1"
                     /coded_by="NM_001438454.1:314..1942"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="GeneID:6507"
                     /db_xref="HGNC:HGNC:10941"
                     /db_xref="MIM:600111"
ORIGIN      
        1 mtksngeepk mggrmerfqq gvrkrtllak kkvqnitked vksylfrnaf vlltvtaviv
       61 gtilgftlrp yrmsyrevky fsfpgellmr mlqmlvlpli isslvtgmaa ldskasgkmg
      121 mravvyymtt tiiavvigii iviiihpgkg tkenmhregk ivrvtaadaf ldlirnmfpp
      181 nlveacfkqf ktnyekrsfk vpiqanetlv gavinnvsea metltritee lvpvpgsvng
      241 vnalglvvfs mcfgfvignm keqgqalref fdslneaimr lvavimwyap vgilfliagk
      301 ivemedmgvi ggqlamytvt vivgllihav ivlpllyflv trknpwvfig gllqalital
      361 gtssssatlp itfkcleenn gvdkrvtrfv lpvgatinmd gtalyealaa ifiaqvnnfe
      421 lnfgqiitis itataasiga agipqaglvt mvivltsvgl ptdditliia vdwfldrlrt
      481 ttnvlgdslg agivehlsrh elknrdvemg nsvieenemk kpyqliaqdn etekpidset
      541 km
//
LOCUS       NP_001424925            1007 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 3 isoform 6 [Homo sapiens].
ACCESSION   NP_001424925 XP_016862724 XP_054203918
VERSION     NP_001424925.1
DBSOURCE    REFSEQ: accession NM_001437996.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1007)
  AUTHORS   Wang,H., Lan,S., Wang,L., Zhao,J., Jia,X., Xu,J., Sun,G., Liu,L.,
            Gong,S., Wang,N., Shan,B., Zhang,F. and Zhang,Z.
  TITLE     Expression of circ-PHC3 enhances ovarian cancer progression via
            regulation of the miR-497-5p/SOX9 pathway
  JOURNAL   J Ovarian Res 16 (1), 142 (2023)
   PUBMED   37468993
  REMARK    GeneRIF: Expression of circ-PHC3 enhances ovarian cancer
            progression via regulation of the miR-497-5p/SOX9 pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1007)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 1007)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1007)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1007)
  AUTHORS   Crea,F., Di Paolo,A., Liu,H.H., Polillo,M., Clermont,P.L.,
            Guerrini,F., Ciabatti,E., Ricci,F., Barate,C., Fontanelli,G.,
            Barsotti,S., Morganti,R., Danesi,R., Wang,Y., Petrini,M.,
            Galimberti,S. and Helgason,C.D.
  TITLE     Polycomb genes are associated with response to imatinib in chronic
            myeloid leukemia
  JOURNAL   Epigenomics 7 (5), 757-765 (2015)
   PUBMED   26343356
  REMARK    GeneRIF: Data show that polycomb-group proteins BMI1, PHC3, CBX6
            and CBX7 expression was significantly increased during imatinib
            treatment.
REFERENCE   6  (residues 1 to 1007)
  AUTHORS   Deshpande,A.M., Akunowicz,J.D., Reveles,X.T., Patel,B.B.,
            Saria,E.A., Gorlick,R.G., Naylor,S.L., Leach,R.J. and Hansen,M.F.
  TITLE     PHC3, a component of the hPRC-H complex, associates with E2F6
            during G0 and is lost in osteosarcoma tumors
  JOURNAL   Oncogene 26 (12), 1714-1722 (2007)
   PUBMED   17001316
  REMARK    GeneRIF: loss of PHC3 may favor tumorigenesis by potentially
            disrupting the ability of cells to remain in G(0)
REFERENCE   7  (residues 1 to 1007)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   8  (residues 1 to 1007)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 1007)
  AUTHORS   Tonkin,E., Hagan,D.M., Li,W. and Strachan,T.
  TITLE     Identification and characterisation of novel mammalian homologues
            of Drosophila polyhomeoticpermits new insights into relationships
            between members of the polyhomeotic family
  JOURNAL   Hum Genet 111 (4-5), 435-442 (2002)
   PUBMED   12384788
REFERENCE   10 (residues 1 to 1007)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC023891.28 and AC008040.7.
            
            On or before Apr 14, 2025 this sequence version replaced
            XP_016862724.1, XP_054203918.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.697846.1,
                                           SRR14372079.2196656.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1007
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.2"
     Protein         1..1007
                     /product="polyhomeotic-like protein 3 isoform 6"
                     /note="early development regulator 3; polyhomeotic-like
                     protein 3; homolog of polyhomeotic 3; early development
                     regulatory protein 3; polyhomeotic like 3"
                     /calculated_mol_wt=108755
     Region          352..>592
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          938..1006
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(956..957,991..992,995..996,999)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(967..971,973..974,977..978,982,987)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..1007
                     /gene="PHC3"
                     /gene_synonym="EDR3; HPH3"
                     /coded_by="NM_001437996.1:19..3042"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:80012"
                     /db_xref="HGNC:HGNC:15682"
                     /db_xref="MIM:620031"
ORIGIN      
        1 maeaefkdhs tamdtepnpg tssvstttss tttttittss srmqqpqisv ysgsdrhavq
       61 alhrppssaa qylqqmyaaq qqhlmlhtaa lqqqhlsssq lqslaavqas lssgrpstsp
      121 tgsvtqqssm sqtsinlsts ptpaqlisrs qassstsgsi tqqtmllgst sptltasqaq
      181 mylraqmlif tpattvaavq sdipvvssss ssscqsaatq vqnltlrsqk lgvlsssqng
      241 ppkstsqtqs ltichnkttv tsskisqrdp spesnkkges pslesrstav trtssihqli
      301 apasyspiqp hslikhqqip lhsppskvsh hqlilqqqqq qiqpitlqns tqdpppsqhc
      361 iplqnhglpp apsnaqsqhc spiqshpspl tvspnqsqsa qqsvvvsppp phspsqspti
      421 iihpqaliqp hplvssalqp gpnlqqstan qvqataqlnl pshlplpasp vvhigpvqqs
      481 alvspgqqiv spshqqyssl qsspipiasp pqmstsppaq ipplplqsmq slqvqpeils
      541 qgqvlvqnal vseeelpaae alvqlpfqtl pppqtvavnl qvqppapvdp pvgmhlnqch
      601 lhkvfslkvy qvedvceeem peesdecvrm drtpppptls paaitvgrge dltsehplle
      661 qvelpavasv sasvikspsd pshvsvpppp lllpaattrs nstsmhssip sienkppqai
      721 vkpqilthvi egfviqegle pfpvsrssll ieqpvkkrpl ldnqvinsvc vqpelqnntk
      781 hadnssdtem edmiaeetle emdsellkce fcgkmgyane flrskrfctm scakrynvsc
      841 skkfalsrwn rkpdnqslgh rgrrpsgpdg aarehilrql pitypsaeed lashedsvps
      901 amttrlrrqs erererelrd vrirkmpens dllpvaqtep siwtvddvwa fihslpgcqd
      961 iadefraqei dgqallllke dhlmsamnik lgpalkicar inslkes
//
LOCUS       NP_001393436             704 aa            linear   PRI 21-NOV-2025
DEFINITION  desmocollin-2 isoform 4 [Homo sapiens].
ACCESSION   NP_001393436
VERSION     NP_001393436.1
DBSOURCE    REFSEQ: accession NM_001406507.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Han,J.Y., Che,N., Mo,J., Zhang,D.F., Liang,X.H., Dong,X.Y.,
            Zhao,X.L. and Sun,B.C.
  TITLE     Desmoglein 2 and desmocollin 2 depletions promote malignancy
            through distinct mechanisms in triple-negative and luminal breast
            cancer
  JOURNAL   BMC Cancer 24 (1), 532 (2024)
   PUBMED   38671389
  REMARK    GeneRIF: Desmoglein 2 and desmocollin 2 depletions promote
            malignancy through distinct mechanisms in triple-negative and
            luminal breast cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 704)
  AUTHORS   Sun,C., Wen,K., Zhang,B., Dong,Y., Chen,C., Neo,S.Y., Leng,B.,
            Gao,T.T. and Wu,J.
  TITLE     DSC2 suppresses the growth of gastric cancer through the inhibition
            of nuclear translocation of gamma-catenin and PTEN/PI3K/AKT
            signaling pathway
  JOURNAL   Aging (Albany NY) 15 (13), 6380-6399 (2023)
   PUBMED   37421607
  REMARK    GeneRIF: DSC2 suppresses the growth of gastric cancer through the
            inhibition of nuclear translocation of gamma-catenin and
            PTEN/PI3K/AKT signaling pathway.
REFERENCE   3  (residues 1 to 704)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   4  (residues 1 to 704)
  AUTHORS   Pariyar,M., Thorne,R.F., Scott,R.J. and Avery-Kiejda,K.A.
  TITLE     Verification and Validation of a Four-Gene Panel as a Prognostic
            Indicator in Triple Negative Breast Cancer
  JOURNAL   Front Oncol 12, 821334 (2022)
   PUBMED   35387118
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 704)
  AUTHORS   Syrris,P., Ward,D., Evans,A., Asimaki,A., Gandjbakhch,E.,
            Sen-Chowdhry,S. and McKenna,W.J.
  TITLE     Arrhythmogenic right ventricular dysplasia/cardiomyopathy
            associated with mutations in the desmosomal gene desmocollin-2
  JOURNAL   Am J Hum Genet 79 (5), 978-984 (2006)
   PUBMED   17033975
REFERENCE   6  (residues 1 to 704)
  AUTHORS   Nuber,U.A., Schafer,S., Schmidt,A., Koch,P.J. and Franke,W.W.
  TITLE     The widespread human desmocollin Dsc2 and tissue-specific patterns
            of synthesis of various desmocollin subtypes
  JOURNAL   Eur J Cell Biol 66 (1), 69-74 (1995)
   PUBMED   7750520
REFERENCE   7  (residues 1 to 704)
  AUTHORS   McNally,E., MacLeod,H. and Dellefave-Castillo,L.
  TITLE     Arrhythmogenic Right Ventricular Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301310
REFERENCE   8  (residues 1 to 704)
  AUTHORS   Arnemann,J., Spurr,N.K., Wheeler,G.N., Parker,A.E. and Buxton,R.S.
  TITLE     Chromosomal assignment of the human genes coding for the major
            proteins of the desmosome junction, desmoglein DGI (DSG),
            desmocollins DGII/III (DSC), desmoplakins DPI/II (DSP), and
            plakoglobin DPIII (JUP)
  JOURNAL   Genomics 10 (3), 640-645 (1991)
   PUBMED   1889810
REFERENCE   9  (residues 1 to 704)
  AUTHORS   Parker,A.E., Wheeler,G.N., Arnemann,J., Pidsley,S.C., Ataliotis,P.,
            Thomas,C.L., Rees,D.A., Magee,A.I. and Buxton,R.S.
  TITLE     Desmosomal glycoproteins II and III. Cadherin-like junctional
            molecules generated by alternative splicing
  JOURNAL   J Biol Chem 266 (16), 10438-10445 (1991)
   PUBMED   2037591
REFERENCE   10 (residues 1 to 704)
  AUTHORS   Garrod,D.R. and Fleming,S.
  TITLE     Early expression of desmosomal components during kidney tubule
            morphogenesis in human and murine embryos
  JOURNAL   Development 108 (2), 313-321 (1990)
   PUBMED   2112455
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012417.13 and KF573685.1.
            
            Summary: This gene encodes a member of the desmocollin protein
            subfamily. Desmocollins, along with desmogleins, are cadherin-like
            transmembrane glycoproteins that are major components of the
            desmosome. Desmosomes are cell-cell junctions that help resist
            shearing forces and are found in high concentrations in cells
            subject to mechanical stress. This gene is found in a cluster with
            other desmocollin family members on chromosome 18. Mutations in
            this gene are associated with arrhythmogenic right ventricular
            dysplasia-11, and reduced protein expression has been described in
            several types of cancer. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.373957.1,
                                           SRR18074967.3962132.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..704
                     /product="desmocollin-2 isoform 4"
                     /note="desmosomal glycoprotein II/III; cadherin family
                     member 2"
                     /calculated_mol_wt=77493
     Region          3..91
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Region          104..208
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(111..112,169,171,204,206..207)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          217..320
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Site            order(223..224,281,283,321,323..324)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          334..430
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(339..340,391,393,426,428..429)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     CDS             1..704
                     /gene="DSC2"
                     /gene_synonym="ARVD11; CDHF2; DG2; DGII/III; DSC3"
                     /coded_by="NM_001406507.1:401..2515"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:1824"
                     /db_xref="HGNC:HGNC:3036"
                     /db_xref="MIM:125645"
ORIGIN      
        1 mlenslgpfp lflqqvqsdt aqnytiyysi rgpgvdqepr nlfyverdtg nlyctrpvdr
       61 eqyesfeiia fattpdgytp elplpliiki edendnypif teetytftif encrvgttvg
      121 qvcatdkdep dtmhtrlkys iigqvppspt lfsmhpttgv itttssqldr elidkyqlki
      181 kvqdmdgqyf glqttstcii niddvndhlp tftrtsyvts veentvdvei lrvtvedkdl
      241 vntanwrany tilkgnengn fkivtdaktn egvlcvvkpl nyeekqqmil qigvvneapf
      301 sreasprsam statvtvnve dqdegpecnp piqtvrmken aevgttsngy kaydpetrss
      361 sgirykkltd ptgwvtiden tgsikvfrsl dreaetikng iynitvlasd qggrtctgtl
      421 giilqdvndn spfipkktvi ickptmssae ivavdpdepi hgppfdfsle sstsevqrmw
      481 rlkaindtaa rlsyqndppf gsyvvpitvr drlgmssvts ldvtlcdcit endcthrvdp
      541 riggggvqlg kwailaillg iallfcilft lvcgasgtsk qpkvipddla qqnlivsnte
      601 apgddkvysa ngfttqtvga saqgvcgtvg sgiknggqet iemvkgghqt sescrgaghh
      661 htldscrggh tevdncryty sewhsftqpr lgeesirght likn
//
LOCUS       NP_001397956            1892 aa            linear   PRI 21-NOV-2025
DEFINITION  Golgi-specific brefeldin A-resistance guanine nucleotide exchange
            factor 1 isoform 17 [Homo sapiens].
ACCESSION   NP_001397956 XP_006718111
VERSION     NP_001397956.1
DBSOURCE    REFSEQ: accession NM_001411027.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1892)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1892)
  AUTHORS   Hirano,J., Hayashi,T., Kitamura,K., Nishimura,Y., Shimizu,H.,
            Okamoto,T., Okada,K., Uemura,K., Yeh,M.T., Ono,C., Taguwa,S.,
            Muramatsu,M. and Matsuura,Y.
  TITLE     Enterovirus 3A protein disrupts endoplasmic reticulum homeostasis
            through interaction with GBF1
  JOURNAL   J Virol 98 (7), e0081324 (2024)
   PUBMED   38904364
  REMARK    GeneRIF: Enterovirus 3A protein disrupts endoplasmic reticulum
            homeostasis through interaction with GBF1.
REFERENCE   3  (residues 1 to 1892)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1892)
  AUTHORS   Navare,A.T., Mast,F.D., Olivier,J.P., Bertomeu,T., Neal,M.L.,
            Carpp,L.N., Kaushansky,A., Coulombe-Huntington,J., Tyers,M. and
            Aitchison,J.D.
  TITLE     Viral protein engagement of GBF1 induces host cell vulnerability
            through synthetic lethality
  JOURNAL   J Cell Biol 221 (11) (2022)
   PUBMED   36305789
  REMARK    GeneRIF: Viral protein engagement of GBF1 induces host cell
            vulnerability through synthetic lethality.
REFERENCE   5  (residues 1 to 1892)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1892)
  AUTHORS   Garcia-Mata,R. and Sztul,E.
  TITLE     The membrane-tethering protein p115 interacts with GBF1, an ARF
            guanine-nucleotide-exchange factor
  JOURNAL   EMBO Rep 4 (3), 320-325 (2003)
   PUBMED   12634853
  REMARK    GeneRIF: novel interaction between p115 and Golgi-specific
            brefeldin-A-resistant factor 1 (GBF1)
REFERENCE   7  (residues 1 to 1892)
  AUTHORS   Kawamoto,K., Yoshida,Y., Tamaki,H., Torii,S., Shinotsuka,C.,
            Yamashina,S. and Nakayama,K.
  TITLE     GBF1, a guanine nucleotide exchange factor for ADP-ribosylation
            factors, is localized to the cis-Golgi and involved in membrane
            association of the COPI coat
  JOURNAL   Traffic 3 (7), 483-495 (2002)
   PUBMED   12047556
  REMARK    GeneRIF: detailed subcellular localization to the cis-Golgi
REFERENCE   8  (residues 1 to 1892)
  AUTHORS   Verhoeven,K., Villanova,M., Rossi,A., Malandrini,A., De Jonghe,P.
            and Timmerman,V.
  TITLE     Localization of the gene for the intermediate form of
            Charcot-Marie-Tooth to chromosome 10q24.1-q25.1
  JOURNAL   Am J Hum Genet 69 (4), 889-894 (2001)
   PUBMED   11533914
REFERENCE   9  (residues 1 to 1892)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   10 (residues 1 to 1892)
  AUTHORS   Mansour,S.J., Herbrick,J.A., Scherer,S.W. and Melancon,P.
  TITLE     Human GBF1 is a ubiquitously expressed gene of the sec7 domain
            family mapping to 10q24
  JOURNAL   Genomics 54 (2), 323-327 (1998)
   PUBMED   9828135
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160011.35, AL356420.14 and
            AL121928.13.
            
            On Aug 20, 2022 this sequence version replaced XP_006718111.1.
            
            Summary: This gene encodes a member of the Sec7 domain family. The
            encoded protein is a guanine nucleotide exchange factor that
            regulates the recruitment of proteins to membranes by mediating GDP
            to GTP exchange. The encoded protein is localized to the Golgi
            apparatus and plays a role in vesicular trafficking by activating
            ADP ribosylation factor 1. The encoded protein has also been
            identified as an important host factor for viral replication.
            Multiple transcript variants have been observed for this gene.
            [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.1523769.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1892
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..1892
                     /product="Golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1 isoform 17"
                     /note="golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1; BFA-resistant GEF 1"
                     /calculated_mol_wt=210039
     Region          1..211
                     /region_name="DCB, DCB:DCB domain and DCB:HUS domain
                     interaction. /evidence=ECO:0000250|UniProtKB:Q9R1D7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          248..299
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          <462..>1211
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          563..583
                     /region_name="HUS, DCB:HUS domain interaction.
                     /evidence=ECO:0000250|UniProtKB:Q9R1D7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          652..698
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          732..917
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          919..1403
                     /region_name="Phosphatidylinositol-phosphate binding,
                     required for translocation to the leading edge and for
                     ARF1 activation upon GPCR signaling.
                     /evidence=ECO:0000269|PubMed:22573891"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1317..1368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1349
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AMPK.
                     /evidence=ECO:0000269|PubMed:18063581; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1383..1403
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1463..1516
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1508
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1758..1841
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1806
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1817
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          <1827..1890
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1892
                     /gene="GBF1"
                     /gene_synonym="ARF1GEF; CMT2GG; CMTDI2; CMTDIA"
                     /coded_by="NM_001411027.1:261..5939"
                     /note="isoform 17 is encoded by transcript variant 25"
                     /db_xref="CCDS:CCDS91329.1"
                     /db_xref="GeneID:8729"
                     /db_xref="HGNC:HGNC:4181"
                     /db_xref="MIM:603698"
ORIGIN      
        1 mvdkniyiiq geinivvgai krnarwstht pldeerdpll hsfghlkevl nsitelseie
       61 pnvflrpfle virsedttgp itglaltsvn kflsyalidp thegtaegme nmadavthar
      121 fvgtdpasde vvlmkilqvl rtllltpvga hltnesvcei mqscfricfe mrlsellrks
      181 aehtlvdmvq llftrlpqfk eepknyvgtn mkkispclln klelssgeqt kalnqlervl
      241 lfknlklkmr aggmsdsskw kkqkrsprpp rhmtkvtpgs elptpngttl ssnltggmpf
      301 idvptpissa sseaasavvs pstdsglefs sqttskedlt dleqpgspgy statepgsse
      361 lgvpeqpdlq egthveksqs asvesipevl eectspadhs dsasvhdmdy vnprgvrftq
      421 ssqkegtalv pyglpcirel frflisltnp hdrhnsevmi hmglhlltva lesapvaqcq
      481 tllglikdem crhlfqllsi erlnlyaasl rvcfllfesm rehlkfqmem yikklmeiit
      541 venpkmpyem kemaleaivq lwripsfvte lyinydcdyy csnlfeeltk llsknafpvs
      601 gqlytthlls ldalltvids teahcqakvl nsltqqekke tarpsceivd gtreasnter
      661 tasdgkavgm asdipglhlp gggrlppehg ksgcsdleea vdsgadkkfa rkpprfscll
      721 pdprelieik nkkkllitgt eqfnqkpkkg iqflqekgll tipmdnteva qwlrenprld
      781 kkmigefvsd rknidllesf vstfsfqglr ldealrlyle afrlpgeapv iqrlleafte
      841 rwmncngspf ansdacfsla yavimlntdq hnhnvrkqna pmtleefrkn lkgvnggkdf
      901 eqdiledmyh aikneeivmp eeqtglvren yvwnvllhrg atpegiflrv ptasydldlf
      961 tmtwgptiaa lsyvfdksle etiiqkaisg frkcamisah yglsdvfdnl iislckftal
     1021 ssesienlps vfgsnpkahi aaktvfhlah rhgdilregw knimeamlql fraqllpkam
     1081 ievedfvdpn gkislqreet psnrgestvl sfvswltlsg peqssvrgps tenqeakrva
     1141 lecikqcdpe kmiteskflq leslqelmka lvsvtpdeet ydeedaafcl emllrivlen
     1201 rdrvgcvwqt vrdhlyhlcv qaqdfcflve ravvgllrla irllrreeis aqvllslril
     1261 llmkpsvlsr vshqvayglh ellktnaani hsgddwatlf tllecigsgv kppaalqata
     1321 radapdagaq sdselpsyhq ndvsldrgyt sdsevytdhg rpgkihrsat dadvvnsgwl
     1381 vvgkddvdns kpgpsrpgps plinqysltv gldlgphdtk sllkcvesls fivrdaahit
     1441 pdnfelcvkt lrifveasln ggcksqekrg kshkydskgn rfkkkskegs mlrrprtssq
     1501 hasrggqsdd dedegvpasy htvslqvsqd lldlmhtlht raasiysswa eeqrhletgg
     1561 qkieadsrtl wahcwcpllq giaclccdar rqvrmqalty lqrallvhdl qkldalewes
     1621 cfnkvlfpll tkllenispa dvggmeetrm rastllskvf lqhlspllsl stfaalwlti
     1681 ldfmdkymha gssdllseai peslknmllv mdtaeifhsa dargggpsal weitweridc
     1741 flphlrdelf kqtviqdpmp mepqgqkpla sahltsaagd trtpghpppp eipselgacd
     1801 fekpespraa sssspgspva sspsrlsptp dgppplaqpp lilqplaspl qvgvppmtlp
     1861 iilnpaliea tspvpllatp rptdpiptse vn
//
LOCUS       NP_001401591             479 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 2 isoform g [Homo sapiens].
ACCESSION   NP_001401591 XP_006719495
VERSION     NP_001401591.1
DBSOURCE    REFSEQ: accession NM_001414662.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Jung,J.H., Lee,D., Ko,H.M. and Jang,H.J.
  TITLE     Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in Colorectal
            Cancer Cells by Activating p53
  JOURNAL   Biomolecules 11 (10), 1492 (2021)
   PUBMED   34680125
  REMARK    GeneRIF: Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in
            Colorectal Cancer Cells by Activating p53.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Royer-Bertrand,B., Cisarova,K., Niel Butschi,F., Foletti,G.,
            Guinchat,V., Tran,C., Superti-Furga,A. and Good,J.M.
  TITLE     CNOT2 haploinsufficiency in a 40-year-old man with intellectual
            disability, autism, and seizures
  JOURNAL   Am J Med Genet A 185 (8), 2602-2606 (2021)
   PUBMED   34018673
  REMARK    GeneRIF: CNOT2 haploinsufficiency in a 40-year-old man with
            intellectual disability, autism, and seizures.
            Review article
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Jayne,S., Zwartjes,C.G., van Schaik,F.M. and Timmers,H.T.
  TITLE     Involvement of the SMRT/NCoR-HDAC3 complex in transcriptional
            repression by the CNOT2 subunit of the human Ccr4-Not complex
  JOURNAL   Biochem J 398 (3), 461-467 (2006)
   PUBMED   16712523
  REMARK    GeneRIF: This study shows that SMRT/NCoR-HDAC3 complex is a
            cofactor of CNOT2-mediated repression and suggests that
            transcriptional regulation by the Ccr4-Not complex involves
            regulation of chromatin modification.
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Winkler,G.S., Mulder,K.W., Bardwell,V.J., Kalkhoven,E. and
            Timmers,H.T.
  TITLE     Human Ccr4-Not complex is a ligand-dependent repressor of nuclear
            receptor-mediated transcription
  JOURNAL   EMBO J 25 (13), 3089-3099 (2006)
   PUBMED   16778766
REFERENCE   7  (residues 1 to 479)
  AUTHORS   Shi,J. and Nelson,M.A.
  TITLE     The cyclin-dependent kinase 11 interacts with NOT2
  JOURNAL   Biochem Biophys Res Commun 334 (4), 1310-1316 (2005)
   PUBMED   16039607
  REMARK    GeneRIF: These findings suggest that CDK11 may contribute to
            apoptosis by regulating the activity of NOT2 independent of its
            kinase activity.
REFERENCE   8  (residues 1 to 479)
  AUTHORS   Zwartjes,C.G., Jayne,S., van den Berg,D.L. and Timmers,H.T.
  TITLE     Repression of promoter activity by CNOT2, a subunit of the
            transcription regulatory Ccr4-not complex
  JOURNAL   J Biol Chem 279 (12), 10848-10854 (2004)
   PUBMED   14707134
  REMARK    GeneRIF: major repression function of CNOT2 is localized in a
            specialized protein motif, the Not-Box
REFERENCE   9  (residues 1 to 479)
  AUTHORS   Denis,C.L. and Chen,J.
  TITLE     The CCR4-NOT complex plays diverse roles in mRNA metabolism
  JOURNAL   Prog Nucleic Acid Res Mol Biol 73, 221-250 (2003)
   PUBMED   12882519
  REMARK    Review article
REFERENCE   10 (residues 1 to 479)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092881.8 and AC025569.37.
            
            On Feb 21, 2023 this sequence version replaced XP_006719495.1.
            
            Summary: This gene encodes a subunit of the multi-component
            CCR4-NOT complex. The CCR4-NOT complex regulates mRNA synthesis and
            degradation and is also thought to be involved in mRNA splicing,
            transport and localization. The encoded protein interacts with
            histone deacetylases and functions as a repressor of polymerase II
            transcription. Alternatively spliced transcript variants have been
            observed for this gene. [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1027629.1,
                                           SRR14038193.3344456.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..479
                     /product="CCR4-NOT transcription complex subunit 2 isoform
                     g"
                     /note="negative regulator of transcription 2;
                     CCR4-associated factor 2; CC chemokine receptor 4-negative
                     regulator of transcription 2"
                     /calculated_mol_wt=53059
     Region          335..458
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..479
                     /gene="CNOT2"
                     /gene_synonym="CDC36; HSPC131; IDNADFS; NOT2; NOT2H"
                     /coded_by="NM_001414662.1:144..1583"
                     /note="isoform g is encoded by transcript variant 16"
                     /db_xref="GeneID:4848"
                     /db_xref="HGNC:HGNC:7878"
                     /db_xref="MIM:604909"
ORIGIN      
        1 mvrtdghtls ekrnyqvtns mfgasrkkfv egvdsdyhde nmyysqssmf phrsekdmla
       61 spstsgqlsq fgaslygqqs alglpmrgms nntpqlnrsl sqgtqlpshv tpttgvptms
      121 lhtppspssm sgfgmnrnqa fgmnnslssn ifngtdgsen vtgldlsdfp aladrnrreg
      181 sgnptplinp lagrapyvgm vtkpaneqsq dfsihnedfp alpgssykdp tssnddsksn
      241 lntsgkttss tdgpkfpgdk ssttqnnnqq kkgiqvlpdg rvtnipqgmv tdqfgmigll
      301 tfiraaetdp gmvhlalgsd lttlglnlns penlypkfas pwasspcrpq didfhvpsey
      361 ltnihirdkl aaiklgryge dllfylyymn ggdvlqllaa velfnrdwry hkeervwitr
      421 apgmeptmkt ntyergtyyf fdclnwrkva kefhleydkl eerphlpstf nynpaqqaf
//
LOCUS       NP_001425389             448 aa            linear   PRI 21-NOV-2025
DEFINITION  excitatory amino acid transporter 1 isoform 7 [Homo sapiens].
ACCESSION   NP_001425389
VERSION     NP_001425389.1
DBSOURCE    REFSEQ: accession NM_001438460.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Albury,C.L., Sutherland,H.G., Lam,A.W.Y., Tran,N.K., Lea,R.A.,
            Haupt,L.M. and Griffiths,L.R.
  TITLE     Identification of Polymorphisms in EAAT1 Glutamate Transporter Gene
            SLC1A3 Associated with Reduced Migraine Risk
  JOURNAL   Genes (Basel) 15 (6), 797 (2024)
   PUBMED   38927733
  REMARK    GeneRIF: Identification of Polymorphisms in EAAT1 Glutamate
            Transporter Gene SLC1A3 Associated with Reduced Migraine Risk.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Welby,E. and Ebert,A.D.
  TITLE     Diminished motor neuron activity driven by abnormal astrocytic
            EAAT1 glutamate transporter activity in spinal muscular atrophy is
            not fully restored after lentiviral SMN delivery
  JOURNAL   Glia 71 (5), 1311-1332 (2023)
   PUBMED   36655314
  REMARK    GeneRIF: Diminished motor neuron activity driven by abnormal
            astrocytic EAAT1 glutamate transporter activity in spinal muscular
            atrophy is not fully restored after lentiviral SMN delivery.
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Pant,S., Wu,Q., Ryan,R. and Tajkhorshid,E.
  TITLE     Microscopic Characterization of the Chloride Permeation Pathway in
            the Human Excitatory Amino Acid Transporter 1 (EAAT1)
  JOURNAL   ACS Chem Neurosci 13 (6), 776-785 (2022)
   PUBMED   35192345
  REMARK    GeneRIF: Microscopic Characterization of the Chloride Permeation
            Pathway in the Human Excitatory Amino Acid Transporter 1 (EAAT1).
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Lee,A., Anderson,A.R., Beasley,S.J., Barnett,N.L., Poronnik,P. and
            Pow,D.V.
  TITLE     A new splice variant of the glutamate-aspartate transporter:
            cloning and immunolocalization of GLAST1c in rat, pig and human
            brains
  JOURNAL   J Chem Neuroanat 43 (1), 52-63 (2012)
   PUBMED   22026960
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Vallejo-Illarramendi,A., Domercq,M. and Matute,C.
  TITLE     A novel alternative splicing form of excitatory amino acid
            transporter 1 is a negative regulator of glutamate uptake
  JOURNAL   J Neurochem 95 (2), 341-348 (2005)
   PUBMED   16042756
  REMARK    GeneRIF: EAAT1ex9skip splice variant is a negative regulator of
            full-length EAAT1 function in the human brain
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Takai,S., Yamada,K., Kawakami,H., Tanaka,K. and Nakamura,S.
  TITLE     Localization of the gene (SLC1A3) encoding human glutamate
            transporter (GluT-1) to 5p13 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 209-210 (1995)
   PUBMED   7698014
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Shashidharan,P., Huntley,G.W., Meyer,T., Morrison,J.H. and
            Plaitakis,A.
  TITLE     Neuron-specific human glutamate transporter: molecular cloning,
            characterization and expression in human brain
  JOURNAL   Brain Res 662 (1-2), 245-250 (1994)
   PUBMED   7859077
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Arriza,J.L., Fairman,W.A., Wadiche,J.I., Murdoch,G.H.,
            Kavanaugh,M.P. and Amara,S.G.
  TITLE     Functional comparisons of three glutamate transporter subtypes
            cloned from human motor cortex
  JOURNAL   J Neurosci 14 (9), 5559-5569 (1994)
   PUBMED   7521911
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010631.6 and AC008957.7.
            
            Summary: This gene encodes a member of a member of a high affinity
            glutamate transporter family. This gene functions in the
            termination of excitatory neurotransmission in central nervous
            system. Mutations are associated with episodic ataxia, Type 6.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.317222.1,
                                           SRR11853566.22037.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2151741
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..448
                     /product="excitatory amino acid transporter 1 isoform 7"
                     /note="excitatory amino acid transporter 1; GLAST-1;
                     sodium-dependent glutamate/aspartate transporter 1; solute
                     carrier family 1 (glial high affinity glutamate
                     transporter), member 3"
                     /calculated_mol_wt=48430
     Region          12..402
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     CDS             1..448
                     /gene="SLC1A3"
                     /gene_synonym="EA6; EAAT1; GLAST; GLAST1"
                     /coded_by="NM_001438460.1:696..2042"
                     /note="isoform 7 is encoded by transcript variant 12"
                     /db_xref="GeneID:6507"
                     /db_xref="HGNC:HGNC:10941"
                     /db_xref="MIM:600111"
ORIGIN      
        1 misgfvgkaq nsgmaaldsk asgkmgmrav vyymtttiia vvigiiivii ihpgkgtken
       61 mhregkivrv taadafldli rnmfppnlve acfkqfktny ekrsfkvpiq anetlvgavi
      121 nnvseametl triteelvpv pgsvngvnal glvvfsmcfg fvignmkeqg qalreffdsl
      181 neaimrlvav imwyapvgil fliagkivem edmgviggql amytvtvivg llihavivlp
      241 llyflvtrkn pwvfiggllq alitalgtss ssatlpitfk cleenngvdk rvtrfvlpvg
      301 atinmdgtal yealaaifia qvnnfelnfg qiitisitat aasigaagip qaglvtmviv
      361 ltsvglptdd itliiavdwf ldrlrtttnv lgdslgagiv ehlsrhelkn rdvemgnsvi
      421 eenemkkpyq liaqdnetek pidsetkm
//
LOCUS       NP_001425739             611 aa            linear   PRI 21-NOV-2025
DEFINITION  nuclear protein localization protein 4 homolog isoform 4 [Homo
            sapiens].
ACCESSION   NP_001425739 XP_047292321 XP_054172605
VERSION     NP_001425739.1
DBSOURCE    REFSEQ: accession NM_001438810.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 611)
  AUTHORS   Bekkari,H., Benmakhlouf,Y., Nourouti,N.G., Barakat,A. and
            Mechita,M.B.
  TITLE     Study of Clinical Characteristics of Intellectual Disability in
            Morocco
  JOURNAL   Innov Clin Neurosci 21 (7-9), 10-14 (2024)
   PUBMED   39329031
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 611)
  AUTHORS   Wang,N., Zhu,D., Liu,Y., Wu,J., Wang,M., Jin,S., Fu,F., Li,B.,
            Ji,H., Du,C. and Zheng,Z.
  TITLE     NPLOC4 is a potential target and a poor prognostic signature in
            lung squamous cell carcinoma
  JOURNAL   Sci Rep 13 (1), 20430 (2023)
   PUBMED   37993584
  REMARK    GeneRIF: NPLOC4 is a potential target and a poor prognostic
            signature in lung squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 611)
  AUTHORS   Tsioras,K., Smith,K.C., Edassery,S.L., Garjani,M., Li,Y.,
            Williams,C., McKenna,E.D., Guo,W., Wilen,A.P., Hark,T.J.,
            Marklund,S.L., Ostrow,L.W., Gilthorpe,J.D., Ichida,J.K., Kalb,R.G.,
            Savas,J.N. and Kiskinis,E.
  TITLE     Analysis of proteome-wide degradation dynamics in ALS SOD1
            iPSC-derived patient neurons reveals disrupted VCP homeostasis
  JOURNAL   Cell Rep 42 (10), 113160 (2023)
   PUBMED   37776851
REFERENCE   4  (residues 1 to 611)
  AUTHORS   Nguyen,T.Q., My Le,L.T., Kim,D.H., Ko,K.S., Lee,H.T., Kim
            Nguyen,Y.T., Kim,H.S., Han,B.W., Kang,W. and Yang,J.K.
  TITLE     Structural basis for the interaction between human Npl4 and
            Npl4-binding motif of human Ufd1
  JOURNAL   Structure 30 (11), 1530-1537 (2022)
   PUBMED   36087575
  REMARK    GeneRIF: Structural basis for the interaction between human Npl4
            and Npl4-binding motif of human Ufd1.
REFERENCE   5  (residues 1 to 611)
  AUTHORS   Fujisawa,R., Polo Rivera,C. and Labib,K.P.M.
  TITLE     Multiple UBX proteins reduce the ubiquitin threshold of the
            mammalian p97-UFD1-NPL4 unfoldase
  JOURNAL   Elife 11, e76763 (2022)
   PUBMED   35920641
  REMARK    GeneRIF: Multiple UBX proteins reduce the ubiquitin threshold of
            the mammalian p97-UFD1-NPL4 unfoldase.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 611)
  AUTHORS   McConnell,E., Lass,A. and Wojcik,C.
  TITLE     Ufd1-Npl4 is a negative regulator of cholera toxin
            retrotranslocation
  JOURNAL   Biochem Biophys Res Commun 355 (4), 1087-1090 (2007)
   PUBMED   17331469
  REMARK    GeneRIF: Ufd1-Npl4 is a negative regulator of retrotranslocation,
            delaying the retrotranslocation of endoplasmic reticulum-associated
            degradation substrates independently of its association with VCP
REFERENCE   7  (residues 1 to 611)
  AUTHORS   Arrigoni,R., Alam,S.L., Wamstad,J.A., Bardwell,V.J., Sundquist,W.I.
            and Schreiber-Agus,N.
  TITLE     The Polycomb-associated protein Rybp is a ubiquitin binding protein
  JOURNAL   FEBS Lett 580 (26), 6233-6241 (2006)
   PUBMED   17070805
  REMARK    Erratum:[FEBS Lett. 2006 Dec 11;580(28-29):6754]
REFERENCE   8  (residues 1 to 611)
  AUTHORS   Gevaert,K., Goethals,M., Martens,L., Van Damme,J., Staes,A.,
            Thomas,G.R. and Vandekerckhove,J.
  TITLE     Exploring proteomes and analyzing protein processing by mass
            spectrometric identification of sorted N-terminal peptides
  JOURNAL   Nat Biotechnol 21 (5), 566-569 (2003)
   PUBMED   12665801
REFERENCE   9  (residues 1 to 611)
  AUTHORS   Botta,A., Tandoi,C., Fini,G., Calabrese,G., Dallapiccola,B. and
            Novelli,G.
  TITLE     Cloning and characterization of the gene encoding human NPL4, a
            protein interacting with the ubiquitin fusion-degradation protein
            (UFD1L)
  JOURNAL   Gene 275 (1), 39-46 (2001)
   PUBMED   11574150
REFERENCE   10 (residues 1 to 611)
  AUTHORS   Meyer,H.H., Shorter,J.G., Seemann,J., Pappin,D. and Warren,G.
  TITLE     A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to
            ubiquitin and nuclear transport pathways
  JOURNAL   EMBO J 19 (10), 2181-2192 (2000)
   PUBMED   10811609
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC139530.3 and AC137896.5.
            
            On or before Apr 24, 2025 this sequence version replaced
            XP_047292321.1, XP_054172605.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853565.14013.1,
                                           SRR11853559.15312.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..611
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..611
                     /product="nuclear protein localization protein 4 homolog
                     isoform 4"
                     /note="nuclear protein localization protein 4 homolog;
                     nuclear protein localization 4 homolog; NPLOC4 ubiquitin
                     recognition factor"
                     /calculated_mol_wt=68431
     Region          1..80
                     /region_name="UN_NPL4"
                     /note="Nuclear pore localization protein NPL4; pfam11543"
                     /db_xref="CDD:431926"
     Region          105..245
                     /region_name="zf-NPL4"
                     /note="NPL4 family, putative zinc binding region;
                     pfam05020"
                     /db_xref="CDD:461523"
     Region          249..555
                     /region_name="NPL4"
                     /note="NPL4 family; pfam05021"
                     /db_xref="CDD:461524"
     CDS             1..611
                     /gene="NPLOC4"
                     /gene_synonym="NPL4"
                     /coded_by="NM_001438810.1:183..2018"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:55666"
                     /db_xref="HGNC:HGNC:18261"
                     /db_xref="MIM:606590"
ORIGIN      
        1 maesiiirvq spdgvkrita tkretaatfl kkvakefgfq nngfsvyinr nktgeitass
       61 nkslnllkik hgdllflfps slagpsseme tsvppgfkvf gapnvvedei dqylskqdgk
      121 iyrsrdpqlc rhgplgkcvh cvplepfded ylnhleppvk hmsfhayirk ltggadkgkf
      181 valeniscki ksgceghlpw pngictkcqp saitlnrqky rhvdnimfen htvadrfldf
      241 wrktgnqhfg ylygrytehk diplgiraev aaiyeppqig tqnslelled pkaevvdeia
      301 aklglrkvgw iftdlvsedt rkgtvrysrn kdtyflssee citagdfqnk hpnmcrlspd
      361 ghfgskfvta vatggpdnqv hfegyqvsnq cmalvrdecl lpckdapelg yakessseqy
      421 vpdvfykdvd kfgneitqla rplpveylii ditttfpkdp vytfsisqnp fpienrdvlg
      481 etqdfhslat ylsqntssvf ldtisdfhll lflvtnevmp lqdsisllle avrtrneela
      541 qtwkrseqwa tieqlctsrv agitdvyhht wrchlyaqla gssqvsmsta psgaphtrpl
      601 qpcgpvstar s
//
LOCUS       NP_001394388            2742 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform j [Homo sapiens].
ACCESSION   NP_001394388
VERSION     NP_001394388.1
DBSOURCE    REFSEQ: accession NM_001407459.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2742)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2742)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2742)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2742)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2742)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2742)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2742)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2742)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2742)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2742)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.953595.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2742
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2742
                     /product="adenomatous polyposis coli protein isoform j"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=300309
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Region          <8..272
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          <307..365
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          364..407
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(398,402,406,441,445,449,485,489,493)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          411..452
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          415..452
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          459..494
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          502..543
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          548..588
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          552..586
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          590..630
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          594..630
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          631..918
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          935..1034
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1156..>1173
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1182..1267
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1190..1600
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1270..1292
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1536..1559
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1561..1614
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1615..1636
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1645..1738
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1772..1846
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1932..1951
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2122..2467
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2569..2742
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2742
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407459.1:168..8396"
                     /note="isoform j is encoded by transcript variant 29"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrriar iqqiekdilr irqllqsqat
      241 eaerssqnkh etgshdaerq negqgvgein matsgngqgs ttrmdhetas vlssssthsa
      301 prrltshlgt kiraycetcw ewqeahepgm dqdknpmpap vehqicpavc vlmklsfdee
      361 hrhamnelgg lqaiaellqv dcemygltnd hysitlrrya gmaltnltfg dvankatlcs
      421 mkgcmralva qlksesedlq qviasvlrnl swradvnskk tlrevgsvka lmecalevkk
      481 estlksvlsa lwnlsahcte nkadicavdg alaflvgtlt yrsqtntlai iesgggilrn
      541 vssliatned hrqilrennc lqtllqhlks hsltivsnac gtlwnlsarn pkdqealwdm
      601 gavsmlknli hskhkmiamg saaalrnlma nrpakykdan imspgsslps lhvrkqkale
      661 aeldaqhlse tfdnidnlsp kashrskqrh kqslygdyvf dtnrhddnrs dnfntgnmtv
      721 lspylnttvl psssssrgsl dssrsekdrs lerergiglg nyhpatenpg tsskrglqis
      781 ttaaqiakvm eevsaihtsq edrssgstte lhcvtderna lrrssaahth sntynftkse
      841 nsnrtcsmpy akleykrssn dslnsvsssd gygkrgqmkp siesysedde skfcsygqyp
      901 adlahkihsa nhmddndgel dtpinyslky sdeqlnsgrq spsqnerwar pkhiiedeik
      961 qseqrqsrnq sttypvytes tddkhlkfqp hfgqqecvsp yrsrgangse tnrvgsnhgi
     1021 nqnvsqslcq eddyeddkpt nyseryseee qheeeerptn ysikyneekr hvdqpidysl
     1081 kyatdipssq kqsfsfskss sgqssktehm ssssentstp ssnakrqnql hpssaqsrsg
     1141 qpqkaatckv ssinqetiqt ycvedtpicf srcsslssls saedeigcnq ttqeadsant
     1201 lqiaeikeki gtrsaedpvs evpavsqhpr tkssrlqgss lssesarhka vefssgaksp
     1261 sksgaqtpks ppehyvqetp lmfsrctsvs sldsfesrsi assvqsepcs gmvsgiisps
     1321 dlpdspgqtm ppsrsktppp ppqtaqtkre vpknkaptae kresgpkqaa vnaavqrvqv
     1381 lpdadtllhf atestpdgfs cssslsalsl depfiqkdve lrimppvqen dngneteseq
     1441 pkesnenqek eaektidsek dllddsdddd ieileeciis amptkssrka kkpaqtaskl
     1501 pppvarkpsq lpvykllpsq nrlqpqkhvs ftpgddmprv ycvegtpinf statslsdlt
     1561 iesppnelaa gegvrggaqs gefekrdtip tegrstdeaq ggktssvtip elddnkaeeg
     1621 dilaecinsa mpkgkshkpf rvkkimdqvq qasasssapn knqldgkkkk ptspvkpipq
     1681 nteyrtrvrk nadsknnlna ervfsdnkds kkqnlknnsk vfndklpnne drvrgsfafd
     1741 sphhytpieg tpycfsrnds lssldfdddd vdlsrekael rkakenkese akvtshtelt
     1801 snqqsanktq aiakqpinrg qpkpilqkqs tfpqsskdip drgaatdekl qnfaientpv
     1861 cfshnsslss lsdidqennn kenepikete ppdsqgepsk pqasgyapks fhvedtpvcf
     1921 srnsslssls idseddllqe cissampkkk kpsrlkgdne khsprnmggi lgedltldlk
     1981 diqrpdsehg lspdsenfdw kaiqegansi vsslhqaaaa aclsrqassd sdsilslksg
     2041 islgspfhlt pdqeekpfts nkgprilkpg ekstletkki eseskgikgg kkvykslitg
     2101 kvrsnseisg qmkqplqanm psisrgrtmi hipgvrnsss stspvskkgp plktpasksp
     2161 segqtattsp rgakpsvkse lspvarqtsq iggsskapsr sgsrdstpsr paqqplsrpi
     2221 qspgrnsisp grngisppnk lsqlprtssp stastkssgs gkmsytspgr qmsqqnltkq
     2281 tglsknassi prsesaskgl nqmnngngan kkvelsrmss tkssgsesdr serpvlvrqs
     2341 tfikeapspt lrrkleesas feslspssrp asptrsqaqt pvlspslpdm slsthssvqa
     2401 ggwrklppnl sptieyndgr pakrhdiars hsespsrlpi nrsgtwkreh skhssslprv
     2461 stwrrtgsss silsassess ekaksedekh vnsisgtkqs kenqvsakgt wrkikenefs
     2521 ptnstsqtvs sgatngaesk tliyqmapav sktedvwvri edcpinnprs grsptgntpp
     2581 vidsvsekan pnikdskdnq akqnvgngsv pmrtvglenr lnsfiqvdap dqkgteikpg
     2641 qnnpvpvset nessivertp fsssssskhs spsgtvaarv tpfnynpspr kssadstsar
     2701 psqiptpvnn ntkkrdsktd stessgtqsp krhsgsylvt sv
//
LOCUS       NP_001425599             829 aa            linear   PRI 21-NOV-2025
DEFINITION  dipeptidyl peptidase 8 isoform 8 [Homo sapiens].
ACCESSION   NP_001425599 XP_047288717 XP_054234280
VERSION     NP_001425599.1
DBSOURCE    REFSEQ: accession NM_001438670.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Li,K., Zhang,Y., Zhao,W., Wang,R., Li,Y., Wei,L., Wang,L., Chen,X.,
            Chen,Z., Liu,P., Nie,N., Tian,X. and Fu,R.
  TITLE     DPP8/9 inhibition attenuates the TGF-beta1-induced excessive
            deposition of extracellular matrix (ECM) in human mesangial cells
            via Smad and Akt signaling pathways
  JOURNAL   Toxicol Lett 395, 1-10 (2024)
   PUBMED   38458339
  REMARK    GeneRIF: DPP8/9 inhibition attenuates the TGF-beta1-induced
            excessive deposition of extracellular matrix (ECM) in human
            mesangial cells via Smad and Akt signaling pathways.
REFERENCE   3  (residues 1 to 829)
  AUTHORS   Zhang,Y., Li,K., Li,Y., Zhao,W., Wang,L., Chen,Z., Ma,X., Yao,T.,
            Wang,J., Dong,W., Li,X., Tian,X. and Fu,R.
  TITLE     Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the
            proximal renal tubule epithelial cells
  JOURNAL   Pharmacol Res 169, 105630 (2021)
   PUBMED   33932609
  REMARK    GeneRIF: Profibrotic mechanisms of DPP8 and DPP9 highly expressed
            in the proximal renal tubule epithelial cells.
REFERENCE   4  (residues 1 to 829)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 829)
  AUTHORS   Hollingsworth,L.R., Sharif,H., Griswold,A.R., Fontana,P.,
            Mintseris,J., Dagbay,K.B., Paulo,J.A., Gygi,S.P., Bachovchin,D.A.
            and Wu,H.
  TITLE     DPP9 sequesters the C terminus of NLRP1 to repress inflammasome
            activation
  JOURNAL   Nature 592 (7856), 778-783 (2021)
   PUBMED   33731932
REFERENCE   6  (residues 1 to 829)
  AUTHORS   Chen,Y.S., Chien,C.H., Goparaju,C.M., Hsu,J.T., Liang,P.H. and
            Chen,X.
  TITLE     Purification and characterization of human prolyl dipeptidase DPP8
            in Sf9 insect cells
  JOURNAL   Protein Expr Purif 35 (1), 142-146 (2004)
   PUBMED   15039077
REFERENCE   7  (residues 1 to 829)
  AUTHORS   Shu,H., Chen,S., Bi,Q., Mumby,M. and Brekken,D.L.
  TITLE     Identification of phosphoproteins and their phosphorylation sites
            in the WEHI-231 B lymphoma cell line
  JOURNAL   Mol Cell Proteomics 3 (3), 279-286 (2004)
   PUBMED   14729942
REFERENCE   8  (residues 1 to 829)
  AUTHORS   Qi,S.Y., Riviere,P.J., Trojnar,J., Junien,J.L. and Akinsanya,K.O.
  TITLE     Cloning and characterization of dipeptidyl peptidase 10, a new
            member of an emerging subgroup of serine proteases
  JOURNAL   Biochem J 373 (Pt 1), 179-189 (2003)
   PUBMED   12662155
REFERENCE   9  (residues 1 to 829)
  AUTHORS   Ajami,K., Abbott,C.A., Obradovic,M., Gysbers,V., Kahne,T.,
            McCaughan,G.W. and Gorrell,M.D.
  TITLE     Structural requirements for catalysis, expression, and dimerization
            in the CD26/DPIV gene family
  JOURNAL   Biochemistry 42 (3), 694-701 (2003)
   PUBMED   12534281
REFERENCE   10 (residues 1 to 829)
  AUTHORS   Abbott,C.A., Yu,D.M., Woollatt,E., Sutherland,G.R., McCaughan,G.W.
            and Gorrell,M.D.
  TITLE     Cloning, expression and chromosomal localization of a novel human
            dipeptidyl peptidase (DPP) IV homolog, DPP8
  JOURNAL   Eur J Biochem 267 (20), 6140-6150 (2000)
   PUBMED   11012666
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011846.16 and AC105129.4.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047288717.1, XP_054234280.1.
            
            Summary: This gene encodes a member of the peptidase S9B family, a
            small family of dipeptidyl peptidases that are able to cleave
            peptide substrates at a prolyl bond. The encoded protein shares
            similarity with dipeptidyl peptidase IV in that it is ubiquitously
            expressed, and hydrolyzes the same substrates. These similarities
            suggest that, like dipeptidyl peptidase IV, this protein may play a
            role in T-cell activation and immune function. Alternatively
            spliced transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.2839257.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..829
                     /product="dipeptidyl peptidase 8 isoform 8"
                     /EC_number="3.4.14.5"
                     /note="prolyl dipeptidase DPP8; dipeptidyl peptidase VIII;
                     DPP VIII; dipeptidyl peptidase IV-related protein 1"
                     /calculated_mol_wt=95221
     Region          8..162
                     /region_name="Dpp_8_9_N"
                     /note="Dipeptidyl peptidase 8 and 9 N-terminal; pfam19520"
                     /db_xref="CDD:466112"
     Region          175..595
                     /region_name="DPPIV_N"
                     /note="Dipeptidyl peptidase IV (DPP IV) N-terminal region;
                     pfam00930"
                     /db_xref="CDD:395744"
     Region          687..>806
                     /region_name="Peptidase_S9"
                     /note="Prolyl oligopeptidase family; pfam00326"
                     /db_xref="CDD:459761"
     CDS             1..829
                     /gene="DPP8"
                     /gene_synonym="DP8; DPRP-1; DPRP1; MST097; MSTP097;
                     MSTP135; MSTP141"
                     /coded_by="NM_001438670.1:304..2793"
                     /note="isoform 8 is encoded by transcript variant 12"
                     /db_xref="GeneID:54878"
                     /db_xref="HGNC:HGNC:16490"
                     /db_xref="MIM:606819"
ORIGIN      
        1 mwkrseqmki ksgkcnmaaa meteqlgvei fetadceeni esqdrpklep fyveryswsq
       61 lkklladtrk yhgymmakap hdfmfvkrnd pdgphsdriy ylamsgenre ntlfyseipk
      121 tinraavlml swkplldlfq atldygmysr eeellrerkr igtvgiasyd yhqgsgtflf
      181 qagsgiyhvk dggpqgftqq plrpnlvets cpnirmdpkl cpadpdwiaf ihsndiwisn
      241 ivtreerrlt yvhnelanme edarsagvat fvlqeefdry sgywwcpkae ttpsggkilr
      301 ilyeendese veiihvtspm letrradsfr ypktgtanpk vtfkmseimi daegriidvi
      361 dkeliqpfei lfegveyiar agwtpegkya wsilldrsqt rlqivlispe lfipveddvm
      421 erqrliesvp dsvtpliiye ettdiwinih difhvfpqsh eeeiefifas ecktgfrhly
      481 kitsilkesk ykrssgglpa psdfkcpike eiaitsgewe vlgrhgsniq vdevrrlvyf
      541 egtkdspleh hlyvvsyvnp gevtrltdrg yshsccisqh cdffiskysn qknphcvsly
      601 klsspeddpt cktkefwati ldsagplpdy tppeifsfes ttgftlygml ykphdlqpgk
      661 kyptvlfiyg gpqvqlvnnr fkgvkyfrln tlaslgyvvv vidnrgschr glkfegafky
      721 kmgqieiddq veglqylasr ydfidldrvg ihgwsyggyl slmalmqrsd ifrvaiagap
      781 vtlwifydtg yterymghpd qneqgyylgs vamqaekfps esilrrdta
//
LOCUS       NP_001428011            1268 aa            linear   PRI 21-NOV-2025
DEFINITION  cohesin subunit SA-2 isoform a [Homo sapiens].
ACCESSION   NP_001428011 XP_047297731 XP_054182354
VERSION     NP_001428011.1
DBSOURCE    REFSEQ: accession NM_001441082.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1268)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1268)
  AUTHORS   Fischer,A., Hernandez-Rodriguez,B., Mulet-Lazaro,R., Nuetzel,M.,
            Holzl,F., van Herk,S., Kavelaars,F.G., Stanewsky,H., Ackermann,U.,
            Niang,A.H., Diaz,N., Reuschel,E., Strieder,N., Hernandez-Lopez,I.,
            Valk,P.J.M., Vaquerizas,J.M., Rehli,M., Delwel,R. and Gebhard,C.
  TITLE     STAG2 mutations reshape the cohesin-structured spatial chromatin
            architecture to drive gene regulation in acute myeloid leukemia
  JOURNAL   Cell Rep 43 (8), 114498 (2024)
   PUBMED   39084219
  REMARK    GeneRIF: STAG2 mutations reshape the cohesin-structured spatial
            chromatin architecture to drive gene regulation in acute myeloid
            leukemia.
REFERENCE   3  (residues 1 to 1268)
  AUTHORS   Huber,J., Tanasie,N.L., Zernia,S. and Stigler,J.
  TITLE     Single-molecule imaging reveals a direct role of CTCF's zinc
            fingers in SA interaction and cluster-dependent RNA recruitment
  JOURNAL   Nucleic Acids Res 52 (11), 6490-6506 (2024)
   PUBMED   38742641
  REMARK    GeneRIF: Single-molecule imaging reveals a direct role of CTCF's
            zinc fingers in SA interaction and cluster-dependent RNA
            recruitment.
REFERENCE   4  (residues 1 to 1268)
  AUTHORS   Xu,W., Kim,J.S., Yang,T., Ya,A., Sadzewicz,L., Tallon,L.,
            Harris,B.T., Sarkaria,J., Jin,F. and Waldman,T.
  TITLE     STAG2 mutations regulate 3D genome organization, chromatin loops,
            and Polycomb signaling in glioblastoma multiforme
  JOURNAL   J Biol Chem 300 (6), 107341 (2024)
   PUBMED   38705393
  REMARK    GeneRIF: STAG2 mutations regulate 3D genome organization, chromatin
            loops, and Polycomb signaling in glioblastoma multiforme.
REFERENCE   5  (residues 1 to 1268)
  AUTHORS   Ros-Pardo,D., Gomez-Puertas,P. and Marcos-Alcalde,I.
  TITLE     STAG2: Computational Analysis of Missense Variants Involved in
            Disease
  JOURNAL   Int J Mol Sci 25 (2), 1280 (2024)
   PUBMED   38279279
  REMARK    GeneRIF: STAG2: Computational Analysis of Missense Variants
            Involved in Disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1268)
  AUTHORS   Gregson,H.C., Schmiesing,J.A., Kim,J.S., Kobayashi,T., Zhou,S. and
            Yokomori,K.
  TITLE     A potential role for human cohesin in mitotic spindle aster
            assembly
  JOURNAL   J Biol Chem 276 (50), 47575-47582 (2001)
   PUBMED   11590136
REFERENCE   7  (residues 1 to 1268)
  AUTHORS   Sumara,I., Vorlaufer,E., Gieffers,C., Peters,B.H. and Peters,J.M.
  TITLE     Characterization of vertebrate cohesin complexes and their
            regulation in prophase
  JOURNAL   J Cell Biol 151 (4), 749-762 (2000)
   PUBMED   11076961
REFERENCE   8  (residues 1 to 1268)
  AUTHORS   Carramolino,L., Lee,B.C., Zaballos,A., Peled,A., Barthelemy,I.,
            Shav-Tal,Y., Prieto,I., Carmi,P., Gothelf,Y., Gonzalez de
            Buitrago,G., Aracil,M., Marquez,G., Barbero,J.L. and Zipori,D.
  TITLE     SA-1, a nuclear protein encoded by one member of a novel gene
            family: molecular cloning and detection in hemopoietic organs
  JOURNAL   Gene 195 (2), 151-159 (1997)
   PUBMED   9305759
  REMARK    Erratum:[Gene 1998 Jan 12;206(2):283]
REFERENCE   9  (residues 1 to 1268)
  AUTHORS   Wu,C., Friedlander,P., Lamoureux,C., Zannis-Hadjopoulos,M. and
            Price,G.B.
  TITLE     cDNA clones contain autonomous replication activity
  JOURNAL   Biochim Biophys Acta 1174 (3), 241-257 (1993)
   PUBMED   7690594
REFERENCE   10 (residues 1 to 1268)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121601.13 and AL355476.12.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297731.1, XP_054182354.1.
            
            Summary: The protein encoded by this gene is a subunit of the
            cohesin complex, which regulates the separation of sister
            chromatids during cell division. Targeted inactivation of this gene
            results in chromatid cohesion defects and aneuploidy, suggesting
            that genetic disruption of cohesin is a cause of aneuploidy in
            human cancer. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.966661.1,
                                           SRR18074969.3788333.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1268
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..1268
                     /product="cohesin subunit SA-2 isoform a"
                     /note="SCC3 homolog 2; cohesin subunit SA-2; SA2
                     stromalin; sister chromatid cohesion 3 homolog B; stromal
                     antigen 2"
                     /calculated_mol_wt=145621
     Region          102..>395
                     /region_name="IRR1"
                     /note="Cohesin [Cell division and chromosome
                     partitioning]; COG5537"
                     /db_xref="CDD:227824"
     Region          157..270
                     /region_name="STAG"
                     /note="STAG domain; pfam08514"
                     /db_xref="CDD:462502"
     CDS             1..1268
                     /gene="STAG2"
                     /gene_synonym="bA517O1.1; HPE13; MKMS; NEDXCF; SA-2; SA2;
                     SCC3B"
                     /coded_by="NM_001441082.1:353..4159"
                     /note="isoform a is encoded by transcript variant 22"
                     /db_xref="GeneID:10735"
                     /db_xref="HGNC:HGNC:11355"
                     /db_xref="MIM:300826"
ORIGIN      
        1 miaapeiptd fnllqeseth fssdtdfedi egknqkqgkg ktckkgkkgp aekgkggngg
       61 gkppsgpnrm nghhqqngve nmmlfevvkm gksamqsvvd dwiesykhdr dialldlinf
      121 fiqcsgckgv vtaemfrhmq nseiirkmte efdedsgdyp ltmagpqwkk fkssfcefig
      181 vlvrqcqysi iydeymmdtv islltglsds qvrafrhtst laamklmtal vnvalnlsin
      241 mdntqrqyea ernkmigkra nerlelllqk rkelqenqde ienmmnaifk gvfvhryrda
      301 iaeiraicie eigiwmkmys daflndsylk yvgwtmhdkq gevrlkclta lqglyynkel
      361 nsklelftsr fkdrivsmtl dkeydvavqa iklltlvlqs seevltaedc envyhlvysa
      421 hrpvavaage flykklfsrr dpeedgmmkr rgrqgpnanl vktlvfffle selhehaayl
      481 vdsmwdcate llkdwecmns llleeplsge ealtdrqesa lieimlctir qaaechppvg
      541 rgtgkrvlta kekktqlddr tkitelfava lpqllakysv daekvtnllq lpqyfdleiy
      601 ttgrlekhld allrqirniv ekhtdtdvle acsktyhalc neeftifnrv disrsqlide
      661 ladkfnrlle dflqegeepd eddayqvlst lkritafhna hdlskwdlfa cnykllktgi
      721 engdmpeqiv ihalqcthyv ilwqlakite ssstkedllr lkkqmrvfcq icqhyltnvn
      781 ttvkeqafti lcdilmifsh qimsggrdml eplvytpdss lqsellsfil dhvfieqddd
      841 nnsadgqqed easkiealhk rrnllaafck livytvvemn taadifkqym kyyndygdii
      901 ketmsktrqi dkiqcaktli lslqqlfnem iqengynfdr ssstfsgike larrfaltfg
      961 ldqlktreai amlhkdgief afkepnpqge shpplnlafl dilsefsskl lrqdkrtvyv
     1021 ylekfmtfqm slrredvwlp lmsyrnslla ggdddtmsvi sgissrgstv rskkskpstg
     1081 krkvvegmql slteessssd smwlsreqtl htpvmmqtpq ltstimrepk rlrpedsfms
     1141 vypmqtehhq tpldyntqvt wmlaqrqqee arqqqeraam syvklrtnlq hairrgtslm
     1201 eddeepived vmmssegrie dlnegmdfdt mdidlppskn rrertelkpd ffdpasimde
     1261 svlgvsmf
//
LOCUS       NP_001397910             234 aa            linear   PRI 21-NOV-2025
DEFINITION  T-cell-specific surface glycoprotein CD28 isoform 4 [Homo sapiens].
ACCESSION   NP_001397910 XP_011510496
VERSION     NP_001397910.1
DBSOURCE    REFSEQ: accession NM_001410981.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Xiong,Y., Taleb,M., Misawa,K., Hou,Z., Banerjee,S.,
            Amador-Molina,A., Jones,D.R., Chintala,N.K. and Adusumilli,P.S.
  TITLE     c-Kit signaling potentiates CAR T cell efficacy in solid tumors by
            CD28- and IL-2-independent co-stimulation
  JOURNAL   Nat Cancer 4 (7), 1001-1015 (2023)
   PUBMED   37336986
  REMARK    GeneRIF: c-Kit signaling potentiates CAR T cell efficacy in solid
            tumors by CD28- and IL-2-independent co-stimulation.
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Pulanco,M.C., Madsen,A.T., Tanwar,A., Corrigan,D.T. and Zang,X.
  TITLE     Recent advancements in the B7/CD28 immune checkpoint families: new
            biology and clinical therapeutic strategies
  JOURNAL   Cell Mol Immunol 20 (7), 694-713 (2023)
   PUBMED   37069229
  REMARK    GeneRIF: Recent advancements in the B7/CD28 immune checkpoint
            families: new biology and clinical therapeutic strategies.
            Review article
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Mai,H.L., Degauque,N., Lorent,M., Rimbert,M., Renaudin,K.,
            Danger,R., Kerleau,C., Tilly,G., Vivet,A., Le Bot,S., Delbos,F.,
            Walencik,A., Giral,M. and Brouard,S.
  TITLE     Kidney allograft rejection is associated with an imbalance of B
            cells, regulatory T cells and differentiated CD28-CD8+ T cells:
            analysis of a cohort of 1095 graft biopsies
  JOURNAL   Front Immunol 14, 1151127 (2023)
   PUBMED   37168864
  REMARK    GeneRIF: Kidney allograft rejection is associated with an imbalance
            of B cells, regulatory T cells and differentiated CD28-CD8+ T
            cells: analysis of a cohort of 1095 graft biopsies.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Gelemanovic,A., Catipovic Ardalic,T., Pribisalic,A., Hayward,C.,
            Kolcic,I. and Polasek,O.
  TITLE     Genome-Wide Meta-Analysis Identifies Multiple Novel Rare Variants
            to Predict Common Human Infectious Diseases Risk
  JOURNAL   Int J Mol Sci 24 (8), 7006 (2023)
   PUBMED   37108169
  REMARK    GeneRIF: Genome-Wide Meta-Analysis Identifies Multiple Novel Rare
            Variants to Predict Common Human Infectious Diseases Risk.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 234)
  AUTHORS   Liu,T.H., Lei,J.Y., Mai,Y.G. and Fang,J.P.
  TITLE     [Clinical Analysis of Pediatric Acute Leukemia Complicated with
            Septic Shock]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 30 (6), 1708-1714 (2022)
   PUBMED   36476893
  REMARK    GeneRIF: [Clinical Analysis of Pediatric Acute Leukemia Complicated
            with Septic Shock].
REFERENCE   6  (residues 1 to 234)
  AUTHORS   Fraser,J.D., Newton,M.E. and Weiss,A.
  TITLE     CD28 and T cell antigen receptor signal transduction coordinately
            regulate interleukin 2 gene expression in response to superantigen
            stimulation
  JOURNAL   J Exp Med 175 (4), 1131-1134 (1992)
   PUBMED   1313075
REFERENCE   7  (residues 1 to 234)
  AUTHORS   Zocchi,M.R., Poggi,A., Crosti,F., Tongiani,S. and Rugarli,C.
  TITLE     Signalling in human tumour infiltrating lymphocytes: the CD28
            molecule is functional and is physically associated with the CD45R0
            molecule
  JOURNAL   Eur J Cancer 28A (4-5), 749-754 (1992)
   PUBMED   1355979
REFERENCE   8  (residues 1 to 234)
  AUTHORS   Gimmi,C.D., Freeman,G.J., Gribben,J.G., Sugita,K., Freedman,A.S.,
            Morimoto,C. and Nadler,L.M.
  TITLE     B-cell surface antigen B7 provides a costimulatory signal that
            induces T cells to proliferate and secrete interleukin 2
  JOURNAL   Proc Natl Acad Sci U S A 88 (15), 6575-6579 (1991)
   PUBMED   1650475
REFERENCE   9  (residues 1 to 234)
  AUTHORS   Linsley,P.S., Brady,W., Grosmaire,L., Aruffo,A., Damle,N.K. and
            Ledbetter,J.A.
  TITLE     Binding of the B cell activation antigen B7 to CD28 costimulates T
            cell proliferation and interleukin 2 mRNA accumulation
  JOURNAL   J Exp Med 173 (3), 721-730 (1991)
   PUBMED   1847722
REFERENCE   10 (residues 1 to 234)
  AUTHORS   Lafage-Pochitaloff,M., Costello,R., Couez,D., Simonetti,J.,
            Mannoni,P., Mawas,C. and Olive,D.
  TITLE     Human CD28 and CTLA-4 Ig superfamily genes are located on
            chromosome 2 at bands q33-q34
  JOURNAL   Immunogenetics 31 (3), 198-201 (1990)
   PUBMED   2156778
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC125238.5.
            
            On Aug 18, 2022 this sequence version replaced XP_011510496.1.
            
            Summary: The protein encoded by this gene is essential for T-cell
            proliferation and survival, cytokine production, and T-helper
            type-2 development. Several alternatively spliced transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, Jul 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1430378.1,
                                           SRR14038193.2767416.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..234
                     /product="T-cell-specific surface glycoprotein CD28
                     isoform 4"
                     /calculated_mol_wt=26055
     Region          35..151
                     /region_name="IgV_CD28"
                     /note="Immunoglobulin Variable (IgV) domain Cluster of
                     Differentiation (CD) 28; cd20925"
                     /db_xref="CDD:409519"
     Region          35..56
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409519"
     Region          35..39
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409519"
     Region          41..44
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409519"
     Region          48..56
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409519"
     Region          57..63
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409519"
     Region          64..74
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409519"
     Region          64..71
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409519"
     Region          75..94
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409519"
     Region          77..84
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409519"
     Region          90..94
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409519"
     Region          95..128
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409519"
     Region          99..105
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409519"
     Region          108..115
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409519"
     Region          122..131
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409519"
     Region          131..136
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409519"
     Site            131..136
                     /site_type="other"
                     /note="CD28/B7 interaction site"
                     /db_xref="CDD:409519"
     Region          137..151
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409519"
     Region          137..140
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409519"
     Region          143..149
                     /region_name="Ig strand G'"
                     /note="Ig strand G' [structural motif]"
                     /db_xref="CDD:409519"
     CDS             1..234
                     /gene="CD28"
                     /gene_synonym="IMD123; Tp44"
                     /coded_by="NM_001410981.1:43..747"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS92935.1"
                     /db_xref="GeneID:940"
                     /db_xref="HGNC:HGNC:1653"
                     /db_xref="MIM:186760"
ORIGIN      
        1 mpcglsalim cpkgmvavvv avddgdsqal agnkilvkqs pmlvaydnav nlsckysynl
       61 fsrefraslh kgldsavevc vvygnysqql qvysktgfnc dgklgnesvt fylqnlyvnq
      121 tdiyfckiev mypppyldne ksngtiihvk gkhlcpsplf pgpskpfwvl vvvggvlacy
      181 sllvtvafii fwvrskrsrl lhsdymnmtp rrpgptrkhy qpyapprdfa ayrs
//
LOCUS       NP_001426131             212 aa            linear   PRI 21-NOV-2025
DEFINITION  programmed cell death protein 10 [Homo sapiens].
ACCESSION   NP_001426131 XP_005247143 XP_054201069
VERSION     NP_001426131.1
DBSOURCE    REFSEQ: accession NM_001439202.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Li,Y., Liu,Y., Liu,K., Tao,T., Yang,L., Liu,R., Zhou,H., Liang,D.,
            Zhang,Y., Huang,D. and Sun,Y.
  TITLE     Study on the role of CCM3 gene and lead exposure induced
            neurotoxicity through neurovascular units
  JOURNAL   Ecotoxicol Environ Saf 277, 116269 (2024)
   PUBMED   38657460
  REMARK    GeneRIF: Study on the role of CCM3 gene and lead exposure induced
            neurotoxicity through neurovascular units.
REFERENCE   3  (residues 1 to 212)
  AUTHORS   da Fontoura Galvao,G., da Silva,E.V., Trefilio,L.M.,
            Alves-Leon,S.V., Fontes-Dantas,F.L. and de Souza,J.M.
  TITLE     Comprehensive CCM3 Mutational Analysis in Two Patients with
            Syndromic Cerebral Cavernous Malformation
  JOURNAL   Transl Stroke Res 15 (2), 411-421 (2024)
   PUBMED   36723700
  REMARK    GeneRIF: Comprehensive CCM3 Mutational Analysis in Two Patients
            with Syndromic Cerebral Cavernous Malformation.
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Tang,L., Zhou,M., Xu,Y., Peng,B., Gao,Y. and Mo,Y.
  TITLE     Knockdown of CCM3 promotes angiogenesis through activation and
            nuclear translocation of YAP/TAZ
  JOURNAL   Biochem Biophys Res Commun 701, 149525 (2024)
   PUBMED   38320423
  REMARK    GeneRIF: Knockdown of CCM3 promotes angiogenesis through activation
            and nuclear translocation of YAP/TAZ.
REFERENCE   5  (residues 1 to 212)
  AUTHORS   Ni,W.J. and Leng,X.M.
  TITLE     Programmed cell death 10 can be used as a potential biomarker for
            ankylosing spondylitis diagnosis and treatment
  JOURNAL   Spinal Cord 62 (3), 99-103 (2024)
   PUBMED   38158408
  REMARK    GeneRIF: Programmed cell death 10 can be used as a potential
            biomarker for ankylosing spondylitis diagnosis and treatment.
REFERENCE   6  (residues 1 to 212)
  AUTHORS   Guclu,B., Ozturk,A.K., Pricola,K.L., Bilguvar,K., Shin,D.,
            O'Roak,B.J. and Gunel,M.
  TITLE     Mutations in apoptosis-related gene, PDCD10, cause cerebral
            cavernous malformation 3
  JOURNAL   Neurosurgery 57 (5), 1008-1013 (2005)
   PUBMED   16284570
  REMARK    GeneRIF: Mutations in apoptosis-related gene, PDCD10, cause
            cerebral cavernous malformation 3.
REFERENCE   7  (residues 1 to 212)
  AUTHORS   Guclu,B., Ozturk,A.K., Pricola,K.L., Seker,A., Ozek,M. and Gunel,M.
  TITLE     Cerebral venous malformations have distinct genetic origin from
            cerebral cavernous malformations
  JOURNAL   Stroke 36 (11), 2479-2480 (2005)
   PUBMED   16239636
  REMARK    GeneRIF: KRIT1, Malcavernin, and PDCD10 are differentially
            expressed in cerebral venous malformations and cerebral cavernous
            malformations
REFERENCE   8  (residues 1 to 212)
  AUTHORS   Bergametti,F., Denier,C., Labauge,P., Arnoult,M., Boetto,S.,
            Clanet,M., Coubes,P., Echenne,B., Ibrahim,R., Irthum,B.,
            Jacquet,G., Lonjon,M., Moreau,J.J., Neau,J.P., Parker,F.,
            Tremoulet,M. and Tournier-Lasserve,E.
  CONSRTM   Societe Francaise de Neurochirurgie
  TITLE     Mutations within the programmed cell death 10 gene cause cerebral
            cavernous malformations
  JOURNAL   Am J Hum Genet 76 (1), 42-51 (2005)
   PUBMED   15543491
  REMARK    GeneRIF: We report herein the identification of PDCD10 (programmed
            cell death 10) as the CCM3 gene.
REFERENCE   9  (residues 1 to 212)
  AUTHORS   Craig,H.D., Gunel,M., Cepeda,O., Johnson,E.W., Ptacek,L.,
            Steinberg,G.K., Ogilvy,C.S., Berg,M.J., Crawford,S.C., Scott,R.M.,
            Steichen-Gersdorf,E., Sabroe,R., Kennedy,C.T., Mettler,G.,
            Beis,M.J., Fryer,A., Awad,I.A. and Lifton,R.P.
  TITLE     Multilocus linkage identifies two new loci for a mendelian form of
            stroke, cerebral cavernous malformation, at 7p15-13 and 3q25.2-27
  JOURNAL   Hum Mol Genet 7 (12), 1851-1858 (1998)
   PUBMED   9811928
REFERENCE   10 (residues 1 to 212)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079822.13.
            
            On or before Apr 28, 2025 this sequence version replaced
            XP_005247143.1, XP_054201069.1.
            
            Summary: This gene encodes an evolutionarily conserved protein
            associated with cell apoptosis. The protein interacts with the
            serine/threonine protein kinase MST4 to modulate the extracellular
            signal-regulated kinase (ERK) pathway. It also interacts with and
            is phosphoryated by serine/threonine kinase 25, and is thought to
            function in a signaling pathway essential for vascular developent.
            Mutations in this gene are one cause of cerebral cavernous
            malformations, which are vascular malformations that cause seizures
            and cerebral hemorrhages. Multiple alternatively spliced variants,
            encoding the same protein, have been identified. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2668007.1,
                                           SRR5189661.182991.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.1"
     Protein         1..212
                     /product="programmed cell death protein 10"
                     /note="apoptosis-related protein 15; TF-1 cell
                     apoptosis-related protein 15; cerebral cavernous
                     malformations 3 protein"
                     /calculated_mol_wt=24571
     Region          14..161
                     /region_name="DUF1241"
                     /note="Protein of unknown function (DUF1241); pfam06840"
                     /db_xref="CDD:462018"
     Site            179
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BUL8.1)"
     CDS             1..212
                     /gene="PDCD10"
                     /gene_synonym="CCM3; TFAR15"
                     /coded_by="NM_001439202.1:336..974"
                     /db_xref="GeneID:11235"
                     /db_xref="HGNC:HGNC:8761"
                     /db_xref="MIM:609118"
ORIGIN      
        1 mrmtmeemkn eaettsmvsm plyavmypvf nelervnlsa aqtlraafik aekenpgltq
       61 diimkilekk svevnftesl lrmaaddvee ymierpepef qdlnekaral kqilskipde
      121 indrvrflqt ikdiasaike lldtvnnvfk kyqyqnrral ehqkkefvky sksfsdtlkt
      181 yfkdgkainv fvsanrlihq tnlilqtfkt va
//
LOCUS       NP_001427587             735 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 3 isoform 7 [Homo sapiens].
ACCESSION   NP_001427587
VERSION     NP_001427587.1
DBSOURCE    REFSEQ: accession NM_001440658.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 735)
  AUTHORS   Ghashghaei,M., Liu,Y., Ettles,J., Bombaci,G., Ramkumar,N., Liu,Z.,
            Escano,L., Miko,S.S., Kim,Y., Waldron,J.A., Do,K., MacPherson,K.,
            Yuen,K.A., Taibi,T., Yue,M., Arsalan,A., Jin,Z., Edin,G.,
            Karsan,A., Morin,G.B., Kuchenbauer,F., Perna,F., Bushell,M. and
            Vu,L.P.
  TITLE     Translation efficiency driven by CNOT3 subunit of the CCR4-NOT
            complex promotes leukemogenesis
  JOURNAL   Nat Commun 15 (1), 2340 (2024)
   PUBMED   38491013
  REMARK    GeneRIF: Translation efficiency driven by CNOT3 subunit of the
            CCR4-NOT complex promotes leukemogenesis.
            Erratum:[Nat Commun. 2024 Oct 7;15(1):8674. doi:
            10.1038/s41467-024-53071-1. PMID: 39375334]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 735)
  AUTHORS   Burgess,H.M., Grande,R., Riccio,S., Dinesh,I., Winkler,G.S.,
            Depledge,D.P. and Mohr,I.
  TITLE     CCR4-NOT differentially controls host versus virus poly(a)-tail
            length and regulates HCMV infection
  JOURNAL   EMBO Rep 24 (12), e56327 (2023)
   PUBMED   37846490
  REMARK    GeneRIF: CCR4-NOT differentially controls host versus virus
            poly(a)-tail length and regulates HCMV infection.
REFERENCE   4  (residues 1 to 735)
  AUTHORS   Zhao,P., Meng,Q., Wan,C., Lei,T., Zhang,L., Zhang,X., Tan,L.,
            Zhu,H. and He,X.
  TITLE     Clinical features of CNOT3-associated neurodevelopmental disorder
            in three Chinese patients
  JOURNAL   Neurogenetics 24 (2), 129-136 (2023)
   PUBMED   36802310
  REMARK    GeneRIF: Clinical features of CNOT3-associated neurodevelopmental
            disorder in three Chinese patients.
REFERENCE   5  (residues 1 to 735)
  AUTHORS   McLenachan,S., Zhang,D., Grainok,J., Zhang,X., Huang,Z., Chen,S.C.,
            Zaw,K., Lima,A., Jennings,L., Roshandel,D., Moon,S.Y., Heath
            Jeffery,R.C., Attia,M.S., Thompson,J.A., Lamey,T.M., McLaren,T.L.,
            De Roach,J., Fletcher,S. and Chen,F.K.
  TITLE     Determinants of Disease Penetrance in PRPF31-Associated Retinopathy
  JOURNAL   Genes (Basel) 12 (10), 1542 (2021)
   PUBMED   34680937
  REMARK    GeneRIF: Determinants of Disease Penetrance in PRPF31-Associated
            Retinopathy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 735)
  AUTHORS   Yin,X., Warner,D.R., Roberts,E.A., Pisano,M.M. and Greene,R.M.
  TITLE     Identification of novel CBP interacting proteins in embryonic
            orofacial tissue
  JOURNAL   Biochem Biophys Res Commun 329 (3), 1010-1017 (2005)
   PUBMED   15752756
REFERENCE   7  (residues 1 to 735)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 735)
  AUTHORS   Aoki,T., Okada,N., Wakamatsu,T. and Tamura,T.A.
  TITLE     TBP-interacting protein 120B, which is induced in relation to
            myogenesis, binds to NOT3
  JOURNAL   Biochem Biophys Res Commun 296 (5), 1097-1103 (2002)
   PUBMED   12207886
  REMARK    GeneRIF: TBP-interacting protein 120B binds to NOT3
REFERENCE   9  (residues 1 to 735)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
REFERENCE   10 (residues 1 to 735)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC245052.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.974309.1,
                                           SRR14038192.4129740.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..735
                     /product="CCR4-NOT transcription complex subunit 3 isoform
                     7"
                     /note="NOT3 (negative regulator of transcription 3, yeast)
                     homolog; CCR4-associated factor 3; leukocyte receptor
                     cluster member 2"
                     /calculated_mol_wt=79042
     Region          3..229
                     /region_name="Not3"
                     /note="Not1 N-terminal domain, CCR4-Not complex component;
                     pfam04065"
                     /db_xref="CDD:461155"
     Region          240..534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75175.1)"
     Region          <288..659
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Region          620..721
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..735
                     /gene="CNOT3"
                     /gene_synonym="IDDSADF; LENG2; NOT3; NOT3H"
                     /coded_by="NM_001440658.1:283..2490"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:4849"
                     /db_xref="HGNC:HGNC:7879"
                     /db_xref="MIM:604910"
ORIGIN      
        1 madkrklqge idrclkkvse gveqfediwq klhnaananq kekyeadlkk eikklqrlrd
       61 qiktwvasne ikdkrqlidn rklietqmer fkvveretkt kayskeglgl aqkvdpaqke
      121 keevgqwltn tidtlnmqvd qfesevesls vqtrkkkgdk dkqdrieglk rhiekhryhv
      181 rmletilrml dndsilvdai rkikddveyy vdssqdpdfe eneflyddld ledipqalva
      241 tsppshshme deifnqssst ptsttssspi ppspanctte nseddkkrgr stdsevsqsp
      301 akngskpvhs nqhpqspavp ptypsgpppa asalsttpgn ngvpapaapp salgpkaspa
      361 pshnsgtpap yaqavappap sgpsttqprp psvqpsgggg ggsggggsss ssnssaggga
      421 gkqngatsys svvadspaev alsssggnna ssqalgppsg phnpppstsk epsaaaptga
      481 ggvapgsgnn sggpsllvpl pvnppssptp sfsdakaaga llngppqfst apeikapepl
      541 sslksmaera aissgiedpv ptlhlterdi ilsstsappa saqpplqlse vniplslgvc
      601 plgpvpltke qlyqqameea awhhmphpsd serirqylpr npcptppyhh qmppphsdtv
      661 efyqrlstet lffifyyleg tkaqylaaka lkkqswrfht kymmwfqrhe epktitdefe
      721 qvrappplfp llglg
//
LOCUS       NP_001425134             687 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase tousled-like 2 isoform G [Homo
            sapiens].
ACCESSION   NP_001425134 XP_016879543 XP_054170780
VERSION     NP_001425134.1
DBSOURCE    REFSEQ: accession NM_001438205.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Liang,B., Yin,J.J., Zhang,S.N., Zhang,C., Hu,Z.L. and Wang,Y.
  TITLE     [Effect of TLK2 Expression Regulated by MiR-21 on Proliferation and
            Apoptosis of Acute Myeloid Leukemia Cells]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 32 (3), 658-662 (2024)
   PUBMED   38926950
  REMARK    GeneRIF: [Effect of TLK2 Expression Regulated by MiR-21 on
            Proliferation and Apoptosis of Acute Myeloid Leukemia Cells].
REFERENCE   3  (residues 1 to 687)
  AUTHORS   Ronald,S., Sunavala-Dossabhoy,G., Adams,L., Williams,B. and De
            Benedetti,A.
  TITLE     The expression of Tousled kinases in CaP cell lines and its
            relation to radiation response and DSB repair
  JOURNAL   Prostate 71 (13), 1367-1373 (2011)
   PUBMED   21647934
  REMARK    GeneRIF: TLKs appear to be intimately linked to the pattern of
            resistance to DNA damage, and specifically double-strand breaks.
REFERENCE   4  (residues 1 to 687)
  AUTHORS   Couch,F.J., Wang,X., Bamlet,W.R., de Andrade,M., Petersen,G.M. and
            McWilliams,R.R.
  TITLE     Association of mitotic regulation pathway polymorphisms with
            pancreatic cancer risk and outcome
  JOURNAL   Cancer Epidemiol Biomarkers Prev 19 (1), 251-257 (2010)
   PUBMED   20056645
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   5  (residues 1 to 687)
  AUTHORS   Pilyugin,M., Demmers,J., Verrijzer,C.P., Karch,F. and Moshkin,Y.M.
  TITLE     Phosphorylation-mediated control of histone chaperone ASF1 levels
            by Tousled-like kinases
  JOURNAL   PLoS One 4 (12), e8328 (2009)
   PUBMED   20016786
  REMARK    GeneRIF: ASF1 cellular levels are tightly controlled by distinct
            pathways and provide a molecular mechanism for post-translational
            regulation of dASF1 and hASF1a by TLK kinases.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 687)
  AUTHORS   Groth,A., Lukas,J., Nigg,E.A., Sillje,H.H., Wernstedt,C., Bartek,J.
            and Hansen,K.
  TITLE     Human Tousled like kinases are targeted by an ATM- and
            Chk1-dependent DNA damage checkpoint
  JOURNAL   EMBO J 22 (7), 1676-1687 (2003)
   PUBMED   12660173
REFERENCE   7  (residues 1 to 687)
  AUTHORS   Sillje,H.H. and Nigg,E.A.
  TITLE     Identification of human Asf1 chromatin assembly factors as
            substrates of Tousled-like kinases
  JOURNAL   Curr Biol 11 (13), 1068-1073 (2001)
   PUBMED   11470414
REFERENCE   8  (residues 1 to 687)
  AUTHORS   Sillje,H.H., Takahashi,K., Tanaka,K., Van Houwe,G. and Nigg,E.A.
  TITLE     Mammalian homologues of the plant Tousled gene code for
            cell-cycle-regulated kinases with maximal activities linked to
            ongoing DNA replication
  JOURNAL   EMBO J 18 (20), 5691-5702 (1999)
   PUBMED   10523312
REFERENCE   9  (residues 1 to 687)
  AUTHORS   Zhang,S., Xing,H. and Muslin,A.J.
  TITLE     Nuclear localization of protein kinase U-alpha is regulated by
            14-3-3
  JOURNAL   J Biol Chem 274 (35), 24865-24872 (1999)
   PUBMED   10455159
REFERENCE   10 (residues 1 to 687)
  AUTHORS   Yamakawa,A., Kameoka,Y., Hashimoto,K., Yoshitake,Y., Nishikawa,K.,
            Tanihara,K. and Date,T.
  TITLE     cDNA cloning and chromosomal mapping of genes encoding novel
            protein kinases termed PKU-alpha and PKU-beta, which have nuclear
            localization signal
  JOURNAL   Gene 202 (1-2), 193-201 (1997)
   PUBMED   9427565
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008026.7 and AC080038.5.
            
            On or before Apr 16, 2025 this sequence version replaced
            XP_016879543.1, XP_054170780.1.
            
            Summary: This gene encodes a nuclear serine/threonine kinase that
            was first identified in Arabidopsis. The encoded protein is thought
            to function in the regulation of chromatin assembly in the S phase
            of the cell cycle by regulating the levels of a histone H3/H4
            chaperone. This protein is associated with double-strand break
            repair of DNA damage caused by radiation. Pseudogenes of this gene
            are present on chromosomes 10 and 17. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.166341.1,
                                           SRR18074967.1003403.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.2"
     Protein         1..687
                     /product="serine/threonine-protein kinase tousled-like 2
                     isoform G"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase tousled-like 2"
                     /calculated_mol_wt=78375
     Region          370..678
                     /region_name="STKc_TLK2"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Tousled-Like Kinase 2; cd14041"
                     /db_xref="CDD:270943"
     Site            order(383..387,391,404,406,442,459..462,466,468,507,509,
                     511..512,514,528,531,554..557)
                     /site_type="active"
                     /db_xref="CDD:270943"
     Site            order(383..387,391,404,406,442,459..462,466,507,509,
                     511..512,514,528)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270943"
     Site            order(387,466,468,507,509,511,531,554..557)
                     /site_type="other"
                     /note="polypeptide substrate binding site"
                     /db_xref="CDD:270943"
     Site            order(527..533,554..557)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270943"
     CDS             1..687
                     /gene="TLK2"
                     /gene_synonym="HsHPK; MRD57; PKU-ALPHA"
                     /coded_by="NM_001438205.1:179..2242"
                     /note="isoform G is encoded by transcript variant M"
                     /db_xref="GeneID:11011"
                     /db_xref="HGNC:HGNC:11842"
                     /db_xref="MIM:608439"
ORIGIN      
        1 mmeelhsldp rrqellearf tgvgvskgpl nsessnqslc svgslsdkev etpekkqndq
       61 rnrkrkaepy etsqgkgtpr ghkisdyfef aggsapgtsp grsvppvars spqhslsnpl
      121 prrveqplyg ldgsaakeat eeqsalptlm svmlakprld teqlaqrgag lcftfvsanc
      181 dlrrqideqq kmlekykerl nrcvtmskkl liekskqekm acrdksmqdr lrlghfttvr
      241 hgasfteqwt dgyafqnlik qqerinsqre eierqrkmla krkppamgqa ppatneqkqr
      301 ksktngaene tltlaeyheq eeifklrlgh lkkeeaeiqa elerlervrn lhirelkrih
      361 nednsqfkdh ptlndrylll hllgrggfse vykafdlteq ryvavkihql nknwrdekke
      421 nyhkhacrey rihkeldhpr ivklydyfsl dtdsfctvle ycegndldfy lkqhklmsek
      481 earsiimqiv nalkylneik ppiihydlkp gnillvngta cgeikitdfg lskimdddsy
      541 nsvdgmelts qgagtywylp pecfvvgkep pkisnkvdvw svgvifyqcl ygrkpfghnq
      601 sqqdilqent ilkatevqfp pkpvvtpeak afirrclayr kedridvqql acdpyllphi
      661 rksvstsspa gaaiastsga snnsssn
//
LOCUS       NP_001191455             184 aa            linear   PRI 21-NOV-2025
DEFINITION  translocon-associated protein subunit delta isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_001191455
VERSION     NP_001191455.1
DBSOURCE    REFSEQ: accession NM_001204526.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Gemmer,M., Chaillet,M.L., van Loenhout,J., Cuevas Arenas,R.,
            Vismpas,D., Grollers-Mulderij,M., Koh,F.A., Albanese,P.,
            Scheltema,R.A., Howes,S.C., Kotecha,A., Fedry,J. and Forster,F.
  TITLE     Visualization of translation and protein biogenesis at the ER
            membrane
  JOURNAL   Nature 614 (7946), 160-167 (2023)
   PUBMED   36697828
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Castiglioni,C., Feillet,F., Barnerias,C., Wiedemann,A., Muchart,J.,
            Cortes,F., Hernando-Davalillo,C., Montero,R., Dupre,T., Bruneel,A.,
            Seta,N., Vuillaumier-Barrot,S. and Serrano,M.
  TITLE     Expanding the phenotype of X-linked SSR4-CDG: Connective tissue
            implications
  JOURNAL   Hum Mutat 42 (2), 142-149 (2021)
   PUBMED   33300232
  REMARK    GeneRIF: Expanding the phenotype of X-linked SSR4-CDG: Connective
            tissue implications.
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Ng,B.G., Raymond,K., Kircher,M., Buckingham,K.J., Wood,T.,
            Shendure,J., Nickerson,D.A., Bamshad,M.J., Wong,J.T.,
            Monteiro,F.P., Graham,B.H., Jackson,S., Sparkes,R., Scheuerle,A.E.,
            Cathey,S., Kok,F., Gibson,J.B. and Freeze,H.H.
  CONSRTM   University of Washington Center for Mendelian Genomics
  TITLE     Expanding the Molecular and Clinical Phenotype of SSR4-CDG
  JOURNAL   Hum Mutat 36 (11), 1048-1051 (2015)
   PUBMED   26264460
  REMARK    GeneRIF: We now report eight affected males with either de novo (4)
            or inherited (4) loss of function mutations in SSR4.
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Wang,Z. and VandeBerg,J.L.
  TITLE     Cloning and molecular characterization of a human ortholog of
            Monodelphis TRAPD in ultraviolet B-induced melanoma
  JOURNAL   Melanoma Res 14 (2), 107-114 (2004)
   PUBMED   15057039
  REMARK    GeneRIF: results of this study implicate TRAPD as a candidate gene
            with potential functions that might be associated with
            ultraviolet-induced melanomagenesis and metastasis
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Dodson,G. and Steiner,D.
  TITLE     The role of assembly in insulin's biosynthesis
  JOURNAL   Curr Opin Struct Biol 8 (2), 189-194 (1998)
   PUBMED   9631292
  REMARK    Review article
REFERENCE   7  (residues 1 to 184)
  AUTHORS   Brenner,V., Nyakatura,G., Rosenthal,A. and Platzer,M.
  TITLE     Genomic organization of two novel genes on human Xq28: compact head
            to head arrangement of IDH gamma and TRAP delta is conserved in rat
            and mouse
  JOURNAL   Genomics 44 (1), 8-14 (1997)
   PUBMED   9286695
REFERENCE   8  (residues 1 to 184)
  AUTHORS   Holthuis,J.C., van Riel,M.C. and Martens,G.J.
  TITLE     Translocon-associated protein TRAP delta and a novel TRAP-like
            protein are coordinately expressed with pro-opiomelanocortin in
            Xenopus intermediate pituitary
  JOURNAL   Biochem J 312 (Pt 1) (Pt 1), 205-213 (1995)
   PUBMED   7492314
REFERENCE   9  (residues 1 to 184)
  AUTHORS   Hartmann,E., Gorlich,D., Kostka,S., Otto,A., Kraft,R., Knespel,S.,
            Burger,E., Rapoport,T.A. and Prehn,S.
  TITLE     A tetrameric complex of membrane proteins in the endoplasmic
            reticulum
  JOURNAL   Eur J Biochem 214 (2), 375-381 (1993)
   PUBMED   7916687
REFERENCE   10 (residues 1 to 184)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U52111.3.
            
            Summary: This gene encodes the delta subunit of the
            translocon-associated protein complex which is involved in
            translocating proteins across the endoplasmic reticulum membrane.
            The encoded protein is located in the Xq28 region and is arranged
            in a compact head-to-head manner with the isocitrate dehydrogenase
            3 (NAD+) gamma gene and both genes are driven by a CpG-embedded
            bidirectional promoter. Alternate splicing results in multiple
            transcript variants.[provided by RefSeq, Mar 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032351.1, BM690567.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..184
                     /product="translocon-associated protein subunit delta
                     isoform 1 precursor"
                     /note="translocon-associated protein subunit delta;
                     SSR-delta; TRAP-delta; signal sequence receptor, delta"
                     /calculated_mol_wt=16766
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3465
     mat_peptide     35..184
                     /product="translocon-associated protein subunit delta
                     isoform 1"
                     /calculated_mol_wt=16766
     Region          35..183
                     /region_name="TRAP-delta"
                     /note="Translocon-associated protein, delta subunit
                     precursor (TRAP-delta); pfam05404"
                     /db_xref="CDD:398850"
     CDS             1..184
                     /gene="SSR4"
                     /gene_synonym="CDG1Y; TRAPD"
                     /coded_by="NM_001204526.2:119..673"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:6748"
                     /db_xref="HGNC:HGNC:11326"
                     /db_xref="MIM:300090"
ORIGIN      
        1 mpaqpfgree amaamaslga lallllssls rcsaeaclep qitpsyytts davistetvf
       61 iveisltckn rvqnmalyad vggkqfpvtr gqdvgryqvs wsldhksaha gtyevrffde
      121 esysllrkaq rnnedisiip plftvsvdhr gtwngpwvst evlaaaiglv iyylafsaks
      181 hiqa
//
LOCUS       NP_001393538            1149 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 8 [Homo sapiens].
ACCESSION   NP_001393538 XP_047279793
VERSION     NP_001393538.1
DBSOURCE    REFSEQ: accession NM_001406609.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1149)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1149)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1149)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1149)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1149)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1149)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1149)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1149)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1149)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1149)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            On May 18, 2022 this sequence version replaced XP_047279793.1.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2922382.1,
                                           SRR18074967.4051220.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1149
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1149
                     /product="hamartin isoform 8"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=127998
     Region          7..718
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          402..786
                     /region_name="Mediates interaction with WDR45B.
                     /evidence=ECO:0000269|PubMed:28561066"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Region          438..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <704..>941
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          991..1070
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1085
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1116..1149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1149
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406609.1:189..3638"
                     /note="isoform 8 is encoded by transcript variant 23"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt ggkgtplgtp atspppaplc hsddyvhisl pqatvtpprk
      421 eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed siekdkeeaa
      481 isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv npeplhssld
      541 klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp trvgfgsgqp
      601 ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr liqqgadahs
      661 kelnklplps ksvdwthfgg sppsdeirtl rdqllllhnq llyerfkrqq halrnrrllr
      721 kvikaaalee hnaamkdqlk lqekdiqmwk vslqkeqary nqlqeqrdtm vtklhsqirq
      781 lqhdreefyn qsqelqtkle dcrnmiaelr ielkkannkl snsesvqqqm eflnrqllvl
      841 gevnelyleq lqnkhsdttk evemmkaayr keleknrshv lqqtqrldts qkrilelesh
      901 lakkdhllle qkkyledvkl qargqlqaae sryeaqkrit qvfeleildl ygrlekdgll
      961 kkleeekaea aeaaeerldc cndgcsdsmv ghneeasghn getktprpss argssgsrgg
     1021 ggssssssel stpekpphqr agpfssrwet tmgeasasip ttvgslpssk sflgmkarel
     1081 frnksesqcd edgmtsslse slktelgkdl gveakiplnl dgphpspptp dsvgqlhimd
     1141 ynethhehs
//
LOCUS       NP_001428148             532 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 6 [Homo sapiens].
ACCESSION   NP_001428148 XP_011537421 XP_054220457
VERSION     NP_001428148.1
DBSOURCE    REFSEQ: accession NM_001441219.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 532)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 532)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 532)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 532)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 532)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 532)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            On or before Jun 5, 2025 this sequence version replaced
            XP_011537421.1, XP_054220457.1.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.978557.1,
                                           SRR14038196.1736274.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..532
                     /product="calcium uptake protein 1, mitochondrial isoform
                     6"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=61083
     Region          <179..>243
                     /region_name="CCDC34"
                     /note="Coiled-coil domain-containing protein 3; pfam13904"
                     /db_xref="CDD:464032"
     Region          278..497
                     /region_name="EFh_MICU1"
                     /note="EF-hand, calcium binding motif, found in calcium
                     uptake protein 1, mitochondrial (MICU1) and similar
                     proteins; cd16173"
                     /db_xref="CDD:320081"
     Region          278..307
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Site            order(280,432,435,438..439,441,459)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:320081"
     Site            order(287,289,291,298,477,479,481,488)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320081"
     Region          333..363
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          431..460
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          468..497
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     CDS             1..532
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001441219.1:72..1670"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mfrlnslsal aelavgsrwy hggsqpiqir rrlmmvaflg asavtastgl lwkrahaesp
       61 pcvdnlksdi gdkgknkdeg dvcnhekkta dlaphpeekk kkrsgfrdrk vmeyenrira
      121 ystpdkifry fatlkvisep geaevfmtpe dfvrsitpne kqpehlgldq yiikrfdgka
      181 rfskkkilhr vrkkskgsil qrrkkalqke ertrhgstkh neqevrrtim ewlekkisqe
      241 rekfadegsi fytlgecgli sfsdyifltt vlstpqrnfe iafkmfdlng dgevdmeefe
      301 qvqsiirsqt smgmrhrdrp ttgntlksgl csalttyffg adlkgkltik nflefqrklq
      361 hdvlklefer hdpvdgrite rqfggmllay sgvqskklta mqrqlkkhfk egkgltfqev
      421 enfftflkni ndvdtalsfy hmagasldkv tmqqvartva kvelsdhvcd vvfalfdcdg
      481 ngelsnkefv simkqrlmrg lekpkdmgft rlmqamwkca qetawdfalp kq
//
LOCUS       NP_001411266              60 aa            linear   PRI 21-NOV-2025
DEFINITION  protein cholesin isoform d [Homo sapiens].
ACCESSION   NP_001411266
VERSION     NP_001411266.1
DBSOURCE    REFSEQ: accession NM_001424337.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 60)
  AUTHORS   Ryk,A., Marcinkiewicz,A., Chrzanowski,J., Michalak,A.M., Drozdz,I.,
            Burzynski,J., Krejca,M. and Fendler,W.
  TITLE     Cholesin receptor signalling is active in cardiovascular
            system-associated adipose tissue and correlates with SGLT2i
            treatment in patients with diabetes
  JOURNAL   Cardiovasc Diabetol 23 (1), 211 (2024)
   PUBMED   38902687
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 60)
  AUTHORS   Hu,X., Chen,F., Jia,L., Long,A., Peng,Y., Li,X., Huang,J., Wei,X.,
            Fang,X., Gao,Z., Zhang,M., Liu,X., Chen,Y.G., Wang,Y., Zhang,H. and
            Wang,Y.
  TITLE     A gut-derived hormone regulates cholesterol metabolism
  JOURNAL   Cell 187 (7), 1685-1700 (2024)
   PUBMED   38503280
  REMARK    GeneRIF: A gut-derived hormone regulates cholesterol metabolism.
REFERENCE   3  (residues 1 to 60)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 60)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 60)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 60)
  AUTHORS   Willer,C.J., Schmidt,E.M., Sengupta,S., Peloso,G.M., Gustafsson,S.,
            Kanoni,S., Ganna,A., Chen,J., Buchkovich,M.L., Mora,S.,
            Beckmann,J.S., Bragg-Gresham,J.L., Chang,H.Y., Demirkan,A., Den
            Hertog,H.M., Do,R., Donnelly,L.A., Ehret,G.B., Esko,T.,
            Feitosa,M.F., Ferreira,T., Fischer,K., Fontanillas,P., Fraser,R.M.,
            Freitag,D.F., Gurdasani,D., Heikkila,K., Hypponen,E., Isaacs,A.,
            Jackson,A.U., Johansson,A., Johnson,T., Kaakinen,M., Kettunen,J.,
            Kleber,M.E., Li,X., Luan,J., Lyytikainen,L.P., Magnusson,P.K.E.,
            Mangino,M., Mihailov,E., Montasser,M.E., Muller-Nurasyid,M.,
            Nolte,I.M., O'Connell,J.R., Palmer,C.D., Perola,M., Petersen,A.K.,
            Sanna,S., Saxena,R., Service,S.K., Shah,S., Shungin,D., Sidore,C.,
            Song,C., Strawbridge,R.J., Surakka,I., Tanaka,T., Teslovich,T.M.,
            Thorleifsson,G., Van den Herik,E.G., Voight,B.F., Volcik,K.A.,
            Waite,L.L., Wong,A., Wu,Y., Zhang,W., Absher,D., Asiki,G.,
            Barroso,I., Been,L.F., Bolton,J.L., Bonnycastle,L.L., Brambilla,P.,
            Burnett,M.S., Cesana,G., Dimitriou,M., Doney,A.S.F., Doring,A.,
            Elliott,P., Epstein,S.E., Ingi Eyjolfsson,G., Gigante,B.,
            Goodarzi,M.O., Grallert,H., Gravito,M.L., Groves,C.J., Hallmans,G.,
            Hartikainen,A.L., Hayward,C., Hernandez,D., Hicks,A.A., Holm,H.,
            Hung,Y.J., Illig,T., Jones,M.R., Kaleebu,P., Kastelein,J.J.P.,
            Khaw,K.T., Kim,E., Klopp,N., Komulainen,P., Kumari,M.,
            Langenberg,C., Lehtimaki,T., Lin,S.Y., Lindstrom,J., Loos,R.J.F.,
            Mach,F., McArdle,W.L., Meisinger,C., Mitchell,B.D., Muller,G.,
            Nagaraja,R., Narisu,N., Nieminen,T.V.M., Nsubuga,R.N., Olafsson,I.,
            Ong,K.K., Palotie,A., Papamarkou,T., Pomilla,C., Pouta,A.,
            Rader,D.J., Reilly,M.P., Ridker,P.M., Rivadeneira,F., Rudan,I.,
            Ruokonen,A., Samani,N., Scharnagl,H., Seeley,J., Silander,K.,
            Stancakova,A., Stirrups,K., Swift,A.J., Tiret,L.,
            Uitterlinden,A.G., van Pelt,L.J., Vedantam,S., Wainwright,N.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilsgaard,T., Wilson,J.F.,
            Young,E.H., Zhao,J.H., Adair,L.S., Arveiler,D., Assimes,T.L.,
            Bandinelli,S., Bennett,F., Bochud,M., Boehm,B.O., Boomsma,D.I.,
            Borecki,I.B., Bornstein,S.R., Bovet,P., Burnier,M., Campbell,H.,
            Chakravarti,A., Chambers,J.C., Chen,Y.I., Collins,F.S.,
            Cooper,R.S., Danesh,J., Dedoussis,G., de Faire,U., Feranil,A.B.,
            Ferrieres,J., Ferrucci,L., Freimer,N.B., Gieger,C., Groop,L.C.,
            Gudnason,V., Gyllensten,U., Hamsten,A., Harris,T.B., Hingorani,A.,
            Hirschhorn,J.N., Hofman,A., Hovingh,G.K., Hsiung,C.A.,
            Humphries,S.E., Hunt,S.C., Hveem,K., Iribarren,C., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kaprio,J., Kesaniemi,A., Kivimaki,M.,
            Kooner,J.S., Koudstaal,P.J., Krauss,R.M., Kuh,D., Kuusisto,J.,
            Kyvik,K.O., Laakso,M., Lakka,T.A., Lind,L., Lindgren,C.M.,
            Martin,N.G., Marz,W., McCarthy,M.I., McKenzie,C.A., Meneton,P.,
            Metspalu,A., Moilanen,L., Morris,A.D., Munroe,P.B., Njolstad,I.,
            Pedersen,N.L., Power,C., Pramstaller,P.P., Price,J.F., Psaty,B.M.,
            Quertermous,T., Rauramaa,R., Saleheen,D., Salomaa,V.,
            Sanghera,D.K., Saramies,J., Schwarz,P.E.H., Sheu,W.H.,
            Shuldiner,A.R., Siegbahn,A., Spector,T.D., Stefansson,K.,
            Strachan,D.P., Tayo,B.O., Tremoli,E., Tuomilehto,J., Uusitupa,M.,
            van Duijn,C.M., Vollenweider,P., Wallentin,L., Wareham,N.J.,
            Whitfield,J.B., Wolffenbuttel,B.H.R., Ordovas,J.M., Boerwinkle,E.,
            Palmer,C.N.A., Thorsteinsdottir,U., Chasman,D.I., Rotter,J.I.,
            Franks,P.W., Ripatti,S., Cupples,L.A., Sandhu,M.S., Rich,S.S.,
            Boehnke,M., Deloukas,P., Kathiresan,S., Mohlke,K.L., Ingelsson,E.
            and Abecasis,G.R.
  CONSRTM   Global Lipids Genetics Consortium
  TITLE     Discovery and refinement of loci associated with lipid levels
  JOURNAL   Nat Genet 45 (11), 1274-1283 (2013)
   PUBMED   24097068
REFERENCE   7  (residues 1 to 60)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 60)
  AUTHORS   Yashin,A.I., Wu,D., Arbeev,K.G. and Ukraintseva,S.V.
  TITLE     Joint influence of small-effect genetic variants on human longevity
  JOURNAL   Aging (Albany NY) 2 (9), 612-620 (2010)
   PUBMED   20834067
REFERENCE   9  (residues 1 to 60)
  AUTHORS   Satoh,J., Obayashi,S., Misawa,T., Sumiyoshi,K., Oosumi,K. and
            Tabunoki,H.
  TITLE     Protein microarray analysis identifies human cellular prion protein
            interactors
  JOURNAL   Neuropathol Appl Neurobiol 35 (1), 16-35 (2009)
   PUBMED   18482256
REFERENCE   10 (residues 1 to 60)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CP068271.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14478891.2422849.1, SRR14584551.512650.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968968, SAMEA2151887 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..60
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..60
                     /product="protein cholesin isoform d"
                     /note="uncharacterized protein C7orf50; protein cholesin"
                     /calculated_mol_wt=6336
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     CDS             1..60
                     /gene="CHLSN"
                     /gene_synonym="C7orf50; YCR016W"
                     /coded_by="NM_001424337.1:42..224"
                     /note="isoform d is encoded by transcript variant 30"
                     /db_xref="GeneID:84310"
                     /db_xref="HGNC:HGNC:22421"
                     /db_xref="MIM:621174"
ORIGIN      
        1 makqkrkvpe vtekknkklk kasaegpllg peaapsgega gskpfgsqhs rfeedsrlms
//
LOCUS       NP_001394262             284 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 16 [Homo sapiens].
ACCESSION   NP_001394262
VERSION     NP_001394262.1
DBSOURCE    REFSEQ: accession NM_001407333.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2240406.1,
                                           SRR14372080.2447591.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..284
                     /product="tropomyosin alpha-1 chain isoform 16"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=32596
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09493.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:3548719; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04692; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Region          48..282
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Region          116..136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09493.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P58771; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P58771; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            213
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P58771; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P04692; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P58771; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by DAPK1.
                     /evidence=ECO:0000269|PubMed:17895359; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     CDS             1..284
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407333.1:84..938"
                     /note="isoform 16 is encoded by transcript variant 21"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle delvslqkkl kgtedeldky
       61 sealkdaqek lelaekkatd aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegkc aeleeelktv tnnlksleaq aekysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledel yaqklkykai seeldhalnd mtsm
//
LOCUS       NP_001427516             435 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform e [Homo sapiens].
ACCESSION   NP_001427516
VERSION     NP_001427516.1
DBSOURCE    REFSEQ: accession NM_001440587.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 435)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 435)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 435)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1668090.1,
                                           SRR14038196.2283510.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..435
                     /product="polycomb protein EED isoform e"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=49421
     Region          117..157
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          119..432
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(134,138,144..145,157..158,177,181,187..188,203..204,
                     221,226,232..233,274,289,299..300,317,319,325,333,
                     352..353,372,377,383..384,400..401,421,425,431..432)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          162..199
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          209..271
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          278..351
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          359..399
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          407..431
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..435
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001440587.1:478..1785"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdendd avsiesgtnt erpdtptntp
       61 napgrkswgk gkwkskkcky sfkcvnslkv tlyechsqge irllqsyvda dadenfytca
      121 wtydsntshp llavagsrgi iriinpitmq cikhyvghgn ainelkfhpr dpnlllsvsk
      181 dhalrlwniq tdtlvaifgg veghrdevls adydllgeki mscgmdhslk lwrinskrmm
      241 naikesydyn pnktnrpfis qkihfpdfst rdihrnyvdc vrwlgdlils ksgrailhsh
      301 qqcmrdpvsp nlrqhlscen aivcwkpgkm eddidkikps esnvtilgrf dysqcdiwym
      361 rfsmdfwqkm lalgnqvgkl yvwdlevedp hkakcttlth hkcgaairqt sfsrdssili
      421 avcddasiwr wdrlr
//
LOCUS       NP_001397643             586 aa            linear   PRI 21-NOV-2025
DEFINITION  O-phosphoseryl-tRNA(Sec) selenium transferase isoform 2 [Homo
            sapiens].
ACCESSION   NP_001397643 XP_016863766
VERSION     NP_001397643.1
DBSOURCE    REFSEQ: accession NM_001410714.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Vishweswaraiah,S., Yilmaz,A., Saiyed,N., Khalid,A., Koladiya,P.R.,
            Pan,X., Macias,S., Robinson,A.C., Mann,D., Green,B.D.,
            Kerseviciute,I., Gordevicius,J., Radhakrishna,U. and Graham,S.F.
  TITLE     Integrative Analysis Unveils the Correlation of Aminoacyl-tRNA
            Biosynthesis Metabolites with the Methylation of the SEPSECS Gene
            in Huntington's Disease Brain Tissue
  JOURNAL   Genes (Basel) 14 (9), 1752 (2023)
   PUBMED   37761892
  REMARK    GeneRIF: Integrative Analysis Unveils the Correlation of
            Aminoacyl-tRNA Biosynthesis Metabolites with the Methylation of the
            SEPSECS Gene in Huntington's Disease Brain Tissue.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Puppala,A.K., Castillo Suchkou,J., French,R.L., Kiernan,K.A. and
            Simonovic,M.
  TITLE     Structural basis for the tRNA-dependent activation of the terminal
            complex of selenocysteine synthesis in humans
  JOURNAL   Nucleic Acids Res 51 (8), 4012-4026 (2023)
   PUBMED   36929010
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Ramadesikan,S., Hickey,S., De Los Reyes,E., Patel,A.D.,
            Franklin,S.J., Brennan,P., Crist,E., Lee,K., White,P.,
            McBride,K.L., Koboldt,D.C. and Wilson,R.K.
  TITLE     Biallelic SEPSECS variants in two siblings with pontocerebellar
            hypoplasia type 2D underscore the relevance of splice-disrupting
            synonymous variants in disease
  JOURNAL   Cold Spring Harb Mol Case Stud 8 (2), a006165 (2022)
   PUBMED   35091508
  REMARK    GeneRIF: Biallelic SEPSECS variants in two siblings with
            pontocerebellar hypoplasia type 2D underscore the relevance of
            splice-disrupting synonymous variants in disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Schoenmakers,E. and Chatterjee,K.
  TITLE     Human Genetic Disorders Resulting in Systemic Selenoprotein
            Deficiency
  JOURNAL   Int J Mol Sci 22 (23), 12927 (2021)
   PUBMED   34884733
  REMARK    GeneRIF: Human Genetic Disorders Resulting in Systemic
            Selenoprotein Deficiency.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Xu,X.M., Mix,H., Carlson,B.A., Grabowski,P.J., Gladyshev,V.N.,
            Berry,M.J. and Hatfield,D.L.
  TITLE     Evidence for direct roles of two additional factors, SECp43 and
            soluble liver antigen, in the selenoprotein synthesis machinery
  JOURNAL   J Biol Chem 280 (50), 41568-41575 (2005)
   PUBMED   16230358
REFERENCE   7  (residues 1 to 586)
  AUTHORS   Herkel,J., Heidrich,B., Nieraad,N., Wies,I., Rother,M. and
            Lohse,A.W.
  TITLE     Fine specificity of autoantibodies to soluble liver antigen and
            liver/pancreas
  JOURNAL   Hepatology 35 (2), 403-408 (2002)
   PUBMED   11826415
REFERENCE   8  (residues 1 to 586)
  AUTHORS   Volkmann,M., Martin,L., Baurle,A., Heid,H., Strassburg,C.P.,
            Trautwein,C., Fiehn,W. and Manns,M.P.
  TITLE     Soluble liver antigen: isolation of a 35-kd recombinant protein
            (SLA-p35) specifically recognizing sera from patients with
            autoimmune hepatitis
  JOURNAL   Hepatology 33 (3), 591-596 (2001)
   PUBMED   11230739
REFERENCE   9  (residues 1 to 586)
  AUTHORS   Costa,M., Rodriguez-Sanchez,J.L., Czaja,A.J. and Gelpi,C.
  TITLE     Isolation and characterization of cDNA encoding the antigenic
            protein of the human tRNP(Ser)Sec complex recognized by
            autoantibodies from patients withtype-1 autoimmune hepatitis
  JOURNAL   Clin Exp Immunol 121 (2), 364-374 (2000)
   PUBMED   10931155
REFERENCE   10 (residues 1 to 586)
  AUTHORS   Wies,I., Brunner,S., Henninger,J., Herkel,J., Kanzler,S., Meyer zum
            Buschenfelde,K.H. and Lohse,A.W.
  TITLE     Identification of target antigen for SLA/LP autoantibodies in
            autoimmune hepatitis
  JOURNAL   Lancet 355 (9214), 1510-1515 (2000)
   PUBMED   10801173
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104662.3 and AC007073.2.
            
            On Aug 15, 2022 this sequence version replaced XP_016863766.1.
            
            Summary: The amino acid selenocysteine is the only amino acid that
            does not have its own tRNA synthetase. Instead, this amino acid is
            synthesized on its cognate tRNA in a three step process. The
            protein encoded by this gene catalyzes the third step in the
            process, the conversion of O-phosphoseryl-tRNA(Sec) to
            selenocysteinyl-tRNA(Sec).[provided by RefSeq, Mar 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2359152.1,
                                           SRR14038192.3585404.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.2"
     Protein         1..586
                     /product="O-phosphoseryl-tRNA(Sec) selenium transferase
                     isoform 2"
                     /EC_number="2.9.1.2"
                     /note="soluble liver antigen/liver pancreas antigen;
                     O-phosphoseryl-tRNA(Sec) selenium transferase; SLA/LP
                     autoantigen; liver-pancreas antigen; UGA suppressor
                     tRNA-associated protein; tRNA(Ser/Sec)-associated
                     antigenic protein"
                     /calculated_mol_wt=64734
     Region          12..543
                     /region_name="selenium_SpcS"
                     /note="O-phosphoseryl-tRNA(Sec) selenium transferase;
                     TIGR03531"
                     /db_xref="CDD:211833"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HD40.2)"
     Site            369
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
     CDS             1..586
                     /gene="SEPSECS"
                     /gene_synonym="LP; PCH2D; SecS; SLA; SLA-p35; SLA/LP"
                     /coded_by="NM_001410714.1:81..1841"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS93487.1"
                     /db_xref="GeneID:51091"
                     /db_xref="HGNC:HGNC:30605"
                     /db_xref="MIM:613009"
ORIGIN      
        1 mnresfaage rlvspayvrq gcearrsheh lirllleksl alsprlecsv tisahcslrl
       61 pgsrhspasa srvagttgar hhtrlmfvfl vemgfhhvgq adlklltssd rpflafqsar
      121 itggkcpeng wdestlelfl helaimdsnn flgncgvger egrvasalva rrhyrfihgi
      181 grsgdisavq pkaagsslln kitnslvldi iklagvhtva ncfvvpmatg msltlcfltl
      241 rhkrpkakyi iwpridqksc fksmitagfe pvvienvleg delrtdlkav eakvqelgpd
      301 cilcihstts cfaprvpdrl eelavicany diphivnnay gvqsskcmhl iqqgarvgri
      361 dafvqsldkn fmvpvggaii agfndsfiqe iskmypgras aspsldvlit llslgsngyk
      421 kllkerkemf sylsnqikkl seaynerllh tphnpislam tlktldehrd kavtqlgsml
      481 ftrqvsgarv vplgsmqtvs gytfrgfmsh tnnypcayln aasaigmkmq dvdlfikrld
      541 rclkavrker skesddnydk tedvdieema lkldnvlldt yqdass
//
LOCUS       NP_001427361             758 aa            linear   PRI 21-NOV-2025
DEFINITION  lipopolysaccharide-responsive and beige-like anchor protein isoform
            6 [Homo sapiens].
ACCESSION   NP_001427361 XP_016864362 XP_054207316
VERSION     NP_001427361.1
DBSOURCE    REFSEQ: accession NM_001440432.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 758)
  AUTHORS   Szentgyorgyi,V., Lueck,L.M., Overwijn,D., Ritz,D., Zoeller,N.,
            Schmidt,A., Hondele,M., Spang,A. and Bakhtiar,S.
  TITLE     Arf1-dependent LRBA recruitment to Rab4 endosomes is required for
            endolysosome homeostasis
  JOURNAL   J Cell Biol 223 (11) (2024)
   PUBMED   39325073
  REMARK    GeneRIF: Arf1-dependent LRBA recruitment to Rab4 endosomes is
            required for endolysosome homeostasis.
REFERENCE   3  (residues 1 to 758)
  AUTHORS   Freund,T., Baxter,S.K., Walsh,T., Golan,H., Kapelushnik,J.,
            Abramsohn-Goldenberg,M., Benor,S., Sarid,N., Ram,R., Alcalay,Y.,
            Segel,R., Renbaum,P., Stepensky,P., King,M.C., Torgerson,T.R. and
            Hagin,D.
  TITLE     Clinically Complex LRBA Deficiency Due to a Founder Allele in the
            Georgian Jewish Population
  JOURNAL   J Clin Immunol 43 (1), 151-164 (2023)
   PUBMED   36063261
  REMARK    GeneRIF: Clinically Complex LRBA Deficiency Due to a Founder Allele
            in the Georgian Jewish Population.
REFERENCE   4  (residues 1 to 758)
  AUTHORS   Catak,M.C., Akcam,B., Bilgic Eltan,S., Babayeva,R., Karakus,I.S.,
            Akgun,G., Baser,D., Bulutoglu,A., Bayram,F., Kasap,N., Kiykim,A.,
            Hancioglu,G., Kokcu Karadag,S.I., Kendir Demirkol,Y., Ozen,S.,
            Cekic,S., Ozcan,D., Edeer Karaca,N., Sasihuseyinoglu,A.S.,
            Cansever,M., Ozek Yucel,E., Tamay,Z., Altintas,D.U., Aydogmus,C.,
            Celmeli,F., Cokugras,H., Gulez,N., Genel,F., Metin,A., Guner,S.N.,
            Kutukculer,N., Keles,S., Reisli,I., Kilic,S.S., Yildiran,A.,
            Karakoc-Aydiner,E., Lo,B., Ozen,A. and Baris,S.
  TITLE     Comparing the levels of CTLA-4-dependent biological defects in
            patients with LRBA deficiency and CTLA-4 insufficiency
  JOURNAL   Allergy 77 (10), 3108-3123 (2022)
   PUBMED   35491430
  REMARK    GeneRIF: Comparing the levels of CTLA-4-dependent biological
            defects in patients with LRBA deficiency and CTLA-4 insufficiency.
REFERENCE   5  (residues 1 to 758)
  AUTHORS   Yao,J., Gu,H., Mou,W., Chen,Z., Ma,J., Ma,H., Li,N., Zhang,R.,
            Wang,T., Jiang,J. and Wu,R.
  TITLE     Various phenotypes of LRBA gene with compound heterozygous
            variation: A case series report of pediatric cytopenia patients
  JOURNAL   Int J Immunopathol Pharmacol 36, 3946320221125591 (2022)
   PUBMED   36074705
  REMARK    GeneRIF: Various phenotypes of LRBA gene with compound heterozygous
            variation: A case series report of pediatric cytopenia patients.
REFERENCE   6  (residues 1 to 758)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 758)
  AUTHORS   Gebauer,D., Li,J., Jogl,G., Shen,Y., Myszka,D.G. and Tong,L.
  TITLE     Crystal structure of the PH-BEACH domains of human LRBA/BGL
  JOURNAL   Biochemistry 43 (47), 14873-14880 (2004)
   PUBMED   15554694
  REMARK    GeneRIF: The crystal structure of the aPH-BEACH domains of LRBA
            were studied.
REFERENCE   8  (residues 1 to 758)
  AUTHORS   Dyomin,V.G., Chaganti,S.R., Dyomina,K., Palanisamy,N., Murty,V.V.,
            Dalla-Favera,R. and Chaganti,R.S.
  TITLE     BCL8 is a novel, evolutionarily conserved human gene family
            encoding proteins with presumptive protein kinase A anchoring
            function
  JOURNAL   Genomics 80 (2), 158-165 (2002)
   PUBMED   12160729
REFERENCE   9  (residues 1 to 758)
  AUTHORS   Wang,J.W., Howson,J., Haller,E. and Kerr,W.G.
  TITLE     Identification of a novel lipopolysaccharide-inducible gene with
            key features of both A kinase anchor proteins and chs1/beige
            proteins
  JOURNAL   J Immunol 166 (7), 4586-4595 (2001)
   PUBMED   11254716
REFERENCE   10 (residues 1 to 758)
  AUTHORS   Feuchter,A.E., Freeman,J.D. and Mager,D.L.
  TITLE     Strategy for detecting cellular transcripts promoted by human
            endogenous long terminal repeats: identification of a novel gene
            (CDC4L) with homology to yeast CDC4
  JOURNAL   Genomics 13 (4), 1237-1246 (1992)
   PUBMED   1505956
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC110813.4, AC097373.3,
            AC092612.3 and AC093748.3.
            
            On or before May 20, 2025 this sequence version replaced
            XP_016864362.1, XP_054207316.1.
            
            Summary: The protein encoded by this gene is a member of the
            WDL-BEACH-WD (WBW) gene family. Its expression is induced in B
            cells and macrophages by bacterial lipopolysaccharides (LPS). The
            encoded protein associates with protein kinase A and may be
            involved in leading intracellular vesicles to activated receptor
            complexes, which aids in the secretion and/or membrane deposition
            of immune effector molecules. Defects in this gene are associated
            with the disorder common variable immunodeficiency-8 with
            autoimmunity. Two transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Dec 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749633.1, SRR18074969.865893.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.3"
     Protein         1..758
                     /product="lipopolysaccharide-responsive and beige-like
                     anchor protein isoform 6"
                     /note="vesicle trafficking, beach and anchor containing;
                     lipopolysaccharide-responsive and beige-like anchor
                     protein; CDC4-like protein; LPS-responsive vesicle
                     trafficking, beach and anchor containing"
                     /calculated_mol_wt=85732
     Region          <13..71
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          102..379
                     /region_name="Beach"
                     /note="Beige/BEACH domain; smart01026"
                     /db_xref="CDD:214982"
     Region          479..743
                     /region_name="NBCH_WD40"
                     /note="Neurobeachin beta propeller domain; pfam20426"
                     /db_xref="CDD:466575"
     Region          495..531
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          537..590
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          595..630
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          635..664
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          677..711
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..758
                     /gene="LRBA"
                     /gene_synonym="BGL; CDC4L; CVID8; LAB300; LBA; uc.147"
                     /coded_by="NM_001440432.1:418..2694"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="GeneID:987"
                     /db_xref="HGNC:HGNC:1742"
                     /db_xref="MIM:606453"
ORIGIN      
        1 mctsegwsgy kilayteglh gkwlfteirs ifsrryllqn taleifmanr vavmfnfpdp
       61 atvkkvvnyl prvgvgtsfg lpqtrrisla sprqlfkasn mtqrwqhrei snfeylmfln
      121 tiagrsyndl nqypvfpwvi tnyeseeldl tlptnfrdls kpigalnpkr aaffaeryes
      181 weddqvpkfh ygthystasf vlawllriep fttyflnlqg gkfdhadrtf ssisrawrns
      241 qrdtsdikel ipefyylpem fvnfnnynlg vmddgtvvsd velppwakts eefvhinrla
      301 lesefvscql hqwidlifgy kqqgpeavra lnvfyyltye gavnlnsitd pvlreaveaq
      361 irsfgqtpsq lliephpprg samqvylllq splmftdkaq qdvimvlkfp snspvthvaa
      421 ntqpglatpa vitvtanrlf avnkwhnlpa hqgavqdqpy qlpveidpli asntgmhrrq
      481 itdlldqsiq vhsqcfvits dnryilvcgf wdksfrvyst dtgrliqvvf ghwdvvtcla
      541 rsesyiggnc yilsgsrdat lllwywngkc sgigdnpgse taaprailtg hdyevtcaav
      601 caelglvlsg sqegpclihs mngdllrtle gpenclkpkl iqasreghcv ifyenglfct
      661 fsvngklqat metddnirai qlsrdgqyll tggdrgvvvv rqvsdlkqlf aypgcdagir
      721 amalsydqrc iisgmasgsi vlfyndfnrw hheyqtry
//
LOCUS       NP_001397918             652 aa            linear   PRI 21-NOV-2025
DEFINITION  tectonic-2 isoform 3 [Homo sapiens].
ACCESSION   NP_001397918 XP_005253680
VERSION     NP_001397918.1
DBSOURCE    REFSEQ: accession NM_001410989.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 652)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 652)
  AUTHORS   Liu,Q., Zhu,C. and Dong,Y.
  TITLE     LncRNA TCTN2 Promotes the Malignant Development of Hepatocellular
            Carcinoma via Regulating mIR-1285-3p/ARF6 Axis
  JOURNAL   Recent Pat Anticancer Drug Discov 18 (4), 517-527 (2023)
   PUBMED   36278455
  REMARK    GeneRIF: LncRNA TCTN2 Promotes the Malignant Development of
            Hepatocellular Carcinoma via Regulating mIR-1285-3p/ARF6 Axis.
REFERENCE   3  (residues 1 to 652)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 652)
  AUTHORS   Litz Philipsborn,S., Hartmajer,S., Shtorch Asor,A., Vinovezky,M.,
            Regev,M., Singer,A. and Reinstein,E.
  TITLE     A founder mutation in TCTN2 causes Meckel-Gruber syndrome type 8
            among Jews of Ethiopian and Yemenite origin
  JOURNAL   Am J Med Genet A 185 (5), 1610-1613 (2021)
   PUBMED   33590725
  REMARK    GeneRIF: A founder mutation in TCTN2 causes Meckel-Gruber syndrome
            type 8 among Jews of Ethiopian and Yemenite origin.
REFERENCE   5  (residues 1 to 652)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 652)
  AUTHORS   Shaheen,R., Faqeih,E., Seidahmed,M.Z., Sunker,A., Alali,F.E.,
            AlQahtani,K. and Alkuraya,F.S.
  TITLE     A TCTN2 mutation defines a novel Meckel Gruber syndrome locus
  JOURNAL   Hum Mutat 32 (6), 573-578 (2011)
   PUBMED   21462283
  REMARK    GeneRIF: a truncating mutation in TCTN2 linked to Meckel Gruber
            syndrome was shown.
REFERENCE   7  (residues 1 to 652)
  AUTHORS   Sang,L., Miller,J.J., Corbit,K.C., Giles,R.H., Brauer,M.J.,
            Otto,E.A., Baye,L.M., Wen,X., Scales,S.J., Kwong,M.,
            Huntzicker,E.G., Sfakianos,M.K., Sandoval,W., Bazan,J.F.,
            Kulkarni,P., Garcia-Gonzalo,F.R., Seol,A.D., O'Toole,J.F., Held,S.,
            Reutter,H.M., Lane,W.S., Rafiq,M.A., Noor,A., Ansar,M., Devi,A.R.,
            Sheffield,V.C., Slusarski,D.C., Vincent,J.B., Doherty,D.A.,
            Hildebrandt,F., Reiter,J.F. and Jackson,P.K.
  TITLE     Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy
            disease genes and pathways
  JOURNAL   Cell 145 (4), 513-528 (2011)
   PUBMED   21565611
  REMARK    GeneRIF: Network building strategy led to the proposal of
            candidates for new ciliopathy disease genes, leading to the
            identification of the first human mutations in the Nephronophthisis
            gene Ataxin10 (ATXN10) and Joubert syndrome gene Tectonic2 (TCTN2).
REFERENCE   8  (residues 1 to 652)
  AUTHORS   Reiter,J.F. and Skarnes,W.C.
  TITLE     Tectonic, a novel regulator of the Hedgehog pathway required for
            both activation and inhibition
  JOURNAL   Genes Dev 20 (1), 22-27 (2006)
   PUBMED   16357211
REFERENCE   9  (residues 1 to 652)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 652)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC117503.8.
            
            On Aug 18, 2022 this sequence version replaced XP_005253680.1.
            
            Summary: This gene encodes a type I membrane protein that belongs
            to the tectonic family. Studies in mice suggest that this protein
            may be involved in hedgehog signaling, and essential for
            ciliogenesis. Mutations in this gene are associated with Meckel
            syndrome type 8. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2111893.1,
                                           SRR14038191.4260947.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..652
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..652
                     /product="tectonic-2 isoform 3"
                     /calculated_mol_wt=71478
     Region          171..399
                     /region_name="TCTN_DUF1619"
                     /note="Tectonic domain DUF1619; pfam07773"
                     /db_xref="CDD:462260"
     CDS             1..652
                     /gene="TCTN2"
                     /gene_synonym="C12orf38; JBTS24; MKS8; TECT2"
                     /coded_by="NM_001410989.1:129..2087"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS91766.1"
                     /db_xref="GeneID:79867"
                     /db_xref="HGNC:HGNC:25774"
                     /db_xref="MIM:613846"
ORIGIN      
        1 mgfqppaall lrlfllqgil rllwgdlafi ppfirmsgpa vsaslvgdte gvtvslavlq
       61 deagilpipt cgvlnneted wsvtvipgak vlevtvrwkr gldwcssnet dsfsespcil
      121 qtllvsashn sscsahlliq veiyansslt hnasenvtvi pnqvyqplgp cpcnltagac
      181 dvrcccdqec ssnlttlfrr scftgvfggd vnppfdqlcs agtttrgvpd wfpflcvqsp
      241 lantpflgyf yhgavspkqd ssfevyvdtd akdfadfgyk qgdpimtvkk ayftipqvsl
      301 agqcmqnapv aflhnfdvkc vtnlelyqer dgiinakikn valggivtpk viyeeatdld
      361 kfitntgimt qrfvvkflsy nsgneeelsg npgyqlgkpv ralninrmnn vttlhlwqsa
      421 grglctsatf kpilfgenvl sgcllevgin enctqlrena verldsliqa thvamrgnsd
      481 yadlsdgwle iirvdapdpg adplassvng mcldipahls irilisdaga vegitqqeil
      541 gvetrfssvn wqyqcgltce hkadllpisa svqfikipaq lphpltrfqi nyteydcnrn
      601 evcwpqllyp wtqyyqgelh sqcvakglll llfltlalfl snpwtricka ys
//
LOCUS       NP_001428006            1231 aa            linear   PRI 21-NOV-2025
DEFINITION  cohesin subunit SA-2 isoform b [Homo sapiens].
ACCESSION   NP_001428006
VERSION     NP_001428006.1
DBSOURCE    REFSEQ: accession NM_001441077.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1231)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1231)
  AUTHORS   Fischer,A., Hernandez-Rodriguez,B., Mulet-Lazaro,R., Nuetzel,M.,
            Holzl,F., van Herk,S., Kavelaars,F.G., Stanewsky,H., Ackermann,U.,
            Niang,A.H., Diaz,N., Reuschel,E., Strieder,N., Hernandez-Lopez,I.,
            Valk,P.J.M., Vaquerizas,J.M., Rehli,M., Delwel,R. and Gebhard,C.
  TITLE     STAG2 mutations reshape the cohesin-structured spatial chromatin
            architecture to drive gene regulation in acute myeloid leukemia
  JOURNAL   Cell Rep 43 (8), 114498 (2024)
   PUBMED   39084219
  REMARK    GeneRIF: STAG2 mutations reshape the cohesin-structured spatial
            chromatin architecture to drive gene regulation in acute myeloid
            leukemia.
REFERENCE   3  (residues 1 to 1231)
  AUTHORS   Huber,J., Tanasie,N.L., Zernia,S. and Stigler,J.
  TITLE     Single-molecule imaging reveals a direct role of CTCF's zinc
            fingers in SA interaction and cluster-dependent RNA recruitment
  JOURNAL   Nucleic Acids Res 52 (11), 6490-6506 (2024)
   PUBMED   38742641
  REMARK    GeneRIF: Single-molecule imaging reveals a direct role of CTCF's
            zinc fingers in SA interaction and cluster-dependent RNA
            recruitment.
REFERENCE   4  (residues 1 to 1231)
  AUTHORS   Xu,W., Kim,J.S., Yang,T., Ya,A., Sadzewicz,L., Tallon,L.,
            Harris,B.T., Sarkaria,J., Jin,F. and Waldman,T.
  TITLE     STAG2 mutations regulate 3D genome organization, chromatin loops,
            and Polycomb signaling in glioblastoma multiforme
  JOURNAL   J Biol Chem 300 (6), 107341 (2024)
   PUBMED   38705393
  REMARK    GeneRIF: STAG2 mutations regulate 3D genome organization, chromatin
            loops, and Polycomb signaling in glioblastoma multiforme.
REFERENCE   5  (residues 1 to 1231)
  AUTHORS   Ros-Pardo,D., Gomez-Puertas,P. and Marcos-Alcalde,I.
  TITLE     STAG2: Computational Analysis of Missense Variants Involved in
            Disease
  JOURNAL   Int J Mol Sci 25 (2), 1280 (2024)
   PUBMED   38279279
  REMARK    GeneRIF: STAG2: Computational Analysis of Missense Variants
            Involved in Disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1231)
  AUTHORS   Gregson,H.C., Schmiesing,J.A., Kim,J.S., Kobayashi,T., Zhou,S. and
            Yokomori,K.
  TITLE     A potential role for human cohesin in mitotic spindle aster
            assembly
  JOURNAL   J Biol Chem 276 (50), 47575-47582 (2001)
   PUBMED   11590136
REFERENCE   7  (residues 1 to 1231)
  AUTHORS   Sumara,I., Vorlaufer,E., Gieffers,C., Peters,B.H. and Peters,J.M.
  TITLE     Characterization of vertebrate cohesin complexes and their
            regulation in prophase
  JOURNAL   J Cell Biol 151 (4), 749-762 (2000)
   PUBMED   11076961
REFERENCE   8  (residues 1 to 1231)
  AUTHORS   Carramolino,L., Lee,B.C., Zaballos,A., Peled,A., Barthelemy,I.,
            Shav-Tal,Y., Prieto,I., Carmi,P., Gothelf,Y., Gonzalez de
            Buitrago,G., Aracil,M., Marquez,G., Barbero,J.L. and Zipori,D.
  TITLE     SA-1, a nuclear protein encoded by one member of a novel gene
            family: molecular cloning and detection in hemopoietic organs
  JOURNAL   Gene 195 (2), 151-159 (1997)
   PUBMED   9305759
  REMARK    Erratum:[Gene 1998 Jan 12;206(2):283]
REFERENCE   9  (residues 1 to 1231)
  AUTHORS   Wu,C., Friedlander,P., Lamoureux,C., Zannis-Hadjopoulos,M. and
            Price,G.B.
  TITLE     cDNA clones contain autonomous replication activity
  JOURNAL   Biochim Biophys Acta 1174 (3), 241-257 (1993)
   PUBMED   7690594
REFERENCE   10 (residues 1 to 1231)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121601.13 and AL355476.12.
            
            Summary: The protein encoded by this gene is a subunit of the
            cohesin complex, which regulates the separation of sister
            chromatids during cell division. Targeted inactivation of this gene
            results in chromatid cohesion defects and aneuploidy, suggesting
            that genetic disruption of cohesin is a cause of aneuploidy in
            human cancer. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2685917.1,
                                           SRR14038194.3063383.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1231
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..1231
                     /product="cohesin subunit SA-2 isoform b"
                     /note="SCC3 homolog 2; cohesin subunit SA-2; SA2
                     stromalin; sister chromatid cohesion 3 homolog B; stromal
                     antigen 2"
                     /calculated_mol_wt=141196
     Region          1..75
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Region          102..>395
                     /region_name="IRR1"
                     /note="Cohesin [Cell division and chromosome
                     partitioning]; COG5537"
                     /db_xref="CDD:227824"
     Region          157..270
                     /region_name="STAG"
                     /note="STAG domain; pfam08514"
                     /db_xref="CDD:462502"
     Site            607
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1058
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1061
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Region          1064..1083
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1064
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35638; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1065
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35638; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1112
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     CDS             1..1231
                     /gene="STAG2"
                     /gene_synonym="bA517O1.1; HPE13; MKMS; NEDXCF; SA-2; SA2;
                     SCC3B"
                     /coded_by="NM_001441077.1:573..4268"
                     /note="isoform b is encoded by transcript variant 25"
                     /db_xref="GeneID:10735"
                     /db_xref="HGNC:HGNC:11355"
                     /db_xref="MIM:300826"
ORIGIN      
        1 miaapeiptd fnllqeseth fssdtdfedi egknqkqgkg ktckkgkkgp aekgkggngg
       61 gkppsgpnrm nghhqqngve nmmlfevvkm gksamqsvvd dwiesykhdr dialldlinf
      121 fiqcsgckgv vtaemfrhmq nseiirkmte efdedsgdyp ltmagpqwkk fkssfcefig
      181 vlvrqcqysi iydeymmdtv islltglsds qvrafrhtst laamklmtal vnvalnlsin
      241 mdntqrqyea ernkmigkra nerlelllqk rkelqenqde ienmmnaifk gvfvhryrda
      301 iaeiraicie eigiwmkmys daflndsylk yvgwtmhdkq gevrlkclta lqglyynkel
      361 nsklelftsr fkdrivsmtl dkeydvavqa iklltlvlqs seevltaedc envyhlvysa
      421 hrpvavaage flykklfsrr dpeedgmmkr rgrqgpnanl vktlvfffle selhehaayl
      481 vdsmwdcate llkdwecmns llleeplsge ealtdrqesa lieimlctir qaaechppvg
      541 rgtgkrvlta kekktqlddr tkitelfava lpqllakysv daekvtnllq lpqyfdleiy
      601 ttgrlekhld allrqirniv ekhtdtdvle acsktyhalc neeftifnrv disrsqlide
      661 ladkfnrlle dflqegeepd eddayqvlst lkritafhna hdlskwdlfa cnykllktgi
      721 engdmpeqiv ihalqcthyv ilwqlakite ssstkedllr lkkqmrvfcq icqhyltnvn
      781 ttvkeqafti lcdilmifsh qimsggrdml eplvytpdss lqsellsfil dhvfieqddd
      841 nnsadgqqed easkiealhk rrnllaafck livytvvemn taadifkqym kyyndygdii
      901 ketmsktrqi dkiqcaktli lslqqlfnem iqengynfdr ssstfsgike larrfaltfg
      961 ldqlktreai amlhkdgief afkepnpqge shpplnlafl dilsefsskl lrqdkrtvyv
     1021 ylekfmtfqm slrredvwlp lmsyrnslla ggdddtmsvi sgissrgstv rskkskpstg
     1081 krkvvegmql slteessssd smwlsreqtl htpvmmqtpq ltstimrepk rlrpedsfms
     1141 vypmqtehhq tpldynrrgt slmeddeepi vedvmmsseg riedlnegmd fdtmdidlpp
     1201 sknrrertel kpdffdpasi mdesvlgvsm f
//
LOCUS       NP_001394191             393 aa            linear   PRI 21-NOV-2025
DEFINITION  cellular tumor antigen p53 isoform a [Homo sapiens].
ACCESSION   NP_001394191
VERSION     NP_001394191.1
DBSOURCE    REFSEQ: accession NM_001407262.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Mirgayazova,R., Khadiullina,R., Chasov,V., Mingaleeva,R.,
            Miftakhova,R., Rizvanov,A. and Bulatov,E.
  TITLE     Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an Option?
  JOURNAL   Genes (Basel) 11 (6), 704 (2020)
   PUBMED   32630614
  REMARK    GeneRIF: Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an
            Option?
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Flynt,E., Bisht,K., Sridharan,V., Ortiz,M., Towfic,F. and
            Thakurta,A.
  TITLE     Prognosis, Biology, and Targeting of TP53 Dysregulation in Multiple
            Myeloma
  JOURNAL   Cells 9 (2), 287 (2020)
   PUBMED   31991614
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Barnoud,T., Parris,J.L.D. and Murphy,M.E.
  TITLE     Common genetic variants in the TP53 pathway and their impact on
            cancer
  JOURNAL   J Mol Cell Biol 11 (7), 578-585 (2019)
   PUBMED   31152665
  REMARK    GeneRIF: Common genetic variants in the TP53 pathway and their
            impact on cancer.
            Review article
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Hu,W., Chen,S., Thorne,R.F. and Wu,M.
  TITLE     TP53, TP53 Target Genes (DRAM, TIGAR), and Autophagy
  JOURNAL   Adv Exp Med Biol 1206, 127-149 (2019)
   PUBMED   31776983
  REMARK    Review article
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Baugh,E.H., Ke,H., Levine,A.J., Bonneau,R.A. and Chan,C.S.
  TITLE     Why are there hotspot mutations in the TP53 gene in human cancers?
  JOURNAL   Cell Death Differ 25 (1), 154-160 (2018)
   PUBMED   29099487
  REMARK    GeneRIF: TP53 missense mutant alleles that occur in human cancers
            are discussed in the context of high resolution models of these p53
            mutant protein structures to determine the structural features of
            mutations (review).
            Review article
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Aubrey,B.J., Strasser,A. and Kelly,G.L.
  TITLE     Tumor-Suppressor Functions of the TP53 Pathway
  JOURNAL   Cold Spring Harb Perspect Med 6 (5), a026062 (2016)
   PUBMED   27141080
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Soussi,T. and Wiman,K.G.
  TITLE     TP53: an oncogene in disguise
  JOURNAL   Cell Death Differ 22 (8), 1239-1249 (2015)
   PUBMED   26024390
  REMARK    Review article
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Soussi,T.
  TITLE     The TP53 gene network in a postgenomic era
  JOURNAL   Hum Mutat 35 (6), 641-642 (2014)
   PUBMED   24753184
  REMARK    GeneRIF: Recommendations and guidelines for reporting and
            annotating TP53 variants are also provided, to help researchers
            generate standardized data that are easy to understand, analyze,
            and exchange across various cancer variant databases
            Review article
REFERENCE   9  (residues 1 to 393)
  AUTHORS   Anczukow,O., Ware,M.D., Buisson,M., Zetoune,A.B.,
            Stoppa-Lyonnet,D., Sinilnikova,O.M. and Mazoyer,S.
  TITLE     Does the nonsense-mediated mRNA decay mechanism prevent the
            synthesis of truncated BRCA1, CHK2, and p53 proteins?
  JOURNAL   Hum Mutat 29 (1), 65-73 (2008)
   PUBMED   17694537
  REMARK    GeneRIF: the p53 protein encoded by the 770delT allele is as
            abundant as the wild-type protein, as removal of the C-terminal p53
            domain leads to a stabilized mutant protein, whose abundance is
            markedly increased when NMD is inhibited.
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Bourdon,J.C.
  TITLE     p53 Family isoforms
  JOURNAL   Curr Pharm Biotechnol 8 (6), 332-336 (2007)
   PUBMED   18289041
  REMARK    Review article
REFERENCE   11 (residues 1 to 393)
  AUTHORS   Candeias,M.M., Powell,D.J., Roubalova,E., Apcher,S., Bourougaa,K.,
            Vojtesek,B., Bruzzoni-Giovanelli,H. and Fahraeus,R.
  TITLE     Expression of p53 and p53/47 are controlled by alternative
            mechanisms of messenger RNA translation initiation
  JOURNAL   Oncogene 25 (52), 6936-6947 (2006)
   PUBMED   16983332
  REMARK    GeneRIF: harbouring alternative translation initiation sites, the
            p53 mRNA gives rise to different levels of the p53 isoforms which
            help to orchestrate the cell biological outcome of p53 activation
REFERENCE   12 (residues 1 to 393)
  AUTHORS   Murray-Zmijewski,F., Lane,D.P. and Bourdon,J.C.
  TITLE     p53/p63/p73 isoforms: an orchestra of isoforms to harmonise cell
            differentiation and response to stress
  JOURNAL   Cell Death Differ 13 (6), 962-972 (2006)
   PUBMED   16601753
  REMARK    Review article
REFERENCE   13 (residues 1 to 393)
  AUTHORS   Bourdon,J.C., Fernandes,K., Murray-Zmijewski,F., Liu,G., Diot,A.,
            Xirodimas,D.P., Saville,M.K. and Lane,D.P.
  TITLE     p53 isoforms can regulate p53 transcriptional activity
  JOURNAL   Genes Dev 19 (18), 2122-2137 (2005)
   PUBMED   16131611
  REMARK    GeneRIF: p53 isoforms can regulate p53 transcriptional activity.
REFERENCE   14 (residues 1 to 393)
  AUTHORS   Ghosh,A., Stewart,D. and Matlashewski,G.
  TITLE     Regulation of human p53 activity and cell localization by
            alternative splicing
  JOURNAL   Mol Cell Biol 24 (18), 7987-7997 (2004)
   PUBMED   15340061
  REMARK    GeneRIF: mechanism of p53 regulation originating through
            alternative splicing of the human p53 gene resulting in the
            expression of a novel p53 mRNA
REFERENCE   15 (residues 1 to 393)
  AUTHORS   Flaman,J.M., Waridel,F., Estreicher,A., Vannier,A., Limacher,J.M.,
            Gilbert,D., Iggo,R. and Frebourg,T.
  TITLE     The human tumour suppressor gene p53 is alternatively spliced in
            normal cells
  JOURNAL   Oncogene 12 (4), 813-818 (1996)
   PUBMED   8632903
REFERENCE   16 (residues 1 to 393)
  AUTHORS   Schneider,K., Zelley,K., Nichols,K.E., Schwartz Levine,A. and
            Garber,J.
  TITLE     Li-Fraumeni Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301488
REFERENCE   17 (residues 1 to 393)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   18 (residues 1 to 393)
  AUTHORS   Lamb,P. and Crawford,L.
  TITLE     Characterization of the human p53 gene
  JOURNAL   Mol Cell Biol 6 (5), 1379-1385 (1986)
   PUBMED   2946935
REFERENCE   19 (residues 1 to 393)
  AUTHORS   Isobe,M., Emanuel,B.S., Givol,D., Oren,M. and Croce,C.M.
  TITLE     Localization of gene for human p53 tumour antigen to band 17p13
  JOURNAL   Nature 320 (6057), 84-85 (1986)
   PUBMED   3456488
REFERENCE   20 (residues 1 to 393)
  AUTHORS   Benchimol,S., Lamb,P., Crawford,L.V., Sheer,D., Shows,T.B.,
            Bruns,G.A. and Peacock,J.
  TITLE     Transformation associated p53 protein is encoded by a gene on human
            chromosome 17
  JOURNAL   Somat Cell Mol Genet 11 (5), 505-510 (1985)
   PUBMED   2994241
REFERENCE   21 (residues 1 to 393)
  AUTHORS   Harlow,E., Williamson,N.M., Ralston,R., Helfman,D.M. and Adams,T.E.
  TITLE     Molecular cloning and in vitro expression of a cDNA clone for human
            cellular tumor antigen p53
  JOURNAL   Mol Cell Biol 5 (7), 1601-1610 (1985)
   PUBMED   3894933
REFERENCE   22 (residues 1 to 393)
  AUTHORS   Zakut-Houri,R., Bienz-Tadmor,B., Givol,D. and Oren,M.
  TITLE     Human p53 cellular tumor antigen: cDNA sequence and expression in
            COS cells
  JOURNAL   EMBO J 4 (5), 1251-1255 (1985)
   PUBMED   4006916
REFERENCE   23 (residues 1 to 393)
  AUTHORS   Matlashewski,G., Lamb,P., Pim,D., Peacock,J., Crawford,L. and
            Benchimol,S.
  TITLE     Isolation and characterization of a human p53 cDNA clone:
            expression of the human p53 gene
  JOURNAL   EMBO J 3 (13), 3257-3262 (1984)
   PUBMED   6396087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087388.9 and AC007421.13.
            
            Summary: This gene encodes a tumor suppressor protein containing
            transcriptional activation, DNA binding, and oligomerization
            domains. The encoded protein responds to diverse cellular stresses
            to regulate expression of target genes, thereby inducing cell cycle
            arrest, apoptosis, senescence, DNA repair, or changes in
            metabolism. Mutations in this gene are associated with a variety of
            human cancers, including hereditary cancers such as Li-Fraumeni
            syndrome. Alternative splicing of this gene and the use of
            alternate promoters result in multiple transcript variants and
            isoforms. Additional isoforms have also been shown to result from
            the use of alternate translation initiation codons from identical
            transcript variants (PMIDs: 12032546, 20937277). [provided by
            RefSeq, Dec 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.663221.1,
                                           SRR14038195.421116.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..393
                     /product="cellular tumor antigen p53 isoform a"
                     /note="tumor protein 53; mutant tumor protein 53; cellular
                     tumor antigen p53; phosphoprotein p53;
                     transformation-related protein 53; antigen NY-CO-13; tumor
                     supressor p53"
                     /calculated_mol_wt=43522
     Region          1..320
                     /region_name="Interaction with CCAR2.
                     /evidence=ECO:0000269|PubMed:25732823"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          1..83
                     /region_name="Interaction with HRMT1L2.
                     /evidence=ECO:0000269|PubMed:15186775"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          1..44
                     /region_name="Transcription activation (acidic)"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          6..30
                     /region_name="P53_TAD"
                     /note="P53 transactivation motif; pfam08563"
                     /db_xref="CDD:462520"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by HIPK4.
                     /evidence=ECO:0000269|PubMed:18022393; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5, PRPK, AMPK, NUAK1 and ATM.
                     /evidence=ECO:0000269|PubMed:10570149,
                     ECO:0000269|PubMed:11554766, ECO:0000269|PubMed:15866171,
                     ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:17591690,
                     ECO:0000269|PubMed:17967874, ECO:0000269|PubMed:21317932,
                     ECO:0000269|PubMed:28842590; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          17..25
                     /region_name="TADI"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK1, VRK1 and VRK2.
                     /evidence=ECO:0000269|PubMed:10606744,
                     ECO:0000269|PubMed:10951572, ECO:0000269|PubMed:16704422,
                     ECO:0000269|PubMed:31527692; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CHEK2, CK1 and PLK3.
                     /evidence=ECO:0000269|PubMed:10570149,
                     ECO:0000269|PubMed:11447225, ECO:0000269|PubMed:11551930,
                     ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:20041275;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5 and CDK7.
                     /evidence=ECO:0000269|PubMed:17591690,
                     ECO:0000269|PubMed:9372954; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          35..59
                     /region_name="TAD2"
                     /note="Transactivation domain 2; pfam18521"
                     /db_xref="CDD:375947"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK5.
                     /evidence=ECO:0000269|PubMed:17254968; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5, DYRK2, HIPK2 and PKC/PRKCG.
                     /evidence=ECO:0000269|PubMed:11740489,
                     ECO:0000269|PubMed:11780126, ECO:0000269|PubMed:16377624,
                     ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:17591690;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          48..56
                     /region_name="TADII"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          50..96
                     /region_name="Disordered.
                     /evidence=ECO:0000269|PubMed:31953488"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by TAF1 and GRK5.
                     /evidence=ECO:0000269|PubMed:15053879,
                     ECO:0000269|PubMed:20124405; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          66..110
                     /region_name="Interaction with WWOX"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          100..370
                     /region_name="Interaction with HIPK1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          100..300
                     /region_name="Required for interaction with ZNF385A.
                     /evidence=ECO:0000269|PubMed:17719541"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          109..288
                     /region_name="P53"
                     /note="P53 DNA-binding domain; cd08367"
                     /db_xref="CDD:176262"
     Region          113..236
                     /region_name="Required for interaction with FBXO42.
                     /evidence=ECO:0000269|PubMed:19509332"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          116..292
                     /region_name="Interaction with AXIN1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            120
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000269|PubMed:16793544,
                     ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            120
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:17189187,
                     ECO:0000269|PubMed:19854137, ECO:0000269|PubMed:23431171;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            order(176,179,238,242)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:176262"
     Site            order(177..179,181)
                     /site_type="other"
                     /note="dimerization site [polypeptide binding]"
                     /db_xref="CDD:176262"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB.
                     /evidence=ECO:0000269|PubMed:20959462; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            order(239,241,248,273,275..277,280)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176262"
     Region          241..248
                     /region_name="Interaction with the 53BP2 SH3 domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          256..294
                     /region_name="Interaction with E4F1.
                     /evidence=ECO:0000269|PubMed:10644996"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB.
                     /evidence=ECO:0000269|PubMed:20959462; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          273..280
                     /region_name="Interaction with DNA"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          282..325
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AURKB.
                     /evidence=ECO:0000269|PubMed:20959462; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          300..393
                     /region_name="Interaction with CARM1.
                     /evidence=ECO:0000269|PubMed:15186775"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          305..321
                     /region_name="Bipartite nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            305
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:12724314; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKA, CDK1 and CDK2.
                     /evidence=ECO:0000269|PubMed:10884347,
                     ECO:0000269|PubMed:14702041; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          319..360
                     /region_name="Interaction with HIPK2"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          319..358
                     /region_name="P53_tetramer"
                     /note="P53 tetramerization motif; pfam07710"
                     /db_xref="CDD:462238"
     Site            321
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P02340; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          325..356
                     /region_name="Oligomerization"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            333
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, by PRMT5.
                     /evidence=ECO:0000269|PubMed:19011621; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            335
                     /site_type="methylation"
                     /note="Symmetric dimethylarginine, by PRMT5.
                     /evidence=ECO:0000269|PubMed:19011621; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            337
                     /site_type="methylation"
                     /note="Symmetric dimethylarginine, by PRMT5.
                     /evidence=ECO:0000269|PubMed:19011621; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          339..350
                     /region_name="Nuclear export signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          351..393
                     /region_name="Disordered.
                     /evidence=ECO:0000269|PubMed:31953488,
                     ECO:0000269|PubMed:36108750"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          359..363
                     /region_name="Interaction with USP7"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          368..387
                     /region_name="Basic (repression of DNA-binding)"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          370..372
                     /region_name="[KR]-[STA]-K motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            370
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:17108971,
                     ECO:0000269|PubMed:22864287; N6-methyllysine, by SMYD2,
                     alternate. /evidence=ECO:0000269|PubMed:17108971,
                     ECO:0000269|PubMed:22864287; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            372
                     /site_type="methylation"
                     /note="N6-methyllysine, by SETD7.
                     /evidence=ECO:0000269|PubMed:15525938,
                     ECO:0000269|PubMed:16415881; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            373
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, by EHMT1 and EHMT2,
                     alternate. /evidence=ECO:0000269|PubMed:20118233;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            373
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:10656795; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          374..393
                     /region_name="Interaction with MORN3.
                     /evidence=ECO:0000269|PubMed:29681526"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            381
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:29474172,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            382
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:17707234,
                     ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22864287;
                     N6-methyllysine, by KMT5A, alternate.
                     /evidence=ECO:0000269|PubMed:17707234,
                     ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22864287;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            382
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:10656795,
                     ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:20228809,
                     ECO:0000269|PubMed:23431171, ECO:0000269|PubMed:29681526,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2, CDK2 and NUAK1.
                     /evidence=ECO:0000269|PubMed:10884347,
                     ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:17108107,
                     ECO:0000269|PubMed:21317932, ECO:0000269|PubMed:22214662,
                     ECO:0000269|PubMed:35618207; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     CDS             1..393
                     /gene="TP53"
                     /gene_synonym="BCC7; BMFS5; LFS1; P53; TRP53"
                     /coded_by="NM_001407262.1:246..1427"
                     /note="isoform a is encoded by transcript variant 9"
                     /db_xref="GeneID:7157"
                     /db_xref="HGNC:HGNC:11998"
                     /db_xref="MIM:191170"
ORIGIN      
        1 meepqsdpsv epplsqetfs dlwkllpenn vlsplpsqam ddlmlspddi eqwftedpgp
       61 deaprmpeaa ppvapapaap tpaapapaps wplsssvpsq ktyqgsygfr lgflhsgtak
      121 svtctyspal nkmfcqlakt cpvqlwvdst pppgtrvram aiykqsqhmt evvrrcphhe
      181 rcsdsdglap pqhlirvegn lrveylddrn tfrhsvvvpy eppevgsdct tihynymcns
      241 scmggmnrrp iltiitleds sgnllgrnsf evrvcacpgr drrteeenlr kkgephhelp
      301 pgstkralpn ntssspqpkk kpldgeyftl qirgrerfem frelnealel kdaqagkepg
      361 gsrahsshlk skkgqstsrh kklmfktegp dsd
//
LOCUS       NP_001428010            1268 aa            linear   PRI 21-NOV-2025
DEFINITION  cohesin subunit SA-2 isoform a [Homo sapiens].
ACCESSION   NP_001428010 XP_047297733 XP_054182357
VERSION     NP_001428010.1
DBSOURCE    REFSEQ: accession NM_001441081.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1268)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1268)
  AUTHORS   Fischer,A., Hernandez-Rodriguez,B., Mulet-Lazaro,R., Nuetzel,M.,
            Holzl,F., van Herk,S., Kavelaars,F.G., Stanewsky,H., Ackermann,U.,
            Niang,A.H., Diaz,N., Reuschel,E., Strieder,N., Hernandez-Lopez,I.,
            Valk,P.J.M., Vaquerizas,J.M., Rehli,M., Delwel,R. and Gebhard,C.
  TITLE     STAG2 mutations reshape the cohesin-structured spatial chromatin
            architecture to drive gene regulation in acute myeloid leukemia
  JOURNAL   Cell Rep 43 (8), 114498 (2024)
   PUBMED   39084219
  REMARK    GeneRIF: STAG2 mutations reshape the cohesin-structured spatial
            chromatin architecture to drive gene regulation in acute myeloid
            leukemia.
REFERENCE   3  (residues 1 to 1268)
  AUTHORS   Huber,J., Tanasie,N.L., Zernia,S. and Stigler,J.
  TITLE     Single-molecule imaging reveals a direct role of CTCF's zinc
            fingers in SA interaction and cluster-dependent RNA recruitment
  JOURNAL   Nucleic Acids Res 52 (11), 6490-6506 (2024)
   PUBMED   38742641
  REMARK    GeneRIF: Single-molecule imaging reveals a direct role of CTCF's
            zinc fingers in SA interaction and cluster-dependent RNA
            recruitment.
REFERENCE   4  (residues 1 to 1268)
  AUTHORS   Xu,W., Kim,J.S., Yang,T., Ya,A., Sadzewicz,L., Tallon,L.,
            Harris,B.T., Sarkaria,J., Jin,F. and Waldman,T.
  TITLE     STAG2 mutations regulate 3D genome organization, chromatin loops,
            and Polycomb signaling in glioblastoma multiforme
  JOURNAL   J Biol Chem 300 (6), 107341 (2024)
   PUBMED   38705393
  REMARK    GeneRIF: STAG2 mutations regulate 3D genome organization, chromatin
            loops, and Polycomb signaling in glioblastoma multiforme.
REFERENCE   5  (residues 1 to 1268)
  AUTHORS   Ros-Pardo,D., Gomez-Puertas,P. and Marcos-Alcalde,I.
  TITLE     STAG2: Computational Analysis of Missense Variants Involved in
            Disease
  JOURNAL   Int J Mol Sci 25 (2), 1280 (2024)
   PUBMED   38279279
  REMARK    GeneRIF: STAG2: Computational Analysis of Missense Variants
            Involved in Disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1268)
  AUTHORS   Gregson,H.C., Schmiesing,J.A., Kim,J.S., Kobayashi,T., Zhou,S. and
            Yokomori,K.
  TITLE     A potential role for human cohesin in mitotic spindle aster
            assembly
  JOURNAL   J Biol Chem 276 (50), 47575-47582 (2001)
   PUBMED   11590136
REFERENCE   7  (residues 1 to 1268)
  AUTHORS   Sumara,I., Vorlaufer,E., Gieffers,C., Peters,B.H. and Peters,J.M.
  TITLE     Characterization of vertebrate cohesin complexes and their
            regulation in prophase
  JOURNAL   J Cell Biol 151 (4), 749-762 (2000)
   PUBMED   11076961
REFERENCE   8  (residues 1 to 1268)
  AUTHORS   Carramolino,L., Lee,B.C., Zaballos,A., Peled,A., Barthelemy,I.,
            Shav-Tal,Y., Prieto,I., Carmi,P., Gothelf,Y., Gonzalez de
            Buitrago,G., Aracil,M., Marquez,G., Barbero,J.L. and Zipori,D.
  TITLE     SA-1, a nuclear protein encoded by one member of a novel gene
            family: molecular cloning and detection in hemopoietic organs
  JOURNAL   Gene 195 (2), 151-159 (1997)
   PUBMED   9305759
  REMARK    Erratum:[Gene 1998 Jan 12;206(2):283]
REFERENCE   9  (residues 1 to 1268)
  AUTHORS   Wu,C., Friedlander,P., Lamoureux,C., Zannis-Hadjopoulos,M. and
            Price,G.B.
  TITLE     cDNA clones contain autonomous replication activity
  JOURNAL   Biochim Biophys Acta 1174 (3), 241-257 (1993)
   PUBMED   7690594
REFERENCE   10 (residues 1 to 1268)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121601.13 and AL355476.12.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297733.1, XP_054182357.1.
            
            Summary: The protein encoded by this gene is a subunit of the
            cohesin complex, which regulates the separation of sister
            chromatids during cell division. Targeted inactivation of this gene
            results in chromatid cohesion defects and aneuploidy, suggesting
            that genetic disruption of cohesin is a cause of aneuploidy in
            human cancer. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038194.4014605.1,
                                    SRR14038191.1086796.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2142680, SAMEA2142853 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1268
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..1268
                     /product="cohesin subunit SA-2 isoform a"
                     /note="SCC3 homolog 2; cohesin subunit SA-2; SA2
                     stromalin; sister chromatid cohesion 3 homolog B; stromal
                     antigen 2"
                     /calculated_mol_wt=145621
     Region          102..>395
                     /region_name="IRR1"
                     /note="Cohesin [Cell division and chromosome
                     partitioning]; COG5537"
                     /db_xref="CDD:227824"
     Region          157..270
                     /region_name="STAG"
                     /note="STAG domain; pfam08514"
                     /db_xref="CDD:462502"
     CDS             1..1268
                     /gene="STAG2"
                     /gene_synonym="bA517O1.1; HPE13; MKMS; NEDXCF; SA-2; SA2;
                     SCC3B"
                     /coded_by="NM_001441081.1:668..4474"
                     /note="isoform a is encoded by transcript variant 21"
                     /db_xref="GeneID:10735"
                     /db_xref="HGNC:HGNC:11355"
                     /db_xref="MIM:300826"
ORIGIN      
        1 miaapeiptd fnllqeseth fssdtdfedi egknqkqgkg ktckkgkkgp aekgkggngg
       61 gkppsgpnrm nghhqqngve nmmlfevvkm gksamqsvvd dwiesykhdr dialldlinf
      121 fiqcsgckgv vtaemfrhmq nseiirkmte efdedsgdyp ltmagpqwkk fkssfcefig
      181 vlvrqcqysi iydeymmdtv islltglsds qvrafrhtst laamklmtal vnvalnlsin
      241 mdntqrqyea ernkmigkra nerlelllqk rkelqenqde ienmmnaifk gvfvhryrda
      301 iaeiraicie eigiwmkmys daflndsylk yvgwtmhdkq gevrlkclta lqglyynkel
      361 nsklelftsr fkdrivsmtl dkeydvavqa iklltlvlqs seevltaedc envyhlvysa
      421 hrpvavaage flykklfsrr dpeedgmmkr rgrqgpnanl vktlvfffle selhehaayl
      481 vdsmwdcate llkdwecmns llleeplsge ealtdrqesa lieimlctir qaaechppvg
      541 rgtgkrvlta kekktqlddr tkitelfava lpqllakysv daekvtnllq lpqyfdleiy
      601 ttgrlekhld allrqirniv ekhtdtdvle acsktyhalc neeftifnrv disrsqlide
      661 ladkfnrlle dflqegeepd eddayqvlst lkritafhna hdlskwdlfa cnykllktgi
      721 engdmpeqiv ihalqcthyv ilwqlakite ssstkedllr lkkqmrvfcq icqhyltnvn
      781 ttvkeqafti lcdilmifsh qimsggrdml eplvytpdss lqsellsfil dhvfieqddd
      841 nnsadgqqed easkiealhk rrnllaafck livytvvemn taadifkqym kyyndygdii
      901 ketmsktrqi dkiqcaktli lslqqlfnem iqengynfdr ssstfsgike larrfaltfg
      961 ldqlktreai amlhkdgief afkepnpqge shpplnlafl dilsefsskl lrqdkrtvyv
     1021 ylekfmtfqm slrredvwlp lmsyrnslla ggdddtmsvi sgissrgstv rskkskpstg
     1081 krkvvegmql slteessssd smwlsreqtl htpvmmqtpq ltstimrepk rlrpedsfms
     1141 vypmqtehhq tpldyntqvt wmlaqrqqee arqqqeraam syvklrtnlq hairrgtslm
     1201 eddeepived vmmssegrie dlnegmdfdt mdidlppskn rrertelkpd ffdpasimde
     1261 svlgvsmf
//
LOCUS       NP_001427926             719 aa            linear   PRI 21-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 6 isoform 7 [Homo sapiens].
ACCESSION   NP_001427926 XP_047298630 XP_054184150
VERSION     NP_001427926.1
DBSOURCE    REFSEQ: accession NM_001440997.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 719)
  AUTHORS   Zheng,T., Zhou,H., Zheng,Z., Guo,Y., Liu,J., Zhang,J. and Li,S.
  TITLE     The pathological significance and potential mechanism of ARHGEF6 in
            lung adenocarcinoma
  JOURNAL   Comput Biol Med 158, 106894 (2023)
   PUBMED   37058762
  REMARK    GeneRIF: The pathological significance and potential mechanism of
            ARHGEF6 in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 719)
  AUTHORS   Li,K., Wang,H., Yang,C., Li,C., Xue,B. and Zhou,J.
  TITLE     Clinical implication and potential function of ARHGEF6 in acute
            myeloid leukemia: An in vitro study
  JOURNAL   PLoS One 18 (4), e0283934 (2023)
   PUBMED   37027440
  REMARK    GeneRIF: Clinical implication and potential function of ARHGEF6 in
            acute myeloid leukemia: An in vitro study.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 719)
  AUTHORS   Klambt,V., Buerger,F., Wang,C., Naert,T., Richter,K., Nauth,T.,
            Weiss,A.C., Sieckmann,T., Lai,E., Connaughton,D.M., Seltzsam,S.,
            Mann,N., Majmundar,A.J., Wu,C.W., Onuchic-Whitford,A.C., Shril,S.,
            Schneider,S., Schierbaum,L., Dai,R., Bekheirnia,M.R., Joosten,M.,
            Shlomovitz,O., Vivante,A., Banne,E., Mane,S., Lifton,R.P.,
            Kirschner,K.M., Kispert,A., Rosenberger,G., Fischer,K.D.,
            Lienkamp,S.S., Zegers,M.M.P. and Hildebrandt,F.
  TITLE     Genetic Variants in ARHGEF6 Cause Congenital Anomalies of the
            Kidneys and Urinary Tract in Humans, Mice, and Frogs
  JOURNAL   J Am Soc Nephrol 34 (2), 273-290 (2023)
   PUBMED   36414417
  REMARK    GeneRIF: Genetic Variants in ARHGEF6 Cause Congenital Anomalies of
            the Kidneys and Urinary Tract in Humans, Mice, and Frogs.
REFERENCE   5  (residues 1 to 719)
  AUTHORS   Wang,N., Li,Y., Zhou,X., Wang,X. and Yang,G.
  TITLE     Comprehensive analysis identifies ARHGEF6 as a potential prognostic
            and immunological biomarker in lung adenocarcinoma
  JOURNAL   Comput Biol Med 153, 106448 (2023)
   PUBMED   36586227
  REMARK    GeneRIF: Comprehensive analysis identifies ARHGEF6 as a potential
            prognostic and immunological biomarker in lung adenocarcinoma.
REFERENCE   6  (residues 1 to 719)
  AUTHORS   Yoshii,S., Tanaka,M., Otsuki,Y., Wang,D.Y., Guo,R.J., Zhu,Y.,
            Takeda,R., Hanai,H., Kaneko,E. and Sugimura,H.
  TITLE     alphaPIX nucleotide exchange factor is activated by interaction
            with phosphatidylinositol 3-kinase
  JOURNAL   Oncogene 18 (41), 5680-5690 (1999)
   PUBMED   10523848
REFERENCE   7  (residues 1 to 719)
  AUTHORS   Yntema,H.G., Hamel,B.C., Smits,A.P., van Roosmalen,T., van den
            Helm,B., Kremer,H., Ropers,H.H., Smeets,D.F. and van Bokhoven,H.
  TITLE     Localisation of a gene for non-specific X linked mental retardation
            (MRX46) to Xq25-q26
  JOURNAL   J Med Genet 35 (10), 801-805 (1998)
   PUBMED   9783701
REFERENCE   8  (residues 1 to 719)
  AUTHORS   Ebinu,J.O., Bottorff,D.A., Chan,E.Y., Stang,S.L., Dunn,R.J. and
            Stone,J.C.
  TITLE     RasGRP, a Ras guanyl nucleotide- releasing protein with calcium-
            and diacylglycerol-binding motifs
  JOURNAL   Science 280 (5366), 1082-1086 (1998)
   PUBMED   9582122
REFERENCE   9  (residues 1 to 719)
  AUTHORS   Manser,E., Loo,T.H., Koh,C.G., Zhao,Z.S., Chen,X.Q., Tan,L.,
            Tan,I., Leung,T. and Lim,L.
  TITLE     PAK kinases are directly coupled to the PIX family of nucleotide
            exchange factors
  JOURNAL   Mol Cell 1 (2), 183-192 (1998)
   PUBMED   9659915
REFERENCE   10 (residues 1 to 719)
  AUTHORS   Nomura,N., Nagase,T., Miyajima,N., Sazuka,T., Tanaka,A., Sato,S.,
            Seki,N., Kawarabayasi,Y., Ishikawa,K. and Tabata,S.
  TITLE     Prediction of the coding sequences of unidentified human genes. II.
            The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
            analysis of cDNA clones from human cell line KG-1 (supplement)
  JOURNAL   DNA Res 1 (5), 251-262 (1994)
   PUBMED   7584048
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135783.6.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047298630.1, XP_054184150.1.
            
            Summary: Rho GTPases play a fundamental role in numerous cellular
            processes that are initiated by extracellular stimuli that work
            through G protein coupled receptors. The encoded protein belongs to
            a family of cytoplasmic proteins that activate the Ras-like family
            of Rho proteins by exchanging bound GDP for GTP. It may form a
            complex with G proteins and stimulate Rho-dependent signals. This
            protein is activated by PI3-kinase. Mutations in this gene can
            cause X-chromosomal non-specific cognitive disability. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3368131.1,
                                           SRR18074967.560129.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.3"
     Protein         1..719
                     /product="rho guanine nucleotide exchange factor 6 isoform
                     7"
                     /note="Rac/Cdc42 guanine exchange factor (GEF) 6; rho
                     guanine nucleotide exchange factor 6; PAK-interacting
                     exchange factor, alpha; Rac/Cdc42 guanine nucleotide
                     exchange factor (GEF) 6"
                     /calculated_mol_wt=81021
     Region          <21..60
                     /region_name="CH_SF"
                     /note="calponin homology (CH) domain superfamily; cl00030"
                     /db_xref="CDD:469584"
     Region          58..103
                     /region_name="RhoGEF67_u1"
                     /note="Unstructured region one on RhoGEF 6 and 7;
                     pfam16615"
                     /db_xref="CDD:465201"
     Region          105..162
                     /region_name="SH3_alphaPIX"
                     /note="Src Homology 3 domain of alpha-Pak Interactive
                     eXchange factor; cd12060"
                     /db_xref="CDD:212993"
     Site            order(112,114,117,120..121,136,138..140,151,153,155..156)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212993"
     Region          185..362
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(191,195,289,313..314,317..318,320..321,324..325,
                     328..329,332,358,362)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          393..490
                     /region_name="PH_Cool_Pix"
                     /note="Cloned out of library/PAK-interactive exchange
                     factor pleckstrin homology (PH) domain; cd01225"
                     /db_xref="CDD:269932"
     Region          519..617
                     /region_name="RhoGEF67_u2"
                     /note="Unstructured region two on RhoGEF 6 and 7;
                     pfam16614"
                     /db_xref="CDD:465200"
     Region          628..712
                     /region_name="betaPIX_CC"
                     /note="betaPIX coiled coil; pfam16523"
                     /db_xref="CDD:465158"
     CDS             1..719
                     /gene="ARHGEF6"
                     /gene_synonym="alpha-PIX; alphaPIX; Cool-2; COOL2; MRX46;
                     PIXA"
                     /coded_by="NM_001440997.1:978..3137"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:9459"
                     /db_xref="HGNC:HGNC:685"
                     /db_xref="MIM:300267"
ORIGIN      
        1 mkspaceagl ntnlyvlhee vsskreifdp ddlysgvnfs kvlstllavn katedqlser
       61 pcgrssslsa antsqtnpqg avsstvsglq rqsktvemte ngshqlivka rfnfkqtned
      121 elsvckgdii yvtrveeggw wegtlngrtg wfpsnyvrei ksserplspk avkgfetapl
      181 tknyytvvlq nildtekeya kelqsllvty lrplqsnnnl stvevtsllg nfeevctfqq
      241 tlcqaleecs kfpenqhkvg gcllslmphf ksmylaycan hpsavnvltq hsdeleqfme
      301 nqgasspgil ilttnlskpf mrlekyvtll qelerhmedt hpdhqdilka ivafktlmgq
      361 cqdlrkrkql elqilsepiq awegediknl gnvifmsqvm vqygaceeke erylmlfsnv
      421 limlsasprm sgfiyqgkip iagtvvtrld eiegndctfe itgntveriv vhcnnnqdfq
      481 ewleqlnrli rgpascssls ktsssscsah ssfsstgqpr gpleppqiik pwslsclrpa
      541 pplrpsaalg ykermsyilk esskspktmk kflhkrkter kpseeeyvir kstaaleeda
      601 qilkvieayc tsanfqqghg sstrkdsipq vllpeeekli ieetrsngqt imeekslvdt
      661 vyalkdevre lkqenkrmkq cleeelksrr dleklvrrll kqtdecirge sssktsilp
//
LOCUS       NP_001425388             497 aa            linear   PRI 21-NOV-2025
DEFINITION  excitatory amino acid transporter 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001425388 XP_047273495 XP_054209165
VERSION     NP_001425388.1
DBSOURCE    REFSEQ: accession NM_001438459.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Albury,C.L., Sutherland,H.G., Lam,A.W.Y., Tran,N.K., Lea,R.A.,
            Haupt,L.M. and Griffiths,L.R.
  TITLE     Identification of Polymorphisms in EAAT1 Glutamate Transporter Gene
            SLC1A3 Associated with Reduced Migraine Risk
  JOURNAL   Genes (Basel) 15 (6), 797 (2024)
   PUBMED   38927733
  REMARK    GeneRIF: Identification of Polymorphisms in EAAT1 Glutamate
            Transporter Gene SLC1A3 Associated with Reduced Migraine Risk.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Welby,E. and Ebert,A.D.
  TITLE     Diminished motor neuron activity driven by abnormal astrocytic
            EAAT1 glutamate transporter activity in spinal muscular atrophy is
            not fully restored after lentiviral SMN delivery
  JOURNAL   Glia 71 (5), 1311-1332 (2023)
   PUBMED   36655314
  REMARK    GeneRIF: Diminished motor neuron activity driven by abnormal
            astrocytic EAAT1 glutamate transporter activity in spinal muscular
            atrophy is not fully restored after lentiviral SMN delivery.
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Pant,S., Wu,Q., Ryan,R. and Tajkhorshid,E.
  TITLE     Microscopic Characterization of the Chloride Permeation Pathway in
            the Human Excitatory Amino Acid Transporter 1 (EAAT1)
  JOURNAL   ACS Chem Neurosci 13 (6), 776-785 (2022)
   PUBMED   35192345
  REMARK    GeneRIF: Microscopic Characterization of the Chloride Permeation
            Pathway in the Human Excitatory Amino Acid Transporter 1 (EAAT1).
REFERENCE   5  (residues 1 to 497)
  AUTHORS   Lee,A., Anderson,A.R., Beasley,S.J., Barnett,N.L., Poronnik,P. and
            Pow,D.V.
  TITLE     A new splice variant of the glutamate-aspartate transporter:
            cloning and immunolocalization of GLAST1c in rat, pig and human
            brains
  JOURNAL   J Chem Neuroanat 43 (1), 52-63 (2012)
   PUBMED   22026960
REFERENCE   6  (residues 1 to 497)
  AUTHORS   Vallejo-Illarramendi,A., Domercq,M. and Matute,C.
  TITLE     A novel alternative splicing form of excitatory amino acid
            transporter 1 is a negative regulator of glutamate uptake
  JOURNAL   J Neurochem 95 (2), 341-348 (2005)
   PUBMED   16042756
  REMARK    GeneRIF: EAAT1ex9skip splice variant is a negative regulator of
            full-length EAAT1 function in the human brain
REFERENCE   7  (residues 1 to 497)
  AUTHORS   Takai,S., Yamada,K., Kawakami,H., Tanaka,K. and Nakamura,S.
  TITLE     Localization of the gene (SLC1A3) encoding human glutamate
            transporter (GluT-1) to 5p13 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 209-210 (1995)
   PUBMED   7698014
REFERENCE   8  (residues 1 to 497)
  AUTHORS   Shashidharan,P., Huntley,G.W., Meyer,T., Morrison,J.H. and
            Plaitakis,A.
  TITLE     Neuron-specific human glutamate transporter: molecular cloning,
            characterization and expression in human brain
  JOURNAL   Brain Res 662 (1-2), 245-250 (1994)
   PUBMED   7859077
REFERENCE   9  (residues 1 to 497)
  AUTHORS   Arriza,J.L., Fairman,W.A., Wadiche,J.I., Murdoch,G.H.,
            Kavanaugh,M.P. and Amara,S.G.
  TITLE     Functional comparisons of three glutamate transporter subtypes
            cloned from human motor cortex
  JOURNAL   J Neurosci 14 (9), 5559-5569 (1994)
   PUBMED   7521911
REFERENCE   10 (residues 1 to 497)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010631.6 and AC008957.7.
            
            On or before Apr 21, 2025 this sequence version replaced
            XP_047273495.1, XP_054209165.1.
            
            Summary: This gene encodes a member of a member of a high affinity
            glutamate transporter family. This gene functions in the
            termination of excitatory neurotransmission in central nervous
            system. Mutations are associated with episodic ataxia, Type 6.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.118568.1,
                                           SRR1660805.147930.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..497
                     /product="excitatory amino acid transporter 1 isoform 2"
                     /note="excitatory amino acid transporter 1; GLAST-1;
                     sodium-dependent glutamate/aspartate transporter 1; solute
                     carrier family 1 (glial high affinity glutamate
                     transporter), member 3"
                     /calculated_mol_wt=55018
     Region          46..451
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     CDS             1..497
                     /gene="SLC1A3"
                     /gene_synonym="EA6; EAAT1; GLAST; GLAST1"
                     /coded_by="NM_001438459.1:314..1807"
                     /note="isoform 2 is encoded by transcript variant 11"
                     /db_xref="GeneID:6507"
                     /db_xref="HGNC:HGNC:10941"
                     /db_xref="MIM:600111"
ORIGIN      
        1 mtksngeepk mggrmerfqq gvrkrtllak kkvqnitked vksylfrnaf vlltvtaviv
       61 gtilgftlrp yrmsyrevky fsfpgellmr mlqmlvlpli isslvtgmaa ldskasgkmg
      121 mravvyymtt tiiavvigii iviiihpgkg tkenmhregk ivrvtaadaf ldlirnmfpp
      181 nlveacfkqf ktnyekrsfk vpiqanetlv gavinnvsea metltritee lvpvpgsvng
      241 vnalglvvfs mcfgfvignm keqgqalref fdslneaimr lvavimwyap vgilfliagk
      301 ivemedmgvi ggqlamytvt vivgllihav ivlpllyflv trknpwvfig gllqalital
      361 gtssssatlp itfkcleenn gvdkrvtrfv lpvgatinmd gtalyealaa ifiaqvnnfe
      421 lnfgqiitir drlrtttnvl gdslgagive hlsrhelknr dvemgnsvie enemkkpyql
      481 iaqdnetekp idsetkm
//
LOCUS       NP_001424930             938 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 3 isoform 10 [Homo sapiens].
ACCESSION   NP_001424930 XP_047304942 XP_054203926
VERSION     NP_001424930.1
DBSOURCE    REFSEQ: accession NM_001438001.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Wang,H., Lan,S., Wang,L., Zhao,J., Jia,X., Xu,J., Sun,G., Liu,L.,
            Gong,S., Wang,N., Shan,B., Zhang,F. and Zhang,Z.
  TITLE     Expression of circ-PHC3 enhances ovarian cancer progression via
            regulation of the miR-497-5p/SOX9 pathway
  JOURNAL   J Ovarian Res 16 (1), 142 (2023)
   PUBMED   37468993
  REMARK    GeneRIF: Expression of circ-PHC3 enhances ovarian cancer
            progression via regulation of the miR-497-5p/SOX9 pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 938)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 938)
  AUTHORS   Crea,F., Di Paolo,A., Liu,H.H., Polillo,M., Clermont,P.L.,
            Guerrini,F., Ciabatti,E., Ricci,F., Barate,C., Fontanelli,G.,
            Barsotti,S., Morganti,R., Danesi,R., Wang,Y., Petrini,M.,
            Galimberti,S. and Helgason,C.D.
  TITLE     Polycomb genes are associated with response to imatinib in chronic
            myeloid leukemia
  JOURNAL   Epigenomics 7 (5), 757-765 (2015)
   PUBMED   26343356
  REMARK    GeneRIF: Data show that polycomb-group proteins BMI1, PHC3, CBX6
            and CBX7 expression was significantly increased during imatinib
            treatment.
REFERENCE   6  (residues 1 to 938)
  AUTHORS   Deshpande,A.M., Akunowicz,J.D., Reveles,X.T., Patel,B.B.,
            Saria,E.A., Gorlick,R.G., Naylor,S.L., Leach,R.J. and Hansen,M.F.
  TITLE     PHC3, a component of the hPRC-H complex, associates with E2F6
            during G0 and is lost in osteosarcoma tumors
  JOURNAL   Oncogene 26 (12), 1714-1722 (2007)
   PUBMED   17001316
  REMARK    GeneRIF: loss of PHC3 may favor tumorigenesis by potentially
            disrupting the ability of cells to remain in G(0)
REFERENCE   7  (residues 1 to 938)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   8  (residues 1 to 938)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 938)
  AUTHORS   Tonkin,E., Hagan,D.M., Li,W. and Strachan,T.
  TITLE     Identification and characterisation of novel mammalian homologues
            of Drosophila polyhomeoticpermits new insights into relationships
            between members of the polyhomeotic family
  JOURNAL   Hum Genet 111 (4-5), 435-442 (2002)
   PUBMED   12384788
REFERENCE   10 (residues 1 to 938)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC023891.28 and AC008040.7.
            
            On or before Apr 14, 2025 this sequence version replaced
            XP_047304942.1, XP_054203926.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.988287.1,
                                           SRR18074969.3549857.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.2"
     Protein         1..938
                     /product="polyhomeotic-like protein 3 isoform 10"
                     /note="early development regulator 3; polyhomeotic-like
                     protein 3; homolog of polyhomeotic 3; early development
                     regulatory protein 3; polyhomeotic like 3"
                     /calculated_mol_wt=101367
     Region          <301..>461
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     Region          869..937
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(887..888,922..923,926..927,930)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(898..902,904..905,908..909,913,918)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..938
                     /gene="PHC3"
                     /gene_synonym="EDR3; HPH3"
                     /coded_by="NM_001438001.1:19..2835"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:80012"
                     /db_xref="HGNC:HGNC:15682"
                     /db_xref="MIM:620031"
ORIGIN      
        1 maeaefkdhs tamdtepnpg tssvstttss tttttittss srmqqpqisv ysgsdrhavq
       61 alhrppssaa qylqqmyaaq qqhlmlhtaa lqqqhlsssq lqslaavqas lssgrpstsp
      121 tgsvtqqssm sqtsliftpa ttvaavqsdi pvvsssssss cqsaatqvqn ltlrsqklgv
      181 lsssqngppk stsqtqslti chnkttvtss kisqrdpspe snkkgespsl esrstavtrt
      241 ssihqliapa syspiqphsl ikhqqiplhs ppskvshhql ilqqqqqqiq pitlqnstqd
      301 pppsqhcipl qnhglppaps naqsqhcspi qshpspltvs pnqsqsaqqs vvvspppphs
      361 psqsptiiih pqaliqphpl vssalqpgpn lqqstanqvq ataqlnlpsh lplpaspvvh
      421 igpvqqsalv spgqqivsps hqqysslqss pipiasppqm stsppaqipp lplqsmqslq
      481 vqpeilsqgq vlvqnalvse eelpaaealv qlpfqtlppp qtvavnlqvq ppapvdppvv
      541 yqvedvceee mpeesdecvr mdrtpppptl spaaitvgrg edltsehpll eqvelpavas
      601 vsasviksps dpshvsvppp plllpaattr snstsmhssi psienkppqa ivkpqilthv
      661 iegfviqegl epfpvsrssl lieqpvkkrp lldnqvinsv cvqpelqnnt khadnssdte
      721 medmiaeetl eemdsellkc efcgkmgyan eflrskrfct mscakrynvs cskkfalsrw
      781 nrkpdnqslg hrgrrpsgpd gaarehilrq lpitypsaee dlashedsvp samttrlrrq
      841 serererelr dvrirkmpen sdllpvaqte psiwtvddvw afihslpgcq diadefraqe
      901 idgqallllk edhlmsamni klgpalkica rinslkes
//
LOCUS       NP_001392783            1105 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001392783 XP_006721887
VERSION     NP_001392783.1
DBSOURCE    REFSEQ: accession NM_001405854.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1105)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1105)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1105)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1105)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1105)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1105)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1105)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1105)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1105)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1105)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            On May 5, 2022 this sequence version replaced XP_006721887.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2383822.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1105
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1105
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 1"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=120835
     Site            104
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          145..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          225..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          399..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          733..857
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          850..882
                     /region_name="Required for activation of KAT8 histone
                     acetyltransferase activity"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          885..1005
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     Region          910..928
                     /region_name="Interaction with KAT8 HAT domain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01397"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          938..1034
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            991
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            994
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            1003
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            1045
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          1058..1105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     CDS             1..1105
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405854.1:423..3740"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS11503.2"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankgli
      481 vlgevpppeh ttdlflplss evktdhgtdk liesvsqple nhgapiighi seslstkscg
      541 alrpvngvin tlqpvladhi pgdssdaeeq lhkkqrlnlv ssssdgtcva artrpvlsck
      601 krrlvrpnsi vplskkvhrn stirpgcdvn pscalcgsgs intmppeihy eapllerlsq
      661 ldscvhpvla fpddvptslh fqsmlksqwq nkpfdkikpp kklslkhrap mpgslpdsar
      721 kdrhklvssf lttaklshhq trpdrthrqh lddvgavpmv ervtapkaer llnppppvhd
      781 pnhskmrlrd hssersevlk hhtdmssssy laathhpphs plvrqlstss dspapassss
      841 qvtastsqqp vrrrrgessf dinnivipms vaattrvekl qykeiltpsw revdlqslkg
      901 spdeeneeie dlsdaafaal hakceemera rwlwttsvpp qrrgsrsyrs sdgrttpqlg
      961 sanpstpqpa spdvssshsl seyshgqspr spispelhsa pltpvardtp rhlasedtrc
     1021 stpelgldeq svqpwerrtf plahspqaec edqldaqera arctrrtsgs ktgreteaap
     1081 tsppivplks rhlvaaataq rpthr
//
LOCUS       NP_001393531            1159 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 5 [Homo sapiens].
ACCESSION   NP_001393531
VERSION     NP_001393531.1
DBSOURCE    REFSEQ: accession NM_001406602.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1159)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1159)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1159)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1159)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1159)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1159)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1159)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1159)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1159)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1159)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.758789.1,
                                           SRR14038196.1990872.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1159
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1159
                     /product="hamartin isoform 5"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=129211
     Region          7..714
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          439..571
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <703..>955
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1001..1080
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1095
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1126..1159
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1159
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406602.1:189..3668"
                     /note="isoform 5 is encoded by transcript variant 16"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt aggkgtplgt patspppapl chsddyvhis lpqatvtppr
      421 keermdsarp clhrqhhlln drgseeppgs kgsvtlsdlp gflgdlasee dsiekdkeea
      481 aisrelseit taeaepvvpr ggfdspfyrd slpgsqrkth saasssqgas vnpeplhssl
      541 dklgpdtpkq aftpidlpcg sadespagdr ecqtsletsi ftpspckipp ptrvgfgsgq
      601 pppydhlfev alpktahhfv irkteellkk akgnteedgv pstspmevld rliqqgadah
      661 skelnklplp sksvdwthfg deirtlrdql lllhnqllye rfkrqqhalr nrrllrkvik
      721 aaaleehnaa mkdqlklqek diqmwkvslq keqarynqlq eqrdtmvtkl hsqirqlqhd
      781 reefynqsqe lqtkledcrn miaelrielk kannkvchte lllsqvsqkl snsesvqqqm
      841 eflnrqllvl gevnelyleq lqnkhsdttk evemmkaayr keleknrshv lqqtqrldts
      901 qkrilelesh lakkdhllle qkkyledvkl qargqlqaae sryeaqkrit qvfeleildl
      961 ygrlekdgll kkleeekaea aeaaeerldc cndgcsdsmv ghneeasghn getktprpss
     1021 argssgsrgg ggssssssel stpekpphqr agpfssrwet tmgeasasip ttvgslpssk
     1081 sflgmkarel frnksesqcd edgmtsslse slktelgkdl gveakiplnl dgphpspptp
     1141 dsvgqlhimd ynethhehs
//
LOCUS       NP_001426091             604 aa            linear   PRI 21-NOV-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein Q isoform 11 [Homo
            sapiens].
ACCESSION   NP_001426091 XP_016865666 XP_054210013
VERSION     NP_001426091.1
DBSOURCE    REFSEQ: accession NM_001439162.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Ishtayeh,H., Galves,M., Barnatan,T.T., Berdichevsky,Y.,
            Amer-Sarsour,F., Pasmanik-Chor,M., Braverman,I., Blumen,S.C. and
            Ashkenazi,A.
  TITLE     Oculopharyngeal muscular dystrophy mutations link the RNA-binding
            protein HNRNPQ to autophagosome biogenesis
  JOURNAL   Aging Cell 22 (10), e13949 (2023)
   PUBMED   37559347
  REMARK    GeneRIF: Oculopharyngeal muscular dystrophy mutations link the
            RNA-binding protein HNRNPQ to autophagosome biogenesis.
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Semino,F., Schroter,J., Willemsen,M.H., Bast,T., Biskup,S.,
            Beck-Woedl,S., Brennenstuhl,H., Schaaf,C.P., Kolker,S.,
            Hoffmann,G.F., Haack,T.B. and Syrbe,S.
  TITLE     Further evidence for de novo variants in SYNCRIP as the cause of a
            neurodevelopmental disorder
  JOURNAL   Hum Mutat 42 (9), 1094-1100 (2021)
   PUBMED   34157790
  REMARK    GeneRIF: Further evidence for de novo variants in SYNCRIP as the
            cause of a neurodevelopmental disorder.
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Mourelatos,Z., Abel,L., Yong,J., Kataoka,N. and Dreyfuss,G.
  TITLE     SMN interacts with a novel family of hnRNP and spliceosomal
            proteins
  JOURNAL   EMBO J 20 (19), 5443-5452 (2001)
   PUBMED   11574476
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Lau,P.P., Chang,B.H. and Chan,L.
  TITLE     Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a
            component of apobec-1 editosome
  JOURNAL   Biochem Biophys Res Commun 282 (4), 977-983 (2001)
   PUBMED   11352648
REFERENCE   7  (residues 1 to 604)
  AUTHORS   Blanc,V., Navaratnam,N., Henderson,J.O., Anant,S., Kennedy,S.,
            Jarmuz,A., Scott,J. and Davidson,N.O.
  TITLE     Identification of GRY-RBP as an apolipoprotein B RNA-binding
            protein that interacts with both apobec-1 and apobec-1
            complementation factor to modulate C to U editing
  JOURNAL   J Biol Chem 276 (13), 10272-10283 (2001)
   PUBMED   11134005
REFERENCE   8  (residues 1 to 604)
  AUTHORS   Grosset,C., Chen,C.Y., Xu,N., Sonenberg,N., Jacquemin-Sablon,H. and
            Shyu,A.B.
  TITLE     A mechanism for translationally coupled mRNA turnover: interaction
            between the poly(A) tail and a c-fos RNA coding determinant via a
            protein complex
  JOURNAL   Cell 103 (1), 29-40 (2000)
   PUBMED   11051545
REFERENCE   9  (residues 1 to 604)
  AUTHORS   Mizutani,A., Fukuda,M., Ibata,K., Shiraishi,Y. and Mikoshiba,K.
  TITLE     SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear
            ribonucleoprotein R, interacts with ubiquitous synaptotagmin
            isoforms
  JOURNAL   J Biol Chem 275 (13), 9823-9831 (2000)
   PUBMED   10734137
REFERENCE   10 (residues 1 to 604)
  AUTHORS   Harris,C.E., Boden,R.A. and Astell,C.R.
  TITLE     A novel heterogeneous nuclear ribonucleoprotein-like protein
            interacts with NS1 of the minute virus of mice
  JOURNAL   J Virol 73 (1), 72-80 (1999)
   PUBMED   9847309
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136082.22.
            
            On or before Apr 28, 2025 this sequence version replaced
            XP_016865666.1, XP_054210013.1.
            
            Summary: This gene encodes a member of the cellular heterogeneous
            nuclear ribonucleoprotein (hnRNP) family. hnRNPs are RNA binding
            proteins that complex with heterogeneous nuclear RNA (hnRNA) and
            regulate alternative splicing, polyadenylation, and other aspects
            of mRNA metabolism and transport. The encoded protein plays a role
            in multiple aspects of mRNA maturation and is associated with
            several multiprotein complexes including the apoB RNA
            editing-complex and survival of motor neurons (SMN) complex.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene, and a pseudogene of this
            gene is located on the short arm of chromosome 20. [provided by
            RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.326480.1,
                                           SRR14038194.3993880.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.3"
     Protein         1..604
                     /product="heterogeneous nuclear ribonucleoprotein Q
                     isoform 11"
                     /note="NS1-associated protein 1; heterogeneous nuclear
                     ribonucleoprotein Q; glycine- and tyrosine-rich
                     RNA-binding protein"
                     /calculated_mol_wt=67173
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          23..107
                     /region_name="NURR_hnRNPQ"
                     /note="NURR (N-terminal unit for RNA recognition) domain
                     found in heterogeneous nuclear ribonucleoprotein Q
                     (hnRNPQ) and similar proteins; cd21066"
                     /db_xref="CDD:410954"
     Region          103..592
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            221
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            363
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:12601080; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          400..561
                     /region_name="Interaction with APOBEC1"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            444
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          448..559
                     /region_name="8 X 3 AA repeats of R-G-G"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Region          460..488
                     /region_name="3 X 4 AA repeats of Y-Y-G-Y"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            496
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            510
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          518..549
                     /region_name="Interaction with SMN.
                     /evidence=ECO:0000269|PubMed:11574476"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            518
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            526
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            536
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            539
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          564..578
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            587
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     CDS             1..604
                     /gene="SYNCRIP"
                     /gene_synonym="GRY-RBP; GRYRBP; hnRNP-Q; HNRNPQ; HNRPQ1;
                     NSAP1; PP68"
                     /coded_by="NM_001439162.1:103..1917"
                     /note="isoform 11 is encoded by transcript variant 13"
                     /db_xref="GeneID:10492"
                     /db_xref="HGNC:HGNC:16918"
                     /db_xref="MIM:616686"
ORIGIN      
        1 matehvngng teepmdttsa vihsenfqtl ldaglpqkva ekldeiyvag lvahsdlder
       61 aiealkefne dgalavlqqf kdsdlshvqn ksaflcgvmk tyrqrekqgt kvadsskgpd
      121 eakikaller tgytldvttg qrkyggpppd svysgqqpsv gteifvgkip rdlfedelvp
      181 lfekagpiwd lrlmmdpltg lnrgyafvtf ctkeaaqeav klynnheirs gkhigvcisv
      241 annrlfvgsi pksktkeqil eefskvtegl tdvilyhqpd dkkknrgfcf leyedhktaa
      301 qarrrlmsgk vkvwgnvgtv ewadpiedpd pevmakvkvl fvrnlantvt eeilekafsq
      361 fgklervkkl kdyafihfde rdgavkamee mngkdlegen ieivfakppd qkrkerkaqr
      421 qaaknqmydd yyyygpphmp pptrgrgrgg rggygyppdy ygyedyydyy gydyhnyrgg
      481 yedpyygyed fqvgargrgg rgargaapsr grgaapprgr agysqrggpg sargvrgarg
      541 gaqqqrgrgv rgarggrggn vggkrkadgy nqpdskrrqt nnqnwgsqpi aqqplqgkrg
      601 rgrs
//
LOCUS       NP_001394193             393 aa            linear   PRI 21-NOV-2025
DEFINITION  cellular tumor antigen p53 isoform a [Homo sapiens].
ACCESSION   NP_001394193
VERSION     NP_001394193.1
DBSOURCE    REFSEQ: accession NM_001407264.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Mirgayazova,R., Khadiullina,R., Chasov,V., Mingaleeva,R.,
            Miftakhova,R., Rizvanov,A. and Bulatov,E.
  TITLE     Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an Option?
  JOURNAL   Genes (Basel) 11 (6), 704 (2020)
   PUBMED   32630614
  REMARK    GeneRIF: Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an
            Option?
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Flynt,E., Bisht,K., Sridharan,V., Ortiz,M., Towfic,F. and
            Thakurta,A.
  TITLE     Prognosis, Biology, and Targeting of TP53 Dysregulation in Multiple
            Myeloma
  JOURNAL   Cells 9 (2), 287 (2020)
   PUBMED   31991614
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Barnoud,T., Parris,J.L.D. and Murphy,M.E.
  TITLE     Common genetic variants in the TP53 pathway and their impact on
            cancer
  JOURNAL   J Mol Cell Biol 11 (7), 578-585 (2019)
   PUBMED   31152665
  REMARK    GeneRIF: Common genetic variants in the TP53 pathway and their
            impact on cancer.
            Review article
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Hu,W., Chen,S., Thorne,R.F. and Wu,M.
  TITLE     TP53, TP53 Target Genes (DRAM, TIGAR), and Autophagy
  JOURNAL   Adv Exp Med Biol 1206, 127-149 (2019)
   PUBMED   31776983
  REMARK    Review article
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Baugh,E.H., Ke,H., Levine,A.J., Bonneau,R.A. and Chan,C.S.
  TITLE     Why are there hotspot mutations in the TP53 gene in human cancers?
  JOURNAL   Cell Death Differ 25 (1), 154-160 (2018)
   PUBMED   29099487
  REMARK    GeneRIF: TP53 missense mutant alleles that occur in human cancers
            are discussed in the context of high resolution models of these p53
            mutant protein structures to determine the structural features of
            mutations (review).
            Review article
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Aubrey,B.J., Strasser,A. and Kelly,G.L.
  TITLE     Tumor-Suppressor Functions of the TP53 Pathway
  JOURNAL   Cold Spring Harb Perspect Med 6 (5), a026062 (2016)
   PUBMED   27141080
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Soussi,T. and Wiman,K.G.
  TITLE     TP53: an oncogene in disguise
  JOURNAL   Cell Death Differ 22 (8), 1239-1249 (2015)
   PUBMED   26024390
  REMARK    Review article
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Soussi,T.
  TITLE     The TP53 gene network in a postgenomic era
  JOURNAL   Hum Mutat 35 (6), 641-642 (2014)
   PUBMED   24753184
  REMARK    GeneRIF: Recommendations and guidelines for reporting and
            annotating TP53 variants are also provided, to help researchers
            generate standardized data that are easy to understand, analyze,
            and exchange across various cancer variant databases
            Review article
REFERENCE   9  (residues 1 to 393)
  AUTHORS   Anczukow,O., Ware,M.D., Buisson,M., Zetoune,A.B.,
            Stoppa-Lyonnet,D., Sinilnikova,O.M. and Mazoyer,S.
  TITLE     Does the nonsense-mediated mRNA decay mechanism prevent the
            synthesis of truncated BRCA1, CHK2, and p53 proteins?
  JOURNAL   Hum Mutat 29 (1), 65-73 (2008)
   PUBMED   17694537
  REMARK    GeneRIF: the p53 protein encoded by the 770delT allele is as
            abundant as the wild-type protein, as removal of the C-terminal p53
            domain leads to a stabilized mutant protein, whose abundance is
            markedly increased when NMD is inhibited.
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Bourdon,J.C.
  TITLE     p53 Family isoforms
  JOURNAL   Curr Pharm Biotechnol 8 (6), 332-336 (2007)
   PUBMED   18289041
  REMARK    Review article
REFERENCE   11 (residues 1 to 393)
  AUTHORS   Candeias,M.M., Powell,D.J., Roubalova,E., Apcher,S., Bourougaa,K.,
            Vojtesek,B., Bruzzoni-Giovanelli,H. and Fahraeus,R.
  TITLE     Expression of p53 and p53/47 are controlled by alternative
            mechanisms of messenger RNA translation initiation
  JOURNAL   Oncogene 25 (52), 6936-6947 (2006)
   PUBMED   16983332
  REMARK    GeneRIF: harbouring alternative translation initiation sites, the
            p53 mRNA gives rise to different levels of the p53 isoforms which
            help to orchestrate the cell biological outcome of p53 activation
REFERENCE   12 (residues 1 to 393)
  AUTHORS   Murray-Zmijewski,F., Lane,D.P. and Bourdon,J.C.
  TITLE     p53/p63/p73 isoforms: an orchestra of isoforms to harmonise cell
            differentiation and response to stress
  JOURNAL   Cell Death Differ 13 (6), 962-972 (2006)
   PUBMED   16601753
  REMARK    Review article
REFERENCE   13 (residues 1 to 393)
  AUTHORS   Bourdon,J.C., Fernandes,K., Murray-Zmijewski,F., Liu,G., Diot,A.,
            Xirodimas,D.P., Saville,M.K. and Lane,D.P.
  TITLE     p53 isoforms can regulate p53 transcriptional activity
  JOURNAL   Genes Dev 19 (18), 2122-2137 (2005)
   PUBMED   16131611
  REMARK    GeneRIF: p53 isoforms can regulate p53 transcriptional activity.
REFERENCE   14 (residues 1 to 393)
  AUTHORS   Ghosh,A., Stewart,D. and Matlashewski,G.
  TITLE     Regulation of human p53 activity and cell localization by
            alternative splicing
  JOURNAL   Mol Cell Biol 24 (18), 7987-7997 (2004)
   PUBMED   15340061
  REMARK    GeneRIF: mechanism of p53 regulation originating through
            alternative splicing of the human p53 gene resulting in the
            expression of a novel p53 mRNA
REFERENCE   15 (residues 1 to 393)
  AUTHORS   Flaman,J.M., Waridel,F., Estreicher,A., Vannier,A., Limacher,J.M.,
            Gilbert,D., Iggo,R. and Frebourg,T.
  TITLE     The human tumour suppressor gene p53 is alternatively spliced in
            normal cells
  JOURNAL   Oncogene 12 (4), 813-818 (1996)
   PUBMED   8632903
REFERENCE   16 (residues 1 to 393)
  AUTHORS   Schneider,K., Zelley,K., Nichols,K.E., Schwartz Levine,A. and
            Garber,J.
  TITLE     Li-Fraumeni Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301488
REFERENCE   17 (residues 1 to 393)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   18 (residues 1 to 393)
  AUTHORS   Lamb,P. and Crawford,L.
  TITLE     Characterization of the human p53 gene
  JOURNAL   Mol Cell Biol 6 (5), 1379-1385 (1986)
   PUBMED   2946935
REFERENCE   19 (residues 1 to 393)
  AUTHORS   Isobe,M., Emanuel,B.S., Givol,D., Oren,M. and Croce,C.M.
  TITLE     Localization of gene for human p53 tumour antigen to band 17p13
  JOURNAL   Nature 320 (6057), 84-85 (1986)
   PUBMED   3456488
REFERENCE   20 (residues 1 to 393)
  AUTHORS   Benchimol,S., Lamb,P., Crawford,L.V., Sheer,D., Shows,T.B.,
            Bruns,G.A. and Peacock,J.
  TITLE     Transformation associated p53 protein is encoded by a gene on human
            chromosome 17
  JOURNAL   Somat Cell Mol Genet 11 (5), 505-510 (1985)
   PUBMED   2994241
REFERENCE   21 (residues 1 to 393)
  AUTHORS   Harlow,E., Williamson,N.M., Ralston,R., Helfman,D.M. and Adams,T.E.
  TITLE     Molecular cloning and in vitro expression of a cDNA clone for human
            cellular tumor antigen p53
  JOURNAL   Mol Cell Biol 5 (7), 1601-1610 (1985)
   PUBMED   3894933
REFERENCE   22 (residues 1 to 393)
  AUTHORS   Zakut-Houri,R., Bienz-Tadmor,B., Givol,D. and Oren,M.
  TITLE     Human p53 cellular tumor antigen: cDNA sequence and expression in
            COS cells
  JOURNAL   EMBO J 4 (5), 1251-1255 (1985)
   PUBMED   4006916
REFERENCE   23 (residues 1 to 393)
  AUTHORS   Matlashewski,G., Lamb,P., Pim,D., Peacock,J., Crawford,L. and
            Benchimol,S.
  TITLE     Isolation and characterization of a human p53 cDNA clone:
            expression of the human p53 gene
  JOURNAL   EMBO J 3 (13), 3257-3262 (1984)
   PUBMED   6396087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087388.9 and AC007421.13.
            
            Summary: This gene encodes a tumor suppressor protein containing
            transcriptional activation, DNA binding, and oligomerization
            domains. The encoded protein responds to diverse cellular stresses
            to regulate expression of target genes, thereby inducing cell cycle
            arrest, apoptosis, senescence, DNA repair, or changes in
            metabolism. Mutations in this gene are associated with a variety of
            human cancers, including hereditary cancers such as Li-Fraumeni
            syndrome. Alternative splicing of this gene and the use of
            alternate promoters result in multiple transcript variants and
            isoforms. Additional isoforms have also been shown to result from
            the use of alternate translation initiation codons from identical
            transcript variants (PMIDs: 12032546, 20937277). [provided by
            RefSeq, Dec 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2206180.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..393
                     /product="cellular tumor antigen p53 isoform a"
                     /note="tumor protein 53; mutant tumor protein 53; cellular
                     tumor antigen p53; phosphoprotein p53;
                     transformation-related protein 53; antigen NY-CO-13; tumor
                     supressor p53"
                     /calculated_mol_wt=43522
     Region          1..320
                     /region_name="Interaction with CCAR2.
                     /evidence=ECO:0000269|PubMed:25732823"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          1..83
                     /region_name="Interaction with HRMT1L2.
                     /evidence=ECO:0000269|PubMed:15186775"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          1..44
                     /region_name="Transcription activation (acidic)"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          6..30
                     /region_name="P53_TAD"
                     /note="P53 transactivation motif; pfam08563"
                     /db_xref="CDD:462520"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by HIPK4.
                     /evidence=ECO:0000269|PubMed:18022393; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5, PRPK, AMPK, NUAK1 and ATM.
                     /evidence=ECO:0000269|PubMed:10570149,
                     ECO:0000269|PubMed:11554766, ECO:0000269|PubMed:15866171,
                     ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:17591690,
                     ECO:0000269|PubMed:17967874, ECO:0000269|PubMed:21317932,
                     ECO:0000269|PubMed:28842590; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          17..25
                     /region_name="TADI"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK1, VRK1 and VRK2.
                     /evidence=ECO:0000269|PubMed:10606744,
                     ECO:0000269|PubMed:10951572, ECO:0000269|PubMed:16704422,
                     ECO:0000269|PubMed:31527692; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CHEK2, CK1 and PLK3.
                     /evidence=ECO:0000269|PubMed:10570149,
                     ECO:0000269|PubMed:11447225, ECO:0000269|PubMed:11551930,
                     ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:20041275;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5 and CDK7.
                     /evidence=ECO:0000269|PubMed:17591690,
                     ECO:0000269|PubMed:9372954; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          35..59
                     /region_name="TAD2"
                     /note="Transactivation domain 2; pfam18521"
                     /db_xref="CDD:375947"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK5.
                     /evidence=ECO:0000269|PubMed:17254968; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5, DYRK2, HIPK2 and PKC/PRKCG.
                     /evidence=ECO:0000269|PubMed:11740489,
                     ECO:0000269|PubMed:11780126, ECO:0000269|PubMed:16377624,
                     ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:17591690;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          48..56
                     /region_name="TADII"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          50..96
                     /region_name="Disordered.
                     /evidence=ECO:0000269|PubMed:31953488"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by TAF1 and GRK5.
                     /evidence=ECO:0000269|PubMed:15053879,
                     ECO:0000269|PubMed:20124405; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          66..110
                     /region_name="Interaction with WWOX"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          100..370
                     /region_name="Interaction with HIPK1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          100..300
                     /region_name="Required for interaction with ZNF385A.
                     /evidence=ECO:0000269|PubMed:17719541"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          109..288
                     /region_name="P53"
                     /note="P53 DNA-binding domain; cd08367"
                     /db_xref="CDD:176262"
     Region          113..236
                     /region_name="Required for interaction with FBXO42.
                     /evidence=ECO:0000269|PubMed:19509332"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          116..292
                     /region_name="Interaction with AXIN1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            120
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000269|PubMed:16793544,
                     ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            120
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:17189187,
                     ECO:0000269|PubMed:19854137, ECO:0000269|PubMed:23431171;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            order(176,179,238,242)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:176262"
     Site            order(177..179,181)
                     /site_type="other"
                     /note="dimerization site [polypeptide binding]"
                     /db_xref="CDD:176262"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB.
                     /evidence=ECO:0000269|PubMed:20959462; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            order(239,241,248,273,275..277,280)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176262"
     Region          241..248
                     /region_name="Interaction with the 53BP2 SH3 domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          256..294
                     /region_name="Interaction with E4F1.
                     /evidence=ECO:0000269|PubMed:10644996"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB.
                     /evidence=ECO:0000269|PubMed:20959462; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          273..280
                     /region_name="Interaction with DNA"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          282..325
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AURKB.
                     /evidence=ECO:0000269|PubMed:20959462; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          300..393
                     /region_name="Interaction with CARM1.
                     /evidence=ECO:0000269|PubMed:15186775"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          305..321
                     /region_name="Bipartite nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            305
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:12724314; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKA, CDK1 and CDK2.
                     /evidence=ECO:0000269|PubMed:10884347,
                     ECO:0000269|PubMed:14702041; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          319..360
                     /region_name="Interaction with HIPK2"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          319..358
                     /region_name="P53_tetramer"
                     /note="P53 tetramerization motif; pfam07710"
                     /db_xref="CDD:462238"
     Site            321
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P02340; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          325..356
                     /region_name="Oligomerization"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            333
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, by PRMT5.
                     /evidence=ECO:0000269|PubMed:19011621; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            335
                     /site_type="methylation"
                     /note="Symmetric dimethylarginine, by PRMT5.
                     /evidence=ECO:0000269|PubMed:19011621; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            337
                     /site_type="methylation"
                     /note="Symmetric dimethylarginine, by PRMT5.
                     /evidence=ECO:0000269|PubMed:19011621; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          339..350
                     /region_name="Nuclear export signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          351..393
                     /region_name="Disordered.
                     /evidence=ECO:0000269|PubMed:31953488,
                     ECO:0000269|PubMed:36108750"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          359..363
                     /region_name="Interaction with USP7"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          368..387
                     /region_name="Basic (repression of DNA-binding)"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          370..372
                     /region_name="[KR]-[STA]-K motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            370
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:17108971,
                     ECO:0000269|PubMed:22864287; N6-methyllysine, by SMYD2,
                     alternate. /evidence=ECO:0000269|PubMed:17108971,
                     ECO:0000269|PubMed:22864287; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            372
                     /site_type="methylation"
                     /note="N6-methyllysine, by SETD7.
                     /evidence=ECO:0000269|PubMed:15525938,
                     ECO:0000269|PubMed:16415881; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            373
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, by EHMT1 and EHMT2,
                     alternate. /evidence=ECO:0000269|PubMed:20118233;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            373
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:10656795; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          374..393
                     /region_name="Interaction with MORN3.
                     /evidence=ECO:0000269|PubMed:29681526"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            381
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:29474172,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            382
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:17707234,
                     ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22864287;
                     N6-methyllysine, by KMT5A, alternate.
                     /evidence=ECO:0000269|PubMed:17707234,
                     ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22864287;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            382
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:10656795,
                     ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:20228809,
                     ECO:0000269|PubMed:23431171, ECO:0000269|PubMed:29681526,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2, CDK2 and NUAK1.
                     /evidence=ECO:0000269|PubMed:10884347,
                     ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:17108107,
                     ECO:0000269|PubMed:21317932, ECO:0000269|PubMed:22214662,
                     ECO:0000269|PubMed:35618207; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     CDS             1..393
                     /gene="TP53"
                     /gene_synonym="BCC7; BMFS5; LFS1; P53; TRP53"
                     /coded_by="NM_001407264.1:153..1334"
                     /note="isoform a is encoded by transcript variant 10"
                     /db_xref="GeneID:7157"
                     /db_xref="HGNC:HGNC:11998"
                     /db_xref="MIM:191170"
ORIGIN      
        1 meepqsdpsv epplsqetfs dlwkllpenn vlsplpsqam ddlmlspddi eqwftedpgp
       61 deaprmpeaa ppvapapaap tpaapapaps wplsssvpsq ktyqgsygfr lgflhsgtak
      121 svtctyspal nkmfcqlakt cpvqlwvdst pppgtrvram aiykqsqhmt evvrrcphhe
      181 rcsdsdglap pqhlirvegn lrveylddrn tfrhsvvvpy eppevgsdct tihynymcns
      241 scmggmnrrp iltiitleds sgnllgrnsf evrvcacpgr drrteeenlr kkgephhelp
      301 pgstkralpn ntssspqpkk kpldgeyftl qirgrerfem frelnealel kdaqagkepg
      361 gsrahsshlk skkgqstsrh kklmfktegp dsd
//
LOCUS       NP_001427236             392 aa            linear   PRI 21-NOV-2025
DEFINITION  G1/S-specific cyclin-E1 isoform 8 [Homo sapiens].
ACCESSION   NP_001427236
VERSION     NP_001427236.1
DBSOURCE    REFSEQ: accession NM_001440307.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Lee,S.J., Jeon,S.H., Cho,S., Kim,C.M., Yoo,J.K., Oh,S.H., Kim,J.H.,
            Yang,Y.D. and Kim,J.K.
  TITLE     hsa-miR-CHA2, a novel microRNA, exhibits anticancer effects by
            suppressing cyclin E1 in human non-small cell lung cancer cells
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (6), 167250 (2024)
   PUBMED   38763409
  REMARK    GeneRIF: hsa-miR-CHA2, a novel microRNA, exhibits anticancer
            effects by suppressing cyclin E1 in human non-small cell lung
            cancer cells.
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Rustgi,N., Wu,S., Samec,T., Walker,P., Xiu,J., Lou,E., Goel,S.,
            Saeed,A. and Moy,R.H.
  TITLE     Molecular Landscape and Clinical Implication of CCNE1-amplified
            Esophagogastric Cancer
  JOURNAL   Cancer Res Commun 4 (6), 1399-1409 (2024)
   PUBMED   38717153
  REMARK    GeneRIF: Molecular Landscape and Clinical Implication of
            CCNE1-amplified Esophagogastric Cancer.
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Audrey,A., Kok,Y.P., Yu,S., de Haan,L., van de Kooij,B., van den
            Tempel,N., Chen,M., de Boer,H.R., van der Vegt,B. and van
            Vugt,M.A.T.M.
  TITLE     RAD52-dependent mitotic DNA synthesis is required for genome
            stability in Cyclin E1-overexpressing cells
  JOURNAL   Cell Rep 43 (4), 114116 (2024)
   PUBMED   38625790
  REMARK    GeneRIF: RAD52-dependent mitotic DNA synthesis is required for
            genome stability in Cyclin E1-overexpressing cells.
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Mumberg,D., Wick,M., Burger,C., Haas,K., Funk,M. and Muller,R.
  TITLE     Cyclin ET, a new splice variant of human cyclin E with a unique
            expression pattern during cell cycle progression and
            differentiation
  JOURNAL   Nucleic Acids Res 25 (11), 2098-2105 (1997)
   PUBMED   9153308
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Sewing,A., Ronicke,V., Burger,C., Funk,M. and Muller,R.
  TITLE     Alternative splicing of human cyclin E
  JOURNAL   J Cell Sci 107 (Pt 2), 581-588 (1994)
   PUBMED   8207080
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Koff,A., Giordano,A., Desai,D., Yamashita,K., Harper,J.W.,
            Elledge,S., Nishimoto,T., Morgan,D.O., Franza,B.R. and Roberts,J.M.
  TITLE     Formation and activation of a cyclin E-cdk2 complex during the G1
            phase of the human cell cycle
  JOURNAL   Science 257 (5077), 1689-1694 (1992)
   PUBMED   1388288
REFERENCE   8  (residues 1 to 392)
  AUTHORS   Hinds,P.W., Mittnacht,S., Dulic,V., Arnold,A., Reed,S.I. and
            Weinberg,R.A.
  TITLE     Regulation of retinoblastoma protein functions by ectopic
            expression of human cyclins
  JOURNAL   Cell 70 (6), 993-1006 (1992)
   PUBMED   1388095
REFERENCE   9  (residues 1 to 392)
  AUTHORS   Koff,A., Cross,F., Fisher,A., Schumacher,J., Leguellec,K.,
            Philippe,M. and Roberts,J.M.
  TITLE     Human cyclin E, a new cyclin that interacts with two members of the
            CDC2 gene family
  JOURNAL   Cell 66 (6), 1217-1228 (1991)
   PUBMED   1833068
REFERENCE   10 (residues 1 to 392)
  AUTHORS   Lew,D.J., Dulic,V. and Reed,S.I.
  TITLE     Isolation of three novel human cyclins by rescue of G1 cyclin (Cln)
            function in yeast
  JOURNAL   Cell 66 (6), 1197-1206 (1991)
   PUBMED   1833066
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008798.10.
            
            Summary: The protein encoded by this gene belongs to the highly
            conserved cyclin family, whose members are characterized by a
            dramatic periodicity in protein abundance through the cell cycle.
            Cyclins function as regulators of CDK kinases. Different cyclins
            exhibit distinct expression and degradation patterns which
            contribute to the temporal coordination of each mitotic event. This
            cyclin forms a complex with and functions as a regulatory subunit
            of CDK2, whose activity is required for cell cycle G1/S transition.
            This protein accumulates at the G1-S phase boundary and is degraded
            as cells progress through S phase. Overexpression of this gene has
            been observed in many tumors, which results in chromosome
            instability, and thus may contribute to tumorigenesis. This protein
            was found to associate with, and be involved in, the
            phosphorylation of NPAT protein (nuclear protein mapped to the ATM
            locus), which participates in cell-cycle regulated histone gene
            expression and plays a critical role in promoting cell-cycle
            progression in the absence of pRB. [provided by RefSeq, Apr 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1826661.1,
                                           SRR14038194.3907219.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..392
                     /product="G1/S-specific cyclin-E1 isoform 8"
                     /note="G1/S-specific cyclin-E1"
                     /calculated_mol_wt=44631
     Region          85..221
                     /region_name="CYCLIN_CCNE1_rpt1"
                     /note="first cyclin box found in G1/S-specific cyclin-E1
                     (CCNE1); cd20579"
                     /db_xref="CDD:410282"
     Site            order(91..92,94,97..98,101..102,105,109,144,179,183..187,
                     191..192,209,212..213,216..217,220..221)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410282"
     Region          225..338
                     /region_name="CYCLIN_CCNE1_rpt2"
                     /note="second cyclin box found in G1/S-specific cyclin-E1
                     (CCNE1); cd20581"
                     /db_xref="CDD:410284"
     Site            order(226,233..234,237,246..250,252,337..338)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410284"
     CDS             1..392
                     /gene="CCNE1"
                     /gene_synonym="CCNE; pCCNE1"
                     /coded_by="NM_001440307.1:185..1363"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:898"
                     /db_xref="HGNC:HGNC:1589"
                     /db_xref="MIM:123837"
ORIGIN      
        1 mkedggaefs arsrkrkanv tvdpdeemak idrtardqcg sqpwdnnavc adpcsliptp
       61 dkedddrvyp nstckpriia psrgsplpvl swanreevwk imlnkektyl rdqhfleqhp
      121 llqpkmrail ldwlmevcev yklhretfyl aqdffdryma tqenvvktll qligisslfi
      181 aakleeiypp klhqfayvtd gacsgdeilt melmimkalk wrlspltivs wlnvymqvay
      241 lndlhevllp qypqqifiqi aelldlcvld vdclefpygi laasalyhfs sselmqkvsg
      301 yqwcdiencv kwmvpfamvi retgssklkh frgvadedah niqthrdsld lldkarakka
      361 mlseqnrasp lpsglltppq sgkkqssgpe ma
//
LOCUS       NP_001396232            2696 aa            linear   PRI 21-NOV-2025
DEFINITION  histone-lysine N-methyltransferase, H3 lysine-36 specific isoform b
            [Homo sapiens].
ACCESSION   NP_001396232
VERSION     NP_001396232.1
DBSOURCE    REFSEQ: accession NM_001409303.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2696)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2696)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   3  (residues 1 to 2696)
  AUTHORS   Conteduca,G., Cangelosi,D., Baldo,C., Arado,A., Testa,B.,
            Wagner,R.T., Robertson,K.D., Dequiedt,F., Fitzsimmons,L.,
            Malacarne,M., Filaci,G. and Coviello,D.A.
  TITLE     Impact of NSD1 Alternative Transcripts in Actin Filament Formation
            and Cellular Division Pathways in Fibroblasts
  JOURNAL   Genes (Basel) 15 (9), 1117 (2024)
   PUBMED   39336709
  REMARK    GeneRIF: Impact of NSD1 Alternative Transcripts in Actin Filament
            Formation and Cellular Division Pathways in Fibroblasts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2696)
  AUTHORS   Ren,Z., Yue,L., Hu,H.Y., Hou,X.L., Chen,W.Q., Tan,Y., Dong,Z. and
            Zhang,J.
  TITLE     Identification of Novel NSD1 variations in four Pediatric cases
            with sotos Syndrome
  JOURNAL   BMC Med Genomics 17 (1), 116 (2024)
   PUBMED   38684994
  REMARK    GeneRIF: Identification of Novel NSD1 variations in four Pediatric
            cases with sotos Syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2696)
  AUTHORS   Wang,X., Yeh,S., Wu,G., Hsu,C.L., Wang,L., Chiang,T., Yang,Y.,
            Guo,Y. and Chang,C.
  TITLE     Identification and characterization of a novel androgen receptor
            coregulator ARA267-alpha in prostate cancer cells
  JOURNAL   J Biol Chem 276 (44), 40417-40423 (2001)
   PUBMED   11509567
REFERENCE   6  (residues 1 to 2696)
  AUTHORS   Jaju,R.J., Fidler,C., Haas,O.A., Strickson,A.J., Watkins,F.,
            Clark,K., Cross,N.C., Cheng,J.F., Aplan,P.D., Kearney,L.,
            Boultwood,J. and Wainscoat,J.S.
  TITLE     A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in
            de novo childhood acute myeloid leukemia
  JOURNAL   Blood 98 (4), 1264-1267 (2001)
   PUBMED   11493482
REFERENCE   7  (residues 1 to 2696)
  AUTHORS   Lee,D.K., Duan,H.O. and Chang,C.
  TITLE     Androgen receptor interacts with the positive elongation factor
            P-TEFb and enhances the efficiency of transcriptional elongation
  JOURNAL   J Biol Chem 276 (13), 9978-9984 (2001)
   PUBMED   11266437
REFERENCE   8  (residues 1 to 2696)
  AUTHORS   Huang,N., vom Baur,E., Garnier,J.M., Lerouge,T., Vonesch,J.L.,
            Lutz,Y., Chambon,P. and Losson,R.
  TITLE     Two distinct nuclear receptor interaction domains in NSD1, a novel
            SET protein that exhibits characteristics of both corepressors and
            coactivators
  JOURNAL   EMBO J 17 (12), 3398-3412 (1998)
   PUBMED   9628876
REFERENCE   9  (residues 1 to 2696)
  AUTHORS   Ocansey,S., Cole,T.R.P., Rahman,N. and Tatton-Brown,K.
  TITLE     Sotos Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301652
REFERENCE   10 (residues 1 to 2696)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027314.5, AC008570.6 and
            AC146507.2.
            
            Summary: This gene encodes a protein containing a SET domain, 2
            LXXLL motifs, 3 nuclear translocation signals (NLSs), 4 plant
            homeodomain (PHD) finger regions, and a proline-rich region. The
            encoded protein enhances androgen receptor (AR) transactivation,
            and this enhancement can be increased further in the presence of
            other androgen receptor associated coregulators. This protein may
            act as a nucleus-localized, basic transcriptional factor and also
            as a bifunctional transcriptional regulator. Mutations of this gene
            have been associated with Sotos syndrome and Weaver syndrome. One
            version of childhood acute myeloid leukemia is the result of a
            cryptic translocation with the breakpoints occurring within nuclear
            receptor-binding Su-var, enhancer of zeste, and trithorax domain
            protein 1 on chromosome 5 and nucleoporin, 98-kd on chromosome 11.
            Multiple transcript variants encoding distinct isoforms have been
            identified for this gene. [provided by RefSeq, Sep 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.203190.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2696
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..2696
                     /product="histone-lysine N-methyltransferase, H3 lysine-36
                     specific isoform b"
                     /EC_number="2.1.1.357"
                     /note="androgen receptor-associated coregulator 267;
                     histone-lysine N-methyltransferase, H3 lysine-36 and H4
                     lysine-20 specific; H3-K36-HMTase; H4-K20-HMTase; lysine
                     N-methyltransferase 3B; NR-binding SET domain-containing
                     protein; androgen receptor coactivator 267 kDa protein;
                     androgen receptor-associated protein of 267 kDa; nuclear
                     receptor-binding SET domain-containing protein 1; nuclear
                     receptor SET domain-containing protein 1; histone-lysine
                     N-methyltransferase, H3 lysine-36 specific"
                     /calculated_mol_wt=296522
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88491; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          207..252
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          281..311
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          318..433
                     /region_name="PWWP_NSD1_rpt1"
                     /note="first PWWP domain found in nuclear receptor-binding
                     SET domain-containing protein 1 (NSD1) and similar
                     proteins; cd20161"
                     /db_xref="CDD:438989"
     Site            order(334,337,368)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438989"
     Site            335..338
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438989"
     Site            order(406..408,411..412)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438989"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          487..514
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17487921; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          872..891
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          936..1035
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1067..1093
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1112..1134
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1243..1272
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1294..1344
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1382..1428
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          <1431..1587
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          1480..1534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            1510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88491; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1545..1587
                     /region_name="PHD1_NSD1_2"
                     /note="PHD finger 1 found in nuclear receptor-binding SET
                     domain-containing protein NSD1 and NSD2; cd15648"
                     /db_xref="CDD:277118"
     Site            order(1545,1554..1558,1563,1581)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277118"
     Region          1592..1638
                     /region_name="PHD2_NSD1"
                     /note="PHD finger 2 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15650"
                     /db_xref="CDD:277120"
     Site            order(1592,1602..1606,1612,1633)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277120"
     Region          1639..1692
                     /region_name="PHD3_NSD1"
                     /note="PHD finger 3 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15653"
                     /db_xref="CDD:277123"
     Site            order(1639,1657..1661,1665,1687)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277123"
     Region          1709..1748
                     /region_name="PHD4_NSD1"
                     /note="PHD finger 4 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15656"
                     /db_xref="CDD:277126"
     Site            order(1709,1718..1722,1726,1743)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277126"
     Region          1755..1850
                     /region_name="PWWP_NSD1_rpt2"
                     /note="second PWWP domain found in nuclear
                     receptor-binding SET domain-containing protein 1 (NSD1)
                     and similar proteins; cd20164"
                     /db_xref="CDD:438992"
     Site            order(1767,1770,1798)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438992"
     Site            1768..1771
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438992"
     Region          1901..1939
                     /region_name="AWS"
                     /note="AWS domain; pfam17907"
                     /db_xref="CDD:465559"
     Region          1941..2082
                     /region_name="SET_NSD1"
                     /note="SET domain (including post-SET domain) found in
                     nuclear receptor-binding SET domain-containing protein 1
                     (NSD1) and similar proteins; cd19210"
                     /db_xref="CDD:380987"
     Site            order(1952..1954,1971,1981,1985,1994..2000,2017..2021,
                     2028..2030,2045,2056..2066,2068..2072,2081)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380987"
     Site            order(1952..1954,1994..1997,2017..2021,2058,2065,
                     2069..2072,2081)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380987"
     Site            order(1971,1981,1985,1996..2000,2028..2030,2045,
                     2056..2060)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:380987"
     Site            order(2023,2070,2072,2077)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380987"
     Region          2060..2066
                     /region_name="Inhibits enzyme activity in the absence of
                     bound histone"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2091..2111
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2120..2162
                     /region_name="PHD5_NSD1"
                     /note="PHD finger 5 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15659"
                     /db_xref="CDD:277129"
     Site            order(2120,2129..2133,2139,2157)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277129"
     Region          2161..2210
                     /region_name="C5HCH"
                     /note="NSD Cys-His rich domain; pfam17982"
                     /db_xref="CDD:465605"
     Region          <2208..2574
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          2213..2422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            2369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            2462
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2464..2499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            2471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2553..2575
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2595..2616
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2665..2696
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     CDS             1..2696
                     /gene="NSD1"
                     /gene_synonym="ARA267; KMT3B; SOTOS; SOTOS1; STO"
                     /coded_by="NM_001409303.1:53..8143"
                     /note="isoform b is encoded by transcript variant 6"
                     /db_xref="GeneID:64324"
                     /db_xref="HGNC:HGNC:14234"
                     /db_xref="MIM:606681"
ORIGIN      
        1 mdqtcelprr ncllpfsnpv nldapedkds pfgngqsnfs eplngctmql stvsgtsqna
       61 ygqdspscyi plrrlqdlas minveylngs adgsesfqdp eksdsraqtp ivctslspgg
      121 ptalamkqep scnnspelqv kvtktikngf lhfenftcvd dadvdsemdp eqpvtedesi
      181 eeifeetqtn atcnyetkse ngvkvamgse qdstpesrhg avkspflpla pqtetqknkq
      241 rnevdgsnek aallpapfsl gdtnitieeq lnsinlsfqd dpdsststlg nmlelpgtss
      301 sstsqelpfc qpkkkstplk yevgdliwak fkrrpwwpcr icsdplinth skmkvsnrrp
      361 yrqyyveafg dpserawvag kaivmfegrh qfeelpvlrr rgkqkekgyr hkvpqkilsk
      421 weasvglaeq ydvpkgsknr kcipgsikld seedmpfedc tndpesehdl llngclksla
      481 fdsehsadek ekpcaksrar kssdnpkrts vkkghiqfea hkderrgkip enlglnfisg
      541 disdtqasne lsriansltg sntapgsflf sscgkntakk efetsngdsl lglpegalis
      601 kcsreknkpq rslvcgskvk lcyigagdee krsdsisict tsddgssdld piehssesdn
      661 svleipdafd rtenmlsmqk nekikysrfa atntrvkakq kplisnshtd hlmgctksae
      721 pgtetsqvnl sdlkastlvh kpqsdftnda lspkfnlsss issenslikg gaanqallhs
      781 kskqpkfrsi kckhkenpvm aeppvineec slkccssdtk gsplasisks gkvdglklln
      841 nmhektrdss dietavvkhv lselkelsyr slgedvsdsg tskpskpllf ssassqnhip
      901 iepdykfstl lmmlkdmhds ktkeqrlmta qnlvsyrspg rgdcstnspv gvskvlvsgg
      961 sthnsekkgd gtqnsanpsp sggdsalsge lsaslpglls dkrdlpasgk srsdcvtrrn
     1021 cgrskpsskl rdafsaqmvk ntvnrkalkt erkrklnqlp svtldavlqg drerggslrg
     1081 gaedpskedp lqimghltse dgdhfsdvhf dskvkqsdpg kisekglsfe ngkgpeldsv
     1141 mnsendelng vnqvvpkkrw qrlnqrrtkp rkrmnrfkek ensecafrvl lpsdpvqegr
     1201 defpehrtps asileeplte qnhadcldsa gprlnvcdks sasigdmeke pgipsltpqa
     1261 elpepavrse kkrlrkpskw lleyteeydq ifapkkkqkk vqeqvhkvss rceeesllar
     1321 grssaqnkqv denslistke eppvlereap flegplaqse lggghaelpq ltlsvpvape
     1381 vsprpalese ellvktpgny eskrqrkptk kllesndldp gfmpkkgdlg lskkcyeagh
     1441 lengitesca tsyskdfggg ttkifdkprk rkrqrhaaak mqckkvkndd sskeipgseg
     1501 elmphrtats pketveegve hdpgmpaskk mqgergggaa lkenvcqnce klgelllcea
     1561 qccgafhlec lgltemprgk ficnecrtgi htcfvckqsg edvkrcllpl cgkfyheecv
     1621 qkypptvmqn kgfrcslhic itchaanpan vsaskgrlmr cvrcpvayha ndfclaagsk
     1681 ilasnsiicp nhftprrgcr nhehvnvswc fvcseggsll ccdscpaafh reclnidipe
     1741 gnwycndcka gkkphyreiv wvkvgryrww paeichprav psnidkmrhd vgefpvlffg
     1801 sndylwthqa rvfpymegdv sskdkmgkgv dgtykkalqe aaarfeelka qkelrqlqed
     1861 rkndkkpppy khikvnrpig rvqiftadls eiprcnckat denpcgidse cinrmllyec
     1921 hptvcpaggr cqnqcfskrq ypeveifrtl qrgwglrtkt dikkgefvne yvgelideee
     1981 crariryaqe hditnfymlt ldkdriidag pkgnyarfmn hccqpncetq kwsvngdtrv
     2041 glfalsdika gteltfnynl eclgngktvc kcgapncsgf lgvrpknqpi ateekskkfk
     2101 kkqqgkrrtq geitkerede cfscgdagql vsckkpgcpk vyhadclnlt krpagkwecp
     2161 whqcdicgke aasfcemcps sfckqhregm lfiskldgrl sctehdpcgp nplepgeire
     2221 yvpppvplpp gpsthlaeqs tgmaaqapkm sdkppadtnq mlslskkala gtcqrpllpe
     2281 rplertdsrp qpldkvrdla gsgtksqslv ssqrpldrpp avagprpqls dkpspvtsps
     2341 sspsvrsqpl erplgtadpr ldksigaasp rpqslektsv ptglrlpppd rllitsspkp
     2401 qtsdrptdkp haslsqrlpp pekvlsavvq tlvakekalr pvdqntqskn raalvmdlid
     2461 ltprqkeraa sphqvtpqad ekmpvlesss wpaskglghm pravekgcvs dplqtsgkaa
     2521 apsedpwqav ksltqarlls qppakaflye pttqasgras agaeqtpgpl sqspglvkqa
     2581 kqmvggqqlp alaaksgqsf rslgkapasl pteekklvtt eqspwalgka ssraglwpiv
     2641 agqtlaqscw sagstqtlaq tcwslgrgqd pkpeqntlpa lnqapsshkc aeseqk
//
LOCUS       NP_001364065            1175 aa            linear   PRI 21-NOV-2025
DEFINITION  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4
            isoform b [Homo sapiens].
ACCESSION   NP_001364065 XP_024307674
VERSION     NP_001364065.1
DBSOURCE    REFSEQ: accession NM_001377136.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1175)
  AUTHORS   Aparicio-Bautista,D.I., Jimenez-Ortega,R.F., Becerra-Cervera,A.,
            Aquino-Galvez,A., de Leon-Suarez,V.P., Casas-Avila,L., Salmeron,J.,
            Hidalgo-Bravo,A., Rivera-Paredez,B. and Velazquez-Cruz,R.
  TITLE     Interaction between MARK3 (rs11623869), PLCB4 (rs6086746) and
            GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women
  JOURNAL   Front Endocrinol (Lausanne) 15, 1392063 (2024)
   PUBMED   38715801
  REMARK    GeneRIF: Interaction between MARK3 (rs11623869), PLCB4 (rs6086746)
            and GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1175)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1175)
  AUTHORS   Kanai,S.M., Heffner,C., Cox,T.C., Cunningham,M.L., Perez,F.A.,
            Bauer,A.M., Reigan,P., Carter,C., Murray,S.A. and Clouthier,D.E.
  TITLE     Auriculocondylar syndrome 2 results from the dominant-negative
            action of PLCB4 variants
  JOURNAL   Dis Model Mech 15 (4) (2022)
   PUBMED   35284927
  REMARK    GeneRIF: Auriculocondylar syndrome 2 results from the
            dominant-negative action of PLCB4 variants.
REFERENCE   4  (residues 1 to 1175)
  AUTHORS   Phan,H.T.N., Kim,N.H., Wei,W., Tall,G.G. and Smrcka,A.V.
  TITLE     Uveal melanoma-associated mutations in PLCbeta4 are constitutively
            activating and promote melanocyte proliferation and tumorigenesis
  JOURNAL   Sci Signal 14 (713), eabj4243 (2021)
   PUBMED   34905385
  REMARK    GeneRIF: Uveal melanoma-associated mutations in PLCbeta4 are
            constitutively activating and promote melanocyte proliferation and
            tumorigenesis.
REFERENCE   5  (residues 1 to 1175)
  AUTHORS   Tsai,D.J., Fang,W.H., Wu,L.W., Tai,M.C., Kao,C.C., Huang,S.M.,
            Chen,W.T., Hsiao,P.J., Chiu,C.C., Su,W., Wu,C.C. and Su,S.L.
  TITLE     The Polymorphism at PLCB4 Promoter (rs6086746) Changes the Binding
            Affinity of RUNX2 and Affects Osteoporosis Susceptibility: An
            Analysis of Bioinformatics-Based Case-Control Study and Functional
            Validation
  JOURNAL   Front Endocrinol (Lausanne) 12, 730686 (2021)
   PUBMED   34899595
  REMARK    GeneRIF: The Polymorphism at PLCB4 Promoter (rs6086746) Changes the
            Binding Affinity of RUNX2 and Affects Osteoporosis Susceptibility:
            An Analysis of Bioinformatics-Based Case-Control Study and
            Functional Validation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1175)
  AUTHORS   Lyu,M.S., Park,D.J., Rhee,S.G. and Kozak,C.A.
  TITLE     Genetic mapping of the human and mouse phospholipase C genes
  JOURNAL   Mamm Genome 7 (7), 501-504 (1996)
   PUBMED   8672127
REFERENCE   7  (residues 1 to 1175)
  AUTHORS   Alvarez,R.A., Ghalayini,A.J., Xu,P., Hardcastle,A.,
            Bhattacharya,S., Rao,P.N., Pettenati,M.J., Anderson,R.E. and
            Baehr,W.
  TITLE     cDNA sequence and gene locus of the human retinal
            phosphoinositide-specific phospholipase-C beta 4 (PLCB4)
  JOURNAL   Genomics 29 (1), 53-61 (1995)
   PUBMED   8530101
REFERENCE   8  (residues 1 to 1175)
  AUTHORS   Zauli,G., Previati,M., Caramelli,E., Bassini,A., Falcieri,E.,
            Gibellini,D., Bertolaso,L., Bosco,D., Robuffo,I. and Capitani,S.
  TITLE     Exogenous human immunodeficiency virus type-1 Tat protein
            selectively stimulates a phosphatidylinositol-specific
            phospholipase C nuclear pathway in the Jurkat T cell line
  JOURNAL   Eur J Immunol 25 (9), 2695-2700 (1995)
   PUBMED   7589147
REFERENCE   9  (residues 1 to 1175)
  AUTHORS   Berstein,G., Blank,J.L., Jhon,D.Y., Exton,J.H., Rhee,S.G. and
            Ross,E.M.
  TITLE     Phospholipase C-beta 1 is a GTPase-activating protein for Gq/11,
            its physiologic regulator
  JOURNAL   Cell 70 (3), 411-418 (1992)
   PUBMED   1322796
REFERENCE   10 (residues 1 to 1175)
  AUTHORS   Banno,Y., Yada,Y. and Nozawa,Y.
  TITLE     Purification and characterization of membrane-bound phospholipase C
            specific for phosphoinositides from human platelets
  JOURNAL   J Biol Chem 263 (23), 11459-11465 (1988)
   PUBMED   2841328
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121898.23, AL121909.10,
            AL023805.2 and AL031652.4.
            
            On Dec 17, 2019 this sequence version replaced XP_024307674.1.
            
            Summary: The protein encoded by this gene catalyzes the formation
            of inositol 1,4,5-trisphosphate and diacylglycerol from
            phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium
            as a cofactor and plays an important role in the intracellular
            transduction of many extracellular signals in the retina. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Feb 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.100582.1,
                                           SRR1803616.18813.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1175
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.3-p12.2"
     Protein         1..1175
                     /product="1-phosphatidylinositol 4,5-bisphosphate
                     phosphodiesterase beta-4 isoform b"
                     /EC_number="3.1.4.11"
                     /note="PLC-beta-4; triphosphoinositide phosphodiesterase;
                     phosphoinositidase C; monophosphatidylinositol
                     phosphodiesterase;
                     1-phosphatidyl-D-myo-inositol-4,5-bisphosphate;
                     inositoltrisphosphohydrolase; dJ1119D9.2 (Phopholipase C,
                     beta 4 (1-Phosphatidylinositol-4,5-Bisphosphate
                     Phosphodiesterase Beta 4)); phosphoinositide phospholipase
                     C-beta-4"
                     /calculated_mol_wt=134333
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.4;
                     propagated from UniProtKB/Swiss-Prot (Q15147.3)"
     Region          17..143
                     /region_name="PH_PLC_beta"
                     /note="Phospholipase C-beta (PLC-beta) pleckstrin homology
                     (PH) domain; cd13361"
                     /db_xref="CDD:270167"
     Site            order(22,24,36,53,117)
                     /site_type="other"
                     /note="Rac1 binding site [polypeptide binding]"
                     /db_xref="CDD:270167"
     Site            order(25,27,33,35,37,52..53)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270167"
     Region          148..300
                     /region_name="EFh_PI-PLCbeta4"
                     /note="EF-hand motif found in phosphoinositide
                     phospholipase C beta 4 (PI-PLC-beta4); cd16211"
                     /db_xref="CDD:320041"
     Region          148..177
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320041"
     Region          183..212
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320041"
     Region          221..250
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320041"
     Region          267..300
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320041"
     Region          312..668
                     /region_name="PI-PLCc_beta"
                     /note="Catalytic domain of metazoan
                     phosphoinositide-specific phospholipase C-beta; cd08591"
                     /db_xref="CDD:176533"
     Site            order(328..329,358,360,375,409,461,463,594,621,623)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176533"
     Site            order(328,375)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176533"
     Site            order(329,358,360,409)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:176533"
     Region          482..511
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15147.3)"
     Region          702..818
                     /region_name="C2_PLC_like"
                     /note="C2 domain present in Phosphoinositide-specific
                     phospholipases C (PLC); cd00275"
                     /db_xref="CDD:175974"
     Site            order(719,745,776,778,780,782)
                     /site_type="other"
                     /note="Ca2+ binding pocket [ion binding]"
                     /db_xref="CDD:175974"
     Region          <839..>1170
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          863..895
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15147.3)"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15147.3)"
     Region          913..955
                     /region_name="DUF1154"
                     /note="Protein of unknown function (DUF1154); pfam06631"
                     /db_xref="CDD:461969"
     Region          1082..1110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15147.3)"
     CDS             1..1175
                     /gene="PLCB4"
                     /gene_synonym="ARCND2; ARCND2A; ARCND2B; PI-PLC"
                     /coded_by="NM_001377136.1:199..3726"
                     /note="isoform b is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS13105.1"
                     /db_xref="GeneID:5332"
                     /db_xref="HGNC:HGNC:9059"
                     /db_xref="MIM:600810"
ORIGIN      
        1 makpyefnwq kevpsflqeg avfdryeees fvfepnclfk vdefgffltw rsegkegqvl
       61 ecslinsirs gaipkdpkil aaleavgkse ndlegrivcv csgtdlvnis ftymvaenpe
      121 vtkqwveglr siihnfrann vspmtclkkh wmklafmtnt ngkipvrsit rtfasgktek
      181 vifqalkelg lpsgkndeie ptafsyekfy eltqkicprt diedlfkkin gdktdyltvd
      241 qlvsflnehq rdprlneilf pfydakramq iiemyepded lkkkglissd gfcrylmsde
      301 napvfldrle lyqemdhpla hyfissshnt yltgrqfggk ssvemyrqvl lagcrcveld
      361 cwdgkgedqe piithgkamc tdilfkdviq aiketafvts eypvilsfen hcskyqqykm
      421 skycedlfgd lllkqalesh plepgralps pndlkrkili knkrlkpeve kkqlealrsm
      481 meagesaspa nileddneee iesadqeeea hpefkfgnel saddlghkea vansvkkglv
      541 tvedeqawma sykyvgattn ihpylstmin yaqpvkfqgf hvaeernihy nmssfnesvg
      601 lgylkthaie fvnynkrqms riypkggrvd ssnympqifw nagcqmvsln yqtpdlamql
      661 nqgkfeyngs cgyllkpdfm rrpdrtfdpf setpvdgvia atcsvqvisg qflsdkkigt
      721 yvevdmyglp tdtirkefrt rmvmnnglnp vyneesfvfr kvilpdlavl riavyddnnk
      781 ligqrilpld glqagyrhis lrnegnkpls lptifcnivl ktyvpdgfgd ivdalsdpkk
      841 flsitekrad qmramgiets diadvpsdts kndkkgkant akanvtpqss selrptttaa
      901 lasgveakkg ielipqvrie dlkqmkaylk hlkkqqkeln slkkkhakeh stmqklhctq
      961 vdkivaqydk eksthekile kamkkkggsn clemkketei kiqtltsdhk skvkeivaqh
     1021 tkewsemint hsaeeqeird lhlsqqcell kkllinaheq qtqqlklshd reskemrahq
     1081 akismenska isqdksiknk aererrvrel nssntkkfle erkrlamkqs kemdqlkkvq
     1141 lehleflekq neqakemqqm vkleaemdrr patvv
//
LOCUS       NP_001400127             661 aa            linear   PRI 21-NOV-2025
DEFINITION  cyclin-T1 isoform c [Homo sapiens].
ACCESSION   NP_001400127
VERSION     NP_001400127.1
DBSOURCE    REFSEQ: accession NM_001413198.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 661)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 661)
  AUTHORS   Chen,W., Chu,J., Miao,Y., Jiang,W., Wang,F., Zhang,N., Jin,J. and
            Cai,Y.
  TITLE     MOF-mediated acetylation of CDK9 promotes global transcription by
            modulating P-TEFb complex formation
  JOURNAL   FEBS J 291 (21), 4796-4812 (2024)
   PUBMED   39250546
REFERENCE   3  (residues 1 to 661)
  AUTHORS   Gao,G., Wu,X., Zhou,J., He,M., He,J.J. and Guo,D.
  TITLE     Inhibition of HIV-1 transcription and replication by a newly
            identified cyclin T1 splice variant
  JOURNAL   J Biol Chem 288 (20), 14297-14309 (2013)
   PUBMED   23569210
  REMARK    GeneRIF: CYCT1b is a newly identified cyclin T1 splice variant
            whose expression leads to direct inhibition of TAT-transactivated
            transcription of the HIV-1 LTR promoter
REFERENCE   4  (residues 1 to 661)
  AUTHORS   Urano,E., Miyauchi,K., Ichikawa,R., Futahashi,Y. and Komano,J.
  TITLE     Regulation of cyclin T1 expression and function by an alternative
            splice variant that skips exon 7 and contains a premature
            termination codon
  JOURNAL   Gene 505 (1), 1-8 (2012)
   PUBMED   22692005
REFERENCE   5  (residues 1 to 661)
  AUTHORS   De Luca,A., De Falco,M., Baldi,A. and Paggi,M.G.
  TITLE     Cyclin T: three forms for different roles in physiological and
            pathological functions
  JOURNAL   J Cell Physiol 194 (2), 101-107 (2003)
   PUBMED   12494448
  REMARK    Review article
REFERENCE   6  (residues 1 to 661)
  AUTHORS   Martin-Serrano,J., Li,K. and Bieniasz,P.D.
  TITLE     Cyclin T1 expression is mediated by a complex and constitutively
            active promoter and does not limit human immunodeficiency virus
            type 1 Tat function in unstimulated primary lymphocytes
  JOURNAL   J Virol 76 (1), 208-219 (2002)
   PUBMED   11739686
REFERENCE   7  (residues 1 to 661)
  AUTHORS   Liu,H. and Rice,A.P.
  TITLE     Isolation and characterization of the human cyclin T1 promoter
  JOURNAL   Gene 252 (1-2), 39-49 (2000)
   PUBMED   10903436
REFERENCE   8  (residues 1 to 661)
  AUTHORS   Wei,P., Garber,M.E., Fang,S.M., Fischer,W.H. and Jones,K.A.
  TITLE     A novel CDK9-associated C-type cyclin interacts directly with HIV-1
            Tat and mediates its high-affinity, loop-specific binding to TAR
            RNA
  JOURNAL   Cell 92 (4), 451-462 (1998)
   PUBMED   9491887
REFERENCE   9  (residues 1 to 661)
  AUTHORS   Yang,X., Herrmann,C.H. and Rice,A.P.
  TITLE     The human immunodeficiency virus Tat proteins specifically
            associate with TAK in vivo and require the carboxyl-terminal domain
            of RNA polymerase II for function
  JOURNAL   J Virol 70 (7), 4576-4584 (1996)
   PUBMED   8676484
REFERENCE   10 (residues 1 to 661)
  AUTHORS   Herrmann,C.H. and Rice,A.P.
  TITLE     Lentivirus Tat proteins specifically associate with a cellular
            protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal
            domain of the large subunit of RNA polymerase II: candidate for a
            Tat cofactor
  JOURNAL   J Virol 69 (3), 1612-1620 (1995)
   PUBMED   7853496
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079951.35.
            
            Summary: This gene encodes a member of the highly conserved cyclin
            C subfamily. The encoded protein tightly associates with
            cyclin-dependent kinase 9, and is a major subunit of positive
            transcription elongation factor b (p-TEFb). In humans, there are
            multiple forms of positive transcription elongation factor b, which
            may include one of several different cyclins along with
            cyclin-dependent kinase 9. The complex containing the encoded
            cyclin and cyclin-dependent kinase 9 acts as a cofactor of human
            immunodeficiency virus type 1 (HIV-1) Tat protein, and is both
            necessary and sufficient for full activation of viral
            transcription. This cyclin and its kinase partner are also involved
            in triggering transcript elongation through phosphorylation of the
            carboxy-terminal domain of the largest RNA polymerase II subunit.
            Overexpression of this gene is implicated in tumor growth.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Apr 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3641955.1,
                                           SRR14038195.581176.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.11-q13.12"
     Protein         1..661
                     /product="cyclin-T1 isoform c"
                     /note="human immunodeficiency virus type 1 (HIV-1)
                     expression (elevated) 1; cyclin C-related protein;
                     CDK9-associated C-type protein; MLLT10/CCNT1 fusion"
                     /calculated_mol_wt=72852
     Region          <1..82
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cl40454"
                     /db_xref="CDD:477360"
     Region          86..194
                     /region_name="CYCLIN_CCNT1_rpt2"
                     /note="second cyclin box found in cyclin-T1 (CCNT1);
                     cd20597"
                     /db_xref="CDD:410300"
     Site            order(90,93,106..107,110..111,114..115,118..119,183..185)
                     /site_type="other"
                     /note="HIV-1 Tat binding site [polypeptide binding]"
                     /db_xref="CDD:410300"
     Site            order(98..100,104..105,107..108,137,141..146,148,150..152,
                     156,159,170,173..174,177..178,180..181,185,187..188,191)
                     /site_type="other"
                     /note="AF4 family member binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410300"
     CDS             1..661
                     /gene="CCNT1"
                     /gene_synonym="CCNT; CYCT1; HIVE1"
                     /coded_by="NM_001413198.1:458..2443"
                     /note="isoform c is encoded by transcript variant c"
                     /db_xref="GeneID:904"
                     /db_xref="HGNC:HGNC:1599"
                     /db_xref="MIM:143055"
ORIGIN      
        1 mhrfymiqsf tqfpgnsvap aalflaakve eqpkklehvi kvahtclhpq eslpdtrsea
       61 ylqqvqdlvi lesiilqtlg feltidhpht hvvkctqlvr askdlaqtsy fmatnslhlt
      121 tfslqytppv vacvcihlac kwsnweipvs tdgkhwweyv datvtlelld eltheflqil
      181 ektpnrlkri wnwraceaak ktkaddrgtd ektseqtiln misqsssdtt iaglmsmsts
      241 ttsavpslpv seesssnlts vemlpgkrwl ssqpsfklep tqghrtsenl altgvdhslp
      301 qdgsnafisq kqnsksvpsa kvslkeyrak haeelaaqkr qlenmeanvk sqyayaaqnl
      361 lshhdshssv ilkmpiegse nperpfleka dktalkmrip vaggdkaass kpeeikmrik
      421 vhaaadkhns vedsvtksre hkekhkthps nhhhhhnhhs hkhshsqlpv gtgnkrpgdp
      481 khssqtsnla hktyslsssf ssssstrkrg pseetggavf dhpakiakst kssslnfsfp
      541 slptmgqmpg hssdtsglsf sqpscktrvp hskldkgptg anghnttqti dyqdtvnmlh
      601 sllsaqgvqp tqptafefvr pysdylnprs ggissrsgnt dkprppplps epppplpplp
      661 k
//
LOCUS       NP_001400682             781 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform n [Homo sapiens].
ACCESSION   NP_001400682
VERSION     NP_001400682.1
DBSOURCE    REFSEQ: accession NM_001413753.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 781)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 781)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 781)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 781)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 781)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 781)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 781)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 781)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 781)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 781)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3717811.1,
                                           SRR18074967.2995981.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..781
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..781
                     /product="polyhomeotic-like protein 1 isoform n"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=82869
     Region          605..712
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          712..780
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(730..731,765..766,769..770,773)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(741..745,747..748,751..752,756,761)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..781
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413753.1:368..2713"
                     /note="isoform n is encoded by transcript variant 17"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq aspqlgnllq vnrtlgrnvp
      121 lasqlilmpn gavaavqqev psaqspgvha dadqvqnlav rnqqasaqgp qmqgstqkai
      181 ppgaspvssl sqassqalav aqassgatnq slnlsqaggg sgnsipgsmg pggggqahgg
      241 lgqlpssgmg ggscprkgtg vvqplpaaqt vtvsqgsqte aesaaakkae adgsgqqnvg
      301 mnltrtatpa psqtlissat ytqiqphsli qqqqqihlqq kqvviqqqia ihhqqqfqhr
      361 qsqllhtath lqlaqqqqqq qqqqqqqqqp qattltapqp pqvpptqqgk pqtlavkrka
      421 dseeerddvs tlgsmlpaka spvaespkvm deksslgeka esvanvnant psselvaltp
      481 apsvppptla mvsrqmgdsk ppqaivkpqi lthiiegfvi qegaepfpvg csqllkesek
      541 plqtglptgl tenqsggplg vdspsaeldk kanllkceyc gkyapaeqfr gskrfcsmtc
      601 akrynvscsh qfrlkrkkmk efqeanyarv rrrgprrsss diarakiqgk chrgqedssr
      661 gsdnssydea lsptspgpls vraghgerdl gnpntapptp elhginpvfl ssnpsrwsve
      721 evyefiaslq gcqeiaeefr sqeidgqall llkeehlmsa mniklgpalk icakinvlke
      781 t
//
LOCUS       NP_001394381            2833 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform p [Homo sapiens].
ACCESSION   NP_001394381
VERSION     NP_001394381.1
DBSOURCE    REFSEQ: accession NM_001407452.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2833)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2833)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2833)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2833)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2833)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2833)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2833)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2833)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2833)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2833)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.3787309.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2833
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2833
                     /product="adenomatous polyposis coli protein isoform p"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=309984
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          312..364
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          365..438
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          462..498
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          495..537
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          502..543
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          506..543
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          538..581
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          553..585
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(576,580,584,623,627,631,668,672,676)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          582..628
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          593..634
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          629..673
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          639..679
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          643..677
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          674..715
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          681..721
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          685..721
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          716..757
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          722..1009
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Site            734
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            738
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            770
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          818..868
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            898
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          913..933
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          948..977
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          950..1327
                     /region_name="Responsible for down-regulation through a
                     process mediated by direct ubiquitination"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            977
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1010..1159
                     /region_name="Interaction with catenins.
                     /evidence=ECO:0000269|PubMed:8259519"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1026..1125
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Site            1028
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1032
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1089..1159
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1180..1234
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1247..>1264
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1273..1358
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1281..1691
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1301..1366
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1393..1465
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1428
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1516..1559
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1573..1601
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1627..1650
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1652..1705
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1654..1707
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1706..1727
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1719..1826
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1736..1829
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Site            1764
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1851
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1853
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1854
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1856..1883
                     /region_name="Highly charged"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1863..1937
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1871..1940
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1955..2001
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1961
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1963
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2023..2042
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2025..2049
                     /region_name="Interaction with AXIN1.
                     /evidence=ECO:0000269|PubMed:10811618"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2033..2062
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2078
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2083
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2137..2625
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2141
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2157..2664
                     /region_name="Basic region.
                     /evidence=ECO:0000269|PubMed:17293347"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2213..2558
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Site            2250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2465..2833
                     /region_name="Interaction with DLG1.
                     /evidence=ECO:0000269|PubMed:8638125"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2559
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2657..2704
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2660..2833
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     Site            2661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2664..2833
                     /region_name="Interaction with MAPRE1.
                     /evidence=ECO:0000269|PubMed:17293347"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2669
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2700
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2714
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2719..2833
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2779
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2793..2796
                     /region_name="Microtubule tip localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2831..2833
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     CDS             1..2833
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407452.1:404..8905"
                     /note="isoform p is encoded by transcript variant 22"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrssqn khetgshdae rqnegqgvge
      241 inmatsgngq gsttrmdhet asvlssssth saprrltshl gtkvemvysl lsmlgthdkd
      301 dmsrtllams ssqdscismr qsgclplliq llhgndkdsv llgnsrgske ararasaalh
      361 niihsqpddk rgrreirvlh lleqirayce tcwewqeahe pgmdqdknpm papvehqicp
      421 avcvlmklsf deehrhamne lgrkatrgis sqelgqglsg glqaiaellq vdcemygltn
      481 dhysitlrry agmaltnltf gdvankatlc smkgcmralv aqlksesedl qqviasvlrn
      541 lswradvnsk ktlrevgsvk almecalevk kestlksvls alwnlsahct enkadicavd
      601 galaflvgtl tyrsqtntla iiesgggilr nvssliatne dhrqilrenn clqtllqhlk
      661 shsltivsna cgtlwnlsar npkdqealwd mgavsmlknl ihskhkmiam gsaaalrnlm
      721 anrpakykda nimspgsslp slhvrkqkal eaeldaqhls etfdnidnls pkashrskqr
      781 hkqslygdyv fdtnrhddnr sdnfntgnmt vlspylnttv lpsssssrgs ldssrsekdr
      841 slerergigl gnyhpatenp gtsskrglqi sttaaqiakv meevsaihts qedrssgstt
      901 elhcvtdern alrrssaaht hsntynftks ensnrtcsmp yakleykrss ndslnsvsss
      961 dgygkrgqmk psiesysedd eskfcsygqy padlahkihs anhmddndge ldtpinyslk
     1021 ysdeqlnsgr qspsqnerwa rpkhiiedei kqseqrqsrn qsttypvyte stddkhlkfq
     1081 phfgqqecvs pyrsrgangs etnrvgsnhg inqnvsqslc qeddyeddkp tnyserysee
     1141 eqheeeerpt nysikyneek rhvdqpidys lkyatdipss qkqsfsfsks ssgqsskteh
     1201 mssssentst pssnakrqnq lhpssaqsrs gqpqkaatck vssinqetiq tycvedtpic
     1261 fsrcsslssl ssaedeigcn qttqeadsan tlqiaeikek igtrsaedpv sevpavsqhp
     1321 rtkssrlqgs slssesarhk avefssgaks psksgaqtpk sppehyvqet plmfsrctsv
     1381 ssldsfesrs iassvqsepc sgmvsgiisp sdlpdspgqt mppsrsktpp pppqtaqtkr
     1441 evpknkapta ekresgpkqa avnaavqrvq vlpdadtllh fatestpdgf scssslsals
     1501 ldepfiqkdv elrimppvqe ndngnetese qpkesnenqe keaektidse kdllddsddd
     1561 dieileecii samptkssrk akkpaqtask lpppvarkps qlpvykllps qnrlqpqkhv
     1621 sftpgddmpr vycvegtpin fstatslsdl tiesppnela agegvrggaq sgefekrdti
     1681 ptegrstdea qggktssvti pelddnkaee gdilaecins ampkgkshkp frvkkimdqv
     1741 qqasasssap nknqldgkkk kptspvkpip qnteyrtrvr knadsknnln aervfsdnkd
     1801 skkqnlknns kvfndklpnn edrvrgsfaf dsphhytpie gtpycfsrnd slssldfddd
     1861 dvdlsrekae lrkakenkes eakvtshtel tsnqqsankt qaiakqpinr gqpkpilqkq
     1921 stfpqsskdi pdrgaatdek lqnfaientp vcfshnssls slsdidqenn nkenepiket
     1981 eppdsqgeps kpqasgyapk sfhvedtpvc fsrnsslssl sidseddllq ecissampkk
     2041 kkpsrlkgdn ekhsprnmgg ilgedltldl kdiqrpdseh glspdsenfd wkaiqegans
     2101 ivsslhqaaa aaclsrqass dsdsilslks gislgspfhl tpdqeekpft snkgprilkp
     2161 gekstletkk ieseskgikg gkkvykslit gkvrsnseis gqmkqplqan mpsisrgrtm
     2221 ihipgvrnss sstspvskkg pplktpasks psegqtatts prgakpsvks elspvarqts
     2281 qiggsskaps rsgsrdstps rpaqqplsrp iqspgrnsis pgrngisppn klsqlprtss
     2341 pstastkssg sgkmsytspg rqmsqqnltk qtglsknass iprsesaskg lnqmnngnga
     2401 nkkvelsrms stkssgsesd rserpvlvrq stfikeapsp tlrrkleesa sfeslspssr
     2461 pasptrsqaq tpvlspslpd mslsthssvq aggwrklppn lsptieyndg rpakrhdiar
     2521 shsespsrlp inrsgtwkre hskhssslpr vstwrrtgss ssilsasses sekaksedek
     2581 hvnsisgtkq skenqvsakg twrkikenef sptnstsqtv ssgatngaes ktliyqmapa
     2641 vsktedvwvr iedcpinnpr sgrsptgntp pvidsvseka npnikdskdn qakqnvgngs
     2701 vpmrtvglen rlnsfiqvda pdqkgteikp gqnnpvpvse tnessivert pfsssssskh
     2761 sspsgtvaar vtpfnynpsp rkssadstsa rpsqiptpvn nntkkrdskt dstessgtqs
     2821 pkrhsgsylv tsv
//
LOCUS       NP_001392808            1041 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 7 [Homo sapiens].
ACCESSION   NP_001392808 XP_016879977
VERSION     NP_001392808.1
DBSOURCE    REFSEQ: accession NM_001405879.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1041)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1041)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1041)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1041)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1041)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1041)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1041)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            On May 5, 2022 this sequence version replaced XP_016879977.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.13239.1,
                                           SRR14038194.846013.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1041
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 7"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=113459
     Site            104
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          145..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          225..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          399..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          821..941
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..1041
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405879.1:251..3376"
                     /note="isoform 7 is encoded by transcript variant 20"
                     /db_xref="CCDS:CCDS92348.1"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankgli
      481 vlgevpppeh ttdlflplss evktdhgtdk liesvsqple nhgapiighi seslstkscg
      541 alrpvngvin tlqpvladhi pgdssdaeeq lhkkqrlnlv ssssdgtcva artrpvlsck
      601 krrlvrpnsi vplskkvhrn stirpgcdvn pscalcgsgs intmppeihy eapllerlsq
      661 ldscvhpvla fpddvptslh fqsmlksqwq nkpfdkikpp kklslkhrap mpgslpdsar
      721 kdrhklvssf lttamlkhht dmssssylaa thhpphsplv rqlstssdsp apassssqvt
      781 astsqpvrrr rgessfdinn ivipmsvaat trveklqyke iltpswrevd lqslkgspde
      841 eneeiedlsd aafaalhakc eemerarwlw ttsvppqrrg srsyrssdgr ttpqlgsanp
      901 stpqpaspdv ssshslseys hgqsprspis pelhsapltp vardtprhla sedtrcstpe
      961 lgldeqsvqp werrtfplah spqaecedql daqeraarct rrtsgsktgr eteaaptspp
     1021 ivplksrhlv aaataqrpth r
//
LOCUS       NP_001428217            1534 aa            linear   PRI 21-NOV-2025
DEFINITION  dynamin-binding protein isoform d [Homo sapiens].
ACCESSION   NP_001428217
VERSION     NP_001428217.1
DBSOURCE    REFSEQ: accession NM_001441288.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1534)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1534)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1534)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1534)
  AUTHORS   Ouyang,C., Mu,J., Lu,Q., Li,J., Zhu,H., Wang,Q., Zou,M.H. and
            Xie,Z.
  TITLE     Autophagic degradation of KAT2A/GCN5 promotes directional migration
            of vascular smooth muscle cells by reducing TUBA/alpha-tubulin
            acetylation
  JOURNAL   Autophagy 16 (10), 1753-1770 (2020)
   PUBMED   31878840
  REMARK    GeneRIF: Autophagic degradation of KAT2A/GCN5 promotes directional
            migration of vascular smooth muscle cells by reducing
            TUBA/alpha-tubulin acetylation.
REFERENCE   5  (residues 1 to 1534)
  AUTHORS   Ansar,M., Chung,H.L., Taylor,R.L., Nazir,A., Imtiaz,S.,
            Sarwar,M.T., Manousopoulou,A., Makrythanasis,P., Saeed,S.,
            Falconnet,E., Guipponi,M., Pournaras,C.J., Ansari,M.A., Ranza,E.,
            Santoni,F.A., Ahmed,J., Shah,I., Gul,K., Black,G.C., Bellen,H.J.
            and Antonarakis,S.E.
  TITLE     Bi-allelic Loss-of-Function Variants in DNMBP Cause Infantile
            Cataracts
  JOURNAL   Am J Hum Genet 103 (4), 568-578 (2018)
   PUBMED   30290152
  REMARK    GeneRIF: DNMBP loss-of-function variants cause infantile-onset
            cataracts in humans.
REFERENCE   6  (residues 1 to 1534)
  AUTHORS   Minster,R.L., DeKosky,S.T. and Kamboh,M.I.
  TITLE     No association of dynamin binding protein (DNMBP) gene SNPs and
            Alzheimer's disease
  JOURNAL   Neurobiol Aging 29 (10), 1602-1604 (2008)
   PUBMED   17442457
  REMARK    GeneRIF: We observed no association of statistical significance in
            either the total sample or the APOE*4 non-carriers for any of the
            SNPs of Dynamin Binding Protein.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1534)
  AUTHORS   Otani,T., Ichii,T., Aono,S. and Takeichi,M.
  TITLE     Cdc42 GEF Tuba regulates the junctional configuration of simple
            epithelial cells
  JOURNAL   J Cell Biol 175 (1), 135-146 (2006)
   PUBMED   17015620
  REMARK    GeneRIF: Tuba controls the shaping of cell junctions through the
            local activation of Cdc42 and its effectors.
REFERENCE   8  (residues 1 to 1534)
  AUTHORS   Kuwano,R., Miyashita,A., Arai,H., Asada,T., Imagawa,M., Shoji,M.,
            Higuchi,S., Urakami,K., Kakita,A., Takahashi,H., Tsukie,T.,
            Toyabe,S., Akazawa,K., Kanazawa,I. and Ihara,Y.
  CONSRTM   Japanese Genetic Study Consortium for Alzeheimer's Disease
  TITLE     Dynamin-binding protein gene on chromosome 10q is associated with
            late-onset Alzheimer's disease
  JOURNAL   Hum Mol Genet 15 (13), 2170-2182 (2006)
   PUBMED   16740596
  REMARK    GeneRIF: Results confirmed DNMBP may be one of the susceptibility
            genes for Alzheimer's disease.
            GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   9  (residues 1 to 1534)
  AUTHORS   Cestra,G., Kwiatkowski,A., Salazar,M., Gertler,F. and De Camilli,P.
  TITLE     Tuba, a GEF for CDC42, links dynamin to actin regulatory proteins
  JOURNAL   Methods Enzymol 404, 537-545 (2005)
   PUBMED   16413298
REFERENCE   10 (residues 1 to 1534)
  AUTHORS   Salazar,M.A., Kwiatkowski,A.V., Pellegrini,L., Cestra,G.,
            Butler,M.H., Rossman,K.L., Serna,D.M., Sondek,J., Gertler,F.B. and
            De Camilli,P.
  TITLE     Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl
            homology domains, links dynamin to regulation of the actin
            cytoskeleton
  JOURNAL   J Biol Chem 278 (49), 49031-49043 (2003)
   PUBMED   14506234
  REMARK    GeneRIF: functions to bring together dynamin with actin regulatory
            proteins
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL441886.18, AL627434.4 and
            AL392107.17.
            
            Summary: This gene encodes a protein belonging to the guanine
            nucleotide exchange factor family, and which regulates the
            configuration of cell junctions. It contains multiple binding sites
            for dynamin and thus links dynamin to actin regulatory proteins.
            Polymorphisms in this gene have been linked to Alzheimer's disease
            in some populations, though there are conflicting reports of such
            linkages in other populations. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2670189.1,
                                           SRR14038196.31484.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1534
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.2"
     Protein         1..1534
                     /product="dynamin-binding protein isoform d"
                     /note="scaffold protein TUBA"
                     /calculated_mol_wt=172131
     Region          6..56
                     /region_name="SH3_DNMBP_N1"
                     /note="First N-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11794"
                     /db_xref="CDD:212728"
     Site            order(11,13,16,20,38..39,52,54..55)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212728"
     Region          70..123
                     /region_name="SH3_DNMBP_N2"
                     /note="Second N-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11795"
                     /db_xref="CDD:212729"
     Site            order(75,77,80,84,102..103,117,119..120)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212729"
     Region          149..199
                     /region_name="SH3_DNMBP_N3"
                     /note="Third N-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11796"
                     /db_xref="CDD:212730"
     Site            order(154,156,159,163,181..182,195,197..198)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212730"
     Region          247..296
                     /region_name="SH3_DNMBP_N4"
                     /note="Fourth N-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11797"
                     /db_xref="CDD:212731"
     Site            order(252,254,257,261,279..280,293,295..296)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212731"
     Region          785..965
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(791,795,884,916..917,920..921,923..924,927..928,
                     931..932,935,961,965)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          1017..1165
                     /region_name="BAR_DNMBP"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin
                     Binding Protein; cd07589"
                     /db_xref="CDD:153273"
     Region          1246..1302
                     /region_name="SH3_DNMBP_C1"
                     /note="First C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11798"
                     /db_xref="CDD:212732"
     Site            order(1251,1253,1256,1260,1282..1283,1296,1298..1299)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212732"
     Region          1474..1530
                     /region_name="SH3_DNMBP_C2"
                     /note="Second C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba, and similar domains;
                     cd12141"
                     /db_xref="CDD:213017"
     Site            order(1479,1481,1484,1488,1510..1511,1524,1526..1527)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213017"
     CDS             1..1534
                     /gene="DNMBP"
                     /gene_synonym="ARHGEF36; CTRCT48; TUBA"
                     /coded_by="NM_001441288.1:121..4725"
                     /note="isoform d is encoded by transcript variant 5"
                     /db_xref="GeneID:23268"
                     /db_xref="HGNC:HGNC:30373"
                     /db_xref="MIM:611282"
ORIGIN      
        1 meagsvvrai fdfcpsvsee lplfvgdiie vlavvdefwl lgkkedvtgq fpssfveivt
       61 ipslkegerl fvciceftsq eldnlplhrg dlvildgipt agwlqgrscw gargffpssc
      121 vrelclssqs rqwhsqsalf qipeysmgqa ralmglsaql deeldfregd vitiigvpep
      181 gwfegelegr rgifpegfve llgplrtvde svssgnqddc ivngevdtpv geeeigpded
      241 eeepgtygva lyrfqalepn eldfevgdki rilatledgw legslkgrtg ifpyrfvklc
      301 pdtrveetma lpqegslari petsldclen tlgveeqrhe tsdheaeepd ciiseaptsp
      361 lghltseydt drnsyqdedt aggpprspgv ewemplatds ptsdptevvn gissqpqvpf
      421 hpnlqksqyy stvggshphs eqypdllple artrdyaslp pkrmysqlkt lqkpvlplyr
      481 gssvsasrvv kprqsspqlh nlasytkkhh tssvysiser lemkpgpqaq glvmeaaths
      541 qgdgstdlds kltqqliefe kslagpgtep dkilrhfsim dfnsekdivr gsskliteqe
      601 lperrkalrp ppprpctpvs tsphllvdqn lkpapplvvr psrpaplpps aqqrtnavsp
      661 kllsrhrptc etlekegpgh mgrsldqtsp cplvlvriee merdldmysr aqeelnlmle
      721 ekqdessrae tledlkfces nieslnmelq qlremtllss qssslvapsg svsaenpeqr
      781 mlekrakvie ellqterdyi rdlemcieri mvpmqqaqvp nidfeglfgn mqmvikvskq
      841 llaaleisda vgpvflghrd elegtykiyc qnhdeaiall eiyekdekiq khlqdsladl
      901 kslynewgct nyinlgsfli kpvqrvmryp lllmellnst peshpdkvpl tnavlavkei
      961 nvnineykrr kdlvlkyrkg dedslmekis klnihsiikk snrvsshlkh ltgfapqikd
     1021 evfeeteknf rmqerliksf irdlslylqh irkerterlv isplnqllsm ftgphklvqk
     1081 rfdklldfyn cteraeklkd kktleelqsa rnnyealnaq lldelpkfhq yaqglftncv
     1141 hgyaeahcdf vhqaleqlkp llsllkvagr egnliaifhe ehsrvlqqlq vftffpeslp
     1201 atkkpferkt idrqsarkpl lglpsymlqs eelrasllar yppeklfqae rnfnaaqdld
     1261 vsllegdlvg vikkkdpmgs qnrwlidngv tkgfvyssfl kpynprrshs dasvgshsst
     1321 esehgssspr fprqnsgstl tfnpssmavs ftsgscqkqp qdaspppkec dqgtlsasln
     1381 psnsesspsr cpsdpdstsq prsgdsadva rdvkqptatp rsyrnfrhpe ivgysvpgrn
     1441 gqsqdlvkgc artaqapedr stepdgseae gnqvyfavyt fkarnpnels vsanqklkil
     1501 efkdvtgnte wwlaevngkk gyvpsnyirk teyt
//
LOCUS       NP_001393917             565 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform H [Homo sapiens].
ACCESSION   NP_001393917
VERSION     NP_001393917.1
DBSOURCE    REFSEQ: accession NM_001406988.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 565)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 565)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 565)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 565)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 565)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 565)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 565)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 565)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 565)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056191.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..565
                     /product="lamin isoform H"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=62722
     Region          30..287
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          335..442
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     CDS             1..565
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406988.1:121..1818"
                     /note="isoform H is encoded by transcript variant 15"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 mdleawdphl epdaeamvdg ntkkegdlia aqarlkdlea llnskeaals talsekrtle
       61 gelhdlrgqv akleaalgea kkqlqdemlr rvdaenrlqt mkeeldfqkn iyseelretk
      121 rrhetrlvei dngkqrefes rladalqelr aqhedqveqy kkelektysa kldnarqsae
      181 rnsnlvgaah eelqqsriri dslsaqlsql qkqlaakeak lrdledslar erdtsrrlla
      241 ekeremaemr armqqqldey qelldiklal dmeihayrkl legeeerlrl spsptsqrsr
      301 grasshssqt qgggsvtkkr klestesrss fsqhartsgr vaveevdeeg kfvrlrnksn
      361 edqsmgnwqi krqngddpll tyrfppkftl kagqvvtiwa agagathspp tdlvwkaqnt
      421 wgcgnslrta linstgeeva mrklvrsvtv veddededgd dllhhhhgsh csssgdpaey
      481 nlrsrtvlcg tcgqpadkas asgsgaqvgg pissgssass vtvtrsyrsv ggsgggsfgd
      541 nlvtrsyllg nssprtqspq ncsim
//
LOCUS       NP_001427340             321 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 7 precursor [Homo
            sapiens].
ACCESSION   NP_001427340
VERSION     NP_001427340.1
DBSOURCE    REFSEQ: accession NM_001440411.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 321)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3 and AP004147.3.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.188213.1,
                                           SRR1803614.77292.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..321
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     7 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=33613
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..>302
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            286
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     CDS             1..321
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440411.1:299..1264"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 13"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk aaelgmvsay
      241 ytyiftnlef slqrmdslvd drvnilgfsi fnqshaffqe faqslnqswq encdhvpftg
      301 pagilvtvks ghvalldkwg n
//
LOCUS       NP_001389634            1145 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 14 [Homo sapiens].
ACCESSION   NP_001389634
VERSION     NP_001389634.1
DBSOURCE    REFSEQ: accession NM_001402705.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1145)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1145)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1145)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1145)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1145)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1145)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1145)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1145)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1145)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1145)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1705984.1,
                                           SRR14038193.272799.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1145
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1145
                     /product="kinectin isoform 14"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=131948
     Region          <142..>400
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          296..1085
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1145
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402705.1:178..3615"
                     /note="isoform 14 is encoded by transcript variant 28"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mvpskrqeal plhqetkqes gsgkkkassk kqktenvfvd eplihattyi plmdnadssp
       61 vvdkrevidl lkpdqvegiq ksgtkklkte tdkenaevkf kdfllslktm mfsedealcv
      121 vdllkeksgv iqdalkkssk gelttlihql qekdkllaav kedaaatkdr ckqltqemmt
      181 ekersnvvit rmkdrigtle kehnvfqnki hvsyqetqqm qmkfqqvreq meaeiahlkq
      241 engilrdavs nttnqleskq saelnklrqd yarlvnelte ktgklqqeev qkknaeqaat
      301 qlkvqlqeae rrweevqsyi rkrtaeheaa qqdlqskfva kenevqslhs kltdtlvskq
      361 qleqrlmqlm eseqkrvnke eslqmqvqdi leqnealkaq iqqfhsqiaa qtsasvlaee
      421 lhkviaekdk qikqtedsla serdrltske eelkdiqnmn fllkaevqkl qalaneqaaa
      481 ahelekmqqs vyvkddkirl leeqlqheis nkmeefkiln dqnkalksev qklqtlvseq
      541 pnkdvveqme kciqekdekl ktveelletg liqvatkeee lnairtenss ltkevqdlka
      601 kqndqvsfas lveelkkvih ekdgkiksve elleaellkv ankektvqdl kqeikalkee
      661 ignvqlekaq qlsitskvqe lqnllkgkee qmntmkavle ekekdlantg kwlqdlqeen
      721 eslkahvqev aqhnlkeass asqfeeleiv lkekenelkr leamlkeres dlssktqllq
      781 dvqdenklfk sqieqlkqqn yqqassfpph eellkviser ekeisglwne ldslkdaveh
      841 qrkknndlre knweameala stekmlqdkv nktskerqqq veaveleake vlkklfpkvs
      901 vpsnlsygew lhgfekkake cmagtsgsee vkvlehklke ademhtllql ecekyksvla
      961 etegilqklq rsveqeenkw kvkvdeshkt ikqmqssfts seqelerlrs enkdienlrr
     1021 erehlemele kaemerstyv tevrelkaql netltklrte qnerqkvagd lhkaqqslel
     1081 iqskivkaag dttviensdv spetesseke tmsvslnqtv tqlqqllqav nqqltkekeh
     1141 yqvle
//
LOCUS       NP_001274676             353 aa            linear   PRI 21-NOV-2025
DEFINITION  squalene synthase isoform 2 [Homo sapiens].
ACCESSION   NP_001274676
VERSION     NP_001274676.1
DBSOURCE    REFSEQ: accession NM_001287747.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Kanmalar,M., Kamal,R., Abdul Sani,S.F., Pathmanathan,D., Bm
            Said,N.A., Paramanantham,Y., Abd Jamil,A.H., Mun,K.S.,
            Kuppusamy,S., Almugren,K.S., Almajid,H.F. and Bradley,D.A.
  TITLE     Spectroscopic diagnosis and metabolite characterization of
            cisplatin resistance regulated by FDFT1 in bladder cancer tissue
  JOURNAL   Appl Radiat Isot 210, 111372 (2024)
   PUBMED   38810354
  REMARK    GeneRIF: Spectroscopic diagnosis and metabolite characterization of
            cisplatin resistance regulated by FDFT1 in bladder cancer tissue.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Avci,D., Heidasch,R., Costa,M., Luchtenborg,C., Kale,D., Brugger,B.
            and Lemberg,M.K.
  TITLE     Intramembrane protease SPP defines a cholesterol-regulated
            abundance control of the mevalonate pathway enzyme squalene
            synthase
  JOURNAL   J Biol Chem 300 (2), 105644 (2024)
   PUBMED   38218226
  REMARK    GeneRIF: Intramembrane protease SPP defines a cholesterol-regulated
            abundance control of the mevalonate pathway enzyme squalene
            synthase.
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Jiang,H., Tang,E., Chen,Y., Liu,H., Zhao,Y., Lin,M. and He,L.
  TITLE     Squalene synthase predicts poor prognosis in stage I-III colon
            adenocarcinoma and synergizes squalene epoxidase to promote tumor
            progression
  JOURNAL   Cancer Sci 113 (3), 971-985 (2022)
   PUBMED   34939274
  REMARK    GeneRIF: Squalene synthase predicts poor prognosis in stage I-III
            colon adenocarcinoma and synergizes squalene epoxidase to promote
            tumor progression.
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Nakae,A., Kodama,M., Okamoto,T., Tokunaga,M., Shimura,H.,
            Hashimoto,K., Sawada,K., Kodama,T., Copeland,N.G., Jenkins,N.A. and
            Kimura,T.
  TITLE     Ubiquitin specific peptidase 32 acts as an oncogene in epithelial
            ovarian cancer by deubiquitylating farnesyl-diphosphate
            farnesyltransferase 1
  JOURNAL   Biochem Biophys Res Commun 552, 120-127 (2021)
   PUBMED   33744759
  REMARK    GeneRIF: Ubiquitin specific peptidase 32 acts as an oncogene in
            epithelial ovarian cancer by deubiquitylating farnesyl-diphosphate
            farnesyltransferase 1.
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Guan,G., Jiang,G., Koch,R.L. and Shechter,I.
  TITLE     Molecular cloning and functional analysis of the promoter of the
            human squalene synthase gene
  JOURNAL   J Biol Chem 270 (37), 21958-21965 (1995)
   PUBMED   7665618
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Soltis,D.A., McMahon,G., Caplan,S.L., Dudas,D.A., Chamberlin,H.A.,
            Vattay,A., Dottavio,D., Rucker,M.L., Engstrom,R.G.,
            Cornell-Kennon,S.A. et al.
  TITLE     Expression, purification, and characterization of the human
            squalene synthase: use of yeast and baculoviral systems
  JOURNAL   Arch Biochem Biophys 316 (2), 713-723 (1995)
   PUBMED   7864626
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Shechter,I., Conrad,D.G., Hart,I., Berger,R.C., McKenzie,T.L.,
            Bleskan,J. and Patterson,D.
  TITLE     Localization of the squalene synthase gene (FDFT1) to human
            chromosome 8p22-p23.1
  JOURNAL   Genomics 20 (1), 116-118 (1994)
   PUBMED   8020937
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Jiang,G., McKenzie,T.L., Conrad,D.G. and Shechter,I.
  TITLE     Transcriptional regulation by lovastatin and 25-hydroxycholesterol
            in HepG2 cells and molecular cloning and expression of the cDNA for
            the human hepatic squalene synthase
  JOURNAL   J Biol Chem 268 (17), 12818-12824 (1993)
   PUBMED   7685352
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Coman,D., Vissers,L., Waterham,H., Christodoulou,J., Wevers,R.A.
            and Pitt,J.
  TITLE     Squalene Synthase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   32027475
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC069185.7.
            
            Summary: This gene encodes a membrane-associated enzyme located at
            a branch point in the mevalonate pathway. The encoded protein is
            the first specific enzyme in cholesterol biosynthesis, catalyzing
            the dimerization of two molecules of farnesyl diphosphate in a
            two-step reaction to form squalene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (6) differs at the 5' end and
            initiates translation from an in-frame downstream start codon
            compared to variant 1. The resulting isoform (2) has a shorter
            N-terminus compared to isoform 1. Variants 4-8 encode the same
            isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK316033.1, SRR11853564.25456.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p23.1"
     Protein         1..353
                     /product="squalene synthase isoform 2"
                     /EC_number="2.5.1.21"
                     /note="presqualene-di-diphosphate synthase; squalene
                     synthase; FPP:FPP farnesyltransferase; squalene
                     synthetase"
                     /calculated_mol_wt=40639
     Region          1..306
                     /region_name="Isoprenoid_Biosyn_C1"
                     /note="Isoprenoid Biosynthesis enzymes, Class 1; cl00210"
                     /db_xref="CDD:469660"
     Site            order(9,16,20,107,115,119,147,154..155,159,164,224..225,
                     229)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:173831"
     Site            order(9,13,16,20,107,112,116,144,147,154..155,158..159,
                     164,224..225)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:173831"
     Site            order(16..20,155..159)
                     /site_type="active"
                     /note="substrate-Mg2+ binding site [active]"
                     /db_xref="CDD:173831"
     Site            16..20
                     /site_type="other"
                     /note="aspartate-rich region 1"
                     /db_xref="CDD:173831"
     Site            155..159
                     /site_type="other"
                     /note="aspartate-rich region 2"
                     /db_xref="CDD:173831"
     CDS             1..353
                     /gene="FDFT1"
                     /gene_synonym="DGPT; ERG9; SQS; SQSD; SS"
                     /coded_by="NM_001287747.2:535..1596"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS75696.1"
                     /db_xref="GeneID:2222"
                     /db_xref="HGNC:HGNC:3629"
                     /db_xref="MIM:184420"
ORIGIN      
        1 mrnavcifyl vlraldtled dmtisvekkv pllhnfhsfl yqpdwrfmes kekdrqvled
       61 fptislefrn laekyqtvia dicrrmgigm aefldkhvts eqewdkychy vaglvgigls
      121 rlfsasefed plvgedtera nsmglflqkt niirdyledq qggrefwpqe vwsryvkklg
      181 dfakpenidl avqclnelit nalhhipdvi tylsrlrnqs vfnfcaipqv maiatlaacy
      241 nnqqvfkgav kirkgqavtl mmdatnmpav kaiiyqymee iyhripdsdp sssktrqiis
      301 tirtqnlpnc qlisrshysp iylsfvmlla alswqylttl sqvtedyvqt geh
//
LOCUS       NP_001276329             278 aa            linear   PRI 21-NOV-2025
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily A member 2 isoform f precursor [Homo sapiens].
ACCESSION   NP_001276329
VERSION     NP_001276329.1
DBSOURCE    REFSEQ: accession NM_001289400.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Zhang,Z., Li,Q., Sun,S., Li,Z., Cui,Z., Liu,Q., Zhang,Y., Xiong,S.
            and Zhang,S.
  TITLE     Expression of SMARCA2 and SMARCA4 in gastric adenocarcinoma and
            construction of a nomogram prognostic model
  JOURNAL   Int J Clin Oncol 28 (11), 1487-1500 (2023)
   PUBMED   37634210
  REMARK    GeneRIF: Expression of SMARCA2 and SMARCA4 in gastric
            adenocarcinoma and construction of a nomogram prognostic model.
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Zhang,Z., Li,Q., Sun,S., Li,Z., Cui,Z.G., Zhang,M., Liu,Q.,
            Zhang,Y., Xiong,S. and Zhang,S.
  TITLE     Clinicopathological and prognostic significance of SWI/SNF complex
            subunits in undifferentiated gastric carcinoma
  JOURNAL   World J Surg Oncol 20 (1), 383 (2022)
   PUBMED   36464671
  REMARK    GeneRIF: Clinicopathological and prognostic significance of SWI/SNF
            complex subunits in undifferentiated gastric carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Zhang,X., Chen,H., Song,Y., Chen,Z., Liu,X., Rong,P. and Ma,R.
  TITLE     Ten-year follow-up of Nicolaides-Baraitser syndrome with a de novo
            mutation and analysis of 58 gene loci of SMARCA2-associated NCBRS
  JOURNAL   Mol Genet Genomic Med 10 (9), e2009 (2022)
   PUBMED   35811451
  REMARK    GeneRIF: Ten-year follow-up of Nicolaides-Baraitser syndrome with a
            de novo mutation and analysis of 58 gene loci of SMARCA2-associated
            NCBRS.
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Aves,S.J., Hindley,J., Phear,G.A. and Tongue,N.
  TITLE     A fission yeast gene mapping close to suc1 encodes a protein
            containing two bromodomains
  JOURNAL   Mol Gen Genet 248 (4), 491-498 (1995)
   PUBMED   7565614
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Chiba,H., Muramatsu,M., Nomoto,A. and Kato,H.
  TITLE     Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and
            Drosophila brahma are transcriptional coactivators cooperating with
            the estrogen receptor and the retinoic acid receptor
  JOURNAL   Nucleic Acids Res 22 (10), 1815-1820 (1994)
   PUBMED   8208605
REFERENCE   8  (residues 1 to 278)
  AUTHORS   Muchardt,C., Yaniv,M. and Mattei,M.G.
  TITLE     Assignment of HBRM, the human homolog of S. cerevisiae SNF2/SWI2
            and Drosophila brm genes, to chromosome region 9p23-p24, by in situ
            hybridization
  JOURNAL   Mamm Genome 5 (4), 241-243 (1994)
   PUBMED   8012116
REFERENCE   9  (residues 1 to 278)
  AUTHORS   Muchardt,C. and Yaniv,M.
  TITLE     A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and
            Drosophila brm genes potentiates transcriptional activation by the
            glucocorticoid receptor
  JOURNAL   EMBO J 12 (11), 4279-4290 (1993)
   PUBMED   8223438
REFERENCE   10 (residues 1 to 278)
  AUTHORS   Abdul-Rahman,O. and May,F.
  TITLE     SMARCA2-Related Nicolaides-Baraitser Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26468571
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138755.13.
            
            Summary: The protein encoded by this gene is a member of the
            SWI/SNF family of proteins and is highly similar to the brahma
            protein of Drosophila. Members of this family have helicase and
            ATPase activities and are thought to regulate transcription of
            certain genes by altering the chromatin structure around those
            genes. The encoded protein is part of the large ATP-dependent
            chromatin remodeling complex SNF/SWI, which is required for
            transcriptional activation of genes normally repressed by
            chromatin. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene, which contains a
            trinucleotide repeat (CAG) length polymorphism. [provided by
            RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK094076.1, SRR14038192.57798.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.3"
     Protein         1..278
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily A member
                     2 isoform f precursor"
                     /note="global transcription activator homologous sequence;
                     SNF2-alpha; sucrose nonfermenting 2-like protein 2;
                     SNF2/SWI2-like protein 2; SWI/SNF-related
                     matrix-associated actin-dependent regulator of chromatin
                     a2; brahma homolog; probable global transcription
                     activator SNF2L2; BAF190B; protein brahma homolog;
                     BRG1-associated factor 190B; ATP-dependent helicase
                     SMARCA2; putative global transcription activator SNF2L2;
                     SWI/SNF related, matrix associated, actin dependent
                     regulator of chromatin, subfamily a, member 2"
                     /calculated_mol_wt=29379
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2618
     Region          39..>101
                     /region_name="Bromodomain"
                     /note="Bromodomains are found in many chromatin-associated
                     proteins and in nuclear histone acetyltransferases. They
                     interact specifically with acetylated lysine; cl02556"
                     /db_xref="CDD:445827"
     Region          88..194
                     /region_name="Bromo_SNF2L2"
                     /note="Bromodomain, SNF2L2-like subfamily, specific to
                     animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related
                     matrix-associated actin-dependent regulator of chromatin
                     subfamily A member 2 is a global transcriptional
                     activator, which cooperates with nuclear hormone...;
                     cd05516"
                     /db_xref="CDD:99947"
     Site            order(119,124,127,166,170,176)
                     /site_type="active"
                     /note="acetyllysine binding site [active]"
                     /db_xref="CDD:99947"
     CDS             1..278
                     /gene="SMARCA2"
                     /gene_synonym="BAF190; BIS; BRM; hBRM; hSNF2a; NCBRS;
                     SAMRCA2; SNF2; SNF2L2; SNF2LA; Sth1p; SWI2"
                     /coded_by="NM_001289400.2:513..1349"
                     /note="isoform f precursor is encoded by transcript
                     variant 7"
                     /db_xref="CCDS:CCDS75808.1"
                     /db_xref="GeneID:6595"
                     /db_xref="HGNC:HGNC:11098"
                     /db_xref="MIM:600014"
ORIGIN      
        1 mlmkrlaarc fagllilspl tvisdsrpad sgkaiedgnl eemeeevrlk krkrrrnvdk
       61 dpakedveka kkrrgrppae klspnppklt kqmnaiidtv inykdssgrq lsevfiqlps
      121 rkelpeyyel irkpvdfkki kerirnhkyr slgdlekdvm llchnaqtfn legsqiyeds
      181 ivlqsvfksa rqkiakeees edesneeeee edeeesesea ksvkvkikln kkddkgrdkg
      241 kgkkrpnrgk akpvvsdfds deeqdereqs egsgtdde
//
LOCUS       NP_001397639             431 aa            linear   PRI 21-NOV-2025
DEFINITION  septin-6 isoform E [Homo sapiens].
ACCESSION   NP_001397639 XP_006724811
VERSION     NP_001397639.1
DBSOURCE    REFSEQ: accession NM_001410710.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Fischer,M., Frank,D., Rosler,R., Johnsson,N. and Gronemeyer,T.
  TITLE     Biochemical Characterization of a Human Septin Octamer
  JOURNAL   Front Cell Dev Biol 10, 771388 (2022)
   PUBMED   35309913
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Mendonca,D.C., Guimaraes,S.L., Pereira,H.D., Pinto,A.A., de
            Farias,M.A., de Godoy,A.S., Araujo,A.P.U., van Heel,M.,
            Portugal,R.V. and Garratt,R.C.
  TITLE     An atomic model for the human septin hexamer by cryo-EM
  JOURNAL   J Mol Biol 433 (15), 167096 (2021)
   PUBMED   34116125
  REMARK    GeneRIF: An atomic model for the human septin hexamer by cryo-EM.
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Sheffield,P.J., Oliver,C.J., Kremer,B.E., Sheng,S., Shao,Z. and
            Macara,I.G.
  TITLE     Borg/septin interactions and the assembly of mammalian septin
            heterodimers, trimers, and filaments
  JOURNAL   J Biol Chem 278 (5), 3483-3488 (2003)
   PUBMED   12446710
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Surka,M.C., Tsang,C.W. and Trimble,W.S.
  TITLE     The mammalian septin MSF localizes with microtubules and is
            required for completion of cytokinesis
  JOURNAL   Mol Biol Cell 13 (10), 3532-3545 (2002)
   PUBMED   12388755
REFERENCE   8  (residues 1 to 431)
  AUTHORS   Slater,D.J., Hilgenfeld,E., Rappaport,E.F., Shah,N., Meek,R.G.,
            Williams,W.R., Lovett,B.D., Osheroff,N., Autar,R.S., Ried,T. and
            Felix,C.A.
  TITLE     MLL-SEPTIN6 fusion recurs in novel translocation of chromosomes 3,
            X, and 11 in infant acute myelomonocytic leukaemia and in t(X;11)
            in infant acute myeloid leukaemia, and MLL genomic breakpoint in
            complex MLL-SEPTIN6 rearrangement is a DNA topoisomerase II
            cleavage site
  JOURNAL   Oncogene 21 (30), 4706-4714 (2002)
   PUBMED   12096348
  REMARK    GeneRIF: MLL-SEPTIN6 fusion recurs in novel translocation of
            chromosomes 3, X, and 11 in infant acute myelomonocytic leukaemia
            and in t(X;11) in infant acute myeloid leukaemia
REFERENCE   9  (residues 1 to 431)
  AUTHORS   Ono,R., Taki,T., Taketani,T., Kawaguchi,H., Taniwaki,M.,
            Okamura,T., Kawa,K., Hanada,R., Kobayashi,M. and Hayashi,Y.
  TITLE     SEPTIN6, a human homologue to mouse Septin6, is fused to MLL in
            infant acute myeloid leukemia with complex chromosomal
            abnormalities involving 11q23 and Xq24
  JOURNAL   Cancer Res 62 (2), 333-337 (2002)
   PUBMED   11809673
REFERENCE   10 (residues 1 to 431)
  AUTHORS   Kinoshita,A., Noda,M. and Kinoshita,M.
  TITLE     Differential localization of septins in the mouse brain
  JOURNAL   J Comp Neurol 428 (2), 223-239 (2000)
   PUBMED   11064363
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005052.2, AL355348.28 and
            AC004913.2.
            
            On Aug 15, 2022 this sequence version replaced XP_006724811.1.
            
            Summary: This gene is a member of the septin family of GTPases.
            Members of this family are required for cytokinesis. One version of
            pediatric acute myeloid leukemia is the result of a reciprocal
            translocation between chromosomes 11 and X, with the breakpoint
            associated with the genes encoding the mixed-lineage leukemia and
            septin 2 proteins. This gene encodes four transcript variants
            encoding three distinct isoforms. An additional transcript variant
            has been identified, but its biological validity has not been
            determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1742067.1,
                                           SRR18074969.1303994.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq24"
     Protein         1..431
                     /product="septin-6 isoform E"
                     /note="septin 2"
                     /calculated_mol_wt=49172
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:12665801,
                     ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q14141.4)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14141.4)"
     Region          39..307
                     /region_name="CDC_Septin"
                     /note="CDC/Septin GTPase family; cd01850"
                     /db_xref="CDD:206649"
     Region          49..56
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14141.4)"
     Site            49..56
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206649"
     Site            order(51..57,101,104,184..185,187,239..240)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206649"
     Site            76..84
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206649"
     Site            78
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206649"
     Region          101..104
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14141.4)"
     Site            101..104
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            order(103..139,141..150)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Region          184..187
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14141.4)"
     Site            184..187
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            239..241
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     Site            367
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14141.4)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14141.4)"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14141.4)"
     CDS             1..431
                     /gene="SEPTIN6"
                     /gene_synonym="SEP2; SEPT2; SEPT6; Septin-6"
                     /coded_by="NM_001410710.1:64..1359"
                     /note="isoform E is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS94661.1"
                     /db_xref="GeneID:23157"
                     /db_xref="HGNC:HGNC:15848"
                     /db_xref="MIM:300683"
ORIGIN      
        1 maatdiarqv gegcrtvpla ghvgfdslpd qlvnksvsqg fcfnilcvge tglgkstlmd
       61 tlfntkfege pathtqpgvq lqsntydlqe snvrlkltiv stvgfgdqin kedsykpive
      121 fidaqfeayl qeelkirrvl htyhdsrihv clyfiaptgh slksldlvtm kkldskvnii
      181 piiakadais kseltkfkik itselvsngv qiyqfptdde svaeingtmn ahlpfavigs
      241 teelkignkm mrarqypwgt vqveneahcd fvklremlir vnmedlreqt htrhyelyrr
      301 ckleemgfkd tdpdskpfsl qetyeakrne flgelqkkee emrqmfvqrv kekeaelkea
      361 ekelhekfdr lkklhqdekk kledkkksld devnafkqrk taaellqsqg sqaggsqtlk
      421 rdkekknlgf l
//
LOCUS       NP_001401588             520 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 2 isoform e [Homo sapiens].
ACCESSION   NP_001401588
VERSION     NP_001401588.1
DBSOURCE    REFSEQ: accession NM_001414659.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Jung,J.H., Lee,D., Ko,H.M. and Jang,H.J.
  TITLE     Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in Colorectal
            Cancer Cells by Activating p53
  JOURNAL   Biomolecules 11 (10), 1492 (2021)
   PUBMED   34680125
  REMARK    GeneRIF: Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in
            Colorectal Cancer Cells by Activating p53.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Royer-Bertrand,B., Cisarova,K., Niel Butschi,F., Foletti,G.,
            Guinchat,V., Tran,C., Superti-Furga,A. and Good,J.M.
  TITLE     CNOT2 haploinsufficiency in a 40-year-old man with intellectual
            disability, autism, and seizures
  JOURNAL   Am J Med Genet A 185 (8), 2602-2606 (2021)
   PUBMED   34018673
  REMARK    GeneRIF: CNOT2 haploinsufficiency in a 40-year-old man with
            intellectual disability, autism, and seizures.
            Review article
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Jayne,S., Zwartjes,C.G., van Schaik,F.M. and Timmers,H.T.
  TITLE     Involvement of the SMRT/NCoR-HDAC3 complex in transcriptional
            repression by the CNOT2 subunit of the human Ccr4-Not complex
  JOURNAL   Biochem J 398 (3), 461-467 (2006)
   PUBMED   16712523
  REMARK    GeneRIF: This study shows that SMRT/NCoR-HDAC3 complex is a
            cofactor of CNOT2-mediated repression and suggests that
            transcriptional regulation by the Ccr4-Not complex involves
            regulation of chromatin modification.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Winkler,G.S., Mulder,K.W., Bardwell,V.J., Kalkhoven,E. and
            Timmers,H.T.
  TITLE     Human Ccr4-Not complex is a ligand-dependent repressor of nuclear
            receptor-mediated transcription
  JOURNAL   EMBO J 25 (13), 3089-3099 (2006)
   PUBMED   16778766
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Shi,J. and Nelson,M.A.
  TITLE     The cyclin-dependent kinase 11 interacts with NOT2
  JOURNAL   Biochem Biophys Res Commun 334 (4), 1310-1316 (2005)
   PUBMED   16039607
  REMARK    GeneRIF: These findings suggest that CDK11 may contribute to
            apoptosis by regulating the activity of NOT2 independent of its
            kinase activity.
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Zwartjes,C.G., Jayne,S., van den Berg,D.L. and Timmers,H.T.
  TITLE     Repression of promoter activity by CNOT2, a subunit of the
            transcription regulatory Ccr4-not complex
  JOURNAL   J Biol Chem 279 (12), 10848-10854 (2004)
   PUBMED   14707134
  REMARK    GeneRIF: major repression function of CNOT2 is localized in a
            specialized protein motif, the Not-Box
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Denis,C.L. and Chen,J.
  TITLE     The CCR4-NOT complex plays diverse roles in mRNA metabolism
  JOURNAL   Prog Nucleic Acid Res Mol Biol 73, 221-250 (2003)
   PUBMED   12882519
  REMARK    Review article
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092881.8 and AC025569.37.
            
            Summary: This gene encodes a subunit of the multi-component
            CCR4-NOT complex. The CCR4-NOT complex regulates mRNA synthesis and
            degradation and is also thought to be involved in mRNA splicing,
            transport and localization. The encoded protein interacts with
            histone deacetylases and functions as a repressor of polymerase II
            transcription. Alternatively spliced transcript variants have been
            observed for this gene. [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2232196.1,
                                           SRR14038191.1471138.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2156670 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..520
                     /product="CCR4-NOT transcription complex subunit 2 isoform
                     e"
                     /note="negative regulator of transcription 2;
                     CCR4-associated factor 2; CC chemokine receptor 4-negative
                     regulator of transcription 2"
                     /calculated_mol_wt=57288
     Region          376..499
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..520
                     /gene="CNOT2"
                     /gene_synonym="CDC36; HSPC131; IDNADFS; NOT2; NOT2H"
                     /coded_by="NM_001414659.1:365..1927"
                     /note="isoform e is encoded by transcript variant 13"
                     /db_xref="GeneID:4848"
                     /db_xref="HGNC:HGNC:7878"
                     /db_xref="MIM:604909"
ORIGIN      
        1 mfgasrkkfv egvdsdyhde nmyysqssmf phrsekdmla spstsgqlsq fgaslygqqs
       61 alglpmrgms nntpqlnrsl sqgtqlpshv tpttgvptms lhtppspsrg ilpmnprnmm
      121 nhsqvgqgig ipsrtnsmss sglgspnrss psiicmpkqq psrqpftvns msgfgmnrnq
      181 afgmnnslss nifngtdgse nvtgldlsdf paladrnrre gsgnptplin plagrapyvg
      241 mvtkpaneqs qdfsihnedf palpgssykd ptssnddsks nlntsgktts stdgpkfpgd
      301 kssttqnnnq qkkgiqvlpd grvtnipqgm vtdqfgmigl ltfiraaetd pgmvhlalgs
      361 dlttlglnln spenlypkfa spwasspcrp qdidfhvpse yltnihirdk laaiklgryg
      421 edllfylyym nggdvlqlla avelfnrdwr yhkeervwit rapgmeptmk tntyergtyy
      481 ffdclnwrkv akefhleydk leerphlpst fnynpaqqaf
//
LOCUS       NP_001394742            1216 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 10 precursor
            [Homo sapiens].
ACCESSION   NP_001394742
VERSION     NP_001394742.1
DBSOURCE    REFSEQ: accession NM_001407813.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1216)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1216)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1216)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1216)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1216)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1216)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1216)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1216)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1216)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1216)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2045126.1,
                                           SRR14038191.817034.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1216
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1216
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 10 precursor"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=136864
     Region          18..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          95..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          418..690
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          717..736
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          788..1216
                     /region_name="Mediates interaction with TEFM.
                     /evidence=ECO:0000269|PubMed:21278163"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          817..1216
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1216
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407813.1:26..3676"
                     /note="isoform 10 precursor is encoded by transcript
                     variant 10"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 msalcwgrga aglkralrpc grpglpgkeg taggvcgprr sssaspqeqd qdrrkdwghv
       61 ellevlqarv rqlqaesvse vvvnrvdvar lpecgsgdgs lqpprkvqmg akdatpvpcg
      121 rwakilekdk rtqqmrmqrl kaklqmpfqs gefkaltrrl qveprllskq magcledctr
      181 qapespweeq larllqeapg klsldveqap sgqhsqaqls gqqqrllaff kcclltdqlp
      241 lahhllvvhh gqrqkrkllt ldmynavmlg warqdagltp dllsyaaalq cmgrqdqdag
      301 tiercleqms qeglklqalf tavllseedr atvlkavhkv kptfslppql pppvntskll
      361 rdvyakdgrv sypklhlplk tlqclfekql hmelasrvcv vsvekptlps kevkharktl
      421 ktlrdqweka lcralretkn rlerevyegr fslypflcll derevvrmll qvlqalpaqg
      481 esfttlarel sartfsrhvv qrqrvsgqvq alqnhyrkyl cllasdaevp epclprqywe
      541 elgapealre qpwplpvqme lgkllaemlv qatqmpcsld kphrssrlvp vlyhvysfrn
      601 vqqigilkph payvqlleka aeptltfeav dvpmlcpplp wtsphsgafl lsptklmrtv
      661 egatqhqell etcpptalhg aldaltqlgn cawrvngrvl dlvlqlfqak gcpqlgvpap
      721 pseapqppea hlphsaapar kaelrrelah cqkvaremhs lraealyrls laqhlrdrvf
      781 wlphnmdfrg rtypcpphfn hlgsdvaral lefaqgrplg phgldwlkih lvnltglkkr
      841 eplrkrlafa eevmddilds adqpltgrkw wmgaeepwqt laccmevana vrasdpaayv
      901 shlpvhqdgs cnglqhyaal grdsvgaasv nlepsdvpqd vysgvaaqve vfrrqdaqrg
      961 mrvaqvlegf itrkvvkqtv mtvvygvtry ggrlqiekrl relsdfpqef vweashylvr
     1021 qvfkslqemf sgtraiqhwl tesarlishm gsvvewvtpl gvpviqpyrl dskvkqiggg
     1081 iqsitythng disrkpntrk qkngfppnfi hsldsshmml talhcyrkgl tfvsvhdcyw
     1141 thaadvsvmn qvcreqfvrl hsepilqdls rflvkrfcse pqkileasql ketlqavpkp
     1201 gafdleqvkr styffs
//
LOCUS       NP_001397925             479 aa            linear   PRI 21-NOV-2025
DEFINITION  nuclear receptor subfamily 6 group A member 1 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001397925 XP_005251974
VERSION     NP_001397925.1
DBSOURCE    REFSEQ: accession NM_001410996.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Neelathi,U.M., Ullah,E., George,A., Maftei,M.I., Boobalan,E.,
            Sanchez-Mendoza,D., Adams,C., McGaughey,D., Sergeev,Y.V., Ai
            Rawi,R., Naik,A., Bender,C., Maumenee,I.H., Michaelides,M.,
            Tan,T.G., Lin,S., Villasmil,R., Blain,D., Hufnagel,R.B., Arno,G.,
            Young,R.M., Guan,B. and Brooks,B.P.
  TITLE     Variants in NR6A1 cause a novel oculo vertebral renal syndrome
  JOURNAL   Nat Commun 16 (1), 6111 (2025)
   PUBMED   40610405
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Wu,Q., Li,X., Long,M., Xie,X. and Liu,Q.
  TITLE     Integrated analysis of histone lysine lactylation (Kla)-specific
            genes suggests that NR6A1, OSBP2 and UNC119B are novel therapeutic
            targets for hepatocellular carcinoma
  JOURNAL   Sci Rep 13 (1), 18642 (2023)
   PUBMED   37903971
  REMARK    GeneRIF: Integrated analysis of histone lysine lactylation
            (Kla)-specific genes suggests that NR6A1, OSBP2 and UNC119B are
            novel therapeutic targets for hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Daisuke,H., Kato,H., Fukumura,K., Mayeda,A., Miyagi,Y., Seiki,M.
            and Koshikawa,N.
  TITLE     Novel LAMC2 fusion protein has tumor-promoting properties in
            ovarian carcinoma
  JOURNAL   Cancer Sci 112 (12), 4957-4967 (2021)
   PUBMED   34689384
  REMARK    GeneRIF: Novel LAMC2 fusion protein has tumor-promoting properties
            in ovarian carcinoma.
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Zhou,W., Jiang,R., Wang,Y., Li,Y., Sun,Z. and Zhao,H.
  TITLE     hsa_circ_001653 up-regulates NR6A1 expression and elicits gastric
            cancer progression by binding to microRNA-377
  JOURNAL   Exp Physiol 105 (12), 2141-2153 (2020)
   PUBMED   33006200
  REMARK    GeneRIF: hsa_circ_001653 up-regulates NR6A1 expression and elicits
            gastric cancer progression by binding to microRNA-377.
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Wang,Y., Wan,X., Hao,Y., Zhao,Y., Du,L., Huang,Y., Liu,Z., Wang,Y.,
            Wang,N. and Zhang,P.
  TITLE     NR6A1 regulates lipid metabolism through mammalian target of
            rapamycin complex 1 in HepG2 cells
  JOURNAL   Cell Commun Signal 17 (1), 77 (2019)
   PUBMED   31315616
  REMARK    GeneRIF: the role of NR6A1 in the lipogenesis in HepG2 cells
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Agoulnik,I.Y., Cho,Y., Niederberger,C., Kieback,D.G. and
            Cooney,A.J.
  TITLE     Cloning, expression analysis and chromosomal localization of the
            human nuclear receptor gene GCNF
  JOURNAL   FEBS Lett 424 (1-2), 73-78 (1998)
   PUBMED   9537518
REFERENCE   7  (residues 1 to 479)
  AUTHORS   Kapelle,M., Kratzschmar,J., Husemann,M. and Schleuning,W.D.
  TITLE     cDNA cloning of two closely related forms of human germ cell
            nuclear factor (GCNF)
  JOURNAL   Biochim Biophys Acta 1352 (1), 13-17 (1997)
   PUBMED   9177477
REFERENCE   8  (residues 1 to 479)
  AUTHORS   Yan,Z.H., Medvedev,A., Hirose,T., Gotoh,H. and Jetten,A.M.
  TITLE     Characterization of the response element and DNA binding properties
            of the nuclear orphan receptor germ cell nuclear factor/retinoid
            receptor-related testis-associated receptor
  JOURNAL   J Biol Chem 272 (16), 10565-10572 (1997)
   PUBMED   9099702
REFERENCE   9  (residues 1 to 479)
  AUTHORS   Lei,W., Hirose,T., Zhang,L.X., Adachi,H., Spinella,M.J.,
            Dmitrovsky,E. and Jetten,A.M.
  TITLE     Cloning of the human orphan receptor germ cell nuclear
            factor/retinoid receptor-related testis-associated receptor and its
            differential regulation during embryonal carcinoma cell
            differentiation
  JOURNAL   J Mol Endocrinol 18 (2), 167-176 (1997)
   PUBMED   9134503
REFERENCE   10 (residues 1 to 479)
  AUTHORS   Susens,U. and Borgmeyer,U.
  TITLE     Characterization of the human germ cell nuclear factor gene
  JOURNAL   Biochim Biophys Acta 1309 (3), 179-182 (1996)
   PUBMED   8982251
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354928.9, AL158075.11 and
            AL354979.17.
            
            On Aug 20, 2022 this sequence version replaced XP_005251974.1.
            
            Summary: This gene encodes an orphan nuclear receptor which is a
            member of the nuclear hormone receptor family. Its expression
            pattern suggests that it may be involved in neurogenesis and germ
            cell development. The protein can homodimerize and bind DNA, but in
            vivo targets have not been identified. Alternate splicing results
            in multiple transcript variants.[provided by RefSeq, Jun 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1329334.1,
                                           SRR14038193.1835922.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..479
                     /product="nuclear receptor subfamily 6 group A member 1
                     isoform 5"
                     /note="retinoic acid receptor-related testis-associated
                     receptor; retinoid receptor-related testis-specific
                     receptor"
                     /calculated_mol_wt=54165
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15406.2)"
     Region          52..141
                     /region_name="NR_DBD_GCNF_like"
                     /note="DNA-binding domain of Germ cell nuclear factor
                     (GCNF) F1 is composed of two C4-type zinc fingers;
                     cd07169"
                     /db_xref="CDD:143543"
     Site            order(60,63,77,80,96,102,112,115)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143543"
     Site            order(70..72,78..79,81,83,86,89,109..110,113,116,127,130)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143543"
     Region          131..150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15406.2)"
     Region          255..466
                     /region_name="NR_LBD_DHR4_like"
                     /note="The ligand binding domain of orphan nuclear
                     receptor Ecdysone-induced receptor DHR4; cd06953"
                     /db_xref="CDD:132751"
     Site            order(285..286,290,324,328,331,345,368)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:132751"
     Site            order(295,298,302,307,312..313,315..316,319..320)
                     /site_type="active"
                     /note="putative coactivator recognition site [active]"
                     /db_xref="CDD:132751"
     CDS             1..479
                     /gene="NR6A1"
                     /gene_synonym="CT150; GCNF; GCNF1; hGCNF; hRTR; NR61; RTR"
                     /coded_by="NM_001410996.1:193..1632"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS94481.1"
                     /db_xref="GeneID:2649"
                     /db_xref="HGNC:HGNC:7985"
                     /db_xref="MIM:602778"
ORIGIN      
        1 merdepppsg ggggggsagf leppaalppp prngfcqdel aeldpgtisv sddraeqrtc
       61 licgdratgl hygiiscegc kgffkrsicn krvyrcsrdk ncvmsrkqrn rcqycrllkc
      121 lqmgmnrkai redgmpggrn ksigpvqise eeierimsgq efeeeanhws nhgdsdhssp
      181 gnrasesnqp spgstlssrs velngfmafr eqymgmsvpp hyqyiphlfs ysghspllpq
      241 qarsldpqsy slihqllsae dleplgtpml iedgyavtqa elfallcrla dellfrqiaw
      301 ikklpffcel sikdytclls stwqelills sltvyskqif geladvtaky spsdeelhrf
      361 sdegmevier liylyhkfhq lkvsneeyac mkainflnqd irgltsasql eqlnkrywyi
      421 cqdfteykyt hqpnrfpdlm mclpeiryia gkmvnvpleq lpllfkvvlh scktsvgke
//
LOCUS       NP_001425595             755 aa            linear   PRI 21-NOV-2025
DEFINITION  TRPM8 channel-associated factor 2 isoform H [Homo sapiens].
ACCESSION   NP_001425595
VERSION     NP_001425595.1
DBSOURCE    REFSEQ: accession NM_001438666.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 755)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 755)
  AUTHORS   Yun,D., Liang,J., Wang,X., Fan,J., Wang,X., Li,J., Ren,X., Liu,J.,
            Ren,X., Zhang,H., Shang,G., Jin,W., Chen,L., Li,T., Zhang,C., Yu,S.
            and Yang,X.
  TITLE     TCAF2 drives glioma cellular migratory/invasion properties through
            STAT3 signaling
  JOURNAL   Mol Cell Biochem 479 (7), 1801-1815 (2024)
   PUBMED   38019450
  REMARK    GeneRIF: TCAF2 drives glioma cellular migratory/invasion properties
            through STAT3 signaling.
REFERENCE   3  (residues 1 to 755)
  AUTHORS   Li,Y., Li,J., Chen,H., Lu,B., Lu,F., Chen,H., Liu,H. and Qian,C.
  TITLE     TCAF2 is associated with the immune microenvironment, promotes
            pathogenesis, and impairs prognosis in glioma
  JOURNAL   Gene 883, 147667 (2023)
   PUBMED   37506986
  REMARK    GeneRIF: TCAF2 is associated with the immune microenvironment,
            promotes pathogenesis, and impairs prognosis in glioma.
REFERENCE   4  (residues 1 to 755)
  AUTHORS   Li,X., Qi,Q., Li,Y., Miao,Q., Yin,W., Pan,J., Zhao,Z., Chen,X.,
            Yang,F., Zhou,X., Huang,M., Wang,C., Deng,L., Huang,D., Qi,M.,
            Fan,S., Zhang,Y., Qiu,S., Deng,W., Liu,T., Chen,M., Ye,W. and
            Zhang,D.
  TITLE     TCAF2 in Pericytes Promotes Colorectal Cancer Liver Metastasis via
            Inhibiting Cold-Sensing TRPM8 Channel
  JOURNAL   Adv Sci (Weinh) 10 (30), e2302717 (2023)
   PUBMED   37635201
  REMARK    GeneRIF: TCAF2 in Pericytes Promotes Colorectal Cancer Liver
            Metastasis via Inhibiting Cold-Sensing TRPM8 Channel.
REFERENCE   5  (residues 1 to 755)
  AUTHORS   Hsieh,P., Dang,V., Vollger,M.R., Mao,Y., Huang,T.H., Dishuck,P.C.,
            Baker,C., Cantsilieris,S., Lewis,A.P., Munson,K.M., Sorensen,M.,
            Welch,A.E., Underwood,J.G. and Eichler,E.E.
  TITLE     Evidence for opposing selective forces operating on human-specific
            duplicated TCAF genes in Neanderthals and humans
  JOURNAL   Nat Commun 12 (1), 5118 (2021)
   PUBMED   34433829
  REMARK    GeneRIF: Evidence for opposing selective forces operating on
            human-specific duplicated TCAF genes in Neanderthals and humans.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 755)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 755)
  AUTHORS   Gkika,D., Lemonnier,L., Shapovalov,G., Gordienko,D., Poux,C.,
            Bernardini,M., Bokhobza,A., Bidaux,G., Degerny,C., Verreman,K.,
            Guarmit,B., Benahmed,M., de Launoit,Y., Bindels,R.J., Fiorio Pla,A.
            and Prevarskaya,N.
  TITLE     TRP channel-associated factors are a novel protein family that
            regulates TRPM8 trafficking and activity
  JOURNAL   J Cell Biol 208 (1), 89-107 (2015)
   PUBMED   25559186
  REMARK    GeneRIF: Report novel TRP channel-associated factors that modulate
            TRPM8 activity.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073264.5 and AC106862.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.51206.1,
                                           SRR7410571.151593.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..755
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q35"
     Protein         1..755
                     /product="TRPM8 channel-associated factor 2 isoform H"
                     /note="family with sequence similarity 139, member A;
                     protein FAM115C; family with sequence similarity 115,
                     member C; TRP channel-associated factor 2"
                     /calculated_mol_wt=83760
     Region          358..468
                     /region_name="M60-like_N"
                     /note="N-terminal domain of M60-like peptidases;
                     pfam17291"
                     /db_xref="CDD:435844"
     Region          469..725
                     /region_name="Peptidase_M60"
                     /note="Peptidase M60, enhancin and enhancin-like;
                     pfam13402"
                     /db_xref="CDD:433178"
     CDS             1..755
                     /gene="TCAF2"
                     /gene_synonym="FAM115C; FAM139A; GATD9; GATD9B"
                     /coded_by="NM_001438666.1:72..2339"
                     /note="isoform H is encoded by transcript variant 13"
                     /db_xref="GeneID:285966"
                     /db_xref="HGNC:HGNC:26878"
                     /db_xref="MIM:616252"
ORIGIN      
        1 mkifqkefkf ilkkctpiqk yreengnsss sphhqlqsha sgprygedvr qdqqqllegi
       61 seldirtggv psqllvhgal afplgldasl ncflaaahyg rgrvvlaahe cllcapkmgp
      121 fllnavrwla rgqtgkvgvn tnlkdlcpll sehglqcsle phlnsdlcvy cckaysdkea
      181 kqlqefvaeg gglliggqaw wwasqnpghc plagfpgnii lncfglsilp qtlkagcfpv
      241 ptpemrsyhf rkalsqfqai lnhengnlek sclaklrvdg aaflqipaeg vpayislhrl
      301 lrkmlrgsgl pavsrenpva sdsyeaavls latglahsgt dcsqlaqglg twtcssslyp
      361 skhpitvein ginpgnndcw vstglylleg qnaevslsea aasaglrvqi gchtddltka
      421 rklsrapvvt hqcwmdrter svsclwggll yvivpkgsql gpvpvtirga vpapyyklgk
      481 tsleewkrqm qenlapwgel atdniiltvp ttnlqalkdp epvlrlwdem mqavarlaae
      541 pfpfrrperi vadvqisagw mhsgypimch lesvkeiine mdmrsrgvwg pihelghnqq
      601 rhgwefppht teatcnlwsv yvhetvlgip raqahealsp pererrikah lgkgaplcdw
      661 nvwtaletyl qlqeafgwep ftqlfaeyqt lshlpkdntg rmnlwvkkfs ekvkknlvpf
      721 feawgwpiqk evadslaslp ewqenpmqvy lrark
//
LOCUS       NP_001402868             422 aa            linear   PRI 21-NOV-2025
DEFINITION  synaptotagmin-1 isoform 1 [Homo sapiens].
ACCESSION   NP_001402868
VERSION     NP_001402868.1
DBSOURCE    REFSEQ: accession NM_001415939.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Stephan,G., Haddock,S., Wang,S., Erdjument-Bromage,H., Liu,W.,
            Ravn-Boess,N., Frenster,J.D., Bready,D., Cai,J., Ronnen,R.,
            Sabio-Ortiz,J., Fenyo,D., Neubert,T.A. and Placantonakis,D.G.
  TITLE     Modulation of GPR133 (ADGRD1) signaling by its intracellular
            interaction partner extended synaptotagmin 1
  JOURNAL   Cell Rep 43 (5), 114229 (2024)
   PUBMED   38758649
  REMARK    GeneRIF: Modulation of GPR133 (ADGRD1) signaling by its
            intracellular interaction partner extended synaptotagmin 1.
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Zhang,J., Ren,G., Huang,T., Sang,Y., Zhong,Y. and Yi,Y.
  TITLE     miRNA-363-3p Hinders Proliferation, Migration, Invasion and
            Autophagy of Thyroid Cancer Cells by Controlling SYT1 Transcription
            to affect NF-kappaB
  JOURNAL   Endocr Metab Immune Disord Drug Targets 24 (1), 153-162 (2024)
   PUBMED   37150983
  REMARK    GeneRIF: miRNA-363-3p Hinders Proliferation, Migration, Invasion
            and Autophagy of Thyroid Cancer Cells by Controlling SYT1
            Transcription to affect NF-kappaB.
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Yamada,K., Motohashi,S., Oikawa,T., Tago,N., Koizumi,R., Ono,M.,
            Tachibana,T., Yoshida,A., Yoshida,S., Shimoda,M., Oka,M., Yoneda,Y.
            and Yoshida,K.
  TITLE     Extended-synaptotagmin 1 engages in unconventional protein
            secretion mediated via SEC22B+ vesicle pathway in liver cancer
  JOURNAL   Proc Natl Acad Sci U S A 119 (36), e2202730119 (2022)
   PUBMED   36044553
  REMARK    GeneRIF: Extended-synaptotagmin 1 engages in unconventional protein
            secretion mediated via SEC22B(+) vesicle pathway in liver cancer.
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Thibord,F., Chan,M.V., Chen,M.H. and Johnson,A.D.
  TITLE     A year of COVID-19 GWAS results from the GRASP portal reveals
            potential genetic risk factors
  JOURNAL   HGG Adv 3 (2), 100095 (2022)
   PUBMED   35224516
REFERENCE   6  (residues 1 to 422)
  AUTHORS   McMahon,H.T., Missler,M., Li,C. and Sudhof,T.C.
  TITLE     Complexins: cytosolic proteins that regulate SNAP receptor function
  JOURNAL   Cell 83 (1), 111-119 (1995)
   PUBMED   7553862
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Chowdhury,D., Travis,G.H., Sutcliffe,J.G. and Burton,F.H.
  TITLE     Synaptotagmin I and 1B4 are identical: implications for
            synaptotagmin distribution in the primate brain
  JOURNAL   Neurosci Lett 190 (1), 9-12 (1995)
   PUBMED   7624059
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Mochly-Rosen,D., Miller,K.G., Scheller,R.H., Khaner,H., Lopez,J.
            and Smith,B.L.
  TITLE     p65 fragments, homologous to the C2 region of protein kinase C,
            bind to the intracellular receptors for protein kinase C
  JOURNAL   Biochemistry 31 (35), 8120-8124 (1992)
   PUBMED   1326322
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Perin,M.S., Johnston,P.A., Ozcelik,T., Jahn,R., Francke,U. and
            Sudhof,T.C.
  TITLE     Structural and functional conservation of synaptotagmin (p65) in
            Drosophila and humans
  JOURNAL   J Biol Chem 266 (1), 615-622 (1991)
   PUBMED   1840599
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Blaustein,R.O., Germann,W.J., Finkelstein,A. and DasGupta,B.R.
  TITLE     The N-terminal half of the heavy chain of botulinum type A
            neurotoxin forms channels in planar phospholipid bilayers
  JOURNAL   FEBS Lett 226 (1), 115-120 (1987)
   PUBMED   2446925
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073606.19, AC073616.17,
            AC073572.19, AC078917.14 and AC027288.26.
            
            Summary: This gene encodes a member of the synaptotagmin protein
            family. The synaptotagmins are integral membrane proteins of
            synaptic vesicles that serve as calcium sensors in the process of
            vesicular trafficking and exocytosis. The encoded protein
            participates in triggering neurotransmitter release at the synapse
            in response to calcium binding. Mutations in this gene are
            associated with Baker-Gordon syndrome. [provided by RefSeq, Jan
            2023].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.205488.1,
                                           SRR1803612.128314.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.2"
     Protein         1..422
                     /product="synaptotagmin-1 isoform 1"
                     /note="sytI; synaptotagmin I"
                     /calculated_mol_wt=47442
     Region          6..113
                     /region_name="Syt1_N"
                     /note="N-terminal domain of synaptotagmin-1 (Syt1) and
                     similar proteins; cd21963"
                     /db_xref="CDD:409248"
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            order(40,43..44,46..48,50..51)
                     /site_type="other"
                     /note="Botolinum neurotoxin B binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409248"
     Site            58..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Region          113..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Region          136..382
                     /region_name="Phospholipid binding. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Region          143..265
                     /region_name="C2A_Synaptotagmin-1-5-6-9-10"
                     /note="C2A domain first repeat present in Synaptotagmins
                     1, 5, 6, 9, and 10; cd08385"
                     /db_xref="CDD:176031"
     Site            order(173,179,231,233,239)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176031"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P46096; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46096; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Region          274..409
                     /region_name="C2B_Synaptotagmin-1"
                     /note="C2 domain second repeat present in Synaptotagmin 1;
                     cd08402"
                     /db_xref="CDD:176047"
     Site            order(304,310,364,366,372)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176047"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21707; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21707; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     CDS             1..422
                     /gene="SYT1"
                     /gene_synonym="BAGOS; P65; SVP65; SYT"
                     /coded_by="NM_001415939.1:595..1863"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="GeneID:6857"
                     /db_xref="HGNC:HGNC:11509"
                     /db_xref="MIM:185605"
ORIGIN      
        1 mvseshheal aappvttvat vlpsnatepa spgegkedaf sklkekfmne lhkiplppwa
       61 liaiaivavl lvltccfcic kkclfkkknk kkgkekggkn ainmkdvkdl gktmkdqalk
      121 dddaetgltd geekeepkee eklgklqysl dydfqnnqll vgiiqaaelp aldmggtsdp
      181 yvkvfllpdk kkkfetkvhr ktlnpvfneq ftfkvpysel ggktlvmavy dfdrfskhdi
      241 igefkvpmnt vdfghvteew rdlqsaekee qeklgdicfs lryvptagkl tvvileaknl
      301 kkmdvgglsd pyvkihlmqn gkrlkkkktt ikkntlnpyy nesfsfevpf eqiqkvqvvv
      361 tvldydkigk ndaigkvfvg ynstgaelrh wsdmlanprr piaqwhtlqv eeevdamlav
      421 kk
//
LOCUS       NP_001427528             377 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform n [Homo sapiens].
ACCESSION   NP_001427528
VERSION     NP_001427528.1
DBSOURCE    REFSEQ: accession NM_001440599.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 377)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.774415.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..377
                     /product="polycomb protein EED isoform n"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=42878
     Region          <120..>374
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          129..166
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          176..238
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          245..293
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          301..341
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          349..373
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..377
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001440599.1:478..1611"
                     /note="isoform n is encoded by transcript variant 14"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdendd avsiesgtnt erpdtptntp
       61 napgrkswgk gkwkskkcky sfkcvnslke dhnqplfgvq fnwhskegdp lvfatvgsnr
      121 hyvghgnain elkfhprdpn lllsvskdha lrlwniqtdt lvaifggveg hrdevlsady
      181 dllgekimsc gmdhslklwr inskrmmnai kesydynpnk tnrpfisqki hfpdfstrdi
      241 hrnyvdcvrw lgdlilsksc enaivcwkpg kmeddidkik psesnvtilg rfdysqcdiw
      301 ymrfsmdfwq kmlalgnqvg klyvwdleve dphkakcttl thhkcgaair qtsfsrdssi
      361 liavcddasi wrwdrlr
//
LOCUS       NP_001427436             583 aa            linear   PRI 21-NOV-2025
DEFINITION  radixin isoform 2 [Homo sapiens].
ACCESSION   NP_001427436 XP_047283346 XP_054225575
VERSION     NP_001427436.1
DBSOURCE    REFSEQ: accession NM_001440507.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 583)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Kruse,T., Benz,C., Garvanska,D.H., Lindqvist,R., Mihalic,F.,
            Coscia,F., Inturi,R., Sayadi,A., Simonetti,L., Nilsson,E., Ali,M.,
            Kliche,J., Moliner Morro,A., Mund,A., Andersson,E., McInerney,G.,
            Mann,M., Jemth,P., Davey,N.E., Overby,A.K., Nilsson,J. and
            Ivarsson,Y.
  TITLE     Large scale discovery of coronavirus-host factor protein
            interaction motifs reveals SARS-CoV-2 specific mechanisms and
            vulnerabilities
  JOURNAL   Nat Commun 12 (1), 6761 (2021)
   PUBMED   34799561
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 583)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 583)
  AUTHORS   Stemmer-Rachamimov,A.O., Gonzalez-Agosti,C., Xu,L., Burwick,J.A.,
            Beauchamp,R., Pinney,D., Louis,D.N. and Ramesh,V.
  TITLE     Expression of NF2-encoded merlin and related ERM family proteins in
            the human central nervous system
  JOURNAL   J Neuropathol Exp Neurol 56 (6), 735-742 (1997)
   PUBMED   9184664
REFERENCE   7  (residues 1 to 583)
  AUTHORS   Hirao,M., Sato,N., Kondo,T., Yonemura,S., Monden,M., Sasaki,T.,
            Takai,Y., Tsukita,S. and Tsukita,S.
  TITLE     Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma
            membrane association: possible involvement of phosphatidylinositol
            turnover and Rho-dependent signaling pathway
  JOURNAL   J Cell Biol 135 (1), 37-51 (1996)
   PUBMED   8858161
REFERENCE   8  (residues 1 to 583)
  AUTHORS   Wilgenbus,K.K., Milatovich,A., Francke,U. and Furthmayr,H.
  TITLE     Molecular cloning, cDNA sequence, and chromosomal assignment of the
            human radixin gene and two dispersed pseudogenes
  JOURNAL   Genomics 16 (1), 199-206 (1993)
   PUBMED   8486357
REFERENCE   9  (residues 1 to 583)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 583)
  AUTHORS   Sato,N., Funayama,N., Nagafuchi,A., Yonemura,S., Tsukita,S. and
            Tsukita,S.
  TITLE     A gene family consisting of ezrin, radixin and moesin. Its specific
            localization at actin filament/plasma membrane association sites
  JOURNAL   J Cell Sci 103 (Pt 1), 131-143 (1992)
   PUBMED   1429901
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002788.3 and AP000901.5.
            
            On or before May 21, 2025 this sequence version replaced
            XP_047283346.1, XP_054225575.1.
            
            Summary: Radixin is a cytoskeletal protein that may be important in
            linking actin to the plasma membrane. It is highly similar in
            sequence to both ezrin and moesin. The radixin gene has been
            localized by fluorescence in situ hybridization to 11q23. A
            truncated version representing a pseudogene (RDXP2) was assigned to
            Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was
            mapped to 11p by Southern and PCR analyses. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1289736.1,
                                           SRR14038196.1240246.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267755 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..583
                     /product="radixin isoform 2"
                     /calculated_mol_wt=68433
     Region          7..206
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          200..296
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(242..243,245..251,260,281,284..285,288)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(242,245..252,260,281,284..285,288)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(278,282)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            281..296
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          310..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35241.1)"
     Region          347..456
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          376..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35241.1)"
     Region          462..526
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35241.1)"
     Region          507..583
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ROCK2.
                     /evidence=ECO:0000250|UniProtKB:P26043; propagated from
                     UniProtKB/Swiss-Prot (P35241.1)"
     CDS             1..583
                     /gene="RDX"
                     /gene_synonym="DFNB24"
                     /coded_by="NM_001440507.1:651..2402"
                     /note="isoform 2 is encoded by transcript variant 9"
                     /db_xref="GeneID:5962"
                     /db_xref="HGNC:HGNC:9944"
                     /db_xref="MIM:179410"
ORIGIN      
        1 mpkpinvrvt tmdaelefai qpnttgkqlf dqvvktvglr evwffglqyv dskgystwlk
       61 lnkkvtqqdv kkenplqfkf rakffpedvs eeliqeitqr lfflqvkeai lndeiycppe
      121 tavllasyav qakygdynke ihkpgyland rllpqrvleq hkltkeqwee riqnwheehr
      181 gmlredsmme ylkiaqdlem ygvnyfeikn kkgtelwlgv dalglniyeh ddkltpkigf
      241 pwseirnisf ndkkfvikpi dkkapdfvfy aprlrinkri lalcmgnhel ymrrrkpdti
      301 evqqmkaqar eekhqkqler aqlenekkkr eiaekekeri erekeelmer lkqieeqtik
      361 aqkeleeqtr kaleldqerk rakeeaerle kerraaeeak saiakqaadq mknqeqlaae
      421 laeftakial leeakkkkee eatewqhkaf aaqedlektk eelktvmsap pppppppvip
      481 ptenehdehd ennaeasael snegvmnhrs eeervtetqk nervkkqlqa lsselaqard
      541 etkktqndvl haenvkagrd kyktlrqirq gntkqridef eam
//
LOCUS       NP_001400677             825 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform k [Homo sapiens].
ACCESSION   NP_001400677
VERSION     NP_001400677.1
DBSOURCE    REFSEQ: accession NM_001413748.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 825)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 825)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 825)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 825)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 825)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.255969.1,
                                           SRR14038192.399364.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..825
                     /product="polyhomeotic-like protein 1 isoform k"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=87435
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          212..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          261..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          649..756
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          756..824
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(774..775,809..810,813..814,817)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(785..789,791..792,795..796,800,805)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..825
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413748.1:157..2634"
                     /note="isoform k is encoded by transcript variant 12"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq asinlattsa aqlisrsqsv
      121 sspsattltq svllgnttsp plnqsqaqmy lrpqlgnllq vnrtlgrnvp lasqlilmpn
      181 gavaavqqev psaqspgvha dadqvqnlav rnqqasaqgp qmqgstqkai ppgaspvssl
      241 sqassqalav aqassgatnq slnlsqaggg sgnsipgsmg pggggqahgg lgqlpssgmg
      301 ggscprkgtg vvqplpaaqt vtvsqgsqte aesaaakkae adgsgqqnvg mnltrtatpa
      361 psqtlissat ytqiqphsli qqqqqihlqq kqvviqqqia ihhqqqfqhr qsqllhtath
      421 lqlaqqqqqq qqqqqqqqqp qattltapqp pqgkpqtlav krkadseeer ddvstlgsml
      481 pakaspvaes pkvmdekssl gekaesvanv nantpsselv altpapsvpp ptlamvsrqm
      541 gdskppqaiv kpqilthiie gfviqegaep fpvgcsqllk esekplqtgl ptgltenqsg
      601 gplgvdspsa eldkkanllk ceycgkyapa eqfrgskrfc smtcakrynv scshqfrlkr
      661 kkmkefqean yarvrrrgpr rsssdiarak iqgkchrgqe dssrgsdnss ydealsptsp
      721 gplsvraghg erdlgnpnta pptpelhgin pvflssnpsr wsveevyefi aslqgcqeia
      781 eefrsqeidg qallllkeeh lmsamniklg palkicakin vlket
//
LOCUS       NP_001394267             281 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 37 [Homo sapiens].
ACCESSION   NP_001394267
VERSION     NP_001394267.1
DBSOURCE    REFSEQ: accession NM_001407338.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138528.80576.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..281
                     /product="tropomyosin alpha-1 chain isoform 37"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=32324
     Region          48..280
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..281
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407338.1:84..929"
                     /note="isoform 37 is encoded by transcript variant 37"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle ediaakekll rvsederdrv
       61 leelhkaeds llaaeeaaak aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegkc aeleeelktv tnnlksleaq aekysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledql yqqleqnrrl tnelklalne d
//
LOCUS       NP_001427985            4373 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HUWE1 isoform 5 [Homo sapiens].
ACCESSION   NP_001427985 XP_047297691 XP_054182286
VERSION     NP_001427985.1
DBSOURCE    REFSEQ: accession NM_001441056.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4373)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 4373)
  AUTHORS   Lee,C., Park,S.H. and Yoon,S.K.
  TITLE     The E3 ligase HUWE1 increases the sensitivity of CRC to oxaliplatin
            through TOMM20 degradation
  JOURNAL   Oncogene 43 (9), 636-649 (2024)
   PUBMED   38184713
  REMARK    GeneRIF: The E3 ligase HUWE1 increases the sensitivity of CRC to
            oxaliplatin through TOMM20 degradation.
REFERENCE   3  (residues 1 to 4373)
  AUTHORS   Li,X.X., Xu,J.K., Su,W.J., Wu,H.L., Zhao,K., Zhang,C.M., Chen,X.K.
            and Yang,L.X.
  TITLE     The role of KDM4A-mediated histone methylation on temozolomide
            resistance in glioma cells through the HUWE1/ROCK2 axis
  JOURNAL   Kaohsiung J Med Sci 40 (2), 161-174 (2024)
   PUBMED   37873881
  REMARK    GeneRIF: The role of KDM4A-mediated histone methylation on
            temozolomide resistance in glioma cells through the HUWE1/ROCK2
            axis.
REFERENCE   4  (residues 1 to 4373)
  AUTHORS   Bernassola,F., Karin,M., Ciechanover,A. and Melino,G.
  TITLE     The HECT family of E3 ubiquitin ligases: multiple players in cancer
            development
  JOURNAL   Cancer Cell 14 (1), 10-21 (2008)
   PUBMED   18598940
  REMARK    Review article
REFERENCE   5  (residues 1 to 4373)
  AUTHORS   Zhong,Q., Gao,W., Du,F. and Wang,X.
  TITLE     Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the
            polyubiquitination of Mcl-1 and regulates apoptosis
  JOURNAL   Cell 121 (7), 1085-1095 (2005)
   PUBMED   15989957
  REMARK    GeneRIF: Mule is both required and sufficient for the
            polyubiquitination of Mcl-1; Mule is a unique BH3-containing E3
            ubiquitin ligase apical to Bcl-2 family proteins during DNA
            damage-induced apoptosis
            GeneRIF: Mule (HUWE1) poly-ubiquitinates anti-apoptotic gene Mcl-1.
REFERENCE   6  (residues 1 to 4373)
  AUTHORS   Chen,D., Kon,N., Li,M., Zhang,W., Qin,J. and Gu,W.
  TITLE     ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
  JOURNAL   Cell 121 (7), 1071-1083 (2005)
   PUBMED   15989956
  REMARK    GeneRIF: study modifies the current view of ARF-mediated p53
            activation and reveals that ARF-BP1 is a critical mediator of both
            the p53-independent and p53-dependent tumor suppressor functions of
            ARF
            GeneRIF: Ubiquitin ligase activity of ARF-BP1 (HUWE1) is inhibited
            by Arf.
REFERENCE   7  (residues 1 to 4373)
  AUTHORS   Liu,Z., Oughtred,R. and Wing,S.S.
  TITLE     Characterization of E3Histone, a novel testis ubiquitin protein
            ligase which ubiquitinates histones
  JOURNAL   Mol Cell Biol 25 (7), 2819-2831 (2005)
   PUBMED   15767685
REFERENCE   8  (residues 1 to 4373)
  AUTHORS   Gu,J., Dubner,R., Fornace,A.J. Jr. and Iadarola,M.J.
  TITLE     UREB1, a tyrosine phosphorylated nuclear protein, inhibits p53
            transactivation
  JOURNAL   Oncogene 11 (10), 2175-2178 (1995)
   PUBMED   7478539
REFERENCE   9  (residues 1 to 4373)
  AUTHORS   Turner,G., Gedeon,A. and Mulley,J.
  TITLE     X-linked mental retardation with heterozygous expression and
            macrocephaly: pericentromeric gene localization
  JOURNAL   Am J Med Genet 51 (4), 575-580 (1994)
   PUBMED   7943042
REFERENCE   10 (residues 1 to 4373)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX323845.7 and AC231658.3.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297691.1, XP_054182286.1.
            
            Summary: This gene encodes a protein containing a C-terminal HECT
            (E6AP type E3 ubiquitin protein ligase) domain that functions as an
            E3 ubiquitin ligase. The encoded protein is required for the
            ubiquitination and subsequent degradation of the anti-apoptotic
            protein Mcl1 (myeloid cell leukemia sequence 1 (BCL2-related)).
            This protein also ubiquitinates the p53 tumor suppressor, core
            histones, and DNA polymerase beta. Mutations in this gene are
            associated with Turner type X-linked syndromic cognitive
            disability. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.328244.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..4373
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..4373
                     /product="E3 ubiquitin-protein ligase HUWE1 isoform 5"
                     /EC_number="2.3.2.26"
                     /note="Mcl-1 ubiquitin ligase E3; BJ-HCC-24 tumor antigen;
                     HECT domain protein LASU1; ARF-binding protein 1;
                     URE-binding protein 1; large structure of UREB1; upstream
                     regulatory element-binding protein 1; homologous to E6AP
                     carboxyl terminus homologous protein 9; HECT-type E3
                     ubiquitin transferase HUWE1; HECT, UBA and WWE domain
                     containing 1, E3 ubiquitin protein ligase"
                     /calculated_mol_wt=481691
     Region          92..367
                     /region_name="DUF908"
                     /note="Domain of Unknown Function (DUF908); pfam06012"
                     /db_xref="CDD:428721"
     Region          431..814
                     /region_name="DUF913"
                     /note="Domain of Unknown Function (DUF913); pfam06025"
                     /db_xref="CDD:461803"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          706..759
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          978..1001
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1014..1037
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1084
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1291..1320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1317..1356
                     /region_name="UBA_HUWE1"
                     /note="UBA domain found in eukaryotic E3 ubiquitin-protein
                     ligase HUWE1 and similar proteins; cd14288"
                     /db_xref="CDD:270474"
     Site            1368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1396..1415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1617..1678
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          1689..1735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1722
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1907
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2017..2064
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2034
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2261..2341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2266
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2355..2479
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2534
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2553
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2594
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2618
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2693..2969
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          <2734..3065
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            2750
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2825
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2832
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2860
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2886
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2887
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2888
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2917
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3009..3042
                     /region_name="UBM"
                     /note="Ubiquitin binding region; pfam14377"
                     /db_xref="CDD:464159"
     Region          3035..3058
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3148
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3244..3266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3403..3423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3470..3511
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3536..3567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3736..3757
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3751
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3780..3847
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3807
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3815
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3826
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3829
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3893..3930
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3905
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3918
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3923
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3926
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          4018..4371
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(4022,4052,4063,4124,4298,4334..4335,4338..4342,4362,
                     4370)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(4152,4155..4156,4158..4159,4162,4169,4171,
                     4175..4176,4178,4183,4188,4205,4209)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     Site            4270
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P51593; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     CDS             1..4373
                     /gene="HUWE1"
                     /gene_synonym="ARF-BP1; HECTH9; HSPC272; Ib772; LASU1;
                     MRXST; MULE; URE-B1; UREB1"
                     /coded_by="NM_001441056.1:426..13547"
                     /note="isoform 5 is encoded by transcript variant 10"
                     /db_xref="GeneID:10075"
                     /db_xref="HGNC:HGNC:30892"
                     /db_xref="MIM:300697"
ORIGIN      
        1 mkvdrtklkk tpteapadcr alidklkvcn deqlllelqq iktwnigkce lyhwvdlldr
       61 fdgiladagq tvenmswmlv cdrpereqlk mlllavlnft allieysfsr hlyssiehlt
      121 tllassdmqv vlavlnllyv fskrsnyitr lgsdkrtpll trlqhlaesw ggkengfgla
      181 eccrdlhmmk yppsattlhf efyadpgaev kiekrttsnt lhyihieqld kisespseim
      241 esltkmysip kdkqmllfth irlahgfsnh rkrlqavqar lhaisilvys nalqesansi
      301 lynglieelv dvlqitdkql meikaaslrt ltsivhlert pklssiidct gtasyhgflp
      361 vlvrnciqam idpsmdpyph qfatalfsfl yhlasydagg ealvscgmme allkvikflg
      421 deqdqitfvt ravrvvdlit nldmaafqsh sglsifiyrl ehevdlcrke cpfvikpkiq
      481 rpnttqegee metdmdgvqc ipqraallks mlnflkkaiq dpafsdgirh vmdgslptsl
      541 khiisnaeyy gpslfllate vvtvfvfqep sllsslqdng ltdvmlhall ikdvpatrev
      601 lgslpnvfsa lclnarglqs fvqcqpferl fkvllspdyl pamrrrrssd plgdtasnlg
      661 savdelmrhq ptlktdatta iiklleeicn lgrdpkyicq kpsiqkadgt atappprsnh
      721 aaeeassede eeeevqamqs fnstqqnete pnqqvvgtee ripiplmdyi lnvmkfvesi
      781 lsnnttddhc qefvnqkgll plvtilglpn lpidfptsaa cqavagvcks iltlshepkv
      841 lqegllqlds ilssleplhr piespggsvl lrelacagnv adatlsaqat pllhaltaah
      901 ayimmfvhtc rvgqseirsi svnqwgsqlg lsvlsklsql ycslvwestv llslctpnsl
      961 psgcefgqad mqklvpkdek agttqggkrs dgeqdgaags mdastqglle gigldgdtla
     1021 pmetdeptas dskgkskitp amaarikqik pllsassrlg ralaelfgll vklcvgspvr
     1081 qrrshhaast ttaptpaars tasaltkllt kglswqpppy tptprfrltf ficsvgftsp
     1141 mlfderkypy hlmlqkflcs gghnalfetf nwalsmggkv pvseglehsd lpdgtgefld
     1201 awlmlvekmv npttvlesph slpaklpggv qnfpqfsalr flvvtqkaaf tciknlwnrk
     1261 plkvyggrma esmlailchi lrgepvirer lskekegsrg eedtgqeegg srrepqvnqq
     1321 qlqqlmdmgf trehameall ntstmeqate yllthpppim ggvvrdlsms eedqmmraia
     1381 mslgqdipmd qraespeeva crkeeeerka rekqeeeeak clekfqdadp leqdelhtft
     1441 dtmlpgcfhl ldelpdtvyr vcdlimtaik rngadyrdmi lkqvvnqvwe aadvlikaal
     1501 plttsdtktv sewisqmatl pqasnlatri llltllfeel klpcawvves sgilnvlikl
     1561 levvqpclqa akeqkevqtp kwitpvllli dfyektaiss krraqmtkyl qsnsnnwrwf
     1621 ddrsgrwcsy sasnnstids awksgetsvr ftagrrrytv qfttmvqvne etgnrrpvml
     1681 tllrvprlnk nsknsngqel ektleeskem dikrkenkgn dtplalestn teketsleet
     1741 kigeiliqgl tedmvtvlir acvsmlgvpv dpdtlhatlr lclrltrdhk yammfaelks
     1801 trmilnltqs sgfngftplv tlllrhiied pctlrhtmek vvrsaatsga gsttsgvvsg
     1861 slgsreinyi lrvlgpaacr npdiftevan ccirialpap rgsgtasdde fenlrikgpn
     1921 avqlvkttpl kpsplpvipd tikeviydml nalaayhape edksdpkpgv mtqevgqllq
     1981 dmgddvyqqy rsltrqssdf dtqsgfsins qvfaadgast etsasgtsqg eastpeesrd
     2041 gkkdkegdra seegkqkgkg skplmptsti lrllaelvrs yvgiatlian ysytvgqsel
     2101 ikedcsvlaf vldhllphtq naedkdtpal arlflaslaa agsgtdaqva lvnevkaalg
     2161 ralamaeste kharlqavmc iistimescp stssfyssat aktqhngmnn iirlflkkgl
     2221 vndlarvphs ldlsspnman tvnaalkple tlsrivnqps slfgsksass knkseqdaqg
     2281 asqdsssnqq dpgepgeaev qeedhdvtqt evadgdimdg eaetdsvvia gqpevlssqe
     2341 mqveneledl idellerdgg sgnstiivsr sgedesqedv lmdeapsnls qastlqanre
     2401 dsmnildped eeehtqeeds sgsnededds qdeeeeeeed eeddqeddeg eegdeddddd
     2461 gsemeldedy pdmnasplvr ferfdreddl iiefdnmfss atdippspgn iptthplmvr
     2521 hadhssltlg sgssttrltq gigrsqrtlr qltantghti hvhypgnrqp npplilqrll
     2581 gpsaaadilq lssslplqsr grarllvgnd dvhiiarsdd ellddffhdq statsqagtl
     2641 ssiptaltrw teeckvldae smhdcvsvvk vsivnhlefl rdeeleerre krrkqlaeee
     2701 tkitdkgked kenrdqsaqc tasksndste qnlsdgtpmp dsypttpsst daatsesket
     2761 lgtlqssqqq ptlptppalg evpqelqspa geggsstqll mpvepeelgp trpsgeaett
     2821 qmelspapti tslsperaed sdaltavssq legspmdtss lasctleeav gdtsaagsse
     2881 qpragsstpg dappavaevq grsdgsgesa qppedssppa ssessstrds avaisgadsr
     2941 gileeplpst sseeedplag islpegvdps flaalpddir revlqnqlgi rpptrtapst
     3001 nssapavvgn pgvtevspef laalppaiqe evlaqqraeq qrrelaqnas sdtpmdpvtf
     3061 iqtlpsdlrr svledmedsv lavmppdiaa eaqalrreqe arqrqlmher lfghsstsal
     3121 sailrspaft srlsgnrgvq ytrlavqrgg tfqmggsssh nrpsgsnvdt llrlrgrlll
     3181 dhealscllv llfvdepkln tsrlhrvlrn lcyhaqtrhw virsllsilq rsseselcie
     3241 tpklttseek gkksskscgs sshenrpldl lhkmeskssn qlswlsvsmd aalgcrtnif
     3301 qiqrsggrkh tekhasggst vhihpqaapv vcrhvldtli qlakvfpshf tqqrtketnc
     3361 esdrergnka cspcssqsss sgictdfwdl lvkldnmnvs rkgknsvksv pvsaggeget
     3421 spysleaspl gqlmnmlshp virrssllte kllrllslis ialpenkvse aqansgsgas
     3481 stttatstts tttttaastt ptpptaptpv tsapalvaat aistivvaas ttvttpttat
     3541 ttvsispttk gskspakvsd ggssstdfkm vssgltenql qlsvevltsh scseegleda
     3601 anvllqlsrg dsgtrdtvlk lllngarhlg ytlckqigtl laelreynle qqrraqcetl
     3661 spdglpeeqp qttklkgkmq srfdmaenvv ivasqkrplg grelqlpsms mltsktstqk
     3721 fflrvlqvii qlrddtrran kkakqtgrlg ssglgsassi qaavrqleae adaiiqmvre
     3781 gqrarrqqqa atsessqsea svrreespmd vdqpspsaqd tqsiasdgtp qgekekeerp
     3841 pelpllseql sldelwdmlg eclkeleesh dqhavlvlqp aveafflvha tereskppvr
     3901 dtresqlahi kdeppplspa pltpatpssl dpffsrepss mhissslppd tqkflrfaet
     3961 hrtvlnqilr qstthladgp favlvdyirv ldfdvkrkyf rqelerldeg lrkedmavhv
     4021 rrdhvfedsy relhrkspee mknrlyivfe geegqdaggl lrewymiisr emfnpmyalf
     4081 rtspgdrvty tinpsshcnp nhlsyfkfvg rivakavydn rllecyftrs fykhilgksv
     4141 rytdmesedy hfyqglvyll endvstlgyd ltfstevqef gvcevrdlkp nganilvtee
     4201 nkkeyvhlvc qmrmtgairk qlaaflegfy eiipkrlisi fteqelelli sglptididd
     4261 lksnteyhky qsnsiqiqwf wralrsfdqa drakflqfvt gtskvplqgf aalegmngiq
     4321 kfqihrddrs tdrlpsahtc fnqldlpaye sfeklrhmll laiqecsegf gla
//
LOCUS       NP_001397991             698 aa            linear   PRI 21-NOV-2025
DEFINITION  metastasis-associated protein MTA1 isoform 4 [Homo sapiens].
ACCESSION   NP_001397991 XP_047287863
VERSION     NP_001397991.1
DBSOURCE    REFSEQ: accession NM_001411062.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 698)
  AUTHORS   Wanka,G., Jueckstock,J., Wild,C.M., Vattai,A., Furst,S.,
            Heidegger,H.H., Kuhn,C., Schmoeckel,E., Jeschke,U. and Dannecker,C.
  TITLE     MTA1 as negative prognostic marker in vulvar carcinoma
  JOURNAL   J Cancer Res Clin Oncol 149 (9), 6191-6201 (2023)
   PUBMED   36689059
  REMARK    GeneRIF: MTA1 as negative prognostic marker in vulvar carcinoma.
REFERENCE   3  (residues 1 to 698)
  AUTHORS   Vattem,C. and Pakala,S.B.
  TITLE     Metastasis-associated protein 1: A potential driver and regulator
            of the hallmarks of cancer
  JOURNAL   J Biosci 47 (2022)
   PUBMED   36210748
  REMARK    GeneRIF: Metastasis-associated protein 1: A potential driver and
            regulator of the hallmarks of cancer.
            Review article
REFERENCE   4  (residues 1 to 698)
  AUTHORS   Kumar,R., Balasenthil,S., Pakala,S.B., Rayala,S.K., Sahin,A.A. and
            Ohshiro,K.
  TITLE     Metastasis-associated protein 1 short form stimulates Wnt1 pathway
            in mammary epithelial and cancer cells
  JOURNAL   Cancer Res 70 (16), 6598-6608 (2010)
   PUBMED   20710043
REFERENCE   5  (residues 1 to 698)
  AUTHORS   Kumar,R., Balasenthil,S., Manavathi,B., Rayala,S.K. and Pakala,S.B.
  TITLE     Metastasis-associated protein 1 and its short form variant
            stimulates Wnt1 transcription through promoting its derepression
            from Six3 corepressor
  JOURNAL   Cancer Res 70 (16), 6649-6658 (2010)
   PUBMED   20682799
REFERENCE   6  (residues 1 to 698)
  AUTHORS   Singh,R.R., Kaluarachchi,K., Chen,M., Rayala,S.K., Balasenthil,S.,
            Ma,J. and Kumar,R.
  TITLE     Solution structure and antiestrogenic activity of the unique
            C-terminal, NR-box motif-containing region of MTA1s
  JOURNAL   J Biol Chem 281 (35), 25612-25621 (2006)
   PUBMED   16807247
  REMARK    GeneRIF: structure and antiestrogenic activity of the unique
            C-terminal, NR-box motif-containing region of MTA1
            Erratum:[J Biol Chem. 2013 Sep 20;288(38):27518]
REFERENCE   7  (residues 1 to 698)
  AUTHORS   Mishra,S.K., Yang,Z., Mazumdar,A., Talukder,A.H., Larose,L. and
            Kumar,R.
  TITLE     Metastatic tumor antigen 1 short form (MTA1s) associates with
            casein kinase I-gamma2, an estrogen-responsive kinase
  JOURNAL   Oncogene 23 (25), 4422-4429 (2004)
   PUBMED   15077195
  REMARK    GeneRIF: MTA1s interacts with CKI-gamma2 in vitro and in vivo and
            colocalizes in the cytoplasm
REFERENCE   8  (residues 1 to 698)
  AUTHORS   Kumar,R., Wang,R.A., Mazumdar,A., Talukder,A.H., Mandal,M.,
            Yang,Z., Bagheri-Yarmand,R., Sahin,A., Hortobagyi,G., Adam,L.,
            Barnes,C.J. and Vadlamudi,R.K.
  TITLE     A naturally occurring MTA1 variant sequesters oestrogen
            receptor-alpha in the cytoplasm
  JOURNAL   Nature 418 (6898), 654-657 (2002)
   PUBMED   12167865
  REMARK    GeneRIF: naturally occurring short form that contains a previously
            unknown sequence of 33 amino acids with an ER-binding motif,
            Leu-Arg-Ile-Leu-Leu (LRILL); MTA1s localizes in the cytoplasm,
            sequesters ER in the cytoplasm, and enhances non-genomic responses
            of ER
REFERENCE   9  (residues 1 to 698)
  AUTHORS   Toh,Y., Pencil,S.D. and Nicolson,G.L.
  TITLE     Analysis of the complete sequence of the novel
            metastasis-associated candidate gene, mta1, differentially
            expressed in mammary adenocarcinoma and breast cancer cell lines
  JOURNAL   Gene 159 (1), 97-104 (1995)
   PUBMED   7607577
REFERENCE   10 (residues 1 to 698)
  AUTHORS   Toh,Y., Pencil,S.D. and Nicolson,G.L.
  TITLE     A novel candidate metastasis-associated gene, mta1, differentially
            expressed in highly metastatic mammary adenocarcinoma cell lines.
            cDNA cloning, expression, and protein analyses
  JOURNAL   J Biol Chem 269 (37), 22958-22963 (1994)
   PUBMED   8083195
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL928654.1.
            
            On Aug 20, 2022 this sequence version replaced XP_047287863.1.
            
            Summary: This gene encodes a protein that was identified in a
            screen for genes expressed in metastatic cells, specifically,
            mammary adenocarcinoma cell lines. Expression of this gene has been
            correlated with the metastatic potential of at least two types of
            carcinomas although it is also expressed in many normal tissues.
            The role it plays in metastasis is unclear. It was initially
            thought to be the 70kD component of a nucleosome remodeling
            deacetylase complex, NuRD, but it is more likely that this
            component is a different but very similar protein. These two
            proteins are so closely related, though, that they share the same
            types of domains. These domains include two DNA binding domains, a
            dimerization domain, and a domain commonly found in proteins that
            methylate DNA. The profile and activity of this gene product
            suggest that it is involved in regulating transcription and that
            this may be accomplished by chromatin remodeling. Two transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Feb 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2056600.1,
                                           SRR14038196.1043885.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..698
                     /product="metastasis-associated protein MTA1 isoform 4"
                     /note="metastasis associated gene 1 protein"
                     /calculated_mol_wt=79062
     Region          3..171
                     /region_name="BAH_MTA"
                     /note="BAH, or Bromo Adjacent Homology domain, as present
                     in MTA1 and similar proteins. The Metastasis-associated
                     protein MTA1 is part of the NURD (nucleosome remodeling
                     and deacetylating) complex and plays a role in cellular
                     transformation and metastasis. BAH...; cd04709"
                     /db_xref="CDD:240060"
     Region          150..202
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          270..315
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(271,301..302,304..305,307..309,311..313)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          371..424
                     /region_name="ZnF_GATA"
                     /note="zinc finger binding to DNA consensus sequence
                     [AT]GATA[AG]; smart00401"
                     /db_xref="CDD:214648"
     Region          447..524
                     /region_name="MTA_R1"
                     /note="MTA R1 domain; pfam17226"
                     /db_xref="CDD:465388"
     CDS             1..698
                     /gene="MTA1"
                     /coded_by="NM_001411062.1:210..2306"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS91957.1"
                     /db_xref="GeneID:9112"
                     /db_xref="HGNC:HGNC:7410"
                     /db_xref="MIM:603526"
ORIGIN      
        1 maanmyrvgd yvyfensssn pylirrieel nktangnvea kvvcfyrrrd isstlialad
       61 khareieeem enpemvdlpe klkhqlrhre lflsrqlesl pathirgkcs vtllnetesl
      121 ksyleredff fyslvydpqq ktlladkgei rvgnryqadi tdllkegeed grdqsrletq
      181 vweahnpltd kqidqflvva rsvgtfaral dcsssvrqps lhmsaaaasr ditlfhamdt
      241 lhkniydisk aisalvpqgg pvlcrdemee wsaseanlfe ealekygkdf tdiqqdflpw
      301 ksltsiieyy ymwkttdryv qqkrlkaaea esklkqvyip nynkpnpnqi svnnvkagvv
      361 ngtgapgqsp gagracescy ttqsyqwysw gppnmqcrlc ascwtywkky gglkmptrld
      421 gerpgpnrsn msphglpars sgspkfamkt rqafylhttk ltriarrlcr eilrpwhaar
      481 hpylpinsaa ikaectarlp easqsplvlk qavrkpleav lrylethprp pkpdpvksvs
      541 svlssltpak vapvinngsp tilgkrsyeq hngvdgnmkk rllmpsrgla nhgqarhmgp
      601 srnlllngks yptkvrlirg gslppvkrrr mnwidapddv fymateetrk irkllssset
      661 kraarrpykp ialrqsqalp prppppapvn depivied
//
LOCUS       NP_001398079            1646 aa            linear   PRI 21-NOV-2025
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily A member 4 isoform G [Homo sapiens].
ACCESSION   NP_001398079 XP_047295201
VERSION     NP_001398079.1
DBSOURCE    REFSEQ: accession NM_001411150.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1646)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1646)
  AUTHORS   Schneppenheim,R., Fruhwald,M.C., Gesk,S., Hasselblatt,M.,
            Jeibmann,A., Kordes,U., Kreuz,M., Leuschner,I., Martin Subero,J.I.,
            Obser,T., Oyen,F., Vater,I. and Siebert,R.
  TITLE     Germline nonsense mutation and somatic inactivation of SMARCA4/BRG1
            in a family with rhabdoid tumor predisposition syndrome
  JOURNAL   Am J Hum Genet 86 (2), 279-284 (2010)
   PUBMED   20137775
  REMARK    GeneRIF: SMARCA4 is involved in cancer predisposition
REFERENCE   3  (residues 1 to 1646)
  AUTHORS   Wong,A.K., Shanahan,F., Chen,Y., Lian,L., Ha,P., Hendricks,K.,
            Ghaffari,S., Iliev,D., Penn,B., Woodland,A.M., Smith,R., Salada,G.,
            Carillo,A., Laity,K., Gupte,J., Swedlund,B., Tavtigian,S.V.,
            Teng,D.H. and Lees,E.
  TITLE     BRG1, a component of the SWI-SNF complex, is mutated in multiple
            human tumor cell lines
  JOURNAL   Cancer Res 60 (21), 6171-6177 (2000)
   PUBMED   11085541
REFERENCE   4  (residues 1 to 1646)
  AUTHORS   Muchardt,C., Reyes,J.C., Bourachot,B., Leguoy,E. and Yaniv,M.
  TITLE     The hbrm and BRG-1 proteins, components of the human SNF/SWI
            complex, are phosphorylated and excluded from the condensed
            chromosomes during mitosis
  JOURNAL   EMBO J 15 (13), 3394-3402 (1996)
   PUBMED   8670841
REFERENCE   5  (residues 1 to 1646)
  AUTHORS   Muchardt,C., Sardet,C., Bourachot,B., Onufryk,C. and Yaniv,M.
  TITLE     A human protein with homology to Saccharomyces cerevisiae SNF5
            interacts with the potential helicase hbrm
  JOURNAL   Nucleic Acids Res 23 (7), 1127-1132 (1995)
   PUBMED   7739891
REFERENCE   6  (residues 1 to 1646)
  AUTHORS   Chiba,H., Muramatsu,M., Nomoto,A. and Kato,H.
  TITLE     Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and
            Drosophila brahma are transcriptional coactivators cooperating with
            the estrogen receptor and the retinoic acid receptor
  JOURNAL   Nucleic Acids Res 22 (10), 1815-1820 (1994)
   PUBMED   8208605
REFERENCE   7  (residues 1 to 1646)
  AUTHORS   Khavari,P.A., Peterson,C.L., Tamkun,J.W., Mendel,D.B. and
            Crabtree,G.R.
  TITLE     BRG1 contains a conserved domain of the SWI2/SNF2 family necessary
            for normal mitotic growth and transcription
  JOURNAL   Nature 366 (6451), 170-174 (1993)
   PUBMED   8232556
REFERENCE   8  (residues 1 to 1646)
  AUTHORS   Nemes,K., Bens,S., Bourdeaut,F., Johann,P., Kordes,U., Siebert,R.
            and Fruhwald,M.C.
  TITLE     Rhabdoid Tumor Predisposition Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29215836
REFERENCE   9  (residues 1 to 1646)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
REFERENCE   10 (residues 1 to 1646)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011442.5, AC006127.1 and
            AC011485.6.
            
            On Aug 22, 2022 this sequence version replaced XP_047295201.1.
            
            Summary: The protein encoded by this gene is a member of the
            SWI/SNF family of proteins and is similar to the brahma protein of
            Drosophila. Members of this family have helicase and ATPase
            activities and are thought to regulate transcription of certain
            genes by altering the chromatin structure around those genes. The
            encoded protein is part of the large ATP-dependent chromatin
            remodeling complex SNF/SWI, which is required for transcriptional
            activation of genes normally repressed by chromatin. In addition,
            this protein can bind BRCA1, as well as regulate the expression of
            the tumorigenic protein CD44. Mutations in this gene cause rhabdoid
            tumor predisposition syndrome type 2. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, May 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2828140.1,
                                           SRR14038191.374744.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1646
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..1646
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily A member
                     4 isoform G"
                     /note="sucrose nonfermenting-like 4; mitotic growth and
                     transcription activator; BRM/SWI2-related gene 1; homeotic
                     gene regulator; nuclear protein GRB1; brahma protein-like
                     1; SNF2-like 4; global transcription activator homologous
                     sequence; transcription activator BRG1; ATP-dependent
                     helicase SMARCA4; protein BRG-1; protein brahma homolog 1;
                     BRG1-associated factor 190A; SWI/SNF related, matrix
                     associated, actin dependent regulator of chromatin,
                     subfamily a, member 4"
                     /calculated_mol_wt=184721
     Region          42..>222
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          171..205
                     /region_name="QLQ"
                     /note="pfam08880"
                     /db_xref="CDD:462622"
     Region          <364..>570
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          460..532
                     /region_name="HSA"
                     /note="domain in helicases and associated with SANT
                     domains; smart00573"
                     /db_xref="CDD:214727"
     Region          612..656
                     /region_name="BRK"
                     /note="domain in transcription and CHROMO domain
                     helicases; smart00592"
                     /db_xref="CDD:197800"
     Region          731..981
                     /region_name="DEXHc_SMARCA4"
                     /note="DEXH-box helicase domain of SMARCA4; cd18062"
                     /db_xref="CDD:350820"
     Region          750..>1232
                     /region_name="PLN03142"
                     /note="Probable chromatin-remodeling complex ATPase chain;
                     Provisional"
                     /db_xref="CDD:215601"
     Site            order(781..787,821,881..882)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350820"
     Region          1289..1356
                     /region_name="SnAC"
                     /note="Snf2-ATP coupling, chromatin remodelling complex;
                     pfam14619"
                     /db_xref="CDD:464219"
     Region          1457..1563
                     /region_name="Bromo_SNF2L2"
                     /note="Bromodomain, SNF2L2-like subfamily, specific to
                     animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related
                     matrix-associated actin-dependent regulator of chromatin
                     subfamily A member 2 is a global transcriptional
                     activator, which cooperates with nuclear hormone...;
                     cd05516"
                     /db_xref="CDD:99947"
     Site            order(1488,1493,1496,1535,1539,1545)
                     /site_type="active"
                     /note="acetyllysine binding site [active]"
                     /db_xref="CDD:99947"
     CDS             1..1646
                     /gene="SMARCA4"
                     /gene_synonym="BAF190; BAF190A; BRG1; CSS4; hSNF2b; MRD16;
                     OTSC12; RTPS2; SNF2; SNF2-beta; SNF2L4; SNF2LB; SWI2"
                     /coded_by="NM_001411150.1:174..5114"
                     /note="isoform G is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS92517.1"
                     /db_xref="GeneID:6597"
                     /db_xref="HGNC:HGNC:11100"
                     /db_xref="MIM:603254"
ORIGIN      
        1 mstpdpplgg tprpgpspgp gpspgamlgp spgpspgsah smmgpspgpp saghpiptqg
       61 pggypqdnmh qmhkpmesmh ekgmsddpry nqmkgmgmrs gghagmgppp spmdqhsqgy
      121 psplggseha sspvpasgps sgpqmssgpg gapldgadpq algqqnrgpt pfnqnqlhql
      181 raqimaykml argqplpdhl qmavqgkrpm pgmqqqmptl pppsvsatgp gpgpgpgpgp
      241 gpgpappnys rphgmggpnm pppgpsgvpp gmpgqppggp pkpwpegpma naaaptstpq
      301 klippqptgr pspappavpp aaspvmppqt qspgqpaqpa pmvplhqkqs ritpiqkprg
      361 ldpveilqer eyrlqariah riqelenlpg slagdlrtka tielkalrll nfqrqlrqev
      421 vvcmrrdtal etalnakayk rskrqslrea riteklekqq kieqerkrrq khqeylnsil
      481 qhakdfkeyh rsvtgkiqkl tkavatyhan tereqkkene riekermrrl maedeegyrk
      541 lidqkkdkrl ayllqqtdey vanltelvrq hkaaqvakek kkkkkkkkae naegqtpaig
      601 pdgepldets qmsdlpvkvi hvesgkiltg tdapkagqle awlemnpgye vaprsdsees
      661 gseeeeeeee eeqpqaaqpp tlpveekkki pdpdsddvse vdarhiiena kqdvddeygv
      721 sqalarglqs yyavahavte rvdkqsalmv ngvlkqyqik glewlvslyn nnlngilade
      781 mglgktiqti alitylmehk ringpfliiv plstlsnway efdkwapsvv kvsykgspaa
      841 rrafvpqlrs gkfnvlltty eyiikdkhil akirwkymiv deghrmknhh ckltqvlnth
      901 yvaprrlllt gtplqnklpe lwallnfllp tifkscstfe qwfnapfamt gekvdlneee
      961 tiliirrlhk vlrpfllrrl kkeveaqlpe kveyvikcdm salqrvlyrh mqakgvlltd
     1021 gsekdkkgkg gtktlmntim qlrkicnhpy mfqhieesfs ehlgftggiv qgldlyrasg
     1081 kfelldrilp klratnhkvl lfcqmtslmt imedyfayrg fkylrldgtt kaedrgmllk
     1141 tfnepgseyf ifllstragg lglnlqsadt viifdsdwnp hqdlqaqdra hrigqqnevr
     1201 vlrlctvnsv eekilaaaky klnvdqkviq agmfdqksss herraflqai leheeqdeee
     1261 devpddetvn qmiarheeef dlfmrmdldr rreearnpkr kprlmeedel pswiikddae
     1321 verltceeee ekmfgrgsrh rkevdysdsl tekqwlkkit gkdihdtass varglqfqrg
     1381 lqfctraska ieegtleeie eevrqkkssr krkrdsdags stpttstrsr dkddeskkqk
     1441 krgrppaekl spnppnltkk mkkivdavik ykdsssgrql sevfiqlpsr kelpeyyeli
     1501 rkpvdfkkik erirnhkyrs lndlekdvml lcqnaqtfnl egsliyedsi vlqsvftsvr
     1561 qkiekeddse geeseeeeeg eeegsesesr svkvkiklgr kekaqdrlkg grrrpsrgsr
     1621 akpvvsddds eeeqeedrsg sgseed
//
LOCUS       NP_001394738            1227 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 6 precursor
            [Homo sapiens].
ACCESSION   NP_001394738
VERSION     NP_001394738.1
DBSOURCE    REFSEQ: accession NM_001407809.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1227)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1227)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1227)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1227)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1227)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1227)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1227)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1227)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1227)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1227)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3031215.1,
                                           SRR14038197.1369857.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1227
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1227
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 6 precursor"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=134190
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O00411.2)"
                     /calculated_mol_wt=4109
     Region          18..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          95..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          261..290
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          296..323
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          432..701
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          728..747
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          799..1227
                     /region_name="Mediates interaction with TEFM.
                     /evidence=ECO:0000269|PubMed:21278163"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          828..1227
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1227
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407809.1:26..3709"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 msalcwgrga aglkralrpc grpglpgkeg taggvcgprr sssaspqeqd qdrrkdwghv
       61 ellevlqarv rqlqaesvse vvvnrvdvar lpecgsgdgs lqpprkvqmg akdatpvpcg
      121 rwakilekdk rtqqmrmqrl kaklqmpfqs gefkaltrrl qveprllskq magcledctr
      181 qapespweeq larllqeapg klsldveqap sgqhsqaqls gqqqrllaff kcclltdqlp
      241 lahhllvvhh gqrqkrkllt ldmynavmlg warqgafkel vyvlfmvkda gltpdllsya
      301 aalqcmgrqd qdagtiercl eqmsqeglkl qalftavlls eedratvlka vhkvkptfsl
      361 ppqlpppvnt skllrdvyak dgrvsypklh lplktlqclf ekqlhmelas rvcvvsvekp
      421 tlpskevkha rktlktlrdq wekalcralr etknrlerev yegrfslypf lcllderevv
      481 rmllqalpaq gesfttlare lsartfsrhv vqrqrvsgqv qalqnhyrky lcllasdaev
      541 pepclprqyw eelgapealr eqpwplpvqm elgkllaeml vqatqmpcsl dkphrssrlv
      601 pvlyhvysfr nvqqigilkp hpayvqllek aaeptltfea vdvpmlcppl pwtsphsgaf
      661 llsptklmrt vegatqhqel letcpptalh galdaltqlg ncawrvngrv ldlvlqlfqa
      721 kgcpqlgvpa ppseapqppe ahlphsaapa rkaelrrela hcqkvaremh slraealyrl
      781 slaqhlrdrv fwlphnmdfr grtypcpphf nhlgsdvara llefaqgrpl gphgldwlki
      841 hlvnltglkk replrkrlaf aeevmddild sadqpltgrk wwmgaeepwq tlaccmevan
      901 avrasdpaay vshlpvhqdg scnglqhyaa lgrdsvgaas vnlepsdvpq dvysgvaaqv
      961 evfrrqdaqr gmrvaqvleg fitrkvvkqt vmtvvygvtr yggrlqiekr lrelsdfpqe
     1021 fvweashylv rqvfkslqem fsgtraiqhw ltesarlish mgsvvewvtp lgvpviqpyr
     1081 ldskvkqigg giqsitythn gdisrkpntr kqkngfppnf ihsldsshmm ltalhcyrkg
     1141 ltfvsvhdcy wthaadvsvm nqvcreqfvr lhsepilqdl srflvkrfcs epqkileasq
     1201 lketlqavpk pgafdleqvk rstyffs
//
LOCUS       NP_001393526            1163 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 3 [Homo sapiens].
ACCESSION   NP_001393526 XP_016870587
VERSION     NP_001393526.1
DBSOURCE    REFSEQ: accession NM_001406597.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1163)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1163)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1163)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1163)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1163)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1163)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1163)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1163)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1163)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1163)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            On May 18, 2022 this sequence version replaced XP_016870587.1.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3237260.1,
                                           SRR14038191.2761147.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1163
                     /product="hamartin isoform 3"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=129565
     Region          7..718
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          402..786
                     /region_name="Mediates interaction with WDR45B.
                     /evidence=ECO:0000269|PubMed:28561066"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Region          438..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <707..>959
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1005..1084
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1099
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1130..1163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1163
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406597.1:189..3680"
                     /note="isoform 3 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS87703.1"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt ggkgtplgtp atspppaplc hsddyvhisl pqatvtpprk
      421 eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed siekdkeeaa
      481 isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv npeplhssld
      541 klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp trvgfgsgqp
      601 ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr liqqgadahs
      661 kelnklplps ksvdwthfgg sppsdeirtl rdqllllhnq llyerfkrqq halrnrrllr
      721 kvikaaalee hnaamkdqlk lqekdiqmwk vslqkeqary nqlqeqrdtm vtklhsqirq
      781 lqhdreefyn qsqelqtkle dcrnmiaelr ielkkannkv chtelllsqv sqklsnsesv
      841 qqqmeflnrq llvlgevnel yleqlqnkhs dttkevemmk aayrkelekn rshvlqqtqr
      901 ldtsqkrile leshlakkdh llleqkkyle dvklqargql qaaesryeaq kritqvfele
      961 ildlygrlek dgllkkleee kaeaaeaaee rldccndgcs dsmvghneea sghngetktp
     1021 rpssargssg srggggssss sselstpekp phqragpfss rwettmgeas asipttvgsl
     1081 pssksflgmk arelfrnkse sqcdedgmts slseslktel gkdlgveaki plnldgphps
     1141 pptpdsvgql himdynethh ehs
//
LOCUS       NP_001398074            1518 aa            linear   PRI 21-NOV-2025
DEFINITION  WD repeat-containing protein 62 isoform 3 [Homo sapiens].
ACCESSION   NP_001398074 XP_011525139
VERSION     NP_001398074.1
DBSOURCE    REFSEQ: accession NM_001411145.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1518)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1518)
  AUTHORS   Aslam,K., Saeed,A., Saeed,H.I., Bashir,R., Abid,H., Akhtar,R.,
            Habib,N., Khan,R., Asif,R., Rafiq,S., Asif,M., Makhdoom,E.U.H.,
            Hussain,M.S., Baig,S.M. and Anjum,I.
  TITLE     Molecular genetics, neuroimaging outcomes, and structural analyses
            of novel and recurrent variants of WDR62 gene in two consanguineous
            Pakistani families with autosomal recessive primary microcephaly
  JOURNAL   Mol Biol Rep 51 (1), 783 (2024)
   PUBMED   38926176
  REMARK    GeneRIF: Molecular genetics, neuroimaging outcomes, and structural
            analyses of novel and recurrent variants of WDR62 gene in two
            consanguineous Pakistani families with autosomal recessive primary
            microcephaly.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1518)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1518)
  AUTHORS   Hao,L., Ma,J., Wu,F., Ma,X., Qian,M., Sheng,W., Yan,T., Tang,N.,
            Jiang,X., Zhang,B., Xiao,D., Qian,Y., Zhang,J., Jiang,N., Zhou,W.,
            Chen,W., Ma,D. and Huang,G.
  TITLE     WDR62 variants contribute to congenital heart disease by inhibiting
            cardiomyocyte proliferation
  JOURNAL   Clin Transl Med 12 (7), e941 (2022)
   PUBMED   35808830
  REMARK    GeneRIF: WDR62 variants contribute to congenital heart disease by
            inhibiting cardiomyocyte proliferation.
REFERENCE   5  (residues 1 to 1518)
  AUTHORS   Wasserman,T., Katsenelson,K., Daniliuc,S., Hasin,T., Choder,M. and
            Aronheim,A.
  TITLE     A novel c-Jun N-terminal kinase (JNK)-binding protein WDR62 is
            recruited to stress granules and mediates a nonclassical JNK
            activation
  JOURNAL   Mol Biol Cell 21 (1), 117-130 (2010)
   PUBMED   19910486
  REMARK    GeneRIF: JNK and WDR62 may regulate the dynamic interplay between
            polysomes stress granule and processing bodies, thereby mediating
            mRNA fate after stress.
REFERENCE   6  (residues 1 to 1518)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   7  (residues 1 to 1518)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1518)
  AUTHORS   Roberts,E., Jackson,A.P., Carradice,A.C., Deeble,V.J., Mannan,J.,
            Rashid,Y., Jafri,H., McHale,D.P., Markham,A.F., Lench,N.J. and
            Woods,C.G.
  TITLE     The second locus for autosomal recessive primary microcephaly
            (MCPH2) maps to chromosome 19q13.1-13.2
  JOURNAL   Eur J Hum Genet 7 (7), 815-820 (1999)
   PUBMED   10573015
REFERENCE   9  (residues 1 to 1518)
  AUTHORS   Verloes,A., Ruaud,L., Drunat,S. and Passemard,S.
  TITLE     WDR62 Primary Microcephaly
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   35188728
REFERENCE   10 (residues 1 to 1518)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AD000813.1 and AC004144.1.
            
            On Aug 22, 2022 this sequence version replaced XP_011525139.1.
            
            Summary: This gene is proposed to play a role in cerebral cortical
            development. Mutations in this gene have been associated with
            microencephaly, cortical malformations, and cognitive disability.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.323791.1,
                                           SRR14038193.1918016.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1518
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..1518
                     /product="WD repeat-containing protein 62 isoform 3"
                     /note="microcephaly, primary autosomal recessive 2; WD
                     repeat-containing protein 62"
                     /calculated_mol_wt=165749
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Region          <93..439
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          109..150
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Region          114..153
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          153..194
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Region          159..197
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          196..234
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Region          201..239
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          270..332
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          291..330
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Region          339..739
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          339..394
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          352..391
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Region          397..445
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Region          402..437
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          485..524
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Region          493..527
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Region          527..569
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Region          533..573
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          573..613
                     /region_name="WD 9"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Region          578..615
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          621..660
                     /region_name="WD 10"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Region          627..662
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          666..708
                     /region_name="WD 11"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Region          671..707
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          709..747
                     /region_name="WD 12"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Region          757..819
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Region          798..841
                     /region_name="WD 13"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Region          903..930
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Site            939
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3U3T8; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Region          957..1050
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Site            1048
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Site            1065
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Site            1093
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Site            1101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Site            1123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Region          1132..1173
                     /region_name="WD 14"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Site            1144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Region          <1165..1408
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1228
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Site            1248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Site            1249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Region          1255..1293
                     /region_name="WD 15"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     Site            1268
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O43379.4)"
     Region          1339..1377
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43379.4)"
     CDS             1..1518
                     /gene="WDR62"
                     /gene_synonym="C19orf14; MCPH2"
                     /coded_by="NM_001411145.1:76..4632"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92603.1"
                     /db_xref="GeneID:284403"
                     /db_xref="HGNC:HGNC:24502"
                     /db_xref="MIM:613583"
ORIGIN      
        1 maavgsggya rndageklps vmagvparrg qsspppappi clrrrtrlst aseetvqnrv
       61 slekvlgita qnssgltcdp gtghvaylag cvvvildpke nkqqhifnta rkslsalafs
      121 pdgkyivtge nghrpavriw dveeknqvae mlghkygvac vafspnmkhi vsmgyqhdmv
      181 lnvwdwkkdi vvasnkvscr vialsfseds syfvtvgnrh vrfwflevst etkvtstvpl
      241 vgrsgilgel hnnifcgvac grgrmagstf cvsysgllcq fnekrvlekw inlkvslssc
      301 lcvsqelifc gctdgivrif qahslhylan lpkphylgvd vaqgleprka eavypdtval
      361 tfdpihqwls cvykdhsiyi wdvkdinrvg kvwselfhss yvwnvevype fedqraclps
      421 gsfltcssdn tirfwnldss pdshwqknif sntllkvvyv endiqhlqdm shfpdrgsen
      481 gtpmdvkagv rvmqvspdgq hlasgdrsgn lrihelhfmd elvkveahda evlcleyskp
      541 etgltllasa srdrlihvln veknynleqt lddhsssita ikfagnrdiq miscgadksi
      601 yfrsaqqgsd glhfvrthhv aekttlydmd iditqkyvav acqdrnvrvy ntvngkqkkc
      661 ykgsqgdegs llkvhvdpsg tflatscsdk sisvidfysg eciakmfghs eiitsmkfty
      721 dchhlitvsg dscvfiwhlg peitncmkqh lleidhrqqq qhtndkkrsg hprqdtyvst
      781 pseihslspg eqteddleee cepeemlktp skdsldpdpr clltngklpl wakrllgddd
      841 vadglafhak rsyqphgrwa eragqeplkt ildaqdldcy ftpmkpesle nsildslepq
      901 slasllsese spqeagrghp sflpqqkess easelilysl eaevtvtgtd sqycrkevea
      961 gpgdqqgdsy lrvssdspkd qsppedsges eadlecsfaa ihspapppdp aprfatslph
     1021 fpgcagpted elslpegpsv pssslpqtpe qekflrhhfe tltespcrel fpaalgdvea
     1081 seaedhffnp rlsistqfls slqkasrfth tfppratqcl vkspevklmd rggsqpragt
     1141 gyaspdrthv laagkaeetl eawrppppcl tslascvpas svlptdrnlp tptsaptpgl
     1201 aqgvhapstc symeatassr arisrsislg dsegpivatl aqplrrpssv gelaslgqel
     1261 qaittattps ldsegqepal rswgnheara nlrltlssac dgllqppvdt qpgvtvpavs
     1321 fpapspvees alrlhgsafr pslpapespg lpahpsnpql pearpgipgg taslleptsg
     1381 algllqgspa rwsepwvpve alppsplels rvgnilhrlq ttfqealdly rvlvssgqvd
     1441 tgqqqartel vstflwihsq leaeclvgts vapaqalpsp gppspptlyp laspdlqall
     1501 ehysellvqa vrrkargh
//
LOCUS       NP_001428097             688 aa            linear   PRI 21-NOV-2025
DEFINITION  PHD finger protein 21A isoform e [Homo sapiens].
ACCESSION   NP_001428097 XP_011518460 XP_054225039
VERSION     NP_001428097.1
DBSOURCE    REFSEQ: accession NM_001441168.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Mustafa,S., Abbas,S., Mahmood,A., Khan,A.Z., Zeb,S., Khan,A. and
            Umair,M.
  TITLE     A novel de novo variant in the PHF21A causes craniofacial
            abnormalities, intellectual disability and skeletal manifestations
  JOURNAL   Clin Genet 104 (1), 142-144 (2023)
   PUBMED   36843358
  REMARK    GeneRIF: A novel de novo variant in the PHF21A causes craniofacial
            abnormalities, intellectual disability and skeletal manifestations.
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Huang,J.Q., Ji,L.C., Jing,Q.A., He,Y.C., Ma,Y.Y. and Tong,X.M.
  TITLE     PHF21A expression as a biomarker of hepatocellular carcinoma
            progression and prognosis
  JOURNAL   Neoplasma 69 (6), 1349-1358 (2022)
   PUBMED   36305691
  REMARK    GeneRIF: PHF21A expression as a biomarker of hepatocellular
            carcinoma progression and prognosis.
REFERENCE   4  (residues 1 to 688)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 688)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 688)
  AUTHORS   Hailesellasse Sene,K., Porter,C.J., Palidwor,G., Perez-Iratxeta,C.,
            Muro,E.M., Campbell,P.A., Rudnicki,M.A. and Andrade-Navarro,M.A.
  TITLE     Gene function in early mouse embryonic stem cell differentiation
  JOURNAL   BMC Genomics 8, 85 (2007)
   PUBMED   17394647
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 688)
  AUTHORS   Shi,Y.J., Matson,C., Lan,F., Iwase,S., Baba,T. and Shi,Y.
  TITLE     Regulation of LSD1 histone demethylase activity by its associated
            factors
  JOURNAL   Mol Cell 19 (6), 857-864 (2005)
   PUBMED   16140033
REFERENCE   8  (residues 1 to 688)
  AUTHORS   Iwase,S., Januma,A., Miyamoto,K., Shono,N., Honda,A., Yanagisawa,J.
            and Baba,T.
  TITLE     Characterization of BHC80 in BRAF-HDAC complex, involved in
            neuron-specific gene repression
  JOURNAL   Biochem Biophys Res Commun 322 (2), 601-608 (2004)
   PUBMED   15325272
  REMARK    GeneRIF: Presumably serves as a scaffold protein in BHC in neuronal
            as well as non-neuronal cells. Possible role in spermatogenesis.
REFERENCE   9  (residues 1 to 688)
  AUTHORS   Hakimi,M.A., Dong,Y., Lane,W.S., Speicher,D.W. and Shiekhattar,R.
  TITLE     A candidate X-linked mental retardation gene is a component of a
            new family of histone deacetylase-containing complexes
  JOURNAL   J Biol Chem 278 (9), 7234-7239 (2003)
   PUBMED   12493763
REFERENCE   10 (residues 1 to 688)
  AUTHORS   Hakimi,M.A., Bochar,D.A., Chenoweth,J., Lane,W.S., Mandel,G. and
            Shiekhattar,R.
  TITLE     A core-BRAF35 complex containing histone deacetylase mediates
            repression of neuronal-specific genes
  JOURNAL   Proc Natl Acad Sci U S A 99 (11), 7420-7425 (2002)
   PUBMED   12032298
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC024475.15 and AC068385.9.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_011518460.1, XP_054225039.1.
            
            Summary: The PHF21A gene encodes BHC80, a component of a BRAF35
            (MIM 605535)/histone deacetylase (HDAC; see MIM 601241) complex
            (BHC) that mediates repression of neuron-specific genes through the
            cis-regulatory element known as repressor element-1 (RE1) or neural
            restrictive silencer (NRS) (Hakimi et al., 2002 [PubMed
            12032298]).[supplied by OMIM, Nov 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038194.3982457.1,
                                    SRR14038193.1918468.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..688
                     /product="PHD finger protein 21A isoform e"
                     /note="BRAF35/HDAC2 complex (80 kDa); BHC80a; BRAF35-HDAC
                     complex protein BHC80"
                     /calculated_mol_wt=75701
     Region          89..125
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          326..371
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          <382..544
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          448..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96BD5.1)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          494..688
                     /region_name="Required for transcriptional repression"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          498..540
                     /region_name="PHD_PHF21A"
                     /note="PHD finger found in PHD finger protein 21A
                     (PHF21A); cd15523"
                     /db_xref="CDD:276998"
     Site            order(498,505..510,530..533,535)
                     /site_type="other"
                     /note="histone H3 binding site [polypeptide binding]"
                     /db_xref="CDD:276998"
     Region          647..688
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     CDS             1..688
                     /gene="PHF21A"
                     /gene_synonym="BHC80; BM-006; IDDBCS; NEDMS"
                     /coded_by="NM_001441168.1:757..2823"
                     /note="isoform e is encoded by transcript variant 14"
                     /db_xref="GeneID:51317"
                     /db_xref="HGNC:HGNC:24156"
                     /db_xref="MIM:608325"
ORIGIN      
        1 melqtlqeal kveiqvhqkl vaqmkqdpqi fflsnqnadl kkqlhelqak italsekqkr
       61 vveqlrknli vkqeqpdkfq iqplpqsenk lqtaqqqplq qlqqqqqyhh hhaqqsaaas
      121 pnltasqktv ttasmittkt lplvlkaata tmpasvvgqr ptiamvtain sqkavlstdv
      181 qntpvnlqts skvtgpgaea vqivakntvt lqvqatppqp ikvpqfippp rltprpnflp
      241 qvrpkpvaqn nipiapappp mlaapqliqr pvmltkftpt tlptsqnsih pvrvvngqta
      301 tiaktfpmaq ltsiviatpg trlagpqtvq lskpslekqt vkshtetdek qtesrtitpp
      361 aapkpkreen pqklafmvsl glvthdhlee iqskrqerkr rttanpvysg avfeperkks
      421 avtylnstmh pgtrkrgrpp kynavlgfga ltptspqssh pdspenekte ttftfpapvq
      481 pvslpsptst dgdihedfcs vcrksgqllm cdtcsrvyhl dcldpplkti pkgmwicprc
      541 qdqmlkkeea ipwpgtlaiv hsyiaykaak eeekqkllkw ssdlkqereq leqkvkqlsn
      601 siskcmemkn tilarqkemh sslekvkqli rlihgidlsk pvdseatvga isngpdctpp
      661 anaatstpap spssqsctan cnqgeetk
//
LOCUS       NP_001425612             893 aa            linear   PRI 21-NOV-2025
DEFINITION  splicing regulator ARVCF isoform 2 [Homo sapiens].
ACCESSION   NP_001425612 XP_047297329 XP_054181612
VERSION     NP_001425612.1
DBSOURCE    REFSEQ: accession NM_001438683.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 893)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 893)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 893)
  AUTHORS   Suzuki,N., Idogawa,M., Tange,S., Ohashi,T., Sasaki,Y., Nakase,H.
            and Tokino,T.
  TITLE     p53-induced ARVCF modulates the splicing landscape and supports the
            tumor suppressive function of p53
  JOURNAL   Oncogene 39 (10), 2202-2211 (2020)
   PUBMED   31827232
  REMARK    GeneRIF: p53-induced ARVCF modulates the splicing landscape and
            supports the tumor suppressive function of p53.
REFERENCE   5  (residues 1 to 893)
  AUTHORS   Zhang,D., Tang,N., Liu,Y. and Wang,E.H.
  TITLE     ARVCF expression is significantly correlated with the malignant
            phenotype of non-small cell lung cancer
  JOURNAL   Mol Carcinog 54 Suppl 1, E185-E191 (2015)
   PUBMED   25683624
  REMARK    GeneRIF: observed ARVCF-dependent changes in small GTPase (mainly
            RhoA) activity in lung cancer cells. We confirmed that ARVCF plays
            an important role in the malignant phenotype
REFERENCE   6  (residues 1 to 893)
  AUTHORS   Mariner,D.J., Wang,J. and Reynolds,A.B.
  TITLE     ARVCF localizes to the nucleus and adherens junction and is
            mutually exclusive with p120(ctn) in E-cadherin complexes
  JOURNAL   J Cell Sci 113 (Pt 8), 1481-1490 (2000)
   PUBMED   10725230
REFERENCE   7  (residues 1 to 893)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   8  (residues 1 to 893)
  AUTHORS   Sirotkin,H., Morrow,B., Saint-Jore,B., Puech,A., Das Gupta,R.,
            Patanjali,S.R., Skoultchi,A., Weissman,S.M. and Kucherlapati,R.
  TITLE     Identification, characterization, and precise mapping of a human
            gene encoding a novel membrane-spanning protein from the 22q11
            region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 42 (2), 245-251 (1997)
   PUBMED   9192844
REFERENCE   9  (residues 1 to 893)
  AUTHORS   Sirotkin,H., O'Donnell,H., DasGupta,R., Halford,S., St Jore,B.,
            Puech,A., Parimoo,S., Morrow,B., Skoultchi,A., Weissman,S.M.,
            Scambler,P. and Kucherlapati,R.
  TITLE     Identification of a new human catenin gene family member (ARVCF)
            from the region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 41 (1), 75-83 (1997)
   PUBMED   9126485
REFERENCE   10 (residues 1 to 893)
  AUTHORS   Lindsay,E.A., Goldberg,R., Jurecic,V., Morrow,B., Carlson,C.,
            Kucherlapati,R.S., Shprintzen,R.J. and Baldini,A.
  TITLE     Velo-cardio-facial syndrome: frequency and extent of 22q11
            deletions
  JOURNAL   Am J Med Genet 57 (3), 514-522 (1995)
   PUBMED   7677167
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005663.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047297329.1, XP_054181612.1.
            
            Summary: Armadillo Repeat gene deleted in Velo-Cardio-Facial
            syndrome (ARVCF) is a member of the catenin family. This family
            plays an important role in the formation of adherens junction
            complexes, which are thought to facilitate communication between
            the inside and outside environments of a cell. The ARVCF gene was
            isolated in the search for the genetic defect responsible for the
            autosomal dominant Velo-Cardio-Facial syndrome (VCFS), a relatively
            common human disorder with phenotypic features including cleft
            palate, conotruncal heart defects and facial dysmorphology. The
            ARVCF gene encodes a protein containing two motifs, a coiled coil
            domain in the N-terminus and a 10 armadillo repeat sequence in the
            midregion. Since these sequences can facilitate protein-protein
            interactions ARVCF is thought to function in a protein complex. In
            addition, ARVCF contains a predicted nuclear-targeting sequence
            suggesting that it may have a function as a nuclear protein.
            [provided by RefSeq, Jun 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2347982.1,
                                           SRR18074968.3261932.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..893
                     /product="splicing regulator ARVCF isoform 2"
                     /note="armadillo repeat protein deleted in
                     velo-cardio-facial syndrome; armadillo repeat gene deleted
                     in velocardiofacial syndrome; splicing regulator ARVCF"
                     /calculated_mol_wt=96697
     Region          297..322
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(313,317,321,355,359,363,398,403,407)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          326..365
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          330..366
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          369..410
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          373..408
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          415..466
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          587..623
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          587..623
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          633..668
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          633..667
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          674..719
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          725..757
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     CDS             1..893
                     /gene="ARVCF"
                     /coded_by="NM_001438683.1:104..2785"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:421"
                     /db_xref="HGNC:HGNC:728"
                     /db_xref="MIM:602269"
ORIGIN      
        1 mpaelrqeqs pgsqaslatm peapdvleet vtveedpgtp tshvsivtse dgttrrtetk
       61 vtktvktvtt rtvrqvpvgp dglplldggp plgpfadgal drhfllrggg pvatlsrayl
      121 ssgggfpegp eprdspsygs lsrglgmrpp ragplgpgpg dgcftlpghr eafpvgpepg
      181 ppggrslper fqaepygled dtrslaadde ggpelepdyg tatrrrpecg rglhtrayed
      241 taddggelad erpafpmvta plaqpergsm gsldrlvrrs psvdsarkep rwrdpelpev
      301 lamlrhpvdp vkanaaaylq hlcfenegvk rrvrqlrglp llvalldhpr aevrrracga
      361 lrnlsygrdt dnkaairdcg gvpalvrllr aardnevrel vtgtlwnlss yeplkmviid
      421 hglqtlthev ivphsgwere pnedskprda ewttvfknts gclrnvssdg aearrrlrec
      481 eglvdallha lqsavgrkdt dnksvencvc imrnlsyhvh kevpgadryq eaepgplgsa
      541 vgsqrrrrdd ascfggkkak gkkdgemdrn fdtldlpkrt eaakgfelly qpevvrlyls
      601 lltesrnfnt leaaagalqn lsagnwmwat yiratvrker glpvlvellq setdkvvrav
      661 aialrnlsld rrnkdligsy amaelvrnvr naqapprpga cleedtvvav lntiheivsd
      721 sldnarsllq argvpalval vassqsvrea kaashvlqtv wsykelrgtl qkdgwtkarf
      781 qsaaatakgp kgalspggfd dstlplvdks legektgsrd vipmdalgpd gystvdrrer
      841 rprgassage asekeplkld psrkapppgp srpavrlvda vgdakpqpvd swv
//
LOCUS       NP_001394116             134 aa            linear   PRI 21-NOV-2025
DEFINITION  sodium channel protein type 5 subunit alpha isoform j [Homo
            sapiens].
ACCESSION   NP_001394116
VERSION     NP_001394116.1
DBSOURCE    REFSEQ: accession NM_001407187.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Hu,Y., Zhang,C., Wang,S., Xiong,H., Xie,W., Zeng,Z., Cai,H.,
            Wang,Q.K. and Lu,Z.
  TITLE     14-3-3epsilon/YWHAE regulates the transcriptional expression of
            cardiac sodium channel NaV1.5
  JOURNAL   Heart Rhythm 21 (11), 2320-2329 (2024)
   PUBMED   38750908
  REMARK    GeneRIF: 14-3-3epsilon/YWHAE regulates the transcriptional
            expression of cardiac sodium channel NaV1.5.
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Cadena-Ullauri,S., Guevara-Ramirez,P., Ruiz-Pozo,V.A.,
            Tamayo-Trujillo,R., Paz-Cruz,E., Simancas-Racines,D.,
            Ibarra-Castillo,R., Laso-Bayas,J.L. and Zambrano,A.K.
  TITLE     Genomic analysis of an Ecuadorian individual carrying an SCN5A rare
            variant
  JOURNAL   BMC Cardiovasc Disord 24 (1), 388 (2024)
   PUBMED   39068398
  REMARK    GeneRIF: Genomic analysis of an Ecuadorian individual carrying an
            SCN5A rare variant.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Tariq,U., Sarkar,S., Malladi,N., Kumar,R., Bugga,P., Chakraborty,P.
            and Banerjee,S.K.
  TITLE     Knockdown of SCN5A alters metabolic-associated genes and aggravates
            hypertrophy in the cardiomyoblast
  JOURNAL   Mol Biol Rep 51 (1), 661 (2024)
   PUBMED   38758505
  REMARK    GeneRIF: Knockdown of SCN5A alters metabolic-associated genes and
            aggravates hypertrophy in the cardiomyoblast.
            Erratum:[Mol Biol Rep. 2024 Jul 26;51(1):852. doi:
            10.1007/s11033-024-09742-9. PMID: 39060789]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 134)
  AUTHORS   Wright,K.M., Nathan,S., Jiang,H., Xia,W., Kim,H., Chakouri,N.,
            Nwafor,J.N., Fossier,L., Srinivasan,L., Chen,Z., Boronina,T.,
            Post,J., Paul,S., Cole,R.N., Ben-Johny,M., Cole,P.A. and
            Gabelli,S.B.
  TITLE     NEDD4L intramolecular interactions regulate its auto and substrate
            NaV1.5 ubiquitination
  JOURNAL   J Biol Chem 300 (3), 105715 (2024)
   PUBMED   38309503
  REMARK    GeneRIF: NEDD4L intramolecular interactions regulate its auto and
            substrate NaV1.5 ubiquitination.
REFERENCE   5  (residues 1 to 134)
  AUTHORS   George,A.L. Jr., Varkony,T.A., Drabkin,H.A., Han,J., Knops,J.F.,
            Finley,W.H., Brown,G.B., Ward,D.C. and Haas,M.
  TITLE     Assignment of the human heart tetrodotoxin-resistant voltage-gated
            Na+ channel alpha-subunit gene (SCN5A) to band 3p21
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 67-70 (1995)
   PUBMED   7956363
REFERENCE   6  (residues 1 to 134)
  AUTHORS   Jiang,C., Atkinson,D., Towbin,J.A., Splawski,I., Lehmann,M.H.,
            Li,H., Timothy,K., Taggart,R.T., Schwartz,P.J., Vincent,G.M. et al.
  TITLE     Two long QT syndrome loci map to chromosomes 3 and 7 with evidence
            for further heterogeneity
  JOURNAL   Nat Genet 8 (2), 141-147 (1994)
   PUBMED   7842012
REFERENCE   7  (residues 1 to 134)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   8  (residues 1 to 134)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 134)
  AUTHORS   Groffen,A.J., Bikker,H. and Christiaans,I.
  TITLE     Long QT Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301308
REFERENCE   10 (residues 1 to 134)
  AUTHORS   Gellens,M.E., George,A.L. Jr., Chen,L.Q., Chahine,M., Horn,R.,
            Barchi,R.L. and Kallen,R.G.
  TITLE     Primary structure and functional expression of the human cardiac
            tetrodotoxin-insensitive voltage-dependent sodium channel
  JOURNAL   Proc Natl Acad Sci U S A 89 (2), 554-558 (1992)
   PUBMED   1309946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP006241.1.
            
            Summary: The protein encoded by this gene is an integral membrane
            protein and tetrodotoxin-resistant voltage-gated sodium channel
            subunit. This protein is found primarily in cardiac muscle and is
            responsible for the initial upstroke of the action potential in an
            electrocardiogram. Defects in this gene have been associated with
            long QT syndrome type 3 (LQT3), atrial fibrillation,
            cardiomyopathy, and Brugada syndrome 1, all autosomal dominant
            cardiac diseases. Alternative splicing results in several
            transcript variants encoding different isoforms. [provided by
            RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4368410.514418.1,
                                           SRR12921934.3666198.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465404, SAMN03465406
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.2"
     Protein         1..134
                     /product="sodium channel protein type 5 subunit alpha
                     isoform j"
                     /note="cardiac tetrodotoxin-insensitive voltage-dependent
                     sodium channel alpha subunit; sodium channel protein type
                     5 subunit alpha; voltage-gated sodium channel subunit
                     alpha Nav1.5; sodium channel protein cardiac muscle
                     subunit alpha; sodium channel, voltage-gated, type V,
                     alpha subunit"
                     /calculated_mol_wt=14951
     Region          28..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     CDS             1..134
                     /gene="SCN5A"
                     /gene_synonym="CDCD2; CMD1E; CMPD2; HB1; HB2; HBBD; HH1;
                     ICCD; IVF; LQT3; Nav1.5; PFHB1; SSS1; VF1"
                     /coded_by="NM_001407187.1:210..614"
                     /note="isoform j is encoded by transcript variant 10"
                     /db_xref="GeneID:6331"
                     /db_xref="HGNC:HGNC:10593"
                     /db_xref="MIM:600163"
ORIGIN      
        1 manfllprgt ssfrrftres laaiekrmae kqargsttlq esreglpeee aprpqldlqa
       61 skklpdlygn ppqeligepl edldpfystq kvttthlqpc lpfcatplsm eqrgkrawpp
      121 ygalfrvahe algk
//
LOCUS       NP_001425622             924 aa            linear   PRI 21-NOV-2025
DEFINITION  splicing regulator ARVCF isoform 7 [Homo sapiens].
ACCESSION   NP_001425622 XP_047297327 XP_054181609
VERSION     NP_001425622.1
DBSOURCE    REFSEQ: accession NM_001438693.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 924)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 924)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 924)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 924)
  AUTHORS   Suzuki,N., Idogawa,M., Tange,S., Ohashi,T., Sasaki,Y., Nakase,H.
            and Tokino,T.
  TITLE     p53-induced ARVCF modulates the splicing landscape and supports the
            tumor suppressive function of p53
  JOURNAL   Oncogene 39 (10), 2202-2211 (2020)
   PUBMED   31827232
  REMARK    GeneRIF: p53-induced ARVCF modulates the splicing landscape and
            supports the tumor suppressive function of p53.
REFERENCE   5  (residues 1 to 924)
  AUTHORS   Zhang,D., Tang,N., Liu,Y. and Wang,E.H.
  TITLE     ARVCF expression is significantly correlated with the malignant
            phenotype of non-small cell lung cancer
  JOURNAL   Mol Carcinog 54 Suppl 1, E185-E191 (2015)
   PUBMED   25683624
  REMARK    GeneRIF: observed ARVCF-dependent changes in small GTPase (mainly
            RhoA) activity in lung cancer cells. We confirmed that ARVCF plays
            an important role in the malignant phenotype
REFERENCE   6  (residues 1 to 924)
  AUTHORS   Mariner,D.J., Wang,J. and Reynolds,A.B.
  TITLE     ARVCF localizes to the nucleus and adherens junction and is
            mutually exclusive with p120(ctn) in E-cadherin complexes
  JOURNAL   J Cell Sci 113 (Pt 8), 1481-1490 (2000)
   PUBMED   10725230
REFERENCE   7  (residues 1 to 924)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   8  (residues 1 to 924)
  AUTHORS   Sirotkin,H., Morrow,B., Saint-Jore,B., Puech,A., Das Gupta,R.,
            Patanjali,S.R., Skoultchi,A., Weissman,S.M. and Kucherlapati,R.
  TITLE     Identification, characterization, and precise mapping of a human
            gene encoding a novel membrane-spanning protein from the 22q11
            region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 42 (2), 245-251 (1997)
   PUBMED   9192844
REFERENCE   9  (residues 1 to 924)
  AUTHORS   Sirotkin,H., O'Donnell,H., DasGupta,R., Halford,S., St Jore,B.,
            Puech,A., Parimoo,S., Morrow,B., Skoultchi,A., Weissman,S.M.,
            Scambler,P. and Kucherlapati,R.
  TITLE     Identification of a new human catenin gene family member (ARVCF)
            from the region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 41 (1), 75-83 (1997)
   PUBMED   9126485
REFERENCE   10 (residues 1 to 924)
  AUTHORS   Lindsay,E.A., Goldberg,R., Jurecic,V., Morrow,B., Carlson,C.,
            Kucherlapati,R.S., Shprintzen,R.J. and Baldini,A.
  TITLE     Velo-cardio-facial syndrome: frequency and extent of 22q11
            deletions
  JOURNAL   Am J Med Genet 57 (3), 514-522 (1995)
   PUBMED   7677167
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005663.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047297327.1, XP_054181609.1.
            
            Summary: Armadillo Repeat gene deleted in Velo-Cardio-Facial
            syndrome (ARVCF) is a member of the catenin family. This family
            plays an important role in the formation of adherens junction
            complexes, which are thought to facilitate communication between
            the inside and outside environments of a cell. The ARVCF gene was
            isolated in the search for the genetic defect responsible for the
            autosomal dominant Velo-Cardio-Facial syndrome (VCFS), a relatively
            common human disorder with phenotypic features including cleft
            palate, conotruncal heart defects and facial dysmorphology. The
            ARVCF gene encodes a protein containing two motifs, a coiled coil
            domain in the N-terminus and a 10 armadillo repeat sequence in the
            midregion. Since these sequences can facilitate protein-protein
            interactions ARVCF is thought to function in a protein complex. In
            addition, ARVCF contains a predicted nuclear-targeting sequence
            suggesting that it may have a function as a nuclear protein.
            [provided by RefSeq, Jun 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1449883.1,
                                           SRR14038193.959699.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..924
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..924
                     /product="splicing regulator ARVCF isoform 7"
                     /note="armadillo repeat protein deleted in
                     velo-cardio-facial syndrome; armadillo repeat gene deleted
                     in velocardiofacial syndrome; splicing regulator ARVCF"
                     /calculated_mol_wt=100140
     Region          95..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            170
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P98203; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          186..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          266..290
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          348..387
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          360..385
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(376,380,384,418,422,426,461,466,470)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          389..428
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          390..429
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          393..429
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          432..473
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          433..467
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          436..471
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          468..508
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          478..529
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          526..565
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          590..614
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          635..675
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          645..681
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          645..681
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          688..727
                     /region_name="ARM 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          691..726
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          691..725
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          728..770
                     /region_name="ARM 9"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          732..777
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          783..815
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            853
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            860
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            861
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            904
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     CDS             1..924
                     /gene="ARVCF"
                     /coded_by="NM_001438693.1:308..3082"
                     /note="isoform 7 is encoded by transcript variant 8"
                     /db_xref="GeneID:421"
                     /db_xref="HGNC:HGNC:728"
                     /db_xref="MIM:602269"
ORIGIN      
        1 medcnvhsaa silasvkeqe arferltral eqerrhvalq leraqqpgmv sggmgsgqpl
       61 pmawqqlvlq eqspgsqasl atmpeapdvl eetvtveedp gtptshvsiv tsedgttrrt
      121 etkvtktvkt vttrtvrqvp vgpdglplld ggpplgpfad galdrhfllr gggpvatlsr
      181 aylssgggfp egpeprdsps ygslsrglgm rppragplgp gpgdgcftlp ghreafpvgp
      241 epgppggrsl perfqaepyg leddtrslaa ddeggpelep dygtatrrrp ecgrglhtra
      301 yedtaddgge laderpafpm vtaplaqper gsmgsldrlv rrspsvdsar keprwrdpel
      361 pevlamlrhp vdpvkanaaa ylqhlcfene gvkrrvrqlr glpllvalld hpraevrrra
      421 cgalrnlsyg rdtdnkaair dcggvpalvr llraardnev relvtgtlwn lssyeplkmv
      481 iidhglqtlt hevivphsgw erepnedskp rdaewttvfk ntsgclrnvs sdgaearrrl
      541 receglvdal lhalqsavgr kdtdnksven cvcimrnlsy hvhkevpgad ryqeaepgpl
      601 gsavgsqrrr rddascfggk kdgemdrnfd tldlpkrtea akgfellyqp evvrlylsll
      661 tesrnfntle aaagalqnls agnwmwatyi ratvrkergl pvlvellqse tdkvvravai
      721 alrnlsldrr nkdligsyam aelvrnvrna qapprpgacl eedtvvavln tiheivsdsl
      781 dnarsllqar gvpalvalva ssqsvreaka ashvlqtvws ykelrgtlqk dgwtkarfqs
      841 aaatakgpkg alspggfdds tlplvdksle gektgsrdvi pmdalgpdgy stvdrrerrp
      901 rgassageas ekeplkgpgp ascs
//
LOCUS       NP_001394382            2784 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform h [Homo sapiens].
ACCESSION   NP_001394382
VERSION     NP_001394382.1
DBSOURCE    REFSEQ: accession NM_001407453.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2784)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2784)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2784)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2784)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2784)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2784)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2784)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2784)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2784)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2784)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.982851.1,
                                           SRR14038191.3302606.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267761, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2784
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2784
                     /product="adenomatous polyposis coli protein isoform h"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=304856
     Region          68..148
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          281..333
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          334..407
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          406..449
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(440,444,448,483,487,491,527,531,535)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          453..494
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          457..494
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          501..536
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          544..585
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          590..630
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          594..628
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          632..672
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          636..672
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          673..960
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          977..1076
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1198..>1215
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1224..1309
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1232..1642
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1578..1601
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1603..1656
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1657..1678
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1687..1780
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1814..1888
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1974..1993
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2164..2509
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2611..2784
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2784
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407453.1:195..8549"
                     /note="isoform h is encoded by transcript variant 23"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 massgqidll erlkelnlds snfpgvklrs kmslrsygsr egsvssrsge cspvpmgsfp
       61 rrgfvngsre stgyleelek ersllladld keekekdwyy aqlqnltkri dslpltenfs
      121 lqtdmtrrql eyearqirva meeqlgtcqd mekraqrria riqqiekdil rirqllqsqa
      181 teaerssqnk hetgshdaer qnegqgvgei nmatsgngqg sttrmdheta svlssssths
      241 aprrltshlg tkvemvysll smlgthdkdd msrtllamss sqdscismrq sgclplliql
      301 lhgndkdsvl lgnsrgskea rarasaalhn iihsqpddkr grreirvlhl leqiraycet
      361 cwewqeahep gmdqdknpmp apvehqicpa vcvlmklsfd eehrhamnel gglqaiaell
      421 qvdcemyglt ndhysitlrr yagmaltnlt fgdvankatl csmkgcmral vaqlksesed
      481 lqqviasvlr nlswradvns kktlrevgsv kalmecalev kkestlksvl salwnlsahc
      541 tenkadicav dgalaflvgt ltyrsqtntl aiiesgggil rnvssliatn edhrqilren
      601 nclqtllqhl kshsltivsn acgtlwnlsa rnpkdqealw dmgavsmlkn lihskhkmia
      661 mgsaaalrnl manrpakykd animspgssl pslhvrkqka leaeldaqhl setfdnidnl
      721 spkashrskq rhkqslygdy vfdtnrhddn rsdnfntgnm tvlspylntt vlpsssssrg
      781 sldssrsekd rslerergig lgnyhpaten pgtsskrglq isttaaqiak vmeevsaiht
      841 sqedrssgst telhcvtder nalrrssaah thsntynftk sensnrtcsm pyakleykrs
      901 sndslnsvss sdgygkrgqm kpsiesysed deskfcsygq ypadlahkih sanhmddndg
      961 eldtpinysl kysdeqlnsg rqspsqnerw arpkhiiede ikqseqrqsr nqsttypvyt
     1021 estddkhlkf qphfgqqecv spyrsrgang setnrvgsnh ginqnvsqsl cqeddyeddk
     1081 ptnyseryse eeqheeeerp tnysikynee krhvdqpidy slkyatdips sqkqsfsfsk
     1141 sssgqsskte hmssssents tpssnakrqn qlhpssaqsr sgqpqkaatc kvssinqeti
     1201 qtycvedtpi cfsrcsslss lssaedeigc nqttqeadsa ntlqiaeike kigtrsaedp
     1261 vsevpavsqh prtkssrlqg sslssesarh kavefssgak spsksgaqtp ksppehyvqe
     1321 tplmfsrcts vssldsfesr siassvqsep csgmvsgiis psdlpdspgq tmppsrsktp
     1381 ppppqtaqtk revpknkapt aekresgpkq aavnaavqrv qvlpdadtll hfatestpdg
     1441 fscssslsal sldepfiqkd velrimppvq endngnetes eqpkesnenq ekeaektids
     1501 ekdllddsdd ddieileeci isamptkssr kakkpaqtas klpppvarkp sqlpvykllp
     1561 sqnrlqpqkh vsftpgddmp rvycvegtpi nfstatslsd ltiesppnel aagegvrgga
     1621 qsgefekrdt iptegrstde aqggktssvt ipelddnkae egdilaecin sampkgkshk
     1681 pfrvkkimdq vqqasasssa pnknqldgkk kkptspvkpi pqnteyrtrv rknadsknnl
     1741 naervfsdnk dskkqnlknn skvfndklpn nedrvrgsfa fdsphhytpi egtpycfsrn
     1801 dslssldfdd ddvdlsreka elrkakenke seakvtshte ltsnqqsank tqaiakqpin
     1861 rgqpkpilqk qstfpqsskd ipdrgaatde klqnfaient pvcfshnssl sslsdidqen
     1921 nnkenepike teppdsqgep skpqasgyap ksfhvedtpv cfsrnsslss lsidseddll
     1981 qecissampk kkkpsrlkgd nekhsprnmg gilgedltld lkdiqrpdse hglspdsenf
     2041 dwkaiqegan sivsslhqaa aaaclsrqas sdsdsilslk sgislgspfh ltpdqeekpf
     2101 tsnkgprilk pgekstletk kieseskgik ggkkvyksli tgkvrsnsei sgqmkqplqa
     2161 nmpsisrgrt mihipgvrns ssstspvskk gpplktpask spsegqtatt sprgakpsvk
     2221 selspvarqt sqiggsskap srsgsrdstp srpaqqplsr piqspgrnsi spgrngispp
     2281 nklsqlprts spstastkss gsgkmsytsp grqmsqqnlt kqtglsknas siprsesask
     2341 glnqmnngng ankkvelsrm sstkssgses drserpvlvr qstfikeaps ptlrrklees
     2401 asfeslspss rpasptrsqa qtpvlspslp dmslsthssv qaggwrklpp nlsptieynd
     2461 grpakrhdia rshsespsrl pinrsgtwkr ehskhssslp rvstwrrtgs sssilsasse
     2521 ssekaksede khvnsisgtk qskenqvsak gtwrkikene fsptnstsqt vssgatngae
     2581 sktliyqmap avsktedvwv riedcpinnp rsgrsptgnt ppvidsvsek anpnikdskd
     2641 nqakqnvgng svpmrtvgle nrlnsfiqvd apdqkgteik pgqnnpvpvs etnessiver
     2701 tpfssssssk hsspsgtvaa rvtpfnynps prkssadsts arpsqiptpv nnntkkrdsk
     2761 tdstessgtq spkrhsgsyl vtsv
//
LOCUS       NP_001394200             302 aa            linear   PRI 21-NOV-2025
DEFINITION  cellular tumor antigen p53 isoform i [Homo sapiens].
ACCESSION   NP_001394200
VERSION     NP_001394200.1
DBSOURCE    REFSEQ: accession NM_001407271.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Mirgayazova,R., Khadiullina,R., Chasov,V., Mingaleeva,R.,
            Miftakhova,R., Rizvanov,A. and Bulatov,E.
  TITLE     Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an Option?
  JOURNAL   Genes (Basel) 11 (6), 704 (2020)
   PUBMED   32630614
  REMARK    GeneRIF: Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an
            Option?
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Flynt,E., Bisht,K., Sridharan,V., Ortiz,M., Towfic,F. and
            Thakurta,A.
  TITLE     Prognosis, Biology, and Targeting of TP53 Dysregulation in Multiple
            Myeloma
  JOURNAL   Cells 9 (2), 287 (2020)
   PUBMED   31991614
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Barnoud,T., Parris,J.L.D. and Murphy,M.E.
  TITLE     Common genetic variants in the TP53 pathway and their impact on
            cancer
  JOURNAL   J Mol Cell Biol 11 (7), 578-585 (2019)
   PUBMED   31152665
  REMARK    GeneRIF: Common genetic variants in the TP53 pathway and their
            impact on cancer.
            Review article
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Hu,W., Chen,S., Thorne,R.F. and Wu,M.
  TITLE     TP53, TP53 Target Genes (DRAM, TIGAR), and Autophagy
  JOURNAL   Adv Exp Med Biol 1206, 127-149 (2019)
   PUBMED   31776983
  REMARK    Review article
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Baugh,E.H., Ke,H., Levine,A.J., Bonneau,R.A. and Chan,C.S.
  TITLE     Why are there hotspot mutations in the TP53 gene in human cancers?
  JOURNAL   Cell Death Differ 25 (1), 154-160 (2018)
   PUBMED   29099487
  REMARK    GeneRIF: TP53 missense mutant alleles that occur in human cancers
            are discussed in the context of high resolution models of these p53
            mutant protein structures to determine the structural features of
            mutations (review).
            Review article
REFERENCE   6  (residues 1 to 302)
  AUTHORS   Aubrey,B.J., Strasser,A. and Kelly,G.L.
  TITLE     Tumor-Suppressor Functions of the TP53 Pathway
  JOURNAL   Cold Spring Harb Perspect Med 6 (5), a026062 (2016)
   PUBMED   27141080
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 302)
  AUTHORS   Soussi,T. and Wiman,K.G.
  TITLE     TP53: an oncogene in disguise
  JOURNAL   Cell Death Differ 22 (8), 1239-1249 (2015)
   PUBMED   26024390
  REMARK    Review article
REFERENCE   8  (residues 1 to 302)
  AUTHORS   Soussi,T.
  TITLE     The TP53 gene network in a postgenomic era
  JOURNAL   Hum Mutat 35 (6), 641-642 (2014)
   PUBMED   24753184
  REMARK    GeneRIF: Recommendations and guidelines for reporting and
            annotating TP53 variants are also provided, to help researchers
            generate standardized data that are easy to understand, analyze,
            and exchange across various cancer variant databases
            Review article
REFERENCE   9  (residues 1 to 302)
  AUTHORS   Anczukow,O., Ware,M.D., Buisson,M., Zetoune,A.B.,
            Stoppa-Lyonnet,D., Sinilnikova,O.M. and Mazoyer,S.
  TITLE     Does the nonsense-mediated mRNA decay mechanism prevent the
            synthesis of truncated BRCA1, CHK2, and p53 proteins?
  JOURNAL   Hum Mutat 29 (1), 65-73 (2008)
   PUBMED   17694537
  REMARK    GeneRIF: the p53 protein encoded by the 770delT allele is as
            abundant as the wild-type protein, as removal of the C-terminal p53
            domain leads to a stabilized mutant protein, whose abundance is
            markedly increased when NMD is inhibited.
REFERENCE   10 (residues 1 to 302)
  AUTHORS   Bourdon,J.C.
  TITLE     p53 Family isoforms
  JOURNAL   Curr Pharm Biotechnol 8 (6), 332-336 (2007)
   PUBMED   18289041
  REMARK    Review article
REFERENCE   11 (residues 1 to 302)
  AUTHORS   Candeias,M.M., Powell,D.J., Roubalova,E., Apcher,S., Bourougaa,K.,
            Vojtesek,B., Bruzzoni-Giovanelli,H. and Fahraeus,R.
  TITLE     Expression of p53 and p53/47 are controlled by alternative
            mechanisms of messenger RNA translation initiation
  JOURNAL   Oncogene 25 (52), 6936-6947 (2006)
   PUBMED   16983332
  REMARK    GeneRIF: harbouring alternative translation initiation sites, the
            p53 mRNA gives rise to different levels of the p53 isoforms which
            help to orchestrate the cell biological outcome of p53 activation
REFERENCE   12 (residues 1 to 302)
  AUTHORS   Murray-Zmijewski,F., Lane,D.P. and Bourdon,J.C.
  TITLE     p53/p63/p73 isoforms: an orchestra of isoforms to harmonise cell
            differentiation and response to stress
  JOURNAL   Cell Death Differ 13 (6), 962-972 (2006)
   PUBMED   16601753
  REMARK    Review article
REFERENCE   13 (residues 1 to 302)
  AUTHORS   Bourdon,J.C., Fernandes,K., Murray-Zmijewski,F., Liu,G., Diot,A.,
            Xirodimas,D.P., Saville,M.K. and Lane,D.P.
  TITLE     p53 isoforms can regulate p53 transcriptional activity
  JOURNAL   Genes Dev 19 (18), 2122-2137 (2005)
   PUBMED   16131611
  REMARK    GeneRIF: p53 isoforms can regulate p53 transcriptional activity.
REFERENCE   14 (residues 1 to 302)
  AUTHORS   Ghosh,A., Stewart,D. and Matlashewski,G.
  TITLE     Regulation of human p53 activity and cell localization by
            alternative splicing
  JOURNAL   Mol Cell Biol 24 (18), 7987-7997 (2004)
   PUBMED   15340061
  REMARK    GeneRIF: mechanism of p53 regulation originating through
            alternative splicing of the human p53 gene resulting in the
            expression of a novel p53 mRNA
REFERENCE   15 (residues 1 to 302)
  AUTHORS   Flaman,J.M., Waridel,F., Estreicher,A., Vannier,A., Limacher,J.M.,
            Gilbert,D., Iggo,R. and Frebourg,T.
  TITLE     The human tumour suppressor gene p53 is alternatively spliced in
            normal cells
  JOURNAL   Oncogene 12 (4), 813-818 (1996)
   PUBMED   8632903
REFERENCE   16 (residues 1 to 302)
  AUTHORS   Schneider,K., Zelley,K., Nichols,K.E., Schwartz Levine,A. and
            Garber,J.
  TITLE     Li-Fraumeni Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301488
REFERENCE   17 (residues 1 to 302)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   18 (residues 1 to 302)
  AUTHORS   Lamb,P. and Crawford,L.
  TITLE     Characterization of the human p53 gene
  JOURNAL   Mol Cell Biol 6 (5), 1379-1385 (1986)
   PUBMED   2946935
REFERENCE   19 (residues 1 to 302)
  AUTHORS   Isobe,M., Emanuel,B.S., Givol,D., Oren,M. and Croce,C.M.
  TITLE     Localization of gene for human p53 tumour antigen to band 17p13
  JOURNAL   Nature 320 (6057), 84-85 (1986)
   PUBMED   3456488
REFERENCE   20 (residues 1 to 302)
  AUTHORS   Benchimol,S., Lamb,P., Crawford,L.V., Sheer,D., Shows,T.B.,
            Bruns,G.A. and Peacock,J.
  TITLE     Transformation associated p53 protein is encoded by a gene on human
            chromosome 17
  JOURNAL   Somat Cell Mol Genet 11 (5), 505-510 (1985)
   PUBMED   2994241
REFERENCE   21 (residues 1 to 302)
  AUTHORS   Harlow,E., Williamson,N.M., Ralston,R., Helfman,D.M. and Adams,T.E.
  TITLE     Molecular cloning and in vitro expression of a cDNA clone for human
            cellular tumor antigen p53
  JOURNAL   Mol Cell Biol 5 (7), 1601-1610 (1985)
   PUBMED   3894933
REFERENCE   22 (residues 1 to 302)
  AUTHORS   Zakut-Houri,R., Bienz-Tadmor,B., Givol,D. and Oren,M.
  TITLE     Human p53 cellular tumor antigen: cDNA sequence and expression in
            COS cells
  JOURNAL   EMBO J 4 (5), 1251-1255 (1985)
   PUBMED   4006916
REFERENCE   23 (residues 1 to 302)
  AUTHORS   Matlashewski,G., Lamb,P., Pim,D., Peacock,J., Crawford,L. and
            Benchimol,S.
  TITLE     Isolation and characterization of a human p53 cDNA clone:
            expression of the human p53 gene
  JOURNAL   EMBO J 3 (13), 3257-3262 (1984)
   PUBMED   6396087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087388.9 and AC007421.13.
            
            Summary: This gene encodes a tumor suppressor protein containing
            transcriptional activation, DNA binding, and oligomerization
            domains. The encoded protein responds to diverse cellular stresses
            to regulate expression of target genes, thereby inducing cell cycle
            arrest, apoptosis, senescence, DNA repair, or changes in
            metabolism. Mutations in this gene are associated with a variety of
            human cancers, including hereditary cancers such as Li-Fraumeni
            syndrome. Alternative splicing of this gene and the use of
            alternate promoters result in multiple transcript variants and
            isoforms. Additional isoforms have also been shown to result from
            the use of alternate translation initiation codons from identical
            transcript variants (PMIDs: 12032546, 20937277). [provided by
            RefSeq, Dec 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2758179.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:2946935)
            NMD candidate                    :: PMID: 16131611, 16601753,
                                                18289041
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..302
                     /product="cellular tumor antigen p53 isoform i"
                     /note="tumor protein 53; mutant tumor protein 53; cellular
                     tumor antigen p53; phosphoprotein p53;
                     transformation-related protein 53; antigen NY-CO-13; tumor
                     supressor p53"
                     /calculated_mol_wt=33362
     Region          1..20
                     /region_name="TAD2"
                     /note="Transactivation domain 2; pfam18521"
                     /db_xref="CDD:375947"
     Region          70..249
                     /region_name="P53"
                     /note="P53 DNA-binding domain; cd08367"
                     /db_xref="CDD:176262"
     Site            order(137,140,199,203)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:176262"
     Site            order(138..140,142)
                     /site_type="other"
                     /note="dimerization site [polypeptide binding]"
                     /db_xref="CDD:176262"
     Site            order(200,202,209,234,236..238,241)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176262"
     CDS             1..302
                     /gene="TP53"
                     /gene_synonym="BCC7; BMFS5; LFS1; P53; TRP53"
                     /coded_by="NM_001407271.1:273..1181"
                     /note="isoform i is encoded by transcript variant 13"
                     /db_xref="GeneID:7157"
                     /db_xref="HGNC:HGNC:11998"
                     /db_xref="MIM:191170"
ORIGIN      
        1 mddlmlspdd ieqwftedpg pdeaprmpea appvapapaa ptpaapapap swplsssvps
       61 qktyqgsygf rlgflhsgta ksvtctyspa lnkmfcqlak tcpvqlwvds tpppgtrvra
      121 maiykqsqhm tevvrrcphh ercsdsdgla ppqhlirveg nlrveylddr ntfrhsvvvp
      181 yeppevgsdc ttihynymcn sscmggmnrr piltiitled ssgnllgrns fevrvcacpg
      241 rdrrteeenl rkkgephhel ppgstkralp nntssspqpk kkpldgeyft lqdqtsfqke
      301 nc
//
LOCUS       NP_001425386             542 aa            linear   PRI 21-NOV-2025
DEFINITION  excitatory amino acid transporter 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001425386
VERSION     NP_001425386.1
DBSOURCE    REFSEQ: accession NM_001438457.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Albury,C.L., Sutherland,H.G., Lam,A.W.Y., Tran,N.K., Lea,R.A.,
            Haupt,L.M. and Griffiths,L.R.
  TITLE     Identification of Polymorphisms in EAAT1 Glutamate Transporter Gene
            SLC1A3 Associated with Reduced Migraine Risk
  JOURNAL   Genes (Basel) 15 (6), 797 (2024)
   PUBMED   38927733
  REMARK    GeneRIF: Identification of Polymorphisms in EAAT1 Glutamate
            Transporter Gene SLC1A3 Associated with Reduced Migraine Risk.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Welby,E. and Ebert,A.D.
  TITLE     Diminished motor neuron activity driven by abnormal astrocytic
            EAAT1 glutamate transporter activity in spinal muscular atrophy is
            not fully restored after lentiviral SMN delivery
  JOURNAL   Glia 71 (5), 1311-1332 (2023)
   PUBMED   36655314
  REMARK    GeneRIF: Diminished motor neuron activity driven by abnormal
            astrocytic EAAT1 glutamate transporter activity in spinal muscular
            atrophy is not fully restored after lentiviral SMN delivery.
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Pant,S., Wu,Q., Ryan,R. and Tajkhorshid,E.
  TITLE     Microscopic Characterization of the Chloride Permeation Pathway in
            the Human Excitatory Amino Acid Transporter 1 (EAAT1)
  JOURNAL   ACS Chem Neurosci 13 (6), 776-785 (2022)
   PUBMED   35192345
  REMARK    GeneRIF: Microscopic Characterization of the Chloride Permeation
            Pathway in the Human Excitatory Amino Acid Transporter 1 (EAAT1).
REFERENCE   5  (residues 1 to 542)
  AUTHORS   Lee,A., Anderson,A.R., Beasley,S.J., Barnett,N.L., Poronnik,P. and
            Pow,D.V.
  TITLE     A new splice variant of the glutamate-aspartate transporter:
            cloning and immunolocalization of GLAST1c in rat, pig and human
            brains
  JOURNAL   J Chem Neuroanat 43 (1), 52-63 (2012)
   PUBMED   22026960
REFERENCE   6  (residues 1 to 542)
  AUTHORS   Vallejo-Illarramendi,A., Domercq,M. and Matute,C.
  TITLE     A novel alternative splicing form of excitatory amino acid
            transporter 1 is a negative regulator of glutamate uptake
  JOURNAL   J Neurochem 95 (2), 341-348 (2005)
   PUBMED   16042756
  REMARK    GeneRIF: EAAT1ex9skip splice variant is a negative regulator of
            full-length EAAT1 function in the human brain
REFERENCE   7  (residues 1 to 542)
  AUTHORS   Takai,S., Yamada,K., Kawakami,H., Tanaka,K. and Nakamura,S.
  TITLE     Localization of the gene (SLC1A3) encoding human glutamate
            transporter (GluT-1) to 5p13 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 209-210 (1995)
   PUBMED   7698014
REFERENCE   8  (residues 1 to 542)
  AUTHORS   Shashidharan,P., Huntley,G.W., Meyer,T., Morrison,J.H. and
            Plaitakis,A.
  TITLE     Neuron-specific human glutamate transporter: molecular cloning,
            characterization and expression in human brain
  JOURNAL   Brain Res 662 (1-2), 245-250 (1994)
   PUBMED   7859077
REFERENCE   9  (residues 1 to 542)
  AUTHORS   Arriza,J.L., Fairman,W.A., Wadiche,J.I., Murdoch,G.H.,
            Kavanaugh,M.P. and Amara,S.G.
  TITLE     Functional comparisons of three glutamate transporter subtypes
            cloned from human motor cortex
  JOURNAL   J Neurosci 14 (9), 5559-5569 (1994)
   PUBMED   7521911
REFERENCE   10 (residues 1 to 542)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010631.6 and AC008957.7.
            
            Summary: This gene encodes a member of a member of a high affinity
            glutamate transporter family. This gene functions in the
            termination of excitatory neurotransmission in central nervous
            system. Mutations are associated with episodic ataxia, Type 6.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1161571.1,
                                           SRR1803611.129992.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..542
                     /product="excitatory amino acid transporter 1 isoform 1"
                     /note="excitatory amino acid transporter 1; GLAST-1;
                     sodium-dependent glutamate/aspartate transporter 1; solute
                     carrier family 1 (glial high affinity glutamate
                     transporter), member 3"
                     /calculated_mol_wt=59441
     Region          46..496
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            87..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            123..145
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            237..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            270..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            319..340
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            386..412
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            473..494
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P43003.1)"
     CDS             1..542
                     /gene="SLC1A3"
                     /gene_synonym="EA6; EAAT1; GLAST; GLAST1"
                     /coded_by="NM_001438457.1:157..1785"
                     /note="isoform 1 is encoded by transcript variant 9"
                     /db_xref="GeneID:6507"
                     /db_xref="HGNC:HGNC:10941"
                     /db_xref="MIM:600111"
ORIGIN      
        1 mtksngeepk mggrmerfqq gvrkrtllak kkvqnitked vksylfrnaf vlltvtaviv
       61 gtilgftlrp yrmsyrevky fsfpgellmr mlqmlvlpli isslvtgmaa ldskasgkmg
      121 mravvyymtt tiiavvigii iviiihpgkg tkenmhregk ivrvtaadaf ldlirnmfpp
      181 nlveacfkqf ktnyekrsfk vpiqanetlv gavinnvsea metltritee lvpvpgsvng
      241 vnalglvvfs mcfgfvignm keqgqalref fdslneaimr lvavimwyap vgilfliagk
      301 ivemedmgvi ggqlamytvt vivgllihav ivlpllyflv trknpwvfig gllqalital
      361 gtssssatlp itfkcleenn gvdkrvtrfv lpvgatinmd gtalyealaa ifiaqvnnfe
      421 lnfgqiitis itataasiga agipqaglvt mvivltsvgl ptdditliia vdwfldrlrt
      481 ttnvlgdslg agivehlsrh elknrdvemg nsvieenemk kpyqliaqdn etekpidset
      541 km
//
LOCUS       NP_001400128             656 aa            linear   PRI 21-NOV-2025
DEFINITION  cyclin-T1 isoform d [Homo sapiens].
ACCESSION   NP_001400128
VERSION     NP_001400128.1
DBSOURCE    REFSEQ: accession NM_001413199.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 656)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 656)
  AUTHORS   Chen,W., Chu,J., Miao,Y., Jiang,W., Wang,F., Zhang,N., Jin,J. and
            Cai,Y.
  TITLE     MOF-mediated acetylation of CDK9 promotes global transcription by
            modulating P-TEFb complex formation
  JOURNAL   FEBS J 291 (21), 4796-4812 (2024)
   PUBMED   39250546
REFERENCE   3  (residues 1 to 656)
  AUTHORS   Gao,G., Wu,X., Zhou,J., He,M., He,J.J. and Guo,D.
  TITLE     Inhibition of HIV-1 transcription and replication by a newly
            identified cyclin T1 splice variant
  JOURNAL   J Biol Chem 288 (20), 14297-14309 (2013)
   PUBMED   23569210
  REMARK    GeneRIF: CYCT1b is a newly identified cyclin T1 splice variant
            whose expression leads to direct inhibition of TAT-transactivated
            transcription of the HIV-1 LTR promoter
REFERENCE   4  (residues 1 to 656)
  AUTHORS   Urano,E., Miyauchi,K., Ichikawa,R., Futahashi,Y. and Komano,J.
  TITLE     Regulation of cyclin T1 expression and function by an alternative
            splice variant that skips exon 7 and contains a premature
            termination codon
  JOURNAL   Gene 505 (1), 1-8 (2012)
   PUBMED   22692005
REFERENCE   5  (residues 1 to 656)
  AUTHORS   De Luca,A., De Falco,M., Baldi,A. and Paggi,M.G.
  TITLE     Cyclin T: three forms for different roles in physiological and
            pathological functions
  JOURNAL   J Cell Physiol 194 (2), 101-107 (2003)
   PUBMED   12494448
  REMARK    Review article
REFERENCE   6  (residues 1 to 656)
  AUTHORS   Martin-Serrano,J., Li,K. and Bieniasz,P.D.
  TITLE     Cyclin T1 expression is mediated by a complex and constitutively
            active promoter and does not limit human immunodeficiency virus
            type 1 Tat function in unstimulated primary lymphocytes
  JOURNAL   J Virol 76 (1), 208-219 (2002)
   PUBMED   11739686
REFERENCE   7  (residues 1 to 656)
  AUTHORS   Liu,H. and Rice,A.P.
  TITLE     Isolation and characterization of the human cyclin T1 promoter
  JOURNAL   Gene 252 (1-2), 39-49 (2000)
   PUBMED   10903436
REFERENCE   8  (residues 1 to 656)
  AUTHORS   Wei,P., Garber,M.E., Fang,S.M., Fischer,W.H. and Jones,K.A.
  TITLE     A novel CDK9-associated C-type cyclin interacts directly with HIV-1
            Tat and mediates its high-affinity, loop-specific binding to TAR
            RNA
  JOURNAL   Cell 92 (4), 451-462 (1998)
   PUBMED   9491887
REFERENCE   9  (residues 1 to 656)
  AUTHORS   Yang,X., Herrmann,C.H. and Rice,A.P.
  TITLE     The human immunodeficiency virus Tat proteins specifically
            associate with TAK in vivo and require the carboxyl-terminal domain
            of RNA polymerase II for function
  JOURNAL   J Virol 70 (7), 4576-4584 (1996)
   PUBMED   8676484
REFERENCE   10 (residues 1 to 656)
  AUTHORS   Herrmann,C.H. and Rice,A.P.
  TITLE     Lentivirus Tat proteins specifically associate with a cellular
            protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal
            domain of the large subunit of RNA polymerase II: candidate for a
            Tat cofactor
  JOURNAL   J Virol 69 (3), 1612-1620 (1995)
   PUBMED   7853496
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079951.35.
            
            Summary: This gene encodes a member of the highly conserved cyclin
            C subfamily. The encoded protein tightly associates with
            cyclin-dependent kinase 9, and is a major subunit of positive
            transcription elongation factor b (p-TEFb). In humans, there are
            multiple forms of positive transcription elongation factor b, which
            may include one of several different cyclins along with
            cyclin-dependent kinase 9. The complex containing the encoded
            cyclin and cyclin-dependent kinase 9 acts as a cofactor of human
            immunodeficiency virus type 1 (HIV-1) Tat protein, and is both
            necessary and sufficient for full activation of viral
            transcription. This cyclin and its kinase partner are also involved
            in triggering transcript elongation through phosphorylation of the
            carboxy-terminal domain of the largest RNA polymerase II subunit.
            Overexpression of this gene is implicated in tumor growth.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Apr 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1705625.1,
                                           SRR14038195.1063518.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..656
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.11-q13.12"
     Protein         1..656
                     /product="cyclin-T1 isoform d"
                     /note="human immunodeficiency virus type 1 (HIV-1)
                     expression (elevated) 1; cyclin C-related protein;
                     CDK9-associated C-type protein; MLLT10/CCNT1 fusion"
                     /calculated_mol_wt=72624
     Region          10..147
                     /region_name="CYCLIN_CCNT1_rpt1"
                     /note="first cyclin box found in cyclin-T1 (CCNT1);
                     cd20595"
                     /db_xref="CDD:410298"
     Site            order(11..12,72..73,89..90,93,96,99..102,130,134,137,
                     141..143,145..146)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410298"
     Site            order(39..40,43..44,46..47,49..51,53..54,56..57,59,81,
                     95..97,111..112)
                     /site_type="other"
                     /note="HIV-1 Tat binding site [polypeptide binding]"
                     /db_xref="CDD:410298"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (O60563.1)"
     Region          <162..194
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cl40454"
                     /db_xref="CDD:477360"
     CDS             1..656
                     /gene="CCNT1"
                     /gene_synonym="CCNT; CYCT1; HIVE1"
                     /coded_by="NM_001413199.1:33..2003"
                     /note="isoform d is encoded by transcript variant d"
                     /db_xref="GeneID:904"
                     /db_xref="HGNC:HGNC:1599"
                     /db_xref="MIM:143055"
ORIGIN      
        1 megerknnnk rwyftreqle nspsrrfgvd pdkelsyrqq aanllqdmgq rlnvsqltin
       61 taivymhrfy miqsftqfpg nsvapaalfl aakveeqpkk lehvikvaht clhpqeslpd
      121 trseaylqqv qdlvilesii lqtlgfelti dhphthvvkc tqlvrelthe flqilektpn
      181 rlkriwnwra ceaakktkad drgtdektse qtilnmisqs ssdttiaglm smststtsav
      241 pslpvseess snltsvemlp gkrwlssqps fkleptqghr tsenlaltgv dhslpqdgsn
      301 afisqkqnsk svpsakvslk eyrakhaeel aaqkrqlenm eanvksqyay aaqnllshhd
      361 shssvilkmp iegsenperp flekadktal kmripvaggd kaasskpeei kmrikvhaaa
      421 dkhnsvedsv tksrehkekh kthpsnhhhh hnhhshkhsh sqlpvgtgnk rpgdpkhssq
      481 tsnlahktys lsssfsssss trkrgpseet ggavfdhpak iakstksssl nfsfpslptm
      541 gqmpghssdt sglsfsqpsc ktrvphskld kgptganghn ttqtidyqdt vnmlhsllsa
      601 qgvqptqpta fefvrpysdy lnprsggiss rsgntdkprp pplpsepppp lpplpk
//
LOCUS       NP_001425261             993 aa            linear   PRI 21-NOV-2025
DEFINITION  centrosome and spindle pole-associated protein 1 isoform 11 [Homo
            sapiens].
ACCESSION   NP_001425261 XP_047278217 XP_054217249
VERSION     NP_001425261.1
DBSOURCE    REFSEQ: accession NM_001438332.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 993)
  AUTHORS   van den Berg,C.M., Volkov,V.A., Schnorrenberg,S., Huang,Z.,
            Stecker,K.E., Grigoriev,I., Gilani,S., Frikstad,K.M., Patzke,S.,
            Zimmermann,T., Dogterom,M. and Akhmanova,A.
  TITLE     CSPP1 stabilizes growing microtubule ends and damaged lattices from
            the luminal side
  JOURNAL   J Cell Biol 222 (4) (2023)
   PUBMED   36752787
  REMARK    GeneRIF: CSPP1 stabilizes growing microtubule ends and damaged
            lattices from the luminal side.
REFERENCE   2  (residues 1 to 993)
  AUTHORS   Odabasi,E., Conkar,D., Deretic,J., Batman,U., Frikstad,K.M.,
            Patzke,S. and Firat-Karalar,E.N.
  TITLE     CCDC66 regulates primary cilium length and signaling via
            interactions with transition zone and axonemal proteins
  JOURNAL   J Cell Sci 136 (3) (2023)
   PUBMED   36606424
REFERENCE   3  (residues 1 to 993)
  AUTHORS   Zhang,L., Yang,S.T., Wang,C., Zhang,L.C., Zhang,X., Li,F.C.,
            Wang,S.Y. and Ma,K.
  TITLE     Circle RNA circCSPP1 promotes human osteosarcoma cell proliferation
            and increases glucose metabolism by suppressing miR-200c maturation
  JOURNAL   Hum Exp Toxicol 41, 9603271221097364 (2022)
   PUBMED   35713481
  REMARK    GeneRIF: Circle RNA circCSPP1 promotes human osteosarcoma cell
            proliferation and increases glucose metabolism by suppressing
            miR-200c maturation.
REFERENCE   4  (residues 1 to 993)
  AUTHORS   Latour,B.L., Van De Weghe,J.C., Rusterholz,T.D., Letteboer,S.J.,
            Gomez,A., Shaheen,R., Gesemann,M., Karamzade,A., Asadollahi,M.,
            Barroso-Gil,M., Chitre,M., Grout,M.E., van Reeuwijk,J., van
            Beersum,S.E., Miller,C.V., Dempsey,J.C., Morsy,H., Bamshad,M.J.,
            Nickerson,D.A., Neuhauss,S.C., Boldt,K., Ueffing,M.,
            Keramatipour,M., Sayer,J.A., Alkuraya,F.S., Bachmann-Gagescu,R.,
            Roepman,R. and Doherty,D.
  CONSRTM   University of Washington Center for Mendelian Genomics; Genomics
            England Research Consortium
  TITLE     Dysfunction of the ciliary ARMC9/TOGARAM1 protein module causes
            Joubert syndrome
  JOURNAL   J Clin Invest 130 (8), 4423-4439 (2020)
   PUBMED   32453716
REFERENCE   5  (residues 1 to 993)
  AUTHORS   Xue,Y.F., Li,M., Li,W., Lin,Q., Yu,B.X., Zhu,Q.B. and Chen,H.J.
  TITLE     Roles of circ-CSPP1 on the proliferation and metastasis of glioma
            cancer
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (10), 5519-5525 (2020)
   PUBMED   32495924
  REMARK    GeneRIF: Roles of circ-CSPP1 on the proliferation and metastasis of
            glioma cancer.
REFERENCE   6  (residues 1 to 993)
  AUTHORS   Patzke,S., Redick,S., Warsame,A., Murga-Zamalloa,C.A., Khanna,H.,
            Doxsey,S. and Stokke,T.
  TITLE     CSPP is a ciliary protein interacting with Nephrocystin 8 and
            required for cilia formation
  JOURNAL   Mol Biol Cell 21 (15), 2555-2567 (2010)
   PUBMED   20519441
  REMARK    GeneRIF: CSPP isoforms require their common C-terminal domain to
            interact with Nephrocystin 8 (NPHP8/RPGRIP1L) and to form a ternary
            complex with NPHP8 and NPHP4.
REFERENCE   7  (residues 1 to 993)
  AUTHORS   Asiedu,M., Wu,D., Matsumura,F. and Wei,Q.
  TITLE     Centrosome/spindle pole-associated protein regulates cytokinesis
            via promoting the recruitment of MyoGEF to the central spindle
  JOURNAL   Mol Biol Cell 20 (5), 1428-1440 (2009)
   PUBMED   19129481
  REMARK    GeneRIF: CSPP interacts with and recruits MyoGEF to the central
            spindle, where MyoGEF contributes to the spatiotemporal regulation
            of cytokinesis.
REFERENCE   8  (residues 1 to 993)
  AUTHORS   Patzke,S., Stokke,T. and Aasheim,H.C.
  TITLE     CSPP and CSPP-L associate with centrosomes and microtubules and
            differently affect microtubule organization
  JOURNAL   J Cell Physiol 209 (1), 199-210 (2006)
   PUBMED   16826565
  REMARK    GeneRIF: Taken together, CSPP and CSPP-L interact with centrosomes
            and microtubules and can differently affect microtubule
            organization.
REFERENCE   9  (residues 1 to 993)
  AUTHORS   Patzke,S., Hauge,H., Sioud,M., Finne,E.F., Sivertsen,E.A.,
            Delabie,J., Stokke,T. and Aasheim,H.C.
  TITLE     Identification of a novel centrosome/microtubule-associated
            coiled-coil protein involved in cell-cycle progression and spindle
            organization
  JOURNAL   Oncogene 24 (7), 1159-1173 (2005)
   PUBMED   15580290
  REMARK    GeneRIF: Novel centrosome/microtubule-associated coiled-coil
            protein (CSPP)is associated with centrosomes and microtubules and
            may play a role in the regulation of G(1)/S-phase progression and
            spindle assembly [CSPP].
REFERENCE   10 (residues 1 to 993)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC109335.5 and AC087359.13.
            
            On or before Apr 17, 2025 this sequence version replaced
            XP_047278217.1, XP_054217249.1.
            
            Summary: This gene encodes a centrosome and spindle pole associated
            protein. The encoded protein plays a role in cell-cycle progression
            and spindle organization, regulates cytokinesis, interacts with
            Nephrocystin 8 and is required for cilia formation. Mutations in
            this gene result in primary cilia abnormalities and classical
            Joubert syndrome. Alternatively spliced transcript variants
            encoding distinct isoforms have been found for this gene. [provided
            by RefSeq, Apr 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.164474.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..993
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1-q13.2"
     Protein         1..993
                     /product="centrosome and spindle pole-associated protein 1
                     isoform 11"
                     /calculated_mol_wt=116086
     CDS             1..993
                     /gene="CSPP1"
                     /gene_synonym="CSPP; CSPP-L; JBTS21"
                     /coded_by="NM_001438332.1:8..2989"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:79848"
                     /db_xref="HGNC:HGNC:26193"
                     /db_xref="MIM:611654"
ORIGIN      
        1 mlfplqvaav tssvrddple hcvsprtrar speickmadn ldefieeqka rlaedkaele
       61 sdppymemkg klsaklsens kilismaken ippnsqqtrg slgidyglsl plgedyerkk
      121 hklkeelrqd yrryltqerl klernkeynq flrgkeesse kfrqvekste pksqrnkkpi
      181 gqvkpdltsq iqtscenseg prkdvltpse ayeellnqrr leedryrqld deielrnrri
      241 ikkaneevgi snlkhqrfas kagipdrrfh rfnedrvfdr ryhrpdqdpe vseemderfr
      301 yesdfdrrls rvytndriap lppppllppl atnyrtpydd ayyfygsrnt fdpslayygs
      361 gmmgvqpaay vsapvthqla qpvvntvgqn elkitsdqvi nsglifedkp kpskqslqsy
      421 qealqqqire reerrkkere ekeeyeakle aemrtynpwg kggggaplrd akgnlishmq
      481 tqsspfargn vfgepptelq ikqqelyknf lrfqieekkq reeaererlr iaeekeerrl
      541 aeqrariqqe yeeeqekkre keeeqrlkne ehirlaeerq keaerkkkee eekynlqlqh
      601 ycerdnlige etkhmrqpsp ivpalqnkia sklqrppsvd siirsfihes smsraqsppv
      661 parknqlrae eekknvimel semrkqlrse errlqerllh mdsddeipir kkernpmdif
      721 dmarhrlqap vrrqspkgld aatfqnvhdf nelkdrdset rvdlkfmyld pprdhhtlei
      781 qqqallreqq krlnrikmqe gakvdldaip sakvreqrmp rddtsdflkn sllesdsafi
      841 gaygetypai eddvlpppsq lpsarerrrn kwkgldidss rpnvapdgls lksissvnvd
      901 elrvrneerm rrlnefhnkp intddesslv dpddimkhig ddgsnsvate pwlrpgtset
      961 lkrfmaeqln qeqqqipgkp gtftwqglst ahg
//
LOCUS       NP_001400234             291 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 2 [Homo sapiens].
ACCESSION   NP_001400234
VERSION     NP_001400234.1
DBSOURCE    REFSEQ: accession NM_001413305.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC103816.2, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.278796.1,
                                           SRR1803614.153089.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968832 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..291
                     /product="RNA-binding Raly-like protein isoform 2"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=32199
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          171..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     Region          199..>244
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     Region          249..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     CDS             1..291
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413305.1:562..1437"
                     /note="isoform 2 is encoded by transcript variant 32"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly rleskepfls
      121 vggyvfdydy yrddfynrlf dyhgrvpppp raviplkrpr vavtttrrgk gvfsmkggsr
      181 stasgstgsk lksdelqtik keltqiktki dsllgrleki ekqqkaeaea qkkqleeslv
      241 liqeecvsei adhsteepae ggpdadgeem tdgieedfde dgghelflqi k
//
LOCUS       NP_001401391             237 aa            linear   PRI 21-NOV-2025
DEFINITION  bax inhibitor 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001401391 XP_047285446
VERSION     NP_001401391.1
DBSOURCE    REFSEQ: accession NM_001414462.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Zhang,X., Chen,Q., He,Y., Shi,Q., Yin,C., Xie,Y., Yu,H., Bao,Y.,
            Wang,X., Tang,C. and Dong,Z.
  TITLE     STRIP2 motivates non-small cell lung cancer progression by
            modulating the TMBIM6 stability through IGF2BP3 dependent
  JOURNAL   J Exp Clin Cancer Res 42 (1), 19 (2023)
   PUBMED   36639675
  REMARK    GeneRIF: STRIP2 motivates non-small cell lung cancer progression by
            modulating the TMBIM6 stability through IGF2BP3 dependent.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Liao,Y., Qiu,Z. and Bai,L.
  TITLE     miR-302d-3p regulates the viability, migration and apoptosis of
            breast cancer cells through regulating the TMBIM6-mediated ERK
            signaling pathway
  JOURNAL   Mol Med Rep 24 (6) (2021)
   PUBMED   34651659
  REMARK    GeneRIF: miR302d3p regulates the viability, migration and apoptosis
            of breast cancer cells through regulating the TMBIM6mediated ERK
            signaling pathway.
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Bhattarai,K.R., Kim,H.K., Chaudhary,M., Ur Rashid,M.M., Kim,J.,
            Kim,H.R. and Chae,H.J.
  TITLE     TMBIM6 regulates redox-associated posttranslational modifications
            of IRE1alpha and ER stress response failure in aging mice and
            humans
  JOURNAL   Redox Biol 47, 102128 (2021)
   PUBMED   34562874
  REMARK    GeneRIF: TMBIM6 regulates redox-associated posttranslational
            modifications of IRE1alpha and ER stress response failure in aging
            mice and humans.
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 237)
  AUTHORS   Grzmil,M., Thelen,P., Hemmerlein,B., Schweyer,S., Voigt,S., Mury,D.
            and Burfeind,P.
  TITLE     Bax inhibitor-1 is overexpressed in prostate cancer and its
            specific down-regulation by RNA interference leads to cell death in
            human prostate carcinoma cells
  JOURNAL   Am J Pathol 163 (2), 543-552 (2003)
   PUBMED   12875974
  REMARK    GeneRIF: Results indicate that the human Bax inhibitor-1 gene may
            serve as a prostate cancer expression marker based on its
            overexpression in prostate carcinoma and prostate cancer cell
            lines.
REFERENCE   7  (residues 1 to 237)
  AUTHORS   Jean,J.C., Oakes,S.M. and Joyce-Brady,M.
  TITLE     The Bax inhibitor-1 gene is differentially regulated in adult
            testis and developing lung by two alternative TATA-less promoters
  JOURNAL   Genomics 57 (2), 201-208 (1999)
   PUBMED   10198159
REFERENCE   8  (residues 1 to 237)
  AUTHORS   Cowling,R.T. and Birnboim,H.C.
  TITLE     Preliminary characterization of the protein encoded by human
            testis-enhanced gene transcript (TEGT)
  JOURNAL   Mol Membr Biol 15 (4), 177-187 (1998)
   PUBMED   10087504
REFERENCE   9  (residues 1 to 237)
  AUTHORS   Xu,Q. and Reed,J.C.
  TITLE     Bax inhibitor-1, a mammalian apoptosis suppressor identified by
            functional screening in yeast
  JOURNAL   Mol Cell 1 (3), 337-346 (1998)
   PUBMED   9660918
REFERENCE   10 (residues 1 to 237)
  AUTHORS   Walter,L., Marynen,P., Szpirer,J., Levan,G. and Gunther,E.
  TITLE     Identification of a novel conserved human gene, TEGT
  JOURNAL   Genomics 28 (2), 301-304 (1995)
   PUBMED   8530040
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC084037.35 and AC131157.4.
            
            On Feb 21, 2023 this sequence version replaced XP_047285446.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1538106.1,
                                           SRR11853567.7018.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..237
                     /product="bax inhibitor 1 isoform 1"
                     /note="BAX inhibitor 1; testis-enhanced gene transcript
                     protein; transmembrane BAX inhibitor motif-containing
                     protein 6; testis enhanced gene transcript"
                     /calculated_mol_wt=26407
     Region          16..228
                     /region_name="BI-1"
                     /note="BAX inhibitor (BI)-1; cd10430"
                     /db_xref="CDD:198412"
     Site            30..50
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            53..73
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            87..107
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            140..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            167..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     CDS             1..237
                     /gene="TMBIM6"
                     /gene_synonym="BAXI1; BI-1; TEGT"
                     /coded_by="NM_001414462.1:245..958"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:7009"
                     /db_xref="HGNC:HGNC:11723"
                     /db_xref="MIM:600748"
ORIGIN      
        1 mnifdrkinf dallkfshit pstqqhlkkv yasfalcmfv aaagayvhmv thfiqaglls
       61 algslilmiw lmatphshet eqkrlgllag fafltgvglg palefciavn psilptafmg
      121 tamiftcftl salyarrrsy lflggilmsa lsllllsslg nvffgsiwlf qanlyvglvv
      181 mcgfvlfdtq liiekaehgd qdyiwhcidl fldfitvfrk lmmilamnek dkkkekk
//
LOCUS       NP_001400679             823 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform l [Homo sapiens].
ACCESSION   NP_001400679
VERSION     NP_001400679.1
DBSOURCE    REFSEQ: accession NM_001413750.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 823)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 823)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 823)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 823)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 823)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 823)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 823)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 823)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 823)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1007309.1,
                                           SRR18074967.1092610.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..823
                     /product="polyhomeotic-like protein 1 isoform l"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=87222
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          204..233
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          253..347
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          647..754
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          754..822
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(772..773,807..808,811..812,815)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(783..787,789..790,793..794,798,803)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..823
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413750.1:368..2839"
                     /note="isoform l is encoded by transcript variant 14"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq asinlattsa aqlisrsqsv
      121 sspsattltq svllgnttsp plnqsqaqmy lrvnrtlgrn vplasqlilm pngavaavqq
      181 evpsaqspgv hadadqvqnl avrnqqasaq gpqmqgstqk aippgaspvs slsqassqal
      241 avaqassgat nqslnlsqag ggsgnsipgs mgpggggqah gglgqlpssg mgggscprkg
      301 tgvvqplpaa qtvtvsqgsq teaesaaakk aeadgsgqqn vgmnltrtat papsqtliss
      361 atytqiqphs liqqqqqihl qqkqvviqqq iaihhqqqfq hrqsqllhta thlqlaqqqq
      421 qqqqqqqqqq qpqattltap qppqvpptqq gkpqtlavkr kadseeerdd vstlgsmlpa
      481 kaspvaespk vmdeksslge kaesvanvna ntpsselval tpapsvpppt lamvsrqmgd
      541 skppqaivkp qilthiiegf viqegaepfp vgcsqllkes ekplqtglpt gltenqsggp
      601 lgvdspsael dkkanllkce ycgkyapaeq frgskrfcsm tcakrynvsc shqfrlkrkk
      661 mkefqeanya rvrrrgprrs ssdiarakiq gkchrgqeds srgsdnssyd ealsptspgp
      721 lsvraghger dlgnpntapp tpelhginpv flssnpsrws veevyefias lqgcqeiaee
      781 frsqeidgqa llllkeehlm samniklgpa lkicakinvl ket
//
LOCUS       NP_001427364            1258 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 isoform 2
            [Homo sapiens].
ACCESSION   NP_001427364 XP_011543301 XP_054224656
VERSION     NP_001427364.1
DBSOURCE    REFSEQ: accession NM_001440435.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1258)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1258)
  AUTHORS   Ji,X., Wu,Q., Cao,X., Liu,S., Zhang,J., Chen,S., Shan,J., Zhang,Y.,
            Li,B. and Zhao,H.
  TITLE     Helicobacter pylori East Asian type CagA hijacks more SHIP2 by its
            EPIYA-D motif to potentiate the oncogenicity
  JOURNAL   Virulence 15 (1), 2375549 (2024)
   PUBMED   38982595
  REMARK    GeneRIF: Helicobacter pylori East Asian type CagA hijacks more
            SHIP2 by its EPIYA-D motif to potentiate the oncogenicity.
REFERENCE   3  (residues 1 to 1258)
  AUTHORS   Ando,K., Kucukali,F., Doeraene,E., Nagaraj,S., Antonelli,E.M.,
            Thazin Htut,M., Yilmaz,Z., Kosa,A.C., Lopez-Guitierrez,L.,
            Quintanilla-Sanchez,C., Aydin,E., Ramos,A.R., Mansour,S.,
            Turbant,S., Schurmans,S., Sleegers,K., Erneux,C., Brion,J.P. and
            Leroy,K.
  CONSRTM   Brain Bank NeuroCEB Neuropathology Network
  TITLE     Alteration of gene expression and protein solubility of the PI
            5-phosphatase SHIP2 are correlated with Alzheimer's disease
            pathology progression
  JOURNAL   Acta Neuropathol 147 (1), 94 (2024)
   PUBMED   38833073
  REMARK    GeneRIF: Alteration of gene expression and protein solubility of
            the PI 5-phosphatase SHIP2 are correlated with Alzheimer's disease
            pathology progression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1258)
  AUTHORS   Bradshaw,W.J., Kennedy,E.C., Moreira,T., Smith,L.A., Chalk,R.,
            Katis,V.L., Benesch,J.L.P., Brennan,P.E., Murphy,E.J. and
            Gileadi,O.
  TITLE     Regulation of inositol 5-phosphatase activity by the C2 domain of
            SHIP1 and SHIP2
  JOURNAL   Structure 32 (4), 453-466 (2024)
   PUBMED   38309262
  REMARK    GeneRIF: Regulation of inositol 5-phosphatase activity by the C2
            domain of SHIP1 and SHIP2.
REFERENCE   5  (residues 1 to 1258)
  AUTHORS   Habib,T., Hejna,J.A., Moses,R.E. and Decker,S.J.
  TITLE     Growth factors and insulin stimulate tyrosine phosphorylation of
            the 51C/SHIP2 protein
  JOURNAL   J Biol Chem 273 (29), 18605-18609 (1998)
   PUBMED   9660833
REFERENCE   6  (residues 1 to 1258)
  AUTHORS   Le Drean,E., Vely,F., Olcese,L., Cambiaggi,A., Guia,S., Krystal,G.,
            Gervois,N., Moretta,A., Jotereau,F. and Vivier,E.
  TITLE     Inhibition of antigen-induced T cell response and antibody-induced
            NK cell cytotoxicity by NKG2A: association of NKG2A with SHP-1 and
            SHP-2 protein-tyrosine phosphatases
  JOURNAL   Eur J Immunol 28 (1), 264-276 (1998)
   PUBMED   9485206
  REMARK    Erratum:[Eur J Immunol 1998 Mar;28(3):1122]
REFERENCE   7  (residues 1 to 1258)
  AUTHORS   Pesesse,X., Deleu,S., De Smedt,F., Drayer,L. and Erneux,C.
  TITLE     Identification of a second SH2-domain-containing protein closely
            related to the phosphatidylinositol polyphosphate 5-phosphatase
            SHIP
  JOURNAL   Biochem Biophys Res Commun 239 (3), 697-700 (1997)
   PUBMED   9367831
REFERENCE   8  (residues 1 to 1258)
  AUTHORS   Hejna,J.A., Saito,H., Merkens,L.S., Tittle,T.V., Jakobs,P.M.,
            Whitney,M.A., Grompe,M., Friedberg,A.S. and Moses,R.E.
  TITLE     Cloning and characterization of a human cDNA (INPPL1) sharing
            homology with inositol polyphosphate phosphatases
  JOURNAL   Genomics 29 (1), 285-287 (1995)
   PUBMED   8530088
REFERENCE   9  (residues 1 to 1258)
  AUTHORS   Huang,S., Earl,D. and White,K.
  TITLE     INPPL1-Related Opsismodysplasia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   40504975
REFERENCE   10 (residues 1 to 1258)
  AUTHORS   Slama,V. and Dudek,J.
  TITLE     [Stability of diluted solutions of peracetic acid]
  JOURNAL   Cesk Farm 17 (1), 40-41 (1968)
   PUBMED   5668240
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000593.4.
            
            On or before May 20, 2025 this sequence version replaced
            XP_011543301.1, XP_054224656.1.
            
            Summary: The protein encoded by this gene is an SH2-containing
            5'-inositol phosphatase that is involved in the regulation of
            insulin function. The encoded protein also plays a role in the
            regulation of epidermal growth factor receptor turnover and actin
            remodelling. Additionally, this gene supports metastatic growth in
            breast cancer and is a valuable biomarker for breast cancer.
            [provided by RefSeq, Jan 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4352444.550205.1,
                                           SRR13170464.49105.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1258
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..1258
                     /product="phosphatidylinositol 3,4,5-trisphosphate
                     5-phosphatase 2 isoform 2"
                     /EC_number="3.1.3.86"
                     /note="SH2 domain-containing inositol-5'-phosphatase 2;
                     51C protein; protein 51C; phosphatidylinositol
                     3,4,5-trisphosphate 5-phosphatase 2"
                     /calculated_mol_wt=138468
     Region          17..119
                     /region_name="SH2_SHIP"
                     /note="Src homology 2 (SH2) domain found in SH2-containing
                     inositol-5'-phosphatase (SHIP) and SLAM-associated protein
                     (SAP); cd10343"
                     /db_xref="CDD:198206"
     Site            order(28,47,68,70)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198206"
     Site            order(68..69,81..82,87,90,106..108)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198206"
     Region          119..180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          424..727
                     /region_name="INPP5c_SHIP2-INPPL1"
                     /note="Catalytic inositol polyphosphate 5-phosphatase
                     (INPP5c) domain of SH2 domain containing inositol
                     5-phosphatase-2 and related proteins; cd09101"
                     /db_xref="CDD:197335"
     Site            order(432,434,473,540..541,561,564..565,607,609,611,
                     661..662,684,690,717..718)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197335"
     Site            order(432,473,561,607,609,690,717..718)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197335"
     Site            order(473,540..541,561,564..565,611,661..662,684,717)
                     /site_type="other"
                     /note="putative PI/IP binding site [chemical binding]"
                     /db_xref="CDD:197335"
     Site            order(473,717)
                     /site_type="other"
                     /note="putative Mg binding site [ion binding]"
                     /db_xref="CDD:197335"
     Site            order(561,609,718)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197335"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            890
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          897..1118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Region          <899..1214
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          944..949
                     /region_name="SH3-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Site            958
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17219406,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          983..986
                     /region_name="NPXY motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Site            986
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:11349134,
                     ECO:0000269|PubMed:12235291; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            1131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            1135
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:11687594,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          1194..1256
                     /region_name="SAM_Ship2"
                     /note="SAM domain of Ship2 lipid phosphatase proteins;
                     cd09491"
                     /db_xref="CDD:188890"
     Site            order(1222..1224,1226..1227,1230,1235)
                     /site_type="other"
                     /note="heterodimer interface ML [polypeptide binding]"
                     /db_xref="CDD:188890"
     Site            1257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     CDS             1..1258
                     /gene="INPPL1"
                     /gene_synonym="OPSMD; SHIP2"
                     /coded_by="NM_001440435.1:273..4049"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:3636"
                     /db_xref="HGNC:HGNC:6080"
                     /db_xref="MIM:600829"
ORIGIN      
        1 masacgapgp ggalgsqaps wyhrdlsraa aeellaragr dgsflvrdse svagafalcv
       61 lyqkhvhtyr ilpdgedfla vqtsqgvpvr rfqtlgelig lyaqpnqglv calllpvege
      121 repdppddrd asdgedekpp lpprsgstsi saptgpsspl papetptapa aesapnglst
      181 vshdylkgsy gldleavrgg ashlphltrt latscrrlhs evdkvlsgle ilskvfdqqs
      241 spmvtrllqq qnlpqtgeqe leslvlklsv lkdflsgiqk kalkalqdms stappapqps
      301 trkaktipvq afevkldvtl gdltkigksq kftlsvdveg grlvllrrqr dsqedwttft
      361 hdrirqliks qrvqnklgvv fekekdrtqr kdfifvsark reafcqllql mknkhskqde
      421 pdmisvfigt wnmgsvpppk nvtswftskg lgktldevtv tiphdiyvfg tqensvgdre
      481 wldllrgglk eltdldyrpi amqslwnikv avlvkpehen rishvstssv ktgiantlgn
      541 kgavgvsfmf ngtsfgfvnc hltsgnekta rrnqnyldil rllslgdrql nafdislrft
      601 hlfwfgdlny rldmdiqeil nyisrkefep llrvdqlnle rekhkvflrf seeeisfppt
      661 yryergsrdt yawhkqkptg vrtnvpswcd rilwksypet hiicnsygct ddivtsdhsp
      721 vfgtfevgvt sqfiskkgls ktsdqayief esieaivkta srtkffiefy stcleeykks
      781 fendaqssdn inflkvqwss rqlptlkpil adieylqdqh llltvksmdg yesygecvva
      841 lksmigstaq qfltflshrg eetgnirgsm kvrvpterlg trerlyewis idkdeagaks
      901 kapsvsrgsq eprsgsrkpa fteascplsr lfeepekppp tgrppappra apreepltpr
      961 lkpegapepe gvaapppkns fnnpayyvle gvphqllppe ppsparapvp satknkvait
     1021 vpapqlghhr hprvgegsss deesggtlpp pdfpppplpd saiflppsld plpgpvvrgr
     1081 ggaeargppp pkahprpplp pgpspastfl gevasgddrs csvlqmaktl sevdyapagp
     1141 arsallpgpl elqpprglps dygrplsfpp priresiqed laeeapclqg grasglgeag
     1201 msawlraigl eryeeglvhn gwddleflsd iteedleeag vqdpahkrll ldtlqlsk
//
LOCUS       NP_001393534            1150 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 7 [Homo sapiens].
ACCESSION   NP_001393534 XP_047279789
VERSION     NP_001393534.1
DBSOURCE    REFSEQ: accession NM_001406605.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1150)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1150)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1150)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1150)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1150)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1150)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1150)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1150)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1150)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1150)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            On May 18, 2022 this sequence version replaced XP_047279789.1.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1990491.1,
                                           SRR14038196.2896212.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1150
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1150
                     /product="hamartin isoform 7"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=128069
     Region          7..719
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          403..787
                     /region_name="Mediates interaction with WDR45B.
                     /evidence=ECO:0000269|PubMed:28561066"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Region          439..571
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <705..>942
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          992..1071
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1086
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1117..1150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1150
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406605.1:218..3670"
                     /note="isoform 7 is encoded by transcript variant 19"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt aggkgtplgt patspppapl chsddyvhis lpqatvtppr
      421 keermdsarp clhrqhhlln drgseeppgs kgsvtlsdlp gflgdlasee dsiekdkeea
      481 aisrelseit taeaepvvpr ggfdspfyrd slpgsqrkth saasssqgas vnpeplhssl
      541 dklgpdtpkq aftpidlpcg sadespagdr ecqtsletsi ftpspckipp ptrvgfgsgq
      601 pppydhlfev alpktahhfv irkteellkk akgnteedgv pstspmevld rliqqgadah
      661 skelnklplp sksvdwthfg gsppsdeirt lrdqllllhn qllyerfkrq qhalrnrrll
      721 rkvikaaale ehnaamkdql klqekdiqmw kvslqkeqar ynqlqeqrdt mvtklhsqir
      781 qlqhdreefy nqsqelqtkl edcrnmiael rielkkannk lsnsesvqqq meflnrqllv
      841 lgevnelyle qlqnkhsdtt kevemmkaay rkeleknrsh vlqqtqrldt sqkrileles
      901 hlakkdhlll eqkkyledvk lqargqlqaa esryeaqkri tqvfeleild lygrlekdgl
      961 lkkleeekae aaeaaeerld ccndgcsdsm vghneeasgh ngetktprps sargssgsrg
     1021 gggsssssse lstpekpphq ragpfssrwe ttmgeasasi pttvgslpss ksflgmkare
     1081 lfrnksesqc dedgmtssls eslktelgkd lgveakipln ldgphpsppt pdsvgqlhim
     1141 dynethhehs
//
LOCUS       NP_001394741            1217 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 9 precursor
            [Homo sapiens].
ACCESSION   NP_001394741
VERSION     NP_001394741.1
DBSOURCE    REFSEQ: accession NM_001407812.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1217)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1217)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1217)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1217)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1217)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1217)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1217)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1217)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1217)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1217)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.356797.1,
                                           SRR14038191.3312200.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1217
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1217
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 9 precursor"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=132884
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O00411.2)"
                     /calculated_mol_wt=4109
     Region          18..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          95..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          261..290
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          296..323
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          432..704
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          731..750
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          831..1217
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1217
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407812.1:26..3679"
                     /note="isoform 9 precursor is encoded by transcript
                     variant 9"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 msalcwgrga aglkralrpc grpglpgkeg taggvcgprr sssaspqeqd qdrrkdwghv
       61 ellevlqarv rqlqaesvse vvvnrvdvar lpecgsgdgs lqpprkvqmg akdatpvpcg
      121 rwakilekdk rtqqmrmqrl kaklqmpfqs gefkaltrrl qveprllskq magcledctr
      181 qapespweeq larllqeapg klsldveqap sgqhsqaqls gqqqrllaff kcclltdqlp
      241 lahhllvvhh gqrqkrkllt ldmynavmlg warqgafkel vyvlfmvkda gltpdllsya
      301 aalqcmgrqd qdagtiercl eqmsqeglkl qalftavlls eedratvlka vhkvkptfsl
      361 ppqlpppvnt skllrdvyak dgrvsypklh lplktlqclf ekqlhmelas rvcvvsvekp
      421 tlpskevkha rktlktlrdq wekalcralr etknrlerev yegrfslypf lcllderevv
      481 rmllqvlqal paqgesfttl arelsartfs rhvvqrqrvs gqvqalqnhy rkylcllasd
      541 aevpepclpr qyweelgape alreqpwplp vqmelgklla emlvqatqmp csldkphrss
      601 rlvpvlyhvy sfrnvqqigi lkphpayvql lekaaeptlt feavdvpmlc pplpwtsphs
      661 gafllsptkl mrtvegatqh qelletcppt alhgaldalt qlgncawrvn grvldlvlql
      721 fqakgcpqlg vpappseapq ppeahlphsa aparkaelrr elahcqkvar emhslraeal
      781 yrlslaqhlr drvfwlphnm dfrgrtypcp phfnhlgsdv arallefaqg rplgphgldw
      841 lkihlvnltg lkkreplrkr lafaeevmdd ildsadqplt grkwwmgaee pwqtlaccme
      901 vanavrasdp aayvshlpvh qdgscnglqh yaalgrdsvg aasvnlepsd vpqdvysgva
      961 aqvevfrrqd aqrgmrvaqv legfitrkvv kqtvmtvvyg vtryggrlqi ekrlrelsdf
     1021 pqvfkslqem fsgtraiqhw ltesarlish mgsvvewvtp lgvpviqpyr ldskvkqigg
     1081 giqsitythn gdisrkpntr kqkngfppnf ihsldsshmm ltalhcyrkg ltfvsvhdcy
     1141 wthaadvsvm nqvcreqfvr lhsepilqdl srflvkrfcs epqkileasq lketlqavpk
     1201 pgafdleqvk rstyffs
//
LOCUS       NP_001424929             942 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 3 isoform 4 [Homo sapiens].
ACCESSION   NP_001424929 XP_016862726 XP_054203925
VERSION     NP_001424929.1
DBSOURCE    REFSEQ: accession NM_001438000.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Wang,H., Lan,S., Wang,L., Zhao,J., Jia,X., Xu,J., Sun,G., Liu,L.,
            Gong,S., Wang,N., Shan,B., Zhang,F. and Zhang,Z.
  TITLE     Expression of circ-PHC3 enhances ovarian cancer progression via
            regulation of the miR-497-5p/SOX9 pathway
  JOURNAL   J Ovarian Res 16 (1), 142 (2023)
   PUBMED   37468993
  REMARK    GeneRIF: Expression of circ-PHC3 enhances ovarian cancer
            progression via regulation of the miR-497-5p/SOX9 pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 942)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 942)
  AUTHORS   Crea,F., Di Paolo,A., Liu,H.H., Polillo,M., Clermont,P.L.,
            Guerrini,F., Ciabatti,E., Ricci,F., Barate,C., Fontanelli,G.,
            Barsotti,S., Morganti,R., Danesi,R., Wang,Y., Petrini,M.,
            Galimberti,S. and Helgason,C.D.
  TITLE     Polycomb genes are associated with response to imatinib in chronic
            myeloid leukemia
  JOURNAL   Epigenomics 7 (5), 757-765 (2015)
   PUBMED   26343356
  REMARK    GeneRIF: Data show that polycomb-group proteins BMI1, PHC3, CBX6
            and CBX7 expression was significantly increased during imatinib
            treatment.
REFERENCE   6  (residues 1 to 942)
  AUTHORS   Deshpande,A.M., Akunowicz,J.D., Reveles,X.T., Patel,B.B.,
            Saria,E.A., Gorlick,R.G., Naylor,S.L., Leach,R.J. and Hansen,M.F.
  TITLE     PHC3, a component of the hPRC-H complex, associates with E2F6
            during G0 and is lost in osteosarcoma tumors
  JOURNAL   Oncogene 26 (12), 1714-1722 (2007)
   PUBMED   17001316
  REMARK    GeneRIF: loss of PHC3 may favor tumorigenesis by potentially
            disrupting the ability of cells to remain in G(0)
REFERENCE   7  (residues 1 to 942)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   8  (residues 1 to 942)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 942)
  AUTHORS   Tonkin,E., Hagan,D.M., Li,W. and Strachan,T.
  TITLE     Identification and characterisation of novel mammalian homologues
            of Drosophila polyhomeoticpermits new insights into relationships
            between members of the polyhomeotic family
  JOURNAL   Hum Genet 111 (4-5), 435-442 (2002)
   PUBMED   12384788
REFERENCE   10 (residues 1 to 942)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC023891.28 and AC008040.7.
            
            On or before Apr 14, 2025 this sequence version replaced
            XP_016862726.1, XP_054203925.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3029144.1,
                                           SRR14038193.537851.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.2"
     Protein         1..942
                     /product="polyhomeotic-like protein 3 isoform 4"
                     /note="early development regulator 3; polyhomeotic-like
                     protein 3; homolog of polyhomeotic 3; early development
                     regulatory protein 3; polyhomeotic like 3"
                     /calculated_mol_wt=101836
     Region          <305..>465
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     Region          873..941
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(891..892,926..927,930..931,934)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(902..906,908..909,912..913,917,922)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..942
                     /gene="PHC3"
                     /gene_synonym="EDR3; HPH3"
                     /coded_by="NM_001438000.1:19..2847"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:80012"
                     /db_xref="HGNC:HGNC:15682"
                     /db_xref="MIM:620031"
ORIGIN      
        1 maeaefkdhs tamdtepnpg tssvstttss tttttittss srmqqpqisv ysgsdrhavq
       61 viqqalhrpp ssaaqylqqm yaaqqqhlml htaalqqqhl sssqlqslaa vqaslssgrp
      121 stsptgsvtq qssmsqtsli ftpattvaav qsdipvvsss sssscqsaat qvqnltlrsq
      181 klgvlsssqn gppkstsqtq sltichnktt vtsskisqrd pspesnkkge spslesrsta
      241 vtrtssihql iapasyspiq phslikhqqi plhsppskvs hhqlilqqqq qqiqpitlqn
      301 stqdpppsqh ciplqnhglp papsnaqsqh cspiqshpsp ltvspnqsqs aqqsvvvspp
      361 pphspsqspt iiihpqaliq phplvssalq pgpnlqqsta nqvqataqln lpshlplpas
      421 pvvhigpvqq salvspgqqi vspshqqyss lqsspipias ppqmstsppa qipplplqsm
      481 qslqvqpeil sqgqvlvqna lvseeelpaa ealvqlpfqt lpppqtvavn lqvqppapvd
      541 ppvvyqvedv ceeempeesd ecvrmdrtpp pptlspaait vgrgedltse hplleqvelp
      601 avasvsasvi kspsdpshvs vpppplllpa attrsnstsm hssipsienk ppqaivkpqi
      661 lthviegfvi qeglepfpvs rssllieqpv kkrplldnqv insvcvqpel qnntkhadns
      721 sdtemedmia eetleemdse llkcefcgkm gyaneflrsk rfctmscakr ynvscskkfa
      781 lsrwnrkpdn qslghrgrrp sgpdgaareh ilrqlpityp saeedlashe dsvpsamttr
      841 lrrqserere relrdvrirk mpensdllpv aqtepsiwtv ddvwafihsl pgcqdiadef
      901 raqeidgqal lllkedhlms amniklgpal kicarinslk es
//
LOCUS       NP_001305873             320 aa            linear   PRI 21-NOV-2025
DEFINITION  vacuolar protein sorting-associated protein 26A isoform 3 [Homo
            sapiens].
ACCESSION   NP_001305873
VERSION     NP_001305873.1
DBSOURCE    REFSEQ: accession NM_001318944.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Hou,J., Wu,H., Xu,B., Shang,J., Xu,X., Li,G., Zhang,H., Zhang,W.,
            Deng,Y., Hong,X., Hu,T., Zhang,M. and Zhan,Y.
  TITLE     The Prognostic Value and the Oncogenic and Immunological Roles of
            Vacuolar Protein Sorting Associated Protein 26 A in Pancreatic
            Adenocarcinoma
  JOURNAL   Int J Mol Sci 24 (4), 3486 (2023)
   PUBMED   36834898
  REMARK    GeneRIF: The Prognostic Value and the Oncogenic and Immunological
            Roles of Vacuolar Protein Sorting Associated Protein 26 A in
            Pancreatic Adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Seaman,M.N., Harbour,M.E., Tattersall,D., Read,E. and Bright,N.
  TITLE     Membrane recruitment of the cargo-selective retromer subcomplex is
            catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP
            TBC1D5
  JOURNAL   J Cell Sci 122 (Pt 14), 2371-2382 (2009)
   PUBMED   19531583
  REMARK    GeneRIF: Membrane recruitment of the cargo-selective retromer
            subcomplex VPS35/29/26 is catalysed by the small GTPase Rab7 and
            inhibited by the Rab-GAP TBC1D5.
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Arighi,C.N., Hartnell,L.M., Aguilar,R.C., Haft,C.R. and
            Bonifacino,J.S.
  TITLE     Role of the mammalian retromer in sorting of the cation-independent
            mannose 6-phosphate receptor
  JOURNAL   J Cell Biol 165 (1), 123-133 (2004)
   PUBMED   15078903
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Seaman,M.N.
  TITLE     Cargo-selective endosomal sorting for retrieval to the Golgi
            requires retromer
  JOURNAL   J Cell Biol 165 (1), 111-122 (2004)
   PUBMED   15078902
REFERENCE   8  (residues 1 to 320)
  AUTHORS   Reddy,J.V. and Seaman,M.N.
  TITLE     Vps26p, a component of retromer, directs the interactions of Vps35p
            in endosome-to-Golgi retrieval
  JOURNAL   Mol Biol Cell 12 (10), 3242-3256 (2001)
   PUBMED   11598206
REFERENCE   9  (residues 1 to 320)
  AUTHORS   Haft,C.R., de la Luz Sierra,M., Bafford,R., Lesniak,M.A., Barr,V.A.
            and Taylor,S.I.
  TITLE     Human orthologs of yeast vacuolar protein sorting proteins Vps26,
            29, and 35: assembly into multimeric complexes
  JOURNAL   Mol Biol Cell 11 (12), 4105-4116 (2000)
   PUBMED   11102511
REFERENCE   10 (residues 1 to 320)
  AUTHORS   Mao,M., Fu,G., Wu,J.S., Zhang,Q.H., Zhou,J., Kan,L.X., Huang,Q.H.,
            He,K.L., Gu,B.W., Han,Z.G., Shen,Y., Gu,J., Yu,Y.P., Xu,S.H.,
            Wang,Y.X., Chen,S.J. and Chen,Z.
  TITLE     Identification of genes expressed in human CD34(+) hematopoietic
            stem/progenitor cells by expressed sequence tags and efficient
            full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 8175-8180 (1998)
   PUBMED   9653160
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA498726.1, AK309021.1,
            BX647725.1 and AL596223.3.
            
            Summary: This gene belongs to a group of vacuolar protein sorting
            (VPS) genes. The encoded protein is a component of a large
            multimeric complex, termed the retromer complex, involved in
            retrograde transport of proteins from endosomes to the trans-Golgi
            network. The close structural similarity between the yeast and
            human proteins that make up this complex suggests a similarity in
            function. Expression studies in yeast and mammalian cells indicate
            that this protein interacts directly with VPS35, which serves as
            the core of the retromer complex. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) includes an additional exon in
            the 5' region, and it thus differs in its 5' UTR and initiates
            translation at an alternate start codon, compared to variant 1. The
            encoded isoform (3) has a shorter and distinct N-terminus, compared
            to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.221137.1,
                                           SRR1803613.39130.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2144835
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..320
                     /product="vacuolar protein sorting-associated protein 26A
                     isoform 3"
                     /note="vacuolar protein sorting-associated protein 26A;
                     vesicle protein sorting 26A; vacuolar protein sorting 26
                     homolog A; VPS26 retromer complex comonent A"
                     /calculated_mol_wt=37608
     Region          45..276
                     /region_name="Vps26"
                     /note="Vacuolar protein sorting-associated protein 26;
                     pfam03643"
                     /db_xref="CDD:397622"
     CDS             1..320
                     /gene="VPS26A"
                     /gene_synonym="HB58; Hbeta58; PEP8A; VPS26"
                     /coded_by="NM_001318944.2:228..1190"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:9559"
                     /db_xref="HGNC:HGNC:12711"
                     /db_xref="MIM:605506"
ORIGIN      
        1 mtenpfqery svedlstfgm clcmvryvyd afykvslfsp flypvnlafk qpgkrlehqg
       61 iriefvgqie lfndksnthe fvnlvkelal pgeltqsrsy dfefmqvekp yesyiganvr
      121 lryflkvtiv rrltdlvkey dlivhqlaty pdvnnsikme vgiedclhie feynkskyhl
      181 kdvivgkiyf llvrikiqhm elqlikkeit gigpstttet etiakyeimd gapvkgesip
      241 irlflagydp tptmrdvnkk fsvryflnlv lvdeedrryf kqqeiilwrk apeklrkqrt
      301 nfhqrfespe sqasaeqpem
//
LOCUS       NP_001398042             432 aa            linear   PRI 21-NOV-2025
DEFINITION  tectonic-like complex member MKS1 isoform 6 [Homo sapiens].
ACCESSION   NP_001398042 XP_016880293
VERSION     NP_001398042.1
DBSOURCE    REFSEQ: accession NM_001411113.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Okazaki,M., Kobayashi,T., Chiba,S., Takei,R., Liang,L., Nakayama,K.
            and Katoh,Y.
  TITLE     Formation of the B9-domain protein complex MKS1-B9D2-B9D1 is
            essential as a diffusion barrier for ciliary membrane proteins
  JOURNAL   Mol Biol Cell 31 (20), 2259-2268 (2020)
   PUBMED   32726168
  REMARK    GeneRIF: Formation of the B9-domain protein complex MKS1-B9D2-B9D1
            is essential as a diffusion barrier for ciliary membrane proteins.
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Goetz,S.C., Bangs,F., Barrington,C.L., Katsanis,N. and
            Anderson,K.V.
  TITLE     The Meckel syndrome- associated protein MKS1 functionally interacts
            with components of the BBSome and IFT complexes to mediate ciliary
            trafficking and hedgehog signaling
  JOURNAL   PLoS One 12 (3), e0173399 (2017)
   PUBMED   28291807
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Dawe,H.R., Smith,U.M., Cullinane,A.R., Gerrelli,D., Cox,P.,
            Badano,J.L., Blair-Reid,S., Sriram,N., Katsanis,N.,
            Attie-Bitach,T., Afford,S.C., Copp,A.J., Kelly,D.A., Gull,K. and
            Johnson,C.A.
  TITLE     The Meckel-Gruber Syndrome proteins MKS1 and meckelin interact and
            are required for primary cilium formation
  JOURNAL   Hum Mol Genet 16 (2), 173-186 (2007)
   PUBMED   17185389
  REMARK    GeneRIF: The Meckel-Gruber Syndrome proteins MKS1 and meckelin
            interact and are required for primary cilium formation.
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Kyttala,M., Tallila,J., Salonen,R., Kopra,O., Kohlschmidt,N.,
            Paavola-Sakki,P., Peltonen,L. and Kestila,M.
  TITLE     MKS1, encoding a component of the flagellar apparatus basal body
            proteome, is mutated in Meckel syndrome
  JOURNAL   Nat Genet 38 (2), 155-157 (2006)
   PUBMED   16415886
  REMARK    GeneRIF: identification of a gene, MKS1,(Meckel syndrome) mutated
            in MKS families linked to 17q.
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Paavola,P., Salonen,R., Weissenbach,J. and Peltonen,L.
  TITLE     The locus for Meckel syndrome with multiple congenital anomalies
            maps to chromosome 17q21-q24
  JOURNAL   Nat Genet 11 (2), 213-215 (1995)
   PUBMED   7550354
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
REFERENCE   10 (residues 1 to 432)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005962.1.
            
            On Aug 22, 2022 this sequence version replaced XP_016880293.1.
            
            Summary: The protein encoded by this gene localizes to the basal
            body and is required for formation of the primary cilium in
            ciliated epithelial cells. Mutations in this gene result in Meckel
            syndrome type 1 and in Bardet-Biedl syndrome type 13. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Sep 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2608369.1,
                                           SRR5189667.133190.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q22"
     Protein         1..432
                     /product="tectonic-like complex member MKS1 isoform 6"
                     /note="POC12 centriolar protein homolog; meckel syndrome
                     type 1 protein; tectonic-like complex member MKS1"
                     /calculated_mol_wt=50081
     Region          313..>424
                     /region_name="B9-C2"
                     /note="Ciliary basal body-associated, B9 protein;
                     pfam07162"
                     /db_xref="CDD:462108"
     CDS             1..432
                     /gene="MKS1"
                     /gene_synonym="BBS13; JBTS28; MES; MKS; POC12"
                     /coded_by="NM_001411113.1:26..1324"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS92365.1"
                     /db_xref="GeneID:54903"
                     /db_xref="HGNC:HGNC:7121"
                     /db_xref="MIM:609883"
ORIGIN      
        1 maetvwstdt geavyrsrdp vrnlrlrvhl qritssnflh yqpaaelgkd lidlatfrpq
       61 ptasghrpee deeeeivigw qeklfsqfev dlyqnetacq spldyqyrqe ilklensggk
      121 knrriftytd sdrytnleeh cqrmttaase vpsflverma nvrrrrqdrr gmeggilksr
      181 ivtwepseef vrnnhvintp lqtmhimadl gpykklgykk yehvlctlkv dsngvitvkp
      241 dftglkgpyr ietegekqel wkytidnvsp haqpeeeere rrvfkdlygr hkeylsslvg
      301 tdfemtvpga lrlfvngevv saqgyeydnl yvhffvelpt ahwsspafqq lsgvtqtctt
      361 kslamdkvah fsypftfeaf flhedessda lpewpvlyce vlsldfwqry rvegygavvl
      421 patpatmtwp wh
//
LOCUS       NP_001427524             409 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform k [Homo sapiens].
ACCESSION   NP_001427524
VERSION     NP_001427524.1
DBSOURCE    REFSEQ: accession NM_001440595.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 409)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 409)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 409)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 409)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 409)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2894879.1,
                                           SRR18074968.3137224.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..409
                     /product="polycomb protein EED isoform k"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=46536
     Region          <83..269
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          96..140
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          148..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          193..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          240..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          309..382
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..409
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001440595.1:478..1707"
                     /note="isoform k is encoded by transcript variant 11"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdendd avsiesgtnt erpdtptntp
       61 napgrkswgk gkwkskkcky sfkcvnslke dhnqplfgvq fnwhskegdp lvfatvgsnr
      121 vtlyechsqg eirllqsyvd adadenfytc awtydsntsh pllavagsrg iiriinpitm
      181 qcikhyvghg nainelkfhp rdpnlllsvs kdhalrlwni qtdtlvaifg gveghrdevl
      241 sadydllgek imscgmdhsl klwrinskrm mnaikesydy npnktnrpfi sqkihfpdfs
      301 trdihrnyvd cvrwlgdlil sksgrailhs hqqcmrdpvs pnlrqhlsce naivcwkpgk
      361 meddidkikp sesnvtilgr fdysqcdiwy mrfsmdfwqk vstyfyilk
//
LOCUS       NP_001424996             224 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding protein with multiple splicing isoform D [Homo
            sapiens].
ACCESSION   NP_001424996 XP_016868473 XP_054215594
VERSION     NP_001424996.1
DBSOURCE    REFSEQ: accession NM_001438067.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Gan,P., Wang,Z., Bezprozvannaya,S., McAnally,J.R., Tan,W., Li,H.,
            Bassel-Duby,R., Liu,N. and Olson,E.N.
  TITLE     RBPMS regulates cardiomyocyte contraction and cardiac function
            through RNA alternative splicing
  JOURNAL   Cardiovasc Res 120 (1), 56-68 (2024)
   PUBMED   37890031
  REMARK    GeneRIF: RBPMS regulates cardiomyocyte contraction and cardiac
            function through RNA alternative splicing.
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Gong,T.T., Liu,F.H., Xiao,Q., Li,Y.Z., Wei,Y.F., Xu,H.L., Cao,F.,
            Sun,M.L., Jiang,F.L., Tao,T., Ma,Q.P., Qin,X., Song,Y., Gao,S.,
            Wu,L., Zhao,Y.H., Huang,D.H. and Wu,Q.J.
  TITLE     SH3RF2 contributes to cisplatin resistance in ovarian cancer cells
            by promoting RBPMS degradation
  JOURNAL   Commun Biol 7 (1), 67 (2024)
   PUBMED   38195842
  REMARK    GeneRIF: SH3RF2 contributes to cisplatin resistance in ovarian
            cancer cells by promoting RBPMS degradation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Yang,Y., Lee,G.C., Nakagaki-Silva,E., Huang,Y., Peacey,M.,
            Partridge,R., Gooding,C. and Smith,C.W.J.
  TITLE     Cell-type specific regulator RBPMS switches alternative splicing
            via higher-order oligomerization and heterotypic interactions with
            other splicing regulators
  JOURNAL   Nucleic Acids Res 51 (18), 9961-9982 (2023)
   PUBMED   37548402
  REMARK    GeneRIF: Cell-type specific regulator RBPMS switches alternative
            splicing via higher-order oligomerization and heterotypic
            interactions with other splicing regulators.
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Bartsch,D., Kalamkar,K., Ahuja,G., Lackmann,J.W., Hescheler,J.,
            Weber,T., Bazzi,H., Clamer,M., Mendjan,S., Papantonis,A. and
            Kurian,L.
  TITLE     mRNA translational specialization by RBPMS presets the competence
            for cardiac commitment in hESCs
  JOURNAL   Sci Adv 9 (13), eade1792 (2023)
   PUBMED   36989351
  REMARK    GeneRIF: mRNA translational specialization by RBPMS presets the
            competence for cardiac commitment in hESCs.
REFERENCE   6  (residues 1 to 224)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   7  (residues 1 to 224)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 224)
  AUTHORS   Sun,Y., Ding,L., Zhang,H., Han,J., Yang,X., Yan,J., Zhu,Y., Li,J.,
            Song,H. and Ye,Q.
  TITLE     Potentiation of Smad-mediated transcriptional activation by the
            RNA-binding protein RBPMS
  JOURNAL   Nucleic Acids Res 34 (21), 6314-6326 (2006)
   PUBMED   17099224
REFERENCE   9  (residues 1 to 224)
  AUTHORS   Hillman,R.T., Green,R.E. and Brenner,S.E.
  TITLE     An unappreciated role for RNA surveillance
  JOURNAL   Genome Biol 5 (2), R8 (2004)
   PUBMED   14759258
REFERENCE   10 (residues 1 to 224)
  AUTHORS   Shimamoto,A., Kitao,S., Ichikawa,K., Suzuki,N., Yamabe,Y.,
            Imamura,O., Tokutake,Y., Satoh,M., Matsumoto,T., Kuromitsu,J.,
            Kataoka,H., Sugawara,K., Sugawara,M., Sugimoto,M., Goto,M. and
            Furuichi,Y.
  TITLE     A unique human gene that spans over 230 kb in the human chromosome
            8p11-12 and codes multiple family proteins sharing RNA-binding
            motifs
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 10913-10917 (1996)
   PUBMED   8855282
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC109329.8 and AC011204.6.
            
            On or before Apr 15, 2025 this sequence version replaced
            XP_016868473.1, XP_054215594.1.
            
            Summary: This gene encodes a member of the RNA recognition motif
            family of RNA-binding proteins. The RNA recognition motif is
            between 80-100 amino acids in length and family members contain one
            to four copies of the motif. The RNA recognition motif consists of
            two short stretches of conserved sequence, as well as a few highly
            conserved hydrophobic residues. The encoded protein has a single,
            putative RNA recognition motif in its N-terminus. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Jun 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1777278.1,
                                           SRR14038195.1266688.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p12"
     Protein         1..224
                     /product="RNA-binding protein with multiple splicing
                     isoform D"
                     /note="heart and RRM expressed sequence; RNA binding
                     protein with multiple splicing"
                     /calculated_mol_wt=24866
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q93062.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVB0; propagated from
                     UniProtKB/Swiss-Prot (Q93062.1)"
     Region          23..98
                     /region_name="RRM_RBPMS"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     RNA-binding protein with multiple splicing (RBP-MS);
                     cd12682"
                     /db_xref="CDD:410083"
     Site            27
                     /site_type="other"
                     /note="Interaction with RNA.
                     /evidence=ECO:0000269|PubMed:26347403; propagated from
                     UniProtKB/Swiss-Prot (Q93062.1)"
     Site            61
                     /site_type="other"
                     /note="Interaction with RNA.
                     /evidence=ECO:0000269|PubMed:26347403; propagated from
                     UniProtKB/Swiss-Prot (Q93062.1)"
     Region          <64..>165
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     Region          98..105
                     /region_name="Interaction with RNA.
                     /evidence=ECO:0000269|PubMed:26347403"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93062.1)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q93062.1)"
     CDS             1..224
                     /gene="RBPMS"
                     /gene_synonym="HERMES"
                     /coded_by="NM_001438067.1:553..1227"
                     /note="isoform D is encoded by transcript variant 5"
                     /db_xref="GeneID:11030"
                     /db_xref="HGNC:HGNC:19097"
                     /db_xref="MIM:601558"
ORIGIN      
        1 mnnggkaeke ntpseanlqe eevrtlfvsg lpldikprel yllfrpfkgy egslikltsk
       61 qpvgfvsfds rseaeaakna lngirfdpei pqtlrlefak antkmaknkl vgtpnpstpl
      121 pntvpqfiar epyeltvpal ypsspevwap yplypaelap alpppaftyp aslhaqvidt
      181 hrpglhslhh qsfqtwfpra hhttntypan rstlkrlmip skss
//
LOCUS       NP_001394400            2459 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform s [Homo sapiens].
ACCESSION   NP_001394400
VERSION     NP_001394400.1
DBSOURCE    REFSEQ: accession NM_001407471.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2459)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2459)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2459)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2459)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2459)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2459)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2459)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2459)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2459)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2459)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3676110.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2161674, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2459
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2459
                     /product="adenomatous polyposis coli protein isoform s"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=268202
     Region          <24..82
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          81..124
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(115,119,123,158,162,166,202,206,210)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          128..169
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          132..169
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          176..211
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          219..260
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          265..305
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          269..303
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          307..347
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          311..347
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          348..635
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          652..751
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          873..>890
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          899..984
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <919..1317
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          987..1009
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1253..1276
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1278..1331
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1332..1353
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1362..1455
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1489..1563
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1649..1668
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1839..2184
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2286..2459
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2459
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407471.1:1095..8474"
                     /note="isoform s is encoded by transcript variant 34"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 mdhetasvls sssthsaprr ltshlgtkir aycetcwewq eahepgmdqd knpmpapveh
       61 qicpavcvlm klsfdeehrh amnelgglqa iaellqvdce mygltndhys itlrryagma
      121 ltnltfgdva nkatlcsmkg cmralvaqlk sesedlqqvi asvlrnlswr advnskktlr
      181 evgsvkalme calevkkest lksvlsalwn lsahctenka dicavdgala flvgtltyrs
      241 qtntlaiies gggilrnvss liatnedhrq ilrennclqt llqhlkshsl tivsnacgtl
      301 wnlsarnpkd qealwdmgav smlknlihsk hkmiamgsaa alrnlmanrp akykdanims
      361 pgsslpslhv rkqkaleael daqhlsetfd nidnlspkas hrskqrhkqs lygdyvfdtn
      421 rhddnrsdnf ntgnmtvlsp ylnttvlpss sssrgsldss rsekdrsler ergiglgnyh
      481 patenpgtss krglqistta aqiakvmeev saihtsqedr ssgsttelhc vtdernalrr
      541 ssaahthsnt ynftksensn rtcsmpyakl eykrssndsl nsvsssdgyg krgqmkpsie
      601 syseddeskf csygqypadl ahkihsanhm ddndgeldtp inyslkysde qlnsgrqsps
      661 qnerwarpkh iiedeikqse qrqsrnqstt ypvytestdd khlkfqphfg qqecvspyrs
      721 rgangsetnr vgsnhginqn vsqslcqedd yeddkptnys eryseeeqhe eeerptnysi
      781 kyneekrhvd qpidyslkya tdipssqkqs fsfsksssgq ssktehmsss sentstpssn
      841 akrqnqlhps saqsrsgqpq kaatckvssi nqetiqtycv edtpicfsrc sslsslssae
      901 deigcnqttq eadsantlqi aeikekigtr saedpvsevp avsqhprtks srlqgsslss
      961 esarhkavef ssgakspsks gaqtpksppe hyvqetplmf srctsvssld sfesrsiass
     1021 vqsepcsgmv sgiispsdlp dspgqtmpps rsktpppppq taqtkrevpk nkaptaekre
     1081 sgpkqaavna avqrvqvlpd adtllhfate stpdgfscss slsalsldep fiqkdvelri
     1141 mppvqendng neteseqpke snenqekeae ktidsekdll ddsddddiei leeciisamp
     1201 tkssrkakkp aqtasklppp varkpsqlpv ykllpsqnrl qpqkhvsftp gddmprvycv
     1261 egtpinfsta tslsdlties ppnelaageg vrggaqsgef ekrdtipteg rstdeaqggk
     1321 tssvtipeld dnkaeegdil aecinsampk gkshkpfrvk kimdqvqqas asssapnknq
     1381 ldgkkkkpts pvkpipqnte yrtrvrknad sknnlnaerv fsdnkdskkq nlknnskvfn
     1441 dklpnnedrv rgsfafdsph hytpiegtpy cfsrndslss ldfddddvdl srekaelrka
     1501 kenkeseakv tshteltsnq qsanktqaia kqpinrgqpk pilqkqstfp qsskdipdrg
     1561 aatdeklqnf aientpvcfs hnsslsslsd idqennnken epiketeppd sqgepskpqa
     1621 sgyapksfhv edtpvcfsrn sslsslsids eddllqecis sampkkkkps rlkgdnekhs
     1681 prnmggilge dltldlkdiq rpdsehglsp dsenfdwkai qegansivss lhqaaaaacl
     1741 srqassdsds ilslksgisl gspfhltpdq eekpftsnkg prilkpgeks tletkkiese
     1801 skgikggkkv ykslitgkvr snseisgqmk qplqanmpsi srgrtmihip gvrnssssts
     1861 pvskkgpplk tpaskspseg qtattsprga kpsvkselsp varqtsqigg sskapsrsgs
     1921 rdstpsrpaq qplsrpiqsp grnsispgrn gisppnklsq lprtsspsta stkssgsgkm
     1981 sytspgrqms qqnltkqtgl sknassiprs esaskglnqm nngngankkv elsrmsstks
     2041 sgsesdrser pvlvrqstfi keapsptlrr kleesasfes lspssrpasp trsqaqtpvl
     2101 spslpdmsls thssvqaggw rklppnlspt ieyndgrpak rhdiarshse spsrlpinrs
     2161 gtwkrehskh ssslprvstw rrtgssssil sassesseka ksedekhvns isgtkqsken
     2221 qvsakgtwrk ikenefsptn stsqtvssga tngaesktli yqmapavskt edvwvriedc
     2281 pinnprsgrs ptgntppvid svsekanpni kdskdnqakq nvgngsvpmr tvglenrlns
     2341 fiqvdapdqk gteikpgqnn pvpvsetnes sivertpfss sssskhssps gtvaarvtpf
     2401 nynpsprkss adstsarpsq iptpvnnntk krdsktdste ssgtqspkrh sgsylvtsv
//
LOCUS       NP_001185730            1621 aa            linear   PRI 21-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4 gamma 3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001185730
VERSION     NP_001185730.1
DBSOURCE    REFSEQ: accession NM_001198801.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1621)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1621)
  AUTHORS   Kang,J.Y., Wen,Z., Pan,D., Zhang,Y., Li,Q., Zhong,A., Yu,X.,
            Wu,Y.C., Chen,Y., Zhang,X., Kou,P.C., Geng,J., Wang,Y.Y., Hua,M.M.,
            Zong,R., Li,B., Shi,H.J., Li,D., Fu,X.D., Li,J., Nelson,D.L.,
            Guo,X., Zhou,Y., Gou,L.T., Huang,Y. and Liu,M.F.
  TITLE     LLPS of FXR1 drives spermiogenesis by activating translation of
            stored mRNAs
  JOURNAL   Science 377 (6607), eabj6647 (2022)
   PUBMED   35951695
REFERENCE   3  (residues 1 to 1621)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1621)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 1621)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1621)
  AUTHORS   Waskiewicz,A.J., Johnson,J.C., Penn,B., Mahalingam,M., Kimball,S.R.
            and Cooper,J.A.
  TITLE     Phosphorylation of the cap-binding protein eukaryotic translation
            initiation factor 4E by protein kinase Mnk1 in vivo
  JOURNAL   Mol Cell Biol 19 (3), 1871-1880 (1999)
   PUBMED   10022874
REFERENCE   7  (residues 1 to 1621)
  AUTHORS   Pyronnet,S., Imataka,H., Gingras,A.C., Fukunaga,R., Hunter,T. and
            Sonenberg,N.
  TITLE     Human eukaryotic translation initiation factor 4G (eIF4G) recruits
            mnk1 to phosphorylate eIF4E
  JOURNAL   EMBO J 18 (1), 270-279 (1999)
   PUBMED   9878069
REFERENCE   8  (residues 1 to 1621)
  AUTHORS   Gingras,A.C., Raught,B. and Sonenberg,N.
  TITLE     eIF4 initiation factors: effectors of mRNA recruitment to ribosomes
            and regulators of translation
  JOURNAL   Annu Rev Biochem 68, 913-963 (1999)
   PUBMED   10872469
  REMARK    Review article
REFERENCE   9  (residues 1 to 1621)
  AUTHORS   Imataka,H., Gradi,A. and Sonenberg,N.
  TITLE     A newly identified N-terminal amino acid sequence of human eIF4G
            binds poly(A)-binding protein and functions in poly(A)-dependent
            translation
  JOURNAL   EMBO J 17 (24), 7480-7489 (1998)
   PUBMED   9857202
REFERENCE   10 (residues 1 to 1621)
  AUTHORS   Gradi,A., Imataka,H., Svitkin,Y.V., Rom,E., Raught,B., Morino,S.
            and Sonenberg,N.
  TITLE     A novel functional human eukaryotic translation initiation factor
            4G
  JOURNAL   Mol Cell Biol 18 (1), 334-342 (1998)
   PUBMED   9418880
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031005.2, AL627311.16,
            AL358392.19 and AL606477.11.
            
            Summary: The protein encoded by this gene is thought to be part of
            the eIF4F protein complex, which is involved in mRNA cap
            recognition and transport of mRNAs to the ribosome. Interestingly,
            a microRNA (miR-520c-3p) has been found that negatively regulates
            synthesis of the encoded protein, and this leads to a global
            decrease in protein translation and cell proliferation. Therefore,
            this protein is a key component of the anti-tumor activity of
            miR-520c-3p. [provided by RefSeq, May 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072413.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1621
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     Protein         1..1621
                     /product="eukaryotic translation initiation factor 4 gamma
                     3 isoform 1"
                     /note="eIF-4-gamma 3; eIF-4-gamma II"
                     /calculated_mol_wt=180368
     Region          <10..>295
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     Region          791..1019
                     /region_name="MIF4G"
                     /note="MIF4G domain; pfam02854"
                     /db_xref="CDD:397130"
     Region          1258..1370
                     /region_name="MA3"
                     /note="MA3 domain; pfam02847"
                     /db_xref="CDD:397128"
     Region          1464..1592
                     /region_name="W2_eIF4G1_like"
                     /note="C-terminal W2 domain of eukaryotic translation
                     initiation factor 4 gamma 1 and similar proteins; cd11559"
                     /db_xref="CDD:211397"
     Region          <1571..1617
                     /region_name="W2"
                     /note="C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon;
                     cl17013"
                     /db_xref="CDD:473053"
     CDS             1..1621
                     /gene="EIF4G3"
                     /gene_synonym="eIF-4G 3; eIF4G 3; eIF4GII"
                     /coded_by="NM_001198801.3:632..5497"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS72723.1"
                     /db_xref="GeneID:8672"
                     /db_xref="HGNC:HGNC:3298"
                     /db_xref="MIM:603929"
ORIGIN      
        1 mnsqpqtrsp ffqrpqiqpp ratipnssps irpgaqtpta vyqanqhimm vnhlpmpypv
       61 pqgpqycipq yrhsgppyvg ppqqypvqpp gpgpfypgpg pgdfpnaygt pfypsqpvyq
      121 sapiivptqq qpppakrekk tirirdpnqg gkditeeims gggsrnptpp igrptstptp
      181 pqlpsqvpeh spvvygtves ahlaastpvt aasdqkqeek pkpdpvlksp spvlrlvlsg
      241 ekkeqegqts ettaivsiae lplppspttv ssvarstiaa ptssalssqp ifttaiddrc
      301 elsspredti pipsltscte tsdplptnen dddickkpcs vapndiplvs stnlineing
      361 vseklsates iveivkqevl pltleleile nppeemklec ipapitpstv psfpptpptp
      421 paspphtpvi vpaaattvss psaaitvqrv leedesirtc lsedakeiqn kieveadgqt
      481 eeildsqnln srrspvpaqi aitvpktwkk pkdrtrttee mleaelelka eeelsidkvl
      541 eseqdkmsqg fhperdpsdl kkvkaveeng eeaepvrnga esvsegegid ansgstdssg
      601 dgvtfpfkpe swkptdtegk kqydreflld fqfmpaciqk peglppisdv vldkinqpkl
      661 pmrtldpril prgpdftpaf adfgrqtpgg rgvpickvqs rhglpileqs kaptcpplvm
      721 shppmkslpl gllnvgsrrs qpgqrreprk iitvsvkedv hlkkaenawk psqkrdsqad
      781 dpeniktqel frkvrsilnk ltpqmfnqlm kqvsgltvdt eerlkgvidl vfekaideps
      841 fsvayanmcr clvtlkvpma dkpgntvnfr klllnrcqke fekdkadddv fekkqkelea
      901 asapeertrl hdeleeakdk arrrsignik figelfklkm lteaimhdcv vkllknhdee
      961 sleclcrllt tigkdldfek akprmdqyfn qmekivkerk tssrirfmlq dvidlrlcnw
     1021 vsrradqgpk tieqihkeak ieeqeeqrkv qqlmtkekrr pgvqrvdegg wntvqgakns
     1081 rvldpskflk itkptideki qlvpkaqlgs wgkgssggak asetdalrss asslnrfsal
     1141 qppapsgstp stpvefdsrr tltsrgsmgr ekndkplpsa tarpntfmrg gsskdlldnq
     1201 sqeeqrreml etvkqltggv dvernsteae rnktresakp eisamsahdk aalseeeler
     1261 ksksiidefl hindfkeamq cveelnaqgl lhvfvrvgve stlersqitr dhmgqllyql
     1321 vqseklskqd ffkgfsetle laddmaidip hiwlylaelv tpmlkeggis mreltiefsk
     1381 pllpvgragv llseilhllc kqmshkkvga lwreadlswk dflpegedvh nflleqkldf
     1441 iesdspcsse alskkelsae elykrlekli iedkandeqi fdwveanlde iqmssptflr
     1501 almtavckaa iiadsstfrv dtavikqrvp illkyldsdt ekelqalyal qasivkldqp
     1561 anllrmffdc lydeevised afykwesskd paeqngkgva lksvtafftw lreaeeesed
     1621 n
//
LOCUS       NP_060919               1119 aa            linear   PRI 21-NOV-2025
DEFINITION  ubiquitin-associated protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_060919
VERSION     NP_060919.4
DBSOURCE    REFSEQ: accession NM_018449.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1119)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1119)
  AUTHORS   Lv,Z., Shi,Y., Wu,H., Cao,K., Liu,X. and Wang,C.
  TITLE     Novel Circular RNA CircUBAP2 Drives Tumor Progression by Regulating
            the miR-143/TFAP2B Axis in Prostate Cancer
  JOURNAL   Protein Pept Lett 31 (1), 61-73 (2024)
   PUBMED   37962045
  REMARK    GeneRIF: Novel Circular RNA CircUBAP2 Drives Tumor Progression by
            Regulating the miR-143/TFAP2B Axis in Prostate Cancer.
REFERENCE   3  (residues 1 to 1119)
  AUTHORS   Chou,M.C., Wang,Y.H., Chen,F.Y., Kung,C.Y., Wu,K.P., Kuo,J.C.,
            Chan,S.J., Cheng,M.L., Lin,C.Y., Chou,Y.C., Ho,M.C., Firestine,S.,
            Huang,J.R. and Chen,R.H.
  TITLE     PAICS ubiquitination recruits UBAP2 to trigger phase separation for
            purinosome assembly
  JOURNAL   Mol Cell 83 (22), 4123-4140 (2023)
   PUBMED   37848033
  REMARK    GeneRIF: PAICS ubiquitination recruits UBAP2 to trigger phase
            separation for purinosome assembly.
REFERENCE   4  (residues 1 to 1119)
  AUTHORS   Herlihy,A.E., Boeing,S., Weems,J.C., Walker,J.,
            Dirac-Svejstrup,A.B., Lehner,M.H., Conaway,R.C., Conaway,J.W. and
            Svejstrup,J.Q.
  TITLE     UBAP2/UBAP2L regulate UV-induced ubiquitylation of RNA polymerase
            II and are the human orthologues of yeast Def1
  JOURNAL   DNA Repair (Amst) 115, 103343 (2022)
   PUBMED   35633597
  REMARK    GeneRIF: UBAP2/UBAP2L regulate UV-induced ubiquitylation of RNA
            polymerase II and are the human orthologues of yeast Def1.
REFERENCE   5  (residues 1 to 1119)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 1119)
  AUTHORS   Zuo,L., Saba,L., Wang,K., Zhang,X., Krystal,J.H., Tabakoff,B. and
            Luo,X.
  TITLE     Exome-wide association study of replicable nonsynonymous variants
            conferring risk for alcohol dependence
  JOURNAL   J Stud Alcohol Drugs 74 (4), 622-625 (2013)
   PUBMED   23739027
  REMARK    GeneRIF: By incorporating the information from bioinformatics and
            RNA expression analyses, we identified at least two of the most
            promising risk genes for alcohol dependence: APOER2 and UBAP2
REFERENCE   7  (residues 1 to 1119)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 1119)
  AUTHORS   Venturelli,E., Villa,C., Fenoglio,C., Clerici,F., Marcone,A.,
            Benussi,L., Ghidoni,R., Gallone,S., Scalabrini,D., Cortini,F.,
            Fumagalli,G., Cappa,S., Binetti,G., Franceschi,M., Rainero,I.,
            Giordana,M.T., Mariani,C., Bresolin,N., Scarpini,E. and
            Galimberti,D.
  TITLE     Is KIF24 a genetic risk factor for Frontotemporal Lobar
            Degeneration?
  JOURNAL   Neurosci Lett 482 (3), 240-244 (2010)
   PUBMED   20670673
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1119)
  AUTHORS   Dieci,G., Preti,M. and Montanini,B.
  TITLE     Eukaryotic snoRNAs: a paradigm for gene expression flexibility
  JOURNAL   Genomics 94 (2), 83-88 (2009)
   PUBMED   19446021
  REMARK    GeneRIF: UBAP2 serves as a host gene for snoRNAs
            Review article
REFERENCE   10 (residues 1 to 1119)
  AUTHORS   Hofmann,K. and Bucher,P.
  TITLE     The UBA domain: a sequence motif present in multiple enzyme classes
            of the ubiquitination pathway
  JOURNAL   Trends Biochem Sci 21 (5), 172-173 (1996)
   PUBMED   8871400
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354989.13 and AL139113.21.
            
            On Feb 24, 2022 this sequence version replaced NP_060919.3.
            
            Summary: The protein encoded by this gene contains a UBA (ubiquitin
            associated) domain, which is characteristic of proteins that
            function in the ubiquitination pathway. This gene may show
            increased expression in the adrenal gland and lymphatic tissues.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1123855.1,
                                           SRR14038193.1955016.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1119
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..1119
                     /product="ubiquitin-associated protein 2 isoform 1"
                     /note="AD-012 protein; RNA polymerase II degradation
                     factor UBAP2"
                     /calculated_mol_wt=116985
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T6F2.1)"
     Region          53..90
                     /region_name="UBA_UBP2_like"
                     /note="UBA domain found in ubiquitin-associated protein 2
                     (UBAP-2) like proteins; cd14277"
                     /db_xref="CDD:270463"
     Region          110..202
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T6F2.1)"
     Site            166
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q5T6F2.1)"
     Region          300..>681
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          385..476
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T6F2.1)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5T6F2.1)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5T6F2.1)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5T6F2.1)"
     Region          512..541
                     /region_name="DUF3697"
                     /note="Ubiquitin-associated protein 2; pfam12478"
                     /db_xref="CDD:372135"
     Region          622..736
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T6F2.1)"
     Site            630
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5T6F2.1)"
     Region          853..905
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T6F2.1)"
     Region          937..966
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T6F2.1)"
     Region          982..1020
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T6F2.1)"
     Region          1082..1119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T6F2.1)"
     CDS             1..1119
                     /gene="UBAP2"
                     /gene_synonym="UBAP-2"
                     /coded_by="NM_018449.4:114..3473"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6547.1"
                     /db_xref="GeneID:55833"
                     /db_xref="HGNC:HGNC:14185"
ORIGIN      
        1 mmtsvssdhc rgarekpqis aaqstqpqkq vvqataeqmr laqvifdknd sdfeakvkql
       61 mevtgknqde civalhdcng dvnkainill egnsdttswe tvgckkknfa kensenkenr
      121 ekksekessr grgnnnrkgr ggnrgrefrg eengidcnqv dkpsdrgkra rgrgfgrgrg
      181 rgagrfstqg mgtfnpadys dststdvcgt klvvweaaqn gadegtelas nthniaqdls
      241 nkssyglkga wknsveewtt edwtedlset kvftassapa enhilpgqsi dlvallqkpv
      301 phsqaseans fetsqqqgfg qalvftnsqh nnqmapgtgs stavnscspq slssvlgsgf
      361 gelappkman itssqildql kapslgqftt tpstqqnsts hpttttswdl kpptsqssvl
      421 shldfksqpe pspvlsqlsq rqqhqsqavt vpppglesfp sqaklrestp gdspstvnkl
      481 lqlpsttien isvsvhqpqp khiklakrri ppaskipasa vempgsadvt glnvqfgale
      541 fgsepslsef gsapssensn qipislysks lseplntsls mtsavqnsty ttsvitscsl
      601 tssslnsasp vamsssydqs svhnripyqs pvsssesapg timnghgggr sqqtldtpkt
      661 tgppsalpsv sslpsttsct allpstsqht gdltssplsq lssslsshqs slsahaalss
      721 stshthasve sasshqssat fstaatsvss sassgaslss smntanslcl ggtpasasss
      781 ssraaplvts gkappnlpqg vppllhnqyl vgpggllpay piygydelqm lqsrlpvdyy
      841 gipfaaptal asrdgslann pypgdvtkfg rgdsaspapa ttpaqpqqsq sqthhtaqqp
      901 fvnpalppgy sytglpyytg mpsafqygpt mfvppasakq hgvnlstptp pfqqasgygq
      961 hgystgyddl tqgtaagdys kggyagssqa pnksagsgpg kgvsvssstt glpdmtgsvy
     1021 nktqtfdkqg fhagtpppfs lpsvlgstgp lasgaapgya pppflhilpa hqqphsqllh
     1081 hhlpqdaqsg sgqrsqpssl qpksqaskpa ygnspywtn
//
LOCUS       NP_001427736            1072 aa            linear   PRI 21-NOV-2025
DEFINITION  ubiquitin-like modifier-activating enzyme 1 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001427736 XP_011542256 XP_054183667
VERSION     NP_001427736.1
DBSOURCE    REFSEQ: accession NM_001440807.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Sirenko,M., Bernard,E., Creignou,M., Domenico,D., Farina,A., Arango
            Ossa,J.E., Kosmider,O., Hasserjian,R., Jadersten,M., Germing,U.,
            Sanz,G., van de Loosdrecht,A.A., Gurnari,C., Follo,M.Y., Thol,F.,
            Zamora,L., Pinheiro,R.F., Pellagatti,A., Elias,H.K., Haase,D.,
            Sander,B., Orna,E., Zoldan,K., Eder,L.N., Sperr,W.R.,
            Thalhammer,R., Ganster,C., Ades,L., Tobiasson,M., Palomo,L., Della
            Porta,M.G., Huberman,K., Fenaux,P., Belickova,M., Savona,M.R.,
            Klimek,V.M., Santos,F.P.S., Boultwood,J., Kotsianidis,I.,
            Santini,V., Sole,F., Platzbecker,U., Heuser,M., Valent,P.,
            Finelli,C., Voso,M.T., Shih,L.Y., Ogawa,S., Fontenay,M.,
            Jansen,J.H., Cervera,J., Ebert,B.L., Bejar,R., Greenberg,P.L.,
            Gattermann,N., Malcovati,L., Cazzola,M., Beck,D.B.,
            Hellstrom-Lindberg,E. and Papaemmanuil,E.
  TITLE     Molecular and clinical presentation of UBA1-mutated myelodysplastic
            syndromes
  JOURNAL   Blood 144 (11), 1221-1229 (2024)
   PUBMED   38687605
  REMARK    GeneRIF: Molecular and clinical presentation of UBA1-mutated
            myelodysplastic syndromes.
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Chen,C., Li,Y., Chen,Z., Shi,P., Li,Y. and Qian,S.
  TITLE     A comprehensive prognostic and immune infiltration analysis of UBA1
            in pan-cancer: A computational analysis and in vitro experiments
  JOURNAL   J Cell Mol Med 28 (16), e70037 (2024)
   PUBMED   39183260
  REMARK    GeneRIF: A comprehensive prognostic and immune infiltration
            analysis of UBA1 in pan-cancer: A computational analysis and in
            vitro experiments.
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Corty,R.W., Brogan,J., Byram,K., Springer,J., Grayson,P.C. and
            Bick,A.G.
  TITLE     VEXAS-Defining UBA1 Somatic Variants in 245,368 Diverse Individuals
            in the NIH All Of Us Cohort
  JOURNAL   Arthritis Rheumatol 76 (6), 942-948 (2024)
   PUBMED   38225170
  REMARK    GeneRIF: VEXAS-Defining UBA1 Somatic Variants in 245,368 Diverse
            Individuals in the NIH All Of Us Cohort.
REFERENCE   4  (residues 1 to 1072)
  AUTHORS   Collins,J.C., Magaziner,S.J., English,M., Hassan,B., Chen,X.,
            Balanda,N., Anderson,M., Lam,A., Fernandez-Pol,S., Kwong,B.,
            Greenberg,P.L., Terrier,B., Likhite,M.E., Kosmider,O., Wang,Y.,
            Samara,N.L., Walters,K.J., Beck,D.B. and Werner,A.
  TITLE     Shared and distinct mechanisms of UBA1 inactivation across
            different diseases
  JOURNAL   EMBO J 43 (10), 1919-1946 (2024)
   PUBMED   38360993
  REMARK    GeneRIF: Shared and distinct mechanisms of UBA1 inactivation across
            different diseases.
REFERENCE   5  (residues 1 to 1072)
  AUTHORS   Hadjadj,J. and Beck,D.
  TITLE     VEXAS Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   40373178
REFERENCE   6  (residues 1 to 1072)
  AUTHORS   Baumbach-Reardon,L., Hunter,J.M., Ahearn,M.E. and Pfautsch,M.
  TITLE     Spinal Muscular Atrophy, X-Linked Infantile
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301739
REFERENCE   7  (residues 1 to 1072)
  AUTHORS   Schwartz,A.L., Trausch,J.S., Ciechanover,A., Slot,J.W. and Geuze,H.
  TITLE     Immunoelectron microscopic localization of the ubiquitin-activating
            enzyme E1 in HepG2 cells
  JOURNAL   Proc Natl Acad Sci U S A 89 (12), 5542-5546 (1992)
   PUBMED   1376922
REFERENCE   8  (residues 1 to 1072)
  AUTHORS   Ayusawa,D., Kaneda,S., Itoh,Y., Yasuda,H., Murakami,Y.,
            Sugasawa,K., Hanaoka,F. and Seno,T.
  TITLE     Complementation by a cloned human ubiquitin-activating enzyme E1 of
            the S-phase-arrested mouse FM3A cell mutant with thermolabile E1
  JOURNAL   Cell Struct Funct 17 (2), 113-122 (1992)
   PUBMED   1606621
REFERENCE   9  (residues 1 to 1072)
  AUTHORS   Takahashi,E., Ayusawa,D., Kaneda,S., Itoh,Y., Seno,T. and Hori,T.
  TITLE     The human ubiquitin-activating enzyme E1 gene (UBE1) mapped to band
            Xp11.3----p11.23 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 59 (4), 268-269 (1992)
   PUBMED   1544321
REFERENCE   10 (residues 1 to 1072)
  AUTHORS   Kudo,M., Sugasawa,K., Hori,T., Enomoto,T., Hanaoka,F. and Ui,M.
  TITLE     Human ubiquitin-activating enzyme (E1): compensation for
            heat-labile mouse E1 and its gene localization on the X chromosome
  JOURNAL   Exp Cell Res 192 (1), 110-117 (1991)
   PUBMED   1845793
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513366.11.
            
            On or before May 30, 2025 this sequence version replaced
            XP_011542256.1, XP_054183667.1.
            
            Summary: The protein encoded by this gene catalyzes the first step
            in ubiquitin conjugation to mark cellular proteins for degradation.
            This gene complements an X-linked mouse temperature-sensitive
            defect in DNA synthesis, and thus may function in DNA repair. It is
            part of a gene cluster on chromosome Xp11.23. Alternatively spliced
            transcript variants that encode the same protein have been
            described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853559.33720.1,
                                           SRR14038196.3490469.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.3"
     Protein         1..1072
                     /product="ubiquitin-like modifier-activating enzyme 1
                     isoform 3"
                     /EC_number="6.2.1.45"
                     /note="POC20 centriolar protein homolog; UBA1,
                     ubiquitin-activating enzyme E1 homolog A; A1S9T and BN75
                     temperature sensitivity complementing; testicular
                     secretory protein Li 63"
                     /calculated_mol_wt=119302
     Region          63..1069
                     /region_name="Ube1"
                     /note="ubiquitin-activating enzyme E1; TIGR01408"
                     /db_xref="CDD:273603"
     CDS             1..1072
                     /gene="UBA1"
                     /gene_synonym="A1S9; A1S9T; A1ST; AMCX1; CFAP124; GXP1;
                     POC20; SMAX2; UBA1A; UBE1; UBE1X; VEXAS"
                     /coded_by="NM_001440807.1:202..3420"
                     /note="isoform 3 is encoded by transcript variant 8"
                     /db_xref="GeneID:7317"
                     /db_xref="HGNC:HGNC:12469"
                     /db_xref="MIM:314370"
ORIGIN      
        1 mlcviyhldn pvgkmssspl skkrrvsgpd pkpgsncspa qsvlsevpsv ptngmakngs
       61 eadideglys rqlyvlghea mkrlqtssvl vsglrglgve iakniilggv kavtlhdqgt
      121 aqwadlssqf ylreedigkn raevsqprla elnsyvpvta ytgplvedfl sgfqvvvltn
      181 tpledqlrvg efchnrgikl vvadtrglfg qlfcdfgeem iltdsngeqp lsamvsmvtk
      241 dnpgvvtcld earhgfesgd fvsfsevqgm velngnqpme ikvlgpytfs icdtsnfsdy
      301 irggivsqvk vpkkisfksl vaslaepdfv vtdfakfsrp aqlhigfqal hqfcaqhgrp
      361 prprneedaa elvalaqavn aralpavqqn nldedlirkl ayvaagdlap inafigglaa
      421 qevmkacsgk fmpimqwlyf daleclpedk evltedkclq rqnrydgqva vfgsdlqekl
      481 gkqkyflvga gaigcellkn famiglgcge ggeiivtdmd tieksnlnrq flfrpwdvtk
      541 lksdtaaaav rqmnphirvt shqnrvgpdt eriydddffq nldgvanald nvdarmymdr
      601 rcvyyrkpll esgtlgtkgn vqvvipflte sysssqdppe ksipictlkn fpnaiehtlq
      661 wardefeglf kqpaenvnqy ltdpkfvert lrlagtqple vleavqrslv lqrpqtwadc
      721 vtwachhwht qysnnirqll hnfppdqlts sgapfwsgpk rcphpltfdv nnplhldyvm
      781 aaanlfaqty gltgsqdraa vatflqsvqv peftpksgvk ihvsdqelqs anasvddsrl
      841 eelkatlpsp dklpgfkmyp idfekdddsn fhmdfivaas nlraenydip sadrhkskli
      901 agkiipaiat ttaavvglvc lelykvvqgh rqldsykngf lnlalpffgf seplaaprhq
      961 yynqewtlwd rfevqglqpn geemtlkqfl dyfktehkle itmlsqgvsm lysffmpaak
     1021 lkerldqpmt eivsrvskrk lgrhvralvl elccndesge dvevpyvryt ir
//
LOCUS       NP_001389628            1277 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 11 [Homo sapiens].
ACCESSION   NP_001389628
VERSION     NP_001389628.1
DBSOURCE    REFSEQ: accession NM_001402699.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1277)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1277)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1277)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1277)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1277)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1277)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1277)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1277)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1277)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1277)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.222926.1,
                                           SRR14372079.3481554.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1277
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1277
                     /product="kinectin isoform 11"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=146845
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          316..>532
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          458..1217
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1277
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402699.1:303..4136"
                     /note="isoform 11 is encoded by transcript variant 22"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqlsitskvq
      841 elqnllkgke eqmntmkavl eekekdlant gkwlqdlqee neslkahvqe vaqhnlkeas
      901 sasqfeelei vlkekenelk rleamlkere sdlssktqll qdvqdenklf ksqieqlkqq
      961 nyqqassfpp heellkvise rekeisglwn eldslkdave hqrkknnerq qqveavelea
     1021 kevlkklfpk vsvpsnlsyg ewlhgfekka kecmagtsgs eevkvlehkl keademhtll
     1081 qlecekyksv laetegilqk lqrsveqeen kwkvkvdesh ktikqmqssf tsseqelerl
     1141 rsenkdienl rrerehleme lekaemerst yvtevrelka qlnetltklr teqnerqkva
     1201 gdlhkaqqsl eliqskivka agdttviens dvspetesse ketmsvslnq tvtqlqqllq
     1261 avnqqltkek ehyqvle
//
LOCUS       NP_001400247             291 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 2 [Homo sapiens].
ACCESSION   NP_001400247
VERSION     NP_001400247.1
DBSOURCE    REFSEQ: accession NM_001413318.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC103816.2, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.226247.1,
                                           SRR1803616.11943.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968832 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..291
                     /product="RNA-binding Raly-like protein isoform 2"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=32199
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          171..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     Region          199..>244
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     Region          249..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     CDS             1..291
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413318.1:400..1275"
                     /note="isoform 2 is encoded by transcript variant 44"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly rleskepfls
      121 vggyvfdydy yrddfynrlf dyhgrvpppp raviplkrpr vavtttrrgk gvfsmkggsr
      181 stasgstgsk lksdelqtik keltqiktki dsllgrleki ekqqkaeaea qkkqleeslv
      241 liqeecvsei adhsteepae ggpdadgeem tdgieedfde dgghelflqi k
//
LOCUS       NP_001393671             952 aa            linear   PRI 21-NOV-2025
DEFINITION  lysosomal alpha-glucosidase preproprotein [Homo sapiens].
ACCESSION   NP_001393671 XP_005257251
VERSION     NP_001393671.1
DBSOURCE    REFSEQ: accession NM_001406742.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 952)
  AUTHORS   Colella,P.
  TITLE     Advances in Pompe Disease Treatment: From Enzyme Replacement to
            Gene Therapy
  JOURNAL   Mol Diagn Ther 28 (6), 703-719 (2024)
   PUBMED   39134822
  REMARK    Review article
REFERENCE   2  (residues 1 to 952)
  AUTHORS   Ruiz-Saavedra,S., Salazar,N., Suarez,A., Diaz,Y., Gonzalez Del
            Rey,C., Gonzalez,S. and de Los Reyes-Gavilan,C.G.
  TITLE     Human fecal alpha-glucosidase activity and its relationship with
            gut microbiota profiles and early stages of intestinal mucosa
            damage
  JOURNAL   Anaerobe 87, 102853 (2024)
   PUBMED   38614290
  REMARK    GeneRIF: Human fecal alpha-glucosidase activity and its
            relationship with gut microbiota profiles and early stages of
            intestinal mucosa damage.
REFERENCE   3  (residues 1 to 952)
  AUTHORS   Schoser,B., Raben,N., Varfaj,F., Walzer,M. and Toscano,A.
  TITLE     Acid alpha-glucosidase (GAA) activity and glycogen content in
            muscle biopsy specimens of patients with Pompe disease: A
            systematic review
  JOURNAL   Mol Genet Metab Rep 39, 101085 (2024)
   PUBMED   38698877
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 952)
  AUTHORS   Lim,J.A., Li,L. and Raben,N.
  TITLE     Pompe disease: from pathophysiology to therapy and back again
  JOURNAL   Front Aging Neurosci 6, 177 (2014)
   PUBMED   25183957
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 952)
  AUTHORS   Moreland,R.J., Jin,X., Zhang,X.K., Decker,R.W., Albee,K.L.,
            Lee,K.L., Cauthron,R.D., Brewer,K., Edmunds,T. and Canfield,W.M.
  TITLE     Lysosomal acid alpha-glucosidase consists of four different
            peptides processed from a single chain precursor
  JOURNAL   J Biol Chem 280 (8), 6780-6791 (2005)
   PUBMED   15520017
  REMARK    GeneRIF: data show that the mature forms of GAA characterized by
            polypeptides of 76 or 70 kDa are in fact larger molecular mass
            multicomponent enzyme complexes; peptides released during
            proteolytic processing remained tightly associated with the major
            species
REFERENCE   6  (residues 1 to 952)
  AUTHORS   Sperry,E., Leslie,N., Berry,L. and Pena,L.
  TITLE     Pompe Disease
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301438
REFERENCE   7  (residues 1 to 952)
  AUTHORS   Martiniuk,F., Mehler,M., Bodkin,M., Tzall,S., Hirschhorn,K.,
            Zhong,N. and Hirschhorn,R.
  TITLE     Identification of a missense mutation in an adult-onset patient
            with glycogenosis type II expressing only one allele
  JOURNAL   DNA Cell Biol 10 (9), 681-687 (1991)
   PUBMED   1684505
REFERENCE   8  (residues 1 to 952)
  AUTHORS   Zhong,N., Martiniuk,F., Tzall,S. and Hirschhorn,R.
  TITLE     Identification of a missense mutation in one allele of a patient
            with Pompe disease, and use of endonuclease digestion of
            PCR-amplified RNA to demonstrate lack of mRNA expression from the
            second allele
  JOURNAL   Am J Hum Genet 49 (3), 635-645 (1991)
   PUBMED   1652892
REFERENCE   9  (residues 1 to 952)
  AUTHORS   Hoefsloot,L.H., Hoogeveen-Westerveld,M., Kroos,M.A., van
            Beeumen,J., Reuser,A.J. and Oostra,B.A.
  TITLE     Primary structure and processing of lysosomal alpha-glucosidase;
            homology with the intestinal sucrase-isomaltase complex
  JOURNAL   EMBO J 7 (6), 1697-1704 (1988)
   PUBMED   3049072
REFERENCE   10 (residues 1 to 952)
  AUTHORS   Murray,A.K., Brown,B.I. and Brown,D.H.
  TITLE     The molecular heterogeneity of purified human liver lysosomal
            alpha-glucosidase (acid alpha-glucosidase)
  JOURNAL   Arch Biochem Biophys 185 (2), 511-524 (1978)
   PUBMED   24417
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087741.18.
            
            On May 20, 2022 this sequence version replaced XP_005257251.1.
            
            Summary: This gene encodes lysosomal alpha-glucosidase, which is
            essential for the degradation of glycogen to glucose in lysosomes.
            The encoded preproprotein is proteolytically processed to generate
            multiple intermediate forms and the mature form of the enzyme.
            Defects in this gene are the cause of glycogen storage disease II,
            also known as Pompe's disease, which is an autosomal recessive
            disorder with a broad clinical spectrum. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jan
            2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853566.12521.1,
                                           SRR14038197.899956.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..952
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..952
                     /product="lysosomal alpha-glucosidase preproprotein"
                     /EC_number="3.2.1.20"
                     /note="lysosomal alpha-glucosidase; acid maltase;
                     aglucosidase alfa; glucosidase alpha, acid"
                     /calculated_mol_wt=102542
     sig_peptide     1..27
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10253.4)"
                     /calculated_mol_wt=2800
     Region          47..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10253.4)"
     mat_peptide     70..952
                     /product="Lysosomal alpha-glucosidase. /id=PRO_0000018566"
                     /note="propagated from UniProtKB/Swiss-Prot (P10253.4)"
                     /calculated_mol_wt=98009
     Region          81..132
                     /region_name="PD"
                     /note="P or trefoil or TFF domain; smart00018"
                     /db_xref="CDD:197472"
     Site            order(95,125..126)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:238059"
     Site            order(111,125)
                     /site_type="active"
                     /note="putative binding specificity loop [active]"
                     /db_xref="CDD:238059"
     mat_peptide     123..952
                     /product="76 kDa lysosomal alpha-glucosidase.
                     /id=PRO_0000018567"
                     /note="propagated from UniProtKB/Swiss-Prot (P10253.4)"
                     /calculated_mol_wt=92314
     Site            140
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:8435067,
                     ECO:0000269|Ref.19, ECO:0007744|PDB:5KZW,
                     ECO:0007744|PDB:5NN3; propagated from UniProtKB/Swiss-Prot
                     (P10253.4)"
     Region          159..254
                     /region_name="NtCtMGAM_N"
                     /note="N-terminal barrel of NtMGAM and CtMGAM,
                     maltase-glucoamylase; pfam16863"
                     /db_xref="CDD:465286"
     mat_peptide     204..952
                     /product="70 kDa lysosomal alpha-glucosidase.
                     /id=PRO_0000018568"
                     /note="propagated from UniProtKB/Swiss-Prot (P10253.4)"
                     /calculated_mol_wt=82826
     Site            233
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29061980,
                     ECO:0000269|PubMed:8435067, ECO:0000269|Ref.19,
                     ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5NN3; propagated
                     from UniProtKB/Swiss-Prot (P10253.4)"
     Region          246..359
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            282
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          340..824
                     /region_name="Glyco_hydro_31"
                     /note="Glycosyl hydrolases family 31; pfam01055"
                     /db_xref="CDD:460044"
     Site            390
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:8435067,
                     ECO:0000269|Ref.19, ECO:0007744|PDB:5KZW,
                     ECO:0007744|PDB:5NN3; propagated from UniProtKB/Swiss-Prot
                     (P10253.4)"
     Site            470
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:29061980,
                     ECO:0000269|PubMed:8435067, ECO:0000269|Ref.19,
                     ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5NN3; propagated
                     from UniProtKB/Swiss-Prot (P10253.4)"
     Site            652
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29061980,
                     ECO:0000269|PubMed:8435067, ECO:0000269|Ref.19,
                     ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5NN3; propagated
                     from UniProtKB/Swiss-Prot (P10253.4)"
     Site            882
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:8435067,
                     ECO:0000269|Ref.19, ECO:0007744|PDB:5KZW,
                     ECO:0007744|PDB:5NN3; propagated from UniProtKB/Swiss-Prot
                     (P10253.4)"
     Site            925
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:8435067; propagated from
                     UniProtKB/Swiss-Prot (P10253.4)"
     CDS             1..952
                     /gene="GAA"
                     /gene_synonym="IOPD; LOPD; LYAG"
                     /coded_by="NM_001406742.1:193..3051"
                     /db_xref="CCDS:CCDS32760.1"
                     /db_xref="GeneID:2548"
                     /db_xref="HGNC:HGNC:4065"
                     /db_xref="MIM:606800"
ORIGIN      
        1 mgvrhppcsh rllavcalvs lataallghi llhdfllvpr elsgsspvle ethpahqqga
       61 srpgprdaqa hpgrpravpt qcdvppnsrf dcapdkaitq eqceargccy ipakqglqga
      121 qmgqpwcffp psypsyklen lsssemgyta tltrttptff pkdiltlrld vmmetenrlh
      181 ftikdpanrr yevpletphv hsrapsplys vefseepfgv ivrrqldgrv llnttvaplf
      241 fadqflqlst slpsqyitgl aehlsplmls tswtritlwn rdlaptpgan lygshpfyla
      301 ledggsahgv fllnsnamdv vlqpspalsw rstggildvy iflgpepksv vqqyldvvgy
      361 pfmppywglg fhlcrwgyss taitrqvven mtrahfpldv qwndldymds rrdftfnkdg
      421 frdfpamvqe lhqggrrymm ivdpaisssg pagsyrpyde glrrgvfitn etgqpligkv
      481 wpgstafpdf tnptalawwe dmvaefhdqv pfdgmwidmn epsnfirgse dgcpnnelen
      541 ppyvpgvvgg tlqaaticas shqflsthyn lhnlygltea iashralvka rgtrpfvisr
      601 stfaghgrya ghwtgdvwss weqlassvpe ilqfnllgvp lvgadvcgfl gntseelcvr
      661 wtqlgafypf mrnhnsllsl pqepysfsep aqqamrkalt lryallphly tlfhqahvag
      721 etvarplfle fpkdsstwtv dhqllwgeal litpvlqagk aevtgyfplg twydlqtvpv
      781 ealgslpppp aaprepaihs egqwvtlpap ldtinvhlra gyiiplqgpg ltttesrqqp
      841 malavaltkg geargelfwd dgeslevler gaytqvifla rnntivnelv rvtsegaglq
      901 lqkvtvlgva tapqqvlsng vpvsnftysp dtkvldicvs llmgeqflvs wc
//
LOCUS       NP_001425382             539 aa            linear   PRI 21-NOV-2025
DEFINITION  F-box and leucine-rich repeat protein 13 isoform 5 [Homo sapiens].
ACCESSION   NP_001425382 XP_024302455 XP_054213566
VERSION     NP_001425382.1
DBSOURCE    REFSEQ: accession NM_001438453.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Walton,T., Gui,M., Velkova,S., Fassad,M.R., Hirst,R.A., Haarman,E.,
            O'Callaghan,C., Bottier,M., Burgoyne,T., Mitchison,H.M. and
            Brown,A.
  TITLE     Axonemal structures reveal mechanoregulatory and disease mechanisms
  JOURNAL   Nature 618 (7965), 625-633 (2023)
   PUBMED   37258679
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Fung,E., Richter,C., Yang,H.B., Schaffer,I., Fischer,R.,
            Kessler,B.M., Bassermann,F. and D'Angiolella,V.
  TITLE     FBXL13 directs the proteolysis of CEP192 to regulate centrosome
            homeostasis and cell migration
  JOURNAL   EMBO Rep 19 (3) (2018)
   PUBMED   29348145
REFERENCE   4  (residues 1 to 539)
  AUTHORS   He,J., Kelly,T.N., Zhao,Q., Li,H., Huang,J., Wang,L., Jaquish,C.E.,
            Sung,Y.J., Shimmin,L.C., Lu,F., Mu,J., Hu,D., Ji,X., Shen,C.,
            Guo,D., Ma,J., Wang,R., Shen,J., Li,S., Chen,J., Mei,H., Chen,C.S.,
            Chen,S., Chen,J., Li,J., Cao,J., Lu,X., Wu,X., Rice,T.K., Gu,C.C.,
            Schwander,K., Hamm,L.L., Liu,D., Rao,D.C., Hixson,J.E. and Gu,D.
  TITLE     Genome-wide association study identifies 8 novel loci associated
            with blood pressure responses to interventions in Han Chinese
  JOURNAL   Circ Cardiovasc Genet 6 (6), 598-607 (2013)
   PUBMED   24165912
REFERENCE   5  (residues 1 to 539)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   6  (residues 1 to 539)
  AUTHORS   Curtiss,N.P., Bonifas,J.M., Lauchle,J.O., Balkman,J.D., Kratz,C.P.,
            Emerling,B.M., Green,E.D., Le Beau,M.M. and Shannon,K.M.
  TITLE     Isolation and analysis of candidate myeloid tumor suppressor genes
            from a commonly deleted segment of 7q22
  JOURNAL   Genomics 85 (5), 600-607 (2005)
   PUBMED   15820312
REFERENCE   7  (residues 1 to 539)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073127.11, AC005250.1 and AC006477.4.
            
            On or before Apr 18, 2025 this sequence version replaced
            XP_024302455.1, XP_054213566.1.
            
            Summary: Members of the F-box protein family, such as FBXL13, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.879465.1,
                                           SRR5189661.68979.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..539
                     /product="F-box and leucine-rich repeat protein 13 isoform
                     5"
                     /note="F-box/LRR-repeat protein 13; dynein regulatory
                     complex subunit 6; cilia and flagella associated protein
                     169"
                     /calculated_mol_wt=60739
     Region          <15..45
                     /region_name="F-box_SF"
                     /note="F-box domain superfamily; cl45894"
                     /db_xref="CDD:459239"
     Region          44..71
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          71..256
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          72..95
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          96..121
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          122..142
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          147..174
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          175..200
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          201..226
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          224..451
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          251..276
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          277..301
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          302..329
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          330..355
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          356..380
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          381..404
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          405..437
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          438..463
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..539
                     /gene="FBXL13"
                     /gene_synonym="CFAP169; DRC6; Fbl13"
                     /coded_by="NM_001438453.1:131..1750"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:222235"
                     /db_xref="HGNC:HGNC:21658"
                     /db_xref="MIM:609080"
ORIGIN      
        1 mkgrlitiil lvtsiffyls lkdviicgqv nhawmlmtql nslwnaidfs svknvipdky
       61 ivstlqrwrl nvlrlnfrgc llrpktfrsv shcrnlqeln vsdcptftde smrhisegcp
      121 gvlclnlsnt titnrtmrll prhfhnlqnl slaycrrftd kglqylnlgn gchkliyldl
      181 sgctqisvqg fryiansctg imhltindmp tltdncvkal vekcsritsl vftgaphisd
      241 ctfralsack lrkirfegnk rvtdasfkfi dknypnlshi ymadckgitd sslrslsplk
      301 qltvlnlanc vrigdmglkq fldgpasmri relnlsncvr lsdasvmkls ercpnlnyls
      361 lrncehltaq gigyivnifs lvsidlsgtd isneglnvls rhkklkelsv secyritddg
      421 iqitdsamem lsakchylhi ldisgcvllt dqiledlqig ckqlrilkmq yctniskkaa
      481 qrmsskvqqq eyntndpprw fgydregnpv teldnitssk galeltvkks tyssedqaa
//
LOCUS       NP_001427739            1064 aa            linear   PRI 21-NOV-2025
DEFINITION  ubiquitin-like modifier-activating enzyme 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001427739 XP_047298379 XP_054183669
VERSION     NP_001427739.1
DBSOURCE    REFSEQ: accession NM_001440810.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Sirenko,M., Bernard,E., Creignou,M., Domenico,D., Farina,A., Arango
            Ossa,J.E., Kosmider,O., Hasserjian,R., Jadersten,M., Germing,U.,
            Sanz,G., van de Loosdrecht,A.A., Gurnari,C., Follo,M.Y., Thol,F.,
            Zamora,L., Pinheiro,R.F., Pellagatti,A., Elias,H.K., Haase,D.,
            Sander,B., Orna,E., Zoldan,K., Eder,L.N., Sperr,W.R.,
            Thalhammer,R., Ganster,C., Ades,L., Tobiasson,M., Palomo,L., Della
            Porta,M.G., Huberman,K., Fenaux,P., Belickova,M., Savona,M.R.,
            Klimek,V.M., Santos,F.P.S., Boultwood,J., Kotsianidis,I.,
            Santini,V., Sole,F., Platzbecker,U., Heuser,M., Valent,P.,
            Finelli,C., Voso,M.T., Shih,L.Y., Ogawa,S., Fontenay,M.,
            Jansen,J.H., Cervera,J., Ebert,B.L., Bejar,R., Greenberg,P.L.,
            Gattermann,N., Malcovati,L., Cazzola,M., Beck,D.B.,
            Hellstrom-Lindberg,E. and Papaemmanuil,E.
  TITLE     Molecular and clinical presentation of UBA1-mutated myelodysplastic
            syndromes
  JOURNAL   Blood 144 (11), 1221-1229 (2024)
   PUBMED   38687605
  REMARK    GeneRIF: Molecular and clinical presentation of UBA1-mutated
            myelodysplastic syndromes.
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Chen,C., Li,Y., Chen,Z., Shi,P., Li,Y. and Qian,S.
  TITLE     A comprehensive prognostic and immune infiltration analysis of UBA1
            in pan-cancer: A computational analysis and in vitro experiments
  JOURNAL   J Cell Mol Med 28 (16), e70037 (2024)
   PUBMED   39183260
  REMARK    GeneRIF: A comprehensive prognostic and immune infiltration
            analysis of UBA1 in pan-cancer: A computational analysis and in
            vitro experiments.
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Corty,R.W., Brogan,J., Byram,K., Springer,J., Grayson,P.C. and
            Bick,A.G.
  TITLE     VEXAS-Defining UBA1 Somatic Variants in 245,368 Diverse Individuals
            in the NIH All Of Us Cohort
  JOURNAL   Arthritis Rheumatol 76 (6), 942-948 (2024)
   PUBMED   38225170
  REMARK    GeneRIF: VEXAS-Defining UBA1 Somatic Variants in 245,368 Diverse
            Individuals in the NIH All Of Us Cohort.
REFERENCE   4  (residues 1 to 1064)
  AUTHORS   Collins,J.C., Magaziner,S.J., English,M., Hassan,B., Chen,X.,
            Balanda,N., Anderson,M., Lam,A., Fernandez-Pol,S., Kwong,B.,
            Greenberg,P.L., Terrier,B., Likhite,M.E., Kosmider,O., Wang,Y.,
            Samara,N.L., Walters,K.J., Beck,D.B. and Werner,A.
  TITLE     Shared and distinct mechanisms of UBA1 inactivation across
            different diseases
  JOURNAL   EMBO J 43 (10), 1919-1946 (2024)
   PUBMED   38360993
  REMARK    GeneRIF: Shared and distinct mechanisms of UBA1 inactivation across
            different diseases.
REFERENCE   5  (residues 1 to 1064)
  AUTHORS   Hadjadj,J. and Beck,D.
  TITLE     VEXAS Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   40373178
REFERENCE   6  (residues 1 to 1064)
  AUTHORS   Baumbach-Reardon,L., Hunter,J.M., Ahearn,M.E. and Pfautsch,M.
  TITLE     Spinal Muscular Atrophy, X-Linked Infantile
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301739
REFERENCE   7  (residues 1 to 1064)
  AUTHORS   Schwartz,A.L., Trausch,J.S., Ciechanover,A., Slot,J.W. and Geuze,H.
  TITLE     Immunoelectron microscopic localization of the ubiquitin-activating
            enzyme E1 in HepG2 cells
  JOURNAL   Proc Natl Acad Sci U S A 89 (12), 5542-5546 (1992)
   PUBMED   1376922
REFERENCE   8  (residues 1 to 1064)
  AUTHORS   Ayusawa,D., Kaneda,S., Itoh,Y., Yasuda,H., Murakami,Y.,
            Sugasawa,K., Hanaoka,F. and Seno,T.
  TITLE     Complementation by a cloned human ubiquitin-activating enzyme E1 of
            the S-phase-arrested mouse FM3A cell mutant with thermolabile E1
  JOURNAL   Cell Struct Funct 17 (2), 113-122 (1992)
   PUBMED   1606621
REFERENCE   9  (residues 1 to 1064)
  AUTHORS   Takahashi,E., Ayusawa,D., Kaneda,S., Itoh,Y., Seno,T. and Hori,T.
  TITLE     The human ubiquitin-activating enzyme E1 gene (UBE1) mapped to band
            Xp11.3----p11.23 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 59 (4), 268-269 (1992)
   PUBMED   1544321
REFERENCE   10 (residues 1 to 1064)
  AUTHORS   Kudo,M., Sugasawa,K., Hori,T., Enomoto,T., Hanaoka,F. and Ui,M.
  TITLE     Human ubiquitin-activating enzyme (E1): compensation for
            heat-labile mouse E1 and its gene localization on the X chromosome
  JOURNAL   Exp Cell Res 192 (1), 110-117 (1991)
   PUBMED   1845793
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513366.11.
            
            On or before May 30, 2025 this sequence version replaced
            XP_047298379.1, XP_054183669.1.
            
            Summary: The protein encoded by this gene catalyzes the first step
            in ubiquitin conjugation to mark cellular proteins for degradation.
            This gene complements an X-linked mouse temperature-sensitive
            defect in DNA synthesis, and thus may function in DNA repair. It is
            part of a gene cluster on chromosome Xp11.23. Alternatively spliced
            transcript variants that encode the same protein have been
            described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2814828.1,
                                           SRR14038195.1813846.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.3"
     Protein         1..1064
                     /product="ubiquitin-like modifier-activating enzyme 1
                     isoform 2"
                     /EC_number="6.2.1.45"
                     /note="POC20 centriolar protein homolog; UBA1,
                     ubiquitin-activating enzyme E1 homolog A; A1S9T and BN75
                     temperature sensitivity complementing; testicular
                     secretory protein Li 63"
                     /calculated_mol_wt=118431
     Region          55..1061
                     /region_name="Ube1"
                     /note="ubiquitin-activating enzyme E1; TIGR01408"
                     /db_xref="CDD:273603"
     CDS             1..1064
                     /gene="UBA1"
                     /gene_synonym="A1S9; A1S9T; A1ST; AMCX1; CFAP124; GXP1;
                     POC20; SMAX2; UBA1A; UBE1; UBE1X; VEXAS"
                     /coded_by="NM_001440810.1:254..3448"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:7317"
                     /db_xref="HGNC:HGNC:12469"
                     /db_xref="MIM:314370"
ORIGIN      
        1 mrslpqmsss plskkrrvsg pdpkpgsncs paqsvlsevp svptngmakn gseadidegl
       61 ysrqlyvlgh eamkrlqtss vlvsglrglg veiakniilg gvkavtlhdq gtaqwadlss
      121 qfylreedig knraevsqpr laelnsyvpv taytgplved flsgfqvvvl tntpledqlr
      181 vgefchnrgi klvvadtrgl fgqlfcdfge emiltdsnge qplsamvsmv tkdnpgvvtc
      241 ldearhgfes gdfvsfsevq gmvelngnqp meikvlgpyt fsicdtsnfs dyirggivsq
      301 vkvpkkisfk slvaslaepd fvvtdfakfs rpaqlhigfq alhqfcaqhg rpprprneed
      361 aaelvalaqa vnaralpavq qnnldedlir klayvaagdl apinafiggl aaqevmkacs
      421 gkfmpimqwl yfdaleclpe dkevltedkc lqrqnrydgq vavfgsdlqe klgkqkyflv
      481 gagaigcell knfamiglgc geggeiivtd mdtieksnln rqflfrpwdv tklksdtaaa
      541 avrqmnphir vtshqnrvgp dteriydddf fqnldgvana ldnvdarmym drrcvyyrkp
      601 llesgtlgtk gnvqvvipfl tesysssqdp peksipictl knfpnaieht lqwardefeg
      661 lfkqpaenvn qyltdpkfve rtlrlagtqp levleavqrs lvlqrpqtwa dcvtwachhw
      721 htqysnnirq llhnfppdql tssgapfwsg pkrcphpltf dvnnplhldy vmaaanlfaq
      781 tygltgsqdr aavatflqsv qvpeftpksg vkihvsdqel qsanasvdds rleelkatlp
      841 spdklpgfkm ypidfekddd snfhmdfiva asnlraenyd ipsadrhksk liagkiipai
      901 atttaavvgl vclelykvvq ghrqldsykn gflnlalpff gfseplaapr hqyynqewtl
      961 wdrfevqglq pngeemtlkq fldyfktehk leitmlsqgv smlysffmpa aklkerldqp
     1021 mteivsrvsk rklgrhvral vlelccndes gedvevpyvr ytir
//
LOCUS       NP_001425384             542 aa            linear   PRI 21-NOV-2025
DEFINITION  excitatory amino acid transporter 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001425384
VERSION     NP_001425384.1
DBSOURCE    REFSEQ: accession NM_001438455.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Albury,C.L., Sutherland,H.G., Lam,A.W.Y., Tran,N.K., Lea,R.A.,
            Haupt,L.M. and Griffiths,L.R.
  TITLE     Identification of Polymorphisms in EAAT1 Glutamate Transporter Gene
            SLC1A3 Associated with Reduced Migraine Risk
  JOURNAL   Genes (Basel) 15 (6), 797 (2024)
   PUBMED   38927733
  REMARK    GeneRIF: Identification of Polymorphisms in EAAT1 Glutamate
            Transporter Gene SLC1A3 Associated with Reduced Migraine Risk.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Welby,E. and Ebert,A.D.
  TITLE     Diminished motor neuron activity driven by abnormal astrocytic
            EAAT1 glutamate transporter activity in spinal muscular atrophy is
            not fully restored after lentiviral SMN delivery
  JOURNAL   Glia 71 (5), 1311-1332 (2023)
   PUBMED   36655314
  REMARK    GeneRIF: Diminished motor neuron activity driven by abnormal
            astrocytic EAAT1 glutamate transporter activity in spinal muscular
            atrophy is not fully restored after lentiviral SMN delivery.
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Pant,S., Wu,Q., Ryan,R. and Tajkhorshid,E.
  TITLE     Microscopic Characterization of the Chloride Permeation Pathway in
            the Human Excitatory Amino Acid Transporter 1 (EAAT1)
  JOURNAL   ACS Chem Neurosci 13 (6), 776-785 (2022)
   PUBMED   35192345
  REMARK    GeneRIF: Microscopic Characterization of the Chloride Permeation
            Pathway in the Human Excitatory Amino Acid Transporter 1 (EAAT1).
REFERENCE   5  (residues 1 to 542)
  AUTHORS   Lee,A., Anderson,A.R., Beasley,S.J., Barnett,N.L., Poronnik,P. and
            Pow,D.V.
  TITLE     A new splice variant of the glutamate-aspartate transporter:
            cloning and immunolocalization of GLAST1c in rat, pig and human
            brains
  JOURNAL   J Chem Neuroanat 43 (1), 52-63 (2012)
   PUBMED   22026960
REFERENCE   6  (residues 1 to 542)
  AUTHORS   Vallejo-Illarramendi,A., Domercq,M. and Matute,C.
  TITLE     A novel alternative splicing form of excitatory amino acid
            transporter 1 is a negative regulator of glutamate uptake
  JOURNAL   J Neurochem 95 (2), 341-348 (2005)
   PUBMED   16042756
  REMARK    GeneRIF: EAAT1ex9skip splice variant is a negative regulator of
            full-length EAAT1 function in the human brain
REFERENCE   7  (residues 1 to 542)
  AUTHORS   Takai,S., Yamada,K., Kawakami,H., Tanaka,K. and Nakamura,S.
  TITLE     Localization of the gene (SLC1A3) encoding human glutamate
            transporter (GluT-1) to 5p13 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 209-210 (1995)
   PUBMED   7698014
REFERENCE   8  (residues 1 to 542)
  AUTHORS   Shashidharan,P., Huntley,G.W., Meyer,T., Morrison,J.H. and
            Plaitakis,A.
  TITLE     Neuron-specific human glutamate transporter: molecular cloning,
            characterization and expression in human brain
  JOURNAL   Brain Res 662 (1-2), 245-250 (1994)
   PUBMED   7859077
REFERENCE   9  (residues 1 to 542)
  AUTHORS   Arriza,J.L., Fairman,W.A., Wadiche,J.I., Murdoch,G.H.,
            Kavanaugh,M.P. and Amara,S.G.
  TITLE     Functional comparisons of three glutamate transporter subtypes
            cloned from human motor cortex
  JOURNAL   J Neurosci 14 (9), 5559-5569 (1994)
   PUBMED   7521911
REFERENCE   10 (residues 1 to 542)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010631.6 and AC008957.7.
            
            Summary: This gene encodes a member of a member of a high affinity
            glutamate transporter family. This gene functions in the
            termination of excitatory neurotransmission in central nervous
            system. Mutations are associated with episodic ataxia, Type 6.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.747157.1,
                                           SRR1803611.70360.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..542
                     /product="excitatory amino acid transporter 1 isoform 1"
                     /note="excitatory amino acid transporter 1; GLAST-1;
                     sodium-dependent glutamate/aspartate transporter 1; solute
                     carrier family 1 (glial high affinity glutamate
                     transporter), member 3"
                     /calculated_mol_wt=59441
     Region          46..496
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            87..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            123..145
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            237..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            270..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            319..340
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            386..412
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            473..494
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P43003.1)"
     CDS             1..542
                     /gene="SLC1A3"
                     /gene_synonym="EA6; EAAT1; GLAST; GLAST1"
                     /coded_by="NM_001438455.1:187..1815"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="GeneID:6507"
                     /db_xref="HGNC:HGNC:10941"
                     /db_xref="MIM:600111"
ORIGIN      
        1 mtksngeepk mggrmerfqq gvrkrtllak kkvqnitked vksylfrnaf vlltvtaviv
       61 gtilgftlrp yrmsyrevky fsfpgellmr mlqmlvlpli isslvtgmaa ldskasgkmg
      121 mravvyymtt tiiavvigii iviiihpgkg tkenmhregk ivrvtaadaf ldlirnmfpp
      181 nlveacfkqf ktnyekrsfk vpiqanetlv gavinnvsea metltritee lvpvpgsvng
      241 vnalglvvfs mcfgfvignm keqgqalref fdslneaimr lvavimwyap vgilfliagk
      301 ivemedmgvi ggqlamytvt vivgllihav ivlpllyflv trknpwvfig gllqalital
      361 gtssssatlp itfkcleenn gvdkrvtrfv lpvgatinmd gtalyealaa ifiaqvnnfe
      421 lnfgqiitis itataasiga agipqaglvt mvivltsvgl ptdditliia vdwfldrlrt
      481 ttnvlgdslg agivehlsrh elknrdvemg nsvieenemk kpyqliaqdn etekpidset
      541 km
//
LOCUS       NP_001427585             756 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 3 isoform 5 [Homo sapiens].
ACCESSION   NP_001427585 XP_047294826 XP_054177064 XP_054185666 XP_054186161
            XP_054186459 XP_054186710 XP_054186940 XP_054187223 XP_054187496
            XP_054189537 XP_054189638
VERSION     NP_001427585.1
DBSOURCE    REFSEQ: accession NM_001440656.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Ghashghaei,M., Liu,Y., Ettles,J., Bombaci,G., Ramkumar,N., Liu,Z.,
            Escano,L., Miko,S.S., Kim,Y., Waldron,J.A., Do,K., MacPherson,K.,
            Yuen,K.A., Taibi,T., Yue,M., Arsalan,A., Jin,Z., Edin,G.,
            Karsan,A., Morin,G.B., Kuchenbauer,F., Perna,F., Bushell,M. and
            Vu,L.P.
  TITLE     Translation efficiency driven by CNOT3 subunit of the CCR4-NOT
            complex promotes leukemogenesis
  JOURNAL   Nat Commun 15 (1), 2340 (2024)
   PUBMED   38491013
  REMARK    GeneRIF: Translation efficiency driven by CNOT3 subunit of the
            CCR4-NOT complex promotes leukemogenesis.
            Erratum:[Nat Commun. 2024 Oct 7;15(1):8674. doi:
            10.1038/s41467-024-53071-1. PMID: 39375334]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 756)
  AUTHORS   Burgess,H.M., Grande,R., Riccio,S., Dinesh,I., Winkler,G.S.,
            Depledge,D.P. and Mohr,I.
  TITLE     CCR4-NOT differentially controls host versus virus poly(a)-tail
            length and regulates HCMV infection
  JOURNAL   EMBO Rep 24 (12), e56327 (2023)
   PUBMED   37846490
  REMARK    GeneRIF: CCR4-NOT differentially controls host versus virus
            poly(a)-tail length and regulates HCMV infection.
REFERENCE   4  (residues 1 to 756)
  AUTHORS   Zhao,P., Meng,Q., Wan,C., Lei,T., Zhang,L., Zhang,X., Tan,L.,
            Zhu,H. and He,X.
  TITLE     Clinical features of CNOT3-associated neurodevelopmental disorder
            in three Chinese patients
  JOURNAL   Neurogenetics 24 (2), 129-136 (2023)
   PUBMED   36802310
  REMARK    GeneRIF: Clinical features of CNOT3-associated neurodevelopmental
            disorder in three Chinese patients.
REFERENCE   5  (residues 1 to 756)
  AUTHORS   McLenachan,S., Zhang,D., Grainok,J., Zhang,X., Huang,Z., Chen,S.C.,
            Zaw,K., Lima,A., Jennings,L., Roshandel,D., Moon,S.Y., Heath
            Jeffery,R.C., Attia,M.S., Thompson,J.A., Lamey,T.M., McLaren,T.L.,
            De Roach,J., Fletcher,S. and Chen,F.K.
  TITLE     Determinants of Disease Penetrance in PRPF31-Associated Retinopathy
  JOURNAL   Genes (Basel) 12 (10), 1542 (2021)
   PUBMED   34680937
  REMARK    GeneRIF: Determinants of Disease Penetrance in PRPF31-Associated
            Retinopathy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 756)
  AUTHORS   Yin,X., Warner,D.R., Roberts,E.A., Pisano,M.M. and Greene,R.M.
  TITLE     Identification of novel CBP interacting proteins in embryonic
            orofacial tissue
  JOURNAL   Biochem Biophys Res Commun 329 (3), 1010-1017 (2005)
   PUBMED   15752756
REFERENCE   7  (residues 1 to 756)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 756)
  AUTHORS   Aoki,T., Okada,N., Wakamatsu,T. and Tamura,T.A.
  TITLE     TBP-interacting protein 120B, which is induced in relation to
            myogenesis, binds to NOT3
  JOURNAL   Biochem Biophys Res Commun 296 (5), 1097-1103 (2002)
   PUBMED   12207886
  REMARK    GeneRIF: TBP-interacting protein 120B binds to NOT3
REFERENCE   9  (residues 1 to 756)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
REFERENCE   10 (residues 1 to 756)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC245052.3.
            
            On or before May 23, 2025 this sequence version replaced
            XP_054186161.1, XP_054189638.1, XP_054189537.1, XP_054187223.1,
            XP_054186459.1, XP_054187496.1, XP_047294826.1, XP_054185666.1,
            XP_054186710.1, XP_054186940.1, XP_054177064.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853559.17667.1,
                                           SRR14038197.1501222.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..756
                     /product="CCR4-NOT transcription complex subunit 3 isoform
                     5"
                     /note="NOT3 (negative regulator of transcription 3, yeast)
                     homolog; CCR4-associated factor 3; leukocyte receptor
                     cluster member 2"
                     /calculated_mol_wt=81268
     Region          3..229
                     /region_name="Not3"
                     /note="Not1 N-terminal domain, CCR4-Not complex component;
                     pfam04065"
                     /db_xref="CDD:461155"
     Region          240..534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75175.1)"
     Region          <288..659
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Region          620..721
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..756
                     /gene="CNOT3"
                     /gene_synonym="IDDSADF; LENG2; NOT3; NOT3H"
                     /coded_by="NM_001440656.1:283..2553"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:4849"
                     /db_xref="HGNC:HGNC:7879"
                     /db_xref="MIM:604910"
ORIGIN      
        1 madkrklqge idrclkkvse gveqfediwq klhnaananq kekyeadlkk eikklqrlrd
       61 qiktwvasne ikdkrqlidn rklietqmer fkvveretkt kayskeglgl aqkvdpaqke
      121 keevgqwltn tidtlnmqvd qfesevesls vqtrkkkgdk dkqdrieglk rhiekhryhv
      181 rmletilrml dndsilvdai rkikddveyy vdssqdpdfe eneflyddld ledipqalva
      241 tsppshshme deifnqssst ptsttssspi ppspanctte nseddkkrgr stdsevsqsp
      301 akngskpvhs nqhpqspavp ptypsgpppa asalsttpgn ngvpapaapp salgpkaspa
      361 pshnsgtpap yaqavappap sgpsttqprp psvqpsgggg ggsggggsss ssnssaggga
      421 gkqngatsys svvadspaev alsssggnna ssqalgppsg phnpppstsk epsaaaptga
      481 ggvapgsgnn sggpsllvpl pvnppssptp sfsdakaaga llngppqfst apeikapepl
      541 sslksmaera aissgiedpv ptlhlterdi ilsstsappa saqpplqlse vniplslgvc
      601 plgpvpltke qlyqqameea awhhmphpsd serirqylpr npcptppyhh qmppphsdtv
      661 efyqrlstet lffifyyleg tkaqylaaka lkkqswrfht kymmwfqrhe epktitdefe
      721 qlaqslsltk ysslwlsaqp gtppshpplg qllgll
//
LOCUS       NP_001426134             212 aa            linear   PRI 21-NOV-2025
DEFINITION  programmed cell death protein 10 [Homo sapiens].
ACCESSION   NP_001426134 XP_006713548 XP_054201072
VERSION     NP_001426134.1
DBSOURCE    REFSEQ: accession NM_001439205.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Li,Y., Liu,Y., Liu,K., Tao,T., Yang,L., Liu,R., Zhou,H., Liang,D.,
            Zhang,Y., Huang,D. and Sun,Y.
  TITLE     Study on the role of CCM3 gene and lead exposure induced
            neurotoxicity through neurovascular units
  JOURNAL   Ecotoxicol Environ Saf 277, 116269 (2024)
   PUBMED   38657460
  REMARK    GeneRIF: Study on the role of CCM3 gene and lead exposure induced
            neurotoxicity through neurovascular units.
REFERENCE   3  (residues 1 to 212)
  AUTHORS   da Fontoura Galvao,G., da Silva,E.V., Trefilio,L.M.,
            Alves-Leon,S.V., Fontes-Dantas,F.L. and de Souza,J.M.
  TITLE     Comprehensive CCM3 Mutational Analysis in Two Patients with
            Syndromic Cerebral Cavernous Malformation
  JOURNAL   Transl Stroke Res 15 (2), 411-421 (2024)
   PUBMED   36723700
  REMARK    GeneRIF: Comprehensive CCM3 Mutational Analysis in Two Patients
            with Syndromic Cerebral Cavernous Malformation.
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Tang,L., Zhou,M., Xu,Y., Peng,B., Gao,Y. and Mo,Y.
  TITLE     Knockdown of CCM3 promotes angiogenesis through activation and
            nuclear translocation of YAP/TAZ
  JOURNAL   Biochem Biophys Res Commun 701, 149525 (2024)
   PUBMED   38320423
  REMARK    GeneRIF: Knockdown of CCM3 promotes angiogenesis through activation
            and nuclear translocation of YAP/TAZ.
REFERENCE   5  (residues 1 to 212)
  AUTHORS   Ni,W.J. and Leng,X.M.
  TITLE     Programmed cell death 10 can be used as a potential biomarker for
            ankylosing spondylitis diagnosis and treatment
  JOURNAL   Spinal Cord 62 (3), 99-103 (2024)
   PUBMED   38158408
  REMARK    GeneRIF: Programmed cell death 10 can be used as a potential
            biomarker for ankylosing spondylitis diagnosis and treatment.
REFERENCE   6  (residues 1 to 212)
  AUTHORS   Guclu,B., Ozturk,A.K., Pricola,K.L., Bilguvar,K., Shin,D.,
            O'Roak,B.J. and Gunel,M.
  TITLE     Mutations in apoptosis-related gene, PDCD10, cause cerebral
            cavernous malformation 3
  JOURNAL   Neurosurgery 57 (5), 1008-1013 (2005)
   PUBMED   16284570
  REMARK    GeneRIF: Mutations in apoptosis-related gene, PDCD10, cause
            cerebral cavernous malformation 3.
REFERENCE   7  (residues 1 to 212)
  AUTHORS   Guclu,B., Ozturk,A.K., Pricola,K.L., Seker,A., Ozek,M. and Gunel,M.
  TITLE     Cerebral venous malformations have distinct genetic origin from
            cerebral cavernous malformations
  JOURNAL   Stroke 36 (11), 2479-2480 (2005)
   PUBMED   16239636
  REMARK    GeneRIF: KRIT1, Malcavernin, and PDCD10 are differentially
            expressed in cerebral venous malformations and cerebral cavernous
            malformations
REFERENCE   8  (residues 1 to 212)
  AUTHORS   Bergametti,F., Denier,C., Labauge,P., Arnoult,M., Boetto,S.,
            Clanet,M., Coubes,P., Echenne,B., Ibrahim,R., Irthum,B.,
            Jacquet,G., Lonjon,M., Moreau,J.J., Neau,J.P., Parker,F.,
            Tremoulet,M. and Tournier-Lasserve,E.
  CONSRTM   Societe Francaise de Neurochirurgie
  TITLE     Mutations within the programmed cell death 10 gene cause cerebral
            cavernous malformations
  JOURNAL   Am J Hum Genet 76 (1), 42-51 (2005)
   PUBMED   15543491
  REMARK    GeneRIF: We report herein the identification of PDCD10 (programmed
            cell death 10) as the CCM3 gene.
REFERENCE   9  (residues 1 to 212)
  AUTHORS   Craig,H.D., Gunel,M., Cepeda,O., Johnson,E.W., Ptacek,L.,
            Steinberg,G.K., Ogilvy,C.S., Berg,M.J., Crawford,S.C., Scott,R.M.,
            Steichen-Gersdorf,E., Sabroe,R., Kennedy,C.T., Mettler,G.,
            Beis,M.J., Fryer,A., Awad,I.A. and Lifton,R.P.
  TITLE     Multilocus linkage identifies two new loci for a mendelian form of
            stroke, cerebral cavernous malformation, at 7p15-13 and 3q25.2-27
  JOURNAL   Hum Mol Genet 7 (12), 1851-1858 (1998)
   PUBMED   9811928
REFERENCE   10 (residues 1 to 212)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079822.13.
            
            On or before Apr 28, 2025 this sequence version replaced
            XP_006713548.1, XP_054201072.1.
            
            Summary: This gene encodes an evolutionarily conserved protein
            associated with cell apoptosis. The protein interacts with the
            serine/threonine protein kinase MST4 to modulate the extracellular
            signal-regulated kinase (ERK) pathway. It also interacts with and
            is phosphoryated by serine/threonine kinase 25, and is thought to
            function in a signaling pathway essential for vascular developent.
            Mutations in this gene are one cause of cerebral cavernous
            malformations, which are vascular malformations that cause seizures
            and cerebral hemorrhages. Multiple alternatively spliced variants,
            encoding the same protein, have been identified. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1068381.1,
                                           SRR14038196.2863809.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.1"
     Protein         1..212
                     /product="programmed cell death protein 10"
                     /note="apoptosis-related protein 15; TF-1 cell
                     apoptosis-related protein 15; cerebral cavernous
                     malformations 3 protein"
                     /calculated_mol_wt=24571
     Region          14..161
                     /region_name="DUF1241"
                     /note="Protein of unknown function (DUF1241); pfam06840"
                     /db_xref="CDD:462018"
     Site            179
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BUL8.1)"
     CDS             1..212
                     /gene="PDCD10"
                     /gene_synonym="CCM3; TFAR15"
                     /coded_by="NM_001439205.1:219..857"
                     /db_xref="GeneID:11235"
                     /db_xref="HGNC:HGNC:8761"
                     /db_xref="MIM:609118"
ORIGIN      
        1 mrmtmeemkn eaettsmvsm plyavmypvf nelervnlsa aqtlraafik aekenpgltq
       61 diimkilekk svevnftesl lrmaaddvee ymierpepef qdlnekaral kqilskipde
      121 indrvrflqt ikdiasaike lldtvnnvfk kyqyqnrral ehqkkefvky sksfsdtlkt
      181 yfkdgkainv fvsanrlihq tnlilqtfkt va
//
LOCUS       NP_001393536            1150 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 7 [Homo sapiens].
ACCESSION   NP_001393536 XP_047279791
VERSION     NP_001393536.1
DBSOURCE    REFSEQ: accession NM_001406607.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1150)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1150)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1150)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1150)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1150)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1150)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1150)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1150)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1150)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1150)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            On May 20, 2022 this sequence version replaced XP_047279791.1.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1857177.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1150
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1150
                     /product="hamartin isoform 7"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=128069
     Region          7..719
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          403..787
                     /region_name="Mediates interaction with WDR45B.
                     /evidence=ECO:0000269|PubMed:28561066"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Region          439..571
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <705..>942
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          992..1071
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1086
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1117..1150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1150
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406607.1:214..3666"
                     /note="isoform 7 is encoded by transcript variant 21"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt aggkgtplgt patspppapl chsddyvhis lpqatvtppr
      421 keermdsarp clhrqhhlln drgseeppgs kgsvtlsdlp gflgdlasee dsiekdkeea
      481 aisrelseit taeaepvvpr ggfdspfyrd slpgsqrkth saasssqgas vnpeplhssl
      541 dklgpdtpkq aftpidlpcg sadespagdr ecqtsletsi ftpspckipp ptrvgfgsgq
      601 pppydhlfev alpktahhfv irkteellkk akgnteedgv pstspmevld rliqqgadah
      661 skelnklplp sksvdwthfg gsppsdeirt lrdqllllhn qllyerfkrq qhalrnrrll
      721 rkvikaaale ehnaamkdql klqekdiqmw kvslqkeqar ynqlqeqrdt mvtklhsqir
      781 qlqhdreefy nqsqelqtkl edcrnmiael rielkkannk lsnsesvqqq meflnrqllv
      841 lgevnelyle qlqnkhsdtt kevemmkaay rkeleknrsh vlqqtqrldt sqkrileles
      901 hlakkdhlll eqkkyledvk lqargqlqaa esryeaqkri tqvfeleild lygrlekdgl
      961 lkkleeekae aaeaaeerld ccndgcsdsm vghneeasgh ngetktprps sargssgsrg
     1021 gggsssssse lstpekpphq ragpfssrwe ttmgeasasi pttvgslpss ksflgmkare
     1081 lfrnksesqc dedgmtssls eslktelgkd lgveakipln ldgphpsppt pdsvgqlhim
     1141 dynethhehs
//
LOCUS       NP_001393915             583 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform G [Homo sapiens].
ACCESSION   NP_001393915
VERSION     NP_001393915.1
DBSOURCE    REFSEQ: accession NM_001406986.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 583)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 583)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 583)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 583)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 583)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 583)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 583)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 583)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3299978.1,
                                           SRR14038192.3832016.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146982, SAMEA2159931
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..583
                     /product="lamin isoform G"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=64636
     Region          48..305
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          353..460
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     CDS             1..583
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406986.1:632..2383"
                     /note="isoform G is encoded by transcript variant 13"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 mqpllclgnl edarertgtl laqhpawgrt rakpgsplnt kkegdliaaq arlkdleall
       61 nskeaalsta lsekrtlege lhdlrgqvak leaalgeakk qlqdemlrrv daenrlqtmk
      121 eeldfqkniy seelretkrr hetrlveidn gkqrefesrl adalqelraq hedqveqykk
      181 elektysakl dnarqsaern snlvgaahee lqqsririds lsaqlsqlqk qlaakeaklr
      241 dledslarer dtsrrllaek eremaemrar mqqqldeyqe lldiklaldm eihayrklle
      301 geeerlrlsp sptsqrsrgr asshssqtqg ggsvtkkrkl estesrssfs qhartsgrva
      361 veevdeegkf vrlrnksned qsmgnwqikr qngddpllty rfppkftlka gqvvtiwaag
      421 agathspptd lvwkaqntwg cgnslrtali nstgeevamr klvrsvtvve ddededgddl
      481 lhhhhgshcs ssgdpaeynl rsrtvlcgtc gqpadkasas gsgaqvggpi ssgssassvt
      541 vtrsyrsvgg sgggsfgdnl vtrsyllgns sprtqspqnc sim
//
LOCUS       NP_001394762            1122 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 18 [Homo
            sapiens].
ACCESSION   NP_001394762
VERSION     NP_001394762.1
DBSOURCE    REFSEQ: accession NM_001407833.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1122)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1122)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1122)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1122)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1122)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1122)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1122)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1122)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1122)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1122)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2305912.1,
                                           SRR14372080.2239069.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1122
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1122
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 18"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=126953
     Region          153..182
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          188..215
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          324..596
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          723..1122
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1122
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407833.1:575..3943"
                     /note="isoform 18 is encoded by transcript variant 18"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 mgakdatpvp cgrwakilek dkrtqqmrmq rlkaklqmpf qsgefkaltr rlqveprlls
       61 kqmagcledc trqapespwe eqlarllqea pgklsldveq apsgqhsqaq lsgqqqrlla
      121 ffkcclltdq lplahhllvv hhgqrqkrkl ltldmynavm lgwarqgafk elvyvlfmvk
      181 dagltpdlls yaaalqcmgr qdqdagtier cleqmsqegl klqalftavl lseedratvl
      241 kavhkvkptf slppqlpppv ntskllrdvy akdgrvsypk lhlplktlqc lfekqlhmel
      301 asrvcvvsve kptlpskevk harktlktlr dqwekalcra lretknrler evyegrfsly
      361 pflclldere vvrmllqvlq alpaqgesft tlarelsart fsrhvvqrqr vsgqvqalqn
      421 hyrkylclla sdaevpepcl prqyweelga pealreqpwp lpvqmelgkl laemlvqatq
      481 mpcsldkphr ssrlvpvlyh vysfrnvqqi gilkphpayv qllekaaept ltfeavdvpm
      541 lcpplpwtsp hsgafllspt klmrtvegat qhqelletcp ptalhgalda ltqlgncawr
      601 vngrvldlvl qlfqakgcpq lgvpappsea pqppeahlph saaparkael rrelahcqkv
      661 aremhslrae alyrlslaqh lrdrvfwlph nmdfrgrtyp cpphfnhlgs dvarallefa
      721 qgrplgphgl dwlkihlvnl tglkkreplr krlafaeevm ddildsadqp ltgrkwwmga
      781 eepwqtlacc mevanavras dpaayvshlp vhqdgscngl qhyaalgrds vgaasvnlep
      841 sdvpqdvysg vaaqvevfrr qdaqrgmrva qvlegfitrk vvkqtvmtvv ygvtryggrl
      901 qiekrlrels dfpqefvwea shylvrqvfk slqemfsgtr aiqhwltesa rlishmgsvv
      961 ewvtplgvpv iqpyrldskv kqigggiqsi tythngdisr kpntrkqkng fppnfihsld
     1021 sshmmltalh cyrkgltfvs vhdcywthaa dvsvmnqvcr eqfvrlhsep ilqdlsrflv
     1081 krfcsepqki leasqlketl qavpkpgafd leqvkrstyf fs
//
LOCUS       NP_001400676             831 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform j [Homo sapiens].
ACCESSION   NP_001400676
VERSION     NP_001400676.1
DBSOURCE    REFSEQ: accession NM_001413747.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 831)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 831)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 831)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 831)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 831)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 831)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 831)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 831)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 831)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 831)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1083086.1,
                                           SRR14038194.3979151.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..831
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..831
                     /product="polyhomeotic-like protein 1 isoform j"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=88086
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          212..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          261..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          655..762
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          762..830
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(780..781,815..816,819..820,823)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(791..795,797..798,801..802,806,811)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..831
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413747.1:368..2863"
                     /note="isoform j is encoded by transcript variant 11"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq asinlattsa aqlisrsqsv
      121 sspsattltq svllgnttsp plnqsqaqmy lrpqlgnllq vnrtlgrnvp lasqlilmpn
      181 gavaavqqev psaqspgvha dadqvqnlav rnqqasaqgp qmqgstqkai ppgaspvssl
      241 sqassqalav aqassgatnq slnlsqaggg sgnsipgsmg pggggqahgg lgqlpssgmg
      301 ggscprkgtg vvqplpaaqt vtvsqgsqte aesaaakkae adgsgqqnvg mnltrtatpa
      361 psqtlissat ytqiqphsli qqqqqihlqq kqvviqqqia ihhqqqfqhr qsqllhtath
      421 lqlaqqqqqq qqqqqqqqqp qattltapqp pqvpptqqgk pqtlavkrka dseeerddvs
      481 tlgsmlpaka spvaespkvm deksslgeka esvanvnant psselvaltp apsvppptla
      541 mvsrqmgdsk ppqaivkpqi lthiiegfvi qegaepfpvg csqllkesek plqtglptgl
      601 tenqsggplg vdspsaeldk kanllkceyc gkyapaeqfr gskrfcsmtc akrynvscsh
      661 qfrlkrkkmk efqeanyarv rrrgprrsss diarakiqgk chrgqedssr gsdnssydea
      721 lsptspgpls vraghgerdl gnpntapptp elhginpvfl ssnpsrwsve evyefiaslq
      781 gcqeiaeefr sqeidgqall llkeehlmsa mniklgpalk icakinvlke t
//
LOCUS       NP_001428261            1655 aa            linear   PRI 21-NOV-2025
DEFINITION  BCL-6 corepressor-like protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001428261 XP_047298298 XP_054183525
VERSION     NP_001428261.1
DBSOURCE    REFSEQ: accession NM_001441332.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1655)
  AUTHORS   Luo,C., Chen,Z., Meng,L., Tan,C., He,W., Tu,C., Du,J., Lu,G.X.,
            Lin,G., Tan,Y.Q. and Hu,T.Y.
  TITLE     A hemizygous loss-of-function variant in BCORL1 is associated with
            male infertility and oligoasthenoteratozoospermia
  JOURNAL   Clin Genet 106 (1), 27-36 (2024)
   PUBMED   38342987
  REMARK    GeneRIF: A hemizygous loss-of-function variant in BCORL1 is
            associated with male infertility and oligoasthenoteratozoospermia.
REFERENCE   2  (residues 1 to 1655)
  AUTHORS   Kommoss,F.K.F., Chiang,S., Kobel,M., Koelsche,C., Chang,K.T.,
            Irving,J.A., Dickson,B., Thiryayi,S., Rouzbahman,M., Rasty,G., von
            Deimling,A., Lee,C.H. and Turashvili,G.
  TITLE     Endometrial Stromal Sarcomas With BCOR Internal Tandem Duplication
            and Variant BCOR/BCORL1 Rearrangements Resemble High-grade
            Endometrial Stromal Sarcomas With Recurrent CDK4 Pathway
            Alterations and MDM2 Amplifications
  JOURNAL   Am J Surg Pathol 46 (8), 1142-1152 (2022)
   PUBMED   35499168
  REMARK    GeneRIF: Endometrial Stromal Sarcomas With BCOR Internal Tandem
            Duplication and Variant BCOR/BCORL1 Rearrangements Resemble
            High-grade Endometrial Stromal Sarcomas With Recurrent CDK4 Pathway
            Alterations and MDM2 Amplifications.
REFERENCE   3  (residues 1 to 1655)
  AUTHORS   Schaefer,E.J., Wang,H.C., Karp,H.Q., Meyer,C.A., Cejas,P.,
            Gearhart,M.D., Adelman,E.R., Fares,I., Apffel,A., Lim,K., Xie,Y.,
            Gibson,C.J., Schenone,M., Murdock,H.M., Wang,E.S., Gondek,L.P.,
            Carroll,M.P., Vedula,R.S., Winer,E.S., Garcia,J.S., Stone,R.M.,
            Luskin,M.R., Carr,S.A., Long,H.W., Bardwell,V.J., Figueroa,M.E. and
            Lindsley,R.C.
  TITLE     BCOR and BCORL1 Mutations Drive Epigenetic Reprogramming and
            Oncogenic Signaling by Unlinking PRC1.1 from Target Genes
  JOURNAL   Blood Cancer Discov 3 (2), 116-135 (2022)
   PUBMED   35015684
  REMARK    GeneRIF: BCOR and BCORL1 Mutations Drive Epigenetic Reprogramming
            and Oncogenic Signaling by Unlinking PRC1.1 from Target Genes.
REFERENCE   4  (residues 1 to 1655)
  AUTHORS   Gafner,M., Michelson,M., Argilli,E., Yosovich,K., Sherr,E.H.,
            Parks,K.C., England,E.M., Hady-Cohen,R., Leibovitz,Z., Lev,D.,
            Michaeli-Yosef,Y., Lerman-Sagie,T. and Blumkin,L.
  TITLE     Major brain malformations: corpus callosum dysgenesis, agenesis of
            septum pellucidum and polymicrogyria in patients with
            BCORL1-related disorders
  JOURNAL   J Hum Genet 67 (2), 95-101 (2022)
   PUBMED   34400773
  REMARK    GeneRIF: Major brain malformations: corpus callosum dysgenesis,
            agenesis of septum pellucidum and polymicrogyria in patients with
            BCORL1-related disorders.
REFERENCE   5  (residues 1 to 1655)
  AUTHORS   Junco,S.E., Wang,R., Gaipa,J.C., Taylor,A.B., Schirf,V.,
            Gearhart,M.D., Bardwell,V.J., Demeler,B., Hart,P.J. and Kim,C.A.
  TITLE     Structure of the polycomb group protein PCGF1 in complex with BCOR
            reveals basis for binding selectivity of PCGF homologs
  JOURNAL   Structure 21 (4), 665-671 (2013)
   PUBMED   23523425
REFERENCE   6  (residues 1 to 1655)
  AUTHORS   Shaffer,J.R., Feingold,E., Wang,X., Lee,M., Tcuenco,K., Weeks,D.E.,
            Weyant,R.J., Crout,R., McNeil,D.W. and Marazita,M.L.
  TITLE     GWAS of dental caries patterns in the permanent dentition
  JOURNAL   J Dent Res 92 (1), 38-44 (2013)
   PUBMED   23064961
REFERENCE   7  (residues 1 to 1655)
  AUTHORS   Gao,Z., Zhang,J., Bonasio,R., Strino,F., Sawai,A., Parisi,F.,
            Kluger,Y. and Reinberg,D.
  TITLE     PCGF homologs, CBX proteins, and RYBP define functionally distinct
            PRC1 family complexes
  JOURNAL   Mol Cell 45 (3), 344-356 (2012)
   PUBMED   22325352
REFERENCE   8  (residues 1 to 1655)
  AUTHORS   Li,M., Collins,R., Jiao,Y., Ouillette,P., Bixby,D., Erba,H.,
            Vogelstein,B., Kinzler,K.W., Papadopoulos,N. and Malek,S.N.
  TITLE     Somatic mutations in the transcriptional corepressor gene BCORL1 in
            adult acute myelogenous leukemia
  JOURNAL   Blood 118 (22), 5914-5917 (2011)
   PUBMED   21989985
  REMARK    GeneRIF: BCORL1 by genetic criteria is a novel candidate tumor
            suppressor gene, joining the growing list of genes recurrently
            mutated in acute myelogenous leukemia.
REFERENCE   9  (residues 1 to 1655)
  AUTHORS   Pagan,J.K., Arnold,J., Hanchard,K.J., Kumar,R., Bruno,T.,
            Jones,M.J., Richard,D.J., Forrest,A., Spurdle,A., Verdin,E.,
            Crossley,M., Fanciulli,M., Chenevix-Trench,G., Young,D.B. and
            Khanna,K.K.
  TITLE     A novel corepressor, BCoR-L1, represses transcription through an
            interaction with CtBP
  JOURNAL   J Biol Chem 282 (20), 15248-15257 (2007)
   PUBMED   17379597
REFERENCE   10 (residues 1 to 1655)
  AUTHORS   Lose,F., Arnold,J., Young,D.B., Brown,C.J., Mann,G.J., Pupo,G.M.,
            Khanna,K.K., Chenevix-Trench,G. and Spurdle,A.B.
  CONSRTM   Kathleen Cuningham Foundation Consortium for Research into Familial
            Breast Cancer
  TITLE     BCoR-L1 variation and breast cancer
  JOURNAL   Breast Cancer Res 9 (4), R54 (2007)
   PUBMED   17697391
  REMARK    GeneRIF: Dysregulated BCoR-L1 expression is associated with breast
            cancer
            Erratum:[Breast Cancer Res. 2008;10(5):406]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL034405.16, Z82208.1,
            KF459400.1 and AL136450.8.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_047298298.1, XP_054183525.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            corepressor that is found tethered to promoter regions by
            DNA-binding proteins. The encoded protein can interact with several
            different class II histone deacetylases to repress transcription.
            Two transcript variants encoding different isoforms have been found
            for this gene. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1737213.1,
                                           SRR14038197.1077823.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1655
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.1"
     Protein         1..1655
                     /product="BCL-6 corepressor-like protein 1 isoform 2"
                     /note="BCoR-like protein 1"
                     /calculated_mol_wt=174863
     Region          65..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          113..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          <198..636
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          343..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          527..550
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          562..646
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          753..781
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          876..901
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          937..977
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1029
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1033
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          <1364..>1473
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1366..1397
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1367,1371..1372,1375..1377,1379..1380,1384,1387,
                     1397,1399,1401,1405..1406,1409..1411,1413..1414,1418,1421,
                     1430,1432,1434,1438..1439,1442..1444,1446..1447,1451,1454)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1399..1430
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1432..1461
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1536..1649
                     /region_name="PUFD_like_1"
                     /note="PCGF Ub-like fold discriminator of BCOR-like 1;
                     cd14260"
                     /db_xref="CDD:271223"
     Site            order(1538,1540..1550,1552,1554,1563..1565,1567,
                     1608..1609,1611,1614,1636,1647,1649)
                     /site_type="other"
                     /note="RAWUL domain interface [polypeptide binding]"
                     /db_xref="CDD:271223"
     CDS             1..1655
                     /gene="BCORL1"
                     /gene_synonym="BCoR-L1; CXorf10; SHUVER"
                     /coded_by="NM_001441332.1:173..5140"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="GeneID:63035"
                     /db_xref="HGNC:HGNC:25657"
                     /db_xref="MIM:300688"
ORIGIN      
        1 mistaplysg vhnwtssdri rmcgineerr aplsdeestt gdcqhfgsqe fcvsssfskv
       61 eltavgsgsn argadpdgsa teklghksed kpddpqpkmd yagnvaeaeg llvplsspgd
      121 glklpasdsa easnsradcs wtplntqmsk qvdcspagvk aldsrqgvge kntfilatlg
      181 tgvpvegtlp lvttnfsplp apicppapgs asvphsvpda fqvplsvpap vphsglvpvq
      241 vatsvpapsp plapvpalap appsvptlis dsnplsvsas vlvpvpasap psgpvplsap
      301 apaplsvpvs applaliqap vppsaptlvl apvptpvlap mpastppaap appsvpmptp
      361 tpssgppstp tlipafaptp vpaptpapif tpaptpmpaa tpaaiptsap ipasfslsrv
      421 cfpaaqapam qkvplsfqpg tvltpsqplv yipppscgqp lsvatlpttl gvsstltlpv
      481 lpsylqdrcl pgvlaspelr sypyafsvar pltsdsklvs levnrlpcts psgstttqpa
      541 pdgvpgplad tslvtasakv lptpqpllpa psgssapphp akmpsgteqq tegtsvtfsp
      601 lksppqlere masppecsem pldlssksnr qklplpnqrk tppmpvltpv htsskallst
      661 vlsrsqrttq aaggnvtscl gstsspfvif peivrngdps twvknstali stipgtyvgv
      721 anpvpaslll nkdpnlglnr dprhlpkqep isiidqgepk gtgatcgkkg sqagaegqps
      781 tvkrytpari apglpgcqtk elslwkptgp aniyprcsvn gkptstqvlp vgwspyhqas
      841 llsigissag qltpsqgapi rptsvvsefs gvpslsssea vhglpegqpr pggsfvpeqd
      901 pvtknktcri aakpyeeqvn pvlltlspqt gtlalsvqps ggdirmnqgp eeseshlcsd
      961 stpkmegpqg acglklagdt kpknqvlaty mshelvlatp qnlpkmpelp llphdshpke
     1021 lildvvpssr rgssterpql gsqvdlgrvk mekvdgdvvf nlatcfradg lpvapqrgqa
     1081 evrakagqar vkqesvgvfa cknkwqpddv teslppkkmk cgkekdseeq qlqpqakavv
     1141 rsshrpkcrk lpsdpqestk ksprgasdsg kehngvrgkh khrkptkpes qspgkradsh
     1201 eegslekkak ssfrdfipvv lstrtrsqsd lkarkqktss sqslehrlrn rnlllpnkvq
     1261 gisdspngfl pnnleepacl ensekpsgkr kcktkhmatv seeakgkgrw sqqktrspks
     1321 ptpvkptepc tpsksrsass eeasesptar qippearrli vnknagetll qraarlgykd
     1381 vvlyclqkds edvnhrdnag ytalheacsr gwtdilnill ehganvncsa qdgtrpvhda
     1441 vvndnletiw lllsygadpt latysgqtam klassdtmkr flsdhlsdlq graegdpgvs
     1501 wdfysssvle ekdgfacdll hnppgssdqe gddpmeeddf mfelsdkpll pcynlqvsvs
     1561 rgpcnwflfs dvlkrlklss rifqarfphf eittmpkaef yrqvassqll tpaerpggld
     1621 drsppgsset velvryepdl lrllgsevef qscns
//
LOCUS       NP_001427724             200 aa            linear   PRI 21-NOV-2025
DEFINITION  translocon-associated protein subunit delta isoform 4 precursor
            [Homo sapiens].
ACCESSION   NP_001427724 XP_047298345 XP_054183597
VERSION     NP_001427724.1
DBSOURCE    REFSEQ: accession NM_001440795.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Gemmer,M., Chaillet,M.L., van Loenhout,J., Cuevas Arenas,R.,
            Vismpas,D., Grollers-Mulderij,M., Koh,F.A., Albanese,P.,
            Scheltema,R.A., Howes,S.C., Kotecha,A., Fedry,J. and Forster,F.
  TITLE     Visualization of translation and protein biogenesis at the ER
            membrane
  JOURNAL   Nature 614 (7946), 160-167 (2023)
   PUBMED   36697828
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Castiglioni,C., Feillet,F., Barnerias,C., Wiedemann,A., Muchart,J.,
            Cortes,F., Hernando-Davalillo,C., Montero,R., Dupre,T., Bruneel,A.,
            Seta,N., Vuillaumier-Barrot,S. and Serrano,M.
  TITLE     Expanding the phenotype of X-linked SSR4-CDG: Connective tissue
            implications
  JOURNAL   Hum Mutat 42 (2), 142-149 (2021)
   PUBMED   33300232
  REMARK    GeneRIF: Expanding the phenotype of X-linked SSR4-CDG: Connective
            tissue implications.
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Ng,B.G., Raymond,K., Kircher,M., Buckingham,K.J., Wood,T.,
            Shendure,J., Nickerson,D.A., Bamshad,M.J., Wong,J.T.,
            Monteiro,F.P., Graham,B.H., Jackson,S., Sparkes,R., Scheuerle,A.E.,
            Cathey,S., Kok,F., Gibson,J.B. and Freeze,H.H.
  CONSRTM   University of Washington Center for Mendelian Genomics
  TITLE     Expanding the Molecular and Clinical Phenotype of SSR4-CDG
  JOURNAL   Hum Mutat 36 (11), 1048-1051 (2015)
   PUBMED   26264460
  REMARK    GeneRIF: We now report eight affected males with either de novo (4)
            or inherited (4) loss of function mutations in SSR4.
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Wang,Z. and VandeBerg,J.L.
  TITLE     Cloning and molecular characterization of a human ortholog of
            Monodelphis TRAPD in ultraviolet B-induced melanoma
  JOURNAL   Melanoma Res 14 (2), 107-114 (2004)
   PUBMED   15057039
  REMARK    GeneRIF: results of this study implicate TRAPD as a candidate gene
            with potential functions that might be associated with
            ultraviolet-induced melanomagenesis and metastasis
REFERENCE   6  (residues 1 to 200)
  AUTHORS   Dodson,G. and Steiner,D.
  TITLE     The role of assembly in insulin's biosynthesis
  JOURNAL   Curr Opin Struct Biol 8 (2), 189-194 (1998)
   PUBMED   9631292
  REMARK    Review article
REFERENCE   7  (residues 1 to 200)
  AUTHORS   Brenner,V., Nyakatura,G., Rosenthal,A. and Platzer,M.
  TITLE     Genomic organization of two novel genes on human Xq28: compact head
            to head arrangement of IDH gamma and TRAP delta is conserved in rat
            and mouse
  JOURNAL   Genomics 44 (1), 8-14 (1997)
   PUBMED   9286695
REFERENCE   8  (residues 1 to 200)
  AUTHORS   Holthuis,J.C., van Riel,M.C. and Martens,G.J.
  TITLE     Translocon-associated protein TRAP delta and a novel TRAP-like
            protein are coordinately expressed with pro-opiomelanocortin in
            Xenopus intermediate pituitary
  JOURNAL   Biochem J 312 (Pt 1) (Pt 1), 205-213 (1995)
   PUBMED   7492314
REFERENCE   9  (residues 1 to 200)
  AUTHORS   Hartmann,E., Gorlich,D., Kostka,S., Otto,A., Kraft,R., Knespel,S.,
            Burger,E., Rapoport,T.A. and Prehn,S.
  TITLE     A tetrameric complex of membrane proteins in the endoplasmic
            reticulum
  JOURNAL   Eur J Biochem 214 (2), 375-381 (1993)
   PUBMED   7916687
REFERENCE   10 (residues 1 to 200)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U52111.3.
            
            On or before May 30, 2025 this sequence version replaced
            XP_047298345.1, XP_054183597.1.
            
            Summary: This gene encodes the delta subunit of the
            translocon-associated protein complex which is involved in
            translocating proteins across the endoplasmic reticulum membrane.
            The encoded protein is located in the Xq28 region and is arranged
            in a compact head-to-head manner with the isocitrate dehydrogenase
            3 (NAD+) gamma gene and both genes are driven by a CpG-embedded
            bidirectional promoter. Alternate splicing results in multiple
            transcript variants.[provided by RefSeq, Mar 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3405020.1,
                                           SRR12514507.843961.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..200
                     /product="translocon-associated protein subunit delta
                     isoform 4 precursor"
                     /note="translocon-associated protein subunit delta;
                     SSR-delta; TRAP-delta; signal sequence receptor, delta"
                     /calculated_mol_wt=16766
     sig_peptide     1..50
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=5319
     Region          51..199
                     /region_name="TRAP-delta"
                     /note="Translocon-associated protein, delta subunit
                     precursor (TRAP-delta); pfam05404"
                     /db_xref="CDD:398850"
     CDS             1..200
                     /gene="SSR4"
                     /gene_synonym="CDG1Y; TRAPD"
                     /coded_by="NM_001440795.1:167..769"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:6748"
                     /db_xref="HGNC:HGNC:11326"
                     /db_xref="MIM:300090"
ORIGIN      
        1 mteseslrts rhadtalarv rrgreeamaa maslgalall llsslsrcsa eaclepqitp
       61 syyttsdavi stetvfivei sltcknrvqn malyadvggk qfpvtrgqdv gryqvswsld
      121 hksahagtye vrffdeesys llrkaqrnne disiipplft vsvdhrgtwn gpwvstevla
      181 aaiglviyyl afsakshiqa
//
LOCUS       NP_001396230            2696 aa            linear   PRI 21-NOV-2025
DEFINITION  histone-lysine N-methyltransferase, H3 lysine-36 specific isoform b
            [Homo sapiens].
ACCESSION   NP_001396230
VERSION     NP_001396230.1
DBSOURCE    REFSEQ: accession NM_001409301.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2696)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2696)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   3  (residues 1 to 2696)
  AUTHORS   Conteduca,G., Cangelosi,D., Baldo,C., Arado,A., Testa,B.,
            Wagner,R.T., Robertson,K.D., Dequiedt,F., Fitzsimmons,L.,
            Malacarne,M., Filaci,G. and Coviello,D.A.
  TITLE     Impact of NSD1 Alternative Transcripts in Actin Filament Formation
            and Cellular Division Pathways in Fibroblasts
  JOURNAL   Genes (Basel) 15 (9), 1117 (2024)
   PUBMED   39336709
  REMARK    GeneRIF: Impact of NSD1 Alternative Transcripts in Actin Filament
            Formation and Cellular Division Pathways in Fibroblasts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2696)
  AUTHORS   Ren,Z., Yue,L., Hu,H.Y., Hou,X.L., Chen,W.Q., Tan,Y., Dong,Z. and
            Zhang,J.
  TITLE     Identification of Novel NSD1 variations in four Pediatric cases
            with sotos Syndrome
  JOURNAL   BMC Med Genomics 17 (1), 116 (2024)
   PUBMED   38684994
  REMARK    GeneRIF: Identification of Novel NSD1 variations in four Pediatric
            cases with sotos Syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2696)
  AUTHORS   Wang,X., Yeh,S., Wu,G., Hsu,C.L., Wang,L., Chiang,T., Yang,Y.,
            Guo,Y. and Chang,C.
  TITLE     Identification and characterization of a novel androgen receptor
            coregulator ARA267-alpha in prostate cancer cells
  JOURNAL   J Biol Chem 276 (44), 40417-40423 (2001)
   PUBMED   11509567
REFERENCE   6  (residues 1 to 2696)
  AUTHORS   Jaju,R.J., Fidler,C., Haas,O.A., Strickson,A.J., Watkins,F.,
            Clark,K., Cross,N.C., Cheng,J.F., Aplan,P.D., Kearney,L.,
            Boultwood,J. and Wainscoat,J.S.
  TITLE     A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in
            de novo childhood acute myeloid leukemia
  JOURNAL   Blood 98 (4), 1264-1267 (2001)
   PUBMED   11493482
REFERENCE   7  (residues 1 to 2696)
  AUTHORS   Lee,D.K., Duan,H.O. and Chang,C.
  TITLE     Androgen receptor interacts with the positive elongation factor
            P-TEFb and enhances the efficiency of transcriptional elongation
  JOURNAL   J Biol Chem 276 (13), 9978-9984 (2001)
   PUBMED   11266437
REFERENCE   8  (residues 1 to 2696)
  AUTHORS   Huang,N., vom Baur,E., Garnier,J.M., Lerouge,T., Vonesch,J.L.,
            Lutz,Y., Chambon,P. and Losson,R.
  TITLE     Two distinct nuclear receptor interaction domains in NSD1, a novel
            SET protein that exhibits characteristics of both corepressors and
            coactivators
  JOURNAL   EMBO J 17 (12), 3398-3412 (1998)
   PUBMED   9628876
REFERENCE   9  (residues 1 to 2696)
  AUTHORS   Ocansey,S., Cole,T.R.P., Rahman,N. and Tatton-Brown,K.
  TITLE     Sotos Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301652
REFERENCE   10 (residues 1 to 2696)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027314.5, AC008570.6 and
            AC146507.2.
            
            Summary: This gene encodes a protein containing a SET domain, 2
            LXXLL motifs, 3 nuclear translocation signals (NLSs), 4 plant
            homeodomain (PHD) finger regions, and a proline-rich region. The
            encoded protein enhances androgen receptor (AR) transactivation,
            and this enhancement can be increased further in the presence of
            other androgen receptor associated coregulators. This protein may
            act as a nucleus-localized, basic transcriptional factor and also
            as a bifunctional transcriptional regulator. Mutations of this gene
            have been associated with Sotos syndrome and Weaver syndrome. One
            version of childhood acute myeloid leukemia is the result of a
            cryptic translocation with the breakpoints occurring within nuclear
            receptor-binding Su-var, enhancer of zeste, and trithorax domain
            protein 1 on chromosome 5 and nucleoporin, 98-kd on chromosome 11.
            Multiple transcript variants encoding distinct isoforms have been
            identified for this gene. [provided by RefSeq, Sep 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3231601.1,
                                           SRR18074969.1414867.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2696
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..2696
                     /product="histone-lysine N-methyltransferase, H3 lysine-36
                     specific isoform b"
                     /EC_number="2.1.1.357"
                     /note="androgen receptor-associated coregulator 267;
                     histone-lysine N-methyltransferase, H3 lysine-36 and H4
                     lysine-20 specific; H3-K36-HMTase; H4-K20-HMTase; lysine
                     N-methyltransferase 3B; NR-binding SET domain-containing
                     protein; androgen receptor coactivator 267 kDa protein;
                     androgen receptor-associated protein of 267 kDa; nuclear
                     receptor-binding SET domain-containing protein 1; nuclear
                     receptor SET domain-containing protein 1; histone-lysine
                     N-methyltransferase, H3 lysine-36 specific"
                     /calculated_mol_wt=296522
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88491; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          207..252
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          281..311
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          318..433
                     /region_name="PWWP_NSD1_rpt1"
                     /note="first PWWP domain found in nuclear receptor-binding
                     SET domain-containing protein 1 (NSD1) and similar
                     proteins; cd20161"
                     /db_xref="CDD:438989"
     Site            order(334,337,368)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438989"
     Site            335..338
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438989"
     Site            order(406..408,411..412)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438989"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          487..514
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17487921; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          872..891
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          936..1035
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1067..1093
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1112..1134
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1243..1272
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1294..1344
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1382..1428
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          <1431..1587
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          1480..1534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            1510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88491; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1545..1587
                     /region_name="PHD1_NSD1_2"
                     /note="PHD finger 1 found in nuclear receptor-binding SET
                     domain-containing protein NSD1 and NSD2; cd15648"
                     /db_xref="CDD:277118"
     Site            order(1545,1554..1558,1563,1581)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277118"
     Region          1592..1638
                     /region_name="PHD2_NSD1"
                     /note="PHD finger 2 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15650"
                     /db_xref="CDD:277120"
     Site            order(1592,1602..1606,1612,1633)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277120"
     Region          1639..1692
                     /region_name="PHD3_NSD1"
                     /note="PHD finger 3 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15653"
                     /db_xref="CDD:277123"
     Site            order(1639,1657..1661,1665,1687)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277123"
     Region          1709..1748
                     /region_name="PHD4_NSD1"
                     /note="PHD finger 4 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15656"
                     /db_xref="CDD:277126"
     Site            order(1709,1718..1722,1726,1743)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277126"
     Region          1755..1850
                     /region_name="PWWP_NSD1_rpt2"
                     /note="second PWWP domain found in nuclear
                     receptor-binding SET domain-containing protein 1 (NSD1)
                     and similar proteins; cd20164"
                     /db_xref="CDD:438992"
     Site            order(1767,1770,1798)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438992"
     Site            1768..1771
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438992"
     Region          1901..1939
                     /region_name="AWS"
                     /note="AWS domain; pfam17907"
                     /db_xref="CDD:465559"
     Region          1941..2082
                     /region_name="SET_NSD1"
                     /note="SET domain (including post-SET domain) found in
                     nuclear receptor-binding SET domain-containing protein 1
                     (NSD1) and similar proteins; cd19210"
                     /db_xref="CDD:380987"
     Site            order(1952..1954,1971,1981,1985,1994..2000,2017..2021,
                     2028..2030,2045,2056..2066,2068..2072,2081)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380987"
     Site            order(1952..1954,1994..1997,2017..2021,2058,2065,
                     2069..2072,2081)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380987"
     Site            order(1971,1981,1985,1996..2000,2028..2030,2045,
                     2056..2060)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:380987"
     Site            order(2023,2070,2072,2077)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380987"
     Region          2060..2066
                     /region_name="Inhibits enzyme activity in the absence of
                     bound histone"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2091..2111
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2120..2162
                     /region_name="PHD5_NSD1"
                     /note="PHD finger 5 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15659"
                     /db_xref="CDD:277129"
     Site            order(2120,2129..2133,2139,2157)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277129"
     Region          2161..2210
                     /region_name="C5HCH"
                     /note="NSD Cys-His rich domain; pfam17982"
                     /db_xref="CDD:465605"
     Region          <2208..2574
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          2213..2422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            2369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            2462
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2464..2499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            2471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2553..2575
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2595..2616
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2665..2696
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     CDS             1..2696
                     /gene="NSD1"
                     /gene_synonym="ARA267; KMT3B; SOTOS; SOTOS1; STO"
                     /coded_by="NM_001409301.1:155..8245"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="GeneID:64324"
                     /db_xref="HGNC:HGNC:14234"
                     /db_xref="MIM:606681"
ORIGIN      
        1 mdqtcelprr ncllpfsnpv nldapedkds pfgngqsnfs eplngctmql stvsgtsqna
       61 ygqdspscyi plrrlqdlas minveylngs adgsesfqdp eksdsraqtp ivctslspgg
      121 ptalamkqep scnnspelqv kvtktikngf lhfenftcvd dadvdsemdp eqpvtedesi
      181 eeifeetqtn atcnyetkse ngvkvamgse qdstpesrhg avkspflpla pqtetqknkq
      241 rnevdgsnek aallpapfsl gdtnitieeq lnsinlsfqd dpdsststlg nmlelpgtss
      301 sstsqelpfc qpkkkstplk yevgdliwak fkrrpwwpcr icsdplinth skmkvsnrrp
      361 yrqyyveafg dpserawvag kaivmfegrh qfeelpvlrr rgkqkekgyr hkvpqkilsk
      421 weasvglaeq ydvpkgsknr kcipgsikld seedmpfedc tndpesehdl llngclksla
      481 fdsehsadek ekpcaksrar kssdnpkrts vkkghiqfea hkderrgkip enlglnfisg
      541 disdtqasne lsriansltg sntapgsflf sscgkntakk efetsngdsl lglpegalis
      601 kcsreknkpq rslvcgskvk lcyigagdee krsdsisict tsddgssdld piehssesdn
      661 svleipdafd rtenmlsmqk nekikysrfa atntrvkakq kplisnshtd hlmgctksae
      721 pgtetsqvnl sdlkastlvh kpqsdftnda lspkfnlsss issenslikg gaanqallhs
      781 kskqpkfrsi kckhkenpvm aeppvineec slkccssdtk gsplasisks gkvdglklln
      841 nmhektrdss dietavvkhv lselkelsyr slgedvsdsg tskpskpllf ssassqnhip
      901 iepdykfstl lmmlkdmhds ktkeqrlmta qnlvsyrspg rgdcstnspv gvskvlvsgg
      961 sthnsekkgd gtqnsanpsp sggdsalsge lsaslpglls dkrdlpasgk srsdcvtrrn
     1021 cgrskpsskl rdafsaqmvk ntvnrkalkt erkrklnqlp svtldavlqg drerggslrg
     1081 gaedpskedp lqimghltse dgdhfsdvhf dskvkqsdpg kisekglsfe ngkgpeldsv
     1141 mnsendelng vnqvvpkkrw qrlnqrrtkp rkrmnrfkek ensecafrvl lpsdpvqegr
     1201 defpehrtps asileeplte qnhadcldsa gprlnvcdks sasigdmeke pgipsltpqa
     1261 elpepavrse kkrlrkpskw lleyteeydq ifapkkkqkk vqeqvhkvss rceeesllar
     1321 grssaqnkqv denslistke eppvlereap flegplaqse lggghaelpq ltlsvpvape
     1381 vsprpalese ellvktpgny eskrqrkptk kllesndldp gfmpkkgdlg lskkcyeagh
     1441 lengitesca tsyskdfggg ttkifdkprk rkrqrhaaak mqckkvkndd sskeipgseg
     1501 elmphrtats pketveegve hdpgmpaskk mqgergggaa lkenvcqnce klgelllcea
     1561 qccgafhlec lgltemprgk ficnecrtgi htcfvckqsg edvkrcllpl cgkfyheecv
     1621 qkypptvmqn kgfrcslhic itchaanpan vsaskgrlmr cvrcpvayha ndfclaagsk
     1681 ilasnsiicp nhftprrgcr nhehvnvswc fvcseggsll ccdscpaafh reclnidipe
     1741 gnwycndcka gkkphyreiv wvkvgryrww paeichprav psnidkmrhd vgefpvlffg
     1801 sndylwthqa rvfpymegdv sskdkmgkgv dgtykkalqe aaarfeelka qkelrqlqed
     1861 rkndkkpppy khikvnrpig rvqiftadls eiprcnckat denpcgidse cinrmllyec
     1921 hptvcpaggr cqnqcfskrq ypeveifrtl qrgwglrtkt dikkgefvne yvgelideee
     1981 crariryaqe hditnfymlt ldkdriidag pkgnyarfmn hccqpncetq kwsvngdtrv
     2041 glfalsdika gteltfnynl eclgngktvc kcgapncsgf lgvrpknqpi ateekskkfk
     2101 kkqqgkrrtq geitkerede cfscgdagql vsckkpgcpk vyhadclnlt krpagkwecp
     2161 whqcdicgke aasfcemcps sfckqhregm lfiskldgrl sctehdpcgp nplepgeire
     2221 yvpppvplpp gpsthlaeqs tgmaaqapkm sdkppadtnq mlslskkala gtcqrpllpe
     2281 rplertdsrp qpldkvrdla gsgtksqslv ssqrpldrpp avagprpqls dkpspvtsps
     2341 sspsvrsqpl erplgtadpr ldksigaasp rpqslektsv ptglrlpppd rllitsspkp
     2401 qtsdrptdkp haslsqrlpp pekvlsavvq tlvakekalr pvdqntqskn raalvmdlid
     2461 ltprqkeraa sphqvtpqad ekmpvlesss wpaskglghm pravekgcvs dplqtsgkaa
     2521 apsedpwqav ksltqarlls qppakaflye pttqasgras agaeqtpgpl sqspglvkqa
     2581 kqmvggqqlp alaaksgqsf rslgkapasl pteekklvtt eqspwalgka ssraglwpiv
     2641 agqtlaqscw sagstqtlaq tcwslgrgqd pkpeqntlpa lnqapsshkc aeseqk
//
LOCUS       NP_001427717            1151 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphorylase b kinase regulatory subunit alpha, skeletal muscle
            isoform isoform 3 [Homo sapiens].
ACCESSION   NP_001427717 XP_047298118 XP_054183174
VERSION     NP_001427717.1
DBSOURCE    REFSEQ: accession NM_001440788.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1151)
  AUTHORS   Yang,X., Zhu,M., Lu,X., Wang,Y. and Xiao,J.
  TITLE     Architecture and activation of human muscle phosphorylase kinase
  JOURNAL   Nat Commun 15 (1), 2719 (2024)
   PUBMED   38548794
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1151)
  AUTHORS   Bisciglia,M., Froissart,R., Bedat-Millet,A.L., Romero,N.B.,
            Pettazzoni,M., Hogrel,J.Y., Petit,F.M. and Stojkovic,T.
  TITLE     A novel PHKA1 mutation associating myopathy and cognitive
            impairment: Expanding the spectrum of phosphorylase kinase b (PhK)
            deficiency
  JOURNAL   J Neurol Sci 424, 117391 (2021)
   PUBMED   33799212
  REMARK    GeneRIF: A novel PHKA1 mutation associating myopathy and cognitive
            impairment: Expanding the spectrum of phosphorylase kinase b (PhK)
            deficiency.
REFERENCE   3  (residues 1 to 1151)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1151)
  AUTHORS   Preisler,N., Orngreen,M.C., Echaniz-Laguna,A., Laforet,P.,
            Lonsdorfer-Wolf,E., Doutreleau,S., Geny,B., Akman,H.O., Dimauro,S.
            and Vissing,J.
  TITLE     Muscle phosphorylase kinase deficiency: a neutral metabolic variant
            or a disease?
  JOURNAL   Neurology 78 (4), 265-268 (2012)
   PUBMED   22238410
  REMARK    GeneRIF: muscle PHKA deficiency may present as an almost
            asymptomatic condition, despite a mild impairment of muscle
REFERENCE   5  (residues 1 to 1151)
  AUTHORS   Echaniz-Laguna,A., Akman,H.O., Mohr,M., Tranchant,C.,
            Talmant-Verbist,V., Rolland,M.O. and Dimauro,S.
  TITLE     Muscle phosphorylase b kinase deficiency revisited
  JOURNAL   Neuromuscul Disord 20 (2), 125-127 (2010)
   PUBMED   20080404
REFERENCE   6  (residues 1 to 1151)
  AUTHORS   Gossen,M., Wullrich,A. and Kilimann,M.W.
  TITLE     Dinucleotide repeat polymorphism within the PHKA1 gene at Xq12-q13
  JOURNAL   Hum Genet 95 (4), 469-470 (1995)
   PUBMED   7705849
REFERENCE   7  (residues 1 to 1151)
  AUTHORS   Wehner,M., Clemens,P.R., Engel,A.G. and Kilimann,M.W.
  TITLE     Human muscle glycogenosis due to phosphorylase kinase deficiency
            associated with a nonsense mutation in the muscle isoform of the
            alpha subunit
  JOURNAL   Hum Mol Genet 3 (11), 1983-1987 (1994)
   PUBMED   7874115
REFERENCE   8  (residues 1 to 1151)
  AUTHORS   Herbert,M., Goldstein,J.L., Rehder,C., Austin,S., Kishnani,P.S. and
            Bali,D.S.
  TITLE     Phosphorylase Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21634085
REFERENCE   9  (residues 1 to 1151)
  AUTHORS   Meyer,H.E., Meyer,G.F., Dirks,H. and Heilmeyer,L.M. Jr.
  TITLE     Localization of phosphoserine residues in the alpha subunit of
            rabbit skeletal muscle phosphorylase kinase
  JOURNAL   Eur J Biochem 188 (2), 367-376 (1990)
   PUBMED   2108025
REFERENCE   10 (residues 1 to 1151)
  AUTHORS   Francke,U., Darras,B.T., Zander,N.F. and Kilimann,M.W.
  TITLE     Assignment of human genes for phosphorylase kinase subunits alpha
            (PHKA) to Xq12-q13 and beta (PHKB) to 16q12-q13
  JOURNAL   Am J Hum Genet 45 (2), 276-282 (1989)
   PUBMED   2757032
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC240504.3, BX295541.1 and
            BX295542.1.
            
            On or before May 29, 2025 this sequence version replaced
            XP_047298118.1, XP_054183174.1.
            
            Summary: Phosphorylase kinase is a polymer of 16 subunits, four
            each of alpha, beta, gamma and delta. The alpha subunit includes
            the skeletal muscle and hepatic isoforms, and the skeletal muscle
            isoform is encoded by this gene. The beta subunit is the same in
            both the muscle and hepatic isoforms, and encoded by one gene. The
            gamma subunit also includes the skeletal muscle and hepatic
            isoforms, which are encoded by two different genes. The delta
            subunit is a calmodulin and can be encoded by three different
            genes. The gamma subunits contain the active site of the enzyme,
            whereas the alpha and beta subunits have regulatory functions
            controlled by phosphorylation. The delta subunit mediates the
            dependence of the enzyme on calcium concentration. Mutations in
            this gene cause glycogen storage disease type 9D, also known as
            X-linked muscle glycogenosis. Alternatively spliced transcript
            variants encoding different isoforms have been identified in this
            gene. A pseudogene has been found on chromosome 1.[provided by
            RefSeq, Feb 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3779784.1,
                                           SRR14038197.2154798.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1151
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..1151
                     /product="phosphorylase b kinase regulatory subunit alpha,
                     skeletal muscle isoform isoform 3"
                     /EC_number="2.7.11.19"
                     /note="phosphorylase kinase, alpha 1 (muscle), muscle
                     glycogenosis; phosphorylase kinase alpha M subunit"
                     /calculated_mol_wt=129257
     Region          8..>439
                     /region_name="Glyco_hydro_15"
                     /note="Glycosyl hydrolases family 15; pfam00723"
                     /db_xref="CDD:395586"
     Region          <745..863
                     /region_name="Bac_rhamnosid6H"
                     /note="Bacterial alpha-L-rhamnosidase 6 hairpin
                     glycosidase domain; cl46875"
                     /db_xref="CDD:481215"
     Region          874..>1062
                     /region_name="KPBB_C"
                     /note="Phosphorylase b kinase C-terminal domain;
                     pfam19292"
                     /db_xref="CDD:437124"
     CDS             1..1151
                     /gene="PHKA1"
                     /gene_synonym="PHKA"
                     /coded_by="NM_001440788.1:318..3773"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="GeneID:5255"
                     /db_xref="HGNC:HGNC:8925"
                     /db_xref="MIM:311870"
ORIGIN      
        1 mrsrsnsgvr ldgyarlvqq tilchqnpvt gllpasydqk dawvrdnvys ilavwglgla
       61 yrknadrded kakayeleqs vvklmrgllh cmirqvdkve sfkysqstkd slhakyntkt
      121 catvvgddqw ghlqldatsv yllflaqmta sglhiihsld evnfiqnlvf yieaayktad
      181 fgiwergdkt nqgiselnas svgmakaale aldeldlfgv kggpqsvihv ladevqhcqs
      241 ilnsllpras tskevdasll svvsfpafav edsqlveltk qeiitklqgr ygccrflrdg
      301 yktpkedpnr lyyepaelkl feniecewpl fwtyfildgv fsgnaeqvqe ykealeavli
      361 kgkngvpllp elysvppdrv deeyqnphtv drvpmgklph mwgqslyilg slmaegflap
      421 geidplnrrf stvpkpdvvv qvsilaetee iktilkdkgi yvetiaevyp irvqparils
      481 hiysslgcnn rmklsgrpyr hmgvlgtskl ydirktiftf tpqfidqqqf ylaldnkmiv
      541 emlrtdlsyl csrwrmtgqp titfpishsm ldedgtslns silaalrkmq dgyfggarvq
      601 tgklsefltt sccthlsfmd pgpegklyse dyddnydyle sgnwmndyds tshdvhmylp
      661 tklfqasrps fnlldsphpr qenqvpsvrv eihlprdqsg evdfkalvlq lketsslqeq
      721 adilymlytm kgpdwntely nersatvrel ltelygkvge irhwgliryi sgilrkkvea
      781 ldeactdlls hqkhltvglp peprektisa plpyealtql ideasegdms isiltqeimv
      841 ylamymrtqp glfaemfrlr igliiqvmat elahslrcsa eeateglmnl spsamknllh
      901 hilsgkefgv ersvrptdsn vspaisihei gavgatkter tgimqlksei kqspgtsmtp
      961 ssgsfpsayd qqsskdsrqg qwqrrrrldg alnrvpvgfy qkvwkvlqkc hglsvegfvl
     1021 pssttremtp geikfsvhve svlnrvpqpe yrqllveail vltmladiei hsigsiiave
     1081 kivhiandlf lqeqktlgad dtmlakdpas gictllydsa psgrfgtmty lskaaatyvq
     1141 eflphsicam q
//
LOCUS       NP_001424664             619 aa            linear   PRI 21-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 8 [Homo sapiens].
ACCESSION   NP_001424664
VERSION     NP_001424664.1
DBSOURCE    REFSEQ: accession NM_001437735.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 619)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 619)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 619)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 619)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 619)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 619)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 619)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008641.7.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.366754.1,
                                           SRR18074968.3398395.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..619
                     /product="TNFAIP3-interacting protein 1 isoform 8"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=69944
     Region          14..>149
                     /region_name="Speriolin_N"
                     /note="Speriolin N terminus; pfam15058"
                     /db_xref="CDD:434426"
     Region          61..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          94..412
                     /region_name="Interaction with Nef"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Region          <214..>251
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          252..283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          <298..>538
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          351..367
                     /region_name="Interaction with Shigella flexneri ipah9.8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          431..588
                     /region_name="Required for inhibitory activity of
                     TNF-induced NF-kappa-B activation. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          452..510
                     /region_name="Ubiquitin-binding domain (UBD)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Region          524..530
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            552
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17632516; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            571
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9WUU8; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            599
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     CDS             1..619
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001437735.1:119..1978"
                     /note="isoform 8 is encoded by transcript variant 14"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 megrgpyriy dpggsvpsge asaaferlvk ensrlkekmq gikmlgelle esqmeatrlr
       61 qkaeelvkdn ellpppspsl gsfdplaelt gkdsnvtasp tapacpsdkp apvqkppssg
      121 tssefevvtp eeqnspesss hanamalgpl predgnlmlh lqrlettlsv caeepdhgql
      181 fthlgrmale fnrlaskvhk neqrtsilqt lceqlrkene alkakldkgl eqrdqaaerl
      241 reenlelkkl lmsngnkega sgrpgspkme gtgkkavagq qqasvtagkv pevvalgaae
      301 kkvkmleqqr sellevnkqw dqhfrsmkqq yeqkitelrq kladlqkqvt dleaereqkq
      361 rdfdrkllla kskiemeetd keqltaeake lrqkvkylqd qlspltrqre yqekeiqrln
      421 kaleealsiq tppsspptaf gspegagall rkqelvtqne llkqqvkife edfqrersdr
      481 ermneekeel kkqveklqaq vtlsnaqlka fkdeekarea lrqqkrkaka sgeryhveph
      541 pehlcgaypy ayppmpamvp hhgfedwsqi ryppppmame hppplpnsrl fhlhqfcrsr
      601 ntpgvypveg feiqirapk
//
LOCUS       NP_001427368            1124 aa            linear   PRI 21-NOV-2025
DEFINITION  tyrosine-protein kinase JAK3 [Homo sapiens].
ACCESSION   NP_001427368 XP_047294742 XP_054176885
VERSION     NP_001427368.1
DBSOURCE    REFSEQ: accession NM_001440439.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1124)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1124)
  AUTHORS   Tsilifis,C., Spegarova,J.S., Good,R., Griffin,H., Engelhardt,K.R.,
            Graham,S., Hughes,S., Arkwright,P.D., Hambleton,S. and Gennery,A.R.
  TITLE     Omenn Syndrome in Two Infants with Different Hypomorphic Variants
            in Janus Kinase 3
  JOURNAL   J Clin Immunol 44 (4), 98 (2024)
   PUBMED   38598033
  REMARK    GeneRIF: Omenn Syndrome in Two Infants with Different Hypomorphic
            Variants in Janus Kinase 3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1124)
  AUTHORS   Liongue,C., Ratnayake,T., Basheer,F. and Ward,A.C.
  TITLE     Janus Kinase 3 (JAK3): A Critical Conserved Node in Immunity
            Disrupted in Immune Cell Cancer and Immunodeficiency
  JOURNAL   Int J Mol Sci 25 (5), 2977 (2024)
   PUBMED   38474223
  REMARK    GeneRIF: Janus Kinase 3 (JAK3): A Critical Conserved Node in
            Immunity Disrupted in Immune Cell Cancer and Immunodeficiency.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1124)
  AUTHORS   Le,K., Vollenweider,J., Han,J., Staudinger,N., Stenson,M.,
            Bayraktar,L., Wellik,L.E., Maurer,M.J., McPhail,E.D., Witzig,T.E.
            and Gupta,M.
  TITLE     Dependence of peripheral T-cell lymphoma on constitutively
            activated JAK3: Implication for JAK3 inhibition as a therapeutic
            approach
  JOURNAL   Hematol Oncol 42 (1), e3233 (2024)
   PUBMED   37876297
  REMARK    GeneRIF: Dependence of peripheral T-cell lymphoma on constitutively
            activated JAK3: Implication for JAK3 inhibition as a therapeutic
            approach.
REFERENCE   5  (residues 1 to 1124)
  AUTHORS   Zhao,Y., Mu,Y., Zou,Y., He,Z., Lu,T., Wang,X., Li,W. and Gao,B.
  TITLE     Conjoint research of WGCNA, single-cell transcriptome and
            structural biology reveals the potential targets of IDD development
            and treatment and JAK3 involvement
  JOURNAL   Aging (Albany NY) 15 (24), 14764-14790 (2023)
   PUBMED   38095643
  REMARK    GeneRIF: Conjoint research of WGCNA, single-cell transcriptome and
            structural biology reveals the potential targets of IDD development
            and treatment and JAK3 involvement.
REFERENCE   6  (residues 1 to 1124)
  AUTHORS   Johnston,J.A., Wang,L.M., Hanson,E.P., Sun,X.J., White,M.F.,
            Oakes,S.A., Pierce,J.H. and O'Shea,J.J.
  TITLE     Interleukins 2, 4, 7, and 15 stimulate tyrosine phosphorylation of
            insulin receptor substrates 1 and 2 in T cells. Potential role of
            JAK kinases
  JOURNAL   J Biol Chem 270 (48), 28527-28530 (1995)
   PUBMED   7499365
REFERENCE   7  (residues 1 to 1124)
  AUTHORS   Russell,S.M., Tayebi,N., Nakajima,H., Riedy,M.C., Roberts,J.L.,
            Aman,M.J., Migone,T.S., Noguchi,M., Markert,M.L., Buckley,R.H.,
            O'Shea,J.J. and Leonard,W.J.
  TITLE     Mutation of Jak3 in a patient with SCID: essential role of Jak3 in
            lymphoid development
  JOURNAL   Science 270 (5237), 797-800 (1995)
   PUBMED   7481768
REFERENCE   8  (residues 1 to 1124)
  AUTHORS   Lai,K.S., Jin,Y., Graham,D.K., Witthuhn,B.A., Ihle,J.N. and
            Liu,E.T.
  TITLE     A kinase-deficient splice variant of the human JAK3 is expressed in
            hematopoietic and epithelial cancer cells
  JOURNAL   J Biol Chem 270 (42), 25028-25036 (1995)
   PUBMED   7559633
REFERENCE   9  (residues 1 to 1124)
  AUTHORS   Rolling,C., Treton,D., Beckmann,P., Galanaud,P. and Richard,Y.
  TITLE     JAK3 associates with the human interleukin 4 receptor and is
            tyrosine phosphorylated following receptor triggering
  JOURNAL   Oncogene 10 (9), 1757-1761 (1995)
   PUBMED   7538655
REFERENCE   10 (residues 1 to 1124)
  AUTHORS   Musso,T., Johnston,J.A., Linnekin,D., Varesio,L., Rowe,T.K.,
            O'Shea,J.J. and McVicar,D.W.
  TITLE     Regulation of JAK3 expression in human monocytes: phosphorylation
            in response to interleukins 2, 4, and 7
  JOURNAL   J Exp Med 181 (4), 1425-1431 (1995)
   PUBMED   7535338
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007201.1.
            
            On or before May 20, 2025 this sequence version replaced
            XP_047294742.1, XP_054176885.1.
            
            Summary: The protein encoded by this gene is a member of the Janus
            kinase (JAK) family of tyrosine kinases involved in cytokine
            receptor-mediated intracellular signal transduction. It is
            predominantly expressed in immune cells and transduces a signal in
            response to its activation via tyrosine phosphorylation by
            interleukin receptors. Mutations in this gene are associated with
            autosomal SCID (severe combined immunodeficiency disease).
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4207180.1,
                                           SRR18074968.2015684.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..1124
                     /product="tyrosine-protein kinase JAK3"
                     /EC_number="2.7.10.2"
                     /note="Janus kinase 3 (a protein tyrosine kinase,
                     leukocyte); leukocyte Janus kinase"
                     /calculated_mol_wt=124968
     Region          1..223
                     /region_name="Interaction with cytokine/interferon/growth
                     hormone receptors. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P52333.2)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62137; propagated from
                     UniProtKB/Swiss-Prot (P52333.2)"
     Region          26..112
                     /region_name="FERM_F1"
                     /note="FERM F1 ubiquitin-like domain; pfam18379"
                     /db_xref="CDD:465733"
     Region          126..245
                     /region_name="FERM_B-lobe"
                     /note="FERM domain B-lobe; cl46853"
                     /db_xref="CDD:481193"
     Region          250..362
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          362..458
                     /region_name="SH2_Jak3"
                     /note="Src homology 2 (SH2) domain in the Janus kinase 3
                     (Jak3) proteins; cd10380"
                     /db_xref="CDD:198243"
     Site            order(382,402,427,429)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198243"
     Site            order(428,457)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198243"
     Region          521..778
                     /region_name="PTK_Jak3_rpt1"
                     /note="Pseudokinase (repeat 1) domain of the Protein
                     Tyrosine Kinase, Janus kinase 3; cd14208"
                     /db_xref="CDD:271110"
     Site            592
                     /site_type="other"
                     /note="V617F mutation site"
                     /db_xref="CDD:271110"
     Site            785
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15121872; propagated from
                     UniProtKB/Swiss-Prot (P52333.2)"
     Region          817..1099
                     /region_name="PTKc_Jak3_rpt2"
                     /note="Catalytic (repeat 2) domain of the Protein Tyrosine
                     Kinase, Janus kinase 3; cd05081"
                     /db_xref="CDD:270665"
     Site            order(828..829,836,853,855,884,902..905,909,911,949,
                     953..954,956,966..967,986..990,999,1047)
                     /site_type="active"
                     /db_xref="CDD:270665"
     Site            order(828..829,836,853,855,884,902..905,909,911,953..954,
                     956,966..967)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270665"
     Site            904
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:18250158; propagated from
                     UniProtKB/Swiss-Prot (P52333.2)"
     Site            939
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:18250158; propagated from
                     UniProtKB/Swiss-Prot (P52333.2)"
     Site            order(949,953,986..990,999,1047)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270665"
     Site            966..992
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270665"
     Site            980
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15831699; propagated from
                     UniProtKB/Swiss-Prot (P52333.2)"
     Site            981
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15831699; propagated from
                     UniProtKB/Swiss-Prot (P52333.2)"
     CDS             1..1124
                     /gene="JAK3"
                     /gene_synonym="JAK-3; JAK3_HUMAN; JAKL; L-JAK; LJAK"
                     /coded_by="NM_001440439.1:82..3456"
                     /db_xref="GeneID:3718"
                     /db_xref="HGNC:HGNC:6193"
                     /db_xref="MIM:600173"
ORIGIN      
        1 mappseetpl ipqrscslls teagalhvll pargpgppqr lsfsfgdhla edlcvqaaka
       61 sgilpvyhsl falatedlsc wfppshifsv edastqvlly rirfyfpnwf glekchrfgl
      121 rkdlasaild lpvlehlfaq hrsdlvsgrl pvglslkeqg eclslavldl armareqaqr
      181 pgellktvsy kaclppslrd liqglsfvtr rrirrtvrra lrrvaacqad rhslmakyim
      241 dlerldpaga aetfhvglpg algghdglgl lrvagdggia wtqgeqevlq pfcdfpeivd
      301 isikqaprvg pagehrlvtv trtdnqilea efpglpeals fvalvdgyfr lttdsqhffc
      361 kevapprlle evaeqchgpi tldfainklk tggsrpgsyv lrrspqdfds flltvcvqnp
      421 lgpdykgcli rrsptgtfll vglsrphssl rellatcwdg glhvdgvavt ltscciprpk
      481 eksnlivvqr ghspptsslv qpqsqyqlsq mtfhkipads lewhenlghg sftkiyrgcr
      541 hevvdgeark tevllkvmda khkncmesfl eaaslmsqvs yrhlvllhgv cmagdstmvq
      601 efvhlgaidm ylrkrghlvp aswklqvvkq layalnyled kglphgnvsa rkvllarega
      661 dgsppfikls dpgvspavls lemltdripw vapeclreaq tlsleadkwg fgatvwevfs
      721 gvtmpisald pakklqfyed rqqlpapkwt elalliqqcm ayepvqrpsf ravirdlnsl
      781 issdyellsd ptpgalaprd glwngaqlya cqdptifeer hlkyisqlgk gnfgsvelcr
      841 ydplgdntga lvavkqlqhs gpdqqrdfqr eiqilkalhs dfivkyrgvs ygpgrqslrl
      901 vmeylpsgcl rdflqrhrar ldasrlllys sqickgmeyl gsrrcvhrdl aarnilvese
      961 ahvkiadfgl akllpldkdy yvvrepgqsp ifwyapesls dnifsrqsdv wsfgvvlyel
     1021 ftycdkscsp saeflrmmgc erdvpalcrl lelleegqrl pappacpaev helmklcwap
     1081 spqdrpsfsa lgpqldmlws gsrgcethaf tahpegkhhs lsfs
//
LOCUS       NP_001392789            1071 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001392789
VERSION     NP_001392789.1
DBSOURCE    REFSEQ: accession NM_001405860.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1071)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1071)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1071)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1071)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1071)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1071)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1071)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1957270.1,
                                           SRR14038191.1605589.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1071
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 3"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=117197
     Region          851..971
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..1071
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405860.1:697..3912"
                     /note="isoform 3 is encoded by transcript variant 11"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankies
      481 vsqplenhga piighisesl stkscgalrp vngvintlqp vladhipgds sdaeeqlhkk
      541 qrlnlvssss dgtcvaartr pvlsckkrrl vrpnsivpls kkvhrnstir pgcdvnpsca
      601 lcgsgsintm ppeihyeapl lerlsqldsc vhpvlafpdd vptslhfqsm lksqwqnkpf
      661 dkikppkkls lkhrapmpgs lpdsarkdrh klvssfltta klshhqtrpd rthrqhlddv
      721 gavpmvervt apkaerllnp pppvhdpnhs kmrlrdhsse rsevlkhhtd mssssylaat
      781 hhpphsplvr qlstssdspa passssqvta stsqqpvrrr rgessfdinn ivipmsvaat
      841 trveklqyke iltpswrevd lqslkgspde eneeiedlsd aafaalhakc eemerarwlw
      901 ttsvppqrrg srsyrssdgr ttpqlgsanp stpqpaspdv ssshslseys hgqsprspis
      961 pelhsapltp vardtprhla sedtrcstpe lgldeqsvqp werrtfplah spqaecedql
     1021 daqeraarct rrtsgsktgr eteaaptspp ivplksrhlv aaataqrpth r
//
LOCUS       NP_001428255            1785 aa            linear   PRI 21-NOV-2025
DEFINITION  BCL-6 corepressor-like protein 1 isoform 1a [Homo sapiens].
ACCESSION   NP_001428255 XP_006724839 XP_054183521
VERSION     NP_001428255.1
DBSOURCE    REFSEQ: accession NM_001441326.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1785)
  AUTHORS   Luo,C., Chen,Z., Meng,L., Tan,C., He,W., Tu,C., Du,J., Lu,G.X.,
            Lin,G., Tan,Y.Q. and Hu,T.Y.
  TITLE     A hemizygous loss-of-function variant in BCORL1 is associated with
            male infertility and oligoasthenoteratozoospermia
  JOURNAL   Clin Genet 106 (1), 27-36 (2024)
   PUBMED   38342987
  REMARK    GeneRIF: A hemizygous loss-of-function variant in BCORL1 is
            associated with male infertility and oligoasthenoteratozoospermia.
REFERENCE   2  (residues 1 to 1785)
  AUTHORS   Kommoss,F.K.F., Chiang,S., Kobel,M., Koelsche,C., Chang,K.T.,
            Irving,J.A., Dickson,B., Thiryayi,S., Rouzbahman,M., Rasty,G., von
            Deimling,A., Lee,C.H. and Turashvili,G.
  TITLE     Endometrial Stromal Sarcomas With BCOR Internal Tandem Duplication
            and Variant BCOR/BCORL1 Rearrangements Resemble High-grade
            Endometrial Stromal Sarcomas With Recurrent CDK4 Pathway
            Alterations and MDM2 Amplifications
  JOURNAL   Am J Surg Pathol 46 (8), 1142-1152 (2022)
   PUBMED   35499168
  REMARK    GeneRIF: Endometrial Stromal Sarcomas With BCOR Internal Tandem
            Duplication and Variant BCOR/BCORL1 Rearrangements Resemble
            High-grade Endometrial Stromal Sarcomas With Recurrent CDK4 Pathway
            Alterations and MDM2 Amplifications.
REFERENCE   3  (residues 1 to 1785)
  AUTHORS   Schaefer,E.J., Wang,H.C., Karp,H.Q., Meyer,C.A., Cejas,P.,
            Gearhart,M.D., Adelman,E.R., Fares,I., Apffel,A., Lim,K., Xie,Y.,
            Gibson,C.J., Schenone,M., Murdock,H.M., Wang,E.S., Gondek,L.P.,
            Carroll,M.P., Vedula,R.S., Winer,E.S., Garcia,J.S., Stone,R.M.,
            Luskin,M.R., Carr,S.A., Long,H.W., Bardwell,V.J., Figueroa,M.E. and
            Lindsley,R.C.
  TITLE     BCOR and BCORL1 Mutations Drive Epigenetic Reprogramming and
            Oncogenic Signaling by Unlinking PRC1.1 from Target Genes
  JOURNAL   Blood Cancer Discov 3 (2), 116-135 (2022)
   PUBMED   35015684
  REMARK    GeneRIF: BCOR and BCORL1 Mutations Drive Epigenetic Reprogramming
            and Oncogenic Signaling by Unlinking PRC1.1 from Target Genes.
REFERENCE   4  (residues 1 to 1785)
  AUTHORS   Gafner,M., Michelson,M., Argilli,E., Yosovich,K., Sherr,E.H.,
            Parks,K.C., England,E.M., Hady-Cohen,R., Leibovitz,Z., Lev,D.,
            Michaeli-Yosef,Y., Lerman-Sagie,T. and Blumkin,L.
  TITLE     Major brain malformations: corpus callosum dysgenesis, agenesis of
            septum pellucidum and polymicrogyria in patients with
            BCORL1-related disorders
  JOURNAL   J Hum Genet 67 (2), 95-101 (2022)
   PUBMED   34400773
  REMARK    GeneRIF: Major brain malformations: corpus callosum dysgenesis,
            agenesis of septum pellucidum and polymicrogyria in patients with
            BCORL1-related disorders.
REFERENCE   5  (residues 1 to 1785)
  AUTHORS   Junco,S.E., Wang,R., Gaipa,J.C., Taylor,A.B., Schirf,V.,
            Gearhart,M.D., Bardwell,V.J., Demeler,B., Hart,P.J. and Kim,C.A.
  TITLE     Structure of the polycomb group protein PCGF1 in complex with BCOR
            reveals basis for binding selectivity of PCGF homologs
  JOURNAL   Structure 21 (4), 665-671 (2013)
   PUBMED   23523425
REFERENCE   6  (residues 1 to 1785)
  AUTHORS   Shaffer,J.R., Feingold,E., Wang,X., Lee,M., Tcuenco,K., Weeks,D.E.,
            Weyant,R.J., Crout,R., McNeil,D.W. and Marazita,M.L.
  TITLE     GWAS of dental caries patterns in the permanent dentition
  JOURNAL   J Dent Res 92 (1), 38-44 (2013)
   PUBMED   23064961
REFERENCE   7  (residues 1 to 1785)
  AUTHORS   Gao,Z., Zhang,J., Bonasio,R., Strino,F., Sawai,A., Parisi,F.,
            Kluger,Y. and Reinberg,D.
  TITLE     PCGF homologs, CBX proteins, and RYBP define functionally distinct
            PRC1 family complexes
  JOURNAL   Mol Cell 45 (3), 344-356 (2012)
   PUBMED   22325352
REFERENCE   8  (residues 1 to 1785)
  AUTHORS   Li,M., Collins,R., Jiao,Y., Ouillette,P., Bixby,D., Erba,H.,
            Vogelstein,B., Kinzler,K.W., Papadopoulos,N. and Malek,S.N.
  TITLE     Somatic mutations in the transcriptional corepressor gene BCORL1 in
            adult acute myelogenous leukemia
  JOURNAL   Blood 118 (22), 5914-5917 (2011)
   PUBMED   21989985
  REMARK    GeneRIF: BCORL1 by genetic criteria is a novel candidate tumor
            suppressor gene, joining the growing list of genes recurrently
            mutated in acute myelogenous leukemia.
REFERENCE   9  (residues 1 to 1785)
  AUTHORS   Pagan,J.K., Arnold,J., Hanchard,K.J., Kumar,R., Bruno,T.,
            Jones,M.J., Richard,D.J., Forrest,A., Spurdle,A., Verdin,E.,
            Crossley,M., Fanciulli,M., Chenevix-Trench,G., Young,D.B. and
            Khanna,K.K.
  TITLE     A novel corepressor, BCoR-L1, represses transcription through an
            interaction with CtBP
  JOURNAL   J Biol Chem 282 (20), 15248-15257 (2007)
   PUBMED   17379597
REFERENCE   10 (residues 1 to 1785)
  AUTHORS   Lose,F., Arnold,J., Young,D.B., Brown,C.J., Mann,G.J., Pupo,G.M.,
            Khanna,K.K., Chenevix-Trench,G. and Spurdle,A.B.
  CONSRTM   Kathleen Cuningham Foundation Consortium for Research into Familial
            Breast Cancer
  TITLE     BCoR-L1 variation and breast cancer
  JOURNAL   Breast Cancer Res 9 (4), R54 (2007)
   PUBMED   17697391
  REMARK    GeneRIF: Dysregulated BCoR-L1 expression is associated with breast
            cancer
            Erratum:[Breast Cancer Res. 2008;10(5):406]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL034405.16, Z82208.1,
            KF459400.1 and AL136450.8.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_006724839.1, XP_054183521.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            corepressor that is found tethered to promoter regions by
            DNA-binding proteins. The encoded protein can interact with several
            different class II histone deacetylases to repress transcription.
            Two transcript variants encoding different isoforms have been found
            for this gene. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3031865.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1785
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.1"
     Protein         1..1785
                     /product="BCL-6 corepressor-like protein 1 isoform 1a"
                     /note="BCoR-like protein 1"
                     /calculated_mol_wt=190431
     Region          65..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          113..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          <198..636
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          343..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          527..550
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          562..646
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          753..781
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          876..901
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          937..977
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1029
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1033
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1107..1293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1312..1487
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1328..1336
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          <1494..>1603
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1496..1527
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1497,1501..1502,1505..1507,1509..1510,1514,1517,
                     1527,1529,1531,1535..1536,1539..1541,1543..1544,1548,1551,
                     1560,1562,1564,1568..1569,1572..1574,1576..1577,1581,1584)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1529..1560
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1529..1558
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1562..1591
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1562..1591
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1595..1623
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          1666..1779
                     /region_name="PUFD_like_1"
                     /note="PCGF Ub-like fold discriminator of BCOR-like 1;
                     cd14260"
                     /db_xref="CDD:271223"
     Region          1668..1785
                     /region_name="PCGF Ub-like fold domain (PUFD), required
                     for the interaction with the KDM2B-SKP1 heterodimeric
                     complex. /evidence=ECO:0000269|PubMed:27568929"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            order(1668,1670..1680,1682,1684,1693..1695,1697,
                     1738..1739,1741,1744,1766,1777,1779)
                     /site_type="other"
                     /note="RAWUL domain interface [polypeptide binding]"
                     /db_xref="CDD:271223"
     CDS             1..1785
                     /gene="BCORL1"
                     /gene_synonym="BCoR-L1; CXorf10; SHUVER"
                     /coded_by="NM_001441326.1:265..5622"
                     /note="isoform 1a is encoded by transcript variant 4"
                     /db_xref="GeneID:63035"
                     /db_xref="HGNC:HGNC:25657"
                     /db_xref="MIM:300688"
ORIGIN      
        1 mistaplysg vhnwtssdri rmcgineerr aplsdeestt gdcqhfgsqe fcvsssfskv
       61 eltavgsgsn argadpdgsa teklghksed kpddpqpkmd yagnvaeaeg llvplsspgd
      121 glklpasdsa easnsradcs wtplntqmsk qvdcspagvk aldsrqgvge kntfilatlg
      181 tgvpvegtlp lvttnfsplp apicppapgs asvphsvpda fqvplsvpap vphsglvpvq
      241 vatsvpapsp plapvpalap appsvptlis dsnplsvsas vlvpvpasap psgpvplsap
      301 apaplsvpvs applaliqap vppsaptlvl apvptpvlap mpastppaap appsvpmptp
      361 tpssgppstp tlipafaptp vpaptpapif tpaptpmpaa tpaaiptsap ipasfslsrv
      421 cfpaaqapam qkvplsfqpg tvltpsqplv yipppscgqp lsvatlpttl gvsstltlpv
      481 lpsylqdrcl pgvlaspelr sypyafsvar pltsdsklvs levnrlpcts psgstttqpa
      541 pdgvpgplad tslvtasakv lptpqpllpa psgssapphp akmpsgteqq tegtsvtfsp
      601 lksppqlere masppecsem pldlssksnr qklplpnqrk tppmpvltpv htsskallst
      661 vlsrsqrttq aaggnvtscl gstsspfvif peivrngdps twvknstali stipgtyvgv
      721 anpvpaslll nkdpnlglnr dprhlpkqep isiidqgepk gtgatcgkkg sqagaegqps
      781 tvkrytpari apglpgcqtk elslwkptgp aniyprcsvn gkptstqvlp vgwspyhqas
      841 llsigissag qltpsqgapi rptsvvsefs gvpslsssea vhglpegqpr pggsfvpeqd
      901 pvtknktcri aakpyeeqvn pvlltlspqt gtlalsvqps ggdirmnqgp eeseshlcsd
      961 stpkmegpqg acglklagdt kpknqvlaty mshelvlatp qnlpkmpelp llphdshpke
     1021 lildvvpssr rgssterpql gsqvdlgrvk mekvdgdvvf nlatcfradg lpvapqrgqa
     1081 evrakagqar vkqesvgvfa cknkwqpddv teslppkkmk cgkekdseeq qlqpqakavv
     1141 rsshrpkcrk lpsdpqestk ksprgasdsg kehngvrgkh khrkptkpes qspgkradsh
     1201 eegslekkak ssfrdfipvv lstrtrsqsg sicssfagma dsdmgsqevf pteeeeevtp
     1261 tpakrrkvrk tqrdtqyrsh haqdksllsq grrhlwrare mpwrteaarq mwdtneeeee
     1321 eeeegllkrk krrrqksrky qtgeylteqe deqrrkgrad lkarkqktss sqslehrlrn
     1381 rnlllpnkvq gisdspngfl pnnleepacl ensekpsgkr kcktkhmatv seeakgkgrw
     1441 sqqktrspks ptpvkptepc tpsksrsass eeasesptar qippearrli vnknagetll
     1501 qraarlgykd vvlyclqkds edvnhrdnag ytalheacsr gwtdilnill ehganvncsa
     1561 qdgtrpvhda vvndnletiw lllsygadpt latysgqtam klassdtmkr flsdhlsdlq
     1621 graegdpgvs wdfysssvle ekdgfacdll hnppgssdqe gddpmeeddf mfelsdkpll
     1681 pcynlqvsvs rgpcnwflfs dvlkrlklss rifqarfphf eittmpkaef yrqvassqll
     1741 tpaerpggld drsppgsset velvryepdl lrllgsevef qscns
//
LOCUS       NP_001425204             320 aa            linear   PRI 21-NOV-2025
DEFINITION  protein GNAS isoform m [Homo sapiens].
ACCESSION   NP_001425204 XP_016883307 XP_054179351
VERSION     NP_001425204.1
DBSOURCE    REFSEQ: accession NM_001438275.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,J., Nie,Q., Cheng,J., Zhong,Y.N., Zhang,T., Zhang,X., Ge,X.,
            Ding,Y., Niu,C., Gao,Y., Wang,K., Gao,M., Wang,X., Chen,W., Yun,C.,
            Ye,C., Xu,J., Shaoyong,W., Zhang,L., Shang,P., Luo,X., Zhang,Z.,
            Zheng,X., Sha,X., Zhang,J., Nie,S., Zhang,X., Ren,F., Liu,H.,
            Dong,E., Yu,X., Ji,L., Pang,Y., Sun,J.P. and Jiang,C.
  TITLE     A microbial amino-acid-conjugated bile acid, tryptophan-cholic
            acid, improves glucose homeostasis via the orphan receptor MRGPRE
  JOURNAL   Cell 188 (17), 4530-4548 (2025)
   PUBMED   40446798
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Crane,J.L., Shamblott,M.J., Axelman,J., Hsu,S., Levine,M.A. and
            Germain-Lee,E.L.
  TITLE     Imprinting status of Galpha(s), NESP55, and XLalphas in cell
            cultures derived from human embryonic germ cells: GNAS imprinting
            in human embryonic germ cells
  JOURNAL   Clin Transl Sci 2 (5), 355-360 (2009)
   PUBMED   20443919
  REMARK    GeneRIF: analysis of the imprinting Status of Galpha(s), NESP55,
            and XLalphas in cell cultures derived from human embryonic germ
            cells
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Bastepe,M.
  TITLE     The GNAS Locus: Quintessential Complex Gene Encoding Gsalpha,
            XLalphas, and other Imprinted Transcripts
  JOURNAL   Curr Genomics 8 (6), 398-414 (2007)
   PUBMED   19412439
  REMARK    GeneRIF: GNAS locus has a highly complex imprinted expression
            pattern, giving rise to transcripts (including non-coding) that are
            maternally, paternally, or biallelically expressed.
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Jakobsen,A.M., Ahlman,H., Kolby,L., Abrahamsson,J.,
            Fischer-Colbrie,R. and Nilsson,O.
  TITLE     NESP55, a novel chromogranin-like peptide, is expressed in
            endocrine tumours of the pancreas and adrenal medulla but not in
            ileal carcinoids
  JOURNAL   Br J Cancer 88 (11), 1746-1754 (2003)
   PUBMED   12771991
  REMARK    GeneRIF: Neuroendocrine secretory protein 55 is found in a subset
            of neuroendocrine tumours showing differentiation towards adrenal
            chromaffin cells and pancreatic islets cells and not in ileal
            carcinoids
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Freson,K., Jaeken,J., Van Helvoirt,M., de Zegher,F.,
            Wittevrongel,C., Thys,C., Hoylaerts,M.F., Vermylen,J. and Van
            Geet,C.
  TITLE     Functional polymorphisms in the paternally expressed XLalphas and
            its cofactor ALEX decrease their mutual interaction and enhance
            receptor-mediated cAMP formation
  JOURNAL   Hum Mol Genet 12 (10), 1121-1130 (2003)
   PUBMED   12719376
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Weiss,U., Ischia,R., Eder,S., Lovisetti-Scamihorn,P., Bauer,R. and
            Fischer-Colbrie,R.
  TITLE     Neuroendocrine secretory protein 55 (NESP55): alternative splicing
            onto transcripts of the GNAS gene and posttranslational processing
            of a maternally expressed protein
  JOURNAL   Neuroendocrinology 71 (3), 177-186 (2000)
   PUBMED   10729789
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Ischia,R., Lovisetti-Scamihorn,P., Hogue-Angeletti,R.,
            Wolkersdorfer,M., Winkler,H. and Fischer-Colbrie,R.
  TITLE     Molecular cloning and characterization of NESP55, a novel
            chromogranin-like precursor of a peptide with 5-HT1B receptor
            antagonist activity
  JOURNAL   J Biol Chem 272 (17), 11657-11662 (1997)
   PUBMED   9111083
REFERENCE   8  (residues 1 to 320)
  AUTHORS   Haldeman-Englert,C.R., Hurst,A.C.E. and Levine,M.A.
  TITLE     Disorders of GNAS Inactivation
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29072892
REFERENCE   9  (residues 1 to 320)
  AUTHORS   Szymczuk,V., Florenzano,P., de Castro,L.F., Collins,M.T. and
            Boyce,A.M.
  TITLE     Fibrous Dysplasia / McCune-Albright Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719192
REFERENCE   10 (residues 1 to 320)
  AUTHORS   Weinstein,L.S., Gejman,P.V., de Mazancourt,P., American,N. and
            Spiegel,A.M.
  TITLE     A heterozygous 4-bp deletion mutation in the Gs alpha gene (GNAS1)
            in a patient with Albright hereditary osteodystrophy
  JOURNAL   Genomics 13 (4), 1319-1321 (1992)
   PUBMED   1505964
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121917.20 and AL109840.24.
            
            On or before Apr 17, 2025 this sequence version replaced
            XP_016883307.1, XP_054179351.1.
            
            Summary: This locus has a highly complex imprinted expression
            pattern. It gives rise to maternally, paternally, and biallelically
            expressed transcripts that are derived from four alternative
            promoters and 5' exons. Some transcripts contain a differentially
            methylated region (DMR) at their 5' exons, and this DMR is commonly
            found in imprinted genes and correlates with transcript expression.
            An antisense transcript is produced from an overlapping locus on
            the opposite strand. One of the transcripts produced from this
            locus, and the antisense transcript, are paternally expressed
            noncoding RNAs, and may regulate imprinting in this region. In
            addition, one of the transcripts contains a second overlapping ORF,
            which encodes a structurally unrelated protein - Alex. Alternative
            splicing of downstream exons is also observed, which results in
            different forms of the stimulatory G-protein alpha subunit, a key
            element of the classical signal transduction pathway linking
            receptor-ligand interactions with the activation of adenylyl
            cyclase and a variety of cellular reponses. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            Mutations in this gene result in pseudohypoparathyroidism type 1a,
            pseudohypoparathyroidism type 1b, Albright hereditary
            osteodystrophy, pseudopseudohypoparathyroidism, McCune-Albright
            syndrome, progressive osseus heteroplasia, polyostotic fibrous
            dysplasia of bone, and some pituitary tumors. [provided by RefSeq,
            Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14478891.487468.1,
                                           SRR7410571.176325.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 19412439
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.32"
     Protein         1..320
                     /product="protein GNAS isoform m"
                     /note="secretogranin VI; G protein subunit alpha S;
                     guanine nucleotide binding protein (G protein), alpha
                     stimulating activity polypeptide 1; guanine nucleotide
                     regulatory protein; adenylate cyclase-stimulating G alpha
                     protein; protein ALEX; extra large alphas protein;
                     alternative gene product encoded by XL-exon"
                     /calculated_mol_wt=37382
     Region          1..314
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Site            order(19,23,27,30,33..34,54,57,98,127,152,160,164)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Site            125..133
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            130
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(131,133,135,146,148,152..154,156,159..160,162..165)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(133,158,161..162,165)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            149..152
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            150..166
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Site            218..221
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(283..294,296..299)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Site            291..293
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..320
                     /gene="GNAS"
                     /gene_synonym="AHO; AIMAH1; C20orf45; GNAS1; GPSA; GSA;
                     GSP; NESP; PITA3; POH; SCG6; SgVI"
                     /coded_by="NM_001438275.1:86..1048"
                     /note="isoform m is encoded by transcript variant 19"
                     /db_xref="GeneID:2778"
                     /db_xref="HGNC:HGNC:4392"
                     /db_xref="MIM:139320"
ORIGIN      
        1 mrilhvngfn gdekatkvqd iknnlkeaie tivaamsnlv ppvelanpen qfrvdyilsv
       61 mnvpdfdfpp efyehakalw edegvracye rsneyqlidc aqyfldkidv ikqadyvpsd
      121 qdllrcrvlt sgifetkfqv dkvnfhmfdv ggqrderrkw iqcfndvtai ifvvasssyn
      181 mvirednqtn rlqealnlfk siwnnrwlrt isvilflnkq dllaekvlag kskiedyfpe
      241 faryttpeda tpepgedprv trakyfirde flristasgd grhycyphft cavdtenirr
      301 vfndcrdiiq rmhlrqyell
//
LOCUS       NP_001400258             207 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 19 [Homo sapiens].
ACCESSION   NP_001400258 XP_016868573
VERSION     NP_001400258.1
DBSOURCE    REFSEQ: accession NM_001413329.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 207)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 207)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 207)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 207)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 207)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC087368.7 and AC009901.6.
            
            On Oct 31, 2022 this sequence version replaced XP_016868573.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.72446.1,
                                           SRR1803617.88839.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..207
                     /product="RNA-binding Raly-like protein isoform 19"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=23401
     Region          115..>160
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     CDS             1..207
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413329.1:98..721"
                     /note="isoform 19 is encoded by transcript variant 51"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtmykskrrh qryinmagep kpyrpkpgnk rplsalysgy vfdydyyrdd fynrlfdyhg
       61 rvppppravi plkrprvavt ttrrgkgvfs mkggsrstas gstgsklksd elqtikkelt
      121 qiktkidsll grlekiekqq kaeaeaqkkq leeslvliqe ecvseiadhs teepaeggpd
      181 adgeemtdgi eedfdedggh elflqik
//
LOCUS       NP_001425162            2062 aa            linear   PRI 21-NOV-2025
DEFINITION  nuclear receptor coactivator 6 isoform 3 [Homo sapiens].
ACCESSION   NP_001425162 XP_047296006 XP_054179227
VERSION     NP_001425162.1
DBSOURCE    REFSEQ: accession NM_001438233.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2062)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2062)
  AUTHORS   Lee,K.G., Hong,B.K., Lee,S., Lee,N., Kim,S.W., Kim,D. and Kim,W.U.
  TITLE     Nuclear receptor coactivator 6 is a critical regulator of NLRP3
            inflammasome activation and gouty arthritis
  JOURNAL   Cell Mol Immunol 21 (3), 227-244 (2024)
   PUBMED   38195836
  REMARK    GeneRIF: Nuclear receptor coactivator 6 is a critical regulator of
            NLRP3 inflammasome activation and gouty arthritis.
REFERENCE   3  (residues 1 to 2062)
  AUTHORS   Fang,Y., Xu,Y., Liao,W., Ji,T., Yu,L., Li,L., Pan,M. and Yang,D.
  TITLE     Multiomics analyses and machine learning of nuclear receptor
            coactivator 6 reveal its essential role in hepatocellular carcinoma
  JOURNAL   Cancer Sci 114 (1), 75-90 (2023)
   PUBMED   36086920
  REMARK    GeneRIF: Multiomics analyses and machine learning of nuclear
            receptor coactivator 6 reveal its essential role in hepatocellular
            carcinoma.
REFERENCE   4  (residues 1 to 2062)
  AUTHORS   Watanabe,N., Kawagoe,J., Sugiyama,A., Takehara,I., Ohta,T. and
            Nagase,S.
  TITLE     Nuclear receptor coactivator-6 is essential for the morphological
            change of human uterine stromal cell decidualization via regulating
            actin fiber reorganization
  JOURNAL   Mol Reprod Dev 89 (4), 165-174 (2022)
   PUBMED   35384116
  REMARK    GeneRIF: Nuclear receptor coactivator-6 is essential for the
            morphological change of human uterine stromal cell decidualization
            via regulating actin fiber reorganization.
REFERENCE   5  (residues 1 to 2062)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 2062)
  AUTHORS   Caira,F., Antonson,P., Pelto-Huikko,M., Treuter,E. and
            Gustafsson,J.A.
  TITLE     Cloning and characterization of RAP250, a novel nuclear receptor
            coactivator
  JOURNAL   J Biol Chem 275 (8), 5308-5317 (2000)
   PUBMED   10681503
REFERENCE   7  (residues 1 to 2062)
  AUTHORS   Lee,S.K., Anzick,S.L., Choi,J.E., Bubendorf,L., Guan,X.Y.,
            Jung,Y.K., Kallioniemi,O.P., Kononen,J., Trent,J.M., Azorsa,D.,
            Jhun,B.H., Cheong,J.H., Lee,Y.C., Meltzer,P.S. and Lee,J.W.
  TITLE     A nuclear factor, ASC-2, as a cancer-amplified transcriptional
            coactivator essential for ligand-dependent transactivation by
            nuclear receptors in vivo
  JOURNAL   J Biol Chem 274 (48), 34283-34293 (1999)
   PUBMED   10567404
REFERENCE   8  (residues 1 to 2062)
  AUTHORS   Guan,X.Y., Xu,J., Anzick,S.L., Zhang,H., Trent,J.M. and
            Meltzer,P.S.
  TITLE     Hybrid selection of transcribed sequences from microdissected DNA:
            isolation of genes within amplified region at 20q11-q13.2 in breast
            cancer
  JOURNAL   Cancer Res 56 (15), 3446-3450 (1996)
   PUBMED   8758910
REFERENCE   9  (residues 1 to 2062)
  AUTHORS   Carney,J.P., McKnight,C., VanEpps,S. and Kelley,M.R.
  TITLE     Random rapid amplification of cDNA ends (RRACE) allows for cloning
            of multiple novel human cDNA fragments containing (CAG)n repeats
  JOURNAL   Gene 155 (2), 289-292 (1995)
   PUBMED   7536696
REFERENCE   10 (residues 1 to 2062)
  AUTHORS   Estey,A., Kemp,M., Allison,S. and Lamb,C.
  TITLE     Evaluation of a patient information booklet
  JOURNAL   J Nurs Staff Dev 9 (6), 278-282 (1993)
   PUBMED   8263591
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049709.18 and AL109824.24.
            
            On or before Apr 16, 2025 this sequence version replaced
            XP_047296006.1, XP_054179227.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            coactivator that can interact with nuclear hormone receptors to
            enhance their transcriptional activator functions. This protein has
            been shown to be involved in the hormone-dependent coactivation of
            several receptors, including prostanoid, retinoid, vitamin D3,
            thyroid hormone, and steroid receptors. Alternatively spliced
            transcript variants encoding different isoforms have been described
            for this gene. [provided by RefSeq, Jun 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3722921.1,
                                           SRR14038197.846709.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2062
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..2062
                     /product="nuclear receptor coactivator 6 isoform 3"
                     /note="amplified in breast cancer-3 protein; activating
                     signal cointegrator-2; nuclear receptor coactivator
                     RAP250; peroxisome proliferator-activated receptor
                     interacting protein; thyroid hormone receptor binding
                     protein; NRC RAP250; PPAR-interacting protein; amplified
                     in breast cancer protein 3; nuclear receptor-activating
                     protein, 250 kDa; cancer-amplified transcriptional
                     coactivator ASC-2"
                     /calculated_mol_wt=218928
     Region          1..1310
                     /region_name="NCOA1-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1..1057
                     /region_name="CREBBP-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1..928
                     /region_name="TBP/GTF2A-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          48..190
                     /region_name="Nucleic_acid_bd"
                     /note="Putative nucleic acid-binding region; pfam13820"
                     /db_xref="CDD:463988"
     Site            95
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          <152..544
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          184..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          281..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          520..>838
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          773..927
                     /region_name="NCOA6IP-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          789..811
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            884
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK, in vitro.
                     /evidence=ECO:0000269|PubMed:11773444; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          887..891
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          899..1278
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1047
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          <1056..1302
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1058
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1096
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1310..1353
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1448..1474
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1491..1495
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1738..1820
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1819
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1822
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1837..1908
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            2017
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     CDS             1..2062
                     /gene="NCOA6"
                     /gene_synonym="AIB3; ASC2; NRC; PRIP; RAP250; TRBP"
                     /coded_by="NM_001438233.1:344..6532"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:23054"
                     /db_xref="HGNC:HGNC:15936"
                     /db_xref="MIM:605299"
ORIGIN      
        1 mvlddlpnle diytslcsst medsemdfds gledddtksd siledstifv afkgniddkd
       61 fkwkldailk nvpnllhmes sklkvqkvep wnsvrvtfni preaaerlri laqsnnqqlr
      121 dlgilsvqie gegainlala qnrsqdvrmn gpmgagnsvr meagfpmasg pgiirmnnpa
      181 tvmippggnv sssmmapgpn pelqprtprp asqsdamdpl lsglhiqqqs hpsgslapph
      241 hpmqpvsvnr qmnpanfpql qqqqqqqqqq qqqqqqqqqq qqqqqlqarp pqqhqqqqpq
      301 girpqftapt qvpvppgwnq lpsgalqppp aqgslgtmta nqgwkkaplp gpmqqqlqar
      361 pslatvqtps hppppypfgs qqasqahtnf pqmsnpgqft apqmkslqgg psrvptplqq
      421 phltnkspas spssfqqgsp assptvnqtq qqmgprppqn nplpqgfqqp vsspgrnpmv
      481 qqgnvppnfm vmqqqppnqg pqslhpglgg mpkrlppgfs agqanpnfmq gqvpsttatt
      541 pgnsgapqlq anqnvqhagg qgagppqnqm qvshgppnmm qpslmgihgn mnnqqagtsg
      601 vpqvnlsnmq gqpqqgppsq lmgmhqqivp sqgqmvqqqg tlnpqnpmil sraqlmpqgq
      661 mmvnppsqnl gpspqrmtpp kqmlsqqgpq mmaphnqmmg pqgqvllqqn pmieqimtnq
      721 mqgnkqqfnt qnqsnvmpgp aqimrgptpn mqgnmvqftg qmsgqmlpqq gpvnnspsqv
      781 mgiqgqvlrp pgpsphmaqq hgdpattann dvslsqmmpd vsiqqtnmvp phvqamqgns
      841 asgnhfsghg msfnapfsga pngnqmscgq npgfpvnkdv tltspllvnl lqsdisaghf
      901 gvnnkqnntn ankpkkkkpp rkkknsqqdl ntpdtrpagl eeadqpplpg eqginldnsg
      961 pklpefsnrp pgypsqpveq rplqqmppql mqhvapppqp pqqqpqpqlp qqqqppppsq
     1021 pqsqqqqqqq qqmmmmlmmq qdpksvrlpv sqnvhpprgp lnpdsqrmpm qqsgsvpvmv
     1081 slqgpasvpp spdkqrmpmp vntplgsnsr kmvyqespqn psssplaema slpeasgsea
     1141 psvpggpnnm pshvvlpqnq lmmtgpkpgp splsatqgat pqqppvnslp sshghhfpnv
     1201 aaptqtsrpk tpnrasprpy ypqtpnnrpp stepseisls perlnasiag lfppqinipl
     1261 pprpnlnrgf dqqglnpttl kaigqapsnl tmnpsnfatp qthkldsvvv nsgkqsnsga
     1321 tkraspsnsr rsspgssrkt tpspgrqnsk apkltlasqt naallqnvel prnvlvsptp
     1381 lanppvpgsf pnnsglnpqn stvsvaavgg vvednkesln vpqdsdcqns qsrkeqvnie
     1441 lkavpaqevk mvvpedqskk dgqpsdpnkl psveenknlv spamreapts lsqlldnsga
     1501 pnvtikppgl tdlevtppvv sgedlkkasv iptlqdlsss kepsnslnlp hsnelcsslv
     1561 hpelsevssn vapsippvms rpvssssist plppnqitvf vtsnpittsa ntsaalpthl
     1621 qsalmstvvt mpnagskvmv segqsaaqsn arpqfitpvf insssiiqvm kgsqpstipa
     1681 aplttnsglm ppsvavvgpl hipqnikfss apvppnalss spapniqtgr plvlssratp
     1741 vqlpsppcts spvvpshppv qqvkelnpde aspqvntsad qntlpssqst tmvsplltns
     1801 pgssgnrrsp vssskgkgkv dkigqilltk ackkvtgsle kgeeqygadg etegqgldtt
     1861 apglmgteql steldsktpt ppaptllkmt sspvgpgtas agpslpggal ptsvrsivtt
     1921 lvpselisav pttksnhggi aseslagglv eekvgshpel lpsiapsqnl vsketsttal
     1981 qasvarpele vnaaivsgqs epkeiveksk ipgrrnsrte eptvasesve nghrkrssrp
     2041 asassstkdi tsavqskrrk sk
//
LOCUS       NP_001425736            1044 aa            linear   PRI 21-NOV-2025
DEFINITION  NHS-like protein 2 isoform 4 [Homo sapiens].
ACCESSION   NP_001425736 XP_047298026 XP_054182941
VERSION     NP_001425736.1
DBSOURCE    REFSEQ: accession NM_001438807.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1044)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1044)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1044)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL929401.8 and BX119917.9.
            
            On or before Apr 24, 2025 this sequence version replaced
            XP_047298026.1, XP_054182941.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3670087.1,
                                           SRR14372079.2154359.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467145, SAMEA2467147
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1044
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..1044
                     /product="NHS-like protein 2 isoform 4"
                     /note="NHS-like protein 2; TPT1-like protein"
                     /calculated_mol_wt=112721
     Region          <358..574
                     /region_name="NHS"
                     /note="NHS-like; pfam15273"
                     /db_xref="CDD:464606"
     Region          <540..774
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1044
                     /gene="NHSL2"
                     /coded_by="NM_001438807.1:244..3378"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:340527"
                     /db_xref="HGNC:HGNC:33737"
                     /db_xref="MIM:301093"
ORIGIN      
        1 mpfyrrtvvp qrlcprnppq qlaelrdvsh laalsllrql adlcghslal ledleghlla
       61 lgrrtdslyr rtvrlrrrlp crllgpeede eelgashwsn ltrsqrarep vdaihtghsn
      121 spagsvahst tsdirpshsv pegvhgrvav gqdarfpslt spvlrtpsse pdephqarsg
      181 pnppgmesmg mvysvpsscn gptestfsts wkgdaftymt psatsqsnqv nengknpscg
      241 nswvslnkvp plvpkeaatl lvardnpagc sgsagyperl iqqrhmperp skiglltsgt
      301 srletgpgga srfrerslsv ptdsgttdvd ydeeqkanea calpfastss egsnsadnia
      361 slsaqqeaqh rrqrsksisl rkakkkpspp trsvslvkde pgllpeggsa lpkdqrpksl
      421 clslehqghh sshpdaqghp aipnhkdpes tqfshhwylt dwksgdtyqs lsssstatgt
      481 tviectqvqg sseslaspst srattpsqls ieveareiss pgrppglmsp ssgyssqset
      541 ptptvsmslt lghlpppsss vrvrpvvper ksslpptspm ekfpksrlsf dlpltsspnl
      601 dlsgmsisir sktkvsrhhs etnfgvklaq ktnpnqpimp mvtqsdlrsv rlrsvsksep
      661 eddiespeya eepraeevft lperktkppv aekppvarrp pslvhkppsv peeyaltspt
      721 lampprssiq harplpqdsy tvvrkpkpss fpdgrspges tapsslvftp fasssdaffs
      781 gtqqppqgsv edegpkvrvl perislqsqe eaekkkgkip ppvpkkpsvl ylpltsptaq
      841 meayvaeprl plspiitlee dtkcpatgdd lqslgqrvts tpqadserea splgssvepg
      901 teekslisdk taewiaeddd dvfvasrtte dlftvihrsk rkllgwkepg eafvggrtss
      961 hspikntaes pisestatag sgssanldag rnddfkallq kkgskatprs rpsaaellkt
     1021 tnplarriia qfskdyettd npst
//
LOCUS       NP_001392788            1071 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001392788 XP_047291752
VERSION     NP_001392788.1
DBSOURCE    REFSEQ: accession NM_001405859.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1071)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1071)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1071)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1071)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1071)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1071)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1071)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            On May 5, 2022 this sequence version replaced XP_047291752.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.316128.1,
                                           SRR14038197.1049518.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1071
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 3"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=117197
     Region          851..971
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..1071
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405859.1:251..3466"
                     /note="isoform 3 is encoded by transcript variant 10"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankies
      481 vsqplenhga piighisesl stkscgalrp vngvintlqp vladhipgds sdaeeqlhkk
      541 qrlnlvssss dgtcvaartr pvlsckkrrl vrpnsivpls kkvhrnstir pgcdvnpsca
      601 lcgsgsintm ppeihyeapl lerlsqldsc vhpvlafpdd vptslhfqsm lksqwqnkpf
      661 dkikppkkls lkhrapmpgs lpdsarkdrh klvssfltta klshhqtrpd rthrqhlddv
      721 gavpmvervt apkaerllnp pppvhdpnhs kmrlrdhsse rsevlkhhtd mssssylaat
      781 hhpphsplvr qlstssdspa passssqvta stsqqpvrrr rgessfdinn ivipmsvaat
      841 trveklqyke iltpswrevd lqslkgspde eneeiedlsd aafaalhakc eemerarwlw
      901 ttsvppqrrg srsyrssdgr ttpqlgsanp stpqpaspdv ssshslseys hgqsprspis
      961 pelhsapltp vardtprhla sedtrcstpe lgldeqsvqp werrtfplah spqaecedql
     1021 daqeraarct rrtsgsktgr eteaaptspp ivplksrhlv aaataqrpth r
//
LOCUS       NP_001424822             526 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol-3-phosphatase SAC1 isoform 2 [Homo sapiens].
ACCESSION   NP_001424822 XP_011531802 XP_054201694
VERSION     NP_001424822.1
DBSOURCE    REFSEQ: accession NM_001437893.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Popescu,M.A., Patriche,D., Dobrica,M.O., Pantazica,A.M., Flintoaca
            Alexandru,P.R., Rouille,Y., Popescu,C.I. and Branza-Nichita,N.
  TITLE     Sac1 phosphatidylinositol 4-phosphate phosphatase is a novel host
            cell factor regulating hepatitis B virus particles assembly and
            release
  JOURNAL   FEBS J 289 (23), 7486-7499 (2022)
   PUBMED   35816160
  REMARK    GeneRIF: Sac1 phosphatidylinositol 4-phosphate phosphatase is a
            novel host cell factor regulating hepatitis B virus particles
            assembly and release.
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Loughran,G., Chou,M.Y., Ivanov,I.P., Jungreis,I., Kellis,M.,
            Kiran,A.M., Baranov,P.V. and Atkins,J.F.
  TITLE     Evidence of efficient stop codon readthrough in four mammalian
            genes
  JOURNAL   Nucleic Acids Res 42 (14), 8928-8938 (2014)
   PUBMED   25013167
REFERENCE   6  (residues 1 to 526)
  AUTHORS   Liu,Y., Boukhelifa,M., Tribble,E., Morin-Kensicki,E., Uetrecht,A.,
            Bear,J.E. and Bankaitis,V.A.
  TITLE     The Sac1 phosphoinositide phosphatase regulates Golgi membrane
            morphology and mitotic spindle organization in mammals
  JOURNAL   Mol Biol Cell 19 (7), 3080-3096 (2008)
   PUBMED   18480408
  REMARK    GeneRIF: Sac1 executes an essential household function in mammals
            that involves organization of both Golgi membranes and mitotic
            spindles
REFERENCE   7  (residues 1 to 526)
  AUTHORS   Rohde,H.M., Cheong,F.Y., Konrad,G., Paiha,K., Mayinger,P. and
            Boehmelt,G.
  TITLE     The human phosphatidylinositol phosphatase SAC1 interacts with the
            coatomer I complex
  JOURNAL   J Biol Chem 278 (52), 52689-52699 (2003)
   PUBMED   14527956
  REMARK    GeneRIF: the enzymatic function of hSAC1 provides a switch for
            accessibility of the COPI interaction motif
REFERENCE   8  (residues 1 to 526)
  AUTHORS   Kiss,H., Kedra,D., Kiss,C., Kost-Alimova,M., Yang,Y., Klein,G.,
            Imreh,S. and Dumanski,J.P.
  TITLE     The LZTFL1 gene is a part of a transcriptional map covering 250 kb
            within the common eliminated region 1 (C3CER1) in 3p21.3
  JOURNAL   Genomics 73 (1), 10-19 (2001)
   PUBMED   11352561
REFERENCE   9  (residues 1 to 526)
  AUTHORS   Nemoto,Y., Kearns,B.G., Wenk,M.R., Chen,H., Mori,K., Alb,J.G. Jr.,
            De Camilli,P. and Bankaitis,V.A.
  TITLE     Functional characterization of a mammalian Sac1 and mutants
            exhibiting substrate-specific defects in phosphoinositide
            phosphatase activity
  JOURNAL   J Biol Chem 275 (44), 34293-34305 (2000)
   PUBMED   10887188
REFERENCE   10 (residues 1 to 526)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098476.2.
            
            On or before Apr 11, 2025 this sequence version replaced
            XP_011531802.1, XP_054201694.1.
            
            Summary: This gene encodes an integral membrane protein, which is
            localized to the endoplasmic reticulum, and functions as a
            phosphoinositide phosphatase that hydrolyzes phosphatidylinositol
            3-phosphate, phosphatidylinositol 4-phosphate, and
            phosphatidylinositol 3,5-bisphosphate. Deletion of this gene in
            mouse results in preimplantation lethality. Other studies suggest
            that this gene is also involved in the organization of golgi
            membranes and mitotic spindles. Alternatively spliced transcript
            variants have been found for this gene. A C-terminally extended
            isoform is also predicted to be produced by the use of an
            alternative in-frame, downstream translation termination codon via
            a stop codon readthrough mechanism.[provided by RefSeq, Dec 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3278854.1,
                                           SRR11853567.20754.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..526
                     /product="phosphatidylinositol-3-phosphatase SAC1 isoform
                     2"
                     /EC_number="3.1.3.64"
                     /note="suppressor of actin 1; phosphatidylinositide
                     phosphatase SAC1; suppressor of actin mutations 1-like
                     protein; SAC1 suppressor of actin mutations 1 like;
                     phosphatidylinositol-4-phosphate phosphatase;
                     phosphatidylinositol-3-phosphatase SAC1"
                     /calculated_mol_wt=60722
     Region          <61..452
                     /region_name="COG5329"
                     /note="Phosphoinositide polyphosphatase (Sac family)
                     [Signal transduction mechanisms]"
                     /db_xref="CDD:227637"
     CDS             1..526
                     /gene="SACM1L"
                     /gene_synonym="SAC1"
                     /coded_by="NM_001437893.1:166..1746"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:22908"
                     /db_xref="HGNC:HGNC:17059"
                     /db_xref="MIM:606569"
ORIGIN      
        1 mwklvmmeqm tylpltvcpq rlplqsrkmf llqlsqdqyl vywaqsiwwq lqdnktflam
       61 lnhvlnvdgf yfsttydlth tlqrlsntsp efqemsller adqrfvwngh llrelsaqpe
      121 vhrfalpvlh gfitmhscsi ngkyfdwili srrscfragv ryyvrgidse ghaanfvete
      181 qivhyngska sfvqtrgsip vfwsqrpnlk ykplpqiskv anhmdgfqrh fdsqviiygk
      241 qviinlinqk gsekpleqtf atmvsslgsg mmryiafdfh kecknmrwdr lsilldqvae
      301 mqdelsyflv dsagqvvanq egvfrsncmd cldrtnviqs llarrslqaq lqrlgvlhvg
      361 qkleeqdefe kiyknawadn anacakqyag tgalktdftr tgkrthlgli mdgwnsmiry
      421 yknnfsdgfr qdsidlflgn ysvdeleshs plsvprdwkf lalpiimvva fsmciicllm
      481 agdtwtetla yvlfwgvasi gtffiilyng kdfvdaprlv qkekid
//
LOCUS       NP_001400343             162 aa            linear   PRI 21-NOV-2025
DEFINITION  alpha-tocopherol transfer protein isoform 2 [Homo sapiens].
ACCESSION   NP_001400343 XP_006716531
VERSION     NP_001400343.1
DBSOURCE    REFSEQ: accession NM_001413414.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 162)
  AUTHORS   Jeridi,C., Rachdi,A., Nabli,F., Saied,Z., Zouari,R., Ben
            Mohamed,D., Ben Said,M., Masmoudi,S., Ben Sassi,S. and Amouri,R.
  TITLE     Genetic heterogeneity within a consanguineous family involving TTPA
            and SETX genes
  JOURNAL   J Neurogenet 37 (4), 124-130 (2023)
   PUBMED   38109176
  REMARK    GeneRIF: Genetic heterogeneity within a consanguineous family
            involving TTPA and SETX genes.
REFERENCE   2  (residues 1 to 162)
  AUTHORS   Ulatowski,L., Ghelfi,M., West,R., Atkinson,J., Finno,C.J. and
            Manor,D.
  TITLE     The tocopherol transfer protein mediates vitamin E trafficking
            between cerebellar astrocytes and neurons
  JOURNAL   J Biol Chem 298 (3), 101712 (2022)
   PUBMED   35150738
  REMARK    GeneRIF: The tocopherol transfer protein mediates vitamin E
            trafficking between cerebellar astrocytes and neurons.
REFERENCE   3  (residues 1 to 162)
  AUTHORS   Arai,H. and Kono,N.
  TITLE     alpha-Tocopherol transfer protein (alpha-TTP)
  JOURNAL   Free Radic Biol Med 176, 162-175 (2021)
   PUBMED   34563650
  REMARK    GeneRIF: alpha-Tocopherol transfer protein (alpha-TTP).
            Review article
REFERENCE   4  (residues 1 to 162)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 162)
  AUTHORS   Gotoda,T., Arita,M., Arai,H., Inoue,K., Yokota,T., Fukuo,Y.,
            Yazaki,Y. and Yamada,N.
  TITLE     Adult-onset spinocerebellar dysfunction caused by a mutation in the
            gene for the alpha-tocopherol-transfer protein
  JOURNAL   N Engl J Med 333 (20), 1313-1318 (1995)
   PUBMED   7566022
REFERENCE   6  (residues 1 to 162)
  AUTHORS   Arita,M., Sato,Y., Miyata,A., Tanabe,T., Takahashi,E., Kayden,H.J.,
            Arai,H. and Inoue,K.
  TITLE     Human alpha-tocopherol transfer protein: cDNA cloning, expression
            and chromosomal localization
  JOURNAL   Biochem J 306 (Pt 2) (Pt 2), 437-443 (1995)
   PUBMED   7887897
REFERENCE   7  (residues 1 to 162)
  AUTHORS   Ouahchi,K., Arita,M., Kayden,H., Hentati,F., Ben Hamida,M.,
            Sokol,R., Arai,H., Inoue,K., Mandel,J.L. and Koenig,M.
  TITLE     Ataxia with isolated vitamin E deficiency is caused by mutations in
            the alpha-tocopherol transfer protein
  JOURNAL   Nat Genet 9 (2), 141-145 (1995)
   PUBMED   7719340
REFERENCE   8  (residues 1 to 162)
  AUTHORS   Ben Hamida,C., Doerflinger,N., Belal,S., Linder,C., Reutenauer,L.,
            Dib,C., Gyapay,G., Vignal,A., Le Paslier,D., Cohen,D. et al.
  TITLE     Localization of Friedreich ataxia phenotype with selective vitamin
            E deficiency to chromosome 8q by homozygosity mapping
  JOURNAL   Nat Genet 5 (2), 195-200 (1993)
   PUBMED   8252047
REFERENCE   9  (residues 1 to 162)
  AUTHORS   Schuelke,M.
  TITLE     Ataxia with Vitamin E Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301419
REFERENCE   10 (residues 1 to 162)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC120042.3.
            
            On Nov 1, 2022 this sequence version replaced XP_006716531.1.
            
            Summary: This gene encodes a soluble protein that binds
            alpha-trocopherol, a form of vitamin E, with high selectivity and
            affinity. This protein plays an important role in regulating
            vitamin E levels in the body by transporting vitamin E between
            membrane vesicles and facilitating the secretion of vitamin E from
            hepatocytes to circulating lipoproteins. Mutations in this gene
            cause hereditary vitamin E deficiency (ataxia with vitamin E
            deficiency, AVED) and retinitis pigmentosa. [provided by RefSeq,
            Nov 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853558.23203.1,
                                           SRR14038191.3035610.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..162
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.3"
     Protein         1..162
                     /product="alpha-tocopherol transfer protein isoform 2"
                     /note="tocopherol (alpha) transfer protein (ataxia
                     (Friedreich-like) with vitamin E deficiency); alpha-TTP"
                     /calculated_mol_wt=18423
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49638.1)"
     Region          <40..67
                     /region_name="CRAL_TRIO_N"
                     /note="CRAL/TRIO, N-terminal domain; smart01100"
                     /db_xref="CDD:215024"
     Region          <69..131
                     /region_name="CRAL_TRIO"
                     /note="CRAL/TRIO domain; pfam00650"
                     /db_xref="CDD:459890"
     CDS             1..162
                     /gene="TTPA"
                     /gene_synonym="alphaTTP; ATTP; AVED; TTP1"
                     /coded_by="NM_001413414.1:33..521"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:7274"
                     /db_xref="HGNC:HGNC:12404"
                     /db_xref="MIM:600415"
ORIGIN      
        1 maearsqpsa gpqlnalpdh spllqpglaa lrrrareagv plaplpltds fllrflrard
       61 fdldlawrds fplkvrgihl inepvifhav fsmikpflte kikerihmhg nnykqsllqh
      121 fpdilpleyg geefsmedic qewtnfimks edylssises iq
//
LOCUS       NP_001427346             250 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 8 precursor [Homo
            sapiens].
ACCESSION   NP_001427346
VERSION     NP_001427346.1
DBSOURCE    REFSEQ: accession NM_001440417.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 250)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 250)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 250)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3 and AP004147.3.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.1383644.1,
                                           SRR18074969.3703580.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..250
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     8 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=25325
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..>230
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     CDS             1..250
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440417.1:299..1051"
                     /note="isoform 8 precursor is encoded by transcript
                     variant 19"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk vgaslspppp
      241 aelhpppslp
//
LOCUS       NP_001424561             115 aa            linear   PRI 21-NOV-2025
DEFINITION  coiled-coil domain-containing protein 28B isoform 3 [Homo sapiens].
ACCESSION   NP_001424561 XP_016857797 XP_054194665
VERSION     NP_001424561.1
DBSOURCE    REFSEQ: accession NM_001437632.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Kang,Y., Lehmann,K.S., Long,H., Jefferson,A., Purice,M., Freeman,M.
            and Clark,S.
  TITLE     Structural basis of lipid transfer by a bridge-like lipid-transfer
            protein
  JOURNAL   Nature 642 (8066), 242-249 (2025)
   PUBMED   40269155
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Capitani,N., Onnis,A., Finetti,F., Cassioli,C., Plebani,A.,
            Brunetti,J., Troilo,A., D'Elios,S., Baronio,M., Gazzurelli,L.,
            Della Bella,C., Billadeau,D.D., D'Elios,M.M., Lougaris,V. and
            Baldari,C.T.
  TITLE     A CVID-associated variant in the ciliogenesis protein CCDC28B
            disrupts immune synapse assembly
  JOURNAL   Cell Death Differ 29 (1), 65-81 (2022)
   PUBMED   34294890
  REMARK    GeneRIF: A CVID-associated variant in the ciliogenesis protein
            CCDC28B disrupts immune synapse assembly.
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Novas,R., Cardenas-Rodriguez,M., Lepanto,P., Fabregat,M., Rodao,M.,
            Fariello,M.I., Ramos,M., Davison,C., Casanova,G., Alfaya,L.,
            Lecumberry,F., Gonzalez-Sapienza,G., Irigoin,F. and Badano,J.L.
  TITLE     Kinesin 1 regulates cilia length through an interaction with the
            Bardet-Biedl syndrome related protein CCDC28B
  JOURNAL   Sci Rep 8 (1), 3019 (2018)
   PUBMED   29445114
  REMARK    GeneRIF: these studies demonstrate that kinesin 1 regulates
            ciliogenesis through CCDC28B
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 115)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 115)
  AUTHORS   Cardenas-Rodriguez,M., Irigoin,F., Osborn,D.P., Gascue,C.,
            Katsanis,N., Beales,P.L. and Badano,J.L.
  TITLE     The Bardet-Biedl syndrome-related protein CCDC28B modulates mTORC2
            function and interacts with SIN1 to control cilia length
            independently of the mTOR complex
  JOURNAL   Hum Mol Genet 22 (20), 4031-4042 (2013)
   PUBMED   23727834
  REMARK    GeneRIF: Findings implicate CCDC28B in the regulation of mTORC2,
            and uncover a novel function of SIN1 regulating cilia length that
            is likely independent of mTOR signaling.
REFERENCE   9  (residues 1 to 115)
  AUTHORS   Cardenas-Rodriguez,M., Osborn,D.P., Irigoin,F., Grana,M.,
            Romero,H., Beales,P.L. and Badano,J.L.
  TITLE     Characterization of CCDC28B reveals its role in ciliogenesis and
            provides insight to understand its modifier effect on Bardet-Biedl
            syndrome
  JOURNAL   Hum Genet 132 (1), 91-105 (2013)
   PUBMED   23015189
  REMARK    GeneRIF: reports CCDC28B as a novel protein involved in the process
            of ciliogenesis whilst providing functional insight into the
            cellular basis of its modifier effect in Bardet-Biedl syndrome.
REFERENCE   10 (residues 1 to 115)
  AUTHORS   Badano,J.L., Leitch,C.C., Ansley,S.J., May-Simera,H., Lawson,S.,
            Lewis,R.A., Beales,P.L., Dietz,H.C., Fisher,S. and Katsanis,N.
  TITLE     Dissection of epistasis in oligogenic Bardet-Biedl syndrome
  JOURNAL   Nature 439 (7074), 326-330 (2006)
   PUBMED   16327777
  REMARK    GeneRIF: identification of a novel locus, MGC1203, that contributes
            epistatic alleles to Bardet-Biedl syndrome, a pleiotropic,
            oligogenic disorder; MGC1203 encodes a pericentriolar protein that
            interacts and colocalizes with the BBS proteins
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049795.21.
            
            On or before Apr 7, 2025 this sequence version replaced
            XP_016857797.1, XP_054194665.1.
            
            Summary: The product of this gene localizes to centrosomes and
            basal bodies. The protein colocalizes with several proteins
            associated with Bardet-Biedl syndrome (BBS) and participates in the
            regulation of cilia development. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jul 2014].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.2520330.1,
                                           SRR14038197.625756.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.2"
     Protein         1..115
                     /product="coiled-coil domain-containing protein 28B
                     isoform 3"
                     /note="coiled-coil domain-containing protein 28B; lipid
                     transport auxiliary protein 2B"
                     /calculated_mol_wt=12176
     Region          1..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUN5.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9BUN5.2)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9BUN5.2)"
     Region          86..>110
                     /region_name="CCDC28"
                     /note="Coiled-coil domain-containing protein 28;
                     pfam13270"
                     /db_xref="CDD:463822"
     CDS             1..115
                     /gene="CCDC28B"
                     /gene_synonym="LTAP2B"
                     /coded_by="NM_001437632.1:139..486"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:79140"
                     /db_xref="HGNC:HGNC:28163"
                     /db_xref="MIM:610162"
ORIGIN      
        1 mddkkkkrsp kpclaqpaqa pgtlrrvpvp tshsgslalg lphlpspkqr akfkrvgkek
       61 crpvlagggs gsagtplqhs fltevtdvye meggllnlln dfhsgrlqaf agrpq
//
LOCUS       NP_001412010             329 aa            linear   PRI 21-NOV-2025
DEFINITION  coatomer subunit delta isoform 11 [Homo sapiens].
ACCESSION   NP_001412010 XP_047282855 XP_054224672
VERSION     NP_001412010.1
DBSOURCE    REFSEQ: accession NM_001425081.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   O'Donoghue,L., Comer,S.P., Hiebner,D.W., Schoen,I., von
            Kriegsheim,A. and Smolenski,A.
  TITLE     RhoGAP6 interacts with COPI to regulate protein transport
  JOURNAL   Biochem J 480 (14), 1109-1127 (2023)
   PUBMED   37409526
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Li,W., Liang,J., Outeda,P., Turner,S., Wakimoto,B.T. and Watnick,T.
  TITLE     A genetic screen in Drosophila reveals an unexpected role for the
            KIP1 ubiquitination-promoting complex in male fertility
  JOURNAL   PLoS Genet 16 (12), e1009217 (2020)
   PUBMED   33378371
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Tidwell,T., Deshotel,M., Palumbos,J., Miller,C., Bayrak-Toydemir,P.
            and Carey,J.C.
  TITLE     Novel de novo ARCN1 intronic variant causes rhizomelic short
            stature with microretrognathia and developmental delay
  JOURNAL   Cold Spring Harb Mol Case Stud 6 (6), a005728 (2020)
   PUBMED   33154040
  REMARK    GeneRIF: Novel de novo ARCN1 intronic variant causes rhizomelic
            short stature with microretrognathia and developmental delay.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Schekman,R. and Orci,L.
  TITLE     Coat proteins and vesicle budding
  JOURNAL   Science 271 (5255), 1526-1533 (1996)
   PUBMED   8599108
  REMARK    Review article
REFERENCE   7  (residues 1 to 329)
  AUTHORS   Cukierman,E., Huber,I., Rotman,M. and Cassel,D.
  TITLE     The ARF1 GTPase-activating protein: zinc finger motif and Golgi
            complex localization
  JOURNAL   Science 270 (5244), 1999-2002 (1995)
   PUBMED   8533093
REFERENCE   8  (residues 1 to 329)
  AUTHORS   Radice,P., Pensotti,V., Jones,C., Perry,H., Pierotti,M.A. and
            Tunnacliffe,A.
  TITLE     The human archain gene, ARCN1, has highly conserved homologs in
            rice and Drosophila
  JOURNAL   Genomics 26 (1), 101-106 (1995)
   PUBMED   7782067
REFERENCE   9  (residues 1 to 329)
  AUTHORS   Orcl,L., Palmer,D.J., Amherdt,M. and Rothman,J.E.
  TITLE     Coated vesicle assembly in the Golgi requires only coatomer and ARF
            proteins from the cytosol
  JOURNAL   Nature 364 (6439), 732-734 (1993)
   PUBMED   8355790
REFERENCE   10 (residues 1 to 329)
  AUTHORS   Waters,M.G., Serafini,T. and Rothman,J.E.
  TITLE     'Coatomer': a cytosolic protein complex containing subunits of
            non-clathrin-coated Golgi transport vesicles
  JOURNAL   Nature 349 (6306), 248-251 (1991)
   PUBMED   1898986
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000941.6.
            
            On or before Oct 25, 2023 this sequence version replaced
            XP_047282855.1, XP_054224672.1.
            
            Summary: This gene maps in a region, which include the mixed
            lineage leukemia and Friend leukemia virus integration 1 genes,
            where multiple disease-associated chromosome translocations occur.
            It is an intracellular protein. Archain sequences are well
            conserved among eukaryotes and this protein may play a fundamental
            role in eukaryotic cell biology. It has similarities to heat shock
            proteins and clathrin-associated proteins, and may be involved in
            vesicle structure or trafficking. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2262325.1,
                                           SRR14038193.3775139.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..329
                     /product="coatomer subunit delta isoform 11"
                     /note="coatomer protein delta-COP; coatomer protein
                     complex, subunit delta; archain vesicle transport protein
                     1; coatomer delta subunit; delta-coat protein; COPI coat
                     complex subunit delta"
                     /calculated_mol_wt=36630
     Region          <2..45
                     /region_name="longin-like"
                     /note="Longin-like domains; cl38905"
                     /db_xref="CDD:365781"
     Region          184..>326
                     /region_name="AP_delta-COPI_MHD"
                     /note="Mu homology domain (MHD) of adaptor protein (AP)
                     coat protein I (COPI) delta subunit; cd09254"
                     /db_xref="CDD:271162"
     CDS             1..329
                     /gene="ARCN1"
                     /gene_synonym="COPD; SRMMD; SSMG"
                     /coded_by="NM_001425081.1:140..1129"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:372"
                     /db_xref="HGNC:HGNC:649"
                     /db_xref="MIM:600820"
ORIGIN      
        1 mipeycrale eneisehcfd lifafdeiva lgyrenvnla qirtftemds heekvfravr
       61 etqereakae mrrkakelqq arrdaerqgk kapgfggfgs savsggstaa mitetiietd
      121 kpkvapapar psgpskalkl gakgkevdnf vdklkseget imsssmgkrt seatkmhapp
      181 inmesvhmki eekitltcgr dgglqnmelh gmimlrisdd kygrirlhve nedkkgvqlq
      241 thpnvdkklf taesliglkn peksfpvnsd vgvlkwrlqt teesfiplti ncwpsesgng
      301 cdvnieyelq ednlelndvv itiplplpk
//
LOCUS       NP_001394740            1223 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 8 precursor
            [Homo sapiens].
ACCESSION   NP_001394740
VERSION     NP_001394740.1
DBSOURCE    REFSEQ: accession NM_001407811.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1223)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1223)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1223)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1223)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1223)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1223)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1223)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1223)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1223)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1223)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.119820.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1223
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1223
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 8 precursor"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=133695
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O00411.2)"
                     /calculated_mol_wt=4109
     Region          18..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          95..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          418..690
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          717..736
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          817..1223
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1223
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407811.1:26..3697"
                     /note="isoform 8 precursor is encoded by transcript
                     variant 8"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 msalcwgrga aglkralrpc grpglpgkeg taggvcgprr sssaspqeqd qdrrkdwghv
       61 ellevlqarv rqlqaesvse vvvnrvdvar lpecgsgdgs lqpprkvqmg akdatpvpcg
      121 rwakilekdk rtqqmrmqrl kaklqmpfqs gefkaltrrl qveprllskq magcledctr
      181 qapespweeq larllqeapg klsldveqap sgqhsqaqls gqqqrllaff kcclltdqlp
      241 lahhllvvhh gqrqkrkllt ldmynavmlg warqdagltp dllsyaaalq cmgrqdqdag
      301 tiercleqms qeglklqalf tavllseedr atvlkavhkv kptfslppql pppvntskll
      361 rdvyakdgrv sypklhlplk tlqclfekql hmelasrvcv vsvekptlps kevkharktl
      421 ktlrdqweka lcralretkn rlerevyegr fslypflcll derevvrmll qvlqalpaqg
      481 esfttlarel sartfsrhvv qrqrvsgqvq alqnhyrkyl cllasdaevp epclprqywe
      541 elgapealre qpwplpvqme lgkllaemlv qatqmpcsld kphrssrlvp vlyhvysfrn
      601 vqqigilkph payvqlleka aeptltfeav dvpmlcpplp wtsphsgafl lsptklmrtv
      661 egatqhqell etcpptalhg aldaltqlgn cawrvngrvl dlvlqlfqak gcpqlgvpap
      721 pseapqppea hlphsaapar kaelrrelah cqkvaremhs lraealyrls laqhlrdrvf
      781 wlphnmdfrg rtypcpphfn hlgsdvaral lefaqgrplg phgldwlkih lvnltglkkr
      841 eplrkrlafa eevmddilds adqpltgrkw wmgaeepwqt laccmevana vrasdpaayv
      901 shlpvhqdgs cnglqhyaal grdsvgaasv nlepsdvpqd vysgvaaqve vfrrqdaqrg
      961 mrvaqvlegf itrkvvkqtv mtvvygvtry ggrlqiekrl relsdfpqef vweashylvr
     1021 qvfkslqemf sgtraiqhwl tesarlishm gsvvewvtpl gvpviqpyrl dskvkqiggg
     1081 iqsitythng disrkpntrk qkngfppnfi hsldsshmml talhcyrspp lchrkgltfv
     1141 svhdcywtha advsvmnqvc reqfvrlhse pilqdlsrfl vkrfcsepqk ileasqlket
     1201 lqavpkpgaf dleqvkrsty ffs
//
LOCUS       NP_001425614             951 aa            linear   PRI 21-NOV-2025
DEFINITION  splicing regulator ARVCF isoform 4 [Homo sapiens].
ACCESSION   NP_001425614 XP_047297326 XP_054181604
VERSION     NP_001425614.1
DBSOURCE    REFSEQ: accession NM_001438685.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 951)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 951)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 951)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 951)
  AUTHORS   Suzuki,N., Idogawa,M., Tange,S., Ohashi,T., Sasaki,Y., Nakase,H.
            and Tokino,T.
  TITLE     p53-induced ARVCF modulates the splicing landscape and supports the
            tumor suppressive function of p53
  JOURNAL   Oncogene 39 (10), 2202-2211 (2020)
   PUBMED   31827232
  REMARK    GeneRIF: p53-induced ARVCF modulates the splicing landscape and
            supports the tumor suppressive function of p53.
REFERENCE   5  (residues 1 to 951)
  AUTHORS   Zhang,D., Tang,N., Liu,Y. and Wang,E.H.
  TITLE     ARVCF expression is significantly correlated with the malignant
            phenotype of non-small cell lung cancer
  JOURNAL   Mol Carcinog 54 Suppl 1, E185-E191 (2015)
   PUBMED   25683624
  REMARK    GeneRIF: observed ARVCF-dependent changes in small GTPase (mainly
            RhoA) activity in lung cancer cells. We confirmed that ARVCF plays
            an important role in the malignant phenotype
REFERENCE   6  (residues 1 to 951)
  AUTHORS   Mariner,D.J., Wang,J. and Reynolds,A.B.
  TITLE     ARVCF localizes to the nucleus and adherens junction and is
            mutually exclusive with p120(ctn) in E-cadherin complexes
  JOURNAL   J Cell Sci 113 (Pt 8), 1481-1490 (2000)
   PUBMED   10725230
REFERENCE   7  (residues 1 to 951)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   8  (residues 1 to 951)
  AUTHORS   Sirotkin,H., Morrow,B., Saint-Jore,B., Puech,A., Das Gupta,R.,
            Patanjali,S.R., Skoultchi,A., Weissman,S.M. and Kucherlapati,R.
  TITLE     Identification, characterization, and precise mapping of a human
            gene encoding a novel membrane-spanning protein from the 22q11
            region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 42 (2), 245-251 (1997)
   PUBMED   9192844
REFERENCE   9  (residues 1 to 951)
  AUTHORS   Sirotkin,H., O'Donnell,H., DasGupta,R., Halford,S., St Jore,B.,
            Puech,A., Parimoo,S., Morrow,B., Skoultchi,A., Weissman,S.M.,
            Scambler,P. and Kucherlapati,R.
  TITLE     Identification of a new human catenin gene family member (ARVCF)
            from the region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 41 (1), 75-83 (1997)
   PUBMED   9126485
REFERENCE   10 (residues 1 to 951)
  AUTHORS   Lindsay,E.A., Goldberg,R., Jurecic,V., Morrow,B., Carlson,C.,
            Kucherlapati,R.S., Shprintzen,R.J. and Baldini,A.
  TITLE     Velo-cardio-facial syndrome: frequency and extent of 22q11
            deletions
  JOURNAL   Am J Med Genet 57 (3), 514-522 (1995)
   PUBMED   7677167
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005663.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047297326.1, XP_054181604.1.
            
            Summary: Armadillo Repeat gene deleted in Velo-Cardio-Facial
            syndrome (ARVCF) is a member of the catenin family. This family
            plays an important role in the formation of adherens junction
            complexes, which are thought to facilitate communication between
            the inside and outside environments of a cell. The ARVCF gene was
            isolated in the search for the genetic defect responsible for the
            autosomal dominant Velo-Cardio-Facial syndrome (VCFS), a relatively
            common human disorder with phenotypic features including cleft
            palate, conotruncal heart defects and facial dysmorphology. The
            ARVCF gene encodes a protein containing two motifs, a coiled coil
            domain in the N-terminus and a 10 armadillo repeat sequence in the
            midregion. Since these sequences can facilitate protein-protein
            interactions ARVCF is thought to function in a protein complex. In
            addition, ARVCF contains a predicted nuclear-targeting sequence
            suggesting that it may have a function as a nuclear protein.
            [provided by RefSeq, Jun 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2638939.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..951
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..951
                     /product="splicing regulator ARVCF isoform 4"
                     /note="armadillo repeat protein deleted in
                     velo-cardio-facial syndrome; armadillo repeat gene deleted
                     in velocardiofacial syndrome; splicing regulator ARVCF"
                     /calculated_mol_wt=103142
     Region          95..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            170
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P98203; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          186..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          266..290
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          348..387
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          360..385
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(376,380,384,418,422,426,461,466,470)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          389..428
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          390..429
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          393..429
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          432..473
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          433..467
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          436..471
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          468..508
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          478..529
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          526..565
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          590..614
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          635..675
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          645..681
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          645..681
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          688..727
                     /region_name="ARM 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          691..726
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          691..725
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          728..770
                     /region_name="ARM 9"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          732..777
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          765..951
                     /region_name="Required for interaction with RNA-binding
                     proteins DDX5, HNRNPH2 and SRSF1 and with mRNAs.
                     /evidence=ECO:0000269|PubMed:24644279"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          783..815
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          843..951
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            853
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            860
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            861
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            904
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     CDS             1..951
                     /gene="ARVCF"
                     /coded_by="NM_001438685.1:308..3163"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:421"
                     /db_xref="HGNC:HGNC:728"
                     /db_xref="MIM:602269"
ORIGIN      
        1 medcnvhsaa silasvkeqe arferltral eqerrhvalq leraqqpgmv sggmgsgqpl
       61 pmawqqlvlq eqspgsqasl atmpeapdvl eetvtveedp gtptshvsiv tsedgttrrt
      121 etkvtktvkt vttrtvrqvp vgpdglplld ggpplgpfad galdrhfllr gggpvatlsr
      181 aylssgggfp egpeprdsps ygslsrglgm rppragplgp gpgdgcftlp ghreafpvgp
      241 epgppggrsl perfqaepyg leddtrslaa ddeggpelep dygtatrrrp ecgrglhtra
      301 yedtaddgge laderpafpm vtaplaqper gsmgsldrlv rrspsvdsar keprwrdpel
      361 pevlamlrhp vdpvkanaaa ylqhlcfene gvkrrvrqlr glpllvalld hpraevrrra
      421 cgalrnlsyg rdtdnkaair dcggvpalvr llraardnev relvtgtlwn lssyeplkmv
      481 iidhglqtlt hevivphsgw erepnedskp rdaewttvfk ntsgclrnvs sdgaearrrl
      541 receglvdal lhalqsavgr kdtdnksven cvcimrnlsy hvhkevpgad ryqeaepgpl
      601 gsavgsqrrr rddascfggk kdgemdrnfd tldlpkrtea akgfellyqp evvrlylsll
      661 tesrnfntle aaagalqnls agnwmwatyi ratvrkergl pvlvellqse tdkvvravai
      721 alrnlsldrr nkdligsyam aelvrnvrna qapprpgacl eedtvvavln tiheivsdsl
      781 dnarsllqar gvpalvalva ssqsvreaka ashvlqtvws ykelrgtlqk dgwtkarfqs
      841 aaatakgpkg alspggfdds tlplvdksle gektgsrdvi pmdalgpdgy stvdrrerrp
      901 rgassageas ekeplkldps rkapppgpsr pavrlvdavg dakpqpvdsw v
//
LOCUS       NP_001428157             365 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 11 [Homo sapiens].
ACCESSION   NP_001428157
VERSION     NP_001428157.1
DBSOURCE    REFSEQ: accession NM_001441228.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 365)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 365)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 365)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 365)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 365)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.325091.1,
                                           SRR14038196.1777962.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..365
                     /product="calcium uptake protein 1, mitochondrial isoform
                     11"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=41924
     Region          111..330
                     /region_name="EFh_MICU1"
                     /note="EF-hand, calcium binding motif, found in calcium
                     uptake protein 1, mitochondrial (MICU1) and similar
                     proteins; cd16173"
                     /db_xref="CDD:320081"
     Region          111..140
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Site            order(113,265,268,271..272,274,292)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:320081"
     Site            order(120,122,124,131,310,312,314,321)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320081"
     Region          166..196
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          264..293
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          301..330
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     CDS             1..365
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001441228.1:74..1171"
                     /note="isoform 11 is encoded by transcript variant 15"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 meyenriray stpdkifryf atlkvisepg eaevfmtped fvrsitpnek qpehlgldqy
       61 iikrfdgkki sqerekfade gsifytlgec glisfsdyif lttvlstpqr nfeiafkmfd
      121 lngdgevdme efeqvqsiir sqtsmgmrhr drpttgntlk sglcsaltty ffgadlkgkl
      181 tiknflefqr klqhdvlkle ferhdpvdgr iterqfggml laysgvqskk ltamqrqlkk
      241 hfkegkgltf qevenfftfl knindvdtal sfyhmagasl dkvtmqqvar tvakvelsdh
      301 vcdvvfalfd cdgngelsnk efvsimkqrl mrglekpkdm gftrlmqamw kcaqetawdf
      361 alpkq
//
LOCUS       NP_001393916             583 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform G [Homo sapiens].
ACCESSION   NP_001393916
VERSION     NP_001393916.1
DBSOURCE    REFSEQ: accession NM_001406987.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 583)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 583)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 583)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 583)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 583)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 583)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 583)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 583)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1665948.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..583
                     /product="lamin isoform G"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=64636
     Region          48..305
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          353..460
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     CDS             1..583
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406987.1:122..1873"
                     /note="isoform G is encoded by transcript variant 14"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 mqpllclgnl edarertgtl laqhpawgrt rakpgsplnt kkegdliaaq arlkdleall
       61 nskeaalsta lsekrtlege lhdlrgqvak leaalgeakk qlqdemlrrv daenrlqtmk
      121 eeldfqkniy seelretkrr hetrlveidn gkqrefesrl adalqelraq hedqveqykk
      181 elektysakl dnarqsaern snlvgaahee lqqsririds lsaqlsqlqk qlaakeaklr
      241 dledslarer dtsrrllaek eremaemrar mqqqldeyqe lldiklaldm eihayrklle
      301 geeerlrlsp sptsqrsrgr asshssqtqg ggsvtkkrkl estesrssfs qhartsgrva
      361 veevdeegkf vrlrnksned qsmgnwqikr qngddpllty rfppkftlka gqvvtiwaag
      421 agathspptd lvwkaqntwg cgnslrtali nstgeevamr klvrsvtvve ddededgddl
      481 lhhhhgshcs ssgdpaeynl rsrtvlcgtc gqpadkasas gsgaqvggpi ssgssassvt
      541 vtrsyrsvgg sgggsfgdnl vtrsyllgns sprtqspqnc sim
//
LOCUS       NP_001393986             550 aa            linear   PRI 21-NOV-2025
DEFINITION  merlin isoform 13 [Homo sapiens].
ACCESSION   NP_001393986
VERSION     NP_001393986.1
DBSOURCE    REFSEQ: accession NM_001407057.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 550)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 550)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 550)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 550)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 550)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005529.7 and AC004882.3.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.538206.1,
                                           SRR14038197.1083705.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145313, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..550
                     /product="merlin isoform 13"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=64391
     Region          23..222
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          216..267
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          262..>322
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          301..420
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          473..550
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..550
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_001407057.1:367..2019"
                     /note="isoform 13 is encoded by transcript variant 19"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 magaiasrms fsslkrkqpk tftvrivtmd aemefncemk wkgkdlfdlv crtlglretw
       61 ffglqytikd tvawlkmdkk vldhdvskee pvtfhflakf ypenaeeelv qeitqhlffl
      121 qvkkqildek iycppeasvl lasyavqaky gdydpsvhkr gflaqeellp krvinlyqmt
      181 pemweerita wyaehrgrar deaemeylki aqdlemygvn yfairftikp ldkkidvfkf
      241 nssklrvnkl ilqlcignhd lfmrrrkads levqqmkaqa reekarkqme rqrlarekqm
      301 reeaertrde lerrllqmke eatmanealm rseetadlla ekaqiteeea kllaqkaaea
      361 eqemqrikat airteeekrl meqkvleaev lalkmaeese rrakeadqlk qdlqeareae
      421 rrakqkllei atkptyppmn pipaplppdi psfnligdsl sfdfkdtdmk rlsmeiekek
      481 veymekskhl qeqlnelkte iealklkere taldilhnen sdrggsskhn tikkltlqsa
      541 ksrvaffeel
//
LOCUS       NP_001427237             350 aa            linear   PRI 21-NOV-2025
DEFINITION  G1/S-specific cyclin-E1 isoform 9 [Homo sapiens].
ACCESSION   NP_001427237
VERSION     NP_001427237.1
DBSOURCE    REFSEQ: accession NM_001440308.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Lee,S.J., Jeon,S.H., Cho,S., Kim,C.M., Yoo,J.K., Oh,S.H., Kim,J.H.,
            Yang,Y.D. and Kim,J.K.
  TITLE     hsa-miR-CHA2, a novel microRNA, exhibits anticancer effects by
            suppressing cyclin E1 in human non-small cell lung cancer cells
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (6), 167250 (2024)
   PUBMED   38763409
  REMARK    GeneRIF: hsa-miR-CHA2, a novel microRNA, exhibits anticancer
            effects by suppressing cyclin E1 in human non-small cell lung
            cancer cells.
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Rustgi,N., Wu,S., Samec,T., Walker,P., Xiu,J., Lou,E., Goel,S.,
            Saeed,A. and Moy,R.H.
  TITLE     Molecular Landscape and Clinical Implication of CCNE1-amplified
            Esophagogastric Cancer
  JOURNAL   Cancer Res Commun 4 (6), 1399-1409 (2024)
   PUBMED   38717153
  REMARK    GeneRIF: Molecular Landscape and Clinical Implication of
            CCNE1-amplified Esophagogastric Cancer.
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Audrey,A., Kok,Y.P., Yu,S., de Haan,L., van de Kooij,B., van den
            Tempel,N., Chen,M., de Boer,H.R., van der Vegt,B. and van
            Vugt,M.A.T.M.
  TITLE     RAD52-dependent mitotic DNA synthesis is required for genome
            stability in Cyclin E1-overexpressing cells
  JOURNAL   Cell Rep 43 (4), 114116 (2024)
   PUBMED   38625790
  REMARK    GeneRIF: RAD52-dependent mitotic DNA synthesis is required for
            genome stability in Cyclin E1-overexpressing cells.
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Mumberg,D., Wick,M., Burger,C., Haas,K., Funk,M. and Muller,R.
  TITLE     Cyclin ET, a new splice variant of human cyclin E with a unique
            expression pattern during cell cycle progression and
            differentiation
  JOURNAL   Nucleic Acids Res 25 (11), 2098-2105 (1997)
   PUBMED   9153308
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Sewing,A., Ronicke,V., Burger,C., Funk,M. and Muller,R.
  TITLE     Alternative splicing of human cyclin E
  JOURNAL   J Cell Sci 107 (Pt 2), 581-588 (1994)
   PUBMED   8207080
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Koff,A., Giordano,A., Desai,D., Yamashita,K., Harper,J.W.,
            Elledge,S., Nishimoto,T., Morgan,D.O., Franza,B.R. and Roberts,J.M.
  TITLE     Formation and activation of a cyclin E-cdk2 complex during the G1
            phase of the human cell cycle
  JOURNAL   Science 257 (5077), 1689-1694 (1992)
   PUBMED   1388288
REFERENCE   8  (residues 1 to 350)
  AUTHORS   Hinds,P.W., Mittnacht,S., Dulic,V., Arnold,A., Reed,S.I. and
            Weinberg,R.A.
  TITLE     Regulation of retinoblastoma protein functions by ectopic
            expression of human cyclins
  JOURNAL   Cell 70 (6), 993-1006 (1992)
   PUBMED   1388095
REFERENCE   9  (residues 1 to 350)
  AUTHORS   Koff,A., Cross,F., Fisher,A., Schumacher,J., Leguellec,K.,
            Philippe,M. and Roberts,J.M.
  TITLE     Human cyclin E, a new cyclin that interacts with two members of the
            CDC2 gene family
  JOURNAL   Cell 66 (6), 1217-1228 (1991)
   PUBMED   1833068
REFERENCE   10 (residues 1 to 350)
  AUTHORS   Lew,D.J., Dulic,V. and Reed,S.I.
  TITLE     Isolation of three novel human cyclins by rescue of G1 cyclin (Cln)
            function in yeast
  JOURNAL   Cell 66 (6), 1197-1206 (1991)
   PUBMED   1833066
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008798.10.
            
            Summary: The protein encoded by this gene belongs to the highly
            conserved cyclin family, whose members are characterized by a
            dramatic periodicity in protein abundance through the cell cycle.
            Cyclins function as regulators of CDK kinases. Different cyclins
            exhibit distinct expression and degradation patterns which
            contribute to the temporal coordination of each mitotic event. This
            cyclin forms a complex with and functions as a regulatory subunit
            of CDK2, whose activity is required for cell cycle G1/S transition.
            This protein accumulates at the G1-S phase boundary and is degraded
            as cells progress through S phase. Overexpression of this gene has
            been observed in many tumors, which results in chromosome
            instability, and thus may contribute to tumorigenesis. This protein
            was found to associate with, and be involved in, the
            phosphorylation of NPAT protein (nuclear protein mapped to the ATM
            locus), which participates in cell-cycle regulated histone gene
            expression and plays a critical role in promoting cell-cycle
            progression in the absence of pRB. [provided by RefSeq, Apr 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.31212.1,
                                           SRR14372080.1679147.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..350
                     /product="G1/S-specific cyclin-E1 isoform 9"
                     /note="G1/S-specific cyclin-E1"
                     /calculated_mol_wt=39681
     Region          88..223
                     /region_name="CYCLIN_CCNE1_rpt1"
                     /note="first cyclin box found in G1/S-specific cyclin-E1
                     (CCNE1); cd20579"
                     /db_xref="CDD:410282"
     Site            order(94..95,97,100..101,104..105,108,112,147,182,
                     186..190,194..195,212,215..216,219..220,223)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410282"
     Region          <218..296
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cl40454"
                     /db_xref="CDD:477360"
     CDS             1..350
                     /gene="CCNE1"
                     /gene_synonym="CCNE; pCCNE1"
                     /coded_by="NM_001440308.1:185..1237"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:898"
                     /db_xref="HGNC:HGNC:1589"
                     /db_xref="MIM:123837"
ORIGIN      
        1 mkedggaefs arsrkrkanv tvflqdpdee makidrtard qcgsqpwdnn avcadpcsli
       61 ptpdkedddr vypnstckpr iiapsrgspl pvlswanree vwkimlnkek tylrdqhfle
      121 qhpllqpkmr ailldwlmev cevyklhret fylaqdffdr ymatqenvvk tllqligiss
      181 lfiaakleei yppklhqfay vtdgacsgde iltmelmimk lldlcvldvd clefpygila
      241 asalyhfsss elmqkvsgyq wcdiencvkw mvpfamvire tgssklkhfr gvadedahni
      301 qthrdsldll dkarakkaml seqnrasplp sglltppqsg kkqssgpema
//
LOCUS       NP_001400847             180 aa            linear   PRI 21-NOV-2025
DEFINITION  transcription factor ETV6 isoform 7 [Homo sapiens].
ACCESSION   NP_001400847
VERSION     NP_001400847.1
DBSOURCE    REFSEQ: accession NM_001413918.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Xu,W., Tian,F., Tai,X., Song,G., Liu,Y., Fan,L., Weng,X., Yang,E.,
            Wang,M., Bornhauser,M., Zhang,C., Lock,R.B., Wong,J.W.H., Wang,J.,
            Jing,D. and Mi,J.Q.
  TITLE     ETV6::ACSL6 translocation-driven super-enhancer activation leads to
            eosinophilia in acute lymphoblastic leukemia through IL-3
            overexpression
  JOURNAL   Haematologica 109 (8), 2445-2458 (2024)
   PUBMED   38356460
  REMARK    GeneRIF: ETV6::ACSL6 translocation-driven super-enhancer activation
            leads to eosinophilia in acute lymphoblastic leukemia through IL-3
            overexpression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Xue,S., Sun,H.P., Huang,X.B., Chen,X., Wang,T., Ma,W., Tian,Y.,
            Pan,Z.L., Li,L.H., Zhang,L., Liu,H.X. and Cao,X.Y.
  TITLE     Characteristics and literature review of ETV6::ABL1 fusion
            gene-positive acute myeloid leukemia
  JOURNAL   Int J Hematol 119 (5), 564-572 (2024)
   PUBMED   38441775
  REMARK    GeneRIF: Characteristics and literature review of ETV6::ABL1 fusion
            gene-positive acute myeloid leukemia.
            Review article
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Mueller,S.B., Pikman,Y., Tasian,S.K., Silverman,L.B., Harris,M.H.
            and Tsai,H.K.
  TITLE     ETV6 fusions from insertions of exons 3-5 in pediatric hematologic
            malignancies
  JOURNAL   Haematologica 108 (12), 3471-3476 (2023)
   PUBMED   37381775
  REMARK    GeneRIF: ETV6 fusions from insertions of exons 3-5 in pediatric
            hematologic malignancies.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Klubickova,N., Mosaieby,E., Ptakova,N., Trinquet,A., Lae,M.,
            Costes-Martineau,V. and Skalova,A.
  TITLE     High-grade non-intestinal type sinonasal adenocarcinoma with
            ETV6::NTRK3 fusion, distinct from secretory carcinoma by
            immunoprofile and morphology
  JOURNAL   Virchows Arch 483 (2), 187-195 (2023)
   PUBMED   37415052
  REMARK    GeneRIF: High-grade non-intestinal type sinonasal adenocarcinoma
            with ETV6::NTRK3 fusion, distinct from secretory carcinoma by
            immunoprofile and morphology.
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Romana,S.P., Mauchauffe,M., Le Coniat,M., Chumakov,I., Le
            Paslier,D., Berger,R. and Bernard,O.A.
  TITLE     The t(12;21) of acute lymphoblastic leukemia results in a tel-AML1
            gene fusion
  JOURNAL   Blood 85 (12), 3662-3670 (1995)
   PUBMED   7780150
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Golub,T.R., Barker,G.F., Bohlander,S.K., Hiebert,S.W., Ward,D.C.,
            Bray-Ward,P., Morgan,E., Raimondi,S.C., Rowley,J.D. and
            Gilliland,D.G.
  TITLE     Fusion of the TEL gene on 12p13 to the AML1 gene on 21q22 in acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 92 (11), 4917-4921 (1995)
   PUBMED   7761424
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Buijs,A., Sherr,S., van Baal,S., van Bezouw,S., van der Plas,D.,
            Geurts van Kessel,A., Riegman,P., Lekanne Deprez,R., Zwarthoff,E.,
            Hagemeijer,A. et al.
  TITLE     Translocation (12;22) (p13;q11) in myeloproliferative disorders
            results in fusion of the ETS-like TEL gene on 12p13 to the MN1 gene
            on 22q11
  JOURNAL   Oncogene 10 (8), 1511-1519 (1995)
   PUBMED   7731705
  REMARK    Erratum:[Oncogene 1995 Aug 17;11(4):809]
REFERENCE   9  (residues 1 to 180)
  AUTHORS   Pencheva,B., Di Paola,J. and Porter,C.C.
  TITLE     ETV6-Related Thrombocytopenia and Predisposition to Leukemia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   33226740
REFERENCE   10 (residues 1 to 180)
  AUTHORS   Fainstein,E., Einat,M., Gokkel,E., Marcelle,C., Croce,C.M.,
            Gale,R.P. and Canaani,E.
  TITLE     Nucleotide sequence analysis of human abl and bcr-abl cDNAs
  JOURNAL   Oncogene 4 (12), 1477-1481 (1989)
   PUBMED   2687768
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007450.1, AC084430.13 and
            AC084358.19.
            
            Summary: This gene encodes an ETS family transcription factor. The
            product of this gene contains two functional domains: a N-terminal
            pointed (PNT) domain that is involved in protein-protein
            interactions with itself and other proteins, and a C-terminal
            DNA-binding domain. Gene knockout studies in mice suggest that it
            is required for hematopoiesis and maintenance of the developing
            vascular network. This gene is known to be involved in a large
            number of chromosomal rearrangements associated with leukemia and
            congenital fibrosarcoma. [provided by RefSeq, Sep 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR13170464.544455.1,
                                           SRR18074968.2365137.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2152719, SAMEA2152798
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..180
                     /product="transcription factor ETV6 isoform 7"
                     /note="ets variant gene 6 (TEL oncogene); TEL1 oncogene;
                     transcription factor ETV6; ETS-related protein Tel1;
                     ETV6-RUNX1 fusion protein"
                     /calculated_mol_wt=20527
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            11..12
                     /site_type="other"
                     /note="Breakpoint for translocation to form CHIC2-ETV6 in
                     AML; propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12435397,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            54..55
                     /site_type="other"
                     /note="Breakpoint for translocation to form ETV6-MDS2 in
                     MDS; propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            55..56
                     /site_type="other"
                     /note="Breakpoint for translocation to form PAX5-ETV6;
                     propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Region          56..>109
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     CDS             1..180
                     /gene="ETV6"
                     /gene_synonym="TEL; TEL/ABL; THC5"
                     /coded_by="NM_001413918.1:455..997"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:2120"
                     /db_xref="HGNC:HGNC:3495"
                     /db_xref="MIM:600618"
ORIGIN      
        1 msetpaqcsi kqerisytpp espvpsyass tplhvpvpra lrmeedsirl pahlrlqpiy
       61 wsrddvaqwl kwaenefslr pidsntfemn gkalllltke dfryrsphsd gfslcrqagv
      121 qcrdlgslqp pppgfkqfsc lsllsswdyr rapqhpanfc ilvemrfhrv gqddlnllts
//
LOCUS       NP_001397808             539 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-binding protein Ikaros isoform 17 [Homo sapiens].
ACCESSION   NP_001397808 XP_011513368
VERSION     NP_001397808.1
DBSOURCE    REFSEQ: accession NM_001410879.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Song,Y., Zhang,Y., Wang,Z., Lin,Y., Cao,X., Han,X., Li,G., Hou,A.
            and Han,S.
  TITLE     CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway
  JOURNAL   Oncogene 43 (36), 2737-2749 (2024)
   PUBMED   39112517
  REMARK    GeneRIF: CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway.
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Ezzat,S., Yu,S. and Asa,S.L.
  TITLE     Ikaros isoforms in human pituitary tumors: distinct localization,
            histone acetylation, and activation of the 5' fibroblast growth
            factor receptor-4 promoter
  JOURNAL   Am J Pathol 163 (3), 1177-1184 (2003)
   PUBMED   12937159
REFERENCE   5  (residues 1 to 539)
  AUTHORS   Payne,K.J., Nicolas,J.H., Zhu,J.Y., Barsky,L.W. and Crooks,G.M.
  TITLE     Cutting edge: predominant expression of a novel Ikaros isoform in
            normal human hemopoiesis
  JOURNAL   J Immunol 167 (4), 1867-1870 (2001)
   PUBMED   11489963
  REMARK    GeneRIF: A novel Ikaros isoform 'Ikx' is the predominant Ikaros
            protein present in normal cord blood and bone marrow cells, but not
            in leukemia cell lines.
REFERENCE   6  (residues 1 to 539)
  AUTHORS   Nakayama,H., Ishimaru,F., Avitahl,N., Sezaki,N., Fujii,N.,
            Nakase,K., Ninomiya,Y., Harashima,A., Minowada,J., Tsuchiyama,J.,
            Imajoh,K., Tsubota,T., Fukuda,S., Sezaki,T., Kojima,K., Hara,M.,
            Takimoto,H., Yorimitsu,S., Takahashi,I., Miyata,A., Taniguchi,S.,
            Tokunaga,Y., Gondo,H., Niho,Y., Harada,M. et al.
  TITLE     Decreases in Ikaros activity correlate with blast crisis in
            patients with chronic myelogenous leukemia
  JOURNAL   Cancer Res 59 (16), 3931-3934 (1999)
   PUBMED   10463586
REFERENCE   7  (residues 1 to 539)
  AUTHORS   Sun,L., Heerema,N., Crotty,L., Wu,X., Navara,C., Vassilev,A.,
            Sensel,M., Reaman,G.H. and Uckun,F.M.
  TITLE     Expression of dominant-negative and mutant isoforms of the
            antileukemic transcription factor Ikaros in infant acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 96 (2), 680-685 (1999)
   PUBMED   9892693
REFERENCE   8  (residues 1 to 539)
  AUTHORS   Molnar,A., Wu,P., Largespada,D.A., Vortkamp,A., Scherer,S.,
            Copeland,N.G., Jenkins,N.A., Bruns,G. and Georgopoulos,K.
  TITLE     The Ikaros gene encodes a family of lymphocyte-restricted zinc
            finger DNA binding proteins, highly conserved in human and mouse
  JOURNAL   J Immunol 156 (2), 585-592 (1996)
   PUBMED   8543809
REFERENCE   9  (residues 1 to 539)
  AUTHORS   Hahm,K., Ernst,P., Lo,K., Kim,G.S., Turck,C. and Smale,S.T.
  TITLE     The lymphoid transcription factor LyF-1 is encoded by specific,
            alternatively spliced mRNAs derived from the Ikaros gene
  JOURNAL   Mol Cell Biol 14 (11), 7111-7123 (1994)
   PUBMED   7935426
REFERENCE   10 (residues 1 to 539)
  AUTHORS   Georgopoulos,K., Moore,D.D. and Derfler,B.
  TITLE     Ikaros, an early lymphoid-specific transcription factor and a
            putative mediator for T cell commitment
  JOURNAL   Science 258 (5083), 808-812 (1992)
   PUBMED   1439790
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC233268.2 and AC124014.3.
            
            On Aug 17, 2022 this sequence version replaced XP_011513368.1.
            
            Summary: This gene encodes a transcription factor that belongs to
            the family of zinc-finger DNA-binding proteins associated with
            chromatin remodeling. The expression of this protein is restricted
            to the fetal and adult hemo-lymphopoietic system, and it functions
            as a regulator of lymphocyte differentiation. Several alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. Most isoforms share a common C-terminal
            domain, which contains two zinc finger motifs that are required for
            hetero- or homo-dimerization, and for interactions with other
            proteins. The isoforms, however, differ in the number of N-terminal
            zinc finger motifs that bind DNA and in nuclear localization signal
            presence, resulting in members with and without DNA-binding
            properties. Only a few isoforms contain the requisite three or more
            N-terminal zinc motifs that confer high affinity binding to a
            specific core DNA sequence element in the promoters of target
            genes. The non-DNA-binding isoforms are largely found in the
            cytoplasm, and are thought to function as dominant-negative
            factors. Overexpression of some dominant-negative isoforms have
            been associated with B-cell malignancies, such as acute
            lymphoblastic leukemia (ALL). [provided by RefSeq, May 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2078540.1,
                                           SRR14038195.1659047.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12.2"
     Protein         1..539
                     /product="DNA-binding protein Ikaros isoform 17"
                     /note="zinc finger protein, subfamily 1A, 1 (Ikaros);
                     DNA-binding protein Ikaros; CLL-associated antigen KW-6;
                     ikaros family zinc finger protein 1; protein phosphatase
                     1, regulatory subunit 92; lymphoid transcription factor
                     LyF-1"
                     /calculated_mol_wt=59692
     Region          139..159
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(144,146,148,150..151,154..155,158,172,174,178..179,
                     182..183,186,200,202,204,206..207,210..211,214)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          152..176
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          167..187
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          179..204
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          195..215
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          223..244
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..539
                     /gene="IKZF1"
                     /gene_synonym="CVID13; Hs.54452; IK1; IKAROS; LyF-1; LYF1;
                     PPP1R92; PRO0758; ZNFN1A1"
                     /coded_by="NM_001410879.1:482..2101"
                     /note="isoform 17 is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS94102.1"
                     /db_xref="GeneID:10320"
                     /db_xref="HGNC:HGNC:13176"
                     /db_xref="MIM:603023"
ORIGIN      
        1 mdadegqdms qvsgkesppv sdtpdegdep mpipedlstt sggqqssksd rvvvtygadd
       61 frdfhaiipk sfspsnvkve tqsdeengra cemngeecae dlrmldasge kmngshrdqg
      121 ssalsgvggi rlpngklkcd icgiicigpn vlmvhkrsht gerpfqcnqc gasftqkgnl
      181 lrhiklhsge kpfkchlcny acrrrdaltg hlrthsvgkp hkcgycgrsy kqrssleehk
      241 erchnylesm glpgtlypvi keetnhsema edlckigser slvldrlasn vakrkssmpq
      301 kflgdkglsd tpydssasye kenemmkshv mdqainnain ylgaeslrpl vqtppggsev
      361 vpvispmyql hkplaegtpr snhsaqdsav enllllskak lvpsereasp snscqdstdt
      421 esnneeqrsg liyltnhiap harnglslke ehraydllra asensqdalr vvstsgeqmk
      481 vykcehcrvl fldhvmytih mgchgfrdpf ecnmcgyhsq dryefsshit rgehrfhms
//
LOCUS       NP_001401232             487 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 3 isoform 3
            precursor [Homo sapiens].
ACCESSION   NP_001401232
VERSION     NP_001401232.1
DBSOURCE    REFSEQ: accession NM_001414303.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Tang,Q., Yuan,Y., Li,L., Xu,Y., Ji,W., Xiao,S., Han,Y., Miao,W.,
            Cai,J., You,P., Chen,M., Ding,S., Li,Z., Qi,Z., Hou,W. and Luo,H.
  TITLE     Comprehensive analysis reveals that LTBR is a immune-related
            biomarker for glioma
  JOURNAL   Comput Biol Med 174, 108457 (2024)
   PUBMED   38599071
  REMARK    GeneRIF: Comprehensive analysis reveals that LTBR is a
            immune-related biomarker for glioma.
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Wu,Y., Zhao,S., Guo,W., Liu,Y., Requena Mullor,M.D.M.,
            Rodriguez,R.A. and Wei,R.
  TITLE     Systematic analysis of the prognostic value and immunological
            function of LTBR in human cancer
  JOURNAL   Aging (Albany NY) 16 (1), 129-152 (2024)
   PUBMED   38175686
  REMARK    GeneRIF: Systematic analysis of the prognostic value and
            immunological function of LTBR in human cancer.
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Shuptrine,C.W., Perez,V.M., Selitsky,S.R., Schreiber,T.H. and
            Fromm,G.
  TITLE     Shining a LIGHT on myeloid cell targeted immunotherapy
  JOURNAL   Eur J Cancer 187, 147-160 (2023)
   PUBMED   37167762
  REMARK    Review article
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Abudukeyoumu,A., Lai,Z.Z., Lu,J.J., Zhang,X., Hou,D.Y., Dong,J.,
            Wu,J.N., Li,M.Q. and Xie,F.
  TITLE     A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion
  JOURNAL   J Reprod Immunol 153, 103693 (2022)
   PUBMED   35987137
  REMARK    GeneRIF: A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion.
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Remouchamps,C., Boutaffala,L., Ganeff,C. and Dejardin,E.
  TITLE     Biology and signal transduction pathways of the
            Lymphotoxin-alphabeta/LTbetaR system
  JOURNAL   Cytokine Growth Factor Rev 22 (5-6), 301-310 (2011)
   PUBMED   22152226
  REMARK    Review article
REFERENCE   6  (residues 1 to 487)
  AUTHORS   Nakano,H., Oshima,H., Chung,W., Williams-Abbott,L., Ware,C.F.,
            Yagita,H. and Okumura,K.
  TITLE     TRAF5, an activator of NF-kappaB and putative signal transducer for
            the lymphotoxin-beta receptor
  JOURNAL   J Biol Chem 271 (25), 14661-14664 (1996)
   PUBMED   8663299
REFERENCE   7  (residues 1 to 487)
  AUTHORS   Browning,J.L., Miatkowski,K., Sizing,I., Griffiths,D., Zafari,M.,
            Benjamin,C.D., Meier,W. and Mackay,F.
  TITLE     Signaling through the lymphotoxin beta receptor induces the death
            of some adenocarcinoma tumor lines
  JOURNAL   J Exp Med 183 (3), 867-878 (1996)
   PUBMED   8642291
REFERENCE   8  (residues 1 to 487)
  AUTHORS   Baens,M., Aerssens,J., van Zand,K., Van den Berghe,H. and
            Marynen,P.
  TITLE     Isolation and regional assignment of human chromosome 12p cDNAs
  JOURNAL   Genomics 29 (1), 44-52 (1995)
   PUBMED   8530100
REFERENCE   9  (residues 1 to 487)
  AUTHORS   Crowe,P.D., VanArsdale,T.L., Walter,B.N., Ware,C.F., Hession,C.,
            Ehrenfels,B., Browning,J.L., Din,W.S., Goodwin,R.G. and Smith,C.A.
  TITLE     A lymphotoxin-beta-specific receptor
  JOURNAL   Science 264 (5159), 707-710 (1994)
   PUBMED   8171323
REFERENCE   10 (residues 1 to 487)
  AUTHORS   Baens,M., Chaffanet,M., Cassiman,J.J., van den Berghe,H. and
            Marynen,P.
  TITLE     Construction and evaluation of a hncDNA library of human 12p
            transcribed sequences derived from a somatic cell hybrid
  JOURNAL   Genomics 16 (1), 214-218 (1993)
   PUBMED   8486360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005840.2.
            
            Summary: This gene encodes a member of the tumor necrosis factor
            receptor superfamily. The major ligands of this receptor include
            lymphotoxin alpha/beta and tumor necrosis factor ligand superfamily
            member 14. The encoded protein plays a role in signalling during
            the development of lymphoid and other organs, lipid metabolism,
            immune response, and programmed cell death. Activity of this
            receptor has also been linked to carcinogenesis. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1968399.1,
                                           SRR14038196.2670959.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..487
                     /product="tumor necrosis factor receptor superfamily
                     member 3 isoform 3 precursor"
                     /note="tumor necrosis factor C receptor; lymphotoxin B
                     receptor; tumor necrosis factor receptor type III;
                     lymphotoxin beta receptor (TNFR superfamily, member 3);
                     tumor necrosis factor receptor 2-related protein"
                     /calculated_mol_wt=49242
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3049
     Region          11..168
                     /region_name="TNFRSF3"
                     /note="Tumor necrosis factor receptor superfamily member 3
                     (TNFRSF3), also known as lymphotoxin beta receptor (LTBR);
                     cd10578"
                     /db_xref="CDD:276904"
     Region          22..80
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276904"
     Region          83..124
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276904"
     Region          126..167
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276904"
     Region          139..>210
                     /region_name="TNFRSF"
                     /note="Tumor necrosis factor receptor superfamily
                     (TNFRSF); cl22855"
                     /db_xref="CDD:473981"
     Region          170..210
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276900"
     CDS             1..487
                     /gene="LTBR"
                     /gene_synonym="D12S370; LT-BETA-R; TNF-R-III; TNFCR;
                     TNFR-RP; TNFR2-RP; TNFR3; TNFRSF3"
                     /coded_by="NM_001414303.1:198..1661"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:4055"
                     /db_xref="HGNC:HGNC:6718"
                     /db_xref="MIM:600979"
ORIGIN      
        1 mllpwatsap glawgplvlg lfgllaasqp qavppyasen qtcrdqekey yepqhriccs
       61 rcppgtyvsa kcsrirdtvc atcaensyne hwnylticql crpcdpvmgl eeiapctskr
      121 ktqcrcqpgm fcaawalect hcellsdcpp gteaelkdev gkgnnhcvpc kaghfqntss
      181 psarcqphtr cenqglveaa pgtaqsdttc knpleplppe msgtmlmlav llplafflll
      241 atvfsciwks hpslcrklaa yseagdesds glflwapgws scytlcwdve aerlglrpag
      301 eptpisfsia gsllkrrpqg egpnpvagsw eppkahpyfp dlvqpllpis gdvspvstgl
      361 paapvleagv pqqqspldlt repqlepgeq sqvahgtngi hvtggsmtit gniyiyngpv
      421 lggppgpgdl patpeppypi peegdpgppg lstphqedgk awhlaetehc gatpsnrgpr
      481 nqfithd
//
LOCUS       NP_001394259             284 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform Tpm1.5cy [Homo sapiens].
ACCESSION   NP_001394259 XP_016878027
VERSION     NP_001394259.1
DBSOURCE    REFSEQ: accession NM_001407330.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            On May 31, 2022 this sequence version replaced XP_016878027.2.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: KU178366.1, SRR11853561.10117.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..284
                     /product="tropomyosin alpha-1 chain isoform Tpm1.5cy"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=32735
     Region          48..282
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..284
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407330.1:84..938"
                     /note="isoform Tpm1.5cy is encoded by transcript variant
                     20"
                     /db_xref="CCDS:CCDS10181.1"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle delvslqkkl kgtedeldky
       61 sealkdaqek lelaekkatd aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegqv rqleeqlrim dqtlkalmaa edkysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledel yaqklkykai seeldhalnd mtsm
//
LOCUS       NP_001415206             443 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B
            beta isoform isoform e [Homo sapiens].
ACCESSION   NP_001415206 NP_004567
VERSION     NP_001415206.1
DBSOURCE    REFSEQ: accession NM_001428277.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Shen,D. and Kang,S.
  TITLE     Comprehensive analysis of mitochondria-related genes indicates that
            PPP2R2B is a novel biomarker and promotes the progression of
            bladder cancer via Wnt signaling pathway
  JOURNAL   Biol Direct 19 (1), 17 (2024)
   PUBMED   38409085
  REMARK    GeneRIF: Comprehensive analysis of mitochondria-related genes
            indicates that PPP2R2B is a novel biomarker and promotes the
            progression of bladder cancer via Wnt signaling pathway.
            Erratum:[Biol Direct. 2024 Apr 18;19(1):27. doi:
            10.1186/s13062-024-00474-1. PMID: 38637864]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Zhou,C., Liu,H.B., Jahanbakhsh,F., Deng,L., Wu,B., Ying,M.,
            Margolis,R.L. and Li,P.P.
  TITLE     Bidirectional Transcription at the PPP2R2B Gene Locus in
            Spinocerebellar Ataxia Type 12
  JOURNAL   Mov Disord 38 (12), 2230-2240 (2023)
   PUBMED   37735923
  REMARK    GeneRIF: Bidirectional Transcription at the PPP2R2B Gene Locus in
            Spinocerebellar Ataxia Type 12.
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Ruediger,R., Brewis,N., Ohst,K. and Walter,G.
  TITLE     Increasing the ratio of PP2A core enzyme to holoenzyme inhibits
            Tat-stimulated HIV-1 transcription and virus production
  JOURNAL   Virology 238 (2), 432-443 (1997)
   PUBMED   9400615
REFERENCE   6  (residues 1 to 443)
  AUTHORS   Tung,H.Y., De Rocquigny,H., Zhao,L.J., Cayla,X., Roques,B.P. and
            Ozon,R.
  TITLE     Direct activation of protein phosphatase-2A0 by HIV-1 encoded
            protein complex NCp7:vpr
  JOURNAL   FEBS Lett 401 (2-3), 197-201 (1997)
   PUBMED   9013886
REFERENCE   7  (residues 1 to 443)
  AUTHORS   Schalling,M., Hudson,T.J., Buetow,K.H. and Housman,D.E.
  TITLE     Direct detection of novel expanded trinucleotide repeats in the
            human genome
  JOURNAL   Nat Genet 4 (2), 135-139 (1993)
   PUBMED   8348150
REFERENCE   8  (residues 1 to 443)
  AUTHORS   Margolis,R.L., Holmes,S.E., Srivastava,A.K., Mukherji,M. and
            Sinha,K.K.
  TITLE     Spinocerebellar Ataxia Type 12 - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301381
REFERENCE   9  (residues 1 to 443)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
REFERENCE   10 (residues 1 to 443)
  AUTHORS   Mayer,R.E., Hendrix,P., Cron,P., Matthies,R., Stone,S.R., Goris,J.,
            Merlevede,W., Hofsteenge,J. and Hemmings,B.A.
  TITLE     Structure of the 55-kDa regulatory subunit of protein phosphatase
            2A: evidence for a neuronal-specific isoform
  JOURNAL   Biochemistry 30 (15), 3589-3597 (1991)
   PUBMED   1849734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011386.6, AC009186.7 and
            AC008728.7.
            
            Summary: The product of this gene belongs to the phosphatase 2
            regulatory subunit B family. Protein phosphatase 2 is one of the
            four major Ser/Thr phosphatases, and it is implicated in the
            negative control of cell growth and division. It consists of a
            common heteromeric core enzyme, which is composed of a catalytic
            subunit and a constant regulatory subunit, that associates with a
            variety of regulatory subunits. The B regulatory subunit might
            modulate substrate selectivity and catalytic activity. This gene
            encodes a beta isoform of the regulatory subunit B55 subfamily.
            Defects in this gene cause autosomal dominant spinocerebellar
            ataxia 12 (SCA12), a disease caused by degeneration of the
            cerebellum, sometimes involving the brainstem and spinal cord, and
            in resulting in poor coordination of speech and body movements.
            Multiple alternatively spliced variants, which encode different
            isoforms, have been identified for this gene. The 5' UTR of some of
            these variants includes a CAG trinucleotide repeat sequence (7-28
            copies) that can be expanded to 55-78 copies in cases of SCA12.
            [provided by RefSeq, Jul 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M64930.1, SRR18074967.1926126.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..443
                     /product="serine/threonine-protein phosphatase 2A 55 kDa
                     regulatory subunit B beta isoform isoform e"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase 2, regulatory subunit B, beta"
                     /calculated_mol_wt=51579
     Region          22..438
                     /region_name="CDC55"
                     /note="Serine/threonine protein phosphatase 2A, regulatory
                     subunit [Signal transduction mechanisms]; COG5170"
                     /db_xref="CDD:227498"
     Region          22..61
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00005.1)"
     Region          27..75
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          87..128
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00005.1)"
     Region          93..170
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          171..209
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00005.1)"
     Region          176..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          220..260
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00005.1)"
     Region          226..277
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P36877; propagated from
                     UniProtKB/Swiss-Prot (Q00005.1)"
     Region          279..317
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00005.1)"
     Region          284..320
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P36877; propagated from
                     UniProtKB/Swiss-Prot (Q00005.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P36877; propagated from
                     UniProtKB/Swiss-Prot (Q00005.1)"
     Region          334..375
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00005.1)"
     Region          341..376
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          410..442
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00005.1)"
     Region          415..438
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..443
                     /gene="PPP2R2B"
                     /gene_synonym="B55BETA; PP2AB55BETA; PP2ABBETA; PP2APR55B;
                     PP2APR55BETA; PR2AB55BETA; PR2ABBETA; PR2APR55BETA; PR52B;
                     PR55-BETA; PR55BETA; SCA12"
                     /coded_by="NM_001428277.1:687..2018"
                     /note="isoform e is encoded by transcript variant 11"
                     /db_xref="GeneID:5521"
                     /db_xref="HGNC:HGNC:9305"
                     /db_xref="MIM:604325"
ORIGIN      
        1 meedidtrki nnsflrdhsy ateadiistv efnhtgella tgdkggrvvi fqreqesknq
       61 vhrrgeynvy stfqshepef dylksleiee kinkirwlpq qnaayfllst ndktvklwkv
      121 serdkrpegy nlkdeegrlr dpatittlrv pvlrpmdlmv eatprrvfan ahtyhinsis
      181 vnsdyetyms addlrinlwn feitnqsfni vdikpanmee ltevitaaef hphhcntfvy
      241 ssskgtirlc dmrasalcdr htkffeeped psnrsffsei issisdvkfs hsgryimtrd
      301 yltvkvwdln menrpietyq vhdylrsklc slyendcifd kfecvwngsd svimtgsynn
      361 ffrmfdrntk rdvtleasre nskprailkp rkvcvggkrr kdeisvdsld fskkilhtaw
      421 hpseniiava atnnlyifqd kvn
//
LOCUS       NP_001411264             193 aa            linear   PRI 21-NOV-2025
DEFINITION  protein cholesin isoform b [Homo sapiens].
ACCESSION   NP_001411264 XP_054215198
VERSION     NP_001411264.1
DBSOURCE    REFSEQ: accession NM_001424335.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Ryk,A., Marcinkiewicz,A., Chrzanowski,J., Michalak,A.M., Drozdz,I.,
            Burzynski,J., Krejca,M. and Fendler,W.
  TITLE     Cholesin receptor signalling is active in cardiovascular
            system-associated adipose tissue and correlates with SGLT2i
            treatment in patients with diabetes
  JOURNAL   Cardiovasc Diabetol 23 (1), 211 (2024)
   PUBMED   38902687
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Hu,X., Chen,F., Jia,L., Long,A., Peng,Y., Li,X., Huang,J., Wei,X.,
            Fang,X., Gao,Z., Zhang,M., Liu,X., Chen,Y.G., Wang,Y., Zhang,H. and
            Wang,Y.
  TITLE     A gut-derived hormone regulates cholesterol metabolism
  JOURNAL   Cell 187 (7), 1685-1700 (2024)
   PUBMED   38503280
  REMARK    GeneRIF: A gut-derived hormone regulates cholesterol metabolism.
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Willer,C.J., Schmidt,E.M., Sengupta,S., Peloso,G.M., Gustafsson,S.,
            Kanoni,S., Ganna,A., Chen,J., Buchkovich,M.L., Mora,S.,
            Beckmann,J.S., Bragg-Gresham,J.L., Chang,H.Y., Demirkan,A., Den
            Hertog,H.M., Do,R., Donnelly,L.A., Ehret,G.B., Esko,T.,
            Feitosa,M.F., Ferreira,T., Fischer,K., Fontanillas,P., Fraser,R.M.,
            Freitag,D.F., Gurdasani,D., Heikkila,K., Hypponen,E., Isaacs,A.,
            Jackson,A.U., Johansson,A., Johnson,T., Kaakinen,M., Kettunen,J.,
            Kleber,M.E., Li,X., Luan,J., Lyytikainen,L.P., Magnusson,P.K.E.,
            Mangino,M., Mihailov,E., Montasser,M.E., Muller-Nurasyid,M.,
            Nolte,I.M., O'Connell,J.R., Palmer,C.D., Perola,M., Petersen,A.K.,
            Sanna,S., Saxena,R., Service,S.K., Shah,S., Shungin,D., Sidore,C.,
            Song,C., Strawbridge,R.J., Surakka,I., Tanaka,T., Teslovich,T.M.,
            Thorleifsson,G., Van den Herik,E.G., Voight,B.F., Volcik,K.A.,
            Waite,L.L., Wong,A., Wu,Y., Zhang,W., Absher,D., Asiki,G.,
            Barroso,I., Been,L.F., Bolton,J.L., Bonnycastle,L.L., Brambilla,P.,
            Burnett,M.S., Cesana,G., Dimitriou,M., Doney,A.S.F., Doring,A.,
            Elliott,P., Epstein,S.E., Ingi Eyjolfsson,G., Gigante,B.,
            Goodarzi,M.O., Grallert,H., Gravito,M.L., Groves,C.J., Hallmans,G.,
            Hartikainen,A.L., Hayward,C., Hernandez,D., Hicks,A.A., Holm,H.,
            Hung,Y.J., Illig,T., Jones,M.R., Kaleebu,P., Kastelein,J.J.P.,
            Khaw,K.T., Kim,E., Klopp,N., Komulainen,P., Kumari,M.,
            Langenberg,C., Lehtimaki,T., Lin,S.Y., Lindstrom,J., Loos,R.J.F.,
            Mach,F., McArdle,W.L., Meisinger,C., Mitchell,B.D., Muller,G.,
            Nagaraja,R., Narisu,N., Nieminen,T.V.M., Nsubuga,R.N., Olafsson,I.,
            Ong,K.K., Palotie,A., Papamarkou,T., Pomilla,C., Pouta,A.,
            Rader,D.J., Reilly,M.P., Ridker,P.M., Rivadeneira,F., Rudan,I.,
            Ruokonen,A., Samani,N., Scharnagl,H., Seeley,J., Silander,K.,
            Stancakova,A., Stirrups,K., Swift,A.J., Tiret,L.,
            Uitterlinden,A.G., van Pelt,L.J., Vedantam,S., Wainwright,N.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilsgaard,T., Wilson,J.F.,
            Young,E.H., Zhao,J.H., Adair,L.S., Arveiler,D., Assimes,T.L.,
            Bandinelli,S., Bennett,F., Bochud,M., Boehm,B.O., Boomsma,D.I.,
            Borecki,I.B., Bornstein,S.R., Bovet,P., Burnier,M., Campbell,H.,
            Chakravarti,A., Chambers,J.C., Chen,Y.I., Collins,F.S.,
            Cooper,R.S., Danesh,J., Dedoussis,G., de Faire,U., Feranil,A.B.,
            Ferrieres,J., Ferrucci,L., Freimer,N.B., Gieger,C., Groop,L.C.,
            Gudnason,V., Gyllensten,U., Hamsten,A., Harris,T.B., Hingorani,A.,
            Hirschhorn,J.N., Hofman,A., Hovingh,G.K., Hsiung,C.A.,
            Humphries,S.E., Hunt,S.C., Hveem,K., Iribarren,C., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kaprio,J., Kesaniemi,A., Kivimaki,M.,
            Kooner,J.S., Koudstaal,P.J., Krauss,R.M., Kuh,D., Kuusisto,J.,
            Kyvik,K.O., Laakso,M., Lakka,T.A., Lind,L., Lindgren,C.M.,
            Martin,N.G., Marz,W., McCarthy,M.I., McKenzie,C.A., Meneton,P.,
            Metspalu,A., Moilanen,L., Morris,A.D., Munroe,P.B., Njolstad,I.,
            Pedersen,N.L., Power,C., Pramstaller,P.P., Price,J.F., Psaty,B.M.,
            Quertermous,T., Rauramaa,R., Saleheen,D., Salomaa,V.,
            Sanghera,D.K., Saramies,J., Schwarz,P.E.H., Sheu,W.H.,
            Shuldiner,A.R., Siegbahn,A., Spector,T.D., Stefansson,K.,
            Strachan,D.P., Tayo,B.O., Tremoli,E., Tuomilehto,J., Uusitupa,M.,
            van Duijn,C.M., Vollenweider,P., Wallentin,L., Wareham,N.J.,
            Whitfield,J.B., Wolffenbuttel,B.H.R., Ordovas,J.M., Boerwinkle,E.,
            Palmer,C.N.A., Thorsteinsdottir,U., Chasman,D.I., Rotter,J.I.,
            Franks,P.W., Ripatti,S., Cupples,L.A., Sandhu,M.S., Rich,S.S.,
            Boehnke,M., Deloukas,P., Kathiresan,S., Mohlke,K.L., Ingelsson,E.
            and Abecasis,G.R.
  CONSRTM   Global Lipids Genetics Consortium
  TITLE     Discovery and refinement of loci associated with lipid levels
  JOURNAL   Nat Genet 45 (11), 1274-1283 (2013)
   PUBMED   24097068
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Yashin,A.I., Wu,D., Arbeev,K.G. and Ukraintseva,S.V.
  TITLE     Joint influence of small-effect genetic variants on human longevity
  JOURNAL   Aging (Albany NY) 2 (9), 612-620 (2010)
   PUBMED   20834067
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Satoh,J., Obayashi,S., Misawa,T., Sumiyoshi,K., Oosumi,K. and
            Tabunoki,H.
  TITLE     Protein microarray analysis identifies human cellular prion protein
            interactors
  JOURNAL   Neuropathol Appl Neurobiol 35 (1), 16-35 (2009)
   PUBMED   18482256
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CP068271.2.
            
            On Sep 21, 2023 this sequence version replaced XP_054215198.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR13170464.66558.1, DRR138515.130920.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMN03465413 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..193
                     /product="protein cholesin isoform b"
                     /note="uncharacterized protein C7orf50; protein cholesin"
                     /calculated_mol_wt=21839
     Region          1..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     Region          104..165
                     /region_name="WKF"
                     /note="WKF domain; pfam10180"
                     /db_xref="CDD:462982"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ6.1)"
     CDS             1..193
                     /gene="CHLSN"
                     /gene_synonym="C7orf50; YCR016W"
                     /coded_by="NM_001424335.1:42..623"
                     /note="isoform b is encoded by transcript variant 28"
                     /db_xref="GeneID:84310"
                     /db_xref="HGNC:HGNC:22421"
                     /db_xref="MIM:621174"
ORIGIN      
        1 makqkrkvpe vtekknkklk kasaegpllg peaapsgega gskgeavlrp gldaepelsp
       61 eeqrvlerkl kkerkkeerq rlreaglvaq hpparrsgae laldylcrwa qkhknwrfqk
      121 trqtwlllhm ydsdkvpdeh fstllayleg lqgrareltv qkaealmrel deegsdpplp
      181 graqrirqtl lgr
//
LOCUS       NP_001394375            2871 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform n [Homo sapiens].
ACCESSION   NP_001394375
VERSION     NP_001394375.1
DBSOURCE    REFSEQ: accession NM_001407446.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2871)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2871)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2871)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2871)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2871)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2871)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2871)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2871)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2871)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2871)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3496861.1,
                                           SRR14038194.867857.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2871
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2871
                     /product="adenomatous polyposis coli protein isoform n"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=313790
     Region          137..217
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          350..402
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          403..476
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          500..536
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          540..581
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          544..581
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          591..623
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(614,618,622,661,665,669,706,710,714)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          631..672
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          677..717
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          681..715
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          719..759
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          723..759
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          760..1047
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          1064..1163
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1285..>1302
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1311..1396
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1319..1729
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1665..1688
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1690..1743
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1744..1765
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1774..1867
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1901..1975
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          2061..2080
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2251..2596
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2698..2871
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2871
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407446.1:221..8836"
                     /note="isoform n is encoded by transcript variant 16"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 myaslgsgpv aplpasvpps vlgswstggs rscvrqetks pggartsghw asvwqevlkq
       61 lqgsiedeam assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec
      121 spvpmgsfpr rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid
      181 slpltenfsl qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrriar iqqiekdilr
      241 irqllqsqat eaerssqnkh etgshdaerq negqgvgein matsgngqgs ttrmdhetas
      301 vlssssthsa prrltshlgt kvemvyslls mlgthdkddm srtllamsss qdscismrqs
      361 gclplliqll hgndkdsvll gnsrgskear arasaalhni ihsqpddkrg rreirvlhll
      421 eqiraycetc wewqeahepg mdqdknpmpa pvehqicpav cvlmklsfde ehrhamnelg
      481 rkatrgissq elgqglsggl qaiaellqvd cemygltndh ysitlrryag maltnltfgd
      541 vankatlcsm kgcmralvaq lksesedlqq viasvlrnls wradvnskkt lrevgsvkal
      601 mecalevkke stlksvlsal wnlsahcten kadicavdga laflvgtlty rsqtntlaii
      661 esgggilrnv ssliatnedh rqilrenncl qtllqhlksh sltivsnacg tlwnlsarnp
      721 kdqealwdmg avsmlknlih skhkmiamgs aaalrnlman rpakykdani mspgsslpsl
      781 hvrkqkalea eldaqhlset fdnidnlspk ashrskqrhk qslygdyvfd tnrhddnrsd
      841 nfntgnmtvl spylnttvlp sssssrgsld ssrsekdrsl erergiglgn yhpatenpgt
      901 sskrglqist taaqiakvme evsaihtsqe drssgsttel hcvtdernal rrssaahths
      961 ntynftksen snrtcsmpya kleykrssnd slnsvsssdg ygkrgqmkps iesyseddes
     1021 kfcsygqypa dlahkihsan hmddndgeld tpinyslkys deqlnsgrqs psqnerwarp
     1081 khiiedeikq seqrqsrnqs ttypvytest ddkhlkfqph fgqqecvspy rsrgangset
     1141 nrvgsnhgin qnvsqslcqe ddyeddkptn yseryseeeq heeeerptny sikyneekrh
     1201 vdqpidyslk yatdipssqk qsfsfsksss gqssktehms sssentstps snakrqnqlh
     1261 pssaqsrsgq pqkaatckvs sinqetiqty cvedtpicfs rcsslsslss aedeigcnqt
     1321 tqeadsantl qiaeikekig trsaedpvse vpavsqhprt kssrlqgssl ssesarhkav
     1381 efssgaksps ksgaqtpksp pehyvqetpl mfsrctsvss ldsfesrsia ssvqsepcsg
     1441 mvsgiispsd lpdspgqtmp psrsktpppp pqtaqtkrev pknkaptaek resgpkqaav
     1501 naavqrvqvl pdadtllhfa testpdgfsc ssslsalsld epfiqkdvel rimppvqend
     1561 ngneteseqp kesnenqeke aektidsekd llddsddddi eileeciisa mptkssrkak
     1621 kpaqtasklp ppvarkpsql pvykllpsqn rlqpqkhvsf tpgddmprvy cvegtpinfs
     1681 tatslsdlti esppnelaag egvrggaqsg efekrdtipt egrstdeaqg gktssvtipe
     1741 lddnkaeegd ilaecinsam pkgkshkpfr vkkimdqvqq asasssapnk nqldgkkkkp
     1801 tspvkpipqn teyrtrvrkn adsknnlnae rvfsdnkdsk kqnlknnskv fndklpnned
     1861 rvrgsfafds phhytpiegt pycfsrndsl ssldfddddv dlsrekaelr kakenkesea
     1921 kvtshtelts nqqsanktqa iakqpinrgq pkpilqkqst fpqsskdipd rgaatdeklq
     1981 nfaientpvc fshnsslssl sdidqennnk enepiketep pdsqgepskp qasgyapksf
     2041 hvedtpvcfs rnsslsslsi dseddllqec issampkkkk psrlkgdnek hsprnmggil
     2101 gedltldlkd iqrpdsehgl spdsenfdwk aiqegansiv sslhqaaaaa clsrqassds
     2161 dsilslksgi slgspfhltp dqeekpftsn kgprilkpge kstletkkie seskgikggk
     2221 kvykslitgk vrsnseisgq mkqplqanmp sisrgrtmih ipgvrnssss tspvskkgpp
     2281 lktpasksps egqtattspr gakpsvksel spvarqtsqi ggsskapsrs gsrdstpsrp
     2341 aqqplsrpiq spgrnsispg rngisppnkl sqlprtssps tastkssgsg kmsytspgrq
     2401 msqqnltkqt glsknassip rsesaskgln qmnngngank kvelsrmsst kssgsesdrs
     2461 erpvlvrqst fikeapsptl rrkleesasf eslspssrpa sptrsqaqtp vlspslpdms
     2521 lsthssvqag gwrklppnls ptieyndgrp akrhdiarsh sespsrlpin rsgtwkrehs
     2581 khssslprvs twrrtgssss ilsassesse kaksedekhv nsisgtkqsk enqvsakgtw
     2641 rkikenefsp tnstsqtvss gatngaeskt liyqmapavs ktedvwvrie dcpinnprsg
     2701 rsptgntppv idsvsekanp nikdskdnqa kqnvgngsvp mrtvglenrl nsfiqvdapd
     2761 qkgteikpgq nnpvpvsetn essivertpf sssssskhss psgtvaarvt pfnynpsprk
     2821 ssadstsarp sqiptpvnnn tkkrdsktds tessgtqspk rhsgsylvts v
//
LOCUS       NP_001425989            2561 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HECTD1 isoform 8 [Homo sapiens].
ACCESSION   NP_001425989 XP_047287157 XP_054231750
VERSION     NP_001425989.1
DBSOURCE    REFSEQ: accession NM_001439060.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2561)
  AUTHORS   Oxman,E., Li,H., Wang,H.Y. and Zohn,I.E.
  TITLE     Identification and functional analysis of rare HECTD1 missense
            variants in human neural tube defects
  JOURNAL   Hum Genet 143 (3), 263-277 (2024)
   PUBMED   38451291
  REMARK    GeneRIF: Identification and functional analysis of rare HECTD1
            missense variants in human neural tube defects.
REFERENCE   2  (residues 1 to 2561)
  AUTHORS   Zhang,J., Xin,Y., Ling,X., Liang,H., Zhang,L., Fang,C. and Ma,J.
  TITLE     Nucleoporin 93, a new substrate of the E3 ubiquitin protein ligase
            HECTD1, promotes esophageal squamous cell carcinoma progression
  JOURNAL   Hum Cell 37 (1), 245-257 (2024)
   PUBMED   37993750
  REMARK    GeneRIF: Nucleoporin 93, a new substrate of the E3 ubiquitin
            protein ligase HECTD1, promotes esophageal squamous cell carcinoma
            progression.
REFERENCE   3  (residues 1 to 2561)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 2561)
  AUTHORS   Vaughan,N., Scholz,N., Lindon,C. and Licchesi,J.D.F.
  TITLE     The E3 ubiquitin ligase HECTD1 contributes to cell proliferation
            through an effect on mitosis
  JOURNAL   Sci Rep 12 (1), 13160 (2022)
   PUBMED   35915203
  REMARK    GeneRIF: The E3 ubiquitin ligase HECTD1 contributes to cell
            proliferation through an effect on mitosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2561)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 2561)
  AUTHORS   Aleidi,S.M., Yang,A., Sharpe,L.J., Rao,G., Cochran,B.J., Rye,K.A.,
            Kockx,M., Brown,A.J. and Gelissen,I.C.
  TITLE     The E3 ubiquitin ligase, HECTD1, is involved in ABCA1-mediated
            cholesterol export from macrophages
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1863 (4), 359-368 (2018)
   PUBMED   29306077
  REMARK    GeneRIF: HECTD1 may be involved in the regulation of ABCA1-mediated
            cholesterol export from unloaded macrophages to apoA-I.
REFERENCE   7  (residues 1 to 2561)
  AUTHORS   Fang,S., Guo,H., Cheng,Y., Zhou,Z., Zhang,W., Han,B., Luo,W.,
            Wang,J., Xie,W. and Chao,J.
  TITLE     circHECTD1 promotes the silica-induced pulmonary
            endothelial-mesenchymal transition via HECTD1
  JOURNAL   Cell Death Dis 9 (3), 396 (2018)
   PUBMED   29540674
  REMARK    GeneRIF: SiO2 concomitantly increased circHECTD1 expression, which,
            in turn, inhibited HECTD1 protein expression.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 2561)
  AUTHORS   Shen,X., Jia,Z., D'Alonzo,D., Wang,X., Bruder,E., Emch,F.H., De
            Geyter,C. and Zhang,H.
  TITLE     HECTD1 controls the protein level of IQGAP1 to regulate the
            dynamics of adhesive structures
  JOURNAL   Cell Commun Signal 15 (1), 2 (2017)
   PUBMED   28073378
  REMARK    GeneRIF: Hectd1 regulates the protein level of IQGAP1 through
            ubiquitination.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 2561)
  AUTHORS   Helander,S., Montecchio,M., Lemak,A., Fares,C., Almlof,J., Yi,Y.,
            Yee,A., Arrowsmith,C., DhePaganon,S. and Sunnerhagen,M.
  TITLE     Basic Tilted Helix Bundle - a new protein fold in human
            FKBP25/FKBP3 and HectD1
  JOURNAL   Biochem Biophys Res Commun 447 (1), 26-31 (2014)
   PUBMED   24667607
  REMARK    GeneRIF: our high-resolution structures show a new fold composed of
            five small helices where H3 and H4 are tilted in a novel
            arrangement; we call this fold the Basic Tilted Helix Bundle (BTHB)
            domain.
REFERENCE   10 (residues 1 to 2561)
  AUTHORS   Tran,H., Bustos,D., Yeh,R., Rubinfeld,B., Lam,C., Shriver,S.,
            Zilberleyb,I., Lee,M.W., Phu,L., Sarkar,A.A., Zohn,I.E.,
            Wertz,I.E., Kirkpatrick,D.S. and Polakis,P.
  TITLE     HectD1 E3 ligase modifies adenomatous polyposis coli (APC) with
            polyubiquitin to promote the APC-axin interaction
  JOURNAL   J Biol Chem 288 (6), 3753-3767 (2013)
   PUBMED   23277359
  REMARK    GeneRIF: HectD1 promotes the APC-Axin interaction to negatively
            regulate Wnt signaling.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136418.4, AL121808.4 and KC877516.1.
            
            On or before Apr 25, 2025 this sequence version replaced
            XP_047287157.1, XP_054231750.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3833449.1,
                                           SRR14372079.2326133.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2561
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..2561
                     /product="E3 ubiquitin-protein ligase HECTD1 isoform 8"
                     /EC_number="2.3.2.26"
                     /note="E3 ubiquitin-protein ligase HECTD1; E3 ligase for
                     inhibin receptor; HECT domain-containing protein 1; HECT
                     domain containing E3 ubiquitin protein ligase 1; HECT-type
                     E3 ubiquitin transferase HECTD1"
                     /calculated_mol_wt=284095
     Region          246..269
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          <366..>479
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          366..393
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          395..424
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          396..426
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(397,401..402,405..407,409..410,414,417,426,428,
                     432..433,436..438,440..441,445,448,457,459,461,465..466,
                     469..471,473..474,478)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          426..455
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          428..457
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          459..491
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          489..513
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          579..612
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          627..657
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZR2; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          707..748
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1107..1240
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     Region          1277..>1321
                     /region_name="MIB_HERC2"
                     /note="Mib_herc2; pfam06701"
                     /db_xref="CDD:461991"
     Site            1337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZR2; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1386..1436
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1449..1468
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZR2; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1545..1564
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1711
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1723
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1728..1748
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1844..1909
                     /region_name="BTHB_HectD1"
                     /note="basic tilted helix bundle (BTHB) domain found in
                     HECT domain-containing protein 1 (HectD1) and similar
                     proteins; cd21062"
                     /db_xref="CDD:439138"
     Region          1980..2054
                     /region_name="K-box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          2082..2559
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(2088,2117,2127,2214,2492,2524..2525,2528..2532,2552,
                     2558)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Region          2248..2269
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            2269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            order(2307,2310..2311,2313..2314,2317,2359,2361,
                     2365..2366,2368,2374,2379,2396,2400)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..2561
                     /gene="HECTD1"
                     /gene_synonym="EULIR"
                     /coded_by="NM_001439060.1:425..8110"
                     /note="isoform 8 is encoded by transcript variant 9"
                     /db_xref="GeneID:25831"
                     /db_xref="HGNC:HGNC:20157"
                     /db_xref="MIM:618649"
ORIGIN      
        1 madvdpdtll ewlqmgqgde rdmqlialeq lcmlllmsdn vdrcfetcpp rtflpalcki
       61 fldesapdnv levtaraity yldvsaectr rivgvdgaik alcnrlvvve lnnrtsrdla
      121 eqcvkvleli ctresgavfe agglncvltf irdsghlvhk dtlhsamavv srlcgkmepq
      181 dssleicves lssllkhedh qvsdgalrcf asladrftrr gvdpaplakh glteellsrm
      241 aaaggtvsgp ssackpgrst tgapsttads klsnqvstiv sllstlcrgs pvvthdllrs
      301 elpdsiesal qgdercvldt mrlvdlllvl lfegrkalpk ssagstgrip glrrldssge
      361 rshrqlidci rskdtdalid aidtgafevn fmddvgqtll nwasafgtqe mveflcerga
      421 dvnrgqrsss lhyaacfgrp qvaktllrhg anpdlrdedg ktpldkarer ghsevvailq
      481 spgdwmcpvn kgddkkkkdt nkdeeecnep kgdpemapiy lkrllpvfaq tfqqtmlpsi
      541 rkaslalirk mihfcseall kevcdsdvgh nlptilveit atvldqeddd dghllalqii
      601 rdlvdkggdi fldqlarlgv iskvstlagp ssddeneees kpekedepqe dakelqqgkp
      661 yhwrdwsiir grdclyiwsd aaalelsngs ngwfrfildg klatmyssgs peggsdsses
      721 rsefleklqr argqvkpsts sqpilsapgp tkltvgnwsl tclkegeiai hnsdgqqati
      781 lkedlpgfvf esnrgtkhsf taetslgsef vtgwtgkrgr klksklektk qkvrtmardl
      841 yddhfkaves mprgvvvtlr niatqlessw elhtnrqcie sentwrdlmk talenlivll
      901 kdentispye mcssglvqal ltvlnnsmdl dmkqdcsqlv erinvfktaf seneddesrp
      961 avalirklia vlesierlpl hlydtpgsty nlqiltrrlr frlerapget alidrtgrml
     1021 kmeplatves leqyllkmva kqwydfdrss fvfvrklreg qnfifrhqhd fdengiiywi
     1081 gtnaktayew vnpaayglvv vtssegrnlp ygrledilsr dnsalnchsn ddknawfaid
     1141 lglwvipsay tlrhargygr salrnwvfqv skdgqnwtsl ythvddcsln epgstatwpl
     1201 dppkdekqgw rhvrikqmgk nasgqthyls lsgfelygtv ngvcedqlgk aakeaeanlr
     1261 rqrrlvrsqv lkymvpgarv irgldwkwrd qdgspqgegt vtgelhngtt qswsslvknn
     1321 cpdktsaaag sssrkgssss vcsvasssdi slgstkterr seivmehsiv sgadvhepiv
     1381 vlssaenvpq tevgssssas tstltaetgs enaerklgpd ssvrtpgess aismgivsvs
     1441 spdvssvsel tnkeaasqrp lsssasnrls vssllaagap msssasvpnl ssretssles
     1501 fvrrvaniar tnatnnmnls rsssdnntnt lgrnvmstat splmgaqsfp nlttpgttst
     1561 vtmstssvts ssnvatattv lsvgqslsnt lttsltstss esdtgqeaey slydfldscr
     1621 astllaeldd dedlpepdee ddeneddnqe dqeyeeilrr pslqrragsr sdvthhavts
     1681 qlpqvpagag srpigeqeee eyetkggrrr twdddyvlkr qfsalvpafd prpgrtnvqq
     1741 ttdleipppg tphselleev ectpsprlal tlkvtglgtt revelpltnf rstifyyvqk
     1801 llqlscngnv ksdklrriwe ptytimyrem kdsdkekeng kmgcwsiehv eqylgtdelp
     1861 kndlitylqk nadaaflrhw kltgtnksir knrncsqlia aykdfcehgt ksglnqgais
     1921 tlqssdilnl tkeqpqakag ngqnscgved vlqllrilyi vasdpysris qedgdeqpqf
     1981 tfppdeftsk kittkilqqi eeplalasga lpdwceqlts kcpflipfet rqlyftctaf
     2041 gasraivwlq nrreatvert rttssvrrdd pgefrvgrlk hervkvprge slmewaenvm
     2101 qihadrksvl eveflgeegt glgptlefya lvaaefqrtd lgawlcddnf pddesrhvdl
     2161 ggglkppgyy vqrscglfta pfpqdsdele ritklfhflg iflakciqdn rlvdlpiskp
     2221 ffklmcmgdi ksnmskliye srgdrdlhct esqseastee ghdslsvgsf eedsksefil
     2281 dppkpkppaw fngiltwedf elvnphrarf lkeikdlaik rrqilsnkgl sedekntklq
     2341 elvlknpsgs gpplsiedlg lnfqfcpssr iygftavdlk psgedemitm dnaeeyvdlm
     2401 fdfcmhtgiq kqmeafrdgf nkvfpmekls sfsheevqmi lcgnqspswa aediinytep
     2461 klgytrdspg flrfvrvlcg mssderkafl qfttgcstlp pgglanlhpr ltvvrkvdat
     2521 dasypsvntc vhylklpeys seeimrerll aatmekgfhl n
//
LOCUS       NP_001397630             708 aa            linear   PRI 21-NOV-2025
DEFINITION  interleukin-1 receptor-associated kinase 1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001397630 XP_005274725
VERSION     NP_001397630.1
DBSOURCE    REFSEQ: accession NM_001410701.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Rao,Z., Ao,G., Zhang,Y., Jiang,Z., Li,L. and Hua,Z.
  TITLE     HNRNP I promotes IRAK1 degradation to reduce podocyte apoptosis and
            inflammatory response alleviating renal injury in diabetic
            nephropathy
  JOURNAL   Immunobiology 229 (5), 152835 (2024)
   PUBMED   38986278
  REMARK    GeneRIF: HNRNP I promotes IRAK1 degradation to reduce podocyte
            apoptosis and inflammatory response alleviating renal injury in
            diabetic nephropathy.
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Fisch,D., Zhang,T., Sun,H., Ma,W., Tan,Y., Gygi,S.P., Higgins,D.E.
            and Kagan,J.C.
  TITLE     Molecular definition of the endogenous Toll-like receptor
            signalling pathways
  JOURNAL   Nature 631 (8021), 635-644 (2024)
   PUBMED   38961291
REFERENCE   3  (residues 1 to 708)
  AUTHORS   Chen,J.J., Lu,T.Z., Wang,T., Yan,W.H., Zhong,F.Y., Qu,X.H.,
            Gong,X.C., Li,J.G., Tou,F.F., Jiang,L.P. and Han,X.J.
  TITLE     The m6A reader HNRNPC promotes glioma progression by enhancing the
            stability of IRAK1 mRNA through the MAPK pathway
  JOURNAL   Cell Death Dis 15 (6), 390 (2024)
   PUBMED   38830885
  REMARK    GeneRIF: The m6A reader HNRNPC promotes glioma progression by
            enhancing the stability of IRAK1 mRNA through the MAPK pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 708)
  AUTHORS   Liu,Y., Yuan,J., Zhang,Y., Qin,F., Bai,X., Sun,W., Chen,T., Liu,F.,
            Zheng,Y., Qi,X., Zhao,W., Liu,B. and Gao,C.
  TITLE     OTUD5 promotes the inflammatory immune response by enhancing MyD88
            oligomerization and Myddosome formation
  JOURNAL   Cell Death Differ 31 (6), 753-767 (2024)
   PUBMED   38605168
REFERENCE   5  (residues 1 to 708)
  AUTHORS   Zhou,M., Liu,Y., Xu,H., Chen,X., Zheng,N., Duan,Z., Ge,Y., Li,D.,
            Lin,T., Zeng,R., Chen,Q. and Li,M.
  TITLE     YTHDC1-Modified m6A Methylation of Hsa_circ_0102678 Promotes
            Keratinocyte Inflammation Induced by Cutibacterium acnes Biofilm
            through Regulating miR-146a/TRAF6 and IRAK1 Axis
  JOURNAL   J Innate Immun 15 (1), 822-835 (2023)
   PUBMED   37903473
  REMARK    GeneRIF: YTHDC1-Modified m6A Methylation of Hsa_circ_0102678
            Promotes Keratinocyte Inflammation Induced by Cutibacterium acnes
            Biofilm through Regulating miR-146a/TRAF6 and IRAK1 Axis.
REFERENCE   6  (residues 1 to 708)
  AUTHORS   Muzio,M., Ni,J., Feng,P. and Dixit,V.M.
  TITLE     IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators
            of IL-1 signaling
  JOURNAL   Science 278 (5343), 1612-1615 (1997)
   PUBMED   9374458
REFERENCE   7  (residues 1 to 708)
  AUTHORS   Huang,J., Gao,X., Li,S. and Cao,Z.
  TITLE     Recruitment of IRAK to the interleukin 1 receptor complex requires
            interleukin 1 receptor accessory protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (24), 12829-12832 (1997)
   PUBMED   9371760
REFERENCE   8  (residues 1 to 708)
  AUTHORS   DiDonato,J.A., Hayakawa,M., Rothwarf,D.M., Zandi,E. and Karin,M.
  TITLE     A cytokine-responsive IkappaB kinase that activates the
            transcription factor NF-kappaB
  JOURNAL   Nature 388 (6642), 548-554 (1997)
   PUBMED   9252186
REFERENCE   9  (residues 1 to 708)
  AUTHORS   Cao,Z., Xiong,J., Takeuchi,M., Kurama,T. and Goeddel,D.V.
  TITLE     TRAF6 is a signal transducer for interleukin-1
  JOURNAL   Nature 383 (6599), 443-446 (1996)
   PUBMED   8837778
REFERENCE   10 (residues 1 to 708)
  AUTHORS   Cao,Z., Henzel,W.J. and Gao,X.
  TITLE     IRAK: a kinase associated with the interleukin-1 receptor
  JOURNAL   Science 271 (5252), 1128-1131 (1996)
   PUBMED   8599092
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U52112.2.
            
            On Aug 15, 2022 this sequence version replaced XP_005274725.1.
            
            Summary: This gene encodes the interleukin-1 receptor-associated
            kinase 1, one of two putative serine/threonine kinases that become
            associated with the interleukin-1 receptor (IL1R) upon stimulation.
            This gene is partially responsible for IL1-induced upregulation of
            the transcription factor NF-kappa B. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1235632.1,
                                           SRR14038192.2667896.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..708
                     /product="interleukin-1 receptor-associated kinase 1
                     isoform 4"
                     /EC_number="2.7.11.1"
                     /note="Pelle homolog"
                     /calculated_mol_wt=75929
     Region          17..126
                     /region_name="Death_IRAK1"
                     /note="Death domain of Interleukin 1 Receptor Associated
                     Kinase-1; cd08794"
                     /db_xref="CDD:260061"
     Site            order(19..20,22..25,84,93..94,97..103,108)
                     /site_type="other"
                     /note="putative IRAK1-IRAK4 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:260061"
     Region          244..539
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(244..247,250,252,263,265,298,314..317,366,370..371,
                     373,383..384)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..708
                     /gene="IRAK1"
                     /gene_synonym="IRAK; pelle"
                     /coded_by="NM_001410701.1:91..2217"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS94700.1"
                     /db_xref="GeneID:3654"
                     /db_xref="HGNC:HGNC:6112"
                     /db_xref="MIM:300283"
ORIGIN      
        1 maggpgpgep aapgaqhfly evppwvmcrf ykvmdalepa dwcqfggwrr aaggreargl
       61 laptpdaprp aaalivrdqt elrlcersgq rtasvlwpwi nrnarvadlv hilthlqllr
      121 ardiitawhp paplpspgtt aprpssipap aeaeawsprk lpssastfls pafpgsqths
      181 gpelglvpsp aslwppppsp apsstkpgpe ssvsllqgar pfpfcwplce isrgthnfse
      241 elkigeggfg cvyravmrnt vyavkrlken adlewtavkq sflteveqls rfrhpnivdf
      301 agycaqngfy clvygflpng sledrlhcqt qacpplswpq rldillgtar aiqflhqdsp
      361 slihgdikss nvllderltp klgdfglarf srfagsspsq ssmvartqtv rgtlaylpee
      421 yiktgrlavd tdtfsfgvvv letlagqrav kthgartkyl kdlveeeaee agvalrstqs
      481 tlqaglaada waapiamqiy kkhldprpgp cppelglglg qlaccclhrr akrrppmtqe
      541 nsyvsstgra hsgaapwqpl aapsgasaqa aeqlqrgpnq pvesdeslgg lsaalrswhl
      601 tpscpldpap lreagcpqgd tagesswgsg pgsrptaveg lalgssasss seppqiiinp
      661 arqkmvqkla lyedgaldsl qllsssslpg lgleqdrqgp eesdefqs
//
LOCUS       NP_001401619             497 aa            linear   PRI 21-NOV-2025
DEFINITION  nucleolar complex protein 4 homolog isoform 4 [Homo sapiens].
ACCESSION   NP_001401619
VERSION     NP_001401619.1
DBSOURCE    REFSEQ: accession NM_001414690.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Talebi,A., Shahidsales,S., Aliakbarian,M., Pezeshki Rad,M. and
            Kerachian,M.A.
  TITLE     Oncogenic fusion transcript analysis identified ADAP1-NOC4L,
            potentially associated with metastatic colorectal cancer
  JOURNAL   Cancer Med 12 (1), 525-540 (2023)
   PUBMED   35702822
  REMARK    GeneRIF: Oncogenic fusion transcript analysis identified
            ADAP1-NOC4L, potentially associated with metastatic colorectal
            cancer.
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Qin,Y., Li,H., Jia,L., Yan,J., Gao,G.F. and Li,X.
  TITLE     Targeted disruption of Noc4l leads to preimplantation embryonic
            lethality in mice
  JOURNAL   Protein Cell 8 (3), 230-235 (2017)
   PUBMED   28012024
  REMARK    GeneRIF: The results provide the first in vivo genetic evidence
            that Noc4l plays important roles in early embryogenesis in mice.
REFERENCE   5  (residues 1 to 497)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 497)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 497)
  AUTHORS   Bernstein,K.A., Gallagher,J.E., Mitchell,B.M., Granneman,S. and
            Baserga,S.J.
  TITLE     The small-subunit processome is a ribosome assembly intermediate
  JOURNAL   Eukaryot Cell 3 (6), 1619-1626 (2004)
   PUBMED   15590835
REFERENCE   8  (residues 1 to 497)
  AUTHORS   Milkereit,P., Strauss,D., Bassler,J., Gadal,O., Kuhn,H., Schutz,S.,
            Gas,N., Lechner,J., Hurt,E. and Tschochner,H.
  TITLE     A Noc complex specifically involved in the formation and nuclear
            export of ribosomal 40 S subunits
  JOURNAL   J Biol Chem 278 (6), 4072-4081 (2003)
   PUBMED   12446671
REFERENCE   9  (residues 1 to 497)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC138466.12.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1030308.1,
                                           SRR18074968.3447644.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.33"
     Protein         1..497
                     /product="nucleolar complex protein 4 homolog isoform 4"
                     /note="nucleolar complex protein 4 homolog; NOC4-like
                     protein; NOC4 protein homolog; nucleolar
                     complex-associated protein 4-like protein"
                     /calculated_mol_wt=56358
     Region          291..433
                     /region_name="CBF"
                     /note="CBF/Mak21 family; pfam03914"
                     /db_xref="CDD:461090"
     CDS             1..497
                     /gene="NOC4L"
                     /gene_synonym="NET49; NOC4; UTP19"
                     /coded_by="NM_001414690.1:33..1526"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:79050"
                     /db_xref="HGNC:HGNC:28461"
                     /db_xref="MIM:612819"
ORIGIN      
        1 merepgaagv rralgrrlea vlasrseana vfdilavlqs edqeeiqeav rtcsrlfgal
       61 lergelfvgq lpseemvmtg sqgatrkykv wmrhryhscc nrlgellghp sfqvkelals
      121 allkfvqleg ahplekskwe gnylfprelf kfreyldydd tryhtmqaav davarvtgqh
      181 pevppafwnn aftllsavsl prreptvssf yvkraelwdt wkvahlkehr rvfqamwlsf
      241 lkhklplsly kkvllivhda ilpqlaqptl midfltracd lggalsllal nglfilihkh
      301 nleypdfyrk lyglldpsvf hvkyrarffh ladlflsssh lpaylvaafa krlarlalta
      361 ppeallmvlp ficnllrrhp acrvlvhrph gpeldadpyd pgeedpaqsr alesslwelq
      421 alqrhyhpev skaasvinqa lsmpevsiap lleltayeif erdlkkkgpe pvplefipaq
      481 gllgrpgelc aqhftls
//
LOCUS       NP_001394260             284 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 31 [Homo sapiens].
ACCESSION   NP_001394260 XP_006720730
VERSION     NP_001394260.1
DBSOURCE    REFSEQ: accession NM_001407331.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            On May 31, 2022 this sequence version replaced XP_006720730.3.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853561.10116.1,
                                           SRR14038191.3290652.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..284
                     /product="tropomyosin alpha-1 chain isoform 31"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=32717
     Region          48..282
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..284
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407331.1:84..938"
                     /note="isoform 31 is encoded by transcript variant 31"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle delvslqkkl kgtedeldky
       61 sealkdaqek lelaekkatd aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegqv rqleeqlrim dqtlkalmaa edkysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledel yaqklkykai seeldhalnd mtsi
//
LOCUS       NP_001393557             846 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 15 [Homo sapiens].
ACCESSION   NP_001393557
VERSION     NP_001393557.1
DBSOURCE    REFSEQ: accession NM_001406628.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 846)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 846)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 846)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 846)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 846)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 846)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 846)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 846)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2217070.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..846
                     /product="hamartin isoform 15"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=93697
     Region          <1..401
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <390..>642
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..846
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406628.1:1095..3635"
                     /note="isoform 15 is encoded by transcript variant 42"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mllnmpgqlp qtlsspstrl iteppqatlw spsmvcgmtt pptspgnvpp dlshpyskvf
       61 gttggkgtpl gtpatspppa plchsddyvh islpqatvtp prkeermdsa rpclhrqhhl
      121 lndrgseepp gskgsvtlsd lpgflgdlas eedsiekdke eaaisrelse ittaeaepvv
      181 prggfdspfy rdslpgsqrk thsaasssqg asvnpeplhs sldklgpdtp kqaftpidlp
      241 cgsadespag drecqtslet siftpspcki ppptrvgfgs gqpppydhlf evalpktahh
      301 fvirkteell kkakgnteed gvpstspmev ldrliqqgad ahskelnklp lpsksvdwth
      361 fggsppsdei rtlrdqllll hnqllyerfk rqqhalrnrr llrkvikaaa leehnaamkd
      421 qlklqekdiq mwkvslqkeq arynqlqeqr dtmvtklhsq irqlqhdree fynqsqelqt
      481 kledcrnmia elrielkkan nkvchtelll sqvsqklsns esvqqqmefl nrqllvlgev
      541 nelyleqlqn khsdttkeve mmkaayrkel eknrshvlqq tqrldtsqkr ileleshlak
      601 kdhllleqkk yledvklqar gqlqaaesry eaqkritqvf eleildlygr lekdgllkkl
      661 eeekaeaaea aeerldccnd gcsdsmvghn eeasghnget ktprpssarg ssgsrggggs
      721 ssssselstp ekpphqragp fssrwettmg easasipttv gslpssksfl gmkarelfrn
      781 ksesqcdedg mtsslseslk telgkdlgve akiplnldgp hpspptpdsv gqlhimdyne
      841 thhehs
//
LOCUS       NP_001424924            1011 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 3 isoform 3 [Homo sapiens].
ACCESSION   NP_001424924 XP_005247846 XP_054203917
VERSION     NP_001424924.1
DBSOURCE    REFSEQ: accession NM_001437995.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Wang,H., Lan,S., Wang,L., Zhao,J., Jia,X., Xu,J., Sun,G., Liu,L.,
            Gong,S., Wang,N., Shan,B., Zhang,F. and Zhang,Z.
  TITLE     Expression of circ-PHC3 enhances ovarian cancer progression via
            regulation of the miR-497-5p/SOX9 pathway
  JOURNAL   J Ovarian Res 16 (1), 142 (2023)
   PUBMED   37468993
  REMARK    GeneRIF: Expression of circ-PHC3 enhances ovarian cancer
            progression via regulation of the miR-497-5p/SOX9 pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1011)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1011)
  AUTHORS   Crea,F., Di Paolo,A., Liu,H.H., Polillo,M., Clermont,P.L.,
            Guerrini,F., Ciabatti,E., Ricci,F., Barate,C., Fontanelli,G.,
            Barsotti,S., Morganti,R., Danesi,R., Wang,Y., Petrini,M.,
            Galimberti,S. and Helgason,C.D.
  TITLE     Polycomb genes are associated with response to imatinib in chronic
            myeloid leukemia
  JOURNAL   Epigenomics 7 (5), 757-765 (2015)
   PUBMED   26343356
  REMARK    GeneRIF: Data show that polycomb-group proteins BMI1, PHC3, CBX6
            and CBX7 expression was significantly increased during imatinib
            treatment.
REFERENCE   6  (residues 1 to 1011)
  AUTHORS   Deshpande,A.M., Akunowicz,J.D., Reveles,X.T., Patel,B.B.,
            Saria,E.A., Gorlick,R.G., Naylor,S.L., Leach,R.J. and Hansen,M.F.
  TITLE     PHC3, a component of the hPRC-H complex, associates with E2F6
            during G0 and is lost in osteosarcoma tumors
  JOURNAL   Oncogene 26 (12), 1714-1722 (2007)
   PUBMED   17001316
  REMARK    GeneRIF: loss of PHC3 may favor tumorigenesis by potentially
            disrupting the ability of cells to remain in G(0)
REFERENCE   7  (residues 1 to 1011)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   8  (residues 1 to 1011)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 1011)
  AUTHORS   Tonkin,E., Hagan,D.M., Li,W. and Strachan,T.
  TITLE     Identification and characterisation of novel mammalian homologues
            of Drosophila polyhomeoticpermits new insights into relationships
            between members of the polyhomeotic family
  JOURNAL   Hum Genet 111 (4-5), 435-442 (2002)
   PUBMED   12384788
REFERENCE   10 (residues 1 to 1011)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC023891.28 and AC008040.7.
            
            On or before Apr 14, 2025 this sequence version replaced
            XP_005247846.1, XP_054203917.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1987722.1,
                                           SRR14038194.1556663.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.2"
     Protein         1..1011
                     /product="polyhomeotic-like protein 3 isoform 3"
                     /note="early development regulator 3; polyhomeotic-like
                     protein 3; homolog of polyhomeotic 3; early development
                     regulatory protein 3; polyhomeotic like 3"
                     /calculated_mol_wt=109224
     Region          356..>596
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          942..1010
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(960..961,995..996,999..1000,1003)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(971..975,977..978,981..982,986,991)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..1011
                     /gene="PHC3"
                     /gene_synonym="EDR3; HPH3"
                     /coded_by="NM_001437995.1:19..3054"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:80012"
                     /db_xref="HGNC:HGNC:15682"
                     /db_xref="MIM:620031"
ORIGIN      
        1 maeaefkdhs tamdtepnpg tssvstttss tttttittss srmqqpqisv ysgsdrhavq
       61 viqqalhrpp ssaaqylqqm yaaqqqhlml htaalqqqhl sssqlqslaa vqaslssgrp
      121 stsptgsvtq qssmsqtsin lstsptpaql isrsqassst sgsitqqtml lgstsptlta
      181 sqaqmylraq mliftpattv aavqsdipvv ssssssscqs aatqvqnltl rsqklgvlss
      241 sqngppksts qtqsltichn kttvtsskis qrdpspesnk kgespslesr stavtrtssi
      301 hqliapasys piqphslikh qqiplhspps kvshhqlilq qqqqqiqpit lqnstqdppp
      361 sqhciplqnh glppapsnaq sqhcspiqsh pspltvspnq sqsaqqsvvv spppphspsq
      421 sptiiihpqa liqphplvss alqpgpnlqq stanqvqata qlnlpshlpl paspvvhigp
      481 vqqsalvspg qqivspshqq ysslqsspip iasppqmsts ppaqipplpl qsmqslqvqp
      541 eilsqgqvlv qnalvseeel paaealvqlp fqtlpppqtv avnlqvqppa pvdppvgmhl
      601 nqchlhkvfs lkvyqvedvc eeempeesde cvrmdrtppp ptlspaaitv grgedltseh
      661 plleqvelpa vasvsasvik spsdpshvsv pppplllpaa ttrsnstsmh ssipsienkp
      721 pqaivkpqil thviegfviq eglepfpvsr ssllieqpvk krplldnqvi nsvcvqpelq
      781 nntkhadnss dtemedmiae etleemdsel lkcefcgkmg yaneflrskr fctmscakry
      841 nvscskkfal srwnrkpdnq slghrgrrps gpdgaarehi lrqlpityps aeedlashed
      901 svpsamttrl rrqsererer elrdvrirkm pensdllpva qtepsiwtvd dvwafihslp
      961 gcqdiadefr aqeidgqall llkedhlmsa mniklgpalk icarinslke s
//
LOCUS       NP_001171596             329 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 1 isoform l [Homo sapiens].
ACCESSION   NP_001171596
VERSION     NP_001171596.1
DBSOURCE    REFSEQ: accession NM_001178125.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Petersen,M. and Dubielecka,P.
  TITLE     Adaptor protein Abelson interactor 1 in homeostasis and disease
  JOURNAL   Cell Commun Signal 22 (1), 468 (2024)
   PUBMED   39354505
  REMARK    GeneRIF: Adaptor protein Abelson interactor 1 in homeostasis and
            disease.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Jin,M., Xie,M., Liu,Y., Song,H., Zhang,M., Li,W., Li,X., Jia,N.,
            Dong,L., Lu,Q., Xue,F., Yan,L. and Yu,Q.
  TITLE     Circulating miR-30e-3p induces disruption of neurite development in
            SH-SY5Y cells by targeting ABI1, a novel biomarker for
            schizophrenia
  JOURNAL   J Psychiatr Res 174, 84-93 (2024)
   PUBMED   38626565
  REMARK    GeneRIF: Circulating miR-30e-3p induces disruption of neurite
            development in SH-SY5Y cells by targeting ABI1, a novel biomarker
            for schizophrenia.
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Lin,T., Guo,J., Peng,Y., Li,M., Liu,Y., Yu,X., Wu,N. and Yu,W.
  TITLE     Pan-cancer transcriptomic data of ABI1 transcript variants and
            molecular constitutive elements identifies novel cancer metastatic
            and prognostic biomarkers
  JOURNAL   Cancer Biomark 39 (1), 49-62 (2024)
   PUBMED   37545215
  REMARK    GeneRIF: Pan-cancer transcriptomic data of ABI1 transcript variants
            and molecular constitutive elements identifies novel cancer
            metastatic and prognostic biomarkers.
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Fan,P.D. and Goff,S.P.
  TITLE     Abl interactor 1 binds to sos and inhibits epidermal growth factor-
            and v-Abl-induced activation of extracellular signal-regulated
            kinases
  JOURNAL   Mol Cell Biol 20 (20), 7591-7601 (2000)
   PUBMED   11003655
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   7  (residues 1 to 329)
  AUTHORS   Scita,G., Nordstrom,J., Carbone,R., Tenca,P., Giardina,G.,
            Gutkind,S., Bjarnegard,M., Betsholtz,C. and Di Fiore,P.P.
  TITLE     EPS8 and E3B1 transduce signals from Ras to Rac
  JOURNAL   Nature 401 (6750), 290-293 (1999)
   PUBMED   10499589
REFERENCE   8  (residues 1 to 329)
  AUTHORS   Taki,T., Shibuya,N., Taniwaki,M., Hanada,R., Morishita,K.,
            Bessho,F., Yanagisawa,M. and Hayashi,Y.
  TITLE     ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL
            gene in acute myeloid leukemia with t(10;11)(p11.2;q23)
  JOURNAL   Blood 92 (4), 1125-1130 (1998)
   PUBMED   9694699
REFERENCE   9  (residues 1 to 329)
  AUTHORS   Ziemnicka-Kotula,D., Xu,J., Gu,H., Potempska,A., Kim,K.S.,
            Jenkins,E.C., Trenkner,E. and Kotula,L.
  TITLE     Identification of a candidate human spectrin Src homology 3
            domain-binding protein suggests a general mechanism of association
            of tyrosine kinases with the spectrin-based membrane skeleton
  JOURNAL   J Biol Chem 273 (22), 13681-13692 (1998)
   PUBMED   9593709
REFERENCE   10 (residues 1 to 329)
  AUTHORS   Biesova,Z., Piccoli,C. and Wong,W.T.
  TITLE     Isolation and characterization of e3B1, an eps8 binding protein
            that regulates cell growth
  JOURNAL   Oncogene 14 (2), 233-241 (1997)
   PUBMED   9010225
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK298646.1 and AL390961.17.
            
            Summary: This gene encodes a member of the Abelson-interactor
            family of adaptor proteins. These proteins facilitate signal
            transduction as components of several multiprotein complexes, and
            regulate actin polymerization and cytoskeletal remodeling through
            interactions with Abelson tyrosine kinases. The encoded protein
            plays a role in macropinocytosis as a component of the WAVE2
            complex, and also forms a complex with EPS8 and SOS1 that mediates
            signal transduction from Ras to Rac. This gene may play a role in
            the progression of several malignancies including melanoma, colon
            cancer and breast cancer, and a t(10;11) chromosomal translocation
            involving this gene and the MLL gene has been associated with acute
            myeloid leukemia. Alternatively spliced transcript variants
            encoding multiple isoforms have been observed for this gene, and a
            pseudogene of this gene is located on the long arm of chromosome
            14. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (12) lacks five alternate in-frame
            coding exons, compared to variant 1. The resulting protein (isoform
            l) has the same N- and C-termini but is shorter when it is compared
            to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK298646.1, SRR14038192.2274489.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.1"
     Protein         1..329
                     /product="abl interactor 1 isoform l"
                     /note="nap1 binding protein; interactor protein AblBP4;
                     Abl-interactor protein 1 long; Abelson interactor 1;
                     abl-binding protein 4; eps8 SH3 domain-binding protein;
                     spectrin SH3 domain-binding protein 1"
                     /calculated_mol_wt=35789
     Region          271..329
                     /region_name="SH3_Abi1"
                     /note="Src homology 3 domain of Abl Interactor 1; cd11971"
                     /db_xref="CDD:212904"
     Site            order(276,278,281,285,303..304,317,319..320)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212904"
     CDS             1..329
                     /gene="ABI1"
                     /gene_synonym="ABI-1; ABLBP4; E3B1; NAP1BP; SSH3BP;
                     SSH3BP1"
                     /coded_by="NM_001178125.2:96..1085"
                     /note="isoform l is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS53497.1"
                     /db_xref="GeneID:10006"
                     /db_xref="HGNC:HGNC:11320"
                     /db_xref="MIM:603050"
ORIGIN      
        1 maelqmllee eipsgkrali esyqnltrva dycennyiqa tdkrkaleet kayttqslas
       61 vayqinalan nvlqlldiqa sqlrrmessi nhisqhgnnq partgtlsrt npptqkppsp
      121 pmsgrgtlgr ntpyktlepv kpptvpndym tsparlgsqh spgrtaslnq rprthsgssg
      181 gsgsrensgs ssigipiavp tpspptigpv adsptppppp ppddipmfdd sppppppppv
      241 dyedeeaavv qyndpyadgd pawapknyie kvvaiydytk dkddelsfme gaiiyvikkn
      301 ddgwyegvcn rvtglfpgny vesimhytd
//
LOCUS       NP_001393540            1112 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 9 [Homo sapiens].
ACCESSION   NP_001393540
VERSION     NP_001393540.1
DBSOURCE    REFSEQ: accession NM_001406611.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1112)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1112)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1112)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1112)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1112)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1112)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1112)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.547186.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1112
                     /product="hamartin isoform 9"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=123813
     Region          7..667
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <656..>908
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1112
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406611.1:218..3556"
                     /note="isoform 9 is encoded by transcript variant 25"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk mdtdvvvltt gvlvlitmlp mipqsgkqhl ldffdifgrl sswclkkpgh
      121 vaevylvhlh asvyalfhrl ygmypcnfvs flrshysmke nletfeevvk pmmehvrihp
      181 elvtgskdhe ldprrwkrle thdvviecak isldpteasy edgysvshqi sarfphrsad
      241 vttspyadtq nsygcatstp ystsrlmlln mpgqlpqtls spstrlitep pqatlwspsm
      301 vcgmttppts pgnvppdlsh pyskvfgttg gkgtplgtpa tspppaplch sddyvhislp
      361 qatvtpprke ermdsarpcl hrqhhllndr gseeppgskg svtlsdlpgf lgdlaseeds
      421 iekdkeeaai srelseitta eaepvvprgg fdspfyrdsl pgsqrkthsa asssqgasvn
      481 peplhssldk lgpdtpkqaf tpidlpcgsa despagdrec qtsletsift pspckipppt
      541 rvgfgsgqpp pydhlfeval pktahhfvir kteellkkak gnteedgvps tspmevldrl
      601 iqqgadahsk elnklplpsk svdwthfggs ppsdeirtlr dqllllhnql lyerfkrqqh
      661 alrnrrllrk vikaaaleeh naamkdqlkl qekdiqmwkv slqkeqaryn qlqeqrdtmv
      721 tklhsqirql qhdreefynq sqelqtkled crnmiaelri elkkannkvc htelllsqvs
      781 qklsnsesvq qqmeflnrql lvlgevnely leqlqnkhsd ttkevemmka ayrkeleknr
      841 shvlqqtqrl dtsqkrilel eshlakkdhl lleqkkyled vklqargqlq aaesryeaqk
      901 ritqvfelei ldlygrlekd gllkkleeek aeaaeaaeer ldccndgcsd smvghneeas
      961 ghngetktpr pssargssgs rggggsssss selstpekpp hqragpfssr wettmgeasa
     1021 sipttvgslp ssksflgmka relfrnkses qcdedgmtss lseslktelg kdlgveakip
     1081 lnldgphpsp ptpdsvgqlh imdynethhe hs
//
LOCUS       NP_001393985             552 aa            linear   PRI 21-NOV-2025
DEFINITION  merlin isoform 12 [Homo sapiens].
ACCESSION   NP_001393985
VERSION     NP_001393985.1
DBSOURCE    REFSEQ: accession NM_001407056.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 552)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 552)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 552)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 552)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 552)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 552)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005529.7 and AC004882.3.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1612794.1,
                                           SRR14038192.3411441.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMN03267772
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..552
                     /product="merlin isoform 12"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=64664
     Region          1..184
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          178..274
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(220..221,223..229,238,259,262..263,266)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(220,223..230,238,259,262..263,266)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(256,260)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            259..274
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          269..>329
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          308..427
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          480..>541
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..552
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_001407056.1:597..2255"
                     /note="isoform 12 is encoded by transcript variant 18"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 mkwkgkdlfd lvcrtlglre twffglqyti kdtvawlkmd kkvldhdvsk eepvtfhfla
       61 kfypenaeee lvqeitqhlf flqvkkqild ekiycppeas vllasyavqa kygdydpsvh
      121 krgflaqeel lpkrvinlyq mtpemweeri tawyaehrgr ardeaemeyl kiaqdlemyg
      181 vnyfairnkk gtelllgvda lglhiydpen rltpkisfpw neirnisysd keftikpldk
      241 kidvfkfnss klrvnklilq lcignhdlfm rrrkadslev qqmkaqaree karkqmerqr
      301 larekqmree aertrdeler rllqmkeeat manealmrse etadllaeka qiteeeakll
      361 aqkaaeaeqe mqrikatair teeekrlmeq kvleaevlal kmaeeserra keadqlkqdl
      421 qeareaerra kqklleiatk ptyppmnpip aplppdipsf nligdslsfd fkdtdmkrls
      481 meiekekvey mekskhlqeq lnelkteiea lklkeretal dilhnensdr ggsskhntik
      541 kpqaqgrrpi ci
//
LOCUS       NP_001153145             464 aa            linear   PRI 21-NOV-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein Q isoform 2 [Homo sapiens].
ACCESSION   NP_001153145
VERSION     NP_001153145.1
DBSOURCE    REFSEQ: accession NM_001159673.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Ishtayeh,H., Galves,M., Barnatan,T.T., Berdichevsky,Y.,
            Amer-Sarsour,F., Pasmanik-Chor,M., Braverman,I., Blumen,S.C. and
            Ashkenazi,A.
  TITLE     Oculopharyngeal muscular dystrophy mutations link the RNA-binding
            protein HNRNPQ to autophagosome biogenesis
  JOURNAL   Aging Cell 22 (10), e13949 (2023)
   PUBMED   37559347
  REMARK    GeneRIF: Oculopharyngeal muscular dystrophy mutations link the
            RNA-binding protein HNRNPQ to autophagosome biogenesis.
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Semino,F., Schroter,J., Willemsen,M.H., Bast,T., Biskup,S.,
            Beck-Woedl,S., Brennenstuhl,H., Schaaf,C.P., Kolker,S.,
            Hoffmann,G.F., Haack,T.B. and Syrbe,S.
  TITLE     Further evidence for de novo variants in SYNCRIP as the cause of a
            neurodevelopmental disorder
  JOURNAL   Hum Mutat 42 (9), 1094-1100 (2021)
   PUBMED   34157790
  REMARK    GeneRIF: Further evidence for de novo variants in SYNCRIP as the
            cause of a neurodevelopmental disorder.
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Mourelatos,Z., Abel,L., Yong,J., Kataoka,N. and Dreyfuss,G.
  TITLE     SMN interacts with a novel family of hnRNP and spliceosomal
            proteins
  JOURNAL   EMBO J 20 (19), 5443-5452 (2001)
   PUBMED   11574476
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Lau,P.P., Chang,B.H. and Chan,L.
  TITLE     Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a
            component of apobec-1 editosome
  JOURNAL   Biochem Biophys Res Commun 282 (4), 977-983 (2001)
   PUBMED   11352648
REFERENCE   7  (residues 1 to 464)
  AUTHORS   Blanc,V., Navaratnam,N., Henderson,J.O., Anant,S., Kennedy,S.,
            Jarmuz,A., Scott,J. and Davidson,N.O.
  TITLE     Identification of GRY-RBP as an apolipoprotein B RNA-binding
            protein that interacts with both apobec-1 and apobec-1
            complementation factor to modulate C to U editing
  JOURNAL   J Biol Chem 276 (13), 10272-10283 (2001)
   PUBMED   11134005
REFERENCE   8  (residues 1 to 464)
  AUTHORS   Grosset,C., Chen,C.Y., Xu,N., Sonenberg,N., Jacquemin-Sablon,H. and
            Shyu,A.B.
  TITLE     A mechanism for translationally coupled mRNA turnover: interaction
            between the poly(A) tail and a c-fos RNA coding determinant via a
            protein complex
  JOURNAL   Cell 103 (1), 29-40 (2000)
   PUBMED   11051545
REFERENCE   9  (residues 1 to 464)
  AUTHORS   Mizutani,A., Fukuda,M., Ibata,K., Shiraishi,Y. and Mikoshiba,K.
  TITLE     SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear
            ribonucleoprotein R, interacts with ubiquitous synaptotagmin
            isoforms
  JOURNAL   J Biol Chem 275 (13), 9823-9831 (2000)
   PUBMED   10734137
REFERENCE   10 (residues 1 to 464)
  AUTHORS   Harris,C.E., Boden,R.A. and Astell,C.R.
  TITLE     A novel heterogeneous nuclear ribonucleoprotein-like protein
            interacts with NS1 of the minute virus of mice
  JOURNAL   J Virol 73 (1), 72-80 (1999)
   PUBMED   9847309
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF037448.1, AB209098.1,
            AL136082.22 and BF221524.1.
            
            Summary: This gene encodes a member of the cellular heterogeneous
            nuclear ribonucleoprotein (hnRNP) family. hnRNPs are RNA binding
            proteins that complex with heterogeneous nuclear RNA (hnRNA) and
            regulate alternative splicing, polyadenylation, and other aspects
            of mRNA metabolism and transport. The encoded protein plays a role
            in multiple aspects of mRNA maturation and is associated with
            several multiprotein complexes including the apoB RNA
            editing-complex and survival of motor neurons (SMN) complex.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene, and a pseudogene of this
            gene is located on the short arm of chromosome 20. [provided by
            RefSeq, Dec 2011].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, 3' UTR,
            and coding region and initiates translation at an alternate
            in-frame start codon, compared to variant 1. The resulting isoform
            (2) is shorter and has distinct N- and C-termini, compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB209098.1, SRR1660803.155080.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.3"
     Protein         1..464
                     /product="heterogeneous nuclear ribonucleoprotein Q
                     isoform 2"
                     /note="NS1-associated protein 1; heterogeneous nuclear
                     ribonucleoprotein Q; glycine- and tyrosine-rich
                     RNA-binding protein"
                     /calculated_mol_wt=51916
     Region          5..459
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     CDS             1..464
                     /gene="SYNCRIP"
                     /gene_synonym="GRY-RBP; GRYRBP; hnRNP-Q; HNRNPQ; HNRPQ1;
                     NSAP1; PP68"
                     /coded_by="NM_001159673.2:237..1631"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS75491.1"
                     /db_xref="GeneID:10492"
                     /db_xref="HGNC:HGNC:16918"
                     /db_xref="MIM:616686"
ORIGIN      
        1 mktyrqrekq gtkvadsskg pdeakikall ertgytldvt tgqrkyggpp pdsvysgqqp
       61 svgteifvgk iprdlfedel vplfekagpi wdlrlmmdpl tglnrgyafv tfctkeaaqe
      121 avklynnhei rsgkhigvci svannrlfvg sipksktkeq ileefskvte gltdvilyhq
      181 pddkkknrgf cfleyedhkt aaqarrrlms gkvkvwgnvg tvewadpied pdpevmakvk
      241 vlfvrnlant vteeilekaf sqfgklervk klkdyafihf derdgavkam eemngkdleg
      301 enieivfakp pdqkrkerka qrqaaknqmy ddyyyygpph mppptrgrgr ggrggygypp
      361 dyygyedyyd yygydyhnyr ggyedpyygy edfqvgargr ggrgargaap srgrgaappr
      421 gragysqrgg pgsargvrga rggaqqqrgr gqgkgveagp dllq
//
LOCUS       NP_001396231            2696 aa            linear   PRI 21-NOV-2025
DEFINITION  histone-lysine N-methyltransferase, H3 lysine-36 specific isoform b
            [Homo sapiens].
ACCESSION   NP_001396231
VERSION     NP_001396231.1
DBSOURCE    REFSEQ: accession NM_001409302.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2696)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2696)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   3  (residues 1 to 2696)
  AUTHORS   Conteduca,G., Cangelosi,D., Baldo,C., Arado,A., Testa,B.,
            Wagner,R.T., Robertson,K.D., Dequiedt,F., Fitzsimmons,L.,
            Malacarne,M., Filaci,G. and Coviello,D.A.
  TITLE     Impact of NSD1 Alternative Transcripts in Actin Filament Formation
            and Cellular Division Pathways in Fibroblasts
  JOURNAL   Genes (Basel) 15 (9), 1117 (2024)
   PUBMED   39336709
  REMARK    GeneRIF: Impact of NSD1 Alternative Transcripts in Actin Filament
            Formation and Cellular Division Pathways in Fibroblasts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2696)
  AUTHORS   Ren,Z., Yue,L., Hu,H.Y., Hou,X.L., Chen,W.Q., Tan,Y., Dong,Z. and
            Zhang,J.
  TITLE     Identification of Novel NSD1 variations in four Pediatric cases
            with sotos Syndrome
  JOURNAL   BMC Med Genomics 17 (1), 116 (2024)
   PUBMED   38684994
  REMARK    GeneRIF: Identification of Novel NSD1 variations in four Pediatric
            cases with sotos Syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2696)
  AUTHORS   Wang,X., Yeh,S., Wu,G., Hsu,C.L., Wang,L., Chiang,T., Yang,Y.,
            Guo,Y. and Chang,C.
  TITLE     Identification and characterization of a novel androgen receptor
            coregulator ARA267-alpha in prostate cancer cells
  JOURNAL   J Biol Chem 276 (44), 40417-40423 (2001)
   PUBMED   11509567
REFERENCE   6  (residues 1 to 2696)
  AUTHORS   Jaju,R.J., Fidler,C., Haas,O.A., Strickson,A.J., Watkins,F.,
            Clark,K., Cross,N.C., Cheng,J.F., Aplan,P.D., Kearney,L.,
            Boultwood,J. and Wainscoat,J.S.
  TITLE     A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in
            de novo childhood acute myeloid leukemia
  JOURNAL   Blood 98 (4), 1264-1267 (2001)
   PUBMED   11493482
REFERENCE   7  (residues 1 to 2696)
  AUTHORS   Lee,D.K., Duan,H.O. and Chang,C.
  TITLE     Androgen receptor interacts with the positive elongation factor
            P-TEFb and enhances the efficiency of transcriptional elongation
  JOURNAL   J Biol Chem 276 (13), 9978-9984 (2001)
   PUBMED   11266437
REFERENCE   8  (residues 1 to 2696)
  AUTHORS   Huang,N., vom Baur,E., Garnier,J.M., Lerouge,T., Vonesch,J.L.,
            Lutz,Y., Chambon,P. and Losson,R.
  TITLE     Two distinct nuclear receptor interaction domains in NSD1, a novel
            SET protein that exhibits characteristics of both corepressors and
            coactivators
  JOURNAL   EMBO J 17 (12), 3398-3412 (1998)
   PUBMED   9628876
REFERENCE   9  (residues 1 to 2696)
  AUTHORS   Ocansey,S., Cole,T.R.P., Rahman,N. and Tatton-Brown,K.
  TITLE     Sotos Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301652
REFERENCE   10 (residues 1 to 2696)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027314.5, AC008570.6 and
            AC146507.2.
            
            Summary: This gene encodes a protein containing a SET domain, 2
            LXXLL motifs, 3 nuclear translocation signals (NLSs), 4 plant
            homeodomain (PHD) finger regions, and a proline-rich region. The
            encoded protein enhances androgen receptor (AR) transactivation,
            and this enhancement can be increased further in the presence of
            other androgen receptor associated coregulators. This protein may
            act as a nucleus-localized, basic transcriptional factor and also
            as a bifunctional transcriptional regulator. Mutations of this gene
            have been associated with Sotos syndrome and Weaver syndrome. One
            version of childhood acute myeloid leukemia is the result of a
            cryptic translocation with the breakpoints occurring within nuclear
            receptor-binding Su-var, enhancer of zeste, and trithorax domain
            protein 1 on chromosome 5 and nucleoporin, 98-kd on chromosome 11.
            Multiple transcript variants encoding distinct isoforms have been
            identified for this gene. [provided by RefSeq, Sep 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1742234.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2696
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..2696
                     /product="histone-lysine N-methyltransferase, H3 lysine-36
                     specific isoform b"
                     /EC_number="2.1.1.357"
                     /note="androgen receptor-associated coregulator 267;
                     histone-lysine N-methyltransferase, H3 lysine-36 and H4
                     lysine-20 specific; H3-K36-HMTase; H4-K20-HMTase; lysine
                     N-methyltransferase 3B; NR-binding SET domain-containing
                     protein; androgen receptor coactivator 267 kDa protein;
                     androgen receptor-associated protein of 267 kDa; nuclear
                     receptor-binding SET domain-containing protein 1; nuclear
                     receptor SET domain-containing protein 1; histone-lysine
                     N-methyltransferase, H3 lysine-36 specific"
                     /calculated_mol_wt=296522
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88491; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          207..252
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          281..311
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          318..433
                     /region_name="PWWP_NSD1_rpt1"
                     /note="first PWWP domain found in nuclear receptor-binding
                     SET domain-containing protein 1 (NSD1) and similar
                     proteins; cd20161"
                     /db_xref="CDD:438989"
     Site            order(334,337,368)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438989"
     Site            335..338
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438989"
     Site            order(406..408,411..412)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438989"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          487..514
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17487921; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          872..891
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          936..1035
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1067..1093
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1112..1134
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1243..1272
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1294..1344
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1382..1428
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          <1431..1587
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          1480..1534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            1510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88491; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          1545..1587
                     /region_name="PHD1_NSD1_2"
                     /note="PHD finger 1 found in nuclear receptor-binding SET
                     domain-containing protein NSD1 and NSD2; cd15648"
                     /db_xref="CDD:277118"
     Site            order(1545,1554..1558,1563,1581)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277118"
     Region          1592..1638
                     /region_name="PHD2_NSD1"
                     /note="PHD finger 2 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15650"
                     /db_xref="CDD:277120"
     Site            order(1592,1602..1606,1612,1633)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277120"
     Region          1639..1692
                     /region_name="PHD3_NSD1"
                     /note="PHD finger 3 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15653"
                     /db_xref="CDD:277123"
     Site            order(1639,1657..1661,1665,1687)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277123"
     Region          1709..1748
                     /region_name="PHD4_NSD1"
                     /note="PHD finger 4 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15656"
                     /db_xref="CDD:277126"
     Site            order(1709,1718..1722,1726,1743)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277126"
     Region          1755..1850
                     /region_name="PWWP_NSD1_rpt2"
                     /note="second PWWP domain found in nuclear
                     receptor-binding SET domain-containing protein 1 (NSD1)
                     and similar proteins; cd20164"
                     /db_xref="CDD:438992"
     Site            order(1767,1770,1798)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438992"
     Site            1768..1771
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438992"
     Region          1901..1939
                     /region_name="AWS"
                     /note="AWS domain; pfam17907"
                     /db_xref="CDD:465559"
     Region          1941..2082
                     /region_name="SET_NSD1"
                     /note="SET domain (including post-SET domain) found in
                     nuclear receptor-binding SET domain-containing protein 1
                     (NSD1) and similar proteins; cd19210"
                     /db_xref="CDD:380987"
     Site            order(1952..1954,1971,1981,1985,1994..2000,2017..2021,
                     2028..2030,2045,2056..2066,2068..2072,2081)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380987"
     Site            order(1952..1954,1994..1997,2017..2021,2058,2065,
                     2069..2072,2081)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380987"
     Site            order(1971,1981,1985,1996..2000,2028..2030,2045,
                     2056..2060)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:380987"
     Site            order(2023,2070,2072,2077)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380987"
     Region          2060..2066
                     /region_name="Inhibits enzyme activity in the absence of
                     bound histone"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2091..2111
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2120..2162
                     /region_name="PHD5_NSD1"
                     /note="PHD finger 5 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15659"
                     /db_xref="CDD:277129"
     Site            order(2120,2129..2133,2139,2157)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277129"
     Region          2161..2210
                     /region_name="C5HCH"
                     /note="NSD Cys-His rich domain; pfam17982"
                     /db_xref="CDD:465605"
     Region          <2208..2574
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          2213..2422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            2369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            2462
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2464..2499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Site            2471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2553..2575
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2595..2616
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     Region          2665..2696
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96L73.1)"
     CDS             1..2696
                     /gene="NSD1"
                     /gene_synonym="ARA267; KMT3B; SOTOS; SOTOS1; STO"
                     /coded_by="NM_001409302.1:158..8248"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="GeneID:64324"
                     /db_xref="HGNC:HGNC:14234"
                     /db_xref="MIM:606681"
ORIGIN      
        1 mdqtcelprr ncllpfsnpv nldapedkds pfgngqsnfs eplngctmql stvsgtsqna
       61 ygqdspscyi plrrlqdlas minveylngs adgsesfqdp eksdsraqtp ivctslspgg
      121 ptalamkqep scnnspelqv kvtktikngf lhfenftcvd dadvdsemdp eqpvtedesi
      181 eeifeetqtn atcnyetkse ngvkvamgse qdstpesrhg avkspflpla pqtetqknkq
      241 rnevdgsnek aallpapfsl gdtnitieeq lnsinlsfqd dpdsststlg nmlelpgtss
      301 sstsqelpfc qpkkkstplk yevgdliwak fkrrpwwpcr icsdplinth skmkvsnrrp
      361 yrqyyveafg dpserawvag kaivmfegrh qfeelpvlrr rgkqkekgyr hkvpqkilsk
      421 weasvglaeq ydvpkgsknr kcipgsikld seedmpfedc tndpesehdl llngclksla
      481 fdsehsadek ekpcaksrar kssdnpkrts vkkghiqfea hkderrgkip enlglnfisg
      541 disdtqasne lsriansltg sntapgsflf sscgkntakk efetsngdsl lglpegalis
      601 kcsreknkpq rslvcgskvk lcyigagdee krsdsisict tsddgssdld piehssesdn
      661 svleipdafd rtenmlsmqk nekikysrfa atntrvkakq kplisnshtd hlmgctksae
      721 pgtetsqvnl sdlkastlvh kpqsdftnda lspkfnlsss issenslikg gaanqallhs
      781 kskqpkfrsi kckhkenpvm aeppvineec slkccssdtk gsplasisks gkvdglklln
      841 nmhektrdss dietavvkhv lselkelsyr slgedvsdsg tskpskpllf ssassqnhip
      901 iepdykfstl lmmlkdmhds ktkeqrlmta qnlvsyrspg rgdcstnspv gvskvlvsgg
      961 sthnsekkgd gtqnsanpsp sggdsalsge lsaslpglls dkrdlpasgk srsdcvtrrn
     1021 cgrskpsskl rdafsaqmvk ntvnrkalkt erkrklnqlp svtldavlqg drerggslrg
     1081 gaedpskedp lqimghltse dgdhfsdvhf dskvkqsdpg kisekglsfe ngkgpeldsv
     1141 mnsendelng vnqvvpkkrw qrlnqrrtkp rkrmnrfkek ensecafrvl lpsdpvqegr
     1201 defpehrtps asileeplte qnhadcldsa gprlnvcdks sasigdmeke pgipsltpqa
     1261 elpepavrse kkrlrkpskw lleyteeydq ifapkkkqkk vqeqvhkvss rceeesllar
     1321 grssaqnkqv denslistke eppvlereap flegplaqse lggghaelpq ltlsvpvape
     1381 vsprpalese ellvktpgny eskrqrkptk kllesndldp gfmpkkgdlg lskkcyeagh
     1441 lengitesca tsyskdfggg ttkifdkprk rkrqrhaaak mqckkvkndd sskeipgseg
     1501 elmphrtats pketveegve hdpgmpaskk mqgergggaa lkenvcqnce klgelllcea
     1561 qccgafhlec lgltemprgk ficnecrtgi htcfvckqsg edvkrcllpl cgkfyheecv
     1621 qkypptvmqn kgfrcslhic itchaanpan vsaskgrlmr cvrcpvayha ndfclaagsk
     1681 ilasnsiicp nhftprrgcr nhehvnvswc fvcseggsll ccdscpaafh reclnidipe
     1741 gnwycndcka gkkphyreiv wvkvgryrww paeichprav psnidkmrhd vgefpvlffg
     1801 sndylwthqa rvfpymegdv sskdkmgkgv dgtykkalqe aaarfeelka qkelrqlqed
     1861 rkndkkpppy khikvnrpig rvqiftadls eiprcnckat denpcgidse cinrmllyec
     1921 hptvcpaggr cqnqcfskrq ypeveifrtl qrgwglrtkt dikkgefvne yvgelideee
     1981 crariryaqe hditnfymlt ldkdriidag pkgnyarfmn hccqpncetq kwsvngdtrv
     2041 glfalsdika gteltfnynl eclgngktvc kcgapncsgf lgvrpknqpi ateekskkfk
     2101 kkqqgkrrtq geitkerede cfscgdagql vsckkpgcpk vyhadclnlt krpagkwecp
     2161 whqcdicgke aasfcemcps sfckqhregm lfiskldgrl sctehdpcgp nplepgeire
     2221 yvpppvplpp gpsthlaeqs tgmaaqapkm sdkppadtnq mlslskkala gtcqrpllpe
     2281 rplertdsrp qpldkvrdla gsgtksqslv ssqrpldrpp avagprpqls dkpspvtsps
     2341 sspsvrsqpl erplgtadpr ldksigaasp rpqslektsv ptglrlpppd rllitsspkp
     2401 qtsdrptdkp haslsqrlpp pekvlsavvq tlvakekalr pvdqntqskn raalvmdlid
     2461 ltprqkeraa sphqvtpqad ekmpvlesss wpaskglghm pravekgcvs dplqtsgkaa
     2521 apsedpwqav ksltqarlls qppakaflye pttqasgras agaeqtpgpl sqspglvkqa
     2581 kqmvggqqlp alaaksgqsf rslgkapasl pteekklvtt eqspwalgka ssraglwpiv
     2641 agqtlaqscw sagstqtlaq tcwslgrgqd pkpeqntlpa lnqapsshkc aeseqk
//
LOCUS       NP_001427987            4358 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HUWE1 isoform 2 [Homo sapiens].
ACCESSION   NP_001427987 XP_047297701 XP_054182297
VERSION     NP_001427987.1
DBSOURCE    REFSEQ: accession NM_001441058.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4358)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 4358)
  AUTHORS   Lee,C., Park,S.H. and Yoon,S.K.
  TITLE     The E3 ligase HUWE1 increases the sensitivity of CRC to oxaliplatin
            through TOMM20 degradation
  JOURNAL   Oncogene 43 (9), 636-649 (2024)
   PUBMED   38184713
  REMARK    GeneRIF: The E3 ligase HUWE1 increases the sensitivity of CRC to
            oxaliplatin through TOMM20 degradation.
REFERENCE   3  (residues 1 to 4358)
  AUTHORS   Li,X.X., Xu,J.K., Su,W.J., Wu,H.L., Zhao,K., Zhang,C.M., Chen,X.K.
            and Yang,L.X.
  TITLE     The role of KDM4A-mediated histone methylation on temozolomide
            resistance in glioma cells through the HUWE1/ROCK2 axis
  JOURNAL   Kaohsiung J Med Sci 40 (2), 161-174 (2024)
   PUBMED   37873881
  REMARK    GeneRIF: The role of KDM4A-mediated histone methylation on
            temozolomide resistance in glioma cells through the HUWE1/ROCK2
            axis.
REFERENCE   4  (residues 1 to 4358)
  AUTHORS   Bernassola,F., Karin,M., Ciechanover,A. and Melino,G.
  TITLE     The HECT family of E3 ubiquitin ligases: multiple players in cancer
            development
  JOURNAL   Cancer Cell 14 (1), 10-21 (2008)
   PUBMED   18598940
  REMARK    Review article
REFERENCE   5  (residues 1 to 4358)
  AUTHORS   Zhong,Q., Gao,W., Du,F. and Wang,X.
  TITLE     Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the
            polyubiquitination of Mcl-1 and regulates apoptosis
  JOURNAL   Cell 121 (7), 1085-1095 (2005)
   PUBMED   15989957
  REMARK    GeneRIF: Mule is both required and sufficient for the
            polyubiquitination of Mcl-1; Mule is a unique BH3-containing E3
            ubiquitin ligase apical to Bcl-2 family proteins during DNA
            damage-induced apoptosis
            GeneRIF: Mule (HUWE1) poly-ubiquitinates anti-apoptotic gene Mcl-1.
REFERENCE   6  (residues 1 to 4358)
  AUTHORS   Chen,D., Kon,N., Li,M., Zhang,W., Qin,J. and Gu,W.
  TITLE     ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
  JOURNAL   Cell 121 (7), 1071-1083 (2005)
   PUBMED   15989956
  REMARK    GeneRIF: study modifies the current view of ARF-mediated p53
            activation and reveals that ARF-BP1 is a critical mediator of both
            the p53-independent and p53-dependent tumor suppressor functions of
            ARF
            GeneRIF: Ubiquitin ligase activity of ARF-BP1 (HUWE1) is inhibited
            by Arf.
REFERENCE   7  (residues 1 to 4358)
  AUTHORS   Liu,Z., Oughtred,R. and Wing,S.S.
  TITLE     Characterization of E3Histone, a novel testis ubiquitin protein
            ligase which ubiquitinates histones
  JOURNAL   Mol Cell Biol 25 (7), 2819-2831 (2005)
   PUBMED   15767685
REFERENCE   8  (residues 1 to 4358)
  AUTHORS   Gu,J., Dubner,R., Fornace,A.J. Jr. and Iadarola,M.J.
  TITLE     UREB1, a tyrosine phosphorylated nuclear protein, inhibits p53
            transactivation
  JOURNAL   Oncogene 11 (10), 2175-2178 (1995)
   PUBMED   7478539
REFERENCE   9  (residues 1 to 4358)
  AUTHORS   Turner,G., Gedeon,A. and Mulley,J.
  TITLE     X-linked mental retardation with heterozygous expression and
            macrocephaly: pericentromeric gene localization
  JOURNAL   Am J Med Genet 51 (4), 575-580 (1994)
   PUBMED   7943042
REFERENCE   10 (residues 1 to 4358)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX323845.7 and AC231658.3.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297701.1, XP_054182297.1.
            
            Summary: This gene encodes a protein containing a C-terminal HECT
            (E6AP type E3 ubiquitin protein ligase) domain that functions as an
            E3 ubiquitin ligase. The encoded protein is required for the
            ubiquitination and subsequent degradation of the anti-apoptotic
            protein Mcl1 (myeloid cell leukemia sequence 1 (BCL2-related)).
            This protein also ubiquitinates the p53 tumor suppressor, core
            histones, and DNA polymerase beta. Mutations in this gene are
            associated with Turner type X-linked syndromic cognitive
            disability. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2361571.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..4358
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..4358
                     /product="E3 ubiquitin-protein ligase HUWE1 isoform 2"
                     /EC_number="2.3.2.26"
                     /note="Mcl-1 ubiquitin ligase E3; BJ-HCC-24 tumor antigen;
                     HECT domain protein LASU1; ARF-binding protein 1;
                     URE-binding protein 1; large structure of UREB1; upstream
                     regulatory element-binding protein 1; homologous to E6AP
                     carboxyl terminus homologous protein 9; HECT-type E3
                     ubiquitin transferase HUWE1; HECT, UBA and WWE domain
                     containing 1, E3 ubiquitin protein ligase"
                     /calculated_mol_wt=479954
     Region          92..367
                     /region_name="DUF908"
                     /note="Domain of Unknown Function (DUF908); pfam06012"
                     /db_xref="CDD:428721"
     Region          431..814
                     /region_name="DUF913"
                     /note="Domain of Unknown Function (DUF913); pfam06025"
                     /db_xref="CDD:461803"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          706..759
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          978..1001
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1014..1037
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1084
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1291..1320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1317..1356
                     /region_name="UBA_HUWE1"
                     /note="UBA domain found in eukaryotic E3 ubiquitin-protein
                     ligase HUWE1 and similar proteins; cd14288"
                     /db_xref="CDD:270474"
     Site            1368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1396..1415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1617..1678
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          1689..1735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1722
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1907
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2017..2064
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2034
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2261..2341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2266
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2355..2479
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2534
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2553
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2594
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2618
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2693..2969
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          <2734..3065
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            2750
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2825
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2832
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2860
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2886
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2887
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2888
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2917
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3009..3042
                     /region_name="UBM"
                     /note="Ubiquitin binding region; pfam14377"
                     /db_xref="CDD:464159"
     Region          3035..3058
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3148
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3244..3266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3403..3423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3470..3511
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3536..3567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3736..3757
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3751
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3792
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3800
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3811
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3814
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3878..3915
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3890
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3903
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3908
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3911
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          4003..4356
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(4007,4037,4048,4109,4283,4319..4320,4323..4327,4347,
                     4355)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(4137,4140..4141,4143..4144,4147,4154,4156,
                     4160..4161,4163,4168,4173,4190,4194)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     Site            4255
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P51593; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     CDS             1..4358
                     /gene="HUWE1"
                     /gene_synonym="ARF-BP1; HECTH9; HSPC272; Ib772; LASU1;
                     MRXST; MULE; URE-B1; UREB1"
                     /coded_by="NM_001441058.1:291..13367"
                     /note="isoform 2 is encoded by transcript variant 12"
                     /db_xref="GeneID:10075"
                     /db_xref="HGNC:HGNC:30892"
                     /db_xref="MIM:300697"
ORIGIN      
        1 mkvdrtklkk tpteapadcr alidklkvcn deqlllelqq iktwnigkce lyhwvdlldr
       61 fdgiladagq tvenmswmlv cdrpereqlk mlllavlnft allieysfsr hlyssiehlt
      121 tllassdmqv vlavlnllyv fskrsnyitr lgsdkrtpll trlqhlaesw ggkengfgla
      181 eccrdlhmmk yppsattlhf efyadpgaev kiekrttsnt lhyihieqld kisespseim
      241 esltkmysip kdkqmllfth irlahgfsnh rkrlqavqar lhaisilvys nalqesansi
      301 lynglieelv dvlqitdkql meikaaslrt ltsivhlert pklssiidct gtasyhgflp
      361 vlvrnciqam idpsmdpyph qfatalfsfl yhlasydagg ealvscgmme allkvikflg
      421 deqdqitfvt ravrvvdlit nldmaafqsh sglsifiyrl ehevdlcrke cpfvikpkiq
      481 rpnttqegee metdmdgvqc ipqraallks mlnflkkaiq dpafsdgirh vmdgslptsl
      541 khiisnaeyy gpslfllate vvtvfvfqep sllsslqdng ltdvmlhall ikdvpatrev
      601 lgslpnvfsa lclnarglqs fvqcqpferl fkvllspdyl pamrrrrssd plgdtasnlg
      661 savdelmrhq ptlktdatta iiklleeicn lgrdpkyicq kpsiqkadgt atappprsnh
      721 aaeeassede eeeevqamqs fnstqqnete pnqqvvgtee ripiplmdyi lnvmkfvesi
      781 lsnnttddhc qefvnqkgll plvtilglpn lpidfptsaa cqavagvcks iltlshepkv
      841 lqegllqlds ilssleplhr piespggsvl lrelacagnv adatlsaqat pllhaltaah
      901 ayimmfvhtc rvgqseirsi svnqwgsqlg lsvlsklsql ycslvwestv llslctpnsl
      961 psgcefgqad mqklvpkdek agttqggkrs dgeqdgaags mdastqglle gigldgdtla
     1021 pmetdeptas dskgkskitp amaarikqik pllsassrlg ralaelfgll vklcvgspvr
     1081 qrrshhaast ttaptpaars tasaltkllt kglswqpppy tptprfrltf ficsvgftsp
     1141 mlfderkypy hlmlqkflcs gghnalfetf nwalsmggkv pvseglehsd lpdgtgefld
     1201 awlmlvekmv npttvlesph slpaklpggv qnfpqfsalr flvvtqkaaf tciknlwnrk
     1261 plkvyggrma esmlailchi lrgepvirer lskekegsrg eedtgqeegg srrepqvnqq
     1321 qlqqlmdmgf trehameall ntstmeqate yllthpppim ggvvrdlsms eedqmmraia
     1381 mslgqdipmd qraespeeva crkeeeerka rekqeeeeak clekfqdadp leqdelhtft
     1441 dtmlpgcfhl ldelpdtvyr vcdlimtaik rngadyrdmi lkqvvnqvwe aadvlikaal
     1501 plttsdtktv sewisqmatl pqasnlatri llltllfeel klpcawvves sgilnvlikl
     1561 levvqpclqa akeqkevqtp kwitpvllli dfyektaiss krraqmtkyl qsnsnnwrwf
     1621 ddrsgrwcsy sasnnstids awksgetsvr ftagrrrytv qfttmvqvne etgnrrpvml
     1681 tllrvprlnk nsknsngqel ektleeskem dikrkenkgn dtplalestn teketsleet
     1741 kigeiliqgl tedmvtvlir acvsmlgvpv dpdtlhatlr lclrltrdhk yammfaelks
     1801 trmilnltqs sgfngftplv tlllrhiied pctlrhtmek vvrsaatsga gsttsgvvsg
     1861 slgsreinyi lrvlgpaacr npdiftevan ccirialpap rgsgtasdde fenlrikgpn
     1921 avqlvkttpl kpsplpvipd tikeviydml nalaayhape edksdpkpgv mtqevgqllq
     1981 dmgddvyqqy rsltrqssdf dtqsgfsins qvfaadgast etsasgtsqg eastpeesrd
     2041 gkkdkegdra seegkqkgkg skplmptsti lrllaelvrs yvgiatlian ysytvgqsel
     2101 ikedcsvlaf vldhllphtq naedkdtpal arlflaslaa agsgtdaqva lvnevkaalg
     2161 ralamaeste kharlqavmc iistimescp stssfyssat aktqhngmnn iirlflkkgl
     2221 vndlarvphs ldlsspnman tvnaalkple tlsrivnqps slfgsksass knkseqdaqg
     2281 asqdsssnqq dpgepgeaev qeedhdvtqt evadgdimdg eaetdsvvia gqpevlssqe
     2341 mqveneledl idellerdgg sgnstiivsr sgedesqedv lmdeapsnls qastlqanre
     2401 dsmnildped eeehtqeeds sgsnededds qdeeeeeeed eeddqeddeg eegdeddddd
     2461 gsemeldedy pdmnasplvr ferfdreddl iiefdnmfss atdippspgn iptthplmvr
     2521 hadhssltlg sgssttrltq gigrsqrtlr qltantghti hvhypgnrqp npplilqrll
     2581 gpsaaadilq lssslplqsr grarllvgnd dvhiiarsdd ellddffhdq statsqagtl
     2641 ssiptaltrw teeckvldae smhdcvsvvk vsivnhlefl rdeeleerre krrkqlaeee
     2701 tkitdkgked kenrdqsaqc tasksndste qnlsdgtpmp dsypttpsst daatsesket
     2761 lgtlqssqqq ptlptppalg evpqelqspa geggsstqll mpvepeelgp trpsgeaett
     2821 qmelspapti tslsperaed sdaltavssq legspmdtss lasctleeav gdtsaagsse
     2881 qpragsstpg dappavaevq grsdgsgesa qppedssppa ssessstrds avaisgadsr
     2941 gileeplpst sseeedplag islpegvdps flaalpddir revlqnqlgi rpptrtapst
     3001 nssapavvgn pgvtevspef laalppaiqe evlaqqraeq qrrelaqnas sdtpmdpvtf
     3061 iqtlpsdlrr svledmedsv lavmppdiaa eaqalrreqe arqrqlmher lfghsstsal
     3121 sailrspaft srlsgnrgvq ytrlavqrgg tfqmggsssh nrpsgsnvdt llrlrgrlll
     3181 dhealscllv llfvdepkln tsrlhrvlrn lcyhaqtrhw virsllsilq rsseselcie
     3241 tpklttseek gkksskscgs sshenrpldl lhkmeskssn qlswlsvsmd aalgcrtnif
     3301 qiqrsggrkh tekhasggst vhihpqaapv vcrhvldtli qlakvfpshf tqqrtketnc
     3361 esdrergnka cspcssqsss sgictdfwdl lvkldnmnvs rkgknsvksv pvsaggeget
     3421 spysleaspl gqlmnmlshp virrssllte kllrllslis ialpenkvse aqansgsgas
     3481 stttatstts tttttaastt ptpptaptpv tsapalvaat aistivvaas ttvttpttat
     3541 ttvsispttk gskspakvsd ggssstdfkm vssgltenql qlsvevltsh scseegleda
     3601 anvllqlsrg dsgtrdtvlk lllngarhlg ytlckqigtl laelreynle qqrraqcetl
     3661 spdglpeeqp qttklkgkmq srfdmaenvv ivasqkrplg grelqlpsms mltsktstqk
     3721 fflrvlqvii qlrddtrran kkakqtgrlg ssglgsassi qaavrqleae adaiiqmses
     3781 sqseasvrre espmdvdqps psaqdtqsia sdgtpqgeke keerppelpl lseqlsldel
     3841 wdmlgeclke leeshdqhav lvlqpaveaf flvhateres kppvrdtres qlahikdepp
     3901 plspapltpa tpssldpffs repssmhiss slppdtqkfl rfaethrtvl nqilrqstth
     3961 ladgpfavlv dyirvldfdv krkyfrqele rldeglrked mavhvrrdhv fedsyrelhr
     4021 kspeemknrl yivfegeegq daggllrewy miisremfnp myalfrtspg drvtytinps
     4081 shcnpnhlsy fkfvgrivak avydnrllec yftrsfykhi lgksvrytdm esedyhfyqg
     4141 lvyllendvs tlgydltfst evqefgvcev rdlkpngani lvteenkkey vhlvcqmrmt
     4201 gairkqlaaf legfyeiipk rlisifteqe lellisglpt ididdlksnt eyhkyqsnsi
     4261 qiqwfwralr sfdqadrakf lqfvtgtskv plqgfaaleg mngiqkfqih rddrstdrlp
     4321 sahtcfnqld lpayesfekl rhmlllaiqe csegfgla
//
LOCUS       NP_001425515            2698 aa            linear   PRI 21-NOV-2025
DEFINITION  nipped-B-like protein isoform C [Homo sapiens].
ACCESSION   NP_001425515 XP_005248337 XP_054208304
VERSION     NP_001425515.1
DBSOURCE    REFSEQ: accession NM_001438586.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2698)
  AUTHORS   Nguyen,A.L., Smith,E.M. and Cheeseman,I.M.
  TITLE     Co-essentiality analysis identifies PRR12 as a cohesin interacting
            protein and contributor to genomic integrity
  JOURNAL   Dev Cell 60 (8), 1217-1233 (2025)
   PUBMED   39742660
REFERENCE   2  (residues 1 to 2698)
  AUTHORS   Xu,X., Wang,D., Xu,W., Li,H., Chen,N., Li,N., Yao,Q., Chen,W.,
            Zhong,J. and Mao,W.
  TITLE     NIPBL-mediated RAD21 facilitates tumorigenicity by the PI3K pathway
            in non-small-cell lung cancer
  JOURNAL   Commun Biol 7 (1), 206 (2024)
   PUBMED   38378967
  REMARK    GeneRIF: NIPBL-mediated RAD21 facilitates tumorigenicity by the
            PI3K pathway in non-small-cell lung cancer.
            Erratum:[Commun Biol. 2024 Apr 1;7(1):397. doi:
            10.1038/s42003-024-06085-w. PMID: 38561443]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2698)
  AUTHORS   Alonso-Gil,D., Cuadrado,A., Gimenez-Llorente,D.,
            Rodriguez-Corsino,M. and Losada,A.
  TITLE     Different NIPBL requirements of cohesin-STAG1 and cohesin-STAG2
  JOURNAL   Nat Commun 14 (1), 1326 (2023)
   PUBMED   36898992
  REMARK    GeneRIF: Different NIPBL requirements of cohesin-STAG1 and
            cohesin-STAG2.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2698)
  AUTHORS   Coursimault,J., Cassinari,K., Lecoquierre,F., Quenez,O.,
            Coutant,S., Derambure,C., Vezain,M., Drouot,N., Vera,G.,
            Schaefer,E., Philippe,A., Doray,B., Lambert,L., Ghoumid,J.,
            Smol,T., Rama,M., Legendre,M., Lacombe,D., Fergelot,P., Olaso,R.,
            Boland,A., Deleuze,J.F., Goldenberg,A., Saugier-Veber,P. and
            Nicolas,G.
  TITLE     Deep intronic NIPBL de novo mutations and differential diagnoses
            revealed by whole genome and RNA sequencing in Cornelia de Lange
            syndrome patients
  JOURNAL   Hum Mutat 43 (12), 1882-1897 (2022)
   PUBMED   35842780
  REMARK    GeneRIF: Deep intronic NIPBL de novo mutations and differential
            diagnoses revealed by whole genome and RNA sequencing in Cornelia
            de Lange syndrome patients.
REFERENCE   5  (residues 1 to 2698)
  AUTHORS   Gillis,L.A., McCallum,J., Kaur,M., DeScipio,C., Yaeger,D.,
            Mariani,A., Kline,A.D., Li,H.H., Devoto,M., Jackson,L.G. and
            Krantz,I.D.
  TITLE     NIPBL mutational analysis in 120 individuals with Cornelia de Lange
            syndrome and evaluation of genotype-phenotype correlations
  JOURNAL   Am J Hum Genet 75 (4), 610-623 (2004)
   PUBMED   15318302
REFERENCE   6  (residues 1 to 2698)
  AUTHORS   Krantz,I.D., McCallum,J., DeScipio,C., Kaur,M., Gillis,L.A.,
            Yaeger,D., Jukofsky,L., Wasserman,N., Bottani,A., Morris,C.A.,
            Nowaczyk,M.J., Toriello,H., Bamshad,M.J., Carey,J.C., Rappaport,E.,
            Kawauchi,S., Lander,A.D., Calof,A.L., Li,H.H., Devoto,M. and
            Jackson,L.G.
  TITLE     Cornelia de Lange syndrome is caused by mutations in NIPBL, the
            human homolog of Drosophila melanogaster Nipped-B
  JOURNAL   Nat Genet 36 (6), 631-635 (2004)
   PUBMED   15146186
  REMARK    GeneRIF: identified mutations in one gene, NIPBL, in four sporadic
            and two familial cases of Cornelia de Lange syndrome
REFERENCE   7  (residues 1 to 2698)
  AUTHORS   Tonkin,E.T., Wang,T.J., Lisgo,S., Bamshad,M.J. and Strachan,T.
  TITLE     NIPBL, encoding a homolog of fungal Scc2-type sister chromatid
            cohesion proteins and fly Nipped-B, is mutated in Cornelia de Lange
            syndrome
  JOURNAL   Nat Genet 36 (6), 636-641 (2004)
   PUBMED   15146185
REFERENCE   8  (residues 1 to 2698)
  AUTHORS   Jackson,L., Kline,A.D., Barr,M.A. and Koch,S.
  TITLE     de Lange syndrome: a clinical review of 310 individuals
  JOURNAL   Am J Med Genet 47 (7), 940-946 (1993)
   PUBMED   8291537
REFERENCE   9  (residues 1 to 2698)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   10 (residues 1 to 2698)
  AUTHORS   Deardorff,M.A., Noon,S.E. and Krantz,I.D.
  TITLE     Cornelia de Lange Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301283
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026741.6 and AC008902.5.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_005248337.1, XP_054208304.1.
            
            Summary: This gene encodes the homolog of the Drosophila
            melanogaster Nipped-B gene product and fungal Scc2-type sister
            chromatid cohesion proteins. The Drosophila protein facilitates
            enhancer-promoter communication of remote enhancers and plays a
            role in developmental regulation. It is also homologous to a family
            of chromosomal adherins with broad roles in sister chromatid
            cohesion, chromosome condensation, and DNA repair. The human
            protein has a bipartite nuclear targeting sequence and a putative
            HEAT repeat. Condensins, cohesins and other complexes with
            chromosome-related functions also contain HEAT repeats. Mutations
            in this gene result in Cornelia de Lange syndrome, a disorder
            characterized by dysmorphic facial features, growth delay, limb
            reduction defects, and cognitive disability. Two transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.407295.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2698
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..2698
                     /product="nipped-B-like protein isoform C"
                     /note="sister chromatid cohesion 2 homolog; nipped-B-like
                     protein; SCC2 homolog; delangin; Nipped-B homolog"
                     /calculated_mol_wt=304351
     Region          128..340
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6KCD5; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6KCD5; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Region          <476..1092
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          482..946
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KC79.2)"
     Region          <597..832
                     /region_name="PspC_subgroup_2"
                     /note="pneumococcal surface protein PspC, LPXTG-anchored
                     form; NF033839"
                     /db_xref="CDD:468202"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            912
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Region          996..1009
                     /region_name="PxVxL motif.
                     /evidence=ECO:0000269|PubMed:20562864,
                     ECO:0000269|PubMed:28167679"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KC79.2)"
     Region          1017..1047
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KC79.2)"
     Region          1060..1191
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            1082
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6KCD5; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            1089
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            1090
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            1096
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            1150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            1152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            1154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            1159
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q6KCD5; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            1160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            1189
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            1197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Region          1263..2473
                     /region_name="SCC2"
                     /note="Sister chromatid cohesion protein 2 and homologs;
                     cd23958"
                     /db_xref="CDD:467937"
     Region          1691..1710
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KC79.2)"
     Region          1767..1805
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KC79.2)"
     Region          1811..1839
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1843..1881
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KC79.2)"
     Region          1848..1874
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1945..1984
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KC79.2)"
     Region          2227..2267
                     /region_name="HEAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KC79.2)"
     Region          2313..2351
                     /region_name="HEAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KC79.2)"
     Region          2473..2520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            2493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6KCD5; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            2509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            2511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            2513
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            2515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            2652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            2658
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            2667
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     Phosphothreonine. /evidence=ECO:0007744|PubMed:18669648;
                     propagated from UniProtKB/Swiss-Prot (Q6KC79.2)"
     Site            2672
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     Phosphoserine. /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6KC79.2)"
     CDS             1..2698
                     /gene="NIPBL"
                     /gene_synonym="CDLS; CDLS1; IDN3; IDN3-B; Scc2"
                     /coded_by="NM_001438586.1:490..8586"
                     /note="isoform C is encoded by transcript variant C"
                     /db_xref="GeneID:25836"
                     /db_xref="HGNC:HGNC:28862"
                     /db_xref="MIM:608667"
ORIGIN      
        1 mngdmphvpi ttlagiaslt dllnqlplps plpatttksl lfnariaeev ncllacrddn
       61 lvsqlvhsln qvstdhielk dnlgsddpeg dipvllqavl arspnvfrek smqnryvqsg
      121 mmmsqyklsq nsmhsspass nyqqttishs pssrfvppqt ssgnrfmpqq nspvpspyap
      181 qspagympys hpssytthpq mqqasvsspi vagglrnihd nkvsgplsgn sanhhadnpr
      241 hgssedylhm vhrlssddgd sstmrnaasf plrspqpvcs pagsegtpkg srpplilqsq
      301 slpcssprdv ppdilldspe rkqkkqkkmk lgkdekeqse kaamydiiss pskdstkltl
      361 rlsrvrssdm dqqedmisgv ensnvsendi pfnvqypgqt sktpitpqdi nrplnaaqcl
      421 sqqeqtaflp anqvpvlqqn tsvaakqpqt svvqnqqqis qqgpiydeve ldalaeieri
      481 eresaierer fskevqdkdk plkkrkqdsy pqeaggatgg nrpasqetgs tgngsrpalm
      541 vsidlhqagr vdsqasitqd sdsikkpeei kqcndapvsv lqedivgslk stpenhpetp
      601 kkksdpelsk semkqsesrl aeskpnenrl vetkssenkl etkvetqtee lkqnesrtte
      661 ckqnestive pkqnenrlsd tkpndnkqnn grsettksrp etpkqkgesr petpkqksdg
      721 hpetpkqkgd grpetpkqkg esrpetpkqk negrpetpkh rhdnrrdsgk pstekkpevs
      781 khkqdtksds prlkseraea lkqrpdgrsv seslrrdhdn kqksddrges erhrgdqsrv
      841 rrpetlrsss rnehgiksds sktdklerkh rhesgdsrer pssgeqksrp dsprvkqgds
      901 nksrsdklgf ksptskddkr tegnkskvdt nkahpdnkae fpsyllggrs galknfvipk
      961 ikrdkdgnvt qetkkmemkg epkdkvekig lvedlnkgak pvvvlqklsl ddvqklikdr
     1021 edksrsslkp iknkpsksnk gsidqsvlke lppellaeie stmplcervk mnkrkrstvn
     1081 ekpkyaeiss dedndsdeaf essrkrhkkd ddkaweyeer drrssgdhrr sghshegrrs
     1141 sgggryrnrs psdsdmedys pppslsevar kmkkkekqkk rkayepkltp eemmdsstfk
     1201 rftasienil dnledmdfta fgdddeipqe lllgkhqlne lgsesakika mgimdklstd
     1261 ktvkvlnile kniqdgskls tllnhnndte eeerlwrdli mervtksada clttinimts
     1321 pnmpkavyie dvierviqyt kfhlqntlyp qydpvyrldp hgggllsska krakcsthkq
     1381 rvivmlynkv cdivsslsel leiqlltdtt ilqvssmgit pffvenvsel qlcaiklvta
     1441 vfsryekhrq lileeiftsl arlptskrsl rnfrlnssdm dgepmyiqmv talvlqliqc
     1501 vvhlpssekd snaeedsnkk idqdvvitns yetamrtaqn flsiflkkcg skqgeedyrp
     1561 lfenfvqdll stvnkpewpa aelllsllgr llvhqfsnks temalrvasl dylgtvaarl
     1621 rkdavtskmd qgsierilkq vsggedeiqq lqkalldyld entetdpslv fsrkfyiaqw
     1681 frdttletek amksqkdees segthhakei ettgqimhra enrkkflrsi ikttpsqfst
     1741 lkmnsdtvdy ddaclivryl asmrpfaqsf diyltqilrv lgenaiavrt kamkclsevv
     1801 avdpsilarl dmqrgvhgrl mdnstsvrea avellgrfvl crpqlaeqyy dmlierildt
     1861 gisvrkrvik ilrdicieqp tfpkitemcv kmirrvndee gikklvnetf qklwftptph
     1921 ndkeamtrki lnitdvvaac rdtgydwfeq llqnllksee dssykpvkka ctqlvdnlve
     1981 hilkyeesla dsdnkgvnsg rlvacittlf lfskirpqlm vkhamtmqpy lttkcstqnd
     2041 fmvicnvaki lelvvplmeh psetflatie edlmkliiky gmtvvqhcvs clgavvnkvt
     2101 qnfkfvwacf nryygaiskl ksqhqedpnn tslltnkpal lrslftvgal crhfdfdled
     2161 fkgnskvnik dkvlellmyf tkhsdeevqt kaiiglgfaf iqhpslmfeq evknlynnil
     2221 sdknssvnlk iqvlknlqty lqeedtrmqq adrdwkkvak qedlkemgdv ssgmsssimq
     2281 lylkqvleaf fhtqssvrhf alnvialtln qglihpvqcv pyliamgtdp epamrnkadq
     2341 qlveidkkya gfihmkavag mkmsyqvqqa intclkdpvr gfrqdesssa lcshlysmir
     2401 gnrqhrrafl isllnlfddt aktdvtmlly iadnlacfpy qtqeeplfim hhiditlsvs
     2461 gsnllqsfke smvkdkrker ksspskenes sdseeevsrp rksrkrvdsd sdsdseddin
     2521 svmkclpens apliefanvs qgillllmlk qhlknlcgfs dskiqkysps esakvydkai
     2581 nrktgvhfhp kqtldflrsd manskiteev krsivkqyld fkllmehldp deeeeegevs
     2641 astnarnkai tsllgggspk nntaaetedd esdgedrggg tsgvrrrrsq risqrith
//
LOCUS       NP_001362672             389 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform uuu [Homo sapiens].
ACCESSION   NP_001362672
VERSION     NP_001362672.1
DBSOURCE    REFSEQ: accession NM_001375743.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 389)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 389)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 389)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 389)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 389)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2448178.1,
                                           SRR1660809.183570.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..389
                     /product="abl interactor 2 isoform uuu"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=42805
     Region          39..100
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          329..>363
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     CDS             1..389
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375743.1:122..1291"
                     /note="isoform uuu is encoded by transcript variant 78"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqt vdihkekvar reigilttnk
       61 ntsrthkiia panlerpvry irkpidytil ddighgvkvs tqnmkmgglp rttpptqkpp
      121 sppmsgkgtl grhspyrtle pvrppvvpnd yvpsptrnma psqqspvrta svnqrnrtys
      181 ssgssggshp ssrsssrens gsgsvgvpia vptpsppsvf pghpvqfysm nrpasrhtpp
      241 tiggslpyrr ppsitsqtsl qnqmnggpfy sqnpvsdtpp ppppveepvf desppppppp
      301 edyeeeeaav veysdpyaee dppwaprsyl ekvvaiydyt kdkedelsfq egaiiyvikk
      361 nddvlktkqa eseqmdlsai ictmlscld
//
LOCUS       NP_001400237             291 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 2 [Homo sapiens].
ACCESSION   NP_001400237
VERSION     NP_001400237.1
DBSOURCE    REFSEQ: accession NM_001413308.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC103816.2, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.219271.1,
                                           SRR1803612.191929.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968832 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..291
                     /product="RNA-binding Raly-like protein isoform 2"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=32199
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          171..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     Region          199..>244
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     Region          249..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     CDS             1..291
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413308.1:467..1342"
                     /note="isoform 2 is encoded by transcript variant 35"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly rleskepfls
      121 vggyvfdydy yrddfynrlf dyhgrvpppp raviplkrpr vavtttrrgk gvfsmkggsr
      181 stasgstgsk lksdelqtik keltqiktki dsllgrleki ekqqkaeaea qkkqleeslv
      241 liqeecvsei adhsteepae ggpdadgeem tdgieedfde dgghelflqi k
//
LOCUS       NP_001400243             291 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 2 [Homo sapiens].
ACCESSION   NP_001400243
VERSION     NP_001400243.1
DBSOURCE    REFSEQ: accession NM_001413314.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.97619.1,
                                           SRR1803612.156240.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968832 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..291
                     /product="RNA-binding Raly-like protein isoform 2"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=32199
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          171..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     Region          199..>244
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     Region          249..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     CDS             1..291
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413314.1:435..1310"
                     /note="isoform 2 is encoded by transcript variant 41"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly rleskepfls
      121 vggyvfdydy yrddfynrlf dyhgrvpppp raviplkrpr vavtttrrgk gvfsmkggsr
      181 stasgstgsk lksdelqtik keltqiktki dsllgrleki ekqqkaeaea qkkqleeslv
      241 liqeecvsei adhsteepae ggpdadgeem tdgieedfde dgghelflqi k
//
LOCUS       NP_001425936            1038 aa            linear   PRI 21-NOV-2025
DEFINITION  2-oxoglutarate dehydrogenase complex component E1 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001425936 XP_005249816 XP_054214282
VERSION     NP_001425936.1
DBSOURCE    REFSEQ: accession NM_001439007.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1038)
  AUTHORS   Nguyen,T.T., Torrini,C., Shang,E., Shu,C., Mun,J.Y., Gao,Q.,
            Humala,N., Akman,H.O., Zhang,G., Westhoff,M.A., Karpel-Massler,G.,
            Bruce,J.N., Canoll,P. and Siegelin,M.D.
  TITLE     OGDH and Bcl-xL loss causes synthetic lethality in glioblastoma
  JOURNAL   JCI Insight 9 (8), e172565 (2024)
   PUBMED   38483541
  REMARK    GeneRIF: OGDH and Bcl-xL loss causes synthetic lethality in
            glioblastoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1038)
  AUTHORS   Hevler,J.F., Albanese,P., Cabrera-Orefice,A., Potter,A.,
            Jankevics,A., Misic,J., Scheltema,R.A., Brandt,U., Arnold,S. and
            Heck,A.J.R.
  TITLE     MRPS36 provides a structural link in the eukaryotic 2-oxoglutarate
            dehydrogenase complex
  JOURNAL   Open Biol 13 (3), 220363 (2023)
   PUBMED   36854377
REFERENCE   3  (residues 1 to 1038)
  AUTHORS   Whittle,E.F., Chilian,M., Karimiani,E.G., Progri,H., Buhas,D.,
            Kose,M., Ganetzky,R.D., Toosi,M.B., Torbati,P.N., Badv,R.S.,
            Shelihan,I., Yang,H., Elloumi,H.Z., Lee,S., Jamshidi,Y.,
            Pittman,A.M., Houlden,H., Ignatius,E., Rahman,S., Maroofian,R.,
            Yoon,W.H. and Carroll,C.J.
  TITLE     Biallelic variants in OGDH encoding oxoglutarate dehydrogenase lead
            to a neurodevelopmental disorder characterized by global
            developmental delay, movement disorder, and metabolic abnormalities
  JOURNAL   Genet Med 25 (2), 100332 (2023)
   PUBMED   36520152
  REMARK    GeneRIF: Biallelic variants in OGDH encoding oxoglutarate
            dehydrogenase lead to a neurodevelopmental disorder characterized
            by global developmental delay, movement disorder, and metabolic
            abnormalities.
REFERENCE   4  (residues 1 to 1038)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 1038)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 1038)
  AUTHORS   McCartney,R.G., Rice,J.E., Sanderson,S.J., Bunik,V., Lindsay,H. and
            Lindsay,J.G.
  TITLE     Subunit interactions in the mammalian alpha-ketoglutarate
            dehydrogenase complex. Evidence for direct association of the
            alpha-ketoglutarate dehydrogenase and dihydrolipoamide
            dehydrogenase components
  JOURNAL   J Biol Chem 273 (37), 24158-24164 (1998)
   PUBMED   9727038
REFERENCE   7  (residues 1 to 1038)
  AUTHORS   Koike,K.
  TITLE     The gene encoding human 2-oxoglutarate dehydrogenase: structural
            organization and mapping to chromosome 7p13-p14
  JOURNAL   Gene 159 (2), 261-266 (1995)
   PUBMED   7622061
REFERENCE   8  (residues 1 to 1038)
  AUTHORS   Szabo,P., Cai,X., Ali,G. and Blass,J.P.
  TITLE     Localization of the gene (OGDH) coding for the E1k component of the
            alpha-ketoglutarate dehydrogenase complex to chromosome 7p13-p11.2
  JOURNAL   Genomics 20 (2), 324-326 (1994)
   PUBMED   8020988
REFERENCE   9  (residues 1 to 1038)
  AUTHORS   Koike,K., Urata,Y. and Goto,S.
  TITLE     Cloning and nucleotide sequence of the cDNA encoding human
            2-oxoglutarate dehydrogenase (lipoamide)
  JOURNAL   Proc Natl Acad Sci U S A 89 (5), 1963-1967 (1992)
   PUBMED   1542694
REFERENCE   10 (residues 1 to 1038)
  AUTHORS   Reed,L.J. and Hackert,M.L.
  TITLE     Structure-function relationships in dihydrolipoamide
            acyltransferases
  JOURNAL   J Biol Chem 265 (16), 8971-8974 (1990)
   PUBMED   2188967
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011894.3 and AC004859.3.
            
            On or before Apr 25, 2025 this sequence version replaced
            XP_005249816.1, XP_054214282.1.
            
            Summary: This gene encodes one subunit of the 2-oxoglutarate
            dehydrogenase complex. This complex catalyzes the overall
            conversion of 2-oxoglutarate (alpha-ketoglutarate) to succinyl-CoA
            and CO(2) during the Krebs cycle. The protein is located in the
            mitochondrial matrix and uses thiamine pyrophosphate as a cofactor.
            A congenital deficiency in 2-oxoglutarate dehydrogenase activity is
            believed to lead to hypotonia, metabolic acidosis, and
            hyperlactatemia. Alternative splicing results in multiple
            transcript variants encoding distinct isoforms.[provided by RefSeq,
            Sep 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.30074.1,
                                           SRR14372079.1328310.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1038
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..1038
                     /product="2-oxoglutarate dehydrogenase complex component
                     E1 isoform 5"
                     /EC_number="1.2.4.2"
                     /note="oxoglutarate dehydrogenase (succinyl-transferring);
                     oxoglutarate (alpha-ketoglutarate) dehydrogenase
                     (lipoamide); 2-oxoglutarate dehydrogenase, mitochondrial;
                     oxoglutarate decarboxylase; OGDC-E1; 2-oxoglutarate
                     dehydrogenase complex component E1; testicular tissue
                     protein Li 131; alpha-KGDH-E1; thiamine diphosphate
                     (ThDP)-dependent 2-oxoglutarate dehydrogenase"
                     /calculated_mol_wt=113071
     transit_peptide 1..40
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q02218.3)"
                     /calculated_mol_wt=4613
     Region          49..1031
                     /region_name="SucA"
                     /note="2-oxoglutarate dehydrogenase complex, dehydrogenase
                     (E1) component, and related enzymes [Energy production and
                     conversion]; COG0567"
                     /db_xref="CDD:440333"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60597; propagated from
                     UniProtKB/Swiss-Prot (Q02218.3)"
     Site            416
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60597; propagated from
                     UniProtKB/Swiss-Prot (Q02218.3)"
     Site            985
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q02218.3)"
     CDS             1..1038
                     /gene="OGDH"
                     /gene_synonym="AKGDH; E1k; E1o; HsOGDH; KGD1; OGDC;
                     OGDH-E1; OGDH2; OGDHD"
                     /coded_by="NM_001439007.1:55..3171"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:4967"
                     /db_xref="HGNC:HGNC:8124"
                     /db_xref="MIM:613022"
ORIGIN      
        1 mfhlrtcaak lrpltasqtv ktfsqnrpaa artfqqircy sapvaaepfl sgtssnyvee
       61 mycawlenpk svhkswdiff rntnagappg tayqsplpls rgslaavaha qslveaqpnv
      121 dklvedhlav qslirayqir ghhvaqldpl gildadldss vpadiisstd kldlavfker
      181 lrmltvggfy gldesdldkv fhlptttfig gqesalplre iirrlemayc qhigvefmfi
      241 ndleqcqwir qkfetpgimq ftneekrtll arlvrstrfe eflqrkwsse krfglegcev
      301 lipalktiid kssengvdyv imgmphrgrl nvlanvirke leqifcqfds kleaadegsg
      361 dvkyhlgmyh rrinrvtdrn itlslvanps hleaadpvvm gktkaeqfyc gdtegkkvms
      421 illhgdaafa gqgivyetfh lsdlpsytth gtvhvvvnnq igfttdprma rsspyptdva
      481 rvvnapifhv nsddpeavmy vckvaaewrs tfhkdvvvdl vcyrrnghne mdepmftqpl
      541 mykqirkqkp vlqkyaellv sqgvvnqpey eeeiskydki ceeafarskd ekilhikhwl
      601 dspwpgfftl dgqprsmscp stgltedilt hignvassvp venftihggl srilktrgem
      661 vknrtvdwal aeymafgsll kegihirlsg qdvergtfsh rhhvlhdqnv dkrtcipmnh
      721 lwpnqapytv cnsslseygv lgfelgfama spnalvlwea qfgdfhntaq ciidqficpg
      781 qakwvrqngi vlllphgmeg mgpehssarp erflqmcndd pdvlpdlkea nfdinqlydc
      841 nwvvvncstp gnffhvlrrq illpfrkpli iftpksllrh pearssfdem lpgthfqrvi
      901 pedgpaaqnp envkrllfct gkvyydltre rkardmvgqv aitrieqlsp fpfdlllkev
      961 qkypnaelaw cqeehknqgy ydyvkprlrt tisrakpvwy agrdpaaapa tgnkkthlte
     1021 lqrlldtafd ldvfknfs
//
LOCUS       NP_001393992             507 aa            linear   PRI 21-NOV-2025
DEFINITION  merlin isoform 7 [Homo sapiens].
ACCESSION   NP_001393992
VERSION     NP_001393992.1
DBSOURCE    REFSEQ: accession NM_001407063.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 507)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 507)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 507)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 507)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005529.7 and AC004882.3.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3027606.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..507
                     /product="merlin isoform 7"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=58965
     Region          20..>41
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     Region          <37..139
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          133..229
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(175..176,178..184,193,214,217..218,221)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(175,178..185,193,214,217..218,221)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(211,215)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            214..229
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          224..>284
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          263..382
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          435..>496
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..507
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_001407063.1:367..1890"
                     /note="isoform 7 is encoded by transcript variant 25"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 magaiasrms fsslkrkqpk tftvrivtmd aemefncevk kqildekiyc ppeasvllas
       61 yavqakygdy dpsvhkrgfl aqeellpkrv inlyqmtpem weeritawya ehrgrardea
      121 emeylkiaqd lemygvnyfa irnkkgtell lgvdalglhi ydpenrltpk isfpwneirn
      181 isysdkefti kpldkkidvf kfnssklrvn klilqlcign hdlfmrrrka dslevqqmka
      241 qareekarkq merqrlarek qmreeaertr delerrllqm keeatmanea lmrseetadl
      301 laekaqitee eakllaqkaa eaeqemqrik atairteeek rlmeqkvlea evlalkmaee
      361 serrakeadq lkqdlqeare aerrakqkll eiatkptypp mnpipaplpp dipsfnligd
      421 slsfdfkdtd mkrlsmeiek ekveymeksk hlqeqlnelk teiealklke retaldilhn
      481 ensdrggssk hntikkpqaq grrpici
//
LOCUS       NP_001425606            1132 aa            linear   PRI 21-NOV-2025
DEFINITION  ras GTPase-activating protein nGAP isoform 7 [Homo sapiens].
ACCESSION   NP_001425606 XP_047290816 XP_054195677
VERSION     NP_001425606.1
DBSOURCE    REFSEQ: accession NM_001438677.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1132)
  AUTHORS   Zhang,Y., Yang,Y., Hu,X., Wei,B., Shen,Q., Shi,C. and Chen,P.
  TITLE     RAS protein activator-like 2 (RASAL2) initiates peritubular
            capillary rarefaction in hypoxic renal interstitial fibrosis
  JOURNAL   Transl Res 269, 14-30 (2024)
   PUBMED   38453052
  REMARK    GeneRIF: RAS protein activator-like 2 (RASAL2) initiates
            peritubular capillary rarefaction in hypoxic renal interstitial
            fibrosis.
REFERENCE   2  (residues 1 to 1132)
  AUTHORS   Singharajkomron,N., Yodsurang,V., Limprasutr,V., Wattanathamsan,O.,
            Iksen,I., Hayakawa,Y. and Pongrakhananon,V.
  TITLE     CAMSAP2 enhances lung cancer cell metastasis by mediating RASAL2
            degradation
  JOURNAL   Life Sci 338, 122391 (2024)
   PUBMED   38159595
  REMARK    GeneRIF: CAMSAP2 enhances lung cancer cell metastasis by mediating
            RASAL2 degradation.
REFERENCE   3  (residues 1 to 1132)
  AUTHORS   Wills,C., Watts,K., Maughan,T.S., Fisher,D., Al-Tassan,N.A.,
            Houlston,R.S., Escott-Price,V. and Cheadle,J.P.
  TITLE     Germline variation in RASAL2 may predict survival in patients with
            RAS-activated colorectal cancer
  JOURNAL   Genes Chromosomes Cancer 62 (6), 332-341 (2023)
   PUBMED   36790221
  REMARK    GeneRIF: Germline variation in RASAL2 may predict survival in
            patients with RAS-activated colorectal cancer.
REFERENCE   4  (residues 1 to 1132)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 1132)
  AUTHORS   Yue,Y., Wu,K., Qian,W., Zhu,Z., Zhang,S., Zhang,W., Zhang,W.,
            Wu,S., Li,L., Wu,Z., Ma,Q., Xie,K. and Wang,Z.
  TITLE     RASAL2 mediated the enhancement of YAP1/TIAM1 signaling promotes
            malignant phenotypes of pancreatic ductal adenocarcinoma
  JOURNAL   Int J Biol Sci 18 (10), 4245-4259 (2022)
   PUBMED   35844783
  REMARK    GeneRIF: RASAL2 mediated the enhancement of YAP1/TIAM1 signaling
            promotes malignant phenotypes of pancreatic ductal adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1132)
  AUTHORS   Melen,E., Himes,B.E., Brehm,J.M., Boutaoui,N., Klanderman,B.J.,
            Sylvia,J.S. and Lasky-Su,J.
  TITLE     Analyses of shared genetic factors between asthma and obesity in
            children
  JOURNAL   J Allergy Clin Immunol 126 (3), 631-7 (2010)
   PUBMED   20816195
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1132)
  AUTHORS   Shibui,T., Kobayashi,T. and Shiratori,M.
  TITLE     Isolation of cross-reacting antigen candidates by mRNA-display
            using a mixed cDNA library
  JOURNAL   Biotechnol Lett 30 (12), 2037-2043 (2008)
   PUBMED   18633578
REFERENCE   8  (residues 1 to 1132)
  AUTHORS   de Chassey,B., Navratil,V., Tafforeau,L., Hiet,M.S., Aublin-Gex,A.,
            Agaugue,S., Meiffren,G., Pradezynski,F., Faria,B.F., Chantier,T.,
            Le Breton,M., Pellet,J., Davoust,N., Mangeot,P.E., Chaboud,A.,
            Penin,F., Jacob,Y., Vidalain,P.O., Vidal,M., Andre,P.,
            Rabourdin-Combe,C. and Lotteau,V.
  TITLE     Hepatitis C virus infection protein network
  JOURNAL   Mol Syst Biol 4, 230 (2008)
   PUBMED   18985028
REFERENCE   9  (residues 1 to 1132)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 1132)
  AUTHORS   Noto,S., Maeda,T., Hattori,S., Inazawa,J., Imamura,M., Asaka,M. and
            Hatakeyama,M.
  TITLE     A novel human RasGAP-like gene that maps within the prostate cancer
            susceptibility locus at chromosome 1q25
  JOURNAL   FEBS Lett 441 (1), 127-131 (1998)
   PUBMED   9877179
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL365357.12 and AL035702.7.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047290816.1, XP_054195677.1.
            
            Summary: This gene encodes a protein that contains the GAP-related
            domain (GRD), a characteristic domain of GTPase-activating proteins
            (GAPs). GAPs function as activators of Ras superfamily of small
            GTPases. The protein encoded by this gene is able to complement the
            defective RasGAP function in a yeast system. Two alternatively
            spliced transcript variants of this gene encoding distinct isoforms
            have been reported. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.911124.1,
                                           SRR14372079.3228072.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1132
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..1132
                     /product="ras GTPase-activating protein nGAP isoform 7"
                     /note="Ras protein activator like 1; ras GTPase-activating
                     protein nGAP; RASAL2/ACVR1 fusion"
                     /calculated_mol_wt=127651
     Region          1..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Region          34..217
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Region          159..298
                     /region_name="C2_SynGAP_like"
                     /note="C2 domain present in Ras GTPase activating protein
                     (GAP) family; cd04013"
                     /db_xref="CDD:175980"
     Region          289..612
                     /region_name="RasGAP_DAB2IP"
                     /note="Ras-GTPase Activating Domain of DAB2IP and similar
                     proteins; cd05136"
                     /db_xref="CDD:213338"
     Site            order(328,365,367,369..370,372,375,379,471,479..480,
                     483..484,487,508,511..512,515,519,521,526..527)
                     /site_type="other"
                     /note="putative RAS interface [polypeptide binding]"
                     /db_xref="CDD:213338"
     Site            369
                     /site_type="other"
                     /note="Arginine finger, crucial for GTP hydrolysis by
                     stabilizing the transition state.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00167; propagated
                     from UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Region          602..1103
                     /region_name="DUF3498"
                     /note="Domain of unknown function (DUF3498); pfam12004"
                     /db_xref="CDD:463427"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Site            656
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Region          677..697
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Region          744..775
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Region          796..862
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Site            857
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Region          903..946
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Region          1109..1132
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJF2.2)"
     CDS             1..1132
                     /gene="RASAL2"
                     /gene_synonym="NGAP"
                     /coded_by="NM_001438677.1:146..3544"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:9462"
                     /db_xref="HGNC:HGNC:9874"
                     /db_xref="MIM:606136"
ORIGIN      
        1 mqtpevpaer sprrrsisgt stsekpnsmd tantspfkvp gffskrlkgs ikrtksqskl
       61 drntsfrlps lrstddrsrg lpklkesrsh esllspcstv ecldlgrgep vsvkplhssi
      121 lgqdfcfevt ylsgskcfsc nsaserdkwm enlrrtvqpn kdncrraenv lrlwiieakd
      181 lapkkkyfce lclddtlfar ttsktkadni fwgehfeffs lpplhsitvh iykdvekkkk
      241 kdknnyvglv niptasvtgr qfvekwypvs tptpnkgktg gpsiriksrf qtitilpmeq
      301 ykefaefvts nytmlcsvle pvisvrnkee lacalvhilq stgrakdflt dlvmsevdrc
      361 gehdvlifre ntiatksiee ylklvgqqyl hdalgefika lyesdencev dpskcsssel
      421 idhqsnlkmc celafckiin sycvfprelk evfaswkqqc lnrgkqdise rlisaslflr
      481 flcpaimsps lfnlmqeypd drtsrtltli akviqnlanf akfgnkeeym afmndflehe
      541 wggmkrflle isnpdtisnt pgfdgyidlg relsvlhsll wevvsqldka tvaklgplpr
      601 vladitkslt nptpiqqqlr rftehnsspn vsgslssglq kifedptdsd lhklkspsqd
      661 ntdsyfrgkt lllvqqassq smtysekder esslpngrsv slmdlqdtha aqvehasvml
      721 dvpirltgsq lsitqvasik qlretqstpq sapqvrrplh palnqpgglq plsfqnpvyh
      781 lnnpipampk asidsslenl stassrsqsn sedfklsgps nssmedftkr stqsedfsrr
      841 htvpdrhipl alprqnstgq aqirkvdqgg lgarakapps lphsaslrst gsmsvvsaal
      901 vaepvqngsr srqqssssre spvpkvraiq rqqtqqvqsp vdsatmspve rtaawvlnng
      961 qyeedveete qnldeakhae kyeqeitklk erlrvssrrl eeyerrllvq eqqmqkllle
     1021 ykarledsee rlrrqqeekd sqmksiisrl maveeelkkd haemqavida kqkiidaqek
     1081 rivsldsant rlmsaltqvk erysmqvrng isptnptkls itengefkns sc
//
LOCUS       NP_001425738             950 aa            linear   PRI 21-NOV-2025
DEFINITION  NHS-like protein 2 isoform 6 [Homo sapiens].
ACCESSION   NP_001425738 XP_047298027 XP_054182946
VERSION     NP_001425738.1
DBSOURCE    REFSEQ: accession NM_001438809.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 950)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 950)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 950)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL929401.8 and BX119917.9.
            
            On or before Apr 24, 2025 this sequence version replaced
            XP_047298027.1, XP_054182946.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.977216.1,
                                           SRR14038191.2432553.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..950
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..950
                     /product="NHS-like protein 2 isoform 6"
                     /note="NHS-like protein 2; TPT1-like protein"
                     /calculated_mol_wt=101880
     Region          <264..480
                     /region_name="NHS"
                     /note="NHS-like; pfam15273"
                     /db_xref="CDD:464606"
     Region          <446..680
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..950
                     /gene="NHSL2"
                     /coded_by="NM_001438809.1:535..3387"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:340527"
                     /db_xref="HGNC:HGNC:33737"
                     /db_xref="MIM:301093"
ORIGIN      
        1 mmgnshhkqp rsksqsrmhs atghsnspag svahsttsdi rpshsvpegv hgrvavgqda
       61 rfpsltspvl rtpssepdep hqarsgpnpp gmesmgmvys vpsscngpte stfstswkgd
      121 aftymtpsat sqsnqvneng knpscgnswv slnkvpplvp keaatllvar dnpagcsgsa
      181 gyperliqqr hmperpskig lltsgtsrle tgpggasrfr erslsvptds gttdvdydee
      241 qkaneacalp fastssegsn sadniaslsa qqeaqhrrqr sksislrkak kkpspptrsv
      301 slvkdepgll peggsalpkd qrpkslclsl ehqghhsshp daqghpaipn hkdpestqfs
      361 hhwyltdwks gdtyqslsss statgttvie ctqvqgsses laspstsrat tpsqlsieve
      421 areisspgrp pglmspssgy ssqsetptpt vsmsltlghl pppsssvrvr pvvperkssl
      481 pptspmekfp ksrlsfdlpl tsspnldlsg msisirsktk vsrhhsetnf gvklaqktnp
      541 nqpimpmvtq sdlrsvrlrs vsksepeddi espeyaeepr aeevftlper ktkppvaekp
      601 pvarrppslv hkppsvpeey altsptlamp prssiqharp lpqdsytvvr kpkpssfpdg
      661 rspgestaps slvftpfass sdaffsgtqq ppqgsvedeg pkvrvlperi slqsqeeaek
      721 kkgkipppvp kkpsvlylpl tsptaqmeay vaeprlplsp iitleedtkc patgddlqsl
      781 gqrvtstpqa dsereasplg ssvepgteek slisdktaew iaeddddvfv asrttedlft
      841 vihrskrkll gwkepgeafv ggrtsshspi kntaespise statagsgss anldagrndd
      901 fkallqkkgs katprsrpsa aellkttnpl arriiaqfsk dyettdnpst
//
LOCUS       NP_001401234             455 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 3 isoform 5
            precursor [Homo sapiens].
ACCESSION   NP_001401234
VERSION     NP_001401234.1
DBSOURCE    REFSEQ: accession NM_001414305.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Tang,Q., Yuan,Y., Li,L., Xu,Y., Ji,W., Xiao,S., Han,Y., Miao,W.,
            Cai,J., You,P., Chen,M., Ding,S., Li,Z., Qi,Z., Hou,W. and Luo,H.
  TITLE     Comprehensive analysis reveals that LTBR is a immune-related
            biomarker for glioma
  JOURNAL   Comput Biol Med 174, 108457 (2024)
   PUBMED   38599071
  REMARK    GeneRIF: Comprehensive analysis reveals that LTBR is a
            immune-related biomarker for glioma.
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Wu,Y., Zhao,S., Guo,W., Liu,Y., Requena Mullor,M.D.M.,
            Rodriguez,R.A. and Wei,R.
  TITLE     Systematic analysis of the prognostic value and immunological
            function of LTBR in human cancer
  JOURNAL   Aging (Albany NY) 16 (1), 129-152 (2024)
   PUBMED   38175686
  REMARK    GeneRIF: Systematic analysis of the prognostic value and
            immunological function of LTBR in human cancer.
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Shuptrine,C.W., Perez,V.M., Selitsky,S.R., Schreiber,T.H. and
            Fromm,G.
  TITLE     Shining a LIGHT on myeloid cell targeted immunotherapy
  JOURNAL   Eur J Cancer 187, 147-160 (2023)
   PUBMED   37167762
  REMARK    Review article
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Abudukeyoumu,A., Lai,Z.Z., Lu,J.J., Zhang,X., Hou,D.Y., Dong,J.,
            Wu,J.N., Li,M.Q. and Xie,F.
  TITLE     A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion
  JOURNAL   J Reprod Immunol 153, 103693 (2022)
   PUBMED   35987137
  REMARK    GeneRIF: A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion.
REFERENCE   5  (residues 1 to 455)
  AUTHORS   Remouchamps,C., Boutaffala,L., Ganeff,C. and Dejardin,E.
  TITLE     Biology and signal transduction pathways of the
            Lymphotoxin-alphabeta/LTbetaR system
  JOURNAL   Cytokine Growth Factor Rev 22 (5-6), 301-310 (2011)
   PUBMED   22152226
  REMARK    Review article
REFERENCE   6  (residues 1 to 455)
  AUTHORS   Nakano,H., Oshima,H., Chung,W., Williams-Abbott,L., Ware,C.F.,
            Yagita,H. and Okumura,K.
  TITLE     TRAF5, an activator of NF-kappaB and putative signal transducer for
            the lymphotoxin-beta receptor
  JOURNAL   J Biol Chem 271 (25), 14661-14664 (1996)
   PUBMED   8663299
REFERENCE   7  (residues 1 to 455)
  AUTHORS   Browning,J.L., Miatkowski,K., Sizing,I., Griffiths,D., Zafari,M.,
            Benjamin,C.D., Meier,W. and Mackay,F.
  TITLE     Signaling through the lymphotoxin beta receptor induces the death
            of some adenocarcinoma tumor lines
  JOURNAL   J Exp Med 183 (3), 867-878 (1996)
   PUBMED   8642291
REFERENCE   8  (residues 1 to 455)
  AUTHORS   Baens,M., Aerssens,J., van Zand,K., Van den Berghe,H. and
            Marynen,P.
  TITLE     Isolation and regional assignment of human chromosome 12p cDNAs
  JOURNAL   Genomics 29 (1), 44-52 (1995)
   PUBMED   8530100
REFERENCE   9  (residues 1 to 455)
  AUTHORS   Crowe,P.D., VanArsdale,T.L., Walter,B.N., Ware,C.F., Hession,C.,
            Ehrenfels,B., Browning,J.L., Din,W.S., Goodwin,R.G. and Smith,C.A.
  TITLE     A lymphotoxin-beta-specific receptor
  JOURNAL   Science 264 (5159), 707-710 (1994)
   PUBMED   8171323
REFERENCE   10 (residues 1 to 455)
  AUTHORS   Baens,M., Chaffanet,M., Cassiman,J.J., van den Berghe,H. and
            Marynen,P.
  TITLE     Construction and evaluation of a hncDNA library of human 12p
            transcribed sequences derived from a somatic cell hybrid
  JOURNAL   Genomics 16 (1), 214-218 (1993)
   PUBMED   8486360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005840.2.
            
            Summary: This gene encodes a member of the tumor necrosis factor
            receptor superfamily. The major ligands of this receptor include
            lymphotoxin alpha/beta and tumor necrosis factor ligand superfamily
            member 14. The encoded protein plays a role in signalling during
            the development of lymphoid and other organs, lipid metabolism,
            immune response, and programmed cell death. Activity of this
            receptor has also been linked to carcinogenesis. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.618565.1,
                                           SRR14038192.2657960.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153307, SAMEA2153347
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..455
                     /product="tumor necrosis factor receptor superfamily
                     member 3 isoform 5 precursor"
                     /note="tumor necrosis factor C receptor; lymphotoxin B
                     receptor; tumor necrosis factor receptor type III;
                     lymphotoxin beta receptor (TNFR superfamily, member 3);
                     tumor necrosis factor receptor 2-related protein"
                     /calculated_mol_wt=45639
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3049
     Region          11..188
                     /region_name="TNFRSF3"
                     /note="Tumor necrosis factor receptor superfamily member 3
                     (TNFRSF3), also known as lymphotoxin beta receptor (LTBR);
                     cd10578"
                     /db_xref="CDD:276904"
     Region          22..80
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276904"
     Region          83..124
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276904"
     Region          126..187
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276904"
     Region          <186..>230
                     /region_name="TNFRSF"
                     /note="Tumor necrosis factor receptor superfamily
                     (TNFRSF); cl22855"
                     /db_xref="CDD:473981"
     Region          190..230
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276900"
     CDS             1..455
                     /gene="LTBR"
                     /gene_synonym="D12S370; LT-BETA-R; TNF-R-III; TNFCR;
                     TNFR-RP; TNFR2-RP; TNFR3; TNFRSF3"
                     /coded_by="NM_001414305.1:198..1565"
                     /note="isoform 5 precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:4055"
                     /db_xref="HGNC:HGNC:6718"
                     /db_xref="MIM:600979"
ORIGIN      
        1 mllpwatsap glawgplvlg lfgllaasqp qavppyasen qtcrdqekey yepqhriccs
       61 rcppgtyvsa kcsrirdtvc atcaensyne hwnylticql crpcdpvmgl eeiapctskr
      121 ktqcrcqpgm fcaawalect hcellsdcpp gteaelkeah rrvleghgtg tgagdtgdev
      181 gkgnnhcvpc kaghfqntss psarcqphtr cenqglveaa pgtaqsdttc knpleplppe
      241 msgtmlmlav llplafflll atvfsciwks hpslcrklgs llkrrpqgeg pnpvagswep
      301 pkahpyfpdl vqpllpisgd vspvstglpa apvleagvpq qqspldltre pqlepgeqsq
      361 vahgtngihv tggsmtitgn iyiyngpvlg gppgpgdlpa tpeppypipe egdpgppgls
      421 tphqedgkaw hlaetehcga tpsnrgprnq fithd
//
LOCUS       NP_001426133             212 aa            linear   PRI 21-NOV-2025
DEFINITION  programmed cell death protein 10 [Homo sapiens].
ACCESSION   NP_001426133 XP_005247145 XP_054201076
VERSION     NP_001426133.1
DBSOURCE    REFSEQ: accession NM_001439204.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Li,Y., Liu,Y., Liu,K., Tao,T., Yang,L., Liu,R., Zhou,H., Liang,D.,
            Zhang,Y., Huang,D. and Sun,Y.
  TITLE     Study on the role of CCM3 gene and lead exposure induced
            neurotoxicity through neurovascular units
  JOURNAL   Ecotoxicol Environ Saf 277, 116269 (2024)
   PUBMED   38657460
  REMARK    GeneRIF: Study on the role of CCM3 gene and lead exposure induced
            neurotoxicity through neurovascular units.
REFERENCE   3  (residues 1 to 212)
  AUTHORS   da Fontoura Galvao,G., da Silva,E.V., Trefilio,L.M.,
            Alves-Leon,S.V., Fontes-Dantas,F.L. and de Souza,J.M.
  TITLE     Comprehensive CCM3 Mutational Analysis in Two Patients with
            Syndromic Cerebral Cavernous Malformation
  JOURNAL   Transl Stroke Res 15 (2), 411-421 (2024)
   PUBMED   36723700
  REMARK    GeneRIF: Comprehensive CCM3 Mutational Analysis in Two Patients
            with Syndromic Cerebral Cavernous Malformation.
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Tang,L., Zhou,M., Xu,Y., Peng,B., Gao,Y. and Mo,Y.
  TITLE     Knockdown of CCM3 promotes angiogenesis through activation and
            nuclear translocation of YAP/TAZ
  JOURNAL   Biochem Biophys Res Commun 701, 149525 (2024)
   PUBMED   38320423
  REMARK    GeneRIF: Knockdown of CCM3 promotes angiogenesis through activation
            and nuclear translocation of YAP/TAZ.
REFERENCE   5  (residues 1 to 212)
  AUTHORS   Ni,W.J. and Leng,X.M.
  TITLE     Programmed cell death 10 can be used as a potential biomarker for
            ankylosing spondylitis diagnosis and treatment
  JOURNAL   Spinal Cord 62 (3), 99-103 (2024)
   PUBMED   38158408
  REMARK    GeneRIF: Programmed cell death 10 can be used as a potential
            biomarker for ankylosing spondylitis diagnosis and treatment.
REFERENCE   6  (residues 1 to 212)
  AUTHORS   Guclu,B., Ozturk,A.K., Pricola,K.L., Bilguvar,K., Shin,D.,
            O'Roak,B.J. and Gunel,M.
  TITLE     Mutations in apoptosis-related gene, PDCD10, cause cerebral
            cavernous malformation 3
  JOURNAL   Neurosurgery 57 (5), 1008-1013 (2005)
   PUBMED   16284570
  REMARK    GeneRIF: Mutations in apoptosis-related gene, PDCD10, cause
            cerebral cavernous malformation 3.
REFERENCE   7  (residues 1 to 212)
  AUTHORS   Guclu,B., Ozturk,A.K., Pricola,K.L., Seker,A., Ozek,M. and Gunel,M.
  TITLE     Cerebral venous malformations have distinct genetic origin from
            cerebral cavernous malformations
  JOURNAL   Stroke 36 (11), 2479-2480 (2005)
   PUBMED   16239636
  REMARK    GeneRIF: KRIT1, Malcavernin, and PDCD10 are differentially
            expressed in cerebral venous malformations and cerebral cavernous
            malformations
REFERENCE   8  (residues 1 to 212)
  AUTHORS   Bergametti,F., Denier,C., Labauge,P., Arnoult,M., Boetto,S.,
            Clanet,M., Coubes,P., Echenne,B., Ibrahim,R., Irthum,B.,
            Jacquet,G., Lonjon,M., Moreau,J.J., Neau,J.P., Parker,F.,
            Tremoulet,M. and Tournier-Lasserve,E.
  CONSRTM   Societe Francaise de Neurochirurgie
  TITLE     Mutations within the programmed cell death 10 gene cause cerebral
            cavernous malformations
  JOURNAL   Am J Hum Genet 76 (1), 42-51 (2005)
   PUBMED   15543491
  REMARK    GeneRIF: We report herein the identification of PDCD10 (programmed
            cell death 10) as the CCM3 gene.
REFERENCE   9  (residues 1 to 212)
  AUTHORS   Craig,H.D., Gunel,M., Cepeda,O., Johnson,E.W., Ptacek,L.,
            Steinberg,G.K., Ogilvy,C.S., Berg,M.J., Crawford,S.C., Scott,R.M.,
            Steichen-Gersdorf,E., Sabroe,R., Kennedy,C.T., Mettler,G.,
            Beis,M.J., Fryer,A., Awad,I.A. and Lifton,R.P.
  TITLE     Multilocus linkage identifies two new loci for a mendelian form of
            stroke, cerebral cavernous malformation, at 7p15-13 and 3q25.2-27
  JOURNAL   Hum Mol Genet 7 (12), 1851-1858 (1998)
   PUBMED   9811928
REFERENCE   10 (residues 1 to 212)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079822.13.
            
            On or before Apr 28, 2025 this sequence version replaced
            XP_005247145.1, XP_054201076.1.
            
            Summary: This gene encodes an evolutionarily conserved protein
            associated with cell apoptosis. The protein interacts with the
            serine/threonine protein kinase MST4 to modulate the extracellular
            signal-regulated kinase (ERK) pathway. It also interacts with and
            is phosphoryated by serine/threonine kinase 25, and is thought to
            function in a signaling pathway essential for vascular developent.
            Mutations in this gene are one cause of cerebral cavernous
            malformations, which are vascular malformations that cause seizures
            and cerebral hemorrhages. Multiple alternatively spliced variants,
            encoding the same protein, have been identified. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BQ214640.1, SRR14038196.76779.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146, SAMN03267758
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.1"
     Protein         1..212
                     /product="programmed cell death protein 10"
                     /note="apoptosis-related protein 15; TF-1 cell
                     apoptosis-related protein 15; cerebral cavernous
                     malformations 3 protein"
                     /calculated_mol_wt=24571
     Region          14..161
                     /region_name="DUF1241"
                     /note="Protein of unknown function (DUF1241); pfam06840"
                     /db_xref="CDD:462018"
     Site            179
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BUL8.1)"
     CDS             1..212
                     /gene="PDCD10"
                     /gene_synonym="CCM3; TFAR15"
                     /coded_by="NM_001439204.1:173..811"
                     /db_xref="GeneID:11235"
                     /db_xref="HGNC:HGNC:8761"
                     /db_xref="MIM:609118"
ORIGIN      
        1 mrmtmeemkn eaettsmvsm plyavmypvf nelervnlsa aqtlraafik aekenpgltq
       61 diimkilekk svevnftesl lrmaaddvee ymierpepef qdlnekaral kqilskipde
      121 indrvrflqt ikdiasaike lldtvnnvfk kyqyqnrral ehqkkefvky sksfsdtlkt
      181 yfkdgkainv fvsanrlihq tnlilqtfkt va
//
LOCUS       NP_001307540             529 aa            linear   PRI 21-NOV-2025
DEFINITION  importin subunit alpha-1 [Homo sapiens].
ACCESSION   NP_001307540 XP_011523085
VERSION     NP_001307540.1
DBSOURCE    REFSEQ: accession NM_001320611.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Lange,A., Mills,R.E., Lange,C.J., Stewart,M., Devine,S.E. and
            Corbett,A.H.
  TITLE     Classical nuclear localization signals: definition, function, and
            interaction with importin alpha
  JOURNAL   J Biol Chem 282 (8), 5101-5105 (2007)
   PUBMED   17170104
  REMARK    Review article
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Teng,S.C., Wu,K.J., Tseng,S.F., Wong,C.W. and Kao,L.
  TITLE     Importin KPNA2, NBS1, DNA repair and tumorigenesis
  JOURNAL   J Mol Histol 37 (5-7), 293-299 (2006)
   PUBMED   16752129
  REMARK    GeneRIF: This review focuses on recent experimental evidences
            demonstrating how NBS1 is translocated into the nucleus by an
            importin KPNA2 which mediates NBS1 subcellular localization and the
            functions of the NBS1 complex in tumorigenesis.
            Review article
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Dorr,S.N., Schlicker,M.N. and Hansmann,I.N.
  TITLE     Genomic structure of karyopherin alpha2 (KPNA2) within a low-copy
            repeat on chromosome 17q23-q24 and mutation analysis in patients
            with Russell-Silver syndrome
  JOURNAL   Hum Genet 109 (5), 479-486 (2001)
   PUBMED   11735022
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Herold,A., Truant,R., Wiegand,H. and Cullen,B.R.
  TITLE     Determination of the functional domain organization of the importin
            alpha nuclear import factor
  JOURNAL   J Cell Biol 143 (2), 309-318 (1998)
   PUBMED   9786944
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Weis,K., Ryder,U. and Lamond,A.I.
  TITLE     The conserved amino-terminal domain of hSRP1 alpha is essential for
            nuclear protein import
  JOURNAL   EMBO J 15 (8), 1818-1825 (1996)
   PUBMED   8617227
REFERENCE   7  (residues 1 to 529)
  AUTHORS   Moroianu,J., Hijikata,M., Blobel,G. and Radu,A.
  TITLE     Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers:
            alpha 1 or alpha 2 subunit binds nuclear localization signal and
            beta subunit interacts with peptide repeat-containing nucleoporins
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6532-6536 (1995)
   PUBMED   7604027
REFERENCE   8  (residues 1 to 529)
  AUTHORS   Weis,K., Mattaj,I.W. and Lamond,A.I.
  TITLE     Identification of hSRP1 alpha as a functional receptor for nuclear
            localization sequences
  JOURNAL   Science 268 (5213), 1049-1053 (1995)
   PUBMED   7754385
REFERENCE   9  (residues 1 to 529)
  AUTHORS   Cuomo,C.A., Kirch,S.A., Gyuris,J., Brent,R. and Oettinger,M.A.
  TITLE     Rch1, a protein that specifically interacts with the RAG-1
            recombination-activating protein
  JOURNAL   Proc Natl Acad Sci U S A 91 (13), 6156-6160 (1994)
   PUBMED   8016130
REFERENCE   10 (residues 1 to 529)
  AUTHORS   Bukrinsky,M.I., Sharova,N., Dempsey,M.P., Stanwick,T.L.,
            Bukrinskaya,A.G., Haggerty,S. and Stevenson,M.
  TITLE     Active nuclear import of human immunodeficiency virus type 1
            preintegration complexes
  JOURNAL   Proc Natl Acad Sci U S A 89 (14), 6580-6584 (1992)
   PUBMED   1631159
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC134407.6.
            
            On Mar 2, 2016 this sequence version replaced XP_011523085.1.
            
            Summary: The import of proteins into the nucleus is a process that
            involves at least 2 steps. The first is an energy-independent
            docking of the protein to the nuclear envelope and the second is an
            energy-dependent translocation through the nuclear pore complex.
            Imported proteins require a nuclear localization sequence (NLS)
            which generally consists of a short region of basic amino acids or
            2 such regions spaced about 10 amino acids apart. Proteins involved
            in the first step of nuclear import have been identified in
            different systems. These include the Xenopus protein importin and
            its yeast homolog, SRP1 (a suppressor of certain
            temperature-sensitive mutations of RNA polymerase I in
            Saccharomyces cerevisiae), which bind to the NLS. KPNA2 protein
            interacts with the NLSs of DNA helicase Q1 and SV40 T antigen and
            may be involved in the nuclear transport of proteins. KPNA2 also
            may play a role in V(D)J recombination. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Feb
            2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC067848.1, SRR14038191.4291241.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..529
                     /product="importin subunit alpha-1"
                     /note="importin-alpha-P1; pendulin; importin subunit
                     alpha-2; RAG cohort protein 1; karyopherin alpha 2 (RAG
                     cohort 1, importin alpha 1); nuclear pore-targeting
                     complex 58kD component"
                     /calculated_mol_wt=57731
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P52292.1)"
     Region          10..528
                     /region_name="SRP1"
                     /note="Karyopherin (importin) alpha [Intracellular
                     trafficking and secretion]; COG5064"
                     /db_xref="CDD:227396"
     Region          43..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          45..54
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52292.1)"
     Region          71..111
                     /region_name="ARM 1, truncated"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          112..151
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          115..147
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(138,142,146,180,184,188,227,231,235)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          142..238
                     /region_name="NLS binding site (major).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          155..191
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          197..236
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          200..244
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          246..282
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          253..278
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(269,273,277,311,315,319,353,357,361)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          283..322
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          286..322
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          315..403
                     /region_name="NLS binding site (minor).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          328..362
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          367..409
                     /region_name="ARM 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          370..404
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          410..456
                     /region_name="ARM 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          413..447
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          457..496
                     /region_name="ARM 10, atypical"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          460..495
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P52292.1)"
     CDS             1..529
                     /gene="KPNA2"
                     /gene_synonym="IPOA1; PTAC58; QIP2; RCH1; SRP1-alpha;
                     SRP1alpha"
                     /coded_by="NM_001320611.3:846..2435"
                     /db_xref="CCDS:CCDS32713.1"
                     /db_xref="GeneID:3838"
                     /db_xref="HGNC:HGNC:6395"
                     /db_xref="MIM:600685"
ORIGIN      
        1 mstnenantp aarlhrfknk gkdstemrrr rievnvelrk akkddqmlkr rnvssfpdda
       61 tsplqenrnn qgtvnwsvdd ivkginssnv enqlqatqaa rkllsrekqp pidniiragl
      121 ipkfvsflgr tdcspiqfes awaltniasg tseqtkavvd ggaipafisl lasphahise
      181 qavwalgnia gdgsvfrdlv ikygavdpll allavpdmss lacgylrnlt wtlsnlcrnk
      241 npappidave qilptlvrll hhddpevlad tcwaisyltd gpnerigmvv ktgvvpqlvk
      301 llgaselpiv tpalraigni vtgtdeqtqv vidagalavf pslltnpktn iqkeatwtms
      361 nitagrqdqi qqvvnhglvp flvsvlskad fktqkeavwa vtnytsggtv eqivylvhcg
      421 iieplmnllt akdtkiilvi ldaisnifqa aeklgetekl simieecggl dkiealqnhe
      481 nesvykasls liekyfsvee eedqnvvpet tsegytfqvq dgapgtfnf
//
LOCUS       NP_001400845             338 aa            linear   PRI 21-NOV-2025
DEFINITION  transcription factor ETV6 isoform 5 [Homo sapiens].
ACCESSION   NP_001400845
VERSION     NP_001400845.1
DBSOURCE    REFSEQ: accession NM_001413916.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Xu,W., Tian,F., Tai,X., Song,G., Liu,Y., Fan,L., Weng,X., Yang,E.,
            Wang,M., Bornhauser,M., Zhang,C., Lock,R.B., Wong,J.W.H., Wang,J.,
            Jing,D. and Mi,J.Q.
  TITLE     ETV6::ACSL6 translocation-driven super-enhancer activation leads to
            eosinophilia in acute lymphoblastic leukemia through IL-3
            overexpression
  JOURNAL   Haematologica 109 (8), 2445-2458 (2024)
   PUBMED   38356460
  REMARK    GeneRIF: ETV6::ACSL6 translocation-driven super-enhancer activation
            leads to eosinophilia in acute lymphoblastic leukemia through IL-3
            overexpression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Xue,S., Sun,H.P., Huang,X.B., Chen,X., Wang,T., Ma,W., Tian,Y.,
            Pan,Z.L., Li,L.H., Zhang,L., Liu,H.X. and Cao,X.Y.
  TITLE     Characteristics and literature review of ETV6::ABL1 fusion
            gene-positive acute myeloid leukemia
  JOURNAL   Int J Hematol 119 (5), 564-572 (2024)
   PUBMED   38441775
  REMARK    GeneRIF: Characteristics and literature review of ETV6::ABL1 fusion
            gene-positive acute myeloid leukemia.
            Review article
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Mueller,S.B., Pikman,Y., Tasian,S.K., Silverman,L.B., Harris,M.H.
            and Tsai,H.K.
  TITLE     ETV6 fusions from insertions of exons 3-5 in pediatric hematologic
            malignancies
  JOURNAL   Haematologica 108 (12), 3471-3476 (2023)
   PUBMED   37381775
  REMARK    GeneRIF: ETV6 fusions from insertions of exons 3-5 in pediatric
            hematologic malignancies.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Klubickova,N., Mosaieby,E., Ptakova,N., Trinquet,A., Lae,M.,
            Costes-Martineau,V. and Skalova,A.
  TITLE     High-grade non-intestinal type sinonasal adenocarcinoma with
            ETV6::NTRK3 fusion, distinct from secretory carcinoma by
            immunoprofile and morphology
  JOURNAL   Virchows Arch 483 (2), 187-195 (2023)
   PUBMED   37415052
  REMARK    GeneRIF: High-grade non-intestinal type sinonasal adenocarcinoma
            with ETV6::NTRK3 fusion, distinct from secretory carcinoma by
            immunoprofile and morphology.
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Romana,S.P., Mauchauffe,M., Le Coniat,M., Chumakov,I., Le
            Paslier,D., Berger,R. and Bernard,O.A.
  TITLE     The t(12;21) of acute lymphoblastic leukemia results in a tel-AML1
            gene fusion
  JOURNAL   Blood 85 (12), 3662-3670 (1995)
   PUBMED   7780150
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Golub,T.R., Barker,G.F., Bohlander,S.K., Hiebert,S.W., Ward,D.C.,
            Bray-Ward,P., Morgan,E., Raimondi,S.C., Rowley,J.D. and
            Gilliland,D.G.
  TITLE     Fusion of the TEL gene on 12p13 to the AML1 gene on 21q22 in acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 92 (11), 4917-4921 (1995)
   PUBMED   7761424
REFERENCE   8  (residues 1 to 338)
  AUTHORS   Buijs,A., Sherr,S., van Baal,S., van Bezouw,S., van der Plas,D.,
            Geurts van Kessel,A., Riegman,P., Lekanne Deprez,R., Zwarthoff,E.,
            Hagemeijer,A. et al.
  TITLE     Translocation (12;22) (p13;q11) in myeloproliferative disorders
            results in fusion of the ETS-like TEL gene on 12p13 to the MN1 gene
            on 22q11
  JOURNAL   Oncogene 10 (8), 1511-1519 (1995)
   PUBMED   7731705
  REMARK    Erratum:[Oncogene 1995 Aug 17;11(4):809]
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Pencheva,B., Di Paola,J. and Porter,C.C.
  TITLE     ETV6-Related Thrombocytopenia and Predisposition to Leukemia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   33226740
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Fainstein,E., Einat,M., Gokkel,E., Marcelle,C., Croce,C.M.,
            Gale,R.P. and Canaani,E.
  TITLE     Nucleotide sequence analysis of human abl and bcr-abl cDNAs
  JOURNAL   Oncogene 4 (12), 1477-1481 (1989)
   PUBMED   2687768
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007450.1, AC084430.13 and
            AC084358.19.
            
            Summary: This gene encodes an ETS family transcription factor. The
            product of this gene contains two functional domains: a N-terminal
            pointed (PNT) domain that is involved in protein-protein
            interactions with itself and other proteins, and a C-terminal
            DNA-binding domain. Gene knockout studies in mice suggest that it
            is required for hematopoiesis and maintenance of the developing
            vascular network. This gene is known to be involved in a large
            number of chromosomal rearrangements associated with leukemia and
            congenital fibrosarcoma. [provided by RefSeq, Sep 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2393966.1, EL734454.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..338
                     /product="transcription factor ETV6 isoform 5"
                     /note="ets variant gene 6 (TEL oncogene); TEL1 oncogene;
                     transcription factor ETV6; ETS-related protein Tel1;
                     ETV6-RUNX1 fusion protein"
                     /calculated_mol_wt=38735
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            11..12
                     /site_type="other"
                     /note="Breakpoint for translocation to form CHIC2-ETV6 in
                     AML; propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12435397,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            54..55
                     /site_type="other"
                     /note="Breakpoint for translocation to form ETV6-MDS2 in
                     MDS; propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            55..56
                     /site_type="other"
                     /note="Breakpoint for translocation to form PAX5-ETV6;
                     propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Region          56..123
                     /region_name="SAM_PNT-Tel_Yan"
                     /note="Sterile alpha motif (SAM)/Pointed domain of Tel/Yan
                     protein; cd08535"
                     /db_xref="CDD:176085"
     Site            order(63,85,88..90,92..93,96,98,100..101,104..105)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:176085"
     Site            order(75..80,107..109,111..112,115..116)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:176085"
     Region          158..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97360; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14.
                     /evidence=ECO:0000269|PubMed:12435397; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            302
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97360; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     CDS             1..338
                     /gene="ETV6"
                     /gene_synonym="TEL; TEL/ABL; THC5"
                     /coded_by="NM_001413916.1:455..1471"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:2120"
                     /db_xref="HGNC:HGNC:3495"
                     /db_xref="MIM:600618"
ORIGIN      
        1 msetpaqcsi kqerisytpp espvpsyass tplhvpvpra lrmeedsirl pahlrlqpiy
       61 wsrddvaqwl kwaenefslr pidsntfemn gkalllltke dfryrsphsg dvlyellqhi
      121 lkqrkprilf spffhpgnsi htqpevilhq nheedncvqr tprpsvdnvh hnpptiellh
      181 rsrspittnh rpspdpeqrp lrspldnmir rlspaeraqg prphqennhq esyplsvspm
      241 ennhcpasse shpkpssprq estrviqlmp spimhpliln prhsvdfkqs rlsedglhre
      301 gkpinlshre dlaymnhimv svsppeeham pigriage
//
LOCUS       NP_001305256             823 aa            linear   PRI 21-NOV-2025
DEFINITION  dynamin-binding protein isoform c [Homo sapiens].
ACCESSION   NP_001305256
VERSION     NP_001305256.2
DBSOURCE    REFSEQ: accession NM_001318327.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 823)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 823)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 823)
  AUTHORS   Ouyang,C., Mu,J., Lu,Q., Li,J., Zhu,H., Wang,Q., Zou,M.H. and
            Xie,Z.
  TITLE     Autophagic degradation of KAT2A/GCN5 promotes directional migration
            of vascular smooth muscle cells by reducing TUBA/alpha-tubulin
            acetylation
  JOURNAL   Autophagy 16 (10), 1753-1770 (2020)
   PUBMED   31878840
  REMARK    GeneRIF: Autophagic degradation of KAT2A/GCN5 promotes directional
            migration of vascular smooth muscle cells by reducing
            TUBA/alpha-tubulin acetylation.
REFERENCE   5  (residues 1 to 823)
  AUTHORS   Ansar,M., Chung,H.L., Taylor,R.L., Nazir,A., Imtiaz,S.,
            Sarwar,M.T., Manousopoulou,A., Makrythanasis,P., Saeed,S.,
            Falconnet,E., Guipponi,M., Pournaras,C.J., Ansari,M.A., Ranza,E.,
            Santoni,F.A., Ahmed,J., Shah,I., Gul,K., Black,G.C., Bellen,H.J.
            and Antonarakis,S.E.
  TITLE     Bi-allelic Loss-of-Function Variants in DNMBP Cause Infantile
            Cataracts
  JOURNAL   Am J Hum Genet 103 (4), 568-578 (2018)
   PUBMED   30290152
  REMARK    GeneRIF: DNMBP loss-of-function variants cause infantile-onset
            cataracts in humans.
REFERENCE   6  (residues 1 to 823)
  AUTHORS   Minster,R.L., DeKosky,S.T. and Kamboh,M.I.
  TITLE     No association of dynamin binding protein (DNMBP) gene SNPs and
            Alzheimer's disease
  JOURNAL   Neurobiol Aging 29 (10), 1602-1604 (2008)
   PUBMED   17442457
  REMARK    GeneRIF: We observed no association of statistical significance in
            either the total sample or the APOE*4 non-carriers for any of the
            SNPs of Dynamin Binding Protein.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 823)
  AUTHORS   Otani,T., Ichii,T., Aono,S. and Takeichi,M.
  TITLE     Cdc42 GEF Tuba regulates the junctional configuration of simple
            epithelial cells
  JOURNAL   J Cell Biol 175 (1), 135-146 (2006)
   PUBMED   17015620
  REMARK    GeneRIF: Tuba controls the shaping of cell junctions through the
            local activation of Cdc42 and its effectors.
REFERENCE   8  (residues 1 to 823)
  AUTHORS   Kuwano,R., Miyashita,A., Arai,H., Asada,T., Imagawa,M., Shoji,M.,
            Higuchi,S., Urakami,K., Kakita,A., Takahashi,H., Tsukie,T.,
            Toyabe,S., Akazawa,K., Kanazawa,I. and Ihara,Y.
  CONSRTM   Japanese Genetic Study Consortium for Alzeheimer's Disease
  TITLE     Dynamin-binding protein gene on chromosome 10q is associated with
            late-onset Alzheimer's disease
  JOURNAL   Hum Mol Genet 15 (13), 2170-2182 (2006)
   PUBMED   16740596
  REMARK    GeneRIF: Results confirmed DNMBP may be one of the susceptibility
            genes for Alzheimer's disease.
            GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   9  (residues 1 to 823)
  AUTHORS   Cestra,G., Kwiatkowski,A., Salazar,M., Gertler,F. and De Camilli,P.
  TITLE     Tuba, a GEF for CDC42, links dynamin to actin regulatory proteins
  JOURNAL   Methods Enzymol 404, 537-545 (2005)
   PUBMED   16413298
REFERENCE   10 (residues 1 to 823)
  AUTHORS   Salazar,M.A., Kwiatkowski,A.V., Pellegrini,L., Cestra,G.,
            Butler,M.H., Rossman,K.L., Serna,D.M., Sondek,J., Gertler,F.B. and
            De Camilli,P.
  TITLE     Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl
            homology domains, links dynamin to regulation of the actin
            cytoskeleton
  JOURNAL   J Biol Chem 278 (49), 49031-49043 (2003)
   PUBMED   14506234
  REMARK    GeneRIF: functions to bring together dynamin with actin regulatory
            proteins
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL627434.4 and AL392107.17.
            
            On Jun 7, 2025 this sequence version replaced NP_001305256.1.
            
            Summary: This gene encodes a protein belonging to the guanine
            nucleotide exchange factor family, and which regulates the
            configuration of cell junctions. It contains multiple binding sites
            for dynamin and thus links dynamin to actin regulatory proteins.
            Polymorphisms in this gene have been linked to Alzheimer's disease
            in some populations, though there are conflicting reports of such
            linkages in other populations. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC041628.1, SRR11853561.3980.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.2"
     Protein         1..823
                     /product="dynamin-binding protein isoform c"
                     /note="scaffold protein TUBA"
                     /calculated_mol_wt=93367
     Region          31..211
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(37,41,130,162..163,166..167,169..170,173..174,
                     177..178,181,207,211)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          263..454
                     /region_name="BAR_DNMBP"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin
                     Binding Protein; cd07589"
                     /db_xref="CDD:153273"
     Site            order(275,278..279,283,285..286,289..290,292..293,
                     307..308,310..311,314..315,317..318,321,327,330..331,415,
                     418..419,421,426,429..430,432..433,436..437,440..441,
                     443..444,447..448,450..451)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153273"
     Region          535..591
                     /region_name="SH3_DNMBP_C1"
                     /note="First C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11798"
                     /db_xref="CDD:212732"
     Site            order(540,542,545,549,571..572,585,587..588)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212732"
     Region          763..819
                     /region_name="SH3_DNMBP_C2"
                     /note="Second C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba, and similar domains;
                     cd12141"
                     /db_xref="CDD:213017"
     Site            order(768,770,773,777,799..800,813,815..816)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213017"
     CDS             1..823
                     /gene="DNMBP"
                     /gene_synonym="ARHGEF36; CTRCT48; TUBA"
                     /coded_by="NM_001318327.2:87..2558"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS81494.1"
                     /db_xref="GeneID:23268"
                     /db_xref="HGNC:HGNC:30373"
                     /db_xref="MIM:611282"
ORIGIN      
        1 mtllssqsss lvapsgsvsa enpeqrmlek rakvieellq terdyirdle mcierimvpm
       61 qqaqvpnidf eglfgnmqmv ikvskqllaa leisdavgpv flghrdeleg tykiycqnhd
      121 eaialleiye kdekiqkhlq dsladlksly newgctnyin lgsflikpvq rvmryplllm
      181 ellnstpesh pdkvpltnav lavkeinvni neykrrkdlv lkyrkgdeds lmekisklni
      241 hsiikksnrv sshlkhltgf apqikdevfe eteknfrmqe rliksfirdl slylqhires
      301 acvkvvaavs mwdvcmergh rdleqfervh ryisdqlftn fkerterlvi splnqllsmf
      361 tgphklvqkr fdklldfync teraeklkdk ktleelqsar nnyealnaql ldelpkfhqy
      421 aqglftncvh gyaeahcdfv hqaleqlkpl lsllkvagre gnliaifhee hsrvlqqlqv
      481 ftffpeslpa tkkpferkti drqsarkpll glpsymlqse elrasllary ppeklfqaer
      541 nfnaaqdldv sllegdlvgv ikkkdpmgsq nrwlidngvt kgfvyssflk pynprrshsd
      601 asvgshsste sehgsssprf prqnsgstlt fnpssmavsf tsgscqkqpq daspppkecd
      661 qgtlsaslnp snsesspsrc psdpdstsqp rsgdsadvar dvkqptatpr syrnfrhpei
      721 vgysvpgrng qsqdlvkgca rtaqapedrs tepdgseaeg nqvyfavytf karnpnelsv
      781 sanqklkile fkdvtgntew wlaevngkkg yvpsnyirkt eyt
//
LOCUS       NP_001427445             555 aa            linear   PRI 21-NOV-2025
DEFINITION  radixin isoform 9 [Homo sapiens].
ACCESSION   NP_001427445
VERSION     NP_001427445.1
DBSOURCE    REFSEQ: accession NM_001440516.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 555)
  AUTHORS   Kruse,T., Benz,C., Garvanska,D.H., Lindqvist,R., Mihalic,F.,
            Coscia,F., Inturi,R., Sayadi,A., Simonetti,L., Nilsson,E., Ali,M.,
            Kliche,J., Moliner Morro,A., Mund,A., Andersson,E., McInerney,G.,
            Mann,M., Jemth,P., Davey,N.E., Overby,A.K., Nilsson,J. and
            Ivarsson,Y.
  TITLE     Large scale discovery of coronavirus-host factor protein
            interaction motifs reveals SARS-CoV-2 specific mechanisms and
            vulnerabilities
  JOURNAL   Nat Commun 12 (1), 6761 (2021)
   PUBMED   34799561
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 555)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 555)
  AUTHORS   Stemmer-Rachamimov,A.O., Gonzalez-Agosti,C., Xu,L., Burwick,J.A.,
            Beauchamp,R., Pinney,D., Louis,D.N. and Ramesh,V.
  TITLE     Expression of NF2-encoded merlin and related ERM family proteins in
            the human central nervous system
  JOURNAL   J Neuropathol Exp Neurol 56 (6), 735-742 (1997)
   PUBMED   9184664
REFERENCE   7  (residues 1 to 555)
  AUTHORS   Hirao,M., Sato,N., Kondo,T., Yonemura,S., Monden,M., Sasaki,T.,
            Takai,Y., Tsukita,S. and Tsukita,S.
  TITLE     Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma
            membrane association: possible involvement of phosphatidylinositol
            turnover and Rho-dependent signaling pathway
  JOURNAL   J Cell Biol 135 (1), 37-51 (1996)
   PUBMED   8858161
REFERENCE   8  (residues 1 to 555)
  AUTHORS   Wilgenbus,K.K., Milatovich,A., Francke,U. and Furthmayr,H.
  TITLE     Molecular cloning, cDNA sequence, and chromosomal assignment of the
            human radixin gene and two dispersed pseudogenes
  JOURNAL   Genomics 16 (1), 199-206 (1993)
   PUBMED   8486357
REFERENCE   9  (residues 1 to 555)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 555)
  AUTHORS   Sato,N., Funayama,N., Nagafuchi,A., Yonemura,S., Tsukita,S. and
            Tsukita,S.
  TITLE     A gene family consisting of ezrin, radixin and moesin. Its specific
            localization at actin filament/plasma membrane association sites
  JOURNAL   J Cell Sci 103 (Pt 1), 131-143 (1992)
   PUBMED   1429901
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002788.3 and AP000901.5.
            
            Summary: Radixin is a cytoskeletal protein that may be important in
            linking actin to the plasma membrane. It is highly similar in
            sequence to both ezrin and moesin. The radixin gene has been
            localized by fluorescence in situ hybridization to 11q23. A
            truncated version representing a pseudogene (RDXP2) was assigned to
            Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was
            mapped to 11p by Southern and PCR analyses. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA2144333, SAMEA2467144
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..555
                     /product="radixin isoform 9"
                     /calculated_mol_wt=65270
     Region          5..178
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          172..268
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(214..215,217..223,232,253,256..257,260)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(214,217..224,232,253,256..257,260)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(250,254)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            253..268
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          319..428
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          479..555
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..555
                     /gene="RDX"
                     /gene_synonym="DFNB24"
                     /coded_by="NM_001440516.1:213..1880"
                     /note="isoform 9 is encoded by transcript variant 18"
                     /db_xref="GeneID:5962"
                     /db_xref="HGNC:HGNC:9944"
                     /db_xref="MIM:179410"
ORIGIN      
        1 mpkpvvktvg lrevwffglq yvdskgystw lklnkkvtqq dvkkenplqf kfrakffped
       61 vseeliqeit qrlfflqvke ailndeiycp petavllasy avqakygdyn keihkpgyla
      121 ndrllpqrvl eqhkltkeqw eeriqnwhee hrgmlredsm meylkiaqdl emygvnyfei
      181 knkkgtelwl gvdalglniy ehddkltpki gfpwseirni sfndkkfvik pidkkapdfv
      241 fyaprlrink rilalcmgnh elymrrrkpd tievqqmkaq areekhqkql eraqlenekk
      301 kreiaekeke rierekeelm erlkqieeqt ikaqkeleeq trkaleldqe rkrakeeaer
      361 lekerraaee aksaiakqaa dqmknqeqla aelaeftaki alleeakkkk eeeatewqhk
      421 afaaqedlek tkeelktvms appppppppv ipptenehde hdennaeasa elsnegvmnh
      481 rseeervtet qknervkkql qalsselaqa rdetkktqnd vlhaenvkag rdkyktlrqi
      541 rqgntkqrid efeam
//
LOCUS       NP_001397751            1433 aa            linear   PRI 21-NOV-2025
DEFINITION  phospholipid-transporting ATPase VB isoform 6 [Homo sapiens].
ACCESSION   NP_001397751 XP_011532774
VERSION     NP_001397751.1
DBSOURCE    REFSEQ: accession NM_001410822.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1433)
  AUTHORS   Sanchiz-Calvo,M., Coccia,E., Cawthorne,C., Morrone Parfitt,G.,
            Torre-Muruzabal,T., Tsafaras,G., Van Laere,K., Cabezudo,D.,
            Cascalho,A., Van den Haute,C., Vangheluwe,P., Blanchard,J.,
            Bentea,E. and Baekelandt,V.
  TITLE     Loss of the lysosomal lipid flippase ATP10B leads to progressive
            dopaminergic neurodegeneration and parkinsonian motor deficits
  JOURNAL   Acta Neuropathol 150 (1), 5 (2025)
   PUBMED   40676227
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1433)
  AUTHORS   Diaz-Belloso,R., Munoz-Delgado,L., Martin-Bornez,M., Ojeda,E.,
            Perinan,M.T., Garcia-Diaz,S., Bonilla-Toribio,M., Buiza-Rueda,D.,
            Pineda-Sanchez,R., Jesus,S., Macias-Garcia,D., Adarmes-Gomez,A.,
            Carrillo,F., Mir,P. and Gomez-Garre,P.
  TITLE     Role of ATP10B in Parkinson disease in a cohort from southern Spain
  JOURNAL   Parkinsonism Relat Disord 124, 106989 (2024)
   PUBMED   38754220
  REMARK    GeneRIF: Role of ATP10B in Parkinson disease in a cohort from
            southern Spain.
REFERENCE   3  (residues 1 to 1433)
  AUTHORS   Wouters,R., Beletchi,I., Van den Haute,C., Baekelandt,V.,
            Martin,S., Eggermont,J. and Vangheluwe,P.
  TITLE     The lipid flippase ATP10B enables cellular lipid uptake under
            stress conditions
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (2), 119652 (2024)
   PUBMED   38086447
  REMARK    GeneRIF: The lipid flippase ATP10B enables cellular lipid uptake
            under stress conditions.
            Review article
REFERENCE   4  (residues 1 to 1433)
  AUTHORS   Ishiguro,M., Yoshino,H., Li,Y., Ikeda,A., Funayama,M., Nishioka,K.
            and Hattori,N.
  TITLE     Genetic analysis of ATP10B for Parkinson's disease in Japan
  JOURNAL   Parkinsonism Relat Disord 88, 10-12 (2021)
   PUBMED   34091411
  REMARK    GeneRIF: Genetic analysis of ATP10B for Parkinson's disease in
            Japan.
REFERENCE   5  (residues 1 to 1433)
  AUTHORS   Martin,S., Smolders,S., Van den Haute,C., Heeman,B., van Veen,S.,
            Crosiers,D., Beletchi,I., Verstraeten,A., Gossye,H., Gelders,G.,
            Pals,P., Hamouda,N.N., Engelborghs,S., Martin,J.J., Eggermont,J.,
            De Deyn,P.P., Cras,P., Baekelandt,V., Vangheluwe,P. and Van
            Broeckhoven,C.
  CONSRTM   BELNEU consortium
  TITLE     Mutated ATP10B increases Parkinson's disease risk by compromising
            lysosomal glucosylceramide export
  JOURNAL   Acta Neuropathol 139 (6), 1001-1024 (2020)
   PUBMED   32172343
  REMARK    GeneRIF: Mutated ATP10B increases Parkinson's disease risk by
            compromising lysosomal glucosylceramide export.
REFERENCE   6  (residues 1 to 1433)
  AUTHORS   Segawa,K., Kurata,S. and Nagata,S.
  TITLE     Human Type IV P-type ATPases That Work as Plasma Membrane
            Phospholipid Flippases and Their Regulation by Caspase and Calcium
  JOURNAL   J Biol Chem 291 (2), 762-772 (2016)
   PUBMED   26567335
REFERENCE   7  (residues 1 to 1433)
  AUTHORS   Naito,T., Takatsu,H., Miyano,R., Takada,N., Nakayama,K. and
            Shin,H.W.
  TITLE     Phospholipid Flippase ATP10A Translocates Phosphatidylcholine and
            Is Involved in Plasma Membrane Dynamics
  JOURNAL   J Biol Chem 290 (24), 15004-15017 (2015)
   PUBMED   25947375
REFERENCE   8  (residues 1 to 1433)
  AUTHORS   Takatsu,H., Baba,K., Shima,T., Umino,H., Kato,U., Umeda,M.,
            Nakayama,K. and Shin,H.W.
  TITLE     ATP9B, a P4-ATPase (a putative aminophospholipid translocase),
            localizes to the trans-Golgi network in a CDC50 protein-independent
            manner
  JOURNAL   J Biol Chem 286 (44), 38159-38167 (2011)
   PUBMED   21914794
  REMARK    Erratum:[J Biol Chem. 2015 Jan 9;290(2):886]
REFERENCE   9  (residues 1 to 1433)
  AUTHORS   Schmutz,J., Martin,J., Terry,A., Couronne,O., Grimwood,J.,
            Lowry,S., Gordon,L.A., Scott,D., Xie,G., Huang,W., Hellsten,U.,
            Tran-Gyamfi,M., She,X., Prabhakar,S., Aerts,A., Altherr,M.,
            Bajorek,E., Black,S., Branscomb,E., Caoile,C., Challacombe,J.F.,
            Chan,Y.M., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Grigoriev,I., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Israni,S.,
            Jett,J., Kadner,K., Kimball,H., Kobayashi,A., Lopez,F., Lou,Y.,
            Martinez,D., Medina,C., Morgan,J., Nandkeshwar,R., Noonan,J.P.,
            Pitluck,S., Pollard,M., Predki,P., Priest,J., Ramirez,L.,
            Retterer,J., Rodriguez,A., Rogers,S., Salamov,A., Salazar,A.,
            Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N., Wheeler,J.,
            Wu,K., Yang,J., Dickson,M., Cheng,J.F., Eichler,E.E., Olsen,A.,
            Pennacchio,L.A., Rokhsar,D.S., Richardson,P., Lucas,S.M.,
            Myers,R.M. and Rubin,E.M.
  TITLE     The DNA sequence and comparative analysis of human chromosome 5
  JOURNAL   Nature 431 (7006), 268-274 (2004)
   PUBMED   15372022
REFERENCE   10 (residues 1 to 1433)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011363.6, AC008456.6 and AC008388.7.
            
            On Aug 16, 2022 this sequence version replaced XP_011532774.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853562.26661.1,
                                           SRR11853565.24095.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1433
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..1433
                     /product="phospholipid-transporting ATPase VB isoform 6"
                     /EC_number="7.6.2.1"
                     /note="probable phospholipid-transporting ATPase VB;
                     P4-ATPase flippase complex alpha subunit ATP10B; ATPase,
                     class V, type 10B"
                     /calculated_mol_wt=161482
     Region          40..1185
                     /region_name="P-type_ATPase_APLT_Dnf-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2,
                     -10D, -11B, -11C; cd02073"
                     /db_xref="CDD:319770"
     Site            order(405..407,738,762..764,840,887..889,1001,1004,1007,
                     1027,1030)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     CDS             1..1433
                     /gene="ATP10B"
                     /gene_synonym="ATPVB"
                     /coded_by="NM_001410822.1:172..4473"
                     /note="isoform 6 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS93811.1"
                     /db_xref="GeneID:23120"
                     /db_xref="HGNC:HGNC:13543"
                     /db_xref="MIM:619791"
ORIGIN      
        1 mkkegrkrwk rkedkkrvvv snllfegwsh kenpnrhhrg nqiktskytv lsfvpknife
       61 qlhrfanlyf vgiavlnfip vvnafqpevs mipicvilav taikdawedl rryksdkvin
      121 nrecliysrk eqtyvqkcwk dvrvgdfiqm kcneivpadi lllfssdpng ichletasld
      181 getnlkqrcv vkgfsqqevq fepelfhnti vcekpnnhln kfkgymehpd qtrtgfgces
      241 lllrgctirn temavgiviy aghetkamln nsgprykrsk ierrmnidif fcigililmc
      301 ligavghsiw ngtfeehppf dvpdangsfl psalggfymf ltmiillqvl ipislyvsie
      361 lvklgqvffl sndldlydee tdlsiqcral niaedlgqiq yifsdktgtl tenkmvfrrc
      421 timgseyshq enakrletpk eldsdgeewt qyqclsfsar waqdpatmrs qkgaqplrrs
      481 qsarvpiqgh yrqrsmghre ssqppvafss siekdvtpdk nlltkvrdaa lwletlsdsr
      541 pakaslstts siadfflalt icnsvmvstt teprqrvtik psskalgtsl ekiqqlfqkl
      601 kllslsqsfs stapsdtdlg eslganvatt dsderddasv csggdstddg gyrssmwdqg
      661 dilesgsgts leealeapat dlarpefcye aespdeaalv haahaysftl vsrtpeqvtv
      721 rlpqgtcltf sllctlgfds vrkrmsvvvr hpltgeivvy tkgadsvimd lledpacvpd
      781 inmekklrki rartqkhldl yardglrtlc iakkvvseed frrwasfrre aeasldnrde
      841 llmetaqhle nqltllgatg iedrlqegvp dtiatlreag iqlwvltgdk qetavniahs
      901 crllnqtdtv ytintenqet cesilncale elkqfrelqk pdrklfgfrl psktpsitse
      961 avvpeaglvi dgktlnaifq gklekkflel tqycrsvlcc rstplqksmi vklvrdklrv
     1021 mtlsigdgan dvsmiqaadi gigisgqegm qavmssdfai trfkhlkkll lvhghwcysr
     1081 larmvvyyly knvcyvnllf wyqffcgfss stmidywqmi ffnlfftslp plvfgvldkd
     1141 isaetllalp elyksgqnse cynlstfwis mvdafyqsli cffipylayk gsdidvftfg
     1201 tpintisltt illhqamemk twtifhgvvl lgsflmyflv sllynatcvi cnsptnpywv
     1261 megqlsnptf ylvcfltpvv allpryffls lqgtcgksli skaqkidklp pdkrnleiqs
     1321 wrsrqrpapv pevarpthhp vssitgqdfs astpkssnpp krkhveesvl heqrcgtecm
     1381 rddscsgdss aqlssgehll gpnrimaysr gqtdmcrcsk rsshrrsqss lti
//
LOCUS       NP_001424242             874 aa            linear   PRI 21-NOV-2025
DEFINITION  ephrin type-A receptor 5 isoform g [Homo sapiens].
ACCESSION   NP_001424242 XP_005265710 XP_054205163
VERSION     NP_001424242.1
DBSOURCE    REFSEQ: accession NM_001437313.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 874)
  AUTHORS   Han,X., Liu,T., Zhai,J., Liu,C., Wang,W., Nie,C., Wang,Q., Zhu,X.,
            Zhou,H. and Tian,W.
  TITLE     Association between EPHA5 methylation status in peripheral blood
            leukocytes and the risk and prognosis of gastric cancer
  JOURNAL   PeerJ 10, e13774 (2022)
   PUBMED   36164608
  REMARK    GeneRIF: Association between EPHA5 methylation status in peripheral
            blood leukocytes and the risk and prognosis of gastric cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 874)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   3  (residues 1 to 874)
  AUTHORS   Liu,C., He,Y., Feng,X., Li,J. and Wang,J.
  TITLE     Expression of EPHA5 in lung adenocarcinoma is associated with lymph
            node metastasis and EGFR mutation
  JOURNAL   APMIS 130 (6), 338-345 (2022)
   PUBMED   35332588
  REMARK    GeneRIF: Expression of EPHA5 in lung adenocarcinoma is associated
            with lymph node metastasis and EGFR mutation.
REFERENCE   4  (residues 1 to 874)
  AUTHORS   Abouhashem,N., Harb,O., Elwan,A., Zaitoun,M. and Saraya,Y.
  TITLE     Immunohistochemical evaluation of forkhead box A1 and EphA5 markers
            in serous ovarian carcinomas, and their impact on the clinical
            outcome of patients
  JOURNAL   Pol J Pathol 73 (2), 120-133 (2022)
   PUBMED   36345952
  REMARK    GeneRIF: Immunohistochemical evaluation of forkhead box A1 and
            EphA5 markers in serous ovarian carcinomas, and their impact on the
            clinical outcome of patients.
REFERENCE   5  (residues 1 to 874)
  AUTHORS   Zhou,R.
  TITLE     Regulation of topographic projection by the Eph family receptor Bsk
            (EphA5) and its ligands
  JOURNAL   Cell Tissue Res 290 (2), 251-259 (1997)
   PUBMED   9321686
  REMARK    Review article
REFERENCE   6  (residues 1 to 874)
  AUTHORS   Miescher,G.C., Taylor,V., Olivieri,G., Mindermann,T., Schrock,E.
            and Steck,A.J.
  TITLE     Extensive splice variation and localization of the EHK-1 receptor
            tyrosine kinase in adult human brain and glial tumors
  JOURNAL   Brain Res Mol Brain Res 46 (1-2), 17-24 (1997)
   PUBMED   9191074
REFERENCE   7  (residues 1 to 874)
  AUTHORS   Gale,N.W., Holland,S.J., Valenzuela,D.M., Flenniken,A., Pan,L.,
            Ryan,T.E., Henkemeyer,M., Strebhardt,K., Hirai,H., Wilkinson,D.G.,
            Pawson,T., Davis,S. and Yancopoulos,G.D.
  TITLE     Eph receptors and ligands comprise two major specificity subclasses
            and are reciprocally compartmentalized during embryogenesis
  JOURNAL   Neuron 17 (1), 9-19 (1996)
   PUBMED   8755474
REFERENCE   8  (residues 1 to 874)
  AUTHORS   Winslow,J.W., Moran,P., Valverde,J., Shih,A., Yuan,J.Q., Wong,S.C.,
            Tsai,S.P., Goddard,A., Henzel,W.J., Hefti,F. et al.
  TITLE     Cloning of AL-1, a ligand for an Eph-related tyrosine kinase
            receptor involved in axon bundle formation
  JOURNAL   Neuron 14 (5), 973-981 (1995)
   PUBMED   7748564
REFERENCE   9  (residues 1 to 874)
  AUTHORS   Fox,G.M., Holst,P.L., Chute,H.T., Lindberg,R.A., Janssen,A.M.,
            Basu,R. and Welcher,A.A.
  TITLE     cDNA cloning and tissue distribution of five human EPH-like
            receptor protein-tyrosine kinases
  JOURNAL   Oncogene 10 (5), 897-905 (1995)
   PUBMED   7898931
REFERENCE   10 (residues 1 to 874)
  AUTHORS   Spritz,R.A., Strunk,K.M., Lee,S.T., Lu-Kuo,J.M., Ward,D.C., Le
            Paslier,D., Altherr,M.R., Dorman,T.E. and Moir,D.T.
  TITLE     A YAC contig spanning a cluster of human type III receptor protein
            tyrosine kinase genes (PDGFRA-KIT-KDR) in chromosome segment 4q12
  JOURNAL   Genomics 22 (2), 431-436 (1994)
   PUBMED   7528718
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104137.5, AC105923.6 and
            AC018683.4.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_005265710.1, XP_054205163.1.
            
            Summary: This gene belongs to the ephrin receptor subfamily of the
            protein-tyrosine kinase family. EPH and EPH-related receptors have
            been implicated in mediating developmental events, particularly in
            the nervous system. Receptors in the EPH subfamily typically have a
            single kinase domain and an extracellular region containing a
            Cys-rich domain and 2 fibronectin type III repeats. The ephrin
            receptors are divided into 2 groups based on the similarity of
            their extracellular domain sequences and their affinities for
            binding ephrin-A and ephrin-B ligands. Alternatively spliced
            transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1966682, SAMEA1968540
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..874
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q13.1-q13.2"
     Protein         1..874
                     /product="ephrin type-A receptor 5 isoform g"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-A receptor 5; receptor protein-tyrosine
                     kinase HEK7; tyrosine-protein kinase receptor EHK-1;
                     EPH-like kinase 7; EPH homology kinase 1; brain-specific
                     kinase; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=96751
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54756.3)"
     Region          60..232
                     /region_name="EphR_LBD_A5"
                     /note="Ligand Binding Domain of Ephrin type-A Receptor 5;
                     cd10483"
                     /db_xref="CDD:198451"
     Site            order(84,86..90,97..98,100,102,133,135,140..141,183,
                     187..188,191..193,220..222,224)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198451"
     Site            264
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54756.3)"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54756.3)"
     Region          305..395
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(305,368,383)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(384..385,387..388)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          412..509
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Region          507..773
                     /region_name="PTKc_EphR_A"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphA Ephrin Receptors; cd05066"
                     /db_xref="CDD:270651"
     Site            order(518,520..522,526,542,544,590..591,593,637,641..642,
                     644,655,674..678,687,721)
                     /site_type="active"
                     /db_xref="CDD:270651"
     Site            order(518..522,526,542,544,590..593,596..597,641..642,644,
                     655)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270651"
     Site            order(637,641,674..678,687,721)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270651"
     Site            654..680
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270651"
     Region          802..867
                     /region_name="SAM_EPH-A5"
                     /note="SAM domain of EPH-A5 subfamily of tyrosine kinase
                     receptors; cd09546"
                     /db_xref="CDD:188945"
     Site            order(819,852)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188945"
     CDS             1..874
                     /gene="EPHA5"
                     /gene_synonym="CEK7; EHK-1; EHK1; EK7; HEK7; TYRO4"
                     /coded_by="NM_001437313.1:748..3372"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="GeneID:2044"
                     /db_xref="HGNC:HGNC:3389"
                     /db_xref="MIM:600004"
ORIGIN      
        1 mrgsgprgag rrrppsgggd tpitpaslag cysaprrapl wtclllcaal rtllaspsne
       61 vnlldsrtvm gdlgwiafpk ngweeigevd enyapihtyq vckvmeqnqn nwlltswisn
      121 egasrifiel kftlrdcnsl pgglgtcket fnmyyfesdd qngrnikenq yikidtiaad
      181 esfteldlgd rvmklntevr dvgplskkgf ylafqdvgac ialvsvrvyy kkcpsvvrhl
      241 avfpdtitga dssqllevsg scvnhsvtde ppkmhcsaeg ewlvpigkcm ckagyeekng
      301 tcqapspvtn vkkgkiakns islswqepdr pngiileyei kyfekdqets ytiikskett
      361 itaeglkpas vyvfqirart aagygvfsrr fefettpvsv aassdqsqip viavsvtvgv
      421 illavvigvl lsgsccecgc grasslcava hpsliwrcgy skakqdpeee kmhfhnghik
      481 lpgvrtyidp htyedpnqav hefakeieas citierviga gefgevcsgr lklpgkrelp
      541 vaiktlkvgy tekqrrdflg easimgqfdh pniihlegvv tkskpvmivt eymengsldt
      601 flkkndgqft viqlvgmlrg isagmkylsd mgyvhrdlaa rnilinsnlv ckvsdfglsr
      661 vleddpeaay ttrggkipir wtapeaiafr kftsasdvws ygivmwevvs ygerpywemt
      721 nqdvikavee gyrlpspmdc paalyqlmld cwqkernsrp kfdeivnmld klirnpsslk
      781 tlvnascrvs nllaehsplg sgayrsvgew leaikmgryt eifmengyss mdavaqvtle
      841 dlrrlgvtlv ghqkkimnsl qemkvqlvng mvpl
//
LOCUS       NP_001428007            1231 aa            linear   PRI 21-NOV-2025
DEFINITION  cohesin subunit SA-2 isoform b [Homo sapiens].
ACCESSION   NP_001428007 XP_047297740 XP_054182365
VERSION     NP_001428007.1
DBSOURCE    REFSEQ: accession NM_001441078.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1231)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1231)
  AUTHORS   Fischer,A., Hernandez-Rodriguez,B., Mulet-Lazaro,R., Nuetzel,M.,
            Holzl,F., van Herk,S., Kavelaars,F.G., Stanewsky,H., Ackermann,U.,
            Niang,A.H., Diaz,N., Reuschel,E., Strieder,N., Hernandez-Lopez,I.,
            Valk,P.J.M., Vaquerizas,J.M., Rehli,M., Delwel,R. and Gebhard,C.
  TITLE     STAG2 mutations reshape the cohesin-structured spatial chromatin
            architecture to drive gene regulation in acute myeloid leukemia
  JOURNAL   Cell Rep 43 (8), 114498 (2024)
   PUBMED   39084219
  REMARK    GeneRIF: STAG2 mutations reshape the cohesin-structured spatial
            chromatin architecture to drive gene regulation in acute myeloid
            leukemia.
REFERENCE   3  (residues 1 to 1231)
  AUTHORS   Huber,J., Tanasie,N.L., Zernia,S. and Stigler,J.
  TITLE     Single-molecule imaging reveals a direct role of CTCF's zinc
            fingers in SA interaction and cluster-dependent RNA recruitment
  JOURNAL   Nucleic Acids Res 52 (11), 6490-6506 (2024)
   PUBMED   38742641
  REMARK    GeneRIF: Single-molecule imaging reveals a direct role of CTCF's
            zinc fingers in SA interaction and cluster-dependent RNA
            recruitment.
REFERENCE   4  (residues 1 to 1231)
  AUTHORS   Xu,W., Kim,J.S., Yang,T., Ya,A., Sadzewicz,L., Tallon,L.,
            Harris,B.T., Sarkaria,J., Jin,F. and Waldman,T.
  TITLE     STAG2 mutations regulate 3D genome organization, chromatin loops,
            and Polycomb signaling in glioblastoma multiforme
  JOURNAL   J Biol Chem 300 (6), 107341 (2024)
   PUBMED   38705393
  REMARK    GeneRIF: STAG2 mutations regulate 3D genome organization, chromatin
            loops, and Polycomb signaling in glioblastoma multiforme.
REFERENCE   5  (residues 1 to 1231)
  AUTHORS   Ros-Pardo,D., Gomez-Puertas,P. and Marcos-Alcalde,I.
  TITLE     STAG2: Computational Analysis of Missense Variants Involved in
            Disease
  JOURNAL   Int J Mol Sci 25 (2), 1280 (2024)
   PUBMED   38279279
  REMARK    GeneRIF: STAG2: Computational Analysis of Missense Variants
            Involved in Disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1231)
  AUTHORS   Gregson,H.C., Schmiesing,J.A., Kim,J.S., Kobayashi,T., Zhou,S. and
            Yokomori,K.
  TITLE     A potential role for human cohesin in mitotic spindle aster
            assembly
  JOURNAL   J Biol Chem 276 (50), 47575-47582 (2001)
   PUBMED   11590136
REFERENCE   7  (residues 1 to 1231)
  AUTHORS   Sumara,I., Vorlaufer,E., Gieffers,C., Peters,B.H. and Peters,J.M.
  TITLE     Characterization of vertebrate cohesin complexes and their
            regulation in prophase
  JOURNAL   J Cell Biol 151 (4), 749-762 (2000)
   PUBMED   11076961
REFERENCE   8  (residues 1 to 1231)
  AUTHORS   Carramolino,L., Lee,B.C., Zaballos,A., Peled,A., Barthelemy,I.,
            Shav-Tal,Y., Prieto,I., Carmi,P., Gothelf,Y., Gonzalez de
            Buitrago,G., Aracil,M., Marquez,G., Barbero,J.L. and Zipori,D.
  TITLE     SA-1, a nuclear protein encoded by one member of a novel gene
            family: molecular cloning and detection in hemopoietic organs
  JOURNAL   Gene 195 (2), 151-159 (1997)
   PUBMED   9305759
  REMARK    Erratum:[Gene 1998 Jan 12;206(2):283]
REFERENCE   9  (residues 1 to 1231)
  AUTHORS   Wu,C., Friedlander,P., Lamoureux,C., Zannis-Hadjopoulos,M. and
            Price,G.B.
  TITLE     cDNA clones contain autonomous replication activity
  JOURNAL   Biochim Biophys Acta 1174 (3), 241-257 (1993)
   PUBMED   7690594
REFERENCE   10 (residues 1 to 1231)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121601.13 and AL355476.12.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297740.1, XP_054182365.1.
            
            Summary: The protein encoded by this gene is a subunit of the
            cohesin complex, which regulates the separation of sister
            chromatids during cell division. Targeted inactivation of this gene
            results in chromatid cohesion defects and aneuploidy, suggesting
            that genetic disruption of cohesin is a cause of aneuploidy in
            human cancer. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2891864.1,
                                           SRR14038197.1639630.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1231
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..1231
                     /product="cohesin subunit SA-2 isoform b"
                     /note="SCC3 homolog 2; cohesin subunit SA-2; SA2
                     stromalin; sister chromatid cohesion 3 homolog B; stromal
                     antigen 2"
                     /calculated_mol_wt=141196
     Region          1..75
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Region          102..>395
                     /region_name="IRR1"
                     /note="Cohesin [Cell division and chromosome
                     partitioning]; COG5537"
                     /db_xref="CDD:227824"
     Region          157..270
                     /region_name="STAG"
                     /note="STAG domain; pfam08514"
                     /db_xref="CDD:462502"
     Site            607
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1058
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1061
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Region          1064..1083
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1064
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35638; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1065
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35638; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1112
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     CDS             1..1231
                     /gene="STAG2"
                     /gene_synonym="bA517O1.1; HPE13; MKMS; NEDXCF; SA-2; SA2;
                     SCC3B"
                     /coded_by="NM_001441078.1:242..3937"
                     /note="isoform b is encoded by transcript variant 18"
                     /db_xref="GeneID:10735"
                     /db_xref="HGNC:HGNC:11355"
                     /db_xref="MIM:300826"
ORIGIN      
        1 miaapeiptd fnllqeseth fssdtdfedi egknqkqgkg ktckkgkkgp aekgkggngg
       61 gkppsgpnrm nghhqqngve nmmlfevvkm gksamqsvvd dwiesykhdr dialldlinf
      121 fiqcsgckgv vtaemfrhmq nseiirkmte efdedsgdyp ltmagpqwkk fkssfcefig
      181 vlvrqcqysi iydeymmdtv islltglsds qvrafrhtst laamklmtal vnvalnlsin
      241 mdntqrqyea ernkmigkra nerlelllqk rkelqenqde ienmmnaifk gvfvhryrda
      301 iaeiraicie eigiwmkmys daflndsylk yvgwtmhdkq gevrlkclta lqglyynkel
      361 nsklelftsr fkdrivsmtl dkeydvavqa iklltlvlqs seevltaedc envyhlvysa
      421 hrpvavaage flykklfsrr dpeedgmmkr rgrqgpnanl vktlvfffle selhehaayl
      481 vdsmwdcate llkdwecmns llleeplsge ealtdrqesa lieimlctir qaaechppvg
      541 rgtgkrvlta kekktqlddr tkitelfava lpqllakysv daekvtnllq lpqyfdleiy
      601 ttgrlekhld allrqirniv ekhtdtdvle acsktyhalc neeftifnrv disrsqlide
      661 ladkfnrlle dflqegeepd eddayqvlst lkritafhna hdlskwdlfa cnykllktgi
      721 engdmpeqiv ihalqcthyv ilwqlakite ssstkedllr lkkqmrvfcq icqhyltnvn
      781 ttvkeqafti lcdilmifsh qimsggrdml eplvytpdss lqsellsfil dhvfieqddd
      841 nnsadgqqed easkiealhk rrnllaafck livytvvemn taadifkqym kyyndygdii
      901 ketmsktrqi dkiqcaktli lslqqlfnem iqengynfdr ssstfsgike larrfaltfg
      961 ldqlktreai amlhkdgief afkepnpqge shpplnlafl dilsefsskl lrqdkrtvyv
     1021 ylekfmtfqm slrredvwlp lmsyrnslla ggdddtmsvi sgissrgstv rskkskpstg
     1081 krkvvegmql slteessssd smwlsreqtl htpvmmqtpq ltstimrepk rlrpedsfms
     1141 vypmqtehhq tpldynrrgt slmeddeepi vedvmmsseg riedlnegmd fdtmdidlpp
     1201 sknrrertel kpdffdpasi mdesvlgvsm f
//
LOCUS       NP_001153148             561 aa            linear   PRI 21-NOV-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein Q isoform 5 [Homo sapiens].
ACCESSION   NP_001153148 XP_005248692 XP_054210016
VERSION     NP_001153148.1
DBSOURCE    REFSEQ: accession NM_001159676.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Ishtayeh,H., Galves,M., Barnatan,T.T., Berdichevsky,Y.,
            Amer-Sarsour,F., Pasmanik-Chor,M., Braverman,I., Blumen,S.C. and
            Ashkenazi,A.
  TITLE     Oculopharyngeal muscular dystrophy mutations link the RNA-binding
            protein HNRNPQ to autophagosome biogenesis
  JOURNAL   Aging Cell 22 (10), e13949 (2023)
   PUBMED   37559347
  REMARK    GeneRIF: Oculopharyngeal muscular dystrophy mutations link the
            RNA-binding protein HNRNPQ to autophagosome biogenesis.
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Semino,F., Schroter,J., Willemsen,M.H., Bast,T., Biskup,S.,
            Beck-Woedl,S., Brennenstuhl,H., Schaaf,C.P., Kolker,S.,
            Hoffmann,G.F., Haack,T.B. and Syrbe,S.
  TITLE     Further evidence for de novo variants in SYNCRIP as the cause of a
            neurodevelopmental disorder
  JOURNAL   Hum Mutat 42 (9), 1094-1100 (2021)
   PUBMED   34157790
  REMARK    GeneRIF: Further evidence for de novo variants in SYNCRIP as the
            cause of a neurodevelopmental disorder.
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 561)
  AUTHORS   Mourelatos,Z., Abel,L., Yong,J., Kataoka,N. and Dreyfuss,G.
  TITLE     SMN interacts with a novel family of hnRNP and spliceosomal
            proteins
  JOURNAL   EMBO J 20 (19), 5443-5452 (2001)
   PUBMED   11574476
REFERENCE   6  (residues 1 to 561)
  AUTHORS   Lau,P.P., Chang,B.H. and Chan,L.
  TITLE     Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a
            component of apobec-1 editosome
  JOURNAL   Biochem Biophys Res Commun 282 (4), 977-983 (2001)
   PUBMED   11352648
REFERENCE   7  (residues 1 to 561)
  AUTHORS   Blanc,V., Navaratnam,N., Henderson,J.O., Anant,S., Kennedy,S.,
            Jarmuz,A., Scott,J. and Davidson,N.O.
  TITLE     Identification of GRY-RBP as an apolipoprotein B RNA-binding
            protein that interacts with both apobec-1 and apobec-1
            complementation factor to modulate C to U editing
  JOURNAL   J Biol Chem 276 (13), 10272-10283 (2001)
   PUBMED   11134005
REFERENCE   8  (residues 1 to 561)
  AUTHORS   Grosset,C., Chen,C.Y., Xu,N., Sonenberg,N., Jacquemin-Sablon,H. and
            Shyu,A.B.
  TITLE     A mechanism for translationally coupled mRNA turnover: interaction
            between the poly(A) tail and a c-fos RNA coding determinant via a
            protein complex
  JOURNAL   Cell 103 (1), 29-40 (2000)
   PUBMED   11051545
REFERENCE   9  (residues 1 to 561)
  AUTHORS   Mizutani,A., Fukuda,M., Ibata,K., Shiraishi,Y. and Mikoshiba,K.
  TITLE     SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear
            ribonucleoprotein R, interacts with ubiquitous synaptotagmin
            isoforms
  JOURNAL   J Biol Chem 275 (13), 9823-9831 (2000)
   PUBMED   10734137
REFERENCE   10 (residues 1 to 561)
  AUTHORS   Harris,C.E., Boden,R.A. and Astell,C.R.
  TITLE     A novel heterogeneous nuclear ribonucleoprotein-like protein
            interacts with NS1 of the minute virus of mice
  JOURNAL   J Virol 73 (1), 72-80 (1999)
   PUBMED   9847309
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136082.22.
            
            On or before Apr 28, 2025 this sequence version replaced
            XP_005248692.1, XP_054210016.1.
            
            Summary: This gene encodes a member of the cellular heterogeneous
            nuclear ribonucleoprotein (hnRNP) family. hnRNPs are RNA binding
            proteins that complex with heterogeneous nuclear RNA (hnRNA) and
            regulate alternative splicing, polyadenylation, and other aspects
            of mRNA metabolism and transport. The encoded protein plays a role
            in multiple aspects of mRNA maturation and is associated with
            several multiprotein complexes including the apoB RNA
            editing-complex and survival of motor neurons (SMN) complex.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene, and a pseudogene of this
            gene is located on the short arm of chromosome 20. [provided by
            RefSeq, Dec 2011].
            
            Transcript Variant: This variant (5) differs in the 5' UTR, 3' UTR,
            and coding region compared to variant 1. The resulting isoform (5)
            is shorter and has a distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2077487.1,
                                           SRR14038197.1571696.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.3"
     Protein         1..561
                     /product="heterogeneous nuclear ribonucleoprotein Q
                     isoform 5"
                     /note="NS1-associated protein 1; heterogeneous nuclear
                     ribonucleoprotein Q; glycine- and tyrosine-rich
                     RNA-binding protein"
                     /calculated_mol_wt=62397
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          23..107
                     /region_name="NURR_hnRNPQ"
                     /note="NURR (N-terminal unit for RNA recognition) domain
                     found in heterogeneous nuclear ribonucleoprotein Q
                     (hnRNPQ) and similar proteins; cd21066"
                     /db_xref="CDD:410954"
     Region          103..553
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            221
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            363
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:12601080; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            444
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          460..488
                     /region_name="3 X 4 AA repeats of Y-Y-G-Y"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            496
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            510
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          518..549
                     /region_name="Interaction with SMN.
                     /evidence=ECO:0000269|PubMed:11574476"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            518
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            526
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            536
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            539
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     CDS             1..561
                     /gene="SYNCRIP"
                     /gene_synonym="GRY-RBP; GRYRBP; hnRNP-Q; HNRNPQ; HNRPQ1;
                     NSAP1; PP68"
                     /coded_by="NM_001159676.2:103..1788"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS93966.1"
                     /db_xref="GeneID:10492"
                     /db_xref="HGNC:HGNC:16918"
                     /db_xref="MIM:616686"
ORIGIN      
        1 matehvngng teepmdttsa vihsenfqtl ldaglpqkva ekldeiyvag lvahsdlder
       61 aiealkefne dgalavlqqf kdsdlshvqn ksaflcgvmk tyrqrekqgt kvadsskgpd
      121 eakikaller tgytldvttg qrkyggpppd svysgqqpsv gteifvgkip rdlfedelvp
      181 lfekagpiwd lrlmmdpltg lnrgyafvtf ctkeaaqeav klynnheirs gkhigvcisv
      241 annrlfvgsi pksktkeqil eefskvtegl tdvilyhqpd dkkknrgfcf leyedhktaa
      301 qarrrlmsgk vkvwgnvgtv ewadpiedpd pevmakvkvl fvrnlantvt eeilekafsq
      361 fgklervkkl kdyafihfde rdgavkamee mngkdlegen ieivfakppd qkrkerkaqr
      421 qaaknqmydd yyyygpphmp pptrgrgrgg rggygyppdy ygyedyydyy gydyhnyrgg
      481 yedpyygyed fqvgargrgg rgargaapsr grgaapprgr agysqrggpg sargvrgarg
      541 gaqqqrgrgg kgveagpdll q
//
LOCUS       NP_001427918             523 aa            linear   PRI 21-NOV-2025
DEFINITION  complement factor I isoform 12 precursor [Homo sapiens].
ACCESSION   NP_001427918 XP_054205921
VERSION     NP_001427918.1
DBSOURCE    REFSEQ: accession NM_001440989.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Moreno,R. and Broderick,L.
  TITLE     Complement factor I deficiency: Diverse phenotypes
  JOURNAL   J Allergy Clin Immunol 156 (2), 305-307 (2025)
   PUBMED   40127737
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Schwotzer,N., Fakhouri,F., Martins,P.V., Delmas,Y., Caillard,S.,
            Zuber,J., Moranne,O., Mesnard,L., Fremeaux-Bacchi,V. and
            El-Sissy,C.
  TITLE     Hot Spot of Complement Factor I Rare Variant p.Ile357Met in
            Patients With Hemolytic Uremic Syndrome
  JOURNAL   Am J Kidney Dis 84 (2), 244-249 (2024)
   PUBMED   38423159
  REMARK    GeneRIF: Hot Spot of Complement Factor I Rare Variant p.Ile357Met
            in Patients With Hemolytic Uremic Syndrome.
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Felberg,A., Bienkowski,M., Stokowy,T., Myszczynski,K.,
            Polakiewicz,Z., Kitowska,K., Sadej,R., Mohlin,F., Kuzniewska,A.,
            Kowalska,D., Stasilojc,G., Jongerius,I., Spaapen,R.,
            Mesa-Guzman,M., Montuenga,L.M., Blom,A.M., Pio,R. and Okroj,M.
  TITLE     Elevated expression of complement factor I in lung cancer cells
            associates with shorter survival-Potentially via non-canonical
            mechanism
  JOURNAL   Transl Res 269, 1-13 (2024)
   PUBMED   38395390
  REMARK    GeneRIF: Elevated expression of complement factor I in lung cancer
            cells associates with shorter survival-Potentially via
            non-canonical mechanism.
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Massey,V., Nguyen,C.E., Francois,T., De Bruycker,J.J., Bonnefoy,A.,
            Lapeyraque,A.L. and Decaluwe,H.
  TITLE     CNS Inflammation as the First Sign of Complement Factor I
            Deficiency: A Severe Myelitis Treated With Intense Immunotherapy
            and Eculizumab
  JOURNAL   Neurol Neuroimmunol Neuroinflamm 11 (2), e200191 (2024)
   PUBMED   38134378
  REMARK    GeneRIF: CNS Inflammation as the First Sign of Complement Factor I
            Deficiency.
REFERENCE   5  (residues 1 to 523)
  AUTHORS   van de Ven,J.P., Nilsson,S.C., Tan,P.L., Buitendijk,G.H.,
            Ristau,T., Mohlin,F.C., Nabuurs,S.B., Schoenmaker-Koller,F.E.,
            Smailhodzic,D., Campochiaro,P.A., Zack,D.J., Duvvari,M.R.,
            Bakker,B., Paun,C.C., Boon,C.J., Uitterlinden,A.G., Liakopoulos,S.,
            Klevering,B.J., Fauser,S., Daha,M.R., Katsanis,N., Klaver,C.C.,
            Blom,A.M., Hoyng,C.B. and den Hollander,A.I.
  TITLE     A functional variant in the CFI gene confers a high risk of
            age-related macular degeneration
  JOURNAL   Nat Genet 45 (7), 813-817 (2013)
   PUBMED   23685748
  REMARK    GeneRIF: these findings demonstrate that rare, highly penetrant
            mutations in CFI contribute to the genetic burden of age-related
            macular degeneration.
REFERENCE   6  (residues 1 to 523)
  AUTHORS   Martin,B. and Smith,R.J.H.
  TITLE     C3 Glomerulopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301598
REFERENCE   7  (residues 1 to 523)
  AUTHORS   Noris,M., Bresin,E., Mele,C. and Remuzzi,G.
  TITLE     Genetic Atypical Hemolytic-Uremic Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301541
REFERENCE   8  (residues 1 to 523)
  AUTHORS   DiScipio,R.G.
  TITLE     Ultrastructures and interactions of complement factors H and I
  JOURNAL   J Immunol 149 (8), 2592-2599 (1992)
   PUBMED   1401896
REFERENCE   9  (residues 1 to 523)
  AUTHORS   Shiang,R., Murray,J.C., Morton,C.C., Buetow,K.H., Wasmuth,J.J.,
            Olney,A.H., Sanger,W.G. and Goldberger,G.
  TITLE     Mapping of the human complement factor I gene to 4q25
  JOURNAL   Genomics 4 (1), 82-86 (1989)
   PUBMED   2563353
REFERENCE   10 (residues 1 to 523)
  AUTHORS   Catterall,C.F., Lyons,A., Sim,R.B., Day,A.J. and Harris,T.J.
  TITLE     Characterization of primary amino acid sequence of human complement
            control protein factor I from an analysis of cDNA clones
  JOURNAL   Biochem J 242 (3), 849-856 (1987)
   PUBMED   2954545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC126283.3.
            
            On Jun 4, 2025 this sequence version replaced XP_054205921.1.
            
            Summary: This gene encodes a serine proteinase that is essential
            for regulating the complement cascade. The encoded preproprotein is
            cleaved to produce both heavy and light chains, which are linked by
            disulfide bonds to form a heterodimeric glycoprotein. This
            heterodimer can cleave and inactivate the complement components C4b
            and C3b, and it prevents the assembly of the C3 and C5 convertase
            enzymes. Defects in this gene cause complement factor I deficiency,
            an autosomal recessive disease associated with a susceptibility to
            pyogenic infections. Mutations in this gene have been associated
            with a predisposition to atypical hemolytic uremic syndrome, a
            disease characterized by acute renal failure, microangiopathic
            hemolytic anemia and thrombocytopenia. Primary glomerulonephritis
            with immune deposits and age-related macular degeneration are other
            conditions associated with mutations of this gene. [provided by
            RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN04284274
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..523
                     /product="complement factor I isoform 12 precursor"
                     /EC_number="3.4.21.45"
                     /note="C3b-inactivator; Konglutinogen-activating factor;
                     complement factor I heavy chain; complement component I;
                     C3B/C4B inactivator; complement control protein factor I;
                     light chain of factor I"
                     /calculated_mol_wt=56887
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2281
     Region          43..108
                     /region_name="FIMAC"
                     /note="factor I membrane attack complex; smart00057"
                     /db_xref="CDD:214493"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Region          114..215
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     Region          224..256
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(227,235,246..247)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(239,242,246,252..253)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            249..253
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          257..293
                     /region_name="Ldl_recept_a"
                     /note="Low-density lipoprotein receptor domain class A;
                     pfam00057"
                     /db_xref="CDD:395011"
     Site            order(264,272,283..284)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(276,279,283,289..290)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            286..290
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          339..>512
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; smart00020"
                     /db_xref="CDD:214473"
     Site            340
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            464
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Site            494
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     CDS             1..523
                     /gene="CFI"
                     /gene_synonym="AHUS3; ARMD13; C3b-INA; C3BINA; FI; IF;
                     KAF"
                     /coded_by="NM_001440989.1:29..1600"
                     /note="isoform 12 precursor is encoded by transcript
                     variant 17"
                     /db_xref="GeneID:3426"
                     /db_xref="HGNC:HGNC:5394"
                     /db_xref="MIM:217030"
ORIGIN      
        1 mkllhvfllf lcfhlrfckv tytsqedlve kkclakkyth lscdkvfcqp wqrciegtcv
       61 cklpyqcpkn gtavcatnrr sfptycqqks leclhpgtkf lnngtctaeg kfsvslkhgn
      121 tdsegivevk lvdqdktmfi cksswsmrea nvacldlgfq qgadtqrrfk lsdlsinste
      181 clhvhcrgle tslaectftk rrtmgyqdfa dvvcytqkad spmddffqcv ngkyisqmka
      241 cdgindcgdq sdelcckacq gkgfhcksgv cipsqyqcng evdcitgede vgcagfasvt
      301 qeeteiltad mdaerrriks llpklscgvk nrmhirrkri vggkraqlgd lpwqvaikda
      361 sgitcggiyi ggcwiltaah clraskthry qiwttvvdwi hpdlkrivie yvdriifhen
      421 ynagtyqndi aliemkkdgn kkdcelprsi pacvpwspyl fqpndtcivs gwgrekdner
      481 vfslqwgevk lisncskfyg nrfyekemec agcnlisvls rik
//
LOCUS       NP_001398028             390 aa            linear   PRI 21-NOV-2025
DEFINITION  eukaryotic initiation factor 4A-III isoform 2 [Homo sapiens].
ACCESSION   NP_001398028 XP_011523824
VERSION     NP_001398028.1
DBSOURCE    REFSEQ: accession NM_001411099.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Li,J., Xin,Y., Zhang,S., Li,Y., Jiang,M., Zhang,S., Yang,L.,
            Yang,J., Cao,P. and Lu,J.
  TITLE     EIF4A3 is stabilized by the long noncoding RNA BC200 to regulate
            gene expression during Epstein-Barr virus infection
  JOURNAL   J Med Virol 96 (10), e29955 (2024)
   PUBMED   39370864
  REMARK    GeneRIF: EIF4A3 is stabilized by the long noncoding RNA BC200 to
            regulate gene expression during Epstein-Barr virus infection.
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Zhou,Q., Cai,B., Liu,K. and Chen,H.
  TITLE     EIF4A3-Induced Upregulation of hsa_circ_0049396 Attenuates the
            Tumorigenesis of Nasopharyngeal Carcinoma by Regulating the
            Hippo-YAP Pathway
  JOURNAL   DNA Cell Biol 43 (10), 510-519 (2024)
   PUBMED   39133108
  REMARK    GeneRIF: EIF4A3-Induced Upregulation of hsa_circ_0049396 Attenuates
            the Tumorigenesis of Nasopharyngeal Carcinoma by Regulating the
            Hippo-YAP Pathway.
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Jiang,X., Peng,M., Liu,Q., Peng,Q., Oyang,L., Li,S., Xu,X.,
            Shen,M., Wang,J., Li,H., Wu,N., Tan,S., Lin,J., Xia,L., Tang,Y.,
            Luo,X., Liao,Q. and Zhou,Y.
  TITLE     Circular RNA hsa_circ_0000467 promotes colorectal cancer
            progression by promoting eIF4A3-mediated c-Myc translation
  JOURNAL   Mol Cancer 23 (1), 151 (2024)
   PUBMED   39085875
  REMARK    GeneRIF: Circular RNA hsa_circ_0000467 promotes colorectal cancer
            progression by promoting eIF4A3-mediated c-Myc translation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Palacios,I.M., Gatfield,D., St Johnston,D. and Izaurralde,E.
  TITLE     An eIF4AIII-containing complex required for mRNA localization and
            nonsense-mediated mRNA decay
  JOURNAL   Nature 427 (6976), 753-757 (2004)
   PUBMED   14973490
  REMARK    GeneRIF: identification of eIF4AIII and Barentsz as components of a
            conserved protein complex that is essential for mRNA localization
            in flies and nonsense-mediated mRNA decay in mammals
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Chan,C.C., Dostie,J., Diem,M.D., Feng,W., Mann,M., Rappsilber,J.
            and Dreyfuss,G.
  TITLE     eIF4A3 is a novel component of the exon junction complex
  JOURNAL   RNA 10 (2), 200-209 (2004)
   PUBMED   14730019
REFERENCE   8  (residues 1 to 390)
  AUTHORS   Le Hir,H., Gatfield,D., Izaurralde,E. and Moore,M.J.
  TITLE     The exon-exon junction complex provides a binding platform for
            factors involved in mRNA export and nonsense-mediated mRNA decay
  JOURNAL   EMBO J 20 (17), 4987-4997 (2001)
   PUBMED   11532962
REFERENCE   9  (residues 1 to 390)
  AUTHORS   Holzmann,K., Gerner,C., Poltl,A., Schafer,R., Obrist,P.,
            Ensinger,C., Grimm,R. and Sauermann,G.
  TITLE     A human common nuclear matrix protein homologous to eukaryotic
            translation initiation factor 4A
  JOURNAL   Biochem Biophys Res Commun 267 (1), 339-344 (2000)
   PUBMED   10623621
  REMARK    GeneRIF: NMP 265, a common part of the nuclear matrix, is located
            in the nucleus via an N-terminal amino acid sequence.
REFERENCE   10 (residues 1 to 390)
  AUTHORS   Li,Q., Imataka,H., Morino,S., Rogers,G.W. Jr., Richter-Cook,N.J.,
            Merrick,W.C. and Sonenberg,N.
  TITLE     Eukaryotic translation initiation factor 4AIII (eIF4AIII) is
            functionally distinct from eIF4AI and eIF4AII
  JOURNAL   Mol Cell Biol 19 (11), 7336-7346 (1999)
   PUBMED   10523622
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087741.18.
            
            On Aug 22, 2022 this sequence version replaced XP_011523824.1.
            
            Summary: This gene encodes a member of the DEAD box protein family.
            DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure, such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this family
            are believed to be involved in embryogenesis, spermatogenesis, and
            cellular growth and division. The protein encoded by this gene is a
            nuclear matrix protein. Its amino acid sequence is highly similar
            to the amino acid sequences of the translation initiation factors
            eIF4AI and eIF4AII, two other members of the DEAD box protein
            family. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2678317.1,
                                           SRR14038193.702495.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..390
                     /product="eukaryotic initiation factor 4A-III isoform 2"
                     /EC_number="3.6.4.13"
                     /note="DEAD (Asp-Glu-Ala-Asp) box polypeptide 48;
                     eukaryotic initiation factor 4A-like NUK-34; nuclear
                     matrix protein 265; ATP-dependent RNA helicase DDX48;
                     ATP-dependent RNA helicase eIF4A-3; eukaryotic initiation
                     factor 4A-III; NMP 265; DEAD box protein 48"
                     /calculated_mol_wt=44380
     Region          35..390
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Site            order(40,56,58..62,65,83..90,166..167)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350803"
     Site            order(63,67,83,86,201..203,206)
                     /site_type="other"
                     /note="Mago interface [polypeptide binding]"
                     /db_xref="CDD:350803"
     Site            order(129..130,133..134,153,156..158,180..181,184..189,
                     209..213)
                     /site_type="other"
                     /note="Barentsz interface [polypeptide binding]"
                     /db_xref="CDD:350803"
     CDS             1..390
                     /gene="EIF4A3"
                     /gene_synonym="DDX48; eIF-4A-III; eIF4A-III; eIF4AIII;
                     Fal1; MUK34; NMP265; NUK34; RCPS"
                     /coded_by="NM_001411099.1:168..1340"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS92411.1"
                     /db_xref="GeneID:9775"
                     /db_xref="HGNC:HGNC:18683"
                     /db_xref="MIM:608546"
ORIGIN      
        1 mattatmats gsarkrllke edmtkvefet seevdvtptf dtmglredll rgiyaygfek
       61 psaiqqraik qiikgrdvia qsqsgtgkta tfsisvlqcl diqgllalgd ymnvqchaci
      121 ggtnvgedir kldygqhvva gtpgrvfdmi rrrslrtrai kmlvldeade mlnkgfkeqi
      181 ydvyrylppa tqvvlisatl pheilemtnk fmtdpirilv krdeltlegi kqffvavere
      241 ewkfdtlcdl ydtltitqav ifcntkrkvd wltekmrean ftvssmhgdm pqkeresimk
      301 efrsgasrvl istdvwargl dvpqvsliin ydlpnnrely ihrigrsgry grkgvainfv
      361 knddirilrd ieqyystqid empmnvadli
//
LOCUS       NP_001394258             284 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 30 [Homo sapiens].
ACCESSION   NP_001394258 XP_047288959
VERSION     NP_001394258.1
DBSOURCE    REFSEQ: accession NM_001407329.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            On May 31, 2022 this sequence version replaced XP_047288959.1.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1302347.1,
                                           SRR14372080.187585.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..284
                     /product="tropomyosin alpha-1 chain isoform 30"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=32658
     Region          48..282
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..284
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407329.1:84..938"
                     /note="isoform 30 is encoded by transcript variant 30"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle ediaakekll rvsederdrv
       61 leelhkaeds llaaeeaaak aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegqv rqleeqlrim dqtlkalmaa edkysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledel yaqklkykai seeldhalnd mtsi
//
LOCUS       NP_001427520             419 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform h [Homo sapiens].
ACCESSION   NP_001427520
VERSION     NP_001427520.1
DBSOURCE    REFSEQ: accession NM_001440591.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 419)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 419)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 419)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1965299, SAMEA1966682
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..419
                     /product="polycomb protein EED isoform h"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=47545
     Region          126..166
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <140..416
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          171..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          218..280
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          287..335
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          343..383
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          391..415
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..419
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001440591.1:478..1737"
                     /note="isoform h is encoded by transcript variant 8"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdendd avsiesgtnt erpdtptntp
       61 napgrkswgk gkwkskkcky sfkcvnslke dhnqplfgvq fnwhskegdp lvfatvgsnr
      121 adenfytcaw tydsntshpl lavagsrgii riinpitmqc ikhyvghgna inelkfhprd
      181 pnlllsvskd halrlwniqt dtlvaifggv eghrdevlsa dydllgekim scgmdhslkl
      241 wrinskrmmn aikesydynp nktnrpfisq kihfpdfstr dihrnyvdcv rwlgdlilsk
      301 scenaivcwk pgkmeddidk ikpsesnvti lgrfdysqcd iwymrfsmdf wqkmlalgnq
      361 vgklyvwdle vedphkakct tlthhkcgaa irqtsfsrds siliavcdda siwrwdrlr
//
LOCUS       NP_001427438             645 aa            linear   PRI 21-NOV-2025
DEFINITION  radixin isoform 5 [Homo sapiens].
ACCESSION   NP_001427438
VERSION     NP_001427438.1
DBSOURCE    REFSEQ: accession NM_001440509.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 645)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 645)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 645)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 645)
  AUTHORS   Kruse,T., Benz,C., Garvanska,D.H., Lindqvist,R., Mihalic,F.,
            Coscia,F., Inturi,R., Sayadi,A., Simonetti,L., Nilsson,E., Ali,M.,
            Kliche,J., Moliner Morro,A., Mund,A., Andersson,E., McInerney,G.,
            Mann,M., Jemth,P., Davey,N.E., Overby,A.K., Nilsson,J. and
            Ivarsson,Y.
  TITLE     Large scale discovery of coronavirus-host factor protein
            interaction motifs reveals SARS-CoV-2 specific mechanisms and
            vulnerabilities
  JOURNAL   Nat Commun 12 (1), 6761 (2021)
   PUBMED   34799561
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 645)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 645)
  AUTHORS   Stemmer-Rachamimov,A.O., Gonzalez-Agosti,C., Xu,L., Burwick,J.A.,
            Beauchamp,R., Pinney,D., Louis,D.N. and Ramesh,V.
  TITLE     Expression of NF2-encoded merlin and related ERM family proteins in
            the human central nervous system
  JOURNAL   J Neuropathol Exp Neurol 56 (6), 735-742 (1997)
   PUBMED   9184664
REFERENCE   7  (residues 1 to 645)
  AUTHORS   Hirao,M., Sato,N., Kondo,T., Yonemura,S., Monden,M., Sasaki,T.,
            Takai,Y., Tsukita,S. and Tsukita,S.
  TITLE     Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma
            membrane association: possible involvement of phosphatidylinositol
            turnover and Rho-dependent signaling pathway
  JOURNAL   J Cell Biol 135 (1), 37-51 (1996)
   PUBMED   8858161
REFERENCE   8  (residues 1 to 645)
  AUTHORS   Wilgenbus,K.K., Milatovich,A., Francke,U. and Furthmayr,H.
  TITLE     Molecular cloning, cDNA sequence, and chromosomal assignment of the
            human radixin gene and two dispersed pseudogenes
  JOURNAL   Genomics 16 (1), 199-206 (1993)
   PUBMED   8486357
REFERENCE   9  (residues 1 to 645)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 645)
  AUTHORS   Sato,N., Funayama,N., Nagafuchi,A., Yonemura,S., Tsukita,S. and
            Tsukita,S.
  TITLE     A gene family consisting of ezrin, radixin and moesin. Its specific
            localization at actin filament/plasma membrane association sites
  JOURNAL   J Cell Sci 103 (Pt 1), 131-143 (1992)
   PUBMED   1429901
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002788.3 and AP000901.5.
            
            Summary: Radixin is a cytoskeletal protein that may be important in
            linking actin to the plasma membrane. It is highly similar in
            sequence to both ezrin and moesin. The radixin gene has been
            localized by fluorescence in situ hybridization to 11q23. A
            truncated version representing a pseudogene (RDXP2) was assigned to
            Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was
            mapped to 11p by Southern and PCR analyses. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..645
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..645
                     /product="radixin isoform 5"
                     /calculated_mol_wt=75093
     Region          7..206
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          200..296
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(242..243,245..251,260,281,284..285,288)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(242,245..252,260,281,284..285,288)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(278,282)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            281..296
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          <298..>601
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          310..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35241.1)"
     Region          419..518
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          569..645
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..645
                     /gene="RDX"
                     /gene_synonym="DFNB24"
                     /coded_by="NM_001440509.1:213..2150"
                     /note="isoform 5 is encoded by transcript variant 11"
                     /db_xref="GeneID:5962"
                     /db_xref="HGNC:HGNC:9944"
                     /db_xref="MIM:179410"
ORIGIN      
        1 mpkpinvrvt tmdaelefai qpnttgkqlf dqvvktvglr evwffglqyv dskgystwlk
       61 lnkkvtqqdv kkenplqfkf rakffpedvs eeliqeitqr lfflqvkeai lndeiycppe
      121 tavllasyav qakygdynke ihkpgyland rllpqrvleq hkltkeqwee riqnwheehr
      181 gmlredsmme ylkiaqdlem ygvnyfeikn kkgtelwlgv dalglniyeh ddkltpkigf
      241 pwseirnisf ndkkfvikpi dkkapdfvfy aprlrinkri lalcmgnhel ymrrrkpdti
      301 evqqmkaqar eekhqkqler aqlenekkkr eiaekekeri erekeelmer lkqieeqtik
      361 aqkvesgfhq vgqsglkllt sndpptsvtq sagitgmshn twpktfqvlt aitqlvlikt
      421 kkiknkleeq trkaleldqe rkrakeeaer lekerraaee aksaiakqaa dqmknqeqla
      481 aelaeftaki alleeakkkk eeeatewqhk afaaqedlek tkeelktvms appppppppv
      541 ipptenehde hdennaeasa elsnegvmnh rseeervtet qknervkkql qalsselaqa
      601 rdetkktqnd vlhaenvkag rdkyktlrqi rqgntkqrid efeam
//
LOCUS       NP_001427444             572 aa            linear   PRI 21-NOV-2025
DEFINITION  radixin isoform 8 [Homo sapiens].
ACCESSION   NP_001427444
VERSION     NP_001427444.1
DBSOURCE    REFSEQ: accession NM_001440515.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Kruse,T., Benz,C., Garvanska,D.H., Lindqvist,R., Mihalic,F.,
            Coscia,F., Inturi,R., Sayadi,A., Simonetti,L., Nilsson,E., Ali,M.,
            Kliche,J., Moliner Morro,A., Mund,A., Andersson,E., McInerney,G.,
            Mann,M., Jemth,P., Davey,N.E., Overby,A.K., Nilsson,J. and
            Ivarsson,Y.
  TITLE     Large scale discovery of coronavirus-host factor protein
            interaction motifs reveals SARS-CoV-2 specific mechanisms and
            vulnerabilities
  JOURNAL   Nat Commun 12 (1), 6761 (2021)
   PUBMED   34799561
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Stemmer-Rachamimov,A.O., Gonzalez-Agosti,C., Xu,L., Burwick,J.A.,
            Beauchamp,R., Pinney,D., Louis,D.N. and Ramesh,V.
  TITLE     Expression of NF2-encoded merlin and related ERM family proteins in
            the human central nervous system
  JOURNAL   J Neuropathol Exp Neurol 56 (6), 735-742 (1997)
   PUBMED   9184664
REFERENCE   7  (residues 1 to 572)
  AUTHORS   Hirao,M., Sato,N., Kondo,T., Yonemura,S., Monden,M., Sasaki,T.,
            Takai,Y., Tsukita,S. and Tsukita,S.
  TITLE     Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma
            membrane association: possible involvement of phosphatidylinositol
            turnover and Rho-dependent signaling pathway
  JOURNAL   J Cell Biol 135 (1), 37-51 (1996)
   PUBMED   8858161
REFERENCE   8  (residues 1 to 572)
  AUTHORS   Wilgenbus,K.K., Milatovich,A., Francke,U. and Furthmayr,H.
  TITLE     Molecular cloning, cDNA sequence, and chromosomal assignment of the
            human radixin gene and two dispersed pseudogenes
  JOURNAL   Genomics 16 (1), 199-206 (1993)
   PUBMED   8486357
REFERENCE   9  (residues 1 to 572)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 572)
  AUTHORS   Sato,N., Funayama,N., Nagafuchi,A., Yonemura,S., Tsukita,S. and
            Tsukita,S.
  TITLE     A gene family consisting of ezrin, radixin and moesin. Its specific
            localization at actin filament/plasma membrane association sites
  JOURNAL   J Cell Sci 103 (Pt 1), 131-143 (1992)
   PUBMED   1429901
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002788.3 and AP000901.5.
            
            Summary: Radixin is a cytoskeletal protein that may be important in
            linking actin to the plasma membrane. It is highly similar in
            sequence to both ezrin and moesin. The radixin gene has been
            localized by fluorescence in situ hybridization to 11q23. A
            truncated version representing a pseudogene (RDXP2) was assigned to
            Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was
            mapped to 11p by Southern and PCR analyses. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038192.767004.1, SRR14038195.2662385.1
                                    [ECO:0000331]
            RNAseq introns       :: partial sample support SAMEA2144333,
                                    SAMEA2467144 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..572
                     /product="radixin isoform 8"
                     /calculated_mol_wt=67195
     Region          5..195
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          189..285
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(231..232,234..240,249,270,273..274,277)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(231,234..241,249,270,273..274,277)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(267,271)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            270..285
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          336..445
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          496..572
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..572
                     /gene="RDX"
                     /gene_synonym="DFNB24"
                     /coded_by="NM_001440515.1:214..1932"
                     /note="isoform 8 is encoded by transcript variant 17"
                     /db_xref="GeneID:5962"
                     /db_xref="HGNC:HGNC:9944"
                     /db_xref="MIM:179410"
ORIGIN      
        1 mdaelefaiq pnttgkqlfd qvvktvglre vwffglqyvd skgystwlkl nkkvtqqdvk
       61 kenplqfkfr akffpedvse eliqeitqrl fflqvkeail ndeiycppet avllasyavq
      121 akygdynkei hkpgylandr llpqrvleqh kltkeqweer iqnwheehrg mlredsmmey
      181 lkiaqdlemy gvnyfeiknk kgtelwlgvd alglniyehd dkltpkigfp wseirnisfn
      241 dkkfvikpid kkapdfvfya prlrinkril alcmgnhely mrrrkpdtie vqqmkaqare
      301 ekhqkqlera qlenekkkre iaekekerie rekeelmerl kqieeqtika qkeleeqtrk
      361 aleldqerkr akeeaerlek erraaeeaks aiakqaadqm knqeqlaael aeftakiall
      421 eeakkkkeee atewqhkafa aqedlektke elktvmsapp ppppppvipp tenehdehde
      481 nnaeasaels negvmnhrse eervtetqkn ervkkqlqal sselaqarde tkktqndvlh
      541 aenvkagrdk yktlrqirqg ntkqridefe am
//
LOCUS       NP_001428018             730 aa            linear   PRI 21-NOV-2025
DEFINITION  fibroblast growth factor receptor 2 isoform 19 precursor [Homo
            sapiens].
ACCESSION   NP_001428018 XP_024303657 XP_054221146
VERSION     NP_001428018.1
DBSOURCE    REFSEQ: accession NM_001441089.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Chen,C.P., Huang,J.P., Huang,K.S., Chen,Y.Y., Wu,F.T., Pan,Y.T.,
            Chiu,C.L. and Wang,W.
  TITLE     Perinatal imaging findings of a fetus with Pfeiffer syndrome and a
            heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation in FGFR2
            presenting a cloverleaf skull, craniosynostosis and short limbs on
            prenatal ultrasound mimicking thanatophoric dysplasia type II
  JOURNAL   Taiwan J Obstet Gynecol 63 (3), 387-390 (2024)
   PUBMED   38802203
  REMARK    GeneRIF: Perinatal imaging findings of a fetus with Pfeiffer
            syndrome and a heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation
            in FGFR2 presenting a cloverleaf skull, craniosynostosis and short
            limbs on prenatal ultrasound mimicking thanatophoric dysplasia type
            II.
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Lian,Y., Bodian,D. and Shehu,A.
  TITLE     Elucidating the Role of Wildtype and Variant FGFR2 Structural
            Dynamics in (Dys)Function and Disorder
  JOURNAL   Int J Mol Sci 25 (8), 4523 (2024)
   PUBMED   38674107
  REMARK    GeneRIF: Elucidating the Role of Wildtype and Variant FGFR2
            Structural Dynamics in (Dys)Function and Disorder.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 730)
  AUTHORS   Xu,N., Hung,K.L., Gong,X., Fan,D., Tian,Y., Yan,M., Wei,Y. and
            Wang,S.
  TITLE     Genetic insights into the 'sandwich fusion' subtype of Klippel-Feil
            syndrome: novel FGFR2 mutations identified by 21 cases of
            whole-exome sequencing
  JOURNAL   Orphanet J Rare Dis 19 (1), 141 (2024)
   PUBMED   38561822
  REMARK    GeneRIF: Genetic insights into the 'sandwich fusion' subtype of
            Klippel-Feil syndrome: novel FGFR2 mutations identified by 21 cases
            of whole-exome sequencing.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 730)
  AUTHORS   Wenger,T.L., Hing,A.V. and Evans,K.N.
  TITLE     Apert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31145570
REFERENCE   5  (residues 1 to 730)
  AUTHORS   Wenger,T., Miller,D. and Evans,K.
  TITLE     FGFR Craniosynostosis Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301628
REFERENCE   6  (residues 1 to 730)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   7  (residues 1 to 730)
  AUTHORS   Dell,K.R. and Williams,L.T.
  TITLE     A novel form of fibroblast growth factor receptor 2. Alternative
            splicing of the third immunoglobulin-like domain confers ligand
            binding specificity
  JOURNAL   J Biol Chem 267 (29), 21225-21229 (1992)
   PUBMED   1400433
REFERENCE   8  (residues 1 to 730)
  AUTHORS   Luqmani,Y.A., Graham,M. and Coombes,R.C.
  TITLE     Expression of basic fibroblast growth factor, FGFR1 and FGFR2 in
            normal and malignant human breast, and comparison with other normal
            tissues
  JOURNAL   Br J Cancer 66 (2), 273-280 (1992)
   PUBMED   1380281
REFERENCE   9  (residues 1 to 730)
  AUTHORS   Katoh,M., Hattori,Y., Sasaki,H., Tanaka,M., Sugano,K., Yazaki,Y.,
            Sugimura,T. and Terada,M.
  TITLE     K-sam gene encodes secreted as well as transmembrane receptor
            tyrosine kinase
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 2960-2964 (1992)
   PUBMED   1313574
REFERENCE   10 (residues 1 to 730)
  AUTHORS   Miki,T., Bottaro,D.P., Fleming,T.P., Smith,C.L., Burgess,W.H.,
            Chan,A.M. and Aaronson,S.A.
  TITLE     Determination of ligand-binding specificity by alternative
            splicing: two distinct growth factor receptors encoded by a single
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 246-250 (1992)
   PUBMED   1309608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009988.12.
            
            On or before Jun 5, 2025 this sequence version replaced
            XP_024303657.1, XP_054221146.1.
            
            Summary: The protein encoded by this gene is a member of the
            fibroblast growth factor receptor family, where amino acid sequence
            is highly conserved between members and throughout evolution. FGFR
            family members differ from one another in their ligand affinities
            and tissue distribution. A full-length representative protein
            consists of an extracellular region, composed of three
            immunoglobulin-like domains, a single hydrophobic membrane-spanning
            segment and a cytoplasmic tyrosine kinase domain. The extracellular
            portion of the protein interacts with fibroblast growth factors,
            setting in motion a cascade of downstream signals, ultimately
            influencing mitogenesis and differentiation. This particular family
            member is a high-affinity receptor for acidic, basic and/or
            keratinocyte growth factor, depending on the isoform. Mutations in
            this gene are associated with Crouzon syndrome, Pfeiffer syndrome,
            Craniosynostosis, Apert syndrome, Jackson-Weiss syndrome,
            Beare-Stevenson cutis gyrata syndrome, Saethre-Chotzen syndrome,
            and syndromic craniosynostosis. Multiple alternatively spliced
            transcript variants encoding different isoforms have been noted for
            this gene. [provided by RefSeq, Jan 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2154617.1,
                                           SRR14038196.364860.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:1309608)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..730
                     /product="fibroblast growth factor receptor 2 isoform 19
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="protein tyrosine kinase, receptor like 14;
                     bacteria-expressed kinase; keratinocyte growth factor
                     receptor; BEK fibroblast growth factor receptor"
                     /calculated_mol_wt=79745
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2298
     Region          65..159
                     /region_name="IgI_2_FGFR"
                     /note="Second immunoglobulin (Ig)-like domain of
                     fibroblast growth factor (FGF) receptor; member of the
                     I-set of IgSF domains; cd05857"
                     /db_xref="CDD:409443"
     Region          65..68
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409443"
     Region          76..81
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409443"
     Site            order(77,79,81)
                     /site_type="other"
                     /note="FGF binding site [polypeptide binding]"
                     /db_xref="CDD:409443"
     Site            order(78,85..87,89)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409443"
     Region          85..93
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409443"
     Region          99..104
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409443"
     Region          107..109
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409443"
     Region          118..121
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409443"
     Region          125..130
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409443"
     Region          139..146
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409443"
     Region          149..159
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409443"
     Region          167..271
                     /region_name="IgI_3_FGFR2"
                     /note="Third immunoglobulin (Ig)-like domain of fibroblast
                     growth factor receptor 2 (FGFR2); member of the I-set of
                     Ig superfamily (IgSF) domains; cd05858"
                     /db_xref="CDD:409444"
     Region          167..170
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409444"
     Region          174..178
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409444"
     Region          186..193
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409444"
     Site            order(191,196..198,227..228,232,236,257)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409444"
     Region          197..204
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409444"
     Region          219..224
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409444"
     Region          236..241
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409444"
     Region          249..257
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409444"
     Region          260..268
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409444"
     Region          365..677
                     /region_name="PTKc_FGFR2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Fibroblast Growth Factor Receptor 2; cd05101"
                     /db_xref="CDD:270679"
     Site            order(396..397,399,404,424,426,443,473..476,480,535,
                     539..540,542,553,571..575,584,618)
                     /site_type="active"
                     /db_xref="CDD:270679"
     Site            order(396..397,399,404,424,426,443,473..476,480,539..540,
                     542,553)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270679"
     Site            order(535,539,571..575,584,618)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270679"
     Site            552..577
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270679"
     CDS             1..730
                     /gene="FGFR2"
                     /gene_synonym="BBDS; BEK; BFR-1; CD332; CEK3; CFD1; ECT1;
                     JWS; K-SAM; KGFR; TK14; TK25"
                     /coded_by="NM_001441089.1:634..2826"
                     /note="isoform 19 precursor is encoded by transcript
                     variant 19"
                     /db_xref="GeneID:2263"
                     /db_xref="HGNC:HGNC:3689"
                     /db_xref="MIM:176943"
ORIGIN      
        1 mvswgrficl vvvtmatlsl arpsfslved ttlepedais sgddeddtdg aedfvsensn
       61 nkrapywtnt ekmekrlhav paantvkfrc paggnpmptm rwlkngkefk qehriggykv
      121 rnqhwslime svvpsdkgny tcvveneygs inhtyhldvv ersphrpilq aglpanastv
      181 vggdvefvck vysdaqphiq wikhvekngs kygpdglpyl kvlkaagvnt tdkeievlyi
      241 rnvtfedage ytclagnsig isfhsawltv lpapgrekei taspdyleia iycigvflia
      301 cmvvtvilcr mknttkkpdf ssqpavhklt kriplrrqvs aessssmnsn tplvrittrl
      361 sstadtpmla gvseyelped pkwefprdkl tlgkplgegc fgqvvmaeav gidkdkpkea
      421 vtvavkmlkd datekdlsdl vsememmkmi gkhkniinll gactqdgply viveyaskgn
      481 lreylrarrp pgmeysydin rvpeeqmtfk dlvsctyqla rgmeylasqk cihrdlaarn
      541 vlvtennvmk iadfglardi nnidyykktt ngrlpvkwma pealfdrvyt hqsdvwsfgv
      601 lmweiftlgg spypgipvee lfkllkeghr mdkpanctne lymmmrdcwh avpsqrptfk
      661 qlvedldril tlttneeyld lsqpleqysp sypdtrsscs sgddsvfspd pmpyepclpq
      721 yphingsvkt
//
LOCUS       NP_001274677             353 aa            linear   PRI 21-NOV-2025
DEFINITION  squalene synthase isoform 2 [Homo sapiens].
ACCESSION   NP_001274677 XP_005272435
VERSION     NP_001274677.1
DBSOURCE    REFSEQ: accession NM_001287748.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Kanmalar,M., Kamal,R., Abdul Sani,S.F., Pathmanathan,D., Bm
            Said,N.A., Paramanantham,Y., Abd Jamil,A.H., Mun,K.S.,
            Kuppusamy,S., Almugren,K.S., Almajid,H.F. and Bradley,D.A.
  TITLE     Spectroscopic diagnosis and metabolite characterization of
            cisplatin resistance regulated by FDFT1 in bladder cancer tissue
  JOURNAL   Appl Radiat Isot 210, 111372 (2024)
   PUBMED   38810354
  REMARK    GeneRIF: Spectroscopic diagnosis and metabolite characterization of
            cisplatin resistance regulated by FDFT1 in bladder cancer tissue.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Avci,D., Heidasch,R., Costa,M., Luchtenborg,C., Kale,D., Brugger,B.
            and Lemberg,M.K.
  TITLE     Intramembrane protease SPP defines a cholesterol-regulated
            abundance control of the mevalonate pathway enzyme squalene
            synthase
  JOURNAL   J Biol Chem 300 (2), 105644 (2024)
   PUBMED   38218226
  REMARK    GeneRIF: Intramembrane protease SPP defines a cholesterol-regulated
            abundance control of the mevalonate pathway enzyme squalene
            synthase.
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Jiang,H., Tang,E., Chen,Y., Liu,H., Zhao,Y., Lin,M. and He,L.
  TITLE     Squalene synthase predicts poor prognosis in stage I-III colon
            adenocarcinoma and synergizes squalene epoxidase to promote tumor
            progression
  JOURNAL   Cancer Sci 113 (3), 971-985 (2022)
   PUBMED   34939274
  REMARK    GeneRIF: Squalene synthase predicts poor prognosis in stage I-III
            colon adenocarcinoma and synergizes squalene epoxidase to promote
            tumor progression.
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Nakae,A., Kodama,M., Okamoto,T., Tokunaga,M., Shimura,H.,
            Hashimoto,K., Sawada,K., Kodama,T., Copeland,N.G., Jenkins,N.A. and
            Kimura,T.
  TITLE     Ubiquitin specific peptidase 32 acts as an oncogene in epithelial
            ovarian cancer by deubiquitylating farnesyl-diphosphate
            farnesyltransferase 1
  JOURNAL   Biochem Biophys Res Commun 552, 120-127 (2021)
   PUBMED   33744759
  REMARK    GeneRIF: Ubiquitin specific peptidase 32 acts as an oncogene in
            epithelial ovarian cancer by deubiquitylating farnesyl-diphosphate
            farnesyltransferase 1.
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Guan,G., Jiang,G., Koch,R.L. and Shechter,I.
  TITLE     Molecular cloning and functional analysis of the promoter of the
            human squalene synthase gene
  JOURNAL   J Biol Chem 270 (37), 21958-21965 (1995)
   PUBMED   7665618
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Soltis,D.A., McMahon,G., Caplan,S.L., Dudas,D.A., Chamberlin,H.A.,
            Vattay,A., Dottavio,D., Rucker,M.L., Engstrom,R.G.,
            Cornell-Kennon,S.A. et al.
  TITLE     Expression, purification, and characterization of the human
            squalene synthase: use of yeast and baculoviral systems
  JOURNAL   Arch Biochem Biophys 316 (2), 713-723 (1995)
   PUBMED   7864626
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Shechter,I., Conrad,D.G., Hart,I., Berger,R.C., McKenzie,T.L.,
            Bleskan,J. and Patterson,D.
  TITLE     Localization of the squalene synthase gene (FDFT1) to human
            chromosome 8p22-p23.1
  JOURNAL   Genomics 20 (1), 116-118 (1994)
   PUBMED   8020937
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Jiang,G., McKenzie,T.L., Conrad,D.G. and Shechter,I.
  TITLE     Transcriptional regulation by lovastatin and 25-hydroxycholesterol
            in HepG2 cells and molecular cloning and expression of the cDNA for
            the human hepatic squalene synthase
  JOURNAL   J Biol Chem 268 (17), 12818-12824 (1993)
   PUBMED   7685352
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Coman,D., Vissers,L., Waterham,H., Christodoulou,J., Wevers,R.A.
            and Pitt,J.
  TITLE     Squalene Synthase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   32027475
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC069185.7.
            
            On Dec 19, 2013 this sequence version replaced XP_005272435.1.
            
            Summary: This gene encodes a membrane-associated enzyme located at
            a branch point in the mevalonate pathway. The encoded protein is
            the first specific enzyme in cholesterol biosynthesis, catalyzing
            the dimerization of two molecules of farnesyl diphosphate in a
            two-step reaction to form squalene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (7) differs at the 5' end and
            initiates translation from an in-frame downstream start codon
            compared to variant 1. The resulting isoform (2) has a shorter
            N-terminus compared to isoform 1. Variants 4-8 encode the same
            isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK316351.1, SRR14038194.1630656.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p23.1"
     Protein         1..353
                     /product="squalene synthase isoform 2"
                     /EC_number="2.5.1.21"
                     /note="presqualene-di-diphosphate synthase; squalene
                     synthase; FPP:FPP farnesyltransferase; squalene
                     synthetase"
                     /calculated_mol_wt=40639
     Region          1..306
                     /region_name="Isoprenoid_Biosyn_C1"
                     /note="Isoprenoid Biosynthesis enzymes, Class 1; cl00210"
                     /db_xref="CDD:469660"
     Site            order(9,16,20,107,115,119,147,154..155,159,164,224..225,
                     229)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:173831"
     Site            order(9,13,16,20,107,112,116,144,147,154..155,158..159,
                     164,224..225)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:173831"
     Site            order(16..20,155..159)
                     /site_type="active"
                     /note="substrate-Mg2+ binding site [active]"
                     /db_xref="CDD:173831"
     Site            16..20
                     /site_type="other"
                     /note="aspartate-rich region 1"
                     /db_xref="CDD:173831"
     Site            155..159
                     /site_type="other"
                     /note="aspartate-rich region 2"
                     /db_xref="CDD:173831"
     CDS             1..353
                     /gene="FDFT1"
                     /gene_synonym="DGPT; ERG9; SQS; SQSD; SS"
                     /coded_by="NM_001287748.2:242..1303"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS75696.1"
                     /db_xref="GeneID:2222"
                     /db_xref="HGNC:HGNC:3629"
                     /db_xref="MIM:184420"
ORIGIN      
        1 mrnavcifyl vlraldtled dmtisvekkv pllhnfhsfl yqpdwrfmes kekdrqvled
       61 fptislefrn laekyqtvia dicrrmgigm aefldkhvts eqewdkychy vaglvgigls
      121 rlfsasefed plvgedtera nsmglflqkt niirdyledq qggrefwpqe vwsryvkklg
      181 dfakpenidl avqclnelit nalhhipdvi tylsrlrnqs vfnfcaipqv maiatlaacy
      241 nnqqvfkgav kirkgqavtl mmdatnmpav kaiiyqymee iyhripdsdp sssktrqiis
      301 tirtqnlpnc qlisrshysp iylsfvmlla alswqylttl sqvtedyvqt geh
//
LOCUS       NP_001411345             206 aa            linear   PRI 21-NOV-2025
DEFINITION  synaptosomal-associated protein 25 isoform SNAP25B [Homo sapiens].
ACCESSION   NP_001411345 XP_005260865 XP_054179861
VERSION     NP_001411345.1
DBSOURCE    REFSEQ: accession NM_001424416.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Wang,W., Gao,W., Gong,P., Song,W., Bu,X., Hou,J., Zhang,L. and
            Zhao,B.
  TITLE     Neuronal-specific TNFAIP1 ablation attenuates postoperative
            cognitive dysfunction via targeting SNAP25 for K48-linked
            ubiquitination
  JOURNAL   Cell Commun Signal 21 (1), 356 (2023)
   PUBMED   38102610
  REMARK    GeneRIF: Neuronal-specific TNFAIP1 ablation attenuates
            postoperative cognitive dysfunction via targeting SNAP25 for
            K48-linked ubiquitination.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Bolognesi,E., Guerini,F.R., Carta,A., Chiappedi,M., Sotgiu,S.,
            Mensi,M.M., Agliardi,C., Zanzottera,M. and Clerici,M.
  TITLE     The Role of SNAP-25 in Autism Spectrum Disorders Onset Patterns
  JOURNAL   Int J Mol Sci 24 (18), 14042 (2023)
   PUBMED   37762342
  REMARK    GeneRIF: The Role of SNAP-25 in Autism Spectrum Disorders Onset
            Patterns.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Yazar,V., Kuhlwein,J.K., Knehr,A., Grozdanov,V., Ekici,A.B.,
            Ludolph,A.C. and Danzer,K.M.
  TITLE     Impaired ATF3 signaling involves SNAP25 in SOD1 mutant ALS patients
  JOURNAL   Sci Rep 13 (1), 12019 (2023)
   PUBMED   37491426
  REMARK    GeneRIF: Impaired ATF3 signaling involves SNAP25 in SOD1 mutant ALS
            patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Zhang,J., Hou,S., Chi,X.Q., Shan,H.F., Li,X.W., Zhang,Q.J.,
            Wang,J.L. and Kang,C.B.
  TITLE     Role of SNAP25 on the occurrence and development of eosinophilic
            gastritis
  JOURNAL   Medicine (Baltimore) 102 (29), e34377 (2023)
   PUBMED   37478220
  REMARK    GeneRIF: Role of SNAP25 on the occurrence and development of
            eosinophilic gastritis.
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Hanson,P.I., Otto,H., Barton,N. and Jahn,R.
  TITLE     The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce
            a conformational change in syntaxin
  JOURNAL   J Biol Chem 270 (28), 16955-16961 (1995)
   PUBMED   7622514
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Hata,Y. and Sudhof,T.C.
  TITLE     A novel ubiquitous form of Munc-18 interacts with multiple
            syntaxins. Use of the yeast two-hybrid system to study interactions
            between proteins involved in membrane traffic
  JOURNAL   J Biol Chem 270 (22), 13022-13028 (1995)
   PUBMED   7768895
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Chapman,E.R., An,S., Barton,N. and Jahn,R.
  TITLE     SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin
            via domains that may form coiled coils
  JOURNAL   J Biol Chem 269 (44), 27427-27432 (1994)
   PUBMED   7961655
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Zhao,N., Hashida,H., Takahashi,N. and Sakaki,Y.
  TITLE     Cloning and sequence analysis of the human SNAP25 cDNA
  JOURNAL   Gene 145 (2), 313-314 (1994)
   PUBMED   8056350
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Abicht,A., Muller,J.S. and Lochmuller,H.
  TITLE     Congenital Myasthenic Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354824.8 and AL023913.6.
            
            On or before Sep 22, 2023 this sequence version replaced
            XP_005260865.1, XP_054179861.1.
            
            Summary: Synaptic vesicle membrane docking and fusion is mediated
            by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment
            protein receptors) located on the vesicle membrane (v-SNAREs) and
            the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE
            complex consists of a bundle of four helices, one of which is
            supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on
            the plasma membrane, the protein syntaxin supplies one helix and
            the protein encoded by this gene contributes the other two.
            Therefore, this gene product is a presynaptic plasma membrane
            protein involved in the regulation of neurotransmitter release. Two
            alternative transcript variants encoding different protein isoforms
            have been described for this gene. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.498316.1,
                                           SRR1660807.15579.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.2"
     Protein         1..206
                     /product="synaptosomal-associated protein 25 isoform
                     SNAP25B"
                     /note="resistance to inhibitors of cholinesterase 4
                     homolog; synaptosome associated protein 25kDa;
                     synaptosomal-associated protein, 25kDa"
                     /calculated_mol_wt=23184
     Region          1..75
                     /region_name="Interaction with CENPF.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P60880.1)"
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60880.1)"
     Region          10..82
                     /region_name="SNARE_SNAP25N"
                     /note="N-terminal SNARE motif of SNAP25; cd15894"
                     /db_xref="CDD:277247"
     Site            order(24..25,28..29,31..33,35..40,42..44,46..47,49..50,
                     53..54,56..61,63..65,67..68,70..75,77..78)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277247"
     Site            53
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277247"
     Region          91..142
                     /region_name="SNAP-25"
                     /note="SNAP-25 family; pfam00835"
                     /db_xref="CDD:459955"
     Region          111..120
                     /region_name="Interaction with ZDHHC17.
                     /evidence=ECO:0000269|PubMed:28757145"
                     /note="propagated from UniProtKB/Swiss-Prot (P60880.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P60879; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     Region          143..201
                     /region_name="SNARE_SNAP25C"
                     /note="C-terminal SNARE motif of SNAP25; cd15885"
                     /db_xref="CDD:277238"
     Site            order(143,145..146,149..154,156..157,160..161,163..165,
                     167..168,171..172,174..175,177..182,184..185,188,191,195,
                     198,201)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277238"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P60879; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     Site            174
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277238"
     Site            180..181
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by C.botulinum
                     neurotoxin type E (BoNT/E).
                     /evidence=ECO:0000269|PubMed:9886085; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P60879; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     Site            197..198
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by C.botulinum
                     neurotoxin type A (BoNT/A, botA).
                     /evidence=ECO:0000269|PubMed:9886085,
                     ECO:0000305|PubMed:15592454; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     Site            198..199
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by C.botulinum
                     neurotoxin type C (BoNT/C).
                     /evidence=ECO:0000269|PubMed:9886085,
                     ECO:0000305|PubMed:15592454; propagated from
                     UniProtKB/Swiss-Prot (P60880.1)"
     CDS             1..206
                     /gene="SNAP25"
                     /gene_synonym="bA416N4.2; CMS18; DEE117; dJ1068F16.2;
                     RIC-4; RIC4; SEC9; SNAP; SNAP-25; SUP"
                     /coded_by="NM_001424416.1:448..1068"
                     /note="isoform SNAP25B is encoded by transcript variant
                     13"
                     /db_xref="GeneID:6616"
                     /db_xref="HGNC:HGNC:11132"
                     /db_xref="MIM:600322"
ORIGIN      
        1 maedadmrne leemqrradq ladeslestr rmlqlveesk dagirtlvml deqgeqleri
       61 eegmdqinkd mkeaeknltd lgkfcglcvc pcnklkssda ykkawgnnqd gvvasqparv
      121 vdereqmais ggfirrvtnd arenemdenl eqvsgiignl rhmaldmgne idtqnrqidr
      181 imekadsnkt rideanqrat kmlgsg
//
LOCUS       NP_001424372             298 aa            linear   PRI 21-NOV-2025
DEFINITION  ADP-ribosylation factor-like protein 13B isoform 6 [Homo sapiens].
ACCESSION   NP_001424372 XP_047303617 XP_054201601
VERSION     NP_001424372.1
DBSOURCE    REFSEQ: accession NM_001437443.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Lin,Z., Shen,Y., Li,Y., Lu,C., Zhu,Y., He,R., Cao,Z., Yin,Z.,
            Gao,H., Guo,B., Ma,X., Cao,M. and Luo,M.
  TITLE     Novel compound heterozygous variants in ARL13B lead to Joubert
            syndrome
  JOURNAL   J Cell Physiol 239 (4), e31189 (2024)
   PUBMED   38219074
  REMARK    GeneRIF: Novel compound heterozygous variants in ARL13B lead to
            Joubert syndrome.
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Shi,P., Tian,J., Mallinger,J.C., Ling,D., Deleyrolle,L.P.,
            McIntyre,J.C., Caspary,T., Breunig,J.J. and Sarkisian,M.R.
  TITLE     Increasing Ciliary ARL13B Expression Drives Active and
            Inhibitor-Resistant Smoothened and GLI into Glioma Primary Cilia
  JOURNAL   Cells 12 (19), 2354 (2023)
   PUBMED   37830570
  REMARK    GeneRIF: Increasing Ciliary ARL13B Expression Drives Active and
            Inhibitor-Resistant Smoothened and GLI into Glioma Primary Cilia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Mahajan,D., Madugula,V. and Lu,L.
  TITLE     Rab8 and TNPO1 are ciliary transport adaptors for GTPase Arl13b by
            interacting with its RVEP motif containing ciliary targeting
            sequence
  JOURNAL   J Biol Chem 299 (5), 104604 (2023)
   PUBMED   36907439
  REMARK    GeneRIF: Rab8 and TNPO1 are ciliary transport adaptors for GTPase
            Arl13b by interacting with its RVEP motif containing ciliary
            targeting sequence.
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Hori,Y., Kobayashi,T., Kikko,Y., Kontani,K. and Katada,T.
  TITLE     Domain architecture of the atypical Arf-family GTPase Arl13b
            involved in cilia formation
  JOURNAL   Biochem Biophys Res Commun 373 (1), 119-124 (2008)
   PUBMED   18554500
  REMARK    GeneRIF: These findings suggest that N and C domains of Arl13b
            cooperatively regulate its ciliary localization and that N
            domain-dependent self-association of Arl13b may be important for
            its function in cilia biogenesis.
REFERENCE   6  (residues 1 to 298)
  AUTHORS   Cantagrel,V., Silhavy,J.L., Bielas,S.L., Swistun,D., Marsh,S.E.,
            Bertrand,J.Y., Audollent,S., Attie-Bitach,T., Holden,K.R.,
            Dobyns,W.B., Traver,D., Al-Gazali,L., Ali,B.R., Lindner,T.H.,
            Caspary,T., Otto,E.A., Hildebrandt,F., Glass,I.A., Logan,C.V.,
            Johnson,C.A., Bennett,C., Brancati,F., Valente,E.M., Woods,C.G. and
            Gleeson,J.G.
  CONSRTM   International Joubert Syndrome Related Disorders Study Group
  TITLE     Mutations in the cilia gene ARL13B lead to the classical form of
            Joubert syndrome
  JOURNAL   Am J Hum Genet 83 (2), 170-179 (2008)
   PUBMED   18674751
  REMARK    GeneRIF: ARL13B has an evolutionarily conserved role mediating
            cilia function in multiple organs
REFERENCE   7  (residues 1 to 298)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   8  (residues 1 to 298)
  AUTHORS   Fan,Y., Esmail,M.A., Ansley,S.J., Blacque,O.E., Boroevich,K.,
            Ross,A.J., Moore,S.J., Badano,J.L., May-Simera,H., Compton,D.S.,
            Green,J.S., Lewis,R.A., van Haelst,M.M., Parfrey,P.S.,
            Baillie,D.L., Beales,P.L., Katsanis,N., Davidson,W.S. and
            Leroux,M.R.
  TITLE     Mutations in a member of the Ras superfamily of small GTP-binding
            proteins causes Bardet-Biedl syndrome
  JOURNAL   Nat Genet 36 (9), 989-993 (2004)
   PUBMED   15314642
REFERENCE   9  (residues 1 to 298)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 298)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC117474.7 and AC130896.3.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_047303617.1, XP_054201601.1.
            
            Summary: This gene encodes a member of the ADP-ribosylation
            factor-like family. The encoded protein is a small GTPase that
            contains both N-terminal and C-terminal guanine nucleotide-binding
            motifs. This protein is localized in the cilia and plays a role in
            cilia formation and in maintenance of cilia. Mutations in this gene
            are the cause of Joubert syndrome 8. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.457015.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q11.1-q11.2"
     Protein         1..298
                     /product="ADP-ribosylation factor-like protein 13B isoform
                     6"
                     /note="ADP-ribosylation factor-like 2-like 1; ARL2-like
                     protein 1; ADP ribosylation factor like GTPase 13B"
                     /calculated_mol_wt=34115
     Region          <21..82
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            23..26
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133361"
     Site            59..61
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133361"
     Region          <92..134
                     /region_name="CCDC47"
                     /note="PAT complex subunit CCDC47; cl46382"
                     /db_xref="CDD:480722"
     CDS             1..298
                     /gene="ARL13B"
                     /gene_synonym="ARL2L1; JBTS8"
                     /coded_by="NM_001437443.1:270..1166"
                     /note="isoform 6 is encoded by transcript variant 9"
                     /db_xref="GeneID:200894"
                     /db_xref="HGNC:HGNC:25419"
                     /db_xref="MIM:608922"
ORIGIN      
        1 mfslmasccg wfkrwrepvr lankqdkega lgeadviecl sleklvnehk clcqiepcsa
       61 isgygkkidk sikkglywll hviardfdal neriqkette qraleeqekq eraervrklr
      121 eerkqneqeq aeldgtsgla eldpeptnpf qpiasviien egklerekkn qkmekdsdgc
      181 hlkhkmeheq ietqgqvnhn gqknnefglv enykealtqq lknedetdrp slesangkkk
      241 tkklrmkrnh rveplniddc apesptpppp pppdfyrkpl pplavpqrpn sdahdvis
//
LOCUS       NP_001424358            1032 aa            linear   PRI 21-NOV-2025
DEFINITION  PDZ domain-containing protein 7 isoform 4 [Homo sapiens].
ACCESSION   NP_001424358 XP_011538480 XP_054222740
VERSION     NP_001424358.1
DBSOURCE    REFSEQ: accession NM_001437429.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Nouri,Z., Sarmadi,A., Narrei,S., Kianersi,H., Kianersi,F. and
            Tabatabaiefar,M.A.
  TITLE     Clinical characterizations and molecular genetic study of two
            co-segregating variants in PDZD7 and PDE6C genes leading
            simultaneously to non-syndromic hearing loss and achromatopsia
  JOURNAL   BMC Med Genomics 17 (1), 173 (2024)
   PUBMED   38956522
  REMARK    GeneRIF: Clinical characterizations and molecular genetic study of
            two co-segregating variants in PDZD7 and PDE6C genes leading
            simultaneously to non-syndromic hearing loss and achromatopsia.
            Erratum:[BMC Med Genomics. 2025 Aug 4;18(1):126. doi:
            10.1186/s12920-025-02197-2. PMID: 40760435]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Du,Q., Sun,Q., Gu,X., Wang,J., Li,W., Guo,L. and Li,H.
  TITLE     Novel homozygous variant in the PDZD7 gene in a family with
            nonsyndromic sensorineural hearing loss
  JOURNAL   BMC Med Genomics 15 (1), 135 (2022)
   PUBMED   35715776
  REMARK    GeneRIF: Novel homozygous variant in the PDZD7 gene in a family
            with nonsyndromic sensorineural hearing loss.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1032)
  AUTHORS   Lee,S.Y., Han,J.H., Kim,B.J., Oh,S.H., Lee,S., Oh,D.Y. and
            Choi,B.Y.
  TITLE     Identification of a Potential Founder Effect of a Novel PDZD7
            Variant Involved in Moderate-to-Severe Sensorineural Hearing Loss
            in Koreans
  JOURNAL   Int J Mol Sci 20 (17), 4174 (2019)
   PUBMED   31454969
  REMARK    GeneRIF: PDZD7 can be an important causative gene for moderate to
            severe ARNSHL in Koreans. Moreover, at least some, if not all,
            p.Arg164Trp alleles in Koreans could exert a potential founder
            effect and arise from diverse haplotypes as a mutational hot spot.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1032)
  AUTHORS   Luo,H., Hassan,R.N., Yan,J., Xie,J., Du,P., Hu,Q., Zhu,Y. and
            Jiang,W.
  TITLE     Novel recessive PDZD7 biallelic mutations associated with
            hereditary hearing loss in a Chinese pedigree
  JOURNAL   Gene 709, 65-74 (2019)
   PUBMED   31129248
  REMARK    GeneRIF: Three mutations in PDZD7 gene linked to autosomal
            recessive non-syndromic hearing loss (ARNSHL) were identified in a
            Chinese pedigree. The findings expand not only our knowledge of
            genetic causes of ARNSHL, but also PDZD7 genes mutation spectrum of
            the disease. They will aid personalized genetic counseling,
            molecular diagnostics and clinical management of this condition.
REFERENCE   6  (residues 1 to 1032)
  AUTHORS   Yoshimura,H., Iwasaki,S., Nishio,S.Y., Kumakawa,K., Tono,T.,
            Kobayashi,Y., Sato,H., Nagai,K., Ishikawa,K., Ikezono,T., Naito,Y.,
            Fukushima,K., Oshikawa,C., Kimitsuki,T., Nakanishi,H. and Usami,S.
  TITLE     Massively parallel DNA sequencing facilitates diagnosis of patients
            with Usher syndrome type 1
  JOURNAL   PLoS One 9 (3), e90688 (2014)
   PUBMED   24618850
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1032)
  AUTHORS   Grati,M., Shin,J.B., Weston,M.D., Green,J., Bhat,M.A.,
            Gillespie,P.G. and Kachar,B.
  TITLE     Localization of PDZD7 to the stereocilia ankle-link associates this
            scaffolding protein with the Usher syndrome protein network
  JOURNAL   J Neurosci 32 (41), 14288-14293 (2012)
   PUBMED   23055499
  REMARK    GeneRIF: PDZD7 is a scaffolding component of the ankle-link complex
            in stereocilia and is associated with the Usher syndrome protein
            network.
REFERENCE   8  (residues 1 to 1032)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   9  (residues 1 to 1032)
  AUTHORS   Ebermann,I., Phillips,J.B., Liebau,M.C., Koenekoop,R.K.,
            Schermer,B., Lopez,I., Schafer,E., Roux,A.F., Dafinger,C.,
            Bernd,A., Zrenner,E., Claustres,M., Blanco,B., Nurnberg,G.,
            Nurnberg,P., Ruland,R., Westerfield,M., Benzing,T. and Bolz,H.J.
  TITLE     PDZD7 is a modifier of retinal disease and a contributor to digenic
            Usher syndrome
  JOURNAL   J Clin Invest 120 (6), 1812-1823 (2010)
   PUBMED   20440071
  REMARK    GeneRIF: PDZD7 is a modifier of retinal disease and a contributor
            to digenic Usher syndrome.
REFERENCE   10 (residues 1 to 1032)
  AUTHORS   Schneider,E., Marker,T., Daser,A., Frey-Mahn,G., Beyer,V.,
            Farcas,R., Schneider-Ratzke,B., Kohlschmidt,N., Grossmann,B.,
            Bauss,K., Napiontek,U., Keilmann,A., Bartsch,O., Zechner,U.,
            Wolfrum,U. and Haaf,T.
  TITLE     Homozygous disruption of PDZD7 by reciprocal translocation in a
            consanguineous family: a new member of the Usher syndrome protein
            interactome causing congenital hearing impairment
  JOURNAL   Hum Mol Genet 18 (4), 655-666 (2009)
   PUBMED   19028668
  REMARK    GeneRIF: PDZD7 is a new autosomal-recessive deafness-causing gene
            and a prime candidate gene for Usher syndrome.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133215.17.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_011538480.1, XP_054222740.1.
            
            Summary: This gene encodes a ciliary protein homologous to proteins
            which are mutated in Usher syndrome patients, and mutations and
            translocations involving this gene have been associated with two
            types of Usher syndrome. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.473173.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.31"
     Protein         1..1032
                     /product="PDZ domain-containing protein 7 isoform 4"
                     /note="PDZ domain-containing protein 7; deafness,
                     autosomal recessive 57"
                     /calculated_mol_wt=111550
     Region          84..167
                     /region_name="PDZ1_PDZD7-like"
                     /note="PDZ domain 1 of the canonical isoform 1 of PDZ
                     domain containing 7 (PDZD7), and related domains; cd10833"
                     /db_xref="CDD:467269"
     Site            order(96..102,114,117,146,150,153..154)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467269"
     Region          208..292
                     /region_name="PDZ2_PDZD7-like"
                     /note="PDZ domain 2 of the canonical isoform 1 of PDZ
                     domain containing 7 (PDZD7), and related domains; cd10834"
                     /db_xref="CDD:467270"
     Site            order(221..227,239,242,271,275,278..279)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467270"
     Region          323..380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H5P4.2)"
     Region          444..464
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H5P4.2)"
     Region          553..629
                     /region_name="HN_PDZD7_like"
                     /note="harmonin_N_like domain, a protein-binding module of
                     PDZ domain-containing protein 7 and related proteins;
                     cd07358"
                     /db_xref="CDD:259824"
     Site            order(554,557,561,574,577,580..581,584)
                     /site_type="other"
                     /note="putative protein binding site [polypeptide
                     binding]"
                     /db_xref="CDD:259824"
     Region          753..863
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H5P4.2)"
     Region          859..947
                     /region_name="PDZ3_PDZD7-like"
                     /note="PDZ domain 3 of the canonical isoform 1 of PDZ
                     domain containing 7 (PDZD7), and related domains; cd06751"
                     /db_xref="CDD:467233"
     Site            order(870..876,890,893,923,927,930..931)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467233"
     Region          942..1032
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H5P4.2)"
     CDS             1..1032
                     /gene="PDZD7"
                     /gene_synonym="DFNB57; PDZK7"
                     /coded_by="NM_001437429.1:223..3321"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:79955"
                     /db_xref="HGNC:HGNC:26257"
                     /db_xref="MIM:612971"
ORIGIN      
        1 maqgfavgfd plglgdlssg slsslssrgh lgsdsgstat ryllrkqqrl lngpprgira
       61 sspmgrvili nspieansde sdiihsvrve kspagrlgfs vrggsehglg ifvskveegs
      121 saeraglcvg dkitevngls lesttmgsav kvltsssrlh mmvrrmgrvp gikfskektt
      181 wvdvvnrrlv vekcgstpsd tssedgvrri vhlyttsddf clgfnirggk efglgiyvsk
      241 vdhgglaeen gikvgdqvla angvrfddis hsqavevlkg qthimltike tgrypaykem
      301 vseycwldrl sngvlqqlsp asessssvss cassapyssg slpsdrmdic lgqeepgsrg
      361 pgwgradtam qtepdaggrv etwcsvrptv ilrdtairsd gphpgrrlds alsespktal
      421 llalsrprpp itrsqsyltl weekqqrkke ksgspgekga lqrsktlmnl ffkggrqgrl
      481 ardgrreawt ldsgslakty prldiekggv gpvqkfvtwr lrrdqergra llsarsgsps
      541 sqlpnvdeqv qawesrrpli qdlaqrlltd devlavtrhc sryvheggie dlvrpllail
      601 drpekllllq dirsvvaptd lgrfdsmvml veleafealk sravrppalr parqdtppkr
      661 hlitpvpdsr ggfyllpvng fpeeedngel rerlgalkvs psasaprhph kgipplqdvp
      721 vdaftplria ctpppqlppv aprplrpnwl lteplsrehp pqsqirgraq srsrsrsrsr
      781 srssrgqgks pgrrspspvp tpapsmtngr yhkprkarpp lprpldgeaa kvgakqgpse
      841 sgtegtakea amknpsgelk tvtlskmkqs lgisisggie skvqpmvkie kifpggaafl
      901 sgalqagfel vavdgenleq vthqravdti rrayrnkare pmelvvrvpg psprpspsds
      961 saltdgglpa dhlpahqpld aapvpahwlp epptnpqtpp tdarllqptp spapspalqt
     1021 pdskpapspr ip
//
LOCUS       NP_001397729             568 aa            linear   PRI 21-NOV-2025
DEFINITION  T-cell surface protein tactile isoform 4 [Homo sapiens].
ACCESSION   NP_001397729 XP_006713533
VERSION     NP_001397729.1
DBSOURCE    REFSEQ: accession NM_001410800.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Zhang,Q., Huang,T., Li,X., Liu,G., Xian,L., Mao,X., Lin,T., Fu,C.,
            Chen,X., Liang,W., Zheng,Y., Zhao,Y., Lin,Q., Xu,X., Lin,Y., Bu,J.,
            Wu,C., Zhou,M. and Shen,E.
  TITLE     Prognostic impact of enhanced CD96 expression on NK cells by
            TGF-beta1 in AML
  JOURNAL   Int Immunopharmacol 141, 112958 (2024)
   PUBMED   39159564
  REMARK    GeneRIF: Prognostic impact of enhanced CD96 expression on NK cells
            by TGF-beta1 in AML.
REFERENCE   2  (residues 1 to 568)
  AUTHORS   ElMenshawy,N., El-Chennawi,F., Darwish,A., Foda,A., Atita,D. and
            Eissa,M.
  TITLE     CD44, CD90 and CD96 expression in immune thrombocytopenia purpura
            (ITP) patients
  JOURNAL   J Immunoassay Immunochem 44 (4), 326-337 (2023)
   PUBMED   36949573
  REMARK    GeneRIF: CD44, CD90 and CD96 expression in immune thrombocytopenia
            purpura (ITP) patients.
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Ohtsuki,S., Wang,C., Watanabe,R., Zhang,H., Akiyama,M., Bois,M.C.,
            Maleszewski,J.J., Warrington,K.J., Berry,G.J., Goronzy,J.J. and
            Weyand,C.M.
  TITLE     Deficiency of the CD155-CD96 immune checkpoint controls IL-9
            production in giant cell arteritis
  JOURNAL   Cell Rep Med 4 (4), 101012 (2023)
   PUBMED   37075705
  REMARK    GeneRIF: Deficiency of the CD155-CD96 immune checkpoint controls
            IL-9 production in giant cell arteritis.
REFERENCE   4  (residues 1 to 568)
  AUTHORS   Li,J., Xia,Q., Di,C., Li,C., Si,H., Zhou,B., Yu,S., Li,Y.,
            Huang,J., Lu,Y., Huang,M., Liang,H., Liu,X. and Zhao,Q.
  TITLE     Tumor Cell-Intrinsic CD96 Mediates Chemoresistance and Cancer
            Stemness by Regulating Mitochondrial Fatty Acid beta-Oxidation
  JOURNAL   Adv Sci (Weinh) 10 (7), e2202956 (2023)
   PUBMED   36581470
  REMARK    GeneRIF: Tumor Cell-Intrinsic CD96 Mediates Chemoresistance and
            Cancer Stemness by Regulating Mitochondrial Fatty Acid
            beta-Oxidation.
REFERENCE   5  (residues 1 to 568)
  AUTHORS   Feng,S., Isayev,O., Werner,J. and Bazhin,A.V.
  TITLE     CD96 as a Potential Immune Regulator in Cancers
  JOURNAL   Int J Mol Sci 24 (2), 1303 (2023)
   PUBMED   36674817
  REMARK    GeneRIF: CD96 as a Potential Immune Regulator in Cancers.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 568)
  AUTHORS   Hosen,N., Park,C.Y., Tatsumi,N., Oji,Y., Sugiyama,H., Gramatzki,M.,
            Krensky,A.M. and Weissman,I.L.
  TITLE     CD96 is a leukemic stem cell-specific marker in human acute myeloid
            leukemia
  JOURNAL   Proc Natl Acad Sci U S A 104 (26), 11008-11013 (2007)
   PUBMED   17576927
  REMARK    GeneRIF: CD96 is a cell surface marker present on many acute
            myeloid leukemia leukemic stem cells
REFERENCE   7  (residues 1 to 568)
  AUTHORS   Fuchs,A., Cella,M., Giurisato,E., Shaw,A.S. and Colonna,M.
  TITLE     Cutting edge: CD96 (tactile) promotes NK cell-target cell adhesion
            by interacting with the poliovirus receptor (CD155)
  JOURNAL   J Immunol 172 (7), 3994-3998 (2004)
   PUBMED   15034010
  REMARK    GeneRIF: CD96 promotes natural killer (NK) cell adhesion to target
            cells expressing the poliovirus receptor (PVR), stimulates
            cytotoxicity of activated NK cells, and mediates acquisition of PVR
            from target cells.
REFERENCE   8  (residues 1 to 568)
  AUTHORS   Gramatzki,M., Ludwig,W.D., Burger,R., Moos,P., Rohwer,P.,
            Grunert,C., Sendler,A., Kalden,J.R., Andreesen,R., Henschke,F. and
            Moldenhauer,G.
  TITLE     Antibodies TC-12 ('unique') and TH-111 (CD96) characterize T-cell
            acute lymphoblastic leukemia and a subgroup of acute myeloid
            leukemia
  JOURNAL   Exp Hematol 26 (13), 1209-1214 (1998)
   PUBMED   9845376
REFERENCE   9  (residues 1 to 568)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   10 (residues 1 to 568)
  AUTHORS   Wang,P.L., O'Farrell,S., Clayberger,C. and Krensky,A.M.
  TITLE     Identification and molecular cloning of tactile. A novel human T
            cell activation antigen that is a member of the Ig gene superfamily
  JOURNAL   J Immunol 148 (8), 2600-2608 (1992)
   PUBMED   1313846
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092916.6 and AC055748.21.
            
            On Aug 16, 2022 this sequence version replaced XP_006713533.1.
            
            Summary: The protein encoded by this gene belongs to the
            immunoglobulin superfamily. It is a type I membrane protein. The
            protein may play a role in the adhesive interactions of activated T
            and NK cells during the late phase of the immune response. It may
            also function in antigen presentation. Alternative splicing
            generates multiple transcript variants encoding distinct isoforms.
            [provided by RefSeq, Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2257707.1,
                                           SRR14038197.2441443.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.13-q13.2"
     Protein         1..568
                     /product="T-cell surface protein tactile isoform 4"
                     /note="T-cell surface protein tactile; T cell activation,
                     increased late expression; cell surface antigen CD96; t
                     cell-activated increased late expression protein"
                     /calculated_mol_wt=63718
     Region          27..126
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          41..45
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409383"
     Region          55..59
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409383"
     Region          101..105
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409383"
     Region          115..120
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409383"
     Region          348..>486
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     CDS             1..568
                     /gene="CD96"
                     /gene_synonym="TACTILE"
                     /coded_by="NM_001410800.1:53..1759"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS93339.1"
                     /db_xref="GeneID:10225"
                     /db_xref="HGNC:HGNC:16892"
                     /db_xref="MIM:606037"
ORIGIN      
        1 mekkwkycav yyiiqihfvk gvwektvnte envyatlgsd vnltcqtqtv gffvqmqwsk
       61 vtnkidliav yhpqygfyca ygrpceslvt ftetpengsk wtlhlrnmsc svsgryecml
      121 vlypegiqtk iynlliqthv tadewnsnht ieieinqtle ipcfqnsssk isseftyaws
      181 vedngtqetl isqnhlisns tllkdrvklg tdyrlhlspv qifddgrkfs chirvgpnki
      241 lrssttvkvf akpeipvive nnstdvlver rftcllknvf pkanitwfid gsflhdekeg
      301 iyitneerkg kdgflelksv ltrvhsnkpa qsdnltiwcm alspvpgnkv wnissekitf
      361 llgseisstd pplsvtestl dtqpspassv sparypatss vtlvdvsalr pnttpqpsns
      421 smttrgfnyp wtssgtdtkk fsripsetys sspsgagstl hdnvftstar afsevpttan
      481 gstktnhvhi tgivvnkpkd gmswpvivaa llfccmilfg lgvrkwcqyq keimerpppf
      541 kpppppikyt ciqepnesdl pyhemetl
//
LOCUS       NP_001400299             407 aa            linear   PRI 21-NOV-2025
DEFINITION  telomeric repeat-binding factor 1 isoform 10 [Homo sapiens].
ACCESSION   NP_001400299
VERSION     NP_001400299.1
DBSOURCE    REFSEQ: accession NM_001413370.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Hu,H., van Roon,A.M., Ghanim,G.E., Ahsan,B., Oluwole,A.O.,
            Peak-Chew,S.Y., Robinson,C.V. and Nguyen,T.H.D.
  TITLE     Structural basis of telomeric nucleosome recognition by shelterin
            factor TRF1
  JOURNAL   Sci Adv 9 (34), eadi4148 (2023)
   PUBMED   37624885
  REMARK    GeneRIF: Structural basis of telomeric nucleosome recognition by
            shelterin factor TRF1.
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Harmak,H., Redouane,S., Charoute,H., Aniq Filali,O., Barakat,A. and
            Rouba,H.
  TITLE     In silico exploration and molecular dynamics of deleterious SNPs on
            the human TERF1 protein triggering male infertility
  JOURNAL   J Biomol Struct Dyn 41 (24), 14665-14688 (2023)
   PUBMED   36995171
  REMARK    GeneRIF: In silico exploration and molecular dynamics of
            deleterious SNPs on the human TERF1 protein triggering male
            infertility.
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Abreu,P.L., Lee,Y.W. and Azzalin,C.M.
  TITLE     In Vitro Characterization of the Physical Interactions between the
            Long Noncoding RNA TERRA and the Telomeric Proteins TRF1 and TRF2
  JOURNAL   Int J Mol Sci 23 (18), 10463 (2022)
   PUBMED   36142374
  REMARK    GeneRIF: In Vitro Characterization of the Physical Interactions
            between the Long Noncoding RNA TERRA and the Telomeric Proteins
            TRF1 and TRF2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Jack,A., Kim,Y., Strom,A.R., Lee,D.S.W., Williams,B., Schaub,J.M.,
            Kellogg,E.H., Finkelstein,I.J., Ferro,L.S., Yildiz,A. and
            Brangwynne,C.P.
  TITLE     Compartmentalization of telomeres through DNA-scaffolded phase
            separation
  JOURNAL   Dev Cell 57 (2), 277-290 (2022)
   PUBMED   35077681
  REMARK    GeneRIF: Compartmentalization of telomeres through DNA-scaffolded
            phase separation.
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Broccoli,D., Chong,L., Oelmann,S., Fernald,A.A., Marziliano,N., van
            Steensel,B., Kipling,D., Le Beau,M.M. and de Lange,T.
  TITLE     Comparison of the human and mouse genes encoding the telomeric
            protein, TRF1: chromosomal localization, expression and conserved
            protein domains
  JOURNAL   Hum Mol Genet 6 (1), 69-76 (1997)
   PUBMED   9002672
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Lu,K.P., Hanes,S.D. and Hunter,T.
  TITLE     A human peptidyl-prolyl isomerase essential for regulation of
            mitosis
  JOURNAL   Nature 380 (6574), 544-547 (1996)
   PUBMED   8606777
REFERENCE   8  (residues 1 to 407)
  AUTHORS   Bilaud,T., Koering,C.E., Binet-Brasselet,E., Ancelin,K.,
            Pollice,A., Gasser,S.M. and Gilson,E.
  TITLE     The telobox, a Myb-related telomeric DNA binding motif found in
            proteins from yeast, plants and human
  JOURNAL   Nucleic Acids Res 24 (7), 1294-1303 (1996)
   PUBMED   8614633
REFERENCE   9  (residues 1 to 407)
  AUTHORS   Chong,L., van Steensel,B., Broccoli,D., Erdjument-Bromage,H.,
            Hanish,J., Tempst,P. and de Lange,T.
  TITLE     A human telomeric protein
  JOURNAL   Science 270 (5242), 1663-1667 (1995)
   PUBMED   7502076
REFERENCE   10 (residues 1 to 407)
  AUTHORS   Zhong,Z., Shiue,L., Kaplan,S. and de Lange,T.
  TITLE     A mammalian factor that binds telomeric TTAGGG repeats in vitro
  JOURNAL   Mol Cell Biol 12 (11), 4834-4843 (1992)
   PUBMED   1406665
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022893.6.
            
            Summary: This gene encodes a telomere specific protein which is a
            component of the telomere nucleoprotein complex. This protein is
            present at telomeres throughout the cell cycle and functions as an
            inhibitor of telomerase, acting in cis to limit the elongation of
            individual chromosome ends. The protein structure contains a
            C-terminal Myb motif, a dimerization domain near its N-terminus and
            an acidic N-terminus. Multiple transcripts of this gene are
            alternatively spliced products. [provided by RefSeq, Aug 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1822717.1,
                                           SRR14038195.2127925.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.11"
     Protein         1..407
                     /product="telomeric repeat-binding factor 1 isoform 10"
                     /note="NIMA-interacting protein 2; telomeric protein
                     Pin2/TRF1; TTAGGG repeat-binding factor 1; telomeric
                     repeat binding factor (NIMA-interacting) 1"
                     /calculated_mol_wt=46655
     Region          76..232
                     /region_name="TRFH"
                     /note="Telomeric Repeat binding Factor or TTAGGG Repeat
                     binding Factor, central (dimerization) domain Homology;
                     TRFH. Telomeres are protein/DNA complexes that make up the
                     physical ends of eukaryotic linear chromosomes and are
                     essential for chromosome stability; cl02779"
                     /db_xref="CDD:413471"
     Region          349..397
                     /region_name="SANT_TRF"
                     /note="Telomere repeat binding factor-like DNA-binding
                     domains of the SANT/myb-like family; cd11660"
                     /db_xref="CDD:212558"
     Site            order(349..351,369,371..372,383,385..387,389..391,
                     393..394)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212558"
     CDS             1..407
                     /gene="TERF1"
                     /gene_synonym="hTRF1-AS; PIN2; t-TRF1; TRBF1; TRF; TRF1"
                     /coded_by="NM_001413370.1:24..1247"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:7013"
                     /db_xref="HGNC:HGNC:11728"
                     /db_xref="MIM:600951"
ORIGIN      
        1 maedvssaap sprgcadgrd adpteeqmae terndeeqfe cqellecqvq vgapeeeeee
       61 eedaglvaea eavaagwmld flclslcraf rdgrsedfrr trnsaedaqf enderitple
      121 salmiwgsie kehdklheei qnlikiqaia vcmengnfke aeevferifg dpnshmpfks
      181 kllmiisqkd tfhsffqhfs ynhmmekiks yvnyvlseks stflmkaaak vveskrtrti
      241 tsqdkpsgnd vemeteanld trksvsdkqs avtessegtv sllrshknlf lsklqhgtqq
      301 qdlnkkerrv gtpqstkkkk esrratesri pvsksqpvtp ekhrarkrqa wlweedknlr
      361 sgvrkygegn wskillhykf nnrtsvmlkd rwrtmkklkl issdsed
//
LOCUS       NP_000323                815 aa            linear   PRI 21-NOV-2025
DEFINITION  ataxin-1 isoform ATXN1 [Homo sapiens].
ACCESSION   NP_000323
VERSION     NP_000323.2
DBSOURCE    REFSEQ: accession NM_000332.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 815)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 815)
  AUTHORS   Sheeler,C., Labrada,E., Duvick,L., Thompson,L.M., Zhang,Y.,
            Orr,H.T. and Cvetanovic,M.
  TITLE     Expanded ATXN1 alters transcription and calcium signaling in SCA1
            human motor neurons differentiated from induced pluripotent stem
            cells
  JOURNAL   Neurobiol Dis 201, 106673 (2024)
   PUBMED   39307401
  REMARK    GeneRIF: Expanded ATXN1 alters transcription and calcium signaling
            in SCA1 human motor neurons differentiated from induced pluripotent
            stem cells.
REFERENCE   3  (residues 1 to 815)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 815)
  AUTHORS   Lou,L.Q., Zhou,W.Q., Song,X. and Chen,Z.
  TITLE     Elevation of hsa-miR-7-5p level mediated by CtBP1-p300-AP1 complex
            targets ATXN1 to trigger NF-kappaB-dependent inflammation response
  JOURNAL   J Mol Med (Berl) 101 (3), 223-235 (2023)
   PUBMED   36629882
  REMARK    GeneRIF: Elevation of hsa-miR-7-5p level mediated by CtBP1-p300-AP1
            complex targets ATXN1 to trigger NF-kappaB-dependent inflammation
            response.
REFERENCE   5  (residues 1 to 815)
  AUTHORS   Bergeron,D., Lapointe,C., Bissonnette,C., Tremblay,G., Motard,J.
            and Roucou,X.
  TITLE     An out-of-frame overlapping reading frame in the ataxin-1 coding
            sequence encodes a novel ataxin-1 interacting protein
  JOURNAL   J Biol Chem 288 (30), 21824-21835 (2013)
   PUBMED   23760502
  REMARK    GeneRIF: Data indicate that the alternative ataxin-1 (ATXN1)
            protein is constitutively co-expressed and interacts with ATXN1.
REFERENCE   6  (residues 1 to 815)
  AUTHORS   Servadio,A., Koshy,B., Armstrong,D., Antalffy,B., Orr,H.T. and
            Zoghbi,H.Y.
  TITLE     Expression analysis of the ataxin-1 protein in tissues from normal
            and spinocerebellar ataxia type 1 individuals
  JOURNAL   Nat Genet 10 (1), 94-98 (1995)
   PUBMED   7647801
REFERENCE   7  (residues 1 to 815)
  AUTHORS   Banfi,S., Servadio,A., Chung,M.Y., Kwiatkowski,T.J. Jr.,
            McCall,A.E., Duvick,L.A., Shen,Y., Roth,E.J., Orr,H.T. and
            Zoghbi,H.Y.
  TITLE     Identification and characterization of the gene causing type 1
            spinocerebellar ataxia
  JOURNAL   Nat Genet 7 (4), 513-520 (1994)
   PUBMED   7951322
REFERENCE   8  (residues 1 to 815)
  AUTHORS   Opal,P. and Ashizawa,T.
  TITLE     Spinocerebellar Ataxia Type 1
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301363
REFERENCE   9  (residues 1 to 815)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
REFERENCE   10 (residues 1 to 815)
  AUTHORS   Volz,A., Fonatsch,C. and Ziegler,A.
  TITLE     Regional mapping of the gene for autosomal dominant spinocerebellar
            ataxia (SCA1) by localizing the closely linked D6S89 locus to
            6p24.2----p23.05
  JOURNAL   Cytogenet Cell Genet 60 (1), 37-39 (1992)
   PUBMED   1582256
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL137003.12, AL031120.1,
            AL034375.23 and AL009031.1.
            
            On Aug 20, 2004 this sequence version replaced NP_000323.1.
            
            Summary: The autosomal dominant cerebellar ataxias (ADCA) are a
            heterogeneous group of neurodegenerative disorders characterized by
            progressive degeneration of the cerebellum, brain stem and spinal
            cord. Clinically, ADCA has been divided into three groups: ADCA
            types I-III. ADCAI is genetically heterogeneous, with five genetic
            loci, designated spinocerebellar ataxia (SCA) 1, 2, 3, 4 and 6,
            being assigned to five different chromosomes. ADCAII, which always
            presents with retinal degeneration (SCA7), and ADCAIII often
            referred to as the `pure' cerebellar syndrome (SCA5), are most
            likely homogeneous disorders. Several SCA genes have been cloned
            and shown to contain CAG repeats in their coding regions. ADCA is
            caused by the expansion of the CAG repeats, producing an elongated
            polyglutamine tract in the corresponding protein. The expanded
            repeats are variable in size and unstable, usually increasing in
            size when transmitted to successive generations. The function of
            the ataxins is not known. This locus has been mapped to chromosome
            6, and it has been determined that the diseased allele contains
            40-83 CAG repeats, compared to 6-39 in the normal allele, and is
            associated with spinocerebellar ataxia type 1 (SCA1). Alternative
            splicing results in multiple transcript variants, with one variant
            encoding multiple distinct proteins, ATXN1 and Alt-ATXN1, due to
            the use of overlapping alternate reading frames. [provided by
            RefSeq, Nov 2017].
            
            Transcript Variant: This variant (1) encodes multiple distinct
            proteins due to the use of alternative translation initiation
            codons. The longer 815 aa protein (ATXN1, PMID:23705062) represents
            the canonical protein, while a shorter protein (Alt-ATXN1,
            PMID:23705062) that uses a different reading frame has also been
            described. This RefSeq represents the longer protein, ATXN1.
            Variant 2 also encodes ATXN1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X79204.1, SRR14038197.970143.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..815
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.3"
     Protein         1..815
                     /product="ataxin-1 isoform ATXN1"
                     /note="alternative ataxin1; spinocerebellar ataxia type 1
                     protein"
                     /calculated_mol_wt=86792
     Region          1..558
                     /region_name="ATXN-1_C"
                     /note="Ataxin-1 like family; pfam12547"
                     /db_xref="CDD:463627"
     Region          1..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54253.2)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54254; propagated from
                     UniProtKB/Swiss-Prot (P54253.2)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54253.2)"
     Region          185..270
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54253.2)"
     Region          197..225
                     /region_name="polyglutamine repeat"
                     /note="29 Q/H repeats"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P54253.2)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54254; propagated from
                     UniProtKB/Swiss-Prot (P54253.2)"
     Region          329..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54253.2)"
     Region          397..424
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54253.2)"
     Region          494..604
                     /region_name="Self-association.
                     /evidence=ECO:0000269|PubMed:9097953"
                     /note="propagated from UniProtKB/Swiss-Prot (P54253.2)"
     Region          538..815
                     /region_name="Interaction with USP7.
                     /evidence=ECO:0000269|PubMed:12093161"
                     /note="propagated from UniProtKB/Swiss-Prot (P54253.2)"
     Region          540..766
                     /region_name="RNA-binding.
                     /evidence=ECO:0000269|PubMed:11136710"
                     /note="propagated from UniProtKB/Swiss-Prot (P54253.2)"
     Region          573..688
                     /region_name="AXH"
                     /note="domain in Ataxins and HMG containing proteins;
                     smart00536"
                     /db_xref="CDD:197779"
     Region          762..798
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54253.2)"
     Site            775
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12741986; propagated from
                     UniProtKB/Swiss-Prot (P54253.2)"
     Region          794..797
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:P54254"
                     /note="propagated from UniProtKB/Swiss-Prot (P54253.2)"
     CDS             1..815
                     /gene="ATXN1"
                     /gene_synonym="ATX1; D6S504E; SCA1"
                     /coded_by="NM_000332.4:942..3389"
                     /note="isoform ATXN1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34342.1"
                     /db_xref="GeneID:6310"
                     /db_xref="HGNC:HGNC:10548"
                     /db_xref="MIM:601556"
ORIGIN      
        1 mksnqersne clppkkreip atsrsseeka ptlpsdnhrv egtawlpgnp ggrghgggrh
       61 gpagtsvelg lqqgiglhka lstgldyspp saprsvpvat tlpaayatpq pgtpvspvqy
      121 ahlphtfqfi gssqysgtya sfipsqlipp tanpvtsava saagattpsq rsqleaystl
      181 lanmgslsqt pghkaeqqqq qqqqqqqqhq hqqqqqqqqq qqqqqhlsra pglitpgspp
      241 paqqnqyvhi ssspqntgrt asppaipvhl hphqtmipht ltlgppsqvv mqyadsgshf
      301 vpreatkkae ssrlqqaiqa kevlngemek srrygapssa dlglgkaggk svphpyesrh
      361 vvvhpspsdy ssrdpsgvra svmvlpnsnt paadlevqqa threaspstl ndksglhlgk
      421 pghrsyalsp htviqtthsa seplpvglpa tafyagtqpp vigylsgqqq aityagslpq
      481 hlvipgtqpl lipvgstdme asgaapaivt sspqfaavph tfvttalpks enfnpealvt
      541 qaaypamvqa qihlpvvqsv aspaaapptl ppyfmkgsii qlangelkkv edlktedfiq
      601 saeisndlki dsstveried shspgvaviq favgehraqv svevlveypf fvfgqgwssc
      661 cpertsqlfd lpcsklsvgd vcisltlknl kngsvkkgqp vdpasvllkh skadglagsr
      721 hryaeqengi nqgsaqmlse ngelkfpekm glpaapfltk iepskpaatr krrwsapesr
      781 kleksedepp ltlpkpslip qevkiciegr snvgk
//
LOCUS       NP_001394194             354 aa            linear   PRI 21-NOV-2025
DEFINITION  cellular tumor antigen p53 isoform g [Homo sapiens].
ACCESSION   NP_001394194
VERSION     NP_001394194.1
DBSOURCE    REFSEQ: accession NM_001407265.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Mirgayazova,R., Khadiullina,R., Chasov,V., Mingaleeva,R.,
            Miftakhova,R., Rizvanov,A. and Bulatov,E.
  TITLE     Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an Option?
  JOURNAL   Genes (Basel) 11 (6), 704 (2020)
   PUBMED   32630614
  REMARK    GeneRIF: Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an
            Option?
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Flynt,E., Bisht,K., Sridharan,V., Ortiz,M., Towfic,F. and
            Thakurta,A.
  TITLE     Prognosis, Biology, and Targeting of TP53 Dysregulation in Multiple
            Myeloma
  JOURNAL   Cells 9 (2), 287 (2020)
   PUBMED   31991614
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Barnoud,T., Parris,J.L.D. and Murphy,M.E.
  TITLE     Common genetic variants in the TP53 pathway and their impact on
            cancer
  JOURNAL   J Mol Cell Biol 11 (7), 578-585 (2019)
   PUBMED   31152665
  REMARK    GeneRIF: Common genetic variants in the TP53 pathway and their
            impact on cancer.
            Review article
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Hu,W., Chen,S., Thorne,R.F. and Wu,M.
  TITLE     TP53, TP53 Target Genes (DRAM, TIGAR), and Autophagy
  JOURNAL   Adv Exp Med Biol 1206, 127-149 (2019)
   PUBMED   31776983
  REMARK    Review article
REFERENCE   5  (residues 1 to 354)
  AUTHORS   Baugh,E.H., Ke,H., Levine,A.J., Bonneau,R.A. and Chan,C.S.
  TITLE     Why are there hotspot mutations in the TP53 gene in human cancers?
  JOURNAL   Cell Death Differ 25 (1), 154-160 (2018)
   PUBMED   29099487
  REMARK    GeneRIF: TP53 missense mutant alleles that occur in human cancers
            are discussed in the context of high resolution models of these p53
            mutant protein structures to determine the structural features of
            mutations (review).
            Review article
REFERENCE   6  (residues 1 to 354)
  AUTHORS   Aubrey,B.J., Strasser,A. and Kelly,G.L.
  TITLE     Tumor-Suppressor Functions of the TP53 Pathway
  JOURNAL   Cold Spring Harb Perspect Med 6 (5), a026062 (2016)
   PUBMED   27141080
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 354)
  AUTHORS   Soussi,T. and Wiman,K.G.
  TITLE     TP53: an oncogene in disguise
  JOURNAL   Cell Death Differ 22 (8), 1239-1249 (2015)
   PUBMED   26024390
  REMARK    Review article
REFERENCE   8  (residues 1 to 354)
  AUTHORS   Soussi,T.
  TITLE     The TP53 gene network in a postgenomic era
  JOURNAL   Hum Mutat 35 (6), 641-642 (2014)
   PUBMED   24753184
  REMARK    GeneRIF: Recommendations and guidelines for reporting and
            annotating TP53 variants are also provided, to help researchers
            generate standardized data that are easy to understand, analyze,
            and exchange across various cancer variant databases
            Review article
REFERENCE   9  (residues 1 to 354)
  AUTHORS   Anczukow,O., Ware,M.D., Buisson,M., Zetoune,A.B.,
            Stoppa-Lyonnet,D., Sinilnikova,O.M. and Mazoyer,S.
  TITLE     Does the nonsense-mediated mRNA decay mechanism prevent the
            synthesis of truncated BRCA1, CHK2, and p53 proteins?
  JOURNAL   Hum Mutat 29 (1), 65-73 (2008)
   PUBMED   17694537
  REMARK    GeneRIF: the p53 protein encoded by the 770delT allele is as
            abundant as the wild-type protein, as removal of the C-terminal p53
            domain leads to a stabilized mutant protein, whose abundance is
            markedly increased when NMD is inhibited.
REFERENCE   10 (residues 1 to 354)
  AUTHORS   Bourdon,J.C.
  TITLE     p53 Family isoforms
  JOURNAL   Curr Pharm Biotechnol 8 (6), 332-336 (2007)
   PUBMED   18289041
  REMARK    Review article
REFERENCE   11 (residues 1 to 354)
  AUTHORS   Candeias,M.M., Powell,D.J., Roubalova,E., Apcher,S., Bourougaa,K.,
            Vojtesek,B., Bruzzoni-Giovanelli,H. and Fahraeus,R.
  TITLE     Expression of p53 and p53/47 are controlled by alternative
            mechanisms of messenger RNA translation initiation
  JOURNAL   Oncogene 25 (52), 6936-6947 (2006)
   PUBMED   16983332
  REMARK    GeneRIF: harbouring alternative translation initiation sites, the
            p53 mRNA gives rise to different levels of the p53 isoforms which
            help to orchestrate the cell biological outcome of p53 activation
REFERENCE   12 (residues 1 to 354)
  AUTHORS   Murray-Zmijewski,F., Lane,D.P. and Bourdon,J.C.
  TITLE     p53/p63/p73 isoforms: an orchestra of isoforms to harmonise cell
            differentiation and response to stress
  JOURNAL   Cell Death Differ 13 (6), 962-972 (2006)
   PUBMED   16601753
  REMARK    Review article
REFERENCE   13 (residues 1 to 354)
  AUTHORS   Bourdon,J.C., Fernandes,K., Murray-Zmijewski,F., Liu,G., Diot,A.,
            Xirodimas,D.P., Saville,M.K. and Lane,D.P.
  TITLE     p53 isoforms can regulate p53 transcriptional activity
  JOURNAL   Genes Dev 19 (18), 2122-2137 (2005)
   PUBMED   16131611
  REMARK    GeneRIF: p53 isoforms can regulate p53 transcriptional activity.
REFERENCE   14 (residues 1 to 354)
  AUTHORS   Ghosh,A., Stewart,D. and Matlashewski,G.
  TITLE     Regulation of human p53 activity and cell localization by
            alternative splicing
  JOURNAL   Mol Cell Biol 24 (18), 7987-7997 (2004)
   PUBMED   15340061
  REMARK    GeneRIF: mechanism of p53 regulation originating through
            alternative splicing of the human p53 gene resulting in the
            expression of a novel p53 mRNA
REFERENCE   15 (residues 1 to 354)
  AUTHORS   Flaman,J.M., Waridel,F., Estreicher,A., Vannier,A., Limacher,J.M.,
            Gilbert,D., Iggo,R. and Frebourg,T.
  TITLE     The human tumour suppressor gene p53 is alternatively spliced in
            normal cells
  JOURNAL   Oncogene 12 (4), 813-818 (1996)
   PUBMED   8632903
REFERENCE   16 (residues 1 to 354)
  AUTHORS   Schneider,K., Zelley,K., Nichols,K.E., Schwartz Levine,A. and
            Garber,J.
  TITLE     Li-Fraumeni Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301488
REFERENCE   17 (residues 1 to 354)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   18 (residues 1 to 354)
  AUTHORS   Lamb,P. and Crawford,L.
  TITLE     Characterization of the human p53 gene
  JOURNAL   Mol Cell Biol 6 (5), 1379-1385 (1986)
   PUBMED   2946935
REFERENCE   19 (residues 1 to 354)
  AUTHORS   Isobe,M., Emanuel,B.S., Givol,D., Oren,M. and Croce,C.M.
  TITLE     Localization of gene for human p53 tumour antigen to band 17p13
  JOURNAL   Nature 320 (6057), 84-85 (1986)
   PUBMED   3456488
REFERENCE   20 (residues 1 to 354)
  AUTHORS   Benchimol,S., Lamb,P., Crawford,L.V., Sheer,D., Shows,T.B.,
            Bruns,G.A. and Peacock,J.
  TITLE     Transformation associated p53 protein is encoded by a gene on human
            chromosome 17
  JOURNAL   Somat Cell Mol Genet 11 (5), 505-510 (1985)
   PUBMED   2994241
REFERENCE   21 (residues 1 to 354)
  AUTHORS   Harlow,E., Williamson,N.M., Ralston,R., Helfman,D.M. and Adams,T.E.
  TITLE     Molecular cloning and in vitro expression of a cDNA clone for human
            cellular tumor antigen p53
  JOURNAL   Mol Cell Biol 5 (7), 1601-1610 (1985)
   PUBMED   3894933
REFERENCE   22 (residues 1 to 354)
  AUTHORS   Zakut-Houri,R., Bienz-Tadmor,B., Givol,D. and Oren,M.
  TITLE     Human p53 cellular tumor antigen: cDNA sequence and expression in
            COS cells
  JOURNAL   EMBO J 4 (5), 1251-1255 (1985)
   PUBMED   4006916
REFERENCE   23 (residues 1 to 354)
  AUTHORS   Matlashewski,G., Lamb,P., Pim,D., Peacock,J., Crawford,L. and
            Benchimol,S.
  TITLE     Isolation and characterization of a human p53 cDNA clone:
            expression of the human p53 gene
  JOURNAL   EMBO J 3 (13), 3257-3262 (1984)
   PUBMED   6396087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087388.9 and AC007421.13.
            
            Summary: This gene encodes a tumor suppressor protein containing
            transcriptional activation, DNA binding, and oligomerization
            domains. The encoded protein responds to diverse cellular stresses
            to regulate expression of target genes, thereby inducing cell cycle
            arrest, apoptosis, senescence, DNA repair, or changes in
            metabolism. Mutations in this gene are associated with a variety of
            human cancers, including hereditary cancers such as Li-Fraumeni
            syndrome. Alternative splicing of this gene and the use of
            alternate promoters result in multiple transcript variants and
            isoforms. Additional isoforms have also been shown to result from
            the use of alternate translation initiation codons from identical
            transcript variants (PMIDs: 12032546, 20937277). [provided by
            RefSeq, Dec 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2206180.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:2946935)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..354
                     /product="cellular tumor antigen p53 isoform g"
                     /note="tumor protein 53; mutant tumor protein 53; cellular
                     tumor antigen p53; phosphoprotein p53;
                     transformation-related protein 53; antigen NY-CO-13; tumor
                     supressor p53"
                     /calculated_mol_wt=39189
     Region          1..20
                     /region_name="TAD2"
                     /note="Transactivation domain 2; pfam18521"
                     /db_xref="CDD:375947"
     Region          70..249
                     /region_name="P53"
                     /note="P53 DNA-binding domain; cd08367"
                     /db_xref="CDD:176262"
     Site            order(137,140,199,203)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:176262"
     Site            order(138..140,142)
                     /site_type="other"
                     /note="dimerization site [polypeptide binding]"
                     /db_xref="CDD:176262"
     Site            order(200,202,209,234,236..238,241)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176262"
     Region          280..319
                     /region_name="P53_tetramer"
                     /note="P53 tetramerization motif; pfam07710"
                     /db_xref="CDD:462238"
     CDS             1..354
                     /gene="TP53"
                     /gene_synonym="BCC7; BMFS5; LFS1; P53; TRP53"
                     /coded_by="NM_001407265.1:270..1334"
                     /note="isoform g is encoded by transcript variant 10"
                     /db_xref="GeneID:7157"
                     /db_xref="HGNC:HGNC:11998"
                     /db_xref="MIM:191170"
ORIGIN      
        1 mddlmlspdd ieqwftedpg pdeaprmpea appvapapaa ptpaapapap swplsssvps
       61 qktyqgsygf rlgflhsgta ksvtctyspa lnkmfcqlak tcpvqlwvds tpppgtrvra
      121 maiykqsqhm tevvrrcphh ercsdsdgla ppqhlirveg nlrveylddr ntfrhsvvvp
      181 yeppevgsdc ttihynymcn sscmggmnrr piltiitled ssgnllgrns fevrvcacpg
      241 rdrrteeenl rkkgephhel ppgstkralp nntssspqpk kkpldgeyft lqirgrerfe
      301 mfrelneale lkdaqagkep ggsrahsshl kskkgqstsr hkklmfkteg pdsd
//
LOCUS       NP_758859               2405 aa            linear   PRI 21-NOV-2025
DEFINITION  histone-lysine N-methyltransferase, H3 lysine-36 specific isoform a
            [Homo sapiens].
ACCESSION   NP_758859
VERSION     NP_758859.2
DBSOURCE    REFSEQ: accession NM_172349.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2405)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2405)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   3  (residues 1 to 2405)
  AUTHORS   Conteduca,G., Cangelosi,D., Baldo,C., Arado,A., Testa,B.,
            Wagner,R.T., Robertson,K.D., Dequiedt,F., Fitzsimmons,L.,
            Malacarne,M., Filaci,G. and Coviello,D.A.
  TITLE     Impact of NSD1 Alternative Transcripts in Actin Filament Formation
            and Cellular Division Pathways in Fibroblasts
  JOURNAL   Genes (Basel) 15 (9), 1117 (2024)
   PUBMED   39336709
  REMARK    GeneRIF: Impact of NSD1 Alternative Transcripts in Actin Filament
            Formation and Cellular Division Pathways in Fibroblasts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2405)
  AUTHORS   Ren,Z., Yue,L., Hu,H.Y., Hou,X.L., Chen,W.Q., Tan,Y., Dong,Z. and
            Zhang,J.
  TITLE     Identification of Novel NSD1 variations in four Pediatric cases
            with sotos Syndrome
  JOURNAL   BMC Med Genomics 17 (1), 116 (2024)
   PUBMED   38684994
  REMARK    GeneRIF: Identification of Novel NSD1 variations in four Pediatric
            cases with sotos Syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2405)
  AUTHORS   Wang,X., Yeh,S., Wu,G., Hsu,C.L., Wang,L., Chiang,T., Yang,Y.,
            Guo,Y. and Chang,C.
  TITLE     Identification and characterization of a novel androgen receptor
            coregulator ARA267-alpha in prostate cancer cells
  JOURNAL   J Biol Chem 276 (44), 40417-40423 (2001)
   PUBMED   11509567
REFERENCE   6  (residues 1 to 2405)
  AUTHORS   Jaju,R.J., Fidler,C., Haas,O.A., Strickson,A.J., Watkins,F.,
            Clark,K., Cross,N.C., Cheng,J.F., Aplan,P.D., Kearney,L.,
            Boultwood,J. and Wainscoat,J.S.
  TITLE     A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in
            de novo childhood acute myeloid leukemia
  JOURNAL   Blood 98 (4), 1264-1267 (2001)
   PUBMED   11493482
REFERENCE   7  (residues 1 to 2405)
  AUTHORS   Lee,D.K., Duan,H.O. and Chang,C.
  TITLE     Androgen receptor interacts with the positive elongation factor
            P-TEFb and enhances the efficiency of transcriptional elongation
  JOURNAL   J Biol Chem 276 (13), 9978-9984 (2001)
   PUBMED   11266437
REFERENCE   8  (residues 1 to 2405)
  AUTHORS   Huang,N., vom Baur,E., Garnier,J.M., Lerouge,T., Vonesch,J.L.,
            Lutz,Y., Chambon,P. and Losson,R.
  TITLE     Two distinct nuclear receptor interaction domains in NSD1, a novel
            SET protein that exhibits characteristics of both corepressors and
            coactivators
  JOURNAL   EMBO J 17 (12), 3398-3412 (1998)
   PUBMED   9628876
REFERENCE   9  (residues 1 to 2405)
  AUTHORS   Ocansey,S., Cole,T.R.P., Rahman,N. and Tatton-Brown,K.
  TITLE     Sotos Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301652
REFERENCE   10 (residues 1 to 2405)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027314.5, AC008570.6 and
            AC146507.2.
            
            On Jul 13, 2022 this sequence version replaced NP_758859.1.
            
            Summary: This gene encodes a protein containing a SET domain, 2
            LXXLL motifs, 3 nuclear translocation signals (NLSs), 4 plant
            homeodomain (PHD) finger regions, and a proline-rich region. The
            encoded protein enhances androgen receptor (AR) transactivation,
            and this enhancement can be increased further in the presence of
            other androgen receptor associated coregulators. This protein may
            act as a nucleus-localized, basic transcriptional factor and also
            as a bifunctional transcriptional regulator. Mutations of this gene
            have been associated with Sotos syndrome and Weaver syndrome. One
            version of childhood acute myeloid leukemia is the result of a
            cryptic translocation with the breakpoints occurring within nuclear
            receptor-binding Su-var, enhancer of zeste, and trithorax domain
            protein 1 on chromosome 5 and nucleoporin, 98-kd on chromosome 11.
            Multiple transcript variants encoding distinct isoforms have been
            identified for this gene. [provided by RefSeq, Sep 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2116158.1,
                                           SRR18074967.3004126.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2405
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..2405
                     /product="histone-lysine N-methyltransferase, H3 lysine-36
                     specific isoform a"
                     /EC_number="2.1.1.357"
                     /note="androgen receptor-associated coregulator 267;
                     histone-lysine N-methyltransferase, H3 lysine-36 and H4
                     lysine-20 specific; H3-K36-HMTase; H4-K20-HMTase; lysine
                     N-methyltransferase 3B; NR-binding SET domain-containing
                     protein; androgen receptor coactivator 267 kDa protein;
                     androgen receptor-associated protein of 267 kDa; nuclear
                     receptor-binding SET domain-containing protein 1; nuclear
                     receptor SET domain-containing protein 1; histone-lysine
                     N-methyltransferase, H3 lysine-36 specific"
                     /calculated_mol_wt=264921
     Region          27..142
                     /region_name="PWWP_NSD1_rpt1"
                     /note="first PWWP domain found in nuclear receptor-binding
                     SET domain-containing protein 1 (NSD1) and similar
                     proteins; cd20161"
                     /db_xref="CDD:438989"
     Site            order(43,46,77)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438989"
     Site            44..47
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438989"
     Site            order(115..117,120..121)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438989"
     Region          <1140..1296
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          1254..1296
                     /region_name="PHD1_NSD1_2"
                     /note="PHD finger 1 found in nuclear receptor-binding SET
                     domain-containing protein NSD1 and NSD2; cd15648"
                     /db_xref="CDD:277118"
     Site            order(1254,1263..1267,1272,1290)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277118"
     Region          1301..1347
                     /region_name="PHD2_NSD1"
                     /note="PHD finger 2 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15650"
                     /db_xref="CDD:277120"
     Site            order(1301,1311..1315,1321,1342)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277120"
     Region          1348..1401
                     /region_name="PHD3_NSD1"
                     /note="PHD finger 3 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15653"
                     /db_xref="CDD:277123"
     Site            order(1348,1366..1370,1374,1396)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277123"
     Region          1418..1457
                     /region_name="PHD4_NSD1"
                     /note="PHD finger 4 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15656"
                     /db_xref="CDD:277126"
     Site            order(1418,1427..1431,1435,1452)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277126"
     Region          1464..1559
                     /region_name="PWWP_NSD1_rpt2"
                     /note="second PWWP domain found in nuclear
                     receptor-binding SET domain-containing protein 1 (NSD1)
                     and similar proteins; cd20164"
                     /db_xref="CDD:438992"
     Site            order(1476,1479,1507)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438992"
     Site            1477..1480
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438992"
     Region          1610..1648
                     /region_name="AWS"
                     /note="AWS domain; pfam17907"
                     /db_xref="CDD:465559"
     Region          1650..1791
                     /region_name="SET_NSD1"
                     /note="SET domain (including post-SET domain) found in
                     nuclear receptor-binding SET domain-containing protein 1
                     (NSD1) and similar proteins; cd19210"
                     /db_xref="CDD:380987"
     Site            order(1661..1663,1680,1690,1694,1703..1709,1726..1730,
                     1737..1739,1754,1765..1775,1777..1781,1790)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380987"
     Site            order(1661..1663,1703..1706,1726..1730,1767,1774,
                     1778..1781,1790)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380987"
     Site            order(1680,1690,1694,1705..1709,1737..1739,1754,
                     1765..1769)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:380987"
     Site            order(1732,1779,1781,1786)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380987"
     Region          1829..1871
                     /region_name="PHD5_NSD1"
                     /note="PHD finger 5 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15659"
                     /db_xref="CDD:277129"
     Site            order(1829,1838..1842,1848,1866)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277129"
     Region          1870..1919
                     /region_name="C5HCH"
                     /note="NSD Cys-His rich domain; pfam17982"
                     /db_xref="CDD:465605"
     Region          <1917..2283
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..2405
                     /gene="NSD1"
                     /gene_synonym="ARA267; KMT3B; SOTOS; SOTOS1; STO"
                     /coded_by="NM_172349.5:291..7508"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4413.1"
                     /db_xref="GeneID:64324"
                     /db_xref="HGNC:HGNC:14234"
                     /db_xref="MIM:606681"
ORIGIN      
        1 mlelpgtsss stsqelpfcq pkkkstplky evgdliwakf krrpwwpcri csdplinths
       61 kmkvsnrrpy rqyyveafgd pserawvagk aivmfegrhq feelpvlrrr gkqkekgyrh
      121 kvpqkilskw easvglaeqy dvpkgsknrk cipgsiklds eedmpfedct ndpesehdll
      181 lngclkslaf dsehsadeke kpcaksrark ssdnpkrtsv kkghiqfeah kderrgkipe
      241 nlglnfisgd isdtqasnel sriansltgs ntapgsflfs scgkntakke fetsngdsll
      301 glpegalisk csreknkpqr slvcgskvkl cyigagdeek rsdsisictt sddgssdldp
      361 iehssesdns vleipdafdr tenmlsmqkn ekikysrfaa tntrvkakqk plisnshtdh
      421 lmgctksaep gtetsqvnls dlkastlvhk pqsdftndal spkfnlsssi ssenslikgg
      481 aanqallhsk skqpkfrsik ckhkenpvma eppvineecs lkccssdtkg splasisksg
      541 kvdglkllnn mhektrdssd ietavvkhvl selkelsyrs lgedvsdsgt skpskpllfs
      601 sassqnhipi epdykfstll mmlkdmhdsk tkeqrlmtaq nlvsyrspgr gdcstnspvg
      661 vskvlvsggs thnsekkgdg tqnsanpsps ggdsalsgel saslpgllsd krdlpasgks
      721 rsdcvtrrnc grskpssklr dafsaqmvkn tvnrkalkte rkrklnqlps vtldavlqgd
      781 rerggslrgg aedpskedpl qimghltsed gdhfsdvhfd skvkqsdpgk isekglsfen
      841 gkgpeldsvm nsendelngv nqvvpkkrwq rlnqrrtkpr krmnrfkeke nsecafrvll
      901 psdpvqegrd efpehrtpsa sileeplteq nhadcldsag prlnvcdkss asigdmekep
      961 gipsltpqae lpepavrsek krlrkpskwl leyteeydqi fapkkkqkkv qeqvhkvssr
     1021 ceeesllarg rssaqnkqvd enslistkee ppvlereapf legplaqsel ggghaelpql
     1081 tlsvpvapev sprpalesee llvktpgnye skrqrkptkk llesndldpg fmpkkgdlgl
     1141 skkcyeaghl engitescat syskdfgggt tkifdkprkr krqrhaaakm qckkvkndds
     1201 skeipgsege lmphrtatsp ketveegveh dpgmpaskkm qgergggaal kenvcqncek
     1261 lgelllceaq ccgafhlecl gltemprgkf icnecrtgih tcfvckqsge dvkrcllplc
     1321 gkfyheecvq kypptvmqnk gfrcslhici tchaanpanv saskgrlmrc vrcpvayhan
     1381 dfclaagski lasnsiicpn hftprrgcrn hehvnvswcf vcseggsllc cdscpaafhr
     1441 eclnidipeg nwycndckag kkphyreivw vkvgryrwwp aeichpravp snidkmrhdv
     1501 gefpvlffgs ndylwthqar vfpymegdvs skdkmgkgvd gtykkalqea aarfeelkaq
     1561 kelrqlqedr kndkkpppyk hikvnrpigr vqiftadlse iprcnckatd enpcgidsec
     1621 inrmllyech ptvcpaggrc qnqcfskrqy peveifrtlq rgwglrtktd ikkgefvney
     1681 vgelideeec rariryaqeh ditnfymltl dkdriidagp kgnyarfmnh ccqpncetqk
     1741 wsvngdtrvg lfalsdikag teltfnynle clgngktvck cgapncsgfl gvrpknqpia
     1801 teekskkfkk kqqgkrrtqg eitkeredec fscgdagqlv sckkpgcpkv yhadclnltk
     1861 rpagkwecpw hqcdicgkea asfcemcpss fckqhregml fiskldgrls ctehdpcgpn
     1921 plepgeirey vpppvplppg psthlaeqst gmaaqapkms dkppadtnqm lslskkalag
     1981 tcqrpllper plertdsrpq pldkvrdlag sgtksqslvs sqrpldrppa vagprpqlsd
     2041 kpspvtspss spsvrsqple rplgtadprl dksigaaspr pqslektsvp tglrlpppdr
     2101 llitsspkpq tsdrptdkph aslsqrlppp ekvlsavvqt lvakekalrp vdqntqsknr
     2161 aalvmdlidl tprqkeraas phqvtpqade kmpvlesssw paskglghmp ravekgcvsd
     2221 plqtsgkaaa psedpwqavk sltqarllsq ppakaflyep ttqasgrasa gaeqtpgpls
     2281 qspglvkqak qmvggqqlpa laaksgqsfr slgkapaslp teekklvtte qspwalgkas
     2341 sraglwpiva gqtlaqscws agstqtlaqt cwslgrgqdp kpeqntlpal nqapsshkca
     2401 eseqk
//
LOCUS       NP_001428220             747 aa            linear   PRI 21-NOV-2025
DEFINITION  dynamin-binding protein isoform f [Homo sapiens].
ACCESSION   NP_001428220
VERSION     NP_001428220.1
DBSOURCE    REFSEQ: accession NM_001441291.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 747)
  AUTHORS   Ouyang,C., Mu,J., Lu,Q., Li,J., Zhu,H., Wang,Q., Zou,M.H. and
            Xie,Z.
  TITLE     Autophagic degradation of KAT2A/GCN5 promotes directional migration
            of vascular smooth muscle cells by reducing TUBA/alpha-tubulin
            acetylation
  JOURNAL   Autophagy 16 (10), 1753-1770 (2020)
   PUBMED   31878840
  REMARK    GeneRIF: Autophagic degradation of KAT2A/GCN5 promotes directional
            migration of vascular smooth muscle cells by reducing
            TUBA/alpha-tubulin acetylation.
REFERENCE   5  (residues 1 to 747)
  AUTHORS   Ansar,M., Chung,H.L., Taylor,R.L., Nazir,A., Imtiaz,S.,
            Sarwar,M.T., Manousopoulou,A., Makrythanasis,P., Saeed,S.,
            Falconnet,E., Guipponi,M., Pournaras,C.J., Ansari,M.A., Ranza,E.,
            Santoni,F.A., Ahmed,J., Shah,I., Gul,K., Black,G.C., Bellen,H.J.
            and Antonarakis,S.E.
  TITLE     Bi-allelic Loss-of-Function Variants in DNMBP Cause Infantile
            Cataracts
  JOURNAL   Am J Hum Genet 103 (4), 568-578 (2018)
   PUBMED   30290152
  REMARK    GeneRIF: DNMBP loss-of-function variants cause infantile-onset
            cataracts in humans.
REFERENCE   6  (residues 1 to 747)
  AUTHORS   Minster,R.L., DeKosky,S.T. and Kamboh,M.I.
  TITLE     No association of dynamin binding protein (DNMBP) gene SNPs and
            Alzheimer's disease
  JOURNAL   Neurobiol Aging 29 (10), 1602-1604 (2008)
   PUBMED   17442457
  REMARK    GeneRIF: We observed no association of statistical significance in
            either the total sample or the APOE*4 non-carriers for any of the
            SNPs of Dynamin Binding Protein.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 747)
  AUTHORS   Otani,T., Ichii,T., Aono,S. and Takeichi,M.
  TITLE     Cdc42 GEF Tuba regulates the junctional configuration of simple
            epithelial cells
  JOURNAL   J Cell Biol 175 (1), 135-146 (2006)
   PUBMED   17015620
  REMARK    GeneRIF: Tuba controls the shaping of cell junctions through the
            local activation of Cdc42 and its effectors.
REFERENCE   8  (residues 1 to 747)
  AUTHORS   Kuwano,R., Miyashita,A., Arai,H., Asada,T., Imagawa,M., Shoji,M.,
            Higuchi,S., Urakami,K., Kakita,A., Takahashi,H., Tsukie,T.,
            Toyabe,S., Akazawa,K., Kanazawa,I. and Ihara,Y.
  CONSRTM   Japanese Genetic Study Consortium for Alzeheimer's Disease
  TITLE     Dynamin-binding protein gene on chromosome 10q is associated with
            late-onset Alzheimer's disease
  JOURNAL   Hum Mol Genet 15 (13), 2170-2182 (2006)
   PUBMED   16740596
  REMARK    GeneRIF: Results confirmed DNMBP may be one of the susceptibility
            genes for Alzheimer's disease.
            GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   9  (residues 1 to 747)
  AUTHORS   Cestra,G., Kwiatkowski,A., Salazar,M., Gertler,F. and De Camilli,P.
  TITLE     Tuba, a GEF for CDC42, links dynamin to actin regulatory proteins
  JOURNAL   Methods Enzymol 404, 537-545 (2005)
   PUBMED   16413298
REFERENCE   10 (residues 1 to 747)
  AUTHORS   Salazar,M.A., Kwiatkowski,A.V., Pellegrini,L., Cestra,G.,
            Butler,M.H., Rossman,K.L., Serna,D.M., Sondek,J., Gertler,F.B. and
            De Camilli,P.
  TITLE     Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl
            homology domains, links dynamin to regulation of the actin
            cytoskeleton
  JOURNAL   J Biol Chem 278 (49), 49031-49043 (2003)
   PUBMED   14506234
  REMARK    GeneRIF: functions to bring together dynamin with actin regulatory
            proteins
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL627434.4 and AL392107.17.
            
            Summary: This gene encodes a protein belonging to the guanine
            nucleotide exchange factor family, and which regulates the
            configuration of cell junctions. It contains multiple binding sites
            for dynamin and thus links dynamin to actin regulatory proteins.
            Polymorphisms in this gene have been linked to Alzheimer's disease
            in some populations, though there are conflicting reports of such
            linkages in other populations. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3328321.1,
                                           SRR14038192.1713612.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.2"
     Protein         1..747
                     /product="dynamin-binding protein isoform f"
                     /note="scaffold protein TUBA"
                     /calculated_mol_wt=84785
     Region          <9..135
                     /region_name="RhoGEF"
                     /note="RhoGEF domain; pfam00621"
                     /db_xref="CDD:459876"
     Region          187..378
                     /region_name="BAR_DNMBP"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin
                     Binding Protein; cd07589"
                     /db_xref="CDD:153273"
     Site            order(199,202..203,207,209..210,213..214,216..217,
                     231..232,234..235,238..239,241..242,245,251,254..255,339,
                     342..343,345,350,353..354,356..357,360..361,364..365,
                     367..368,371..372,374..375)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153273"
     Region          459..515
                     /region_name="SH3_DNMBP_C1"
                     /note="First C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11798"
                     /db_xref="CDD:212732"
     Site            order(464,466,469,473,495..496,509,511..512)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212732"
     Region          687..743
                     /region_name="SH3_DNMBP_C2"
                     /note="Second C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba, and similar domains;
                     cd12141"
                     /db_xref="CDD:213017"
     Site            order(692,694,697,701,723..724,737,739..740)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213017"
     CDS             1..747
                     /gene="DNMBP"
                     /gene_synonym="ARHGEF36; CTRCT48; TUBA"
                     /coded_by="NM_001441291.1:646..2889"
                     /note="isoform f is encoded by transcript variant 7"
                     /db_xref="GeneID:23268"
                     /db_xref="HGNC:HGNC:30373"
                     /db_xref="MIM:611282"
ORIGIN      
        1 mqmvikvskq llaaleisda vgpvflghrd elegtykiyc qnhdeaiall eiyekdekiq
       61 khlqdsladl kslynewgct nyinlgsfli kpvqrvmryp lllmellnst peshpdkvpl
      121 tnavlavkei nvnineykrr kdlvlkyrkg dedslmekis klnihsiikk snrvsshlkh
      181 ltgfapqikd evfeeteknf rmqerliksf irdlslylqh iresacvkvv aavsmwdvcm
      241 erghrdleqf ervhryisdq lftnfkerte rlvisplnql lsmftgphkl vqkrfdklld
      301 fyncteraek lkdkktleel qsarnnyeal naqlldelpk fhqyaqglft ncvhgyaeah
      361 cdfvhqaleq lkpllsllkv agregnliai fheehsrvlq qlqvftffpe slpatkkpfe
      421 rktidrqsar kpllglpsym lqseelrasl laryppeklf qaernfnaaq dldvsllegd
      481 lvgvikkkdp mgsqnrwlid ngvtkgfvys sflkpynprr shsdasvgsh sstesehgss
      541 sprfprqnsg stltfnpssm avsftsgscq kqpqdasppp kecdqgtlsa slnpsnsess
      601 psrcpsdpds tsqprsgdsa dvardvkqpt atprsyrnfr hpeivgysvp grngqsqdlv
      661 kgcartaqap edrstepdgs eaegnqvyfa vytfkarnpn elsvsanqkl kilefkdvtg
      721 ntewwlaevn gkkgyvpsny irkteyt
//
LOCUS       NP_851397                735 aa            linear   PRI 21-NOV-2025
DEFINITION  hypoxia-inducible factor 1-alpha isoform 2 [Homo sapiens].
ACCESSION   NP_851397
VERSION     NP_851397.1
DBSOURCE    REFSEQ: accession NM_181054.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 735)
  AUTHORS   Nie,L., Huang,L., Zhu,Q., Yao,Q., Wu,Y., Zhao,L., Yu,L. and Fu,F.
  TITLE     HIF-1alpha Activates Hypoxia-Induced MXRA5 Expression in the
            Progression of Ovarian Cancer
  JOURNAL   J Environ Pathol Toxicol Oncol 44 (1), 47-55 (2025)
   PUBMED   39462449
  REMARK    GeneRIF: HIF-1alpha Activates Hypoxia-Induced MXRA5 Expression in
            the Progression of Ovarian Cancer.
REFERENCE   3  (residues 1 to 735)
  AUTHORS   VON Fournier,A., Wilhelm,C., Tirtey,C., Stoth,M., Kasemo,T.E.,
            Hackenberg,S. and Scherzad,A.
  TITLE     Impact of Hypoxia and the Levels of Transcription Factor HIF-1alpha
            and JMJD1A on Epithelial-Mesenchymal Transition in Head and Neck
            Squamous Cell Carcinoma Cell Lines
  JOURNAL   Cancer Genomics Proteomics 21 (6), 591-607 (2024)
   PUBMED   39467631
  REMARK    GeneRIF: Impact of Hypoxia and the Levels of Transcription Factor
            HIF-1alpha and JMJD1A on Epithelial-Mesenchymal Transition in Head
            and Neck Squamous Cell Carcinoma Cell Lines.
REFERENCE   4  (residues 1 to 735)
  AUTHORS   Kling,L., Eulenberg-Gustavus,C., Jerke,U., Rousselle,A.,
            Eckardt,K.U., Schreiber,A. and Kettritz,R.
  TITLE     beta2-integrins control HIF1alpha activation in human neutrophils
  JOURNAL   Front Immunol 15, 1406967 (2024)
   PUBMED   39469705
  REMARK    GeneRIF: beta2-integrins control HIF1alpha activation in human
            neutrophils.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 735)
  AUTHORS   Zarychta,J., Kowalczyk,A., Slowik,K., Przywara,D., Petniak,A.,
            Kondracka,A., Wojtowicz-Marzec,M., Slyk-Gulewska,P.,
            Kwasniewska,A., Kocki,J. and Gil-Kulik,P.
  TITLE     Pilot Study on the Effect of Patient Condition and Clinical
            Parameters on Hypoxia-Induced Factor Expression: HIF1A, EPAS1 and
            HIF3A in Human Colostrum Cells
  JOURNAL   Int J Mol Sci 25 (20), 11042 (2024)
   PUBMED   39456823
  REMARK    GeneRIF: Pilot Study on the Effect of Patient Condition and
            Clinical Parameters on Hypoxia-Induced Factor Expression: HIF1A,
            EPAS1 and HIF3A in Human Colostrum Cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 735)
  AUTHORS   Wang,G.L., Jiang,B.H., Rue,E.A. and Semenza,G.L.
  TITLE     Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS
            heterodimer regulated by cellular O2 tension
  JOURNAL   Proc Natl Acad Sci U S A 92 (12), 5510-5514 (1995)
   PUBMED   7539918
REFERENCE   7  (residues 1 to 735)
  AUTHORS   Wang,G.L. and Semenza,G.L.
  TITLE     Purification and characterization of hypoxia-inducible factor 1
  JOURNAL   J Biol Chem 270 (3), 1230-1237 (1995)
   PUBMED   7836384
REFERENCE   8  (residues 1 to 735)
  AUTHORS   Semenza,G.L., Roth,P.H., Fang,H.M. and Wang,G.L.
  TITLE     Transcriptional regulation of genes encoding glycolytic enzymes by
            hypoxia-inducible factor 1
  JOURNAL   J Biol Chem 269 (38), 23757-23763 (1994)
   PUBMED   8089148
REFERENCE   9  (residues 1 to 735)
  AUTHORS   Wang,G.L. and Semenza,G.L.
  TITLE     General involvement of hypoxia-inducible factor 1 in
            transcriptional response to hypoxia
  JOURNAL   Proc Natl Acad Sci U S A 90 (9), 4304-4308 (1993)
   PUBMED   8387214
REFERENCE   10 (residues 1 to 735)
  AUTHORS   Semenza,G.L. and Wang,G.L.
  TITLE     A nuclear factor induced by hypoxia via de novo protein synthesis
            binds to the human erythropoietin gene enhancer at a site required
            for transcriptional activation
  JOURNAL   Mol Cell Biol 12 (12), 5447-5454 (1992)
   PUBMED   1448077
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC344032.1, AB073325.1,
            CN264295.1 and BC012527.2.
            
            Summary: This gene encodes the alpha subunit of transcription
            factor hypoxia-inducible factor-1 (HIF-1), which is a heterodimer
            composed of an alpha and a beta subunit. HIF-1 functions as a
            master regulator of cellular and systemic homeostatic response to
            hypoxia by activating transcription of many genes, including those
            involved in energy metabolism, angiogenesis, apoptosis, and other
            genes whose protein products increase oxygen delivery or facilitate
            metabolic adaptation to hypoxia. HIF-1 thus plays an essential role
            in embryonic vascularization, tumor angiogenesis and
            pathophysiology of ischemic disease. Alternatively spliced
            transcript variants encoding different isoforms have been
            identified for this gene. [provided by RefSeq, Jul 2011].
            
            Transcript Variant: This variant (2) lacks the penultimate coding
            exon compared to variant 1. This results in a frame-shift, and a
            shorter isoform (2) with a distinct C-terminus compared to isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.250908.1,
                                           SRR1660807.224891.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..735
                     /product="hypoxia-inducible factor 1-alpha isoform 2"
                     /note="ARNT interacting protein; hypoxia inducible factor
                     1, alpha subunit (basic helix-loop-helix transcription
                     factor); member of PAS superfamily 1; hypoxia-inducible
                     factor 1-alpha; member of PAS protein 1; PAS
                     domain-containing protein 8; hypoxia inducible factor 1
                     alpha subunit; basic-helix-loop-helix-PAS protein MOP1;
                     class E basic helix-loop-helix protein 78;
                     hypoxia-inducible factor1alpha"
                     /calculated_mol_wt=82616
     Region          1..401
                     /region_name="Interaction with TSGA10.
                     /evidence=ECO:0000250|UniProtKB:Q61221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Region          13..83
                     /region_name="bHLH-PAS_HIF1a_PASD8"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in hypoxia-inducible factor 1-alpha (HIF1a)
                     and similar proteins; cd19727"
                     /db_xref="CDD:381570"
     Site            order(18..19,21..23,26..27,29..30,55..56)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381570"
     Site            18
                     /site_type="glycosylation"
                     /note="(Microbial infection) N-beta-linked (GlcNAc)
                     arginine. /evidence=ECO:0000269|PubMed:30125331;
                     propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Region          21..30
                     /region_name="DNA-binding.
                     /evidence=ECO:0000250|UniProtKB:Q61221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Site            order(32..33,35..36,39..40,43..44,55..57,60..61,64,67..68,
                     71)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381570"
     Region          93..148
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Region          170..191
                     /region_name="Required for heterodimer formation with
                     ARNT. /evidence=ECO:0000250|UniProtKB:Q61221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:20699359; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Region          254..339
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(255,259,265,278..281,307,312)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(275,279,287,290..291,319,321)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          380..417
                     /region_name="N-terminal VHL recognition site"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Region          401..603
                     /region_name="ODD. /evidence=ECO:0000303|PubMed:16288748"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Site            402
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:11566883; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Region          494..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Region          531..575
                     /region_name="NTAD. /evidence=ECO:0000303|PubMed:10202154,
                     ECO:0000303|PubMed:9235919"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Site            532
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:24681946; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Region          551..581
                     /region_name="HIF-1"
                     /note="Hypoxia-inducible factor-1; pfam11413"
                     /db_xref="CDD:463274"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta.
                     /evidence=ECO:0000269|PubMed:20889502; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Site            555
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by GSK3-beta.
                     /evidence=ECO:0000269|PubMed:20889502; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Region          556..572
                     /region_name="C-terminal VHL recognition site"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Site            564
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:11292861,
                     ECO:0000269|PubMed:11566883, ECO:0000269|PubMed:12351678,
                     ECO:0000269|PubMed:25974097; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000269|PubMed:20889502; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Site            589
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta.
                     /evidence=ECO:0000269|PubMed:20889502; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Region          642..688
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000269|PubMed:20889502; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Site            709
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:24681946; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Region          718..721
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     CDS             1..735
                     /gene="HIF1A"
                     /gene_synonym="bHLHe78; HIF-1-alpha; HIF-1A; HIF-1alpha;
                     HIF1; HIF1-ALPHA; MOP1; PASD8"
                     /coded_by="NM_181054.3:293..2500"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9754.1"
                     /db_xref="GeneID:3091"
                     /db_xref="HGNC:HGNC:4910"
                     /db_xref="MIM:603348"
ORIGIN      
        1 megaggandk kkisserrke ksrdaarsrr skesevfyel ahqlplphnv sshldkasvm
       61 rltisylrvr klldagdldi eddmkaqmnc fylkaldgfv mvltddgdmi yisdnvnkym
      121 gltqfeltgh svfdfthpcd heemremlth rnglvkkgke qntqrsfflr mkctltsrgr
      181 tmniksatwk vlhctghihv ydtnsnqpqc gykkppmtcl vlicepiphp snieipldsk
      241 tflsrhsldm kfsycderit elmgyepeel lgrsiyeyyh aldsdhltkt hhdmftkgqv
      301 ttgqyrmlak rggyvwvetq atviyntkns qpqcivcvny vvsgiiqhdl ifslqqtecv
      361 lkpvessdmk mtqlftkves edtsslfdkl kkepdaltll apaagdtiis ldfgsndtet
      421 ddqqleevpl yndvmlpspn eklqninlam splptaetpk plrssadpal nqevalklep
      481 npeslelsft mpqiqdqtps psdgstrqss pepnspseyc fyvdsdmvne fklelveklf
      541 aedteaknpf stqdtdldle mlapyipmdd dfqlrsfdql splesssasp esaspqstvt
      601 vfqqtqiqep tanattttat tdelktvtkd rmedikilia spspthihke ttsatsspyr
      661 dtqsrtaspn ragkgvieqt ekshprspnv lsvalsqrtt vpeeelnpki lalqnaqrkr
      721 kmehdgslfq avgii
//
LOCUS       NP_001400012             328 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001400012
VERSION     NP_001400012.1
DBSOURCE    REFSEQ: accession NM_001413083.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2645328.1,
                                           SRR14038193.2470908.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..328
                     /product="mitochondrial fission regulator 1 isoform 4
                     precursor"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=30859
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=5550
     Region          22..251
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15390.2)"
     Region          177..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          179..304
                     /region_name="Necessary and sufficient to promote
                     mitochondrial fission. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     CDS             1..328
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001413083.1:132..1118"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 18"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsvlwsrkpy gssrsivrki gtnlsliqcp rvqfqinsha
       61 tewspshpge davasfadvg wvakeegecs arlrtevrsr pplqddllff ekapsrqisl
      121 pdlsqeepql ktpalaneea lqkicalene laalraqiak ivtqqeqqnl tagdldsttf
      181 gtipphpppp ppplpppalg lhqstsavdl ikerrekran agktlvknnp kkpempnmle
      241 ilkemnsvkl rsvkrseqdv kpkpvdatdp aaliaealkk kfayryrsds qdevekgipk
      301 seseatserv lslpagfiqp hvskhclg
//
LOCUS       NP_001427332             902 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_001427332 XP_011541086 XP_054224543
VERSION     NP_001427332.1
DBSOURCE    REFSEQ: accession NM_001440403.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 902)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 902)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 902)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 902)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 902)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 902)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 902)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 902)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 902)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 902)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3, AP004147.3 and
            AP001929.5.
            
            On or before May 20, 2025 this sequence version replaced
            XP_011541086.1, XP_054224543.1.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK014580.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..902
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     3 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=98969
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..348
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Region          361..731
                     /region_name="PBP2_iGluR_kainate_KA1"
                     /note="The ligand-binding domain of the kainate subtype
                     KA1 of ionotropic glutamate receptors, a member of the
                     type 2 periplasmic-binding fold protein superfamily;
                     cd13724"
                     /db_xref="CDD:270442"
     Site            order(363,370,377,408..409,414..415)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:270442"
     Site            order(419,446..448,453)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270442"
     CDS             1..902
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440403.1:299..3007"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk aaelgmvsay
      241 ytyiftnlls sallfdavya vvtavqelnr sqeigvkpls cgsaqiwqhg tslmnylrmv
      301 elegltghie fnskgqrsny alkilqftrn gfrqigqwhv aeglsmdshl yasnisdtlf
      361 nttlvvttil enpylmlkgn hqemegndry egfcvdmlke laeilrfnyk irlvgdgvyg
      421 vpeangtwtg mvgeliarka dlavagltit aerekvidfs kpfmtlgisi lyrvhmgrkp
      481 gyfsfldpfs pgvwlfmlla ylavscvlfl varltpyewy sphpcaqgrc nllvnqyslg
      541 nslwfpvggf mqqgstiapr alstrcvsgv wwaftliiis sytanlaafl tvqrmdvpie
      601 svddladqta ieygtihggs smtffqnsry qtyqrmwnym yskqpsvfvk steegiarvl
      661 nsnyaflles tmneyyrqrn cnltqiggll dtkgygigmp vgsvfrdefd lailqlqenn
      721 rleilkrkww eggkcpkeed hrakglgmen iggifvvlic glivaifmam leflwtlrhs
      781 eatevsvcqe mvtelrsiil cqdsihprrr raavppprpp ipeerrprgt atlsngklcg
      841 agepdqlaqr laqeaalvar gcthirvcpe crrfqglrar psparseesl ewekttnsse
      901 pe
//
LOCUS       NP_001401393             237 aa            linear   PRI 21-NOV-2025
DEFINITION  bax inhibitor 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001401393 XP_024304941
VERSION     NP_001401393.1
DBSOURCE    REFSEQ: accession NM_001414464.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Zhang,X., Chen,Q., He,Y., Shi,Q., Yin,C., Xie,Y., Yu,H., Bao,Y.,
            Wang,X., Tang,C. and Dong,Z.
  TITLE     STRIP2 motivates non-small cell lung cancer progression by
            modulating the TMBIM6 stability through IGF2BP3 dependent
  JOURNAL   J Exp Clin Cancer Res 42 (1), 19 (2023)
   PUBMED   36639675
  REMARK    GeneRIF: STRIP2 motivates non-small cell lung cancer progression by
            modulating the TMBIM6 stability through IGF2BP3 dependent.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Liao,Y., Qiu,Z. and Bai,L.
  TITLE     miR-302d-3p regulates the viability, migration and apoptosis of
            breast cancer cells through regulating the TMBIM6-mediated ERK
            signaling pathway
  JOURNAL   Mol Med Rep 24 (6) (2021)
   PUBMED   34651659
  REMARK    GeneRIF: miR302d3p regulates the viability, migration and apoptosis
            of breast cancer cells through regulating the TMBIM6mediated ERK
            signaling pathway.
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Bhattarai,K.R., Kim,H.K., Chaudhary,M., Ur Rashid,M.M., Kim,J.,
            Kim,H.R. and Chae,H.J.
  TITLE     TMBIM6 regulates redox-associated posttranslational modifications
            of IRE1alpha and ER stress response failure in aging mice and
            humans
  JOURNAL   Redox Biol 47, 102128 (2021)
   PUBMED   34562874
  REMARK    GeneRIF: TMBIM6 regulates redox-associated posttranslational
            modifications of IRE1alpha and ER stress response failure in aging
            mice and humans.
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 237)
  AUTHORS   Grzmil,M., Thelen,P., Hemmerlein,B., Schweyer,S., Voigt,S., Mury,D.
            and Burfeind,P.
  TITLE     Bax inhibitor-1 is overexpressed in prostate cancer and its
            specific down-regulation by RNA interference leads to cell death in
            human prostate carcinoma cells
  JOURNAL   Am J Pathol 163 (2), 543-552 (2003)
   PUBMED   12875974
  REMARK    GeneRIF: Results indicate that the human Bax inhibitor-1 gene may
            serve as a prostate cancer expression marker based on its
            overexpression in prostate carcinoma and prostate cancer cell
            lines.
REFERENCE   7  (residues 1 to 237)
  AUTHORS   Jean,J.C., Oakes,S.M. and Joyce-Brady,M.
  TITLE     The Bax inhibitor-1 gene is differentially regulated in adult
            testis and developing lung by two alternative TATA-less promoters
  JOURNAL   Genomics 57 (2), 201-208 (1999)
   PUBMED   10198159
REFERENCE   8  (residues 1 to 237)
  AUTHORS   Cowling,R.T. and Birnboim,H.C.
  TITLE     Preliminary characterization of the protein encoded by human
            testis-enhanced gene transcript (TEGT)
  JOURNAL   Mol Membr Biol 15 (4), 177-187 (1998)
   PUBMED   10087504
REFERENCE   9  (residues 1 to 237)
  AUTHORS   Xu,Q. and Reed,J.C.
  TITLE     Bax inhibitor-1, a mammalian apoptosis suppressor identified by
            functional screening in yeast
  JOURNAL   Mol Cell 1 (3), 337-346 (1998)
   PUBMED   9660918
REFERENCE   10 (residues 1 to 237)
  AUTHORS   Walter,L., Marynen,P., Szpirer,J., Levan,G. and Gunther,E.
  TITLE     Identification of a novel conserved human gene, TEGT
  JOURNAL   Genomics 28 (2), 301-304 (1995)
   PUBMED   8530040
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC084037.35 and AC131157.4.
            
            On Feb 21, 2023 this sequence version replaced XP_024304941.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2480422.1,
                                           SRR14038192.1888115.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..237
                     /product="bax inhibitor 1 isoform 1"
                     /note="BAX inhibitor 1; testis-enhanced gene transcript
                     protein; transmembrane BAX inhibitor motif-containing
                     protein 6; testis enhanced gene transcript"
                     /calculated_mol_wt=26407
     Region          16..228
                     /region_name="BI-1"
                     /note="BAX inhibitor (BI)-1; cd10430"
                     /db_xref="CDD:198412"
     Site            30..50
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            53..73
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            87..107
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            140..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            167..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     CDS             1..237
                     /gene="TMBIM6"
                     /gene_synonym="BAXI1; BI-1; TEGT"
                     /coded_by="NM_001414464.1:243..956"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="GeneID:7009"
                     /db_xref="HGNC:HGNC:11723"
                     /db_xref="MIM:600748"
ORIGIN      
        1 mnifdrkinf dallkfshit pstqqhlkkv yasfalcmfv aaagayvhmv thfiqaglls
       61 algslilmiw lmatphshet eqkrlgllag fafltgvglg palefciavn psilptafmg
      121 tamiftcftl salyarrrsy lflggilmsa lsllllsslg nvffgsiwlf qanlyvglvv
      181 mcgfvlfdtq liiekaehgd qdyiwhcidl fldfitvfrk lmmilamnek dkkkekk
//
LOCUS       NP_001400013             328 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001400013
VERSION     NP_001400013.1
DBSOURCE    REFSEQ: accession NM_001413084.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.41944.1,
                                           SRR14372080.490629.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..328
                     /product="mitochondrial fission regulator 1 isoform 4
                     precursor"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=30859
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=5550
     Region          22..251
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15390.2)"
     Region          177..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          179..304
                     /region_name="Necessary and sufficient to promote
                     mitochondrial fission. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     CDS             1..328
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001413084.1:132..1118"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 19"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsvlwsrkpy gssrsivrki gtnlsliqcp rvqfqinsha
       61 tewspshpge davasfadvg wvakeegecs arlrtevrsr pplqddllff ekapsrqisl
      121 pdlsqeepql ktpalaneea lqkicalene laalraqiak ivtqqeqqnl tagdldsttf
      181 gtipphpppp ppplpppalg lhqstsavdl ikerrekran agktlvknnp kkpempnmle
      241 ilkemnsvkl rsvkrseqdv kpkpvdatdp aaliaealkk kfayryrsds qdevekgipk
      301 seseatserv lslpagfiqp hvskhclg
//
LOCUS       NP_001427529             372 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform o [Homo sapiens].
ACCESSION   NP_001427529
VERSION     NP_001427529.1
DBSOURCE    REFSEQ: accession NM_001440600.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 372)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14478891.972388.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..372
                     /product="polycomb protein EED isoform o"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=42279
     Region          117..157
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          119..367
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          162..199
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          209..271
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          278..326
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          334..360
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..372
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001440600.1:478..1596"
                     /note="isoform o is encoded by transcript variant 15"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdendd avsiesgtnt erpdtptntp
       61 napgrkswgk gkwkskkcky sfkcvnslkv tlyechsqge irllqsyvda dadenfytca
      121 wtydsntshp llavagsrgi iriinpitmq cikhyvghgn ainelkfhpr dpnlllsvsk
      181 dhalrlwniq tdtlvaifgg veghrdevls adydllgeki mscgmdhslk lwrinskrmm
      241 naikesydyn pnktnrpfis qkihfpdfst rdihrnyvdc vrwlgdlils kscenaivcw
      301 kpgkmeddid kikpsesnvt ilgrfdysqc diwymrfsmd fwqkmlalgn qvgklyvwdl
      361 evedphkanr dh
//
LOCUS       NP_001424260             922 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, NMDA 1 isoform 7 precursor [Homo
            sapiens].
ACCESSION   NP_001424260 XP_005266129 XP_054218783
VERSION     NP_001424260.1
DBSOURCE    REFSEQ: accession NM_001437331.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Korinek,M., Candelas Serra,M., Abdel Rahman,F., Dobrovolski,M.,
            Kuchtiak,V., Abramova,V., Fili,K., Tomovic,E., Hrcka Krausova,B.,
            Krusek,J., Cerny,J., Vyklicky,L., Balik,A. and Smejkalova,T.
  TITLE     Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B genes:
            Insights into NMDA Receptor Structure, Function, and
            Pathophysiology
  JOURNAL   Physiol Res 73 (Suppl 1), S413-S434 (2024)
   PUBMED   38836461
  REMARK    GeneRIF: Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B
            genes: Insights into NMDA Receptor Structure, Function, and
            Pathophysiology.
            Review article
REFERENCE   2  (residues 1 to 922)
  AUTHORS   Michalski,K. and Furukawa,H.
  TITLE     Structure and function of GluN1-3A NMDA receptor excitatory glycine
            receptor channel
  JOURNAL   Sci Adv 10 (15), eadl5952 (2024)
   PUBMED   38598639
REFERENCE   3  (residues 1 to 922)
  AUTHORS   Xu,Y., Song,R., Perszyk,R.E., Chen,W., Kim,S., Park,K.L.,
            Allen,J.P., Nocilla,K.A., Zhang,J., XiangWei,W., Tankovic,A.,
            McDaniels,E.D., Sheikh,R., Mizu,R.K., Karamchandani,M.M., Hu,C.,
            Kusumoto,H., Pecha,J., Cappuccio,G., Gaitanis,J., Sullivan,J.,
            Shashi,V., Petrovski,S., Jauss,R.T., Lee,H.K., Bozarth,X.,
            Lynch,D.R., Helbig,I., Pierson,T.M., Boerkoel,C.F., Myers,S.J.,
            Lemke,J.R., Benke,T.A., Yuan,H. and Traynelis,S.F.
  TITLE     De novo GRIN variants in M3 helix associated with neurological
            disorders control channel gating of NMDA receptor
  JOURNAL   Cell Mol Life Sci 81 (1), 153 (2024)
   PUBMED   38538865
  REMARK    GeneRIF: De novo GRIN variants in M3 helix associated with
            neurological disorders control channel gating of NMDA receptor.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 922)
  AUTHORS   Ragnarsson,L., Zhang,Z., Das,S.S., Tran,P., Andersson,A., des
            Portes,V., Desmettre Altuzarra,C., Remerand,G., Labalme,A.,
            Chatron,N., Sanlaville,D., Lesca,G., Anggono,V., Vetter,I. and
            Keramidas,A.
  TITLE     GRIN1 variants associated with neurodevelopmental disorders reveal
            channel gating pathomechanisms
  JOURNAL   Epilepsia 64 (12), 3377-3388 (2023)
   PUBMED   37734923
  REMARK    GeneRIF: GRIN1 variants associated with neurodevelopmental
            disorders reveal channel gating pathomechanisms.
REFERENCE   5  (residues 1 to 922)
  AUTHORS   McNearney,T.A. and Westlund,K.N.
  TITLE     Pluripotential GluN1 (NMDA NR1): Functional Significance in
            Cellular Nuclei in Pain/Nociception
  JOURNAL   Int J Mol Sci 24 (17), 13196 (2023)
   PUBMED   37686003
  REMARK    GeneRIF: Pluripotential GluN1 (NMDA NR1): Functional Significance
            in Cellular Nuclei in Pain/Nociception.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 922)
  AUTHORS   Zimmer,M., Fink,T.M., Franke,Y., Lichter,P. and Spiess,J.
  TITLE     Cloning and structure of the gene encoding the human
            N-methyl-D-aspartate receptor (NMDAR1)
  JOURNAL   Gene 159 (2), 219-223 (1995)
   PUBMED   7622053
REFERENCE   7  (residues 1 to 922)
  AUTHORS   Younkin,D.P., Tang,C.M., Hardy,M., Reddy,U.R., Shi,Q.Y.,
            Pleasure,S.J., Lee,V.M. and Pleasure,D.
  TITLE     Inducible expression of neuronal glutamate receptor channels in the
            NT2 human cell line
  JOURNAL   Proc Natl Acad Sci U S A 90 (6), 2174-2178 (1993)
   PUBMED   7681588
REFERENCE   8  (residues 1 to 922)
  AUTHORS   Karp,S.J., Masu,M., Eki,T., Ozawa,K. and Nakanishi,S.
  TITLE     Molecular cloning and chromosomal localization of the key subunit
            of the human N-methyl-D-aspartate receptor
  JOURNAL   J Biol Chem 268 (5), 3728-3733 (1993)
   PUBMED   7679115
REFERENCE   9  (residues 1 to 922)
  AUTHORS   Platzer,K. and Lemke,J.R.
  TITLE     GRIN1-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31219694
REFERENCE   10 (residues 1 to 922)
  AUTHORS   Monyer,H., Sprengel,R., Schoepfer,R., Herb,A., Higuchi,M.,
            Lomeli,H., Burnashev,N., Sakmann,B. and Seeburg,P.H.
  TITLE     Heteromeric NMDA receptors: molecular and functional distinction of
            subtypes
  JOURNAL   Science 256 (5060), 1217-1221 (1992)
   PUBMED   1350383
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL929554.20.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_005266129.1, XP_054218783.1.
            
            Summary: The protein encoded by this gene is a critical subunit of
            N-methyl-D-aspartate receptors, members of the glutamate receptor
            channel superfamily which are heteromeric protein complexes with
            multiple subunits arranged to form a ligand-gated ion channel.
            These subunits play a key role in the plasticity of synapses, which
            is believed to underlie memory and learning. Cell-specific factors
            are thought to control expression of different isoforms, possibly
            contributing to the functional diversity of the subunits.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2145743,
                              SAMEA2154665 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..922
                     /product="glutamate receptor ionotropic, NMDA 1 isoform 7
                     precursor"
                     /note="N-methyl-D-aspartate receptor channel, subunit
                     zeta-1; glutamate [NMDA] receptor subunit zeta-1;
                     N-methyl-D-aspartate receptor subunit NR1; glutamate
                     receptor ionotropic, NMDA 1; glutamate receptor,
                     ionotropic, N-methyl D-aspartate 1; putative
                     NMDtranscript(altAcc_e2)"
                     /calculated_mol_wt=101579
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2185
     Region          25..404
                     /region_name="PBP1_iGluR_NMDA_NR1"
                     /note="N-terminal leucine-isoleucine-valine-binding
                     protein (LIVBP)-like domain of the NR1, an essential
                     channel-forming subunit of the NMDA receptor; cd06379"
                     /db_xref="CDD:380602"
     Site            order(69..72,76,79,113,340,344,363)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:380602"
     Site            order(69..73,75..76,79..80,113..114,131,135,329..331,
                     340..341,343..344)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:380602"
     Region          416..820
                     /region_name="PBP2_iGluR_NMDA_Nr1"
                     /note="The ligand-binding domain of the NR1 subunit of
                     ionotropic NMDA (N-methyl-D-aspartate) glutamate
                     receptors, a member of the type 2 periplasmic binding fold
                     protein superfamily; cd13719"
                     /db_xref="CDD:270437"
     Site            order(537..540,542,544..546,689,708..709,713,753,774..776,
                     779,785,801..804,807)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270437"
     Site            order(537..539,544,708..710,752..753)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270437"
     Region          856..884
                     /region_name="CaM_bdg_C0"
                     /note="Calmodulin-binding domain C0 of NMDA receptor NR1
                     subunit; pfam10562"
                     /db_xref="CDD:402271"
     CDS             1..922
                     /gene="GRIN1"
                     /gene_synonym="DEE101; GluN1; hNR1; MRD8; NDHMSD; NDHMSR;
                     NMD-R1; NMDA1; NMDAR1; NR1"
                     /coded_by="NM_001437331.1:334..3102"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:2902"
                     /db_xref="HGNC:HGNC:4584"
                     /db_xref="MIM:138249"
ORIGIN      
        1 mstmrlltla llfscsvara acdpkivnig avlstrkheq mfreavnqan krhgswkiql
       61 natsvthkpn aiqmalsvce dlissqvyai lvshpptpnd hftptpvsyt agfyripvlg
      121 lttrmsiysd ksihlsflrt vppyshqssv wfemmrvysw nhiillvsdd hegraaqkrl
      181 etlleeresk skkrnyenld qlsydnkrgp kaekvlqfdp gtknvtallm eakelearvi
      241 ilsaseddaa tvyraaamln mtgsgyvwlv gereisgnal ryapdgilgl qlingknesa
      301 hisdavgvva qavhelleke nitdpprgcv gntniwktgp lfkrvlmssk yadgvtgrve
      361 fnedgdrkfa nysimnlqnr klvqvgiyng thvipndrki iwpggetekp rgyqmstrlk
      421 ivtihqepfv yvkptlsdgt ckeeftvngd pvkkvictgp ndtspgsprh tvpqccygfc
      481 idlliklart mnftyevhlv adgkfgtqer vnnsnkkewn gmmgellsgq admivaplti
      541 nneraqyief skpfkyqglt ilvkkeiprs tldsfmqpfq stlwllvgls vhvvavmlyl
      601 ldrfspfgrf kvnseeeeed altlssamwf swgvllnsgi gegaprsfsa rilgmvwagf
      661 amiivasyta nlaaflvldr peeritgind prlrnpsdkf iyatvkqssv diyfrrqvel
      721 stmyrhmekh nyesaaeaiq avrdnklhaf iwdsavlefe asqkcdlvtt gelffrsgfg
      781 igmrkdspwk qnvslsilks hengfmedld ktwvryqecd srsnapatlt fenmagvfml
      841 vaggivagif lifieiaykr hkdarrkqmq lafaavnvwr knlqstgggr galqnqkdtv
      901 lprraieree gqlqlcsrhr es
//
LOCUS       NP_001424220            1053 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            beta isoform isoform 3 [Homo sapiens].
ACCESSION   NP_001424220 XP_047304269 XP_054202832
VERSION     NP_001424220.1
DBSOURCE    REFSEQ: accession NM_001437291.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Liu,L., Feng,X., Fan,C., Kong,D., Feng,X., Sun,C., Xu,Y., Li,B.,
            Jiang,Y. and Zheng,C.
  TITLE     PDCD4 interacting with PIK3CB and CTSZ promotes the apoptosis of
            multiple myeloma cells
  JOURNAL   FASEB J 38 (16), e70024 (2024)
   PUBMED   39190024
  REMARK    GeneRIF: PDCD4 interacting with PIK3CB and CTSZ promotes the
            apoptosis of multiple myeloma cells.
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Liu,G., Hou,Y., Jin,X., Zhang,Y., Sun,C., Huang,C., Ren,Y., Gao,J.,
            Wang,X. and Jiang,X.
  TITLE     PI3K/HSCB axis facilitates FOG1 nuclear translocation to promote
            erythropoiesis and megakaryopoiesis
  JOURNAL   Elife 13, 95815 (2024)
   PUBMED   38757931
  REMARK    GeneRIF: PI3K/HSCB axis facilitates FOG1 nuclear translocation to
            promote erythropoiesis and megakaryopoiesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1053)
  AUTHORS   Duewell,B.R., Wilson,N.E., Bailey,G.M., Peabody,S.E. and
            Hansen,S.D.
  TITLE     Molecular dissection of PI3Kbeta synergistic activation by receptor
            tyrosine kinases, GbetaGgamma, and Rho-family GTPases
  JOURNAL   Elife 12, 88991 (2024)
   PUBMED   38713746
  REMARK    GeneRIF: Molecular dissection of PI3Kbeta synergistic activation by
            receptor tyrosine kinases, GbetaGgamma, and Rho-family GTPases.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1053)
  AUTHORS   Xu,W., Chen,Y., Zhang,Z., Jiang,Y. and Wang,Z.
  TITLE     Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma
  JOURNAL   Med Oncol 40 (8), 221 (2023)
   PUBMED   37402056
  REMARK    GeneRIF: Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1053)
  AUTHORS   Milani,D., Mazzoni,M., Borgatti,P., Zauli,G., Cantley,L. and
            Capitani,S.
  TITLE     Extracellular human immunodeficiency virus type-1 Tat protein
            activates phosphatidylinositol 3-kinase in PC12 neuronal cells
  JOURNAL   J Biol Chem 271 (38), 22961-22964 (1996)
   PUBMED   8798481
REFERENCE   7  (residues 1 to 1053)
  AUTHORS   Bonnefoy-Berard,N., Liu,Y.C., von Willebrand,M., Sung,A., Elly,C.,
            Mustelin,T., Yoshida,H., Ishizaka,K. and Altman,A.
  TITLE     Inhibition of phosphatidylinositol 3-kinase activity by association
            with 14-3-3 proteins in T cells
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10142-10146 (1995)
   PUBMED   7479742
REFERENCE   8  (residues 1 to 1053)
  AUTHORS   Hu,P. and Schlessinger,J.
  TITLE     Direct association of p110 beta phosphatidylinositol 3-kinase with
            p85 is mediated by an N-terminal fragment of p110 beta
  JOURNAL   Mol Cell Biol 14 (4), 2577-2583 (1994)
   PUBMED   8139559
REFERENCE   9  (residues 1 to 1053)
  AUTHORS   Hu,P., Mondino,A., Skolnik,E.Y. and Schlessinger,J.
  TITLE     Cloning of a novel, ubiquitously expressed human
            phosphatidylinositol 3-kinase and identification of its binding
            site on p85
  JOURNAL   Mol Cell Biol 13 (12), 7677-7688 (1993)
   PUBMED   8246984
REFERENCE   10 (residues 1 to 1053)
  AUTHORS   Carpenter,C.L., Duckworth,B.C., Auger,K.R., Cohen,B.,
            Schaffhausen,B.S. and Cantley,L.C.
  TITLE     Purification and characterization of phosphoinositide 3-kinase from
            rat liver
  JOURNAL   J Biol Chem 265 (32), 19704-19711 (1990)
   PUBMED   2174051
  REMARK    GeneRIF: This paper reports the first purification of a
            phosphoinositide 3-kinase and shows that the protein is a
            heterodimer of an 85 kd regulatory subunit that mediates binding to
            phosphorylated proteins and a 110 kd catalytic subunit.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC067728.25, AC117389.5 and AC020890.22.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_047304269.1, XP_054202832.1.
            
            Summary: This gene encodes an isoform of the catalytic subunit of
            phosphoinositide 3-kinase (PI3K). These kinases are important in
            signaling pathways involving receptors on the outer membrane of
            eukaryotic cells and are named for their catalytic subunit. The
            encoded protein is the catalytic subunit for PI3Kbeta (PI3KB).
            PI3KB has been shown to be part of the activation pathway in
            neutrophils which have bound immune complexes at sites of injury or
            infection. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.555356.1,
                                           SRR1803616.131525.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..1053
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit beta isoform isoform 3"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.1.153"
                     /note="PI3-kinase p110 subunit beta; PtdIns-3-kinase p110;
                     PI3K-beta; PI3-kinase subunit beta; ptdIns-3-kinase
                     subunit beta; ptdIns-3-kinase subunit p110-beta;
                     phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa
                     catalytic subunit beta; serine/threonine protein kinase
                     PIK3CB; phosphoinositide-3-kinase, catalytic, beta
                     polypeptide"
                     /calculated_mol_wt=120945
     Region          41..118
                     /region_name="PI3K_p85B"
                     /note="PI3-kinase family, p85-binding domain; smart00143"
                     /db_xref="CDD:197539"
     Region          180..288
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, Ras-binding domain; smart00144"
                     /db_xref="CDD:197540"
     Region          324..501
                     /region_name="C2_PI3K_class_I_beta_delta"
                     /note="C2 domain present in class I beta and delta
                     phosphatidylinositol 3-kinases (PI3Ks); cd08693"
                     /db_xref="CDD:176075"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI9; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     Region          410..418
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Region          515..685
                     /region_name="PI3Ka_I"
                     /note="Phosphoinositide 3-kinase (PI3K) class I, accessory
                     domain; PIK domain is conserved in all PI3 and
                     PI4-kinases. Its role is unclear but it has been suggested
                     to be involved in substrate presentation. In general, PI3K
                     class I prefer phosphoinositol (4,5)...; cd00872"
                     /db_xref="CDD:238444"
     Region          689..1050
                     /region_name="PI3Kc_IA_beta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase beta; cd05173"
                     /db_xref="CDD:270717"
     Region          761..767
                     /region_name="G-loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(762,764..766,768,786,788,791,822,834..837,842,845,
                     907,909,919..920)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270717"
     Site            order(829..830,857..858,861,931..932,945,948,956..959,962,
                     1029,1032..1033,1035..1036)
                     /site_type="other"
                     /note="regulatory subunit interface [polypeptide binding]"
                     /db_xref="CDD:270717"
     Site            876
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270717"
     Region          899..907
                     /region_name="Catalytic loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            899..907
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270717"
     Region          918..944
                     /region_name="Activation loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(920..933,939..944)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270717"
     Site            1053
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12502714; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     CDS             1..1053
                     /gene="PIK3CB"
                     /gene_synonym="P110BETA; PI3K; PI3KBETA; PIK3C1"
                     /coded_by="NM_001437291.1:583..3744"
                     /note="isoform 3 is encoded by transcript variant 9"
                     /db_xref="GeneID:5291"
                     /db_xref="HGNC:HGNC:8976"
                     /db_xref="MIM:602925"
ORIGIN      
        1 mcfsfimppa madildiwav dsqiasdgsi pvdfllptgi yiqlevprea tisyikqmlw
       61 kqvhnypmfn llmdidsymf acvnqtavye eledetrrlc dvrpflpvlk lvtrscdpge
      121 kldskigvli gkglhefdsl kdpevnefrr kmrkfseeki lslvglswmd wlkqtyppeh
      181 epsipenled klyggkliva vhfencqdvf sfqvspnmnp ikvnelaiqk rltihgkede
      241 vspydyvlqv sgrveyvfgd hpliqfqyir ncvmnralph filvecckik kmyeqemiai
      301 eaainrnssn lplplppkkt riishvwenn npfqivlvkg nklnteetvk vhvraglfhg
      361 tellcktivs sevsgkndhi wneplefdin icdlprmarl cfavyavldk vktkkstkti
      421 npskyqtirk agkvhypvaw vntmvfdfkg qlrtgdiilh swssfpdele emlnpmgtvq
      481 tnpytenata lhvkfpenkk qpyyyppfdk srggkkflpv lkeildrdpl sqlcenemdl
      541 iwtlrqdcre ifpqslpkll lsikwnkled vaqlqallqi wpklppreal elldfnypdq
      601 yvreyavgcl rqmsdeelsq yllqlvqvlk yepfldcals rflleralgn rrigqflfwh
      661 lrsevhipav svqfgvilea ycrgsvghmk vlskqvealn klktlnslik lnavklnrak
      721 gkeamhtclk qsayrealsd lqsplnpcvi lselyvekck ymdskmkplw lvynnkvfge
      781 dsvgvifkng ddlrqdmltl qmlrlmdllw keagldlrml pygclatgdr sglievvsts
      841 etiadiqlns snvaaaaafn kdallnwlke ynsgddldra ieeftlscag ycvasyvlgi
      901 gdrhsdnimv kktgqlfhid fghilgnfks kfgikrervp filtydfihv iqqgktgnte
      961 kfgrfrqcce daylilrrhg nlfitlfalm ltaglpelts vkdiqylkds lalgkseeea
     1021 lkqfkqkfde alreswttkv nwmahtvrkd yrs
//
LOCUS       NP_001428009            1231 aa            linear   PRI 21-NOV-2025
DEFINITION  cohesin subunit SA-2 isoform b [Homo sapiens].
ACCESSION   NP_001428009 XP_024308096 XP_054182361
VERSION     NP_001428009.1
DBSOURCE    REFSEQ: accession NM_001441080.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1231)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1231)
  AUTHORS   Fischer,A., Hernandez-Rodriguez,B., Mulet-Lazaro,R., Nuetzel,M.,
            Holzl,F., van Herk,S., Kavelaars,F.G., Stanewsky,H., Ackermann,U.,
            Niang,A.H., Diaz,N., Reuschel,E., Strieder,N., Hernandez-Lopez,I.,
            Valk,P.J.M., Vaquerizas,J.M., Rehli,M., Delwel,R. and Gebhard,C.
  TITLE     STAG2 mutations reshape the cohesin-structured spatial chromatin
            architecture to drive gene regulation in acute myeloid leukemia
  JOURNAL   Cell Rep 43 (8), 114498 (2024)
   PUBMED   39084219
  REMARK    GeneRIF: STAG2 mutations reshape the cohesin-structured spatial
            chromatin architecture to drive gene regulation in acute myeloid
            leukemia.
REFERENCE   3  (residues 1 to 1231)
  AUTHORS   Huber,J., Tanasie,N.L., Zernia,S. and Stigler,J.
  TITLE     Single-molecule imaging reveals a direct role of CTCF's zinc
            fingers in SA interaction and cluster-dependent RNA recruitment
  JOURNAL   Nucleic Acids Res 52 (11), 6490-6506 (2024)
   PUBMED   38742641
  REMARK    GeneRIF: Single-molecule imaging reveals a direct role of CTCF's
            zinc fingers in SA interaction and cluster-dependent RNA
            recruitment.
REFERENCE   4  (residues 1 to 1231)
  AUTHORS   Xu,W., Kim,J.S., Yang,T., Ya,A., Sadzewicz,L., Tallon,L.,
            Harris,B.T., Sarkaria,J., Jin,F. and Waldman,T.
  TITLE     STAG2 mutations regulate 3D genome organization, chromatin loops,
            and Polycomb signaling in glioblastoma multiforme
  JOURNAL   J Biol Chem 300 (6), 107341 (2024)
   PUBMED   38705393
  REMARK    GeneRIF: STAG2 mutations regulate 3D genome organization, chromatin
            loops, and Polycomb signaling in glioblastoma multiforme.
REFERENCE   5  (residues 1 to 1231)
  AUTHORS   Ros-Pardo,D., Gomez-Puertas,P. and Marcos-Alcalde,I.
  TITLE     STAG2: Computational Analysis of Missense Variants Involved in
            Disease
  JOURNAL   Int J Mol Sci 25 (2), 1280 (2024)
   PUBMED   38279279
  REMARK    GeneRIF: STAG2: Computational Analysis of Missense Variants
            Involved in Disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1231)
  AUTHORS   Gregson,H.C., Schmiesing,J.A., Kim,J.S., Kobayashi,T., Zhou,S. and
            Yokomori,K.
  TITLE     A potential role for human cohesin in mitotic spindle aster
            assembly
  JOURNAL   J Biol Chem 276 (50), 47575-47582 (2001)
   PUBMED   11590136
REFERENCE   7  (residues 1 to 1231)
  AUTHORS   Sumara,I., Vorlaufer,E., Gieffers,C., Peters,B.H. and Peters,J.M.
  TITLE     Characterization of vertebrate cohesin complexes and their
            regulation in prophase
  JOURNAL   J Cell Biol 151 (4), 749-762 (2000)
   PUBMED   11076961
REFERENCE   8  (residues 1 to 1231)
  AUTHORS   Carramolino,L., Lee,B.C., Zaballos,A., Peled,A., Barthelemy,I.,
            Shav-Tal,Y., Prieto,I., Carmi,P., Gothelf,Y., Gonzalez de
            Buitrago,G., Aracil,M., Marquez,G., Barbero,J.L. and Zipori,D.
  TITLE     SA-1, a nuclear protein encoded by one member of a novel gene
            family: molecular cloning and detection in hemopoietic organs
  JOURNAL   Gene 195 (2), 151-159 (1997)
   PUBMED   9305759
  REMARK    Erratum:[Gene 1998 Jan 12;206(2):283]
REFERENCE   9  (residues 1 to 1231)
  AUTHORS   Wu,C., Friedlander,P., Lamoureux,C., Zannis-Hadjopoulos,M. and
            Price,G.B.
  TITLE     cDNA clones contain autonomous replication activity
  JOURNAL   Biochim Biophys Acta 1174 (3), 241-257 (1993)
   PUBMED   7690594
REFERENCE   10 (residues 1 to 1231)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121601.13 and AL355476.12.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_024308096.1, XP_054182361.1.
            
            Summary: The protein encoded by this gene is a subunit of the
            cohesin complex, which regulates the separation of sister
            chromatids during cell division. Targeted inactivation of this gene
            results in chromatid cohesion defects and aneuploidy, suggesting
            that genetic disruption of cohesin is a cause of aneuploidy in
            human cancer. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.185417.1,
                                           SRR14038195.2702133.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2155974
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1231
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..1231
                     /product="cohesin subunit SA-2 isoform b"
                     /note="SCC3 homolog 2; cohesin subunit SA-2; SA2
                     stromalin; sister chromatid cohesion 3 homolog B; stromal
                     antigen 2"
                     /calculated_mol_wt=141196
     Region          1..75
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Region          102..>395
                     /region_name="IRR1"
                     /note="Cohesin [Cell division and chromosome
                     partitioning]; COG5537"
                     /db_xref="CDD:227824"
     Region          157..270
                     /region_name="STAG"
                     /note="STAG domain; pfam08514"
                     /db_xref="CDD:462502"
     Site            607
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1058
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1061
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Region          1064..1083
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1064
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35638; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1065
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35638; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1112
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     CDS             1..1231
                     /gene="STAG2"
                     /gene_synonym="bA517O1.1; HPE13; MKMS; NEDXCF; SA-2; SA2;
                     SCC3B"
                     /coded_by="NM_001441080.1:418..4113"
                     /note="isoform b is encoded by transcript variant 20"
                     /db_xref="GeneID:10735"
                     /db_xref="HGNC:HGNC:11355"
                     /db_xref="MIM:300826"
ORIGIN      
        1 miaapeiptd fnllqeseth fssdtdfedi egknqkqgkg ktckkgkkgp aekgkggngg
       61 gkppsgpnrm nghhqqngve nmmlfevvkm gksamqsvvd dwiesykhdr dialldlinf
      121 fiqcsgckgv vtaemfrhmq nseiirkmte efdedsgdyp ltmagpqwkk fkssfcefig
      181 vlvrqcqysi iydeymmdtv islltglsds qvrafrhtst laamklmtal vnvalnlsin
      241 mdntqrqyea ernkmigkra nerlelllqk rkelqenqde ienmmnaifk gvfvhryrda
      301 iaeiraicie eigiwmkmys daflndsylk yvgwtmhdkq gevrlkclta lqglyynkel
      361 nsklelftsr fkdrivsmtl dkeydvavqa iklltlvlqs seevltaedc envyhlvysa
      421 hrpvavaage flykklfsrr dpeedgmmkr rgrqgpnanl vktlvfffle selhehaayl
      481 vdsmwdcate llkdwecmns llleeplsge ealtdrqesa lieimlctir qaaechppvg
      541 rgtgkrvlta kekktqlddr tkitelfava lpqllakysv daekvtnllq lpqyfdleiy
      601 ttgrlekhld allrqirniv ekhtdtdvle acsktyhalc neeftifnrv disrsqlide
      661 ladkfnrlle dflqegeepd eddayqvlst lkritafhna hdlskwdlfa cnykllktgi
      721 engdmpeqiv ihalqcthyv ilwqlakite ssstkedllr lkkqmrvfcq icqhyltnvn
      781 ttvkeqafti lcdilmifsh qimsggrdml eplvytpdss lqsellsfil dhvfieqddd
      841 nnsadgqqed easkiealhk rrnllaafck livytvvemn taadifkqym kyyndygdii
      901 ketmsktrqi dkiqcaktli lslqqlfnem iqengynfdr ssstfsgike larrfaltfg
      961 ldqlktreai amlhkdgief afkepnpqge shpplnlafl dilsefsskl lrqdkrtvyv
     1021 ylekfmtfqm slrredvwlp lmsyrnslla ggdddtmsvi sgissrgstv rskkskpstg
     1081 krkvvegmql slteessssd smwlsreqtl htpvmmqtpq ltstimrepk rlrpedsfms
     1141 vypmqtehhq tpldynrrgt slmeddeepi vedvmmsseg riedlnegmd fdtmdidlpp
     1201 sknrrertel kpdffdpasi mdesvlgvsm f
//
LOCUS       NP_001428083             431 aa            linear   PRI 21-NOV-2025
DEFINITION  urokinase-type plasminogen activator isoform 1 preproprotein [Homo
            sapiens].
ACCESSION   NP_001428083 XP_011538168
VERSION     NP_001428083.1
DBSOURCE    REFSEQ: accession NM_001441154.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Li,D., Ding,C., Huang,F., Chang,M., Lu,Z., Li,G., Li,Y., Gao,H. and
            Sun,F.
  TITLE     Bioinformatics Analysis of the Expression and Prognostic Value of
            PLAU Gene in Wilms' Tumor
  JOURNAL   Anticancer Res 44 (9), 3829-3842 (2024)
   PUBMED   39197889
  REMARK    GeneRIF: Bioinformatics Analysis of the Expression and Prognostic
            Value of PLAU Gene in Wilms' Tumor.
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Guo,J., Wang,H., Huang,C., Lai,C., Shang,W., Luo,S. and Chen,L.
  TITLE     PLAU, transcriptionally negatively regulated by GATA6, promotes
            lung squamous carcinoma cell proliferation and migration
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (5), 119744 (2024)
   PUBMED   38702016
  REMARK    GeneRIF: PLAU, transcriptionally negatively regulated by GATA6,
            promotes lung squamous carcinoma cell proliferation and migration.
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Cui,X., Sun,H., Liu,X., Bai,Y., Bai,Y., Cui,Y., Wang,B., Zhang,S.
            and Li,X.
  TITLE     PLAU promotes cell proliferation and migration of head and neck
            cancer via STAT3 signaling pathway
  JOURNAL   Exp Cell Res 438 (2), 114056 (2024)
   PUBMED   38663475
  REMARK    GeneRIF: PLAU promotes cell proliferation and migration of head and
            neck cancer via STAT3 signaling pathway.
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Cetinsoy,O., Anyanwu,I., Krishnanand,H., Natarajan,G.,
            Ramachandran,N., Thomas,A. and Brookes,K.J.
  TITLE     Gene Association Study of the Urokinase Plasminogen Activator and
            Its Receptor Gene in Alzheimer's Disease
  JOURNAL   J Alzheimers Dis 99 (1), 241-250 (2024)
   PUBMED   38669542
  REMARK    GeneRIF: Gene Association Study of the Urokinase Plasminogen
            Activator and Its Receptor Gene in Alzheimer's Disease.
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Mekkawy,A.H., Pourgholami,M.H. and Morris,D.L.
  TITLE     Involvement of urokinase-type plasminogen activator system in
            cancer: an overview
  JOURNAL   Med Res Rev 34 (5), 918-956 (2014)
   PUBMED   24549574
  REMARK    Review article
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Naldini,L., Tamagnone,L., Vigna,E., Sachs,M., Hartmann,G.,
            Birchmeier,W., Daikuhara,Y., Tsubouchi,H., Blasi,F. and
            Comoglio,P.M.
  TITLE     Extracellular proteolytic cleavage by urokinase is required for
            activation of hepatocyte growth factor/scatter factor
  JOURNAL   EMBO J 11 (13), 4825-4833 (1992)
   PUBMED   1334458
REFERENCE   8  (residues 1 to 431)
  AUTHORS   Li,X., Smith,R.A. and Dobson,C.M.
  TITLE     Sequential 1H NMR assignments and secondary structure of the
            kringle domain from urokinase
  JOURNAL   Biochemistry 31 (40), 9562-9571 (1992)
   PUBMED   1327118
REFERENCE   9  (residues 1 to 431)
  AUTHORS   Stephens,R.W., Aumailley,M., Timpl,R., Reisberg,T., Tapiovaara,H.,
            Myohanen,H., Murphy-Ullrich,J. and Vaheri,A.
  TITLE     Urokinase binding to laminin-nidogen. Structural requirements and
            interactions with heparin
  JOURNAL   Eur J Biochem 207 (3), 937-942 (1992)
   PUBMED   1499567
REFERENCE   10 (residues 1 to 431)
  AUTHORS   Moroi,M. and Aoki,N.
  TITLE     Isolation and characterization of alpha2-plasmin inhibitor from
            human plasma. A novel proteinase inhibitor which inhibits
            activator-induced clot lysis
  JOURNAL   J Biol Chem 251 (19), 5956-5965 (1976)
   PUBMED   134998
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22.
            
            On Jun 5, 2025 this sequence version replaced XP_011538168.1.
            
            Summary: This gene encodes a secreted serine protease that converts
            plasminogen to plasmin. The encoded preproprotein is
            proteolytically processed to generate A and B polypeptide chains.
            These chains associate via a single disulfide bond to form the
            catalytically inactive high molecular weight urokinase-type
            plasminogen activator (HMW-uPA). HMW-uPA can be further processed
            into the catalytically active low molecular weight urokinase-type
            plasminogen activator (LMW-uPA). This low molecular weight form
            does not bind to the urokinase-type plasminogen activator receptor.
            Mutations in this gene may be associated with Quebec platelet
            disorder and late-onset Alzheimer's disease. Alternative splicing
            results in multiple transcript variants, at least one of which
            encodes an isoform that is proteolytically processed. [provided by
            RefSeq, Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.272854.1,
                                           SRR14038193.1400156.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..431
                     /product="urokinase-type plasminogen activator isoform 1
                     preproprotein"
                     /EC_number="3.4.21.73"
                     /note="plasminogen activator, urinary; U-plasminogen
                     activator; urokinase-type plasminogen activator"
                     /calculated_mol_wt=46384
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2158
     mat_peptide     21..431
                     /product="Urokinase-type plasminogen activator.
                     /id=PRO_0000028318"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=46384
     mat_peptide     21..177
                     /product="Urokinase-type plasminogen activator long chain
                     A. /id=PRO_0000028319"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=17849
     Region          34..57
                     /region_name="Binds urokinase plasminogen activator
                     surface receptor. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
     Site            38
                     /site_type="glycosylation"
                     /note="O-linked (Fuc) threonine.
                     /evidence=ECO:0000269|PubMed:2023947; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Region          67..152
                     /region_name="KR"
                     /note="Kringle domain; Kringle domains are believed to
                     play a role in binding mediators, such as peptides, other
                     proteins, membranes, or phospholipids. They are autonomous
                     structural domains, found in a varying number of copies,
                     in blood clotting and...; cd00108"
                     /db_xref="CDD:238056"
     Site            79
                     /site_type="active"
                     /note="putative domain interaction site [active]"
                     /db_xref="CDD:238056"
     Site            order(94,104,132,134,143)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Region          152..177
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
     mat_peptide     156..177
                     /product="Urokinase-type plasminogen activator short chain
                     A. /id=PRO_0000028320"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=2574
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9151681; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Site            177..178
                     /site_type="cleavage"
                     /note="Cleavage, during zymogen activation; propagated
                     from UniProtKB/Swiss-Prot (P00749.3)"
     mat_peptide     179..431
                     /product="Urokinase-type plasminogen activator chain B.
                     /id=PRO_0000028321"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=28425
     Region          179..422
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            179
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(224,275,376)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            322
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine. /id=CAR_000026;
                     propagated from UniProtKB/Swiss-Prot (P00749.3)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9151681; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Site            order(370,395,397)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..431
                     /gene="PLAU"
                     /gene_synonym="ATF; BDPLT5; QPD; u-PA; UPA; URK"
                     /coded_by="NM_001441154.1:410..1705"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:5328"
                     /db_xref="HGNC:HGNC:9052"
                     /db_xref="MIM:191840"
ORIGIN      
        1 mrallarlll cvlvvsdskg snelhqvpsn cdclnggtcv snkyfsnihw cncpkkfggq
       61 hceidksktc yegnghfyrg kastdtmgrp clpwnsatvl qqtyhahrsd alqlglgkhn
      121 ycrnpdnrrr pwcyvqvglk llvqecmvhd cadgkkpssp peelkfqcgq ktlrprfkii
      181 ggefttienq pwfaaiyrrh rggsvtyvcg gslispcwvi sathcfidyp kkedyivylg
      241 rsrlnsntqg emkfevenli lhkdysadtl ahhndiallk irskegrcaq psrtiqticl
      301 psmyndpqfg tsceitgfgk enstdylype qlkmtvvkli shrecqqphy ygsevttkml
      361 caadpqwktd scqgdsggpl vcslqgrmtl tgivswgrgc alkdkpgvyt rvshflpwir
      421 shtkeengla l
//
LOCUS       NP_001317132             191 aa            linear   PRI 21-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4E type 2 isoform F [Homo
            sapiens].
ACCESSION   NP_001317132 XP_016860866
VERSION     NP_001317132.1
DBSOURCE    REFSEQ: accession NM_001330203.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Wang,F., Zhang,J., Lin,X., Yang,L., Zhou,Q., Mi,X., Li,Q., Wang,S.,
            Li,D., Liu,X.M. and Zhou,J.
  TITLE     METTL16 promotes translation and lung tumorigenesis by sequestering
            cytoplasmic eIF4E2
  JOURNAL   Cell Rep 42 (3), 112150 (2023)
   PUBMED   36840945
  REMARK    GeneRIF: METTL16 promotes translation and lung tumorigenesis by
            sequestering cytoplasmic eIF4E2.
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Xu,Z., Choi,J.H., Dai,D.L., Luo,J., Ladak,R.J., Li,Q., Wang,Y.,
            Zhang,C., Wiebe,S., Liu,A.C.H., Ran,X., Yang,J., Naeli,P.,
            Garzia,A., Zhou,L., Mahmood,N., Deng,Q., Elaish,M., Lin,R.,
            Mahal,L.K., Hobman,T.C., Pelletier,J., Alain,T., Vidal,S.M.,
            Duchaine,T., Mazhab-Jafari,M.T., Mao,X., Jafarnejad,S.M. and
            Sonenberg,N.
  TITLE     SARS-CoV-2 impairs interferon production via NSP2-induced
            repression of mRNA translation
  JOURNAL   Proc Natl Acad Sci U S A 119 (32), e2204539119 (2022)
   PUBMED   35878012
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Zinshteyn,B., Sinha,N.K., Enam,S.U., Koleske,B. and Green,R.
  TITLE     Translational repression of NMD targets by GIGYF2 and EIF4E2
  JOURNAL   PLoS Genet 17 (10), e1009813 (2021)
   PUBMED   34665823
  REMARK    GeneRIF: Translational repression of NMD targets by GIGYF2 and
            EIF4E2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Joshi,B., Cameron,A. and Jagus,R.
  TITLE     Characterization of mammalian eIF4E-family members
  JOURNAL   Eur J Biochem 271 (11), 2189-2203 (2004)
   PUBMED   15153109
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Tee,A.R., Tee,J.A. and Blenis,J.
  TITLE     Characterizing the interaction of the mammalian eIF4E-related
            protein 4EHP with 4E-BP1
  JOURNAL   FEBS Lett 564 (1-2), 58-62 (2004)
   PUBMED   15094042
  REMARK    GeneRIF: 4EHP over-expression instigates a negative feedback loop
            that inhibits upstream signaling to 4E-BP1 and ribosomal protein S6
            kinase 1 (S6K1) whereas the 4E-BP1-binding-deficient mutant of
            4EHP(W95A) was unable to trigger this feedback loop
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Tan,N.G., Ardley,H.C., Scott,G.B., Rose,S.A., Markham,A.F. and
            Robinson,P.A.
  TITLE     Human homologue of ariadne promotes the ubiquitylation of
            translation initiation factor 4E homologous protein, 4EHP
  JOURNAL   FEBS Lett 554 (3), 501-504 (2003)
   PUBMED   14623119
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Rom,E., Kim,H.C., Gingras,A.C., Marcotrigiano,J., Favre,D.,
            Olsen,H., Burley,S.K. and Sonenberg,N.
  TITLE     Cloning and characterization of 4EHP, a novel mammalian
            eIF4E-related cap-binding protein
  JOURNAL   J Biol Chem 273 (21), 13104-13109 (1998)
   PUBMED   9582349
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092165.4 and AC073254.6.
            
            On Aug 20, 2016 this sequence version replaced XP_016860866.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2651551.1,
                                           SRR14038191.3142895.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..191
                     /product="eukaryotic translation initiation factor 4E type
                     2 isoform F"
                     /note="eIF4E-like cap-binding protein; eukaryotic
                     translation initiation factor 4E-like 3; eukaryotic
                     translation initiation factor 4E type 2; eIF-4E type 2;
                     eIF4E-like protein 4E-LP; mRNA cap-binding protein type 3;
                     eukaryotic translation initiation factor 4E homologous
                     protein"
                     /calculated_mol_wt=21975
     Region          <46..169
                     /region_name="IF4E"
                     /note="Eukaryotic initiation factor 4E; pfam01652"
                     /db_xref="CDD:460281"
     CDS             1..191
                     /gene="EIF4E2"
                     /gene_synonym="4E-LP; 4EHP; EIF4EL3; h4EHP; IF4e"
                     /coded_by="NM_001330203.2:37..612"
                     /note="isoform F is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS92971.1"
                     /db_xref="GeneID:9470"
                     /db_xref="HGNC:HGNC:3293"
                     /db_xref="MIM:605895"
ORIGIN      
        1 mnnkfdalkd ddsgdhdqne enstqkdgek ekterdknqs sskrkveqfw rfyshmvrpg
       61 dltghsdfhl fkegikpmwe ddanknggkw iirlrkglas rcwenlilam lgeqfmvgee
      121 icgavvsvrf qediisiwnk tasdqattar irdtlrrvln lppntimeyk thtdsikawe
      181 efhglvnssg r
//
LOCUS       NP_001412008             416 aa            linear   PRI 21-NOV-2025
DEFINITION  coatomer subunit delta isoform 9 [Homo sapiens].
ACCESSION   NP_001412008
VERSION     NP_001412008.1
DBSOURCE    REFSEQ: accession NM_001425079.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   O'Donoghue,L., Comer,S.P., Hiebner,D.W., Schoen,I., von
            Kriegsheim,A. and Smolenski,A.
  TITLE     RhoGAP6 interacts with COPI to regulate protein transport
  JOURNAL   Biochem J 480 (14), 1109-1127 (2023)
   PUBMED   37409526
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Li,W., Liang,J., Outeda,P., Turner,S., Wakimoto,B.T. and Watnick,T.
  TITLE     A genetic screen in Drosophila reveals an unexpected role for the
            KIP1 ubiquitination-promoting complex in male fertility
  JOURNAL   PLoS Genet 16 (12), e1009217 (2020)
   PUBMED   33378371
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Tidwell,T., Deshotel,M., Palumbos,J., Miller,C., Bayrak-Toydemir,P.
            and Carey,J.C.
  TITLE     Novel de novo ARCN1 intronic variant causes rhizomelic short
            stature with microretrognathia and developmental delay
  JOURNAL   Cold Spring Harb Mol Case Stud 6 (6), a005728 (2020)
   PUBMED   33154040
  REMARK    GeneRIF: Novel de novo ARCN1 intronic variant causes rhizomelic
            short stature with microretrognathia and developmental delay.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Schekman,R. and Orci,L.
  TITLE     Coat proteins and vesicle budding
  JOURNAL   Science 271 (5255), 1526-1533 (1996)
   PUBMED   8599108
  REMARK    Review article
REFERENCE   7  (residues 1 to 416)
  AUTHORS   Cukierman,E., Huber,I., Rotman,M. and Cassel,D.
  TITLE     The ARF1 GTPase-activating protein: zinc finger motif and Golgi
            complex localization
  JOURNAL   Science 270 (5244), 1999-2002 (1995)
   PUBMED   8533093
REFERENCE   8  (residues 1 to 416)
  AUTHORS   Radice,P., Pensotti,V., Jones,C., Perry,H., Pierotti,M.A. and
            Tunnacliffe,A.
  TITLE     The human archain gene, ARCN1, has highly conserved homologs in
            rice and Drosophila
  JOURNAL   Genomics 26 (1), 101-106 (1995)
   PUBMED   7782067
REFERENCE   9  (residues 1 to 416)
  AUTHORS   Orcl,L., Palmer,D.J., Amherdt,M. and Rothman,J.E.
  TITLE     Coated vesicle assembly in the Golgi requires only coatomer and ARF
            proteins from the cytosol
  JOURNAL   Nature 364 (6439), 732-734 (1993)
   PUBMED   8355790
REFERENCE   10 (residues 1 to 416)
  AUTHORS   Waters,M.G., Serafini,T. and Rothman,J.E.
  TITLE     'Coatomer': a cytosolic protein complex containing subunits of
            non-clathrin-coated Golgi transport vesicles
  JOURNAL   Nature 349 (6306), 248-251 (1991)
   PUBMED   1898986
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000941.6.
            
            Summary: This gene maps in a region, which include the mixed
            lineage leukemia and Friend leukemia virus integration 1 genes,
            where multiple disease-associated chromosome translocations occur.
            It is an intracellular protein. Archain sequences are well
            conserved among eukaryotes and this protein may play a fundamental
            role in eukaryotic cell biology. It has similarities to heat shock
            proteins and clathrin-associated proteins, and may be involved in
            vesicle structure or trafficking. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4643919.2944.1,
                                           ERR4643830.280274.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN02400308 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..416
                     /product="coatomer subunit delta isoform 9"
                     /note="coatomer protein delta-COP; coatomer protein
                     complex, subunit delta; archain vesicle transport protein
                     1; coatomer delta subunit; delta-coat protein; COPI coat
                     complex subunit delta"
                     /calculated_mol_wt=46537
     Region          4..132
                     /region_name="Delta_COP_N"
                     /note="delta subunit of the F-COPI complex, N-terminal
                     domain; cd14830"
                     /db_xref="CDD:341434"
     Region          167..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48444.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            232
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            240
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q5XJY5; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Region          271..>413
                     /region_name="AP_delta-COPI_MHD"
                     /note="Mu homology domain (MHD) of adaptor protein (AP)
                     coat protein I (COPI) delta subunit; cd09254"
                     /db_xref="CDD:271162"
     Site            308
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            350
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q5XJY5; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     CDS             1..416
                     /gene="ARCN1"
                     /gene_synonym="COPD; SRMMD; SSMG"
                     /coded_by="NM_001425079.1:140..1390"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:372"
                     /db_xref="HGNC:HGNC:649"
                     /db_xref="MIM:600820"
ORIGIN      
        1 mvllaaavct kagkaivsrq fvemtrtrie gllaafpklm ntgkqhtfve tesvryvyqp
       61 meklymvlit tknsniledl etlrlfsrip eycraleene isehcfdlif afdeivalgy
      121 renvnlaqir tftemdshee kvfravretq ereakaemrr kakelqqarr daerqgkkap
      181 gfggfgssav sggstaamit etiietdkpk vapaparpsg pskalklgak gkevdnfvdk
      241 lksegetims ssmgkrtsea tkmhappinm esvhmkieek itltcgrdgg lqnmelhgmi
      301 mlrisddkyg rirlhvened kkgvqlqthp nvdkklftae sliglknpek sfpvnsdvgv
      361 lkwrlqttee sfipltincw psesgngcdv nieyelqedn lelndvviti plplpk
//
LOCUS       NP_001400922             337 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, NMDA 2B isoform b precursor [Homo
            sapiens].
ACCESSION   NP_001400922
VERSION     NP_001400922.1
DBSOURCE    REFSEQ: accession NM_001413993.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Korinek,M., Candelas Serra,M., Abdel Rahman,F., Dobrovolski,M.,
            Kuchtiak,V., Abramova,V., Fili,K., Tomovic,E., Hrcka Krausova,B.,
            Krusek,J., Cerny,J., Vyklicky,L., Balik,A. and Smejkalova,T.
  TITLE     Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B genes:
            Insights into NMDA Receptor Structure, Function, and
            Pathophysiology
  JOURNAL   Physiol Res 73 (Suppl 1), S413-S434 (2024)
   PUBMED   38836461
  REMARK    GeneRIF: Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B
            genes: Insights into NMDA Receptor Structure, Function, and
            Pathophysiology.
            Review article
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Raich,I., Lillo,J., Rebassa,J.B., Capo,T., Cordomi,A.,
            Reyes-Resina,I., Pallas,M. and Navarro,G.
  TITLE     Dual Role of NMDAR Containing NR2A and NR2B Subunits in Alzheimer's
            Disease
  JOURNAL   Int J Mol Sci 25 (9), 4757 (2024)
   PUBMED   38731978
  REMARK    GeneRIF: Dual Role of NMDAR Containing NR2A and NR2B Subunits in
            Alzheimer's Disease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Iacobucci,G.J. and Popescu,G.K.
  TITLE     NMDA receptors: linking physiological output to biophysical
            operation
  JOURNAL   Nat Rev Neurosci 18 (4), 236-249 (2017)
   PUBMED   28303017
  REMARK    Review article
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Hu,C., Chen,W., Myers,S.J., Yuan,H. and Traynelis,S.F.
  TITLE     Human GRIN2B variants in neurodevelopmental disorders
  JOURNAL   J Pharmacol Sci 132 (2), 115-121 (2016)
   PUBMED   27818011
  REMARK    GeneRIF: In this review, mutations in GRIN2B were described as
            distributed throughout the entire gene in patients with
            neuropsychiatric and developmental disorders.
            Review article
            Erratum:[J Pharmacol Sci. 2017 Apr;133(4):280. doi:
            10.1016/j.jphs.2017.04.001. PMID: 28434657]
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Hess,S.D., Daggett,L.P., Crona,J., Deal,C., Lu,C.C., Urrutia,A.,
            Chavez-Noriega,L., Ellis,S.B., Johnson,E.C. and Velicelebi,G.
  TITLE     Cloning and functional characterization of human heteromeric
            N-methyl-D-aspartate receptors
  JOURNAL   J Pharmacol Exp Ther 278 (2), 808-816 (1996)
   PUBMED   8768735
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Kornau,H.C., Schenker,L.T., Kennedy,M.B. and Seeburg,P.H.
  TITLE     Domain interaction between NMDA receptor subunits and the
            postsynaptic density protein PSD-95
  JOURNAL   Science 269 (5231), 1737-1740 (1995)
   PUBMED   7569905
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Magnuson,D.S., Knudsen,B.E., Geiger,J.D., Brownstone,R.M. and
            Nath,A.
  TITLE     Human immunodeficiency virus type 1 tat activates
            non-N-methyl-D-aspartate excitatory amino acid receptors and causes
            neurotoxicity
  JOURNAL   Ann Neurol 37 (3), 373-380 (1995)
   PUBMED   7695237
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Mandich,P., Schito,A.M., Bellone,E., Antonacci,R., Finelli,P.,
            Rocchi,M. and Ajmar,F.
  TITLE     Mapping of the human NMDAR2B receptor subunit gene (GRIN2B) to
            chromosome 12p12
  JOURNAL   Genomics 22 (1), 216-218 (1994)
   PUBMED   7959773
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Platzer,K. and Lemke,J.R.
  TITLE     GRIN2B-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29851452
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Monyer,H., Sprengel,R., Schoepfer,R., Herb,A., Higuchi,M.,
            Lomeli,H., Burnashev,N., Sakmann,B. and Seeburg,P.H.
  TITLE     Heteromeric NMDA receptors: molecular and functional distinction of
            subtypes
  JOURNAL   Science 256 (5060), 1217-1221 (1992)
   PUBMED   1350383
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007916.10, AC007784.7 and
            AC007397.21.
            
            Summary: This gene encodes a member of the N-methyl-D-aspartate
            (NMDA) receptor family within the ionotropic glutamate receptor
            superfamily. The encoded protein is a subunit of the NMDA receptor
            ion channel which acts as an agonist binding site for glutamate.
            The NMDA receptors mediate a slow calcium-permeable component of
            excitatory synaptic transmission in the central nervous system. The
            NMDA receptors are heterotetramers of seven genetically encoded,
            differentially expressed subunits including NR1 (GRIN1), NR2
            (GRIN2A, GRIN2B, GRIN2C, or GRIN2D) and NR3 (GRIN3A or GRIN3B). The
            early expression of this gene in development suggests a role in
            brain development, circuit formation, synaptic plasticity, and
            cellular migration and differentiation. Naturally occurring
            mutations within this gene are associated with neurodevelopmental
            disorders including autism spectrum disorder, attention deficit
            hyperactivity disorder, epilepsy, and schizophrenia. [provided by
            RefSeq, Aug 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1298947.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465404 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.1"
     Protein         1..337
                     /product="glutamate receptor ionotropic, NMDA 2B isoform b
                     precursor"
                     /note="glutamate [NMDA] receptor subunit epsilon-2;
                     glutamate receptor subunit epsilon-2; N-methyl-D-aspartate
                     receptor subunit 3; N-methyl D-aspartate receptor subtype
                     2B; GluN2B(alt_5'UTR); glutamate receptor ionotropic, NMDA
                     2B; glutamate receptor, ionotropic, N-methyl D-aspartate
                     2B"
                     /calculated_mol_wt=34767
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2820
     Region          33..337
                     /region_name="PBP1_iGluR_NMDA_NR2"
                     /note="N-terminal leucine-isoleucine-valine-binding
                     protein (LIVBP)-like domain of the NR2 subunit of NMDA
                     receptor family; cd06378"
                     /db_xref="CDD:380601"
     Site            order(33,77..79,114,135,175,177,192,207..208,311..312)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:380601"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:26912815,
                     ECO:0007744|PDB:5EWJ, ECO:0007744|PDB:5EWL,
                     ECO:0007744|PDB:5EWM; propagated from UniProtKB/Swiss-Prot
                     (Q13224.3)"
     Site            order(75..80,82..83,118..119,175,179,206,208,311..317,
                     321..323,334)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:380601"
     CDS             1..337
                     /gene="GRIN2B"
                     /gene_synonym="DEE27; EIEE27; GluN2B; hNR3; MRD6; NMDAR2B;
                     NR2B; NR3"
                     /coded_by="NM_001413993.1:473..1486"
                     /note="isoform b precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:2904"
                     /db_xref="HGNC:HGNC:4586"
                     /db_xref="MIM:138252"
ORIGIN      
        1 mkpraeccsp kfwlvlavla vsgsrarsqk sppsigiavi lvgtsdevai kdahekddfh
       61 hlsvvprvel vamnetdpks iitricdlms drkiqgvvfa ddtdqeaiaq ildfisaqtl
      121 tpilgihggs smimadkdes smffqfgpsi eqqasvmlni meeydwyifs ivttyfpgyq
      181 dfvnkirsti ensfvgwele evllldmsld dgdskiqnql kklqspiill yctkeeatyi
      241 fevansvglt gygytwivps lvagdtdtvp aefptglisv sydewdyglp arvrdgiaii
      301 ttaasdmlse hsfipepkss cynthekriy qsnmlnr
//
LOCUS       NP_001425719             600 aa            linear   PRI 21-NOV-2025
DEFINITION  semaphorin-4F isoform 6 precursor [Homo sapiens].
ACCESSION   NP_001425719 XP_011530778 XP_054196166
VERSION     NP_001425719.1
DBSOURCE    REFSEQ: accession NM_001438790.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 600)
  AUTHORS   Fan,Q., Barathi,V.A., Cheng,C.Y., Zhou,X., Meguro,A., Nakata,I.,
            Khor,C.C., Goh,L.K., Li,Y.J., Lim,W., Ho,C.E., Hawthorne,F.,
            Zheng,Y., Chua,D., Inoko,H., Yamashiro,K., Ohno-Matsui,K.,
            Matsuo,K., Matsuda,F., Vithana,E., Seielstad,M., Mizuki,N.,
            Beuerman,R.W., Tai,E.S., Yoshimura,N., Aung,T., Young,T.L.,
            Wong,T.Y., Teo,Y.Y. and Saw,S.M.
  TITLE     Genetic variants on chromosome 1q41 influence ocular axial length
            and high myopia
  JOURNAL   PLoS Genet 8 (6), e1002753 (2012)
   PUBMED   22685421
REFERENCE   5  (residues 1 to 600)
  AUTHORS   Parrinello,S., Noon,L.A., Harrisingh,M.C., Wingfield Digby,P.,
            Rosenberg,L.H., Cremona,C.A., Echave,P., Flanagan,A.M., Parada,L.F.
            and Lloyd,A.C.
  TITLE     NF1 loss disrupts Schwann cell-axonal interactions: a novel role
            for semaphorin 4F
  JOURNAL   Genes Dev 22 (23), 3335-3348 (2008)
   PUBMED   19056885
  REMARK    GeneRIF: Sema4F levels were strongly reduced in a panel of human
            neurofibromas, confirming the relevance of these findings to the
            human disease.
REFERENCE   6  (residues 1 to 600)
  AUTHORS   Ayala,G.E., Dai,H., Powell,M., Li,R., Ding,Y., Wheeler,T.M.,
            Shine,D., Kadmon,D., Thompson,T., Miles,B.J., Ittmann,M.M. and
            Rowley,D.
  TITLE     Cancer-related axonogenesis and neurogenesis in prostate cancer
  JOURNAL   Clin Cancer Res 14 (23), 7593-7603 (2008)
   PUBMED   19047084
REFERENCE   7  (residues 1 to 600)
  AUTHORS   Park,Y.D., Park,D., Bhak,J. and Yang,J.M.
  TITLE     Proteomic approaches to the analysis of atopic dermatitis and new
            insights from interactomics
  JOURNAL   Proteomics Clin Appl 2 (3), 290-300 (2008)
   PUBMED   21136834
REFERENCE   8  (residues 1 to 600)
  AUTHORS   Francks,C., Fisher,S.E., Olson,R.K., Pennington,B.F., Smith,S.D.,
            DeFries,J.C. and Monaco,A.P.
  TITLE     Fine mapping of the chromosome 2p12-16 dyslexia susceptibility
            locus: quantitative association analysis and positional candidate
            genes SEMA4F and OTX1
  JOURNAL   Psychiatr Genet 12 (1), 35-41 (2002)
   PUBMED   11901358
  REMARK    GeneRIF: Fine mapping of the chromosome 2p12-16 dyslexia
            susceptibility candidate gene
REFERENCE   9  (residues 1 to 600)
  AUTHORS   Schultze,W., Eulenburg,V., Lessmann,V., Herrmann,L., Dittmar,T.,
            Gundelfinger,E.D., Heumann,R. and Erdmann,K.S.
  TITLE     Semaphorin4F interacts with the synapse-associated protein
            SAP90/PSD-95
  JOURNAL   J Neurochem 78 (3), 482-489 (2001)
   PUBMED   11483650
REFERENCE   10 (residues 1 to 600)
  AUTHORS   Encinas,J.A., Kikuchi,K., Chedotal,A., de Castro,F., Goodman,C.S.
            and Kimura,T.
  TITLE     Cloning, expression, and genetic mapping of Sema W, a member of the
            semaphorin family
  JOURNAL   Proc Natl Acad Sci U S A 96 (5), 2491-2496 (1999)
   PUBMED   10051670
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007387.4.
            
            On or before Apr 24, 2025 this sequence version replaced
            XP_011530778.1, XP_054196166.1.
            
            Summary: This gene encodes a transmembrane class IV semaphorin
            family protein, which plays a role in neural development. This gene
            may be involved in neurogenesis in prostate cancer, the development
            of neurofibromas, and breast cancer tumorigenesis. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Nov 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2733752.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..600
                     /product="semaphorin-4F isoform 6 precursor"
                     /note="semaphorin M; semaphorin-4F; semaphorin-W; sema
                     domain immunoglobulin domain transmembrane domain (TM) and
                     short cytoplasmic domain (semaphorin) 4F; sema domain,
                     immunoglobulin domain (Ig), transmembrane domain (TM) and
                     short cytoplasmic domain, (semaphorin) 4F"
                     /calculated_mol_wt=62792
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3311
     Region          52..511
                     /region_name="Sema_4F"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 4F (Sema4F); cd11261"
                     /db_xref="CDD:200522"
     Site            64
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95754.2)"
     Site            order(114..116,172,193,195..196,198,214,217,219,224,256,
                     280..284,286,365..366,402,406,409)
                     /site_type="other"
                     /note="plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200522"
     Site            133
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95754.2)"
     Site            order(257..258,260,263..265,299,302..304,306,308,332..334,
                     338..339,415,430)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200522"
     Site            509
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95754.2)"
     Region          512..563
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     CDS             1..600
                     /gene="SEMA4F"
                     /gene_synonym="M-SEMA; m-Sema-M; PRO2353; S4F; SEMAM;
                     SEMAW"
                     /coded_by="NM_001438790.1:131..1933"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 8"
                     /db_xref="GeneID:10505"
                     /db_xref="HGNC:HGNC:10734"
                     /db_xref="MIM:603706"
ORIGIN      
        1 mpasaarprp gpgqptaspf pllllavlsg pvsgrvprsv prtslpisea dscltrfavp
       61 htynysvllv dpashtlyvg ardtifalsl pfsgerprri dwmvpeahrq ncrkkgkked
      121 echnfvqila ianashlltc gtfafdpkcg vidvsrfqqv erlesgrgkc pfepaqrsaa
      181 vmaggvlyaa tvknylgtep iitravgrae dwirtdtlps wlnapafvaa valspaewgd
      241 edgddeiyff ftetsrafds yerikvprva rvcagdlggr ktlqqrwttf lkadllcpgp
      301 ehgrassvlq dvavlrpelg agtpifygif ssqwegatis avcafrpqdi rtvlngpfre
      361 lkhdcnrglp vvdndvpqpr pgecitnnmk lrhfgsslsl pdrvltfird hplmdrpvfp
      421 adghpllvtt dtaylrvvah rvtslsgkey dvlylgtedg hlhravriga qlsvledlal
      481 fpepqpvenm klyhswllvg srtevtqvnt tncgrlqscs ecilaqdpvc awsfrldecv
      541 ahagehrglv qdiesadvss lcpkepggkr pwkkgnmnlq dssqqnklst cylykegggr
//
LOCUS       NP_001425390             442 aa            linear   PRI 21-NOV-2025
DEFINITION  excitatory amino acid transporter 1 isoform 8 [Homo sapiens].
ACCESSION   NP_001425390
VERSION     NP_001425390.1
DBSOURCE    REFSEQ: accession NM_001438461.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Albury,C.L., Sutherland,H.G., Lam,A.W.Y., Tran,N.K., Lea,R.A.,
            Haupt,L.M. and Griffiths,L.R.
  TITLE     Identification of Polymorphisms in EAAT1 Glutamate Transporter Gene
            SLC1A3 Associated with Reduced Migraine Risk
  JOURNAL   Genes (Basel) 15 (6), 797 (2024)
   PUBMED   38927733
  REMARK    GeneRIF: Identification of Polymorphisms in EAAT1 Glutamate
            Transporter Gene SLC1A3 Associated with Reduced Migraine Risk.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Welby,E. and Ebert,A.D.
  TITLE     Diminished motor neuron activity driven by abnormal astrocytic
            EAAT1 glutamate transporter activity in spinal muscular atrophy is
            not fully restored after lentiviral SMN delivery
  JOURNAL   Glia 71 (5), 1311-1332 (2023)
   PUBMED   36655314
  REMARK    GeneRIF: Diminished motor neuron activity driven by abnormal
            astrocytic EAAT1 glutamate transporter activity in spinal muscular
            atrophy is not fully restored after lentiviral SMN delivery.
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Pant,S., Wu,Q., Ryan,R. and Tajkhorshid,E.
  TITLE     Microscopic Characterization of the Chloride Permeation Pathway in
            the Human Excitatory Amino Acid Transporter 1 (EAAT1)
  JOURNAL   ACS Chem Neurosci 13 (6), 776-785 (2022)
   PUBMED   35192345
  REMARK    GeneRIF: Microscopic Characterization of the Chloride Permeation
            Pathway in the Human Excitatory Amino Acid Transporter 1 (EAAT1).
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Lee,A., Anderson,A.R., Beasley,S.J., Barnett,N.L., Poronnik,P. and
            Pow,D.V.
  TITLE     A new splice variant of the glutamate-aspartate transporter:
            cloning and immunolocalization of GLAST1c in rat, pig and human
            brains
  JOURNAL   J Chem Neuroanat 43 (1), 52-63 (2012)
   PUBMED   22026960
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Vallejo-Illarramendi,A., Domercq,M. and Matute,C.
  TITLE     A novel alternative splicing form of excitatory amino acid
            transporter 1 is a negative regulator of glutamate uptake
  JOURNAL   J Neurochem 95 (2), 341-348 (2005)
   PUBMED   16042756
  REMARK    GeneRIF: EAAT1ex9skip splice variant is a negative regulator of
            full-length EAAT1 function in the human brain
REFERENCE   7  (residues 1 to 442)
  AUTHORS   Takai,S., Yamada,K., Kawakami,H., Tanaka,K. and Nakamura,S.
  TITLE     Localization of the gene (SLC1A3) encoding human glutamate
            transporter (GluT-1) to 5p13 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 209-210 (1995)
   PUBMED   7698014
REFERENCE   8  (residues 1 to 442)
  AUTHORS   Shashidharan,P., Huntley,G.W., Meyer,T., Morrison,J.H. and
            Plaitakis,A.
  TITLE     Neuron-specific human glutamate transporter: molecular cloning,
            characterization and expression in human brain
  JOURNAL   Brain Res 662 (1-2), 245-250 (1994)
   PUBMED   7859077
REFERENCE   9  (residues 1 to 442)
  AUTHORS   Arriza,J.L., Fairman,W.A., Wadiche,J.I., Murdoch,G.H.,
            Kavanaugh,M.P. and Amara,S.G.
  TITLE     Functional comparisons of three glutamate transporter subtypes
            cloned from human motor cortex
  JOURNAL   J Neurosci 14 (9), 5559-5569 (1994)
   PUBMED   7521911
REFERENCE   10 (residues 1 to 442)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010631.6 and AC008957.7.
            
            Summary: This gene encodes a member of a member of a high affinity
            glutamate transporter family. This gene functions in the
            termination of excitatory neurotransmission in central nervous
            system. Mutations are associated with episodic ataxia, Type 6.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3268355.1,
                                           SRR14038197.1830215.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2149398
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..442
                     /product="excitatory amino acid transporter 1 isoform 8"
                     /note="excitatory amino acid transporter 1; GLAST-1;
                     sodium-dependent glutamate/aspartate transporter 1; solute
                     carrier family 1 (glial high affinity glutamate
                     transporter), member 3"
                     /calculated_mol_wt=47844
     Region          2..396
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     CDS             1..442
                     /gene="SLC1A3"
                     /gene_synonym="EA6; EAAT1; GLAST; GLAST1"
                     /coded_by="NM_001438461.1:696..2024"
                     /note="isoform 8 is encoded by transcript variant 13"
                     /db_xref="GeneID:6507"
                     /db_xref="HGNC:HGNC:10941"
                     /db_xref="MIM:600111"
ORIGIN      
        1 misgfvgmaa ldskasgkmg mravvyymtt tiiavvigii iviiihpgkg tkenmhregk
       61 ivrvtaadaf ldlirnmfpp nlveacfkqf ktnyekrsfk vpiqanetlv gavinnvsea
      121 metltritee lvpvpgsvng vnalglvvfs mcfgfvignm keqgqalref fdslneaimr
      181 lvavimwyap vgilfliagk ivemedmgvi ggqlamytvt vivgllihav ivlpllyflv
      241 trknpwvfig gllqalital gtssssatlp itfkcleenn gvdkrvtrfv lpvgatinmd
      301 gtalyealaa ifiaqvnnfe lnfgqiitis itataasiga agipqaglvt mvivltsvgl
      361 ptdditliia vdwfldrlrt ttnvlgdslg agivehlsrh elknrdvemg nsvieenemk
      421 kpyqliaqdn etekpidset km
//
LOCUS       NP_001411050             256 aa            linear   PRI 21-NOV-2025
DEFINITION  radial spoke head protein 9 homolog isoform 5 [Homo sapiens].
ACCESSION   NP_001411050
VERSION     NP_001411050.1
DBSOURCE    REFSEQ: accession NM_001424121.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Hwang,J.Y., Chai,P., Nawaz,S., Choi,J., Lopez-Giraldez,F.,
            Hussain,S., Bilguvar,K., Mane,S., Lifton,R.P., Ahmad,W., Zhang,K.
            and Chung,J.J.
  TITLE     LRRC23 truncation impairs radial spoke 3 head assembly and sperm
            motility underlying male infertility
  JOURNAL   Elife 12, 90095 (2023)
   PUBMED   38091523
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Zhang,X., Xiao,Z., Zhang,J., Xu,C., Liu,S., Cheng,L., Zhou,S.,
            Zhao,S., Zhang,Y., Wu,J., Wang,Y. and Liu,M.
  TITLE     Differential requirements of IQUB for the assembly of radial spoke
            1 and the motility of mouse cilia and flagella
  JOURNAL   Cell Rep 41 (8), 111683 (2022)
   PUBMED   36417862
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Zhu,L., Liu,H., Chen,Y., Yan,X. and Zhu,X.
  TITLE     Rsph9 is critical for ciliary radial spoke assembly and central
            pair microtubule stability
  JOURNAL   Biol Cell 111 (2), 29-38 (2019)
   PUBMED   30383886
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Zietkiewicz,E., Bukowy-Bieryllo,Z., Voelkel,K., Klimek,B.,
            Dmenska,H., Pogorzelski,A., Sulikowska-Rowinska,A., Rutkiewicz,E.
            and Witt,M.
  TITLE     Mutations in radial spoke head genes and ultrastructural cilia
            defects in East-European cohort of primary ciliary dyskinesia
            patients
  JOURNAL   PLoS One 7 (3), e33667 (2012)
   PUBMED   22448264
  REMARK    GeneRIF: Mutations in RSPH9 leads to ultrastructural cilia defects
            and ciliary dyskinesia.
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Reish,O., Slatkin,M., Chapman-Shimshoni,D., Elizur,A., Chioza,B.,
            Castleman,V. and Mitchison,H.M.
  TITLE     Founder mutation(s) in the RSPH9 gene leading to primary ciliary
            dyskinesia in two inbred Bedouin families
  JOURNAL   Ann Hum Genet 74 (2), 117-125 (2010)
   PUBMED   20070851
  REMARK    GeneRIF: Study focused on an extended 5 generation Bedouin family,
            analysed mutation segregation, and calculated the age of the
            mutated allele in 2 families based on haplotypes and
            haplotype+microsatellite in an attempt to define the source of the
            mutation.
REFERENCE   8  (residues 1 to 256)
  AUTHORS   Castleman,V.H., Romio,L., Chodhari,R., Hirst,R.A., de Castro,S.C.,
            Parker,K.A., Ybot-Gonzalez,P., Emes,R.D., Wilson,S.W., Wallis,C.,
            Johnson,C.A., Herrera,R.J., Rutman,A., Dixon,M., Shoemark,A.,
            Bush,A., Hogg,C., Gardiner,R.M., Reish,O., Greene,N.D.,
            O'Callaghan,C., Purton,S., Chung,E.M. and Mitchison,H.M.
  TITLE     Mutations in radial spoke head protein genes RSPH9 and RSPH4A cause
            primary ciliary dyskinesia with central-microtubular-pair
            abnormalities
  JOURNAL   Am J Hum Genet 84 (2), 197-209 (2009)
   PUBMED   19200523
REFERENCE   9  (residues 1 to 256)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   10 (residues 1 to 256)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136131.15.
            
            Summary: This gene encodes a protein thought to be a component of
            the radial spoke head in motile cilia and flagella. Mutations in
            this gene are associated with primary ciliary dyskinesia 12.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Jul 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3788577.1,
                                           SRR14038193.99276.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..256
                     /product="radial spoke head protein 9 homolog isoform 5"
                     /note="radial spoke head protein 9 homolog; radial spoke
                     head 9 homolog"
                     /calculated_mol_wt=28457
     Region          <17..>106
                     /region_name="Radial_spoke"
                     /note="Radial spokehead-like protein; pfam04712"
                     /db_xref="CDD:461405"
     CDS             1..256
                     /gene="RSPH9"
                     /gene_synonym="C6orf206; CILD12; MRPS18AL1"
                     /coded_by="NM_001424121.1:64..834"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:221421"
                     /db_xref="HGNC:HGNC:21057"
                     /db_xref="MIM:612648"
ORIGIN      
        1 mdadslllsl elasgsgqgl spdrrasllt slmlvkrdyr ydrvlfwgri lglvadyyia
       61 qglsedqlap rktlyslnct ewsllppate emvaqssvvk grfmgdpsye yehtelqkvn
      121 egekvfeeei vvqikeetrl vsvidqidka vaiiprgalf ktpfgpthvn rtfeglslse
      181 akklssyfhf repvelknkt llekadldps ldfmdslehd ipkgnsplpg ghgicpqaia
      241 vghatchfpl rlepra
//
LOCUS       NP_001400238             303 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 14 [Homo sapiens].
ACCESSION   NP_001400238
VERSION     NP_001400238.1
DBSOURCE    REFSEQ: accession NM_001413309.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 303)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 303)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 303)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.168929.1,
                                           SRR3476690.391741.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..303
                     /product="RNA-binding Raly-like protein isoform 14"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=33224
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          171..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     Region          199..>244
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     CDS             1..303
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413309.1:329..1240"
                     /note="isoform 14 is encoded by transcript variant 36"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly rleskepfls
      121 vggyvfdydy yrddfynrlf dyhgrvpppp raviplkrpr vavtttrrgk gvfsmkggsr
      181 stasgstgsk lksdelqtik keltqiktki dsllgrleki ekqqkaeaea qkkqleeslv
      241 liqeecvsei adhsteepae ggpdadgeem tdgieedfde dgghelnvse ygksqapglp
      301 apg
//
LOCUS       NP_001393543            1043 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 5 [Homo sapiens].
ACCESSION   NP_001393543
VERSION     NP_001393543.1
DBSOURCE    REFSEQ: accession NM_001406614.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1043)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1043)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1043)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1043)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1043)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1043)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1043)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR18074969.3368626.1, SRR14038197.581070.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1043
                     /product="hamartin isoform 5"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=116145
     Region          16..598
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <587..>839
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1043
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406614.1:569..3700"
                     /note="isoform 5 is encoded by transcript variant 28"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mdtdvvvltt gvlvlitmlp mipqsgkqhl ldffdifgrl sswclkkpgh vaevylvhlh
       61 asvyalfhrl ygmypcnfvs flrshysmke nletfeevvk pmmehvrihp elvtgskdhe
      121 ldprrwkrle thdvviecak isldpteasy edgysvshqi sarfphrsad vttspyadtq
      181 nsygcatstp ystsrlmlln mpgqlpqtls spstrlitep pqatlwspsm vcgmttppts
      241 pgnvppdlsh pyskvfgtta ggkgtplgtp atspppaplc hsddyvhisl pqatvtpprk
      301 eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed siekdkeeaa
      361 isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv npeplhssld
      421 klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp trvgfgsgqp
      481 ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr liqqgadahs
      541 kelnklplps ksvdwthfgg sppsdeirtl rdqllllhnq llyerfkrqq halrnrrllr
      601 kvikaaalee hnaamkdqlk lqekdiqmwk vslqkeqary nqlqeqrdtm vtklhsqirq
      661 lqhdreefyn qsqelqtkle dcrnmiaelr ielkkannkv chtelllsqv sqklsnsesv
      721 qqqmeflnrq llvlgevnel yleqlqnkhs dttkevemmk aayrkelekn rshvlqqtqr
      781 ldtsqkrile leshlakkdh llleqkkyle dvklqargql qaaesryeaq kritqvfele
      841 ildlygrlek dgllkkleee kaeaaeaaee rldccndgcs dsmvghneea sghngetktp
      901 rpssargssg srggggssss sselstpekp phqragpfss rwettmgeas asipttvgsl
      961 pssksflgmk arelfrnkse sqcdedgmts slseslktel gkdlgveaki plnldgphps
     1021 pptpdsvgql himdynethh ehs
//
LOCUS       NP_001400002             328 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001400002
VERSION     NP_001400002.1
DBSOURCE    REFSEQ: accession NM_001413073.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.340260.1,
                                           SRR14038192.3665400.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..328
                     /product="mitochondrial fission regulator 1 isoform 4
                     precursor"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=30859
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=5550
     Region          22..251
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15390.2)"
     Region          177..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          179..304
                     /region_name="Necessary and sufficient to promote
                     mitochondrial fission. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     CDS             1..328
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001413073.1:132..1118"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 8"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsvlwsrkpy gssrsivrki gtnlsliqcp rvqfqinsha
       61 tewspshpge davasfadvg wvakeegecs arlrtevrsr pplqddllff ekapsrqisl
      121 pdlsqeepql ktpalaneea lqkicalene laalraqiak ivtqqeqqnl tagdldsttf
      181 gtipphpppp ppplpppalg lhqstsavdl ikerrekran agktlvknnp kkpempnmle
      241 ilkemnsvkl rsvkrseqdv kpkpvdatdp aaliaealkk kfayryrsds qdevekgipk
      301 seseatserv lslpagfiqp hvskhclg
//
LOCUS       NP_001400346             125 aa            linear   PRI 21-NOV-2025
DEFINITION  alpha-tocopherol transfer protein isoform 5 [Homo sapiens].
ACCESSION   NP_001400346
VERSION     NP_001400346.1
DBSOURCE    REFSEQ: accession NM_001413417.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Jeridi,C., Rachdi,A., Nabli,F., Saied,Z., Zouari,R., Ben
            Mohamed,D., Ben Said,M., Masmoudi,S., Ben Sassi,S. and Amouri,R.
  TITLE     Genetic heterogeneity within a consanguineous family involving TTPA
            and SETX genes
  JOURNAL   J Neurogenet 37 (4), 124-130 (2023)
   PUBMED   38109176
  REMARK    GeneRIF: Genetic heterogeneity within a consanguineous family
            involving TTPA and SETX genes.
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Ulatowski,L., Ghelfi,M., West,R., Atkinson,J., Finno,C.J. and
            Manor,D.
  TITLE     The tocopherol transfer protein mediates vitamin E trafficking
            between cerebellar astrocytes and neurons
  JOURNAL   J Biol Chem 298 (3), 101712 (2022)
   PUBMED   35150738
  REMARK    GeneRIF: The tocopherol transfer protein mediates vitamin E
            trafficking between cerebellar astrocytes and neurons.
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Arai,H. and Kono,N.
  TITLE     alpha-Tocopherol transfer protein (alpha-TTP)
  JOURNAL   Free Radic Biol Med 176, 162-175 (2021)
   PUBMED   34563650
  REMARK    GeneRIF: alpha-Tocopherol transfer protein (alpha-TTP).
            Review article
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 125)
  AUTHORS   Gotoda,T., Arita,M., Arai,H., Inoue,K., Yokota,T., Fukuo,Y.,
            Yazaki,Y. and Yamada,N.
  TITLE     Adult-onset spinocerebellar dysfunction caused by a mutation in the
            gene for the alpha-tocopherol-transfer protein
  JOURNAL   N Engl J Med 333 (20), 1313-1318 (1995)
   PUBMED   7566022
REFERENCE   6  (residues 1 to 125)
  AUTHORS   Arita,M., Sato,Y., Miyata,A., Tanabe,T., Takahashi,E., Kayden,H.J.,
            Arai,H. and Inoue,K.
  TITLE     Human alpha-tocopherol transfer protein: cDNA cloning, expression
            and chromosomal localization
  JOURNAL   Biochem J 306 (Pt 2) (Pt 2), 437-443 (1995)
   PUBMED   7887897
REFERENCE   7  (residues 1 to 125)
  AUTHORS   Ouahchi,K., Arita,M., Kayden,H., Hentati,F., Ben Hamida,M.,
            Sokol,R., Arai,H., Inoue,K., Mandel,J.L. and Koenig,M.
  TITLE     Ataxia with isolated vitamin E deficiency is caused by mutations in
            the alpha-tocopherol transfer protein
  JOURNAL   Nat Genet 9 (2), 141-145 (1995)
   PUBMED   7719340
REFERENCE   8  (residues 1 to 125)
  AUTHORS   Ben Hamida,C., Doerflinger,N., Belal,S., Linder,C., Reutenauer,L.,
            Dib,C., Gyapay,G., Vignal,A., Le Paslier,D., Cohen,D. et al.
  TITLE     Localization of Friedreich ataxia phenotype with selective vitamin
            E deficiency to chromosome 8q by homozygosity mapping
  JOURNAL   Nat Genet 5 (2), 195-200 (1993)
   PUBMED   8252047
REFERENCE   9  (residues 1 to 125)
  AUTHORS   Schuelke,M.
  TITLE     Ataxia with Vitamin E Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301419
REFERENCE   10 (residues 1 to 125)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC120042.3.
            
            Summary: This gene encodes a soluble protein that binds
            alpha-trocopherol, a form of vitamin E, with high selectivity and
            affinity. This protein plays an important role in regulating
            vitamin E levels in the body by transporting vitamin E between
            membrane vesicles and facilitating the secretion of vitamin E from
            hepatocytes to circulating lipoproteins. Mutations in this gene
            cause hereditary vitamin E deficiency (ataxia with vitamin E
            deficiency, AVED) and retinitis pigmentosa. [provided by RefSeq,
            Nov 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.52460.1,
                                           SRR14372080.3150445.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162895, SAMN04284274
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.3"
     Protein         1..125
                     /product="alpha-tocopherol transfer protein isoform 5"
                     /note="tocopherol (alpha) transfer protein (ataxia
                     (Friedreich-like) with vitamin E deficiency); alpha-TTP"
                     /calculated_mol_wt=14090
     Region          <40..67
                     /region_name="CRAL_TRIO_N"
                     /note="CRAL/TRIO, N-terminal domain; smart01100"
                     /db_xref="CDD:215024"
     Region          <64..95
                     /region_name="SEC14"
                     /note="Domain in homologues of a S. cerevisiae
                     phosphatidylinositol transfer protein (Sec14p);
                     smart00516"
                     /db_xref="CDD:214706"
     CDS             1..125
                     /gene="TTPA"
                     /gene_synonym="alphaTTP; ATTP; AVED; TTP1"
                     /coded_by="NM_001413417.1:33..410"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:7274"
                     /db_xref="HGNC:HGNC:12404"
                     /db_xref="MIM:600415"
ORIGIN      
        1 maearsqpsa gpqlnalpdh spllqpglaa lrrrareagv plaplpltds fllrflrard
       61 fdldlawrih mhgnnykqsl lqhfpdilpl eyggeefsme dicqewtnfi mksedylssi
      121 sesiq
//
LOCUS       NP_001397670             895 aa            linear   PRI 21-NOV-2025
DEFINITION  trafficking kinesin-binding protein 1 isoform 11 [Homo sapiens].
ACCESSION   NP_001397670 XP_047303672
VERSION     NP_001397670.1
DBSOURCE    REFSEQ: accession NM_001410741.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 895)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 895)
  AUTHORS   Baltrusaitis,E.E., Ravitch,E.E., Fenton,A.R., Perez,T.A.,
            Holzbaur,E.L.F. and Dominguez,R.
  TITLE     Interaction between the mitochondrial adaptor MIRO and the motor
            adaptor TRAK
  JOURNAL   J Biol Chem 299 (12), 105441 (2023)
   PUBMED   37949220
  REMARK    GeneRIF: Interaction between the mitochondrial adaptor MIRO and the
            motor adaptor TRAK.
REFERENCE   3  (residues 1 to 895)
  AUTHORS   Benhamida,J.K., Harmsen,H.J., Ma,D., William,C.M., Li,B.K.,
            Villafania,L., Sukhadia,P., Mullaney,K.A., Dewan,M.C., Vakiani,E.,
            Karajannis,M.A., Snuderl,M., Zagzag,D., Ladanyi,M., Rosenblum,M.K.
            and Bale,T.A.
  TITLE     Recurrent TRAK1::RAF1 Fusions in pediatric low-grade gliomas
  JOURNAL   Brain Pathol 33 (5), e13185 (2023)
   PUBMED   37399073
  REMARK    GeneRIF: Recurrent TRAK1::RAF1 Fusions in pediatric low-grade
            gliomas.
REFERENCE   4  (residues 1 to 895)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 895)
  AUTHORS   Wu,H., Liu,Y., Li,H., Du,C., Li,K., Dong,S., Meng,Q. and Zhang,H.
  TITLE     TRAK1-Mediated Abnormality of Mitochondrial Fission Increases
            Seizure Susceptibility in Temporal Lobe Epilepsy
  JOURNAL   Mol Neurobiol 58 (3), 1237-1247 (2021)
   PUBMED   33119838
  REMARK    GeneRIF: TRAK1-Mediated Abnormality of Mitochondrial Fission
            Increases Seizure Susceptibility in Temporal Lobe Epilepsy.
REFERENCE   6  (residues 1 to 895)
  AUTHORS   Ozyildirim,A.M., Wistow,G.J., Gao,J., Wang,J., Dickinson,D.P.,
            Frierson,H.F. Jr. and Laurie,G.W.
  TITLE     The lacrimal gland transcriptome is an unusually rich source of
            rare and poorly characterized gene transcripts
  JOURNAL   Invest Ophthalmol Vis Sci 46 (5), 1572-1580 (2005)
   PUBMED   15851553
REFERENCE   7  (residues 1 to 895)
  AUTHORS   Brickley,K., Smith,M.J., Beck,M. and Stephenson,F.A.
  TITLE     GRIF-1 and OIP106, members of a novel gene family of coiled-coil
            domain proteins: association in vivo and in vitro with kinesin
  JOURNAL   J Biol Chem 280 (15), 14723-14732 (2005)
   PUBMED   15644324
  REMARK    GeneRIF: GRIF-1 and OIP106 have roles in protein and/or organelle
            transport in excitable cells in a manner analogous to glutamate
            receptor-interacting-protein 1
REFERENCE   8  (residues 1 to 895)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   9  (residues 1 to 895)
  AUTHORS   Iyer,S.P. and Hart,G.W.
  TITLE     Roles of the tetratricopeptide repeat domain in O-GlcNAc
            transferase targeting and protein substrate specificity
  JOURNAL   J Biol Chem 278 (27), 24608-24616 (2003)
   PUBMED   12724313
REFERENCE   10 (residues 1 to 895)
  AUTHORS   Iyer,S.P., Akimoto,Y. and Hart,G.W.
  TITLE     Identification and cloning of a novel family of coiled-coil domain
            proteins that interact with O-GlcNAc transferase
  JOURNAL   J Biol Chem 278 (7), 5399-5409 (2003)
   PUBMED   12435728
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093414.3 and AC018358.20.
            
            On Aug 15, 2022 this sequence version replaced XP_047303672.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853562.23071.1,
                                           SRR14372079.3012881.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.1"
     Protein         1..895
                     /product="trafficking kinesin-binding protein 1 isoform
                     11"
                     /note="OGT(O-Glc-NAc transferase)-interacting protein 106
                     KDa; 106 kDa O-GlcNAc transferase-interacting protein;
                     milton homolog 1; O-linked N-acetylglucosamine transferase
                     interacting protein 106; protein Milton; trafficking
                     protein, kinesin binding 1"
                     /calculated_mol_wt=99552
     Region          38..295
                     /region_name="HAP1_N"
                     /note="HAP1 N-terminal conserved region; pfam04849"
                     /db_xref="CDD:461455"
     Region          356..525
                     /region_name="Milton"
                     /note="Kinesin associated protein; pfam12448"
                     /db_xref="CDD:463588"
     CDS             1..895
                     /gene="TRAK1"
                     /gene_synonym="DEE68; EIEE68; MILT1; OIP106"
                     /coded_by="NM_001410741.1:170..2857"
                     /note="isoform 11 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS93249.1"
                     /db_xref="GeneID:22906"
                     /db_xref="HGNC:HGNC:29947"
                     /db_xref="MIM:608112"
ORIGIN      
        1 mslrdkggee ecfeydcqde erkpthrqhd tqdlleevlc aervgqmtkt yndidavtrl
       61 leekerdlel aarigqsllk knktlterne lleeqvehir eevsqlrhel smkdellqfy
      121 tsaaeesepe svcstplkrn essssvqnyf hldslqkklk dleeenvvlr seasqlktet
      181 ityeekeqql vndcvkelrd anvqiasise elakktedaa rqqeeithll sqivdlqkka
      241 kacaveneel vqhlgaakda qrqltaelre ledkyaecme mlheaqeelk nlrnktmpnt
      301 tsrryhslgl fpmdslaaei egtmrkelql eeaespdith qkrvfetvrn inqvvkqrsl
      361 tpspmnipgs nqssamnsll sscvstprss fygsdignvv ldnktnsiil eteaadlgnd
      421 erskkpgtpg tpgshdleta lrrlslrren ylserrffee eqerklqela ekgelrsgsl
      481 tptesimslg thsrfseftg fsgmsfssrs ylpeklqivk plegsatlhh wqqlaqphlg
      541 gildprpgvv tkgfrtldvd ldevyclndf eeddtgdhis lprlatstpv qhpetsahhp
      601 gkcmsqtnst ftfttcrilh psdeltrvtp slnsaptpac gstshlkstp vatpctprrl
      661 slaesftntr estttmstsl glvwllkerg isaavydpqs wdragrgsll hsytpkmavi
      721 pstppnspmq tptssppsfe fkctsppydn flaskpassi lrevreknvr ssesqtdvsv
      781 snlnlvdkvr rfgvakvvns grahvptlte eqgpllcgpp gpapalvprg lvpeglplrc
      841 ptvtsaiggl qlnsgirrnr sfptmvgssm qmkapvtlts gilmgaklsk qtslr
//
LOCUS       NP_001411344             206 aa            linear   PRI 21-NOV-2025
DEFINITION  synaptosomal-associated protein 25 isoform SNAP25A [Homo sapiens].
ACCESSION   NP_001411344 XP_016883510 XP_054179862
VERSION     NP_001411344.1
DBSOURCE    REFSEQ: accession NM_001424415.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Wang,W., Gao,W., Gong,P., Song,W., Bu,X., Hou,J., Zhang,L. and
            Zhao,B.
  TITLE     Neuronal-specific TNFAIP1 ablation attenuates postoperative
            cognitive dysfunction via targeting SNAP25 for K48-linked
            ubiquitination
  JOURNAL   Cell Commun Signal 21 (1), 356 (2023)
   PUBMED   38102610
  REMARK    GeneRIF: Neuronal-specific TNFAIP1 ablation attenuates
            postoperative cognitive dysfunction via targeting SNAP25 for
            K48-linked ubiquitination.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Bolognesi,E., Guerini,F.R., Carta,A., Chiappedi,M., Sotgiu,S.,
            Mensi,M.M., Agliardi,C., Zanzottera,M. and Clerici,M.
  TITLE     The Role of SNAP-25 in Autism Spectrum Disorders Onset Patterns
  JOURNAL   Int J Mol Sci 24 (18), 14042 (2023)
   PUBMED   37762342
  REMARK    GeneRIF: The Role of SNAP-25 in Autism Spectrum Disorders Onset
            Patterns.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Yazar,V., Kuhlwein,J.K., Knehr,A., Grozdanov,V., Ekici,A.B.,
            Ludolph,A.C. and Danzer,K.M.
  TITLE     Impaired ATF3 signaling involves SNAP25 in SOD1 mutant ALS patients
  JOURNAL   Sci Rep 13 (1), 12019 (2023)
   PUBMED   37491426
  REMARK    GeneRIF: Impaired ATF3 signaling involves SNAP25 in SOD1 mutant ALS
            patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Zhang,J., Hou,S., Chi,X.Q., Shan,H.F., Li,X.W., Zhang,Q.J.,
            Wang,J.L. and Kang,C.B.
  TITLE     Role of SNAP25 on the occurrence and development of eosinophilic
            gastritis
  JOURNAL   Medicine (Baltimore) 102 (29), e34377 (2023)
   PUBMED   37478220
  REMARK    GeneRIF: Role of SNAP25 on the occurrence and development of
            eosinophilic gastritis.
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Hanson,P.I., Otto,H., Barton,N. and Jahn,R.
  TITLE     The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce
            a conformational change in syntaxin
  JOURNAL   J Biol Chem 270 (28), 16955-16961 (1995)
   PUBMED   7622514
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Hata,Y. and Sudhof,T.C.
  TITLE     A novel ubiquitous form of Munc-18 interacts with multiple
            syntaxins. Use of the yeast two-hybrid system to study interactions
            between proteins involved in membrane traffic
  JOURNAL   J Biol Chem 270 (22), 13022-13028 (1995)
   PUBMED   7768895
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Chapman,E.R., An,S., Barton,N. and Jahn,R.
  TITLE     SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin
            via domains that may form coiled coils
  JOURNAL   J Biol Chem 269 (44), 27427-27432 (1994)
   PUBMED   7961655
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Zhao,N., Hashida,H., Takahashi,N. and Sakaki,Y.
  TITLE     Cloning and sequence analysis of the human SNAP25 cDNA
  JOURNAL   Gene 145 (2), 313-314 (1994)
   PUBMED   8056350
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Abicht,A., Muller,J.S. and Lochmuller,H.
  TITLE     Congenital Myasthenic Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354824.8 and AL023913.6.
            
            On or before Sep 22, 2023 this sequence version replaced
            XP_016883510.1, XP_054179862.1.
            
            Summary: Synaptic vesicle membrane docking and fusion is mediated
            by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment
            protein receptors) located on the vesicle membrane (v-SNAREs) and
            the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE
            complex consists of a bundle of four helices, one of which is
            supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on
            the plasma membrane, the protein syntaxin supplies one helix and
            the protein encoded by this gene contributes the other two.
            Therefore, this gene product is a presynaptic plasma membrane
            protein involved in the regulation of neurotransmitter release. Two
            alternative transcript variants encoding different protein isoforms
            have been described for this gene. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14243140.3359716.1,
                                           SRR3476690.760244.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2146411
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.2"
     Protein         1..206
                     /product="synaptosomal-associated protein 25 isoform
                     SNAP25A"
                     /note="resistance to inhibitors of cholinesterase 4
                     homolog; synaptosome associated protein 25kDa;
                     synaptosomal-associated protein, 25kDa"
                     /calculated_mol_wt=23205
     Region          10..82
                     /region_name="SNARE_SNAP25N"
                     /note="N-terminal SNARE motif of SNAP25; cd15894"
                     /db_xref="CDD:277247"
     Site            order(24..25,28..29,31..33,35..40,42..44,46..47,49..50,
                     53..54,56..61,63..65,67..68,70..75,77..78)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277247"
     Site            53
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277247"
     Region          91..142
                     /region_name="SNAP-25"
                     /note="SNAP-25 family; pfam00835"
                     /db_xref="CDD:459955"
     Region          143..201
                     /region_name="SNARE_SNAP25C"
                     /note="C-terminal SNARE motif of SNAP25; cd15885"
                     /db_xref="CDD:277238"
     Site            order(143,145..146,149..154,156..157,160..161,163..165,
                     167..168,171..172,174..175,177..182,184..185,188,191,195,
                     198,201)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277238"
     Site            174
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277238"
     CDS             1..206
                     /gene="SNAP25"
                     /gene_synonym="bA416N4.2; CMS18; DEE117; dJ1068F16.2;
                     RIC-4; RIC4; SEC9; SNAP; SNAP-25; SUP"
                     /coded_by="NM_001424415.1:272..892"
                     /note="isoform SNAP25A is encoded by transcript variant
                     12"
                     /db_xref="GeneID:6616"
                     /db_xref="HGNC:HGNC:11132"
                     /db_xref="MIM:600322"
ORIGIN      
        1 maedadmrne leemqrradq ladeslestr rmlqlveesk dagirtlvml deqgeqldrv
       61 eegmnhinqd mkeaeknlkd lgkccglfic pcnklkssda ykkawgnnqd gvvasqparv
      121 vdereqmais ggfirrvtnd arenemdenl eqvsgiignl rhmaldmgne idtqnrqidr
      181 imekadsnkt rideanqrat kmlgsg
//
LOCUS       NP_001393541            1112 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 9 [Homo sapiens].
ACCESSION   NP_001393541
VERSION     NP_001393541.1
DBSOURCE    REFSEQ: accession NM_001406612.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1112)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1112)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1112)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1112)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1112)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1112)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1112)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1112)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1112)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1112)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1994992.1,
                                           SRR14038193.1171687.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1112
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1112
                     /product="hamartin isoform 9"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=123813
     Region          7..667
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <656..>908
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1112
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406612.1:189..3527"
                     /note="isoform 9 is encoded by transcript variant 26"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk mdtdvvvltt gvlvlitmlp mipqsgkqhl ldffdifgrl sswclkkpgh
      121 vaevylvhlh asvyalfhrl ygmypcnfvs flrshysmke nletfeevvk pmmehvrihp
      181 elvtgskdhe ldprrwkrle thdvviecak isldpteasy edgysvshqi sarfphrsad
      241 vttspyadtq nsygcatstp ystsrlmlln mpgqlpqtls spstrlitep pqatlwspsm
      301 vcgmttppts pgnvppdlsh pyskvfgttg gkgtplgtpa tspppaplch sddyvhislp
      361 qatvtpprke ermdsarpcl hrqhhllndr gseeppgskg svtlsdlpgf lgdlaseeds
      421 iekdkeeaai srelseitta eaepvvprgg fdspfyrdsl pgsqrkthsa asssqgasvn
      481 peplhssldk lgpdtpkqaf tpidlpcgsa despagdrec qtsletsift pspckipppt
      541 rvgfgsgqpp pydhlfeval pktahhfvir kteellkkak gnteedgvps tspmevldrl
      601 iqqgadahsk elnklplpsk svdwthfggs ppsdeirtlr dqllllhnql lyerfkrqqh
      661 alrnrrllrk vikaaaleeh naamkdqlkl qekdiqmwkv slqkeqaryn qlqeqrdtmv
      721 tklhsqirql qhdreefynq sqelqtkled crnmiaelri elkkannkvc htelllsqvs
      781 qklsnsesvq qqmeflnrql lvlgevnely leqlqnkhsd ttkevemmka ayrkeleknr
      841 shvlqqtqrl dtsqkrilel eshlakkdhl lleqkkyled vklqargqlq aaesryeaqk
      901 ritqvfelei ldlygrlekd gllkkleeek aeaaeaaeer ldccndgcsd smvghneeas
      961 ghngetktpr pssargssgs rggggsssss selstpekpp hqragpfssr wettmgeasa
     1021 sipttvgslp ssksflgmka relfrnkses qcdedgmtss lseslktelg kdlgveakip
     1081 lnldgphpsp ptpdsvgqlh imdynethhe hs
//
LOCUS       NP_001401586             520 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 2 isoform e [Homo sapiens].
ACCESSION   NP_001401586
VERSION     NP_001401586.1
DBSOURCE    REFSEQ: accession NM_001414657.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Jung,J.H., Lee,D., Ko,H.M. and Jang,H.J.
  TITLE     Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in Colorectal
            Cancer Cells by Activating p53
  JOURNAL   Biomolecules 11 (10), 1492 (2021)
   PUBMED   34680125
  REMARK    GeneRIF: Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in
            Colorectal Cancer Cells by Activating p53.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Royer-Bertrand,B., Cisarova,K., Niel Butschi,F., Foletti,G.,
            Guinchat,V., Tran,C., Superti-Furga,A. and Good,J.M.
  TITLE     CNOT2 haploinsufficiency in a 40-year-old man with intellectual
            disability, autism, and seizures
  JOURNAL   Am J Med Genet A 185 (8), 2602-2606 (2021)
   PUBMED   34018673
  REMARK    GeneRIF: CNOT2 haploinsufficiency in a 40-year-old man with
            intellectual disability, autism, and seizures.
            Review article
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Jayne,S., Zwartjes,C.G., van Schaik,F.M. and Timmers,H.T.
  TITLE     Involvement of the SMRT/NCoR-HDAC3 complex in transcriptional
            repression by the CNOT2 subunit of the human Ccr4-Not complex
  JOURNAL   Biochem J 398 (3), 461-467 (2006)
   PUBMED   16712523
  REMARK    GeneRIF: This study shows that SMRT/NCoR-HDAC3 complex is a
            cofactor of CNOT2-mediated repression and suggests that
            transcriptional regulation by the Ccr4-Not complex involves
            regulation of chromatin modification.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Winkler,G.S., Mulder,K.W., Bardwell,V.J., Kalkhoven,E. and
            Timmers,H.T.
  TITLE     Human Ccr4-Not complex is a ligand-dependent repressor of nuclear
            receptor-mediated transcription
  JOURNAL   EMBO J 25 (13), 3089-3099 (2006)
   PUBMED   16778766
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Shi,J. and Nelson,M.A.
  TITLE     The cyclin-dependent kinase 11 interacts with NOT2
  JOURNAL   Biochem Biophys Res Commun 334 (4), 1310-1316 (2005)
   PUBMED   16039607
  REMARK    GeneRIF: These findings suggest that CDK11 may contribute to
            apoptosis by regulating the activity of NOT2 independent of its
            kinase activity.
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Zwartjes,C.G., Jayne,S., van den Berg,D.L. and Timmers,H.T.
  TITLE     Repression of promoter activity by CNOT2, a subunit of the
            transcription regulatory Ccr4-not complex
  JOURNAL   J Biol Chem 279 (12), 10848-10854 (2004)
   PUBMED   14707134
  REMARK    GeneRIF: major repression function of CNOT2 is localized in a
            specialized protein motif, the Not-Box
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Denis,C.L. and Chen,J.
  TITLE     The CCR4-NOT complex plays diverse roles in mRNA metabolism
  JOURNAL   Prog Nucleic Acid Res Mol Biol 73, 221-250 (2003)
   PUBMED   12882519
  REMARK    Review article
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092881.8 and AC025569.37.
            
            Summary: This gene encodes a subunit of the multi-component
            CCR4-NOT complex. The CCR4-NOT complex regulates mRNA synthesis and
            degradation and is also thought to be involved in mRNA splicing,
            transport and localization. The encoded protein interacts with
            histone deacetylases and functions as a repressor of polymerase II
            transcription. Alternatively spliced transcript variants have been
            observed for this gene. [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3293763.1,
                                           SRR18074969.258756.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..520
                     /product="CCR4-NOT transcription complex subunit 2 isoform
                     e"
                     /note="negative regulator of transcription 2;
                     CCR4-associated factor 2; CC chemokine receptor 4-negative
                     regulator of transcription 2"
                     /calculated_mol_wt=57288
     Region          376..499
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..520
                     /gene="CNOT2"
                     /gene_synonym="CDC36; HSPC131; IDNADFS; NOT2; NOT2H"
                     /coded_by="NM_001414657.1:383..1945"
                     /note="isoform e is encoded by transcript variant 11"
                     /db_xref="GeneID:4848"
                     /db_xref="HGNC:HGNC:7878"
                     /db_xref="MIM:604909"
ORIGIN      
        1 mfgasrkkfv egvdsdyhde nmyysqssmf phrsekdmla spstsgqlsq fgaslygqqs
       61 alglpmrgms nntpqlnrsl sqgtqlpshv tpttgvptms lhtppspsrg ilpmnprnmm
      121 nhsqvgqgig ipsrtnsmss sglgspnrss psiicmpkqq psrqpftvns msgfgmnrnq
      181 afgmnnslss nifngtdgse nvtgldlsdf paladrnrre gsgnptplin plagrapyvg
      241 mvtkpaneqs qdfsihnedf palpgssykd ptssnddsks nlntsgktts stdgpkfpgd
      301 kssttqnnnq qkkgiqvlpd grvtnipqgm vtdqfgmigl ltfiraaetd pgmvhlalgs
      361 dlttlglnln spenlypkfa spwasspcrp qdidfhvpse yltnihirdk laaiklgryg
      421 edllfylyym nggdvlqlla avelfnrdwr yhkeervwit rapgmeptmk tntyergtyy
      481 ffdclnwrkv akefhleydk leerphlpst fnynpaqqaf
//
LOCUS       NP_001424669             519 aa            linear   PRI 21-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 11 [Homo sapiens].
ACCESSION   NP_001424669 XP_047272583 XP_054207402
VERSION     NP_001424669.1
DBSOURCE    REFSEQ: accession NM_001437740.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 519)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 519)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 519)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 519)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 519)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 519)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008641.7.
            
            On or before Apr 9, 2025 this sequence version replaced
            XP_047272583.1, XP_054207402.1.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1266700.1,
                                           SRR14038193.179140.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..519
                     /product="TNFAIP3-interacting protein 1 isoform 11"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=58516
     Region          <161..>198
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          <245..>476
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..519
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001437740.1:106..1665"
                     /note="isoform 11 is encoded by transcript variant 19"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 meatrlrqka eelvkdnell pppspslgsf dplaeltgkd snvtasptap acpsdkpapv
       61 qkppssgtss efevvtpeeq nspessshan amalgplpre dgnlmlhlqr lettlsvcae
      121 epdhgqlfth lgrmalefnr laskvhkneq rtsilqtlce qlrkenealk akldkgleqr
      181 dqaaerlree nlelkkllms ngnkegasgr pgspkmegtg kkavagqqqa svtagkvpev
      241 valgaaekkv kmleqqrsel levnkqwdqh frsmkqqyeq kitelrqkla dlqkqvtdle
      301 aereqkqrdf drklllaksk iemeetdkeq ltaeakelrq kvkylqdqls pltrqreyqe
      361 keiqrlnkal eealsiqtpp sspptafgsp egagallrkq elvtqnellk qqvkifeedf
      421 qrersdrerm neekeelkkq veklqaqvtl snaqlkafkd eekarealrq qkrkakpeyt
      481 wrlpcggvrn pnqssqvmdp ptarptepes pkndregpq
//
LOCUS       NP_001394376            2861 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform c [Homo sapiens].
ACCESSION   NP_001394376
VERSION     NP_001394376.1
DBSOURCE    REFSEQ: accession NM_001407447.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2861)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2861)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2861)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2861)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2861)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2861)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2861)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2861)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2861)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2861)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2350871.1,
                                           SRR11853567.24422.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2861
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2861
                     /product="adenomatous polyposis coli protein isoform c"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=313343
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Region          <8..272
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          239..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          340..392
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          393..466
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          490..526
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          523..565
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          530..571
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          534..571
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          566..609
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          581..613
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(604,608,612,651,655,659,696,700,704)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          610..656
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          621..662
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          657..701
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          667..707
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          671..705
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          702..743
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          709..749
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          713..749
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          744..785
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          750..1037
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Site            762
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            798
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          846..896
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            926
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          941..961
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          976..1005
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          978..1355
                     /region_name="Responsible for down-regulation through a
                     process mediated by direct ubiquitination"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1005
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1038..1187
                     /region_name="Interaction with catenins.
                     /evidence=ECO:0000269|PubMed:8259519"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1054..1153
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Site            1056
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1060
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1117..1187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1208..1262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1275..>1292
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1301..1386
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1309..1719
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1329..1394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1421..1493
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1456
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1544..1587
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1601..1629
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1655..1678
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1680..1733
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1682..1735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1734..1755
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1747..1854
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1764..1857
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Site            1792
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1879
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1881
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1882
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1884..1911
                     /region_name="Highly charged"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1891..1965
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1899..1968
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1983..2029
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1989
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1991
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2051..2070
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2053..2077
                     /region_name="Interaction with AXIN1.
                     /evidence=ECO:0000269|PubMed:10811618"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2061..2090
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2165..2653
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2169
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2185..2692
                     /region_name="Basic region.
                     /evidence=ECO:0000269|PubMed:17293347"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2241..2586
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Site            2278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2491
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2493..2861
                     /region_name="Interaction with DLG1.
                     /evidence=ECO:0000269|PubMed:8638125"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2553
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2587
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2685..2732
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2688..2861
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     Site            2689
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2692..2861
                     /region_name="Interaction with MAPRE1.
                     /evidence=ECO:0000269|PubMed:17293347"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2697
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2728
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2742
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2747..2861
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2807
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2821..2824
                     /region_name="Microtubule tip localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2859..2861
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     CDS             1..2861
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407447.1:404..8989"
                     /note="isoform c is encoded by transcript variant 17"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrriar iqqiekdilr irqllqsqat
      241 eaerssqnkh etgshdaerq negqgvgein matsgngqgs ttrmdhetas vlssssthsa
      301 prrltshlgt kvemvyslls mlgthdkddm srtllamsss qdscismrqs gclplliqll
      361 hgndkdsvll gnsrgskear arasaalhni ihsqpddkrg rreirvlhll eqiraycetc
      421 wewqeahepg mdqdknpmpa pvehqicpav cvlmklsfde ehrhamnelg rkatrgissq
      481 elgqglsggl qaiaellqvd cemygltndh ysitlrryag maltnltfgd vankatlcsm
      541 kgcmralvaq lksesedlqq viasvlrnls wradvnskkt lrevgsvkal mecalevkke
      601 stlksvlsal wnlsahcten kadicavdga laflvgtlty rsqtntlaii esgggilrnv
      661 ssliatnedh rqilrenncl qtllqhlksh sltivsnacg tlwnlsarnp kdqealwdmg
      721 avsmlknlih skhkmiamgs aaalrnlman rpakykdani mspgsslpsl hvrkqkalea
      781 eldaqhlset fdnidnlspk ashrskqrhk qslygdyvfd tnrhddnrsd nfntgnmtvl
      841 spylnttvlp sssssrgsld ssrsekdrsl erergiglgn yhpatenpgt sskrglqist
      901 taaqiakvme evsaihtsqe drssgsttel hcvtdernal rrssaahths ntynftksen
      961 snrtcsmpya kleykrssnd slnsvsssdg ygkrgqmkps iesyseddes kfcsygqypa
     1021 dlahkihsan hmddndgeld tpinyslkys deqlnsgrqs psqnerwarp khiiedeikq
     1081 seqrqsrnqs ttypvytest ddkhlkfqph fgqqecvspy rsrgangset nrvgsnhgin
     1141 qnvsqslcqe ddyeddkptn yseryseeeq heeeerptny sikyneekrh vdqpidyslk
     1201 yatdipssqk qsfsfsksss gqssktehms sssentstps snakrqnqlh pssaqsrsgq
     1261 pqkaatckvs sinqetiqty cvedtpicfs rcsslsslss aedeigcnqt tqeadsantl
     1321 qiaeikekig trsaedpvse vpavsqhprt kssrlqgssl ssesarhkav efssgaksps
     1381 ksgaqtpksp pehyvqetpl mfsrctsvss ldsfesrsia ssvqsepcsg mvsgiispsd
     1441 lpdspgqtmp psrsktpppp pqtaqtkrev pknkaptaek resgpkqaav naavqrvqvl
     1501 pdadtllhfa testpdgfsc ssslsalsld epfiqkdvel rimppvqend ngneteseqp
     1561 kesnenqeke aektidsekd llddsddddi eileeciisa mptkssrkak kpaqtasklp
     1621 ppvarkpsql pvykllpsqn rlqpqkhvsf tpgddmprvy cvegtpinfs tatslsdlti
     1681 esppnelaag egvrggaqsg efekrdtipt egrstdeaqg gktssvtipe lddnkaeegd
     1741 ilaecinsam pkgkshkpfr vkkimdqvqq asasssapnk nqldgkkkkp tspvkpipqn
     1801 teyrtrvrkn adsknnlnae rvfsdnkdsk kqnlknnskv fndklpnned rvrgsfafds
     1861 phhytpiegt pycfsrndsl ssldfddddv dlsrekaelr kakenkesea kvtshtelts
     1921 nqqsanktqa iakqpinrgq pkpilqkqst fpqsskdipd rgaatdeklq nfaientpvc
     1981 fshnsslssl sdidqennnk enepiketep pdsqgepskp qasgyapksf hvedtpvcfs
     2041 rnsslsslsi dseddllqec issampkkkk psrlkgdnek hsprnmggil gedltldlkd
     2101 iqrpdsehgl spdsenfdwk aiqegansiv sslhqaaaaa clsrqassds dsilslksgi
     2161 slgspfhltp dqeekpftsn kgprilkpge kstletkkie seskgikggk kvykslitgk
     2221 vrsnseisgq mkqplqanmp sisrgrtmih ipgvrnssss tspvskkgpp lktpasksps
     2281 egqtattspr gakpsvksel spvarqtsqi ggsskapsrs gsrdstpsrp aqqplsrpiq
     2341 spgrnsispg rngisppnkl sqlprtssps tastkssgsg kmsytspgrq msqqnltkqt
     2401 glsknassip rsesaskgln qmnngngank kvelsrmsst kssgsesdrs erpvlvrqst
     2461 fikeapsptl rrkleesasf eslspssrpa sptrsqaqtp vlspslpdms lsthssvqag
     2521 gwrklppnls ptieyndgrp akrhdiarsh sespsrlpin rsgtwkrehs khssslprvs
     2581 twrrtgssss ilsassesse kaksedekhv nsisgtkqsk enqvsakgtw rkikenefsp
     2641 tnstsqtvss gatngaeskt liyqmapavs ktedvwvrie dcpinnprsg rsptgntppv
     2701 idsvsekanp nikdskdnqa kqnvgngsvp mrtvglenrl nsfiqvdapd qkgteikpgq
     2761 nnpvpvsetn essivertpf sssssskhss psgtvaarvt pfnynpsprk ssadstsarp
     2821 sqiptpvnnn tkkrdsktds tessgtqspk rhsgsylvts v
//
LOCUS       NP_001425735            1196 aa            linear   PRI 21-NOV-2025
DEFINITION  NHS-like protein 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001425735 XP_047298022 XP_054182933
VERSION     NP_001425735.1
DBSOURCE    REFSEQ: accession NM_001438806.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1196)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1196)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1196)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL929401.8 and BX119917.9.
            
            On or before Apr 24, 2025 this sequence version replaced
            XP_047298022.1, XP_054182933.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2354078.1,
                                           SRR14372079.2902448.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155550, SAMN03568912
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..1196
                     /product="NHS-like protein 2 isoform 3"
                     /note="NHS-like protein 2; TPT1-like protein"
                     /calculated_mol_wt=130099
     Region          <510..726
                     /region_name="NHS"
                     /note="NHS-like; pfam15273"
                     /db_xref="CDD:464606"
     Region          <692..926
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1196
                     /gene="NHSL2"
                     /coded_by="NM_001438806.1:244..3834"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:340527"
                     /db_xref="HGNC:HGNC:33737"
                     /db_xref="MIM:301093"
ORIGIN      
        1 mpfyrrtvvp qrlcprnppq qlaelrdvsh laalsllrql adlcghslal ledleghlla
       61 lgrrtdslyr rtvrlrrrlp crllgpeede eelgashwsn ltrsqrarep vdaihteeye
      121 eqysearlvg qtfrssdeat kptpnprpqs arrlefilmp tkrqlsedet ttqgvrapea
      181 slslsttadk qtawnslfpl pileekrwpq lcstqsdivp inisgqqfdk haslrhslfn
      241 tetavnpkst lrrrrtiigf snfsqrdqgh snspagsvah sttsdirpsh svpegvhgrv
      301 avgqdarfps ltspvlrtps sepdephqar sgpnppgmes mgmvysvpss cngptestfs
      361 tswkgdafty mtpsatsqsn qvnengknps cgnswvslnk vpplvpkeaa tllvardnpa
      421 gcsgsagype rliqqrhmpe rpskigllts gtsrletgpg gasrfrersl svptdsgttd
      481 vdydeeqkan eacalpfast ssegsnsadn iaslsaqqea qhrrqrsksi slrkakkkps
      541 pptrsvslvk depgllpegg salpkdqrpk slclslehqg hhsshpdaqg hpaipnhkdp
      601 estqfshhwy ltdwksgdty qslsssstat gttviectqv qgsseslasp stsrattpsq
      661 lsievearei sspgrppglm spssgyssqs etptptvsms ltlghlppps ssvrvrpvvp
      721 erksslppts pmekfpksrl sfdlpltssp nldlsgmsis irsktkvsrh hsetnfgvkl
      781 aqktnpnqpi mpmvtqsdlr svrlrsvsks epeddiespe yaeepraeev ftlperktkp
      841 pvaekppvar rppslvhkpp svpeeyalts ptlampprss iqharplpqd sytvvrkpkp
      901 ssfpdgrspg estapsslvf tpfasssdaf fsgtqqppqg svedegpkvr vlperislqs
      961 qeeaekkkgk ipppvpkkps vlylpltspt aqmeayvaep rlplspiitl eedtkcpatg
     1021 ddlqslgqrv tstpqadser easplgssve pgteekslis dktaewiaed dddvfvasrt
     1081 tedlftvihr skrkllgwke pgeafvggrt sshspiknta espisestat agsgssanld
     1141 agrnddfkal lqkkgskatp rsrpsaaell kttnplarri iaqfskdyet tdnpst
//
LOCUS       NP_001427876             975 aa            linear   PRI 21-NOV-2025
DEFINITION  centriole and centriolar satellite protein OFD1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001427876 XP_047298543 XP_054183981
VERSION     NP_001427876.1
DBSOURCE    REFSEQ: accession NM_001440947.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 975)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 975)
  AUTHORS   Kim,N.H., Lee,C.H. and Lee,A.Y.
  TITLE     Extraciliary OFD1 Is Involved in Melanocyte Survival through Cell
            Adhesion to ECM via Paxillin
  JOURNAL   Int J Mol Sci 24 (24), 17528 (2023)
   PUBMED   38139355
  REMARK    GeneRIF: Extraciliary OFD1 Is Involved in Melanocyte Survival
            through Cell Adhesion to ECM via Paxillin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 975)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 975)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   5  (residues 1 to 975)
  AUTHORS   Alitalo,T., Francis,F., Kere,J., Lehrach,H., Schlessinger,D. and
            Willard,H.F.
  TITLE     A 6-Mb YAC contig in Xp22.1-p22.2 spanning the DXS69E, XE59, GLRA2,
            PIGA, GRPR, CALB3, and PHKA2 genes
  JOURNAL   Genomics 25 (3), 691-700 (1995)
   PUBMED   7759104
REFERENCE   6  (residues 1 to 975)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   7  (residues 1 to 975)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   8  (residues 1 to 975)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
REFERENCE   9  (residues 1 to 975)
  AUTHORS   Franco,B., Bruel,A.L. and Thauvin-Robinet,C.
  TITLE     Oral-Facial-Digital Syndrome Type I
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301367
REFERENCE   10 (residues 1 to 975)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC003037.1.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047298543.1, XP_054183981.1.
            
            Summary: This gene is located on the X chromosome and encodes a
            centrosomal protein. A knockout mouse model has been used to study
            the effect of mutations in this gene. The mouse gene is also
            located on the X chromosome, however, unlike the human gene it is
            not subject to X inactivation. Mutations in this gene are
            associated with oral-facial-digital syndrome type I and
            Simpson-Golabi-Behmel syndrome type 2. Many pseudogenes have been
            identified; a single pseudogene is found on chromosome 5 while as
            many as fifteen have been found on the Y chromosome. [provided by
            RefSeq, Aug 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1675812.1,
                                           SRR14038193.3550750.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..975
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..975
                     /product="centriole and centriolar satellite protein OFD1
                     isoform 4"
                     /note="oral-facial-digital syndrome 1 protein; protein
                     71-7A; Joubert syndrome type 10; centriole and centriolar
                     satellite protein OFD1"
                     /calculated_mol_wt=112839
     Region          75..101
                     /region_name="LisH_2"
                     /note="pfam16045"
                     /db_xref="CDD:464992"
     Region          191..>954
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          <273..>556
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..975
                     /gene="OFD1"
                     /gene_synonym="71-7A; CXorf5; JBTS10; RP23; SGBS2"
                     /coded_by="NM_001440947.1:325..3252"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:8481"
                     /db_xref="HGNC:HGNC:2567"
                     /db_xref="MIM:300170"
ORIGIN      
        1 mmaqsnmftv advlsqdelr kklyqtfkdr gildtlktql rnqlihelmh pvlsgelqpr
       61 sisvegssll igasnslvad hlqrcgyeys lsvffpesgl akekvftmqd llqlikinpt
      121 sslykslvsg sdkenqkgfl mhflkelaey hqakescnme tqtsstfnrd slaeklqlid
      181 dqfadaypqr ikfesleikl neykreieeq lraemcqklk ffkdteiaki kmeakkkyek
      241 eltmfqndfe kacqakseal vlrekstler ihkhqeietk eiyaqrqlll kdmdllrgre
      301 aelkqrveaf elnqklqeek hksitealrr qeqniksfee tydrklknel lkyqlelkdd
      361 yiirtnrlie derknkekav hlqeeliain skkeelnqsv nrvkelelel esvkaqslai
      421 tkqnhmlnek vkemsdysll keeklellaq nkllkqqlee srnenlrlln rlaqpapela
      481 vfqkelrkae kaivveheef escrqalhkq lqdeiehsaq lkaqilgyka svkslttqva
      541 dlklqlkqtq talenevycn pkqsvidrsv nglingnvvp cngeisgdfl nnpfkqenvl
      601 armvasritn yptawvegss pdsdlefvan tkarvkelqq eaerlekafr syhrrvikns
      661 aksplaaksp pslhlleafk nitsssperh ifgedrvvse qpqvgtleer ndvvealtgs
      721 aasrlrggts srrlsstplp kakrslesem yleglgrshi aspspcpdrm plpsptesrh
      781 slsippvssp peqkvglyrr qtelqdksef sdvdklafkd neefessfec vdqkqieeqk
      841 eeekireqqv kerrqreerr qsnlqevler erreleklyq erkmieeslk ikikkeleme
      901 nelemsnqei kdksahsenp lekymkiiqq eqdqesadks skkmvqegsl vdtlqssdkv
      961 esltgfshee lddsw
//
LOCUS       NP_001401580             540 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 2 isoform a [Homo sapiens].
ACCESSION   NP_001401580 XP_011536701
VERSION     NP_001401580.1
DBSOURCE    REFSEQ: accession NM_001414651.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 540)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 540)
  AUTHORS   Jung,J.H., Lee,D., Ko,H.M. and Jang,H.J.
  TITLE     Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in Colorectal
            Cancer Cells by Activating p53
  JOURNAL   Biomolecules 11 (10), 1492 (2021)
   PUBMED   34680125
  REMARK    GeneRIF: Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in
            Colorectal Cancer Cells by Activating p53.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 540)
  AUTHORS   Royer-Bertrand,B., Cisarova,K., Niel Butschi,F., Foletti,G.,
            Guinchat,V., Tran,C., Superti-Furga,A. and Good,J.M.
  TITLE     CNOT2 haploinsufficiency in a 40-year-old man with intellectual
            disability, autism, and seizures
  JOURNAL   Am J Med Genet A 185 (8), 2602-2606 (2021)
   PUBMED   34018673
  REMARK    GeneRIF: CNOT2 haploinsufficiency in a 40-year-old man with
            intellectual disability, autism, and seizures.
            Review article
REFERENCE   4  (residues 1 to 540)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 540)
  AUTHORS   Jayne,S., Zwartjes,C.G., van Schaik,F.M. and Timmers,H.T.
  TITLE     Involvement of the SMRT/NCoR-HDAC3 complex in transcriptional
            repression by the CNOT2 subunit of the human Ccr4-Not complex
  JOURNAL   Biochem J 398 (3), 461-467 (2006)
   PUBMED   16712523
  REMARK    GeneRIF: This study shows that SMRT/NCoR-HDAC3 complex is a
            cofactor of CNOT2-mediated repression and suggests that
            transcriptional regulation by the Ccr4-Not complex involves
            regulation of chromatin modification.
REFERENCE   6  (residues 1 to 540)
  AUTHORS   Winkler,G.S., Mulder,K.W., Bardwell,V.J., Kalkhoven,E. and
            Timmers,H.T.
  TITLE     Human Ccr4-Not complex is a ligand-dependent repressor of nuclear
            receptor-mediated transcription
  JOURNAL   EMBO J 25 (13), 3089-3099 (2006)
   PUBMED   16778766
REFERENCE   7  (residues 1 to 540)
  AUTHORS   Shi,J. and Nelson,M.A.
  TITLE     The cyclin-dependent kinase 11 interacts with NOT2
  JOURNAL   Biochem Biophys Res Commun 334 (4), 1310-1316 (2005)
   PUBMED   16039607
  REMARK    GeneRIF: These findings suggest that CDK11 may contribute to
            apoptosis by regulating the activity of NOT2 independent of its
            kinase activity.
REFERENCE   8  (residues 1 to 540)
  AUTHORS   Zwartjes,C.G., Jayne,S., van den Berg,D.L. and Timmers,H.T.
  TITLE     Repression of promoter activity by CNOT2, a subunit of the
            transcription regulatory Ccr4-not complex
  JOURNAL   J Biol Chem 279 (12), 10848-10854 (2004)
   PUBMED   14707134
  REMARK    GeneRIF: major repression function of CNOT2 is localized in a
            specialized protein motif, the Not-Box
REFERENCE   9  (residues 1 to 540)
  AUTHORS   Denis,C.L. and Chen,J.
  TITLE     The CCR4-NOT complex plays diverse roles in mRNA metabolism
  JOURNAL   Prog Nucleic Acid Res Mol Biol 73, 221-250 (2003)
   PUBMED   12882519
  REMARK    Review article
REFERENCE   10 (residues 1 to 540)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092881.8 and AC025569.37.
            
            On Feb 21, 2023 this sequence version replaced XP_011536701.1.
            
            Summary: This gene encodes a subunit of the multi-component
            CCR4-NOT complex. The CCR4-NOT complex regulates mRNA synthesis and
            degradation and is also thought to be involved in mRNA splicing,
            transport and localization. The encoded protein interacts with
            histone deacetylases and functions as a repressor of polymerase II
            transcription. Alternatively spliced transcript variants have been
            observed for this gene. [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3525189.1,
                                           SRR14038193.707325.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..540
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..540
                     /product="CCR4-NOT transcription complex subunit 2 isoform
                     a"
                     /note="negative regulator of transcription 2;
                     CCR4-associated factor 2; CC chemokine receptor 4-negative
                     regulator of transcription 2"
                     /calculated_mol_wt=59607
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Region          96..126
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C5L3; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C5L3; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Region          276..342
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN8.1)"
     Region          396..519
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     Region          437..540
                     /region_name="Repressor domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN8.1)"
     CDS             1..540
                     /gene="CNOT2"
                     /gene_synonym="CDC36; HSPC131; IDNADFS; NOT2; NOT2H"
                     /coded_by="NM_001414651.1:545..2167"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="GeneID:4848"
                     /db_xref="HGNC:HGNC:7878"
                     /db_xref="MIM:604909"
ORIGIN      
        1 mvrtdghtls ekrnyqvtns mfgasrkkfv egvdsdyhde nmyysqssmf phrsekdmla
       61 spstsgqlsq fgaslygqqs alglpmrgms nntpqlnrsl sqgtqlpshv tpttgvptms
      121 lhtppspsrg ilpmnprnmm nhsqvgqgig ipsrtnsmss sglgspnrss psiicmpkqq
      181 psrqpftvns msgfgmnrnq afgmnnslss nifngtdgse nvtgldlsdf paladrnrre
      241 gsgnptplin plagrapyvg mvtkpaneqs qdfsihnedf palpgssykd ptssnddsks
      301 nlntsgktts stdgpkfpgd kssttqnnnq qkkgiqvlpd grvtnipqgm vtdqfgmigl
      361 ltfiraaetd pgmvhlalgs dlttlglnln spenlypkfa spwasspcrp qdidfhvpse
      421 yltnihirdk laaiklgryg edllfylyym nggdvlqlla avelfnrdwr yhkeervwit
      481 rapgmeptmk tntyergtyy ffdclnwrkv akefhleydk leerphlpst fnynpaqqaf
//
LOCUS       NP_001411258              65 aa            linear   PRI 21-NOV-2025
DEFINITION  protein cholesin isoform g [Homo sapiens].
ACCESSION   NP_001411258
VERSION     NP_001411258.1
DBSOURCE    REFSEQ: accession NM_001424329.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 65)
  AUTHORS   Ryk,A., Marcinkiewicz,A., Chrzanowski,J., Michalak,A.M., Drozdz,I.,
            Burzynski,J., Krejca,M. and Fendler,W.
  TITLE     Cholesin receptor signalling is active in cardiovascular
            system-associated adipose tissue and correlates with SGLT2i
            treatment in patients with diabetes
  JOURNAL   Cardiovasc Diabetol 23 (1), 211 (2024)
   PUBMED   38902687
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 65)
  AUTHORS   Hu,X., Chen,F., Jia,L., Long,A., Peng,Y., Li,X., Huang,J., Wei,X.,
            Fang,X., Gao,Z., Zhang,M., Liu,X., Chen,Y.G., Wang,Y., Zhang,H. and
            Wang,Y.
  TITLE     A gut-derived hormone regulates cholesterol metabolism
  JOURNAL   Cell 187 (7), 1685-1700 (2024)
   PUBMED   38503280
  REMARK    GeneRIF: A gut-derived hormone regulates cholesterol metabolism.
REFERENCE   3  (residues 1 to 65)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 65)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 65)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 65)
  AUTHORS   Willer,C.J., Schmidt,E.M., Sengupta,S., Peloso,G.M., Gustafsson,S.,
            Kanoni,S., Ganna,A., Chen,J., Buchkovich,M.L., Mora,S.,
            Beckmann,J.S., Bragg-Gresham,J.L., Chang,H.Y., Demirkan,A., Den
            Hertog,H.M., Do,R., Donnelly,L.A., Ehret,G.B., Esko,T.,
            Feitosa,M.F., Ferreira,T., Fischer,K., Fontanillas,P., Fraser,R.M.,
            Freitag,D.F., Gurdasani,D., Heikkila,K., Hypponen,E., Isaacs,A.,
            Jackson,A.U., Johansson,A., Johnson,T., Kaakinen,M., Kettunen,J.,
            Kleber,M.E., Li,X., Luan,J., Lyytikainen,L.P., Magnusson,P.K.E.,
            Mangino,M., Mihailov,E., Montasser,M.E., Muller-Nurasyid,M.,
            Nolte,I.M., O'Connell,J.R., Palmer,C.D., Perola,M., Petersen,A.K.,
            Sanna,S., Saxena,R., Service,S.K., Shah,S., Shungin,D., Sidore,C.,
            Song,C., Strawbridge,R.J., Surakka,I., Tanaka,T., Teslovich,T.M.,
            Thorleifsson,G., Van den Herik,E.G., Voight,B.F., Volcik,K.A.,
            Waite,L.L., Wong,A., Wu,Y., Zhang,W., Absher,D., Asiki,G.,
            Barroso,I., Been,L.F., Bolton,J.L., Bonnycastle,L.L., Brambilla,P.,
            Burnett,M.S., Cesana,G., Dimitriou,M., Doney,A.S.F., Doring,A.,
            Elliott,P., Epstein,S.E., Ingi Eyjolfsson,G., Gigante,B.,
            Goodarzi,M.O., Grallert,H., Gravito,M.L., Groves,C.J., Hallmans,G.,
            Hartikainen,A.L., Hayward,C., Hernandez,D., Hicks,A.A., Holm,H.,
            Hung,Y.J., Illig,T., Jones,M.R., Kaleebu,P., Kastelein,J.J.P.,
            Khaw,K.T., Kim,E., Klopp,N., Komulainen,P., Kumari,M.,
            Langenberg,C., Lehtimaki,T., Lin,S.Y., Lindstrom,J., Loos,R.J.F.,
            Mach,F., McArdle,W.L., Meisinger,C., Mitchell,B.D., Muller,G.,
            Nagaraja,R., Narisu,N., Nieminen,T.V.M., Nsubuga,R.N., Olafsson,I.,
            Ong,K.K., Palotie,A., Papamarkou,T., Pomilla,C., Pouta,A.,
            Rader,D.J., Reilly,M.P., Ridker,P.M., Rivadeneira,F., Rudan,I.,
            Ruokonen,A., Samani,N., Scharnagl,H., Seeley,J., Silander,K.,
            Stancakova,A., Stirrups,K., Swift,A.J., Tiret,L.,
            Uitterlinden,A.G., van Pelt,L.J., Vedantam,S., Wainwright,N.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilsgaard,T., Wilson,J.F.,
            Young,E.H., Zhao,J.H., Adair,L.S., Arveiler,D., Assimes,T.L.,
            Bandinelli,S., Bennett,F., Bochud,M., Boehm,B.O., Boomsma,D.I.,
            Borecki,I.B., Bornstein,S.R., Bovet,P., Burnier,M., Campbell,H.,
            Chakravarti,A., Chambers,J.C., Chen,Y.I., Collins,F.S.,
            Cooper,R.S., Danesh,J., Dedoussis,G., de Faire,U., Feranil,A.B.,
            Ferrieres,J., Ferrucci,L., Freimer,N.B., Gieger,C., Groop,L.C.,
            Gudnason,V., Gyllensten,U., Hamsten,A., Harris,T.B., Hingorani,A.,
            Hirschhorn,J.N., Hofman,A., Hovingh,G.K., Hsiung,C.A.,
            Humphries,S.E., Hunt,S.C., Hveem,K., Iribarren,C., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kaprio,J., Kesaniemi,A., Kivimaki,M.,
            Kooner,J.S., Koudstaal,P.J., Krauss,R.M., Kuh,D., Kuusisto,J.,
            Kyvik,K.O., Laakso,M., Lakka,T.A., Lind,L., Lindgren,C.M.,
            Martin,N.G., Marz,W., McCarthy,M.I., McKenzie,C.A., Meneton,P.,
            Metspalu,A., Moilanen,L., Morris,A.D., Munroe,P.B., Njolstad,I.,
            Pedersen,N.L., Power,C., Pramstaller,P.P., Price,J.F., Psaty,B.M.,
            Quertermous,T., Rauramaa,R., Saleheen,D., Salomaa,V.,
            Sanghera,D.K., Saramies,J., Schwarz,P.E.H., Sheu,W.H.,
            Shuldiner,A.R., Siegbahn,A., Spector,T.D., Stefansson,K.,
            Strachan,D.P., Tayo,B.O., Tremoli,E., Tuomilehto,J., Uusitupa,M.,
            van Duijn,C.M., Vollenweider,P., Wallentin,L., Wareham,N.J.,
            Whitfield,J.B., Wolffenbuttel,B.H.R., Ordovas,J.M., Boerwinkle,E.,
            Palmer,C.N.A., Thorsteinsdottir,U., Chasman,D.I., Rotter,J.I.,
            Franks,P.W., Ripatti,S., Cupples,L.A., Sandhu,M.S., Rich,S.S.,
            Boehnke,M., Deloukas,P., Kathiresan,S., Mohlke,K.L., Ingelsson,E.
            and Abecasis,G.R.
  CONSRTM   Global Lipids Genetics Consortium
  TITLE     Discovery and refinement of loci associated with lipid levels
  JOURNAL   Nat Genet 45 (11), 1274-1283 (2013)
   PUBMED   24097068
REFERENCE   7  (residues 1 to 65)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 65)
  AUTHORS   Yashin,A.I., Wu,D., Arbeev,K.G. and Ukraintseva,S.V.
  TITLE     Joint influence of small-effect genetic variants on human longevity
  JOURNAL   Aging (Albany NY) 2 (9), 612-620 (2010)
   PUBMED   20834067
REFERENCE   9  (residues 1 to 65)
  AUTHORS   Satoh,J., Obayashi,S., Misawa,T., Sumiyoshi,K., Oosumi,K. and
            Tabunoki,H.
  TITLE     Protein microarray analysis identifies human cellular prion protein
            interactors
  JOURNAL   Neuropathol Appl Neurobiol 35 (1), 16-35 (2009)
   PUBMED   18482256
REFERENCE   10 (residues 1 to 65)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073957.7.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4352444.505781.1,
                                           ERR4352441.274923.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..65
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..65
                     /product="protein cholesin isoform g"
                     /note="uncharacterized protein C7orf50; protein cholesin"
                     /calculated_mol_wt=7203
     Region          <7..36
                     /region_name="WKF"
                     /note="WKF domain; pfam10180"
                     /db_xref="CDD:462982"
     CDS             1..65
                     /gene="CHLSN"
                     /gene_synonym="C7orf50; YCR016W"
                     /coded_by="NM_001424329.1:375..572"
                     /note="isoform g is encoded by transcript variant 19"
                     /db_xref="GeneID:84310"
                     /db_xref="HGNC:HGNC:22421"
                     /db_xref="MIM:621174"
ORIGIN      
        1 mtvtrcvpde hfstllayle glqgrarelt vqkaealmre ldeegsdppl pgraqrirqv
       61 lqlls
//
LOCUS       NP_001401164             248 aa            linear   PRI 21-NOV-2025
DEFINITION  L-lactate dehydrogenase B chain isoform 5 [Homo sapiens].
ACCESSION   NP_001401164
VERSION     NP_001401164.1
DBSOURCE    REFSEQ: accession NM_001414235.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Zhang,P., Wan,Y., Ma,J., Gong,J., Zhong,Z., Cui,Y., Zhang,H.,
            Da,Y., Ma,J., Li,C., Liu,L., Gong,T., Tan,Y. and Zhang,C.
  TITLE     Epigenetic silencing of LDHB promotes hepatocellular carcinoma by
            remodeling the tumor microenvironment
  JOURNAL   Cancer Immunol Immunother 73 (7), 127 (2024)
   PUBMED   38739169
  REMARK    GeneRIF: Epigenetic silencing of LDHB promotes hepatocellular
            carcinoma by remodeling the tumor microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Shi,F., Zhang,G., Li,J., Shu,L., Yu,C., Ren,D., Zhang,Y. and
            Zheng,P.
  TITLE     Integrated analysis of single cell-RNA sequencing and Mendelian
            randomization identifies lactate dehydrogenase B as a target of
            melatonin in ischemic stroke
  JOURNAL   CNS Neurosci Ther 30 (5), e14741 (2024)
   PUBMED   38702940
  REMARK    GeneRIF: Integrated analysis of single cell-RNA sequencing and
            Mendelian randomization identifies lactate dehydrogenase B as a
            target of melatonin in ischemic stroke.
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Stiebler,A.C., Freitag,J., Schink,K.O., Stehlik,T., Tillmann,B.A.,
            Ast,J. and Bolker,M.
  TITLE     Ribosomal readthrough at a short UGA stop codon context triggers
            dual localization of metabolic enzymes in Fungi and animals
  JOURNAL   PLoS Genet 10 (10), e1004685 (2014)
   PUBMED   25340584
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Schueren,F., Lingner,T., George,R., Hofhuis,J., Dickel,C.,
            Gartner,J. and Thoms,S.
  TITLE     Peroxisomal lactate dehydrogenase is generated by translational
            readthrough in mammals
  JOURNAL   Elife 3, e03640 (2014)
   PUBMED   25247702
  REMARK    GeneRIF: The readthrough-extended lactate dehydrogenase subunit
            LDHBx can also co-import LDHA, the other LDH subunit, into
            peroxisomes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Takeno,T. and Li,S.S.
  TITLE     Structure of the human lactate dehydrogenase B gene
  JOURNAL   Biochem J 257 (3), 921-924 (1989)
   PUBMED   2930497
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Sakai,I., Sharief,F.S., Pan,Y.C. and Li,S.S.
  TITLE     The cDNA and protein sequences of human lactate dehydrogenase B
  JOURNAL   Biochem J 248 (3), 933-936 (1987)
   PUBMED   3435492
REFERENCE   9  (residues 1 to 248)
  AUTHORS   Law,M.L. and Kao,F.T.
  TITLE     Regional assignment of human genes TPI1, GAPDH, LDHB, SHMT, and
            PEPB on chromosome 12
  JOURNAL   Cytogenet Cell Genet 24 (2), 102-114 (1979)
   PUBMED   477403
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Rethore,M.O., Kaplan,J.C., Junien,C., Cruveiller,J., Dutrillaux,B.,
            Aurias,A., Carpentier,S., Lafourcade,J. and Lejeune.
  TITLE     [Increase of the LDH-B activity in a boy with 12p trisomy by
            malsegregation of a maternal translocation t(12;14) (q12;p11)]
  JOURNAL   Ann Genet 18 (2), 81-87 (1975)
   PUBMED   1081369
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010197.7.
            
            Summary: This gene encodes the B subunit of lactate dehydrogenase
            enzyme, which catalyzes the interconversion of pyruvate and lactate
            with concomitant interconversion of NADH and NAD+ in a
            post-glycolysis process. Alternatively spliced transcript variants
            have been found for this gene. Recent studies have shown that a
            C-terminally extended isoform is produced by use of an alternative
            in-frame translation termination codon via a stop codon readthrough
            mechanism, and that this isoform is localized in the peroxisomes.
            Mutations in this gene are associated with lactate dehydrogenase B
            deficiency. Pseudogenes have been identified on chromosomes X, 5
            and 13. [provided by RefSeq, Feb 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..248
                     /product="L-lactate dehydrogenase B chain isoform 5"
                     /EC_number="1.1.1.27"
                     /note="L-lactate dehydrogenase B chain; LDH heart subunit;
                     renal carcinoma antigen NY-REN-46; lactate dehydrogenase H
                     chain; epididymis secretory protein Li 281; testicular
                     secretory protein Li 25"
                     /calculated_mol_wt=26895
     Region          20..>246
                     /region_name="LDH_1"
                     /note="A subgroup of L-lactate dehydrogenases; cd05293"
                     /db_xref="CDD:133429"
     Site            order(30..32,53,55,58,96..100,137,139,162,166,194)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133429"
     Site            order(101,107,139,170,194,239)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133429"
     CDS             1..248
                     /gene="LDHB"
                     /gene_synonym="HEL-S-281; LDH-B; LDH-H; LDHBD; TRG-5"
                     /coded_by="NM_001414235.1:99..845"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:3945"
                     /db_xref="HGNC:HGNC:6541"
                     /db_xref="MIM:150100"
ORIGIN      
        1 matlkeklia pvaeeeatvp nnkitvvgvg qvgmacaisi lgksladela lvdvledklk
       61 gemmdlqhgs lflqtpkiva dkdysvtans kivvvtagvr qqegesrlnl vqrnvnvfkf
      121 iipqivkysp dciiivvsnp vdiltyvtwk lsglpkhrvi gsgcnldsar frylmaeklg
      181 ihpsschgwi lgehgdssva vwsgvnvagv slqelnpemg tdndsenwke vhkmvvergc
      241 malrmkss
//
LOCUS       NP_001400512             348 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001400512
VERSION     NP_001400512.1
DBSOURCE    REFSEQ: accession NM_001413583.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 348)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 348)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 348)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.110864.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..348
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 1 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=35211
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     mat_peptide     42..348
                     /product="Dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3. /id=PRO_0000215300"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
                     /calculated_mol_wt=35211
     Region          54..342
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            277..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            313..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     CDS             1..348
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413583.1:169..1215"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvsyih gssqaqfvae shiilvlnaa itmgmvllne
      301 aatskgdvgk rriiclvglg lvvfffsfll sifrskyhgy pysdldfe
//
LOCUS       NP_001424670             649 aa            linear   PRI 21-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 12 [Homo sapiens].
ACCESSION   NP_001424670
VERSION     NP_001424670.1
DBSOURCE    REFSEQ: accession NM_001437741.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 649)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 649)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 649)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 649)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 649)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 649)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 649)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 649)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008641.7.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4465401.1,
                                           SRR14038191.4214592.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..649
                     /product="TNFAIP3-interacting protein 1 isoform 12"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=73127
     Region          14..>149
                     /region_name="Speriolin_N"
                     /note="Speriolin N terminus; pfam15058"
                     /db_xref="CDD:434426"
     Region          61..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          94..412
                     /region_name="Interaction with Nef"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Region          <214..>251
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          252..283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          <298..>538
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          351..367
                     /region_name="Interaction with Shigella flexneri ipah9.8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          431..588
                     /region_name="Required for inhibitory activity of
                     TNF-induced NF-kappa-B activation. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          452..510
                     /region_name="Ubiquitin-binding domain (UBD)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Region          524..530
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            552
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17632516; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            571
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9WUU8; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            599
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     CDS             1..649
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001437741.1:192..2141"
                     /note="isoform 12 is encoded by transcript variant 20"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 megrgpyriy dpggsvpsge asaaferlvk ensrlkekmq gikmlgelle esqmeatrlr
       61 qkaeelvkdn ellpppspsl gsfdplaelt gkdsnvtasp tapacpsdkp apvqkppssg
      121 tssefevvtp eeqnspesss hanamalgpl predgnlmlh lqrlettlsv caeepdhgql
      181 fthlgrmale fnrlaskvhk neqrtsilqt lceqlrkene alkakldkgl eqrdqaaerl
      241 reenlelkkl lmsngnkega sgrpgspkme gtgkkavagq qqasvtagkv pevvalgaae
      301 kkvkmleqqr sellevnkqw dqhfrsmkqq yeqkitelrq kladlqkqvt dleaereqkq
      361 rdfdrkllla kskiemeetd keqltaeake lrqkvkylqd qlspltrqre yqekeiqrln
      421 kaleealsiq tppsspptaf gspegagall rkqelvtqne llkqqvkife edfqrersdr
      481 ermneekeel kkqveklqaq vtlsnaqlka fkdeekarea lrqqkrkaka sgeryhveph
      541 pehlcgaypy ayppmpamvp hhgfedwsqi ryppppmame hppplpnsrl fhlpeytwrl
      601 pcggvrnpnq ssqvmdppta rptepgtqlc rngassgrwr vslcrvskk
//
LOCUS       NP_001333244             550 aa            linear   PRI 21-NOV-2025
DEFINITION  autophagy-related protein 13 isoform a [Homo sapiens].
ACCESSION   NP_001333244
VERSION     NP_001333244.1
DBSOURCE    REFSEQ: accession NM_001346315.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Patel,A. and Faesen,A.C.
  TITLE     Metamorphosis by ATG13 and ATG101 in human autophagy initiation
  JOURNAL   Autophagy 20 (4), 968-969 (2024)
   PUBMED   37394799
  REMARK    GeneRIF: Metamorphosis by ATG13 and ATG101 in human autophagy
            initiation.
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Nguyen,A. and Faesen,A.C.
  TITLE     The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis
  JOURNAL   FEBS Lett 598 (1), 114-126 (2024)
   PUBMED   37567770
  REMARK    GeneRIF: The role of the HORMA domain proteins ATG13 and ATG101 in
            initiating autophagosome biogenesis.
            Review article
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Karabi,Z., Moradian,F. and Kheirabadi,M.
  TITLE     The effect of lactoferrin on ULK1 and ATG13 genes expression in
            breast cancer cell line MCF7 and bioinformatics studies of protein
            interaction between lactoferrin and the autophagy initiation
            complex
  JOURNAL   Cell Biochem Biophys 80 (4), 795-806 (2022)
   PUBMED   36169801
  REMARK    GeneRIF: The effect of lactoferrin on ULK1 and ATG13 genes
            expression in breast cancer cell line MCF7 and bioinformatics
            studies of protein interaction between lactoferrin and the
            autophagy initiation complex.
REFERENCE   5  (residues 1 to 550)
  AUTHORS   Gottschalk,G., Peterson,D., Knox,K., Maynard,M., Whelan,R.J. and
            Roy,A.
  TITLE     Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE)
  JOURNAL   Mol Cell Neurosci 120, 103731 (2022)
   PUBMED   35487443
  REMARK    GeneRIF: Elevated ATG13 in serum of patients with ME/CFS stimulates
            oxidative stress response in microglial cells via activation of
            receptor for advanced glycation end products (RAGE).
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Jung,C.H., Jun,C.B., Ro,S.H., Kim,Y.M., Otto,N.M., Cao,J., Kundu,M.
            and Kim,D.H.
  TITLE     ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy
            machinery
  JOURNAL   Mol Biol Cell 20 (7), 1992-2003 (2009)
   PUBMED   19225151
  REMARK    GeneRIF: The ULK-Atg13-FIP200 complexes are direct targets of mTOR
            and important regulators of autophagy in response to mTOR
            signaling.
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Hosokawa,N., Hara,T., Kaizuka,T., Kishi,C., Takamura,A., Miura,Y.,
            Iemura,S., Natsume,T., Takehana,K., Yamada,N., Guan,J.L., Oshiro,N.
            and Mizushima,N.
  TITLE     Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200
            complex required for autophagy
  JOURNAL   Mol Biol Cell 20 (7), 1981-1991 (2009)
   PUBMED   19211835
  REMARK    GeneRIF: mTORC1 suppresses autophagy through direct regulation of
            the approximately 3-MDa ULK1-Atg13-FIP200 complex.
REFERENCE   8  (residues 1 to 550)
  AUTHORS   Chan,E.Y., Longatti,A., McKnight,N.C. and Tooze,S.A.
  TITLE     Kinase-inactivated ULK proteins inhibit autophagy via their
            conserved C-terminal domains using an Atg13-independent mechanism
  JOURNAL   Mol Cell Biol 29 (1), 157-171 (2009)
   PUBMED   18936157
  REMARK    GeneRIF: The functions of ULK1 and ULK2 are controlled by
            autophosphorylation and conformational changes involving exposure
            of the C-terminal domain and interaction with the putative human
            homologue of Atg13.
            GeneRIF: The gene product is the functional homologue of yeast
            Atg13, and required for autophagy in mammalian cells.
REFERENCE   9  (residues 1 to 550)
  AUTHORS   Meijer,W.H., van der Klei,I.J., Veenhuis,M. and Kiel,J.A.
  TITLE     ATG genes involved in non-selective autophagy are conserved from
            yeast to man, but the selective Cvt and pexophagy pathways also
            require organism-specific genes
  JOURNAL   Autophagy 3 (2), 106-116 (2007)
   PUBMED   17204848
REFERENCE   10 (residues 1 to 550)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC127035.6 and AC115088.6.
            
            Summary: The protein encoded by this gene is an autophagy factor
            and a target of the TOR kinase signaling pathway. The encoded
            protein is essential for autophagosome formation and mitophagy.
            [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (11), as well as variants 3, 7-10,
            and 12, encodes isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.164997.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2142348,
                                           SAMEA2146982 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..550
                     /product="autophagy-related protein 13 isoform a"
                     /note="autophagy-related protein 13; ATG13 autophagy
                     related 13 homolog"
                     /calculated_mol_wt=60024
     Region          19..192
                     /region_name="ATG13"
                     /note="Autophagy-related protein 13; pfam10033"
                     /db_xref="CDD:431003"
     CDS             1..550
                     /gene="ATG13"
                     /gene_synonym="KIAA0652; PARATARG8"
                     /coded_by="NM_001346315.2:622..2274"
                     /note="isoform a is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS55760.1"
                     /db_xref="GeneID:9776"
                     /db_xref="HGNC:HGNC:29091"
                     /db_xref="MIM:615088"
ORIGIN      
        1 metdlnsqdr kdldkfikff alktvqvivq arlgekictr ssssptgsdw fnlaikdipe
       61 vtheakkala gqlpavgrsm cveislktse gdsmeleiwc lemnekcdke ikvsytvynr
      121 lslllkslla itrvtpayrl srkqgheyvi lyriyfgevq lsglgegfqt vrvgtvgtpv
      181 gtitlscayr inlafmstrq fertppimgi iidhfvdrpy pssspmhpcn yrtagedtgv
      241 iypsvedsqe vcttsfstsp psqcvftvtk ahfqtptpvv tdtlrvpmag lafshqlsss
      301 rlsyqpaalg vgsadlaypv vfaaglnath phqlmvpgke ggvplapnqp vhgtqadqer
      361 latctpsdrt hcaatpssse dtetvsnsse grasphdvle tifvrkvgaf vnkpinqvtl
      421 tsldipfamf apknleledt dpmvnppdsp etesplqgsl hsdgssggss gnthddfvmi
      481 dfkpafskdd ilpmdlgtfy refqnppqls slsidigaqs maedldslpe klavheknvr
      541 efdafvetlq
//
LOCUS       NP_001394760            1129 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 16 [Homo
            sapiens].
ACCESSION   NP_001394760 XP_047294908
VERSION     NP_001394760.1
DBSOURCE    REFSEQ: accession NM_001407831.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1129)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1129)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1129)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1129)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1129)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1129)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1129)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1129)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1129)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1129)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            On Jun 7, 2022 this sequence version replaced XP_047294908.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2763120.1,
                                           SRR14372079.3578112.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1129
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1129
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 16"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=127744
     Region          153..182
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          188..215
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          324..596
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          723..1129
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1129
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407831.1:575..3964"
                     /note="isoform 16 is encoded by transcript variant 16"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 mgakdatpvp cgrwakilek dkrtqqmrmq rlkaklqmpf qsgefkaltr rlqveprlls
       61 kqmagcledc trqapespwe eqlarllqea pgklsldveq apsgqhsqaq lsgqqqrlla
      121 ffkcclltdq lplahhllvv hhgqrqkrkl ltldmynavm lgwarqgafk elvyvlfmvk
      181 dagltpdlls yaaalqcmgr qdqdagtier cleqmsqegl klqalftavl lseedratvl
      241 kavhkvkptf slppqlpppv ntskllrdvy akdgrvsypk lhlplktlqc lfekqlhmel
      301 asrvcvvsve kptlpskevk harktlktlr dqwekalcra lretknrler evyegrfsly
      361 pflclldere vvrmllqvlq alpaqgesft tlarelsart fsrhvvqrqr vsgqvqalqn
      421 hyrkylclla sdaevpepcl prqyweelga pealreqpwp lpvqmelgkl laemlvqatq
      481 mpcsldkphr ssrlvpvlyh vysfrnvqqi gilkphpayv qllekaaept ltfeavdvpm
      541 lcpplpwtsp hsgafllspt klmrtvegat qhqelletcp ptalhgalda ltqlgncawr
      601 vngrvldlvl qlfqakgcpq lgvpappsea pqppeahlph saaparkael rrelahcqkv
      661 aremhslrae alyrlslaqh lrdrvfwlph nmdfrgrtyp cpphfnhlgs dvarallefa
      721 qgrplgphgl dwlkihlvnl tglkkreplr krlafaeevm ddildsadqp ltgrkwwmga
      781 eepwqtlacc mevanavras dpaayvshlp vhqdgscngl qhyaalgrds vgaasvnlep
      841 sdvpqdvysg vaaqvevfrr qdaqrgmrva qvlegfitrk vvkqtvmtvv ygvtryggrl
      901 qiekrlrels dfpqefvwea shylvrqvfk slqemfsgtr aiqhwltesa rlishmgsvv
      961 ewvtplgvpv iqpyrldskv kqigggiqsi tythngdisr kpntrkqkng fppnfihsld
     1021 sshmmltalh cyrspplchr kgltfvsvhd cywthaadvs vmnqvcreqf vrlhsepilq
     1081 dlsrflvkrf csepqkilea sqlketlqav pkpgafdleq vkrstyffs
//
LOCUS       NP_001393913             572 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform C [Homo sapiens].
ACCESSION   NP_001393913
VERSION     NP_001393913.1
DBSOURCE    REFSEQ: accession NM_001406984.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 572)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 572)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 572)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 572)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 572)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 572)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355388.30 and AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3837710.1,
                                           SRR14372080.3135959.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155371, SAMN03465404
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..572
                     /product="lamin isoform C"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=65004
     Region          1..130
                     /region_name="Interaction with MLIP.
                     /evidence=ECO:0000269|PubMed:21498514"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          1..33
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          30..386
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Site            32
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          34..70
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          71..80
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            78
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          81..218
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            108
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            114
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            123
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            135
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            155
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            171
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            180
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            201
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            208
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          219..242
                     /region_name="Linker 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          243..383
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          259..331
                     /region_name="Necessary and sufficient for the interaction
                     with IFFO1. /evidence=ECO:0000269|PubMed:31548606"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            265
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            266
                     /site_type="other"
                     /note="Heptad change of phase; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            270
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATR.
                     /evidence=ECO:0000269|PubMed:37832547; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            311
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            316
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            325
                     /site_type="other"
                     /note="Stutter. /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            330
                     /site_type="other"
                     /note="Heptad change of phase; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            341
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          384..442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:37788673,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATR.
                     /evidence=ECO:0000269|PubMed:37788673,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:24741066, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          417..422
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            417
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          434..541
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     Site            450
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            457
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            486
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48679; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48679; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            546
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     CDS             1..572
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406984.1:535..2253"
                     /note="isoform C is encoded by transcript variant 10"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 metpsqrrat rsgaqasstp lsptritrlq ekedlqelnd rlavyidrvr sletenaglr
       61 lriteseevv srevsgikaa yeaelgdark tldsvakera rlqlelskvr eefkelkarn
      121 tkkegdliaa qarlkdleal lnskeaalst alsekrtleg elhdlrgqva kleaalgeak
      181 kqlqdemlrr vdaenrlqtm keeldfqkni yseelretkr rhetrlveid ngkqrefesr
      241 ladalqelra qhedqveqyk kelektysak ldnarqsaer nsnlvgaahe elqqsririd
      301 slsaqlsqlq kqlaakeakl rdledslare rdtsrrllae keremaemra rmqqqldeyq
      361 elldiklald meihayrkll egeeerlrls psptsqrsrg rasshssqtq gggsvtkkrk
      421 lestesrssf sqhartsgrv aveevdeegk fvrlrnksne dqsmgnwqik rqngddpllt
      481 yrfppkftlk agqvvtiwaa gagathsppt dlvwkaqntw gcgnslrtal instgeevam
      541 rklvrsvtvv eddededgdd llhhhhvsgs rr
//
LOCUS       NP_001425132             718 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase tousled-like 2 isoform B [Homo
            sapiens].
ACCESSION   NP_001425132 XP_016879540 XP_054170776
VERSION     NP_001425132.1
DBSOURCE    REFSEQ: accession NM_001438203.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 718)
  AUTHORS   Liang,B., Yin,J.J., Zhang,S.N., Zhang,C., Hu,Z.L. and Wang,Y.
  TITLE     [Effect of TLK2 Expression Regulated by MiR-21 on Proliferation and
            Apoptosis of Acute Myeloid Leukemia Cells]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 32 (3), 658-662 (2024)
   PUBMED   38926950
  REMARK    GeneRIF: [Effect of TLK2 Expression Regulated by MiR-21 on
            Proliferation and Apoptosis of Acute Myeloid Leukemia Cells].
REFERENCE   3  (residues 1 to 718)
  AUTHORS   Ronald,S., Sunavala-Dossabhoy,G., Adams,L., Williams,B. and De
            Benedetti,A.
  TITLE     The expression of Tousled kinases in CaP cell lines and its
            relation to radiation response and DSB repair
  JOURNAL   Prostate 71 (13), 1367-1373 (2011)
   PUBMED   21647934
  REMARK    GeneRIF: TLKs appear to be intimately linked to the pattern of
            resistance to DNA damage, and specifically double-strand breaks.
REFERENCE   4  (residues 1 to 718)
  AUTHORS   Couch,F.J., Wang,X., Bamlet,W.R., de Andrade,M., Petersen,G.M. and
            McWilliams,R.R.
  TITLE     Association of mitotic regulation pathway polymorphisms with
            pancreatic cancer risk and outcome
  JOURNAL   Cancer Epidemiol Biomarkers Prev 19 (1), 251-257 (2010)
   PUBMED   20056645
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   5  (residues 1 to 718)
  AUTHORS   Pilyugin,M., Demmers,J., Verrijzer,C.P., Karch,F. and Moshkin,Y.M.
  TITLE     Phosphorylation-mediated control of histone chaperone ASF1 levels
            by Tousled-like kinases
  JOURNAL   PLoS One 4 (12), e8328 (2009)
   PUBMED   20016786
  REMARK    GeneRIF: ASF1 cellular levels are tightly controlled by distinct
            pathways and provide a molecular mechanism for post-translational
            regulation of dASF1 and hASF1a by TLK kinases.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 718)
  AUTHORS   Groth,A., Lukas,J., Nigg,E.A., Sillje,H.H., Wernstedt,C., Bartek,J.
            and Hansen,K.
  TITLE     Human Tousled like kinases are targeted by an ATM- and
            Chk1-dependent DNA damage checkpoint
  JOURNAL   EMBO J 22 (7), 1676-1687 (2003)
   PUBMED   12660173
REFERENCE   7  (residues 1 to 718)
  AUTHORS   Sillje,H.H. and Nigg,E.A.
  TITLE     Identification of human Asf1 chromatin assembly factors as
            substrates of Tousled-like kinases
  JOURNAL   Curr Biol 11 (13), 1068-1073 (2001)
   PUBMED   11470414
REFERENCE   8  (residues 1 to 718)
  AUTHORS   Sillje,H.H., Takahashi,K., Tanaka,K., Van Houwe,G. and Nigg,E.A.
  TITLE     Mammalian homologues of the plant Tousled gene code for
            cell-cycle-regulated kinases with maximal activities linked to
            ongoing DNA replication
  JOURNAL   EMBO J 18 (20), 5691-5702 (1999)
   PUBMED   10523312
REFERENCE   9  (residues 1 to 718)
  AUTHORS   Zhang,S., Xing,H. and Muslin,A.J.
  TITLE     Nuclear localization of protein kinase U-alpha is regulated by
            14-3-3
  JOURNAL   J Biol Chem 274 (35), 24865-24872 (1999)
   PUBMED   10455159
REFERENCE   10 (residues 1 to 718)
  AUTHORS   Yamakawa,A., Kameoka,Y., Hashimoto,K., Yoshitake,Y., Nishikawa,K.,
            Tanihara,K. and Date,T.
  TITLE     cDNA cloning and chromosomal mapping of genes encoding novel
            protein kinases termed PKU-alpha and PKU-beta, which have nuclear
            localization signal
  JOURNAL   Gene 202 (1-2), 193-201 (1997)
   PUBMED   9427565
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008026.7 and AC080038.5.
            
            On or before Apr 16, 2025 this sequence version replaced
            XP_016879540.1, XP_054170776.1.
            
            Summary: This gene encodes a nuclear serine/threonine kinase that
            was first identified in Arabidopsis. The encoded protein is thought
            to function in the regulation of chromatin assembly in the S phase
            of the cell cycle by regulating the levels of a histone H3/H4
            chaperone. This protein is associated with double-strand break
            repair of DNA damage caused by radiation. Pseudogenes of this gene
            are present on chromosomes 10 and 17. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3358192.1,
                                           SRR18074969.829571.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.2"
     Protein         1..718
                     /product="serine/threonine-protein kinase tousled-like 2
                     isoform B"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase tousled-like 2"
                     /calculated_mol_wt=82217
     Region          139..>378
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          401..709
                     /region_name="STKc_TLK2"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Tousled-Like Kinase 2; cd14041"
                     /db_xref="CDD:270943"
     Site            order(414..418,422,435,437,473,490..493,497,499,538,540,
                     542..543,545,559,562,585..588)
                     /site_type="active"
                     /db_xref="CDD:270943"
     Site            order(414..418,422,435,437,473,490..493,497,538,540,
                     542..543,545,559)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270943"
     Site            order(418,497,499,538,540,542,562,585..588)
                     /site_type="other"
                     /note="polypeptide substrate binding site"
                     /db_xref="CDD:270943"
     Site            order(558..564,585..588)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270943"
     CDS             1..718
                     /gene="TLK2"
                     /gene_synonym="HsHPK; MRD57; PKU-ALPHA"
                     /coded_by="NM_001438203.1:179..2335"
                     /note="isoform B is encoded by transcript variant K"
                     /db_xref="GeneID:11011"
                     /db_xref="HGNC:HGNC:11842"
                     /db_xref="MIM:608439"
ORIGIN      
        1 mmeelhsldp rrqellearf tgvgvskgpl nsessnqslc svgslsdkev etpekkqndq
       61 rnrkrkaepy etsqgkgtpr ghkisdyfer rveqplygld gsaakeatee qsalptlmsv
      121 mlakprldte qlaqrgaglc ftfvsaqqns psstgsgnte hscssqkqis iqhrqtqsdl
      181 tiekisalen sknsdlekke griddllran cdlrrqideq qkmlekyker lnrcvtmskk
      241 lliekskqek macrdksmqd rlrlghfttv rhgasfteqw tdgyafqnli kqqerinsqr
      301 eeierqrkml akrkppamgq appatneqkq rksktngaen etltlaeyhe qeeifklrlg
      361 hlkkeeaeiq aelerlervr nlhirelkri hnednsqfkd hptlndryll lhllgrggfs
      421 evykafdlte qryvavkihq lnknwrdekk enyhkhacre yrihkeldhp rivklydyfs
      481 ldtdsfctvl eycegndldf ylkqhklmse kearsiimqi vnalkylnei kppiihydlk
      541 pgnillvngt acgeikitdf glskimddds ynsvdgmelt sqgagtywyl ppecfvvgke
      601 ppkisnkvdv wsvgvifyqc lygrkpfghn qsqqdilqen tilkatevqf ppkpvvtpea
      661 kafirrclay rkedridvqq lacdpyllph irksvstssp agaaiastsg asnnsssn
//
LOCUS       NP_001400607             218 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 11 [Homo sapiens].
ACCESSION   NP_001400607
VERSION     NP_001400607.1
DBSOURCE    REFSEQ: accession NM_001413678.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 218)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 218)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 218)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1510678.1,
                                           SRR14038194.1937194.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..218
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 11"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=24401
     Region          <1..213
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     CDS             1..218
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413678.1:386..1042"
                     /note="isoform 11 is encoded by transcript variant 14"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mvdydegtdv fqqlnmnsap tfmhfppkgr pkradtfdlq rigfaaeqla kwiadrtdvh
       61 irvfrppnys gtialallvs lvggllylrr nnlefiynkt gwamvslciv famtsgqmwn
      121 hirgppyahk nphngqvsyi hgssqaqfva eshiilvlna aitmgmvlln eaatskgdvg
      181 krriiclvgl glvvfffsfl lsifrskyhg ypysflik
//
LOCUS       NP_001397772             490 aa            linear   PRI 21-NOV-2025
DEFINITION  rhotekin isoform d [Homo sapiens].
ACCESSION   NP_001397772 XP_005264535
VERSION     NP_001397772.1
DBSOURCE    REFSEQ: accession NM_001410843.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 490)
  AUTHORS   Li,B., Chen,P., Chang,Y., Qi,J., Fu,H. and Guo,H.
  TITLE     Let-7a inhibits tumor cell growth and metastasis by directly
            targeting RTKN in human colon cancer
  JOURNAL   Biochem Biophys Res Commun 478 (2), 739-745 (2016)
   PUBMED   27498032
  REMARK    GeneRIF: Let-7a microRNA inhibits tumor cell growth and metastasis
            by directly targeting RTKN in human colon cancer.
REFERENCE   6  (residues 1 to 490)
  AUTHORS   Katoh,H. and Negishi,M.
  TITLE     RhoG activates Rac1 by direct interaction with the Dock180-binding
            protein Elmo
  JOURNAL   Nature 424 (6947), 461-464 (2003)
   PUBMED   12879077
REFERENCE   7  (residues 1 to 490)
  AUTHORS   Sharfe,N., Freywald,A., Toro,A., Dadi,H. and Roifman,C.
  TITLE     Ephrin stimulation modulates T cell chemotaxis
  JOURNAL   Eur J Immunol 32 (12), 3745-3755 (2002)
   PUBMED   12516569
REFERENCE   8  (residues 1 to 490)
  AUTHORS   Reynaud,C., Fabre,S. and Jalinot,P.
  TITLE     The PDZ protein TIP-1 interacts with the Rho effector rhotekin and
            is involved in Rho signaling to the serum response element
  JOURNAL   J Biol Chem 275 (43), 33962-33968 (2000)
   PUBMED   10940294
REFERENCE   9  (residues 1 to 490)
  AUTHORS   Fu,Q., Yu,L., Liu,Q., Zhang,J., Zhang,H. and Zhao,S.
  TITLE     Molecular cloning, expression characterization, and mapping of a
            novel putative inhibitor of rho GTPase activity, RTKN, to
            D2S145-D2S286
  JOURNAL   Genomics 66 (3), 328-332 (2000)
   PUBMED   10873388
REFERENCE   10 (residues 1 to 490)
  AUTHORS   Jang,W., Weber,J.S., Harkins,E.B. and Meisler,M.H.
  TITLE     Localization of the rhotekin gene RTKN on the physical maps of
            mouse chromosome 6 and human chromosome 2p13 and exclusion as a
            candidate for mnd2 and LGMD2B
  JOURNAL   Genomics 40 (3), 506-507 (1997)
   PUBMED   9073523
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005041.2.
            
            On Aug 16, 2022 this sequence version replaced XP_005264535.1.
            
            Summary: This gene encodes a scaffold protein that interacts with
            GTP-bound Rho proteins. Binding of this protein inhibits the GTPase
            activity of Rho proteins. This protein may interfere with the
            conversion of active, GTP-bound Rho to the inactive GDP-bound form
            by RhoGAP. Rho proteins regulate many important cellular processes,
            including cytokinesis, transcription, smooth muscle contraction,
            cell growth and transformation. Dysregulation of the Rho signal
            transduction pathway has been implicated in many forms of cancer.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.120353.1,
                                           SRR1660803.80256.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..490
                     /product="rhotekin isoform d"
                     /calculated_mol_wt=54401
     Site            14
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9BST9.2)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9BST9.2)"
     Region          37..91
                     /region_name="Hr1"
                     /note="Rho effector or protein kinase C-related kinase
                     homology region 1 homologues; smart00742"
                     /db_xref="CDD:128981"
     Region          96..116
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BST9.2)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9BST9.2)"
     Region          117..270
                     /region_name="Anillin"
                     /note="Cell division protein anillin; pfam08174"
                     /db_xref="CDD:462393"
     Site            230
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8C6B2; propagated from
                     UniProtKB/Swiss-Prot (Q9BST9.2)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BST9.2)"
     Region          309..419
                     /region_name="PH_rhotekin2"
                     /note="Anillin Pleckstrin homology (PH) domain; cd13249"
                     /db_xref="CDD:270069"
     CDS             1..490
                     /gene="RTKN"
                     /gene_synonym="RTKN-1"
                     /coded_by="NM_001410843.1:122..1594"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS92783.1"
                     /db_xref="GeneID:6242"
                     /db_xref="HGNC:HGNC:10466"
                     /db_xref="MIM:602288"
ORIGIN      
        1 mfsrnhrsrv tvargsalem efkrgrfrls lfsdlpedte lqrkldheir mregacklla
       61 acsqreqale atksllvcns rilsymgelq rrkeaqvlgk tsrrpsdsgp paerspcrgr
      121 vcisdlripl mwkdteyfkn kgdlhrwavf lllqlgehiq dtemilvdrt ltdisfqsnv
      181 lfaeagpdfe lrlelygacv eeegaltggp krlatklsss lgrssgrrvr asldsaggsg
      241 sspillptpv vggpryhlla httltlaavq dgfrthdltl asheenpawl plygsvccrl
      301 aaqplcmtqp tasgtlrvqq agemqnwaqv hgvlkgtnlf cyrqpedadt geeplltiav
      361 nketrvrage ldqalgrpft lsisnqygdd evthtlqtes realqswmea lwqlffdmsq
      421 wkqccdeimk ietpaprkpp qalakqgsly hemvlsepva pggpgeglll qdnaisteiq
      481 allssyysdr
//
LOCUS       NP_001397779            1349 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger protein 827 isoform 3 [Homo sapiens].
ACCESSION   NP_001397779 XP_011529936
VERSION     NP_001397779.1
DBSOURCE    REFSEQ: accession NM_001410850.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1349)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1349)
  AUTHORS   Kim,K.Y., Kim,J.O., Kim,Y.S., Choi,J.E., Park,J.M., Han,K.,
            Park,D.H., Park,Y.C., Kim,B.T. and Hong,K.W.
  TITLE     Genome-wide association of individual vulnerability with
            alcohol-associated liver disease: A Korean genome and epidemiology
            study
  JOURNAL   Hepatology 75 (2), 391-402 (2022)
   PUBMED   34387878
  REMARK    GeneRIF: Genome-wide association of individual vulnerability with
            alcohol-associated liver disease: A Korean genome and epidemiology
            study.
REFERENCE   3  (residues 1 to 1349)
  AUTHORS   Hollensen,A.K., Thomsen,H.S., Lloret-Llinares,M., Kamstrup,A.B.,
            Jensen,J.M., Luckmann,M., Birkmose,N., Palmfeldt,J., Jensen,T.H.,
            Hansen,T.B. and Damgaard,C.K.
  TITLE     circZNF827 nucleates a transcription inhibitory complex to balance
            neuronal differentiation
  JOURNAL   Elife 9, e58478 (2020)
   PUBMED   33174841
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1349)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1349)
  AUTHORS   Yang,S.F., Sun,A.A., Shi,Y., Li,F. and Pickett,H.A.
  TITLE     Structural and functional characterization of the RBBP4-ZNF827
            interaction and its role in NuRD recruitment to telomeres
  JOURNAL   Biochem J 475 (16), 2667-2679 (2018)
   PUBMED   30045876
  REMARK    GeneRIF: RBBP4 forms a negatively charged channel that binds to
            ZNF827 through a network of electrostatic interactions.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1349)
  AUTHORS   Kennedy,R.B., Ovsyannikova,I.G., Pankratz,V.S., Haralambieva,I.H.,
            Vierkant,R.A. and Poland,G.A.
  TITLE     Genome-wide analysis of polymorphisms associated with cytokine
            responses in smallpox vaccine recipients
  JOURNAL   Hum Genet 131 (9), 1403-1421 (2012)
   PUBMED   22610502
REFERENCE   7  (residues 1 to 1349)
  AUTHORS   Chambers,J.C., Zhang,W., Sehmi,J., Li,X., Wass,M.N., Van der
            Harst,P., Holm,H., Sanna,S., Kavousi,M., Baumeister,S.E.,
            Coin,L.J., Deng,G., Gieger,C., Heard-Costa,N.L., Hottenga,J.J.,
            Kuhnel,B., Kumar,V., Lagou,V., Liang,L., Luan,J., Vidal,P.M., Mateo
            Leach,I., O'Reilly,P.F., Peden,J.F., Rahmioglu,N., Soininen,P.,
            Speliotes,E.K., Yuan,X., Thorleifsson,G., Alizadeh,B.Z.,
            Atwood,L.D., Borecki,I.B., Brown,M.J., Charoen,P., Cucca,F.,
            Das,D., de Geus,E.J., Dixon,A.L., Doring,A., Ehret,G.,
            Eyjolfsson,G.I., Farrall,M., Forouhi,N.G., Friedrich,N.,
            Goessling,W., Gudbjartsson,D.F., Harris,T.B., Hartikainen,A.L.,
            Heath,S., Hirschfield,G.M., Hofman,A., Homuth,G., Hypponen,E.,
            Janssen,H.L., Johnson,T., Kangas,A.J., Kema,I.P., Kuhn,J.P.,
            Lai,S., Lathrop,M., Lerch,M.M., Li,Y., Liang,T.J., Lin,J.P.,
            Loos,R.J., Martin,N.G., Moffatt,M.F., Montgomery,G.W., Munroe,P.B.,
            Musunuru,K., Nakamura,Y., O'Donnell,C.J., Olafsson,I.,
            Penninx,B.W., Pouta,A., Prins,B.P., Prokopenko,I., Puls,R.,
            Ruokonen,A., Savolainen,M.J., Schlessinger,D., Schouten,J.N.,
            Seedorf,U., Sen-Chowdhry,S., Siminovitch,K.A., Smit,J.H.,
            Spector,T.D., Tan,W., Teslovich,T.M., Tukiainen,T.,
            Uitterlinden,A.G., Van der Klauw,M.M., Vasan,R.S., Wallace,C.,
            Wallaschofski,H., Wichmann,H.E., Willemsen,G., Wurtz,P., Xu,C.,
            Yerges-Armstrong,L.M., Abecasis,G.R., Ahmadi,K.R., Boomsma,D.I.,
            Caulfield,M., Cookson,W.O., van Duijn,C.M., Froguel,P., Matsuda,K.,
            McCarthy,M.I., Meisinger,C., Mooser,V., Pietilainen,K.H.,
            Schumann,G., Snieder,H., Sternberg,M.J., Stolk,R.P., Thomas,H.C.,
            Thorsteinsdottir,U., Uda,M., Waeber,G., Wareham,N.J.,
            Waterworth,D.M., Watkins,H., Whitfield,J.B., Witteman,J.C.,
            Wolffenbuttel,B.H., Fox,C.S., Ala-Korpela,M., Stefansson,K.,
            Vollenweider,P., Volzke,H., Schadt,E.E., Scott,J., Jarvelin,M.R.,
            Elliott,P. and Kooner,J.S.
  CONSRTM   Alcohol Genome-wide Association (AlcGen) Consortium; Diabetes
            Genetics Replication and Meta-analyses (DIAGRAM+) Study; Genetic
            Investigation of Anthropometric Traits (GIANT) Consortium; Global
            Lipids Genetics Consortium; Genetics of Liver Disease (GOLD)
            Consortium; International Consortium for Blood Pressure
            (ICBP-GWAS); Meta-analyses of Glucose and Insulin-Related Traits
            Consortium (MAGIC)
  TITLE     Genome-wide association study identifies loci influencing
            concentrations of liver enzymes in plasma
  JOURNAL   Nat Genet 43 (11), 1131-1138 (2011)
   PUBMED   22001757
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1349)
  AUTHORS   Kim,Y.J., Go,M.J., Hu,C., Hong,C.B., Kim,Y.K., Lee,J.Y.,
            Hwang,J.Y., Oh,J.H., Kim,D.J., Kim,N.H., Kim,S., Hong,E.J.,
            Kim,J.H., Min,H., Kim,Y., Zhang,R., Jia,W., Okada,Y., Takahashi,A.,
            Kubo,M., Tanaka,T., Kamatani,N., Matsuda,K., Park,T., Oh,B.,
            Kimm,K., Kang,D., Shin,C., Cho,N.H., Kim,H.L., Han,B.G., Lee,J.Y.
            and Cho,Y.S.
  CONSRTM   MAGIC consortium
  TITLE     Large-scale genome-wide association studies in East Asians identify
            new genetic loci influencing metabolic traits
  JOURNAL   Nat Genet 43 (10), 990-995 (2011)
   PUBMED   21909109
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1349)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 1349)
  AUTHORS   Bubb,K.L., Bovee,D., Buckley,D., Haugen,E., Kibukawa,M.,
            Paddock,M., Palmieri,A., Subramanian,S., Zhou,Y., Kaul,R., Green,P.
            and Olson,M.V.
  TITLE     Scan of human genome reveals no new Loci under ancient balancing
            selection
  JOURNAL   Genetics 173 (4), 2165-2177 (2006)
   PUBMED   16751668
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104791.3 and AC107212.5.
            
            On Aug 16, 2022 this sequence version replaced XP_011529936.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.25880.1,
                                           SRR18074969.2269568.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1349
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.21-q31.22"
     Protein         1..1349
                     /product="zinc finger protein 827 isoform 3"
                     /calculated_mol_wt=149211
     Region          1..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17R98.1)"
     Region          1..14
                     /region_name="Mediates direct interaction with RBBP4.
                     /evidence=ECO:0000269|PubMed:30045876"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17R98.1)"
     Region          3..5
                     /region_name="RRK motif, mediates NuRD recruitment to
                     telomeres. /evidence=ECO:0000269|PubMed:25150861"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17R98.1)"
     Region          259..278
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17R98.1)"
     Region          307..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17R98.1)"
     Region          355..>443
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          376..396
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(381,383,385,387..388,391..392,395,409,411,415..416,
                     419..420,423,440,442,444,446..447,450..451,454)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          404..424
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          435..455
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          819..839
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Site            order(824,826,828,830..831,834..835,838,852,854..856,
                     858..859,863,866)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275370"
     Region          847..867
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          947..996
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17R98.1)"
     Region          1021..1041
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(1026,1028,1030,1032..1033,1036..1037,1040,1054,1056,
                     1060..1061,1064..1065,1068,1083,1085,1087,1089..1090,
                     1093..1094,1097)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          1049..1069
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1078..1098
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1105..1125
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(1110,1112,1114,1116..1117,1120..1121,1124,1138,1140,
                     1144..1145,1148..1149,1152,1166,1168,1170,1172..1173,
                     1176..1177,1180)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          1131..1155
                     /region_name="zf-H2C2_5"
                     /note="C2H2-type zinc-finger domain; pfam13909"
                     /db_xref="CDD:404746"
     Region          1133..1153
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1146..1170
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          1161..1180
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1190..1210
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..1349
                     /gene="ZNF827"
                     /coded_by="NM_001410850.1:417..4466"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS93645.1"
                     /db_xref="GeneID:152485"
                     /db_xref="HGNC:HGNC:27193"
                     /db_xref="MIM:617962"
ORIGIN      
        1 mprrkqeqpk rlpshvsrqe eaegelsege hwygnssetp seasygevqe nyklsledri
       61 qeqstspdts lgsttpssht lelvaldsev lrdslqcqdh lspgvsslcd ddpgsnkpls
      121 snlrrlleag slkldaaata ngrvespvnv gsnlsfspps hhaqqlsvla rklaekqeqn
      181 dqytpsnrfi wnqgkwlpns tttcslspds ailklkaaan avlqdksltr teetmrfesf
      241 sspfssqsas stlaalskkv sersltpgqe hpppassfls lasmtssaal lkevaaraag
      301 sllaekssll pedplpppps ekkpekvtpp pppppppppp pppqslelll lpvpkgrvsk
      361 psnsaseees gkpfqcpicg lvikrksywk rhmvihtglk shqcplcpfr carkdnlksh
      421 mkvhqhqdrg etfqcqlcpf tssrhfslkl hmrchqhflr teakvkeeip dpdvkgsphl
      481 sdsaclgqqr egggtelvgt mmtsntpert sqggagvspl lvkeepkedn glptsftlna
      541 adrpanhtkl kdpseyvans asalfsqdis vkmasdflmk lsaanqkepm nlnfkvkeep
      601 kegeslsttl prssyvfspe sevsapgvse dalkpqegkg svlrrdvsvk aasellmkls
      661 aesyketqmv kikeepmevd iqdshvsisp srnvgystli grekteplqk mpegrvpper
      721 nlfsqdisvk masellfqls ekvskehnht kentirttts pffsedtfrq spftsnskel
      781 lpsdsvlhgr isapetekiv leagnglpsw kfndqlfpcd vcgkvfgrqq tlsrhlslht
      841 eerkykchlc pyaakcranl nqhltvhsvk lvstdtediv savtsegsdg kkhpyyysch
      901 vcgfetelnv qfvshmslhv dkeqwmfsic ctacdfvtme eaeikthigt khtgedrktp
      961 sesnspssss lsalsdsans kddsdgsqkn kggnnllvis vmpgsqpsln seekpekgfe
     1021 cvfcnfvckt knmferhlqi hlitrmfecd vchkfmktpe qllehkkcht vptgglkcpf
     1081 ciystnrpaa mechlkthyk meykcricqt vkanqlelet htrehrlgnh ykcdqcgyls
     1141 ktankliehv rvhtgerpfh cdqcsysckr kdnlnlhkkl khaprqtfsc eeclfktthp
     1201 fvfsrhvkkh qsgdcpeedk kglcpapkep agpgapllvv gssrnllspl svmsasqalq
     1261 tvalsaahgs ssepnlalka lafngsplrf dkyrnsdfah lipltmlypk nhldltfhpp
     1321 rpqtappsip spkhsflayl glreraetv
//
LOCUS       NP_001397756             903 aa            linear   PRI 21-NOV-2025
DEFINITION  cytokine receptor common subunit beta isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001397756 XP_005261397
VERSION     NP_001397756.1
DBSOURCE    REFSEQ: accession NM_001410827.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 903)
  AUTHORS   Charlet,A., Kappenstein,M., Keye,P., Klasener,K., Endres,C.,
            Poggio,T., Gorantla,S.P., Kreutmair,S., Sanger,J., Illert,A.L.,
            Miething,C., Reth,M., Duyster,J., Rummelt,C. and von Bubnoff,N.
  TITLE     The IL-3, IL-5, and GM-CSF common receptor beta chain mediates
            oncogenic activity of FLT3-ITD-positive AML
  JOURNAL   Leukemia 36 (3), 701-711 (2022)
   PUBMED   34750506
  REMARK    GeneRIF: The IL-3, IL-5, and GM-CSF common receptor beta chain
            mediates oncogenic activity of FLT3-ITD-positive AML.
REFERENCE   2  (residues 1 to 903)
  AUTHORS   Rashid,M., Ali,R., Almuzzaini,B., Song,H., AlHallaj,A.,
            Abdulkarim,A.A., Mohamed Baz,O., Al Zahrani,H., Mustafa Sabeena,M.,
            Alharbi,W., Hussein,M. and Boudjelal,M.
  TITLE     Discovery of a novel potentially transforming somatic mutation in
            CSF2RB gene in breast cancer
  JOURNAL   Cancer Med 10 (22), 8138-8150 (2021)
   PUBMED   34729943
  REMARK    GeneRIF: Discovery of a novel potentially transforming somatic
            mutation in CSF2RB gene in breast cancer.
REFERENCE   3  (residues 1 to 903)
  AUTHORS   Benard,A., Jacobsen,A., Brunner,M., Krautz,C., Klosch,B.,
            Swierzy,I., Naschberger,E., Podolska,M.J., Kouhestani,D., David,P.,
            Birkholz,T., Castellanos,I., Trufa,D., Sirbu,H., Vetter,M.,
            Kremer,A.E., Hildner,K., Hecker,A., Edinger,F., Tenbusch,M.,
            Muhl-Zurbes,P., Steinkasserer,A., Richter,E., Streeck,H.,
            Berger,M.M., Brenner,T., Weigand,M.A., Swirski,F.K., Schett,G.,
            Grutzmann,R. and Weber,G.F.
  TITLE     Interleukin-3 is a predictive marker for severity and outcome
            during SARS-CoV-2 infections
  JOURNAL   Nat Commun 12 (1), 1112 (2021)
   PUBMED   33602937
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 903)
  AUTHORS   Sakaue,S., Yamaguchi,E., Inoue,Y., Takahashi,M., Hirata,J.,
            Suzuki,K., Ito,S., Arai,T., Hirose,M., Tanino,Y., Nikaido,T.,
            Ichiwata,T., Ohkouchi,S., Hirano,T., Takada,T., Miyawaki,S.,
            Dofuku,S., Maeda,Y., Nii,T., Kishikawa,T., Ogawa,K., Masuda,T.,
            Yamamoto,K., Sonehara,K., Tazawa,R., Morimoto,K., Takaki,M.,
            Konno,S., Suzuki,M., Tomii,K., Nakagawa,A., Handa,T., Tanizawa,K.,
            Ishii,H., Ishida,M., Kato,T., Takeda,N., Yokomura,K., Matsui,T.,
            Watanabe,M., Inoue,H., Imaizumi,K., Goto,Y., Kida,H., Fujisawa,T.,
            Suda,T., Yamada,T., Satake,Y., Ibata,H., Hizawa,N., Mochizuki,H.,
            Kumanogoh,A., Matsuda,F., Nakata,K., Hirota,T., Tamari,M. and
            Okada,Y.
  TITLE     Genetic determinants of risk in autoimmune pulmonary alveolar
            proteinosis
  JOURNAL   Nat Commun 12 (1), 1032 (2021)
   PUBMED   33589587
  REMARK    GeneRIF: Genetic determinants of risk in autoimmune pulmonary
            alveolar proteinosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 903)
  AUTHORS   Schulte,V., Sipol,A., Burdach,S. and Rieger-Fackeldey,E.
  TITLE     The Truncated Splice Variant of the
            Granulocyte-Macrophage-Colony-Stimulating Factor Receptor beta-
            Chain in Peripheral Blood Serves as Severity Biomarker of
            Respiratory Failure in Newborns
  JOURNAL   Neonatology 118 (2), 187-193 (2021)
   PUBMED   33784678
  REMARK    GeneRIF: The Truncated Splice Variant of the
            Granulocyte-Macrophage-Colony-Stimulating Factor Receptor beta-
            Chain in Peripheral Blood Serves as Severity Biomarker of
            Respiratory Failure in Newborns.
REFERENCE   6  (residues 1 to 903)
  AUTHORS   Sakamaki,K., Miyajima,I., Kitamura,T. and Miyajima,A.
  TITLE     Critical cytoplasmic domains of the common beta subunit of the
            human GM-CSF, IL-3 and IL-5 receptors for growth signal
            transduction and tyrosine phosphorylation
  JOURNAL   EMBO J 11 (10), 3541-3549 (1992)
   PUBMED   1396555
REFERENCE   7  (residues 1 to 903)
  AUTHORS   Torigoe,T., O'Connor,R., Santoli,D. and Reed,J.C.
  TITLE     Interleukin-3 regulates the activity of the LYN protein-tyrosine
            kinase in myeloid-committed leukemic cell lines
  JOURNAL   Blood 80 (3), 617-624 (1992)
   PUBMED   1638019
REFERENCE   8  (residues 1 to 903)
  AUTHORS   Tavernier,J., Tuypens,T., Plaetinck,G., Verhee,A., Fiers,W. and
            Devos,R.
  TITLE     Molecular basis of the membrane-anchored and two soluble isoforms
            of the human interleukin 5 receptor alpha subunit
  JOURNAL   Proc Natl Acad Sci U S A 89 (15), 7041-7045 (1992)
   PUBMED   1495999
REFERENCE   9  (residues 1 to 903)
  AUTHORS   Shen,Y., Baker,E., Callen,D.F., Sutherland,G.R., Willson,T.A.,
            Rakar,S. and Gough,N.M.
  TITLE     Localization of the human GM-CSF receptor beta chain gene (CSF2RB)
            to chromosome 22q12.2-->q13.1
  JOURNAL   Cytogenet Cell Genet 61 (3), 175-177 (1992)
   PUBMED   1424804
REFERENCE   10 (residues 1 to 903)
  AUTHORS   Hayashida,K., Kitamura,T., Gorman,D.M., Arai,K., Yokota,T. and
            Miyajima,A.
  TITLE     Molecular cloning of a second subunit of the receptor for human
            granulocyte-macrophage colony-stimulating factor (GM-CSF):
            reconstitution of a high-affinity GM-CSF receptor
  JOURNAL   Proc Natl Acad Sci U S A 87 (24), 9655-9659 (1990)
   PUBMED   1702217
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL008637.1 and AL133392.1.
            
            On Aug 16, 2022 this sequence version replaced XP_005261397.1.
            
            Summary: The protein encoded by this gene is the common beta chain
            of the high affinity receptor for IL-3, IL-5 and CSF. Defects in
            this gene have been reported to be associated with protein alveolar
            proteinosis (PAP). [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2883588.1,
                                           SRR14038194.794015.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..903
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..903
                     /product="cytokine receptor common subunit beta isoform 1
                     precursor"
                     /note="interleukin 3 receptor/granulocyte-macrophage
                     colony stimulating factor 3 receptor, beta (high
                     affinity); cytokine receptor common subunit beta;
                     GM-CSF/IL-3/IL-5 receptor common beta-chain;
                     colony-stimulating factor-2 receptor, beta, low-affinity;
                     colony stimulating factor 2 receptor, beta, low-affinity
                     (granulocyte-macrophage); GM-CSF/IL-3/IL-5 receptor common
                     beta subunit; beta common cytokine receptor; beta-GM-CSF
                     receptor; colony stimulating factor 2 receptor beta common
                     subunit"
                     /calculated_mol_wt=95604
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2390
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16754968,
                     ECO:0000269|PubMed:18692472; propagated from
                     UniProtKB/Swiss-Prot (P32927.2)"
     Region          133..233
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(133,204,219)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16754968,
                     ECO:0000269|PubMed:18692472; propagated from
                     UniProtKB/Swiss-Prot (P32927.2)"
     Site            order(226..227,229..230)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          347..442
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            352
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32927.2)"
     Region          431..435
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Site            order(431..432,434..435)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            450..466
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Region          480..488
                     /region_name="Box 1 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Region          504..523
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Region          538..636
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Region          <554..873
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          654..818
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Site            772
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P26955; propagated from
                     UniProtKB/Swiss-Prot (P32927.2)"
     Region          836..855
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     CDS             1..903
                     /gene="CSF2RB"
                     /gene_synonym="betaGMR; CD131; CDw131; IL3RB; IL5RB;
                     SMDP5"
                     /coded_by="NM_001410827.1:223..2934"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS93160.1"
                     /db_xref="GeneID:1439"
                     /db_xref="HGNC:HGNC:2436"
                     /db_xref="MIM:138981"
ORIGIN      
        1 mvlaqgllsm allalcwers lagaeetipl qtlrcyndyt shitcrwadt qdaqrlvnvt
       61 lirrvnedll epvscdlsdd mpwsacphpr cvprrcvipc qsfvvtdvdy fsfqpdrplg
      121 trltvtltqh vqppeprdlq istdqdhfll twsvalgspq shwlspgdle fevvykrlqd
      181 swedaaills ntsqatlgpe hlmpsstyva rvrtrlapgs rlsgrpskws pevcwdsqpg
      241 deaqpqnlec ffdgaavlsc swevrkevas svsfglfykp spdagsavll reeecspvlr
      301 eglgslhtrh hcqipvpdpa thgqyivsvq prraekhiks svniqmapps lnvtkdgdsy
      361 slrwetmkmr yehidhtfei qyrkdtatwk dsktetlqna hsmalpalep strywarvrv
      421 rtsrtgyngi wsewsearsw dtesvlpmwv laliviflti avllalrfcg iygyrlrrkw
      481 eekipnpsks hlfqngsael wppgsmsaft sgspphqgpw gsrfpelegv fpvgfgdsev
      541 spltiedpkh vcdppsgpdt tpaasdlpte qppspqpgpp aashtpekqa ssfdfngpyl
      601 gpphsrslpd ilgqpeppqe ggsqkspppg sleylclpag gqvqlvplaq amgpgqavev
      661 errpsqgaag spslesgggp appalgprvg gqdqkdspva ipmssgdted pgvasgyvss
      721 adlvftpnsg assvslvpsl glpsdqtpsl cpglasgppg apgpvksgfe gyvelppieg
      781 rsprsprnnp vppeakspvl npgerpadvs ptspqpegll vlqqvgdycf lpglgpgpls
      841 lrskpsspgp gpeiknldqa fqvkkppgqa vpqvpviqlf kalkqqdyls lppwevnkpg
      901 evc
//
LOCUS       NP_001394399            2560 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform m [Homo sapiens].
ACCESSION   NP_001394399
VERSION     NP_001394399.1
DBSOURCE    REFSEQ: accession NM_001407470.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2560)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2560)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2560)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2560)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2560)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2560)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2560)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2560)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2560)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2560)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1896267.1,
                                           SRR14038192.3918259.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158188, SAMEA2161674
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2560
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2560
                     /product="adenomatous polyposis coli protein isoform m"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=279409
     Region          57..109
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          110..183
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          182..225
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(216,220,224,259,263,267,303,307,311)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          229..270
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          233..270
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          277..312
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          320..361
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          366..406
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          370..404
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          408..448
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          412..448
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          449..736
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          753..852
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          974..>991
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1000..1085
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1008..1418
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1088..1110
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1354..1377
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1379..1432
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1433..1454
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1463..1556
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1590..1664
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1750..1769
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1940..2285
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2387..2560
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2560
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407470.1:1439..9121"
                     /note="isoform m is encoded by transcript variant 33"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 mdhetasvls sssthsaprr ltshlgtkve mvysllsmlg thdkddmsrt llamsssqds
       61 cismrqsgcl plliqllhgn dkdsvllgns rgskearara saalhniihs qpddkrgrre
      121 irvlhlleqi raycetcwew qeahepgmdq dknpmpapve hqicpavcvl mklsfdeehr
      181 hamnelgglq aiaellqvdc emygltndhy sitlrryagm altnltfgdv ankatlcsmk
      241 gcmralvaql ksesedlqqv iasvlrnlsw radvnskktl revgsvkalm ecalevkkes
      301 tlksvlsalw nlsahctenk adicavdgal aflvgtltyr sqtntlaiie sgggilrnvs
      361 sliatnedhr qilrennclq tllqhlkshs ltivsnacgt lwnlsarnpk dqealwdmga
      421 vsmlknlihs khkmiamgsa aalrnlmanr pakykdanim spgsslpslh vrkqkaleae
      481 ldaqhlsetf dnidnlspka shrskqrhkq slygdyvfdt nrhddnrsdn fntgnmtvls
      541 pylnttvlps ssssrgslds srsekdrsle rergiglgny hpatenpgts skrglqistt
      601 aaqiakvmee vsaihtsqed rssgsttelh cvtdernalr rssaahthsn tynftksens
      661 nrtcsmpyak leykrssnds lnsvsssdgy gkrgqmkpsi esyseddesk fcsygqypad
      721 lahkihsanh mddndgeldt pinyslkysd eqlnsgrqsp sqnerwarpk hiiedeikqs
      781 eqrqsrnqst typvytestd dkhlkfqphf gqqecvspyr srgangsetn rvgsnhginq
      841 nvsqslcqed dyeddkptny seryseeeqh eeeerptnys ikyneekrhv dqpidyslky
      901 atdipssqkq sfsfsksssg qssktehmss ssentstpss nakrqnqlhp ssaqsrsgqp
      961 qkaatckvss inqetiqtyc vedtpicfsr csslsslssa edeigcnqtt qeadsantlq
     1021 iaeikekigt rsaedpvsev pavsqhprtk ssrlqgssls sesarhkave fssgakspsk
     1081 sgaqtpkspp ehyvqetplm fsrctsvssl dsfesrsias svqsepcsgm vsgiispsdl
     1141 pdspgqtmpp srsktppppp qtaqtkrevp knkaptaekr esgpkqaavn aavqrvqvlp
     1201 dadtllhfat estpdgfscs sslsalslde pfiqkdvelr imppvqendn gneteseqpk
     1261 esnenqekea ektidsekdl lddsddddie ileeciisam ptkssrkakk paqtasklpp
     1321 pvarkpsqlp vykllpsqnr lqpqkhvsft pgddmprvyc vegtpinfst atslsdltie
     1381 sppnelaage gvrggaqsge fekrdtipte grstdeaqgg ktssvtipel ddnkaeegdi
     1441 laecinsamp kgkshkpfrv kkimdqvqqa sasssapnkn qldgkkkkpt spvkpipqnt
     1501 eyrtrvrkna dsknnlnaer vfsdnkdskk qnlknnskvf ndklpnnedr vrgsfafdsp
     1561 hhytpiegtp ycfsrndsls sldfddddvd lsrekaelrk akenkeseak vtshteltsn
     1621 qqsanktqai akqpinrgqp kpilqkqstf pqsskdipdr gaatdeklqn faientpvcf
     1681 shnsslssls didqennnke nepiketepp dsqgepskpq asgyapksfh vedtpvcfsr
     1741 nsslsslsid seddllqeci ssampkkkkp srlkgdnekh sprnmggilg edltldlkdi
     1801 qrpdsehgls pdsenfdwka iqegansivs slhqaaaaac lsrqassdsd silslksgis
     1861 lgspfhltpd qeekpftsnk gprilkpgek stletkkies eskgikggkk vykslitgkv
     1921 rsnseisgqm kqplqanmps isrgrtmihi pgvrnsssst spvskkgppl ktpaskspse
     1981 gqtattsprg akpsvksels pvarqtsqig gsskapsrsg srdstpsrpa qqplsrpiqs
     2041 pgrnsispgr ngisppnkls qlprtsspst astkssgsgk msytspgrqm sqqnltkqtg
     2101 lsknassipr sesaskglnq mnngngankk velsrmsstk ssgsesdrse rpvlvrqstf
     2161 ikeapsptlr rkleesasfe slspssrpas ptrsqaqtpv lspslpdmsl sthssvqagg
     2221 wrklppnlsp tieyndgrpa krhdiarshs espsrlpinr sgtwkrehsk hssslprvst
     2281 wrrtgssssi lsassessek aksedekhvn sisgtkqske nqvsakgtwr kikenefspt
     2341 nstsqtvssg atngaesktl iyqmapavsk tedvwvried cpinnprsgr sptgntppvi
     2401 dsvsekanpn ikdskdnqak qnvgngsvpm rtvglenrln sfiqvdapdq kgteikpgqn
     2461 npvpvsetne ssivertpfs ssssskhssp sgtvaarvtp fnynpsprks sadstsarps
     2521 qiptpvnnnt kkrdsktdst essgtqspkr hsgsylvtsv
//
LOCUS       NP_001426201             612 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA replication licensing factor MCM7 isoform 3 [Homo sapiens].
ACCESSION   NP_001426201
VERSION     NP_001426201.1
DBSOURCE    REFSEQ: accession NM_001439272.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Sun,Q., Sui,Y., Li,S., Zhou,R., Fu,Z., Luo,J. and Zhao,W.
  TITLE     RNF8-mediated multi-ubiquitination of MCM7: Linking disassembly of
            the CMG helicase with DNA damage response in human cells
  JOURNAL   Life Sci 353, 122912 (2024)
   PUBMED   39004272
  REMARK    GeneRIF: RNF8-mediated multi-ubiquitination of MCM7: Linking
            disassembly of the CMG helicase with DNA damage response in human
            cells.
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Wang,J., Amin,A., Cheung,M.H., Shi,L. and Liang,C.
  TITLE     Targeted inhibition of the expression of both MCM5 and MCM7 by
            miRNA-214 impedes DNA replication and tumorigenesis in
            hepatocellular carcinoma cells
  JOURNAL   Cancer Lett 539, 215677 (2022)
   PUBMED   35490917
  REMARK    GeneRIF: Targeted inhibition of the expression of both MCM5 and
            MCM7 by miRNA-214 impedes DNA replication and tumorigenesis in
            hepatocellular carcinoma cells.
REFERENCE   4  (residues 1 to 612)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 612)
  AUTHORS   Su,D.
  TITLE     MCM7 affects the cisplatin resistance of liver cancer cells and the
            development of liver cancer by regulating the PI3K/Akt signaling
            pathway
  JOURNAL   Immunopharmacol Immunotoxicol 44 (1), 17-27 (2022)
   PUBMED   34821526
  REMARK    GeneRIF: MCM7 affects the cisplatin resistance of liver cancer
            cells and the development of liver cancer by regulating the
            PI3K/Akt signaling pathway.
REFERENCE   6  (residues 1 to 612)
  AUTHORS   Suzuki,S., Adachi,A., Hiraiwa,A., Ohashi,M., Ishibashi,M. and
            Kiyono,T.
  TITLE     Cloning and characterization of human MCM7 promoter
  JOURNAL   Gene 216 (1), 85-91 (1998)
   PUBMED   9714754
REFERENCE   7  (residues 1 to 612)
  AUTHORS   Fujita,M., Kiyono,T., Hayashi,Y. and Ishibashi,M.
  TITLE     hCDC47, a human member of the MCM family. Dissociation of the
            nucleus-bound form during S phase
  JOURNAL   J Biol Chem 271 (8), 4349-4354 (1996)
   PUBMED   8626784
REFERENCE   8  (residues 1 to 612)
  AUTHORS   Musahl,C., Schulte,D., Burkhart,R. and Knippers,R.
  TITLE     A human homologue of the yeast replication protein Cdc21.
            Interactions with other Mcm proteins
  JOURNAL   Eur J Biochem 230 (3), 1096-1101 (1995)
   PUBMED   7601140
REFERENCE   9  (residues 1 to 612)
  AUTHORS   Nakatsuru,S., Sudo,K. and Nakamura,Y.
  TITLE     Isolation and mapping of a human gene (MCM2) encoding a product
            homologous to yeast proteins involved in DNA replication
  JOURNAL   Cytogenet Cell Genet 68 (3-4), 226-230 (1995)
   PUBMED   7842741
REFERENCE   10 (residues 1 to 612)
  AUTHORS   Hu,B., Burkhart,R., Schulte,D., Musahl,C. and Knippers,R.
  TITLE     The P1 family: a new class of nuclear mammalian proteins related to
            the yeast Mcm replication proteins
  JOURNAL   Nucleic Acids Res 21 (23), 5289-5293 (1993)
   PUBMED   8265339
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073842.5.
            
            Summary: The protein encoded by this gene is one of the highly
            conserved mini-chromosome maintenance proteins (MCM) that are
            essential for the initiation of eukaryotic genome replication. The
            hexameric protein complex formed by the MCM proteins is a key
            component of the pre-replication complex (pre_RC) and may be
            involved in the formation of replication forks and in the
            recruitment of other DNA replication related proteins. The MCM
            complex consisting of this protein and MCM2, 4 and 6 proteins
            possesses DNA helicase activity, and may act as a DNA unwinding
            enzyme. Cyclin D1-dependent kinase, CDK4, is found to associate
            with this protein, and may regulate the binding of this protein
            with the tumorsuppressor protein RB1/RB. Alternatively spliced
            transcript variants encoding distinct isoforms have been reported.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2359524.1,
                                           SRR14038195.202995.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..612
                     /product="DNA replication licensing factor MCM7 isoform 3"
                     /EC_number="3.6.4.12"
                     /note="minichromosome maintenance deficient 7; DNA
                     replication licensing factor MCM7; homolog of S.
                     cerevisiae Cdc47; CDC47 homolog; protein phosphatase 1,
                     regulatory subunit 104"
                     /calculated_mol_wt=68485
     Region          38..534
                     /region_name="MCM"
                     /note="minichromosome maintenance proteins; smart00350"
                     /db_xref="CDD:214631"
     Site            order(236,260..262,276,281..282,285,289,296,298,300,302,
                     305..306,313,316,319..320,322,324,331,339,342,345,349,
                     352..353,356,361..365,368..369,371..372,374,386..387,403,
                     406,416,418,420,423..424,427,430..431,434..435,437,449,
                     465..468,471,475,478..479,482..483,495..497,503)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:350664"
     Site            order(236..238,276..282,407,430,497)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350664"
     Site            order(305,364..365)
                     /site_type="other"
                     /note="nucleic acid binding site [nucleotide binding]"
                     /db_xref="CDD:350664"
     CDS             1..612
                     /gene="MCM7"
                     /gene_synonym="CDC47; MCM2; P1.1-MCM3; P1CDC47; P85MCM;
                     PNAS146; PPP1R104"
                     /coded_by="NM_001439272.1:489..2327"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:4176"
                     /db_xref="HGNC:HGNC:6950"
                     /db_xref="MIM:600592"
ORIGIN      
        1 mmeqrsrdpg mvrspqnqyp aelmrrfely fqgpssnkpr virevradsv gklvtvrgiv
       61 trvsevkpkm vvatytcdqc gaetyqpiqs ptfmplimcp sqecqtnrsg grlylqtrgs
      121 rfikfqemkm qehsdqvpvg niprsitvlv egentriaqp gdhvsvtgif lpilrtgfrq
      181 vvqgllsety leahrivkmn kseddesgag eltreelrqi aeedfyekla asiapeiygh
      241 edvkkallll lvggvdqspr gmkirgnini clmgdpgvak sqllsyidrl aprsqyttgr
      301 gssgvgltaa vlrdsvsgel tleggalvla dqgvccidef dkmaeadrta ihevmeqqti
      361 siakagiltt lnarcsilaa anpaygrynp rrsleqniql paallsrfdl lwliqdrpdr
      421 dndlrlaqhi tyvhqhsrqp psqfepldmk lmrryiamcr ekqpmvpesl adyitaayve
      481 mrreawaskd atytsartll ailrlstala rlrmvdvvek edvneairlm emskdsllgd
      541 kgqtartqrp advifatvre lvsggrsvrf seaeqrcvsr gftpaqfqaa ldeyeelnvw
      601 qvnasrtrit fv
//
LOCUS       NP_001397842            1022 aa            linear   PRI 21-NOV-2025
DEFINITION  protein GNAS isoform k [Homo sapiens].
ACCESSION   NP_001397842 XP_016883303
VERSION     NP_001397842.1
DBSOURCE    REFSEQ: accession NM_001410913.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1022)
  AUTHORS   Lin,J., Nie,Q., Cheng,J., Zhong,Y.N., Zhang,T., Zhang,X., Ge,X.,
            Ding,Y., Niu,C., Gao,Y., Wang,K., Gao,M., Wang,X., Chen,W., Yun,C.,
            Ye,C., Xu,J., Shaoyong,W., Zhang,L., Shang,P., Luo,X., Zhang,Z.,
            Zheng,X., Sha,X., Zhang,J., Nie,S., Zhang,X., Ren,F., Liu,H.,
            Dong,E., Yu,X., Ji,L., Pang,Y., Sun,J.P. and Jiang,C.
  TITLE     A microbial amino-acid-conjugated bile acid, tryptophan-cholic
            acid, improves glucose homeostasis via the orphan receptor MRGPRE
  JOURNAL   Cell 188 (17), 4530-4548 (2025)
   PUBMED   40446798
REFERENCE   2  (residues 1 to 1022)
  AUTHORS   Crane,J.L., Shamblott,M.J., Axelman,J., Hsu,S., Levine,M.A. and
            Germain-Lee,E.L.
  TITLE     Imprinting status of Galpha(s), NESP55, and XLalphas in cell
            cultures derived from human embryonic germ cells: GNAS imprinting
            in human embryonic germ cells
  JOURNAL   Clin Transl Sci 2 (5), 355-360 (2009)
   PUBMED   20443919
  REMARK    GeneRIF: analysis of the imprinting Status of Galpha(s), NESP55,
            and XLalphas in cell cultures derived from human embryonic germ
            cells
REFERENCE   3  (residues 1 to 1022)
  AUTHORS   Bastepe,M.
  TITLE     The GNAS Locus: Quintessential Complex Gene Encoding Gsalpha,
            XLalphas, and other Imprinted Transcripts
  JOURNAL   Curr Genomics 8 (6), 398-414 (2007)
   PUBMED   19412439
  REMARK    GeneRIF: GNAS locus has a highly complex imprinted expression
            pattern, giving rise to transcripts (including non-coding) that are
            maternally, paternally, or biallelically expressed.
REFERENCE   4  (residues 1 to 1022)
  AUTHORS   Jakobsen,A.M., Ahlman,H., Kolby,L., Abrahamsson,J.,
            Fischer-Colbrie,R. and Nilsson,O.
  TITLE     NESP55, a novel chromogranin-like peptide, is expressed in
            endocrine tumours of the pancreas and adrenal medulla but not in
            ileal carcinoids
  JOURNAL   Br J Cancer 88 (11), 1746-1754 (2003)
   PUBMED   12771991
  REMARK    GeneRIF: Neuroendocrine secretory protein 55 is found in a subset
            of neuroendocrine tumours showing differentiation towards adrenal
            chromaffin cells and pancreatic islets cells and not in ileal
            carcinoids
REFERENCE   5  (residues 1 to 1022)
  AUTHORS   Freson,K., Jaeken,J., Van Helvoirt,M., de Zegher,F.,
            Wittevrongel,C., Thys,C., Hoylaerts,M.F., Vermylen,J. and Van
            Geet,C.
  TITLE     Functional polymorphisms in the paternally expressed XLalphas and
            its cofactor ALEX decrease their mutual interaction and enhance
            receptor-mediated cAMP formation
  JOURNAL   Hum Mol Genet 12 (10), 1121-1130 (2003)
   PUBMED   12719376
REFERENCE   6  (residues 1 to 1022)
  AUTHORS   Weiss,U., Ischia,R., Eder,S., Lovisetti-Scamihorn,P., Bauer,R. and
            Fischer-Colbrie,R.
  TITLE     Neuroendocrine secretory protein 55 (NESP55): alternative splicing
            onto transcripts of the GNAS gene and posttranslational processing
            of a maternally expressed protein
  JOURNAL   Neuroendocrinology 71 (3), 177-186 (2000)
   PUBMED   10729789
REFERENCE   7  (residues 1 to 1022)
  AUTHORS   Ischia,R., Lovisetti-Scamihorn,P., Hogue-Angeletti,R.,
            Wolkersdorfer,M., Winkler,H. and Fischer-Colbrie,R.
  TITLE     Molecular cloning and characterization of NESP55, a novel
            chromogranin-like precursor of a peptide with 5-HT1B receptor
            antagonist activity
  JOURNAL   J Biol Chem 272 (17), 11657-11662 (1997)
   PUBMED   9111083
REFERENCE   8  (residues 1 to 1022)
  AUTHORS   Haldeman-Englert,C.R., Hurst,A.C.E. and Levine,M.A.
  TITLE     Disorders of GNAS Inactivation
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29072892
REFERENCE   9  (residues 1 to 1022)
  AUTHORS   Szymczuk,V., Florenzano,P., de Castro,L.F., Collins,M.T. and
            Boyce,A.M.
  TITLE     Fibrous Dysplasia / McCune-Albright Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719192
REFERENCE   10 (residues 1 to 1022)
  AUTHORS   Weinstein,L.S., Gejman,P.V., de Mazancourt,P., American,N. and
            Spiegel,A.M.
  TITLE     A heterozygous 4-bp deletion mutation in the Gs alpha gene (GNAS1)
            in a patient with Albright hereditary osteodystrophy
  JOURNAL   Genomics 13 (4), 1319-1321 (1992)
   PUBMED   1505964
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL132655.13, AL121917.20 and
            AL109840.24.
            
            On Aug 17, 2022 this sequence version replaced XP_016883303.1.
            
            Summary: This locus has a highly complex imprinted expression
            pattern. It gives rise to maternally, paternally, and biallelically
            expressed transcripts that are derived from four alternative
            promoters and 5' exons. Some transcripts contain a differentially
            methylated region (DMR) at their 5' exons, and this DMR is commonly
            found in imprinted genes and correlates with transcript expression.
            An antisense transcript is produced from an overlapping locus on
            the opposite strand. One of the transcripts produced from this
            locus, and the antisense transcript, are paternally expressed
            noncoding RNAs, and may regulate imprinting in this region. In
            addition, one of the transcripts contains a second overlapping ORF,
            which encodes a structurally unrelated protein - Alex. Alternative
            splicing of downstream exons is also observed, which results in
            different forms of the stimulatory G-protein alpha subunit, a key
            element of the classical signal transduction pathway linking
            receptor-ligand interactions with the activation of adenylyl
            cyclase and a variety of cellular reponses. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            Mutations in this gene result in pseudohypoparathyroidism type 1a,
            pseudohypoparathyroidism type 1b, Albright hereditary
            osteodystrophy, pseudopseudohypoparathyroidism, McCune-Albright
            syndrome, progressive osseus heteroplasia, polyostotic fibrous
            dysplasia of bone, and some pituitary tumors. [provided by RefSeq,
            Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2279463.1,
                                           SRR14038192.2193067.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 19412439
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1022
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.32"
     Protein         1..1022
                     /product="protein GNAS isoform k"
                     /note="secretogranin VI; G protein subunit alpha S;
                     guanine nucleotide binding protein (G protein), alpha
                     stimulating activity polypeptide 1; guanine nucleotide
                     regulatory protein; adenylate cyclase-stimulating G alpha
                     protein; protein ALEX; extra large alphas protein;
                     alternative gene product encoded by XL-exon"
                     /calculated_mol_wt=109408
     Region          1..105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWF2.2)"
     Region          <84..300
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          185..224
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWF2.2)"
     Region          283..588
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWF2.2)"
     Region          640..666
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWF2.2)"
     Region          642..>676
                     /region_name="UDM1_RNF168_RNF169-like"
                     /note="UDM1 (ubiquitin-dependent DSB recruitment module 1)
                     found in RING finger proteins RNF168, RNF169 and similar
                     proteins; cd22249"
                     /db_xref="CDD:409016"
     Region          684..1016
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Region          685..698
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWF2.2)"
     Site            order(690,695..697,832,851,854,920..921,923,993..994)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206639"
     Site            690..697
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206639"
     Site            order(691..693,721,725,729,732,735..736,756,759,800,829,
                     854,862,866)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Region          824..832
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWF2.2)"
     Site            827..835
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            832
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(833,835,837,848,850,854..856,858,861..862,864..867)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(835,860,863..864,867)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Region          847..856
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWF2.2)"
     Site            851..854
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            852..868
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Region          916..923
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWF2.2)"
     Site            920..923
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            980
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5JWF2.2)"
     Site            order(985..996,998..1001)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Region          992..997
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JWF2.2)"
     Site            993..995
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..1022
                     /gene="GNAS"
                     /gene_synonym="AHO; AIMAH1; C20orf45; GNAS1; GPSA; GSA;
                     GSP; NESP; PITA3; POH; SCG6; SgVI"
                     /coded_by="NM_001410913.1:551..3619"
                     /note="isoform k is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS93066.1"
                     /db_xref="GeneID:2778"
                     /db_xref="HGNC:HGNC:4392"
                     /db_xref="MIM:139320"
ORIGIN      
        1 mgvrnclygn nmsgqrdipp eigeqpeqpp leapgaaapg agpspaeeme tepphnepip
       61 vendgeacgp pevsrpnfqv lnpafreaga hgsyspppee ampfeaeqps lggfwptleq
      121 pgfpsgvhag leafgpalme pgafsgarpg lggyspppee ampfefdqpa qrgcsqlllq
      181 vpdlapggpg aagvpgappe epqalrpaka gsrggysppp eetmpfeldg egfgddsppp
      241 glsrviaqvd gssqfaavaa ssavrltpaa napplwvpga igspsqeavr ppsnftgssp
      301 wmeisgppfe igsapagvdd tpvnmdsppi aldgppikvs gapdkrerae rppveeeaae
      361 megaadaaeg gkvpspgygs paagaasadt aaraapaapa dpdsgatped pdsgtapadp
      421 dsgafaadpd sgaapaapad pdsgaapdap adpdsgaapd apadpdagaa peapaapaaa
      481 etraahvapa apdagaptap aasatraaqv rraasaapas garrkihlrp pspeiqaadp
      541 ptprptrasa wrgksessrg rrvyydegva ssdddssgde sddgtsgclr wfqhrrnrrr
      601 rkpqrnllrn flvqafggcf grsespqpka srslkvkkvp laekrrqmrk ealekraqkr
      661 aekkrsklid kqlqdekmgy mcthrllllg agesgkstiv kqmrilhvng fngdekatkv
      721 qdiknnlkea ietivaamsn lvppvelanp enqfrvdyil svmnvpdfdf ppefyehaka
      781 lwedegvrac yersneyqli dcaqyfldki dvikqadyvp sdqdllrcrv ltsgifetkf
      841 qvdkvnfhmf dvggqrderr kwiqcfndvt aiifvvasss ynmvirednq tnrlqealnl
      901 fksiwnnrwl rtisvilfln kqdllaekvl agkskiedyf pefaryttpe datpepgedp
      961 rvtrakyfir deflristas gdgrhycyph ftcavdteni rrvfndcrdi iqrmhlrqye
     1021 ll
//
LOCUS       NP_001393547            1043 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 5 [Homo sapiens].
ACCESSION   NP_001393547
VERSION     NP_001393547.1
DBSOURCE    REFSEQ: accession NM_001406618.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1043)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1043)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1043)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1043)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1043)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1043)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1043)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1804065.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1043
                     /product="hamartin isoform 5"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=116145
     Region          16..598
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <587..>839
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1043
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406618.1:262..3393"
                     /note="isoform 5 is encoded by transcript variant 32"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mdtdvvvltt gvlvlitmlp mipqsgkqhl ldffdifgrl sswclkkpgh vaevylvhlh
       61 asvyalfhrl ygmypcnfvs flrshysmke nletfeevvk pmmehvrihp elvtgskdhe
      121 ldprrwkrle thdvviecak isldpteasy edgysvshqi sarfphrsad vttspyadtq
      181 nsygcatstp ystsrlmlln mpgqlpqtls spstrlitep pqatlwspsm vcgmttppts
      241 pgnvppdlsh pyskvfgtta ggkgtplgtp atspppaplc hsddyvhisl pqatvtpprk
      301 eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed siekdkeeaa
      361 isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv npeplhssld
      421 klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp trvgfgsgqp
      481 ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr liqqgadahs
      541 kelnklplps ksvdwthfgg sppsdeirtl rdqllllhnq llyerfkrqq halrnrrllr
      601 kvikaaalee hnaamkdqlk lqekdiqmwk vslqkeqary nqlqeqrdtm vtklhsqirq
      661 lqhdreefyn qsqelqtkle dcrnmiaelr ielkkannkv chtelllsqv sqklsnsesv
      721 qqqmeflnrq llvlgevnel yleqlqnkhs dttkevemmk aayrkelekn rshvlqqtqr
      781 ldtsqkrile leshlakkdh llleqkkyle dvklqargql qaaesryeaq kritqvfele
      841 ildlygrlek dgllkkleee kaeaaeaaee rldccndgcs dsmvghneea sghngetktp
      901 rpssargssg srggggssss sselstpekp phqragpfss rwettmgeas asipttvgsl
      961 pssksflgmk arelfrnkse sqcdedgmts slseslktel gkdlgveaki plnldgphps
     1021 pptpdsvgql himdynethh ehs
//
LOCUS       NP_001400296             335 aa            linear   PRI 21-NOV-2025
DEFINITION  telomeric repeat-binding factor 1 isoform 7 [Homo sapiens].
ACCESSION   NP_001400296 XP_024303014
VERSION     NP_001400296.1
DBSOURCE    REFSEQ: accession NM_001413367.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Hu,H., van Roon,A.M., Ghanim,G.E., Ahsan,B., Oluwole,A.O.,
            Peak-Chew,S.Y., Robinson,C.V. and Nguyen,T.H.D.
  TITLE     Structural basis of telomeric nucleosome recognition by shelterin
            factor TRF1
  JOURNAL   Sci Adv 9 (34), eadi4148 (2023)
   PUBMED   37624885
  REMARK    GeneRIF: Structural basis of telomeric nucleosome recognition by
            shelterin factor TRF1.
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Harmak,H., Redouane,S., Charoute,H., Aniq Filali,O., Barakat,A. and
            Rouba,H.
  TITLE     In silico exploration and molecular dynamics of deleterious SNPs on
            the human TERF1 protein triggering male infertility
  JOURNAL   J Biomol Struct Dyn 41 (24), 14665-14688 (2023)
   PUBMED   36995171
  REMARK    GeneRIF: In silico exploration and molecular dynamics of
            deleterious SNPs on the human TERF1 protein triggering male
            infertility.
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Abreu,P.L., Lee,Y.W. and Azzalin,C.M.
  TITLE     In Vitro Characterization of the Physical Interactions between the
            Long Noncoding RNA TERRA and the Telomeric Proteins TRF1 and TRF2
  JOURNAL   Int J Mol Sci 23 (18), 10463 (2022)
   PUBMED   36142374
  REMARK    GeneRIF: In Vitro Characterization of the Physical Interactions
            between the Long Noncoding RNA TERRA and the Telomeric Proteins
            TRF1 and TRF2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Jack,A., Kim,Y., Strom,A.R., Lee,D.S.W., Williams,B., Schaub,J.M.,
            Kellogg,E.H., Finkelstein,I.J., Ferro,L.S., Yildiz,A. and
            Brangwynne,C.P.
  TITLE     Compartmentalization of telomeres through DNA-scaffolded phase
            separation
  JOURNAL   Dev Cell 57 (2), 277-290 (2022)
   PUBMED   35077681
  REMARK    GeneRIF: Compartmentalization of telomeres through DNA-scaffolded
            phase separation.
REFERENCE   6  (residues 1 to 335)
  AUTHORS   Broccoli,D., Chong,L., Oelmann,S., Fernald,A.A., Marziliano,N., van
            Steensel,B., Kipling,D., Le Beau,M.M. and de Lange,T.
  TITLE     Comparison of the human and mouse genes encoding the telomeric
            protein, TRF1: chromosomal localization, expression and conserved
            protein domains
  JOURNAL   Hum Mol Genet 6 (1), 69-76 (1997)
   PUBMED   9002672
REFERENCE   7  (residues 1 to 335)
  AUTHORS   Lu,K.P., Hanes,S.D. and Hunter,T.
  TITLE     A human peptidyl-prolyl isomerase essential for regulation of
            mitosis
  JOURNAL   Nature 380 (6574), 544-547 (1996)
   PUBMED   8606777
REFERENCE   8  (residues 1 to 335)
  AUTHORS   Bilaud,T., Koering,C.E., Binet-Brasselet,E., Ancelin,K.,
            Pollice,A., Gasser,S.M. and Gilson,E.
  TITLE     The telobox, a Myb-related telomeric DNA binding motif found in
            proteins from yeast, plants and human
  JOURNAL   Nucleic Acids Res 24 (7), 1294-1303 (1996)
   PUBMED   8614633
REFERENCE   9  (residues 1 to 335)
  AUTHORS   Chong,L., van Steensel,B., Broccoli,D., Erdjument-Bromage,H.,
            Hanish,J., Tempst,P. and de Lange,T.
  TITLE     A human telomeric protein
  JOURNAL   Science 270 (5242), 1663-1667 (1995)
   PUBMED   7502076
REFERENCE   10 (residues 1 to 335)
  AUTHORS   Zhong,Z., Shiue,L., Kaplan,S. and de Lange,T.
  TITLE     A mammalian factor that binds telomeric TTAGGG repeats in vitro
  JOURNAL   Mol Cell Biol 12 (11), 4834-4843 (1992)
   PUBMED   1406665
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022893.6.
            
            On Oct 31, 2022 this sequence version replaced XP_024303014.1.
            
            Summary: This gene encodes a telomere specific protein which is a
            component of the telomere nucleoprotein complex. This protein is
            present at telomeres throughout the cell cycle and functions as an
            inhibitor of telomerase, acting in cis to limit the elongation of
            individual chromosome ends. The protein structure contains a
            C-terminal Myb motif, a dimerization domain near its N-terminus and
            an acidic N-terminus. Multiple transcripts of this gene are
            alternatively spliced products. [provided by RefSeq, Aug 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3656729.1,
                                           SRR14038192.3831628.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.11"
     Protein         1..335
                     /product="telomeric repeat-binding factor 1 isoform 7"
                     /note="NIMA-interacting protein 2; telomeric protein
                     Pin2/TRF1; TTAGGG repeat-binding factor 1; telomeric
                     repeat binding factor (NIMA-interacting) 1"
                     /calculated_mol_wt=38677
     Region          1..160
                     /region_name="TRFH"
                     /note="Telomeric Repeat binding Factor or TTAGGG Repeat
                     binding Factor, central (dimerization) domain Homology;
                     TRFH. Telomeres are protein/DNA complexes that make up the
                     physical ends of eukaryotic linear chromosomes and are
                     essential for chromosome stability; cl02779"
                     /db_xref="CDD:413471"
     Site            order(2,5,19,23,27,37..41,49,52..53,56)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238174"
     Region          277..325
                     /region_name="SANT_TRF"
                     /note="Telomere repeat binding factor-like DNA-binding
                     domains of the SANT/myb-like family; cd11660"
                     /db_xref="CDD:212558"
     Site            order(277..279,297,299..300,311,313..315,317..319,
                     321..322)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212558"
     CDS             1..335
                     /gene="TERF1"
                     /gene_synonym="hTRF1-AS; PIN2; t-TRF1; TRBF1; TRF; TRF1"
                     /coded_by="NM_001413367.1:412..1419"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:7013"
                     /db_xref="HGNC:HGNC:11728"
                     /db_xref="MIM:600951"
ORIGIN      
        1 mftiihglss ltacqlrtiy icqfltriaa gktldaqfen deritplesa lmiwgsieke
       61 hdklheeiqn likiqaiavc mengnfkeae evferifgdp nshmpfkskl lmiisqkdtf
      121 hsffqhfsyn hmmekiksyv nyvlseksst flmkaaakvv eskrtrtits qdkpsgndve
      181 meteanldtr ksvsdkqsav tessegtvsl lrshknlfls klqhgtqqqd lnkkerrvgt
      241 pqstkkkkes rratesripv sksqpvtpek hrarkrqawl weedknlrsg vrkygegnws
      301 killhykfnn rtsvmlkdrw rtmkklklis sdsed
//
LOCUS       NP_001394254             311 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 26 [Homo sapiens].
ACCESSION   NP_001394254
VERSION     NP_001394254.1
DBSOURCE    REFSEQ: accession NM_001407325.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 311)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 311)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 311)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 311)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 311)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2438962.1,
                                           SRR18074969.530871.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..311
                     /product="tropomyosin alpha-1 chain isoform 26"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=35751
     Region          48..262
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..311
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407325.1:84..1019"
                     /note="isoform 26 is encoded by transcript variant 26"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle delvslqkkl kgtedeldky
       61 sealkdaqek lelaekkatd aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegqv rqleeqlrim dqtlkalmaa edkysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddlegki lssvfslilm veyqpgktif qfkgihidtl lctctfflcv
      301 lwgfslwlln s
//
LOCUS       NP_001394114             816 aa            linear   PRI 21-NOV-2025
DEFINITION  sodium channel protein type 5 subunit alpha isoform h [Homo
            sapiens].
ACCESSION   NP_001394114
VERSION     NP_001394114.1
DBSOURCE    REFSEQ: accession NM_001407185.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Hu,Y., Zhang,C., Wang,S., Xiong,H., Xie,W., Zeng,Z., Cai,H.,
            Wang,Q.K. and Lu,Z.
  TITLE     14-3-3epsilon/YWHAE regulates the transcriptional expression of
            cardiac sodium channel NaV1.5
  JOURNAL   Heart Rhythm 21 (11), 2320-2329 (2024)
   PUBMED   38750908
  REMARK    GeneRIF: 14-3-3epsilon/YWHAE regulates the transcriptional
            expression of cardiac sodium channel NaV1.5.
REFERENCE   2  (residues 1 to 816)
  AUTHORS   Cadena-Ullauri,S., Guevara-Ramirez,P., Ruiz-Pozo,V.A.,
            Tamayo-Trujillo,R., Paz-Cruz,E., Simancas-Racines,D.,
            Ibarra-Castillo,R., Laso-Bayas,J.L. and Zambrano,A.K.
  TITLE     Genomic analysis of an Ecuadorian individual carrying an SCN5A rare
            variant
  JOURNAL   BMC Cardiovasc Disord 24 (1), 388 (2024)
   PUBMED   39068398
  REMARK    GeneRIF: Genomic analysis of an Ecuadorian individual carrying an
            SCN5A rare variant.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 816)
  AUTHORS   Tariq,U., Sarkar,S., Malladi,N., Kumar,R., Bugga,P., Chakraborty,P.
            and Banerjee,S.K.
  TITLE     Knockdown of SCN5A alters metabolic-associated genes and aggravates
            hypertrophy in the cardiomyoblast
  JOURNAL   Mol Biol Rep 51 (1), 661 (2024)
   PUBMED   38758505
  REMARK    GeneRIF: Knockdown of SCN5A alters metabolic-associated genes and
            aggravates hypertrophy in the cardiomyoblast.
            Erratum:[Mol Biol Rep. 2024 Jul 26;51(1):852. doi:
            10.1007/s11033-024-09742-9. PMID: 39060789]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 816)
  AUTHORS   Wright,K.M., Nathan,S., Jiang,H., Xia,W., Kim,H., Chakouri,N.,
            Nwafor,J.N., Fossier,L., Srinivasan,L., Chen,Z., Boronina,T.,
            Post,J., Paul,S., Cole,R.N., Ben-Johny,M., Cole,P.A. and
            Gabelli,S.B.
  TITLE     NEDD4L intramolecular interactions regulate its auto and substrate
            NaV1.5 ubiquitination
  JOURNAL   J Biol Chem 300 (3), 105715 (2024)
   PUBMED   38309503
  REMARK    GeneRIF: NEDD4L intramolecular interactions regulate its auto and
            substrate NaV1.5 ubiquitination.
REFERENCE   5  (residues 1 to 816)
  AUTHORS   George,A.L. Jr., Varkony,T.A., Drabkin,H.A., Han,J., Knops,J.F.,
            Finley,W.H., Brown,G.B., Ward,D.C. and Haas,M.
  TITLE     Assignment of the human heart tetrodotoxin-resistant voltage-gated
            Na+ channel alpha-subunit gene (SCN5A) to band 3p21
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 67-70 (1995)
   PUBMED   7956363
REFERENCE   6  (residues 1 to 816)
  AUTHORS   Jiang,C., Atkinson,D., Towbin,J.A., Splawski,I., Lehmann,M.H.,
            Li,H., Timothy,K., Taggart,R.T., Schwartz,P.J., Vincent,G.M. et al.
  TITLE     Two long QT syndrome loci map to chromosomes 3 and 7 with evidence
            for further heterogeneity
  JOURNAL   Nat Genet 8 (2), 141-147 (1994)
   PUBMED   7842012
REFERENCE   7  (residues 1 to 816)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   8  (residues 1 to 816)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 816)
  AUTHORS   Groffen,A.J., Bikker,H. and Christiaans,I.
  TITLE     Long QT Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301308
REFERENCE   10 (residues 1 to 816)
  AUTHORS   Gellens,M.E., George,A.L. Jr., Chen,L.Q., Chahine,M., Horn,R.,
            Barchi,R.L. and Kallen,R.G.
  TITLE     Primary structure and functional expression of the human cardiac
            tetrodotoxin-insensitive voltage-dependent sodium channel
  JOURNAL   Proc Natl Acad Sci U S A 89 (2), 554-558 (1992)
   PUBMED   1309946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP006241.1.
            
            Summary: The protein encoded by this gene is an integral membrane
            protein and tetrodotoxin-resistant voltage-gated sodium channel
            subunit. This protein is found primarily in cardiac muscle and is
            responsible for the initial upstroke of the action potential in an
            electrocardiogram. Defects in this gene have been associated with
            long QT syndrome type 3 (LQT3), atrial fibrillation,
            cardiomyopathy, and Brugada syndrome 1, all autosomal dominant
            cardiac diseases. Alternative splicing results in several
            transcript variants encoding different isoforms. [provided by
            RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1409025.1,
                                           SRR14038193.1753919.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.2"
     Protein         1..816
                     /product="sodium channel protein type 5 subunit alpha
                     isoform h"
                     /note="cardiac tetrodotoxin-insensitive voltage-dependent
                     sodium channel alpha subunit; sodium channel protein type
                     5 subunit alpha; voltage-gated sodium channel subunit
                     alpha Nav1.5; sodium channel protein cardiac muscle
                     subunit alpha; sodium channel, voltage-gated, type V,
                     alpha subunit"
                     /calculated_mol_wt=90843
     Region          28..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Region          113..420
                     /region_name="I. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Region          130..423
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            130..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            158..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            189..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            214
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            217..236
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            250..272
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            283
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            288
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            291
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            318
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:P15389; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            328
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            387..413
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            457
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Region          461..591
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P15389; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Region          507..667
                     /region_name="Na_trans_cytopl"
                     /note="Cytoplasmic domain of voltage-gated Na+ ion
                     channel; pfam11933"
                     /db_xref="CDD:463401"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            513
                     /site_type="methylation"
                     /note="Dimethylated arginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            526
                     /site_type="methylation"
                     /note="Dimethylated arginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JJV9; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23092124; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            680
                     /site_type="methylation"
                     /note="Dimethylated arginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:21726068; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     Site            720..737
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14524.2)"
     Site            740
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14524.2)"
     CDS             1..816
                     /gene="SCN5A"
                     /gene_synonym="CDCD2; CMD1E; CMPD2; HB1; HB2; HBBD; HH1;
                     ICCD; IVF; LQT3; Nav1.5; PFHB1; SSS1; VF1"
                     /coded_by="NM_001407185.1:210..2660"
                     /note="isoform h is encoded by transcript variant 8"
                     /db_xref="GeneID:6331"
                     /db_xref="HGNC:HGNC:10593"
                     /db_xref="MIM:600163"
ORIGIN      
        1 manfllprgt ssfrrftres laaiekrmae kqargsttlq esreglpeee aprpqldlqa
       61 skklpdlygn ppqeligepl edldpfystq ktfivlnkgk tifrfsatna lyvlspfhpi
      121 rraavkilvh slfnmlimct iltncvfmaq hdpppwtkyv eytftaiytf eslvkilarg
      181 fclhaftflr dpwnwldfsv iimayvseni klgnlsalrt frvlralkti svipglktiv
      241 galiqsvkkl advmvltvfc lsvfaliglq lfmgnlrhkc vrnftalngt ngsveadglv
      301 wesldlylsd penyllkngt sdvllcgnss dagtcpegyr clkagenpdh gytsfdsfaw
      361 aflalfrlmt qdcwerlyqq tlrsagkiym iffmlviflg sfylvnlila vvamayeeqn
      421 qatiaeteek ekrfqeamem lkkehealti rgvdtvsrss lemsplapvn sherrskrrk
      481 rmssgteecg edrlpksdse dgpramnhls ltrglsrtsm kprssrgsif tfrrrdlgse
      541 adfaddenst ageseshhts llvpwplrrt saqgqpspgt sapghalhgk knstvdcngv
      601 vsllgagdpe atspgshllr pvmlehppdt ttpseepggp qmltsqapcv dgfeepgarq
      661 ralsavsvlt saleeleesr hkcppcwnrl aqryliwecc plwmsikqgv klvvmdpftd
      721 ltitmcivln tlfmalehyn mtsefeemlq vgnlvraacs wlsnghpgrr gpraagtafm
      781 gkeegilhte gsfeggnhhr ghlgggresq grllrs
//
LOCUS       NP_001425603             771 aa            linear   PRI 21-NOV-2025
DEFINITION  dipeptidyl peptidase 8 isoform 12 [Homo sapiens].
ACCESSION   NP_001425603 XP_047288722 XP_054234286
VERSION     NP_001425603.1
DBSOURCE    REFSEQ: accession NM_001438674.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 771)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 771)
  AUTHORS   Li,K., Zhang,Y., Zhao,W., Wang,R., Li,Y., Wei,L., Wang,L., Chen,X.,
            Chen,Z., Liu,P., Nie,N., Tian,X. and Fu,R.
  TITLE     DPP8/9 inhibition attenuates the TGF-beta1-induced excessive
            deposition of extracellular matrix (ECM) in human mesangial cells
            via Smad and Akt signaling pathways
  JOURNAL   Toxicol Lett 395, 1-10 (2024)
   PUBMED   38458339
  REMARK    GeneRIF: DPP8/9 inhibition attenuates the TGF-beta1-induced
            excessive deposition of extracellular matrix (ECM) in human
            mesangial cells via Smad and Akt signaling pathways.
REFERENCE   3  (residues 1 to 771)
  AUTHORS   Zhang,Y., Li,K., Li,Y., Zhao,W., Wang,L., Chen,Z., Ma,X., Yao,T.,
            Wang,J., Dong,W., Li,X., Tian,X. and Fu,R.
  TITLE     Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the
            proximal renal tubule epithelial cells
  JOURNAL   Pharmacol Res 169, 105630 (2021)
   PUBMED   33932609
  REMARK    GeneRIF: Profibrotic mechanisms of DPP8 and DPP9 highly expressed
            in the proximal renal tubule epithelial cells.
REFERENCE   4  (residues 1 to 771)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 771)
  AUTHORS   Hollingsworth,L.R., Sharif,H., Griswold,A.R., Fontana,P.,
            Mintseris,J., Dagbay,K.B., Paulo,J.A., Gygi,S.P., Bachovchin,D.A.
            and Wu,H.
  TITLE     DPP9 sequesters the C terminus of NLRP1 to repress inflammasome
            activation
  JOURNAL   Nature 592 (7856), 778-783 (2021)
   PUBMED   33731932
REFERENCE   6  (residues 1 to 771)
  AUTHORS   Chen,Y.S., Chien,C.H., Goparaju,C.M., Hsu,J.T., Liang,P.H. and
            Chen,X.
  TITLE     Purification and characterization of human prolyl dipeptidase DPP8
            in Sf9 insect cells
  JOURNAL   Protein Expr Purif 35 (1), 142-146 (2004)
   PUBMED   15039077
REFERENCE   7  (residues 1 to 771)
  AUTHORS   Shu,H., Chen,S., Bi,Q., Mumby,M. and Brekken,D.L.
  TITLE     Identification of phosphoproteins and their phosphorylation sites
            in the WEHI-231 B lymphoma cell line
  JOURNAL   Mol Cell Proteomics 3 (3), 279-286 (2004)
   PUBMED   14729942
REFERENCE   8  (residues 1 to 771)
  AUTHORS   Qi,S.Y., Riviere,P.J., Trojnar,J., Junien,J.L. and Akinsanya,K.O.
  TITLE     Cloning and characterization of dipeptidyl peptidase 10, a new
            member of an emerging subgroup of serine proteases
  JOURNAL   Biochem J 373 (Pt 1), 179-189 (2003)
   PUBMED   12662155
REFERENCE   9  (residues 1 to 771)
  AUTHORS   Ajami,K., Abbott,C.A., Obradovic,M., Gysbers,V., Kahne,T.,
            McCaughan,G.W. and Gorrell,M.D.
  TITLE     Structural requirements for catalysis, expression, and dimerization
            in the CD26/DPIV gene family
  JOURNAL   Biochemistry 42 (3), 694-701 (2003)
   PUBMED   12534281
REFERENCE   10 (residues 1 to 771)
  AUTHORS   Abbott,C.A., Yu,D.M., Woollatt,E., Sutherland,G.R., McCaughan,G.W.
            and Gorrell,M.D.
  TITLE     Cloning, expression and chromosomal localization of a novel human
            dipeptidyl peptidase (DPP) IV homolog, DPP8
  JOURNAL   Eur J Biochem 267 (20), 6140-6150 (2000)
   PUBMED   11012666
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011846.16 and AC105129.4.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047288722.1, XP_054234286.1.
            
            Summary: This gene encodes a member of the peptidase S9B family, a
            small family of dipeptidyl peptidases that are able to cleave
            peptide substrates at a prolyl bond. The encoded protein shares
            similarity with dipeptidyl peptidase IV in that it is ubiquitously
            expressed, and hydrolyzes the same substrates. These similarities
            suggest that, like dipeptidyl peptidase IV, this protein may play a
            role in T-cell activation and immune function. Alternatively
            spliced transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2562917.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..771
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..771
                     /product="dipeptidyl peptidase 8 isoform 12"
                     /EC_number="3.4.14.5"
                     /note="prolyl dipeptidase DPP8; dipeptidyl peptidase VIII;
                     DPP VIII; dipeptidyl peptidase IV-related protein 1"
                     /calculated_mol_wt=88806
     Region          8..143
                     /region_name="Dpp_8_9_N"
                     /note="Dipeptidyl peptidase 8 and 9 N-terminal; pfam19520"
                     /db_xref="CDD:466112"
     Region          142..537
                     /region_name="DPPIV_N"
                     /note="Dipeptidyl peptidase IV (DPP IV) N-terminal region;
                     pfam00930"
                     /db_xref="CDD:395744"
     Region          629..>748
                     /region_name="Peptidase_S9"
                     /note="Prolyl oligopeptidase family; pfam00326"
                     /db_xref="CDD:459761"
     CDS             1..771
                     /gene="DPP8"
                     /gene_synonym="DP8; DPRP-1; DPRP1; MST097; MSTP097;
                     MSTP135; MSTP141"
                     /coded_by="NM_001438674.1:304..2619"
                     /note="isoform 12 is encoded by transcript variant 16"
                     /db_xref="GeneID:54878"
                     /db_xref="HGNC:HGNC:16490"
                     /db_xref="MIM:606819"
ORIGIN      
        1 mwkrseqmki ksgkcnmaaa meteqlgvei fetadceeni esqdrpklep fyveryswsq
       61 lkklladtrk yhgymmakap hdfmfvkrnd pdgphsdriy ylamsgenre ntlfyseipk
      121 tinraavlml swkplldlfq qqplrpnlve tscpnirmdp klcpadpdwi afihsndiwi
      181 snivtreerr ltyvhnelan meedarsagv atfvlqeefd rysgywwcpk aettpsggki
      241 lrilyeende seveiihvts pmletrrads frypktgtan pkvtfkmsei midaegriid
      301 vidkeliqpf eilfegveyi aragwtpegk yawsilldrs qtrlqivlis pelfipvedd
      361 vmerqrlies vpdsvtplii yeettdiwin ihdifhvfpq sheeeiefif asecktgfrh
      421 lykitsilke skykrssggl papsdfkcpi keeiaitsge wevlgrhgsn iqvdevrrlv
      481 yfegtkdspl ehhlyvvsyv npgevtrltd rgyshsccis qhcdffisky snqknphcvs
      541 lyklsspedd ptcktkefwa tildsagplp dytppeifsf esttgftlyg mlykphdlqp
      601 gkkyptvlfi yggpqvqlvn nrfkgvkyfr lntlaslgyv vvvidnrgsc hrglkfegaf
      661 kykmgqieid dqveglqyla srydfidldr vgihgwsygg ylslmalmqr sdifrvaiag
      721 apvtlwifyd tgyterymgh pdqneqgyyl gsvamqaekf psesilrrdt a
//
LOCUS       NP_001428258            1655 aa            linear   PRI 21-NOV-2025
DEFINITION  BCL-6 corepressor-like protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001428258 XP_005262513 XP_054183524
VERSION     NP_001428258.1
DBSOURCE    REFSEQ: accession NM_001441329.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1655)
  AUTHORS   Luo,C., Chen,Z., Meng,L., Tan,C., He,W., Tu,C., Du,J., Lu,G.X.,
            Lin,G., Tan,Y.Q. and Hu,T.Y.
  TITLE     A hemizygous loss-of-function variant in BCORL1 is associated with
            male infertility and oligoasthenoteratozoospermia
  JOURNAL   Clin Genet 106 (1), 27-36 (2024)
   PUBMED   38342987
  REMARK    GeneRIF: A hemizygous loss-of-function variant in BCORL1 is
            associated with male infertility and oligoasthenoteratozoospermia.
REFERENCE   2  (residues 1 to 1655)
  AUTHORS   Kommoss,F.K.F., Chiang,S., Kobel,M., Koelsche,C., Chang,K.T.,
            Irving,J.A., Dickson,B., Thiryayi,S., Rouzbahman,M., Rasty,G., von
            Deimling,A., Lee,C.H. and Turashvili,G.
  TITLE     Endometrial Stromal Sarcomas With BCOR Internal Tandem Duplication
            and Variant BCOR/BCORL1 Rearrangements Resemble High-grade
            Endometrial Stromal Sarcomas With Recurrent CDK4 Pathway
            Alterations and MDM2 Amplifications
  JOURNAL   Am J Surg Pathol 46 (8), 1142-1152 (2022)
   PUBMED   35499168
  REMARK    GeneRIF: Endometrial Stromal Sarcomas With BCOR Internal Tandem
            Duplication and Variant BCOR/BCORL1 Rearrangements Resemble
            High-grade Endometrial Stromal Sarcomas With Recurrent CDK4 Pathway
            Alterations and MDM2 Amplifications.
REFERENCE   3  (residues 1 to 1655)
  AUTHORS   Schaefer,E.J., Wang,H.C., Karp,H.Q., Meyer,C.A., Cejas,P.,
            Gearhart,M.D., Adelman,E.R., Fares,I., Apffel,A., Lim,K., Xie,Y.,
            Gibson,C.J., Schenone,M., Murdock,H.M., Wang,E.S., Gondek,L.P.,
            Carroll,M.P., Vedula,R.S., Winer,E.S., Garcia,J.S., Stone,R.M.,
            Luskin,M.R., Carr,S.A., Long,H.W., Bardwell,V.J., Figueroa,M.E. and
            Lindsley,R.C.
  TITLE     BCOR and BCORL1 Mutations Drive Epigenetic Reprogramming and
            Oncogenic Signaling by Unlinking PRC1.1 from Target Genes
  JOURNAL   Blood Cancer Discov 3 (2), 116-135 (2022)
   PUBMED   35015684
  REMARK    GeneRIF: BCOR and BCORL1 Mutations Drive Epigenetic Reprogramming
            and Oncogenic Signaling by Unlinking PRC1.1 from Target Genes.
REFERENCE   4  (residues 1 to 1655)
  AUTHORS   Gafner,M., Michelson,M., Argilli,E., Yosovich,K., Sherr,E.H.,
            Parks,K.C., England,E.M., Hady-Cohen,R., Leibovitz,Z., Lev,D.,
            Michaeli-Yosef,Y., Lerman-Sagie,T. and Blumkin,L.
  TITLE     Major brain malformations: corpus callosum dysgenesis, agenesis of
            septum pellucidum and polymicrogyria in patients with
            BCORL1-related disorders
  JOURNAL   J Hum Genet 67 (2), 95-101 (2022)
   PUBMED   34400773
  REMARK    GeneRIF: Major brain malformations: corpus callosum dysgenesis,
            agenesis of septum pellucidum and polymicrogyria in patients with
            BCORL1-related disorders.
REFERENCE   5  (residues 1 to 1655)
  AUTHORS   Junco,S.E., Wang,R., Gaipa,J.C., Taylor,A.B., Schirf,V.,
            Gearhart,M.D., Bardwell,V.J., Demeler,B., Hart,P.J. and Kim,C.A.
  TITLE     Structure of the polycomb group protein PCGF1 in complex with BCOR
            reveals basis for binding selectivity of PCGF homologs
  JOURNAL   Structure 21 (4), 665-671 (2013)
   PUBMED   23523425
REFERENCE   6  (residues 1 to 1655)
  AUTHORS   Shaffer,J.R., Feingold,E., Wang,X., Lee,M., Tcuenco,K., Weeks,D.E.,
            Weyant,R.J., Crout,R., McNeil,D.W. and Marazita,M.L.
  TITLE     GWAS of dental caries patterns in the permanent dentition
  JOURNAL   J Dent Res 92 (1), 38-44 (2013)
   PUBMED   23064961
REFERENCE   7  (residues 1 to 1655)
  AUTHORS   Gao,Z., Zhang,J., Bonasio,R., Strino,F., Sawai,A., Parisi,F.,
            Kluger,Y. and Reinberg,D.
  TITLE     PCGF homologs, CBX proteins, and RYBP define functionally distinct
            PRC1 family complexes
  JOURNAL   Mol Cell 45 (3), 344-356 (2012)
   PUBMED   22325352
REFERENCE   8  (residues 1 to 1655)
  AUTHORS   Li,M., Collins,R., Jiao,Y., Ouillette,P., Bixby,D., Erba,H.,
            Vogelstein,B., Kinzler,K.W., Papadopoulos,N. and Malek,S.N.
  TITLE     Somatic mutations in the transcriptional corepressor gene BCORL1 in
            adult acute myelogenous leukemia
  JOURNAL   Blood 118 (22), 5914-5917 (2011)
   PUBMED   21989985
  REMARK    GeneRIF: BCORL1 by genetic criteria is a novel candidate tumor
            suppressor gene, joining the growing list of genes recurrently
            mutated in acute myelogenous leukemia.
REFERENCE   9  (residues 1 to 1655)
  AUTHORS   Pagan,J.K., Arnold,J., Hanchard,K.J., Kumar,R., Bruno,T.,
            Jones,M.J., Richard,D.J., Forrest,A., Spurdle,A., Verdin,E.,
            Crossley,M., Fanciulli,M., Chenevix-Trench,G., Young,D.B. and
            Khanna,K.K.
  TITLE     A novel corepressor, BCoR-L1, represses transcription through an
            interaction with CtBP
  JOURNAL   J Biol Chem 282 (20), 15248-15257 (2007)
   PUBMED   17379597
REFERENCE   10 (residues 1 to 1655)
  AUTHORS   Lose,F., Arnold,J., Young,D.B., Brown,C.J., Mann,G.J., Pupo,G.M.,
            Khanna,K.K., Chenevix-Trench,G. and Spurdle,A.B.
  CONSRTM   Kathleen Cuningham Foundation Consortium for Research into Familial
            Breast Cancer
  TITLE     BCoR-L1 variation and breast cancer
  JOURNAL   Breast Cancer Res 9 (4), R54 (2007)
   PUBMED   17697391
  REMARK    GeneRIF: Dysregulated BCoR-L1 expression is associated with breast
            cancer
            Erratum:[Breast Cancer Res. 2008;10(5):406]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL034405.16, Z82208.1,
            KF459400.1 and AL136450.8.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_005262513.2, XP_054183524.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            corepressor that is found tethered to promoter regions by
            DNA-binding proteins. The encoded protein can interact with several
            different class II histone deacetylases to repress transcription.
            Two transcript variants encoding different isoforms have been found
            for this gene. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2441306.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1655
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.1"
     Protein         1..1655
                     /product="BCL-6 corepressor-like protein 1 isoform 2"
                     /note="BCoR-like protein 1"
                     /calculated_mol_wt=174863
     Region          65..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          113..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          <198..636
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          343..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          527..550
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          562..646
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          753..781
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          876..901
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          937..977
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1029
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1033
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          <1364..>1473
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1366..1397
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1367,1371..1372,1375..1377,1379..1380,1384,1387,
                     1397,1399,1401,1405..1406,1409..1411,1413..1414,1418,1421,
                     1430,1432,1434,1438..1439,1442..1444,1446..1447,1451,1454)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1399..1430
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1432..1461
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1536..1649
                     /region_name="PUFD_like_1"
                     /note="PCGF Ub-like fold discriminator of BCOR-like 1;
                     cd14260"
                     /db_xref="CDD:271223"
     Site            order(1538,1540..1550,1552,1554,1563..1565,1567,
                     1608..1609,1611,1614,1636,1647,1649)
                     /site_type="other"
                     /note="RAWUL domain interface [polypeptide binding]"
                     /db_xref="CDD:271223"
     CDS             1..1655
                     /gene="BCORL1"
                     /gene_synonym="BCoR-L1; CXorf10; SHUVER"
                     /coded_by="NM_001441329.1:480..5447"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:63035"
                     /db_xref="HGNC:HGNC:25657"
                     /db_xref="MIM:300688"
ORIGIN      
        1 mistaplysg vhnwtssdri rmcgineerr aplsdeestt gdcqhfgsqe fcvsssfskv
       61 eltavgsgsn argadpdgsa teklghksed kpddpqpkmd yagnvaeaeg llvplsspgd
      121 glklpasdsa easnsradcs wtplntqmsk qvdcspagvk aldsrqgvge kntfilatlg
      181 tgvpvegtlp lvttnfsplp apicppapgs asvphsvpda fqvplsvpap vphsglvpvq
      241 vatsvpapsp plapvpalap appsvptlis dsnplsvsas vlvpvpasap psgpvplsap
      301 apaplsvpvs applaliqap vppsaptlvl apvptpvlap mpastppaap appsvpmptp
      361 tpssgppstp tlipafaptp vpaptpapif tpaptpmpaa tpaaiptsap ipasfslsrv
      421 cfpaaqapam qkvplsfqpg tvltpsqplv yipppscgqp lsvatlpttl gvsstltlpv
      481 lpsylqdrcl pgvlaspelr sypyafsvar pltsdsklvs levnrlpcts psgstttqpa
      541 pdgvpgplad tslvtasakv lptpqpllpa psgssapphp akmpsgteqq tegtsvtfsp
      601 lksppqlere masppecsem pldlssksnr qklplpnqrk tppmpvltpv htsskallst
      661 vlsrsqrttq aaggnvtscl gstsspfvif peivrngdps twvknstali stipgtyvgv
      721 anpvpaslll nkdpnlglnr dprhlpkqep isiidqgepk gtgatcgkkg sqagaegqps
      781 tvkrytpari apglpgcqtk elslwkptgp aniyprcsvn gkptstqvlp vgwspyhqas
      841 llsigissag qltpsqgapi rptsvvsefs gvpslsssea vhglpegqpr pggsfvpeqd
      901 pvtknktcri aakpyeeqvn pvlltlspqt gtlalsvqps ggdirmnqgp eeseshlcsd
      961 stpkmegpqg acglklagdt kpknqvlaty mshelvlatp qnlpkmpelp llphdshpke
     1021 lildvvpssr rgssterpql gsqvdlgrvk mekvdgdvvf nlatcfradg lpvapqrgqa
     1081 evrakagqar vkqesvgvfa cknkwqpddv teslppkkmk cgkekdseeq qlqpqakavv
     1141 rsshrpkcrk lpsdpqestk ksprgasdsg kehngvrgkh khrkptkpes qspgkradsh
     1201 eegslekkak ssfrdfipvv lstrtrsqsd lkarkqktss sqslehrlrn rnlllpnkvq
     1261 gisdspngfl pnnleepacl ensekpsgkr kcktkhmatv seeakgkgrw sqqktrspks
     1321 ptpvkptepc tpsksrsass eeasesptar qippearrli vnknagetll qraarlgykd
     1381 vvlyclqkds edvnhrdnag ytalheacsr gwtdilnill ehganvncsa qdgtrpvhda
     1441 vvndnletiw lllsygadpt latysgqtam klassdtmkr flsdhlsdlq graegdpgvs
     1501 wdfysssvle ekdgfacdll hnppgssdqe gddpmeeddf mfelsdkpll pcynlqvsvs
     1561 rgpcnwflfs dvlkrlklss rifqarfphf eittmpkaef yrqvassqll tpaerpggld
     1621 drsppgsset velvryepdl lrllgsevef qscns
//
LOCUS       NP_001397867             525 aa            linear   PRI 21-NOV-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein Q isoform 8 [Homo sapiens].
ACCESSION   NP_001397867 XP_005248693
VERSION     NP_001397867.1
DBSOURCE    REFSEQ: accession NM_001410938.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Ishtayeh,H., Galves,M., Barnatan,T.T., Berdichevsky,Y.,
            Amer-Sarsour,F., Pasmanik-Chor,M., Braverman,I., Blumen,S.C. and
            Ashkenazi,A.
  TITLE     Oculopharyngeal muscular dystrophy mutations link the RNA-binding
            protein HNRNPQ to autophagosome biogenesis
  JOURNAL   Aging Cell 22 (10), e13949 (2023)
   PUBMED   37559347
  REMARK    GeneRIF: Oculopharyngeal muscular dystrophy mutations link the
            RNA-binding protein HNRNPQ to autophagosome biogenesis.
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Semino,F., Schroter,J., Willemsen,M.H., Bast,T., Biskup,S.,
            Beck-Woedl,S., Brennenstuhl,H., Schaaf,C.P., Kolker,S.,
            Hoffmann,G.F., Haack,T.B. and Syrbe,S.
  TITLE     Further evidence for de novo variants in SYNCRIP as the cause of a
            neurodevelopmental disorder
  JOURNAL   Hum Mutat 42 (9), 1094-1100 (2021)
   PUBMED   34157790
  REMARK    GeneRIF: Further evidence for de novo variants in SYNCRIP as the
            cause of a neurodevelopmental disorder.
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 525)
  AUTHORS   Mourelatos,Z., Abel,L., Yong,J., Kataoka,N. and Dreyfuss,G.
  TITLE     SMN interacts with a novel family of hnRNP and spliceosomal
            proteins
  JOURNAL   EMBO J 20 (19), 5443-5452 (2001)
   PUBMED   11574476
REFERENCE   6  (residues 1 to 525)
  AUTHORS   Lau,P.P., Chang,B.H. and Chan,L.
  TITLE     Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a
            component of apobec-1 editosome
  JOURNAL   Biochem Biophys Res Commun 282 (4), 977-983 (2001)
   PUBMED   11352648
REFERENCE   7  (residues 1 to 525)
  AUTHORS   Blanc,V., Navaratnam,N., Henderson,J.O., Anant,S., Kennedy,S.,
            Jarmuz,A., Scott,J. and Davidson,N.O.
  TITLE     Identification of GRY-RBP as an apolipoprotein B RNA-binding
            protein that interacts with both apobec-1 and apobec-1
            complementation factor to modulate C to U editing
  JOURNAL   J Biol Chem 276 (13), 10272-10283 (2001)
   PUBMED   11134005
REFERENCE   8  (residues 1 to 525)
  AUTHORS   Grosset,C., Chen,C.Y., Xu,N., Sonenberg,N., Jacquemin-Sablon,H. and
            Shyu,A.B.
  TITLE     A mechanism for translationally coupled mRNA turnover: interaction
            between the poly(A) tail and a c-fos RNA coding determinant via a
            protein complex
  JOURNAL   Cell 103 (1), 29-40 (2000)
   PUBMED   11051545
REFERENCE   9  (residues 1 to 525)
  AUTHORS   Mizutani,A., Fukuda,M., Ibata,K., Shiraishi,Y. and Mikoshiba,K.
  TITLE     SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear
            ribonucleoprotein R, interacts with ubiquitous synaptotagmin
            isoforms
  JOURNAL   J Biol Chem 275 (13), 9823-9831 (2000)
   PUBMED   10734137
REFERENCE   10 (residues 1 to 525)
  AUTHORS   Harris,C.E., Boden,R.A. and Astell,C.R.
  TITLE     A novel heterogeneous nuclear ribonucleoprotein-like protein
            interacts with NS1 of the minute virus of mice
  JOURNAL   J Virol 73 (1), 72-80 (1999)
   PUBMED   9847309
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136082.22.
            
            On Aug 18, 2022 this sequence version replaced XP_005248693.1.
            
            Summary: This gene encodes a member of the cellular heterogeneous
            nuclear ribonucleoprotein (hnRNP) family. hnRNPs are RNA binding
            proteins that complex with heterogeneous nuclear RNA (hnRNA) and
            regulate alternative splicing, polyadenylation, and other aspects
            of mRNA metabolism and transport. The encoded protein plays a role
            in multiple aspects of mRNA maturation and is associated with
            several multiprotein complexes including the apoB RNA
            editing-complex and survival of motor neurons (SMN) complex.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene, and a pseudogene of this
            gene is located on the short arm of chromosome 20. [provided by
            RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.246845.1,
                                           SRR14372079.2852059.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.3"
     Protein         1..525
                     /product="heterogeneous nuclear ribonucleoprotein Q
                     isoform 8"
                     /note="NS1-associated protein 1; heterogeneous nuclear
                     ribonucleoprotein Q; glycine- and tyrosine-rich
                     RNA-binding protein"
                     /calculated_mol_wt=58862
     Region          5..517
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     CDS             1..525
                     /gene="SYNCRIP"
                     /gene_synonym="GRY-RBP; GRYRBP; hnRNP-Q; HNRNPQ; HNRPQ1;
                     NSAP1; PP68"
                     /coded_by="NM_001410938.1:237..1814"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS93965.1"
                     /db_xref="GeneID:10492"
                     /db_xref="HGNC:HGNC:16918"
                     /db_xref="MIM:616686"
ORIGIN      
        1 mktyrqrekq gtkvadsskg pdeakikall ertgytldvt tgqrkyggpp pdsvysgqqp
       61 svgteifvgk iprdlfedel vplfekagpi wdlrlmmdpl tglnrgyafv tfctkeaaqe
      121 avklynnhei rsgkhigvci svannrlfvg sipksktkeq ileefskvte gltdvilyhq
      181 pddkkknrgf cfleyedhkt aaqarrrlms gkvkvwgnvg tvewadpied pdpevmakvk
      241 vlfvrnlant vteeilekaf sqfgklervk klkdyafihf derdgavkam eemngkdleg
      301 enieivfakp pdqkrkerka qrqaaknqmy ddyyyygpph mppptrgrgr ggrggygypp
      361 dyygyedyyd yygydyhnyr ggyedpyygy edfqvgargr ggrgargaap srgrgaappr
      421 gragysqrgg pgsargvrga rggaqqqrgr gvrgarggrg gnvggkrkad gynqpdskrr
      481 qtnnqnwgsq piaqqplqgg dhsgnygyks enqefyqdtf gqqwk
//
LOCUS       NP_001397813             429 aa            linear   PRI 21-NOV-2025
DEFINITION  adrenocortical dysplasia protein homolog isoform 3 [Homo sapiens].
ACCESSION   NP_001397813 XP_005256172
VERSION     NP_001397813.1
DBSOURCE    REFSEQ: accession NM_001410884.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Wang,Q.L., Gong,C., Meng,X.Y., Fu,M., Yang,H., Zhou,F., Wu,Q. and
            Zhou,Y.
  TITLE     TPP1 is associated with risk of advanced precursors and cervical
            cancer survival
  JOURNAL   PLoS One 19 (5), e0298118 (2024)
   PUBMED   38722833
  REMARK    GeneRIF: TPP1 is associated with risk of advanced precursors and
            cervical cancer survival.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Bertrand,A., Ba,I., Kermasson,L., Pirabakaran,V., Chable,N.,
            Lainey,E., Menard,C., Kallel,F., Picard,C., Hadiji,S.,
            Coolen-Allou,N., Blanchard,E., de Villartay,J.P., Moshous,D.,
            Roelens,M., Callebaut,I., Kannengiesser,C. and Revy,P.
  TITLE     Characterization of novel mutations in the TEL-patch domain of the
            telomeric factor TPP1 associated with telomere biology disorders
  JOURNAL   Hum Mol Genet 33 (7), 612-623 (2024)
   PUBMED   38176734
  REMARK    GeneRIF: Characterization of novel mutations in the TEL-patch
            domain of the telomeric factor TPP1 associated with telomere
            biology disorders.
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Wang,H., Ma,T., Zhang,X., Chen,W., Lan,Y., Kuang,G., Hsu,S.J.,
            He,Z., Chen,Y., Stewart,J., Bhattacharjee,A., Luo,Z., Price,C. and
            Feng,X.
  TITLE     CTC1 OB-B interaction with TPP1 terminates telomerase and prevents
            telomere overextension
  JOURNAL   Nucleic Acids Res 51 (10), 4914-4928 (2023)
   PUBMED   37021555
  REMARK    GeneRIF: CTC1 OB-B interaction with TPP1 terminates telomerase and
            prevents telomere overextension.
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Lambert-Lanteigne,P., Young,A. and Autexier,C.
  TITLE     Complex interaction network revealed by mutation of human
            telomerase 'insertion in fingers' and essential N-terminal domains
            and the telomere protein TPP1
  JOURNAL   J Biol Chem 299 (3), 102916 (2023)
   PUBMED   36649908
  REMARK    GeneRIF: Complex interaction network revealed by mutation of human
            telomerase 'insertion in fingers' and essential N-terminal domains
            and the telomere protein TPP1.
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Liu,D., O'Connor,M.S., Qin,J. and Songyang,Z.
  TITLE     Telosome, a mammalian telomere-associated complex formed by
            multiple telomeric proteins
  JOURNAL   J Biol Chem 279 (49), 51338-51342 (2004)
   PUBMED   15383534
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Houghtaling,B.R., Cuttonaro,L., Chang,W. and Smith,S.
  TITLE     A dynamic molecular link between the telomere length regulator TRF1
            and the chromosome end protector TRF2
  JOURNAL   Curr Biol 14 (18), 1621-1631 (2004)
   PUBMED   15380063
  REMARK    GeneRIF: TINT1 localized to telomeres via TIN2, where it functions
            as a negative regulator of telomerase-mediated telomere elongation.
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Ye,J.Z., Hockemeyer,D., Krutchinsky,A.N., Loayza,D., Hooper,S.M.,
            Chait,B.T. and de Lange,T.
  TITLE     POT1-interacting protein PIP1: a telomere length regulator that
            recruits POT1 to the TIN2/TRF1 complex
  JOURNAL   Genes Dev 18 (14), 1649-1654 (2004)
   PUBMED   15231715
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Liu,D., Safari,A., O'Connor,M.S., Chan,D.W., Laegeler,A., Qin,J.
            and Songyang,Z.
  TITLE     PTOP interacts with POT1 and regulates its localization to
            telomeres
  JOURNAL   Nat Cell Biol 6 (7), 673-680 (2004)
   PUBMED   15181449
  REMARK    GeneRIF: a paper that firstly reported cloning of human TTP1 (PTOP)
            and its biological function at telomere. TPP1 interacts with both
            POT1 and TIN2, heterodimerizes with POT1 and regulates POT1
            telomeric recruitment and telomere length.
REFERENCE   10 (residues 1 to 429)
  AUTHORS   Savage,S.A. and Niewisch,M.R.
  TITLE     Dyskeratosis Congenita and Related Telomere Biology Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301779
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010530.8.
            
            On Aug 17, 2022 this sequence version replaced XP_005256172.2.
            
            Summary: This gene encodes a protein that is involved in telomere
            function. This protein is one of six core proteins in the
            telosome/shelterin telomeric complex, which functions to maintain
            telomere length and to protect telomere ends. Through its
            interaction with other components, this protein plays a key role in
            the assembly and stabilization of this complex, and it mediates the
            access of telomerase to the telomere. Multiple transcript variants
            encoding different isoforms have been found for this gene. This
            gene, which is also referred to as TPP1, is distinct from the
            unrelated TPP1 gene on chromosome 11, which encodes
            tripeptidyl-peptidase I. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1121039.1,
                                           SRR7410571.166078.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..429
                     /product="adrenocortical dysplasia protein homolog isoform
                     3"
                     /note="TIN2 interacting protein 1; POT1 and
                     TIN2-interacting protein; adrenocortical dysplasia
                     homolog"
                     /calculated_mol_wt=45983
     Region          11..120
                     /region_name="TPP1"
                     /note="Shelterin complex subunit, TPP1/ACD; pfam10341"
                     /db_xref="CDD:431220"
     Region          257..>352
                     /region_name="PRK13042"
                     /note="superantigen-like protein SSL4; Reviewed"
                     /db_xref="CDD:183854"
     CDS             1..429
                     /gene="ACD"
                     /gene_synonym="DKCA6; DKCB7; PIP1; PTOP; TINT1; TPP1"
                     /coded_by="NM_001410884.1:41..1330"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92179.1"
                     /db_xref="GeneID:65057"
                     /db_xref="HGNC:HGNC:25070"
                     /db_xref="MIM:609377"
ORIGIN      
        1 magsgrlvlr pwirelilgs etpsspragq llevlqdaea avagpshapd tsdvgatllv
       61 sdgthsvrcl vtrealdtsd weekefgfrg tegrllllqd cgvhvqvaeg gapaefylqv
      121 drfsllpteq prlrvpgcnq dldvqkklyd cleehlsest ssnaglslsq lldemredqe
      181 hqgalvclae scltlegpct appvthwaas rckatgeavy tvpssmlcis endqlilssl
      241 gpcqrtqgtp alpghmssee sgtsisllpa lslaapdpgq rsssqpspai csapatltpr
      301 sphasrtpss plqsctpsls prshvpsphq alvtrpqkps lefkefvglp cknrppfprt
      361 gatrgaqepc svweppkrhr dgsafqyeye ppctslcarv qavrlppqlm awalhflmda
      421 qpgseptpm
//
LOCUS       NP_001400675             857 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform i [Homo sapiens].
ACCESSION   NP_001400675
VERSION     NP_001400675.1
DBSOURCE    REFSEQ: accession NM_001413746.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 857)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 857)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 857)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 857)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 857)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 857)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 857)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 857)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 857)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 857)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1767146.1,
                                           SRR14038191.3371223.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..857
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..857
                     /product="polyhomeotic-like protein 1 isoform i"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=90626
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          212..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          261..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          681..788
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          788..856
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(806..807,841..842,845..846,849)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(817..821,823..824,827..828,832,837)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..857
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413746.1:368..2941"
                     /note="isoform i is encoded by transcript variant 10"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq asinlattsa aqlisrsqsv
      121 sspsattltq svllgnttsp plnqsqaqmy lrpqlgnllq vnrtlgrnvp lasqlilmpn
      181 gavaavqqev psaqspgvha dadqvqnlav rnqqasaqgp qmqgstqkai ppgaspvssl
      241 sqassqalav aqassgatnq slnlsqaggg sgnsipgsmg pggggqahgg lgqlpssgmg
      301 ggscprkgtg vvqplpaaqt vtvsqgsqte aesaaakkae adgsgqqnvg mnltrtatpa
      361 psqtlissat ytqiqphsli qqqqqihlqq kqvviqqqia ihhqqqfqhr qsqllhtath
      421 lqlaqqqqqq qqqqqqqqqp qattltapqp pqgtahvvkg gattsspvva qvpaafymqs
      481 vhlpgkpqtl avkrkadsee erddvstlgs mlpakaspva espkvmdeks slgekaesva
      541 nvnantpsse lvaltpapsv ppptlamvsr qmgdskppqa ivkpqilthi iegfviqega
      601 epfpvgcsql lkesekplqt glptgltenq sggplgvdsp saeldkkanl lkceycgkya
      661 paeqfrgskr fcsmtcakry nvscshqfrl krkkmkefqe anyarvrrrg prrsssdiar
      721 akiqgkchrg qedssrgsdn ssydealspt spgplsvrag hgerdlgnpn tapptpelhg
      781 inpvflssnp srwsveevye fiaslqgcqe iaeefrsqei dgqallllke ehlmsamnik
      841 lgpalkicak invlket
//
LOCUS       NP_001424671             636 aa            linear   PRI 21-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001424671 XP_047272571 XP_054207389
VERSION     NP_001424671.1
DBSOURCE    REFSEQ: accession NM_001437742.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 636)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 636)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 636)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 636)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 636)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 636)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 636)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 636)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 636)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 636)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008641.7.
            
            On or before Apr 9, 2025 this sequence version replaced
            XP_047272571.1, XP_054207389.1.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.766065.1,
                                           SRR18074968.763422.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..636
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..636
                     /product="TNFAIP3-interacting protein 1 isoform 3"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=71733
     Region          14..>149
                     /region_name="Speriolin_N"
                     /note="Speriolin N terminus; pfam15058"
                     /db_xref="CDD:434426"
     Region          61..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          94..412
                     /region_name="Interaction with Nef"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Region          <214..>251
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          252..283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          <298..>538
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          351..367
                     /region_name="Interaction with Shigella flexneri ipah9.8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          431..588
                     /region_name="Required for inhibitory activity of
                     TNF-induced NF-kappa-B activation. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          452..510
                     /region_name="Ubiquitin-binding domain (UBD)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Region          524..530
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            552
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17632516; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            571
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9WUU8; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            599
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          603..636
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            627
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     CDS             1..636
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001437742.1:228..2138"
                     /note="isoform 3 is encoded by transcript variant 21"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 megrgpyriy dpggsvpsge asaaferlvk ensrlkekmq gikmlgelle esqmeatrlr
       61 qkaeelvkdn ellpppspsl gsfdplaelt gkdsnvtasp tapacpsdkp apvqkppssg
      121 tssefevvtp eeqnspesss hanamalgpl predgnlmlh lqrlettlsv caeepdhgql
      181 fthlgrmale fnrlaskvhk neqrtsilqt lceqlrkene alkakldkgl eqrdqaaerl
      241 reenlelkkl lmsngnkega sgrpgspkme gtgkkavagq qqasvtagkv pevvalgaae
      301 kkvkmleqqr sellevnkqw dqhfrsmkqq yeqkitelrq kladlqkqvt dleaereqkq
      361 rdfdrkllla kskiemeetd keqltaeake lrqkvkylqd qlspltrqre yqekeiqrln
      421 kaleealsiq tppsspptaf gspegagall rkqelvtqne llkqqvkife edfqrersdr
      481 ermneekeel kkqveklqaq vtlsnaqlka fkdeekarea lrqqkrkaka sgeryhveph
      541 pehlcgaypy ayppmpamvp hhgfedwsqi ryppppmame hppplpnsrl fhlpeytwrl
      601 pcggvrnpnq ssqvmdppta rptepespkn dregpq
//
LOCUS       NP_001400248             303 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 20 [Homo sapiens].
ACCESSION   NP_001400248
VERSION     NP_001400248.1
DBSOURCE    REFSEQ: accession NM_001413319.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 303)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 303)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 303)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.72200.1,
                                           SRR1803617.114338.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..303
                     /product="RNA-binding Raly-like protein isoform 20"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=33651
     Region          28..110
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          <207..>257
                     /region_name="APG6_N"
                     /note="Apg6 coiled-coil region; pfam17675"
                     /db_xref="CDD:465452"
     CDS             1..303
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413319.1:329..1240"
                     /note="isoform 20 is encoded by transcript variant 45"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mskrrrlkqg epimtgktqt snvtnkndpk sinsrvfign lntaivkkvd ieaifskygk
       61 ivgcsvhkgy afvqymserh araavagena rviagqpldi nmagepkpyr pkpgnkrpls
      121 alyrleskep flsvggyvfd ydyyrddfyn rlfdyhgrvp pppraviplk rprvavtttr
      181 rgkgvfsmkg gsrstasgst gsklksdelq tikkeltqik tkidsllgrl ekiekqqkae
      241 aaqkkqlees lvliqeecvs eiadhsteep aeggpdadge emtdgieedf dedgghelfl
      301 qik
//
LOCUS       NP_001352613            2405 aa            linear   PRI 21-NOV-2025
DEFINITION  histone-lysine N-methyltransferase, H3 lysine-36 specific isoform a
            [Homo sapiens].
ACCESSION   NP_001352613 XP_024301925
VERSION     NP_001352613.2
DBSOURCE    REFSEQ: accession NM_001365684.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2405)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2405)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   3  (residues 1 to 2405)
  AUTHORS   Conteduca,G., Cangelosi,D., Baldo,C., Arado,A., Testa,B.,
            Wagner,R.T., Robertson,K.D., Dequiedt,F., Fitzsimmons,L.,
            Malacarne,M., Filaci,G. and Coviello,D.A.
  TITLE     Impact of NSD1 Alternative Transcripts in Actin Filament Formation
            and Cellular Division Pathways in Fibroblasts
  JOURNAL   Genes (Basel) 15 (9), 1117 (2024)
   PUBMED   39336709
  REMARK    GeneRIF: Impact of NSD1 Alternative Transcripts in Actin Filament
            Formation and Cellular Division Pathways in Fibroblasts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2405)
  AUTHORS   Ren,Z., Yue,L., Hu,H.Y., Hou,X.L., Chen,W.Q., Tan,Y., Dong,Z. and
            Zhang,J.
  TITLE     Identification of Novel NSD1 variations in four Pediatric cases
            with sotos Syndrome
  JOURNAL   BMC Med Genomics 17 (1), 116 (2024)
   PUBMED   38684994
  REMARK    GeneRIF: Identification of Novel NSD1 variations in four Pediatric
            cases with sotos Syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2405)
  AUTHORS   Wang,X., Yeh,S., Wu,G., Hsu,C.L., Wang,L., Chiang,T., Yang,Y.,
            Guo,Y. and Chang,C.
  TITLE     Identification and characterization of a novel androgen receptor
            coregulator ARA267-alpha in prostate cancer cells
  JOURNAL   J Biol Chem 276 (44), 40417-40423 (2001)
   PUBMED   11509567
REFERENCE   6  (residues 1 to 2405)
  AUTHORS   Jaju,R.J., Fidler,C., Haas,O.A., Strickson,A.J., Watkins,F.,
            Clark,K., Cross,N.C., Cheng,J.F., Aplan,P.D., Kearney,L.,
            Boultwood,J. and Wainscoat,J.S.
  TITLE     A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in
            de novo childhood acute myeloid leukemia
  JOURNAL   Blood 98 (4), 1264-1267 (2001)
   PUBMED   11493482
REFERENCE   7  (residues 1 to 2405)
  AUTHORS   Lee,D.K., Duan,H.O. and Chang,C.
  TITLE     Androgen receptor interacts with the positive elongation factor
            P-TEFb and enhances the efficiency of transcriptional elongation
  JOURNAL   J Biol Chem 276 (13), 9978-9984 (2001)
   PUBMED   11266437
REFERENCE   8  (residues 1 to 2405)
  AUTHORS   Huang,N., vom Baur,E., Garnier,J.M., Lerouge,T., Vonesch,J.L.,
            Lutz,Y., Chambon,P. and Losson,R.
  TITLE     Two distinct nuclear receptor interaction domains in NSD1, a novel
            SET protein that exhibits characteristics of both corepressors and
            coactivators
  JOURNAL   EMBO J 17 (12), 3398-3412 (1998)
   PUBMED   9628876
REFERENCE   9  (residues 1 to 2405)
  AUTHORS   Ocansey,S., Cole,T.R.P., Rahman,N. and Tatton-Brown,K.
  TITLE     Sotos Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301652
REFERENCE   10 (residues 1 to 2405)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027314.5, AC008570.6 and
            AC146507.2.
            
            On Jul 13, 2022 this sequence version replaced NP_001352613.1.
            
            Summary: This gene encodes a protein containing a SET domain, 2
            LXXLL motifs, 3 nuclear translocation signals (NLSs), 4 plant
            homeodomain (PHD) finger regions, and a proline-rich region. The
            encoded protein enhances androgen receptor (AR) transactivation,
            and this enhancement can be increased further in the presence of
            other androgen receptor associated coregulators. This protein may
            act as a nucleus-localized, basic transcriptional factor and also
            as a bifunctional transcriptional regulator. Mutations of this gene
            have been associated with Sotos syndrome and Weaver syndrome. One
            version of childhood acute myeloid leukemia is the result of a
            cryptic translocation with the breakpoints occurring within nuclear
            receptor-binding Su-var, enhancer of zeste, and trithorax domain
            protein 1 on chromosome 5 and nucleoporin, 98-kd on chromosome 11.
            Multiple transcript variants encoding distinct isoforms have been
            identified for this gene. [provided by RefSeq, Sep 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF380302.1, SRR11853559.27120.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2405
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..2405
                     /product="histone-lysine N-methyltransferase, H3 lysine-36
                     specific isoform a"
                     /EC_number="2.1.1.357"
                     /note="androgen receptor-associated coregulator 267;
                     histone-lysine N-methyltransferase, H3 lysine-36 and H4
                     lysine-20 specific; H3-K36-HMTase; H4-K20-HMTase; lysine
                     N-methyltransferase 3B; NR-binding SET domain-containing
                     protein; androgen receptor coactivator 267 kDa protein;
                     androgen receptor-associated protein of 267 kDa; nuclear
                     receptor-binding SET domain-containing protein 1; nuclear
                     receptor SET domain-containing protein 1; histone-lysine
                     N-methyltransferase, H3 lysine-36 specific"
                     /calculated_mol_wt=264921
     Region          27..142
                     /region_name="PWWP_NSD1_rpt1"
                     /note="first PWWP domain found in nuclear receptor-binding
                     SET domain-containing protein 1 (NSD1) and similar
                     proteins; cd20161"
                     /db_xref="CDD:438989"
     Site            order(43,46,77)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438989"
     Site            44..47
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438989"
     Site            order(115..117,120..121)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438989"
     Region          <1140..1296
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          1254..1296
                     /region_name="PHD1_NSD1_2"
                     /note="PHD finger 1 found in nuclear receptor-binding SET
                     domain-containing protein NSD1 and NSD2; cd15648"
                     /db_xref="CDD:277118"
     Site            order(1254,1263..1267,1272,1290)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277118"
     Region          1301..1347
                     /region_name="PHD2_NSD1"
                     /note="PHD finger 2 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15650"
                     /db_xref="CDD:277120"
     Site            order(1301,1311..1315,1321,1342)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277120"
     Region          1348..1401
                     /region_name="PHD3_NSD1"
                     /note="PHD finger 3 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15653"
                     /db_xref="CDD:277123"
     Site            order(1348,1366..1370,1374,1396)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277123"
     Region          1418..1457
                     /region_name="PHD4_NSD1"
                     /note="PHD finger 4 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15656"
                     /db_xref="CDD:277126"
     Site            order(1418,1427..1431,1435,1452)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277126"
     Region          1464..1559
                     /region_name="PWWP_NSD1_rpt2"
                     /note="second PWWP domain found in nuclear
                     receptor-binding SET domain-containing protein 1 (NSD1)
                     and similar proteins; cd20164"
                     /db_xref="CDD:438992"
     Site            order(1476,1479,1507)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438992"
     Site            1477..1480
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438992"
     Region          1610..1648
                     /region_name="AWS"
                     /note="AWS domain; pfam17907"
                     /db_xref="CDD:465559"
     Region          1650..1791
                     /region_name="SET_NSD1"
                     /note="SET domain (including post-SET domain) found in
                     nuclear receptor-binding SET domain-containing protein 1
                     (NSD1) and similar proteins; cd19210"
                     /db_xref="CDD:380987"
     Site            order(1661..1663,1680,1690,1694,1703..1709,1726..1730,
                     1737..1739,1754,1765..1775,1777..1781,1790)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380987"
     Site            order(1661..1663,1703..1706,1726..1730,1767,1774,
                     1778..1781,1790)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380987"
     Site            order(1680,1690,1694,1705..1709,1737..1739,1754,
                     1765..1769)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:380987"
     Site            order(1732,1779,1781,1786)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380987"
     Region          1829..1871
                     /region_name="PHD5_NSD1"
                     /note="PHD finger 5 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15659"
                     /db_xref="CDD:277129"
     Site            order(1829,1838..1842,1848,1866)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277129"
     Region          1870..1919
                     /region_name="C5HCH"
                     /note="NSD Cys-His rich domain; pfam17982"
                     /db_xref="CDD:465605"
     Region          <1917..2283
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..2405
                     /gene="NSD1"
                     /gene_synonym="ARA267; KMT3B; SOTOS; SOTOS1; STO"
                     /coded_by="NM_001365684.2:261..7478"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS4413.1"
                     /db_xref="GeneID:64324"
                     /db_xref="HGNC:HGNC:14234"
                     /db_xref="MIM:606681"
ORIGIN      
        1 mlelpgtsss stsqelpfcq pkkkstplky evgdliwakf krrpwwpcri csdplinths
       61 kmkvsnrrpy rqyyveafgd pserawvagk aivmfegrhq feelpvlrrr gkqkekgyrh
      121 kvpqkilskw easvglaeqy dvpkgsknrk cipgsiklds eedmpfedct ndpesehdll
      181 lngclkslaf dsehsadeke kpcaksrark ssdnpkrtsv kkghiqfeah kderrgkipe
      241 nlglnfisgd isdtqasnel sriansltgs ntapgsflfs scgkntakke fetsngdsll
      301 glpegalisk csreknkpqr slvcgskvkl cyigagdeek rsdsisictt sddgssdldp
      361 iehssesdns vleipdafdr tenmlsmqkn ekikysrfaa tntrvkakqk plisnshtdh
      421 lmgctksaep gtetsqvnls dlkastlvhk pqsdftndal spkfnlsssi ssenslikgg
      481 aanqallhsk skqpkfrsik ckhkenpvma eppvineecs lkccssdtkg splasisksg
      541 kvdglkllnn mhektrdssd ietavvkhvl selkelsyrs lgedvsdsgt skpskpllfs
      601 sassqnhipi epdykfstll mmlkdmhdsk tkeqrlmtaq nlvsyrspgr gdcstnspvg
      661 vskvlvsggs thnsekkgdg tqnsanpsps ggdsalsgel saslpgllsd krdlpasgks
      721 rsdcvtrrnc grskpssklr dafsaqmvkn tvnrkalkte rkrklnqlps vtldavlqgd
      781 rerggslrgg aedpskedpl qimghltsed gdhfsdvhfd skvkqsdpgk isekglsfen
      841 gkgpeldsvm nsendelngv nqvvpkkrwq rlnqrrtkpr krmnrfkeke nsecafrvll
      901 psdpvqegrd efpehrtpsa sileeplteq nhadcldsag prlnvcdkss asigdmekep
      961 gipsltpqae lpepavrsek krlrkpskwl leyteeydqi fapkkkqkkv qeqvhkvssr
     1021 ceeesllarg rssaqnkqvd enslistkee ppvlereapf legplaqsel ggghaelpql
     1081 tlsvpvapev sprpalesee llvktpgnye skrqrkptkk llesndldpg fmpkkgdlgl
     1141 skkcyeaghl engitescat syskdfgggt tkifdkprkr krqrhaaakm qckkvkndds
     1201 skeipgsege lmphrtatsp ketveegveh dpgmpaskkm qgergggaal kenvcqncek
     1261 lgelllceaq ccgafhlecl gltemprgkf icnecrtgih tcfvckqsge dvkrcllplc
     1321 gkfyheecvq kypptvmqnk gfrcslhici tchaanpanv saskgrlmrc vrcpvayhan
     1381 dfclaagski lasnsiicpn hftprrgcrn hehvnvswcf vcseggsllc cdscpaafhr
     1441 eclnidipeg nwycndckag kkphyreivw vkvgryrwwp aeichpravp snidkmrhdv
     1501 gefpvlffgs ndylwthqar vfpymegdvs skdkmgkgvd gtykkalqea aarfeelkaq
     1561 kelrqlqedr kndkkpppyk hikvnrpigr vqiftadlse iprcnckatd enpcgidsec
     1621 inrmllyech ptvcpaggrc qnqcfskrqy peveifrtlq rgwglrtktd ikkgefvney
     1681 vgelideeec rariryaqeh ditnfymltl dkdriidagp kgnyarfmnh ccqpncetqk
     1741 wsvngdtrvg lfalsdikag teltfnynle clgngktvck cgapncsgfl gvrpknqpia
     1801 teekskkfkk kqqgkrrtqg eitkeredec fscgdagqlv sckkpgcpkv yhadclnltk
     1861 rpagkwecpw hqcdicgkea asfcemcpss fckqhregml fiskldgrls ctehdpcgpn
     1921 plepgeirey vpppvplppg psthlaeqst gmaaqapkms dkppadtnqm lslskkalag
     1981 tcqrpllper plertdsrpq pldkvrdlag sgtksqslvs sqrpldrppa vagprpqlsd
     2041 kpspvtspss spsvrsqple rplgtadprl dksigaaspr pqslektsvp tglrlpppdr
     2101 llitsspkpq tsdrptdkph aslsqrlppp ekvlsavvqt lvakekalrp vdqntqsknr
     2161 aalvmdlidl tprqkeraas phqvtpqade kmpvlesssw paskglghmp ravekgcvsd
     2221 plqtsgkaaa psedpwqavk sltqarllsq ppakaflyep ttqasgrasa gaeqtpgpls
     2281 qspglvkqak qmvggqqlpa laaksgqsfr slgkapaslp teekklvtte qspwalgkas
     2341 sraglwpiva gqtlaqscws agstqtlaqt cwslgrgqdp kpeqntlpal nqapsshkca
     2401 eseqk
//
LOCUS       NP_001424928             958 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 3 isoform 9 [Homo sapiens].
ACCESSION   NP_001424928 XP_011511490 XP_054203923
VERSION     NP_001424928.1
DBSOURCE    REFSEQ: accession NM_001437999.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 958)
  AUTHORS   Wang,H., Lan,S., Wang,L., Zhao,J., Jia,X., Xu,J., Sun,G., Liu,L.,
            Gong,S., Wang,N., Shan,B., Zhang,F. and Zhang,Z.
  TITLE     Expression of circ-PHC3 enhances ovarian cancer progression via
            regulation of the miR-497-5p/SOX9 pathway
  JOURNAL   J Ovarian Res 16 (1), 142 (2023)
   PUBMED   37468993
  REMARK    GeneRIF: Expression of circ-PHC3 enhances ovarian cancer
            progression via regulation of the miR-497-5p/SOX9 pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 958)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 958)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 958)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 958)
  AUTHORS   Crea,F., Di Paolo,A., Liu,H.H., Polillo,M., Clermont,P.L.,
            Guerrini,F., Ciabatti,E., Ricci,F., Barate,C., Fontanelli,G.,
            Barsotti,S., Morganti,R., Danesi,R., Wang,Y., Petrini,M.,
            Galimberti,S. and Helgason,C.D.
  TITLE     Polycomb genes are associated with response to imatinib in chronic
            myeloid leukemia
  JOURNAL   Epigenomics 7 (5), 757-765 (2015)
   PUBMED   26343356
  REMARK    GeneRIF: Data show that polycomb-group proteins BMI1, PHC3, CBX6
            and CBX7 expression was significantly increased during imatinib
            treatment.
REFERENCE   6  (residues 1 to 958)
  AUTHORS   Deshpande,A.M., Akunowicz,J.D., Reveles,X.T., Patel,B.B.,
            Saria,E.A., Gorlick,R.G., Naylor,S.L., Leach,R.J. and Hansen,M.F.
  TITLE     PHC3, a component of the hPRC-H complex, associates with E2F6
            during G0 and is lost in osteosarcoma tumors
  JOURNAL   Oncogene 26 (12), 1714-1722 (2007)
   PUBMED   17001316
  REMARK    GeneRIF: loss of PHC3 may favor tumorigenesis by potentially
            disrupting the ability of cells to remain in G(0)
REFERENCE   7  (residues 1 to 958)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   8  (residues 1 to 958)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 958)
  AUTHORS   Tonkin,E., Hagan,D.M., Li,W. and Strachan,T.
  TITLE     Identification and characterisation of novel mammalian homologues
            of Drosophila polyhomeoticpermits new insights into relationships
            between members of the polyhomeotic family
  JOURNAL   Hum Genet 111 (4-5), 435-442 (2002)
   PUBMED   12384788
REFERENCE   10 (residues 1 to 958)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC023891.28 and AC008040.7.
            
            On or before Apr 14, 2025 this sequence version replaced
            XP_011511490.1, XP_054203923.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1783896.1,
                                           SRR14038192.2536616.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..958
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.2"
     Protein         1..958
                     /product="polyhomeotic-like protein 3 isoform 9"
                     /note="early development regulator 3; polyhomeotic-like
                     protein 3; homolog of polyhomeotic 3; early development
                     regulatory protein 3; polyhomeotic like 3"
                     /calculated_mol_wt=103710
     Region          303..>543
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          889..957
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(907..908,942..943,946..947,950)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(918..922,924..925,928..929,933,938)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..958
                     /gene="PHC3"
                     /gene_synonym="EDR3; HPH3"
                     /coded_by="NM_001437999.1:19..2895"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:80012"
                     /db_xref="HGNC:HGNC:15682"
                     /db_xref="MIM:620031"
ORIGIN      
        1 maeaefkdhs tamdtepnpg tssvstttss tttttittss srmqqpqisv ysgsdrhavq
       61 viqqalhrpp ssaaqylqqm yaaqqqhlml htaalqqqhl sssqlqslaa vqaslssgrp
      121 stsptgsvtq qssmsqtsli ftpattvaav qsdipvvsss sssscqsaat qvqnltlrsq
      181 klgvlsssqn gppkstsqtq sltichnktt vtsskisqrd pspesnkkge spslesrsta
      241 vtrtssihql iapasyspiq phslikhqqi plhsppskvs hhqlilqqqq qqiqpitlqn
      301 stqdpppsqh ciplqnhglp papsnaqsqh cspiqshpsp ltvspnqsqs aqqsvvvspp
      361 pphspsqspt iiihpqaliq phplvssalq pgpnlqqsta nqvqataqln lpshlplpas
      421 pvvhigpvqq salvspgqqi vspshqqyss lqsspipias ppqmstsppa qipplplqsm
      481 qslqvqpeil sqgqvlvqna lvseeelpaa ealvqlpfqt lpppqtvavn lqvqppapvd
      541 ppvgmhlnqc hlhkvfslkv yqvedvceee mpeesdecvr mdrtpppptl spaaitvgrg
      601 edltsehpll eqvelpavas vsasviksps dpshvsvppp plllpaattr snstsmhssi
      661 psienkppqa ivkpqilthv iegfviqegl epfpvsrssl lieqpvkkrp lldnqvinsv
      721 cvqpelqnnt khadnssdte medmiaeetl eemdsellkc efcgkmgyan eflrskrfct
      781 mscakrynvs cskkfalsrw nrkpdnqslg hrgrrpsgpd gaarehilrq lpitypsaee
      841 dlashedsvp samttrlrrq serererelr dvrirkmpen sdllpvaqte psiwtvddvw
      901 afihslpgcq diadefraqe idgqallllk edhlmsamni klgpalkica rinslkes
//
LOCUS       NP_001427517             428 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform f [Homo sapiens].
ACCESSION   NP_001427517 XP_011543632 XP_054226332
VERSION     NP_001427517.1
DBSOURCE    REFSEQ: accession NM_001440588.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 428)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 428)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 428)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 428)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2.
            
            On or before May 22, 2025 this sequence version replaced
            XP_011543632.1, XP_054226332.1.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.152189.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..428
                     /product="polycomb protein EED isoform f"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=48651
     Region          96..140
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          148..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          150..423
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          193..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          240..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          309..382
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          390..416
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..428
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001440588.1:478..1764"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdendd avsiesgtnt erpdtptntp
       61 napgrkswgk gkwkskkcky sfkcvnslke dhnqplfgvq fnwhskegdp lvfatvgsnr
      121 vtlyechsqg eirllqsyvd adadenfytc awtydsntsh pllavagsrg iiriinpitm
      181 qcikhyvghg nainelkfhp rdpnlllsvs kdhalrlwni qtdtlvaifg gveghrdevl
      241 sadydllgek imscgmdhsl klwrinskrm mnaikesydy npnktnrpfi sqkihfpdfs
      301 trdihrnyvd cvrwlgdlil sksgrailhs hqqcmrdpvs pnlrqhlsce naivcwkpgk
      361 meddidkikp sesnvtilgr fdysqcdiwy mrfsmdfwqk mlalgnqvgk lyvwdleved
      421 phkanrdh
//
LOCUS       NP_001424439            1755 aa            linear   PRI 21-NOV-2025
DEFINITION  BCL-6 corepressor isoform c [Homo sapiens].
ACCESSION   NP_001424439 XP_005272673 XP_054183268
VERSION     NP_001424439.1
DBSOURCE    REFSEQ: accession NM_001437510.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1755)
  AUTHORS   Batkova,M., Havlovicova,M., Nocar,A., Dudakova,L., Macek,M.,
            Liskova,P. and Dostalova,T.
  TITLE     Dental abnormalities observed in the oculo-facio-cardio-dental
            (OFCD) syndrome present in two Czech families bearing novel de novo
            BCOR pathogenic variants
  JOURNAL   BMC Oral Health 24 (1), 1264 (2024)
   PUBMED   39438869
  REMARK    GeneRIF: Dental abnormalities observed in the
            oculo-facio-cardio-dental (OFCD) syndrome present in two Czech
            families bearing novel de novo BCOR pathogenic variants.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1755)
  AUTHORS   Giner,F., Medina-Ceballos,E., Lopez-Reig,R., Machado,I.,
            Lopez-Guerrero,J.A., Navarro,S., Rubio-Martinez,L.A., Espino,M.,
            Mayordomo-Aranda,E. and Llombart-Bosch,A.
  TITLE     The Combined Immunohistochemical Expression of GLI1 and BCOR in
            Synovial Sarcomas for the Identification of Three Risk Groups and
            Their Prognostic Outcomes: A Study of 52 Patients
  JOURNAL   Int J Mol Sci 25 (14), 7615 (2024)
   PUBMED   39062853
  REMARK    GeneRIF: The Combined Immunohistochemical Expression of GLI1 and
            BCOR in Synovial Sarcomas for the Identification of Three Risk
            Groups and Their Prognostic Outcomes: A Study of 52 Patients.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1755)
  AUTHORS   Mavridou,E., Lema Fernandez,A.G., Nardelli,C., Pierini,V.,
            Quintini,M., Arniani,S., Di Giacomo,D., Crescenzi,B., Matteucci,C.,
            Sambani,C. and Mecucci,C.
  TITLE     A novel t(X;21)(p11.4;q22.12) translocation adds to the role of
            BCOR and RUNX1 in myelodysplastic syndromes and acute myeloid
            leukemias
  JOURNAL   Genes Chromosomes Cancer 63 (4), e23235 (2024)
   PUBMED   38656651
  REMARK    GeneRIF: A novel t(X;21)(p11.4;q22.12) translocation adds to the
            role of BCOR and RUNX1 in myelodysplastic syndromes and acute
            myeloid leukemias.
REFERENCE   4  (residues 1 to 1755)
  AUTHORS   Pierron,G., Tirode,F., Lucchesi,C., Reynaud,S., Ballet,S.,
            Cohen-Gogo,S., Perrin,V., Coindre,J.M. and Delattre,O.
  TITLE     A new subtype of bone sarcoma defined by BCOR-CCNB3 gene fusion
  JOURNAL   Nat Genet 44 (4), 461-466 (2012)
   PUBMED   22387997
  REMARK    GeneRIF: A new fusion was observed between BCOR (encoding the BCL6
            co-repressor) and CCNB3 (encoding the testis-specific cyclin B3) on
            the X chromosome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1755)
  AUTHORS   Tomsig,J.L., Snyder,S.L. and Creutz,C.E.
  TITLE     Identification of targets for calcium signaling through the copine
            family of proteins. Characterization of a coiled-coil
            copine-binding motif
  JOURNAL   J Biol Chem 278 (12), 10048-10054 (2003)
   PUBMED   12522145
REFERENCE   6  (residues 1 to 1755)
  AUTHORS   Ng,D., Hadley,D.W., Tifft,C.J. and Biesecker,L.G.
  TITLE     Genetic heterogeneity of syndromic X-linked recessive
            microphthalmia-anophthalmia: is Lenz microphthalmia a single
            disorder?
  JOURNAL   Am J Med Genet 110 (4), 308-314 (2002)
   PUBMED   12116202
REFERENCE   7  (residues 1 to 1755)
  AUTHORS   Tang,T.T., Dowbenko,D., Jackson,A., Toney,L., Lewin,D.A., Dent,A.L.
            and Lasky,L.A.
  TITLE     The forkhead transcription factor AFX activates apoptosis by
            induction of the BCL-6 transcriptional repressor
  JOURNAL   J Biol Chem 277 (16), 14255-14265 (2002)
   PUBMED   11777915
  REMARK    GeneRIF: The forkhead transcription factor AFX activates apoptosis
            by induction of the BCL-6 transcriptional repressor.
REFERENCE   8  (residues 1 to 1755)
  AUTHORS   Huynh,K.D., Fischle,W., Verdin,E. and Bardwell,V.J.
  TITLE     BCoR, a novel corepressor involved in BCL-6 repression
  JOURNAL   Genes Dev 14 (14), 1810-1823 (2000)
   PUBMED   10898795
  REMARK    GeneRIF: Function:BCoR is a transcriptional corepressor for BCL-6.
            Nomenclature:BCoR (BCL-6 corepressor)
REFERENCE   9  (residues 1 to 1755)
  AUTHORS   Ng,D.
  TITLE     Lenz Microphthalmia Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301694
REFERENCE   10 (residues 1 to 1755)
  AUTHORS   Bardakjian,T., Weiss,A. and Schneider,A.
  TITLE     Microphthalmia/Anophthalmia/Coloboma Spectrum - RETIRED CHAPTER,
            FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301552
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091806.4 and AC092198.5.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_005272673.1, XP_054183268.1.
            
            Summary: The protein encoded by this gene was identified as an
            interacting corepressor of BCL6, a POZ/zinc finger transcription
            repressor that is required for germinal center formation and may
            influence apoptosis. This protein selectively interacts with the
            POZ domain of BCL6, but not with eight other POZ proteins. Specific
            class I and II histone deacetylases (HDACs) have been shown to
            interact with this protein, which suggests a possible link between
            the two classes of HDACs. Several transcript variants encoding
            different isoforms have been found for this gene. A pseudogene of
            this gene is found on chromosome Y.[provided by RefSeq, Jun 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.102970.1,
                                           SRR14038193.3770353.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1755
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.4"
     Protein         1..1755
                     /product="BCL-6 corepressor isoform c"
                     /note="BCL-6 interacting corepressor; BCL6 interacting
                     corepressor; BCL-6 coreceptor"
                     /calculated_mol_wt=192058
     Region          <257..673
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          309..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          388..438
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            392
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          498..514
                     /region_name="Interaction with BCL6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          557..641
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          737..760
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          773..794
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          815..844
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1071..1187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGN4; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1202..1414
                     /region_name="BCOR"
                     /note="BCL-6 co-repressor, non-ankyrin-repeat region;
                     pfam15808"
                     /db_xref="CDD:434953"
     Region          1220..1328
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGN4; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1430..1451
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          <1461..1593
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1462..1495
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1463..1494
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1464,1468..1469,1472..1474,1476..1477,1481,1484,
                     1494,1496,1498,1502..1503,1506..1508,1510..1511,1515,1518,
                     1527,1529,1531,1535..1536,1539..1541,1543..1544,1548,1551)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1496..1527
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1496..1525
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1529..1558
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1529..1558
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1634..1748
                     /region_name="Necessary and sufficient for interaction
                     with PCGF1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1634..1747
                     /region_name="PUFD"
                     /note="BCORL-PCGF1-binding domain; pfam16553"
                     /db_xref="CDD:465171"
     Site            order(1636..1637,1639..1643,1645..1647,1649,1651,1660,
                     1662,1704..1706,1708..1709,1711..1712,1729,1740,1742,
                     1744..1746)
                     /site_type="other"
                     /note="RAWUL domain interface [polypeptide binding]"
                     /db_xref="CDD:271224"
     CDS             1..1755
                     /gene="BCOR"
                     /gene_synonym="ANOP2; MAA2; MCOPS2"
                     /coded_by="NM_001437510.1:312..5579"
                     /note="isoform c is encoded by transcript variant 7"
                     /db_xref="GeneID:54880"
                     /db_xref="HGNC:HGNC:20893"
                     /db_xref="MIM:300485"
ORIGIN      
        1 mlsatplygn vhswmnserv rmcgasedrk ilvndgdask arlelreenp lnhnvvdast
       61 ahridglaal smdrtglire glrvpgnivy sslcglgsek greaatstlg glgfssernp
      121 emqfkpntpe tveasavsgk ppngfsaiyk tppgiqksav ataealgldr pasdkqspln
      181 ingasylrlp wvnpymegat paiypfldsp nkyslnmyka llpqqsysla qplyspvctn
      241 gerflylppp hyvgphipss laspmrlstp saspaipplv hcadkslpwk mgvspgnpvd
      301 shayphiqns kqprvpsaka vtsglpgdta lllppsprps prvhlptqpa adtysefhkh
      361 yaristspsv alskpymtvs sefpaarlsn gkypkapegg egaqpvpgha rktavqdrkd
      421 gssppllekq tvtkdvtdkp ldlsskvvdv daskadhmkk maptvlvhsr agsglvlsgs
      481 eipketlspp gngcaiyrse iistapsswv vpgpspneen ngksmslknk aldwaipqqr
      541 ssscprmggt davitnvsgs vssagrpasa spapnanadg tktsrssvet tpsviqhvgq
      601 ppatpakhss stsskgakas npepsfkane nglppssifl spneafrspp ipyprsylpy
      661 papegiavsp lslhgkgpvy phpvllpngs lfpghlapkp glpyglptgr pefvtyqdal
      721 glgmvhpmli phtpieitke ekperrsrsh eraryedptl rnrfseilet sstklhpdvp
      781 tdknlkpnpn wnqgktvvks dklvyvdllr eepdaktdtn vskpsfaaes vgqsaeppkp
      841 svepalqqhr dfialreelg risdfhetyt fkqpvftvsk dsvlagtnke nlglpvstpf
      901 lepplgsdgp avtfgktqed pkpfcvgsap psvdvtptyt kdgadeaesn dgkvlkpkps
      961 klakriansa gyvgdrfkcv ttelyadssq lsreqralqm eglqedsilc lpaayceram
     1021 mrfselemke regghpatkd semckfspad werlkgnqdk kpksvtleea iaeqneserc
     1081 eysvgnkhrd pfeapedkdl pvekyfverq pvseppadqv asdmphsptl rvdrkrkvsg
     1141 dsshtettae evpedpllka krrrvskddw peremtnsss nhledphyse ltnlkvciel
     1201 tglhpkkqrh llhlrerweq qvsaadgkpg rqsrkevtqa tqpeaipqgt niteekpgrk
     1261 raeakgnrsw seeslkpsdn eqglpvfsgs ppmkslssts aggkkqaqps capasrppak
     1321 qqkikenqkt dvlcadeeed cqaasllqky tdnsekpsgk rlcktkhlip qesrrglplt
     1381 geyyvenadg kvtvrrfrkr pepssdydls pakqepkpfd rlqqllpasq stqlpcsssp
     1441 qettqsrpmp pearrlivnk nagetllqra arlgyeevvl yclenkicdv nhrdnagyca
     1501 lheacargwl nivrhlleyg advncsaqdg trplhdaven dhleivrlll sygadptlat
     1561 ysgrtimkmt hselmekflt dylndlqgrn dddasgtwdf ygssvcepdd esgydvlanp
     1621 pgpedqdddd daysdvfefe fsetpllpcy niqvsvaqgp rnwlllsdvl kklkmssrif
     1681 rcnfpnveiv tiaeaefyrq vsasllfscs kdleafnpes kelldlveft neiqtllgss
     1741 vewlhpsdla sdnyw
//
LOCUS       NP_001412004             492 aa            linear   PRI 21-NOV-2025
DEFINITION  coatomer subunit delta isoform 5 [Homo sapiens].
ACCESSION   NP_001412004
VERSION     NP_001412004.1
DBSOURCE    REFSEQ: accession NM_001425075.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   O'Donoghue,L., Comer,S.P., Hiebner,D.W., Schoen,I., von
            Kriegsheim,A. and Smolenski,A.
  TITLE     RhoGAP6 interacts with COPI to regulate protein transport
  JOURNAL   Biochem J 480 (14), 1109-1127 (2023)
   PUBMED   37409526
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Li,W., Liang,J., Outeda,P., Turner,S., Wakimoto,B.T. and Watnick,T.
  TITLE     A genetic screen in Drosophila reveals an unexpected role for the
            KIP1 ubiquitination-promoting complex in male fertility
  JOURNAL   PLoS Genet 16 (12), e1009217 (2020)
   PUBMED   33378371
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Tidwell,T., Deshotel,M., Palumbos,J., Miller,C., Bayrak-Toydemir,P.
            and Carey,J.C.
  TITLE     Novel de novo ARCN1 intronic variant causes rhizomelic short
            stature with microretrognathia and developmental delay
  JOURNAL   Cold Spring Harb Mol Case Stud 6 (6), a005728 (2020)
   PUBMED   33154040
  REMARK    GeneRIF: Novel de novo ARCN1 intronic variant causes rhizomelic
            short stature with microretrognathia and developmental delay.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 492)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 492)
  AUTHORS   Schekman,R. and Orci,L.
  TITLE     Coat proteins and vesicle budding
  JOURNAL   Science 271 (5255), 1526-1533 (1996)
   PUBMED   8599108
  REMARK    Review article
REFERENCE   7  (residues 1 to 492)
  AUTHORS   Cukierman,E., Huber,I., Rotman,M. and Cassel,D.
  TITLE     The ARF1 GTPase-activating protein: zinc finger motif and Golgi
            complex localization
  JOURNAL   Science 270 (5244), 1999-2002 (1995)
   PUBMED   8533093
REFERENCE   8  (residues 1 to 492)
  AUTHORS   Radice,P., Pensotti,V., Jones,C., Perry,H., Pierotti,M.A. and
            Tunnacliffe,A.
  TITLE     The human archain gene, ARCN1, has highly conserved homologs in
            rice and Drosophila
  JOURNAL   Genomics 26 (1), 101-106 (1995)
   PUBMED   7782067
REFERENCE   9  (residues 1 to 492)
  AUTHORS   Orcl,L., Palmer,D.J., Amherdt,M. and Rothman,J.E.
  TITLE     Coated vesicle assembly in the Golgi requires only coatomer and ARF
            proteins from the cytosol
  JOURNAL   Nature 364 (6439), 732-734 (1993)
   PUBMED   8355790
REFERENCE   10 (residues 1 to 492)
  AUTHORS   Waters,M.G., Serafini,T. and Rothman,J.E.
  TITLE     'Coatomer': a cytosolic protein complex containing subunits of
            non-clathrin-coated Golgi transport vesicles
  JOURNAL   Nature 349 (6306), 248-251 (1991)
   PUBMED   1898986
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000941.6.
            
            Summary: This gene maps in a region, which include the mixed
            lineage leukemia and Friend leukemia virus integration 1 genes,
            where multiple disease-associated chromosome translocations occur.
            It is an intracellular protein. Archain sequences are well
            conserved among eukaryotes and this protein may play a fundamental
            role in eukaryotic cell biology. It has similarities to heat shock
            proteins and clathrin-associated proteins, and may be involved in
            vesicle structure or trafficking. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3319412.1,
                                           SRR14038197.484833.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146982, SAMEA2155751
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..492
                     /product="coatomer subunit delta isoform 5"
                     /note="coatomer protein delta-COP; coatomer protein
                     complex, subunit delta; archain vesicle transport protein
                     1; coatomer delta subunit; delta-coat protein; COPI coat
                     complex subunit delta"
                     /calculated_mol_wt=55198
     Region          2..114
                     /region_name="Delta_COP_N"
                     /note="delta subunit of the F-COPI complex, N-terminal
                     domain; cd14830"
                     /db_xref="CDD:341434"
     Region          253..489
                     /region_name="AP_delta-COPI_MHD"
                     /note="Mu homology domain (MHD) of adaptor protein (AP)
                     coat protein I (COPI) delta subunit; cd09254"
                     /db_xref="CDD:271162"
     CDS             1..492
                     /gene="ARCN1"
                     /gene_synonym="COPD; SRMMD; SSMG"
                     /coded_by="NM_001425075.1:140..1618"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:372"
                     /db_xref="HGNC:HGNC:649"
                     /db_xref="MIM:600820"
ORIGIN      
        1 mfvemtrtri egllaafpkl mntgkqhtfv etesvryvyq pmeklymvli ttknsniled
       61 letlrlfsrv ipeycralee neisehcfdl ifafdeival gyrenvnlaq irtftemdsh
      121 eekvfravre tqereakaem rrkakelqqa rrdaerqgkk apgfggfgss avsggstaam
      181 itetiietdk pkvapaparp sgpskalklg akgkevdnfv dklksegeti msssmgkrts
      241 eatkmhappi nmesvhmkie ekitltcgrd gglqnmelhg mimlrisddk ygrirlhven
      301 edkkgvqlqt hpnvdkklft aesliglknp eksfpvnsdv gvlkwrlqtt eesfipltin
      361 cwpsesgngc dvnieyelqe dnlelndvvi tiplpsgvga pvigeidgey rhdsrrntle
      421 wclpvidakn ksgslefsia gqpndffpvq vsfvskknyc niqvtkvtqv dgnspvrfst
      481 ettflvdkye il
//
LOCUS       NP_001427589             554 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 3 isoform 9 [Homo sapiens].
ACCESSION   NP_001427589
VERSION     NP_001427589.1
DBSOURCE    REFSEQ: accession NM_001440660.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Ghashghaei,M., Liu,Y., Ettles,J., Bombaci,G., Ramkumar,N., Liu,Z.,
            Escano,L., Miko,S.S., Kim,Y., Waldron,J.A., Do,K., MacPherson,K.,
            Yuen,K.A., Taibi,T., Yue,M., Arsalan,A., Jin,Z., Edin,G.,
            Karsan,A., Morin,G.B., Kuchenbauer,F., Perna,F., Bushell,M. and
            Vu,L.P.
  TITLE     Translation efficiency driven by CNOT3 subunit of the CCR4-NOT
            complex promotes leukemogenesis
  JOURNAL   Nat Commun 15 (1), 2340 (2024)
   PUBMED   38491013
  REMARK    GeneRIF: Translation efficiency driven by CNOT3 subunit of the
            CCR4-NOT complex promotes leukemogenesis.
            Erratum:[Nat Commun. 2024 Oct 7;15(1):8674. doi:
            10.1038/s41467-024-53071-1. PMID: 39375334]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Burgess,H.M., Grande,R., Riccio,S., Dinesh,I., Winkler,G.S.,
            Depledge,D.P. and Mohr,I.
  TITLE     CCR4-NOT differentially controls host versus virus poly(a)-tail
            length and regulates HCMV infection
  JOURNAL   EMBO Rep 24 (12), e56327 (2023)
   PUBMED   37846490
  REMARK    GeneRIF: CCR4-NOT differentially controls host versus virus
            poly(a)-tail length and regulates HCMV infection.
REFERENCE   4  (residues 1 to 554)
  AUTHORS   Zhao,P., Meng,Q., Wan,C., Lei,T., Zhang,L., Zhang,X., Tan,L.,
            Zhu,H. and He,X.
  TITLE     Clinical features of CNOT3-associated neurodevelopmental disorder
            in three Chinese patients
  JOURNAL   Neurogenetics 24 (2), 129-136 (2023)
   PUBMED   36802310
  REMARK    GeneRIF: Clinical features of CNOT3-associated neurodevelopmental
            disorder in three Chinese patients.
REFERENCE   5  (residues 1 to 554)
  AUTHORS   McLenachan,S., Zhang,D., Grainok,J., Zhang,X., Huang,Z., Chen,S.C.,
            Zaw,K., Lima,A., Jennings,L., Roshandel,D., Moon,S.Y., Heath
            Jeffery,R.C., Attia,M.S., Thompson,J.A., Lamey,T.M., McLaren,T.L.,
            De Roach,J., Fletcher,S. and Chen,F.K.
  TITLE     Determinants of Disease Penetrance in PRPF31-Associated Retinopathy
  JOURNAL   Genes (Basel) 12 (10), 1542 (2021)
   PUBMED   34680937
  REMARK    GeneRIF: Determinants of Disease Penetrance in PRPF31-Associated
            Retinopathy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 554)
  AUTHORS   Yin,X., Warner,D.R., Roberts,E.A., Pisano,M.M. and Greene,R.M.
  TITLE     Identification of novel CBP interacting proteins in embryonic
            orofacial tissue
  JOURNAL   Biochem Biophys Res Commun 329 (3), 1010-1017 (2005)
   PUBMED   15752756
REFERENCE   7  (residues 1 to 554)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 554)
  AUTHORS   Aoki,T., Okada,N., Wakamatsu,T. and Tamura,T.A.
  TITLE     TBP-interacting protein 120B, which is induced in relation to
            myogenesis, binds to NOT3
  JOURNAL   Biochem Biophys Res Commun 296 (5), 1097-1103 (2002)
   PUBMED   12207886
  REMARK    GeneRIF: TBP-interacting protein 120B binds to NOT3
REFERENCE   9  (residues 1 to 554)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
REFERENCE   10 (residues 1 to 554)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC245052.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2187122.1,
                                           SRR14038194.39757.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..554
                     /product="CCR4-NOT transcription complex subunit 3 isoform
                     9"
                     /note="NOT3 (negative regulator of transcription 3, yeast)
                     homolog; CCR4-associated factor 3; leukocyte receptor
                     cluster member 2"
                     /calculated_mol_wt=57558
     Region          <2..48
                     /region_name="Not3"
                     /note="Not1 N-terminal domain, CCR4-Not complex component;
                     pfam04065"
                     /db_xref="CDD:461155"
     Region          439..540
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..554
                     /gene="CNOT3"
                     /gene_synonym="IDDSADF; LENG2; NOT3; NOT3H"
                     /coded_by="NM_001440660.1:882..2546"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:4849"
                     /db_xref="HGNC:HGNC:7879"
                     /db_xref="MIM:604910"
ORIGIN      
        1 mletilrmld ndsilvdair kikddveyyv dssqdpdfee neflyddldl edipqalvat
       61 sppshshmed eifnqssstp tsttssspip pspanctten seddkkrgrs tdsevsqspa
      121 kngskpvhsn qhpqspavpp typsgpppaa salsttpgnn gvpapaapps algpkaspap
      181 shnsgtpapy aqavappaps gpsttqprpp svqpsggggg gsggggssss snssagggag
      241 kqngatsyss vvadspaeva lsssggnnas sqalgppsgp hnpppstske psaaaptgag
      301 gvapgsgnns ggpsllvplp vnppssptps fsdakaagal lngppqfsta peikapepls
      361 slksmaeraa issgiedpvp tlhlterdii lsstsappas aqpplqlsev niplslgvcp
      421 lgpvpltkeq lyqqameeaa whhmphpsds erirqylprn pcptppyhhq mppphsdtve
      481 fyqrlstetl ffifyylegt kaqylaakal kkqswrfhtk ymmwfqrhee pktitdefeq
      541 vrappplfpl lglg
//
LOCUS       NP_001411048             321 aa            linear   PRI 21-NOV-2025
DEFINITION  radial spoke head protein 9 homolog isoform 3 [Homo sapiens].
ACCESSION   NP_001411048
VERSION     NP_001411048.1
DBSOURCE    REFSEQ: accession NM_001424119.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Hwang,J.Y., Chai,P., Nawaz,S., Choi,J., Lopez-Giraldez,F.,
            Hussain,S., Bilguvar,K., Mane,S., Lifton,R.P., Ahmad,W., Zhang,K.
            and Chung,J.J.
  TITLE     LRRC23 truncation impairs radial spoke 3 head assembly and sperm
            motility underlying male infertility
  JOURNAL   Elife 12, 90095 (2023)
   PUBMED   38091523
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Zhang,X., Xiao,Z., Zhang,J., Xu,C., Liu,S., Cheng,L., Zhou,S.,
            Zhao,S., Zhang,Y., Wu,J., Wang,Y. and Liu,M.
  TITLE     Differential requirements of IQUB for the assembly of radial spoke
            1 and the motility of mouse cilia and flagella
  JOURNAL   Cell Rep 41 (8), 111683 (2022)
   PUBMED   36417862
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Zhu,L., Liu,H., Chen,Y., Yan,X. and Zhu,X.
  TITLE     Rsph9 is critical for ciliary radial spoke assembly and central
            pair microtubule stability
  JOURNAL   Biol Cell 111 (2), 29-38 (2019)
   PUBMED   30383886
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Zietkiewicz,E., Bukowy-Bieryllo,Z., Voelkel,K., Klimek,B.,
            Dmenska,H., Pogorzelski,A., Sulikowska-Rowinska,A., Rutkiewicz,E.
            and Witt,M.
  TITLE     Mutations in radial spoke head genes and ultrastructural cilia
            defects in East-European cohort of primary ciliary dyskinesia
            patients
  JOURNAL   PLoS One 7 (3), e33667 (2012)
   PUBMED   22448264
  REMARK    GeneRIF: Mutations in RSPH9 leads to ultrastructural cilia defects
            and ciliary dyskinesia.
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Reish,O., Slatkin,M., Chapman-Shimshoni,D., Elizur,A., Chioza,B.,
            Castleman,V. and Mitchison,H.M.
  TITLE     Founder mutation(s) in the RSPH9 gene leading to primary ciliary
            dyskinesia in two inbred Bedouin families
  JOURNAL   Ann Hum Genet 74 (2), 117-125 (2010)
   PUBMED   20070851
  REMARK    GeneRIF: Study focused on an extended 5 generation Bedouin family,
            analysed mutation segregation, and calculated the age of the
            mutated allele in 2 families based on haplotypes and
            haplotype+microsatellite in an attempt to define the source of the
            mutation.
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Castleman,V.H., Romio,L., Chodhari,R., Hirst,R.A., de Castro,S.C.,
            Parker,K.A., Ybot-Gonzalez,P., Emes,R.D., Wilson,S.W., Wallis,C.,
            Johnson,C.A., Herrera,R.J., Rutman,A., Dixon,M., Shoemark,A.,
            Bush,A., Hogg,C., Gardiner,R.M., Reish,O., Greene,N.D.,
            O'Callaghan,C., Purton,S., Chung,E.M. and Mitchison,H.M.
  TITLE     Mutations in radial spoke head protein genes RSPH9 and RSPH4A cause
            primary ciliary dyskinesia with central-microtubular-pair
            abnormalities
  JOURNAL   Am J Hum Genet 84 (2), 197-209 (2009)
   PUBMED   19200523
REFERENCE   9  (residues 1 to 321)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136131.15.
            
            Summary: This gene encodes a protein thought to be a component of
            the radial spoke head in motile cilia and flagella. Mutations in
            this gene are associated with primary ciliary dyskinesia 12.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Jul 2010].
            
            Transcript Variant: This variant (3) encodes the longest isoform
            (3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.97624.1,
                                           DRR138524.72309.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..321
                     /product="radial spoke head protein 9 homolog isoform 3"
                     /note="radial spoke head protein 9 homolog; radial spoke
                     head 9 homolog"
                     /calculated_mol_wt=36038
     Region          <17..>106
                     /region_name="Radial_spoke"
                     /note="Radial spokehead-like protein; pfam04712"
                     /db_xref="CDD:461405"
     CDS             1..321
                     /gene="RSPH9"
                     /gene_synonym="C6orf206; CILD12; MRPS18AL1"
                     /coded_by="NM_001424119.1:64..1029"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:221421"
                     /db_xref="HGNC:HGNC:21057"
                     /db_xref="MIM:612648"
ORIGIN      
        1 mdadslllsl elasgsgqgl spdrrasllt slmlvkrdyr ydrvlfwgri lglvadyyia
       61 qglsedqlap rktlyslnct ewsllppate emvaqssvvk grfmgdpsye yehtelqkvn
      121 egekvfeeei vvqikeetrl vsvidqidka vaiiprgalf ktpfgpthvn rtfeglslse
      181 akklssyfhf repvelknkt llekadldps ldfmdslehd ipkgseavvq gdftwllsrc
      241 gfgwpcswds csvsmrvleh pdgegqcpgg aaqpalagph llpcsphqel wlrlrghwre
      301 ehglalhaie wepawmflnr v
//
LOCUS       NP_001393918             552 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform I [Homo sapiens].
ACCESSION   NP_001393918 XP_011507835
VERSION     NP_001393918.1
DBSOURCE    REFSEQ: accession NM_001406989.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 552)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 552)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 552)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 552)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 552)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 552)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 552)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 552)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            On May 24, 2022 this sequence version replaced XP_011507835.1.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1903137.1,
                                           SRR18074967.3762701.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2146982
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..552
                     /product="lamin isoform I"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=61177
     Region          17..274
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          322..429
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     CDS             1..552
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406989.1:35..1693"
                     /note="isoform I is encoded by transcript variant 16"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 mgnsegcntk kegdliaaqa rlkdlealln skeaalstal sekrtlegel hdlrgqvakl
       61 eaalgeakkq lqdemlrrvd aenrlqtmke eldfqkniys eelretkrrh etrlveidng
      121 kqrefesrla dalqelraqh edqveqykke lektysakld narqsaerns nlvgaaheel
      181 qqsriridsl saqlsqlqkq laakeaklrd ledslarerd tsrrllaeke remaemrarm
      241 qqqldeyqel ldiklaldme ihayrklleg eeerlrlsps ptsqrsrgra sshssqtqgg
      301 gsvtkkrkle stesrssfsq hartsgrvav eevdeegkfv rlrnksnedq smgnwqikrq
      361 ngddplltyr fppkftlkag qvvtiwaaga gathspptdl vwkaqntwgc gnslrtalin
      421 stgeevamrk lvrsvtvved dededgddll hhhhgshcss sgdpaeynlr srtvlcgtcg
      481 qpadkasasg sgaqvggpis sgssassvtv trsyrsvggs gggsfgdnlv trsyllgnss
      541 prtqspqncs im
//
LOCUS       NP_001400235             197 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 13 [Homo sapiens].
ACCESSION   NP_001400235
VERSION     NP_001400235.1
DBSOURCE    REFSEQ: accession NM_001413306.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 197)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 197)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 197)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 197)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 197)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 197)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.23522.1,
                                           SRR1803616.60835.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1970526 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..197
                     /product="RNA-binding Raly-like protein isoform 13"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=21669
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     CDS             1..197
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413306.1:329..922"
                     /note="isoform 13 is encoded by transcript variant 33"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly rleskepfls
      121 vggyvfdydy yrddfynrlf dyhgrvpppp raviplkrpr vavtttrrgk gvfsmkggsr
      181 stasgstgsk fstdkvi
//
LOCUS       NP_001427977            4358 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HUWE1 isoform 2 [Homo sapiens].
ACCESSION   NP_001427977 XP_047297700 XP_054182296
VERSION     NP_001427977.1
DBSOURCE    REFSEQ: accession NM_001441048.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4358)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 4358)
  AUTHORS   Lee,C., Park,S.H. and Yoon,S.K.
  TITLE     The E3 ligase HUWE1 increases the sensitivity of CRC to oxaliplatin
            through TOMM20 degradation
  JOURNAL   Oncogene 43 (9), 636-649 (2024)
   PUBMED   38184713
  REMARK    GeneRIF: The E3 ligase HUWE1 increases the sensitivity of CRC to
            oxaliplatin through TOMM20 degradation.
REFERENCE   3  (residues 1 to 4358)
  AUTHORS   Li,X.X., Xu,J.K., Su,W.J., Wu,H.L., Zhao,K., Zhang,C.M., Chen,X.K.
            and Yang,L.X.
  TITLE     The role of KDM4A-mediated histone methylation on temozolomide
            resistance in glioma cells through the HUWE1/ROCK2 axis
  JOURNAL   Kaohsiung J Med Sci 40 (2), 161-174 (2024)
   PUBMED   37873881
  REMARK    GeneRIF: The role of KDM4A-mediated histone methylation on
            temozolomide resistance in glioma cells through the HUWE1/ROCK2
            axis.
REFERENCE   4  (residues 1 to 4358)
  AUTHORS   Bernassola,F., Karin,M., Ciechanover,A. and Melino,G.
  TITLE     The HECT family of E3 ubiquitin ligases: multiple players in cancer
            development
  JOURNAL   Cancer Cell 14 (1), 10-21 (2008)
   PUBMED   18598940
  REMARK    Review article
REFERENCE   5  (residues 1 to 4358)
  AUTHORS   Zhong,Q., Gao,W., Du,F. and Wang,X.
  TITLE     Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the
            polyubiquitination of Mcl-1 and regulates apoptosis
  JOURNAL   Cell 121 (7), 1085-1095 (2005)
   PUBMED   15989957
  REMARK    GeneRIF: Mule is both required and sufficient for the
            polyubiquitination of Mcl-1; Mule is a unique BH3-containing E3
            ubiquitin ligase apical to Bcl-2 family proteins during DNA
            damage-induced apoptosis
            GeneRIF: Mule (HUWE1) poly-ubiquitinates anti-apoptotic gene Mcl-1.
REFERENCE   6  (residues 1 to 4358)
  AUTHORS   Chen,D., Kon,N., Li,M., Zhang,W., Qin,J. and Gu,W.
  TITLE     ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
  JOURNAL   Cell 121 (7), 1071-1083 (2005)
   PUBMED   15989956
  REMARK    GeneRIF: study modifies the current view of ARF-mediated p53
            activation and reveals that ARF-BP1 is a critical mediator of both
            the p53-independent and p53-dependent tumor suppressor functions of
            ARF
            GeneRIF: Ubiquitin ligase activity of ARF-BP1 (HUWE1) is inhibited
            by Arf.
REFERENCE   7  (residues 1 to 4358)
  AUTHORS   Liu,Z., Oughtred,R. and Wing,S.S.
  TITLE     Characterization of E3Histone, a novel testis ubiquitin protein
            ligase which ubiquitinates histones
  JOURNAL   Mol Cell Biol 25 (7), 2819-2831 (2005)
   PUBMED   15767685
REFERENCE   8  (residues 1 to 4358)
  AUTHORS   Gu,J., Dubner,R., Fornace,A.J. Jr. and Iadarola,M.J.
  TITLE     UREB1, a tyrosine phosphorylated nuclear protein, inhibits p53
            transactivation
  JOURNAL   Oncogene 11 (10), 2175-2178 (1995)
   PUBMED   7478539
REFERENCE   9  (residues 1 to 4358)
  AUTHORS   Turner,G., Gedeon,A. and Mulley,J.
  TITLE     X-linked mental retardation with heterozygous expression and
            macrocephaly: pericentromeric gene localization
  JOURNAL   Am J Med Genet 51 (4), 575-580 (1994)
   PUBMED   7943042
REFERENCE   10 (residues 1 to 4358)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX323845.7 and AC231658.3.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297700.1, XP_054182296.1.
            
            Summary: This gene encodes a protein containing a C-terminal HECT
            (E6AP type E3 ubiquitin protein ligase) domain that functions as an
            E3 ubiquitin ligase. The encoded protein is required for the
            ubiquitination and subsequent degradation of the anti-apoptotic
            protein Mcl1 (myeloid cell leukemia sequence 1 (BCL2-related)).
            This protein also ubiquitinates the p53 tumor suppressor, core
            histones, and DNA polymerase beta. Mutations in this gene are
            associated with Turner type X-linked syndromic cognitive
            disability. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.728067.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..4358
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..4358
                     /product="E3 ubiquitin-protein ligase HUWE1 isoform 2"
                     /EC_number="2.3.2.26"
                     /note="Mcl-1 ubiquitin ligase E3; BJ-HCC-24 tumor antigen;
                     HECT domain protein LASU1; ARF-binding protein 1;
                     URE-binding protein 1; large structure of UREB1; upstream
                     regulatory element-binding protein 1; homologous to E6AP
                     carboxyl terminus homologous protein 9; HECT-type E3
                     ubiquitin transferase HUWE1; HECT, UBA and WWE domain
                     containing 1, E3 ubiquitin protein ligase"
                     /calculated_mol_wt=479954
     Region          92..367
                     /region_name="DUF908"
                     /note="Domain of Unknown Function (DUF908); pfam06012"
                     /db_xref="CDD:428721"
     Region          431..814
                     /region_name="DUF913"
                     /note="Domain of Unknown Function (DUF913); pfam06025"
                     /db_xref="CDD:461803"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          706..759
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          978..1001
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1014..1037
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1084
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1291..1320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1317..1356
                     /region_name="UBA_HUWE1"
                     /note="UBA domain found in eukaryotic E3 ubiquitin-protein
                     ligase HUWE1 and similar proteins; cd14288"
                     /db_xref="CDD:270474"
     Site            1368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1396..1415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1617..1678
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          1689..1735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1722
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1907
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2017..2064
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2034
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2261..2341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2266
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2355..2479
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2534
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2553
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2594
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2618
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2693..2969
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          <2734..3065
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            2750
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2825
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2832
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2860
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2886
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2887
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2888
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2917
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3009..3042
                     /region_name="UBM"
                     /note="Ubiquitin binding region; pfam14377"
                     /db_xref="CDD:464159"
     Region          3035..3058
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3148
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3244..3266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3403..3423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3470..3511
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3536..3567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3736..3757
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3751
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3792
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3800
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3811
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3814
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3878..3915
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3890
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3903
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3908
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3911
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          4003..4356
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(4007,4037,4048,4109,4283,4319..4320,4323..4327,4347,
                     4355)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(4137,4140..4141,4143..4144,4147,4154,4156,
                     4160..4161,4163,4168,4173,4190,4194)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     Site            4255
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P51593; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     CDS             1..4358
                     /gene="HUWE1"
                     /gene_synonym="ARF-BP1; HECTH9; HSPC272; Ib772; LASU1;
                     MRXST; MULE; URE-B1; UREB1"
                     /coded_by="NM_001441048.1:394..13470"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:10075"
                     /db_xref="HGNC:HGNC:30892"
                     /db_xref="MIM:300697"
ORIGIN      
        1 mkvdrtklkk tpteapadcr alidklkvcn deqlllelqq iktwnigkce lyhwvdlldr
       61 fdgiladagq tvenmswmlv cdrpereqlk mlllavlnft allieysfsr hlyssiehlt
      121 tllassdmqv vlavlnllyv fskrsnyitr lgsdkrtpll trlqhlaesw ggkengfgla
      181 eccrdlhmmk yppsattlhf efyadpgaev kiekrttsnt lhyihieqld kisespseim
      241 esltkmysip kdkqmllfth irlahgfsnh rkrlqavqar lhaisilvys nalqesansi
      301 lynglieelv dvlqitdkql meikaaslrt ltsivhlert pklssiidct gtasyhgflp
      361 vlvrnciqam idpsmdpyph qfatalfsfl yhlasydagg ealvscgmme allkvikflg
      421 deqdqitfvt ravrvvdlit nldmaafqsh sglsifiyrl ehevdlcrke cpfvikpkiq
      481 rpnttqegee metdmdgvqc ipqraallks mlnflkkaiq dpafsdgirh vmdgslptsl
      541 khiisnaeyy gpslfllate vvtvfvfqep sllsslqdng ltdvmlhall ikdvpatrev
      601 lgslpnvfsa lclnarglqs fvqcqpferl fkvllspdyl pamrrrrssd plgdtasnlg
      661 savdelmrhq ptlktdatta iiklleeicn lgrdpkyicq kpsiqkadgt atappprsnh
      721 aaeeassede eeeevqamqs fnstqqnete pnqqvvgtee ripiplmdyi lnvmkfvesi
      781 lsnnttddhc qefvnqkgll plvtilglpn lpidfptsaa cqavagvcks iltlshepkv
      841 lqegllqlds ilssleplhr piespggsvl lrelacagnv adatlsaqat pllhaltaah
      901 ayimmfvhtc rvgqseirsi svnqwgsqlg lsvlsklsql ycslvwestv llslctpnsl
      961 psgcefgqad mqklvpkdek agttqggkrs dgeqdgaags mdastqglle gigldgdtla
     1021 pmetdeptas dskgkskitp amaarikqik pllsassrlg ralaelfgll vklcvgspvr
     1081 qrrshhaast ttaptpaars tasaltkllt kglswqpppy tptprfrltf ficsvgftsp
     1141 mlfderkypy hlmlqkflcs gghnalfetf nwalsmggkv pvseglehsd lpdgtgefld
     1201 awlmlvekmv npttvlesph slpaklpggv qnfpqfsalr flvvtqkaaf tciknlwnrk
     1261 plkvyggrma esmlailchi lrgepvirer lskekegsrg eedtgqeegg srrepqvnqq
     1321 qlqqlmdmgf trehameall ntstmeqate yllthpppim ggvvrdlsms eedqmmraia
     1381 mslgqdipmd qraespeeva crkeeeerka rekqeeeeak clekfqdadp leqdelhtft
     1441 dtmlpgcfhl ldelpdtvyr vcdlimtaik rngadyrdmi lkqvvnqvwe aadvlikaal
     1501 plttsdtktv sewisqmatl pqasnlatri llltllfeel klpcawvves sgilnvlikl
     1561 levvqpclqa akeqkevqtp kwitpvllli dfyektaiss krraqmtkyl qsnsnnwrwf
     1621 ddrsgrwcsy sasnnstids awksgetsvr ftagrrrytv qfttmvqvne etgnrrpvml
     1681 tllrvprlnk nsknsngqel ektleeskem dikrkenkgn dtplalestn teketsleet
     1741 kigeiliqgl tedmvtvlir acvsmlgvpv dpdtlhatlr lclrltrdhk yammfaelks
     1801 trmilnltqs sgfngftplv tlllrhiied pctlrhtmek vvrsaatsga gsttsgvvsg
     1861 slgsreinyi lrvlgpaacr npdiftevan ccirialpap rgsgtasdde fenlrikgpn
     1921 avqlvkttpl kpsplpvipd tikeviydml nalaayhape edksdpkpgv mtqevgqllq
     1981 dmgddvyqqy rsltrqssdf dtqsgfsins qvfaadgast etsasgtsqg eastpeesrd
     2041 gkkdkegdra seegkqkgkg skplmptsti lrllaelvrs yvgiatlian ysytvgqsel
     2101 ikedcsvlaf vldhllphtq naedkdtpal arlflaslaa agsgtdaqva lvnevkaalg
     2161 ralamaeste kharlqavmc iistimescp stssfyssat aktqhngmnn iirlflkkgl
     2221 vndlarvphs ldlsspnman tvnaalkple tlsrivnqps slfgsksass knkseqdaqg
     2281 asqdsssnqq dpgepgeaev qeedhdvtqt evadgdimdg eaetdsvvia gqpevlssqe
     2341 mqveneledl idellerdgg sgnstiivsr sgedesqedv lmdeapsnls qastlqanre
     2401 dsmnildped eeehtqeeds sgsnededds qdeeeeeeed eeddqeddeg eegdeddddd
     2461 gsemeldedy pdmnasplvr ferfdreddl iiefdnmfss atdippspgn iptthplmvr
     2521 hadhssltlg sgssttrltq gigrsqrtlr qltantghti hvhypgnrqp npplilqrll
     2581 gpsaaadilq lssslplqsr grarllvgnd dvhiiarsdd ellddffhdq statsqagtl
     2641 ssiptaltrw teeckvldae smhdcvsvvk vsivnhlefl rdeeleerre krrkqlaeee
     2701 tkitdkgked kenrdqsaqc tasksndste qnlsdgtpmp dsypttpsst daatsesket
     2761 lgtlqssqqq ptlptppalg evpqelqspa geggsstqll mpvepeelgp trpsgeaett
     2821 qmelspapti tslsperaed sdaltavssq legspmdtss lasctleeav gdtsaagsse
     2881 qpragsstpg dappavaevq grsdgsgesa qppedssppa ssessstrds avaisgadsr
     2941 gileeplpst sseeedplag islpegvdps flaalpddir revlqnqlgi rpptrtapst
     3001 nssapavvgn pgvtevspef laalppaiqe evlaqqraeq qrrelaqnas sdtpmdpvtf
     3061 iqtlpsdlrr svledmedsv lavmppdiaa eaqalrreqe arqrqlmher lfghsstsal
     3121 sailrspaft srlsgnrgvq ytrlavqrgg tfqmggsssh nrpsgsnvdt llrlrgrlll
     3181 dhealscllv llfvdepkln tsrlhrvlrn lcyhaqtrhw virsllsilq rsseselcie
     3241 tpklttseek gkksskscgs sshenrpldl lhkmeskssn qlswlsvsmd aalgcrtnif
     3301 qiqrsggrkh tekhasggst vhihpqaapv vcrhvldtli qlakvfpshf tqqrtketnc
     3361 esdrergnka cspcssqsss sgictdfwdl lvkldnmnvs rkgknsvksv pvsaggeget
     3421 spysleaspl gqlmnmlshp virrssllte kllrllslis ialpenkvse aqansgsgas
     3481 stttatstts tttttaastt ptpptaptpv tsapalvaat aistivvaas ttvttpttat
     3541 ttvsispttk gskspakvsd ggssstdfkm vssgltenql qlsvevltsh scseegleda
     3601 anvllqlsrg dsgtrdtvlk lllngarhlg ytlckqigtl laelreynle qqrraqcetl
     3661 spdglpeeqp qttklkgkmq srfdmaenvv ivasqkrplg grelqlpsms mltsktstqk
     3721 fflrvlqvii qlrddtrran kkakqtgrlg ssglgsassi qaavrqleae adaiiqmses
     3781 sqseasvrre espmdvdqps psaqdtqsia sdgtpqgeke keerppelpl lseqlsldel
     3841 wdmlgeclke leeshdqhav lvlqpaveaf flvhateres kppvrdtres qlahikdepp
     3901 plspapltpa tpssldpffs repssmhiss slppdtqkfl rfaethrtvl nqilrqstth
     3961 ladgpfavlv dyirvldfdv krkyfrqele rldeglrked mavhvrrdhv fedsyrelhr
     4021 kspeemknrl yivfegeegq daggllrewy miisremfnp myalfrtspg drvtytinps
     4081 shcnpnhlsy fkfvgrivak avydnrllec yftrsfykhi lgksvrytdm esedyhfyqg
     4141 lvyllendvs tlgydltfst evqefgvcev rdlkpngani lvteenkkey vhlvcqmrmt
     4201 gairkqlaaf legfyeiipk rlisifteqe lellisglpt ididdlksnt eyhkyqsnsi
     4261 qiqwfwralr sfdqadrakf lqfvtgtskv plqgfaaleg mngiqkfqih rddrstdrlp
     4321 sahtcfnqld lpayesfekl rhmlllaiqe csegfgla
//
LOCUS       NP_001427993             709 aa            linear   PRI 21-NOV-2025
DEFINITION  inhibitor of nuclear factor kappa-B kinase subunit alpha isoform 6
            [Homo sapiens].
ACCESSION   NP_001427993
VERSION     NP_001427993.1
DBSOURCE    REFSEQ: accession NM_001441064.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Chen,X., Wu,W., Jeong,J.H., Rokavec,M., Wei,R., Feng,S.,
            Schroth,W., Brauch,H., Zhong,S. and Luo,J.L.
  TITLE     Cytokines-activated nuclear IKKalpha-FAT10 pathway induces breast
            cancer tamoxifen-resistance
  JOURNAL   Sci China Life Sci 67 (7), 1413-1426 (2024)
   PUBMED   38565741
  REMARK    GeneRIF: Cytokines-activated nuclear IKKalpha-FAT10 pathway induces
            breast cancer tamoxifen-resistance.
REFERENCE   3  (residues 1 to 709)
  AUTHORS   Chang,X., Guo,Y., Zhang,Q., Zheng,X., Cui,X., Hu,J., Zhang,Z.,
            Zhang,F. and Wang,X.
  TITLE     GRP78 recognizes EV-F 3D protein and activates NF-kappaB to repress
            virus replication by interacting with CHUK/IKBKB
  JOURNAL   J Virol 98 (6), e0026824 (2024)
   PUBMED   38775480
  REMARK    GeneRIF: GRP78 recognizes EV-F 3D protein and activates NF-kappaB
            to repress virus replication by interacting with CHUK/IKBKB.
REFERENCE   4  (residues 1 to 709)
  AUTHORS   McIntosh,K., Khalaf,Y.H., Craig,R., West,C., McCulloch,A.,
            Waghmare,A., Lawson,C., Chan,E.Y.W., Mackay,S., Paul,A. and
            Plevin,R.
  TITLE     IL-1beta stimulates a novel, IKKalpha -dependent, NIK -independent
            activation of non-canonical NFkappaB signalling
  JOURNAL   Cell Signal 107, 110684 (2023)
   PUBMED   37080443
  REMARK    GeneRIF: IL-1beta stimulates a novel, IKKalpha -dependent, NIK
            -independent activation of non-canonical NFkappaB signalling.
REFERENCE   5  (residues 1 to 709)
  AUTHORS   Yang,H., Espada,C.E., Phillips,S., Martinez,N., Kenney,A.D.,
            Yount,J.S., Xiong,Y. and Wu,L.
  TITLE     The host antiviral protein SAMHD1 suppresses NF-kappaB activation
            by interacting with the IKK complex during inflammatory responses
            and viral infection
  JOURNAL   J Biol Chem 299 (6), 104750 (2023)
   PUBMED   37100289
  REMARK    GeneRIF: The host antiviral protein SAMHD1 suppresses NF-kappaB
            activation by interacting with the IKK complex during inflammatory
            responses and viral infection.
REFERENCE   6  (residues 1 to 709)
  AUTHORS   Scherer,D.C., Brockman,J.A., Chen,Z., Maniatis,T. and Ballard,D.W.
  TITLE     Signal-induced degradation of I kappa B alpha requires
            site-specific ubiquitination
  JOURNAL   Proc Natl Acad Sci U S A 92 (24), 11259-11263 (1995)
   PUBMED   7479976
REFERENCE   7  (residues 1 to 709)
  AUTHORS   Mock,B.A., Connelly,M.A., McBride,O.W., Kozak,C.A. and Marcu,K.B.
  TITLE     CHUK, a conserved helix-loop-helix ubiquitous kinase, maps to human
            chromosome 10 and mouse chromosome 19
  JOURNAL   Genomics 27 (2), 348-351 (1995)
   PUBMED   7558004
REFERENCE   8  (residues 1 to 709)
  AUTHORS   Connelly,M.A. and Marcu,K.B.
  TITLE     CHUK, a new member of the helix-loop-helix and leucine zipper
            families of interacting proteins, contains a serine-threonine
            kinase catalytic domain
  JOURNAL   Cell Mol Biol Res 41 (6), 537-549 (1995)
   PUBMED   8777433
REFERENCE   9  (residues 1 to 709)
  AUTHORS   Ganchi,P.A., Sun,S.C., Greene,W.C. and Ballard,D.W.
  TITLE     A novel NF-kappa B complex containing p65 homodimers: implications
            for transcriptional control at the level of subunit dimerization
  JOURNAL   Mol Cell Biol 13 (12), 7826-7835 (1993)
   PUBMED   8246997
REFERENCE   10 (residues 1 to 709)
  AUTHORS   Ganchi,P.A., Sun,S.C., Greene,W.C. and Ballard,D.W.
  TITLE     I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B
            p65 and requires the transactivation domain to inhibit NF-kappa B
            p65 DNA binding
  JOURNAL   Mol Biol Cell 3 (12), 1339-1352 (1992)
   PUBMED   1493333
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138921.14.
            
            Summary: This gene encodes a member of the serine/threonine protein
            kinase family. The encoded protein, a component of a
            cytokine-activated protein complex that is an inhibitor of the
            essential transcription factor NF-kappa-B complex, phosphorylates
            sites that trigger the degradation of the inhibitor via the
            ubiquination pathway, thereby activating the transcription factor.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1528051.1,
                                           SRR1660809.201675.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.31"
     Protein         1..709
                     /product="inhibitor of nuclear factor kappa-B kinase
                     subunit alpha isoform 6"
                     /EC_number="2.7.11.10"
                     /note="I-kappa-B kinase-alpha; I-kappa-B kinase 1; Nuclear
                     factor NFkappaB inhibitor kinase alpha; IKK-a kinase; IkB
                     kinase alpha subunit; inhibitor of nuclear factor kappa-B
                     kinase subunit alpha; conserved helix-loop-helix
                     ubiquitous kinase; transcription factor 16"
                     /calculated_mol_wt=80384
     Region          21..309
                     /region_name="STKc_IKK_alpha"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha;
                     cd14039"
                     /db_xref="CDD:270941"
     Site            order(21..25,29,42,44,74,95..98,102,104,144,146,148..149,
                     151,165,168,183..186)
                     /site_type="active"
                     /db_xref="CDD:270941"
     Site            order(21..25,29,42,44,74,95..98,102,144,146,148..149,151,
                     165)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270941"
     Site            order(25,102,104,144,146,148,168,183..186)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270941"
     Site            order(108,110,114,117,218,223,251..252,254,260..263)
                     /site_type="other"
                     /note="putative SDD interface [polypeptide binding]"
                     /db_xref="CDD:270941"
     Site            164..186
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270941"
     Region          311..373
                     /region_name="Ubl_IKKA_like"
                     /note="ubiquitin-like (Ubl) domain found in inhibitor of
                     nuclear factor kappa-B kinases, IKK-alpha and IKK-beta,
                     and similar proteins; cd17046"
                     /db_xref="CDD:340566"
     Region          377..623
                     /region_name="IKBKB_SDD"
                     /note="IQBAL scaffold dimerization domain; pfam18397"
                     /db_xref="CDD:465745"
     Region          671..707
                     /region_name="IKKbetaNEMObind"
                     /note="I-kappa-kinase-beta NEMO binding domain; pfam12179"
                     /db_xref="CDD:463485"
     CDS             1..709
                     /gene="CHUK"
                     /gene_synonym="BPS2; IKBKA; IKK-1; IKK-alpha; IKK1; IKKA;
                     NFKBIKA; TCF16"
                     /coded_by="NM_001441064.1:65..2194"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:1147"
                     /db_xref="HGNC:HGNC:1974"
                     /db_xref="MIM:600664"
ORIGIN      
        1 merppglrpg aggpwemrer lgtggfgnvc lyqhreldlk iaikscrlel stknrerwch
       61 eiqimkklnh anvvkacdvp eelnilihdv pllameycsg gdlrkllnkp enccglkesq
      121 ilsllsdigs girylhenki ihrdlkpeni vlqdvggkii hkiidlgyak dvdqgslcts
      181 fvgtlqylap elfenkpyta tvdywsfgtm vfeciagyrp flhhlqpftw hekikkkdpk
      241 cifaceemsg evrfsshlpq pnslcslvve pmenwlqlml nwdpqqrggp vdltlkqprc
      301 fvlmdhilnl kivhilnmts akiisfllpp deslhslqsr ieretgintg sqellsetgi
      361 sldprkpasq cvldgvdski qlpiiqlrkv waeavhyvsg lkedysrlfq gqraamlsll
      421 rynanltkmk ntlisasqql kakleffhks iqldleryse qmtygissek mlkawkemee
      481 kaihyaevgv igyledqims lhaeimelqk spygrrqgdl mesleqraid lykqlkhrps
      541 dhsysdstem vkiivhtvqs qdrvlkelfg hlskllgckq kiidllpkve valsnikead
      601 ntvmfmqgkr qkeiwhllki actqssarsl vgsslegavt pqtsawlppt saehdhslsc
      661 vvtpqdgets aqmieenlnc lghlstiihe aneeqgnsmm nldwswlte
//
LOCUS       NP_001400297             315 aa            linear   PRI 21-NOV-2025
DEFINITION  telomeric repeat-binding factor 1 isoform 8 [Homo sapiens].
ACCESSION   NP_001400297
VERSION     NP_001400297.1
DBSOURCE    REFSEQ: accession NM_001413368.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Hu,H., van Roon,A.M., Ghanim,G.E., Ahsan,B., Oluwole,A.O.,
            Peak-Chew,S.Y., Robinson,C.V. and Nguyen,T.H.D.
  TITLE     Structural basis of telomeric nucleosome recognition by shelterin
            factor TRF1
  JOURNAL   Sci Adv 9 (34), eadi4148 (2023)
   PUBMED   37624885
  REMARK    GeneRIF: Structural basis of telomeric nucleosome recognition by
            shelterin factor TRF1.
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Harmak,H., Redouane,S., Charoute,H., Aniq Filali,O., Barakat,A. and
            Rouba,H.
  TITLE     In silico exploration and molecular dynamics of deleterious SNPs on
            the human TERF1 protein triggering male infertility
  JOURNAL   J Biomol Struct Dyn 41 (24), 14665-14688 (2023)
   PUBMED   36995171
  REMARK    GeneRIF: In silico exploration and molecular dynamics of
            deleterious SNPs on the human TERF1 protein triggering male
            infertility.
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Abreu,P.L., Lee,Y.W. and Azzalin,C.M.
  TITLE     In Vitro Characterization of the Physical Interactions between the
            Long Noncoding RNA TERRA and the Telomeric Proteins TRF1 and TRF2
  JOURNAL   Int J Mol Sci 23 (18), 10463 (2022)
   PUBMED   36142374
  REMARK    GeneRIF: In Vitro Characterization of the Physical Interactions
            between the Long Noncoding RNA TERRA and the Telomeric Proteins
            TRF1 and TRF2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Jack,A., Kim,Y., Strom,A.R., Lee,D.S.W., Williams,B., Schaub,J.M.,
            Kellogg,E.H., Finkelstein,I.J., Ferro,L.S., Yildiz,A. and
            Brangwynne,C.P.
  TITLE     Compartmentalization of telomeres through DNA-scaffolded phase
            separation
  JOURNAL   Dev Cell 57 (2), 277-290 (2022)
   PUBMED   35077681
  REMARK    GeneRIF: Compartmentalization of telomeres through DNA-scaffolded
            phase separation.
REFERENCE   6  (residues 1 to 315)
  AUTHORS   Broccoli,D., Chong,L., Oelmann,S., Fernald,A.A., Marziliano,N., van
            Steensel,B., Kipling,D., Le Beau,M.M. and de Lange,T.
  TITLE     Comparison of the human and mouse genes encoding the telomeric
            protein, TRF1: chromosomal localization, expression and conserved
            protein domains
  JOURNAL   Hum Mol Genet 6 (1), 69-76 (1997)
   PUBMED   9002672
REFERENCE   7  (residues 1 to 315)
  AUTHORS   Lu,K.P., Hanes,S.D. and Hunter,T.
  TITLE     A human peptidyl-prolyl isomerase essential for regulation of
            mitosis
  JOURNAL   Nature 380 (6574), 544-547 (1996)
   PUBMED   8606777
REFERENCE   8  (residues 1 to 315)
  AUTHORS   Bilaud,T., Koering,C.E., Binet-Brasselet,E., Ancelin,K.,
            Pollice,A., Gasser,S.M. and Gilson,E.
  TITLE     The telobox, a Myb-related telomeric DNA binding motif found in
            proteins from yeast, plants and human
  JOURNAL   Nucleic Acids Res 24 (7), 1294-1303 (1996)
   PUBMED   8614633
REFERENCE   9  (residues 1 to 315)
  AUTHORS   Chong,L., van Steensel,B., Broccoli,D., Erdjument-Bromage,H.,
            Hanish,J., Tempst,P. and de Lange,T.
  TITLE     A human telomeric protein
  JOURNAL   Science 270 (5242), 1663-1667 (1995)
   PUBMED   7502076
REFERENCE   10 (residues 1 to 315)
  AUTHORS   Zhong,Z., Shiue,L., Kaplan,S. and de Lange,T.
  TITLE     A mammalian factor that binds telomeric TTAGGG repeats in vitro
  JOURNAL   Mol Cell Biol 12 (11), 4834-4843 (1992)
   PUBMED   1406665
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022893.6.
            
            Summary: This gene encodes a telomere specific protein which is a
            component of the telomere nucleoprotein complex. This protein is
            present at telomeres throughout the cell cycle and functions as an
            inhibitor of telomerase, acting in cis to limit the elongation of
            individual chromosome ends. The protein structure contains a
            C-terminal Myb motif, a dimerization domain near its N-terminus and
            an acidic N-terminus. Multiple transcripts of this gene are
            alternatively spliced products. [provided by RefSeq, Aug 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.428667.1,
                                           SRR18074969.1098296.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.11"
     Protein         1..315
                     /product="telomeric repeat-binding factor 1 isoform 8"
                     /note="NIMA-interacting protein 2; telomeric protein
                     Pin2/TRF1; TTAGGG repeat-binding factor 1; telomeric
                     repeat binding factor (NIMA-interacting) 1"
                     /calculated_mol_wt=36671
     Region          1..160
                     /region_name="TRFH"
                     /note="Telomeric Repeat binding Factor or TTAGGG Repeat
                     binding Factor, central (dimerization) domain Homology;
                     TRFH. Telomeres are protein/DNA complexes that make up the
                     physical ends of eukaryotic linear chromosomes and are
                     essential for chromosome stability; cl02779"
                     /db_xref="CDD:413471"
     Site            order(2,5,19,23,27,37..41,49,52..53,56)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238174"
     Region          257..305
                     /region_name="SANT_TRF"
                     /note="Telomere repeat binding factor-like DNA-binding
                     domains of the SANT/myb-like family; cd11660"
                     /db_xref="CDD:212558"
     Site            order(257..259,277,279..280,291,293..295,297..299,
                     301..302)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212558"
     CDS             1..315
                     /gene="TERF1"
                     /gene_synonym="hTRF1-AS; PIN2; t-TRF1; TRBF1; TRF; TRF1"
                     /coded_by="NM_001413368.1:412..1359"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:7013"
                     /db_xref="HGNC:HGNC:11728"
                     /db_xref="MIM:600951"
ORIGIN      
        1 mftiihglss ltacqlrtiy icqfltriaa gktldaqfen deritplesa lmiwgsieke
       61 hdklheeiqn likiqaiavc mengnfkeae evferifgdp nshmpfkskl lmiisqkdtf
      121 hsffqhfsyn hmmekiksyv nyvlseksst flmkaaakvv eskrtrtits qdkpsgndve
      181 meteanldtr krshknlfls klqhgtqqqd lnkkerrvgt pqstkkkkes rratesripv
      241 sksqpvtpek hrarkrqawl weedknlrsg vrkygegnws killhykfnn rtsvmlkdrw
      301 rtmkklklis sdsed
//
LOCUS       NP_001428086             431 aa            linear   PRI 21-NOV-2025
DEFINITION  urokinase-type plasminogen activator isoform 1 preproprotein [Homo
            sapiens].
ACCESSION   NP_001428086
VERSION     NP_001428086.1
DBSOURCE    REFSEQ: accession NM_001441157.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Li,D., Ding,C., Huang,F., Chang,M., Lu,Z., Li,G., Li,Y., Gao,H. and
            Sun,F.
  TITLE     Bioinformatics Analysis of the Expression and Prognostic Value of
            PLAU Gene in Wilms' Tumor
  JOURNAL   Anticancer Res 44 (9), 3829-3842 (2024)
   PUBMED   39197889
  REMARK    GeneRIF: Bioinformatics Analysis of the Expression and Prognostic
            Value of PLAU Gene in Wilms' Tumor.
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Guo,J., Wang,H., Huang,C., Lai,C., Shang,W., Luo,S. and Chen,L.
  TITLE     PLAU, transcriptionally negatively regulated by GATA6, promotes
            lung squamous carcinoma cell proliferation and migration
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (5), 119744 (2024)
   PUBMED   38702016
  REMARK    GeneRIF: PLAU, transcriptionally negatively regulated by GATA6,
            promotes lung squamous carcinoma cell proliferation and migration.
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Cui,X., Sun,H., Liu,X., Bai,Y., Bai,Y., Cui,Y., Wang,B., Zhang,S.
            and Li,X.
  TITLE     PLAU promotes cell proliferation and migration of head and neck
            cancer via STAT3 signaling pathway
  JOURNAL   Exp Cell Res 438 (2), 114056 (2024)
   PUBMED   38663475
  REMARK    GeneRIF: PLAU promotes cell proliferation and migration of head and
            neck cancer via STAT3 signaling pathway.
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Cetinsoy,O., Anyanwu,I., Krishnanand,H., Natarajan,G.,
            Ramachandran,N., Thomas,A. and Brookes,K.J.
  TITLE     Gene Association Study of the Urokinase Plasminogen Activator and
            Its Receptor Gene in Alzheimer's Disease
  JOURNAL   J Alzheimers Dis 99 (1), 241-250 (2024)
   PUBMED   38669542
  REMARK    GeneRIF: Gene Association Study of the Urokinase Plasminogen
            Activator and Its Receptor Gene in Alzheimer's Disease.
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Mekkawy,A.H., Pourgholami,M.H. and Morris,D.L.
  TITLE     Involvement of urokinase-type plasminogen activator system in
            cancer: an overview
  JOURNAL   Med Res Rev 34 (5), 918-956 (2014)
   PUBMED   24549574
  REMARK    Review article
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Naldini,L., Tamagnone,L., Vigna,E., Sachs,M., Hartmann,G.,
            Birchmeier,W., Daikuhara,Y., Tsubouchi,H., Blasi,F. and
            Comoglio,P.M.
  TITLE     Extracellular proteolytic cleavage by urokinase is required for
            activation of hepatocyte growth factor/scatter factor
  JOURNAL   EMBO J 11 (13), 4825-4833 (1992)
   PUBMED   1334458
REFERENCE   8  (residues 1 to 431)
  AUTHORS   Li,X., Smith,R.A. and Dobson,C.M.
  TITLE     Sequential 1H NMR assignments and secondary structure of the
            kringle domain from urokinase
  JOURNAL   Biochemistry 31 (40), 9562-9571 (1992)
   PUBMED   1327118
REFERENCE   9  (residues 1 to 431)
  AUTHORS   Stephens,R.W., Aumailley,M., Timpl,R., Reisberg,T., Tapiovaara,H.,
            Myohanen,H., Murphy-Ullrich,J. and Vaheri,A.
  TITLE     Urokinase binding to laminin-nidogen. Structural requirements and
            interactions with heparin
  JOURNAL   Eur J Biochem 207 (3), 937-942 (1992)
   PUBMED   1499567
REFERENCE   10 (residues 1 to 431)
  AUTHORS   Moroi,M. and Aoki,N.
  TITLE     Isolation and characterization of alpha2-plasmin inhibitor from
            human plasma. A novel proteinase inhibitor which inhibits
            activator-induced clot lysis
  JOURNAL   J Biol Chem 251 (19), 5956-5965 (1976)
   PUBMED   134998
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22.
            
            Summary: This gene encodes a secreted serine protease that converts
            plasminogen to plasmin. The encoded preproprotein is
            proteolytically processed to generate A and B polypeptide chains.
            These chains associate via a single disulfide bond to form the
            catalytically inactive high molecular weight urokinase-type
            plasminogen activator (HMW-uPA). HMW-uPA can be further processed
            into the catalytically active low molecular weight urokinase-type
            plasminogen activator (LMW-uPA). This low molecular weight form
            does not bind to the urokinase-type plasminogen activator receptor.
            Mutations in this gene may be associated with Quebec platelet
            disorder and late-onset Alzheimer's disease. Alternative splicing
            results in multiple transcript variants, at least one of which
            encodes an isoform that is proteolytically processed. [provided by
            RefSeq, Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR6380200.27285.11,
                                           SRR14038194.218887.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145774, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..431
                     /product="urokinase-type plasminogen activator isoform 1
                     preproprotein"
                     /EC_number="3.4.21.73"
                     /note="plasminogen activator, urinary; U-plasminogen
                     activator; urokinase-type plasminogen activator"
                     /calculated_mol_wt=46384
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2158
     mat_peptide     21..431
                     /product="Urokinase-type plasminogen activator.
                     /id=PRO_0000028318"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=46384
     mat_peptide     21..177
                     /product="Urokinase-type plasminogen activator long chain
                     A. /id=PRO_0000028319"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=17849
     Region          34..57
                     /region_name="Binds urokinase plasminogen activator
                     surface receptor. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
     Site            38
                     /site_type="glycosylation"
                     /note="O-linked (Fuc) threonine.
                     /evidence=ECO:0000269|PubMed:2023947; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Region          67..152
                     /region_name="KR"
                     /note="Kringle domain; Kringle domains are believed to
                     play a role in binding mediators, such as peptides, other
                     proteins, membranes, or phospholipids. They are autonomous
                     structural domains, found in a varying number of copies,
                     in blood clotting and...; cd00108"
                     /db_xref="CDD:238056"
     Site            79
                     /site_type="active"
                     /note="putative domain interaction site [active]"
                     /db_xref="CDD:238056"
     Site            order(94,104,132,134,143)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Region          152..177
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
     mat_peptide     156..177
                     /product="Urokinase-type plasminogen activator short chain
                     A. /id=PRO_0000028320"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=2574
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9151681; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Site            177..178
                     /site_type="cleavage"
                     /note="Cleavage, during zymogen activation; propagated
                     from UniProtKB/Swiss-Prot (P00749.3)"
     mat_peptide     179..431
                     /product="Urokinase-type plasminogen activator chain B.
                     /id=PRO_0000028321"
                     /note="propagated from UniProtKB/Swiss-Prot (P00749.3)"
                     /calculated_mol_wt=28425
     Region          179..422
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            179
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(224,275,376)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            322
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine. /id=CAR_000026;
                     propagated from UniProtKB/Swiss-Prot (P00749.3)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9151681; propagated from
                     UniProtKB/Swiss-Prot (P00749.3)"
     Site            order(370,395,397)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..431
                     /gene="PLAU"
                     /gene_synonym="ATF; BDPLT5; QPD; u-PA; UPA; URK"
                     /coded_by="NM_001441157.1:425..1720"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:5328"
                     /db_xref="HGNC:HGNC:9052"
                     /db_xref="MIM:191840"
ORIGIN      
        1 mrallarlll cvlvvsdskg snelhqvpsn cdclnggtcv snkyfsnihw cncpkkfggq
       61 hceidksktc yegnghfyrg kastdtmgrp clpwnsatvl qqtyhahrsd alqlglgkhn
      121 ycrnpdnrrr pwcyvqvglk llvqecmvhd cadgkkpssp peelkfqcgq ktlrprfkii
      181 ggefttienq pwfaaiyrrh rggsvtyvcg gslispcwvi sathcfidyp kkedyivylg
      241 rsrlnsntqg emkfevenli lhkdysadtl ahhndiallk irskegrcaq psrtiqticl
      301 psmyndpqfg tsceitgfgk enstdylype qlkmtvvkli shrecqqphy ygsevttkml
      361 caadpqwktd scqgdsggpl vcslqgrmtl tgivswgrgc alkdkpgvyt rvshflpwir
      421 shtkeengla l
//
LOCUS       NP_001389622            1300 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform c [Homo sapiens].
ACCESSION   NP_001389622
VERSION     NP_001389622.1
DBSOURCE    REFSEQ: accession NM_001402693.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1300)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1300)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1300)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1300)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1300)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1300)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1300)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1300)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1300)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1300)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.182385.1,
                                           SRR14372079.3906380.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1300
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1300
                     /product="kinectin isoform c"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=149480
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          316..>532
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          448..1240
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1300
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402693.1:1042..4944"
                     /note="isoform c is encoded by transcript variant 18"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqdlkqeika
      841 lkeeignvql ekaqqlsits kvqelqnllk gkeeqmntmk avleekekdl antgkwlqdl
      901 qeeneslkah vqevaqhnlk eassasqfee leivlkeken elkrleamlk eresdlsskt
      961 qllqdvqden klfksqieql kqqnyqqass fppheellkv iserekeisg lwneldslkd
     1021 avehqrkknn erqqqveave leakevlkkl fpkvsvpsnl sygewlhgfe kkakecmagt
     1081 sgseevkvle hklkeademh tllqleceky ksvlaetegi lqklqrsveq eenkwkvkvd
     1141 eshktikqmq ssftsseqel erlrsenkdi enlrrerehl emelekaeme rstyvtevre
     1201 lkaqlnetlt klrteqnerq kvagdlhkaq qsleliqski vkaagdttvi ensdvspete
     1261 sseketmsvs lnqtvtqlqq llqavnqqlt kekehyqvle
//
LOCUS       NP_001425411            2415 aa            linear   PRI 21-NOV-2025
DEFINITION  AT-rich interactive domain-containing protein 1B isoform 5 [Homo
            sapiens].
ACCESSION   NP_001425411 XP_047275088 XP_054212008
VERSION     NP_001425411.1
DBSOURCE    REFSEQ: accession NM_001438482.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2415)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2415)
  AUTHORS   Bosch,E., Guse,E., Kirchner,P., Winterpacht,A., Walther,M.,
            Alders,M., Kerkhof,J., Ekici,A.B., Sticht,H., Sadikovic,B., Reis,A.
            and Vasileiou,G.
  TITLE     The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation
  JOURNAL   Hum Genet 143 (8), 965-978 (2024)
   PUBMED   39028335
  REMARK    GeneRIF: The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation.
REFERENCE   3  (residues 1 to 2415)
  AUTHORS   Huang,X., Li,H., Yang,S., Ma,M., Lian,Y., Wu,X., Qi,X., Wang,X.,
            Rong,W. and Sheng,X.
  TITLE     De novo variation in ARID1B gene causes Coffin-Siris syndrome 1 in
            a Chinese family with excessive early-onset high myopia
  JOURNAL   BMC Med Genomics 17 (1), 142 (2024)
   PUBMED   38790056
  REMARK    GeneRIF: De novo variation in ARID1B gene causes Coffin-Siris
            syndrome 1 in a Chinese family with excessive early-onset high
            myopia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2415)
  AUTHORS   Hurlstone,A.F., Olave,I.A., Barker,N., van Noort,M. and Clevers,H.
  TITLE     Cloning and characterization of hELD/OSA1, a novel BRG1 interacting
            protein
  JOURNAL   Biochem J 364 (Pt 1), 255-264 (2002)
   PUBMED   11988099
  REMARK    GeneRIF: Cloning and characterization of hELD/OSA1, a novel BRG1
            interacting protein.
REFERENCE   5  (residues 1 to 2415)
  AUTHORS   Phelan,M.L., Sif,S., Narlikar,G.J. and Kingston,R.E.
  TITLE     Reconstitution of a core chromatin remodeling complex from SWI/SNF
            subunits
  JOURNAL   Mol Cell 3 (2), 247-253 (1999)
   PUBMED   10078207
REFERENCE   6  (residues 1 to 2415)
  AUTHORS   Imbert,G., Saudou,F., Yvert,G., Devys,D., Trottier,Y.,
            Garnier,J.M., Weber,C., Mandel,J.L., Cancel,G., Abbas,N., Durr,A.,
            Didierjean,O., Stevanin,G., Agid,Y. and Brice,A.
  TITLE     Cloning of the gene for spinocerebellar ataxia 2 reveals a locus
            with high sensitivity to expanded CAG/glutamine repeats
  JOURNAL   Nat Genet 14 (3), 285-291 (1996)
   PUBMED   8896557
REFERENCE   7  (residues 1 to 2415)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
REFERENCE   8  (residues 1 to 2415)
  AUTHORS   Vergano,S.A., van der Sluijs,P.J. and Santen,G.
  TITLE     ARID1B-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31132234
REFERENCE   9  (residues 1 to 2415)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
REFERENCE   10 (residues 1 to 2415)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355297.20, AL162578.13,
            AL049820.23 and AL591545.6.
            
            On or before Apr 21, 2025 this sequence version replaced
            XP_047275088.1, XP_054212008.1.
            
            Summary: This locus encodes an AT-rich DNA interacting
            domain-containing protein. The encoded protein is a component of
            the SWI/SNF chromatin remodeling complex and may play a role in
            cell-cycle activation. The protein encoded by this locus is similar
            to AT-rich interactive domain-containing protein 1A. These two
            proteins function as alternative, mutually exclusive ARID-subunits
            of the SWI/SNF complex. The associated complexes play opposing
            roles. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2638160.1,
                                           SRR18074969.2402838.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2415
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..2415
                     /product="AT-rich interactive domain-containing protein 1B
                     isoform 5"
                     /note="BRG1-binding protein ELD/OSA1; ELD (eyelid)/OSA
                     protein; BRG1-associated factor 250b; ARID
                     domain-containing protein 1B; AT rich interactive domain
                     1B (SWI1-like)"
                     /calculated_mol_wt=253796
     Region          744..>1092
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          1233..1325
                     /region_name="ARID_ARID1B"
                     /note="ARID/BRIGHT DNA binding domain of AT-rich
                     interactive domain-containing protein 1B (ARID1B) and
                     similar proteins; cd16877"
                     /db_xref="CDD:350641"
     Site            order(1255..1261,1286,1288..1289,1292,1302,1304..1306,
                     1308)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350641"
     Region          1346..>1726
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          2106..2361
                     /region_name="BAF250_C"
                     /note="SWI/SNF-like complex subunit BAF250/Osa; pfam12031"
                     /db_xref="CDD:463439"
     CDS             1..2415
                     /gene="ARID1B"
                     /gene_synonym="6A3-5; BAF250B; BRIGHT; CSS1; DAN15;
                     ELD/OSA1; MRD12; OSA2; P250R; SMARCF2"
                     /coded_by="NM_001438482.1:304..7551"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:57492"
                     /db_xref="HGNC:HGNC:18040"
                     /db_xref="MIM:614556"
ORIGIN      
        1 maaraaaaaa aaaararara gsgerrappg prpapgardl eagargaaaa aaapgpmlgg
       61 ggdgggglns vhhhpllprh elnmahnaga aaaagthsak sggseaalke ggsaaalsss
      121 ssssaaaaaa ssssssgpgs ametgllpnh klktvgeapa apphqqhhhh hhahhhhhha
      181 hhlhhhhalq qqlnqfqqqq qqqqqqqqqq qqqqhpisnn nslggaggga pqpgpdmeqp
      241 qhggakdsaa ggqadppgpp llskpgdedd appkmgepag gryehpglga lgtqqppvav
      301 pgggggpaav pefnnyygsa apasggpggr agpcfdqhgg qqspgmgmmh sasaaaagap
      361 gsmdplqnsh egypnsqcnh ypgysrpgag gggggggggg ggsggggggg gagaggagag
      421 avaaaaaaaa aaaggggggg yggssagygv lssprqqggg mmmgpgggga aslskaaags
      481 aaggfqrfag qnqhpsgatp tlnqlltsps pmmrsyggsy peysspsapp pppsqpqsqa
      541 aaagaaaggq qaaagmglgk dmgaqyaaas pawaaaqqrs hpamspgtpg ptmgrsqgsp
      601 mdpmvmkrpq lygmgsnphs qpqqsspypg gsygppgpqr ypigiqgrtp gamagmqypq
      661 qqmppqygqq gvsgycqqgq qpyysqqpqp phlppqaqyl psqsqqryqp qqdmsqegyg
      721 trsqpplapg kpnhedlnli qqerpsslpd lsgsiddlpt gteatlssav sasgstssqg
      781 dqsnpaqspf sphasphlss ipggpspspv gspvgsnqsr sgpispasip gsqmppqppg
      841 sqsessshpa lsqspmpqer gfmagtqrnp qmaqygpqqt gpsmsphpsp ggqmhagiss
      901 fqqsnssgty gpqmsqygpq gnysrppays gvpsasysgp gpgmgisann qmhgqgpsqp
      961 cgavplgrmp sagmqnrpfp gnmssmtpss pgmsqqggpg mgppmptvnr kaqeaaaavm
     1021 qaaansaqsr ppyirspayp sqsgaggrpm fssqhpnygn sqapmvhqpd qygqgsfpgm
     1081 nqsglmasss pysqpmnnss slmntqappy smapamvnss aasvgladmm spgesklplp
     1141 lkadgkeegt pqpeskskds yssqgisqpp tpgnlpvpsp mspssasiss fhgdesdsis
     1201 spgwpktpss pksssstttg ekitkvyelg neperklwvd ryltfmeerg spvsslpavg
     1261 kkpldlfrly vcvkeiggla qvnknkkwre latnlnvgts ssaasslkkq yiqylfafec
     1321 kiergeeppp evfstgdtkk qpklqppspa nsgslqgpqt pqstgsnsma evpgdlkppt
     1381 pastphgqmt pmqggrssti svhdpfsdvs dssfpkrnsm tpnapyqqgm smpdvmgrmp
     1441 yepnkdpfgg mrkvpgssep fmtqgqmpns smqdmynqsp sgamsnlgmg qrqqfpygas
     1501 ydrrhepygq qypgqgppsg qppygghqpg lypqqpnykr hmdgmygppa krhegdmynm
     1561 qyssqqqemy nqyggsysgp drrpiqgqyp ypysrermqg pgqiqthgip pqmmggplqs
     1621 sssegpqqnm waarndmpyp yqnrqgpggp tqappypgmn rtddmmvpdq rinhesqwps
     1681 hvsqrqpyms ssasmqpitr ppqpsyqtpp slpnhisrap spasfqrsle nrmspskspf
     1741 lpsmkmqkvm ptvptsqvtg pppqpppirr eitfppgsve asqpvlkqrr kitskdivtp
     1801 eawrvmmslk sgllaestwa ldtinillyd dstvatfnls qlsgflellv eyfrkclidi
     1861 fgilmeyevg dpsqkaldhn aarkddsqsl addsgkeeed aecidddeed eedeeedsek
     1921 tesdekssia ltapdaaadp kekpkqaskf dklpikivkk nnlfvvdrsd klgrvqefns
     1981 gllhwqlggg dttehiqthf eskmeipprr rpppplssag rkkeqegkgd seeqqeksii
     2041 atiddvlsar pgalpedanp gpqtesskfp fgiqqakshr niklledepr srdetplcti
     2101 ahwqdslakr cicvsnivrs lsfvpgndae mskhpglvli lgklillhhe hperkrapqt
     2161 yekeededkg vacskdewww dclevlrdnt lvtlanisgq ldlsaytesi clpildgllh
     2221 wmvcpsaeaq dpfptvgpns vlspqrlvle tlcklsiqdn nvdlilatpp fsrqekfyat
     2281 lvryvgdrkn pvcremsmal lsnlaqgdal aaraiavqkg signlisfle dgvtmaqyqq
     2341 sqhnlmhmqp ppleppsvdm mcraakalla marvdenrse fllhegrlld isisavlnsl
     2401 vasvicdvlf qigql
//
LOCUS       NP_001393550            1042 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 11 [Homo sapiens].
ACCESSION   NP_001393550
VERSION     NP_001393550.1
DBSOURCE    REFSEQ: accession NM_001406621.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1042)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1042)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1042)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1042)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1042)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1042)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1042)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.298495.1,
                                           SRR14372079.1111175.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1042
                     /product="hamartin isoform 11"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=116074
     Region          16..597
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <586..>838
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1042
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406621.1:448..3576"
                     /note="isoform 11 is encoded by transcript variant 35"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mdtdvvvltt gvlvlitmlp mipqsgkqhl ldffdifgrl sswclkkpgh vaevylvhlh
       61 asvyalfhrl ygmypcnfvs flrshysmke nletfeevvk pmmehvrihp elvtgskdhe
      121 ldprrwkrle thdvviecak isldpteasy edgysvshqi sarfphrsad vttspyadtq
      181 nsygcatstp ystsrlmlln mpgqlpqtls spstrlitep pqatlwspsm vcgmttppts
      241 pgnvppdlsh pyskvfgttg gkgtplgtpa tspppaplch sddyvhislp qatvtpprke
      301 ermdsarpcl hrqhhllndr gseeppgskg svtlsdlpgf lgdlaseeds iekdkeeaai
      361 srelseitta eaepvvprgg fdspfyrdsl pgsqrkthsa asssqgasvn peplhssldk
      421 lgpdtpkqaf tpidlpcgsa despagdrec qtsletsift pspckipppt rvgfgsgqpp
      481 pydhlfeval pktahhfvir kteellkkak gnteedgvps tspmevldrl iqqgadahsk
      541 elnklplpsk svdwthfggs ppsdeirtlr dqllllhnql lyerfkrqqh alrnrrllrk
      601 vikaaaleeh naamkdqlkl qekdiqmwkv slqkeqaryn qlqeqrdtmv tklhsqirql
      661 qhdreefynq sqelqtkled crnmiaelri elkkannkvc htelllsqvs qklsnsesvq
      721 qqmeflnrql lvlgevnely leqlqnkhsd ttkevemmka ayrkeleknr shvlqqtqrl
      781 dtsqkrilel eshlakkdhl lleqkkyled vklqargqlq aaesryeaqk ritqvfelei
      841 ldlygrlekd gllkkleeek aeaaeaaeer ldccndgcsd smvghneeas ghngetktpr
      901 pssargssgs rggggsssss selstpekpp hqragpfssr wettmgeasa sipttvgslp
      961 ssksflgmka relfrnkses qcdedgmtss lseslktelg kdlgveakip lnldgphpsp
     1021 ptpdsvgqlh imdynethhe hs
//
LOCUS       NP_001427310             477 aa            linear   PRI 21-NOV-2025
DEFINITION  TELO2-interacting protein 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001427310 XP_047278222 XP_054217262
VERSION     NP_001427310.1
DBSOURCE    REFSEQ: accession NM_001440381.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Kim,Y., Park,J., Joo,S.Y., Kim,B.G., Jo,A., Lee,H. and Cho,Y.
  TITLE     Structure of the Human TELO2-TTI1-TTI2 Complex
  JOURNAL   J Mol Biol 434 (2), 167370 (2022)
   PUBMED   34838521
  REMARK    GeneRIF: Structure of the Human TELO2-TTI1-TTI2 Complex.
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Rao,F., Cha,J., Xu,J., Xu,R., Vandiver,M.S., Tyagi,R., Tokhunts,R.,
            Koldobskiy,M.A., Fu,C., Barrow,R., Wu,M., Fiedler,D., Barrow,J.C.
            and Snyder,S.H.
  TITLE     Inositol pyrophosphates mediate the DNA-PK/ATM-p53 cell death
            pathway by regulating CK2 phosphorylation of Tti1/Tel2
  JOURNAL   Mol Cell 54 (1), 119-132 (2014)
   PUBMED   24657168
  REMARK    Erratum:[Mol Cell. 2020 Aug 20;79(4):702. doi:
            10.1016/j.molcel.2020.07.021. PMID: 32822581]
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Langouet,M., Saadi,A., Rieunier,G., Moutton,S., Siquier-Pernet,K.,
            Fernet,M., Nitschke,P., Munnich,A., Stern,M.H., Chaouch,M. and
            Colleaux,L.
  TITLE     Mutation in TTI2 reveals a role for triple T complex in human brain
            development
  JOURNAL   Hum Mutat 34 (11), 1472-1476 (2013)
   PUBMED   23956177
  REMARK    GeneRIF: The findings emphasises the role of the TTI2 gene in the
            etiology of intellectual disability.
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Takai,H., Xie,Y., de Lange,T. and Pavletich,N.P.
  TITLE     Tel2 structure and function in the Hsp90-dependent maturation of
            mTOR and ATR complexes
  JOURNAL   Genes Dev 24 (18), 2019-2030 (2010)
   PUBMED   20801936
REFERENCE   5  (residues 1 to 477)
  AUTHORS   Hurov,K.E., Cotta-Ramusino,C. and Elledge,S.J.
  TITLE     A genetic screen identifies the Triple T complex required for DNA
            damage signaling and ATM and ATR stability
  JOURNAL   Genes Dev 24 (17), 1939-1950 (2010)
   PUBMED   20810650
  REMARK    GeneRIF: TTI1 and TTI2 protect cells from spontaneous DNA damage,
            and are required for the establishment of the intra-S and G2/M
            checkpoint.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091144.12.
            
            On or before May 19, 2025 this sequence version replaced
            XP_047278222.1, XP_054217262.1.
            
            Summary: This gene encodes a regulator of the DNA damage response.
            The protein is a component of the Triple T complex (TTT) which also
            includes telomere length regulation protein and TELO2 interacting
            protein 1. The TTT complex is involved in cellular resistance to
            DNA damage stresses and may act as a regulator of
            phosphoinositide-3-kinase-related protein kinase (PIKK) abundance.
            [provided by RefSeq, May 2013].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4341643.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p12"
     Protein         1..477
                     /product="TELO2-interacting protein 2 isoform 2"
                     /note="Tel2 interacting protein 2 homolog"
                     /calculated_mol_wt=53175
     Region          155..353
                     /region_name="Tti2"
                     /note="Tti2 family; pfam10521"
                     /db_xref="CDD:431336"
     CDS             1..477
                     /gene="TTI2"
                     /gene_synonym="C8orf41; MRT39"
                     /coded_by="NM_001440381.1:276..1709"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:80185"
                     /db_xref="HGNC:HGNC:26262"
                     /db_xref="MIM:614426"
ORIGIN      
        1 meldsaleap sqedsnlsee lshsafgqaf skilhclarp earrgnvkda vlkdlgdlie
       61 atefdrlfeg tgarlrgmpe tlgqvakale kyaapskeee gggdghseaa ekaaqvgllf
      121 lkllgkveta knslvgpawq tglhhlagpv yifaithsle qpwttprsre varevltsll
      181 qvtecgsvag flhgenedek grlsvilgll kpdlykeswk nnpaikhvfs wtlqqvtrpw
      241 lsqhlervlp aslvisddyq tenkilgvhc lhhivlnvav llclldlfpi lektlhwkgd
      301 garptthcde vlrlilthme pehrlllrrt yarnlpafvn rlgiltvrhl krlerviigy
      361 levydgpeee arlkiletlk llmqhtwprv scrlvvllka llklicdvar dpnltpesvk
      421 sallqeatdc lilldrcsqg rvkgllakip qscedrkvvn yirkvqqvse gapyngt
//
LOCUS       NP_001422923             830 aa            linear   PRI 21-NOV-2025
DEFINITION  histone deacetylase 4 isoform 5 [Homo sapiens].
ACCESSION   NP_001422923
VERSION     NP_001422923.1
DBSOURCE    REFSEQ: accession NM_001435994.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 830)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 830)
  AUTHORS   Liu,W. and Luo,G.
  TITLE     NEDD9 is transcriptionally regulated by HDAC4 and promotes breast
            cancer metastasis and macrophage M2 polarization via the
            FAK/NF-kappaB signaling pathway
  JOURNAL   Neoplasia 57, 101059 (2024)
   PUBMED   39326322
  REMARK    GeneRIF: NEDD9 is transcriptionally regulated by HDAC4 and promotes
            breast cancer metastasis and macrophage M2 polarization via the
            FAK/NF-kappaB signaling pathway.
REFERENCE   3  (residues 1 to 830)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 830)
  AUTHORS   Di Giorgio,E., Dalla,E., Tolotto,V., D'Este,F., Paluvai,H.,
            Ranzino,L. and Brancolini,C.
  TITLE     HDAC4 influences the DNA damage response and counteracts senescence
            by assembling with HDAC1/HDAC2 to control H2BK120 acetylation and
            homology-directed repair
  JOURNAL   Nucleic Acids Res 52 (14), 8218-8240 (2024)
   PUBMED   38874468
  REMARK    GeneRIF: HDAC4 influences the DNA damage response and counteracts
            senescence by assembling with HDAC1/HDAC2 to control H2BK120
            acetylation and homology-directed repair.
REFERENCE   5  (residues 1 to 830)
  AUTHORS   Chen,Q. and Lao,J.
  TITLE     Interference with Histone Deacetylase 4 Regulates c-Jun N-terminal
            Kinase/Activating Protein-1 Signaling to Ameliorate Sepsis-induced
            Alveolar Epithelial Cell Injury
  JOURNAL   J Physiol Investig 67 (4), 174-186 (2024)
   PUBMED   39133038
  REMARK    GeneRIF: Interference with Histone Deacetylase 4 Regulates c-Jun
            N-terminal Kinase/Activating Protein-1 Signaling to Ameliorate
            Sepsis-induced Alveolar Epithelial Cell Injury.
REFERENCE   6  (residues 1 to 830)
  AUTHORS   Pazin,M.J. and Kadonaga,J.T.
  TITLE     What's up and down with histone deacetylation and transcription?
  JOURNAL   Cell 89 (3), 325-328 (1997)
   PUBMED   9150131
  REMARK    Review article
REFERENCE   7  (residues 1 to 830)
  AUTHORS   Wolffe,A.P.
  TITLE     Transcriptional control. Sinful repression
  JOURNAL   Nature 387 (6628), 16-17 (1997)
   PUBMED   9139815
REFERENCE   8  (residues 1 to 830)
  AUTHORS   Ohara,O., Nagase,T., Ishikawa,K., Nakajima,D., Ohira,M., Seki,N.
            and Nomura,N.
  TITLE     Construction and characterization of human brain cDNA libraries
            suitable for analysis of cDNA clones encoding relatively large
            proteins
  JOURNAL   DNA Res 4 (1), 53-59 (1997)
   PUBMED   9179496
REFERENCE   9  (residues 1 to 830)
  AUTHORS   Wilson,L.C., Leverton,K., Oude Luttikhuis,M.E., Oley,C.A.,
            Flint,J., Wolstenholme,J., Duckett,D.P., Barrow,M.A., Leonard,J.V.,
            Read,A.P. et al.
  TITLE     Brachydactyly and mental retardation: an Albright hereditary
            osteodystrophy-like syndrome localized to 2q37
  JOURNAL   Am J Hum Genet 56 (2), 400-407 (1995)
   PUBMED   7847374
REFERENCE   10 (residues 1 to 830)
  AUTHORS   Doherty,E.S. and Lacbawan,F.L.
  TITLE     2q37 Microdeletion Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301337
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC062017.6 and AC017028.11.
            
            Summary: Histones play a critical role in transcriptional
            regulation, cell cycle progression, and developmental events.
            Histone acetylation/deacetylation alters chromosome structure and
            affects transcription factor access to DNA. The protein encoded by
            this gene belongs to class II of the histone deacetylase/acuc/apha
            family. It possesses histone deacetylase activity and represses
            transcription when tethered to a promoter. This protein does not
            bind DNA directly, but through transcription factors MEF2C and
            MEF2D. It seems to interact in a multiprotein complex with RbAp48
            and HDAC3. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..830
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..830
                     /product="histone deacetylase 4 isoform 5"
                     /EC_number="3.5.1.98"
                     /note="histone deacetylase A"
                     /calculated_mol_wt=92136
     Region          36..125
                     /region_name="ClassIIa_HDAC4_Gln-rich-N"
                     /note="Glutamine-rich N-terminal helical domain of HDAC4,
                     a Class IIa histone deacetylase; cd10162"
                     /db_xref="CDD:197398"
     Site            order(37..38,40..41,44,48,51..52,55..56,58..59,62..63,
                     65..66,69..71,73..75,77..78,80..82,84..85,88,91..92,
                     95..97)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:197398"
     Site            order(37..38,40..41,44,48,51,55,58,62..63,65..66,69..70,
                     73,77,80,84,91,95)
                     /site_type="other"
                     /note="dimer interface A, C [polypeptide binding]"
                     /db_xref="CDD:197398"
     Site            order(48,52,56,59,63,66,70..71,74..75,78,82,85)
                     /site_type="other"
                     /note="dimer interface A, D [polypeptide binding]"
                     /db_xref="CDD:197398"
     Site            order(66,70,81..82,85,92,96..97)
                     /site_type="other"
                     /note="dimer interface A, B [polypeptide binding]"
                     /db_xref="CDD:197398"
     Region          627..>733
                     /region_name="Arginase_HDAC"
                     /note="Arginase-like and histone-like hydrolases; cl17011"
                     /db_xref="CDD:450134"
     CDS             1..830
                     /gene="HDAC4"
                     /gene_synonym="AHO3; BDMR; HA6116; HD4; HDAC-4; HDAC-A;
                     HDACA; NEDCHF; NEDCHID"
                     /coded_by="NM_001435994.1:234..2726"
                     /note="isoform 5 is encoded by transcript variant 9"
                     /db_xref="GeneID:9759"
                     /db_xref="HGNC:HGNC:14063"
                     /db_xref="MIM:605314"
ORIGIN      
        1 mpstvdvata lplqvapsav pmdlrldhqf slpvaepalr eqqlqqella lkqkqqiqrq
       61 iliaefqrqh eqlsrqheaq lhehikqqqe mlamkhqqel lehqrklerh rqeqelekqh
      121 reqklqqlkn kekgkesava stevkmklqe fvlnkkkala hrnlnhciss dprywygktq
      181 hssldqsspp qsgvstsynh pvlgmydakd dfplrktase pnlklrsrlk qkvaerrssp
      241 llrrkdgpvv talkkrpldv tdsacssapg sgpsspnnss gsvsaengia pavpsipaet
      301 slahrlvare gsaaplplyt spslpnitlg lpatgpsagt agqqdaerlt lpalqqrlsl
      361 fpgthltpyl stsplerdgg aahspllqhm vlleqppaqa plvtdwylsg lgalplhaqs
      421 lvgadrvsps ihklrqhrpl grtqsaplpq naqalqhlvi qqqhqqflek hkqqfqqqql
      481 qmnkiipkps eparqpeshp eeteeelreh qalldepyld rlpgqkeaha qagvqvkqep
      541 iesdeeeaep prevepgqrq pseqellfrq qallleqqri hqlrnyqasm eaagipvsfg
      601 ghrplsraqs spasatfpvs vqepptkprf ttglvydtlm lkhqctcgss sshpehagri
      661 qsiwsrlqet glrgkcecir grkatleelq tvhseahtll ygtnplnrqk ldskkllgsl
      721 asvfvrlpcg gvgglpmcgf kgrvsrerfd rrlghlslgk vvwrrwlglw gavalalrnr
      781 ilyaasissp sksvavicsh qatsmvrvgc vllysvpsfh pklqvglpvq
//
LOCUS       NP_001397698             213 aa            linear   PRI 21-NOV-2025
DEFINITION  transcription initiation factor TFIID subunit 12 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001397698 XP_024305128
VERSION     NP_001397698.1
DBSOURCE    REFSEQ: accession NM_001410769.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 213)
  AUTHORS   Xu,Y., Milazzo,J.P., Somerville,T.D.D., Tarumoto,Y., Huang,Y.H.,
            Ostrander,E.L., Wilkinson,J.E., Challen,G.A. and Vakoc,C.R.
  TITLE     A TFIID-SAGA Perturbation that Targets MYB and Suppresses Acute
            Myeloid Leukemia
  JOURNAL   Cancer Cell 33 (1), 13-28 (2018)
   PUBMED   29316427
  REMARK    GeneRIF: Ectopic expression of the TAF4 histone-fold fragment can
            efficiently squelch TAF12 in cells
REFERENCE   6  (residues 1 to 213)
  AUTHORS   Hisatake,K., Ohta,T., Takada,R., Guermah,M., Horikoshi,M.,
            Nakatani,Y. and Roeder,R.G.
  TITLE     Evolutionary conservation of human
            TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and
            interactions of TAFII80 with other TAFs and with general
            transcription factors
  JOURNAL   Proc Natl Acad Sci U S A 92 (18), 8195-8199 (1995)
   PUBMED   7667268
REFERENCE   7  (residues 1 to 213)
  AUTHORS   Mengus,G., May,M., Jacq,X., Staub,A., Tora,L., Chambon,P. and
            Davidson,I.
  TITLE     Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28:
            three subunits of the human transcription factor TFIID
  JOURNAL   EMBO J 14 (7), 1520-1531 (1995)
   PUBMED   7729427
REFERENCE   8  (residues 1 to 213)
  AUTHORS   Zhou,Q. and Sharp,P.A.
  TITLE     Novel mechanism and factor for regulation by HIV-1 Tat
  JOURNAL   EMBO J 14 (2), 321-328 (1995)
   PUBMED   7835343
REFERENCE   9  (residues 1 to 213)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   10 (residues 1 to 213)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL360012.18 and AL513497.21.
            
            On Aug 15, 2022 this sequence version replaced XP_024305128.1.
            
            Summary: Control of transcription by RNA polymerase II involves the
            basal transcription machinery which is a collection of proteins.
            These proteins with RNA polymerase II, assemble into complexes
            which are modulated by transactivator proteins that bind to
            cis-regulatory elements located adjacent to the transcription start
            site. Some modulators interact directly with the basal complex,
            whereas others may act as bridging proteins linking transactivators
            to the basal transcription factors. Some of these associated
            factors are weakly attached while others are tightly associated
            with TBP in the TFIID complex. Among the latter are the TAF
            proteins. Different TAFs are predicted to mediate the function of
            distinct transcriptional activators for a variety of gene promoters
            and RNA polymerases. TAF12 interacts directly with TBP as well as
            with TAF2I. Two transcript variants encoding the same protein have
            been found for this gene. [provided by RefSeq, Sep 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.193017.1,
                                           SRR5189667.218205.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.3"
     Protein         1..213
                     /product="transcription initiation factor TFIID subunit 12
                     isoform 2"
                     /note="transcription initiation factor TFIID 20/15 kDa
                     subunits; TATA box binding protein (TBP)-associated
                     factor, RNA polymerase II, J, 20kD; transcription
                     initiation factor TFIID subunit 12; TAFII20/TAFII15;
                     TAFII-20/TAFII-15; TAF12 RNA polymerase II, TATA box
                     binding protein (TBP)-associated factor, 20kDa"
                     /calculated_mol_wt=23441
     Region          107..180
                     /region_name="HFD_TAF12"
                     /note="histone-fold domain found in transcription
                     initiation factor TFIID subunit 12 (TAF12) and similar
                     proteins; cd07981"
                     /db_xref="CDD:467025"
     Site            order(107..110,114,118,121..122,136,139..141,143..145,
                     148..149,152,155,163..165,168..169,172,176,178,180)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467025"
     Site            order(128,132,136,157..159,170,174)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467025"
     CDS             1..213
                     /gene="TAF12"
                     /gene_synonym="TAF2J; TAFII20"
                     /coded_by="NM_001410769.1:90..731"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS90896.1"
                     /db_xref="GeneID:6883"
                     /db_xref="HGNC:HGNC:11545"
                     /db_xref="MIM:600773"
ORIGIN      
        1 maashftglt avadvikdld tqialiglgp hsskkkqdld klyelkskar qimnqfgpsa
       61 linlsnfssi kpepastppq gsmanstavv kipgtpgagg rlspennqvl tkkklqdlvr
      121 evdpneqlde dveemllqia ddfiesvvta acqlarhrks stlevkdvql hlerqwnmwi
      181 pgfgseeirp ykkactteah kqrmalirkt tkk
//
LOCUS       NP_001427452             289 aa            linear   PRI 21-NOV-2025
DEFINITION  syntaxin-3 isoform 1 [Homo sapiens].
ACCESSION   NP_001427452 XP_047283456 XP_054225738
VERSION     NP_001427452.1
DBSOURCE    REFSEQ: accession NM_001440523.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Shinozuka,T., Kanda,M., Sato,Y., Shimizu,D., Tanaka,C., Umeda,S.,
            Inokawa,Y., Hattori,N., Hayashi,M., Nakayama,G. and Kodera,Y.
  TITLE     Increased STX3 transcript and protein levels were associated with
            poor prognosis in two independent cohorts of esophageal squamous
            cell carcinoma patients
  JOURNAL   Cancer Med 12 (24), 22185-22195 (2023)
   PUBMED   38014487
  REMARK    GeneRIF: Increased STX3 transcript and protein levels were
            associated with poor prognosis in two independent cohorts of
            esophageal squamous cell carcinoma patients.
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Janecke,A.R., Liu,X., Adam,R., Punuru,S., Viestenz,A., Strauss,V.,
            Laass,M., Sanchez,E., Adachi,R., Schatz,M.P., Saboo,U.S.,
            Mittal,N., Rohrschneider,K., Escher,J., Ganesh,A., Al Zuhaibi,S.,
            Al Murshedi,F., AlSaleem,B., Alfadhel,M., Al Sinani,S.,
            Alkuraya,F.S., Huber,L.A., Muller,T., Heidelberger,R. and Janz,R.
  TITLE     Pathogenic STX3 variants affecting the retinal and intestinal
            transcripts cause an early-onset severe retinal dystrophy in
            microvillus inclusion disease subjects
  JOURNAL   Hum Genet 140 (8), 1143-1156 (2021)
   PUBMED   33974130
  REMARK    GeneRIF: Pathogenic STX3 variants affecting the retinal and
            intestinal transcripts cause an early-onset severe retinal
            dystrophy in microvillus inclusion disease subjects.
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Low,S.H., Vasanji,A., Nanduri,J., He,M., Sharma,N., Koo,M.,
            Drazba,J. and Weimbs,T.
  TITLE     Syntaxins 3 and 4 are concentrated in separate clusters on the
            plasma membrane before the establishment of cell polarity
  JOURNAL   Mol Biol Cell 17 (2), 977-989 (2006)
   PUBMED   16339081
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Martin-Martin,B., Nabokina,S.M., Lazo,P.A. and Mollinedo,F.
  TITLE     Co-expression of several human syntaxin genes in neutrophils and
            differentiating HL-60 cells: variant isoforms and detection of
            syntaxin 1
  JOURNAL   J Leukoc Biol 65 (3), 397-406 (1999)
   PUBMED   10080545
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Steegmaier,M., Yang,B., Yoo,J.S., Huang,B., Shen,M., Yu,S., Luo,Y.
            and Scheller,R.H.
  TITLE     Three novel proteins of the syntaxin/SNAP-25 family
  JOURNAL   J Biol Chem 273 (51), 34171-34179 (1998)
   PUBMED   9852078
REFERENCE   8  (residues 1 to 289)
  AUTHORS   Riento,K., Galli,T., Jansson,S., Ehnholm,C., Lehtonen,E. and
            Olkkonen,V.M.
  TITLE     Interaction of Munc-18-2 with syntaxin 3 controls the association
            of apical SNAREs in epithelial cells
  JOURNAL   J Cell Sci 111 (Pt 17), 2681-2688 (1998)
   PUBMED   9701566
REFERENCE   9  (residues 1 to 289)
  AUTHORS   Galli,T., Zahraoui,A., Vaidyanathan,V.V., Raposo,G., Tian,J.M.,
            Karin,M., Niemann,H. and Louvard,D.
  TITLE     A novel tetanus neurotoxin-insensitive vesicle-associated membrane
            protein in SNARE complexes of the apical plasma membrane of
            epithelial cells
  JOURNAL   Mol Biol Cell 9 (6), 1437-1448 (1998)
   PUBMED   9614185
REFERENCE   10 (residues 1 to 289)
  AUTHORS   Delgrossi,M.H., Breuza,L., Mirre,C., Chavrier,P. and Le Bivic,A.
  TITLE     Human syntaxin 3 is localized apically in human intestinal cells
  JOURNAL   J Cell Sci 110 (Pt 18), 2207-2214 (1997)
   PUBMED   9378770
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000640.5.
            
            On or before May 21, 2025 this sequence version replaced
            XP_047283456.1, XP_054225738.1.
            
            Summary: The gene is a member of the syntaxin family. The encoded
            protein is targeted to the apical membrane of epithelial cells
            where it forms clusters and is important in establishing and
            maintaining polarity necessary for protein trafficking involving
            vesicle fusion and exocytosis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3630021.1,
                                           SRR14372080.4064308.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..289
                     /product="syntaxin-3 isoform 1"
                     /note="syntaxin 3A; syntaxin 3B"
                     /calculated_mol_wt=33024
     Region          34..226
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     Region          194..260
                     /region_name="SNARE"
                     /note="SNARE motif; cl22856"
                     /db_xref="CDD:473982"
     Site            order(222,229,232)
                     /site_type="other"
                     /note="flanking leucine-zipper layers"
                     /db_xref="CDD:277192"
     Site            225
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277192"
     Site            264..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13277.3)"
     CDS             1..289
                     /gene="STX3"
                     /gene_synonym="DIAR12; MVID2; RDMVID; STX3A"
                     /coded_by="NM_001440523.1:231..1100"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:6809"
                     /db_xref="HGNC:HGNC:11438"
                     /db_xref="MIM:600876"
ORIGIN      
        1 mkdrleqlka kqltqdddtd aveiaidnta fmdeffseie etrlnidkis ehveeakkly
       61 siilsapipe pktkddleql tteikkrann vrnklksmek hieedevrss adlrirksqh
      121 svlsrkfvev mtkyneaqvd frerskgriq rqleitgkkt tdeeleemle sgnpaiftsg
      181 iidsqiskqa lseiegrhkd ivrlessike lhdmfmdiam lvenqgemld nielnvmhtv
      241 dhvekardet kkavkyqsqa rkkliiiivl vvvllgilal iiglsvgln
//
LOCUS       NP_001295016             234 aa            linear   PRI 21-NOV-2025
DEFINITION  protein Largen isoform 3 [Homo sapiens].
ACCESSION   NP_001295016 XP_011541759
VERSION     NP_001295016.1
DBSOURCE    REFSEQ: accession NM_001308087.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Thiebaut,R., Esmiol,S., Lecine,P., Mahfouz,B., Hermant,A.,
            Nicoletti,C., Parnis,S., Perroy,J., Borg,J.P., Pascoe,L.,
            Hugot,J.P. and Ollendorff,V.
  TITLE     Characterization and Genetic Analyses of New Genes Coding for NOD2
            Interacting Proteins
  JOURNAL   PLoS One 11 (11), e0165420 (2016)
   PUBMED   27812135
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 234)
  AUTHORS   Scannell Bryan,M., Argos,M., Pierce,B., Tong,L., Rakibuz-Zaman,M.,
            Ahmed,A., Rahman,M., Islam,T., Yunus,M., Parvez,F., Roy,S.,
            Jasmine,F., Baron,J.A., Kibriya,M.G. and Ahsan,H.
  TITLE     Genome-wide association studies and heritability estimates of body
            mass index related phenotypes in Bangladeshi adults
  JOURNAL   PLoS One 9 (8), e105062 (2014)
   PUBMED   25133637
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 234)
  AUTHORS   Yamamoto,K., Gandin,V., Sasaki,M., McCracken,S., Li,W.,
            Silvester,J.L., Elia,A.J., Wang,F., Wakutani,Y., Alexandrova,R.,
            Oo,Y.D., Mullen,P.J., Inoue,S., Itsumi,M., Lapin,V., Haight,J.,
            Wakeham,A., Shahinian,A., Ikura,M., Topisirovic,I., Sonenberg,N.
            and Mak,T.W.
  TITLE     Largen: a molecular regulator of mammalian cell size control
  JOURNAL   Mol Cell 53 (6), 904-915 (2014)
   PUBMED   24656129
  REMARK    GeneRIF: Largen, the product of a gene PRR16, increases cell size
            upon overexpression in human cells.
REFERENCE   7  (residues 1 to 234)
  AUTHORS   Wang,H., St Julien,K.R., Stevenson,D.K., Hoffmann,T.J., Witte,J.S.,
            Lazzeroni,L.C., Krasnow,M.A., Quaintance,C.C., Oehlert,J.W.,
            Jelliffe-Pawlowski,L.L., Gould,J.B., Shaw,G.M. and O'Brodovich,H.M.
  TITLE     A genome-wide association study (GWAS) for bronchopulmonary
            dysplasia
  JOURNAL   Pediatrics 132 (2), 290-297 (2013)
   PUBMED   23897914
REFERENCE   8  (residues 1 to 234)
  AUTHORS   Kennedy,R.B., Ovsyannikova,I.G., Pankratz,V.S., Haralambieva,I.H.,
            Vierkant,R.A. and Poland,G.A.
  TITLE     Genome-wide analysis of polymorphisms associated with cytokine
            responses in smallpox vaccine recipients
  JOURNAL   Hum Genet 131 (9), 1403-1421 (2012)
   PUBMED   22610502
REFERENCE   9  (residues 1 to 234)
  AUTHORS   Sakai,Y., Shaw,C.A., Dawson,B.C., Dugas,D.V., Al-Mohtaseb,Z.,
            Hill,D.E. and Zoghbi,H.Y.
  TITLE     Protein interactome reveals converging molecular pathways among
            autism disorders
  JOURNAL   Sci Transl Med 3 (86), 86ra49 (2011)
   PUBMED   21653829
REFERENCE   10 (residues 1 to 234)
  AUTHORS   Barberi,T., Willis,L.M., Socci,N.D. and Studer,L.
  TITLE     Derivation of multipotent mesenchymal precursors from human
            embryonic stem cells
  JOURNAL   PLoS Med 2 (6), e161 (2005)
   PUBMED   15971941
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC113418.2 and AC093301.3.
            
            On Apr 22, 2015 this sequence version replaced XP_011541759.1.
            
            Transcript Variant: This variant (3) contains an alternate 5'
            terminal exon, and it thus differs in the 5' UTR and initiates
            translation at a downstream in-frame start codon, compared to
            variant 1. The encoded isoform (3) is shorter at the N-terminus,
            compared to isoform 1. Both variants 3 and 4 encode isoform 3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA328660.1, DB464089.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q23.1"
     Protein         1..234
                     /product="protein Largen isoform 3"
                     /note="mesenchymal stem cell protein DSC54; proline-rich
                     protein 16; protein Largen"
                     /calculated_mol_wt=25175
     Region          2..234
                     /region_name="DUF4589"
                     /note="Domain of unknown function (DUF4589); pfam15252"
                     /db_xref="CDD:464592"
     CDS             1..234
                     /gene="PRR16"
                     /gene_synonym="DSC54; LARGEN"
                     /coded_by="NM_001308087.2:138..842"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS78053.1"
                     /db_xref="GeneID:51334"
                     /db_xref="HGNC:HGNC:29654"
                     /db_xref="MIM:615931"
ORIGIN      
        1 mtdssktdtl nssssgttas slekikvqan aplikppahp sailtvlrkp npppppprlt
       61 pvkcedpkrv vptanpvktn gtllrngglp ggpnkipngd iccipnsnld kapvqllmhr
      121 pekdrcpqag prervrfnek vqyhgycpdc dtryniknre vhlhsepvhp pgkiphqgpp
      181 lpptphlppf plenggmgis hsnsfppirp atvppptapk pqktilrkst tttv
//
LOCUS       NP_001425385             542 aa            linear   PRI 21-NOV-2025
DEFINITION  excitatory amino acid transporter 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001425385
VERSION     NP_001425385.1
DBSOURCE    REFSEQ: accession NM_001438456.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Albury,C.L., Sutherland,H.G., Lam,A.W.Y., Tran,N.K., Lea,R.A.,
            Haupt,L.M. and Griffiths,L.R.
  TITLE     Identification of Polymorphisms in EAAT1 Glutamate Transporter Gene
            SLC1A3 Associated with Reduced Migraine Risk
  JOURNAL   Genes (Basel) 15 (6), 797 (2024)
   PUBMED   38927733
  REMARK    GeneRIF: Identification of Polymorphisms in EAAT1 Glutamate
            Transporter Gene SLC1A3 Associated with Reduced Migraine Risk.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Welby,E. and Ebert,A.D.
  TITLE     Diminished motor neuron activity driven by abnormal astrocytic
            EAAT1 glutamate transporter activity in spinal muscular atrophy is
            not fully restored after lentiviral SMN delivery
  JOURNAL   Glia 71 (5), 1311-1332 (2023)
   PUBMED   36655314
  REMARK    GeneRIF: Diminished motor neuron activity driven by abnormal
            astrocytic EAAT1 glutamate transporter activity in spinal muscular
            atrophy is not fully restored after lentiviral SMN delivery.
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Pant,S., Wu,Q., Ryan,R. and Tajkhorshid,E.
  TITLE     Microscopic Characterization of the Chloride Permeation Pathway in
            the Human Excitatory Amino Acid Transporter 1 (EAAT1)
  JOURNAL   ACS Chem Neurosci 13 (6), 776-785 (2022)
   PUBMED   35192345
  REMARK    GeneRIF: Microscopic Characterization of the Chloride Permeation
            Pathway in the Human Excitatory Amino Acid Transporter 1 (EAAT1).
REFERENCE   5  (residues 1 to 542)
  AUTHORS   Lee,A., Anderson,A.R., Beasley,S.J., Barnett,N.L., Poronnik,P. and
            Pow,D.V.
  TITLE     A new splice variant of the glutamate-aspartate transporter:
            cloning and immunolocalization of GLAST1c in rat, pig and human
            brains
  JOURNAL   J Chem Neuroanat 43 (1), 52-63 (2012)
   PUBMED   22026960
REFERENCE   6  (residues 1 to 542)
  AUTHORS   Vallejo-Illarramendi,A., Domercq,M. and Matute,C.
  TITLE     A novel alternative splicing form of excitatory amino acid
            transporter 1 is a negative regulator of glutamate uptake
  JOURNAL   J Neurochem 95 (2), 341-348 (2005)
   PUBMED   16042756
  REMARK    GeneRIF: EAAT1ex9skip splice variant is a negative regulator of
            full-length EAAT1 function in the human brain
REFERENCE   7  (residues 1 to 542)
  AUTHORS   Takai,S., Yamada,K., Kawakami,H., Tanaka,K. and Nakamura,S.
  TITLE     Localization of the gene (SLC1A3) encoding human glutamate
            transporter (GluT-1) to 5p13 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 209-210 (1995)
   PUBMED   7698014
REFERENCE   8  (residues 1 to 542)
  AUTHORS   Shashidharan,P., Huntley,G.W., Meyer,T., Morrison,J.H. and
            Plaitakis,A.
  TITLE     Neuron-specific human glutamate transporter: molecular cloning,
            characterization and expression in human brain
  JOURNAL   Brain Res 662 (1-2), 245-250 (1994)
   PUBMED   7859077
REFERENCE   9  (residues 1 to 542)
  AUTHORS   Arriza,J.L., Fairman,W.A., Wadiche,J.I., Murdoch,G.H.,
            Kavanaugh,M.P. and Amara,S.G.
  TITLE     Functional comparisons of three glutamate transporter subtypes
            cloned from human motor cortex
  JOURNAL   J Neurosci 14 (9), 5559-5569 (1994)
   PUBMED   7521911
REFERENCE   10 (residues 1 to 542)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010631.6 and AC008957.7.
            
            Summary: This gene encodes a member of a member of a high affinity
            glutamate transporter family. This gene functions in the
            termination of excitatory neurotransmission in central nervous
            system. Mutations are associated with episodic ataxia, Type 6.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.345059.1,
                                           SRR14038196.1209287.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..542
                     /product="excitatory amino acid transporter 1 isoform 1"
                     /note="excitatory amino acid transporter 1; GLAST-1;
                     sodium-dependent glutamate/aspartate transporter 1; solute
                     carrier family 1 (glial high affinity glutamate
                     transporter), member 3"
                     /calculated_mol_wt=59441
     Region          46..496
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            87..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            123..145
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            237..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            270..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            319..340
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            386..412
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            473..494
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P43003.1)"
     CDS             1..542
                     /gene="SLC1A3"
                     /gene_synonym="EA6; EAAT1; GLAST; GLAST1"
                     /coded_by="NM_001438456.1:365..1993"
                     /note="isoform 1 is encoded by transcript variant 8"
                     /db_xref="GeneID:6507"
                     /db_xref="HGNC:HGNC:10941"
                     /db_xref="MIM:600111"
ORIGIN      
        1 mtksngeepk mggrmerfqq gvrkrtllak kkvqnitked vksylfrnaf vlltvtaviv
       61 gtilgftlrp yrmsyrevky fsfpgellmr mlqmlvlpli isslvtgmaa ldskasgkmg
      121 mravvyymtt tiiavvigii iviiihpgkg tkenmhregk ivrvtaadaf ldlirnmfpp
      181 nlveacfkqf ktnyekrsfk vpiqanetlv gavinnvsea metltritee lvpvpgsvng
      241 vnalglvvfs mcfgfvignm keqgqalref fdslneaimr lvavimwyap vgilfliagk
      301 ivemedmgvi ggqlamytvt vivgllihav ivlpllyflv trknpwvfig gllqalital
      361 gtssssatlp itfkcleenn gvdkrvtrfv lpvgatinmd gtalyealaa ifiaqvnnfe
      421 lnfgqiitis itataasiga agipqaglvt mvivltsvgl ptdditliia vdwfldrlrt
      481 ttnvlgdslg agivehlsrh elknrdvemg nsvieenemk kpyqliaqdn etekpidset
      541 km
//
LOCUS       NP_001394115             173 aa            linear   PRI 21-NOV-2025
DEFINITION  sodium channel protein type 5 subunit alpha isoform i [Homo
            sapiens].
ACCESSION   NP_001394115
VERSION     NP_001394115.1
DBSOURCE    REFSEQ: accession NM_001407186.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Hu,Y., Zhang,C., Wang,S., Xiong,H., Xie,W., Zeng,Z., Cai,H.,
            Wang,Q.K. and Lu,Z.
  TITLE     14-3-3epsilon/YWHAE regulates the transcriptional expression of
            cardiac sodium channel NaV1.5
  JOURNAL   Heart Rhythm 21 (11), 2320-2329 (2024)
   PUBMED   38750908
  REMARK    GeneRIF: 14-3-3epsilon/YWHAE regulates the transcriptional
            expression of cardiac sodium channel NaV1.5.
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Cadena-Ullauri,S., Guevara-Ramirez,P., Ruiz-Pozo,V.A.,
            Tamayo-Trujillo,R., Paz-Cruz,E., Simancas-Racines,D.,
            Ibarra-Castillo,R., Laso-Bayas,J.L. and Zambrano,A.K.
  TITLE     Genomic analysis of an Ecuadorian individual carrying an SCN5A rare
            variant
  JOURNAL   BMC Cardiovasc Disord 24 (1), 388 (2024)
   PUBMED   39068398
  REMARK    GeneRIF: Genomic analysis of an Ecuadorian individual carrying an
            SCN5A rare variant.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Tariq,U., Sarkar,S., Malladi,N., Kumar,R., Bugga,P., Chakraborty,P.
            and Banerjee,S.K.
  TITLE     Knockdown of SCN5A alters metabolic-associated genes and aggravates
            hypertrophy in the cardiomyoblast
  JOURNAL   Mol Biol Rep 51 (1), 661 (2024)
   PUBMED   38758505
  REMARK    GeneRIF: Knockdown of SCN5A alters metabolic-associated genes and
            aggravates hypertrophy in the cardiomyoblast.
            Erratum:[Mol Biol Rep. 2024 Jul 26;51(1):852. doi:
            10.1007/s11033-024-09742-9. PMID: 39060789]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Wright,K.M., Nathan,S., Jiang,H., Xia,W., Kim,H., Chakouri,N.,
            Nwafor,J.N., Fossier,L., Srinivasan,L., Chen,Z., Boronina,T.,
            Post,J., Paul,S., Cole,R.N., Ben-Johny,M., Cole,P.A. and
            Gabelli,S.B.
  TITLE     NEDD4L intramolecular interactions regulate its auto and substrate
            NaV1.5 ubiquitination
  JOURNAL   J Biol Chem 300 (3), 105715 (2024)
   PUBMED   38309503
  REMARK    GeneRIF: NEDD4L intramolecular interactions regulate its auto and
            substrate NaV1.5 ubiquitination.
REFERENCE   5  (residues 1 to 173)
  AUTHORS   George,A.L. Jr., Varkony,T.A., Drabkin,H.A., Han,J., Knops,J.F.,
            Finley,W.H., Brown,G.B., Ward,D.C. and Haas,M.
  TITLE     Assignment of the human heart tetrodotoxin-resistant voltage-gated
            Na+ channel alpha-subunit gene (SCN5A) to band 3p21
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 67-70 (1995)
   PUBMED   7956363
REFERENCE   6  (residues 1 to 173)
  AUTHORS   Jiang,C., Atkinson,D., Towbin,J.A., Splawski,I., Lehmann,M.H.,
            Li,H., Timothy,K., Taggart,R.T., Schwartz,P.J., Vincent,G.M. et al.
  TITLE     Two long QT syndrome loci map to chromosomes 3 and 7 with evidence
            for further heterogeneity
  JOURNAL   Nat Genet 8 (2), 141-147 (1994)
   PUBMED   7842012
REFERENCE   7  (residues 1 to 173)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   8  (residues 1 to 173)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 173)
  AUTHORS   Groffen,A.J., Bikker,H. and Christiaans,I.
  TITLE     Long QT Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301308
REFERENCE   10 (residues 1 to 173)
  AUTHORS   Gellens,M.E., George,A.L. Jr., Chen,L.Q., Chahine,M., Horn,R.,
            Barchi,R.L. and Kallen,R.G.
  TITLE     Primary structure and functional expression of the human cardiac
            tetrodotoxin-insensitive voltage-dependent sodium channel
  JOURNAL   Proc Natl Acad Sci U S A 89 (2), 554-558 (1992)
   PUBMED   1309946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP006241.1.
            
            Summary: The protein encoded by this gene is an integral membrane
            protein and tetrodotoxin-resistant voltage-gated sodium channel
            subunit. This protein is found primarily in cardiac muscle and is
            responsible for the initial upstroke of the action potential in an
            electrocardiogram. Defects in this gene have been associated with
            long QT syndrome type 3 (LQT3), atrial fibrillation,
            cardiomyopathy, and Brugada syndrome 1, all autosomal dominant
            cardiac diseases. Alternative splicing results in several
            transcript variants encoding different isoforms. [provided by
            RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2464650.1,
                                           SRR14038192.2048988.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN03267764,
                                           SAMN03465404 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.2"
     Protein         1..173
                     /product="sodium channel protein type 5 subunit alpha
                     isoform i"
                     /note="cardiac tetrodotoxin-insensitive voltage-dependent
                     sodium channel alpha subunit; sodium channel protein type
                     5 subunit alpha; voltage-gated sodium channel subunit
                     alpha Nav1.5; sodium channel protein cardiac muscle
                     subunit alpha; sodium channel, voltage-gated, type V,
                     alpha subunit"
                     /calculated_mol_wt=19202
     CDS             1..173
                     /gene="SCN5A"
                     /gene_synonym="CDCD2; CMD1E; CMPD2; HB1; HB2; HBBD; HH1;
                     ICCD; IVF; LQT3; Nav1.5; PFHB1; SSS1; VF1"
                     /coded_by="NM_001407186.1:210..731"
                     /note="isoform i is encoded by transcript variant 9"
                     /db_xref="GeneID:6331"
                     /db_xref="HGNC:HGNC:10593"
                     /db_xref="MIM:600163"
ORIGIN      
        1 manfllprgt ssfrrftres laaiekrmae kqargsttlq esreglpeee aprpqldlqa
       61 skklpdlygn ppqeligepl edldpfystq ktfivlnkgk tifrfsatna lyvlspfhpi
      121 rraavkilvh syplqlipae yplgahagdv hvlppphlhs slgvrvalip cws
//
LOCUS       NP_001427741            1058 aa            linear   PRI 21-NOV-2025
DEFINITION  ubiquitin-like modifier-activating enzyme 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001427741
VERSION     NP_001427741.1
DBSOURCE    REFSEQ: accession NM_001440812.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Sirenko,M., Bernard,E., Creignou,M., Domenico,D., Farina,A., Arango
            Ossa,J.E., Kosmider,O., Hasserjian,R., Jadersten,M., Germing,U.,
            Sanz,G., van de Loosdrecht,A.A., Gurnari,C., Follo,M.Y., Thol,F.,
            Zamora,L., Pinheiro,R.F., Pellagatti,A., Elias,H.K., Haase,D.,
            Sander,B., Orna,E., Zoldan,K., Eder,L.N., Sperr,W.R.,
            Thalhammer,R., Ganster,C., Ades,L., Tobiasson,M., Palomo,L., Della
            Porta,M.G., Huberman,K., Fenaux,P., Belickova,M., Savona,M.R.,
            Klimek,V.M., Santos,F.P.S., Boultwood,J., Kotsianidis,I.,
            Santini,V., Sole,F., Platzbecker,U., Heuser,M., Valent,P.,
            Finelli,C., Voso,M.T., Shih,L.Y., Ogawa,S., Fontenay,M.,
            Jansen,J.H., Cervera,J., Ebert,B.L., Bejar,R., Greenberg,P.L.,
            Gattermann,N., Malcovati,L., Cazzola,M., Beck,D.B.,
            Hellstrom-Lindberg,E. and Papaemmanuil,E.
  TITLE     Molecular and clinical presentation of UBA1-mutated myelodysplastic
            syndromes
  JOURNAL   Blood 144 (11), 1221-1229 (2024)
   PUBMED   38687605
  REMARK    GeneRIF: Molecular and clinical presentation of UBA1-mutated
            myelodysplastic syndromes.
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Chen,C., Li,Y., Chen,Z., Shi,P., Li,Y. and Qian,S.
  TITLE     A comprehensive prognostic and immune infiltration analysis of UBA1
            in pan-cancer: A computational analysis and in vitro experiments
  JOURNAL   J Cell Mol Med 28 (16), e70037 (2024)
   PUBMED   39183260
  REMARK    GeneRIF: A comprehensive prognostic and immune infiltration
            analysis of UBA1 in pan-cancer: A computational analysis and in
            vitro experiments.
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Corty,R.W., Brogan,J., Byram,K., Springer,J., Grayson,P.C. and
            Bick,A.G.
  TITLE     VEXAS-Defining UBA1 Somatic Variants in 245,368 Diverse Individuals
            in the NIH All Of Us Cohort
  JOURNAL   Arthritis Rheumatol 76 (6), 942-948 (2024)
   PUBMED   38225170
  REMARK    GeneRIF: VEXAS-Defining UBA1 Somatic Variants in 245,368 Diverse
            Individuals in the NIH All Of Us Cohort.
REFERENCE   4  (residues 1 to 1058)
  AUTHORS   Collins,J.C., Magaziner,S.J., English,M., Hassan,B., Chen,X.,
            Balanda,N., Anderson,M., Lam,A., Fernandez-Pol,S., Kwong,B.,
            Greenberg,P.L., Terrier,B., Likhite,M.E., Kosmider,O., Wang,Y.,
            Samara,N.L., Walters,K.J., Beck,D.B. and Werner,A.
  TITLE     Shared and distinct mechanisms of UBA1 inactivation across
            different diseases
  JOURNAL   EMBO J 43 (10), 1919-1946 (2024)
   PUBMED   38360993
  REMARK    GeneRIF: Shared and distinct mechanisms of UBA1 inactivation across
            different diseases.
REFERENCE   5  (residues 1 to 1058)
  AUTHORS   Hadjadj,J. and Beck,D.
  TITLE     VEXAS Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   40373178
REFERENCE   6  (residues 1 to 1058)
  AUTHORS   Baumbach-Reardon,L., Hunter,J.M., Ahearn,M.E. and Pfautsch,M.
  TITLE     Spinal Muscular Atrophy, X-Linked Infantile
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301739
REFERENCE   7  (residues 1 to 1058)
  AUTHORS   Schwartz,A.L., Trausch,J.S., Ciechanover,A., Slot,J.W. and Geuze,H.
  TITLE     Immunoelectron microscopic localization of the ubiquitin-activating
            enzyme E1 in HepG2 cells
  JOURNAL   Proc Natl Acad Sci U S A 89 (12), 5542-5546 (1992)
   PUBMED   1376922
REFERENCE   8  (residues 1 to 1058)
  AUTHORS   Ayusawa,D., Kaneda,S., Itoh,Y., Yasuda,H., Murakami,Y.,
            Sugasawa,K., Hanaoka,F. and Seno,T.
  TITLE     Complementation by a cloned human ubiquitin-activating enzyme E1 of
            the S-phase-arrested mouse FM3A cell mutant with thermolabile E1
  JOURNAL   Cell Struct Funct 17 (2), 113-122 (1992)
   PUBMED   1606621
REFERENCE   9  (residues 1 to 1058)
  AUTHORS   Takahashi,E., Ayusawa,D., Kaneda,S., Itoh,Y., Seno,T. and Hori,T.
  TITLE     The human ubiquitin-activating enzyme E1 gene (UBE1) mapped to band
            Xp11.3----p11.23 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 59 (4), 268-269 (1992)
   PUBMED   1544321
REFERENCE   10 (residues 1 to 1058)
  AUTHORS   Kudo,M., Sugasawa,K., Hori,T., Enomoto,T., Hanaoka,F. and Ui,M.
  TITLE     Human ubiquitin-activating enzyme (E1): compensation for
            heat-labile mouse E1 and its gene localization on the X chromosome
  JOURNAL   Exp Cell Res 192 (1), 110-117 (1991)
   PUBMED   1845793
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513366.11.
            
            Summary: The protein encoded by this gene catalyzes the first step
            in ubiquitin conjugation to mark cellular proteins for degradation.
            This gene complements an X-linked mouse temperature-sensitive
            defect in DNA synthesis, and thus may function in DNA repair. It is
            part of a gene cluster on chromosome Xp11.23. Alternatively spliced
            transcript variants that encode the same protein have been
            described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.916291.1,
                                           SRR14038194.4108365.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.3"
     Protein         1..1058
                     /product="ubiquitin-like modifier-activating enzyme 1
                     isoform 1"
                     /EC_number="6.2.1.45"
                     /note="POC20 centriolar protein homolog; UBA1,
                     ubiquitin-activating enzyme E1 homolog A; A1S9T and BN75
                     temperature sensitivity complementing; testicular
                     secretory protein Li 63"
                     /calculated_mol_wt=117718
     Region          1..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22314.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9099746; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Region          5..11
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P22314.3)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02053; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02053; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P22314.3)"
     Region          49..1055
                     /region_name="Ube1"
                     /note="ubiquitin-activating enzyme E1; TIGR01408"
                     /db_xref="CDD:273603"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q02053; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Region          63..611
                     /region_name="2 approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P22314.3)"
     Site            671
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            800
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            810
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            816
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02053; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            820
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            835
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            980
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     CDS             1..1058
                     /gene="UBA1"
                     /gene_synonym="A1S9; A1S9T; A1ST; AMCX1; CFAP124; GXP1;
                     POC20; SMAX2; UBA1A; UBE1; UBE1X; VEXAS"
                     /coded_by="NM_001440812.1:270..3446"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:7317"
                     /db_xref="HGNC:HGNC:12469"
                     /db_xref="MIM:314370"
ORIGIN      
        1 msssplskkr rvsgpdpkpg sncspaqsvl sevpsvptng makngseadi deglysrqly
       61 vlgheamkrl qtssvlvsgl rglgveiakn iilggvkavt lhdqgtaqwa dlssqfylre
      121 edigknraev sqprlaelns yvpvtaytgp lvedflsgfq vvvltntple dqlrvgefch
      181 nrgiklvvad trglfgqlfc dfgeemiltd sngeqplsam vsmvtkdnpg vvtcldearh
      241 gfesgdfvsf sevqgmveln gnqpmeikvl gpytfsicdt snfsdyirgg ivsqvkvpkk
      301 isfkslvasl aepdfvvtdf akfsrpaqlh igfqalhqfc aqhgrpprpr needaaelva
      361 laqavnaral pavqqnnlde dlirklayva agdlapinaf igglaaqevm kacsgkfmpi
      421 mqwlyfdale clpedkevlt edkclqrqnr ydgqvavfgs dlqeklgkqk yflvgagaig
      481 cellknfami glgcgeggei ivtdmdtiek snlnrqflfr pwdvtklksd taaaavrqmn
      541 phirvtshqn rvgpdteriy dddffqnldg vanaldnvda rmymdrrcvy yrkpllesgt
      601 lgtkgnvqvv ipfltesyss sqdppeksip ictlknfpna iehtlqward efeglfkqpa
      661 envnqyltdp kfvertlrla gtqplevlea vqrslvlqrp qtwadcvtwa chhwhtqysn
      721 nirqllhnfp pdqltssgap fwsgpkrcph pltfdvnnpl hldyvmaaan lfaqtygltg
      781 sqdraavatf lqsvqvpeft pksgvkihvs dqelqsanas vddsrleelk atlpspdklp
      841 gfkmypidfe kdddsnfhmd fivaasnlra enydipsadr hkskliagki ipaiatttaa
      901 vvglvclely kvvqghrqld sykngflnla lpffgfsepl aaprhqyynq ewtlwdrfev
      961 qglqpngeem tlkqfldyfk tehkleitml sqgvsmlysf fmpaaklker ldqpmteivs
     1021 rvskrklgrh vralvlelcc ndesgedvev pyvrytir
//
LOCUS       NP_001425591             919 aa            linear   PRI 21-NOV-2025
DEFINITION  TRPM8 channel-associated factor 2 isoform C [Homo sapiens].
ACCESSION   NP_001425591
VERSION     NP_001425591.2
DBSOURCE    REFSEQ: accession NM_001438662.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Yun,D., Liang,J., Wang,X., Fan,J., Wang,X., Li,J., Ren,X., Liu,J.,
            Ren,X., Zhang,H., Shang,G., Jin,W., Chen,L., Li,T., Zhang,C., Yu,S.
            and Yang,X.
  TITLE     TCAF2 drives glioma cellular migratory/invasion properties through
            STAT3 signaling
  JOURNAL   Mol Cell Biochem 479 (7), 1801-1815 (2024)
   PUBMED   38019450
  REMARK    GeneRIF: TCAF2 drives glioma cellular migratory/invasion properties
            through STAT3 signaling.
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Li,Y., Li,J., Chen,H., Lu,B., Lu,F., Chen,H., Liu,H. and Qian,C.
  TITLE     TCAF2 is associated with the immune microenvironment, promotes
            pathogenesis, and impairs prognosis in glioma
  JOURNAL   Gene 883, 147667 (2023)
   PUBMED   37506986
  REMARK    GeneRIF: TCAF2 is associated with the immune microenvironment,
            promotes pathogenesis, and impairs prognosis in glioma.
REFERENCE   4  (residues 1 to 919)
  AUTHORS   Li,X., Qi,Q., Li,Y., Miao,Q., Yin,W., Pan,J., Zhao,Z., Chen,X.,
            Yang,F., Zhou,X., Huang,M., Wang,C., Deng,L., Huang,D., Qi,M.,
            Fan,S., Zhang,Y., Qiu,S., Deng,W., Liu,T., Chen,M., Ye,W. and
            Zhang,D.
  TITLE     TCAF2 in Pericytes Promotes Colorectal Cancer Liver Metastasis via
            Inhibiting Cold-Sensing TRPM8 Channel
  JOURNAL   Adv Sci (Weinh) 10 (30), e2302717 (2023)
   PUBMED   37635201
  REMARK    GeneRIF: TCAF2 in Pericytes Promotes Colorectal Cancer Liver
            Metastasis via Inhibiting Cold-Sensing TRPM8 Channel.
REFERENCE   5  (residues 1 to 919)
  AUTHORS   Hsieh,P., Dang,V., Vollger,M.R., Mao,Y., Huang,T.H., Dishuck,P.C.,
            Baker,C., Cantsilieris,S., Lewis,A.P., Munson,K.M., Sorensen,M.,
            Welch,A.E., Underwood,J.G. and Eichler,E.E.
  TITLE     Evidence for opposing selective forces operating on human-specific
            duplicated TCAF genes in Neanderthals and humans
  JOURNAL   Nat Commun 12 (1), 5118 (2021)
   PUBMED   34433829
  REMARK    GeneRIF: Evidence for opposing selective forces operating on
            human-specific duplicated TCAF genes in Neanderthals and humans.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 919)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 919)
  AUTHORS   Gkika,D., Lemonnier,L., Shapovalov,G., Gordienko,D., Poux,C.,
            Bernardini,M., Bokhobza,A., Bidaux,G., Degerny,C., Verreman,K.,
            Guarmit,B., Benahmed,M., de Launoit,Y., Bindels,R.J., Fiorio Pla,A.
            and Prevarskaya,N.
  TITLE     TRP channel-associated factors are a novel protein family that
            regulates TRPM8 trafficking and activity
  JOURNAL   J Cell Biol 208 (1), 89-107 (2015)
   PUBMED   25559186
  REMARK    GeneRIF: Report novel TRP channel-associated factors that modulate
            TRPM8 activity.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073264.5 and AC106862.3.
            
            On Apr 25, 2025 this sequence version replaced NP_001425591.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.31140.1,
                                           SRR11853567.28190.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q35"
     Protein         1..919
                     /product="TRPM8 channel-associated factor 2 isoform C"
                     /note="family with sequence similarity 139, member A;
                     protein FAM115C; family with sequence similarity 115,
                     member C; TRP channel-associated factor 2"
                     /calculated_mol_wt=100775
     Region          522..632
                     /region_name="M60-like_N"
                     /note="N-terminal domain of M60-like peptidases;
                     pfam17291"
                     /db_xref="CDD:435844"
     Region          633..889
                     /region_name="Peptidase_M60"
                     /note="Peptidase M60, enhancin and enhancin-like;
                     pfam13402"
                     /db_xref="CDD:433178"
     CDS             1..919
                     /gene="TCAF2"
                     /gene_synonym="FAM115C; FAM139A; GATD9; GATD9B"
                     /coded_by="NM_001438662.2:62..2821"
                     /note="isoform C is encoded by transcript variant 9"
                     /db_xref="GeneID:285966"
                     /db_xref="HGNC:HGNC:26878"
                     /db_xref="MIM:616252"
ORIGIN      
        1 matiaaaafe almdgvtcwd vprgpipsel lligeaafpv mvndkgqvli aassygrgrl
       61 vvvshegyls htglapflln avswlcpcpg apvgvhpsla plvnilqdag leaqvkpepg
      121 eplgvycina yndtltatli qfvkhgggll iggqawywas qhgpdkvlsr fpgnkvtsva
      181 gvyftdtygd rdrfkvskkv pkiplhvryg edvrqdqqql legiseldir tggvpsqllv
      241 hgalafplgl daslncflaa ahygrgrvvl aahecllcap kmgpfllnav rwlargqtgk
      301 vgvntnlkdl cpllsehglq cslephlnsd lcvycckays dkeakqlqef vaegggllig
      361 gqawwwasqn pghcplagfp gniilncfgl silpqtlkag cfpvptpemr syhfrkalsq
      421 fqailnheng nleksclakl rvdgaaflqi paegvpayis lhrllrkmlr gsglpavsre
      481 npvasdsyea avlslatgla hsgtdcsqla qglgtwtcss slypskhpit veinginpgn
      541 ndcwvstgly llegqnaevs lseaaasagl rvqigchtdd ltkarklsra pvvthqcwmd
      601 rtersvsclw ggllyvivpk gsqlgpvpvt irgavpapyy klgktsleew krqmqenlap
      661 wgelatdnii ltvpttnlqa lkdpepvlrl wdemmqavar laaepfpfrr perivadvqi
      721 sagwmhsgyp imchlesvke iinemdmrsr gvwgpihelg hnqqrhgwef pphtteatcn
      781 lwsvyvhetv lgipraqahe alsppererr ikahlgkgap lcdwnvwtal etylqlqeaf
      841 gwepftqlfa eyqtlshlpk dntgrmnlwv kkfsekvkkn lvpffeawgw piqkevadsl
      901 aslpewqenp mqvylrark
//
LOCUS       NP_001425202             320 aa            linear   PRI 21-NOV-2025
DEFINITION  protein GNAS isoform m [Homo sapiens].
ACCESSION   NP_001425202 XP_016883306 XP_054179344
VERSION     NP_001425202.1
DBSOURCE    REFSEQ: accession NM_001438273.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,J., Nie,Q., Cheng,J., Zhong,Y.N., Zhang,T., Zhang,X., Ge,X.,
            Ding,Y., Niu,C., Gao,Y., Wang,K., Gao,M., Wang,X., Chen,W., Yun,C.,
            Ye,C., Xu,J., Shaoyong,W., Zhang,L., Shang,P., Luo,X., Zhang,Z.,
            Zheng,X., Sha,X., Zhang,J., Nie,S., Zhang,X., Ren,F., Liu,H.,
            Dong,E., Yu,X., Ji,L., Pang,Y., Sun,J.P. and Jiang,C.
  TITLE     A microbial amino-acid-conjugated bile acid, tryptophan-cholic
            acid, improves glucose homeostasis via the orphan receptor MRGPRE
  JOURNAL   Cell 188 (17), 4530-4548 (2025)
   PUBMED   40446798
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Crane,J.L., Shamblott,M.J., Axelman,J., Hsu,S., Levine,M.A. and
            Germain-Lee,E.L.
  TITLE     Imprinting status of Galpha(s), NESP55, and XLalphas in cell
            cultures derived from human embryonic germ cells: GNAS imprinting
            in human embryonic germ cells
  JOURNAL   Clin Transl Sci 2 (5), 355-360 (2009)
   PUBMED   20443919
  REMARK    GeneRIF: analysis of the imprinting Status of Galpha(s), NESP55,
            and XLalphas in cell cultures derived from human embryonic germ
            cells
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Bastepe,M.
  TITLE     The GNAS Locus: Quintessential Complex Gene Encoding Gsalpha,
            XLalphas, and other Imprinted Transcripts
  JOURNAL   Curr Genomics 8 (6), 398-414 (2007)
   PUBMED   19412439
  REMARK    GeneRIF: GNAS locus has a highly complex imprinted expression
            pattern, giving rise to transcripts (including non-coding) that are
            maternally, paternally, or biallelically expressed.
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Jakobsen,A.M., Ahlman,H., Kolby,L., Abrahamsson,J.,
            Fischer-Colbrie,R. and Nilsson,O.
  TITLE     NESP55, a novel chromogranin-like peptide, is expressed in
            endocrine tumours of the pancreas and adrenal medulla but not in
            ileal carcinoids
  JOURNAL   Br J Cancer 88 (11), 1746-1754 (2003)
   PUBMED   12771991
  REMARK    GeneRIF: Neuroendocrine secretory protein 55 is found in a subset
            of neuroendocrine tumours showing differentiation towards adrenal
            chromaffin cells and pancreatic islets cells and not in ileal
            carcinoids
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Freson,K., Jaeken,J., Van Helvoirt,M., de Zegher,F.,
            Wittevrongel,C., Thys,C., Hoylaerts,M.F., Vermylen,J. and Van
            Geet,C.
  TITLE     Functional polymorphisms in the paternally expressed XLalphas and
            its cofactor ALEX decrease their mutual interaction and enhance
            receptor-mediated cAMP formation
  JOURNAL   Hum Mol Genet 12 (10), 1121-1130 (2003)
   PUBMED   12719376
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Weiss,U., Ischia,R., Eder,S., Lovisetti-Scamihorn,P., Bauer,R. and
            Fischer-Colbrie,R.
  TITLE     Neuroendocrine secretory protein 55 (NESP55): alternative splicing
            onto transcripts of the GNAS gene and posttranslational processing
            of a maternally expressed protein
  JOURNAL   Neuroendocrinology 71 (3), 177-186 (2000)
   PUBMED   10729789
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Ischia,R., Lovisetti-Scamihorn,P., Hogue-Angeletti,R.,
            Wolkersdorfer,M., Winkler,H. and Fischer-Colbrie,R.
  TITLE     Molecular cloning and characterization of NESP55, a novel
            chromogranin-like precursor of a peptide with 5-HT1B receptor
            antagonist activity
  JOURNAL   J Biol Chem 272 (17), 11657-11662 (1997)
   PUBMED   9111083
REFERENCE   8  (residues 1 to 320)
  AUTHORS   Haldeman-Englert,C.R., Hurst,A.C.E. and Levine,M.A.
  TITLE     Disorders of GNAS Inactivation
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29072892
REFERENCE   9  (residues 1 to 320)
  AUTHORS   Szymczuk,V., Florenzano,P., de Castro,L.F., Collins,M.T. and
            Boyce,A.M.
  TITLE     Fibrous Dysplasia / McCune-Albright Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719192
REFERENCE   10 (residues 1 to 320)
  AUTHORS   Weinstein,L.S., Gejman,P.V., de Mazancourt,P., American,N. and
            Spiegel,A.M.
  TITLE     A heterozygous 4-bp deletion mutation in the Gs alpha gene (GNAS1)
            in a patient with Albright hereditary osteodystrophy
  JOURNAL   Genomics 13 (4), 1319-1321 (1992)
   PUBMED   1505964
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121917.20 and AL109840.24.
            
            On or before Apr 18, 2025 this sequence version replaced
            XP_016883306.1, XP_054179344.1.
            
            Summary: This locus has a highly complex imprinted expression
            pattern. It gives rise to maternally, paternally, and biallelically
            expressed transcripts that are derived from four alternative
            promoters and 5' exons. Some transcripts contain a differentially
            methylated region (DMR) at their 5' exons, and this DMR is commonly
            found in imprinted genes and correlates with transcript expression.
            An antisense transcript is produced from an overlapping locus on
            the opposite strand. One of the transcripts produced from this
            locus, and the antisense transcript, are paternally expressed
            noncoding RNAs, and may regulate imprinting in this region. In
            addition, one of the transcripts contains a second overlapping ORF,
            which encodes a structurally unrelated protein - Alex. Alternative
            splicing of downstream exons is also observed, which results in
            different forms of the stimulatory G-protein alpha subunit, a key
            element of the classical signal transduction pathway linking
            receptor-ligand interactions with the activation of adenylyl
            cyclase and a variety of cellular reponses. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            Mutations in this gene result in pseudohypoparathyroidism type 1a,
            pseudohypoparathyroidism type 1b, Albright hereditary
            osteodystrophy, pseudopseudohypoparathyroidism, McCune-Albright
            syndrome, progressive osseus heteroplasia, polyostotic fibrous
            dysplasia of bone, and some pituitary tumors. [provided by RefSeq,
            Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.998792.1,
                                           SRR14372079.158388.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 19412439
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.32"
     Protein         1..320
                     /product="protein GNAS isoform m"
                     /note="secretogranin VI; G protein subunit alpha S;
                     guanine nucleotide binding protein (G protein), alpha
                     stimulating activity polypeptide 1; guanine nucleotide
                     regulatory protein; adenylate cyclase-stimulating G alpha
                     protein; protein ALEX; extra large alphas protein;
                     alternative gene product encoded by XL-exon"
                     /calculated_mol_wt=37382
     Region          1..314
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Site            order(19,23,27,30,33..34,54,57,98,127,152,160,164)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Site            125..133
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            130
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(131,133,135,146,148,152..154,156,159..160,162..165)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(133,158,161..162,165)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            149..152
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            150..166
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Site            218..221
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(283..294,296..299)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Site            291..293
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..320
                     /gene="GNAS"
                     /gene_synonym="AHO; AIMAH1; C20orf45; GNAS1; GPSA; GSA;
                     GSP; NESP; PITA3; POH; SCG6; SgVI"
                     /coded_by="NM_001438273.1:213..1175"
                     /note="isoform m is encoded by transcript variant 17"
                     /db_xref="GeneID:2778"
                     /db_xref="HGNC:HGNC:4392"
                     /db_xref="MIM:139320"
ORIGIN      
        1 mrilhvngfn gdekatkvqd iknnlkeaie tivaamsnlv ppvelanpen qfrvdyilsv
       61 mnvpdfdfpp efyehakalw edegvracye rsneyqlidc aqyfldkidv ikqadyvpsd
      121 qdllrcrvlt sgifetkfqv dkvnfhmfdv ggqrderrkw iqcfndvtai ifvvasssyn
      181 mvirednqtn rlqealnlfk siwnnrwlrt isvilflnkq dllaekvlag kskiedyfpe
      241 faryttpeda tpepgedprv trakyfirde flristasgd grhycyphft cavdtenirr
      301 vfndcrdiiq rmhlrqyell
//
LOCUS       NP_001400301             387 aa            linear   PRI 21-NOV-2025
DEFINITION  telomeric repeat-binding factor 1 isoform 12 [Homo sapiens].
ACCESSION   NP_001400301
VERSION     NP_001400301.1
DBSOURCE    REFSEQ: accession NM_001413372.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Hu,H., van Roon,A.M., Ghanim,G.E., Ahsan,B., Oluwole,A.O.,
            Peak-Chew,S.Y., Robinson,C.V. and Nguyen,T.H.D.
  TITLE     Structural basis of telomeric nucleosome recognition by shelterin
            factor TRF1
  JOURNAL   Sci Adv 9 (34), eadi4148 (2023)
   PUBMED   37624885
  REMARK    GeneRIF: Structural basis of telomeric nucleosome recognition by
            shelterin factor TRF1.
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Harmak,H., Redouane,S., Charoute,H., Aniq Filali,O., Barakat,A. and
            Rouba,H.
  TITLE     In silico exploration and molecular dynamics of deleterious SNPs on
            the human TERF1 protein triggering male infertility
  JOURNAL   J Biomol Struct Dyn 41 (24), 14665-14688 (2023)
   PUBMED   36995171
  REMARK    GeneRIF: In silico exploration and molecular dynamics of
            deleterious SNPs on the human TERF1 protein triggering male
            infertility.
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Abreu,P.L., Lee,Y.W. and Azzalin,C.M.
  TITLE     In Vitro Characterization of the Physical Interactions between the
            Long Noncoding RNA TERRA and the Telomeric Proteins TRF1 and TRF2
  JOURNAL   Int J Mol Sci 23 (18), 10463 (2022)
   PUBMED   36142374
  REMARK    GeneRIF: In Vitro Characterization of the Physical Interactions
            between the Long Noncoding RNA TERRA and the Telomeric Proteins
            TRF1 and TRF2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Jack,A., Kim,Y., Strom,A.R., Lee,D.S.W., Williams,B., Schaub,J.M.,
            Kellogg,E.H., Finkelstein,I.J., Ferro,L.S., Yildiz,A. and
            Brangwynne,C.P.
  TITLE     Compartmentalization of telomeres through DNA-scaffolded phase
            separation
  JOURNAL   Dev Cell 57 (2), 277-290 (2022)
   PUBMED   35077681
  REMARK    GeneRIF: Compartmentalization of telomeres through DNA-scaffolded
            phase separation.
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Broccoli,D., Chong,L., Oelmann,S., Fernald,A.A., Marziliano,N., van
            Steensel,B., Kipling,D., Le Beau,M.M. and de Lange,T.
  TITLE     Comparison of the human and mouse genes encoding the telomeric
            protein, TRF1: chromosomal localization, expression and conserved
            protein domains
  JOURNAL   Hum Mol Genet 6 (1), 69-76 (1997)
   PUBMED   9002672
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Lu,K.P., Hanes,S.D. and Hunter,T.
  TITLE     A human peptidyl-prolyl isomerase essential for regulation of
            mitosis
  JOURNAL   Nature 380 (6574), 544-547 (1996)
   PUBMED   8606777
REFERENCE   8  (residues 1 to 387)
  AUTHORS   Bilaud,T., Koering,C.E., Binet-Brasselet,E., Ancelin,K.,
            Pollice,A., Gasser,S.M. and Gilson,E.
  TITLE     The telobox, a Myb-related telomeric DNA binding motif found in
            proteins from yeast, plants and human
  JOURNAL   Nucleic Acids Res 24 (7), 1294-1303 (1996)
   PUBMED   8614633
REFERENCE   9  (residues 1 to 387)
  AUTHORS   Chong,L., van Steensel,B., Broccoli,D., Erdjument-Bromage,H.,
            Hanish,J., Tempst,P. and de Lange,T.
  TITLE     A human telomeric protein
  JOURNAL   Science 270 (5242), 1663-1667 (1995)
   PUBMED   7502076
REFERENCE   10 (residues 1 to 387)
  AUTHORS   Zhong,Z., Shiue,L., Kaplan,S. and de Lange,T.
  TITLE     A mammalian factor that binds telomeric TTAGGG repeats in vitro
  JOURNAL   Mol Cell Biol 12 (11), 4834-4843 (1992)
   PUBMED   1406665
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022893.6.
            
            Summary: This gene encodes a telomere specific protein which is a
            component of the telomere nucleoprotein complex. This protein is
            present at telomeres throughout the cell cycle and functions as an
            inhibitor of telomerase, acting in cis to limit the elongation of
            individual chromosome ends. The protein structure contains a
            C-terminal Myb motif, a dimerization domain near its N-terminus and
            an acidic N-terminus. Multiple transcripts of this gene are
            alternatively spliced products. [provided by RefSeq, Aug 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2055487.1,
                                           SRR14038196.3370421.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.11"
     Protein         1..387
                     /product="telomeric repeat-binding factor 1 isoform 12"
                     /note="NIMA-interacting protein 2; telomeric protein
                     Pin2/TRF1; TTAGGG repeat-binding factor 1; telomeric
                     repeat binding factor (NIMA-interacting) 1"
                     /calculated_mol_wt=44649
     Region          76..232
                     /region_name="TRFH"
                     /note="Telomeric Repeat binding Factor or TTAGGG Repeat
                     binding Factor, central (dimerization) domain Homology;
                     TRFH. Telomeres are protein/DNA complexes that make up the
                     physical ends of eukaryotic linear chromosomes and are
                     essential for chromosome stability; cl02779"
                     /db_xref="CDD:413471"
     Region          329..377
                     /region_name="SANT_TRF"
                     /note="Telomere repeat binding factor-like DNA-binding
                     domains of the SANT/myb-like family; cd11660"
                     /db_xref="CDD:212558"
     Site            order(329..331,349,351..352,363,365..367,369..371,
                     373..374)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212558"
     CDS             1..387
                     /gene="TERF1"
                     /gene_synonym="hTRF1-AS; PIN2; t-TRF1; TRBF1; TRF; TRF1"
                     /coded_by="NM_001413372.1:24..1187"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="GeneID:7013"
                     /db_xref="HGNC:HGNC:11728"
                     /db_xref="MIM:600951"
ORIGIN      
        1 maedvssaap sprgcadgrd adpteeqmae terndeeqfe cqellecqvq vgapeeeeee
       61 eedaglvaea eavaagwmld flclslcraf rdgrsedfrr trnsaedaqf enderitple
      121 salmiwgsie kehdklheei qnlikiqaia vcmengnfke aeevferifg dpnshmpfks
      181 kllmiisqkd tfhsffqhfs ynhmmekiks yvnyvlseks stflmkaaak vveskrtrti
      241 tsqdkpsgnd vemeteanld trkrshknlf lsklqhgtqq qdlnkkerrv gtpqstkkkk
      301 esrratesri pvsksqpvtp ekhrarkrqa wlweedknlr sgvrkygegn wskillhykf
      361 nnrtsvmlkd rwrtmkklkl issdsed
//
LOCUS       NP_001392813             620 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 11 [Homo sapiens].
ACCESSION   NP_001392813
VERSION     NP_001392813.1
DBSOURCE    REFSEQ: accession NM_001405884.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 620)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 620)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 620)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 620)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 620)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 620)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 620)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 620)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 620)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 620)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3179519.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..620
                     /product="KAT8 regulatory NSL complex subunit 1 isoform
                     11"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=68358
     Region          400..520
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..620
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405884.1:139..2001"
                     /note="isoform 11 is encoded by transcript variant 25"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 mllgcllrrr rsewkwaadr aaivsrwnwl qahvsdleyr irqqtdiykq irankglivl
       61 gevpppehtt dlflplssev ktdhgtdkli esvsqplenh gapiighise slstkscgal
      121 rpvngvintl qpvladhipg dssdaeeqlh kkqrlnlvss ssdgtcvaar trpvlsckkr
      181 rlvrpnsivp lskkvhrnst irpgcdvnps calcgsgsin tmppeihyea pllerlsqld
      241 scvhpvlafp ddvptslhfq smlksqwqnk pfdkikppkk lslkhrapmp gslpdsarkd
      301 rhklvssflt tamlkhhtdm ssssylaath hpphsplvrq lstssdspap assssqvtas
      361 tsqqpvrrrr gessfdinni vipmsvaatt rveklqykei ltpswrevdl qslkgspdee
      421 neeiedlsda afaalhakce emerarwlwt tsvppqrrgs rsyrssdgrt tpqlgsanps
      481 tpqpaspdvs sshslseysh gqsprspisp elhsapltpv ardtprhlas edtrcstpel
      541 gldeqsvqpw errtfplahs pqaecedqld aqeraarctr rtsgsktgre teaaptsppi
      601 vplksrhlva aataqrpthr
//
LOCUS       NP_001428154             446 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 8 [Homo sapiens].
ACCESSION   NP_001428154
VERSION     NP_001428154.1
DBSOURCE    REFSEQ: accession NM_001441225.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 446)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3510109.1,
                                           SRR18074967.2516858.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..446
                     /product="calcium uptake protein 1, mitochondrial isoform
                     8"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=50899
     Region          222..411
                     /region_name="EFh_MICU"
                     /note="EF-hand, calcium binding motif, found in
                     mitochondrial calcium uptake proteins MICU1, MICU2, MICU3,
                     and similar proteins; cl28896"
                     /db_xref="CDD:333716"
     Region          222..251
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320080"
     Region          277..307
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320080"
     CDS             1..446
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001441225.1:72..1412"
                     /note="isoform 8 is encoded by transcript variant 12"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mfrlnslsal aelavgsrwy hggsqpiqir rrlmmvaflg asavtastgl lwkrahaesp
       61 pcvdnlksdi gdkgknkdeg dvcnhekkta dlaphpeekk kkrsgfrdrk vmeyenrira
      121 ystpdkifry fatlkvisep geaevfmtpe dfvrsitpne kqpehlgldq yiikrfdgkk
      181 isqerekfad egsifytlge cglisfsdyi flttvlstpq rnfeiafkmf dlngdgevdm
      241 eefeqvqsii rsqtsmgmrh rdrpttgntl ksglcsaltt yffgadlkgk ltiknflefq
      301 rklqhdvlkl eferhdpvdg riterqfggm llaysgvqsk kltamqrqlk khfkegkglt
      361 fqevenfftf lknindvdta lsfyhmagas ldkgngelsn kefvsimkqr lmrglekpkd
      421 mgftrlmqam wkcaqetawd falpkq
//
LOCUS       NP_001392804            1042 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 6 [Homo sapiens].
ACCESSION   NP_001392804 XP_047291754
VERSION     NP_001392804.1
DBSOURCE    REFSEQ: accession NM_001405875.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1042)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1042)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1042)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1042)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1042)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1042)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1042)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            On May 6, 2022 this sequence version replaced XP_047291754.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2223824.1,
                                           SRR18074967.1714374.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1042
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 6"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=113587
     Site            104
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          145..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          225..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          399..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          822..942
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..1042
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405875.1:251..3379"
                     /note="isoform 6 is encoded by transcript variant 16"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankgli
      481 vlgevpppeh ttdlflplss evktdhgtdk liesvsqple nhgapiighi seslstkscg
      541 alrpvngvin tlqpvladhi pgdssdaeeq lhkkqrlnlv ssssdgtcva artrpvlsck
      601 krrlvrpnsi vplskkvhrn stirpgcdvn pscalcgsgs intmppeihy eapllerlsq
      661 ldscvhpvla fpddvptslh fqsmlksqwq nkpfdkikpp kklslkhrap mpgslpdsar
      721 kdrhklvssf lttamlkhht dmssssylaa thhpphsplv rqlstssdsp apassssqvt
      781 astsqqpvrr rrgessfdin nivipmsvaa ttrveklqyk eiltpswrev dlqslkgspd
      841 eeneeiedls daafaalhak ceemerarwl wttsvppqrr gsrsyrssdg rttpqlgsan
      901 pstpqpaspd vssshslsey shgqsprspi spelhsaplt pvardtprhl asedtrcstp
      961 elgldeqsvq pwerrtfpla hspqaecedq ldaqeraarc trrtsgsktg reteaaptsp
     1021 pivplksrhl vaaataqrpt hr
//
LOCUS       NP_001401585             526 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 2 isoform d [Homo sapiens].
ACCESSION   NP_001401585
VERSION     NP_001401585.1
DBSOURCE    REFSEQ: accession NM_001414656.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Jung,J.H., Lee,D., Ko,H.M. and Jang,H.J.
  TITLE     Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in Colorectal
            Cancer Cells by Activating p53
  JOURNAL   Biomolecules 11 (10), 1492 (2021)
   PUBMED   34680125
  REMARK    GeneRIF: Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in
            Colorectal Cancer Cells by Activating p53.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Royer-Bertrand,B., Cisarova,K., Niel Butschi,F., Foletti,G.,
            Guinchat,V., Tran,C., Superti-Furga,A. and Good,J.M.
  TITLE     CNOT2 haploinsufficiency in a 40-year-old man with intellectual
            disability, autism, and seizures
  JOURNAL   Am J Med Genet A 185 (8), 2602-2606 (2021)
   PUBMED   34018673
  REMARK    GeneRIF: CNOT2 haploinsufficiency in a 40-year-old man with
            intellectual disability, autism, and seizures.
            Review article
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Jayne,S., Zwartjes,C.G., van Schaik,F.M. and Timmers,H.T.
  TITLE     Involvement of the SMRT/NCoR-HDAC3 complex in transcriptional
            repression by the CNOT2 subunit of the human Ccr4-Not complex
  JOURNAL   Biochem J 398 (3), 461-467 (2006)
   PUBMED   16712523
  REMARK    GeneRIF: This study shows that SMRT/NCoR-HDAC3 complex is a
            cofactor of CNOT2-mediated repression and suggests that
            transcriptional regulation by the Ccr4-Not complex involves
            regulation of chromatin modification.
REFERENCE   6  (residues 1 to 526)
  AUTHORS   Winkler,G.S., Mulder,K.W., Bardwell,V.J., Kalkhoven,E. and
            Timmers,H.T.
  TITLE     Human Ccr4-Not complex is a ligand-dependent repressor of nuclear
            receptor-mediated transcription
  JOURNAL   EMBO J 25 (13), 3089-3099 (2006)
   PUBMED   16778766
REFERENCE   7  (residues 1 to 526)
  AUTHORS   Shi,J. and Nelson,M.A.
  TITLE     The cyclin-dependent kinase 11 interacts with NOT2
  JOURNAL   Biochem Biophys Res Commun 334 (4), 1310-1316 (2005)
   PUBMED   16039607
  REMARK    GeneRIF: These findings suggest that CDK11 may contribute to
            apoptosis by regulating the activity of NOT2 independent of its
            kinase activity.
REFERENCE   8  (residues 1 to 526)
  AUTHORS   Zwartjes,C.G., Jayne,S., van den Berg,D.L. and Timmers,H.T.
  TITLE     Repression of promoter activity by CNOT2, a subunit of the
            transcription regulatory Ccr4-not complex
  JOURNAL   J Biol Chem 279 (12), 10848-10854 (2004)
   PUBMED   14707134
  REMARK    GeneRIF: major repression function of CNOT2 is localized in a
            specialized protein motif, the Not-Box
REFERENCE   9  (residues 1 to 526)
  AUTHORS   Denis,C.L. and Chen,J.
  TITLE     The CCR4-NOT complex plays diverse roles in mRNA metabolism
  JOURNAL   Prog Nucleic Acid Res Mol Biol 73, 221-250 (2003)
   PUBMED   12882519
  REMARK    Review article
REFERENCE   10 (residues 1 to 526)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092881.8 and AC025569.37.
            
            Summary: This gene encodes a subunit of the multi-component
            CCR4-NOT complex. The CCR4-NOT complex regulates mRNA synthesis and
            degradation and is also thought to be involved in mRNA splicing,
            transport and localization. The encoded protein interacts with
            histone deacetylases and functions as a repressor of polymerase II
            transcription. Alternatively spliced transcript variants have been
            observed for this gene. [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.890568.1,
                                           SRR14038193.3052031.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..526
                     /product="CCR4-NOT transcription complex subunit 2 isoform
                     d"
                     /note="negative regulator of transcription 2;
                     CCR4-associated factor 2; CC chemokine receptor 4-negative
                     regulator of transcription 2"
                     /calculated_mol_wt=58111
     Region          382..505
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..526
                     /gene="CNOT2"
                     /gene_synonym="CDC36; HSPC131; IDNADFS; NOT2; NOT2H"
                     /coded_by="NM_001414656.1:144..1724"
                     /note="isoform d is encoded by transcript variant 10"
                     /db_xref="GeneID:4848"
                     /db_xref="HGNC:HGNC:7878"
                     /db_xref="MIM:604909"
ORIGIN      
        1 mvrtdghtls ekrnyqvtns mfgasrkkfv egvdsdyhde nmyysqssmf phrsekdmla
       61 spstsgalgl pmrgmsnntp qlnrslsqgt qlpshvtptt gvptmslhtp pspsrgilpm
      121 nprnmmnhsq vgqgigipsr tnsmsssglg spnrsspsii cmpkqqpsrq pftvnsmsgf
      181 gmnrnqafgm nnslssnifn gtdgsenvtg ldlsdfpala drnrregsgn ptplinplag
      241 rapyvgmvtk paneqsqdfs ihnedfpalp gssykdptss nddsksnlnt sgkttsstdg
      301 pkfpgdksst tqnnnqqkkg iqvlpdgrvt nipqgmvtdq fgmiglltfi raaetdpgmv
      361 hlalgsdltt lglnlnspen lypkfaspwa sspcrpqdid fhvpseyltn ihirdklaai
      421 klgrygedll fylyymnggd vlqllaavel fnrdwryhke ervwitrapg meptmktnty
      481 ergtyyffdc lnwrkvakef hleydkleer phlpstfnyn paqqaf
//
LOCUS       NP_001394264             284 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 33 [Homo sapiens].
ACCESSION   NP_001394264
VERSION     NP_001394264.1
DBSOURCE    REFSEQ: accession NM_001407335.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1770248.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..284
                     /product="tropomyosin alpha-1 chain isoform 33"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=32676
     Region          48..282
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..284
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407335.1:84..938"
                     /note="isoform 33 is encoded by transcript variant 34"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle ediaakekll rvsederdrv
       61 leelhkaeds llaaeeaaak aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegqv rqleeqlrim dqtlkalmaa edkysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledel yaqklkykai seeldhalnd mtsm
//
LOCUS       NP_001425417            1486 aa            linear   PRI 21-NOV-2025
DEFINITION  AT-rich interactive domain-containing protein 1B isoform 10 [Homo
            sapiens].
ACCESSION   NP_001425417
VERSION     NP_001425417.1
DBSOURCE    REFSEQ: accession NM_001438488.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1486)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1486)
  AUTHORS   Bosch,E., Guse,E., Kirchner,P., Winterpacht,A., Walther,M.,
            Alders,M., Kerkhof,J., Ekici,A.B., Sticht,H., Sadikovic,B., Reis,A.
            and Vasileiou,G.
  TITLE     The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation
  JOURNAL   Hum Genet 143 (8), 965-978 (2024)
   PUBMED   39028335
  REMARK    GeneRIF: The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation.
REFERENCE   3  (residues 1 to 1486)
  AUTHORS   Huang,X., Li,H., Yang,S., Ma,M., Lian,Y., Wu,X., Qi,X., Wang,X.,
            Rong,W. and Sheng,X.
  TITLE     De novo variation in ARID1B gene causes Coffin-Siris syndrome 1 in
            a Chinese family with excessive early-onset high myopia
  JOURNAL   BMC Med Genomics 17 (1), 142 (2024)
   PUBMED   38790056
  REMARK    GeneRIF: De novo variation in ARID1B gene causes Coffin-Siris
            syndrome 1 in a Chinese family with excessive early-onset high
            myopia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1486)
  AUTHORS   Hurlstone,A.F., Olave,I.A., Barker,N., van Noort,M. and Clevers,H.
  TITLE     Cloning and characterization of hELD/OSA1, a novel BRG1 interacting
            protein
  JOURNAL   Biochem J 364 (Pt 1), 255-264 (2002)
   PUBMED   11988099
  REMARK    GeneRIF: Cloning and characterization of hELD/OSA1, a novel BRG1
            interacting protein.
REFERENCE   5  (residues 1 to 1486)
  AUTHORS   Phelan,M.L., Sif,S., Narlikar,G.J. and Kingston,R.E.
  TITLE     Reconstitution of a core chromatin remodeling complex from SWI/SNF
            subunits
  JOURNAL   Mol Cell 3 (2), 247-253 (1999)
   PUBMED   10078207
REFERENCE   6  (residues 1 to 1486)
  AUTHORS   Imbert,G., Saudou,F., Yvert,G., Devys,D., Trottier,Y.,
            Garnier,J.M., Weber,C., Mandel,J.L., Cancel,G., Abbas,N., Durr,A.,
            Didierjean,O., Stevanin,G., Agid,Y. and Brice,A.
  TITLE     Cloning of the gene for spinocerebellar ataxia 2 reveals a locus
            with high sensitivity to expanded CAG/glutamine repeats
  JOURNAL   Nat Genet 14 (3), 285-291 (1996)
   PUBMED   8896557
REFERENCE   7  (residues 1 to 1486)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
REFERENCE   8  (residues 1 to 1486)
  AUTHORS   Vergano,S.A., van der Sluijs,P.J. and Santen,G.
  TITLE     ARID1B-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31132234
REFERENCE   9  (residues 1 to 1486)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
REFERENCE   10 (residues 1 to 1486)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049820.23 and AL591545.6.
            
            Summary: This locus encodes an AT-rich DNA interacting
            domain-containing protein. The encoded protein is a component of
            the SWI/SNF chromatin remodeling complex and may play a role in
            cell-cycle activation. The protein encoded by this locus is similar
            to AT-rich interactive domain-containing protein 1A. These two
            proteins function as alternative, mutually exclusive ARID-subunits
            of the SWI/SNF complex. The associated complexes play opposing
            roles. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.3780602.1,
                                           SRR14038196.3318370.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145893, SAMEA2156670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1486
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..1486
                     /product="AT-rich interactive domain-containing protein 1B
                     isoform 10"
                     /note="BRG1-binding protein ELD/OSA1; ELD (eyelid)/OSA
                     protein; BRG1-associated factor 250b; ARID
                     domain-containing protein 1B; AT rich interactive domain
                     1B (SWI1-like)"
                     /calculated_mol_wt=162339
     Region          <1..>236
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          304..396
                     /region_name="ARID_ARID1B"
                     /note="ARID/BRIGHT DNA binding domain of AT-rich
                     interactive domain-containing protein 1B (ARID1B) and
                     similar proteins; cd16877"
                     /db_xref="CDD:350641"
     Site            order(326..332,357,359..360,363,373,375..377,379)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350641"
     Region          417..>797
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          1177..1432
                     /region_name="BAF250_C"
                     /note="SWI/SNF-like complex subunit BAF250/Osa; pfam12031"
                     /db_xref="CDD:463439"
     CDS             1..1486
                     /gene="ARID1B"
                     /gene_synonym="6A3-5; BAF250B; BRIGHT; CSS1; DAN15;
                     ELD/OSA1; MRD12; OSA2; P250R; SMARCF2"
                     /coded_by="NM_001438488.1:390..4850"
                     /note="isoform 10 is encoded by transcript variant 11"
                     /db_xref="GeneID:57492"
                     /db_xref="HGNC:HGNC:18040"
                     /db_xref="MIM:614556"
ORIGIN      
        1 mppqppgsqs essshpalsq spmpqergfm agtqrnpqma qygpqqtgps msphpspggq
       61 mhagissfqq snssgtygpq msqygpqgny srppaysgvp sasysgpgpg mgisannqmh
      121 gqgpsqpcga vplgrmpsag mqnrpfpgnm ssmtpsspgm sqqggpgmgp pmptvnrkaq
      181 eaaaavmqaa ansaqsrqgs fpgmnqsglm assspysqpm nnssslmntq appysmapam
      241 vnssaasvgl admmspgesk lplplkadgk eegtpqpesk skkssssttt gekitkvyel
      301 gneperklwv dryltfmeer gspvsslpav gkkpldlfrl yvcvkeiggl aqvnknkkwr
      361 elatnlnvgt sssaasslkk qyiqylfafe ckiergeepp pevfstgdtk kqpklqppsp
      421 ansgslqgpq tpqstgsnsm aevpgdlkpp tpastphgqm tpmqggrsst isvhdpfsdv
      481 sdssfpkrns mtpnapyqqg msmpdvmgrm pyepnkdpfg gmrkvpgsse pfmtqgqmpn
      541 ssmqdmynqs psgamsnlgm gqrqqfpyga sydrrhepyg qqypgqgpps gqppygghqp
      601 glypqqpnyk rhmdgmygpp akrhegdmyn mqyssqqqem ynqyggsysg pdrrpiqgqy
      661 pypysrermq gpgqiqthgi ppqmmggplq ssssegpqqn mwaarndmpy pyqnrqgpgg
      721 ptqappypgm nrtddmmvpd qrinhesqwp shvsqrqpym sssasmqpit rppqpsyqtp
      781 pslpnhisra pspasfqrsl enrmspsksp flpsmkmqkv mptvptsqvt gpppqpppir
      841 reitfppgsv easqpvlkqr rkitskdivt peawrvmmsl ksgllaestw aldtinilly
      901 ddstvatfnl sqlsgflell veyfrkclid ifgilmeyev gdpsqkaldh naarkddsqs
      961 laddsgkeee daecidddee deedeeedse ktesdekssi altapdaaad pkekpkqask
     1021 fdklpikivk knnlfvvdrs dklgrvqefn sgllhwqlgg gdttehiqth feskmeippr
     1081 rrpppplssa grkkeqegkg dseeqqeksi iatiddvlsa rpgalpedan pgpqtesskf
     1141 pfgiqqaksh rniklledep rsrdetplct iahwqdslak rcicvsnivr slsfvpgnda
     1201 emskhpglvl ilgklillhh ehperkrapq tyekeededk gvacskdeww wdclevlrdn
     1261 tlvtlanisg qldlsaytes iclpildgll hwmvcpsaea qdpfptvgpn svlspqrlvl
     1321 etlcklsiqd nnvdlilatp pfsrqekfya tlvryvgdrk npvcremsma llsnlaqgda
     1381 laaraiavqk gsignlisfl edgvtmaqyq qsqhnlmhmq pppleppsvd mmcraakall
     1441 amarvdenrs efllhegrll disisavlns lvasvicdvl fqigql
//
LOCUS       NP_001425260            1117 aa            linear   PRI 21-NOV-2025
DEFINITION  centrosome and spindle pole-associated protein 1 isoform 10 [Homo
            sapiens].
ACCESSION   NP_001425260 XP_047278212
VERSION     NP_001425260.1
DBSOURCE    REFSEQ: accession NM_001438331.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1117)
  AUTHORS   van den Berg,C.M., Volkov,V.A., Schnorrenberg,S., Huang,Z.,
            Stecker,K.E., Grigoriev,I., Gilani,S., Frikstad,K.M., Patzke,S.,
            Zimmermann,T., Dogterom,M. and Akhmanova,A.
  TITLE     CSPP1 stabilizes growing microtubule ends and damaged lattices from
            the luminal side
  JOURNAL   J Cell Biol 222 (4) (2023)
   PUBMED   36752787
  REMARK    GeneRIF: CSPP1 stabilizes growing microtubule ends and damaged
            lattices from the luminal side.
REFERENCE   2  (residues 1 to 1117)
  AUTHORS   Odabasi,E., Conkar,D., Deretic,J., Batman,U., Frikstad,K.M.,
            Patzke,S. and Firat-Karalar,E.N.
  TITLE     CCDC66 regulates primary cilium length and signaling via
            interactions with transition zone and axonemal proteins
  JOURNAL   J Cell Sci 136 (3) (2023)
   PUBMED   36606424
REFERENCE   3  (residues 1 to 1117)
  AUTHORS   Zhang,L., Yang,S.T., Wang,C., Zhang,L.C., Zhang,X., Li,F.C.,
            Wang,S.Y. and Ma,K.
  TITLE     Circle RNA circCSPP1 promotes human osteosarcoma cell proliferation
            and increases glucose metabolism by suppressing miR-200c maturation
  JOURNAL   Hum Exp Toxicol 41, 9603271221097364 (2022)
   PUBMED   35713481
  REMARK    GeneRIF: Circle RNA circCSPP1 promotes human osteosarcoma cell
            proliferation and increases glucose metabolism by suppressing
            miR-200c maturation.
REFERENCE   4  (residues 1 to 1117)
  AUTHORS   Latour,B.L., Van De Weghe,J.C., Rusterholz,T.D., Letteboer,S.J.,
            Gomez,A., Shaheen,R., Gesemann,M., Karamzade,A., Asadollahi,M.,
            Barroso-Gil,M., Chitre,M., Grout,M.E., van Reeuwijk,J., van
            Beersum,S.E., Miller,C.V., Dempsey,J.C., Morsy,H., Bamshad,M.J.,
            Nickerson,D.A., Neuhauss,S.C., Boldt,K., Ueffing,M.,
            Keramatipour,M., Sayer,J.A., Alkuraya,F.S., Bachmann-Gagescu,R.,
            Roepman,R. and Doherty,D.
  CONSRTM   University of Washington Center for Mendelian Genomics; Genomics
            England Research Consortium
  TITLE     Dysfunction of the ciliary ARMC9/TOGARAM1 protein module causes
            Joubert syndrome
  JOURNAL   J Clin Invest 130 (8), 4423-4439 (2020)
   PUBMED   32453716
REFERENCE   5  (residues 1 to 1117)
  AUTHORS   Xue,Y.F., Li,M., Li,W., Lin,Q., Yu,B.X., Zhu,Q.B. and Chen,H.J.
  TITLE     Roles of circ-CSPP1 on the proliferation and metastasis of glioma
            cancer
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (10), 5519-5525 (2020)
   PUBMED   32495924
  REMARK    GeneRIF: Roles of circ-CSPP1 on the proliferation and metastasis of
            glioma cancer.
REFERENCE   6  (residues 1 to 1117)
  AUTHORS   Patzke,S., Redick,S., Warsame,A., Murga-Zamalloa,C.A., Khanna,H.,
            Doxsey,S. and Stokke,T.
  TITLE     CSPP is a ciliary protein interacting with Nephrocystin 8 and
            required for cilia formation
  JOURNAL   Mol Biol Cell 21 (15), 2555-2567 (2010)
   PUBMED   20519441
  REMARK    GeneRIF: CSPP isoforms require their common C-terminal domain to
            interact with Nephrocystin 8 (NPHP8/RPGRIP1L) and to form a ternary
            complex with NPHP8 and NPHP4.
REFERENCE   7  (residues 1 to 1117)
  AUTHORS   Asiedu,M., Wu,D., Matsumura,F. and Wei,Q.
  TITLE     Centrosome/spindle pole-associated protein regulates cytokinesis
            via promoting the recruitment of MyoGEF to the central spindle
  JOURNAL   Mol Biol Cell 20 (5), 1428-1440 (2009)
   PUBMED   19129481
  REMARK    GeneRIF: CSPP interacts with and recruits MyoGEF to the central
            spindle, where MyoGEF contributes to the spatiotemporal regulation
            of cytokinesis.
REFERENCE   8  (residues 1 to 1117)
  AUTHORS   Patzke,S., Stokke,T. and Aasheim,H.C.
  TITLE     CSPP and CSPP-L associate with centrosomes and microtubules and
            differently affect microtubule organization
  JOURNAL   J Cell Physiol 209 (1), 199-210 (2006)
   PUBMED   16826565
  REMARK    GeneRIF: Taken together, CSPP and CSPP-L interact with centrosomes
            and microtubules and can differently affect microtubule
            organization.
REFERENCE   9  (residues 1 to 1117)
  AUTHORS   Patzke,S., Hauge,H., Sioud,M., Finne,E.F., Sivertsen,E.A.,
            Delabie,J., Stokke,T. and Aasheim,H.C.
  TITLE     Identification of a novel centrosome/microtubule-associated
            coiled-coil protein involved in cell-cycle progression and spindle
            organization
  JOURNAL   Oncogene 24 (7), 1159-1173 (2005)
   PUBMED   15580290
  REMARK    GeneRIF: Novel centrosome/microtubule-associated coiled-coil
            protein (CSPP)is associated with centrosomes and microtubules and
            may play a role in the regulation of G(1)/S-phase progression and
            spindle assembly [CSPP].
REFERENCE   10 (residues 1 to 1117)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC109335.5 and AC087359.13.
            
            On Apr 17, 2025 this sequence version replaced XP_047278212.1.
            
            Summary: This gene encodes a centrosome and spindle pole associated
            protein. The encoded protein plays a role in cell-cycle progression
            and spindle organization, regulates cytokinesis, interacts with
            Nephrocystin 8 and is required for cilia formation. Mutations in
            this gene result in primary cilia abnormalities and classical
            Joubert syndrome. Alternatively spliced transcript variants
            encoding distinct isoforms have been found for this gene. [provided
            by RefSeq, Apr 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2132520.1,
                                           SRR18074967.3420601.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1117
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1-q13.2"
     Protein         1..1117
                     /product="centrosome and spindle pole-associated protein 1
                     isoform 10"
                     /calculated_mol_wt=130227
     CDS             1..1117
                     /gene="CSPP1"
                     /gene_synonym="CSPP; CSPP-L; JBTS21"
                     /coded_by="NM_001438331.1:8..3361"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:79848"
                     /db_xref="HGNC:HGNC:26193"
                     /db_xref="MIM:611654"
ORIGIN      
        1 mlfplqvaav tssvrddple hcvsprtrar speickmadn ldefieeqka rlaedkaele
       61 sdppymemkg klsaklsens kilismaken ippnsqqtrg slgidyglsl plgedyerkk
      121 hklkeelrqd yrryltqerl klernkeynq flrgkeesse kfrqvekste pksqrnkkpi
      181 gqvkpdltsq iqtscenseg prkdvltpse ayeellnqrr leedryrqld deielrnrri
      241 ikkaneevgi snlkhqrfas kagipdrrfh rfnedrvfdr ryhrpdqdpe vseemderfr
      301 yesdfdrrls rvytndrmhr nkrgnmppme hdgdvieqsn irissaenks apdnetsksa
      361 nqdtcspfag mlfggedrel iqrrkekyrl elleqmaeqq rnkrrekdle lrvaasgaqd
      421 pekspdrlkq fsvaprhfee mipperpria fqtplpplsa psvppipsvh pvpsqnedlr
      481 sglssalgem vspriaplpp ppllpplatn yrtpyddayy fygsrntfdp slayygsgmm
      541 gvqpaayvsa pvthqlaqpv vntvgqnelk itsdqvinsg lifedkpkps kqslqsyqea
      601 lqqqireree rrkkereeke eyeakleaem rtynpwgkgg ggaplrdakg nlitdlnrmh
      661 rqnidayhnp dartyedkra vvsldpnlat snaenledaa nkssghmqtq sspfargnvf
      721 gepptelqik qqelyknflr fqieekkqre eaererlria eekeerrlae qrariqqeye
      781 eeqekkreke eeqrlkneeh irlaeerqke aerkkkeeee kynlqlqhyc erdnligeet
      841 khmrqpspiv palqnkiask lqrppsvdsi irsfihessm sraqsppvpa rknqlraeee
      901 kknvimelse mrkqlrseer rlqerllhmd sddeipirkk ernpmdifdm arhrlqapvr
      961 rqspkgldaa tfqnvhdfne lkdrdsetrv dlkfmyldpp rdhhtleiqq qallreqqkr
     1021 lnrikmqega kvdldaipsa kvreqrmprd dtsdflknsl lesdsafiga ygetypaied
     1081 dvlpppsqlp sarerrrnkw kgldimmrvh wltlmts
//
LOCUS       NP_001425594             638 aa            linear   PRI 21-NOV-2025
DEFINITION  TRPM8 channel-associated factor 2 isoform G [Homo sapiens].
ACCESSION   NP_001425594
VERSION     NP_001425594.1
DBSOURCE    REFSEQ: accession NM_001438665.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Yun,D., Liang,J., Wang,X., Fan,J., Wang,X., Li,J., Ren,X., Liu,J.,
            Ren,X., Zhang,H., Shang,G., Jin,W., Chen,L., Li,T., Zhang,C., Yu,S.
            and Yang,X.
  TITLE     TCAF2 drives glioma cellular migratory/invasion properties through
            STAT3 signaling
  JOURNAL   Mol Cell Biochem 479 (7), 1801-1815 (2024)
   PUBMED   38019450
  REMARK    GeneRIF: TCAF2 drives glioma cellular migratory/invasion properties
            through STAT3 signaling.
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Li,Y., Li,J., Chen,H., Lu,B., Lu,F., Chen,H., Liu,H. and Qian,C.
  TITLE     TCAF2 is associated with the immune microenvironment, promotes
            pathogenesis, and impairs prognosis in glioma
  JOURNAL   Gene 883, 147667 (2023)
   PUBMED   37506986
  REMARK    GeneRIF: TCAF2 is associated with the immune microenvironment,
            promotes pathogenesis, and impairs prognosis in glioma.
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Li,X., Qi,Q., Li,Y., Miao,Q., Yin,W., Pan,J., Zhao,Z., Chen,X.,
            Yang,F., Zhou,X., Huang,M., Wang,C., Deng,L., Huang,D., Qi,M.,
            Fan,S., Zhang,Y., Qiu,S., Deng,W., Liu,T., Chen,M., Ye,W. and
            Zhang,D.
  TITLE     TCAF2 in Pericytes Promotes Colorectal Cancer Liver Metastasis via
            Inhibiting Cold-Sensing TRPM8 Channel
  JOURNAL   Adv Sci (Weinh) 10 (30), e2302717 (2023)
   PUBMED   37635201
  REMARK    GeneRIF: TCAF2 in Pericytes Promotes Colorectal Cancer Liver
            Metastasis via Inhibiting Cold-Sensing TRPM8 Channel.
REFERENCE   5  (residues 1 to 638)
  AUTHORS   Hsieh,P., Dang,V., Vollger,M.R., Mao,Y., Huang,T.H., Dishuck,P.C.,
            Baker,C., Cantsilieris,S., Lewis,A.P., Munson,K.M., Sorensen,M.,
            Welch,A.E., Underwood,J.G. and Eichler,E.E.
  TITLE     Evidence for opposing selective forces operating on human-specific
            duplicated TCAF genes in Neanderthals and humans
  JOURNAL   Nat Commun 12 (1), 5118 (2021)
   PUBMED   34433829
  REMARK    GeneRIF: Evidence for opposing selective forces operating on
            human-specific duplicated TCAF genes in Neanderthals and humans.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 638)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 638)
  AUTHORS   Gkika,D., Lemonnier,L., Shapovalov,G., Gordienko,D., Poux,C.,
            Bernardini,M., Bokhobza,A., Bidaux,G., Degerny,C., Verreman,K.,
            Guarmit,B., Benahmed,M., de Launoit,Y., Bindels,R.J., Fiorio Pla,A.
            and Prevarskaya,N.
  TITLE     TRP channel-associated factors are a novel protein family that
            regulates TRPM8 trafficking and activity
  JOURNAL   J Cell Biol 208 (1), 89-107 (2015)
   PUBMED   25559186
  REMARK    GeneRIF: Report novel TRP channel-associated factors that modulate
            TRPM8 activity.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073264.5 and AC106862.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2899640.1,
                                           SRR14372079.792917.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q35"
     Protein         1..638
                     /product="TRPM8 channel-associated factor 2 isoform G"
                     /note="family with sequence similarity 139, member A;
                     protein FAM115C; family with sequence similarity 115,
                     member C; TRP channel-associated factor 2"
                     /calculated_mol_wt=70865
     Region          241..351
                     /region_name="M60-like_N"
                     /note="N-terminal domain of M60-like peptidases;
                     pfam17291"
                     /db_xref="CDD:435844"
     Region          352..608
                     /region_name="Peptidase_M60"
                     /note="Peptidase M60, enhancin and enhancin-like;
                     pfam13402"
                     /db_xref="CDD:433178"
     CDS             1..638
                     /gene="TCAF2"
                     /gene_synonym="FAM115C; FAM139A; GATD9; GATD9B"
                     /coded_by="NM_001438665.1:526..2442"
                     /note="isoform G is encoded by transcript variant 12"
                     /db_xref="GeneID:285966"
                     /db_xref="HGNC:HGNC:26878"
                     /db_xref="MIM:616252"
ORIGIN      
        1 mgpfllnavr wlargqtgkv gvntnlkdlc pllsehglqc slephlnsdl cvycckaysd
       61 keakqlqefv aeggglligg qawwwasqnp ghcplagfpg niilncfgls ilpqtlkagc
      121 fpvptpemrs yhfrkalsqf qailnhengn leksclaklr vdgaaflqip aegvpayisl
      181 hrllrkmlrg sglpavsren pvasdsyeaa vlslatglah sgtdcsqlaq glgtwtcsss
      241 lypskhpitv einginpgnn dcwvstglyl legqnaevsl seaaasaglr vqigchtddl
      301 tkarklsrap vvthqcwmdr tersvsclwg gllyvivpkg sqlgpvpvti rgavpapyyk
      361 lgktsleewk rqmqenlapw gelatdniil tvpttnlqal kdpepvlrlw demmqavarl
      421 aaepfpfrrp erivadvqis agwmhsgypi mchlesvkei inemdmrsrg vwgpihelgh
      481 nqqrhgwefp phtteatcnl wsvyvhetvl gipraqahea lsppererri kahlgkgapl
      541 cdwnvwtale tylqlqeafg wepftqlfae yqtlshlpkd ntgrmnlwvk kfsekvkknl
      601 vpffeawgwp iqkevadsla slpewqenpm qvylrark
//
LOCUS       NP_001425613             956 aa            linear   PRI 21-NOV-2025
DEFINITION  splicing regulator ARVCF isoform 3 [Homo sapiens].
ACCESSION   NP_001425613 XP_047297324 XP_054181602
VERSION     NP_001425613.1
DBSOURCE    REFSEQ: accession NM_001438684.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 956)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 956)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 956)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 956)
  AUTHORS   Suzuki,N., Idogawa,M., Tange,S., Ohashi,T., Sasaki,Y., Nakase,H.
            and Tokino,T.
  TITLE     p53-induced ARVCF modulates the splicing landscape and supports the
            tumor suppressive function of p53
  JOURNAL   Oncogene 39 (10), 2202-2211 (2020)
   PUBMED   31827232
  REMARK    GeneRIF: p53-induced ARVCF modulates the splicing landscape and
            supports the tumor suppressive function of p53.
REFERENCE   5  (residues 1 to 956)
  AUTHORS   Zhang,D., Tang,N., Liu,Y. and Wang,E.H.
  TITLE     ARVCF expression is significantly correlated with the malignant
            phenotype of non-small cell lung cancer
  JOURNAL   Mol Carcinog 54 Suppl 1, E185-E191 (2015)
   PUBMED   25683624
  REMARK    GeneRIF: observed ARVCF-dependent changes in small GTPase (mainly
            RhoA) activity in lung cancer cells. We confirmed that ARVCF plays
            an important role in the malignant phenotype
REFERENCE   6  (residues 1 to 956)
  AUTHORS   Mariner,D.J., Wang,J. and Reynolds,A.B.
  TITLE     ARVCF localizes to the nucleus and adherens junction and is
            mutually exclusive with p120(ctn) in E-cadherin complexes
  JOURNAL   J Cell Sci 113 (Pt 8), 1481-1490 (2000)
   PUBMED   10725230
REFERENCE   7  (residues 1 to 956)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   8  (residues 1 to 956)
  AUTHORS   Sirotkin,H., Morrow,B., Saint-Jore,B., Puech,A., Das Gupta,R.,
            Patanjali,S.R., Skoultchi,A., Weissman,S.M. and Kucherlapati,R.
  TITLE     Identification, characterization, and precise mapping of a human
            gene encoding a novel membrane-spanning protein from the 22q11
            region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 42 (2), 245-251 (1997)
   PUBMED   9192844
REFERENCE   9  (residues 1 to 956)
  AUTHORS   Sirotkin,H., O'Donnell,H., DasGupta,R., Halford,S., St Jore,B.,
            Puech,A., Parimoo,S., Morrow,B., Skoultchi,A., Weissman,S.M.,
            Scambler,P. and Kucherlapati,R.
  TITLE     Identification of a new human catenin gene family member (ARVCF)
            from the region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 41 (1), 75-83 (1997)
   PUBMED   9126485
REFERENCE   10 (residues 1 to 956)
  AUTHORS   Lindsay,E.A., Goldberg,R., Jurecic,V., Morrow,B., Carlson,C.,
            Kucherlapati,R.S., Shprintzen,R.J. and Baldini,A.
  TITLE     Velo-cardio-facial syndrome: frequency and extent of 22q11
            deletions
  JOURNAL   Am J Med Genet 57 (3), 514-522 (1995)
   PUBMED   7677167
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005663.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047297324.1, XP_054181602.1.
            
            Summary: Armadillo Repeat gene deleted in Velo-Cardio-Facial
            syndrome (ARVCF) is a member of the catenin family. This family
            plays an important role in the formation of adherens junction
            complexes, which are thought to facilitate communication between
            the inside and outside environments of a cell. The ARVCF gene was
            isolated in the search for the genetic defect responsible for the
            autosomal dominant Velo-Cardio-Facial syndrome (VCFS), a relatively
            common human disorder with phenotypic features including cleft
            palate, conotruncal heart defects and facial dysmorphology. The
            ARVCF gene encodes a protein containing two motifs, a coiled coil
            domain in the N-terminus and a 10 armadillo repeat sequence in the
            midregion. Since these sequences can facilitate protein-protein
            interactions ARVCF is thought to function in a protein complex. In
            addition, ARVCF contains a predicted nuclear-targeting sequence
            suggesting that it may have a function as a nuclear protein.
            [provided by RefSeq, Jun 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1069160.1,
                                           SRR14038191.4558362.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..956
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..956
                     /product="splicing regulator ARVCF isoform 3"
                     /note="armadillo repeat protein deleted in
                     velo-cardio-facial syndrome; armadillo repeat gene deleted
                     in velocardiofacial syndrome; splicing regulator ARVCF"
                     /calculated_mol_wt=103654
     Region          95..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            170
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P98203; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          186..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          266..290
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          348..387
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          360..385
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(376,380,384,418,422,426,461,466,470)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          389..428
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          390..429
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          393..429
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          432..473
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          433..467
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          436..471
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          468..508
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          478..529
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          526..565
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          575..622
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          590..614
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          607..623
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          640..680
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          650..686
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          650..686
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          693..732
                     /region_name="ARM 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          696..731
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          696..730
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          733..775
                     /region_name="ARM 9"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          737..782
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          770..956
                     /region_name="Required for interaction with RNA-binding
                     proteins DDX5, HNRNPH2 and SRSF1 and with mRNAs.
                     /evidence=ECO:0000269|PubMed:24644279"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          788..820
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          848..956
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            858
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            865
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            866
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            909
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     CDS             1..956
                     /gene="ARVCF"
                     /coded_by="NM_001438684.1:308..3178"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:421"
                     /db_xref="HGNC:HGNC:728"
                     /db_xref="MIM:602269"
ORIGIN      
        1 medcnvhsaa silasvkeqe arferltral eqerrhvalq leraqqpgmv sggmgsgqpl
       61 pmawqqlvlq eqspgsqasl atmpeapdvl eetvtveedp gtptshvsiv tsedgttrrt
      121 etkvtktvkt vttrtvrqvp vgpdglplld ggpplgpfad galdrhfllr gggpvatlsr
      181 aylssgggfp egpeprdsps ygslsrglgm rppragplgp gpgdgcftlp ghreafpvgp
      241 epgppggrsl perfqaepyg leddtrslaa ddeggpelep dygtatrrrp ecgrglhtra
      301 yedtaddgge laderpafpm vtaplaqper gsmgsldrlv rrspsvdsar keprwrdpel
      361 pevlamlrhp vdpvkanaaa ylqhlcfene gvkrrvrqlr glpllvalld hpraevrrra
      421 cgalrnlsyg rdtdnkaair dcggvpalvr llraardnev relvtgtlwn lssyeplkmv
      481 iidhglqtlt hevivphsgw erepnedskp rdaewttvfk ntsgclrnvs sdgaearrrl
      541 receglvdal lhalqsavgr kdtdnksven cvcimrnlsy hvhkevpgad ryqeaepgpl
      601 gsavgsqrrr rddascfggk kakgkkdgem drnfdtldlp krteaakgfe llyqpevvrl
      661 ylslltesrn fntleaaaga lqnlsagnwm watyiratvr kerglpvlve llqsetdkvv
      721 ravaialrnl sldrrnkdli gsyamaelvr nvrnaqappr pgacleedtv vavlntihei
      781 vsdsldnars llqargvpal valvassqsv reakaashvl qtvwsykelr gtlqkdgwtk
      841 arfqsaaata kgpkgalspg gfddstlplv dkslegektg srdvipmdal gpdgystvdr
      901 rerrprgass ageasekepl kldpsrkapp pgpsrpavrl vdavgdakpq pvdswv
//
LOCUS       NP_001397686             666 aa            linear   PRI 21-NOV-2025
DEFINITION  SH3 domain-containing kinase-binding protein 1 isoform l [Homo
            sapiens].
ACCESSION   NP_001397686 XP_011543802
VERSION     NP_001397686.1
DBSOURCE    REFSEQ: accession NM_001410757.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 666)
  AUTHORS   Ahmed,S.F., Buetow,L., Gabrielsen,M., Lilla,S., Sibbet,G.J.,
            Sumpton,D., Zanivan,S., Hedley,A., Clark,W. and Huang,D.T.
  TITLE     E3 ligase-inactivation rewires CBL interactome to elicit
            oncogenesis by hijacking RTK-CBL-CIN85 axis
  JOURNAL   Oncogene 40 (12), 2149-2164 (2021)
   PUBMED   33627783
  REMARK    GeneRIF: E3 ligase-inactivation rewires CBL interactome to elicit
            oncogenesis by hijacking RTK-CBL-CIN85 axis.
REFERENCE   5  (residues 1 to 666)
  AUTHORS   Soubeyran,P., Kowanetz,K., Szymkiewicz,I., Langdon,W.Y. and
            Dikic,I.
  TITLE     Cbl-CIN85-endophilin complex mediates ligand-induced downregulation
            of EGF receptors
  JOURNAL   Nature 416 (6877), 183-187 (2002)
   PUBMED   11894095
  REMARK    GeneRIF: Cbl-CIN85-endophilin complex mediates ligand-induced
            downregulation of EGF receptors
            Erratum:[Nature 2002 May 2;417(6884):102]
REFERENCE   6  (residues 1 to 666)
  AUTHORS   Narita,T., Amano,F., Yoshizaki,K., Nishimoto,N., Nishimura,T.,
            Tajima,T., Namiki,H. and Taniyama,T.
  TITLE     Assignment of SH3KBP1 to human chromosome band Xp22.1-->p21.3 by in
            situ hybridization
  JOURNAL   Cytogenet Cell Genet 93 (1-2), 133-134 (2001)
   PUBMED   11474197
REFERENCE   7  (residues 1 to 666)
  AUTHORS   Watanabe,S., Take,H., Takeda,K., Yu,Z.X., Iwata,N. and Kajigaya,S.
  TITLE     Characterization of the CIN85 adaptor protein and identification of
            components involved in CIN85 complexes
  JOURNAL   Biochem Biophys Res Commun 278 (1), 167-174 (2000)
   PUBMED   11071869
REFERENCE   8  (residues 1 to 666)
  AUTHORS   Gout,I., Middleton,G., Adu,J., Ninkina,N.N., Drobot,L.B.,
            Filonenko,V., Matsuka,G., Davies,A.M., Waterfield,M. and
            Buchman,V.L.
  TITLE     Negative regulation of PI 3-kinase by Ruk, a novel adaptor protein
  JOURNAL   EMBO J 19 (15), 4015-4025 (2000)
   PUBMED   10921882
REFERENCE   9  (residues 1 to 666)
  AUTHORS   Take,H., Watanabe,S., Takeda,K., Yu,Z.X., Iwata,N. and Kajigaya,S.
  TITLE     Cloning and characterization of a novel adaptor protein, CIN85,
            that interacts with c-Cbl
  JOURNAL   Biochem Biophys Res Commun 268 (2), 321-328 (2000)
   PUBMED   10679202
REFERENCE   10 (residues 1 to 666)
  AUTHORS   Salvatore,P., Hanash,C.R., Kido,Y., Imai,Y. and Accili,D.
  TITLE     Identification of sirm, a novel insulin-regulated SH3 binding
            protein that associates with Grb-2 and FYN
  JOURNAL   J Biol Chem 273 (12), 6989-6997 (1998)
   PUBMED   9507006
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL772197.12, AL732325.6,
            AL732327.6 and AL732423.12.
            
            On Aug 15, 2022 this sequence version replaced XP_011543802.1.
            
            Summary: This gene encodes an adapter protein that contains one or
            more N-terminal Src homology domains, a proline rich region and a
            C-terminal coiled-coil domain. The encoded protein facilitates
            protein-protein interactions and has been implicated in numerous
            cellular processes including apoptosis, cytoskeletal rearrangement,
            cell adhesion and in the regulation of clathrin-dependent
            endocytosis. Alternate splicing results in multiple transcript
            variants encoding distinct isoforms. [provided by RefSeq, Jul
            2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.19109.1,
                                           SRR1803613.197096.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.12"
     Protein         1..666
                     /product="SH3 domain-containing kinase-binding protein 1
                     isoform l"
                     /note="Src family kinase-binding protein 1; src-related
                     kinase binding protein-1; CD2-binding protein 3;
                     migration-inducing gene 18; c-Cbl-interacting protein;
                     cbl-interacting protein of 85 kDa; SH3-domain kinase
                     binding protein 1; human Src family kinase-binding protein
                     1"
                     /calculated_mol_wt=73164
     Region          3..55
                     /region_name="SH3_CIN85_1"
                     /note="First Src Homology 3 domain (SH3A) of
                     Cbl-interacting protein of 85 kDa; cd12052"
                     /db_xref="CDD:212985"
     Site            order(7..13,17,21..22,34..36,46..47,49,51..52)
                     /site_type="other"
                     /note="putative ubiquitin interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:212985"
     Site            order(8,10,13..14,16..17,34,36,47,51..52,54)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212985"
     Region          102..154
                     /region_name="SH3_CIN85_2"
                     /note="Second Src Homology 3 domain (SH3B) of
                     Cbl-interacting protein of 85 kDa; cd12055"
                     /db_xref="CDD:212988"
     Site            order(106..112,116,120..121,133..135,145..146,148,
                     150..151)
                     /site_type="other"
                     /note="putative ubiquitin interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:212988"
     Site            order(107,109,112,116,133..135,146,148,150..151)
                     /site_type="other"
                     /note="putative peptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:212988"
     Region          315..370
                     /region_name="SH3_CIN85_3"
                     /note="Third Src Homology 3 domain (SH3C) of
                     Cbl-interacting protein of 85 kDa; cd12057"
                     /db_xref="CDD:212990"
     Site            order(319..326,328..329,333..334,347..350,360..361,363,
                     365..366,368)
                     /site_type="other"
                     /note="ubiquitin interaction site [polypeptide binding]"
                     /db_xref="CDD:212990"
     Site            order(320,322,325,329,348..350,361,363,365..366)
                     /site_type="other"
                     /note="putative peptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:212990"
     CDS             1..666
                     /gene="SH3KBP1"
                     /gene_synonym="AGMX2; CD2BP3; CIN85; GIG10; HSB-1; HSB1;
                     IMD61; MIG18"
                     /coded_by="NM_001410757.1:291..2291"
                     /note="isoform l is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS94574.1"
                     /db_xref="GeneID:30011"
                     /db_xref="HGNC:HGNC:13867"
                     /db_xref="MIM:300374"
ORIGIN      
        1 mveaivefdy qaqhddelti svgeiitnir kedggwwegq ingrrglfpd nfvreikkem
       61 kkdpltnkap ekplhevpsg nsllssetil rtnkrgerrr rrcqvafsyl pqnddelelk
      121 vgdiievvge veegwwegvl ngktgmfpsn fikelsgesd elgisqdeql sksrpeglpp
      181 asllpfpahg akgkttfegt ilyraapgkt eghrryyslr ettgsesdgg dssstksega
      241 ngtvataaiq pkkvkgvgfg difkdkpikl rprsievend flpvektigk klpattatpd
      301 ssktemdsrt kskdyckvif pyeaqnddel tikegdivtl inkdcidvgw wegelngrrg
      361 vfpdnfvkll ppdfekegnr pkkppppsap vikqgagtte rkheikkipp erpemlpnrt
      421 eekerperep kldlqkpsvp aippkkprpp ktnslsrpga lpprrperpv gplthtrgds
      481 pkidlagssl sgildkdlsd rsndidlegf dsvvsstekl shpttsrpka tgrrppsqsl
      541 tsvsdnkasl ppkpgtmaag gggpaplssa apsplssslg taghransps lfgtegkpkm
      601 epaassqaav eelrtqvrel rsiietmkdq qkreikqlls eldeekkirl rlqmevndik
      661 kalqsk
//
LOCUS       NP_001423775             597 aa            linear   PRI 21-NOV-2025
DEFINITION  semaphorin-4F isoform 4 precursor [Homo sapiens].
ACCESSION   NP_001423775 XP_047298883 XP_054196167
VERSION     NP_001423775.1
DBSOURCE    REFSEQ: accession NM_001436846.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 597)
  AUTHORS   Fan,Q., Barathi,V.A., Cheng,C.Y., Zhou,X., Meguro,A., Nakata,I.,
            Khor,C.C., Goh,L.K., Li,Y.J., Lim,W., Ho,C.E., Hawthorne,F.,
            Zheng,Y., Chua,D., Inoko,H., Yamashiro,K., Ohno-Matsui,K.,
            Matsuo,K., Matsuda,F., Vithana,E., Seielstad,M., Mizuki,N.,
            Beuerman,R.W., Tai,E.S., Yoshimura,N., Aung,T., Young,T.L.,
            Wong,T.Y., Teo,Y.Y. and Saw,S.M.
  TITLE     Genetic variants on chromosome 1q41 influence ocular axial length
            and high myopia
  JOURNAL   PLoS Genet 8 (6), e1002753 (2012)
   PUBMED   22685421
REFERENCE   5  (residues 1 to 597)
  AUTHORS   Parrinello,S., Noon,L.A., Harrisingh,M.C., Wingfield Digby,P.,
            Rosenberg,L.H., Cremona,C.A., Echave,P., Flanagan,A.M., Parada,L.F.
            and Lloyd,A.C.
  TITLE     NF1 loss disrupts Schwann cell-axonal interactions: a novel role
            for semaphorin 4F
  JOURNAL   Genes Dev 22 (23), 3335-3348 (2008)
   PUBMED   19056885
  REMARK    GeneRIF: Sema4F levels were strongly reduced in a panel of human
            neurofibromas, confirming the relevance of these findings to the
            human disease.
REFERENCE   6  (residues 1 to 597)
  AUTHORS   Ayala,G.E., Dai,H., Powell,M., Li,R., Ding,Y., Wheeler,T.M.,
            Shine,D., Kadmon,D., Thompson,T., Miles,B.J., Ittmann,M.M. and
            Rowley,D.
  TITLE     Cancer-related axonogenesis and neurogenesis in prostate cancer
  JOURNAL   Clin Cancer Res 14 (23), 7593-7603 (2008)
   PUBMED   19047084
REFERENCE   7  (residues 1 to 597)
  AUTHORS   Park,Y.D., Park,D., Bhak,J. and Yang,J.M.
  TITLE     Proteomic approaches to the analysis of atopic dermatitis and new
            insights from interactomics
  JOURNAL   Proteomics Clin Appl 2 (3), 290-300 (2008)
   PUBMED   21136834
REFERENCE   8  (residues 1 to 597)
  AUTHORS   Francks,C., Fisher,S.E., Olson,R.K., Pennington,B.F., Smith,S.D.,
            DeFries,J.C. and Monaco,A.P.
  TITLE     Fine mapping of the chromosome 2p12-16 dyslexia susceptibility
            locus: quantitative association analysis and positional candidate
            genes SEMA4F and OTX1
  JOURNAL   Psychiatr Genet 12 (1), 35-41 (2002)
   PUBMED   11901358
  REMARK    GeneRIF: Fine mapping of the chromosome 2p12-16 dyslexia
            susceptibility candidate gene
REFERENCE   9  (residues 1 to 597)
  AUTHORS   Schultze,W., Eulenburg,V., Lessmann,V., Herrmann,L., Dittmar,T.,
            Gundelfinger,E.D., Heumann,R. and Erdmann,K.S.
  TITLE     Semaphorin4F interacts with the synapse-associated protein
            SAP90/PSD-95
  JOURNAL   J Neurochem 78 (3), 482-489 (2001)
   PUBMED   11483650
REFERENCE   10 (residues 1 to 597)
  AUTHORS   Encinas,J.A., Kikuchi,K., Chedotal,A., de Castro,F., Goodman,C.S.
            and Kimura,T.
  TITLE     Cloning, expression, and genetic mapping of Sema W, a member of the
            semaphorin family
  JOURNAL   Proc Natl Acad Sci U S A 96 (5), 2491-2496 (1999)
   PUBMED   10051670
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007387.4.
            
            On or before Mar 24, 2025 this sequence version replaced
            XP_047298883.1, XP_054196167.1.
            
            Summary: This gene encodes a transmembrane class IV semaphorin
            family protein, which plays a role in neural development. This gene
            may be involved in neurogenesis in prostate cancer, the development
            of neurofibromas, and breast cancer tumorigenesis. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Nov 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.1826987.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMEA2159912
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..597
                     /product="semaphorin-4F isoform 4 precursor"
                     /note="semaphorin M; semaphorin-4F; semaphorin-W; sema
                     domain immunoglobulin domain transmembrane domain (TM) and
                     short cytoplasmic domain (semaphorin) 4F; sema domain,
                     immunoglobulin domain (Ig), transmembrane domain (TM) and
                     short cytoplasmic domain, (semaphorin) 4F"
                     /calculated_mol_wt=62505
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3311
     Region          52..511
                     /region_name="Sema_4F"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 4F (Sema4F); cd11261"
                     /db_xref="CDD:200522"
     Site            64
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95754.2)"
     Site            order(114..116,172,193,195..196,198,214,217,219,224,256,
                     280..284,286,365..366,402,406,409)
                     /site_type="other"
                     /note="plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200522"
     Site            133
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95754.2)"
     Site            order(257..258,260,263..265,299,302..304,306,308,332..334,
                     338..339,415,430)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200522"
     Site            509
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95754.2)"
     Region          512..563
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     CDS             1..597
                     /gene="SEMA4F"
                     /gene_synonym="M-SEMA; m-Sema-M; PRO2353; S4F; SEMAM;
                     SEMAW"
                     /coded_by="NM_001436846.1:131..1924"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:10505"
                     /db_xref="HGNC:HGNC:10734"
                     /db_xref="MIM:603706"
ORIGIN      
        1 mpasaarprp gpgqptaspf pllllavlsg pvsgrvprsv prtslpisea dscltrfavp
       61 htynysvllv dpashtlyvg ardtifalsl pfsgerprri dwmvpeahrq ncrkkgkked
      121 echnfvqila ianashlltc gtfafdpkcg vidvsrfqqv erlesgrgkc pfepaqrsaa
      181 vmaggvlyaa tvknylgtep iitravgrae dwirtdtlps wlnapafvaa valspaewgd
      241 edgddeiyff ftetsrafds yerikvprva rvcagdlggr ktlqqrwttf lkadllcpgp
      301 ehgrassvlq dvavlrpelg agtpifygif ssqwegatis avcafrpqdi rtvlngpfre
      361 lkhdcnrglp vvdndvpqpr pgecitnnmk lrhfgsslsl pdrvltfird hplmdrpvfp
      421 adghpllvtt dtaylrvvah rvtslsgkey dvlylgtedg hlhravriga qlsvledlal
      481 fpepqpvenm klyhswllvg srtevtqvnt tncgrlqscs ecilaqdpvc awsfrldecv
      541 ahagehrglv qdiesadvss lcpkepggkr pwkkgnmnlq dssqqnklst cylykgl
//
LOCUS       NP_001427533             304 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform s [Homo sapiens].
ACCESSION   NP_001427533 XP_047283758 XP_054226337
VERSION     NP_001427533.1
DBSOURCE    REFSEQ: accession NM_001440604.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 304)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2.
            
            On or before May 22, 2025 this sequence version replaced
            XP_047283758.1, XP_054226337.1.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.3020730.1,
                                           SRR14038197.512945.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..304
                     /product="polycomb protein EED isoform s"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=33876
     Region          1..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q921E6; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            66
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918; N6-methyllysine,
                     alternate. /evidence=ECO:0000269|PubMed:20974918;
                     propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Region          <81..264
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          96..140
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          148..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          193..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            197
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918; N6-methyllysine,
                     alternate. /evidence=ECO:0000269|PubMed:20974918;
                     propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Region          240..269
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            268
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918; N6-methyllysine,
                     alternate. /evidence=ECO:0000269|PubMed:20974918;
                     propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Site            284
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918; N6-methyllysine,
                     alternate. /evidence=ECO:0000269|PubMed:20974918;
                     propagated from UniProtKB/Swiss-Prot (O75530.2)"
     CDS             1..304
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001440604.1:478..1392"
                     /note="isoform s is encoded by transcript variant 19"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdendd avsiesgtnt erpdtptntp
       61 napgrkswgk gkwkskkcky sfkcvnslke dhnqplfgvq fnwhskegdp lvfatvgsnr
      121 vtlyechsqg eirllqsyvd adadenfytc awtydsntsh pllavagsrg iiriinpitm
      181 qcikhyvghg nainelkfhp rdpnlllsvs kdhalrlwni qtdtlvaifg gveghrdevl
      241 sadydllgek imscgmdhsl klwrinskrm mnaikesydy npnktnslvk mplcagnlar
      301 wkmi
//
LOCUS       NP_001389623            1300 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform c [Homo sapiens].
ACCESSION   NP_001389623 XP_016876771
VERSION     NP_001389623.1
DBSOURCE    REFSEQ: accession NM_001402694.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1300)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1300)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1300)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1300)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1300)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1300)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1300)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1300)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1300)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1300)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            On Apr 22, 2022 this sequence version replaced XP_016876771.1.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2451948.1,
                                           SRR18074968.1940530.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1300
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1300
                     /product="kinectin isoform c"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=149480
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          316..>532
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          448..1240
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1300
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402694.1:303..4205"
                     /note="isoform c is encoded by transcript variant 19"
                     /db_xref="CCDS:CCDS41958.1"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqdlkqeika
      841 lkeeignvql ekaqqlsits kvqelqnllk gkeeqmntmk avleekekdl antgkwlqdl
      901 qeeneslkah vqevaqhnlk eassasqfee leivlkeken elkrleamlk eresdlsskt
      961 qllqdvqden klfksqieql kqqnyqqass fppheellkv iserekeisg lwneldslkd
     1021 avehqrkknn erqqqveave leakevlkkl fpkvsvpsnl sygewlhgfe kkakecmagt
     1081 sgseevkvle hklkeademh tllqleceky ksvlaetegi lqklqrsveq eenkwkvkvd
     1141 eshktikqmq ssftsseqel erlrsenkdi enlrrerehl emelekaeme rstyvtevre
     1201 lkaqlnetlt klrteqnerq kvagdlhkaq qsleliqski vkaagdttvi ensdvspete
     1261 sseketmsvs lnqtvtqlqq llqavnqqlt kekehyqvle
//
LOCUS       NP_001397653             543 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 47 [Homo sapiens].
ACCESSION   NP_001397653 XP_047272173
VERSION     NP_001397653.1
DBSOURCE    REFSEQ: accession NM_001410724.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Muckenfuss,L.M., Migenda Herranz,A.C., Boneberg,F.M., Clerici,M.
            and Jinek,M.
  TITLE     Fip1 is a multivalent interaction scaffold for processing factors
            in human mRNA 3' end biogenesis
  JOURNAL   Elife 11, e80332 (2022)
   PUBMED   36073787
  REMARK    GeneRIF: Fip1 is a multivalent interaction scaffold for processing
            factors in human mRNA 3' end biogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Tennenbaum,J., Groh,M., Venditti,L., Campos-Gazeau,F., Chalayer,E.,
            De Broucker,T., Hamidou,M., Hunault,M., Lyoubi,A., Meunier,R.,
            Muron,T., Sene,D., Slama,B., Guidoux,C., Lefevre,G., Kahn,J.E.,
            Denier,C. and Rohmer,J.
  TITLE     FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a Treatable
            Cause of Watershed Infarction
  JOURNAL   Stroke 52 (10), e605-e609 (2021)
   PUBMED   34304603
  REMARK    GeneRIF: FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a
            Treatable Cause of Watershed Infarction.
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 543)
  AUTHORS   Helbig,G., Lewandowski,K., Swiderska,A., Rodzaj,M., Seferynska,I.
            and Gajkowska-Kulik,J.
  TITLE     Exquisite response to imatinib mesylate in FIP1L1-PDGFRA-mutated
            hypereosinophilic syndrome: a 12-year experience of the Polish
            Hypereosinophilic Syndrome Study Group
  JOURNAL   Pol Arch Intern Med 130 (3), 255-257 (2020)
   PUBMED   32125294
  REMARK    GeneRIF: Exquisite response to imatinib mesylate in
            FIP1L1-PDGFRA-mutated hypereosinophilic syndrome: a 12-year
            experience of the Polish Hypereosinophilic Syndrome Study Group.
REFERENCE   6  (residues 1 to 543)
  AUTHORS   Cools,J., Quentmeier,H., Huntly,B.J., Marynen,P., Griffin,J.D.,
            Drexler,H.G. and Gilliland,D.G.
  TITLE     The EOL-1 cell line as an in vitro model for the study of
            FIP1L1-PDGFRA-positive chronic eosinophilic leukemia
  JOURNAL   Blood 103 (7), 2802-2805 (2004)
   PUBMED   14630792
  REMARK    GeneRIF: results indicate that the fusion of FIP1L1 to PDGFRA
            occurs rarely in leukemia cell lines
REFERENCE   7  (residues 1 to 543)
  AUTHORS   Kaufmann,I., Martin,G., Friedlein,A., Langen,H. and Keller,W.
  TITLE     Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements
            and stimulates poly(A) polymerase
  JOURNAL   EMBO J 23 (3), 616-626 (2004)
   PUBMED   14749727
REFERENCE   8  (residues 1 to 543)
  AUTHORS   Pardanani,A., Ketterling,R.P., Brockman,S.R., Flynn,H.C.,
            Paternoster,S.F., Shearer,B.M., Reeder,T.L., Li,C.Y., Cross,N.C.,
            Cools,J., Gilliland,D.G., Dewald,G.W. and Tefferi,A.
  TITLE     CHIC2 deletion, a surrogate for FIP1L1-PDGFRA fusion, occurs in
            systemic mastocytosis associated with eosinophilia and predicts
            response to imatinib mesylate therapy
  JOURNAL   Blood 102 (9), 3093-3096 (2003)
   PUBMED   12842979
  REMARK    GeneRIF: observations suggest that the FIP1L1-PDGFRA rearrangement
            occurs in an early hematopoietic progenitor and suggests that the
            molecular pathogenesis for a subset of SMCD patients is similar to
            that of HES
REFERENCE   9  (residues 1 to 543)
  AUTHORS   Griffin,J.H., Leung,J., Bruner,R.J., Caligiuri,M.A. and
            Briesewitz,R.
  TITLE     Discovery of a fusion kinase in EOL-1 cells and idiopathic
            hypereosinophilic syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (13), 7830-7835 (2003)
   PUBMED   12808148
REFERENCE   10 (residues 1 to 543)
  AUTHORS   Cools,J., DeAngelo,D.J., Gotlib,J., Stover,E.H., Legare,R.D.,
            Cortes,J., Kutok,J., Clark,J., Galinsky,I., Griffin,J.D.,
            Cross,N.C., Tefferi,A., Malone,J., Alam,R., Schrier,S.L.,
            Schmid,J., Rose,M., Vandenberghe,P., Verhoef,G., Boogaerts,M.,
            Wlodarska,I., Kantarjian,H., Marynen,P., Coutre,S.E., Stone,R. and
            Gilliland,D.G.
  TITLE     A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes
            as a therapeutic target of imatinib in idiopathic hypereosinophilic
            syndrome
  JOURNAL   N Engl J Med 348 (13), 1201-1214 (2003)
   PUBMED   12660384
  REMARK    GeneRIF: The hypereosinophilic syndrome may result from a novel
            fusion tyrosine kinase - FIP1L1-PDGFRalpha - that is a consequence
            of an interstitial chromosomal deletion.
            GeneRIF: Describes the fusion gene Fip1-like-1-PDGFRalpha in
            patients with idiopathic hypereosinophilic syndrome, mostly
            responsive to imatinib therapy.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098821.3 and AC058822.6.
            
            On Aug 15, 2022 this sequence version replaced XP_047272173.1.
            
            Summary: This gene encodes a subunit of the CPSF (cleavage and
            polyadenylation specificity factor) complex that polyadenylates the
            3' end of mRNA precursors. This gene, the homolog of yeast Fip1
            (factor interacting with PAP), binds to U-rich sequences of
            pre-mRNA and stimulates poly(A) polymerase activity. Its N-terminus
            contains a PAP-binding site and its C-terminus an RNA-binding
            domain. An interstitial chromosomal deletion on 4q12 creates an
            in-frame fusion of human genes FIP1L1 and PDGFRA (platelet-derived
            growth factor receptor, alpha). The FIP1L1-PDGFRA fusion gene
            encodes a constitutively activated tyrosine kinase that joins the
            first 233 amino acids of FIP1L1 to the last 523 amino acids of
            PDGFRA. This gene fusion and chromosomal deletion is the cause of
            some forms of idiopathic hypereosinophilic syndrome (HES). This
            syndrome, recently reclassified as chronic eosinophilic leukemia
            (CEL), is responsive to treatment with tyrosine kinase inhibitors.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.321113.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..543
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     47"
                     /note="rearranged in hypereosinophilia; pre-mRNA
                     3'-end-processing factor FIP1; FIP1-like 1 protein; factor
                     interacting with PAP; FIP1 like 1; FIP1L1 cleavage and
                     polyadenylation specific factor subunit"
                     /calculated_mol_wt=58858
     Region          139..181
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     CDS             1..543
                     /gene="FIP1L1"
                     /gene_synonym="FIP1; hFip1; Rhe"
                     /coded_by="NM_001410724.1:199..1830"
                     /note="isoform 47 is encoded by transcript variant 50"
                     /db_xref="CCDS:CCDS93514.1"
                     /db_xref="GeneID:81608"
                     /db_xref="HGNC:HGNC:19124"
                     /db_xref="MIM:607686"
ORIGIN      
        1 msageverlv selsggtggd eeeewlygde neverpeeen asanppsgie detaengvpk
       61 pkvtetedds dsdsdddedd vhvtigdikt gapqygsygt apvnlniktg grvygttgtk
      121 vkgvdldapg singvpllev dldsfedkpw rkpgadlsdy fnygfnedtw kaycekqkri
      181 rmglevipvt sttnkitaed ctmevtpgae iqdgrfnlfk vqqgrtgnse ketalpstka
      241 eftsppslfk tglppsrnst ssqsqtstas rkanssvgkw qdrygraesp dlrrlpgaid
      301 vigqtitisr vegrrranen sniqvlsers atevdnnfsk pppffppgap pthlppppfl
      361 pppptvstap plipppgipi tvpppgfppp pgapppslip tiesghssgy dsrsarafpy
      421 gnamkndtdt gnmqkevmsv teqvekkknd iekddtgrkr kpdisllevi vdvamkvkke
      481 ivtgdtntkn lkeakkekkr avslplnrra pklhlqnrhg fgllcilvpe vdtinlvifl
      541 dnv
//
LOCUS       NP_001393527            1163 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 3 [Homo sapiens].
ACCESSION   NP_001393527 XP_047279786
VERSION     NP_001393527.1
DBSOURCE    REFSEQ: accession NM_001406598.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1163)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1163)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1163)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1163)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1163)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1163)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1163)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1163)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1163)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1163)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            On May 18, 2022 this sequence version replaced XP_047279786.1.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.374103.1,
                                           SRR14038195.803500.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1163
                     /product="hamartin isoform 3"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=129565
     Region          7..718
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          402..786
                     /region_name="Mediates interaction with WDR45B.
                     /evidence=ECO:0000269|PubMed:28561066"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Region          438..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <707..>959
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1005..1084
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1099
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1130..1163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1163
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406598.1:214..3705"
                     /note="isoform 3 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS87703.1"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt ggkgtplgtp atspppaplc hsddyvhisl pqatvtpprk
      421 eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed siekdkeeaa
      481 isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv npeplhssld
      541 klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp trvgfgsgqp
      601 ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr liqqgadahs
      661 kelnklplps ksvdwthfgg sppsdeirtl rdqllllhnq llyerfkrqq halrnrrllr
      721 kvikaaalee hnaamkdqlk lqekdiqmwk vslqkeqary nqlqeqrdtm vtklhsqirq
      781 lqhdreefyn qsqelqtkle dcrnmiaelr ielkkannkv chtelllsqv sqklsnsesv
      841 qqqmeflnrq llvlgevnel yleqlqnkhs dttkevemmk aayrkelekn rshvlqqtqr
      901 ldtsqkrile leshlakkdh llleqkkyle dvklqargql qaaesryeaq kritqvfele
      961 ildlygrlek dgllkkleee kaeaaeaaee rldccndgcs dsmvghneea sghngetktp
     1021 rpssargssg srggggssss sselstpekp phqragpfss rwettmgeas asipttvgsl
     1081 pssksflgmk arelfrnkse sqcdedgmts slseslktel gkdlgveaki plnldgphps
     1141 pptpdsvgql himdynethh ehs
//
LOCUS       NP_001399057             858 aa            linear   PRI 21-NOV-2025
DEFINITION  protein PTHB1 isoform 16 [Homo sapiens].
ACCESSION   NP_001399057
VERSION     NP_001399057.1
DBSOURCE    REFSEQ: accession NM_001412128.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 858)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 858)
  AUTHORS   Zhang,Y., Xu,M., Zhang,M., Yang,G. and Li,X.
  TITLE     A Novel BBS9 Mutation Identified via Whole-Exome Sequencing in a
            Chinese Family with Bardet-Biedl Syndrome
  JOURNAL   Biomed Res Int 2021, 4514967 (2021)
   PUBMED   34692830
  REMARK    GeneRIF: A Novel BBS9 Mutation Identified via Whole-Exome
            Sequencing in a Chinese Family with Bardet-Biedl Syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 858)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 858)
  AUTHORS   Jeziorny,K., Antosik,K., Jakiel,P., Mlynarski,W., Borowiec,M. and
            Zmyslowska,A.
  TITLE     Next-Generation Sequencing in the Diagnosis of Patients with
            Bardet-Biedl Syndrome-New Variants and Relationship with
            Hyperglycemia and Insulin Resistance
  JOURNAL   Genes (Basel) 11 (11), 1283 (2020)
   PUBMED   33138063
  REMARK    GeneRIF: Next-Generation Sequencing in the Diagnosis of Patients
            with Bardet-Biedl Syndrome-New Variants and Relationship with
            Hyperglycemia and Insulin Resistance.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 858)
  AUTHORS   Nachury,M.V., Loktev,A.V., Zhang,Q., Westlake,C.J., Peranen,J.,
            Merdes,A., Slusarski,D.C., Scheller,R.H., Bazan,J.F.,
            Sheffield,V.C. and Jackson,P.K.
  TITLE     A core complex of BBS proteins cooperates with the GTPase Rab8 to
            promote ciliary membrane biogenesis
  JOURNAL   Cell 129 (6), 1201-1213 (2007)
   PUBMED   17574030
REFERENCE   6  (residues 1 to 858)
  AUTHORS   Nishimura,D.Y., Swiderski,R.E., Searby,C.C., Berg,E.M.,
            Ferguson,A.L., Hennekam,R., Merin,S., Weleber,R.G., Biesecker,L.G.,
            Stone,E.M. and Sheffield,V.C.
  TITLE     Comparative genomics and gene expression analysis identifies BBS9,
            a new Bardet-Biedl syndrome gene
  JOURNAL   Am J Hum Genet 77 (6), 1021-1033 (2005)
   PUBMED   16380913
  REMARK    GeneRIF: Comparative genomics and gene expression analysis
            identifies PHTB1 protein as BBS9, a new Bardet-Biedl syndrome gene.
REFERENCE   7  (residues 1 to 858)
  AUTHORS   Vernon,E.G., Malik,K., Reynolds,P., Powlesland,R., Dallosso,A.R.,
            Jackson,S., Henthorn,K., Green,E.D. and Brown,K.W.
  TITLE     The parathyroid hormone-responsive B1 gene is interrupted by a
            t(1;7)(q42;p15) breakpoint associated with Wilms' tumour
  JOURNAL   Oncogene 22 (9), 1371-1380 (2003)
   PUBMED   12618763
  REMARK    GeneRIF: gene is interrupted by a t(1;7)(q42;p15) breakpoint
            associated with Wilms' tumour; new alternately spliced isoforms
            were found in a wide range of adult and foetal tissues
REFERENCE   8  (residues 1 to 858)
  AUTHORS   Adams,A.E., Rosenblatt,M. and Suva,L.J.
  TITLE     Identification of a novel parathyroid hormone-responsive gene in
            human osteoblastic cells
  JOURNAL   Bone 24 (4), 305-313 (1999)
   PUBMED   10221542
REFERENCE   9  (residues 1 to 858)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 858)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CP068271.2.
            
            Summary: This gene is downregulated by parathyroid hormone in
            osteoblastic cells, and therefore is thought to be involved in
            parathyroid hormone action in bones. The exact function of this
            gene has not yet been determined. Alternatively spliced transcript
            variants encoding different isoforms have been identified.
            [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (21) uses the same exon
            combination as variant 19 but represents the allele encoded by the
            T2T-CHM13v2.0 genome assembly. The encoded isoform (16) has a
            frameshifted C-terminus compared to isoform 14.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2142363,
                              SAMEA2144333 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..858
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.3"
     Protein         1..858
                     /product="protein PTHB1 isoform 16"
                     /note="protein PTHB1; PTH-responsive osteosarcoma B1
                     protein; bardet-Biedl syndrome 9 protein; parathyroid
                     hormone-responsive B1 gene protein"
                     /calculated_mol_wt=96102
     Region          1..418
                     /region_name="PHTB1_N"
                     /note="PTHB1 N-terminus; pfam14727"
                     /db_xref="CDD:464284"
     Region          1..407
                     /region_name="Seven-bladed beta-propeller.
                     /evidence=ECO:0000269|PubMed:26085087"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SYG4.1)"
     Site            141
                     /site_type="other"
                     /note="Critical for protein stability.
                     /evidence=ECO:0000269|PubMed:26085087; propagated from
                     UniProtKB/Swiss-Prot (Q3SYG4.1)"
     Region          441..819
                     /region_name="PHTB1_C"
                     /note="PTHB1 C-terminus; pfam14728"
                     /db_xref="CDD:464285"
     Region          685..765
                     /region_name="Interaction with LZTL1.
                     /evidence=ECO:0000269|PubMed:22072986"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SYG4.1)"
     CDS             1..858
                     /gene="BBS9"
                     /gene_synonym="B1; C18; D1; PTHB1"
                     /coded_by="NM_001412128.2:490..3066"
                     /note="isoform 16 is encoded by transcript variant 21"
                     /db_xref="GeneID:27241"
                     /db_xref="HGNC:HGNC:30000"
                     /db_xref="MIM:607968"
ORIGIN      
        1 mslfkardww stilgdkeef dqgclclanv dnsgngqdki ivgsfmgylr ifsphpaktg
       61 dgaqaedlll evdlrdpvlq vevgkfvsgt emlhlavlhs rklcvysvsg tlgnvehgnq
      121 cqmklmyehn lqrtacnmty gsfggvkgrd liciqsmdgm lmvfeqesya fgrflpgfll
      181 pgplayssrt dsfltvsscq qvesykyqvl afatdadkrq eteqqklgsg krlvvdwtln
      241 igeqaldici vsfnqsassv fvlgernffc lkdngqirfm kkldwspscf lpycsvsegt
      301 intlignhnn mlhiyqdvtl kwatqlphip vavrvgclhd lkgvivtlsd dghlqcsylg
      361 tdpslfqapn vqsrelnyde ldvemkelqk iikdvnksqg vwpmteredd lnvsvvvspn
      421 fdsvsqatdv evgtdlvpsv tvkvtlqnrv ilqkaklsvy vqppleltcd qftfefmtpd
      481 ltrtvsfsvy lkrsytpsel egnavvsysr ptdrnpdgip rviqckfrlp lkliclpgqp
      541 sktashkiti dtnkspvsll slfpgfasqs dddqvnvmgf hflggaritv lasktsqryr
      601 iqseqfedlw litnelilrl qeyfekqgvk dfacsfsgsi plqeyfelid hhfelringe
      661 kleellsera vqfraiqrrl larfkdktpa plqhldtlld gtykqviala daveenqgnl
      721 fqsftrlksa thlvillial wqklsadqva ileaaflplq edtqelgwee tvdaaishll
      781 ktclsksske qalnlnsqln ipkdtsqlkk hitllcdrls kggrlclstd aaapqtmvmp
      841 dprtgqriea wtlriphs
//
LOCUS       NP_001400010             333 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001400010
VERSION     NP_001400010.1
DBSOURCE    REFSEQ: accession NM_001413081.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2487069.1,
                                           SRR18074968.4180732.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..333
                     /product="mitochondrial fission regulator 1 isoform 1
                     precursor"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=31469
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=5550
     Region          22..251
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     mat_peptide     49..333
                     /product="Mitochondrial fission regulator 1.
                     /id=PRO_0000096622"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=31469
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15390.2)"
     Region          177..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          179..304
                     /region_name="Necessary and sufficient to promote
                     mitochondrial fission. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          288..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     CDS             1..333
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001413081.1:446..1447"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 16"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsvlwsrkpy gssrsivrki gtnlsliqcp rvqfqinsha
       61 tewspshpge davasfadvg wvakeegecs arlrtevrsr pplqddllff ekapsrqisl
      121 pdlsqeepql ktpalaneea lqkicalene laalraqiak ivtqqeqqnl tagdldsttf
      181 gtipphpppp ppplpppalg lhqstsavdl ikerrekran agktlvknnp kkpempnmle
      241 ilkemnsvkl rsvkrseqdv kpkpvdatdp aaliaealkk kfayryrsds qdevekgipk
      301 seseatserv lfgphmlkpt gkmkalienv sds
//
LOCUS       NP_001426220             335 aa            linear   PRI 21-NOV-2025
DEFINITION  protein ALEX isoform h [Homo sapiens].
ACCESSION   NP_001426220 XP_024307643
VERSION     NP_001426220.1
DBSOURCE    REFSEQ: accession NM_001439291.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Lin,J., Nie,Q., Cheng,J., Zhong,Y.N., Zhang,T., Zhang,X., Ge,X.,
            Ding,Y., Niu,C., Gao,Y., Wang,K., Gao,M., Wang,X., Chen,W., Yun,C.,
            Ye,C., Xu,J., Shaoyong,W., Zhang,L., Shang,P., Luo,X., Zhang,Z.,
            Zheng,X., Sha,X., Zhang,J., Nie,S., Zhang,X., Ren,F., Liu,H.,
            Dong,E., Yu,X., Ji,L., Pang,Y., Sun,J.P. and Jiang,C.
  TITLE     A microbial amino-acid-conjugated bile acid, tryptophan-cholic
            acid, improves glucose homeostasis via the orphan receptor MRGPRE
  JOURNAL   Cell 188 (17), 4530-4548 (2025)
   PUBMED   40446798
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Crane,J.L., Shamblott,M.J., Axelman,J., Hsu,S., Levine,M.A. and
            Germain-Lee,E.L.
  TITLE     Imprinting status of Galpha(s), NESP55, and XLalphas in cell
            cultures derived from human embryonic germ cells: GNAS imprinting
            in human embryonic germ cells
  JOURNAL   Clin Transl Sci 2 (5), 355-360 (2009)
   PUBMED   20443919
  REMARK    GeneRIF: analysis of the imprinting Status of Galpha(s), NESP55,
            and XLalphas in cell cultures derived from human embryonic germ
            cells
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Bastepe,M.
  TITLE     The GNAS Locus: Quintessential Complex Gene Encoding Gsalpha,
            XLalphas, and other Imprinted Transcripts
  JOURNAL   Curr Genomics 8 (6), 398-414 (2007)
   PUBMED   19412439
  REMARK    GeneRIF: GNAS locus has a highly complex imprinted expression
            pattern, giving rise to transcripts (including non-coding) that are
            maternally, paternally, or biallelically expressed.
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Jakobsen,A.M., Ahlman,H., Kolby,L., Abrahamsson,J.,
            Fischer-Colbrie,R. and Nilsson,O.
  TITLE     NESP55, a novel chromogranin-like peptide, is expressed in
            endocrine tumours of the pancreas and adrenal medulla but not in
            ileal carcinoids
  JOURNAL   Br J Cancer 88 (11), 1746-1754 (2003)
   PUBMED   12771991
  REMARK    GeneRIF: Neuroendocrine secretory protein 55 is found in a subset
            of neuroendocrine tumours showing differentiation towards adrenal
            chromaffin cells and pancreatic islets cells and not in ileal
            carcinoids
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Freson,K., Jaeken,J., Van Helvoirt,M., de Zegher,F.,
            Wittevrongel,C., Thys,C., Hoylaerts,M.F., Vermylen,J. and Van
            Geet,C.
  TITLE     Functional polymorphisms in the paternally expressed XLalphas and
            its cofactor ALEX decrease their mutual interaction and enhance
            receptor-mediated cAMP formation
  JOURNAL   Hum Mol Genet 12 (10), 1121-1130 (2003)
   PUBMED   12719376
REFERENCE   6  (residues 1 to 335)
  AUTHORS   Weiss,U., Ischia,R., Eder,S., Lovisetti-Scamihorn,P., Bauer,R. and
            Fischer-Colbrie,R.
  TITLE     Neuroendocrine secretory protein 55 (NESP55): alternative splicing
            onto transcripts of the GNAS gene and posttranslational processing
            of a maternally expressed protein
  JOURNAL   Neuroendocrinology 71 (3), 177-186 (2000)
   PUBMED   10729789
REFERENCE   7  (residues 1 to 335)
  AUTHORS   Ischia,R., Lovisetti-Scamihorn,P., Hogue-Angeletti,R.,
            Wolkersdorfer,M., Winkler,H. and Fischer-Colbrie,R.
  TITLE     Molecular cloning and characterization of NESP55, a novel
            chromogranin-like precursor of a peptide with 5-HT1B receptor
            antagonist activity
  JOURNAL   J Biol Chem 272 (17), 11657-11662 (1997)
   PUBMED   9111083
REFERENCE   8  (residues 1 to 335)
  AUTHORS   Haldeman-Englert,C.R., Hurst,A.C.E. and Levine,M.A.
  TITLE     Disorders of GNAS Inactivation
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29072892
REFERENCE   9  (residues 1 to 335)
  AUTHORS   Szymczuk,V., Florenzano,P., de Castro,L.F., Collins,M.T. and
            Boyce,A.M.
  TITLE     Fibrous Dysplasia / McCune-Albright Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719192
REFERENCE   10 (residues 1 to 335)
  AUTHORS   Weinstein,L.S., Gejman,P.V., de Mazancourt,P., American,N. and
            Spiegel,A.M.
  TITLE     A heterozygous 4-bp deletion mutation in the Gs alpha gene (GNAS1)
            in a patient with Albright hereditary osteodystrophy
  JOURNAL   Genomics 13 (4), 1319-1321 (1992)
   PUBMED   1505964
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121917.20 and AL109840.24.
            
            On Apr 29, 2025 this sequence version replaced XP_024307643.1.
            
            Summary: This locus has a highly complex imprinted expression
            pattern. It gives rise to maternally, paternally, and biallelically
            expressed transcripts that are derived from four alternative
            promoters and 5' exons. Some transcripts contain a differentially
            methylated region (DMR) at their 5' exons, and this DMR is commonly
            found in imprinted genes and correlates with transcript expression.
            An antisense transcript is produced from an overlapping locus on
            the opposite strand. One of the transcripts produced from this
            locus, and the antisense transcript, are paternally expressed
            noncoding RNAs, and may regulate imprinting in this region. In
            addition, one of the transcripts contains a second overlapping ORF,
            which encodes a structurally unrelated protein - Alex. Alternative
            splicing of downstream exons is also observed, which results in
            different forms of the stimulatory G-protein alpha subunit, a key
            element of the classical signal transduction pathway linking
            receptor-ligand interactions with the activation of adenylyl
            cyclase and a variety of cellular reponses. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            Mutations in this gene result in pseudohypoparathyroidism type 1a,
            pseudohypoparathyroidism type 1b, Albright hereditary
            osteodystrophy, pseudopseudohypoparathyroidism, McCune-Albright
            syndrome, progressive osseus heteroplasia, polyostotic fibrous
            dysplasia of bone, and some pituitary tumors. [provided by RefSeq,
            Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1770708.1,
                                           SRR14038195.1269954.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 19412439
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.32"
     Protein         1..335
                     /product="protein ALEX isoform h"
                     /note="secretogranin VI; G protein subunit alpha S;
                     guanine nucleotide binding protein (G protein), alpha
                     stimulating activity polypeptide 1; guanine nucleotide
                     regulatory protein; adenylate cyclase-stimulating G alpha
                     protein; protein ALEX; extra large alphas protein;
                     alternative gene product encoded by XL-exon"
                     /calculated_mol_wt=38867
     Region          1..329
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Site            order(34,38,42,45,48..49,69,72,113,142,167,175,179)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Site            140..148
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            145
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(146,148,150,161,163,167..169,171,174..175,177..180)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(148,173,176..177,180)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            164..167
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            165..181
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Site            233..236
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(298..309,311..314)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Site            306..308
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..335
                     /gene="GNAS"
                     /gene_synonym="AHO; AIMAH1; C20orf45; GNAS1; GPSA; GSA;
                     GSP; NESP; PITA3; POH; SCG6; SgVI"
                     /coded_by="NM_001439291.1:192..1199"
                     /note="isoform h is encoded by transcript variant 21"
                     /db_xref="GeneID:2778"
                     /db_xref="HGNC:HGNC:4392"
                     /db_xref="MIM:139320"
ORIGIN      
        1 mrilhvngfn geggeedpqa arsnsdgeka tkvqdiknnl keaietivaa msnlvppvel
       61 anpenqfrvd yilsvmnvpd fdfppefyeh akalwedegv racyersney qlidcaqyfl
      121 dkidvikqad yvpsdqdllr crvltsgife tkfqvdkvnf hmfdvggqrd errkwiqcfn
      181 dvtaiifvva sssynmvire dnqtnrlqea lnlfksiwnn rwlrtisvil flnkqdllae
      241 kvlagkskie dyfpefaryt tpedatpepg edprvtraky firdeflris tasgdgrhyc
      301 yphftcavdt enirrvfndc rdiiqrmhlr qyell
//
LOCUS       NP_001400612             350 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 16 precursor [Homo sapiens].
ACCESSION   NP_001400612
VERSION     NP_001400612.1
DBSOURCE    REFSEQ: accession NM_001413683.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 350)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 350)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 350)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3195265.1,
                                           SRR14038196.956790.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..350
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 16 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=35404
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..342
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            277..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            313..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     CDS             1..350
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413683.1:169..1221"
                     /note="isoform 16 precursor is encoded by transcript
                     variant 19"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvsyih gssqaqfvae shiilvlnaa itmgmvllne
      301 aatskgdvgk rriiclvglg lvvfffsfll sifrskyhgy pysvfkdhad
//
LOCUS       NP_001424672             629 aa            linear   PRI 21-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 13 [Homo sapiens].
ACCESSION   NP_001424672
VERSION     NP_001424672.1
DBSOURCE    REFSEQ: accession NM_001437743.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 629)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 629)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 629)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 629)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 629)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 629)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 629)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008641.7.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.2453590.1,
                                           ERR4352443.346899.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..629
                     /product="TNFAIP3-interacting protein 1 isoform 13"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=70938
     Region          14..>149
                     /region_name="Speriolin_N"
                     /note="Speriolin N terminus; pfam15058"
                     /db_xref="CDD:434426"
     Region          61..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          94..412
                     /region_name="Interaction with Nef"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Region          <214..>251
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          252..283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          <298..>538
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          351..367
                     /region_name="Interaction with Shigella flexneri ipah9.8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          431..588
                     /region_name="Required for inhibitory activity of
                     TNF-induced NF-kappa-B activation. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          452..510
                     /region_name="Ubiquitin-binding domain (UBD)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Region          524..530
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            552
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17632516; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            571
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9WUU8; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            599
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            627
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     CDS             1..629
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001437743.1:192..2081"
                     /note="isoform 13 is encoded by transcript variant 22"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 megrgpyriy dpggsvpsge asaaferlvk ensrlkekmq gikmlgelle esqmeatrlr
       61 qkaeelvkdn ellpppspsl gsfdplaelt gkdsnvtasp tapacpsdkp apvqkppssg
      121 tssefevvtp eeqnspesss hanamalgpl predgnlmlh lqrlettlsv caeepdhgql
      181 fthlgrmale fnrlaskvhk neqrtsilqt lceqlrkene alkakldkgl eqrdqaaerl
      241 reenlelkkl lmsngnkega sgrpgspkme gtgkkavagq qqasvtagkv pevvalgaae
      301 kkvkmleqqr sellevnkqw dqhfrsmkqq yeqkitelrq kladlqkqvt dleaereqkq
      361 rdfdrkllla kskiemeetd keqltaeake lrqkvkylqd qlspltrqre yqekeiqrln
      421 kaleealsiq tppsspptaf gspegagall rkqelvtqne llkqqvkife edfqrersdr
      481 ermneekeel kkqveklqaq vtlsnaqlka fkdeekarea lrqqkrkaka sgeryhveph
      541 pehlcgaypy ayppmpamvp hhgfedwsqi ryppppmame hppplpnsrl fhlpeytwrl
      601 pcggvrnpnq ssqvmdppta rptepvskk
//
LOCUS       NP_001397703             513 aa            linear   PRI 21-NOV-2025
DEFINITION  actin-related protein 8 isoform 2 [Homo sapiens].
ACCESSION   NP_001397703 XP_011532551
VERSION     NP_001397703.1
DBSOURCE    REFSEQ: accession NM_001410774.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Zhang,S., Zhou,B., Wang,L., Li,P., Bennett,B.D., Snyder,R.,
            Garantziotis,S., Fargo,D.C., Cox,A.D., Chen,L. and Hu,G.
  TITLE     INO80 is required for oncogenic transcription and tumor growth in
            non-small cell lung cancer
  JOURNAL   Oncogene 36 (10), 1430-1439 (2017)
   PUBMED   27641337
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Cao,L., Ding,J., Dong,L., Zhao,J., Su,J., Wang,L., Sui,Y., Zhao,T.,
            Wang,F., Jin,J. and Cai,Y.
  TITLE     Negative Regulation of p21Waf1/Cip1 by Human INO80 Chromatin
            Remodeling Complex Is Implicated in Cell Cycle Phase G2/M Arrest
            and Abnormal Chromosome Stability
  JOURNAL   PLoS One 10 (9), e0137411 (2015)
   PUBMED   26340092
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 513)
  AUTHORS   Yao,T., Song,L., Jin,J., Cai,Y., Takahashi,H., Swanson,S.K.,
            Washburn,M.P., Florens,L., Conaway,R.C., Cohen,R.E. and
            Conaway,J.W.
  TITLE     Distinct modes of regulation of the Uch37 deubiquitinating enzyme
            in the proteasome and in the Ino80 chromatin-remodeling complex
  JOURNAL   Mol Cell 31 (6), 909-917 (2008)
   PUBMED   18922472
REFERENCE   7  (residues 1 to 513)
  AUTHORS   Aoyama,N., Oka,A., Kitayama,K., Kurumizaka,H. and Harata,M.
  TITLE     The actin-related protein hArp8 accumulates on the mitotic
            chromosomes and functions in chromosome alignment
  JOURNAL   Exp Cell Res 314 (4), 859-868 (2008)
   PUBMED   18163988
  REMARK    GeneRIF: Expression of truncated hArp8 proteins and depletion of
            endogenous hArp8 by RNA interference caused misalignment of mitotic
            chromosomes, suggesting that chromosome-associated hArp8 has a role
            in chromosome behavior.
REFERENCE   8  (residues 1 to 513)
  AUTHORS   Wu,S., Shi,Y., Mulligan,P., Gay,F., Landry,J., Liu,H., Lu,J.,
            Qi,H.H., Wang,W., Nickoloff,J.A., Wu,C. and Shi,Y.
  TITLE     A YY1-INO80 complex regulates genomic stability through homologous
            recombination-based repair
  JOURNAL   Nat Struct Mol Biol 14 (12), 1165-1172 (2007)
   PUBMED   18026119
REFERENCE   9  (residues 1 to 513)
  AUTHORS   Jin,J., Cai,Y., Yao,T., Gottschalk,A.J., Florens,L., Swanson,S.K.,
            Gutierrez,J.L., Coleman,M.K., Workman,J.L., Mushegian,A.,
            Washburn,M.P., Conaway,R.C. and Conaway,J.W.
  TITLE     A mammalian chromatin remodeling complex with similarities to the
            yeast INO80 complex
  JOURNAL   J Biol Chem 280 (50), 41207-41212 (2005)
   PUBMED   16230350
REFERENCE   10 (residues 1 to 513)
  AUTHORS   Hassel,S., Eichner,A., Yakymovych,M., Hellman,U., Knaus,P. and
            Souchelnytskyi,S.
  TITLE     Proteins associated with type II bone morphogenetic protein
            receptor (BMPR-II) and identified by two-dimensional gel
            electrophoresis and mass spectrometry
  JOURNAL   Proteomics 4 (5), 1346-1358 (2004)
   PUBMED   15188402
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012467.9.
            
            On Aug 15, 2022 this sequence version replaced XP_011532551.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14243140.4961166.1,
                                           SRR14038194.1901467.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.1"
     Protein         1..513
                     /product="actin-related protein 8 isoform 2"
                     /note="INO80 complex subunit N; ARP8 actin related protein
                     8 homolog"
                     /calculated_mol_wt=57914
     Region          1..508
                     /region_name="ASKHA_NBD_Arp8-like"
                     /note="nucleotide-binding domain (NBD) of the
                     actin-related protein 8 (Arp8)-like subfamily; cd10206"
                     /db_xref="CDD:466812"
     CDS             1..513
                     /gene="ACTR8"
                     /gene_synonym="ARP8; hArp8; INO80N"
                     /coded_by="NM_001410774.1:385..1926"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS93290.1"
                     /db_xref="GeneID:93973"
                     /db_xref="HGNC:HGNC:14672"
                     /db_xref="MIM:619716"
ORIGIN      
        1 mvdqaiwskk msngtrripv speqarsynk qmrpaildhc sgnkwtntsh hpeylvgeea
       61 lyvnpldcyn ihwpirrgql nihpgpggsl tavladievi wshaiqkyle iplkdlkyyr
      121 cillipdiyn kqhvkelvnm ilmkmgfsgi vvhqesvcat ygsglsstci vdvgdqktsv
      181 ccvedgvshr ntrlclaygg sdvsrcfywl mqragfpyre cqltnkmdcl llqhlketfc
      241 hldqdisglq dhefqirhpd spallyqfrl gdeklqapma lfypatfgiv gqkmttlqhr
      301 sqgdpedphd ehyllatqsk qeqsakatad rksaskpigf egdlrgqssd lperlhsqev
      361 dlgsaqgdgl magndseeal talmsrktai slfegkalgl dkailhsidc cssddtkkkm
      421 yssilvvggg lmfhkaqefl qhrilnkmpp sfrriienvd vitrpkdmdp rliawkggav
      481 lacldttqel wiyqrewqrf gvrmlreraa fvw
//
LOCUS       NP_001394763            1119 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 19 [Homo
            sapiens].
ACCESSION   NP_001394763
VERSION     NP_001394763.1
DBSOURCE    REFSEQ: accession NM_001407834.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1119)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1119)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1119)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1119)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1119)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1119)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1119)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1119)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1119)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1119)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1266972.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1119
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1119
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 19"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=126612
     Region          153..182
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          188..215
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          324..593
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          720..1119
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1119
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407834.1:575..3934"
                     /note="isoform 19 is encoded by transcript variant 19"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 mgakdatpvp cgrwakilek dkrtqqmrmq rlkaklqmpf qsgefkaltr rlqveprlls
       61 kqmagcledc trqapespwe eqlarllqea pgklsldveq apsgqhsqaq lsgqqqrlla
      121 ffkcclltdq lplahhllvv hhgqrqkrkl ltldmynavm lgwarqgafk elvyvlfmvk
      181 dagltpdlls yaaalqcmgr qdqdagtier cleqmsqegl klqalftavl lseedratvl
      241 kavhkvkptf slppqlpppv ntskllrdvy akdgrvsypk lhlplktlqc lfekqlhmel
      301 asrvcvvsve kptlpskevk harktlktlr dqwekalcra lretknrler evyegrfsly
      361 pflclldere vvrmllqalp aqgesfttla relsartfsr hvvqrqrvsg qvqalqnhyr
      421 kylcllasda evpepclprq yweelgapea lreqpwplpv qmelgkllae mlvqatqmpc
      481 sldkphrssr lvpvlyhvys frnvqqigil kphpayvqll ekaaeptltf eavdvpmlcp
      541 plpwtsphsg afllsptklm rtvegatqhq elletcppta lhgaldaltq lgncawrvng
      601 rvldlvlqlf qakgcpqlgv pappseapqp peahlphsaa parkaelrre lahcqkvare
      661 mhslraealy rlslaqhlrd rvfwlphnmd frgrtypcpp hfnhlgsdva rallefaqgr
      721 plgphgldwl kihlvnltgl kkreplrkrl afaeevmddi ldsadqpltg rkwwmgaeep
      781 wqtlaccmev anavrasdpa ayvshlpvhq dgscnglqhy aalgrdsvga asvnlepsdv
      841 pqdvysgvaa qvevfrrqda qrgmrvaqvl egfitrkvvk qtvmtvvygv tryggrlqie
      901 krlrelsdfp qefvweashy lvrqvfkslq emfsgtraiq hwltesarli shmgsvvewv
      961 tplgvpviqp yrldskvkqi gggiqsityt hngdisrkpn trkqkngfpp nfihsldssh
     1021 mmltalhcyr kgltfvsvhd cywthaadvs vmnqvcreqf vrlhsepilq dlsrflvkrf
     1081 csepqkilea sqlketlqav pkpgafdleq vkrstyffs
//
LOCUS       NP_001425137            1721 aa            linear   PRI 21-NOV-2025
DEFINITION  BCL-6 corepressor isoform a [Homo sapiens].
ACCESSION   NP_001425137 XP_047298166 XP_054183296
VERSION     NP_001425137.1
DBSOURCE    REFSEQ: accession NM_001438208.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1721)
  AUTHORS   Batkova,M., Havlovicova,M., Nocar,A., Dudakova,L., Macek,M.,
            Liskova,P. and Dostalova,T.
  TITLE     Dental abnormalities observed in the oculo-facio-cardio-dental
            (OFCD) syndrome present in two Czech families bearing novel de novo
            BCOR pathogenic variants
  JOURNAL   BMC Oral Health 24 (1), 1264 (2024)
   PUBMED   39438869
  REMARK    GeneRIF: Dental abnormalities observed in the
            oculo-facio-cardio-dental (OFCD) syndrome present in two Czech
            families bearing novel de novo BCOR pathogenic variants.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1721)
  AUTHORS   Giner,F., Medina-Ceballos,E., Lopez-Reig,R., Machado,I.,
            Lopez-Guerrero,J.A., Navarro,S., Rubio-Martinez,L.A., Espino,M.,
            Mayordomo-Aranda,E. and Llombart-Bosch,A.
  TITLE     The Combined Immunohistochemical Expression of GLI1 and BCOR in
            Synovial Sarcomas for the Identification of Three Risk Groups and
            Their Prognostic Outcomes: A Study of 52 Patients
  JOURNAL   Int J Mol Sci 25 (14), 7615 (2024)
   PUBMED   39062853
  REMARK    GeneRIF: The Combined Immunohistochemical Expression of GLI1 and
            BCOR in Synovial Sarcomas for the Identification of Three Risk
            Groups and Their Prognostic Outcomes: A Study of 52 Patients.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1721)
  AUTHORS   Mavridou,E., Lema Fernandez,A.G., Nardelli,C., Pierini,V.,
            Quintini,M., Arniani,S., Di Giacomo,D., Crescenzi,B., Matteucci,C.,
            Sambani,C. and Mecucci,C.
  TITLE     A novel t(X;21)(p11.4;q22.12) translocation adds to the role of
            BCOR and RUNX1 in myelodysplastic syndromes and acute myeloid
            leukemias
  JOURNAL   Genes Chromosomes Cancer 63 (4), e23235 (2024)
   PUBMED   38656651
  REMARK    GeneRIF: A novel t(X;21)(p11.4;q22.12) translocation adds to the
            role of BCOR and RUNX1 in myelodysplastic syndromes and acute
            myeloid leukemias.
REFERENCE   4  (residues 1 to 1721)
  AUTHORS   Pierron,G., Tirode,F., Lucchesi,C., Reynaud,S., Ballet,S.,
            Cohen-Gogo,S., Perrin,V., Coindre,J.M. and Delattre,O.
  TITLE     A new subtype of bone sarcoma defined by BCOR-CCNB3 gene fusion
  JOURNAL   Nat Genet 44 (4), 461-466 (2012)
   PUBMED   22387997
  REMARK    GeneRIF: A new fusion was observed between BCOR (encoding the BCL6
            co-repressor) and CCNB3 (encoding the testis-specific cyclin B3) on
            the X chromosome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1721)
  AUTHORS   Tomsig,J.L., Snyder,S.L. and Creutz,C.E.
  TITLE     Identification of targets for calcium signaling through the copine
            family of proteins. Characterization of a coiled-coil
            copine-binding motif
  JOURNAL   J Biol Chem 278 (12), 10048-10054 (2003)
   PUBMED   12522145
REFERENCE   6  (residues 1 to 1721)
  AUTHORS   Ng,D., Hadley,D.W., Tifft,C.J. and Biesecker,L.G.
  TITLE     Genetic heterogeneity of syndromic X-linked recessive
            microphthalmia-anophthalmia: is Lenz microphthalmia a single
            disorder?
  JOURNAL   Am J Med Genet 110 (4), 308-314 (2002)
   PUBMED   12116202
REFERENCE   7  (residues 1 to 1721)
  AUTHORS   Tang,T.T., Dowbenko,D., Jackson,A., Toney,L., Lewin,D.A., Dent,A.L.
            and Lasky,L.A.
  TITLE     The forkhead transcription factor AFX activates apoptosis by
            induction of the BCL-6 transcriptional repressor
  JOURNAL   J Biol Chem 277 (16), 14255-14265 (2002)
   PUBMED   11777915
  REMARK    GeneRIF: The forkhead transcription factor AFX activates apoptosis
            by induction of the BCL-6 transcriptional repressor.
REFERENCE   8  (residues 1 to 1721)
  AUTHORS   Huynh,K.D., Fischle,W., Verdin,E. and Bardwell,V.J.
  TITLE     BCoR, a novel corepressor involved in BCL-6 repression
  JOURNAL   Genes Dev 14 (14), 1810-1823 (2000)
   PUBMED   10898795
  REMARK    GeneRIF: Function:BCoR is a transcriptional corepressor for BCL-6.
            Nomenclature:BCoR (BCL-6 corepressor)
REFERENCE   9  (residues 1 to 1721)
  AUTHORS   Ng,D.
  TITLE     Lenz Microphthalmia Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301694
REFERENCE   10 (residues 1 to 1721)
  AUTHORS   Bardakjian,T., Weiss,A. and Schneider,A.
  TITLE     Microphthalmia/Anophthalmia/Coloboma Spectrum - RETIRED CHAPTER,
            FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301552
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091806.4 and AC092198.5.
            
            On or before Apr 16, 2025 this sequence version replaced
            XP_047298166.1, XP_054183296.1.
            
            Summary: The protein encoded by this gene was identified as an
            interacting corepressor of BCL6, a POZ/zinc finger transcription
            repressor that is required for germinal center formation and may
            influence apoptosis. This protein selectively interacts with the
            POZ domain of BCL6, but not with eight other POZ proteins. Specific
            class I and II histone deacetylases (HDACs) have been shown to
            interact with this protein, which suggests a possible link between
            the two classes of HDACs. Several transcript variants encoding
            different isoforms have been found for this gene. A pseudogene of
            this gene is found on chromosome Y.[provided by RefSeq, Jun 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3899006.1,
                                           SRR18074967.849304.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1721
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.4"
     Protein         1..1721
                     /product="BCL-6 corepressor isoform a"
                     /note="BCL-6 interacting corepressor; BCL6 interacting
                     corepressor; BCL-6 coreceptor"
                     /calculated_mol_wt=188072
     Region          <257..673
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          309..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          388..438
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            392
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          498..514
                     /region_name="Interaction with BCL6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          557..641
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          737..760
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          773..794
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          815..844
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGN4; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1168..1380
                     /region_name="BCOR"
                     /note="BCL-6 co-repressor, non-ankyrin-repeat region;
                     pfam15808"
                     /db_xref="CDD:434953"
     Region          1186..1294
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CGN4; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Site            1376
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1396..1417
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          <1427..1559
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1428..1461
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1429..1460
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1430,1434..1435,1438..1440,1442..1443,1447,1450,
                     1460,1462,1464,1468..1469,1472..1474,1476..1477,1481,1484,
                     1493,1495,1497,1501..1502,1505..1507,1509..1510,1514,1517)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1462..1493
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1462..1491
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1495..1524
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1495..1524
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1600..1714
                     /region_name="Necessary and sufficient for interaction
                     with PCGF1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6W2J9.1)"
     Region          1600..1713
                     /region_name="PUFD"
                     /note="BCORL-PCGF1-binding domain; pfam16553"
                     /db_xref="CDD:465171"
     Site            order(1602..1603,1605..1609,1611..1613,1615,1617,1626,
                     1628,1670..1672,1674..1675,1677..1678,1695,1706,1708,
                     1710..1712)
                     /site_type="other"
                     /note="RAWUL domain interface [polypeptide binding]"
                     /db_xref="CDD:271224"
     CDS             1..1721
                     /gene="BCOR"
                     /gene_synonym="ANOP2; MAA2; MCOPS2"
                     /coded_by="NM_001438208.1:207..5372"
                     /note="isoform a is encoded by transcript variant 10"
                     /db_xref="GeneID:54880"
                     /db_xref="HGNC:HGNC:20893"
                     /db_xref="MIM:300485"
ORIGIN      
        1 mlsatplygn vhswmnserv rmcgasedrk ilvndgdask arlelreenp lnhnvvdast
       61 ahridglaal smdrtglire glrvpgnivy sslcglgsek greaatstlg glgfssernp
      121 emqfkpntpe tveasavsgk ppngfsaiyk tppgiqksav ataealgldr pasdkqspln
      181 ingasylrlp wvnpymegat paiypfldsp nkyslnmyka llpqqsysla qplyspvctn
      241 gerflylppp hyvgphipss laspmrlstp saspaipplv hcadkslpwk mgvspgnpvd
      301 shayphiqns kqprvpsaka vtsglpgdta lllppsprps prvhlptqpa adtysefhkh
      361 yaristspsv alskpymtvs sefpaarlsn gkypkapegg egaqpvpgha rktavqdrkd
      421 gssppllekq tvtkdvtdkp ldlsskvvdv daskadhmkk maptvlvhsr agsglvlsgs
      481 eipketlspp gngcaiyrse iistapsswv vpgpspneen ngksmslknk aldwaipqqr
      541 ssscprmggt davitnvsgs vssagrpasa spapnanadg tktsrssvet tpsviqhvgq
      601 ppatpakhss stsskgakas npepsfkane nglppssifl spneafrspp ipyprsylpy
      661 papegiavsp lslhgkgpvy phpvllpngs lfpghlapkp glpyglptgr pefvtyqdal
      721 glgmvhpmli phtpieitke ekperrsrsh eraryedptl rnrfseilet sstklhpdvp
      781 tdknlkpnpn wnqgktvvks dklvyvdllr eepdaktdtn vskpsfaaes vgqsaeppkp
      841 svepalqqhr dfialreelg risdfhetyt fkqpvftvsk dsvlagtnke nlglpvstpf
      901 lepplgsdgp avtfgktqed pkpfcvgsap psvdvtptyt kdgadeaesn dgkvlkpkps
      961 klakriansa gyvgdrfkcv ttelyadssq lsreqralqm eglqedsilc lpaayceram
     1021 mrfselemke regghpatkd semckfspad werlkgnqdk kpksvtleea iaeqneserc
     1081 eysvgnkhrd pfeapedkdl pvekyfverq pvseppadqv asdmphsptl rvdrkrkvsg
     1141 dsshtettae evpedpllka krrrvskglh pkkqrhllhl rerweqqvsa adgkpgrqsr
     1201 kevtqatqpe aipqgtnite ekpgrkraea kgnrswsees lkpsdneqgl pvfsgsppmk
     1261 slsstsaggk kqaqpscapa srppakqqki kenqktdvlc adeeedcqaa sllqkytdns
     1321 ekpsgkrlck tkhlipqesr rglpltgeyy venadgkvtv rrfrkrpeps sdydlspakq
     1381 epkpfdrlqq llpasqstql pcssspqett qsrpmppear rlivnknage tllqraarlg
     1441 yeevvlycle nkicdvnhrd nagycalhea cargwlnivr hlleygadvn csaqdgtrpl
     1501 hdavendhle ivrlllsyga dptlatysgr timkmthsel mekfltdyln dlqgrnddda
     1561 sgtwdfygss vcepddesgy dvlanppgpe dqdddddays dvfefefset pllpcyniqv
     1621 svaqgprnwl llsdvlkklk mssrifrcnf pnveivtiae aefyrqvsas llfscskdle
     1681 afnpeskell dlveftneiq tllgssvewl hpsdlasdny w
//
LOCUS       NP_001425412            2386 aa            linear   PRI 21-NOV-2025
DEFINITION  AT-rich interactive domain-containing protein 1B isoform 6 [Homo
            sapiens].
ACCESSION   NP_001425412 XP_047275089 XP_054212011
VERSION     NP_001425412.1
DBSOURCE    REFSEQ: accession NM_001438483.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2386)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2386)
  AUTHORS   Bosch,E., Guse,E., Kirchner,P., Winterpacht,A., Walther,M.,
            Alders,M., Kerkhof,J., Ekici,A.B., Sticht,H., Sadikovic,B., Reis,A.
            and Vasileiou,G.
  TITLE     The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation
  JOURNAL   Hum Genet 143 (8), 965-978 (2024)
   PUBMED   39028335
  REMARK    GeneRIF: The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation.
REFERENCE   3  (residues 1 to 2386)
  AUTHORS   Huang,X., Li,H., Yang,S., Ma,M., Lian,Y., Wu,X., Qi,X., Wang,X.,
            Rong,W. and Sheng,X.
  TITLE     De novo variation in ARID1B gene causes Coffin-Siris syndrome 1 in
            a Chinese family with excessive early-onset high myopia
  JOURNAL   BMC Med Genomics 17 (1), 142 (2024)
   PUBMED   38790056
  REMARK    GeneRIF: De novo variation in ARID1B gene causes Coffin-Siris
            syndrome 1 in a Chinese family with excessive early-onset high
            myopia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2386)
  AUTHORS   Hurlstone,A.F., Olave,I.A., Barker,N., van Noort,M. and Clevers,H.
  TITLE     Cloning and characterization of hELD/OSA1, a novel BRG1 interacting
            protein
  JOURNAL   Biochem J 364 (Pt 1), 255-264 (2002)
   PUBMED   11988099
  REMARK    GeneRIF: Cloning and characterization of hELD/OSA1, a novel BRG1
            interacting protein.
REFERENCE   5  (residues 1 to 2386)
  AUTHORS   Phelan,M.L., Sif,S., Narlikar,G.J. and Kingston,R.E.
  TITLE     Reconstitution of a core chromatin remodeling complex from SWI/SNF
            subunits
  JOURNAL   Mol Cell 3 (2), 247-253 (1999)
   PUBMED   10078207
REFERENCE   6  (residues 1 to 2386)
  AUTHORS   Imbert,G., Saudou,F., Yvert,G., Devys,D., Trottier,Y.,
            Garnier,J.M., Weber,C., Mandel,J.L., Cancel,G., Abbas,N., Durr,A.,
            Didierjean,O., Stevanin,G., Agid,Y. and Brice,A.
  TITLE     Cloning of the gene for spinocerebellar ataxia 2 reveals a locus
            with high sensitivity to expanded CAG/glutamine repeats
  JOURNAL   Nat Genet 14 (3), 285-291 (1996)
   PUBMED   8896557
REFERENCE   7  (residues 1 to 2386)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
REFERENCE   8  (residues 1 to 2386)
  AUTHORS   Vergano,S.A., van der Sluijs,P.J. and Santen,G.
  TITLE     ARID1B-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31132234
REFERENCE   9  (residues 1 to 2386)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
REFERENCE   10 (residues 1 to 2386)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355297.20, AL162578.13,
            AL049820.23 and AL591545.6.
            
            On or before Apr 21, 2025 this sequence version replaced
            XP_047275089.1, XP_054212011.1.
            
            Summary: This locus encodes an AT-rich DNA interacting
            domain-containing protein. The encoded protein is a component of
            the SWI/SNF chromatin remodeling complex and may play a role in
            cell-cycle activation. The protein encoded by this locus is similar
            to AT-rich interactive domain-containing protein 1A. These two
            proteins function as alternative, mutually exclusive ARID-subunits
            of the SWI/SNF complex. The associated complexes play opposing
            roles. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2768077.1,
                                           SRR14038192.3354473.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2386
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..2386
                     /product="AT-rich interactive domain-containing protein 1B
                     isoform 6"
                     /note="BRG1-binding protein ELD/OSA1; ELD (eyelid)/OSA
                     protein; BRG1-associated factor 250b; ARID
                     domain-containing protein 1B; AT rich interactive domain
                     1B (SWI1-like)"
                     /calculated_mol_wt=250584
     Region          774..>974
                     /region_name="Enamelin"
                     /note="pfam15362"
                     /db_xref="CDD:464672"
     Region          1204..1296
                     /region_name="ARID_ARID1B"
                     /note="ARID/BRIGHT DNA binding domain of AT-rich
                     interactive domain-containing protein 1B (ARID1B) and
                     similar proteins; cd16877"
                     /db_xref="CDD:350641"
     Site            order(1226..1232,1257,1259..1260,1263,1273,1275..1277,
                     1279)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350641"
     Region          1317..>1697
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          2077..2332
                     /region_name="BAF250_C"
                     /note="SWI/SNF-like complex subunit BAF250/Osa; pfam12031"
                     /db_xref="CDD:463439"
     CDS             1..2386
                     /gene="ARID1B"
                     /gene_synonym="6A3-5; BAF250B; BRIGHT; CSS1; DAN15;
                     ELD/OSA1; MRD12; OSA2; P250R; SMARCF2"
                     /coded_by="NM_001438483.1:304..7464"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="GeneID:57492"
                     /db_xref="HGNC:HGNC:18040"
                     /db_xref="MIM:614556"
ORIGIN      
        1 maaraaaaaa aaaararara gsgerrappg prpapgardl eagargaaaa aaapgpmlgg
       61 ggdgggglns vhhhpllprh elnmahnaga aaaagthsak sggseaalke ggsaaalsss
      121 ssssaaaaaa ssssssgpgs ametgllpnh klktvgeapa apphqqhhhh hhahhhhhha
      181 hhlhhhhalq qqlnqfqqqq qqqqqqqqqq qqqqhpisnn nslggaggga pqpgpdmeqp
      241 qhggakdsaa ggqadppgpp llskpgdedd appkmgepag gryehpglga lgtqqppvav
      301 pgggggpaav pefnnyygsa apasggpggr agpcfdqhgg qqspgmgmmh sasaaaagap
      361 gsmdplqnsh egypnsqcnh ypgysrpgag gggggggggg ggsggggggg gagaggagag
      421 avaaaaaaaa aaaggggggg yggssagygv lssprqqggg mmmgpgggga aslskaaags
      481 aaggfqrfag qnqhpsgatp tlnqlltsps pmmrsyggsy peysspsapp pppsqpqsqa
      541 aaagaaaggq qaaagmglgk dmgaqyaaas pawaaaqqrs hpamspgtpg ptmgrsqgsp
      601 mdpmvmkrpq lygmgsnphs qpqqsspypg gsygppgpqr ypigiqgrtp gamagmqypq
      661 qqmppqygqq gvsgycqqgq qpyysqqpqp phlppqaqyl psqsqqryqp qqdmsqegyg
      721 trsqpplapg kpnhedlnli qqerpsslpv evlasedaaf glkdlsgsid dlptgteatl
      781 ssavsasgst ssqgdqsnpa qspfsphasp hlssipggps pspvgspvgs nqsrsgpisp
      841 asipgsqmpp qppgsqsess shpalsqspm pqergfmagt qrnpqmaqyg pqqtgpsmsp
      901 hpspggqmha gissfqqsns sgtygpqmsq ygpqgnysrp paysgvpsas ysgpgpgmgi
      961 sannqmhgqg psqpcgavpl grmpsagmqn rpfpgnmssm tpsspgmsqq ggpgmgppmp
     1021 tvnrkaqeaa aavmqaaans aqsrqgsfpg mnqsglmass spysqpmnns sslmntqapp
     1081 ysmapamvns saasvgladm mspgesklpl plkadgkeeg tpqpeskskd syssqgisqp
     1141 ptpgnlpvps pmspssasis sfhgdesdsi sspgwpktps spkssssttt gekitkvyel
     1201 gneperklwv dryltfmeer gspvsslpav gkkpldlfrl yvcvkeiggl aqvnknkkwr
     1261 elatnlnvgt sssaasslkk qyiqylfafe ckiergeepp pevfstgdtk kqpklqppsp
     1321 ansgslqgpq tpqstgsnsm aevpgdlkpp tpastphgqm tpmqggrsst isvhdpfsdv
     1381 sdssfpkrns mtpnapyqqg msmpdvmgrm pyepnkdpfg gmrkvpgsse pfmtqgqmpn
     1441 ssmqdmynqs psgamsnlgm gqrqqfpyga sydrrhepyg qqypgqgpps gqppygghqp
     1501 glypqqpnyk rhmdgmygpp akrhegdmyn mqyssqqqem ynqyggsysg pdrrpiqgqy
     1561 pypysrermq gpgqiqthgi ppqmmggplq ssssegpqqn mwaarndmpy pyqnrqgpgg
     1621 ptqappypgm nrtddmmvpd qrinhesqwp shvsqrqpym sssasmqpit rppqpsyqtp
     1681 pslpnhisra pspasfqrsl enrmspsksp flpsmkmqkv mptvptsqvt gpppqpppir
     1741 reitfppgsv easqpvlkqr rkitskdivt peawrvmmsl ksgllaestw aldtinilly
     1801 ddstvatfnl sqlsgflell veyfrkclid ifgilmeyev gdpsqkaldh naarkddsqs
     1861 laddsgkeee daecidddee deedeeedse ktesdekssi altapdaaad pkekpkqask
     1921 fdklpikivk knnlfvvdrs dklgrvqefn sgllhwqlgg gdttehiqth feskmeippr
     1981 rrpppplssa grkkeqegkg dseeqqeksi iatiddvlsa rpgalpedan pgpqtesskf
     2041 pfgiqqaksh rniklledep rsrdetplct iahwqdslak rcicvsnivr slsfvpgnda
     2101 emskhpglvl ilgklillhh ehperkrapq tyekeededk gvacskdeww wdclevlrdn
     2161 tlvtlanisg qldlsaytes iclpildgll hwmvcpsaea qdpfptvgpn svlspqrlvl
     2221 etlcklsiqd nnvdlilatp pfsrqekfya tlvryvgdrk npvcremsma llsnlaqgda
     2281 laaraiavqk gsignlisfl edgvtmaqyq qsqhnlmhmq pppleppsvd mmcraakall
     2341 amarvdenrs efllhegrll disisavlns lvasvicdvl fqigql
//
LOCUS       NP_001389640             968 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 20 [Homo sapiens].
ACCESSION   NP_001389640
VERSION     NP_001389640.1
DBSOURCE    REFSEQ: accession NM_001402711.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 968)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 968)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 968)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 968)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 968)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 968)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 968)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 968)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 968)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 968)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2553624.1,
                                           SRR18074969.386835.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145893, SAMEA2149178
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..968
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..968
                     /product="kinectin isoform 20"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=112183
     Region          <16..>195
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          119..908
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..968
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402711.1:269..3175"
                     /note="isoform 20 is encoded by transcript variant 34"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mmtekersnv vitrmkdrig tlekehnvfq nkihvsyqet qqmqmkfqqv reqmeaeiah
       61 lkqengilrd avsnttnqle skqsaelnkl rqdyarlvne ltektgklqq eevqkknaeq
      121 aatqlkvqlq eaerrweevq syirkrtaeh eaaqqdlqsk fvakenevqs lhskltdtlv
      181 skqqleqrlm qlmeseqkrv nkeeslqmqv qdileqneal kaqiqqfhsq iaaqtsasvl
      241 aeelhkviae kdkqikqted slaserdrlt skeeelkdiq nmnfllkaev qklqalaneq
      301 aaaahelekm qqsvyvkddk irlleeqlqh eisnkmeefk ilndqnkalk sevqklqtlv
      361 seqpnkdvve qmekciqekd eklktveell etgliqvatk eeelnairte nssltkevqd
      421 lkakqndqvs faslveelkk vihekdgkik sveelleael lkvankektv qdlkqeikal
      481 keeignvqle kaqqlsitsk vqelqnllkg keeqmntmka vleekekdla ntgkwlqdlq
      541 eeneslkahv qevaqhnlke assasqfeel eivlkekene lkrleamlke resdlssktq
      601 llqdvqdenk lfksqieqlk qqnyqqassf ppheellkvi serekeisgl wneldslkda
      661 vehqrkknnd lreknweame alastekmlq dkvnktsker qqqveavele akevlkklfp
      721 kvsvpsnlsy gewlhgfekk akecmagtsg seevkvlehk lkeademhtl lqlecekyks
      781 vlaetegilq klqrsveqee nkwkvkvdes hktikqmqss ftsseqeler lrsenkdien
      841 lrrerehlem elekaemers tyvtevrelk aqlnetltkl rteqnerqkv agdlhkaqqs
      901 leliqskivk aagdttvien sdvspetess eketmsvsln qtvtqlqqll qavnqqltke
      961 kehyqvle
//
LOCUS       NP_001422927             736 aa            linear   PRI 21-NOV-2025
DEFINITION  histone deacetylase 4 isoform 7 [Homo sapiens].
ACCESSION   NP_001422927
VERSION     NP_001422927.1
DBSOURCE    REFSEQ: accession NM_001435998.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Liu,W. and Luo,G.
  TITLE     NEDD9 is transcriptionally regulated by HDAC4 and promotes breast
            cancer metastasis and macrophage M2 polarization via the
            FAK/NF-kappaB signaling pathway
  JOURNAL   Neoplasia 57, 101059 (2024)
   PUBMED   39326322
  REMARK    GeneRIF: NEDD9 is transcriptionally regulated by HDAC4 and promotes
            breast cancer metastasis and macrophage M2 polarization via the
            FAK/NF-kappaB signaling pathway.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 736)
  AUTHORS   Di Giorgio,E., Dalla,E., Tolotto,V., D'Este,F., Paluvai,H.,
            Ranzino,L. and Brancolini,C.
  TITLE     HDAC4 influences the DNA damage response and counteracts senescence
            by assembling with HDAC1/HDAC2 to control H2BK120 acetylation and
            homology-directed repair
  JOURNAL   Nucleic Acids Res 52 (14), 8218-8240 (2024)
   PUBMED   38874468
  REMARK    GeneRIF: HDAC4 influences the DNA damage response and counteracts
            senescence by assembling with HDAC1/HDAC2 to control H2BK120
            acetylation and homology-directed repair.
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Chen,Q. and Lao,J.
  TITLE     Interference with Histone Deacetylase 4 Regulates c-Jun N-terminal
            Kinase/Activating Protein-1 Signaling to Ameliorate Sepsis-induced
            Alveolar Epithelial Cell Injury
  JOURNAL   J Physiol Investig 67 (4), 174-186 (2024)
   PUBMED   39133038
  REMARK    GeneRIF: Interference with Histone Deacetylase 4 Regulates c-Jun
            N-terminal Kinase/Activating Protein-1 Signaling to Ameliorate
            Sepsis-induced Alveolar Epithelial Cell Injury.
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Pazin,M.J. and Kadonaga,J.T.
  TITLE     What's up and down with histone deacetylation and transcription?
  JOURNAL   Cell 89 (3), 325-328 (1997)
   PUBMED   9150131
  REMARK    Review article
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Wolffe,A.P.
  TITLE     Transcriptional control. Sinful repression
  JOURNAL   Nature 387 (6628), 16-17 (1997)
   PUBMED   9139815
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Ohara,O., Nagase,T., Ishikawa,K., Nakajima,D., Ohira,M., Seki,N.
            and Nomura,N.
  TITLE     Construction and characterization of human brain cDNA libraries
            suitable for analysis of cDNA clones encoding relatively large
            proteins
  JOURNAL   DNA Res 4 (1), 53-59 (1997)
   PUBMED   9179496
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Wilson,L.C., Leverton,K., Oude Luttikhuis,M.E., Oley,C.A.,
            Flint,J., Wolstenholme,J., Duckett,D.P., Barrow,M.A., Leonard,J.V.,
            Read,A.P. et al.
  TITLE     Brachydactyly and mental retardation: an Albright hereditary
            osteodystrophy-like syndrome localized to 2q37
  JOURNAL   Am J Hum Genet 56 (2), 400-407 (1995)
   PUBMED   7847374
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Doherty,E.S. and Lacbawan,F.L.
  TITLE     2q37 Microdeletion Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301337
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC062017.6 and AC017028.11.
            
            Summary: Histones play a critical role in transcriptional
            regulation, cell cycle progression, and developmental events.
            Histone acetylation/deacetylation alters chromosome structure and
            affects transcription factor access to DNA. The protein encoded by
            this gene belongs to class II of the histone deacetylase/acuc/apha
            family. It possesses histone deacetylase activity and represses
            transcription when tethered to a promoter. This protein does not
            bind DNA directly, but through transcription factors MEF2C and
            MEF2D. It seems to interact in a multiprotein complex with RbAp48
            and HDAC3. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.948854.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..736
                     /product="histone deacetylase 4 isoform 7"
                     /EC_number="3.5.1.98"
                     /note="histone deacetylase A"
                     /calculated_mol_wt=81647
     Region          36..125
                     /region_name="ClassIIa_HDAC4_Gln-rich-N"
                     /note="Glutamine-rich N-terminal helical domain of HDAC4,
                     a Class IIa histone deacetylase; cd10162"
                     /db_xref="CDD:197398"
     Site            order(37..38,40..41,44,48,51..52,55..56,58..59,62..63,
                     65..66,69..71,73..75,77..78,80..82,84..85,88,91..92,
                     95..97)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:197398"
     Site            order(37..38,40..41,44,48,51,55,58,62..63,65..66,69..70,
                     73,77,80,84,91,95)
                     /site_type="other"
                     /note="dimer interface A, C [polypeptide binding]"
                     /db_xref="CDD:197398"
     Site            order(48,52,56,59,63,66,70..71,74..75,78,82,85)
                     /site_type="other"
                     /note="dimer interface A, D [polypeptide binding]"
                     /db_xref="CDD:197398"
     Site            order(66,70,81..82,85,92,96..97)
                     /site_type="other"
                     /note="dimer interface A, B [polypeptide binding]"
                     /db_xref="CDD:197398"
     Region          622..>729
                     /region_name="Arginase_HDAC"
                     /note="Arginase-like and histone-like hydrolases; cl17011"
                     /db_xref="CDD:450134"
     CDS             1..736
                     /gene="HDAC4"
                     /gene_synonym="AHO3; BDMR; HA6116; HD4; HDAC-4; HDAC-A;
                     HDACA; NEDCHF; NEDCHID"
                     /coded_by="NM_001435998.1:234..2444"
                     /note="isoform 7 is encoded by transcript variant 11"
                     /db_xref="GeneID:9759"
                     /db_xref="HGNC:HGNC:14063"
                     /db_xref="MIM:605314"
ORIGIN      
        1 mpstvdvata lplqvapsav pmdlrldhqf slpvaepalr eqqlqqella lkqkqqiqrq
       61 iliaefqrqh eqlsrqheaq lhehikqqqe mlamkhqqel lehqrklerh rqeqelekqh
      121 reqklqqlkn kekgkesava stevkmklqe fvlnkkkala hrnlnhciss dprywygktq
      181 hssldqsspp qsgvstsynh pvlgmydakd dfplrktase pnlklrsrlk qkvaerrssp
      241 llrrkdgpvv talkkrpldv tdsacssapg sgpsspnnss gsvsaengia pavpsipaet
      301 slahrlvare gsaaplplyt spslpnitlg lpatgpsagt agqqdaerlt lpalqqrlsl
      361 fpgthltpyl stsplerdgg aahspllqhm vlleqppaqa plvtglgalp lhaqslvgad
      421 rvspsihklr qhrplgrtqs aplpqnaqal qhlviqqqhq qflekhkqqf qqqqlqmnki
      481 ipkpseparq peshpeetee elrehqalld epyldrlpgq keahaqagvq vkqepiesde
      541 eeaeppreve pgqrqpseqe llfrqqalll eqqrihqlrn yqasmeaagi pvsfgghrpl
      601 sraqsspasa tfpvsvqepp tkprfttglv ydtlmlkhqc tcgsssshpe hagriqsiws
      661 rlqetglrgk cecirgrkat leelqtvhse ahtllygtnp lnrqkldskk llgslasvfv
      721 rlpcggvgvs vplmck
//
LOCUS       NP_001427459             282 aa            linear   PRI 21-NOV-2025
DEFINITION  syntaxin-3 isoform 6 [Homo sapiens].
ACCESSION   NP_001427459
VERSION     NP_001427459.1
DBSOURCE    REFSEQ: accession NM_001440530.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Shinozuka,T., Kanda,M., Sato,Y., Shimizu,D., Tanaka,C., Umeda,S.,
            Inokawa,Y., Hattori,N., Hayashi,M., Nakayama,G. and Kodera,Y.
  TITLE     Increased STX3 transcript and protein levels were associated with
            poor prognosis in two independent cohorts of esophageal squamous
            cell carcinoma patients
  JOURNAL   Cancer Med 12 (24), 22185-22195 (2023)
   PUBMED   38014487
  REMARK    GeneRIF: Increased STX3 transcript and protein levels were
            associated with poor prognosis in two independent cohorts of
            esophageal squamous cell carcinoma patients.
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Janecke,A.R., Liu,X., Adam,R., Punuru,S., Viestenz,A., Strauss,V.,
            Laass,M., Sanchez,E., Adachi,R., Schatz,M.P., Saboo,U.S.,
            Mittal,N., Rohrschneider,K., Escher,J., Ganesh,A., Al Zuhaibi,S.,
            Al Murshedi,F., AlSaleem,B., Alfadhel,M., Al Sinani,S.,
            Alkuraya,F.S., Huber,L.A., Muller,T., Heidelberger,R. and Janz,R.
  TITLE     Pathogenic STX3 variants affecting the retinal and intestinal
            transcripts cause an early-onset severe retinal dystrophy in
            microvillus inclusion disease subjects
  JOURNAL   Hum Genet 140 (8), 1143-1156 (2021)
   PUBMED   33974130
  REMARK    GeneRIF: Pathogenic STX3 variants affecting the retinal and
            intestinal transcripts cause an early-onset severe retinal
            dystrophy in microvillus inclusion disease subjects.
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Low,S.H., Vasanji,A., Nanduri,J., He,M., Sharma,N., Koo,M.,
            Drazba,J. and Weimbs,T.
  TITLE     Syntaxins 3 and 4 are concentrated in separate clusters on the
            plasma membrane before the establishment of cell polarity
  JOURNAL   Mol Biol Cell 17 (2), 977-989 (2006)
   PUBMED   16339081
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Martin-Martin,B., Nabokina,S.M., Lazo,P.A. and Mollinedo,F.
  TITLE     Co-expression of several human syntaxin genes in neutrophils and
            differentiating HL-60 cells: variant isoforms and detection of
            syntaxin 1
  JOURNAL   J Leukoc Biol 65 (3), 397-406 (1999)
   PUBMED   10080545
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Steegmaier,M., Yang,B., Yoo,J.S., Huang,B., Shen,M., Yu,S., Luo,Y.
            and Scheller,R.H.
  TITLE     Three novel proteins of the syntaxin/SNAP-25 family
  JOURNAL   J Biol Chem 273 (51), 34171-34179 (1998)
   PUBMED   9852078
REFERENCE   8  (residues 1 to 282)
  AUTHORS   Riento,K., Galli,T., Jansson,S., Ehnholm,C., Lehtonen,E. and
            Olkkonen,V.M.
  TITLE     Interaction of Munc-18-2 with syntaxin 3 controls the association
            of apical SNAREs in epithelial cells
  JOURNAL   J Cell Sci 111 (Pt 17), 2681-2688 (1998)
   PUBMED   9701566
REFERENCE   9  (residues 1 to 282)
  AUTHORS   Galli,T., Zahraoui,A., Vaidyanathan,V.V., Raposo,G., Tian,J.M.,
            Karin,M., Niemann,H. and Louvard,D.
  TITLE     A novel tetanus neurotoxin-insensitive vesicle-associated membrane
            protein in SNARE complexes of the apical plasma membrane of
            epithelial cells
  JOURNAL   Mol Biol Cell 9 (6), 1437-1448 (1998)
   PUBMED   9614185
REFERENCE   10 (residues 1 to 282)
  AUTHORS   Delgrossi,M.H., Breuza,L., Mirre,C., Chavrier,P. and Le Bivic,A.
  TITLE     Human syntaxin 3 is localized apically in human intestinal cells
  JOURNAL   J Cell Sci 110 (Pt 18), 2207-2214 (1997)
   PUBMED   9378770
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000640.5.
            
            Summary: The gene is a member of the syntaxin family. The encoded
            protein is targeted to the apical membrane of epithelial cells
            where it forms clusters and is important in establishing and
            maintaining polarity necessary for protein trafficking involving
            vesicle fusion and exocytosis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.917716.1,
                                           SRR14372079.2576274.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154405 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..282
                     /product="syntaxin-3 isoform 6"
                     /note="syntaxin 3A; syntaxin 3B"
                     /calculated_mol_wt=32216
     Region          34..219
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     Region          187..253
                     /region_name="SNARE"
                     /note="SNARE motif; cl22856"
                     /db_xref="CDD:473982"
     Site            order(215,222,225)
                     /site_type="other"
                     /note="flanking leucine-zipper layers"
                     /db_xref="CDD:277192"
     Site            218
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277192"
     CDS             1..282
                     /gene="STX3"
                     /gene_synonym="DIAR12; MVID2; RDMVID; STX3A"
                     /coded_by="NM_001440530.1:231..1079"
                     /note="isoform 6 is encoded by transcript variant 11"
                     /db_xref="GeneID:6809"
                     /db_xref="HGNC:HGNC:11438"
                     /db_xref="MIM:600876"
ORIGIN      
        1 mkdrleqlka kqltqdddtd aveiaidnta fmdeffseie etrlnidkis ehveeakkly
       61 siilsapipe pktkddleql tteikkrann vrnklksmek hieedevrss adlrirksqf
      121 vevmtkynea qvdfrerskg riqrqleitg kkttdeelee mlesgnpaif tsgiidsqis
      181 kqalseiegr hkdivrless ikelhdmfmd iamlvenqge mldnielnvm htvdhvekar
      241 detkkavkyq sqarkkliii ivlvvvllgi laliiglsvg ln
//
LOCUS       NP_001400608             408 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 12 precursor [Homo sapiens].
ACCESSION   NP_001400608
VERSION     NP_001400608.1
DBSOURCE    REFSEQ: accession NM_001413679.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 408)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 408)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 408)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2432891.1,
                                           SRR14038194.1512799.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..408
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 12 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=42178
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..329
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            277..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     CDS             1..408
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413679.1:169..1395"
                     /note="isoform 12 precursor is encoded by transcript
                     variant 15"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvsyih gssqaqfvae shiilvlnaa itmgmvllne
      301 aatskgdvgk rrstcptlpp sslllvilwv hletreknht hvvltslmqt gvdyfivnfl
      361 rvisdfkpgs ykitelfish nipdtitckd neviiffrsf svmdfrlw
//
LOCUS       NP_001425592             919 aa            linear   PRI 21-NOV-2025
DEFINITION  TRPM8 channel-associated factor 2 isoform C [Homo sapiens].
ACCESSION   NP_001425592 XP_047276173
VERSION     NP_001425592.2
DBSOURCE    REFSEQ: accession NM_001438663.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Yun,D., Liang,J., Wang,X., Fan,J., Wang,X., Li,J., Ren,X., Liu,J.,
            Ren,X., Zhang,H., Shang,G., Jin,W., Chen,L., Li,T., Zhang,C., Yu,S.
            and Yang,X.
  TITLE     TCAF2 drives glioma cellular migratory/invasion properties through
            STAT3 signaling
  JOURNAL   Mol Cell Biochem 479 (7), 1801-1815 (2024)
   PUBMED   38019450
  REMARK    GeneRIF: TCAF2 drives glioma cellular migratory/invasion properties
            through STAT3 signaling.
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Li,Y., Li,J., Chen,H., Lu,B., Lu,F., Chen,H., Liu,H. and Qian,C.
  TITLE     TCAF2 is associated with the immune microenvironment, promotes
            pathogenesis, and impairs prognosis in glioma
  JOURNAL   Gene 883, 147667 (2023)
   PUBMED   37506986
  REMARK    GeneRIF: TCAF2 is associated with the immune microenvironment,
            promotes pathogenesis, and impairs prognosis in glioma.
REFERENCE   4  (residues 1 to 919)
  AUTHORS   Li,X., Qi,Q., Li,Y., Miao,Q., Yin,W., Pan,J., Zhao,Z., Chen,X.,
            Yang,F., Zhou,X., Huang,M., Wang,C., Deng,L., Huang,D., Qi,M.,
            Fan,S., Zhang,Y., Qiu,S., Deng,W., Liu,T., Chen,M., Ye,W. and
            Zhang,D.
  TITLE     TCAF2 in Pericytes Promotes Colorectal Cancer Liver Metastasis via
            Inhibiting Cold-Sensing TRPM8 Channel
  JOURNAL   Adv Sci (Weinh) 10 (30), e2302717 (2023)
   PUBMED   37635201
  REMARK    GeneRIF: TCAF2 in Pericytes Promotes Colorectal Cancer Liver
            Metastasis via Inhibiting Cold-Sensing TRPM8 Channel.
REFERENCE   5  (residues 1 to 919)
  AUTHORS   Hsieh,P., Dang,V., Vollger,M.R., Mao,Y., Huang,T.H., Dishuck,P.C.,
            Baker,C., Cantsilieris,S., Lewis,A.P., Munson,K.M., Sorensen,M.,
            Welch,A.E., Underwood,J.G. and Eichler,E.E.
  TITLE     Evidence for opposing selective forces operating on human-specific
            duplicated TCAF genes in Neanderthals and humans
  JOURNAL   Nat Commun 12 (1), 5118 (2021)
   PUBMED   34433829
  REMARK    GeneRIF: Evidence for opposing selective forces operating on
            human-specific duplicated TCAF genes in Neanderthals and humans.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 919)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 919)
  AUTHORS   Gkika,D., Lemonnier,L., Shapovalov,G., Gordienko,D., Poux,C.,
            Bernardini,M., Bokhobza,A., Bidaux,G., Degerny,C., Verreman,K.,
            Guarmit,B., Benahmed,M., de Launoit,Y., Bindels,R.J., Fiorio Pla,A.
            and Prevarskaya,N.
  TITLE     TRP channel-associated factors are a novel protein family that
            regulates TRPM8 trafficking and activity
  JOURNAL   J Cell Biol 208 (1), 89-107 (2015)
   PUBMED   25559186
  REMARK    GeneRIF: Report novel TRP channel-associated factors that modulate
            TRPM8 activity.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073264.5 and AC106862.3.
            
            On or before Apr 25, 2025 this sequence version replaced
            XP_047276173.1, NP_001425592.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2875495.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2142348,
                                           SAMEA2151405 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q35"
     Protein         1..919
                     /product="TRPM8 channel-associated factor 2 isoform C"
                     /note="family with sequence similarity 139, member A;
                     protein FAM115C; family with sequence similarity 115,
                     member C; TRP channel-associated factor 2"
                     /calculated_mol_wt=100775
     Region          522..632
                     /region_name="M60-like_N"
                     /note="N-terminal domain of M60-like peptidases;
                     pfam17291"
                     /db_xref="CDD:435844"
     Region          633..889
                     /region_name="Peptidase_M60"
                     /note="Peptidase M60, enhancin and enhancin-like;
                     pfam13402"
                     /db_xref="CDD:433178"
     CDS             1..919
                     /gene="TCAF2"
                     /gene_synonym="FAM115C; FAM139A; GATD9; GATD9B"
                     /coded_by="NM_001438663.2:175..2934"
                     /note="isoform C is encoded by transcript variant 10"
                     /db_xref="GeneID:285966"
                     /db_xref="HGNC:HGNC:26878"
                     /db_xref="MIM:616252"
ORIGIN      
        1 matiaaaafe almdgvtcwd vprgpipsel lligeaafpv mvndkgqvli aassygrgrl
       61 vvvshegyls htglapflln avswlcpcpg apvgvhpsla plvnilqdag leaqvkpepg
      121 eplgvycina yndtltatli qfvkhgggll iggqawywas qhgpdkvlsr fpgnkvtsva
      181 gvyftdtygd rdrfkvskkv pkiplhvryg edvrqdqqql legiseldir tggvpsqllv
      241 hgalafplgl daslncflaa ahygrgrvvl aahecllcap kmgpfllnav rwlargqtgk
      301 vgvntnlkdl cpllsehglq cslephlnsd lcvycckays dkeakqlqef vaegggllig
      361 gqawwwasqn pghcplagfp gniilncfgl silpqtlkag cfpvptpemr syhfrkalsq
      421 fqailnheng nleksclakl rvdgaaflqi paegvpayis lhrllrkmlr gsglpavsre
      481 npvasdsyea avlslatgla hsgtdcsqla qglgtwtcss slypskhpit veinginpgn
      541 ndcwvstgly llegqnaevs lseaaasagl rvqigchtdd ltkarklsra pvvthqcwmd
      601 rtersvsclw ggllyvivpk gsqlgpvpvt irgavpapyy klgktsleew krqmqenlap
      661 wgelatdnii ltvpttnlqa lkdpepvlrl wdemmqavar laaepfpfrr perivadvqi
      721 sagwmhsgyp imchlesvke iinemdmrsr gvwgpihelg hnqqrhgwef pphtteatcn
      781 lwsvyvhetv lgipraqahe alsppererr ikahlgkgap lcdwnvwtal etylqlqeaf
      841 gwepftqlfa eyqtlshlpk dntgrmnlwv kkfsekvkkn lvpffeawgw piqkevadsl
      901 aslpewqenp mqvylrark
//
LOCUS       NP_001428013            1231 aa            linear   PRI 21-NOV-2025
DEFINITION  cohesin subunit SA-2 isoform b [Homo sapiens].
ACCESSION   NP_001428013 XP_047297741 XP_054182366
VERSION     NP_001428013.1
DBSOURCE    REFSEQ: accession NM_001441084.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1231)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1231)
  AUTHORS   Fischer,A., Hernandez-Rodriguez,B., Mulet-Lazaro,R., Nuetzel,M.,
            Holzl,F., van Herk,S., Kavelaars,F.G., Stanewsky,H., Ackermann,U.,
            Niang,A.H., Diaz,N., Reuschel,E., Strieder,N., Hernandez-Lopez,I.,
            Valk,P.J.M., Vaquerizas,J.M., Rehli,M., Delwel,R. and Gebhard,C.
  TITLE     STAG2 mutations reshape the cohesin-structured spatial chromatin
            architecture to drive gene regulation in acute myeloid leukemia
  JOURNAL   Cell Rep 43 (8), 114498 (2024)
   PUBMED   39084219
  REMARK    GeneRIF: STAG2 mutations reshape the cohesin-structured spatial
            chromatin architecture to drive gene regulation in acute myeloid
            leukemia.
REFERENCE   3  (residues 1 to 1231)
  AUTHORS   Huber,J., Tanasie,N.L., Zernia,S. and Stigler,J.
  TITLE     Single-molecule imaging reveals a direct role of CTCF's zinc
            fingers in SA interaction and cluster-dependent RNA recruitment
  JOURNAL   Nucleic Acids Res 52 (11), 6490-6506 (2024)
   PUBMED   38742641
  REMARK    GeneRIF: Single-molecule imaging reveals a direct role of CTCF's
            zinc fingers in SA interaction and cluster-dependent RNA
            recruitment.
REFERENCE   4  (residues 1 to 1231)
  AUTHORS   Xu,W., Kim,J.S., Yang,T., Ya,A., Sadzewicz,L., Tallon,L.,
            Harris,B.T., Sarkaria,J., Jin,F. and Waldman,T.
  TITLE     STAG2 mutations regulate 3D genome organization, chromatin loops,
            and Polycomb signaling in glioblastoma multiforme
  JOURNAL   J Biol Chem 300 (6), 107341 (2024)
   PUBMED   38705393
  REMARK    GeneRIF: STAG2 mutations regulate 3D genome organization, chromatin
            loops, and Polycomb signaling in glioblastoma multiforme.
REFERENCE   5  (residues 1 to 1231)
  AUTHORS   Ros-Pardo,D., Gomez-Puertas,P. and Marcos-Alcalde,I.
  TITLE     STAG2: Computational Analysis of Missense Variants Involved in
            Disease
  JOURNAL   Int J Mol Sci 25 (2), 1280 (2024)
   PUBMED   38279279
  REMARK    GeneRIF: STAG2: Computational Analysis of Missense Variants
            Involved in Disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1231)
  AUTHORS   Gregson,H.C., Schmiesing,J.A., Kim,J.S., Kobayashi,T., Zhou,S. and
            Yokomori,K.
  TITLE     A potential role for human cohesin in mitotic spindle aster
            assembly
  JOURNAL   J Biol Chem 276 (50), 47575-47582 (2001)
   PUBMED   11590136
REFERENCE   7  (residues 1 to 1231)
  AUTHORS   Sumara,I., Vorlaufer,E., Gieffers,C., Peters,B.H. and Peters,J.M.
  TITLE     Characterization of vertebrate cohesin complexes and their
            regulation in prophase
  JOURNAL   J Cell Biol 151 (4), 749-762 (2000)
   PUBMED   11076961
REFERENCE   8  (residues 1 to 1231)
  AUTHORS   Carramolino,L., Lee,B.C., Zaballos,A., Peled,A., Barthelemy,I.,
            Shav-Tal,Y., Prieto,I., Carmi,P., Gothelf,Y., Gonzalez de
            Buitrago,G., Aracil,M., Marquez,G., Barbero,J.L. and Zipori,D.
  TITLE     SA-1, a nuclear protein encoded by one member of a novel gene
            family: molecular cloning and detection in hemopoietic organs
  JOURNAL   Gene 195 (2), 151-159 (1997)
   PUBMED   9305759
  REMARK    Erratum:[Gene 1998 Jan 12;206(2):283]
REFERENCE   9  (residues 1 to 1231)
  AUTHORS   Wu,C., Friedlander,P., Lamoureux,C., Zannis-Hadjopoulos,M. and
            Price,G.B.
  TITLE     cDNA clones contain autonomous replication activity
  JOURNAL   Biochim Biophys Acta 1174 (3), 241-257 (1993)
   PUBMED   7690594
REFERENCE   10 (residues 1 to 1231)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121601.13 and AL355476.12.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297741.1, XP_054182366.1.
            
            Summary: The protein encoded by this gene is a subunit of the
            cohesin complex, which regulates the separation of sister
            chromatids during cell division. Targeted inactivation of this gene
            results in chromatid cohesion defects and aneuploidy, suggesting
            that genetic disruption of cohesin is a cause of aneuploidy in
            human cancer. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.414213.1,
                                           SRR14038194.4072881.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142363, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1231
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..1231
                     /product="cohesin subunit SA-2 isoform b"
                     /note="SCC3 homolog 2; cohesin subunit SA-2; SA2
                     stromalin; sister chromatid cohesion 3 homolog B; stromal
                     antigen 2"
                     /calculated_mol_wt=141196
     Region          1..75
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Region          102..>395
                     /region_name="IRR1"
                     /note="Cohesin [Cell division and chromosome
                     partitioning]; COG5537"
                     /db_xref="CDD:227824"
     Region          157..270
                     /region_name="STAG"
                     /note="STAG domain; pfam08514"
                     /db_xref="CDD:462502"
     Site            607
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1058
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1061
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Region          1064..1083
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1064
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35638; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1065
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35638; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1112
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     CDS             1..1231
                     /gene="STAG2"
                     /gene_synonym="bA517O1.1; HPE13; MKMS; NEDXCF; SA-2; SA2;
                     SCC3B"
                     /coded_by="NM_001441084.1:352..4047"
                     /note="isoform b is encoded by transcript variant 23"
                     /db_xref="GeneID:10735"
                     /db_xref="HGNC:HGNC:11355"
                     /db_xref="MIM:300826"
ORIGIN      
        1 miaapeiptd fnllqeseth fssdtdfedi egknqkqgkg ktckkgkkgp aekgkggngg
       61 gkppsgpnrm nghhqqngve nmmlfevvkm gksamqsvvd dwiesykhdr dialldlinf
      121 fiqcsgckgv vtaemfrhmq nseiirkmte efdedsgdyp ltmagpqwkk fkssfcefig
      181 vlvrqcqysi iydeymmdtv islltglsds qvrafrhtst laamklmtal vnvalnlsin
      241 mdntqrqyea ernkmigkra nerlelllqk rkelqenqde ienmmnaifk gvfvhryrda
      301 iaeiraicie eigiwmkmys daflndsylk yvgwtmhdkq gevrlkclta lqglyynkel
      361 nsklelftsr fkdrivsmtl dkeydvavqa iklltlvlqs seevltaedc envyhlvysa
      421 hrpvavaage flykklfsrr dpeedgmmkr rgrqgpnanl vktlvfffle selhehaayl
      481 vdsmwdcate llkdwecmns llleeplsge ealtdrqesa lieimlctir qaaechppvg
      541 rgtgkrvlta kekktqlddr tkitelfava lpqllakysv daekvtnllq lpqyfdleiy
      601 ttgrlekhld allrqirniv ekhtdtdvle acsktyhalc neeftifnrv disrsqlide
      661 ladkfnrlle dflqegeepd eddayqvlst lkritafhna hdlskwdlfa cnykllktgi
      721 engdmpeqiv ihalqcthyv ilwqlakite ssstkedllr lkkqmrvfcq icqhyltnvn
      781 ttvkeqafti lcdilmifsh qimsggrdml eplvytpdss lqsellsfil dhvfieqddd
      841 nnsadgqqed easkiealhk rrnllaafck livytvvemn taadifkqym kyyndygdii
      901 ketmsktrqi dkiqcaktli lslqqlfnem iqengynfdr ssstfsgike larrfaltfg
      961 ldqlktreai amlhkdgief afkepnpqge shpplnlafl dilsefsskl lrqdkrtvyv
     1021 ylekfmtfqm slrredvwlp lmsyrnslla ggdddtmsvi sgissrgstv rskkskpstg
     1081 krkvvegmql slteessssd smwlsreqtl htpvmmqtpq ltstimrepk rlrpedsfms
     1141 vypmqtehhq tpldynrrgt slmeddeepi vedvmmsseg riedlnegmd fdtmdidlpp
     1201 sknrrertel kpdffdpasi mdesvlgvsm f
//
LOCUS       NP_001401235             449 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 3 isoform 6
            precursor [Homo sapiens].
ACCESSION   NP_001401235
VERSION     NP_001401235.1
DBSOURCE    REFSEQ: accession NM_001414306.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Tang,Q., Yuan,Y., Li,L., Xu,Y., Ji,W., Xiao,S., Han,Y., Miao,W.,
            Cai,J., You,P., Chen,M., Ding,S., Li,Z., Qi,Z., Hou,W. and Luo,H.
  TITLE     Comprehensive analysis reveals that LTBR is a immune-related
            biomarker for glioma
  JOURNAL   Comput Biol Med 174, 108457 (2024)
   PUBMED   38599071
  REMARK    GeneRIF: Comprehensive analysis reveals that LTBR is a
            immune-related biomarker for glioma.
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Wu,Y., Zhao,S., Guo,W., Liu,Y., Requena Mullor,M.D.M.,
            Rodriguez,R.A. and Wei,R.
  TITLE     Systematic analysis of the prognostic value and immunological
            function of LTBR in human cancer
  JOURNAL   Aging (Albany NY) 16 (1), 129-152 (2024)
   PUBMED   38175686
  REMARK    GeneRIF: Systematic analysis of the prognostic value and
            immunological function of LTBR in human cancer.
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Shuptrine,C.W., Perez,V.M., Selitsky,S.R., Schreiber,T.H. and
            Fromm,G.
  TITLE     Shining a LIGHT on myeloid cell targeted immunotherapy
  JOURNAL   Eur J Cancer 187, 147-160 (2023)
   PUBMED   37167762
  REMARK    Review article
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Abudukeyoumu,A., Lai,Z.Z., Lu,J.J., Zhang,X., Hou,D.Y., Dong,J.,
            Wu,J.N., Li,M.Q. and Xie,F.
  TITLE     A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion
  JOURNAL   J Reprod Immunol 153, 103693 (2022)
   PUBMED   35987137
  REMARK    GeneRIF: A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion.
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Remouchamps,C., Boutaffala,L., Ganeff,C. and Dejardin,E.
  TITLE     Biology and signal transduction pathways of the
            Lymphotoxin-alphabeta/LTbetaR system
  JOURNAL   Cytokine Growth Factor Rev 22 (5-6), 301-310 (2011)
   PUBMED   22152226
  REMARK    Review article
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Nakano,H., Oshima,H., Chung,W., Williams-Abbott,L., Ware,C.F.,
            Yagita,H. and Okumura,K.
  TITLE     TRAF5, an activator of NF-kappaB and putative signal transducer for
            the lymphotoxin-beta receptor
  JOURNAL   J Biol Chem 271 (25), 14661-14664 (1996)
   PUBMED   8663299
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Browning,J.L., Miatkowski,K., Sizing,I., Griffiths,D., Zafari,M.,
            Benjamin,C.D., Meier,W. and Mackay,F.
  TITLE     Signaling through the lymphotoxin beta receptor induces the death
            of some adenocarcinoma tumor lines
  JOURNAL   J Exp Med 183 (3), 867-878 (1996)
   PUBMED   8642291
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Baens,M., Aerssens,J., van Zand,K., Van den Berghe,H. and
            Marynen,P.
  TITLE     Isolation and regional assignment of human chromosome 12p cDNAs
  JOURNAL   Genomics 29 (1), 44-52 (1995)
   PUBMED   8530100
REFERENCE   9  (residues 1 to 449)
  AUTHORS   Crowe,P.D., VanArsdale,T.L., Walter,B.N., Ware,C.F., Hession,C.,
            Ehrenfels,B., Browning,J.L., Din,W.S., Goodwin,R.G. and Smith,C.A.
  TITLE     A lymphotoxin-beta-specific receptor
  JOURNAL   Science 264 (5159), 707-710 (1994)
   PUBMED   8171323
REFERENCE   10 (residues 1 to 449)
  AUTHORS   Baens,M., Chaffanet,M., Cassiman,J.J., van den Berghe,H. and
            Marynen,P.
  TITLE     Construction and evaluation of a hncDNA library of human 12p
            transcribed sequences derived from a somatic cell hybrid
  JOURNAL   Genomics 16 (1), 214-218 (1993)
   PUBMED   8486360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005840.2.
            
            Summary: This gene encodes a member of the tumor necrosis factor
            receptor superfamily. The major ligands of this receptor include
            lymphotoxin alpha/beta and tumor necrosis factor ligand superfamily
            member 14. The encoded protein plays a role in signalling during
            the development of lymphoid and other organs, lipid metabolism,
            immune response, and programmed cell death. Activity of this
            receptor has also been linked to carcinogenesis. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1713219.1,
                                           SRR14038193.4427162.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..449
                     /product="tumor necrosis factor receptor superfamily
                     member 3 isoform 6 precursor"
                     /note="tumor necrosis factor C receptor; lymphotoxin B
                     receptor; tumor necrosis factor receptor type III;
                     lymphotoxin beta receptor (TNFR superfamily, member 3);
                     tumor necrosis factor receptor 2-related protein"
                     /calculated_mol_wt=45180
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3049
     Region          11..182
                     /region_name="TNFRSF3"
                     /note="Tumor necrosis factor receptor superfamily member 3
                     (TNFRSF3), also known as lymphotoxin beta receptor (LTBR);
                     cd10578"
                     /db_xref="CDD:276904"
     Region          22..80
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276904"
     Region          83..124
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276904"
     Region          126..181
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276904"
     Region          148..>224
                     /region_name="TNFRSF"
                     /note="Tumor necrosis factor receptor superfamily
                     (TNFRSF); cl22855"
                     /db_xref="CDD:473981"
     Region          184..224
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276900"
     CDS             1..449
                     /gene="LTBR"
                     /gene_synonym="D12S370; LT-BETA-R; TNF-R-III; TNFCR;
                     TNFR-RP; TNFR2-RP; TNFR3; TNFRSF3"
                     /coded_by="NM_001414306.1:198..1547"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:4055"
                     /db_xref="HGNC:HGNC:6718"
                     /db_xref="MIM:600979"
ORIGIN      
        1 mllpwatsap glawgplvlg lfgllaasqp qavppyasen qtcrdqekey yepqhriccs
       61 rcppgtyvsa kcsrirdtvc atcaensyne hwnylticql crpcdpvmgl eeiapctskr
      121 ktqcrcqpgm fcaawalect hcellsdcpp gteaelkeah rrvleghgtg tdevgkgnnh
      181 cvpckaghfq ntsspsarcq phtrcenqgl veaapgtaqs dttcknplep lppemsgtml
      241 mlavllplaf flllatvfsc iwkshpslcr klgsllkrrp qgegpnpvag sweppkahpy
      301 fpdlvqpllp isgdvspvst glpaapvlea gvpqqqspld ltrepqlepg eqsqvahgtn
      361 gihvtggsmt itgniyiyng pvlggppgpg dlpatpeppy pipeegdpgp pglstphqed
      421 gkawhlaete hcgatpsnrg prnqfithd
//
LOCUS       NP_001362675             386 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 2 isoform xxx [Homo sapiens].
ACCESSION   NP_001362675
VERSION     NP_001362675.1
DBSOURCE    REFSEQ: accession NM_001375746.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Li,H., Liu,J., Lai,J., Su,X., Wang,X., Cao,J., Mao,S., Zhang,T. and
            Gu,Q.
  TITLE     The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like properties
            and tumorigenesis in HCC
  JOURNAL   J Transl Med 22 (1), 537 (2024)
   PUBMED   38844969
  REMARK    GeneRIF: The HHEX-ABI2/SLC17A9 axis induces cancer stem cell-like
            properties and tumorigenesis in HCC.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Zhu,Q., Combs,M.E., Liu,J., Bai,X., Wang,W.B., Herring,L.E.,
            Liu,J., Locasale,J.W., Bowles,D.E., Gross,R.T., Pla,M.M., Mack,C.P.
            and Taylor,J.M.
  TITLE     GRAF1 integrates PINK1-Parkin signaling and actin dynamics to
            mediate cardiac mitochondrial homeostasis
  JOURNAL   Nat Commun 14 (1), 8187 (2023)
   PUBMED   38081847
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Jensen,C.C., Clements,A.N., Liou,H., Ball,L.E., Bethard,J.R.,
            Langlais,P.R., Toth,R.K., Chauhan,S.S., Casillas,A.L., Daulat,S.R.,
            Kraft,A.S., Cress,A.E., Miranti,C.K., Mouneimne,G., Rogers,G.C. and
            Warfel,N.A.
  TITLE     PIM1 phosphorylates ABI2 to enhance actin dynamics and promote
            tumor invasion
  JOURNAL   J Cell Biol 222 (6) (2023)
   PUBMED   37042842
  REMARK    GeneRIF: PIM1 phosphorylates ABI2 to enhance actin dynamics and
            promote tumor invasion.
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Machado,R.D., Pauciulo,M.W., Fretwell,N., Veal,C., Thomson,J.R.,
            Vilarino Guell,C., Aldred,M., Brannon,C.A., Trembath,R.C. and
            Nichols,W.C.
  TITLE     A physical and transcript map based upon refinement of the critical
            interval for PPH1, a gene for familial primary pulmonary
            hypertension. The International PPH Consortium
  JOURNAL   Genomics 68 (2), 220-228 (2000)
   PUBMED   10964520
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   8  (residues 1 to 386)
  AUTHORS   Juang,J.L. and Hoffmann,F.M.
  TITLE     Drosophila abelson interacting protein (dAbi) is a positive
            regulator of abelson tyrosine kinase activity
  JOURNAL   Oncogene 18 (37), 5138-5147 (1999)
   PUBMED   10498863
REFERENCE   9  (residues 1 to 386)
  AUTHORS   Wang,B., Mysliwiec,T., Krainc,D., Jensen,R.A., Sonoda,G.,
            Testa,J.R., Golemis,E.A. and Kruh,G.D.
  TITLE     Identification of ArgBP1, an Arg protein tyrosine kinase binding
            protein that is the human homologue of a CNS-specific Xenopus gene
  JOURNAL   Oncogene 12 (9), 1921-1929 (1996)
   PUBMED   8649853
REFERENCE   10 (residues 1 to 386)
  AUTHORS   Dai,Z. and Pendergast,A.M.
  TITLE     Abi-2, a novel SH3-containing protein interacts with the c-Abl
            tyrosine kinase and modulates c-Abl transforming activity
  JOURNAL   Genes Dev 9 (21), 2569-2582 (1995)
   PUBMED   7590236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC080075.7 and AC018891.9.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3063074.1,
                                           SRR14038195.214836.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..386
                     /product="abl interactor 2 isoform xxx"
                     /note="abl-interacting protein 1 (SH3-containing protein);
                     abl binding protein 3; arg protein tyrosine kinase-binding
                     protein; abl-interactor protein 2b; abelson interactor 2;
                     arg-binding protein 1"
                     /calculated_mol_wt=42374
     Region          325..385
                     /region_name="SH3_Abi2"
                     /note="Src homology 3 domain of Abl Interactor 2; cd11972"
                     /db_xref="CDD:212905"
     Site            order(333,335,338,342,360..361,374,376..377)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212905"
     CDS             1..386
                     /gene="ABI2"
                     /gene_synonym="ABI-2; ABI2B; AblBP3; AIP-1; AIP1; argBP1;
                     argBPIA; argBPIB; SSH3BP2"
                     /coded_by="NM_001375746.1:122..1282"
                     /note="isoform xxx is encoded by transcript variant 81"
                     /db_xref="GeneID:10152"
                     /db_xref="HGNC:HGNC:24011"
                     /db_xref="MIM:606442"
ORIGIN      
        1 maelqmllee eipggrralf dsytnlerva dycennyiqs adkqraleet kayttqslas
       61 vaylintlan nvlqmldiqa sqlrrmessi nhisqvstqn mkmgglprtt pptqkppspp
      121 msgkgtlgrh spyrtlepvr ppvvpndyvp sptrnmapsq qspvrtasvn qrnrtyssgs
      181 sggshpssrs ssrensgsgs vgvpiavptp sppsvfpghp vqfysmnrpa srhtpptigg
      241 slpyrrppsi tsqtslqnqm nggpfysqnp vsdtpppppp veepvfdesp ppppppedye
      301 eeeaavveys dpyaeedppw aprsylekvv aiydytkdke delsfqegai iyvikknddg
      361 wyegvmngvt glfpgnyves imhyse
//
LOCUS       NP_001425938            1019 aa            linear   PRI 21-NOV-2025
DEFINITION  2-oxoglutarate dehydrogenase complex component E1 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001425938 XP_047276384 XP_054214286
VERSION     NP_001425938.1
DBSOURCE    REFSEQ: accession NM_001439009.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Nguyen,T.T., Torrini,C., Shang,E., Shu,C., Mun,J.Y., Gao,Q.,
            Humala,N., Akman,H.O., Zhang,G., Westhoff,M.A., Karpel-Massler,G.,
            Bruce,J.N., Canoll,P. and Siegelin,M.D.
  TITLE     OGDH and Bcl-xL loss causes synthetic lethality in glioblastoma
  JOURNAL   JCI Insight 9 (8), e172565 (2024)
   PUBMED   38483541
  REMARK    GeneRIF: OGDH and Bcl-xL loss causes synthetic lethality in
            glioblastoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Hevler,J.F., Albanese,P., Cabrera-Orefice,A., Potter,A.,
            Jankevics,A., Misic,J., Scheltema,R.A., Brandt,U., Arnold,S. and
            Heck,A.J.R.
  TITLE     MRPS36 provides a structural link in the eukaryotic 2-oxoglutarate
            dehydrogenase complex
  JOURNAL   Open Biol 13 (3), 220363 (2023)
   PUBMED   36854377
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Whittle,E.F., Chilian,M., Karimiani,E.G., Progri,H., Buhas,D.,
            Kose,M., Ganetzky,R.D., Toosi,M.B., Torbati,P.N., Badv,R.S.,
            Shelihan,I., Yang,H., Elloumi,H.Z., Lee,S., Jamshidi,Y.,
            Pittman,A.M., Houlden,H., Ignatius,E., Rahman,S., Maroofian,R.,
            Yoon,W.H. and Carroll,C.J.
  TITLE     Biallelic variants in OGDH encoding oxoglutarate dehydrogenase lead
            to a neurodevelopmental disorder characterized by global
            developmental delay, movement disorder, and metabolic abnormalities
  JOURNAL   Genet Med 25 (2), 100332 (2023)
   PUBMED   36520152
  REMARK    GeneRIF: Biallelic variants in OGDH encoding oxoglutarate
            dehydrogenase lead to a neurodevelopmental disorder characterized
            by global developmental delay, movement disorder, and metabolic
            abnormalities.
REFERENCE   4  (residues 1 to 1019)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 1019)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 1019)
  AUTHORS   McCartney,R.G., Rice,J.E., Sanderson,S.J., Bunik,V., Lindsay,H. and
            Lindsay,J.G.
  TITLE     Subunit interactions in the mammalian alpha-ketoglutarate
            dehydrogenase complex. Evidence for direct association of the
            alpha-ketoglutarate dehydrogenase and dihydrolipoamide
            dehydrogenase components
  JOURNAL   J Biol Chem 273 (37), 24158-24164 (1998)
   PUBMED   9727038
REFERENCE   7  (residues 1 to 1019)
  AUTHORS   Koike,K.
  TITLE     The gene encoding human 2-oxoglutarate dehydrogenase: structural
            organization and mapping to chromosome 7p13-p14
  JOURNAL   Gene 159 (2), 261-266 (1995)
   PUBMED   7622061
REFERENCE   8  (residues 1 to 1019)
  AUTHORS   Szabo,P., Cai,X., Ali,G. and Blass,J.P.
  TITLE     Localization of the gene (OGDH) coding for the E1k component of the
            alpha-ketoglutarate dehydrogenase complex to chromosome 7p13-p11.2
  JOURNAL   Genomics 20 (2), 324-326 (1994)
   PUBMED   8020988
REFERENCE   9  (residues 1 to 1019)
  AUTHORS   Koike,K., Urata,Y. and Goto,S.
  TITLE     Cloning and nucleotide sequence of the cDNA encoding human
            2-oxoglutarate dehydrogenase (lipoamide)
  JOURNAL   Proc Natl Acad Sci U S A 89 (5), 1963-1967 (1992)
   PUBMED   1542694
REFERENCE   10 (residues 1 to 1019)
  AUTHORS   Reed,L.J. and Hackert,M.L.
  TITLE     Structure-function relationships in dihydrolipoamide
            acyltransferases
  JOURNAL   J Biol Chem 265 (16), 8971-8974 (1990)
   PUBMED   2188967
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011894.3 and AC004859.3.
            
            On or before Apr 25, 2025 this sequence version replaced
            XP_047276384.1, XP_054214286.1.
            
            Summary: This gene encodes one subunit of the 2-oxoglutarate
            dehydrogenase complex. This complex catalyzes the overall
            conversion of 2-oxoglutarate (alpha-ketoglutarate) to succinyl-CoA
            and CO(2) during the Krebs cycle. The protein is located in the
            mitochondrial matrix and uses thiamine pyrophosphate as a cofactor.
            A congenital deficiency in 2-oxoglutarate dehydrogenase activity is
            believed to lead to hypotonia, metabolic acidosis, and
            hyperlactatemia. Alternative splicing results in multiple
            transcript variants encoding distinct isoforms.[provided by RefSeq,
            Sep 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2813557.1,
                                           SRR11853563.30067.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..1019
                     /product="2-oxoglutarate dehydrogenase complex component
                     E1 isoform 3"
                     /EC_number="1.2.4.2"
                     /note="oxoglutarate dehydrogenase (succinyl-transferring);
                     oxoglutarate (alpha-ketoglutarate) dehydrogenase
                     (lipoamide); 2-oxoglutarate dehydrogenase, mitochondrial;
                     oxoglutarate decarboxylase; OGDC-E1; 2-oxoglutarate
                     dehydrogenase complex component E1; testicular tissue
                     protein Li 131; alpha-KGDH-E1; thiamine diphosphate
                     (ThDP)-dependent 2-oxoglutarate dehydrogenase"
                     /calculated_mol_wt=115383
     Region          49..1012
                     /region_name="SucA"
                     /note="2-oxoglutarate dehydrogenase complex, dehydrogenase
                     (E1) component, and related enzymes [Energy production and
                     conversion]; COG0567"
                     /db_xref="CDD:440333"
     CDS             1..1019
                     /gene="OGDH"
                     /gene_synonym="AKGDH; E1k; E1o; HsOGDH; KGD1; OGDC;
                     OGDH-E1; OGDH2; OGDHD"
                     /coded_by="NM_001439009.1:166..3225"
                     /note="isoform 3 is encoded by transcript variant 7"
                     /db_xref="GeneID:4967"
                     /db_xref="HGNC:HGNC:8124"
                     /db_xref="MIM:613022"
ORIGIN      
        1 mfhlrtcaak lrpltasqtv ktfsqnrpaa artfqqircy sapvaaepfl sgtssnyvee
       61 mycawlenpk svhkswdiff rntnagappg tayqsplpls rgslaavaha qslveaqpnv
      121 dklvedhlav qslirayqvr ghhiakldpl giscvnfdda pvtvssnvgf ygldesdldk
      181 vfhlptttfi ggqesalplr eiirrlemay cqhigvefmf indleqcqwi rqkfetpgim
      241 qftneekrtl larlvrstrf eeflqrkwss ekrfglegce vlipalktii dkssengvdy
      301 vimgmphrgr lnvlanvirk eleqifcqfd skleaadegs gdvkyhlgmy hrrinrvtdr
      361 nitlslvanp shleaadpvv mgktkaeqfy cgdtegkkvm sillhgdaaf agqgivyetf
      421 hlsdlpsytt hgtvhvvvnn qigfttdprm arsspyptdv arvvnapifh vnsddpeavm
      481 yvckvaaewr stfhkdvvvd lvcyrrnghn emdepmftqp lmykqirkqk pvlqkyaell
      541 vsqgvvnqpe yeeeiskydk iceeafarsk dekilhikhw ldspwpgfft ldgqprsmsc
      601 pstgltedil thignvassv pvenftihgg lsrilktrge mvknrtvdwa laeymafgsl
      661 lkegihirls gqdvergtfs hrhhvlhdqn vdkrtcipmn hlwpnqapyt vcnsslseyg
      721 vlgfelgfam aspnalvlwe aqfgdfhnta qciidqficp gqakwvrqng ivlllphgme
      781 gmgpehssar perflqmcnd dpdvlpdlke anfdinqlyd cnwvvvncst pgnffhvlrr
      841 qillpfrkpl iiftpksllr hpearssfde mlpgthfqrv ipedgpaaqn penvkrllfc
      901 tgkvyydltr erkardmvgq vaitrieqls pfpfdlllke vqkypnaela wcqeehknqg
      961 yydyvkprlr ttisrakpvw yagrdpaaap atgnkkthlt elqrlldtaf dldvfknfs
//
LOCUS       NP_001401582             531 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 2 isoform c [Homo sapiens].
ACCESSION   NP_001401582
VERSION     NP_001401582.1
DBSOURCE    REFSEQ: accession NM_001414653.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Jung,J.H., Lee,D., Ko,H.M. and Jang,H.J.
  TITLE     Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in Colorectal
            Cancer Cells by Activating p53
  JOURNAL   Biomolecules 11 (10), 1492 (2021)
   PUBMED   34680125
  REMARK    GeneRIF: Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in
            Colorectal Cancer Cells by Activating p53.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Royer-Bertrand,B., Cisarova,K., Niel Butschi,F., Foletti,G.,
            Guinchat,V., Tran,C., Superti-Furga,A. and Good,J.M.
  TITLE     CNOT2 haploinsufficiency in a 40-year-old man with intellectual
            disability, autism, and seizures
  JOURNAL   Am J Med Genet A 185 (8), 2602-2606 (2021)
   PUBMED   34018673
  REMARK    GeneRIF: CNOT2 haploinsufficiency in a 40-year-old man with
            intellectual disability, autism, and seizures.
            Review article
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Jayne,S., Zwartjes,C.G., van Schaik,F.M. and Timmers,H.T.
  TITLE     Involvement of the SMRT/NCoR-HDAC3 complex in transcriptional
            repression by the CNOT2 subunit of the human Ccr4-Not complex
  JOURNAL   Biochem J 398 (3), 461-467 (2006)
   PUBMED   16712523
  REMARK    GeneRIF: This study shows that SMRT/NCoR-HDAC3 complex is a
            cofactor of CNOT2-mediated repression and suggests that
            transcriptional regulation by the Ccr4-Not complex involves
            regulation of chromatin modification.
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Winkler,G.S., Mulder,K.W., Bardwell,V.J., Kalkhoven,E. and
            Timmers,H.T.
  TITLE     Human Ccr4-Not complex is a ligand-dependent repressor of nuclear
            receptor-mediated transcription
  JOURNAL   EMBO J 25 (13), 3089-3099 (2006)
   PUBMED   16778766
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Shi,J. and Nelson,M.A.
  TITLE     The cyclin-dependent kinase 11 interacts with NOT2
  JOURNAL   Biochem Biophys Res Commun 334 (4), 1310-1316 (2005)
   PUBMED   16039607
  REMARK    GeneRIF: These findings suggest that CDK11 may contribute to
            apoptosis by regulating the activity of NOT2 independent of its
            kinase activity.
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Zwartjes,C.G., Jayne,S., van den Berg,D.L. and Timmers,H.T.
  TITLE     Repression of promoter activity by CNOT2, a subunit of the
            transcription regulatory Ccr4-not complex
  JOURNAL   J Biol Chem 279 (12), 10848-10854 (2004)
   PUBMED   14707134
  REMARK    GeneRIF: major repression function of CNOT2 is localized in a
            specialized protein motif, the Not-Box
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Denis,C.L. and Chen,J.
  TITLE     The CCR4-NOT complex plays diverse roles in mRNA metabolism
  JOURNAL   Prog Nucleic Acid Res Mol Biol 73, 221-250 (2003)
   PUBMED   12882519
  REMARK    Review article
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092881.8 and AC025569.37.
            
            Summary: This gene encodes a subunit of the multi-component
            CCR4-NOT complex. The CCR4-NOT complex regulates mRNA synthesis and
            degradation and is also thought to be involved in mRNA splicing,
            transport and localization. The encoded protein interacts with
            histone deacetylases and functions as a repressor of polymerase II
            transcription. Alternatively spliced transcript variants have been
            observed for this gene. [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1334290.1,
                                           SRR1803615.244525.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..531
                     /product="CCR4-NOT transcription complex subunit 2 isoform
                     c"
                     /note="negative regulator of transcription 2;
                     CCR4-associated factor 2; CC chemokine receptor 4-negative
                     regulator of transcription 2"
                     /calculated_mol_wt=58490
     Region          387..510
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..531
                     /gene="CNOT2"
                     /gene_synonym="CDC36; HSPC131; IDNADFS; NOT2; NOT2H"
                     /coded_by="NM_001414653.1:395..1990"
                     /note="isoform c is encoded by transcript variant 7"
                     /db_xref="GeneID:4848"
                     /db_xref="HGNC:HGNC:7878"
                     /db_xref="MIM:604909"
ORIGIN      
        1 mlkevaqvtn smfgasrkkf vegvdsdyhd enmyysqssm fphrsekdml aspstsgqls
       61 qfgaslygqq salglpmrgm snntpqlnrs lsqgtqlpsh vtpttgvptm slhtppspsr
      121 gilpmnprnm mnhsqvgqgi gipsrtnsms ssglgspnrs spsiicmpkq qpsrqpftvn
      181 smsgfgmnrn qafgmnnsls snifngtdgs envtgldlsd fpaladrnrr egsgnptpli
      241 nplagrapyv gmvtkpaneq sqdfsihned fpalpgssyk dptssnddsk snlntsgktt
      301 sstdgpkfpg dkssttqnnn qqkkgiqvlp dgrvtnipqg mvtdqfgmig lltfiraaet
      361 dpgmvhlalg sdlttlglnl nspenlypkf aspwasspcr pqdidfhvps eyltnihird
      421 klaaiklgry gedllfylyy mnggdvlqll aavelfnrdw ryhkeervwi trapgmeptm
      481 ktntyergty yffdclnwrk vakefhleyd kleerphlps tfnynpaqqa f
//
LOCUS       NP_001389636            1122 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 16 [Homo sapiens].
ACCESSION   NP_001389636
VERSION     NP_001389636.1
DBSOURCE    REFSEQ: accession NM_001402707.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1122)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1122)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1122)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1122)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1122)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1122)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1122)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1122)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1122)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1122)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.260450.1,
                                           SRR1803613.142535.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1122
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1122
                     /product="kinectin isoform 16"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=129313
     Region          <142..>400
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          274..1062
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1122
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402707.1:178..3546"
                     /note="isoform 16 is encoded by transcript variant 30"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mvpskrqeal plhqetkqes gsgkkkassk kqktenvfvd eplihattyi plmdnadssp
       61 vvdkrevidl lkpdqvegiq ksgtkklkte tdkenaevkf kdfllslktm mfsedealcv
      121 vdllkeksgv iqdalkkssk gelttlihql qekdkllaav kedaaatkdr ckqltqemmt
      181 ekersnvvit rmkdrigtle kehnvfqnki hvsyqetqqm qmkfqqvreq meaeiahlkq
      241 engilrdavs nttnqleskq saelnklrqd yarlvnelte ktgklqqeev qkknaeqaat
      301 qlkvqlqeae rrweevqsyi rkrtaeheaa qqdlqskfva kenevqslhs kltdtlvskq
      361 qleqrlmqlm eseqkrvnke eslqmqvqdi leqnealkaq iqqfhsqiaa qtsasvlaee
      421 lhkviaekdk qikqtedsla serdrltske eelkdiqnmn fllkaevqkl qalaneqaaa
      481 ahelekmqqs vyvkddkirl leeqlqheis nkmeefkiln dqnkalksev qklqtlvseq
      541 pnkdvveqme kciqekdekl ktveelletg liqvatkeee lnairtenss ltkevqdlka
      601 kqndqvsfas lveelkkvih ekdgkiksve elleaellkv ankektvqls itskvqelqn
      661 llkgkeeqmn tmkavleeke kdlantgkwl qdlqeenesl kahvqevaqh nlkeassasq
      721 feeleivlke kenelkrlea mlkeresdls sktqllqdvq denklfksqi eqlkqqnyqq
      781 assfppheel lkvisereke isglwnelds lkdavehqrk knndlreknw eamealaste
      841 kmlqdkvnkt skerqqqvea veleakevlk klfpkvsvps nlsygewlhg fekkakecma
      901 gtsgseevkv lehklkeade mhtllqlece kyksvlaete gilqklqrsv eqeenkwkvk
      961 vdeshktikq mqssftsseq elerlrsenk dienlrrere hlemelekae merstyvtev
     1021 relkaqlnet ltklrteqne rqkvagdlhk aqqsleliqs kivkaagdtt viensdvspe
     1081 tesseketms vslnqtvtql qqllqavnqq ltkekehyqv le
//
LOCUS       NP_001393530            1159 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 5 [Homo sapiens].
ACCESSION   NP_001393530
VERSION     NP_001393530.1
DBSOURCE    REFSEQ: accession NM_001406601.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1159)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1159)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1159)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1159)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1159)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1159)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1159)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1159)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1159)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1159)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1065013.1,
                                           SRR18074969.1011536.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1159
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1159
                     /product="hamartin isoform 5"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=129211
     Region          7..714
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          439..571
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <703..>955
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1001..1080
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1095
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1126..1159
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1159
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406601.1:218..3697"
                     /note="isoform 5 is encoded by transcript variant 15"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt aggkgtplgt patspppapl chsddyvhis lpqatvtppr
      421 keermdsarp clhrqhhlln drgseeppgs kgsvtlsdlp gflgdlasee dsiekdkeea
      481 aisrelseit taeaepvvpr ggfdspfyrd slpgsqrkth saasssqgas vnpeplhssl
      541 dklgpdtpkq aftpidlpcg sadespagdr ecqtsletsi ftpspckipp ptrvgfgsgq
      601 pppydhlfev alpktahhfv irkteellkk akgnteedgv pstspmevld rliqqgadah
      661 skelnklplp sksvdwthfg deirtlrdql lllhnqllye rfkrqqhalr nrrllrkvik
      721 aaaleehnaa mkdqlklqek diqmwkvslq keqarynqlq eqrdtmvtkl hsqirqlqhd
      781 reefynqsqe lqtkledcrn miaelrielk kannkvchte lllsqvsqkl snsesvqqqm
      841 eflnrqllvl gevnelyleq lqnkhsdttk evemmkaayr keleknrshv lqqtqrldts
      901 qkrilelesh lakkdhllle qkkyledvkl qargqlqaae sryeaqkrit qvfeleildl
      961 ygrlekdgll kkleeekaea aeaaeerldc cndgcsdsmv ghneeasghn getktprpss
     1021 argssgsrgg ggssssssel stpekpphqr agpfssrwet tmgeasasip ttvgslpssk
     1081 sflgmkarel frnksesqcd edgmtsslse slktelgkdl gveakiplnl dgphpspptp
     1141 dsvgqlhimd ynethhehs
//
LOCUS       NP_001394197             341 aa            linear   PRI 21-NOV-2025
DEFINITION  cellular tumor antigen p53 isoform b [Homo sapiens].
ACCESSION   NP_001394197
VERSION     NP_001394197.1
DBSOURCE    REFSEQ: accession NM_001407268.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Mirgayazova,R., Khadiullina,R., Chasov,V., Mingaleeva,R.,
            Miftakhova,R., Rizvanov,A. and Bulatov,E.
  TITLE     Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an Option?
  JOURNAL   Genes (Basel) 11 (6), 704 (2020)
   PUBMED   32630614
  REMARK    GeneRIF: Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an
            Option?
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Flynt,E., Bisht,K., Sridharan,V., Ortiz,M., Towfic,F. and
            Thakurta,A.
  TITLE     Prognosis, Biology, and Targeting of TP53 Dysregulation in Multiple
            Myeloma
  JOURNAL   Cells 9 (2), 287 (2020)
   PUBMED   31991614
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Barnoud,T., Parris,J.L.D. and Murphy,M.E.
  TITLE     Common genetic variants in the TP53 pathway and their impact on
            cancer
  JOURNAL   J Mol Cell Biol 11 (7), 578-585 (2019)
   PUBMED   31152665
  REMARK    GeneRIF: Common genetic variants in the TP53 pathway and their
            impact on cancer.
            Review article
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Hu,W., Chen,S., Thorne,R.F. and Wu,M.
  TITLE     TP53, TP53 Target Genes (DRAM, TIGAR), and Autophagy
  JOURNAL   Adv Exp Med Biol 1206, 127-149 (2019)
   PUBMED   31776983
  REMARK    Review article
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Baugh,E.H., Ke,H., Levine,A.J., Bonneau,R.A. and Chan,C.S.
  TITLE     Why are there hotspot mutations in the TP53 gene in human cancers?
  JOURNAL   Cell Death Differ 25 (1), 154-160 (2018)
   PUBMED   29099487
  REMARK    GeneRIF: TP53 missense mutant alleles that occur in human cancers
            are discussed in the context of high resolution models of these p53
            mutant protein structures to determine the structural features of
            mutations (review).
            Review article
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Aubrey,B.J., Strasser,A. and Kelly,G.L.
  TITLE     Tumor-Suppressor Functions of the TP53 Pathway
  JOURNAL   Cold Spring Harb Perspect Med 6 (5), a026062 (2016)
   PUBMED   27141080
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Soussi,T. and Wiman,K.G.
  TITLE     TP53: an oncogene in disguise
  JOURNAL   Cell Death Differ 22 (8), 1239-1249 (2015)
   PUBMED   26024390
  REMARK    Review article
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Soussi,T.
  TITLE     The TP53 gene network in a postgenomic era
  JOURNAL   Hum Mutat 35 (6), 641-642 (2014)
   PUBMED   24753184
  REMARK    GeneRIF: Recommendations and guidelines for reporting and
            annotating TP53 variants are also provided, to help researchers
            generate standardized data that are easy to understand, analyze,
            and exchange across various cancer variant databases
            Review article
REFERENCE   9  (residues 1 to 341)
  AUTHORS   Anczukow,O., Ware,M.D., Buisson,M., Zetoune,A.B.,
            Stoppa-Lyonnet,D., Sinilnikova,O.M. and Mazoyer,S.
  TITLE     Does the nonsense-mediated mRNA decay mechanism prevent the
            synthesis of truncated BRCA1, CHK2, and p53 proteins?
  JOURNAL   Hum Mutat 29 (1), 65-73 (2008)
   PUBMED   17694537
  REMARK    GeneRIF: the p53 protein encoded by the 770delT allele is as
            abundant as the wild-type protein, as removal of the C-terminal p53
            domain leads to a stabilized mutant protein, whose abundance is
            markedly increased when NMD is inhibited.
REFERENCE   10 (residues 1 to 341)
  AUTHORS   Bourdon,J.C.
  TITLE     p53 Family isoforms
  JOURNAL   Curr Pharm Biotechnol 8 (6), 332-336 (2007)
   PUBMED   18289041
  REMARK    Review article
REFERENCE   11 (residues 1 to 341)
  AUTHORS   Candeias,M.M., Powell,D.J., Roubalova,E., Apcher,S., Bourougaa,K.,
            Vojtesek,B., Bruzzoni-Giovanelli,H. and Fahraeus,R.
  TITLE     Expression of p53 and p53/47 are controlled by alternative
            mechanisms of messenger RNA translation initiation
  JOURNAL   Oncogene 25 (52), 6936-6947 (2006)
   PUBMED   16983332
  REMARK    GeneRIF: harbouring alternative translation initiation sites, the
            p53 mRNA gives rise to different levels of the p53 isoforms which
            help to orchestrate the cell biological outcome of p53 activation
REFERENCE   12 (residues 1 to 341)
  AUTHORS   Murray-Zmijewski,F., Lane,D.P. and Bourdon,J.C.
  TITLE     p53/p63/p73 isoforms: an orchestra of isoforms to harmonise cell
            differentiation and response to stress
  JOURNAL   Cell Death Differ 13 (6), 962-972 (2006)
   PUBMED   16601753
  REMARK    Review article
REFERENCE   13 (residues 1 to 341)
  AUTHORS   Bourdon,J.C., Fernandes,K., Murray-Zmijewski,F., Liu,G., Diot,A.,
            Xirodimas,D.P., Saville,M.K. and Lane,D.P.
  TITLE     p53 isoforms can regulate p53 transcriptional activity
  JOURNAL   Genes Dev 19 (18), 2122-2137 (2005)
   PUBMED   16131611
  REMARK    GeneRIF: p53 isoforms can regulate p53 transcriptional activity.
REFERENCE   14 (residues 1 to 341)
  AUTHORS   Ghosh,A., Stewart,D. and Matlashewski,G.
  TITLE     Regulation of human p53 activity and cell localization by
            alternative splicing
  JOURNAL   Mol Cell Biol 24 (18), 7987-7997 (2004)
   PUBMED   15340061
  REMARK    GeneRIF: mechanism of p53 regulation originating through
            alternative splicing of the human p53 gene resulting in the
            expression of a novel p53 mRNA
REFERENCE   15 (residues 1 to 341)
  AUTHORS   Flaman,J.M., Waridel,F., Estreicher,A., Vannier,A., Limacher,J.M.,
            Gilbert,D., Iggo,R. and Frebourg,T.
  TITLE     The human tumour suppressor gene p53 is alternatively spliced in
            normal cells
  JOURNAL   Oncogene 12 (4), 813-818 (1996)
   PUBMED   8632903
REFERENCE   16 (residues 1 to 341)
  AUTHORS   Schneider,K., Zelley,K., Nichols,K.E., Schwartz Levine,A. and
            Garber,J.
  TITLE     Li-Fraumeni Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301488
REFERENCE   17 (residues 1 to 341)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   18 (residues 1 to 341)
  AUTHORS   Lamb,P. and Crawford,L.
  TITLE     Characterization of the human p53 gene
  JOURNAL   Mol Cell Biol 6 (5), 1379-1385 (1986)
   PUBMED   2946935
REFERENCE   19 (residues 1 to 341)
  AUTHORS   Isobe,M., Emanuel,B.S., Givol,D., Oren,M. and Croce,C.M.
  TITLE     Localization of gene for human p53 tumour antigen to band 17p13
  JOURNAL   Nature 320 (6057), 84-85 (1986)
   PUBMED   3456488
REFERENCE   20 (residues 1 to 341)
  AUTHORS   Benchimol,S., Lamb,P., Crawford,L.V., Sheer,D., Shows,T.B.,
            Bruns,G.A. and Peacock,J.
  TITLE     Transformation associated p53 protein is encoded by a gene on human
            chromosome 17
  JOURNAL   Somat Cell Mol Genet 11 (5), 505-510 (1985)
   PUBMED   2994241
REFERENCE   21 (residues 1 to 341)
  AUTHORS   Harlow,E., Williamson,N.M., Ralston,R., Helfman,D.M. and Adams,T.E.
  TITLE     Molecular cloning and in vitro expression of a cDNA clone for human
            cellular tumor antigen p53
  JOURNAL   Mol Cell Biol 5 (7), 1601-1610 (1985)
   PUBMED   3894933
REFERENCE   22 (residues 1 to 341)
  AUTHORS   Zakut-Houri,R., Bienz-Tadmor,B., Givol,D. and Oren,M.
  TITLE     Human p53 cellular tumor antigen: cDNA sequence and expression in
            COS cells
  JOURNAL   EMBO J 4 (5), 1251-1255 (1985)
   PUBMED   4006916
REFERENCE   23 (residues 1 to 341)
  AUTHORS   Matlashewski,G., Lamb,P., Pim,D., Peacock,J., Crawford,L. and
            Benchimol,S.
  TITLE     Isolation and characterization of a human p53 cDNA clone:
            expression of the human p53 gene
  JOURNAL   EMBO J 3 (13), 3257-3262 (1984)
   PUBMED   6396087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087388.9 and AC007421.13.
            
            Summary: This gene encodes a tumor suppressor protein containing
            transcriptional activation, DNA binding, and oligomerization
            domains. The encoded protein responds to diverse cellular stresses
            to regulate expression of target genes, thereby inducing cell cycle
            arrest, apoptosis, senescence, DNA repair, or changes in
            metabolism. Mutations in this gene are associated with a variety of
            human cancers, including hereditary cancers such as Li-Fraumeni
            syndrome. Alternative splicing of this gene and the use of
            alternate promoters result in multiple transcript variants and
            isoforms. Additional isoforms have also been shown to result from
            the use of alternate translation initiation codons from identical
            transcript variants (PMIDs: 12032546, 20937277). [provided by
            RefSeq, Dec 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2378303.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: PMID: 16131611, 16601753, 18289041
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..341
                     /product="cellular tumor antigen p53 isoform b"
                     /note="tumor protein 53; mutant tumor protein 53; cellular
                     tumor antigen p53; phosphoprotein p53;
                     transformation-related protein 53; antigen NY-CO-13; tumor
                     supressor p53"
                     /calculated_mol_wt=37695
     Region          1..320
                     /region_name="Interaction with CCAR2.
                     /evidence=ECO:0000269|PubMed:25732823"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          1..83
                     /region_name="Interaction with HRMT1L2.
                     /evidence=ECO:0000269|PubMed:15186775"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          1..44
                     /region_name="Transcription activation (acidic)"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          6..30
                     /region_name="P53_TAD"
                     /note="P53 transactivation motif; pfam08563"
                     /db_xref="CDD:462520"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by HIPK4.
                     /evidence=ECO:0000269|PubMed:18022393; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5, PRPK, AMPK, NUAK1 and ATM.
                     /evidence=ECO:0000269|PubMed:10570149,
                     ECO:0000269|PubMed:11554766, ECO:0000269|PubMed:15866171,
                     ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:17591690,
                     ECO:0000269|PubMed:17967874, ECO:0000269|PubMed:21317932,
                     ECO:0000269|PubMed:28842590; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          17..25
                     /region_name="TADI"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK1, VRK1 and VRK2.
                     /evidence=ECO:0000269|PubMed:10606744,
                     ECO:0000269|PubMed:10951572, ECO:0000269|PubMed:16704422,
                     ECO:0000269|PubMed:31527692; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CHEK2, CK1 and PLK3.
                     /evidence=ECO:0000269|PubMed:10570149,
                     ECO:0000269|PubMed:11447225, ECO:0000269|PubMed:11551930,
                     ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:20041275;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5 and CDK7.
                     /evidence=ECO:0000269|PubMed:17591690,
                     ECO:0000269|PubMed:9372954; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          35..59
                     /region_name="TAD2"
                     /note="Transactivation domain 2; pfam18521"
                     /db_xref="CDD:375947"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK5.
                     /evidence=ECO:0000269|PubMed:17254968; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5, DYRK2, HIPK2 and PKC/PRKCG.
                     /evidence=ECO:0000269|PubMed:11740489,
                     ECO:0000269|PubMed:11780126, ECO:0000269|PubMed:16377624,
                     ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:17591690;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          48..56
                     /region_name="TADII"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          50..96
                     /region_name="Disordered.
                     /evidence=ECO:0000269|PubMed:31953488"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by TAF1 and GRK5.
                     /evidence=ECO:0000269|PubMed:15053879,
                     ECO:0000269|PubMed:20124405; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          66..110
                     /region_name="Interaction with WWOX"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          100..300
                     /region_name="Required for interaction with ZNF385A.
                     /evidence=ECO:0000269|PubMed:17719541"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          109..288
                     /region_name="P53"
                     /note="P53 DNA-binding domain; cd08367"
                     /db_xref="CDD:176262"
     Region          113..236
                     /region_name="Required for interaction with FBXO42.
                     /evidence=ECO:0000269|PubMed:19509332"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          116..292
                     /region_name="Interaction with AXIN1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            120
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000269|PubMed:16793544,
                     ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            120
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:17189187,
                     ECO:0000269|PubMed:19854137, ECO:0000269|PubMed:23431171;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            order(176,179,238,242)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:176262"
     Site            order(177..179,181)
                     /site_type="other"
                     /note="dimerization site [polypeptide binding]"
                     /db_xref="CDD:176262"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB.
                     /evidence=ECO:0000269|PubMed:20959462; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            order(239,241,248,273,275..277,280)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176262"
     Region          241..248
                     /region_name="Interaction with the 53BP2 SH3 domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          256..294
                     /region_name="Interaction with E4F1.
                     /evidence=ECO:0000269|PubMed:10644996"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB.
                     /evidence=ECO:0000269|PubMed:20959462; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          273..280
                     /region_name="Interaction with DNA"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          282..325
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AURKB.
                     /evidence=ECO:0000269|PubMed:20959462; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          305..321
                     /region_name="Bipartite nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            305
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:12724314; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKA, CDK1 and CDK2.
                     /evidence=ECO:0000269|PubMed:10884347,
                     ECO:0000269|PubMed:14702041; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            321
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P02340; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     CDS             1..341
                     /gene="TP53"
                     /gene_synonym="BCC7; BMFS5; LFS1; P53; TRP53"
                     /coded_by="NM_001407268.1:140..1165"
                     /note="isoform b is encoded by transcript variant 12"
                     /db_xref="GeneID:7157"
                     /db_xref="HGNC:HGNC:11998"
                     /db_xref="MIM:191170"
ORIGIN      
        1 meepqsdpsv epplsqetfs dlwkllpenn vlsplpsqam ddlmlspddi eqwftedpgp
       61 deaprmpeaa ppvapapaap tpaapapaps wplsssvpsq ktyqgsygfr lgflhsgtak
      121 svtctyspal nkmfcqlakt cpvqlwvdst pppgtrvram aiykqsqhmt evvrrcphhe
      181 rcsdsdglap pqhlirvegn lrveylddrn tfrhsvvvpy eppevgsdct tihynymcns
      241 scmggmnrrp iltiitleds sgnllgrnsf evrvcacpgr drrteeenlr kkgephhelp
      301 pgstkralpn ntssspqpkk kpldgeyftl qdqtsfqken c
//
LOCUS       NP_001424216            1070 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            beta isoform isoform 1 [Homo sapiens].
ACCESSION   NP_001424216 XP_011511197 XP_054202824
VERSION     NP_001424216.1
DBSOURCE    REFSEQ: accession NM_001437287.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Liu,L., Feng,X., Fan,C., Kong,D., Feng,X., Sun,C., Xu,Y., Li,B.,
            Jiang,Y. and Zheng,C.
  TITLE     PDCD4 interacting with PIK3CB and CTSZ promotes the apoptosis of
            multiple myeloma cells
  JOURNAL   FASEB J 38 (16), e70024 (2024)
   PUBMED   39190024
  REMARK    GeneRIF: PDCD4 interacting with PIK3CB and CTSZ promotes the
            apoptosis of multiple myeloma cells.
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Liu,G., Hou,Y., Jin,X., Zhang,Y., Sun,C., Huang,C., Ren,Y., Gao,J.,
            Wang,X. and Jiang,X.
  TITLE     PI3K/HSCB axis facilitates FOG1 nuclear translocation to promote
            erythropoiesis and megakaryopoiesis
  JOURNAL   Elife 13, 95815 (2024)
   PUBMED   38757931
  REMARK    GeneRIF: PI3K/HSCB axis facilitates FOG1 nuclear translocation to
            promote erythropoiesis and megakaryopoiesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1070)
  AUTHORS   Duewell,B.R., Wilson,N.E., Bailey,G.M., Peabody,S.E. and
            Hansen,S.D.
  TITLE     Molecular dissection of PI3Kbeta synergistic activation by receptor
            tyrosine kinases, GbetaGgamma, and Rho-family GTPases
  JOURNAL   Elife 12, 88991 (2024)
   PUBMED   38713746
  REMARK    GeneRIF: Molecular dissection of PI3Kbeta synergistic activation by
            receptor tyrosine kinases, GbetaGgamma, and Rho-family GTPases.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1070)
  AUTHORS   Xu,W., Chen,Y., Zhang,Z., Jiang,Y. and Wang,Z.
  TITLE     Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma
  JOURNAL   Med Oncol 40 (8), 221 (2023)
   PUBMED   37402056
  REMARK    GeneRIF: Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1070)
  AUTHORS   Milani,D., Mazzoni,M., Borgatti,P., Zauli,G., Cantley,L. and
            Capitani,S.
  TITLE     Extracellular human immunodeficiency virus type-1 Tat protein
            activates phosphatidylinositol 3-kinase in PC12 neuronal cells
  JOURNAL   J Biol Chem 271 (38), 22961-22964 (1996)
   PUBMED   8798481
REFERENCE   7  (residues 1 to 1070)
  AUTHORS   Bonnefoy-Berard,N., Liu,Y.C., von Willebrand,M., Sung,A., Elly,C.,
            Mustelin,T., Yoshida,H., Ishizaka,K. and Altman,A.
  TITLE     Inhibition of phosphatidylinositol 3-kinase activity by association
            with 14-3-3 proteins in T cells
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10142-10146 (1995)
   PUBMED   7479742
REFERENCE   8  (residues 1 to 1070)
  AUTHORS   Hu,P. and Schlessinger,J.
  TITLE     Direct association of p110 beta phosphatidylinositol 3-kinase with
            p85 is mediated by an N-terminal fragment of p110 beta
  JOURNAL   Mol Cell Biol 14 (4), 2577-2583 (1994)
   PUBMED   8139559
REFERENCE   9  (residues 1 to 1070)
  AUTHORS   Hu,P., Mondino,A., Skolnik,E.Y. and Schlessinger,J.
  TITLE     Cloning of a novel, ubiquitously expressed human
            phosphatidylinositol 3-kinase and identification of its binding
            site on p85
  JOURNAL   Mol Cell Biol 13 (12), 7677-7688 (1993)
   PUBMED   8246984
REFERENCE   10 (residues 1 to 1070)
  AUTHORS   Carpenter,C.L., Duckworth,B.C., Auger,K.R., Cohen,B.,
            Schaffhausen,B.S. and Cantley,L.C.
  TITLE     Purification and characterization of phosphoinositide 3-kinase from
            rat liver
  JOURNAL   J Biol Chem 265 (32), 19704-19711 (1990)
   PUBMED   2174051
  REMARK    GeneRIF: This paper reports the first purification of a
            phosphoinositide 3-kinase and shows that the protein is a
            heterodimer of an 85 kd regulatory subunit that mediates binding to
            phosphorylated proteins and a 110 kd catalytic subunit.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC067728.25, AC117389.5 and AC020890.22.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_011511197.1, XP_054202824.1.
            
            Summary: This gene encodes an isoform of the catalytic subunit of
            phosphoinositide 3-kinase (PI3K). These kinases are important in
            signaling pathways involving receptors on the outer membrane of
            eukaryotic cells and are named for their catalytic subunit. The
            encoded protein is the catalytic subunit for PI3Kbeta (PI3KB).
            PI3KB has been shown to be part of the activation pathway in
            neutrophils which have bound immune complexes at sites of injury or
            infection. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853559.23779.1,
                                           SRR18074969.3655695.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..1070
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit beta isoform isoform 1"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.1.153"
                     /note="PI3-kinase p110 subunit beta; PtdIns-3-kinase p110;
                     PI3K-beta; PI3-kinase subunit beta; ptdIns-3-kinase
                     subunit beta; ptdIns-3-kinase subunit p110-beta;
                     phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa
                     catalytic subunit beta; serine/threonine protein kinase
                     PIK3CB; phosphoinositide-3-kinase, catalytic, beta
                     polypeptide"
                     /calculated_mol_wt=122632
     Region          41..118
                     /region_name="PI3K_p85B"
                     /note="PI3-kinase family, p85-binding domain; smart00143"
                     /db_xref="CDD:197539"
     Region          180..288
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, Ras-binding domain; smart00144"
                     /db_xref="CDD:197540"
     Region          324..501
                     /region_name="C2_PI3K_class_I_beta_delta"
                     /note="C2 domain present in class I beta and delta
                     phosphatidylinositol 3-kinases (PI3Ks); cd08693"
                     /db_xref="CDD:176075"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI9; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     Region          410..418
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Region          532..702
                     /region_name="PI3Ka_I"
                     /note="Phosphoinositide 3-kinase (PI3K) class I, accessory
                     domain; PIK domain is conserved in all PI3 and
                     PI4-kinases. Its role is unclear but it has been suggested
                     to be involved in substrate presentation. In general, PI3K
                     class I prefer phosphoinositol (4,5)...; cd00872"
                     /db_xref="CDD:238444"
     Region          706..1067
                     /region_name="PI3Kc_IA_beta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase beta; cd05173"
                     /db_xref="CDD:270717"
     Region          778..784
                     /region_name="G-loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(779,781..783,785,803,805,808,839,851..854,859,862,
                     924,926,936..937)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270717"
     Site            order(846..847,874..875,878,948..949,962,965,973..976,979,
                     1046,1049..1050,1052..1053)
                     /site_type="other"
                     /note="regulatory subunit interface [polypeptide binding]"
                     /db_xref="CDD:270717"
     Site            893
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270717"
     Region          916..924
                     /region_name="Catalytic loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            916..924
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270717"
     Region          935..961
                     /region_name="Activation loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(937..950,956..961)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270717"
     Site            1070
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12502714; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     CDS             1..1070
                     /gene="PIK3CB"
                     /gene_synonym="P110BETA; PI3K; PI3KBETA; PIK3C1"
                     /coded_by="NM_001437287.1:423..3635"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="GeneID:5291"
                     /db_xref="HGNC:HGNC:8976"
                     /db_xref="MIM:602925"
ORIGIN      
        1 mcfsfimppa madildiwav dsqiasdgsi pvdfllptgi yiqlevprea tisyikqmlw
       61 kqvhnypmfn llmdidsymf acvnqtavye eledetrrlc dvrpflpvlk lvtrscdpge
      121 kldskigvli gkglhefdsl kdpevnefrr kmrkfseeki lslvglswmd wlkqtyppeh
      181 epsipenled klyggkliva vhfencqdvf sfqvspnmnp ikvnelaiqk rltihgkede
      241 vspydyvlqv sgrveyvfgd hpliqfqyir ncvmnralph filvecckik kmyeqemiai
      301 eaainrnssn lplplppkkt riishvwenn npfqivlvkg nklnteetvk vhvraglfhg
      361 tellcktivs sevsgkndhi wneplefdin icdlprmarl cfavyavldk vktkkstkti
      421 npskyqtirk agkvhypvaw vntmvfdfkg qlrtgdiilh swssfpdele emlnpmgtvq
      481 tnpytenata lhvkfpenkk qpyyyppfdk iiekaaeias sdsanvssrg gkkflpvlke
      541 ildrdplsql cenemdliwt lrqdcreifp qslpklllsi kwnkledvaq lqallqiwpk
      601 lpprealell dfnypdqyvr eyavgclrqm sdeelsqyll qlvqvlkyep fldcalsrfl
      661 leralgnrri gqflfwhlrs evhipavsvq fgvileaycr gsvghmkvls kqvealnklk
      721 tlnsliklna vklnrakgke amhtclkqsa yrealsdlqs plnpcvilse lyvekckymd
      781 skmkplwlvy nnkvfgedsv gvifkngddl rqdmltlqml rlmdllwkea gldlrmlpyg
      841 clatgdrsgl ievvstseti adiqlnssnv aaaaafnkda llnwlkeyns gddldraiee
      901 ftlscagycv asyvlgigdr hsdnimvkkt gqlfhidfgh ilgnfkskfg ikrervpfil
      961 tydfihviqq gktgntekfg rfrqcceday lilrrhgnlf itlfalmlta glpeltsvkd
     1021 iqylkdslal gkseeealkq fkqkfdealr eswttkvnwm ahtvrkdyrs
//
LOCUS       NP_001427716            1210 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphorylase b kinase regulatory subunit alpha, skeletal muscle
            isoform isoform 2 [Homo sapiens].
ACCESSION   NP_001427716 XP_047298117 XP_054183172
VERSION     NP_001427716.1
DBSOURCE    REFSEQ: accession NM_001440787.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1210)
  AUTHORS   Yang,X., Zhu,M., Lu,X., Wang,Y. and Xiao,J.
  TITLE     Architecture and activation of human muscle phosphorylase kinase
  JOURNAL   Nat Commun 15 (1), 2719 (2024)
   PUBMED   38548794
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1210)
  AUTHORS   Bisciglia,M., Froissart,R., Bedat-Millet,A.L., Romero,N.B.,
            Pettazzoni,M., Hogrel,J.Y., Petit,F.M. and Stojkovic,T.
  TITLE     A novel PHKA1 mutation associating myopathy and cognitive
            impairment: Expanding the spectrum of phosphorylase kinase b (PhK)
            deficiency
  JOURNAL   J Neurol Sci 424, 117391 (2021)
   PUBMED   33799212
  REMARK    GeneRIF: A novel PHKA1 mutation associating myopathy and cognitive
            impairment: Expanding the spectrum of phosphorylase kinase b (PhK)
            deficiency.
REFERENCE   3  (residues 1 to 1210)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1210)
  AUTHORS   Preisler,N., Orngreen,M.C., Echaniz-Laguna,A., Laforet,P.,
            Lonsdorfer-Wolf,E., Doutreleau,S., Geny,B., Akman,H.O., Dimauro,S.
            and Vissing,J.
  TITLE     Muscle phosphorylase kinase deficiency: a neutral metabolic variant
            or a disease?
  JOURNAL   Neurology 78 (4), 265-268 (2012)
   PUBMED   22238410
  REMARK    GeneRIF: muscle PHKA deficiency may present as an almost
            asymptomatic condition, despite a mild impairment of muscle
REFERENCE   5  (residues 1 to 1210)
  AUTHORS   Echaniz-Laguna,A., Akman,H.O., Mohr,M., Tranchant,C.,
            Talmant-Verbist,V., Rolland,M.O. and Dimauro,S.
  TITLE     Muscle phosphorylase b kinase deficiency revisited
  JOURNAL   Neuromuscul Disord 20 (2), 125-127 (2010)
   PUBMED   20080404
REFERENCE   6  (residues 1 to 1210)
  AUTHORS   Gossen,M., Wullrich,A. and Kilimann,M.W.
  TITLE     Dinucleotide repeat polymorphism within the PHKA1 gene at Xq12-q13
  JOURNAL   Hum Genet 95 (4), 469-470 (1995)
   PUBMED   7705849
REFERENCE   7  (residues 1 to 1210)
  AUTHORS   Wehner,M., Clemens,P.R., Engel,A.G. and Kilimann,M.W.
  TITLE     Human muscle glycogenosis due to phosphorylase kinase deficiency
            associated with a nonsense mutation in the muscle isoform of the
            alpha subunit
  JOURNAL   Hum Mol Genet 3 (11), 1983-1987 (1994)
   PUBMED   7874115
REFERENCE   8  (residues 1 to 1210)
  AUTHORS   Herbert,M., Goldstein,J.L., Rehder,C., Austin,S., Kishnani,P.S. and
            Bali,D.S.
  TITLE     Phosphorylase Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21634085
REFERENCE   9  (residues 1 to 1210)
  AUTHORS   Meyer,H.E., Meyer,G.F., Dirks,H. and Heilmeyer,L.M. Jr.
  TITLE     Localization of phosphoserine residues in the alpha subunit of
            rabbit skeletal muscle phosphorylase kinase
  JOURNAL   Eur J Biochem 188 (2), 367-376 (1990)
   PUBMED   2108025
REFERENCE   10 (residues 1 to 1210)
  AUTHORS   Francke,U., Darras,B.T., Zander,N.F. and Kilimann,M.W.
  TITLE     Assignment of human genes for phosphorylase kinase subunits alpha
            (PHKA) to Xq12-q13 and beta (PHKB) to 16q12-q13
  JOURNAL   Am J Hum Genet 45 (2), 276-282 (1989)
   PUBMED   2757032
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC240504.3, BX295541.1 and
            BX295542.1.
            
            On or before May 29, 2025 this sequence version replaced
            XP_047298117.1, XP_054183172.1.
            
            Summary: Phosphorylase kinase is a polymer of 16 subunits, four
            each of alpha, beta, gamma and delta. The alpha subunit includes
            the skeletal muscle and hepatic isoforms, and the skeletal muscle
            isoform is encoded by this gene. The beta subunit is the same in
            both the muscle and hepatic isoforms, and encoded by one gene. The
            gamma subunit also includes the skeletal muscle and hepatic
            isoforms, which are encoded by two different genes. The delta
            subunit is a calmodulin and can be encoded by three different
            genes. The gamma subunits contain the active site of the enzyme,
            whereas the alpha and beta subunits have regulatory functions
            controlled by phosphorylation. The delta subunit mediates the
            dependence of the enzyme on calcium concentration. Mutations in
            this gene cause glycogen storage disease type 9D, also known as
            X-linked muscle glycogenosis. Alternatively spliced transcript
            variants encoding different isoforms have been identified in this
            gene. A pseudogene has been found on chromosome 1.[provided by
            RefSeq, Feb 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.100538.1,
                                           SRR18074969.254853.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..1210
                     /product="phosphorylase b kinase regulatory subunit alpha,
                     skeletal muscle isoform isoform 2"
                     /EC_number="2.7.11.19"
                     /note="phosphorylase kinase, alpha 1 (muscle), muscle
                     glycogenosis; phosphorylase kinase alpha M subunit"
                     /calculated_mol_wt=135678
     Region          8..>439
                     /region_name="Glyco_hydro_15"
                     /note="Glycosyl hydrolases family 15; pfam00723"
                     /db_xref="CDD:395586"
     Site            629
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64649; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Site            735
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Site            758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Region          <804..922
                     /region_name="Bac_rhamnosid6H"
                     /note="Bacterial alpha-L-rhamnosidase 6 hairpin
                     glycosidase domain; cl46875"
                     /db_xref="CDD:481215"
     Region          810..840
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P46020.2)"
     Region          933..>1121
                     /region_name="KPBB_C"
                     /note="Phosphorylase b kinase C-terminal domain;
                     pfam19292"
                     /db_xref="CDD:437124"
     Site            972
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46020.2)"
     Site            981
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Site            985
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46020.2)"
     Site            1007
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P18688; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Region          1033..1073
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P46020.2)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64649; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     CDS             1..1210
                     /gene="PHKA1"
                     /gene_synonym="PHKA"
                     /coded_by="NM_001440787.1:318..3950"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:5255"
                     /db_xref="HGNC:HGNC:8925"
                     /db_xref="MIM:311870"
ORIGIN      
        1 mrsrsnsgvr ldgyarlvqq tilchqnpvt gllpasydqk dawvrdnvys ilavwglgla
       61 yrknadrded kakayeleqs vvklmrgllh cmirqvdkve sfkysqstkd slhakyntkt
      121 catvvgddqw ghlqldatsv yllflaqmta sglhiihsld evnfiqnlvf yieaayktad
      181 fgiwergdkt nqgiselnas svgmakaale aldeldlfgv kggpqsvihv ladevqhcqs
      241 ilnsllpras tskevdasll svvsfpafav edsqlveltk qeiitklqgr ygccrflrdg
      301 yktpkedpnr lyyepaelkl feniecewpl fwtyfildgv fsgnaeqvqe ykealeavli
      361 kgkngvpllp elysvppdrv deeyqnphtv drvpmgklph mwgqslyilg slmaegflap
      421 geidplnrrf stvpkpdvvv qvsilaetee iktilkdkgi yvetiaevyp irvqparils
      481 hiysslgcnn rmklsgrpyr hmgvlgtskl ydirktiftf tpqfidqqqf ylaldnkmiv
      541 emlrtdlsyl csrwrmtgqp titfpishsm ldedgtslns silaalrkmq dgyfggarvq
      601 tgklsefltt sccthlsfmd pgpegklyse dyddnydyle sgnwmndyds tsharcgdev
      661 aryldhllah taphpklapt sqkggldrfq aavqttcdlm slvtkakelh vqnvhmylpt
      721 klfqasrpsf nlldsphprq enqvpsvrve ihlprdqsge vdfkalvlql ketsslqeqa
      781 dilymlytmk gpdwntelyn ersatvrell telygkvgei rhwgliryis gilrkkveal
      841 deactdllsh qkhltvglpp eprektisap lpyealtqli deasegdmsi siltqeimvy
      901 lamymrtqpg lfaemfrlri gliiqvmate lahslrcsae eateglmnls psamknllhh
      961 ilsgkefgve rsvrptdsnv spaisiheig avgatktert gimqlkseik qspgtsmtps
     1021 sgsfpsaydq qsskdsrqgq wqrrrrldga lnrvpvgfyq kvwkvlqkch glsvegfvlp
     1081 ssttremtpg eikfsvhves vlnrvpqpey rqllveailv ltmladieih sigsiiavek
     1141 ivhiandlfl qeqktlgadd tmlakdpasg ictllydsap sgrfgtmtyl skaaatyvqe
     1201 flphsicamq
//
LOCUS       NP_001427335             898 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001427335
VERSION     NP_001427335.1
DBSOURCE    REFSEQ: accession NM_001440406.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 898)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 898)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 898)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 898)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 898)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 898)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 898)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3, AP004147.3 and
            AP001929.5.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.635391.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465404 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..898
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     4 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=98772
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..402
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Region          415..727
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     CDS             1..898
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440406.1:296..2992"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 8"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk aaelgmvsay
      241 ytyiftnlef slqrmdslvd drvnilgfsi fnqshaffqe faqslnqswq encdhvpftg
      301 palssallfd avyavvtavq elnrsqeigv kplscgsaqi wqhgtslmny lrmveleglt
      361 ghiefnskgq rsnyalkilq ftrngfrqig qwhvaeglsm dshlyasnis dtlfnttlvv
      421 ttilenpylm lkgnhqemeg ndryegfcvd mlkelaeilr fnykirlvgd gvygvpeang
      481 twtgmvgeli arkadlavag ltitaerekv idfskpfmtl gisilyrvhm grkpgyfsfl
      541 dpfspgvwlf mllaylavsc vlflvarwaf tliiissyta nlaafltvqr mdvpiesvdd
      601 ladqtaieyg tihggssmtf fqnsryqtyq rmwnymyskq psvfvkstee giarvlnsny
      661 afllestmne yyrqrncnlt qigglldtkg ygigmpvgsv frdefdlail qlqennrlei
      721 lkrkwweggk cpkeedhrak glgmeniggi fvvlicgliv aifmamlefl wtlrhseate
      781 vsvcqemvte lrsiilcqds ihprrrraav ppprppipee rrprgtatls ngklcgagep
      841 dqlaqrlaqe aalvargcth irvcpecrrf qglrarpspa rseeslewek ttnssepe
//
LOCUS       NP_001393927             460 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform L [Homo sapiens].
ACCESSION   NP_001393927
VERSION     NP_001393927.1
DBSOURCE    REFSEQ: accession NM_001406998.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 460)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 460)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 460)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 460)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 460)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 460)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 460)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 460)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2051981.1,
                                           SRR14243140.5649968.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2146982
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..460
                     /product="lamin isoform L"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=52172
     Region          17..274
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          322..429
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     CDS             1..460
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406998.1:35..1417"
                     /note="isoform L is encoded by transcript variant 23"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 mgnsegcntk kegdliaaqa rlkdlealln skeaalstal sekrtlegel hdlrgqvakl
       61 eaalgeakkq lqdemlrrvd aenrlqtmke eldfqkniys eelretkrrh etrlveidng
      121 kqrefesrla dalqelraqh edqveqykke lektysakld narqsaerns nlvgaaheel
      181 qqsriridsl saqlsqlqkq laakeaklrd ledslarerd tsrrllaeke remaemrarm
      241 qqqldeyqel ldiklaldme ihayrklleg eeerlrlsps ptsqrsrgra sshssqtqgg
      301 gsvtkkrkle stesrssfsq hartsgrvav eevdeegkfv rlrnksnedq smgnwqikrq
      361 ngddplltyr fppkftlkag qvvtiwaaga gathspptdl vwkaqntwgc gnslrtalin
      421 stgeevamrk lvrsvtvved dededgddll hhhhvsgsrr
//
LOCUS       NP_001397880            1816 aa            linear   PRI 21-NOV-2025
DEFINITION  afadin isoform 9 [Homo sapiens].
ACCESSION   NP_001397880 XP_016866373
VERSION     NP_001397880.1
DBSOURCE    REFSEQ: accession NM_001410951.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1816)
  AUTHORS   Serafin,D.S., Harris,N.R., Balint,L., Douglas,E.S. and Caron,K.M.
  TITLE     Proximity interactome of lymphatic VE-cadherin reveals mechanisms
            of junctional remodeling and reelin secretion
  JOURNAL   Nat Commun 15 (1), 7734 (2024)
   PUBMED   39232006
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1816)
  AUTHORS   Awotoye,W., Mossey,P.A., Hetmanski,J.B., Gowans,L.J.J.,
            Eshete,M.A., Adeyemo,W.L., Alade,A., Zeng,E., Adamson,O., James,O.,
            Fashina,A., Ogunlewe,M.O., Naicker,T., Adeleke,C., Busch,T., Li,M.,
            Petrin,A., Oladayo,A., Kayali,S., Olotu,J., Sule,V., Hassan,M.,
            Pape,J., Aladenika,E.T., Donkor,P., Arthur,F.K.N., Obiri-Yeboah,S.,
            Sabbah,D.K., Agbenorku,P., Ray,D., Plange-Rhule,G., Oti,A.A.,
            Albokhari,D., Sobreira,N., Dunnwald,M., Beaty,T.H., Taub,M.,
            Marazita,M.L., Adeyemo,A.A., Murray,J.C. and Butali,A.
  TITLE     Damaging Mutations in AFDN Contribute to Risk of Nonsyndromic Cleft
            Lip With or Without Cleft Palate
  JOURNAL   Cleft Palate Craniofac J 61 (4), 697-705 (2024)
   PUBMED   36384317
  REMARK    GeneRIF: Damaging Mutations in AFDN Contribute to Risk of
            Nonsyndromic Cleft Lip With or Without Cleft Palate.
REFERENCE   3  (residues 1 to 1816)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1816)
  AUTHORS   Lorger,M. and Moelling,K.
  TITLE     Regulation of epithelial wound closure and intercellular adhesion
            by interaction of AF6 with actin cytoskeleton
  JOURNAL   J Cell Sci 119 (Pt 16), 3385-3398 (2006)
   PUBMED   16882694
REFERENCE   5  (residues 1 to 1816)
  AUTHORS   Saito,S., Matsushima,M., Shirahama,S., Minaguchi,T., Kanamori,Y.,
            Minami,M. and Nakamura,Y.
  TITLE     Complete genomic structure DNA polymorphisms, and alternative
            splicing of the human AF-6 gene
  JOURNAL   DNA Res 5 (2), 115-120 (1998)
   PUBMED   9679199
REFERENCE   6  (residues 1 to 1816)
  AUTHORS   Mandai,K., Nakanishi,H., Satoh,A., Obaishi,H., Wada,M.,
            Nishioka,H., Itoh,M., Mizoguchi,A., Aoki,T., Fujimoto,T.,
            Matsuda,Y., Tsukita,S. and Takai,Y.
  TITLE     Afadin: A novel actin filament-binding protein with one PDZ domain
            localized at cadherin-based cell-to-cell adherens junction
  JOURNAL   J Cell Biol 139 (2), 517-528 (1997)
   PUBMED   9334353
  REMARK    Erratum:[J Cell Biol 1997 Nov 17;139(4):1060]
REFERENCE   7  (residues 1 to 1816)
  AUTHORS   Joh,T., Yamamoto,K., Kagami,Y., Kakuda,H., Sato,T., Yamamoto,T.,
            Takahashi,T., Ueda,R., Kaibuchi,K. and Seto,M.
  TITLE     Chimeric MLL products with a Ras binding cytoplasmic protein AF6
            involved in t(6;11) (q27;q23) leukemia localize in the nucleus
  JOURNAL   Oncogene 15 (14), 1681-1687 (1997)
   PUBMED   9349501
REFERENCE   8  (residues 1 to 1816)
  AUTHORS   Tanabe,S., Zeleznik-Le,N.J., Kobayashi,H., Vignon,C., Espinosa,R.
            3rd, LeBeau,M.M., Thirman,M.J. and Rowley,J.D.
  TITLE     Analysis of the t(6;11)(q27;q23) in leukemia shows a consistent
            breakpoint in AF6 in three patients and in the ML-2 cell line
  JOURNAL   Genes Chromosomes Cancer 15 (4), 206-216 (1996)
   PUBMED   8703846
REFERENCE   9  (residues 1 to 1816)
  AUTHORS   Saha,V., Lillington,D.M., Shelling,A.N., Chaplin,T., Yaspo,M.L.,
            Ganesan,T.S. and Young,B.D.
  TITLE     AF6 gene on chromosome band 6q27 maps distal to the minimal region
            of deletion in epithelial ovarian cancer
  JOURNAL   Genes Chromosomes Cancer 14 (3), 220-222 (1995)
   PUBMED   8589040
REFERENCE   10 (residues 1 to 1816)
  AUTHORS   Prasad,R., Gu,Y., Alder,H., Nakamura,T., Canaani,O., Saito,H.,
            Huebner,K., Gale,R.P., Nowell,P.C., Kuriyama,K. et al.
  TITLE     Cloning of the ALL-1 fusion partner, the AF-6 gene, involved in
            acute myeloid leukemias with the t(6;11) chromosome translocation
  JOURNAL   Cancer Res 53 (23), 5624-5628 (1993)
   PUBMED   8242616
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL009178.4, AL731868.5 and
            AL049698.3.
            
            On Aug 18, 2022 this sequence version replaced XP_016866373.1.
            
            Summary: This gene encodes a multi-domain protein involved in
            signaling and organization of cell junctions during embryogenesis.
            It has also been identified as the fusion partner of acute
            lymphoblastic leukemia (ALL-1) gene, involved in acute myeloid
            leukemias with t(6;11)(q27;q23) translocation. Alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene, however, not all have been fully
            characterized.[provided by RefSeq, May 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1801923.1,
                                           SRR14038193.3912682.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1816
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q27"
     Protein         1..1816
                     /product="afadin isoform 9"
                     /note="myeloid/lymphoid or mixed-lineage leukemia
                     (trithorax homolog, Drosophila); translocated to, 4;
                     myeloid/lymphoid or mixed-lineage leukemia; translocated
                     to, 4; ALL1-fused gene from chromosome 6 protein; protein
                     AF-6"
                     /calculated_mol_wt=205515
     Region          20..131
                     /region_name="RA1_Afadin"
                     /note="Ras-associating (RA) domain 1 found in Afadin;
                     cd01782"
                     /db_xref="CDD:340480"
     Site            26
                     /site_type="other"
                     /note="Breakpoint for translocation to form
                     KMT2A/MLL1-AFDN; propagated from UniProtKB/Swiss-Prot
                     (P55196.3)"
     Site            order(44,58,78)
                     /site_type="other"
                     /note="RA - Ras interaction site [polypeptide binding]"
                     /db_xref="CDD:340480"
     Region          128..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55196.3)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Region          247..347
                     /region_name="RA2_Afadin"
                     /note="Ras-associating (RA) domain 2 found in Afadin;
                     cd01781"
                     /db_xref="CDD:340479"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Region          349..378
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55196.3)"
     Region          384..487
                     /region_name="FHA_AFDN"
                     /note="forkhead associated (FHA) domain found in afadin
                     and similar proteins; cd22711"
                     /db_xref="CDD:438763"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35889; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Region          519..580
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55196.3)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            574
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Region          596..924
                     /region_name="Myo5p-like_CBD_afadin"
                     /note="cargo binding domain of myosin 5-like of afadin;
                     cd15471"
                     /db_xref="CDD:271255"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Region          997..1084
                     /region_name="PDZ_AFDN-like"
                     /note="PDZ domain of afadin (AFDN), and related domains;
                     cd06789"
                     /db_xref="CDD:467251"
     Site            order(1009..1015,1030,1033,1063,1067,1070..1071)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467251"
     Site            1075
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Region          1099..1215
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55196.3)"
     Site            1099
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZQ1; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35889; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZQ1; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1203
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1224
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Region          1227..1465
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55196.3)"
     Site            1230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1322
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Region          <1454..1672
                     /region_name="DUF4670"
                     /note="Domain of unknown function (DUF4670); pfam15709"
                     /db_xref="CDD:464815"
     Region          1493..1520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55196.3)"
     Site            1493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1504
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Region          1561..1816
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55196.3)"
     Site            1688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZQ1; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1771
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     Site            1791
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P55196.3)"
     Site            1799
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZQ1; propagated from
                     UniProtKB/Swiss-Prot (P55196.3)"
     CDS             1..1816
                     /gene="AFDN"
                     /gene_synonym="AF6; l-afadin; MLL-AF6; MLLT4"
                     /coded_by="NM_001410951.1:223..5673"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS94035.1"
                     /db_xref="GeneID:4301"
                     /db_xref="HGNC:HGNC:7137"
                     /db_xref="MIM:159559"
ORIGIN      
        1 msaggrdeer rkladiihhw nanrldlfei sqptedlefh gvmrfyfqdk aagnfatkci
       61 rvsstattqd vietlaekfr pdmrmlsspk yslyevhvsg errldidekp lvvqlnwnkd
      121 dregrfvlkn endaippkka qsngpekqek egviqnfkrt lskkekkekk krekealrqa
      181 sdkddrpfqg edvensrlaa evykdmpets ftrtisnpev vmkrrrqqkl ekrmqefrss
      241 dgrpdsggtl riyadslkpn ipyktillst tdpadfavae alekygleke npkdyciarv
      301 mlppgaqhsd ekgakeiild ddecplqifr ewpsdkgilv fqlkrrppdh ipkktkkhle
      361 gktpkgkera dgsgygstlp peklpylvel spdgsdsrdk pklyrlqlsv tevgtekldd
      421 nsiqlfgpgi qphhcdltnm dgvvtvtprs mdaetyvegq risettmlqs gmkvqfgash
      481 vfkfvdpsqd halakrsvdg glmvkgprhk pgivqettfd lggdihsgta lptsksttrl
      541 dsdrvssass taergmvkpm irveqqpdyr rqesrtqdas gpelilpasi efressedsf
      601 lsaiinytns stvhfklspt yvlymacryv lsnqyrpdis pterthkvia vvnkmvsmme
      661 gviqevdqvd qkqkniagal afwmanasel lnfikqdrdl sritldaqdv lahlvqmafk
      721 ylvhclqsel nnympafldd peenslqrpk iddvlhtltg amsllrrcrv naaltiqlfs
      781 qlfhfinmwl fnrlvtdpds glcshywgai irqqlghiea waekqglela adchlsrivq
      841 attlltmdky apddipnins tcfklnslql qallqnyhca pdepfiptdl ienvvtvaen
      901 tadelarsdg revqleedpd lqlpfllped gyscdvvrni pnglqefldp lcqrgfcrli
      961 phtrspgtwt iyfegadyes hllrentela qplrkepeii tvtlkkqngm glsivaakga
     1021 gqdklgiyvk svvkggaadv dgrlaagdql lsvdgrslvg lsqeraaelm trtssvvtle
     1081 vakqgaiyhg latllnqpsp mmqrisdrrg sgkprpkseg felynnstqn gspespqlpw
     1141 aeysepkklp gddrlmknra dhrsspnvan qppspggksa yasgttakit svstgnlcte
     1201 eqtppprpea ypiptqtytr eyftfpasks qdrmappqnq wpnyeekphm htdsnhssia
     1261 iqrvtrsqee lredkayqle rhrieaamdr ksdsdmwinq sssldsstss qehlnhssks
     1321 vtpastltks gpgrwktpaa ipatpvavsq pirtdlpppp ppppvhyagd fdgmsmdlpl
     1381 ppppsanqig lpsaqvaaae rrkreehqrw yekekarlee ererkrreqe rklgqmrtqs
     1441 lnpapfsplt aqqmkpekps tlqrpqetvi relqpqqqpr tierrdlqyi tvskeelssg
     1501 dslspdpwkr dakeklekqq qmhivdmlsk eiqelqskpd rsaeesdrlr klmlewqfqk
     1561 rlqeskqkde ddeeeedddv dtmlimqrle aerrarlqde errrqqqlee mrkreaedra
     1621 rqeeerrrqe eertkrdaee krrqeegyys rleaerrrqh deaarrllep eapglcrppl
     1681 prdyeppsps papgappppp qrnasylktq vlspdslfta kfvayneeee eedcslagpn
     1741 sypgstgaav gahdacrdak ekrsksqdad spgssgapen ltfkerqrlf sqgqdvsnkv
     1801 kasrkltele nelntk
//
LOCUS       NP_001389617            1328 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 7 [Homo sapiens].
ACCESSION   NP_001389617 XP_047287316
VERSION     NP_001389617.1
DBSOURCE    REFSEQ: accession NM_001402688.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1328)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1328)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1328)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1328)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1328)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1328)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1328)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1328)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1328)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1328)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            On Apr 22, 2022 this sequence version replaced XP_047287316.1.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1791581.1,
                                           SRR14038194.1304754.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1328
                     /product="kinectin isoform 7"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=152768
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          316..>532
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          448..1268
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1328
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402688.1:303..4289"
                     /note="isoform 7 is encoded by transcript variant 13"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqdlkqeika
      841 lkeeignvql ekaqqlsits kvqelqnllk gkeeqmntmk avleekekdl antgkwlqdl
      901 qeeneslkah vqevaqhnlk eassasqfee leivlkeken elkrleamlk eresdlsskt
      961 qllqdvqden klfksqieql kqqnyqqass fppheellkv iserekeisg lwneldslkd
     1021 avehqrkknn erqqqveave leakevlkkl fpkvsvpsnl sygewlhgfe kkakecmagt
     1081 sgseevkvle hklkeademh tllqleceky ksvlaetegi lqklqrsveq eenkwkvkvd
     1141 eshktikqmq ssftsseqel erlrsenkdi enlrrerehl emelekaeme rstyvtevre
     1201 lkdlltelqk klddsyseav rqneelnllk aqlnetltkl rteqnerqkv agdlhkaqqs
     1261 leliqskivk aagdttvien sdvspetess eketmsvsln qtvtqlqqll qavnqqltke
     1321 kehyqvle
//
LOCUS       NP_001424543            1305 aa            linear   PRI 21-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4 gamma 3 isoform 16 [Homo
            sapiens].
ACCESSION   NP_001424543 XP_016858197
VERSION     NP_001424543.1
DBSOURCE    REFSEQ: accession NM_001437614.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1305)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1305)
  AUTHORS   Kang,J.Y., Wen,Z., Pan,D., Zhang,Y., Li,Q., Zhong,A., Yu,X.,
            Wu,Y.C., Chen,Y., Zhang,X., Kou,P.C., Geng,J., Wang,Y.Y., Hua,M.M.,
            Zong,R., Li,B., Shi,H.J., Li,D., Fu,X.D., Li,J., Nelson,D.L.,
            Guo,X., Zhou,Y., Gou,L.T., Huang,Y. and Liu,M.F.
  TITLE     LLPS of FXR1 drives spermiogenesis by activating translation of
            stored mRNAs
  JOURNAL   Science 377 (6607), eabj6647 (2022)
   PUBMED   35951695
REFERENCE   3  (residues 1 to 1305)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1305)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 1305)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1305)
  AUTHORS   Waskiewicz,A.J., Johnson,J.C., Penn,B., Mahalingam,M., Kimball,S.R.
            and Cooper,J.A.
  TITLE     Phosphorylation of the cap-binding protein eukaryotic translation
            initiation factor 4E by protein kinase Mnk1 in vivo
  JOURNAL   Mol Cell Biol 19 (3), 1871-1880 (1999)
   PUBMED   10022874
REFERENCE   7  (residues 1 to 1305)
  AUTHORS   Pyronnet,S., Imataka,H., Gingras,A.C., Fukunaga,R., Hunter,T. and
            Sonenberg,N.
  TITLE     Human eukaryotic translation initiation factor 4G (eIF4G) recruits
            mnk1 to phosphorylate eIF4E
  JOURNAL   EMBO J 18 (1), 270-279 (1999)
   PUBMED   9878069
REFERENCE   8  (residues 1 to 1305)
  AUTHORS   Gingras,A.C., Raught,B. and Sonenberg,N.
  TITLE     eIF4 initiation factors: effectors of mRNA recruitment to ribosomes
            and regulators of translation
  JOURNAL   Annu Rev Biochem 68, 913-963 (1999)
   PUBMED   10872469
  REMARK    Review article
REFERENCE   9  (residues 1 to 1305)
  AUTHORS   Imataka,H., Gradi,A. and Sonenberg,N.
  TITLE     A newly identified N-terminal amino acid sequence of human eIF4G
            binds poly(A)-binding protein and functions in poly(A)-dependent
            translation
  JOURNAL   EMBO J 17 (24), 7480-7489 (1998)
   PUBMED   9857202
REFERENCE   10 (residues 1 to 1305)
  AUTHORS   Gradi,A., Imataka,H., Svitkin,Y.V., Rom,E., Raught,B., Morino,S.
            and Sonenberg,N.
  TITLE     A novel functional human eukaryotic translation initiation factor
            4G
  JOURNAL   Mol Cell Biol 18 (1), 334-342 (1998)
   PUBMED   9418880
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031005.2, AL627311.16,
            AL358392.19 and AL606477.11.
            
            On Apr 7, 2025 this sequence version replaced XP_016858197.1.
            
            Summary: The protein encoded by this gene is thought to be part of
            the eIF4F protein complex, which is involved in mRNA cap
            recognition and transport of mRNAs to the ribosome. Interestingly,
            a microRNA (miR-520c-3p) has been found that negatively regulates
            synthesis of the encoded protein, and this leads to a global
            decrease in protein translation and cell proliferation. Therefore,
            this protein is a key component of the anti-tumor activity of
            miR-520c-3p. [provided by RefSeq, May 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2460210.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1305
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     Protein         1..1305
                     /product="eukaryotic translation initiation factor 4 gamma
                     3 isoform 16"
                     /note="eIF-4-gamma 3; eIF-4-gamma II"
                     /calculated_mol_wt=146740
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          <10..>232
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     Region          128..190
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          134..162
                     /region_name="PABPC1-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q80XI3; propagated from
                     UniProtKB/Swiss-Prot (O43432.2)"
     Region          475..703
                     /region_name="MIF4G"
                     /note="MIF4G domain; pfam02854"
                     /db_xref="CDD:397130"
     Region          942..1054
                     /region_name="MA3"
                     /note="MA3 domain; pfam02847"
                     /db_xref="CDD:397128"
     Region          1148..1276
                     /region_name="W2_eIF4G1_like"
                     /note="C-terminal W2 domain of eukaryotic translation
                     initiation factor 4 gamma 1 and similar proteins; cd11559"
                     /db_xref="CDD:211397"
     Region          <1255..1301
                     /region_name="W2"
                     /note="C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon;
                     cl17013"
                     /db_xref="CDD:473053"
     CDS             1..1305
                     /gene="EIF4G3"
                     /gene_synonym="eIF-4G 3; eIF4G 3; eIF4GII"
                     /coded_by="NM_001437614.1:632..4549"
                     /note="isoform 16 is encoded by transcript variant 21"
                     /db_xref="GeneID:8672"
                     /db_xref="HGNC:HGNC:3298"
                     /db_xref="MIM:603929"
ORIGIN      
        1 mnsqpqtrsp ffqrpqiqpp ratipnssps irpgaqtpta vyqanqhimm vnhlpmpypv
       61 pqgpqycipq yrhsgppyvg ppqqypvqpp gpgpfypgpg pgdfpnaygt pfypsqpvyq
      121 sapiivptqq qpppakrekk tirirdpnqg gkditeeims gggsrnptpp igrptstptp
      181 pqqlpsqvpe hspvvygtve sahlaastpv taasdqkqaq iaitvpktwk kpkdrtrtte
      241 emleaelelk aeeelsidkv leseqdkmsq gfhperdpsd lkkvkaveen geeaepvrng
      301 aesvsegegi dansgstdss gdgvtfpfkp eswkptdteg kkqydrefll dfqfmpaciq
      361 kpeglppisd vvldkinqpk lpmrtldpri lprgpdftpa fadfgrqtpg grgvpllnvg
      421 srrsqpgqrr eprkiitvsv kedvhlkkae nawkpsqkrd sqaddpenik tqelfrkvrs
      481 ilnkltpqmf nqlmkqvsgl tvdteerlkg vidlvfekai depsfsvaya nmcrclvtlk
      541 vpmadkpgnt vnfrklllnr cqkefekdka dddvfekkqk eleaasapee rtrlhdelee
      601 akdkarrrsi gnikfigelf klkmlteaim hdcvvkllkn hdeesleclc rllttigkdl
      661 dfekakprmd qyfnqmekiv kerktssrir fmlqdvidlr lcnwvsrrad qgpktieqih
      721 keakieeqee qrkvqqlmtk ekrrpgvqrv deggwntvqg aknsrvldps kflkitkpti
      781 dekiqlvpka qlgswgkgss ggakasetda lrssasslnr fsalqppaps gstpstpvef
      841 dsrrtltsrg smgrekndkp lpsatarpnt fmrggsskdl ldnqsqeeqr remletvkql
      901 tggvdverns teaernktre sakpeisams ahdkaalsee elerksksii deflhindfk
      961 eamqcveeln aqgllhvfvr vgvestlers qitrdhmgql lyqlvqsekl skqdffkgfs
     1021 etleladdma idiphiwlyl aelvtpmlke ggismrelti efskpllpvg ragvllseil
     1081 hllckqmshk kvgalwread lswkdflpeg edvhnflleq kldfiesdsp cssealskke
     1141 lsaeelykrl ekliiedkan deqifdwvea nldeiqmssp tflralmtav ckaaiiadss
     1201 tfrvdtavik qrvpillkyl dsdtekelqa lyalqasivk ldqpanllrm ffdclydeev
     1261 isedafykwe sskdpaeqng kgvalksvta fftwlreaee esedn
//
LOCUS       NP_001401590             499 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 2 isoform f [Homo sapiens].
ACCESSION   NP_001401590
VERSION     NP_001401590.1
DBSOURCE    REFSEQ: accession NM_001414661.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Jung,J.H., Lee,D., Ko,H.M. and Jang,H.J.
  TITLE     Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in Colorectal
            Cancer Cells by Activating p53
  JOURNAL   Biomolecules 11 (10), 1492 (2021)
   PUBMED   34680125
  REMARK    GeneRIF: Inhibition of CNOT2 Induces Apoptosis via MID1IP1 in
            Colorectal Cancer Cells by Activating p53.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Royer-Bertrand,B., Cisarova,K., Niel Butschi,F., Foletti,G.,
            Guinchat,V., Tran,C., Superti-Furga,A. and Good,J.M.
  TITLE     CNOT2 haploinsufficiency in a 40-year-old man with intellectual
            disability, autism, and seizures
  JOURNAL   Am J Med Genet A 185 (8), 2602-2606 (2021)
   PUBMED   34018673
  REMARK    GeneRIF: CNOT2 haploinsufficiency in a 40-year-old man with
            intellectual disability, autism, and seizures.
            Review article
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Jayne,S., Zwartjes,C.G., van Schaik,F.M. and Timmers,H.T.
  TITLE     Involvement of the SMRT/NCoR-HDAC3 complex in transcriptional
            repression by the CNOT2 subunit of the human Ccr4-Not complex
  JOURNAL   Biochem J 398 (3), 461-467 (2006)
   PUBMED   16712523
  REMARK    GeneRIF: This study shows that SMRT/NCoR-HDAC3 complex is a
            cofactor of CNOT2-mediated repression and suggests that
            transcriptional regulation by the Ccr4-Not complex involves
            regulation of chromatin modification.
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Winkler,G.S., Mulder,K.W., Bardwell,V.J., Kalkhoven,E. and
            Timmers,H.T.
  TITLE     Human Ccr4-Not complex is a ligand-dependent repressor of nuclear
            receptor-mediated transcription
  JOURNAL   EMBO J 25 (13), 3089-3099 (2006)
   PUBMED   16778766
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Shi,J. and Nelson,M.A.
  TITLE     The cyclin-dependent kinase 11 interacts with NOT2
  JOURNAL   Biochem Biophys Res Commun 334 (4), 1310-1316 (2005)
   PUBMED   16039607
  REMARK    GeneRIF: These findings suggest that CDK11 may contribute to
            apoptosis by regulating the activity of NOT2 independent of its
            kinase activity.
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Zwartjes,C.G., Jayne,S., van den Berg,D.L. and Timmers,H.T.
  TITLE     Repression of promoter activity by CNOT2, a subunit of the
            transcription regulatory Ccr4-not complex
  JOURNAL   J Biol Chem 279 (12), 10848-10854 (2004)
   PUBMED   14707134
  REMARK    GeneRIF: major repression function of CNOT2 is localized in a
            specialized protein motif, the Not-Box
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Denis,C.L. and Chen,J.
  TITLE     The CCR4-NOT complex plays diverse roles in mRNA metabolism
  JOURNAL   Prog Nucleic Acid Res Mol Biol 73, 221-250 (2003)
   PUBMED   12882519
  REMARK    Review article
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092881.8 and AC025569.37.
            
            Summary: This gene encodes a subunit of the multi-component
            CCR4-NOT complex. The CCR4-NOT complex regulates mRNA synthesis and
            degradation and is also thought to be involved in mRNA splicing,
            transport and localization. The encoded protein interacts with
            histone deacetylases and functions as a repressor of polymerase II
            transcription. Alternatively spliced transcript variants have been
            observed for this gene. [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2859328.1,
                                           SRR14038195.2238897.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..499
                     /product="CCR4-NOT transcription complex subunit 2 isoform
                     f"
                     /note="negative regulator of transcription 2;
                     CCR4-associated factor 2; CC chemokine receptor 4-negative
                     regulator of transcription 2"
                     /calculated_mol_wt=54817
     Region          355..478
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..499
                     /gene="CNOT2"
                     /gene_synonym="CDC36; HSPC131; IDNADFS; NOT2; NOT2H"
                     /coded_by="NM_001414661.1:144..1643"
                     /note="isoform f is encoded by transcript variant 15"
                     /db_xref="GeneID:4848"
                     /db_xref="HGNC:HGNC:7878"
                     /db_xref="MIM:604909"
ORIGIN      
        1 mvrtdghtls ekrnyqmlas pstsgqlsqf gaslygqqsa lglpmrgmsn ntpqlnrsls
       61 qgtqlpshvt pttgvptmsl htppspsrgi lpmnprnmmn hsqvgqgigi psrtnsmsss
      121 glgspnrssp siicmpkqqp srqpftvnsm sgfgmnrnqa fgmnnslssn ifngtdgsen
      181 vtgldlsdfp aladrnrreg sgnptplinp lagrapyvgm vtkpaneqsq dfsihnedfp
      241 alpgssykdp tssnddsksn lntsgkttss tdgpkfpgdk ssttqnnnqq kkgiqvlpdg
      301 rvtnipqgmv tdqfgmigll tfiraaetdp gmvhlalgsd lttlglnlns penlypkfas
      361 pwasspcrpq didfhvpsey ltnihirdkl aaiklgryge dllfylyymn ggdvlqllaa
      421 velfnrdwry hkeervwitr apgmeptmkt ntyergtyyf fdclnwrkva kefhleydkl
      481 eerphlpstf nynpaqqaf
//
LOCUS       NP_001424665             583 aa            linear   PRI 21-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001424665 XP_047272579 XP_054207397
VERSION     NP_001424665.1
DBSOURCE    REFSEQ: accession NM_001437736.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 583)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 583)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 583)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 583)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 583)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 583)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 583)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008641.7.
            
            On or before Apr 9, 2025 this sequence version replaced
            XP_047272579.1, XP_054207397.1.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1164451.1,
                                           SRR7346977.1085594.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..583
                     /product="TNFAIP3-interacting protein 1 isoform 2"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=65881
     Region          <161..>198
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          <245..>485
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..583
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001437736.1:106..1857"
                     /note="isoform 2 is encoded by transcript variant 15"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 meatrlrqka eelvkdnell pppspslgsf dplaeltgkd snvtasptap acpsdkpapv
       61 qkppssgtss efevvtpeeq nspessshan amalgplpre dgnlmlhlqr lettlsvcae
      121 epdhgqlfth lgrmalefnr laskvhkneq rtsilqtlce qlrkenealk akldkgleqr
      181 dqaaerlree nlelkkllms ngnkegasgr pgspkmegtg kkavagqqqa svtagkvpev
      241 valgaaekkv kmleqqrsel levnkqwdqh frsmkqqyeq kitelrqkla dlqkqvtdle
      301 aereqkqrdf drklllaksk iemeetdkeq ltaeakelrq kvkylqdqls pltrqreyqe
      361 keiqrlnkal eealsiqtpp sspptafgsp egagallrkq elvtqnellk qqvkifeedf
      421 qrersdrerm neekeelkkq veklqaqvtl snaqlkafkd eekarealrq qkrkakasge
      481 ryhvephpeh lcgaypyayp pmpamvphhg fedwsqiryp pppmamehpp plpnsrlfhl
      541 peytwrlpcg gvrnpnqssq vmdpptarpt epespkndre gpq
//
LOCUS       NP_001420634            1149 aa            linear   PRI 21-NOV-2025
DEFINITION  NACHT, LRR and PYD domains-containing protein 5 [Homo sapiens].
ACCESSION   NP_001420634
VERSION     NP_001420634.1
DBSOURCE    REFSEQ: accession NM_001433705.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1149)
  AUTHORS   Unoki,M., Uemura,S., Fujimoto,A. and Sasaki,H.
  TITLE     The maternal protein NLRP5 stabilizes UHRF1 in the cytoplasm:
            implication for the pathogenesis of multilocus imprinting
            disturbance
  JOURNAL   Hum Mol Genet 33 (18), 1575-1583 (2024)
   PUBMED   38868925
  REMARK    GeneRIF: The maternal protein NLRP5 stabilizes UHRF1 in the
            cytoplasm: implication for the pathogenesis of multilocus
            imprinting disturbance.
REFERENCE   2  (residues 1 to 1149)
  AUTHORS   Jentoft,I.M.A., Bauerlein,F.J.B., Welp,L.M., Cooper,B.H.,
            Petrovic,A., So,C., Penir,S.M., Politi,A.Z., Horokhovskyi,Y.,
            Takala,I., Eckel,H., Moltrecht,R., Lenart,P., Cavazza,T., Liepe,J.,
            Brose,N., Urlaub,H., Fernandez-Busnadiego,R. and Schuh,M.
  TITLE     Mammalian oocytes store proteins for the early embryo on
            cytoplasmic lattices
  JOURNAL   Cell 186 (24), 5308-5327 (2023)
   PUBMED   37922900
REFERENCE   3  (residues 1 to 1149)
  AUTHORS   Tong,X., Jin,J., Hu,Z., Zhang,Y., Fan,H.Y., Zhang,Y.L. and Zhang,S.
  TITLE     Mutations in OOEP and NLRP5 identified in infertile patients with
            early embryonic arrest
  JOURNAL   Hum Mutat 43 (12), 1909-1920 (2022)
   PUBMED   35946397
  REMARK    GeneRIF: Mutations in OOEP and NLRP5 identified in infertile
            patients with early embryonic arrest.
REFERENCE   4  (residues 1 to 1149)
  AUTHORS   Huang,L., Wang,Y., Lu,F., Jin,Q., Song,G., Ji,J., Luo,L., Jin,R.
            and Tong,X.
  TITLE     Novel mutations in NLRP5 and PATL2 cause female infertility
            characterized by primarily oocyte maturation abnormality and
            consequent early embryonic arrest
  JOURNAL   J Assist Reprod Genet 39 (3), 711-718 (2022)
   PUBMED   35091966
  REMARK    GeneRIF: Novel mutations in NLRP5 and PATL2 cause female
            infertility characterized by primarily oocyte maturation
            abnormality and consequent early embryonic arrest.
REFERENCE   5  (residues 1 to 1149)
  AUTHORS   Ramachandran,A., Kumar,B., Waris,G. and Everly,D.
  TITLE     Deubiquitination and Activation of the NLRP3 Inflammasome by UCHL5
            in HCV-Infected Cells
  JOURNAL   Microbiol Spectr 9 (1), e0075521 (2021)
   PUBMED   34431717
  REMARK    GeneRIF: Deubiquitination and Activation of the NLRP3 Inflammasome
            by UCHL5 in HCV-Infected Cells.
REFERENCE   6  (residues 1 to 1149)
  AUTHORS   Enjuanes,A., Benavente,Y., Bosch,F., Martin-Guerrero,I.,
            Colomer,D., Perez-Alvarez,S., Reina,O., Ardanaz,M.T., Jares,P.,
            Garcia-Orad,A., Pujana,M.A., Montserrat,E., de Sanjose,S. and
            Campo,E.
  TITLE     Genetic variants in apoptosis and immunoregulation-related genes
            are associated with risk of chronic lymphocytic leukemia
  JOURNAL   Cancer Res 68 (24), 10178-10186 (2008)
   PUBMED   19074885
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1149)
  AUTHORS   Alimohammadi,M., Bjorklund,P., Hallgren,A., Pontynen,N.,
            Szinnai,G., Shikama,N., Keller,M.P., Ekwall,O., Kinkel,S.A.,
            Husebye,E.S., Gustafsson,J., Rorsman,F., Peltonen,L., Betterle,C.,
            Perheentupa,J., Akerstrom,G., Westin,G., Scott,H.S., Hollander,G.A.
            and Kampe,O.
  TITLE     Autoimmune polyendocrine syndrome type 1 and NALP5, a parathyroid
            autoantigen
  JOURNAL   N Engl J Med 358 (10), 1018-1028 (2008)
   PUBMED   18322283
  REMARK    GeneRIF: NALP5 appears to be a tissue-specific autoantigen involved
            in hypoparathyroidism in patients with APS-1. Autoantibodies
            against NALP5 appear to be highly specific and may be diagnostic
            for this prominent component of APS-1
REFERENCE   8  (residues 1 to 1149)
  AUTHORS   Tschopp,J., Martinon,F. and Burns,K.
  TITLE     NALPs: a novel protein family involved in inflammation
  JOURNAL   Nat Rev Mol Cell Biol 4 (2), 95-104 (2003)
   PUBMED   12563287
  REMARK    Review article
REFERENCE   9  (residues 1 to 1149)
  AUTHORS   Tong,Z.B., Bondy,C.A., Zhou,J. and Nelson,L.M.
  TITLE     A human homologue of mouse Mater, a maternal effect gene essential
            for early embryonic development
  JOURNAL   Hum Reprod 17 (4), 903-911 (2002)
   PUBMED   11925379
  REMARK    GeneRIF: characterization of the MATER gene and its protein; this
            provides a basis for investigating their clinical implications in
            autoimmune premature ovarian failure and infertility in women
REFERENCE   10 (residues 1 to 1149)
  AUTHORS   Tumer,Z., Eggermann,T., Maas,S., Bliek,J. and Mackay,D.
  TITLE     Maternal Effect Gene-Related Multilocus Imprinting Disturbances
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   40373180
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011470.5 and AC024580.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the NALP
            protein family. Members of the NALP protein family typically
            contain a NACHT domain, a NACHT-associated domain (NAD), a
            C-terminal leucine-rich repeat (LRR) region, and an N-terminal
            pyrin domain (PYD). Expression of this gene is restricted to the
            oocyte. A mouse gene that encodes a maternal oocyte protein,
            similar to this encoded protein, is required for normal early
            embryogenesis. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.149203.1,
                                           SRR14038197.161910.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000850973.1/ ENSP00000521055.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1149
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..1149
                     /product="NACHT, LRR and PYD domains-containing protein 5"
                     /note="NACHT, leucine rich repeat and PYD containing 5;
                     nucleotide-binding oligomerization domain, leucine rich
                     repeat and pyrin domain containing 5; maternal antigen
                     that embryos require; mater protein homolog"
                     /calculated_mol_wt=129066
     Region          14..97
                     /region_name="Pyrin_NALPs"
                     /note="Pyrin death domain found in NALP proteins; cd08320"
                     /db_xref="CDD:260032"
     Region          229..392
                     /region_name="NACHT"
                     /note="NACHT domain; pfam05729"
                     /db_xref="CDD:428606"
     Region          476..531
                     /region_name="NOD2_WH"
                     /note="NOD2 winged helix domain; pfam17779"
                     /db_xref="CDD:465501"
     Region          533..650
                     /region_name="NLRC4_HD2"
                     /note="NLRC4 helical domain HD2; pfam17776"
                     /db_xref="CDD:465499"
     Region          584..934
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Site            order(585,588,590,605,608,610,613,615,633,636,638,641,643,
                     662,667,669,672,674,714,735,737,740,742,761,764,766,768,
                     770,788,791,793,796,798,817,820,822,825,827,845,848,850,
                     853,855,874,877,879,882,884,902,905,907,910,912,931,934)
                     /site_type="active"
                     /note="Leucine-rich repeats [active]"
                     /db_xref="CDD:238064"
     Site            order(611..612,671,767,795,852,878,880,906)
                     /site_type="other"
                     /note="Substrate binding site [chemical binding]"
                     /db_xref="CDD:238064"
     Region          732..753
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          754..785
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          788..812
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          817..844
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          845..873
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          846..1108
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          874..901
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Site            order(880..881,938,995,1023,1080,1106,1108)
                     /site_type="other"
                     /note="Substrate binding site [chemical binding]"
                     /db_xref="CDD:238064"
     Region          902..930
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          931..958
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          959..986
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          988..1015
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          1016..1040
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          1045..1072
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..1149
                     /gene="NLRP5"
                     /gene_synonym="CLR19.8; MATER; NALP5; OZEMA19; PAN11;
                     PYPAF8"
                     /coded_by="NM_001433705.1:119..3568"
                     /db_xref="GeneID:126206"
                     /db_xref="HGNC:HGNC:21269"
                     /db_xref="MIM:609658"
ORIGIN      
        1 megdksltfs syglqwclye ldkeefqtfk ellkkksses ttcsipqfei enanveclal
       61 llheyygasl awatsisife nmnlrtlsek arddmkrhsp edpeatmtdq gpskekvpgi
      121 sqavqqdsat aaetkeqeis qameqegata aeteeqeisq ameqegataa eteeqghggd
      181 twdykshvmt kfaeeedvrr sfentaadwp emqtlagafd sdrwgfrprt vvlhgksgig
      241 ksalarrivl cwaqgglyqg mfsyvfflpv remqrkkess vtefisrewp dsqapvteim
      301 srperllfii dgfddlgsvl nndtklckdw aekqppftli rsllrkvllp esflivtvrd
      361 vgteklksev vspryllvrg isgeqrihll lergigehqk tqglraimnn relldqcqvp
      421 avgslicval qlqdvvgesv apfnqtltgl haafvfhqlt prgvvrrcln leervvlkrf
      481 crmavegvwn rksvfdgddl mvqglgesel ralfhmnill pdshceeyyt ffhlslqdfc
      541 aalyyvlegl eiepalcply vektkrsmel kqagfhihsl wmkrflfglv sedvrrplev
      601 llgcpvplgv kqkllhwvsl lgqqpnattp gdtldafhcl fetqdkefvr lalnsfqevw
      661 lpinqnldli assfclqhcp ylrkirvdvk gifprdesae acpvvplwmr dktlieeqwe
      721 dfcsmlgthp hlrqldlgss ilteramktl caklrhptck iqtlmfrnaq itpgvqhlwr
      781 ivmanrnlrs lnlggthlke edvrmaceal khpkcllesl rldccgltha cylkisqilt
      841 tspslkslsl agnkvtdqgv mplsdalrvs qcalqklile dcgitatgcq slasalvsnr
      901 slthlclsnn slgnegvnll crsmrlphcs lqrlmlnqch ldtagcgfla lalmgnswlt
      961 hlslsmnpve dngvkllcev mrepschlqd lelvkchlta acceslscvi srsrhlksld
     1021 ltdnalgdgg vaalceglkq knsvlarlgl kacgltsdcc ealslalscn rhltslnlvq
     1081 nnfspkgmmk lcsafacpts nlqiiglwkw qypvqirkll eevqllkprv vidgswhsfd
     1141 eddrywwkn
//
LOCUS       NP_001424280             643 aa            linear   PRI 21-NOV-2025
DEFINITION  MAP/microtubule affinity-regulating kinase 3 isoform h [Homo
            sapiens].
ACCESSION   NP_001424280 XP_005267700 XP_054232050
VERSION     NP_001424280.1
DBSOURCE    REFSEQ: accession NM_001437351.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Aparicio-Bautista,D.I., Jimenez-Ortega,R.F., Becerra-Cervera,A.,
            Aquino-Galvez,A., de Leon-Suarez,V.P., Casas-Avila,L., Salmeron,J.,
            Hidalgo-Bravo,A., Rivera-Paredez,B. and Velazquez-Cruz,R.
  TITLE     Interaction between MARK3 (rs11623869), PLCB4 (rs6086746) and
            GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women
  JOURNAL   Front Endocrinol (Lausanne) 15, 1392063 (2024)
   PUBMED   38715801
  REMARK    GeneRIF: Interaction between MARK3 (rs11623869), PLCB4 (rs6086746)
            and GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 643)
  AUTHORS   Li,M.G., Katsura,K., Nomiyama,H., Komaki,K., Ninomiya-Tsuji,J.,
            Matsumoto,K., Kobayashi,T. and Tamura,S.
  TITLE     Regulation of the interleukin-1-induced signaling pathways by a
            novel member of the protein phosphatase 2C family (PP2Cepsilon)
  JOURNAL   J Biol Chem 278 (14), 12013-12021 (2003)
   PUBMED   12556533
REFERENCE   7  (residues 1 to 643)
  AUTHORS   Sun,T.Q., Lu,B., Feng,J.J., Reinhard,C., Jan,Y.N., Fantl,W.J. and
            Williams,L.T.
  TITLE     PAR-1 is a Dishevelled-associated kinase and a positive regulator
            of Wnt signalling
  JOURNAL   Nat Cell Biol 3 (7), 628-636 (2001)
   PUBMED   11433294
REFERENCE   8  (residues 1 to 643)
  AUTHORS   Peng,C.Y., Graves,P.R., Ogg,S., Thoma,R.S., Byrnes,M.J. 3rd, Wu,Z.,
            Stephenson,M.T. and Piwnica-Worms,H.
  TITLE     C-TAK1 protein kinase phosphorylates human Cdc25C on serine 216 and
            promotes 14-3-3 protein binding
  JOURNAL   Cell Growth Differ 9 (3), 197-208 (1998)
   PUBMED   9543386
REFERENCE   9  (residues 1 to 643)
  AUTHORS   Ono,T., Kawabe,T., Sonta,S. and Okamoto,T.
  TITLE     Assignment of MARK3 alias KP78 to human chromosome band 14q32.3 by
            in situ hybridization
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 101-102 (1997)
   PUBMED   9533022
REFERENCE   10 (residues 1 to 643)
  AUTHORS   Meller,N., Liu,Y.C., Collins,T.L., Bonnefoy-Berard,N., Baier,G.,
            Isakov,N. and Altman,A.
  TITLE     Direct interaction between protein kinase C theta (PKC theta) and
            14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition
            of PKC theta translocation and function
  JOURNAL   Mol Cell Biol 16 (10), 5782-5791 (1996)
   PUBMED   8816492
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133367.4 and KF456011.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_005267700.2, XP_054232050.1.
            
            Summary: The protein encoded by this gene is activated by
            phosphorylation and in turn is involved in the phosphorylation of
            tau proteins MAP2 and MAP4. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2563273.1,
                                           SRR14038192.3145080.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.32-q32.33"
     Protein         1..643
                     /product="MAP/microtubule affinity-regulating kinase 3
                     isoform h"
                     /EC_number="2.7.11.1"
                     /note="EMK-2; C-TAK1; ELKL motif kinase 2; protein kinase
                     STK10; ser/Thr protein kinase PAR-1; cdc25C-associated
                     protein kinase 1; MAP/microtubule affinity-regulating
                     kinase 3; serine/threonine-protein kinase p78"
                     /calculated_mol_wt=71992
     Region          55..307
                     /region_name="STKc_MARK"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     MAP/microtubule affinity-regulating kinases; cd14072"
                     /db_xref="CDD:270974"
     Site            order(62..66,70,83,85,116,132..135,139,141..142,144,
                     177..178,180,182..183,185,195..196,199,212..217,219,
                     249..252,254)
                     /site_type="active"
                     /db_xref="CDD:270974"
     Site            order(62..65,70,83,85,116,132..135,139,182..183,185,
                     195..196)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270974"
     Site            order(66,139,141,177..178,180,182,199,213..217,219)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270974"
     Site            195..217
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270974"
     Region          325..367
                     /region_name="UBA_MARK3_4"
                     /note="UBA domain found in MAP/microtubule
                     affinity-regulating kinase MARK3, MARK4, and similar
                     proteins; cd14407"
                     /db_xref="CDD:270590"
     Region          544..641
                     /region_name="MARK1-3_C"
                     /note="C-terminal, kinase associated domain 1 (KA1), a
                     phospholipid binding domain, of microtubule
                     affinity-regulating kinases 1-3; cd12196"
                     /db_xref="CDD:213381"
     Site            order(546,549,619,621..622)
                     /site_type="other"
                     /note="putative phospholipid binding site [chemical
                     binding]"
                     /db_xref="CDD:213381"
     CDS             1..643
                     /gene="MARK3"
                     /gene_synonym="CTAK1; KP78; Par-1a; PAR1A; VIPB"
                     /coded_by="NM_001437351.1:616..2547"
                     /note="isoform h is encoded by transcript variant 8"
                     /db_xref="GeneID:4140"
                     /db_xref="HGNC:HGNC:6897"
                     /db_xref="MIM:602678"
ORIGIN      
        1 mstrtplptv nerdtenhts hgdgrqevts rtsrsgarcr nsiascadeq phignyrllk
       61 tigkgnfakv klarhiltgr evaikiidkt qlnptslqkl frevrimkil nhpnivklfe
      121 vietektlyl imeyasggev fdylvahgrm kekearskfr qivsavqych qkrivhrdlk
      181 aenllldadm nikiadfgfs neftvggkld tfcgsppyaa pelfqgkkyd gpevdvwslg
      241 vilytlvsgs lpfdgqnlke lrervlrgky ripfymstdc enllkrflvl npikrgtleq
      301 imkdrwinag heedelkpfv epeldisdqk ridimvgmgy sqeeiqesls kmkydeitat
      361 ylllgrksse ldasdsssss nlslakvrps sdlnnstgqs phhkvqrsvs ssqkqrrysd
      421 hagpaipsvv aypkrsqtst adsdlkedgi ssrkssgsav ggkgiapasp mlgnasnpnk
      481 adiperkkss tvpssntasg gmtrrntyvc serttadrhs viqngkensr nvsaeqkden
      541 keakprslrf twsmkttssm dpgdmmreir kvldanncdy eqrerfllfc vhgdghaenl
      601 vqwemevckl prlslngvrf krisgtsiaf kniaskiane lkl
//
LOCUS       NP_001427435             604 aa            linear   PRI 21-NOV-2025
DEFINITION  radixin isoform 1 [Homo sapiens].
ACCESSION   NP_001427435
VERSION     NP_001427435.1
DBSOURCE    REFSEQ: accession NM_001440506.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Kruse,T., Benz,C., Garvanska,D.H., Lindqvist,R., Mihalic,F.,
            Coscia,F., Inturi,R., Sayadi,A., Simonetti,L., Nilsson,E., Ali,M.,
            Kliche,J., Moliner Morro,A., Mund,A., Andersson,E., McInerney,G.,
            Mann,M., Jemth,P., Davey,N.E., Overby,A.K., Nilsson,J. and
            Ivarsson,Y.
  TITLE     Large scale discovery of coronavirus-host factor protein
            interaction motifs reveals SARS-CoV-2 specific mechanisms and
            vulnerabilities
  JOURNAL   Nat Commun 12 (1), 6761 (2021)
   PUBMED   34799561
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Stemmer-Rachamimov,A.O., Gonzalez-Agosti,C., Xu,L., Burwick,J.A.,
            Beauchamp,R., Pinney,D., Louis,D.N. and Ramesh,V.
  TITLE     Expression of NF2-encoded merlin and related ERM family proteins in
            the human central nervous system
  JOURNAL   J Neuropathol Exp Neurol 56 (6), 735-742 (1997)
   PUBMED   9184664
REFERENCE   7  (residues 1 to 604)
  AUTHORS   Hirao,M., Sato,N., Kondo,T., Yonemura,S., Monden,M., Sasaki,T.,
            Takai,Y., Tsukita,S. and Tsukita,S.
  TITLE     Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma
            membrane association: possible involvement of phosphatidylinositol
            turnover and Rho-dependent signaling pathway
  JOURNAL   J Cell Biol 135 (1), 37-51 (1996)
   PUBMED   8858161
REFERENCE   8  (residues 1 to 604)
  AUTHORS   Wilgenbus,K.K., Milatovich,A., Francke,U. and Furthmayr,H.
  TITLE     Molecular cloning, cDNA sequence, and chromosomal assignment of the
            human radixin gene and two dispersed pseudogenes
  JOURNAL   Genomics 16 (1), 199-206 (1993)
   PUBMED   8486357
REFERENCE   9  (residues 1 to 604)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 604)
  AUTHORS   Sato,N., Funayama,N., Nagafuchi,A., Yonemura,S., Tsukita,S. and
            Tsukita,S.
  TITLE     A gene family consisting of ezrin, radixin and moesin. Its specific
            localization at actin filament/plasma membrane association sites
  JOURNAL   J Cell Sci 103 (Pt 1), 131-143 (1992)
   PUBMED   1429901
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002788.3 and AP000901.5.
            
            Summary: Radixin is a cytoskeletal protein that may be important in
            linking actin to the plasma membrane. It is highly similar in
            sequence to both ezrin and moesin. The radixin gene has been
            localized by fluorescence in situ hybridization to 11q23. A
            truncated version representing a pseudogene (RDXP2) was assigned to
            Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was
            mapped to 11p by Southern and PCR analyses. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1560809.1,
                                           SRR14038193.1387930.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467148 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..604
                     /product="radixin isoform 1"
                     /calculated_mol_wt=70918
     Region          7..206
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          200..296
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(242..243,245..251,260,281,284..285,288)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(242,245..252,260,281,284..285,288)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(278,282)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            281..296
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          310..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35241.1)"
     Region          347..456
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          376..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35241.1)"
     Region          462..526
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35241.1)"
     Region          507..583
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ROCK2.
                     /evidence=ECO:0000250|UniProtKB:P26043; propagated from
                     UniProtKB/Swiss-Prot (P35241.1)"
     CDS             1..604
                     /gene="RDX"
                     /gene_synonym="DFNB24"
                     /coded_by="NM_001440506.1:213..2027"
                     /note="isoform 1 is encoded by transcript variant 8"
                     /db_xref="GeneID:5962"
                     /db_xref="HGNC:HGNC:9944"
                     /db_xref="MIM:179410"
ORIGIN      
        1 mpkpinvrvt tmdaelefai qpnttgkqlf dqvvktvglr evwffglqyv dskgystwlk
       61 lnkkvtqqdv kkenplqfkf rakffpedvs eeliqeitqr lfflqvkeai lndeiycppe
      121 tavllasyav qakygdynke ihkpgyland rllpqrvleq hkltkeqwee riqnwheehr
      181 gmlredsmme ylkiaqdlem ygvnyfeikn kkgtelwlgv dalglniyeh ddkltpkigf
      241 pwseirnisf ndkkfvikpi dkkapdfvfy aprlrinkri lalcmgnhel ymrrrkpdti
      301 evqqmkaqar eekhqkqler aqlenekkkr eiaekekeri erekeelmer lkqieeqtik
      361 aqkeleeqtr kaleldqerk rakeeaerle kerraaeeak saiakqaadq mknqeqlaae
      421 laeftakial leeakkkkee eatewqhkaf aaqedlektk eelktvmsap pppppppvip
      481 ptenehdehd ennaeasael snegvmnhrs eeervtetqk nervkkqlqa lsselaqard
      541 etkktqndvl haenvkagrd kyktlrqirq gntkqridef eamwgpklya lfqmrscqss
      601 ikqm
//
LOCUS       NP_001424249             873 aa            linear   PRI 21-NOV-2025
DEFINITION  ephrin type-A receptor 5 isoform i [Homo sapiens].
ACCESSION   NP_001424249 XP_047305719 XP_054205164
VERSION     NP_001424249.1
DBSOURCE    REFSEQ: accession NM_001437320.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 873)
  AUTHORS   Han,X., Liu,T., Zhai,J., Liu,C., Wang,W., Nie,C., Wang,Q., Zhu,X.,
            Zhou,H. and Tian,W.
  TITLE     Association between EPHA5 methylation status in peripheral blood
            leukocytes and the risk and prognosis of gastric cancer
  JOURNAL   PeerJ 10, e13774 (2022)
   PUBMED   36164608
  REMARK    GeneRIF: Association between EPHA5 methylation status in peripheral
            blood leukocytes and the risk and prognosis of gastric cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 873)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   3  (residues 1 to 873)
  AUTHORS   Liu,C., He,Y., Feng,X., Li,J. and Wang,J.
  TITLE     Expression of EPHA5 in lung adenocarcinoma is associated with lymph
            node metastasis and EGFR mutation
  JOURNAL   APMIS 130 (6), 338-345 (2022)
   PUBMED   35332588
  REMARK    GeneRIF: Expression of EPHA5 in lung adenocarcinoma is associated
            with lymph node metastasis and EGFR mutation.
REFERENCE   4  (residues 1 to 873)
  AUTHORS   Abouhashem,N., Harb,O., Elwan,A., Zaitoun,M. and Saraya,Y.
  TITLE     Immunohistochemical evaluation of forkhead box A1 and EphA5 markers
            in serous ovarian carcinomas, and their impact on the clinical
            outcome of patients
  JOURNAL   Pol J Pathol 73 (2), 120-133 (2022)
   PUBMED   36345952
  REMARK    GeneRIF: Immunohistochemical evaluation of forkhead box A1 and
            EphA5 markers in serous ovarian carcinomas, and their impact on the
            clinical outcome of patients.
REFERENCE   5  (residues 1 to 873)
  AUTHORS   Zhou,R.
  TITLE     Regulation of topographic projection by the Eph family receptor Bsk
            (EphA5) and its ligands
  JOURNAL   Cell Tissue Res 290 (2), 251-259 (1997)
   PUBMED   9321686
  REMARK    Review article
REFERENCE   6  (residues 1 to 873)
  AUTHORS   Miescher,G.C., Taylor,V., Olivieri,G., Mindermann,T., Schrock,E.
            and Steck,A.J.
  TITLE     Extensive splice variation and localization of the EHK-1 receptor
            tyrosine kinase in adult human brain and glial tumors
  JOURNAL   Brain Res Mol Brain Res 46 (1-2), 17-24 (1997)
   PUBMED   9191074
REFERENCE   7  (residues 1 to 873)
  AUTHORS   Gale,N.W., Holland,S.J., Valenzuela,D.M., Flenniken,A., Pan,L.,
            Ryan,T.E., Henkemeyer,M., Strebhardt,K., Hirai,H., Wilkinson,D.G.,
            Pawson,T., Davis,S. and Yancopoulos,G.D.
  TITLE     Eph receptors and ligands comprise two major specificity subclasses
            and are reciprocally compartmentalized during embryogenesis
  JOURNAL   Neuron 17 (1), 9-19 (1996)
   PUBMED   8755474
REFERENCE   8  (residues 1 to 873)
  AUTHORS   Winslow,J.W., Moran,P., Valverde,J., Shih,A., Yuan,J.Q., Wong,S.C.,
            Tsai,S.P., Goddard,A., Henzel,W.J., Hefti,F. et al.
  TITLE     Cloning of AL-1, a ligand for an Eph-related tyrosine kinase
            receptor involved in axon bundle formation
  JOURNAL   Neuron 14 (5), 973-981 (1995)
   PUBMED   7748564
REFERENCE   9  (residues 1 to 873)
  AUTHORS   Fox,G.M., Holst,P.L., Chute,H.T., Lindberg,R.A., Janssen,A.M.,
            Basu,R. and Welcher,A.A.
  TITLE     cDNA cloning and tissue distribution of five human EPH-like
            receptor protein-tyrosine kinases
  JOURNAL   Oncogene 10 (5), 897-905 (1995)
   PUBMED   7898931
REFERENCE   10 (residues 1 to 873)
  AUTHORS   Spritz,R.A., Strunk,K.M., Lee,S.T., Lu-Kuo,J.M., Ward,D.C., Le
            Paslier,D., Altherr,M.R., Dorman,T.E. and Moir,D.T.
  TITLE     A YAC contig spanning a cluster of human type III receptor protein
            tyrosine kinase genes (PDGFRA-KIT-KDR) in chromosome segment 4q12
  JOURNAL   Genomics 22 (2), 431-436 (1994)
   PUBMED   7528718
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104137.5, AC105923.6 and
            AC018683.4.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_047305719.1, XP_054205164.1.
            
            Summary: This gene belongs to the ephrin receptor subfamily of the
            protein-tyrosine kinase family. EPH and EPH-related receptors have
            been implicated in mediating developmental events, particularly in
            the nervous system. Receptors in the EPH subfamily typically have a
            single kinase domain and an extracellular region containing a
            Cys-rich domain and 2 fibronectin type III repeats. The ephrin
            receptors are divided into 2 groups based on the similarity of
            their extracellular domain sequences and their affinities for
            binding ephrin-A and ephrin-B ligands. Alternatively spliced
            transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2259708.1,
                                           SRR14038191.931343.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..873
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q13.1-q13.2"
     Protein         1..873
                     /product="ephrin type-A receptor 5 isoform i"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-A receptor 5; receptor protein-tyrosine
                     kinase HEK7; tyrosine-protein kinase receptor EHK-1;
                     EPH-like kinase 7; EPH homology kinase 1; brain-specific
                     kinase; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=96712
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54756.3)"
     Region          60..232
                     /region_name="EphR_LBD_A5"
                     /note="Ligand Binding Domain of Ephrin type-A Receptor 5;
                     cd10483"
                     /db_xref="CDD:198451"
     Site            order(84,86..90,97..98,100,102,133,135,140..141,183,
                     187..188,191..193,220..222,224)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198451"
     Site            264
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54756.3)"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54756.3)"
     Region          305..395
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(305,368,383)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(384..385,387..388)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          411..508
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Region          506..772
                     /region_name="PTKc_EphR_A"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphA Ephrin Receptors; cd05066"
                     /db_xref="CDD:270651"
     Site            order(517,519..521,525,541,543,589..590,592,636,640..641,
                     643,654,673..677,686,720)
                     /site_type="active"
                     /db_xref="CDD:270651"
     Site            order(517..521,525,541,543,589..592,595..596,640..641,643,
                     654)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270651"
     Site            order(636,640,673..677,686,720)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270651"
     Site            653..679
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270651"
     Region          801..866
                     /region_name="SAM_EPH-A5"
                     /note="SAM domain of EPH-A5 subfamily of tyrosine kinase
                     receptors; cd09546"
                     /db_xref="CDD:188945"
     Site            order(818,851)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188945"
     CDS             1..873
                     /gene="EPHA5"
                     /gene_synonym="CEK7; EHK-1; EHK1; EK7; HEK7; TYRO4"
                     /coded_by="NM_001437320.1:748..3369"
                     /note="isoform i is encoded by transcript variant 9"
                     /db_xref="GeneID:2044"
                     /db_xref="HGNC:HGNC:3389"
                     /db_xref="MIM:600004"
ORIGIN      
        1 mrgsgprgag rrrppsgggd tpitpaslag cysaprrapl wtclllcaal rtllaspsne
       61 vnlldsrtvm gdlgwiafpk ngweeigevd enyapihtyq vckvmeqnqn nwlltswisn
      121 egasrifiel kftlrdcnsl pgglgtcket fnmyyfesdd qngrnikenq yikidtiaad
      181 esfteldlgd rvmklntevr dvgplskkgf ylafqdvgac ialvsvrvyy kkcpsvvrhl
      241 avfpdtitga dssqllevsg scvnhsvtde ppkmhcsaeg ewlvpigkcm ckagyeekng
      301 tcqapspvtn vkkgkiakns islswqepdr pngiileyei kyfekdqets ytiikskett
      361 itaeglkpas vyvfqirart aagygvfsrr fefettpvfa assdqsqipv iavsvtvgvi
      421 llavvigvll sgsccecgcg rasslcavah psliwrcgys kakqdpeeek mhfhnghikl
      481 pgvrtyidph tyedpnqavh efakeieasc itiervigag efgevcsgrl klpgkrelpv
      541 aiktlkvgyt ekqrrdflge asimgqfdhp niihlegvvt kskpvmivte ymengsldtf
      601 lkkndgqftv iqlvgmlrgi sagmkylsdm gyvhrdlaar nilinsnlvc kvsdfglsrv
      661 leddpeaayt trggkipirw tapeaiafrk ftsasdvwsy givmwevvsy gerpywemtn
      721 qdvikaveeg yrlpspmdcp aalyqlmldc wqkernsrpk fdeivnmldk lirnpsslkt
      781 lvnascrvsn llaehsplgs gayrsvgewl eaikmgryte ifmengyssm davaqvtled
      841 lrrlgvtlvg hqkkimnslq emkvqlvngm vpl
//
LOCUS       NP_001389625            1299 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 9 [Homo sapiens].
ACCESSION   NP_001389625
VERSION     NP_001389625.1
DBSOURCE    REFSEQ: accession NM_001402696.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1299)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1299)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1299)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1299)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1299)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1299)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1299)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1299)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1299)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1299)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.755101.1,
                                           SRR14038196.2166071.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1299
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1299
                     /product="kinectin isoform 9"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=149438
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          316..>532
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          448..1239
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1299
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402696.1:179..4078"
                     /note="isoform 9 is encoded by transcript variant 20"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqdlkqeika
      841 lkeeignvql ekaqqlsits kvqelqnllk gkeeqmntmk avleekekdl antgkwlqdl
      901 qeeneslkah vqevaqhnlk eassasqfee leivlkeken elkrleamlk eresdlsskt
      961 qllqdvqden klfksqieql kqqnyqqass fppheellkv iserekeisg lwneldslkd
     1021 avehqrkknn dlreknweam ealastekml qdkvnktsks ygewlhgfek kakecmagts
     1081 gseevkvleh klkeademht llqlecekyk svlaetegil qklqrsveqe enkwkvkvde
     1141 shktikqmqs sftsseqele rlrsenkdie nlrrerehle melekaemer styvtevrel
     1201 kaqlnetltk lrteqnerqk vagdlhkaqq sleliqskiv kaagdttvie nsdvspetes
     1261 seketmsvsl nqtvtqlqql lqavnqqltk ekehyqvle
//
LOCUS       NP_001427334             898 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001427334
VERSION     NP_001427334.1
DBSOURCE    REFSEQ: accession NM_001440405.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 898)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 898)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 898)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 898)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 898)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 898)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 898)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3, AP004147.3 and
            AP001929.5.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2144120
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..898
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     4 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=98772
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..402
                     /region_name="Periplasmic_Binding_Protein_type1"
                     /note="Type 1 periplasmic binding fold superfamily;
                     cl10011"
                     /db_xref="CDD:471960"
     Region          415..727
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     CDS             1..898
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440405.1:191..2887"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk aaelgmvsay
      241 ytyiftnlef slqrmdslvd drvnilgfsi fnqshaffqe faqslnqswq encdhvpftg
      301 palssallfd avyavvtavq elnrsqeigv kplscgsaqi wqhgtslmny lrmveleglt
      361 ghiefnskgq rsnyalkilq ftrngfrqig qwhvaeglsm dshlyasnis dtlfnttlvv
      421 ttilenpylm lkgnhqemeg ndryegfcvd mlkelaeilr fnykirlvgd gvygvpeang
      481 twtgmvgeli arkadlavag ltitaerekv idfskpfmtl gisilyrvhm grkpgyfsfl
      541 dpfspgvwlf mllaylavsc vlflvarwaf tliiissyta nlaafltvqr mdvpiesvdd
      601 ladqtaieyg tihggssmtf fqnsryqtyq rmwnymyskq psvfvkstee giarvlnsny
      661 afllestmne yyrqrncnlt qigglldtkg ygigmpvgsv frdefdlail qlqennrlei
      721 lkrkwweggk cpkeedhrak glgmeniggi fvvlicgliv aifmamlefl wtlrhseate
      781 vsvcqemvte lrsiilcqds ihprrrraav ppprppipee rrprgtatls ngklcgagep
      841 dqlaqrlaqe aalvargcth irvcpecrrf qglrarpspa rseeslewek ttnssepe
//
LOCUS       NP_001398061            2395 aa            linear   PRI 21-NOV-2025
DEFINITION  spatacsin isoform 3 [Homo sapiens].
ACCESSION   NP_001398061 XP_006720763
VERSION     NP_001398061.1
DBSOURCE    REFSEQ: accession NM_001411132.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2395)
  AUTHORS   Mai,X., Wang,Y., Wang,X., Liu,M., Teng,F., Liu,Z., Su,M.Y. and
            Stjepanovic,G.
  TITLE     Structural basis for membrane remodeling by the AP5-SPG11-SPG15
            complex
  JOURNAL   Nat Struct Mol Biol 32 (8), 1334-1346 (2025)
   PUBMED   40175557
REFERENCE   2  (residues 1 to 2395)
  AUTHORS   Pierga,A., Matusiak,R., Cauhape,M., Branchu,J., Danglot,L.,
            Boutry,M. and Darios,F.
  TITLE     Spatacsin regulates directionality of lysosome trafficking by
            promoting the degradation of its partner AP5Z1
  JOURNAL   PLoS Biol 21 (10), e3002337 (2023)
   PUBMED   37871017
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2395)
  AUTHORS   Regensburger,M., Krumm,L., Schmidt,M.A., Schmid,A., Spatz,I.T.,
            Marterstock,D.C., Kopp,C., Kohl,Z., Doerfler,A., Karrasch,T.,
            Winner,B. and Winkler,J.
  TITLE     Neurometabolic Dysfunction in SPG11 Hereditary Spastic Paraplegia
  JOURNAL   Nutrients 14 (22), 4803 (2022)
   PUBMED   36432490
  REMARK    GeneRIF: Neurometabolic Dysfunction in SPG11 Hereditary Spastic
            Paraplegia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2395)
  AUTHORS   Cogo,S., Tomkins,J.E., Vavouraki,N., Giusti,V., Forcellato,F.,
            Franchin,C., Tessari,I., Arrigoni,G., Cendron,L., Manzoni,C.,
            Civiero,L., Lewis,P.A. and Greggio,E.
  TITLE     Cytosolic sequestration of spatacsin by Protein Kinase A and 14-3-3
            proteins
  JOURNAL   Neurobiol Dis 174, 105858 (2022)
   PUBMED   36096339
REFERENCE   5  (residues 1 to 2395)
  AUTHORS   Martinez Murillo,F., Kobayashi,H., Pegoraro,E., Galluzzi,G.,
            Creel,G., Mariani,C., Farina,E., Ricci,E., Alfonso,G., Pauli,R.M.
            and Hoffman,E.P.
  TITLE     Genetic localization of a new locus for recessive familial spastic
            paraparesis to 15q13-15
  JOURNAL   Neurology 53 (1), 50-56 (1999)
   PUBMED   10408536
REFERENCE   6  (residues 1 to 2395)
  AUTHORS   Hentati,A., Ouahchi,K., Pericak-Vance,M.A., Nijhawan,D., Ahmad,A.,
            Yang,Y., Rimmler,J., Hung,W., Schlotter,B., Ahmed,A., Ben
            Hamida,M., Hentati,F. and Siddique,T.
  TITLE     Linkage of a commoner form of recessive amyotrophic lateral
            sclerosis to chromosome 15q15-q22 markers
  JOURNAL   Neurogenetics 2 (1), 55-60 (1998)
   PUBMED   9933301
REFERENCE   7  (residues 1 to 2395)
  AUTHORS   Almenoff,J.S., Jurka,J. and Schoolnik,G.K.
  TITLE     Induction of heat-stable enterotoxin receptor activity by a human
            Alu repeat
  JOURNAL   J Biol Chem 269 (24), 16610-16617 (1994)
   PUBMED   8206979
REFERENCE   8  (residues 1 to 2395)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   9  (residues 1 to 2395)
  AUTHORS   Siddique,N. and Siddique,T.
  TITLE     Amyotrophic Lateral Sclerosis Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301623
REFERENCE   10 (residues 1 to 2395)
  AUTHORS   Stevanin,G.
  TITLE     Spastic Paraplegia 11
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301389
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009996.7.
            
            On Aug 22, 2022 this sequence version replaced XP_006720763.1.
            
            Summary: The protein encoded by this gene is a potential
            transmembrane protein that is phosphorylated upon DNA damage.
            Defects in this gene are a cause of spastic paraplegia type 11
            (SPG11). Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, May 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1648571.1,
                                           SRR14038197.2317722.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.1"
     Protein         1..2395
                     /product="spatacsin isoform 3"
                     /note="spatacsin; spastic paraplegia 11 protein;
                     colorectal carcinoma-associated protein; SPG11, spatacsin
                     vesicle trafficking associated; spastic paraplegia 11
                     (autosomal recessive); amyotrophic lateral sclerosis 5"
                     /calculated_mol_wt=273039
     Site            1907
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UHA3; propagated from
                     UniProtKB/Swiss-Prot (Q96JI7.3)"
     Region          2047..2339
                     /region_name="Spatacsin_C"
                     /note="Spatacsin C-terminus; pfam14649"
                     /db_xref="CDD:464236"
     CDS             1..2395
                     /gene="SPG11"
                     /gene_synonym="ALS5; CMT2X; KIAA1840"
                     /coded_by="NM_001411132.1:16..7203"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS91991.1"
                     /db_xref="GeneID:80208"
                     /db_xref="HGNC:HGNC:11226"
                     /db_xref="MIM:610844"
ORIGIN      
        1 maaeegvasa asaggswgta amgrvlpmll vpvpaeamgq lgsraqlrtq pealgsltaa
       61 gslqvlsltp gsrgggrccl egpfwhflwe dsrnsstpte kpkllalgen yelliyefnl
      121 kdgrcdatil yscsrealqk liddqdisis llslrilsfh nntsllfink cvilhiifpe
      181 rdaairvlnc ftlplpaqav dmiidtqlcr gilfvlsslg wiyifdvvdg tyvahvdlal
      241 hkedmcneqq qepakissft slkvsqdldv avivsssnsa valnlnlyfr qhpghllcer
      301 iledlpiqgp kgvdeddpvn saynmklakf sfqidrswka qlsslnetik nsklevscca
      361 pwfqdilhle spesgnhsts vqswafipqd imhgqynvlq kdhaktsdpg rswkimhise
      421 qeepielkcv svtgftalft wevermgyti tlwdletqgm qcfslgtkci pvdssgdqql
      481 cfvltengls lilfgltqee flnrlmihgs astvdtlchl ngwgrcsipi haleagienr
      541 qldtvnfflk skenlfnpss kssvsdqfdh lsshlylrnv eelipaldll csairesyse
      601 pqskhfseql lnltlsflnn qikelfihte eldehlqkgv niltsyinel rtfmikfpwk
      661 ltdaideydv henvpkvkes niwkklsfee viasailnnk ipeaqtffri dshsaqklee
      721 ligiglnlvf dnlkknnike asellknmgf dvkgqllkic fyttnknird flveilkekn
      781 yfsekekrti dfvhqvekly lghfqenmqi qsfprywike qdffkhksvl dsflkydckd
      841 efnkqdhriv lnwalwwdql tqesillpri speeyksysp ealwryltar hdwlniilwi
      901 gefqtqhsya slqqnkwpll tvdvinqnts cnnymrneil dklarngvfl aseledfecf
      961 llrlsriggv iqdtlpvqny ktkegwdfhs qfilyclehs lqhllyvyld cyklspencp
     1021 flekkelhea hpwfeflvqc rqvasnltdp klifqaslan aqiliptnqa svssmllegh
     1081 tllalattmy spggvsqvvq neenenclkk vdpqllkmal tpypklktal fpqctppsvl
     1141 psditiyhli qslspfdpsr lfgwqsantl aigdawshlp hfsspdlvnk yaiverlnfa
     1201 yylhngrpsf afgtflvqel iksktpkqli qqvgneayvi glssfhipsi gaacvcflel
     1261 lgldslklrv dmkvaniils ykcrnedaqy sfiresvaek lskladgekt tteellvlle
     1321 egtwnsiqqq eikrlssess sqwalvvqfc rlhnmklsis ylrecakand wlqfiihsql
     1381 hnyhpaevks liqyfspviq dhlrlafenl psvptskmds dqvcnkcpqe lqgskqemtd
     1441 lfeillqcse epdswhwllv eavkqqapil svlasclqga saisclcvwi itsvednvat
     1501 eamghiqdst edhtwnledl sviwrtlltr qksktlirgf qlffkdspll lvmemyelcm
     1561 ffrnykeaea kllefqksle tlntaatkvh pvipamwled qvcfllklml qqcktqyelg
     1621 kllqlfvere hlfsdgpdvk klcilcqilk dtsiainhti itsysienlq hecrsilerl
     1681 qtdgqfalar rvaelaelpv dnlvikeahv acehptgwss meerhllltl aghwlaqedv
     1741 vpldkleele kqiwlcritq htlgrnqeet eprfsrqist sgelsfdsla sefsfsklaa
     1801 lntskyleln slpsketcen rldwkeqesl nfligrlldd gcvheasrvc ryfhfynpdv
     1861 alvlhcrala sgeasmedlh peihallqsa elleeeapdi plrrvhstss ldsqkfvtvp
     1921 ssnevvtnle vltskclhgk nycrqvlcly dlakelgcsy tdvaaqdgea mlrkilasqq
     1981 pdrckraqaf istqglkpdt vaelvaeevt relltssqgt ghkqmfnpte esqtflqltt
     2041 lcqdrtlvgm klldkissvp hgelscttel lilahhcftl tchmegiirv lqaahmltdn
     2101 hlapseeygl vvrlltgigr ynemtyifdl lhkkhyfevl mrkkldpsgt lktalldyik
     2161 rcrpgdsekh nmialcfsmc reigenheaa ariqlklies qpwedslkdg hqlkqlllka
     2221 ltlmldaaes yakdscvrqa qhcqrltkli tlqihflntg qntmlinlgr hklmdcilal
     2281 prfyqasiva eaydfvpdwa eilyqqvilk gdfnyleefk qqrllkssif eeiskkykqh
     2341 qptdmvmenl kklltycedv ylyyklayeh kfyeivnvll kdpqtgcclk dmlag
//
LOCUS       NP_001400603             314 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 7 precursor [Homo sapiens].
ACCESSION   NP_001400603
VERSION     NP_001400603.1
DBSOURCE    REFSEQ: accession NM_001413674.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 314)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 314)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 314)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 314)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 314)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3215172.1,
                                           SRR14038197.666980.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..314
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 7 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=31270
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..314
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            277..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     CDS             1..314
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413674.1:169..1113"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 10"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvsyih gssqaqfvae shiilvlnaa itmgmvllne
      301 aatskgdvgk rrtf
//
LOCUS       NP_001427365            1258 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 isoform 2
            [Homo sapiens].
ACCESSION   NP_001427365 XP_047282846 XP_054224657
VERSION     NP_001427365.1
DBSOURCE    REFSEQ: accession NM_001440436.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1258)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1258)
  AUTHORS   Ji,X., Wu,Q., Cao,X., Liu,S., Zhang,J., Chen,S., Shan,J., Zhang,Y.,
            Li,B. and Zhao,H.
  TITLE     Helicobacter pylori East Asian type CagA hijacks more SHIP2 by its
            EPIYA-D motif to potentiate the oncogenicity
  JOURNAL   Virulence 15 (1), 2375549 (2024)
   PUBMED   38982595
  REMARK    GeneRIF: Helicobacter pylori East Asian type CagA hijacks more
            SHIP2 by its EPIYA-D motif to potentiate the oncogenicity.
REFERENCE   3  (residues 1 to 1258)
  AUTHORS   Ando,K., Kucukali,F., Doeraene,E., Nagaraj,S., Antonelli,E.M.,
            Thazin Htut,M., Yilmaz,Z., Kosa,A.C., Lopez-Guitierrez,L.,
            Quintanilla-Sanchez,C., Aydin,E., Ramos,A.R., Mansour,S.,
            Turbant,S., Schurmans,S., Sleegers,K., Erneux,C., Brion,J.P. and
            Leroy,K.
  CONSRTM   Brain Bank NeuroCEB Neuropathology Network
  TITLE     Alteration of gene expression and protein solubility of the PI
            5-phosphatase SHIP2 are correlated with Alzheimer's disease
            pathology progression
  JOURNAL   Acta Neuropathol 147 (1), 94 (2024)
   PUBMED   38833073
  REMARK    GeneRIF: Alteration of gene expression and protein solubility of
            the PI 5-phosphatase SHIP2 are correlated with Alzheimer's disease
            pathology progression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1258)
  AUTHORS   Bradshaw,W.J., Kennedy,E.C., Moreira,T., Smith,L.A., Chalk,R.,
            Katis,V.L., Benesch,J.L.P., Brennan,P.E., Murphy,E.J. and
            Gileadi,O.
  TITLE     Regulation of inositol 5-phosphatase activity by the C2 domain of
            SHIP1 and SHIP2
  JOURNAL   Structure 32 (4), 453-466 (2024)
   PUBMED   38309262
  REMARK    GeneRIF: Regulation of inositol 5-phosphatase activity by the C2
            domain of SHIP1 and SHIP2.
REFERENCE   5  (residues 1 to 1258)
  AUTHORS   Habib,T., Hejna,J.A., Moses,R.E. and Decker,S.J.
  TITLE     Growth factors and insulin stimulate tyrosine phosphorylation of
            the 51C/SHIP2 protein
  JOURNAL   J Biol Chem 273 (29), 18605-18609 (1998)
   PUBMED   9660833
REFERENCE   6  (residues 1 to 1258)
  AUTHORS   Le Drean,E., Vely,F., Olcese,L., Cambiaggi,A., Guia,S., Krystal,G.,
            Gervois,N., Moretta,A., Jotereau,F. and Vivier,E.
  TITLE     Inhibition of antigen-induced T cell response and antibody-induced
            NK cell cytotoxicity by NKG2A: association of NKG2A with SHP-1 and
            SHP-2 protein-tyrosine phosphatases
  JOURNAL   Eur J Immunol 28 (1), 264-276 (1998)
   PUBMED   9485206
  REMARK    Erratum:[Eur J Immunol 1998 Mar;28(3):1122]
REFERENCE   7  (residues 1 to 1258)
  AUTHORS   Pesesse,X., Deleu,S., De Smedt,F., Drayer,L. and Erneux,C.
  TITLE     Identification of a second SH2-domain-containing protein closely
            related to the phosphatidylinositol polyphosphate 5-phosphatase
            SHIP
  JOURNAL   Biochem Biophys Res Commun 239 (3), 697-700 (1997)
   PUBMED   9367831
REFERENCE   8  (residues 1 to 1258)
  AUTHORS   Hejna,J.A., Saito,H., Merkens,L.S., Tittle,T.V., Jakobs,P.M.,
            Whitney,M.A., Grompe,M., Friedberg,A.S. and Moses,R.E.
  TITLE     Cloning and characterization of a human cDNA (INPPL1) sharing
            homology with inositol polyphosphate phosphatases
  JOURNAL   Genomics 29 (1), 285-287 (1995)
   PUBMED   8530088
REFERENCE   9  (residues 1 to 1258)
  AUTHORS   Huang,S., Earl,D. and White,K.
  TITLE     INPPL1-Related Opsismodysplasia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   40504975
REFERENCE   10 (residues 1 to 1258)
  AUTHORS   Slama,V. and Dudek,J.
  TITLE     [Stability of diluted solutions of peracetic acid]
  JOURNAL   Cesk Farm 17 (1), 40-41 (1968)
   PUBMED   5668240
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000593.4.
            
            On or before May 20, 2025 this sequence version replaced
            XP_047282846.1, XP_054224657.1.
            
            Summary: The protein encoded by this gene is an SH2-containing
            5'-inositol phosphatase that is involved in the regulation of
            insulin function. The encoded protein also plays a role in the
            regulation of epidermal growth factor receptor turnover and actin
            remodelling. Additionally, this gene supports metastatic growth in
            breast cancer and is a valuable biomarker for breast cancer.
            [provided by RefSeq, Jan 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR13170464.553234.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2145774
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1258
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..1258
                     /product="phosphatidylinositol 3,4,5-trisphosphate
                     5-phosphatase 2 isoform 2"
                     /EC_number="3.1.3.86"
                     /note="SH2 domain-containing inositol-5'-phosphatase 2;
                     51C protein; protein 51C; phosphatidylinositol
                     3,4,5-trisphosphate 5-phosphatase 2"
                     /calculated_mol_wt=138468
     Region          17..119
                     /region_name="SH2_SHIP"
                     /note="Src homology 2 (SH2) domain found in SH2-containing
                     inositol-5'-phosphatase (SHIP) and SLAM-associated protein
                     (SAP); cd10343"
                     /db_xref="CDD:198206"
     Site            order(28,47,68,70)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198206"
     Site            order(68..69,81..82,87,90,106..108)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198206"
     Region          119..180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          424..727
                     /region_name="INPP5c_SHIP2-INPPL1"
                     /note="Catalytic inositol polyphosphate 5-phosphatase
                     (INPP5c) domain of SH2 domain containing inositol
                     5-phosphatase-2 and related proteins; cd09101"
                     /db_xref="CDD:197335"
     Site            order(432,434,473,540..541,561,564..565,607,609,611,
                     661..662,684,690,717..718)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197335"
     Site            order(432,473,561,607,609,690,717..718)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197335"
     Site            order(473,540..541,561,564..565,611,661..662,684,717)
                     /site_type="other"
                     /note="putative PI/IP binding site [chemical binding]"
                     /db_xref="CDD:197335"
     Site            order(473,717)
                     /site_type="other"
                     /note="putative Mg binding site [ion binding]"
                     /db_xref="CDD:197335"
     Site            order(561,609,718)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197335"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            890
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          897..1118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Region          <899..1214
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          944..949
                     /region_name="SH3-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Site            958
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17219406,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          983..986
                     /region_name="NPXY motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Site            986
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:11349134,
                     ECO:0000269|PubMed:12235291; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            1131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            1135
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:11687594,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          1194..1256
                     /region_name="SAM_Ship2"
                     /note="SAM domain of Ship2 lipid phosphatase proteins;
                     cd09491"
                     /db_xref="CDD:188890"
     Site            order(1222..1224,1226..1227,1230,1235)
                     /site_type="other"
                     /note="heterodimer interface ML [polypeptide binding]"
                     /db_xref="CDD:188890"
     Site            1257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     CDS             1..1258
                     /gene="INPPL1"
                     /gene_synonym="OPSMD; SHIP2"
                     /coded_by="NM_001440436.1:447..4223"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:3636"
                     /db_xref="HGNC:HGNC:6080"
                     /db_xref="MIM:600829"
ORIGIN      
        1 masacgapgp ggalgsqaps wyhrdlsraa aeellaragr dgsflvrdse svagafalcv
       61 lyqkhvhtyr ilpdgedfla vqtsqgvpvr rfqtlgelig lyaqpnqglv calllpvege
      121 repdppddrd asdgedekpp lpprsgstsi saptgpsspl papetptapa aesapnglst
      181 vshdylkgsy gldleavrgg ashlphltrt latscrrlhs evdkvlsgle ilskvfdqqs
      241 spmvtrllqq qnlpqtgeqe leslvlklsv lkdflsgiqk kalkalqdms stappapqps
      301 trkaktipvq afevkldvtl gdltkigksq kftlsvdveg grlvllrrqr dsqedwttft
      361 hdrirqliks qrvqnklgvv fekekdrtqr kdfifvsark reafcqllql mknkhskqde
      421 pdmisvfigt wnmgsvpppk nvtswftskg lgktldevtv tiphdiyvfg tqensvgdre
      481 wldllrgglk eltdldyrpi amqslwnikv avlvkpehen rishvstssv ktgiantlgn
      541 kgavgvsfmf ngtsfgfvnc hltsgnekta rrnqnyldil rllslgdrql nafdislrft
      601 hlfwfgdlny rldmdiqeil nyisrkefep llrvdqlnle rekhkvflrf seeeisfppt
      661 yryergsrdt yawhkqkptg vrtnvpswcd rilwksypet hiicnsygct ddivtsdhsp
      721 vfgtfevgvt sqfiskkgls ktsdqayief esieaivkta srtkffiefy stcleeykks
      781 fendaqssdn inflkvqwss rqlptlkpil adieylqdqh llltvksmdg yesygecvva
      841 lksmigstaq qfltflshrg eetgnirgsm kvrvpterlg trerlyewis idkdeagaks
      901 kapsvsrgsq eprsgsrkpa fteascplsr lfeepekppp tgrppappra apreepltpr
      961 lkpegapepe gvaapppkns fnnpayyvle gvphqllppe ppsparapvp satknkvait
     1021 vpapqlghhr hprvgegsss deesggtlpp pdfpppplpd saiflppsld plpgpvvrgr
     1081 ggaeargppp pkahprpplp pgpspastfl gevasgddrs csvlqmaktl sevdyapagp
     1141 arsallpgpl elqpprglps dygrplsfpp priresiqed laeeapclqg grasglgeag
     1201 msawlraigl eryeeglvhn gwddleflsd iteedleeag vqdpahkrll ldtlqlsk
//
LOCUS       NP_001428161             248 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 15 [Homo sapiens].
ACCESSION   NP_001428161
VERSION     NP_001428161.1
DBSOURCE    REFSEQ: accession NM_001441232.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 248)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.18528.1,
                                           SRR14038194.3915341.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..248
                     /product="calcium uptake protein 1, mitochondrial isoform
                     15"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=28262
     Region          1..213
                     /region_name="EFh_MICU"
                     /note="EF-hand, calcium binding motif, found in
                     mitochondrial calcium uptake proteins MICU1, MICU2, MICU3,
                     and similar proteins; cl28896"
                     /db_xref="CDD:333716"
     Site            order(3,5,7,14,193,195,197,204)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320081"
     Region          49..79
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          147..176
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          184..213
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     CDS             1..248
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001441232.1:333..1079"
                     /note="isoform 15 is encoded by transcript variant 19"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mfdlngdgev dmeefeqvqs iirsqtsmgm rhrdrpttgn tlksglcsal ttyffgadlk
       61 gkltiknfle fqrklqhdvl kleferhdpv dgriterqfg gmllaysgvq skkltamqrq
      121 lkkhfkegkg ltfqevenff tflknindvd talsfyhmag asldkvtmqq vartvakvel
      181 sdhvcdvvfa lfdcdgngel snkefvsimk qrlmrglekp kdmgftrlmq amwkcaqeta
      241 wdfalpkq
//
LOCUS       NP_001389633            1145 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 14 [Homo sapiens].
ACCESSION   NP_001389633
VERSION     NP_001389633.1
DBSOURCE    REFSEQ: accession NM_001402704.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1145)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1145)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1145)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1145)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1145)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1145)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1145)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1145)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1145)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1145)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2442604.1,
                                           SRR14038191.4378915.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1145
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1145
                     /product="kinectin isoform 14"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=131948
     Region          <142..>400
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          296..1085
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1145
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402704.1:302..3739"
                     /note="isoform 14 is encoded by transcript variant 27"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mvpskrqeal plhqetkqes gsgkkkassk kqktenvfvd eplihattyi plmdnadssp
       61 vvdkrevidl lkpdqvegiq ksgtkklkte tdkenaevkf kdfllslktm mfsedealcv
      121 vdllkeksgv iqdalkkssk gelttlihql qekdkllaav kedaaatkdr ckqltqemmt
      181 ekersnvvit rmkdrigtle kehnvfqnki hvsyqetqqm qmkfqqvreq meaeiahlkq
      241 engilrdavs nttnqleskq saelnklrqd yarlvnelte ktgklqqeev qkknaeqaat
      301 qlkvqlqeae rrweevqsyi rkrtaeheaa qqdlqskfva kenevqslhs kltdtlvskq
      361 qleqrlmqlm eseqkrvnke eslqmqvqdi leqnealkaq iqqfhsqiaa qtsasvlaee
      421 lhkviaekdk qikqtedsla serdrltske eelkdiqnmn fllkaevqkl qalaneqaaa
      481 ahelekmqqs vyvkddkirl leeqlqheis nkmeefkiln dqnkalksev qklqtlvseq
      541 pnkdvveqme kciqekdekl ktveelletg liqvatkeee lnairtenss ltkevqdlka
      601 kqndqvsfas lveelkkvih ekdgkiksve elleaellkv ankektvqdl kqeikalkee
      661 ignvqlekaq qlsitskvqe lqnllkgkee qmntmkavle ekekdlantg kwlqdlqeen
      721 eslkahvqev aqhnlkeass asqfeeleiv lkekenelkr leamlkeres dlssktqllq
      781 dvqdenklfk sqieqlkqqn yqqassfpph eellkviser ekeisglwne ldslkdaveh
      841 qrkknndlre knweameala stekmlqdkv nktskerqqq veaveleake vlkklfpkvs
      901 vpsnlsygew lhgfekkake cmagtsgsee vkvlehklke ademhtllql ecekyksvla
      961 etegilqklq rsveqeenkw kvkvdeshkt ikqmqssfts seqelerlrs enkdienlrr
     1021 erehlemele kaemerstyv tevrelkaql netltklrte qnerqkvagd lhkaqqslel
     1081 iqskivkaag dttviensdv spetesseke tmsvslnqtv tqlqqllqav nqqltkekeh
     1141 yqvle
//
LOCUS       NP_001394195             393 aa            linear   PRI 21-NOV-2025
DEFINITION  cellular tumor antigen p53 isoform a [Homo sapiens].
ACCESSION   NP_001394195
VERSION     NP_001394195.1
DBSOURCE    REFSEQ: accession NM_001407266.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Mirgayazova,R., Khadiullina,R., Chasov,V., Mingaleeva,R.,
            Miftakhova,R., Rizvanov,A. and Bulatov,E.
  TITLE     Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an Option?
  JOURNAL   Genes (Basel) 11 (6), 704 (2020)
   PUBMED   32630614
  REMARK    GeneRIF: Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an
            Option?
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Flynt,E., Bisht,K., Sridharan,V., Ortiz,M., Towfic,F. and
            Thakurta,A.
  TITLE     Prognosis, Biology, and Targeting of TP53 Dysregulation in Multiple
            Myeloma
  JOURNAL   Cells 9 (2), 287 (2020)
   PUBMED   31991614
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Barnoud,T., Parris,J.L.D. and Murphy,M.E.
  TITLE     Common genetic variants in the TP53 pathway and their impact on
            cancer
  JOURNAL   J Mol Cell Biol 11 (7), 578-585 (2019)
   PUBMED   31152665
  REMARK    GeneRIF: Common genetic variants in the TP53 pathway and their
            impact on cancer.
            Review article
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Hu,W., Chen,S., Thorne,R.F. and Wu,M.
  TITLE     TP53, TP53 Target Genes (DRAM, TIGAR), and Autophagy
  JOURNAL   Adv Exp Med Biol 1206, 127-149 (2019)
   PUBMED   31776983
  REMARK    Review article
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Baugh,E.H., Ke,H., Levine,A.J., Bonneau,R.A. and Chan,C.S.
  TITLE     Why are there hotspot mutations in the TP53 gene in human cancers?
  JOURNAL   Cell Death Differ 25 (1), 154-160 (2018)
   PUBMED   29099487
  REMARK    GeneRIF: TP53 missense mutant alleles that occur in human cancers
            are discussed in the context of high resolution models of these p53
            mutant protein structures to determine the structural features of
            mutations (review).
            Review article
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Aubrey,B.J., Strasser,A. and Kelly,G.L.
  TITLE     Tumor-Suppressor Functions of the TP53 Pathway
  JOURNAL   Cold Spring Harb Perspect Med 6 (5), a026062 (2016)
   PUBMED   27141080
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Soussi,T. and Wiman,K.G.
  TITLE     TP53: an oncogene in disguise
  JOURNAL   Cell Death Differ 22 (8), 1239-1249 (2015)
   PUBMED   26024390
  REMARK    Review article
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Soussi,T.
  TITLE     The TP53 gene network in a postgenomic era
  JOURNAL   Hum Mutat 35 (6), 641-642 (2014)
   PUBMED   24753184
  REMARK    GeneRIF: Recommendations and guidelines for reporting and
            annotating TP53 variants are also provided, to help researchers
            generate standardized data that are easy to understand, analyze,
            and exchange across various cancer variant databases
            Review article
REFERENCE   9  (residues 1 to 393)
  AUTHORS   Anczukow,O., Ware,M.D., Buisson,M., Zetoune,A.B.,
            Stoppa-Lyonnet,D., Sinilnikova,O.M. and Mazoyer,S.
  TITLE     Does the nonsense-mediated mRNA decay mechanism prevent the
            synthesis of truncated BRCA1, CHK2, and p53 proteins?
  JOURNAL   Hum Mutat 29 (1), 65-73 (2008)
   PUBMED   17694537
  REMARK    GeneRIF: the p53 protein encoded by the 770delT allele is as
            abundant as the wild-type protein, as removal of the C-terminal p53
            domain leads to a stabilized mutant protein, whose abundance is
            markedly increased when NMD is inhibited.
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Bourdon,J.C.
  TITLE     p53 Family isoforms
  JOURNAL   Curr Pharm Biotechnol 8 (6), 332-336 (2007)
   PUBMED   18289041
  REMARK    Review article
REFERENCE   11 (residues 1 to 393)
  AUTHORS   Candeias,M.M., Powell,D.J., Roubalova,E., Apcher,S., Bourougaa,K.,
            Vojtesek,B., Bruzzoni-Giovanelli,H. and Fahraeus,R.
  TITLE     Expression of p53 and p53/47 are controlled by alternative
            mechanisms of messenger RNA translation initiation
  JOURNAL   Oncogene 25 (52), 6936-6947 (2006)
   PUBMED   16983332
  REMARK    GeneRIF: harbouring alternative translation initiation sites, the
            p53 mRNA gives rise to different levels of the p53 isoforms which
            help to orchestrate the cell biological outcome of p53 activation
REFERENCE   12 (residues 1 to 393)
  AUTHORS   Murray-Zmijewski,F., Lane,D.P. and Bourdon,J.C.
  TITLE     p53/p63/p73 isoforms: an orchestra of isoforms to harmonise cell
            differentiation and response to stress
  JOURNAL   Cell Death Differ 13 (6), 962-972 (2006)
   PUBMED   16601753
  REMARK    Review article
REFERENCE   13 (residues 1 to 393)
  AUTHORS   Bourdon,J.C., Fernandes,K., Murray-Zmijewski,F., Liu,G., Diot,A.,
            Xirodimas,D.P., Saville,M.K. and Lane,D.P.
  TITLE     p53 isoforms can regulate p53 transcriptional activity
  JOURNAL   Genes Dev 19 (18), 2122-2137 (2005)
   PUBMED   16131611
  REMARK    GeneRIF: p53 isoforms can regulate p53 transcriptional activity.
REFERENCE   14 (residues 1 to 393)
  AUTHORS   Ghosh,A., Stewart,D. and Matlashewski,G.
  TITLE     Regulation of human p53 activity and cell localization by
            alternative splicing
  JOURNAL   Mol Cell Biol 24 (18), 7987-7997 (2004)
   PUBMED   15340061
  REMARK    GeneRIF: mechanism of p53 regulation originating through
            alternative splicing of the human p53 gene resulting in the
            expression of a novel p53 mRNA
REFERENCE   15 (residues 1 to 393)
  AUTHORS   Flaman,J.M., Waridel,F., Estreicher,A., Vannier,A., Limacher,J.M.,
            Gilbert,D., Iggo,R. and Frebourg,T.
  TITLE     The human tumour suppressor gene p53 is alternatively spliced in
            normal cells
  JOURNAL   Oncogene 12 (4), 813-818 (1996)
   PUBMED   8632903
REFERENCE   16 (residues 1 to 393)
  AUTHORS   Schneider,K., Zelley,K., Nichols,K.E., Schwartz Levine,A. and
            Garber,J.
  TITLE     Li-Fraumeni Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301488
REFERENCE   17 (residues 1 to 393)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   18 (residues 1 to 393)
  AUTHORS   Lamb,P. and Crawford,L.
  TITLE     Characterization of the human p53 gene
  JOURNAL   Mol Cell Biol 6 (5), 1379-1385 (1986)
   PUBMED   2946935
REFERENCE   19 (residues 1 to 393)
  AUTHORS   Isobe,M., Emanuel,B.S., Givol,D., Oren,M. and Croce,C.M.
  TITLE     Localization of gene for human p53 tumour antigen to band 17p13
  JOURNAL   Nature 320 (6057), 84-85 (1986)
   PUBMED   3456488
REFERENCE   20 (residues 1 to 393)
  AUTHORS   Benchimol,S., Lamb,P., Crawford,L.V., Sheer,D., Shows,T.B.,
            Bruns,G.A. and Peacock,J.
  TITLE     Transformation associated p53 protein is encoded by a gene on human
            chromosome 17
  JOURNAL   Somat Cell Mol Genet 11 (5), 505-510 (1985)
   PUBMED   2994241
REFERENCE   21 (residues 1 to 393)
  AUTHORS   Harlow,E., Williamson,N.M., Ralston,R., Helfman,D.M. and Adams,T.E.
  TITLE     Molecular cloning and in vitro expression of a cDNA clone for human
            cellular tumor antigen p53
  JOURNAL   Mol Cell Biol 5 (7), 1601-1610 (1985)
   PUBMED   3894933
REFERENCE   22 (residues 1 to 393)
  AUTHORS   Zakut-Houri,R., Bienz-Tadmor,B., Givol,D. and Oren,M.
  TITLE     Human p53 cellular tumor antigen: cDNA sequence and expression in
            COS cells
  JOURNAL   EMBO J 4 (5), 1251-1255 (1985)
   PUBMED   4006916
REFERENCE   23 (residues 1 to 393)
  AUTHORS   Matlashewski,G., Lamb,P., Pim,D., Peacock,J., Crawford,L. and
            Benchimol,S.
  TITLE     Isolation and characterization of a human p53 cDNA clone:
            expression of the human p53 gene
  JOURNAL   EMBO J 3 (13), 3257-3262 (1984)
   PUBMED   6396087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087388.9 and AC007421.13.
            
            Summary: This gene encodes a tumor suppressor protein containing
            transcriptional activation, DNA binding, and oligomerization
            domains. The encoded protein responds to diverse cellular stresses
            to regulate expression of target genes, thereby inducing cell cycle
            arrest, apoptosis, senescence, DNA repair, or changes in
            metabolism. Mutations in this gene are associated with a variety of
            human cancers, including hereditary cancers such as Li-Fraumeni
            syndrome. Alternative splicing of this gene and the use of
            alternate promoters result in multiple transcript variants and
            isoforms. Additional isoforms have also been shown to result from
            the use of alternate translation initiation codons from identical
            transcript variants (PMIDs: 12032546, 20937277). [provided by
            RefSeq, Dec 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.139836.1,
                                           SRR14038195.336928.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..393
                     /product="cellular tumor antigen p53 isoform a"
                     /note="tumor protein 53; mutant tumor protein 53; cellular
                     tumor antigen p53; phosphoprotein p53;
                     transformation-related protein 53; antigen NY-CO-13; tumor
                     supressor p53"
                     /calculated_mol_wt=43522
     Region          1..320
                     /region_name="Interaction with CCAR2.
                     /evidence=ECO:0000269|PubMed:25732823"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          1..83
                     /region_name="Interaction with HRMT1L2.
                     /evidence=ECO:0000269|PubMed:15186775"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          1..44
                     /region_name="Transcription activation (acidic)"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          6..30
                     /region_name="P53_TAD"
                     /note="P53 transactivation motif; pfam08563"
                     /db_xref="CDD:462520"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by HIPK4.
                     /evidence=ECO:0000269|PubMed:18022393; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5, PRPK, AMPK, NUAK1 and ATM.
                     /evidence=ECO:0000269|PubMed:10570149,
                     ECO:0000269|PubMed:11554766, ECO:0000269|PubMed:15866171,
                     ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:17591690,
                     ECO:0000269|PubMed:17967874, ECO:0000269|PubMed:21317932,
                     ECO:0000269|PubMed:28842590; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          17..25
                     /region_name="TADI"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK1, VRK1 and VRK2.
                     /evidence=ECO:0000269|PubMed:10606744,
                     ECO:0000269|PubMed:10951572, ECO:0000269|PubMed:16704422,
                     ECO:0000269|PubMed:31527692; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CHEK2, CK1 and PLK3.
                     /evidence=ECO:0000269|PubMed:10570149,
                     ECO:0000269|PubMed:11447225, ECO:0000269|PubMed:11551930,
                     ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:20041275;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5 and CDK7.
                     /evidence=ECO:0000269|PubMed:17591690,
                     ECO:0000269|PubMed:9372954; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          35..59
                     /region_name="TAD2"
                     /note="Transactivation domain 2; pfam18521"
                     /db_xref="CDD:375947"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK5.
                     /evidence=ECO:0000269|PubMed:17254968; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK5, DYRK2, HIPK2 and PKC/PRKCG.
                     /evidence=ECO:0000269|PubMed:11740489,
                     ECO:0000269|PubMed:11780126, ECO:0000269|PubMed:16377624,
                     ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:17591690;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          48..56
                     /region_name="TADII"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          50..96
                     /region_name="Disordered.
                     /evidence=ECO:0000269|PubMed:31953488"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by TAF1 and GRK5.
                     /evidence=ECO:0000269|PubMed:15053879,
                     ECO:0000269|PubMed:20124405; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          66..110
                     /region_name="Interaction with WWOX"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          100..370
                     /region_name="Interaction with HIPK1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          100..300
                     /region_name="Required for interaction with ZNF385A.
                     /evidence=ECO:0000269|PubMed:17719541"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          109..288
                     /region_name="P53"
                     /note="P53 DNA-binding domain; cd08367"
                     /db_xref="CDD:176262"
     Region          113..236
                     /region_name="Required for interaction with FBXO42.
                     /evidence=ECO:0000269|PubMed:19509332"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          116..292
                     /region_name="Interaction with AXIN1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            120
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000269|PubMed:16793544,
                     ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            120
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:17189187,
                     ECO:0000269|PubMed:19854137, ECO:0000269|PubMed:23431171;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            order(176,179,238,242)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:176262"
     Site            order(177..179,181)
                     /site_type="other"
                     /note="dimerization site [polypeptide binding]"
                     /db_xref="CDD:176262"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB.
                     /evidence=ECO:0000269|PubMed:20959462; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            order(239,241,248,273,275..277,280)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176262"
     Region          241..248
                     /region_name="Interaction with the 53BP2 SH3 domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          256..294
                     /region_name="Interaction with E4F1.
                     /evidence=ECO:0000269|PubMed:10644996"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB.
                     /evidence=ECO:0000269|PubMed:20959462; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          273..280
                     /region_name="Interaction with DNA"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          282..325
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AURKB.
                     /evidence=ECO:0000269|PubMed:20959462; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          300..393
                     /region_name="Interaction with CARM1.
                     /evidence=ECO:0000269|PubMed:15186775"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          305..321
                     /region_name="Bipartite nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            305
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:12724314; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKA, CDK1 and CDK2.
                     /evidence=ECO:0000269|PubMed:10884347,
                     ECO:0000269|PubMed:14702041; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          319..360
                     /region_name="Interaction with HIPK2"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          319..358
                     /region_name="P53_tetramer"
                     /note="P53 tetramerization motif; pfam07710"
                     /db_xref="CDD:462238"
     Site            321
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P02340; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          325..356
                     /region_name="Oligomerization"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            333
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, by PRMT5.
                     /evidence=ECO:0000269|PubMed:19011621; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            335
                     /site_type="methylation"
                     /note="Symmetric dimethylarginine, by PRMT5.
                     /evidence=ECO:0000269|PubMed:19011621; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            337
                     /site_type="methylation"
                     /note="Symmetric dimethylarginine, by PRMT5.
                     /evidence=ECO:0000269|PubMed:19011621; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          339..350
                     /region_name="Nuclear export signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          351..393
                     /region_name="Disordered.
                     /evidence=ECO:0000269|PubMed:31953488,
                     ECO:0000269|PubMed:36108750"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          359..363
                     /region_name="Interaction with USP7"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          368..387
                     /region_name="Basic (repression of DNA-binding)"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Region          370..372
                     /region_name="[KR]-[STA]-K motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            370
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:17108971,
                     ECO:0000269|PubMed:22864287; N6-methyllysine, by SMYD2,
                     alternate. /evidence=ECO:0000269|PubMed:17108971,
                     ECO:0000269|PubMed:22864287; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            372
                     /site_type="methylation"
                     /note="N6-methyllysine, by SETD7.
                     /evidence=ECO:0000269|PubMed:15525938,
                     ECO:0000269|PubMed:16415881; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            373
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, by EHMT1 and EHMT2,
                     alternate. /evidence=ECO:0000269|PubMed:20118233;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            373
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:10656795; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Region          374..393
                     /region_name="Interaction with MORN3.
                     /evidence=ECO:0000269|PubMed:29681526"
                     /note="propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            381
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:29474172,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            382
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:17707234,
                     ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22864287;
                     N6-methyllysine, by KMT5A, alternate.
                     /evidence=ECO:0000269|PubMed:17707234,
                     ECO:0000269|PubMed:20870725, ECO:0000269|PubMed:22864287;
                     propagated from UniProtKB/Swiss-Prot (P04637.4)"
     Site            382
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:10656795,
                     ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:20228809,
                     ECO:0000269|PubMed:23431171, ECO:0000269|PubMed:29681526,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2, CDK2 and NUAK1.
                     /evidence=ECO:0000269|PubMed:10884347,
                     ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:17108107,
                     ECO:0000269|PubMed:21317932, ECO:0000269|PubMed:22214662,
                     ECO:0000269|PubMed:35618207; propagated from
                     UniProtKB/Swiss-Prot (P04637.4)"
     CDS             1..393
                     /gene="TP53"
                     /gene_synonym="BCC7; BMFS5; LFS1; P53; TRP53"
                     /coded_by="NM_001407266.1:156..1337"
                     /note="isoform a is encoded by transcript variant 11"
                     /db_xref="GeneID:7157"
                     /db_xref="HGNC:HGNC:11998"
                     /db_xref="MIM:191170"
ORIGIN      
        1 meepqsdpsv epplsqetfs dlwkllpenn vlsplpsqam ddlmlspddi eqwftedpgp
       61 deaprmpeaa ppvapapaap tpaapapaps wplsssvpsq ktyqgsygfr lgflhsgtak
      121 svtctyspal nkmfcqlakt cpvqlwvdst pppgtrvram aiykqsqhmt evvrrcphhe
      181 rcsdsdglap pqhlirvegn lrveylddrn tfrhsvvvpy eppevgsdct tihynymcns
      241 scmggmnrrp iltiitleds sgnllgrnsf evrvcacpgr drrteeenlr kkgephhelp
      301 pgstkralpn ntssspqpkk kpldgeyftl qirgrerfem frelnealel kdaqagkepg
      361 gsrahsshlk skkgqstsrh kklmfktegp dsd
//
LOCUS       NP_001425934            1298 aa            linear   PRI 21-NOV-2025
DEFINITION  receptor tyrosine-protein kinase erbB-4 isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_001425934 XP_005246433 XP_054196998
VERSION     NP_001425934.1
DBSOURCE    REFSEQ: accession NM_001439005.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1298)
  AUTHORS   Li,X., Zhang,H., Li,W., Tuo,H., He,B. and Jiang,H.
  TITLE     The role and mechanism of NRG1/ErbB4 in inducing the
            differentiation of induced pluripotent stem cells into
            cardiomyocytes
  JOURNAL   BMC Cardiovasc Disord 24 (1), 559 (2024)
   PUBMED   39407109
  REMARK    GeneRIF: The role and mechanism of NRG1/ErbB4 in inducing the
            differentiation of induced pluripotent stem cells into
            cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1298)
  AUTHORS   Singh,P.K., Kim,S. and Smith,A.W.
  TITLE     HER4 is a high-affinity dimerization partner for all EGFR/HER/ErbB
            family proteins
  JOURNAL   Protein Sci 33 (10), e5171 (2024)
   PUBMED   39276020
  REMARK    GeneRIF: HER4 is a high-affinity dimerization partner for all
            EGFR/HER/ErbB family proteins.
REFERENCE   3  (residues 1 to 1298)
  AUTHORS   Adashek,J.J., Pandya,C., Maragakis,N.J., De,P., Cohen,P.R., Kato,S.
            and Kurzrock,R.
  TITLE     Neuregulin-1 and ALS19 (ERBB4): at the crossroads of amyotrophic
            lateral sclerosis and cancer
  JOURNAL   BMC Med 22 (1), 74 (2024)
   PUBMED   38369520
  REMARK    GeneRIF: Neuregulin-1 and ALS19 (ERBB4): at the crossroads of
            amyotrophic lateral sclerosis and cancer.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1298)
  AUTHORS   Li,R., Wang,Y., Yang,L., Zhong,P., Huang,G., Liang,Q. and Yu,X.
  TITLE     Genetic variants of ERBB4 gene and risk of gestational diabetes
            mellitus: a susceptibility and diagnostic nomogram study
  JOURNAL   Front Endocrinol (Lausanne) 14, 1283539 (2023)
   PUBMED   38149095
  REMARK    GeneRIF: Genetic variants of ERBB4 gene and risk of gestational
            diabetes mellitus: a susceptibility and diagnostic nomogram study.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1298)
  AUTHORS   Tang,R., Cui,H., Dou,R., Tao,L., Tan,L., Guo,T. and Luo,D.
  TITLE     ErbB4 affects Th1/Th17 cell differentiation and promotes psoriasis
            progression
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (12), 1-5 (2023)
   PUBMED   38063127
  REMARK    GeneRIF: ErbB4 affects Th1/Th17 cell differentiation and promotes
            psoriasis progression.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1298)
  AUTHORS   Barbacci,E.G., Guarino,B.C., Stroh,J.G., Singleton,D.H.,
            Rosnack,K.J., Moyer,J.D. and Andrews,G.C.
  TITLE     The structural basis for the specificity of epidermal growth factor
            and heregulin binding
  JOURNAL   J Biol Chem 270 (16), 9585-9589 (1995)
   PUBMED   7721889
  REMARK    Erratum:[J Biol Chem 1995 Nov 24;270(47):28494]
REFERENCE   7  (residues 1 to 1298)
  AUTHORS   Zimonjic,D.B., Alimandi,M., Miki,T., Popescu,N.C. and Kraus,M.H.
  TITLE     Localization of the human HER4/erbB-4 gene to chromosome 2
  JOURNAL   Oncogene 10 (6), 1235-1237 (1995)
   PUBMED   7700649
REFERENCE   8  (residues 1 to 1298)
  AUTHORS   Nagata,K., Kohda,D., Hatanaka,H., Ichikawa,S., Matsuda,S.,
            Yamamoto,T., Suzuki,A. and Inagaki,F.
  TITLE     Solution structure of the epidermal growth factor-like domain of
            heregulin-alpha, a ligand for p180erbB-4
  JOURNAL   EMBO J 13 (15), 3517-3523 (1994)
   PUBMED   8062828
REFERENCE   9  (residues 1 to 1298)
  AUTHORS   Culouscou,J.M., Plowman,G.D., Carlton,G.W., Green,J.M. and
            Shoyab,M.
  TITLE     Characterization of a breast cancer cell differentiation factor
            that specifically activates the HER4/p180erbB4 receptor
  JOURNAL   J Biol Chem 268 (25), 18407-18410 (1993)
   PUBMED   7689552
REFERENCE   10 (residues 1 to 1298)
  AUTHORS   Siddique,N. and Siddique,T.
  TITLE     Amyotrophic Lateral Sclerosis Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC096765.3, AC096547.1,
            AC093823.2, AC105921.5, AC068970.6 and AC012069.10.
            
            On or before Apr 25, 2025 this sequence version replaced
            XP_005246433.1, XP_054196998.1.
            
            Summary: This gene is a member of the Tyr protein kinase family and
            the epidermal growth factor receptor subfamily. It encodes a
            single-pass type I membrane protein with multiple cysteine rich
            domains, a transmembrane domain, a tyrosine kinase domain, a
            phosphotidylinositol-3 kinase binding site and a PDZ domain binding
            motif. The protein binds to and is activated by neuregulins and
            other factors and induces a variety of cellular responses including
            mitogenesis and differentiation. Multiple proteolytic events allow
            for the release of a cytoplasmic fragment and an extracellular
            fragment. Mutations in this gene have been associated with cancer.
            Alternatively spliced variants which encode different protein
            isoforms have been described; however, not all variants have been
            fully characterized. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143747.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1298
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..1298
                     /product="receptor tyrosine-protein kinase erbB-4 isoform
                     3 precursor"
                     /EC_number="2.7.10.1"
                     /note="receptor tyrosine-protein kinase erbB-4; tyrosine
                     kinase-type cell surface receptor HER4; avian
                     erythroblastic leukemia viral (v-erb-b2) oncogene homolog
                     4; proto-oncogene-like protein c-ErbB-4; v-erb-a
                     erythroblastic leukemia viral oncogene homolog 4; v-erb-b2
                     avian erythroblastic leukemia viral oncogene homolog 4;
                     human epidermal growth factor receptor 4"
                     /calculated_mol_wt=142983
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
                     /calculated_mol_wt=2614
     Region          55..167
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16203964; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            174
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16203964; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Region          186..332
                     /region_name="Furin-like"
                     /note="Furin-like cysteine rich region; pfam00757"
                     /db_xref="CDD:395614"
     Site            253
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16203964; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Region          358..478
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Site            358
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16203964; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            410
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16203964; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            473
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16203964; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            495
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16203964; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Region          502..634
                     /region_name="GF_recep_IV"
                     /note="Growth factor receptor domain IV; pfam14843"
                     /db_xref="CDD:464344"
     Site            548
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            576
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16203964; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            620
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Region          632..675
                     /region_name="TM_ErbB4"
                     /note="Transmembrane domain of ErbB4, a Protein Tyrosine
                     Kinase; cd12092"
                     /db_xref="CDD:213053"
     Site            order(632..633,635..638,641..642,645..646,649..650,
                     653..654,657,661)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:213053"
     Site            642..665
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15303.1)"
     mat_peptide     666..1298
                     /product="ERBB4 intracellular domain.
                     /evidence=ECO:0000250. /id=PRO_0000396797"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15303.1)"
                     /calculated_mol_wt=71995
     Region          666..674
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15303.1)"
     Region          700..1002
                     /region_name="PTKc_HER4"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     HER4; cd05110"
                     /db_xref="CDD:173655"
     Site            order(714..715,722,739,741,762,784,786..787,789,837..838,
                     840,851,872..876,881,885)
                     /site_type="active"
                     /db_xref="CDD:173655"
     Site            order(714..715,722,739,741,762,784,786..787,789,837..838,
                     840,851)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173655"
     Site            850..875
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173655"
     Site            865
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            order(872..876,881,885)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173655"
     Region          1022..1025
                     /region_name="PPxY motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15303.1)"
     Site            1025
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Region          1043..1046
                     /region_name="PPxY motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15303.1)"
     Site            1046
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:17120616,
                     ECO:0000269|PubMed:18721752, ECO:0000269|PubMed:8617750;
                     propagated from UniProtKB/Swiss-Prot (Q15303.1)"
     Region          1107..1140
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15303.1)"
     Site            1140
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            1152
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            1178
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752,
                     ECO:0000269|PubMed:8617750; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            1192
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            1232
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752,
                     ECO:0000269|PubMed:8617750; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            1248
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            1274
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Region          1288..1291
                     /region_name="PPxY motif 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15303.1)"
     Region          1296..1298
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15303.1)"
     CDS             1..1298
                     /gene="ERBB4"
                     /gene_synonym="ALS19; HER4; p180erbB4"
                     /coded_by="NM_001439005.1:273..4169"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:2066"
                     /db_xref="HGNC:HGNC:3432"
                     /db_xref="MIM:600543"
ORIGIN      
        1 mkpatglwvw vsllvaagtv qpsdsqsvca gtenklssls dleqqyralr kyyencevvm
       61 gnleitsieh nrdlsflrsv revtgyvlva lnqfrylple nlriirgtkl yedryalaif
      121 lnyrkdgnfg lqelglknlt eilnggvyvd qnkflcyadt ihwqdivrnp wpsnltlvst
      181 ngssgcgrch ksctgrcwgp tenhcqtltr tvcaeqcdgr cygpyvsdcc hrecaggcsg
      241 pkdtdcfacm nfndsgacvt qcpqtfvynp ttfqlehnfn akytygafcv kkcphnfvvd
      301 ssscvracps skmeveengi kmckpctdic pkacdgigtg slmsaqtvds snidkfinct
      361 kingnliflv tgihgdpyna ieaidpekln vfrtvreitg flniqswppn mtdfsvfsnl
      421 vtiggrvlys glsllilkqq gitslqfqsl keisagniyi tdnsnlcyyh tinwttlfst
      481 inqrivirdn rkaenctaeg mvcnhlcssd gcwgpgpdqc lscrrfsrgr iciescnlyd
      541 gefrefengs icvecdpqce kmedglltch gpgpdnctkc shfkdgpncv ekcpdglqga
      601 nsfifkyadp drechpchpn ctqgcigssi edciglmdrt pliaagvigg lfilvivglt
      661 favyvrrksi kkkralrrfl etelvepltp sgtapnqaql rilketelkr vkvlgsgafg
      721 tvykgiwvpe getvkipvai kilnettgpk anvefmdeal imasmdhphl vrllgvclsp
      781 tiqlvtqlmp hgclleyvhe hkdnigsqll lnwcvqiakg mmyleerrlv hrdlaarnvl
      841 vkspnhvkit dfglarlleg dekeynadgg kmpikwmale cihyrkfthq sdvwsygvti
      901 welmtfggkp ydgiptreip dllekgerlp qppictidvy mvmvkcwmid adsrpkfkel
      961 aaefsrmard pqrylviqgd drmklpspnd skffqnllde edledmmdae eylvpqafni
     1021 pppiytsrar idsnrseigh spppaytpms gnqfvyrdgg faaeqgvsvp yraptstipe
     1081 apvaqgatae ifddsccngt lrkpvaphvq edsstqrysa dptvfapers prgeldeegy
     1141 mtpmrdkpkq eylnpveenp fvsrrkngdl qaldnpeyhn asngppkaed eyvneplyln
     1201 tfantlgkae ylknnilsmp ekakkafdnp dywnhslppr stlqhpdylq eystkyfykq
     1261 ngrirpivae npeylsefsl kpgtvlpppp yrhrntvv
//
LOCUS       NP_001393539            1113 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 4 [Homo sapiens].
ACCESSION   NP_001393539
VERSION     NP_001393539.1
DBSOURCE    REFSEQ: accession NM_001406610.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1113)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1113)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1113)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1113)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1113)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1113)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1113)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1113)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1113)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1113)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1975713.1,
                                           SRR14038193.1712546.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1113
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1113
                     /product="hamartin isoform 4"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=123884
     Region          7..668
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <657..>909
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1113
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406610.1:189..3530"
                     /note="isoform 4 is encoded by transcript variant 24"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk mdtdvvvltt gvlvlitmlp mipqsgkqhl ldffdifgrl sswclkkpgh
      121 vaevylvhlh asvyalfhrl ygmypcnfvs flrshysmke nletfeevvk pmmehvrihp
      181 elvtgskdhe ldprrwkrle thdvviecak isldpteasy edgysvshqi sarfphrsad
      241 vttspyadtq nsygcatstp ystsrlmlln mpgqlpqtls spstrlitep pqatlwspsm
      301 vcgmttppts pgnvppdlsh pyskvfgtta ggkgtplgtp atspppaplc hsddyvhisl
      361 pqatvtpprk eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed
      421 siekdkeeaa isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv
      481 npeplhssld klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp
      541 trvgfgsgqp ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr
      601 liqqgadahs kelnklplps ksvdwthfgg sppsdeirtl rdqllllhnq llyerfkrqq
      661 halrnrrllr kvikaaalee hnaamkdqlk lqekdiqmwk vslqkeqary nqlqeqrdtm
      721 vtklhsqirq lqhdreefyn qsqelqtkle dcrnmiaelr ielkkannkv chtelllsqv
      781 sqklsnsesv qqqmeflnrq llvlgevnel yleqlqnkhs dttkevemmk aayrkelekn
      841 rshvlqqtqr ldtsqkrile leshlakkdh llleqkkyle dvklqargql qaaesryeaq
      901 kritqvfele ildlygrlek dgllkkleee kaeaaeaaee rldccndgcs dsmvghneea
      961 sghngetktp rpssargssg srggggssss sselstpekp phqragpfss rwettmgeas
     1021 asipttvgsl pssksflgmk arelfrnkse sqcdedgmts slseslktel gkdlgveaki
     1081 plnldgphps pptpdsvgql himdynethh ehs
//
LOCUS       NP_001403221             754 aa            linear   PRI 21-NOV-2025
DEFINITION  oxysterol-binding protein-related protein 9 isoform j [Homo
            sapiens].
ACCESSION   NP_001403221
VERSION     NP_001403221.1
DBSOURCE    REFSEQ: accession NM_001416292.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Cabukusta,B., Borst Pauwels,S., Akkermans,J.J.L.L., Blomberg,N.,
            Mulder,A.A., Koning,R.I., Giera,M. and Neefjes,J.
  TITLE     The ORP9-ORP11 dimer promotes sphingomyelin synthesis
  JOURNAL   Elife 12, 91345 (2024)
   PUBMED   39106189
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 754)
  AUTHORS   He,R., Liu,F., Wang,H., Huang,S., Xu,K., Zhang,C., Liu,Y. and Yu,H.
  TITLE     ORP9 and ORP10 form a heterocomplex to transfer
            phosphatidylinositol 4-phosphate at ER-TGN contact sites
  JOURNAL   Cell Mol Life Sci 80 (3), 77 (2023)
   PUBMED   36853333
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Tan,J.X. and Finkel,T.
  TITLE     A phosphoinositide signalling pathway mediates rapid lysosomal
            repair
  JOURNAL   Nature 609 (7928), 815-821 (2022)
   PUBMED   36071159
REFERENCE   4  (residues 1 to 754)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 754)
  AUTHORS   Hacker,B., Schultheiss,C., Doring,M. and Kurzik-Dumke,U.
  TITLE     Molecular partners of hNOT/ALG3, the human counterpart of the
            Drosophila NOT and yeast ALG3 gene, suggest its involvement in
            distinct cellular processes relevant to congenital disorders of
            glycosylation, cancer, neurodegeneration and a variety of further
            pathologies
  JOURNAL   Hum Mol Genet 27 (11), 1858-1878 (2018)
   PUBMED   29547901
REFERENCE   6  (residues 1 to 754)
  AUTHORS   Gauci,S., Helbig,A.O., Slijper,M., Krijgsveld,J., Heck,A.J. and
            Mohammed,S.
  TITLE     Lys-N and trypsin cover complementary parts of the phosphoproteome
            in a refined SCX-based approach
  JOURNAL   Anal Chem 81 (11), 4493-4501 (2009)
   PUBMED   19413330
  REMARK    GeneRIF: Includes data showing N-alpha terminal acetylation of this
            protein (OSBL9_HUMAN), which begins with nASIMEGPLSK following
            cleavage of the initiating Met-1 residue.
REFERENCE   7  (residues 1 to 754)
  AUTHORS   Lessmann,E., Ngo,M., Leitges,M., Minguet,S., Ridgway,N.D. and
            Huber,M.
  TITLE     Oxysterol-binding protein-related protein (ORP) 9 is a PDK-2
            substrate and regulates Akt phosphorylation
  JOURNAL   Cell Signal 19 (2), 384-392 (2007)
   PUBMED   16962287
  REMARK    GeneRIF: Furthermore, mammalian target of rapamycin was implicated
            in ORP9L phosphorylation in HEK293 cells. These studies identify
            ORP9 as a PDK-2 substrate and negative regulator of Akt
            phosphorylation at the PDK-2 site.
REFERENCE   8  (residues 1 to 754)
  AUTHORS   Wyles,J.P. and Ridgway,N.D.
  TITLE     VAMP-associated protein-A regulates partitioning of
            oxysterol-binding protein-related protein-9 between the endoplasmic
            reticulum and Golgi apparatus
  JOURNAL   Exp Cell Res 297 (2), 533-547 (2004)
   PUBMED   15212954
REFERENCE   9  (residues 1 to 754)
  AUTHORS   Jaworski,C.J., Moreira,E., Li,A., Lee,R. and Rodriguez,I.R.
  TITLE     A family of 12 human genes containing oxysterol-binding domains
  JOURNAL   Genomics 78 (3), 185-196 (2001)
   PUBMED   11735225
REFERENCE   10 (residues 1 to 754)
  AUTHORS   Lehto,M., Laitinen,S., Chinetti,G., Johansson,M., Ehnholm,C.,
            Staels,B., Ikonen,E. and Olkkonen,V.M.
  TITLE     The OSBP-related protein family in humans
  JOURNAL   J Lipid Res 42 (8), 1203-1213 (2001)
   PUBMED   11483621
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104170.2, AL772260.3,
            AL831767.8 and AL050343.17.
            
            Summary: This gene encodes a member of the oxysterol-binding
            protein (OSBP) family, a group of intracellular lipid receptors.
            Most members contain an N-terminal pleckstrin homology domain and a
            highly conserved C-terminal OSBP-like sterol-binding domain,
            although some members contain only the sterol-binding domain. This
            family member functions as a cholesterol transfer protein that
            regulates Golgi structure and function. Multiple transcript
            variants, most of which encode distinct isoforms, have been
            identified. Related pseudogenes have been identified on chromosomes
            3, 11 and 12. [provided by RefSeq, Jul 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853565.867.1,
                                           SRR14038194.774993.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..754
                     /product="oxysterol-binding protein-related protein 9
                     isoform j"
                     /note="oxysterol-binding protein-related protein 9;
                     OSBP-related protein 9"
                     /calculated_mol_wt=85052
     Region          23..124
                     /region_name="PH_ORP9"
                     /note="Human Oxysterol binding protein related protein 9
                     Pleckstrin homology (PH) domain; cd13290"
                     /db_xref="CDD:241444"
     Region          395..741
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     CDS             1..754
                     /gene="OSBPL9"
                     /gene_synonym="ORP-9; ORP9"
                     /coded_by="NM_001416292.1:499..2763"
                     /note="isoform j is encoded by transcript variant 13"
                     /db_xref="GeneID:114883"
                     /db_xref="HGNC:HGNC:16386"
                     /db_xref="MIM:606737"
ORIGIN      
        1 mpyrrvtsgr llslaapkma simegplskw tnvmkgwqyr wfvldynagl lsyytskdkm
       61 mrgsrrgcvr lrgavigidd eddstftitv dqktfhfqar daderekwih aleetilrht
      121 lqlqgldsgf vpsvqdfdkk lteadaylqi lieqlklfdd klqnckedeq rkkietlket
      181 tnsmvesikh civllqiakd qsnaekhadg mistinpvda iyqpsplepv istmpsqtvl
      241 ppepvqlcks eqrpsslpvg pvlatlghhq tptpnstgsg hsppssslts pshvnlspnt
      301 vpefsyssse defydadefh qsgsspkrli dssgsasvlt hsssgnslkr pdtteslnss
      361 lsngtsdadl fdshddrddd aeagsveehk svimhllsqv rlgmdltkvv lptfilerrs
      421 llemyadffa hpdlfvsisd qkdpkdrmvq vvkwylsafh agrkgsvakk pynpilgeif
      481 qchwtlpndt eentelvseg pvpwvsknsv tfvaeqvshh ppisafyaec fnkkiqfnah
      541 iwtkskflgm sigvhnigqg cvscldydeh yiltfpngyg rsiltvpwve lggecnincs
      601 ktgysaniif htkpfyggkk hritaeifsp ndkksfcsie gewngvmyak yatgentvfv
      661 dtkklpiikk kvrkledqne yesrslwkdv tfnlkirdid aateakhrle erqraearer
      721 kekeiqwetr lfhedgecwv ydepllkrlg aakh
//
LOCUS       NP_001401239             399 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 3 isoform 10
            precursor [Homo sapiens].
ACCESSION   NP_001401239 XP_005253745
VERSION     NP_001401239.1
DBSOURCE    REFSEQ: accession NM_001414310.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Tang,Q., Yuan,Y., Li,L., Xu,Y., Ji,W., Xiao,S., Han,Y., Miao,W.,
            Cai,J., You,P., Chen,M., Ding,S., Li,Z., Qi,Z., Hou,W. and Luo,H.
  TITLE     Comprehensive analysis reveals that LTBR is a immune-related
            biomarker for glioma
  JOURNAL   Comput Biol Med 174, 108457 (2024)
   PUBMED   38599071
  REMARK    GeneRIF: Comprehensive analysis reveals that LTBR is a
            immune-related biomarker for glioma.
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Wu,Y., Zhao,S., Guo,W., Liu,Y., Requena Mullor,M.D.M.,
            Rodriguez,R.A. and Wei,R.
  TITLE     Systematic analysis of the prognostic value and immunological
            function of LTBR in human cancer
  JOURNAL   Aging (Albany NY) 16 (1), 129-152 (2024)
   PUBMED   38175686
  REMARK    GeneRIF: Systematic analysis of the prognostic value and
            immunological function of LTBR in human cancer.
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Shuptrine,C.W., Perez,V.M., Selitsky,S.R., Schreiber,T.H. and
            Fromm,G.
  TITLE     Shining a LIGHT on myeloid cell targeted immunotherapy
  JOURNAL   Eur J Cancer 187, 147-160 (2023)
   PUBMED   37167762
  REMARK    Review article
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Abudukeyoumu,A., Lai,Z.Z., Lu,J.J., Zhang,X., Hou,D.Y., Dong,J.,
            Wu,J.N., Li,M.Q. and Xie,F.
  TITLE     A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion
  JOURNAL   J Reprod Immunol 153, 103693 (2022)
   PUBMED   35987137
  REMARK    GeneRIF: A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion.
REFERENCE   5  (residues 1 to 399)
  AUTHORS   Remouchamps,C., Boutaffala,L., Ganeff,C. and Dejardin,E.
  TITLE     Biology and signal transduction pathways of the
            Lymphotoxin-alphabeta/LTbetaR system
  JOURNAL   Cytokine Growth Factor Rev 22 (5-6), 301-310 (2011)
   PUBMED   22152226
  REMARK    Review article
REFERENCE   6  (residues 1 to 399)
  AUTHORS   Nakano,H., Oshima,H., Chung,W., Williams-Abbott,L., Ware,C.F.,
            Yagita,H. and Okumura,K.
  TITLE     TRAF5, an activator of NF-kappaB and putative signal transducer for
            the lymphotoxin-beta receptor
  JOURNAL   J Biol Chem 271 (25), 14661-14664 (1996)
   PUBMED   8663299
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Browning,J.L., Miatkowski,K., Sizing,I., Griffiths,D., Zafari,M.,
            Benjamin,C.D., Meier,W. and Mackay,F.
  TITLE     Signaling through the lymphotoxin beta receptor induces the death
            of some adenocarcinoma tumor lines
  JOURNAL   J Exp Med 183 (3), 867-878 (1996)
   PUBMED   8642291
REFERENCE   8  (residues 1 to 399)
  AUTHORS   Baens,M., Aerssens,J., van Zand,K., Van den Berghe,H. and
            Marynen,P.
  TITLE     Isolation and regional assignment of human chromosome 12p cDNAs
  JOURNAL   Genomics 29 (1), 44-52 (1995)
   PUBMED   8530100
REFERENCE   9  (residues 1 to 399)
  AUTHORS   Crowe,P.D., VanArsdale,T.L., Walter,B.N., Ware,C.F., Hession,C.,
            Ehrenfels,B., Browning,J.L., Din,W.S., Goodwin,R.G. and Smith,C.A.
  TITLE     A lymphotoxin-beta-specific receptor
  JOURNAL   Science 264 (5159), 707-710 (1994)
   PUBMED   8171323
REFERENCE   10 (residues 1 to 399)
  AUTHORS   Baens,M., Chaffanet,M., Cassiman,J.J., van den Berghe,H. and
            Marynen,P.
  TITLE     Construction and evaluation of a hncDNA library of human 12p
            transcribed sequences derived from a somatic cell hybrid
  JOURNAL   Genomics 16 (1), 214-218 (1993)
   PUBMED   8486360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005840.2.
            
            On Nov 17, 2022 this sequence version replaced XP_005253745.1.
            
            Summary: This gene encodes a member of the tumor necrosis factor
            receptor superfamily. The major ligands of this receptor include
            lymphotoxin alpha/beta and tumor necrosis factor ligand superfamily
            member 14. The encoded protein plays a role in signalling during
            the development of lymphoid and other organs, lipid metabolism,
            immune response, and programmed cell death. Activity of this
            receptor has also been linked to carcinogenesis. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2583208.1,
                                           SRR14038191.2662092.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..399
                     /product="tumor necrosis factor receptor superfamily
                     member 3 isoform 10 precursor"
                     /note="tumor necrosis factor C receptor; lymphotoxin B
                     receptor; tumor necrosis factor receptor type III;
                     lymphotoxin beta receptor (TNFR superfamily, member 3);
                     tumor necrosis factor receptor 2-related protein"
                     /calculated_mol_wt=39662
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3049
     Region          11..168
                     /region_name="TNFRSF3"
                     /note="Tumor necrosis factor receptor superfamily member 3
                     (TNFRSF3), also known as lymphotoxin beta receptor (LTBR);
                     cd10578"
                     /db_xref="CDD:276904"
     Region          22..80
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276904"
     Region          83..124
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276904"
     Region          126..167
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276904"
     Region          148..>210
                     /region_name="TNFRSF"
                     /note="Tumor necrosis factor receptor superfamily
                     (TNFRSF); cl22855"
                     /db_xref="CDD:473981"
     Region          170..210
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276900"
     CDS             1..399
                     /gene="LTBR"
                     /gene_synonym="D12S370; LT-BETA-R; TNF-R-III; TNFCR;
                     TNFR-RP; TNFR2-RP; TNFR3; TNFRSF3"
                     /coded_by="NM_001414310.1:198..1397"
                     /note="isoform 10 precursor is encoded by transcript
                     variant 10"
                     /db_xref="GeneID:4055"
                     /db_xref="HGNC:HGNC:6718"
                     /db_xref="MIM:600979"
ORIGIN      
        1 mllpwatsap glawgplvlg lfgllaasqp qavppyasen qtcrdqekey yepqhriccs
       61 rcppgtyvsa kcsrirdtvc atcaensyne hwnylticql crpcdpvmgl eeiapctskr
      121 ktqcrcqpgm fcaawalect hcellsdcpp gteaelkdev gkgnnhcvpc kaghfqntss
      181 psarcqphtr cenqglveaa pgtaqsdttc knpleplppe msgsllkrrp qgegpnpvag
      241 sweppkahpy fpdlvqpllp isgdvspvst glpaapvlea gvpqqqspld ltrepqlepg
      301 eqsqvahgtn gihvtggsmt itgniyiyng pvlggppgpg dlpatpeppy pipeegdpgp
      361 pglstphqed gkawhlaete hcgatpsnrg prnqfithd
//
LOCUS       NP_001425623             866 aa            linear   PRI 21-NOV-2025
DEFINITION  splicing regulator ARVCF isoform 8 [Homo sapiens].
ACCESSION   NP_001425623 XP_047297331 XP_054181614
VERSION     NP_001425623.1
DBSOURCE    REFSEQ: accession NM_001438694.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 866)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 866)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 866)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 866)
  AUTHORS   Suzuki,N., Idogawa,M., Tange,S., Ohashi,T., Sasaki,Y., Nakase,H.
            and Tokino,T.
  TITLE     p53-induced ARVCF modulates the splicing landscape and supports the
            tumor suppressive function of p53
  JOURNAL   Oncogene 39 (10), 2202-2211 (2020)
   PUBMED   31827232
  REMARK    GeneRIF: p53-induced ARVCF modulates the splicing landscape and
            supports the tumor suppressive function of p53.
REFERENCE   5  (residues 1 to 866)
  AUTHORS   Zhang,D., Tang,N., Liu,Y. and Wang,E.H.
  TITLE     ARVCF expression is significantly correlated with the malignant
            phenotype of non-small cell lung cancer
  JOURNAL   Mol Carcinog 54 Suppl 1, E185-E191 (2015)
   PUBMED   25683624
  REMARK    GeneRIF: observed ARVCF-dependent changes in small GTPase (mainly
            RhoA) activity in lung cancer cells. We confirmed that ARVCF plays
            an important role in the malignant phenotype
REFERENCE   6  (residues 1 to 866)
  AUTHORS   Mariner,D.J., Wang,J. and Reynolds,A.B.
  TITLE     ARVCF localizes to the nucleus and adherens junction and is
            mutually exclusive with p120(ctn) in E-cadherin complexes
  JOURNAL   J Cell Sci 113 (Pt 8), 1481-1490 (2000)
   PUBMED   10725230
REFERENCE   7  (residues 1 to 866)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   8  (residues 1 to 866)
  AUTHORS   Sirotkin,H., Morrow,B., Saint-Jore,B., Puech,A., Das Gupta,R.,
            Patanjali,S.R., Skoultchi,A., Weissman,S.M. and Kucherlapati,R.
  TITLE     Identification, characterization, and precise mapping of a human
            gene encoding a novel membrane-spanning protein from the 22q11
            region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 42 (2), 245-251 (1997)
   PUBMED   9192844
REFERENCE   9  (residues 1 to 866)
  AUTHORS   Sirotkin,H., O'Donnell,H., DasGupta,R., Halford,S., St Jore,B.,
            Puech,A., Parimoo,S., Morrow,B., Skoultchi,A., Weissman,S.M.,
            Scambler,P. and Kucherlapati,R.
  TITLE     Identification of a new human catenin gene family member (ARVCF)
            from the region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 41 (1), 75-83 (1997)
   PUBMED   9126485
REFERENCE   10 (residues 1 to 866)
  AUTHORS   Lindsay,E.A., Goldberg,R., Jurecic,V., Morrow,B., Carlson,C.,
            Kucherlapati,R.S., Shprintzen,R.J. and Baldini,A.
  TITLE     Velo-cardio-facial syndrome: frequency and extent of 22q11
            deletions
  JOURNAL   Am J Med Genet 57 (3), 514-522 (1995)
   PUBMED   7677167
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005663.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047297331.1, XP_054181614.1.
            
            Summary: Armadillo Repeat gene deleted in Velo-Cardio-Facial
            syndrome (ARVCF) is a member of the catenin family. This family
            plays an important role in the formation of adherens junction
            complexes, which are thought to facilitate communication between
            the inside and outside environments of a cell. The ARVCF gene was
            isolated in the search for the genetic defect responsible for the
            autosomal dominant Velo-Cardio-Facial syndrome (VCFS), a relatively
            common human disorder with phenotypic features including cleft
            palate, conotruncal heart defects and facial dysmorphology. The
            ARVCF gene encodes a protein containing two motifs, a coiled coil
            domain in the N-terminus and a 10 armadillo repeat sequence in the
            midregion. Since these sequences can facilitate protein-protein
            interactions ARVCF is thought to function in a protein complex. In
            addition, ARVCF contains a predicted nuclear-targeting sequence
            suggesting that it may have a function as a nuclear protein.
            [provided by RefSeq, Jun 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2287613.1,
                                           SRR11853561.19595.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..866
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..866
                     /product="splicing regulator ARVCF isoform 8"
                     /note="armadillo repeat protein deleted in
                     velo-cardio-facial syndrome; armadillo repeat gene deleted
                     in velocardiofacial syndrome; splicing regulator ARVCF"
                     /calculated_mol_wt=93696
     Region          297..322
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(313,317,321,355,359,363,398,403,407)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          326..365
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          330..366
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          369..410
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          373..408
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          415..466
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          587..623
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          587..623
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          633..668
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          633..667
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          674..719
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          725..757
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     CDS             1..866
                     /gene="ARVCF"
                     /coded_by="NM_001438694.1:104..2704"
                     /note="isoform 8 is encoded by transcript variant 9"
                     /db_xref="GeneID:421"
                     /db_xref="HGNC:HGNC:728"
                     /db_xref="MIM:602269"
ORIGIN      
        1 mpaelrqeqs pgsqaslatm peapdvleet vtveedpgtp tshvsivtse dgttrrtetk
       61 vtktvktvtt rtvrqvpvgp dglplldggp plgpfadgal drhfllrggg pvatlsrayl
      121 ssgggfpegp eprdspsygs lsrglgmrpp ragplgpgpg dgcftlpghr eafpvgpepg
      181 ppggrslper fqaepygled dtrslaadde ggpelepdyg tatrrrpecg rglhtrayed
      241 taddggelad erpafpmvta plaqpergsm gsldrlvrrs psvdsarkep rwrdpelpev
      301 lamlrhpvdp vkanaaaylq hlcfenegvk rrvrqlrglp llvalldhpr aevrrracga
      361 lrnlsygrdt dnkaairdcg gvpalvrllr aardnevrel vtgtlwnlss yeplkmviid
      421 hglqtlthev ivphsgwere pnedskprda ewttvfknts gclrnvssdg aearrrlrec
      481 eglvdallha lqsavgrkdt dnksvencvc imrnlsyhvh kevpgadryq eaepgplgsa
      541 vgsqrrrrdd ascfggkkak gkkdgemdrn fdtldlpkrt eaakgfelly qpevvrlyls
      601 lltesrnfnt leaaagalqn lsagnwmwat yiratvrker glpvlvellq setdkvvrav
      661 aialrnlsld rrnkdligsy amaelvrnvr naqapprpga cleedtvvav lntiheivsd
      721 sldnarsllq argvpalval vassqsvrea kaashvlqtv wsykelrgtl qkdgwtkarf
      781 qsaaatakgp kgalspggfd dstlplvdks legektgsrd vipmdalgpd gystvdrrer
      841 rprgassage asekeplkgp gpascs
//
LOCUS       NP_001427440             593 aa            linear   PRI 21-NOV-2025
DEFINITION  radixin isoform 6 [Homo sapiens].
ACCESSION   NP_001427440
VERSION     NP_001427440.1
DBSOURCE    REFSEQ: accession NM_001440511.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 593)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 593)
  AUTHORS   Kruse,T., Benz,C., Garvanska,D.H., Lindqvist,R., Mihalic,F.,
            Coscia,F., Inturi,R., Sayadi,A., Simonetti,L., Nilsson,E., Ali,M.,
            Kliche,J., Moliner Morro,A., Mund,A., Andersson,E., McInerney,G.,
            Mann,M., Jemth,P., Davey,N.E., Overby,A.K., Nilsson,J. and
            Ivarsson,Y.
  TITLE     Large scale discovery of coronavirus-host factor protein
            interaction motifs reveals SARS-CoV-2 specific mechanisms and
            vulnerabilities
  JOURNAL   Nat Commun 12 (1), 6761 (2021)
   PUBMED   34799561
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 593)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 593)
  AUTHORS   Stemmer-Rachamimov,A.O., Gonzalez-Agosti,C., Xu,L., Burwick,J.A.,
            Beauchamp,R., Pinney,D., Louis,D.N. and Ramesh,V.
  TITLE     Expression of NF2-encoded merlin and related ERM family proteins in
            the human central nervous system
  JOURNAL   J Neuropathol Exp Neurol 56 (6), 735-742 (1997)
   PUBMED   9184664
REFERENCE   7  (residues 1 to 593)
  AUTHORS   Hirao,M., Sato,N., Kondo,T., Yonemura,S., Monden,M., Sasaki,T.,
            Takai,Y., Tsukita,S. and Tsukita,S.
  TITLE     Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma
            membrane association: possible involvement of phosphatidylinositol
            turnover and Rho-dependent signaling pathway
  JOURNAL   J Cell Biol 135 (1), 37-51 (1996)
   PUBMED   8858161
REFERENCE   8  (residues 1 to 593)
  AUTHORS   Wilgenbus,K.K., Milatovich,A., Francke,U. and Furthmayr,H.
  TITLE     Molecular cloning, cDNA sequence, and chromosomal assignment of the
            human radixin gene and two dispersed pseudogenes
  JOURNAL   Genomics 16 (1), 199-206 (1993)
   PUBMED   8486357
REFERENCE   9  (residues 1 to 593)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 593)
  AUTHORS   Sato,N., Funayama,N., Nagafuchi,A., Yonemura,S., Tsukita,S. and
            Tsukita,S.
  TITLE     A gene family consisting of ezrin, radixin and moesin. Its specific
            localization at actin filament/plasma membrane association sites
  JOURNAL   J Cell Sci 103 (Pt 1), 131-143 (1992)
   PUBMED   1429901
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002788.3 and AP000901.5.
            
            Summary: Radixin is a cytoskeletal protein that may be important in
            linking actin to the plasma membrane. It is highly similar in
            sequence to both ezrin and moesin. The radixin gene has been
            localized by fluorescence in situ hybridization to 11q23. A
            truncated version representing a pseudogene (RDXP2) was assigned to
            Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was
            mapped to 11p by Southern and PCR analyses. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803614.81532.1, SRR1803612.256542.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMN03267755 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..593
                     /product="radixin isoform 6"
                     /calculated_mol_wt=69680
     Region          5..195
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          189..285
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(231..232,234..240,249,270,273..274,277)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(231,234..241,249,270,273..274,277)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(267,271)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            270..285
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          336..445
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          496..572
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..593
                     /gene="RDX"
                     /gene_synonym="DFNB24"
                     /coded_by="NM_001440511.1:170..1951"
                     /note="isoform 6 is encoded by transcript variant 13"
                     /db_xref="GeneID:5962"
                     /db_xref="HGNC:HGNC:9944"
                     /db_xref="MIM:179410"
ORIGIN      
        1 mdaelefaiq pnttgkqlfd qvvktvglre vwffglqyvd skgystwlkl nkkvtqqdvk
       61 kenplqfkfr akffpedvse eliqeitqrl fflqvkeail ndeiycppet avllasyavq
      121 akygdynkei hkpgylandr llpqrvleqh kltkeqweer iqnwheehrg mlredsmmey
      181 lkiaqdlemy gvnyfeiknk kgtelwlgvd alglniyehd dkltpkigfp wseirnisfn
      241 dkkfvikpid kkapdfvfya prlrinkril alcmgnhely mrrrkpdtie vqqmkaqare
      301 ekhqkqlera qlenekkkre iaekekerie rekeelmerl kqieeqtika qkeleeqtrk
      361 aleldqerkr akeeaerlek erraaeeaks aiakqaadqm knqeqlaael aeftakiall
      421 eeakkkkeee atewqhkafa aqedlektke elktvmsapp ppppppvipp tenehdehde
      481 nnaeasaels negvmnhrse eervtetqkn ervkkqlqal sselaqarde tkktqndvlh
      541 aenvkagrdk yktlrqirqg ntkqridefe amwgpklyal fqmrscqssi kqm
//
LOCUS       NP_001397932            1884 aa            linear   PRI 21-NOV-2025
DEFINITION  Golgi-specific brefeldin A-resistance guanine nucleotide exchange
            factor 1 isoform 16 [Homo sapiens].
ACCESSION   NP_001397932 XP_047281924
VERSION     NP_001397932.1
DBSOURCE    REFSEQ: accession NM_001411003.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1884)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1884)
  AUTHORS   Hirano,J., Hayashi,T., Kitamura,K., Nishimura,Y., Shimizu,H.,
            Okamoto,T., Okada,K., Uemura,K., Yeh,M.T., Ono,C., Taguwa,S.,
            Muramatsu,M. and Matsuura,Y.
  TITLE     Enterovirus 3A protein disrupts endoplasmic reticulum homeostasis
            through interaction with GBF1
  JOURNAL   J Virol 98 (7), e0081324 (2024)
   PUBMED   38904364
  REMARK    GeneRIF: Enterovirus 3A protein disrupts endoplasmic reticulum
            homeostasis through interaction with GBF1.
REFERENCE   3  (residues 1 to 1884)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1884)
  AUTHORS   Navare,A.T., Mast,F.D., Olivier,J.P., Bertomeu,T., Neal,M.L.,
            Carpp,L.N., Kaushansky,A., Coulombe-Huntington,J., Tyers,M. and
            Aitchison,J.D.
  TITLE     Viral protein engagement of GBF1 induces host cell vulnerability
            through synthetic lethality
  JOURNAL   J Cell Biol 221 (11) (2022)
   PUBMED   36305789
  REMARK    GeneRIF: Viral protein engagement of GBF1 induces host cell
            vulnerability through synthetic lethality.
REFERENCE   5  (residues 1 to 1884)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1884)
  AUTHORS   Garcia-Mata,R. and Sztul,E.
  TITLE     The membrane-tethering protein p115 interacts with GBF1, an ARF
            guanine-nucleotide-exchange factor
  JOURNAL   EMBO Rep 4 (3), 320-325 (2003)
   PUBMED   12634853
  REMARK    GeneRIF: novel interaction between p115 and Golgi-specific
            brefeldin-A-resistant factor 1 (GBF1)
REFERENCE   7  (residues 1 to 1884)
  AUTHORS   Kawamoto,K., Yoshida,Y., Tamaki,H., Torii,S., Shinotsuka,C.,
            Yamashina,S. and Nakayama,K.
  TITLE     GBF1, a guanine nucleotide exchange factor for ADP-ribosylation
            factors, is localized to the cis-Golgi and involved in membrane
            association of the COPI coat
  JOURNAL   Traffic 3 (7), 483-495 (2002)
   PUBMED   12047556
  REMARK    GeneRIF: detailed subcellular localization to the cis-Golgi
REFERENCE   8  (residues 1 to 1884)
  AUTHORS   Verhoeven,K., Villanova,M., Rossi,A., Malandrini,A., De Jonghe,P.
            and Timmerman,V.
  TITLE     Localization of the gene for the intermediate form of
            Charcot-Marie-Tooth to chromosome 10q24.1-q25.1
  JOURNAL   Am J Hum Genet 69 (4), 889-894 (2001)
   PUBMED   11533914
REFERENCE   9  (residues 1 to 1884)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   10 (residues 1 to 1884)
  AUTHORS   Mansour,S.J., Herbrick,J.A., Scherer,S.W. and Melancon,P.
  TITLE     Human GBF1 is a ubiquitously expressed gene of the sec7 domain
            family mapping to 10q24
  JOURNAL   Genomics 54 (2), 323-327 (1998)
   PUBMED   9828135
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160011.35, AL356420.14 and
            AL121928.13.
            
            On Aug 20, 2022 this sequence version replaced XP_047281924.1.
            
            Summary: This gene encodes a member of the Sec7 domain family. The
            encoded protein is a guanine nucleotide exchange factor that
            regulates the recruitment of proteins to membranes by mediating GDP
            to GTP exchange. The encoded protein is localized to the Golgi
            apparatus and plays a role in vesicular trafficking by activating
            ADP ribosylation factor 1. The encoded protein has also been
            identified as an important host factor for viral replication.
            Multiple transcript variants have been observed for this gene.
            [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2295352.1,
                                           SRR14372080.4079655.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2146982
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1884
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..1884
                     /product="Golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1 isoform 16"
                     /note="golgi-specific brefeldin A-resistance guanine
                     nucleotide exchange factor 1; BFA-resistant GEF 1"
                     /calculated_mol_wt=209083
     Region          1..211
                     /region_name="DCB, DCB:DCB domain and DCB:HUS domain
                     interaction. /evidence=ECO:0000250|UniProtKB:Q9R1D7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          240..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          <454..>1203
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          555..575
                     /region_name="HUS, DCB:HUS domain interaction.
                     /evidence=ECO:0000250|UniProtKB:Q9R1D7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          644..690
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          724..909
                     /region_name="Sec7"
                     /note="Sec7 domain; pfam01369"
                     /db_xref="CDD:460178"
     Region          911..1395
                     /region_name="Phosphatidylinositol-phosphate binding,
                     required for translocation to the leading edge and for
                     ARF1 activation upon GPCR signaling.
                     /evidence=ECO:0000269|PubMed:22573891"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1309..1360
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1341
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1362
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AMPK.
                     /evidence=ECO:0000269|PubMed:18063581; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1375..1395
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1455..1508
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1500
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          1750..1833
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1798
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Site            1809
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92538.3)"
     Region          <1819..1882
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1884
                     /gene="GBF1"
                     /gene_synonym="ARF1GEF; CMT2GG; CMTDI2; CMTDIA"
                     /coded_by="NM_001411003.1:261..5915"
                     /note="isoform 16 is encoded by transcript variant 24"
                     /db_xref="CCDS:CCDS91328.1"
                     /db_xref="GeneID:8729"
                     /db_xref="HGNC:HGNC:4181"
                     /db_xref="MIM:603698"
ORIGIN      
        1 mvdkniyiiq geinivvgai krnarwstht pldeerdpll hsfghlkevl nsitelseie
       61 pnvflrpfle virsedttgp itglaltsvn kflsyalidp thegtaegme nmadavthar
      121 fvgtdpasde vvlmkilqvl rtllltpvga hltnesvcei mqscfricfe mrlsellrks
      181 aehtlvdmvq llftrlpqfk eepknyvgtn mkkispclln klelssgeqt kalnqlerlk
      241 mraggmsdss kwkkqkrspr pprhmtkvtp gselptpngt tlssnltggm pfidvptpis
      301 sasseaasav vspstdsgle fssqttsked ltdleqpgsp gystatepgs selgvpeqpd
      361 lqegthveks qsasvesipe vleectspad hsdsasvhdm dyvnprgvrf tqssqkegta
      421 lvpyglpcir elfrflislt nphdrhnsev mihmglhllt valesapvaq cqtllglikd
      481 emcrhlfqll sierlnlyaa slrvcfllfe smrehlkfqm emyikklmei itvenpkmpy
      541 emkemaleai vqlwripsfv telyinydcd yycsnlfeel tkllsknafp vsgqlytthl
      601 lsldalltvi dsteahcqak vlnsltqqek ketarpscei vdgtreasnt ertasdgkav
      661 gmasdipglh lpgggrlppe hgksgcsdle eavdsgadkk farkpprfsc llpdprelie
      721 iknkkkllit gteqfnqkpk kgiqflqekg lltipmdnte vaqwlrenpr ldkkmigefv
      781 sdrknidlle sfvstfsfqg lrldealrly leafrlpgea pviqrlleaf terwmncngs
      841 pfansdacfs layavimlnt dqhnhnvrkq napmtleefr knlkgvnggk dfeqdiledm
      901 yhaikneeiv mpeeqtglvr enyvwnvllh rgatpegifl rvptasydld lftmtwgpti
      961 aalsyvfdks leetiiqkai sgfrkcamis ahyglsdvfd nliislckft alssesienl
     1021 psvfgsnpka hiaaktvfhl ahrhgdilre gwknimeaml qlfraqllpk amievedfvd
     1081 pngkislqre etpsnrgest vlsfvswltl sgpeqssvrg pstenqeakr valecikqcd
     1141 pekmiteskf lqleslqelm kalvsvtpde etydeedaaf clemllrivl enrdrvgcvw
     1201 qtvrdhlyhl cvqaqdfcfl veravvgllr lairllrree isaqvllslr illlmkpsvl
     1261 srvshqvayg lhellktnaa nihsgddwat lftllecigs gvkppaalqa taradapdag
     1321 aqsdselpsy hqndvsldrg ytsdsevytd hgrpgkihrs atdadvvnsg wlvvgkddvd
     1381 nskpgpsrpg psplinqysl tvgldlgphd tksllkcves lsfivrdaah itpdnfelcv
     1441 ktlrifveas lnggcksqek rgkshkydsk gnrfkkkske gsmlrrprts sqhasrggqs
     1501 dddedegvpa syhtvslqvs qdlldlmhtl htraasiyss waeeqrhlet ggqkieadsr
     1561 tlwahcwcpl lqgiaclccd arrqvrmqal tylqrallvh dlqkldalew escfnkvlfp
     1621 lltkllenis padvggmeet rmrastllsk vflqhlspll slstfaalwl tildfmdkym
     1681 hagssdllse aipeslknml lvmdtaeifh sadargggps alweitweri dcflphlrde
     1741 lfkqtviqdp mpmepqgqkp lasahltsaa gdtrtpghpp ppeipselga cdfekpespr
     1801 aasssspgsp vasspsrlsp tpdgppplaq pplilqplas plqvgvppmt lpiilnpali
     1861 eatspvplla tprptdpipt sevn
//
LOCUS       NP_001394735            1234 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 2 precursor
            [Homo sapiens].
ACCESSION   NP_001394735
VERSION     NP_001394735.1
DBSOURCE    REFSEQ: accession NM_001407806.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1234)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1234)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1234)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1234)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1234)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1234)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1234)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1234)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1234)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1234)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.3638487.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1234
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1234
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 2 precursor"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=134981
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O00411.2)"
                     /calculated_mol_wt=4109
     Region          18..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          95..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          261..290
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          296..323
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          432..701
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          728..747
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          828..1234
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1234
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407806.1:26..3730"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 msalcwgrga aglkralrpc grpglpgkeg taggvcgprr sssaspqeqd qdrrkdwghv
       61 ellevlqarv rqlqaesvse vvvnrvdvar lpecgsgdgs lqpprkvqmg akdatpvpcg
      121 rwakilekdk rtqqmrmqrl kaklqmpfqs gefkaltrrl qveprllskq magcledctr
      181 qapespweeq larllqeapg klsldveqap sgqhsqaqls gqqqrllaff kcclltdqlp
      241 lahhllvvhh gqrqkrkllt ldmynavmlg warqgafkel vyvlfmvkda gltpdllsya
      301 aalqcmgrqd qdagtiercl eqmsqeglkl qalftavlls eedratvlka vhkvkptfsl
      361 ppqlpppvnt skllrdvyak dgrvsypklh lplktlqclf ekqlhmelas rvcvvsvekp
      421 tlpskevkha rktlktlrdq wekalcralr etknrlerev yegrfslypf lcllderevv
      481 rmllqalpaq gesfttlare lsartfsrhv vqrqrvsgqv qalqnhyrky lcllasdaev
      541 pepclprqyw eelgapealr eqpwplpvqm elgkllaeml vqatqmpcsl dkphrssrlv
      601 pvlyhvysfr nvqqigilkp hpayvqllek aaeptltfea vdvpmlcppl pwtsphsgaf
      661 llsptklmrt vegatqhqel letcpptalh galdaltqlg ncawrvngrv ldlvlqlfqa
      721 kgcpqlgvpa ppseapqppe ahlphsaapa rkaelrrela hcqkvaremh slraealyrl
      781 slaqhlrdrv fwlphnmdfr grtypcpphf nhlgsdvara llefaqgrpl gphgldwlki
      841 hlvnltglkk replrkrlaf aeevmddild sadqpltgrk wwmgaeepwq tlaccmevan
      901 avrasdpaay vshlpvhqdg scnglqhyaa lgrdsvgaas vnlepsdvpq dvysgvaaqv
      961 evfrrqdaqr gmrvaqvleg fitrkvvkqt vmtvvygvtr yggrlqiekr lrelsdfpqe
     1021 fvweashylv rqvfkslqem fsgtraiqhw ltesarlish mgsvvewvtp lgvpviqpyr
     1081 ldskvkqigg giqsitythn gdisrkpntr kqkngfppnf ihsldsshmm ltalhcyrsp
     1141 plchrkgltf vsvhdcywth aadvsvmnqv creqfvrlhs epilqdlsrf lvkrfcsepq
     1201 kileasqlke tlqavpkpga fdleqvkrst yffs
//
LOCUS       NP_001394198             302 aa            linear   PRI 21-NOV-2025
DEFINITION  cellular tumor antigen p53 isoform i [Homo sapiens].
ACCESSION   NP_001394198
VERSION     NP_001394198.1
DBSOURCE    REFSEQ: accession NM_001407269.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Mirgayazova,R., Khadiullina,R., Chasov,V., Mingaleeva,R.,
            Miftakhova,R., Rizvanov,A. and Bulatov,E.
  TITLE     Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an Option?
  JOURNAL   Genes (Basel) 11 (6), 704 (2020)
   PUBMED   32630614
  REMARK    GeneRIF: Therapeutic Editing of the TP53 Gene: Is CRISPR/Cas9 an
            Option?
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Flynt,E., Bisht,K., Sridharan,V., Ortiz,M., Towfic,F. and
            Thakurta,A.
  TITLE     Prognosis, Biology, and Targeting of TP53 Dysregulation in Multiple
            Myeloma
  JOURNAL   Cells 9 (2), 287 (2020)
   PUBMED   31991614
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Barnoud,T., Parris,J.L.D. and Murphy,M.E.
  TITLE     Common genetic variants in the TP53 pathway and their impact on
            cancer
  JOURNAL   J Mol Cell Biol 11 (7), 578-585 (2019)
   PUBMED   31152665
  REMARK    GeneRIF: Common genetic variants in the TP53 pathway and their
            impact on cancer.
            Review article
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Hu,W., Chen,S., Thorne,R.F. and Wu,M.
  TITLE     TP53, TP53 Target Genes (DRAM, TIGAR), and Autophagy
  JOURNAL   Adv Exp Med Biol 1206, 127-149 (2019)
   PUBMED   31776983
  REMARK    Review article
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Baugh,E.H., Ke,H., Levine,A.J., Bonneau,R.A. and Chan,C.S.
  TITLE     Why are there hotspot mutations in the TP53 gene in human cancers?
  JOURNAL   Cell Death Differ 25 (1), 154-160 (2018)
   PUBMED   29099487
  REMARK    GeneRIF: TP53 missense mutant alleles that occur in human cancers
            are discussed in the context of high resolution models of these p53
            mutant protein structures to determine the structural features of
            mutations (review).
            Review article
REFERENCE   6  (residues 1 to 302)
  AUTHORS   Aubrey,B.J., Strasser,A. and Kelly,G.L.
  TITLE     Tumor-Suppressor Functions of the TP53 Pathway
  JOURNAL   Cold Spring Harb Perspect Med 6 (5), a026062 (2016)
   PUBMED   27141080
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 302)
  AUTHORS   Soussi,T. and Wiman,K.G.
  TITLE     TP53: an oncogene in disguise
  JOURNAL   Cell Death Differ 22 (8), 1239-1249 (2015)
   PUBMED   26024390
  REMARK    Review article
REFERENCE   8  (residues 1 to 302)
  AUTHORS   Soussi,T.
  TITLE     The TP53 gene network in a postgenomic era
  JOURNAL   Hum Mutat 35 (6), 641-642 (2014)
   PUBMED   24753184
  REMARK    GeneRIF: Recommendations and guidelines for reporting and
            annotating TP53 variants are also provided, to help researchers
            generate standardized data that are easy to understand, analyze,
            and exchange across various cancer variant databases
            Review article
REFERENCE   9  (residues 1 to 302)
  AUTHORS   Anczukow,O., Ware,M.D., Buisson,M., Zetoune,A.B.,
            Stoppa-Lyonnet,D., Sinilnikova,O.M. and Mazoyer,S.
  TITLE     Does the nonsense-mediated mRNA decay mechanism prevent the
            synthesis of truncated BRCA1, CHK2, and p53 proteins?
  JOURNAL   Hum Mutat 29 (1), 65-73 (2008)
   PUBMED   17694537
  REMARK    GeneRIF: the p53 protein encoded by the 770delT allele is as
            abundant as the wild-type protein, as removal of the C-terminal p53
            domain leads to a stabilized mutant protein, whose abundance is
            markedly increased when NMD is inhibited.
REFERENCE   10 (residues 1 to 302)
  AUTHORS   Bourdon,J.C.
  TITLE     p53 Family isoforms
  JOURNAL   Curr Pharm Biotechnol 8 (6), 332-336 (2007)
   PUBMED   18289041
  REMARK    Review article
REFERENCE   11 (residues 1 to 302)
  AUTHORS   Candeias,M.M., Powell,D.J., Roubalova,E., Apcher,S., Bourougaa,K.,
            Vojtesek,B., Bruzzoni-Giovanelli,H. and Fahraeus,R.
  TITLE     Expression of p53 and p53/47 are controlled by alternative
            mechanisms of messenger RNA translation initiation
  JOURNAL   Oncogene 25 (52), 6936-6947 (2006)
   PUBMED   16983332
  REMARK    GeneRIF: harbouring alternative translation initiation sites, the
            p53 mRNA gives rise to different levels of the p53 isoforms which
            help to orchestrate the cell biological outcome of p53 activation
REFERENCE   12 (residues 1 to 302)
  AUTHORS   Murray-Zmijewski,F., Lane,D.P. and Bourdon,J.C.
  TITLE     p53/p63/p73 isoforms: an orchestra of isoforms to harmonise cell
            differentiation and response to stress
  JOURNAL   Cell Death Differ 13 (6), 962-972 (2006)
   PUBMED   16601753
  REMARK    Review article
REFERENCE   13 (residues 1 to 302)
  AUTHORS   Bourdon,J.C., Fernandes,K., Murray-Zmijewski,F., Liu,G., Diot,A.,
            Xirodimas,D.P., Saville,M.K. and Lane,D.P.
  TITLE     p53 isoforms can regulate p53 transcriptional activity
  JOURNAL   Genes Dev 19 (18), 2122-2137 (2005)
   PUBMED   16131611
  REMARK    GeneRIF: p53 isoforms can regulate p53 transcriptional activity.
REFERENCE   14 (residues 1 to 302)
  AUTHORS   Ghosh,A., Stewart,D. and Matlashewski,G.
  TITLE     Regulation of human p53 activity and cell localization by
            alternative splicing
  JOURNAL   Mol Cell Biol 24 (18), 7987-7997 (2004)
   PUBMED   15340061
  REMARK    GeneRIF: mechanism of p53 regulation originating through
            alternative splicing of the human p53 gene resulting in the
            expression of a novel p53 mRNA
REFERENCE   15 (residues 1 to 302)
  AUTHORS   Flaman,J.M., Waridel,F., Estreicher,A., Vannier,A., Limacher,J.M.,
            Gilbert,D., Iggo,R. and Frebourg,T.
  TITLE     The human tumour suppressor gene p53 is alternatively spliced in
            normal cells
  JOURNAL   Oncogene 12 (4), 813-818 (1996)
   PUBMED   8632903
REFERENCE   16 (residues 1 to 302)
  AUTHORS   Schneider,K., Zelley,K., Nichols,K.E., Schwartz Levine,A. and
            Garber,J.
  TITLE     Li-Fraumeni Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301488
REFERENCE   17 (residues 1 to 302)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   18 (residues 1 to 302)
  AUTHORS   Lamb,P. and Crawford,L.
  TITLE     Characterization of the human p53 gene
  JOURNAL   Mol Cell Biol 6 (5), 1379-1385 (1986)
   PUBMED   2946935
REFERENCE   19 (residues 1 to 302)
  AUTHORS   Isobe,M., Emanuel,B.S., Givol,D., Oren,M. and Croce,C.M.
  TITLE     Localization of gene for human p53 tumour antigen to band 17p13
  JOURNAL   Nature 320 (6057), 84-85 (1986)
   PUBMED   3456488
REFERENCE   20 (residues 1 to 302)
  AUTHORS   Benchimol,S., Lamb,P., Crawford,L.V., Sheer,D., Shows,T.B.,
            Bruns,G.A. and Peacock,J.
  TITLE     Transformation associated p53 protein is encoded by a gene on human
            chromosome 17
  JOURNAL   Somat Cell Mol Genet 11 (5), 505-510 (1985)
   PUBMED   2994241
REFERENCE   21 (residues 1 to 302)
  AUTHORS   Harlow,E., Williamson,N.M., Ralston,R., Helfman,D.M. and Adams,T.E.
  TITLE     Molecular cloning and in vitro expression of a cDNA clone for human
            cellular tumor antigen p53
  JOURNAL   Mol Cell Biol 5 (7), 1601-1610 (1985)
   PUBMED   3894933
REFERENCE   22 (residues 1 to 302)
  AUTHORS   Zakut-Houri,R., Bienz-Tadmor,B., Givol,D. and Oren,M.
  TITLE     Human p53 cellular tumor antigen: cDNA sequence and expression in
            COS cells
  JOURNAL   EMBO J 4 (5), 1251-1255 (1985)
   PUBMED   4006916
REFERENCE   23 (residues 1 to 302)
  AUTHORS   Matlashewski,G., Lamb,P., Pim,D., Peacock,J., Crawford,L. and
            Benchimol,S.
  TITLE     Isolation and characterization of a human p53 cDNA clone:
            expression of the human p53 gene
  JOURNAL   EMBO J 3 (13), 3257-3262 (1984)
   PUBMED   6396087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087388.9 and AC007421.13.
            
            Summary: This gene encodes a tumor suppressor protein containing
            transcriptional activation, DNA binding, and oligomerization
            domains. The encoded protein responds to diverse cellular stresses
            to regulate expression of target genes, thereby inducing cell cycle
            arrest, apoptosis, senescence, DNA repair, or changes in
            metabolism. Mutations in this gene are associated with a variety of
            human cancers, including hereditary cancers such as Li-Fraumeni
            syndrome. Alternative splicing of this gene and the use of
            alternate promoters result in multiple transcript variants and
            isoforms. Additional isoforms have also been shown to result from
            the use of alternate translation initiation codons from identical
            transcript variants (PMIDs: 12032546, 20937277). [provided by
            RefSeq, Dec 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2378303.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:2946935)
            NMD candidate                    :: PMID: 16131611, 16601753,
                                                18289041
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..302
                     /product="cellular tumor antigen p53 isoform i"
                     /note="tumor protein 53; mutant tumor protein 53; cellular
                     tumor antigen p53; phosphoprotein p53;
                     transformation-related protein 53; antigen NY-CO-13; tumor
                     supressor p53"
                     /calculated_mol_wt=33362
     Region          1..20
                     /region_name="TAD2"
                     /note="Transactivation domain 2; pfam18521"
                     /db_xref="CDD:375947"
     Region          70..249
                     /region_name="P53"
                     /note="P53 DNA-binding domain; cd08367"
                     /db_xref="CDD:176262"
     Site            order(137,140,199,203)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:176262"
     Site            order(138..140,142)
                     /site_type="other"
                     /note="dimerization site [polypeptide binding]"
                     /db_xref="CDD:176262"
     Site            order(200,202,209,234,236..238,241)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:176262"
     CDS             1..302
                     /gene="TP53"
                     /gene_synonym="BCC7; BMFS5; LFS1; P53; TRP53"
                     /coded_by="NM_001407269.1:257..1165"
                     /note="isoform i is encoded by transcript variant 12"
                     /db_xref="GeneID:7157"
                     /db_xref="HGNC:HGNC:11998"
                     /db_xref="MIM:191170"
ORIGIN      
        1 mddlmlspdd ieqwftedpg pdeaprmpea appvapapaa ptpaapapap swplsssvps
       61 qktyqgsygf rlgflhsgta ksvtctyspa lnkmfcqlak tcpvqlwvds tpppgtrvra
      121 maiykqsqhm tevvrrcphh ercsdsdgla ppqhlirveg nlrveylddr ntfrhsvvvp
      181 yeppevgsdc ttihynymcn sscmggmnrr piltiitled ssgnllgrns fevrvcacpg
      241 rdrrteeenl rkkgephhel ppgstkralp nntssspqpk kkpldgeyft lqdqtsfqke
      301 nc
//
LOCUS       NP_001412009             363 aa            linear   PRI 21-NOV-2025
DEFINITION  coatomer subunit delta isoform 10 [Homo sapiens].
ACCESSION   NP_001412009
VERSION     NP_001412009.1
DBSOURCE    REFSEQ: accession NM_001425080.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   O'Donoghue,L., Comer,S.P., Hiebner,D.W., Schoen,I., von
            Kriegsheim,A. and Smolenski,A.
  TITLE     RhoGAP6 interacts with COPI to regulate protein transport
  JOURNAL   Biochem J 480 (14), 1109-1127 (2023)
   PUBMED   37409526
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Li,W., Liang,J., Outeda,P., Turner,S., Wakimoto,B.T. and Watnick,T.
  TITLE     A genetic screen in Drosophila reveals an unexpected role for the
            KIP1 ubiquitination-promoting complex in male fertility
  JOURNAL   PLoS Genet 16 (12), e1009217 (2020)
   PUBMED   33378371
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Tidwell,T., Deshotel,M., Palumbos,J., Miller,C., Bayrak-Toydemir,P.
            and Carey,J.C.
  TITLE     Novel de novo ARCN1 intronic variant causes rhizomelic short
            stature with microretrognathia and developmental delay
  JOURNAL   Cold Spring Harb Mol Case Stud 6 (6), a005728 (2020)
   PUBMED   33154040
  REMARK    GeneRIF: Novel de novo ARCN1 intronic variant causes rhizomelic
            short stature with microretrognathia and developmental delay.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 363)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 363)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 363)
  AUTHORS   Schekman,R. and Orci,L.
  TITLE     Coat proteins and vesicle budding
  JOURNAL   Science 271 (5255), 1526-1533 (1996)
   PUBMED   8599108
  REMARK    Review article
REFERENCE   7  (residues 1 to 363)
  AUTHORS   Cukierman,E., Huber,I., Rotman,M. and Cassel,D.
  TITLE     The ARF1 GTPase-activating protein: zinc finger motif and Golgi
            complex localization
  JOURNAL   Science 270 (5244), 1999-2002 (1995)
   PUBMED   8533093
REFERENCE   8  (residues 1 to 363)
  AUTHORS   Radice,P., Pensotti,V., Jones,C., Perry,H., Pierotti,M.A. and
            Tunnacliffe,A.
  TITLE     The human archain gene, ARCN1, has highly conserved homologs in
            rice and Drosophila
  JOURNAL   Genomics 26 (1), 101-106 (1995)
   PUBMED   7782067
REFERENCE   9  (residues 1 to 363)
  AUTHORS   Orcl,L., Palmer,D.J., Amherdt,M. and Rothman,J.E.
  TITLE     Coated vesicle assembly in the Golgi requires only coatomer and ARF
            proteins from the cytosol
  JOURNAL   Nature 364 (6439), 732-734 (1993)
   PUBMED   8355790
REFERENCE   10 (residues 1 to 363)
  AUTHORS   Waters,M.G., Serafini,T. and Rothman,J.E.
  TITLE     'Coatomer': a cytosolic protein complex containing subunits of
            non-clathrin-coated Golgi transport vesicles
  JOURNAL   Nature 349 (6306), 248-251 (1991)
   PUBMED   1898986
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000941.6.
            
            Summary: This gene maps in a region, which include the mixed
            lineage leukemia and Friend leukemia virus integration 1 genes,
            where multiple disease-associated chromosome translocations occur.
            It is an intracellular protein. Archain sequences are well
            conserved among eukaryotes and this protein may play a fundamental
            role in eukaryotic cell biology. It has similarities to heat shock
            proteins and clathrin-associated proteins, and may be involved in
            vesicle structure or trafficking. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.6243.1,
                                           SRR11853560.6171.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..363
                     /product="coatomer subunit delta isoform 10"
                     /note="coatomer protein delta-COP; coatomer protein
                     complex, subunit delta; archain vesicle transport protein
                     1; coatomer delta subunit; delta-coat protein; COPI coat
                     complex subunit delta"
                     /calculated_mol_wt=39954
     Region          124..360
                     /region_name="AP_delta-COPI_MHD"
                     /note="Mu homology domain (MHD) of adaptor protein (AP)
                     coat protein I (COPI) delta subunit; cd09254"
                     /db_xref="CDD:271162"
     CDS             1..363
                     /gene="ARCN1"
                     /gene_synonym="COPD; SRMMD; SSMG"
                     /coded_by="NM_001425080.1:140..1231"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:372"
                     /db_xref="HGNC:HGNC:649"
                     /db_xref="MIM:600820"
ORIGIN      
        1 mtqereakae mrrkakelqq arrdaerqgk kapgfggfgs savsggstaa mitetiietd
       61 kpkvapapar psgpskalkl gakgkevdnf vdklkseget imsssmgkrt seatkmhapp
      121 inmesvhmki eekitltcgr dgglqnmelh gmimlrisdd kygrirlhve nedkkgvqlq
      181 thpnvdkklf taesliglkn peksfpvnsd vgvlkwrlqt teesfiplti ncwpsesgng
      241 cdvnieyelq ednlelndvv itiplpsgvg apvigeidge yrhdsrrntl ewclpvidak
      301 nksgslefsi agqpndffpv qvsfvskkny cniqvtkvtq vdgnspvrfs tettflvdky
      361 eil
//
LOCUS       NP_001425990            2502 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HECTD1 isoform 9 [Homo sapiens].
ACCESSION   NP_001425990 XP_047287161 XP_054231755
VERSION     NP_001425990.1
DBSOURCE    REFSEQ: accession NM_001439061.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2502)
  AUTHORS   Oxman,E., Li,H., Wang,H.Y. and Zohn,I.E.
  TITLE     Identification and functional analysis of rare HECTD1 missense
            variants in human neural tube defects
  JOURNAL   Hum Genet 143 (3), 263-277 (2024)
   PUBMED   38451291
  REMARK    GeneRIF: Identification and functional analysis of rare HECTD1
            missense variants in human neural tube defects.
REFERENCE   2  (residues 1 to 2502)
  AUTHORS   Zhang,J., Xin,Y., Ling,X., Liang,H., Zhang,L., Fang,C. and Ma,J.
  TITLE     Nucleoporin 93, a new substrate of the E3 ubiquitin protein ligase
            HECTD1, promotes esophageal squamous cell carcinoma progression
  JOURNAL   Hum Cell 37 (1), 245-257 (2024)
   PUBMED   37993750
  REMARK    GeneRIF: Nucleoporin 93, a new substrate of the E3 ubiquitin
            protein ligase HECTD1, promotes esophageal squamous cell carcinoma
            progression.
REFERENCE   3  (residues 1 to 2502)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 2502)
  AUTHORS   Vaughan,N., Scholz,N., Lindon,C. and Licchesi,J.D.F.
  TITLE     The E3 ubiquitin ligase HECTD1 contributes to cell proliferation
            through an effect on mitosis
  JOURNAL   Sci Rep 12 (1), 13160 (2022)
   PUBMED   35915203
  REMARK    GeneRIF: The E3 ubiquitin ligase HECTD1 contributes to cell
            proliferation through an effect on mitosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2502)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 2502)
  AUTHORS   Aleidi,S.M., Yang,A., Sharpe,L.J., Rao,G., Cochran,B.J., Rye,K.A.,
            Kockx,M., Brown,A.J. and Gelissen,I.C.
  TITLE     The E3 ubiquitin ligase, HECTD1, is involved in ABCA1-mediated
            cholesterol export from macrophages
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1863 (4), 359-368 (2018)
   PUBMED   29306077
  REMARK    GeneRIF: HECTD1 may be involved in the regulation of ABCA1-mediated
            cholesterol export from unloaded macrophages to apoA-I.
REFERENCE   7  (residues 1 to 2502)
  AUTHORS   Fang,S., Guo,H., Cheng,Y., Zhou,Z., Zhang,W., Han,B., Luo,W.,
            Wang,J., Xie,W. and Chao,J.
  TITLE     circHECTD1 promotes the silica-induced pulmonary
            endothelial-mesenchymal transition via HECTD1
  JOURNAL   Cell Death Dis 9 (3), 396 (2018)
   PUBMED   29540674
  REMARK    GeneRIF: SiO2 concomitantly increased circHECTD1 expression, which,
            in turn, inhibited HECTD1 protein expression.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 2502)
  AUTHORS   Shen,X., Jia,Z., D'Alonzo,D., Wang,X., Bruder,E., Emch,F.H., De
            Geyter,C. and Zhang,H.
  TITLE     HECTD1 controls the protein level of IQGAP1 to regulate the
            dynamics of adhesive structures
  JOURNAL   Cell Commun Signal 15 (1), 2 (2017)
   PUBMED   28073378
  REMARK    GeneRIF: Hectd1 regulates the protein level of IQGAP1 through
            ubiquitination.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 2502)
  AUTHORS   Helander,S., Montecchio,M., Lemak,A., Fares,C., Almlof,J., Yi,Y.,
            Yee,A., Arrowsmith,C., DhePaganon,S. and Sunnerhagen,M.
  TITLE     Basic Tilted Helix Bundle - a new protein fold in human
            FKBP25/FKBP3 and HectD1
  JOURNAL   Biochem Biophys Res Commun 447 (1), 26-31 (2014)
   PUBMED   24667607
  REMARK    GeneRIF: our high-resolution structures show a new fold composed of
            five small helices where H3 and H4 are tilted in a novel
            arrangement; we call this fold the Basic Tilted Helix Bundle (BTHB)
            domain.
REFERENCE   10 (residues 1 to 2502)
  AUTHORS   Tran,H., Bustos,D., Yeh,R., Rubinfeld,B., Lam,C., Shriver,S.,
            Zilberleyb,I., Lee,M.W., Phu,L., Sarkar,A.A., Zohn,I.E.,
            Wertz,I.E., Kirkpatrick,D.S. and Polakis,P.
  TITLE     HectD1 E3 ligase modifies adenomatous polyposis coli (APC) with
            polyubiquitin to promote the APC-axin interaction
  JOURNAL   J Biol Chem 288 (6), 3753-3767 (2013)
   PUBMED   23277359
  REMARK    GeneRIF: HectD1 promotes the APC-Axin interaction to negatively
            regulate Wnt signaling.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136418.4, AL121808.4 and KC877516.1.
            
            On or before Apr 25, 2025 this sequence version replaced
            XP_047287161.1, XP_054231755.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1157917.1,
                                           SRR14372079.1082298.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2502
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..2502
                     /product="E3 ubiquitin-protein ligase HECTD1 isoform 9"
                     /EC_number="2.3.2.26"
                     /note="E3 ubiquitin-protein ligase HECTD1; E3 ligase for
                     inhibin receptor; HECT domain-containing protein 1; HECT
                     domain containing E3 ubiquitin protein ligase 1; HECT-type
                     E3 ubiquitin transferase HECTD1"
                     /calculated_mol_wt=277277
     Region          <366..>479
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          366..393
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          396..426
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(397,401..402,405..407,409..410,414,417,426,428,
                     432..433,436..438,440..441,445,448,457,459,461,465..466,
                     469..471,473..474,478)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          428..457
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1107..1240
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     Region          1277..>1321
                     /region_name="MIB_HERC2"
                     /note="Mib_herc2; pfam06701"
                     /db_xref="CDD:461991"
     Region          2023..2500
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(2029,2058,2068,2155,2433,2465..2466,2469..2473,2493,
                     2499)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(2248,2251..2252,2254..2255,2258,2300,2302,
                     2306..2307,2309,2315,2320,2337,2341)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..2502
                     /gene="HECTD1"
                     /gene_synonym="EULIR"
                     /coded_by="NM_001439061.1:800..8308"
                     /note="isoform 9 is encoded by transcript variant 10"
                     /db_xref="GeneID:25831"
                     /db_xref="HGNC:HGNC:20157"
                     /db_xref="MIM:618649"
ORIGIN      
        1 madvdpdtll ewlqmgqgde rdmqlialeq lcmlllmsdn vdrcfetcpp rtflpalcki
       61 fldesapdnv levtaraity yldvsaectr rivgvdgaik alcnrlvvve lnnrtsrdla
      121 eqcvkvleli ctresgavfe agglncvltf irdsghlvhk dtlhsamavv srlcgkmepq
      181 dssleicves lssllkhedh qvsdgalrcf asladrftrr gvdpaplakh glteellsrm
      241 aaaggtvsgp ssackpgrst tgapsttads klsnqvstiv sllstlcrgs pvvthdllrs
      301 elpdsiesal qgdercvldt mrlvdlllvl lfegrkalpk ssagstgrip glrrldssge
      361 rshrqlidci rskdtdalid aidtgafevn fmddvgqtll nwasafgtqe mveflcerga
      421 dvnrgqrsss lhyaacfgrp qvaktllrhg anpdlrdedg ktpldkarer ghsevvailq
      481 spgdwmcpvn kgddkkkkdt nkdeeecnep kgdpemapiy lkrllpvfaq tfqqtmlpsi
      541 rkaslalirk mihfcseall kevcdsdvgh nlptilveit atvldqeddd dghllalqii
      601 rdlvdkggdi fldqlarlgv iskvstlagp ssddeneees kpekedepqe dakelqqgkp
      661 yhwrdwsiir grdclyiwsd aaalelsngs ngwfrfildg klatmyssgs peggsdsses
      721 rsefleklqr argqvkpsts sqpilsapgp tkltvgnwsl tclkegeiai hnsdgqqati
      781 lkedlpgfvf esnrgtkhsf taetslgsef vtgwtgkrgr klksklektk qkvrtmardl
      841 yddhfkaves mprgvvvtlr niatqlessw elhtnrqcie sentwrdlmk talenlivll
      901 kdentispye mcssglvqal ltvlnnsmdl dmkqdcsqlv erinvfktaf seneddesrp
      961 avalirklia vlesierlpl hlydtpgsty nlqiltrrlr frlerapget alidrtgrml
     1021 kmeplatves leqyllkmva kqwydfdrss fvfvrklreg qnfifrhqhd fdengiiywi
     1081 gtnaktayew vnpaayglvv vtssegrnlp ygrledilsr dnsalnchsn ddknawfaid
     1141 lglwvipsay tlrhargygr salrnwvfqv skdgqnwtsl ythvddcsln epgstatwpl
     1201 dppkdekqgw rhvrikqmgk nasgqthyls lsgfelygtv ngvcedqlgk aakeaeanlr
     1261 rqrrlvrsqv lkymvpgarv irgldwkwrd qdgspqgegt vtgelhngtt qswsslvknn
     1321 cpdktsaaag sssrkgssss vcsvasssdi slgstkterr seivmehsiv sgadvhepiv
     1381 vlssaenvpq tevgssssas tstltaetgs enaerklgpd ssvrtpgess aismgivsvs
     1441 spdvssvsel tnkeaasqrp lsssasnrls vssllaagap msssasvpnl ssretssles
     1501 fvrrvaniar tnatnnmnls rsssdnntnt lgrnvmstat splmgaqsfp nlttpgttst
     1561 vtmstssvts ssnvatattv lsvgqslsnt lttsltstss esdtgqeaey slydfldscr
     1621 astllaeldd dedlpepdee ddeneddnqe dqeyeevmil rrpslqrrag srsdvthhav
     1681 tsqlpqvpag agsrpigeqe eeeyetkggr rrtwdddyvl krqfsalvpa fdprpgrtnv
     1741 qqttdleipp pgtphselle evectpsprl altlkvtglg ttrevelplt nfrstifyyv
     1801 qkllqlscng nvksdklrri weptytimyr emkdsdkeke ngkmdfcehg tksglnqgai
     1861 stlqssdiln ltkeqpqaka gngqnscgve dvlqllrily ivasdpysri sqedgdeqpq
     1921 ftfppdefts kkittkilqq ieeplalasg alpdwceqlt skcpflipfe trqlyftcta
     1981 fgasraivwl qnrreatver trttssvrrd dpgefrvgrl khervkvprg eslmewaenv
     2041 mqihadrksv leveflgeeg tglgptlefy alvaaefqrt dlgawlcddn fpddesrhvd
     2101 lggglkppgy yvqrscglft apfpqdsdel eritklfhfl giflakciqd nrlvdlpisk
     2161 pffklmcmgd iksnmskliy esrgdrdlhc tesqseaste eghdslsvgs feedsksefi
     2221 ldppkpkppa wfngiltwed felvnphrar flkeikdlai krrqilsnkg lsedekntkl
     2281 qelvlknpsg sgpplsiedl glnfqfcpss riygftavdl kpsgedemit mdnaeeyvdl
     2341 mfdfcmhtgi qkqmeafrdg fnkvfpmekl ssfsheevqm ilcgnqspsw aaediinyte
     2401 pklgytrdsp gflrfvrvlc gmssderkaf lqfttgcstl ppgglanlhp rltvvrkvda
     2461 tdasypsvnt cvhylklpey sseeimrerl laatmekgfh ln
//
LOCUS       NP_001424675             566 aa            linear   PRI 21-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 9 [Homo sapiens].
ACCESSION   NP_001424675
VERSION     NP_001424675.1
DBSOURCE    REFSEQ: accession NM_001437746.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 566)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 566)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 566)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 566)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 566)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008641.7.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.263023.1,
                                           SRR14243140.4811610.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..566
                     /product="TNFAIP3-interacting protein 1 isoform 9"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=64091
     Region          <161..>198
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          <245..>485
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..566
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001437746.1:179..1879"
                     /note="isoform 9 is encoded by transcript variant 26"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 meatrlrqka eelvkdnell pppspslgsf dplaeltgkd snvtasptap acpsdkpapv
       61 qkppssgtss efevvtpeeq nspessshan amalgplpre dgnlmlhlqr lettlsvcae
      121 epdhgqlfth lgrmalefnr laskvhkneq rtsilqtlce qlrkenealk akldkgleqr
      181 dqaaerlree nlelkkllms ngnkegasgr pgspkmegtg kkavagqqqa svtagkvpev
      241 valgaaekkv kmleqqrsel levnkqwdqh frsmkqqyeq kitelrqkla dlqkqvtdle
      301 aereqkqrdf drklllaksk iemeetdkeq ltaeakelrq kvkylqdqls pltrqreyqe
      361 keiqrlnkal eealsiqtpp sspptafgsp egagallrkq elvtqnellk qqvkifeedf
      421 qrersdrerm neekeelkkq veklqaqvtl snaqlkafkd eekarealrq qkrkakasge
      481 ryhvephpeh lcgaypyayp pmpamvphhg fedwsqiryp pppmamehpp plpnsrlfhl
      541 hqfcrsrntp gvypvegfei qirapk
//
LOCUS       NP_001389632            1173 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 13 [Homo sapiens].
ACCESSION   NP_001389632
VERSION     NP_001389632.1
DBSOURCE    REFSEQ: accession NM_001402703.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1173)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1173)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1173)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1173)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1173)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1173)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1173)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1173)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1173)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1173)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3324324.1,
                                           SRR14038195.1146660.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1173
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1173
                     /product="kinectin isoform 13"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=135236
     Region          <142..>400
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          296..1086
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          <1006..>1173
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1173
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402703.1:178..3699"
                     /note="isoform 13 is encoded by transcript variant 26"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mvpskrqeal plhqetkqes gsgkkkassk kqktenvfvd eplihattyi plmdnadssp
       61 vvdkrevidl lkpdqvegiq ksgtkklkte tdkenaevkf kdfllslktm mfsedealcv
      121 vdllkeksgv iqdalkkssk gelttlihql qekdkllaav kedaaatkdr ckqltqemmt
      181 ekersnvvit rmkdrigtle kehnvfqnki hvsyqetqqm qmkfqqvreq meaeiahlkq
      241 engilrdavs nttnqleskq saelnklrqd yarlvnelte ktgklqqeev qkknaeqaat
      301 qlkvqlqeae rrweevqsyi rkrtaeheaa qqdlqskfva kenevqslhs kltdtlvskq
      361 qleqrlmqlm eseqkrvnke eslqmqvqdi leqnealkaq iqqfhsqiaa qtsasvlaee
      421 lhkviaekdk qikqtedsla serdrltske eelkdiqnmn fllkaevqkl qalaneqaaa
      481 ahelekmqqs vyvkddkirl leeqlqheis nkmeefkiln dqnkalksev qklqtlvseq
      541 pnkdvveqme kciqekdekl ktveelletg liqvatkeee lnairtenss ltkevqdlka
      601 kqndqvsfas lveelkkvih ekdgkiksve elleaellkv ankektvqdl kqeikalkee
      661 ignvqlekaq qlsitskvqe lqnllkgkee qmntmkavle ekekdlantg kwlqdlqeen
      721 eslkahvqev aqhnlkeass asqfeeleiv lkekenelkr leamlkeres dlssktqllq
      781 dvqdenklfk sqieqlkqqn yqqassfpph eellkviser ekeisglwne ldslkdaveh
      841 qrkknndlre knweameala stekmlqdkv nktskerqqq veaveleake vlkklfpkvs
      901 vpsnlsygew lhgfekkake cmagtsgsee vkvlehklke ademhtllql ecekyksvla
      961 etegilqklq rsveqeenkw kvkvdeshkt ikqmqssfts seqelerlrs enkdienlrr
     1021 erehlemele kaemerstyv tevrelkdll telqkkldds yseavrqnee lnllkaqlne
     1081 tltklrteqn erqkvagdlh kaqqsleliq skivkaagdt tviensdvsp etesseketm
     1141 svslnqtvtq lqqllqavnq qltkekehyq vle
//
LOCUS       NP_001424666             582 aa            linear   PRI 21-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 7 [Homo sapiens].
ACCESSION   NP_001424666 XP_047272580 XP_054207398
VERSION     NP_001424666.1
DBSOURCE    REFSEQ: accession NM_001437737.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 582)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 582)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 582)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 582)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 582)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 582)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008641.7.
            
            On or before Apr 9, 2025 this sequence version replaced
            XP_047272580.1, XP_054207398.1.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2504344.1,
                                           SRR14038197.1776162.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..582
                     /product="TNFAIP3-interacting protein 1 isoform 7"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=65805
     Region          <161..>198
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          <245..>485
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..582
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001437737.1:106..1854"
                     /note="isoform 7 is encoded by transcript variant 16"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 meatrlrqka eelvkdnell pppspslgsf dplaeltgkd snvtasptap acpsdkpapv
       61 qkppssgtss efevvtpeeq nspessshan amalgplpre dgnlmlhlqr lettlsvcae
      121 epdhgqlfth lgrmalefnr laskvhkneq rtsilqtlce qlrkenealk akldkgleqr
      181 dqaaerlree nlelkkllms ngnkegasgr pgspkmegtg kkavagqqqa svtagkvpev
      241 valgaaekkv kmleqqrsel levnkqwdqh frsmkqqyeq kitelrqkla dlqkqvtdle
      301 aereqkqrdf drklllaksk iemeetdkeq ltaeakelrq kvkylqdqls pltrqreyqe
      361 keiqrlnkal eealsiqtpp sspptafgsp egagallrkq elvtqnellk qqvkifeedf
      421 qrersdrerm neekeelkkq veklqaqvtl snaqlkafkd eekarealrq qkrkakasge
      481 ryhvephpeh lcgaypyayp pmpamvphhg fedwsqiryp pppmamehpp plpnsrlfhl
      541 peytwrlpcg gvrnpnqssq vmdpptarpt epepadlrlp rn
//
LOCUS       NP_001397930             570 aa            linear   PRI 21-NOV-2025
DEFINITION  nucleoporin p58/p45 isoform c [Homo sapiens].
ACCESSION   NP_001397930 XP_011533630
VERSION     NP_001397930.1
DBSOURCE    REFSEQ: accession NM_001411001.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Targa,A., Larrimore,K.E., Wong,C.K., Chong,Y.L., Fung,R., Lee,J.,
            Choi,H. and Rancati,G.
  TITLE     Non-genetic and genetic rewiring underlie adaptation to hypomorphic
            alleles of an essential gene
  JOURNAL   EMBO J 40 (21), e107839 (2021)
   PUBMED   34528284
  REMARK    GeneRIF: Non-genetic and genetic rewiring underlie adaptation to
            hypomorphic alleles of an essential gene.
REFERENCE   3  (residues 1 to 570)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 570)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 570)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 570)
  AUTHORS   Kaltenbach,L.S., Romero,E., Becklin,R.R., Chettier,R., Bell,R.,
            Phansalkar,A., Strand,A., Torcassi,C., Savage,J., Hurlburt,A.,
            Cha,G.H., Ukani,L., Chepanoske,C.L., Zhen,Y., Sahasrabudhe,S.,
            Olson,J., Kurschner,C., Ellerby,L.M., Peltier,J.M., Botas,J. and
            Hughes,R.E.
  TITLE     Huntingtin interacting proteins are genetic modifiers of
            neurodegeneration
  JOURNAL   PLoS Genet 3 (5), e82 (2007)
   PUBMED   17500595
REFERENCE   7  (residues 1 to 570)
  AUTHORS   Le Rouzic,E., Mousnier,A., Rustum,C., Stutz,F., Hallberg,E.,
            Dargemont,C. and Benichou,S.
  TITLE     Docking of HIV-1 Vpr to the nuclear envelope is mediated by the
            interaction with the nucleoporin hCG1
  JOURNAL   J Biol Chem 277 (47), 45091-45098 (2002)
   PUBMED   12228227
REFERENCE   8  (residues 1 to 570)
  AUTHORS   Ben-Efraim,I. and Gerace,L.
  TITLE     Gradient of increasing affinity of importin beta for nucleoporins
            along the pathway of nuclear import
  JOURNAL   J Cell Biol 152 (2), 411-417 (2001)
   PUBMED   11266456
REFERENCE   9  (residues 1 to 570)
  AUTHORS   Shiota,C., Coffey,J., Grimsby,J., Grippo,J.F. and Magnuson,M.A.
  TITLE     Nuclear import of hepatic glucokinase depends upon glucokinase
            regulatory protein, whereas export is due to a nuclear export
            signal sequence in glucokinase
  JOURNAL   J Biol Chem 274 (52), 37125-37130 (1999)
   PUBMED   10601273
REFERENCE   10 (residues 1 to 570)
  AUTHORS   Buss,F. and Stewart,M.
  TITLE     Macromolecular interactions in the nucleoporin p62 complex of rat
            nuclear pores: binding of nucleoporin p54 to the rod domain of p62
  JOURNAL   J Cell Biol 128 (3), 251-261 (1995)
   PUBMED   7531196
  REMARK    GeneRIF: The human gene NUPL1 shares 87% sequence identity with rat
            nucleoporin p58.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590787.24, AL646102.4 and
            AL138958.18.
            
            On Aug 20, 2022 this sequence version replaced XP_011533630.1.
            
            Summary: This gene encodes a member of the nucleoporin family that
            shares 87% sequence identity with rat nucleoporin p58. The protein
            is localized to the nuclear rim and is a component of the nuclear
            pore complex (NPC). All molecules entering or leaving the nucleus
            either diffuse through or are actively transported by the NPC.
            Alternate transcriptional splice variants, encoding different
            isoforms, have been characterized. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.370200.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.13"
     Protein         1..570
                     /product="nucleoporin p58/p45 isoform c"
                     /note="nucleoporin p58/p45; nucleoporin-like protein 1;
                     nucleoporin like 1; 58 kDa nucleoporin; nucleoporin 58kDa"
                     /calculated_mol_wt=58387
     Region          3..553
                     /region_name="Nucleoporin_FG2"
                     /note="Nucleoporin FG repeated region; pfam15967"
                     /db_xref="CDD:435043"
     CDS             1..570
                     /gene="NUP58"
                     /gene_synonym="NUP45; NUPL1; PRO2463"
                     /coded_by="NM_001411001.1:150..1862"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS91790.1"
                     /db_xref="GeneID:9818"
                     /db_xref="HGNC:HGNC:20261"
                     /db_xref="MIM:607615"
ORIGIN      
        1 mstgfsfgsg tlgsttvaag gtstggvfsf gtgassnpsv glnfgnlgst stpattsaps
       61 sgfgtglfgs kpatgftlgg tntgiattit tgltlgtpat tsaattgfsl gfnkpaasat
      121 pfalpitsts asgltlssal tstpaastgf tlnnlggtta ttttastgls lggalaglgg
      181 slfqstntgt sglgqnalgl tlgttaatst agneglggid fssssdkksd ktgtrpedsk
      241 alkdenlppv icqdvenlqk fvkeqkqvqe eisrmsskam lkvqedikal kqllslaang
      301 iqrntlnidk lkietaqelk naeialrtqk tppglqheya apadyfrilv qqfevqlqqy
      361 rqqieelenh latqannshi tpqdlsmamq kiyqtfvala aqlqsihenv kvlkeqylgy
      421 rkmflgdavd vfetrraeak kwqntprvtt gptpfstmpn aaavamaatl tqqqqpatgp
      481 qpslgvsfgt pfgsgigtgl qssglgssnl ggfgtssgfg csttgastfg fgttnkpsgs
      541 lsagnksqvl tefrkpsvte tneigrkiqf
//
LOCUS       NP_001427455             287 aa            linear   PRI 21-NOV-2025
DEFINITION  syntaxin-3 isoform 4 [Homo sapiens].
ACCESSION   NP_001427455 XP_005274255 XP_054225739
VERSION     NP_001427455.1
DBSOURCE    REFSEQ: accession NM_001440526.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Shinozuka,T., Kanda,M., Sato,Y., Shimizu,D., Tanaka,C., Umeda,S.,
            Inokawa,Y., Hattori,N., Hayashi,M., Nakayama,G. and Kodera,Y.
  TITLE     Increased STX3 transcript and protein levels were associated with
            poor prognosis in two independent cohorts of esophageal squamous
            cell carcinoma patients
  JOURNAL   Cancer Med 12 (24), 22185-22195 (2023)
   PUBMED   38014487
  REMARK    GeneRIF: Increased STX3 transcript and protein levels were
            associated with poor prognosis in two independent cohorts of
            esophageal squamous cell carcinoma patients.
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Janecke,A.R., Liu,X., Adam,R., Punuru,S., Viestenz,A., Strauss,V.,
            Laass,M., Sanchez,E., Adachi,R., Schatz,M.P., Saboo,U.S.,
            Mittal,N., Rohrschneider,K., Escher,J., Ganesh,A., Al Zuhaibi,S.,
            Al Murshedi,F., AlSaleem,B., Alfadhel,M., Al Sinani,S.,
            Alkuraya,F.S., Huber,L.A., Muller,T., Heidelberger,R. and Janz,R.
  TITLE     Pathogenic STX3 variants affecting the retinal and intestinal
            transcripts cause an early-onset severe retinal dystrophy in
            microvillus inclusion disease subjects
  JOURNAL   Hum Genet 140 (8), 1143-1156 (2021)
   PUBMED   33974130
  REMARK    GeneRIF: Pathogenic STX3 variants affecting the retinal and
            intestinal transcripts cause an early-onset severe retinal
            dystrophy in microvillus inclusion disease subjects.
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Low,S.H., Vasanji,A., Nanduri,J., He,M., Sharma,N., Koo,M.,
            Drazba,J. and Weimbs,T.
  TITLE     Syntaxins 3 and 4 are concentrated in separate clusters on the
            plasma membrane before the establishment of cell polarity
  JOURNAL   Mol Biol Cell 17 (2), 977-989 (2006)
   PUBMED   16339081
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Martin-Martin,B., Nabokina,S.M., Lazo,P.A. and Mollinedo,F.
  TITLE     Co-expression of several human syntaxin genes in neutrophils and
            differentiating HL-60 cells: variant isoforms and detection of
            syntaxin 1
  JOURNAL   J Leukoc Biol 65 (3), 397-406 (1999)
   PUBMED   10080545
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Steegmaier,M., Yang,B., Yoo,J.S., Huang,B., Shen,M., Yu,S., Luo,Y.
            and Scheller,R.H.
  TITLE     Three novel proteins of the syntaxin/SNAP-25 family
  JOURNAL   J Biol Chem 273 (51), 34171-34179 (1998)
   PUBMED   9852078
REFERENCE   8  (residues 1 to 287)
  AUTHORS   Riento,K., Galli,T., Jansson,S., Ehnholm,C., Lehtonen,E. and
            Olkkonen,V.M.
  TITLE     Interaction of Munc-18-2 with syntaxin 3 controls the association
            of apical SNAREs in epithelial cells
  JOURNAL   J Cell Sci 111 (Pt 17), 2681-2688 (1998)
   PUBMED   9701566
REFERENCE   9  (residues 1 to 287)
  AUTHORS   Galli,T., Zahraoui,A., Vaidyanathan,V.V., Raposo,G., Tian,J.M.,
            Karin,M., Niemann,H. and Louvard,D.
  TITLE     A novel tetanus neurotoxin-insensitive vesicle-associated membrane
            protein in SNARE complexes of the apical plasma membrane of
            epithelial cells
  JOURNAL   Mol Biol Cell 9 (6), 1437-1448 (1998)
   PUBMED   9614185
REFERENCE   10 (residues 1 to 287)
  AUTHORS   Delgrossi,M.H., Breuza,L., Mirre,C., Chavrier,P. and Le Bivic,A.
  TITLE     Human syntaxin 3 is localized apically in human intestinal cells
  JOURNAL   J Cell Sci 110 (Pt 18), 2207-2214 (1997)
   PUBMED   9378770
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000640.5.
            
            On or before May 21, 2025 this sequence version replaced
            XP_005274255.1, XP_054225739.1.
            
            Summary: The gene is a member of the syntaxin family. The encoded
            protein is targeted to the apical membrane of epithelial cells
            where it forms clusters and is important in establishing and
            maintaining polarity necessary for protein trafficking involving
            vesicle fusion and exocytosis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1019295.1,
                                           SRR14038192.1008457.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..287
                     /product="syntaxin-3 isoform 4"
                     /note="syntaxin 3A; syntaxin 3B"
                     /calculated_mol_wt=32922
     Region          34..226
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     Region          194..260
                     /region_name="SNARE"
                     /note="SNARE motif; cl22856"
                     /db_xref="CDD:473982"
     Site            order(222,229,232)
                     /site_type="other"
                     /note="flanking leucine-zipper layers"
                     /db_xref="CDD:277229"
     Site            225
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277229"
     CDS             1..287
                     /gene="STX3"
                     /gene_synonym="DIAR12; MVID2; RDMVID; STX3A"
                     /coded_by="NM_001440526.1:231..1094"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:6809"
                     /db_xref="HGNC:HGNC:11438"
                     /db_xref="MIM:600876"
ORIGIN      
        1 mkdrleqlka kqltqdddtd aveiaidnta fmdeffseie etrlnidkis ehveeakkly
       61 siilsapipe pktkddleql tteikkrann vrnklksmek hieedevrss adlrirksqh
      121 svlsrkfvev mtkyneaqvd frerskgriq rqleitgkkt tdeeleemle sgnpaiftsg
      181 iidsqiskqa lseiegrhkd ivrlessike lhdmfmdiam lvenqgemld nielnvmhtv
      241 dhvekardet kkavkyqsqa rkkkimimic ciilaiilas tigsifa
//
LOCUS       NP_001424519             581 aa            linear   PRI 21-NOV-2025
DEFINITION  glycerol kinase isoform 6 [Homo sapiens].
ACCESSION   NP_001424519 XP_006724546 XP_054182804
VERSION     NP_001424519.1
DBSOURCE    REFSEQ: accession NM_001437590.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Ying,F., Chen,X. and Lv,L.
  TITLE     Glycerol kinase enzyme is a prognostic predictor in esophageal
            carcinoma and is associated with immune cell infiltration
  JOURNAL   Sci Rep 14 (1), 3922 (2024)
   PUBMED   38365953
  REMARK    GeneRIF: Glycerol kinase enzyme is a prognostic predictor in
            esophageal carcinoma and is associated with immune cell
            infiltration.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Rani,R.M., Syngkli,S., Nongkhlaw,J. and Das,B.
  TITLE     Expression and characterisation of human glycerol kinase: the role
            of solubilising agents and molecular chaperones
  JOURNAL   Biosci Rep 43 (4) (2023)
   PUBMED   37021775
  REMARK    GeneRIF: Expression and characterisation of human glycerol kinase:
            the role of solubilising agents and molecular chaperones.
            Erratum:[Biosci Rep. 2023 Oct 31;43(10):BSR-2022-2258_COR. doi:
            10.1042/BSR-2022-2258_COR. PMID: 37860917]
REFERENCE   4  (residues 1 to 581)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 581)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 581)
  AUTHORS   Sargent,C.A., Young,C., Marsh,S., Ferguson-Smith,M.A. and
            Affara,N.A.
  TITLE     The glycerol kinase gene family: structure of the Xp gene, and
            related intronless retroposons
  JOURNAL   Hum Mol Genet 3 (8), 1317-1324 (1994)
   PUBMED   7987308
REFERENCE   7  (residues 1 to 581)
  AUTHORS   Achermann,J.C. and Vilain,E.J.
  TITLE     NR0B1-Related Adrenal Hypoplasia Congenita
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301604
REFERENCE   8  (residues 1 to 581)
  AUTHORS   Love,D.R., Bloomfield,J.F., Kenwrick,S.J., Yates,J.R. and
            Davies,K.E.
  TITLE     Physical mapping distal to the DMD locus
  JOURNAL   Genomics 8 (1), 106-112 (1990)
   PUBMED   2081587
REFERENCE   9  (residues 1 to 581)
  AUTHORS   Pillers,D.A., Weleber,R.G., Powell,B.R., Hanna,C.E., Magenis,R.E.
            and Buist,N.R.
  TITLE     Aland Island eye disease (Forsius-Eriksson ocular albinism) and an
            Xp21 deletion in a patient with Duchenne muscular dystrophy,
            glycerol kinase deficiency, and congenital adrenal hypoplasia
  JOURNAL   Am J Med Genet 36 (1), 23-28 (1990)
   PUBMED   2159212
REFERENCE   10 (residues 1 to 581)
  AUTHORS   Kaneko,M., Kurokawa,M. and Ishibashi,S.
  TITLE     Binding and function of mitochondrial glycerol kinase in comparison
            with those of mitochondrial hexokinase
  JOURNAL   Arch Biochem Biophys 237 (1), 135-141 (1985)
   PUBMED   2982325
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005913.2, AC117404.7 and
            AC112496.2.
            
            On or before Apr 4, 2025 this sequence version replaced
            XP_006724546.1, XP_054182804.1.
            
            Summary: The protein encoded by this gene belongs to the FGGY
            kinase family. This protein is a key enzyme in the regulation of
            glycerol uptake and metabolism. It catalyzes the phosphorylation of
            glycerol by ATP, yielding ADP and glycerol-3-phosphate. Mutations
            in this gene are associated with glycerol kinase deficiency (GKD).
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Mar
            2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1374559.1,
                                           SRR14038192.2102836.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp21.2"
     Protein         1..581
                     /product="glycerol kinase isoform 6"
                     /EC_number="2.7.1.30"
                     /note="ATP:glycerol 3-phosphotransferase; glycerokinase"
                     /calculated_mol_wt=62903
     Region          11..538
                     /region_name="ASKHA_NBD_FGGY_GK1-3-like"
                     /note="nucleotide-binding domain (NBD) of metazoan
                     glycerol kinase 1-3 (GK1-3) and similar proteins; cd07792"
                     /db_xref="CDD:466802"
     CDS             1..581
                     /gene="GK"
                     /gene_synonym="GK1; GKD"
                     /coded_by="NM_001437590.1:116..1861"
                     /note="isoform 6 is encoded by transcript variant 13"
                     /db_xref="GeneID:2710"
                     /db_xref="HGNC:HGNC:4289"
                     /db_xref="MIM:300474"
ORIGIN      
        1 maaskkavlg plvgavdqgt sstrflvfns ktaellshhq veikqefpre gwveqdpkei
       61 lhsvyeciek tceklgqlni disnikaigv snqrettvvw dkitgeplyn avaapvspgp
      121 svpvavvpsg ssvpapgtss vwldlrtqst veslskripg nnnfvksktg lplstyfsav
      181 klrwlldnvr kvqkaveekr alfgtidswl iwsltggvng gvhctdvtna srtmlfnihs
      241 lewdkqlcef fgipmeilpn vrssseiygl mkagalegvp isgclgdqsa alvgqmcfqi
      301 gqakntygtg cfllcntghk cvfsdhgllt tvayklgrdk pvyyalegsv aiagavirwl
      361 rdnlgiikts eeieklakev gtsygcyfvp afsglyapyw epsargiicg ltqftnkchi
      421 afaaleavcf qtreildamn rdcgiplshl qvdggmtsnk ilmqlqadil yipvvkpsmp
      481 ettalgaama agaaegvgvw slepedlsav tmerfepqin aeeseiryst wkkavmksmg
      541 wvttqspesg dpsifcslpl gffivssmvm ligaryisgi p
//
LOCUS       NP_001427285             734 aa            linear   PRI 21-NOV-2025
DEFINITION  general transcription and DNA repair factor IIH helicase subunit
            XPD isoform 4 [Homo sapiens].
ACCESSION   NP_001427285 XP_011524913 XP_054176156
VERSION     NP_001427285.1
DBSOURCE    REFSEQ: accession NM_001440356.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Barbour,J.A., Ou,T., Yang,H., Fang,H., Yue,N.C., Zhu,X.,
            Wong-Brown,M.W., Wong,Y.T., Bowden,N.A., Wu,S. and Wong,J.W.H.
  TITLE     ERCC2 mutations alter the genomic distribution pattern of somatic
            mutations and are independently prognostic in bladder cancer
  JOURNAL   Cell Genom 4 (8), 100627 (2024)
   PUBMED   39096913
  REMARK    GeneRIF: ERCC2 mutations alter the genomic distribution pattern of
            somatic mutations and are independently prognostic in bladder
            cancer.
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Zeng,W., Xu,W. and Long,W.
  TITLE     The association between XPD rs13181 and rs1799793 polymorphism and
            oral cancer risk: evidence from a meta-analysis
  JOURNAL   BMC Cancer 24 (1), 738 (2024)
   PUBMED   38879503
  REMARK    GeneRIF: The association between XPD rs13181 and rs1799793
            polymorphism and oral cancer risk: evidence from a meta-analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 734)
  AUTHORS   Gudur,A.K., Kale,S.R., Gudur,R.A., Bhosale,S.J. and Datkhile,K.D.
  TITLE     Genetic Polymorphisms of XPC, XPD, XPG Genes and their Association
            with Radiotherapy Induced Toxicity among Head and Neck Cancer
            Patients: A Hospital Based Study from Maharashtra
  JOURNAL   Asian Pac J Cancer Prev 25 (1), 191-199 (2024)
   PUBMED   38285784
  REMARK    GeneRIF: Genetic Polymorphisms of XPC, XPD, XPG Genes and their
            Association with Radiotherapy Induced Toxicity among Head and Neck
            Cancer Patients: A Hospital Based Study from Maharashtra.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 734)
  AUTHORS   Fu,I., Geacintov,N.E. and Broyde,S.
  TITLE     Differing structures and dynamics of two photolesions portray
            verification differences by the human XPD helicase
  JOURNAL   Nucleic Acids Res 51 (22), 12261-12274 (2023)
   PUBMED   37933861
  REMARK    GeneRIF: Differing structures and dynamics of two photolesions
            portray verification differences by the human XPD helicase.
REFERENCE   5  (residues 1 to 734)
  AUTHORS   Sun,G.F. and Ding,H.
  TITLE     NOP2-mediated m5C methylation of XPD is associated with
            hepatocellular carcinoma progression
  JOURNAL   Neoplasma 70 (3), 340-349 (2023)
   PUBMED   37498063
  REMARK    GeneRIF: NOP2-mediated m5C methylation of XPD is associated with
            hepatocellular carcinoma progression.
REFERENCE   6  (residues 1 to 734)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
REFERENCE   7  (residues 1 to 734)
  AUTHORS   Flejter,W.L., McDaniel,L.D., Johns,D., Friedberg,E.C. and
            Schultz,R.A.
  TITLE     Correction of xeroderma pigmentosum complementation group D mutant
            cell phenotypes by chromosome and gene transfer: involvement of the
            human ERCC2 DNA repair gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 261-265 (1992)
   PUBMED   1729695
REFERENCE   8  (residues 1 to 734)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 734)
  AUTHORS   Weber,C.A., Salazar,E.P., Stewart,S.A. and Thompson,L.H.
  TITLE     ERCC2: cDNA cloning and molecular characterization of a human
            nucleotide excision repair gene with high homology to yeast RAD3
  JOURNAL   EMBO J 9 (5), 1437-1447 (1990)
   PUBMED   2184031
REFERENCE   10 (residues 1 to 734)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from L47234.2.
            
            On or before May 19, 2025 this sequence version replaced
            XP_011524913.1, XP_054176156.1.
            
            Summary: The nucleotide excision repair pathway is a mechanism to
            repair damage to DNA. The protein encoded by this gene is involved
            in transcription-coupled nucleotide excision repair and is an
            integral member of the basal transcription factor BTF2/TFIIH
            complex. The gene product has ATP-dependent DNA helicase activity
            and belongs to the RAD3/XPD subfamily of helicases. Defects in this
            gene can result in three different disorders, the cancer-prone
            syndrome xeroderma pigmentosum complementation group D,
            trichothiodystrophy, and Cockayne syndrome. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853560.14874.1,
                                           SRR18074968.3432657.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..734
                     /product="general transcription and DNA repair factor IIH
                     helicase subunit XPD isoform 4"
                     /EC_number="5.6.2.3"
                     /note="xeroderma pigmentosum complementary group D; TFIIH
                     basal transcription factor complex helicase XPD subunit;
                     TFIIH subunit XPD; DNA 5'-3' helicase XPD; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 2; xeroderma pigmentosum group
                     D-complementing protein; TFIIH basal transcription factor
                     complex 80 kDa subunit; BTF2 p80; TFIIH p80; TFIIH 80 kDa
                     subunit; DNA excision repair protein ERCC-2; DNA repair
                     protein complementing XP-D cells; basic transcription
                     factor 2 80 kDa subunit; excision repair
                     cross-complementation group 2; general transcription and
                     DNA repair factor IIH helicase subunit XPD"
                     /calculated_mol_wt=84066
     Region          7..682
                     /region_name="rad3"
                     /note="DNA repair helicase (rad3); TIGR00604"
                     /db_xref="CDD:273169"
     CDS             1..734
                     /gene="ERCC2"
                     /gene_synonym="COFS2; CXPD; EM9; TFIIH; TTD; TTD1; XPD"
                     /coded_by="NM_001440356.1:34..2238"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:2068"
                     /db_xref="HGNC:HGNC:3434"
                     /db_xref="MIM:126340"
ORIGIN      
        1 mklnvdgllv yfpydyiype qfsymrelkr tldakayple vtkliycsrt vpeiekviee
       61 lrkllnfyek qegeklpflg lalssrknlc ihpevtplrf gkdvdgkchs ltasyvraqy
      121 qhdtslphcr fyeefdahgr evplpagiyn lddlkalgrr qgwcpyflar ysilhanvvv
      181 ysyhylldpk iadlvskela rkavvvfdea hnidnvcids msvnltrrtl drcqgnletl
      241 qktvlriket deqrlrdeyr rlveglreas aaretdahla npvlpdevlq eavpgsirta
      301 ehflgflrrl leyvkwrlrv qhvvqesppa flsglaqrvc iqrkplrfca erlrsllhtl
      361 eitdladfsp ltllanfatl vstyakgfti iiepfddrtp tianpilhfs cmdaslaikp
      421 vferfqsvii tsgtlspldi ypkildfhpv tmatftmtla rvclcpmiig rgndqvaiss
      481 kfetrediav irnygnllle msavvpdgiv afftsyqyme stvaswyeqg ileniqrnkl
      541 lfietqdgae tsvalekyqe acengrgail lsvargkvse gidfvhhygr avimfgvpyv
      601 ytqsrilkar leylrdqfqi rendfltfda mrhaaqcvgr airgktdygl mvfadkrfar
      661 gdkrgklprw iqehltdanl nltvdegvqv akyflrqmaq pfhredqlgl sllsleqles
      721 eetlkrieqi aqql
//
LOCUS       NP_001425831             336 aa            linear   PRI 21-NOV-2025
DEFINITION  STAM-binding protein isoform 5 [Homo sapiens].
ACCESSION   NP_001425831 XP_047298928 XP_054196184
VERSION     NP_001425831.1
DBSOURCE    REFSEQ: accession NM_001438902.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Zhang,W., Xu,Z., Du,Y., Liu,T., Xiong,Z., Hu,J., Chen,L., Peng,X.
            and Zhou,F.
  TITLE     Identification of STAM-binding protein as a target for the
            treatment of gemcitabine resistance pancreatic cancer in a
            nutrient-poor microenvironment
  JOURNAL   Cell Death Dis 15 (9), 657 (2024)
   PUBMED   39242557
  REMARK    GeneRIF: Identification of STAM-binding protein as a target for the
            treatment of gemcitabine resistance pancreatic cancer in a
            nutrient-poor microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Li,L., Yang,X., He,M., Xu,X., Xuan,X., Zhang,J., Zhang,L., Xu,H.
            and Li,D.
  TITLE     The expression and clinical significance of STAMBP in breast cancer
  JOURNAL   Mol Biol Rep 50 (1), 899-906 (2023)
   PUBMED   36309616
  REMARK    GeneRIF: The expression and clinical significance of STAMBP in
            breast cancer.
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Yang,Q., Yan,D., Zou,C., Xue,Q., Lin,S., Huang,Q., Li,X., Tang,D.,
            Chen,X. and Liu,J.
  TITLE     The deubiquitinating enzyme STAMBP is a newly discovered driver of
            triple-negative breast cancer progression that maintains RAI14
            protein stability
  JOURNAL   Exp Mol Med 54 (11), 2047-2059 (2022)
   PUBMED   36434041
  REMARK    GeneRIF: The deubiquitinating enzyme STAMBP is a newly discovered
            driver of triple-negative breast cancer progression that maintains
            RAI14 protein stability.
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Yu,S., E,C. and Yang,J.
  TITLE     STAM binding protein regulated by hsa_circ_0007334 exerts oncogenic
            potential in pancreatic cancer
  JOURNAL   Pancreatology 22 (7), 1003-1012 (2022)
   PUBMED   36089485
  REMARK    GeneRIF: STAM binding protein regulated by hsa_circ_0007334 exerts
            oncogenic potential in pancreatic cancer.
REFERENCE   6  (residues 1 to 336)
  AUTHORS   Itoh,F., Asao,H., Sugamura,K., Heldin,C.H., ten Dijke,P. and
            Itoh,S.
  TITLE     Promoting bone morphogenetic protein signaling through negative
            regulation of inhibitory Smads
  JOURNAL   EMBO J 20 (15), 4132-4142 (2001)
   PUBMED   11483516
REFERENCE   7  (residues 1 to 336)
  AUTHORS   Endo,K., Takeshita,T., Kasai,H., Sasaki,Y., Tanaka,N., Asao,H.,
            Kikuchi,K., Yamada,M., Chenb,M., O'Shea,J.J. and Sugamura,K.
  TITLE     STAM2, a new member of the STAM family, binding to the Janus
            kinases
  JOURNAL   FEBS Lett 477 (1-2), 55-61 (2000)
   PUBMED   10899310
REFERENCE   8  (residues 1 to 336)
  AUTHORS   Tanaka,N., Kaneko,K., Asao,H., Kasai,H., Endo,Y., Fujita,T.,
            Takeshita,T. and Sugamura,K.
  TITLE     Possible involvement of a novel STAM-associated molecule 'AMSH' in
            intracellular signal transduction mediated by cytokines
  JOURNAL   J Biol Chem 274 (27), 19129-19135 (1999)
   PUBMED   10383417
REFERENCE   9  (residues 1 to 336)
  AUTHORS   Asada,H., Ishii,N., Sasaki,Y., Endo,K., Kasai,H., Tanaka,N.,
            Takeshita,T., Tsuchiya,S., Konno,T. and Sugamura,K.
  TITLE     Grf40, A novel Grb2 family member, is involved in T cell signaling
            through interaction with SLP-76 and LAT
  JOURNAL   J Exp Med 189 (9), 1383-1390 (1999)
   PUBMED   10224278
REFERENCE   10 (residues 1 to 336)
  AUTHORS   Carter,M.T., Mirzaa,G., McDonell,L.M. and Boycott,K.M.
  TITLE     Microcephaly-Capillary Malformation Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24354023
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073046.7.
            
            On or before Apr 25, 2025 this sequence version replaced
            XP_047298928.1, XP_054196184.1.
            
            Summary: Cytokine-mediated signal transduction in the JAK-STAT
            cascade requires the involvement of adaptor molecules. One such
            signal-transducing adaptor molecule contains an SH3 domain that is
            required for induction of MYC and cell growth. The protein encoded
            by this gene binds to the SH3 domain of the signal-transducing
            adaptor molecule, and plays a critical role in cytokine-mediated
            signaling for MYC induction and cell cycle progression. Multiple
            alternatively spliced transcript variants encoding the same protein
            isoform have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.20918.1,
                                           SRR14038191.865607.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..336
                     /product="STAM-binding protein isoform 5"
                     /EC_number="3.1.2.15"
                     /note="associated molecule with the SH3 domain of STAM;
                     endosome-associated ubiquitin isopeptidase; testicular
                     secretory protein Li 54"
                     /calculated_mol_wt=38074
     Region          1..127
                     /region_name="Interaction with CHMP3.
                     /evidence=ECO:0000269|PubMed:17146056"
                     /note="propagated from UniProtKB/Swiss-Prot (O95630.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          13..117
                     /region_name="USP8_dimer"
                     /note="USP8 dimerization domain; pfam08969"
                     /db_xref="CDD:462647"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          227..231
                     /region_name="Interaction with STAM.
                     /evidence=ECO:0000269|PubMed:10383417"
                     /note="propagated from UniProtKB/Swiss-Prot (O95630.1)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          254..>335
                     /region_name="MPN"
                     /note="Mpr1p, Pad1p N-terminal (MPN) domains; cl13996"
                     /db_xref="CDD:472685"
     Site            280
                     /site_type="other"
                     /note="Indirect zinc-binding.
                     /evidence=ECO:0000250|UniProtKB:Q96FJ0; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     CDS             1..336
                     /gene="STAMBP"
                     /gene_synonym="AMSH; MICCAP"
                     /coded_by="NM_001438902.1:49..1059"
                     /note="isoform 5 is encoded by transcript variant 20"
                     /db_xref="GeneID:10617"
                     /db_xref="HGNC:HGNC:16950"
                     /db_xref="MIM:606247"
ORIGIN      
        1 msdhgdvslp pedrvralsq lgsavevned ipprryfrsg veiirmasiy seegniehaf
       61 ilynkyitlf ieklpkhrdy ksavipekkd tvkklkeiaf pkaeelkael lkrytkeyte
      121 yneekkkeae elarnmaiqq elekekqrva qqkqqqleqe qfhafeemir nqelekerlk
      181 ivqefgkvdp glggplvpdl ekpsldvfpt ltvssiqpsd chttvrpakp pvvdrslkpg
      241 alsnsesipt idglrhvvvp grlcpqflql asantargve tcgilcgklm rneftithvl
      301 ipkqsagsdy cnteneeelf liqdqqglit lgwiha
//
LOCUS       NP_001392787            1104 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001392787
VERSION     NP_001392787.1
DBSOURCE    REFSEQ: accession NM_001405858.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1104)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1104)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1104)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1104)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1104)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1104)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1104)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1104)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.723842.1,
                                           SRR14038194.1672863.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1104
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 2"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=120707
     Site            104
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          145..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          225..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          399..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          849..881
                     /region_name="Required for activation of KAT8 histone
                     acetyltransferase activity"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          884..1004
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     Region          909..927
                     /region_name="Interaction with KAT8 HAT domain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01397"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          937..1033
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            990
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            993
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            1002
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Site            1044
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     Region          1057..1104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3B3.3)"
     CDS             1..1104
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405858.1:391..3705"
                     /note="isoform 2 is encoded by transcript variant 9"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankgli
      481 vlgevpppeh ttdlflplss evktdhgtdk liesvsqple nhgapiighi seslstkscg
      541 alrpvngvin tlqpvladhi pgdssdaeeq lhkkqrlnlv ssssdgtcva artrpvlsck
      601 krrlvrpnsi vplskkvhrn stirpgcdvn pscalcgsgs intmppeihy eapllerlsq
      661 ldscvhpvla fpddvptslh fqsmlksqwq nkpfdkikpp kklslkhrap mpgslpdsar
      721 kdrhklvssf lttaklshhq trpdrthrqh lddvgavpmv ervtapkaer llnppppvhd
      781 pnhskmrlrd hssersevlk hhtdmssssy laathhpphs plvrqlstss dspapassss
      841 qvtastsqpv rrrrgessfd innivipmsv aattrveklq ykeiltpswr evdlqslkgs
      901 pdeeneeied lsdaafaalh akceemerar wlwttsvppq rrgsrsyrss dgrttpqlgs
      961 anpstpqpas pdvssshsls eyshgqsprs pispelhsap ltpvardtpr hlasedtrcs
     1021 tpelgldeqs vqpwerrtfp lahspqaece dqldaqeraa rctrrtsgsk tgreteaapt
     1081 sppivplksr hlvaaataqr pthr
//
LOCUS       NP_001400846             338 aa            linear   PRI 21-NOV-2025
DEFINITION  transcription factor ETV6 isoform 6 [Homo sapiens].
ACCESSION   NP_001400846
VERSION     NP_001400846.1
DBSOURCE    REFSEQ: accession NM_001413917.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Xu,W., Tian,F., Tai,X., Song,G., Liu,Y., Fan,L., Weng,X., Yang,E.,
            Wang,M., Bornhauser,M., Zhang,C., Lock,R.B., Wong,J.W.H., Wang,J.,
            Jing,D. and Mi,J.Q.
  TITLE     ETV6::ACSL6 translocation-driven super-enhancer activation leads to
            eosinophilia in acute lymphoblastic leukemia through IL-3
            overexpression
  JOURNAL   Haematologica 109 (8), 2445-2458 (2024)
   PUBMED   38356460
  REMARK    GeneRIF: ETV6::ACSL6 translocation-driven super-enhancer activation
            leads to eosinophilia in acute lymphoblastic leukemia through IL-3
            overexpression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Xue,S., Sun,H.P., Huang,X.B., Chen,X., Wang,T., Ma,W., Tian,Y.,
            Pan,Z.L., Li,L.H., Zhang,L., Liu,H.X. and Cao,X.Y.
  TITLE     Characteristics and literature review of ETV6::ABL1 fusion
            gene-positive acute myeloid leukemia
  JOURNAL   Int J Hematol 119 (5), 564-572 (2024)
   PUBMED   38441775
  REMARK    GeneRIF: Characteristics and literature review of ETV6::ABL1 fusion
            gene-positive acute myeloid leukemia.
            Review article
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Mueller,S.B., Pikman,Y., Tasian,S.K., Silverman,L.B., Harris,M.H.
            and Tsai,H.K.
  TITLE     ETV6 fusions from insertions of exons 3-5 in pediatric hematologic
            malignancies
  JOURNAL   Haematologica 108 (12), 3471-3476 (2023)
   PUBMED   37381775
  REMARK    GeneRIF: ETV6 fusions from insertions of exons 3-5 in pediatric
            hematologic malignancies.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Klubickova,N., Mosaieby,E., Ptakova,N., Trinquet,A., Lae,M.,
            Costes-Martineau,V. and Skalova,A.
  TITLE     High-grade non-intestinal type sinonasal adenocarcinoma with
            ETV6::NTRK3 fusion, distinct from secretory carcinoma by
            immunoprofile and morphology
  JOURNAL   Virchows Arch 483 (2), 187-195 (2023)
   PUBMED   37415052
  REMARK    GeneRIF: High-grade non-intestinal type sinonasal adenocarcinoma
            with ETV6::NTRK3 fusion, distinct from secretory carcinoma by
            immunoprofile and morphology.
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Romana,S.P., Mauchauffe,M., Le Coniat,M., Chumakov,I., Le
            Paslier,D., Berger,R. and Bernard,O.A.
  TITLE     The t(12;21) of acute lymphoblastic leukemia results in a tel-AML1
            gene fusion
  JOURNAL   Blood 85 (12), 3662-3670 (1995)
   PUBMED   7780150
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Golub,T.R., Barker,G.F., Bohlander,S.K., Hiebert,S.W., Ward,D.C.,
            Bray-Ward,P., Morgan,E., Raimondi,S.C., Rowley,J.D. and
            Gilliland,D.G.
  TITLE     Fusion of the TEL gene on 12p13 to the AML1 gene on 21q22 in acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 92 (11), 4917-4921 (1995)
   PUBMED   7761424
REFERENCE   8  (residues 1 to 338)
  AUTHORS   Buijs,A., Sherr,S., van Baal,S., van Bezouw,S., van der Plas,D.,
            Geurts van Kessel,A., Riegman,P., Lekanne Deprez,R., Zwarthoff,E.,
            Hagemeijer,A. et al.
  TITLE     Translocation (12;22) (p13;q11) in myeloproliferative disorders
            results in fusion of the ETS-like TEL gene on 12p13 to the MN1 gene
            on 22q11
  JOURNAL   Oncogene 10 (8), 1511-1519 (1995)
   PUBMED   7731705
  REMARK    Erratum:[Oncogene 1995 Aug 17;11(4):809]
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Pencheva,B., Di Paola,J. and Porter,C.C.
  TITLE     ETV6-Related Thrombocytopenia and Predisposition to Leukemia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   33226740
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Fainstein,E., Einat,M., Gokkel,E., Marcelle,C., Croce,C.M.,
            Gale,R.P. and Canaani,E.
  TITLE     Nucleotide sequence analysis of human abl and bcr-abl cDNAs
  JOURNAL   Oncogene 4 (12), 1477-1481 (1989)
   PUBMED   2687768
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007450.1, AC084430.13 and
            AC084358.19.
            
            Summary: This gene encodes an ETS family transcription factor. The
            product of this gene contains two functional domains: a N-terminal
            pointed (PNT) domain that is involved in protein-protein
            interactions with itself and other proteins, and a C-terminal
            DNA-binding domain. Gene knockout studies in mice suggest that it
            is required for hematopoiesis and maintenance of the developing
            vascular network. This gene is known to be involved in a large
            number of chromosomal rearrangements associated with leukemia and
            congenital fibrosarcoma. [provided by RefSeq, Sep 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: KU178050.1, SRR14372079.2441160.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..338
                     /product="transcription factor ETV6 isoform 6"
                     /note="ets variant gene 6 (TEL oncogene); TEL1 oncogene;
                     transcription factor ETV6; ETS-related protein Tel1;
                     ETV6-RUNX1 fusion protein"
                     /calculated_mol_wt=38719
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            11..12
                     /site_type="other"
                     /note="Breakpoint for translocation to form CHIC2-ETV6 in
                     AML; propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12435397,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            54..55
                     /site_type="other"
                     /note="Breakpoint for translocation to form ETV6-MDS2 in
                     MDS; propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            55..56
                     /site_type="other"
                     /note="Breakpoint for translocation to form PAX5-ETV6;
                     propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Region          56..123
                     /region_name="SAM_PNT-Tel_Yan"
                     /note="Sterile alpha motif (SAM)/Pointed domain of Tel/Yan
                     protein; cd08535"
                     /db_xref="CDD:176085"
     Site            order(63,85,88..90,92..93,96,98,100..101,104..105)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:176085"
     Site            order(75..80,107..109,111..112,115..116)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:176085"
     Region          158..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41212.1)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97360; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14.
                     /evidence=ECO:0000269|PubMed:12435397; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            302
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97360; propagated from
                     UniProtKB/Swiss-Prot (P41212.1)"
     CDS             1..338
                     /gene="ETV6"
                     /gene_synonym="TEL; TEL/ABL; THC5"
                     /coded_by="NM_001413917.1:455..1471"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:2120"
                     /db_xref="HGNC:HGNC:3495"
                     /db_xref="MIM:600618"
ORIGIN      
        1 msetpaqcsi kqerisytpp espvpsyass tplhvpvpra lrmeedsirl pahlrlqpiy
       61 wsrddvaqwl kwaenefslr pidsntfemn gkalllltke dfryrsphsg dvlyellqhi
      121 lkqrkprilf spffhpgnsi htqpevilhq nheedncvqr tprpsvdnvh hnpptiellh
      181 rsrspittnh rpspdpeqrp lrspldnmir rlspaeraqg prphqennhq esyplsvspm
      241 ennhcpasse shpkpssprq estrviqlmp spimhpliln prhsvdfkqs rlsedglhre
      301 gkpinlshre dlaymnhimv svsppeeham pigriagl
//
LOCUS       NP_001394739            1226 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 7 precursor
            [Homo sapiens].
ACCESSION   NP_001394739
VERSION     NP_001394739.1
DBSOURCE    REFSEQ: accession NM_001407810.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1226)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1226)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1226)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1226)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1226)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1226)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1226)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1226)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1226)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1226)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1378388.1,
                                           SRR14038191.3633110.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1226
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1226
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 7 precursor"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=134095
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O00411.2)"
                     /calculated_mol_wt=4109
     Region          18..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          95..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          261..290
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          296..323
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          428..700
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          727..746
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          798..1226
                     /region_name="Mediates interaction with TEFM.
                     /evidence=ECO:0000269|PubMed:21278163"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          827..1226
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1226
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407810.1:26..3706"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 msalcwgrga aglkralrpc grpglpgkeg taggvcgprr sssaspqeqd qdrrkdwghv
       61 ellevlqarv rqlqaesvse vvvnrvdvar lpecgsgdgs lqpprkvqmg akdatpvpcg
      121 rwakilekdk rtqqmrmqrl kaklqmpfqs gefkaltrrl qveprllskq magcledctr
      181 qapespweeq larllqeapg klsldveqap sgqhsqaqls gqqqrllaff kcclltdqlp
      241 lahhllvvhh gqrqkrkllt ldmynavmlg warqgafkel vyvlfmvkda gltpdllsya
      301 aalqcmgrqd qdagtiercl eqmsqeglkl qalftavlls eedratvlka vhkvkptfsl
      361 ppqlpppvnt skllrdvyak dgrvsypklh lplktlqclf ekqlhmelas rvcvvsvekp
      421 tlpskerktl ktlrdqweka lcralretkn rlerevyegr fslypflcll derevvrmll
      481 qvlqalpaqg esfttlarel sartfsrhvv qrqrvsgqvq alqnhyrkyl cllasdaevp
      541 epclprqywe elgapealre qpwplpvqme lgkllaemlv qatqmpcsld kphrssrlvp
      601 vlyhvysfrn vqqigilkph payvqlleka aeptltfeav dvpmlcpplp wtsphsgafl
      661 lsptklmrtv egatqhqell etcpptalhg aldaltqlgn cawrvngrvl dlvlqlfqak
      721 gcpqlgvpap pseapqppea hlphsaapar kaelrrelah cqkvaremhs lraealyrls
      781 laqhlrdrvf wlphnmdfrg rtypcpphfn hlgsdvaral lefaqgrplg phgldwlkih
      841 lvnltglkkr eplrkrlafa eevmddilds adqpltgrkw wmgaeepwqt laccmevana
      901 vrasdpaayv shlpvhqdgs cnglqhyaal grdsvgaasv nlepsdvpqd vysgvaaqve
      961 vfrrqdaqrg mrvaqvlegf itrkvvkqtv mtvvygvtry ggrlqiekrl relsdfpqef
     1021 vweashylvr qvfkslqemf sgtraiqhwl tesarlishm gsvvewvtpl gvpviqpyrl
     1081 dskvkqiggg iqsitythng disrkpntrk qkngfppnfi hsldsshmml talhcyrkgl
     1141 tfvsvhdcyw thaadvsvmn qvcreqfvrl hsepilqdls rflvkrfcse pqkileasql
     1201 ketlqavpkp gafdleqvkr styffs
//
LOCUS       NP_001428221             651 aa            linear   PRI 21-NOV-2025
DEFINITION  dynamin-binding protein isoform g [Homo sapiens].
ACCESSION   NP_001428221
VERSION     NP_001428221.1
DBSOURCE    REFSEQ: accession NM_001441292.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 651)
  AUTHORS   Ouyang,C., Mu,J., Lu,Q., Li,J., Zhu,H., Wang,Q., Zou,M.H. and
            Xie,Z.
  TITLE     Autophagic degradation of KAT2A/GCN5 promotes directional migration
            of vascular smooth muscle cells by reducing TUBA/alpha-tubulin
            acetylation
  JOURNAL   Autophagy 16 (10), 1753-1770 (2020)
   PUBMED   31878840
  REMARK    GeneRIF: Autophagic degradation of KAT2A/GCN5 promotes directional
            migration of vascular smooth muscle cells by reducing
            TUBA/alpha-tubulin acetylation.
REFERENCE   5  (residues 1 to 651)
  AUTHORS   Ansar,M., Chung,H.L., Taylor,R.L., Nazir,A., Imtiaz,S.,
            Sarwar,M.T., Manousopoulou,A., Makrythanasis,P., Saeed,S.,
            Falconnet,E., Guipponi,M., Pournaras,C.J., Ansari,M.A., Ranza,E.,
            Santoni,F.A., Ahmed,J., Shah,I., Gul,K., Black,G.C., Bellen,H.J.
            and Antonarakis,S.E.
  TITLE     Bi-allelic Loss-of-Function Variants in DNMBP Cause Infantile
            Cataracts
  JOURNAL   Am J Hum Genet 103 (4), 568-578 (2018)
   PUBMED   30290152
  REMARK    GeneRIF: DNMBP loss-of-function variants cause infantile-onset
            cataracts in humans.
REFERENCE   6  (residues 1 to 651)
  AUTHORS   Minster,R.L., DeKosky,S.T. and Kamboh,M.I.
  TITLE     No association of dynamin binding protein (DNMBP) gene SNPs and
            Alzheimer's disease
  JOURNAL   Neurobiol Aging 29 (10), 1602-1604 (2008)
   PUBMED   17442457
  REMARK    GeneRIF: We observed no association of statistical significance in
            either the total sample or the APOE*4 non-carriers for any of the
            SNPs of Dynamin Binding Protein.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 651)
  AUTHORS   Otani,T., Ichii,T., Aono,S. and Takeichi,M.
  TITLE     Cdc42 GEF Tuba regulates the junctional configuration of simple
            epithelial cells
  JOURNAL   J Cell Biol 175 (1), 135-146 (2006)
   PUBMED   17015620
  REMARK    GeneRIF: Tuba controls the shaping of cell junctions through the
            local activation of Cdc42 and its effectors.
REFERENCE   8  (residues 1 to 651)
  AUTHORS   Kuwano,R., Miyashita,A., Arai,H., Asada,T., Imagawa,M., Shoji,M.,
            Higuchi,S., Urakami,K., Kakita,A., Takahashi,H., Tsukie,T.,
            Toyabe,S., Akazawa,K., Kanazawa,I. and Ihara,Y.
  CONSRTM   Japanese Genetic Study Consortium for Alzeheimer's Disease
  TITLE     Dynamin-binding protein gene on chromosome 10q is associated with
            late-onset Alzheimer's disease
  JOURNAL   Hum Mol Genet 15 (13), 2170-2182 (2006)
   PUBMED   16740596
  REMARK    GeneRIF: Results confirmed DNMBP may be one of the susceptibility
            genes for Alzheimer's disease.
            GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   9  (residues 1 to 651)
  AUTHORS   Cestra,G., Kwiatkowski,A., Salazar,M., Gertler,F. and De Camilli,P.
  TITLE     Tuba, a GEF for CDC42, links dynamin to actin regulatory proteins
  JOURNAL   Methods Enzymol 404, 537-545 (2005)
   PUBMED   16413298
REFERENCE   10 (residues 1 to 651)
  AUTHORS   Salazar,M.A., Kwiatkowski,A.V., Pellegrini,L., Cestra,G.,
            Butler,M.H., Rossman,K.L., Serna,D.M., Sondek,J., Gertler,F.B. and
            De Camilli,P.
  TITLE     Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl
            homology domains, links dynamin to regulation of the actin
            cytoskeleton
  JOURNAL   J Biol Chem 278 (49), 49031-49043 (2003)
   PUBMED   14506234
  REMARK    GeneRIF: functions to bring together dynamin with actin regulatory
            proteins
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL627434.4 and AL392107.17.
            
            Summary: This gene encodes a protein belonging to the guanine
            nucleotide exchange factor family, and which regulates the
            configuration of cell junctions. It contains multiple binding sites
            for dynamin and thus links dynamin to actin regulatory proteins.
            Polymorphisms in this gene have been linked to Alzheimer's disease
            in some populations, though there are conflicting reports of such
            linkages in other populations. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2346698.1,
                                           SRR18074967.2716997.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.2"
     Protein         1..651
                     /product="dynamin-binding protein isoform g"
                     /note="scaffold protein TUBA"
                     /calculated_mol_wt=73808
     Region          <1..39
                     /region_name="RhoGEF"
                     /note="RhoGEF domain; pfam00621"
                     /db_xref="CDD:459876"
     Region          91..282
                     /region_name="BAR_DNMBP"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin
                     Binding Protein; cd07589"
                     /db_xref="CDD:153273"
     Site            order(103,106..107,111,113..114,117..118,120..121,
                     135..136,138..139,142..143,145..146,149,155,158..159,243,
                     246..247,249,254,257..258,260..261,264..265,268..269,
                     271..272,275..276,278..279)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153273"
     Region          363..419
                     /region_name="SH3_DNMBP_C1"
                     /note="First C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11798"
                     /db_xref="CDD:212732"
     Site            order(368,370,373,377,399..400,413,415..416)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212732"
     Region          591..647
                     /region_name="SH3_DNMBP_C2"
                     /note="Second C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba, and similar domains;
                     cd12141"
                     /db_xref="CDD:213017"
     Site            order(596,598,601,605,627..628,641,643..644)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213017"
     CDS             1..651
                     /gene="DNMBP"
                     /gene_synonym="ARHGEF36; CTRCT48; TUBA"
                     /coded_by="NM_001441292.1:503..2458"
                     /note="isoform g is encoded by transcript variant 8"
                     /db_xref="GeneID:23268"
                     /db_xref="HGNC:HGNC:30373"
                     /db_xref="MIM:611282"
ORIGIN      
        1 mryplllmel lnstpeshpd kvpltnavla vkeinvnine ykrrkdlvlk yrkgdedslm
       61 ekisklnihs iikksnrvss hlkhltgfap qikdevfeet eknfrmqerl iksfirdlsl
      121 ylqhiresac vkvvaavsmw dvcmerghrd leqfervhry isdqlftnfk erterlvisp
      181 lnqllsmftg phklvqkrfd klldfyncte raeklkdkkt leelqsarnn yealnaqlld
      241 elpkfhqyaq glftncvhgy aeahcdfvhq aleqlkplls llkvagregn liaifheehs
      301 rvlqqlqvft ffpeslpatk kpferktidr qsarkpllgl psymlqseel rasllarypp
      361 eklfqaernf naaqdldvsl legdlvgvik kkdpmgsqnr wlidngvtkg fvyssflkpy
      421 nprrshsdas vgshsstese hgsssprfpr qnsgstltfn pssmavsfts gscqkqpqda
      481 spppkecdqg tlsaslnpsn sesspsrcps dpdstsqprs gdsadvardv kqptatprsy
      541 rnfrhpeivg ysvpgrngqs qdlvkgcart aqapedrste pdgseaegnq vyfavytfka
      601 rnpnelsvsa nqklkilefk dvtgntewwl aevngkkgyv psnyirktey t
//
LOCUS       NP_001393554            1028 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 13 [Homo sapiens].
ACCESSION   NP_001393554
VERSION     NP_001393554.1
DBSOURCE    REFSEQ: accession NM_001406625.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1028)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1028)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1028)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1028)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1028)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1028)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1028)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.774912.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1028
                     /product="hamartin isoform 13"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=114507
     Region          16..597
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <583..>820
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1028
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406625.1:448..3534"
                     /note="isoform 13 is encoded by transcript variant 39"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mdtdvvvltt gvlvlitmlp mipqsgkqhl ldffdifgrl sswclkkpgh vaevylvhlh
       61 asvyalfhrl ygmypcnfvs flrshysmke nletfeevvk pmmehvrihp elvtgskdhe
      121 ldprrwkrle thdvviecak isldpteasy edgysvshqi sarfphrsad vttspyadtq
      181 nsygcatstp ystsrlmlln mpgqlpqtls spstrlitep pqatlwspsm vcgmttppts
      241 pgnvppdlsh pyskvfgttg gkgtplgtpa tspppaplch sddyvhislp qatvtpprke
      301 ermdsarpcl hrqhhllndr gseeppgskg svtlsdlpgf lgdlaseeds iekdkeeaai
      361 srelseitta eaepvvprgg fdspfyrdsl pgsqrkthsa asssqgasvn peplhssldk
      421 lgpdtpkqaf tpidlpcgsa despagdrec qtsletsift pspckipppt rvgfgsgqpp
      481 pydhlfeval pktahhfvir kteellkkak gnteedgvps tspmevldrl iqqgadahsk
      541 elnklplpsk svdwthfggs ppsdeirtlr dqllllhnql lyerfkrqqh alrnrrllrk
      601 vikaaaleeh naamkdqlkl qekdiqmwkv slqkeqaryn qlqeqrdtmv tklhsqirql
      661 qhdreefynq sqelqtkled crnmiaelri elkkannkls nsesvqqqme flnrqllvlg
      721 evnelyleql qnkhsdttke vemmkaayrk eleknrshvl qqtqrldtsq krileleshl
      781 akkdhllleq kkyledvklq argqlqaaes ryeaqkritq vfeleildly grlekdgllk
      841 kleeekaeaa eaaeerldcc ndgcsdsmvg hneeasghng etktprpssa rgssgsrggg
      901 gssssssels tpekpphqra gpfssrwett mgeasasipt tvgslpssks flgmkarelf
      961 rnksesqcde dgmtsslses lktelgkdlg veakiplnld gphpspptpd svgqlhimdy
     1021 nethhehs
//
LOCUS       NP_001402871             419 aa            linear   PRI 21-NOV-2025
DEFINITION  synaptotagmin-1 isoform 2 [Homo sapiens].
ACCESSION   NP_001402871 XP_006719639
VERSION     NP_001402871.1
DBSOURCE    REFSEQ: accession NM_001415942.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Stephan,G., Haddock,S., Wang,S., Erdjument-Bromage,H., Liu,W.,
            Ravn-Boess,N., Frenster,J.D., Bready,D., Cai,J., Ronnen,R.,
            Sabio-Ortiz,J., Fenyo,D., Neubert,T.A. and Placantonakis,D.G.
  TITLE     Modulation of GPR133 (ADGRD1) signaling by its intracellular
            interaction partner extended synaptotagmin 1
  JOURNAL   Cell Rep 43 (5), 114229 (2024)
   PUBMED   38758649
  REMARK    GeneRIF: Modulation of GPR133 (ADGRD1) signaling by its
            intracellular interaction partner extended synaptotagmin 1.
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Zhang,J., Ren,G., Huang,T., Sang,Y., Zhong,Y. and Yi,Y.
  TITLE     miRNA-363-3p Hinders Proliferation, Migration, Invasion and
            Autophagy of Thyroid Cancer Cells by Controlling SYT1 Transcription
            to affect NF-kappaB
  JOURNAL   Endocr Metab Immune Disord Drug Targets 24 (1), 153-162 (2024)
   PUBMED   37150983
  REMARK    GeneRIF: miRNA-363-3p Hinders Proliferation, Migration, Invasion
            and Autophagy of Thyroid Cancer Cells by Controlling SYT1
            Transcription to affect NF-kappaB.
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Yamada,K., Motohashi,S., Oikawa,T., Tago,N., Koizumi,R., Ono,M.,
            Tachibana,T., Yoshida,A., Yoshida,S., Shimoda,M., Oka,M., Yoneda,Y.
            and Yoshida,K.
  TITLE     Extended-synaptotagmin 1 engages in unconventional protein
            secretion mediated via SEC22B+ vesicle pathway in liver cancer
  JOURNAL   Proc Natl Acad Sci U S A 119 (36), e2202730119 (2022)
   PUBMED   36044553
  REMARK    GeneRIF: Extended-synaptotagmin 1 engages in unconventional protein
            secretion mediated via SEC22B(+) vesicle pathway in liver cancer.
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Thibord,F., Chan,M.V., Chen,M.H. and Johnson,A.D.
  TITLE     A year of COVID-19 GWAS results from the GRASP portal reveals
            potential genetic risk factors
  JOURNAL   HGG Adv 3 (2), 100095 (2022)
   PUBMED   35224516
REFERENCE   6  (residues 1 to 419)
  AUTHORS   McMahon,H.T., Missler,M., Li,C. and Sudhof,T.C.
  TITLE     Complexins: cytosolic proteins that regulate SNAP receptor function
  JOURNAL   Cell 83 (1), 111-119 (1995)
   PUBMED   7553862
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Chowdhury,D., Travis,G.H., Sutcliffe,J.G. and Burton,F.H.
  TITLE     Synaptotagmin I and 1B4 are identical: implications for
            synaptotagmin distribution in the primate brain
  JOURNAL   Neurosci Lett 190 (1), 9-12 (1995)
   PUBMED   7624059
REFERENCE   8  (residues 1 to 419)
  AUTHORS   Mochly-Rosen,D., Miller,K.G., Scheller,R.H., Khaner,H., Lopez,J.
            and Smith,B.L.
  TITLE     p65 fragments, homologous to the C2 region of protein kinase C,
            bind to the intracellular receptors for protein kinase C
  JOURNAL   Biochemistry 31 (35), 8120-8124 (1992)
   PUBMED   1326322
REFERENCE   9  (residues 1 to 419)
  AUTHORS   Perin,M.S., Johnston,P.A., Ozcelik,T., Jahn,R., Francke,U. and
            Sudhof,T.C.
  TITLE     Structural and functional conservation of synaptotagmin (p65) in
            Drosophila and humans
  JOURNAL   J Biol Chem 266 (1), 615-622 (1991)
   PUBMED   1840599
REFERENCE   10 (residues 1 to 419)
  AUTHORS   Blaustein,R.O., Germann,W.J., Finkelstein,A. and DasGupta,B.R.
  TITLE     The N-terminal half of the heavy chain of botulinum type A
            neurotoxin forms channels in planar phospholipid bilayers
  JOURNAL   FEBS Lett 226 (1), 115-120 (1987)
   PUBMED   2446925
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073616.17, AC073572.19,
            AC078917.14 and AC027288.26.
            
            On Jan 5, 2023 this sequence version replaced XP_006719639.1.
            
            Summary: This gene encodes a member of the synaptotagmin protein
            family. The synaptotagmins are integral membrane proteins of
            synaptic vesicles that serve as calcium sensors in the process of
            vesicular trafficking and exocytosis. The encoded protein
            participates in triggering neurotransmitter release at the synapse
            in response to calcium binding. Mutations in this gene are
            associated with Baker-Gordon syndrome. [provided by RefSeq, Jan
            2023].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.161024.1,
                                           SRR1803611.272201.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.2"
     Protein         1..419
                     /product="synaptotagmin-1 isoform 2"
                     /note="sytI; synaptotagmin I"
                     /calculated_mol_wt=47130
     Region          6..113
                     /region_name="Syt1_N"
                     /note="N-terminal domain of synaptotagmin-1 (Syt1) and
                     similar proteins; cd21963"
                     /db_xref="CDD:409248"
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            order(40,43..44,46..48,50..51)
                     /site_type="other"
                     /note="Botolinum neurotoxin B binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409248"
     Site            58..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Region          133..379
                     /region_name="Phospholipid binding. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Region          140..262
                     /region_name="C2A_Synaptotagmin-1-5-6-9-10"
                     /note="C2A domain first repeat present in Synaptotagmins
                     1, 5, 6, 9, and 10; cd08385"
                     /db_xref="CDD:176031"
     Site            order(170,176,228,230,236)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176031"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P46096; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46096; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Region          271..406
                     /region_name="C2B_Synaptotagmin-1"
                     /note="C2 domain second repeat present in Synaptotagmin 1;
                     cd08402"
                     /db_xref="CDD:176047"
     Site            order(301,307,361,363,369)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176047"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21707; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21707; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     CDS             1..419
                     /gene="SYT1"
                     /gene_synonym="BAGOS; P65; SVP65; SYT"
                     /coded_by="NM_001415942.1:219..1478"
                     /note="isoform 2 is encoded by transcript variant 9"
                     /db_xref="GeneID:6857"
                     /db_xref="HGNC:HGNC:11509"
                     /db_xref="MIM:185605"
ORIGIN      
        1 mvseshheal aappvttvat vlpsnatepa spgegkedaf sklkekfmne lhkiplppwa
       61 liaiaivavl lvltccfcic kkclfkkknk kkgkekggkn ainmkdvkdl gktmkdqddd
      121 aetgltdgee keepkeeekl gklqysldyd fqnnqllvgi iqaaelpald mggtsdpyvk
      181 vfllpdkkkk fetkvhrktl npvfneqftf kvpyselggk tlvmavydfd rfskhdiige
      241 fkvpmntvdf ghvteewrdl qsaekeeqek lgdicfslry vptagkltvv ileaknlkkm
      301 dvgglsdpyv kihlmqngkr lkkkkttikk ntlnpyynes fsfevpfeqi qkvqvvvtvl
      361 dydkigknda igkvfvgyns tgaelrhwsd mlanprrpia qwhtlqveee vdamlavkk
//
LOCUS       NP_001393925             478 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform K [Homo sapiens].
ACCESSION   NP_001393925
VERSION     NP_001393925.1
DBSOURCE    REFSEQ: accession NM_001406996.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 478)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 478)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: M13452.1, SRR14038195.2062896.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968968, SAMEA2148874 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..478
                     /product="lamin isoform K"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=53246
     Region          <1..200
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          248..355
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     CDS             1..478
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406996.1:471..1907"
                     /note="isoform K is encoded by transcript variant 21"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 mlrrvdaenr lqtmkeeldf qkniyseelr etkrrhetrl veidngkqre fesrladalq
       61 elraqhedqv eqykkelekt ysakldnarq saernsnlvg aaheelqqsr iridslsaql
      121 sqlqkqlaak eaklrdleds larerdtsrr llaekerema emrarmqqql deyqelldik
      181 laldmeihay rkllegeeer lrlspsptsq rsrgrasshs sqtqgggsvt kkrklestes
      241 rssfsqhart sgrvaveevd eegkfvrlrn ksnedqsmgn wqikrqngdd plltyrfppk
      301 ftlkagqvvt iwaagagath spptdlvwka qntwgcgnsl rtalinstge evamrklvrs
      361 vtvveddede dgddllhhhh gshcsssgdp aeynlrsrtv lcgtcgqpad kasasgsgaq
      421 vggpissgss assvtvtrsy rsvggsgggs fgdnlvtrsy llgnssprtq spqncsim
//
LOCUS       NP_001036064            1292 aa            linear   PRI 21-NOV-2025
DEFINITION  receptor tyrosine-protein kinase erbB-4 isoform JM-a/CYT-2
            precursor [Homo sapiens].
ACCESSION   NP_001036064
VERSION     NP_001036064.1
DBSOURCE    REFSEQ: accession NM_001042599.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1292)
  AUTHORS   Li,X., Zhang,H., Li,W., Tuo,H., He,B. and Jiang,H.
  TITLE     The role and mechanism of NRG1/ErbB4 in inducing the
            differentiation of induced pluripotent stem cells into
            cardiomyocytes
  JOURNAL   BMC Cardiovasc Disord 24 (1), 559 (2024)
   PUBMED   39407109
  REMARK    GeneRIF: The role and mechanism of NRG1/ErbB4 in inducing the
            differentiation of induced pluripotent stem cells into
            cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1292)
  AUTHORS   Singh,P.K., Kim,S. and Smith,A.W.
  TITLE     HER4 is a high-affinity dimerization partner for all EGFR/HER/ErbB
            family proteins
  JOURNAL   Protein Sci 33 (10), e5171 (2024)
   PUBMED   39276020
  REMARK    GeneRIF: HER4 is a high-affinity dimerization partner for all
            EGFR/HER/ErbB family proteins.
REFERENCE   3  (residues 1 to 1292)
  AUTHORS   Adashek,J.J., Pandya,C., Maragakis,N.J., De,P., Cohen,P.R., Kato,S.
            and Kurzrock,R.
  TITLE     Neuregulin-1 and ALS19 (ERBB4): at the crossroads of amyotrophic
            lateral sclerosis and cancer
  JOURNAL   BMC Med 22 (1), 74 (2024)
   PUBMED   38369520
  REMARK    GeneRIF: Neuregulin-1 and ALS19 (ERBB4): at the crossroads of
            amyotrophic lateral sclerosis and cancer.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1292)
  AUTHORS   Li,R., Wang,Y., Yang,L., Zhong,P., Huang,G., Liang,Q. and Yu,X.
  TITLE     Genetic variants of ERBB4 gene and risk of gestational diabetes
            mellitus: a susceptibility and diagnostic nomogram study
  JOURNAL   Front Endocrinol (Lausanne) 14, 1283539 (2023)
   PUBMED   38149095
  REMARK    GeneRIF: Genetic variants of ERBB4 gene and risk of gestational
            diabetes mellitus: a susceptibility and diagnostic nomogram study.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1292)
  AUTHORS   Tang,R., Cui,H., Dou,R., Tao,L., Tan,L., Guo,T. and Luo,D.
  TITLE     ErbB4 affects Th1/Th17 cell differentiation and promotes psoriasis
            progression
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (12), 1-5 (2023)
   PUBMED   38063127
  REMARK    GeneRIF: ErbB4 affects Th1/Th17 cell differentiation and promotes
            psoriasis progression.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1292)
  AUTHORS   Barbacci,E.G., Guarino,B.C., Stroh,J.G., Singleton,D.H.,
            Rosnack,K.J., Moyer,J.D. and Andrews,G.C.
  TITLE     The structural basis for the specificity of epidermal growth factor
            and heregulin binding
  JOURNAL   J Biol Chem 270 (16), 9585-9589 (1995)
   PUBMED   7721889
  REMARK    Erratum:[J Biol Chem 1995 Nov 24;270(47):28494]
REFERENCE   7  (residues 1 to 1292)
  AUTHORS   Zimonjic,D.B., Alimandi,M., Miki,T., Popescu,N.C. and Kraus,M.H.
  TITLE     Localization of the human HER4/erbB-4 gene to chromosome 2
  JOURNAL   Oncogene 10 (6), 1235-1237 (1995)
   PUBMED   7700649
REFERENCE   8  (residues 1 to 1292)
  AUTHORS   Nagata,K., Kohda,D., Hatanaka,H., Ichikawa,S., Matsuda,S.,
            Yamamoto,T., Suzuki,A. and Inagaki,F.
  TITLE     Solution structure of the epidermal growth factor-like domain of
            heregulin-alpha, a ligand for p180erbB-4
  JOURNAL   EMBO J 13 (15), 3517-3523 (1994)
   PUBMED   8062828
REFERENCE   9  (residues 1 to 1292)
  AUTHORS   Culouscou,J.M., Plowman,G.D., Carlton,G.W., Green,J.M. and
            Shoyab,M.
  TITLE     Characterization of a breast cancer cell differentiation factor
            that specifically activates the HER4/p180erbB4 receptor
  JOURNAL   J Biol Chem 268 (25), 18407-18410 (1993)
   PUBMED   7689552
REFERENCE   10 (residues 1 to 1292)
  AUTHORS   Siddique,N. and Siddique,T.
  TITLE     Amyotrophic Lateral Sclerosis Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC096765.3, AC096547.1,
            AC093823.2, AC105921.5, AC068970.6 and AC012069.10.
            
            Summary: This gene is a member of the Tyr protein kinase family and
            the epidermal growth factor receptor subfamily. It encodes a
            single-pass type I membrane protein with multiple cysteine rich
            domains, a transmembrane domain, a tyrosine kinase domain, a
            phosphotidylinositol-3 kinase binding site and a PDZ domain binding
            motif. The protein binds to and is activated by neuregulins and
            other factors and induces a variety of cellular responses including
            mitogenesis and differentiation. Multiple proteolytic events allow
            for the release of a cytoplasmic fragment and an extracellular
            fragment. Mutations in this gene have been associated with cancer.
            Alternatively spliced variants which encode different protein
            isoforms have been described; however, not all variants have been
            fully characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (JM-a/CYT-2) lacks an alternate
            in-frame exon, compared to variant JM-a/CYT-1, resulting in a
            shorter protein (isoform JM-a/CYT-2) that lacks the
            phosphotidylinositol-3 kinase binding site, compared to isoform
            JM-a/CYT-1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143741.1, SRR14038196.2667171.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..1292
                     /product="receptor tyrosine-protein kinase erbB-4 isoform
                     JM-a/CYT-2 precursor"
                     /EC_number="2.7.10.1"
                     /note="receptor tyrosine-protein kinase erbB-4; tyrosine
                     kinase-type cell surface receptor HER4; avian
                     erythroblastic leukemia viral (v-erb-b2) oncogene homolog
                     4; proto-oncogene-like protein c-ErbB-4; v-erb-a
                     erythroblastic leukemia viral oncogene homolog 4; v-erb-b2
                     avian erythroblastic leukemia viral oncogene homolog 4;
                     human epidermal growth factor receptor 4"
                     /calculated_mol_wt=142892
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2325
     mat_peptide     26..1292
                     /product="receptor tyrosine-protein kinase erbB-4 isoform
                     JM-a/CYT-2"
                     /calculated_mol_wt=142603
     Region          26..651
                     /region_name="extracellular domain"
     Region          55..167
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16203964; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            174
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16203964; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Region          186..332
                     /region_name="Furin-like"
                     /note="Furin-like cysteine rich region; pfam00757"
                     /db_xref="CDD:395614"
     Site            253
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16203964; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Region          358..478
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Site            358
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16203964; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            410
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16203964; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            473
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16203964; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            495
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16203964; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Region          502..634
                     /region_name="GF_recep_IV"
                     /note="Growth factor receptor domain IV; pfam14843"
                     /db_xref="CDD:464344"
     Site            548
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            576
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16203964; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            620
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Region          642..685
                     /region_name="TM_ErbB4"
                     /note="Transmembrane domain of ErbB4, a Protein Tyrosine
                     Kinase; cd12092"
                     /db_xref="CDD:213053"
     Site            order(642..643,645..648,651..652,655..656,659..660,
                     663..664,667,671)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:213053"
     Site            652..675
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15303.1)"
     Region          676..1292
                     /region_name="cytoplasmic domain"
     Region          710..1012
                     /region_name="PTKc_HER4"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     HER4; cd05110"
                     /db_xref="CDD:173655"
     Site            order(724..725,732,749,751,772,794,796..797,799,847..848,
                     850,861,882..886,891,895)
                     /site_type="active"
                     /db_xref="CDD:173655"
     Site            order(724..725,732,749,751,772,794,796..797,799,847..848,
                     850,861)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173655"
     Site            860..885
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173655"
     Site            875
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            order(882..886,891,895)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173655"
     Site            1035
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            1134
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            1146
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            1172
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752,
                     ECO:0000269|PubMed:8617750; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            1186
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            1226
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752,
                     ECO:0000269|PubMed:8617750; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            1242
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     Site            1268
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:18721752; propagated from
                     UniProtKB/Swiss-Prot (Q15303.1)"
     CDS             1..1292
                     /gene="ERBB4"
                     /gene_synonym="ALS19; HER4; p180erbB4"
                     /coded_by="NM_001042599.2:273..4151"
                     /note="isoform JM-a/CYT-2 precursor is encoded by
                     transcript variant JM-a/CYT-2"
                     /db_xref="CCDS:CCDS42811.1"
                     /db_xref="GeneID:2066"
                     /db_xref="HGNC:HGNC:3432"
                     /db_xref="MIM:600543"
ORIGIN      
        1 mkpatglwvw vsllvaagtv qpsdsqsvca gtenklssls dleqqyralr kyyencevvm
       61 gnleitsieh nrdlsflrsv revtgyvlva lnqfrylple nlriirgtkl yedryalaif
      121 lnyrkdgnfg lqelglknlt eilnggvyvd qnkflcyadt ihwqdivrnp wpsnltlvst
      181 ngssgcgrch ksctgrcwgp tenhcqtltr tvcaeqcdgr cygpyvsdcc hrecaggcsg
      241 pkdtdcfacm nfndsgacvt qcpqtfvynp ttfqlehnfn akytygafcv kkcphnfvvd
      301 ssscvracps skmeveengi kmckpctdic pkacdgigtg slmsaqtvds snidkfinct
      361 kingnliflv tgihgdpyna ieaidpekln vfrtvreitg flniqswppn mtdfsvfsnl
      421 vtiggrvlys glsllilkqq gitslqfqsl keisagniyi tdnsnlcyyh tinwttlfst
      481 inqrivirdn rkaenctaeg mvcnhlcssd gcwgpgpdqc lscrrfsrgr iciescnlyd
      541 gefrefengs icvecdpqce kmedglltch gpgpdnctkc shfkdgpncv ekcpdglqga
      601 nsfifkyadp drechpchpn ctqgcngpts hdciyypwtg hstlpqhart pliaagvigg
      661 lfilvivglt favyvrrksi kkkralrrfl etelvepltp sgtapnqaql rilketelkr
      721 vkvlgsgafg tvykgiwvpe getvkipvai kilnettgpk anvefmdeal imasmdhphl
      781 vrllgvclsp tiqlvtqlmp hgclleyvhe hkdnigsqll lnwcvqiakg mmyleerrlv
      841 hrdlaarnvl vkspnhvkit dfglarlleg dekeynadgg kmpikwmale cihyrkfthq
      901 sdvwsygvti welmtfggkp ydgiptreip dllekgerlp qppictidvy mvmvkcwmid
      961 adsrpkfkel aaefsrmard pqrylviqgd drmklpspnd skffqnllde edledmmdae
     1021 eylvpqafni pppiytsrar idsnrnqfvy rdggfaaeqg vsvpyrapts tipeapvaqg
     1081 ataeifddsc cngtlrkpva phvqedsstq rysadptvfa persprgeld eegymtpmrd
     1141 kpkqeylnpv eenpfvsrrk ngdlqaldnp eyhnasngpp kaedeyvnep lylntfantl
     1201 gkaeylknni lsmpekakka fdnpdywnhs lpprstlqhp dylqeystky fykqngrirp
     1261 ivaenpeyls efslkpgtvl ppppyrhrnt vv
//
LOCUS       NP_001412005             488 aa            linear   PRI 21-NOV-2025
DEFINITION  coatomer subunit delta isoform 6 [Homo sapiens].
ACCESSION   NP_001412005
VERSION     NP_001412005.1
DBSOURCE    REFSEQ: accession NM_001425076.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   O'Donoghue,L., Comer,S.P., Hiebner,D.W., Schoen,I., von
            Kriegsheim,A. and Smolenski,A.
  TITLE     RhoGAP6 interacts with COPI to regulate protein transport
  JOURNAL   Biochem J 480 (14), 1109-1127 (2023)
   PUBMED   37409526
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Li,W., Liang,J., Outeda,P., Turner,S., Wakimoto,B.T. and Watnick,T.
  TITLE     A genetic screen in Drosophila reveals an unexpected role for the
            KIP1 ubiquitination-promoting complex in male fertility
  JOURNAL   PLoS Genet 16 (12), e1009217 (2020)
   PUBMED   33378371
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Tidwell,T., Deshotel,M., Palumbos,J., Miller,C., Bayrak-Toydemir,P.
            and Carey,J.C.
  TITLE     Novel de novo ARCN1 intronic variant causes rhizomelic short
            stature with microretrognathia and developmental delay
  JOURNAL   Cold Spring Harb Mol Case Stud 6 (6), a005728 (2020)
   PUBMED   33154040
  REMARK    GeneRIF: Novel de novo ARCN1 intronic variant causes rhizomelic
            short stature with microretrognathia and developmental delay.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 488)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 488)
  AUTHORS   Schekman,R. and Orci,L.
  TITLE     Coat proteins and vesicle budding
  JOURNAL   Science 271 (5255), 1526-1533 (1996)
   PUBMED   8599108
  REMARK    Review article
REFERENCE   7  (residues 1 to 488)
  AUTHORS   Cukierman,E., Huber,I., Rotman,M. and Cassel,D.
  TITLE     The ARF1 GTPase-activating protein: zinc finger motif and Golgi
            complex localization
  JOURNAL   Science 270 (5244), 1999-2002 (1995)
   PUBMED   8533093
REFERENCE   8  (residues 1 to 488)
  AUTHORS   Radice,P., Pensotti,V., Jones,C., Perry,H., Pierotti,M.A. and
            Tunnacliffe,A.
  TITLE     The human archain gene, ARCN1, has highly conserved homologs in
            rice and Drosophila
  JOURNAL   Genomics 26 (1), 101-106 (1995)
   PUBMED   7782067
REFERENCE   9  (residues 1 to 488)
  AUTHORS   Orcl,L., Palmer,D.J., Amherdt,M. and Rothman,J.E.
  TITLE     Coated vesicle assembly in the Golgi requires only coatomer and ARF
            proteins from the cytosol
  JOURNAL   Nature 364 (6439), 732-734 (1993)
   PUBMED   8355790
REFERENCE   10 (residues 1 to 488)
  AUTHORS   Waters,M.G., Serafini,T. and Rothman,J.E.
  TITLE     'Coatomer': a cytosolic protein complex containing subunits of
            non-clathrin-coated Golgi transport vesicles
  JOURNAL   Nature 349 (6306), 248-251 (1991)
   PUBMED   1898986
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000941.6.
            
            Summary: This gene maps in a region, which include the mixed
            lineage leukemia and Friend leukemia virus integration 1 genes,
            where multiple disease-associated chromosome translocations occur.
            It is an intracellular protein. Archain sequences are well
            conserved among eukaryotes and this protein may play a fundamental
            role in eukaryotic cell biology. It has similarities to heat shock
            proteins and clathrin-associated proteins, and may be involved in
            vesicle structure or trafficking. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX640860.1, SRR14038193.145220.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245, SAMEA2153946
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..488
                     /product="coatomer subunit delta isoform 6"
                     /note="coatomer protein delta-COP; coatomer protein
                     complex, subunit delta; archain vesicle transport protein
                     1; coatomer delta subunit; delta-coat protein; COPI coat
                     complex subunit delta"
                     /calculated_mol_wt=54692
     Region          1..110
                     /region_name="Delta_COP_N"
                     /note="delta subunit of the F-COPI complex, N-terminal
                     domain; cd14830"
                     /db_xref="CDD:341434"
     Region          249..485
                     /region_name="AP_delta-COPI_MHD"
                     /note="Mu homology domain (MHD) of adaptor protein (AP)
                     coat protein I (COPI) delta subunit; cd09254"
                     /db_xref="CDD:271162"
     CDS             1..488
                     /gene="ARCN1"
                     /gene_synonym="COPD; SRMMD; SSMG"
                     /coded_by="NM_001425076.1:373..1839"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:372"
                     /db_xref="HGNC:HGNC:649"
                     /db_xref="MIM:600820"
ORIGIN      
        1 mtrtriegll aafpklmntg kqhtfvetes vryvyqpmek lymvlittkn sniledletl
       61 rlfsrvipey craleeneis ehcfdlifaf deivalgyre nvnlaqirtf temdsheekv
      121 fravretqer eakaemrrka kelqqarrda erqgkkapgf ggfgssavsg gstaamitet
      181 iietdkpkva paparpsgps kalklgakgk evdnfvdklk segetimsss mgkrtseatk
      241 mhappinmes vhmkieekit ltcgrdgglq nmelhgmiml risddkygri rlhvenedkk
      301 gvqlqthpnv dkklftaesl iglknpeksf pvnsdvgvlk wrlqtteesf ipltincwps
      361 esgngcdvni eyelqednle lndvvitipl psgvgapvig eidgeyrhds rrntlewclp
      421 vidaknksgs lefsiagqpn dffpvqvsfv skknycniqv tkvtqvdgns pvrfstettf
      481 lvdkyeil
//
LOCUS       NP_001397990             703 aa            linear   PRI 21-NOV-2025
DEFINITION  metastasis-associated protein MTA1 isoform 3 [Homo sapiens].
ACCESSION   NP_001397990 XP_047287861
VERSION     NP_001397990.1
DBSOURCE    REFSEQ: accession NM_001411061.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Wanka,G., Jueckstock,J., Wild,C.M., Vattai,A., Furst,S.,
            Heidegger,H.H., Kuhn,C., Schmoeckel,E., Jeschke,U. and Dannecker,C.
  TITLE     MTA1 as negative prognostic marker in vulvar carcinoma
  JOURNAL   J Cancer Res Clin Oncol 149 (9), 6191-6201 (2023)
   PUBMED   36689059
  REMARK    GeneRIF: MTA1 as negative prognostic marker in vulvar carcinoma.
REFERENCE   3  (residues 1 to 703)
  AUTHORS   Vattem,C. and Pakala,S.B.
  TITLE     Metastasis-associated protein 1: A potential driver and regulator
            of the hallmarks of cancer
  JOURNAL   J Biosci 47 (2022)
   PUBMED   36210748
  REMARK    GeneRIF: Metastasis-associated protein 1: A potential driver and
            regulator of the hallmarks of cancer.
            Review article
REFERENCE   4  (residues 1 to 703)
  AUTHORS   Kumar,R., Balasenthil,S., Pakala,S.B., Rayala,S.K., Sahin,A.A. and
            Ohshiro,K.
  TITLE     Metastasis-associated protein 1 short form stimulates Wnt1 pathway
            in mammary epithelial and cancer cells
  JOURNAL   Cancer Res 70 (16), 6598-6608 (2010)
   PUBMED   20710043
REFERENCE   5  (residues 1 to 703)
  AUTHORS   Kumar,R., Balasenthil,S., Manavathi,B., Rayala,S.K. and Pakala,S.B.
  TITLE     Metastasis-associated protein 1 and its short form variant
            stimulates Wnt1 transcription through promoting its derepression
            from Six3 corepressor
  JOURNAL   Cancer Res 70 (16), 6649-6658 (2010)
   PUBMED   20682799
REFERENCE   6  (residues 1 to 703)
  AUTHORS   Singh,R.R., Kaluarachchi,K., Chen,M., Rayala,S.K., Balasenthil,S.,
            Ma,J. and Kumar,R.
  TITLE     Solution structure and antiestrogenic activity of the unique
            C-terminal, NR-box motif-containing region of MTA1s
  JOURNAL   J Biol Chem 281 (35), 25612-25621 (2006)
   PUBMED   16807247
  REMARK    GeneRIF: structure and antiestrogenic activity of the unique
            C-terminal, NR-box motif-containing region of MTA1
            Erratum:[J Biol Chem. 2013 Sep 20;288(38):27518]
REFERENCE   7  (residues 1 to 703)
  AUTHORS   Mishra,S.K., Yang,Z., Mazumdar,A., Talukder,A.H., Larose,L. and
            Kumar,R.
  TITLE     Metastatic tumor antigen 1 short form (MTA1s) associates with
            casein kinase I-gamma2, an estrogen-responsive kinase
  JOURNAL   Oncogene 23 (25), 4422-4429 (2004)
   PUBMED   15077195
  REMARK    GeneRIF: MTA1s interacts with CKI-gamma2 in vitro and in vivo and
            colocalizes in the cytoplasm
REFERENCE   8  (residues 1 to 703)
  AUTHORS   Kumar,R., Wang,R.A., Mazumdar,A., Talukder,A.H., Mandal,M.,
            Yang,Z., Bagheri-Yarmand,R., Sahin,A., Hortobagyi,G., Adam,L.,
            Barnes,C.J. and Vadlamudi,R.K.
  TITLE     A naturally occurring MTA1 variant sequesters oestrogen
            receptor-alpha in the cytoplasm
  JOURNAL   Nature 418 (6898), 654-657 (2002)
   PUBMED   12167865
  REMARK    GeneRIF: naturally occurring short form that contains a previously
            unknown sequence of 33 amino acids with an ER-binding motif,
            Leu-Arg-Ile-Leu-Leu (LRILL); MTA1s localizes in the cytoplasm,
            sequesters ER in the cytoplasm, and enhances non-genomic responses
            of ER
REFERENCE   9  (residues 1 to 703)
  AUTHORS   Toh,Y., Pencil,S.D. and Nicolson,G.L.
  TITLE     Analysis of the complete sequence of the novel
            metastasis-associated candidate gene, mta1, differentially
            expressed in mammary adenocarcinoma and breast cancer cell lines
  JOURNAL   Gene 159 (1), 97-104 (1995)
   PUBMED   7607577
REFERENCE   10 (residues 1 to 703)
  AUTHORS   Toh,Y., Pencil,S.D. and Nicolson,G.L.
  TITLE     A novel candidate metastasis-associated gene, mta1, differentially
            expressed in highly metastatic mammary adenocarcinoma cell lines.
            cDNA cloning, expression, and protein analyses
  JOURNAL   J Biol Chem 269 (37), 22958-22963 (1994)
   PUBMED   8083195
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL928654.1.
            
            On Aug 20, 2022 this sequence version replaced XP_047287861.1.
            
            Summary: This gene encodes a protein that was identified in a
            screen for genes expressed in metastatic cells, specifically,
            mammary adenocarcinoma cell lines. Expression of this gene has been
            correlated with the metastatic potential of at least two types of
            carcinomas although it is also expressed in many normal tissues.
            The role it plays in metastasis is unclear. It was initially
            thought to be the 70kD component of a nucleosome remodeling
            deacetylase complex, NuRD, but it is more likely that this
            component is a different but very similar protein. These two
            proteins are so closely related, though, that they share the same
            types of domains. These domains include two DNA binding domains, a
            dimerization domain, and a domain commonly found in proteins that
            methylate DNA. The profile and activity of this gene product
            suggest that it is involved in regulating transcription and that
            this may be accomplished by chromatin remodeling. Two transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Feb 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1972666.1,
                                           SRR14038197.280427.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..703
                     /product="metastasis-associated protein MTA1 isoform 3"
                     /note="metastasis associated gene 1 protein"
                     /calculated_mol_wt=79243
     Region          3..188
                     /region_name="BAH_MTA"
                     /note="BAH, or Bromo Adjacent Homology domain, as present
                     in MTA1 and similar proteins. The Metastasis-associated
                     protein MTA1 is part of the NURD (nucleosome remodeling
                     and deacetylating) complex and plays a role in cellular
                     transformation and metastasis. BAH...; cd04709"
                     /db_xref="CDD:240060"
     Region          167..219
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          287..332
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(288,318..319,321..322,324..326,328..330)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Region          388..441
                     /region_name="ZnF_GATA"
                     /note="zinc finger binding to DNA consensus sequence
                     [AT]GATA[AG]; smart00401"
                     /db_xref="CDD:214648"
     Region          435..460
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13330.2)"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13330.2)"
     Region          464..541
                     /region_name="MTA_R1"
                     /note="MTA R1 domain; pfam17226"
                     /db_xref="CDD:465388"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Region          545..552
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13330.2)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Site            578
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Site            614
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:16617102,
                     ECO:0000269|PubMed:17671180, ECO:0000269|PubMed:19805145;
                     propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Site            627
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13330.2)"
     Region          644..674
                     /region_name="Interaction with RBBP4.
                     /evidence=ECO:0000269|PubMed:24920672"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Region          661..703
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Region          684..693
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     Region          699..703
                     /region_name="SUMO interaction motif 1 (SIM), crucial for
                     efficient sumoylation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13330.2)"
     CDS             1..703
                     /gene="MTA1"
                     /coded_by="NM_001411061.1:210..2321"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS91956.1"
                     /db_xref="GeneID:9112"
                     /db_xref="HGNC:HGNC:7410"
                     /db_xref="MIM:603526"
ORIGIN      
        1 maanmyrvgd yvyfensssn pylirrieel nktangnvea kvvcfyrrrd isstlialad
       61 khatlsvcyk agpgadngee geieeemenp emvdlpeklk hqlrhrelfl srqleslpat
      121 hirgkcsvtl lneteslksy leredfffys lvydpqqktl ladkgeirvg nryqaditdl
      181 lkegeedgrd qsrletqvwe ahnpltdkqi dqflvvarsv gtfaraldcs ssvrqpslhm
      241 saaaasrdit lfhamdtlhk niydiskais alvpqggpvl crdemeewsa seanlfeeal
      301 ekygkdftdi qqdflpwksl tsiieyyymw kttdryvqqk rlkaaeaesk lkqvyipnyn
      361 kpnpnqisvn nvkagvvngt gapgqspgag racescyttq syqwyswgpp nmqcrlcasc
      421 wtywkkyggl kmptrldger pgpnrsnmsp hglparssgs pkfamktrqa fylhttkltr
      481 iarrlcreil rpwhaarhpy lpinsaaika ectarlpeas qsplvlkqav rkpleavlry
      541 lethprppkp dpvksvssvl ssltpakvap vinngsptil gkrsyeqhng vdglanhgqa
      601 rhmgpsrnll lngksyptkv rlirggslpp vkrrrmnwid apddvfymat eetrkirkll
      661 sssetkraar rpykpialrq sqalpprppp papvndepiv ied
//
LOCUS       NP_001191380             424 aa            linear   PRI 21-NOV-2025
DEFINITION  cell cycle progression protein 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001191380
VERSION     NP_001191380.1
DBSOURCE    REFSEQ: accession NM_001204451.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Wang,G., Liu,Z., Wang,Q., Liu,B. and Li,J.
  TITLE     Clinical and prognostic significance of CCPG1 in hepatocellular
            carcinoma
  JOURNAL   Gen Physiol Biophys 42 (5), 431-442 (2023)
   PUBMED   37702448
  REMARK    GeneRIF: Clinical and prognostic significance of CCPG1 in
            hepatocellular carcinoma.
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Chino,H., Hatta,T., Natsume,T. and Mizushima,N.
  TITLE     Intrinsically Disordered Protein TEX264 Mediates ER-phagy
  JOURNAL   Mol Cell 74 (5), 909-921 (2019)
   PUBMED   31006538
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Smith,M.D., Harley,M.E., Kemp,A.J., Wills,J., Lee,M., Arends,M.,
            von Kriegsheim,A., Behrends,C. and Wilkinson,S.
  TITLE     CCPG1 Is a Non-canonical Autophagy Cargo Receptor Essential for
            ER-Phagy and Pancreatic ER Proteostasis
  JOURNAL   Dev Cell 44 (2), 217-232 (2018)
   PUBMED   29290589
  REMARK    GeneRIF: identification of cell-cycle progression gene 1 (CCPG1),
            an ER-resident protein, as a non-canonical cargo receptor that
            directly binds to core autophagy proteins via an LIR motif to
            mammalian ATG8 proteins and, independently and via a discrete
            motif, to FIP200.
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Dunlop,E.A., Seifan,S., Claessens,T., Behrends,C., Kamps,M.A.,
            Rozycka,E., Kemp,A.J., Nookala,R.K., Blenis,J., Coull,B.J.,
            Murray,J.T., van Steensel,M.A., Wilkinson,S. and Tee,A.R.
  TITLE     FLCN, a novel autophagy component, interacts with GABARAP and is
            regulated by ULK1 phosphorylation
  JOURNAL   Autophagy 10 (10), 1749-1760 (2014)
   PUBMED   25126726
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Faghihi,M.A., Kocerha,J., Modarresi,F., Engstrom,P.G., Chalk,A.M.,
            Brothers,S.P., Koesema,E., St Laurent,G. and Wahlestedt,C.
  TITLE     RNAi screen indicates widespread biological function for human
            natural antisense transcripts
  JOURNAL   PLoS One 5 (10), e13177 (2010)
   PUBMED   20957177
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Myslinski,E., Gerard,M.A., Krol,A. and Carbon,P.
  TITLE     A genome scale location analysis of human Staf/ZNF143-binding sites
            suggests a widespread role for human Staf/ZNF143 in mammalian
            promoters
  JOURNAL   J Biol Chem 281 (52), 39953-39962 (2006)
   PUBMED   17092945
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Edwards,M.C., Liegeois,N., Horecka,J., DePinho,R.A., Sprague,G.F.
            Jr., Tyers,M. and Elledge,S.J.
  TITLE     Human CPR (cell cycle progression restoration) genes impart a Far-
            phenotype on yeast cells
  JOURNAL   Genetics 147 (3), 1063-1076 (1997)
   PUBMED   9383053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB084778.1, AK022459.1, AC018926.10 and AA740595.1.
            
            Transcript Variant: This variant (4) lacks two segments in the 3'
            coding region, one of which causes a frameshift. The encoded
            isoform (3) has a distinct C-terminus and is shorter than isoform
            1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK022459.1, SRR14038197.1591508.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.3"
     Protein         1..424
                     /product="cell cycle progression protein 1 isoform 3"
                     /note="cell cycle progression restoration protein 8"
                     /calculated_mol_wt=48438
     Region          1..308
                     /region_name="Interaction with MCF2L and SRC.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULG6.3)"
     Region          84..>231
                     /region_name="PLN02328"
                     /note="lysine-specific histone demethylase 1 homolog"
                     /db_xref="CDD:215187"
     Region          152..207
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULG6.3)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9ULG6.3)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULG6.3)"
     CDS             1..424
                     /gene="CCPG1"
                     /gene_synonym="CPR8"
                     /coded_by="NM_001204451.2:149..1423"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS55967.1"
                     /db_xref="GeneID:9236"
                     /db_xref="HGNC:HGNC:24227"
                     /db_xref="MIM:611326"
ORIGIN      
        1 msenssdsds scgwtvishe gsdiemlnsv tptdscepap ecssleqeel qalqieqges
       61 sqngtvlmee taypaleets stieaeeqki pedsiyigta sddsdivtle ppkleeignq
      121 evviveeaqs sedfnmgsss ssqytfcqpe tvfssqpsdd esssdetsnq pspafrrrra
      181 rkktvsases edrlvaeqet epskelskrq fssglnkcvi lalviaismg fghfygtiqi
      241 qkrqqlvrki hedelndmkd ylsqcqqeqe sfidykslke nlarcwtlte aekmsfetqk
      301 tnlatenqyl rklftdfvnd vkdylrnmke yevdndgvfe kldeyiyrhf fghtfsppyg
      361 psrpdkkqrm vniensrhrk qeqkhlqpqp ykregkwhky grtngrqman leielgqlpf
      421 dpqy
//
LOCUS       NP_001424673             619 aa            linear   PRI 21-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001424673 XP_005268412 XP_054207395
VERSION     NP_001424673.1
DBSOURCE    REFSEQ: accession NM_001437744.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 619)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 619)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 619)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 619)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 619)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 619)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 619)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008641.7.
            
            On or before Apr 9, 2025 this sequence version replaced
            XP_005268412.1, XP_054207395.1.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.993582.1,
                                           SRR11853563.27344.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..619
                     /product="TNFAIP3-interacting protein 1 isoform 1"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=69944
     Region          14..>149
                     /region_name="Speriolin_N"
                     /note="Speriolin N terminus; pfam15058"
                     /db_xref="CDD:434426"
     Region          61..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          94..412
                     /region_name="Interaction with Nef"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Region          <214..>251
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          252..283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          <298..>538
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          351..367
                     /region_name="Interaction with Shigella flexneri ipah9.8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          431..588
                     /region_name="Required for inhibitory activity of
                     TNF-induced NF-kappa-B activation. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Region          452..510
                     /region_name="Ubiquitin-binding domain (UBD)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Region          524..530
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15025.2)"
     Site            552
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:17632516; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            571
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9WUU8; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     Site            599
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15025.2)"
     CDS             1..619
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001437744.1:192..2051"
                     /note="isoform 1 is encoded by transcript variant 24"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 megrgpyriy dpggsvpsge asaaferlvk ensrlkekmq gikmlgelle esqmeatrlr
       61 qkaeelvkdn ellpppspsl gsfdplaelt gkdsnvtasp tapacpsdkp apvqkppssg
      121 tssefevvtp eeqnspesss hanamalgpl predgnlmlh lqrlettlsv caeepdhgql
      181 fthlgrmale fnrlaskvhk neqrtsilqt lceqlrkene alkakldkgl eqrdqaaerl
      241 reenlelkkl lmsngnkega sgrpgspkme gtgkkavagq qqasvtagkv pevvalgaae
      301 kkvkmleqqr sellevnkqw dqhfrsmkqq yeqkitelrq kladlqkqvt dleaereqkq
      361 rdfdrkllla kskiemeetd keqltaeake lrqkvkylqd qlspltrqre yqekeiqrln
      421 kaleealsiq tppsspptaf gspegagall rkqelvtqne llkqqvkife edfqrersdr
      481 ermneekeel kkqveklqaq vtlsnaqlka fkdeekarea lrqqkrkaka sgeryhveph
      541 pehlcgaypy ayppmpamvp hhgfedwsqi ryppppmame hppplpnsrl fhlhqfcrsr
      601 ntpgvypveg feiqirapk
//
LOCUS       NP_001400229             280 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 3 [Homo sapiens].
ACCESSION   NP_001400229 XP_016868560
VERSION     NP_001400229.1
DBSOURCE    REFSEQ: accession NM_001413300.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 280)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 280)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 280)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            On Oct 31, 2022 this sequence version replaced XP_016868560.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.11072.1,
                                           SRR3476690.493713.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2163459, SAMN03465401
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..280
                     /product="RNA-binding Raly-like protein isoform 3"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=30943
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          188..>233
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     CDS             1..280
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413300.1:245..1087"
                     /note="isoform 3 is encoded by transcript variant 14"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly sgyvfdydyy
      121 rddfynrlfd yhgrvppppr aviplkrprv avtttrrgkg vfsmkggsrs tasgstgskl
      181 ksdelqtikk eltqiktkid sllgrlekie kqqkaeaeaq kkqleeslvl iqeecvseia
      241 dhsteepaeg gpdadgeemt dgieedfded gghelflqik
//
LOCUS       NP_001427366            1211 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 isoform 3
            [Homo sapiens].
ACCESSION   NP_001427366
VERSION     NP_001427366.1
DBSOURCE    REFSEQ: accession NM_001440437.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1211)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1211)
  AUTHORS   Ji,X., Wu,Q., Cao,X., Liu,S., Zhang,J., Chen,S., Shan,J., Zhang,Y.,
            Li,B. and Zhao,H.
  TITLE     Helicobacter pylori East Asian type CagA hijacks more SHIP2 by its
            EPIYA-D motif to potentiate the oncogenicity
  JOURNAL   Virulence 15 (1), 2375549 (2024)
   PUBMED   38982595
  REMARK    GeneRIF: Helicobacter pylori East Asian type CagA hijacks more
            SHIP2 by its EPIYA-D motif to potentiate the oncogenicity.
REFERENCE   3  (residues 1 to 1211)
  AUTHORS   Ando,K., Kucukali,F., Doeraene,E., Nagaraj,S., Antonelli,E.M.,
            Thazin Htut,M., Yilmaz,Z., Kosa,A.C., Lopez-Guitierrez,L.,
            Quintanilla-Sanchez,C., Aydin,E., Ramos,A.R., Mansour,S.,
            Turbant,S., Schurmans,S., Sleegers,K., Erneux,C., Brion,J.P. and
            Leroy,K.
  CONSRTM   Brain Bank NeuroCEB Neuropathology Network
  TITLE     Alteration of gene expression and protein solubility of the PI
            5-phosphatase SHIP2 are correlated with Alzheimer's disease
            pathology progression
  JOURNAL   Acta Neuropathol 147 (1), 94 (2024)
   PUBMED   38833073
  REMARK    GeneRIF: Alteration of gene expression and protein solubility of
            the PI 5-phosphatase SHIP2 are correlated with Alzheimer's disease
            pathology progression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1211)
  AUTHORS   Bradshaw,W.J., Kennedy,E.C., Moreira,T., Smith,L.A., Chalk,R.,
            Katis,V.L., Benesch,J.L.P., Brennan,P.E., Murphy,E.J. and
            Gileadi,O.
  TITLE     Regulation of inositol 5-phosphatase activity by the C2 domain of
            SHIP1 and SHIP2
  JOURNAL   Structure 32 (4), 453-466 (2024)
   PUBMED   38309262
  REMARK    GeneRIF: Regulation of inositol 5-phosphatase activity by the C2
            domain of SHIP1 and SHIP2.
REFERENCE   5  (residues 1 to 1211)
  AUTHORS   Habib,T., Hejna,J.A., Moses,R.E. and Decker,S.J.
  TITLE     Growth factors and insulin stimulate tyrosine phosphorylation of
            the 51C/SHIP2 protein
  JOURNAL   J Biol Chem 273 (29), 18605-18609 (1998)
   PUBMED   9660833
REFERENCE   6  (residues 1 to 1211)
  AUTHORS   Le Drean,E., Vely,F., Olcese,L., Cambiaggi,A., Guia,S., Krystal,G.,
            Gervois,N., Moretta,A., Jotereau,F. and Vivier,E.
  TITLE     Inhibition of antigen-induced T cell response and antibody-induced
            NK cell cytotoxicity by NKG2A: association of NKG2A with SHP-1 and
            SHP-2 protein-tyrosine phosphatases
  JOURNAL   Eur J Immunol 28 (1), 264-276 (1998)
   PUBMED   9485206
  REMARK    Erratum:[Eur J Immunol 1998 Mar;28(3):1122]
REFERENCE   7  (residues 1 to 1211)
  AUTHORS   Pesesse,X., Deleu,S., De Smedt,F., Drayer,L. and Erneux,C.
  TITLE     Identification of a second SH2-domain-containing protein closely
            related to the phosphatidylinositol polyphosphate 5-phosphatase
            SHIP
  JOURNAL   Biochem Biophys Res Commun 239 (3), 697-700 (1997)
   PUBMED   9367831
REFERENCE   8  (residues 1 to 1211)
  AUTHORS   Hejna,J.A., Saito,H., Merkens,L.S., Tittle,T.V., Jakobs,P.M.,
            Whitney,M.A., Grompe,M., Friedberg,A.S. and Moses,R.E.
  TITLE     Cloning and characterization of a human cDNA (INPPL1) sharing
            homology with inositol polyphosphate phosphatases
  JOURNAL   Genomics 29 (1), 285-287 (1995)
   PUBMED   8530088
REFERENCE   9  (residues 1 to 1211)
  AUTHORS   Huang,S., Earl,D. and White,K.
  TITLE     INPPL1-Related Opsismodysplasia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   40504975
REFERENCE   10 (residues 1 to 1211)
  AUTHORS   Slama,V. and Dudek,J.
  TITLE     [Stability of diluted solutions of peracetic acid]
  JOURNAL   Cesk Farm 17 (1), 40-41 (1968)
   PUBMED   5668240
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000593.4.
            
            Summary: The protein encoded by this gene is an SH2-containing
            5'-inositol phosphatase that is involved in the regulation of
            insulin function. The encoded protein also plays a role in the
            regulation of epidermal growth factor receptor turnover and actin
            remodelling. Additionally, this gene supports metastatic growth in
            breast cancer and is a valuable biomarker for breast cancer.
            [provided by RefSeq, Jan 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.453719.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..1211
                     /product="phosphatidylinositol 3,4,5-trisphosphate
                     5-phosphatase 2 isoform 3"
                     /EC_number="3.1.3.86"
                     /note="SH2 domain-containing inositol-5'-phosphatase 2;
                     51C protein; protein 51C; phosphatidylinositol
                     3,4,5-trisphosphate 5-phosphatase 2"
                     /calculated_mol_wt=133470
     Region          17..119
                     /region_name="SH2_SHIP"
                     /note="Src homology 2 (SH2) domain found in SH2-containing
                     inositol-5'-phosphatase (SHIP) and SLAM-associated protein
                     (SAP); cd10343"
                     /db_xref="CDD:198206"
     Site            order(28,47,68,70)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198206"
     Site            order(68..69,81..82,87,90,106..108)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198206"
     Region          377..680
                     /region_name="INPP5c_SHIP2-INPPL1"
                     /note="Catalytic inositol polyphosphate 5-phosphatase
                     (INPP5c) domain of SH2 domain containing inositol
                     5-phosphatase-2 and related proteins; cd09101"
                     /db_xref="CDD:197335"
     Site            order(385,387,426,493..494,514,517..518,560,562,564,
                     614..615,637,643,670..671)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197335"
     Site            order(385,426,514,560,562,643,670..671)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197335"
     Site            order(426,493..494,514,517..518,564,614..615,637,670)
                     /site_type="other"
                     /note="putative PI/IP binding site [chemical binding]"
                     /db_xref="CDD:197335"
     Site            order(426,670)
                     /site_type="other"
                     /note="putative Mg binding site [ion binding]"
                     /db_xref="CDD:197335"
     Site            order(514,562,671)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197335"
     Region          <852..1167
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1147..1209
                     /region_name="SAM_Ship2"
                     /note="SAM domain of Ship2 lipid phosphatase proteins;
                     cd09491"
                     /db_xref="CDD:188890"
     Site            order(1175..1177,1179..1180,1183,1188)
                     /site_type="other"
                     /note="heterodimer interface ML [polypeptide binding]"
                     /db_xref="CDD:188890"
     CDS             1..1211
                     /gene="INPPL1"
                     /gene_synonym="OPSMD; SHIP2"
                     /coded_by="NM_001440437.1:219..3854"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:3636"
                     /db_xref="HGNC:HGNC:6080"
                     /db_xref="MIM:600829"
ORIGIN      
        1 masacgapgp ggalgsqaps wyhrdlsraa aeellaragr dgsflvrdse svagafalcv
       61 lyqkhvhtyr ilpdgedfla vqtsqgvpvr rfqtlgelig lyaqpnqglv calllpvege
      121 repdppddrd asdgedekpp lpprsgstsi saptgpsspl papetptapa aesevdkvls
      181 gleilskvfd qqsspmvtrl lqqqnlpqtg eqeleslvlk lsvlkdflsg iqkkalkalq
      241 dmsstappap qpstrkakti pvqafevkld vtlgdltkig ksqkftlsvd veggrlvllr
      301 rqrdsqedwt tfthdrirql iksqrvqnkl gvvfekekdr tqrkdfifvs arkreafcql
      361 lqlmknkhsk qdepdmisvf igtwnmgsvp ppknvtswft skglgktlde vtvtiphdiy
      421 vfgtqensvg drewldllrg glkeltdldy rpiamqslwn ikvavlvkpe henrishvst
      481 ssvktgiant lgnkgavgvs fmfngtsfgf vnchltsgne ktarrnqnyl dilrllslgd
      541 rqlnafdisl rfthlfwfgd lnyrldmdiq eilnyisrke fepllrvdql nlerekhkvf
      601 lrfseeeisf pptyryergs rdtyawhkqk ptgvrtnvps wcdrilwksy pethiicnsy
      661 gctddivtsd hspvfgtfev gvtsqfiskk glsktsdqay iefesieaiv ktasrtkffi
      721 efystcleey kksfendaqs sdninflkvq wssrqlptlk piladieylq dqhllltvks
      781 mdgyesygec vvalksmigs taqqfltfls hrgeetgnir gsmkvrvpte rlgtrerlye
      841 wisidkdeag akskapsvsr gsqeprsgsr kpafteascp lsrlfeepek ppptgrppap
      901 praapreepl tprlkpegap epegvaappp knsfnnpayy vlegvphqll ppeppspara
      961 pvpsatknkv aitvpapqlg hhrhprvgeg sssdeesggt lpppdfpppp lpdsaiflpp
     1021 sldplpgpvv rgrggaearg ppppkahprp plppgpspas tflgevasgd drscsvlqma
     1081 ktlsevdyap agparsallp gplelqpprg lpsdygrpls fpppriresi qedlaeeapc
     1141 lqggrasglg eagmsawlra igleryeegl vhngwddlef lsditeedle eagvqdpahk
     1201 rllldtlqls k
//
LOCUS       NP_001397996            1140 aa            linear   PRI 21-NOV-2025
DEFINITION  CST complex subunit CTC1 isoform 2 [Homo sapiens].
ACCESSION   NP_001397996 XP_006721641
VERSION     NP_001397996.1
DBSOURCE    REFSEQ: accession NM_001411067.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1140)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1140)
  AUTHORS   Takai,H., Aria,V., Borges,P., Yeeles,J.T.P. and de Lange,T.
  TITLE     CST-polymerase alpha-primase solves a second telomere
            end-replication problem
  JOURNAL   Nature 627 (8004), 664-670 (2024)
   PUBMED   38418884
  REMARK    GeneRIF: CST-polymerase alpha-primase solves a second telomere
            end-replication problem.
REFERENCE   3  (residues 1 to 1140)
  AUTHORS   Liu,L., Luo,H., Sheng,Y., Kang,X., Peng,H., Luo,H. and Fan,L.L.
  TITLE     A novel mutation of CTC1 leads to telomere shortening in a chinese
            family with interstitial lung disease
  JOURNAL   Hereditas 160 (1), 37 (2023)
   PUBMED   37978541
  REMARK    GeneRIF: A novel mutation of CTC1 leads to telomere shortening in a
            chinese family with interstitial lung disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1140)
  AUTHORS   Wang,H., Ma,T., Zhang,X., Chen,W., Lan,Y., Kuang,G., Hsu,S.J.,
            He,Z., Chen,Y., Stewart,J., Bhattacharjee,A., Luo,Z., Price,C. and
            Feng,X.
  TITLE     CTC1 OB-B interaction with TPP1 terminates telomerase and prevents
            telomere overextension
  JOURNAL   Nucleic Acids Res 51 (10), 4914-4928 (2023)
   PUBMED   37021555
  REMARK    GeneRIF: CTC1 OB-B interaction with TPP1 terminates telomerase and
            prevents telomere overextension.
REFERENCE   5  (residues 1 to 1140)
  AUTHORS   Polvi,A., Linnankivi,T., Kivela,T., Herva,R., Keating,J.P.,
            Makitie,O., Pareyson,D., Vainionpaa,L., Lahtinen,J., Hovatta,I.,
            Pihko,H. and Lehesjoki,A.E.
  TITLE     Mutations in CTC1, encoding the CTS telomere maintenance complex
            component 1, cause cerebroretinal microangiopathy with
            calcifications and cysts
  JOURNAL   Am J Hum Genet 90 (3), 540-549 (2012)
   PUBMED   22387016
  REMARK    GeneRIF: Observed four recessively inherited compound heterozygous
            mutations in CTC1, which encodes the CTS telomere maintenance
            complex component 1.
REFERENCE   6  (residues 1 to 1140)
  AUTHORS   Anderson,B.H., Kasher,P.R., Mayer,J., Szynkiewicz,M.,
            Jenkinson,E.M., Bhaskar,S.S., Urquhart,J.E., Daly,S.B.,
            Dickerson,J.E., O'Sullivan,J., Leibundgut,E.O., Muter,J.,
            Abdel-Salem,G.M., Babul-Hirji,R., Baxter,P., Berger,A., Bonafe,L.,
            Brunstom-Hernandez,J.E., Buckard,J.A., Chitayat,D., Chong,W.K.,
            Cordelli,D.M., Ferreira,P., Fluss,J., Forrest,E.H., Franzoni,E.,
            Garone,C., Hammans,S.R., Houge,G., Hughes,I., Jacquemont,S.,
            Jeannet,P.Y., Jefferson,R.J., Kumar,R., Kutschke,G., Lundberg,S.,
            Lourenco,C.M., Mehta,R., Naidu,S., Nischal,K.K., Nunes,L.,
            Ounap,K., Philippart,M., Prabhakar,P., Risen,S.R., Schiffmann,R.,
            Soh,C., Stephenson,J.B., Stewart,H., Stone,J., Tolmie,J.L., van der
            Knaap,M.S., Vieira,J.P., Vilain,C.N., Wakeling,E.L., Wermenbol,V.,
            Whitney,A., Lovell,S.C., Meyer,S., Livingston,J.H.,
            Baerlocher,G.M., Black,G.C., Rice,G.I. and Crow,Y.J.
  TITLE     Mutations in CTC1, encoding conserved telomere maintenance
            component 1, cause Coats plus
  JOURNAL   Nat Genet 44 (3), 338-342 (2012)
   PUBMED   22267198
  REMARK    GeneRIF: Mutations in CTC1, encoding conserved telomere maintenance
            component 1, cause Coats plus.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1140)
  AUTHORS   Surovtseva,Y.V., Churikov,D., Boltz,K.A., Song,X., Lamb,J.C.,
            Warrington,R., Leehy,K., Heacock,M., Price,C.M. and Shippen,D.E.
  TITLE     Conserved telomere maintenance component 1 interacts with STN1 and
            maintains chromosome ends in higher eukaryotes
  JOURNAL   Mol Cell 36 (2), 207-218 (2009)
   PUBMED   19854131
  REMARK    GeneRIF: CTC1 participates in telomere maintenance in diverse
            species and that a CST-like complex is required for telomere
            integrity in multicellular organisms.
REFERENCE   8  (residues 1 to 1140)
  AUTHORS   Miyake,Y., Nakamura,M., Nabetani,A., Shimamura,S., Tamura,M.,
            Yonehara,S., Saito,M. and Ishikawa,F.
  TITLE     RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded
            DNA and protects telomeres independently of the Pot1 pathway
  JOURNAL   Mol Cell 36 (2), 193-206 (2009)
   PUBMED   19854130
  REMARK    GeneRIF: Ctc1-Stn1-Ten1 is a replication protein A (RPA)-like
            complex that is not directly involved in conventional DNA
            replication at forks but plays a role in DNA metabolism frequently
            required by telomeres.
REFERENCE   9  (residues 1 to 1140)
  AUTHORS   Casteel,D.E., Zhuang,S., Zeng,Y., Perrino,F.W., Boss,G.R.,
            Goulian,M. and Pilz,R.B.
  TITLE     A DNA polymerase-{alpha}{middle dot}primase cofactor with homology
            to replication protein A-32 regulates DNA replication in mammalian
            cells
  JOURNAL   J Biol Chem 284 (9), 5807-5818 (2009)
   PUBMED   19119139
REFERENCE   10 (residues 1 to 1140)
  AUTHORS   Savage,S.A. and Niewisch,M.R.
  TITLE     Dyskeratosis Congenita and Related Telomere Biology Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301779
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC135178.13 and KF456245.1.
            
            On Aug 20, 2022 this sequence version replaced XP_006721641.1.
            
            Summary: This gene encodes a component of the CST complex. This
            complex plays an essential role in protecting telomeres from
            degradation. This protein also forms a heterodimer with the CST
            complex subunit STN1 to form the enzyme alpha accessory factor.
            This enzyme regulates DNA replication. Mutations in this gene are
            the cause of cerebroretinal microangiopathy with calcifications and
            cysts. Alternate splicing results in both coding and non-coding
            variants. [provided by RefSeq, Mar 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.685395.1,
                                           SRR14038192.4133052.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..1140
                     /product="CST complex subunit CTC1 isoform 2"
                     /note="CST complex subunit CTC1; alpha accessory factor
                     132; conserved telomere capping protein 1; HBV
                     DNAPTP1-transactivated protein B; CTS telomere maintenance
                     complex component 1; CST telomere maintenance complex
                     component 1"
                     /calculated_mol_wt=126383
     Region          61..1124
                     /region_name="CTC1"
                     /note="CST, telomere maintenance, complex subunit CTC1;
                     pfam15489"
                     /db_xref="CDD:464744"
     Region          328..347
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2NKJ3.2)"
     CDS             1..1140
                     /gene="CTC1"
                     /gene_synonym="AAF-132; AAF132; C17orf68; CRMCC;
                     tmp494178"
                     /coded_by="NM_001411067.1:21..3443"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92251.1"
                     /db_xref="GeneID:80169"
                     /db_xref="HGNC:HGNC:26169"
                     /db_xref="MIM:613129"
ORIGIN      
        1 maagraqvps seqawledaq vfiqktlcpa vkepnvqltp lvidcvktvw lsqgrnqgst
       61 lplsysfvsv qdlkthqrlp ccshlswsss ayqawaqeag pngnplpreq llllgtltdl
      121 sadleqecrn gslyvrdntg vlscelidld lswlghlflf prwsylppar wnssgeghle
      181 lwdapvpvfp ltispgpvtp ipvlypesas cllrlrnklr gvqrnlagsl vrlsalvksk
      241 qkayfilslg rshpavthvs iivqvpaqlv whralrpgta yvltelrvsk irgqrqhvwm
      301 tsqssrllll kpecvqelel elegpllead pkplpmpsns edkkdpeslv rysrllsysg
      361 avtgvlnepa glyeldgqlg lclayqqfrg lrrvmrpgvc lqlqdvhllq svgggtrrpv
      421 lapclrgavl lqsfsrqkpg ahssrqayga slyeqlvwer qlglplylwa tkaleelack
      481 lcphvlrhhq flqhsspgsp slglqllapt ldllappgsp vrnahneile ephhcplqky
      541 trlqtpssfp tlatlkeegq rkawasfdpk allplpeasy lpscqlnrrl awswlcllps
      601 afcpaqvllg vlvasshkgc lqlrdqsgsl pclllakhsq plsdprligc lvraerfqli
      661 verdvrssfp swkelsmpgf iqkqqarvyv qffladalil pvprpclhsa tpstpqtdpt
      721 gpegphlgqs rlfllchkea lmkrnfcvpp gaspevpkpa lsfyvlgswl ggtqrkegtg
      781 wglpepqgnd dndqkvhlif fgssvrwfef lhpgqvyrli apgpatpmlf ekdgsscisr
      841 rplelagcas cltvqdnwtl elessqdiqd vldankslpe ssltdllsdn ftdslvsfsa
      901 eilsrtlcep lvaslwmklg ntgamrrcvk ltvaletaec efpphldvyi edphlppslg
      961 llpgarvhfs qlekrvsrsh nvyccfrsst yvqvlsfppe ttisiplphi ylaellqggq
     1021 spfqatasch ivsvfslqlf wvcayctsic rqssarvdep mtmflwtlct spsvlrpivl
     1081 sfelerkpsk ivplepprlq rfqcgelpfl thvnprlrls clsireseys sslgilassc
//
LOCUS       NP_001394251             326 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 23 [Homo sapiens].
ACCESSION   NP_001394251
VERSION     NP_001394251.1
DBSOURCE    REFSEQ: accession NM_001407322.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.389939.1,
                                           SRR18074969.1398070.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..326
                     /product="tropomyosin alpha-1 chain isoform 23"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=37433
     Region          2..>159
                     /region_name="EmrA"
                     /note="Multidrug resistance efflux pump EmrA [Defense
                     mechanisms]; COG1566"
                     /db_xref="CDD:441174"
     Region          90..324
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..326
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407322.1:84..1064"
                     /note="isoform 23 is encoded by transcript variant 23"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle ediaakekll rvsederdrv
       61 leelhkaeds llaaeeaaak ledelvslqk klkgtedeld kysealkdaq eklelaekka
      121 tdaeadvasl nrriqlveee ldraqerlat alqkleeaek aadesergmk viesraqkde
      181 ekmeiqeiql keakhiaeda drkyeevark lviiesdler aeeraelseg qvrqleeqlr
      241 imdqtlkalm aaedkysqke dryeeeikvl sdklkeaetr aefaersvtk leksiddled
      301 elyaqklkyk aiseeldhal ndmtsi
//
LOCUS       NP_001397841             362 aa            linear   PRI 21-NOV-2025
DEFINITION  protein GNAS isoform j [Homo sapiens].
ACCESSION   NP_001397841 XP_024307640
VERSION     NP_001397841.1
DBSOURCE    REFSEQ: accession NM_001410912.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Lin,J., Nie,Q., Cheng,J., Zhong,Y.N., Zhang,T., Zhang,X., Ge,X.,
            Ding,Y., Niu,C., Gao,Y., Wang,K., Gao,M., Wang,X., Chen,W., Yun,C.,
            Ye,C., Xu,J., Shaoyong,W., Zhang,L., Shang,P., Luo,X., Zhang,Z.,
            Zheng,X., Sha,X., Zhang,J., Nie,S., Zhang,X., Ren,F., Liu,H.,
            Dong,E., Yu,X., Ji,L., Pang,Y., Sun,J.P. and Jiang,C.
  TITLE     A microbial amino-acid-conjugated bile acid, tryptophan-cholic
            acid, improves glucose homeostasis via the orphan receptor MRGPRE
  JOURNAL   Cell 188 (17), 4530-4548 (2025)
   PUBMED   40446798
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Crane,J.L., Shamblott,M.J., Axelman,J., Hsu,S., Levine,M.A. and
            Germain-Lee,E.L.
  TITLE     Imprinting status of Galpha(s), NESP55, and XLalphas in cell
            cultures derived from human embryonic germ cells: GNAS imprinting
            in human embryonic germ cells
  JOURNAL   Clin Transl Sci 2 (5), 355-360 (2009)
   PUBMED   20443919
  REMARK    GeneRIF: analysis of the imprinting Status of Galpha(s), NESP55,
            and XLalphas in cell cultures derived from human embryonic germ
            cells
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Bastepe,M.
  TITLE     The GNAS Locus: Quintessential Complex Gene Encoding Gsalpha,
            XLalphas, and other Imprinted Transcripts
  JOURNAL   Curr Genomics 8 (6), 398-414 (2007)
   PUBMED   19412439
  REMARK    GeneRIF: GNAS locus has a highly complex imprinted expression
            pattern, giving rise to transcripts (including non-coding) that are
            maternally, paternally, or biallelically expressed.
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Jakobsen,A.M., Ahlman,H., Kolby,L., Abrahamsson,J.,
            Fischer-Colbrie,R. and Nilsson,O.
  TITLE     NESP55, a novel chromogranin-like peptide, is expressed in
            endocrine tumours of the pancreas and adrenal medulla but not in
            ileal carcinoids
  JOURNAL   Br J Cancer 88 (11), 1746-1754 (2003)
   PUBMED   12771991
  REMARK    GeneRIF: Neuroendocrine secretory protein 55 is found in a subset
            of neuroendocrine tumours showing differentiation towards adrenal
            chromaffin cells and pancreatic islets cells and not in ileal
            carcinoids
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Freson,K., Jaeken,J., Van Helvoirt,M., de Zegher,F.,
            Wittevrongel,C., Thys,C., Hoylaerts,M.F., Vermylen,J. and Van
            Geet,C.
  TITLE     Functional polymorphisms in the paternally expressed XLalphas and
            its cofactor ALEX decrease their mutual interaction and enhance
            receptor-mediated cAMP formation
  JOURNAL   Hum Mol Genet 12 (10), 1121-1130 (2003)
   PUBMED   12719376
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Weiss,U., Ischia,R., Eder,S., Lovisetti-Scamihorn,P., Bauer,R. and
            Fischer-Colbrie,R.
  TITLE     Neuroendocrine secretory protein 55 (NESP55): alternative splicing
            onto transcripts of the GNAS gene and posttranslational processing
            of a maternally expressed protein
  JOURNAL   Neuroendocrinology 71 (3), 177-186 (2000)
   PUBMED   10729789
REFERENCE   7  (residues 1 to 362)
  AUTHORS   Ischia,R., Lovisetti-Scamihorn,P., Hogue-Angeletti,R.,
            Wolkersdorfer,M., Winkler,H. and Fischer-Colbrie,R.
  TITLE     Molecular cloning and characterization of NESP55, a novel
            chromogranin-like precursor of a peptide with 5-HT1B receptor
            antagonist activity
  JOURNAL   J Biol Chem 272 (17), 11657-11662 (1997)
   PUBMED   9111083
REFERENCE   8  (residues 1 to 362)
  AUTHORS   Haldeman-Englert,C.R., Hurst,A.C.E. and Levine,M.A.
  TITLE     Disorders of GNAS Inactivation
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29072892
REFERENCE   9  (residues 1 to 362)
  AUTHORS   Szymczuk,V., Florenzano,P., de Castro,L.F., Collins,M.T. and
            Boyce,A.M.
  TITLE     Fibrous Dysplasia / McCune-Albright Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719192
REFERENCE   10 (residues 1 to 362)
  AUTHORS   Weinstein,L.S., Gejman,P.V., de Mazancourt,P., American,N. and
            Spiegel,A.M.
  TITLE     A heterozygous 4-bp deletion mutation in the Gs alpha gene (GNAS1)
            in a patient with Albright hereditary osteodystrophy
  JOURNAL   Genomics 13 (4), 1319-1321 (1992)
   PUBMED   1505964
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL132655.13, AL121917.20 and
            AL109840.24.
            
            On Aug 17, 2022 this sequence version replaced XP_024307640.1.
            
            Summary: This locus has a highly complex imprinted expression
            pattern. It gives rise to maternally, paternally, and biallelically
            expressed transcripts that are derived from four alternative
            promoters and 5' exons. Some transcripts contain a differentially
            methylated region (DMR) at their 5' exons, and this DMR is commonly
            found in imprinted genes and correlates with transcript expression.
            An antisense transcript is produced from an overlapping locus on
            the opposite strand. One of the transcripts produced from this
            locus, and the antisense transcript, are paternally expressed
            noncoding RNAs, and may regulate imprinting in this region. In
            addition, one of the transcripts contains a second overlapping ORF,
            which encodes a structurally unrelated protein - Alex. Alternative
            splicing of downstream exons is also observed, which results in
            different forms of the stimulatory G-protein alpha subunit, a key
            element of the classical signal transduction pathway linking
            receptor-ligand interactions with the activation of adenylyl
            cyclase and a variety of cellular reponses. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            Mutations in this gene result in pseudohypoparathyroidism type 1a,
            pseudohypoparathyroidism type 1b, Albright hereditary
            osteodystrophy, pseudopseudohypoparathyroidism, McCune-Albright
            syndrome, progressive osseus heteroplasia, polyostotic fibrous
            dysplasia of bone, and some pituitary tumors. [provided by RefSeq,
            Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1066800.1, BC036081.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 19412439
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.32"
     Protein         1..362
                     /product="protein GNAS isoform j"
                     /note="secretogranin VI; G protein subunit alpha S;
                     guanine nucleotide binding protein (G protein), alpha
                     stimulating activity polypeptide 1; guanine nucleotide
                     regulatory protein; adenylate cyclase-stimulating G alpha
                     protein; protein ALEX; extra large alphas protein;
                     alternative gene product encoded by XL-exon"
                     /calculated_mol_wt=41703
     Region          5..356
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Site            order(15,20..22,172,191,194,260..261,263,333..334)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206639"
     Site            15..22
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206639"
     Site            order(16..18,61,65,69,72,75..76,96,99,140,169,194,202,206)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Site            167..175
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            172
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(173,175,177,188,190,194..196,198,201..202,204..207)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(175,200,203..204,207)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            191..194
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            192..208
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Site            260..263
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(325..336,338..341)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Site            333..335
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..362
                     /gene="GNAS"
                     /gene_synonym="AHO; AIMAH1; C20orf45; GNAS1; GPSA; GSA;
                     GSP; NESP; PITA3; POH; SCG6; SgVI"
                     /coded_by="NM_001410912.1:1097..2185"
                     /note="isoform j is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS93063.1"
                     /db_xref="GeneID:2778"
                     /db_xref="HGNC:HGNC:4392"
                     /db_xref="MIM:139320"
ORIGIN      
        1 medavqillv fmdsgagesg kstivkqmri lhvngfngeg geedpqaars nsdgekatkv
       61 qdiknnlkea ietivaamsn lvppvelanp enqfrvdyil svmnvpdfdf ppefyehaka
      121 lwedegvrac yersneyqli dcaqyfldki dvikqadyvp sdqdllrcrv ltsgifetkf
      181 qvdkvnfhmf dvggqrderr kwiqcfndvt aiifvvasss ynmvirednq tnrlqealnl
      241 fksiwnnrwl rtisvilfln kqdllaekvl agkskiedyf pefaryttpe datpepgedp
      301 rvtrakyfir deflristas gdgrhycyph ftcavdteni rrvfndcrdi iqrmhlrqye
      361 ll
//
LOCUS       NP_001397912             981 aa            linear   PRI 21-NOV-2025
DEFINITION  spliceosome associated factor 3, U4/U6 recycling protein isoform 2
            [Homo sapiens].
ACCESSION   NP_001397912 XP_005269298
VERSION     NP_001397912.1
DBSOURCE    REFSEQ: accession NM_001410983.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 981)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 981)
  AUTHORS   Wang,Y., Zhou,J., He,W., Fu,R., Shi,L., Dang,N.K., Liu,B., Xu,H.,
            Cheng,X. and Bedford,M.T.
  TITLE     SART3 reads methylarginine-marked glycine- and arginine-rich motifs
  JOURNAL   Cell Rep 43 (7), 114459 (2024)
   PUBMED   38985674
  REMARK    GeneRIF: SART3 reads methylarginine-marked glycine- and
            arginine-rich motifs.
REFERENCE   3  (residues 1 to 981)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   4  (residues 1 to 981)
  AUTHORS   Kim,J., Taketomi,T., Yamada,A., Uematsu,Y., Ueda,K., Chiba,T. and
            Tsuruta,F.
  TITLE     USP4 regulates TUT1 ubiquitination status in concert with SART3
  JOURNAL   Biochem Biophys Res Commun 701, 149557 (2024)
   PUBMED   38310689
  REMARK    GeneRIF: USP4 regulates TUT1 ubiquitination status in concert with
            SART3.
REFERENCE   5  (residues 1 to 981)
  AUTHORS   Ayers,K.L., Eggers,S., Rollo,B.N., Smith,K.R., Davidson,N.M.,
            Siddall,N.A., Zhao,L., Bowles,J., Weiss,K., Zanni,G., Burglen,L.,
            Ben-Shachar,S., Rosensaft,J., Raas-Rothschild,A., Jorgensen,A.,
            Schittenhelm,R.B., Huang,C., Robevska,G., van den Bergen,J.,
            Casagranda,F., Cyza,J., Pachernegg,S., Wright,D.K., Bahlo,M.,
            Oshlack,A., O'Brien,T.J., Kwan,P., Koopman,P., Hime,G.R.,
            Girard,N., Hoffmann,C., Shilon,Y., Zung,A., Bertini,E., Milh,M.,
            Ben Rhouma,B., Belguith,N., Bashamboo,A., McElreavey,K., Banne,E.,
            Weintrob,N., BenZeev,B. and Sinclair,A.H.
  TITLE     Variants in SART3 cause a spliceosomopathy characterised by failure
            of testis development and neuronal defects
  JOURNAL   Nat Commun 14 (1), 3403 (2023)
   PUBMED   37296101
  REMARK    GeneRIF: Variants in SART3 cause a spliceosomopathy characterised
            by failure of testis development and neuronal defects.
            Erratum:[Nat Commun. 2023 Jun 15;14(1):3566. doi:
            10.1038/s41467-023-39372-x. PMID: 37322043]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 981)
  AUTHORS   Tanaka,S., Tsuda,N., Kawano,K., Sakamoto,M., Nishida,T.,
            Hashimoto,T., Shichijo,S., Kamura,T. and Itoh,K.
  TITLE     Expression of tumor-rejection antigens in gynecologic cancers
  JOURNAL   Jpn J Cancer Res 91 (11), 1177-1184 (2000)
   PUBMED   11092984
REFERENCE   7  (residues 1 to 981)
  AUTHORS   Xia,J.H., Yang,Y.F., Deng,H., Tang,B.S., Tang,D.S., He,Y.G.,
            Xia,K., Chen,S.X., Li,Y.X., Pan,Q., Long,Z.G., Dai,H.P., Liao,X.D.,
            Xiao,J.F., Liu,Z.R., Lu,C.Y., Yu,K.P. and Deng,H.X.
  TITLE     Identification of a locus for disseminated superficial actinic
            porokeratosis at chromosome 12q23.2-24.1
  JOURNAL   J Invest Dermatol 114 (6), 1071-1074 (2000)
   PUBMED   10844547
REFERENCE   8  (residues 1 to 981)
  AUTHORS   Harada,K., Yamada,A., Mine,T., Kawagoe,N., Takasu,H. and Itoh,K.
  TITLE     Mouse homologue of the human SART3 gene encoding tumor-rejection
            antigen
  JOURNAL   Jpn J Cancer Res 91 (2), 239-247 (2000)
   PUBMED   10761712
REFERENCE   9  (residues 1 to 981)
  AUTHORS   Nottrott,S., Hartmuth,K., Fabrizio,P., Urlaub,H., Vidovic,I.,
            Ficner,R. and Luhrmann,R.
  TITLE     Functional interaction of a novel 15.5kD [U4/U6.U5] tri-snRNP
            protein with the 5' stem-loop of U4 snRNA
  JOURNAL   EMBO J 18 (21), 6119-6133 (1999)
   PUBMED   10545122
REFERENCE   10 (residues 1 to 981)
  AUTHORS   Yang,D., Nakao,M., Shichijo,S., Sasatomi,T., Takasu,H.,
            Matsumoto,H., Mori,K., Hayashi,A., Yamana,H., Shirouzu,K. and
            Itoh,K.
  TITLE     Identification of a gene coding for a protein possessing shared
            tumor epitopes capable of inducing HLA-A24-restricted cytotoxic T
            lymphocytes in cancer patients
  JOURNAL   Cancer Res 59 (16), 4056-4063 (1999)
   PUBMED   10463607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008119.6 and AC010206.8.
            
            On Aug 18, 2022 this sequence version replaced XP_005269298.1.
            
            Summary: The protein encoded by this gene is an RNA-binding nuclear
            protein that is a tumor-rejection antigen. This antigen possesses
            tumor epitopes capable of inducing HLA-A24-restricted and
            tumor-specific cytotoxic T lymphocytes in cancer patients and may
            be useful for specific immunotherapy. This gene product is found to
            be an important cellular factor for HIV-1 gene expression and viral
            replication. It also associates transiently with U6 and U4/U6
            snRNPs during the recycling phase of the spliceosome cycle. This
            encoded protein is thought to be involved in the regulation of mRNA
            splicing. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853560.7621.1,
                                           SRR18074969.3475961.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..981
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.3"
     Protein         1..981
                     /product="spliceosome associated factor 3, U4/U6 recycling
                     protein isoform 2"
                     /note="tat-interacting protein of 110 kDa; SART-3;
                     hSART-3; squamous cell carcinoma antigen recognized by T
                     cells 3; p110 nuclear RNA-binding protein; HIV-1
                     Tat-interacting protein of 110kDa; PRP24 homolog"
                     /calculated_mol_wt=111827
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.13,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Region          50..90
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          100..>478
                     /region_name="RNA14"
                     /note="Pre-mRNA 3'-end processing (cleavage and
                     polyadenylation) factor [RNA processing and modification];
                     COG5107"
                     /db_xref="CDD:227438"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Region          342..374
                     /region_name="HAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          377..409
                     /region_name="HAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          412..448
                     /region_name="HAT 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          505..538
                     /region_name="Required for interaction with USP4.
                     /evidence=ECO:0000269|PubMed:20595234"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          555..971
                     /region_name="Necessary and sufficient for U6 snRNA
                     binding. /evidence=ECO:0000269|PubMed:15314151"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          608..712
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          618..688
                     /region_name="Required for nuclear localization.
                     /evidence=ECO:0000269|PubMed:11959860"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          619..626
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00768"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Site            675
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Region          723..796
                     /region_name="RRM1_SART3"
                     /note="RNA recognition motif 1 (RRM1) found in squamous
                     cell carcinoma antigen recognized by T-cells 3 (SART3) and
                     similar proteins; cd12391"
                     /db_xref="CDD:409825"
     Site            787
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Site            813
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Region          817..897
                     /region_name="RRM2_SART3"
                     /note="RNA recognition motif 2 (RRM2) found in squamous
                     cell carcinoma antigen recognized by T-cells 3 (SART3) and
                     similar proteins; cd12392"
                     /db_xref="CDD:409826"
     Site            870
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Region          895..951
                     /region_name="LSM_int_assoc"
                     /note="LSM-interacting associated unstructured; pfam16605"
                     /db_xref="CDD:465192"
     Region          896..916
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Site            924
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Region          938..966
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     CDS             1..981
                     /gene="SART3"
                     /gene_synonym="DSAP1; P100; p110; p110(nrb); RP11-13G14;
                     TIP110"
                     /coded_by="NM_001410983.1:20..2965"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS91747.1"
                     /db_xref="GeneID:9733"
                     /db_xref="HGNC:HGNC:16860"
                     /db_xref="MIM:611684"
ORIGIN      
        1 mataaetsas epeaeskagp kadgeedevk aartrrkvls ravaaatykt mgpawdqqee
       61 gvsesdgdey amassaessp geyeweydee eeknqleier leeqlsinvy dynchvdlir
      121 llrlegeltk vrmarqkmse ifplteelwl ewlhdeisma qdgldrehvy dlfekavkdy
      181 icpniwleyg qysvggigqk gglekvrsvf eralssvglh mtkglalwea yrefesaive
      241 aarpvagfls pfdreqtfds qlekvhslfr rqlaiplydm eatfaeyeew sedpipesvi
      301 qnynkalqql ekykpyeeal lqaeaprlae yqayidfemk igdpariqli feralvencl
      361 vpdlwirysq yldrqlkvkd lvlsvhnrai rncpwtvalw sryllamerh gvdhqvisvt
      421 fekalnagfi qatdyveiwq ayldylrrrv dfkqdsskel eelraaftra leylkqevee
      481 rfnesgdpsc vimqnwarie arlcnnmqka relwdsimtr gnakyanmwl eyynlerahg
      541 dtqhcrkalh ravqctsdyp ehvcevlltm ertegsledw diavqktetr larvneqrmk
      601 aaekeaalvq qeeekaeqrk raraekkalk kkkkirgpek rgadeddeke wgddeeeqps
      661 krrrvensip aagetqnvev aagpagkcaa vdveppskqk ekaaslkrdm pkvlhdsskd
      721 sitvfvsnlp ysmqepdtkl rplfeacgev vqirpifsnr gdfrgycyve fkeeksalqa
      781 lemdrksveg rpmfvspcvd ksknpdfkvf rystslekhk lfisglpfsc tkeeleeick
      841 ahgtvkdlrl vtnragkpkg layveyenes qasqavmkmd gmtikeniik vaisnppqrk
      901 vpekpetrka pggpmllpqt ygargkgrtq lsllpralqr psaaapqaen gpaaapavaa
      961 paateapkms nadfaklflr k
//
LOCUS       NP_001394736            1233 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 3 precursor
            [Homo sapiens].
ACCESSION   NP_001394736
VERSION     NP_001394736.1
DBSOURCE    REFSEQ: accession NM_001407807.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1233)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1233)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1233)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1233)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1233)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1233)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1233)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1233)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1233)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1233)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2019497.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1233
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1233
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 3 precursor"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=134886
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O00411.2)"
                     /calculated_mol_wt=4109
     Region          18..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          95..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          261..290
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          296..323
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          428..700
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          727..746
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          827..1233
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1233
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407807.1:26..3727"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 msalcwgrga aglkralrpc grpglpgkeg taggvcgprr sssaspqeqd qdrrkdwghv
       61 ellevlqarv rqlqaesvse vvvnrvdvar lpecgsgdgs lqpprkvqmg akdatpvpcg
      121 rwakilekdk rtqqmrmqrl kaklqmpfqs gefkaltrrl qveprllskq magcledctr
      181 qapespweeq larllqeapg klsldveqap sgqhsqaqls gqqqrllaff kcclltdqlp
      241 lahhllvvhh gqrqkrkllt ldmynavmlg warqgafkel vyvlfmvkda gltpdllsya
      301 aalqcmgrqd qdagtiercl eqmsqeglkl qalftavlls eedratvlka vhkvkptfsl
      361 ppqlpppvnt skllrdvyak dgrvsypklh lplktlqclf ekqlhmelas rvcvvsvekp
      421 tlpskerktl ktlrdqweka lcralretkn rlerevyegr fslypflcll derevvrmll
      481 qvlqalpaqg esfttlarel sartfsrhvv qrqrvsgqvq alqnhyrkyl cllasdaevp
      541 epclprqywe elgapealre qpwplpvqme lgkllaemlv qatqmpcsld kphrssrlvp
      601 vlyhvysfrn vqqigilkph payvqlleka aeptltfeav dvpmlcpplp wtsphsgafl
      661 lsptklmrtv egatqhqell etcpptalhg aldaltqlgn cawrvngrvl dlvlqlfqak
      721 gcpqlgvpap pseapqppea hlphsaapar kaelrrelah cqkvaremhs lraealyrls
      781 laqhlrdrvf wlphnmdfrg rtypcpphfn hlgsdvaral lefaqgrplg phgldwlkih
      841 lvnltglkkr eplrkrlafa eevmddilds adqpltgrkw wmgaeepwqt laccmevana
      901 vrasdpaayv shlpvhqdgs cnglqhyaal grdsvgaasv nlepsdvpqd vysgvaaqve
      961 vfrrqdaqrg mrvaqvlegf itrkvvkqtv mtvvygvtry ggrlqiekrl relsdfpqef
     1021 vweashylvr qvfkslqemf sgtraiqhwl tesarlishm gsvvewvtpl gvpviqpyrl
     1081 dskvkqiggg iqsitythng disrkpntrk qkngfppnfi hsldsshmml talhcyrspp
     1141 lchrkgltfv svhdcywtha advsvmnqvc reqfvrlhse pilqdlsrfl vkrfcsepqk
     1201 ileasqlket lqavpkpgaf dleqvkrsty ffs
//
LOCUS       NP_001427730            1207 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphorylase b kinase regulatory subunit alpha, liver isoform
            isoform 3 [Homo sapiens].
ACCESSION   NP_001427730 XP_005274607 XP_054183178
VERSION     NP_001427730.1
DBSOURCE    REFSEQ: accession NM_001440801.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1207)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1207)
  AUTHORS   Dong,R., Wei,X., Zhang,K., Song,F., Lv,Y., Gao,M., Wang,D., Ma,J.,
            Gai,Z. and Liu,Y.
  TITLE     Genotypic and phenotypic characteristics of 12 chinese children
            with glycogen storage diseases
  JOURNAL   Front Genet 13, 932760 (2022)
   PUBMED   36105079
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1207)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1207)
  AUTHORS   Benner,A., Alhaidan,Y., Lines,M.A., Brusgaard,K., De Leon,D.D.,
            Sparkes,R., Frederiksen,A.L. and Christesen,H.T.
  TITLE     PHKA2 variants expand the phenotype of phosphorylase B kinase
            deficiency to include patients with ketotic hypoglycemia only
  JOURNAL   Am J Med Genet A 185 (10), 2959-2975 (2021)
   PUBMED   34117828
  REMARK    GeneRIF: PHKA2 variants expand the phenotype of phosphorylase B
            kinase deficiency to include patients with ketotic hypoglycemia
            only.
REFERENCE   5  (residues 1 to 1207)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1207)
  AUTHORS   Herbert,M., Goldstein,J.L., Rehder,C., Austin,S., Kishnani,P.S. and
            Bali,D.S.
  TITLE     Phosphorylase Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21634085
REFERENCE   7  (residues 1 to 1207)
  AUTHORS   Davidson,J.J., Ozcelik,T., Hamacher,C., Willems,P.J., Francke,U.
            and Kilimann,M.W.
  TITLE     cDNA cloning of a liver isoform of the phosphorylase kinase alpha
            subunit and mapping of the gene to Xp22.2-p22.1, the region of
            human X-linked liver glycogenosis
  JOURNAL   Proc Natl Acad Sci U S A 89 (6), 2096-2100 (1992)
   PUBMED   1372435
REFERENCE   8  (residues 1 to 1207)
  AUTHORS   Wauters,J.G., Bossuyt,P.J., Davidson,J., Hendrickx,J.,
            Kilimann,M.W. and Willems,P.J.
  TITLE     Regional mapping of a liver alpha-subunit gene of phosphorylase
            kinase (PHKA) to the distal region of human chromosome Xp
  JOURNAL   Cytogenet Cell Genet 60 (3-4), 194-196 (1992)
   PUBMED   1505214
REFERENCE   9  (residues 1 to 1207)
  AUTHORS   Willems,P.
  TITLE     Families with X-linked liver glycogenosis due to phosphorylase
            kinase deficiency
  JOURNAL   Clin Genet 38 (1), 80 (1990)
   PUBMED   2387090
REFERENCE   10 (residues 1 to 1207)
  AUTHORS   Willems,P.J., Gerver,W.J., Berger,R. and Fernandes,J.
  TITLE     The natural history of liver glycogenosis due to phosphorylase
            kinase deficiency: a longitudinal study of 41 patients
  JOURNAL   Eur J Pediatr 149 (4), 268-271 (1990)
   PUBMED   2303074
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL732509.4 and AL096700.14.
            
            On or before May 30, 2025 this sequence version replaced
            XP_005274607.1, XP_054183178.1.
            
            Summary: Phosphorylase kinase is a polymer of 16 subunits, four
            each of alpha, beta, gamma and delta. The alpha subunit includes
            the skeletal muscle and hepatic isoforms, and the hepatic isoform
            is encoded by this gene. The beta subunit is the same in both the
            muscle and hepatic isoforms, and encoded by one gene. The gamma
            subunit also includes the skeletal muscle and hepatic isoforms,
            which are encoded by two different genes. The delta subunit is a
            calmodulin and can be encoded by three different genes. The gamma
            subunits contain the active site of the enzyme, whereas the alpha
            and beta subunits have regulatory functions controlled by
            phosphorylation. The delta subunit mediates the dependence of the
            enzyme on calcium concentration. Mutations in this gene cause
            glycogen storage disease type 9A, also known as X-linked liver
            glycogenosis. Alternatively spliced transcript variants have been
            reported, but the full-length nature of these variants has not been
            determined.[provided by RefSeq, Feb 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2349029.1,
                                           SRR18074967.2336390.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1207
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.13"
     Protein         1..1207
                     /product="phosphorylase b kinase regulatory subunit alpha,
                     liver isoform isoform 3"
                     /EC_number="2.7.11.19"
                     /note="phosphorylase kinase alpha L subunit; phosphorylase
                     kinase alpha-subunit"
                     /calculated_mol_wt=135317
     Region          8..>439
                     /region_name="Glyco_hydro_15"
                     /note="Glycosyl hydrolases family 15; pfam00723"
                     /db_xref="CDD:395586"
     Region          <802..919
                     /region_name="Bac_rhamnosid6H"
                     /note="Bacterial alpha-L-rhamnosidase 6 hairpin
                     glycosidase domain; cl46875"
                     /db_xref="CDD:481215"
     Region          930..>1119
                     /region_name="KPBB_C"
                     /note="Phosphorylase b kinase C-terminal domain;
                     pfam19292"
                     /db_xref="CDD:437124"
     CDS             1..1207
                     /gene="PHKA2"
                     /gene_synonym="GSD9A; PHK; PYK; PYKL; XLG; XLG2"
                     /coded_by="NM_001440801.1:183..3806"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:5256"
                     /db_xref="HGNC:HGNC:8926"
                     /db_xref="MIM:300798"
ORIGIN      
        1 mrsrsnsgvr ldgyarlvqq tilcyqnpvt gllsasheqk dawvrdniys ilavwglgma
       61 yrknadrded kakayeleqn vvklmrgllq cmmrqvakve kfkhtqstkd slhakyntat
      121 cgtvvgddqw ghlqvdatsl fllflaqmta sglriiftld evafiqnlvf yieaaykvad
      181 ygmwergdkt nqgipelnas svgmakaale aideldlfga hggrksvihv lpdevehcqs
      241 ilfsmlpras tskeidagll siisfpafav edvnlvnvtk neiisklqgr ygccrflrdg
      301 yktpredpnr lhydpaelkl feniecewpv fwtyfiidgv fsgdavqvqe yrealegili
      361 rgkngirlvp elyavppnkv deeyknphtv drvpmgkvph lwgqslyils sllaegflaa
      421 geidplnrrf stsvkpdvvv qvtvlaennh ikdllrkhgv nvqsiadihp iqvqpgrils
      481 hiyaklgrnk nmnlsgrpyr higvlgtskl yvirnqiftf tpqftdqhhf ylaldnemiv
      541 emlrielayl ctcwrmtgrp tltfpisrtm ltndgsdihs avlstirkle dgyfggarvk
      601 lgnlsefltt sfytyltfld pdcdeklfdn asegtfspds dsdlvgyled tcnqesqdel
      661 dhyinhllqs tslrsylppl ckntedrhvf saihstrdil svmakakgle vpfvpmtlpt
      721 kvlsahrksl nlvdspqpll ekvpesdfqw prddhgdvdc eklveqlkdc snlqdqadil
      781 yilyvikgps wdtnlsgqhg vtvqnllgel ygkaglnqew gliryisgll rkkvevlaea
      841 ctdllshqkq ltvglppepr ekiisaplpp eeltkliyea sgqdisiavl tqeivvylam
      901 yvraqpslfv emlrlrigli iqvmatelar slncsgeeas eslmnlspfd mknllhhils
      961 gkefgversv rpihsstssp tisihevght gvtktersgi nrlrsemkqr sstpssptgt
     1021 sssdsgghhi gwgerqgqwl rrrrldgain rvpvgfyqrv wkilqkchgl sidgyvlpss
     1081 ttremtphei kfavhvesvl nrvpqpeyrq llveaimvlt llsdtemtsi ggiihvdqiv
     1141 qmasqlflqd qvsigamdtl ekdqatgich ffydsapsga ygtmtyltra vasylqellp
     1201 nsgcqmq
//
LOCUS       NP_001397711             405 aa            linear   PRI 21-NOV-2025
DEFINITION  ADP-ribosylation factor-like protein 13B isoform 5 [Homo sapiens].
ACCESSION   NP_001397711 XP_047303616
VERSION     NP_001397711.1
DBSOURCE    REFSEQ: accession NM_001410782.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Lin,Z., Shen,Y., Li,Y., Lu,C., Zhu,Y., He,R., Cao,Z., Yin,Z.,
            Gao,H., Guo,B., Ma,X., Cao,M. and Luo,M.
  TITLE     Novel compound heterozygous variants in ARL13B lead to Joubert
            syndrome
  JOURNAL   J Cell Physiol 239 (4), e31189 (2024)
   PUBMED   38219074
  REMARK    GeneRIF: Novel compound heterozygous variants in ARL13B lead to
            Joubert syndrome.
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Shi,P., Tian,J., Mallinger,J.C., Ling,D., Deleyrolle,L.P.,
            McIntyre,J.C., Caspary,T., Breunig,J.J. and Sarkisian,M.R.
  TITLE     Increasing Ciliary ARL13B Expression Drives Active and
            Inhibitor-Resistant Smoothened and GLI into Glioma Primary Cilia
  JOURNAL   Cells 12 (19), 2354 (2023)
   PUBMED   37830570
  REMARK    GeneRIF: Increasing Ciliary ARL13B Expression Drives Active and
            Inhibitor-Resistant Smoothened and GLI into Glioma Primary Cilia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Mahajan,D., Madugula,V. and Lu,L.
  TITLE     Rab8 and TNPO1 are ciliary transport adaptors for GTPase Arl13b by
            interacting with its RVEP motif containing ciliary targeting
            sequence
  JOURNAL   J Biol Chem 299 (5), 104604 (2023)
   PUBMED   36907439
  REMARK    GeneRIF: Rab8 and TNPO1 are ciliary transport adaptors for GTPase
            Arl13b by interacting with its RVEP motif containing ciliary
            targeting sequence.
REFERENCE   5  (residues 1 to 405)
  AUTHORS   Hori,Y., Kobayashi,T., Kikko,Y., Kontani,K. and Katada,T.
  TITLE     Domain architecture of the atypical Arf-family GTPase Arl13b
            involved in cilia formation
  JOURNAL   Biochem Biophys Res Commun 373 (1), 119-124 (2008)
   PUBMED   18554500
  REMARK    GeneRIF: These findings suggest that N and C domains of Arl13b
            cooperatively regulate its ciliary localization and that N
            domain-dependent self-association of Arl13b may be important for
            its function in cilia biogenesis.
REFERENCE   6  (residues 1 to 405)
  AUTHORS   Cantagrel,V., Silhavy,J.L., Bielas,S.L., Swistun,D., Marsh,S.E.,
            Bertrand,J.Y., Audollent,S., Attie-Bitach,T., Holden,K.R.,
            Dobyns,W.B., Traver,D., Al-Gazali,L., Ali,B.R., Lindner,T.H.,
            Caspary,T., Otto,E.A., Hildebrandt,F., Glass,I.A., Logan,C.V.,
            Johnson,C.A., Bennett,C., Brancati,F., Valente,E.M., Woods,C.G. and
            Gleeson,J.G.
  CONSRTM   International Joubert Syndrome Related Disorders Study Group
  TITLE     Mutations in the cilia gene ARL13B lead to the classical form of
            Joubert syndrome
  JOURNAL   Am J Hum Genet 83 (2), 170-179 (2008)
   PUBMED   18674751
  REMARK    GeneRIF: ARL13B has an evolutionarily conserved role mediating
            cilia function in multiple organs
REFERENCE   7  (residues 1 to 405)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   8  (residues 1 to 405)
  AUTHORS   Fan,Y., Esmail,M.A., Ansley,S.J., Blacque,O.E., Boroevich,K.,
            Ross,A.J., Moore,S.J., Badano,J.L., May-Simera,H., Compton,D.S.,
            Green,J.S., Lewis,R.A., van Haelst,M.M., Parfrey,P.S.,
            Baillie,D.L., Beales,P.L., Katsanis,N., Davidson,W.S. and
            Leroux,M.R.
  TITLE     Mutations in a member of the Ras superfamily of small GTP-binding
            proteins causes Bardet-Biedl syndrome
  JOURNAL   Nat Genet 36 (9), 989-993 (2004)
   PUBMED   15314642
REFERENCE   9  (residues 1 to 405)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 405)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC117474.7 and AC130896.3.
            
            On Aug 16, 2022 this sequence version replaced XP_047303616.1.
            
            Summary: This gene encodes a member of the ADP-ribosylation
            factor-like family. The encoded protein is a small GTPase that
            contains both N-terminal and C-terminal guanine nucleotide-binding
            motifs. This protein is localized in the cilia and plays a role in
            cilia formation and in maintenance of cilia. Mutations in this gene
            are the cause of Joubert syndrome 8. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2047544.1,
                                           SRR14038195.1325317.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q11.1-q11.2"
     Protein         1..405
                     /product="ADP-ribosylation factor-like protein 13B isoform
                     5"
                     /note="ADP-ribosylation factor-like 2-like 1; ARL2-like
                     protein 1; ADP ribosylation factor like GTPase 13B"
                     /calculated_mol_wt=45963
     Region          23..189
                     /region_name="Arl2l1_Arl13_like"
                     /note="Arl2-like protein 1 (Arl2l1) and Arl13; cd04161"
                     /db_xref="CDD:133361"
     Site            28..35
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133361"
     Site            order(30..36,51..52,74,130..131,133,166..168)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133361"
     Site            order(30..31,35,39,51..58,80,85)
                     /site_type="other"
                     /note="putative GAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133361"
     Site            order(40..43,45..55)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133361"
     Site            order(52..56,61,71,75,81,83..85)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133361"
     Site            52
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133361"
     Site            order(53..60,70,81,84..85)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:133361"
     Site            order(56..62,65..70)
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:133361"
     Site            71..88
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133361"
     Site            71..74
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133361"
     Site            130..133
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133361"
     Site            166..168
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133361"
     Region          <199..241
                     /region_name="CCDC47"
                     /note="PAT complex subunit CCDC47; cl46382"
                     /db_xref="CDD:480722"
     CDS             1..405
                     /gene="ARL13B"
                     /gene_synonym="ARL2L1; JBTS8"
                     /coded_by="NM_001410782.1:270..1487"
                     /note="isoform 5 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS93326.1"
                     /db_xref="GeneID:200894"
                     /db_xref="HGNC:HGNC:25419"
                     /db_xref="MIM:608922"
ORIGIN      
        1 mfslmasccg wfkrwrepvr kvtllmvgld nagktatakg iqgeypedva ptvgfskinl
       61 rqgkfevtif dlgggirirg iwknyyaesy gvifvvdssd eermeetkea msemlrhpri
      121 sgkpilvlan kqdkegalge advieclsle klvnehkclc qiepcsaisg ygkkidksik
      181 kglywllhvi ardfdalner iqketteqra leeqekqera ervrklreer kqneqeqael
      241 dgtsglaeld peptnpfqpi asviienegk lerekknqkm ekdsdgchlk hkmeheqiet
      301 qgqvnhngqk nnefglveny kealtqqlkn edetdrpsle sangkkktkk lrmkrnhrve
      361 plniddcape sptppppppp dfyrkplppl avpqrpnsda hdvis
//
LOCUS       NP_001394377            2861 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform c [Homo sapiens].
ACCESSION   NP_001394377
VERSION     NP_001394377.1
DBSOURCE    REFSEQ: accession NM_001407448.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2861)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2861)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2861)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2861)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2861)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2861)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2861)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2861)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2861)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2861)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1775415.1,
                                           SRR14038193.2255709.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2861
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2861
                     /product="adenomatous polyposis coli protein isoform c"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=313343
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Region          <8..272
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          239..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          340..392
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          393..466
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          490..526
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          523..565
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          530..571
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          534..571
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          566..609
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          581..613
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(604,608,612,651,655,659,696,700,704)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          610..656
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          621..662
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          657..701
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          667..707
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          671..705
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          702..743
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          709..749
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          713..749
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          744..785
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          750..1037
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Site            762
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            798
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          846..896
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            926
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          941..961
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          976..1005
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          978..1355
                     /region_name="Responsible for down-regulation through a
                     process mediated by direct ubiquitination"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1005
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1038..1187
                     /region_name="Interaction with catenins.
                     /evidence=ECO:0000269|PubMed:8259519"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1054..1153
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Site            1056
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1060
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1117..1187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1208..1262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1275..>1292
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1301..1386
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1309..1719
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1329..1394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1421..1493
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1456
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1544..1587
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1601..1629
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1655..1678
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1680..1733
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1682..1735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1734..1755
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1747..1854
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1764..1857
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Site            1792
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1879
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1881
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1882
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1884..1911
                     /region_name="Highly charged"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1891..1965
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1899..1968
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1983..2029
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1989
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1991
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2051..2070
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2053..2077
                     /region_name="Interaction with AXIN1.
                     /evidence=ECO:0000269|PubMed:10811618"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2061..2090
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2165..2653
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2169
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2185..2692
                     /region_name="Basic region.
                     /evidence=ECO:0000269|PubMed:17293347"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2241..2586
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Site            2278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2491
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2493..2861
                     /region_name="Interaction with DLG1.
                     /evidence=ECO:0000269|PubMed:8638125"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2553
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2587
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2685..2732
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2688..2861
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     Site            2689
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2692..2861
                     /region_name="Interaction with MAPRE1.
                     /evidence=ECO:0000269|PubMed:17293347"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2697
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2728
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2742
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2747..2861
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2807
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2821..2824
                     /region_name="Microtubule tip localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2859..2861
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     CDS             1..2861
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407448.1:171..8756"
                     /note="isoform c is encoded by transcript variant 18"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrriar iqqiekdilr irqllqsqat
      241 eaerssqnkh etgshdaerq negqgvgein matsgngqgs ttrmdhetas vlssssthsa
      301 prrltshlgt kvemvyslls mlgthdkddm srtllamsss qdscismrqs gclplliqll
      361 hgndkdsvll gnsrgskear arasaalhni ihsqpddkrg rreirvlhll eqiraycetc
      421 wewqeahepg mdqdknpmpa pvehqicpav cvlmklsfde ehrhamnelg rkatrgissq
      481 elgqglsggl qaiaellqvd cemygltndh ysitlrryag maltnltfgd vankatlcsm
      541 kgcmralvaq lksesedlqq viasvlrnls wradvnskkt lrevgsvkal mecalevkke
      601 stlksvlsal wnlsahcten kadicavdga laflvgtlty rsqtntlaii esgggilrnv
      661 ssliatnedh rqilrenncl qtllqhlksh sltivsnacg tlwnlsarnp kdqealwdmg
      721 avsmlknlih skhkmiamgs aaalrnlman rpakykdani mspgsslpsl hvrkqkalea
      781 eldaqhlset fdnidnlspk ashrskqrhk qslygdyvfd tnrhddnrsd nfntgnmtvl
      841 spylnttvlp sssssrgsld ssrsekdrsl erergiglgn yhpatenpgt sskrglqist
      901 taaqiakvme evsaihtsqe drssgsttel hcvtdernal rrssaahths ntynftksen
      961 snrtcsmpya kleykrssnd slnsvsssdg ygkrgqmkps iesyseddes kfcsygqypa
     1021 dlahkihsan hmddndgeld tpinyslkys deqlnsgrqs psqnerwarp khiiedeikq
     1081 seqrqsrnqs ttypvytest ddkhlkfqph fgqqecvspy rsrgangset nrvgsnhgin
     1141 qnvsqslcqe ddyeddkptn yseryseeeq heeeerptny sikyneekrh vdqpidyslk
     1201 yatdipssqk qsfsfsksss gqssktehms sssentstps snakrqnqlh pssaqsrsgq
     1261 pqkaatckvs sinqetiqty cvedtpicfs rcsslsslss aedeigcnqt tqeadsantl
     1321 qiaeikekig trsaedpvse vpavsqhprt kssrlqgssl ssesarhkav efssgaksps
     1381 ksgaqtpksp pehyvqetpl mfsrctsvss ldsfesrsia ssvqsepcsg mvsgiispsd
     1441 lpdspgqtmp psrsktpppp pqtaqtkrev pknkaptaek resgpkqaav naavqrvqvl
     1501 pdadtllhfa testpdgfsc ssslsalsld epfiqkdvel rimppvqend ngneteseqp
     1561 kesnenqeke aektidsekd llddsddddi eileeciisa mptkssrkak kpaqtasklp
     1621 ppvarkpsql pvykllpsqn rlqpqkhvsf tpgddmprvy cvegtpinfs tatslsdlti
     1681 esppnelaag egvrggaqsg efekrdtipt egrstdeaqg gktssvtipe lddnkaeegd
     1741 ilaecinsam pkgkshkpfr vkkimdqvqq asasssapnk nqldgkkkkp tspvkpipqn
     1801 teyrtrvrkn adsknnlnae rvfsdnkdsk kqnlknnskv fndklpnned rvrgsfafds
     1861 phhytpiegt pycfsrndsl ssldfddddv dlsrekaelr kakenkesea kvtshtelts
     1921 nqqsanktqa iakqpinrgq pkpilqkqst fpqsskdipd rgaatdeklq nfaientpvc
     1981 fshnsslssl sdidqennnk enepiketep pdsqgepskp qasgyapksf hvedtpvcfs
     2041 rnsslsslsi dseddllqec issampkkkk psrlkgdnek hsprnmggil gedltldlkd
     2101 iqrpdsehgl spdsenfdwk aiqegansiv sslhqaaaaa clsrqassds dsilslksgi
     2161 slgspfhltp dqeekpftsn kgprilkpge kstletkkie seskgikggk kvykslitgk
     2221 vrsnseisgq mkqplqanmp sisrgrtmih ipgvrnssss tspvskkgpp lktpasksps
     2281 egqtattspr gakpsvksel spvarqtsqi ggsskapsrs gsrdstpsrp aqqplsrpiq
     2341 spgrnsispg rngisppnkl sqlprtssps tastkssgsg kmsytspgrq msqqnltkqt
     2401 glsknassip rsesaskgln qmnngngank kvelsrmsst kssgsesdrs erpvlvrqst
     2461 fikeapsptl rrkleesasf eslspssrpa sptrsqaqtp vlspslpdms lsthssvqag
     2521 gwrklppnls ptieyndgrp akrhdiarsh sespsrlpin rsgtwkrehs khssslprvs
     2581 twrrtgssss ilsassesse kaksedekhv nsisgtkqsk enqvsakgtw rkikenefsp
     2641 tnstsqtvss gatngaeskt liyqmapavs ktedvwvrie dcpinnprsg rsptgntppv
     2701 idsvsekanp nikdskdnqa kqnvgngsvp mrtvglenrl nsfiqvdapd qkgteikpgq
     2761 nnpvpvsetn essivertpf sssssskhss psgtvaarvt pfnynpsprk ssadstsarp
     2821 sqiptpvnnn tkkrdsktds tessgtqspk rhsgsylvts v
//
LOCUS       NP_001400619             345 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 22 precursor [Homo sapiens].
ACCESSION   NP_001400619
VERSION     NP_001400619.1
DBSOURCE    REFSEQ: accession NM_001413690.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 345)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 345)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 345)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR3218380.474051.1,
                                           SRR14243140.4357216.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..345
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 22 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=34834
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..340
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            195..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            220..240
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            275..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            311..331
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     CDS             1..345
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413690.1:169..1206"
                     /note="isoform 22 precursor is encoded by transcript
                     variant 26"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vqaneeyqil answryssaf
      121 cnklffsmvd ydegtdvfqq lnmnsaptfm hfppkgrpkr adtfdlqrig faaeqlakwi
      181 adrtdvhirv frppnysgti alallvslvg gllylrrnnl efiynktgwa mvslcivfam
      241 tsgqmwnhir gppyahknph ngqvsyihgs sqaqfvaesh iilvlnaait mgmvllneaa
      301 tskgdvgkrr iiclvglglv vfffsfllsi frskyhgypy sflik
//
LOCUS       NP_001393532            1158 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 6 [Homo sapiens].
ACCESSION   NP_001393532
VERSION     NP_001393532.1
DBSOURCE    REFSEQ: accession NM_001406603.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1158)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1158)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1158)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1158)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1158)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1158)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1158)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1158)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1158)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1158)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3783952.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1158
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1158
                     /product="hamartin isoform 6"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=129140
     Region          7..713
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          438..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <702..>954
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1000..1079
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1094
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1125..1158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1158
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406603.1:189..3665"
                     /note="isoform 6 is encoded by transcript variant 17"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt ggkgtplgtp atspppaplc hsddyvhisl pqatvtpprk
      421 eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed siekdkeeaa
      481 isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv npeplhssld
      541 klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp trvgfgsgqp
      601 ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr liqqgadahs
      661 kelnklplps ksvdwthfgd eirtlrdqll llhnqllyer fkrqqhalrn rrllrkvika
      721 aaleehnaam kdqlklqekd iqmwkvslqk eqarynqlqe qrdtmvtklh sqirqlqhdr
      781 eefynqsqel qtkledcrnm iaelrielkk annkvchtel llsqvsqkls nsesvqqqme
      841 flnrqllvlg evnelyleql qnkhsdttke vemmkaayrk eleknrshvl qqtqrldtsq
      901 krileleshl akkdhllleq kkyledvklq argqlqaaes ryeaqkritq vfeleildly
      961 grlekdgllk kleeekaeaa eaaeerldcc ndgcsdsmvg hneeasghng etktprpssa
     1021 rgssgsrggg gssssssels tpekpphqra gpfssrwett mgeasasipt tvgslpssks
     1081 flgmkarelf rnksesqcde dgmtsslses lktelgkdlg veakiplnld gphpspptpd
     1141 svgqlhimdy nethhehs
//
LOCUS       NP_001398076            1406 aa            linear   PRI 21-NOV-2025
DEFINITION  WD repeat-containing protein 62 isoform 5 [Homo sapiens].
ACCESSION   NP_001398076 XP_011525141
VERSION     NP_001398076.1
DBSOURCE    REFSEQ: accession NM_001411147.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1406)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1406)
  AUTHORS   Aslam,K., Saeed,A., Saeed,H.I., Bashir,R., Abid,H., Akhtar,R.,
            Habib,N., Khan,R., Asif,R., Rafiq,S., Asif,M., Makhdoom,E.U.H.,
            Hussain,M.S., Baig,S.M. and Anjum,I.
  TITLE     Molecular genetics, neuroimaging outcomes, and structural analyses
            of novel and recurrent variants of WDR62 gene in two consanguineous
            Pakistani families with autosomal recessive primary microcephaly
  JOURNAL   Mol Biol Rep 51 (1), 783 (2024)
   PUBMED   38926176
  REMARK    GeneRIF: Molecular genetics, neuroimaging outcomes, and structural
            analyses of novel and recurrent variants of WDR62 gene in two
            consanguineous Pakistani families with autosomal recessive primary
            microcephaly.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1406)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1406)
  AUTHORS   Hao,L., Ma,J., Wu,F., Ma,X., Qian,M., Sheng,W., Yan,T., Tang,N.,
            Jiang,X., Zhang,B., Xiao,D., Qian,Y., Zhang,J., Jiang,N., Zhou,W.,
            Chen,W., Ma,D. and Huang,G.
  TITLE     WDR62 variants contribute to congenital heart disease by inhibiting
            cardiomyocyte proliferation
  JOURNAL   Clin Transl Med 12 (7), e941 (2022)
   PUBMED   35808830
  REMARK    GeneRIF: WDR62 variants contribute to congenital heart disease by
            inhibiting cardiomyocyte proliferation.
REFERENCE   5  (residues 1 to 1406)
  AUTHORS   Wasserman,T., Katsenelson,K., Daniliuc,S., Hasin,T., Choder,M. and
            Aronheim,A.
  TITLE     A novel c-Jun N-terminal kinase (JNK)-binding protein WDR62 is
            recruited to stress granules and mediates a nonclassical JNK
            activation
  JOURNAL   Mol Biol Cell 21 (1), 117-130 (2010)
   PUBMED   19910486
  REMARK    GeneRIF: JNK and WDR62 may regulate the dynamic interplay between
            polysomes stress granule and processing bodies, thereby mediating
            mRNA fate after stress.
REFERENCE   6  (residues 1 to 1406)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   7  (residues 1 to 1406)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1406)
  AUTHORS   Roberts,E., Jackson,A.P., Carradice,A.C., Deeble,V.J., Mannan,J.,
            Rashid,Y., Jafri,H., McHale,D.P., Markham,A.F., Lench,N.J. and
            Woods,C.G.
  TITLE     The second locus for autosomal recessive primary microcephaly
            (MCPH2) maps to chromosome 19q13.1-13.2
  JOURNAL   Eur J Hum Genet 7 (7), 815-820 (1999)
   PUBMED   10573015
REFERENCE   9  (residues 1 to 1406)
  AUTHORS   Verloes,A., Ruaud,L., Drunat,S. and Passemard,S.
  TITLE     WDR62 Primary Microcephaly
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   35188728
REFERENCE   10 (residues 1 to 1406)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AD000813.1 and AC004144.1.
            
            On Aug 22, 2022 this sequence version replaced XP_011525141.1.
            
            Summary: This gene is proposed to play a role in cerebral cortical
            development. Mutations in this gene have been associated with
            microencephaly, cortical malformations, and cognitive disability.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2420198.1,
                                           SRR14038194.2936384.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..1406
                     /product="WD repeat-containing protein 62 isoform 5"
                     /note="microcephaly, primary autosomal recessive 2; WD
                     repeat-containing protein 62"
                     /calculated_mol_wt=152986
     Region          <93..450
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          115..153
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          158..194
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          202..236
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          254..297
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <307..627
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          381..415
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          421..461
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          466..503
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          515..550
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          559..595
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <1053..1296
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1406
                     /gene="WDR62"
                     /gene_synonym="C19orf14; MCPH2"
                     /coded_by="NM_001411147.1:76..4296"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS92604.1"
                     /db_xref="GeneID:284403"
                     /db_xref="HGNC:HGNC:24502"
                     /db_xref="MIM:613583"
ORIGIN      
        1 maavgsggya rndageklps vmagvparrg qsspppappi clrrrtrlst aseetvqnrv
       61 slekvlgita qnssgltcdp gtghvaylag cvvvildpke nkqqhifnta rkslsalafs
      121 pdgkyivtge nghrpavriw dveeknqvae mlghkygvac vafspnmkhi vsmgyqhdmv
      181 lnvwdwkkdi vvasnkvscr vialsfseds syfvtvgnrh vrfwflevst etkvtstvpl
      241 vgrsgilgel hnnifcgvac grgrmagstf cvsysgllcq fnekrvlekw inlkvypefe
      301 dqraclpsgs fltcssdnti rfwnldsspd shwqknifsn tllkvvyven diqhlqdmsh
      361 fpdrgsengt pmdvkagvrv mqvspdgqhl asgdrsgnlr ihelhfmdel vkveahdaev
      421 lcleyskpet gltllasasr drlihvlnve knynleqtld dhsssitaik fagnrdiqmi
      481 scgadksiyf rsaqqgsdgl hfvrthhvae kttlydmdid itqkyvavac qdrnvrvynt
      541 vngkqkkcyk gsqgdegsll kvhvdpsgtf latscsdksi svidfysgec iakmfghsei
      601 itsmkftydc hhlitvsgds cvfiwhlgpe itncmkqhll eidhrqqqqh tndkkrsghp
      661 rqdtyvstps eihslspgeq teddleeece peemlktpsk dsldpdprcl ltngklplwa
      721 krllgdddva dglafhakrs yqphgrwaer agqeplktil daqdldcyft pmkpeslens
      781 ildslepqsl asllsesesp qeagrghpsf lpqqkessea selilyslea evtvtgtdsq
      841 ycrkeveagp gdqqgdsylr vssdspkdqs ppedsgesea dlecsfaaih spapppdpap
      901 rfatslphfp gcagptedel slpegpsvps sslpqtpeqe kflrhhfetl tespcrelfp
      961 aalgdvease aedhffnprl sistqflssl qkasrfthtf ppratqclvk spevklmdrg
     1021 gsqpragtgy aspdrthvla agkaeetlea wrppppclts lascvpassv lptdrnlptp
     1081 tsaptpglaq gvhapstcsy meatassrar isrsislgds egpivatlaq plrrpssvge
     1141 laslgqelqa ittattpsld segqepalrs wgnhearanl rltlssacdg llqppvdtqp
     1201 gvtvpavsfp apspveesal rlhgsafrps lpapespglp ahpsnpqlpe arpgipggta
     1261 slleptsgal gllqgsparw sepwvpveal ppsplelsrv gnilhrlqtt fqealdlyrv
     1321 lvssgqvdtg qqqartelvs tflwihsqle aeclvgtsva paqalpspgp pspptlypla
     1381 spdlqalleh ysellvqavr rkargh
//
LOCUS       NP_001397816             610 aa            linear   PRI 21-NOV-2025
DEFINITION  copine-5 isoform j [Homo sapiens].
ACCESSION   NP_001397816 XP_005249304
VERSION     NP_001397816.1
DBSOURCE    REFSEQ: accession NM_001410887.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Zhu,P., Qian,T., Si,C., Liu,Y., Cui,L., Huang,W., Fu,L., Deng,C.
            and Zeng,T.
  TITLE     High expression of CPNE5 and CPNE9 predicts positive prognosis in
            multiple myeloma
  JOURNAL   Cancer Biomark 31 (1), 77-85 (2021)
   PUBMED   33780365
  REMARK    GeneRIF: High expression of CPNE5 and CPNE9 predicts positive
            prognosis in multiple myeloma.
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Umeda,S., Kanda,M., Koike,M., Tanaka,H., Miwa,T., Tanaka,C.,
            Kobayashi,D., Suenaga,M., Hayashi,M., Yamada,S., Nakayama,G. and
            Kodera,Y.
  TITLE     Copine 5 expression predicts prognosis following curative resection
            of esophageal squamous cell carcinoma
  JOURNAL   Oncol Rep 40 (6), 3772-3780 (2018)
   PUBMED   30272363
  REMARK    GeneRIF: Data revealed that CPNE5 mRNA expression was significantly
            lower in ESCC tissues and cell lines and correlated with
            significantly shorter overall survival. Multivariable analysis
            identified low CPNE5 expression to be an independent prognostic
            factor of OS. Analysis of recurrence patterns revealed that
            significantly more patients with local recurrence expressed lower
            levels of CPNE5 mRNA.
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Wang,K.S., Zuo,L., Pan,Y., Xie,C. and Luo,X.
  TITLE     Genetic variants in the CPNE5 gene are associated with alcohol
            dependence and obesity in Caucasian populations
  JOURNAL   J Psychiatr Res 71, 1-7 (2015)
   PUBMED   26522866
  REMARK    GeneRIF: Results provide the first evidence of genetic variants in
            the CPNE5 gene influencing both alcohol dependence and obesity
REFERENCE   5  (residues 1 to 610)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 610)
  AUTHORS   den Hoed,M., Eijgelsheim,M., Esko,T., Brundel,B.J., Peal,D.S.,
            Evans,D.M., Nolte,I.M., Segre,A.V., Holm,H., Handsaker,R.E.,
            Westra,H.J., Johnson,T., Isaacs,A., Yang,J., Lundby,A., Zhao,J.H.,
            Kim,Y.J., Go,M.J., Almgren,P., Bochud,M., Boucher,G.,
            Cornelis,M.C., Gudbjartsson,D., Hadley,D., van der Harst,P.,
            Hayward,C., den Heijer,M., Igl,W., Jackson,A.U., Kutalik,Z.,
            Luan,J., Kemp,J.P., Kristiansson,K., Ladenvall,C., Lorentzon,M.,
            Montasser,M.E., Njajou,O.T., O'Reilly,P.F., Padmanabhan,S., St
            Pourcain,B., Rankinen,T., Salo,P., Tanaka,T., Timpson,N.J.,
            Vitart,V., Waite,L., Wheeler,W., Zhang,W., Draisma,H.H.,
            Feitosa,M.F., Kerr,K.F., Lind,P.A., Mihailov,E., Onland-Moret,N.C.,
            Song,C., Weedon,M.N., Xie,W., Yengo,L., Absher,D., Albert,C.M.,
            Alonso,A., Arking,D.E., de Bakker,P.I., Balkau,B., Barlassina,C.,
            Benaglio,P., Bis,J.C., Bouatia-Naji,N., Brage,S., Chanock,S.J.,
            Chines,P.S., Chung,M., Darbar,D., Dina,C., Dorr,M., Elliott,P.,
            Felix,S.B., Fischer,K., Fuchsberger,C., de Geus,E.J., Goyette,P.,
            Gudnason,V., Harris,T.B., Hartikainen,A.L., Havulinna,A.S.,
            Heckbert,S.R., Hicks,A.A., Hofman,A., Holewijn,S.,
            Hoogstra-Berends,F., Hottenga,J.J., Jensen,M.K., Johansson,A.,
            Junttila,J., Kaab,S., Kanon,B., Ketkar,S., Khaw,K.T., Knowles,J.W.,
            Kooner,A.S., Kors,J.A., Kumari,M., Milani,L., Laiho,P.,
            Lakatta,E.G., Langenberg,C., Leusink,M., Liu,Y., Luben,R.N.,
            Lunetta,K.L., Lynch,S.N., Markus,M.R., Marques-Vidal,P., Mateo
            Leach,I., McArdle,W.L., McCarroll,S.A., Medland,S.E., Miller,K.A.,
            Montgomery,G.W., Morrison,A.C., Muller-Nurasyid,M., Navarro,P.,
            Nelis,M., O'Connell,J.R., O'Donnell,C.J., Ong,K.K., Newman,A.B.,
            Peters,A., Polasek,O., Pouta,A., Pramstaller,P.P., Psaty,B.M.,
            Rao,D.C., Ring,S.M., Rossin,E.J., Rudan,D., Sanna,S., Scott,R.A.,
            Sehmi,J.S., Sharp,S., Shin,J.T., Singleton,A.B., Smith,A.V.,
            Soranzo,N., Spector,T.D., Stewart,C., Stringham,H.M., Tarasov,K.V.,
            Uitterlinden,A.G., Vandenput,L., Hwang,S.J., Whitfield,J.B.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilson,J.F., Witteman,J.C.,
            Wong,A., Wong,Q., Jamshidi,Y., Zitting,P., Boer,J.M., Boomsma,D.I.,
            Borecki,I.B., van Duijn,C.M., Ekelund,U., Forouhi,N.G., Froguel,P.,
            Hingorani,A., Ingelsson,E., Kivimaki,M., Kronmal,R.A., Kuh,D.,
            Lind,L., Martin,N.G., Oostra,B.A., Pedersen,N.L., Quertermous,T.,
            Rotter,J.I., van der Schouw,Y.T., Verschuren,W.M., Walker,M.,
            Albanes,D., Arnar,D.O., Assimes,T.L., Bandinelli,S., Boehnke,M., de
            Boer,R.A., Bouchard,C., Caulfield,W.L., Chambers,J.C., Curhan,G.,
            Cusi,D., Eriksson,J., Ferrucci,L., van Gilst,W.H., Glorioso,N., de
            Graaf,J., Groop,L., Gyllensten,U., Hsueh,W.C., Hu,F.B.,
            Huikuri,H.V., Hunter,D.J., Iribarren,C., Isomaa,B., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kiemeney,L.A., van der Klauw,M.M.,
            Kooner,J.S., Kraft,P., Iacoviello,L., Lehtimaki,T., Lokki,M.L.,
            Mitchell,B.D., Navis,G., Nieminen,M.S., Ohlsson,C., Poulter,N.R.,
            Qi,L., Raitakari,O.T., Rimm,E.B., Rioux,J.D., Rizzi,F., Rudan,I.,
            Salomaa,V., Sever,P.S., Shields,D.C., Shuldiner,A.R., Sinisalo,J.,
            Stanton,A.V., Stolk,R.P., Strachan,D.P., Tardif,J.C.,
            Thorsteinsdottir,U., Tuomilehto,J., van Veldhuisen,D.J.,
            Virtamo,J., Viikari,J., Vollenweider,P., Waeber,G., Widen,E.,
            Cho,Y.S., Olsen,J.V., Visscher,P.M., Willer,C., Franke,L.,
            Erdmann,J., Thompson,J.R., Pfeufer,A., Sotoodehnia,N.,
            Newton-Cheh,C., Ellinor,P.T., Stricker,B.H., Metspalu,A.,
            Perola,M., Beckmann,J.S., Smith,G.D., Stefansson,K., Wareham,N.J.,
            Munroe,P.B., Sibon,O.C., Milan,D.J., Snieder,H., Samani,N.J. and
            Loos,R.J.
  CONSRTM   Global BPgen Consortium; CARDIoGRAM Consortium; PR GWAS Consortium;
            QRS GWAS Consortium; QT-IGC Consortium; CHARGE-AF Consortium
  TITLE     Identification of heart rate-associated loci and their effects on
            cardiac conduction and rhythm disorders
  JOURNAL   Nat Genet 45 (6), 621-631 (2013)
   PUBMED   23583979
REFERENCE   7  (residues 1 to 610)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   8  (residues 1 to 610)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   9  (residues 1 to 610)
  AUTHORS   Tripodis,N., Mason,R., Humphray,S.J., Davies,A.F., Herberg,J.A.,
            Trowsdale,J., Nizetic,D., Senger,G. and Ragoussis,J.
  TITLE     Physical map of human 6p21.2-6p21.3: region flanking the
            centromeric end of the major histocompatibility complex
  JOURNAL   Genome Res 8 (6), 631-643 (1998)
   PUBMED   9647638
REFERENCE   10 (residues 1 to 610)
  AUTHORS   Creutz,C.E., Tomsig,J.L., Snyder,S.L., Gautier,M.C., Skouri,F.,
            Beisson,J. and Cohen,J.
  TITLE     The copines, a novel class of C2 domain-containing,
            calcium-dependent, phospholipid-binding proteins conserved from
            Paramecium to humans
  JOURNAL   J Biol Chem 273 (3), 1393-1402 (1998)
   PUBMED   9430674
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z85996.1 and KF510949.1.
            
            On Aug 17, 2022 this sequence version replaced XP_005249304.1.
            
            Summary: Calcium-dependent membrane-binding proteins may regulate
            molecular events at the interface of the cell membrane and
            cytoplasm. This gene is one of several genes that encode a
            calcium-dependent protein containing two N-terminal type II C2
            domains and an integrin A domain-like sequence in the C-terminus.
            Several alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. More variants may
            exist, but their full-length natures could not be determined.
            [provided by RefSeq, Sep 2015].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2567748.1,
                                           SRR14038192.3453958.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..610
                     /product="copine-5 isoform j"
                     /note="copine V"
                     /calculated_mol_wt=67380
     Region          23..137
                     /region_name="C2A_Copine"
                     /note="C2 domain first repeat in Copine; cd04048"
                     /db_xref="CDD:176013"
     Site            order(38,44,98,100,110)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176013"
     Region          194..305
                     /region_name="C2B_Copine"
                     /note="C2 domain second repeat in Copine; cd04047"
                     /db_xref="CDD:176012"
     Site            order(209,215,271,273,279)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176012"
     Region          315..571
                     /region_name="vWA_copine_like"
                     /note="VWA Copine: Copines are phospholipid-binding
                     proteins originally identified in paramecium. They are
                     found in human and orthologues have been found in C.
                     elegans and Arabidopsis Thaliana. None have been found in
                     D. Melanogaster or S. Cereviciae; cd01459"
                     /db_xref="CDD:238736"
     Site            order(351,353,355,449,479)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238736"
     CDS             1..610
                     /gene="CPNE5"
                     /gene_synonym="COPN5; CPN5"
                     /coded_by="NM_001410887.1:68..1900"
                     /note="isoform j is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS93904.1"
                     /db_xref="GeneID:57699"
                     /db_xref="HGNC:HGNC:2318"
                     /db_xref="MIM:604209"
ORIGIN      
        1 meqpedmasl sefdslagsi patkveitvs crnlldkdmf sksdplcvmy tqgmenkqwr
       61 efgrtevidn tlnpdfvrkf ivdyffeekq nlrfdlydvd skspdlskhd flgqafctlg
      121 eivgspgsrl ekpltigafs lnsrtgkpmp avsngsglwm eslrttglea sggvpgkkcg
      181 tiilsaeels ncrdvatmqf cankldkkdf fgksdpflvf yrsnedgtft ichktevmkn
      241 tlnpvwqtfs ipvralcngd ydrtikvevy dwdrdgshdf igefttsyre largqsqfni
      301 yevvnpkkkm kkkkyvnsgt vtllsfaves ectfldyikg gtqinftvai dftasngnps
      361 qstslhymsp yqlnayalal tavgeiiqhy dsdkmfpalg fgaklppdgr vshefplngn
      421 qenpsccgid gileayhrsl rtvqlygptn fapvvthvar naaavqdgsq ysvlliitdg
      481 visdmaqtke aivnaaklpm siiivgvgqa efdamveldg ddvrissrgk laerdivqfv
      541 pfrdyvdrtg nhvlsmarla rdvlaeipdq lvsymkaqgi rprpppaapt hspsqspart
      601 ppasplhthi
//
LOCUS       NP_001407091             554 aa            linear   PRI 21-NOV-2025
DEFINITION  protein enabled homolog isoform i [Homo sapiens].
ACCESSION   NP_001407091 XP_047280921 XP_054193589
VERSION     NP_001407091.1
DBSOURCE    REFSEQ: accession NM_001420162.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Yin,X., Wang,J., Shen,Z., Jia,Q., Bian,Y., Yang,Z., Liu,Y., Li,Y.
            and Zhang,H.
  TITLE     ENAH transcriptionally activated by YY1 promotes growth and
            invasion of laryngocarcinoma cells through PI3K/AKT signaling
  JOURNAL   Eur J Pharmacol 983, 176991 (2024)
   PUBMED   39265883
  REMARK    GeneRIF: ENAH transcriptionally activated by YY1 promotes growth
            and invasion of laryngocarcinoma cells through PI3K/AKT signaling.
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Cui,H., Liang,X., Zhu,Y., Elayah,S.A., Qi,H., Xie,L., Guo,Z.,
            Siya,F., Ming,Y., Yuxin,G., Tu,J. and Na,S.
  TITLE     Mena as a key enhancer factor of EMT to promote metastasis of human
            tongue squamous cell carcinoma
  JOURNAL   Oral Dis 30 (4), 2084-2096 (2024)
   PUBMED   37203597
  REMARK    GeneRIF: Mena as a key enhancer factor of EMT to promote metastasis
            of human tongue squamous cell carcinoma.
REFERENCE   4  (residues 1 to 554)
  AUTHORS   He,L., She,C., Jiang,S., Qi,Z., Deng,Z., Ji,L., Cui,Y. and Wu,J.
  TITLE     Mammalian enabled protein enhances tamoxifen sensitivity of the
            hormone receptor-positive breast cancer patients by suppressing the
            AKT signaling pathway
  JOURNAL   Biol Direct 19 (1), 21 (2024)
   PUBMED   38459605
  REMARK    GeneRIF: Mammalian enabled protein enhances tamoxifen sensitivity
            of the hormone receptor-positive breast cancer patients by
            suppressing the AKT signaling pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 554)
  AUTHORS   Liu,R., Miao,K., Gao,L. and He,L.
  TITLE     TRIM67 interacts with ENAH to regulate the apoptosis and autophagy
            of lung cancer cells
  JOURNAL   Gen Physiol Biophys 43 (2), 163-173 (2024)
   PUBMED   38477606
  REMARK    GeneRIF: TRIM67 interacts with ENAH to regulate the apoptosis and
            autophagy of lung cancer cells.
REFERENCE   6  (residues 1 to 554)
  AUTHORS   Urbanelli,L., Massini,C., Emiliani,C., Orlacchio,A., Bernardi,G.
            and Orlacchio,A.
  TITLE     Characterization of human Enah gene
  JOURNAL   Biochim Biophys Acta 1759 (1-2), 99-107 (2006)
   PUBMED   16494957
REFERENCE   7  (residues 1 to 554)
  AUTHORS   Mammoto,A., Sasaki,T., Asakura,T., Hotta,I., Imamura,H.,
            Takahashi,K., Matsuura,Y., Shirao,T. and Takai,Y.
  TITLE     Interactions of drebrin and gephyrin with profilin
  JOURNAL   Biochem Biophys Res Commun 243 (1), 86-89 (1998)
   PUBMED   9473484
REFERENCE   8  (residues 1 to 554)
  AUTHORS   Ermekova,K.S., Zambrano,N., Linn,H., Minopoli,G., Gertler,F.,
            Russo,T. and Sudol,M.
  TITLE     The WW domain of neural protein FE65 interacts with proline-rich
            motifs in Mena, the mammalian homolog of Drosophila enabled
  JOURNAL   J Biol Chem 272 (52), 32869-32877 (1997)
   PUBMED   9407065
REFERENCE   9  (residues 1 to 554)
  AUTHORS   Niebuhr,K., Ebel,F., Frank,R., Reinhard,M., Domann,E., Carl,U.D.,
            Walter,U., Gertler,F.B., Wehland,J. and Chakraborty,T.
  TITLE     A novel proline-rich motif present in ActA of Listeria
            monocytogenes and cytoskeletal proteins is the ligand for the EVH1
            domain, a protein module present in the Ena/VASP family
  JOURNAL   EMBO J 16 (17), 5433-5444 (1997)
   PUBMED   9312002
REFERENCE   10 (residues 1 to 554)
  AUTHORS   Sazuka,T., Tomooka,Y., Kathju,S., Ikawa,Y., Noda,M. and Kumar,S.
  TITLE     Identification of a developmentally regulated gene in the mouse
            central nervous system which encodes a novel proline rich protein
  JOURNAL   Biochim Biophys Acta 1132 (3), 240-248 (1992)
   PUBMED   1420303
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL591380.21, AL356216.13 and
            AC092811.2.
            
            On or before Apr 26, 2023 this sequence version replaced
            XP_047280921.1, XP_054193589.1.
            
            Summary: This gene encodes a member of the enabled/
            vasodilator-stimulated phosphoprotein. Members of this gene family
            are involved in actin-based motility. This protein is involved in
            regulating the assembly of actin filaments and modulates cell
            adhesion and motility. Alternate splice variants of this gene have
            been correlated with tumor invasiveness in certain tissues and
            these variants may serve as prognostic markers. A pseudogene of
            this gene is found on chromosome 3. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3491081.1,
                                           SRR18074969.948553.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.12"
     Protein         1..554
                     /product="protein enabled homolog isoform i"
                     /note="protein enabled homolog; Mena delta 11a"
                     /calculated_mol_wt=62804
     Region          5..112
                     /region_name="EVH1_Ena_VASP-like"
                     /note="Enabled/VASP family EVH1 domain; cd01207"
                     /db_xref="CDD:269918"
     Site            order(16,23,69,71,77,79,81)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269918"
     Region          348..374
                     /region_name="WH2_hVASP-like"
                     /note="Wiskott-Aldrich syndrome protein (WASP)-homology
                     domain 2 (WH2) of human Vasodilator-stimulated
                     phosphoprotein and related proteins; cd22185"
                     /db_xref="CDD:409225"
     Site            order(355..356,358..359,362,364..368)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409225"
     Region          364..367
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409225"
     Region          516..550
                     /region_name="VASP_tetra"
                     /note="VASP tetramerization domain; pfam08776"
                     /db_xref="CDD:462599"
     CDS             1..554
                     /gene="ENAH"
                     /gene_synonym="ENA; MENA; NDPP1"
                     /coded_by="NM_001420162.1:434..2098"
                     /note="isoform i is encoded by transcript variant 9"
                     /db_xref="GeneID:55740"
                     /db_xref="HGNC:HGNC:18271"
                     /db_xref="MIM:609061"
ORIGIN      
        1 mseqsicqar aavmvyddan kkwvpaggst gfsrvhiyhh tgnntfrvvg rkiqdhqvvi
       61 ncaipkglky nqatqtfhqw rdarqvygln fgskedanvf asammhalev lnsqetgptl
      121 prqnsqlpaq vqngpsqeel eiqrrqlqeq qrqkelerer lerermerer lererlerer
      181 lererleqeq lererqerer qerlerqerl erqerlerqe rldrerqerq ererlerler
      241 erqererqeq lereqlewer errissagiv lgplappppp plppgpaqas valppppgpp
      301 pppplpstgp pppppppplp nqvppppppp papplpasgf flasmsednr pltglaaaia
      361 gaklrkvsrm edtsfpsggn aigvnsassk tdtgrgngpl plggsglmee msallarrrr
      421 iaekgstiet eqkedkgeds epvtskasst stpeptrkpw ertntmngsk spvisrrdsp
      481 rknqivfdnr sydslhrpks tplsqpsang vqtegldydr lkqdildemr keltklkeel
      541 idairqelsk snta
//
LOCUS       NP_001425133             718 aa            linear   PRI 21-NOV-2025
DEFINITION  serine/threonine-protein kinase tousled-like 2 isoform B [Homo
            sapiens].
ACCESSION   NP_001425133 XP_016879542 XP_054170774
VERSION     NP_001425133.1
DBSOURCE    REFSEQ: accession NM_001438204.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 718)
  AUTHORS   Liang,B., Yin,J.J., Zhang,S.N., Zhang,C., Hu,Z.L. and Wang,Y.
  TITLE     [Effect of TLK2 Expression Regulated by MiR-21 on Proliferation and
            Apoptosis of Acute Myeloid Leukemia Cells]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 32 (3), 658-662 (2024)
   PUBMED   38926950
  REMARK    GeneRIF: [Effect of TLK2 Expression Regulated by MiR-21 on
            Proliferation and Apoptosis of Acute Myeloid Leukemia Cells].
REFERENCE   3  (residues 1 to 718)
  AUTHORS   Ronald,S., Sunavala-Dossabhoy,G., Adams,L., Williams,B. and De
            Benedetti,A.
  TITLE     The expression of Tousled kinases in CaP cell lines and its
            relation to radiation response and DSB repair
  JOURNAL   Prostate 71 (13), 1367-1373 (2011)
   PUBMED   21647934
  REMARK    GeneRIF: TLKs appear to be intimately linked to the pattern of
            resistance to DNA damage, and specifically double-strand breaks.
REFERENCE   4  (residues 1 to 718)
  AUTHORS   Couch,F.J., Wang,X., Bamlet,W.R., de Andrade,M., Petersen,G.M. and
            McWilliams,R.R.
  TITLE     Association of mitotic regulation pathway polymorphisms with
            pancreatic cancer risk and outcome
  JOURNAL   Cancer Epidemiol Biomarkers Prev 19 (1), 251-257 (2010)
   PUBMED   20056645
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   5  (residues 1 to 718)
  AUTHORS   Pilyugin,M., Demmers,J., Verrijzer,C.P., Karch,F. and Moshkin,Y.M.
  TITLE     Phosphorylation-mediated control of histone chaperone ASF1 levels
            by Tousled-like kinases
  JOURNAL   PLoS One 4 (12), e8328 (2009)
   PUBMED   20016786
  REMARK    GeneRIF: ASF1 cellular levels are tightly controlled by distinct
            pathways and provide a molecular mechanism for post-translational
            regulation of dASF1 and hASF1a by TLK kinases.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 718)
  AUTHORS   Groth,A., Lukas,J., Nigg,E.A., Sillje,H.H., Wernstedt,C., Bartek,J.
            and Hansen,K.
  TITLE     Human Tousled like kinases are targeted by an ATM- and
            Chk1-dependent DNA damage checkpoint
  JOURNAL   EMBO J 22 (7), 1676-1687 (2003)
   PUBMED   12660173
REFERENCE   7  (residues 1 to 718)
  AUTHORS   Sillje,H.H. and Nigg,E.A.
  TITLE     Identification of human Asf1 chromatin assembly factors as
            substrates of Tousled-like kinases
  JOURNAL   Curr Biol 11 (13), 1068-1073 (2001)
   PUBMED   11470414
REFERENCE   8  (residues 1 to 718)
  AUTHORS   Sillje,H.H., Takahashi,K., Tanaka,K., Van Houwe,G. and Nigg,E.A.
  TITLE     Mammalian homologues of the plant Tousled gene code for
            cell-cycle-regulated kinases with maximal activities linked to
            ongoing DNA replication
  JOURNAL   EMBO J 18 (20), 5691-5702 (1999)
   PUBMED   10523312
REFERENCE   9  (residues 1 to 718)
  AUTHORS   Zhang,S., Xing,H. and Muslin,A.J.
  TITLE     Nuclear localization of protein kinase U-alpha is regulated by
            14-3-3
  JOURNAL   J Biol Chem 274 (35), 24865-24872 (1999)
   PUBMED   10455159
REFERENCE   10 (residues 1 to 718)
  AUTHORS   Yamakawa,A., Kameoka,Y., Hashimoto,K., Yoshitake,Y., Nishikawa,K.,
            Tanihara,K. and Date,T.
  TITLE     cDNA cloning and chromosomal mapping of genes encoding novel
            protein kinases termed PKU-alpha and PKU-beta, which have nuclear
            localization signal
  JOURNAL   Gene 202 (1-2), 193-201 (1997)
   PUBMED   9427565
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008026.7 and AC080038.5.
            
            On or before Apr 21, 2025 this sequence version replaced
            XP_016879542.1, XP_054170774.1.
            
            Summary: This gene encodes a nuclear serine/threonine kinase that
            was first identified in Arabidopsis. The encoded protein is thought
            to function in the regulation of chromatin assembly in the S phase
            of the cell cycle by regulating the levels of a histone H3/H4
            chaperone. This protein is associated with double-strand break
            repair of DNA damage caused by radiation. Pseudogenes of this gene
            are present on chromosomes 10 and 17. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1278022.1,
                                           SRR14372080.681752.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.2"
     Protein         1..718
                     /product="serine/threonine-protein kinase tousled-like 2
                     isoform B"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase tousled-like 2"
                     /calculated_mol_wt=82217
     Region          139..>378
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          401..709
                     /region_name="STKc_TLK2"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Tousled-Like Kinase 2; cd14041"
                     /db_xref="CDD:270943"
     Site            order(414..418,422,435,437,473,490..493,497,499,538,540,
                     542..543,545,559,562,585..588)
                     /site_type="active"
                     /db_xref="CDD:270943"
     Site            order(414..418,422,435,437,473,490..493,497,538,540,
                     542..543,545,559)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270943"
     Site            order(418,497,499,538,540,542,562,585..588)
                     /site_type="other"
                     /note="polypeptide substrate binding site"
                     /db_xref="CDD:270943"
     Site            order(558..564,585..588)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270943"
     CDS             1..718
                     /gene="TLK2"
                     /gene_synonym="HsHPK; MRD57; PKU-ALPHA"
                     /coded_by="NM_001438204.1:274..2430"
                     /note="isoform B is encoded by transcript variant L"
                     /db_xref="GeneID:11011"
                     /db_xref="HGNC:HGNC:11842"
                     /db_xref="MIM:608439"
ORIGIN      
        1 mmeelhsldp rrqellearf tgvgvskgpl nsessnqslc svgslsdkev etpekkqndq
       61 rnrkrkaepy etsqgkgtpr ghkisdyfer rveqplygld gsaakeatee qsalptlmsv
      121 mlakprldte qlaqrgaglc ftfvsaqqns psstgsgnte hscssqkqis iqhrqtqsdl
      181 tiekisalen sknsdlekke griddllran cdlrrqideq qkmlekyker lnrcvtmskk
      241 lliekskqek macrdksmqd rlrlghfttv rhgasfteqw tdgyafqnli kqqerinsqr
      301 eeierqrkml akrkppamgq appatneqkq rksktngaen etltlaeyhe qeeifklrlg
      361 hlkkeeaeiq aelerlervr nlhirelkri hnednsqfkd hptlndryll lhllgrggfs
      421 evykafdlte qryvavkihq lnknwrdekk enyhkhacre yrihkeldhp rivklydyfs
      481 ldtdsfctvl eycegndldf ylkqhklmse kearsiimqi vnalkylnei kppiihydlk
      541 pgnillvngt acgeikitdf glskimddds ynsvdgmelt sqgagtywyl ppecfvvgke
      601 ppkisnkvdv wsvgvifyqc lygrkpfghn qsqqdilqen tilkatevqf ppkpvvtpea
      661 kafirrclay rkedridvqq lacdpyllph irksvstssp agaaiastsg asnnsssn
//
LOCUS       NP_001394263             284 aa            linear   PRI 21-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 33 [Homo sapiens].
ACCESSION   NP_001394263
VERSION     NP_001394263.1
DBSOURCE    REFSEQ: accession NM_001407334.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.4143558.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..284
                     /product="tropomyosin alpha-1 chain isoform 33"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=32676
     Region          48..282
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..284
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001407334.1:84..938"
                     /note="isoform 33 is encoded by transcript variant 33"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle ediaakekll rvsederdrv
       61 leelhkaeds llaaeeaaak aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegqv rqleeqlrim dqtlkalmaa edkysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledel yaqklkykai seeldhalnd mtsm
//
LOCUS       NP_001428087             345 aa            linear   PRI 21-NOV-2025
DEFINITION  urokinase-type plasminogen activator isoform 3 [Homo sapiens].
ACCESSION   NP_001428087
VERSION     NP_001428087.1
DBSOURCE    REFSEQ: accession NM_001441158.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Li,D., Ding,C., Huang,F., Chang,M., Lu,Z., Li,G., Li,Y., Gao,H. and
            Sun,F.
  TITLE     Bioinformatics Analysis of the Expression and Prognostic Value of
            PLAU Gene in Wilms' Tumor
  JOURNAL   Anticancer Res 44 (9), 3829-3842 (2024)
   PUBMED   39197889
  REMARK    GeneRIF: Bioinformatics Analysis of the Expression and Prognostic
            Value of PLAU Gene in Wilms' Tumor.
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Guo,J., Wang,H., Huang,C., Lai,C., Shang,W., Luo,S. and Chen,L.
  TITLE     PLAU, transcriptionally negatively regulated by GATA6, promotes
            lung squamous carcinoma cell proliferation and migration
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (5), 119744 (2024)
   PUBMED   38702016
  REMARK    GeneRIF: PLAU, transcriptionally negatively regulated by GATA6,
            promotes lung squamous carcinoma cell proliferation and migration.
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Cui,X., Sun,H., Liu,X., Bai,Y., Bai,Y., Cui,Y., Wang,B., Zhang,S.
            and Li,X.
  TITLE     PLAU promotes cell proliferation and migration of head and neck
            cancer via STAT3 signaling pathway
  JOURNAL   Exp Cell Res 438 (2), 114056 (2024)
   PUBMED   38663475
  REMARK    GeneRIF: PLAU promotes cell proliferation and migration of head and
            neck cancer via STAT3 signaling pathway.
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Cetinsoy,O., Anyanwu,I., Krishnanand,H., Natarajan,G.,
            Ramachandran,N., Thomas,A. and Brookes,K.J.
  TITLE     Gene Association Study of the Urokinase Plasminogen Activator and
            Its Receptor Gene in Alzheimer's Disease
  JOURNAL   J Alzheimers Dis 99 (1), 241-250 (2024)
   PUBMED   38669542
  REMARK    GeneRIF: Gene Association Study of the Urokinase Plasminogen
            Activator and Its Receptor Gene in Alzheimer's Disease.
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Mekkawy,A.H., Pourgholami,M.H. and Morris,D.L.
  TITLE     Involvement of urokinase-type plasminogen activator system in
            cancer: an overview
  JOURNAL   Med Res Rev 34 (5), 918-956 (2014)
   PUBMED   24549574
  REMARK    Review article
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Naldini,L., Tamagnone,L., Vigna,E., Sachs,M., Hartmann,G.,
            Birchmeier,W., Daikuhara,Y., Tsubouchi,H., Blasi,F. and
            Comoglio,P.M.
  TITLE     Extracellular proteolytic cleavage by urokinase is required for
            activation of hepatocyte growth factor/scatter factor
  JOURNAL   EMBO J 11 (13), 4825-4833 (1992)
   PUBMED   1334458
REFERENCE   8  (residues 1 to 345)
  AUTHORS   Li,X., Smith,R.A. and Dobson,C.M.
  TITLE     Sequential 1H NMR assignments and secondary structure of the
            kringle domain from urokinase
  JOURNAL   Biochemistry 31 (40), 9562-9571 (1992)
   PUBMED   1327118
REFERENCE   9  (residues 1 to 345)
  AUTHORS   Stephens,R.W., Aumailley,M., Timpl,R., Reisberg,T., Tapiovaara,H.,
            Myohanen,H., Murphy-Ullrich,J. and Vaheri,A.
  TITLE     Urokinase binding to laminin-nidogen. Structural requirements and
            interactions with heparin
  JOURNAL   Eur J Biochem 207 (3), 937-942 (1992)
   PUBMED   1499567
REFERENCE   10 (residues 1 to 345)
  AUTHORS   Moroi,M. and Aoki,N.
  TITLE     Isolation and characterization of alpha2-plasmin inhibitor from
            human plasma. A novel proteinase inhibitor which inhibits
            activator-induced clot lysis
  JOURNAL   J Biol Chem 251 (19), 5956-5965 (1976)
   PUBMED   134998
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22.
            
            Summary: This gene encodes a secreted serine protease that converts
            plasminogen to plasmin. The encoded preproprotein is
            proteolytically processed to generate A and B polypeptide chains.
            These chains associate via a single disulfide bond to form the
            catalytically inactive high molecular weight urokinase-type
            plasminogen activator (HMW-uPA). HMW-uPA can be further processed
            into the catalytically active low molecular weight urokinase-type
            plasminogen activator (LMW-uPA). This low molecular weight form
            does not bind to the urokinase-type plasminogen activator receptor.
            Mutations in this gene may be associated with Quebec platelet
            disorder and late-onset Alzheimer's disease. Alternative splicing
            results in multiple transcript variants, at least one of which
            encodes an isoform that is proteolytically processed. [provided by
            RefSeq, Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1289477.1,
                                           SRR14038192.4206976.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..345
                     /product="urokinase-type plasminogen activator isoform 3"
                     /EC_number="3.4.21.73"
                     /note="plasminogen activator, urinary; U-plasminogen
                     activator; urokinase-type plasminogen activator"
                     /calculated_mol_wt=38910
     Region          <1..66
                     /region_name="KR"
                     /note="Kringle domain; Kringle domains are believed to
                     play a role in binding mediators, such as peptides, other
                     proteins, membranes, or phospholipids. They are autonomous
                     structural domains, found in a varying number of copies,
                     in blood clotting and...; cd00108"
                     /db_xref="CDD:238056"
     Site            order(8,18,46,48,57)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:238056"
     Region          93..336
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            93
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(138,189,290)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            order(284,309,311)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..345
                     /gene="PLAU"
                     /gene_synonym="ATF; BDPLT5; QPD; u-PA; UPA; URK"
                     /coded_by="NM_001441158.1:690..1727"
                     /note="isoform 3 is encoded by transcript variant 8"
                     /db_xref="GeneID:5328"
                     /db_xref="HGNC:HGNC:9052"
                     /db_xref="MIM:191840"
ORIGIN      
        1 mgrpclpwns atvlqqtyha hrsdalqlgl gkhnycrnpd nrrrpwcyvq vglkllvqec
       61 mvhdcadgkk pssppeelkf qcgqktlrpr fkiiggeftt ienqpwfaai yrrhrggsvt
      121 yvcggslisp cwvisathcf idypkkedyi vylgrsrlns ntqgemkfev enlilhkdys
      181 adtlahhndi allkirskeg rcaqpsrtiq ticlpsmynd pqfgtsceit gfgkenstdy
      241 lypeqlkmtv vklishrecq qphyygsevt tkmlcaadpq wktdscqgds ggplvcslqg
      301 rmtltgivsw grgcalkdkp gvytrvshfl pwirshtkee nglal
//
LOCUS       NP_001427337             765 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_001427337
VERSION     NP_001427337.1
DBSOURCE    REFSEQ: accession NM_001440408.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 765)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 765)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 765)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 765)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 765)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 765)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 765)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 765)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 765)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3, AP004147.3 and
            AP001929.5.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.272160.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..765
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     2 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=83674
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..402
                     /region_name="PBP1_iGluR_Kainate_KA1_2"
                     /note="N-terminal leucine-isoleucine-valine binding
                     protein (LIVBP)-like domain of the KA1 and KA2 subunits of
                     Kainate receptor; cd06394"
                     /db_xref="CDD:380616"
     Site            order(75..77,81,113,166,169,173,176,179..180,190..193)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380616"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            286
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            323
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            408
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Region          415..763
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            415
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            479
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            546..566
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16099.2)"
     Site            624..644
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16099.2)"
     Site            736
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     CDS             1..765
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440408.1:191..2488"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 10"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk aaelgmvsay
      241 ytyiftnlef slqrmdslvd drvnilgfsi fnqshaffqe faqslnqswq encdhvpftg
      301 palssallfd avyavvtavq elnrsqeigv kplscgsaqi wqhgtslmny lrmveleglt
      361 ghiefnskgq rsnyalkilq ftrngfrqig qwhvaeglsm dshlyasnis dtlfnttlvv
      421 ttilenpylm lkgnhqemeg ndryegfcvd mlkelaeilr fnykirlvgd gvygvpeang
      481 twtgmvgeli arkadlavag ltitaerekv idfskpfmtl gisilyrvhm grkpgyfsfl
      541 dpfspgvwlf mllaylavsc vlflvarltp yewysphpca qgrcnllvnq yslgnslwfp
      601 vggfmqqgst iapralstrc vsgvwwaftl iiissytanl aafltvqrmd vpiesvddla
      661 dqtaieygti hggssmtffq nsryqtyqrm wnymyskqps vfvksteegi arvlnsnyaf
      721 llestmneyy rqrncnltqi gglldtkgyg igmpvgmrer nslfg
//
LOCUS       NP_001427573             206 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol N-acetylglucosaminyltransferase subunit H
            isoform 4 [Homo sapiens].
ACCESSION   NP_001427573 XP_016876860 XP_054232199
VERSION     NP_001427573.1
DBSOURCE    REFSEQ: accession NM_001440644.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Wegner,J., Zillinger,T., Schlee-Guimaraes,T.M., Bartok,E. and
            Schlee,M.
  TITLE     An epigenetic GPI anchor defect impairs TLR4 signaling in the B
            cell transdifferentiation model for primary human monocytes BLaER1
  JOURNAL   Sci Rep 11 (1), 14983 (2021)
   PUBMED   34294787
  REMARK    GeneRIF: An epigenetic GPI anchor defect impairs TLR4 signaling in
            the B cell transdifferentiation model for primary human monocytes
            BLaER1.
            Erratum:[Sci Rep. 2021 Aug 30;11(1):17661. doi:
            10.1038/s41598-021-97277-5. PMID: 34462520]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Tremblay-Laganiere,C., Kaiyrzhanov,R., Maroofian,R., Nguyen,T.T.M.,
            Salayev,K., Chilton,I.T., Chung,W.K., Madden,J.A., Phornphutkul,C.,
            Agrawal,P.B., Houlden,H. and Campeau,P.M.
  TITLE     PIGH deficiency can be associated with severe neurodevelopmental
            and skeletal manifestations
  JOURNAL   Clin Genet 99 (2), 313-317 (2021)
   PUBMED   33156547
  REMARK    GeneRIF: PIGH deficiency can be associated with severe
            neurodevelopmental and skeletal manifestations.
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Loeff,F.C., Rijs,K., van Egmond,E.H.M., Zoutman,W.H., Qiao,X.,
            Kroes,W.G.M., Veld,S.A.J., Griffioen,M., Vermeer,M.H., Neefjes,J.,
            Frederik Falkenburg,J.H., Halkes,C.J.M. and Jedema,I.
  TITLE     Loss of the GPI-anchor in B-lymphoblastic leukemia by epigenetic
            downregulation of PIGH expression
  JOURNAL   Am J Hematol 94 (1), 93-102 (2019)
   PUBMED   30370942
  REMARK    GeneRIF: The GPI-anchor negative phenotype results from loss of
            mRNA expression of the PIGH gene, which is involved in the first
            step of GPI-anchor synthesis. Loss of PIGH mRNA expression within
            these B-ALL cells follows epigenetic silencing rather than gene
            mutation or deletion.
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Watanabe,R., Murakami,Y., Marmor,M.D., Inoue,N., Maeda,Y., Hino,J.,
            Kangawa,K., Julius,M. and Kinoshita,T.
  TITLE     Initial enzyme for glycosylphosphatidylinositol biosynthesis
            requires PIG-P and is regulated by DPM2
  JOURNAL   EMBO J 19 (16), 4402-4411 (2000)
   PUBMED   10944123
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Watanabe,R., Inoue,N., Westfall,B., Taron,C.H., Orlean,P.,
            Takeda,J. and Kinoshita,T.
  TITLE     The first step of glycosylphosphatidylinositol biosynthesis is
            mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1
  JOURNAL   EMBO J 17 (4), 877-885 (1998)
   PUBMED   9463366
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Watanabe,R., Kinoshita,T., Masaki,R., Yamamoto,A., Takeda,J. and
            Inoue,N.
  TITLE     PIG-A and PIG-H, which participate in glycosylphosphatidylinositol
            anchor biosynthesis, form a protein complex in the endoplasmic
            reticulum
  JOURNAL   J Biol Chem 271 (43), 26868-26875 (1996)
   PUBMED   8900170
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Ware,R.E., Howard,T.A., Kamitani,T., Chang,H.-M., Yeh,E.T.H. and
            Seldin,M.F.
  TITLE     Chromosomal assignment of genes involved in
            glycosylphosphatidylinositol anchor biosynthesis: implications for
            the pathogenesis of paroxysmal nocturnal hemoglobinuria
  JOURNAL   Blood 83 (12), 3753-3757 (1994)
   PUBMED   8204896
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Kamitani,T., Chang,H.M., Rollins,C., Waneck,G.L. and Yeh,E.T.
  TITLE     Correction of the class H defect in glycosylphosphatidylinositol
            anchor biosynthesis in Ltk- cells by a human cDNA clone
  JOURNAL   J Biol Chem 268 (28), 20733-20736 (1993)
   PUBMED   8407896
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL132640.4.
            
            On or before May 23, 2025 this sequence version replaced
            XP_016876860.1, XP_054232199.1.
            
            Summary: This gene encodes an endoplasmic reticulum associated
            protein that is involved in glycosylphosphatidylinositol
            (GPI)-anchor biosynthesis. The GPI anchor is a glycolipid found on
            many blood cells and which serves to anchor proteins to the cell
            surface. The protein encoded by this gene is a subunit of the GPI
            N-acetylglucosaminyl (GlcNAc) transferase that transfers GlcNAc to
            phosphatidylinositol (PI) on the cytoplasmic side of the
            endoplasmic reticulum. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2625936.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.1"
     Protein         1..206
                     /product="phosphatidylinositol
                     N-acetylglucosaminyltransferase subunit H isoform 4"
                     /EC_number="2.4.1.198"
                     /note="phosphatidylinositol
                     N-acetylglucosaminyltransferase subunit H;
                     phosphatidylinositol-glycan biosynthesis, class H protein"
                     /calculated_mol_wt=23089
     Region          89..157
                     /region_name="PIG-H"
                     /note="GPI-GlcNAc transferase complex, PIG-H component;
                     pfam10181"
                     /db_xref="CDD:462983"
     CDS             1..206
                     /gene="PIGH"
                     /gene_synonym="GPI-H"
                     /coded_by="NM_001440644.1:66..686"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:5283"
                     /db_xref="HGNC:HGNC:8964"
                     /db_xref="MIM:600154"
ORIGIN      
        1 medersfsdi cggrlalqrr yyspscrefc lscprlslrs ltavtctvwl aayglftlce
       61 nsmilsaaif itllgllgyl hfvkidqetl liidslgiqm tssyasgkes ttfiemgkvk
      121 divineaiym kviyylcill kdpvephgis qvvpvfqrqs ltlsprlecs dnhhslqppp
      181 prlkksscls llrtwdyrvp spgwta
//
LOCUS       NP_001397810            1343 aa            linear   PRI 21-NOV-2025
DEFINITION  protein cordon-bleu isoform h [Homo sapiens].
ACCESSION   NP_001397810 XP_011513537
VERSION     NP_001397810.1
DBSOURCE    REFSEQ: accession NM_001410881.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1343)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1343)
  AUTHORS   Abdul Majeed,S., Dunzendorfer,H., Weiner,J., Heiker,J.T., Kiess,W.,
            Korner,A. and Landgraf,K.
  TITLE     COBL, MKX and MYOC Are Potential Regulators of Brown Adipose Tissue
            Development Associated with Obesity-Related Metabolic Dysfunction
            in Children
  JOURNAL   Int J Mol Sci 24 (4), 3085 (2023)
   PUBMED   36834493
  REMARK    GeneRIF: COBL, MKX and MYOC Are Potential Regulators of Brown
            Adipose Tissue Development Associated with Obesity-Related
            Metabolic Dysfunction in Children.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1343)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1343)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1343)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 1343)
  AUTHORS   Husson,C., Renault,L., Didry,D., Pantaloni,D. and Carlier,M.F.
  TITLE     Cordon-Bleu uses WH2 domains as multifunctional dynamizers of actin
            filament assembly
  JOURNAL   Mol Cell 43 (3), 464-477 (2011)
   PUBMED   21816349
  REMARK    GeneRIF: Cordon-Bleu works as a dynamizer of actin assembly by
            combining many properties of profilin with weak filament nucleating
            and powerful filament severing activities and sequestration of
            ADP-actin, which generate oscillatory polymerization kinetics.
REFERENCE   7  (residues 1 to 1343)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 1343)
  AUTHORS   de Krom,M., Staal,W.G., Ophoff,R.A., Hendriks,J., Buitelaar,J.,
            Franke,B., de Jonge,M.V., Bolton,P., Collier,D., Curran,S., van
            Engeland,H. and van Ree,J.M.
  TITLE     A common variant in DRD3 receptor is associated with autism
            spectrum disorder
  JOURNAL   Biol Psychiatry 65 (7), 625-630 (2009)
   PUBMED   19058789
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1343)
  AUTHORS   Carroll,E.A., Gerrelli,D., Gasca,S., Berg,E., Beier,D.R., Copp,A.J.
            and Klingensmith,J.
  TITLE     Cordon-bleu is a conserved gene involved in neural tube formation
  JOURNAL   Dev Biol 262 (1), 16-31 (2003)
   PUBMED   14512015
REFERENCE   10 (residues 1 to 1343)
  AUTHORS   Gasca,S., Hill,D.P., Klingensmith,J. and Rossant,J.
  TITLE     Characterization of a gene trap insertion into a novel gene,
            cordon-bleu, expressed in axial structures of the gastrulating
            mouse embryo
  JOURNAL   Dev Genet 17 (2), 141-154 (1995)
   PUBMED   7586755
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005535.2, AC012372.4 and
            AC004414.1.
            
            On Aug 17, 2022 this sequence version replaced XP_011513537.1.
            
            Summary: This gene encodes a protein that contains WH2 domains
            (WASP, Wiskott-Aldrich syndrome protein, homology domain-2) that
            interact with actin. The encoded actin regulator protein is
            required for growth and assembly of brush border microvilli that
            play a role in maintaining intestinal homeostasis. A similar
            protein in mouse functions in midbrain neural tube closure. A
            pseudogene of this gene is located on chromosome X. [provided by
            RefSeq, Oct 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3195203.1,
                                           SRR14038193.2168128.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1343
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12.1"
     Protein         1..1343
                     /product="protein cordon-bleu isoform h"
                     /note="protein cordon-bleu"
                     /calculated_mol_wt=143797
     Region          152..230
                     /region_name="Cobl"
                     /note="Cordon-bleu ubiquitin-like domain; pfam09469"
                     /db_xref="CDD:462810"
     Region          1181..1213
                     /region_name="WH2_Wa_Cobl"
                     /note="first Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wa) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21799"
                     /db_xref="CDD:409197"
     Site            order(1192,1194..1196,1198..1200,1202,1206,1208..1212)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409197"
     Region          1208..1211
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409197"
     Region          1227..1270
                     /region_name="WH2_Wb_Cobl"
                     /note="second Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wb) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21800"
                     /db_xref="CDD:409198"
     Site            order(1227,1229..1242,1248..1251,1253,1255..1256,
                     1258..1259,1262,1266..1270)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409198"
     Region          1248..1251
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409198"
     Region          1315..1340
                     /region_name="WH2_Wc_Cobl"
                     /note="third Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wc) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21801"
                     /db_xref="CDD:409199"
     Site            order(1319..1320,1322..1324,1326..1328,1336..1339)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409199"
     Region          1336..1339
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409199"
     CDS             1..1343
                     /gene="COBL"
                     /coded_by="NM_001410881.1:177..4208"
                     /note="isoform h is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS94104.1"
                     /db_xref="GeneID:23242"
                     /db_xref="HGNC:HGNC:22199"
                     /db_xref="MIM:610317"
ORIGIN      
        1 mdaprasaak pptgrkmkar appppgkaat lhvhsdqkpp hdgalgsqqn lvrmkealra
       61 stmdvtvvlp sglekrsvln gshammdllv elclqnhlnp shhaleirss etqqplsfkp
      121 ntligtlnvh tvflkekvpe ekvkpgppkv peksvrlvvn ylrtqkavvr vspevplqni
      181 lpvicakcev spehvvllrd niageelels kslnelgike lyawdnrret frksslgnde
      241 tdkekkkflg ffkvnkrsns kaeqlvlsga dsdedtsraa pgrglngclt tpnspsmhsr
      301 sltlgpslsl gsisgvsvks emkkrrappp pgsgppvqdk asekvslgsq idlqkkkrra
      361 pappppqppp psplipnrte dkeenrkstm gggrqvpqkp prgtargppq lvlpppppyp
      421 ppdtdvvepl sfpgegagse asdpipklsl plgsgshcsp dgapqvlsea eetvsvgscf
      481 asedttedsg vmsspsdivs ldsqqdsmky kdkwatdqed csdqdlagtp dlgpqksplw
      541 ekngsenshl rtekavtasn deedlliage frktlaelde dleemedsye tdtssltssi
      601 hgasnhcpqd amiphgdtda ipvtfigevs ddpvdsglfs nrnnnagsfd segvasrrds
      661 laplqaehsq phekareevp alhpashdvg kgirvalsni skdgnlmeta prvtsfasnl
      721 htdnlnakvk dkvygcadge rtqatervns qpvnekdsnd knaalaptsw hqrgqnpgks
      781 yrlkhgltty kiippksemr cydrdvslst gaikidelgn lvsphatgir iislsssvpe
      841 aesqpigkvr efwrcnsvek hlgrpsessa rgppstpvpt qtqnpesrlq adpkpispqq
      901 ksahhegrnp lgegrnqppt mgmghvrvpa ahttevtflk pqrrtssqyv asaiakriga
      961 pkvhadvvrp hgyaekgyag kapvlaappv tvkddrtssp hsetqgwkdg aqwpcvtppn
     1021 nhgedlavga pprgevigph rklstqdrpa aihrsscfsl vqssqrdrvs vgqscgfsgk
     1081 qstssqeass aseprrapdg tdpppphtsd tqacsrelvn gsvrapghge pshppggsgt
     1141 eshilleree kpsvfstdgn etdsiwppsi fgpkkkfkpv vqrpvpkdts lhsalmeaih
     1201 saggkdrlrk taehtgegrp aklsyteaeg ersallaair ghsgtcslrk vassaseelq
     1261 sfrdaalsaq gsesplledl gllsppaipp pppppsqals aprtasrfst gtlsntadar
     1321 qalmdairsg tgaarlrkvp llv
//
LOCUS       NP_001394758            1196 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 14 precursor
            [Homo sapiens].
ACCESSION   NP_001394758
VERSION     NP_001394758.1
DBSOURCE    REFSEQ: accession NM_001407829.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1196)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1196)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1196)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1196)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1196)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1196)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1196)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1196)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1196)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1196)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.900042.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1196
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 14 precursor"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=134702
     Region          261..290
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          296..323
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          432..704
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          831..1196
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1196
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407829.1:26..3616"
                     /note="isoform 14 precursor is encoded by transcript
                     variant 14"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 msalcwgrga aglkralrpc grpglpgkeg taggvcgprr sssaspqeqd qdrrkdwghv
       61 ellevlqarv rqlqaesvse vvvnrvdvar lpecgsgdgs lqpprkvqmg akdatpvpcg
      121 rwakilekdk rtqqmrmqrl kaklqmpfqs gefkaltrrl qveprllskq magcledctr
      181 qapespweeq larllqeapg klsldveqap sgqhsqaqls gqqqrllaff kcclltdqlp
      241 lahhllvvhh gqrqkrkllt ldmynavmlg warqgafkel vyvlfmvkda gltpdllsya
      301 aalqcmgrqd qdagtiercl eqmsqeglkl qalftavlls eedratvlka vhkvkptfsl
      361 ppqlpppvnt skllrdvyak dgrvsypklh lplktlqclf ekqlhmelas rvcvvsvekp
      421 tlpskevkha rktlktlrdq wekalcralr etknrlerev yegrfslypf lcllderevv
      481 rmllqvlqal paqgesfttl arelsartfs rhvvqrqrvs gqvqalqnhy rkylcllasd
      541 aevpepclpr qyweelgape alreqpwplp vqmelgklla emlvqatqmp csldkphrss
      601 rlvpvlyhvy sfrnvqqigi lkphpayvql lekaaeptlt feavdvpmlc pplpwtsphs
      661 gafllsptkl mrtvegatqh qelletcppt alhgaldalt qlgncawrvn grvldlvlql
      721 fqakgcpqlg vpappseapq ppeahlphsa aparkaelrr elahcqkvar emhslraeal
      781 yrlslaqhlr drvfwlphnm dfrgrtypcp phfnhlgsdv arallefaqg rplgphgldw
      841 lkihlvnltg lkkreplrkr lafaeevmdd ildsadqplt dgscnglqhy aalgrdsvga
      901 asvnlepsdv pqdvysgvaa qvevfrrqda qrgmrvaqvl egfitrkvvk qtvmtvvygv
      961 tryggrlqie krlrelsdfp qefvweashy lvrqvfkslq emfsgtraiq hwltesarli
     1021 shmgsvvewv tplgvpviqp yrldskvkqi gggiqsityt hngdisrkpn trkqkngfpp
     1081 nfihsldssh mmltalhcyr spplchrkgl tfvsvhdcyw thaadvsvmn qvcreqfvrl
     1141 hsepilqdls rflvkrfcse pqkileasql ketlqavpkp gafdleqvkr styffs
//
LOCUS       NP_001389637            1116 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 17 [Homo sapiens].
ACCESSION   NP_001389637
VERSION     NP_001389637.1
DBSOURCE    REFSEQ: accession NM_001402708.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1116)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1116)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1116)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1116)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1116)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1116)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1116)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1116)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1116)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1116)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4257005.1,
                                           SRR14038197.2083428.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1116
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1116
                     /product="kinectin isoform 17"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=128571
     Region          <142..>400
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          296..1056
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1116
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402708.1:178..3528"
                     /note="isoform 17 is encoded by transcript variant 31"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mvpskrqeal plhqetkqes gsgkkkassk kqktenvfvd eplihattyi plmdnadssp
       61 vvdkrevidl lkpdqvegiq ksgtkklkte tdkenaevkf kdfllslktm mfsedealcv
      121 vdllkeksgv iqdalkkssk gelttlihql qekdkllaav kedaaatkdr ckqltqemmt
      181 ekersnvvit rmkdrigtle kehnvfqnki hvsyqetqqm qmkfqqvreq meaeiahlkq
      241 engilrdavs nttnqleskq saelnklrqd yarlvnelte ktgklqqeev qkknaeqaat
      301 qlkvqlqeae rrweevqsyi rkrtaeheaa qqdlqskfva kenevqslhs kltdtlvskq
      361 qleqrlmqlm eseqkrvnke eslqmqvqdi leqnealkaq iqqfhsqiaa qtsasvlaee
      421 lhkviaekdk qikqtedsla serdrltske eelkdiqnmn fllkaevqkl qalaneqaaa
      481 ahelekmqqs vyvkddkirl leeqlqheis nkmeefkiln dqnkalksev qklqtlvseq
      541 pnkdvveqme kciqekdekl ktveelletg liqvatkeee lnairtenss ltkevqdlka
      601 kqndqvsfas lveelkkvih ekdgkiksve elleaellkv ankektvqdl kqeikalkee
      661 ignvqlekaq qlsitskvqe lqnllkgkee qmntmkavle ekekdlantg kwlqdlqeen
      721 eslkahvqev aqhnlkeass asqfeeleiv lkekenelkr leamlkeres dlssktqllq
      781 dvqdenklfk sqieqlkqqn yqqassfpph eellkviser ekeisglwne ldslkdaveh
      841 qrkknnerqq qveaveleak evlkklfpkv svpsnlsyge wlhgfekkak ecmagtsgse
      901 evkvlehklk eademhtllq lecekyksvl aetegilqkl qrsveqeenk wkvkvdeshk
      961 tikqmqssft sseqelerlr senkdienlr rerehlemel ekaemersty vtevrelkaq
     1021 lnetltklrt eqnerqkvag dlhkaqqsle liqskivkaa gdttviensd vspetessek
     1081 etmsvslnqt vtqlqqllqa vnqqltkeke hyqvle
//
LOCUS       NP_001394734            1237 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_001394734 XP_005259637
VERSION     NP_001394734.1
DBSOURCE    REFSEQ: accession NM_001407805.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1237)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1237)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1237)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1237)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1237)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1237)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1237)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1237)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1237)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1237)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            On Jun 7, 2022 this sequence version replaced XP_005259637.3.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4158822.1,
                                           SRR14038193.3358640.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1237
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1237
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 1 precursor"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=135321
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O00411.2)"
                     /calculated_mol_wt=4109
     Region          18..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          95..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          261..290
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          296..323
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          432..704
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          731..750
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00411.2)"
     Region          831..1237
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1237
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407805.1:26..3739"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 msalcwgrga aglkralrpc grpglpgkeg taggvcgprr sssaspqeqd qdrrkdwghv
       61 ellevlqarv rqlqaesvse vvvnrvdvar lpecgsgdgs lqpprkvqmg akdatpvpcg
      121 rwakilekdk rtqqmrmqrl kaklqmpfqs gefkaltrrl qveprllskq magcledctr
      181 qapespweeq larllqeapg klsldveqap sgqhsqaqls gqqqrllaff kcclltdqlp
      241 lahhllvvhh gqrqkrkllt ldmynavmlg warqgafkel vyvlfmvkda gltpdllsya
      301 aalqcmgrqd qdagtiercl eqmsqeglkl qalftavlls eedratvlka vhkvkptfsl
      361 ppqlpppvnt skllrdvyak dgrvsypklh lplktlqclf ekqlhmelas rvcvvsvekp
      421 tlpskevkha rktlktlrdq wekalcralr etknrlerev yegrfslypf lcllderevv
      481 rmllqvlqal paqgesfttl arelsartfs rhvvqrqrvs gqvqalqnhy rkylcllasd
      541 aevpepclpr qyweelgape alreqpwplp vqmelgklla emlvqatqmp csldkphrss
      601 rlvpvlyhvy sfrnvqqigi lkphpayvql lekaaeptlt feavdvpmlc pplpwtsphs
      661 gafllsptkl mrtvegatqh qelletcppt alhgaldalt qlgncawrvn grvldlvlql
      721 fqakgcpqlg vpappseapq ppeahlphsa aparkaelrr elahcqkvar emhslraeal
      781 yrlslaqhlr drvfwlphnm dfrgrtypcp phfnhlgsdv arallefaqg rplgphgldw
      841 lkihlvnltg lkkreplrkr lafaeevmdd ildsadqplt grkwwmgaee pwqtlaccme
      901 vanavrasdp aayvshlpvh qdgscnglqh yaalgrdsvg aasvnlepsd vpqdvysgva
      961 aqvevfrrqd aqrgmrvaqv legfitrkvv kqtvmtvvyg vtryggrlqi ekrlrelsdf
     1021 pqefvweash ylvrqvfksl qemfsgtrai qhwltesarl ishmgsvvew vtplgvpviq
     1081 pyrldskvkq igggiqsity thngdisrkp ntrkqkngfp pnfihsldss hmmltalhcy
     1141 rspplchrkg ltfvsvhdcy wthaadvsvm nqvcreqfvr lhsepilqdl srflvkrfcs
     1201 epqkileasq lketlqavpk pgafdleqvk rstyffs
//
LOCUS       NP_001398075            1440 aa            linear   PRI 21-NOV-2025
DEFINITION  WD repeat-containing protein 62 isoform 4 [Homo sapiens].
ACCESSION   NP_001398075 XP_011525140
VERSION     NP_001398075.1
DBSOURCE    REFSEQ: accession NM_001411146.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1440)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1440)
  AUTHORS   Aslam,K., Saeed,A., Saeed,H.I., Bashir,R., Abid,H., Akhtar,R.,
            Habib,N., Khan,R., Asif,R., Rafiq,S., Asif,M., Makhdoom,E.U.H.,
            Hussain,M.S., Baig,S.M. and Anjum,I.
  TITLE     Molecular genetics, neuroimaging outcomes, and structural analyses
            of novel and recurrent variants of WDR62 gene in two consanguineous
            Pakistani families with autosomal recessive primary microcephaly
  JOURNAL   Mol Biol Rep 51 (1), 783 (2024)
   PUBMED   38926176
  REMARK    GeneRIF: Molecular genetics, neuroimaging outcomes, and structural
            analyses of novel and recurrent variants of WDR62 gene in two
            consanguineous Pakistani families with autosomal recessive primary
            microcephaly.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1440)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1440)
  AUTHORS   Hao,L., Ma,J., Wu,F., Ma,X., Qian,M., Sheng,W., Yan,T., Tang,N.,
            Jiang,X., Zhang,B., Xiao,D., Qian,Y., Zhang,J., Jiang,N., Zhou,W.,
            Chen,W., Ma,D. and Huang,G.
  TITLE     WDR62 variants contribute to congenital heart disease by inhibiting
            cardiomyocyte proliferation
  JOURNAL   Clin Transl Med 12 (7), e941 (2022)
   PUBMED   35808830
  REMARK    GeneRIF: WDR62 variants contribute to congenital heart disease by
            inhibiting cardiomyocyte proliferation.
REFERENCE   5  (residues 1 to 1440)
  AUTHORS   Wasserman,T., Katsenelson,K., Daniliuc,S., Hasin,T., Choder,M. and
            Aronheim,A.
  TITLE     A novel c-Jun N-terminal kinase (JNK)-binding protein WDR62 is
            recruited to stress granules and mediates a nonclassical JNK
            activation
  JOURNAL   Mol Biol Cell 21 (1), 117-130 (2010)
   PUBMED   19910486
  REMARK    GeneRIF: JNK and WDR62 may regulate the dynamic interplay between
            polysomes stress granule and processing bodies, thereby mediating
            mRNA fate after stress.
REFERENCE   6  (residues 1 to 1440)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   7  (residues 1 to 1440)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1440)
  AUTHORS   Roberts,E., Jackson,A.P., Carradice,A.C., Deeble,V.J., Mannan,J.,
            Rashid,Y., Jafri,H., McHale,D.P., Markham,A.F., Lench,N.J. and
            Woods,C.G.
  TITLE     The second locus for autosomal recessive primary microcephaly
            (MCPH2) maps to chromosome 19q13.1-13.2
  JOURNAL   Eur J Hum Genet 7 (7), 815-820 (1999)
   PUBMED   10573015
REFERENCE   9  (residues 1 to 1440)
  AUTHORS   Verloes,A., Ruaud,L., Drunat,S. and Passemard,S.
  TITLE     WDR62 Primary Microcephaly
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   35188728
REFERENCE   10 (residues 1 to 1440)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AD000813.1 and AC004144.1.
            
            On Aug 23, 2022 this sequence version replaced XP_011525140.1.
            
            Summary: This gene is proposed to play a role in cerebral cortical
            development. Mutations in this gene have been associated with
            microencephaly, cortical malformations, and cognitive disability.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3027069.1,
                                           SRR18074967.3986074.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1440
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..1440
                     /product="WD repeat-containing protein 62 isoform 4"
                     /note="microcephaly, primary autosomal recessive 2; WD
                     repeat-containing protein 62"
                     /calculated_mol_wt=157532
     Region          42..567
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          114..153
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          159..197
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          201..239
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          270..332
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          350..399
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <364..744
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          407..442
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          498..532
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          538..578
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          583..620
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          632..667
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          676..712
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <980..1330
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1440
                     /gene="WDR62"
                     /gene_synonym="C19orf14; MCPH2"
                     /coded_by="NM_001411146.1:76..4398"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS92602.1"
                     /db_xref="GeneID:284403"
                     /db_xref="HGNC:HGNC:24502"
                     /db_xref="MIM:613583"
ORIGIN      
        1 maavgsggya rndageklps vmagvparrg qsspppappi clrrrtrlst aseetvqnrv
       61 slekvlgita qnssgltcdp gtghvaylag cvvvildpke nkqqhifnta rkslsalafs
      121 pdgkyivtge nghrpavriw dveeknqvae mlghkygvac vafspnmkhi vsmgyqhdmv
      181 lnvwdwkkdi vvasnkvscr vialsfseds syfvtvgnrh vrfwflevst etkvtstvpl
      241 vgrsgilgel hnnifcgvac grgrmagstf cvsysgllcq fnekrvlekw inlkvslssc
      301 lcvsqelifc gctdgivrif qahslhylan lpkphylgvd vaqglepsfl fhrkaeavyp
      361 dtvaltfdpi hqwlscvykd hsiyiwdvkd inrvgkvwse lfhssyvwnv evypefedqr
      421 aclpsgsflt cssdntirfw nldsspdshw qknifsntll kvvyvendiq hlqdmshfpd
      481 rgsengtpmd vkagvrvmqv spdgqhlasg drsgnlrihe lhfmdelvkv eahdaevlcl
      541 eyskpetglt llasasrdrl ihvlnvekny nleqtlddhs ssitaikfag nrdiqmiscg
      601 adksiyfrsa qqgsdglhfv rthhvaektt lydmdiditq kyvavacqdr nvrvyntvng
      661 kqkkcykgsq gdegsllkvh vdpsgtflat scsdksisvi dfysgeciak mfghseiits
      721 mkftydchhl itvsgdscvf iwhlgpeitn cmkqhlleid hrqqqqhtnd kkrsghprqd
      781 tyvstpseih slspgeqted dleeecepee mlktpskdsl dpdprclltn gklplwakrl
      841 lgdddvadgl afhakrsyqp hgrwaeragq eplktildaq dldcyftpmk peslensild
      901 slepqslasl lsesespqea grghpsflpq qkesseasel ilysleaevt vtgtdsqycr
      961 keveagpgdq qgdsylrvss dspkdqsppe elfpaalgdv easeaedhff nprlsistqf
     1021 lsslqkasrf thtfppratq clvkspevkl mdrggsqpra gtgyaspdrt hvlaagkaee
     1081 tleawrpppp cltslascvp assvlptdrn lptptsaptp glaqgvhaps tcsymeatas
     1141 srarisrsis lgdsegpiva tlaqplrrps svgelaslgq elqaittatt psldsegqep
     1201 alrswgnhea ranlrltlss acdgllqppv dtqpgvtvpa vsfpapspve esalrlhgsa
     1261 frpslpapes pglpahpsnp qlpearpgip ggtasllept sgalgllqgs parwsepwvp
     1321 vealppsple lsrvgnilhr lqttfqeald lyrvlvssgq vdtgqqqart elvstflwih
     1381 sqleaeclvg tsvapaqalp spgppspptl yplaspdlqa llehysellv qavrrkargh
//
LOCUS       NP_001397828             410 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial carrier homolog 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001397828 XP_005249036
VERSION     NP_001397828.1
DBSOURCE    REFSEQ: accession NM_001410899.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Xie,L., Shu,Y., Ye,M. and Li,Y.
  TITLE     Identification of MTCH1 as a novel prognostic indicator and
            therapeutic target in hepatocellular carcinoma
  JOURNAL   Pathol Res Pract 259, 155358 (2024)
   PUBMED   38820930
  REMARK    GeneRIF: Identification of MTCH1 as a novel prognostic indicator
            and therapeutic target in hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Wang,X., Ji,Y., Qi,J., Zhou,S., Wan,S., Fan,C., Gu,Z., An,P.,
            Luo,Y. and Luo,J.
  TITLE     Mitochondrial carrier 1 (MTCH1) governs ferroptosis by triggering
            the FoxO1-GPX4 axis-mediated retrograde signaling in cervical
            cancer cells
  JOURNAL   Cell Death Dis 14 (8), 508 (2023)
   PUBMED   37550282
  REMARK    GeneRIF: Mitochondrial carrier 1 (MTCH1) governs ferroptosis by
            triggering the FoxO1-GPX4 axis-mediated retrograde signaling in
            cervical cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Guna,A., Stevens,T.A., Inglis,A.J., Replogle,J.M., Esantsi,T.K.,
            Muthukumar,G., Shaffer,K.C.L., Wang,M.L., Pogson,A.N., Jones,J.J.,
            Lomenick,B., Chou,T.F., Weissman,J.S. and Voorhees,R.M.
  TITLE     MTCH2 is a mitochondrial outer membrane protein insertase
  JOURNAL   Science 378 (6617), 317-322 (2022)
   PUBMED   36264797
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Lamarca,V., Marzo,I., Sanz-Clemente,A. and Carrodeguas,J.A.
  TITLE     Exposure of any of two proapoptotic domains of presenilin
            1-associated protein/mitochondrial carrier homolog 1 on the surface
            of mitochondria is sufficient for induction of apoptosis in a
            Bax/Bak-independent manner
  JOURNAL   Eur J Cell Biol 87 (5), 325-334 (2008)
   PUBMED   18375015
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Mao,G., Tan,J., Gao,W., Shi,Y., Cui,M.Z. and Xu,X.
  TITLE     Both the N-terminal fragment and the protein-protein interaction
            domain (PDZ domain) are required for the pro-apoptotic activity of
            presenilin-associated protein PSAP
  JOURNAL   Biochim Biophys Acta 1780 (4), 696-708 (2008)
   PUBMED   18291114
  REMARK    GeneRIF: Data show that all PSAP splicing isoforms are localized in
            the mitochondria and are pro-apoptotic.
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Lamarca,V., Sanz-Clemente,A., Perez-Pe,R., Martinez-Lorenzo,M.J.,
            Halaihel,N., Muniesa,P. and Carrodeguas,J.A.
  TITLE     Two isoforms of PSAP/MTCH1 share two proapoptotic domains and
            multiple internal signals for import into the mitochondrial outer
            membrane
  JOURNAL   Am J Physiol Cell Physiol 293 (4), C1347-C1361 (2007)
   PUBMED   17670888
  REMARK    GeneRIF: PSAP has two proapoptotic isoforms generated by
            alternative splicing, and both proteins are imported into the
            mitochondrial outer membrane using multiple internal targeting
            signals, and both contain two proapoptotic domains.
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Xu,X., Shi,Y.C., Gao,W., Mao,G., Zhao,G., Agrawal,S., Chisolm,G.M.,
            Sui,D. and Cui,M.Z.
  TITLE     The novel presenilin-1-associated protein is a proapoptotic
            mitochondrial protein
  JOURNAL   J Biol Chem 277 (50), 48913-48922 (2002)
   PUBMED   12377771
  REMARK    GeneRIF: mitochondrial localization and proapoptotic activity of
            PSAP suggest that it is an important regulator of apoptosis
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Xu,X., Shi,Yc., Wu,X., Gambetti,P., Sui,D. and Cui,M.Z.
  TITLE     Identification of a novel PSD-95/Dlg/ZO-1 (PDZ)-like protein
            interacting with the C terminus of presenilin-1
  JOURNAL   J Biol Chem 274 (46), 32543-32546 (1999)
   PUBMED   10551805
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL122034.29.
            
            On Aug 17, 2022 this sequence version replaced XP_005249036.1.
            
            Summary: This gene encodes a member of the mitochondrial carrier
            family. The encoded protein is localized to the mitochondrion inner
            membrane and induces apoptosis independent of the proapoptotic
            proteins Bax and Bak. Pseudogenes on chromosomes 6 and 11 have been
            identified for this gene. Alternatively spliced transcript variants
            encoding multiple isoforms have been observed. [provided by RefSeq,
            Oct 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4305698.1,
                                           SRR11853567.25585.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..410
                     /product="mitochondrial carrier homolog 1 isoform 4"
                     /note="presenilin-associated protein; cell
                     proliferation-inducing protein 60; mitochondrial carrier
                     homolog 1; solute carrier family 25, member 49"
                     /calculated_mol_wt=44544
     Region          76..173
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Region          206..>264
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     CDS             1..410
                     /gene="MTCH1"
                     /gene_synonym="CGI-64; PIG60; PSAP; SLC25A49"
                     /coded_by="NM_001410899.1:334..1566"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS93906.1"
                     /db_xref="GeneID:23787"
                     /db_xref="HGNC:HGNC:17586"
                     /db_xref="MIM:610449"
ORIGIN      
        1 mgasdpevap warggaagma gagagagarg gaaagveara rdpppahrah prhprpaaqp
       61 sarrmdggsg glgsgdnapt tealfvalga gvtalshpll yvklliqvgh epmpptlgtn
      121 vlgrkvlylp sfftyakyiv qvdgkiglfr glsprlmsna lstvtrgsmk kvfppdeieq
      181 vsnkddmkts lkkvvketsy emmmqcvsrm lahplhvism rcmvqfvgre akysgvlssi
      241 gkifkeegll gffvgliphl lgdvvflwgc nllahfinay lvddsfsqal airsytkfvm
      301 giavsmltyp fllvgdlmav nncglqaglp pyspvfkswi hcwkylsvqv skhwtaeafp
      361 vlcyilqlkw fcgcfiackd kwfhgiqyce eilgiykafk fssyiiseri
//
LOCUS       NP_001428098             687 aa            linear   PRI 21-NOV-2025
DEFINITION  PHD finger protein 21A isoform f [Homo sapiens].
ACCESSION   NP_001428098 XP_016873378 XP_054225042
VERSION     NP_001428098.1
DBSOURCE    REFSEQ: accession NM_001441169.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Mustafa,S., Abbas,S., Mahmood,A., Khan,A.Z., Zeb,S., Khan,A. and
            Umair,M.
  TITLE     A novel de novo variant in the PHF21A causes craniofacial
            abnormalities, intellectual disability and skeletal manifestations
  JOURNAL   Clin Genet 104 (1), 142-144 (2023)
   PUBMED   36843358
  REMARK    GeneRIF: A novel de novo variant in the PHF21A causes craniofacial
            abnormalities, intellectual disability and skeletal manifestations.
REFERENCE   3  (residues 1 to 687)
  AUTHORS   Huang,J.Q., Ji,L.C., Jing,Q.A., He,Y.C., Ma,Y.Y. and Tong,X.M.
  TITLE     PHF21A expression as a biomarker of hepatocellular carcinoma
            progression and prognosis
  JOURNAL   Neoplasma 69 (6), 1349-1358 (2022)
   PUBMED   36305691
  REMARK    GeneRIF: PHF21A expression as a biomarker of hepatocellular
            carcinoma progression and prognosis.
REFERENCE   4  (residues 1 to 687)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 687)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 687)
  AUTHORS   Hailesellasse Sene,K., Porter,C.J., Palidwor,G., Perez-Iratxeta,C.,
            Muro,E.M., Campbell,P.A., Rudnicki,M.A. and Andrade-Navarro,M.A.
  TITLE     Gene function in early mouse embryonic stem cell differentiation
  JOURNAL   BMC Genomics 8, 85 (2007)
   PUBMED   17394647
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 687)
  AUTHORS   Shi,Y.J., Matson,C., Lan,F., Iwase,S., Baba,T. and Shi,Y.
  TITLE     Regulation of LSD1 histone demethylase activity by its associated
            factors
  JOURNAL   Mol Cell 19 (6), 857-864 (2005)
   PUBMED   16140033
REFERENCE   8  (residues 1 to 687)
  AUTHORS   Iwase,S., Januma,A., Miyamoto,K., Shono,N., Honda,A., Yanagisawa,J.
            and Baba,T.
  TITLE     Characterization of BHC80 in BRAF-HDAC complex, involved in
            neuron-specific gene repression
  JOURNAL   Biochem Biophys Res Commun 322 (2), 601-608 (2004)
   PUBMED   15325272
  REMARK    GeneRIF: Presumably serves as a scaffold protein in BHC in neuronal
            as well as non-neuronal cells. Possible role in spermatogenesis.
REFERENCE   9  (residues 1 to 687)
  AUTHORS   Hakimi,M.A., Dong,Y., Lane,W.S., Speicher,D.W. and Shiekhattar,R.
  TITLE     A candidate X-linked mental retardation gene is a component of a
            new family of histone deacetylase-containing complexes
  JOURNAL   J Biol Chem 278 (9), 7234-7239 (2003)
   PUBMED   12493763
REFERENCE   10 (residues 1 to 687)
  AUTHORS   Hakimi,M.A., Bochar,D.A., Chenoweth,J., Lane,W.S., Mandel,G. and
            Shiekhattar,R.
  TITLE     A core-BRAF35 complex containing histone deacetylase mediates
            repression of neuronal-specific genes
  JOURNAL   Proc Natl Acad Sci U S A 99 (11), 7420-7425 (2002)
   PUBMED   12032298
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC024475.15 and AC068385.9.
            
            On or before Jun 5, 2025 this sequence version replaced
            XP_016873378.1, XP_054225042.1.
            
            Summary: The PHF21A gene encodes BHC80, a component of a BRAF35
            (MIM 605535)/histone deacetylase (HDAC; see MIM 601241) complex
            (BHC) that mediates repression of neuron-specific genes through the
            cis-regulatory element known as repressor element-1 (RE1) or neural
            restrictive silencer (NRS) (Hakimi et al., 2002 [PubMed
            12032298]).[supplied by OMIM, Nov 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.890020.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..687
                     /product="PHD finger protein 21A isoform f"
                     /note="BRAF35/HDAC2 complex (80 kDa); BHC80a; BRAF35-HDAC
                     complex protein BHC80"
                     /calculated_mol_wt=75573
     Region          89..125
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          <118..325
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     Region          325..370
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          <381..543
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          447..470
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96BD5.1)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          493..687
                     /region_name="Required for transcriptional repression"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     Region          497..539
                     /region_name="PHD_PHF21A"
                     /note="PHD finger found in PHD finger protein 21A
                     (PHF21A); cd15523"
                     /db_xref="CDD:276998"
     Site            order(497,504..509,529..532,534)
                     /site_type="other"
                     /note="histone H3 binding site [polypeptide binding]"
                     /db_xref="CDD:276998"
     Region          646..687
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BD5.1)"
     CDS             1..687
                     /gene="PHF21A"
                     /gene_synonym="BHC80; BM-006; IDDBCS; NEDMS"
                     /coded_by="NM_001441169.1:757..2820"
                     /note="isoform f is encoded by transcript variant 15"
                     /db_xref="GeneID:51317"
                     /db_xref="HGNC:HGNC:24156"
                     /db_xref="MIM:608325"
ORIGIN      
        1 melqtlqeal kveiqvhqkl vaqmkqdpqi fflsnqnadl kkqlhelqak italsekqkr
       61 vveqlrknli vkqeqpdkfq iqplpqsenk lqtaqqqplq qlqqqqqyhh hhaqqsaaas
      121 pnltasqtvt tasmittktl plvlkaatat mpasvvgqrp tiamvtains qkavlstdvq
      181 ntpvnlqtss kvtgpgaeav qivakntvtl qvqatppqpi kvpqfipppr ltprpnflpq
      241 vrpkpvaqnn ipiapapppm laapqliqrp vmltkftptt lptsqnsihp vrvvngqtat
      301 iaktfpmaql tsiviatpgt rlagpqtvql skpslekqtv kshtetdekq tesrtitppa
      361 apkpkreenp qklafmvslg lvthdhleei qskrqerkrr ttanpvysga vfeperkksa
      421 vtylnstmhp gtrkrgrppk ynavlgfgal tptspqsshp dspenektet tftfpapvqp
      481 vslpsptstd gdihedfcsv crksgqllmc dtcsrvyhld cldpplktip kgmwicprcq
      541 dqmlkkeeai pwpgtlaivh syiaykaake eekqkllkws sdlkqereql eqkvkqlsns
      601 iskcmemknt ilarqkemhs slekvkqlir lihgidlskp vdseatvgai sngpdctppa
      661 naatstpaps pssqsctanc nqgeetk
//
LOCUS       NP_001400249             210 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 16 [Homo sapiens].
ACCESSION   NP_001400249
VERSION     NP_001400249.1
DBSOURCE    REFSEQ: accession NM_001413320.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 210)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 210)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 210)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 210)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 210)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.311000.1,
                                           SRR1803614.381406.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1970526 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..210
                     /product="RNA-binding Raly-like protein isoform 16"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=23250
     Region          28..110
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     CDS             1..210
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413320.1:329..961"
                     /note="isoform 16 is encoded by transcript variant 46"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mskrrrlkqg epimtgktqt snvtnkndpk sinsrvfign lntaivkkvd ieaifskygk
       61 ivgcsvhkgy afvqymserh araavagena rviagqpldi nmagepkpyr pkpgnkrpls
      121 alyrleskep flsvggyvfd ydyyrddfyn rlfdyhgrvp pppraviplk rprvavtttr
      181 rgkgvfsmkg gsrstasgst gskfstdkvi
//
LOCUS       NP_001393545            1043 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 5 [Homo sapiens].
ACCESSION   NP_001393545
VERSION     NP_001393545.1
DBSOURCE    REFSEQ: accession NM_001406616.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1043)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1043)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1043)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1043)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1043)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1043)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1043)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3238481.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1043
                     /product="hamartin isoform 5"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=116145
     Region          16..598
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          <587..>839
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..1043
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406616.1:673..3804"
                     /note="isoform 5 is encoded by transcript variant 30"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 mdtdvvvltt gvlvlitmlp mipqsgkqhl ldffdifgrl sswclkkpgh vaevylvhlh
       61 asvyalfhrl ygmypcnfvs flrshysmke nletfeevvk pmmehvrihp elvtgskdhe
      121 ldprrwkrle thdvviecak isldpteasy edgysvshqi sarfphrsad vttspyadtq
      181 nsygcatstp ystsrlmlln mpgqlpqtls spstrlitep pqatlwspsm vcgmttppts
      241 pgnvppdlsh pyskvfgtta ggkgtplgtp atspppaplc hsddyvhisl pqatvtpprk
      301 eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed siekdkeeaa
      361 isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv npeplhssld
      421 klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp trvgfgsgqp
      481 ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr liqqgadahs
      541 kelnklplps ksvdwthfgg sppsdeirtl rdqllllhnq llyerfkrqq halrnrrllr
      601 kvikaaalee hnaamkdqlk lqekdiqmwk vslqkeqary nqlqeqrdtm vtklhsqirq
      661 lqhdreefyn qsqelqtkle dcrnmiaelr ielkkannkv chtelllsqv sqklsnsesv
      721 qqqmeflnrq llvlgevnel yleqlqnkhs dttkevemmk aayrkelekn rshvlqqtqr
      781 ldtsqkrile leshlakkdh llleqkkyle dvklqargql qaaesryeaq kritqvfele
      841 ildlygrlek dgllkkleee kaeaaeaaee rldccndgcs dsmvghneea sghngetktp
      901 rpssargssg srggggssss sselstpekp phqragpfss rwettmgeas asipttvgsl
      961 pssksflgmk arelfrnkse sqcdedgmts slseslktel gkdlgveaki plnldgphps
     1021 pptpdsvgql himdynethh ehs
//
LOCUS       NP_001396237            2405 aa            linear   PRI 21-NOV-2025
DEFINITION  histone-lysine N-methyltransferase, H3 lysine-36 specific isoform a
            [Homo sapiens].
ACCESSION   NP_001396237
VERSION     NP_001396237.1
DBSOURCE    REFSEQ: accession NM_001409308.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2405)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2405)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   3  (residues 1 to 2405)
  AUTHORS   Conteduca,G., Cangelosi,D., Baldo,C., Arado,A., Testa,B.,
            Wagner,R.T., Robertson,K.D., Dequiedt,F., Fitzsimmons,L.,
            Malacarne,M., Filaci,G. and Coviello,D.A.
  TITLE     Impact of NSD1 Alternative Transcripts in Actin Filament Formation
            and Cellular Division Pathways in Fibroblasts
  JOURNAL   Genes (Basel) 15 (9), 1117 (2024)
   PUBMED   39336709
  REMARK    GeneRIF: Impact of NSD1 Alternative Transcripts in Actin Filament
            Formation and Cellular Division Pathways in Fibroblasts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2405)
  AUTHORS   Ren,Z., Yue,L., Hu,H.Y., Hou,X.L., Chen,W.Q., Tan,Y., Dong,Z. and
            Zhang,J.
  TITLE     Identification of Novel NSD1 variations in four Pediatric cases
            with sotos Syndrome
  JOURNAL   BMC Med Genomics 17 (1), 116 (2024)
   PUBMED   38684994
  REMARK    GeneRIF: Identification of Novel NSD1 variations in four Pediatric
            cases with sotos Syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2405)
  AUTHORS   Wang,X., Yeh,S., Wu,G., Hsu,C.L., Wang,L., Chiang,T., Yang,Y.,
            Guo,Y. and Chang,C.
  TITLE     Identification and characterization of a novel androgen receptor
            coregulator ARA267-alpha in prostate cancer cells
  JOURNAL   J Biol Chem 276 (44), 40417-40423 (2001)
   PUBMED   11509567
REFERENCE   6  (residues 1 to 2405)
  AUTHORS   Jaju,R.J., Fidler,C., Haas,O.A., Strickson,A.J., Watkins,F.,
            Clark,K., Cross,N.C., Cheng,J.F., Aplan,P.D., Kearney,L.,
            Boultwood,J. and Wainscoat,J.S.
  TITLE     A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in
            de novo childhood acute myeloid leukemia
  JOURNAL   Blood 98 (4), 1264-1267 (2001)
   PUBMED   11493482
REFERENCE   7  (residues 1 to 2405)
  AUTHORS   Lee,D.K., Duan,H.O. and Chang,C.
  TITLE     Androgen receptor interacts with the positive elongation factor
            P-TEFb and enhances the efficiency of transcriptional elongation
  JOURNAL   J Biol Chem 276 (13), 9978-9984 (2001)
   PUBMED   11266437
REFERENCE   8  (residues 1 to 2405)
  AUTHORS   Huang,N., vom Baur,E., Garnier,J.M., Lerouge,T., Vonesch,J.L.,
            Lutz,Y., Chambon,P. and Losson,R.
  TITLE     Two distinct nuclear receptor interaction domains in NSD1, a novel
            SET protein that exhibits characteristics of both corepressors and
            coactivators
  JOURNAL   EMBO J 17 (12), 3398-3412 (1998)
   PUBMED   9628876
REFERENCE   9  (residues 1 to 2405)
  AUTHORS   Ocansey,S., Cole,T.R.P., Rahman,N. and Tatton-Brown,K.
  TITLE     Sotos Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301652
REFERENCE   10 (residues 1 to 2405)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027314.5, AC008570.6 and
            AC146507.2.
            
            Summary: This gene encodes a protein containing a SET domain, 2
            LXXLL motifs, 3 nuclear translocation signals (NLSs), 4 plant
            homeodomain (PHD) finger regions, and a proline-rich region. The
            encoded protein enhances androgen receptor (AR) transactivation,
            and this enhancement can be increased further in the presence of
            other androgen receptor associated coregulators. This protein may
            act as a nucleus-localized, basic transcriptional factor and also
            as a bifunctional transcriptional regulator. Mutations of this gene
            have been associated with Sotos syndrome and Weaver syndrome. One
            version of childhood acute myeloid leukemia is the result of a
            cryptic translocation with the breakpoints occurring within nuclear
            receptor-binding Su-var, enhancer of zeste, and trithorax domain
            protein 1 on chromosome 5 and nucleoporin, 98-kd on chromosome 11.
            Multiple transcript variants encoding distinct isoforms have been
            identified for this gene. [provided by RefSeq, Sep 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3538515.1,
                                           SRR14038197.1830840.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2405
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..2405
                     /product="histone-lysine N-methyltransferase, H3 lysine-36
                     specific isoform a"
                     /EC_number="2.1.1.357"
                     /note="androgen receptor-associated coregulator 267;
                     histone-lysine N-methyltransferase, H3 lysine-36 and H4
                     lysine-20 specific; H3-K36-HMTase; H4-K20-HMTase; lysine
                     N-methyltransferase 3B; NR-binding SET domain-containing
                     protein; androgen receptor coactivator 267 kDa protein;
                     androgen receptor-associated protein of 267 kDa; nuclear
                     receptor-binding SET domain-containing protein 1; nuclear
                     receptor SET domain-containing protein 1; histone-lysine
                     N-methyltransferase, H3 lysine-36 specific"
                     /calculated_mol_wt=264921
     Region          27..142
                     /region_name="PWWP_NSD1_rpt1"
                     /note="first PWWP domain found in nuclear receptor-binding
                     SET domain-containing protein 1 (NSD1) and similar
                     proteins; cd20161"
                     /db_xref="CDD:438989"
     Site            order(43,46,77)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438989"
     Site            44..47
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438989"
     Site            order(115..117,120..121)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438989"
     Region          <1140..1296
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          1254..1296
                     /region_name="PHD1_NSD1_2"
                     /note="PHD finger 1 found in nuclear receptor-binding SET
                     domain-containing protein NSD1 and NSD2; cd15648"
                     /db_xref="CDD:277118"
     Site            order(1254,1263..1267,1272,1290)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277118"
     Region          1301..1347
                     /region_name="PHD2_NSD1"
                     /note="PHD finger 2 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15650"
                     /db_xref="CDD:277120"
     Site            order(1301,1311..1315,1321,1342)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277120"
     Region          1348..1401
                     /region_name="PHD3_NSD1"
                     /note="PHD finger 3 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15653"
                     /db_xref="CDD:277123"
     Site            order(1348,1366..1370,1374,1396)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277123"
     Region          1418..1457
                     /region_name="PHD4_NSD1"
                     /note="PHD finger 4 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15656"
                     /db_xref="CDD:277126"
     Site            order(1418,1427..1431,1435,1452)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277126"
     Region          1464..1559
                     /region_name="PWWP_NSD1_rpt2"
                     /note="second PWWP domain found in nuclear
                     receptor-binding SET domain-containing protein 1 (NSD1)
                     and similar proteins; cd20164"
                     /db_xref="CDD:438992"
     Site            order(1476,1479,1507)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438992"
     Site            1477..1480
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438992"
     Region          1610..1648
                     /region_name="AWS"
                     /note="AWS domain; pfam17907"
                     /db_xref="CDD:465559"
     Region          1650..1791
                     /region_name="SET_NSD1"
                     /note="SET domain (including post-SET domain) found in
                     nuclear receptor-binding SET domain-containing protein 1
                     (NSD1) and similar proteins; cd19210"
                     /db_xref="CDD:380987"
     Site            order(1661..1663,1680,1690,1694,1703..1709,1726..1730,
                     1737..1739,1754,1765..1775,1777..1781,1790)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380987"
     Site            order(1661..1663,1703..1706,1726..1730,1767,1774,
                     1778..1781,1790)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380987"
     Site            order(1680,1690,1694,1705..1709,1737..1739,1754,
                     1765..1769)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:380987"
     Site            order(1732,1779,1781,1786)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380987"
     Region          1829..1871
                     /region_name="PHD5_NSD1"
                     /note="PHD finger 5 found in nuclear receptor-binding SET
                     domain-containing protein 1 (NSD1); cd15659"
                     /db_xref="CDD:277129"
     Site            order(1829,1838..1842,1848,1866)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277129"
     Region          1870..1919
                     /region_name="C5HCH"
                     /note="NSD Cys-His rich domain; pfam17982"
                     /db_xref="CDD:465605"
     Region          <1917..2283
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..2405
                     /gene="NSD1"
                     /gene_synonym="ARA267; KMT3B; SOTOS; SOTOS1; STO"
                     /coded_by="NM_001409308.1:288..7505"
                     /note="isoform a is encoded by transcript variant 11"
                     /db_xref="GeneID:64324"
                     /db_xref="HGNC:HGNC:14234"
                     /db_xref="MIM:606681"
ORIGIN      
        1 mlelpgtsss stsqelpfcq pkkkstplky evgdliwakf krrpwwpcri csdplinths
       61 kmkvsnrrpy rqyyveafgd pserawvagk aivmfegrhq feelpvlrrr gkqkekgyrh
      121 kvpqkilskw easvglaeqy dvpkgsknrk cipgsiklds eedmpfedct ndpesehdll
      181 lngclkslaf dsehsadeke kpcaksrark ssdnpkrtsv kkghiqfeah kderrgkipe
      241 nlglnfisgd isdtqasnel sriansltgs ntapgsflfs scgkntakke fetsngdsll
      301 glpegalisk csreknkpqr slvcgskvkl cyigagdeek rsdsisictt sddgssdldp
      361 iehssesdns vleipdafdr tenmlsmqkn ekikysrfaa tntrvkakqk plisnshtdh
      421 lmgctksaep gtetsqvnls dlkastlvhk pqsdftndal spkfnlsssi ssenslikgg
      481 aanqallhsk skqpkfrsik ckhkenpvma eppvineecs lkccssdtkg splasisksg
      541 kvdglkllnn mhektrdssd ietavvkhvl selkelsyrs lgedvsdsgt skpskpllfs
      601 sassqnhipi epdykfstll mmlkdmhdsk tkeqrlmtaq nlvsyrspgr gdcstnspvg
      661 vskvlvsggs thnsekkgdg tqnsanpsps ggdsalsgel saslpgllsd krdlpasgks
      721 rsdcvtrrnc grskpssklr dafsaqmvkn tvnrkalkte rkrklnqlps vtldavlqgd
      781 rerggslrgg aedpskedpl qimghltsed gdhfsdvhfd skvkqsdpgk isekglsfen
      841 gkgpeldsvm nsendelngv nqvvpkkrwq rlnqrrtkpr krmnrfkeke nsecafrvll
      901 psdpvqegrd efpehrtpsa sileeplteq nhadcldsag prlnvcdkss asigdmekep
      961 gipsltpqae lpepavrsek krlrkpskwl leyteeydqi fapkkkqkkv qeqvhkvssr
     1021 ceeesllarg rssaqnkqvd enslistkee ppvlereapf legplaqsel ggghaelpql
     1081 tlsvpvapev sprpalesee llvktpgnye skrqrkptkk llesndldpg fmpkkgdlgl
     1141 skkcyeaghl engitescat syskdfgggt tkifdkprkr krqrhaaakm qckkvkndds
     1201 skeipgsege lmphrtatsp ketveegveh dpgmpaskkm qgergggaal kenvcqncek
     1261 lgelllceaq ccgafhlecl gltemprgkf icnecrtgih tcfvckqsge dvkrcllplc
     1321 gkfyheecvq kypptvmqnk gfrcslhici tchaanpanv saskgrlmrc vrcpvayhan
     1381 dfclaagski lasnsiicpn hftprrgcrn hehvnvswcf vcseggsllc cdscpaafhr
     1441 eclnidipeg nwycndckag kkphyreivw vkvgryrwwp aeichpravp snidkmrhdv
     1501 gefpvlffgs ndylwthqar vfpymegdvs skdkmgkgvd gtykkalqea aarfeelkaq
     1561 kelrqlqedr kndkkpppyk hikvnrpigr vqiftadlse iprcnckatd enpcgidsec
     1621 inrmllyech ptvcpaggrc qnqcfskrqy peveifrtlq rgwglrtktd ikkgefvney
     1681 vgelideeec rariryaqeh ditnfymltl dkdriidagp kgnyarfmnh ccqpncetqk
     1741 wsvngdtrvg lfalsdikag teltfnynle clgngktvck cgapncsgfl gvrpknqpia
     1801 teekskkfkk kqqgkrrtqg eitkeredec fscgdagqlv sckkpgcpkv yhadclnltk
     1861 rpagkwecpw hqcdicgkea asfcemcpss fckqhregml fiskldgrls ctehdpcgpn
     1921 plepgeirey vpppvplppg psthlaeqst gmaaqapkms dkppadtnqm lslskkalag
     1981 tcqrpllper plertdsrpq pldkvrdlag sgtksqslvs sqrpldrppa vagprpqlsd
     2041 kpspvtspss spsvrsqple rplgtadprl dksigaaspr pqslektsvp tglrlpppdr
     2101 llitsspkpq tsdrptdkph aslsqrlppp ekvlsavvqt lvakekalrp vdqntqsknr
     2161 aalvmdlidl tprqkeraas phqvtpqade kmpvlesssw paskglghmp ravekgcvsd
     2221 plqtsgkaaa psedpwqavk sltqarllsq ppakaflyep ttqasgrasa gaeqtpgpls
     2281 qspglvkqak qmvggqqlpa laaksgqsfr slgkapaslp teekklvtte qspwalgkas
     2341 sraglwpiva gqtlaqscws agstqtlaqt cwslgrgqdp kpeqntlpal nqapsshkca
     2401 eseqk
//
LOCUS       NP_001185731            1591 aa            linear   PRI 21-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4 gamma 3 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001185731
VERSION     NP_001185731.1
DBSOURCE    REFSEQ: accession NM_001198802.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1591)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1591)
  AUTHORS   Kang,J.Y., Wen,Z., Pan,D., Zhang,Y., Li,Q., Zhong,A., Yu,X.,
            Wu,Y.C., Chen,Y., Zhang,X., Kou,P.C., Geng,J., Wang,Y.Y., Hua,M.M.,
            Zong,R., Li,B., Shi,H.J., Li,D., Fu,X.D., Li,J., Nelson,D.L.,
            Guo,X., Zhou,Y., Gou,L.T., Huang,Y. and Liu,M.F.
  TITLE     LLPS of FXR1 drives spermiogenesis by activating translation of
            stored mRNAs
  JOURNAL   Science 377 (6607), eabj6647 (2022)
   PUBMED   35951695
REFERENCE   3  (residues 1 to 1591)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1591)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 1591)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1591)
  AUTHORS   Waskiewicz,A.J., Johnson,J.C., Penn,B., Mahalingam,M., Kimball,S.R.
            and Cooper,J.A.
  TITLE     Phosphorylation of the cap-binding protein eukaryotic translation
            initiation factor 4E by protein kinase Mnk1 in vivo
  JOURNAL   Mol Cell Biol 19 (3), 1871-1880 (1999)
   PUBMED   10022874
REFERENCE   7  (residues 1 to 1591)
  AUTHORS   Pyronnet,S., Imataka,H., Gingras,A.C., Fukunaga,R., Hunter,T. and
            Sonenberg,N.
  TITLE     Human eukaryotic translation initiation factor 4G (eIF4G) recruits
            mnk1 to phosphorylate eIF4E
  JOURNAL   EMBO J 18 (1), 270-279 (1999)
   PUBMED   9878069
REFERENCE   8  (residues 1 to 1591)
  AUTHORS   Gingras,A.C., Raught,B. and Sonenberg,N.
  TITLE     eIF4 initiation factors: effectors of mRNA recruitment to ribosomes
            and regulators of translation
  JOURNAL   Annu Rev Biochem 68, 913-963 (1999)
   PUBMED   10872469
  REMARK    Review article
REFERENCE   9  (residues 1 to 1591)
  AUTHORS   Imataka,H., Gradi,A. and Sonenberg,N.
  TITLE     A newly identified N-terminal amino acid sequence of human eIF4G
            binds poly(A)-binding protein and functions in poly(A)-dependent
            translation
  JOURNAL   EMBO J 17 (24), 7480-7489 (1998)
   PUBMED   9857202
REFERENCE   10 (residues 1 to 1591)
  AUTHORS   Gradi,A., Imataka,H., Svitkin,Y.V., Rom,E., Raught,B., Morino,S.
            and Sonenberg,N.
  TITLE     A novel functional human eukaryotic translation initiation factor
            4G
  JOURNAL   Mol Cell Biol 18 (1), 334-342 (1998)
   PUBMED   9418880
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031005.2, AL627311.16,
            AL358392.19 and AL606477.11.
            
            Summary: The protein encoded by this gene is thought to be part of
            the eIF4F protein complex, which is involved in mRNA cap
            recognition and transport of mRNAs to the ribosome. Interestingly,
            a microRNA (miR-520c-3p) has been found that negatively regulates
            synthesis of the encoded protein, and this leads to a global
            decrease in protein translation and cell proliferation. Therefore,
            this protein is a key component of the anti-tumor activity of
            miR-520c-3p. [provided by RefSeq, May 2016].
            
            Transcript Variant: This variant (2) has an additional in-frame
            smaller exon in the 5' coding region and lacks an in-frame larger
            exon in the middle coding region, as compared to variant 1. The
            resulting isoform (2) has an extra smaller segment in one region
            and lacks a larger segment in another region, as compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB209119.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1591
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     Protein         1..1591
                     /product="eukaryotic translation initiation factor 4 gamma
                     3 isoform 2"
                     /note="eIF-4-gamma 3; eIF-4-gamma II"
                     /calculated_mol_wt=177150
     Region          <27..>302
                     /region_name="PRK10263"
                     /note="DNA translocase FtsK; Provisional"
                     /db_xref="CDD:236669"
     Region          141..169
                     /region_name="PABPC1-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q80XI3; propagated from
                     UniProtKB/Swiss-Prot (O43432.2)"
     Region          214..238
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43432.2)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43432.2)"
     Region          311..338
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XI3; propagated from
                     UniProtKB/Swiss-Prot (O43432.2)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          573..626
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          625..636
                     /region_name="EIF4E-binding.
                     /evidence=ECO:0000250|UniProtKB:Q04637"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          692..717
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          705..1025
                     /region_name="eIF3/EIF4A-binding.
                     /evidence=ECO:0000250|UniProtKB:Q04637"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Site            705..706
                     /site_type="cleavage"
                     /note="Cleavage, by enterovirus/rhinovirus protease 2A;
                     propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Site            706..707
                     /site_type="cleavage"
                     /note="Cleavage, by foot-and-mouth disease virus leader
                     protease; propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          735..755
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          761..989
                     /region_name="MIF4G"
                     /note="MIF4G domain; pfam02854"
                     /db_xref="CDD:397130"
     Region          866..886
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          1023..1048
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          1078..1225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK1.
                     /evidence=ECO:0000269|PubMed:14507913; propagated from
                     UniProtKB/Swiss-Prot (O43432.2)"
     Site            1224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43432.2)"
     Region          1228..1340
                     /region_name="MA3"
                     /note="MA3 domain; pfam02847"
                     /db_xref="CDD:397128"
     Site            1415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43432.2)"
     Region          1434..1562
                     /region_name="W2_eIF4G1_like"
                     /note="C-terminal W2 domain of eukaryotic translation
                     initiation factor 4 gamma 1 and similar proteins; cd11559"
                     /db_xref="CDD:211397"
     Region          1439..1591
                     /region_name="EIF4A-binding.
                     /evidence=ECO:0000250|UniProtKB:Q04637"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     Region          <1541..1587
                     /region_name="W2"
                     /note="C-terminal domain of eIF4-gamma/eIF5/eIF2b-epsilon;
                     cl17013"
                     /db_xref="CDD:473053"
     Region          1577..1591
                     /region_name="Necessary but not sufficient for
                     MKNK1-binding. /evidence=ECO:0000250|UniProtKB:Q04637"
                     /note="propagated from UniProtKB/Swiss-Prot (O43432.2)"
     CDS             1..1591
                     /gene="EIF4G3"
                     /gene_synonym="eIF-4G 3; eIF4G 3; eIF4GII"
                     /coded_by="NM_001198802.3:632..5407"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55580.1"
                     /db_xref="GeneID:8672"
                     /db_xref="HGNC:HGNC:3298"
                     /db_xref="MIM:603929"
ORIGIN      
        1 mnsqpqtrsp ggfrpiqffq rpqiqpprat ipnsspsirp gaqtptavyq anqhimmvnh
       61 lpmpypvpqg pqycipqyrh sgppyvgppq qypvqppgpg pfypgpgpgd fpnaygtpfy
      121 psqpvyqsap iivptqqqpp pakrekktir irdpnqggkd iteeimsggg srnptppigr
      181 ptstptppql psqvpehspv vygtvesahl aastpvtaas dqkqeekpkp dpvlkspspv
      241 lrlvlsgekk eqegqtsett aivsiaelpl ppspttvssv arstiaapts salssqpift
      301 taiddrcels spredtipip sltsctetsd plptnenddd ickkpcsvap ndiplvsstn
      361 lineingvse klsatesive ivkqevlplt leleilenpp eemklecipa pitpstvpsf
      421 pptpptppas pphtpvivpa aattvsspsa aitvqrvlee desirtclse dakeiqnkie
      481 veadgqteei ldsqnlnsrr spvpaqiait vpktwkkpkd rtrtteemle aelelkaeee
      541 lsidkvlese qdkmsqgfhp erdpsdlkkv kaveengeea epvrngaesv segegidans
      601 gstdssgdgv tfpfkpeswk ptdtegkkqy dreflldfqf mpaciqkpeg lppisdvvld
      661 kinqpklpmr tldprilprg pdftpafadf grqtpggrgv pllnvgsrrs qpgqrreprk
      721 iitvsvkedv hlkkaenawk psqkrdsqad dpeniktqel frkvrsilnk ltpqmfnqlm
      781 kqvsgltvdt eerlkgvidl vfekaideps fsvayanmcr clvtlkvpma dkpgntvnfr
      841 klllnrcqke fekdkadddv fekkqkelea asapeertrl hdeleeakdk arrrsignik
      901 figelfklkm lteaimhdcv vkllknhdee sleclcrllt tigkdldfek akprmdqyfn
      961 qmekivkerk tssrirfmlq dvidlrlcnw vsrradqgpk tieqihkeak ieeqeeqrkv
     1021 qqlmtkekrr pgvqrvdegg wntvqgakns rvldpskflk itkptideki qlvpkaqlgs
     1081 wgkgssggak asetdalrss asslnrfsal qppapsgstp stpvefdsrr tltsrgsmgr
     1141 ekndkplpsa tarpntfmrg gsskdlldnq sqeeqrreml etvkqltggv dvernsteae
     1201 rnktresakp eisamsahdk aalseeeler ksksiidefl hindfkeamq cveelnaqgl
     1261 lhvfvrvgve stlersqitr dhmgqllyql vqseklskqd ffkgfsetle laddmaidip
     1321 hiwlylaelv tpmlkeggis mreltiefsk pllpvgragv llseilhllc kqmshkkvga
     1381 lwreadlswk dflpegedvh nflleqkldf iesdspcsse alskkelsae elykrlekli
     1441 iedkandeqi fdwveanlde iqmssptflr almtavckaa iiadsstfrv dtavikqrvp
     1501 illkyldsdt ekelqalyal qasivkldqp anllrmffdc lydeevised afykwesskd
     1561 paeqngkgva lksvtafftw lreaeeesed n
//
LOCUS       NP_001425600             798 aa            linear   PRI 21-NOV-2025
DEFINITION  dipeptidyl peptidase 8 isoform 9 [Homo sapiens].
ACCESSION   NP_001425600 XP_047288718 XP_054234282
VERSION     NP_001425600.1
DBSOURCE    REFSEQ: accession NM_001438671.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Li,K., Zhang,Y., Zhao,W., Wang,R., Li,Y., Wei,L., Wang,L., Chen,X.,
            Chen,Z., Liu,P., Nie,N., Tian,X. and Fu,R.
  TITLE     DPP8/9 inhibition attenuates the TGF-beta1-induced excessive
            deposition of extracellular matrix (ECM) in human mesangial cells
            via Smad and Akt signaling pathways
  JOURNAL   Toxicol Lett 395, 1-10 (2024)
   PUBMED   38458339
  REMARK    GeneRIF: DPP8/9 inhibition attenuates the TGF-beta1-induced
            excessive deposition of extracellular matrix (ECM) in human
            mesangial cells via Smad and Akt signaling pathways.
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Zhang,Y., Li,K., Li,Y., Zhao,W., Wang,L., Chen,Z., Ma,X., Yao,T.,
            Wang,J., Dong,W., Li,X., Tian,X. and Fu,R.
  TITLE     Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the
            proximal renal tubule epithelial cells
  JOURNAL   Pharmacol Res 169, 105630 (2021)
   PUBMED   33932609
  REMARK    GeneRIF: Profibrotic mechanisms of DPP8 and DPP9 highly expressed
            in the proximal renal tubule epithelial cells.
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Hollingsworth,L.R., Sharif,H., Griswold,A.R., Fontana,P.,
            Mintseris,J., Dagbay,K.B., Paulo,J.A., Gygi,S.P., Bachovchin,D.A.
            and Wu,H.
  TITLE     DPP9 sequesters the C terminus of NLRP1 to repress inflammasome
            activation
  JOURNAL   Nature 592 (7856), 778-783 (2021)
   PUBMED   33731932
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Chen,Y.S., Chien,C.H., Goparaju,C.M., Hsu,J.T., Liang,P.H. and
            Chen,X.
  TITLE     Purification and characterization of human prolyl dipeptidase DPP8
            in Sf9 insect cells
  JOURNAL   Protein Expr Purif 35 (1), 142-146 (2004)
   PUBMED   15039077
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Shu,H., Chen,S., Bi,Q., Mumby,M. and Brekken,D.L.
  TITLE     Identification of phosphoproteins and their phosphorylation sites
            in the WEHI-231 B lymphoma cell line
  JOURNAL   Mol Cell Proteomics 3 (3), 279-286 (2004)
   PUBMED   14729942
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Qi,S.Y., Riviere,P.J., Trojnar,J., Junien,J.L. and Akinsanya,K.O.
  TITLE     Cloning and characterization of dipeptidyl peptidase 10, a new
            member of an emerging subgroup of serine proteases
  JOURNAL   Biochem J 373 (Pt 1), 179-189 (2003)
   PUBMED   12662155
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Ajami,K., Abbott,C.A., Obradovic,M., Gysbers,V., Kahne,T.,
            McCaughan,G.W. and Gorrell,M.D.
  TITLE     Structural requirements for catalysis, expression, and dimerization
            in the CD26/DPIV gene family
  JOURNAL   Biochemistry 42 (3), 694-701 (2003)
   PUBMED   12534281
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Abbott,C.A., Yu,D.M., Woollatt,E., Sutherland,G.R., McCaughan,G.W.
            and Gorrell,M.D.
  TITLE     Cloning, expression and chromosomal localization of a novel human
            dipeptidyl peptidase (DPP) IV homolog, DPP8
  JOURNAL   Eur J Biochem 267 (20), 6140-6150 (2000)
   PUBMED   11012666
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011846.16 and AC105129.4.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047288718.1, XP_054234282.1.
            
            Summary: This gene encodes a member of the peptidase S9B family, a
            small family of dipeptidyl peptidases that are able to cleave
            peptide substrates at a prolyl bond. The encoded protein shares
            similarity with dipeptidyl peptidase IV in that it is ubiquitously
            expressed, and hydrolyzes the same substrates. These similarities
            suggest that, like dipeptidyl peptidase IV, this protein may play a
            role in T-cell activation and immune function. Alternatively
            spliced transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.206573.1,
                                           SRR18074969.3441660.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..798
                     /product="dipeptidyl peptidase 8 isoform 9"
                     /EC_number="3.4.14.5"
                     /note="prolyl dipeptidase DPP8; dipeptidyl peptidase VIII;
                     DPP VIII; dipeptidyl peptidase IV-related protein 1"
                     /calculated_mol_wt=91713
     Region          8..162
                     /region_name="Dpp_8_9_N"
                     /note="Dipeptidyl peptidase 8 and 9 N-terminal; pfam19520"
                     /db_xref="CDD:466112"
     Region          175..595
                     /region_name="DPPIV_N"
                     /note="Dipeptidyl peptidase IV (DPP IV) N-terminal region;
                     pfam00930"
                     /db_xref="CDD:395744"
     Region          <673..791
                     /region_name="Peptidase_S9"
                     /note="Prolyl oligopeptidase family; pfam00326"
                     /db_xref="CDD:459761"
     CDS             1..798
                     /gene="DPP8"
                     /gene_synonym="DP8; DPRP-1; DPRP1; MST097; MSTP097;
                     MSTP135; MSTP141"
                     /coded_by="NM_001438671.1:304..2700"
                     /note="isoform 9 is encoded by transcript variant 13"
                     /db_xref="GeneID:54878"
                     /db_xref="HGNC:HGNC:16490"
                     /db_xref="MIM:606819"
ORIGIN      
        1 mwkrseqmki ksgkcnmaaa meteqlgvei fetadceeni esqdrpklep fyveryswsq
       61 lkklladtrk yhgymmakap hdfmfvkrnd pdgphsdriy ylamsgenre ntlfyseipk
      121 tinraavlml swkplldlfq atldygmysr eeellrerkr igtvgiasyd yhqgsgtflf
      181 qagsgiyhvk dggpqgftqq plrpnlvets cpnirmdpkl cpadpdwiaf ihsndiwisn
      241 ivtreerrlt yvhnelanme edarsagvat fvlqeefdry sgywwcpkae ttpsggkilr
      301 ilyeendese veiihvtspm letrradsfr ypktgtanpk vtfkmseimi daegriidvi
      361 dkeliqpfei lfegveyiar agwtpegkya wsilldrsqt rlqivlispe lfipveddvm
      421 erqrliesvp dsvtpliiye ettdiwinih difhvfpqsh eeeiefifas ecktgfrhly
      481 kitsilkesk ykrssgglpa psdfkcpike eiaitsgewe vlgrhgsniq vdevrrlvyf
      541 egtkdspleh hlyvvsyvnp gevtrltdrg yshsccisqh cdffiskysn qknphcvsly
      601 klsspeddpt cktkefwati ldsagplpdy tppeifsfes ttgftlygml ykphdlqpgk
      661 kyptvlfiyg gpqvaiagap vtlwifydtg yterymghpd qneqgyylgs vamqaekfps
      721 epnrllllhg fldenvhfah tsillsflvr agkpydlqiy pqerhsirvp esgehyelhl
      781 lhylqenlgs riaalkvi
//
LOCUS       NP_001394379            2843 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform b [Homo sapiens].
ACCESSION   NP_001394379
VERSION     NP_001394379.1
DBSOURCE    REFSEQ: accession NM_001407450.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2843)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2843)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2843)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2843)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2843)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2843)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2843)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2843)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2843)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2843)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1278735.1,
                                           SRR14038197.1445753.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2843
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2843
                     /product="adenomatous polyposis coli protein isoform b"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=311516
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Region          <8..272
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          239..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          340..392
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          393..466
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          453..495
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          465..508
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(499,503,507,542,546,550,586,590,594)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          505..547
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          512..553
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          516..553
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          548..591
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          560..595
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          592..638
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          603..644
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          639..683
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          649..689
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          653..687
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          684..725
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          691..731
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          695..731
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          726..767
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          732..1019
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Site            744
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            748
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            780
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          828..878
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            908
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          923..943
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          958..987
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          960..1337
                     /region_name="Responsible for down-regulation through a
                     process mediated by direct ubiquitination"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            987
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1020..1169
                     /region_name="Interaction with catenins.
                     /evidence=ECO:0000269|PubMed:8259519"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1036..1135
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Site            1038
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1042
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1099..1169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1190..1244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1257..>1274
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1283..1368
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1291..1701
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1311..1376
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1403..1475
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1438
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1526..1569
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1583..1611
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1637..1660
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1662..1715
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1664..1717
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1716..1737
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1729..1836
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1746..1839
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Site            1774
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1861
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1863
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1864
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1866..1893
                     /region_name="Highly charged"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1873..1947
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1881..1950
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1965..2011
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1971
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1973
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2033..2052
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2035..2059
                     /region_name="Interaction with AXIN1.
                     /evidence=ECO:0000269|PubMed:10811618"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2043..2072
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2088
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2093
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2147..2635
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2151
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2167..2674
                     /region_name="Basic region.
                     /evidence=ECO:0000269|PubMed:17293347"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2223..2568
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Site            2260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2475..2843
                     /region_name="Interaction with DLG1.
                     /evidence=ECO:0000269|PubMed:8638125"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2569
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2667..2714
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2670..2843
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     Site            2671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2674..2843
                     /region_name="Interaction with MAPRE1.
                     /evidence=ECO:0000269|PubMed:17293347"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2674
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2679
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2710
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2724
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2729..2843
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2803..2806
                     /region_name="Microtubule tip localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2841..2843
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     CDS             1..2843
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407450.1:171..8702"
                     /note="isoform b is encoded by transcript variant 20"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrriar iqqiekdilr irqllqsqat
      241 eaerssqnkh etgshdaerq negqgvgein matsgngqgs ttrmdhetas vlssssthsa
      301 prrltshlgt kvemvyslls mlgthdkddm srtllamsss qdscismrqs gclplliqll
      361 hgndkdsvll gnsrgskear arasaalhni ihsqpddkrg rreirvlhll eqiraycetc
      421 wewqeahepg mdqdknpmpa pvehqicpav cvlmklsfde ehrhamnelg glqaiaellq
      481 vdcemygltn dhysitlrry agmaltnltf gdvankatlc smkgcmralv aqlksesedl
      541 qqviasvlrn lswradvnsk ktlrevgsvk almecalevk kestlksvls alwnlsahct
      601 enkadicavd galaflvgtl tyrsqtntla iiesgggilr nvssliatne dhrqilrenn
      661 clqtllqhlk shsltivsna cgtlwnlsar npkdqealwd mgavsmlknl ihskhkmiam
      721 gsaaalrnlm anrpakykda nimspgsslp slhvrkqkal eaeldaqhls etfdnidnls
      781 pkashrskqr hkqslygdyv fdtnrhddnr sdnfntgnmt vlspylnttv lpsssssrgs
      841 ldssrsekdr slerergigl gnyhpatenp gtsskrglqi sttaaqiakv meevsaihts
      901 qedrssgstt elhcvtdern alrrssaaht hsntynftks ensnrtcsmp yakleykrss
      961 ndslnsvsss dgygkrgqmk psiesysedd eskfcsygqy padlahkihs anhmddndge
     1021 ldtpinyslk ysdeqlnsgr qspsqnerwa rpkhiiedei kqseqrqsrn qsttypvyte
     1081 stddkhlkfq phfgqqecvs pyrsrgangs etnrvgsnhg inqnvsqslc qeddyeddkp
     1141 tnyserysee eqheeeerpt nysikyneek rhvdqpidys lkyatdipss qkqsfsfsks
     1201 ssgqsskteh mssssentst pssnakrqnq lhpssaqsrs gqpqkaatck vssinqetiq
     1261 tycvedtpic fsrcsslssl ssaedeigcn qttqeadsan tlqiaeikek igtrsaedpv
     1321 sevpavsqhp rtkssrlqgs slssesarhk avefssgaks psksgaqtpk sppehyvqet
     1381 plmfsrctsv ssldsfesrs iassvqsepc sgmvsgiisp sdlpdspgqt mppsrsktpp
     1441 pppqtaqtkr evpknkapta ekresgpkqa avnaavqrvq vlpdadtllh fatestpdgf
     1501 scssslsals ldepfiqkdv elrimppvqe ndngnetese qpkesnenqe keaektidse
     1561 kdllddsddd dieileecii samptkssrk akkpaqtask lpppvarkps qlpvykllps
     1621 qnrlqpqkhv sftpgddmpr vycvegtpin fstatslsdl tiesppnela agegvrggaq
     1681 sgefekrdti ptegrstdea qggktssvti pelddnkaee gdilaecins ampkgkshkp
     1741 frvkkimdqv qqasasssap nknqldgkkk kptspvkpip qnteyrtrvr knadsknnln
     1801 aervfsdnkd skkqnlknns kvfndklpnn edrvrgsfaf dsphhytpie gtpycfsrnd
     1861 slssldfddd dvdlsrekae lrkakenkes eakvtshtel tsnqqsankt qaiakqpinr
     1921 gqpkpilqkq stfpqsskdi pdrgaatdek lqnfaientp vcfshnssls slsdidqenn
     1981 nkenepiket eppdsqgeps kpqasgyapk sfhvedtpvc fsrnsslssl sidseddllq
     2041 ecissampkk kkpsrlkgdn ekhsprnmgg ilgedltldl kdiqrpdseh glspdsenfd
     2101 wkaiqegans ivsslhqaaa aaclsrqass dsdsilslks gislgspfhl tpdqeekpft
     2161 snkgprilkp gekstletkk ieseskgikg gkkvykslit gkvrsnseis gqmkqplqan
     2221 mpsisrgrtm ihipgvrnss sstspvskkg pplktpasks psegqtatts prgakpsvks
     2281 elspvarqts qiggsskaps rsgsrdstps rpaqqplsrp iqspgrnsis pgrngisppn
     2341 klsqlprtss pstastkssg sgkmsytspg rqmsqqnltk qtglsknass iprsesaskg
     2401 lnqmnngnga nkkvelsrms stkssgsesd rserpvlvrq stfikeapsp tlrrkleesa
     2461 sfeslspssr pasptrsqaq tpvlspslpd mslsthssvq aggwrklppn lsptieyndg
     2521 rpakrhdiar shsespsrlp inrsgtwkre hskhssslpr vstwrrtgss ssilsasses
     2581 sekaksedek hvnsisgtkq skenqvsakg twrkikenef sptnstsqtv ssgatngaes
     2641 ktliyqmapa vsktedvwvr iedcpinnpr sgrsptgntp pvidsvseka npnikdskdn
     2701 qakqnvgngs vpmrtvglen rlnsfiqvda pdqkgteikp gqnnpvpvse tnessivert
     2761 pfsssssskh sspsgtvaar vtpfnynpsp rkssadstsa rpsqiptpvn nntkkrdskt
     2821 dstessgtqs pkrhsgsylv tsv
//
LOCUS       NP_001397660             380 aa            linear   PRI 21-NOV-2025
DEFINITION  Golgi reassembly-stacking protein 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001397660 XP_016862540
VERSION     NP_001397660.1
DBSOURCE    REFSEQ: accession NM_001410731.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Ahat,E., Song,Y., Xia,K., Reid,W., Li,J., Bui,S., Zhang,F.,
            Linhardt,R.J. and Wang,Y.
  TITLE     GRASP depletion-mediated Golgi fragmentation impairs
            glycosaminoglycan synthesis, sulfation, and secretion
  JOURNAL   Cell Mol Life Sci 79 (4), 199 (2022)
   PUBMED   35312866
  REMARK    GeneRIF: GRASP depletion-mediated Golgi fragmentation impairs
            glycosaminoglycan synthesis, sulfation, and secretion.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Zhang,Y. and Seemann,J.
  TITLE     Rapid degradation of GRASP55 and GRASP65 reveals their immediate
            impact on the Golgi structure
  JOURNAL   J Cell Biol 220 (1) (2021)
   PUBMED   33301566
  REMARK    GeneRIF: Rapid degradation of GRASP55 and GRASP65 reveals their
            immediate impact on the Golgi structure.
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Sutterlin,C., Lin,C.Y., Feng,Y., Ferris,D.K., Erikson,R.L. and
            Malhotra,V.
  TITLE     Polo-like kinase is required for the fragmentation of
            pericentriolar Golgi stacks during mitosis
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 9128-9132 (2001)
   PUBMED   11447294
REFERENCE   7  (residues 1 to 380)
  AUTHORS   Moyer,B.D., Allan,B.B. and Balch,W.E.
  TITLE     Rab1 interaction with a GM130 effector complex regulates COPII
            vesicle cis--Golgi tethering
  JOURNAL   Traffic 2 (4), 268-276 (2001)
   PUBMED   11285137
REFERENCE   8  (residues 1 to 380)
  AUTHORS   Lin,C.Y., Madsen,M.L., Yarm,F.R., Jang,Y.J., Liu,X. and
            Erikson,R.L.
  TITLE     Peripheral Golgi protein GRASP65 is a target of mitotic polo-like
            kinase (Plk) and Cdc2
  JOURNAL   Proc Natl Acad Sci U S A 97 (23), 12589-12594 (2000)
   PUBMED   11050165
REFERENCE   9  (residues 1 to 380)
  AUTHORS   Barr,F.A., Nakamura,N. and Warren,G.
  TITLE     Mapping the interaction between GRASP65 and GM130, components of a
            protein complex involved in the stacking of Golgi cisternae
  JOURNAL   EMBO J 17 (12), 3258-3268 (1998)
   PUBMED   9628863
  REMARK    GeneRIF: A study showing that GRASP65 binds directly to the
            coiled-coil vesicle tethering factor GM130, and targets it to Golgi
            membranes.
REFERENCE   10 (residues 1 to 380)
  AUTHORS   Barr,F.A., Puype,M., Vandekerckhove,J. and Warren,G.
  TITLE     GRASP65, a protein involved in the stacking of Golgi cisternae
  JOURNAL   Cell 91 (2), 253-262 (1997)
   PUBMED   9346242
  REMARK    GeneRIF: Identification of GRASP65, and demonstration that it
            functions in the formation of stacked Golgi cisternae.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC138124.2.
            
            On Aug 15, 2022 this sequence version replaced XP_016862540.1.
            
            Summary: The Golgi complex plays a key role in the sorting and
            modification of proteins exported from the endoplasmic reticulum.
            The protein encoded by this gene is a membrane protein involved in
            establishing the stacked structure of the Golgi apparatus. It is a
            caspase-3 substrate, and cleavage of this encoded protein
            contributes to Golgi fragmentation in apoptosis. This encoded
            protein can form a complex with the Golgi matrix protein GOLGA2,
            and this complex binds to the vesicle docking protein p115.
            Alternative splicing results in multiple transcript variants of
            this gene. [provided by RefSeq, Jul 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3036068.1,
                                           SRR11853565.20140.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.2"
     Protein         1..380
                     /product="Golgi reassembly-stacking protein 1 isoform 5"
                     /note="Golgi reassembly and stacking protein 1; Golgi
                     phosphoprotein 5; Golgi peripheral membrane protein p65;
                     golgi reassembly-stacking protein of 65 kDa; golgi
                     reassembly stacking protein 1, 65kDa; Golgi
                     reassembly-stacking protein 1"
                     /calculated_mol_wt=39821
     Region          3..100
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     Region          69..>145
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     Region          <146..238
                     /region_name="PHA03264"
                     /note="envelope glycoprotein D; Provisional"
                     /db_xref="CDD:223029"
     CDS             1..380
                     /gene="GORASP1"
                     /gene_synonym="GOLPH5; GRASP65; P65"
                     /coded_by="NM_001410731.1:87..1229"
                     /note="isoform 5 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS93245.1"
                     /db_xref="GeneID:64689"
                     /db_xref="HGNC:HGNC:16769"
                     /db_xref="MIM:606867"
ORIGIN      
        1 mglgvsaeqp aggaegfhlh gvqenspaqq aglepyfdfi itighsrlnk endtlkallk
       61 anvekpvkle vfnmktmrvr evevvpsnmw ggqgllgasv rfcsfrrase qvwhvldvep
      121 sspaalaglr pytdyvvgsd qilqeppsyh kkppgtppps alplgapppd alppgptped
      181 spsletgsrq sdymeallqa pgssmedplp gpgspshsap dpdglphfme tplqppppvq
      241 rvmdpgfldv sgislldnsn asvwpslpss teltttavst sgpedicsss ssherggeat
      301 wsgsefevsf ldspgaqaqa dhlpqltlpd sltsaasped glsaelleaq aeeepasteg
      361 ldtgteaegl dsqaqistte
//
LOCUS       NP_001424530             440 aa            linear   PRI 21-NOV-2025
DEFINITION  sorting nexin-27 isoform 3 [Homo sapiens].
ACCESSION   NP_001424530 XP_011508326 XP_054194888
VERSION     NP_001424530.1
DBSOURCE    REFSEQ: accession NM_001437601.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Broniarczyk,J., Trejo-Cerro,O., Massimi,P., Kavcic,N., Myers,M.P.
            and Banks,L.
  TITLE     HPV-18 E6 enhances the interaction between EMILIN2 and SNX27 to
            promote WNT signaling
  JOURNAL   J Virol 98 (7), e0073524 (2024)
   PUBMED   38874360
  REMARK    GeneRIF: HPV-18 E6 enhances the interaction between EMILIN2 and
            SNX27 to promote WNT signaling.
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Xi,Y., Gai,Y., Zhang,W., Wang,M., Liu,Q. and Bi,Y.
  TITLE     Circular RNA SNX27 Facilitates Gastric Cancer Progression By
            Sponging miR-638
  JOURNAL   Turk J Gastroenterol 35 (4), 280-287 (2024)
   PUBMED   39128090
  REMARK    GeneRIF: Circular RNA SNX27 Facilitates Gastric Cancer Progression
            By Sponging miR-638.
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Broniarczyk,J.K., Massimi,P., Trejo-Cerro,O., Myers,M.P. and
            Banks,L.
  TITLE     HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in a
            PBM-Dependent Manner and Promotes Increased Cell Proliferation
  JOURNAL   J Virol 96 (22), e0136522 (2022)
   PUBMED   36326272
  REMARK    GeneRIF: HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in
            a PBM-Dependent Manner and Promotes Increased Cell Proliferation.
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 440)
  AUTHORS   MacNeil,A.J., Mansour,M. and Pohajdak,B.
  TITLE     Sorting nexin 27 interacts with the Cytohesin associated
            scaffolding protein (CASP) in lymphocytes
  JOURNAL   Biochem Biophys Res Commun 359 (4), 848-853 (2007)
   PUBMED   17577583
  REMARK    GeneRIF: These results suggest that endosomal SNX27 may recruit
            CASP to orchestrate intracellular trafficking and/or signaling
            complexes.
REFERENCE   7  (residues 1 to 440)
  AUTHORS   Rincon,E., Santos,T., Avila-Flores,A., Albar,J.P., Lalioti,V.,
            Lei,C., Hong,W. and Merida,I.
  TITLE     Proteomics identification of sorting nexin 27 as a diacylglycerol
            kinase zeta-associated protein: new diacylglycerol kinase roles in
            endocytic recycling
  JOURNAL   Mol Cell Proteomics 6 (6), 1073-1087 (2007)
   PUBMED   17351151
  REMARK    GeneRIF: These data support a previously unreported role for
            diacylglycerol kinase zeta in the modulation of membrane
            trafficking, which may also help to define SNX27 function.
REFERENCE   8  (residues 1 to 440)
  AUTHORS   Joubert,L., Hanson,B., Barthet,G., Sebben,M., Claeysen,S., Hong,W.,
            Marin,P., Dumuis,A. and Bockaert,J.
  TITLE     New sorting nexin (SNX27) and NHERF specifically interact with the
            5-HT4a receptor splice variant: roles in receptor targeting
  JOURNAL   J Cell Sci 117 (Pt 22), 5367-5379 (2004)
   PUBMED   15466885
  REMARK    GeneRIF: SNX27a redirects part of the 5-HT4(a)R to early endosomes.
REFERENCE   9  (residues 1 to 440)
  AUTHORS   Worby,C.A. and Dixon,J.E.
  TITLE     Sorting out the cellular functions of sorting nexins
  JOURNAL   Nat Rev Mol Cell Biol 3 (12), 919-931 (2002)
   PUBMED   12461558
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol. 2003 Feb;4(2):156.]
REFERENCE   10 (residues 1 to 440)
  AUTHORS   Teasdale,R.D., Loci,D., Houghton,F., Karlsson,L. and Gleeson,P.A.
  TITLE     A large family of endosome-localized proteins related to sorting
            nexin 1
  JOURNAL   Biochem J 358 (Pt 1), 7-16 (2001)
   PUBMED   11485546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL391335.32 and AL589765.19.
            
            On or before Apr 7, 2025 this sequence version replaced
            XP_011508326.1, XP_054194888.1.
            
            Summary: This gene encodes a member of the sorting nexin family, a
            diverse group of cytoplasmic and membrane-associated proteins
            involved in endocytosis of plasma membrane receptors and protein
            trafficking through these compartments. All members of this protein
            family contain a phosphoinositide binding domain (PX domain). A
            highly similar protein in mouse is responsible for the specific
            recruitment of an isoform of serotonin 5-hydroxytryptamine 4
            receptor into early endosomes, suggesting the analogous role for
            the human protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2716598.1,
                                           SRR14038192.3003616.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..440
                     /product="sorting nexin-27 isoform 3"
                     /note="methamphetamine-responsive transcript 1; sorting
                     nexin family member 27"
                     /calculated_mol_wt=50150
     Region          42..>88
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     Region          70..164
                     /region_name="PX_domain"
                     /note="The Phox Homology domain, a phosphoinositide
                     binding module; cl02563"
                     /db_xref="CDD:470617"
     Site            order(95..97,121..122,134)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132768"
     Region          172..264
                     /region_name="FERM_F1_SNX27"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F1 sub-domain, found in sorting nexin protein 27
                     (SNX27); cd01777"
                     /db_xref="CDD:340475"
     Region          324..425
                     /region_name="FERM-like_C_SNX27"
                     /note="Atypical FERM-like domain C-lobe of Sorting nexin
                     27; cd13338"
                     /db_xref="CDD:270146"
     CDS             1..440
                     /gene="SNX27"
                     /gene_synonym="MRT1; MY014"
                     /coded_by="NM_001437601.1:153..1475"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:81609"
                     /db_xref="HGNC:HGNC:20073"
                     /db_xref="MIM:611541"
ORIGIN      
        1 madedgegih psaphrnggg gggggsglhc agnggggggg prvvrivkse sgygfnvrgq
       61 vseggqlrsi ngelyaplqh vynvymagrq lcskryrefa ilhqnlkref anftfprlpg
      121 kwpfslseqq ldarrrglee ylekvcsirv igesdimqef lsesdenyng vsdvelrval
      181 pdgttvtvrv kknsttdqvy qaiaakvgmd sttvnyfalf evishsfvrk lapnefphkl
      241 yiqnytsavp gtcltirkwl ftteeeilln dndlavtyff hqavddvkkg yikaeeksyq
      301 lqklyeqrkm vmylnmlrtc egyneiifph cacdsrrkgh vitaisithf klhacteegq
      361 lenqviafew demqrwdtde egmafcfeya rgekkprwvk iftpyfnymh ecfervfcel
      421 kwrkenifqm arsqqrdvat
//
LOCUS       NP_001401233             462 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 3 isoform 4
            precursor [Homo sapiens].
ACCESSION   NP_001401233
VERSION     NP_001401233.1
DBSOURCE    REFSEQ: accession NM_001414304.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Tang,Q., Yuan,Y., Li,L., Xu,Y., Ji,W., Xiao,S., Han,Y., Miao,W.,
            Cai,J., You,P., Chen,M., Ding,S., Li,Z., Qi,Z., Hou,W. and Luo,H.
  TITLE     Comprehensive analysis reveals that LTBR is a immune-related
            biomarker for glioma
  JOURNAL   Comput Biol Med 174, 108457 (2024)
   PUBMED   38599071
  REMARK    GeneRIF: Comprehensive analysis reveals that LTBR is a
            immune-related biomarker for glioma.
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Wu,Y., Zhao,S., Guo,W., Liu,Y., Requena Mullor,M.D.M.,
            Rodriguez,R.A. and Wei,R.
  TITLE     Systematic analysis of the prognostic value and immunological
            function of LTBR in human cancer
  JOURNAL   Aging (Albany NY) 16 (1), 129-152 (2024)
   PUBMED   38175686
  REMARK    GeneRIF: Systematic analysis of the prognostic value and
            immunological function of LTBR in human cancer.
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Shuptrine,C.W., Perez,V.M., Selitsky,S.R., Schreiber,T.H. and
            Fromm,G.
  TITLE     Shining a LIGHT on myeloid cell targeted immunotherapy
  JOURNAL   Eur J Cancer 187, 147-160 (2023)
   PUBMED   37167762
  REMARK    Review article
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Abudukeyoumu,A., Lai,Z.Z., Lu,J.J., Zhang,X., Hou,D.Y., Dong,J.,
            Wu,J.N., Li,M.Q. and Xie,F.
  TITLE     A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion
  JOURNAL   J Reprod Immunol 153, 103693 (2022)
   PUBMED   35987137
  REMARK    GeneRIF: A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion.
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Remouchamps,C., Boutaffala,L., Ganeff,C. and Dejardin,E.
  TITLE     Biology and signal transduction pathways of the
            Lymphotoxin-alphabeta/LTbetaR system
  JOURNAL   Cytokine Growth Factor Rev 22 (5-6), 301-310 (2011)
   PUBMED   22152226
  REMARK    Review article
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Nakano,H., Oshima,H., Chung,W., Williams-Abbott,L., Ware,C.F.,
            Yagita,H. and Okumura,K.
  TITLE     TRAF5, an activator of NF-kappaB and putative signal transducer for
            the lymphotoxin-beta receptor
  JOURNAL   J Biol Chem 271 (25), 14661-14664 (1996)
   PUBMED   8663299
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Browning,J.L., Miatkowski,K., Sizing,I., Griffiths,D., Zafari,M.,
            Benjamin,C.D., Meier,W. and Mackay,F.
  TITLE     Signaling through the lymphotoxin beta receptor induces the death
            of some adenocarcinoma tumor lines
  JOURNAL   J Exp Med 183 (3), 867-878 (1996)
   PUBMED   8642291
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Baens,M., Aerssens,J., van Zand,K., Van den Berghe,H. and
            Marynen,P.
  TITLE     Isolation and regional assignment of human chromosome 12p cDNAs
  JOURNAL   Genomics 29 (1), 44-52 (1995)
   PUBMED   8530100
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Crowe,P.D., VanArsdale,T.L., Walter,B.N., Ware,C.F., Hession,C.,
            Ehrenfels,B., Browning,J.L., Din,W.S., Goodwin,R.G. and Smith,C.A.
  TITLE     A lymphotoxin-beta-specific receptor
  JOURNAL   Science 264 (5159), 707-710 (1994)
   PUBMED   8171323
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Baens,M., Chaffanet,M., Cassiman,J.J., van den Berghe,H. and
            Marynen,P.
  TITLE     Construction and evaluation of a hncDNA library of human 12p
            transcribed sequences derived from a somatic cell hybrid
  JOURNAL   Genomics 16 (1), 214-218 (1993)
   PUBMED   8486360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005840.2.
            
            Summary: This gene encodes a member of the tumor necrosis factor
            receptor superfamily. The major ligands of this receptor include
            lymphotoxin alpha/beta and tumor necrosis factor ligand superfamily
            member 14. The encoded protein plays a role in signalling during
            the development of lymphoid and other organs, lipid metabolism,
            immune response, and programmed cell death. Activity of this
            receptor has also been linked to carcinogenesis. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.128315.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..462
                     /product="tumor necrosis factor receptor superfamily
                     member 3 isoform 4 precursor"
                     /note="tumor necrosis factor C receptor; lymphotoxin B
                     receptor; tumor necrosis factor receptor type III;
                     lymphotoxin beta receptor (TNFR superfamily, member 3);
                     tumor necrosis factor receptor 2-related protein"
                     /calculated_mol_wt=46777
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3049
     Region          11..195
                     /region_name="TNFRSF3"
                     /note="Tumor necrosis factor receptor superfamily member 3
                     (TNFRSF3), also known as lymphotoxin beta receptor (LTBR);
                     cd10578"
                     /db_xref="CDD:276904"
     Region          22..107
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276904"
     Region          110..151
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276904"
     Region          153..194
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276904"
     Region          175..>237
                     /region_name="TNFRSF"
                     /note="Tumor necrosis factor receptor superfamily
                     (TNFRSF); cl22855"
                     /db_xref="CDD:473981"
     Region          197..237
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276900"
     CDS             1..462
                     /gene="LTBR"
                     /gene_synonym="D12S370; LT-BETA-R; TNF-R-III; TNFCR;
                     TNFR-RP; TNFR2-RP; TNFR3; TNFRSF3"
                     /coded_by="NM_001414304.1:198..1586"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:4055"
                     /db_xref="HGNC:HGNC:6718"
                     /db_xref="MIM:600979"
ORIGIN      
        1 mllpwatsap glawgplvlg lfgllaasqp qavppyasen qtcrdqekey yepqhriccs
       61 rcppgerqwq depgprkwvt gapapsrpqr egtyvsakcs rirdtvcatc aensynehwn
      121 ylticqlcrp cdpvmgleei apctskrktq crcqpgmfca awalecthce llsdcppgte
      181 aelkdevgkg nnhcvpckag hfqntsspsa rcqphtrcen qglveaapgt aqsdttcknp
      241 leplppemsg tmlmlavllp lafflllatv fsciwkshps lcrklgsllk rrpqgegpnp
      301 vagsweppka hpyfpdlvqp llpisgdvsp vstglpaapv leagvpqqqs pldltrepql
      361 epgeqsqvah gtngihvtgg smtitgniyi yngpvlggpp gpgdlpatpe ppypipeegd
      421 pgppglstph qedgkawhla etehcgatps nrgprnqfit hd
//
LOCUS       NP_001389621            1305 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 8 [Homo sapiens].
ACCESSION   NP_001389621
VERSION     NP_001389621.1
DBSOURCE    REFSEQ: accession NM_001402692.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1305)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1305)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1305)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1305)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1305)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1305)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1305)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1305)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1305)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1305)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1053509.1,
                                           SRR14372080.4350623.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1305
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1305
                     /product="kinectin isoform 8"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=150133
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          <326..>584
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          458..1245
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1305
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402692.1:179..4096"
                     /note="isoform 8 is encoded by transcript variant 17"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqlsitskvq
      841 elqnllkgke eqmntmkavl eekekdlant gkwlqdlqee neslkahvqe vaqhnlkeas
      901 sasqfeelei vlkekenelk rleamlkere sdlssktqll qdvqdenklf ksqieqlkqq
      961 nyqqassfpp heellkvise rekeisglwn eldslkdave hqrkknnerq qqveavelea
     1021 kevlkklfpk vsvpsnlsyg ewlhgfekka kecmagtsgs eevkvlehkl keademhtll
     1081 qlecekyksv laetegilqk lqrsveqeen kwkvkvdesh ktikqmqssf tsseqelerl
     1141 rsenkdienl rrerehleme lekaemerst yvtevrelkd lltelqkkld dsyseavrqn
     1201 eelnllkaql netltklrte qnerqkvagd lhkaqqslel iqskivkaag dttviensdv
     1261 spetesseke tmsvslnqtv tqlqqllqav nqqltkekeh yqvle
//
LOCUS       NP_001428216            1577 aa            linear   PRI 21-NOV-2025
DEFINITION  dynamin-binding protein isoform a [Homo sapiens].
ACCESSION   NP_001428216 XP_011537861 XP_054221324
VERSION     NP_001428216.1
DBSOURCE    REFSEQ: accession NM_001441287.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1577)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1577)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1577)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1577)
  AUTHORS   Ouyang,C., Mu,J., Lu,Q., Li,J., Zhu,H., Wang,Q., Zou,M.H. and
            Xie,Z.
  TITLE     Autophagic degradation of KAT2A/GCN5 promotes directional migration
            of vascular smooth muscle cells by reducing TUBA/alpha-tubulin
            acetylation
  JOURNAL   Autophagy 16 (10), 1753-1770 (2020)
   PUBMED   31878840
  REMARK    GeneRIF: Autophagic degradation of KAT2A/GCN5 promotes directional
            migration of vascular smooth muscle cells by reducing
            TUBA/alpha-tubulin acetylation.
REFERENCE   5  (residues 1 to 1577)
  AUTHORS   Ansar,M., Chung,H.L., Taylor,R.L., Nazir,A., Imtiaz,S.,
            Sarwar,M.T., Manousopoulou,A., Makrythanasis,P., Saeed,S.,
            Falconnet,E., Guipponi,M., Pournaras,C.J., Ansari,M.A., Ranza,E.,
            Santoni,F.A., Ahmed,J., Shah,I., Gul,K., Black,G.C., Bellen,H.J.
            and Antonarakis,S.E.
  TITLE     Bi-allelic Loss-of-Function Variants in DNMBP Cause Infantile
            Cataracts
  JOURNAL   Am J Hum Genet 103 (4), 568-578 (2018)
   PUBMED   30290152
  REMARK    GeneRIF: DNMBP loss-of-function variants cause infantile-onset
            cataracts in humans.
REFERENCE   6  (residues 1 to 1577)
  AUTHORS   Minster,R.L., DeKosky,S.T. and Kamboh,M.I.
  TITLE     No association of dynamin binding protein (DNMBP) gene SNPs and
            Alzheimer's disease
  JOURNAL   Neurobiol Aging 29 (10), 1602-1604 (2008)
   PUBMED   17442457
  REMARK    GeneRIF: We observed no association of statistical significance in
            either the total sample or the APOE*4 non-carriers for any of the
            SNPs of Dynamin Binding Protein.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1577)
  AUTHORS   Otani,T., Ichii,T., Aono,S. and Takeichi,M.
  TITLE     Cdc42 GEF Tuba regulates the junctional configuration of simple
            epithelial cells
  JOURNAL   J Cell Biol 175 (1), 135-146 (2006)
   PUBMED   17015620
  REMARK    GeneRIF: Tuba controls the shaping of cell junctions through the
            local activation of Cdc42 and its effectors.
REFERENCE   8  (residues 1 to 1577)
  AUTHORS   Kuwano,R., Miyashita,A., Arai,H., Asada,T., Imagawa,M., Shoji,M.,
            Higuchi,S., Urakami,K., Kakita,A., Takahashi,H., Tsukie,T.,
            Toyabe,S., Akazawa,K., Kanazawa,I. and Ihara,Y.
  CONSRTM   Japanese Genetic Study Consortium for Alzeheimer's Disease
  TITLE     Dynamin-binding protein gene on chromosome 10q is associated with
            late-onset Alzheimer's disease
  JOURNAL   Hum Mol Genet 15 (13), 2170-2182 (2006)
   PUBMED   16740596
  REMARK    GeneRIF: Results confirmed DNMBP may be one of the susceptibility
            genes for Alzheimer's disease.
            GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   9  (residues 1 to 1577)
  AUTHORS   Cestra,G., Kwiatkowski,A., Salazar,M., Gertler,F. and De Camilli,P.
  TITLE     Tuba, a GEF for CDC42, links dynamin to actin regulatory proteins
  JOURNAL   Methods Enzymol 404, 537-545 (2005)
   PUBMED   16413298
REFERENCE   10 (residues 1 to 1577)
  AUTHORS   Salazar,M.A., Kwiatkowski,A.V., Pellegrini,L., Cestra,G.,
            Butler,M.H., Rossman,K.L., Serna,D.M., Sondek,J., Gertler,F.B. and
            De Camilli,P.
  TITLE     Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl
            homology domains, links dynamin to regulation of the actin
            cytoskeleton
  JOURNAL   J Biol Chem 278 (49), 49031-49043 (2003)
   PUBMED   14506234
  REMARK    GeneRIF: functions to bring together dynamin with actin regulatory
            proteins
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL441886.18, AL627434.4 and
            AL392107.17.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_011537861.1, XP_054221324.1.
            
            Summary: This gene encodes a protein belonging to the guanine
            nucleotide exchange factor family, and which regulates the
            configuration of cell junctions. It contains multiple binding sites
            for dynamin and thus links dynamin to actin regulatory proteins.
            Polymorphisms in this gene have been linked to Alzheimer's disease
            in some populations, though there are conflicting reports of such
            linkages in other populations. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3931343.1,
                                           SRR14372079.2829125.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1577
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.2"
     Protein         1..1577
                     /product="dynamin-binding protein isoform a"
                     /note="scaffold protein TUBA"
                     /calculated_mol_wt=177217
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          6..56
                     /region_name="SH3_DNMBP_N1"
                     /note="First N-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11794"
                     /db_xref="CDD:212728"
     Site            order(11,13,16,20,38..39,52,54..55)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212728"
     Region          70..123
                     /region_name="SH3_DNMBP_N2"
                     /note="Second N-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11795"
                     /db_xref="CDD:212729"
     Site            order(75,77,80,84,102..103,117,119..120)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212729"
     Region          149..199
                     /region_name="SH3_DNMBP_N3"
                     /note="Third N-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11796"
                     /db_xref="CDD:212730"
     Site            order(154,156,159,163,181..182,195,197..198)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212730"
     Region          211..244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          247..296
                     /region_name="SH3_DNMBP_N4"
                     /note="Fourth N-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11797"
                     /db_xref="CDD:212731"
     Site            order(252,254,257,261,279..280,293,295..296)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212731"
     Region          335..395
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          591..624
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          639..659
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Site            684
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          785..965
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(791,795,884,916..917,920..921,923..924,927..928,
                     931..932,935,961,965)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          1017..1208
                     /region_name="BAR_DNMBP"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin
                     Binding Protein; cd07589"
                     /db_xref="CDD:153273"
     Site            order(1029,1032..1033,1037,1039..1040,1043..1044,
                     1046..1047,1061..1062,1064..1065,1068..1069,1071..1072,
                     1075,1081,1084..1085,1169,1172..1173,1175,1180,1183..1184,
                     1186..1187,1190..1191,1194..1195,1197..1198,1201..1202,
                     1204..1205)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153273"
     Region          1289..1345
                     /region_name="SH3_DNMBP_C1"
                     /note="First C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11798"
                     /db_xref="CDD:212732"
     Site            order(1294,1296,1299,1303,1325..1326,1339,1341..1342)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212732"
     Region          1348..1487
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          1517..1573
                     /region_name="SH3_DNMBP_C2"
                     /note="Second C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba, and similar domains;
                     cd12141"
                     /db_xref="CDD:213017"
     Site            order(1522,1524,1527,1531,1553..1554,1567,1569..1570)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213017"
     CDS             1..1577
                     /gene="DNMBP"
                     /gene_synonym="ARHGEF36; CTRCT48; TUBA"
                     /coded_by="NM_001441287.1:203..4936"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="GeneID:23268"
                     /db_xref="HGNC:HGNC:30373"
                     /db_xref="MIM:611282"
ORIGIN      
        1 meagsvvrai fdfcpsvsee lplfvgdiie vlavvdefwl lgkkedvtgq fpssfveivt
       61 ipslkegerl fvciceftsq eldnlplhrg dlvildgipt agwlqgrscw gargffpssc
      121 vrelclssqs rqwhsqsalf qipeysmgqa ralmglsaql deeldfregd vitiigvpep
      181 gwfegelegr rgifpegfve llgplrtvde svssgnqddc ivngevdtpv geeeigpded
      241 eeepgtygva lyrfqalepn eldfevgdki rilatledgw legslkgrtg ifpyrfvklc
      301 pdtrveetma lpqegslari petsldclen tlgveeqrhe tsdheaeepd ciiseaptsp
      361 lghltseydt drnsyqdedt aggpprspgv ewemplatds ptsdptevvn gissqpqvpf
      421 hpnlqksqyy stvggshphs eqypdllple artrdyaslp pkrmysqlkt lqkpvlplyr
      481 gssvsasrvv kprqsspqlh nlasytkkhh tssvysiser lemkpgpqaq glvmeaaths
      541 qgdgstdlds kltqqliefe kslagpgtep dkilrhfsim dfnsekdivr gsskliteqe
      601 lperrkalrp ppprpctpvs tsphllvdqn lkpapplvvr psrpaplpps aqqrtnavsp
      661 kllsrhrptc etlekegpgh mgrsldqtsp cplvlvriee merdldmysr aqeelnlmle
      721 ekqdessrae tledlkfces nieslnmelq qlremtllss qssslvapsg svsaenpeqr
      781 mlekrakvie ellqterdyi rdlemcieri mvpmqqaqvp nidfeglfgn mqmvikvskq
      841 llaaleisda vgpvflghrd elegtykiyc qnhdeaiall eiyekdekiq khlqdsladl
      901 kslynewgct nyinlgsfli kpvqrvmryp lllmellnst peshpdkvpl tnavlavkei
      961 nvnineykrr kdlvlkyrkg dedslmekis klnihsiikk snrvsshlkh ltgfapqikd
     1021 evfeeteknf rmqerliksf irdlslylqh iresacvkvv aavsmwdvcm erghrdleqf
     1081 ervhryisdq lftnfkerte rlvisplnql lsmftgphkl vqkrfdklld fyncteraek
     1141 lkdkktleel qsarnnyeal naqlldelpk fhqyaqglft ncvhgyaeah cdfvhqaleq
     1201 lkpllsllkv agregnliai fheehsrvlq qlqvftffpe slpatkkpfe rktidrqsar
     1261 kpllglpsym lqseelrasl laryppeklf qaernfnaaq dldvsllegd lvgvikkkdp
     1321 mgsqnrwlid ngvtkgfvys sflkpynprr shsdasvgsh sstesehgss sprfprqnsg
     1381 stltfnpssm avsftsgscq kqpqdasppp kecdqgtlsa slnpsnsess psrcpsdpds
     1441 tsqprsgdsa dvardvkqpt atprsyrnfr hpeivgysvp grngqsqdlv kgcartaqap
     1501 edrstepdgs eaegnqvyfa vytfkarnpn elsvsanqkl kilefkdvtg ntewwlaevn
     1561 gkkgyvpsny irkteyt
//
LOCUS       NP_001400683             775 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform o [Homo sapiens].
ACCESSION   NP_001400683
VERSION     NP_001400683.1
DBSOURCE    REFSEQ: accession NM_001413754.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 775)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 775)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 775)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 775)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 775)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 775)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 775)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 775)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 775)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 775)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2957728.1,
                                           SRR18074969.2109494.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..775
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..775
                     /product="polyhomeotic-like protein 1 isoform o"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=82218
     Region          599..706
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          706..774
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(724..725,759..760,763..764,767)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(735..739,741..742,745..746,750,755)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..775
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413754.1:368..2695"
                     /note="isoform o is encoded by transcript variant 18"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq aspqlgnllq vnrtlgrnvp
      121 lasqlilmpn gavaavqqev psaqspgvha dadqvqnlav rnqqasaqgp qmqgstqkai
      181 ppgaspvssl sqassqalav aqassgatnq slnlsqaggg sgnsipgsmg pggggqahgg
      241 lgqlpssgmg ggscprkgtg vvqplpaaqt vtvsqgsqte aesaaakkae adgsgqqnvg
      301 mnltrtatpa psqtlissat ytqiqphsli qqqqqihlqq kqvviqqqia ihhqqqfqhr
      361 qsqllhtath lqlaqqqqqq qqqqqqqqqp qattltapqp pqgkpqtlav krkadseeer
      421 ddvstlgsml pakaspvaes pkvmdekssl gekaesvanv nantpsselv altpapsvpp
      481 ptlamvsrqm gdskppqaiv kpqilthiie gfviqegaep fpvgcsqllk esekplqtgl
      541 ptgltenqsg gplgvdspsa eldkkanllk ceycgkyapa eqfrgskrfc smtcakrynv
      601 scshqfrlkr kkmkefqean yarvrrrgpr rsssdiarak iqgkchrgqe dssrgsdnss
      661 ydealsptsp gplsvraghg erdlgnpnta pptpelhgin pvflssnpsr wsveevyefi
      721 aslqgcqeia eefrsqeidg qallllkeeh lmsamniklg palkicakin vlket
//
LOCUS       NP_001389635            1144 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 15 [Homo sapiens].
ACCESSION   NP_001389635
VERSION     NP_001389635.1
DBSOURCE    REFSEQ: accession NM_001402706.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1144)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1144)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1144)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1144)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1144)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1144)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1144)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1144)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1144)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1144)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.906856.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1144
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1144
                     /product="kinectin isoform 15"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=131859
     Region          <142..>400
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          296..1084
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1144
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402706.1:302..3736"
                     /note="isoform 15 is encoded by transcript variant 29"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mvpskrqeal plhqetkqes gsgkkkassk kqktenvfvd eplihattyi plmdnadssp
       61 vvdkrevidl lkpdqvegiq ksgtkklkte tdkenaevkf kdfllslktm mfsedealcv
      121 vdllkeksgv iqdalkkssk gelttlihql qekdkllaav kedaaatkdr ckqltqemmt
      181 ekersnvvit rmkdrigtle kehnvfqnki hvsyqetqqm qmkfqqvreq meaeiahlkq
      241 engilrdavs nttnqleskq saelnklrqd yarlvnelte ktgklqqeev qkknaeqaat
      301 qlkvqlqeae rrweevqsyi rkrtaeheaa qqdlqskfva kenevqslhs kltdtlvskq
      361 qleqrlmqlm eseqkrvnke eslqmqvqdi leqnealkaq iqqfhsqiaa qtsasvlaee
      421 lhkviaekdk qikqtedsla serdrltske eelkdiqnmn fllkaevqkl qalaneqaaa
      481 ahelekmqqs vyvkddkirl leeqlqheis nkmeefkiln dqnkalksev qklqtlvseq
      541 pnkdvveqme kciqekdekl ktveelletg liqvatkeee lnairtenss ltkevqdlka
      601 kqndqvsfas lveelkkvih ekdgkiksve elleaellkv ankektvqdl kqeikalkee
      661 ignvqlekaq qlsitskvqe lqnllkgkee qmntmkavle ekekdlantg kwlqdlqeen
      721 eslkahvqev aqhnlkeass asqfeeleiv lkekenelkr leamlkeres dlssktqllq
      781 dvqdenklfk sqieqlkqqn yqqassfpph eellkviser ekeisglwne ldslkdaveh
      841 qrkknnerqq qveaveleak evlkklfpkv svpsnlsyge wlhgfekkak ecmagtsgse
      901 evkvlehklk eademhtllq lecekyksvl aetegilqkl qrsveqeenk wkvkvdeshk
      961 tikqmqssft sseqelerlr senkdienlr rerehlemel ekaemersty vtevrelkdl
     1021 ltelqkkldd syseavrqne elnllkaqln etltklrteq nerqkvagdl hkaqqsleli
     1081 qskivkaagd ttviensdvs petesseket msvslnqtvt qlqqllqavn qqltkekehy
     1141 qvle
//
LOCUS       NP_001411049             261 aa            linear   PRI 21-NOV-2025
DEFINITION  radial spoke head protein 9 homolog isoform 4 [Homo sapiens].
ACCESSION   NP_001411049
VERSION     NP_001411049.1
DBSOURCE    REFSEQ: accession NM_001424120.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Hwang,J.Y., Chai,P., Nawaz,S., Choi,J., Lopez-Giraldez,F.,
            Hussain,S., Bilguvar,K., Mane,S., Lifton,R.P., Ahmad,W., Zhang,K.
            and Chung,J.J.
  TITLE     LRRC23 truncation impairs radial spoke 3 head assembly and sperm
            motility underlying male infertility
  JOURNAL   Elife 12, 90095 (2023)
   PUBMED   38091523
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Zhang,X., Xiao,Z., Zhang,J., Xu,C., Liu,S., Cheng,L., Zhou,S.,
            Zhao,S., Zhang,Y., Wu,J., Wang,Y. and Liu,M.
  TITLE     Differential requirements of IQUB for the assembly of radial spoke
            1 and the motility of mouse cilia and flagella
  JOURNAL   Cell Rep 41 (8), 111683 (2022)
   PUBMED   36417862
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Zhu,L., Liu,H., Chen,Y., Yan,X. and Zhu,X.
  TITLE     Rsph9 is critical for ciliary radial spoke assembly and central
            pair microtubule stability
  JOURNAL   Biol Cell 111 (2), 29-38 (2019)
   PUBMED   30383886
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Zietkiewicz,E., Bukowy-Bieryllo,Z., Voelkel,K., Klimek,B.,
            Dmenska,H., Pogorzelski,A., Sulikowska-Rowinska,A., Rutkiewicz,E.
            and Witt,M.
  TITLE     Mutations in radial spoke head genes and ultrastructural cilia
            defects in East-European cohort of primary ciliary dyskinesia
            patients
  JOURNAL   PLoS One 7 (3), e33667 (2012)
   PUBMED   22448264
  REMARK    GeneRIF: Mutations in RSPH9 leads to ultrastructural cilia defects
            and ciliary dyskinesia.
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Reish,O., Slatkin,M., Chapman-Shimshoni,D., Elizur,A., Chioza,B.,
            Castleman,V. and Mitchison,H.M.
  TITLE     Founder mutation(s) in the RSPH9 gene leading to primary ciliary
            dyskinesia in two inbred Bedouin families
  JOURNAL   Ann Hum Genet 74 (2), 117-125 (2010)
   PUBMED   20070851
  REMARK    GeneRIF: Study focused on an extended 5 generation Bedouin family,
            analysed mutation segregation, and calculated the age of the
            mutated allele in 2 families based on haplotypes and
            haplotype+microsatellite in an attempt to define the source of the
            mutation.
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Castleman,V.H., Romio,L., Chodhari,R., Hirst,R.A., de Castro,S.C.,
            Parker,K.A., Ybot-Gonzalez,P., Emes,R.D., Wilson,S.W., Wallis,C.,
            Johnson,C.A., Herrera,R.J., Rutman,A., Dixon,M., Shoemark,A.,
            Bush,A., Hogg,C., Gardiner,R.M., Reish,O., Greene,N.D.,
            O'Callaghan,C., Purton,S., Chung,E.M. and Mitchison,H.M.
  TITLE     Mutations in radial spoke head protein genes RSPH9 and RSPH4A cause
            primary ciliary dyskinesia with central-microtubular-pair
            abnormalities
  JOURNAL   Am J Hum Genet 84 (2), 197-209 (2009)
   PUBMED   19200523
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136131.15.
            
            Summary: This gene encodes a protein thought to be a component of
            the radial spoke head in motile cilia and flagella. Mutations in
            this gene are associated with primary ciliary dyskinesia 12.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Jul 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.407918.1,
                                           SRR14243140.1682449.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..261
                     /product="radial spoke head protein 9 homolog isoform 4"
                     /note="radial spoke head protein 9 homolog; radial spoke
                     head 9 homolog"
                     /calculated_mol_wt=29422
     Region          <17..254
                     /region_name="Radial_spoke"
                     /note="Radial spokehead-like protein; pfam04712"
                     /db_xref="CDD:461405"
     CDS             1..261
                     /gene="RSPH9"
                     /gene_synonym="C6orf206; CILD12; MRPS18AL1"
                     /coded_by="NM_001424120.1:64..849"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:221421"
                     /db_xref="HGNC:HGNC:21057"
                     /db_xref="MIM:612648"
ORIGIN      
        1 mdadslllsl elasgsgqgl spdrrasllt slmlvkrdyr ydrvlfwgri lglvadyyia
       61 qglsedqlap rktlyslnct ewsllppate emvaqssvvk grfmgdpsye yehtelqkvn
      121 egekvfeeei vidkavaiip rgalfktpfg pthvnrtfeg lslseakkls syfhfrepve
      181 lknktlleka dldpsldfmd slehdipkgs wsiqmergna lvvlrsllwp gltfyhaprt
      241 knygyvyvgt geknmdlpfm l
//
LOCUS       NP_001427515             400 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb protein EED isoform b [Homo sapiens].
ACCESSION   NP_001427515
VERSION     NP_001427515.1
DBSOURCE    REFSEQ: accession NM_001440586.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 400)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 400)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 400)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 400)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003084.2.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF099032.1, SRR14038192.1167755.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..400
                     /product="polycomb protein EED isoform b"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=45393
     Region          1..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q921E6; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            66
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918; N6-methyllysine,
                     alternate. /evidence=ECO:0000269|PubMed:20974918;
                     propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Region          96..140
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          148..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          149..303
                     /region_name="Required for interaction with the matrix
                     protein MA of HIV-1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Region          150..398
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          193..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            197
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918; N6-methyllysine,
                     alternate. /evidence=ECO:0000269|PubMed:20974918;
                     propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Region          240..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            268
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918; N6-methyllysine,
                     alternate. /evidence=ECO:0000269|PubMed:20974918;
                     propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Site            284
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918; N6-methyllysine,
                     alternate. /evidence=ECO:0000269|PubMed:20974918;
                     propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Region          309..357
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          365..391
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..400
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_001440586.1:478..1680"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdendd avsiesgtnt erpdtptntp
       61 napgrkswgk gkwkskkcky sfkcvnslke dhnqplfgvq fnwhskegdp lvfatvgsnr
      121 vtlyechsqg eirllqsyvd adadenfytc awtydsntsh pllavagsrg iiriinpitm
      181 qcikhyvghg nainelkfhp rdpnlllsvs kdhalrlwni qtdtlvaifg gveghrdevl
      241 sadydllgek imscgmdhsl klwrinskrm mnaikesydy npnktnrpfi sqkihfpdfs
      301 trdihrnyvd cvrwlgdlil skscenaivc wkpgkmeddi dkikpsesnv tilgrfdysq
      361 cdiwymrfsm dfwqkmlalg nqvgklyvwd levedphkak
//
LOCUS       NP_001392810            1026 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 8 [Homo sapiens].
ACCESSION   NP_001392810
VERSION     NP_001392810.1
DBSOURCE    REFSEQ: accession NM_001405881.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 1026)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 1026)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 1026)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 1026)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1026)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 1026)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 1026)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR12921934.1230387.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1026
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 8"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=112485
     Region          850..>912
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..1026
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405881.1:251..3331"
                     /note="isoform 8 is encoded by transcript variant 22"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 maamapaltd aaaeahhirf klappsstls pgsaenngna niliaangtk rkaiaaedps
       61 ldfrnnptke dlgklqplva sylcsdvtsv pskeslklqg vfskqtvlks hpllsqsyel
      121 raellgrqpv lefslenlrt mntsgqtalp qapvnglakk ltkssthsdh dnstslnggk
      181 raltssalhg gemggsesgd lkggmtnctl phrsldveht tlysnnstan kssvnsmeqp
      241 alqgssrlsp gtdsssnlgg vklegkkspl ssilfsalds dtritallrr qadiesrarr
      301 lqkrlqvvqa kqverhiqhq lggflektls klpnleslrp rsqlmltrka eaalrkaase
      361 tttseglsnf lksnsiseel erftasgian lrcseqafds dvtdsssgge sdieeeeltr
      421 adpeqrhvpl rrrsewkwaa draaivsrwn wlqahvsdle yrirqqtdiy kqirankies
      481 vsqplenhga piighisesl stkscgalrp vngvintlqp vladhipgds sdaeeqlhkk
      541 qrlnlvssss dgtcvaartr pvlsckkrrl vrpnsivpls kkvhrnstir pgcdvnpsca
      601 lcgsgsintm ppeihyeapl lerlsqldsc vhpvlafpdd vptslhfqsm lksqwqnkpf
      661 dkikppkkls lkhrapmpgs lpdsarkdrh klvssfltta klshhqtrpd rthrqhlddv
      721 gavpmvervt apkaerllnp pppvhdpnhs kmrlrdhsse rsevlkhhtd mssssylaat
      781 hhpphsplvr qlstssdspa passssqvta stsqpvrrrr gessfdinni vipmsvaatt
      841 rveklqykei ltpswrevdl qslkgspdee neeiedlsda afaalhakce emerarwlwt
      901 tsvppqrrgs rspispelhs apltpvardt prhlasedtr cstpelglde qsvqpwerrt
      961 fplahspqae cedqldaqer aarctrrtsg sktgreteaa ptsppivplk srhlvaaata
     1021 qrpthr
//
LOCUS       NP_001427920             516 aa            linear   PRI 21-NOV-2025
DEFINITION  complement factor I isoform 13 precursor [Homo sapiens].
ACCESSION   NP_001427920 XP_047271610 XP_054205922
VERSION     NP_001427920.1
DBSOURCE    REFSEQ: accession NM_001440991.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Moreno,R. and Broderick,L.
  TITLE     Complement factor I deficiency: Diverse phenotypes
  JOURNAL   J Allergy Clin Immunol 156 (2), 305-307 (2025)
   PUBMED   40127737
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Schwotzer,N., Fakhouri,F., Martins,P.V., Delmas,Y., Caillard,S.,
            Zuber,J., Moranne,O., Mesnard,L., Fremeaux-Bacchi,V. and
            El-Sissy,C.
  TITLE     Hot Spot of Complement Factor I Rare Variant p.Ile357Met in
            Patients With Hemolytic Uremic Syndrome
  JOURNAL   Am J Kidney Dis 84 (2), 244-249 (2024)
   PUBMED   38423159
  REMARK    GeneRIF: Hot Spot of Complement Factor I Rare Variant p.Ile357Met
            in Patients With Hemolytic Uremic Syndrome.
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Felberg,A., Bienkowski,M., Stokowy,T., Myszczynski,K.,
            Polakiewicz,Z., Kitowska,K., Sadej,R., Mohlin,F., Kuzniewska,A.,
            Kowalska,D., Stasilojc,G., Jongerius,I., Spaapen,R.,
            Mesa-Guzman,M., Montuenga,L.M., Blom,A.M., Pio,R. and Okroj,M.
  TITLE     Elevated expression of complement factor I in lung cancer cells
            associates with shorter survival-Potentially via non-canonical
            mechanism
  JOURNAL   Transl Res 269, 1-13 (2024)
   PUBMED   38395390
  REMARK    GeneRIF: Elevated expression of complement factor I in lung cancer
            cells associates with shorter survival-Potentially via
            non-canonical mechanism.
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Massey,V., Nguyen,C.E., Francois,T., De Bruycker,J.J., Bonnefoy,A.,
            Lapeyraque,A.L. and Decaluwe,H.
  TITLE     CNS Inflammation as the First Sign of Complement Factor I
            Deficiency: A Severe Myelitis Treated With Intense Immunotherapy
            and Eculizumab
  JOURNAL   Neurol Neuroimmunol Neuroinflamm 11 (2), e200191 (2024)
   PUBMED   38134378
  REMARK    GeneRIF: CNS Inflammation as the First Sign of Complement Factor I
            Deficiency.
REFERENCE   5  (residues 1 to 516)
  AUTHORS   van de Ven,J.P., Nilsson,S.C., Tan,P.L., Buitendijk,G.H.,
            Ristau,T., Mohlin,F.C., Nabuurs,S.B., Schoenmaker-Koller,F.E.,
            Smailhodzic,D., Campochiaro,P.A., Zack,D.J., Duvvari,M.R.,
            Bakker,B., Paun,C.C., Boon,C.J., Uitterlinden,A.G., Liakopoulos,S.,
            Klevering,B.J., Fauser,S., Daha,M.R., Katsanis,N., Klaver,C.C.,
            Blom,A.M., Hoyng,C.B. and den Hollander,A.I.
  TITLE     A functional variant in the CFI gene confers a high risk of
            age-related macular degeneration
  JOURNAL   Nat Genet 45 (7), 813-817 (2013)
   PUBMED   23685748
  REMARK    GeneRIF: these findings demonstrate that rare, highly penetrant
            mutations in CFI contribute to the genetic burden of age-related
            macular degeneration.
REFERENCE   6  (residues 1 to 516)
  AUTHORS   Martin,B. and Smith,R.J.H.
  TITLE     C3 Glomerulopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301598
REFERENCE   7  (residues 1 to 516)
  AUTHORS   Noris,M., Bresin,E., Mele,C. and Remuzzi,G.
  TITLE     Genetic Atypical Hemolytic-Uremic Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301541
REFERENCE   8  (residues 1 to 516)
  AUTHORS   DiScipio,R.G.
  TITLE     Ultrastructures and interactions of complement factors H and I
  JOURNAL   J Immunol 149 (8), 2592-2599 (1992)
   PUBMED   1401896
REFERENCE   9  (residues 1 to 516)
  AUTHORS   Shiang,R., Murray,J.C., Morton,C.C., Buetow,K.H., Wasmuth,J.J.,
            Olney,A.H., Sanger,W.G. and Goldberger,G.
  TITLE     Mapping of the human complement factor I gene to 4q25
  JOURNAL   Genomics 4 (1), 82-86 (1989)
   PUBMED   2563353
REFERENCE   10 (residues 1 to 516)
  AUTHORS   Catterall,C.F., Lyons,A., Sim,R.B., Day,A.J. and Harris,T.J.
  TITLE     Characterization of primary amino acid sequence of human complement
            control protein factor I from an analysis of cDNA clones
  JOURNAL   Biochem J 242 (3), 849-856 (1987)
   PUBMED   2954545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC126283.3.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047271610.1, XP_054205922.1.
            
            Summary: This gene encodes a serine proteinase that is essential
            for regulating the complement cascade. The encoded preproprotein is
            cleaved to produce both heavy and light chains, which are linked by
            disulfide bonds to form a heterodimeric glycoprotein. This
            heterodimer can cleave and inactivate the complement components C4b
            and C3b, and it prevents the assembly of the C3 and C5 convertase
            enzymes. Defects in this gene cause complement factor I deficiency,
            an autosomal recessive disease associated with a susceptibility to
            pyogenic infections. Mutations in this gene have been associated
            with a predisposition to atypical hemolytic uremic syndrome, a
            disease characterized by acute renal failure, microangiopathic
            hemolytic anemia and thrombocytopenia. Primary glomerulonephritis
            with immune deposits and age-related macular degeneration are other
            conditions associated with mutations of this gene. [provided by
            RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.3865628.1,
                                           SRR14372079.308670.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..516
                     /product="complement factor I isoform 13 precursor"
                     /EC_number="3.4.21.45"
                     /note="C3b-inactivator; Konglutinogen-activating factor;
                     complement factor I heavy chain; complement component I;
                     C3B/C4B inactivator; complement control protein factor I;
                     light chain of factor I"
                     /calculated_mol_wt=56196
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2281
     Region          43..108
                     /region_name="FIMAC"
                     /note="factor I membrane attack complex; smart00057"
                     /db_xref="CDD:214493"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Region          114..215
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:21768352, ECO:0007744|PDB:2XRC;
                     propagated from UniProtKB/Swiss-Prot (P05156.2)"
     Region          224..256
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(227,235,246..247)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(239,242,246,252..253)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            249..253
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          257..293
                     /region_name="Ldl_recept_a"
                     /note="Low-density lipoprotein receptor domain class A;
                     pfam00057"
                     /db_xref="CDD:395011"
     Site            order(264,272,283..284)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(276,279,283,289..290)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            286..290
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          332..>505
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; smart00020"
                     /db_xref="CDD:214473"
     Site            333
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            457
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     Site            487
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21768352,
                     ECO:0007744|PDB:2XRC; propagated from UniProtKB/Swiss-Prot
                     (P05156.2)"
     CDS             1..516
                     /gene="CFI"
                     /gene_synonym="AHUS3; ARMD13; C3b-INA; C3BINA; FI; IF;
                     KAF"
                     /coded_by="NM_001440991.1:29..1579"
                     /note="isoform 13 precursor is encoded by transcript
                     variant 18"
                     /db_xref="GeneID:3426"
                     /db_xref="HGNC:HGNC:5394"
                     /db_xref="MIM:217030"
ORIGIN      
        1 mkllhvfllf lcfhlrfckv tytsqedlve kkclakkyth lscdkvfcqp wqrciegtcv
       61 cklpyqcpkn gtavcatnrr sfptycqqks leclhpgtkf lnngtctaeg kfsvslkhgn
      121 tdsegivevk lvdqdktmfi cksswsmrea nvacldlgfq qgadtqrrfk lsdlsinste
      181 clhvhcrgle tslaectftk rrtmgyqdfa dvvcytqkad spmddffqcv ngkyisqmka
      241 cdgindcgdq sdelcckacq gkgfhcksgv cipsqyqcng evdcitgede vgcaeeteil
      301 tadmdaerrr iksllpklsc gvknrmhirr krivggkraq lgdlpwqvai kdasgitcgg
      361 iyiggcwilt aahclraskt hryqiwttvv dwihpdlkri vieyvdriif henynagtyq
      421 ndialiemkk dgnkkdcelp rsipacvpws pylfqpndtc ivsgwgrekd nervfslqwg
      481 evklisncsk fygnrfyeke mecagcnlis vlsrik
//
LOCUS       NP_001402860             408 aa            linear   PRI 21-NOV-2025
DEFINITION  solute carrier family 35 member F1 [Homo sapiens].
ACCESSION   NP_001402860 XP_005266922
VERSION     NP_001402860.1
DBSOURCE    REFSEQ: accession NM_001415931.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Van den Bossche,F., Tevel,V., Gilis,F., Gaussin,J.F., Boonen,M. and
            Jadot,M.
  TITLE     Residence of the Nucleotide Sugar Transporter Family Members
            SLC35F1 and SLC35F6 in the Endosomal/Lysosomal Pathway
  JOURNAL   Int J Mol Sci 25 (12), 6718 (2024)
   PUBMED   38928424
  REMARK    GeneRIF: Residence of the Nucleotide Sugar Transporter Family
            Members SLC35F1 and SLC35F6 in the Endosomal/Lysosomal Pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Thibord,F., Chan,M.V., Chen,M.H. and Johnson,A.D.
  TITLE     A year of COVID-19 GWAS results from the GRASP portal reveals
            potential genetic risk factors
  JOURNAL   HGG Adv 3 (2), 100095 (2022)
   PUBMED   35224516
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Qian,C., Wu,Z., Sun,R., Yu,H., Zeng,J., Rao,Y. and Li,Y.
  TITLE     Localization, proteomics, and metabolite profiling reveal a
            putative vesicular transporter for UDP-glucose
  JOURNAL   Elife 10, e65417 (2021)
   PUBMED   34269178
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Eijgelsheim,M., Newton-Cheh,C., Sotoodehnia,N., de Bakker,P.I.,
            Muller,M., Morrison,A.C., Smith,A.V., Isaacs,A., Sanna,S., Dorr,M.,
            Navarro,P., Fuchsberger,C., Nolte,I.M., de Geus,E.J., Estrada,K.,
            Hwang,S.J., Bis,J.C., Ruckert,I.M., Alonso,A., Launer,L.J.,
            Hottenga,J.J., Rivadeneira,F., Noseworthy,P.A., Rice,K.M., Perz,S.,
            Arking,D.E., Spector,T.D., Kors,J.A., Aulchenko,Y.S., Tarasov,K.V.,
            Homuth,G., Wild,S.H., Marroni,F., Gieger,C., Licht,C.M.,
            Prineas,R.J., Hofman,A., Rotter,J.I., Hicks,A.A., Ernst,F.,
            Najjar,S.S., Wright,A.F., Peters,A., Fox,E.R., Oostra,B.A.,
            Kroemer,H.K., Couper,D., Volzke,H., Campbell,H., Meitinger,T.,
            Uda,M., Witteman,J.C., Psaty,B.M., Wichmann,H.E., Harris,T.B.,
            Kaab,S., Siscovick,D.S., Jamshidi,Y., Uitterlinden,A.G.,
            Folsom,A.R., Larson,M.G., Wilson,J.F., Penninx,B.W., Snieder,H.,
            Pramstaller,P.P., van Duijn,C.M., Lakatta,E.G., Felix,S.B.,
            Gudnason,V., Pfeufer,A., Heckbert,S.R., Stricker,B.H.,
            Boerwinkle,E. and O'Donnell,C.J.
  TITLE     Genome-wide association analysis identifies multiple loci related
            to resting heart rate
  JOURNAL   Hum Mol Genet 19 (19), 3885-3894 (2010)
   PUBMED   20639392
  REMARK    GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Karasik,D., Hsu,Y.H., Zhou,Y., Cupples,L.A., Kiel,D.P. and
            Demissie,S.
  TITLE     Genome-wide pleiotropy of osteoporosis-related phenotypes: the
            Framingham Study
  JOURNAL   J Bone Miner Res 25 (7), 1555-1563 (2010)
   PUBMED   20200953
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 408)
  AUTHORS   Nolte,I.M., Wallace,C., Newhouse,S.J., Waggott,D., Fu,J.,
            Soranzo,N., Gwilliam,R., Deloukas,P., Savelieva,I., Zheng,D.,
            Dalageorgou,C., Farrall,M., Samani,N.J., Connell,J., Brown,M.,
            Dominiczak,A., Lathrop,M., Zeggini,E., Wain,L.V., Newton-Cheh,C.,
            Eijgelsheim,M., Rice,K., de Bakker,P.I., Pfeufer,A., Sanna,S.,
            Arking,D.E., Asselbergs,F.W., Spector,T.D., Carter,N.D.,
            Jeffery,S., Tobin,M., Caulfield,M., Snieder,H., Paterson,A.D.,
            Munroe,P.B. and Jamshidi,Y.
  CONSRTM   Wellcome Trust Case Control Consortium; DCCT/EDIC Research Group;
            QTGEN consortium; QTSCD consortium
  TITLE     Common genetic variation near the phospholamban gene is associated
            with cardiac repolarisation: meta-analysis of three genome-wide
            association studies
  JOURNAL   PLoS One 4 (7), e6138 (2009)
   PUBMED   19587794
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 408)
  AUTHORS   Vasan,R.S., Glazer,N.L., Felix,J.F., Lieb,W., Wild,P.S.,
            Felix,S.B., Watzinger,N., Larson,M.G., Smith,N.L., Dehghan,A.,
            Grosshennig,A., Schillert,A., Teumer,A., Schmidt,R., Kathiresan,S.,
            Lumley,T., Aulchenko,Y.S., Konig,I.R., Zeller,T., Homuth,G.,
            Struchalin,M., Aragam,J., Bis,J.C., Rivadeneira,F., Erdmann,J.,
            Schnabel,R.B., Dorr,M., Zweiker,R., Lind,L., Rodeheffer,R.J.,
            Greiser,K.H., Levy,D., Haritunians,T., Deckers,J.W., Stritzke,J.,
            Lackner,K.J., Volker,U., Ingelsson,E., Kullo,I., Haerting,J.,
            O'Donnell,C.J., Heckbert,S.R., Stricker,B.H., Ziegler,A.,
            Reffelmann,T., Redfield,M.M., Werdan,K., Mitchell,G.F., Rice,K.,
            Arnett,D.K., Hofman,A., Gottdiener,J.S., Uitterlinden,A.G.,
            Meitinger,T., Blettner,M., Friedrich,N., Wang,T.J., Psaty,B.M., van
            Duijn,C.M., Wichmann,H.E., Munzel,T.F., Kroemer,H.K.,
            Benjamin,E.J., Rotter,J.I., Witteman,J.C., Schunkert,H.,
            Schmidt,H., Volzke,H. and Blankenberg,S.
  TITLE     Genetic variants associated with cardiac structure and function: a
            meta-analysis and replication of genome-wide association data
  JOURNAL   JAMA 302 (2), 168-178 (2009)
   PUBMED   19584346
  REMARK    GeneRIF: Meta-analysis and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   10 (residues 1 to 408)
  AUTHORS   Newton-Cheh,C., Eijgelsheim,M., Rice,K.M., de Bakker,P.I., Yin,X.,
            Estrada,K., Bis,J.C., Marciante,K., Rivadeneira,F.,
            Noseworthy,P.A., Sotoodehnia,N., Smith,N.L., Rotter,J.I.,
            Kors,J.A., Witteman,J.C., Hofman,A., Heckbert,S.R., O'Donnell,C.J.,
            Uitterlinden,A.G., Psaty,B.M., Lumley,T., Larson,M.G. and
            Stricker,B.H.
  TITLE     Common variants at ten loci influence QT interval duration in the
            QTGEN Study
  JOURNAL   Nat Genet 41 (4), 399-406 (2009)
   PUBMED   19305408
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136478.9, Z95326.1, AL449196.1 and AL133379.3.
            
            On Jan 5, 2023 this sequence version replaced XP_005266922.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.869173.1,
                                           SRR1660809.315496.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.2-q22.31"
     Protein         1..408
                     /product="solute carrier family 35 member F1"
                     /calculated_mol_wt=45215
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Region          56..355
                     /region_name="SLC35F"
                     /note="Solute carrier family 35; pfam06027"
                     /db_xref="CDD:283644"
     Site            60..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            129..147
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            158..178
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            186..206
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            221..241
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            247..267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            284..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            311..331
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            335..355
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     CDS             1..408
                     /gene="SLC35F1"
                     /gene_synonym="C6orf169; dJ230I3.1"
                     /coded_by="NM_001415931.1:464..1690"
                     /db_xref="GeneID:222553"
                     /db_xref="HGNC:HGNC:21483"
                     /db_xref="MIM:620349"
ORIGIN      
        1 mippeqpqqq lqppspappn hvvttienlp aegsggggsl sassragvrq rirkvlnrem
       61 lisvalgqvl sllicgiglt skylsedfha ntpvfqsfln yillflvytt tlavrqgeen
      121 llailrrrww kymilglidl eanylvvkay qyttltsiql ldcfvipvvi llswffllir
      181 ykavhfigiv vcilgmgcmv gadvlvgrhq gagenklvgd llvlggatly gisnvweeyi
      241 irtlsrvefl gmiglfgaff sgiqlaimeh kellkvpwdw qigllyvgfs acmfglysfm
      301 pvvikktsat svnlslltad lyslfcglfl fhykfsglyl lsfftiligl vlysststyi
      361 aqdprvykqf rnpsgpvvdl pttaqvepsv tytslgqete eephvrva
//
LOCUS       NP_001392814             619 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 12 [Homo sapiens].
ACCESSION   NP_001392814
VERSION     NP_001392814.1
DBSOURCE    REFSEQ: accession NM_001405885.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 619)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 619)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 619)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 619)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 619)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 619)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 619)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2122682.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..619
                     /product="KAT8 regulatory NSL complex subunit 1 isoform
                     12"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=68230
     Region          399..519
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..619
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405885.1:139..1998"
                     /note="isoform 12 is encoded by transcript variant 26"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 mllgcllrrr rsewkwaadr aaivsrwnwl qahvsdleyr irqqtdiykq irankglivl
       61 gevpppehtt dlflplssev ktdhgtdkli esvsqplenh gapiighise slstkscgal
      121 rpvngvintl qpvladhipg dssdaeeqlh kkqrlnlvss ssdgtcvaar trpvlsckkr
      181 rlvrpnsivp lskkvhrnst irpgcdvnps calcgsgsin tmppeihyea pllerlsqld
      241 scvhpvlafp ddvptslhfq smlksqwqnk pfdkikppkk lslkhrapmp gslpdsarkd
      301 rhklvssflt tamlkhhtdm ssssylaath hpphsplvrq lstssdspap assssqvtas
      361 tsqpvrrrrg essfdinniv ipmsvaattr veklqykeil tpswrevdlq slkgspdeen
      421 eeiedlsdaa faalhakcee merarwlwtt svppqrrgsr syrssdgrtt pqlgsanpst
      481 pqpaspdvss shslseyshg qsprspispe lhsapltpva rdtprhlase dtrcstpelg
      541 ldeqsvqpwe rrtfplahsp qaecedqlda qeraarctrr tsgsktgret eaaptsppiv
      601 plksrhlvaa ataqrpthr
//
LOCUS       NP_001401154             156 aa            linear   PRI 21-NOV-2025
DEFINITION  natural killer cells antigen CD94 isoform 6 [Homo sapiens].
ACCESSION   NP_001401154
VERSION     NP_001401154.1
DBSOURCE    REFSEQ: accession NM_001414225.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Verma,K., Croft,W., Pearce,H., Zuo,J., Stephens,C., Nunnick,J.,
            Kinsella,F.A., Malladi,R. and Moss,P.
  TITLE     Early expression of CD94 and loss of CD96 on CD8+ T cells after
            allogeneic stem cell tranplantation is predictive of subsequent
            relapse and survival
  JOURNAL   Haematologica 108 (2), 433-443 (2023)
   PUBMED   35924575
  REMARK    GeneRIF: Early expression of CD94 and loss of CD96 on CD8+ T cells
            after allogeneic stem cell tranplantation is predictive of
            subsequent relapse and survival.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Fang,H., Wang,W., Kadia,T.M., El Hussein,S., Wang,S.A. and
            Khoury,J.D.
  TITLE     CD94 expression patterns in reactive and neoplastic T-cell and
            NK-cell proliferations
  JOURNAL   Leuk Res 108, 106614 (2021)
   PUBMED   33990003
  REMARK    GeneRIF: CD94 expression patterns in reactive and neoplastic T-cell
            and NK-cell proliferations.
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Zhang,Q., Zheng,Y., Ning,M. and Li,T.
  TITLE     KLRD1, FOSL2 and LILRB3 as potential biomarkers for plaques
            progression in acute myocardial infarction and stable coronary
            artery disease
  JOURNAL   BMC Cardiovasc Disord 21 (1), 344 (2021)
   PUBMED   34271875
  REMARK    GeneRIF: KLRD1, FOSL2 and LILRB3 as potential biomarkers for
            plaques progression in acute myocardial infarction and stable
            coronary artery disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Prasnikar,E., Perdih,A. and Borisek,J.
  TITLE     Nonameric Peptide Orchestrates Signal Transduction in the
            Activating HLA-E/NKG2C/CD94 Immune Complex as Revealed by All-Atom
            Simulations
  JOURNAL   Int J Mol Sci 22 (13), 6670 (2021)
   PUBMED   34206395
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 156)
  AUTHORS   Shreeve,N., Depierreux,D., Hawkes,D., Traherne,J.A., Sovio,U.,
            Huhn,O., Jayaraman,J., Horowitz,A., Ghadially,H., Perry,J.R.B.,
            Moffett,A., Sled,J.G., Sharkey,A.M. and Colucci,F.
  TITLE     The CD94/NKG2A inhibitory receptor educates uterine NK cells to
            optimize pregnancy outcomes in humans and mice
  JOURNAL   Immunity 54 (6), 1231-1244 (2021)
   PUBMED   33887202
  REMARK    GeneRIF: The CD94/NKG2A inhibitory receptor educates uterine NK
            cells to optimize pregnancy outcomes in humans and mice.
REFERENCE   6  (residues 1 to 156)
  AUTHORS   Brooks,A.G., Posch,P.E., Scorzelli,C.J., Borrego,F. and
            Coligan,J.E.
  TITLE     NKG2A complexed with CD94 defines a novel inhibitory natural killer
            cell receptor
  JOURNAL   J Exp Med 185 (4), 795-800 (1997)
   PUBMED   9034158
REFERENCE   7  (residues 1 to 156)
  AUTHORS   Lazetic,S., Chang,C., Houchins,J.P., Lanier,L.L. and Phillips,J.H.
  TITLE     Human natural killer cell receptors involved in MHC class I
            recognition are disulfide-linked heterodimers of CD94 and NKG2
            subunits
  JOURNAL   J Immunol 157 (11), 4741-4745 (1996)
   PUBMED   8943374
REFERENCE   8  (residues 1 to 156)
  AUTHORS   Phillips,J.H., Chang,C., Mattson,J., Gumperz,J.E., Parham,P. and
            Lanier,L.L.
  TITLE     CD94 and a novel associated protein (94AP) form a NK cell receptor
            involved in the recognition of HLA-A, HLA-B, and HLA-C allotypes
  JOURNAL   Immunity 5 (2), 163-172 (1996)
   PUBMED   8769479
REFERENCE   9  (residues 1 to 156)
  AUTHORS   Chang,C., Rodriguez,A., Carretero,M., Lopez-Botet,M., Phillips,J.H.
            and Lanier,L.L.
  TITLE     Molecular characterization of human CD94: a type II membrane
            glycoprotein related to the C-type lectin superfamily
  JOURNAL   Eur J Immunol 25 (9), 2433-2437 (1995)
   PUBMED   7589107
REFERENCE   10 (residues 1 to 156)
  AUTHORS   Moretta,A., Vitale,M., Sivori,S., Bottino,C., Morelli,L.,
            Augugliaro,R., Barbaresi,M., Pende,D., Ciccone,E., Lopez-Botet,M.
            and Moretta,L.
  TITLE     Human natural killer cell receptors for HLA-class I molecules.
            Evidence that the Kp43 (CD94) molecule functions as receptor for
            HLA-B alleles
  JOURNAL   J Exp Med 180 (2), 545-555 (1994)
   PUBMED   8046333
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022075.29.
            
            Summary: Natural killer (NK) cells are a distinct lineage of
            lymphocytes that mediate cytotoxic activity and secrete cytokines
            upon immune stimulation. Several genes of the C-type lectin
            superfamily, including members of the NKG2 family, are expressed by
            NK cells and may be involved in the regulation of NK cell function.
            KLRD1 (CD94) is an antigen preferentially expressed on NK cells and
            is classified as a type II membrane protein because it has an
            external C terminus. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, May
            2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138524.337021.1, CV030397.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..156
                     /product="natural killer cells antigen CD94 isoform 6"
                     /note="natural killer cells antigen CD94; CD94 antigen;
                     KP43; NK cell receptor; killer cell lectin-like receptor
                     subfamily D, member 1"
                     /calculated_mol_wt=17863
     Region          38..153
                     /region_name="CLECT_NK_receptors_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in natural killer cell receptors (NKRs); cd03593"
                     /db_xref="CDD:153063"
     Site            order(91,118,136,139..140)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153063"
     CDS             1..156
                     /gene="KLRD1"
                     /gene_synonym="CD94"
                     /coded_by="NM_001414225.1:94..564"
                     /note="isoform 6 is encoded by transcript variant 11"
                     /db_xref="GeneID:3824"
                     /db_xref="HGNC:HGNC:6378"
                     /db_xref="MIM:602894"
ORIGIN      
        1 mstlgillkn sftklsiepa ftpgpnielq kdsdccscqe kwvgyrcncy fisseqktwn
       61 esrhlcasqk ssllqlqntd eldfmsssqq fywiglsyse ehtawlweng salsqylfps
      121 fetfntknci aynpngnald escedknryi ckqqli
//
LOCUS       NP_001402994             330 aa            linear   PRI 21-NOV-2025
DEFINITION  DDB1- and CUL4-associated factor 13 isoform 2 [Homo sapiens].
ACCESSION   NP_001402994
VERSION     NP_001402994.1
DBSOURCE    REFSEQ: accession NM_001416065.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Tang,Z.Y., Wang,X.M., Xu,C.W., Sun,Q.Q., Hua,Y.X., Zhou,Q.Y.,
            Hu,H.Y., Liu,S.B., Guo,Y.J., Ao,L., Che,X., Zhang,X.C., Heger,M.,
            Zheng,X., Liu,A.J., Wang,Q., Zhan,Z.J., Cheng,S.Q. and Pan,W.W.
  TITLE     DCAF13 promotes ovarian cancer progression by activating
            FRAS1-mediated FAK signaling pathway
  JOURNAL   Cell Mol Life Sci 81 (1), 421 (2024)
   PUBMED   39367995
  REMARK    GeneRIF: DCAF13 promotes ovarian cancer progression by activating
            FRAS1-mediated FAK signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Ren,P., Tong,X., Li,J., Jiang,H., Liu,S., Li,X., Lai,M., Yang,W.,
            Rong,Y., Zhang,Y., Jin,J., Ma,Y., Pan,W., Fan,H.Y., Zhang,S. and
            Zhang,Y.L.
  TITLE     CRL4DCAF13 E3 ubiquitin ligase targets MeCP2 for degradation to
            prevent DNA hypermethylation and ensure normal transcription in
            growing oocytes
  JOURNAL   Cell Mol Life Sci 81 (1), 165 (2024)
   PUBMED   38578457
  REMARK    GeneRIF: CRL4[DCAF13] E3 ubiquitin ligase targets MeCP2 for
            degradation to prevent DNA hypermethylation and ensure normal
            transcription in growing oocytes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Manzoor,H., Zahid,H., Emerling,C.A., Kumar,K.R., Hussain,H.M.J.,
            Seo,G.H., Wajid,M. and Naz,S.
  TITLE     A biallelic variant of DCAF13 implicated in a neuromuscular
            disorder in humans
  JOURNAL   Eur J Hum Genet 31 (6), 629-637 (2023)
   PUBMED   36797467
  REMARK    GeneRIF: A biallelic variant of DCAF13 implicated in a
            neuromuscular disorder in humans.
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Wei,S., Lu,K., Xing,J. and Yu,W.
  TITLE     A multidimensional pan-cancer analysis of DCAF13 and its
            protumorigenic effect in lung adenocarcinoma
  JOURNAL   FASEB J 37 (4), e22849 (2023)
   PUBMED   36884358
  REMARK    GeneRIF: A multidimensional pan-cancer analysis of DCAF13 and its
            protumorigenic effect in lung adenocarcinoma.
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Yan,X., Rong,M., Zhou,Q. and Zhang,C.
  TITLE     DCAF13 is essential for the pathogenesis of preeclampsia through
            its involvement in endometrial decidualization
  JOURNAL   Mol Cell Endocrinol 556, 111741 (2022)
   PUBMED   35932979
  REMARK    GeneRIF: DCAF13 is essential for the pathogenesis of preeclampsia
            through its involvement in endometrial decidualization.
REFERENCE   6  (residues 1 to 330)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 330)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 330)
  AUTHORS   Urano,T., Shiraki,M., Usui,T., Sasaki,N., Ouchi,Y. and Inoue,S.
  TITLE     Identification of non-synonymous polymorphisms in the WDSOF1 gene
            as novel susceptibility markers for low bone mineral density in
            Japanese postmenopausal women
  JOURNAL   Bone 47 (3), 636-642 (2010)
   PUBMED   20601284
  REMARK    GeneRIF: This study suggests that non-synonymous WDSOF1
            polymorphisms play a role in the genetic susceptibility to
            osteoporosis.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 330)
  AUTHORS   Jin,J., Arias,E.E., Chen,J., Harper,J.W. and Walter,J.C.
  TITLE     A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
            which is required for S phase destruction of the replication factor
            Cdt1
  JOURNAL   Mol Cell 23 (5), 709-721 (2006)
   PUBMED   16949367
REFERENCE   10 (residues 1 to 330)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012213.8.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3507283.1,
                                           SRR14038195.999506.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..330
                     /product="DDB1- and CUL4-associated factor 13 isoform 2"
                     /note="WD repeats and SOF1 domain containing; WD repeat
                     and SOF domain-containing protein 1"
                     /calculated_mol_wt=38179
     Region          <12..238
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          44..79
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          85..122
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          126..163
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          171..209
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          213..244
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          239..320
                     /region_name="Sof1"
                     /note="Sof1-like domain; pfam04158"
                     /db_xref="CDD:427753"
     CDS             1..330
                     /gene="DCAF13"
                     /gene_synonym="GM83; HSPC064; Sof1; WDSOF1"
                     /coded_by="NM_001416065.1:99..1091"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25879"
                     /db_xref="HGNC:HGNC:24535"
                     /db_xref="MIM:616196"
ORIGIN      
        1 msakpswtyr evgddktvkq wkmdgpgygd eeeplhtilg ktvytgidhh wkeavfatcg
       61 qqvdiwdeqr tnpicsmtwg fdsissvkfn pietfllgsc asdrnivlyd mrqatplkkv
      121 ildmrtntic wnpmeafift aanedynlyt fdmraldtpv mvhmdhvsav ldvdysptgk
      181 efvsasfdks irifpvdksr srevyhtkrm qhvicvkwts dskyimcgsd emnirlwkan
      241 aseklgvlts rekaakdynq klkekfqhyp hikriarhrh lpksiysqiq eqrimkearr
      301 rkevnrikhs kpgsvplvse kkkhvvavvk
//
LOCUS       NP_001400004             328 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001400004
VERSION     NP_001400004.1
DBSOURCE    REFSEQ: accession NM_001413075.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4111495.1,
                                           SRR18074968.16729.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..328
                     /product="mitochondrial fission regulator 1 isoform 4
                     precursor"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=30859
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=5550
     Region          22..251
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15390.2)"
     Region          177..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          179..304
                     /region_name="Necessary and sufficient to promote
                     mitochondrial fission. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     CDS             1..328
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001413075.1:132..1118"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 10"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsvlwsrkpy gssrsivrki gtnlsliqcp rvqfqinsha
       61 tewspshpge davasfadvg wvakeegecs arlrtevrsr pplqddllff ekapsrqisl
      121 pdlsqeepql ktpalaneea lqkicalene laalraqiak ivtqqeqqnl tagdldsttf
      181 gtipphpppp ppplpppalg lhqstsavdl ikerrekran agktlvknnp kkpempnmle
      241 ilkemnsvkl rsvkrseqdv kpkpvdatdp aaliaealkk kfayryrsds qdevekgipk
      301 seseatserv lslpagfiqp hvskhclg
//
LOCUS       NP_001399526            4002 aa            linear   PRI 21-NOV-2025
DEFINITION  histone-lysine N-methyltransferase 2A isoform 3 [Homo sapiens].
ACCESSION   NP_001399526 XP_011541133
VERSION     NP_001399526.1
DBSOURCE    REFSEQ: accession NM_001412597.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4002)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 4002)
  AUTHORS   Yang,Z., Zhang,G., Zhao,R., Tian,T., Zhi,J., Wei,G., Roeder,R.G.,
            Jing,L. and Yu,M.
  TITLE     MLL-AF9 regulates transcriptional initiation in mixed lineage
            leukemic cells
  JOURNAL   J Biol Chem 300 (8), 107566 (2024)
   PUBMED   39002676
  REMARK    GeneRIF: MLL-AF9 regulates transcriptional initiation in mixed
            lineage leukemic cells.
REFERENCE   3  (residues 1 to 4002)
  AUTHORS   Cho,U.S.
  TITLE     The Core Complex of Yeast COMPASS and Human Mixed-Lineage Leukemia
            (MLL), Structure, Function, and Recognition of the Nucleosome
  JOURNAL   Subcell Biochem 104, 101-117 (2024)
   PUBMED   38963485
  REMARK    GeneRIF: The Core Complex of Yeast COMPASS and Human Mixed-Lineage
            Leukemia (MLL), Structure, Function, and Recognition of the
            Nucleosome.
            Review article
REFERENCE   4  (residues 1 to 4002)
  AUTHORS   Liu,H., Cheng,E.H. and Hsieh,J.J.
  TITLE     MLL fusions: pathways to leukemia
  JOURNAL   Cancer Biol Ther 8 (13), 1204-1211 (2009)
   PUBMED   19729989
  REMARK    GeneRIF: Stduies indicate that leukemogenic MLL translocations fuse
            the common MLL N-terminus (approximately 1,400 aa) in frame with
            more than 60 translocation partner genes.
            Review article
REFERENCE   5  (residues 1 to 4002)
  AUTHORS   Sheppard,S.E. and Quintero-Rivera,F.
  TITLE     Wiedemann-Steiner Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   35617449
REFERENCE   6  (residues 1 to 4002)
  AUTHORS   Gu,Y., Nakamura,T., Alder,H., Prasad,R., Canaani,O., Cimino,G.,
            Croce,C.M. and Canaani,E.
  TITLE     The t(4;11) chromosome translocation of human acute leukemias fuses
            the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene
  JOURNAL   Cell 71 (4), 701-708 (1992)
   PUBMED   1423625
REFERENCE   7  (residues 1 to 4002)
  AUTHORS   Tkachuk,D.C., Kohler,S. and Cleary,M.L.
  TITLE     Involvement of a homolog of Drosophila trithorax by 11q23
            chromosomal translocations in acute leukemias
  JOURNAL   Cell 71 (4), 691-700 (1992)
   PUBMED   1423624
REFERENCE   8  (residues 1 to 4002)
  AUTHORS   Djabali,M., Selleri,L., Parry,P., Bower,M., Young,B.D. and
            Evans,G.A.
  TITLE     A trithorax-like gene is interrupted by chromosome 11q23
            translocations in acute leukaemias
  JOURNAL   Nat Genet 2 (2), 113-118 (1992)
   PUBMED   1303259
  REMARK    Erratum:[Nat Genet. 1993 Aug;4(4):431. doi: 10.1038/ng0893-431.
            PMID: 8401594]
REFERENCE   9  (residues 1 to 4002)
  AUTHORS   Cimino,G., Moir,D.T., Canaani,O., Williams,K., Crist,W.M.,
            Katzav,S., Cannizzaro,L., Lange,B., Nowell,P.C., Croce,C.M. et al.
  TITLE     Cloning of ALL-1, the locus involved in leukemias with the
            t(4;11)(q21;q23), t(9;11)(p22;q23), and t(11;19)(q23;p13)
            chromosome translocations
  JOURNAL   Cancer Res 51 (24), 6712-6714 (1991)
   PUBMED   1835902
REFERENCE   10 (residues 1 to 4002)
  AUTHORS   Ziemin-van der Poel,S., McCabe,N.R., Gill,H.J., Espinosa,R. 3rd,
            Patel,Y., Harden,A., Rubinelli,P., Smith,S.D., LeBeau,M.M.,
            Rowley,J.D. et al.
  TITLE     Identification of a gene, MLL, that spans the breakpoint in 11q23
            translocations associated with human leukemias
  JOURNAL   Proc Natl Acad Sci U S A 88 (23), 10735-10739 (1991)
   PUBMED   1720549
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1992 May 1;89(9):4220]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001267.4 and AP000941.6.
            
            On Oct 11, 2022 this sequence version replaced XP_011541133.1.
            
            Summary: This gene encodes a transcriptional coactivator that plays
            an essential role in regulating gene expression during early
            development and hematopoiesis. The encoded protein contains
            multiple conserved functional domains. One of these domains, the
            SET domain, is responsible for its histone H3 lysine 4 (H3K4)
            methyltransferase activity which mediates chromatin modifications
            associated with epigenetic transcriptional activation. This protein
            is processed by the enzyme Taspase 1 into two fragments, MLL-C and
            MLL-N. These fragments reassociate and further assemble into
            different multiprotein complexes that regulate the transcription of
            specific target genes, including many of the HOX genes. Multiple
            chromosomal translocations involving this gene are the cause of
            certain acute lymphoid leukemias and acute myeloid leukemias.
            Alternate splicing results in multiple transcript
            variants.[provided by RefSeq, Oct 2010].
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longest isoform (3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..4002
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..4002
                     /product="histone-lysine N-methyltransferase 2A isoform 3"
                     /EC_number="2.1.1.364"
                     /note="zinc finger protein HRX; trithorax-like protein;
                     lysine (K)-specific methyltransferase 2A; lysine
                     N-methyltransferase 2A; CXXC-type zinc finger protein 7;
                     myeloid/lymphoid or mixed-lineage leukemia (trithorax
                     homolog, Drosophila); mixed lineage leukemia 1;
                     histone-lysine N-methyltransferase 2A; Acute lymphocytic
                     1"
                     /calculated_mol_wt=435585
     Region          1180..1227
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          1466..1512
                     /region_name="PHD1_KMT2A"
                     /note="PHD finger 1 found in histone-lysine
                     N-methyltransferase 2A (KMT2A); cd15588"
                     /db_xref="CDD:277063"
     Site            order(1466,1477..1481,1485,1507)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277063"
     Region          1514..1563
                     /region_name="PHD2_KMT2A"
                     /note="PHD finger 2 found in histone-lysine
                     N-methyltransferase 2A (KMT2A); cd15590"
                     /db_xref="CDD:277065"
     Site            order(1514,1527..1531,1535,1558)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277065"
     Region          1601..1657
                     /region_name="PHD3_KMT2A"
                     /note="PHD finger 3 found in histone-lysine
                     N-methyltransferase 2A (KMT2A); cd15592"
                     /db_xref="CDD:277067"
     Site            order(1601,1617..1621,1625,1652)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277067"
     Region          1680..1810
                     /region_name="Bromo_ALL-1"
                     /note="Bromodomain, ALL-1 like proteins. ALL-1 is a
                     vertebrate homologue of Drosophila trithorax and is often
                     affected in chromosomal rearrangements that are linked to
                     acute leukemias, such as acute lymphocytic leukemia (ALL).
                     Bromodomains are found in many...; cd05493"
                     /db_xref="CDD:99925"
     Site            order(1723,1728,1731,1770,1774,1792)
                     /site_type="other"
                     /note="putative acetyllysine binding site [chemical
                     binding]"
                     /db_xref="CDD:99925"
     Region          1904..2016
                     /region_name="ePHD_KMT2A"
                     /note="Extended PHD finger found in histone-lysine
                     N-methyltransferase 2A (KMT2A); cd15693"
                     /db_xref="CDD:277163"
     Site            order(1965,1974..1978,1984,2005)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277163"
     Region          2057..2104
                     /region_name="FYRN"
                     /note="F/Y-rich N-terminus; pfam05964"
                     /db_xref="CDD:461787"
     Region          3702..3785
                     /region_name="FYRC"
                     /note="FY-rich domain, C-terminal region; smart00542"
                     /db_xref="CDD:197781"
     Region          3849..4002
                     /region_name="SET_KMT2A_2B"
                     /note="SET domain (including post-SET domain) found in
                     histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B)
                     and similar proteins; cd19170"
                     /db_xref="CDD:380947"
     Site            order(3871..3874,3891,3916..3921,3935..3940,3948..3950,
                     3959,3975..3980,3989..3992,4001)
                     /site_type="active"
                     /db_xref="CDD:380947"
     Site            order(3871..3874,3916,3936..3940,3977,3989..3992)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380947"
     Site            order(3891,3916..3921,3935..3936,3938,3948..3950,3959,
                     3975..3980)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:380947"
     Site            order(3942,3990,3992,3997)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380947"
     CDS             1..4002
                     /gene="KMT2A"
                     /gene_synonym="ALL-1; ALL1; CXXC7; GAS7; HRX; HTRX; HTRX1;
                     MLL; MLL1; MLL1A; TRX1; WDSTS"
                     /coded_by="NM_001412597.1:22..12030"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:4297"
                     /db_xref="HGNC:HGNC:7132"
                     /db_xref="MIM:159555"
ORIGIN      
        1 mahscrwrfp arpgttgggg gggrrglgga prqrvpalll ppgppvgggg pgappsppav
       61 aaaaaaagss gagvpggaaa asaassssas ssssssssas sgpallrvgp gfdaalqvsa
      121 aigtnlrrfr avfgesgggg gsgelttqip cswrtkghih dkktepfrll awswclndeq
      181 flgfgsdeev rvrsptrsps vktsprkprg rprsgsdrns ailsdpsvfs plnksetksg
      241 dkikkkdsks iekkrgrppt fpgvkikith gkdiselpkg nkedslkkik rtpsatfqqa
      301 tkikklragk lsplkskfkt gklqigrkgv qivrrrgrpp steriktpsg llinselekp
      361 qkvrkdkegt ppltkedktv vrqsprrikp vriipsskrt datiakqllq rakkgaqkki
      421 ekeaaqlqgr kvktqvknir qfimpvvsai ssriiktprr fiededydpp ikiarlestp
      481 nsrfsapscg ssekssaasq hssqmssdss rssspsvdts tdsqaseeiq vlpeersdtp
      541 evhpplpisq spenesndrr srrysvsers fgsrttkkls tlqsapqqqt sssppppllt
      601 pppplqpass isdhtpwlmp ptiplaspfl pastapmqgk rksilreptf rwtslkhsrs
      661 epqyfssaky akeglirkpi fdnfrppplt pedvgfasgf sasgtaasar lfsplhsgtr
      721 fdmhkrspll raprftpsea hsrifesvtl psnrtsagts ssgvsnrkrk rkvfspirse
      781 prspshsmrt rsgrlsssel spltppssvs sslsisvspl atsalnptft fpshsltqsg
      841 esaeknqrpr kqtsapaepf ssssptplfp wftpgsqter grnkdkapee lskdrdadks
      901 vekdksrerd rerekenkre srkekrkkgs eiqsssalyp vgrvskekvv gedvatsssa
      961 kkatgrkkss shdsgtdits vtlgdttavk tkilikkgrg nlektnldlg ptapslekek
     1021 tlclstpsss tvkhstssig smlaqadklp mtdkrvasll kkakaqlcki ekskslkqtd
     1081 qpkaqgqesd ssetsvrgpr ikhvcrraav algrkravfp ddmptlsalp weerekilss
     1141 mgnddkssia gsedaeplap pikpikpvtr nkapqeppvk kgrrsrrcgq cpgcqvpedc
     1201 gvctncldkp kfggrnikkq cckmrkcqnl qwmpskaylq kqakavkkke kksktsekkd
     1261 skessvvknv vdssqkptps aredpapkks sseppprkpv eekseegnvs apgpeskqat
     1321 tpasrksskq vsqpalvipp qppttgpprk evpkttpsep kkkqppppes gpeqskqkkv
     1381 aprpsipvkq kpkekekppp vnkqenagtl nilstlsngn sskqkipadg vhrirvdfke
     1441 dceaenvwem gglgiltsvp itprvvcflc assghvefvy cqvccepfhk fcleenerpl
     1501 edqlenwccr rckfchvcgr qhqatkqlle cnkcrnsyhp eclgpnyptk ptkkkkvwic
     1561 tkcvrckscg sttpgkgwda qwshdfslch dcaklfakgn fcplcdkcyd dddyeskmmq
     1621 cgkcdrwvhs kcenlsdemy eilsnlpesv aytcvncter hpaewrlale kelqislkqv
     1681 ltallnsrtt shllryrqaa kppdlnpete esipsrsspe gpdppvltev skqddqqpld
     1741 legvkrkmdq gnytsvlefs ddivkiiqaa insdggqpei kkansmvksf firqmervfp
     1801 wfsvkksrfw epnkvssnsg mlpnavlpps ldhnyaqwqe reenshteqp plmkkiipap
     1861 kpkgpgepds ptplhpptpp ilstdrsred spelnpppgi ednrqcalcl tygddsanda
     1921 grllyigqne wthvncalws aevfedddgs lknvhmavir gkqlrcefcq kpgatvgccl
     1981 tsctsnyhfm csrakncvfl ddkkvycqrh rdlikgevvp engfevfrrv fvdfegislr
     2041 rkflnglepe nihmmigsmt idclgilndl sdcedklfpi gyqcsrvyws ttdarkrcvy
     2101 tckivecrpp vvepdinstv ehdenrtiah sptsftesss kesqntaeii sppspdrpph
     2161 sqtsgscyyh viskvprirt psysptqrsp gcrplpsags ptpttheivt vgdpllssgl
     2221 rsigsrrhst sslspqrskl rimspmrtgn tysrnnvssv sttgtatdle ssakvvdhvl
     2281 gplnsstslg qntstssnlq rtvvtvgnkn shldgsssse mkqssasdlv skssslkgek
     2341 tkvlssksse gsahnvaypg ipklapqvhn ttsrelnvsk igsfaepssv sfsskealsf
     2401 phlhlrgqrn drdqhtdstq sansspdedt evktlklsgm snrssiineh mgsssrdrrq
     2461 kgkkscketf kekhssksfl epgqvttgee gnlkpefmde vltpeymgqr pcnnvssdki
     2521 gdkglsmpgv pkappmqveg sakelqaprk rtvkvtltpl kmenesqskn alkesspasp
     2581 lqiestspte pisasenpgd gpvaqpspnn tscqdsqsnn yqnlpvqdrn lmlpdgpkpq
     2641 edgsfkrryp rrsararsnm ffgltplygv rsygeedipf yssstgkkrg krsaegqvdg
     2701 addlstsded dlyyynftrt vissggeerl ashnlfreee qcdlpkisql dgvddgtesd
     2761 tsvtattrks sqipkrngke ngtenlkidr pedagekehv tkssvghkne pkmdnchsvs
     2821 rvktqgqdsl eaqlssless rrvhtstpsd knlldtynte llksdsdnnn sddcgnilps
     2881 dimdfvlknt psmqalgesp essssellnl geglgldsnr ekdmglfevf sqqlpttepv
     2941 dssvsssisa eeqfelplel psdlsvlttr sptvpsqnps rlavisdsge krvtiteksv
     3001 assesdpall spgvdptpeg hmtpdhfiqg hmdadhissp pcgsveqghg nnqdltrnss
     3061 tpglqvpvsp tvpiqnqkyv pnstdspgps qisnaavqtt pphlkpatek livvnqnmqp
     3121 lyvlqtlpng vtqkiqltss vsstpsvmet ntsvlgpmgg gltlttglnp slptsqslfp
     3181 saskgllpms hhqhlhsfpa atqssfppni snppsgllig vqpppdpqll vsessqrtdl
     3241 sttvatpssg lkkrpisrlq trknkklaps stpsniapsd vvsnmtlinf tpsqlpnhps
     3301 lldlgslnts shrtvpniik rskssimyfe papllpqsvg gtaataagts tisqdtshlt
     3361 sgsvsglass ssvlnvvsmq ttttptssas vpghvtltnp rllgtpdigs isnllikasq
     3421 qslgiqdqpv alppssgmfp qlgtsqtpst aaitaassic vlpstqttgi taaspsgead
     3481 ehyqlqhvnq llasktgihs sqrdldsasg pqvsnftqtv dapnsmgleq nkalssavqa
     3541 sptspggsps spssgqrsas psvpgptkpk pktkrfqlpl dkgngkkhkv shlrtsssea
     3601 hipdqettsl tsgtgtpgae aeqqdtasve qssqkecgqp agqvavlpev qvtqnpaneq
     3661 esaepktvee eesnfssplm lwlqqeqkrk esitekkpkk glvfeissdd gfqicaesie
     3721 dawksltdkv qearsnarlk qlsfagvngl rmlgilhdav vflieqlsga khcrnykfrf
     3781 hkpeeanepp lnphgsarae vhlrksafdm fnflaskhrq ppeynpndee eeevqlksar
     3841 ratsmdlpmp mrfrhlkkts keavgvyrsp ihgrglfckr nidagemvie yagnvirsiq
     3901 tdkrekyyds kgigcymfri ddsevvdatm hgnaarfinh scepncysrv inidgqkhiv
     3961 ifamrkiyrg eeltydykfp iedasnklpc ncgakkcrkf ln
//
LOCUS       NP_001424276            2610 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HECTD1 isoform 1 [Homo sapiens].
ACCESSION   NP_001424276 XP_005267559 XP_054231745
VERSION     NP_001424276.1
DBSOURCE    REFSEQ: accession NM_001437347.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2610)
  AUTHORS   Oxman,E., Li,H., Wang,H.Y. and Zohn,I.E.
  TITLE     Identification and functional analysis of rare HECTD1 missense
            variants in human neural tube defects
  JOURNAL   Hum Genet 143 (3), 263-277 (2024)
   PUBMED   38451291
  REMARK    GeneRIF: Identification and functional analysis of rare HECTD1
            missense variants in human neural tube defects.
REFERENCE   2  (residues 1 to 2610)
  AUTHORS   Zhang,J., Xin,Y., Ling,X., Liang,H., Zhang,L., Fang,C. and Ma,J.
  TITLE     Nucleoporin 93, a new substrate of the E3 ubiquitin protein ligase
            HECTD1, promotes esophageal squamous cell carcinoma progression
  JOURNAL   Hum Cell 37 (1), 245-257 (2024)
   PUBMED   37993750
  REMARK    GeneRIF: Nucleoporin 93, a new substrate of the E3 ubiquitin
            protein ligase HECTD1, promotes esophageal squamous cell carcinoma
            progression.
REFERENCE   3  (residues 1 to 2610)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 2610)
  AUTHORS   Vaughan,N., Scholz,N., Lindon,C. and Licchesi,J.D.F.
  TITLE     The E3 ubiquitin ligase HECTD1 contributes to cell proliferation
            through an effect on mitosis
  JOURNAL   Sci Rep 12 (1), 13160 (2022)
   PUBMED   35915203
  REMARK    GeneRIF: The E3 ubiquitin ligase HECTD1 contributes to cell
            proliferation through an effect on mitosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2610)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 2610)
  AUTHORS   Aleidi,S.M., Yang,A., Sharpe,L.J., Rao,G., Cochran,B.J., Rye,K.A.,
            Kockx,M., Brown,A.J. and Gelissen,I.C.
  TITLE     The E3 ubiquitin ligase, HECTD1, is involved in ABCA1-mediated
            cholesterol export from macrophages
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1863 (4), 359-368 (2018)
   PUBMED   29306077
  REMARK    GeneRIF: HECTD1 may be involved in the regulation of ABCA1-mediated
            cholesterol export from unloaded macrophages to apoA-I.
REFERENCE   7  (residues 1 to 2610)
  AUTHORS   Fang,S., Guo,H., Cheng,Y., Zhou,Z., Zhang,W., Han,B., Luo,W.,
            Wang,J., Xie,W. and Chao,J.
  TITLE     circHECTD1 promotes the silica-induced pulmonary
            endothelial-mesenchymal transition via HECTD1
  JOURNAL   Cell Death Dis 9 (3), 396 (2018)
   PUBMED   29540674
  REMARK    GeneRIF: SiO2 concomitantly increased circHECTD1 expression, which,
            in turn, inhibited HECTD1 protein expression.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 2610)
  AUTHORS   Shen,X., Jia,Z., D'Alonzo,D., Wang,X., Bruder,E., Emch,F.H., De
            Geyter,C. and Zhang,H.
  TITLE     HECTD1 controls the protein level of IQGAP1 to regulate the
            dynamics of adhesive structures
  JOURNAL   Cell Commun Signal 15 (1), 2 (2017)
   PUBMED   28073378
  REMARK    GeneRIF: Hectd1 regulates the protein level of IQGAP1 through
            ubiquitination.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 2610)
  AUTHORS   Helander,S., Montecchio,M., Lemak,A., Fares,C., Almlof,J., Yi,Y.,
            Yee,A., Arrowsmith,C., DhePaganon,S. and Sunnerhagen,M.
  TITLE     Basic Tilted Helix Bundle - a new protein fold in human
            FKBP25/FKBP3 and HectD1
  JOURNAL   Biochem Biophys Res Commun 447 (1), 26-31 (2014)
   PUBMED   24667607
  REMARK    GeneRIF: our high-resolution structures show a new fold composed of
            five small helices where H3 and H4 are tilted in a novel
            arrangement; we call this fold the Basic Tilted Helix Bundle (BTHB)
            domain.
REFERENCE   10 (residues 1 to 2610)
  AUTHORS   Tran,H., Bustos,D., Yeh,R., Rubinfeld,B., Lam,C., Shriver,S.,
            Zilberleyb,I., Lee,M.W., Phu,L., Sarkar,A.A., Zohn,I.E.,
            Wertz,I.E., Kirkpatrick,D.S. and Polakis,P.
  TITLE     HectD1 E3 ligase modifies adenomatous polyposis coli (APC) with
            polyubiquitin to promote the APC-axin interaction
  JOURNAL   J Biol Chem 288 (6), 3753-3767 (2013)
   PUBMED   23277359
  REMARK    GeneRIF: HectD1 promotes the APC-Axin interaction to negatively
            regulate Wnt signaling.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136418.4, AL121808.4 and KC877516.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_005267559.2, XP_054231745.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.8882.1,
                                           SRR18074967.973936.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2610
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..2610
                     /product="E3 ubiquitin-protein ligase HECTD1 isoform 1"
                     /EC_number="2.3.2.26"
                     /note="E3 ubiquitin-protein ligase HECTD1; E3 ligase for
                     inhibin receptor; HECT domain-containing protein 1; HECT
                     domain containing E3 ubiquitin protein ligase 1; HECT-type
                     E3 ubiquitin transferase HECTD1"
                     /calculated_mol_wt=289239
     Region          246..269
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          <366..>479
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          366..393
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          395..424
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          396..426
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(397,401..402,405..407,409..410,414,417,426,428,
                     432..433,436..438,440..441,445,448,457,459,461,465..466,
                     469..471,473..474,478)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          426..455
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          428..457
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          459..491
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          489..513
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          579..612
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          627..657
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZR2; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          707..748
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1107..1240
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     Region          1277..1335
                     /region_name="MIB_HERC2"
                     /note="Mib_herc2; pfam06701"
                     /db_xref="CDD:461991"
     Region          1343..1406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZR2; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1433..1483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1496..1515
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZR2; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1592..1611
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1674..1757
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1760
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            1772
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1777..1797
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          1893..1958
                     /region_name="BTHB_HectD1"
                     /note="basic tilted helix bundle (BTHB) domain found in
                     HECT domain-containing protein 1 (HectD1) and similar
                     proteins; cd21062"
                     /db_xref="CDD:439138"
     Region          2029..2103
                     /region_name="K-box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Region          2131..2608
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(2137,2166,2176,2263,2541,2573..2574,2577..2581,2601,
                     2607)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Region          2297..2318
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            2318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9ULT8.4)"
     Site            order(2356,2359..2360,2362..2363,2366,2408,2410,
                     2414..2415,2417,2423,2428,2445,2449)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..2610
                     /gene="HECTD1"
                     /gene_synonym="EULIR"
                     /coded_by="NM_001437347.1:425..8257"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:25831"
                     /db_xref="HGNC:HGNC:20157"
                     /db_xref="MIM:618649"
ORIGIN      
        1 madvdpdtll ewlqmgqgde rdmqlialeq lcmlllmsdn vdrcfetcpp rtflpalcki
       61 fldesapdnv levtaraity yldvsaectr rivgvdgaik alcnrlvvve lnnrtsrdla
      121 eqcvkvleli ctresgavfe agglncvltf irdsghlvhk dtlhsamavv srlcgkmepq
      181 dssleicves lssllkhedh qvsdgalrcf asladrftrr gvdpaplakh glteellsrm
      241 aaaggtvsgp ssackpgrst tgapsttads klsnqvstiv sllstlcrgs pvvthdllrs
      301 elpdsiesal qgdercvldt mrlvdlllvl lfegrkalpk ssagstgrip glrrldssge
      361 rshrqlidci rskdtdalid aidtgafevn fmddvgqtll nwasafgtqe mveflcerga
      421 dvnrgqrsss lhyaacfgrp qvaktllrhg anpdlrdedg ktpldkarer ghsevvailq
      481 spgdwmcpvn kgddkkkkdt nkdeeecnep kgdpemapiy lkrllpvfaq tfqqtmlpsi
      541 rkaslalirk mihfcseall kevcdsdvgh nlptilveit atvldqeddd dghllalqii
      601 rdlvdkggdi fldqlarlgv iskvstlagp ssddeneees kpekedepqe dakelqqgkp
      661 yhwrdwsiir grdclyiwsd aaalelsngs ngwfrfildg klatmyssgs peggsdsses
      721 rsefleklqr argqvkpsts sqpilsapgp tkltvgnwsl tclkegeiai hnsdgqqati
      781 lkedlpgfvf esnrgtkhsf taetslgsef vtgwtgkrgr klksklektk qkvrtmardl
      841 yddhfkaves mprgvvvtlr niatqlessw elhtnrqcie sentwrdlmk talenlivll
      901 kdentispye mcssglvqal ltvlnnsmdl dmkqdcsqlv erinvfktaf seneddesrp
      961 avalirklia vlesierlpl hlydtpgsty nlqiltrrlr frlerapget alidrtgrml
     1021 kmeplatves leqyllkmva kqwydfdrss fvfvrklreg qnfifrhqhd fdengiiywi
     1081 gtnaktayew vnpaayglvv vtssegrnlp ygrledilsr dnsalnchsn ddknawfaid
     1141 lglwvipsay tlrhargygr salrnwvfqv skdgqnwtsl ythvddcsln epgstatwpl
     1201 dppkdekqgw rhvrikqmgk nasgqthyls lsgfelygtv ngvcedqlgk aakeaeanlr
     1261 rqrrlvrsqv lkymvpgarv irgldwkwrd qdgspqgegt vtgelhngwi dvtwdaggsn
     1321 syrmgaegkf dlklapgydp dtvaspkpvs stvsgttqsw sslvknncpd ktsaaagsss
     1381 rkgssssvcs vasssdislg stkterrsei vmehsivsga dvhepivvls saenvpqtev
     1441 gssssastst ltaetgsena erklgpdssv rtpgessais mgivsvsspd vssvseltnk
     1501 eaasqrplss sasnrlsvss llaagapmss sasvpnlssr etsslesfvr rvaniartna
     1561 tnnmnlsrss sdnntntlgr nvmstatspl mgaqsfpnlt tpgttstvtm stssvtsssn
     1621 vatattvlsv gqslsntltt sltstssesd tgqeaeysly dfldscrast llaelddded
     1681 lpepdeedde neddnqedqe yeevmilrrp slqrragsrs dvthhavtsq lpqvpagags
     1741 rpigeqeeee yetkggrrrt wdddyvlkrq fsalvpafdp rpgrtnvqqt tdleipppgt
     1801 phselleeve ctpsprlalt lkvtglgttr evelpltnfr stifyyvqkl lqlscngnvk
     1861 sdklrriwep tytimyremk dsdkekengk mgcwsiehve qylgtdelpk ndlitylqkn
     1921 adaaflrhwk ltgtnksirk nrncsqliaa ykdfcehgtk sglnqgaist lqssdilnlt
     1981 keqpqakagn gqnscgvedv lqllrilyiv asdpysrisq edgdeqpqft fppdeftskk
     2041 ittkilqqie eplalasgal pdwceqltsk cpflipfetr qlyftctafg asraivwlqn
     2101 rreatvertr ttssvrrddp gefrvgrlkh ervkvprges lmewaenvmq ihadrksvle
     2161 veflgeegtg lgptlefyal vaaefqrtdl gawlcddnfp ddesrhvdlg gglkppgyyv
     2221 qrscglftap fpqdsdeler itklfhflgi flakciqdnr lvdlpiskpf fklmcmgdik
     2281 snmskliyes rgdrdlhcte sqseasteeg hdslsvgsfe edsksefild ppkpkppawf
     2341 ngiltwedfe lvnphrarfl keikdlaikr rqilsnkgls edekntklqe lvlknpsgsg
     2401 pplsiedlgl nfqfcpssri ygftavdlkp sgedemitmd naeeyvdlmf dfcmhtgiqk
     2461 qmeafrdgfn kvfpmeklss fsheevqmil cgnqspswaa ediinytepk lgytrdspgf
     2521 lrfvrvlcgm ssderkaflq fttgcstlpp gglanlhprl tvvrkvdatd asypsvntcv
     2581 hylklpeyss eeimrerlla atmekgfhln
//
LOCUS       NP_001424555            1287 aa            linear   PRI 21-NOV-2025
DEFINITION  ras GTPase-activating protein nGAP isoform 4 [Homo sapiens].
ACCESSION   NP_001424555 XP_011508469 XP_054195666
VERSION     NP_001424555.1
DBSOURCE    REFSEQ: accession NM_001437626.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1287)
  AUTHORS   Zhang,Y., Yang,Y., Hu,X., Wei,B., Shen,Q., Shi,C. and Chen,P.
  TITLE     RAS protein activator-like 2 (RASAL2) initiates peritubular
            capillary rarefaction in hypoxic renal interstitial fibrosis
  JOURNAL   Transl Res 269, 14-30 (2024)
   PUBMED   38453052
  REMARK    GeneRIF: RAS protein activator-like 2 (RASAL2) initiates
            peritubular capillary rarefaction in hypoxic renal interstitial
            fibrosis.
REFERENCE   2  (residues 1 to 1287)
  AUTHORS   Singharajkomron,N., Yodsurang,V., Limprasutr,V., Wattanathamsan,O.,
            Iksen,I., Hayakawa,Y. and Pongrakhananon,V.
  TITLE     CAMSAP2 enhances lung cancer cell metastasis by mediating RASAL2
            degradation
  JOURNAL   Life Sci 338, 122391 (2024)
   PUBMED   38159595
  REMARK    GeneRIF: CAMSAP2 enhances lung cancer cell metastasis by mediating
            RASAL2 degradation.
REFERENCE   3  (residues 1 to 1287)
  AUTHORS   Wills,C., Watts,K., Maughan,T.S., Fisher,D., Al-Tassan,N.A.,
            Houlston,R.S., Escott-Price,V. and Cheadle,J.P.
  TITLE     Germline variation in RASAL2 may predict survival in patients with
            RAS-activated colorectal cancer
  JOURNAL   Genes Chromosomes Cancer 62 (6), 332-341 (2023)
   PUBMED   36790221
  REMARK    GeneRIF: Germline variation in RASAL2 may predict survival in
            patients with RAS-activated colorectal cancer.
REFERENCE   4  (residues 1 to 1287)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 1287)
  AUTHORS   Yue,Y., Wu,K., Qian,W., Zhu,Z., Zhang,S., Zhang,W., Zhang,W.,
            Wu,S., Li,L., Wu,Z., Ma,Q., Xie,K. and Wang,Z.
  TITLE     RASAL2 mediated the enhancement of YAP1/TIAM1 signaling promotes
            malignant phenotypes of pancreatic ductal adenocarcinoma
  JOURNAL   Int J Biol Sci 18 (10), 4245-4259 (2022)
   PUBMED   35844783
  REMARK    GeneRIF: RASAL2 mediated the enhancement of YAP1/TIAM1 signaling
            promotes malignant phenotypes of pancreatic ductal adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1287)
  AUTHORS   Melen,E., Himes,B.E., Brehm,J.M., Boutaoui,N., Klanderman,B.J.,
            Sylvia,J.S. and Lasky-Su,J.
  TITLE     Analyses of shared genetic factors between asthma and obesity in
            children
  JOURNAL   J Allergy Clin Immunol 126 (3), 631-7 (2010)
   PUBMED   20816195
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1287)
  AUTHORS   Shibui,T., Kobayashi,T. and Shiratori,M.
  TITLE     Isolation of cross-reacting antigen candidates by mRNA-display
            using a mixed cDNA library
  JOURNAL   Biotechnol Lett 30 (12), 2037-2043 (2008)
   PUBMED   18633578
REFERENCE   8  (residues 1 to 1287)
  AUTHORS   de Chassey,B., Navratil,V., Tafforeau,L., Hiet,M.S., Aublin-Gex,A.,
            Agaugue,S., Meiffren,G., Pradezynski,F., Faria,B.F., Chantier,T.,
            Le Breton,M., Pellet,J., Davoust,N., Mangeot,P.E., Chaboud,A.,
            Penin,F., Jacob,Y., Vidalain,P.O., Vidal,M., Andre,P.,
            Rabourdin-Combe,C. and Lotteau,V.
  TITLE     Hepatitis C virus infection protein network
  JOURNAL   Mol Syst Biol 4, 230 (2008)
   PUBMED   18985028
REFERENCE   9  (residues 1 to 1287)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 1287)
  AUTHORS   Noto,S., Maeda,T., Hattori,S., Inazawa,J., Imamura,M., Asaka,M. and
            Hatakeyama,M.
  TITLE     A novel human RasGAP-like gene that maps within the prostate cancer
            susceptibility locus at chromosome 1q25
  JOURNAL   FEBS Lett 441 (1), 127-131 (1998)
   PUBMED   9877179
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160281.17, AL499617.16,
            AL365357.12 and AL035702.7.
            
            On or before Apr 7, 2025 this sequence version replaced
            XP_011508469.1, XP_054195666.1.
            
            Summary: This gene encodes a protein that contains the GAP-related
            domain (GRD), a characteristic domain of GTPase-activating proteins
            (GAPs). GAPs function as activators of Ras superfamily of small
            GTPases. The protein encoded by this gene is able to complement the
            defective RasGAP function in a yeast system. Two alternatively
            spliced transcript variants of this gene encoding distinct isoforms
            have been reported. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3338642.1,
                                           SRR14038196.2394691.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1287
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..1287
                     /product="ras GTPase-activating protein nGAP isoform 4"
                     /note="Ras protein activator like 1; ras GTPase-activating
                     protein nGAP; RASAL2/ACVR1 fusion"
                     /calculated_mol_wt=144544
     Region          182..365
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          307..446
                     /region_name="C2_SynGAP_like"
                     /note="C2 domain present in Ras GTPase activating protein
                     (GAP) family; cd04013"
                     /db_xref="CDD:175980"
     Region          437..767
                     /region_name="RasGAP_DAB2IP"
                     /note="Ras-GTPase Activating Domain of DAB2IP and similar
                     proteins; cd05136"
                     /db_xref="CDD:213338"
     Site            order(476,513,515,517..518,520,523,527,619,627..628,
                     631..632,635,656,659..660,663,667,669,674..675)
                     /site_type="other"
                     /note="putative RAS interface [polypeptide binding]"
                     /db_xref="CDD:213338"
     Region          757..1258
                     /region_name="DUF3498"
                     /note="Domain of unknown function (DUF3498); pfam12004"
                     /db_xref="CDD:463427"
     CDS             1..1287
                     /gene="RASAL2"
                     /gene_synonym="NGAP"
                     /coded_by="NM_001437626.1:390..4253"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:9462"
                     /db_xref="HGNC:HGNC:9874"
                     /db_xref="MIM:606136"
ORIGIN      
        1 melspssgga aealswpemf palesdsplp pedldavvpv sgavaggmld rillesvcqq
       61 qswvrvydvk gppthrlscg qspytetttw erkyciltds qlvllnkeke ipveggqeqq
      121 tdstkgrclr rtvsvpsegq fpeyppegat klevpaersp rrrsisgtst sekpnsmdta
      181 ntspfkvpgf fskrlkgsik rtksqskldr ntsfrlpslr stddrsrglp klkesrshes
      241 llspcstvec ldlgrgepvs vkplhssilg qdfcfevtyl sgskcfscns aserdkwmen
      301 lrrtvqpnkd ncrraenvlr lwiieakdla pkkkyfcelc lddtlfartt sktkadnifw
      361 gehfeffslp plhsitvhiy kdvekkkkkd knnyvglvni ptasvtgrqf vekwypvstp
      421 tpnkgktggp siriksrfqt itilpmeqyk efaefvtsny tmlcsvlepv isvrnkeela
      481 calvhilqst grakdfltdl vmsevdrcge hdvlifrent iatksieeyl klvgqqylhd
      541 algefikaly esdencevdp skcssselid hqsnlkmcce lafckiinsy cvfprelkev
      601 faswkqqcln rgkqdiserl isaslflrfl cpaimspslf nlmqeypddr tsrtltliak
      661 viqnlanfak fgnkeeymaf mndflehewg gmkrflleis npdtisntpg fdgyidlgre
      721 lsvlhsllwe vvsqldkgen sflqatvakl gplprvladi tksltnptpi qqqlrrfteh
      781 nsspnvsgsl ssglqkifed ptdsdlhklk spsqdntdsy frgktlllvq qassqsmtys
      841 ekderesslp ngrsvslmdl qdthaaqveh asvmldvpir ltgsqlsitq vasikqlret
      901 qstpqsapqv rrplhpalnq pgglqplsfq npvyhlnnpi pampkasids slenlstass
      961 rsqsnsedfk lsgpsnssme dftkrstqse dfsrrhtvpd rhiplalprq nstgqaqirk
     1021 vdqgglgara kappslphsa slrstgsmsv vsaalvaepv qngsrsrqqs sssrespvpk
     1081 vraiqrqqtq qvqspvdsat mspvertaaw vlnngqyeed veeteqnlde akhaekyeqe
     1141 itklkerlrv ssrrleeyer rllvqeqqmq kllleykarl edseerlrrq qeekdsqmks
     1201 iisrlmavee elkkdhaemq avidakqkii daqekrivsl dsantrlmsa ltqvkerysm
     1261 qvrngisptn ptklsiteng efknssc
//
LOCUS       NP_001424217            1070 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit
            beta isoform isoform 1 [Homo sapiens].
ACCESSION   NP_001424217 XP_047304264 XP_054202827
VERSION     NP_001424217.1
DBSOURCE    REFSEQ: accession NM_001437288.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1070)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1070)
  AUTHORS   Liu,L., Feng,X., Fan,C., Kong,D., Feng,X., Sun,C., Xu,Y., Li,B.,
            Jiang,Y. and Zheng,C.
  TITLE     PDCD4 interacting with PIK3CB and CTSZ promotes the apoptosis of
            multiple myeloma cells
  JOURNAL   FASEB J 38 (16), e70024 (2024)
   PUBMED   39190024
  REMARK    GeneRIF: PDCD4 interacting with PIK3CB and CTSZ promotes the
            apoptosis of multiple myeloma cells.
REFERENCE   3  (residues 1 to 1070)
  AUTHORS   Liu,G., Hou,Y., Jin,X., Zhang,Y., Sun,C., Huang,C., Ren,Y., Gao,J.,
            Wang,X. and Jiang,X.
  TITLE     PI3K/HSCB axis facilitates FOG1 nuclear translocation to promote
            erythropoiesis and megakaryopoiesis
  JOURNAL   Elife 13, 95815 (2024)
   PUBMED   38757931
  REMARK    GeneRIF: PI3K/HSCB axis facilitates FOG1 nuclear translocation to
            promote erythropoiesis and megakaryopoiesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1070)
  AUTHORS   Duewell,B.R., Wilson,N.E., Bailey,G.M., Peabody,S.E. and
            Hansen,S.D.
  TITLE     Molecular dissection of PI3Kbeta synergistic activation by receptor
            tyrosine kinases, GbetaGgamma, and Rho-family GTPases
  JOURNAL   Elife 12, 88991 (2024)
   PUBMED   38713746
  REMARK    GeneRIF: Molecular dissection of PI3Kbeta synergistic activation by
            receptor tyrosine kinases, GbetaGgamma, and Rho-family GTPases.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1070)
  AUTHORS   Xu,W., Chen,Y., Zhang,Z., Jiang,Y. and Wang,Z.
  TITLE     Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma
  JOURNAL   Med Oncol 40 (8), 221 (2023)
   PUBMED   37402056
  REMARK    GeneRIF: Exosomal PIK3CB promotes PD-L1 expression and malignant
            transformation in esophageal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1070)
  AUTHORS   Milani,D., Mazzoni,M., Borgatti,P., Zauli,G., Cantley,L. and
            Capitani,S.
  TITLE     Extracellular human immunodeficiency virus type-1 Tat protein
            activates phosphatidylinositol 3-kinase in PC12 neuronal cells
  JOURNAL   J Biol Chem 271 (38), 22961-22964 (1996)
   PUBMED   8798481
REFERENCE   7  (residues 1 to 1070)
  AUTHORS   Bonnefoy-Berard,N., Liu,Y.C., von Willebrand,M., Sung,A., Elly,C.,
            Mustelin,T., Yoshida,H., Ishizaka,K. and Altman,A.
  TITLE     Inhibition of phosphatidylinositol 3-kinase activity by association
            with 14-3-3 proteins in T cells
  JOURNAL   Proc Natl Acad Sci U S A 92 (22), 10142-10146 (1995)
   PUBMED   7479742
REFERENCE   8  (residues 1 to 1070)
  AUTHORS   Hu,P. and Schlessinger,J.
  TITLE     Direct association of p110 beta phosphatidylinositol 3-kinase with
            p85 is mediated by an N-terminal fragment of p110 beta
  JOURNAL   Mol Cell Biol 14 (4), 2577-2583 (1994)
   PUBMED   8139559
REFERENCE   9  (residues 1 to 1070)
  AUTHORS   Hu,P., Mondino,A., Skolnik,E.Y. and Schlessinger,J.
  TITLE     Cloning of a novel, ubiquitously expressed human
            phosphatidylinositol 3-kinase and identification of its binding
            site on p85
  JOURNAL   Mol Cell Biol 13 (12), 7677-7688 (1993)
   PUBMED   8246984
REFERENCE   10 (residues 1 to 1070)
  AUTHORS   Carpenter,C.L., Duckworth,B.C., Auger,K.R., Cohen,B.,
            Schaffhausen,B.S. and Cantley,L.C.
  TITLE     Purification and characterization of phosphoinositide 3-kinase from
            rat liver
  JOURNAL   J Biol Chem 265 (32), 19704-19711 (1990)
   PUBMED   2174051
  REMARK    GeneRIF: This paper reports the first purification of a
            phosphoinositide 3-kinase and shows that the protein is a
            heterodimer of an 85 kd regulatory subunit that mediates binding to
            phosphorylated proteins and a 110 kd catalytic subunit.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC067728.25, AC117389.5 and AC020890.22.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_047304264.1, XP_054202827.1.
            
            Summary: This gene encodes an isoform of the catalytic subunit of
            phosphoinositide 3-kinase (PI3K). These kinases are important in
            signaling pathways involving receptors on the outer membrane of
            eukaryotic cells and are named for their catalytic subunit. The
            encoded protein is the catalytic subunit for PI3Kbeta (PI3KB).
            PI3KB has been shown to be part of the activation pathway in
            neutrophils which have bound immune complexes at sites of injury or
            infection. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3273104.1,
                                           SRR18074967.540462.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1070
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..1070
                     /product="phosphatidylinositol 4,5-bisphosphate 3-kinase
                     catalytic subunit beta isoform isoform 1"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.1.153"
                     /note="PI3-kinase p110 subunit beta; PtdIns-3-kinase p110;
                     PI3K-beta; PI3-kinase subunit beta; ptdIns-3-kinase
                     subunit beta; ptdIns-3-kinase subunit p110-beta;
                     phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa
                     catalytic subunit beta; serine/threonine protein kinase
                     PIK3CB; phosphoinositide-3-kinase, catalytic, beta
                     polypeptide"
                     /calculated_mol_wt=122632
     Region          41..118
                     /region_name="PI3K_p85B"
                     /note="PI3-kinase family, p85-binding domain; smart00143"
                     /db_xref="CDD:197539"
     Region          180..288
                     /region_name="PI3K_rbd"
                     /note="PI3-kinase family, Ras-binding domain; smart00144"
                     /db_xref="CDD:197540"
     Region          324..501
                     /region_name="C2_PI3K_class_I_beta_delta"
                     /note="C2 domain present in class I beta and delta
                     phosphatidylinositol 3-kinases (PI3Ks); cd08693"
                     /db_xref="CDD:176075"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI9; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     Region          410..418
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Region          532..702
                     /region_name="PI3Ka_I"
                     /note="Phosphoinositide 3-kinase (PI3K) class I, accessory
                     domain; PIK domain is conserved in all PI3 and
                     PI4-kinases. Its role is unclear but it has been suggested
                     to be involved in substrate presentation. In general, PI3K
                     class I prefer phosphoinositol (4,5)...; cd00872"
                     /db_xref="CDD:238444"
     Region          706..1067
                     /region_name="PI3Kc_IA_beta"
                     /note="Catalytic domain of Class IA Phosphoinositide
                     3-kinase beta; cd05173"
                     /db_xref="CDD:270717"
     Region          778..784
                     /region_name="G-loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(779,781..783,785,803,805,808,839,851..854,859,862,
                     924,926,936..937)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270717"
     Site            order(846..847,874..875,878,948..949,962,965,973..976,979,
                     1046,1049..1050,1052..1053)
                     /site_type="other"
                     /note="regulatory subunit interface [polypeptide binding]"
                     /db_xref="CDD:270717"
     Site            893
                     /site_type="other"
                     /note="Ras binding site [polypeptide binding]"
                     /db_xref="CDD:270717"
     Region          916..924
                     /region_name="Catalytic loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            916..924
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270717"
     Region          935..961
                     /region_name="Activation loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42338.1)"
     Site            order(937..950,956..961)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270717"
     Site            1070
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12502714; propagated from
                     UniProtKB/Swiss-Prot (P42338.1)"
     CDS             1..1070
                     /gene="PIK3CB"
                     /gene_synonym="P110BETA; PI3K; PI3KBETA; PIK3C1"
                     /coded_by="NM_001437288.1:583..3795"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="GeneID:5291"
                     /db_xref="HGNC:HGNC:8976"
                     /db_xref="MIM:602925"
ORIGIN      
        1 mcfsfimppa madildiwav dsqiasdgsi pvdfllptgi yiqlevprea tisyikqmlw
       61 kqvhnypmfn llmdidsymf acvnqtavye eledetrrlc dvrpflpvlk lvtrscdpge
      121 kldskigvli gkglhefdsl kdpevnefrr kmrkfseeki lslvglswmd wlkqtyppeh
      181 epsipenled klyggkliva vhfencqdvf sfqvspnmnp ikvnelaiqk rltihgkede
      241 vspydyvlqv sgrveyvfgd hpliqfqyir ncvmnralph filvecckik kmyeqemiai
      301 eaainrnssn lplplppkkt riishvwenn npfqivlvkg nklnteetvk vhvraglfhg
      361 tellcktivs sevsgkndhi wneplefdin icdlprmarl cfavyavldk vktkkstkti
      421 npskyqtirk agkvhypvaw vntmvfdfkg qlrtgdiilh swssfpdele emlnpmgtvq
      481 tnpytenata lhvkfpenkk qpyyyppfdk iiekaaeias sdsanvssrg gkkflpvlke
      541 ildrdplsql cenemdliwt lrqdcreifp qslpklllsi kwnkledvaq lqallqiwpk
      601 lpprealell dfnypdqyvr eyavgclrqm sdeelsqyll qlvqvlkyep fldcalsrfl
      661 leralgnrri gqflfwhlrs evhipavsvq fgvileaycr gsvghmkvls kqvealnklk
      721 tlnsliklna vklnrakgke amhtclkqsa yrealsdlqs plnpcvilse lyvekckymd
      781 skmkplwlvy nnkvfgedsv gvifkngddl rqdmltlqml rlmdllwkea gldlrmlpyg
      841 clatgdrsgl ievvstseti adiqlnssnv aaaaafnkda llnwlkeyns gddldraiee
      901 ftlscagycv asyvlgigdr hsdnimvkkt gqlfhidfgh ilgnfkskfg ikrervpfil
      961 tydfihviqq gktgntekfg rfrqcceday lilrrhgnlf itlfalmlta glpeltsvkd
     1021 iqylkdslal gkseeealkq fkqkfdealr eswttkvnwm ahtvrkdyrs
//
LOCUS       NP_001415238             326 aa            linear   PRI 21-NOV-2025
DEFINITION  polycomb complex protein BMI-1 [Homo sapiens].
ACCESSION   NP_001415238
VERSION     NP_001415238.1
DBSOURCE    REFSEQ: accession NM_001428309.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Szustka,A. and Krzeslak,A.
  TITLE     BMI-1 in Breast Cancer - Biological Role and Clinical Implications
  JOURNAL   Cell Physiol Biochem 58 (5), 584-596 (2024)
   PUBMED   39429016
  REMARK    GeneRIF: BMI-1 in Breast Cancer - Biological Role and Clinical
            Implications.
            Review article
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Hsu,Y.C., Luo,C.W., Chang,S.J., Lai,C.Y., Yang,Y.T., Chen,Y.Z.,
            Liu,W.T., Wu,C.C., Sun,C.K., Hou,M.F. and Pan,M.R.
  TITLE     Targeting Bmi1 for Enhancing Anoikis Sensitivity and Inhibiting
            Metastasis in Colorectal Cancer
  JOURNAL   Cancer Genomics Proteomics 21 (5), 523-532 (2024)
   PUBMED   39191496
  REMARK    GeneRIF: Targeting Bmi1 for Enhancing Anoikis Sensitivity and
            Inhibiting Metastasis in Colorectal Cancer.
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Li,Q., Fu,T., Wei,N., Wang,Q. and Zhang,X.
  TITLE     Bmi-1 promotes the proliferation, migration and invasion, and
            inhibits cell apoptosis of human retinoblastoma cells via RKIP
  JOURNAL   Sci Rep 14 (1), 14544 (2024)
   PUBMED   38914697
  REMARK    GeneRIF: Bmi-1 promotes the proliferation, migration and invasion,
            and inhibits cell apoptosis of human retinoblastoma cells via RKIP.
            Erratum:[Sci Rep. 2025 Aug 5;15(1):28521. doi:
            10.1038/s41598-025-11879-x. PMID: 40764337]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Park,I.K., Qian,D., Kiel,M., Becker,M.W., Pihalja,M.,
            Weissman,I.L., Morrison,S.J. and Clarke,M.F.
  TITLE     Bmi-1 is required for maintenance of adult self-renewing
            haematopoietic stem cells
  JOURNAL   Nature 423 (6937), 302-305 (2003)
   PUBMED   12714971
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Satijn,D.P. and Otte,A.P.
  TITLE     RING1 interacts with multiple Polycomb-group proteins and displays
            tumorigenic activity
  JOURNAL   Mol Cell Biol 19 (1), 57-68 (1999)
   PUBMED   9858531
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Alkema,M.J., Jacobs,J., Voncken,J.W., Jenkins,N.A., Copeland,N.G.,
            Satijn,D.P., Otte,A.P., Berns,A. and van Lohuizen,M.
  TITLE     MPc2, a new murine homolog of the Drosophila polycomb protein is a
            member of the mouse polycomb transcriptional repressor complex
  JOURNAL   J Mol Biol 273 (5), 993-1003 (1997)
   PUBMED   9367786
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Alkema,M.J., Bronk,M., Verhoeven,E., Otte,A., van 't Veer,L.J.,
            Berns,A. and van Lohuizen,M.
  TITLE     Identification of Bmi1-interacting proteins as constituents of a
            multimeric mammalian polycomb complex
  JOURNAL   Genes Dev 11 (2), 226-240 (1997)
   PUBMED   9009205
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Alkema,M.J., Wiegant,J., Raap,A.K., Berns,A. and van Lohuizen,M.
  TITLE     Characterization and chromosomal localization of the human
            proto-oncogene BMI-1
  JOURNAL   Hum Mol Genet 2 (10), 1597-1603 (1993)
   PUBMED   8268912
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158211.29.
            
            Summary: This gene encodes a ring finger protein that is major
            component of the polycomb group complex 1 (PRC1). This complex
            functions through chromatin remodeling as an essential epigenetic
            repressor of multiple regulatory genes involved in embryonic
            development and self-renewal in somatic stem cells. This protein
            also plays a central role in DNA damage repair. This gene is an
            oncogene and aberrant expression is associated with numerous
            cancers and is associated with resistance to certain
            chemotherapies. A pseudogene of this gene is found on chromosome X.
            Read-through transcription also exists between this gene and the
            upstream COMM domain containing 3 (COMMD3) gene. [provided by
            RefSeq, Sep 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.253051.1,
                                           SRR14038194.1076500.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.2"
     Protein         1..326
                     /product="polycomb complex protein BMI-1"
                     /note="murine leukemia viral (bmi-1) oncogene homolog; B
                     lymphoma Mo-MLV insertion region 1 homolog; ring finger
                     protein 51; polycomb group protein Bmi1; polycomb group
                     RING finger protein 4; BMI1 polycomb ring finger oncogene;
                     BMI1 polycomb ring finger proto-oncogene"
                     /calculated_mol_wt=36818
     Region          5..101
                     /region_name="RING-HC_PCGF4"
                     /note="RING finger found in polycomb group RING finger
                     protein 4 (PCGF4) and similar proteins; cd16736"
                     /db_xref="CDD:438394"
     Site            order(5..13,15,17,21,23..24,26..27,29..30,32..36,39..42,
                     44..45,66,69..72,74,78,81..82,84,86,89..90,93..94,97)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438394"
     Region          81..95
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     Region          130..226
                     /region_name="RAWUL_PCGF4"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in polycomb group RING finger protein
                     4 (PCGF4); cd17165"
                     /db_xref="CDD:340685"
     Region          162..182
                     /region_name="Interaction with PHC2.
                     /evidence=ECO:0000269|PubMed:27827373"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     Region          164..228
                     /region_name="Interaction with E4F1.
                     /evidence=ECO:0000269|PubMed:16882984"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     Region          236..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     CDS             1..326
                     /gene="BMI1"
                     /gene_synonym="flvi-2/bmi-1; FLVI2/BMI1; PCGF4; RNF51"
                     /coded_by="NM_001428309.1:235..1215"
                     /db_xref="GeneID:648"
                     /db_xref="HGNC:HGNC:1066"
                     /db_xref="MIM:164831"
ORIGIN      
        1 mhrttrikit elnphlmcvl cggyfidatt iieclhsfck tcivrylets kycpicdvqv
       61 hktrpllnir sdktlqdivy klvpglfkne mkrrrdfyaa hpsadaangs nedrgevade
      121 dkriitddei islsieffdq nrldrkvnkd kekskeevnd krylrcpaam tvmhlrkflr
      181 skmdipntfq idvmyeeepl kdyytlmdia yiytwrrngp lplkyrvrpt ckrmkishqr
      241 dgltnagele sdsgsdkans paggipstss clpspstpvq sphpqfphis stmngtsnsp
      301 sgnhqssfan rprkssvngs satssg
//
LOCUS       NP_001393922             478 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform K [Homo sapiens].
ACCESSION   NP_001393922
VERSION     NP_001393922.1
DBSOURCE    REFSEQ: accession NM_001406993.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 478)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 478)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355388.30 and AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2494915.1,
                                           SRR14038192.1641597.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..478
                     /product="lamin isoform K"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=53246
     Region          <1..200
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          248..355
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     CDS             1..478
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406993.1:311..1747"
                     /note="isoform K is encoded by transcript variant 18"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 mlrrvdaenr lqtmkeeldf qkniyseelr etkrrhetrl veidngkqre fesrladalq
       61 elraqhedqv eqykkelekt ysakldnarq saernsnlvg aaheelqqsr iridslsaql
      121 sqlqkqlaak eaklrdleds larerdtsrr llaekerema emrarmqqql deyqelldik
      181 laldmeihay rkllegeeer lrlspsptsq rsrgrasshs sqtqgggsvt kkrklestes
      241 rssfsqhart sgrvaveevd eegkfvrlrn ksnedqsmgn wqikrqngdd plltyrfppk
      301 ftlkagqvvt iwaagagath spptdlvwka qntwgcgnsl rtalinstge evamrklvrs
      361 vtvveddede dgddllhhhh gshcsssgdp aeynlrsrtv lcgtcgqpad kasasgsgaq
      421 vggpissgss assvtvtrsy rsvggsgggs fgdnlvtrsy llgnssprtq spqncsim
//
LOCUS       NP_001397669             348 aa            linear   PRI 21-NOV-2025
DEFINITION  spliceosome-associated protein CWC27 homolog isoform 6 [Homo
            sapiens].
ACCESSION   NP_001397669 XP_011541398
VERSION     NP_001397669.1
DBSOURCE    REFSEQ: accession NM_001410740.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Yassin,S.H., Henderson,R., Lenberg,J., Murillo,V., Murdock,D.R.,
            Friedman,J., Jones,M.C., Wigby,K. and Borooah,S.
  TITLE     Further delineation of the CWC27-associated spliceosomeopathy: Case
            report and review of the literature
  JOURNAL   Am J Med Genet A 191 (5), 1378-1383 (2023)
   PUBMED   36718996
  REMARK    GeneRIF: Further delineation of the CWC27-associated
            spliceosomeopathy: Case report and review of the literature.
            Review article
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Busetto,V., Barbosa,I., Basquin,J., Marquenet,E., Hocq,R.,
            Hennion,M., Paternina,J.A., Namane,A., Conti,E., Bensaude,O. and Le
            Hir,H.
  TITLE     Structural and functional insights into CWC27/CWC22 heterodimer
            linking the exon junction complex to spliceosomes
  JOURNAL   Nucleic Acids Res 48 (10), 5670-5683 (2020)
   PUBMED   32329775
  REMARK    GeneRIF: Structural and functional insights into CWC27/CWC22
            heterodimer linking the exon junction complex to spliceosomes.
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Wang,M., Li,Z., Chu,H., Lv,Q., Ye,D., Ding,Q., Xu,C., Guo,J.,
            Du,M., Chen,J., Song,Z., Yin,C., Qin,C., Gu,C., Zhu,Y., Xia,G.,
            Liu,F., Zhang,Z., Yuan,L., Fu,G., Hu,Z., Tong,N., Shen,J., Liu,K.,
            Sun,J., Sun,Y., Li,J., Li,X., Shen,H., Xu,J., Shi,Y. and Zhang,Z.
  TITLE     Genome-Wide Association Study of Bladder Cancer in a Chinese Cohort
            Reveals a New Susceptibility Locus at 5q12.3
  JOURNAL   Cancer Res 76 (11), 3277-3284 (2016)
   PUBMED   27206850
  REMARK    GeneRIF: CWC27 overexpression is associated with Bladder Cancer.
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Ulrich,A. and Wahl,M.C.
  TITLE     Structure and evolution of the spliceosomal peptidyl-prolyl
            cis-trans isomerase Cwc27
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 12), 3110-3123 (2014)
   PUBMED   25478830
  REMARK    GeneRIF: The crystal structure of a relatively protease-resistant
            N-terminal fragment of human Cwc27 containing the cyclophilin-type
            peptidyl-prolyl cis-trans isomerase domain was determined at 2.0 A
            resolution.
REFERENCE   8  (residues 1 to 348)
  AUTHORS   Davis,T.L., Walker,J.R., Campagna-Slater,V., Finerty,P.J.,
            Paramanathan,R., Bernstein,G., MacKenzie,F., Tempel,W., Ouyang,H.,
            Lee,W.H., Eisenmesser,E.Z. and Dhe-Paganon,S.
  TITLE     Structural and biochemical characterization of the human
            cyclophilin family of peptidyl-prolyl isomerases
  JOURNAL   PLoS Biol 8 (7), e1000439 (2010)
   PUBMED   20676357
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 348)
  AUTHORS   Fabrizio,P., Dannenberg,J., Dube,P., Kastner,B., Stark,H.,
            Urlaub,H. and Luhrmann,R.
  TITLE     The evolutionarily conserved core design of the catalytic
            activation step of the yeast spliceosome
  JOURNAL   Mol Cell 36 (4), 593-608 (2009)
   PUBMED   19941820
REFERENCE   10 (residues 1 to 348)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008898.6 and AC109465.3.
            
            On Nov 13, 2025 this sequence version replaced XP_011541398.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.948933.1,
                                           SRR14038192.3016042.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..348
                     /product="spliceosome-associated protein CWC27 homolog
                     isoform 6"
                     /EC_number="5.2.1.8"
                     /note="serologically defined colon cancer antigen 10;
                     peptidyl-prolyl cis-trans isomerase SDCCAG10;
                     peptidyl-prolyl cis-trans isomerase CWC27 homolog; PPIase
                     SDCCAG10; antigen NY-CO-10; PPIase CWC27; probable
                     inactive peptidyl-prolyl cis-trans isomerase CWC27
                     homolog; spliceosome-associated protein CWC27 homolog;
                     CWC27 spliceosome associated protein homolog"
                     /calculated_mol_wt=39003
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q6UX04.1)"
     Region          8..178
                     /region_name="cyclophilin_CeCYP16-like"
                     /note="cyclophilin-type peptidylprolyl cis- trans
                     isomerase) (PPIase) domain similar to Caenorhabditis
                     elegans cyclophilin 16. C. elegans CeCYP-16, compared to
                     the archetypal cyclophilin Human cyclophilin A has, a
                     reduced peptidylprolyl cis- trans isomerase...; cd01925"
                     /db_xref="CDD:238906"
     Site            order(55..56,61,112,114,122)
                     /site_type="active"
                     /db_xref="CDD:238906"
     Site            109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UX04.1)"
     Site            201
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (Q6UX04.1)"
     CDS             1..348
                     /gene="CWC27"
                     /gene_synonym="NY-CO-10; RPSKA; SDCCAG-10; SDCCAG10"
                     /coded_by="NM_001410740.1:218..1264"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:10283"
                     /db_xref="HGNC:HGNC:10664"
                     /db_xref="MIM:617170"
ORIGIN      
        1 msniyiqepp tngkvllktt agdidielws keapkacrnf iqlcleayyd ntifhrvvpg
       61 fivqggdptg tgsggesiyg apfkdefhsr lrfnrrglva managshdng sqffftlgra
      121 delnnkhtif gkvtgdtvyn mlrlsevdid dderphnphk ikscevlfnp fddiipreik
      181 rlkkekpeee vkklkpkgtk nfsllsfgee aeeeeeevnr vsqsmkgksk sshdllkddp
      241 hlssvpvves ekgdapdlvd dgedesaehd eyidgdeknl mreriakklk kdtsanvksa
      301 gegevekksv srscgsaphh lhsrpgmkeq llsemcyshg rrkrvmke
//
LOCUS       NP_001393996             513 aa            linear   PRI 21-NOV-2025
DEFINITION  merlin isoform 16 [Homo sapiens].
ACCESSION   NP_001393996
VERSION     NP_001393996.1
DBSOURCE    REFSEQ: accession NM_001407067.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 513)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 513)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 513)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 513)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 513)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005529.7 and AC004882.3.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF369667.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2163105
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..513
                     /product="merlin isoform 16"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=59943
     Region          <4..145
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          139..235
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(181..182,184..190,199,220,223..224,227)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(181,184..191,199,220,223..224,227)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(217,221)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            220..235
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          230..>290
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          269..388
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          441..>502
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     CDS             1..513
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_001407067.1:623..2164"
                     /note="isoform 16 is encoded by transcript variant 23"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 mklvldhdvs keepvtfhfl akfypenaee elvqeitqhl fflqvkkqil dekiycppea
       61 svllasyavq akygdydpsv hkrgflaqee llpkrvinly qmtpemweer itawyaehrg
      121 rardeaemey lkiaqdlemy gvnyfairnk kgtelllgvd alglhiydpe nrltpkisfp
      181 wneirnisys dkeftikpld kkidvfkfns sklrvnklil qlcignhdlf mrrrkadsle
      241 vqqmkaqare ekarkqmerq rlarekqmre eaertrdele rrllqmkeea tmanealmrs
      301 eetadllaek aqiteeeakl laqkaaeaeq emqrikatai rteeekrlme qkvleaevla
      361 lkmaeeserr akeadqlkqd lqeareaerr akqklleiat kptyppmnpi paplppdips
      421 fnligdslsf dfkdtdmkrl smeiekekve ymekskhlqe qlnelkteie alklkereta
      481 ldilhnensd rggsskhnti kkpqaqgrrp ici
//
LOCUS       NP_001394386            2760 aa            linear   PRI 21-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform q [Homo sapiens].
ACCESSION   NP_001394386
VERSION     NP_001394386.1
DBSOURCE    REFSEQ: accession NM_001407457.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2760)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2760)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2760)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2760)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2760)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2760)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2760)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2760)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2760)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2760)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.4497727.1,
                                           SRR18074967.1992203.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2760
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2760
                     /product="adenomatous polyposis coli protein isoform q"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=302136
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Region          <8..272
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          239..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          <307..365
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          389..425
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          429..470
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          433..470
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          480..512
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(503,507,511,550,554,558,595,599,603)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          520..561
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          566..606
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          570..604
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          608..648
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          612..648
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          649..936
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          953..1052
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1174..>1191
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1200..1285
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1208..1618
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1288..1310
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1554..1577
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1579..1632
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1633..1654
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1663..1756
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1790..1864
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1950..1969
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2140..2485
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2587..2760
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2760
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001407457.1:171..8453"
                     /note="isoform q is encoded by transcript variant 27"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrriar iqqiekdilr irqllqsqat
      241 eaerssqnkh etgshdaerq negqgvgein matsgngqgs ttrmdhetas vlssssthsa
      301 prrltshlgt kiraycetcw ewqeahepgm dqdknpmpap vehqicpavc vlmklsfdee
      361 hrhamnelgr katrgissqe lgqglsgglq aiaellqvdc emygltndhy sitlrryagm
      421 altnltfgdv ankatlcsmk gcmralvaql ksesedlqqv iasvlrnlsw radvnskktl
      481 revgsvkalm ecalevkkes tlksvlsalw nlsahctenk adicavdgal aflvgtltyr
      541 sqtntlaiie sgggilrnvs sliatnedhr qilrennclq tllqhlkshs ltivsnacgt
      601 lwnlsarnpk dqealwdmga vsmlknlihs khkmiamgsa aalrnlmanr pakykdanim
      661 spgsslpslh vrkqkaleae ldaqhlsetf dnidnlspka shrskqrhkq slygdyvfdt
      721 nrhddnrsdn fntgnmtvls pylnttvlps ssssrgslds srsekdrsle rergiglgny
      781 hpatenpgts skrglqistt aaqiakvmee vsaihtsqed rssgsttelh cvtdernalr
      841 rssaahthsn tynftksens nrtcsmpyak leykrssnds lnsvsssdgy gkrgqmkpsi
      901 esyseddesk fcsygqypad lahkihsanh mddndgeldt pinyslkysd eqlnsgrqsp
      961 sqnerwarpk hiiedeikqs eqrqsrnqst typvytestd dkhlkfqphf gqqecvspyr
     1021 srgangsetn rvgsnhginq nvsqslcqed dyeddkptny seryseeeqh eeeerptnys
     1081 ikyneekrhv dqpidyslky atdipssqkq sfsfsksssg qssktehmss ssentstpss
     1141 nakrqnqlhp ssaqsrsgqp qkaatckvss inqetiqtyc vedtpicfsr csslsslssa
     1201 edeigcnqtt qeadsantlq iaeikekigt rsaedpvsev pavsqhprtk ssrlqgssls
     1261 sesarhkave fssgakspsk sgaqtpkspp ehyvqetplm fsrctsvssl dsfesrsias
     1321 svqsepcsgm vsgiispsdl pdspgqtmpp srsktppppp qtaqtkrevp knkaptaekr
     1381 esgpkqaavn aavqrvqvlp dadtllhfat estpdgfscs sslsalslde pfiqkdvelr
     1441 imppvqendn gneteseqpk esnenqekea ektidsekdl lddsddddie ileeciisam
     1501 ptkssrkakk paqtasklpp pvarkpsqlp vykllpsqnr lqpqkhvsft pgddmprvyc
     1561 vegtpinfst atslsdltie sppnelaage gvrggaqsge fekrdtipte grstdeaqgg
     1621 ktssvtipel ddnkaeegdi laecinsamp kgkshkpfrv kkimdqvqqa sasssapnkn
     1681 qldgkkkkpt spvkpipqnt eyrtrvrkna dsknnlnaer vfsdnkdskk qnlknnskvf
     1741 ndklpnnedr vrgsfafdsp hhytpiegtp ycfsrndsls sldfddddvd lsrekaelrk
     1801 akenkeseak vtshteltsn qqsanktqai akqpinrgqp kpilqkqstf pqsskdipdr
     1861 gaatdeklqn faientpvcf shnsslssls didqennnke nepiketepp dsqgepskpq
     1921 asgyapksfh vedtpvcfsr nsslsslsid seddllqeci ssampkkkkp srlkgdnekh
     1981 sprnmggilg edltldlkdi qrpdsehgls pdsenfdwka iqegansivs slhqaaaaac
     2041 lsrqassdsd silslksgis lgspfhltpd qeekpftsnk gprilkpgek stletkkies
     2101 eskgikggkk vykslitgkv rsnseisgqm kqplqanmps isrgrtmihi pgvrnsssst
     2161 spvskkgppl ktpaskspse gqtattsprg akpsvksels pvarqtsqig gsskapsrsg
     2221 srdstpsrpa qqplsrpiqs pgrnsispgr ngisppnkls qlprtsspst astkssgsgk
     2281 msytspgrqm sqqnltkqtg lsknassipr sesaskglnq mnngngankk velsrmsstk
     2341 ssgsesdrse rpvlvrqstf ikeapsptlr rkleesasfe slspssrpas ptrsqaqtpv
     2401 lspslpdmsl sthssvqagg wrklppnlsp tieyndgrpa krhdiarshs espsrlpinr
     2461 sgtwkrehsk hssslprvst wrrtgssssi lsassessek aksedekhvn sisgtkqske
     2521 nqvsakgtwr kikenefspt nstsqtvssg atngaesktl iyqmapavsk tedvwvried
     2581 cpinnprsgr sptgntppvi dsvsekanpn ikdskdnqak qnvgngsvpm rtvglenrln
     2641 sfiqvdapdq kgteikpgqn npvpvsetne ssivertpfs ssssskhssp sgtvaarvtp
     2701 fnynpsprks sadstsarps qiptpvnnnt kkrdsktdst essgtqspkr hsgsylvtsv
//
LOCUS       NP_001427981            4240 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HUWE1 isoform 6 [Homo sapiens].
ACCESSION   NP_001427981 XP_047297706 XP_054182302
VERSION     NP_001427981.1
DBSOURCE    REFSEQ: accession NM_001441052.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4240)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 4240)
  AUTHORS   Lee,C., Park,S.H. and Yoon,S.K.
  TITLE     The E3 ligase HUWE1 increases the sensitivity of CRC to oxaliplatin
            through TOMM20 degradation
  JOURNAL   Oncogene 43 (9), 636-649 (2024)
   PUBMED   38184713
  REMARK    GeneRIF: The E3 ligase HUWE1 increases the sensitivity of CRC to
            oxaliplatin through TOMM20 degradation.
REFERENCE   3  (residues 1 to 4240)
  AUTHORS   Li,X.X., Xu,J.K., Su,W.J., Wu,H.L., Zhao,K., Zhang,C.M., Chen,X.K.
            and Yang,L.X.
  TITLE     The role of KDM4A-mediated histone methylation on temozolomide
            resistance in glioma cells through the HUWE1/ROCK2 axis
  JOURNAL   Kaohsiung J Med Sci 40 (2), 161-174 (2024)
   PUBMED   37873881
  REMARK    GeneRIF: The role of KDM4A-mediated histone methylation on
            temozolomide resistance in glioma cells through the HUWE1/ROCK2
            axis.
REFERENCE   4  (residues 1 to 4240)
  AUTHORS   Bernassola,F., Karin,M., Ciechanover,A. and Melino,G.
  TITLE     The HECT family of E3 ubiquitin ligases: multiple players in cancer
            development
  JOURNAL   Cancer Cell 14 (1), 10-21 (2008)
   PUBMED   18598940
  REMARK    Review article
REFERENCE   5  (residues 1 to 4240)
  AUTHORS   Zhong,Q., Gao,W., Du,F. and Wang,X.
  TITLE     Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the
            polyubiquitination of Mcl-1 and regulates apoptosis
  JOURNAL   Cell 121 (7), 1085-1095 (2005)
   PUBMED   15989957
  REMARK    GeneRIF: Mule is both required and sufficient for the
            polyubiquitination of Mcl-1; Mule is a unique BH3-containing E3
            ubiquitin ligase apical to Bcl-2 family proteins during DNA
            damage-induced apoptosis
            GeneRIF: Mule (HUWE1) poly-ubiquitinates anti-apoptotic gene Mcl-1.
REFERENCE   6  (residues 1 to 4240)
  AUTHORS   Chen,D., Kon,N., Li,M., Zhang,W., Qin,J. and Gu,W.
  TITLE     ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
  JOURNAL   Cell 121 (7), 1071-1083 (2005)
   PUBMED   15989956
  REMARK    GeneRIF: study modifies the current view of ARF-mediated p53
            activation and reveals that ARF-BP1 is a critical mediator of both
            the p53-independent and p53-dependent tumor suppressor functions of
            ARF
            GeneRIF: Ubiquitin ligase activity of ARF-BP1 (HUWE1) is inhibited
            by Arf.
REFERENCE   7  (residues 1 to 4240)
  AUTHORS   Liu,Z., Oughtred,R. and Wing,S.S.
  TITLE     Characterization of E3Histone, a novel testis ubiquitin protein
            ligase which ubiquitinates histones
  JOURNAL   Mol Cell Biol 25 (7), 2819-2831 (2005)
   PUBMED   15767685
REFERENCE   8  (residues 1 to 4240)
  AUTHORS   Gu,J., Dubner,R., Fornace,A.J. Jr. and Iadarola,M.J.
  TITLE     UREB1, a tyrosine phosphorylated nuclear protein, inhibits p53
            transactivation
  JOURNAL   Oncogene 11 (10), 2175-2178 (1995)
   PUBMED   7478539
REFERENCE   9  (residues 1 to 4240)
  AUTHORS   Turner,G., Gedeon,A. and Mulley,J.
  TITLE     X-linked mental retardation with heterozygous expression and
            macrocephaly: pericentromeric gene localization
  JOURNAL   Am J Med Genet 51 (4), 575-580 (1994)
   PUBMED   7943042
REFERENCE   10 (residues 1 to 4240)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX323845.7 and AC231658.3.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297706.1, XP_054182302.1.
            
            Summary: This gene encodes a protein containing a C-terminal HECT
            (E6AP type E3 ubiquitin protein ligase) domain that functions as an
            E3 ubiquitin ligase. The encoded protein is required for the
            ubiquitination and subsequent degradation of the anti-apoptotic
            protein Mcl1 (myeloid cell leukemia sequence 1 (BCL2-related)).
            This protein also ubiquitinates the p53 tumor suppressor, core
            histones, and DNA polymerase beta. Mutations in this gene are
            associated with Turner type X-linked syndromic cognitive
            disability. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3008101.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..4240
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..4240
                     /product="E3 ubiquitin-protein ligase HUWE1 isoform 6"
                     /EC_number="2.3.2.26"
                     /note="Mcl-1 ubiquitin ligase E3; BJ-HCC-24 tumor antigen;
                     HECT domain protein LASU1; ARF-binding protein 1;
                     URE-binding protein 1; large structure of UREB1; upstream
                     regulatory element-binding protein 1; homologous to E6AP
                     carboxyl terminus homologous protein 9; HECT-type E3
                     ubiquitin transferase HUWE1; HECT, UBA and WWE domain
                     containing 1, E3 ubiquitin protein ligase"
                     /calculated_mol_wt=466388
     Region          92..367
                     /region_name="DUF908"
                     /note="Domain of Unknown Function (DUF908); pfam06012"
                     /db_xref="CDD:428721"
     Region          431..814
                     /region_name="DUF913"
                     /note="Domain of Unknown Function (DUF913); pfam06025"
                     /db_xref="CDD:461803"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          706..759
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          978..1001
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1014..1037
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1084
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1291..1320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1317..1356
                     /region_name="UBA_HUWE1"
                     /note="UBA domain found in eukaryotic E3 ubiquitin-protein
                     ligase HUWE1 and similar proteins; cd14288"
                     /db_xref="CDD:270474"
     Site            1368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1396..1415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1617..1678
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          1689..1735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1722
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1907
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2018..2065
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2035
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2262..2342
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2267
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          <2601..2932
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          2876..2909
                     /region_name="UBM"
                     /note="Ubiquitin binding region; pfam14377"
                     /db_xref="CDD:464159"
     Region          3885..4238
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(3889,3919,3930,3991,4165,4201..4202,4205..4209,4229,
                     4237)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(4019,4022..4023,4025..4026,4029,4036,4038,
                     4042..4043,4045,4050,4055,4072,4076)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..4240
                     /gene="HUWE1"
                     /gene_synonym="ARF-BP1; HECTH9; HSPC272; Ib772; LASU1;
                     MRXST; MULE; URE-B1; UREB1"
                     /coded_by="NM_001441052.1:426..13148"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:10075"
                     /db_xref="HGNC:HGNC:30892"
                     /db_xref="MIM:300697"
ORIGIN      
        1 mkvdrtklkk tpteapadcr alidklkvcn deqlllelqq iktwnigkce lyhwvdlldr
       61 fdgiladagq tvenmswmlv cdrpereqlk mlllavlnft allieysfsr hlyssiehlt
      121 tllassdmqv vlavlnllyv fskrsnyitr lgsdkrtpll trlqhlaesw ggkengfgla
      181 eccrdlhmmk yppsattlhf efyadpgaev kiekrttsnt lhyihieqld kisespseim
      241 esltkmysip kdkqmllfth irlahgfsnh rkrlqavqar lhaisilvys nalqesansi
      301 lynglieelv dvlqitdkql meikaaslrt ltsivhlert pklssiidct gtasyhgflp
      361 vlvrnciqam idpsmdpyph qfatalfsfl yhlasydagg ealvscgmme allkvikflg
      421 deqdqitfvt ravrvvdlit nldmaafqsh sglsifiyrl ehevdlcrke cpfvikpkiq
      481 rpnttqegee metdmdgvqc ipqraallks mlnflkkaiq dpafsdgirh vmdgslptsl
      541 khiisnaeyy gpslfllate vvtvfvfqep sllsslqdng ltdvmlhall ikdvpatrev
      601 lgslpnvfsa lclnarglqs fvqcqpferl fkvllspdyl pamrrrrssd plgdtasnlg
      661 savdelmrhq ptlktdatta iiklleeicn lgrdpkyicq kpsiqkadgt atappprsnh
      721 aaeeassede eeeevqamqs fnstqqnete pnqqvvgtee ripiplmdyi lnvmkfvesi
      781 lsnnttddhc qefvnqkgll plvtilglpn lpidfptsaa cqavagvcks iltlshepkv
      841 lqegllqlds ilssleplhr piespggsvl lrelacagnv adatlsaqat pllhaltaah
      901 ayimmfvhtc rvgqseirsi svnqwgsqlg lsvlsklsql ycslvwestv llslctpnsl
      961 psgcefgqad mqklvpkdek agttqggkrs dgeqdgaags mdastqglle gigldgdtla
     1021 pmetdeptas dskgkskitp amaarikqik pllsassrlg ralaelfgll vklcvgspvr
     1081 qrrshhaast ttaptpaars tasaltkllt kglswqpppy tptprfrltf ficsvgftsp
     1141 mlfderkypy hlmlqkflcs gghnalfetf nwalsmggkv pvseglehsd lpdgtgefld
     1201 awlmlvekmv npttvlesph slpaklpggv qnfpqfsalr flvvtqkaaf tciknlwnrk
     1261 plkvyggrma esmlailchi lrgepvirer lskekegsrg eedtgqeegg srrepqvnqq
     1321 qlqqlmdmgf trehameall ntstmeqate yllthpppim ggvvrdlsms eedqmmraia
     1381 mslgqdipmd qraespeeva crkeeeerka rekqeeeeak clekfqdadp leqdelhtft
     1441 dtmlpgcfhl ldelpdtvyr vcdlimtaik rngadyrdmi lkqvvnqvwe aadvlikaal
     1501 plttsdtktv sewisqmatl pqasnlatri llltllfeel klpcawvves sgilnvlikl
     1561 levvqpclqa akeqkevqtp kwitpvllli dfyektaiss krraqmtkyl qsnsnnwrwf
     1621 ddrsgrwcsy sasnnstids awksgetsvr ftagrrrytv qfttmvqvne etgnrrpvml
     1681 tllrvprlnk nsknsngqel ektleeskem dikrkenkgn dtplalestn teketsleet
     1741 kigeiliqgl tedmvtvlir acvsmlgvpv dpdtlhatlr lclrltrdhk yammfaelks
     1801 trmilnltqs sgfngftplv tlllrhiied pctlrhtmek vvrsaatsga gsttsgvvsg
     1861 slgsreinyi lrvlgpaacr npdiftevan ccirialpap rgsgtasdde fenlrikgpn
     1921 avqlvkttpl kpsplpvipd tikeviydml nalaayhape eadksdpkpg vmtqevgqll
     1981 qdmgddvyqq yrsltrqssd fdtqsgfsin sqvfaadgas tetsasgtsq geastpeesr
     2041 dgkkdkegdr aseegkqkgk gskplmptst ilrllaelvr syvgiatlia nysytvgqse
     2101 likedcsvla fvldhllpht qnaedkdtpa larlflasla aagsgtdaqv alvnevkaal
     2161 gralamaest ekharlqavm ciistimesc pstssfyssa taktqhngmn niirlflkkg
     2221 lvndlarvph sldlsspnma ntvnaalkpl etlsrivnqp sslfgsksas sknkseqdaq
     2281 gasqdsssnq qdpgepgeae vqeedhdvtq tevadgdimd geaetdsvvi agqpevlssq
     2341 emqveneled lidellerdg gsgnstiiad ippspgnipt thplmvrhad hssltlgsgs
     2401 sttrltqgig rsqrtlrqlt antghtihvh ypgnrqpnpp lilqrllgps aaadilqlss
     2461 slplqsrgra rllvgnddvh iiarsddell ddffhdqsta tsqagtlssi ptaltrwtee
     2521 ckvldaesmh dcvsvvkvsi vnhleflrde eleerrekrr kqlaeeetki tdkgkedken
     2581 rdqsaqctas ksndsteqnl sdgtpmpdsy pttpsstdaa tsesketlgt lqssqqqptl
     2641 ptppalgevp qelqspageg gsstqllmpv epeelgptrp sgeaettqme lspaptitsl
     2701 speraedsda ltavssqleg spmdtsslas ctleeavgdt saagsseqpr agsstpgdap
     2761 pavaevqgrs dgsgesaqpp edssppasse ssstrdsava isgadsrgil eeplpstsse
     2821 eedplagisl pegvdpsfla alpddirrev lqnqlgirpp trtapstnss apavvgnpgv
     2881 tevspeflaa lppaiqeevl aqqraeqqrr elaqnassdt pmdpvtfiqt lpsdlrrsvl
     2941 edmedsvlav mppdiaaeaq alrreqearq rqlmherlfg hsstsalsai lrspaftsrl
     3001 sgnrgvqytr lavqrggtfq mggssshnrp sgsnvdtllr lrgrllldhe alscllvllf
     3061 vdepklntsr lhrvlrnlcy haqtrhwvir sllsilqrss eselcietpk lttseekgkk
     3121 sskscgsssh enrpldllhk meskssnqls wlsvsmdaal gcrtnifqiq rsggrkhtek
     3181 hasggstvhi hpqaapvvcr hvldtliqla kvfpshftqq rtketncesd rergnkacsp
     3241 cssqssssgi ctdfwdllvk ldnmnvsrkg knsvksvpvs aggegetspy sleasplgql
     3301 mnmlshpvir rsslltekll rllslisial penkvseaqa nsgsgasstt tatsttsttt
     3361 ttaasttptp ptaptpvtsa palvaatais tivvaasttv ttpttatttv sispttkgsk
     3421 spakvsdggs sstdfkmvss gltenqlqls vevltshscs eegledaanv llqlsrgdsg
     3481 trdtvlklll ngarhlgytl ckqigtllae lreynleqqr raqcetlspd glpeeqpqtt
     3541 klkgkmqsrf dmaenvviva sqkrplggre lqlpsmsmlt sktstqkffl rvlqviiqlr
     3601 ddtrrankka kqtgrlgssg lgsassiqaa vrqleaeada iiqmvregqr arrqqqaats
     3661 essqseasvr reespmdvdq pspsaqdtqs iasdgtpqge kekeerppel pllseqlsld
     3721 elwdmlgecl keleeshdqh avlvlqpave afflvhater eskppvrdtr esqlahikde
     3781 ppplspaplt patpssldpf fsrepssmhi ssslppdtqk flrfaethrt vlnqilrqst
     3841 thladgpfav lvdyirvldf dvkrkyfrqe lerldeglrk edmavhvrrd hvfedsyrel
     3901 hrkspeemkn rlyivfegee gqdaggllre wymiisremf npmyalfrts pgdrvtytin
     3961 psshcnpnhl syfkfvgriv akavydnrll ecyftrsfyk hilgksvryt dmesedyhfy
     4021 qglvyllend vstlgydltf stevqefgvc evrdlkpnga nilvteenkk eyvhlvcqmr
     4081 mtgairkqla aflegfyeii pkrlisifte qelellisgl ptididdlks nteyhkyqsn
     4141 siqiqwfwra lrsfdqadra kflqfvtgts kvplqgfaal egmngiqkfq ihrddrstdr
     4201 lpsahtcfnq ldlpayesfe klrhmlllai qecsegfgla
//
LOCUS       NP_001401618             499 aa            linear   PRI 21-NOV-2025
DEFINITION  nucleolar complex protein 4 homolog isoform 3 [Homo sapiens].
ACCESSION   NP_001401618 XP_016875449
VERSION     NP_001401618.1
DBSOURCE    REFSEQ: accession NM_001414689.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Talebi,A., Shahidsales,S., Aliakbarian,M., Pezeshki Rad,M. and
            Kerachian,M.A.
  TITLE     Oncogenic fusion transcript analysis identified ADAP1-NOC4L,
            potentially associated with metastatic colorectal cancer
  JOURNAL   Cancer Med 12 (1), 525-540 (2023)
   PUBMED   35702822
  REMARK    GeneRIF: Oncogenic fusion transcript analysis identified
            ADAP1-NOC4L, potentially associated with metastatic colorectal
            cancer.
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Qin,Y., Li,H., Jia,L., Yan,J., Gao,G.F. and Li,X.
  TITLE     Targeted disruption of Noc4l leads to preimplantation embryonic
            lethality in mice
  JOURNAL   Protein Cell 8 (3), 230-235 (2017)
   PUBMED   28012024
  REMARK    GeneRIF: The results provide the first in vivo genetic evidence
            that Noc4l plays important roles in early embryogenesis in mice.
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Bernstein,K.A., Gallagher,J.E., Mitchell,B.M., Granneman,S. and
            Baserga,S.J.
  TITLE     The small-subunit processome is a ribosome assembly intermediate
  JOURNAL   Eukaryot Cell 3 (6), 1619-1626 (2004)
   PUBMED   15590835
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Milkereit,P., Strauss,D., Bassler,J., Gadal,O., Kuhn,H., Schutz,S.,
            Gas,N., Lechner,J., Hurt,E. and Tschochner,H.
  TITLE     A Noc complex specifically involved in the formation and nuclear
            export of ribosomal 40 S subunits
  JOURNAL   J Biol Chem 278 (6), 4072-4081 (2003)
   PUBMED   12446671
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC138466.12.
            
            On Dec 6, 2022 this sequence version replaced XP_016875449.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.994200.1,
                                           SRR18074969.1853124.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.33"
     Protein         1..499
                     /product="nucleolar complex protein 4 homolog isoform 3"
                     /note="nucleolar complex protein 4 homolog; NOC4-like
                     protein; NOC4 protein homolog; nucleolar
                     complex-associated protein 4-like protein"
                     /calculated_mol_wt=56141
     Region          293..435
                     /region_name="CBF"
                     /note="CBF/Mak21 family; pfam03914"
                     /db_xref="CDD:461090"
     CDS             1..499
                     /gene="NOC4L"
                     /gene_synonym="NET49; NOC4; UTP19"
                     /coded_by="NM_001414689.1:33..1532"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:79050"
                     /db_xref="HGNC:HGNC:28461"
                     /db_xref="MIM:612819"
ORIGIN      
        1 merepgaagv rralgrrlea vlasrseana vfdilavlqs edqeeiqeav rtcsrlfgal
       61 lergelfvgq lpseemvmtg sqgatrkykv wmrhryhscc nrlgellghp sfqvkelals
      121 allkfvqleg ahplekskwe gnylfprelf klvvggllsp eedqslllsq freyldyddt
      181 ryhtmqaavd avarvtgqhp evppafwnna ftllsavslp rreptvssfy vkraelwdtw
      241 kvahlklpls lykkvllivh dailpqlaqp tlmidfltra cdlggalsll alnglfilih
      301 khnleypdfy rklyglldps vfhvkyrarf fhladlflss shlpaylvaa fakrlarlal
      361 tappeallmv lpficnllrr hpacrvlvhr phgpeldadp ydpgeedpaq sralesslwe
      421 lqalqrhyhp evskaasvin qalsmpevsi aplleltaye iferdlkkkg pepvplefip
      481 aqgllgrpge lcaqhftls
//
LOCUS       NP_001428028             373 aa            linear   PRI 21-NOV-2025
DEFINITION  sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating [Homo
            sapiens].
ACCESSION   NP_001428028 XP_011529480 XP_054183139 XP_054189320
VERSION     NP_001428028.1
DBSOURCE    REFSEQ: accession NM_001441099.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Chen,M., Zhao,Y., Yang,X., Zhao,Y., Liu,Q., Liu,Y., Hou,Y., Sun,H.
            and Jin,W.
  TITLE     NSDHL promotes triple-negative breast cancer metastasis through the
            TGFbeta signaling pathway and cholesterol biosynthesis
  JOURNAL   Breast Cancer Res Treat 187 (2), 349-362 (2021)
   PUBMED   33864166
  REMARK    GeneRIF: NSDHL promotes triple-negative breast cancer metastasis
            through the TGFbeta signaling pathway and cholesterol biosynthesis.
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tang,M.M., Tan,W.C., Surana,U., Leong,K.F. and Pramano,Z.A.D.
  TITLE     CHILD syndrome in a Malaysian adult with identification of a novel
            heterozygous missense mutation NSDHL c.602A>G
  JOURNAL   Int J Dermatol 60 (4), e154-e156 (2021)
   PUBMED   33169834
  REMARK    GeneRIF: CHILD syndrome in a Malaysian adult with identification of
            a novel heterozygous missense mutation NSDHL c.602A>G.
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Xiao,Y., Xie,J., Liu,L., Huang,W., Han,Q., Qin,J., Liu,S. and
            Jiang,Z.
  TITLE     NAD(P)-dependent steroid dehydrogenase-like protein and neutral
            cholesterol ester hydrolase 1 serve as novel markers for early
            detection of gastric cancer identified using quantitative
            proteomics
  JOURNAL   J Clin Lab Anal 35 (2), e23652 (2021)
   PUBMED   33219617
  REMARK    GeneRIF: NAD(P)-dependent steroid dehydrogenase-like protein and
            neutral cholesterol ester hydrolase 1 serve as novel markers for
            early detection of gastric cancer identified using quantitative
            proteomics.
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Yoon,S.H., Kim,H.S., Kim,R.N., Jung,S.Y., Hong,B.S., Kang,E.J.,
            Lee,H.B., Moon,H.G., Noh,D.Y. and Han,W.
  TITLE     NAD(P)-dependent steroid dehydrogenase-like is involved in breast
            cancer cell growth and metastasis
  JOURNAL   BMC Cancer 20 (1), 375 (2020)
   PUBMED   32366230
  REMARK    GeneRIF: NAD(P)-dependent steroid dehydrogenase-like is involved in
            breast cancer cell growth and metastasis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Heiss,N.S., Rogner,U.C., Kioschis,P., Korn,B. and Poustka,A.
  TITLE     Transcription mapping in a 700-kb region around the DXS52 locus in
            Xq28: isolation of six novel transcripts and a novel ATPase isoform
            (hPMCA5)
  JOURNAL   Genome Res 6 (6), 478-491 (1996)
   PUBMED   8828037
REFERENCE   7  (residues 1 to 373)
  AUTHORS   Levin,M.L., Chatterjee,A., Pragliola,A., Worley,K.C., Wehnert,M.,
            Zhuchenko,O., Smith,R.F., Lee,C.C. and Herman,G.E.
  TITLE     A comparative transcription map of the murine bare patches (Bpa)
            and striated (Str) critical regions and human Xq28
  JOURNAL   Genome Res 6 (6), 465-477 (1996)
   PUBMED   8828036
REFERENCE   8  (residues 1 to 373)
  AUTHORS   Kurban,M., El Feghaly,J. and Hamie,L.
  TITLE     NSDHL-Related Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21290788
REFERENCE   9  (residues 1 to 373)
  AUTHORS   Angel,T.A., Faust,C.J., Gonzales,J.C., Kenwrick,S., Lewis,R.A. and
            Herman,G.E.
  TITLE     Genetic mapping of the X-linked dominant mutations striated (Str)
            and bare patches (Bpa) to a 600-kb region of the mouse X
            chromosome: implications for mapping human disorders in Xq28
  JOURNAL   Mamm Genome 4 (3), 171-176 (1993)
   PUBMED   8439729
REFERENCE   10 (residues 1 to 373)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U82671.5.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_011529480.1, XP_054189320.1, XP_054183139.1.
            
            Summary: The protein encoded by this gene is localized in the
            endoplasmic reticulum and is involved in cholesterol biosynthesis.
            Mutations in this gene are associated with CHILD syndrome, which is
            a X-linked dominant disorder of lipid metabolism with disturbed
            cholesterol biosynthesis, and typically lethal in males.
            Alternatively spliced transcript variants with differing 5' UTR
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4420920.1,
                                           SRR14372079.1860219.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..373
                     /product="sterol-4-alpha-carboxylate 3-dehydrogenase,
                     decarboxylating"
                     /EC_number="1.1.1.170"
                     /note="short chain dehydrogenase/reductase family 31E,
                     member 1; protein H105e3; 3-beta-hydroxysteroid
                     dehydrogenase; epididymis secretory sperm binding protein;
                     NAD(P) dependent steroid dehydrogenase-like protein
                     transcript; 3beta-hydroxysteroid-4alpha-carboxylate
                     3-dehydrogenase (decarboxylating)"
                     /calculated_mol_wt=41769
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q15738.2)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15738.2)"
     Region          39..366
                     /region_name="3b-HSD-NSDHL-like_SDR_e"
                     /note="human NSDHL (NAD(P)H steroid dehydrogenase-like
                     protein)-like, extended (e) SDRs; cd09813"
                     /db_xref="CDD:187673"
     Site            order(44,46..49,68..70,104..106,120,143..145,172,176,
                     200..203)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187673"
     Site            order(121,145,172,176)
                     /site_type="active"
                     /db_xref="CDD:187673"
     Site            order(145,172,202,215,226,231)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187673"
     Site            298..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15738.2)"
     Region          370..373
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000250|UniProtKB:Q9R1J0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15738.2)"
     CDS             1..373
                     /gene="NSDHL"
                     /gene_synonym="H105E3; SDR31E1; XAP104"
                     /coded_by="NM_001441099.1:260..1381"
                     /db_xref="GeneID:50814"
                     /db_xref="HGNC:HGNC:13398"
                     /db_xref="MIM:300275"
ORIGIN      
        1 mepavsepmr dqvarthlte dtpkvnadie kvnqnqakrc tviggsgflg qhmveqllar
       61 gyavnvfdiq qgfdnpqvrf flgdlcsrqd lypalkgvnt vfhcasppps snnkelfyrv
      121 nyigtknvie tckeagvqkl iltssasvif egvdikngte dlpyamkpid yytetkilqe
      181 ravlgandpe knflttairp hgifgprdpq lvpilieaar ngkmkfvign gknlvdftfv
      241 envvhghila aeqlsrdstl ggkafhitnd epipfwtfls riltglnyea pkyhipywva
      301 yylalllsll vmvispviql qptftpmrva lagtfhyysc erakkamgyq plvtmddame
      361 rtvqsfrhlr rvk
//
LOCUS       NP_001392811             683 aa            linear   PRI 21-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 1 isoform 9 [Homo sapiens].
ACCESSION   NP_001392811
VERSION     NP_001392811.1
DBSOURCE    REFSEQ: accession NM_001405882.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Awamleh,Z., Choufani,S., Wu,W., Rots,D., Dingemans,A.J.M., Nadif
            Kasri,N., Boronat,S., Ibanez-Mico,S., Cuesta Herraiz,L., Ferrer,I.,
            Martinez Carrascal,A., Perez-Jurado,L.A., Aznar Lain,G.,
            Ortigoza-Escobar,J.D., de Vries,B.B.A., Koolen,D.A. and Weksberg,R.
  TITLE     A new blood DNA methylation signature for Koolen-de Vries syndrome:
            Classification of missense KANSL1 variants and comparison to
            fibroblast cells
  JOURNAL   Eur J Hum Genet 32 (3), 324-332 (2024)
   PUBMED   38282074
  REMARK    GeneRIF: A new blood DNA methylation signature for Koolen-de Vries
            syndrome: Classification of missense KANSL1 variants and comparison
            to fibroblast cells.
            Erratum:[Eur J Hum Genet. 2024 Mar;32(3):366. doi:
            10.1038/s41431-024-01561-7. PMID: 38355964]
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   4  (residues 1 to 683)
  AUTHORS   Agaimy,A., Clarke,B.A., Kolin,D.L., Lee,C.H., Lee,J.C.,
            McCluggage,W.G., Poschke,P., Stoehr,R., Swanson,D., Turashvili,G.,
            Beckmann,M.W., Hartmann,A., Antonescu,C.R. and Dickson,B.C.
  TITLE     Recurrent KAT6B/A::KANSL1 Fusions Characterize a Potentially
            Aggressive Uterine Sarcoma Morphologically Overlapping With
            Low-grade Endometrial Stromal Sarcoma
  JOURNAL   Am J Surg Pathol 46 (9), 1298-1308 (2022)
   PUBMED   35575789
  REMARK    GeneRIF: Recurrent KAT6B/A::KANSL1 Fusions Characterize a
            Potentially Aggressive Uterine Sarcoma Morphologically Overlapping
            With Low-grade Endometrial Stromal Sarcoma.
REFERENCE   5  (residues 1 to 683)
  AUTHORS   Kousathanas,A., Pairo-Castineira,E., Rawlik,K., Stuckey,A.,
            Odhams,C.A., Walker,S., Russell,C.D., Malinauskas,T., Wu,Y.,
            Millar,J., Shen,X., Elliott,K.S., Griffiths,F., Oosthuyzen,W.,
            Morrice,K., Keating,S., Wang,B., Rhodes,D., Klaric,L., Zechner,M.,
            Parkinson,N., Siddiq,A., Goddard,P., Donovan,S., Maslove,D.,
            Nichol,A., Semple,M.G., Zainy,T., Maleady-Crowe,F., Todd,L.,
            Salehi,S., Knight,J., Elgar,G., Chan,G., Arumugam,P., Patch,C.,
            Rendon,A., Bentley,D., Kingsley,C., Kosmicki,J.A., Horowitz,J.E.,
            Baras,A., Abecasis,G.R., Ferreira,M.A.R., Justice,A., Mirshahi,T.,
            Oetjens,M., Rader,D.J., Ritchie,M.D., Verma,A., Fowler,T.A.,
            Shankar-Hari,M., Summers,C., Hinds,C., Horby,P., Ling,L.,
            McAuley,D., Montgomery,H., Openshaw,P.J.M., Elliott,P., Walsh,T.,
            Tenesa,A., Fawkes,A., Murphy,L., Rowan,K., Ponting,C.P., Vitart,V.,
            Wilson,J.F., Yang,J., Bretherick,A.D., Scott,R.H., Hendry,S.C.,
            Moutsianas,L., Law,A., Caulfield,M.J. and Baillie,J.K.
  CONSRTM   GenOMICC investigators; 23andMe investigators; COVID-19 Human
            Genetics Initiative
  TITLE     Whole-genome sequencing reveals host factors underlying critical
            COVID-19
  JOURNAL   Nature 607 (7917), 97-103 (2022)
   PUBMED   35255492
REFERENCE   6  (residues 1 to 683)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
REFERENCE   7  (residues 1 to 683)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 683)
  AUTHORS   Poorkaj,P., Kas,A., D'Souza,I., Zhou,Y., Pham,Q., Stone,M.,
            Olson,M.V. and Schellenberg,G.D.
  TITLE     A genomic sequence analysis of the mouse and human
            microtubule-associated protein tau
  JOURNAL   Mamm Genome 12 (9), 700-712 (2001)
   PUBMED   11641718
REFERENCE   9  (residues 1 to 683)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 683)
  AUTHORS   Koolen,D.A., Morgan,A. and de Vries,B.B.A.
  TITLE     Koolen-de Vries Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301783
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC217773.1, CR936218.6 and
            KF495991.1.
            
            Summary: This gene encodes a nuclear protein that is a subunit of
            two protein complexes involved with histone acetylation, the MLL1
            complex and the NSL1 complex. The encoded protein has been
            implicated in a variety of cellular processes including enhancer
            regulation, cell proliferation, and mitosis. Mutations in this gene
            are associated with Koolen-de Vries Syndrome. [provided by RefSeq,
            May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2563414.1,
                                           SRR18074969.2251281.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..683
                     /product="KAT8 regulatory NSL complex subunit 1 isoform 9"
                     /note="male-specific lethal 1 homolog; centromere protein
                     36; NSL complex protein NSL1; non-specific lethal 1
                     homolog; MSL1 homolog 1; MLL1/MLL complex subunit KANSL1"
                     /calculated_mol_wt=75606
     Region          463..583
                     /region_name="PEHE"
                     /note="PEHE domain; pfam15275"
                     /db_xref="CDD:464607"
     CDS             1..683
                     /gene="KANSL1"
                     /gene_synonym="C17DELq21.31; CENP-36; DEL17Q21.31;
                     hMSL1v1; KDVS; KIAA1267; MSL1v1; NSL1"
                     /coded_by="NM_001405882.1:139..2190"
                     /note="isoform 9 is encoded by transcript variant 23"
                     /db_xref="GeneID:284058"
                     /db_xref="HGNC:HGNC:24565"
                     /db_xref="MIM:612452"
ORIGIN      
        1 mllgcllrrr rsewkwaadr aaivsrwnwl qahvsdleyr irqqtdiykq irankglivl
       61 gevpppehtt dlflplssev ktdhgtdkli esvsqplenh gapiighise slstkscgal
      121 rpvngvintl qpvladhipg dssdaeeqlh kkqrlnlvss ssdgtcvaar trpvlsckkr
      181 rlvrpnsivp lskkvhrnst irpgcdvnps calcgsgsin tmppeihyea pllerlsqld
      241 scvhpvlafp ddvptslhfq smlksqwqnk pfdkikppkk lslkhrapmp gslpdsarkd
      301 rhklvssflt taklshhqtr pdrthrqhld dvgavpmver vtapkaerll nppppvhdpn
      361 hskmrlrdhs sersevlkhh tdmssssyla athhpphspl vrqlstssds papassssqv
      421 tastsqqpvr rrrgessfdi nnivipmsva attrveklqy keiltpswre vdlqslkgsp
      481 deeneeiedl sdaafaalha kceemerarw lwttsvppqr rgsrsyrssd grttpqlgsa
      541 npstpqpasp dvssshslse yshgqsprsp ispelhsapl tpvardtprh lasedtrcst
      601 pelgldeqsv qpwerrtfpl ahspqaeced qldaqeraar ctrrtsgskt greteaapts
      661 ppivplksrh lvaaataqrp thr
//
LOCUS       NP_001428260            1655 aa            linear   PRI 21-NOV-2025
DEFINITION  BCL-6 corepressor-like protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001428260 XP_047298301 XP_054183528
VERSION     NP_001428260.1
DBSOURCE    REFSEQ: accession NM_001441331.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1655)
  AUTHORS   Luo,C., Chen,Z., Meng,L., Tan,C., He,W., Tu,C., Du,J., Lu,G.X.,
            Lin,G., Tan,Y.Q. and Hu,T.Y.
  TITLE     A hemizygous loss-of-function variant in BCORL1 is associated with
            male infertility and oligoasthenoteratozoospermia
  JOURNAL   Clin Genet 106 (1), 27-36 (2024)
   PUBMED   38342987
  REMARK    GeneRIF: A hemizygous loss-of-function variant in BCORL1 is
            associated with male infertility and oligoasthenoteratozoospermia.
REFERENCE   2  (residues 1 to 1655)
  AUTHORS   Kommoss,F.K.F., Chiang,S., Kobel,M., Koelsche,C., Chang,K.T.,
            Irving,J.A., Dickson,B., Thiryayi,S., Rouzbahman,M., Rasty,G., von
            Deimling,A., Lee,C.H. and Turashvili,G.
  TITLE     Endometrial Stromal Sarcomas With BCOR Internal Tandem Duplication
            and Variant BCOR/BCORL1 Rearrangements Resemble High-grade
            Endometrial Stromal Sarcomas With Recurrent CDK4 Pathway
            Alterations and MDM2 Amplifications
  JOURNAL   Am J Surg Pathol 46 (8), 1142-1152 (2022)
   PUBMED   35499168
  REMARK    GeneRIF: Endometrial Stromal Sarcomas With BCOR Internal Tandem
            Duplication and Variant BCOR/BCORL1 Rearrangements Resemble
            High-grade Endometrial Stromal Sarcomas With Recurrent CDK4 Pathway
            Alterations and MDM2 Amplifications.
REFERENCE   3  (residues 1 to 1655)
  AUTHORS   Schaefer,E.J., Wang,H.C., Karp,H.Q., Meyer,C.A., Cejas,P.,
            Gearhart,M.D., Adelman,E.R., Fares,I., Apffel,A., Lim,K., Xie,Y.,
            Gibson,C.J., Schenone,M., Murdock,H.M., Wang,E.S., Gondek,L.P.,
            Carroll,M.P., Vedula,R.S., Winer,E.S., Garcia,J.S., Stone,R.M.,
            Luskin,M.R., Carr,S.A., Long,H.W., Bardwell,V.J., Figueroa,M.E. and
            Lindsley,R.C.
  TITLE     BCOR and BCORL1 Mutations Drive Epigenetic Reprogramming and
            Oncogenic Signaling by Unlinking PRC1.1 from Target Genes
  JOURNAL   Blood Cancer Discov 3 (2), 116-135 (2022)
   PUBMED   35015684
  REMARK    GeneRIF: BCOR and BCORL1 Mutations Drive Epigenetic Reprogramming
            and Oncogenic Signaling by Unlinking PRC1.1 from Target Genes.
REFERENCE   4  (residues 1 to 1655)
  AUTHORS   Gafner,M., Michelson,M., Argilli,E., Yosovich,K., Sherr,E.H.,
            Parks,K.C., England,E.M., Hady-Cohen,R., Leibovitz,Z., Lev,D.,
            Michaeli-Yosef,Y., Lerman-Sagie,T. and Blumkin,L.
  TITLE     Major brain malformations: corpus callosum dysgenesis, agenesis of
            septum pellucidum and polymicrogyria in patients with
            BCORL1-related disorders
  JOURNAL   J Hum Genet 67 (2), 95-101 (2022)
   PUBMED   34400773
  REMARK    GeneRIF: Major brain malformations: corpus callosum dysgenesis,
            agenesis of septum pellucidum and polymicrogyria in patients with
            BCORL1-related disorders.
REFERENCE   5  (residues 1 to 1655)
  AUTHORS   Junco,S.E., Wang,R., Gaipa,J.C., Taylor,A.B., Schirf,V.,
            Gearhart,M.D., Bardwell,V.J., Demeler,B., Hart,P.J. and Kim,C.A.
  TITLE     Structure of the polycomb group protein PCGF1 in complex with BCOR
            reveals basis for binding selectivity of PCGF homologs
  JOURNAL   Structure 21 (4), 665-671 (2013)
   PUBMED   23523425
REFERENCE   6  (residues 1 to 1655)
  AUTHORS   Shaffer,J.R., Feingold,E., Wang,X., Lee,M., Tcuenco,K., Weeks,D.E.,
            Weyant,R.J., Crout,R., McNeil,D.W. and Marazita,M.L.
  TITLE     GWAS of dental caries patterns in the permanent dentition
  JOURNAL   J Dent Res 92 (1), 38-44 (2013)
   PUBMED   23064961
REFERENCE   7  (residues 1 to 1655)
  AUTHORS   Gao,Z., Zhang,J., Bonasio,R., Strino,F., Sawai,A., Parisi,F.,
            Kluger,Y. and Reinberg,D.
  TITLE     PCGF homologs, CBX proteins, and RYBP define functionally distinct
            PRC1 family complexes
  JOURNAL   Mol Cell 45 (3), 344-356 (2012)
   PUBMED   22325352
REFERENCE   8  (residues 1 to 1655)
  AUTHORS   Li,M., Collins,R., Jiao,Y., Ouillette,P., Bixby,D., Erba,H.,
            Vogelstein,B., Kinzler,K.W., Papadopoulos,N. and Malek,S.N.
  TITLE     Somatic mutations in the transcriptional corepressor gene BCORL1 in
            adult acute myelogenous leukemia
  JOURNAL   Blood 118 (22), 5914-5917 (2011)
   PUBMED   21989985
  REMARK    GeneRIF: BCORL1 by genetic criteria is a novel candidate tumor
            suppressor gene, joining the growing list of genes recurrently
            mutated in acute myelogenous leukemia.
REFERENCE   9  (residues 1 to 1655)
  AUTHORS   Pagan,J.K., Arnold,J., Hanchard,K.J., Kumar,R., Bruno,T.,
            Jones,M.J., Richard,D.J., Forrest,A., Spurdle,A., Verdin,E.,
            Crossley,M., Fanciulli,M., Chenevix-Trench,G., Young,D.B. and
            Khanna,K.K.
  TITLE     A novel corepressor, BCoR-L1, represses transcription through an
            interaction with CtBP
  JOURNAL   J Biol Chem 282 (20), 15248-15257 (2007)
   PUBMED   17379597
REFERENCE   10 (residues 1 to 1655)
  AUTHORS   Lose,F., Arnold,J., Young,D.B., Brown,C.J., Mann,G.J., Pupo,G.M.,
            Khanna,K.K., Chenevix-Trench,G. and Spurdle,A.B.
  CONSRTM   Kathleen Cuningham Foundation Consortium for Research into Familial
            Breast Cancer
  TITLE     BCoR-L1 variation and breast cancer
  JOURNAL   Breast Cancer Res 9 (4), R54 (2007)
   PUBMED   17697391
  REMARK    GeneRIF: Dysregulated BCoR-L1 expression is associated with breast
            cancer
            Erratum:[Breast Cancer Res. 2008;10(5):406]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL034405.16, Z82208.1,
            KF459400.1 and AL136450.8.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_047298301.1, XP_054183528.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            corepressor that is found tethered to promoter regions by
            DNA-binding proteins. The encoded protein can interact with several
            different class II histone deacetylases to repress transcription.
            Two transcript variants encoding different isoforms have been found
            for this gene. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.611731.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1655
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.1"
     Protein         1..1655
                     /product="BCL-6 corepressor-like protein 1 isoform 2"
                     /note="BCoR-like protein 1"
                     /calculated_mol_wt=174863
     Region          65..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          113..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          <198..636
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          343..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          527..550
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          562..646
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          753..781
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          876..901
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          937..977
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1029
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1033
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          <1364..>1473
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1366..1397
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1367,1371..1372,1375..1377,1379..1380,1384,1387,
                     1397,1399,1401,1405..1406,1409..1411,1413..1414,1418,1421,
                     1430,1432,1434,1438..1439,1442..1444,1446..1447,1451,1454)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1399..1430
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1432..1461
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1536..1649
                     /region_name="PUFD_like_1"
                     /note="PCGF Ub-like fold discriminator of BCOR-like 1;
                     cd14260"
                     /db_xref="CDD:271223"
     Site            order(1538,1540..1550,1552,1554,1563..1565,1567,
                     1608..1609,1611,1614,1636,1647,1649)
                     /site_type="other"
                     /note="RAWUL domain interface [polypeptide binding]"
                     /db_xref="CDD:271223"
     CDS             1..1655
                     /gene="BCORL1"
                     /gene_synonym="BCoR-L1; CXorf10; SHUVER"
                     /coded_by="NM_001441331.1:296..5263"
                     /note="isoform 2 is encoded by transcript variant 9"
                     /db_xref="GeneID:63035"
                     /db_xref="HGNC:HGNC:25657"
                     /db_xref="MIM:300688"
ORIGIN      
        1 mistaplysg vhnwtssdri rmcgineerr aplsdeestt gdcqhfgsqe fcvsssfskv
       61 eltavgsgsn argadpdgsa teklghksed kpddpqpkmd yagnvaeaeg llvplsspgd
      121 glklpasdsa easnsradcs wtplntqmsk qvdcspagvk aldsrqgvge kntfilatlg
      181 tgvpvegtlp lvttnfsplp apicppapgs asvphsvpda fqvplsvpap vphsglvpvq
      241 vatsvpapsp plapvpalap appsvptlis dsnplsvsas vlvpvpasap psgpvplsap
      301 apaplsvpvs applaliqap vppsaptlvl apvptpvlap mpastppaap appsvpmptp
      361 tpssgppstp tlipafaptp vpaptpapif tpaptpmpaa tpaaiptsap ipasfslsrv
      421 cfpaaqapam qkvplsfqpg tvltpsqplv yipppscgqp lsvatlpttl gvsstltlpv
      481 lpsylqdrcl pgvlaspelr sypyafsvar pltsdsklvs levnrlpcts psgstttqpa
      541 pdgvpgplad tslvtasakv lptpqpllpa psgssapphp akmpsgteqq tegtsvtfsp
      601 lksppqlere masppecsem pldlssksnr qklplpnqrk tppmpvltpv htsskallst
      661 vlsrsqrttq aaggnvtscl gstsspfvif peivrngdps twvknstali stipgtyvgv
      721 anpvpaslll nkdpnlglnr dprhlpkqep isiidqgepk gtgatcgkkg sqagaegqps
      781 tvkrytpari apglpgcqtk elslwkptgp aniyprcsvn gkptstqvlp vgwspyhqas
      841 llsigissag qltpsqgapi rptsvvsefs gvpslsssea vhglpegqpr pggsfvpeqd
      901 pvtknktcri aakpyeeqvn pvlltlspqt gtlalsvqps ggdirmnqgp eeseshlcsd
      961 stpkmegpqg acglklagdt kpknqvlaty mshelvlatp qnlpkmpelp llphdshpke
     1021 lildvvpssr rgssterpql gsqvdlgrvk mekvdgdvvf nlatcfradg lpvapqrgqa
     1081 evrakagqar vkqesvgvfa cknkwqpddv teslppkkmk cgkekdseeq qlqpqakavv
     1141 rsshrpkcrk lpsdpqestk ksprgasdsg kehngvrgkh khrkptkpes qspgkradsh
     1201 eegslekkak ssfrdfipvv lstrtrsqsd lkarkqktss sqslehrlrn rnlllpnkvq
     1261 gisdspngfl pnnleepacl ensekpsgkr kcktkhmatv seeakgkgrw sqqktrspks
     1321 ptpvkptepc tpsksrsass eeasesptar qippearrli vnknagetll qraarlgykd
     1381 vvlyclqkds edvnhrdnag ytalheacsr gwtdilnill ehganvncsa qdgtrpvhda
     1441 vvndnletiw lllsygadpt latysgqtam klassdtmkr flsdhlsdlq graegdpgvs
     1501 wdfysssvle ekdgfacdll hnppgssdqe gddpmeeddf mfelsdkpll pcynlqvsvs
     1561 rgpcnwflfs dvlkrlklss rifqarfphf eittmpkaef yrqvassqll tpaerpggld
     1621 drsppgsset velvryepdl lrllgsevef qscns
//
LOCUS       NP_001389614            1329 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform d [Homo sapiens].
ACCESSION   NP_001389614 XP_006720202
VERSION     NP_001389614.1
DBSOURCE    REFSEQ: accession NM_001402685.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1329)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1329)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1329)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1329)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1329)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1329)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1329)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1329)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1329)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1329)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            On Apr 22, 2022 this sequence version replaced XP_006720202.1.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2659656.1,
                                           SRR14038192.1977387.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1329
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1329
                     /product="kinectin isoform d"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=152857
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          316..>532
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          448..1269
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1329
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402685.1:179..4168"
                     /note="isoform d is encoded by transcript variant 10"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqdlkqeika
      841 lkeeignvql ekaqqlsits kvqelqnllk gkeeqmntmk avleekekdl antgkwlqdl
      901 qeeneslkah vqevaqhnlk eassasqfee leivlkeken elkrleamlk eresdlsskt
      961 qllqdvqden klfksqieql kqqnyqqass fppheellkv iserekeisg lwneldslkd
     1021 avehqrkknn dlreknweam ealastekml qdkvnktske rqqqveavel eakevlkklf
     1081 pkvsvpsnls ygewlhgfek kakecmagts gseevkvleh klkeademht llqlecekyk
     1141 svlaetegil qklqrsveqe enkwkvkvde shktikqmqs sftsseqele rlrsenkdie
     1201 nlrrerehle melekaemer styvtevrel kaqlnetltk lrteqnerqk vagdlhkaqq
     1261 sleliqskiv kaagdttvie nsdvspetes seketmsvsl nqtvtqlqql lqavnqqltk
     1321 ekehyqvle
//
LOCUS       NP_001428162             248 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 16 [Homo sapiens].
ACCESSION   NP_001428162
VERSION     NP_001428162.1
DBSOURCE    REFSEQ: accession NM_001441233.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 248)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.567313.1,
                                           SRR14038195.1879221.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..248
                     /product="calcium uptake protein 1, mitochondrial isoform
                     16"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=28262
     Region          1..213
                     /region_name="EFh_MICU"
                     /note="EF-hand, calcium binding motif, found in
                     mitochondrial calcium uptake proteins MICU1, MICU2, MICU3,
                     and similar proteins; cl28896"
                     /db_xref="CDD:333716"
     Site            order(3,5,7,14,193,195,197,204)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320081"
     Region          49..79
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          147..176
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          184..213
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     CDS             1..248
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001441233.1:641..1387"
                     /note="isoform 16 is encoded by transcript variant 20"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mfdlngdgev dmeefeqvqs iirsqtsmgm rhrdrpttgn tlksglcsal ttyffgadlk
       61 gkltiknfle fqrklqhdvl kleferhdpv dgriterqfg gmllaysgvq skkltamqrq
      121 lkkhfkegkg ltfqevenff tflknindvd talsfyhmag asldkvtmqq vartvakvel
      181 sdhvcdvvfa lfdcdgngel snkefvsimk qrlmrglekp kdmgftrlmq amwkcaqeta
      241 wdfalpkq
//
LOCUS       NP_001427927             719 aa            linear   PRI 21-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 6 isoform 7 [Homo sapiens].
ACCESSION   NP_001427927
VERSION     NP_001427927.1
DBSOURCE    REFSEQ: accession NM_001440998.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 719)
  AUTHORS   Zheng,T., Zhou,H., Zheng,Z., Guo,Y., Liu,J., Zhang,J. and Li,S.
  TITLE     The pathological significance and potential mechanism of ARHGEF6 in
            lung adenocarcinoma
  JOURNAL   Comput Biol Med 158, 106894 (2023)
   PUBMED   37058762
  REMARK    GeneRIF: The pathological significance and potential mechanism of
            ARHGEF6 in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 719)
  AUTHORS   Li,K., Wang,H., Yang,C., Li,C., Xue,B. and Zhou,J.
  TITLE     Clinical implication and potential function of ARHGEF6 in acute
            myeloid leukemia: An in vitro study
  JOURNAL   PLoS One 18 (4), e0283934 (2023)
   PUBMED   37027440
  REMARK    GeneRIF: Clinical implication and potential function of ARHGEF6 in
            acute myeloid leukemia: An in vitro study.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 719)
  AUTHORS   Klambt,V., Buerger,F., Wang,C., Naert,T., Richter,K., Nauth,T.,
            Weiss,A.C., Sieckmann,T., Lai,E., Connaughton,D.M., Seltzsam,S.,
            Mann,N., Majmundar,A.J., Wu,C.W., Onuchic-Whitford,A.C., Shril,S.,
            Schneider,S., Schierbaum,L., Dai,R., Bekheirnia,M.R., Joosten,M.,
            Shlomovitz,O., Vivante,A., Banne,E., Mane,S., Lifton,R.P.,
            Kirschner,K.M., Kispert,A., Rosenberger,G., Fischer,K.D.,
            Lienkamp,S.S., Zegers,M.M.P. and Hildebrandt,F.
  TITLE     Genetic Variants in ARHGEF6 Cause Congenital Anomalies of the
            Kidneys and Urinary Tract in Humans, Mice, and Frogs
  JOURNAL   J Am Soc Nephrol 34 (2), 273-290 (2023)
   PUBMED   36414417
  REMARK    GeneRIF: Genetic Variants in ARHGEF6 Cause Congenital Anomalies of
            the Kidneys and Urinary Tract in Humans, Mice, and Frogs.
REFERENCE   5  (residues 1 to 719)
  AUTHORS   Wang,N., Li,Y., Zhou,X., Wang,X. and Yang,G.
  TITLE     Comprehensive analysis identifies ARHGEF6 as a potential prognostic
            and immunological biomarker in lung adenocarcinoma
  JOURNAL   Comput Biol Med 153, 106448 (2023)
   PUBMED   36586227
  REMARK    GeneRIF: Comprehensive analysis identifies ARHGEF6 as a potential
            prognostic and immunological biomarker in lung adenocarcinoma.
REFERENCE   6  (residues 1 to 719)
  AUTHORS   Yoshii,S., Tanaka,M., Otsuki,Y., Wang,D.Y., Guo,R.J., Zhu,Y.,
            Takeda,R., Hanai,H., Kaneko,E. and Sugimura,H.
  TITLE     alphaPIX nucleotide exchange factor is activated by interaction
            with phosphatidylinositol 3-kinase
  JOURNAL   Oncogene 18 (41), 5680-5690 (1999)
   PUBMED   10523848
REFERENCE   7  (residues 1 to 719)
  AUTHORS   Yntema,H.G., Hamel,B.C., Smits,A.P., van Roosmalen,T., van den
            Helm,B., Kremer,H., Ropers,H.H., Smeets,D.F. and van Bokhoven,H.
  TITLE     Localisation of a gene for non-specific X linked mental retardation
            (MRX46) to Xq25-q26
  JOURNAL   J Med Genet 35 (10), 801-805 (1998)
   PUBMED   9783701
REFERENCE   8  (residues 1 to 719)
  AUTHORS   Ebinu,J.O., Bottorff,D.A., Chan,E.Y., Stang,S.L., Dunn,R.J. and
            Stone,J.C.
  TITLE     RasGRP, a Ras guanyl nucleotide- releasing protein with calcium-
            and diacylglycerol-binding motifs
  JOURNAL   Science 280 (5366), 1082-1086 (1998)
   PUBMED   9582122
REFERENCE   9  (residues 1 to 719)
  AUTHORS   Manser,E., Loo,T.H., Koh,C.G., Zhao,Z.S., Chen,X.Q., Tan,L.,
            Tan,I., Leung,T. and Lim,L.
  TITLE     PAK kinases are directly coupled to the PIX family of nucleotide
            exchange factors
  JOURNAL   Mol Cell 1 (2), 183-192 (1998)
   PUBMED   9659915
REFERENCE   10 (residues 1 to 719)
  AUTHORS   Nomura,N., Nagase,T., Miyajima,N., Sazuka,T., Tanaka,A., Sato,S.,
            Seki,N., Kawarabayasi,Y., Ishikawa,K. and Tabata,S.
  TITLE     Prediction of the coding sequences of unidentified human genes. II.
            The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
            analysis of cDNA clones from human cell line KG-1 (supplement)
  JOURNAL   DNA Res 1 (5), 251-262 (1994)
   PUBMED   7584048
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL683813.10 and AL135783.6.
            
            Summary: Rho GTPases play a fundamental role in numerous cellular
            processes that are initiated by extracellular stimuli that work
            through G protein coupled receptors. The encoded protein belongs to
            a family of cytoplasmic proteins that activate the Ras-like family
            of Rho proteins by exchanging bound GDP for GTP. It may form a
            complex with G proteins and stimulate Rho-dependent signals. This
            protein is activated by PI3-kinase. Mutations in this gene can
            cause X-chromosomal non-specific cognitive disability. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2307863.1,
                                           SRR14038194.1091962.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.3"
     Protein         1..719
                     /product="rho guanine nucleotide exchange factor 6 isoform
                     7"
                     /note="Rac/Cdc42 guanine exchange factor (GEF) 6; rho
                     guanine nucleotide exchange factor 6; PAK-interacting
                     exchange factor, alpha; Rac/Cdc42 guanine nucleotide
                     exchange factor (GEF) 6"
                     /calculated_mol_wt=81021
     Region          <21..60
                     /region_name="CH_SF"
                     /note="calponin homology (CH) domain superfamily; cl00030"
                     /db_xref="CDD:469584"
     Region          58..103
                     /region_name="RhoGEF67_u1"
                     /note="Unstructured region one on RhoGEF 6 and 7;
                     pfam16615"
                     /db_xref="CDD:465201"
     Region          105..162
                     /region_name="SH3_alphaPIX"
                     /note="Src Homology 3 domain of alpha-Pak Interactive
                     eXchange factor; cd12060"
                     /db_xref="CDD:212993"
     Site            order(112,114,117,120..121,136,138..140,151,153,155..156)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212993"
     Region          185..362
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(191,195,289,313..314,317..318,320..321,324..325,
                     328..329,332,358,362)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          393..490
                     /region_name="PH_Cool_Pix"
                     /note="Cloned out of library/PAK-interactive exchange
                     factor pleckstrin homology (PH) domain; cd01225"
                     /db_xref="CDD:269932"
     Region          519..617
                     /region_name="RhoGEF67_u2"
                     /note="Unstructured region two on RhoGEF 6 and 7;
                     pfam16614"
                     /db_xref="CDD:465200"
     Region          628..712
                     /region_name="betaPIX_CC"
                     /note="betaPIX coiled coil; pfam16523"
                     /db_xref="CDD:465158"
     CDS             1..719
                     /gene="ARHGEF6"
                     /gene_synonym="alpha-PIX; alphaPIX; Cool-2; COOL2; MRX46;
                     PIXA"
                     /coded_by="NM_001440998.1:605..2764"
                     /note="isoform 7 is encoded by transcript variant 8"
                     /db_xref="GeneID:9459"
                     /db_xref="HGNC:HGNC:685"
                     /db_xref="MIM:300267"
ORIGIN      
        1 mkspaceagl ntnlyvlhee vsskreifdp ddlysgvnfs kvlstllavn katedqlser
       61 pcgrssslsa antsqtnpqg avsstvsglq rqsktvemte ngshqlivka rfnfkqtned
      121 elsvckgdii yvtrveeggw wegtlngrtg wfpsnyvrei ksserplspk avkgfetapl
      181 tknyytvvlq nildtekeya kelqsllvty lrplqsnnnl stvevtsllg nfeevctfqq
      241 tlcqaleecs kfpenqhkvg gcllslmphf ksmylaycan hpsavnvltq hsdeleqfme
      301 nqgasspgil ilttnlskpf mrlekyvtll qelerhmedt hpdhqdilka ivafktlmgq
      361 cqdlrkrkql elqilsepiq awegediknl gnvifmsqvm vqygaceeke erylmlfsnv
      421 limlsasprm sgfiyqgkip iagtvvtrld eiegndctfe itgntveriv vhcnnnqdfq
      481 ewleqlnrli rgpascssls ktsssscsah ssfsstgqpr gpleppqiik pwslsclrpa
      541 pplrpsaalg ykermsyilk esskspktmk kflhkrkter kpseeeyvir kstaaleeda
      601 qilkvieayc tsanfqqghg sstrkdsipq vllpeeekli ieetrsngqt imeekslvdt
      661 vyalkdevre lkqenkrmkq cleeelksrr dleklvrrll kqtdecirge sssktsilp
//
LOCUS       NP_001425203             320 aa            linear   PRI 21-NOV-2025
DEFINITION  protein GNAS isoform m [Homo sapiens].
ACCESSION   NP_001425203 XP_016883308
VERSION     NP_001425203.1
DBSOURCE    REFSEQ: accession NM_001438274.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Lin,J., Nie,Q., Cheng,J., Zhong,Y.N., Zhang,T., Zhang,X., Ge,X.,
            Ding,Y., Niu,C., Gao,Y., Wang,K., Gao,M., Wang,X., Chen,W., Yun,C.,
            Ye,C., Xu,J., Shaoyong,W., Zhang,L., Shang,P., Luo,X., Zhang,Z.,
            Zheng,X., Sha,X., Zhang,J., Nie,S., Zhang,X., Ren,F., Liu,H.,
            Dong,E., Yu,X., Ji,L., Pang,Y., Sun,J.P. and Jiang,C.
  TITLE     A microbial amino-acid-conjugated bile acid, tryptophan-cholic
            acid, improves glucose homeostasis via the orphan receptor MRGPRE
  JOURNAL   Cell 188 (17), 4530-4548 (2025)
   PUBMED   40446798
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Crane,J.L., Shamblott,M.J., Axelman,J., Hsu,S., Levine,M.A. and
            Germain-Lee,E.L.
  TITLE     Imprinting status of Galpha(s), NESP55, and XLalphas in cell
            cultures derived from human embryonic germ cells: GNAS imprinting
            in human embryonic germ cells
  JOURNAL   Clin Transl Sci 2 (5), 355-360 (2009)
   PUBMED   20443919
  REMARK    GeneRIF: analysis of the imprinting Status of Galpha(s), NESP55,
            and XLalphas in cell cultures derived from human embryonic germ
            cells
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Bastepe,M.
  TITLE     The GNAS Locus: Quintessential Complex Gene Encoding Gsalpha,
            XLalphas, and other Imprinted Transcripts
  JOURNAL   Curr Genomics 8 (6), 398-414 (2007)
   PUBMED   19412439
  REMARK    GeneRIF: GNAS locus has a highly complex imprinted expression
            pattern, giving rise to transcripts (including non-coding) that are
            maternally, paternally, or biallelically expressed.
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Jakobsen,A.M., Ahlman,H., Kolby,L., Abrahamsson,J.,
            Fischer-Colbrie,R. and Nilsson,O.
  TITLE     NESP55, a novel chromogranin-like peptide, is expressed in
            endocrine tumours of the pancreas and adrenal medulla but not in
            ileal carcinoids
  JOURNAL   Br J Cancer 88 (11), 1746-1754 (2003)
   PUBMED   12771991
  REMARK    GeneRIF: Neuroendocrine secretory protein 55 is found in a subset
            of neuroendocrine tumours showing differentiation towards adrenal
            chromaffin cells and pancreatic islets cells and not in ileal
            carcinoids
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Freson,K., Jaeken,J., Van Helvoirt,M., de Zegher,F.,
            Wittevrongel,C., Thys,C., Hoylaerts,M.F., Vermylen,J. and Van
            Geet,C.
  TITLE     Functional polymorphisms in the paternally expressed XLalphas and
            its cofactor ALEX decrease their mutual interaction and enhance
            receptor-mediated cAMP formation
  JOURNAL   Hum Mol Genet 12 (10), 1121-1130 (2003)
   PUBMED   12719376
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Weiss,U., Ischia,R., Eder,S., Lovisetti-Scamihorn,P., Bauer,R. and
            Fischer-Colbrie,R.
  TITLE     Neuroendocrine secretory protein 55 (NESP55): alternative splicing
            onto transcripts of the GNAS gene and posttranslational processing
            of a maternally expressed protein
  JOURNAL   Neuroendocrinology 71 (3), 177-186 (2000)
   PUBMED   10729789
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Ischia,R., Lovisetti-Scamihorn,P., Hogue-Angeletti,R.,
            Wolkersdorfer,M., Winkler,H. and Fischer-Colbrie,R.
  TITLE     Molecular cloning and characterization of NESP55, a novel
            chromogranin-like precursor of a peptide with 5-HT1B receptor
            antagonist activity
  JOURNAL   J Biol Chem 272 (17), 11657-11662 (1997)
   PUBMED   9111083
REFERENCE   8  (residues 1 to 320)
  AUTHORS   Haldeman-Englert,C.R., Hurst,A.C.E. and Levine,M.A.
  TITLE     Disorders of GNAS Inactivation
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29072892
REFERENCE   9  (residues 1 to 320)
  AUTHORS   Szymczuk,V., Florenzano,P., de Castro,L.F., Collins,M.T. and
            Boyce,A.M.
  TITLE     Fibrous Dysplasia / McCune-Albright Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719192
REFERENCE   10 (residues 1 to 320)
  AUTHORS   Weinstein,L.S., Gejman,P.V., de Mazancourt,P., American,N. and
            Spiegel,A.M.
  TITLE     A heterozygous 4-bp deletion mutation in the Gs alpha gene (GNAS1)
            in a patient with Albright hereditary osteodystrophy
  JOURNAL   Genomics 13 (4), 1319-1321 (1992)
   PUBMED   1505964
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121917.20 and AL109840.24.
            
            On Apr 17, 2025 this sequence version replaced XP_016883308.1.
            
            Summary: This locus has a highly complex imprinted expression
            pattern. It gives rise to maternally, paternally, and biallelically
            expressed transcripts that are derived from four alternative
            promoters and 5' exons. Some transcripts contain a differentially
            methylated region (DMR) at their 5' exons, and this DMR is commonly
            found in imprinted genes and correlates with transcript expression.
            An antisense transcript is produced from an overlapping locus on
            the opposite strand. One of the transcripts produced from this
            locus, and the antisense transcript, are paternally expressed
            noncoding RNAs, and may regulate imprinting in this region. In
            addition, one of the transcripts contains a second overlapping ORF,
            which encodes a structurally unrelated protein - Alex. Alternative
            splicing of downstream exons is also observed, which results in
            different forms of the stimulatory G-protein alpha subunit, a key
            element of the classical signal transduction pathway linking
            receptor-ligand interactions with the activation of adenylyl
            cyclase and a variety of cellular reponses. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            Mutations in this gene result in pseudohypoparathyroidism type 1a,
            pseudohypoparathyroidism type 1b, Albright hereditary
            osteodystrophy, pseudopseudohypoparathyroidism, McCune-Albright
            syndrome, progressive osseus heteroplasia, polyostotic fibrous
            dysplasia of bone, and some pituitary tumors. [provided by RefSeq,
            Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.491860.1,
                                           SRR14038194.700797.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 19412439
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.32"
     Protein         1..320
                     /product="protein GNAS isoform m"
                     /note="secretogranin VI; G protein subunit alpha S;
                     guanine nucleotide binding protein (G protein), alpha
                     stimulating activity polypeptide 1; guanine nucleotide
                     regulatory protein; adenylate cyclase-stimulating G alpha
                     protein; protein ALEX; extra large alphas protein;
                     alternative gene product encoded by XL-exon"
                     /calculated_mol_wt=37382
     Region          1..314
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Site            order(19,23,27,30,33..34,54,57,98,127,152,160,164)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Site            125..133
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            130
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(131,133,135,146,148,152..154,156,159..160,162..165)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(133,158,161..162,165)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            149..152
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            150..166
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Site            218..221
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(283..294,296..299)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Site            291..293
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..320
                     /gene="GNAS"
                     /gene_synonym="AHO; AIMAH1; C20orf45; GNAS1; GPSA; GSA;
                     GSP; NESP; PITA3; POH; SCG6; SgVI"
                     /coded_by="NM_001438274.1:192..1154"
                     /note="isoform m is encoded by transcript variant 18"
                     /db_xref="GeneID:2778"
                     /db_xref="HGNC:HGNC:4392"
                     /db_xref="MIM:139320"
ORIGIN      
        1 mrilhvngfn gdekatkvqd iknnlkeaie tivaamsnlv ppvelanpen qfrvdyilsv
       61 mnvpdfdfpp efyehakalw edegvracye rsneyqlidc aqyfldkidv ikqadyvpsd
      121 qdllrcrvlt sgifetkfqv dkvnfhmfdv ggqrderrkw iqcfndvtai ifvvasssyn
      181 mvirednqtn rlqealnlfk siwnnrwlrt isvilflnkq dllaekvlag kskiedyfpe
      241 faryttpeda tpepgedprv trakyfirde flristasgd grhycyphft cavdtenirr
      301 vfndcrdiiq rmhlrqyell
//
LOCUS       NP_001428147             553 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 5 [Homo sapiens].
ACCESSION   NP_001428147
VERSION     NP_001428147.1
DBSOURCE    REFSEQ: accession NM_001441218.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 553)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 553)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 553)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 553)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 553)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 553)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.225391.1,
                                           SRR1803612.268303.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..553
                     /product="calcium uptake protein 1, mitochondrial isoform
                     5"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=59780
     transit_peptide 1..33
                     /note="Mitochondrion. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:26387864; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
                     /calculated_mol_wt=3784
     Region          68..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          99..110
                     /region_name="Polybasic region.
                     /evidence=ECO:0000269|PubMed:27099988"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCX5; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          126..129
                     /region_name="K/R-ring.
                     /evidence=ECO:0000269|PubMed:32494073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          299..518
                     /region_name="EFh_MICU1"
                     /note="EF-hand, calcium binding motif, found in calcium
                     uptake protein 1, mitochondrial (MICU1) and similar
                     proteins; cd16173"
                     /db_xref="CDD:320081"
     Region          299..328
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Site            order(301,453,456,459..460,462,480)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:320081"
     Site            order(308,310,312,319,498,500,502,509)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320081"
     Region          354..384
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          452..481
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          489..518
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     CDS             1..553
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001441218.1:72..1733"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mfrlnslsal aelavgsrwy hggsqpiqir rrlmmvaflg asavtastgl lwkrahaesp
       61 pcvdnlksdi gdkgknkdeg dvcnhekkta dlaphpeekk kkrsgfrdrk vmeyenrira
      121 ystpdkifry fatlkvisep geaevfmtpe dfvrsitpne kqpehlgldq yiikrfdgka
      181 gvqwhhlssl qpptpwfkrf fclsllsswd yrhtppcpan ffifsrdrvs pcwpgwsryp
      241 dlmirppwlr kvlglqkisq erekfadegs ifytlgecgl isfsdyiflt tvlstpqrnf
      301 eiafkmfdln gdgevdmeef eqvqsiirsq tsmgmrhrdr pttgntlksg lcsalttyff
      361 gadlkgklti knflefqrkl qhdvlklefe rhdpvdgrit erqfggmlla ysgvqskklt
      421 amqrqlkkhf kegkgltfqe venfftflkn indvdtalsf yhmagasldk vtmqqvartv
      481 akvelsdhvc dvvfalfdcd gngelsnkef vsimkqrlmr glekpkdmgf trlmqamwkc
      541 aqetawdfal pkq
//
LOCUS       NP_001393435             758 aa            linear   PRI 21-NOV-2025
DEFINITION  desmocollin-2 isoform 3 [Homo sapiens].
ACCESSION   NP_001393435 XP_005258263
VERSION     NP_001393435.1
DBSOURCE    REFSEQ: accession NM_001406506.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Han,J.Y., Che,N., Mo,J., Zhang,D.F., Liang,X.H., Dong,X.Y.,
            Zhao,X.L. and Sun,B.C.
  TITLE     Desmoglein 2 and desmocollin 2 depletions promote malignancy
            through distinct mechanisms in triple-negative and luminal breast
            cancer
  JOURNAL   BMC Cancer 24 (1), 532 (2024)
   PUBMED   38671389
  REMARK    GeneRIF: Desmoglein 2 and desmocollin 2 depletions promote
            malignancy through distinct mechanisms in triple-negative and
            luminal breast cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 758)
  AUTHORS   Sun,C., Wen,K., Zhang,B., Dong,Y., Chen,C., Neo,S.Y., Leng,B.,
            Gao,T.T. and Wu,J.
  TITLE     DSC2 suppresses the growth of gastric cancer through the inhibition
            of nuclear translocation of gamma-catenin and PTEN/PI3K/AKT
            signaling pathway
  JOURNAL   Aging (Albany NY) 15 (13), 6380-6399 (2023)
   PUBMED   37421607
  REMARK    GeneRIF: DSC2 suppresses the growth of gastric cancer through the
            inhibition of nuclear translocation of gamma-catenin and
            PTEN/PI3K/AKT signaling pathway.
REFERENCE   3  (residues 1 to 758)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   4  (residues 1 to 758)
  AUTHORS   Pariyar,M., Thorne,R.F., Scott,R.J. and Avery-Kiejda,K.A.
  TITLE     Verification and Validation of a Four-Gene Panel as a Prognostic
            Indicator in Triple Negative Breast Cancer
  JOURNAL   Front Oncol 12, 821334 (2022)
   PUBMED   35387118
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 758)
  AUTHORS   Syrris,P., Ward,D., Evans,A., Asimaki,A., Gandjbakhch,E.,
            Sen-Chowdhry,S. and McKenna,W.J.
  TITLE     Arrhythmogenic right ventricular dysplasia/cardiomyopathy
            associated with mutations in the desmosomal gene desmocollin-2
  JOURNAL   Am J Hum Genet 79 (5), 978-984 (2006)
   PUBMED   17033975
REFERENCE   6  (residues 1 to 758)
  AUTHORS   Nuber,U.A., Schafer,S., Schmidt,A., Koch,P.J. and Franke,W.W.
  TITLE     The widespread human desmocollin Dsc2 and tissue-specific patterns
            of synthesis of various desmocollin subtypes
  JOURNAL   Eur J Cell Biol 66 (1), 69-74 (1995)
   PUBMED   7750520
REFERENCE   7  (residues 1 to 758)
  AUTHORS   McNally,E., MacLeod,H. and Dellefave-Castillo,L.
  TITLE     Arrhythmogenic Right Ventricular Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301310
REFERENCE   8  (residues 1 to 758)
  AUTHORS   Arnemann,J., Spurr,N.K., Wheeler,G.N., Parker,A.E. and Buxton,R.S.
  TITLE     Chromosomal assignment of the human genes coding for the major
            proteins of the desmosome junction, desmoglein DGI (DSG),
            desmocollins DGII/III (DSC), desmoplakins DPI/II (DSP), and
            plakoglobin DPIII (JUP)
  JOURNAL   Genomics 10 (3), 640-645 (1991)
   PUBMED   1889810
REFERENCE   9  (residues 1 to 758)
  AUTHORS   Parker,A.E., Wheeler,G.N., Arnemann,J., Pidsley,S.C., Ataliotis,P.,
            Thomas,C.L., Rees,D.A., Magee,A.I. and Buxton,R.S.
  TITLE     Desmosomal glycoproteins II and III. Cadherin-like junctional
            molecules generated by alternative splicing
  JOURNAL   J Biol Chem 266 (16), 10438-10445 (1991)
   PUBMED   2037591
REFERENCE   10 (residues 1 to 758)
  AUTHORS   Garrod,D.R. and Fleming,S.
  TITLE     Early expression of desmosomal components during kidney tubule
            morphogenesis in human and murine embryos
  JOURNAL   Development 108 (2), 313-321 (1990)
   PUBMED   2112455
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012417.13 and KF573685.1.
            
            On May 16, 2022 this sequence version replaced XP_005258263.1.
            
            Summary: This gene encodes a member of the desmocollin protein
            subfamily. Desmocollins, along with desmogleins, are cadherin-like
            transmembrane glycoproteins that are major components of the
            desmosome. Desmosomes are cell-cell junctions that help resist
            shearing forces and are found in high concentrations in cells
            subject to mechanical stress. This gene is found in a cluster with
            other desmocollin family members on chromosome 18. Mutations in
            this gene are associated with arrhythmogenic right ventricular
            dysplasia-11, and reduced protein expression has been described in
            several types of cancer. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853558.11668.1,
                                           SRR14038191.2545911.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..758
                     /product="desmocollin-2 isoform 3"
                     /note="desmosomal glycoprotein II/III; cadherin family
                     member 2"
                     /calculated_mol_wt=83686
     Region          3..91
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Region          104..208
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(111..112,169,171,204,206..207)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          217..320
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Site            order(223..224,281,283,321,323..324)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          334..430
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(339..340,391,393,426,428..429)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          709..753
                     /region_name="CADH_Y-type_LIR"
                     /note="Cadherin, Y-type LIR-motif; pfam01049"
                     /db_xref="CDD:460041"
     CDS             1..758
                     /gene="DSC2"
                     /gene_synonym="ARVD11; CDHF2; DG2; DGII/III; DSC3"
                     /coded_by="NM_001406506.1:401..2677"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92447.1"
                     /db_xref="GeneID:1824"
                     /db_xref="HGNC:HGNC:3036"
                     /db_xref="MIM:125645"
ORIGIN      
        1 mlenslgpfp lflqqvqsdt aqnytiyysi rgpgvdqepr nlfyverdtg nlyctrpvdr
       61 eqyesfeiia fattpdgytp elplpliiki edendnypif teetytftif encrvgttvg
      121 qvcatdkdep dtmhtrlkys iigqvppspt lfsmhpttgv itttssqldr elidkyqlki
      181 kvqdmdgqyf glqttstcii niddvndhlp tftrtsyvts veentvdvei lrvtvedkdl
      241 vntanwrany tilkgnengn fkivtdaktn egvlcvvkpl nyeekqqmil qigvvneapf
      301 sreasprsam statvtvnve dqdegpecnp piqtvrmken aevgttsngy kaydpetrss
      361 sgirykkltd ptgwvtiden tgsikvfrsl dreaetikng iynitvlasd qggrtctgtl
      421 giilqdvndn spfipkktvi ickptmssae ivavdpdepi hgppfdfsle sstsevqrmw
      481 rlkaindtaa rlsyqndppf gsyvvpitvr drlgmssvts ldvtlcdcit endcthrvdp
      541 riggggvqlg kwailaillg iallfcilft lvcgasgtsk qpkvipddla qqnlivsnte
      601 apgddkvysa ngfttqtvga saqgvcgtvg sgiknggqet iemvkgghqt sescrgaghh
      661 htldscrggh tevdncryty sewhsftqpr lgekvylcnq denhkhaqdy vltynyegrg
      721 svagsvgccs erqeedglef ldnlepkfrt laeacmkr
//
LOCUS       NP_001428159             311 aa            linear   PRI 21-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 13 [Homo sapiens].
ACCESSION   NP_001428159
VERSION     NP_001428159.1
DBSOURCE    REFSEQ: accession NM_001441230.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 311)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 311)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 311)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 311)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 311)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513185.12 and AC091769.6.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.262757.1,
                                           SRR1803617.153610.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..311
                     /product="calcium uptake protein 1, mitochondrial isoform
                     13"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=35574
     Region          57..276
                     /region_name="EFh_MICU1"
                     /note="EF-hand, calcium binding motif, found in calcium
                     uptake protein 1, mitochondrial (MICU1) and similar
                     proteins; cd16173"
                     /db_xref="CDD:320081"
     Region          57..86
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Site            order(59,211,214,217..218,220,238)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:320081"
     Site            order(66,68,70,77,256,258,260,267)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320081"
     Region          112..142
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          210..239
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          247..276
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     CDS             1..311
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001441230.1:821..1756"
                     /note="isoform 13 is encoded by transcript variant 17"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mirppwlrkv lglqkisqer ekfadegsif ytlgecglis fsdyiflttv lstpqrnfei
       61 afkmfdlngd gevdmeefeq vqsiirsqts mgmrhrdrpt tgntlksglc salttyffga
      121 dlkgkltikn flefqrklqh dvlkleferh dpvdgriter qfggmllays gvqskkltam
      181 qrqlkkhfke gkgltfqeve nfftflknin dvdtalsfyh magasldkvt mqqvartvak
      241 velsdhvcdv vfalfdcdgn gelsnkefvs imkqrlmrgl ekpkdmgftr lmqamwkcaq
      301 etawdfalpk q
//
LOCUS       NP_001427731            1202 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphorylase b kinase regulatory subunit alpha, liver isoform
            isoform 4 [Homo sapiens].
ACCESSION   NP_001427731 XP_047298119 XP_054183179
VERSION     NP_001427731.1
DBSOURCE    REFSEQ: accession NM_001440802.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1202)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1202)
  AUTHORS   Dong,R., Wei,X., Zhang,K., Song,F., Lv,Y., Gao,M., Wang,D., Ma,J.,
            Gai,Z. and Liu,Y.
  TITLE     Genotypic and phenotypic characteristics of 12 chinese children
            with glycogen storage diseases
  JOURNAL   Front Genet 13, 932760 (2022)
   PUBMED   36105079
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1202)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1202)
  AUTHORS   Benner,A., Alhaidan,Y., Lines,M.A., Brusgaard,K., De Leon,D.D.,
            Sparkes,R., Frederiksen,A.L. and Christesen,H.T.
  TITLE     PHKA2 variants expand the phenotype of phosphorylase B kinase
            deficiency to include patients with ketotic hypoglycemia only
  JOURNAL   Am J Med Genet A 185 (10), 2959-2975 (2021)
   PUBMED   34117828
  REMARK    GeneRIF: PHKA2 variants expand the phenotype of phosphorylase B
            kinase deficiency to include patients with ketotic hypoglycemia
            only.
REFERENCE   5  (residues 1 to 1202)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1202)
  AUTHORS   Herbert,M., Goldstein,J.L., Rehder,C., Austin,S., Kishnani,P.S. and
            Bali,D.S.
  TITLE     Phosphorylase Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21634085
REFERENCE   7  (residues 1 to 1202)
  AUTHORS   Davidson,J.J., Ozcelik,T., Hamacher,C., Willems,P.J., Francke,U.
            and Kilimann,M.W.
  TITLE     cDNA cloning of a liver isoform of the phosphorylase kinase alpha
            subunit and mapping of the gene to Xp22.2-p22.1, the region of
            human X-linked liver glycogenosis
  JOURNAL   Proc Natl Acad Sci U S A 89 (6), 2096-2100 (1992)
   PUBMED   1372435
REFERENCE   8  (residues 1 to 1202)
  AUTHORS   Wauters,J.G., Bossuyt,P.J., Davidson,J., Hendrickx,J.,
            Kilimann,M.W. and Willems,P.J.
  TITLE     Regional mapping of a liver alpha-subunit gene of phosphorylase
            kinase (PHKA) to the distal region of human chromosome Xp
  JOURNAL   Cytogenet Cell Genet 60 (3-4), 194-196 (1992)
   PUBMED   1505214
REFERENCE   9  (residues 1 to 1202)
  AUTHORS   Willems,P.
  TITLE     Families with X-linked liver glycogenosis due to phosphorylase
            kinase deficiency
  JOURNAL   Clin Genet 38 (1), 80 (1990)
   PUBMED   2387090
REFERENCE   10 (residues 1 to 1202)
  AUTHORS   Willems,P.J., Gerver,W.J., Berger,R. and Fernandes,J.
  TITLE     The natural history of liver glycogenosis due to phosphorylase
            kinase deficiency: a longitudinal study of 41 patients
  JOURNAL   Eur J Pediatr 149 (4), 268-271 (1990)
   PUBMED   2303074
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL732509.4 and AL096700.14.
            
            On or before May 30, 2025 this sequence version replaced
            XP_047298119.1, XP_054183179.1.
            
            Summary: Phosphorylase kinase is a polymer of 16 subunits, four
            each of alpha, beta, gamma and delta. The alpha subunit includes
            the skeletal muscle and hepatic isoforms, and the hepatic isoform
            is encoded by this gene. The beta subunit is the same in both the
            muscle and hepatic isoforms, and encoded by one gene. The gamma
            subunit also includes the skeletal muscle and hepatic isoforms,
            which are encoded by two different genes. The delta subunit is a
            calmodulin and can be encoded by three different genes. The gamma
            subunits contain the active site of the enzyme, whereas the alpha
            and beta subunits have regulatory functions controlled by
            phosphorylation. The delta subunit mediates the dependence of the
            enzyme on calcium concentration. Mutations in this gene cause
            glycogen storage disease type 9A, also known as X-linked liver
            glycogenosis. Alternatively spliced transcript variants have been
            reported, but the full-length nature of these variants has not been
            determined.[provided by RefSeq, Feb 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1365486.1,
                                           SRR14038191.2530576.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1202
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.13"
     Protein         1..1202
                     /product="phosphorylase b kinase regulatory subunit alpha,
                     liver isoform isoform 4"
                     /EC_number="2.7.11.19"
                     /note="phosphorylase kinase alpha L subunit; phosphorylase
                     kinase alpha-subunit"
                     /calculated_mol_wt=134726
     Region          8..>406
                     /region_name="Glyco_hydro_15"
                     /note="Glycosyl hydrolases family 15; pfam00723"
                     /db_xref="CDD:395586"
     Region          <769..886
                     /region_name="Bac_rhamnosid6H"
                     /note="Bacterial alpha-L-rhamnosidase 6 hairpin
                     glycosidase domain; cl46875"
                     /db_xref="CDD:481215"
     Region          897..>1114
                     /region_name="KPBB_C"
                     /note="Phosphorylase b kinase C-terminal domain;
                     pfam19292"
                     /db_xref="CDD:437124"
     CDS             1..1202
                     /gene="PHKA2"
                     /gene_synonym="GSD9A; PHK; PYK; PYKL; XLG; XLG2"
                     /coded_by="NM_001440802.1:183..3791"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:5256"
                     /db_xref="HGNC:HGNC:8926"
                     /db_xref="MIM:300798"
ORIGIN      
        1 mrsrsnsgvr ldgyarlvqq tilcyqnpvt gllsasheqk dawvrdniys ilavwglgma
       61 yrknadrded kakayeleqn vvklmrgllq cmmrqvakve kfkhtqstkd slhakyntat
      121 cgtvvgddqw ghlqvdatsl fllflaqmta sglriiftld evafiqnlvf yieaaykvad
      181 ygmwergdkt nqgipelnas svgmaksilf smlprastsk eidagllsii sfpafavedv
      241 nlvnvtknei isklqgrygc crflrdgykt predpnrlhy dpaelklfen iecewpvfwt
      301 yfiidgvfsg davqvqeyre alegilirgk ngirlvpely avppnkvdee yknphtvdrv
      361 pmgkvphlwg qslyilssll aegflaagei dplnrrfsts vkpdvvvqvt vlaennhikd
      421 llrkhgvnvq siadihpiqv qpgrilshiy aklgrnknmn lsgrpyrhig vlgtsklyvi
      481 rnqiftftpq ftdqhhfyla ldnemiveml rielaylctc wrmtgrptlt fpisrtmltn
      541 dgsdihsavl stirkledgy fggarvklgn lseflttsfy tyltfldpdc deklfdnase
      601 gtfspdsdsd lvgyledtcn qesqdeldhy inhllqstsl rsylpplckn tedrhvfsai
      661 hstrdilsvm akakglevpf vpmtlptkvl sahrkslnlv dspqpllekv pesdfqwprd
      721 dhgdvdcekl veqlkdcsnl qdqadilyil yvikgpswdt nlsgqhgvtv qnllgelygk
      781 aglnqewgli ryisgllrkk vevlaeactd llshqkqltv glppepreki isaplppeel
      841 tkliyeasgq disiavltqe ivvylamyvr aqpslfveml rlrigliiqv matelarsln
      901 csgeeasesl mnlspfdmkn llhhilsgke fgversvrpi hsstssptis ihevghtgvt
      961 ktersginrl rsemkqmtrr fsadeqffsv gqaasssahs sksarsstps sptgtsssds
     1021 gghhigwger qgqwlrrrrl dgainrvpvg fyqrvwkilq kchglsidgy vlpssttrem
     1081 tpheikfavh vesvlnrvpq peyrqllvea imvltllsdt emtsiggiih vdqivqmasq
     1141 lflqdqvsig amdtlekdqa tgichffyds apsgaygtmt yltravasyl qellpnsgcq
     1201 mq
//
LOCUS       NP_001401153             185 aa            linear   PRI 21-NOV-2025
DEFINITION  natural killer cells antigen CD94 isoform 5 [Homo sapiens].
ACCESSION   NP_001401153 XP_047284781
VERSION     NP_001401153.1
DBSOURCE    REFSEQ: accession NM_001414224.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Verma,K., Croft,W., Pearce,H., Zuo,J., Stephens,C., Nunnick,J.,
            Kinsella,F.A., Malladi,R. and Moss,P.
  TITLE     Early expression of CD94 and loss of CD96 on CD8+ T cells after
            allogeneic stem cell tranplantation is predictive of subsequent
            relapse and survival
  JOURNAL   Haematologica 108 (2), 433-443 (2023)
   PUBMED   35924575
  REMARK    GeneRIF: Early expression of CD94 and loss of CD96 on CD8+ T cells
            after allogeneic stem cell tranplantation is predictive of
            subsequent relapse and survival.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Fang,H., Wang,W., Kadia,T.M., El Hussein,S., Wang,S.A. and
            Khoury,J.D.
  TITLE     CD94 expression patterns in reactive and neoplastic T-cell and
            NK-cell proliferations
  JOURNAL   Leuk Res 108, 106614 (2021)
   PUBMED   33990003
  REMARK    GeneRIF: CD94 expression patterns in reactive and neoplastic T-cell
            and NK-cell proliferations.
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Zhang,Q., Zheng,Y., Ning,M. and Li,T.
  TITLE     KLRD1, FOSL2 and LILRB3 as potential biomarkers for plaques
            progression in acute myocardial infarction and stable coronary
            artery disease
  JOURNAL   BMC Cardiovasc Disord 21 (1), 344 (2021)
   PUBMED   34271875
  REMARK    GeneRIF: KLRD1, FOSL2 and LILRB3 as potential biomarkers for
            plaques progression in acute myocardial infarction and stable
            coronary artery disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Prasnikar,E., Perdih,A. and Borisek,J.
  TITLE     Nonameric Peptide Orchestrates Signal Transduction in the
            Activating HLA-E/NKG2C/CD94 Immune Complex as Revealed by All-Atom
            Simulations
  JOURNAL   Int J Mol Sci 22 (13), 6670 (2021)
   PUBMED   34206395
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 185)
  AUTHORS   Shreeve,N., Depierreux,D., Hawkes,D., Traherne,J.A., Sovio,U.,
            Huhn,O., Jayaraman,J., Horowitz,A., Ghadially,H., Perry,J.R.B.,
            Moffett,A., Sled,J.G., Sharkey,A.M. and Colucci,F.
  TITLE     The CD94/NKG2A inhibitory receptor educates uterine NK cells to
            optimize pregnancy outcomes in humans and mice
  JOURNAL   Immunity 54 (6), 1231-1244 (2021)
   PUBMED   33887202
  REMARK    GeneRIF: The CD94/NKG2A inhibitory receptor educates uterine NK
            cells to optimize pregnancy outcomes in humans and mice.
REFERENCE   6  (residues 1 to 185)
  AUTHORS   Brooks,A.G., Posch,P.E., Scorzelli,C.J., Borrego,F. and
            Coligan,J.E.
  TITLE     NKG2A complexed with CD94 defines a novel inhibitory natural killer
            cell receptor
  JOURNAL   J Exp Med 185 (4), 795-800 (1997)
   PUBMED   9034158
REFERENCE   7  (residues 1 to 185)
  AUTHORS   Lazetic,S., Chang,C., Houchins,J.P., Lanier,L.L. and Phillips,J.H.
  TITLE     Human natural killer cell receptors involved in MHC class I
            recognition are disulfide-linked heterodimers of CD94 and NKG2
            subunits
  JOURNAL   J Immunol 157 (11), 4741-4745 (1996)
   PUBMED   8943374
REFERENCE   8  (residues 1 to 185)
  AUTHORS   Phillips,J.H., Chang,C., Mattson,J., Gumperz,J.E., Parham,P. and
            Lanier,L.L.
  TITLE     CD94 and a novel associated protein (94AP) form a NK cell receptor
            involved in the recognition of HLA-A, HLA-B, and HLA-C allotypes
  JOURNAL   Immunity 5 (2), 163-172 (1996)
   PUBMED   8769479
REFERENCE   9  (residues 1 to 185)
  AUTHORS   Chang,C., Rodriguez,A., Carretero,M., Lopez-Botet,M., Phillips,J.H.
            and Lanier,L.L.
  TITLE     Molecular characterization of human CD94: a type II membrane
            glycoprotein related to the C-type lectin superfamily
  JOURNAL   Eur J Immunol 25 (9), 2433-2437 (1995)
   PUBMED   7589107
REFERENCE   10 (residues 1 to 185)
  AUTHORS   Moretta,A., Vitale,M., Sivori,S., Bottino,C., Morelli,L.,
            Augugliaro,R., Barbaresi,M., Pende,D., Ciccone,E., Lopez-Botet,M.
            and Moretta,L.
  TITLE     Human natural killer cell receptors for HLA-class I molecules.
            Evidence that the Kp43 (CD94) molecule functions as receptor for
            HLA-B alleles
  JOURNAL   J Exp Med 180 (2), 545-555 (1994)
   PUBMED   8046333
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022075.29.
            
            On Nov 16, 2022 this sequence version replaced XP_047284781.1.
            
            Summary: Natural killer (NK) cells are a distinct lineage of
            lymphocytes that mediate cytotoxic activity and secrete cytokines
            upon immune stimulation. Several genes of the C-type lectin
            superfamily, including members of the NKG2 family, are expressed by
            NK cells and may be involved in the regulation of NK cell function.
            KLRD1 (CD94) is an antigen preferentially expressed on NK cells and
            is classified as a type II membrane protein because it has an
            external C terminus. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, May
            2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138524.1178442.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..185
                     /product="natural killer cells antigen CD94 isoform 5"
                     /note="natural killer cells antigen CD94; CD94 antigen;
                     KP43; NK cell receptor; killer cell lectin-like receptor
                     subfamily D, member 1"
                     /calculated_mol_wt=21120
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13241.2)"
     Region          61..173
                     /region_name="CLECT_NK_receptors_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in natural killer cell receptors (NKRs); cd03593"
                     /db_xref="CDD:153063"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13241.2)"
     Site            order(114,141,159,162..163)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153063"
     Site            132
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13241.2)"
     CDS             1..185
                     /gene="KLRD1"
                     /gene_synonym="CD94"
                     /coded_by="NM_001414224.1:209..766"
                     /note="isoform 5 is encoded by transcript variant 10"
                     /db_xref="GeneID:3824"
                     /db_xref="HGNC:HGNC:6378"
                     /db_xref="MIM:602894"
ORIGIN      
        1 mavfkttlwr lisgtlgiic lslmstlgil lknsftklsi epaftpgpni elqkdsdccs
       61 cqekwvgyrc ncyfisseqk twnesrhlca sqkssllqlq ntdeldfmss sqqfywigls
      121 yseehtawlw engsalsqyl fpsfetfntk nciaynpngn aldescedkn ryiyyliwgk
      181 pvims
//
LOCUS       NP_001397747             920 aa            linear   PRI 21-NOV-2025
DEFINITION  MICAL-like protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001397747 XP_011528775
VERSION     NP_001397747.1
DBSOURCE    REFSEQ: accession NM_001410818.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Frisby,D., Murakonda,A.B., Ashraf,B., Dhawan,K., Almeida-Souza,L.,
            Naslavsky,N. and Caplan,S.
  TITLE     Endosomal actin branching, fission, and receptor recycling require
            FCHSD2 recruitment by MICAL-L1
  JOURNAL   Mol Biol Cell 35 (11), ar144 (2024)
   PUBMED   39382837
  REMARK    GeneRIF: Endosomal actin branching, fission, and receptor recycling
            require FCHSD2 recruitment by MICAL-L1.
REFERENCE   3  (residues 1 to 920)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 920)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 920)
  AUTHORS   Sikora,R., Bun,P., Danglot,L., Alqabandi,M., Bassereau,P.,
            Niedergang,F., Galli,T. and Zahraoui,A.
  TITLE     MICAL-L1 is required for cargo protein delivery to the cell surface
  JOURNAL   Biol Open 10 (6) (2021)
   PUBMED   34100897
  REMARK    GeneRIF: MICAL-L1 is required for cargo protein delivery to the
            cell surface.
REFERENCE   6  (residues 1 to 920)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 920)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   8  (residues 1 to 920)
  AUTHORS   Weide,T., Teuber,J., Bayer,M. and Barnekow,A.
  TITLE     MICAL-1 isoforms, novel rab1 interacting proteins
  JOURNAL   Biochem Biophys Res Commun 306 (1), 79-86 (2003)
   PUBMED   12788069
REFERENCE   9  (residues 1 to 920)
  AUTHORS   Terman,J.R., Mao,T., Pasterkamp,R.J., Yu,H.H. and Kolodkin,A.L.
  TITLE     MICALs, a family of conserved flavoprotein oxidoreductases,
            function in plexin-mediated axonal repulsion
  JOURNAL   Cell 109 (7), 887-900 (2002)
   PUBMED   12110185
REFERENCE   10 (residues 1 to 920)
  AUTHORS   Marzesco,A.M., Dunia,I., Pandjaitan,R., Recouvreur,M., Dauzonne,D.,
            Benedetti,E.L., Louvard,D. and Zahraoui,A.
  TITLE     The small GTPase Rab13 regulates assembly of functional tight
            junctions in epithelial cells
  JOURNAL   Mol Biol Cell 13 (6), 1819-1831 (2002)
   PUBMED   12058051
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL022311.5.
            
            On Aug 16, 2022 this sequence version replaced XP_011528775.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR13170464.375968.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..920
                     /product="MICAL-like protein 1 isoform 1"
                     /note="molecule interacting with Rab13; MICAL-like protein
                     1"
                     /calculated_mol_wt=99413
     Region          4..110
                     /region_name="CH_MICALL1"
                     /note="calponin homology (CH) domain found in MICAL-like
                     protein 1; cd21252"
                     /db_xref="CDD:409101"
     Site            order(4,8,58,60..61,64..65,67,76..84,92,94..95,97..98,
                     101..102,105)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409101"
     Region          164..218
                     /region_name="LIM_Mical_like_1"
                     /note="This domain belongs to the LIM domain family which
                     are found on Mical (molecule interacting with CasL) like
                     proteins; cd09444"
                     /db_xref="CDD:188828"
     Site            order(164,167,185,188,191,194,214,217)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188828"
     Region          <253..724
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          744..865
                     /region_name="bMERB_dom"
                     /note="Bivalent Mical/EHBP Rab binding domain; pfam12130"
                     /db_xref="CDD:463467"
     CDS             1..920
                     /gene="MICALL1"
                     /gene_synonym="MICAL-L1; MIRAB13"
                     /coded_by="NM_001410818.1:127..2889"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS93161.1"
                     /db_xref="GeneID:85377"
                     /db_xref="HGNC:HGNC:29804"
                     /db_xref="MIM:619563"
ORIGIN      
        1 magprgalla wcrrqcegyr gveirdlsss frdglafcai lhrhrpdlld fdslskdnvf
       61 ennrlafeva ekelgipall dpndmvsmsv pdclsimtyv sqyynhfcsp gqagvspprk
      121 glapcsppsv aptpvepedv aqgeelssgs lseqgtgqtp sstcaacqqh vhlvqrylad
      181 grlyhrhcfr crrcsstllp gayengpeeg tfvcaehcar lgpgtrsgtr pgpfsqpkqq
      241 hqqqlaedak dvpgggpsss apagaeadgp kaspearpqi ptkprvpgkl qelasppagr
      301 ptpaprkase sttpapptpr prsslqqenl veqagssslv ngrlhelpvp kprgtpkpse
      361 gtpaprkdpp witlvqaepk kkpaplppss spgppsqdsr qvenggteev aqpsptasle
      421 skpynpfeee eedkeeeapa apslatspal ghpestpksl hpwygitpts spktkkrpap
      481 rapsaspldn vfgsiisish eeinwcpavp vpelvaaraa cssplpphcr sgaeegpplf
      541 lwhsqalhas rlshseppsa tpspalsves lssesasqta gaelleppav pksssepavh
      601 apgtpgnpvs lstnsslass gelveprveq mpqaspglap rtrgssgpqp akpcsgatpt
      661 plllvgdrsp vpspgssspq lqvksscken pfnrkpspaa spatkkatkg skpvrppapg
      721 hgfplikrkv qadqyipeed ihgemdtier rldalehrgv lleeklrggl negreddmlv
      781 dwfklihekh llvrreseli yvfkqqnleq rqadveyelr cllnkpekdw teedrarekv
      841 lmqelvtlie qrnaiincld edrqreeeed kmleamikkk efqreaepeg kkkgkfktmk
      901 mlkllgnkrd aksksprdks
//
LOCUS       NP_001427590             754 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 3 isoform 10 [Homo sapiens].
ACCESSION   NP_001427590 XP_005278339 XP_054177066 XP_054185668 XP_054186163
            XP_054186461 XP_054186711 XP_054186941 XP_054187225 XP_054187497
            XP_054189539 XP_054189640
VERSION     NP_001427590.1
DBSOURCE    REFSEQ: accession NM_001440661.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Ghashghaei,M., Liu,Y., Ettles,J., Bombaci,G., Ramkumar,N., Liu,Z.,
            Escano,L., Miko,S.S., Kim,Y., Waldron,J.A., Do,K., MacPherson,K.,
            Yuen,K.A., Taibi,T., Yue,M., Arsalan,A., Jin,Z., Edin,G.,
            Karsan,A., Morin,G.B., Kuchenbauer,F., Perna,F., Bushell,M. and
            Vu,L.P.
  TITLE     Translation efficiency driven by CNOT3 subunit of the CCR4-NOT
            complex promotes leukemogenesis
  JOURNAL   Nat Commun 15 (1), 2340 (2024)
   PUBMED   38491013
  REMARK    GeneRIF: Translation efficiency driven by CNOT3 subunit of the
            CCR4-NOT complex promotes leukemogenesis.
            Erratum:[Nat Commun. 2024 Oct 7;15(1):8674. doi:
            10.1038/s41467-024-53071-1. PMID: 39375334]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Burgess,H.M., Grande,R., Riccio,S., Dinesh,I., Winkler,G.S.,
            Depledge,D.P. and Mohr,I.
  TITLE     CCR4-NOT differentially controls host versus virus poly(a)-tail
            length and regulates HCMV infection
  JOURNAL   EMBO Rep 24 (12), e56327 (2023)
   PUBMED   37846490
  REMARK    GeneRIF: CCR4-NOT differentially controls host versus virus
            poly(a)-tail length and regulates HCMV infection.
REFERENCE   4  (residues 1 to 754)
  AUTHORS   Zhao,P., Meng,Q., Wan,C., Lei,T., Zhang,L., Zhang,X., Tan,L.,
            Zhu,H. and He,X.
  TITLE     Clinical features of CNOT3-associated neurodevelopmental disorder
            in three Chinese patients
  JOURNAL   Neurogenetics 24 (2), 129-136 (2023)
   PUBMED   36802310
  REMARK    GeneRIF: Clinical features of CNOT3-associated neurodevelopmental
            disorder in three Chinese patients.
REFERENCE   5  (residues 1 to 754)
  AUTHORS   McLenachan,S., Zhang,D., Grainok,J., Zhang,X., Huang,Z., Chen,S.C.,
            Zaw,K., Lima,A., Jennings,L., Roshandel,D., Moon,S.Y., Heath
            Jeffery,R.C., Attia,M.S., Thompson,J.A., Lamey,T.M., McLaren,T.L.,
            De Roach,J., Fletcher,S. and Chen,F.K.
  TITLE     Determinants of Disease Penetrance in PRPF31-Associated Retinopathy
  JOURNAL   Genes (Basel) 12 (10), 1542 (2021)
   PUBMED   34680937
  REMARK    GeneRIF: Determinants of Disease Penetrance in PRPF31-Associated
            Retinopathy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 754)
  AUTHORS   Yin,X., Warner,D.R., Roberts,E.A., Pisano,M.M. and Greene,R.M.
  TITLE     Identification of novel CBP interacting proteins in embryonic
            orofacial tissue
  JOURNAL   Biochem Biophys Res Commun 329 (3), 1010-1017 (2005)
   PUBMED   15752756
REFERENCE   7  (residues 1 to 754)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 754)
  AUTHORS   Aoki,T., Okada,N., Wakamatsu,T. and Tamura,T.A.
  TITLE     TBP-interacting protein 120B, which is induced in relation to
            myogenesis, binds to NOT3
  JOURNAL   Biochem Biophys Res Commun 296 (5), 1097-1103 (2002)
   PUBMED   12207886
  REMARK    GeneRIF: TBP-interacting protein 120B binds to NOT3
REFERENCE   9  (residues 1 to 754)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
REFERENCE   10 (residues 1 to 754)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC245052.3.
            
            On or before May 23, 2025 this sequence version replaced
            XP_054186163.1, XP_054189640.1, XP_054189539.1, XP_054187225.1,
            XP_054186461.1, XP_054187497.1, XP_005278339.1, XP_054185668.1,
            XP_054186711.1, XP_054186941.1, XP_054177066.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1434311.1,
                                           SRR14038193.1291509.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..754
                     /product="CCR4-NOT transcription complex subunit 3 isoform
                     10"
                     /note="NOT3 (negative regulator of transcription 3, yeast)
                     homolog; CCR4-associated factor 3; leukocyte receptor
                     cluster member 2"
                     /calculated_mol_wt=81869
     Region          3..230
                     /region_name="Not3"
                     /note="Not1 N-terminal domain, CCR4-Not complex component;
                     pfam04065"
                     /db_xref="CDD:461155"
     Region          241..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75175.1)"
     Region          <289..660
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Region          621..746
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     Region          662..754
                     /region_name="Repressor domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O75175.1)"
     CDS             1..754
                     /gene="CNOT3"
                     /gene_synonym="IDDSADF; LENG2; NOT3; NOT3H"
                     /coded_by="NM_001440661.1:283..2547"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:4849"
                     /db_xref="HGNC:HGNC:7879"
                     /db_xref="MIM:604910"
ORIGIN      
        1 madkrklqge idrclkkvse gveqfediwq klhnaananq kekyeadlkk eikklqrlrd
       61 qiktwvasne ikdkrqlidn rklietqmer fkvveretkt kayskeglgl aqkvdpaqke
      121 keevgqwltn tidtlnmqvd qfesevesls vqtrkkkgdk dqkqdriegl krhiekhryh
      181 vrmletilrm ldndsilvda irkikddvey yvdssqdpdf eeneflyddl dledipqalv
      241 atsppshshm edeifnqsss tptsttsssp ippspanctt enseddkkrg rstdsevsqs
      301 pakngskpvh snqhpqspav pptypsgppp aasalsttpg nngvpapaap psalgpkasp
      361 apshnsgtpa pyaqavappa psgpsttqpr ppsvqpsggg gggsggggss sssnssaggg
      421 agkqngatsy ssvvadspae valsssggnn assqalgpps gphnpppsts kepsaaaptg
      481 aggvapgsgn nsggpsllvp lpvnppsspt psfsdakaag allngppqfs tapeikapep
      541 lsslksmaer aaissgiedp vptlhlterd iilsstsapp asaqpplqls evniplslgv
      601 cplgpvpltk eqlyqqamee aawhhmphps dserirqylp rnpcptppyh hqmppphsdt
      661 vefyqrlste tlffifyyle gtkaqylaak alkkqswrfh tkymmwfqrh eepktitdef
      721 eqgtyiyfdy ekwgqrkkeg ftfeyryled rdlq
//
LOCUS       NP_001414274            1437 aa            linear   PRI 21-NOV-2025
DEFINITION  enhancer of mRNA-decapping protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_001414274
VERSION     NP_001414274.1
DBSOURCE    REFSEQ: accession NM_001427345.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1437)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1437)
  AUTHORS   Bloch,D.B., Sinow,C.O., Sauer,A.J. and Corman,B.H.P.
  TITLE     Assembly and regulation of the mammalian mRNA processing body
  JOURNAL   PLoS One 18 (3), e0282496 (2023)
   PUBMED   36877681
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1437)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1437)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   5  (residues 1 to 1437)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1437)
  AUTHORS   Bloch,D.B., Gulick,T., Bloch,K.D. and Yang,W.H.
  TITLE     Processing body autoantibodies reconsidered
  JOURNAL   RNA 12 (5), 707-709 (2006)
   PUBMED   16641511
REFERENCE   7  (residues 1 to 1437)
  AUTHORS   Fenger-Gron,M., Fillman,C., Norrild,B. and Lykke-Andersen,J.
  TITLE     Multiple processing body factors and the ARE binding protein TTP
            activate mRNA decapping
  JOURNAL   Mol Cell 20 (6), 905-915 (2005)
   PUBMED   16364915
REFERENCE   8  (residues 1 to 1437)
  AUTHORS   Yu,J.H., Yang,W.H., Gulick,T., Bloch,K.D. and Bloch,D.B.
  TITLE     Ge-1 is a central component of the mammalian cytoplasmic mRNA
            processing body
  JOURNAL   RNA 11 (12), 1795-1802 (2005)
   PUBMED   16314453
REFERENCE   9  (residues 1 to 1437)
  AUTHORS   Garcia-Lozano,J.R., Gonzalez-Escribano,M.F., Wichmann,I. and
            Nunez-Roldan,A.
  TITLE     Cytoplasmic detection of a novel protein containing a nuclear
            localization sequence by human autoantibodies
  JOURNAL   Clin Exp Immunol 107 (3), 501-506 (1997)
   PUBMED   9067524
REFERENCE   10 (residues 1 to 1437)
  AUTHORS   Bloch,D.B., Rabkina,D., Quertermous,T. and Bloch,K.D.
  TITLE     The immunoreactive region in a novel autoantigen contains a nuclear
            localization sequence
  JOURNAL   Clin Immunol Immunopathol 72 (3), 380-389 (1994)
   PUBMED   7520377
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC040162.5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: MW689236.1, SRR14038191.397736.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1437
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..1437
                     /product="enhancer of mRNA-decapping protein 4 isoform 1"
                     /note="enhancer of mRNA-decapping protein 4; autoantigen
                     Ge-1; autoantigen RCD-8; human enhancer of decapping large
                     subunit"
                     /calculated_mol_wt=155299
     Region          114..441
                     /region_name="Ge1_WD40"
                     /note="WD40 region of Ge1, enhancer of mRNA-decapping
                     protein; pfam16529"
                     /db_xref="CDD:465162"
     Region          180..219
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          232..288
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          300..341
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          348..393
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <525..982
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1437
                     /gene="EDC4"
                     /gene_synonym="Ge-1; GE1; HEDL5; HEDLS; RCD-8; RCD8"
                     /coded_by="NM_001427345.1:211..4524"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:23644"
                     /db_xref="HGNC:HGNC:17157"
                     /db_xref="MIM:606030"
ORIGIN      
        1 mascasidie datqhlrdil kldrpaggps aesprpssay ngdlngllvp dplcsgdsts
       61 anktglrtmp pinlqekqvi clsgddsstc igilakevei vassdssiss kargsnkvki
      121 qpvakydweq kyyygnliav snsflayair aanngsamvr visvstsert llkgftgsva
      181 dlafahlnsp qlacldeagn lfvwrlalvn gkiqeeilvh irqpegtpln hfrriiwcpf
      241 ipeesedcce essptvallh edraevwdld mlrsshstwp vdvsqikqgf ivvkghstcl
      301 segalspdgt vlatashdgy vkfwqiyieg qdeprclhew kphdgrplsc llfcdnhkkq
      361 dpdvpfwrfl itgadqnrel kmwctvswtc lqtirfspdi fssvsvppsl kvcldlsaey
      421 lilsdvqrkv lyvmellqnq eeghacfssi sefllthpvl sfgiqvvsrc rlrhtevlpa
      481 eeendslgad gthgagames aagvliklfc vhtkalqdvq irfqpqlnpd vvaplpthta
      541 hedftfgesr pelgseglgs aahgsqpdlr rivelpapad flslssetkp klmtpdafmt
      601 psaslqqita spsssssgss sssssssssl tavsamssts avdpsltrpp eeltlspklq
      661 ldgsltmsss gslqasprgl lpgllpapad kltpkgpgqv ptatsalsle lqeveplglp
      721 qaspsrtrsp dvissastal sqdipeiase alsrgfgssa peglepdsma saasalhlls
      781 prprpgpelg pqlgldggpg dgdrhntpsl leaaltqeas tpdsqvwpta pditretcst
      841 laesprnglq ekhkslafhr ppyhllqqrd sqdasaeqsd hddevaslas asggfgtkvp
      901 aprlpakdwk tkgsprtspk lkrkskkddg daamgsrlte hqvaeppedw paliwqqqre
      961 laelrhsqee llqrlctqle glqstvtghv eraletrheq eriletgstt whrdggsilg
     1021 lgrstrpapg pflsygaerr leralaegqq rggqlqeqlt qqlsqalssa vagrlersir
     1081 deikktvppc vsrslepmag qlsnsvatkl tavegsmken iskllksknl tdaiaraaad
     1141 tlqgpmqaay reafqsvvlp afekscqamf qqindsfrlg tqeylqqles hmksrkareq
     1201 earepvlaql rglvstlqsa teqmaatvag svraevqhql hvavgslqes ilaqvqrivk
     1261 gevsvalkeq qaavtssimq amrsaagtpv psahldcqaq qahilqllqq ghlnqafqqa
     1321 ltaadlnlvl yvcetvdpaq vfgqppcpls qpvllsliqq lasdlgtrtd lklsyleeav
     1381 mhldhsdpit rdhmgsvmaq vrqklfqflq aephnslgka arrlslmlhg lvtpslp
//
LOCUS       NP_001425416            2312 aa            linear   PRI 21-NOV-2025
DEFINITION  AT-rich interactive domain-containing protein 1B isoform 9 [Homo
            sapiens].
ACCESSION   NP_001425416 XP_047275103 XP_054212026
VERSION     NP_001425416.1
DBSOURCE    REFSEQ: accession NM_001438487.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2312)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2312)
  AUTHORS   Bosch,E., Guse,E., Kirchner,P., Winterpacht,A., Walther,M.,
            Alders,M., Kerkhof,J., Ekici,A.B., Sticht,H., Sadikovic,B., Reis,A.
            and Vasileiou,G.
  TITLE     The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation
  JOURNAL   Hum Genet 143 (8), 965-978 (2024)
   PUBMED   39028335
  REMARK    GeneRIF: The missing link: ARID1B non-truncating variants causing
            Coffin-Siris syndrome due to protein aggregation.
REFERENCE   3  (residues 1 to 2312)
  AUTHORS   Huang,X., Li,H., Yang,S., Ma,M., Lian,Y., Wu,X., Qi,X., Wang,X.,
            Rong,W. and Sheng,X.
  TITLE     De novo variation in ARID1B gene causes Coffin-Siris syndrome 1 in
            a Chinese family with excessive early-onset high myopia
  JOURNAL   BMC Med Genomics 17 (1), 142 (2024)
   PUBMED   38790056
  REMARK    GeneRIF: De novo variation in ARID1B gene causes Coffin-Siris
            syndrome 1 in a Chinese family with excessive early-onset high
            myopia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2312)
  AUTHORS   Hurlstone,A.F., Olave,I.A., Barker,N., van Noort,M. and Clevers,H.
  TITLE     Cloning and characterization of hELD/OSA1, a novel BRG1 interacting
            protein
  JOURNAL   Biochem J 364 (Pt 1), 255-264 (2002)
   PUBMED   11988099
  REMARK    GeneRIF: Cloning and characterization of hELD/OSA1, a novel BRG1
            interacting protein.
REFERENCE   5  (residues 1 to 2312)
  AUTHORS   Phelan,M.L., Sif,S., Narlikar,G.J. and Kingston,R.E.
  TITLE     Reconstitution of a core chromatin remodeling complex from SWI/SNF
            subunits
  JOURNAL   Mol Cell 3 (2), 247-253 (1999)
   PUBMED   10078207
REFERENCE   6  (residues 1 to 2312)
  AUTHORS   Imbert,G., Saudou,F., Yvert,G., Devys,D., Trottier,Y.,
            Garnier,J.M., Weber,C., Mandel,J.L., Cancel,G., Abbas,N., Durr,A.,
            Didierjean,O., Stevanin,G., Agid,Y. and Brice,A.
  TITLE     Cloning of the gene for spinocerebellar ataxia 2 reveals a locus
            with high sensitivity to expanded CAG/glutamine repeats
  JOURNAL   Nat Genet 14 (3), 285-291 (1996)
   PUBMED   8896557
REFERENCE   7  (residues 1 to 2312)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
REFERENCE   8  (residues 1 to 2312)
  AUTHORS   Vergano,S.A., van der Sluijs,P.J. and Santen,G.
  TITLE     ARID1B-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31132234
REFERENCE   9  (residues 1 to 2312)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
REFERENCE   10 (residues 1 to 2312)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355297.20, AL162578.13,
            AL049820.23 and AL591545.6.
            
            On or before Apr 21, 2025 this sequence version replaced
            XP_047275103.1, XP_054212026.1.
            
            Summary: This locus encodes an AT-rich DNA interacting
            domain-containing protein. The encoded protein is a component of
            the SWI/SNF chromatin remodeling complex and may play a role in
            cell-cycle activation. The protein encoded by this locus is similar
            to AT-rich interactive domain-containing protein 1A. These two
            proteins function as alternative, mutually exclusive ARID-subunits
            of the SWI/SNF complex. The associated complexes play opposing
            roles. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1922571.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2312
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..2312
                     /product="AT-rich interactive domain-containing protein 1B
                     isoform 9"
                     /note="BRG1-binding protein ELD/OSA1; ELD (eyelid)/OSA
                     protein; BRG1-associated factor 250b; ARID
                     domain-containing protein 1B; AT rich interactive domain
                     1B (SWI1-like)"
                     /calculated_mol_wt=242884
     Region          <741..1070
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1130..1222
                     /region_name="ARID_ARID1B"
                     /note="ARID/BRIGHT DNA binding domain of AT-rich
                     interactive domain-containing protein 1B (ARID1B) and
                     similar proteins; cd16877"
                     /db_xref="CDD:350641"
     Site            order(1152..1158,1183,1185..1186,1189,1199,1201..1203,
                     1205)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350641"
     Region          1243..>1623
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          2003..2258
                     /region_name="BAF250_C"
                     /note="SWI/SNF-like complex subunit BAF250/Osa; pfam12031"
                     /db_xref="CDD:463439"
     CDS             1..2312
                     /gene="ARID1B"
                     /gene_synonym="6A3-5; BAF250B; BRIGHT; CSS1; DAN15;
                     ELD/OSA1; MRD12; OSA2; P250R; SMARCF2"
                     /coded_by="NM_001438487.1:304..7242"
                     /note="isoform 9 is encoded by transcript variant 10"
                     /db_xref="GeneID:57492"
                     /db_xref="HGNC:HGNC:18040"
                     /db_xref="MIM:614556"
ORIGIN      
        1 maaraaaaaa aaaararara gsgerrappg prpapgardl eagargaaaa aaapgpmlgg
       61 ggdgggglns vhhhpllprh elnmahnaga aaaagthsak sggseaalke ggsaaalsss
      121 ssssaaaaaa ssssssgpgs ametgllpnh klktvgeapa apphqqhhhh hhahhhhhha
      181 hhlhhhhalq qqlnqfqqqq qqqqqqqqqq qqqqhpisnn nslggaggga pqpgpdmeqp
      241 qhggakdsaa ggqadppgpp llskpgdedd appkmgepag gryehpglga lgtqqppvav
      301 pgggggpaav pefnnyygsa apasggpggr agpcfdqhgg qqspgmgmmh sasaaaagap
      361 gsmdplqnsh egypnsqcnh ypgysrpgag gggggggggg ggsggggggg gagaggagag
      421 avaaaaaaaa aaaggggggg yggssagygv lssprqqggg mmmgpgggga aslskaaags
      481 aaggfqrfag qnqhpsgatp tlnqlltsps pmmrsyggsy peysspsapp pppsqpqsqa
      541 aaagaaaggq qaaagmglgk dmgaqyaaas pawaaaqqrs hpamspgtpg ptmgrsqgsp
      601 mdpmvmkrpq lygmgsnphs qpqqsspypg gsygppgpqr ypigiqgrtp gamagmqypq
      661 qqmppqygqq gvsgycqqgq qpyysqqpqp phlppqaqyl psqsqqryqp qqdmsqegyg
      721 trsqpplapg kpnhedlnli qqerpsslpd lsgsiddlpt gteatlssav sasgstssqg
      781 dqsnpaqspf sphasphlss ipggpspspv gspvgsnqsr sgpispasip gsqmppqppg
      841 sqsessshpa lsqspmpqer gnysrppays gvpsasysgp gpgmgisann qmhgqgpsqp
      901 cgavplgrmp sagmqnrpfp gnmssmtpss pgmsqqggpg mgppmptvnr kaqeaaaavm
      961 qaaansaqsr qgsfpgmnqs glmassspys qpmnnssslm ntqappysma pamvnssaas
     1021 vgladmmspg esklplplka dgkeegtpqp eskskdsyss qgisqpptpg nlpvpspmsp
     1081 ssasissfhg desdsisspg wpktpsspks ssstttgeki tkvyelgnep erklwvdryl
     1141 tfmeergspv sslpavgkkp ldlfrlyvcv keigglaqvn knkkwrelat nlnvgtsssa
     1201 asslkkqyiq ylfafeckie rgeepppevf stgdtkkqpk lqppspansg slqgpqtpqs
     1261 tgsnsmaevp gdlkpptpas tphgqmtpmq ggrsstisvh dpfsdvsdss fpkrnsmtpn
     1321 apyqqgmsmp dvmgrmpyep nkdpfggmrk vpgssepfmt qgqmpnssmq dmynqspsga
     1381 msnlgmgqrq qfpygasydr rhepygqqyp gqgppsgqpp ygghqpglyp qqpnykrhmd
     1441 gmygppakrh egdmynmqys sqqqemynqy ggsysgpdrr piqgqypypy srermqgpgq
     1501 iqthgippqm mggplqssss egpqqnmwaa rndmpypyqn rqgpggptqa ppypgmnrtd
     1561 dmmvpdqrin hesqwpshvs qrqpymsssa smqpitrppq psyqtppslp nhisrapspa
     1621 sfqrslenrm spskspflps mkmqkvmptv ptsqvtgppp qpppirreit fppgsveasq
     1681 pvlkqrrkit skdivtpeaw rvmmslksgl laestwaldt inillyddst vatfnlsqls
     1741 gflellveyf rkclidifgi lmeyevgdps qkaldhnaar kddsqsladd sgkeeedaec
     1801 idddeedeed eeedsektes dekssialta pdaaadpkek pkqaskfdkl pikivkknnl
     1861 fvvdrsdklg rvqefnsgll hwqlgggdtt ehiqthfesk meipprrrpp pplssagrkk
     1921 eqegkgdsee qqeksiiati ddvlsarpga lpedanpgpq tesskfpfgi qqakshrnik
     1981 lledeprsrd etplctiahw qdslakrcic vsnivrslsf vpgndaemsk hpglvlilgk
     2041 lillhhehpe rkrapqtyek eededkgvac skdewwwdcl evlrdntlvt lanisgqldl
     2101 saytesiclp ildgllhwmv cpsaeaqdpf ptvgpnsvls pqrlvletlc klsiqdnnvd
     2161 lilatppfsr qekfyatlvr yvgdrknpvc remsmallsn laqgdalaar aiavqkgsig
     2221 nlisfledgv tmaqyqqsqh nlmhmqpppl eppsvdmmcr aakallamar vdenrsefll
     2281 hegrlldisi savlnslvas vicdvlfqig ql
//
LOCUS       NP_001397702             201 aa            linear   PRI 21-NOV-2025
DEFINITION  ephrin-A5 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001397702 XP_006714628
VERSION     NP_001397702.1
DBSOURCE    REFSEQ: accession NM_001410773.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Jukonen,J., Moyano-Galceran,L., Hopfner,K., Pietila,E.A.,
            Lehtinen,L., Huhtinen,K., Gucciardo,E., Hynninen,J., Hietanen,S.,
            Grenman,S., Ojala,P.M., Carpen,O. and Lehti,K.
  TITLE     Aggressive and recurrent ovarian cancers upregulate ephrinA5, a
            non-canonical effector of EphA2 signaling duality
  JOURNAL   Sci Rep 11 (1), 8856 (2021)
   PUBMED   33893375
  REMARK    GeneRIF: Aggressive and recurrent ovarian cancers upregulate
            ephrinA5, a non-canonical effector of EphA2 signaling duality.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Xie,J., Xing,S., Shen,B.Y., Chen,H.T., Sun,B., Wang,Z.T., Wang,J.W.
            and Lu,X.X.
  TITLE     PIWIL1 interacting RNA piR-017061 inhibits pancreatic cancer growth
            via regulating EFNA5
  JOURNAL   Hum Cell 34 (2), 550-563 (2021)
   PUBMED   33389678
  REMARK    GeneRIF: PIWIL1 interacting RNA piR-017061 inhibits pancreatic
            cancer growth via regulating EFNA5.
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 201)
  AUTHORS   Kozlosky,C.J., VandenBos,T., Park,L., Cerretti,D.P. and
            Carpenter,M.K.
  TITLE     LERK-7: a ligand of the Eph-related kinases is developmentally
            regulated in the brain
  JOURNAL   Cytokine 9 (8), 540-549 (1997)
   PUBMED   9245480
REFERENCE   7  (residues 1 to 201)
  AUTHORS   Lackmann,M., Mann,R.J., Kravets,L., Smith,F.M., Bucci,T.A.,
            Maxwell,K.F., Howlett,G.J., Olsson,J.E., Vanden Bos,T.,
            Cerretti,D.P. and Boyd,A.W.
  TITLE     Ligand for EPH-related kinase (LERK) 7 is the preferred high
            affinity ligand for the HEK receptor
  JOURNAL   J Biol Chem 272 (26), 16521-16530 (1997)
   PUBMED   9195962
REFERENCE   8  (residues 1 to 201)
  AUTHORS   Cerretti,D.P., Copeland,N.G., Gilbert,D.J., Jenkins,N.A.,
            Kuefer,M.U., Valentine,V., Shapiro,D.N., Cui,X. and Morris,S.W.
  TITLE     The gene encoding LERK-7 (EPLG7, Epl7), a ligand for the
            Eph-related receptor tyrosine kinases, maps to human chromosome 5
            at band q21 and to mouse chromosome 17
  JOURNAL   Genomics 35 (2), 376-379 (1996)
   PUBMED   8661153
REFERENCE   9  (residues 1 to 201)
  AUTHORS   Gale,N.W., Holland,S.J., Valenzuela,D.M., Flenniken,A., Pan,L.,
            Ryan,T.E., Henkemeyer,M., Strebhardt,K., Hirai,H., Wilkinson,D.G.,
            Pawson,T., Davis,S. and Yancopoulos,G.D.
  TITLE     Eph receptors and ligands comprise two major specificity subclasses
            and are reciprocally compartmentalized during embryogenesis
  JOURNAL   Neuron 17 (1), 9-19 (1996)
   PUBMED   8755474
REFERENCE   10 (residues 1 to 201)
  AUTHORS   Winslow,J.W., Moran,P., Valverde,J., Shih,A., Yuan,J.Q., Wong,S.C.,
            Tsai,S.P., Goddard,A., Henzel,W.J., Hefti,F. et al.
  TITLE     Cloning of AL-1, a ligand for an Eph-related tyrosine kinase
            receptor involved in axon bundle formation
  JOURNAL   Neuron 14 (5), 973-981 (1995)
   PUBMED   7748564
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC024587.5 and AC008952.7.
            
            On Aug 15, 2022 this sequence version replaced XP_006714628.1.
            
            Summary: Ephrin-A5, a member of the ephrin gene family, prevents
            axon bundling in cocultures of cortical neurons with astrocytes, a
            model of late stage nervous system development and differentiation.
            The EPH and EPH-related receptors comprise the largest subfamily of
            receptor protein-tyrosine kinases and have been implicated in
            mediating developmental events, particularly in the nervous system.
            EPH receptors typically have a single kinase domain and an
            extracellular region containing a Cys-rich domain and 2 fibronectin
            type III repeats. The ephrin ligands and receptors have been named
            by the Eph Nomenclature Committee (1997). Based on their structures
            and sequence relationships, ephrins are divided into the ephrin-A
            (EFNA) class, which are anchored to the membrane by a
            glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB)
            class, which are transmembrane proteins. The Eph family of
            receptors are similarly divided into 2 groups based on the
            similarity of their extracellular domain sequences and their
            affinities for binding ephrin-A and ephrin-B ligands. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.2156425.1,
                                           SRR14038192.3911343.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q21.3"
     Protein         1..201
                     /product="ephrin-A5 isoform 2 precursor"
                     /note="eph-related receptor tyrosine kinase ligand 7;
                     AL-1; LERK-7"
                     /calculated_mol_wt=20902
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2412
     Region          30..159
                     /region_name="Ephrin-A_Ectodomain"
                     /note="Ectodomain of Ephrin A; cd10425"
                     /db_xref="CDD:259896"
     Site            order(57,97..101,113..114,121..126,128..129)
                     /site_type="other"
                     /note="receptor binding site [polypeptide binding]"
                     /db_xref="CDD:259896"
     CDS             1..201
                     /gene="EFNA5"
                     /gene_synonym="AF1; EFL5; EPLG7; GLC1M; LERK7; RAGS"
                     /coded_by="NM_001410773.1:325..930"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS93759.1"
                     /db_xref="GeneID:1946"
                     /db_xref="HGNC:HGNC:3225"
                     /db_xref="MIM:601535"
ORIGIN      
        1 mlhvemltlv flvlwmcvfs qdpgskavad ryavywnssn prfqrgdyhi dvcindyldv
       61 fcphyedsvp edkteryvly mvnfdgysac dhtskgfkrw ecnrphspng plkfsekfql
      121 ftpfslgfef rpgreyfyis saipdngrrs clklkvfvrp tndtvhesae psrgenaaqt
      181 pripsrllai llfllamllt l
//
LOCUS       NP_001393923             478 aa            linear   PRI 21-NOV-2025
DEFINITION  lamin isoform K [Homo sapiens].
ACCESSION   NP_001393923
VERSION     NP_001393923.1
DBSOURCE    REFSEQ: accession NM_001406994.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 478)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 478)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.566214.1,
                                           SRR14038191.4191787.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..478
                     /product="lamin isoform K"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=52497
     Region          <104..178
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          226..333
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     CDS             1..478
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001406994.1:873..2309"
                     /note="isoform K is encoded by transcript variant 19"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 mrpdwwrltm gssvslragw rmrcrncgps mrtrwssirr swrrlilpsw tmpgsllrgt
       61 atwwglptrs cssrasasta slpssassrs ralgsspnpp tplqlaakea klrdledsla
      121 rerdtsrrll aekeremaem rarmqqqlde yqelldikla ldmeihayrk llegeeerlr
      181 lspsptsqrs rgrasshssq tqgggsvtkk rklestesrs sfsqhartsg rvaveevdee
      241 gkfvrlrnks nedqsmgnwq ikrqngddpl ltyrfppkft lkagqvvtiw aagagathsp
      301 ptdlvwkaqn twgcgnslrt alinstgeev amrklvrsvt vveddededg ddllhhhhgs
      361 hcsssgdpae ynlrsrtvlc gtcgqpadka sasgsgaqvg gpissgssas svtvtrsyrs
      421 vggsgggsfg dnlvtrsyll gnssprtqsp qncsiiqemg mrweveegrr kvslsclp
//
LOCUS       NP_001427733            1174 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphorylase b kinase regulatory subunit alpha, liver isoform
            isoform 6 [Homo sapiens].
ACCESSION   NP_001427733 XP_047298121 XP_054183181
VERSION     NP_001427733.1
DBSOURCE    REFSEQ: accession NM_001440804.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1174)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1174)
  AUTHORS   Dong,R., Wei,X., Zhang,K., Song,F., Lv,Y., Gao,M., Wang,D., Ma,J.,
            Gai,Z. and Liu,Y.
  TITLE     Genotypic and phenotypic characteristics of 12 chinese children
            with glycogen storage diseases
  JOURNAL   Front Genet 13, 932760 (2022)
   PUBMED   36105079
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1174)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1174)
  AUTHORS   Benner,A., Alhaidan,Y., Lines,M.A., Brusgaard,K., De Leon,D.D.,
            Sparkes,R., Frederiksen,A.L. and Christesen,H.T.
  TITLE     PHKA2 variants expand the phenotype of phosphorylase B kinase
            deficiency to include patients with ketotic hypoglycemia only
  JOURNAL   Am J Med Genet A 185 (10), 2959-2975 (2021)
   PUBMED   34117828
  REMARK    GeneRIF: PHKA2 variants expand the phenotype of phosphorylase B
            kinase deficiency to include patients with ketotic hypoglycemia
            only.
REFERENCE   5  (residues 1 to 1174)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1174)
  AUTHORS   Herbert,M., Goldstein,J.L., Rehder,C., Austin,S., Kishnani,P.S. and
            Bali,D.S.
  TITLE     Phosphorylase Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21634085
REFERENCE   7  (residues 1 to 1174)
  AUTHORS   Davidson,J.J., Ozcelik,T., Hamacher,C., Willems,P.J., Francke,U.
            and Kilimann,M.W.
  TITLE     cDNA cloning of a liver isoform of the phosphorylase kinase alpha
            subunit and mapping of the gene to Xp22.2-p22.1, the region of
            human X-linked liver glycogenosis
  JOURNAL   Proc Natl Acad Sci U S A 89 (6), 2096-2100 (1992)
   PUBMED   1372435
REFERENCE   8  (residues 1 to 1174)
  AUTHORS   Wauters,J.G., Bossuyt,P.J., Davidson,J., Hendrickx,J.,
            Kilimann,M.W. and Willems,P.J.
  TITLE     Regional mapping of a liver alpha-subunit gene of phosphorylase
            kinase (PHKA) to the distal region of human chromosome Xp
  JOURNAL   Cytogenet Cell Genet 60 (3-4), 194-196 (1992)
   PUBMED   1505214
REFERENCE   9  (residues 1 to 1174)
  AUTHORS   Willems,P.
  TITLE     Families with X-linked liver glycogenosis due to phosphorylase
            kinase deficiency
  JOURNAL   Clin Genet 38 (1), 80 (1990)
   PUBMED   2387090
REFERENCE   10 (residues 1 to 1174)
  AUTHORS   Willems,P.J., Gerver,W.J., Berger,R. and Fernandes,J.
  TITLE     The natural history of liver glycogenosis due to phosphorylase
            kinase deficiency: a longitudinal study of 41 patients
  JOURNAL   Eur J Pediatr 149 (4), 268-271 (1990)
   PUBMED   2303074
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL732509.4 and AL096700.14.
            
            On or before May 30, 2025 this sequence version replaced
            XP_047298121.1, XP_054183181.1.
            
            Summary: Phosphorylase kinase is a polymer of 16 subunits, four
            each of alpha, beta, gamma and delta. The alpha subunit includes
            the skeletal muscle and hepatic isoforms, and the hepatic isoform
            is encoded by this gene. The beta subunit is the same in both the
            muscle and hepatic isoforms, and encoded by one gene. The gamma
            subunit also includes the skeletal muscle and hepatic isoforms,
            which are encoded by two different genes. The delta subunit is a
            calmodulin and can be encoded by three different genes. The gamma
            subunits contain the active site of the enzyme, whereas the alpha
            and beta subunits have regulatory functions controlled by
            phosphorylation. The delta subunit mediates the dependence of the
            enzyme on calcium concentration. Mutations in this gene cause
            glycogen storage disease type 9A, also known as X-linked liver
            glycogenosis. Alternatively spliced transcript variants have been
            reported, but the full-length nature of these variants has not been
            determined.[provided by RefSeq, Feb 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2836262.1,
                                           SRR14038192.4082990.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1174
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.13"
     Protein         1..1174
                     /product="phosphorylase b kinase regulatory subunit alpha,
                     liver isoform isoform 6"
                     /EC_number="2.7.11.19"
                     /note="phosphorylase kinase alpha L subunit; phosphorylase
                     kinase alpha-subunit"
                     /calculated_mol_wt=131765
     Region          8..>406
                     /region_name="Glyco_hydro_15"
                     /note="Glycosyl hydrolases family 15; pfam00723"
                     /db_xref="CDD:395586"
     Region          <769..886
                     /region_name="Bac_rhamnosid6H"
                     /note="Bacterial alpha-L-rhamnosidase 6 hairpin
                     glycosidase domain; cl46875"
                     /db_xref="CDD:481215"
     Region          897..>1086
                     /region_name="KPBB_C"
                     /note="Phosphorylase b kinase C-terminal domain;
                     pfam19292"
                     /db_xref="CDD:437124"
     CDS             1..1174
                     /gene="PHKA2"
                     /gene_synonym="GSD9A; PHK; PYK; PYKL; XLG; XLG2"
                     /coded_by="NM_001440804.1:183..3707"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:5256"
                     /db_xref="HGNC:HGNC:8926"
                     /db_xref="MIM:300798"
ORIGIN      
        1 mrsrsnsgvr ldgyarlvqq tilcyqnpvt gllsasheqk dawvrdniys ilavwglgma
       61 yrknadrded kakayeleqn vvklmrgllq cmmrqvakve kfkhtqstkd slhakyntat
      121 cgtvvgddqw ghlqvdatsl fllflaqmta sglriiftld evafiqnlvf yieaaykvad
      181 ygmwergdkt nqgipelnas svgmaksilf smlprastsk eidagllsii sfpafavedv
      241 nlvnvtknei isklqgrygc crflrdgykt predpnrlhy dpaelklfen iecewpvfwt
      301 yfiidgvfsg davqvqeyre alegilirgk ngirlvpely avppnkvdee yknphtvdrv
      361 pmgkvphlwg qslyilssll aegflaagei dplnrrfsts vkpdvvvqvt vlaennhikd
      421 llrkhgvnvq siadihpiqv qpgrilshiy aklgrnknmn lsgrpyrhig vlgtsklyvi
      481 rnqiftftpq ftdqhhfyla ldnemiveml rielaylctc wrmtgrptlt fpisrtmltn
      541 dgsdihsavl stirkledgy fggarvklgn lseflttsfy tyltfldpdc deklfdnase
      601 gtfspdsdsd lvgyledtcn qesqdeldhy inhllqstsl rsylpplckn tedrhvfsai
      661 hstrdilsvm akakglevpf vpmtlptkvl sahrkslnlv dspqpllekv pesdfqwprd
      721 dhgdvdcekl veqlkdcsnl qdqadilyil yvikgpswdt nlsgqhgvtv qnllgelygk
      781 aglnqewgli ryisgllrkk vevlaeactd llshqkqltv glppepreki isaplppeel
      841 tkliyeasgq disiavltqe ivvylamyvr aqpslfveml rlrigliiqv matelarsln
      901 csgeeasesl mnlspfdmkn llhhilsgke fgversvrpi hsstssptis ihevghtgvt
      961 ktersginrl rsemkqrsst pssptgtsss dsgghhigwg erqgqwlrrr rldgainrvp
     1021 vgfyqrvwki lqkchglsid gyvlpssttr emtpheikfa vhvesvlnrv pqpeyrqllv
     1081 eaimvltlls dtemtsiggi ihvdqivqma sqlflqdqvs igamdtlekd qatgichffy
     1141 dsapsgaygt mtyltravas ylqellpnsg cqmq
//
LOCUS       NP_001407089             819 aa            linear   PRI 21-NOV-2025
DEFINITION  protein enabled homolog isoform g [Homo sapiens].
ACCESSION   NP_001407089 XP_024304083 XP_054193580
VERSION     NP_001407089.1
DBSOURCE    REFSEQ: accession NM_001420160.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Yin,X., Wang,J., Shen,Z., Jia,Q., Bian,Y., Yang,Z., Liu,Y., Li,Y.
            and Zhang,H.
  TITLE     ENAH transcriptionally activated by YY1 promotes growth and
            invasion of laryngocarcinoma cells through PI3K/AKT signaling
  JOURNAL   Eur J Pharmacol 983, 176991 (2024)
   PUBMED   39265883
  REMARK    GeneRIF: ENAH transcriptionally activated by YY1 promotes growth
            and invasion of laryngocarcinoma cells through PI3K/AKT signaling.
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Cui,H., Liang,X., Zhu,Y., Elayah,S.A., Qi,H., Xie,L., Guo,Z.,
            Siya,F., Ming,Y., Yuxin,G., Tu,J. and Na,S.
  TITLE     Mena as a key enhancer factor of EMT to promote metastasis of human
            tongue squamous cell carcinoma
  JOURNAL   Oral Dis 30 (4), 2084-2096 (2024)
   PUBMED   37203597
  REMARK    GeneRIF: Mena as a key enhancer factor of EMT to promote metastasis
            of human tongue squamous cell carcinoma.
REFERENCE   4  (residues 1 to 819)
  AUTHORS   He,L., She,C., Jiang,S., Qi,Z., Deng,Z., Ji,L., Cui,Y. and Wu,J.
  TITLE     Mammalian enabled protein enhances tamoxifen sensitivity of the
            hormone receptor-positive breast cancer patients by suppressing the
            AKT signaling pathway
  JOURNAL   Biol Direct 19 (1), 21 (2024)
   PUBMED   38459605
  REMARK    GeneRIF: Mammalian enabled protein enhances tamoxifen sensitivity
            of the hormone receptor-positive breast cancer patients by
            suppressing the AKT signaling pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 819)
  AUTHORS   Liu,R., Miao,K., Gao,L. and He,L.
  TITLE     TRIM67 interacts with ENAH to regulate the apoptosis and autophagy
            of lung cancer cells
  JOURNAL   Gen Physiol Biophys 43 (2), 163-173 (2024)
   PUBMED   38477606
  REMARK    GeneRIF: TRIM67 interacts with ENAH to regulate the apoptosis and
            autophagy of lung cancer cells.
REFERENCE   6  (residues 1 to 819)
  AUTHORS   Urbanelli,L., Massini,C., Emiliani,C., Orlacchio,A., Bernardi,G.
            and Orlacchio,A.
  TITLE     Characterization of human Enah gene
  JOURNAL   Biochim Biophys Acta 1759 (1-2), 99-107 (2006)
   PUBMED   16494957
REFERENCE   7  (residues 1 to 819)
  AUTHORS   Mammoto,A., Sasaki,T., Asakura,T., Hotta,I., Imamura,H.,
            Takahashi,K., Matsuura,Y., Shirao,T. and Takai,Y.
  TITLE     Interactions of drebrin and gephyrin with profilin
  JOURNAL   Biochem Biophys Res Commun 243 (1), 86-89 (1998)
   PUBMED   9473484
REFERENCE   8  (residues 1 to 819)
  AUTHORS   Ermekova,K.S., Zambrano,N., Linn,H., Minopoli,G., Gertler,F.,
            Russo,T. and Sudol,M.
  TITLE     The WW domain of neural protein FE65 interacts with proline-rich
            motifs in Mena, the mammalian homolog of Drosophila enabled
  JOURNAL   J Biol Chem 272 (52), 32869-32877 (1997)
   PUBMED   9407065
REFERENCE   9  (residues 1 to 819)
  AUTHORS   Niebuhr,K., Ebel,F., Frank,R., Reinhard,M., Domann,E., Carl,U.D.,
            Walter,U., Gertler,F.B., Wehland,J. and Chakraborty,T.
  TITLE     A novel proline-rich motif present in ActA of Listeria
            monocytogenes and cytoskeletal proteins is the ligand for the EVH1
            domain, a protein module present in the Ena/VASP family
  JOURNAL   EMBO J 16 (17), 5433-5444 (1997)
   PUBMED   9312002
REFERENCE   10 (residues 1 to 819)
  AUTHORS   Sazuka,T., Tomooka,Y., Kathju,S., Ikawa,Y., Noda,M. and Kumar,S.
  TITLE     Identification of a developmentally regulated gene in the mouse
            central nervous system which encodes a novel proline rich protein
  JOURNAL   Biochim Biophys Acta 1132 (3), 240-248 (1992)
   PUBMED   1420303
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL591380.21, AL356216.13 and
            AC092811.2.
            
            On or before Apr 26, 2023 this sequence version replaced
            XP_024304083.1, XP_054193580.1.
            
            Summary: This gene encodes a member of the enabled/
            vasodilator-stimulated phosphoprotein. Members of this gene family
            are involved in actin-based motility. This protein is involved in
            regulating the assembly of actin filaments and modulates cell
            adhesion and motility. Alternate splice variants of this gene have
            been correlated with tumor invasiveness in certain tissues and
            these variants may serve as prognostic markers. A pseudogene of
            this gene is found on chromosome 3. [provided by RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853560.2951.1,
                                           SRR14038191.510270.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.12"
     Protein         1..819
                     /product="protein enabled homolog isoform g"
                     /note="protein enabled homolog; Mena delta 11a"
                     /calculated_mol_wt=89332
     Region          5..112
                     /region_name="EVH1_Ena_VASP-like"
                     /note="Enabled/VASP family EVH1 domain; cd01207"
                     /db_xref="CDD:269918"
     Site            order(16,23,69,71,77,79,81)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269918"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N8S7.2)"
     Region          <329..564
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          613..639
                     /region_name="WH2_hVASP-like"
                     /note="Wiskott-Aldrich syndrome protein (WASP)-homology
                     domain 2 (WH2) of human Vasodilator-stimulated
                     phosphoprotein and related proteins; cd22185"
                     /db_xref="CDD:409225"
     Site            order(620..621,623..624,627,629..633)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409225"
     Region          629..632
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409225"
     Region          781..815
                     /region_name="VASP_tetra"
                     /note="VASP tetramerization domain; pfam08776"
                     /db_xref="CDD:462599"
     CDS             1..819
                     /gene="ENAH"
                     /gene_synonym="ENA; MENA; NDPP1"
                     /coded_by="NM_001420160.1:434..2893"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="GeneID:55740"
                     /db_xref="HGNC:HGNC:18271"
                     /db_xref="MIM:609061"
ORIGIN      
        1 mseqsicqar aavmvyddan kkwvpaggst gfsrvhiyhh tgnntfrvvg rkiqdhqvvi
       61 ncaipkglky nqatqtfhqw rdarqvygln fgskedanvf asammhalev lnsqetgptl
      121 prqnsqlpaq vqngpsqeel eiqrrqlqeq qrqkelerer lerermerer lererlerer
      181 lererleqeq lererqerer qerlerqerl erqerlerqe rldrerqerq ererlerler
      241 erqererqeq lereqlewer errissaaps sdsslynapl peysscqpps apppsyakvi
      301 sapvsdatpd yavvtalppt stpptpplrh satrfatslg safhpvlphy atvprplnkn
      361 srpsspvntp ssqppatkpc awstsnfspl ppsppimiss ppgkatgprp vlpvcvsspv
      421 pqmppsptap nglvdsvtyp vsppptsgpa apppppplps laslshcgsq aspppstpia
      481 stpsskpsvl pspsaaapas vetplnsvlg dssasepglq aasqpaetps qqgivlgpla
      541 pppppplppg paqasvalpp ppgppppppl pstgpppppp ppplpnqvpp ppppppappl
      601 pasgfflasm sednrpltgl aaaiagaklr kvsrmedtsf psggnaigvn sassktdtgr
      661 gngplplggs glmeemsall arrrriaekg stieteqked kgedsepvts kasststpep
      721 trkpwertnt mngskspvis rrdsprknqi vfdnrsydsl hrpkstplsq psangvqteg
      781 ldydrlkqdi ldemrkeltk lkeelidair qelsksnta
//
LOCUS       NP_001428259            1655 aa            linear   PRI 21-NOV-2025
DEFINITION  BCL-6 corepressor-like protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001428259 XP_047298299 XP_054183527
VERSION     NP_001428259.1
DBSOURCE    REFSEQ: accession NM_001441330.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1655)
  AUTHORS   Luo,C., Chen,Z., Meng,L., Tan,C., He,W., Tu,C., Du,J., Lu,G.X.,
            Lin,G., Tan,Y.Q. and Hu,T.Y.
  TITLE     A hemizygous loss-of-function variant in BCORL1 is associated with
            male infertility and oligoasthenoteratozoospermia
  JOURNAL   Clin Genet 106 (1), 27-36 (2024)
   PUBMED   38342987
  REMARK    GeneRIF: A hemizygous loss-of-function variant in BCORL1 is
            associated with male infertility and oligoasthenoteratozoospermia.
REFERENCE   2  (residues 1 to 1655)
  AUTHORS   Kommoss,F.K.F., Chiang,S., Kobel,M., Koelsche,C., Chang,K.T.,
            Irving,J.A., Dickson,B., Thiryayi,S., Rouzbahman,M., Rasty,G., von
            Deimling,A., Lee,C.H. and Turashvili,G.
  TITLE     Endometrial Stromal Sarcomas With BCOR Internal Tandem Duplication
            and Variant BCOR/BCORL1 Rearrangements Resemble High-grade
            Endometrial Stromal Sarcomas With Recurrent CDK4 Pathway
            Alterations and MDM2 Amplifications
  JOURNAL   Am J Surg Pathol 46 (8), 1142-1152 (2022)
   PUBMED   35499168
  REMARK    GeneRIF: Endometrial Stromal Sarcomas With BCOR Internal Tandem
            Duplication and Variant BCOR/BCORL1 Rearrangements Resemble
            High-grade Endometrial Stromal Sarcomas With Recurrent CDK4 Pathway
            Alterations and MDM2 Amplifications.
REFERENCE   3  (residues 1 to 1655)
  AUTHORS   Schaefer,E.J., Wang,H.C., Karp,H.Q., Meyer,C.A., Cejas,P.,
            Gearhart,M.D., Adelman,E.R., Fares,I., Apffel,A., Lim,K., Xie,Y.,
            Gibson,C.J., Schenone,M., Murdock,H.M., Wang,E.S., Gondek,L.P.,
            Carroll,M.P., Vedula,R.S., Winer,E.S., Garcia,J.S., Stone,R.M.,
            Luskin,M.R., Carr,S.A., Long,H.W., Bardwell,V.J., Figueroa,M.E. and
            Lindsley,R.C.
  TITLE     BCOR and BCORL1 Mutations Drive Epigenetic Reprogramming and
            Oncogenic Signaling by Unlinking PRC1.1 from Target Genes
  JOURNAL   Blood Cancer Discov 3 (2), 116-135 (2022)
   PUBMED   35015684
  REMARK    GeneRIF: BCOR and BCORL1 Mutations Drive Epigenetic Reprogramming
            and Oncogenic Signaling by Unlinking PRC1.1 from Target Genes.
REFERENCE   4  (residues 1 to 1655)
  AUTHORS   Gafner,M., Michelson,M., Argilli,E., Yosovich,K., Sherr,E.H.,
            Parks,K.C., England,E.M., Hady-Cohen,R., Leibovitz,Z., Lev,D.,
            Michaeli-Yosef,Y., Lerman-Sagie,T. and Blumkin,L.
  TITLE     Major brain malformations: corpus callosum dysgenesis, agenesis of
            septum pellucidum and polymicrogyria in patients with
            BCORL1-related disorders
  JOURNAL   J Hum Genet 67 (2), 95-101 (2022)
   PUBMED   34400773
  REMARK    GeneRIF: Major brain malformations: corpus callosum dysgenesis,
            agenesis of septum pellucidum and polymicrogyria in patients with
            BCORL1-related disorders.
REFERENCE   5  (residues 1 to 1655)
  AUTHORS   Junco,S.E., Wang,R., Gaipa,J.C., Taylor,A.B., Schirf,V.,
            Gearhart,M.D., Bardwell,V.J., Demeler,B., Hart,P.J. and Kim,C.A.
  TITLE     Structure of the polycomb group protein PCGF1 in complex with BCOR
            reveals basis for binding selectivity of PCGF homologs
  JOURNAL   Structure 21 (4), 665-671 (2013)
   PUBMED   23523425
REFERENCE   6  (residues 1 to 1655)
  AUTHORS   Shaffer,J.R., Feingold,E., Wang,X., Lee,M., Tcuenco,K., Weeks,D.E.,
            Weyant,R.J., Crout,R., McNeil,D.W. and Marazita,M.L.
  TITLE     GWAS of dental caries patterns in the permanent dentition
  JOURNAL   J Dent Res 92 (1), 38-44 (2013)
   PUBMED   23064961
REFERENCE   7  (residues 1 to 1655)
  AUTHORS   Gao,Z., Zhang,J., Bonasio,R., Strino,F., Sawai,A., Parisi,F.,
            Kluger,Y. and Reinberg,D.
  TITLE     PCGF homologs, CBX proteins, and RYBP define functionally distinct
            PRC1 family complexes
  JOURNAL   Mol Cell 45 (3), 344-356 (2012)
   PUBMED   22325352
REFERENCE   8  (residues 1 to 1655)
  AUTHORS   Li,M., Collins,R., Jiao,Y., Ouillette,P., Bixby,D., Erba,H.,
            Vogelstein,B., Kinzler,K.W., Papadopoulos,N. and Malek,S.N.
  TITLE     Somatic mutations in the transcriptional corepressor gene BCORL1 in
            adult acute myelogenous leukemia
  JOURNAL   Blood 118 (22), 5914-5917 (2011)
   PUBMED   21989985
  REMARK    GeneRIF: BCORL1 by genetic criteria is a novel candidate tumor
            suppressor gene, joining the growing list of genes recurrently
            mutated in acute myelogenous leukemia.
REFERENCE   9  (residues 1 to 1655)
  AUTHORS   Pagan,J.K., Arnold,J., Hanchard,K.J., Kumar,R., Bruno,T.,
            Jones,M.J., Richard,D.J., Forrest,A., Spurdle,A., Verdin,E.,
            Crossley,M., Fanciulli,M., Chenevix-Trench,G., Young,D.B. and
            Khanna,K.K.
  TITLE     A novel corepressor, BCoR-L1, represses transcription through an
            interaction with CtBP
  JOURNAL   J Biol Chem 282 (20), 15248-15257 (2007)
   PUBMED   17379597
REFERENCE   10 (residues 1 to 1655)
  AUTHORS   Lose,F., Arnold,J., Young,D.B., Brown,C.J., Mann,G.J., Pupo,G.M.,
            Khanna,K.K., Chenevix-Trench,G. and Spurdle,A.B.
  CONSRTM   Kathleen Cuningham Foundation Consortium for Research into Familial
            Breast Cancer
  TITLE     BCoR-L1 variation and breast cancer
  JOURNAL   Breast Cancer Res 9 (4), R54 (2007)
   PUBMED   17697391
  REMARK    GeneRIF: Dysregulated BCoR-L1 expression is associated with breast
            cancer
            Erratum:[Breast Cancer Res. 2008;10(5):406]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL034405.16, Z82208.1,
            KF459400.1 and AL136450.8.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_047298299.1, XP_054183527.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            corepressor that is found tethered to promoter regions by
            DNA-binding proteins. The encoded protein can interact with several
            different class II histone deacetylases to repress transcription.
            Two transcript variants encoding different isoforms have been found
            for this gene. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1429317.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1655
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.1"
     Protein         1..1655
                     /product="BCL-6 corepressor-like protein 1 isoform 2"
                     /note="BCoR-like protein 1"
                     /calculated_mol_wt=174863
     Region          65..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          113..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          <198..636
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          343..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          527..550
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          562..646
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          753..781
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          876..901
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          937..977
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1029
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1033
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5H9F3.2)"
     Region          <1364..>1473
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1366..1397
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1367,1371..1372,1375..1377,1379..1380,1384,1387,
                     1397,1399,1401,1405..1406,1409..1411,1413..1414,1418,1421,
                     1430,1432,1434,1438..1439,1442..1444,1446..1447,1451,1454)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1399..1430
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1432..1461
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1536..1649
                     /region_name="PUFD_like_1"
                     /note="PCGF Ub-like fold discriminator of BCOR-like 1;
                     cd14260"
                     /db_xref="CDD:271223"
     Site            order(1538,1540..1550,1552,1554,1563..1565,1567,
                     1608..1609,1611,1614,1636,1647,1649)
                     /site_type="other"
                     /note="RAWUL domain interface [polypeptide binding]"
                     /db_xref="CDD:271223"
     CDS             1..1655
                     /gene="BCORL1"
                     /gene_synonym="BCoR-L1; CXorf10; SHUVER"
                     /coded_by="NM_001441330.1:265..5232"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="GeneID:63035"
                     /db_xref="HGNC:HGNC:25657"
                     /db_xref="MIM:300688"
ORIGIN      
        1 mistaplysg vhnwtssdri rmcgineerr aplsdeestt gdcqhfgsqe fcvsssfskv
       61 eltavgsgsn argadpdgsa teklghksed kpddpqpkmd yagnvaeaeg llvplsspgd
      121 glklpasdsa easnsradcs wtplntqmsk qvdcspagvk aldsrqgvge kntfilatlg
      181 tgvpvegtlp lvttnfsplp apicppapgs asvphsvpda fqvplsvpap vphsglvpvq
      241 vatsvpapsp plapvpalap appsvptlis dsnplsvsas vlvpvpasap psgpvplsap
      301 apaplsvpvs applaliqap vppsaptlvl apvptpvlap mpastppaap appsvpmptp
      361 tpssgppstp tlipafaptp vpaptpapif tpaptpmpaa tpaaiptsap ipasfslsrv
      421 cfpaaqapam qkvplsfqpg tvltpsqplv yipppscgqp lsvatlpttl gvsstltlpv
      481 lpsylqdrcl pgvlaspelr sypyafsvar pltsdsklvs levnrlpcts psgstttqpa
      541 pdgvpgplad tslvtasakv lptpqpllpa psgssapphp akmpsgteqq tegtsvtfsp
      601 lksppqlere masppecsem pldlssksnr qklplpnqrk tppmpvltpv htsskallst
      661 vlsrsqrttq aaggnvtscl gstsspfvif peivrngdps twvknstali stipgtyvgv
      721 anpvpaslll nkdpnlglnr dprhlpkqep isiidqgepk gtgatcgkkg sqagaegqps
      781 tvkrytpari apglpgcqtk elslwkptgp aniyprcsvn gkptstqvlp vgwspyhqas
      841 llsigissag qltpsqgapi rptsvvsefs gvpslsssea vhglpegqpr pggsfvpeqd
      901 pvtknktcri aakpyeeqvn pvlltlspqt gtlalsvqps ggdirmnqgp eeseshlcsd
      961 stpkmegpqg acglklagdt kpknqvlaty mshelvlatp qnlpkmpelp llphdshpke
     1021 lildvvpssr rgssterpql gsqvdlgrvk mekvdgdvvf nlatcfradg lpvapqrgqa
     1081 evrakagqar vkqesvgvfa cknkwqpddv teslppkkmk cgkekdseeq qlqpqakavv
     1141 rsshrpkcrk lpsdpqestk ksprgasdsg kehngvrgkh khrkptkpes qspgkradsh
     1201 eegslekkak ssfrdfipvv lstrtrsqsd lkarkqktss sqslehrlrn rnlllpnkvq
     1261 gisdspngfl pnnleepacl ensekpsgkr kcktkhmatv seeakgkgrw sqqktrspks
     1321 ptpvkptepc tpsksrsass eeasesptar qippearrli vnknagetll qraarlgykd
     1381 vvlyclqkds edvnhrdnag ytalheacsr gwtdilnill ehganvncsa qdgtrpvhda
     1441 vvndnletiw lllsygadpt latysgqtam klassdtmkr flsdhlsdlq graegdpgvs
     1501 wdfysssvle ekdgfacdll hnppgssdqe gddpmeeddf mfelsdkpll pcynlqvsvs
     1561 rgpcnwflfs dvlkrlklss rifqarfphf eittmpkaef yrqvassqll tpaerpggld
     1621 drsppgsset velvryepdl lrllgsevef qscns
//
LOCUS       NP_001424295             735 aa            linear   PRI 21-NOV-2025
DEFINITION  MAP/microtubule affinity-regulating kinase 3 isoform i [Homo
            sapiens].
ACCESSION   NP_001424295 XP_047287334 XP_054232030
VERSION     NP_001424295.1
DBSOURCE    REFSEQ: accession NM_001437366.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 735)
  AUTHORS   Aparicio-Bautista,D.I., Jimenez-Ortega,R.F., Becerra-Cervera,A.,
            Aquino-Galvez,A., de Leon-Suarez,V.P., Casas-Avila,L., Salmeron,J.,
            Hidalgo-Bravo,A., Rivera-Paredez,B. and Velazquez-Cruz,R.
  TITLE     Interaction between MARK3 (rs11623869), PLCB4 (rs6086746) and
            GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women
  JOURNAL   Front Endocrinol (Lausanne) 15, 1392063 (2024)
   PUBMED   38715801
  REMARK    GeneRIF: Interaction between MARK3 (rs11623869), PLCB4 (rs6086746)
            and GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 735)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 735)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 735)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 735)
  AUTHORS   Li,M.G., Katsura,K., Nomiyama,H., Komaki,K., Ninomiya-Tsuji,J.,
            Matsumoto,K., Kobayashi,T. and Tamura,S.
  TITLE     Regulation of the interleukin-1-induced signaling pathways by a
            novel member of the protein phosphatase 2C family (PP2Cepsilon)
  JOURNAL   J Biol Chem 278 (14), 12013-12021 (2003)
   PUBMED   12556533
REFERENCE   7  (residues 1 to 735)
  AUTHORS   Sun,T.Q., Lu,B., Feng,J.J., Reinhard,C., Jan,Y.N., Fantl,W.J. and
            Williams,L.T.
  TITLE     PAR-1 is a Dishevelled-associated kinase and a positive regulator
            of Wnt signalling
  JOURNAL   Nat Cell Biol 3 (7), 628-636 (2001)
   PUBMED   11433294
REFERENCE   8  (residues 1 to 735)
  AUTHORS   Peng,C.Y., Graves,P.R., Ogg,S., Thoma,R.S., Byrnes,M.J. 3rd, Wu,Z.,
            Stephenson,M.T. and Piwnica-Worms,H.
  TITLE     C-TAK1 protein kinase phosphorylates human Cdc25C on serine 216 and
            promotes 14-3-3 protein binding
  JOURNAL   Cell Growth Differ 9 (3), 197-208 (1998)
   PUBMED   9543386
REFERENCE   9  (residues 1 to 735)
  AUTHORS   Ono,T., Kawabe,T., Sonta,S. and Okamoto,T.
  TITLE     Assignment of MARK3 alias KP78 to human chromosome band 14q32.3 by
            in situ hybridization
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 101-102 (1997)
   PUBMED   9533022
REFERENCE   10 (residues 1 to 735)
  AUTHORS   Meller,N., Liu,Y.C., Collins,T.L., Bonnefoy-Berard,N., Baier,G.,
            Isakov,N. and Altman,A.
  TITLE     Direct interaction between protein kinase C theta (PKC theta) and
            14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition
            of PKC theta translocation and function
  JOURNAL   Mol Cell Biol 16 (10), 5782-5791 (1996)
   PUBMED   8816492
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133367.4 and KF456011.1.
            
            On or before Apr 3, 2025 this sequence version replaced
            XP_047287334.1, XP_054232030.1.
            
            Summary: The protein encoded by this gene is activated by
            phosphorylation and in turn is involved in the phosphorylation of
            tau proteins MAP2 and MAP4. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2120772.1,
                                           SRR14038193.964941.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.32-q32.33"
     Protein         1..735
                     /product="MAP/microtubule affinity-regulating kinase 3
                     isoform i"
                     /EC_number="2.7.11.1"
                     /note="EMK-2; C-TAK1; ELKL motif kinase 2; protein kinase
                     STK10; ser/Thr protein kinase PAR-1; cdc25C-associated
                     protein kinase 1; MAP/microtubule affinity-regulating
                     kinase 3; serine/threonine-protein kinase p78"
                     /calculated_mol_wt=82305
     Region          55..289
                     /region_name="STKc_MARK"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     MAP/microtubule affinity-regulating kinases; cd14072"
                     /db_xref="CDD:270974"
     Site            order(62..66,70,98,114..117,121,123..124,126,159..160,162,
                     164..165,167,177..178,181,194..199,201,231..234,236)
                     /site_type="active"
                     /db_xref="CDD:270974"
     Site            order(62..65,70,98,114..117,121,164..165,167,177..178)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270974"
     Site            order(66,121,123,159..160,162,164,181,195..199,201)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270974"
     Site            177..199
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270974"
     Region          307..349
                     /region_name="UBA_MARK3_4"
                     /note="UBA domain found in MAP/microtubule
                     affinity-regulating kinase MARK3, MARK4, and similar
                     proteins; cd14407"
                     /db_xref="CDD:270590"
     Region          636..733
                     /region_name="MARK1-3_C"
                     /note="C-terminal, kinase associated domain 1 (KA1), a
                     phospholipid binding domain, of microtubule
                     affinity-regulating kinases 1-3; cd12196"
                     /db_xref="CDD:213381"
     Site            order(638,641,711,713..714)
                     /site_type="other"
                     /note="putative phospholipid binding site [chemical
                     binding]"
                     /db_xref="CDD:213381"
     CDS             1..735
                     /gene="MARK3"
                     /gene_synonym="CTAK1; KP78; Par-1a; PAR1A; VIPB"
                     /coded_by="NM_001437366.1:616..2823"
                     /note="isoform i is encoded by transcript variant 9"
                     /db_xref="GeneID:4140"
                     /db_xref="HGNC:HGNC:6897"
                     /db_xref="MIM:602678"
ORIGIN      
        1 mstrtplptv nerdtenhts hgdgrqevts rtsrsgarcr nsiascadeq phignyrllk
       61 tigkgnfakv klarhiltgr elfrevrimk ilnhpnivkl fevietektl ylimeyasgg
      121 evfdylvahg rmkekearsk frqivsavqy chqkrivhrd lkaenlllda dmnikiadfg
      181 fsneftvggk ldtfcgsppy aapelfqgkk ydgpevdvws lgvilytlvs gslpfdgqnl
      241 kelrervlrg kyripfymst dcenllkrfl vlnpikrgtl eqimkdrwin agheedelkp
      301 fvepeldisd qkridimvgm gysqeeiqes lskmkydeit atylllgrks seldasdsss
      361 ssnlslakvr pssdlnnstg qsphhkvqrs vsssqkqrry sdhagpaips vvaypkrsqt
      421 stadsdlked gissrkssgs avggkgiapa spmlgnasnp nkadiperkk sstvpssnta
      481 sggmtrrnty vcserttadr hsviqngken stipdqrtpv asthsissaa tpdrirfprg
      541 tasrstfhgq prerrtatyn gppaspslsh eatplsqtrs rgstnlfskl tskltrrnms
      601 frfikrlpte yerngryegs srnvsaeqkd enkeakprsl rftwsmktts smdpgdmmre
      661 irkvldannc dyeqrerfll fcvhgdghae nlvqwemevc klprlslngv rfkrisgtsi
      721 afkniaskia nelkl
//
LOCUS       NP_001401432             583 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial ribonuclease P catalytic subunit isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_001401432 XP_047287948
VERSION     NP_001401432.1
DBSOURCE    REFSEQ: accession NM_001414503.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Zhang,E., Sun,Q., Zhang,C., Ma,H., Zhang,J., Ding,Y., Wang,G.,
            Jin,C., Jin,C., Fu,Y., Yan,C., Zhu,M., Wang,C., Dai,J., Jin,G.,
            Hu,Z., Shen,H. and Ma,H.
  TITLE     Comprehensive functional interrogation of susceptibility loci in
            GWASs identified KIAA0391 as a novel oncogenic driver via
            regulating pyroptosis in NSCLC
  JOURNAL   Cancer Lett 585, 216646 (2024)
   PUBMED   38262497
  REMARK    GeneRIF: Comprehensive functional interrogation of susceptibility
            loci in GWASs identified KIAA0391 as a novel oncogenic driver via
            regulating pyroptosis in NSCLC.
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Smith,T.B., Rea,A., Thomas,H.B., Thompson,K., Olahova,M.,
            Maroofian,R., Zamani,M., He,L., Sadeghian,S., Galehdari,H.,
            Lotan,N.S., Gilboa,T., Herman,K.C., McCorvie,T.J., Yue,W.W.,
            Houlden,H., Taylor,R.W., Newman,W.G. and O'Keefe,R.T.
  TITLE     Novel homozygous variants in PRORP expand the genotypic spectrum of
            combined oxidative phosphorylation deficiency 54
  JOURNAL   Eur J Hum Genet 31 (10), 1190-1194 (2023)
   PUBMED   37558808
  REMARK    GeneRIF: Novel homozygous variants in PRORP expand the genotypic
            spectrum of combined oxidative phosphorylation deficiency 54.
REFERENCE   3  (residues 1 to 583)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Hochberg,I., Demain,L.A.M., Richer,J., Thompson,K., Urquhart,J.E.,
            Rea,A., Pagarkar,W., Rodriguez-Palmero,A., Schluter,A., Verdura,E.,
            Pujol,A., Quijada-Fraile,P., Amberger,A., Deutschmann,A.J.,
            Demetz,S., Gillespie,M., Belyantseva,I.A., McMillan,H.J.,
            Barzik,M., Beaman,G.M., Motha,R., Ng,K.Y., O'Sullivan,J.,
            Williams,S.G., Bhaskar,S.S., Lawrence,I.R., Jenkinson,E.M.,
            Zambonin,J.L., Blumenfeld,Z., Yalonetsky,S., Oerum,S.,
            Rossmanith,W., Yue,W.W., Zschocke,J., Munro,K.J., Battersby,B.J.,
            Friedman,T.B., Taylor,R.W., O'Keefe,R.T. and Newman,W.G.
  CONSRTM   Genomics England Research Consortium
  TITLE     Bi-allelic variants in the mitochondrial RNase P subunit PRORP
            cause mitochondrial tRNA processing defects and pleiotropic
            multisystem presentations
  JOURNAL   Am J Hum Genet 108 (11), 2195-2204 (2021)
   PUBMED   34715011
  REMARK    GeneRIF: Bi-allelic variants in the mitochondrial RNase P subunit
            PRORP cause mitochondrial tRNA processing defects and pleiotropic
            multisystem presentations.
REFERENCE   5  (residues 1 to 583)
  AUTHORS   Bhatta,A., Dienemann,C., Cramer,P. and Hillen,H.S.
  TITLE     Structural basis of RNA processing by human mitochondrial RNase P
  JOURNAL   Nat Struct Mol Biol 28 (9), 713-723 (2021)
   PUBMED   34489609
  REMARK    GeneRIF: Structural basis of RNA processing by human mitochondrial
            RNase P.
REFERENCE   6  (residues 1 to 583)
  AUTHORS   Alsmadi,O., Muiya,P., Khalak,H., Al-Saud,H., Meyer,B.F.,
            Al-Mohanna,F., Alshahid,M. and Dzimiri,N.
  TITLE     Haplotypes encompassing the KIAA0391 and PSMA6 gene cluster confer
            a genetic link for myocardial infarction and coronary artery
            disease
  JOURNAL   Ann Hum Genet 73 (Pt 5), 475-483 (2009)
   PUBMED   19624571
  REMARK    GeneRIF: Haplotypes in KIAA0391 and PSMA6 genes is a genetic link
            for myocardial infarction and coronary artery disease.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 583)
  AUTHORS   Holzmann,J., Frank,P., Loffler,E., Bennett,K.L., Gerner,C. and
            Rossmanith,W.
  TITLE     RNase P without RNA: identification and functional reconstitution
            of the human mitochondrial tRNA processing enzyme
  JOURNAL   Cell 135 (3), 462-474 (2008)
   PUBMED   18984158
REFERENCE   8  (residues 1 to 583)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   9  (residues 1 to 583)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The NYN domains: novel predicted RNAses with a PIN domain-like fold
  JOURNAL   RNA Biol 3 (1), 18-27 (2006)
   PUBMED   17114934
REFERENCE   10 (residues 1 to 583)
  AUTHORS   Li,T., Faridi,R., Newman,W.G. and Friedman,T.B.
  TITLE     Perrault Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25254289
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL121594.6.
            
            On Nov 29, 2022 this sequence version replaced XP_047287948.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2378110.1,
                                           SRR14038192.79382.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.2"
     Protein         1..583
                     /product="mitochondrial ribonuclease P catalytic subunit
                     isoform 1 precursor"
                     /EC_number="3.1.26.5"
                     /note="mitochondrial ribonuclease P protein 3;
                     mitochondrial RNase P protein 3; mitochondrial RNase P
                     subunit 3; proteinaceous RNase P; mitochondrial
                     ribonuclease P catalytic subunit"
                     /calculated_mol_wt=62099
     transit_peptide 1..45
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O15091.2)"
                     /calculated_mol_wt=5235
     mat_peptide     46..583
                     /product="Mitochondrial ribonuclease P catalytic subunit.
                     /id=PRO_0000050749"
                     /note="propagated from UniProtKB/Swiss-Prot (O15091.2)"
                     /calculated_mol_wt=62099
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15091.2)"
     Region          174..204
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          210..239
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          244..271
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          342..578
                     /region_name="PRORP"
                     /note="Protein-only RNase P; pfam16953"
                     /db_xref="CDD:465320"
     CDS             1..583
                     /gene="PRORP"
                     /gene_synonym="COXPD54; KIAA0391; MRPP3"
                     /coded_by="NM_001414503.1:509..2260"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:9692"
                     /db_xref="HGNC:HGNC:19958"
                     /db_xref="MIM:609947"
ORIGIN      
        1 mtfylfgirs fpklwkspyl glgpghsyvs lfladrcgir nqqrlfslkt mspqntkatn
       61 liakarylrk degsnkqvys vphfflagaa kersqmnsqt edhalapvrn tiqlptqpln
      121 seewdklked lkentgktsf eswiisqmag chssidvaks llawvaaknn givsydllvk
      181 ylylcvfhmq tsevidvfei mkaryktlep rgysllirgl ihsdrwreal llledikkvi
      241 tpskknyndc iqgallhqdv ntawnlyqel lghdivpmle tlkaffdfgk dikddnysnk
      301 lldilsylrn nqlypgesfa hsiktwfesv pgkqwkgqft tvrksgqcsg cgktiesiql
      361 speeyeclkg kimrdvidgg dqyrkttpqe lkrfenfiks rppfdvvidg lnvakmfpkv
      421 resqlllnvv sqlakrnlrl lvlgrkhmlr rssqwsrdem eevqkqascf faddiseddp
      481 fllyatlhsg nhcrfitrdl mrdhkaclpd aktqrlffkw qqghqlaivn rfpgskltfq
      541 rilsydtvvq ttgdswhipy dedlvercsc evptkwlclh qkt
//
LOCUS       NP_001364163             404 aa            linear   PRI 21-NOV-2025
DEFINITION  pleckstrin homology domain-containing family A member 1 isoform 1
            [Homo sapiens].
ACCESSION   NP_001364163
VERSION     NP_001364163.1
DBSOURCE    REFSEQ: accession NM_001377234.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Huang,Q. and Xiang,Y.
  TITLE     Polymorphisms in Selected Genes and Their Association with
            Age-Related Macular Degeneration in a Chinese Population
  JOURNAL   Med Sci Monit 24, 1693-1700 (2018)
   PUBMED   29565837
  REMARK    GeneRIF: investigated the association of PLEKHA1 958A/G,
            polymorphisms with Age-Related Macular Degeneration (AMD) risk.
            PLEKHA1 958A/G polymorphism was associated with a decreased AMD
            risk (additive model: aOR=0.722, 95% CI=0.450-0.979, P=0.019;
            allele model: aOR=0.883, 95% CI=0.736-0.992, P=0.014)
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Kortvely,E. and Ueffing,M.
  TITLE     Gene Structure of the 10q26 Locus: A Clue to Cracking the
            ARMS2/HTRA1 Riddle?
  JOURNAL   Adv Exp Med Biol 854, 23-29 (2016)
   PUBMED   26427389
  REMARK    GeneRIF: Studies indicate that the high-risk allele of the 10q26
            locus encompasses three genes, PLEKHA1, ARMS2, and HTRA1 with high
            linkage disequilibrium.
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Gupta,D., Gupta,V., Singh,V., Chawla,S., Parveen,F., Agrawal,S. and
            Phadke,S.R.
  TITLE     Study of Polymorphisms in CX3CR1, PLEKHA1 and VEGF genes as risk
            factors for age-related macular degeneration in Indian patients
  JOURNAL   Arch Med Res 45 (6), 489-494 (2014)
   PUBMED   25050486
  REMARK    GeneRIF: CX3CR1 (T280M and V249I) and PLEKHA1 (A320T) polymorphisms
            were not found to be associated with age-related macular
            degeneration in an Indian population.
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Hogan,A., Yakubchyk,Y., Chabot,J., Obagi,C., Daher,E., Maekawa,K.
            and Gee,S.H.
  TITLE     The phosphoinositol 3,4-bisphosphate-binding protein TAPP1
            interacts with syntrophins and regulates actin cytoskeletal
            organization
  JOURNAL   J Biol Chem 279 (51), 53717-53724 (2004)
   PUBMED   15485858
  REMARK    GeneRIF: syntrophins regulate the localization of TAPP1, which may
            be important for remodeling the actin cytoskeleton in response to
            growth factor stimulation
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Kimber,W.A., Deak,M., Prescott,A.R. and Alessi,D.R.
  TITLE     Interaction of the protein tyrosine phosphatase PTPL1 with the
            PtdIns(3,4)P2-binding adaptor protein TAPP1
  JOURNAL   Biochem J 376 (Pt 2), 525-535 (2003)
   PUBMED   14516276
  REMARK    GeneRIF: TAPP1 binds to protein tyrosine phosphatase PTPL1.
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Marshall,A.J., Krahn,A.K., Ma,K., Duronio,V. and Hou,S.
  TITLE     TAPP1 and TAPP2 are targets of phosphatidylinositol 3-kinase
            signaling in B cells: sustained plasma membrane recruitment
            triggered by the B-cell antigen receptor
  JOURNAL   Mol Cell Biol 22 (15), 5479-5491 (2002)
   PUBMED   12101241
REFERENCE   8  (residues 1 to 404)
  AUTHORS   Kimber,W.A., Trinkle-Mulcahy,L., Cheung,P.C., Deak,M.,
            Marsden,L.J., Kieloch,A., Watt,S., Javier,R.T., Gray,A.,
            Downes,C.P., Lucocq,J.M. and Alessi,D.R.
  TITLE     Evidence that the tandem-pleckstrin-homology-domain-containing
            protein TAPP1 interacts with Ptd(3,4)P2 and the
            multi-PDZ-domain-containing protein MUPP1 in vivo
  JOURNAL   Biochem J 361 (Pt 3), 525-536 (2002)
   PUBMED   11802782
REFERENCE   9  (residues 1 to 404)
  AUTHORS   Thomas,C.C., Dowler,S., Deak,M., Alessi,D.R. and van Aalten,D.M.
  TITLE     Crystal structure of the phosphatidylinositol
            3,4-bisphosphate-binding pleckstrin homology (PH) domain of tandem
            PH-domain-containing protein 1 (TAPP1): molecular basis of lipid
            specificity
  JOURNAL   Biochem J 358 (Pt 2), 287-294 (2001)
   PUBMED   11513726
REFERENCE   10 (residues 1 to 404)
  AUTHORS   Dowler,S., Currie,R.A., Campbell,D.G., Deak,M., Kular,G.,
            Downes,C.P. and Alessi,D.R.
  TITLE     Identification of pleckstrin-homology-domain-containing proteins
            with novel phosphoinositide-binding specificities
  JOURNAL   Biochem J 351 (Pt 1), 19-31 (2000)
   PUBMED   11001876
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX664700.3 and BX842242.1.
            
            Summary: This gene encodes a pleckstrin homology domain-containing
            adapter protein. The encoded protein is localized to the plasma
            membrane where it specifically binds phosphatidylinositol
            3,4-bisphosphate. This protein may be involved in the formation of
            signaling complexes in the plasma membrane. Polymorphisms in this
            gene are associated with age-related macular degeneration.
            Alternate splicing results in multiple transcript variants. A
            pseudogene of this gene is found on chromosome 5.[provided by
            RefSeq, Sep 2010].
            
            Transcript Variant: This variant (8), as well as variants 1, 2,
            5-7, and 9, encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.154204.1,
                                           SRR14038191.2210855.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154405, SAMN04284274
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..404
                     /product="pleckstrin homology domain-containing family A
                     member 1 isoform 1"
                     /note="tandem PH domain-containing protein 1; pleckstrin
                     homology domain containing, family A (phosphoinositide
                     binding specific) member 1"
                     /calculated_mol_wt=45423
     Region          1..117
                     /region_name="PH1_TAPP1_2"
                     /note="Tandem PH-domain-containing proteins 1 and 2
                     Pleckstrin homology (PH) domain, N-terminal repeat;
                     cd13270"
                     /db_xref="CDD:270089"
     Region          185..298
                     /region_name="PH2_TAPP1_2"
                     /note="Tandem PH-domain-containing proteins 1 and 2
                     Pleckstrin homology (PH) domain, C-terminal repeat;
                     cd13271"
                     /db_xref="CDD:270090"
     Site            order(200,202..203,211,222,232..233,265)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270090"
     Region          291..332
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB21.2)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HB21.2)"
     Region          355..404
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB21.2)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9HB21.2)"
     CDS             1..404
                     /gene="PLEKHA1"
                     /gene_synonym="TAPP1"
                     /coded_by="NM_001377234.1:402..1616"
                     /note="isoform 1 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS7629.1"
                     /db_xref="GeneID:59338"
                     /db_xref="HGNC:HGNC:14335"
                     /db_xref="MIM:607772"
ORIGIN      
        1 mpyvdrqnri cgfldieene nsgkflrryf ildtredsfv wymdnpqnlp sgssrvgaik
       61 ltyiskvsda tklrpkaefc fvmnagmrky flqandqqdl vewvnvlnka ikitvpkqsd
      121 sqpnsdnlsr hgecgkkqvs yrtdivggvp iitptqkeev necgesidrn nlkrsqshlp
      181 yftpkppqds avikagycvk qgavmknwkr ryfqldenti gyfkseleke plrviplkev
      241 hkvqeckqsd immrdnlfei vttsrtfyvq adspeemhsw ikavsgaiva qrgpgrsass
      301 ehppgpsesk hafrptnaat atshstasrs nslvstftme krgfyeslak vkpgnfkvqt
      361 vsprepaskv teqallrpqs kngpqekdcd lvdlddaslp vsdv
//
LOCUS       NP_001389630            1270 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 12 [Homo sapiens].
ACCESSION   NP_001389630 XP_024305347
VERSION     NP_001389630.1
DBSOURCE    REFSEQ: accession NM_001402701.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1270)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1270)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1270)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1270)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1270)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1270)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1270)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1270)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1270)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1270)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            On Apr 22, 2022 this sequence version replaced XP_024305347.1.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.4026806.1,
                                           SRR18074969.3651779.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1270
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1270
                     /product="kinectin isoform 12"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=146061
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          <326..>584
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          480..>1210
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1270
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402701.1:179..3991"
                     /note="isoform 12 is encoded by transcript variant 24"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqdlkqeika
      841 lkeeignvql ekaqqlsits kvqelqnllk gkeeqmntmk avleekekdl antgkwlqdl
      901 qeeneslkah vqevaqhnlk eassasqfee leivlkeken elkrleamlk eresdlsskt
      961 qllqdvqden klfksqieql kqqnyqqass fppheellkv iserekeisg lwneldslkd
     1021 avehqrkknn sygewlhgfe kkakecmagt sgseevkvle hklkeademh tllqleceky
     1081 ksvlaetegi lqklqrsveq eenkwkvkvd eshktikqmq ssftsseqel erlrsenkdi
     1141 enlrrerehl emelekaeme rstyvtevre lkaqlnetlt klrteqnerq kvagdlhkaq
     1201 qsleliqski vkaagdttvi ensdvspete sseketmsvs lnqtvtqlqq llqavnqqlt
     1261 kekehyqvle
//
LOCUS       NP_001425605            1135 aa            linear   PRI 21-NOV-2025
DEFINITION  ras GTPase-activating protein nGAP isoform 6 [Homo sapiens].
ACCESSION   NP_001425605 XP_047290815 XP_054195676
VERSION     NP_001425605.1
DBSOURCE    REFSEQ: accession NM_001438676.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1135)
  AUTHORS   Zhang,Y., Yang,Y., Hu,X., Wei,B., Shen,Q., Shi,C. and Chen,P.
  TITLE     RAS protein activator-like 2 (RASAL2) initiates peritubular
            capillary rarefaction in hypoxic renal interstitial fibrosis
  JOURNAL   Transl Res 269, 14-30 (2024)
   PUBMED   38453052
  REMARK    GeneRIF: RAS protein activator-like 2 (RASAL2) initiates
            peritubular capillary rarefaction in hypoxic renal interstitial
            fibrosis.
REFERENCE   2  (residues 1 to 1135)
  AUTHORS   Singharajkomron,N., Yodsurang,V., Limprasutr,V., Wattanathamsan,O.,
            Iksen,I., Hayakawa,Y. and Pongrakhananon,V.
  TITLE     CAMSAP2 enhances lung cancer cell metastasis by mediating RASAL2
            degradation
  JOURNAL   Life Sci 338, 122391 (2024)
   PUBMED   38159595
  REMARK    GeneRIF: CAMSAP2 enhances lung cancer cell metastasis by mediating
            RASAL2 degradation.
REFERENCE   3  (residues 1 to 1135)
  AUTHORS   Wills,C., Watts,K., Maughan,T.S., Fisher,D., Al-Tassan,N.A.,
            Houlston,R.S., Escott-Price,V. and Cheadle,J.P.
  TITLE     Germline variation in RASAL2 may predict survival in patients with
            RAS-activated colorectal cancer
  JOURNAL   Genes Chromosomes Cancer 62 (6), 332-341 (2023)
   PUBMED   36790221
  REMARK    GeneRIF: Germline variation in RASAL2 may predict survival in
            patients with RAS-activated colorectal cancer.
REFERENCE   4  (residues 1 to 1135)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 1135)
  AUTHORS   Yue,Y., Wu,K., Qian,W., Zhu,Z., Zhang,S., Zhang,W., Zhang,W.,
            Wu,S., Li,L., Wu,Z., Ma,Q., Xie,K. and Wang,Z.
  TITLE     RASAL2 mediated the enhancement of YAP1/TIAM1 signaling promotes
            malignant phenotypes of pancreatic ductal adenocarcinoma
  JOURNAL   Int J Biol Sci 18 (10), 4245-4259 (2022)
   PUBMED   35844783
  REMARK    GeneRIF: RASAL2 mediated the enhancement of YAP1/TIAM1 signaling
            promotes malignant phenotypes of pancreatic ductal adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1135)
  AUTHORS   Melen,E., Himes,B.E., Brehm,J.M., Boutaoui,N., Klanderman,B.J.,
            Sylvia,J.S. and Lasky-Su,J.
  TITLE     Analyses of shared genetic factors between asthma and obesity in
            children
  JOURNAL   J Allergy Clin Immunol 126 (3), 631-7 (2010)
   PUBMED   20816195
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1135)
  AUTHORS   Shibui,T., Kobayashi,T. and Shiratori,M.
  TITLE     Isolation of cross-reacting antigen candidates by mRNA-display
            using a mixed cDNA library
  JOURNAL   Biotechnol Lett 30 (12), 2037-2043 (2008)
   PUBMED   18633578
REFERENCE   8  (residues 1 to 1135)
  AUTHORS   de Chassey,B., Navratil,V., Tafforeau,L., Hiet,M.S., Aublin-Gex,A.,
            Agaugue,S., Meiffren,G., Pradezynski,F., Faria,B.F., Chantier,T.,
            Le Breton,M., Pellet,J., Davoust,N., Mangeot,P.E., Chaboud,A.,
            Penin,F., Jacob,Y., Vidalain,P.O., Vidal,M., Andre,P.,
            Rabourdin-Combe,C. and Lotteau,V.
  TITLE     Hepatitis C virus infection protein network
  JOURNAL   Mol Syst Biol 4, 230 (2008)
   PUBMED   18985028
REFERENCE   9  (residues 1 to 1135)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 1135)
  AUTHORS   Noto,S., Maeda,T., Hattori,S., Inazawa,J., Imamura,M., Asaka,M. and
            Hatakeyama,M.
  TITLE     A novel human RasGAP-like gene that maps within the prostate cancer
            susceptibility locus at chromosome 1q25
  JOURNAL   FEBS Lett 441 (1), 127-131 (1998)
   PUBMED   9877179
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL365357.12 and AL035702.7.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047290815.1, XP_054195676.1.
            
            Summary: This gene encodes a protein that contains the GAP-related
            domain (GRD), a characteristic domain of GTPase-activating proteins
            (GAPs). GAPs function as activators of Ras superfamily of small
            GTPases. The protein encoded by this gene is able to complement the
            defective RasGAP function in a yeast system. Two alternatively
            spliced transcript variants of this gene encoding distinct isoforms
            have been reported. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3941185.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1135
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..1135
                     /product="ras GTPase-activating protein nGAP isoform 6"
                     /note="Ras protein activator like 1; ras GTPase-activating
                     protein nGAP; RASAL2/ACVR1 fusion"
                     /calculated_mol_wt=128032
     Region          1..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Region          36..173
                     /region_name="PH_nGAP"
                     /note="Neuronal growth-associated proteins Pleckstrin
                     homology (PH) domain; cd13373"
                     /db_xref="CDD:270176"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Region          159..298
                     /region_name="C2_SynGAP_like"
                     /note="C2 domain present in Ras GTPase activating protein
                     (GAP) family; cd04013"
                     /db_xref="CDD:175980"
     Region          289..612
                     /region_name="RasGAP_DAB2IP"
                     /note="Ras-GTPase Activating Domain of DAB2IP and similar
                     proteins; cd05136"
                     /db_xref="CDD:213338"
     Site            order(328,365,367,369..370,372,375,379,471,479..480,
                     483..484,487,508,511..512,515,519,521,526..527)
                     /site_type="other"
                     /note="putative RAS interface [polypeptide binding]"
                     /db_xref="CDD:213338"
     Site            369
                     /site_type="other"
                     /note="Arginine finger, crucial for GTP hydrolysis by
                     stabilizing the transition state.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00167; propagated
                     from UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Region          602..1078
                     /region_name="DUF3498"
                     /note="Domain of unknown function (DUF3498); pfam12004"
                     /db_xref="CDD:463427"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Site            656
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Region          677..697
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Region          744..775
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Region          796..862
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Site            857
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UJF2.2)"
     Region          903..946
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJF2.2)"
     CDS             1..1135
                     /gene="RASAL2"
                     /gene_synonym="NGAP"
                     /coded_by="NM_001438676.1:146..3553"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:9462"
                     /db_xref="HGNC:HGNC:9874"
                     /db_xref="MIM:606136"
ORIGIN      
        1 mqtpevpaer sprrrsisgt stsekpnsmd tantspfkvp gffskrlkgs ikrtksqskl
       61 drntsfrlps lrstddrsrg lpklkesrsh esllspcstv ecldlgrgep vsvkplhssi
      121 lgqdfcfevt ylsgskcfsc nsaserdkwm enlrrtvqpn kdncrraenv lrlwiieakd
      181 lapkkkyfce lclddtlfar ttsktkadni fwgehfeffs lpplhsitvh iykdvekkkk
      241 kdknnyvglv niptasvtgr qfvekwypvs tptpnkgktg gpsiriksrf qtitilpmeq
      301 ykefaefvts nytmlcsvle pvisvrnkee lacalvhilq stgrakdflt dlvmsevdrc
      361 gehdvlifre ntiatksiee ylklvgqqyl hdalgefika lyesdencev dpskcsssel
      421 idhqsnlkmc celafckiin sycvfprelk evfaswkqqc lnrgkqdise rlisaslflr
      481 flcpaimsps lfnlmqeypd drtsrtltli akviqnlanf akfgnkeeym afmndflehe
      541 wggmkrflle isnpdtisnt pgfdgyidlg relsvlhsll wevvsqldka tvaklgplpr
      601 vladitkslt nptpiqqqlr rftehnsspn vsgslssglq kifedptdsd lhklkspsqd
      661 ntdsyfrgkt lllvqqassq smtysekder esslpngrsv slmdlqdtha aqvehasvml
      721 dvpirltgsq lsitqvasik qlretqstpq sapqvrrplh palnqpgglq plsfqnpvyh
      781 lnnpipampk asidsslenl stassrsqsn sedfklsgps nssmedftkr stqsedfsrr
      841 htvpdrhipl alprqnstgq aqirkvdqgg lgarakapps lphsaslrst gsmsvvsaal
      901 vaepvqngsr srqqssssre spvpkvraiq rqqtqqvqsp vdsatmspve rtaawvlnng
      961 qyeedveete qnldeakhae kyeqeitklk erlrvssrrl eeyerrllvq eqqmqkllle
     1021 ykarledsee rlrrqqeekd sqmksiisrl maveeelkkd haemqavida kqkiidaqvi
     1081 ngdeiiqtgk tdrvpgfsqh qtderadpse gavqhagpqw hlphqphqaf hhgew
//
LOCUS       NP_001400232             224 aa            linear   PRI 21-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 12 [Homo sapiens].
ACCESSION   NP_001400232 XP_016868571
VERSION     NP_001400232.1
DBSOURCE    REFSEQ: accession NM_001413303.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 224)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 224)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 224)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 224)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 224)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            On Oct 31, 2022 this sequence version replaced XP_016868571.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.898482.1,
                                           SRR1803613.141058.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..224
                     /product="RNA-binding Raly-like protein isoform 12"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=24742
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     CDS             1..224
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_001413303.1:329..1003"
                     /note="isoform 12 is encoded by transcript variant 30"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly sgyvfdydyy
      121 rddfynrlfd yhgrvppppr aviplkrprv avtttrrgkg vfsmkggsrs tasgstgskl
      181 ksdelqtikk eltqiktkid sllgrlekie kqqkaeavst dkvi
//
LOCUS       NP_001352358             845 aa            linear   PRI 21-NOV-2025
DEFINITION  TRPM8 channel-associated factor 2 isoform A [Homo sapiens].
ACCESSION   NP_001352358
VERSION     NP_001352358.2
DBSOURCE    REFSEQ: accession NM_001365429.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 845)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 845)
  AUTHORS   Yun,D., Liang,J., Wang,X., Fan,J., Wang,X., Li,J., Ren,X., Liu,J.,
            Ren,X., Zhang,H., Shang,G., Jin,W., Chen,L., Li,T., Zhang,C., Yu,S.
            and Yang,X.
  TITLE     TCAF2 drives glioma cellular migratory/invasion properties through
            STAT3 signaling
  JOURNAL   Mol Cell Biochem 479 (7), 1801-1815 (2024)
   PUBMED   38019450
  REMARK    GeneRIF: TCAF2 drives glioma cellular migratory/invasion properties
            through STAT3 signaling.
REFERENCE   3  (residues 1 to 845)
  AUTHORS   Li,Y., Li,J., Chen,H., Lu,B., Lu,F., Chen,H., Liu,H. and Qian,C.
  TITLE     TCAF2 is associated with the immune microenvironment, promotes
            pathogenesis, and impairs prognosis in glioma
  JOURNAL   Gene 883, 147667 (2023)
   PUBMED   37506986
  REMARK    GeneRIF: TCAF2 is associated with the immune microenvironment,
            promotes pathogenesis, and impairs prognosis in glioma.
REFERENCE   4  (residues 1 to 845)
  AUTHORS   Li,X., Qi,Q., Li,Y., Miao,Q., Yin,W., Pan,J., Zhao,Z., Chen,X.,
            Yang,F., Zhou,X., Huang,M., Wang,C., Deng,L., Huang,D., Qi,M.,
            Fan,S., Zhang,Y., Qiu,S., Deng,W., Liu,T., Chen,M., Ye,W. and
            Zhang,D.
  TITLE     TCAF2 in Pericytes Promotes Colorectal Cancer Liver Metastasis via
            Inhibiting Cold-Sensing TRPM8 Channel
  JOURNAL   Adv Sci (Weinh) 10 (30), e2302717 (2023)
   PUBMED   37635201
  REMARK    GeneRIF: TCAF2 in Pericytes Promotes Colorectal Cancer Liver
            Metastasis via Inhibiting Cold-Sensing TRPM8 Channel.
REFERENCE   5  (residues 1 to 845)
  AUTHORS   Hsieh,P., Dang,V., Vollger,M.R., Mao,Y., Huang,T.H., Dishuck,P.C.,
            Baker,C., Cantsilieris,S., Lewis,A.P., Munson,K.M., Sorensen,M.,
            Welch,A.E., Underwood,J.G. and Eichler,E.E.
  TITLE     Evidence for opposing selective forces operating on human-specific
            duplicated TCAF genes in Neanderthals and humans
  JOURNAL   Nat Commun 12 (1), 5118 (2021)
   PUBMED   34433829
  REMARK    GeneRIF: Evidence for opposing selective forces operating on
            human-specific duplicated TCAF genes in Neanderthals and humans.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 845)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 845)
  AUTHORS   Gkika,D., Lemonnier,L., Shapovalov,G., Gordienko,D., Poux,C.,
            Bernardini,M., Bokhobza,A., Bidaux,G., Degerny,C., Verreman,K.,
            Guarmit,B., Benahmed,M., de Launoit,Y., Bindels,R.J., Fiorio Pla,A.
            and Prevarskaya,N.
  TITLE     TRP channel-associated factors are a novel protein family that
            regulates TRPM8 trafficking and activity
  JOURNAL   J Cell Biol 208 (1), 89-107 (2015)
   PUBMED   25559186
  REMARK    GeneRIF: Report novel TRP channel-associated factors that modulate
            TRPM8 activity.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073264.5 and AC106862.3.
            
            On Apr 25, 2025 this sequence version replaced NP_001352358.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1098684.1,
                                           SRR14372080.2659376.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..845
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q35"
     Protein         1..845
                     /product="TRPM8 channel-associated factor 2 isoform A"
                     /note="family with sequence similarity 139, member A;
                     protein FAM115C; family with sequence similarity 115,
                     member C; TRP channel-associated factor 2"
                     /calculated_mol_wt=91877
     Region          522..632
                     /region_name="M60-like_N"
                     /note="N-terminal domain of M60-like peptidases;
                     pfam17291"
                     /db_xref="CDD:435844"
     Region          633..>835
                     /region_name="Peptidase_M60"
                     /note="Peptidase M60, enhancin and enhancin-like;
                     pfam13402"
                     /db_xref="CDD:433178"
     CDS             1..845
                     /gene="TCAF2"
                     /gene_synonym="FAM115C; FAM139A; GATD9; GATD9B"
                     /coded_by="NM_001365429.2:62..2599"
                     /note="isoform A is encoded by transcript variant 7"
                     /db_xref="GeneID:285966"
                     /db_xref="HGNC:HGNC:26878"
                     /db_xref="MIM:616252"
ORIGIN      
        1 matiaaaafe almdgvtcwd vprgpipsel lligeaafpv mvndkgqvli aassygrgrl
       61 vvvshegyls htglapflln avswlcpcpg apvgvhpsla plvnilqdag leaqvkpepg
      121 eplgvycina yndtltatli qfvkhgggll iggqawywas qhgpdkvlsr fpgnkvtsva
      181 gvyftdtygd rdrfkvskkv pkiplhvryg edvrqdqqql legiseldir tggvpsqllv
      241 hgalafplgl daslncflaa ahygrgrvvl aahecllcap kmgpfllnav rwlargqtgk
      301 vgvntnlkdl cpllsehglq cslephlnsd lcvycckays dkeakqlqef vaegggllig
      361 gqawwwasqn pghcplagfp gniilncfgl silpqtlkag cfpvptpemr syhfrkalsq
      421 fqailnheng nleksclakl rvdgaaflqi paegvpayis lhrllrkmlr gsglpavsre
      481 npvasdsyea avlslatgla hsgtdcsqla qglgtwtcss slypskhpit veinginpgn
      541 ndcwvstgly llegqnaevs lseaaasagl rvqigchtdd ltkarklsra pvvthqcwmd
      601 rtersvsclw ggllyvivpk gsqlgpvpvt irgavpapyy klgktsleew krqmqenlap
      661 wgelatdnii ltvpttnlqa lkdpepvlrl wdemmqavar laaepfpfrr perivadvqi
      721 sagwmhsgyp imchlesvke iinemdmrsr gvwgpihelg hnqqrhgwef pphtteatcn
      781 lwsvyvhetv lgipraqahe alsppererr ikahlgkgap lcdwnvwtal etylqvlsrn
      841 sgrrg
//
LOCUS       NP_001417997            1240 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphorylase b kinase regulatory subunit alpha, skeletal muscle
            isoform isoform 4 [Homo sapiens].
ACCESSION   NP_001417997
VERSION     NP_001417997.1
DBSOURCE    REFSEQ: accession NM_001431068.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1240)
  AUTHORS   Yang,X., Zhu,M., Lu,X., Wang,Y. and Xiao,J.
  TITLE     Architecture and activation of human muscle phosphorylase kinase
  JOURNAL   Nat Commun 15 (1), 2719 (2024)
   PUBMED   38548794
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1240)
  AUTHORS   Bisciglia,M., Froissart,R., Bedat-Millet,A.L., Romero,N.B.,
            Pettazzoni,M., Hogrel,J.Y., Petit,F.M. and Stojkovic,T.
  TITLE     A novel PHKA1 mutation associating myopathy and cognitive
            impairment: Expanding the spectrum of phosphorylase kinase b (PhK)
            deficiency
  JOURNAL   J Neurol Sci 424, 117391 (2021)
   PUBMED   33799212
  REMARK    GeneRIF: A novel PHKA1 mutation associating myopathy and cognitive
            impairment: Expanding the spectrum of phosphorylase kinase b (PhK)
            deficiency.
REFERENCE   3  (residues 1 to 1240)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1240)
  AUTHORS   Preisler,N., Orngreen,M.C., Echaniz-Laguna,A., Laforet,P.,
            Lonsdorfer-Wolf,E., Doutreleau,S., Geny,B., Akman,H.O., Dimauro,S.
            and Vissing,J.
  TITLE     Muscle phosphorylase kinase deficiency: a neutral metabolic variant
            or a disease?
  JOURNAL   Neurology 78 (4), 265-268 (2012)
   PUBMED   22238410
  REMARK    GeneRIF: muscle PHKA deficiency may present as an almost
            asymptomatic condition, despite a mild impairment of muscle
REFERENCE   5  (residues 1 to 1240)
  AUTHORS   Echaniz-Laguna,A., Akman,H.O., Mohr,M., Tranchant,C.,
            Talmant-Verbist,V., Rolland,M.O. and Dimauro,S.
  TITLE     Muscle phosphorylase b kinase deficiency revisited
  JOURNAL   Neuromuscul Disord 20 (2), 125-127 (2010)
   PUBMED   20080404
REFERENCE   6  (residues 1 to 1240)
  AUTHORS   Gossen,M., Wullrich,A. and Kilimann,M.W.
  TITLE     Dinucleotide repeat polymorphism within the PHKA1 gene at Xq12-q13
  JOURNAL   Hum Genet 95 (4), 469-470 (1995)
   PUBMED   7705849
REFERENCE   7  (residues 1 to 1240)
  AUTHORS   Wehner,M., Clemens,P.R., Engel,A.G. and Kilimann,M.W.
  TITLE     Human muscle glycogenosis due to phosphorylase kinase deficiency
            associated with a nonsense mutation in the muscle isoform of the
            alpha subunit
  JOURNAL   Hum Mol Genet 3 (11), 1983-1987 (1994)
   PUBMED   7874115
REFERENCE   8  (residues 1 to 1240)
  AUTHORS   Herbert,M., Goldstein,J.L., Rehder,C., Austin,S., Kishnani,P.S. and
            Bali,D.S.
  TITLE     Phosphorylase Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21634085
REFERENCE   9  (residues 1 to 1240)
  AUTHORS   Meyer,H.E., Meyer,G.F., Dirks,H. and Heilmeyer,L.M. Jr.
  TITLE     Localization of phosphoserine residues in the alpha subunit of
            rabbit skeletal muscle phosphorylase kinase
  JOURNAL   Eur J Biochem 188 (2), 367-376 (1990)
   PUBMED   2108025
REFERENCE   10 (residues 1 to 1240)
  AUTHORS   Francke,U., Darras,B.T., Zander,N.F. and Kilimann,M.W.
  TITLE     Assignment of human genes for phosphorylase kinase subunits alpha
            (PHKA) to Xq12-q13 and beta (PHKB) to 16q12-q13
  JOURNAL   Am J Hum Genet 45 (2), 276-282 (1989)
   PUBMED   2757032
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC240504.3, BX295541.1 and
            BX295542.1.
            
            Summary: Phosphorylase kinase is a polymer of 16 subunits, four
            each of alpha, beta, gamma and delta. The alpha subunit includes
            the skeletal muscle and hepatic isoforms, and the skeletal muscle
            isoform is encoded by this gene. The beta subunit is the same in
            both the muscle and hepatic isoforms, and encoded by one gene. The
            gamma subunit also includes the skeletal muscle and hepatic
            isoforms, which are encoded by two different genes. The delta
            subunit is a calmodulin and can be encoded by three different
            genes. The gamma subunits contain the active site of the enzyme,
            whereas the alpha and beta subunits have regulatory functions
            controlled by phosphorylation. The delta subunit mediates the
            dependence of the enzyme on calcium concentration. Mutations in
            this gene cause glycogen storage disease type 9D, also known as
            X-linked muscle glycogenosis. Alternatively spliced transcript
            variants encoding different isoforms have been identified in this
            gene. A pseudogene has been found on chromosome 1.[provided by
            RefSeq, Feb 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1971014.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1240
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..1240
                     /product="phosphorylase b kinase regulatory subunit alpha,
                     skeletal muscle isoform isoform 4"
                     /EC_number="2.7.11.19"
                     /note="phosphorylase kinase, alpha 1 (muscle), muscle
                     glycogenosis; phosphorylase kinase alpha M subunit"
                     /calculated_mol_wt=138924
     Region          8..>439
                     /region_name="Glyco_hydro_15"
                     /note="Glycosyl hydrolases family 15; pfam00723"
                     /db_xref="CDD:395586"
     Site            629
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64649; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Site            735
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Site            758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Region          <804..922
                     /region_name="Bac_rhamnosid6H"
                     /note="Bacterial alpha-L-rhamnosidase 6 hairpin
                     glycosidase domain; cl46875"
                     /db_xref="CDD:481215"
     Region          810..840
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P46020.2)"
     Site            972
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46020.2)"
     Site            981
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Site            985
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46020.2)"
     Site            1007
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P18688; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Site            1018
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:P18688; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Site            1020
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P18688; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Site            1023
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P18688; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     Region          1063..1103
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P46020.2)"
     Region          <1077..>1151
                     /region_name="KPBB_C"
                     /note="Phosphorylase b kinase C-terminal domain;
                     pfam19292"
                     /db_xref="CDD:437124"
     Site            1130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64649; propagated from
                     UniProtKB/Swiss-Prot (P46020.2)"
     CDS             1..1240
                     /gene="PHKA1"
                     /gene_synonym="PHKA"
                     /coded_by="NM_001431068.1:427..4149"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:5255"
                     /db_xref="HGNC:HGNC:8925"
                     /db_xref="MIM:311870"
ORIGIN      
        1 mrsrsnsgvr ldgyarlvqq tilchqnpvt gllpasydqk dawvrdnvys ilavwglgla
       61 yrknadrded kakayeleqs vvklmrgllh cmirqvdkve sfkysqstkd slhakyntkt
      121 catvvgddqw ghlqldatsv yllflaqmta sglhiihsld evnfiqnlvf yieaayktad
      181 fgiwergdkt nqgiselnas svgmakaale aldeldlfgv kggpqsvihv ladevqhcqs
      241 ilnsllpras tskevdasll svvsfpafav edsqlveltk qeiitklqgr ygccrflrdg
      301 yktpkedpnr lyyepaelkl feniecewpl fwtyfildgv fsgnaeqvqe ykealeavli
      361 kgkngvpllp elysvppdrv deeyqnphtv drvpmgklph mwgqslyilg slmaegflap
      421 geidplnrrf stvpkpdvvv qvsilaetee iktilkdkgi yvetiaevyp irvqparils
      481 hiysslgcnn rmklsgrpyr hmgvlgtskl ydirktiftf tpqfidqqqf ylaldnkmiv
      541 emlrtdlsyl csrwrmtgqp titfpishsm ldedgtslns silaalrkmq dgyfggarvq
      601 tgklsefltt sccthlsfmd pgpegklyse dyddnydyle sgnwmndyds tsharcgdev
      661 aryldhllah taphpklapt sqkggldrfq aavqttcdlm slvtkakelh vqnvhmylpt
      721 klfqasrpsf nlldsphprq enqvpsvrve ihlprdqsge vdfkalvlql ketsslqeqa
      781 dilymlytmk gpdwntelyn ersatvrell telygkvgei rhwgliryis gilrkkveal
      841 deactdllsh qkhltvglpp eprektisap lpyealtqli deasegdmsi siltqeimvy
      901 lamymrtqpg lfaemfrlri gliiqvmate lahslrcsae eateglmnls psamknllhh
      961 ilsgkefgve rsvrptdsnv spaisiheig avgatktert gimqlkseik qvefrrlsis
     1021 aesqsngghp lgidlmspsf mspgtsmtps sgsfpsaydq qsskdsrqgq wqrrrrldga
     1081 lnrvpvgfyq kvwkvlqkch glsvegfvlp ssttremtpg eikfsvhves vlnrvpqpey
     1141 rqllveailv ltmladieih sigsiiavek ivhiandlfl qeqktlgadd tmlakdpasg
     1201 ictllydsap sgrfgtmtyl skaaatyvqe flphsicamq
//
LOCUS       NP_001400671             952 aa            linear   PRI 21-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform e [Homo sapiens].
ACCESSION   NP_001400671
VERSION     NP_001400671.1
DBSOURCE    REFSEQ: accession NM_001413742.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 952)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 952)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 952)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 952)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 952)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 952)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 952)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 952)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 952)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 952)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3170730.1,
                                           SRR18074969.2526069.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2155974
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..952
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..952
                     /product="polyhomeotic-like protein 1 isoform e"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=100036
     Region          <422..618
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          776..883
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          883..951
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(901..902,936..937,940..941,944)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(912..916,918..919,922..923,927,932)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..952
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_001413742.1:157..3015"
                     /note="isoform e is encoded by transcript variant 6"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq asinlattsa aqlisrsqsv
      121 sspsattltq svllgnttsp plnqsqaqmy lrvqnlavrn qqasaqgpqm qgstqkaipp
      181 gaspvsslsq assqalavaq assgatnqsl nlsqagggsg nsipgsmgpg gggqahgglg
      241 qlpssgmggg scprkgtgvv qplpaaqtvt vsqgsqteae saaakkaead gsgqqnvgmn
      301 ltrtatpaps qtlissatyt qiqphsliqq qqqihlqqkq vviqqqiaih hqqqfqhrqs
      361 qllhtathlq laqqqqqqqq qqqqqqqpqa ttltapqppq vpptqqvpps qsqqqaqtlv
      421 vqpmlqsspl slppdaapkp pipiqskppv apikppqlga akmsaaqqpp phipvqvvgt
      481 rqpgtaqaqa lglaqlaaav ptsrgmpgtv qsgqahlass ppssqapgal qecpptlapg
      541 mtlapvqgta hvvkggatts spvvaqvpaa fymqsvhlpg kpqtlavkrk adseeerddv
      601 stlgsmlpak aspvaespkv mdeksslgek aesvanvnan tpsselvalt papsvppptl
      661 amvsrqmgds kppqaivkpq ilthiiegfv iqegaepfpv gcsqllkese kplqtglptg
      721 ltenqsggpl gvdspsaeld kkanllkcey cgkyapaeqf rgskrfcsmt cakrynvscs
      781 hqfrlkrkkm kefqeanyar vrrrgprrss sdiarakiqg kchrgqedss rgsdnssyde
      841 alsptspgpl svraghgerd lgnpntappt pelhginpvf lssnpsrwsv eevyefiasl
      901 qgcqeiaeef rsqeidgqal lllkeehlms amniklgpal kicakinvlk et
//
LOCUS       NP_001397759             157 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA replication complex GINS protein PSF1 isoform 2 [Homo sapiens].
ACCESSION   NP_001397759 XP_047296582
VERSION     NP_001397759.1
DBSOURCE    REFSEQ: accession NM_001410830.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 157)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 157)
  AUTHORS   Zhu,W., Wu,C., Liu,Z., Zhao,S. and Huang,J.
  TITLE     OTU deubiquitinase, ubiquitin aldehyde binding 2 (OTUB2) modulates
            the stemness feature, chemoresistance, and epithelial-mesenchymal
            transition of colon cancer via regulating GINS complex subunit 1
            (GINS1) expression
  JOURNAL   Cell Commun Signal 22 (1), 420 (2024)
   PUBMED   39210373
  REMARK    GeneRIF: OTU deubiquitinase, ubiquitin aldehyde binding 2 (OTUB2)
            modulates the stemness feature, chemoresistance, and
            epithelial-mesenchymal transition of colon cancer via regulating
            GINS complex subunit 1 (GINS1) expression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 157)
  AUTHORS   Fu,Q., Zheng,H., Wang,X., Tang,F., Yu,H., Wang,H., Wan,Z.,
            Zheng,Z., Yang,Z., Liu,T. and Peng,J.
  TITLE     GINS1 promotes the initiation and progression of bladder cancer by
            activating the AKT/mTOR/c-Myc signaling pathway
  JOURNAL   Exp Cell Res 440 (1), 114125 (2024)
   PUBMED   38880324
  REMARK    GeneRIF: GINS1 promotes the initiation and progression of bladder
            cancer by activating the AKT/mTOR/c-Myc signaling pathway.
REFERENCE   4  (residues 1 to 157)
  AUTHORS   Liang,J., Yao,N., Deng,B., Li,J., Jiang,Y., Liu,T., Hu,Y., Cao,M.
            and Hong,J.
  TITLE     GINS1 promotes ZEB1-mediated epithelial-mesenchymal transition and
            tumor metastasis via beta-catenin signaling in hepatocellular
            carcinoma
  JOURNAL   J Cell Physiol 239 (5), e31237 (2024)
   PUBMED   38468464
  REMARK    GeneRIF: GINS1 promotes ZEB1-mediated epithelial-mesenchymal
            transition and tumor metastasis via beta-catenin signaling in
            hepatocellular carcinoma.
REFERENCE   5  (residues 1 to 157)
  AUTHORS   Ren,X., Shen,L. and Gao,S.
  TITLE     Transcription Factor E2F1 Enhances Hepatocellular Carcinoma Cell
            Proliferation and Stemness by Activating GINS1
  JOURNAL   J Environ Pathol Toxicol Oncol 43 (1), 79-90 (2024)
   PUBMED   37824372
  REMARK    GeneRIF: Transcription Factor E2F1 Enhances Hepatocellular
            Carcinoma Cell Proliferation and Stemness by Activating GINS1.
REFERENCE   6  (residues 1 to 157)
  AUTHORS   De Falco,M., Ferrari,E., De Felice,M., Rossi,M., Hubscher,U. and
            Pisani,F.M.
  TITLE     The human GINS complex binds to and specifically stimulates human
            DNA polymerase alpha-primase
  JOURNAL   EMBO Rep 8 (1), 99-103 (2007)
   PUBMED   17170760
REFERENCE   7  (residues 1 to 157)
  AUTHORS   Hayashi,R., Arauchi,T., Tategu,M., Goto,Y. and Yoshida,K.
  TITLE     A combined computational and experimental study on the
            structure-regulation relationships of putative mammalian DNA
            replication initiator GINS
  JOURNAL   Genomics Proteomics Bioinformatics 4 (3), 156-164 (2006)
   PUBMED   17127213
  REMARK    GeneRIF: expression of mammalian GINS is regulated by
            17beta-Estradiol-stimulated estrogen receptor alpha, and PSF3 acts
            as a gene responsive to transcription factor E2F1
REFERENCE   8  (residues 1 to 157)
  AUTHORS   Ueno,M., Itoh,M., Kong,L., Sugihara,K., Asano,M. and Takakura,N.
  TITLE     PSF1 is essential for early embryogenesis in mice
  JOURNAL   Mol Cell Biol 25 (23), 10528-10532 (2005)
   PUBMED   16287864
REFERENCE   9  (residues 1 to 157)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   10 (residues 1 to 157)
  AUTHORS   Hoja,M.R., Wahlestedt,C. and Hoog,C.
  TITLE     A visual intracellular classification strategy for uncharacterized
            human proteins
  JOURNAL   Exp Cell Res 259 (1), 239-246 (2000)
   PUBMED   10942595
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL353812.13 and AL031672.13.
            
            On Aug 16, 2022 this sequence version replaced XP_047296582.1.
            
            Summary: The yeast heterotetrameric GINS complex is made up of Sld5
            (GINS4; MIM 610611), Psf1, Psf2 (GINS2; MIM 610609), and Psf3
            (GINS3; MIM 610610). The formation of the GINS complex is essential
            for the initiation of DNA replication in yeast and Xenopus egg
            extracts (Ueno et al., 2005 [PubMed 16287864]).[supplied by OMIM,
            Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2877603.1,
                                           SRR14038193.3828289.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..157
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.21"
     Protein         1..157
                     /product="DNA replication complex GINS protein PSF1
                     isoform 2"
                     /note="DNA replication complex GINS protein PSF1; partner
                     of sld five-1; GINS complex subunit 1 (Psf1 homolog)"
                     /calculated_mol_wt=18276
     Region          3..119
                     /region_name="GINS_A_psf1"
                     /note="Alpha-helical domain of GINS complex protein Psf1;
                     cd11710"
                     /db_xref="CDD:212548"
     Site            order(30,33,80,84,88..89,106,109,111,113..119)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:212548"
     Region          110..155
                     /region_name="GINS_B_Psf1"
                     /note="beta-strand (B) domain of GINS complex protein
                     Psf1; cd21696"
                     /db_xref="CDD:412032"
     Site            order(110,112,119,124,126..127,131,133..139,141,154)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:412032"
     CDS             1..157
                     /gene="GINS1"
                     /gene_synonym="IMD55; PSF1"
                     /coded_by="NM_001410830.1:149..622"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS93022.1"
                     /db_xref="GeneID:9837"
                     /db_xref="HGNC:HGNC:28980"
                     /db_xref="MIM:610608"
ORIGIN      
        1 mfcekameli relhrapegq lpafnedglr qvleemkaly eqnqsdvnea ksggrsdlip
       61 tikfrhcsll rnrrctvayl ydrllriral rweygsvlpn alrfhmaaee vrclkdygef
      121 evddgtsvll kknsqhflpr wkceqlirqg vlehils
//
LOCUS       NP_001397760             111 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA replication complex GINS protein PSF1 isoform 3 [Homo sapiens].
ACCESSION   NP_001397760 XP_047296583
VERSION     NP_001397760.1
DBSOURCE    REFSEQ: accession NM_001410831.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 111)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 111)
  AUTHORS   Zhu,W., Wu,C., Liu,Z., Zhao,S. and Huang,J.
  TITLE     OTU deubiquitinase, ubiquitin aldehyde binding 2 (OTUB2) modulates
            the stemness feature, chemoresistance, and epithelial-mesenchymal
            transition of colon cancer via regulating GINS complex subunit 1
            (GINS1) expression
  JOURNAL   Cell Commun Signal 22 (1), 420 (2024)
   PUBMED   39210373
  REMARK    GeneRIF: OTU deubiquitinase, ubiquitin aldehyde binding 2 (OTUB2)
            modulates the stemness feature, chemoresistance, and
            epithelial-mesenchymal transition of colon cancer via regulating
            GINS complex subunit 1 (GINS1) expression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 111)
  AUTHORS   Fu,Q., Zheng,H., Wang,X., Tang,F., Yu,H., Wang,H., Wan,Z.,
            Zheng,Z., Yang,Z., Liu,T. and Peng,J.
  TITLE     GINS1 promotes the initiation and progression of bladder cancer by
            activating the AKT/mTOR/c-Myc signaling pathway
  JOURNAL   Exp Cell Res 440 (1), 114125 (2024)
   PUBMED   38880324
  REMARK    GeneRIF: GINS1 promotes the initiation and progression of bladder
            cancer by activating the AKT/mTOR/c-Myc signaling pathway.
REFERENCE   4  (residues 1 to 111)
  AUTHORS   Liang,J., Yao,N., Deng,B., Li,J., Jiang,Y., Liu,T., Hu,Y., Cao,M.
            and Hong,J.
  TITLE     GINS1 promotes ZEB1-mediated epithelial-mesenchymal transition and
            tumor metastasis via beta-catenin signaling in hepatocellular
            carcinoma
  JOURNAL   J Cell Physiol 239 (5), e31237 (2024)
   PUBMED   38468464
  REMARK    GeneRIF: GINS1 promotes ZEB1-mediated epithelial-mesenchymal
            transition and tumor metastasis via beta-catenin signaling in
            hepatocellular carcinoma.
REFERENCE   5  (residues 1 to 111)
  AUTHORS   Ren,X., Shen,L. and Gao,S.
  TITLE     Transcription Factor E2F1 Enhances Hepatocellular Carcinoma Cell
            Proliferation and Stemness by Activating GINS1
  JOURNAL   J Environ Pathol Toxicol Oncol 43 (1), 79-90 (2024)
   PUBMED   37824372
  REMARK    GeneRIF: Transcription Factor E2F1 Enhances Hepatocellular
            Carcinoma Cell Proliferation and Stemness by Activating GINS1.
REFERENCE   6  (residues 1 to 111)
  AUTHORS   De Falco,M., Ferrari,E., De Felice,M., Rossi,M., Hubscher,U. and
            Pisani,F.M.
  TITLE     The human GINS complex binds to and specifically stimulates human
            DNA polymerase alpha-primase
  JOURNAL   EMBO Rep 8 (1), 99-103 (2007)
   PUBMED   17170760
REFERENCE   7  (residues 1 to 111)
  AUTHORS   Hayashi,R., Arauchi,T., Tategu,M., Goto,Y. and Yoshida,K.
  TITLE     A combined computational and experimental study on the
            structure-regulation relationships of putative mammalian DNA
            replication initiator GINS
  JOURNAL   Genomics Proteomics Bioinformatics 4 (3), 156-164 (2006)
   PUBMED   17127213
  REMARK    GeneRIF: expression of mammalian GINS is regulated by
            17beta-Estradiol-stimulated estrogen receptor alpha, and PSF3 acts
            as a gene responsive to transcription factor E2F1
REFERENCE   8  (residues 1 to 111)
  AUTHORS   Ueno,M., Itoh,M., Kong,L., Sugihara,K., Asano,M. and Takakura,N.
  TITLE     PSF1 is essential for early embryogenesis in mice
  JOURNAL   Mol Cell Biol 25 (23), 10528-10532 (2005)
   PUBMED   16287864
REFERENCE   9  (residues 1 to 111)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   10 (residues 1 to 111)
  AUTHORS   Hoja,M.R., Wahlestedt,C. and Hoog,C.
  TITLE     A visual intracellular classification strategy for uncharacterized
            human proteins
  JOURNAL   Exp Cell Res 259 (1), 239-246 (2000)
   PUBMED   10942595
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL353812.13 and AL031672.13.
            
            On Aug 16, 2022 this sequence version replaced XP_047296583.1.
            
            Summary: The yeast heterotetrameric GINS complex is made up of Sld5
            (GINS4; MIM 610611), Psf1, Psf2 (GINS2; MIM 610609), and Psf3
            (GINS3; MIM 610610). The formation of the GINS complex is essential
            for the initiation of DNA replication in yeast and Xenopus egg
            extracts (Ueno et al., 2005 [PubMed 16287864]).[supplied by OMIM,
            Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.526998.1,
                                           SRR14038193.3442471.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..111
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.21"
     Protein         1..111
                     /product="DNA replication complex GINS protein PSF1
                     isoform 3"
                     /note="DNA replication complex GINS protein PSF1; partner
                     of sld five-1; GINS complex subunit 1 (Psf1 homolog)"
                     /calculated_mol_wt=12893
     Region          <7..45
                     /region_name="GINS_A"
                     /note="Alpha-helical domain of GINS complex proteins;
                     Sld5, Psf1, Psf2 and Psf3; cl17012"
                     /db_xref="CDD:450135"
     Region          61..109
                     /region_name="GINS_B_Psf1"
                     /note="beta-strand (B) domain of GINS complex protein
                     Psf1; cd21696"
                     /db_xref="CDD:412032"
     Site            order(61..64,66,73,78,80..81,85,87..93,95,108)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:412032"
     CDS             1..111
                     /gene="GINS1"
                     /gene_synonym="IMD55; PSF1"
                     /coded_by="NM_001410831.1:149..484"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS93023.1"
                     /db_xref="GeneID:9837"
                     /db_xref="HGNC:HGNC:28980"
                     /db_xref="MIM:610608"
ORIGIN      
        1 mfcekameli relhrapegq lpafnmewfn nykrslatym rslggdegld itqdmkppks
       61 lyievrclkd ygefevddgt svllkknsqh flprwkceql irqgvlehil s
//
LOCUS       NP_001427588             572 aa            linear   PRI 21-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 3 isoform 8 [Homo sapiens].
ACCESSION   NP_001427588
VERSION     NP_001427588.1
DBSOURCE    REFSEQ: accession NM_001440659.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Ghashghaei,M., Liu,Y., Ettles,J., Bombaci,G., Ramkumar,N., Liu,Z.,
            Escano,L., Miko,S.S., Kim,Y., Waldron,J.A., Do,K., MacPherson,K.,
            Yuen,K.A., Taibi,T., Yue,M., Arsalan,A., Jin,Z., Edin,G.,
            Karsan,A., Morin,G.B., Kuchenbauer,F., Perna,F., Bushell,M. and
            Vu,L.P.
  TITLE     Translation efficiency driven by CNOT3 subunit of the CCR4-NOT
            complex promotes leukemogenesis
  JOURNAL   Nat Commun 15 (1), 2340 (2024)
   PUBMED   38491013
  REMARK    GeneRIF: Translation efficiency driven by CNOT3 subunit of the
            CCR4-NOT complex promotes leukemogenesis.
            Erratum:[Nat Commun. 2024 Oct 7;15(1):8674. doi:
            10.1038/s41467-024-53071-1. PMID: 39375334]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Burgess,H.M., Grande,R., Riccio,S., Dinesh,I., Winkler,G.S.,
            Depledge,D.P. and Mohr,I.
  TITLE     CCR4-NOT differentially controls host versus virus poly(a)-tail
            length and regulates HCMV infection
  JOURNAL   EMBO Rep 24 (12), e56327 (2023)
   PUBMED   37846490
  REMARK    GeneRIF: CCR4-NOT differentially controls host versus virus
            poly(a)-tail length and regulates HCMV infection.
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Zhao,P., Meng,Q., Wan,C., Lei,T., Zhang,L., Zhang,X., Tan,L.,
            Zhu,H. and He,X.
  TITLE     Clinical features of CNOT3-associated neurodevelopmental disorder
            in three Chinese patients
  JOURNAL   Neurogenetics 24 (2), 129-136 (2023)
   PUBMED   36802310
  REMARK    GeneRIF: Clinical features of CNOT3-associated neurodevelopmental
            disorder in three Chinese patients.
REFERENCE   5  (residues 1 to 572)
  AUTHORS   McLenachan,S., Zhang,D., Grainok,J., Zhang,X., Huang,Z., Chen,S.C.,
            Zaw,K., Lima,A., Jennings,L., Roshandel,D., Moon,S.Y., Heath
            Jeffery,R.C., Attia,M.S., Thompson,J.A., Lamey,T.M., McLaren,T.L.,
            De Roach,J., Fletcher,S. and Chen,F.K.
  TITLE     Determinants of Disease Penetrance in PRPF31-Associated Retinopathy
  JOURNAL   Genes (Basel) 12 (10), 1542 (2021)
   PUBMED   34680937
  REMARK    GeneRIF: Determinants of Disease Penetrance in PRPF31-Associated
            Retinopathy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Yin,X., Warner,D.R., Roberts,E.A., Pisano,M.M. and Greene,R.M.
  TITLE     Identification of novel CBP interacting proteins in embryonic
            orofacial tissue
  JOURNAL   Biochem Biophys Res Commun 329 (3), 1010-1017 (2005)
   PUBMED   15752756
REFERENCE   7  (residues 1 to 572)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 572)
  AUTHORS   Aoki,T., Okada,N., Wakamatsu,T. and Tamura,T.A.
  TITLE     TBP-interacting protein 120B, which is induced in relation to
            myogenesis, binds to NOT3
  JOURNAL   Biochem Biophys Res Commun 296 (5), 1097-1103 (2002)
   PUBMED   12207886
  REMARK    GeneRIF: TBP-interacting protein 120B binds to NOT3
REFERENCE   9  (residues 1 to 572)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
REFERENCE   10 (residues 1 to 572)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC245052.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1921836.1,
                                           SRR14038192.2442386.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..572
                     /product="CCR4-NOT transcription complex subunit 3 isoform
                     8"
                     /note="NOT3 (negative regulator of transcription 3, yeast)
                     homolog; CCR4-associated factor 3; leukocyte receptor
                     cluster member 2"
                     /calculated_mol_wt=60257
     Region          <2..48
                     /region_name="Not3"
                     /note="Not1 N-terminal domain, CCR4-Not complex component;
                     pfam04065"
                     /db_xref="CDD:461155"
     Region          <107..478
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          439..564
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     CDS             1..572
                     /gene="CNOT3"
                     /gene_synonym="IDDSADF; LENG2; NOT3; NOT3H"
                     /coded_by="NM_001440659.1:882..2600"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:4849"
                     /db_xref="HGNC:HGNC:7879"
                     /db_xref="MIM:604910"
ORIGIN      
        1 mletilrmld ndsilvdair kikddveyyv dssqdpdfee neflyddldl edipqalvat
       61 sppshshmed eifnqssstp tsttssspip pspanctten seddkkrgrs tdsevsqspa
      121 kngskpvhsn qhpqspavpp typsgpppaa salsttpgnn gvpapaapps algpkaspap
      181 shnsgtpapy aqavappaps gpsttqprpp svqpsggggg gsggggssss snssagggag
      241 kqngatsyss vvadspaeva lsssggnnas sqalgppsgp hnpppstske psaaaptgag
      301 gvapgsgnns ggpsllvplp vnppssptps fsdakaagal lngppqfsta peikapepls
      361 slksmaeraa issgiedpvp tlhlterdii lsstsappas aqpplqlsev niplslgvcp
      421 lgpvpltkeq lyqqameeaa whhmphpsds erirqylprn pcptppyhhq mppphsdtve
      481 fyqrlstetl ffifyylegt kaqylaakal kkqswrfhtk ymmwfqrhee pktitdefeq
      541 gtyiyfdyek wgqrkkegft feyryledrd lq
//
LOCUS       NP_001425269             712 aa            linear   PRI 21-NOV-2025
DEFINITION  ribosomal protein S6 kinase alpha-3 isoform 2 [Homo sapiens].
ACCESSION   NP_001425269 XP_016885206 XP_054183506
VERSION     NP_001425269.1
DBSOURCE    REFSEQ: accession NM_001438340.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Schaeffer,S., Gupta,B., Calatayud,A.L., Calderaro,J., Caruso,S.,
            Hirsch,T.Z., Pelletier,L., Zucman-Rossi,J. and Rebouissou,S.
  TITLE     RSK2 inactivation cooperates with AXIN1 inactivation or
            beta-catenin activation to promote hepatocarcinogenesis
  JOURNAL   J Hepatol 79 (3), 704-716 (2023)
   PUBMED   37201672
  REMARK    GeneRIF: RSK2 inactivation cooperates with AXIN1 inactivation or
            beta-catenin activation to promote hepatocarcinogenesis.
REFERENCE   3  (residues 1 to 712)
  AUTHORS   Pan,J., Liu,M., Duan,X. and Wang,D.
  TITLE     A short peptide LINC00665_18aa encoded by lncRNA LINC00665
            suppresses the proliferation and migration of osteosarcoma cells
            through the regulation of the CREB1/RPS6KA3 interaction
  JOURNAL   PLoS One 18 (6), e0286422 (2023)
   PUBMED   37285335
  REMARK    GeneRIF: A short peptide LINC00665_18aa encoded by lncRNA LINC00665
            suppresses the proliferation and migration of osteosarcoma cells
            through the regulation of the CREB1/RPS6KA3 interaction.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 712)
  AUTHORS   Lopez,J., Bonsor,D.A., Sale,M.J., Urisman,A., Mehalko,J.L.,
            Cabanski-Dunning,M., Castel,P., Simanshu,D.K. and McCormick,F.
  TITLE     The ribosomal S6 kinase 2 (RSK2)-SPRED2 complex regulates the
            phosphorylation of RSK substrates and MAPK signaling
  JOURNAL   J Biol Chem 299 (6), 104789 (2023)
   PUBMED   37149146
  REMARK    GeneRIF: The ribosomal S6 kinase 2 (RSK2)-SPRED2 complex regulates
            the phosphorylation of RSK substrates and MAPK signaling.
REFERENCE   5  (residues 1 to 712)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 712)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   7  (residues 1 to 712)
  AUTHORS   Zhao,Y., Bjorbaek,C., Weremowicz,S., Morton,C.C. and Moller,D.E.
  TITLE     RSK3 encodes a novel pp90rsk isoform with a unique N-terminal
            sequence: growth factor-stimulated kinase function and nuclear
            translocation
  JOURNAL   Mol Cell Biol 15 (8), 4353-4363 (1995)
   PUBMED   7623830
REFERENCE   8  (residues 1 to 712)
  AUTHORS   Ku,N.O. and Omary,M.B.
  TITLE     Identification of the major physiologic phosphorylation site of
            human keratin 18: potential kinases and a role in filament
            reorganization
  JOURNAL   J Cell Biol 127 (1), 161-171 (1994)
   PUBMED   7523419
REFERENCE   9  (residues 1 to 712)
  AUTHORS   Rogers,R.C. and Abidi,F.E.
  TITLE     RPS6KA3-Related Intellectual Disability
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301520
REFERENCE   10 (residues 1 to 712)
  AUTHORS   Omary,M.B., Baxter,G.T., Chou,C.F., Riopel,C.L., Lin,W.Y. and
            Strulovici,B.
  TITLE     PKC epsilon-related kinase associates with and phosphorylates
            cytokeratin 8 and 18
  JOURNAL   J Cell Biol 117 (3), 583-593 (1992)
   PUBMED   1374067
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL807772.12 and AL732366.7.
            
            On or before Apr 21, 2025 this sequence version replaced
            XP_016885206.1, XP_054183506.1.
            
            Summary: This gene encodes a member of the RSK (ribosomal S6
            kinase) family of serine/threonine kinases. This kinase contains 2
            non-identical kinase catalytic domains and phosphorylates various
            substrates, including members of the mitogen-activated kinase
            (MAPK) signalling pathway. The activity of this protein has been
            implicated in controlling cell growth and differentiation.
            Mutations in this gene have been associated with Coffin-Lowry
            syndrome (CLS). [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853565.30223.1,
                                           SRR14038197.1851313.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.12"
     Protein         1..712
                     /product="ribosomal protein S6 kinase alpha-3 isoform 2"
                     /EC_number="2.7.11.1"
                     /note="insulin-stimulated protein kinase 1; ribosomal
                     protein S6 kinase alpha-3; RSK-2; p90-RSK 3; MAPKAPK-1b;
                     S6K-alpha-3; MAPKAP kinase 1b; ribosomal S6 kinase 2;
                     MAPK-activated protein kinase 1b; MAP kinase-activated
                     protein kinase 1b; ribosomal protein S6 kinase, 90kDa,
                     polypeptide 3; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=80581
     Region          44..360
                     /region_name="STKc_RSK_N"
                     /note="N-terminal catalytic domain of the Serine/Threonine
                     Kinase, 90 kDa ribosomal protein S6 kinase; cd05582"
                     /db_xref="CDD:270734"
     Site            order(46..50,54,70,72,103,119..120,122,126,128,165,167,
                     169..170,172,182..183,186,200..205,232,238,241)
                     /site_type="active"
                     /db_xref="CDD:270734"
     Site            order(46..50,54,70,72,103,120..122,126,165,167,169..170,
                     172,182..183)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270734"
     Site            order(50,126,128,165,167,169,186,200..205,232,238,241)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270734"
     Site            order(182..193,195..205)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270734"
     Site            341
                     /site_type="other"
                     /note="turn motif phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:270734"
     Site            354..359
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270734"
     Region          374..712
                     /region_name="STKc_RSK2_C"
                     /note="C-terminal catalytic domain of the Serine/Threonine
                     Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal
                     protein S6 kinase 3 or Ribosomal protein S6 kinase
                     alpha-3); cd14176"
                     /db_xref="CDD:271078"
     Site            order(400..404,406,408,421,423,449,465..468,471..472,474,
                     510..511,513,515..516,518,532..533,536,551..555,557)
                     /site_type="active"
                     /db_xref="CDD:271078"
     Site            order(400..403,406,408,421,423,449,465..468,471..472,
                     515..516,518,532..533)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271078"
     Site            order(404,472,474,510..511,513,515,536,551..555,557)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271078"
     Site            532..555
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271078"
     CDS             1..712
                     /gene="RPS6KA3"
                     /gene_synonym="CLS; HU-3; ISPK-1; MAPKAPK1B; MRX19;
                     p90-RSK2; pp90RSK2; RSK; RSK2; S6K-alpha3; XLID19"
                     /coded_by="NM_001438340.1:68..2206"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:6197"
                     /db_xref="HGNC:HGNC:10432"
                     /db_xref="MIM:300075"
ORIGIN      
        1 mdepmgeeei npqteevsik eiaithhvke ghekadpsqf ellkvlgqgs fgkvflvkki
       61 sgsdarqlya mkvlkkatlk vrdrvrtkme rdilvevnhp fivklhyafq tegklylild
      121 flrggdlftr lskevmftee dvkfylaela laldhlhslg iiyrdlkpen illdeeghik
      181 ltdfglskes idhekkaysf cgtveymape vvnrrghtqs adwwsfgvlm femltgtlpf
      241 qgkdrketmt milkaklgmp qflspeaqsl lrmlfkrnpa nrlgagpdgv eeikrhsffs
      301 tidwnklyrr eihppfkpat grpedtfyfd peftaktpkd spgippsana hqlfrgfsfv
      361 aitsddesqa mqtvgvhsiv qqlhrnsiqf tdgyevkedi gvgsysvckr cihkatnmef
      421 avkiidkskr dpteeieill rygqhpniit lkdvyddgky vyvvtelmkg gelldkilrq
      481 kffsereasa vlftitktve ylhaqgvvhr dlkpsnilyv desgnpesir icdfgfakql
      541 raengllmtp cytanfvape vlkrqgydaa cdiwslgvll ytmltgytpf angpddtpee
      601 ilarigsgkf slsggywnsv sdtakdlvsk mlhvdphqrl taalvlrhpw ivhwdqlpqy
      661 qlnrqdaphl vkgamaatys alnrnqspvl epvgrstlaq rrgikkitst al
//
LOCUS       NP_001425734            1248 aa            linear   PRI 21-NOV-2025
DEFINITION  NHS-like protein 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001425734 XP_047298020 XP_054182932
VERSION     NP_001425734.1
DBSOURCE    REFSEQ: accession NM_001438805.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1248)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1248)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1248)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL929401.8 and BX119917.9.
            
            On or before Apr 24, 2025 this sequence version replaced
            XP_047298020.1, XP_054182932.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2785737.1,
                                           SRR18074967.1266359.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245, SAMN03465409
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..1248
                     /product="NHS-like protein 2 isoform 2"
                     /note="NHS-like protein 2; TPT1-like protein"
                     /calculated_mol_wt=135727
     Region          184..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5HYW2.2)"
     Region          216..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5HYW2.2)"
     Region          314..394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5HYW2.2)"
     Region          489..533
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5HYW2.2)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B1AXH1; propagated from
                     UniProtKB/Swiss-Prot (Q5HYW2.2)"
     Region          <548..778
                     /region_name="NHS"
                     /note="NHS-like; pfam15273"
                     /db_xref="CDD:464606"
     Region          566..655
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5HYW2.2)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B1AXH1; propagated from
                     UniProtKB/Swiss-Prot (Q5HYW2.2)"
     Region          693..789
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5HYW2.2)"
     Site            714
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B1AXH1; propagated from
                     UniProtKB/Swiss-Prot (Q5HYW2.2)"
     Region          <744..978
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          835..1032
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5HYW2.2)"
     Region          1065..1116
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5HYW2.2)"
     Site            1077
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B1AXH1; propagated from
                     UniProtKB/Swiss-Prot (Q5HYW2.2)"
     Region          1151..1226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5HYW2.2)"
     CDS             1..1248
                     /gene="NHSL2"
                     /coded_by="NM_001438805.1:244..3990"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:340527"
                     /db_xref="HGNC:HGNC:33737"
                     /db_xref="MIM:301093"
ORIGIN      
        1 mpfyrrtvvp qrlcprnppq qlaelrdvsh laalsllrql adlcghslal ledleghlla
       61 lgrrtdslyr rtvrlrrrlp crllgpeede eelgashwsn ltrsqrarep vdaihtaaan
      121 sgrenatata hsrsswrqpv nvflssgrpp sveellreaq lnlqsllqee yeeqysearl
      181 vgqtfrssde atkptpnprp qsarrlefil mptkrqlsed etttqgvrap easlslstta
      241 dkqtawnslf plpileekrw pqlcstqsdi vpinisgqqf dkhaslrhsl fntetavnpk
      301 stlrrrrtii gfsnfsqrdq ghsnspagsv ahsttsdirp shsvpegvhg rvavgqdarf
      361 psltspvlrt pssepdephq arsgpnppgm esmgmvysvp sscngptest fstswkgdaf
      421 tymtpsatsq snqvnengkn pscgnswvsl nkvpplvpke aatllvardn pagcsgsagy
      481 perliqqrhm perpskigll tsgtsrletg pggasrfrer slsvptdsgt tdvdydeeqk
      541 aneacalpfa stssegsnsa dniaslsaqq eaqhrrqrsk sislrkakkk pspptrsvsl
      601 vkdepgllpe ggsalpkdqr pkslclsleh qghhsshpda qghpaipnhk dpestqfshh
      661 wyltdwksgd tyqslsssst atgttviect qvqgssesla spstsrattp sqlsievear
      721 eisspgrppg lmspssgyss qsetptptvs msltlghlpp psssvrvrpv vperksslpp
      781 tspmekfpks rlsfdlplts spnldlsgms isirsktkvs rhhsetnfgv klaqktnpnq
      841 pimpmvtqsd lrsvrlrsvs ksepeddies peyaeeprae evftlperkt kppvaekppv
      901 arrppslvhk ppsvpeeyal tsptlamppr ssiqharplp qdsytvvrkp kpssfpdgrs
      961 pgestapssl vftpfasssd affsgtqqpp qgsvedegpk vrvlperisl qsqeeaekkk
     1021 gkipppvpkk psvlylplts ptaqmeayva eprlplspii tleedtkcpa tgddlqslgq
     1081 rvtstpqads ereasplgss vepgteeksl isdktaewia eddddvfvas rttedlftvi
     1141 hrskrkllgw kepgeafvgg rtsshspikn taespisest atagsgssan ldagrnddfk
     1201 allqkkgska tprsrpsaae llkttnplar riiaqfskdy ettdnpst
//
LOCUS       NP_001397885             350 aa            linear   PRI 21-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 6 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001397885 XP_011538069
VERSION     NP_001397885.1
DBSOURCE    REFSEQ: accession NM_001410956.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Bartels,N., van der Voort,N.T.M., Opanasyuk,O., Felekyan,S.,
            Greife,A., Shang,X., Bister,A., Wiek,C., Seidel,C.A.M. and
            Monzel,C.
  TITLE     Advanced multiparametric image spectroscopy and super-resolution
            microscopy reveal a minimal model of CD95 signal initiation
  JOURNAL   Sci Adv 10 (35), eadn3238 (2024)
   PUBMED   39213362
  REMARK    GeneRIF: Advanced multiparametric image spectroscopy and
            super-resolution microscopy reveal a minimal model of CD95 signal
            initiation.
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Liu,Y., Sardana,R., Nemirovsky,D., Frosina,D., Jungbluth,A.,
            Johnson,W.T., Vardhana,S., Arcila,M., Horwitz,S.M., Derkach,A.,
            Dogan,A. and Xiao,W.
  TITLE     Somatic mutations in FAS pathway increase hemophagocytic
            lymphohistiocytosis risk in patients with T- and/or NK-cell
            lymphoma
  JOURNAL   Blood Adv 8 (12), 3064-3075 (2024)
   PUBMED   38593227
  REMARK    GeneRIF: Somatic mutations in FAS pathway increase hemophagocytic
            lymphohistiocytosis risk in patients with T- and/or NK-cell
            lymphoma.
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Yang,Z., Zhang,X., Zhang,X., Liu,Y., Zhang,J. and Yuan,X.
  TITLE     [Porphyromonas gingivalis infection facilitates immune escape of
            esophageal cancer by enhancing YTHDF2-mediated Fas degradation]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 44 (6), 1159-1165 (2024)
   PUBMED   38977346
  REMARK    GeneRIF: [Porphyromonas gingivalis infection facilitates immune
            escape of esophageal cancer by enhancing YTHDF2-mediated Fas
            degradation].
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Staniek,J., Kalina,T., Andrieux,G., Boerries,M., Janowska,I.,
            Fuentes,M., Diez,P., Bakardjieva,M., Stancikova,J., Raabe,J.,
            Neumann,J., Schwenk,S., Arpesella,L., Stuchly,J., Benes,V., Garcia
            Valiente,R., Fernandez Garcia,J., Carsetti,R., Piano Mortari,E.,
            Catala,A., de la Calle,O., Sogkas,G., Neven,B., Rieux-Laucat,F.,
            Magerus,A., Neth,O., Olbrich,P., Voll,R.E., Alsina,L.,
            Allende,L.M., Gonzalez-Granado,L.I., Bohler,C., Thiel,J.,
            Venhoff,N., Lorenzetti,R., Warnatz,K., Unger,S., Seidl,M.,
            Mielenz,D., Schneider,P., Ehl,S., Rensing-Ehl,A., Smulski,C.R. and
            Rizzi,M.
  TITLE     Non-apoptotic FAS signaling controls mTOR activation and
            extrafollicular maturation in human B cells
  JOURNAL   Sci Immunol 9 (91), eadj5948 (2024)
   PUBMED   38215192
  REMARK    GeneRIF: Non-apoptotic FAS signaling controls mTOR activation and
            extrafollicular maturation in human B cells.
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Jenkins,M., Keir,M. and McCune,J.M.
  TITLE     A membrane-bound Fas decoy receptor expressed by human thymocytes
  JOURNAL   J Biol Chem 275 (11), 7988-7993 (2000)
   PUBMED   10713117
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Cascino,I., Papoff,G., Eramo,A. and Ruberti,G.
  TITLE     Soluble Fas/Apo-1 splicing variants and apoptosis
  JOURNAL   Front Biosci 1, d12-d18 (1996)
   PUBMED   9159204
  REMARK    GeneRIF: A review of alternative spliced APO-1 variants and their
            possible biological roles.
            Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Cheng,J., Zhou,T., Liu,C., Shapiro,J.P., Brauer,M.J., Kiefer,M.C.,
            Barr,P.J. and Mountz,J.D.
  TITLE     Protection from Fas-mediated apoptosis by a soluble form of the Fas
            molecule
  JOURNAL   Science 263 (5154), 1759-1762 (1994)
   PUBMED   7510905
REFERENCE   8  (residues 1 to 350)
  AUTHORS   Bleesing,J.J.H., Nagaraj,C.B. and Zhang,K.
  TITLE     Autoimmune Lymphoproliferative Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301287
REFERENCE   9  (residues 1 to 350)
  AUTHORS   Inazawa,J., Itoh,N., Abe,T. and Nagata,S.
  TITLE     Assignment of the human Fas antigen gene (Fas) to 10q24.1
  JOURNAL   Genomics 14 (3), 821-822 (1992)
   PUBMED   1385309
REFERENCE   10 (residues 1 to 350)
  AUTHORS   Oehm,A., Behrmann,I., Falk,W., Pawlita,M., Maier,G., Klas,C.,
            Li-Weber,M., Richards,S., Dhein,J., Trauth,B.C. et al.
  TITLE     Purification and molecular cloning of the APO-1 cell surface
            antigen, a member of the tumor necrosis factor/nerve growth factor
            receptor superfamily. Sequence identity with the Fas antigen
  JOURNAL   J Biol Chem 267 (15), 10709-10715 (1992)
   PUBMED   1375228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157394.15.
            
            On Aug 18, 2022 this sequence version replaced XP_011538069.1.
            
            Summary: The protein encoded by this gene is a member of the
            TNF-receptor superfamily. This receptor contains a death domain. It
            has been shown to play a central role in the physiological
            regulation of programmed cell death, and has been implicated in the
            pathogenesis of various malignancies and diseases of the immune
            system. The interaction of this receptor with its ligand allows the
            formation of a death-inducing signaling complex that includes
            Fas-associated death domain protein (FADD), caspase 8, and caspase
            10. The autoproteolytic processing of the caspases in the complex
            triggers a downstream caspase cascade, and leads to apoptosis. This
            receptor has been also shown to activate NF-kappaB, MAPK3/ERK1, and
            MAPK8/JNK, and is found to be involved in transducing the
            proliferating signals in normal diploid fibroblast and T cells.
            Several alternatively spliced transcript variants have been
            described, some of which are candidates for nonsense-mediated mRNA
            decay (NMD). The isoforms lacking the transmembrane domain may
            negatively regulate the apoptosis mediated by the full length
            isoform. [provided by RefSeq, Mar 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2182185.1,
                                           SRR14038197.374836.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.31"
     Protein         1..350
                     /product="tumor necrosis factor receptor superfamily
                     member 6 isoform 5"
                     /note="tumor necrosis factor receptor superfamily, member
                     6; APO-1 cell surface antigen; apoptosis antigen 1; Fas
                     AMA; CD95 antigen; FASLG receptor; apoptosis-mediating
                     surface antigen FAS; apoptosis signaling receptor FAS; Fas
                     (TNF receptor superfamily, member 6); TNF receptor
                     superfamily member 6; mutant tumor necrosis receptor
                     superfamily member 6"
                     /calculated_mol_wt=39114
     Region          54..182
                     /region_name="TNFRSF6"
                     /note="Tumor necrosis factor receptor superfamily member 6
                     (TNFRSF6), also known as fas cell surface death receptor
                     (Fas); cd10579"
                     /db_xref="CDD:276905"
     Region          63..97
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276905"
     Site            order(74..80,109..112,117)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:276905"
     Region          100..142
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276905"
     Region          144..164
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276905"
     Region          241..334
                     /region_name="Death_FAS_TNFRSF6"
                     /note="Death domain of FAS or TNF receptor superfamily
                     member 6; cd08316"
                     /db_xref="CDD:260028"
     Site            order(243..244,246..247,250..251,253..254,266,299..301,
                     303..304,306,309..311,313..315,317,320..324,326,329..330)
                     /site_type="other"
                     /note="FAS-FADD heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:260028"
     Site            order(266,322..323,326,330,333..334)
                     /site_type="other"
                     /note="octamer interface [polypeptide binding]"
                     /db_xref="CDD:260028"
     Site            order(311,314,318,321..322,329,332..333)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:260028"
     CDS             1..350
                     /gene="FAS"
                     /gene_synonym="ALPS1A; APO-1; APT1; CD95; FAS1; FASTM;
                     TNFRSF6"
                     /coded_by="NM_001410956.1:225..1277"
                     /note="isoform 5 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS91297.1"
                     /db_xref="GeneID:355"
                     /db_xref="HGNC:HGNC:11920"
                     /db_xref="MIM:134637"
ORIGIN      
        1 mrsadpagqa gqlrrssett alhvevltsv arlssksvna qvtdinskgl elrktvttve
       61 tqnleglhhd gqfchkpcpp gerkardctv ngdepdcvpc qegkeytdka hfsskcrrcr
      121 lcdeghglev einctrtqnt kcrckpnffc nstvcehcdp ctkcehgiik ectltsntkc
      181 keegsrsnlg wlcllllpip livwvkrkev qktcrkhrke nqgshesptl npetvainls
      241 dvdlskyitt iagvmtlsqv kgfvrkngvn eakideiknd nvqdtaeqkv qllrnwhqlh
      301 gkkeaydtli kdlkkanlct laekiqtiil kditsdsens nfrneiqslv
//
LOCUS       NP_001427499            1012 aa            linear   PRI 21-NOV-2025
DEFINITION  lysosomal alpha-mannosidase isoform 3 precursor [Homo sapiens].
ACCESSION   NP_001427499 XP_005259970 XP_054177008
VERSION     NP_001427499.1
DBSOURCE    REFSEQ: accession NM_001440570.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Lehalle,D., Colombo,R., O'Grady,M., Heron,B., Houcinat,N.,
            Kuentz,P., Moutton,S., Sorlin,A., Thevenon,J., Delanne,J., Gay,S.,
            Racine,C., Garde,A., Tran Mau-Them,F., Philippe,C., Vitobello,A.,
            Nambot,S., Huet,F., Duffourd,Y., Feillet,F., Thauvin-Robinet,C.,
            Marlin,S. and Faivre,L.
  TITLE     Hearing impairment as an early sign of alpha-mannosidosis in
            children with a mild phenotype: Report of seven new cases
  JOURNAL   Am J Med Genet A 179 (9), 1756-1763 (2019)
   PUBMED   31241255
  REMARK    GeneRIF: A diagnosis can be established by measuring the activity
            of lysosomal alpha-mannosidase in leucocytes and screening for
            abnormal urinary excretion of mannose-rich oligosaccharides.
            Genetic confirmation is obtained with the identification of MAN2B1
            mutations.
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Yu,P., Cui,Y., Cai,W., Wu,H., Xiao,X., Shao,Q., Ma,L., Guo,S.,
            Wu,N., Jin,Z.B., Wang,Y., Cai,T., Sun,Z.S. and Qu,J.
  TITLE     Lysosomal storage disease in the brain: mutations of the
            beta-mannosidase gene identified in autosomal dominant nystagmus
  JOURNAL   Genet Med 17 (12), 971-979 (2015)
   PUBMED   25741867
  REMARK    GeneRIF: A novel heterozygous mutation (c.2013G>A; p.R638H) of
            MANBA was identified in patients with autosomal-dominant nystagmus.
            An additional mutation (c.2346T>A; p.L749H) in MANBA was found by
            screening patients with sporadic nystagmus.
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Borgwardt,L., Stensland,H.M., Olsen,K.J., Wibrand,F., Klenow,H.B.,
            Beck,M., Amraoui,Y., Arash,L., Fogh,J., Nilssen,O., Dali,C.I. and
            Lund,A.M.
  TITLE     Alpha-mannosidosis: correlation between phenotype, genotype and
            mutant MAN2B1 subcellular localisation
  JOURNAL   Orphanet J Rare Dis 10, 70 (2015)
   PUBMED   26048034
  REMARK    GeneRIF: Our results indicate a correlation between the MAN2B1
            genotypes and the cognitive function, upper limb coordination,
            balance, FVC% and the storage of oligosaccharides in CSF.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1012)
  AUTHORS   Thaysen-Andersen,M., Venkatakrishnan,V., Loke,I., Laurini,C.,
            Diestel,S., Parker,B.L. and Packer,N.H.
  TITLE     Human neutrophils secrete bioactive paucimannosidic proteins from
            azurophilic granules into pathogen-infected sputum
  JOURNAL   J Biol Chem 290 (14), 8789-8802 (2015)
   PUBMED   25645918
REFERENCE   5  (residues 1 to 1012)
  AUTHORS   Manichaikul,A., Hoffman,E.A., Smolonska,J., Gao,W., Cho,M.H.,
            Baumhauer,H., Budoff,M., Austin,J.H., Washko,G.R., Carr,J.J.,
            Kaufman,J.D., Pottinger,T., Powell,C.A., Wijmenga,C., Zanen,P.,
            Groen,H.J., Postma,D.S., Wanner,A., Rouhani,F.N., Brantly,M.L.,
            Powell,R., Smith,B.M., Rabinowitz,D., Raffel,L.J., Hinckley
            Stukovsky,K.D., Crapo,J.D., Beaty,T.H., Hokanson,J.E.,
            Silverman,E.K., Dupuis,J., O'Connor,G.T., Boezen,H.M., Rich,S.S.
            and Barr,R.G.
  TITLE     Genome-wide study of percent emphysema on computed tomography in
            the general population. The Multi-Ethnic Study of Atherosclerosis
            Lung/SNP Health Association Resource Study
  JOURNAL   Am J Respir Crit Care Med 189 (4), 408-418 (2014)
   PUBMED   24383474
REFERENCE   6  (residues 1 to 1012)
  AUTHORS   Emiliani,C., Martino,S., Stirling,J.L., Maras,B. and Orlacchio,A.
  TITLE     Partial sequence of the purified protein confirms the identity of
            cDNA coding for human lysosomal alpha-mannosidase B
  JOURNAL   Biochem J 305 (Pt 2) (Pt 2), 363-366 (1995)
   PUBMED   7832746
REFERENCE   7  (residues 1 to 1012)
  AUTHORS   Ficicioglu,C. and Stepien,K.M.
  TITLE     Alpha-Mannosidosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301570
REFERENCE   8  (residues 1 to 1012)
  AUTHORS   Kaneda,Y., Hayes,H., Uchida,T., Yoshida,M.C. and Okada,Y.
  TITLE     Regional assignment of five genes on human chromosome 19
  JOURNAL   Chromosoma 95 (1), 8-12 (1987)
   PUBMED   3034518
REFERENCE   9  (residues 1 to 1012)
  AUTHORS   Champion,M.J. and Shows,T.B.
  TITLE     Electrophoretic abnormalities of lysosomal enzymes in mucolipidosis
            fibroblast lines
  JOURNAL   Am J Hum Genet 29 (2), 149-163 (1977)
   PUBMED   848490
REFERENCE   10 (residues 1 to 1012)
  AUTHORS   Phillips,N.C., Robinson,D. and Winchester,B.G.
  TITLE     Characterization of human liver alpha-D-mannosidase purified by
            affinity chromatography
  JOURNAL   Biochem J 153 (3), 579-587 (1976)
   PUBMED   821469
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010422.7.
            
            On or before May 22, 2025 this sequence version replaced
            XP_005259970.1, XP_054177008.1.
            
            Summary: This gene encodes an enzyme that hydrolyzes terminal,
            non-reducing alpha-D-mannose residues in alpha-D-mannosides. Its
            activity is necessary for the catabolism of N-linked carbohydrates
            released during glycoprotein turnover and it is member of family 38
            of glycosyl hydrolases. The full length protein is processed in two
            steps. First, a 49 aa leader sequence is cleaved off and the
            remainder of the protein is processed into 3 peptides of 70 kDa, 42
            kDa (D) and 13/15 kDa (E). Next, the 70 kDa peptide is further
            processed into three peptides (A, B and C). The A, B and C peptides
            are disulfide-linked. Defects in this gene have been associated
            with lysosomal alpha-mannosidosis. Alternatively spliced transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1035301.1,
                                           SRR18074967.979071.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.13"
     Protein         1..1012
                     /product="lysosomal alpha-mannosidase isoform 3 precursor"
                     /EC_number="3.2.1.24"
                     /note="mannosidase, alpha B, lysosomal; lysosomal acid
                     alpha-mannosidase; lysosomal alpha-mannosidase;
                     mannosidase alpha-B"
                     /calculated_mol_wt=108842
     sig_peptide     1..49
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=5049
     Region          63..1001
                     /region_name="PLN02701"
                     /note="alpha-mannosidase"
                     /db_xref="CDD:178304"
     Region          63..341
                     /region_name="GH38N_AMII_LAM_like"
                     /note="N-terminal catalytic domain of lysosomal
                     alpha-mannosidase and similar proteins; glycoside
                     hydrolase family 38 (GH38); cd10810"
                     /db_xref="CDD:212121"
     Site            order(72,74,77,196,198,220,319)
                     /site_type="active"
                     /db_xref="CDD:212121"
     Site            order(74..80,155..171,173..174,196,198..203,207,220..225,
                     241..243)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:212121"
     Site            133
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     Site            310
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     mat_peptide     347..430
                     /product="Lysosomal alpha-mannosidase B peptide.
                     /id=PRO_0000012071"
                     /note="propagated from UniProtKB/Swiss-Prot (O00754.3)"
                     /calculated_mol_wt=9578
     Site            368
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     mat_peptide     431..602
                     /product="Lysosomal alpha-mannosidase C peptide.
                     /id=PRO_0000012072"
                     /note="propagated from UniProtKB/Swiss-Prot (O00754.3)"
                     /calculated_mol_wt=18886
     Site            498
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     mat_peptide     603..883
                     /product="Lysosomal alpha-mannosidase D peptide.
                     /id=PRO_0000012073"
                     /note="propagated from UniProtKB/Swiss-Prot (O00754.3)"
                     /calculated_mol_wt=31575
     Site            646
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     Site            652
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     Site            693
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     Site            767
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     Site            833
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     mat_peptide     884..1012
                     /product="Lysosomal alpha-mannosidase E peptide.
                     /id=PRO_0000012074"
                     /note="propagated from UniProtKB/Swiss-Prot (O00754.3)"
                     /calculated_mol_wt=14491
     Site            931
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     Site            990
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     CDS             1..1012
                     /gene="MAN2B1"
                     /gene_synonym="LAMAN; MANB"
                     /coded_by="NM_001440570.1:42..3080"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:4125"
                     /db_xref="HGNC:HGNC:6826"
                     /db_xref="MIM:609458"
ORIGIN      
        1 mgayarasgv cargcldsag pwtmsralrp plpplcffll llaaagarag gyetcptvqp
       61 nmlnvhllph thddvgwlkt vdqyfygikn diqhagvqyi ldsvisalla dptrrfiyve
      121 iaffsrwwhq qtnatqevvr dlvrqgrlef anggwvmnde aathygaivd qmtlglrfle
      181 dtfgndgrpr vawhidpfgh sreqaslfaq mgfdgfffgr ldyqdkwvrm qklemeqvwr
      241 astslkppta dlftgvlpng ynpprnlcwd vlcvdqplve dprspeynak elvdyflnva
      301 taqgryyrtn htvmtmgsdf qyenanmwfk nldklirlvn aqqqakgssv hvlystpacy
      361 lwelnkanlt wsvkhddffp yadgphqfwt gyfssrpalk ryerlsynfl qvcnqlealv
      421 glaanvgpyg sgdsaplnea mavlqhhdav sgtsrqhvan dyarqlaagw gpcevllsna
      481 larlrgfkdh ftfcqqlnis icplsqtaar fqvivynplg rkvnwmvrlp vsegvfvvkd
      541 pngrtvpsdv vifpssdsqa hppellfsas lpalgfstys vaqvprwkpq arapqpiprr
      601 swspaltien ehiratfdpd tgllmeimnm nqqlllpvrq tffwynasig dnesdqasga
      661 yifrpnqqkp lpvsrwaqih lvktplvqev hqnfsawcsq vvrlypgqrh lelewsvgpi
      721 pvgdtwgkev isrfdtplet kgrfytdsng reilerrrdy rptwklnqte pvagnyypvn
      781 triyitdgnm qltvltdrsq ggsslrdgsl elmvhrrllk ddgrgvsepl mengsgawvr
      841 grhlvlldta qaaaaghrll aeqevlapqv vlapgggaay nlgapprtqf sglrrdlpps
      901 vhlltlaswg pemvllrleh qfavgedsgr nlsapvtlnl rdlfstftit rlqettlvan
      961 qlreaasrlk wttntgptph qtpyqldpan itlepmeirt flasvqwkev dg
//
LOCUS       NP_001426089             561 aa            linear   PRI 21-NOV-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein Q isoform 5 [Homo sapiens].
ACCESSION   NP_001426089 XP_016865668 XP_054210017
VERSION     NP_001426089.1
DBSOURCE    REFSEQ: accession NM_001439160.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Ishtayeh,H., Galves,M., Barnatan,T.T., Berdichevsky,Y.,
            Amer-Sarsour,F., Pasmanik-Chor,M., Braverman,I., Blumen,S.C. and
            Ashkenazi,A.
  TITLE     Oculopharyngeal muscular dystrophy mutations link the RNA-binding
            protein HNRNPQ to autophagosome biogenesis
  JOURNAL   Aging Cell 22 (10), e13949 (2023)
   PUBMED   37559347
  REMARK    GeneRIF: Oculopharyngeal muscular dystrophy mutations link the
            RNA-binding protein HNRNPQ to autophagosome biogenesis.
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Semino,F., Schroter,J., Willemsen,M.H., Bast,T., Biskup,S.,
            Beck-Woedl,S., Brennenstuhl,H., Schaaf,C.P., Kolker,S.,
            Hoffmann,G.F., Haack,T.B. and Syrbe,S.
  TITLE     Further evidence for de novo variants in SYNCRIP as the cause of a
            neurodevelopmental disorder
  JOURNAL   Hum Mutat 42 (9), 1094-1100 (2021)
   PUBMED   34157790
  REMARK    GeneRIF: Further evidence for de novo variants in SYNCRIP as the
            cause of a neurodevelopmental disorder.
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 561)
  AUTHORS   Mourelatos,Z., Abel,L., Yong,J., Kataoka,N. and Dreyfuss,G.
  TITLE     SMN interacts with a novel family of hnRNP and spliceosomal
            proteins
  JOURNAL   EMBO J 20 (19), 5443-5452 (2001)
   PUBMED   11574476
REFERENCE   6  (residues 1 to 561)
  AUTHORS   Lau,P.P., Chang,B.H. and Chan,L.
  TITLE     Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a
            component of apobec-1 editosome
  JOURNAL   Biochem Biophys Res Commun 282 (4), 977-983 (2001)
   PUBMED   11352648
REFERENCE   7  (residues 1 to 561)
  AUTHORS   Blanc,V., Navaratnam,N., Henderson,J.O., Anant,S., Kennedy,S.,
            Jarmuz,A., Scott,J. and Davidson,N.O.
  TITLE     Identification of GRY-RBP as an apolipoprotein B RNA-binding
            protein that interacts with both apobec-1 and apobec-1
            complementation factor to modulate C to U editing
  JOURNAL   J Biol Chem 276 (13), 10272-10283 (2001)
   PUBMED   11134005
REFERENCE   8  (residues 1 to 561)
  AUTHORS   Grosset,C., Chen,C.Y., Xu,N., Sonenberg,N., Jacquemin-Sablon,H. and
            Shyu,A.B.
  TITLE     A mechanism for translationally coupled mRNA turnover: interaction
            between the poly(A) tail and a c-fos RNA coding determinant via a
            protein complex
  JOURNAL   Cell 103 (1), 29-40 (2000)
   PUBMED   11051545
REFERENCE   9  (residues 1 to 561)
  AUTHORS   Mizutani,A., Fukuda,M., Ibata,K., Shiraishi,Y. and Mikoshiba,K.
  TITLE     SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear
            ribonucleoprotein R, interacts with ubiquitous synaptotagmin
            isoforms
  JOURNAL   J Biol Chem 275 (13), 9823-9831 (2000)
   PUBMED   10734137
REFERENCE   10 (residues 1 to 561)
  AUTHORS   Harris,C.E., Boden,R.A. and Astell,C.R.
  TITLE     A novel heterogeneous nuclear ribonucleoprotein-like protein
            interacts with NS1 of the minute virus of mice
  JOURNAL   J Virol 73 (1), 72-80 (1999)
   PUBMED   9847309
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136082.22.
            
            On or before Apr 28, 2025 this sequence version replaced
            XP_016865668.1, XP_054210017.1.
            
            Summary: This gene encodes a member of the cellular heterogeneous
            nuclear ribonucleoprotein (hnRNP) family. hnRNPs are RNA binding
            proteins that complex with heterogeneous nuclear RNA (hnRNA) and
            regulate alternative splicing, polyadenylation, and other aspects
            of mRNA metabolism and transport. The encoded protein plays a role
            in multiple aspects of mRNA maturation and is associated with
            several multiprotein complexes including the apoB RNA
            editing-complex and survival of motor neurons (SMN) complex.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene, and a pseudogene of this
            gene is located on the short arm of chromosome 20. [provided by
            RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2268910.1,
                                           SRR18074969.2460901.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.3"
     Protein         1..561
                     /product="heterogeneous nuclear ribonucleoprotein Q
                     isoform 5"
                     /note="NS1-associated protein 1; heterogeneous nuclear
                     ribonucleoprotein Q; glycine- and tyrosine-rich
                     RNA-binding protein"
                     /calculated_mol_wt=62397
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          23..107
                     /region_name="NURR_hnRNPQ"
                     /note="NURR (N-terminal unit for RNA recognition) domain
                     found in heterogeneous nuclear ribonucleoprotein Q
                     (hnRNPQ) and similar proteins; cd21066"
                     /db_xref="CDD:410954"
     Region          103..553
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            221
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            363
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:12601080; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            444
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          460..488
                     /region_name="3 X 4 AA repeats of Y-Y-G-Y"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            496
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            510
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          518..549
                     /region_name="Interaction with SMN.
                     /evidence=ECO:0000269|PubMed:11574476"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            518
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            526
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            536
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            539
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     CDS             1..561
                     /gene="SYNCRIP"
                     /gene_synonym="GRY-RBP; GRYRBP; hnRNP-Q; HNRNPQ; HNRPQ1;
                     NSAP1; PP68"
                     /coded_by="NM_001439160.1:134..1819"
                     /note="isoform 5 is encoded by transcript variant 11"
                     /db_xref="GeneID:10492"
                     /db_xref="HGNC:HGNC:16918"
                     /db_xref="MIM:616686"
ORIGIN      
        1 matehvngng teepmdttsa vihsenfqtl ldaglpqkva ekldeiyvag lvahsdlder
       61 aiealkefne dgalavlqqf kdsdlshvqn ksaflcgvmk tyrqrekqgt kvadsskgpd
      121 eakikaller tgytldvttg qrkyggpppd svysgqqpsv gteifvgkip rdlfedelvp
      181 lfekagpiwd lrlmmdpltg lnrgyafvtf ctkeaaqeav klynnheirs gkhigvcisv
      241 annrlfvgsi pksktkeqil eefskvtegl tdvilyhqpd dkkknrgfcf leyedhktaa
      301 qarrrlmsgk vkvwgnvgtv ewadpiedpd pevmakvkvl fvrnlantvt eeilekafsq
      361 fgklervkkl kdyafihfde rdgavkamee mngkdlegen ieivfakppd qkrkerkaqr
      421 qaaknqmydd yyyygpphmp pptrgrgrgg rggygyppdy ygyedyydyy gydyhnyrgg
      481 yedpyygyed fqvgargrgg rgargaapsr grgaapprgr agysqrggpg sargvrgarg
      541 gaqqqrgrgg kgveagpdll q
//
LOCUS       NP_001397931             566 aa            linear   PRI 21-NOV-2025
DEFINITION  nucleoporin p58/p45 isoform d [Homo sapiens].
ACCESSION   NP_001397931 XP_005266657
VERSION     NP_001397931.1
DBSOURCE    REFSEQ: accession NM_001411002.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Targa,A., Larrimore,K.E., Wong,C.K., Chong,Y.L., Fung,R., Lee,J.,
            Choi,H. and Rancati,G.
  TITLE     Non-genetic and genetic rewiring underlie adaptation to hypomorphic
            alleles of an essential gene
  JOURNAL   EMBO J 40 (21), e107839 (2021)
   PUBMED   34528284
  REMARK    GeneRIF: Non-genetic and genetic rewiring underlie adaptation to
            hypomorphic alleles of an essential gene.
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 566)
  AUTHORS   Kaltenbach,L.S., Romero,E., Becklin,R.R., Chettier,R., Bell,R.,
            Phansalkar,A., Strand,A., Torcassi,C., Savage,J., Hurlburt,A.,
            Cha,G.H., Ukani,L., Chepanoske,C.L., Zhen,Y., Sahasrabudhe,S.,
            Olson,J., Kurschner,C., Ellerby,L.M., Peltier,J.M., Botas,J. and
            Hughes,R.E.
  TITLE     Huntingtin interacting proteins are genetic modifiers of
            neurodegeneration
  JOURNAL   PLoS Genet 3 (5), e82 (2007)
   PUBMED   17500595
REFERENCE   7  (residues 1 to 566)
  AUTHORS   Le Rouzic,E., Mousnier,A., Rustum,C., Stutz,F., Hallberg,E.,
            Dargemont,C. and Benichou,S.
  TITLE     Docking of HIV-1 Vpr to the nuclear envelope is mediated by the
            interaction with the nucleoporin hCG1
  JOURNAL   J Biol Chem 277 (47), 45091-45098 (2002)
   PUBMED   12228227
REFERENCE   8  (residues 1 to 566)
  AUTHORS   Ben-Efraim,I. and Gerace,L.
  TITLE     Gradient of increasing affinity of importin beta for nucleoporins
            along the pathway of nuclear import
  JOURNAL   J Cell Biol 152 (2), 411-417 (2001)
   PUBMED   11266456
REFERENCE   9  (residues 1 to 566)
  AUTHORS   Shiota,C., Coffey,J., Grimsby,J., Grippo,J.F. and Magnuson,M.A.
  TITLE     Nuclear import of hepatic glucokinase depends upon glucokinase
            regulatory protein, whereas export is due to a nuclear export
            signal sequence in glucokinase
  JOURNAL   J Biol Chem 274 (52), 37125-37130 (1999)
   PUBMED   10601273
REFERENCE   10 (residues 1 to 566)
  AUTHORS   Buss,F. and Stewart,M.
  TITLE     Macromolecular interactions in the nucleoporin p62 complex of rat
            nuclear pores: binding of nucleoporin p54 to the rod domain of p62
  JOURNAL   J Cell Biol 128 (3), 251-261 (1995)
   PUBMED   7531196
  REMARK    GeneRIF: The human gene NUPL1 shares 87% sequence identity with rat
            nucleoporin p58.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590787.24, AL646102.4 and
            AL138958.18.
            
            On Aug 20, 2022 this sequence version replaced XP_005266657.1.
            
            Summary: This gene encodes a member of the nucleoporin family that
            shares 87% sequence identity with rat nucleoporin p58. The protein
            is localized to the nuclear rim and is a component of the nuclear
            pore complex (NPC). All molecules entering or leaving the nucleus
            either diffuse through or are actively transported by the NPC.
            Alternate transcriptional splice variants, encoding different
            isoforms, have been characterized. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853560.8121.1,
                                           SRR11853567.8331.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.13"
     Protein         1..566
                     /product="nucleoporin p58/p45 isoform d"
                     /note="nucleoporin p58/p45; nucleoporin-like protein 1;
                     nucleoporin like 1; 58 kDa nucleoporin; nucleoporin 58kDa"
                     /calculated_mol_wt=57763
     Region          3..566
                     /region_name="Nucleoporin_FG2"
                     /note="Nucleoporin FG repeated region; pfam15967"
                     /db_xref="CDD:435043"
     CDS             1..566
                     /gene="NUP58"
                     /gene_synonym="NUP45; NUPL1; PRO2463"
                     /coded_by="NM_001411002.1:150..1850"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS91791.1"
                     /db_xref="GeneID:9818"
                     /db_xref="HGNC:HGNC:20261"
                     /db_xref="MIM:607615"
ORIGIN      
        1 mstgfsfgsg tlgsttvaag gtstggvfsf gtgassnpsv glnfgnlgst stpattsaps
       61 sgfgtglfgs kpatgftlgg tntgiattit tgltlgtpat tsaattgfsl gfnkpaasat
      121 pfalpitsts asgltlssal tstpaastgf tlnnlggtta ttttastgls lggalaglgg
      181 slfqstntgt sglgqnalgl tlgttaatst agneglggid fssssdkksd ktgtrpedsk
      241 alkdenlppv icqdvenlqk fvkeqkqvqe eisrmsskam lkvqedikal kqllslaang
      301 iqrntlnidk lkietaqelk naeialrtqk tppglqheya apadyfrilv qqfevqlqqy
      361 rqqieelenh latqannshi tpqdlsmamq kiyqtfvala aqlqsihenv kvlkeqylgy
      421 rkmflgdavd vfetrraeak kwqntprvtt gptpfstmpn aaavamaatl tqqqqpatgf
      481 gtssgfgcst tgastfgfgt tnkpsgslsa gfgssstsgf nfsnpgitas agltfgvsnp
      541 asagfgtggq llqlkkppag nkrgkr
//
LOCUS       NP_001389612            1334 aa            linear   PRI 21-NOV-2025
DEFINITION  kinectin isoform 5 [Homo sapiens].
ACCESSION   NP_001389612
VERSION     NP_001389612.1
DBSOURCE    REFSEQ: accession NM_001402683.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1334)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1334)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1334)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1334)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1334)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1334)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1334)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1334)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1334)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1334)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138499.4.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.219200.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1334
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1334
                     /product="kinectin isoform 5"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=153510
     Site            7..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UP2.1)"
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          48..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Region          103..218
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            172
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Region          <326..>584
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            435
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Region          458..1247
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            772
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            881
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            1032
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            1061
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            1065
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Region          <1167..>1334
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            1240
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            1290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            1306
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     CDS             1..1334
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001402683.1:179..4183"
                     /note="isoform 5 is encoded by transcript variant 8"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqlsitskvq
      841 elqnllkgke eqmntmkavl eekekdlant gkwlqdlqee neslkahvqe vaqhnlkeas
      901 sasqfeelei vlkekenelk rleamlkere sdlssktqll qdvqdenklf ksqieqlkqq
      961 nyqqassfpp heellkvise rekeisglwn eldslkdave hqrkknndlr eknweameal
     1021 astekmlqdk vnktskerqq qveaveleak evlkklfpkv svpsnlsyge wlhgfekkak
     1081 ecmagtsgse evkvlehklk eademhtllq lecekyksvl aetegilqkl qrsveqeenk
     1141 wkvkvdeshk tikqmqssft sseqelerlr senkdienlr rerehlemel ekaemersty
     1201 vtevrelkdl ltelqkkldd syseavrqne elnllkaqln etltklrteq nerqkvagdl
     1261 hkaqqsleli qskivkaagd ttviensdvs petesseket msvslnqtvt qlqqllqavn
     1321 qqltkekehy qvle
//
LOCUS       NP_001428015            1231 aa            linear   PRI 21-NOV-2025
DEFINITION  cohesin subunit SA-2 isoform b [Homo sapiens].
ACCESSION   NP_001428015
VERSION     NP_001428015.1
DBSOURCE    REFSEQ: accession NM_001441086.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1231)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1231)
  AUTHORS   Fischer,A., Hernandez-Rodriguez,B., Mulet-Lazaro,R., Nuetzel,M.,
            Holzl,F., van Herk,S., Kavelaars,F.G., Stanewsky,H., Ackermann,U.,
            Niang,A.H., Diaz,N., Reuschel,E., Strieder,N., Hernandez-Lopez,I.,
            Valk,P.J.M., Vaquerizas,J.M., Rehli,M., Delwel,R. and Gebhard,C.
  TITLE     STAG2 mutations reshape the cohesin-structured spatial chromatin
            architecture to drive gene regulation in acute myeloid leukemia
  JOURNAL   Cell Rep 43 (8), 114498 (2024)
   PUBMED   39084219
  REMARK    GeneRIF: STAG2 mutations reshape the cohesin-structured spatial
            chromatin architecture to drive gene regulation in acute myeloid
            leukemia.
REFERENCE   3  (residues 1 to 1231)
  AUTHORS   Huber,J., Tanasie,N.L., Zernia,S. and Stigler,J.
  TITLE     Single-molecule imaging reveals a direct role of CTCF's zinc
            fingers in SA interaction and cluster-dependent RNA recruitment
  JOURNAL   Nucleic Acids Res 52 (11), 6490-6506 (2024)
   PUBMED   38742641
  REMARK    GeneRIF: Single-molecule imaging reveals a direct role of CTCF's
            zinc fingers in SA interaction and cluster-dependent RNA
            recruitment.
REFERENCE   4  (residues 1 to 1231)
  AUTHORS   Xu,W., Kim,J.S., Yang,T., Ya,A., Sadzewicz,L., Tallon,L.,
            Harris,B.T., Sarkaria,J., Jin,F. and Waldman,T.
  TITLE     STAG2 mutations regulate 3D genome organization, chromatin loops,
            and Polycomb signaling in glioblastoma multiforme
  JOURNAL   J Biol Chem 300 (6), 107341 (2024)
   PUBMED   38705393
  REMARK    GeneRIF: STAG2 mutations regulate 3D genome organization, chromatin
            loops, and Polycomb signaling in glioblastoma multiforme.
REFERENCE   5  (residues 1 to 1231)
  AUTHORS   Ros-Pardo,D., Gomez-Puertas,P. and Marcos-Alcalde,I.
  TITLE     STAG2: Computational Analysis of Missense Variants Involved in
            Disease
  JOURNAL   Int J Mol Sci 25 (2), 1280 (2024)
   PUBMED   38279279
  REMARK    GeneRIF: STAG2: Computational Analysis of Missense Variants
            Involved in Disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1231)
  AUTHORS   Gregson,H.C., Schmiesing,J.A., Kim,J.S., Kobayashi,T., Zhou,S. and
            Yokomori,K.
  TITLE     A potential role for human cohesin in mitotic spindle aster
            assembly
  JOURNAL   J Biol Chem 276 (50), 47575-47582 (2001)
   PUBMED   11590136
REFERENCE   7  (residues 1 to 1231)
  AUTHORS   Sumara,I., Vorlaufer,E., Gieffers,C., Peters,B.H. and Peters,J.M.
  TITLE     Characterization of vertebrate cohesin complexes and their
            regulation in prophase
  JOURNAL   J Cell Biol 151 (4), 749-762 (2000)
   PUBMED   11076961
REFERENCE   8  (residues 1 to 1231)
  AUTHORS   Carramolino,L., Lee,B.C., Zaballos,A., Peled,A., Barthelemy,I.,
            Shav-Tal,Y., Prieto,I., Carmi,P., Gothelf,Y., Gonzalez de
            Buitrago,G., Aracil,M., Marquez,G., Barbero,J.L. and Zipori,D.
  TITLE     SA-1, a nuclear protein encoded by one member of a novel gene
            family: molecular cloning and detection in hemopoietic organs
  JOURNAL   Gene 195 (2), 151-159 (1997)
   PUBMED   9305759
  REMARK    Erratum:[Gene 1998 Jan 12;206(2):283]
REFERENCE   9  (residues 1 to 1231)
  AUTHORS   Wu,C., Friedlander,P., Lamoureux,C., Zannis-Hadjopoulos,M. and
            Price,G.B.
  TITLE     cDNA clones contain autonomous replication activity
  JOURNAL   Biochim Biophys Acta 1174 (3), 241-257 (1993)
   PUBMED   7690594
REFERENCE   10 (residues 1 to 1231)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121601.13 and AL355476.12.
            
            Summary: The protein encoded by this gene is a subunit of the
            cohesin complex, which regulates the separation of sister
            chromatids during cell division. Targeted inactivation of this gene
            results in chromatid cohesion defects and aneuploidy, suggesting
            that genetic disruption of cohesin is a cause of aneuploidy in
            human cancer. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1941409.1,
                                           SRR14372080.1611934.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1231
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..1231
                     /product="cohesin subunit SA-2 isoform b"
                     /note="SCC3 homolog 2; cohesin subunit SA-2; SA2
                     stromalin; sister chromatid cohesion 3 homolog B; stromal
                     antigen 2"
                     /calculated_mol_wt=141196
     Region          1..75
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Region          102..>395
                     /region_name="IRR1"
                     /note="Cohesin [Cell division and chromosome
                     partitioning]; COG5537"
                     /db_xref="CDD:227824"
     Region          157..270
                     /region_name="STAG"
                     /note="STAG domain; pfam08514"
                     /db_xref="CDD:462502"
     Site            607
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1058
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1061
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Region          1064..1083
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1064
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35638; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1065
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35638; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1112
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     Site            1178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3U4.3)"
     CDS             1..1231
                     /gene="STAG2"
                     /gene_synonym="bA517O1.1; HPE13; MKMS; NEDXCF; SA-2; SA2;
                     SCC3B"
                     /coded_by="NM_001441086.1:428..4123"
                     /note="isoform b is encoded by transcript variant 27"
                     /db_xref="GeneID:10735"
                     /db_xref="HGNC:HGNC:11355"
                     /db_xref="MIM:300826"
ORIGIN      
        1 miaapeiptd fnllqeseth fssdtdfedi egknqkqgkg ktckkgkkgp aekgkggngg
       61 gkppsgpnrm nghhqqngve nmmlfevvkm gksamqsvvd dwiesykhdr dialldlinf
      121 fiqcsgckgv vtaemfrhmq nseiirkmte efdedsgdyp ltmagpqwkk fkssfcefig
      181 vlvrqcqysi iydeymmdtv islltglsds qvrafrhtst laamklmtal vnvalnlsin
      241 mdntqrqyea ernkmigkra nerlelllqk rkelqenqde ienmmnaifk gvfvhryrda
      301 iaeiraicie eigiwmkmys daflndsylk yvgwtmhdkq gevrlkclta lqglyynkel
      361 nsklelftsr fkdrivsmtl dkeydvavqa iklltlvlqs seevltaedc envyhlvysa
      421 hrpvavaage flykklfsrr dpeedgmmkr rgrqgpnanl vktlvfffle selhehaayl
      481 vdsmwdcate llkdwecmns llleeplsge ealtdrqesa lieimlctir qaaechppvg
      541 rgtgkrvlta kekktqlddr tkitelfava lpqllakysv daekvtnllq lpqyfdleiy
      601 ttgrlekhld allrqirniv ekhtdtdvle acsktyhalc neeftifnrv disrsqlide
      661 ladkfnrlle dflqegeepd eddayqvlst lkritafhna hdlskwdlfa cnykllktgi
      721 engdmpeqiv ihalqcthyv ilwqlakite ssstkedllr lkkqmrvfcq icqhyltnvn
      781 ttvkeqafti lcdilmifsh qimsggrdml eplvytpdss lqsellsfil dhvfieqddd
      841 nnsadgqqed easkiealhk rrnllaafck livytvvemn taadifkqym kyyndygdii
      901 ketmsktrqi dkiqcaktli lslqqlfnem iqengynfdr ssstfsgike larrfaltfg
      961 ldqlktreai amlhkdgief afkepnpqge shpplnlafl dilsefsskl lrqdkrtvyv
     1021 ylekfmtfqm slrredvwlp lmsyrnslla ggdddtmsvi sgissrgstv rskkskpstg
     1081 krkvvegmql slteessssd smwlsreqtl htpvmmqtpq ltstimrepk rlrpedsfms
     1141 vypmqtehhq tpldynrrgt slmeddeepi vedvmmsseg riedlnegmd fdtmdidlpp
     1201 sknrrertel kpdffdpasi mdesvlgvsm f
//
LOCUS       NP_001427979            4366 aa            linear   PRI 21-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HUWE1 isoform 4 [Homo sapiens].
ACCESSION   NP_001427979 XP_047297695 XP_054182291
VERSION     NP_001427979.1
DBSOURCE    REFSEQ: accession NM_001441050.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4366)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 4366)
  AUTHORS   Lee,C., Park,S.H. and Yoon,S.K.
  TITLE     The E3 ligase HUWE1 increases the sensitivity of CRC to oxaliplatin
            through TOMM20 degradation
  JOURNAL   Oncogene 43 (9), 636-649 (2024)
   PUBMED   38184713
  REMARK    GeneRIF: The E3 ligase HUWE1 increases the sensitivity of CRC to
            oxaliplatin through TOMM20 degradation.
REFERENCE   3  (residues 1 to 4366)
  AUTHORS   Li,X.X., Xu,J.K., Su,W.J., Wu,H.L., Zhao,K., Zhang,C.M., Chen,X.K.
            and Yang,L.X.
  TITLE     The role of KDM4A-mediated histone methylation on temozolomide
            resistance in glioma cells through the HUWE1/ROCK2 axis
  JOURNAL   Kaohsiung J Med Sci 40 (2), 161-174 (2024)
   PUBMED   37873881
  REMARK    GeneRIF: The role of KDM4A-mediated histone methylation on
            temozolomide resistance in glioma cells through the HUWE1/ROCK2
            axis.
REFERENCE   4  (residues 1 to 4366)
  AUTHORS   Bernassola,F., Karin,M., Ciechanover,A. and Melino,G.
  TITLE     The HECT family of E3 ubiquitin ligases: multiple players in cancer
            development
  JOURNAL   Cancer Cell 14 (1), 10-21 (2008)
   PUBMED   18598940
  REMARK    Review article
REFERENCE   5  (residues 1 to 4366)
  AUTHORS   Zhong,Q., Gao,W., Du,F. and Wang,X.
  TITLE     Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the
            polyubiquitination of Mcl-1 and regulates apoptosis
  JOURNAL   Cell 121 (7), 1085-1095 (2005)
   PUBMED   15989957
  REMARK    GeneRIF: Mule is both required and sufficient for the
            polyubiquitination of Mcl-1; Mule is a unique BH3-containing E3
            ubiquitin ligase apical to Bcl-2 family proteins during DNA
            damage-induced apoptosis
            GeneRIF: Mule (HUWE1) poly-ubiquitinates anti-apoptotic gene Mcl-1.
REFERENCE   6  (residues 1 to 4366)
  AUTHORS   Chen,D., Kon,N., Li,M., Zhang,W., Qin,J. and Gu,W.
  TITLE     ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
  JOURNAL   Cell 121 (7), 1071-1083 (2005)
   PUBMED   15989956
  REMARK    GeneRIF: study modifies the current view of ARF-mediated p53
            activation and reveals that ARF-BP1 is a critical mediator of both
            the p53-independent and p53-dependent tumor suppressor functions of
            ARF
            GeneRIF: Ubiquitin ligase activity of ARF-BP1 (HUWE1) is inhibited
            by Arf.
REFERENCE   7  (residues 1 to 4366)
  AUTHORS   Liu,Z., Oughtred,R. and Wing,S.S.
  TITLE     Characterization of E3Histone, a novel testis ubiquitin protein
            ligase which ubiquitinates histones
  JOURNAL   Mol Cell Biol 25 (7), 2819-2831 (2005)
   PUBMED   15767685
REFERENCE   8  (residues 1 to 4366)
  AUTHORS   Gu,J., Dubner,R., Fornace,A.J. Jr. and Iadarola,M.J.
  TITLE     UREB1, a tyrosine phosphorylated nuclear protein, inhibits p53
            transactivation
  JOURNAL   Oncogene 11 (10), 2175-2178 (1995)
   PUBMED   7478539
REFERENCE   9  (residues 1 to 4366)
  AUTHORS   Turner,G., Gedeon,A. and Mulley,J.
  TITLE     X-linked mental retardation with heterozygous expression and
            macrocephaly: pericentromeric gene localization
  JOURNAL   Am J Med Genet 51 (4), 575-580 (1994)
   PUBMED   7943042
REFERENCE   10 (residues 1 to 4366)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX323845.7 and AC231658.3.
            
            On or before Jun 4, 2025 this sequence version replaced
            XP_047297695.1, XP_054182291.1.
            
            Summary: This gene encodes a protein containing a C-terminal HECT
            (E6AP type E3 ubiquitin protein ligase) domain that functions as an
            E3 ubiquitin ligase. The encoded protein is required for the
            ubiquitination and subsequent degradation of the anti-apoptotic
            protein Mcl1 (myeloid cell leukemia sequence 1 (BCL2-related)).
            This protein also ubiquitinates the p53 tumor suppressor, core
            histones, and DNA polymerase beta. Mutations in this gene are
            associated with Turner type X-linked syndromic cognitive
            disability. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.476297.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..4366
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..4366
                     /product="E3 ubiquitin-protein ligase HUWE1 isoform 4"
                     /EC_number="2.3.2.26"
                     /note="Mcl-1 ubiquitin ligase E3; BJ-HCC-24 tumor antigen;
                     HECT domain protein LASU1; ARF-binding protein 1;
                     URE-binding protein 1; large structure of UREB1; upstream
                     regulatory element-binding protein 1; homologous to E6AP
                     carboxyl terminus homologous protein 9; HECT-type E3
                     ubiquitin transferase HUWE1; HECT, UBA and WWE domain
                     containing 1, E3 ubiquitin protein ligase"
                     /calculated_mol_wt=480773
     Region          92..374
                     /region_name="DUF908"
                     /note="Domain of Unknown Function (DUF908); pfam06012"
                     /db_xref="CDD:428721"
     Region          438..821
                     /region_name="DUF913"
                     /note="Domain of Unknown Function (DUF913); pfam06025"
                     /db_xref="CDD:461803"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            656
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          713..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            747
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          985..1008
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1021..1044
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1091
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1298..1327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1324..1363
                     /region_name="UBA_HUWE1"
                     /note="UBA domain found in eukaryotic E3 ubiquitin-protein
                     ligase HUWE1 and similar proteins; cd14288"
                     /db_xref="CDD:270474"
     Site            1375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1403..1422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1624..1685
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          1696..1742
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1729
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1914
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2025..2072
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2042
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2269..2349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2274
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2363..2487
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2534
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2561
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2591
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2602
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2701..2977
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          <2742..3073
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            2758
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2833
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2840
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2842
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2868
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2894
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2895
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2896
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2925
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3017..3050
                     /region_name="UBM"
                     /note="Ubiquitin binding region; pfam14377"
                     /db_xref="CDD:464159"
     Region          3043..3066
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3156
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3252..3274
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3411..3431
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3478..3519
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3544..3575
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3562
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3669
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3744..3765
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3764
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3800
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3808
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3819
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3822
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3886..3923
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3898
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3911
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3916
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3919
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          4011..4364
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(4015,4045,4056,4117,4291,4327..4328,4331..4335,4355,
                     4363)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(4145,4148..4149,4151..4152,4155,4162,4164,
                     4168..4169,4171,4176,4181,4198,4202)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     Site            4263
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P51593; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     CDS             1..4366
                     /gene="HUWE1"
                     /gene_synonym="ARF-BP1; HECTH9; HSPC272; Ib772; LASU1;
                     MRXST; MULE; URE-B1; UREB1"
                     /coded_by="NM_001441050.1:394..13494"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:10075"
                     /db_xref="HGNC:HGNC:30892"
                     /db_xref="MIM:300697"
ORIGIN      
        1 mkvdrtklkk tpteapadcr alidklkvcn deqlllelqq iktwnigkce lyhwvdlldr
       61 fdgiladagq tvenmswmlv cdrpereqlk mlllavlnft allieysfsr hlyssiehlt
      121 tllassdmqv vlavlnllyv fskrsnyitr lgsdkrtpll trlqhlaesw ggkengfgla
      181 eccrdlhmmk yppsattlhf efyadpgaev kiekrttsnt lhyihieqld kisespseim
      241 esltkmysip kdkqmllfth irlahgfsnh rkrlqavqar lhaisilvfv spfavysnal
      301 qesansilyn glieelvdvl qitdkqlmei kaaslrtlts ivhlertpkl ssiidctgta
      361 syhgflpvlv rnciqamidp smdpyphqfa talfsflyhl asydaggeal vscgmmeall
      421 kvikflgdeq dqitfvtrav rvvdlitnld maafqshsgl sifiyrlehe vdlcrkecpf
      481 vikpkiqrpn ttqegeemet dmdgvqcipq raallksmln flkkaiqdpa fsdgirhvmd
      541 gslptslkhi isnaeyygps lfllatevvt vfvfqepsll sslqdngltd vmlhallikd
      601 vpatrevlgs lpnvfsalcl narglqsfvq cqpferlfkv llspdylpam rrrrssdplg
      661 dtasnlgsav delmrhqptl ktdattaiik lleeicnlgr dpkyicqkps iqkadgtata
      721 ppprsnhaae eassedeeee evqamqsfns tqqnetepnq qvvgteerip iplmdyilnv
      781 mkfvesilsn nttddhcqef vnqkgllplv tilglpnlpi dfptsaacqa vagvcksilt
      841 lshepkvlqe gllqldsils sleplhrpie spggsvllre lacagnvada tlsaqatpll
      901 haltaahayi mmfvhtcrvg qseirsisvn qwgsqlglsv lsklsqlycs lvwestvlls
      961 lctpnslpsg cefgqadmqk lvpkdekagt tqggkrsdge qdgaagsmda stqgllegig
     1021 ldgdtlapme tdeptasdsk gkskitpama arikqikpll sassrlgral aelfgllvkl
     1081 cvgspvrqrr shhaasttta ptpaarstas altklltkgl swqpppytpt prfrltffic
     1141 svgftspmlf derkypyhlm lqkflcsggh nalfetfnwa lsmggkvpvs eglehsdlpd
     1201 gtgefldawl mlvekmvnpt tvlesphslp aklpggvqnf pqfsalrflv vtqkaaftci
     1261 knlwnrkplk vyggrmaesm lailchilrg epvirerlsk ekegsrgeed tgqeeggsrr
     1321 epqvnqqqlq qlmdmgftre hameallnts tmeqateyll thpppimggv vrdlsmseed
     1381 qmmraiamsl gqdipmdqra espeevacrk eeeerkarek qeeeeakcle kfqdadpleq
     1441 delhtftdtm lpgcfhllde lpdtvyrvcd limtaikrng adyrdmilkq vvnqvweaad
     1501 vlikaalplt tsdtktvsew isqmatlpqa snlatrilll tllfeelklp cawvvessgi
     1561 lnvlikllev vqpclqaake qkevqtpkwi tpvlllidfy ektaisskrr aqmtkylqsn
     1621 snnwrwfddr sgrwcsysas nnstidsawk sgetsvrfta grrrytvqft tmvqvneetg
     1681 nrrpvmltll rvprlnknsk nsngqelekt leeskemdik rkenkgndtp lalestntek
     1741 etsleetkig eiliqglted mvtvliracv smlgvpvdpd tlhatlrlcl rltrdhkyam
     1801 mfaelkstrm ilnltqssgf ngftplvtll lrhiiedpct lrhtmekvvr saatsgagst
     1861 tsgvvsgslg sreinyilrv lgpaacrnpd iftevancci rialpaprgs gtasddefen
     1921 lrikgpnavq lvkttplkps plpvipdtik eviydmlnal aayhapeead ksdpkpgvmt
     1981 qevgqllqdm gddvyqqyrs ltrqssdfdt qsgfsinsqv faadgastet sasgtsqgea
     2041 stpeesrdgk kdkegdrase egkqkgkgsk plmptstilr llaelvrsyv giatlianys
     2101 ytvgqselik edcsvlafvl dhllphtqna edkdtpalar lflaslaaag sgtdaqvalv
     2161 nevkaalgra lamaestekh arlqavmcii stimescpst ssfyssatak tqhngmnnii
     2221 rlflkkglvn dlarvphsld lsspnmantv naalkpletl srivnqpssl fgsksasskn
     2281 kseqdaqgas qdsssnqqdp gepgeaevqe edhdvtqtev adgdimdgea etdsvviagq
     2341 pevlssqemq veneledlid ellerdggsg nstiivsrsg edesqedvlm deapsnlsqa
     2401 stlqanreds mnildpedee ehtqeedssg snededdsqd eeeeeeedee ddqeddegee
     2461 gdedddddgs emeldedypd mnasplvrfe rfdreddlii efdnmfssat dippspgnip
     2521 tthplmvrha dhssltlgsg ssttrltqgi grsqrtlrql tantghtihv hypgnrqpnp
     2581 plilqrllgp saaadilqls sslplqsrgr arllvgnddv hiiarsddel lddffhdqst
     2641 atsqagtlss iptaltrwte eckvldaesm hdcvsvvkvs ivnhleflrd eeleerrekr
     2701 rkqlaeeetk itdkgkedke nrdqsaqcta sksndsteqn lsdgtpmpds ypttpsstda
     2761 atsesketlg tlqssqqqpt lptppalgev pqelqspage ggsstqllmp vepeelgptr
     2821 psgeaettqm elspaptits lsperaedsd altavssqle gspmdtssla sctleeavgd
     2881 tsaagsseqp ragsstpgda ppavaevqgr sdgsgesaqp pedssppass essstrdsav
     2941 aisgadsrgi leeplpstss eeedplagis lpegvdpsfl aalpddirre vlqnqlgirp
     3001 ptrtapstns sapavvgnpg vtevspefla alppaiqeev laqqraeqqr relaqnassd
     3061 tpmdpvtfiq tlpsdlrrsv ledmedsvla vmppdiaaea qalrreqear qrqlmherlf
     3121 ghsstsalsa ilrspaftsr lsgnrgvqyt rlavqrggtf qmggssshnr psgsnvdtll
     3181 rlrgrllldh ealscllvll fvdepklnts rlhrvlrnlc yhaqtrhwvi rsllsilqrs
     3241 seselcietp klttseekgk ksskscgsss henrpldllh kmeskssnql swlsvsmdaa
     3301 lgcrtnifqi qrsggrkhte khasggstvh ihpqaapvvc rhvldtliql akvfpshftq
     3361 qrtketnces drergnkacs pcssqssssg ictdfwdllv kldnmnvsrk gknsvksvpv
     3421 saggegetsp ysleasplgq lmnmlshpvi rrsslltekl lrllslisia lpenkvseaq
     3481 ansgsgasst ttatsttstt tttaasttpt pptaptpvts apalvaatai stivvaastt
     3541 vttpttattt vsispttkgs kspakvsdgg ssstdfkmvs sgltenqlql svevltshsc
     3601 seegledaan vllqlsrgds gtrdtvlkll lngarhlgyt lckqigtlla elreynleqq
     3661 rraqcetlsp dglpeeqpqt tklkgkmqsr fdmaenvviv asqkrplggr elqlpsmsml
     3721 tsktstqkff lrvlqviiql rddtrrankk akqtgrlgss glgsassiqa avrqleaead
     3781 aiiqmsessq seasvrrees pmdvdqpsps aqdtqsiasd gtpqgekeke erppelplls
     3841 eqlsldelwd mlgeclkele eshdqhavlv lqpaveaffl vhatereskp pvrdtresql
     3901 ahikdepppl spapltpatp ssldpffsre pssmhisssl ppdtqkflrf aethrtvlnq
     3961 ilrqstthla dgpfavlvdy irvldfdvkr kyfrqelerl deglrkedma vhvrrdhvfe
     4021 dsyrelhrks peemknrlyi vfegeegqda ggllrewymi isremfnpmy alfrtspgdr
     4081 vtytinpssh cnpnhlsyfk fvgrivakav ydnrllecyf trsfykhilg ksvrytdmes
     4141 edyhfyqglv yllendvstl gydltfstev qefgvcevrd lkpnganilv teenkkeyvh
     4201 lvcqmrmtga irkqlaafle gfyeiipkrl isifteqele llisglptid iddlksntey
     4261 hkyqsnsiqi qwfwralrsf dqadrakflq fvtgtskvpl qgfaalegmn giqkfqihrd
     4321 drstdrlpsa htcfnqldlp ayesfeklrh mlllaiqecs egfgla
//
LOCUS       NP_001402872             419 aa            linear   PRI 21-NOV-2025
DEFINITION  synaptotagmin-1 isoform 2 [Homo sapiens].
ACCESSION   NP_001402872
VERSION     NP_001402872.1
DBSOURCE    REFSEQ: accession NM_001415943.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Stephan,G., Haddock,S., Wang,S., Erdjument-Bromage,H., Liu,W.,
            Ravn-Boess,N., Frenster,J.D., Bready,D., Cai,J., Ronnen,R.,
            Sabio-Ortiz,J., Fenyo,D., Neubert,T.A. and Placantonakis,D.G.
  TITLE     Modulation of GPR133 (ADGRD1) signaling by its intracellular
            interaction partner extended synaptotagmin 1
  JOURNAL   Cell Rep 43 (5), 114229 (2024)
   PUBMED   38758649
  REMARK    GeneRIF: Modulation of GPR133 (ADGRD1) signaling by its
            intracellular interaction partner extended synaptotagmin 1.
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Zhang,J., Ren,G., Huang,T., Sang,Y., Zhong,Y. and Yi,Y.
  TITLE     miRNA-363-3p Hinders Proliferation, Migration, Invasion and
            Autophagy of Thyroid Cancer Cells by Controlling SYT1 Transcription
            to affect NF-kappaB
  JOURNAL   Endocr Metab Immune Disord Drug Targets 24 (1), 153-162 (2024)
   PUBMED   37150983
  REMARK    GeneRIF: miRNA-363-3p Hinders Proliferation, Migration, Invasion
            and Autophagy of Thyroid Cancer Cells by Controlling SYT1
            Transcription to affect NF-kappaB.
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Yamada,K., Motohashi,S., Oikawa,T., Tago,N., Koizumi,R., Ono,M.,
            Tachibana,T., Yoshida,A., Yoshida,S., Shimoda,M., Oka,M., Yoneda,Y.
            and Yoshida,K.
  TITLE     Extended-synaptotagmin 1 engages in unconventional protein
            secretion mediated via SEC22B+ vesicle pathway in liver cancer
  JOURNAL   Proc Natl Acad Sci U S A 119 (36), e2202730119 (2022)
   PUBMED   36044553
  REMARK    GeneRIF: Extended-synaptotagmin 1 engages in unconventional protein
            secretion mediated via SEC22B(+) vesicle pathway in liver cancer.
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Thibord,F., Chan,M.V., Chen,M.H. and Johnson,A.D.
  TITLE     A year of COVID-19 GWAS results from the GRASP portal reveals
            potential genetic risk factors
  JOURNAL   HGG Adv 3 (2), 100095 (2022)
   PUBMED   35224516
REFERENCE   6  (residues 1 to 419)
  AUTHORS   McMahon,H.T., Missler,M., Li,C. and Sudhof,T.C.
  TITLE     Complexins: cytosolic proteins that regulate SNAP receptor function
  JOURNAL   Cell 83 (1), 111-119 (1995)
   PUBMED   7553862
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Chowdhury,D., Travis,G.H., Sutcliffe,J.G. and Burton,F.H.
  TITLE     Synaptotagmin I and 1B4 are identical: implications for
            synaptotagmin distribution in the primate brain
  JOURNAL   Neurosci Lett 190 (1), 9-12 (1995)
   PUBMED   7624059
REFERENCE   8  (residues 1 to 419)
  AUTHORS   Mochly-Rosen,D., Miller,K.G., Scheller,R.H., Khaner,H., Lopez,J.
            and Smith,B.L.
  TITLE     p65 fragments, homologous to the C2 region of protein kinase C,
            bind to the intracellular receptors for protein kinase C
  JOURNAL   Biochemistry 31 (35), 8120-8124 (1992)
   PUBMED   1326322
REFERENCE   9  (residues 1 to 419)
  AUTHORS   Perin,M.S., Johnston,P.A., Ozcelik,T., Jahn,R., Francke,U. and
            Sudhof,T.C.
  TITLE     Structural and functional conservation of synaptotagmin (p65) in
            Drosophila and humans
  JOURNAL   J Biol Chem 266 (1), 615-622 (1991)
   PUBMED   1840599
REFERENCE   10 (residues 1 to 419)
  AUTHORS   Blaustein,R.O., Germann,W.J., Finkelstein,A. and DasGupta,B.R.
  TITLE     The N-terminal half of the heavy chain of botulinum type A
            neurotoxin forms channels in planar phospholipid bilayers
  JOURNAL   FEBS Lett 226 (1), 115-120 (1987)
   PUBMED   2446925
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073606.19, AC090709.6,
            AC073616.17, AC073572.19, AC078917.14 and AC027288.26.
            
            Summary: This gene encodes a member of the synaptotagmin protein
            family. The synaptotagmins are integral membrane proteins of
            synaptic vesicles that serve as calcium sensors in the process of
            vesicular trafficking and exocytosis. The encoded protein
            participates in triggering neurotransmitter release at the synapse
            in response to calcium binding. Mutations in this gene are
            associated with Baker-Gordon syndrome. [provided by RefSeq, Jan
            2023].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.146456.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968189,
                                           SAMEA1968968 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: locus in the vicinity of disease-associated
                                   variant(s)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.2"
     Protein         1..419
                     /product="synaptotagmin-1 isoform 2"
                     /note="sytI; synaptotagmin I"
                     /calculated_mol_wt=47130
     Region          6..113
                     /region_name="Syt1_N"
                     /note="N-terminal domain of synaptotagmin-1 (Syt1) and
                     similar proteins; cd21963"
                     /db_xref="CDD:409248"
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            order(40,43..44,46..48,50..51)
                     /site_type="other"
                     /note="Botolinum neurotoxin B binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409248"
     Site            58..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Region          133..379
                     /region_name="Phospholipid binding. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P21579.1)"
     Region          140..262
                     /region_name="C2A_Synaptotagmin-1-5-6-9-10"
                     /note="C2A domain first repeat present in Synaptotagmins
                     1, 5, 6, 9, and 10; cd08385"
                     /db_xref="CDD:176031"
     Site            order(170,176,228,230,236)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176031"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P46096; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46096; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Region          271..406
                     /region_name="C2B_Synaptotagmin-1"
                     /note="C2 domain second repeat present in Synaptotagmin 1;
                     cd08402"
                     /db_xref="CDD:176047"
     Site            order(301,307,361,363,369)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176047"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21707; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21707; propagated from
                     UniProtKB/Swiss-Prot (P21579.1)"
     CDS             1..419
                     /gene="SYT1"
                     /gene_synonym="BAGOS; P65; SVP65; SYT"
                     /coded_by="NM_001415943.1:642..1901"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="GeneID:6857"
                     /db_xref="HGNC:HGNC:11509"
                     /db_xref="MIM:185605"
ORIGIN      
        1 mvseshheal aappvttvat vlpsnatepa spgegkedaf sklkekfmne lhkiplppwa
       61 liaiaivavl lvltccfcic kkclfkkknk kkgkekggkn ainmkdvkdl gktmkdqddd
      121 aetgltdgee keepkeeekl gklqysldyd fqnnqllvgi iqaaelpald mggtsdpyvk
      181 vfllpdkkkk fetkvhrktl npvfneqftf kvpyselggk tlvmavydfd rfskhdiige
      241 fkvpmntvdf ghvteewrdl qsaekeeqek lgdicfslry vptagkltvv ileaknlkkm
      301 dvgglsdpyv kihlmqngkr lkkkkttikk ntlnpyynes fsfevpfeqi qkvqvvvtvl
      361 dydkigknda igkvfvgyns tgaelrhwsd mlanprrpia qwhtlqveee vdamlavkk
//
LOCUS       NP_001309041             541 aa            linear   PRI 21-NOV-2025
DEFINITION  2-hydroxyacylsphingosine 1-beta-galactosyltransferase precursor
            [Homo sapiens].
ACCESSION   NP_001309041 XP_011530534
VERSION     NP_001309041.2
DBSOURCE    REFSEQ: accession NM_001322112.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Ji,J., Xie,M., Qian,Q., Xu,Y., Shi,W., Chen,Z., Ren,D., Liu,W.,
            He,X., Lv,M., Ma,J., Liu,W., Li,A. and Liu,B.
  TITLE     SOX9-mediated UGT8 expression promotes glycolysis and maintains the
            malignancy of non-small cell lung cancer
  JOURNAL   Biochem Biophys Res Commun 587, 139-145 (2022)
   PUBMED   34872002
  REMARK    GeneRIF: SOX9-mediated UGT8 expression promotes glycolysis and
            maintains the malignancy of non-small cell lung cancer.
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Reza,S., Ugorski,M. and Suchanski,J.
  TITLE     Glucosylceramide and galactosylceramide, small glycosphingolipids
            with significant impact on health and disease
  JOURNAL   Glycobiology 31 (11), 1416-1434 (2021)
   PUBMED   34080016
  REMARK    Review article
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Lemay,A.M., Courtemanche,O., Couttas,T.A., Jamsari,G., Gagne,A.,
            Bosse,Y., Joubert,P., Don,A.S. and Marsolais,D.
  TITLE     High FA2H and UGT8 transcript levels predict hydroxylated
            hexosylceramide accumulation in lung adenocarcinoma
  JOURNAL   J Lipid Res 60 (10), 1776-1786 (2019)
   PUBMED   31409741
  REMARK    GeneRIF: High FA2H and UGT8 transcript levels predict hydroxylated
            hexosylceramide accumulation in lung adenocarcinoma
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Cao,Q., Chen,X., Wu,X., Liao,R., Huang,P., Tan,Y., Wang,L., Ren,G.,
            Huang,J. and Dong,C.
  TITLE     Inhibition of UGT8 suppresses basal-like breast cancer progression
            by attenuating sulfatide-alphaVbeta5 axis
  JOURNAL   J Exp Med 215 (6), 1679-1692 (2018)
   PUBMED   29728441
  REMARK    GeneRIF: UGT8 is a potential prognostic indicator and druggable
            target of basal-like breast cancer.
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Tencomnao,T., Kapitonov,D., Bieberich,E. and Yu,R.K.
  TITLE     Transcriptional regulation of the human UDP-galactose:ceramide
            galactosyltransferase (hCGT) gene expression: functional role of
            GC-box and CRE
  JOURNAL   Glycoconj J 20 (5), 339-351 (2004)
   PUBMED   15229398
  REMARK    GeneRIF: the GC-box and CRE function cooperatively, and that the
            CRE regulates the cell-specific expression of the hCGT gene
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Sprong,H., Degroote,S., Nilsson,T., Kawakita,M., Ishida,N., van der
            Sluijs,P. and van Meer,G.
  TITLE     Association of the Golgi UDP-galactose transporter with
            UDP-galactose:ceramide galactosyltransferase allows UDP-galactose
            import in the endoplasmic reticulum
  JOURNAL   Mol Biol Cell 14 (8), 3482-3493 (2003)
   PUBMED   12925779
  REMARK    Erratum:[Mol Biol Cell. 2003 Sep;14(9):preceding table of contents]
REFERENCE   7  (residues 1 to 541)
  AUTHORS   Iida,A., Saito,S., Sekine,A., Mishima,C., Kitamura,Y., Kondo,K.,
            Harigae,S., Osawa,S. and Nakamura,Y.
  TITLE     Catalog of 86 single-nucleotide polymorphisms (SNPs) in three
            uridine diphosphate glycosyltransferase genes: UGT2A1, UGT2B15, and
            UGT8
  JOURNAL   J Hum Genet 47 (10), 505-510 (2002)
   PUBMED   12376738
  REMARK    GeneRIF: Single-nucleotide polymorphisms (SNPs) were found in UGT8
            gene
REFERENCE   8  (residues 1 to 541)
  AUTHORS   Sprong,H., Kruithof,B., Leijendekker,R., Slot,J.W., van Meer,G. and
            van der Sluijs,P.
  TITLE     UDP-galactose:ceramide galactosyltransferase is a class I integral
            membrane protein of the endoplasmic reticulum
  JOURNAL   J Biol Chem 273 (40), 25880-25888 (1998)
   PUBMED   9748263
REFERENCE   9  (residues 1 to 541)
  AUTHORS   Kapitonov,D. and Yu,R.K.
  TITLE     Cloning, characterization, and expression of human ceramide
            galactosyltransferase cDNA
  JOURNAL   Biochem Biophys Res Commun 232 (2), 449-453 (1997)
   PUBMED   9125199
REFERENCE   10 (residues 1 to 541)
  AUTHORS   Bosio,A., Binczek,E., Le Beau,M.M., Fernald,A.A. and Stoffel,W.
  TITLE     The human gene CGT encoding the UDP-galactose ceramide galactosyl
            transferase (cerebroside synthase): cloning, characterization, and
            assignment to human chromosome 4, band q26
  JOURNAL   Genomics 34 (1), 69-75 (1996)
   PUBMED   8661025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC127386.5 and AC122938.3.
            
            On Feb 23, 2022 this sequence version replaced NP_001309041.1.
            
            Summary: The protein encoded by this gene belongs to the
            UDP-glycosyltransferase family. It catalyzes the transfer of
            galactose to ceramide, a key enzymatic step in the biosynthesis of
            galactocerebrosides, which are abundant sphingolipids of the myelin
            membrane of the central and peripheral nervous systems.
            Alternatively spliced transcript variants have been found for this
            gene. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (3) contains an additional 5'
            non-coding exon compared to variant 1. Variants 1-5 encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.218077.1,
                                           SRR18074969.2100928.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..541
                     /product="2-hydroxyacylsphingosine
                     1-beta-galactosyltransferase precursor"
                     /EC_number="2.4.1.47"
                     /note="cerebroside synthase; 2-hydroxyacylsphingosine
                     1-beta-galactosyltransferase; uridine diphosphate
                     glycosyltransferase 8; ceramide UDP-galactosyltransferase;
                     UDP-galactose-ceramide galactosyltransferase"
                     /calculated_mol_wt=59196
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2260
     mat_peptide     21..541
                     /product="2-hydroxyacylsphingosine
                     1-beta-galactosyltransferase. /id=PRO_0000036064"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16880.2)"
                     /calculated_mol_wt=59196
     Region          21..502
                     /region_name="Glycosyltransferase_GTB-type"
                     /note="glycosyltransferase family 1 and related proteins
                     with GTB topology; cl10013"
                     /db_xref="CDD:471961"
     Site            order(33..34,36,186,189..190,194,221,295,358,360,362..363,
                     366)
                     /site_type="active"
                     /db_xref="CDD:340817"
     Site            order(33,295,358,360,362..363)
                     /site_type="active"
                     /note="TDP-binding site [active]"
                     /db_xref="CDD:340817"
     Site            34
                     /site_type="active"
                     /note="acceptor substrate-binding pocket [active]"
                     /db_xref="CDD:340817"
     Site            78
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16880.2)"
     Site            333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16880.2)"
     Site            442
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16880.2)"
     Site            472..492
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16880.2)"
     CDS             1..541
                     /gene="UGT8"
                     /gene_synonym="CGT; UGT4"
                     /coded_by="NM_001322112.2:679..2304"
                     /db_xref="CCDS:CCDS3705.1"
                     /db_xref="GeneID:7368"
                     /db_xref="HGNC:HGNC:12555"
                     /db_xref="MIM:601291"
ORIGIN      
        1 mksytpyfil lwsavgiaka akiiivppim feshmyifkt lasalhergh htvfllsegr
       61 diapsnhysl qrypgifnst tsdaflqskm rnifsgrlta ielfdildhy tkncdlmvgn
      121 haliqglkke kfdlllvdpn dmcgfviahl lgvkyavfst glwypaevga paplayvpef
      181 nslltdrmnl lqrmkntgvy lisrlgvsfl vlpkyerimq kynllpeksm ydlvhgsslw
      241 mlctdvalef prptlpnvvy vggiltkpas plpedlqrwv nganehgfvl vsfgagvkyl
      301 sedianklag algrlpqkvi wrfsgpkpkn lgnntkliew lpqndllghs kikaflshgg
      361 lnsifetiyh gvpvvgiplf gdhydtmtrv qakgmgille wktvtekely ealvkvinnp
      421 syrqraqkls eihkdqpghp vnrtiywidy iirhngahhl raavhqisfc qyflldiafv
      481 lllgaallyf llswvtkfiy rkikslwsrn khstvnghyh ngilngkykr nghikhekkv
      541 k
//
LOCUS       NP_001397770             261 aa            linear   PRI 21-NOV-2025
DEFINITION  zinc finger and SCAN domain-containing protein 9 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001397770 XP_016866756
VERSION     NP_001397770.1
DBSOURCE    REFSEQ: accession NM_001410841.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Ravasi,T., Suzuki,H., Cannistraci,C.V., Katayama,S., Bajic,V.B.,
            Tan,K., Akalin,A., Schmeier,S., Kanamori-Katayama,M., Bertin,N.,
            Carninci,P., Daub,C.O., Forrest,A.R., Gough,J., Grimmond,S.,
            Han,J.H., Hashimoto,T., Hide,W., Hofmann,O., Kamburov,A., Kaur,M.,
            Kawaji,H., Kubosaki,A., Lassmann,T., van Nimwegen,E.,
            MacPherson,C.R., Ogawa,C., Radovanovic,A., Schwartz,A.,
            Teasdale,R.D., Tegner,J., Lenhard,B., Teichmann,S.A., Arakawa,T.,
            Ninomiya,N., Murakami,K., Tagami,M., Fukuda,S., Imamura,K., Kai,C.,
            Ishihara,R., Kitazume,Y., Kawai,J., Hume,D.A., Ideker,T. and
            Hayashizaki,Y.
  TITLE     An atlas of combinatorial transcriptional regulation in mouse and
            man
  JOURNAL   Cell 140 (5), 744-752 (2010)
   PUBMED   20211142
  REMARK    Erratum:[Cell. 2010 Apr 16;141(2):369. Kamburov, Atanas [added];
            Kaur, Mandeep [added]; MacPherson, Cameron Ross [added];
            Radovanovic, Aleksandar [added]; Schwartz, Ariel [added]]
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Williams,A.J., Blacklow,S.C. and Collins,T.
  TITLE     The zinc finger-associated SCAN box is a conserved oligomerization
            domain
  JOURNAL   Mol Cell Biol 19 (12), 8526-8535 (1999)
   PUBMED   10567577
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Lee,P.L., Gelbart,T., West,C., Adams,M., Blackstone,R. and
            Beutler,E.
  TITLE     Three genes encoding zinc finger proteins on human chromosome
            6p21.3: members of a new subclass of the Kruppel gene family
            containing the conserved SCAN box domain
  JOURNAL   Genomics 43 (2), 191-201 (1997)
   PUBMED   9244436
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL022393.1.
            
            On Aug 16, 2022 this sequence version replaced XP_016866756.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.4172992.1,
                                           SRR14372079.2183021.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.1"
     Protein         1..261
                     /product="zinc finger and SCAN domain-containing protein 9
                     isoform 3"
                     /note="cell proliferation-inducing protein 12; cell
                     proliferation-inducing gene 12 protein; zinc finger and
                     SCAN domain-containing protein 9; zinc finger protein 193"
                     /calculated_mol_wt=29784
     Region          48..160
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     CDS             1..261
                     /gene="ZSCAN9"
                     /gene_synonym="PRD51; ZNF193"
                     /coded_by="NM_001410841.1:103..888"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS93875.1"
                     /db_xref="GeneID:7746"
                     /db_xref="HGNC:HGNC:12984"
                     /db_xref="MIM:602246"
ORIGIN      
        1 mntnskevls lgvqvpeawe elltmkveak shlqwqesrl krsnplarei frrhfrqlcy
       61 qetpgpreal trlqelcyqw lrphvstkeq ildllvleqf lsilpkelqg wvrehcpesg
      121 eeavilledl ereldepqhe mvahrhrqev lckemvplae qtpltlqsqp kepqltcdsa
      181 qkchsigetg egqhlfdver ippgqaktnn kpragktgdp ktpyqiavmv ssseslvcss
      241 ltllpacrll peyhpgsfld f
//
LOCUS       NP_001427437             583 aa            linear   PRI 21-NOV-2025
DEFINITION  radixin isoform 2 [Homo sapiens].
ACCESSION   NP_001427437
VERSION     NP_001427437.1
DBSOURCE    REFSEQ: accession NM_001440508.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 583)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Kruse,T., Benz,C., Garvanska,D.H., Lindqvist,R., Mihalic,F.,
            Coscia,F., Inturi,R., Sayadi,A., Simonetti,L., Nilsson,E., Ali,M.,
            Kliche,J., Moliner Morro,A., Mund,A., Andersson,E., McInerney,G.,
            Mann,M., Jemth,P., Davey,N.E., Overby,A.K., Nilsson,J. and
            Ivarsson,Y.
  TITLE     Large scale discovery of coronavirus-host factor protein
            interaction motifs reveals SARS-CoV-2 specific mechanisms and
            vulnerabilities
  JOURNAL   Nat Commun 12 (1), 6761 (2021)
   PUBMED   34799561
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 583)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 583)
  AUTHORS   Stemmer-Rachamimov,A.O., Gonzalez-Agosti,C., Xu,L., Burwick,J.A.,
            Beauchamp,R., Pinney,D., Louis,D.N. and Ramesh,V.
  TITLE     Expression of NF2-encoded merlin and related ERM family proteins in
            the human central nervous system
  JOURNAL   J Neuropathol Exp Neurol 56 (6), 735-742 (1997)
   PUBMED   9184664
REFERENCE   7  (residues 1 to 583)
  AUTHORS   Hirao,M., Sato,N., Kondo,T., Yonemura,S., Monden,M., Sasaki,T.,
            Takai,Y., Tsukita,S. and Tsukita,S.
  TITLE     Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma
            membrane association: possible involvement of phosphatidylinositol
            turnover and Rho-dependent signaling pathway
  JOURNAL   J Cell Biol 135 (1), 37-51 (1996)
   PUBMED   8858161
REFERENCE   8  (residues 1 to 583)
  AUTHORS   Wilgenbus,K.K., Milatovich,A., Francke,U. and Furthmayr,H.
  TITLE     Molecular cloning, cDNA sequence, and chromosomal assignment of the
            human radixin gene and two dispersed pseudogenes
  JOURNAL   Genomics 16 (1), 199-206 (1993)
   PUBMED   8486357
REFERENCE   9  (residues 1 to 583)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 583)
  AUTHORS   Sato,N., Funayama,N., Nagafuchi,A., Yonemura,S., Tsukita,S. and
            Tsukita,S.
  TITLE     A gene family consisting of ezrin, radixin and moesin. Its specific
            localization at actin filament/plasma membrane association sites
  JOURNAL   J Cell Sci 103 (Pt 1), 131-143 (1992)
   PUBMED   1429901
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002788.3 and AP000901.5.
            
            Summary: Radixin is a cytoskeletal protein that may be important in
            linking actin to the plasma membrane. It is highly similar in
            sequence to both ezrin and moesin. The radixin gene has been
            localized by fluorescence in situ hybridization to 11q23. A
            truncated version representing a pseudogene (RDXP2) was assigned to
            Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was
            mapped to 11p by Southern and PCR analyses. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.683140.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..583
                     /product="radixin isoform 2"
                     /calculated_mol_wt=68433
     Region          7..206
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          200..296
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(242..243,245..251,260,281,284..285,288)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(242,245..252,260,281,284..285,288)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(278,282)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            281..296
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          310..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35241.1)"
     Region          347..456
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          376..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35241.1)"
     Region          462..526
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35241.1)"
     Region          507..583
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ROCK2.
                     /evidence=ECO:0000250|UniProtKB:P26043; propagated from
                     UniProtKB/Swiss-Prot (P35241.1)"
     CDS             1..583
                     /gene="RDX"
                     /gene_synonym="DFNB24"
                     /coded_by="NM_001440508.1:421..2172"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="GeneID:5962"
                     /db_xref="HGNC:HGNC:9944"
                     /db_xref="MIM:179410"
ORIGIN      
        1 mpkpinvrvt tmdaelefai qpnttgkqlf dqvvktvglr evwffglqyv dskgystwlk
       61 lnkkvtqqdv kkenplqfkf rakffpedvs eeliqeitqr lfflqvkeai lndeiycppe
      121 tavllasyav qakygdynke ihkpgyland rllpqrvleq hkltkeqwee riqnwheehr
      181 gmlredsmme ylkiaqdlem ygvnyfeikn kkgtelwlgv dalglniyeh ddkltpkigf
      241 pwseirnisf ndkkfvikpi dkkapdfvfy aprlrinkri lalcmgnhel ymrrrkpdti
      301 evqqmkaqar eekhqkqler aqlenekkkr eiaekekeri erekeelmer lkqieeqtik
      361 aqkeleeqtr kaleldqerk rakeeaerle kerraaeeak saiakqaadq mknqeqlaae
      421 laeftakial leeakkkkee eatewqhkaf aaqedlektk eelktvmsap pppppppvip
      481 ptenehdehd ennaeasael snegvmnhrs eeervtetqk nervkkqlqa lsselaqard
      541 etkktqndvl haenvkagrd kyktlrqirq gntkqridef eam
//
LOCUS       NP_001427729            1217 aa            linear   PRI 21-NOV-2025
DEFINITION  phosphorylase b kinase regulatory subunit alpha, liver isoform
            isoform 2 [Homo sapiens].
ACCESSION   NP_001427729 XP_005274605 XP_054183176
VERSION     NP_001427729.1
DBSOURCE    REFSEQ: accession NM_001440800.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1217)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1217)
  AUTHORS   Dong,R., Wei,X., Zhang,K., Song,F., Lv,Y., Gao,M., Wang,D., Ma,J.,
            Gai,Z. and Liu,Y.
  TITLE     Genotypic and phenotypic characteristics of 12 chinese children
            with glycogen storage diseases
  JOURNAL   Front Genet 13, 932760 (2022)
   PUBMED   36105079
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1217)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1217)
  AUTHORS   Benner,A., Alhaidan,Y., Lines,M.A., Brusgaard,K., De Leon,D.D.,
            Sparkes,R., Frederiksen,A.L. and Christesen,H.T.
  TITLE     PHKA2 variants expand the phenotype of phosphorylase B kinase
            deficiency to include patients with ketotic hypoglycemia only
  JOURNAL   Am J Med Genet A 185 (10), 2959-2975 (2021)
   PUBMED   34117828
  REMARK    GeneRIF: PHKA2 variants expand the phenotype of phosphorylase B
            kinase deficiency to include patients with ketotic hypoglycemia
            only.
REFERENCE   5  (residues 1 to 1217)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1217)
  AUTHORS   Herbert,M., Goldstein,J.L., Rehder,C., Austin,S., Kishnani,P.S. and
            Bali,D.S.
  TITLE     Phosphorylase Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21634085
REFERENCE   7  (residues 1 to 1217)
  AUTHORS   Davidson,J.J., Ozcelik,T., Hamacher,C., Willems,P.J., Francke,U.
            and Kilimann,M.W.
  TITLE     cDNA cloning of a liver isoform of the phosphorylase kinase alpha
            subunit and mapping of the gene to Xp22.2-p22.1, the region of
            human X-linked liver glycogenosis
  JOURNAL   Proc Natl Acad Sci U S A 89 (6), 2096-2100 (1992)
   PUBMED   1372435
REFERENCE   8  (residues 1 to 1217)
  AUTHORS   Wauters,J.G., Bossuyt,P.J., Davidson,J., Hendrickx,J.,
            Kilimann,M.W. and Willems,P.J.
  TITLE     Regional mapping of a liver alpha-subunit gene of phosphorylase
            kinase (PHKA) to the distal region of human chromosome Xp
  JOURNAL   Cytogenet Cell Genet 60 (3-4), 194-196 (1992)
   PUBMED   1505214
REFERENCE   9  (residues 1 to 1217)
  AUTHORS   Willems,P.
  TITLE     Families with X-linked liver glycogenosis due to phosphorylase
            kinase deficiency
  JOURNAL   Clin Genet 38 (1), 80 (1990)
   PUBMED   2387090
REFERENCE   10 (residues 1 to 1217)
  AUTHORS   Willems,P.J., Gerver,W.J., Berger,R. and Fernandes,J.
  TITLE     The natural history of liver glycogenosis due to phosphorylase
            kinase deficiency: a longitudinal study of 41 patients
  JOURNAL   Eur J Pediatr 149 (4), 268-271 (1990)
   PUBMED   2303074
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL732509.4 and AL096700.14.
            
            On or before May 30, 2025 this sequence version replaced
            XP_005274605.1, XP_054183176.1.
            
            Summary: Phosphorylase kinase is a polymer of 16 subunits, four
            each of alpha, beta, gamma and delta. The alpha subunit includes
            the skeletal muscle and hepatic isoforms, and the hepatic isoform
            is encoded by this gene. The beta subunit is the same in both the
            muscle and hepatic isoforms, and encoded by one gene. The gamma
            subunit also includes the skeletal muscle and hepatic isoforms,
            which are encoded by two different genes. The delta subunit is a
            calmodulin and can be encoded by three different genes. The gamma
            subunits contain the active site of the enzyme, whereas the alpha
            and beta subunits have regulatory functions controlled by
            phosphorylation. The delta subunit mediates the dependence of the
            enzyme on calcium concentration. Mutations in this gene cause
            glycogen storage disease type 9A, also known as X-linked liver
            glycogenosis. Alternatively spliced transcript variants have been
            reported, but the full-length nature of these variants has not been
            determined.[provided by RefSeq, Feb 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2869230.1,
                                           SRR14038194.459099.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1217
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.13"
     Protein         1..1217
                     /product="phosphorylase b kinase regulatory subunit alpha,
                     liver isoform isoform 2"
                     /EC_number="2.7.11.19"
                     /note="phosphorylase kinase alpha L subunit; phosphorylase
                     kinase alpha-subunit"
                     /calculated_mol_wt=136540
     Region          8..>439
                     /region_name="Glyco_hydro_15"
                     /note="Glycosyl hydrolases family 15; pfam00723"
                     /db_xref="CDD:395586"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46019.1)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P46019.1)"
     Site            735
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46019.1)"
     Region          <802..919
                     /region_name="Bac_rhamnosid6H"
                     /note="Bacterial alpha-L-rhamnosidase 6 hairpin
                     glycosidase domain; cl46875"
                     /db_xref="CDD:481215"
     Region          807..837
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P46019.1)"
     Region          930..>1129
                     /region_name="KPBB_C"
                     /note="Phosphorylase b kinase C-terminal domain;
                     pfam19292"
                     /db_xref="CDD:437124"
     Region          972..998
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46019.1)"
     Site            983
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P46019.1)"
     Site            1015
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46019.1)"
     Site            1026
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P46019.1)"
     Region          1041..1081
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P46019.1)"
     CDS             1..1217
                     /gene="PHKA2"
                     /gene_synonym="GSD9A; PHK; PYK; PYKL; XLG; XLG2"
                     /coded_by="NM_001440800.1:183..3836"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:5256"
                     /db_xref="HGNC:HGNC:8926"
                     /db_xref="MIM:300798"
ORIGIN      
        1 mrsrsnsgvr ldgyarlvqq tilcyqnpvt gllsasheqk dawvrdniys ilavwglgma
       61 yrknadrded kakayeleqn vvklmrgllq cmmrqvakve kfkhtqstkd slhakyntat
      121 cgtvvgddqw ghlqvdatsl fllflaqmta sglriiftld evafiqnlvf yieaaykvad
      181 ygmwergdkt nqgipelnas svgmakaale aideldlfga hggrksvihv lpdevehcqs
      241 ilfsmlpras tskeidagll siisfpafav edvnlvnvtk neiisklqgr ygccrflrdg
      301 yktpredpnr lhydpaelkl feniecewpv fwtyfiidgv fsgdavqvqe yrealegili
      361 rgkngirlvp elyavppnkv deeyknphtv drvpmgkvph lwgqslyils sllaegflaa
      421 geidplnrrf stsvkpdvvv qvtvlaennh ikdllrkhgv nvqsiadihp iqvqpgrils
      481 hiyaklgrnk nmnlsgrpyr higvlgtskl yvirnqiftf tpqftdqhhf ylaldnemiv
      541 emlrielayl ctcwrmtgrp tltfpisrtm ltndgsdihs avlstirkle dgyfggarvk
      601 lgnlsefltt sfytyltfld pdcdeklfdn asegtfspds dsdlvgyled tcnqesqdel
      661 dhyinhllqs tslrsylppl ckntedrhvf saihstrdil svmakakgle vpfvpmtlpt
      721 kvlsahrksl nlvdspqpll ekvpesdfqw prddhgdvdc eklveqlkdc snlqdqadil
      781 yilyvikgps wdtnlsgqhg vtvqnllgel ygkaglnqew gliryisgll rkkvevlaea
      841 ctdllshqkq ltvglppepr ekiisaplpp eeltkliyea sgqdisiavl tqeivvylam
      901 yvraqpslfv emlrlrigli iqvmatelar slncsgeeas eslmnlspfd mknllhhils
      961 gkefgversv rpihsstssp tisihevght gvtktersgi nrlrsemkqm trrfsadeqr
     1021 sstpssptgt sssdsgghhi gwgerqgqwl rrrrldgain rvpvgfyqrv wkilqkchgl
     1081 sidgyvlpss ttremtphei kfavhvesvl nrvpqpeyrq llveaimvlt llsdtemtsi
     1141 ggiihvdqiv qmasqlflqd qvsigamdtl ekdqatgich ffydsapsga ygtmtyltra
     1201 vasylqellp nsgcqmq
//
LOCUS       NP_001397838             475 aa            linear   PRI 21-NOV-2025
DEFINITION  abl interactor 1 isoform s [Homo sapiens].
ACCESSION   NP_001397838 XP_005252390
VERSION     NP_001397838.1
DBSOURCE    REFSEQ: accession NM_001410909.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Petersen,M. and Dubielecka,P.
  TITLE     Adaptor protein Abelson interactor 1 in homeostasis and disease
  JOURNAL   Cell Commun Signal 22 (1), 468 (2024)
   PUBMED   39354505
  REMARK    GeneRIF: Adaptor protein Abelson interactor 1 in homeostasis and
            disease.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Jin,M., Xie,M., Liu,Y., Song,H., Zhang,M., Li,W., Li,X., Jia,N.,
            Dong,L., Lu,Q., Xue,F., Yan,L. and Yu,Q.
  TITLE     Circulating miR-30e-3p induces disruption of neurite development in
            SH-SY5Y cells by targeting ABI1, a novel biomarker for
            schizophrenia
  JOURNAL   J Psychiatr Res 174, 84-93 (2024)
   PUBMED   38626565
  REMARK    GeneRIF: Circulating miR-30e-3p induces disruption of neurite
            development in SH-SY5Y cells by targeting ABI1, a novel biomarker
            for schizophrenia.
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Lin,T., Guo,J., Peng,Y., Li,M., Liu,Y., Yu,X., Wu,N. and Yu,W.
  TITLE     Pan-cancer transcriptomic data of ABI1 transcript variants and
            molecular constitutive elements identifies novel cancer metastatic
            and prognostic biomarkers
  JOURNAL   Cancer Biomark 39 (1), 49-62 (2024)
   PUBMED   37545215
  REMARK    GeneRIF: Pan-cancer transcriptomic data of ABI1 transcript variants
            and molecular constitutive elements identifies novel cancer
            metastatic and prognostic biomarkers.
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Fan,P.D. and Goff,S.P.
  TITLE     Abl interactor 1 binds to sos and inhibits epidermal growth factor-
            and v-Abl-induced activation of extracellular signal-regulated
            kinases
  JOURNAL   Mol Cell Biol 20 (20), 7591-7601 (2000)
   PUBMED   11003655
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Courtney,K.D., Grove,M., Vandongen,H., Vandongen,A., LaMantia,A.S.
            and Pendergast,A.M.
  TITLE     Localization and phosphorylation of Abl-interactor proteins, Abi-1
            and Abi-2, in the developing nervous system
  JOURNAL   Mol Cell Neurosci 16 (3), 244-257 (2000)
   PUBMED   10995551
REFERENCE   7  (residues 1 to 475)
  AUTHORS   Scita,G., Nordstrom,J., Carbone,R., Tenca,P., Giardina,G.,
            Gutkind,S., Bjarnegard,M., Betsholtz,C. and Di Fiore,P.P.
  TITLE     EPS8 and E3B1 transduce signals from Ras to Rac
  JOURNAL   Nature 401 (6750), 290-293 (1999)
   PUBMED   10499589
REFERENCE   8  (residues 1 to 475)
  AUTHORS   Taki,T., Shibuya,N., Taniwaki,M., Hanada,R., Morishita,K.,
            Bessho,F., Yanagisawa,M. and Hayashi,Y.
  TITLE     ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL
            gene in acute myeloid leukemia with t(10;11)(p11.2;q23)
  JOURNAL   Blood 92 (4), 1125-1130 (1998)
   PUBMED   9694699
REFERENCE   9  (residues 1 to 475)
  AUTHORS   Ziemnicka-Kotula,D., Xu,J., Gu,H., Potempska,A., Kim,K.S.,
            Jenkins,E.C., Trenkner,E. and Kotula,L.
  TITLE     Identification of a candidate human spectrin Src homology 3
            domain-binding protein suggests a general mechanism of association
            of tyrosine kinases with the spectrin-based membrane skeleton
  JOURNAL   J Biol Chem 273 (22), 13681-13692 (1998)
   PUBMED   9593709
REFERENCE   10 (residues 1 to 475)
  AUTHORS   Biesova,Z., Piccoli,C. and Wong,W.T.
  TITLE     Isolation and characterization of e3B1, an eps8 binding protein
            that regulates cell growth
  JOURNAL   Oncogene 14 (2), 233-241 (1997)
   PUBMED   9010225
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139404.9 and AL390961.17.
            
            On Aug 17, 2022 this sequence version replaced XP_005252390.1.
            
            Summary: This gene encodes a member of the Abelson-interactor
            family of adaptor proteins. These proteins facilitate signal
            transduction as components of several multiprotein complexes, and
            regulate actin polymerization and cytoskeletal remodeling through
            interactions with Abelson tyrosine kinases. The encoded protein
            plays a role in macropinocytosis as a component of the WAVE2
            complex, and also forms a complex with EPS8 and SOS1 that mediates
            signal transduction from Ras to Rac. This gene may play a role in
            the progression of several malignancies including melanoma, colon
            cancer and breast cancer, and a t(10;11) chromosomal translocation
            involving this gene and the MLL gene has been associated with acute
            myeloid leukemia. Alternatively spliced transcript variants
            encoding multiple isoforms have been observed for this gene, and a
            pseudogene of this gene is located on the long arm of chromosome
            14. [provided by RefSeq, Sep 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3418724.1,
                                           SRR14038191.1586042.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.1"
     Protein         1..475
                     /product="abl interactor 1 isoform s"
                     /note="nap1 binding protein; interactor protein AblBP4;
                     Abl-interactor protein 1 long; Abelson interactor 1;
                     abl-binding protein 4; eps8 SH3 domain-binding protein;
                     spectrin SH3 domain-binding protein 1"
                     /calculated_mol_wt=51639
     Region          93..154
                     /region_name="Abi_HHR"
                     /note="Abl-interactor HHR; pfam07815"
                     /db_xref="CDD:462279"
     Region          417..475
                     /region_name="SH3_Abi1"
                     /note="Src homology 3 domain of Abl Interactor 1; cd11971"
                     /db_xref="CDD:212904"
     Site            order(422,424,427,431,449..450,463,465..466)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212904"
     CDS             1..475
                     /gene="ABI1"
                     /gene_synonym="ABI-1; ABLBP4; E3B1; NAP1BP; SSH3BP;
                     SSH3BP1"
                     /coded_by="NM_001410909.1:96..1523"
                     /note="isoform s is encoded by transcript variant 20"
                     /db_xref="CCDS:CCDS91224.1"
                     /db_xref="GeneID:10006"
                     /db_xref="HGNC:HGNC:11320"
                     /db_xref="MIM:603050"
ORIGIN      
        1 maelqmllee eipsgkrali esyqnltrva dycennyiqa tdkrkaleet kayttqslas
       61 vayqinalan nvlqlldiqa sqlrrmessi nhisqtvdih kekvarreig ilttnkntsr
      121 thkiiapanm erpvryirkp idytvlddvg hgvkhgnnqp artgtlsrtn pptqkppspp
      181 msgrgtlgrn tpyktlepvk pptvpndymt sparlgsqhs pgrtaslnqr prthsgssgg
      241 sgsrensgss sigipiavpt pspptigpap gsapgsqygt mtrqisrhns ttsstssggy
      301 rrtpsvtaqf saqphvnggp lysqnsisia pppppmpqlt pqipltgfva rvqeniadsp
      361 tpppppppdd ipmfddsppp pppppvdyed eeaavvqynd pyadgdpawa pknyiekvva
      421 iydytkdkdd elsfmegaii yvikknddgw yegvcnrvtg lfpgnyvesi mhytd
//
LOCUS       NP_001397652             591 aa            linear   PRI 21-NOV-2025
DEFINITION  pre-mRNA 3'-end-processing factor FIP1 isoform 46 [Homo sapiens].
ACCESSION   NP_001397652 XP_047272165
VERSION     NP_001397652.1
DBSOURCE    REFSEQ: accession NM_001410723.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Muckenfuss,L.M., Migenda Herranz,A.C., Boneberg,F.M., Clerici,M.
            and Jinek,M.
  TITLE     Fip1 is a multivalent interaction scaffold for processing factors
            in human mRNA 3' end biogenesis
  JOURNAL   Elife 11, e80332 (2022)
   PUBMED   36073787
  REMARK    GeneRIF: Fip1 is a multivalent interaction scaffold for processing
            factors in human mRNA 3' end biogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Tennenbaum,J., Groh,M., Venditti,L., Campos-Gazeau,F., Chalayer,E.,
            De Broucker,T., Hamidou,M., Hunault,M., Lyoubi,A., Meunier,R.,
            Muron,T., Sene,D., Slama,B., Guidoux,C., Lefevre,G., Kahn,J.E.,
            Denier,C. and Rohmer,J.
  TITLE     FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a Treatable
            Cause of Watershed Infarction
  JOURNAL   Stroke 52 (10), e605-e609 (2021)
   PUBMED   34304603
  REMARK    GeneRIF: FIP1L1-PDGFRA-Associated Hypereosinophilic Syndrome as a
            Treatable Cause of Watershed Infarction.
REFERENCE   4  (residues 1 to 591)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 591)
  AUTHORS   Helbig,G., Lewandowski,K., Swiderska,A., Rodzaj,M., Seferynska,I.
            and Gajkowska-Kulik,J.
  TITLE     Exquisite response to imatinib mesylate in FIP1L1-PDGFRA-mutated
            hypereosinophilic syndrome: a 12-year experience of the Polish
            Hypereosinophilic Syndrome Study Group
  JOURNAL   Pol Arch Intern Med 130 (3), 255-257 (2020)
   PUBMED   32125294
  REMARK    GeneRIF: Exquisite response to imatinib mesylate in
            FIP1L1-PDGFRA-mutated hypereosinophilic syndrome: a 12-year
            experience of the Polish Hypereosinophilic Syndrome Study Group.
REFERENCE   6  (residues 1 to 591)
  AUTHORS   Cools,J., Quentmeier,H., Huntly,B.J., Marynen,P., Griffin,J.D.,
            Drexler,H.G. and Gilliland,D.G.
  TITLE     The EOL-1 cell line as an in vitro model for the study of
            FIP1L1-PDGFRA-positive chronic eosinophilic leukemia
  JOURNAL   Blood 103 (7), 2802-2805 (2004)
   PUBMED   14630792
  REMARK    GeneRIF: results indicate that the fusion of FIP1L1 to PDGFRA
            occurs rarely in leukemia cell lines
REFERENCE   7  (residues 1 to 591)
  AUTHORS   Kaufmann,I., Martin,G., Friedlein,A., Langen,H. and Keller,W.
  TITLE     Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements
            and stimulates poly(A) polymerase
  JOURNAL   EMBO J 23 (3), 616-626 (2004)
   PUBMED   14749727
REFERENCE   8  (residues 1 to 591)
  AUTHORS   Pardanani,A., Ketterling,R.P., Brockman,S.R., Flynn,H.C.,
            Paternoster,S.F., Shearer,B.M., Reeder,T.L., Li,C.Y., Cross,N.C.,
            Cools,J., Gilliland,D.G., Dewald,G.W. and Tefferi,A.
  TITLE     CHIC2 deletion, a surrogate for FIP1L1-PDGFRA fusion, occurs in
            systemic mastocytosis associated with eosinophilia and predicts
            response to imatinib mesylate therapy
  JOURNAL   Blood 102 (9), 3093-3096 (2003)
   PUBMED   12842979
  REMARK    GeneRIF: observations suggest that the FIP1L1-PDGFRA rearrangement
            occurs in an early hematopoietic progenitor and suggests that the
            molecular pathogenesis for a subset of SMCD patients is similar to
            that of HES
REFERENCE   9  (residues 1 to 591)
  AUTHORS   Griffin,J.H., Leung,J., Bruner,R.J., Caligiuri,M.A. and
            Briesewitz,R.
  TITLE     Discovery of a fusion kinase in EOL-1 cells and idiopathic
            hypereosinophilic syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (13), 7830-7835 (2003)
   PUBMED   12808148
REFERENCE   10 (residues 1 to 591)
  AUTHORS   Cools,J., DeAngelo,D.J., Gotlib,J., Stover,E.H., Legare,R.D.,
            Cortes,J., Kutok,J., Clark,J., Galinsky,I., Griffin,J.D.,
            Cross,N.C., Tefferi,A., Malone,J., Alam,R., Schrier,S.L.,
            Schmid,J., Rose,M., Vandenberghe,P., Verhoef,G., Boogaerts,M.,
            Wlodarska,I., Kantarjian,H., Marynen,P., Coutre,S.E., Stone,R. and
            Gilliland,D.G.
  TITLE     A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes
            as a therapeutic target of imatinib in idiopathic hypereosinophilic
            syndrome
  JOURNAL   N Engl J Med 348 (13), 1201-1214 (2003)
   PUBMED   12660384
  REMARK    GeneRIF: The hypereosinophilic syndrome may result from a novel
            fusion tyrosine kinase - FIP1L1-PDGFRalpha - that is a consequence
            of an interstitial chromosomal deletion.
            GeneRIF: Describes the fusion gene Fip1-like-1-PDGFRalpha in
            patients with idiopathic hypereosinophilic syndrome, mostly
            responsive to imatinib therapy.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098821.3 and AC058822.6.
            
            On Aug 15, 2022 this sequence version replaced XP_047272165.1.
            
            Summary: This gene encodes a subunit of the CPSF (cleavage and
            polyadenylation specificity factor) complex that polyadenylates the
            3' end of mRNA precursors. This gene, the homolog of yeast Fip1
            (factor interacting with PAP), binds to U-rich sequences of
            pre-mRNA and stimulates poly(A) polymerase activity. Its N-terminus
            contains a PAP-binding site and its C-terminus an RNA-binding
            domain. An interstitial chromosomal deletion on 4q12 creates an
            in-frame fusion of human genes FIP1L1 and PDGFRA (platelet-derived
            growth factor receptor, alpha). The FIP1L1-PDGFRA fusion gene
            encodes a constitutively activated tyrosine kinase that joins the
            first 233 amino acids of FIP1L1 to the last 523 amino acids of
            PDGFRA. This gene fusion and chromosomal deletion is the cause of
            some forms of idiopathic hypereosinophilic syndrome (HES). This
            syndrome, recently reclassified as chronic eosinophilic leukemia
            (CEL), is responsive to treatment with tyrosine kinase inhibitors.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.772261.1,
                                           SRR14038196.1081292.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..591
                     /product="pre-mRNA 3'-end-processing factor FIP1 isoform
                     46"
                     /note="rearranged in hypereosinophilia; pre-mRNA
                     3'-end-processing factor FIP1; FIP1-like 1 protein; factor
                     interacting with PAP; FIP1 like 1; FIP1L1 cleavage and
                     polyadenylation specific factor subunit"
                     /calculated_mol_wt=65969
     Region          139..181
                     /region_name="Fip1"
                     /note="Fip1 motif; pfam05182"
                     /db_xref="CDD:461573"
     CDS             1..591
                     /gene="FIP1L1"
                     /gene_synonym="FIP1; hFip1; Rhe"
                     /coded_by="NM_001410723.1:199..1974"
                     /note="isoform 46 is encoded by transcript variant 49"
                     /db_xref="CCDS:CCDS93513.1"
                     /db_xref="GeneID:81608"
                     /db_xref="HGNC:HGNC:19124"
                     /db_xref="MIM:607686"
ORIGIN      
        1 msageverlv selsggtggd eeeewlygde neverpeeen asanppsgie detaengvpk
       61 pkvtetedds dsdsdddedd vhvtigdikt gapqygsygt apvnlniktg grvygttgtk
      121 vkgvdldapg singvpllev dldsfedkpw rkpgadlsdy fnygfnedtw kaycekqkri
      181 rmglevipvt sttnkitaed ctmevtpgae iqdgrfnlfk vqqgrtgnse ketalpstka
      241 eftsppslfk tglppsrnst ssqsqtstas rkanssvgkw qdrygraesp dlrrlpgaid
      301 vigqtitisr vegrrranen sniqvlsers atevdnnfsk pppffppgap pthlppppfl
      361 pppptvstap plipppgipi tvpppgfppp pgapppslip tiesghssgy dsrsarafpy
      421 gnvafphlpg sapswpslvd tskqwdyyar rekdrdrerd rdrerdrdrd rerertrere
      481 rerdhsptps vfnrfvgdee ryryreyaer gyerhrasre keerhrerrh rekeetrhks
      541 srsnsrrrhe seegdshrrh khkkskrske gkeagsepap eqesteatpa e
//
LOCUS       NP_001425163            2051 aa            linear   PRI 21-NOV-2025
DEFINITION  nuclear receptor coactivator 6 isoform 4 [Homo sapiens].
ACCESSION   NP_001425163 XP_016883233 XP_054179233
VERSION     NP_001425163.1
DBSOURCE    REFSEQ: accession NM_001438234.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2051)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2051)
  AUTHORS   Lee,K.G., Hong,B.K., Lee,S., Lee,N., Kim,S.W., Kim,D. and Kim,W.U.
  TITLE     Nuclear receptor coactivator 6 is a critical regulator of NLRP3
            inflammasome activation and gouty arthritis
  JOURNAL   Cell Mol Immunol 21 (3), 227-244 (2024)
   PUBMED   38195836
  REMARK    GeneRIF: Nuclear receptor coactivator 6 is a critical regulator of
            NLRP3 inflammasome activation and gouty arthritis.
REFERENCE   3  (residues 1 to 2051)
  AUTHORS   Fang,Y., Xu,Y., Liao,W., Ji,T., Yu,L., Li,L., Pan,M. and Yang,D.
  TITLE     Multiomics analyses and machine learning of nuclear receptor
            coactivator 6 reveal its essential role in hepatocellular carcinoma
  JOURNAL   Cancer Sci 114 (1), 75-90 (2023)
   PUBMED   36086920
  REMARK    GeneRIF: Multiomics analyses and machine learning of nuclear
            receptor coactivator 6 reveal its essential role in hepatocellular
            carcinoma.
REFERENCE   4  (residues 1 to 2051)
  AUTHORS   Watanabe,N., Kawagoe,J., Sugiyama,A., Takehara,I., Ohta,T. and
            Nagase,S.
  TITLE     Nuclear receptor coactivator-6 is essential for the morphological
            change of human uterine stromal cell decidualization via regulating
            actin fiber reorganization
  JOURNAL   Mol Reprod Dev 89 (4), 165-174 (2022)
   PUBMED   35384116
  REMARK    GeneRIF: Nuclear receptor coactivator-6 is essential for the
            morphological change of human uterine stromal cell decidualization
            via regulating actin fiber reorganization.
REFERENCE   5  (residues 1 to 2051)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 2051)
  AUTHORS   Caira,F., Antonson,P., Pelto-Huikko,M., Treuter,E. and
            Gustafsson,J.A.
  TITLE     Cloning and characterization of RAP250, a novel nuclear receptor
            coactivator
  JOURNAL   J Biol Chem 275 (8), 5308-5317 (2000)
   PUBMED   10681503
REFERENCE   7  (residues 1 to 2051)
  AUTHORS   Lee,S.K., Anzick,S.L., Choi,J.E., Bubendorf,L., Guan,X.Y.,
            Jung,Y.K., Kallioniemi,O.P., Kononen,J., Trent,J.M., Azorsa,D.,
            Jhun,B.H., Cheong,J.H., Lee,Y.C., Meltzer,P.S. and Lee,J.W.
  TITLE     A nuclear factor, ASC-2, as a cancer-amplified transcriptional
            coactivator essential for ligand-dependent transactivation by
            nuclear receptors in vivo
  JOURNAL   J Biol Chem 274 (48), 34283-34293 (1999)
   PUBMED   10567404
REFERENCE   8  (residues 1 to 2051)
  AUTHORS   Guan,X.Y., Xu,J., Anzick,S.L., Zhang,H., Trent,J.M. and
            Meltzer,P.S.
  TITLE     Hybrid selection of transcribed sequences from microdissected DNA:
            isolation of genes within amplified region at 20q11-q13.2 in breast
            cancer
  JOURNAL   Cancer Res 56 (15), 3446-3450 (1996)
   PUBMED   8758910
REFERENCE   9  (residues 1 to 2051)
  AUTHORS   Carney,J.P., McKnight,C., VanEpps,S. and Kelley,M.R.
  TITLE     Random rapid amplification of cDNA ends (RRACE) allows for cloning
            of multiple novel human cDNA fragments containing (CAG)n repeats
  JOURNAL   Gene 155 (2), 289-292 (1995)
   PUBMED   7536696
REFERENCE   10 (residues 1 to 2051)
  AUTHORS   Estey,A., Kemp,M., Allison,S. and Lamb,C.
  TITLE     Evaluation of a patient information booklet
  JOURNAL   J Nurs Staff Dev 9 (6), 278-282 (1993)
   PUBMED   8263591
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049709.18 and AL109824.24.
            
            On or before Apr 16, 2025 this sequence version replaced
            XP_016883233.1, XP_054179233.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            coactivator that can interact with nuclear hormone receptors to
            enhance their transcriptional activator functions. This protein has
            been shown to be involved in the hormone-dependent coactivation of
            several receptors, including prostanoid, retinoid, vitamin D3,
            thyroid hormone, and steroid receptors. Alternatively spliced
            transcript variants encoding different isoforms have been described
            for this gene. [provided by RefSeq, Jun 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1711919.1,
                                           SRR14038196.2930318.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2051
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..2051
                     /product="nuclear receptor coactivator 6 isoform 4"
                     /note="amplified in breast cancer-3 protein; activating
                     signal cointegrator-2; nuclear receptor coactivator
                     RAP250; peroxisome proliferator-activated receptor
                     interacting protein; thyroid hormone receptor binding
                     protein; NRC RAP250; PPAR-interacting protein; amplified
                     in breast cancer protein 3; nuclear receptor-activating
                     protein, 250 kDa; cancer-amplified transcriptional
                     coactivator ASC-2"
                     /calculated_mol_wt=217776
     Region          48..190
                     /region_name="Nucleic_acid_bd"
                     /note="Putative nucleic acid-binding region; pfam13820"
                     /db_xref="CDD:463988"
     Site            95
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          184..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          <185..514
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          512..>826
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          761..915
                     /region_name="NCOA6IP-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          777..799
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            872
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK, in vitro.
                     /evidence=ECO:0000269|PubMed:11773444; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          875..879
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          887..1266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1035
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          <1044..1290
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1046
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1084
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1298..1341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1436..1462
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1479..1483
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1629..2051
                     /region_name="EP300/CRSP3-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1726..1808
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1807
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1810
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1825..1896
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1983..2051
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            2006
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     CDS             1..2051
                     /gene="NCOA6"
                     /gene_synonym="AIB3; ASC2; NRC; PRIP; RAP250; TRBP"
                     /coded_by="NM_001438234.1:344..6499"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:23054"
                     /db_xref="HGNC:HGNC:15936"
                     /db_xref="MIM:605299"
ORIGIN      
        1 mvlddlpnle diytslcsst medsemdfds gledddtksd siledstifv afkgniddkd
       61 fkwkldailk nvpnllhmes sklkvqkvep wnsvrvtfni preaaerlri laqsnnqqlr
      121 dlgilsvqie gegainlala qnrsqdvrmn gpmgagnsvr meagfpmasg pgiirmnnpa
      181 tvmippggnv sssmmapgpn pelqprtprp asqsdamdpl lsglhiqqqs hpsgslapph
      241 hpmqpvsvnr qmnpanfpql qqqqqqqqqq qqqqqqqqqq qqqqqlqarp pqqhqqqqpq
      301 girpqftapt qvpvppgwnq lpsgalqppp aqgslgtmta nqgwkkaplp gpmqqqlqar
      361 pslatvqtps hppppypfgs qqasqahtnf pqmsnpgqft apqmkslqgg psrvptplqq
      421 phltnkspas spssfqqgsp assptvnqtq qqmgprppqn nplpqgfqqp vsspgrnpmv
      481 qqgnvppnfm vmqqqppnqg pqslhpglgg qanpnfmqgq vpsttattpg nsgapqlqan
      541 qnvqhaggqg agppqnqmqv shgppnmmqp slmgihgnmn nqqagtsgvp qvnlsnmqgq
      601 pqqgppsqlm gmhqqivpsq gqmvqqqgtl npqnpmilsr aqlmpqgqmm vnppsqnlgp
      661 spqrmtppkq mlsqqgpqmm aphnqmmgpq gqvllqqnpm ieqimtnqmq gnkqqfntqn
      721 qsnvmpgpaq imrgptpnmq gnmvqftgqm sgqmlpqqgp vnnspsqvmg iqgqvlrppg
      781 psphmaqqhg dpattanndv slsqmmpdvs iqqtnmvpph vqamqgnsas gnhfsghgms
      841 fnapfsgapn gnqmscgqnp gfpvnkdvtl tspllvnllq sdisaghfgv nnkqnntnan
      901 kpkkkkpprk kknsqqdlnt pdtrpaglee adqpplpgeq ginldnsgpk lpefsnrppg
      961 ypsqpveqrp lqqmppqlmq hvapppqppq qqpqpqlpqq qqppppsqpq sqqqqqqqqq
     1021 mmmmlmmqqd pksvrlpvsq nvhpprgpln pdsqrmpmqq sgsvpvmvsl qgpasvppsp
     1081 dkqrmpmpvn tplgsnsrkm vyqespqnps ssplaemasl peasgseaps vpggpnnmps
     1141 hvvlpqnqlm mtgpkpgpsp lsatqgatpq qppvnslpss hghhfpnvaa ptqtsrpktp
     1201 nrasprpyyp qtpnnrppst epseislspe rlnasiaglf ppqiniplpp rpnlnrgfdq
     1261 qglnpttlka igqapsnltm npsnfatpqt hkldsvvvns gkqsnsgatk raspsnsrrs
     1321 spgssrkttp spgrqnskap kltlasqtna allqnvelpr nvlvsptpla nppvpgsfpn
     1381 nsglnpqnst vsvaavggvv ednkeslnvp qdsdcqnsqs rkeqvnielk avpaqevkmv
     1441 vpedqskkdg qpsdpnklps veenknlvsp amreaptsls qlldnsgapn vtikppgltd
     1501 levtppvvsg edlkkasvip tlqdlssske psnslnlphs nelcsslvhp elsevssnva
     1561 psippvmsrp vssssistpl ppnqitvfvt snpittsant saalpthlqs almstvvtmp
     1621 nagskvmvse gqsaaqsnar pqfitpvfin sssiiqvmkg sqpstipaap lttnsglmpp
     1681 svavvgplhi pqnikfssap vppnalsssp apniqtgrpl vlssratpvq lpsppctssp
     1741 vvpshppvqq vkelnpdeas pqvntsadqn tlpssqsttm vsplltnspg ssgnrrspvs
     1801 sskgkgkvdk igqilltkac kkvtgslekg eeqygadget egqgldttap glmgteqlst
     1861 eldsktptpp aptllkmtss pvgpgtasag pslpggalpt svrsivttlv pselisavpt
     1921 tksnhggias eslagglvee kvgshpellp siapsqnlvs ketsttalqa svarpelevn
     1981 aaivsgqsse pkeivekski pgrrnsrtee ptvasesven ghrkrssrpa sassstkdit
     2041 savqskrrks k
//
LOCUS       NP_001427684             447 aa            linear   PRI 21-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform c [Homo sapiens].
ACCESSION   NP_001427684 XP_024305445 XP_054232490
VERSION     NP_001427684.1
DBSOURCE    REFSEQ: accession NM_001440755.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 447)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 447)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 447)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 447)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            On or before May 28, 2025 this sequence version replaced
            XP_024305445.1, XP_054232490.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2478909.1,
                                           SRR14038192.633903.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..447
                     /product="lysosomal cobalamin transporter ABCD4 isoform c"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=50111
     Region          <32..444
                     /region_name="YddA"
                     /note="ABC-type uncharacterized transport system, permease
                     and ATPase components [General function prediction only];
                     COG4178"
                     /db_xref="CDD:443337"
     CDS             1..447
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_001440755.1:232..1575"
                     /note="isoform c is encoded by transcript variant 13"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 maskliispf tlvyytyqcf qstgwlgpvs ifgyfilgtv vnktlmgpiv mklvhqekle
       61 gdfrfkhmqi rvnaepaafy raghvehmrt drrlqrllqt qrelmskelw lyigintfdy
      121 lgsilsyvvi aipifsgvyg dlspaelstl vsknafvciy liscftqlid lsttlsdvag
      181 ythrigqlre tlldmslksq dceilgesew gldtppgwpa aepadtafll ervsisapss
      241 dkplikdlsl kisegqslli tgntgtgkts llrvlgglwt strgsvqmlt dfgphgvlfl
      301 pqkpfftdgt lreqviyplk evypdsgsad derilrflel aglsnlvart egldqqvdwn
      361 wydvlspgem qrlsfarlfy lqpkyavlde atsalteeve selyrigqql gmtfisvghr
      421 qslekfhslv lklcgggrwe lmrikve
//
LOCUS       NP_001400300             391 aa            linear   PRI 21-NOV-2025
DEFINITION  telomeric repeat-binding factor 1 isoform 11 [Homo sapiens].
ACCESSION   NP_001400300
VERSION     NP_001400300.1
DBSOURCE    REFSEQ: accession NM_001413371.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Hu,H., van Roon,A.M., Ghanim,G.E., Ahsan,B., Oluwole,A.O.,
            Peak-Chew,S.Y., Robinson,C.V. and Nguyen,T.H.D.
  TITLE     Structural basis of telomeric nucleosome recognition by shelterin
            factor TRF1
  JOURNAL   Sci Adv 9 (34), eadi4148 (2023)
   PUBMED   37624885
  REMARK    GeneRIF: Structural basis of telomeric nucleosome recognition by
            shelterin factor TRF1.
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Harmak,H., Redouane,S., Charoute,H., Aniq Filali,O., Barakat,A. and
            Rouba,H.
  TITLE     In silico exploration and molecular dynamics of deleterious SNPs on
            the human TERF1 protein triggering male infertility
  JOURNAL   J Biomol Struct Dyn 41 (24), 14665-14688 (2023)
   PUBMED   36995171
  REMARK    GeneRIF: In silico exploration and molecular dynamics of
            deleterious SNPs on the human TERF1 protein triggering male
            infertility.
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Abreu,P.L., Lee,Y.W. and Azzalin,C.M.
  TITLE     In Vitro Characterization of the Physical Interactions between the
            Long Noncoding RNA TERRA and the Telomeric Proteins TRF1 and TRF2
  JOURNAL   Int J Mol Sci 23 (18), 10463 (2022)
   PUBMED   36142374
  REMARK    GeneRIF: In Vitro Characterization of the Physical Interactions
            between the Long Noncoding RNA TERRA and the Telomeric Proteins
            TRF1 and TRF2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Jack,A., Kim,Y., Strom,A.R., Lee,D.S.W., Williams,B., Schaub,J.M.,
            Kellogg,E.H., Finkelstein,I.J., Ferro,L.S., Yildiz,A. and
            Brangwynne,C.P.
  TITLE     Compartmentalization of telomeres through DNA-scaffolded phase
            separation
  JOURNAL   Dev Cell 57 (2), 277-290 (2022)
   PUBMED   35077681
  REMARK    GeneRIF: Compartmentalization of telomeres through DNA-scaffolded
            phase separation.
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Broccoli,D., Chong,L., Oelmann,S., Fernald,A.A., Marziliano,N., van
            Steensel,B., Kipling,D., Le Beau,M.M. and de Lange,T.
  TITLE     Comparison of the human and mouse genes encoding the telomeric
            protein, TRF1: chromosomal localization, expression and conserved
            protein domains
  JOURNAL   Hum Mol Genet 6 (1), 69-76 (1997)
   PUBMED   9002672
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Lu,K.P., Hanes,S.D. and Hunter,T.
  TITLE     A human peptidyl-prolyl isomerase essential for regulation of
            mitosis
  JOURNAL   Nature 380 (6574), 544-547 (1996)
   PUBMED   8606777
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Bilaud,T., Koering,C.E., Binet-Brasselet,E., Ancelin,K.,
            Pollice,A., Gasser,S.M. and Gilson,E.
  TITLE     The telobox, a Myb-related telomeric DNA binding motif found in
            proteins from yeast, plants and human
  JOURNAL   Nucleic Acids Res 24 (7), 1294-1303 (1996)
   PUBMED   8614633
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Chong,L., van Steensel,B., Broccoli,D., Erdjument-Bromage,H.,
            Hanish,J., Tempst,P. and de Lange,T.
  TITLE     A human telomeric protein
  JOURNAL   Science 270 (5242), 1663-1667 (1995)
   PUBMED   7502076
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Zhong,Z., Shiue,L., Kaplan,S. and de Lange,T.
  TITLE     A mammalian factor that binds telomeric TTAGGG repeats in vitro
  JOURNAL   Mol Cell Biol 12 (11), 4834-4843 (1992)
   PUBMED   1406665
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022893.6.
            
            Summary: This gene encodes a telomere specific protein which is a
            component of the telomere nucleoprotein complex. This protein is
            present at telomeres throughout the cell cycle and functions as an
            inhibitor of telomerase, acting in cis to limit the elongation of
            individual chromosome ends. The protein structure contains a
            C-terminal Myb motif, a dimerization domain near its N-terminus and
            an acidic N-terminus. Multiple transcripts of this gene are
            alternatively spliced products. [provided by RefSeq, Aug 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1268060.1,
                                           SRR1660807.89198.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.11"
     Protein         1..391
                     /product="telomeric repeat-binding factor 1 isoform 11"
                     /note="NIMA-interacting protein 2; telomeric protein
                     Pin2/TRF1; TTAGGG repeat-binding factor 1; telomeric
                     repeat binding factor (NIMA-interacting) 1"
                     /calculated_mol_wt=44183
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54274.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P54274.3)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P54274.3)"
     Region          58..268
                     /region_name="TRFH mediates dimerization.
                     /evidence=ECO:0000269|PubMed:18202258"
                     /note="propagated from UniProtKB/Swiss-Prot (P54274.3)"
     Region          76..264
                     /region_name="TRFH"
                     /note="Telomeric Repeat binding Factor or TTAGGG Repeat
                     binding Factor, central (dimerization) domain Homology;
                     TRFH. Telomeres are protein/DNA complexes that make up the
                     physical ends of eukaryotic linear chromosomes and are
                     essential for chromosome stability; cd00280"
                     /db_xref="CDD:238174"
     Site            order(106,109,123,127,131,141..145,153,156..157,160)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238174"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000269|PubMed:11375976; propagated from
                     UniProtKB/Swiss-Prot (P54274.3)"
     Region          265..378
                     /region_name="Interaction with RLIM.
                     /evidence=ECO:0000269|PubMed:19164295"
                     /note="propagated from UniProtKB/Swiss-Prot (P54274.3)"
     Region          266..311
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54274.3)"
     Region          326..375
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54274.3)"
     Region          337..356
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P54274.3)"
     CDS             1..391
                     /gene="TERF1"
                     /gene_synonym="hTRF1-AS; PIN2; t-TRF1; TRBF1; TRF; TRF1"
                     /coded_by="NM_001413371.1:24..1199"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:7013"
                     /db_xref="HGNC:HGNC:11728"
                     /db_xref="MIM:600951"
ORIGIN      
        1 maedvssaap sprgcadgrd adpteeqmae terndeeqfe cqellecqvq vgapeeeeee
       61 eedaglvaea eavaagwmld flclslcraf rdgrsedfrr trnsaeaiih glssltacql
      121 rtiyicqflt riaagktlda qfenderitp lesalmiwgs iekehdklhe eiqnlikiqa
      181 iavcmengnf keaeevferi fgdpnshmpf kskllmiisq kdtfhsffqh fsynhmmeki
      241 ksyvnyvlse ksstflmkaa akvveskrtr titsqdkpsg ndvemetean ldtrksvsdk
      301 qsavtesseg tvsllrshkn lflsklqhgt qqqdlnkker rvgtpqstkk kkesrrates
      361 ripvsksqpv tpekhrarkr qgssvkrvff t
//
LOCUS       NP_001412006             456 aa            linear   PRI 21-NOV-2025
DEFINITION  coatomer subunit delta isoform 7 [Homo sapiens].
ACCESSION   NP_001412006
VERSION     NP_001412006.1
DBSOURCE    REFSEQ: accession NM_001425077.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   O'Donoghue,L., Comer,S.P., Hiebner,D.W., Schoen,I., von
            Kriegsheim,A. and Smolenski,A.
  TITLE     RhoGAP6 interacts with COPI to regulate protein transport
  JOURNAL   Biochem J 480 (14), 1109-1127 (2023)
   PUBMED   37409526
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Li,W., Liang,J., Outeda,P., Turner,S., Wakimoto,B.T. and Watnick,T.
  TITLE     A genetic screen in Drosophila reveals an unexpected role for the
            KIP1 ubiquitination-promoting complex in male fertility
  JOURNAL   PLoS Genet 16 (12), e1009217 (2020)
   PUBMED   33378371
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Tidwell,T., Deshotel,M., Palumbos,J., Miller,C., Bayrak-Toydemir,P.
            and Carey,J.C.
  TITLE     Novel de novo ARCN1 intronic variant causes rhizomelic short
            stature with microretrognathia and developmental delay
  JOURNAL   Cold Spring Harb Mol Case Stud 6 (6), a005728 (2020)
   PUBMED   33154040
  REMARK    GeneRIF: Novel de novo ARCN1 intronic variant causes rhizomelic
            short stature with microretrognathia and developmental delay.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Schekman,R. and Orci,L.
  TITLE     Coat proteins and vesicle budding
  JOURNAL   Science 271 (5255), 1526-1533 (1996)
   PUBMED   8599108
  REMARK    Review article
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Cukierman,E., Huber,I., Rotman,M. and Cassel,D.
  TITLE     The ARF1 GTPase-activating protein: zinc finger motif and Golgi
            complex localization
  JOURNAL   Science 270 (5244), 1999-2002 (1995)
   PUBMED   8533093
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Radice,P., Pensotti,V., Jones,C., Perry,H., Pierotti,M.A. and
            Tunnacliffe,A.
  TITLE     The human archain gene, ARCN1, has highly conserved homologs in
            rice and Drosophila
  JOURNAL   Genomics 26 (1), 101-106 (1995)
   PUBMED   7782067
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Orcl,L., Palmer,D.J., Amherdt,M. and Rothman,J.E.
  TITLE     Coated vesicle assembly in the Golgi requires only coatomer and ARF
            proteins from the cytosol
  JOURNAL   Nature 364 (6439), 732-734 (1993)
   PUBMED   8355790
REFERENCE   10 (residues 1 to 456)
  AUTHORS   Waters,M.G., Serafini,T. and Rothman,J.E.
  TITLE     'Coatomer': a cytosolic protein complex containing subunits of
            non-clathrin-coated Golgi transport vesicles
  JOURNAL   Nature 349 (6306), 248-251 (1991)
   PUBMED   1898986
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000941.6.
            
            Summary: This gene maps in a region, which include the mixed
            lineage leukemia and Friend leukemia virus integration 1 genes,
            where multiple disease-associated chromosome translocations occur.
            It is an intracellular protein. Archain sequences are well
            conserved among eukaryotes and this protein may play a fundamental
            role in eukaryotic cell biology. It has similarities to heat shock
            proteins and clathrin-associated proteins, and may be involved in
            vesicle structure or trafficking. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4080719.1,
                                           SRR14038191.2983479.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2154529
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..456
                     /product="coatomer subunit delta isoform 7"
                     /note="coatomer protein delta-COP; coatomer protein
                     complex, subunit delta; archain vesicle transport protein
                     1; coatomer delta subunit; delta-coat protein; COPI coat
                     complex subunit delta"
                     /calculated_mol_wt=51194
     Region          4..133
                     /region_name="Delta_COP_N"
                     /note="delta subunit of the F-COPI complex, N-terminal
                     domain; cd14830"
                     /db_xref="CDD:341434"
     Region          217..453
                     /region_name="AP_delta-COPI_MHD"
                     /note="Mu homology domain (MHD) of adaptor protein (AP)
                     coat protein I (COPI) delta subunit; cd09254"
                     /db_xref="CDD:271162"
     CDS             1..456
                     /gene="ARCN1"
                     /gene_synonym="COPD; SRMMD; SSMG"
                     /coded_by="NM_001425077.1:140..1510"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:372"
                     /db_xref="HGNC:HGNC:649"
                     /db_xref="MIM:600820"
ORIGIN      
        1 mvllaaavct kagkaivsrq fvemtrtrie gllaafpklm ntgkqhtfve tesvryvyqp
       61 meklymvlit tknsniledl etlrlfsrvi peycraleen eisehcfdli fafdeivalg
      121 yrenvnlaqi rtftemdshe ekvfravret qereakaemr rkakelqqar rdaerqgkka
      181 pgfggfgssa vsggstaami tetiietdkp kvapapasvh mkieekitlt cgrdgglqnm
      241 elhgmimlri sddkygrirl hvenedkkgv qlqthpnvdk klftaeslig lknpeksfpv
      301 nsdvgvlkwr lqtteesfip ltincwpses gngcdvniey elqednleln dvvitiplps
      361 gvgapvigei dgeyrhdsrr ntlewclpvi daknksgsle fsiagqpndf fpvqvsfvsk
      421 knycniqvtk vtqvdgnspv rfstettflv dkyeil
//
LOCUS       NP_001400003             328 aa            linear   PRI 21-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001400003
VERSION     NP_001400003.1
DBSOURCE    REFSEQ: accession NM_001413074.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.836452.1,
                                           SRR14372080.4219903.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..328
                     /product="mitochondrial fission regulator 1 isoform 4
                     precursor"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=30859
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=5550
     Region          22..251
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15390.2)"
     Region          177..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          179..304
                     /region_name="Necessary and sufficient to promote
                     mitochondrial fission. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     CDS             1..328
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001413074.1:132..1118"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 9"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsvlwsrkpy gssrsivrki gtnlsliqcp rvqfqinsha
       61 tewspshpge davasfadvg wvakeegecs arlrtevrsr pplqddllff ekapsrqisl
      121 pdlsqeepql ktpalaneea lqkicalene laalraqiak ivtqqeqqnl tagdldsttf
      181 gtipphpppp ppplpppalg lhqstsavdl ikerrekran agktlvknnp kkpempnmle
      241 ilkemnsvkl rsvkrseqdv kpkpvdatdp aaliaealkk kfayryrsds qdevekgipk
      301 seseatserv lslpagfiqp hvskhclg
//
LOCUS       NP_001186211            2851 aa            linear   PRI 21-NOV-2025
DEFINITION  lipopolysaccharide-responsive and beige-like anchor protein isoform
            1 [Homo sapiens].
ACCESSION   NP_001186211
VERSION     NP_001186211.2
DBSOURCE    REFSEQ: accession NM_001199282.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2851)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2851)
  AUTHORS   Szentgyorgyi,V., Lueck,L.M., Overwijn,D., Ritz,D., Zoeller,N.,
            Schmidt,A., Hondele,M., Spang,A. and Bakhtiar,S.
  TITLE     Arf1-dependent LRBA recruitment to Rab4 endosomes is required for
            endolysosome homeostasis
  JOURNAL   J Cell Biol 223 (11) (2024)
   PUBMED   39325073
  REMARK    GeneRIF: Arf1-dependent LRBA recruitment to Rab4 endosomes is
            required for endolysosome homeostasis.
REFERENCE   3  (residues 1 to 2851)
  AUTHORS   Freund,T., Baxter,S.K., Walsh,T., Golan,H., Kapelushnik,J.,
            Abramsohn-Goldenberg,M., Benor,S., Sarid,N., Ram,R., Alcalay,Y.,
            Segel,R., Renbaum,P., Stepensky,P., King,M.C., Torgerson,T.R. and
            Hagin,D.
  TITLE     Clinically Complex LRBA Deficiency Due to a Founder Allele in the
            Georgian Jewish Population
  JOURNAL   J Clin Immunol 43 (1), 151-164 (2023)
   PUBMED   36063261
  REMARK    GeneRIF: Clinically Complex LRBA Deficiency Due to a Founder Allele
            in the Georgian Jewish Population.
REFERENCE   4  (residues 1 to 2851)
  AUTHORS   Catak,M.C., Akcam,B., Bilgic Eltan,S., Babayeva,R., Karakus,I.S.,
            Akgun,G., Baser,D., Bulutoglu,A., Bayram,F., Kasap,N., Kiykim,A.,
            Hancioglu,G., Kokcu Karadag,S.I., Kendir Demirkol,Y., Ozen,S.,
            Cekic,S., Ozcan,D., Edeer Karaca,N., Sasihuseyinoglu,A.S.,
            Cansever,M., Ozek Yucel,E., Tamay,Z., Altintas,D.U., Aydogmus,C.,
            Celmeli,F., Cokugras,H., Gulez,N., Genel,F., Metin,A., Guner,S.N.,
            Kutukculer,N., Keles,S., Reisli,I., Kilic,S.S., Yildiran,A.,
            Karakoc-Aydiner,E., Lo,B., Ozen,A. and Baris,S.
  TITLE     Comparing the levels of CTLA-4-dependent biological defects in
            patients with LRBA deficiency and CTLA-4 insufficiency
  JOURNAL   Allergy 77 (10), 3108-3123 (2022)
   PUBMED   35491430
  REMARK    GeneRIF: Comparing the levels of CTLA-4-dependent biological
            defects in patients with LRBA deficiency and CTLA-4 insufficiency.
REFERENCE   5  (residues 1 to 2851)
  AUTHORS   Yao,J., Gu,H., Mou,W., Chen,Z., Ma,J., Ma,H., Li,N., Zhang,R.,
            Wang,T., Jiang,J. and Wu,R.
  TITLE     Various phenotypes of LRBA gene with compound heterozygous
            variation: A case series report of pediatric cytopenia patients
  JOURNAL   Int J Immunopathol Pharmacol 36, 3946320221125591 (2022)
   PUBMED   36074705
  REMARK    GeneRIF: Various phenotypes of LRBA gene with compound heterozygous
            variation: A case series report of pediatric cytopenia patients.
REFERENCE   6  (residues 1 to 2851)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 2851)
  AUTHORS   Gebauer,D., Li,J., Jogl,G., Shen,Y., Myszka,D.G. and Tong,L.
  TITLE     Crystal structure of the PH-BEACH domains of human LRBA/BGL
  JOURNAL   Biochemistry 43 (47), 14873-14880 (2004)
   PUBMED   15554694
  REMARK    GeneRIF: The crystal structure of the aPH-BEACH domains of LRBA
            were studied.
REFERENCE   8  (residues 1 to 2851)
  AUTHORS   Dyomin,V.G., Chaganti,S.R., Dyomina,K., Palanisamy,N., Murty,V.V.,
            Dalla-Favera,R. and Chaganti,R.S.
  TITLE     BCL8 is a novel, evolutionarily conserved human gene family
            encoding proteins with presumptive protein kinase A anchoring
            function
  JOURNAL   Genomics 80 (2), 158-165 (2002)
   PUBMED   12160729
REFERENCE   9  (residues 1 to 2851)
  AUTHORS   Wang,J.W., Howson,J., Haller,E. and Kerr,W.G.
  TITLE     Identification of a novel lipopolysaccharide-inducible gene with
            key features of both A kinase anchor proteins and chs1/beige
            proteins
  JOURNAL   J Immunol 166 (7), 4586-4595 (2001)
   PUBMED   11254716
REFERENCE   10 (residues 1 to 2851)
  AUTHORS   Feuchter,A.E., Freeman,J.D. and Mager,D.L.
  TITLE     Strategy for detecting cellular transcripts promoted by human
            endogenous long terminal repeats: identification of a novel gene
            (CDC4L) with homology to yeast CDC4
  JOURNAL   Genomics 13 (4), 1237-1246 (1992)
   PUBMED   1505956
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104796.4, AC092544.4,
            AC110813.4, AC097373.3, AC092612.3 and AC093748.3.
            
            On Sep 4, 2011 this sequence version replaced NP_001186211.1.
            
            Summary: The protein encoded by this gene is a member of the
            WDL-BEACH-WD (WBW) gene family. Its expression is induced in B
            cells and macrophages by bacterial lipopolysaccharides (LPS). The
            encoded protein associates with protein kinase A and may be
            involved in leading intracellular vesicles to activated receptor
            complexes, which aids in the secretion and/or membrane deposition
            of immune effector molecules. Defects in this gene are associated
            with the disorder common variable immunodeficiency-8 with
            autoimmunity. Two transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (1) differs in the 5' UTR, lacks
            an alternate in-frame exon, and uses an alternate in-frame splice
            junction at the 3' end of an exon compared to variant 2. The
            resulting isoform (1) has the same N- and C-termini but is shorter
            compared to isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF467287.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2154361,
                                           SAMEA2157511 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2851
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.3"
     Protein         1..2851
                     /product="lipopolysaccharide-responsive and beige-like
                     anchor protein isoform 1"
                     /note="vesicle trafficking, beach and anchor containing;
                     lipopolysaccharide-responsive and beige-like anchor
                     protein; CDC4-like protein; LPS-responsive vesicle
                     trafficking, beach and anchor containing"
                     /calculated_mol_wt=317573
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          229..376
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
     Region          441..921
                     /region_name="DUF4704"
                     /note="Neurobeachin/BDCP, DUF4704 alpha solenoid region;
                     pfam15787"
                     /db_xref="CDD:464870"
     Region          969..1005
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            979
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1003
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1018..1039
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1161..1193
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1301..1343
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1531..1548
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          1586..1668
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1759..1789
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1770
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1880..2047
                     /region_name="DUF1088"
                     /note="Neurobeachin-like, DUF1088; pfam06469"
                     /db_xref="CDD:461925"
     Site            2053
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          2073..2170
                     /region_name="PH_BEACH"
                     /note="PH domain associated with Beige/BEACH; pfam14844"
                     /db_xref="CDD:434260"
     Region          2201..2478
                     /region_name="Beach"
                     /note="Beige/BEACH domain; smart01026"
                     /db_xref="CDD:214982"
     Site            2485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          2573..2836
                     /region_name="NBCH_WD40"
                     /note="Neurobeachin beta propeller domain; pfam20426"
                     /db_xref="CDD:466575"
     Region          2580..2622
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2589..2625
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2625..2668
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2631..2683
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2683..2723
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2688..2723
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2728..2757
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2765..2804
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2770..2804
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2807..2846
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     CDS             1..2851
                     /gene="LRBA"
                     /gene_synonym="BGL; CDC4L; CVID8; LAB300; LBA; uc.147"
                     /coded_by="NM_001199282.3:303..8858"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS58928.1"
                     /db_xref="GeneID:987"
                     /db_xref="HGNC:HGNC:1742"
                     /db_xref="MIM:606453"
ORIGIN      
        1 masednrvps ppptgddggg ggreetpteg galslkpglp irgirmkfav ltglvevgev
       61 snrdivetvf nllvggqfdl emnfiiqege sincmvdlle kcditcqaev wsmftailkk
      121 sirnlqvcte vglvekvlgk iekvdnmiad llvdmlgvla synltvrelk lffsklqgdk
      181 grwpphagkl lsvlkhmpqk ygpdaffnfp gksaaaialp piakwpyqng ftfhtwlrmd
      241 pvnninvdkd kpylycfrts kglgysahfv ggclivtsik skgkgfqhcv kfdfkpqkwy
      301 mvtivhiynr wknselrcyv ngelasygei twfvntsdtf dkcflgsset adanrvfcgq
      361 mtavylfsea lnaaqifaiy qlglgykgtf kfkaesdlfl aehhklllyd gklssaiaft
      421 ynpratdaql clesspkdnp sifvhsphal mlqdvkavlt hsiqsamhsi ggvqvlfplf
      481 aqldyrqyls deidlticst llafimellk nsiamqeqml ackgflvigy sleksskshv
      541 sravlelcla fskylsnlqn gmpllkqlcd hvllnpaiwi htpakvqlml ytylstefig
      601 tvniyntirr vgtvllimht lkyyywavnp qdrsgitpkg ldgprpnqke mlslrafllm
      661 fikqlvmkds gvkedelqai lnylltmhed dnlmdvlqll valmsehpns mipafdqrng
      721 lrviykllas ksegirvqal kamgyflkhl apkrkaevml ghglfsllae rlmlqtnlit
      781 mttynvlfei lieqigtqvi hkqhpdpdss vkiqnpqilk viatllrnsp qcpesmevrr
      841 aflsdmiklf nnsrenrrsl lqcsvwqewm lslcyfnpkn sdeqkitemv yaifrillyh
      901 avkyewggwr vwvdtlsith skvtfeihke nlanifreqq gkvdeeiglc sstsvqaasg
      961 irrdinvsvg sqqpdtkdsp vcphfttngn enssiektss lesasnielq ttntsyeemk
     1021 aeqenqelpd egtleetltn etrnaddlev ssdiieavai ssnsfittgk dsmtvsevta
     1081 sisspseeda sempefldks iveeeedddy velkvegspt eeanlptelq dnslspaase
     1141 agekldmfgn ddklifqegk pvtekqtdte tqdskdsgiq tmtasgssam spettvsqia
     1201 vesdlgqmle egkkatnltr etklindchg svseasseqk iakldvsnva tdterlelka
     1261 spnveapqph rhvleisrqh eqpgqgiapd avngqrrdsr stvfripefn wsqmhqrllt
     1321 dllfsietdi qmwrshstkt vmdfvnssdn vifvhntihl isqvmdnmvm acggilplls
     1381 aatsathele nieptqglsi easvtflqrl islvdvlifa sslgfteiea eksmssggil
     1441 rqclrlvcav avrnclecqq hsqlktrgdk alkpmhslip lgksaakspv divtggispv
     1501 rdldrllqdm dinrlravvf rdiedskqaq flalavvyfi svlmvskyrd ilepqnerhs
     1561 qsctetgsen envslseitp aafstlttas veesestssa rrrdsgigee tatglgshve
     1621 vtphtappgv sagpdaisev lstlslevnk spetkndrgn dldtkatpsv svsknvnvkd
     1681 ilrslvnipa dgvtvdpall ppaclgalgd lsveqpvqfr sfdrsvivaa kksavspstf
     1741 ntsiptnavs vvssvdsaqa sdmggespgs rssnaklpsv ptvdsvsqdp vsnmsiterl
     1801 ehalekaapl lreifvdfap flsrtllgsh gqelliegts lvcmkssssv velvmllcsq
     1861 ewqnsiqkna glafielvne grllsqtmkd hlvrvaneae filsrqraed ihrhaefesl
     1921 caqysadkre dekmcdhlir aakyrdhvta tqliqkiini ltdkhgawgn savsrplefw
     1981 rldyweddlr rrrrfvrnpl gsthpeatlk tavehatded ilakgkqsir sqalgnqnse
     2041 neillegddd tlssvdekdl enlagpvsls tpaqlvapsv vvkgtlsvts selyfevdee
     2101 dpnfkkidpk ilayteglhg kwlfteirsi fsrryllqnt aleifmanrv avmfnfpdpa
     2161 tvkkvvnylp rvgvgtsfgl pqtrrislas prqlfkasnm tqrwqhreis nfeylmflnt
     2221 iagrsyndln qypvfpwvit nyeseeldlt lptnfrdlsk pigalnpkra affaeryesw
     2281 eddqvpkfhy gthystasfv lawllriepf ttyflnlqgg kfdhadrtfs sisrawrnsq
     2341 rdtsdikeli pefyylpemf vnfnnynlgv mddgtvvsdv elppwaktse efvhinrlal
     2401 esefvscqlh qwidlifgyk qqgpeavral nvfyyltyeg avnlnsitdp vlreaveaqi
     2461 rsfgqtpsql liephpprgs amqvsplmft dkaqqdvimv lkfpsnspvt hvaantqpgl
     2521 atpavitvta nrlfavnkwh nlpahqgavq dqpyqlpvei dpliasntgm hrrqitdlld
     2581 qsiqvhsqcf vitsdnryil vcgfwdksfr vystdtgrli qvvfghwdvv tclarsesyi
     2641 ggncyilsgs rdatlllwyw ngkcsgigdn pgetaaprai ltghdyevtc aavcaelglv
     2701 lsgsqegpcl ihsmngdllr tlegpenclk pkliqasreg hcvifyengl fctfsvngkl
     2761 qatmetddni raiqlsrdgq ylltggdrgv vvvrqvsdlk qlfaypgcda giramalsyd
     2821 qrciisgmas gsivlfyndf nrwhheyqtr y
//
LOCUS       NP_001428019             706 aa            linear   PRI 21-NOV-2025
DEFINITION  fibroblast growth factor receptor 2 isoform 20 precursor [Homo
            sapiens].
ACCESSION   NP_001428019 XP_016871413 XP_054221148
VERSION     NP_001428019.1
DBSOURCE    REFSEQ: accession NM_001441090.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 706)
  AUTHORS   Chen,C.P., Huang,J.P., Huang,K.S., Chen,Y.Y., Wu,F.T., Pan,Y.T.,
            Chiu,C.L. and Wang,W.
  TITLE     Perinatal imaging findings of a fetus with Pfeiffer syndrome and a
            heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation in FGFR2
            presenting a cloverleaf skull, craniosynostosis and short limbs on
            prenatal ultrasound mimicking thanatophoric dysplasia type II
  JOURNAL   Taiwan J Obstet Gynecol 63 (3), 387-390 (2024)
   PUBMED   38802203
  REMARK    GeneRIF: Perinatal imaging findings of a fetus with Pfeiffer
            syndrome and a heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation
            in FGFR2 presenting a cloverleaf skull, craniosynostosis and short
            limbs on prenatal ultrasound mimicking thanatophoric dysplasia type
            II.
REFERENCE   2  (residues 1 to 706)
  AUTHORS   Lian,Y., Bodian,D. and Shehu,A.
  TITLE     Elucidating the Role of Wildtype and Variant FGFR2 Structural
            Dynamics in (Dys)Function and Disorder
  JOURNAL   Int J Mol Sci 25 (8), 4523 (2024)
   PUBMED   38674107
  REMARK    GeneRIF: Elucidating the Role of Wildtype and Variant FGFR2
            Structural Dynamics in (Dys)Function and Disorder.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 706)
  AUTHORS   Xu,N., Hung,K.L., Gong,X., Fan,D., Tian,Y., Yan,M., Wei,Y. and
            Wang,S.
  TITLE     Genetic insights into the 'sandwich fusion' subtype of Klippel-Feil
            syndrome: novel FGFR2 mutations identified by 21 cases of
            whole-exome sequencing
  JOURNAL   Orphanet J Rare Dis 19 (1), 141 (2024)
   PUBMED   38561822
  REMARK    GeneRIF: Genetic insights into the 'sandwich fusion' subtype of
            Klippel-Feil syndrome: novel FGFR2 mutations identified by 21 cases
            of whole-exome sequencing.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 706)
  AUTHORS   Wenger,T.L., Hing,A.V. and Evans,K.N.
  TITLE     Apert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31145570
REFERENCE   5  (residues 1 to 706)
  AUTHORS   Wenger,T., Miller,D. and Evans,K.
  TITLE     FGFR Craniosynostosis Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301628
REFERENCE   6  (residues 1 to 706)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   7  (residues 1 to 706)
  AUTHORS   Dell,K.R. and Williams,L.T.
  TITLE     A novel form of fibroblast growth factor receptor 2. Alternative
            splicing of the third immunoglobulin-like domain confers ligand
            binding specificity
  JOURNAL   J Biol Chem 267 (29), 21225-21229 (1992)
   PUBMED   1400433
REFERENCE   8  (residues 1 to 706)
  AUTHORS   Luqmani,Y.A., Graham,M. and Coombes,R.C.
  TITLE     Expression of basic fibroblast growth factor, FGFR1 and FGFR2 in
            normal and malignant human breast, and comparison with other normal
            tissues
  JOURNAL   Br J Cancer 66 (2), 273-280 (1992)
   PUBMED   1380281
REFERENCE   9  (residues 1 to 706)
  AUTHORS   Katoh,M., Hattori,Y., Sasaki,H., Tanaka,M., Sugano,K., Yazaki,Y.,
            Sugimura,T. and Terada,M.
  TITLE     K-sam gene encodes secreted as well as transmembrane receptor
            tyrosine kinase
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 2960-2964 (1992)
   PUBMED   1313574
REFERENCE   10 (residues 1 to 706)
  AUTHORS   Miki,T., Bottaro,D.P., Fleming,T.P., Smith,C.L., Burgess,W.H.,
            Chan,A.M. and Aaronson,S.A.
  TITLE     Determination of ligand-binding specificity by alternative
            splicing: two distinct growth factor receptors encoded by a single
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 246-250 (1992)
   PUBMED   1309608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009988.12.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_016871413.1, XP_054221148.1.
            
            Summary: The protein encoded by this gene is a member of the
            fibroblast growth factor receptor family, where amino acid sequence
            is highly conserved between members and throughout evolution. FGFR
            family members differ from one another in their ligand affinities
            and tissue distribution. A full-length representative protein
            consists of an extracellular region, composed of three
            immunoglobulin-like domains, a single hydrophobic membrane-spanning
            segment and a cytoplasmic tyrosine kinase domain. The extracellular
            portion of the protein interacts with fibroblast growth factors,
            setting in motion a cascade of downstream signals, ultimately
            influencing mitogenesis and differentiation. This particular family
            member is a high-affinity receptor for acidic, basic and/or
            keratinocyte growth factor, depending on the isoform. Mutations in
            this gene are associated with Crouzon syndrome, Pfeiffer syndrome,
            Craniosynostosis, Apert syndrome, Jackson-Weiss syndrome,
            Beare-Stevenson cutis gyrata syndrome, Saethre-Chotzen syndrome,
            and syndromic craniosynostosis. Multiple alternatively spliced
            transcript variants encoding different isoforms have been noted for
            this gene. [provided by RefSeq, Jan 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:1309608)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..706
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..706
                     /product="fibroblast growth factor receptor 2 isoform 20
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="protein tyrosine kinase, receptor like 14;
                     bacteria-expressed kinase; keratinocyte growth factor
                     receptor; BEK fibroblast growth factor receptor"
                     /calculated_mol_wt=77118
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2298
     Region          39..133
                     /region_name="IgI_2_FGFR"
                     /note="Second immunoglobulin (Ig)-like domain of
                     fibroblast growth factor (FGF) receptor; member of the
                     I-set of IgSF domains; cd05857"
                     /db_xref="CDD:409443"
     Region          39..42
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409443"
     Region          50..55
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409443"
     Site            order(51,53,55)
                     /site_type="other"
                     /note="FGF binding site [polypeptide binding]"
                     /db_xref="CDD:409443"
     Site            order(52,59..61,63)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409443"
     Region          59..67
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409443"
     Region          73..78
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409443"
     Region          81..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409443"
     Region          92..95
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409443"
     Region          99..104
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409443"
     Region          113..120
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409443"
     Region          123..133
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409443"
     Region          141..245
                     /region_name="IgI_3_FGFR2"
                     /note="Third immunoglobulin (Ig)-like domain of fibroblast
                     growth factor receptor 2 (FGFR2); member of the I-set of
                     Ig superfamily (IgSF) domains; cd05858"
                     /db_xref="CDD:409444"
     Region          141..144
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409444"
     Region          148..152
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409444"
     Region          160..167
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409444"
     Site            order(165,170..172,201..202,206,210,231)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409444"
     Region          171..178
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409444"
     Region          193..198
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409444"
     Region          210..215
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409444"
     Region          223..231
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409444"
     Region          234..242
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409444"
     Region          341..653
                     /region_name="PTKc_FGFR2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Fibroblast Growth Factor Receptor 2; cd05101"
                     /db_xref="CDD:270679"
     Site            order(372..373,375,380,400,402,419,449..452,456,511,
                     515..516,518,529,547..551,560,594)
                     /site_type="active"
                     /db_xref="CDD:270679"
     Site            order(372..373,375,380,400,402,419,449..452,456,515..516,
                     518,529)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270679"
     Site            order(511,515,547..551,560,594)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270679"
     Site            528..553
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270679"
     CDS             1..706
                     /gene="FGFR2"
                     /gene_synonym="BBDS; BEK; BFR-1; CD332; CEK3; CFD1; ECT1;
                     JWS; K-SAM; KGFR; TK14; TK25"
                     /coded_by="NM_001441090.1:634..2754"
                     /note="isoform 20 precursor is encoded by transcript
                     variant 20"
                     /db_xref="GeneID:2263"
                     /db_xref="HGNC:HGNC:3689"
                     /db_xref="MIM:176943"
ORIGIN      
        1 mvswgrficl vvvtmatlsl arpsfslved ttlepegapy wtntekmekr lhavpaantv
       61 kfrcpaggnp mptmrwlkng kefkqehrig gykvrnqhws limesvvpsd kgnytcvven
      121 eygsinhtyh ldvversphr pilqaglpan astvvggdve fvckvysdaq phiqwikhve
      181 kngskygpdg lpylkvlkaa gvnttdkeie vlyirnvtfe dageytclag nsigisfhsa
      241 wltvlpapgr ekeitaspdy leiaiycigv fliacmvvtv ilcrmknttk kpdfssqpav
      301 hkltkriplr rqvtvsaess ssmnsntplv rittrlssta dtpmlagvse yelpedpkwe
      361 fprdkltlgk plgegcfgqv vmaeavgidk dkpkeavtva vkmlkddate kdlsdlvsem
      421 emmkmigkhk niinllgact qdgplyvive yaskgnlrey lrarrppgme ysydinrvpe
      481 eqmtfkdlvs ctyqlargme ylasqkcihr dlaarnvlvt ennvmkiadf glardinnid
      541 yykkttngrl pvkwmapeal fdrvythqsd vwsfgvlmwe iftlggspyp gipveelfkl
      601 lkeghrmdkp anctnelymm mrdcwhavps qrptfkqlve dldriltltt neeyldlsqp
      661 leqyspsypd trsscssgdd svfspdpmpy epclpqyphi ngsvkt
//
LOCUS       NP_001394744            1204 aa            linear   PRI 21-NOV-2025
DEFINITION  DNA-directed RNA polymerase, mitochondrial isoform 12 precursor
            [Homo sapiens].
ACCESSION   NP_001394744
VERSION     NP_001394744.1
DBSOURCE    REFSEQ: accession NM_001407815.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1204)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1204)
  AUTHORS   Yan,W., Xie,C., Sun,S., Zheng,Q., Wang,J., Wang,Z., Man,C.H.,
            Wang,H., Yang,Y., Wang,T., Shi,L., Zhang,S., Huang,C., Xu,S. and
            Wang,Y.P.
  TITLE     SUCLG1 restricts POLRMT succinylation to enhance mitochondrial
            biogenesis and leukemia progression
  JOURNAL   EMBO J 43 (12), 2337-2367 (2024)
   PUBMED   38649537
  REMARK    GeneRIF: SUCLG1 restricts POLRMT succinylation to enhance
            mitochondrial biogenesis and leukemia progression.
REFERENCE   3  (residues 1 to 1204)
  AUTHORS   Liu,Y., Chen,Z., Wang,Z.H., Delaney,K.M., Tang,J., Pirooznia,M.,
            Lee,D.Y., Tunc,I., Li,Y. and Xu,H.
  TITLE     The PPR domain of mitochondrial RNA polymerase is an
            exoribonuclease required for mtDNA replication in Drosophila
            melanogaster
  JOURNAL   Nat Cell Biol 24 (5), 757-765 (2022)
   PUBMED   35449456
REFERENCE   4  (residues 1 to 1204)
  AUTHORS   Inatomi,T., Matsuda,S., Ishiuchi,T., Do,Y., Nakayama,M., Abe,S.,
            Kasho,K., Wanrooij,S., Nakada,K., Ichiyanagi,K., Sasaki,H.,
            Yasukawa,T. and Kang,D.
  TITLE     TFB2M and POLRMT are essential for mammalian mitochondrial DNA
            replication
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1869 (1), 119167 (2022)
   PUBMED   34744028
  REMARK    GeneRIF: TFB2M and POLRMT are essential for mammalian mitochondrial
            DNA replication.
REFERENCE   5  (residues 1 to 1204)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 1204)
  AUTHORS   Graziewicz,M.A., Longley,M.J., Bienstock,R.J., Zeviani,M. and
            Copeland,W.C.
  TITLE     Structure-function defects of human mitochondrial DNA polymerase in
            autosomal dominant progressive external ophthalmoplegia
  JOURNAL   Nat Struct Mol Biol 11 (8), 770-776 (2004)
   PUBMED   15258572
  REMARK    GeneRIF: human mitochondrial DNA polymerase has a role in autosomal
            dominant progressive external ophthalmoplegia
REFERENCE   7  (residues 1 to 1204)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   8  (residues 1 to 1204)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 1204)
  AUTHORS   Falkenberg,M., Gaspari,M., Rantanen,A., Trifunovic,A., Larsson,N.G.
            and Gustafsson,C.M.
  TITLE     Mitochondrial transcription factors B1 and B2 activate
            transcription of human mtDNA
  JOURNAL   Nat Genet 31 (3), 289-294 (2002)
   PUBMED   12068295
REFERENCE   10 (residues 1 to 1204)
  AUTHORS   Tiranti,V., Savoia,A., Forti,F., D'Apolito,M.F., Centra,M.,
            Rocchi,M. and Zeviani,M.
  TITLE     Identification of the gene encoding the human mitochondrial RNA
            polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence
            Tags database
  JOURNAL   Hum Mol Genet 6 (4), 615-625 (1997)
   PUBMED   9097968
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004449.1.
            
            Summary: This gene encodes a mitochondrial DNA-directed RNA
            polymerase. The gene product is responsible for mitochondrial gene
            expression as well as for providing RNA primers for initiation of
            replication of the mitochondrial genome. Although this polypeptide
            has the same function as the three nuclear DNA-directed RNA
            polymerases, it is more closely related to RNA polymerases of phage
            and mitochondrial polymerases of lower eukaryotes. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.866744.1,
                                           SRR14038191.697999.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1204
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1204
                     /product="DNA-directed RNA polymerase, mitochondrial
                     isoform 12 precursor"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) mitochondrial (DNA directed)"
                     /calculated_mol_wt=135417
     Region          261..290
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          296..323
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          432..704
                     /region_name="RPOL_N"
                     /note="DNA-directed RNA polymerase N-terminal; pfam14700"
                     /db_xref="CDD:464270"
     Region          831..1204
                     /region_name="RNA_pol"
                     /note="DNA-dependent RNA polymerase; pfam00940"
                     /db_xref="CDD:460006"
     CDS             1..1204
                     /gene="POLRMT"
                     /gene_synonym="APOLMT; COXPD55; h-mtRPOL; MTRNAP; MTRPOL"
                     /coded_by="NM_001407815.1:26..3640"
                     /note="isoform 12 precursor is encoded by transcript
                     variant 12"
                     /db_xref="GeneID:5442"
                     /db_xref="HGNC:HGNC:9200"
                     /db_xref="MIM:601778"
ORIGIN      
        1 msalcwgrga aglkralrpc grpglpgkeg taggvcgprr sssaspqeqd qdrrkdwghv
       61 ellevlqarv rqlqaesvse vvvnrvdvar lpecgsgdgs lqpprkvqmg akdatpvpcg
      121 rwakilekdk rtqqmrmqrl kaklqmpfqs gefkaltrrl qveprllskq magcledctr
      181 qapespweeq larllqeapg klsldveqap sgqhsqaqls gqqqrllaff kcclltdqlp
      241 lahhllvvhh gqrqkrkllt ldmynavmlg warqgafkel vyvlfmvkda gltpdllsya
      301 aalqcmgrqd qdagtiercl eqmsqeglkl qalftavlls eedratvlka vhkvkptfsl
      361 ppqlpppvnt skllrdvyak dgrvsypklh lplktlqclf ekqlhmelas rvcvvsvekp
      421 tlpskevkha rktlktlrdq wekalcralr etknrlerev yegrfslypf lcllderevv
      481 rmllqvlqal paqgesfttl arelsartfs rhvvqrqrvs gqvqalqnhy rkylcllasd
      541 aevpepclpr qyweelgape alreqpwplp vqmelgklla emlvqatqmp csldkphrss
      601 rlvpvlyhvy sfrnvqqigi lkphpayvql lekaaeptlt feavdvpmlc pplpwtsphs
      661 gafllsptkl mrtvegatqh qelletcppt alhgaldalt qlgncawrvn grvldlvlql
      721 fqakgcpqlg vpappseapq ppeahlphsa aparkaelrr elahcqkvar emhslraeal
      781 yrlslaqhlr drvfwlphnm dfrgrtypcp phfnhlgsdv arallefaqg rplgphgldw
      841 lkihlvnltg lkkreplrkr lafaeevmdd ildsadqplt grkwwmgaee pwqtlaccme
      901 vanavrasdp aayvshlpvh qdgscnglqh yaalgrdsvg aasvnlepsd vpqdvysgva
      961 aqvvkqtvmt vvygvtrygg rlqiekrlre lsdfpqefvw eashylvrqv fkslqemfsg
     1021 traiqhwlte sarlishmgs vvewvtplgv pviqpyrlds kvkqigggiq sitythngdi
     1081 srkpntrkqk ngfppnfihs ldsshmmlta lhcyrkgltf vsvhdcywth aadvsvmnqv
     1141 creqfvrlhs epilqdlsrf lvkrfcsepq kileasqlke tlqavpkpga fdleqvkrst
     1201 yffs
//
LOCUS       NP_001393533            1158 aa            linear   PRI 21-NOV-2025
DEFINITION  hamartin isoform 6 [Homo sapiens].
ACCESSION   NP_001393533
VERSION     NP_001393533.1
DBSOURCE    REFSEQ: accession NM_001406604.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1158)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1158)
  AUTHORS   Wang,C., Zhai,J.X. and Chen,Y.J.
  TITLE     Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review
  JOURNAL   Medicine (Baltimore) 103 (42), e40151 (2024)
   PUBMED   39432612
  REMARK    GeneRIF: Identification of a novel TSC1 variant in a family with
            developmental and epileptic encephalopathies: A case report and
            literature review.
            Review article
REFERENCE   3  (residues 1 to 1158)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1158)
  AUTHORS   Huang,J. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex: a molecular switchboard controlling cell
            growth
  JOURNAL   Biochem J 412 (2), 179-190 (2008)
   PUBMED   18466115
  REMARK    Review article
REFERENCE   5  (residues 1 to 1158)
  AUTHORS   Huang,J., Dibble,C.C., Matsuzaki,M. and Manning,B.D.
  TITLE     The TSC1-TSC2 complex is required for proper activation of mTOR
            complex 2
  JOURNAL   Mol Cell Biol 28 (12), 4104-4115 (2008)
   PUBMED   18411301
  REMARK    GeneRIF: the TSC1-TSC2 complex inhibits mTORC1 and activates
            mTORC2, which through different mechanisms promotes Akt activation
REFERENCE   6  (residues 1 to 1158)
  AUTHORS   Plank,T.L., Yeung,R.S. and Henske,E.P.
  TITLE     Hamartin, the product of the tuberous sclerosis 1 (TSC1) gene,
            interacts with tuberin and appears to be localized to cytoplasmic
            vesicles
  JOURNAL   Cancer Res 58 (21), 4766-4770 (1998)
   PUBMED   9809973
REFERENCE   7  (residues 1 to 1158)
  AUTHORS   van Slegtenhorst,M., Nellist,M., Nagelkerken,B., Cheadle,J.,
            Snell,R., van den Ouweland,A., Reuser,A., Sampson,J., Halley,D. and
            van der Sluijs,P.
  TITLE     Interaction between hamartin and tuberin, the TSC1 and TSC2 gene
            products
  JOURNAL   Hum Mol Genet 7 (6), 1053-1057 (1998)
   PUBMED   9580671
REFERENCE   8  (residues 1 to 1158)
  AUTHORS   Jones,A.C., Daniells,C.E., Snell,R.G., Tachataki,M.,
            Idziaszczyk,S.A., Krawczak,M., Sampson,J.R. and Cheadle,J.P.
  TITLE     Molecular genetic and phenotypic analysis reveals differences
            between TSC1 and TSC2 associated familial and sporadic tuberous
            sclerosis
  JOURNAL   Hum Mol Genet 6 (12), 2155-2161 (1997)
   PUBMED   9328481
REFERENCE   9  (residues 1 to 1158)
  AUTHORS   van Slegtenhorst,M., de Hoogt,R., Hermans,C., Nellist,M.,
            Janssen,B., Verhoef,S., Lindhout,D., van den Ouweland,A.,
            Halley,D., Young,J., Burley,M., Jeremiah,S., Woodward,K.,
            Nahmias,J., Fox,M., Ekong,R., Osborne,J., Wolfe,J., Povey,S.,
            Snell,R.G., Cheadle,J.P., Jones,A.C., Tachataki,M., Ravine,D.,
            Sampson,J.R., Reeve,M.P., Richardson,P., Wilmer,F., Munro,C.,
            Hawkins,T.L., Sepp,T., Ali,J.B., Ward,S., Green,A.J., Yates,J.R.,
            Kwiatkowska,J., Henske,E.P., Short,M.P., Haines,J.H., Jozwiak,S.
            and Kwiatkowski,D.J.
  TITLE     Identification of the tuberous sclerosis gene TSC1 on chromosome
            9q34
  JOURNAL   Science 277 (5327), 805-808 (1997)
   PUBMED   9242607
REFERENCE   10 (residues 1 to 1158)
  AUTHORS   Northrup,H., Koenig,M.K., Pearson,D.A. and Au,K.S.
  TITLE     Tuberous Sclerosis Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301399
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445645.10.
            
            Summary: This gene is a tumor suppressor gene that encodes the
            growth inhibitory protein hamartin. The encoded protein interacts
            with and stabilizes the GTPase activating protein tuberin. This
            hamartin-tuberin complex negatively regulates mammalian target of
            rapamycin complex 1 (mTORC1) signaling which is a major regulator
            of anabolic cell growth. This protein also functions as a
            co-chaperone for Hsp90 that inhibits its ATPase activity. This
            protein functions as a facilitator of Hsp90-mediated folding of
            kinase and non-kinase clients, including TSC2 and thereby
            preventing their ubiquitination and proteasomal degradation.
            Mutations in this gene have been associated with tuberous sclerosis
            and lymphangioleiomyomatosis. [provided by RefSeq, May 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2985264.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1158
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..1158
                     /product="hamartin isoform 6"
                     /note="hamartin; tuberous sclerosis 1 protein"
                     /calculated_mol_wt=129140
     Region          7..713
                     /region_name="Hamartin"
                     /note="Hamartin protein; pfam04388"
                     /db_xref="CDD:461287"
     Region          438..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15963462,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          <702..>954
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1000..1079
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     Site            1094
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92574.2)"
     Region          1125..1158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92574.2)"
     CDS             1..1158
                     /gene="TSC1"
                     /gene_synonym="LAM; TSC"
                     /coded_by="NM_001406604.1:218..3694"
                     /note="isoform 6 is encoded by transcript variant 18"
                     /db_xref="GeneID:7248"
                     /db_xref="HGNC:HGNC:12362"
                     /db_xref="MIM:605284"
ORIGIN      
        1 maqqanvgel lamldspmlg vrddvtavfk enlnsdrgpm lvntlvdyyl etssqpalhi
       61 lttlqephdk hlldrineyv gkaatrlsil sllghvirlq pswkhklsqa pllpsllkcl
      121 kmdtdvvvlt tgvlvlitml pmipqsgkqh lldffdifgr lsswclkkpg hvaevylvhl
      181 hasvyalfhr lygmypcnfv sflrshysmk enletfeevv kpmmehvrih pelvtgskdh
      241 eldprrwkrl ethdvvieca kisldpteas yedgysvshq isarfphrsa dvttspyadt
      301 qnsygcatst pystsrlmll nmpgqlpqtl sspstrlite ppqatlwsps mvcgmttppt
      361 spgnvppdls hpyskvfgtt ggkgtplgtp atspppaplc hsddyvhisl pqatvtpprk
      421 eermdsarpc lhrqhhllnd rgseeppgsk gsvtlsdlpg flgdlaseed siekdkeeaa
      481 isrelseitt aeaepvvprg gfdspfyrds lpgsqrkths aasssqgasv npeplhssld
      541 klgpdtpkqa ftpidlpcgs adespagdre cqtsletsif tpspckippp trvgfgsgqp
      601 ppydhlfeva lpktahhfvi rkteellkka kgnteedgvp stspmevldr liqqgadahs
      661 kelnklplps ksvdwthfgd eirtlrdqll llhnqllyer fkrqqhalrn rrllrkvika
      721 aaleehnaam kdqlklqekd iqmwkvslqk eqarynqlqe qrdtmvtklh sqirqlqhdr
      781 eefynqsqel qtkledcrnm iaelrielkk annkvchtel llsqvsqkls nsesvqqqme
      841 flnrqllvlg evnelyleql qnkhsdttke vemmkaayrk eleknrshvl qqtqrldtsq
      901 krileleshl akkdhllleq kkyledvklq argqlqaaes ryeaqkritq vfeleildly
      961 grlekdgllk kleeekaeaa eaaeerldcc ndgcsdsmvg hneeasghng etktprpssa
     1021 rgssgsrggg gssssssels tpekpphqra gpfssrwett mgeasasipt tvgslpssks
     1081 flgmkarelf rnksesqcde dgmtsslses lktelgkdlg veakiplnld gphpspptpd
     1141 svgqlhimdy nethhehs
//
LOCUS       NP_001158286            1328 aa            linear   PRI 21-NOV-2025
DEFINITION  apoptotic chromatin condensation inducer in the nucleus isoform 2
            [Homo sapiens].
ACCESSION   NP_001158286
VERSION     NP_001158286.2
DBSOURCE    REFSEQ: accession NM_001164814.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1328)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1328)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1328)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1328)
  AUTHORS   Chen,Y.S., Liu,C.W., Lin,Y.C., Tsai,C.Y., Yang,C.H. and Lin,J.C.
  TITLE     The SRSF3-MBNL1-Acin1 circuit constitutes an emerging axis to
            lessen DNA fragmentation in colorectal cancer via an alternative
            splicing mechanism
  JOURNAL   Neoplasia 22 (12), 702-713 (2020)
   PUBMED   33142236
  REMARK    GeneRIF: The SRSF3-MBNL1-Acin1 circuit constitutes an emerging axis
            to lessen DNA fragmentation in colorectal cancer via an alternative
            splicing mechanism.
REFERENCE   5  (residues 1 to 1328)
  AUTHORS   Xue,L., Xie,L., Song,X. and Song,X.
  TITLE     [Expression and Significance of ACIN1 mRNA in Platelets of Lung
            Cancer]
  JOURNAL   Zhongguo Fei Ai Za Zhi 21 (9), 677-681 (2018)
   PUBMED   30201066
  REMARK    GeneRIF: ACIN1 mRNA was highly expressed in platelets of lung
            cancer patients
REFERENCE   6  (residues 1 to 1328)
  AUTHORS   Hu,Y., Yao,J., Liu,Z., Liu,X., Fu,H. and Ye,K.
  TITLE     Akt phosphorylates acinus and inhibits its proteolytic cleavage,
            preventing chromatin condensation
  JOURNAL   EMBO J 24 (20), 3543-3554 (2005)
   PUBMED   16177823
  REMARK    GeneRIF: Akt phosphorylation of acinus on serine 422 and 573
            results in its resistance to caspase cleavage in the nucleus and
            the inhibition of acinus-dependent chromatin condensation.
REFERENCE   7  (residues 1 to 1328)
  AUTHORS   Schwerk,C., Prasad,J., Degenhardt,K., Erdjument-Bromage,H.,
            White,E., Tempst,P., Kidd,V.J., Manley,J.L., Lahti,J.M. and
            Reinberg,D.
  TITLE     ASAP, a novel protein complex involved in RNA processing and
            apoptosis
  JOURNAL   Mol Cell Biol 23 (8), 2981-2990 (2003)
   PUBMED   12665594
REFERENCE   8  (residues 1 to 1328)
  AUTHORS   Sordet,O., Rebe,C., Plenchette,S., Zermati,Y., Hermine,O.,
            Vainchenker,W., Garrido,C., Solary,E. and Dubrez-Daloz,L.
  TITLE     Specific involvement of caspases in the differentiation of
            monocytes into macrophages
  JOURNAL   Blood 100 (13), 4446-4453 (2002)
   PUBMED   12393560
REFERENCE   9  (residues 1 to 1328)
  AUTHORS   Zermati,Y., Garrido,C., Amsellem,S., Fishelson,S., Bouscary,D.,
            Valensi,F., Varet,B., Solary,E. and Hermine,O.
  TITLE     Caspase activation is required for terminal erythroid
            differentiation
  JOURNAL   J Exp Med 193 (2), 247-254 (2001)
   PUBMED   11208865
REFERENCE   10 (residues 1 to 1328)
  AUTHORS   Sahara,S., Aoto,M., Eguchi,Y., Imamoto,N., Yoneda,Y. and
            Tsujimoto,Y.
  TITLE     Acinus is a caspase-3-activated protein required for apoptotic
            chromatin condensation
  JOURNAL   Nature 401 (6749), 168-173 (1999)
   PUBMED   10490026
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL117258.4 and AL132780.5.
            
            On Dec 12, 2023 this sequence version replaced NP_001158286.1.
            
            Summary: Apoptosis is defined by several morphologic nuclear
            changes, including chromatin condensation and nuclear
            fragmentation. This gene encodes a nuclear protein that induces
            apoptotic chromatin condensation after activation by caspase-3,
            without inducing DNA fragmentation. This protein has also been
            shown to be a component of a splicing-dependent multiprotein exon
            junction complex (EJC) that is deposited at splice junctions on
            mRNAs, as a consequence of pre-mRNA splicing. It may thus be
            involved in mRNA metabolism associated with splicing. Alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (2) uses two alternate in-frame
            splice sites in the 3' coding region, compared to variant 1. This
            results in a shorter protein (isoform 2), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC140805.1, SRR18074967.205189.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..1328
                     /product="apoptotic chromatin condensation inducer in the
                     nucleus isoform 2"
                     /note="apoptotic chromatin condensation inducer in the
                     nucleus; functional spliceosome-associated protein 152"
                     /calculated_mol_wt=150426
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          72..106
                     /region_name="SAP"
                     /note="Putative DNA-binding (bihelical) motif predicted to
                     be involved in chromosomal organisation; smart00513"
                     /db_xref="CDD:128789"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          159..460
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          <210..413
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            388
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            453
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          475..530
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            561
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            654
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, by EHMT2, alternate.
                     /evidence=ECO:0000269|PubMed:18438403;
                     N6,N6-dimethyllysine, by EHMT2, alternate.
                     /evidence=ECO:0000269|PubMed:18438403; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            682
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            710
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            714
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            717
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            825
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     Phosphoserine. /evidence=ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            837
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            860
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9JIX8; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          879..940
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            882
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            885
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            963
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            974
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            977
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            991
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          998..1084
                     /region_name="RRM_ACINU"
                     /note="RNA recognition motif (RRM) found in apoptotic
                     chromatin condensation inducer in the nucleus (acinus) and
                     similar proteins; cd12432"
                     /db_xref="CDD:409866"
     Site            1080..1081
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          1085..1328
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Site            1167
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by SRPK2 and PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:18559500; propagated from
                     UniProtKB/Swiss-Prot (Q9UKV3.2)"
     Region          <1193..1223
                     /region_name="RSB_motif"
                     /note="RNSP1-SAP18 binding (RSB) motif; pfam16294"
                     /db_xref="CDD:465085"
     Region          1197..1224
                     /region_name="Sufficient for interaction with RNPS1 and
                     SAP18 and formation of the ASAP complex.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKV3.2)"
     CDS             1..1328
                     /gene="ACIN1"
                     /gene_synonym="ACINUS; ACN; fSAP152"
                     /coded_by="NM_001164814.2:186..4172"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55905.1"
                     /db_xref="GeneID:22985"
                     /db_xref="HGNC:HGNC:17066"
                     /db_xref="MIM:604562"
ORIGIN      
        1 mwrrkhprts ggtrgvlsgn rgveygsgrg hlgtfegrwr klpkmpeavg tdpstsrkma
       61 eleevtldgk plqalrvtdl kaaleqrgla ksgqksalvk rlkgalmlen lqkhstphaa
      121 fqpnsqigee msqnsfikqy lekqqellrq rlereareaa eleeasaese demihpegva
      181 sllppdfqss lerpelelsr hsprksssis eekgdsddek prkgerrssr vrqaraakls
      241 egsqpaeeee dqetpsrnlr vradrnlkte eeeeeeeeee eddeeeegdd egqksreapi
      301 lkefkeegee iprvkpeemm derpktrsqe qevlerggrf trsqeearks hlarqqqeke
      361 mkttspleee ereikssqgl kekskspspp rltedrkkas lvalpeqtas eeetpppllt
      421 keassppphp qlhseeeiep megpapavli qlsppntdad trellvsqht vqlvgglspl
      481 sspsdtkaes paekvpeesv lplvqkstla dysaqkdlep esdrsaqplp lkieelalak
      541 giteeclkqp sleqkegrra shtllpshrl kqsadssssr sssssssssr srsrspdssg
      601 srshsplrsk qrdvaqarth anprgrpkmg srstsesrsr srsrsrsass nsrkslspgv
      661 srdsstsyte tkdpssgqev atppvpqlqv cepkertsts sssvqarrls qpesaekhvt
      721 qrlqpergsp kkceaeeaep paatqpqtse tqtshlpese rihhtveeke evtmdtsenr
      781 pendvpeppm piadqvsndd rpegsvedee kkesslpksf krkisvvstk gvpagnsdte
      841 ggqpgrkrrw gastattqkk psisittesl keavvdlhad dsrisedete rngddgthdk
      901 glkicrtvtq vvpaegqeng qreeeeeeke peaeppvppq vsvevalppp aehevkkvtl
      961 gdtltrrsis qqksgvsiti ddpvrtaqvp spprgkisni vhisnlvrpf tlgqlkellg
     1021 rtgtlveeaf widkikshcf vtystveeav atrtalhgvk wpqsnpkflc adyaeqdeld
     1081 yhrgllvdrp setkteeqgi prplhppppp pvqppqhpra eqreqeravr eqwaererem
     1141 errertrser ewdrdkvreg prsrsrsrdr rrkerakske kksekkekaq eeppaklldd
     1201 lfrktkaapc iywlpltdsq ivqkeaerae rakerekrrk eqeeeeqker ekeaerernr
     1261 qlerekrreh srerdrerer ererdrgdrd rdrerdrerg rerdrrdtkr hsrsrsrstp
     1321 vrdrggrr
//
LOCUS       NP_001427681             572 aa            linear   PRI 21-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform n [Homo sapiens].
ACCESSION   NP_001427681 XP_016877020 XP_054232484
VERSION     NP_001427681.1
DBSOURCE    REFSEQ: accession NM_001440752.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 572)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 572)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 572)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 572)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            On or before May 28, 2025 this sequence version replaced
            XP_016877020.1, XP_054232484.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4072546.1,
                                           SRR14038192.2008877.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..572
                     /product="lysosomal cobalamin transporter ABCD4 isoform n"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=64132
     Region          27..294
                     /region_name="ABC_membrane_2"
                     /note="ABC transporter transmembrane region 2; pfam06472"
                     /db_xref="CDD:399466"
     Site            43..63
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Site            76..96
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Site            190..210
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Site            279..299
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Site            314..334
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Region          387..>481
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            421..428
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213190"
     Site            458..461
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213190"
     CDS             1..572
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_001440752.1:23..1741"
                     /note="isoform n is encoded by transcript variant 35"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 mavagpapga garprldlqf lqrflqilkv lfpswssqna lmfltllclt lleqfviyqv
       61 glipsqyygv lgnkdlegfk tltflavmli vlnstlksfd qftcnllyvs wrkdltehlh
      121 rlyfrgrayy tlnvlrddid npdqrisqdv erfcrqlssm askliispft lvyytyqcfq
      181 stgwlgpvsi fgyfilgtvv nktlmgpivm klvhqekleg dfrfkhmqir vnaepaafyr
      241 aghvehmrtd rrlqrllqtq relmskelwl yigintfdyl gsilsyvvia ipifsgvygd
      301 lspaelstlv sknafvciyl iscftqlidl sttlsdvagy thrigqlret lldmslksqd
      361 ceilgesewg ldtppgwpaa epadtaflle rvsisapssd kplikdlslk isegqsllit
      421 gntgtgktsl lrvlgglwts trgsvqmltd fgphgvlflp qkpfftdgtl reqviyplke
      481 vypdsgsadd erilrflela glvsgerdpq dpsppgstsy sptwwqgqra wtsrwtgtgm
      541 mfcprgrcng splpdsstcs rstqclmkpp vp
//
LOCUS       NP_001427331             956 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001427331
VERSION     NP_001427331.1
DBSOURCE    REFSEQ: accession NM_001440402.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 956)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 956)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 956)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 956)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 956)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 956)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 956)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 956)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 956)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 956)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3, AP004147.3 and
            AP001929.5.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2218904.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..956
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..956
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     1 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=105201
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..402
                     /region_name="PBP1_iGluR_Kainate_KA1_2"
                     /note="N-terminal leucine-isoleucine-valine binding
                     protein (LIVBP)-like domain of the KA1 and KA2 subunits of
                     Kainate receptor; cd06394"
                     /db_xref="CDD:380616"
     Site            order(75..77,81,113,166,169,173,176,179..180,190..193)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380616"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            286
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            323
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            408
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Region          415..785
                     /region_name="PBP2_iGluR_kainate_KA1"
                     /note="The ligand-binding domain of the kainate subtype
                     KA1 of ionotropic glutamate receptors, a member of the
                     type 2 periplasmic-binding fold protein superfamily;
                     cd13724"
                     /db_xref="CDD:270442"
     Site            415
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            order(417,424,431,462..463,468..469)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:270442"
     Site            order(473,500..502,507)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270442"
     Site            479
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            546..566
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16099.2)"
     Site            624..644
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16099.2)"
     Site            736
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            805..825
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16099.2)"
     Region          863..889
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16099.2)"
     Region          931..956
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16099.2)"
     CDS             1..956
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440402.1:863..3733"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk aaelgmvsay
      241 ytyiftnlef slqrmdslvd drvnilgfsi fnqshaffqe faqslnqswq encdhvpftg
      301 palssallfd avyavvtavq elnrsqeigv kplscgsaqi wqhgtslmny lrmveleglt
      361 ghiefnskgq rsnyalkilq ftrngfrqig qwhvaeglsm dshlyasnis dtlfnttlvv
      421 ttilenpylm lkgnhqemeg ndryegfcvd mlkelaeilr fnykirlvgd gvygvpeang
      481 twtgmvgeli arkadlavag ltitaerekv idfskpfmtl gisilyrvhm grkpgyfsfl
      541 dpfspgvwlf mllaylavsc vlflvarltp yewysphpca qgrcnllvnq yslgnslwfp
      601 vggfmqqgst iapralstrc vsgvwwaftl iiissytanl aafltvqrmd vpiesvddla
      661 dqtaieygti hggssmtffq nsryqtyqrm wnymyskqps vfvksteegi arvlnsnyaf
      721 llestmneyy rqrncnltqi gglldtkgyg igmpvgsvfr defdlailql qennrleilk
      781 rkwweggkcp keedhrakgl gmeniggifv vlicglivai fmamleflwt lrhseatevs
      841 vcqemvtelr siilcqdsih prrrraavpp prppipeerr prgtatlsng klcgagepdq
      901 laqrlaqeaa lvargcthir vcpecrrfqg lrarpspars eeslewektt nssepe
//
LOCUS       NP_001393390            1187 aa            linear   PRI 21-NOV-2025
DEFINITION  non-receptor tyrosine-protein kinase TYK2 isoform 2 [Homo sapiens].
ACCESSION   NP_001393390 XP_011526547
VERSION     NP_001393390.1
DBSOURCE    REFSEQ: accession NM_001406461.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1187)
  AUTHORS   Chen,H., Ge,X., Li,C., Zeng,J. and Wang,X.
  TITLE     Structure and assembly of the human IL-12 signaling complex
  JOURNAL   Structure 32 (10), 1640-1651 (2024)
   PUBMED   39111304
REFERENCE   2  (residues 1 to 1187)
  AUTHORS   Lesgidou,N. and Vlassi,M.
  TITLE     Community analysis of large-scale molecular dynamics simulations
            elucidated dynamics-driven allostery in tyrosine kinase 2
  JOURNAL   Proteins 92 (4), 474-498 (2024)
   PUBMED   37950407
  REMARK    GeneRIF: Community analysis of large-scale molecular dynamics
            simulations elucidated dynamics-driven allostery in tyrosine kinase
            2.
REFERENCE   3  (residues 1 to 1187)
  AUTHORS   Zhang,M., Liu,Z., Zhu,Y., Wu,K., Zhou,L., Peng,Y., Pan,J., Chen,B.,
            Wang,X. and Chen,S.
  TITLE     Associations of genetic variants within TYK2 with pulmonary
            tuberculosis among Chinese population
  JOURNAL   Mol Genet Genomic Med 12 (2), e2386 (2024)
   PUBMED   38337161
  REMARK    GeneRIF: Associations of genetic variants within TYK2 with
            pulmonary tuberculosis among Chinese population.
REFERENCE   4  (residues 1 to 1187)
  AUTHORS   Benmansour,R., Tagajdid,M.R., El Hamzaoui,H., Fjouji,S., Doghmi,N.,
            Houba,A., Belbacha,I., Elkochri,S., Aabi,R., Elannaz,H.,
            Laraqui,A., El Mchichi,B., Chmitah,T., Touil,N., Ennibi,K.,
            Eljaoudi,R., Elmir,E., Amine Lahlou,I. and Oumzil,H.
  TITLE     TYK2, IFITM3, IFNAR2 and OAS3 single-nucleotide polymorphisms among
            severe COVID-19 ICU patients in Morocco
  JOURNAL   Int J Immunopathol Pharmacol 38, 3946320241257241 (2024)
   PUBMED   38760017
  REMARK    GeneRIF: TYK2, IFITM3, IFNAR2 and OAS3 single-nucleotide
            polymorphisms among severe COVID-19 ICU patients in Morocco.
REFERENCE   5  (residues 1 to 1187)
  AUTHORS   Yang,Z., Xiang,Q. and Nicholas,J.
  TITLE     Direct and biologically significant interactions of human
            herpesvirus 8 interferon regulatory factor 1 with STAT3 and Janus
            kinase TYK2
  JOURNAL   PLoS Pathog 19 (11), e1011806 (2023)
   PUBMED   37983265
  REMARK    GeneRIF: Direct and biologically significant interactions of human
            herpesvirus 8 interferon regulatory factor 1 with STAT3 and Janus
            kinase TYK2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1187)
  AUTHORS   Tavernier,J., Tuypens,T., Plaetinck,G., Verhee,A., Fiers,W. and
            Devos,R.
  TITLE     Molecular basis of the membrane-anchored and two soluble isoforms
            of the human interleukin 5 receptor alpha subunit
  JOURNAL   Proc Natl Acad Sci U S A 89 (15), 7041-7045 (1992)
   PUBMED   1495999
REFERENCE   7  (residues 1 to 1187)
  AUTHORS   Velazquez,L., Fellous,M., Stark,G.R. and Pellegrini,S.
  TITLE     A protein tyrosine kinase in the interferon alpha/beta signaling
            pathway
  JOURNAL   Cell 70 (2), 313-322 (1992)
   PUBMED   1386289
REFERENCE   8  (residues 1 to 1187)
  AUTHORS   Partanen,J., Makela,T.P., Alitalo,R., Lehvaslaiho,H. and Alitalo,K.
  TITLE     Putative tyrosine kinases expressed in K-562 human leukemia cells
  JOURNAL   Proc Natl Acad Sci U S A 87 (22), 8913-8917 (1990)
   PUBMED   2247464
REFERENCE   9  (residues 1 to 1187)
  AUTHORS   Firmbach-Kraft,I., Byers,M., Shows,T., Dalla-Favera,R. and
            Krolewski,J.J.
  TITLE     tyk2, prototype of a novel class of non-receptor tyrosine kinase
            genes
  JOURNAL   Oncogene 5 (9), 1329-1336 (1990)
   PUBMED   2216457
REFERENCE   10 (residues 1 to 1187)
  AUTHORS   Krolewski,J.J., Lee,R., Eddy,R., Shows,T.B. and Dalla-Favera,R.
  TITLE     Identification and chromosomal mapping of new human tyrosine kinase
            genes
  JOURNAL   Oncogene 5 (3), 277-282 (1990)
   PUBMED   2156206
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011557.7.
            
            On May 16, 2022 this sequence version replaced XP_011526547.1.
            
            Summary: This gene encodes a member of the tyrosine kinase and,
            more specifically, the Janus kinases (JAKs) protein families. This
            protein associates with the cytoplasmic domain of type I and type
            II cytokine receptors and promulgate cytokine signals by
            phosphorylating receptor subunits. It is also a component of both
            the type I and type III interferon signaling pathways. As such, it
            may play a role in anti-viral immunity. A mutation in this gene has
            been associated with Immunodeficiency 35. [provided by RefSeq, Sep
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853559.16342.1,
                                           SRR14038195.362340.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1187
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..1187
                     /product="non-receptor tyrosine-protein kinase TYK2
                     isoform 2"
                     /EC_number="2.7.10.2"
                     /note="non-receptor tyrosine-protein kinase TYK2"
                     /calculated_mol_wt=133519
     Region          28..125
                     /region_name="FERM_F1"
                     /note="FERM F1 ubiquitin-like domain; pfam18379"
                     /db_xref="CDD:465733"
     Region          143..266
                     /region_name="FERM_F2"
                     /note="FERM F2 acyl-CoA binding protein-like domain;
                     pfam18377"
                     /db_xref="CDD:436450"
     Region          285..432
                     /region_name="Jak1_Phl"
                     /note="Jak1 pleckstrin homology-like domain; pfam17887"
                     /db_xref="CDD:465552"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P29597.3)"
     Region          335..366
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29597.3)"
     Region          437..534
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(457,474,504,506)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198244"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P29597.3)"
     Site            order(505,532)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198244"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R117; propagated from
                     UniProtKB/Swiss-Prot (P29597.3)"
     Region          589..867
                     /region_name="PTK_Tyk2_rpt1"
                     /note="Pseudokinase (repeat 1) domain of the Protein
                     Tyrosine Kinase, Tyrosine kinase 2; cd05076"
                     /db_xref="CDD:270661"
     Site            604
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9R117; propagated from
                     UniProtKB/Swiss-Prot (P29597.3)"
     Region          610..629
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29597.3)"
     Site            884
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P29597.3)"
     Region          892..1174
                     /region_name="PTKc_Tyk2_rpt2"
                     /note="Catalytic (repeat 2) domain of the Protein Tyrosine
                     Kinase, Tyrosine kinase 2; cd05080"
                     /db_xref="CDD:270664"
     Site            order(903..904,906,911,928,930,960,978..982,984,1023,
                     1027..1028,1030,1040..1041,1060..1064,1073,1121)
                     /site_type="active"
                     /db_xref="CDD:270664"
     Site            order(903..904,906,911,928,930,960,978..982,984,
                     1027..1028,1030,1040..1041)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270664"
     Site            order(1023,1027,1060..1064,1073,1121)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270664"
     Site            1040..1066
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270664"
     Site            1054
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20478313,
                     ECO:0000269|PubMed:8702790; propagated from
                     UniProtKB/Swiss-Prot (P29597.3)"
     Site            1055
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:8702790; propagated from
                     UniProtKB/Swiss-Prot (P29597.3)"
     CDS             1..1187
                     /gene="TYK2"
                     /gene_synonym="IMD35; JTK1"
                     /coded_by="NM_001406461.1:289..3852"
                     /note="isoform 2 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS12236.1"
                     /db_xref="GeneID:7297"
                     /db_xref="HGNC:HGNC:12440"
                     /db_xref="MIM:176941"
ORIGIN      
        1 mplrhwgmar gskpvgdgaq pmaamgglkv llhwagpggg epwvtfsess ltaeevcihi
       61 ahkvgitppc fnlfalfdaq aqvwlppnhi leiprdaslm lyfrirfyfr nwhgmnprep
      121 avyrcgppgt eassdqtaqg mqlldpasfe ylfeqgkhef vndvaslwel steeeihhfk
      181 neslgmaflh lchlalrhgi pleevakkts fkdciprsfr rhirqhsalt rlrlrnvfrr
      241 flrdfqpgrl sqqmvmvkyl atlerlaprf gtervpvchl rllaqaegep cyirdsgvap
      301 tdpgpesaag ppthevlvtg tggiqwwpve eevnkeegss gssgrnpqas lfgkkakahk
      361 avgqpadrpr eplwayfcdf rdithvvlke hcvsihrqdn kclelslpsr aaalsfvslv
      421 dgyfrltads shylchevap prlvmsirdg ihgpllepfv qaklrpedgl ylihwstshp
      481 yrliltvaqr sqapdgmqsl rlrkfpieqq dgafvlegwg rsfpsvrelg aalqgcllra
      541 gddcfslrrc clpqpgetsn liimrgaras prtlnlsqls fhrvdqkeit qlshlgqgtr
      601 tnvyegrlrv egsgdpeegk mddedplvpg rdrgqelrvv lkvldpshhd ialafyetas
      661 lmsqvshthl afvhgvcvrg penimvteyv ehgpldvwlr rerghvpmaw kmvvaqqlas
      721 alsylenknl vhgnvcgrni llarlglaeg tspfiklsdp gvglgalsre erveripwla
      781 peclpggans lstamdkwgf gatlleicfd geaplqsrsp sekehfyqrq hrlpepscpq
      841 latltsqclt yeptqrpsfr tilrdltrlq phnladvltv npdspasdpt vfhkrylkki
      901 rdlgeghfgk vslycydptn dgtgemvavk alkadcgpqh rsgwkqeidi lrtlyhehii
      961 kykgccedqg ekslqlvmey vplgslrdyl prhsiglaql llfaqqiceg maylhaqhyi
     1021 hrdlaarnvl ldndrlvkig dfglakavpe gheyyrvred gdspvfwyap eclkeykfyy
     1081 asdvwsfgvt lyellthcds sqspptkfle ligiaqgqmt vlrlteller gerlprpdkc
     1141 pcevyhlmkn cweteasfrp tfenlipilk tvhekyqgqa psvfsvc
//
LOCUS       NP_001427338             765 aa            linear   PRI 21-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 4 isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_001427338
VERSION     NP_001427338.1
DBSOURCE    REFSEQ: accession NM_001440409.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 765)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   3  (residues 1 to 765)
  AUTHORS   Pu,M., Wang,X. and Zhang,J.
  TITLE     Impact of GRIK4 gene polymorphisms on cognitive dysfunction in
            patients with major depression
  JOURNAL   Rev Neurol (Paris) 176 (10), 823-828 (2020)
   PUBMED   32245654
  REMARK    GeneRIF: Impact of GRIK4 gene polymorphisms on cognitive
            dysfunction in patients with major depression.
REFERENCE   4  (residues 1 to 765)
  AUTHORS   Poweleit,E.A., Aldrich,S.L., Martin,L.J., Hahn,D., Strawn,J.R. and
            Ramsey,L.B.
  TITLE     Pharmacogenetics of Sertraline Tolerability and Response in
            Pediatric Anxiety and Depressive Disorders
  JOURNAL   J Child Adolesc Psychopharmacol 29 (5), 348-361 (2019)
   PUBMED   31066578
  REMARK    GeneRIF: In addition, while GRIK4 was not associated with
            sertraline tolerability and response, both HTR2A and SLC6A4 could
            influence tolerability and accelerate treatment response in
            pediatric patients.
REFERENCE   5  (residues 1 to 765)
  AUTHORS   Koromina,M., Flitton,M., Mellor,I.R. and Knight,H.M.
  TITLE     A kainate receptor GluK4 deletion, protective against bipolar
            disorder, is associated with enhanced cognitive performance across
            diagnoses in the TwinsUK cohort
  JOURNAL   World J Biol Psychiatry 20 (5), 393-401 (2019)
   PUBMED   29243543
  REMARK    GeneRIF: GluK4 deletion carriers who had a mental health problem
            (predominately depression) showed better performance in
            visuo-spatial ability and mental processing speed compared to
            individuals with mental health problems homozygous for the
            insertion.
REFERENCE   6  (residues 1 to 765)
  AUTHORS   Darstein,M., Petralia,R.S., Swanson,G.T., Wenthold,R.J. and
            Heinemann,S.F.
  TITLE     Distribution of kainate receptor subunits at hippocampal mossy
            fiber synapses
  JOURNAL   J Neurosci 23 (22), 8013-8019 (2003)
   PUBMED   12954862
REFERENCE   7  (residues 1 to 765)
  AUTHORS   Ritter,L.M., Unis,A.S. and Meador-Woodruff,J.H.
  TITLE     Ontogeny of ionotropic glutamate receptor expression in human fetal
            brain
  JOURNAL   Brain Res Dev Brain Res 127 (2), 123-133 (2001)
   PUBMED   11334999
REFERENCE   8  (residues 1 to 765)
  AUTHORS   Szpirer,C., Molne,M., Antonacci,R., Jenkins,N.A., Finelli,P.,
            Szpirer,J., Riviere,M., Rocchi,M., Gilbert,D.J., Copeland,N.G. et
            al.
  TITLE     The genes encoding the glutamate receptor subunits KA1 and KA2
            (GRIK4 and GRIK5) are located on separate chromosomes in human,
            mouse, and rat
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 11849-11853 (1994)
   PUBMED   7527545
REFERENCE   9  (residues 1 to 765)
  AUTHORS   Wenthold,R.J., Trumpy,V.A., Zhu,W.S. and Petralia,R.S.
  TITLE     Biochemical and assembly properties of GluR6 and KA2, two members
            of the kainate receptor family, determined with subunit-specific
            antibodies
  JOURNAL   J Biol Chem 269 (2), 1332-1339 (1994)
   PUBMED   8288598
REFERENCE   10 (residues 1 to 765)
  AUTHORS   Kamboj,R.K., Schoepp,D.D., Nutt,S., Shekter,L., Korczak,B.,
            True,R.A., Rampersad,V., Zimmerman,D.M. and Wosnick,M.A.
  TITLE     Molecular cloning, expression, and pharmacological characterization
            of humEAA1, a human kainate receptor subunit
  JOURNAL   J Neurochem 62 (1), 1-9 (1994)
   PUBMED   8263508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002348.3, AP004147.3 and
            AP001929.5.
            
            Summary: This gene encodes a protein that belongs to the
            glutamate-gated ionic channel family. Glutamate functions as the
            major excitatory neurotransmitter in the central nervous system
            through activation of ligand-gated ion channels and G
            protein-coupled membrane receptors. The protein encoded by this
            gene forms functional heteromeric kainate-preferring ionic channels
            with the subunits encoded by related gene family members.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.71070.1,
                                           SRR14372080.1786937.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..765
                     /product="glutamate receptor ionotropic, kainate 4 isoform
                     2 precursor"
                     /note="excitatory amino acid receptor 1; glutamate
                     receptor KA1; glutamate receptor, ionotropic, kainate 4;
                     putative NMDtranscript(altAcc_e11); GluK4(alt_5'UTR)"
                     /calculated_mol_wt=83674
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2064
     Region          24..402
                     /region_name="PBP1_iGluR_Kainate_KA1_2"
                     /note="N-terminal leucine-isoleucine-valine binding
                     protein (LIVBP)-like domain of the KA1 and KA2 subunits of
                     Kainate receptor; cd06394"
                     /db_xref="CDD:380616"
     Site            order(75..77,81,113,166,169,173,176,179..180,190..193)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380616"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            272
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            286
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            323
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            408
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Region          415..763
                     /region_name="Periplasmic_Binding_Protein_Type_2"
                     /note="Type 2 periplasmic binding fold superfamily;
                     cl21456"
                     /db_xref="CDD:473866"
     Site            415
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            479
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     Site            546..566
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16099.2)"
     Site            624..644
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16099.2)"
     Site            736
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16099.2)"
     CDS             1..765
                     /gene="GRIK4"
                     /gene_synonym="EAA1; GluK4; GluK4-2; GRIK; KA1"
                     /coded_by="NM_001440409.1:299..2596"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 11"
                     /db_xref="GeneID:2900"
                     /db_xref="HGNC:HGNC:4582"
                     /db_xref="MIM:600282"
ORIGIN      
        1 mprvsaplvl lpawlvmvac sphslriaai lddpmecsrg erlsitlakn rinraperlg
       61 kakvevdife llrdseyeta etmcqilpkg vvavlgpsss passsiisni cgekevphfk
      121 vapeefvkfq fqrfttlnlh psntdisvav agilnffnct taclicakae cllnlekllr
      181 qfliskdtls vrmlddtrdp tpllkeirdd ktatiiihan asmshtillk aaelgmvsay
      241 ytyiftnlef slqrmdslvd drvnilgfsi fnqshaffqe faqslnqswq encdhvpftg
      301 palssallfd avyavvtavq elnrsqeigv kplscgsaqi wqhgtslmny lrmveleglt
      361 ghiefnskgq rsnyalkilq ftrngfrqig qwhvaeglsm dshlyasnis dtlfnttlvv
      421 ttilenpylm lkgnhqemeg ndryegfcvd mlkelaeilr fnykirlvgd gvygvpeang
      481 twtgmvgeli arkadlavag ltitaerekv idfskpfmtl gisilyrvhm grkpgyfsfl
      541 dpfspgvwlf mllaylavsc vlflvarltp yewysphpca qgrcnllvnq yslgnslwfp
      601 vggfmqqgst iapralstrc vsgvwwaftl iiissytanl aafltvqrmd vpiesvddla
      661 dqtaieygti hggssmtffq nsryqtyqrm wnymyskqps vfvksteegi arvlnsnyaf
      721 llestmneyy rqrncnltqi gglldtkgyg igmpvgmrer nslfg
//
LOCUS       NP_001400613             394 aa            linear   PRI 21-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 17 precursor [Homo sapiens].
ACCESSION   NP_001400613
VERSION     NP_001400613.1
DBSOURCE    REFSEQ: accession NM_001413684.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 394)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 394)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 394)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091559.7, AC010656.7 and
            AC019292.10.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4495075.1,
                                           SRR1803614.90758.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..394
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 17 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=40338
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..342
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            277..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            313..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     CDS             1..394
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_001413684.1:169..1353"
                     /note="isoform 17 precursor is encoded by transcript
                     variant 20"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvsyih gssqaqfvae shiilvlnaa itmgmvllne
      301 aatskgdvgk rriiclvglg lvvfffsfll sifrskyhgy pyrylpnsas ffaasgdtlg
      361 afgnqrkksh tccldfpyan rcrlfhckls qghq
//
LOCUS       NP_001428101             597 aa            linear   PRI 22-NOV-2025
DEFINITION  PHD finger protein 21A isoform h [Homo sapiens].
ACCESSION   NP_001428101 XP_016873396 XP_054225079
VERSION     NP_001428101.1
DBSOURCE    REFSEQ: accession NM_001441172.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Mustafa,S., Abbas,S., Mahmood,A., Khan,A.Z., Zeb,S., Khan,A. and
            Umair,M.
  TITLE     A novel de novo variant in the PHF21A causes craniofacial
            abnormalities, intellectual disability and skeletal manifestations
  JOURNAL   Clin Genet 104 (1), 142-144 (2023)
   PUBMED   36843358
  REMARK    GeneRIF: A novel de novo variant in the PHF21A causes craniofacial
            abnormalities, intellectual disability and skeletal manifestations.
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Huang,J.Q., Ji,L.C., Jing,Q.A., He,Y.C., Ma,Y.Y. and Tong,X.M.
  TITLE     PHF21A expression as a biomarker of hepatocellular carcinoma
            progression and prognosis
  JOURNAL   Neoplasma 69 (6), 1349-1358 (2022)
   PUBMED   36305691
  REMARK    GeneRIF: PHF21A expression as a biomarker of hepatocellular
            carcinoma progression and prognosis.
REFERENCE   4  (residues 1 to 597)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 597)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 597)
  AUTHORS   Hailesellasse Sene,K., Porter,C.J., Palidwor,G., Perez-Iratxeta,C.,
            Muro,E.M., Campbell,P.A., Rudnicki,M.A. and Andrade-Navarro,M.A.
  TITLE     Gene function in early mouse embryonic stem cell differentiation
  JOURNAL   BMC Genomics 8, 85 (2007)
   PUBMED   17394647
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 597)
  AUTHORS   Shi,Y.J., Matson,C., Lan,F., Iwase,S., Baba,T. and Shi,Y.
  TITLE     Regulation of LSD1 histone demethylase activity by its associated
            factors
  JOURNAL   Mol Cell 19 (6), 857-864 (2005)
   PUBMED   16140033
REFERENCE   8  (residues 1 to 597)
  AUTHORS   Iwase,S., Januma,A., Miyamoto,K., Shono,N., Honda,A., Yanagisawa,J.
            and Baba,T.
  TITLE     Characterization of BHC80 in BRAF-HDAC complex, involved in
            neuron-specific gene repression
  JOURNAL   Biochem Biophys Res Commun 322 (2), 601-608 (2004)
   PUBMED   15325272
  REMARK    GeneRIF: Presumably serves as a scaffold protein in BHC in neuronal
            as well as non-neuronal cells. Possible role in spermatogenesis.
REFERENCE   9  (residues 1 to 597)
  AUTHORS   Hakimi,M.A., Dong,Y., Lane,W.S., Speicher,D.W. and Shiekhattar,R.
  TITLE     A candidate X-linked mental retardation gene is a component of a
            new family of histone deacetylase-containing complexes
  JOURNAL   J Biol Chem 278 (9), 7234-7239 (2003)
   PUBMED   12493763
REFERENCE   10 (residues 1 to 597)
  AUTHORS   Hakimi,M.A., Bochar,D.A., Chenoweth,J., Lane,W.S., Mandel,G. and
            Shiekhattar,R.
  TITLE     A core-BRAF35 complex containing histone deacetylase mediates
            repression of neuronal-specific genes
  JOURNAL   Proc Natl Acad Sci U S A 99 (11), 7420-7425 (2002)
   PUBMED   12032298
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC024475.15 and AC068385.9.
            
            On or before Jun 7, 2025 this sequence version replaced
            XP_016873396.1, XP_054225079.1.
            
            Summary: The PHF21A gene encodes BHC80, a component of a BRAF35
            (MIM 605535)/histone deacetylase (HDAC; see MIM 601241) complex
            (BHC) that mediates repression of neuron-specific genes through the
            cis-regulatory element known as repressor element-1 (RE1) or neural
            restrictive silencer (NRS) (Hakimi et al., 2002 [PubMed
            12032298]).[supplied by OMIM, Nov 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.2413331.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..597
                     /product="PHD finger protein 21A isoform h"
                     /note="BRAF35/HDAC2 complex (80 kDa); BHC80a; BRAF35-HDAC
                     complex protein BHC80"
                     /calculated_mol_wt=66291
     Region          <291..453
                     /region_name="TNG2"
                     /note="Chromatin remodeling protein, contains PhD zinc
                     finger [Chromatin structure and dynamics]; COG5034"
                     /db_xref="CDD:227367"
     Region          407..449
                     /region_name="PHD_PHF21A"
                     /note="PHD finger found in PHD finger protein 21A
                     (PHF21A); cd15523"
                     /db_xref="CDD:276998"
     Site            order(407,414..419,439..442,444)
                     /site_type="other"
                     /note="histone H3 binding site [polypeptide binding]"
                     /db_xref="CDD:276998"
     CDS             1..597
                     /gene="PHF21A"
                     /gene_synonym="BHC80; BM-006; IDDBCS; NEDMS"
                     /coded_by="NM_001441172.1:757..2550"
                     /note="isoform h is encoded by transcript variant 18"
                     /db_xref="GeneID:51317"
                     /db_xref="HGNC:HGNC:24156"
                     /db_xref="MIM:608325"
ORIGIN      
        1 melqtlqeal kveiqvhqkl vaqmkqdpqn adlkkqlhel qakitalsek qkrvveqlrk
       61 nlivkqeqpd kfqiqplpqs enklqtaqqq plqqlqqqqq yhhhhaqqsa aaspnltasq
      121 qvqatppqpi kvpqfipppr ltprpnflpq vrpkpvaqnn ipiapapppm laapqliqrp
      181 vmltkftptt lptsqnsihp vrvvngqtat iaktfpmaql tsiviatpgt rlagpqtvql
      241 skpslekqtv kshtetdekq tesrtitppa apkpkreenp qklafmvslg lvthdhleei
      301 qskrqerkrr ttanpvysga vfeperkksa vtylnstmhp gtrkrgrppk ynavlgfgal
      361 tptspqsshp dspenektet tftfpapvqp vslpsptstd gdihedfcsv crksgqllmc
      421 dtcsrvyhld cldpplktip kgmwicprcq dqmlkkeeai pwpgtlaivh syiaykaake
      481 eekqkllkws sdlkqereql eqkvkqlsns iskcmemknt ilarqkemhs slekvkqlir
      541 lihgidlskp vdseatvgai sngpdctppa naatstpaps pssqsctanc nqgeetk
//
LOCUS       NP_001400011             333 aa            linear   PRI 22-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001400011
VERSION     NP_001400011.1
DBSOURCE    REFSEQ: accession NM_001413082.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.4001702.1,
                                           SRR14038194.1603721.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..333
                     /product="mitochondrial fission regulator 1 isoform 1
                     precursor"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=31469
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=5550
     Region          22..251
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     mat_peptide     49..333
                     /product="Mitochondrial fission regulator 1.
                     /id=PRO_0000096622"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=31469
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15390.2)"
     Region          177..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          179..304
                     /region_name="Necessary and sufficient to promote
                     mitochondrial fission. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          288..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     CDS             1..333
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_001413082.1:352..1353"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 17"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsvlwsrkpy gssrsivrki gtnlsliqcp rvqfqinsha
       61 tewspshpge davasfadvg wvakeegecs arlrtevrsr pplqddllff ekapsrqisl
      121 pdlsqeepql ktpalaneea lqkicalene laalraqiak ivtqqeqqnl tagdldsttf
      181 gtipphpppp ppplpppalg lhqstsavdl ikerrekran agktlvknnp kkpempnmle
      241 ilkemnsvkl rsvkrseqdv kpkpvdatdp aaliaealkk kfayryrsds qdevekgipk
      301 seseatserv lfgphmlkpt gkmkalienv sds
//
LOCUS       NP_001837               1712 aa            linear   PRI 23-NOV-2025
DEFINITION  collagen alpha-2(IV) chain preproprotein [Homo sapiens].
ACCESSION   NP_001837
VERSION     NP_001837.2
DBSOURCE    REFSEQ: accession NM_001846.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1712)
  AUTHORS   Wang,H., Zhu,Y., Zheng,L., Chen,M., Hao,Z., Guo,R., Feng,L. and
            Wang,D.
  TITLE     Association of the COL4A2 Gene Polymorphisms with Primary
            Intracerebral Hemorrhage Risk and Outcome in Chinese Han Population
  JOURNAL   Mol Neurobiol 61 (11), 8787-8796 (2024)
   PUBMED   38565785
  REMARK    GeneRIF: Association of the COL4A2 Gene Polymorphisms with Primary
            Intracerebral Hemorrhage Risk and Outcome in Chinese Han
            Population.
REFERENCE   2  (residues 1 to 1712)
  AUTHORS   McNeilly,S., Thomson,C.R., Gonzalez-Trueba,L., Sin,Y.Y.,
            Granata,A., Hamilton,G., Lee,M., Boland,E., McClure,J.D.,
            Lumbreras-Perales,C., Aman,A., Kumar,A.A., Cantini,M., Gok,C.,
            Graham,D., Tomono,Y., Anderson,C.D., Lu,Y., Smith,C., Markus,H.S.,
            Abramowicz,M., Vilain,C., Al-Shahi Salman,R., Salmeron-Sanchez,M.,
            Hainsworth,A.H., Fuller,W., Kadler,K.E., Bulleid,N.J. and Van
            Agtmael,T.
  TITLE     Collagen IV deficiency causes hypertrophic remodeling and
            endothelium-dependent hyperpolarization in small vessel disease
            with intracerebral hemorrhage
  JOURNAL   EBioMedicine 107, 105315 (2024)
   PUBMED   39216230
  REMARK    GeneRIF: Collagen IV deficiency causes hypertrophic remodeling and
            endothelium-dependent hyperpolarization in small vessel disease
            with intracerebral hemorrhage.
REFERENCE   3  (residues 1 to 1712)
  AUTHORS   He,L., Han,W., Yue,K. and Wang,X.
  TITLE     COL4A2 enhances thyroid cancer cell proliferation through the AKT
            pathway
  JOURNAL   Oncol Res 32 (9), 1467-1478 (2024)
   PUBMED   39220121
  REMARK    GeneRIF: COL4A2 enhances thyroid cancer cell proliferation through
            the AKT pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1712)
  AUTHORS   Hu,C., Liu,D. and Wang,H.
  TITLE     Col4a2 Mutations Contribute to Infantile Epileptic Spasm Syndrome
            and Neuroinflammation
  JOURNAL   Int J Med Sci 21 (9), 1756-1768 (2024)
   PUBMED   39006838
  REMARK    GeneRIF: Col4a2 Mutations Contribute to Infantile Epileptic Spasm
            Syndrome and Neuroinflammation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1712)
  AUTHORS   Oh,J.K., Levi,S.R., de Carvalho,J.R.L. Jr., Abdelhakim,A.H.,
            Hirano,M., Maumenee,I.H. and Tsang,S.H.
  TITLE     Venous Tortuosity in COL4A2-Associated Gould Syndrome
  JOURNAL   Ophthalmic Surg Lasers Imaging Retina 54 (9), 536-539 (2023)
   PUBMED   37642429
  REMARK    GeneRIF: Venous Tortuosity in COL4A2-Associated Gould Syndrome.
REFERENCE   6  (residues 1 to 1712)
  AUTHORS   Ghebrehiwet,B., Peerschke,E.I., Hong,Y., Munoz,P. and Gorevic,P.D.
  TITLE     Short amino acid sequences derived from C1q receptor (C1q-R) show
            homology with the alpha chains of fibronectin and vitronectin
            receptors and collagen type IV
  JOURNAL   J Leukoc Biol 51 (6), 546-556 (1992)
   PUBMED   1377218
REFERENCE   7  (residues 1 to 1712)
  AUTHORS   Gupta,S., Batchu,R.B. and Datta,K.
  TITLE     Purification, partial characterization of rat kidney hyaluronic
            acid binding protein and its localization on the cell surface
  JOURNAL   Eur J Cell Biol 56 (1), 58-67 (1991)
   PUBMED   1724753
REFERENCE   8  (residues 1 to 1712)
  AUTHORS   Paralkar,V.M., Nandedkar,A.K., Pointer,R.H., Kleinman,H.K. and
            Reddi,A.H.
  TITLE     Interaction of osteogenin, a heparin binding bone morphogenetic
            protein, with type IV collagen
  JOURNAL   J Biol Chem 265 (28), 17281-17284 (1990)
   PUBMED   2211625
REFERENCE   9  (residues 1 to 1712)
  AUTHORS   Myers,J.C., Howard,P.S., Jelen,A.M., Dion,A.S. and Macarak,E.J.
  TITLE     Duplication of type IV collagen COOH-terminal repeats and
            species-specific expression of alpha 1(IV) and alpha 2(IV) collagen
            genes
  JOURNAL   J Biol Chem 262 (19), 9231-9238 (1987)
   PUBMED   2439508
  REMARK    Erratum:[J Biol Chem 1987 Oct 15;262(29):14372]
REFERENCE   10 (residues 1 to 1712)
  AUTHORS   Hernandez,M.R., Igoe,F. and Neufeld,A.H.
  TITLE     Extracellular matrix of the human optic nerve head
  JOURNAL   Am J Ophthalmol 102 (2), 139-148 (1986)
   PUBMED   2426947
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL161773.21, AL159153.17 and
            AL139385.12.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 17, 2006 this sequence version replaced NP_001837.1.
            
            Summary: This gene encodes one of the six subunits of type IV
            collagen, the major structural component of basement membranes. The
            C-terminal portion of the protein, known as canstatin, is an
            inhibitor of angiogenesis and tumor growth. Like the other members
            of the type IV collagen gene family, this gene is organized in a
            head-to-head conformation with another type IV collagen gene so
            that each gene pair shares a common promoter. [provided by RefSeq,
            Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360467.7/ ENSP00000353654.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1712
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..1712
                     /product="collagen alpha-2(IV) chain preproprotein"
                     /note="canstatin; collagen alpha-2(IV) chain"
                     /calculated_mol_wt=164048
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3524
     Region          <58..>346
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          60..237
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08572.4)"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:3198637; propagated from
                     UniProtKB/Swiss-Prot (P08572.4)"
     mat_peptide     184..1712
                     /product="Collagen alpha-2(IV) chain. /id=PRO_0000005825"
                     /note="propagated from UniProtKB/Swiss-Prot (P08572.4)"
                     /calculated_mol_wt=149188
     Region          184..1484
                     /region_name="Triple-helical region"
                     /note="propagated from UniProtKB/Swiss-Prot (P08572.4)"
     Region          302..448
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08572.4)"
     Region          <309..>581
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          507..640
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08572.4)"
     Region          690..906
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08572.4)"
     Region          <728..>965
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <990..>1212
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          1157..1480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08572.4)"
     Region          <1245..>1476
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     mat_peptide     1486..1712
                     /product="Canstatin. /id=PRO_0000283775"
                     /note="propagated from UniProtKB/Swiss-Prot (P08572.4)"
                     /calculated_mol_wt=25005
     Region          1490..1595
                     /region_name="C4"
                     /note="C-terminal tandem repeated domain in type 4
                     procollagen; pfam01413"
                     /db_xref="CDD:460201"
     Region          1598..1710
                     /region_name="C4"
                     /note="C-terminal tandem repeated domain in type 4
                     procollagen; pfam01413"
                     /db_xref="CDD:460201"
     CDS             1..1712
                     /gene="COL4A2"
                     /gene_synonym="BSVD2; BSVD2A; BSVD2B; ICH; POREN2"
                     /coded_by="NM_001846.4:290..5428"
                     /db_xref="CCDS:CCDS41907.1"
                     /db_xref="GeneID:1284"
                     /db_xref="HGNC:HGNC:2203"
                     /db_xref="MIM:120090"
ORIGIN      
        1 mgrdqravag palrrwlllg tvtvgflaqs vlagvkkfdv pcggrdcsgg cqcypekggr
       61 gqpgpvgpqg yngppglqgf pglqgrkgdk gergapgvtg pkgdvgargv sgfpgadgip
      121 ghpgqggprg rpgydgcngt qgdsgpqgpp gsegftgppg pqgpkgqkge pyalpkeerd
      181 ryrgepgepg lvgfqgppgr pghvgqmgpv gapgrpgppg ppgpkgqqgn rglgfygvkg
      241 ekgdvgqpgp ngipsdtlhp iiaptgvtfh pdqykgekgs egepgirgis lkgeegimgf
      301 pglrgypgls gekgspgqkg srgldgyqgp dgprgpkgea gdpgppglpa ysphpslakg
      361 argdpgfpga qgepgsqgep gdpglpgppg lsigdgdqrr glpgemgpkg figdpgipal
      421 yggppgpdgk rgppgppglp gppgpdgflf glkgakgrag fpglpgspga rgpkgwkgda
      481 gecrctegde aikglpglpg pkgfaginge pgrkgdrgdp gqhglpgfpg lkgvpgniga
      541 pgpkgakgds rtittkgerg qpgvpgvpgm kgddgspgrd gldgfpglpg ppgdgikgpp
      601 gdpgypgipg tkgtpgemgp pglglpglkg qrgfpgdagl pgppgflgpp gpagtpgqid
      661 cdtdvkravg gdrqeaiqpg ciggpkglpg lpgppgptga kglrgipgfa gadggpgprg
      721 lpgdagregf pgppgfigpr gskgavglpg pdgspgpigl pgpdgppger glpgevlgaq
      781 pgprgdagvp gqpglkglpg drgppgfrgs qgmpgmpglk gqpglpgpsg qpglygppgl
      841 hgfpgapgqe gplglpgipg reglpgdrgd pgdtgapgpv gmkglsgdrg dagftgeqgh
      901 pgspgfkgid gmpgtpglkg drgspgmdgf qgmpglkgrp gfpgskgeag ffgipglkgl
      961 agepgfkgsr gdpgppgppp vilpgmkdik gekgdegpmg lkgylgakgi qgmpgipgls
     1021 gipglpgrpg hikgvkgdig vpgipglpgf pgvagppgit gfpgfigsrg dkgapgragl
     1081 ygeigatgdf gdigdtinlp grpglkgerg ttgipglkgf fgekgtegdi gfpgitgvtg
     1141 vqgppglkgq tgfpgltgpp gsqgelgrig lpggkgddgw pgapglpgfp glrgirglhg
     1201 lpgtkgfpgs pgsdihgdpg fpgppgergd pgeantlpgp vgvpgqkgdq gapgergppg
     1261 spglqgfpgi tppsnisgap gdkgapgifg lkgyrgppgp pgsaalpgsk gdtgnpgapg
     1321 tpgtkgwagd sgpqgrpgvf glpgekgprg eqgfmgntgp tgavgdrgpk gpkgdpgfpg
     1381 apgtvgapgi agipqkiavq pgtvgpqgrr gppgapgemg pqgppgepgf rgapgkagpq
     1441 grggvsavpg frgdegpigh qgpigqegap grpgspglpg mpgrsvsigy llvkhsqtdq
     1501 epmcpvgmnk lwsgysllyf egqekahnqd lglagsclar fstmpflycn pgdvcyyasr
     1561 ndksywlstt aplpmmpvae deikpyisrc svceapaiai avhsqdvsip hcpagwrslw
     1621 igysflmhta agdegggqsl vspgscledf ratpfiecng grgtchyyan kysfwlttip
     1681 eqsfqgspsa dtlkaglirt hisrcqvcmk nl
//
LOCUS       NP_002087                517 aa            linear   PRI 24-NOV-2025
DEFINITION  general transcription factor IIF subunit 1 [Homo sapiens].
ACCESSION   NP_002087
VERSION     NP_002087.2
DBSOURCE    REFSEQ: accession NM_002096.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Hamilton,K., Morrow,K., Markantoni,E. and Harvey,J.
  TITLE     Leptin prevents aberrant targeting of tau to hippocampal synapses
            via PI 3 kinase driven inhibition of GSK3beta
  JOURNAL   J Neurochem 167 (4), 520-537 (2023)
   PUBMED   37822142
  REMARK    GeneRIF: Leptin prevents aberrant targeting of tau to hippocampal
            synapses via PI 3 kinase driven inhibition of GSK3beta.
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Choi,S.G., Olivet,J., Cassonnet,P., Vidalain,P.O., Luck,K.,
            Lambourne,L., Spirohn,K., Lemmens,I., Dos Santos,M., Demeret,C.,
            Jones,L., Rangarajan,S., Bian,W., Coutant,E.P., Janin,Y.L., van der
            Werf,S., Trepte,P., Wanker,E.E., De Las Rivas,J., Tavernier,J.,
            Twizere,J.C., Hao,T., Hill,D.E., Vidal,M., Calderwood,M.A. and
            Jacob,Y.
  TITLE     Maximizing binary interactome mapping with a minimal number of
            assays
  JOURNAL   Nat Commun 10 (1), 3907 (2019)
   PUBMED   31467278
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 517)
  AUTHORS   De Mol,E., Szulc,E., Di Sanza,C., Martinez-Cristobal,P.,
            Bertoncini,C.W., Fenwick,R.B., Frigole-Vivas,M., Masin,M.,
            Hunter,I., Buzon,V., Brun-Heath,I., Garcia,J., De Fabritiis,G.,
            Estebanez-Perpina,E., McEwan,I.J., Nebreda,A.R. and Salvatella,X.
  TITLE     Regulation of Androgen Receptor Activity by Transient Interactions
            of Its Transactivation Domain with General Transcription Regulators
  JOURNAL   Structure 26 (1), 145-152 (2018)
   PUBMED   29225078
  REMARK    GeneRIF: An AR motif of the transactivation domain has been
            identified that contributes to transcriptional activity by
            recruiting the C-terminal domain of subunit 1 of the general
            transcription regulator TFIIF.
REFERENCE   5  (residues 1 to 517)
  AUTHORS   He,Y., Yan,C., Fang,J., Inouye,C., Tjian,R., Ivanov,I. and
            Nogales,E.
  TITLE     Near-atomic resolution visualization of human transcription
            promoter opening
  JOURNAL   Nature 533 (7603), 359-365 (2016)
   PUBMED   27193682
REFERENCE   6  (residues 1 to 517)
  AUTHORS   Kato,H., Sumimoto,H., Pognonec,P., Chen,C.H., Rosen,C.A. and
            Roeder,R.G.
  TITLE     HIV-1 Tat acts as a processivity factor in vitro in conjunction
            with cellular elongation factors
  JOURNAL   Genes Dev 6 (4), 655-666 (1992)
   PUBMED   1559613
REFERENCE   7  (residues 1 to 517)
  AUTHORS   Finkelstein,A., Kostrub,C.F., Li,J., Chavez,D.P., Wang,B.Q.,
            Fang,S.M., Greenblatt,J. and Burton,Z.F.
  TITLE     A cDNA encoding RAP74, a general initiation factor for
            transcription by RNA polymerase II
  JOURNAL   Nature 355 (6359), 464-467 (1992)
   PUBMED   1734284
REFERENCE   8  (residues 1 to 517)
  AUTHORS   Aso,T., Vasavada,H.A., Kawaguchi,T., Germino,F.J., Ganguly,S.,
            Kitajima,S., Weissman,S.M. and Yasukochi,Y.
  TITLE     Characterization of cDNA for the large subunit of the transcription
            initiation factor TFIIF
  JOURNAL   Nature 355 (6359), 461-464 (1992)
   PUBMED   1734283
REFERENCE   9  (residues 1 to 517)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   10 (residues 1 to 517)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            X64037.1, BC013007.2 and X64002.1.
            
            On Aug 17, 2007 this sequence version replaced NP_002087.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X64002.1, X64037.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394456.10/ ENSP00000377969.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..517
                     /product="general transcription factor IIF subunit 1"
                     /note="transcription initiation factor RAP74; general
                     transcription factor IIF 74 kDa subunit; transcription
                     initiation factor IIF subunit alpha; general transcription
                     factor IIF, polypeptide 1, 74kDa"
                     /calculated_mol_wt=58110
     Region          2..517
                     /region_name="TFIIF_alpha"
                     /note="Transcription initiation factor IIF, alpha subunit
                     (TFIIF-alpha); pfam05793"
                     /db_xref="CDD:310411"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P35269.2)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35269.2)"
     Region          178..466
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35269.2)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35269.2)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P35269.2)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P35269.2)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P35269.2)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35269.2)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35269.2)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35269.2)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35269.2)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10428810,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P35269.2)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:10428810,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35269.2)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35269.2)"
     Site            407
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P35269.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35269.2)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35269.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35269.2)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35269.2)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35269.2)"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35269.2)"
     CDS             1..517
                     /gene="GTF2F1"
                     /gene_synonym="BTF4; RAP74; TF2F1; TFIIF; TFIIF-alpha"
                     /coded_by="NM_002096.3:170..1723"
                     /db_xref="CCDS:CCDS12165.1"
                     /db_xref="GeneID:2962"
                     /db_xref="HGNC:HGNC:4652"
                     /db_xref="MIM:189968"
ORIGIN      
        1 maalgpssqn vteyvvrvpk nttkkynima fnaadkvnfa twnqarlerd lsnkkiyqee
       61 empesgagse fnrklreear rkkygivlke frpedqpwll rvngksgrkf kgikkggvte
      121 ntsyyiftqc pdgafeafpv hnwynftpla rhrtltaeea eeewerrnkv lnhfsimqqr
      181 rlkdqdqded eeekekrgrr kaselrihdl eddlemssda sdasgeeggr vpkakkkapl
      241 akggrkkkkk kgsddeafed sddgdfegqe vdymsdgsss sqeepeskak apqqeegpkg
      301 vdeqsdssee seeekppeed keeeeekkap tpqekkrrkd sseesdssee sdidseassa
      361 lfmakkktpp krerkpsggs srgnsrpgtp saeggstsst lraaaskleq gkrvsempaa
      421 krlrldtgpq slsgkstpqp psgkttpnsg dvqvtedavr ryltrkpmtt kdllkkfqtk
      481 ktglsseqtv nvlaqilkrl nperkmindk mhfslke
//
LOCUS       NP_004949               2549 aa            linear   PRI 24-NOV-2025
DEFINITION  serine/threonine-protein kinase mTOR isoform 1 [Homo sapiens].
ACCESSION   NP_004949
VERSION     NP_004949.1
DBSOURCE    REFSEQ: accession NM_004958.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2549)
  AUTHORS   Azimzadeh,M., Cheah,P.S. and Ling,K.H.
  TITLE     Brain insulin resistance in Down syndrome: Involvement of
            PI3K-Akt/mTOR axis in early-onset of Alzheimer's disease and its
            potential as a therapeutic target
  JOURNAL   Biochem Biophys Res Commun 733, 150713 (2024)
   PUBMED   39307112
  REMARK    GeneRIF: Brain insulin resistance in Down syndrome: Involvement of
            PI3K-Akt/mTOR axis in early-onset of Alzheimer's disease and its
            potential as a therapeutic target.
            Review article
REFERENCE   2  (residues 1 to 2549)
  AUTHORS   Xue,Z., Liu,J., Xing,W., Mu,F., Wu,Y., Zhao,J., Liu,X., Wang,D.,
            Wang,J., Li,X., Wang,J. and Huang,B.
  TITLE     Hypoxic glioma-derived exosomal miR-25-3p promotes macrophage M2
            polarization by activating the PI3K-AKT-mTOR signaling pathway
  JOURNAL   J Nanobiotechnology 22 (1), 628 (2024)
   PUBMED   39407269
  REMARK    GeneRIF: Hypoxic glioma-derived exosomal miR-25-3p promotes
            macrophage M2 polarization by activating the PI3K-AKT-mTOR
            signaling pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2549)
  AUTHORS   Witucki,L. and Jakubowski,H.
  TITLE     Homocysteine metabolites impair the PHF8/H4K20me1/mTOR/autophagy
            pathway by upregulating the expression of histone demethylase
            PHF8-targeting microRNAs in human vascular endothelial cells and
            mice
  JOURNAL   FASEB J 38 (18), e70072 (2024)
   PUBMED   39323294
  REMARK    GeneRIF: Homocysteine metabolites impair the
            PHF8/H4K20me1/mTOR/autophagy pathway by upregulating the expression
            of histone demethylase PHF8-targeting microRNAs in human vascular
            endothelial cells and mice.
REFERENCE   4  (residues 1 to 2549)
  AUTHORS   Zhan,J., Harwood,F., Have,S.T., Lamond,A., Phillips,A.H.,
            Kriwacki,R.W., Halder,P., Cardone,M. and Grosveld,G.C.
  TITLE     Assembly of mTORC3 Involves Binding of ETV7 to Two Separate
            Sequences in the mTOR Kinase Domain
  JOURNAL   Int J Mol Sci 25 (18), 10042 (2024)
   PUBMED   39337528
  REMARK    GeneRIF: Assembly of mTORC3 Involves Binding of ETV7 to Two
            Separate Sequences in the mTOR Kinase Domain.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2549)
  AUTHORS   Gordon,D.E., Jang,G.M., Bouhaddou,M., Xu,J., Obernier,K.,
            White,K.M., O'Meara,M.J., Rezelj,V.V., Guo,J.Z., Swaney,D.L.,
            Tummino,T.A., Huttenhain,R., Kaake,R.M., Richards,A.L.,
            Tutuncuoglu,B., Foussard,H., Batra,J., Haas,K., Modak,M., Kim,M.,
            Haas,P., Polacco,B.J., Braberg,H., Fabius,J.M., Eckhardt,M.,
            Soucheray,M., Bennett,M.J., Cakir,M., McGregor,M.J., Li,Q.,
            Meyer,B., Roesch,F., Vallet,T., Mac Kain,A., Miorin,L., Moreno,E.,
            Naing,Z.Z.C., Zhou,Y., Peng,S., Shi,Y., Zhang,Z., Shen,W.,
            Kirby,I.T., Melnyk,J.E., Chorba,J.S., Lou,K., Dai,S.A.,
            Barrio-Hernandez,I., Memon,D., Hernandez-Armenta,C., Lyu,J.,
            Mathy,C.J.P., Perica,T., Pilla,K.B., Ganesan,S.J., Saltzberg,D.J.,
            Rakesh,R., Liu,X., Rosenthal,S.B., Calviello,L., Venkataramanan,S.,
            Liboy-Lugo,J., Lin,Y., Huang,X.P., Liu,Y., Wankowicz,S.A., Bohn,M.,
            Safari,M., Ugur,F.S., Koh,C., Savar,N.S., Tran,Q.D., Shengjuler,D.,
            Fletcher,S.J., O'Neal,M.C., Cai,Y., Chang,J.C.J., Broadhurst,D.J.,
            Klippsten,S., Sharp,P.P., Wenzell,N.A., Kuzuoglu-Ozturk,D.,
            Wang,H.Y., Trenker,R., Young,J.M., Cavero,D.A., Hiatt,J.,
            Roth,T.L., Rathore,U., Subramanian,A., Noack,J., Hubert,M.,
            Stroud,R.M., Frankel,A.D., Rosenberg,O.S., Verba,K.A., Agard,D.A.,
            Ott,M., Emerman,M., Jura,N., von Zastrow,M., Verdin,E.,
            Ashworth,A., Schwartz,O., d'Enfert,C., Mukherjee,S., Jacobson,M.,
            Malik,H.S., Fujimori,D.G., Ideker,T., Craik,C.S., Floor,S.N.,
            Fraser,J.S., Gross,J.D., Sali,A., Roth,B.L., Ruggero,D.,
            Taunton,J., Kortemme,T., Beltrao,P., Vignuzzi,M., Garcia-Sastre,A.,
            Shokat,K.M., Shoichet,B.K. and Krogan,N.J.
  TITLE     A SARS-CoV-2 protein interaction map reveals targets for drug
            repurposing
  JOURNAL   Nature 583 (7816), 459-468 (2020)
   PUBMED   32353859
REFERENCE   6  (residues 1 to 2549)
  AUTHORS   Zhou,Y., Hou,Y., Shen,J., Huang,Y., Martin,W. and Cheng,F.
  TITLE     Network-based drug repurposing for novel coronavirus
            2019-nCoV/SARS-CoV-2
  JOURNAL   Cell Discov 6, 14 (2020)
   PUBMED   32194980
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 2549)
  AUTHORS   Chen,J., Zheng,X.F., Brown,E.J. and Schreiber,S.L.
  TITLE     Identification of an 11-kDa FKBP12-rapamycin-binding domain within
            the 289-kDa FKBP12-rapamycin-associated protein and
            characterization of a critical serine residue
  JOURNAL   Proc Natl Acad Sci U S A 92 (11), 4947-4951 (1995)
   PUBMED   7539137
REFERENCE   8  (residues 1 to 2549)
  AUTHORS   Chiu,M.I., Katz,H. and Berlin,V.
  TITLE     RAPT1, a mammalian homolog of yeast Tor, interacts with the
            FKBP12/rapamycin complex
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 12574-12578 (1994)
   PUBMED   7809080
REFERENCE   9  (residues 1 to 2549)
  AUTHORS   Prada,C.E., Raski,C.R., Mirzaa,G., Besterman,A., Krueger,D.A. and
            Liu,A.C.
  TITLE     Smith-Kingsmore Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41264764
REFERENCE   10 (residues 1 to 2549)
  AUTHORS   Grove,J.R., Banerjee,P., Balasubramanyam,A., Coffer,P.J.,
            Price,D.J., Avruch,J. and Woodgett,J.R.
  TITLE     Cloning and expression of two human p70 S6 kinase polypeptides
            differing only at their amino termini
  JOURNAL   Mol Cell Biol 11 (11), 5541-5550 (1991)
   PUBMED   1922062
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP250183.1, DC403129.1,
            L34075.1, U88966.1, BC117166.1, AB209995.1 and AA725390.1.
            
            Summary: The protein encoded by this gene belongs to a family of
            phosphatidylinositol kinase-related kinases. These kinases mediate
            cellular responses to stresses such as DNA damage and nutrient
            deprivation. This kinase is a component of two distinct complexes,
            mTORC1, which controls protein synthesis, cell growth and
            proliferation, and mTORC2, which is a regulator of the actin
            cytoskeleton, and promotes cell survival and cell cycle
            progression. This protein acts as the target for the cell-cycle
            arrest and immunosuppressive effects of the FKBP12-rapamycin
            complex. Inhibitors of mTOR are used in organ transplants as
            immunosuppressants, and are being evaluated for their therapeutic
            potential in SARS-CoV-2 infections. Mutations in this gene are
            associated with Smith-Kingsmore syndrome and somatic focal cortical
            dysplasia type II. The ANGPTL7 gene is located in an intron of this
            gene. [provided by RefSeq, Aug 2020].
            
            Transcript Variant: Variants 1 and 2 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U88966.1, SRR18074967.3489518.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: relevant for COVID-19 treatment
            MANE Ensembl match     :: ENST00000361445.9/ ENSP00000354558.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..2549
                     /product="serine/threonine-protein kinase mTOR isoform 1"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="mammalian target of rapamycin; FK506 binding
                     protein 12-rapamycin associated protein 2; rapamycin and
                     FKBP12 target 1; mechanistic target of rapamycin
                     (serine/threonine kinase); serine/threonine-protein kinase
                     mTOR; FKBP12-rapamycin complex-associated protein 1;
                     FKBP-rapamycin associated protein; rapamycin associated
                     protein FRAP2; rapamycin target protein 1;
                     tyrosine-protein kinase mTOR; FK506-binding protein
                     12-rapamycin complex-associated protein 1"
                     /calculated_mol_wt=288762
     Region          1..651
                     /region_name="Interaction with NBN.
                     /evidence=ECO:0000269|PubMed:23762398"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Region          363..2549
                     /region_name="TEL1"
                     /note="Phosphatidylinositol kinase or protein kinase, PI-3
                     family [Signal transduction mechanisms]; COG5032"
                     /db_xref="CDD:227365"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          637..683
                     /region_name="HEAT 16"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          655..681
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          686..724
                     /region_name="HEAT 17"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          691..721
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          727..766
                     /region_name="HEAT 18"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          729..759
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          769..811
                     /region_name="HEAT 19"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          772..805
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          814..853
                     /region_name="HEAT 20"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          817..847
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          857..893
                     /region_name="HEAT 21"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          894..942
                     /region_name="HEAT 22"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          943..988
                     /region_name="HEAT 23"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          955..981
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(969..970,973,980..981,1010..1011,1014,1017..1018,
                     1021,1050..1051,1054,1057..1058,1061,1091..1092,1095,
                     1098..1099,1133..1134,1137,1140..1141)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          989..1027
                     /region_name="HEAT 24"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          993..1021
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1029..1068
                     /region_name="HEAT 25"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1033..1062
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1069..1105
                     /region_name="HEAT 26"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1073..1099
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1106..1144
                     /region_name="HEAT 27"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1111..1142
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1145..1188
                     /region_name="HEAT 28"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1154..1180
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Region          1189..1225
                     /region_name="HEAT 29"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Site            1218
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Region          1226..1273
                     /region_name="HEAT 30"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Site            1261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19487463,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Region          1274..1311
                     /region_name="HEAT 31"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1312..1345
                     /region_name="HEAT 32"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1346..1382
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1383..1408
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1409..1442
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1443..1473
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1474..1507
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1508..1541
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1542..1574
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1575..1614
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1615..1649
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1650..1693
                     /region_name="TPR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1694..1731
                     /region_name="TPR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1732..1786
                     /region_name="TPR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1787..1846
                     /region_name="TPR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1812..1867
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1898..1930
                     /region_name="TPR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1931..1970
                     /region_name="TPR 15"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1971..2005
                     /region_name="TPR 16"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          2012..2144
                     /region_name="Sufficient for interaction with the
                     FKBP1A/rapamycin complex.
                     /evidence=ECO:0000250|UniProtKB:Q9JLN9"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          2025..2114
                     /region_name="FKBP12-rapamycin binding domain"
     Site            2159
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TBK1.
                     /evidence=ECO:0000269|PubMed:21576368,
                     ECO:0000269|PubMed:29150432; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Region          2162..2168
                     /region_name="G-loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Site            2164
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:21576368; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Site            2173
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:24247430; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Region          2258..2296
                     /region_name="Interaction with MLST8"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          2335..2343
                     /region_name="Catalytic loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          2355..2380
                     /region_name="Activation loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Site            2446
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by RPS6KB1.
                     /evidence=ECO:0000269|PubMed:15905173; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Site            2448
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KB1.
                     /evidence=ECO:0000269|PubMed:15899889,
                     ECO:0000269|PubMed:15905173, ECO:0000269|PubMed:19145465,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Site            2478
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Site            2481
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20022946,
                     ECO:0000269|PubMed:21576368, ECO:0007744|PubMed:18669648;
                     propagated from UniProtKB/Swiss-Prot (P42345.1)"
     CDS             1..2549
                     /gene="MTOR"
                     /gene_synonym="FRAP; FRAP1; FRAP2; RAFT1; RAPT1; SKS"
                     /coded_by="NM_004958.4:122..7771"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS127.1"
                     /db_xref="GeneID:2475"
                     /db_xref="HGNC:HGNC:3942"
                     /db_xref="MIM:601231"
ORIGIN      
        1 mlgtgpaaat taattssnvs vlqqfasglk srneetraka akelqhyvtm elremsqees
       61 trfydqlnhh ifelvsssda nerkggilai asligveggn atrigrfany lrnllpsndp
      121 vvmemaskai grlamagdtf taeyvefevk ralewlgadr negrrhaavl vlrelaisvp
      181 tfffqqvqpf fdnifvavwd pkqairegav aalraclilt tqrepkemqk pqwyrhtfee
      241 aekgfdetla kekgmnrddr ihgallilne lvrissmege rlreemeeit qqqlvhdkyc
      301 kdlmgfgtkp rhitpftsfq avqpqqsnal vgllgysshq glmgfgtsps pakstlvesr
      361 ccrdlmeekf dqvcqwvlkc rnsknsliqm tilnllprla afrpsaftdt qylqdtmnhv
      421 lscvkkeker taafqalgll svavrsefkv ylprvldiir aalppkdfah krqkamqvda
      481 tvftcismla ramgpgiqqd ikellepmla vglspaltav lydlsrqipq lkkdiqdgll
      541 kmlslvlmhk plrhpgmpkg lahqlaspgl ttlpeasdvg sitlalrtlg sfefeghslt
      601 qfvrhcadhf lnsehkeirm eaartcsrll tpsihlisgh ahvvsqtavq vvadvlskll
      661 vvgitdpdpd irycvlasld erfdahlaqa enlqalfval ndqvfeirel aictvgrlss
      721 mnpafvmpfl rkmliqilte lehsgigrik eqsarmlghl vsnaprlirp ymepilkali
      781 lklkdpdpdp npgvinnvla tigelaqvsg lemrkwvdel fiiimdmlqd ssllakrqva
      841 lwtlgqlvas tgyvvepyrk yptllevlln flkteqnqgt rreairvlgl lgaldpykhk
      901 vnigmidqsr dasavslses kssqdssdys tsemlvnmgn lpldefypav smvalmrifr
      961 dqslshhhtm vvqaitfifk slglkcvqfl pqvmptflnv irvcdgaire flfqqlgmlv
     1021 sfvkshirpy mdeivtlmre fwvmntsiqs tiillieqiv valggefkly lpqliphmlr
     1081 vfmhdnspgr ivsikllaai qlfganlddy lhlllppivk lfdapeaplp srkaaletvd
     1141 rltesldftd yasriihpiv rtldqspelr stamdtlssl vfqlgkkyqi fipmvnkvlv
     1201 rhrinhqryd vlicrivkgy tladeeedpl iyqhrmlrsg qgdalasgpv etgpmkklhv
     1261 stinlqkawg aarrvskddw lewlrrlsle llkdssspsl rscwalaqay npmardlfna
     1321 afvscwseln edqqdelirs ielaltsqdi aevtqtllnl aefmehsdkg plplrddngi
     1381 vllgeraakc rayakalhyk elefqkgptp aileslisin nklqqpeaaa gvleyamkhf
     1441 geleiqatwy eklhewedal vaydkkmdtn kddpelmlgr mrclealgew gqlhqqccek
     1501 wtlvndetqa kmarmaaaaa wglgqwdsme eytcmiprdt hdgafyravl alhqdlfsla
     1561 qqcidkardl ldaeltamag esysraygam vschmlsele eviqyklvpe rreiirqiww
     1621 erlqgcqriv edwqkilmvr slvvsphedm rtwlkyaslc gksgrlalah ktlvlllgvd
     1681 psrqldhplp tvhpqvtyay mknmwksark idafqhmqhf vqtmqqqaqh aiatedqqhk
     1741 qelhklmarc flklgewqln lqginestip kvlqyysaat ehdrswykaw hawavmnfea
     1801 vlhykhqnqa rdekkklrha sganitnatt aattaatatt tastegsnse seaestensp
     1861 tpsplqkkvt edlsktllmy tvpavqgffr sislsrgnnl qdtlrvltlw fdyghwpdvn
     1921 ealvegvkai qidtwlqvip qliaridtpr plvgrlihql ltdigryhpq aliypltvas
     1981 kstttarhna ankilknmce hsntlvqqam mvseelirva ilwhemwheg leeasrlyfg
     2041 ernvkgmfev leplhammer gpqtlketsf nqaygrdlme aqewcrkymk sgnvkdltqa
     2101 wdlyyhvfrr iskqlpqlts lelqyvspkl lmcrdlelav pgtydpnqpi iriqsiapsl
     2161 qvitskqrpr kltlmgsngh efvfllkghe dlrqdervmq lfglvntlla ndptslrknl
     2221 siqryavipl stnsgligwv phcdtlhali rdyrekkkil lniehrimlr mapdydhltl
     2281 mqkvevfeha vnntagddla kllwlkspss evwfdrrtny trslavmsmv gyilglgdrh
     2341 psnlmldrls gkilhidfgd cfevamtrek fpekipfrlt rmltnamevt gldgnyritc
     2401 htvmevlreh kdsvmavlea fvydpllnwr lmdtntkgnk rsrtrtdsys agqsveildg
     2461 velgepahkk tgttvpesih sfigdglvkp ealnkkaiqi inrvrdkltg rdfshddtld
     2521 vptqvellik qatshenlcq cyigwcpfw
//
LOCUS       NP_001373429            2549 aa            linear   PRI 24-NOV-2025
DEFINITION  serine/threonine-protein kinase mTOR isoform 1 [Homo sapiens].
ACCESSION   NP_001373429 XP_005263495
VERSION     NP_001373429.1
DBSOURCE    REFSEQ: accession NM_001386500.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2549)
  AUTHORS   Azimzadeh,M., Cheah,P.S. and Ling,K.H.
  TITLE     Brain insulin resistance in Down syndrome: Involvement of
            PI3K-Akt/mTOR axis in early-onset of Alzheimer's disease and its
            potential as a therapeutic target
  JOURNAL   Biochem Biophys Res Commun 733, 150713 (2024)
   PUBMED   39307112
  REMARK    GeneRIF: Brain insulin resistance in Down syndrome: Involvement of
            PI3K-Akt/mTOR axis in early-onset of Alzheimer's disease and its
            potential as a therapeutic target.
            Review article
REFERENCE   2  (residues 1 to 2549)
  AUTHORS   Xue,Z., Liu,J., Xing,W., Mu,F., Wu,Y., Zhao,J., Liu,X., Wang,D.,
            Wang,J., Li,X., Wang,J. and Huang,B.
  TITLE     Hypoxic glioma-derived exosomal miR-25-3p promotes macrophage M2
            polarization by activating the PI3K-AKT-mTOR signaling pathway
  JOURNAL   J Nanobiotechnology 22 (1), 628 (2024)
   PUBMED   39407269
  REMARK    GeneRIF: Hypoxic glioma-derived exosomal miR-25-3p promotes
            macrophage M2 polarization by activating the PI3K-AKT-mTOR
            signaling pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2549)
  AUTHORS   Witucki,L. and Jakubowski,H.
  TITLE     Homocysteine metabolites impair the PHF8/H4K20me1/mTOR/autophagy
            pathway by upregulating the expression of histone demethylase
            PHF8-targeting microRNAs in human vascular endothelial cells and
            mice
  JOURNAL   FASEB J 38 (18), e70072 (2024)
   PUBMED   39323294
  REMARK    GeneRIF: Homocysteine metabolites impair the
            PHF8/H4K20me1/mTOR/autophagy pathway by upregulating the expression
            of histone demethylase PHF8-targeting microRNAs in human vascular
            endothelial cells and mice.
REFERENCE   4  (residues 1 to 2549)
  AUTHORS   Zhan,J., Harwood,F., Have,S.T., Lamond,A., Phillips,A.H.,
            Kriwacki,R.W., Halder,P., Cardone,M. and Grosveld,G.C.
  TITLE     Assembly of mTORC3 Involves Binding of ETV7 to Two Separate
            Sequences in the mTOR Kinase Domain
  JOURNAL   Int J Mol Sci 25 (18), 10042 (2024)
   PUBMED   39337528
  REMARK    GeneRIF: Assembly of mTORC3 Involves Binding of ETV7 to Two
            Separate Sequences in the mTOR Kinase Domain.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2549)
  AUTHORS   Gordon,D.E., Jang,G.M., Bouhaddou,M., Xu,J., Obernier,K.,
            White,K.M., O'Meara,M.J., Rezelj,V.V., Guo,J.Z., Swaney,D.L.,
            Tummino,T.A., Huttenhain,R., Kaake,R.M., Richards,A.L.,
            Tutuncuoglu,B., Foussard,H., Batra,J., Haas,K., Modak,M., Kim,M.,
            Haas,P., Polacco,B.J., Braberg,H., Fabius,J.M., Eckhardt,M.,
            Soucheray,M., Bennett,M.J., Cakir,M., McGregor,M.J., Li,Q.,
            Meyer,B., Roesch,F., Vallet,T., Mac Kain,A., Miorin,L., Moreno,E.,
            Naing,Z.Z.C., Zhou,Y., Peng,S., Shi,Y., Zhang,Z., Shen,W.,
            Kirby,I.T., Melnyk,J.E., Chorba,J.S., Lou,K., Dai,S.A.,
            Barrio-Hernandez,I., Memon,D., Hernandez-Armenta,C., Lyu,J.,
            Mathy,C.J.P., Perica,T., Pilla,K.B., Ganesan,S.J., Saltzberg,D.J.,
            Rakesh,R., Liu,X., Rosenthal,S.B., Calviello,L., Venkataramanan,S.,
            Liboy-Lugo,J., Lin,Y., Huang,X.P., Liu,Y., Wankowicz,S.A., Bohn,M.,
            Safari,M., Ugur,F.S., Koh,C., Savar,N.S., Tran,Q.D., Shengjuler,D.,
            Fletcher,S.J., O'Neal,M.C., Cai,Y., Chang,J.C.J., Broadhurst,D.J.,
            Klippsten,S., Sharp,P.P., Wenzell,N.A., Kuzuoglu-Ozturk,D.,
            Wang,H.Y., Trenker,R., Young,J.M., Cavero,D.A., Hiatt,J.,
            Roth,T.L., Rathore,U., Subramanian,A., Noack,J., Hubert,M.,
            Stroud,R.M., Frankel,A.D., Rosenberg,O.S., Verba,K.A., Agard,D.A.,
            Ott,M., Emerman,M., Jura,N., von Zastrow,M., Verdin,E.,
            Ashworth,A., Schwartz,O., d'Enfert,C., Mukherjee,S., Jacobson,M.,
            Malik,H.S., Fujimori,D.G., Ideker,T., Craik,C.S., Floor,S.N.,
            Fraser,J.S., Gross,J.D., Sali,A., Roth,B.L., Ruggero,D.,
            Taunton,J., Kortemme,T., Beltrao,P., Vignuzzi,M., Garcia-Sastre,A.,
            Shokat,K.M., Shoichet,B.K. and Krogan,N.J.
  TITLE     A SARS-CoV-2 protein interaction map reveals targets for drug
            repurposing
  JOURNAL   Nature 583 (7816), 459-468 (2020)
   PUBMED   32353859
REFERENCE   6  (residues 1 to 2549)
  AUTHORS   Zhou,Y., Hou,Y., Shen,J., Huang,Y., Martin,W. and Cheng,F.
  TITLE     Network-based drug repurposing for novel coronavirus
            2019-nCoV/SARS-CoV-2
  JOURNAL   Cell Discov 6, 14 (2020)
   PUBMED   32194980
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 2549)
  AUTHORS   Chen,J., Zheng,X.F., Brown,E.J. and Schreiber,S.L.
  TITLE     Identification of an 11-kDa FKBP12-rapamycin-binding domain within
            the 289-kDa FKBP12-rapamycin-associated protein and
            characterization of a critical serine residue
  JOURNAL   Proc Natl Acad Sci U S A 92 (11), 4947-4951 (1995)
   PUBMED   7539137
REFERENCE   8  (residues 1 to 2549)
  AUTHORS   Chiu,M.I., Katz,H. and Berlin,V.
  TITLE     RAPT1, a mammalian homolog of yeast Tor, interacts with the
            FKBP12/rapamycin complex
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 12574-12578 (1994)
   PUBMED   7809080
REFERENCE   9  (residues 1 to 2549)
  AUTHORS   Prada,C.E., Raski,C.R., Mirzaa,G., Besterman,A., Krueger,D.A. and
            Liu,A.C.
  TITLE     Smith-Kingsmore Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41264764
REFERENCE   10 (residues 1 to 2549)
  AUTHORS   Grove,J.R., Banerjee,P., Balasubramanyam,A., Coffer,P.J.,
            Price,D.J., Avruch,J. and Woodgett,J.R.
  TITLE     Cloning and expression of two human p70 S6 kinase polypeptides
            differing only at their amino termini
  JOURNAL   Mol Cell Biol 11 (11), 5541-5550 (1991)
   PUBMED   1922062
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049653.7, AL391561.20 and
            AL109811.40.
            
            On Aug 24, 2020 this sequence version replaced XP_005263495.1.
            
            Summary: The protein encoded by this gene belongs to a family of
            phosphatidylinositol kinase-related kinases. These kinases mediate
            cellular responses to stresses such as DNA damage and nutrient
            deprivation. This kinase is a component of two distinct complexes,
            mTORC1, which controls protein synthesis, cell growth and
            proliferation, and mTORC2, which is a regulator of the actin
            cytoskeleton, and promotes cell survival and cell cycle
            progression. This protein acts as the target for the cell-cycle
            arrest and immunosuppressive effects of the FKBP12-rapamycin
            complex. Inhibitors of mTOR are used in organ transplants as
            immunosuppressants, and are being evaluated for their therapeutic
            potential in SARS-CoV-2 infections. Mutations in this gene are
            associated with Smith-Kingsmore syndrome and somatic focal cortical
            dysplasia type II. The ANGPTL7 gene is located in an intron of this
            gene. [provided by RefSeq, Aug 2020].
            
            Transcript Variant: Variants 1 and 2 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2974226.1,
                                           SRR14038194.1904474.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: relevant for COVID-19 treatment
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..2549
                     /product="serine/threonine-protein kinase mTOR isoform 1"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="mammalian target of rapamycin; FK506 binding
                     protein 12-rapamycin associated protein 2; rapamycin and
                     FKBP12 target 1; mechanistic target of rapamycin
                     (serine/threonine kinase); serine/threonine-protein kinase
                     mTOR; FKBP12-rapamycin complex-associated protein 1;
                     FKBP-rapamycin associated protein; rapamycin associated
                     protein FRAP2; rapamycin target protein 1;
                     tyrosine-protein kinase mTOR; FK506-binding protein
                     12-rapamycin complex-associated protein 1"
                     /calculated_mol_wt=288762
     Region          1..651
                     /region_name="Interaction with NBN.
                     /evidence=ECO:0000269|PubMed:23762398"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Region          363..2549
                     /region_name="TEL1"
                     /note="Phosphatidylinositol kinase or protein kinase, PI-3
                     family [Signal transduction mechanisms]; COG5032"
                     /db_xref="CDD:227365"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          637..683
                     /region_name="HEAT 16"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          655..681
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          686..724
                     /region_name="HEAT 17"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          691..721
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          727..766
                     /region_name="HEAT 18"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          729..759
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          769..811
                     /region_name="HEAT 19"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          772..805
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          814..853
                     /region_name="HEAT 20"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          817..847
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          857..893
                     /region_name="HEAT 21"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          894..942
                     /region_name="HEAT 22"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          943..988
                     /region_name="HEAT 23"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          955..981
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(969..970,973,980..981,1010..1011,1014,1017..1018,
                     1021,1050..1051,1054,1057..1058,1061,1091..1092,1095,
                     1098..1099,1133..1134,1137,1140..1141)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          989..1027
                     /region_name="HEAT 24"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          993..1021
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1029..1068
                     /region_name="HEAT 25"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1033..1062
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1069..1105
                     /region_name="HEAT 26"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1073..1099
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1106..1144
                     /region_name="HEAT 27"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1111..1142
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          1145..1188
                     /region_name="HEAT 28"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1154..1180
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Region          1189..1225
                     /region_name="HEAT 29"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Site            1218
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Region          1226..1273
                     /region_name="HEAT 30"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Site            1261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19487463,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Region          1274..1311
                     /region_name="HEAT 31"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1312..1345
                     /region_name="HEAT 32"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1346..1382
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1383..1408
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1409..1442
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1443..1473
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1474..1507
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1508..1541
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1542..1574
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1575..1614
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1615..1649
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1650..1693
                     /region_name="TPR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1694..1731
                     /region_name="TPR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1732..1786
                     /region_name="TPR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1787..1846
                     /region_name="TPR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1812..1867
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1898..1930
                     /region_name="TPR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1931..1970
                     /region_name="TPR 15"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          1971..2005
                     /region_name="TPR 16"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          2012..2144
                     /region_name="Sufficient for interaction with the
                     FKBP1A/rapamycin complex.
                     /evidence=ECO:0000250|UniProtKB:Q9JLN9"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Site            2159
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TBK1.
                     /evidence=ECO:0000269|PubMed:21576368,
                     ECO:0000269|PubMed:29150432; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Region          2162..2168
                     /region_name="G-loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Site            2164
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:21576368; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Site            2173
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:24247430; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Region          2258..2296
                     /region_name="Interaction with MLST8"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          2335..2343
                     /region_name="Catalytic loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Region          2355..2380
                     /region_name="Activation loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (P42345.1)"
     Site            2446
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by RPS6KB1.
                     /evidence=ECO:0000269|PubMed:15905173; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Site            2448
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KB1.
                     /evidence=ECO:0000269|PubMed:15899889,
                     ECO:0000269|PubMed:15905173, ECO:0000269|PubMed:19145465,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Site            2478
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P42345.1)"
     Site            2481
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20022946,
                     ECO:0000269|PubMed:21576368, ECO:0007744|PubMed:18669648;
                     propagated from UniProtKB/Swiss-Prot (P42345.1)"
     CDS             1..2549
                     /gene="MTOR"
                     /gene_synonym="FRAP; FRAP1; FRAP2; RAFT1; RAPT1; SKS"
                     /coded_by="NM_001386500.1:149..7798"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS127.1"
                     /db_xref="GeneID:2475"
                     /db_xref="HGNC:HGNC:3942"
                     /db_xref="MIM:601231"
ORIGIN      
        1 mlgtgpaaat taattssnvs vlqqfasglk srneetraka akelqhyvtm elremsqees
       61 trfydqlnhh ifelvsssda nerkggilai asligveggn atrigrfany lrnllpsndp
      121 vvmemaskai grlamagdtf taeyvefevk ralewlgadr negrrhaavl vlrelaisvp
      181 tfffqqvqpf fdnifvavwd pkqairegav aalraclilt tqrepkemqk pqwyrhtfee
      241 aekgfdetla kekgmnrddr ihgallilne lvrissmege rlreemeeit qqqlvhdkyc
      301 kdlmgfgtkp rhitpftsfq avqpqqsnal vgllgysshq glmgfgtsps pakstlvesr
      361 ccrdlmeekf dqvcqwvlkc rnsknsliqm tilnllprla afrpsaftdt qylqdtmnhv
      421 lscvkkeker taafqalgll svavrsefkv ylprvldiir aalppkdfah krqkamqvda
      481 tvftcismla ramgpgiqqd ikellepmla vglspaltav lydlsrqipq lkkdiqdgll
      541 kmlslvlmhk plrhpgmpkg lahqlaspgl ttlpeasdvg sitlalrtlg sfefeghslt
      601 qfvrhcadhf lnsehkeirm eaartcsrll tpsihlisgh ahvvsqtavq vvadvlskll
      661 vvgitdpdpd irycvlasld erfdahlaqa enlqalfval ndqvfeirel aictvgrlss
      721 mnpafvmpfl rkmliqilte lehsgigrik eqsarmlghl vsnaprlirp ymepilkali
      781 lklkdpdpdp npgvinnvla tigelaqvsg lemrkwvdel fiiimdmlqd ssllakrqva
      841 lwtlgqlvas tgyvvepyrk yptllevlln flkteqnqgt rreairvlgl lgaldpykhk
      901 vnigmidqsr dasavslses kssqdssdys tsemlvnmgn lpldefypav smvalmrifr
      961 dqslshhhtm vvqaitfifk slglkcvqfl pqvmptflnv irvcdgaire flfqqlgmlv
     1021 sfvkshirpy mdeivtlmre fwvmntsiqs tiillieqiv valggefkly lpqliphmlr
     1081 vfmhdnspgr ivsikllaai qlfganlddy lhlllppivk lfdapeaplp srkaaletvd
     1141 rltesldftd yasriihpiv rtldqspelr stamdtlssl vfqlgkkyqi fipmvnkvlv
     1201 rhrinhqryd vlicrivkgy tladeeedpl iyqhrmlrsg qgdalasgpv etgpmkklhv
     1261 stinlqkawg aarrvskddw lewlrrlsle llkdssspsl rscwalaqay npmardlfna
     1321 afvscwseln edqqdelirs ielaltsqdi aevtqtllnl aefmehsdkg plplrddngi
     1381 vllgeraakc rayakalhyk elefqkgptp aileslisin nklqqpeaaa gvleyamkhf
     1441 geleiqatwy eklhewedal vaydkkmdtn kddpelmlgr mrclealgew gqlhqqccek
     1501 wtlvndetqa kmarmaaaaa wglgqwdsme eytcmiprdt hdgafyravl alhqdlfsla
     1561 qqcidkardl ldaeltamag esysraygam vschmlsele eviqyklvpe rreiirqiww
     1621 erlqgcqriv edwqkilmvr slvvsphedm rtwlkyaslc gksgrlalah ktlvlllgvd
     1681 psrqldhplp tvhpqvtyay mknmwksark idafqhmqhf vqtmqqqaqh aiatedqqhk
     1741 qelhklmarc flklgewqln lqginestip kvlqyysaat ehdrswykaw hawavmnfea
     1801 vlhykhqnqa rdekkklrha sganitnatt aattaatatt tastegsnse seaestensp
     1861 tpsplqkkvt edlsktllmy tvpavqgffr sislsrgnnl qdtlrvltlw fdyghwpdvn
     1921 ealvegvkai qidtwlqvip qliaridtpr plvgrlihql ltdigryhpq aliypltvas
     1981 kstttarhna ankilknmce hsntlvqqam mvseelirva ilwhemwheg leeasrlyfg
     2041 ernvkgmfev leplhammer gpqtlketsf nqaygrdlme aqewcrkymk sgnvkdltqa
     2101 wdlyyhvfrr iskqlpqlts lelqyvspkl lmcrdlelav pgtydpnqpi iriqsiapsl
     2161 qvitskqrpr kltlmgsngh efvfllkghe dlrqdervmq lfglvntlla ndptslrknl
     2221 siqryavipl stnsgligwv phcdtlhali rdyrekkkil lniehrimlr mapdydhltl
     2281 mqkvevfeha vnntagddla kllwlkspss evwfdrrtny trslavmsmv gyilglgdrh
     2341 psnlmldrls gkilhidfgd cfevamtrek fpekipfrlt rmltnamevt gldgnyritc
     2401 htvmevlreh kdsvmavlea fvydpllnwr lmdtntkgnk rsrtrtdsys agqsveildg
     2461 velgepahkk tgttvpesih sfigdglvkp ealnkkaiqi inrvrdkltg rdfshddtld
     2521 vptqvellik qatshenlcq cyigwcpfw
//
LOCUS       NP_932164                338 aa            linear   PRI 24-NOV-2025
DEFINITION  3-hydroxyisobutyryl-CoA hydrolase, mitochondrial isoform 2
            precursor [Homo sapiens].
ACCESSION   NP_932164
VERSION     NP_932164.1
DBSOURCE    REFSEQ: accession NM_198047.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Li,Y., Wu,T., Li,Y., Xu,C., Zhou,C., Li,Z., Shang,W., Wang,L.,
            Liu,Z., Wang,J., Liu,Y., Fang,F., Yang,B. and Tong,C.
  TITLE     Ectopic protein lysine methacrylation contributes to defects caused
            by loss of HIBCH or ECHS1
  JOURNAL   Cell Rep 44 (3), 115379 (2025)
   PUBMED   40056416
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Meng,X.H., Weng,Y.T., Rao,Y., Xu,Y.Q., Sun,H. and Li,C.
  TITLE     Two genetic variants in the HIBCH and FTCDNL1 genes are associated
            with susceptibility to developmental dysplasia of the hips among
            the Han Chinese population of Southwest China
  JOURNAL   J Orthop Surg Res 19 (1), 464 (2024)
   PUBMED   39113043
  REMARK    GeneRIF: Two genetic variants in the HIBCH and FTCDNL1 genes are
            associated with susceptibility to developmental dysplasia of the
            hips among the Han Chinese population of Southwest China.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Marti-Sanchez,L., Baide-Mairena,H., Marce-Grau,A., Pons,R.,
            Skouma,A., Lopez-Laso,E., Sigatullina,M., Rizzo,C., Semeraro,M.,
            Martinelli,D., Carrozzo,R., Dionisi-Vici,C.,
            Gonzalez-Gutierrez-Solana,L., Correa-Vela,M.,
            Ortigoza-Escobar,J.D., Sanchez-Montanez,A., Vazquez,E., Delgado,I.,
            Aguilera-Albesa,S., Yoldi,M.E., Ribes,A., Tort,F., Pollini,L.,
            Galosi,S., Leuzzi,V., Tolve,M., Perez-Gay,L.,
            Aldamiz-Echevarria,L., Del Toro,M., Arranz,A., Roelens,F.,
            Urreizti,R., Artuch,R., Macaya,A. and Perez-Duenas,B.
  TITLE     Delineating the neurological phenotype in children with defects in
            the ECHS1 or HIBCH gene
  JOURNAL   J Inherit Metab Dis 44 (2), 401-414 (2021)
   PUBMED   32677093
  REMARK    GeneRIF: Delineating the neurological phenotype in children with
            defects in the ECHS1 or HIBCH gene.
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Wu,C., Ma,M.H., Brown,K.R., Geisler,M., Li,L., Tzeng,E., Jia,C.Y.,
            Jurisica,I. and Li,S.S.
  TITLE     Systematic identification of SH3 domain-mediated human
            protein-protein interactions by peptide array target screening
  JOURNAL   Proteomics 7 (11), 1775-1785 (2007)
   PUBMED   17474147
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Loupatty,F.J., Clayton,P.T., Ruiter,J.P., Ofman,R., Ijlst,L.,
            Brown,G.K., Thorburn,D.R., Harris,R.A., Duran,M., Desousa,C.,
            Krywawych,S., Heales,S.J. and Wanders,R.J.
  TITLE     Mutations in the gene encoding 3-hydroxyisobutyryl-CoA hydrolase
            results in progressive infantile neurodegeneration
  JOURNAL   Am J Hum Genet 80 (1), 195-199 (2007)
   PUBMED   17160907
  REMARK    GeneRIF: Molecular analysis in both patients uncovered mutations in
            the HIBCH gene, including one missense mutation in a conserved part
            of the protein and two mutations affecting splicing.
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Ishigure,K., Shimomura,Y., Murakami,T., Kaneko,T., Takeda,S.,
            Inoue,S., Nomoto,S., Koshikawa,K., Nonami,T. and Nakao,A.
  TITLE     Human liver disease decreases methacrylyl-CoA hydratase and
            beta-hydroxyisobutyryl-CoA hydrolase activities in valine
            catabolism
  JOURNAL   Clin Chim Acta 312 (1-2), 115-121 (2001)
   PUBMED   11580916
REFERENCE   8  (residues 1 to 338)
  AUTHORS   Hawes,J.W., Jaskiewicz,J., Shimomura,Y., Huang,B., Bunting,J.,
            Harper,E.T. and Harris,R.A.
  TITLE     Primary structure and tissue-specific expression of human
            beta-hydroxyisobutyryl-coenzyme A hydrolase
  JOURNAL   J Biol Chem 271 (42), 26430-26434 (1996)
   PUBMED   8824301
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Abdenur,J. and Barrick,R.
  TITLE     3-Hydroxyisobutyryl-CoA Hydrolase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41264763
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Rahman,S., Thorburn,D.R. and Ball,M.
  TITLE     Nuclear Gene-Encoded Leigh Syndrome Spectrum Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26425749
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092178.4, BC005190.1,
            AK223023.1 and AC010679.6.
            
            Summary: This gene encodes the enzyme responsible for hydrolysis of
            both HIBYL-CoA and beta-hydroxypropionyl-CoA. Mutations in this
            gene have been associated with 3-hyroxyisobutyryl-CoA hydrolase
            deficiency. Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (2) lacks an exon in the 3' coding
            region, which results in a frameshift and an early stop codon,
            compared to variant 1. The encoded isoform (2) has a distinct
            C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.102143.1,
                                           SRR14038193.1102044.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.2"
     Protein         1..338
                     /product="3-hydroxyisobutyryl-CoA hydrolase, mitochondrial
                     isoform 2 precursor"
                     /EC_number="3.1.2.4"
                     /note="3-hydroxyisobutyryl-Coenzyme A hydrolase;
                     3-hydroxyisobutyryl-CoA hydrolase, mitochondrial; HIB-CoA
                     hydrolase; HIBYL-CoA-H; testicular tissue protein Li 86"
                     /calculated_mol_wt=34015
     transit_peptide 1..32
                     /calculated_mol_wt=4016
     mat_peptide     33..338
                     /product="3-hydroxyisobutyryl-CoA hydrolase, mitochondrial
                     isoform 2"
                     /calculated_mol_wt=34015
     Region          46..337
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
     Site            55
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8QZS1; propagated from
                     UniProtKB/Swiss-Prot (Q6NVY1.2)"
     Site            92
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q6NVY1.2)"
     Site            221
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8QZS1; propagated from
                     UniProtKB/Swiss-Prot (Q6NVY1.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NVY1.2)"
     Site            297
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8QZS1; propagated from
                     UniProtKB/Swiss-Prot (Q6NVY1.2)"
     CDS             1..338
                     /gene="HIBCH"
                     /gene_synonym="HIBYLCOAH"
                     /coded_by="NM_198047.3:77..1093"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS46475.1"
                     /db_xref="GeneID:26275"
                     /db_xref="HGNC:HGNC:4908"
                     /db_xref="MIM:610690"
ORIGIN      
        1 mgqremwrlm srfnafkrtn tilhhlrmsk htdaaeevll ekkgctgvit lnrpkflnal
       61 tlnmirqiyp qlkkweqdpe tfliiikgag gkafcaggdi rviseaekak qkiapvffre
      121 eymlnnavgs cqkpyvalih gitmgggvgl svhgqfrvat ekclfampet aiglfpdvgg
      181 gyflprlqgk lgyflaltgf rlkgrdvyra giathfvdse klamleedll alkspskeni
      241 asvlenyhte skidrdksfi leehmdkins cfsantveei ienlqqdgss faleqlkvin
      301 kmsptslkit lrqlmegssk tlqevltmey rlsqacmf
//
LOCUS       NP_055085                487 aa            linear   PRI 24-NOV-2025
DEFINITION  B(0,+)-type amino acid transporter 1 [Homo sapiens].
ACCESSION   NP_055085
VERSION     NP_055085.1
DBSOURCE    REFSEQ: accession NM_014270.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Wu,C.W., Badreddine,J., Chang,J., Huang,Y.M., Kim,F.J., Wild,T.,
            Tsai,A.C., Meeks,N., Donalisio Da Silva,R., Molina,W.R. and
            Schumacher,F.R.
  TITLE     Population genetics analysis of SLC3A1 and SLC7A9 revealed the
            etiology of cystine stone may be more than what our current genetic
            knowledge can explain
  JOURNAL   Urolithiasis 51 (1), 101 (2023)
   PUBMED   37561200
  REMARK    GeneRIF: Population genetics analysis of SLC3A1 and SLC7A9 revealed
            the etiology of cystine stone may be more than what our current
            genetic knowledge can explain.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Lee,B., Lee,S.Y., Han,D.H. and Park,H.D.
  TITLE     Interpretation of SLC3A1 and SLC7A9 variants in cystinuria
            patients: The significance of the PM3 criterion and protein
            stability
  JOURNAL   Urolithiasis 51 (1), 94 (2023)
   PUBMED   37439839
  REMARK    GeneRIF: Interpretation of SLC3A1 and SLC7A9 variants in cystinuria
            patients: The significance of the PM3 criterion and protein
            stability.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Baba,H., Kanda,M., Sawaki,K., Nakamura,S., Ueda,S., Shimizu,D.,
            Koike,M., Kodera,Y. and Fujii,T.
  TITLE     SLC7A9 as a Potential Biomarker for Lymph Node Metastasis of
            Esophageal Squamous Cell Carcinoma
  JOURNAL   Ann Surg Oncol 29 (4), 2699-2709 (2022)
   PUBMED   34773193
  REMARK    GeneRIF: SLC7A9 as a Potential Biomarker for Lymph Node Metastasis
            of Esophageal Squamous Cell Carcinoma.
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Tkaczyk,M., Gadomska-Prokop,K., Zaluska-Lesniewska,I., Musial,K.,
            Zawadzki,J., Jobs,K., Porowski,T., Rogowska-Kalisz,A., Jander,A.,
            Kirolos,M., Halinski,A., Krzemien,A., Sobieszczanska-Drozdziel,A.,
            Zachwieja,K., Beck,B.B., Sikora,P. and Zaniew,M.
  TITLE     Clinical profile of a Polish cohort of children and young adults
            with cystinuria
  JOURNAL   Ren Fail 43 (1), 62-70 (2021)
   PUBMED   33349102
  REMARK    GeneRIF: Clinical profile of a Polish cohort of children and young
            adults with cystinuria.
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Wu,D., Grund,T.N., Welsch,S., Mills,D.J., Michel,M., Safarian,S.
            and Michel,H.
  TITLE     Structural basis for amino acid exchange by a human heteromeric
            amino acid transporter
  JOURNAL   Proc Natl Acad Sci U S A 117 (35), 21281-21287 (2020)
   PUBMED   32817565
  REMARK    GeneRIF: Structural basis for amino acid exchange by a human
            heteromeric amino acid transporter.
REFERENCE   6  (residues 1 to 487)
  AUTHORS   Feliubadalo,L., Font,M., Purroy,J., Rousaud,F., Estivill,X.,
            Nunes,V., Golomb,E., Centola,M., Aksentijevich,I., Kreiss,Y.,
            Goldman,B., Pras,M., Kastner,D.L., Pras,E., Gasparini,P.,
            Bisceglia,L., Beccia,E., Gallucci,M., de Sanctis,L., Ponzone,A.,
            Rizzoni,G.F., Zelante,L., Bassi,M.T., George,A.L. Jr., Manzoni,M.,
            De Grandi,A., Riboni,M., Endsley,J.K., Ballabio,A., Borsani,G.,
            Reig,N., Fernandez,E., Estevez,R., Pineda,M., Torrents,D.,
            Camps,M., Lloberas,J., Zorzano,A. and Palacin,M.
  CONSRTM   International Cystinuria Consortium
  TITLE     Non-type I cystinuria caused by mutations in SLC7A9, encoding a
            subunit (bo,+AT) of rBAT
  JOURNAL   Nat Genet 23 (1), 52-57 (1999)
   PUBMED   10471498
REFERENCE   7  (residues 1 to 487)
  AUTHORS   Wartenfeld,R., Golomb,E., Katz,G., Bale,S.J., Goldman,B., Pras,M.,
            Kastner,D.L. and Pras,E.
  TITLE     Molecular analysis of cystinuria in Libyan Jews: exclusion of the
            SLC3A1 gene and mapping of a new locus on 19q
  JOURNAL   Am J Hum Genet 60 (3), 617-624 (1997)
   PUBMED   9042922
REFERENCE   8  (residues 1 to 487)
  AUTHORS   Bisceglia,L., Calonge,M.J., Totaro,A., Feliubadalo,L.,
            Melchionda,S., Garcia,J., Testar,X., Gallucci,M., Ponzone,A.,
            Zelante,L., Zorzano,A., Estivill,X., Gasparini,P., Nunes,V. and
            Palacin,M.
  TITLE     Localization, by linkage analysis, of the cystinuria type III gene
            to chromosome 19q13.1
  JOURNAL   Am J Hum Genet 60 (3), 611-616 (1997)
   PUBMED   9042921
REFERENCE   9  (residues 1 to 487)
  AUTHORS   Chillaron,J., Estevez,R., Mora,C., Wagner,C.A., Suessbrich,H.,
            Lang,F., Gelpi,J.L., Testar,X., Busch,A.E., Zorzano,A. and
            Palacin,M.
  TITLE     Obligatory amino acid exchange via systems bo,+-like and y+L-like.
            A tertiary active transport mechanism for renal reabsorption of
            cystine and dibasic amino acids
  JOURNAL   J Biol Chem 271 (30), 17761-17770 (1996)
   PUBMED   8663357
REFERENCE   10 (residues 1 to 487)
  AUTHORS   Spasiano,A., Halbritter,J. and Ferraro,P.M.
  TITLE     Cystinuria
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41264765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP276659.1, AK026446.1 and
            BC017962.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that belongs to a family of
            light subunits of amino acid transporters. This protein plays a
            role in the high-affinity and sodium-independent transport of
            cystine and neutral and dibasic amino acids, and appears to
            function in the reabsorption of cystine in the kidney tubule.
            Mutations in this gene cause non-type I cystinuria, a disease that
            leads to cystine stones in the urinary system due to impaired
            transport of cystine and dibasic amino acids. Alternate transcript
            variants, which encode the same protein, have been found for this
            gene. [provided by RefSeq, Jul 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2, and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026446.1, BC017962.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000023064.9/ ENSP00000023064.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.11"
     Protein         1..487
                     /product="B(0,+)-type amino acid transporter 1"
                     /note="solute carrier family 7 (cationic amino acid
                     transporter, y+ system), member 9; glycoprotein-associated
                     amino acid transporter b0,+AT1; b(0,+)AT; cystinuria type
                     3; solute carrier family 7 (glycoprotein-associated amino
                     acid transporter light chain, bo,+ system), member 9;
                     solute carrier family 7 (amino acid transporter light
                     chain, bo,+ system), member 9"
                     /calculated_mol_wt=53351
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P82252; propagated from
                     UniProtKB/Swiss-Prot (P82251.1)"
     Region          26..484
                     /region_name="2A0308"
                     /note="L-type amino acid transporter; TIGR00911"
                     /db_xref="CDD:273332"
     Site            32..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            63..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            111..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            148..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            170..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            252..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            303..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            352..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            371..391
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            411..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            435..450
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     CDS             1..487
                     /gene="SLC7A9"
                     /gene_synonym="BAT1; CSNU3"
                     /coded_by="NM_014270.5:194..1657"
                     /db_xref="CCDS:CCDS12425.1"
                     /db_xref="GeneID:11136"
                     /db_xref="HGNC:HGNC:11067"
                     /db_xref="MIM:604144"
ORIGIN      
        1 mgdtglrkrr edeksiqsqe pkttslqkel glisgisiiv gtiigsgifv spksvlsnte
       61 avgpcliiwa acgvlatlga lcfaelgtmi tksggeypyl meaygpipay lfswaslivi
      121 kptsfaiicl sfseyvcapf yvgckppqiv vkclaaaail fistvnslsv rlgsyvqnif
      181 taaklvivai iiisglvlla qgntknfdns fegaqlsvga islafynglw aydgwnqlny
      241 iteelrnpyr nlplaiiigi plvtacyilm nvsyftvmta tellqsqava vtfgdrvlyp
      301 aswivplfva fstigaangt cftagrliyv agreghmlkv lsyisvrrlt papaiifygi
      361 iatiyiipgd inslvnyfsf aawlfyglti lglivmrftr kelerpikvp vvipvlmtli
      421 svflvlapii skptweylyc vlfilsgllf yflfvhykfg waqkiskpit mhlqmlmevv
      481 ppeedpe
//
LOCUS       NP_001229965             487 aa            linear   PRI 24-NOV-2025
DEFINITION  B(0,+)-type amino acid transporter 1 [Homo sapiens].
ACCESSION   NP_001229965
VERSION     NP_001229965.1
DBSOURCE    REFSEQ: accession NM_001243036.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Wu,C.W., Badreddine,J., Chang,J., Huang,Y.M., Kim,F.J., Wild,T.,
            Tsai,A.C., Meeks,N., Donalisio Da Silva,R., Molina,W.R. and
            Schumacher,F.R.
  TITLE     Population genetics analysis of SLC3A1 and SLC7A9 revealed the
            etiology of cystine stone may be more than what our current genetic
            knowledge can explain
  JOURNAL   Urolithiasis 51 (1), 101 (2023)
   PUBMED   37561200
  REMARK    GeneRIF: Population genetics analysis of SLC3A1 and SLC7A9 revealed
            the etiology of cystine stone may be more than what our current
            genetic knowledge can explain.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Lee,B., Lee,S.Y., Han,D.H. and Park,H.D.
  TITLE     Interpretation of SLC3A1 and SLC7A9 variants in cystinuria
            patients: The significance of the PM3 criterion and protein
            stability
  JOURNAL   Urolithiasis 51 (1), 94 (2023)
   PUBMED   37439839
  REMARK    GeneRIF: Interpretation of SLC3A1 and SLC7A9 variants in cystinuria
            patients: The significance of the PM3 criterion and protein
            stability.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Baba,H., Kanda,M., Sawaki,K., Nakamura,S., Ueda,S., Shimizu,D.,
            Koike,M., Kodera,Y. and Fujii,T.
  TITLE     SLC7A9 as a Potential Biomarker for Lymph Node Metastasis of
            Esophageal Squamous Cell Carcinoma
  JOURNAL   Ann Surg Oncol 29 (4), 2699-2709 (2022)
   PUBMED   34773193
  REMARK    GeneRIF: SLC7A9 as a Potential Biomarker for Lymph Node Metastasis
            of Esophageal Squamous Cell Carcinoma.
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Tkaczyk,M., Gadomska-Prokop,K., Zaluska-Lesniewska,I., Musial,K.,
            Zawadzki,J., Jobs,K., Porowski,T., Rogowska-Kalisz,A., Jander,A.,
            Kirolos,M., Halinski,A., Krzemien,A., Sobieszczanska-Drozdziel,A.,
            Zachwieja,K., Beck,B.B., Sikora,P. and Zaniew,M.
  TITLE     Clinical profile of a Polish cohort of children and young adults
            with cystinuria
  JOURNAL   Ren Fail 43 (1), 62-70 (2021)
   PUBMED   33349102
  REMARK    GeneRIF: Clinical profile of a Polish cohort of children and young
            adults with cystinuria.
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Wu,D., Grund,T.N., Welsch,S., Mills,D.J., Michel,M., Safarian,S.
            and Michel,H.
  TITLE     Structural basis for amino acid exchange by a human heteromeric
            amino acid transporter
  JOURNAL   Proc Natl Acad Sci U S A 117 (35), 21281-21287 (2020)
   PUBMED   32817565
  REMARK    GeneRIF: Structural basis for amino acid exchange by a human
            heteromeric amino acid transporter.
REFERENCE   6  (residues 1 to 487)
  AUTHORS   Feliubadalo,L., Font,M., Purroy,J., Rousaud,F., Estivill,X.,
            Nunes,V., Golomb,E., Centola,M., Aksentijevich,I., Kreiss,Y.,
            Goldman,B., Pras,M., Kastner,D.L., Pras,E., Gasparini,P.,
            Bisceglia,L., Beccia,E., Gallucci,M., de Sanctis,L., Ponzone,A.,
            Rizzoni,G.F., Zelante,L., Bassi,M.T., George,A.L. Jr., Manzoni,M.,
            De Grandi,A., Riboni,M., Endsley,J.K., Ballabio,A., Borsani,G.,
            Reig,N., Fernandez,E., Estevez,R., Pineda,M., Torrents,D.,
            Camps,M., Lloberas,J., Zorzano,A. and Palacin,M.
  CONSRTM   International Cystinuria Consortium
  TITLE     Non-type I cystinuria caused by mutations in SLC7A9, encoding a
            subunit (bo,+AT) of rBAT
  JOURNAL   Nat Genet 23 (1), 52-57 (1999)
   PUBMED   10471498
REFERENCE   7  (residues 1 to 487)
  AUTHORS   Wartenfeld,R., Golomb,E., Katz,G., Bale,S.J., Goldman,B., Pras,M.,
            Kastner,D.L. and Pras,E.
  TITLE     Molecular analysis of cystinuria in Libyan Jews: exclusion of the
            SLC3A1 gene and mapping of a new locus on 19q
  JOURNAL   Am J Hum Genet 60 (3), 617-624 (1997)
   PUBMED   9042922
REFERENCE   8  (residues 1 to 487)
  AUTHORS   Bisceglia,L., Calonge,M.J., Totaro,A., Feliubadalo,L.,
            Melchionda,S., Garcia,J., Testar,X., Gallucci,M., Ponzone,A.,
            Zelante,L., Zorzano,A., Estivill,X., Gasparini,P., Nunes,V. and
            Palacin,M.
  TITLE     Localization, by linkage analysis, of the cystinuria type III gene
            to chromosome 19q13.1
  JOURNAL   Am J Hum Genet 60 (3), 611-616 (1997)
   PUBMED   9042921
REFERENCE   9  (residues 1 to 487)
  AUTHORS   Chillaron,J., Estevez,R., Mora,C., Wagner,C.A., Suessbrich,H.,
            Lang,F., Gelpi,J.L., Testar,X., Busch,A.E., Zorzano,A. and
            Palacin,M.
  TITLE     Obligatory amino acid exchange via systems bo,+-like and y+L-like.
            A tertiary active transport mechanism for renal reabsorption of
            cystine and dibasic amino acids
  JOURNAL   J Biol Chem 271 (30), 17761-17770 (1996)
   PUBMED   8663357
REFERENCE   10 (residues 1 to 487)
  AUTHORS   Spasiano,A., Halbritter,J. and Ferraro,P.M.
  TITLE     Cystinuria
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41264765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP276659.1, AK313708.1,
            AF141289.1 and BC017962.1.
            
            Summary: This gene encodes a protein that belongs to a family of
            light subunits of amino acid transporters. This protein plays a
            role in the high-affinity and sodium-independent transport of
            cystine and neutral and dibasic amino acids, and appears to
            function in the reabsorption of cystine in the kidney tubule.
            Mutations in this gene cause non-type I cystinuria, a disease that
            leads to cystine stones in the urinary system due to impaired
            transport of cystine and dibasic amino acids. Alternate transcript
            variants, which encode the same protein, have been found for this
            gene. [provided by RefSeq, Jul 2011].
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. Variants 1, 2, and 3 encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF141289.1, SRR14038193.852451.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.11"
     Protein         1..487
                     /product="B(0,+)-type amino acid transporter 1"
                     /note="solute carrier family 7 (cationic amino acid
                     transporter, y+ system), member 9; glycoprotein-associated
                     amino acid transporter b0,+AT1; b(0,+)AT; cystinuria type
                     3; solute carrier family 7 (glycoprotein-associated amino
                     acid transporter light chain, bo,+ system), member 9;
                     solute carrier family 7 (amino acid transporter light
                     chain, bo,+ system), member 9"
                     /calculated_mol_wt=53351
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P82252; propagated from
                     UniProtKB/Swiss-Prot (P82251.1)"
     Region          26..484
                     /region_name="2A0308"
                     /note="L-type amino acid transporter; TIGR00911"
                     /db_xref="CDD:273332"
     Site            32..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            63..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            111..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            148..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            170..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            252..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            303..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            352..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            371..391
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            411..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            435..450
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     CDS             1..487
                     /gene="SLC7A9"
                     /gene_synonym="BAT1; CSNU3"
                     /coded_by="NM_001243036.2:203..1666"
                     /db_xref="CCDS:CCDS12425.1"
                     /db_xref="GeneID:11136"
                     /db_xref="HGNC:HGNC:11067"
                     /db_xref="MIM:604144"
ORIGIN      
        1 mgdtglrkrr edeksiqsqe pkttslqkel glisgisiiv gtiigsgifv spksvlsnte
       61 avgpcliiwa acgvlatlga lcfaelgtmi tksggeypyl meaygpipay lfswaslivi
      121 kptsfaiicl sfseyvcapf yvgckppqiv vkclaaaail fistvnslsv rlgsyvqnif
      181 taaklvivai iiisglvlla qgntknfdns fegaqlsvga islafynglw aydgwnqlny
      241 iteelrnpyr nlplaiiigi plvtacyilm nvsyftvmta tellqsqava vtfgdrvlyp
      301 aswivplfva fstigaangt cftagrliyv agreghmlkv lsyisvrrlt papaiifygi
      361 iatiyiipgd inslvnyfsf aawlfyglti lglivmrftr kelerpikvp vvipvlmtli
      421 svflvlapii skptweylyc vlfilsgllf yflfvhykfg waqkiskpit mhlqmlmevv
      481 ppeedpe
//
LOCUS       NP_055177                386 aa            linear   PRI 24-NOV-2025
DEFINITION  3-hydroxyisobutyryl-CoA hydrolase, mitochondrial isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_055177
VERSION     NP_055177.2
DBSOURCE    REFSEQ: accession NM_014362.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Li,Y., Wu,T., Li,Y., Xu,C., Zhou,C., Li,Z., Shang,W., Wang,L.,
            Liu,Z., Wang,J., Liu,Y., Fang,F., Yang,B. and Tong,C.
  TITLE     Ectopic protein lysine methacrylation contributes to defects caused
            by loss of HIBCH or ECHS1
  JOURNAL   Cell Rep 44 (3), 115379 (2025)
   PUBMED   40056416
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Meng,X.H., Weng,Y.T., Rao,Y., Xu,Y.Q., Sun,H. and Li,C.
  TITLE     Two genetic variants in the HIBCH and FTCDNL1 genes are associated
            with susceptibility to developmental dysplasia of the hips among
            the Han Chinese population of Southwest China
  JOURNAL   J Orthop Surg Res 19 (1), 464 (2024)
   PUBMED   39113043
  REMARK    GeneRIF: Two genetic variants in the HIBCH and FTCDNL1 genes are
            associated with susceptibility to developmental dysplasia of the
            hips among the Han Chinese population of Southwest China.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Marti-Sanchez,L., Baide-Mairena,H., Marce-Grau,A., Pons,R.,
            Skouma,A., Lopez-Laso,E., Sigatullina,M., Rizzo,C., Semeraro,M.,
            Martinelli,D., Carrozzo,R., Dionisi-Vici,C.,
            Gonzalez-Gutierrez-Solana,L., Correa-Vela,M.,
            Ortigoza-Escobar,J.D., Sanchez-Montanez,A., Vazquez,E., Delgado,I.,
            Aguilera-Albesa,S., Yoldi,M.E., Ribes,A., Tort,F., Pollini,L.,
            Galosi,S., Leuzzi,V., Tolve,M., Perez-Gay,L.,
            Aldamiz-Echevarria,L., Del Toro,M., Arranz,A., Roelens,F.,
            Urreizti,R., Artuch,R., Macaya,A. and Perez-Duenas,B.
  TITLE     Delineating the neurological phenotype in children with defects in
            the ECHS1 or HIBCH gene
  JOURNAL   J Inherit Metab Dis 44 (2), 401-414 (2021)
   PUBMED   32677093
  REMARK    GeneRIF: Delineating the neurological phenotype in children with
            defects in the ECHS1 or HIBCH gene.
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Wu,C., Ma,M.H., Brown,K.R., Geisler,M., Li,L., Tzeng,E., Jia,C.Y.,
            Jurisica,I. and Li,S.S.
  TITLE     Systematic identification of SH3 domain-mediated human
            protein-protein interactions by peptide array target screening
  JOURNAL   Proteomics 7 (11), 1775-1785 (2007)
   PUBMED   17474147
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Loupatty,F.J., Clayton,P.T., Ruiter,J.P., Ofman,R., Ijlst,L.,
            Brown,G.K., Thorburn,D.R., Harris,R.A., Duran,M., Desousa,C.,
            Krywawych,S., Heales,S.J. and Wanders,R.J.
  TITLE     Mutations in the gene encoding 3-hydroxyisobutyryl-CoA hydrolase
            results in progressive infantile neurodegeneration
  JOURNAL   Am J Hum Genet 80 (1), 195-199 (2007)
   PUBMED   17160907
  REMARK    GeneRIF: Molecular analysis in both patients uncovered mutations in
            the HIBCH gene, including one missense mutation in a conserved part
            of the protein and two mutations affecting splicing.
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Ishigure,K., Shimomura,Y., Murakami,T., Kaneko,T., Takeda,S.,
            Inoue,S., Nomoto,S., Koshikawa,K., Nonami,T. and Nakao,A.
  TITLE     Human liver disease decreases methacrylyl-CoA hydratase and
            beta-hydroxyisobutyryl-CoA hydrolase activities in valine
            catabolism
  JOURNAL   Clin Chim Acta 312 (1-2), 115-121 (2001)
   PUBMED   11580916
REFERENCE   8  (residues 1 to 386)
  AUTHORS   Hawes,J.W., Jaskiewicz,J., Shimomura,Y., Huang,B., Bunting,J.,
            Harper,E.T. and Harris,R.A.
  TITLE     Primary structure and tissue-specific expression of human
            beta-hydroxyisobutyryl-coenzyme A hydrolase
  JOURNAL   J Biol Chem 271 (42), 26430-26434 (1996)
   PUBMED   8824301
REFERENCE   9  (residues 1 to 386)
  AUTHORS   Abdenur,J. and Barrick,R.
  TITLE     3-Hydroxyisobutyryl-CoA Hydrolase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41264763
REFERENCE   10 (residues 1 to 386)
  AUTHORS   Rahman,S., Thorburn,D.R. and Ball,M.
  TITLE     Nuclear Gene-Encoded Leigh Syndrome Spectrum Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26425749
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092178.4, AC010679.6 and
            AK223023.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 9, 2003 this sequence version replaced NP_055177.1.
            
            Summary: This gene encodes the enzyme responsible for hydrolysis of
            both HIBYL-CoA and beta-hydroxypropionyl-CoA. Mutations in this
            gene have been associated with 3-hyroxyisobutyryl-CoA hydrolase
            deficiency. Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.42595.1,
                                           SRR1660803.57272.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000359678.10/
                                                  ENSP00000352706.5
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.2"
     Protein         1..386
                     /product="3-hydroxyisobutyryl-CoA hydrolase, mitochondrial
                     isoform 1 precursor"
                     /EC_number="3.1.2.4"
                     /note="3-hydroxyisobutyryl-Coenzyme A hydrolase;
                     3-hydroxyisobutyryl-CoA hydrolase, mitochondrial; HIB-CoA
                     hydrolase; HIBYL-CoA-H; testicular tissue protein Li 86"
                     /calculated_mol_wt=39485
     transit_peptide 1..32
                     /calculated_mol_wt=4016
     mat_peptide     33..386
                     /product="3-hydroxyisobutyryl-CoA hydrolase, mitochondrial
                     isoform 1"
                     /calculated_mol_wt=39485
     Region          46..376
                     /region_name="ECH_2"
                     /note="Enoyl-CoA hydratase/isomerase; pfam16113"
                     /db_xref="CDD:465024"
     Site            55
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8QZS1; propagated from
                     UniProtKB/Swiss-Prot (Q6NVY1.2)"
     Site            92
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q6NVY1.2)"
     Site            221
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8QZS1; propagated from
                     UniProtKB/Swiss-Prot (Q6NVY1.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NVY1.2)"
     Site            297
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8QZS1; propagated from
                     UniProtKB/Swiss-Prot (Q6NVY1.2)"
     Site            353
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8QZS1; propagated from
                     UniProtKB/Swiss-Prot (Q6NVY1.2)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NVY1.2)"
     Site            360
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8QZS1; propagated from
                     UniProtKB/Swiss-Prot (Q6NVY1.2)"
     Site            365
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8QZS1; propagated from
                     UniProtKB/Swiss-Prot (Q6NVY1.2)"
     CDS             1..386
                     /gene="HIBCH"
                     /gene_synonym="HIBYLCOAH"
                     /coded_by="NM_014362.4:77..1237"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS2304.1"
                     /db_xref="GeneID:26275"
                     /db_xref="HGNC:HGNC:4908"
                     /db_xref="MIM:610690"
ORIGIN      
        1 mgqremwrlm srfnafkrtn tilhhlrmsk htdaaeevll ekkgctgvit lnrpkflnal
       61 tlnmirqiyp qlkkweqdpe tfliiikgag gkafcaggdi rviseaekak qkiapvffre
      121 eymlnnavgs cqkpyvalih gitmgggvgl svhgqfrvat ekclfampet aiglfpdvgg
      181 gyflprlqgk lgyflaltgf rlkgrdvyra giathfvdse klamleedll alkspskeni
      241 asvlenyhte skidrdksfi leehmdkins cfsantveei ienlqqdgss faleqlkvin
      301 kmsptslkit lrqlmegssk tlqevltmey rlsqacmrgh dfhegvravl idkdqspkwk
      361 padlkevtee dlnnhfkslg ssdlkf
//
LOCUS       NP_001186930            1235 aa            linear   PRI 24-NOV-2025
DEFINITION  neurogenic locus notch homolog protein 2 isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_001186930
VERSION     NP_001186930.1
DBSOURCE    REFSEQ: accession NM_001200001.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1235)
  AUTHORS   Zhou,X., Zhang,C., Yu,H., Feng,Z., Bai,X., Mei,Y., Li,L., Li,X.,
            Gou,X. and Deng,Y.
  TITLE     The MEF2A/SNHG16/miR-425-5p/NOTCH2 axis induces gemcitabine
            resistance by inhibiting ferroptosis in the starving bladder tumor
            microenvironment
  JOURNAL   Cell Signal 122, 111337 (2024)
   PUBMED   39121977
  REMARK    GeneRIF: The MEF2A/SNHG16/miR-425-5p/NOTCH2 axis induces
            gemcitabine resistance by inhibiting ferroptosis in the starving
            bladder tumor microenvironment.
REFERENCE   2  (residues 1 to 1235)
  AUTHORS   Yang,S., Xiong,L., Yang,G., Xiang,J., Li,L., Kang,L. and Liang,Z.
  TITLE     KLF13 restrains Dll4-muscular Notch2 axis to improve the muscle
            atrophy
  JOURNAL   J Cachexia Sarcopenia Muscle 15 (5), 1869-1882 (2024)
   PUBMED   38973459
  REMARK    GeneRIF: KLF13 restrains Dll4-muscular Notch2 axis to improve the
            muscle atrophy.
REFERENCE   3  (residues 1 to 1235)
  AUTHORS   Ferrandino,M., Cardiero,G., Di Dato,F., Cerrato,Y., Vitagliano,L.,
            Mandato,C., Morisco,F., Spagnuolo,M.I., Iorio,R., Di Taranto,M.D.
            and Fortunato,G.
  TITLE     Association of Very Rare NOTCH2 Variants with Clinical Features of
            Alagille Syndrome
  JOURNAL   Genes (Basel) 15 (8), 1034 (2024)
   PUBMED   39202394
  REMARK    GeneRIF: Association of Very Rare NOTCH2 Variants with Clinical
            Features of Alagille Syndrome.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1235)
  AUTHORS   Lin,H., Fu,L., Zhou,X., Yu,A., Chen,Y., Liao,W., Shu,G., Zhang,L.,
            Tan,L., Liang,H., Wang,Z., Deng,Q., Wang,J., Jin,M., Chen,Z.,
            Wei,J., Cao,J., Chen,W., Li,X., Li,P., Lu,J. and Luo,J.
  TITLE     LRP1 induces anti-PD-1 resistance by modulating the
            DLL4-NOTCH2-CCL2 axis and redirecting M2-like macrophage
            polarisation in bladder cancer
  JOURNAL   Cancer Lett 593, 216807 (2024)
   PUBMED   38462037
  REMARK    GeneRIF: LRP1 induces anti-PD-1 resistance by modulating the
            DLL4-NOTCH2-CCL2 axis and redirecting M2-like macrophage
            polarisation in bladder cancer.
REFERENCE   5  (residues 1 to 1235)
  AUTHORS   Li,M., He,W., Wang,F., Zhang,P., Zhang,X., Li,Q., Liu,T. and Li,Y.
  TITLE     High expression of NOTCH2 in gastric adenocarcinoma: A novel early
            diagnostic target
  JOURNAL   J Gastroenterol Hepatol 39 (6), 1115-1122 (2024)
   PUBMED   38577711
  REMARK    GeneRIF: High expression of NOTCH2 in gastric adenocarcinoma: A
            novel early diagnostic target.
REFERENCE   6  (residues 1 to 1235)
  AUTHORS   Hsieh,J.J., Nofziger,D.E., Weinmaster,G. and Hayward,S.D.
  TITLE     Epstein-Barr virus immortalization: Notch2 interacts with CBF1 and
            blocks differentiation
  JOURNAL   J Virol 71 (3), 1938-1945 (1997)
   PUBMED   9032325
REFERENCE   7  (residues 1 to 1235)
  AUTHORS   Katsanis,N., Fitzgibbon,J. and Fisher,E.M.
  TITLE     Paralogy mapping: identification of a region in the human MHC
            triplicated onto human chromosomes 1 and 9 allows the prediction
            and isolation of novel PBX and NOTCH loci
  JOURNAL   Genomics 35 (1), 101-108 (1996)
   PUBMED   8661110
REFERENCE   8  (residues 1 to 1235)
  AUTHORS   Larsson,C., Lardelli,M., White,I. and Lendahl,U.
  TITLE     The human NOTCH1, 2, and 3 genes are located at chromosome
            positions 9q34, 1p13-p11, and 19p13.2-p13.1 in regions of
            neoplasia-associated translocation
  JOURNAL   Genomics 24 (2), 253-258 (1994)
   PUBMED   7698746
REFERENCE   9  (residues 1 to 1235)
  AUTHORS   Spinner,N.B., Loomes,K.M., Krantz,I.D. and Gilbert,M.A.
  TITLE     Alagille Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301450
REFERENCE   10 (residues 1 to 1235)
  AUTHORS   Stifani,S., Blaumueller,C.M., Redhead,N.J., Hill,R.E. and
            Artavanis-Tsakonas,S.
  TITLE     Human homologs of a Drosophila Enhancer of split gene product
            define a novel family of nuclear proteins
  JOURNAL   Nat Genet 2 (2), 119-127 (1992)
   PUBMED   1303260
  REMARK    Erratum:[Nat Genet. 1992 Dec;2(4):343. doi: 10.1038/ng1292-343a.
            PMID: 1303292]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB290699.1, BC071562.1 and
            AF315356.1.
            
            Summary: This gene encodes a member of the Notch family. Members of
            this Type 1 transmembrane protein family share structural
            characteristics including an extracellular domain consisting of
            multiple epidermal growth factor-like (EGF) repeats, and an
            intracellular domain consisting of multiple, different domain
            types. Notch family members play a role in a variety of
            developmental processes by controlling cell fate decisions. The
            Notch signaling network is an evolutionarily conserved
            intercellular signaling pathway which regulates interactions
            between physically adjacent cells. In Drosophilia, notch
            interaction with its cell-bound ligands (delta, serrate)
            establishes an intercellular signaling pathway that plays a key
            role in development. Homologues of the notch-ligands have also been
            identified in human, but precise interactions between these ligands
            and the human notch homologues remain to be determined. This
            protein is cleaved in the trans-Golgi network, and presented on the
            cell surface as a heterodimer. This protein functions as a receptor
            for membrane bound ligands, and may play a role in vascular, renal
            and hepatic development. Two transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jan
            2011].
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            coding sequence compared to variant 1. The resulting isoform (2)
            has a shorter and distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC071562.1, SRR7346977.2813777.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..1235
                     /product="neurogenic locus notch homolog protein 2 isoform
                     2 precursor"
                     /note="Notch homolog 2; notch 2"
                     /calculated_mol_wt=129398
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2673
     mat_peptide     26..1235
                     /product="neurogenic locus notch homolog protein 2 isoform
                     2"
                     /calculated_mol_wt=129398
     Region          182..218
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(182,185,200)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          260..296
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(260,263,277)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          298..335
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(298,301,317)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          415..454
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(415,418,435)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          456..492
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(456,459,473)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          495..530
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          532..568
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(532,535,549)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          608..643
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          682..717
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(682,685,699)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          757..793
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(757,760,774)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          795..831
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(795,798,812)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          873..909
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(873,876,890)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          911..947
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(911,914,928)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          949..985
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(949,952,966)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          987..1022
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(987,990,1004)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1026..1061
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1151..1185
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1188..1219
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     CDS             1..1235
                     /gene="NOTCH2"
                     /gene_synonym="AGS2; HJCYS; hN2"
                     /coded_by="NM_001200001.2:257..3964"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:4853"
                     /db_xref="HGNC:HGNC:7882"
                     /db_xref="MIM:600275"
ORIGIN      
        1 mpalrpallw allalwlcca apahalqcrd gyepcvnegm cvtyhngtgy ckcpegflge
       61 ycqhrdpcek nrcqnggtcv aqamlgkatc rcasgftged cqystshpcf vsrpclnggt
      121 chmlsrdtye ctcqvgftgk ecqwtdacls hpcangstct tvanqfsckc ltgftgqkce
      181 tdvnecdipg hcqhggtcln lpgsyqcqcp qgftgqycds lyvpcapspc vnggtcrqtg
      241 dftfecnclp gfegstcern iddcpnhrcq nggvcvdgvn tyncrcppqw tgqfctedvd
      301 ecllqpnacq nggtcanrng gygcvcvngw sgddcsenid dcafasctpg stcidrvasf
      361 scmcpegkag llchlddaci snpchkgalc dtnplngqyi ctcpqgykga dctedvdeca
      421 mansnpceha gkcvntdgaf hceclkgyag prcemdinec hsdpcqndat cldkiggftc
      481 lcmpgfkgvh celeinecqs npcvnngqcv dkvnrfqclc ppgftgpvcq ididdcsstp
      541 clngakcidh pngyecqcat gftgvlceen idncdpdpch hgqcqdgids ytcicnpgym
      601 gaicsdqide cysspclndg rcidlvngyq cncqpgtsgv nceinfddca snpcihgicm
      661 dginryscvc spgftgqrcn ididecasnp crkgatcing vngfrcicpe gphhpscysq
      721 vneclsnpci hgnctgglsg ykclcdagwv gincevdkne clsnpcqngg tcdnlvngyr
      781 ctckkgfkgy ncqvnideca snpclnqgtc fddisgytch cvlpytgknc qtvlapcspn
      841 pcenaavcke spnfesytcl capgwqgqrc tididecisk pcmnhglchn tqgsymcecp
      901 pgfsgmdcee diddclanpc qnggscmdgv ntfsclclpg ftgdkcqtdm neclsepckn
      961 ggtcsdyvns ytckcqagfd gvhcennine ctesscfngg tcvdginsfs clcpvgftgs
     1021 fclheinecs shpclnegtc vdglgtyrcs cplgytgknc qtlvnlcsrs pcknkgtcvq
     1081 kkaesqclcp sgwagaycdv pnvscdiaas rrgvlvehlc qhsgvcinag nthycqcplg
     1141 ytgsyceeql decasnpcqh gatcsdfigg yrcecvpgyq gvnceyevde cqnqpcqngg
     1201 tcidlvnhfk cscppgtrgm ksslsifhpg hclkl
//
LOCUS       NP_001373430            2133 aa            linear   PRI 24-NOV-2025
DEFINITION  serine/threonine-protein kinase mTOR isoform 2 [Homo sapiens].
ACCESSION   NP_001373430 XP_016856390
VERSION     NP_001373430.1
DBSOURCE    REFSEQ: accession NM_001386501.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2133)
  AUTHORS   Azimzadeh,M., Cheah,P.S. and Ling,K.H.
  TITLE     Brain insulin resistance in Down syndrome: Involvement of
            PI3K-Akt/mTOR axis in early-onset of Alzheimer's disease and its
            potential as a therapeutic target
  JOURNAL   Biochem Biophys Res Commun 733, 150713 (2024)
   PUBMED   39307112
  REMARK    GeneRIF: Brain insulin resistance in Down syndrome: Involvement of
            PI3K-Akt/mTOR axis in early-onset of Alzheimer's disease and its
            potential as a therapeutic target.
            Review article
REFERENCE   2  (residues 1 to 2133)
  AUTHORS   Xue,Z., Liu,J., Xing,W., Mu,F., Wu,Y., Zhao,J., Liu,X., Wang,D.,
            Wang,J., Li,X., Wang,J. and Huang,B.
  TITLE     Hypoxic glioma-derived exosomal miR-25-3p promotes macrophage M2
            polarization by activating the PI3K-AKT-mTOR signaling pathway
  JOURNAL   J Nanobiotechnology 22 (1), 628 (2024)
   PUBMED   39407269
  REMARK    GeneRIF: Hypoxic glioma-derived exosomal miR-25-3p promotes
            macrophage M2 polarization by activating the PI3K-AKT-mTOR
            signaling pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2133)
  AUTHORS   Witucki,L. and Jakubowski,H.
  TITLE     Homocysteine metabolites impair the PHF8/H4K20me1/mTOR/autophagy
            pathway by upregulating the expression of histone demethylase
            PHF8-targeting microRNAs in human vascular endothelial cells and
            mice
  JOURNAL   FASEB J 38 (18), e70072 (2024)
   PUBMED   39323294
  REMARK    GeneRIF: Homocysteine metabolites impair the
            PHF8/H4K20me1/mTOR/autophagy pathway by upregulating the expression
            of histone demethylase PHF8-targeting microRNAs in human vascular
            endothelial cells and mice.
REFERENCE   4  (residues 1 to 2133)
  AUTHORS   Zhan,J., Harwood,F., Have,S.T., Lamond,A., Phillips,A.H.,
            Kriwacki,R.W., Halder,P., Cardone,M. and Grosveld,G.C.
  TITLE     Assembly of mTORC3 Involves Binding of ETV7 to Two Separate
            Sequences in the mTOR Kinase Domain
  JOURNAL   Int J Mol Sci 25 (18), 10042 (2024)
   PUBMED   39337528
  REMARK    GeneRIF: Assembly of mTORC3 Involves Binding of ETV7 to Two
            Separate Sequences in the mTOR Kinase Domain.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2133)
  AUTHORS   Gordon,D.E., Jang,G.M., Bouhaddou,M., Xu,J., Obernier,K.,
            White,K.M., O'Meara,M.J., Rezelj,V.V., Guo,J.Z., Swaney,D.L.,
            Tummino,T.A., Huttenhain,R., Kaake,R.M., Richards,A.L.,
            Tutuncuoglu,B., Foussard,H., Batra,J., Haas,K., Modak,M., Kim,M.,
            Haas,P., Polacco,B.J., Braberg,H., Fabius,J.M., Eckhardt,M.,
            Soucheray,M., Bennett,M.J., Cakir,M., McGregor,M.J., Li,Q.,
            Meyer,B., Roesch,F., Vallet,T., Mac Kain,A., Miorin,L., Moreno,E.,
            Naing,Z.Z.C., Zhou,Y., Peng,S., Shi,Y., Zhang,Z., Shen,W.,
            Kirby,I.T., Melnyk,J.E., Chorba,J.S., Lou,K., Dai,S.A.,
            Barrio-Hernandez,I., Memon,D., Hernandez-Armenta,C., Lyu,J.,
            Mathy,C.J.P., Perica,T., Pilla,K.B., Ganesan,S.J., Saltzberg,D.J.,
            Rakesh,R., Liu,X., Rosenthal,S.B., Calviello,L., Venkataramanan,S.,
            Liboy-Lugo,J., Lin,Y., Huang,X.P., Liu,Y., Wankowicz,S.A., Bohn,M.,
            Safari,M., Ugur,F.S., Koh,C., Savar,N.S., Tran,Q.D., Shengjuler,D.,
            Fletcher,S.J., O'Neal,M.C., Cai,Y., Chang,J.C.J., Broadhurst,D.J.,
            Klippsten,S., Sharp,P.P., Wenzell,N.A., Kuzuoglu-Ozturk,D.,
            Wang,H.Y., Trenker,R., Young,J.M., Cavero,D.A., Hiatt,J.,
            Roth,T.L., Rathore,U., Subramanian,A., Noack,J., Hubert,M.,
            Stroud,R.M., Frankel,A.D., Rosenberg,O.S., Verba,K.A., Agard,D.A.,
            Ott,M., Emerman,M., Jura,N., von Zastrow,M., Verdin,E.,
            Ashworth,A., Schwartz,O., d'Enfert,C., Mukherjee,S., Jacobson,M.,
            Malik,H.S., Fujimori,D.G., Ideker,T., Craik,C.S., Floor,S.N.,
            Fraser,J.S., Gross,J.D., Sali,A., Roth,B.L., Ruggero,D.,
            Taunton,J., Kortemme,T., Beltrao,P., Vignuzzi,M., Garcia-Sastre,A.,
            Shokat,K.M., Shoichet,B.K. and Krogan,N.J.
  TITLE     A SARS-CoV-2 protein interaction map reveals targets for drug
            repurposing
  JOURNAL   Nature 583 (7816), 459-468 (2020)
   PUBMED   32353859
REFERENCE   6  (residues 1 to 2133)
  AUTHORS   Zhou,Y., Hou,Y., Shen,J., Huang,Y., Martin,W. and Cheng,F.
  TITLE     Network-based drug repurposing for novel coronavirus
            2019-nCoV/SARS-CoV-2
  JOURNAL   Cell Discov 6, 14 (2020)
   PUBMED   32194980
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 2133)
  AUTHORS   Chen,J., Zheng,X.F., Brown,E.J. and Schreiber,S.L.
  TITLE     Identification of an 11-kDa FKBP12-rapamycin-binding domain within
            the 289-kDa FKBP12-rapamycin-associated protein and
            characterization of a critical serine residue
  JOURNAL   Proc Natl Acad Sci U S A 92 (11), 4947-4951 (1995)
   PUBMED   7539137
REFERENCE   8  (residues 1 to 2133)
  AUTHORS   Chiu,M.I., Katz,H. and Berlin,V.
  TITLE     RAPT1, a mammalian homolog of yeast Tor, interacts with the
            FKBP12/rapamycin complex
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 12574-12578 (1994)
   PUBMED   7809080
REFERENCE   9  (residues 1 to 2133)
  AUTHORS   Prada,C.E., Raski,C.R., Mirzaa,G., Besterman,A., Krueger,D.A. and
            Liu,A.C.
  TITLE     Smith-Kingsmore Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41264764
REFERENCE   10 (residues 1 to 2133)
  AUTHORS   Grove,J.R., Banerjee,P., Balasubramanyam,A., Coffer,P.J.,
            Price,D.J., Avruch,J. and Woodgett,J.R.
  TITLE     Cloning and expression of two human p70 S6 kinase polypeptides
            differing only at their amino termini
  JOURNAL   Mol Cell Biol 11 (11), 5541-5550 (1991)
   PUBMED   1922062
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049653.7, AL391561.20 and
            AL109811.40.
            
            On Aug 24, 2020 this sequence version replaced XP_016856390.1.
            
            Summary: The protein encoded by this gene belongs to a family of
            phosphatidylinositol kinase-related kinases. These kinases mediate
            cellular responses to stresses such as DNA damage and nutrient
            deprivation. This kinase is a component of two distinct complexes,
            mTORC1, which controls protein synthesis, cell growth and
            proliferation, and mTORC2, which is a regulator of the actin
            cytoskeleton, and promotes cell survival and cell cycle
            progression. This protein acts as the target for the cell-cycle
            arrest and immunosuppressive effects of the FKBP12-rapamycin
            complex. Inhibitors of mTOR are used in organ transplants as
            immunosuppressants, and are being evaluated for their therapeutic
            potential in SARS-CoV-2 infections. Mutations in this gene are
            associated with Smith-Kingsmore syndrome and somatic focal cortical
            dysplasia type II. The ANGPTL7 gene is located in an intron of this
            gene. [provided by RefSeq, Aug 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2260615.1,
                                           SRR14038196.2607050.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: relevant for COVID-19 treatment
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2133
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..2133
                     /product="serine/threonine-protein kinase mTOR isoform 2"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="mammalian target of rapamycin; FK506 binding
                     protein 12-rapamycin associated protein 2; rapamycin and
                     FKBP12 target 1; mechanistic target of rapamycin
                     (serine/threonine kinase); serine/threonine-protein kinase
                     mTOR; FKBP12-rapamycin complex-associated protein 1;
                     FKBP-rapamycin associated protein; rapamycin associated
                     protein FRAP2; rapamycin target protein 1;
                     tyrosine-protein kinase mTOR; FK506-binding protein
                     12-rapamycin complex-associated protein 1"
                     /calculated_mol_wt=241985
     Region          66..2133
                     /region_name="TEL1"
                     /note="Phosphatidylinositol kinase or protein kinase, PI-3
                     family [Signal transduction mechanisms]; COG5032"
                     /db_xref="CDD:227365"
     Region          239..265
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          275..305
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          313..343
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          356..389
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          401..431
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          539..565
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(553..554,557,564..565,594..595,598,601..602,605,
                     634..635,638,641..642,645,675..676,679,682..683,717..718,
                     721,724..725)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          577..605
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          617..646
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          657..683
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          695..726
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          738..764
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..2133
                     /gene="MTOR"
                     /gene_synonym="FRAP; FRAP1; FRAP2; RAFT1; RAPT1; SKS"
                     /coded_by="NM_001386501.1:1261..7662"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:2475"
                     /db_xref="HGNC:HGNC:3942"
                     /db_xref="MIM:601231"
ORIGIN      
        1 mnhvlscvkk ekertaafqa lgllsvavrs efkvylprvl diiraalppk dfahkrqkam
       61 qvdatvftci smlaramgpg iqqdikelle pmlavglspa ltavlydlsr qipqlkkdiq
      121 dgllkmlslv lmhkplrhpg mpkglahqla spglttlpea sdvgsitlal rtlgsfefeg
      181 hsltqfvrhc adhflnsehk eirmeaartc srlltpsihl isghahvvsq tavqvvadvl
      241 skllvvgitd pdpdirycvl aslderfdah laqaenlqal fvalndqvfe irelaictvg
      301 rlssmnpafv mpflrkmliq iltelehsgi grikeqsarm lghlvsnapr lirpymepil
      361 kalilklkdp dpdpnpgvin nvlatigela qvsglemrkw vdelfiiimd mlqdssllak
      421 rqvalwtlgq lvastgyvve pyrkyptlle vllnflkteq nqgtrreair vlgllgaldp
      481 ykhkvnigmi dqsrdasavs lseskssqds sdystsemlv nmgnlpldef ypavsmvalm
      541 rifrdqslsh hhtmvvqait fifkslglkc vqflpqvmpt flnvirvcdg aireflfqql
      601 gmlvsfvksh irpymdeivt lmrefwvmnt siqstiilli eqivvalgge fklylpqlip
      661 hmlrvfmhdn spgrivsikl laaiqlfgan lddylhlllp pivklfdape aplpsrkaal
      721 etvdrltesl dftdyasrii hpivrtldqs pelrstamdt lsslvfqlgk kyqifipmvn
      781 kvlvrhrinh qrydvlicri vkgytladee edpliyqhrm lrsgqgdala sgpvetgpmk
      841 klhvstinlq kawgaarrvs kddwlewlrr lslellkdss spslrscwal aqaynpmard
      901 lfnaafvscw selnedqqde lirsielalt sqdiaevtqt llnlaefmeh sdkgplplrd
      961 dngivllger aakcrayaka lhykelefqk gptpailesl isinnklqqp eaaagvleya
     1021 mkhfgeleiq atwyeklhew edalvaydkk mdtnkddpel mlgrmrclea lgewgqlhqq
     1081 ccekwtlvnd etqakmarma aaaawglgqw dsmeeytcmi prdthdgafy ravlalhqdl
     1141 fslaqqcidk ardlldaelt amagesysra ygamvschml seleeviqyk lvperreiir
     1201 qiwwerlqgc qrivedwqki lmvrslvvsp hedmrtwlky aslcgksgrl alahktlvll
     1261 lgvdpsrqld hplptvhpqv tyaymknmwk sarkidafqh mqhfvqtmqq qaqhaiated
     1321 qqhkqelhkl marcflklge wqlnlqgine stipkvlqyy saatehdrsw ykawhawavm
     1381 nfeavlhykh qnqardekkk lrhasganit nattaattaa tatttasteg snseseaest
     1441 ensptpsplq kkvtedlskt llmytvpavq gffrsislsr gnnlqdtlrv ltlwfdyghw
     1501 pdvnealveg vkaiqidtwl qvipqliari dtprplvgrl ihqlltdigr yhpqaliypl
     1561 tvasksttta rhnaankilk nmcehsntlv qqammvseel irvailwhem whegleeasr
     1621 lyfgernvkg mfevleplha mmergpqtlk etsfnqaygr dlmeaqewcr kymksgnvkd
     1681 ltqawdlyyh vfrriskqlp qltslelqyv spkllmcrdl elavpgtydp nqpiiriqsi
     1741 apslqvitsk qrprkltlmg snghefvfll kghedlrqde rvmqlfglvn tllandptsl
     1801 rknlsiqrya viplstnsgl igwvphcdtl halirdyrek kkillniehr imlrmapdyd
     1861 hltlmqkvev fehavnntag ddlakllwlk spssevwfdr rtnytrslav msmvgyilgl
     1921 gdrhpsnlml drlsgkilhi dfgdcfevam trekfpekip frltrmltna mevtgldgny
     1981 ritchtvmev lrehkdsvma vleafvydpl lnwrlmdtnt kgnkrsrtrt dsysagqsve
     2041 ildgvelgep ahkktgttvp esihsfigdg lvkpealnkk aiqiinrvrd kltgrdfshd
     2101 dtldvptqve llikqatshe nlcqcyigwc pfw
//
LOCUS       NP_000332                685 aa            linear   PRI 24-NOV-2025
DEFINITION  amino acid transporter heavy chain SLC3A1 [Homo sapiens].
ACCESSION   NP_000332
VERSION     NP_000332.2
DBSOURCE    REFSEQ: accession NM_000341.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Liu,D., Zhao,Y., Xue,X., Hou,X., Xu,H., Zhao,X., Tian,Y., Tang,W.,
            Guo,J. and Xu,C.
  TITLE     Novel compound heterozygous pathogenic variants in the SLC3A1 gene
            in a Chinese family with cystinuria
  JOURNAL   BMC Med Genomics 16 (1), 333 (2023)
   PUBMED   38114997
  REMARK    GeneRIF: Novel compound heterozygous pathogenic variants in the
            SLC3A1 gene in a Chinese family with cystinuria.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 685)
  AUTHORS   Wu,C.W., Badreddine,J., Chang,J., Huang,Y.M., Kim,F.J., Wild,T.,
            Tsai,A.C., Meeks,N., Donalisio Da Silva,R., Molina,W.R. and
            Schumacher,F.R.
  TITLE     Population genetics analysis of SLC3A1 and SLC7A9 revealed the
            etiology of cystine stone may be more than what our current genetic
            knowledge can explain
  JOURNAL   Urolithiasis 51 (1), 101 (2023)
   PUBMED   37561200
  REMARK    GeneRIF: Population genetics analysis of SLC3A1 and SLC7A9 revealed
            the etiology of cystine stone may be more than what our current
            genetic knowledge can explain.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 685)
  AUTHORS   Lee,B., Lee,S.Y., Han,D.H. and Park,H.D.
  TITLE     Interpretation of SLC3A1 and SLC7A9 variants in cystinuria
            patients: The significance of the PM3 criterion and protein
            stability
  JOURNAL   Urolithiasis 51 (1), 94 (2023)
   PUBMED   37439839
  REMARK    GeneRIF: Interpretation of SLC3A1 and SLC7A9 variants in cystinuria
            patients: The significance of the PM3 criterion and protein
            stability.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 685)
  AUTHORS   Tkaczyk,M., Gadomska-Prokop,K., Zaluska-Lesniewska,I., Musial,K.,
            Zawadzki,J., Jobs,K., Porowski,T., Rogowska-Kalisz,A., Jander,A.,
            Kirolos,M., Halinski,A., Krzemien,A., Sobieszczanska-Drozdziel,A.,
            Zachwieja,K., Beck,B.B., Sikora,P. and Zaniew,M.
  TITLE     Clinical profile of a Polish cohort of children and young adults
            with cystinuria
  JOURNAL   Ren Fail 43 (1), 62-70 (2021)
   PUBMED   33349102
  REMARK    GeneRIF: Clinical profile of a Polish cohort of children and young
            adults with cystinuria.
REFERENCE   5  (residues 1 to 685)
  AUTHORS   Wu,D., Grund,T.N., Welsch,S., Mills,D.J., Michel,M., Safarian,S.
            and Michel,H.
  TITLE     Structural basis for amino acid exchange by a human heteromeric
            amino acid transporter
  JOURNAL   Proc Natl Acad Sci U S A 117 (35), 21281-21287 (2020)
   PUBMED   32817565
  REMARK    GeneRIF: Structural basis for amino acid exchange by a human
            heteromeric amino acid transporter.
REFERENCE   6  (residues 1 to 685)
  AUTHORS   Calonge,M.J., Volpini,V., Bisceglia,L., Rousaud,F., de Sanctis,L.,
            Beccia,E., Zelante,L., Testar,X., Zorzano,A., Estivill,X. et al.
  TITLE     Genetic heterogeneity in cystinuria: the SLC3A1 gene is linked to
            type I but not to type III cystinuria
  JOURNAL   Proc Natl Acad Sci U S A 92 (21), 9667-9671 (1995)
   PUBMED   7568194
REFERENCE   7  (residues 1 to 685)
  AUTHORS   Gasparini,P., Calonge,M.J., Bisceglia,L., Purroy,J., Dianzani,I.,
            Notarangelo,A., Rousaud,F., Gallucci,M., Testar,X., Ponzone,A. et
            al.
  TITLE     Molecular genetics of cystinuria: identification of four new
            mutations and seven polymorphisms, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 57 (4), 781-788 (1995)
   PUBMED   7573036
REFERENCE   8  (residues 1 to 685)
  AUTHORS   Miyamoto,K., Katai,K., Tatsumi,S., Sone,K., Segawa,H., Yamamoto,H.,
            Taketani,Y., Takada,K., Morita,K., Kanayama,H. et al.
  TITLE     Mutations of the basic amino acid transporter gene associated with
            cystinuria
  JOURNAL   Biochem J 310 (Pt 3) (Pt 3), 951-955 (1995)
   PUBMED   7575432
REFERENCE   9  (residues 1 to 685)
  AUTHORS   Pras,E., Raben,N., Golomb,E., Arber,N., Aksentijevich,I.,
            Schapiro,J.M., Harel,D., Katz,G., Liberman,U., Pras,M. et al.
  TITLE     Mutations in the SLC3A1 transporter gene in cystinuria
  JOURNAL   Am J Hum Genet 56 (6), 1297-1303 (1995)
   PUBMED   7539209
REFERENCE   10 (residues 1 to 685)
  AUTHORS   Spasiano,A., Halbritter,J. and Ferraro,P.M.
  TITLE     Cystinuria
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41264765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC013717.8, BC093626.1 and
            AK223146.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 2, 2008 this sequence version replaced NP_000332.1.
            
            Summary: This gene encodes a type II membrane glycoprotein which is
            one of the components of the renal amino acid transporter which
            transports neutral and basic amino acids in the renal tubule and
            intestinal tract. Mutations and deletions in this gene are
            associated with cystinuria. Alternatively spliced transcript
            variants have been described, but their biological validity has not
            been determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK289636.1, L11696.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260649.11/ ENSP00000260649.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p21"
     Protein         1..685
                     /product="amino acid transporter heavy chain SLC3A1"
                     /note="amino acid transporter 1; solute carrier family 3
                     (cystine, dibasic and neutral amino acid transporters),
                     member 1; neutral and basic amino acid transport protein
                     rBAT; B(0,+)-type amino acid transport protein; solute
                     carrier family 3 (amino acid transporter heavy chain),
                     member 1; solute carrier family 3 (cystine, dibasic and
                     neutral amino acid transporters, activator of cystine,
                     dibasic and neutral amino acid transport), member 1;
                     b(0,+)-type amino acid transporter-related heavy chain"
                     /calculated_mol_wt=78721
     Region          1..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07837.2)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64319; propagated from
                     UniProtKB/Swiss-Prot (Q07837.2)"
     Site            88..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07837.2)"
     Region          116..569
                     /region_name="AmyAc_SLC3A1"
                     /note="Alpha amylase catalytic domain found in Solute
                     Carrier family 3 member 1 proteins; cd11359"
                     /db_xref="CDD:200494"
     Site            order(172,175,212,215,259,278,282,314,384,448..449)
                     /site_type="active"
                     /db_xref="CDD:200494"
     Site            214
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07837.2)"
     Site            261
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07837.2)"
     Site            order(314,384,449)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:200494"
     Site            332
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07837.2)"
     Site            495
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07837.2)"
     Site            513
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07837.2)"
     Site            575
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q07837.2)"
     CDS             1..685
                     /gene="SLC3A1"
                     /gene_synonym="ATR1; CSNU1; D2H; NBAT; RBAT"
                     /coded_by="NM_000341.4:57..2114"
                     /db_xref="CCDS:CCDS1819.1"
                     /db_xref="GeneID:6519"
                     /db_xref="HGNC:HGNC:11025"
                     /db_xref="MIM:104614"
ORIGIN      
        1 maedkskrds iemsmkgcqt nngfvhnedi leqtpdpgss tdnlkhstrg ilgsqepdfk
       61 gvqpyagmpk evlfqfsgqa ryripreilf wltvasvlvl iaatiaiial spkcldwwqe
      121 gpmyqiyprs fkdsnkdgng dlkgiqdkld yitalniktv witsfykssl kdfrygvedf
      181 revdpifgtm edfenlvaai hdkglkliid fipnhtsdkh iwfqlsrtrt gkytdyyiwh
      241 dcthengkti ppnnwlsvyg nsswhfdevr nqcyfhqfmk eqpdlnfrnp dvqeeikeil
      301 rfwltkgvdg fsldavkfll eakhlrdeiq vnktqipdtv tqyselyhdf tttqvgmhdi
      361 vrsfrqtmdq ystepgryrf mgteayaesi drtvmyyglp fiqeadfpfn nylsmldtvs
      421 gnsvyevits wmenmpegkw pnwmiggpds srltsrlgnq yvnvmnmllf tlpgtpityy
      481 geeigmgniv aanlnesydi ntlrskspmq wdnssnagfs easntwlptn sdyhtvnvdv
      541 qktqprsalk lyqdlsllha nelllnrgwf chlrndshyv vytreldgid rifivvlnfg
      601 estllnlhnm isglpakmri rlstnsadkg skvdtsgifl dkgeglifeh ntknllhrqt
      661 afrdrcfvsn racyssvlni lytsc
//
LOCUS       NP_002040                413 aa            linear   PRI 24-NOV-2025
DEFINITION  erythroid transcription factor [Homo sapiens].
ACCESSION   NP_002040
VERSION     NP_002040.1
DBSOURCE    REFSEQ: accession NM_002049.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Wang,C., Hu,M., Yu,K., Liu,W., Hu,A., Kuang,Y., Huang,L.,
            Gajendran,B., Zacksenhaus,E., Xiao,X. and Ben-David,Y.
  TITLE     An intricate regulatory circuit between FLI1 and
            GATA1/GATA2/LDB1/ERG dictates erythroid vs. megakaryocytic
            differentiation
  JOURNAL   Mol Med Rep 29 (6) (2024)
   PUBMED   38695236
  REMARK    GeneRIF: An intricate regulatory circuit between FLI1 and
            GATA1/GATA2/LDB1/ERG dictates erythroid vs. megakaryocytic
            differentiation.
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Sessa,R., Trombetti,S., Bianco,A.L., Amendola,G., Catapano,R.,
            Cesaro,E., Petruzziello,F., D'Armiento,M., Maruotti,G.M., Menna,G.,
            Izzo,P. and Grosso,M.
  TITLE     miR-1202 acts as anti-oncomiR in myeloid leukaemia by
            down-modulating GATA-1S expression
  JOURNAL   Open Biol 14 (2), 230319 (2024)
   PUBMED   38350611
  REMARK    GeneRIF: miR-1202 acts as anti-oncomiR in myeloid leukaemia by
            down-modulating GATA-1S expression.
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Ding,B., Mao,Y., Li,Y., Xin,M., Jiang,S., Hu,X., Xu,Q., Ding,Q. and
            Wang,X.
  TITLE     A novel GATA1 variant p.G229D causing the defect of procoagulant
            platelet formation
  JOURNAL   Thromb Res 234, 39-50 (2024)
   PUBMED   38159323
  REMARK    GeneRIF: A novel GATA1 variant p.G229D causing the defect of
            procoagulant platelet formation.
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Takasaki,K. and Chou,S.T.
  TITLE     GATA1 in Normal and Pathologic Megakaryopoiesis and Platelet
            Development
  JOURNAL   Adv Exp Med Biol 1459, 261-287 (2024)
   PUBMED   39017848
  REMARK    GeneRIF: GATA1 in Normal and Pathologic Megakaryopoiesis and
            Platelet Development.
            Review article
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Erwin,A., Balwani,M. and Desnick,R.J.
  CONSRTM   Porphyrias Consortium of the NIH-Sponsored Rare Diseases Clinical
            Research Network
  TITLE     Congenital Erythropoietic Porphyria
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24027798
REFERENCE   6  (residues 1 to 413)
  AUTHORS   Sieff,C.
  TITLE     DBA Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301769
REFERENCE   7  (residues 1 to 413)
  AUTHORS   Takasaki,K., Kacena,M.A., Raskind,W.H., Weiss,M.J. and Chou,S.T.
  TITLE     GATA1-Related Cytopenia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301538
REFERENCE   8  (residues 1 to 413)
  AUTHORS   Caiulo,A., Nicolis,S., Bianchi,P., Zuffardi,O., Bardoni,B.,
            Maraschio,P., Ottolenghi,S., Camerino,G. and Giglioni,B.
  TITLE     Mapping the gene encoding the human erythroid transcriptional
            factor NFE1-GF1 to Xp11.23
  JOURNAL   Hum Genet 86 (4), 388-390 (1991)
   PUBMED   1999341
REFERENCE   9  (residues 1 to 413)
  AUTHORS   Trainor,C.D., Evans,T., Felsenfeld,G. and Boguski,M.S.
  TITLE     Structure and evolution of a human erythroid transcription factor
  JOURNAL   Nature 343 (6253), 92-96 (1990)
   PUBMED   2104960
REFERENCE   10 (residues 1 to 413)
  AUTHORS   Zon,L.I., Tsai,S.F., Burgess,S., Matsudaira,P., Bruns,G.A. and
            Orkin,S.H.
  TITLE     The major human erythroid DNA-binding protein (GF-1): primary
            sequence and localization of the gene to the X chromosome
  JOURNAL   Proc Natl Acad Sci U S A 87 (2), 668-672 (1990)
   PUBMED   2300555
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X17254.1 and AI057349.1.
            
            Summary: This gene encodes a protein which belongs to the GATA
            family of transcription factors. The protein plays an important
            role in erythroid development by regulating the switch of fetal
            hemoglobin to adult hemoglobin. Mutations in this gene have been
            associated with X-linked dyserythropoietic anemia and
            thrombocytopenia. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X17254.1, M30601.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142363, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376670.9/ ENSP00000365858.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.23"
     Protein         1..413
                     /product="erythroid transcription factor"
                     /note="globin transcription factor 1; transcription factor
                     GATA1; NF-E1 DNA-binding protein; erythroid transcription
                     factor 1; GATA-binding factor 1; nuclear factor, erythroid
                     1"
                     /calculated_mol_wt=42620
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17679; propagated from
                     UniProtKB/Swiss-Prot (P15976.1)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17679; propagated from
                     UniProtKB/Swiss-Prot (P15976.1)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P15976.1)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P15976.1)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16371476; propagated from
                     UniProtKB/Swiss-Prot (P15976.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17679; propagated from
                     UniProtKB/Swiss-Prot (P15976.1)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17679; propagated from
                     UniProtKB/Swiss-Prot (P15976.1)"
     Region          200..330
                     /region_name="Interaction with MED1 and CCAR1.
                     /evidence=ECO:0000269|PubMed:24245781"
                     /note="propagated from UniProtKB/Swiss-Prot (P15976.1)"
     Region          203..247
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cd00202"
                     /db_xref="CDD:238123"
     Region          203..222
                     /region_name="Required for interaction with ZFPM1"
                     /note="propagated from UniProtKB/Swiss-Prot (P15976.1)"
     Site            order(204,207,225,228)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238123"
     Site            order(213..214,216,225..235)
                     /site_type="DNA binding"
                     /note="DNA-binding region [nucleotide binding]"
                     /db_xref="CDD:238123"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000305|PubMed:9859997; propagated from
                     UniProtKB/Swiss-Prot (P15976.1)"
     Site            245
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000305|PubMed:9859997; propagated from
                     UniProtKB/Swiss-Prot (P15976.1)"
     Site            246
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by CREBBP.
                     /evidence=ECO:0000250|UniProtKB:P17679; N6-acetyllysine,
                     by EP300. /evidence=ECO:0000305|PubMed:9859997; propagated
                     from UniProtKB/Swiss-Prot (P15976.1)"
     Region          249..315
                     /region_name="Interaction with CALCOCO1.
                     /evidence=ECO:0000269|PubMed:24245781"
                     /note="propagated from UniProtKB/Swiss-Prot (P15976.1)"
     Site            252
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by CREBBP.
                     /evidence=ECO:0000250|UniProtKB:P17679; propagated from
                     UniProtKB/Swiss-Prot (P15976.1)"
     Region          <268..308
                     /region_name="ZnF_GATA"
                     /note="Zinc finger DNA binding domain; binds specifically
                     to DNA consensus sequence [AT]GATA[AG] promoter elements;
                     a subset of family members may also bind protein;
                     zinc-finger consensus topology is C-X(2)-C-X(17)-C-X(2)-C;
                     cd00202"
                     /db_xref="CDD:238123"
     Site            order(268,270,279..289,305,307..308)
                     /site_type="DNA binding"
                     /note="DNA-binding region [nucleotide binding]"
                     /db_xref="CDD:238123"
     Region          297..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15976.1)"
     Site            308
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P17679; propagated from
                     UniProtKB/Swiss-Prot (P15976.1)"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17679; propagated from
                     UniProtKB/Swiss-Prot (P15976.1)"
     Site            312
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by CREBBP.
                     /evidence=ECO:0000250|UniProtKB:P17679; propagated from
                     UniProtKB/Swiss-Prot (P15976.1)"
     Site            314
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P17679; propagated from
                     UniProtKB/Swiss-Prot (P15976.1)"
     Site            315
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P17679; propagated from
                     UniProtKB/Swiss-Prot (P15976.1)"
     CDS             1..413
                     /gene="GATA1"
                     /gene_synonym="CNSHA9; ERYF1; GATA-1; GF-1; GF1; HAEADA;
                     NF-E1; NFE1; XLANP; XLTDA; XLTT"
                     /coded_by="NM_002049.4:76..1317"
                     /db_xref="CCDS:CCDS14305.1"
                     /db_xref="GeneID:2623"
                     /db_xref="HGNC:HGNC:4170"
                     /db_xref="MIM:305371"
ORIGIN      
        1 mefpglgslg tseplpqfvd palvsstpes gvffpsgpeg ldaaasstap stataaaaal
       61 ayyrdaeayr hspvfqvypl lncmegipgg spyagwaygk tglypastvc ptredsppqa
      121 vedldgkgst sfletlkter lspdlltlgp alpsslpvpn sayggpdfss tffsptgspl
      181 nsaaysspkl rgtlplppce arecvncgat atplwrrdrt ghylcnacgl yhkmngqnrp
      241 lirpkkrliv skragtqctn cqtttttlwr rnasgdpvcn acglyyklhq vnrpltmrkd
      301 giqtrnrkas gkgkkkrgss lggtgaaegp aggfmvvagg sgsgncgeva sgltlgppgt
      361 ahlyqglgpv vlsgpvshlm pfpgpllgsp tgsfptgpmp pttsttvvap lss
//
LOCUS       NP_077719               2471 aa            linear   PRI 24-NOV-2025
DEFINITION  neurogenic locus notch homolog protein 2 isoform 1 preproprotein
            [Homo sapiens].
ACCESSION   NP_077719 XP_946791 XP_950472
VERSION     NP_077719.2
DBSOURCE    REFSEQ: accession NM_024408.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2471)
  AUTHORS   Zhou,X., Zhang,C., Yu,H., Feng,Z., Bai,X., Mei,Y., Li,L., Li,X.,
            Gou,X. and Deng,Y.
  TITLE     The MEF2A/SNHG16/miR-425-5p/NOTCH2 axis induces gemcitabine
            resistance by inhibiting ferroptosis in the starving bladder tumor
            microenvironment
  JOURNAL   Cell Signal 122, 111337 (2024)
   PUBMED   39121977
  REMARK    GeneRIF: The MEF2A/SNHG16/miR-425-5p/NOTCH2 axis induces
            gemcitabine resistance by inhibiting ferroptosis in the starving
            bladder tumor microenvironment.
REFERENCE   2  (residues 1 to 2471)
  AUTHORS   Yang,S., Xiong,L., Yang,G., Xiang,J., Li,L., Kang,L. and Liang,Z.
  TITLE     KLF13 restrains Dll4-muscular Notch2 axis to improve the muscle
            atrophy
  JOURNAL   J Cachexia Sarcopenia Muscle 15 (5), 1869-1882 (2024)
   PUBMED   38973459
  REMARK    GeneRIF: KLF13 restrains Dll4-muscular Notch2 axis to improve the
            muscle atrophy.
REFERENCE   3  (residues 1 to 2471)
  AUTHORS   Ferrandino,M., Cardiero,G., Di Dato,F., Cerrato,Y., Vitagliano,L.,
            Mandato,C., Morisco,F., Spagnuolo,M.I., Iorio,R., Di Taranto,M.D.
            and Fortunato,G.
  TITLE     Association of Very Rare NOTCH2 Variants with Clinical Features of
            Alagille Syndrome
  JOURNAL   Genes (Basel) 15 (8), 1034 (2024)
   PUBMED   39202394
  REMARK    GeneRIF: Association of Very Rare NOTCH2 Variants with Clinical
            Features of Alagille Syndrome.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2471)
  AUTHORS   Lin,H., Fu,L., Zhou,X., Yu,A., Chen,Y., Liao,W., Shu,G., Zhang,L.,
            Tan,L., Liang,H., Wang,Z., Deng,Q., Wang,J., Jin,M., Chen,Z.,
            Wei,J., Cao,J., Chen,W., Li,X., Li,P., Lu,J. and Luo,J.
  TITLE     LRP1 induces anti-PD-1 resistance by modulating the
            DLL4-NOTCH2-CCL2 axis and redirecting M2-like macrophage
            polarisation in bladder cancer
  JOURNAL   Cancer Lett 593, 216807 (2024)
   PUBMED   38462037
  REMARK    GeneRIF: LRP1 induces anti-PD-1 resistance by modulating the
            DLL4-NOTCH2-CCL2 axis and redirecting M2-like macrophage
            polarisation in bladder cancer.
REFERENCE   5  (residues 1 to 2471)
  AUTHORS   Li,M., He,W., Wang,F., Zhang,P., Zhang,X., Li,Q., Liu,T. and Li,Y.
  TITLE     High expression of NOTCH2 in gastric adenocarcinoma: A novel early
            diagnostic target
  JOURNAL   J Gastroenterol Hepatol 39 (6), 1115-1122 (2024)
   PUBMED   38577711
  REMARK    GeneRIF: High expression of NOTCH2 in gastric adenocarcinoma: A
            novel early diagnostic target.
REFERENCE   6  (residues 1 to 2471)
  AUTHORS   Hsieh,J.J., Nofziger,D.E., Weinmaster,G. and Hayward,S.D.
  TITLE     Epstein-Barr virus immortalization: Notch2 interacts with CBF1 and
            blocks differentiation
  JOURNAL   J Virol 71 (3), 1938-1945 (1997)
   PUBMED   9032325
REFERENCE   7  (residues 1 to 2471)
  AUTHORS   Katsanis,N., Fitzgibbon,J. and Fisher,E.M.
  TITLE     Paralogy mapping: identification of a region in the human MHC
            triplicated onto human chromosomes 1 and 9 allows the prediction
            and isolation of novel PBX and NOTCH loci
  JOURNAL   Genomics 35 (1), 101-108 (1996)
   PUBMED   8661110
REFERENCE   8  (residues 1 to 2471)
  AUTHORS   Larsson,C., Lardelli,M., White,I. and Lendahl,U.
  TITLE     The human NOTCH1, 2, and 3 genes are located at chromosome
            positions 9q34, 1p13-p11, and 19p13.2-p13.1 in regions of
            neoplasia-associated translocation
  JOURNAL   Genomics 24 (2), 253-258 (1994)
   PUBMED   7698746
REFERENCE   9  (residues 1 to 2471)
  AUTHORS   Spinner,N.B., Loomes,K.M., Krantz,I.D. and Gilbert,M.A.
  TITLE     Alagille Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301450
REFERENCE   10 (residues 1 to 2471)
  AUTHORS   Stifani,S., Blaumueller,C.M., Redhead,N.J., Hill,R.E. and
            Artavanis-Tsakonas,S.
  TITLE     Human homologs of a Drosophila Enhancer of split gene product
            define a novel family of nuclear proteins
  JOURNAL   Nat Genet 2 (2), 119-127 (1992)
   PUBMED   1303260
  REMARK    Erratum:[Nat Genet. 1992 Dec;2(4):343. doi: 10.1038/ng1292-343a.
            PMID: 1303292]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB290699.1, BC071562.1,
            AF315356.1 and AL133036.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_946791.1, XP_950472.1, NP_077719.1.
            
            Summary: This gene encodes a member of the Notch family. Members of
            this Type 1 transmembrane protein family share structural
            characteristics including an extracellular domain consisting of
            multiple epidermal growth factor-like (EGF) repeats, and an
            intracellular domain consisting of multiple, different domain
            types. Notch family members play a role in a variety of
            developmental processes by controlling cell fate decisions. The
            Notch signaling network is an evolutionarily conserved
            intercellular signaling pathway which regulates interactions
            between physically adjacent cells. In Drosophilia, notch
            interaction with its cell-bound ligands (delta, serrate)
            establishes an intercellular signaling pathway that plays a key
            role in development. Homologues of the notch-ligands have also been
            identified in human, but precise interactions between these ligands
            and the human notch homologues remain to be determined. This
            protein is cleaved in the trans-Golgi network, and presented on the
            cell surface as a heterodimer. This protein functions as a receptor
            for membrane bound ligands, and may play a role in vascular, renal
            and hepatic development. Two transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jan
            2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2645516.1,
                                           SRR11853559.2248.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256646.7/ ENSP00000256646.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2471
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..2471
                     /product="neurogenic locus notch homolog protein 2 isoform
                     1 preproprotein"
                     /note="Notch homolog 2; notch 2"
                     /calculated_mol_wt=262752
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2673
     proprotein      26..2471
                     /product="neurogenic locus notch homolog protein 2 isoform
                     1 proprotein"
                     /calculated_mol_wt=262752
     mat_peptide     26..1677
                     /product="neurogenic locus notch homolog protein 2 isoform
                     1 N-terminal extracellular peptide"
                     /calculated_mol_wt=177531
     Region          182..218
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(182,185,200)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          260..296
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(260,263,277)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          298..335
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(298,301,317)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          415..454
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(415,418,435)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          456..492
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(456,459,473)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          495..530
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          532..568
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(532,535,549)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          570..604
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(570,573,586)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          608..643
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          645..679
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(645,648,661)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          682..717
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(682,685,699)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          757..793
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(757,760,774)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          795..831
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(795,798,812)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          873..909
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(873,876,890)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          911..947
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(911,914,928)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          949..985
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(949,952,966)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          987..1022
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(987,990,1004)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1026..1061
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1117..1147
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1151..1185
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1188..1223
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1225..1262
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1225,1228,1243)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1264..1302
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1264,1267,1283)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          <1312..1343
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          1423..1456
                     /region_name="Notch"
                     /note="LNR domain; pfam00066"
                     /db_xref="CDD:459658"
     Region          1463..1497
                     /region_name="Notch"
                     /note="LNR domain; pfam00066"
                     /db_xref="CDD:459658"
     Region          1501..1534
                     /region_name="Notch"
                     /note="LNR domain; pfam00066"
                     /db_xref="CDD:459658"
     Region          1539..1594
                     /region_name="NOD"
                     /note="NOTCH protein; pfam06816"
                     /db_xref="CDD:462014"
     Region          1618..1673
                     /region_name="NODP"
                     /note="NOTCH protein; pfam07684"
                     /db_xref="CDD:462229"
     Region          1659..1740
                     /region_name="JMTM_Notch2"
                     /note="juxtamembrane and transmembrane (JMTM) domain found
                     in neurogenic locus notch homolog protein 2 (Notch2) and
                     similar proteins; cd21703"
                     /db_xref="CDD:411986"
     Site            order(1661..1663,1666..1668,1682..1683,1685,1687..1703)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:411986"
     mat_peptide     1678..2471
                     /product="neurogenic locus notch homolog protein 2 isoform
                     1 C-terminal transmembrane and cytoplasmic peptide"
                     /calculated_mol_wt=85238
     Region          1827..1874
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <1851..2066
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1877..1907
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1943,1945,1949..1950,1953..1955,1957..1958,1962,
                     1965,1974,1976,1978,1982..1983,1986..1988,1990..1991,1995,
                     1998,2007,2009,2011,2015..2016,2019..2021,2023..2024,2028,
                     2031,2040)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1943..1974
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1976..2007
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          2009..2040
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          2068..2422
                     /region_name="DUF5585"
                     /note="Family of unknown function (DUF5585); pfam17823"
                     /db_xref="CDD:465521"
     CDS             1..2471
                     /gene="NOTCH2"
                     /gene_synonym="AGS2; HJCYS; hN2"
                     /coded_by="NM_024408.4:257..7672"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS908.1"
                     /db_xref="GeneID:4853"
                     /db_xref="HGNC:HGNC:7882"
                     /db_xref="MIM:600275"
ORIGIN      
        1 mpalrpallw allalwlcca apahalqcrd gyepcvnegm cvtyhngtgy ckcpegflge
       61 ycqhrdpcek nrcqnggtcv aqamlgkatc rcasgftged cqystshpcf vsrpclnggt
      121 chmlsrdtye ctcqvgftgk ecqwtdacls hpcangstct tvanqfsckc ltgftgqkce
      181 tdvnecdipg hcqhggtcln lpgsyqcqcp qgftgqycds lyvpcapspc vnggtcrqtg
      241 dftfecnclp gfegstcern iddcpnhrcq nggvcvdgvn tyncrcppqw tgqfctedvd
      301 ecllqpnacq nggtcanrng gygcvcvngw sgddcsenid dcafasctpg stcidrvasf
      361 scmcpegkag llchlddaci snpchkgalc dtnplngqyi ctcpqgykga dctedvdeca
      421 mansnpceha gkcvntdgaf hceclkgyag prcemdinec hsdpcqndat cldkiggftc
      481 lcmpgfkgvh celeinecqs npcvnngqcv dkvnrfqclc ppgftgpvcq ididdcsstp
      541 clngakcidh pngyecqcat gftgvlceen idncdpdpch hgqcqdgids ytcicnpgym
      601 gaicsdqide cysspclndg rcidlvngyq cncqpgtsgv nceinfddca snpcihgicm
      661 dginryscvc spgftgqrcn ididecasnp crkgatcing vngfrcicpe gphhpscysq
      721 vneclsnpci hgnctgglsg ykclcdagwv gincevdkne clsnpcqngg tcdnlvngyr
      781 ctckkgfkgy ncqvnideca snpclnqgtc fddisgytch cvlpytgknc qtvlapcspn
      841 pcenaavcke spnfesytcl capgwqgqrc tididecisk pcmnhglchn tqgsymcecp
      901 pgfsgmdcee diddclanpc qnggscmdgv ntfsclclpg ftgdkcqtdm neclsepckn
      961 ggtcsdyvns ytckcqagfd gvhcennine ctesscfngg tcvdginsfs clcpvgftgs
     1021 fclheinecs shpclnegtc vdglgtyrcs cplgytgknc qtlvnlcsrs pcknkgtcvq
     1081 kkaesqclcp sgwagaycdv pnvscdiaas rrgvlvehlc qhsgvcinag nthycqcplg
     1141 ytgsyceeql decasnpcqh gatcsdfigg yrcecvpgyq gvnceyevde cqnqpcqngg
     1201 tcidlvnhfk cscppgtrgl lceeniddca rgphclnggq cmdriggysc rclpgfager
     1261 cegdinecls npcssegsld ciqltndylc vcrsaftgrh cetfvdvcpq mpclnggtca
     1321 vasnmpdgfi crcppgfsga rcqsscgqvk crkgeqcvht asgprcfcps prdcesgcas
     1381 spcqhggsch pqrqppyysc qcappfsgsr celytappst ppatclsqyc adkardgvcd
     1441 eacnshacqw dggdcsltme npwancsspl pcwdyinnqc delcntvecl fdnfecqgns
     1501 ktckydkyca dhfkdnhcdq gcnseecgwd gldcaadqpe nlaegtlviv vlmppeqllq
     1561 darsflralg tllhtnlrik rdsqgelmvy pyygeksaam kkqrmtrrsl pgeqeqevag
     1621 skvfleidnr qcvqdsdhcf kntdaaaall ashaiqgtls yplvsvvses ltpertqlly
     1681 llavavviil fiillgvima krkrkhgslw lpegftlrrd asnhkrrepv gqdavglknl
     1741 svqvseanli gtgtsehwvd degpqpkkvk aedeallsee ddpidrrpwt qqhleaadir
     1801 rtpslaltpp qaeqevdvld vnvrgpdgct plmlaslrgg ssdlsdeded aedssaniit
     1861 dlvyqgaslq aqtdrtgema lhlaarysra daakrlldag adanaqdnmg rcplhaavaa
     1921 daqgvfqili rnrvtdldar mndgttplil aarlavegmv aelincqadv navddhgksa
     1981 lhwaaavnnv eatllllkng anrdmqdnke etplflaare gsyeaakill dhfanrditd
     2041 hmdrlprdva rdrmhhdivr lldeynvtps ppgtvltsal spvicgpnrs flslkhtpmg
     2101 kksrrpsaks tmptslpnla keakdakgsr rkkslsekvq lsessvtlsp vdslesphty
     2161 vsdttsspmi tspgilqasp npmlataapp apvhaqhals fsnlhemqpl ahgastvlps
     2221 vsqllshhhi vspgsgsags lsrlhpvpvp adwmnrmevn etqynemfgm vlapaegthp
     2281 giapqsrppe gkhittprep lppivtfqli pkgsiaqpag apqpqstcpp avagplptmy
     2341 qipemarlps vafptammpq qdgqvaqtil payhpfpasv gkyptppsqh syassnaaer
     2401 tpshsghlqg ehpyltpspe spdqwssssp hsasdwsdvt tsptpggagg gqrgpgthms
     2461 epphnnmqvy a
//
LOCUS       NP_001119807             487 aa            linear   PRI 24-NOV-2025
DEFINITION  B(0,+)-type amino acid transporter 1 [Homo sapiens].
ACCESSION   NP_001119807
VERSION     NP_001119807.1
DBSOURCE    REFSEQ: accession NM_001126335.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Wu,C.W., Badreddine,J., Chang,J., Huang,Y.M., Kim,F.J., Wild,T.,
            Tsai,A.C., Meeks,N., Donalisio Da Silva,R., Molina,W.R. and
            Schumacher,F.R.
  TITLE     Population genetics analysis of SLC3A1 and SLC7A9 revealed the
            etiology of cystine stone may be more than what our current genetic
            knowledge can explain
  JOURNAL   Urolithiasis 51 (1), 101 (2023)
   PUBMED   37561200
  REMARK    GeneRIF: Population genetics analysis of SLC3A1 and SLC7A9 revealed
            the etiology of cystine stone may be more than what our current
            genetic knowledge can explain.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Lee,B., Lee,S.Y., Han,D.H. and Park,H.D.
  TITLE     Interpretation of SLC3A1 and SLC7A9 variants in cystinuria
            patients: The significance of the PM3 criterion and protein
            stability
  JOURNAL   Urolithiasis 51 (1), 94 (2023)
   PUBMED   37439839
  REMARK    GeneRIF: Interpretation of SLC3A1 and SLC7A9 variants in cystinuria
            patients: The significance of the PM3 criterion and protein
            stability.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Baba,H., Kanda,M., Sawaki,K., Nakamura,S., Ueda,S., Shimizu,D.,
            Koike,M., Kodera,Y. and Fujii,T.
  TITLE     SLC7A9 as a Potential Biomarker for Lymph Node Metastasis of
            Esophageal Squamous Cell Carcinoma
  JOURNAL   Ann Surg Oncol 29 (4), 2699-2709 (2022)
   PUBMED   34773193
  REMARK    GeneRIF: SLC7A9 as a Potential Biomarker for Lymph Node Metastasis
            of Esophageal Squamous Cell Carcinoma.
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Tkaczyk,M., Gadomska-Prokop,K., Zaluska-Lesniewska,I., Musial,K.,
            Zawadzki,J., Jobs,K., Porowski,T., Rogowska-Kalisz,A., Jander,A.,
            Kirolos,M., Halinski,A., Krzemien,A., Sobieszczanska-Drozdziel,A.,
            Zachwieja,K., Beck,B.B., Sikora,P. and Zaniew,M.
  TITLE     Clinical profile of a Polish cohort of children and young adults
            with cystinuria
  JOURNAL   Ren Fail 43 (1), 62-70 (2021)
   PUBMED   33349102
  REMARK    GeneRIF: Clinical profile of a Polish cohort of children and young
            adults with cystinuria.
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Wu,D., Grund,T.N., Welsch,S., Mills,D.J., Michel,M., Safarian,S.
            and Michel,H.
  TITLE     Structural basis for amino acid exchange by a human heteromeric
            amino acid transporter
  JOURNAL   Proc Natl Acad Sci U S A 117 (35), 21281-21287 (2020)
   PUBMED   32817565
  REMARK    GeneRIF: Structural basis for amino acid exchange by a human
            heteromeric amino acid transporter.
REFERENCE   6  (residues 1 to 487)
  AUTHORS   Feliubadalo,L., Font,M., Purroy,J., Rousaud,F., Estivill,X.,
            Nunes,V., Golomb,E., Centola,M., Aksentijevich,I., Kreiss,Y.,
            Goldman,B., Pras,M., Kastner,D.L., Pras,E., Gasparini,P.,
            Bisceglia,L., Beccia,E., Gallucci,M., de Sanctis,L., Ponzone,A.,
            Rizzoni,G.F., Zelante,L., Bassi,M.T., George,A.L. Jr., Manzoni,M.,
            De Grandi,A., Riboni,M., Endsley,J.K., Ballabio,A., Borsani,G.,
            Reig,N., Fernandez,E., Estevez,R., Pineda,M., Torrents,D.,
            Camps,M., Lloberas,J., Zorzano,A. and Palacin,M.
  CONSRTM   International Cystinuria Consortium
  TITLE     Non-type I cystinuria caused by mutations in SLC7A9, encoding a
            subunit (bo,+AT) of rBAT
  JOURNAL   Nat Genet 23 (1), 52-57 (1999)
   PUBMED   10471498
REFERENCE   7  (residues 1 to 487)
  AUTHORS   Wartenfeld,R., Golomb,E., Katz,G., Bale,S.J., Goldman,B., Pras,M.,
            Kastner,D.L. and Pras,E.
  TITLE     Molecular analysis of cystinuria in Libyan Jews: exclusion of the
            SLC3A1 gene and mapping of a new locus on 19q
  JOURNAL   Am J Hum Genet 60 (3), 617-624 (1997)
   PUBMED   9042922
REFERENCE   8  (residues 1 to 487)
  AUTHORS   Bisceglia,L., Calonge,M.J., Totaro,A., Feliubadalo,L.,
            Melchionda,S., Garcia,J., Testar,X., Gallucci,M., Ponzone,A.,
            Zelante,L., Zorzano,A., Estivill,X., Gasparini,P., Nunes,V. and
            Palacin,M.
  TITLE     Localization, by linkage analysis, of the cystinuria type III gene
            to chromosome 19q13.1
  JOURNAL   Am J Hum Genet 60 (3), 611-616 (1997)
   PUBMED   9042921
REFERENCE   9  (residues 1 to 487)
  AUTHORS   Chillaron,J., Estevez,R., Mora,C., Wagner,C.A., Suessbrich,H.,
            Lang,F., Gelpi,J.L., Testar,X., Busch,A.E., Zorzano,A. and
            Palacin,M.
  TITLE     Obligatory amino acid exchange via systems bo,+-like and y+L-like.
            A tertiary active transport mechanism for renal reabsorption of
            cystine and dibasic amino acids
  JOURNAL   J Biol Chem 271 (30), 17761-17770 (1996)
   PUBMED   8663357
REFERENCE   10 (residues 1 to 487)
  AUTHORS   Spasiano,A., Halbritter,J. and Ferraro,P.M.
  TITLE     Cystinuria
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41264765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP276659.1, AK313708.1 and
            CK300669.1.
            
            Summary: This gene encodes a protein that belongs to a family of
            light subunits of amino acid transporters. This protein plays a
            role in the high-affinity and sodium-independent transport of
            cystine and neutral and dibasic amino acids, and appears to
            function in the reabsorption of cystine in the kidney tubule.
            Mutations in this gene cause non-type I cystinuria, a disease that
            leads to cystine stones in the urinary system due to impaired
            transport of cystine and dibasic amino acids. Alternate transcript
            variants, which encode the same protein, have been found for this
            gene. [provided by RefSeq, Jul 2011].
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1, 2, and 3 encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB033548.1, AK313708.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.11"
     Protein         1..487
                     /product="B(0,+)-type amino acid transporter 1"
                     /note="solute carrier family 7 (cationic amino acid
                     transporter, y+ system), member 9; glycoprotein-associated
                     amino acid transporter b0,+AT1; b(0,+)AT; cystinuria type
                     3; solute carrier family 7 (glycoprotein-associated amino
                     acid transporter light chain, bo,+ system), member 9;
                     solute carrier family 7 (amino acid transporter light
                     chain, bo,+ system), member 9"
                     /calculated_mol_wt=53351
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P82252; propagated from
                     UniProtKB/Swiss-Prot (P82251.1)"
     Region          26..484
                     /region_name="2A0308"
                     /note="L-type amino acid transporter; TIGR00911"
                     /db_xref="CDD:273332"
     Site            32..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            63..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            111..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            148..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            170..193
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            252..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            303..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            352..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            371..391
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            411..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     Site            435..450
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P82251.1)"
     CDS             1..487
                     /gene="SLC7A9"
                     /gene_synonym="BAT1; CSNU3"
                     /coded_by="NM_001126335.2:108..1571"
                     /db_xref="CCDS:CCDS12425.1"
                     /db_xref="GeneID:11136"
                     /db_xref="HGNC:HGNC:11067"
                     /db_xref="MIM:604144"
ORIGIN      
        1 mgdtglrkrr edeksiqsqe pkttslqkel glisgisiiv gtiigsgifv spksvlsnte
       61 avgpcliiwa acgvlatlga lcfaelgtmi tksggeypyl meaygpipay lfswaslivi
      121 kptsfaiicl sfseyvcapf yvgckppqiv vkclaaaail fistvnslsv rlgsyvqnif
      181 taaklvivai iiisglvlla qgntknfdns fegaqlsvga islafynglw aydgwnqlny
      241 iteelrnpyr nlplaiiigi plvtacyilm nvsyftvmta tellqsqava vtfgdrvlyp
      301 aswivplfva fstigaangt cftagrliyv agreghmlkv lsyisvrrlt papaiifygi
      361 iatiyiipgd inslvnyfsf aawlfyglti lglivmrftr kelerpikvp vvipvlmtli
      421 svflvlapii skptweylyc vlfilsgllf yflfvhykfg waqkiskpit mhlqmlmevv
      481 ppeedpe
//
LOCUS       NP_001306977             718 aa            linear   PRI 25-NOV-2025
DEFINITION  FIGNL1-interacting regulator of recombination and mitosis isoform 2
            [Homo sapiens].
ACCESSION   NP_001306977 XP_005245376
VERSION     NP_001306977.1
DBSOURCE    REFSEQ: accession NM_001320048.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Tischler,J.D., Tsuchida,H., Bosire,R., Oda,T.T., Park,A. and
            Adeyemi,R.O.
  TITLE     FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin association
            to promote viability after replication stress
  JOURNAL   Nat Commun 15 (1), 866 (2024)
   PUBMED   38286805
  REMARK    GeneRIF: FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin
            association to promote viability after replication stress.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 718)
  AUTHORS   Zhou,Z., Yang,H., Liang,X., Zhou,T., Zhang,T., Yang,Y., Wang,J. and
            Wang,W.
  TITLE     C1orf112 teams up with FIGNL1 to facilitate RAD51 filament
            disassembly and DNA interstrand cross-link repair
  JOURNAL   Cell Rep 42 (8), 112907 (2023)
   PUBMED   37515771
REFERENCE   3  (residues 1 to 718)
  AUTHORS   Stok,C., Tsaridou,S., van den Tempel,N., Everts,M., Wierenga,E.,
            Bakker,F.J., Kok,Y., Alves,I.T., Jae,L.T., Raas,M.W.D., Huis In 't
            Veld,P.J., de Boer,H.R., Bhattacharya,A., Karanika,E., Warner,H.,
            Chen,M., van de Kooij,B., Dessapt,J., Ter Morsche,L.,
            Perepelkina,P., Fradet-Turcotte,A., Guryev,V., Tromer,E.C.,
            Chan,K.L., Fehrmann,R.S.N. and van Vugt,M.A.T.M.
  TITLE     FIRRM/C1orf112 is synthetic lethal with PICH and mediates RAD51
            dynamics
  JOURNAL   Cell Rep 42 (7), 112668 (2023)
   PUBMED   37347663
REFERENCE   4  (residues 1 to 718)
  AUTHORS   Mazouzi,A., Moser,S.C., Abascal,F., van den Broek,B., Del Castillo
            Velasco-Herrera,M., van der Heijden,I., Hekkelman,M., Drenth,A.P.,
            van der Burg,E., Kroese,L.J., Jalink,K., Adams,D.J., Jonkers,J. and
            Brummelkamp,T.R.
  TITLE     FIRRM/C1orf112 mediates resolution of homologous recombination
            intermediates in response to DNA interstrand crosslinks
  JOURNAL   Sci Adv 9 (22), eadf4409 (2023)
   PUBMED   37256941
REFERENCE   5  (residues 1 to 718)
  AUTHORS   Zhang,Z., Tan,Z., Lv,Q., Wang,L., Yu,K., Yang,H., Liang,H., Lu,T.,
            Ji,Y., Chen,J., He,W., Chen,Z., Chen,S. and Shen,X.
  TITLE     High Expression of C1ORF112 Predicts a Poor Outcome: A Potential
            Target for the Treatment of Low-Grade Gliomas
  JOURNAL   Front Genet 12, 710944 (2021)
   PUBMED   34880897
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 718)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 718)
  AUTHORS   van Dam,S., Cordeiro,R., Craig,T., van Dam,J., Wood,S.H. and de
            Magalhaes,J.P.
  TITLE     GeneFriends: an online co-expression analysis tool to identify
            novel gene targets for aging and complex diseases
  JOURNAL   BMC Genomics 13, 535 (2012)
   PUBMED   23039964
  REMARK    GeneRIF: Knockdown of C1orf112 by siRNA in HeLa cells significantly
            suppressed their growth.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 718)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 718)
  AUTHORS   Cheung,C.L., Chan,B.Y., Chan,V., Ikegawa,S., Kou,I., Ngai,H.,
            Smith,D., Luk,K.D., Huang,Q.Y., Mori,S., Sham,P.C. and Kung,A.W.
  TITLE     Pre-B-cell leukemia homeobox 1 (PBX1) shows functional and possible
            genetic association with bone mineral density variation
  JOURNAL   Hum Mol Genet 18 (4), 679-687 (2009)
   PUBMED   19064610
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 718)
  AUTHORS   Fedorova,N.I.
  TITLE     [Remote results of health resort treatment of chronic prostatitis]
  JOURNAL   Vestn Dermatol Venerol 46 (2), 71-73 (1972)
   PUBMED   4260926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK303296.1, AK001568.1, BC091516.1 and AL031297.4.
            
            On Feb 10, 2016 this sequence version replaced XP_005245376.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001568.1, SRR1803616.29842.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.2"
     Protein         1..718
                     /product="FIGNL1-interacting regulator of recombination
                     and mitosis isoform 2"
                     /note="uncharacterized protein C1orf112; associating
                     protein with POLO1; Fidgetin-like-1 interacting protein;
                     POLO1-associating protein"
                     /calculated_mol_wt=81187
     Region          41..593
                     /region_name="DUF4487"
                     /note="Domain of unknown function (DUF4487); pfam14868"
                     /db_xref="CDD:464352"
     CDS             1..718
                     /gene="FIRRM"
                     /gene_synonym="Apolo1; C1orf112; FLIP; MEICA1"
                     /coded_by="NM_001320048.2:517..2673"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:55732"
                     /db_xref="HGNC:HGNC:25565"
                     /db_xref="MIM:621430"
ORIGIN      
        1 melldmvcmd plvddnddil nmvivihsll dicsvissmd hafhantwkf iikqslkhqs
       61 iiksqlkhkd iitslcedil fsfhsclqla eqmtqsdaqd nadyrlfqkt lklcrffans
      121 llhyakeflp flsdscctlh qlylqihskf ppslyatris kahqeeiaga flvtldplis
      181 qlltfqpfmq vvldskldlp celqfpqcll lvvvmdklps qpkevqtlwc tdsqvsettt
      241 risllkavfy sfeqcsgels lpvhlqglks kgkaevavtl yqhvcvhlct fitsfhpslf
      301 aeldaallna vlsanmitsl lamdawcfla rygtaelcah hvtivahlik scpgecyqli
      361 nlsillkrlf ffmapphqle fiqkfspkea enlplwqhis fqalppelre qtvhevttvg
      421 taecrkwlsr srtlgelesl ntvlsallav cnsagealdt gkqtaiievv sqlwaflnik
      481 qvadqpyvqq tfslllpllg ffiqtldpkl ilqavtlqts llklelpdyv rlamldfvss
      541 lgklfipeai qdrilpnlsc mfallladrs wlleqhtlea ftqfaegtnh eeivpqclss
      601 eetknkvvsf lektgfvdet eaakvervkq ekgifwepfa nvtveeakrs slqpyakrar
      661 qefpweeeyr salhtiagal eatesllqkg papawlsmem ealqermdkl kryihtlg
//
LOCUS       NP_001353702             530 aa            linear   PRI 25-NOV-2025
DEFINITION  FIGNL1-interacting regulator of recombination and mitosis isoform 5
            [Homo sapiens].
ACCESSION   NP_001353702
VERSION     NP_001353702.1
DBSOURCE    REFSEQ: accession NM_001366773.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Tischler,J.D., Tsuchida,H., Bosire,R., Oda,T.T., Park,A. and
            Adeyemi,R.O.
  TITLE     FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin association
            to promote viability after replication stress
  JOURNAL   Nat Commun 15 (1), 866 (2024)
   PUBMED   38286805
  REMARK    GeneRIF: FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin
            association to promote viability after replication stress.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Zhou,Z., Yang,H., Liang,X., Zhou,T., Zhang,T., Yang,Y., Wang,J. and
            Wang,W.
  TITLE     C1orf112 teams up with FIGNL1 to facilitate RAD51 filament
            disassembly and DNA interstrand cross-link repair
  JOURNAL   Cell Rep 42 (8), 112907 (2023)
   PUBMED   37515771
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Stok,C., Tsaridou,S., van den Tempel,N., Everts,M., Wierenga,E.,
            Bakker,F.J., Kok,Y., Alves,I.T., Jae,L.T., Raas,M.W.D., Huis In 't
            Veld,P.J., de Boer,H.R., Bhattacharya,A., Karanika,E., Warner,H.,
            Chen,M., van de Kooij,B., Dessapt,J., Ter Morsche,L.,
            Perepelkina,P., Fradet-Turcotte,A., Guryev,V., Tromer,E.C.,
            Chan,K.L., Fehrmann,R.S.N. and van Vugt,M.A.T.M.
  TITLE     FIRRM/C1orf112 is synthetic lethal with PICH and mediates RAD51
            dynamics
  JOURNAL   Cell Rep 42 (7), 112668 (2023)
   PUBMED   37347663
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Mazouzi,A., Moser,S.C., Abascal,F., van den Broek,B., Del Castillo
            Velasco-Herrera,M., van der Heijden,I., Hekkelman,M., Drenth,A.P.,
            van der Burg,E., Kroese,L.J., Jalink,K., Adams,D.J., Jonkers,J. and
            Brummelkamp,T.R.
  TITLE     FIRRM/C1orf112 mediates resolution of homologous recombination
            intermediates in response to DNA interstrand crosslinks
  JOURNAL   Sci Adv 9 (22), eadf4409 (2023)
   PUBMED   37256941
REFERENCE   5  (residues 1 to 530)
  AUTHORS   Zhang,Z., Tan,Z., Lv,Q., Wang,L., Yu,K., Yang,H., Liang,H., Lu,T.,
            Ji,Y., Chen,J., He,W., Chen,Z., Chen,S. and Shen,X.
  TITLE     High Expression of C1ORF112 Predicts a Poor Outcome: A Potential
            Target for the Treatment of Low-Grade Gliomas
  JOURNAL   Front Genet 12, 710944 (2021)
   PUBMED   34880897
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 530)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 530)
  AUTHORS   van Dam,S., Cordeiro,R., Craig,T., van Dam,J., Wood,S.H. and de
            Magalhaes,J.P.
  TITLE     GeneFriends: an online co-expression analysis tool to identify
            novel gene targets for aging and complex diseases
  JOURNAL   BMC Genomics 13, 535 (2012)
   PUBMED   23039964
  REMARK    GeneRIF: Knockdown of C1orf112 by siRNA in HeLa cells significantly
            suppressed their growth.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 530)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 530)
  AUTHORS   Cheung,C.L., Chan,B.Y., Chan,V., Ikegawa,S., Kou,I., Ngai,H.,
            Smith,D., Luk,K.D., Huang,Q.Y., Mori,S., Sham,P.C. and Kung,A.W.
  TITLE     Pre-B-cell leukemia homeobox 1 (PBX1) shows functional and possible
            genetic association with bone mineral density variation
  JOURNAL   Hum Mol Genet 18 (4), 679-687 (2009)
   PUBMED   19064610
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 530)
  AUTHORS   Fedorova,N.I.
  TITLE     [Remote results of health resort treatment of chronic prostatitis]
  JOURNAL   Vestn Dermatol Venerol 46 (2), 71-73 (1972)
   PUBMED   4260926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL021940.1 and AL031297.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.137379.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.2"
     Protein         1..530
                     /product="FIGNL1-interacting regulator of recombination
                     and mitosis isoform 5"
                     /note="uncharacterized protein C1orf112; associating
                     protein with POLO1; Fidgetin-like-1 interacting protein;
                     POLO1-associating protein"
                     /calculated_mol_wt=59566
     Region          <1..405
                     /region_name="DUF4487"
                     /note="Domain of unknown function (DUF4487); pfam14868"
                     /db_xref="CDD:464352"
     CDS             1..530
                     /gene="FIRRM"
                     /gene_synonym="Apolo1; C1orf112; FLIP; MEICA1"
                     /coded_by="NM_001366773.1:979..2571"
                     /note="isoform 5 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS86030.1"
                     /db_xref="GeneID:55732"
                     /db_xref="HGNC:HGNC:25565"
                     /db_xref="MIM:621430"
ORIGIN      
        1 mqvvldskld lpcelqfpqc lllvvvmdkl psqpkevqtl wctdsqvset ttrisllkav
       61 fysfeqcsge lslpvhlqgl kskgkaevav tlyqhvcvhl ctfitsfhps lfaeldaall
      121 navlsanmit sllamdawcf larygtaelc ahhvtivahl ikscpgecyq linlsillkr
      181 lfffmapphq lefiqkfspk eaenlplwqh isfqalppel reqtvhevtt vgtaecrkwl
      241 srsrtlgele slntvlsall avcnsageal dtgkqtaiie vvsqlwafln ikqvadqpyv
      301 qqtfslllpl lgffiqtldp klilqavtlq tsllklelpd yvrlamldfv sslgklfipe
      361 aiqdrilpnl scmfalllad rswlleqhtl eaftqfaegt nheeivpqcl sseetknkvv
      421 sflektgfvd eteaakverv kqekgifwep fanvtveeak rsslqpyakr arqefpweee
      481 yrsalhtiag aleatesllq kgpapawlsm emealqermd klkryihtlg
//
LOCUS       NP_001353699             884 aa            linear   PRI 25-NOV-2025
DEFINITION  FIGNL1-interacting regulator of recombination and mitosis isoform 8
            [Homo sapiens].
ACCESSION   NP_001353699
VERSION     NP_001353699.1
DBSOURCE    REFSEQ: accession NM_001366770.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 884)
  AUTHORS   Tischler,J.D., Tsuchida,H., Bosire,R., Oda,T.T., Park,A. and
            Adeyemi,R.O.
  TITLE     FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin association
            to promote viability after replication stress
  JOURNAL   Nat Commun 15 (1), 866 (2024)
   PUBMED   38286805
  REMARK    GeneRIF: FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin
            association to promote viability after replication stress.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 884)
  AUTHORS   Zhou,Z., Yang,H., Liang,X., Zhou,T., Zhang,T., Yang,Y., Wang,J. and
            Wang,W.
  TITLE     C1orf112 teams up with FIGNL1 to facilitate RAD51 filament
            disassembly and DNA interstrand cross-link repair
  JOURNAL   Cell Rep 42 (8), 112907 (2023)
   PUBMED   37515771
REFERENCE   3  (residues 1 to 884)
  AUTHORS   Stok,C., Tsaridou,S., van den Tempel,N., Everts,M., Wierenga,E.,
            Bakker,F.J., Kok,Y., Alves,I.T., Jae,L.T., Raas,M.W.D., Huis In 't
            Veld,P.J., de Boer,H.R., Bhattacharya,A., Karanika,E., Warner,H.,
            Chen,M., van de Kooij,B., Dessapt,J., Ter Morsche,L.,
            Perepelkina,P., Fradet-Turcotte,A., Guryev,V., Tromer,E.C.,
            Chan,K.L., Fehrmann,R.S.N. and van Vugt,M.A.T.M.
  TITLE     FIRRM/C1orf112 is synthetic lethal with PICH and mediates RAD51
            dynamics
  JOURNAL   Cell Rep 42 (7), 112668 (2023)
   PUBMED   37347663
REFERENCE   4  (residues 1 to 884)
  AUTHORS   Mazouzi,A., Moser,S.C., Abascal,F., van den Broek,B., Del Castillo
            Velasco-Herrera,M., van der Heijden,I., Hekkelman,M., Drenth,A.P.,
            van der Burg,E., Kroese,L.J., Jalink,K., Adams,D.J., Jonkers,J. and
            Brummelkamp,T.R.
  TITLE     FIRRM/C1orf112 mediates resolution of homologous recombination
            intermediates in response to DNA interstrand crosslinks
  JOURNAL   Sci Adv 9 (22), eadf4409 (2023)
   PUBMED   37256941
REFERENCE   5  (residues 1 to 884)
  AUTHORS   Zhang,Z., Tan,Z., Lv,Q., Wang,L., Yu,K., Yang,H., Liang,H., Lu,T.,
            Ji,Y., Chen,J., He,W., Chen,Z., Chen,S. and Shen,X.
  TITLE     High Expression of C1ORF112 Predicts a Poor Outcome: A Potential
            Target for the Treatment of Low-Grade Gliomas
  JOURNAL   Front Genet 12, 710944 (2021)
   PUBMED   34880897
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 884)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 884)
  AUTHORS   van Dam,S., Cordeiro,R., Craig,T., van Dam,J., Wood,S.H. and de
            Magalhaes,J.P.
  TITLE     GeneFriends: an online co-expression analysis tool to identify
            novel gene targets for aging and complex diseases
  JOURNAL   BMC Genomics 13, 535 (2012)
   PUBMED   23039964
  REMARK    GeneRIF: Knockdown of C1orf112 by siRNA in HeLa cells significantly
            suppressed their growth.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 884)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 884)
  AUTHORS   Cheung,C.L., Chan,B.Y., Chan,V., Ikegawa,S., Kou,I., Ngai,H.,
            Smith,D., Luk,K.D., Huang,Q.Y., Mori,S., Sham,P.C. and Kung,A.W.
  TITLE     Pre-B-cell leukemia homeobox 1 (PBX1) shows functional and possible
            genetic association with bone mineral density variation
  JOURNAL   Hum Mol Genet 18 (4), 679-687 (2009)
   PUBMED   19064610
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 884)
  AUTHORS   Fedorova,N.I.
  TITLE     [Remote results of health resort treatment of chronic prostatitis]
  JOURNAL   Vestn Dermatol Venerol 46 (2), 71-73 (1972)
   PUBMED   4260926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL021940.1 and AL031297.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1768006.1,
                                           SRR7346977.1613505.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..884
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.2"
     Protein         1..884
                     /product="FIGNL1-interacting regulator of recombination
                     and mitosis isoform 8"
                     /note="uncharacterized protein C1orf112; associating
                     protein with POLO1; Fidgetin-like-1 interacting protein;
                     POLO1-associating protein"
                     /calculated_mol_wt=99899
     Region          234..786
                     /region_name="DUF4487"
                     /note="Domain of unknown function (DUF4487); pfam14868"
                     /db_xref="CDD:464352"
     CDS             1..884
                     /gene="FIRRM"
                     /gene_synonym="Apolo1; C1orf112; FLIP; MEICA1"
                     /coded_by="NM_001366770.1:64..2718"
                     /note="isoform 8 is encoded by transcript variant 13"
                     /db_xref="GeneID:55732"
                     /db_xref="HGNC:HGNC:25565"
                     /db_xref="MIM:621430"
ORIGIN      
        1 msqegavpas avpleelssw peelcrrelp svlprllsls qhsdswiehi qilkiivemf
       61 lphmnhltle qtffsqvlpk tvklfddmmy eltsqargls sqnleiqttl rnilqtmvql
      121 lgaltgcvqh icatqesiil eniqslpssv lhiikstfvh cknsesvysg clhlvsdllq
      181 alfkeayslq kqlmelldmv cmdplvddnd dilnmvivih slldicsvis smdhafhant
      241 wkfiikqslk hqsiiksqlk hkdiitslce dilfsfhscl qlaeqmtqsd aqdnadyrlf
      301 qktlklcrff ansllhyake flpflsdscc tlhqlylqih skfppslyat riskahqeei
      361 agaflvtldp lisqlltfqp fmqvvldskl dlpcelqfpq clllvvvmdk lpsqpkevqt
      421 lwctdsqvse tttrisllka vfysfeqcsg elslpvhlqg lkskgkaeva vtlyqhvcvh
      481 lctfitsfhp slfaeldaal lnavlsanmi tsllamdawc flarygtael cahhvtivah
      541 likscpgecy qlinlsillk rlfffmapph qlefiqkfsp keaenlplwq hisfqalppe
      601 lreqtvhevt tvgtaecrkw lsrsrtlgel eslntvlsal lavcnsagea ldtgkqtaii
      661 evvsqlwafl nikqvadqpy vqqtfslllp llgffiqtld pklilqavtl qtsllklelp
      721 dyvrlamldf vsslgklfip eaiqdrilpn lscmfallla drswlleqht leaftqfaeg
      781 tnheeivpqc lsseetknkv vsflektgfv deteaakver vkqekgifwe pfanvtveea
      841 krsslqvwad fnrgqtltrq ilpflltdet nqcgfqpyae fqik
//
LOCUS       NP_001350668             530 aa            linear   PRI 25-NOV-2025
DEFINITION  FIGNL1-interacting regulator of recombination and mitosis isoform 5
            [Homo sapiens].
ACCESSION   NP_001350668 XP_016857214
VERSION     NP_001350668.1
DBSOURCE    REFSEQ: accession NM_001363739.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Tischler,J.D., Tsuchida,H., Bosire,R., Oda,T.T., Park,A. and
            Adeyemi,R.O.
  TITLE     FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin association
            to promote viability after replication stress
  JOURNAL   Nat Commun 15 (1), 866 (2024)
   PUBMED   38286805
  REMARK    GeneRIF: FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin
            association to promote viability after replication stress.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Zhou,Z., Yang,H., Liang,X., Zhou,T., Zhang,T., Yang,Y., Wang,J. and
            Wang,W.
  TITLE     C1orf112 teams up with FIGNL1 to facilitate RAD51 filament
            disassembly and DNA interstrand cross-link repair
  JOURNAL   Cell Rep 42 (8), 112907 (2023)
   PUBMED   37515771
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Stok,C., Tsaridou,S., van den Tempel,N., Everts,M., Wierenga,E.,
            Bakker,F.J., Kok,Y., Alves,I.T., Jae,L.T., Raas,M.W.D., Huis In 't
            Veld,P.J., de Boer,H.R., Bhattacharya,A., Karanika,E., Warner,H.,
            Chen,M., van de Kooij,B., Dessapt,J., Ter Morsche,L.,
            Perepelkina,P., Fradet-Turcotte,A., Guryev,V., Tromer,E.C.,
            Chan,K.L., Fehrmann,R.S.N. and van Vugt,M.A.T.M.
  TITLE     FIRRM/C1orf112 is synthetic lethal with PICH and mediates RAD51
            dynamics
  JOURNAL   Cell Rep 42 (7), 112668 (2023)
   PUBMED   37347663
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Mazouzi,A., Moser,S.C., Abascal,F., van den Broek,B., Del Castillo
            Velasco-Herrera,M., van der Heijden,I., Hekkelman,M., Drenth,A.P.,
            van der Burg,E., Kroese,L.J., Jalink,K., Adams,D.J., Jonkers,J. and
            Brummelkamp,T.R.
  TITLE     FIRRM/C1orf112 mediates resolution of homologous recombination
            intermediates in response to DNA interstrand crosslinks
  JOURNAL   Sci Adv 9 (22), eadf4409 (2023)
   PUBMED   37256941
REFERENCE   5  (residues 1 to 530)
  AUTHORS   Zhang,Z., Tan,Z., Lv,Q., Wang,L., Yu,K., Yang,H., Liang,H., Lu,T.,
            Ji,Y., Chen,J., He,W., Chen,Z., Chen,S. and Shen,X.
  TITLE     High Expression of C1ORF112 Predicts a Poor Outcome: A Potential
            Target for the Treatment of Low-Grade Gliomas
  JOURNAL   Front Genet 12, 710944 (2021)
   PUBMED   34880897
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 530)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 530)
  AUTHORS   van Dam,S., Cordeiro,R., Craig,T., van Dam,J., Wood,S.H. and de
            Magalhaes,J.P.
  TITLE     GeneFriends: an online co-expression analysis tool to identify
            novel gene targets for aging and complex diseases
  JOURNAL   BMC Genomics 13, 535 (2012)
   PUBMED   23039964
  REMARK    GeneRIF: Knockdown of C1orf112 by siRNA in HeLa cells significantly
            suppressed their growth.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 530)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 530)
  AUTHORS   Cheung,C.L., Chan,B.Y., Chan,V., Ikegawa,S., Kou,I., Ngai,H.,
            Smith,D., Luk,K.D., Huang,Q.Y., Mori,S., Sham,P.C. and Kung,A.W.
  TITLE     Pre-B-cell leukemia homeobox 1 (PBX1) shows functional and possible
            genetic association with bone mineral density variation
  JOURNAL   Hum Mol Genet 18 (4), 679-687 (2009)
   PUBMED   19064610
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 530)
  AUTHORS   Fedorova,N.I.
  TITLE     [Remote results of health resort treatment of chronic prostatitis]
  JOURNAL   Vestn Dermatol Venerol 46 (2), 71-73 (1972)
   PUBMED   4260926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL021940.1 and AL031297.4.
            
            On May 30, 2018 this sequence version replaced XP_016857214.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.33164.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.2"
     Protein         1..530
                     /product="FIGNL1-interacting regulator of recombination
                     and mitosis isoform 5"
                     /note="uncharacterized protein C1orf112; associating
                     protein with POLO1; Fidgetin-like-1 interacting protein;
                     POLO1-associating protein"
                     /calculated_mol_wt=59566
     Region          <1..405
                     /region_name="DUF4487"
                     /note="Domain of unknown function (DUF4487); pfam14868"
                     /db_xref="CDD:464352"
     CDS             1..530
                     /gene="FIRRM"
                     /gene_synonym="Apolo1; C1orf112; FLIP; MEICA1"
                     /coded_by="NM_001363739.2:1191..2783"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS86030.1"
                     /db_xref="GeneID:55732"
                     /db_xref="HGNC:HGNC:25565"
                     /db_xref="MIM:621430"
ORIGIN      
        1 mqvvldskld lpcelqfpqc lllvvvmdkl psqpkevqtl wctdsqvset ttrisllkav
       61 fysfeqcsge lslpvhlqgl kskgkaevav tlyqhvcvhl ctfitsfhps lfaeldaall
      121 navlsanmit sllamdawcf larygtaelc ahhvtivahl ikscpgecyq linlsillkr
      181 lfffmapphq lefiqkfspk eaenlplwqh isfqalppel reqtvhevtt vgtaecrkwl
      241 srsrtlgele slntvlsall avcnsageal dtgkqtaiie vvsqlwafln ikqvadqpyv
      301 qqtfslllpl lgffiqtldp klilqavtlq tsllklelpd yvrlamldfv sslgklfipe
      361 aiqdrilpnl scmfalllad rswlleqhtl eaftqfaegt nheeivpqcl sseetknkvv
      421 sflektgfvd eteaakverv kqekgifwep fanvtveeak rsslqpyakr arqefpweee
      481 yrsalhtiag aleatesllq kgpapawlsm emealqermd klkryihtlg
//
LOCUS       NP_001353701             530 aa            linear   PRI 25-NOV-2025
DEFINITION  FIGNL1-interacting regulator of recombination and mitosis isoform 5
            [Homo sapiens].
ACCESSION   NP_001353701
VERSION     NP_001353701.1
DBSOURCE    REFSEQ: accession NM_001366772.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Tischler,J.D., Tsuchida,H., Bosire,R., Oda,T.T., Park,A. and
            Adeyemi,R.O.
  TITLE     FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin association
            to promote viability after replication stress
  JOURNAL   Nat Commun 15 (1), 866 (2024)
   PUBMED   38286805
  REMARK    GeneRIF: FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin
            association to promote viability after replication stress.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Zhou,Z., Yang,H., Liang,X., Zhou,T., Zhang,T., Yang,Y., Wang,J. and
            Wang,W.
  TITLE     C1orf112 teams up with FIGNL1 to facilitate RAD51 filament
            disassembly and DNA interstrand cross-link repair
  JOURNAL   Cell Rep 42 (8), 112907 (2023)
   PUBMED   37515771
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Stok,C., Tsaridou,S., van den Tempel,N., Everts,M., Wierenga,E.,
            Bakker,F.J., Kok,Y., Alves,I.T., Jae,L.T., Raas,M.W.D., Huis In 't
            Veld,P.J., de Boer,H.R., Bhattacharya,A., Karanika,E., Warner,H.,
            Chen,M., van de Kooij,B., Dessapt,J., Ter Morsche,L.,
            Perepelkina,P., Fradet-Turcotte,A., Guryev,V., Tromer,E.C.,
            Chan,K.L., Fehrmann,R.S.N. and van Vugt,M.A.T.M.
  TITLE     FIRRM/C1orf112 is synthetic lethal with PICH and mediates RAD51
            dynamics
  JOURNAL   Cell Rep 42 (7), 112668 (2023)
   PUBMED   37347663
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Mazouzi,A., Moser,S.C., Abascal,F., van den Broek,B., Del Castillo
            Velasco-Herrera,M., van der Heijden,I., Hekkelman,M., Drenth,A.P.,
            van der Burg,E., Kroese,L.J., Jalink,K., Adams,D.J., Jonkers,J. and
            Brummelkamp,T.R.
  TITLE     FIRRM/C1orf112 mediates resolution of homologous recombination
            intermediates in response to DNA interstrand crosslinks
  JOURNAL   Sci Adv 9 (22), eadf4409 (2023)
   PUBMED   37256941
REFERENCE   5  (residues 1 to 530)
  AUTHORS   Zhang,Z., Tan,Z., Lv,Q., Wang,L., Yu,K., Yang,H., Liang,H., Lu,T.,
            Ji,Y., Chen,J., He,W., Chen,Z., Chen,S. and Shen,X.
  TITLE     High Expression of C1ORF112 Predicts a Poor Outcome: A Potential
            Target for the Treatment of Low-Grade Gliomas
  JOURNAL   Front Genet 12, 710944 (2021)
   PUBMED   34880897
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 530)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 530)
  AUTHORS   van Dam,S., Cordeiro,R., Craig,T., van Dam,J., Wood,S.H. and de
            Magalhaes,J.P.
  TITLE     GeneFriends: an online co-expression analysis tool to identify
            novel gene targets for aging and complex diseases
  JOURNAL   BMC Genomics 13, 535 (2012)
   PUBMED   23039964
  REMARK    GeneRIF: Knockdown of C1orf112 by siRNA in HeLa cells significantly
            suppressed their growth.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 530)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 530)
  AUTHORS   Cheung,C.L., Chan,B.Y., Chan,V., Ikegawa,S., Kou,I., Ngai,H.,
            Smith,D., Luk,K.D., Huang,Q.Y., Mori,S., Sham,P.C. and Kung,A.W.
  TITLE     Pre-B-cell leukemia homeobox 1 (PBX1) shows functional and possible
            genetic association with bone mineral density variation
  JOURNAL   Hum Mol Genet 18 (4), 679-687 (2009)
   PUBMED   19064610
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 530)
  AUTHORS   Fedorova,N.I.
  TITLE     [Remote results of health resort treatment of chronic prostatitis]
  JOURNAL   Vestn Dermatol Venerol 46 (2), 71-73 (1972)
   PUBMED   4260926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL021940.1 and AL031297.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.81812.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.2"
     Protein         1..530
                     /product="FIGNL1-interacting regulator of recombination
                     and mitosis isoform 5"
                     /note="uncharacterized protein C1orf112; associating
                     protein with POLO1; Fidgetin-like-1 interacting protein;
                     POLO1-associating protein"
                     /calculated_mol_wt=59566
     Region          <1..405
                     /region_name="DUF4487"
                     /note="Domain of unknown function (DUF4487); pfam14868"
                     /db_xref="CDD:464352"
     CDS             1..530
                     /gene="FIRRM"
                     /gene_synonym="Apolo1; C1orf112; FLIP; MEICA1"
                     /coded_by="NM_001366772.1:1031..2623"
                     /note="isoform 5 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS86030.1"
                     /db_xref="GeneID:55732"
                     /db_xref="HGNC:HGNC:25565"
                     /db_xref="MIM:621430"
ORIGIN      
        1 mqvvldskld lpcelqfpqc lllvvvmdkl psqpkevqtl wctdsqvset ttrisllkav
       61 fysfeqcsge lslpvhlqgl kskgkaevav tlyqhvcvhl ctfitsfhps lfaeldaall
      121 navlsanmit sllamdawcf larygtaelc ahhvtivahl ikscpgecyq linlsillkr
      181 lfffmapphq lefiqkfspk eaenlplwqh isfqalppel reqtvhevtt vgtaecrkwl
      241 srsrtlgele slntvlsall avcnsageal dtgkqtaiie vvsqlwafln ikqvadqpyv
      301 qqtfslllpl lgffiqtldp klilqavtlq tsllklelpd yvrlamldfv sslgklfipe
      361 aiqdrilpnl scmfalllad rswlleqhtl eaftqfaegt nheeivpqcl sseetknkvv
      421 sflektgfvd eteaakverv kqekgifwep fanvtveeak rsslqpyakr arqefpweee
      481 yrsalhtiag aleatesllq kgpapawlsm emealqermd klkryihtlg
//
LOCUS       NP_001306980             161 aa            linear   PRI 25-NOV-2025
DEFINITION  FIGNL1-interacting regulator of recombination and mitosis isoform 4
            [Homo sapiens].
ACCESSION   NP_001306980
VERSION     NP_001306980.1
DBSOURCE    REFSEQ: accession NM_001320051.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Tischler,J.D., Tsuchida,H., Bosire,R., Oda,T.T., Park,A. and
            Adeyemi,R.O.
  TITLE     FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin association
            to promote viability after replication stress
  JOURNAL   Nat Commun 15 (1), 866 (2024)
   PUBMED   38286805
  REMARK    GeneRIF: FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin
            association to promote viability after replication stress.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Zhou,Z., Yang,H., Liang,X., Zhou,T., Zhang,T., Yang,Y., Wang,J. and
            Wang,W.
  TITLE     C1orf112 teams up with FIGNL1 to facilitate RAD51 filament
            disassembly and DNA interstrand cross-link repair
  JOURNAL   Cell Rep 42 (8), 112907 (2023)
   PUBMED   37515771
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Stok,C., Tsaridou,S., van den Tempel,N., Everts,M., Wierenga,E.,
            Bakker,F.J., Kok,Y., Alves,I.T., Jae,L.T., Raas,M.W.D., Huis In 't
            Veld,P.J., de Boer,H.R., Bhattacharya,A., Karanika,E., Warner,H.,
            Chen,M., van de Kooij,B., Dessapt,J., Ter Morsche,L.,
            Perepelkina,P., Fradet-Turcotte,A., Guryev,V., Tromer,E.C.,
            Chan,K.L., Fehrmann,R.S.N. and van Vugt,M.A.T.M.
  TITLE     FIRRM/C1orf112 is synthetic lethal with PICH and mediates RAD51
            dynamics
  JOURNAL   Cell Rep 42 (7), 112668 (2023)
   PUBMED   37347663
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Mazouzi,A., Moser,S.C., Abascal,F., van den Broek,B., Del Castillo
            Velasco-Herrera,M., van der Heijden,I., Hekkelman,M., Drenth,A.P.,
            van der Burg,E., Kroese,L.J., Jalink,K., Adams,D.J., Jonkers,J. and
            Brummelkamp,T.R.
  TITLE     FIRRM/C1orf112 mediates resolution of homologous recombination
            intermediates in response to DNA interstrand crosslinks
  JOURNAL   Sci Adv 9 (22), eadf4409 (2023)
   PUBMED   37256941
REFERENCE   5  (residues 1 to 161)
  AUTHORS   Zhang,Z., Tan,Z., Lv,Q., Wang,L., Yu,K., Yang,H., Liang,H., Lu,T.,
            Ji,Y., Chen,J., He,W., Chen,Z., Chen,S. and Shen,X.
  TITLE     High Expression of C1ORF112 Predicts a Poor Outcome: A Potential
            Target for the Treatment of Low-Grade Gliomas
  JOURNAL   Front Genet 12, 710944 (2021)
   PUBMED   34880897
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 161)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 161)
  AUTHORS   van Dam,S., Cordeiro,R., Craig,T., van Dam,J., Wood,S.H. and de
            Magalhaes,J.P.
  TITLE     GeneFriends: an online co-expression analysis tool to identify
            novel gene targets for aging and complex diseases
  JOURNAL   BMC Genomics 13, 535 (2012)
   PUBMED   23039964
  REMARK    GeneRIF: Knockdown of C1orf112 by siRNA in HeLa cells significantly
            suppressed their growth.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 161)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 161)
  AUTHORS   Cheung,C.L., Chan,B.Y., Chan,V., Ikegawa,S., Kou,I., Ngai,H.,
            Smith,D., Luk,K.D., Huang,Q.Y., Mori,S., Sham,P.C. and Kung,A.W.
  TITLE     Pre-B-cell leukemia homeobox 1 (PBX1) shows functional and possible
            genetic association with bone mineral density variation
  JOURNAL   Hum Mol Genet 18 (4), 679-687 (2009)
   PUBMED   19064610
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 161)
  AUTHORS   Fedorova,N.I.
  TITLE     [Remote results of health resort treatment of chronic prostatitis]
  JOURNAL   Vestn Dermatol Venerol 46 (2), 71-73 (1972)
   PUBMED   4260926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC011445.1, AL354614.1, BC091516.1 and CB159947.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC011445.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.2"
     Protein         1..161
                     /product="FIGNL1-interacting regulator of recombination
                     and mitosis isoform 4"
                     /note="uncharacterized protein C1orf112; associating
                     protein with POLO1; Fidgetin-like-1 interacting protein;
                     POLO1-associating protein"
                     /calculated_mol_wt=18059
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:34260926,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NSG2.1)"
     CDS             1..161
                     /gene="FIRRM"
                     /gene_synonym="Apolo1; C1orf112; FLIP; MEICA1"
                     /coded_by="NM_001320051.2:302..787"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS81401.1"
                     /db_xref="GeneID:55732"
                     /db_xref="HGNC:HGNC:25565"
                     /db_xref="MIM:621430"
ORIGIN      
        1 mflphmnhlt leqtffsqvl pktvklfddm myeltsqarg lssqnleiqt tlrnilqtmv
       61 qllgaltgcv qhicatqesi ileniqslps svlhiikstf vhcknsesvy sgclhlvsdl
      121 lqalfkeays lqkqlmelld mvcmdplvdd nddilnmvig e
//
LOCUS       NP_001353698             911 aa            linear   PRI 25-NOV-2025
DEFINITION  FIGNL1-interacting regulator of recombination and mitosis isoform 7
            [Homo sapiens].
ACCESSION   NP_001353698 XP_005245374
VERSION     NP_001353698.1
DBSOURCE    REFSEQ: accession NM_001366769.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Tischler,J.D., Tsuchida,H., Bosire,R., Oda,T.T., Park,A. and
            Adeyemi,R.O.
  TITLE     FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin association
            to promote viability after replication stress
  JOURNAL   Nat Commun 15 (1), 866 (2024)
   PUBMED   38286805
  REMARK    GeneRIF: FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin
            association to promote viability after replication stress.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Zhou,Z., Yang,H., Liang,X., Zhou,T., Zhang,T., Yang,Y., Wang,J. and
            Wang,W.
  TITLE     C1orf112 teams up with FIGNL1 to facilitate RAD51 filament
            disassembly and DNA interstrand cross-link repair
  JOURNAL   Cell Rep 42 (8), 112907 (2023)
   PUBMED   37515771
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Stok,C., Tsaridou,S., van den Tempel,N., Everts,M., Wierenga,E.,
            Bakker,F.J., Kok,Y., Alves,I.T., Jae,L.T., Raas,M.W.D., Huis In 't
            Veld,P.J., de Boer,H.R., Bhattacharya,A., Karanika,E., Warner,H.,
            Chen,M., van de Kooij,B., Dessapt,J., Ter Morsche,L.,
            Perepelkina,P., Fradet-Turcotte,A., Guryev,V., Tromer,E.C.,
            Chan,K.L., Fehrmann,R.S.N. and van Vugt,M.A.T.M.
  TITLE     FIRRM/C1orf112 is synthetic lethal with PICH and mediates RAD51
            dynamics
  JOURNAL   Cell Rep 42 (7), 112668 (2023)
   PUBMED   37347663
REFERENCE   4  (residues 1 to 911)
  AUTHORS   Mazouzi,A., Moser,S.C., Abascal,F., van den Broek,B., Del Castillo
            Velasco-Herrera,M., van der Heijden,I., Hekkelman,M., Drenth,A.P.,
            van der Burg,E., Kroese,L.J., Jalink,K., Adams,D.J., Jonkers,J. and
            Brummelkamp,T.R.
  TITLE     FIRRM/C1orf112 mediates resolution of homologous recombination
            intermediates in response to DNA interstrand crosslinks
  JOURNAL   Sci Adv 9 (22), eadf4409 (2023)
   PUBMED   37256941
REFERENCE   5  (residues 1 to 911)
  AUTHORS   Zhang,Z., Tan,Z., Lv,Q., Wang,L., Yu,K., Yang,H., Liang,H., Lu,T.,
            Ji,Y., Chen,J., He,W., Chen,Z., Chen,S. and Shen,X.
  TITLE     High Expression of C1ORF112 Predicts a Poor Outcome: A Potential
            Target for the Treatment of Low-Grade Gliomas
  JOURNAL   Front Genet 12, 710944 (2021)
   PUBMED   34880897
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 911)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 911)
  AUTHORS   van Dam,S., Cordeiro,R., Craig,T., van Dam,J., Wood,S.H. and de
            Magalhaes,J.P.
  TITLE     GeneFriends: an online co-expression analysis tool to identify
            novel gene targets for aging and complex diseases
  JOURNAL   BMC Genomics 13, 535 (2012)
   PUBMED   23039964
  REMARK    GeneRIF: Knockdown of C1orf112 by siRNA in HeLa cells significantly
            suppressed their growth.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 911)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 911)
  AUTHORS   Cheung,C.L., Chan,B.Y., Chan,V., Ikegawa,S., Kou,I., Ngai,H.,
            Smith,D., Luk,K.D., Huang,Q.Y., Mori,S., Sham,P.C. and Kung,A.W.
  TITLE     Pre-B-cell leukemia homeobox 1 (PBX1) shows functional and possible
            genetic association with bone mineral density variation
  JOURNAL   Hum Mol Genet 18 (4), 679-687 (2009)
   PUBMED   19064610
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 911)
  AUTHORS   Fedorova,N.I.
  TITLE     [Remote results of health resort treatment of chronic prostatitis]
  JOURNAL   Vestn Dermatol Venerol 46 (2), 71-73 (1972)
   PUBMED   4260926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL021940.1 and AL031297.4.
            
            On Oct 19, 2018 this sequence version replaced XP_005245374.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.151798.1,
                                           SRR1803616.37833.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.2"
     Protein         1..911
                     /product="FIGNL1-interacting regulator of recombination
                     and mitosis isoform 7"
                     /note="uncharacterized protein C1orf112; associating
                     protein with POLO1; Fidgetin-like-1 interacting protein;
                     POLO1-associating protein"
                     /calculated_mol_wt=102954
     Region          234..786
                     /region_name="DUF4487"
                     /note="Domain of unknown function (DUF4487); pfam14868"
                     /db_xref="CDD:464352"
     CDS             1..911
                     /gene="FIRRM"
                     /gene_synonym="Apolo1; C1orf112; FLIP; MEICA1"
                     /coded_by="NM_001366769.1:64..2799"
                     /note="isoform 7 is encoded by transcript variant 10"
                     /db_xref="GeneID:55732"
                     /db_xref="HGNC:HGNC:25565"
                     /db_xref="MIM:621430"
ORIGIN      
        1 msqegavpas avpleelssw peelcrrelp svlprllsls qhsdswiehi qilkiivemf
       61 lphmnhltle qtffsqvlpk tvklfddmmy eltsqargls sqnleiqttl rnilqtmvql
      121 lgaltgcvqh icatqesiil eniqslpssv lhiikstfvh cknsesvysg clhlvsdllq
      181 alfkeayslq kqlmelldmv cmdplvddnd dilnmvivih slldicsvis smdhafhant
      241 wkfiikqslk hqsiiksqlk hkdiitslce dilfsfhscl qlaeqmtqsd aqdnadyrlf
      301 qktlklcrff ansllhyake flpflsdscc tlhqlylqih skfppslyat riskahqeei
      361 agaflvtldp lisqlltfqp fmqvvldskl dlpcelqfpq clllvvvmdk lpsqpkevqt
      421 lwctdsqvse tttrisllka vfysfeqcsg elslpvhlqg lkskgkaeva vtlyqhvcvh
      481 lctfitsfhp slfaeldaal lnavlsanmi tsllamdawc flarygtael cahhvtivah
      541 likscpgecy qlinlsillk rlfffmapph qlefiqkfsp keaenlplwq hisfqalppe
      601 lreqtvhevt tvgtaecrkw lsrsrtlgel eslntvlsal lavcnsagea ldtgkqtaii
      661 evvsqlwafl nikqvadqpy vqqtfslllp llgffiqtld pklilqavtl qtsllklelp
      721 dyvrlamldf vsslgklfip eaiqdrilpn lscmfallla drswlleqht leaftqfaeg
      781 tnheeivpqc lsseetknkv vsflektgfv deteaakver vkqekgifwe pfanvtveea
      841 krsslqpyak rarqefpwee eyrsalhtia galeatesll qkgpapawls memealqerm
      901 dklkryihtl g
//
LOCUS       NP_001306976             853 aa            linear   PRI 25-NOV-2025
DEFINITION  FIGNL1-interacting regulator of recombination and mitosis isoform 1
            [Homo sapiens].
ACCESSION   NP_001306976 XP_011508033
VERSION     NP_001306976.1
DBSOURCE    REFSEQ: accession NM_001320047.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Tischler,J.D., Tsuchida,H., Bosire,R., Oda,T.T., Park,A. and
            Adeyemi,R.O.
  TITLE     FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin association
            to promote viability after replication stress
  JOURNAL   Nat Commun 15 (1), 866 (2024)
   PUBMED   38286805
  REMARK    GeneRIF: FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin
            association to promote viability after replication stress.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 853)
  AUTHORS   Zhou,Z., Yang,H., Liang,X., Zhou,T., Zhang,T., Yang,Y., Wang,J. and
            Wang,W.
  TITLE     C1orf112 teams up with FIGNL1 to facilitate RAD51 filament
            disassembly and DNA interstrand cross-link repair
  JOURNAL   Cell Rep 42 (8), 112907 (2023)
   PUBMED   37515771
REFERENCE   3  (residues 1 to 853)
  AUTHORS   Stok,C., Tsaridou,S., van den Tempel,N., Everts,M., Wierenga,E.,
            Bakker,F.J., Kok,Y., Alves,I.T., Jae,L.T., Raas,M.W.D., Huis In 't
            Veld,P.J., de Boer,H.R., Bhattacharya,A., Karanika,E., Warner,H.,
            Chen,M., van de Kooij,B., Dessapt,J., Ter Morsche,L.,
            Perepelkina,P., Fradet-Turcotte,A., Guryev,V., Tromer,E.C.,
            Chan,K.L., Fehrmann,R.S.N. and van Vugt,M.A.T.M.
  TITLE     FIRRM/C1orf112 is synthetic lethal with PICH and mediates RAD51
            dynamics
  JOURNAL   Cell Rep 42 (7), 112668 (2023)
   PUBMED   37347663
REFERENCE   4  (residues 1 to 853)
  AUTHORS   Mazouzi,A., Moser,S.C., Abascal,F., van den Broek,B., Del Castillo
            Velasco-Herrera,M., van der Heijden,I., Hekkelman,M., Drenth,A.P.,
            van der Burg,E., Kroese,L.J., Jalink,K., Adams,D.J., Jonkers,J. and
            Brummelkamp,T.R.
  TITLE     FIRRM/C1orf112 mediates resolution of homologous recombination
            intermediates in response to DNA interstrand crosslinks
  JOURNAL   Sci Adv 9 (22), eadf4409 (2023)
   PUBMED   37256941
REFERENCE   5  (residues 1 to 853)
  AUTHORS   Zhang,Z., Tan,Z., Lv,Q., Wang,L., Yu,K., Yang,H., Liang,H., Lu,T.,
            Ji,Y., Chen,J., He,W., Chen,Z., Chen,S. and Shen,X.
  TITLE     High Expression of C1ORF112 Predicts a Poor Outcome: A Potential
            Target for the Treatment of Low-Grade Gliomas
  JOURNAL   Front Genet 12, 710944 (2021)
   PUBMED   34880897
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 853)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 853)
  AUTHORS   van Dam,S., Cordeiro,R., Craig,T., van Dam,J., Wood,S.H. and de
            Magalhaes,J.P.
  TITLE     GeneFriends: an online co-expression analysis tool to identify
            novel gene targets for aging and complex diseases
  JOURNAL   BMC Genomics 13, 535 (2012)
   PUBMED   23039964
  REMARK    GeneRIF: Knockdown of C1orf112 by siRNA in HeLa cells significantly
            suppressed their growth.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 853)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 853)
  AUTHORS   Cheung,C.L., Chan,B.Y., Chan,V., Ikegawa,S., Kou,I., Ngai,H.,
            Smith,D., Luk,K.D., Huang,Q.Y., Mori,S., Sham,P.C. and Kung,A.W.
  TITLE     Pre-B-cell leukemia homeobox 1 (PBX1) shows functional and possible
            genetic association with bone mineral density variation
  JOURNAL   Hum Mol Genet 18 (4), 679-687 (2009)
   PUBMED   19064610
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 853)
  AUTHORS   Fedorova,N.I.
  TITLE     [Remote results of health resort treatment of chronic prostatitis]
  JOURNAL   Vestn Dermatol Venerol 46 (2), 71-73 (1972)
   PUBMED   4260926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC401980.1, DA770714.1, BC091516.1 and AL031297.4.
            
            On Feb 10, 2016 this sequence version replaced XP_011508033.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091516.1, AK096493.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359326.9/ ENSP00000352276.4
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.2"
     Protein         1..853
                     /product="FIGNL1-interacting regulator of recombination
                     and mitosis isoform 1"
                     /note="uncharacterized protein C1orf112; associating
                     protein with POLO1; Fidgetin-like-1 interacting protein;
                     POLO1-associating protein"
                     /calculated_mol_wt=96424
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:34260926,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NSG2.1)"
     Region          176..728
                     /region_name="DUF4487"
                     /note="Domain of unknown function (DUF4487); pfam14868"
                     /db_xref="CDD:464352"
     Site            744
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK1.
                     /evidence=ECO:0000269|PubMed:34260926; propagated from
                     UniProtKB/Swiss-Prot (Q9NSG2.1)"
     Site            792
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NSG2.1)"
     CDS             1..853
                     /gene="FIRRM"
                     /gene_synonym="Apolo1; C1orf112; FLIP; MEICA1"
                     /coded_by="NM_001320047.2:357..2918"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1285.1"
                     /db_xref="GeneID:55732"
                     /db_xref="HGNC:HGNC:25565"
                     /db_xref="MIM:621430"
ORIGIN      
        1 mflphmnhlt leqtffsqvl pktvklfddm myeltsqarg lssqnleiqt tlrnilqtmv
       61 qllgaltgcv qhicatqesi ileniqslps svlhiikstf vhcknsesvy sgclhlvsdl
      121 lqalfkeays lqkqlmelld mvcmdplvdd nddilnmviv ihslldicsv issmdhafha
      181 ntwkfiikqs lkhqsiiksq lkhkdiitsl cedilfsfhs clqlaeqmtq sdaqdnadyr
      241 lfqktlklcr ffansllhya keflpflsds cctlhqlylq ihskfppsly atriskahqe
      301 eiagaflvtl dplisqlltf qpfmqvvlds kldlpcelqf pqclllvvvm dklpsqpkev
      361 qtlwctdsqv setttrisll kavfysfeqc sgelslpvhl qglkskgkae vavtlyqhvc
      421 vhlctfitsf hpslfaelda allnavlsan mitsllamda wcflarygta elcahhvtiv
      481 ahlikscpge cyqlinlsil lkrlfffmap phqlefiqkf spkeaenlpl wqhisfqalp
      541 pelreqtvhe vttvgtaecr kwlsrsrtlg eleslntvls allavcnsag ealdtgkqta
      601 iievvsqlwa flnikqvadq pyvqqtfsll lpllgffiqt ldpklilqav tlqtsllkle
      661 lpdyvrlaml dfvsslgklf ipeaiqdril pnlscmfall ladrswlleq htleaftqfa
      721 egtnheeivp qclsseetkn kvvsflektg fvdeteaakv ervkqekgif wepfanvtve
      781 eakrsslqpy akrarqefpw eeeyrsalht iagaleates llqkgpapaw lsmemealqe
      841 rmdklkryih tlg
//
LOCUS       NP_001353700             530 aa            linear   PRI 25-NOV-2025
DEFINITION  FIGNL1-interacting regulator of recombination and mitosis isoform 5
            [Homo sapiens].
ACCESSION   NP_001353700 XP_016857213
VERSION     NP_001353700.1
DBSOURCE    REFSEQ: accession NM_001366771.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Tischler,J.D., Tsuchida,H., Bosire,R., Oda,T.T., Park,A. and
            Adeyemi,R.O.
  TITLE     FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin association
            to promote viability after replication stress
  JOURNAL   Nat Commun 15 (1), 866 (2024)
   PUBMED   38286805
  REMARK    GeneRIF: FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin
            association to promote viability after replication stress.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Zhou,Z., Yang,H., Liang,X., Zhou,T., Zhang,T., Yang,Y., Wang,J. and
            Wang,W.
  TITLE     C1orf112 teams up with FIGNL1 to facilitate RAD51 filament
            disassembly and DNA interstrand cross-link repair
  JOURNAL   Cell Rep 42 (8), 112907 (2023)
   PUBMED   37515771
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Stok,C., Tsaridou,S., van den Tempel,N., Everts,M., Wierenga,E.,
            Bakker,F.J., Kok,Y., Alves,I.T., Jae,L.T., Raas,M.W.D., Huis In 't
            Veld,P.J., de Boer,H.R., Bhattacharya,A., Karanika,E., Warner,H.,
            Chen,M., van de Kooij,B., Dessapt,J., Ter Morsche,L.,
            Perepelkina,P., Fradet-Turcotte,A., Guryev,V., Tromer,E.C.,
            Chan,K.L., Fehrmann,R.S.N. and van Vugt,M.A.T.M.
  TITLE     FIRRM/C1orf112 is synthetic lethal with PICH and mediates RAD51
            dynamics
  JOURNAL   Cell Rep 42 (7), 112668 (2023)
   PUBMED   37347663
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Mazouzi,A., Moser,S.C., Abascal,F., van den Broek,B., Del Castillo
            Velasco-Herrera,M., van der Heijden,I., Hekkelman,M., Drenth,A.P.,
            van der Burg,E., Kroese,L.J., Jalink,K., Adams,D.J., Jonkers,J. and
            Brummelkamp,T.R.
  TITLE     FIRRM/C1orf112 mediates resolution of homologous recombination
            intermediates in response to DNA interstrand crosslinks
  JOURNAL   Sci Adv 9 (22), eadf4409 (2023)
   PUBMED   37256941
REFERENCE   5  (residues 1 to 530)
  AUTHORS   Zhang,Z., Tan,Z., Lv,Q., Wang,L., Yu,K., Yang,H., Liang,H., Lu,T.,
            Ji,Y., Chen,J., He,W., Chen,Z., Chen,S. and Shen,X.
  TITLE     High Expression of C1ORF112 Predicts a Poor Outcome: A Potential
            Target for the Treatment of Low-Grade Gliomas
  JOURNAL   Front Genet 12, 710944 (2021)
   PUBMED   34880897
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 530)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 530)
  AUTHORS   van Dam,S., Cordeiro,R., Craig,T., van Dam,J., Wood,S.H. and de
            Magalhaes,J.P.
  TITLE     GeneFriends: an online co-expression analysis tool to identify
            novel gene targets for aging and complex diseases
  JOURNAL   BMC Genomics 13, 535 (2012)
   PUBMED   23039964
  REMARK    GeneRIF: Knockdown of C1orf112 by siRNA in HeLa cells significantly
            suppressed their growth.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 530)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 530)
  AUTHORS   Cheung,C.L., Chan,B.Y., Chan,V., Ikegawa,S., Kou,I., Ngai,H.,
            Smith,D., Luk,K.D., Huang,Q.Y., Mori,S., Sham,P.C. and Kung,A.W.
  TITLE     Pre-B-cell leukemia homeobox 1 (PBX1) shows functional and possible
            genetic association with bone mineral density variation
  JOURNAL   Hum Mol Genet 18 (4), 679-687 (2009)
   PUBMED   19064610
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 530)
  AUTHORS   Fedorova,N.I.
  TITLE     [Remote results of health resort treatment of chronic prostatitis]
  JOURNAL   Vestn Dermatol Venerol 46 (2), 71-73 (1972)
   PUBMED   4260926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL021940.1 and AL031297.4.
            
            On Oct 19, 2018 this sequence version replaced XP_016857213.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.258524.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.2"
     Protein         1..530
                     /product="FIGNL1-interacting regulator of recombination
                     and mitosis isoform 5"
                     /note="uncharacterized protein C1orf112; associating
                     protein with POLO1; Fidgetin-like-1 interacting protein;
                     POLO1-associating protein"
                     /calculated_mol_wt=59566
     Region          <1..405
                     /region_name="DUF4487"
                     /note="Domain of unknown function (DUF4487); pfam14868"
                     /db_xref="CDD:464352"
     CDS             1..530
                     /gene="FIRRM"
                     /gene_synonym="Apolo1; C1orf112; FLIP; MEICA1"
                     /coded_by="NM_001366771.1:1330..2922"
                     /note="isoform 5 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS86030.1"
                     /db_xref="GeneID:55732"
                     /db_xref="HGNC:HGNC:25565"
                     /db_xref="MIM:621430"
ORIGIN      
        1 mqvvldskld lpcelqfpqc lllvvvmdkl psqpkevqtl wctdsqvset ttrisllkav
       61 fysfeqcsge lslpvhlqgl kskgkaevav tlyqhvcvhl ctfitsfhps lfaeldaall
      121 navlsanmit sllamdawcf larygtaelc ahhvtivahl ikscpgecyq linlsillkr
      181 lfffmapphq lefiqkfspk eaenlplwqh isfqalppel reqtvhevtt vgtaecrkwl
      241 srsrtlgele slntvlsall avcnsageal dtgkqtaiie vvsqlwafln ikqvadqpyv
      301 qqtfslllpl lgffiqtldp klilqavtlq tsllklelpd yvrlamldfv sslgklfipe
      361 aiqdrilpnl scmfalllad rswlleqhtl eaftqfaegt nheeivpqcl sseetknkvv
      421 sflektgfvd eteaakverv kqekgifwep fanvtveeak rsslqpyakr arqefpweee
      481 yrsalhtiag aleatesllq kgpapawlsm emealqermd klkryihtlg
//
LOCUS       NP_001306979             180 aa            linear   PRI 25-NOV-2025
DEFINITION  FIGNL1-interacting regulator of recombination and mitosis isoform 3
            [Homo sapiens].
ACCESSION   NP_001306979
VERSION     NP_001306979.1
DBSOURCE    REFSEQ: accession NM_001320050.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Tischler,J.D., Tsuchida,H., Bosire,R., Oda,T.T., Park,A. and
            Adeyemi,R.O.
  TITLE     FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin association
            to promote viability after replication stress
  JOURNAL   Nat Commun 15 (1), 866 (2024)
   PUBMED   38286805
  REMARK    GeneRIF: FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin
            association to promote viability after replication stress.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Zhou,Z., Yang,H., Liang,X., Zhou,T., Zhang,T., Yang,Y., Wang,J. and
            Wang,W.
  TITLE     C1orf112 teams up with FIGNL1 to facilitate RAD51 filament
            disassembly and DNA interstrand cross-link repair
  JOURNAL   Cell Rep 42 (8), 112907 (2023)
   PUBMED   37515771
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Stok,C., Tsaridou,S., van den Tempel,N., Everts,M., Wierenga,E.,
            Bakker,F.J., Kok,Y., Alves,I.T., Jae,L.T., Raas,M.W.D., Huis In 't
            Veld,P.J., de Boer,H.R., Bhattacharya,A., Karanika,E., Warner,H.,
            Chen,M., van de Kooij,B., Dessapt,J., Ter Morsche,L.,
            Perepelkina,P., Fradet-Turcotte,A., Guryev,V., Tromer,E.C.,
            Chan,K.L., Fehrmann,R.S.N. and van Vugt,M.A.T.M.
  TITLE     FIRRM/C1orf112 is synthetic lethal with PICH and mediates RAD51
            dynamics
  JOURNAL   Cell Rep 42 (7), 112668 (2023)
   PUBMED   37347663
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Mazouzi,A., Moser,S.C., Abascal,F., van den Broek,B., Del Castillo
            Velasco-Herrera,M., van der Heijden,I., Hekkelman,M., Drenth,A.P.,
            van der Burg,E., Kroese,L.J., Jalink,K., Adams,D.J., Jonkers,J. and
            Brummelkamp,T.R.
  TITLE     FIRRM/C1orf112 mediates resolution of homologous recombination
            intermediates in response to DNA interstrand crosslinks
  JOURNAL   Sci Adv 9 (22), eadf4409 (2023)
   PUBMED   37256941
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Zhang,Z., Tan,Z., Lv,Q., Wang,L., Yu,K., Yang,H., Liang,H., Lu,T.,
            Ji,Y., Chen,J., He,W., Chen,Z., Chen,S. and Shen,X.
  TITLE     High Expression of C1ORF112 Predicts a Poor Outcome: A Potential
            Target for the Treatment of Low-Grade Gliomas
  JOURNAL   Front Genet 12, 710944 (2021)
   PUBMED   34880897
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 180)
  AUTHORS   van Dam,S., Cordeiro,R., Craig,T., van Dam,J., Wood,S.H. and de
            Magalhaes,J.P.
  TITLE     GeneFriends: an online co-expression analysis tool to identify
            novel gene targets for aging and complex diseases
  JOURNAL   BMC Genomics 13, 535 (2012)
   PUBMED   23039964
  REMARK    GeneRIF: Knockdown of C1orf112 by siRNA in HeLa cells significantly
            suppressed their growth.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 180)
  AUTHORS   Cheung,C.L., Chan,B.Y., Chan,V., Ikegawa,S., Kou,I., Ngai,H.,
            Smith,D., Luk,K.D., Huang,Q.Y., Mori,S., Sham,P.C. and Kung,A.W.
  TITLE     Pre-B-cell leukemia homeobox 1 (PBX1) shows functional and possible
            genetic association with bone mineral density variation
  JOURNAL   Hum Mol Genet 18 (4), 679-687 (2009)
   PUBMED   19064610
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 180)
  AUTHORS   Fedorova,N.I.
  TITLE     [Remote results of health resort treatment of chronic prostatitis]
  JOURNAL   Vestn Dermatol Venerol 46 (2), 71-73 (1972)
   PUBMED   4260926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC401980.1, BC011012.1, AK096493.1, BC011445.1 and CB159947.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC011012.1, DC350747.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.2"
     Protein         1..180
                     /product="FIGNL1-interacting regulator of recombination
                     and mitosis isoform 3"
                     /note="uncharacterized protein C1orf112; associating
                     protein with POLO1; Fidgetin-like-1 interacting protein;
                     POLO1-associating protein"
                     /calculated_mol_wt=20387
     CDS             1..180
                     /gene="FIRRM"
                     /gene_synonym="Apolo1; C1orf112; FLIP; MEICA1"
                     /coded_by="NM_001320050.2:64..606"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS81400.1"
                     /db_xref="GeneID:55732"
                     /db_xref="HGNC:HGNC:25565"
                     /db_xref="MIM:621430"
ORIGIN      
        1 msqegavpas avpleelssw peelcrrelp svlprllsls qhsdswiehi qilkiivemf
       61 lphmnhltle qtffsqvlpk tvklfddmmy eltsqargls sqnleiqttl rnilqtmvql
      121 lgaltgcvqh icatqesiil eniqslpssv lhiikstfvh ckfqtfsrlf srrpilfkss
//
LOCUS       NP_001353697             824 aa            linear   PRI 25-NOV-2025
DEFINITION  FIGNL1-interacting regulator of recombination and mitosis isoform 6
            [Homo sapiens].
ACCESSION   NP_001353697
VERSION     NP_001353697.1
DBSOURCE    REFSEQ: accession NM_001366768.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Tischler,J.D., Tsuchida,H., Bosire,R., Oda,T.T., Park,A. and
            Adeyemi,R.O.
  TITLE     FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin association
            to promote viability after replication stress
  JOURNAL   Nat Commun 15 (1), 866 (2024)
   PUBMED   38286805
  REMARK    GeneRIF: FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin
            association to promote viability after replication stress.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Zhou,Z., Yang,H., Liang,X., Zhou,T., Zhang,T., Yang,Y., Wang,J. and
            Wang,W.
  TITLE     C1orf112 teams up with FIGNL1 to facilitate RAD51 filament
            disassembly and DNA interstrand cross-link repair
  JOURNAL   Cell Rep 42 (8), 112907 (2023)
   PUBMED   37515771
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Stok,C., Tsaridou,S., van den Tempel,N., Everts,M., Wierenga,E.,
            Bakker,F.J., Kok,Y., Alves,I.T., Jae,L.T., Raas,M.W.D., Huis In 't
            Veld,P.J., de Boer,H.R., Bhattacharya,A., Karanika,E., Warner,H.,
            Chen,M., van de Kooij,B., Dessapt,J., Ter Morsche,L.,
            Perepelkina,P., Fradet-Turcotte,A., Guryev,V., Tromer,E.C.,
            Chan,K.L., Fehrmann,R.S.N. and van Vugt,M.A.T.M.
  TITLE     FIRRM/C1orf112 is synthetic lethal with PICH and mediates RAD51
            dynamics
  JOURNAL   Cell Rep 42 (7), 112668 (2023)
   PUBMED   37347663
REFERENCE   4  (residues 1 to 824)
  AUTHORS   Mazouzi,A., Moser,S.C., Abascal,F., van den Broek,B., Del Castillo
            Velasco-Herrera,M., van der Heijden,I., Hekkelman,M., Drenth,A.P.,
            van der Burg,E., Kroese,L.J., Jalink,K., Adams,D.J., Jonkers,J. and
            Brummelkamp,T.R.
  TITLE     FIRRM/C1orf112 mediates resolution of homologous recombination
            intermediates in response to DNA interstrand crosslinks
  JOURNAL   Sci Adv 9 (22), eadf4409 (2023)
   PUBMED   37256941
REFERENCE   5  (residues 1 to 824)
  AUTHORS   Zhang,Z., Tan,Z., Lv,Q., Wang,L., Yu,K., Yang,H., Liang,H., Lu,T.,
            Ji,Y., Chen,J., He,W., Chen,Z., Chen,S. and Shen,X.
  TITLE     High Expression of C1ORF112 Predicts a Poor Outcome: A Potential
            Target for the Treatment of Low-Grade Gliomas
  JOURNAL   Front Genet 12, 710944 (2021)
   PUBMED   34880897
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 824)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 824)
  AUTHORS   van Dam,S., Cordeiro,R., Craig,T., van Dam,J., Wood,S.H. and de
            Magalhaes,J.P.
  TITLE     GeneFriends: an online co-expression analysis tool to identify
            novel gene targets for aging and complex diseases
  JOURNAL   BMC Genomics 13, 535 (2012)
   PUBMED   23039964
  REMARK    GeneRIF: Knockdown of C1orf112 by siRNA in HeLa cells significantly
            suppressed their growth.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 824)
  AUTHORS   Ehret,G.B., O'Connor,A.A., Weder,A., Cooper,R.S. and Chakravarti,A.
  TITLE     Follow-up of a major linkage peak on chromosome 1 reveals
            suggestive QTLs associated with essential hypertension: GenNet
            study
  JOURNAL   Eur J Hum Genet 17 (12), 1650-1657 (2009)
   PUBMED   19536175
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 824)
  AUTHORS   Cheung,C.L., Chan,B.Y., Chan,V., Ikegawa,S., Kou,I., Ngai,H.,
            Smith,D., Luk,K.D., Huang,Q.Y., Mori,S., Sham,P.C. and Kung,A.W.
  TITLE     Pre-B-cell leukemia homeobox 1 (PBX1) shows functional and possible
            genetic association with bone mineral density variation
  JOURNAL   Hum Mol Genet 18 (4), 679-687 (2009)
   PUBMED   19064610
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 824)
  AUTHORS   Fedorova,N.I.
  TITLE     [Remote results of health resort treatment of chronic prostatitis]
  JOURNAL   Vestn Dermatol Venerol 46 (2), 71-73 (1972)
   PUBMED   4260926
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL021940.1 and AL031297.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.151518.1,
                                           SRR1803611.136050.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.2"
     Protein         1..824
                     /product="FIGNL1-interacting regulator of recombination
                     and mitosis isoform 6"
                     /note="uncharacterized protein C1orf112; associating
                     protein with POLO1; Fidgetin-like-1 interacting protein;
                     POLO1-associating protein"
                     /calculated_mol_wt=92964
     Region          147..699
                     /region_name="DUF4487"
                     /note="Domain of unknown function (DUF4487); pfam14868"
                     /db_xref="CDD:464352"
     CDS             1..824
                     /gene="FIRRM"
                     /gene_synonym="Apolo1; C1orf112; FLIP; MEICA1"
                     /coded_by="NM_001366768.1:236..2710"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="GeneID:55732"
                     /db_xref="HGNC:HGNC:25565"
                     /db_xref="MIM:621430"
ORIGIN      
        1 mmyeltsqar glssqnleiq ttlrnilqtm vqllgaltgc vqhicatqes iileniqslp
       61 ssvlhiikst fvhcknsesv ysgclhlvsd llqalfkeay slqkqlmell dmvcmdplvd
      121 dnddilnmvi vihslldics vissmdhafh antwkfiikq slkhqsiiks qlkhkdiits
      181 lcedilfsfh sclqlaeqmt qsdaqdnady rlfqktlklc rffansllhy akeflpflsd
      241 scctlhqlyl qihskfppsl yatriskahq eeiagaflvt ldplisqllt fqpfmqvvld
      301 skldlpcelq fpqclllvvv mdklpsqpke vqtlwctdsq vsetttrisl lkavfysfeq
      361 csgelslpvh lqglkskgka evavtlyqhv cvhlctfits fhpslfaeld aallnavlsa
      421 nmitsllamd awcflarygt aelcahhvti vahlikscpg ecyqlinlsi llkrlfffma
      481 pphqlefiqk fspkeaenlp lwqhisfqal ppelreqtvh evttvgtaec rkwlsrsrtl
      541 geleslntvl sallavcnsa gealdtgkqt aiievvsqlw aflnikqvad qpyvqqtfsl
      601 llpllgffiq tldpklilqa vtlqtsllkl elpdyvrlam ldfvsslgkl fipeaiqdri
      661 lpnlscmfal lladrswlle qhtleaftqf aegtnheeiv pqclsseetk nkvvsflekt
      721 gfvdeteaak vervkqekgi fwepfanvtv eeakrsslqp yakrarqefp weeeyrsalh
      781 tiagaleate sllqkgpapa wlsmemealq ermdklkryi htlg
//
LOCUS       NP_071746                351 aa            linear   PRI 26-NOV-2025
DEFINITION  N-terminal EF-hand calcium-binding protein 1 [Homo sapiens].
ACCESSION   NP_071746
VERSION     NP_071746.1
DBSOURCE    REFSEQ: accession NM_022351.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Zhang,M.D., Barde,S., Szodorai,E., Josephson,A., Mitsios,N.,
            Watanabe,M., Attems,J., Lubec,G., Kovacs,G.G., Uhlen,M., Mulder,J.,
            Harkany,T. and Hokfelt,T.
  TITLE     Comparative anatomical distribution of neuronal calcium-binding
            protein (NECAB) 1 and -2 in rodent and human spinal cord
  JOURNAL   Brain Struct Funct 221 (7), 3803-3823 (2016)
   PUBMED   26843217
  REMARK    GeneRIF: Study suggests that the phenotypic segregation of Neuronal
            calcium-binding protein 1 and -2 (NECAB1 and -2) to respective
            excitatory and inhibitory spinal systems can underpin functional
            modalities in determining the fidelity of synaptic
            neurotransmission and neuronal responsiveness, and might bear
            translational relevance to humans.
            Erratum:[Brain Struct Funct. 2016 Sep;221(7):3843. doi:
            10.1007/s00429-016-1236-7. PMID: 27206425]
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Wu,H., Li,D., Shan,Y., Wan,B., Hexige,S., Guo,J., Wu,C. and Yu,L.
  TITLE     EFCBP1/NECAB1, a brain-specifically expressed gene with highest
            abundance in temporal lobe, encodes a protein containing EF-hand
            and antibiotic biosynthesis monooxygenase domains
  JOURNAL   DNA Seq 18 (1), 73-79 (2007)
   PUBMED   17364817
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Sugita,S., Ho,A. and Sudhof,T.C.
  TITLE     NECABs: a family of neuronal Ca(2+)-binding proteins with an
            unusual domain structure and a restricted expression pattern
  JOURNAL   Neuroscience 112 (1), 51-63 (2002)
   PUBMED   12044471
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF414126.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.195227.1,
                                           SRR1660809.70887.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000417640.7/ ENSP00000387380.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.3"
     Protein         1..351
                     /product="N-terminal EF-hand calcium-binding protein 1"
                     /note="synaptotagmin interacting protein 1; neuronal
                     calcium binding protein; EF-hand calcium-binding protein
                     1; neuronal calcium-binding protein 1"
                     /calculated_mol_wt=40440
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESB5; propagated from
                     UniProtKB/Swiss-Prot (Q8N987.1)"
     Region          <33..92
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     Region          180..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N987.1)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG18; propagated from
                     UniProtKB/Swiss-Prot (Q8N987.1)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BG18; propagated from
                     UniProtKB/Swiss-Prot (Q8N987.1)"
     Region          254..324
                     /region_name="ABM"
                     /note="Antibiotic biosynthesis monooxygenase; pfam03992"
                     /db_xref="CDD:427635"
     CDS             1..351
                     /gene="NECAB1"
                     /gene_synonym="EFCAB1; EFCBP1; STIP-1"
                     /coded_by="NM_022351.5:113..1168"
                     /db_xref="CCDS:CCDS47889.1"
                     /db_xref="GeneID:64168"
                     /db_xref="HGNC:HGNC:20983"
                     /db_xref="MIM:621427"
ORIGIN      
        1 medsqetsps snnsseelss alhlskgmsi fldilrradk nddgklsfee fkayfadgvl
       61 sgeelhelfh tidthntnnl dteelceyfs qhlgeyenvl aaledlnlsi lkamgktkkd
      121 yqeasnleqf vtrfllketl nqlqslqnsl ecametteeq trqerqgpak pevlsiqwpg
      181 krssrrvqrh nsfspnspqf nvsgpgllee dnqwmtqinr lqklidrlek kdlkleppee
      241 eiiegntksh imlvqrqmsv ieedleefql alkhyvesas sqsgclrisi qklsnesrym
      301 iyefwenssv wnshlqtnys ktfqrsnvdf letpeltstm lvpaswwiln n
//
LOCUS       NP_001398067             950 aa            linear   PRI 26-NOV-2025
DEFINITION  coiled-coil and C2 domain-containing protein 1A isoform 2 [Homo
            sapiens].
ACCESSION   NP_001398067 XP_047294969
VERSION     NP_001398067.1
DBSOURCE    REFSEQ: accession NM_001411138.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 950)
  AUTHORS   Pandey,S., Singh,R., Habib,N., Kushwaha,R. and Mahdi,A.A.
  TITLE     Characterization, expression, and mutational analysis of endosomal
            protein lethal giant disc (Lgd/CC2D1A) as a biomarker in patients
            with T-cell acute lymphoblastic leukemia
  JOURNAL   Discov Oncol 16 (1), 2066 (2025)
   PUBMED   41212303
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 950)
  AUTHORS   Kim,A.H., Sakin,I., Viviano,S., Tuncel,G., Aguilera,S.M., Goles,G.,
            Jeffries,L., Ji,W., Lakhani,S.A., Kose,C.C., Silan,F., Oner,S.S.,
            Kaplan,O.I., Ergoren,M.C., Mishra-Gorur,K., Gunel,M., Sag,S.O.,
            Temel,S.G. and Deniz,E.
  CONSRTM   MarmaRare Group
  TITLE     CC2D1A causes ciliopathy, intellectual disability, heterotaxy,
            renal dysplasia, and abnormal CSF flow
  JOURNAL   Life Sci Alliance 7 (10), e202402708 (2024)
   PUBMED   39168639
  REMARK    GeneRIF: CC2D1A causes ciliopathy, intellectual disability,
            heterotaxy, renal dysplasia, and abnormal CSF flow.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 950)
  AUTHORS   Belokopytova,I.I., Kondaurova,E.M., Kulikova,E.A., Ilchibaeva,T.V.,
            Naumenko,V.S. and Popova,N.K.
  TITLE     Effects of the Cc2d1a/Freud-1 Knockdown in the Hippocampus of BTBR
            Mice on the Autistic-Like Behavior, Expression of Serotonin 5-HT1A
            and D2 Dopamine Receptors, and CREB and NF-kB Intracellular
            Signaling
  JOURNAL   Biochemistry (Mosc) 87 (10), 1206-1218 (2022)
   PUBMED   36273889
  REMARK    GeneRIF: Effects of the Cc2d1a/Freud-1 Knockdown in the Hippocampus
            of BTBR Mice on the Autistic-Like Behavior, Expression of Serotonin
            5-HT1A and D2 Dopamine Receptors, and CREB and NF-kB Intracellular
            Signaling.
REFERENCE   4  (residues 1 to 950)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 950)
  AUTHORS   Rogaeva,A. and Albert,P.R.
  TITLE     The mental retardation gene CC2D1A/Freud-1 encodes a long isoform
            that binds conserved DNA elements to repress gene transcription
  JOURNAL   Eur J Neurosci 26 (4), 965-974 (2007)
   PUBMED   17714190
  REMARK    GeneRIF: disruption of transcriptional regulation by mutation of
            Freud-1 may play a role in abnormal brain function leading to
            mental retardation
REFERENCE   6  (residues 1 to 950)
  AUTHORS   Basel-Vanagaite,L., Attia,R., Yahav,M., Ferland,R.J., Anteki,L.,
            Walsh,C.A., Olender,T., Straussberg,R., Magal,N., Taub,E.,
            Drasinover,V., Alkelai,A., Bercovich,D., Rechavi,G., Simon,A.J. and
            Shohat,M.
  TITLE     The CC2D1A, a member of a new gene family with C2 domains, is
            involved in autosomal recessive non-syndromic mental retardation
  JOURNAL   J Med Genet 43 (3), 203-210 (2006)
   PUBMED   16033914
  REMARK    GeneRIF: A protein truncating mutation was identified in the gene
            CC2D1A in nine consanguineous families with severe autosomal
            recessive mental retardation.
REFERENCE   7  (residues 1 to 950)
  AUTHORS   Albert,P.R. and Lemonde,S.
  TITLE     5-HT1A receptors, gene repression, and depression: guilt by
            association
  JOURNAL   Neuroscientist 10 (6), 575-593 (2004)
   PUBMED   15534042
  REMARK    GeneRIF: Review of Freud-1 as a repressor of serotonin 1A receptor
            gene.
            Review article
REFERENCE   8  (residues 1 to 950)
  AUTHORS   Lemonde,S., Rogaeva,A. and Albert,P.R.
  TITLE     Cell type-dependent recruitment of trichostatin A-sensitive
            repression of the human 5-HT1A receptor gene
  JOURNAL   J Neurochem 88 (4), 857-868 (2004)
   PUBMED   14756806
  REMARK    GeneRIF: Freud-1 mediates HDAC-independent repression of the 5-HT1A
            receptor promoter in neuronal 5-HT1A-positive cells.
REFERENCE   9  (residues 1 to 950)
  AUTHORS   Basel-Vanagaite,L., Alkelai,A., Straussberg,R., Magal,N., Inbar,D.,
            Mahajna,M. and Shohat,M.
  TITLE     Mapping of a new locus for autosomal recessive non-syndromic mental
            retardation in the chromosomal region 19p13.12-p13.2: further
            genetic heterogeneity
  JOURNAL   J Med Genet 40 (10), 729-732 (2003)
   PUBMED   14569116
REFERENCE   10 (residues 1 to 950)
  AUTHORS   Ou,X.M., Lemonde,S., Jafar-Nejad,H., Bown,C.D., Goto,A., Rogaeva,A.
            and Albert,P.R.
  TITLE     Freud-1: A neuronal calcium-regulated repressor of the 5-HT1A
            receptor gene
  JOURNAL   J Neurosci 23 (19), 7415-7425 (2003)
   PUBMED   12917378
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020916.8.
            
            On Aug 22, 2022 this sequence version replaced XP_047294969.1.
            
            Summary: This gene encodes a transcriptional repressor that binds
            to a conserved 14-bp 5'-repressor element and regulates expression
            of the 5-hydroxytryptamine (serotonin) receptor 1A gene in neuronal
            cells. The DNA binding and transcriptional repressor activities of
            the protein are inhibited by calcium. A mutation in this gene
            results in a nonsyndromic form of cognitive disability (MRT3).
            [provided by RefSeq, Jul 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4443853.1,
                                           SRR14038193.4450074.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..950
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..950
                     /product="coiled-coil and C2 domain-containing protein 1A
                     isoform 2"
                     /note="coiled-coil and C2 domain-containing protein 1A;
                     five repressor element under dual repression-binding
                     protein 1; Akt kinase-interacting protein 1; putative NFkB
                     activating protein; FRE under dual repression-binding
                     protein 1; putative NF-kappa-B-activating protein 023N;
                     five prime repressor element under dual repression-binding
                     protein 1; TBK1-associated protein in endolysosomes;
                     lethal (2) giant discs homolog 2"
                     /calculated_mol_wt=103804
     Region          80..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q66HA5; propagated from
                     UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Region          <116..477
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          140..195
                     /region_name="DM14"
                     /note="Repeats in fly CG4713, worm Y37H9A.3 and human
                     FLJ20241; smart00685"
                     /db_xref="CDD:128928"
     Region          185..266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:20171170,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Region          257..310
                     /region_name="DM14"
                     /note="Repeats in fly CG4713, worm Y37H9A.3 and human
                     FLJ20241; smart00685"
                     /db_xref="CDD:128928"
     Region          306..346
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Region          349..407
                     /region_name="DM14"
                     /note="Repeats in fly CG4713, worm Y37H9A.3 and human
                     FLJ20241; smart00685"
                     /db_xref="CDD:128928"
     Region          437..491
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Region          494..552
                     /region_name="DM14"
                     /note="Repeats in fly CG4713, worm Y37H9A.3 and human
                     FLJ20241; smart00685"
                     /db_xref="CDD:128928"
     Region          652..809
                     /region_name="C2_Freud-1"
                     /note="C2 domain found in 5' repressor element under dual
                     repression binding protein-1 (Freud-1); cd08690"
                     /db_xref="CDD:176072"
     Site            order(679,740,742,748,751)
                     /site_type="other"
                     /note="putative Ca2+ binding pocket [ion binding]"
                     /db_xref="CDD:176072"
     Region          850..917
                     /region_name="chemoreceptor_sensor"
                     /note="4-helix bundle ligand binding sensor domain of
                     chemoreceptors such as Tar or Tsr; cl00144"
                     /db_xref="CDD:444710"
     Site            order(853,905..906,908)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:438631"
     CDS             1..950
                     /gene="CC2D1A"
                     /gene_synonym="Aki-1; FREUD-1; Freud-1/Aki1; Lgd2; MRT3;
                     TAPE"
                     /coded_by="NM_001411138.1:242..3094"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS92537.1"
                     /db_xref="GeneID:54862"
                     /db_xref="HGNC:HGNC:30237"
                     /db_xref="MIM:610055"
ORIGIN      
        1 mhkrkgppgp pgrgaaaarq lgllvdlspd glmipedgan deeleaefla lvggqppale
       61 klkgkgplpm eaiekmaslc mrdpdedeee gtdeddlead ddllaelnev lgeeqkaset
      121 pppvaqpkpe aphpglettl qerlalyqta iesarqagds akmrrydrgl ktlenllasi
      181 rkgnaidead ipppvaigkg pastptyspa ptqpaprias apeprvtleg psatapassp
      241 glakpqmppg pcspgplaql qsrqrdykla alhakqqgdt taaarhfrva ksfdavleal
      301 srgepvdlsc lppppdqlpp dppsppsqpp tpatapstte vpppprtlle aleqrmeryq
      361 vaaaqakskg dqrkarmher ivkqyqdair ahkagravdv aelpvppgfp piqgleatkp
      421 tqqslvgvle tamklanqde gpedeedevp kkqnspvapt aqpkappsrt pqsgsaptak
      481 appkatstra qqqlaflegr kkqllqaalr akqkndvega kmhlrqakgl epmleasrng
      541 lpvditkvpp apvnkddfal vqrpgpglsq eaarrygelt klirqqhemc lnhsnqftql
      601 gnitettkfe klaedckrsm dilkqafvrg lptptarfeq rtfsvikifp dlssndmllf
      661 ivkginlptp pglspgdldv fvrfdfpypn veeaqkdkts vikntdspef keqfklcinr
      721 shrgfrraiq tkgikfevvh kgglfktdrv lgtaqlklda leiacevrei levldgrrpt
      781 ggrlevmvri repltaqqle ttterwlvid pvpaavptva gpkgkappvp aparesgnrs
      841 arplhslsvl afdqerlerk ilalrqarrp vppevaqqyq dimqrsqwqr aqleqggvgi
      901 rreyaaqler qlqfyteaar rlgndgsrda akealyrrnl veselqrlrr
//
LOCUS       NP_060191                951 aa            linear   PRI 26-NOV-2025
DEFINITION  coiled-coil and C2 domain-containing protein 1A isoform 1 [Homo
            sapiens].
ACCESSION   NP_060191
VERSION     NP_060191.3
DBSOURCE    REFSEQ: accession NM_017721.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 951)
  AUTHORS   Pandey,S., Singh,R., Habib,N., Kushwaha,R. and Mahdi,A.A.
  TITLE     Characterization, expression, and mutational analysis of endosomal
            protein lethal giant disc (Lgd/CC2D1A) as a biomarker in patients
            with T-cell acute lymphoblastic leukemia
  JOURNAL   Discov Oncol 16 (1), 2066 (2025)
   PUBMED   41212303
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 951)
  AUTHORS   Kim,A.H., Sakin,I., Viviano,S., Tuncel,G., Aguilera,S.M., Goles,G.,
            Jeffries,L., Ji,W., Lakhani,S.A., Kose,C.C., Silan,F., Oner,S.S.,
            Kaplan,O.I., Ergoren,M.C., Mishra-Gorur,K., Gunel,M., Sag,S.O.,
            Temel,S.G. and Deniz,E.
  CONSRTM   MarmaRare Group
  TITLE     CC2D1A causes ciliopathy, intellectual disability, heterotaxy,
            renal dysplasia, and abnormal CSF flow
  JOURNAL   Life Sci Alliance 7 (10), e202402708 (2024)
   PUBMED   39168639
  REMARK    GeneRIF: CC2D1A causes ciliopathy, intellectual disability,
            heterotaxy, renal dysplasia, and abnormal CSF flow.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 951)
  AUTHORS   Belokopytova,I.I., Kondaurova,E.M., Kulikova,E.A., Ilchibaeva,T.V.,
            Naumenko,V.S. and Popova,N.K.
  TITLE     Effects of the Cc2d1a/Freud-1 Knockdown in the Hippocampus of BTBR
            Mice on the Autistic-Like Behavior, Expression of Serotonin 5-HT1A
            and D2 Dopamine Receptors, and CREB and NF-kB Intracellular
            Signaling
  JOURNAL   Biochemistry (Mosc) 87 (10), 1206-1218 (2022)
   PUBMED   36273889
  REMARK    GeneRIF: Effects of the Cc2d1a/Freud-1 Knockdown in the Hippocampus
            of BTBR Mice on the Autistic-Like Behavior, Expression of Serotonin
            5-HT1A and D2 Dopamine Receptors, and CREB and NF-kB Intracellular
            Signaling.
REFERENCE   4  (residues 1 to 951)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 951)
  AUTHORS   Rogaeva,A. and Albert,P.R.
  TITLE     The mental retardation gene CC2D1A/Freud-1 encodes a long isoform
            that binds conserved DNA elements to repress gene transcription
  JOURNAL   Eur J Neurosci 26 (4), 965-974 (2007)
   PUBMED   17714190
  REMARK    GeneRIF: disruption of transcriptional regulation by mutation of
            Freud-1 may play a role in abnormal brain function leading to
            mental retardation
REFERENCE   6  (residues 1 to 951)
  AUTHORS   Basel-Vanagaite,L., Attia,R., Yahav,M., Ferland,R.J., Anteki,L.,
            Walsh,C.A., Olender,T., Straussberg,R., Magal,N., Taub,E.,
            Drasinover,V., Alkelai,A., Bercovich,D., Rechavi,G., Simon,A.J. and
            Shohat,M.
  TITLE     The CC2D1A, a member of a new gene family with C2 domains, is
            involved in autosomal recessive non-syndromic mental retardation
  JOURNAL   J Med Genet 43 (3), 203-210 (2006)
   PUBMED   16033914
  REMARK    GeneRIF: A protein truncating mutation was identified in the gene
            CC2D1A in nine consanguineous families with severe autosomal
            recessive mental retardation.
REFERENCE   7  (residues 1 to 951)
  AUTHORS   Albert,P.R. and Lemonde,S.
  TITLE     5-HT1A receptors, gene repression, and depression: guilt by
            association
  JOURNAL   Neuroscientist 10 (6), 575-593 (2004)
   PUBMED   15534042
  REMARK    GeneRIF: Review of Freud-1 as a repressor of serotonin 1A receptor
            gene.
            Review article
REFERENCE   8  (residues 1 to 951)
  AUTHORS   Lemonde,S., Rogaeva,A. and Albert,P.R.
  TITLE     Cell type-dependent recruitment of trichostatin A-sensitive
            repression of the human 5-HT1A receptor gene
  JOURNAL   J Neurochem 88 (4), 857-868 (2004)
   PUBMED   14756806
  REMARK    GeneRIF: Freud-1 mediates HDAC-independent repression of the 5-HT1A
            receptor promoter in neuronal 5-HT1A-positive cells.
REFERENCE   9  (residues 1 to 951)
  AUTHORS   Basel-Vanagaite,L., Alkelai,A., Straussberg,R., Magal,N., Inbar,D.,
            Mahajna,M. and Shohat,M.
  TITLE     Mapping of a new locus for autosomal recessive non-syndromic mental
            retardation in the chromosomal region 19p13.12-p13.2: further
            genetic heterogeneity
  JOURNAL   J Med Genet 40 (10), 729-732 (2003)
   PUBMED   14569116
REFERENCE   10 (residues 1 to 951)
  AUTHORS   Ou,X.M., Lemonde,S., Jafar-Nejad,H., Bown,C.D., Goto,A., Rogaeva,A.
            and Albert,P.R.
  TITLE     Freud-1: A neuronal calcium-regulated repressor of the 5-HT1A
            receptor gene
  JOURNAL   J Neurosci 23 (19), 7415-7425 (2003)
   PUBMED   12917378
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB065701.1 and BC064981.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 16, 2006 this sequence version replaced NP_060191.2.
            
            Summary: This gene encodes a transcriptional repressor that binds
            to a conserved 14-bp 5'-repressor element and regulates expression
            of the 5-hydroxytryptamine (serotonin) receptor 1A gene in neuronal
            cells. The DNA binding and transcriptional repressor activities of
            the protein are inhibited by calcium. A mutation in this gene
            results in a nonsyndromic form of cognitive disability (MRT3).
            [provided by RefSeq, Jul 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB097002.1, AK315068.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000318003.11/ ENSP00000313601.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..951
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..951
                     /product="coiled-coil and C2 domain-containing protein 1A
                     isoform 1"
                     /note="coiled-coil and C2 domain-containing protein 1A;
                     five repressor element under dual repression-binding
                     protein 1; Akt kinase-interacting protein 1; putative NFkB
                     activating protein; FRE under dual repression-binding
                     protein 1; putative NF-kappa-B-activating protein 023N;
                     five prime repressor element under dual repression-binding
                     protein 1; TBK1-associated protein in endolysosomes;
                     lethal (2) giant discs homolog 2"
                     /calculated_mol_wt=103932
     Region          80..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q66HA5; propagated from
                     UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Region          <116..477
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          140..195
                     /region_name="DM14"
                     /note="Repeats in fly CG4713, worm Y37H9A.3 and human
                     FLJ20241; smart00685"
                     /db_xref="CDD:128928"
     Region          185..266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:20171170,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Region          257..310
                     /region_name="DM14"
                     /note="Repeats in fly CG4713, worm Y37H9A.3 and human
                     FLJ20241; smart00685"
                     /db_xref="CDD:128928"
     Region          306..346
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Region          349..407
                     /region_name="DM14"
                     /note="Repeats in fly CG4713, worm Y37H9A.3 and human
                     FLJ20241; smart00685"
                     /db_xref="CDD:128928"
     Region          437..491
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Region          494..552
                     /region_name="DM14"
                     /note="Repeats in fly CG4713, worm Y37H9A.3 and human
                     FLJ20241; smart00685"
                     /db_xref="CDD:128928"
     Region          652..809
                     /region_name="C2_Freud-1"
                     /note="C2 domain found in 5' repressor element under dual
                     repression binding protein-1 (Freud-1); cd08690"
                     /db_xref="CDD:176072"
     Site            order(679,740,742,748,751)
                     /site_type="other"
                     /note="putative Ca2+ binding pocket [ion binding]"
                     /db_xref="CDD:176072"
     Region          818..841
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P1N0.1)"
     Region          851..918
                     /region_name="chemoreceptor_sensor"
                     /note="4-helix bundle ligand binding sensor domain of
                     chemoreceptors such as Tar or Tsr; cl00144"
                     /db_xref="CDD:444710"
     Site            order(854,906..907,909)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:438631"
     CDS             1..951
                     /gene="CC2D1A"
                     /gene_synonym="Aki-1; FREUD-1; Freud-1/Aki1; Lgd2; MRT3;
                     TAPE"
                     /coded_by="NM_017721.5:242..3097"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42512.1"
                     /db_xref="GeneID:54862"
                     /db_xref="HGNC:HGNC:30237"
                     /db_xref="MIM:610055"
ORIGIN      
        1 mhkrkgppgp pgrgaaaarq lgllvdlspd glmipedgan deeleaefla lvggqppale
       61 klkgkgplpm eaiekmaslc mrdpdedeee gtdeddlead ddllaelnev lgeeqkaset
      121 pppvaqpkpe aphpglettl qerlalyqta iesarqagds akmrrydrgl ktlenllasi
      181 rkgnaidead ipppvaigkg pastptyspa ptqpaprias apeprvtleg psatapassp
      241 glakpqmppg pcspgplaql qsrqrdykla alhakqqgdt taaarhfrva ksfdavleal
      301 srgepvdlsc lppppdqlpp dppsppsqpp tpatapstte vpppprtlle aleqrmeryq
      361 vaaaqakskg dqrkarmher ivkqyqdair ahkagravdv aelpvppgfp piqgleatkp
      421 tqqslvgvle tamklanqde gpedeedevp kkqnspvapt aqpkappsrt pqsgsaptak
      481 appkatstra qqqlaflegr kkqllqaalr akqkndvega kmhlrqakgl epmleasrng
      541 lpvditkvpp apvnkddfal vqrpgpglsq eaarrygelt klirqqhemc lnhsnqftql
      601 gnitettkfe klaedckrsm dilkqafvrg lptptarfeq rtfsvikifp dlssndmllf
      661 ivkginlptp pglspgdldv fvrfdfpypn veeaqkdkts vikntdspef keqfklcinr
      721 shrgfrraiq tkgikfevvh kgglfktdrv lgtaqlklda leiacevrei levldgrrpt
      781 ggrlevmvri repltaqqle ttterwlvid pvpaavptqv agpkgkappv paparesgnr
      841 sarplhslsv lafdqerler kilalrqarr pvppevaqqy qdimqrsqwq raqleqggvg
      901 irreyaaqle rqlqfyteaa rrlgndgsrd aakealyrrn lveselqrlr r
//
LOCUS       NP_037407               2663 aa            linear   PRI 27-NOV-2025
DEFINITION  ankyrin repeat domain-containing protein 11 [Homo sapiens].
ACCESSION   NP_037407
VERSION     NP_037407.4
DBSOURCE    REFSEQ: accession NM_013275.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2663)
  AUTHORS   He,D., Zhang,M., Li,Y., Liu,F. and Ban,B.
  TITLE     Insights into the ANKRD11 variants and short-stature phenotype
            through literature review and ClinVar database search
  JOURNAL   Orphanet J Rare Dis 19 (1), 292 (2024)
   PUBMED   39135054
  REMARK    GeneRIF: Insights into the ANKRD11 variants and short-stature
            phenotype through literature review and ClinVar database search.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2663)
  AUTHORS   Chen,M., Yang,X., Liu,H. and Wan,J.
  TITLE     Identification and functional characterization of a bipartite
            nuclear localization signal in ANKRD11
  JOURNAL   Biochem Biophys Res Commun 670, 117-123 (2023)
   PUBMED   37290286
  REMARK    GeneRIF: Identification and functional characterization of a
            bipartite nuclear localization signal in ANKRD11.
REFERENCE   3  (residues 1 to 2663)
  AUTHORS   Yuan,M., Barefoot,M.E., Peterson,K., Campbell,M.J., Blancato,J.K.,
            Chen,M., Schmidt,M.O., Kiliti,A.J., Fang,H.B., Wellstein,A.,
            Riegel,A.T. and Sharif,G.M.
  TITLE     Loss of ANCO1 Expression Regulates Chromatin Accessibility and
            Drives Progression of Early-Stage Triple-Negative Breast Cancer
  JOURNAL   Int J Mol Sci 24 (14), 11505 (2023)
   PUBMED   37511268
  REMARK    GeneRIF: Loss of ANCO1 Expression Regulates Chromatin Accessibility
            and Drives Progression of Early-Stage Triple-Negative Breast
            Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2663)
  AUTHORS   Borja,N., Zafeer,M.F., Rodriguez,J.A., Morel Swols,D., Thorson,W.,
            Bademci,G. and Tekin,M.
  TITLE     Deletion of first noncoding exon in ANKRD11 leads to KBG syndrome
  JOURNAL   Am J Med Genet A 191 (4), 1044-1049 (2023)
   PUBMED   36628575
  REMARK    GeneRIF: Deletion of first noncoding exon in ANKRD11 leads to KBG
            syndrome.
            Review article
REFERENCE   5  (residues 1 to 2663)
  AUTHORS   Wang,L., Li,J., Xu,J., Xu,Y., Wang,J., Feng,Y. and Kong,X.
  TITLE     [Clinical and genetic analysis of three children with KBG syndrome
            due to novel variants of ANKRD11 gene]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 40 (1), 1-6 (2023)
   PUBMED   36584991
  REMARK    GeneRIF: [Clinical and genetic analysis of three children with KBG
            syndrome due to novel variants of ANKRD11 gene].
REFERENCE   6  (residues 1 to 2663)
  AUTHORS   Willemsen,M.H., Fernandez,B.A., Bacino,C.A., Gerkes,E., de
            Brouwer,A.P., Pfundt,R., Sikkema-Raddatz,B., Scherer,S.W.,
            Marshall,C.R., Potocki,L., van Bokhoven,H. and Kleefstra,T.
  TITLE     Identification of ANKRD11 and ZNF778 as candidate genes for autism
            and variable cognitive impairment in the novel 16q24.3
            microdeletion syndrome
  JOURNAL   Eur J Hum Genet 18 (4), 429-435 (2010)
   PUBMED   19920853
  REMARK    GeneRIF: ANKRD11 is a candidate gene for autism and variable
            cognitive impairment in the novel 16q24.3 microdeletion syndrome.
REFERENCE   7  (residues 1 to 2663)
  AUTHORS   Neilsen,P.M., Cheney,K.M., Li,C.W., Chen,J.D., Cawrse,J.E.,
            Schulz,R.B., Powell,J.A., Kumar,R. and Callen,D.F.
  TITLE     Identification of ANKRD11 as a p53 coactivator
  JOURNAL   J Cell Sci 121 (Pt 21), 3541-3552 (2008)
   PUBMED   18840648
  REMARK    GeneRIF: ANKRD11 has a role as a p53 coactivator and may be
            involved in a regulatory feedback loop with p53
REFERENCE   8  (residues 1 to 2663)
  AUTHORS   Zhang,A., Li,C.W. and Chen,J.D.
  TITLE     Characterization of transcriptional regulatory domains of ankyrin
            repeat cofactor-1
  JOURNAL   Biochem Biophys Res Commun 358 (4), 1034-1040 (2007)
   PUBMED   17521611
  REMARK    GeneRIF: Together, these results indicate that the transcriptional
            potential of ANCO-1 may be modulated by a combination of repression
            and activation signals.
REFERENCE   9  (residues 1 to 2663)
  AUTHORS   Zhang,A., Yeung,P.L., Li,C.W., Tsai,S.C., Dinh,G.K., Wu,X., Li,H.
            and Chen,J.D.
  TITLE     Identification of a novel family of ankyrin repeats containing
            cofactors for p160 nuclear receptor coactivators
  JOURNAL   J Biol Chem 279 (32), 33799-33805 (2004)
   PUBMED   15184363
REFERENCE   10 (residues 1 to 2663)
  AUTHORS   Morel Swols,D. and Tekin,M.
  TITLE     KBG Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29565525
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY373756.1, BC017437.1,
            AY533563.1 and DA172996.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 16, 2004 this sequence version replaced NP_037407.3.
            
            Summary: This locus encodes an ankryin repeat domain-containing
            protein. The encoded protein inhibits ligand-dependent activation
            of transcription. Mutations in this gene have been associated with
            KBG syndrome, which is characterized by macrodontia, distinctive
            craniofacial features, short stature, skeletal anomalies, global
            developmental delay, seizures and intellectual disability.
            Alternatively spliced transcript variants have been described.
            Related pseudogenes exist on chromosomes 2 and X. [provided by
            RefSeq, Jan 2012].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AY533563.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301030.10/ ENSP00000301030.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2663
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..2663
                     /product="ankyrin repeat domain-containing protein 11"
                     /note="nasopharyngeal carcinoma susceptibility protein;
                     ankyrin repeat-containing cofactor 1; ankyrin repeats
                     containing cofactor 1; ankyrin repeat domain containing
                     11"
                     /calculated_mol_wt=297784
     Region          1..90
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          128..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          <158..>287
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(167,169,173..174,177..179,181..182,186,189,198,200,
                     202,206..207,210..212,214..215,219,222,231,233,235,
                     239..240,243..245,247..248,252,255)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          167..198
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          167..196
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          200..231
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          200..229
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          233..262
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          233..261
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          266..292
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          289..380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          398..647
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          <583..789
                     /region_name="PTZ00108"
                     /note="DNA topoisomerase 2-like protein; Provisional"
                     /db_xref="CDD:240271"
     Region          <694..1308
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          723..783
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          881..1043
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          1059..1393
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1079
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4F7; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1120
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1419
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          1424..1710
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          <1691..2354
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4F7; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1792
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          1814..1836
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1847
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1850
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4F7; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1851
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4F7; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1852
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4F7; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1859
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          1988..2019
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1990
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          2131..2406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          2369..2663
                     /region_name="Important for protein degradation.
                     /evidence=ECO:0000269|PubMed:25413698"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     CDS             1..2663
                     /gene="ANKRD11"
                     /gene_synonym="ANCO-1; ANCO1; LZ16; T13"
                     /coded_by="NM_013275.6:462..8453"
                     /db_xref="CCDS:CCDS32513.1"
                     /db_xref="GeneID:29123"
                     /db_xref="HGNC:HGNC:21316"
                     /db_xref="MIM:611192"
ORIGIN      
        1 mpkggcpkap qqeelplssd mvekqtgkkd kdkvsltktp klergdggke vreraskrkl
       61 pftagangeq kdsdtekqgp erkrikkepv trkagllfgm glsgiragyp lserqqvall
      121 mqmtaeesan spvdttpkhp sqstvcqkgt pnsasktkdk vnkrnerget rlhraairgd
      181 arrikelise gadvnvkdfa gwtalheacn rgyydvakql laagaevntk gldddtplhd
      241 aannghykvv klllryggnp qqsnrkgetp lkvansptmv nlllgkgtyt sseesstess
      301 eeedapsfap sssvdgnntd sefekglkhk aknpepqkat apvkdeyefd eddeqdrvpp
      361 vddkhllkkd yrketksnsf isipkmevks ytknntiapk kashrilsdt sdeedasvtv
      421 gtgeklrlsa htilpgsktr epsnakqqke knkvkkkrkk etkgrevrfg krsdkfcsse
      481 sesessesge ddrdslgssg clkgsplvlk dpslfsslsa sstsshgssa aqkqnpshtd
      541 qhtkhwrtdn wktisspaws evsslsdstr trltsesdys segssveslk pvrkrqehrk
      601 raslsekksp flssaegavp kldkegkvvk khktkhkhkn kekgqcsisq elklksftye
      661 yedskqksdk aillendlst enklkvlkhd rdhfkkeekl skmkleekew lfkdekslkr
      721 ikdtnkdisr sfreekdrsn kaekerslke kspkeeklrl ykeerkkksk drpsklekkn
      781 dlkedkiske kekifkedke klkkekvyre dsafdeycnk nqflenedtk fslsddqrdr
      841 wfsdlsdssf dfkgedswds pvtdyrdmks dsvaklilet vkedskerrr dsrarekrdy
      901 repffrkkdr dyldknsekr keqtekhksv pgylsekdkk rresaeagrd rkdalescke
      961 rrdgrakpee ahreelkecg cesgfkdksd gdfgkglepw erhhpareke kkdgpdkerk
     1021 ektkperyke kssdkdksek silekcqkdk efdkcfkekk dtkekhkdth gkdkerkasl
     1081 dqgkekkeka fpgiisedfs ekkddkkgke kswyiadift deseddrdsc mgsgfkmgea
     1141 sdlprtdglq ekeegreaya sdrhrkssdk qhperqkdke prdrrkdrga adagrdkkek
     1201 vfekhkekkd kestekykdr kdrasvdstq dkknkqklpe kaekkhaaed kakskhkeks
     1261 dkehskerks srsadaeksl lekleeealh eyredsndki sevssdsftd rgqepgltaf
     1321 levsfteppg ddkpresacl peklkekerh rhssssskks hdrerakkek aekkekgedy
     1381 keggsrkdsg qyekdflead aygvsynmka diedeldkti elfstekkdk ndserepskk
     1441 iekelkpygs sainilkekk krekhrekwr dekerhrdrh adgllrhhrd ellrhhrdeq
     1501 kpatrdkdsp prvlkdksrd egprlgdakl kekfkdgaek ekgdpvkmsn gndkvapskd
     1561 pgkkdarpre kllgdgdlmm tsfermlsqk dleieerhkr hkermkqmek lrhrsgdpkl
     1621 kekakpaddg rkkgldipak kppgldppfk dkklkestpi ppaaenklhp asgadskdwl
     1681 agphmkevlp asprpdqsrp tgvptptsvl scpsyeevmh tprtpscsad dyadlvfdca
     1741 dsqhstpvpt aptsacspsf fdrfsvassg lsenasqapa rplstnlyrs vsvdirrtpe
     1801 eefsvgdklf rqqsvpaass ydspmppsme draplppvpa ekfaclspgy yspdyglpsp
     1861 kvdalhcppa avvtvtpspe gvfsslqakp spspraellv pslegalppd ldtsedqqat
     1921 aaiippepsy lepldegpfs aviteepvew ahpseqalas sliggtsenp vswpvgsdll
     1981 lkspqrfpes pkrfcpadpl hsaapgpfsa seapypappa spapyalpva epgledvkdg
     2041 vdavpaaist seaapyapps glesffsnck slpeapldva pepacvaava qvealgplen
     2101 sfldgsrgls hlgqvepvpw adafagpedd ldlgpfslpe lplqtkdaad geaepveesl
     2161 appeemppga pgvinggdvs tvvaeeppal ppdqastrlp aelepepsge pkldvaleaa
     2221 veaetvpeer argdpdssve papvppeqrp lgsgdqgaea egppaaslca pdgpapntva
     2281 qaqaadgagp eddteasraa apaegppggi qpeaaepkpt aeapkaprve eipqrmtrnr
     2341 aqmlanqskq gpppsekeca ptpapvtrak argsedddaq aqhprkrrfq rstqqlqqql
     2401 ntstqqtrev iqqtlaaivd aikldaiepy hsdranpyfe ylqirkkiee krkilccitp
     2461 qapqcyaeyv tytgsylldg kplsklhipv iapppslaep lkelfrqqea vrgklrlqhs
     2521 iereklivsc eqeilrvhcr aartianqav pfsactmlld sevynmples qgdenksvrd
     2581 rfnarqfisw lqdvddkydr mktcllmrqq heaaalnavq rmewqlkvqe ldpaghkslc
     2641 vnevpsfyvp mvdvnddfvl lpa
//
LOCUS       NP_001185625             373 aa            linear   PRI 27-NOV-2025
DEFINITION  ferroptosis suppressor protein 1 [Homo sapiens].
ACCESSION   NP_001185625
VERSION     NP_001185625.1
DBSOURCE    REFSEQ: accession NM_001198696.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Yang,J.S., Morris,A.J., Kamizaki,K., Chen,J., Stark,J.,
            Oldham,W.M., Nakamura,T., Mishima,E., Loscalzo,J., Minami,Y.,
            Conrad,M., Henry,W.S. and Hsu,V.W.
  TITLE     ALDH7A1 protects against ferroptosis by generating membrane NADH
            and regulating FSP1
  JOURNAL   Cell 188 (10), 2569-2585 (2025)
   PUBMED   40233740
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Lan,H., Gao,Y., Hong,T., Chang,Z., Zhao,Z., Wang,Y. and Wang,F.
  TITLE     Structural insight into 6-OH-FAD-dependent activation of hFSP1 for
            ferroptosis suppression
  JOURNAL   Cell Discov 10 (1), 88 (2024)
   PUBMED   39160155
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Tan,Y.R., Jiang,B.H., Feng,W.J., He,Z.L., Jiang,Y.L., Xun,Y.,
            Wu,X.P., Li,Y.H. and Zhu,H.B.
  TITLE     Circ0060467 sponges miR-6805 to promote hepatocellular carcinoma
            progression through regulating AIFM2 and GPX4 expression
  JOURNAL   Aging (Albany NY) 16 (2), 1796-1807 (2024)
   PUBMED   38244593
  REMARK    GeneRIF: Circ0060467 sponges miR-6805 to promote hepatocellular
            carcinoma progression through regulating AIFM2 and GPX4 expression.
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Yuan,S., Xi,S., Weng,H., Guo,M.M., Zhang,J.H., Yu,Z.P., Zhang,H.,
            Yu,Z., Xing,Z., Liu,M.Y., Ming,D.J., Sah,R.K., Zhou,Y., Li,G.,
            Zeng,T., Hong,X., Li,Y., Zeng,X.T. and Hu,H.
  TITLE     YTHDC1 as a tumor progression suppressor through modulating
            FSP1-dependent ferroptosis suppression in lung cancer
  JOURNAL   Cell Death Differ 30 (12), 2477-2490 (2023)
   PUBMED   37903990
  REMARK    GeneRIF: YTHDC1 as a tumor progression suppressor through
            modulating FSP1-dependent ferroptosis suppression in lung cancer.
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Nakamura,T., Mishima,E., Yamada,N., Mourao,A.S.D., Trumbach,D.,
            Doll,S., Wanninger,J., Lytton,E., Sennhenn,P., Nishida Xavier da
            Silva,T., Angeli,J.P.F., Sattler,M., Proneth,B. and Conrad,M.
  TITLE     Integrated chemical and genetic screens unveil FSP1 mechanisms of
            ferroptosis regulation
  JOURNAL   Nat Struct Mol Biol 30 (11), 1806-1815 (2023)
   PUBMED   37957306
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Wu,M., Xu,L.G., Su,T., Tian,Y., Zhai,Z. and Shu,H.B.
  TITLE     AMID is a p53-inducible gene downregulated in tumors
  JOURNAL   Oncogene 23 (40), 6815-6819 (2004)
   PUBMED   15273740
  REMARK    GeneRIF: AMID is a p53-downstream gene involved in tumorigenesis.
REFERENCE   7  (residues 1 to 373)
  AUTHORS   Fujimoto,Y., Itabe,H., Sakai,J., Makita,M., Noda,J., Mori,M.,
            Higashi,Y., Kojima,S. and Takano,T.
  TITLE     Identification of major proteins in the lipid droplet-enriched
            fraction isolated from the human hepatocyte cell line HuH7
  JOURNAL   Biochim Biophys Acta 1644 (1), 47-59 (2004)
   PUBMED   14741744
REFERENCE   8  (residues 1 to 373)
  AUTHORS   Ohiro,Y., Garkavtsev,I., Kobayashi,S., Sreekumar,K.R., Nantz,R.,
            Higashikubo,B.T., Duffy,S.L., Higashikubo,R., Usheva,A., Gius,D.,
            Kley,N. and Horikoshi,N.
  TITLE     A novel p53-inducible apoptogenic gene, PRG3, encodes a homologue
            of the apoptosis-inducing factor (AIF)
  JOURNAL   FEBS Lett 524 (1-3), 163-171 (2002)
   PUBMED   12135761
  REMARK    GeneRIF: encodes a homologue of the apoptosis-inducing factor
REFERENCE   9  (residues 1 to 373)
  AUTHORS   Wu,M., Xu,L.G., Li,X., Zhai,Z. and Shu,H.B.
  TITLE     AMID, an apoptosis-inducing factor-homologous
            mitochondrion-associated protein, induces caspase-independent
            apoptosis
  JOURNAL   J Biol Chem 277 (28), 25617-25623 (2002)
   PUBMED   11980907
  REMARK    GeneRIF: induces caspase-independent apoptosis
REFERENCE   10 (residues 1 to 373)
  AUTHORS   Horikoshi,N., Cong,J., Kley,N. and Shenk,T.
  TITLE     Isolation of differentially expressed cDNAs from p53-dependent
            apoptotic cells: activation of the human homologue of the
            Drosophila peroxidasin gene
  JOURNAL   Biochem Biophys Res Commun 261 (3), 864-869 (1999)
   PUBMED   10441517
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP331371.1, BC023601.2,
            AL731540.4 and AI922797.1.
            
            Summary: This gene encodes a flavoprotein oxidoreductase that binds
            single stranded DNA and is thought to contribute to apoptosis in
            the presence of bacterial and viral DNA. The expression of this
            gene is also found to be induced by tumor suppressor protein p53 in
            colon cancer cells. [provided by RefSeq, Nov 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3856354.1,
                                           SRR14038194.2806033.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..373
                     /product="ferroptosis suppressor protein 1"
                     /note="apoptosis-inducing factor (AIF)-like
                     mitochondrion-associated inducer of death;
                     apoptosis-inducing factor 2; p53-responsive gene 3
                     protein; apoptosis-inducing factor,
                     mitochondrion-associated, 2; ferroptosis suppressor 1;
                     apoptosis inducing factor mitochondria associated 2; AIF
                     family member 2"
                     /calculated_mol_wt=40396
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRQ8.1)"
     Region          76..355
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
     Site            168
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by KAT2B.
                     /evidence=ECO:0000269|PubMed:39881208; propagated from
                     UniProtKB/Swiss-Prot (Q9BRQ8.1)"
     Site            174
                     /site_type="other"
                     /note="4-hydroxy-2-nonenal adduction.
                     /evidence=ECO:0000250|UniProtKB:Q8BUE4; propagated from
                     UniProtKB/Swiss-Prot (Q9BRQ8.1)"
     CDS             1..373
                     /gene="AIFM2"
                     /gene_synonym="AMID; FSP1; PRG3"
                     /coded_by="NM_001198696.2:109..1230"
                     /db_xref="CCDS:CCDS7297.1"
                     /db_xref="GeneID:84883"
                     /db_xref="HGNC:HGNC:21411"
                     /db_xref="MIM:605159"
ORIGIN      
        1 mgsqvsvesg alhvvivggg fggiaaasql qalnvpfmlv dmkdsfhhnv aalrasvetg
       61 fakktfisys vtfkdnfrqg lvvgidlknq mvllqggeal pfshlilatg stgpfpgkfn
      121 evssqqaaiq ayedmvrqvq rsrfivvvgg gsagvemaae ikteypekev tlihsqvala
      181 dkellpsvrq evkeillrkg vqlllservs nleelplney reyikvqtdk gtevatnlvi
      241 lctgikinss ayrkafesrl assgalrvne hlqveghsnv yaigdcadvr tpkmaylagl
      301 haniavaniv nsvkqrplqa ykpgaltfll smgrndgvgq isgfyvgrlm vrltksrdlf
      361 vstswktmrq spp
//
LOCUS       NP_001308641            1395 aa            linear   PRI 27-NOV-2025
DEFINITION  nuclear receptor coactivator 2 isoform b [Homo sapiens].
ACCESSION   NP_001308641
VERSION     NP_001308641.1
DBSOURCE    REFSEQ: accession NM_001321712.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1395)
  AUTHORS   Yu,X., Wang,X., Ma,K., Gao,D., Deng,Y., Zhou,D., Ding,W., Zhao,Y.,
            Liu,Q. and Zhou,Z.
  TITLE     Tai/NCOA2 suppresses the Hedgehog pathway by directly targeting the
            transcription factor Ci/GLI
  JOURNAL   Proc Natl Acad Sci U S A 121 (47), e2409380121 (2024)
   PUBMED   39531503
REFERENCE   2  (residues 1 to 1395)
  AUTHORS   Warmke,L.M., Mustafa,A., Zou,Y.S., Davis,J.L., Ulbright,T.M. and
            Segura,S.E.
  TITLE     Myxoid epithelioid smooth muscle tumor of the vulva: A distinct
            entity with MEF2D::NCOA2 gene fusion
  JOURNAL   Genes Chromosomes Cancer 63 (1), e23209 (2024)
   PUBMED   37870842
  REMARK    GeneRIF: Myxoid epithelioid smooth muscle tumor of the vulva: A
            distinct entity with MEF2D::NCOA2 gene fusion.
REFERENCE   3  (residues 1 to 1395)
  AUTHORS   Watson,S., LaVigne,C.A., Xu,L., Surdez,D., Cyrta,J., Calderon,D.,
            Cannon,M.V., Kent,M.R., Silvius,K.M., Kucinski,J.P., Harrison,E.N.,
            Murchison,W., Rakheja,D., Tirode,F., Delattre,O., Amatruda,J.F. and
            Kendall,G.C.
  TITLE     VGLL2-NCOA2 leverages developmental programs for pediatric
            sarcomagenesis
  JOURNAL   Cell Rep 42 (1), 112013 (2023)
   PUBMED   36656711
  REMARK    GeneRIF: VGLL2-NCOA2 leverages developmental programs for pediatric
            sarcomagenesis.
REFERENCE   4  (residues 1 to 1395)
  AUTHORS   Wang,L., Motoi,T., Khanin,R., Olshen,A., Mertens,F., Bridge,J., Dal
            Cin,P., Antonescu,C.R., Singer,S., Hameed,M., Bovee,J.V.,
            Hogendoorn,P.C., Socci,N. and Ladanyi,M.
  TITLE     Identification of a novel, recurrent HEY1-NCOA2 fusion in
            mesenchymal chondrosarcoma based on a genome-wide screen of
            exon-level expression data
  JOURNAL   Genes Chromosomes Cancer 51 (2), 127-139 (2012)
   PUBMED   22034177
  REMARK    GeneRIF: The novel HEY1-NCOA2 fusion appears to be the defining and
            diagnostic gene fusion in mesenchymal chondrosarcomas
REFERENCE   5  (residues 1 to 1395)
  AUTHORS   Strehl,S., Nebral,K., Konig,M., Harbott,J., Strobl,H., Ratei,R.,
            Struski,S., Bielorai,B., Lessard,M., Zimmermann,M., Haas,O.A. and
            Izraeli,S.
  TITLE     ETV6-NCOA2: a novel fusion gene in acute leukemia associated with
            coexpression of T-lymphoid and myeloid markers and frequent NOTCH1
            mutations
  JOURNAL   Clin Cancer Res 14 (4), 977-983 (2008)
   PUBMED   18281529
  REMARK    GeneRIF: ETV6-NCOA2 fusion may define a novel subgroup of acute
            leukemia with T-lymphoid and myeloid features, which is associated
            with a high prevalence of NOTCH1 mutations.
REFERENCE   6  (residues 1 to 1395)
  AUTHORS   Fryer,C.J. and Archer,T.K.
  TITLE     Chromatin remodelling by the glucocorticoid receptor requires the
            BRG1 complex
  JOURNAL   Nature 393 (6680), 88-91 (1998)
   PUBMED   9590696
REFERENCE   7  (residues 1 to 1395)
  AUTHORS   Carapeti,M., Aguiar,R.C., Goldman,J.M. and Cross,N.C.
  TITLE     A novel fusion between MOZ and the nuclear receptor coactivator
            TIF2 in acute myeloid leukemia
  JOURNAL   Blood 91 (9), 3127-3133 (1998)
   PUBMED   9558366
REFERENCE   8  (residues 1 to 1395)
  AUTHORS   Voegel,J.J., Heine,M.J., Tini,M., Vivat,V., Chambon,P. and
            Gronemeyer,H.
  TITLE     The coactivator TIF2 contains three nuclear receptor-binding motifs
            and mediates transactivation through CBP binding-dependent and
            -independent pathways
  JOURNAL   EMBO J 17 (2), 507-519 (1998)
   PUBMED   9430642
REFERENCE   9  (residues 1 to 1395)
  AUTHORS   Hong,H., Kohli,K., Garabedian,M.J. and Stallcup,M.R.
  TITLE     GRIP1, a transcriptional coactivator for the AF-2 transactivation
            domain of steroid, thyroid, retinoid, and vitamin D receptors
  JOURNAL   Mol Cell Biol 17 (5), 2735-2744 (1997)
   PUBMED   9111344
REFERENCE   10 (residues 1 to 1395)
  AUTHORS   Voegel,J.J., Heine,M.J., Zechel,C., Chambon,P. and Gronemeyer,H.
  TITLE     TIF2, a 160 kDa transcriptional mediator for the ligand-dependent
            activation function AF-2 of nuclear receptors
  JOURNAL   EMBO J 15 (14), 3667-3675 (1996)
   PUBMED   8670870
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022730.7, CK002637.1,
            X97674.1, AK298528.1, AW504723.1, DA691975.1, CN291204.1,
            CB270668.1, CK903771.1 and BC047111.1.
            
            Summary: The protein encoded by this gene functions as a
            transcriptional coactivator for nuclear hormone receptors,
            including steroid, thyroid, retinoid, and vitamin D receptors. The
            encoded protein acts as an intermediary factor for the
            ligand-dependent activity of these nuclear receptors, which
            regulate their target genes upon binding of cognate response
            elements. This gene has been found to be involved in translocations
            that result in fusions with other genes in various cancers,
            including the lysine acetyltransferase 6A (KAT6A) gene in acute
            myeloid leukemia, the ETS variant 6 (ETV6) gene in acute
            lymphoblastic leukemia, and the hes related family bHLH
            transcription factor with YRPW motif 1 (HEY1) gene in mesenchymal
            chondrosarcoma. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (5) differs in the 5' UTR and
            lacks an alternate in-frame exon in the central coding region,
            compared to variant 1, resulting in an isoform (b) that is shorter
            than isoform 1. Both variants 4 and 5 encode isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.731868.1,
                                           SRR1803614.101185.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.3"
     Protein         1..1395
                     /product="nuclear receptor coactivator 2 isoform b"
                     /note="glucocorticoid receptor-interacting protein-1;
                     transcriptional intermediary factor 2; class E basic
                     helix-loop-helix protein 75; p160 steroid receptor
                     coactivator 2"
                     /calculated_mol_wt=151914
     Region          28..91
                     /region_name="bHLH-PAS_NCoA2_SRC2"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in nuclear receptor coactivator 2 (NCoA-2)
                     and similar proteins; cd18950"
                     /db_xref="CDD:381520"
     Site            order(30..32,36,38..39,43,68..69)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381520"
     Site            order(41..42,45..46,48..49,70,73,77,79..80,84,86)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381520"
     Region          118..175
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Site            order(139,143,149,162..165,195)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(159,163,172,175..176,202,204)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          268..378
                     /region_name="PAS_11"
                     /note="PAS domain; pfam14598"
                     /db_xref="CDD:464214"
     Region          463..587
                     /region_name="NCOA_u2"
                     /note="Unstructured region on nuclear receptor coactivator
                     protein; pfam16665"
                     /db_xref="CDD:465223"
     Region          636..709
                     /region_name="SRC-1"
                     /note="Steroid receptor coactivator; pfam08832"
                     /db_xref="CDD:462615"
     Region          731..816
                     /region_name="DUF4927"
                     /note="Domain of unknown function (DUF4927); pfam16279"
                     /db_xref="CDD:465083"
     Region          1002..1046
                     /region_name="Nuc_rec_co-act"
                     /note="Nuclear receptor coactivator; pfam08815"
                     /db_xref="CDD:462608"
     Region          1212..1269
                     /region_name="DUF1518"
                     /note="Nuclear receptor coactivator, DUF1518; pfam07469"
                     /db_xref="CDD:462174"
     CDS             1..1395
                     /gene="NCOA2"
                     /gene_synonym="bHLHe75; GRIP1; KAT13C; NCoA-2; SRC-2;
                     SRC2; TIF2"
                     /coded_by="NM_001321712.2:270..4457"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="GeneID:10499"
                     /db_xref="HGNC:HGNC:7669"
                     /db_xref="MIM:601993"
ORIGIN      
        1 msgmgentsd psraetrkrk ecpdqlgpsp krntekrnre qenkyieela elifanfndi
       61 dnfnfkpdkc ailketvkqi rqikeqekaa aanidevqks dvsstgqgvi dkdalgpmml
      121 ealdgfffvv nlegnvvfvs envtqylryn qeelmnksvy silhvgdhte fvknllpksi
      181 vnggswsgep prrnshtfnc rmlvkplpds eeeghdnqea hqkyetmqcf avsqpksike
      241 egedlqscli cvarrvpmke rpvlpssesf ttrqdlqgki tsldtstmra amkpgwedlv
      301 rrciqkfhaq hegesvsyak rhhhevlrqg lafsqiyrfs lsdgtlvaaq tksklirsqt
      361 tnepqlvisl hmlhreqnvc vmnpdltgqt mgkplnpiss nspahqalcs gnpgqdmtls
      421 sninfpingp keqmgmpmgr fggsggmnhv sgmqattpqg snyalkmnsp sqsspgmnpg
      481 qptsmlsprh rmspgvagsp rippsqfspa gslhspvgvc sstgnshsyt nsslnalqal
      541 seghgvslgs slaspdlkmg nlqnspvnmn ppplskmgsl dskdcfglyg epsegttgqa
      601 esschpgeqk etndpnlppa vsseradgqs rlhdskgqtk llqllttksd qmepsplass
      661 lsdtnkdstg slpgsgsthg tslkekhkil hrllqdsssp vdlakltaea tgkdlsqess
      721 stapgsevti kqepvspkkk enallrylld kddtkdiglp eitpklerld sktdpasntk
      781 liamktekee msfepgdqpg seldnleeil ddlqnsqlpq lfpdtrpgap agsvdkqaii
      841 ndlmqltaen spvtpvgaqk talrisqsrm ignsasrptm psgewapqss avrvtcaatt
      901 samnrpvqgg mirnpaasip mrpssqpgqr qtlqsqvmni gpselemnmg gpqysqqqap
      961 pnqtapwpes ilpidqasfa sqnrqpfgss pddllcphpa aespsdegal ldqlylalrn
     1021 fdgleeidra lgipelvsqs qavdpeqfss qdsnimleqk apvfpqqyas qaqmaqgsys
     1081 pmqdpnfhtm gqrpsyatlr mqprpglrpt glvqnqpnql rlqlqhrlqa qqnrqplmnq
     1141 isnvsnvnlt lrpgvptqap inaqmlaqrq reilnqhlrq rqmhqqqqvq qrtlmmrgqg
     1201 lnmtpsmvap sgmpatmsnp ripqanaqqf pfppnygisq qpdpgftgat tpqsplmspr
     1261 mahtqspmmq qsqanpayqa psdingwaqg nmggnsmfsq qspphfgqqa ntsmysnnmn
     1321 invsmatntg gmssmnqmtg qismtsvtsv ptsglssmgp eqvndpalrg gnlfpnqlpg
     1381 mdmikqegdt trkyc
//
LOCUS       NP_001161354            1250 aa            linear   PRI 27-NOV-2025
DEFINITION  ankyrin repeat domain-containing protein 50 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001161354
VERSION     NP_001161354.1
DBSOURCE    REFSEQ: accession NM_001167882.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1250)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 1250)
  AUTHORS   Kvainickas,A., Orgaz,A.J., Nagele,H., Diedrich,B., Heesom,K.J.,
            Dengjel,J., Cullen,P.J. and Steinberg,F.
  TITLE     Retromer- and WASH-dependent sorting of nutrient transporters
            requires a multivalent interaction network with ANKRD50
  JOURNAL   J Cell Sci 130 (2), 382-395 (2017)
   PUBMED   27909246
  REMARK    GeneRIF: ANKRD50 simultaneously engages multiple parts of the
            SNX27-retromer-WASH complex machinery in a direct and co-operative
            interaction network that is needed to efficiently recycle the
            nutrient transporters.
REFERENCE   3  (residues 1 to 1250)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 1250)
  AUTHORS   McGough,I.J., Steinberg,F., Gallon,M., Yatsu,A., Ohbayashi,N.,
            Heesom,K.J., Fukuda,M. and Cullen,P.J.
  TITLE     Identification of molecular heterogeneity in
            SNX27-retromer-mediated endosome-to-plasma-membrane recycling
  JOURNAL   J Cell Sci 127 (Pt 22), 4940-4953 (2014)
   PUBMED   25278552
REFERENCE   5  (residues 1 to 1250)
  AUTHORS   Khadka,S., Vangeloff,A.D., Zhang,C., Siddavatam,P., Heaton,N.S.,
            Wang,L., Sengupta,R., Sahasrabudhe,S., Randall,G., Gribskov,M.,
            Kuhn,R.J., Perera,R. and LaCount,D.J.
  TITLE     A physical interaction network of dengue virus and human proteins
  JOURNAL   Mol Cell Proteomics 10 (12), M111.012187 (2011)
   PUBMED   21911577
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK295135.1, BC024725.1, AB033049.2 and AC105421.2.
            
            Transcript Variant: This variant (2) lacks an internal exon in the
            5' region, as compared to variant 1. The resulting isoform (2) has
            a shorter N-terminus, as compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295135.1, SRR14038191.2494998.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1250
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.1"
     Protein         1..1250
                     /product="ankyrin repeat domain-containing protein 50
                     isoform 2"
                     /note="ankyrin repeat domain-containing protein 50;
                     ankyrin repeat domain containing 50"
                     /calculated_mol_wt=136369
     Region          <316..>430
                     /region_name="PHA03100"
                     /note="ankyrin repeat protein; Provisional; cl39094"
                     /db_xref="CDD:476869"
     Region          365..396
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          379..672
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          398..429
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          431..462
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          464..495
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(497,499,503..504,507..509,511..512,516,519,528,530,
                     532,536..537,545..547,549..550,554,557,566,568,570,
                     574..575,578..580,582..583,587,590,599)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          497..528
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          530..566
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          568..599
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          601..632
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          634..665
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          654..923
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          668..698
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(669,673..674,677..679,681..682,686,689,698,700,702,
                     706..707,710..712,714..715,719,722,731,733,735,739..740,
                     743..745,747..748,752,755,764)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          700..731
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          733..764
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          766..797
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(799,801,805..806,809..811,813..814,818,821,830,832,
                     834,838..839,842..844,846..847,851,854,863,865,867,
                     871..872,875..877,879..880,884,887,896)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          799..830
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          832..863
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          865..896
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          898..923
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <1031..1224
                     /region_name="Semenogelin"
                     /note="pfam05474"
                     /db_xref="CDD:368458"
     CDS             1..1250
                     /gene="ANKRD50"
                     /coded_by="NM_001167882.2:301..4053"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54802.1"
                     /db_xref="GeneID:57182"
                     /db_xref="HGNC:HGNC:29223"
                     /db_xref="MIM:619856"
ORIGIN      
        1 mkppqqslyl lvdsvdegcn itegeqtsts lsgtvaalla ghheffppwl lllcsarkqs
       61 kavtkmftgf rkislddlrk ayivkdvqqy ilhrldqeea lrqhltketa emlnqlhiks
      121 sgcflylerv ldgvvenfim lreirdipgt lnglylwlcq rlfvrkqfak vqpilnvila
      181 acrpltitel yhavwtknms ltledfqrkl dilskllvdg lgntkilfhy sfaewlldvk
      241 hctqkylcna aeghrmlams ytcqaknltp leaqefalhl insnlqleta elalwmiwng
      301 tpvrdslstl ipkeqevlql lvkagahvns eddrtscivr qaleredsir tlldngasvn
      361 qcdsngrtll anaaysgsld vvnllvsrga dleiedahgh tpltlaarqg htkvvnclig
      421 cganinhtdq dgwtalrsaa wgghtevvsa llyagvkvdc adadsrtalr aaawgghedi
      481 vlnllqhgae vnkadnegrt aliaaaymgh reivehlldh gaevnhedvd grtalsvaal
      541 cvpaskghas vvsllidrga evdhcdkdgm tpllvaayeg hvdvvdllle ggadvdhtdn
      601 ngrtpllaaa smghasvvnt llfwgaavds idsegrtvls iasaqgnvev vrtlldrgld
      661 enhrddagwt plhmaafegh rlicealieq gartneidnd gripfilasq eghydcvqil
      721 lenksnidqr gydgrnalrv aaleghrdiv ellfshgadv nckdadgrpt lyilalenql
      781 tmaeyfleng anveasdaeg rtalhvscwq ghmemvqvli ayhadvnaad nekrsalqsa
      841 awqghvkvvq lliehgavvd htcnqgatal ciaaqeghid vvqvllehga dpnhadqfgr
      901 tamrvaakng hsqiikllek ygasslngcs pspvhtmeqk plqslsskvq sltiksnssg
      961 stgggdmqps lrglpngpth afsspsespd stvdrqkssl snnslksskn sslrttssta
     1021 taqtvpidsf hnlsfteqiq qhslprsrsr qsivspsstt qslgqshnsp ssefewsqvk
     1081 pslkstkask ggksensaks gsagkkakqs nssqpkvley emtqfdrrgp iaksgtaapp
     1141 kqmpaesqck imipsaqqei grsqqqflih qqsgeqkkrn gimtnpnyhl qsnqvflgrv
     1201 svprtmqdrg hqevlegyps setelslkqa lklqiegsdp sfnykketpl
//
LOCUS       NP_001243111            2663 aa            linear   PRI 27-NOV-2025
DEFINITION  ankyrin repeat domain-containing protein 11 [Homo sapiens].
ACCESSION   NP_001243111
VERSION     NP_001243111.1
DBSOURCE    REFSEQ: accession NM_001256182.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2663)
  AUTHORS   He,D., Zhang,M., Li,Y., Liu,F. and Ban,B.
  TITLE     Insights into the ANKRD11 variants and short-stature phenotype
            through literature review and ClinVar database search
  JOURNAL   Orphanet J Rare Dis 19 (1), 292 (2024)
   PUBMED   39135054
  REMARK    GeneRIF: Insights into the ANKRD11 variants and short-stature
            phenotype through literature review and ClinVar database search.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2663)
  AUTHORS   Chen,M., Yang,X., Liu,H. and Wan,J.
  TITLE     Identification and functional characterization of a bipartite
            nuclear localization signal in ANKRD11
  JOURNAL   Biochem Biophys Res Commun 670, 117-123 (2023)
   PUBMED   37290286
  REMARK    GeneRIF: Identification and functional characterization of a
            bipartite nuclear localization signal in ANKRD11.
REFERENCE   3  (residues 1 to 2663)
  AUTHORS   Yuan,M., Barefoot,M.E., Peterson,K., Campbell,M.J., Blancato,J.K.,
            Chen,M., Schmidt,M.O., Kiliti,A.J., Fang,H.B., Wellstein,A.,
            Riegel,A.T. and Sharif,G.M.
  TITLE     Loss of ANCO1 Expression Regulates Chromatin Accessibility and
            Drives Progression of Early-Stage Triple-Negative Breast Cancer
  JOURNAL   Int J Mol Sci 24 (14), 11505 (2023)
   PUBMED   37511268
  REMARK    GeneRIF: Loss of ANCO1 Expression Regulates Chromatin Accessibility
            and Drives Progression of Early-Stage Triple-Negative Breast
            Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2663)
  AUTHORS   Borja,N., Zafeer,M.F., Rodriguez,J.A., Morel Swols,D., Thorson,W.,
            Bademci,G. and Tekin,M.
  TITLE     Deletion of first noncoding exon in ANKRD11 leads to KBG syndrome
  JOURNAL   Am J Med Genet A 191 (4), 1044-1049 (2023)
   PUBMED   36628575
  REMARK    GeneRIF: Deletion of first noncoding exon in ANKRD11 leads to KBG
            syndrome.
            Review article
REFERENCE   5  (residues 1 to 2663)
  AUTHORS   Wang,L., Li,J., Xu,J., Xu,Y., Wang,J., Feng,Y. and Kong,X.
  TITLE     [Clinical and genetic analysis of three children with KBG syndrome
            due to novel variants of ANKRD11 gene]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 40 (1), 1-6 (2023)
   PUBMED   36584991
  REMARK    GeneRIF: [Clinical and genetic analysis of three children with KBG
            syndrome due to novel variants of ANKRD11 gene].
REFERENCE   6  (residues 1 to 2663)
  AUTHORS   Willemsen,M.H., Fernandez,B.A., Bacino,C.A., Gerkes,E., de
            Brouwer,A.P., Pfundt,R., Sikkema-Raddatz,B., Scherer,S.W.,
            Marshall,C.R., Potocki,L., van Bokhoven,H. and Kleefstra,T.
  TITLE     Identification of ANKRD11 and ZNF778 as candidate genes for autism
            and variable cognitive impairment in the novel 16q24.3
            microdeletion syndrome
  JOURNAL   Eur J Hum Genet 18 (4), 429-435 (2010)
   PUBMED   19920853
  REMARK    GeneRIF: ANKRD11 is a candidate gene for autism and variable
            cognitive impairment in the novel 16q24.3 microdeletion syndrome.
REFERENCE   7  (residues 1 to 2663)
  AUTHORS   Neilsen,P.M., Cheney,K.M., Li,C.W., Chen,J.D., Cawrse,J.E.,
            Schulz,R.B., Powell,J.A., Kumar,R. and Callen,D.F.
  TITLE     Identification of ANKRD11 as a p53 coactivator
  JOURNAL   J Cell Sci 121 (Pt 21), 3541-3552 (2008)
   PUBMED   18840648
  REMARK    GeneRIF: ANKRD11 has a role as a p53 coactivator and may be
            involved in a regulatory feedback loop with p53
REFERENCE   8  (residues 1 to 2663)
  AUTHORS   Zhang,A., Li,C.W. and Chen,J.D.
  TITLE     Characterization of transcriptional regulatory domains of ankyrin
            repeat cofactor-1
  JOURNAL   Biochem Biophys Res Commun 358 (4), 1034-1040 (2007)
   PUBMED   17521611
  REMARK    GeneRIF: Together, these results indicate that the transcriptional
            potential of ANCO-1 may be modulated by a combination of repression
            and activation signals.
REFERENCE   9  (residues 1 to 2663)
  AUTHORS   Zhang,A., Yeung,P.L., Li,C.W., Tsai,S.C., Dinh,G.K., Wu,X., Li,H.
            and Chen,J.D.
  TITLE     Identification of a novel family of ankyrin repeats containing
            cofactors for p160 nuclear receptor coactivators
  JOURNAL   J Biol Chem 279 (32), 33799-33805 (2004)
   PUBMED   15184363
REFERENCE   10 (residues 1 to 2663)
  AUTHORS   Morel Swols,D. and Tekin,M.
  TITLE     KBG Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29565525
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY373756.1, AY533563.1 and
            DA172996.1.
            
            Summary: This locus encodes an ankryin repeat domain-containing
            protein. The encoded protein inhibits ligand-dependent activation
            of transcription. Mutations in this gene have been associated with
            KBG syndrome, which is characterized by macrodontia, distinctive
            craniofacial features, short stature, skeletal anomalies, global
            developmental delay, seizures and intellectual disability.
            Alternatively spliced transcript variants have been described.
            Related pseudogenes exist on chromosomes 2 and X. [provided by
            RefSeq, Jan 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY533563.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2663
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..2663
                     /product="ankyrin repeat domain-containing protein 11"
                     /note="nasopharyngeal carcinoma susceptibility protein;
                     ankyrin repeat-containing cofactor 1; ankyrin repeats
                     containing cofactor 1; ankyrin repeat domain containing
                     11"
                     /calculated_mol_wt=297784
     Region          1..90
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          128..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          <158..>287
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(167,169,173..174,177..179,181..182,186,189,198,200,
                     202,206..207,210..212,214..215,219,222,231,233,235,
                     239..240,243..245,247..248,252,255)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          167..198
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          167..196
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          200..231
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          200..229
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          233..262
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          233..261
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          266..292
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          289..380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          398..647
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          <583..789
                     /region_name="PTZ00108"
                     /note="DNA topoisomerase 2-like protein; Provisional"
                     /db_xref="CDD:240271"
     Region          <694..1308
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          723..783
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          881..1043
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          1059..1393
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1079
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4F7; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1120
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1419
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          1424..1710
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          <1691..2354
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4F7; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1792
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          1814..1836
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1847
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1850
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4F7; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1851
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4F7; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1852
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4F7; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1859
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          1988..2019
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1990
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          2131..2406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          2369..2663
                     /region_name="Important for protein degradation.
                     /evidence=ECO:0000269|PubMed:25413698"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     CDS             1..2663
                     /gene="ANKRD11"
                     /gene_synonym="ANCO-1; ANCO1; LZ16; T13"
                     /coded_by="NM_001256182.2:533..8524"
                     /db_xref="CCDS:CCDS32513.1"
                     /db_xref="GeneID:29123"
                     /db_xref="HGNC:HGNC:21316"
                     /db_xref="MIM:611192"
ORIGIN      
        1 mpkggcpkap qqeelplssd mvekqtgkkd kdkvsltktp klergdggke vreraskrkl
       61 pftagangeq kdsdtekqgp erkrikkepv trkagllfgm glsgiragyp lserqqvall
      121 mqmtaeesan spvdttpkhp sqstvcqkgt pnsasktkdk vnkrnerget rlhraairgd
      181 arrikelise gadvnvkdfa gwtalheacn rgyydvakql laagaevntk gldddtplhd
      241 aannghykvv klllryggnp qqsnrkgetp lkvansptmv nlllgkgtyt sseesstess
      301 eeedapsfap sssvdgnntd sefekglkhk aknpepqkat apvkdeyefd eddeqdrvpp
      361 vddkhllkkd yrketksnsf isipkmevks ytknntiapk kashrilsdt sdeedasvtv
      421 gtgeklrlsa htilpgsktr epsnakqqke knkvkkkrkk etkgrevrfg krsdkfcsse
      481 sesessesge ddrdslgssg clkgsplvlk dpslfsslsa sstsshgssa aqkqnpshtd
      541 qhtkhwrtdn wktisspaws evsslsdstr trltsesdys segssveslk pvrkrqehrk
      601 raslsekksp flssaegavp kldkegkvvk khktkhkhkn kekgqcsisq elklksftye
      661 yedskqksdk aillendlst enklkvlkhd rdhfkkeekl skmkleekew lfkdekslkr
      721 ikdtnkdisr sfreekdrsn kaekerslke kspkeeklrl ykeerkkksk drpsklekkn
      781 dlkedkiske kekifkedke klkkekvyre dsafdeycnk nqflenedtk fslsddqrdr
      841 wfsdlsdssf dfkgedswds pvtdyrdmks dsvaklilet vkedskerrr dsrarekrdy
      901 repffrkkdr dyldknsekr keqtekhksv pgylsekdkk rresaeagrd rkdalescke
      961 rrdgrakpee ahreelkecg cesgfkdksd gdfgkglepw erhhpareke kkdgpdkerk
     1021 ektkperyke kssdkdksek silekcqkdk efdkcfkekk dtkekhkdth gkdkerkasl
     1081 dqgkekkeka fpgiisedfs ekkddkkgke kswyiadift deseddrdsc mgsgfkmgea
     1141 sdlprtdglq ekeegreaya sdrhrkssdk qhperqkdke prdrrkdrga adagrdkkek
     1201 vfekhkekkd kestekykdr kdrasvdstq dkknkqklpe kaekkhaaed kakskhkeks
     1261 dkehskerks srsadaeksl lekleeealh eyredsndki sevssdsftd rgqepgltaf
     1321 levsfteppg ddkpresacl peklkekerh rhssssskks hdrerakkek aekkekgedy
     1381 keggsrkdsg qyekdflead aygvsynmka diedeldkti elfstekkdk ndserepskk
     1441 iekelkpygs sainilkekk krekhrekwr dekerhrdrh adgllrhhrd ellrhhrdeq
     1501 kpatrdkdsp prvlkdksrd egprlgdakl kekfkdgaek ekgdpvkmsn gndkvapskd
     1561 pgkkdarpre kllgdgdlmm tsfermlsqk dleieerhkr hkermkqmek lrhrsgdpkl
     1621 kekakpaddg rkkgldipak kppgldppfk dkklkestpi ppaaenklhp asgadskdwl
     1681 agphmkevlp asprpdqsrp tgvptptsvl scpsyeevmh tprtpscsad dyadlvfdca
     1741 dsqhstpvpt aptsacspsf fdrfsvassg lsenasqapa rplstnlyrs vsvdirrtpe
     1801 eefsvgdklf rqqsvpaass ydspmppsme draplppvpa ekfaclspgy yspdyglpsp
     1861 kvdalhcppa avvtvtpspe gvfsslqakp spspraellv pslegalppd ldtsedqqat
     1921 aaiippepsy lepldegpfs aviteepvew ahpseqalas sliggtsenp vswpvgsdll
     1981 lkspqrfpes pkrfcpadpl hsaapgpfsa seapypappa spapyalpva epgledvkdg
     2041 vdavpaaist seaapyapps glesffsnck slpeapldva pepacvaava qvealgplen
     2101 sfldgsrgls hlgqvepvpw adafagpedd ldlgpfslpe lplqtkdaad geaepveesl
     2161 appeemppga pgvinggdvs tvvaeeppal ppdqastrlp aelepepsge pkldvaleaa
     2221 veaetvpeer argdpdssve papvppeqrp lgsgdqgaea egppaaslca pdgpapntva
     2281 qaqaadgagp eddteasraa apaegppggi qpeaaepkpt aeapkaprve eipqrmtrnr
     2341 aqmlanqskq gpppsekeca ptpapvtrak argsedddaq aqhprkrrfq rstqqlqqql
     2401 ntstqqtrev iqqtlaaivd aikldaiepy hsdranpyfe ylqirkkiee krkilccitp
     2461 qapqcyaeyv tytgsylldg kplsklhipv iapppslaep lkelfrqqea vrgklrlqhs
     2521 iereklivsc eqeilrvhcr aartianqav pfsactmlld sevynmples qgdenksvrd
     2581 rfnarqfisw lqdvddkydr mktcllmrqq heaaalnavq rmewqlkvqe ldpaghkslc
     2641 vnevpsfyvp mvdvnddfvl lpa
//
LOCUS       NP_056474                490 aa            linear   PRI 27-NOV-2025
DEFINITION  ribosomal L1 domain-containing protein 1 [Homo sapiens].
ACCESSION   NP_056474 XP_085525
VERSION     NP_056474.2
DBSOURCE    REFSEQ: accession NM_015659.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 490)
  AUTHORS   Jin,Y., Zhao,L., Wang,S., Zhang,X., Quan,J., Lin,Z. and Piao,J.
  TITLE     RSL1D1 knockdown induces ferroptosis and mediates ferrous iron
            accumulation in senescent cells by inhibiting FTH1 mRNA stability
  JOURNAL   Carcinogenesis 44 (2), 129-142 (2023)
   PUBMED   36913375
  REMARK    GeneRIF: RSL1D1 knockdown induces ferroptosis and mediates ferrous
            iron accumulation in senescent cells by inhibiting FTH1 mRNA
            stability.
REFERENCE   2  (residues 1 to 490)
  AUTHORS   Wang,W., Miyamoto,Y., Chen,B., Shi,J., Diao,F., Zheng,W., Li,Q.,
            Yu,L., Li,L., Xu,Y., Wu,L., Mao,X., Fu,J., Li,B., Yan,Z., Shi,R.,
            Xue,X., Mu,J., Zhang,Z., Wu,T., Zhao,L., Wang,W., Zhou,Z., Dong,J.,
            Li,Q., Jin,L., He,L., Sun,X., Lin,G., Kuang,Y., Wang,L. and Sang,Q.
  TITLE     Karyopherin alpha deficiency contributes to human preimplantation
            embryo arrest
  JOURNAL   J Clin Invest 133 (2), e159951 (2023)
   PUBMED   36647821
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 490)
  AUTHORS   Ding,L., Zhao,C., Xu,Y., Zhang,Z., Nie,Y., Liao,K., Chen,Y., Tu,B.
            and Zhang,X.
  TITLE     Mutations in DNA binding domain of p53 impede RSL1D1-p53
            interaction to escape from degradation in human colorectal cancer
            cells
  JOURNAL   Exp Cell Res 417 (1), 113211 (2022)
   PUBMED   35597299
  REMARK    GeneRIF: Mutations in DNA binding domain of p53 impede RSL1D1-p53
            interaction to escape from degradation in human colorectal cancer
            cells.
REFERENCE   4  (residues 1 to 490)
  AUTHORS   Liu,X., Chen,J., Long,X., Lan,J., Liu,X., Zhou,M., Zhang,S. and
            Zhou,J.
  TITLE     RSL1D1 promotes the progression of colorectal cancer through
            RAN-mediated autophagy suppression
  JOURNAL   Cell Death Dis 13 (1), 43 (2022)
   PUBMED   35013134
  REMARK    GeneRIF: RSL1D1 promotes the progression of colorectal cancer
            through RAN-mediated autophagy suppression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 490)
  AUTHORS   Ding,L., Zhang,Z., Zhao,C., Chen,L., Chen,Z., Zhang,J., Liu,Y.,
            Nie,Y., He,Y., Liao,K. and Zhang,X.
  TITLE     Ribosomal L1 domain-containing protein 1 coordinates with HDM2 to
            negatively regulate p53 in human colorectal Cancer cells
  JOURNAL   J Exp Clin Cancer Res 40 (1), 245 (2021)
   PUBMED   34362424
  REMARK    GeneRIF: Ribosomal L1 domain-containing protein 1 coordinates with
            HDM2 to negatively regulate p53 in human colorectal Cancer cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 490)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
REFERENCE   7  (residues 1 to 490)
  AUTHORS   Cai,Y., Jin,J., Tomomori-Sato,C., Sato,S., Sorokina,I.,
            Parmely,T.J., Conaway,R.C. and Conaway,J.W.
  TITLE     Identification of new subunits of the multiprotein mammalian
            TRRAP/TIP60-containing histone acetyltransferase complex
  JOURNAL   J Biol Chem 278 (44), 42733-42736 (2003)
   PUBMED   12963728
REFERENCE   8  (residues 1 to 490)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   9  (residues 1 to 490)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   10 (residues 1 to 490)
  AUTHORS   Huch,G., Hohn,H.P. and Denker,H.W.
  TITLE     Identification of differentially expressed genes in human
            trophoblast cells by differential-display RT-PCR
  JOURNAL   Placenta 19 (8), 557-567 (1998)
   PUBMED   9859858
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI856275.1, BC113699.1 and AC010654.8.
            
            On Nov 30, 2006 this sequence version replaced NP_056474.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.272823.1,
                                           SRR1803612.17981.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467148 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000571133.6/ ENSP00000460871.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..490
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.13"
     Protein         1..490
                     /product="ribosomal L1 domain-containing protein 1"
                     /note="CATX-11; cellular senescence-inhibited gene
                     protein"
                     /calculated_mol_wt=54842
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O76021.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O76021.3)"
     Region          43..258
                     /region_name="Ribosomal_L1"
                     /note="Ribosomal protein L1p/L10e family; pfam00687"
                     /db_xref="CDD:459905"
     Region          280..490
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O76021.3)"
     Region          <324..>462
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O76021.3)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O76021.3)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O76021.3)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O76021.3)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (O76021.3)"
     Site            396
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (O76021.3)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O76021.3)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O76021.3)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O76021.3)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O76021.3)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O76021.3)"
     Site            468
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O76021.3)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O76021.3)"
     CDS             1..490
                     /gene="RSL1D1"
                     /gene_synonym="Cic1; CSIG; L12; PBK1; UTP30"
                     /coded_by="NM_015659.3:31..1503"
                     /db_xref="CCDS:CCDS10551.1"
                     /db_xref="GeneID:26156"
                     /db_xref="HGNC:HGNC:24534"
                     /db_xref="MIM:615874"
ORIGIN      
        1 medsasasls saaatgtsts tpaaptarkq ldkeqvrkav dallthcksr knnyglllne
       61 neslflmvvl wkipskelrv rltlphsirs dsediclftk depnstpekt eqfyrkllnk
      121 hgiktvsqii slqtlkkeyk syeaklrlls sfdffltdar irrllpslig rhfyqrkkvp
      181 vsvnllsknl sreindcigg tvlnisksgs csairighvg mqiehiieni vavtkglsek
      241 lpekwesvkl lfvkteksaa lpifssfvsn wdeatkrsll nkkkkearrk rrernfekqk
      301 erkkkrqqar ktasvlskdd vapesgdttv kkpeskkeqt pehgkkkrgr gkaqvkatne
      361 sedeipqlvp igkktpanek veiqkhatgk kspakspnps tprgkkrkal pasetpkaae
      421 setpgkspek kpkikeeavk ekspslgkkd arqtpkkpea kffttpsksv rkashtpkkw
      481 pkkpkvpqst
//
LOCUS       NP_001243112            2663 aa            linear   PRI 27-NOV-2025
DEFINITION  ankyrin repeat domain-containing protein 11 [Homo sapiens].
ACCESSION   NP_001243112
VERSION     NP_001243112.1
DBSOURCE    REFSEQ: accession NM_001256183.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2663)
  AUTHORS   He,D., Zhang,M., Li,Y., Liu,F. and Ban,B.
  TITLE     Insights into the ANKRD11 variants and short-stature phenotype
            through literature review and ClinVar database search
  JOURNAL   Orphanet J Rare Dis 19 (1), 292 (2024)
   PUBMED   39135054
  REMARK    GeneRIF: Insights into the ANKRD11 variants and short-stature
            phenotype through literature review and ClinVar database search.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2663)
  AUTHORS   Chen,M., Yang,X., Liu,H. and Wan,J.
  TITLE     Identification and functional characterization of a bipartite
            nuclear localization signal in ANKRD11
  JOURNAL   Biochem Biophys Res Commun 670, 117-123 (2023)
   PUBMED   37290286
  REMARK    GeneRIF: Identification and functional characterization of a
            bipartite nuclear localization signal in ANKRD11.
REFERENCE   3  (residues 1 to 2663)
  AUTHORS   Yuan,M., Barefoot,M.E., Peterson,K., Campbell,M.J., Blancato,J.K.,
            Chen,M., Schmidt,M.O., Kiliti,A.J., Fang,H.B., Wellstein,A.,
            Riegel,A.T. and Sharif,G.M.
  TITLE     Loss of ANCO1 Expression Regulates Chromatin Accessibility and
            Drives Progression of Early-Stage Triple-Negative Breast Cancer
  JOURNAL   Int J Mol Sci 24 (14), 11505 (2023)
   PUBMED   37511268
  REMARK    GeneRIF: Loss of ANCO1 Expression Regulates Chromatin Accessibility
            and Drives Progression of Early-Stage Triple-Negative Breast
            Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2663)
  AUTHORS   Borja,N., Zafeer,M.F., Rodriguez,J.A., Morel Swols,D., Thorson,W.,
            Bademci,G. and Tekin,M.
  TITLE     Deletion of first noncoding exon in ANKRD11 leads to KBG syndrome
  JOURNAL   Am J Med Genet A 191 (4), 1044-1049 (2023)
   PUBMED   36628575
  REMARK    GeneRIF: Deletion of first noncoding exon in ANKRD11 leads to KBG
            syndrome.
            Review article
REFERENCE   5  (residues 1 to 2663)
  AUTHORS   Wang,L., Li,J., Xu,J., Xu,Y., Wang,J., Feng,Y. and Kong,X.
  TITLE     [Clinical and genetic analysis of three children with KBG syndrome
            due to novel variants of ANKRD11 gene]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 40 (1), 1-6 (2023)
   PUBMED   36584991
  REMARK    GeneRIF: [Clinical and genetic analysis of three children with KBG
            syndrome due to novel variants of ANKRD11 gene].
REFERENCE   6  (residues 1 to 2663)
  AUTHORS   Willemsen,M.H., Fernandez,B.A., Bacino,C.A., Gerkes,E., de
            Brouwer,A.P., Pfundt,R., Sikkema-Raddatz,B., Scherer,S.W.,
            Marshall,C.R., Potocki,L., van Bokhoven,H. and Kleefstra,T.
  TITLE     Identification of ANKRD11 and ZNF778 as candidate genes for autism
            and variable cognitive impairment in the novel 16q24.3
            microdeletion syndrome
  JOURNAL   Eur J Hum Genet 18 (4), 429-435 (2010)
   PUBMED   19920853
  REMARK    GeneRIF: ANKRD11 is a candidate gene for autism and variable
            cognitive impairment in the novel 16q24.3 microdeletion syndrome.
REFERENCE   7  (residues 1 to 2663)
  AUTHORS   Neilsen,P.M., Cheney,K.M., Li,C.W., Chen,J.D., Cawrse,J.E.,
            Schulz,R.B., Powell,J.A., Kumar,R. and Callen,D.F.
  TITLE     Identification of ANKRD11 as a p53 coactivator
  JOURNAL   J Cell Sci 121 (Pt 21), 3541-3552 (2008)
   PUBMED   18840648
  REMARK    GeneRIF: ANKRD11 has a role as a p53 coactivator and may be
            involved in a regulatory feedback loop with p53
REFERENCE   8  (residues 1 to 2663)
  AUTHORS   Zhang,A., Li,C.W. and Chen,J.D.
  TITLE     Characterization of transcriptional regulatory domains of ankyrin
            repeat cofactor-1
  JOURNAL   Biochem Biophys Res Commun 358 (4), 1034-1040 (2007)
   PUBMED   17521611
  REMARK    GeneRIF: Together, these results indicate that the transcriptional
            potential of ANCO-1 may be modulated by a combination of repression
            and activation signals.
REFERENCE   9  (residues 1 to 2663)
  AUTHORS   Zhang,A., Yeung,P.L., Li,C.W., Tsai,S.C., Dinh,G.K., Wu,X., Li,H.
            and Chen,J.D.
  TITLE     Identification of a novel family of ankyrin repeats containing
            cofactors for p160 nuclear receptor coactivators
  JOURNAL   J Biol Chem 279 (32), 33799-33805 (2004)
   PUBMED   15184363
REFERENCE   10 (residues 1 to 2663)
  AUTHORS   Morel Swols,D. and Tekin,M.
  TITLE     KBG Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29565525
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY373756.1, BC069013.1,
            AY533563.1 and DA172996.1.
            
            Summary: This locus encodes an ankryin repeat domain-containing
            protein. The encoded protein inhibits ligand-dependent activation
            of transcription. Mutations in this gene have been associated with
            KBG syndrome, which is characterized by macrodontia, distinctive
            craniofacial features, short stature, skeletal anomalies, global
            developmental delay, seizures and intellectual disability.
            Alternatively spliced transcript variants have been described.
            Related pseudogenes exist on chromosomes 2 and X. [provided by
            RefSeq, Jan 2012].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2663
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..2663
                     /product="ankyrin repeat domain-containing protein 11"
                     /note="nasopharyngeal carcinoma susceptibility protein;
                     ankyrin repeat-containing cofactor 1; ankyrin repeats
                     containing cofactor 1; ankyrin repeat domain containing
                     11"
                     /calculated_mol_wt=297784
     Region          1..90
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          128..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          <158..>287
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(167,169,173..174,177..179,181..182,186,189,198,200,
                     202,206..207,210..212,214..215,219,222,231,233,235,
                     239..240,243..245,247..248,252,255)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          167..198
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          167..196
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          200..231
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          200..229
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          233..262
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          233..261
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          266..292
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          289..380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          398..647
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          <583..789
                     /region_name="PTZ00108"
                     /note="DNA topoisomerase 2-like protein; Provisional"
                     /db_xref="CDD:240271"
     Region          <694..1308
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          723..783
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          881..1043
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          1059..1393
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1079
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4F7; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1120
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1419
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          1424..1710
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          <1691..2354
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4F7; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1792
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          1814..1836
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1847
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1850
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4F7; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1851
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4F7; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1852
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:E9Q4F7; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1859
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          1988..2019
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Site            1990
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          2131..2406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     Region          2369..2663
                     /region_name="Important for protein degradation.
                     /evidence=ECO:0000269|PubMed:25413698"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UB99.3)"
     CDS             1..2663
                     /gene="ANKRD11"
                     /gene_synonym="ANCO-1; ANCO1; LZ16; T13"
                     /coded_by="NM_001256183.2:459..8450"
                     /db_xref="CCDS:CCDS32513.1"
                     /db_xref="GeneID:29123"
                     /db_xref="HGNC:HGNC:21316"
                     /db_xref="MIM:611192"
ORIGIN      
        1 mpkggcpkap qqeelplssd mvekqtgkkd kdkvsltktp klergdggke vreraskrkl
       61 pftagangeq kdsdtekqgp erkrikkepv trkagllfgm glsgiragyp lserqqvall
      121 mqmtaeesan spvdttpkhp sqstvcqkgt pnsasktkdk vnkrnerget rlhraairgd
      181 arrikelise gadvnvkdfa gwtalheacn rgyydvakql laagaevntk gldddtplhd
      241 aannghykvv klllryggnp qqsnrkgetp lkvansptmv nlllgkgtyt sseesstess
      301 eeedapsfap sssvdgnntd sefekglkhk aknpepqkat apvkdeyefd eddeqdrvpp
      361 vddkhllkkd yrketksnsf isipkmevks ytknntiapk kashrilsdt sdeedasvtv
      421 gtgeklrlsa htilpgsktr epsnakqqke knkvkkkrkk etkgrevrfg krsdkfcsse
      481 sesessesge ddrdslgssg clkgsplvlk dpslfsslsa sstsshgssa aqkqnpshtd
      541 qhtkhwrtdn wktisspaws evsslsdstr trltsesdys segssveslk pvrkrqehrk
      601 raslsekksp flssaegavp kldkegkvvk khktkhkhkn kekgqcsisq elklksftye
      661 yedskqksdk aillendlst enklkvlkhd rdhfkkeekl skmkleekew lfkdekslkr
      721 ikdtnkdisr sfreekdrsn kaekerslke kspkeeklrl ykeerkkksk drpsklekkn
      781 dlkedkiske kekifkedke klkkekvyre dsafdeycnk nqflenedtk fslsddqrdr
      841 wfsdlsdssf dfkgedswds pvtdyrdmks dsvaklilet vkedskerrr dsrarekrdy
      901 repffrkkdr dyldknsekr keqtekhksv pgylsekdkk rresaeagrd rkdalescke
      961 rrdgrakpee ahreelkecg cesgfkdksd gdfgkglepw erhhpareke kkdgpdkerk
     1021 ektkperyke kssdkdksek silekcqkdk efdkcfkekk dtkekhkdth gkdkerkasl
     1081 dqgkekkeka fpgiisedfs ekkddkkgke kswyiadift deseddrdsc mgsgfkmgea
     1141 sdlprtdglq ekeegreaya sdrhrkssdk qhperqkdke prdrrkdrga adagrdkkek
     1201 vfekhkekkd kestekykdr kdrasvdstq dkknkqklpe kaekkhaaed kakskhkeks
     1261 dkehskerks srsadaeksl lekleeealh eyredsndki sevssdsftd rgqepgltaf
     1321 levsfteppg ddkpresacl peklkekerh rhssssskks hdrerakkek aekkekgedy
     1381 keggsrkdsg qyekdflead aygvsynmka diedeldkti elfstekkdk ndserepskk
     1441 iekelkpygs sainilkekk krekhrekwr dekerhrdrh adgllrhhrd ellrhhrdeq
     1501 kpatrdkdsp prvlkdksrd egprlgdakl kekfkdgaek ekgdpvkmsn gndkvapskd
     1561 pgkkdarpre kllgdgdlmm tsfermlsqk dleieerhkr hkermkqmek lrhrsgdpkl
     1621 kekakpaddg rkkgldipak kppgldppfk dkklkestpi ppaaenklhp asgadskdwl
     1681 agphmkevlp asprpdqsrp tgvptptsvl scpsyeevmh tprtpscsad dyadlvfdca
     1741 dsqhstpvpt aptsacspsf fdrfsvassg lsenasqapa rplstnlyrs vsvdirrtpe
     1801 eefsvgdklf rqqsvpaass ydspmppsme draplppvpa ekfaclspgy yspdyglpsp
     1861 kvdalhcppa avvtvtpspe gvfsslqakp spspraellv pslegalppd ldtsedqqat
     1921 aaiippepsy lepldegpfs aviteepvew ahpseqalas sliggtsenp vswpvgsdll
     1981 lkspqrfpes pkrfcpadpl hsaapgpfsa seapypappa spapyalpva epgledvkdg
     2041 vdavpaaist seaapyapps glesffsnck slpeapldva pepacvaava qvealgplen
     2101 sfldgsrgls hlgqvepvpw adafagpedd ldlgpfslpe lplqtkdaad geaepveesl
     2161 appeemppga pgvinggdvs tvvaeeppal ppdqastrlp aelepepsge pkldvaleaa
     2221 veaetvpeer argdpdssve papvppeqrp lgsgdqgaea egppaaslca pdgpapntva
     2281 qaqaadgagp eddteasraa apaegppggi qpeaaepkpt aeapkaprve eipqrmtrnr
     2341 aqmlanqskq gpppsekeca ptpapvtrak argsedddaq aqhprkrrfq rstqqlqqql
     2401 ntstqqtrev iqqtlaaivd aikldaiepy hsdranpyfe ylqirkkiee krkilccitp
     2461 qapqcyaeyv tytgsylldg kplsklhipv iapppslaep lkelfrqqea vrgklrlqhs
     2521 iereklivsc eqeilrvhcr aartianqav pfsactmlld sevynmples qgdenksvrd
     2581 rfnarqfisw lqdvddkydr mktcllmrqq heaaalnavq rmewqlkvqe ldpaghkslc
     2641 vnevpsfyvp mvdvnddfvl lpa
//
LOCUS       NP_115766                293 aa            linear   PRI 27-NOV-2025
DEFINITION  MKI67 FHA domain-interacting nucleolar phosphoprotein [Homo
            sapiens].
ACCESSION   NP_115766
VERSION     NP_115766.3
DBSOURCE    REFSEQ: accession NM_032390.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Tan,L., He,Y., Wu,L., Liu,S., Peng,P. and Huang,J.
  TITLE     NIFK as a potential prognostic biomarker in colorectal cancer
            correlating with immune infiltrates
  JOURNAL   Medicine (Baltimore) 102 (40), e35452 (2023)
   PUBMED   37800782
  REMARK    GeneRIF: NIFK as a potential prognostic biomarker in colorectal
            cancer correlating with immune infiltrates.
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Lin,T.C., Su,C.Y., Wu,P.Y., Lai,T.C., Pan,W.A., Jan,Y.H.,
            Chang,Y.C., Yeh,C.T., Chen,C.L., Ger,L.P., Chang,H.T., Yang,C.J.,
            Huang,M.S., Liu,Y.P., Lin,Y.F., Shyy,J.Y., Tsai,M.D. and Hsiao,M.
  TITLE     The nucleolar protein NIFK promotes cancer progression via
            CK1alpha/beta-catenin in metastasis and Ki-67-dependent cell
            proliferation
  JOURNAL   Elife 5, e11288 (2016)
   PUBMED   26984280
  REMARK    GeneRIF: NIFK is required for lung cancer progression via the
            RUNX1-dependent CK1alpha repression, which activates
            TCF4/beta-catenin signaling in metastasis and the Ki-67-dependent
            regulation in cell proliferation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Sobecki,M., Mrouj,K., Camasses,A., Parisis,N., Nicolas,E.,
            Lleres,D., Gerbe,F., Prieto,S., Krasinska,L., David,A., Eguren,M.,
            Birling,M.C., Urbach,S., Hem,S., Dejardin,J., Malumbres,M., Jay,P.,
            Dulic,V., Lafontaine,D.Lj., Feil,R. and Fisher,D.
  TITLE     The cell proliferation antigen Ki-67 organises heterochromatin
  JOURNAL   Elife 5, e13722 (2016)
   PUBMED   26949251
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Pan,W.A., Tsai,H.Y., Wang,S.C., Hsiao,M., Wu,P.Y. and Tsai,M.D.
  TITLE     The RNA recognition motif of NIFK is required for rRNA maturation
            during cell cycle progression
  JOURNAL   RNA Biol 12 (3), 255-267 (2015)
   PUBMED   25826659
  REMARK    GeneRIF: The RNA recognition motif of NIFK is required for rRNA
            maturation during cell cycle progression.
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 293)
  AUTHORS   Panteva,M.T., Salari,R., Bhattacharjee,M. and Chong,L.T.
  TITLE     Direct observations of shifts in the beta-sheet register of a
            protein-peptide complex using explicit solvent simulations
  JOURNAL   Biophys J 100 (9), L50-L52 (2011)
   PUBMED   21539773
  REMARK    GeneRIF: Potential encounter complexes of the Ki67FHA receptor and
            hNIFK peptide are misregistered states of the beta-sheet.
REFERENCE   7  (residues 1 to 293)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   8  (residues 1 to 293)
  AUTHORS   Byeon,I.J., Li,H., Song,H., Gronenborn,A.M. and Tsai,M.D.
  TITLE     Sequential phosphorylation and multisite interactions characterize
            specific target recognition by the FHA domain of Ki67
  JOURNAL   Nat Struct Mol Biol 12 (11), 987-993 (2005)
   PUBMED   16244663
REFERENCE   9  (residues 1 to 293)
  AUTHORS   Li,H., Byeon,I.J., Ju,Y. and Tsai,M.D.
  TITLE     Structure of human Ki67 FHA domain and its binding to a
            phosphoprotein fragment from hNIFK reveal unique recognition sites
            and new views to the structural basis of FHA domain functions
  JOURNAL   J Mol Biol 335 (1), 371-381 (2004)
   PUBMED   14659764
  REMARK    GeneRIF: nmr analysis of the solution structure of the FHA domain
            of human Ki67 and mapping of the binding surface for NIFK binding
REFERENCE   10 (residues 1 to 293)
  AUTHORS   Takagi,M., Sueishi,M., Saiwaki,T., Kametaka,A. and Yoneda,Y.
  TITLE     A novel nucleolar protein, NIFK, interacts with the forkhead
            associated domain of Ki-67 antigen in mitosis
  JOURNAL   J Biol Chem 276 (27), 25386-25391 (2001)
   PUBMED   11342549
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC022990.1, BC024238.2 and
            BE671589.1.
            
            On Jan 31, 2009 this sequence version replaced NP_115766.2.
            
            Summary: This gene encodes a protein that interacts with the
            forkhead-associated domain of the Ki-67 antigen. The encoded
            protein may bind RNA and may play a role in mitosis and cell cycle
            progression. Multiple pseudogenes exist on chromosomes 5, 10, 12,
            15, and 19.[provided by RefSeq, Jan 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.257496.1,
                                           SRR1660803.182395.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000285814.9/ ENSP00000285814.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..293
                     /product="MKI67 FHA domain-interacting nucleolar
                     phosphoprotein"
                     /note="nucleolar phosphoprotein Nopp34; nucleolar protein
                     interacting with the FHA domain of pKi-67; hNIFK"
                     /calculated_mol_wt=34091
     Region          2..>151
                     /region_name="half-pint"
                     /note="poly-U binding splicing factor, half-pint family;
                     TIGR01645"
                     /db_xref="CDD:130706"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895;
                     propagated from UniProtKB/Swiss-Prot (Q9BYG3.1)"
     Region          46..119
                     /region_name="RRM_NIFK_like"
                     /note="RNA recognition motif in nucleolar protein
                     interacting with the FHA domain of pKI-67 (NIFK) and
                     similar proteins; cd12307"
                     /db_xref="CDD:409748"
     Site            114
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, by PRMT1 and PRMT8.
                     /evidence=ECO:0000269|PubMed:26529540; propagated from
                     UniProtKB/Swiss-Prot (Q9BYG3.1)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BYG3.1)"
     Region          197..239
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYG3.1)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BYG3.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BYG3.1)"
     Region          226..269
                     /region_name="Interaction with MKI67"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYG3.1)"
     Region          227..266
                     /region_name="hNIFK_binding"
                     /note="FHA Ki67 binding domain of hNIFK; pfam12196"
                     /db_xref="CDD:463489"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16244663; propagated from
                     UniProtKB/Swiss-Prot (Q9BYG3.1)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14659764,
                     ECO:0000269|PubMed:16244663, ECO:0007744|PubMed:18669648;
                     propagated from UniProtKB/Swiss-Prot (Q9BYG3.1)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:16244663,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BYG3.1)"
     Site            244
                     /site_type="methylation"
                     /note="Omega-N-methylated arginine, by PRMT1 and PRMT8.
                     /evidence=ECO:0000269|PubMed:26529540; propagated from
                     UniProtKB/Swiss-Prot (Q9BYG3.1)"
     Site            245
                     /site_type="methylation"
                     /note="Omega-N-methylated arginine, by PRMT1 and PRMT8.
                     /evidence=ECO:0000269|PubMed:26529540; propagated from
                     UniProtKB/Swiss-Prot (Q9BYG3.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BYG3.1)"
     Region          271..293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYG3.1)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BYG3.1)"
     Site            284
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, by PRMT1 and PRMT8.
                     /evidence=ECO:0000269|PubMed:26529540; propagated from
                     UniProtKB/Swiss-Prot (Q9BYG3.1)"
     CDS             1..293
                     /gene="NIFK"
                     /gene_synonym="MKI67IP; Nop15; Nopp34"
                     /coded_by="NM_032390.5:26..907"
                     /db_xref="CCDS:CCDS2135.1"
                     /db_xref="GeneID:84365"
                     /db_xref="HGNC:HGNC:17838"
                     /db_xref="MIM:611970"
ORIGIN      
        1 matfsgpagp ilslnpqedv efqkevaqvr kritqrkkqe qltpgvvyvr hlpnlldetq
       61 ifsyfsqfgt vtrfrlsrsk rtgnskgyaf vefesedvak ivaetmnnyl fgerllechf
      121 mppekvhkel fkdwnipfkq psypsvkryn rnrtltqklr meerfkkker llrkklakkg
      181 idydfpslil qktesisktn rqtstkgqvl rkkkkkvsgt ldtpektvds qgptpvctpt
      241 flerrksqva elndddkdde ivfkqpiscv keeiqetqtp thsrkkrrrs snq
//
LOCUS       NP_001308640            1395 aa            linear   PRI 27-NOV-2025
DEFINITION  nuclear receptor coactivator 2 isoform b [Homo sapiens].
ACCESSION   NP_001308640 XP_005251190
VERSION     NP_001308640.1
DBSOURCE    REFSEQ: accession NM_001321711.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1395)
  AUTHORS   Yu,X., Wang,X., Ma,K., Gao,D., Deng,Y., Zhou,D., Ding,W., Zhao,Y.,
            Liu,Q. and Zhou,Z.
  TITLE     Tai/NCOA2 suppresses the Hedgehog pathway by directly targeting the
            transcription factor Ci/GLI
  JOURNAL   Proc Natl Acad Sci U S A 121 (47), e2409380121 (2024)
   PUBMED   39531503
REFERENCE   2  (residues 1 to 1395)
  AUTHORS   Warmke,L.M., Mustafa,A., Zou,Y.S., Davis,J.L., Ulbright,T.M. and
            Segura,S.E.
  TITLE     Myxoid epithelioid smooth muscle tumor of the vulva: A distinct
            entity with MEF2D::NCOA2 gene fusion
  JOURNAL   Genes Chromosomes Cancer 63 (1), e23209 (2024)
   PUBMED   37870842
  REMARK    GeneRIF: Myxoid epithelioid smooth muscle tumor of the vulva: A
            distinct entity with MEF2D::NCOA2 gene fusion.
REFERENCE   3  (residues 1 to 1395)
  AUTHORS   Watson,S., LaVigne,C.A., Xu,L., Surdez,D., Cyrta,J., Calderon,D.,
            Cannon,M.V., Kent,M.R., Silvius,K.M., Kucinski,J.P., Harrison,E.N.,
            Murchison,W., Rakheja,D., Tirode,F., Delattre,O., Amatruda,J.F. and
            Kendall,G.C.
  TITLE     VGLL2-NCOA2 leverages developmental programs for pediatric
            sarcomagenesis
  JOURNAL   Cell Rep 42 (1), 112013 (2023)
   PUBMED   36656711
  REMARK    GeneRIF: VGLL2-NCOA2 leverages developmental programs for pediatric
            sarcomagenesis.
REFERENCE   4  (residues 1 to 1395)
  AUTHORS   Wang,L., Motoi,T., Khanin,R., Olshen,A., Mertens,F., Bridge,J., Dal
            Cin,P., Antonescu,C.R., Singer,S., Hameed,M., Bovee,J.V.,
            Hogendoorn,P.C., Socci,N. and Ladanyi,M.
  TITLE     Identification of a novel, recurrent HEY1-NCOA2 fusion in
            mesenchymal chondrosarcoma based on a genome-wide screen of
            exon-level expression data
  JOURNAL   Genes Chromosomes Cancer 51 (2), 127-139 (2012)
   PUBMED   22034177
  REMARK    GeneRIF: The novel HEY1-NCOA2 fusion appears to be the defining and
            diagnostic gene fusion in mesenchymal chondrosarcomas
REFERENCE   5  (residues 1 to 1395)
  AUTHORS   Strehl,S., Nebral,K., Konig,M., Harbott,J., Strobl,H., Ratei,R.,
            Struski,S., Bielorai,B., Lessard,M., Zimmermann,M., Haas,O.A. and
            Izraeli,S.
  TITLE     ETV6-NCOA2: a novel fusion gene in acute leukemia associated with
            coexpression of T-lymphoid and myeloid markers and frequent NOTCH1
            mutations
  JOURNAL   Clin Cancer Res 14 (4), 977-983 (2008)
   PUBMED   18281529
  REMARK    GeneRIF: ETV6-NCOA2 fusion may define a novel subgroup of acute
            leukemia with T-lymphoid and myeloid features, which is associated
            with a high prevalence of NOTCH1 mutations.
REFERENCE   6  (residues 1 to 1395)
  AUTHORS   Fryer,C.J. and Archer,T.K.
  TITLE     Chromatin remodelling by the glucocorticoid receptor requires the
            BRG1 complex
  JOURNAL   Nature 393 (6680), 88-91 (1998)
   PUBMED   9590696
REFERENCE   7  (residues 1 to 1395)
  AUTHORS   Carapeti,M., Aguiar,R.C., Goldman,J.M. and Cross,N.C.
  TITLE     A novel fusion between MOZ and the nuclear receptor coactivator
            TIF2 in acute myeloid leukemia
  JOURNAL   Blood 91 (9), 3127-3133 (1998)
   PUBMED   9558366
REFERENCE   8  (residues 1 to 1395)
  AUTHORS   Voegel,J.J., Heine,M.J., Tini,M., Vivat,V., Chambon,P. and
            Gronemeyer,H.
  TITLE     The coactivator TIF2 contains three nuclear receptor-binding motifs
            and mediates transactivation through CBP binding-dependent and
            -independent pathways
  JOURNAL   EMBO J 17 (2), 507-519 (1998)
   PUBMED   9430642
REFERENCE   9  (residues 1 to 1395)
  AUTHORS   Hong,H., Kohli,K., Garabedian,M.J. and Stallcup,M.R.
  TITLE     GRIP1, a transcriptional coactivator for the AF-2 transactivation
            domain of steroid, thyroid, retinoid, and vitamin D receptors
  JOURNAL   Mol Cell Biol 17 (5), 2735-2744 (1997)
   PUBMED   9111344
REFERENCE   10 (residues 1 to 1395)
  AUTHORS   Voegel,J.J., Heine,M.J., Zechel,C., Chambon,P. and Gronemeyer,H.
  TITLE     TIF2, a 160 kDa transcriptional mediator for the ligand-dependent
            activation function AF-2 of nuclear receptors
  JOURNAL   EMBO J 15 (14), 3667-3675 (1996)
   PUBMED   8670870
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL712418.1, X97674.1,
            AK298528.1, AW504723.1, DA691975.1, CN291204.1, CB270668.1,
            CK903771.1 and BC047111.1.
            
            On Mar 30, 2016 this sequence version replaced XP_005251190.1.
            
            Summary: The protein encoded by this gene functions as a
            transcriptional coactivator for nuclear hormone receptors,
            including steroid, thyroid, retinoid, and vitamin D receptors. The
            encoded protein acts as an intermediary factor for the
            ligand-dependent activity of these nuclear receptors, which
            regulate their target genes upon binding of cognate response
            elements. This gene has been found to be involved in translocations
            that result in fusions with other genes in various cancers,
            including the lysine acetyltransferase 6A (KAT6A) gene in acute
            myeloid leukemia, the ETS variant 6 (ETV6) gene in acute
            lymphoblastic leukemia, and the hes related family bHLH
            transcription factor with YRPW motif 1 (HEY1) gene in mesenchymal
            chondrosarcoma. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            lacks an alternate in-frame exon in the central coding region,
            compared to variant 1, resulting in an isoform (b) that is shorter
            than isoform 1. Both variants 4 and 5 encode isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3894660.1,
                                           SRR18074967.2500713.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.3"
     Protein         1..1395
                     /product="nuclear receptor coactivator 2 isoform b"
                     /note="glucocorticoid receptor-interacting protein-1;
                     transcriptional intermediary factor 2; class E basic
                     helix-loop-helix protein 75; p160 steroid receptor
                     coactivator 2"
                     /calculated_mol_wt=151914
     Region          28..91
                     /region_name="bHLH-PAS_NCoA2_SRC2"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in nuclear receptor coactivator 2 (NCoA-2)
                     and similar proteins; cd18950"
                     /db_xref="CDD:381520"
     Site            order(30..32,36,38..39,43,68..69)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381520"
     Site            order(41..42,45..46,48..49,70,73,77,79..80,84,86)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381520"
     Region          118..175
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Site            order(139,143,149,162..165,195)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(159,163,172,175..176,202,204)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          268..378
                     /region_name="PAS_11"
                     /note="PAS domain; pfam14598"
                     /db_xref="CDD:464214"
     Region          463..587
                     /region_name="NCOA_u2"
                     /note="Unstructured region on nuclear receptor coactivator
                     protein; pfam16665"
                     /db_xref="CDD:465223"
     Region          636..709
                     /region_name="SRC-1"
                     /note="Steroid receptor coactivator; pfam08832"
                     /db_xref="CDD:462615"
     Region          731..816
                     /region_name="DUF4927"
                     /note="Domain of unknown function (DUF4927); pfam16279"
                     /db_xref="CDD:465083"
     Region          1002..1046
                     /region_name="Nuc_rec_co-act"
                     /note="Nuclear receptor coactivator; pfam08815"
                     /db_xref="CDD:462608"
     Region          1212..1269
                     /region_name="DUF1518"
                     /note="Nuclear receptor coactivator, DUF1518; pfam07469"
                     /db_xref="CDD:462174"
     CDS             1..1395
                     /gene="NCOA2"
                     /gene_synonym="bHLHe75; GRIP1; KAT13C; NCoA-2; SRC-2;
                     SRC2; TIF2"
                     /coded_by="NM_001321711.2:186..4373"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="GeneID:10499"
                     /db_xref="HGNC:HGNC:7669"
                     /db_xref="MIM:601993"
ORIGIN      
        1 msgmgentsd psraetrkrk ecpdqlgpsp krntekrnre qenkyieela elifanfndi
       61 dnfnfkpdkc ailketvkqi rqikeqekaa aanidevqks dvsstgqgvi dkdalgpmml
      121 ealdgfffvv nlegnvvfvs envtqylryn qeelmnksvy silhvgdhte fvknllpksi
      181 vnggswsgep prrnshtfnc rmlvkplpds eeeghdnqea hqkyetmqcf avsqpksike
      241 egedlqscli cvarrvpmke rpvlpssesf ttrqdlqgki tsldtstmra amkpgwedlv
      301 rrciqkfhaq hegesvsyak rhhhevlrqg lafsqiyrfs lsdgtlvaaq tksklirsqt
      361 tnepqlvisl hmlhreqnvc vmnpdltgqt mgkplnpiss nspahqalcs gnpgqdmtls
      421 sninfpingp keqmgmpmgr fggsggmnhv sgmqattpqg snyalkmnsp sqsspgmnpg
      481 qptsmlsprh rmspgvagsp rippsqfspa gslhspvgvc sstgnshsyt nsslnalqal
      541 seghgvslgs slaspdlkmg nlqnspvnmn ppplskmgsl dskdcfglyg epsegttgqa
      601 esschpgeqk etndpnlppa vsseradgqs rlhdskgqtk llqllttksd qmepsplass
      661 lsdtnkdstg slpgsgsthg tslkekhkil hrllqdsssp vdlakltaea tgkdlsqess
      721 stapgsevti kqepvspkkk enallrylld kddtkdiglp eitpklerld sktdpasntk
      781 liamktekee msfepgdqpg seldnleeil ddlqnsqlpq lfpdtrpgap agsvdkqaii
      841 ndlmqltaen spvtpvgaqk talrisqsrm ignsasrptm psgewapqss avrvtcaatt
      901 samnrpvqgg mirnpaasip mrpssqpgqr qtlqsqvmni gpselemnmg gpqysqqqap
      961 pnqtapwpes ilpidqasfa sqnrqpfgss pddllcphpa aespsdegal ldqlylalrn
     1021 fdgleeidra lgipelvsqs qavdpeqfss qdsnimleqk apvfpqqyas qaqmaqgsys
     1081 pmqdpnfhtm gqrpsyatlr mqprpglrpt glvqnqpnql rlqlqhrlqa qqnrqplmnq
     1141 isnvsnvnlt lrpgvptqap inaqmlaqrq reilnqhlrq rqmhqqqqvq qrtlmmrgqg
     1201 lnmtpsmvap sgmpatmsnp ripqanaqqf pfppnygisq qpdpgftgat tpqsplmspr
     1261 mahtqspmmq qsqanpayqa psdingwaqg nmggnsmfsq qspphfgqqa ntsmysnnmn
     1321 invsmatntg gmssmnqmtg qismtsvtsv ptsglssmgp eqvndpalrg gnlfpnqlpg
     1381 mdmikqegdt trkyc
//
LOCUS       NP_001308636            1464 aa            linear   PRI 27-NOV-2025
DEFINITION  nuclear receptor coactivator 2 isoform a [Homo sapiens].
ACCESSION   NP_001308636
VERSION     NP_001308636.1
DBSOURCE    REFSEQ: accession NM_001321707.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1464)
  AUTHORS   Yu,X., Wang,X., Ma,K., Gao,D., Deng,Y., Zhou,D., Ding,W., Zhao,Y.,
            Liu,Q. and Zhou,Z.
  TITLE     Tai/NCOA2 suppresses the Hedgehog pathway by directly targeting the
            transcription factor Ci/GLI
  JOURNAL   Proc Natl Acad Sci U S A 121 (47), e2409380121 (2024)
   PUBMED   39531503
REFERENCE   2  (residues 1 to 1464)
  AUTHORS   Warmke,L.M., Mustafa,A., Zou,Y.S., Davis,J.L., Ulbright,T.M. and
            Segura,S.E.
  TITLE     Myxoid epithelioid smooth muscle tumor of the vulva: A distinct
            entity with MEF2D::NCOA2 gene fusion
  JOURNAL   Genes Chromosomes Cancer 63 (1), e23209 (2024)
   PUBMED   37870842
  REMARK    GeneRIF: Myxoid epithelioid smooth muscle tumor of the vulva: A
            distinct entity with MEF2D::NCOA2 gene fusion.
REFERENCE   3  (residues 1 to 1464)
  AUTHORS   Watson,S., LaVigne,C.A., Xu,L., Surdez,D., Cyrta,J., Calderon,D.,
            Cannon,M.V., Kent,M.R., Silvius,K.M., Kucinski,J.P., Harrison,E.N.,
            Murchison,W., Rakheja,D., Tirode,F., Delattre,O., Amatruda,J.F. and
            Kendall,G.C.
  TITLE     VGLL2-NCOA2 leverages developmental programs for pediatric
            sarcomagenesis
  JOURNAL   Cell Rep 42 (1), 112013 (2023)
   PUBMED   36656711
  REMARK    GeneRIF: VGLL2-NCOA2 leverages developmental programs for pediatric
            sarcomagenesis.
REFERENCE   4  (residues 1 to 1464)
  AUTHORS   Wang,L., Motoi,T., Khanin,R., Olshen,A., Mertens,F., Bridge,J., Dal
            Cin,P., Antonescu,C.R., Singer,S., Hameed,M., Bovee,J.V.,
            Hogendoorn,P.C., Socci,N. and Ladanyi,M.
  TITLE     Identification of a novel, recurrent HEY1-NCOA2 fusion in
            mesenchymal chondrosarcoma based on a genome-wide screen of
            exon-level expression data
  JOURNAL   Genes Chromosomes Cancer 51 (2), 127-139 (2012)
   PUBMED   22034177
  REMARK    GeneRIF: The novel HEY1-NCOA2 fusion appears to be the defining and
            diagnostic gene fusion in mesenchymal chondrosarcomas
REFERENCE   5  (residues 1 to 1464)
  AUTHORS   Strehl,S., Nebral,K., Konig,M., Harbott,J., Strobl,H., Ratei,R.,
            Struski,S., Bielorai,B., Lessard,M., Zimmermann,M., Haas,O.A. and
            Izraeli,S.
  TITLE     ETV6-NCOA2: a novel fusion gene in acute leukemia associated with
            coexpression of T-lymphoid and myeloid markers and frequent NOTCH1
            mutations
  JOURNAL   Clin Cancer Res 14 (4), 977-983 (2008)
   PUBMED   18281529
  REMARK    GeneRIF: ETV6-NCOA2 fusion may define a novel subgroup of acute
            leukemia with T-lymphoid and myeloid features, which is associated
            with a high prevalence of NOTCH1 mutations.
REFERENCE   6  (residues 1 to 1464)
  AUTHORS   Fryer,C.J. and Archer,T.K.
  TITLE     Chromatin remodelling by the glucocorticoid receptor requires the
            BRG1 complex
  JOURNAL   Nature 393 (6680), 88-91 (1998)
   PUBMED   9590696
REFERENCE   7  (residues 1 to 1464)
  AUTHORS   Carapeti,M., Aguiar,R.C., Goldman,J.M. and Cross,N.C.
  TITLE     A novel fusion between MOZ and the nuclear receptor coactivator
            TIF2 in acute myeloid leukemia
  JOURNAL   Blood 91 (9), 3127-3133 (1998)
   PUBMED   9558366
REFERENCE   8  (residues 1 to 1464)
  AUTHORS   Voegel,J.J., Heine,M.J., Tini,M., Vivat,V., Chambon,P. and
            Gronemeyer,H.
  TITLE     The coactivator TIF2 contains three nuclear receptor-binding motifs
            and mediates transactivation through CBP binding-dependent and
            -independent pathways
  JOURNAL   EMBO J 17 (2), 507-519 (1998)
   PUBMED   9430642
REFERENCE   9  (residues 1 to 1464)
  AUTHORS   Hong,H., Kohli,K., Garabedian,M.J. and Stallcup,M.R.
  TITLE     GRIP1, a transcriptional coactivator for the AF-2 transactivation
            domain of steroid, thyroid, retinoid, and vitamin D receptors
  JOURNAL   Mol Cell Biol 17 (5), 2735-2744 (1997)
   PUBMED   9111344
REFERENCE   10 (residues 1 to 1464)
  AUTHORS   Voegel,J.J., Heine,M.J., Zechel,C., Chambon,P. and Gronemeyer,H.
  TITLE     TIF2, a 160 kDa transcriptional mediator for the ligand-dependent
            activation function AF-2 of nuclear receptors
  JOURNAL   EMBO J 15 (14), 3667-3675 (1996)
   PUBMED   8670870
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022730.7, X97674.1,
            AW504723.1, DA691975.1, CN291204.1, CB270668.1, CK903771.1 and
            BC047111.1.
            
            Summary: The protein encoded by this gene functions as a
            transcriptional coactivator for nuclear hormone receptors,
            including steroid, thyroid, retinoid, and vitamin D receptors. The
            encoded protein acts as an intermediary factor for the
            ligand-dependent activity of these nuclear receptors, which
            regulate their target genes upon binding of cognate response
            elements. This gene has been found to be involved in translocations
            that result in fusions with other genes in various cancers,
            including the lysine acetyltransferase 6A (KAT6A) gene in acute
            myeloid leukemia, the ETS variant 6 (ETV6) gene in acute
            lymphoblastic leukemia, and the hes related family bHLH
            transcription factor with YRPW motif 1 (HEY1) gene in mesenchymal
            chondrosarcoma. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 all encode isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.718494.1,
                                           SRR14038192.2346183.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.3"
     Protein         1..1464
                     /product="nuclear receptor coactivator 2 isoform a"
                     /note="glucocorticoid receptor-interacting protein-1;
                     transcriptional intermediary factor 2; class E basic
                     helix-loop-helix protein 75; p160 steroid receptor
                     coactivator 2"
                     /calculated_mol_wt=159026
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          28..91
                     /region_name="bHLH-PAS_NCoA2_SRC2"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in nuclear receptor coactivator 2 (NCoA-2)
                     and similar proteins; cd18950"
                     /db_xref="CDD:381520"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            order(30..32,36,38..39,43,68..69)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381520"
     Site            order(41..42,45..46,48..49,70,73,77,79..80,84,86)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381520"
     Region          118..175
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Site            order(139,143,149,162..165,195)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(159,163,172,175..176,202,204)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          268..378
                     /region_name="PAS_11"
                     /note="PAS domain; pfam14598"
                     /db_xref="CDD:464214"
     Site            338
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q61026; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          463..587
                     /region_name="NCOA_u2"
                     /note="Unstructured region on nuclear receptor coactivator
                     protein; pfam16665"
                     /db_xref="CDD:465223"
     Region          468..513
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          557..683
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          636..709
                     /region_name="SRC-1"
                     /note="Steroid receptor coactivator; pfam08832"
                     /db_xref="CDD:462615"
     Site            636
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q61026; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            640
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          641..645
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            682
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          690..694
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          691..743
                     /region_name="CASP8AP2-binding.
                     /evidence=ECO:0000250|UniProtKB:Q61026"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            699
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          709..737
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          730..1121
                     /region_name="Interaction with BMAL1.
                     /evidence=ECO:0000250|UniProtKB:Q61026"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          731..816
                     /region_name="DUF4927"
                     /note="Domain of unknown function (DUF4927); pfam16279"
                     /db_xref="CDD:465083"
     Site            736
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          745..749
                     /region_name="LXXLL motif 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            771
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            780
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            785
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            864
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q61026; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            869..870
                     /site_type="other"
                     /note="Breakpoint for translocation to form KAT6A-NCOA2.
                     /evidence=ECO:0000269|PubMed:12676584,
                     ECO:0000269|PubMed:15657427, ECO:0000269|PubMed:9558366;
                     propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            874
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q61026; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          878..882
                     /region_name="LXXLL motif 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          973..1003
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          1017..1038
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          1051..1074
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          1071..1115
                     /region_name="Nuc_rec_co-act"
                     /note="Nuclear receptor coactivator; pfam08815"
                     /db_xref="CDD:462608"
     Region          1079..1087
                     /region_name="LLXXLXXXL motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1173
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1177
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1190
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1196
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1203
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1221
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1240
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q61026; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1261
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1266
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          1281..1338
                     /region_name="DUF1518"
                     /note="Nuclear receptor coactivator, DUF1518; pfam07469"
                     /db_xref="CDD:462174"
     Region          1441..1464
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     CDS             1..1464
                     /gene="NCOA2"
                     /gene_synonym="bHLHe75; GRIP1; KAT13C; NCoA-2; SRC-2;
                     SRC2; TIF2"
                     /coded_by="NM_001321707.2:134..4528"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS47872.1"
                     /db_xref="GeneID:10499"
                     /db_xref="HGNC:HGNC:7669"
                     /db_xref="MIM:601993"
ORIGIN      
        1 msgmgentsd psraetrkrk ecpdqlgpsp krntekrnre qenkyieela elifanfndi
       61 dnfnfkpdkc ailketvkqi rqikeqekaa aanidevqks dvsstgqgvi dkdalgpmml
      121 ealdgfffvv nlegnvvfvs envtqylryn qeelmnksvy silhvgdhte fvknllpksi
      181 vnggswsgep prrnshtfnc rmlvkplpds eeeghdnqea hqkyetmqcf avsqpksike
      241 egedlqscli cvarrvpmke rpvlpssesf ttrqdlqgki tsldtstmra amkpgwedlv
      301 rrciqkfhaq hegesvsyak rhhhevlrqg lafsqiyrfs lsdgtlvaaq tksklirsqt
      361 tnepqlvisl hmlhreqnvc vmnpdltgqt mgkplnpiss nspahqalcs gnpgqdmtls
      421 sninfpingp keqmgmpmgr fggsggmnhv sgmqattpqg snyalkmnsp sqsspgmnpg
      481 qptsmlsprh rmspgvagsp rippsqfspa gslhspvgvc sstgnshsyt nsslnalqal
      541 seghgvslgs slaspdlkmg nlqnspvnmn ppplskmgsl dskdcfglyg epsegttgqa
      601 esschpgeqk etndpnlppa vsseradgqs rlhdskgqtk llqllttksd qmepsplass
      661 lsdtnkdstg slpgsgsthg tslkekhkil hrllqdsssp vdlakltaea tgkdlsqess
      721 stapgsevti kqepvspkkk enallrylld kddtkdiglp eitpklerld sktdpasntk
      781 liamktekee msfepgdqpg seldnleeil ddlqnsqlpq lfpdtrpgap agsvdkqaii
      841 ndlmqltaen spvtpvgaqk talrisqstf nnprpgqlgr llpnqnlpld itlqsptgag
      901 pfppirnssp ysvipqpgmm gnqgmignqg nlgnsstgmi gnsasrptmp sgewapqssa
      961 vrvtcaatts amnrpvqggm irnpaasipm rpssqpgqrq tlqsqvmnig pselemnmgg
     1021 pqysqqqapp nqtapwpesi lpidqasfas qnrqpfgssp ddllcphpaa espsdegall
     1081 dqlylalrnf dgleeidral gipelvsqsq avdpeqfssq dsnimleqka pvfpqqyasq
     1141 aqmaqgsysp mqdpnfhtmg qrpsyatlrm qprpglrptg lvqnqpnqlr lqlqhrlqaq
     1201 qnrqplmnqi snvsnvnltl rpgvptqapi naqmlaqrqr eilnqhlrqr qmhqqqqvqq
     1261 rtlmmrgqgl nmtpsmvaps gmpatmsnpr ipqanaqqfp fppnygisqq pdpgftgatt
     1321 pqsplmsprm ahtqspmmqq sqanpayqap sdingwaqgn mggnsmfsqq spphfgqqan
     1381 tsmysnnmni nvsmatntgg mssmnqmtgq ismtsvtsvp tsglssmgpe qvndpalrgg
     1441 nlfpnqlpgm dmikqegdtt rkyc
//
LOCUS       NP_001107605             977 aa            linear   PRI 27-NOV-2025
DEFINITION  synaptopodin 2-like protein isoform a [Homo sapiens].
ACCESSION   NP_001107605
VERSION     NP_001107605.1
DBSOURCE    REFSEQ: accession NM_001114133.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 977)
  AUTHORS   Wu,J., Ouyang,P., Huang,R., Cui,Y., Yang,Z., Xu,W., Ma,R.,
            Xiang,G., Zeng,W., Wu,W. and Li,J.
  TITLE     METTL16 Promotes Stability of SYNPO2L mRNA and leading to Cancer
            Cell Lung Metastasis by Secretion of COL10A1 and attract the
            Cancer-Associated Fibroblasts
  JOURNAL   Int J Biol Sci 20 (11), 4128-4145 (2024)
   PUBMED   39247832
  REMARK    GeneRIF: METTL16 Promotes Stability of SYNPO2L mRNA and leading to
            Cancer Cell Lung Metastasis by Secretion of COL10A1 and attract the
            Cancer-Associated Fibroblasts.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 977)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 977)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 977)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 977)
  AUTHORS   van Eldik,W., den Adel,B., Monshouwer-Kloots,J., Salvatori,D.,
            Maas,S., van der Made,I., Creemers,E.E., Frank,D., Frey,N.,
            Boontje,N., van der Velden,J., Steendijk,P., Mummery,C., Passier,R.
            and Beqqali,A.
  TITLE     Z-disc protein CHAPb induces cardiomyopathy and contractile
            dysfunction in the postnatal heart
  JOURNAL   PLoS One 12 (12), e0189139 (2017)
   PUBMED   29206857
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 977)
  AUTHORS   Lubitz,S.A., Brody,J.A., Bihlmeyer,N.A., Roselli,C., Weng,L.C.,
            Christophersen,I.E., Alonso,A., Boerwinkle,E., Gibbs,R.A.,
            Bis,J.C., Cupples,L.A., Mohler,P.J., Nickerson,D.A., Muzny,D.,
            Perez,M.V., Psaty,B.M., Soliman,E.Z., Sotoodehnia,N., Lunetta,K.L.,
            Benjamin,E.J., Heckbert,S.R., Arking,D.E., Ellinor,P.T. and Lin,H.
  CONSRTM   NHLBI GO Exome Sequencing Project
  TITLE     Whole Exome Sequencing in Atrial Fibrillation
  JOURNAL   PLoS Genet 12 (9), e1006284 (2016)
   PUBMED   27589061
  REMARK    GeneRIF: we did not observe associations between coding genetic
            variants and Atrial fibrillation (AF), suggesting that large-effect
            coding variation is not the predominant mechanism underlying AF. A
            coding variant in SYNPO2L requires further evaluation to determine
            whether it is causally related to AF
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 977)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 977)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 977)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB188489.1 and AK022983.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB188489.1, AK295873.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA2142363 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394810.3/ ENSP00000378289.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..977
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..977
                     /product="synaptopodin 2-like protein isoform a"
                     /note="synaptopodin 2-like protein"
                     /calculated_mol_wt=102350
     Region          8..85
                     /region_name="PDZ_SYNPO2-like"
                     /note="PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin
                     2-like protein (SYNPO2L), and related domains; cd10820"
                     /db_xref="CDD:467264"
     Site            order(16..22,34,37,66,70,73..74)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467264"
     Region          91..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Region          <168..650
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Region          317..352
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Region          364..677
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            386
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Region          <415..550
                     /region_name="PRK14954"
                     /note="DNA polymerase III subunits gamma and tau;
                     Provisional"
                     /db_xref="CDD:184918"
     Site            466
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            469
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            479
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            670
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            678
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Region          697..802
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            705
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            757
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            788
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            790
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            792
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            806
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            826
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            889
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            891
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            892
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            898
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            910
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            921
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Region          922..950
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            955
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     Site            957
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWB1; propagated from
                     UniProtKB/Swiss-Prot (Q9H987.3)"
     CDS             1..977
                     /gene="SYNPO2L"
                     /gene_synonym="CHAP"
                     /coded_by="NM_001114133.3:108..3041"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44438.1"
                     /db_xref="GeneID:79933"
                     /db_xref="HGNC:HGNC:23532"
                     /db_xref="MIM:621429"
ORIGIN      
        1 mgaeeevlvt lsggapwgfr lhggaeqrkp lqvskirrrs qagraglrer dqllaingvs
       61 ctnlshasam slidasgnql vltvqrlade gpvqspsphe lqvlsplspl speppgapvp
      121 qplqpgslrs ppdseayyge tdsdadgpat qekprrprrr gptrptppga ppdevylsds
      181 paepaptipg ppsqgdsrvs spswedgaal qpppaealll phgplrpgph lipmvgpvph
      241 pvaedlttty tqkakqaklq raeslqeksi keaktkcrti aslltaapnp hskgvlmfkk
      301 rrqrakkytl vsfgaaagtg aeeedgvppt seseldeeaf sdarsltnqs dwdspyldme
      361 laragsrase gqgsglggql sevsgrgvql feqqrqrads stqelarvep aamlngeglq
      421 sppraqsapp eaavlppspl papvasprpf qpgggaptpa psifnrsarp ftpglqgqrp
      481 tttsvifrpl apkrandslg glspapppfl ssqgptplps ftsgvpshap vsgspstprs
      541 sgpvtatssl yipapsrpvt pggapeppap psaaamtsta siflsaplrp sarpeapapg
      601 pgapeppsar eqrisvpaar tgilqearrr gtrkqmfrpg keetknspnp ellslvqnld
      661 ekpraggaes gpeedalslg aeacnfmqpv garsyktlph vtpktpppma pktpppmtpk
      721 tpppvapkpp srglldglvn gaassagipe pprlqgrgge lfakrqsrad ryvvegtpgp
      781 glgprprsps ptpslppswk yspnirappp iaynpllspf fpqaartlpk aqsqgpratp
      841 kqgikaldfm rhqpyqlkta mfcfdevppt pgpiasgspk tarvqeirrf stpapqptae
      901 plaptvlapr aattldepiw rtelasapvp spapppeapr glgaspsscg fqvarprfsa
      961 trtglqahvw rpgaghq
//
LOCUS       NP_055730               1710 aa            linear   PRI 27-NOV-2025
DEFINITION  ankyrin repeat domain-containing protein 26 isoform 1 [Homo
            sapiens].
ACCESSION   NP_055730 XP_374779
VERSION     NP_055730.2
DBSOURCE    REFSEQ: accession NM_014915.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1710)
  AUTHORS   Trizuljak,J., Likavcova,P., Stano Kozubik,K., Vrzalova,Z.,
            Hynst,J., Deissova,T., Stika,J., Radova,L., Prudkova,M.,
            Vaculova,J., Blahakova,I., Smejkal,P., Kamelander,J.,
            Pospisilova,S. and Doubek,M.
  TITLE     Impact of thrombocytopenia-associated c.-118C>T and c.-140C>G
            ANKRD26 5'UTR variants in three-generational pedigree
  JOURNAL   Platelets 35 (1), 2388103 (2024)
   PUBMED   39212265
  REMARK    GeneRIF: Impact of thrombocytopenia-associated c.-118C>T and
            c.-140C>G ANKRD26 5'UTR variants in three-generational pedigree.
REFERENCE   2  (residues 1 to 1710)
  AUTHORS   Dunstan-Harrison,C., Morison,I.M. and Ledgerwood,E.C.
  TITLE     Inherited thrombocytopenia associated with a variant in the FLI1
            binding site in the 5' UTR of ANKRD26
  JOURNAL   Clin Genet 106 (3), 315-320 (2024)
   PUBMED   38757516
  REMARK    GeneRIF: Inherited thrombocytopenia associated with a variant in
            the FLI1 binding site in the 5' UTR of ANKRD26.
REFERENCE   3  (residues 1 to 1710)
  AUTHORS   Homan,C.C., Scott,H.S. and Brown,A.L.
  TITLE     Hereditary platelet disorders associated with germ line variants in
            RUNX1, ETV6, and ANKRD26
  JOURNAL   Blood 141 (13), 1533-1543 (2023)
   PUBMED   36626254
  REMARK    GeneRIF: Hereditary platelet disorders associated with germ line
            variants in RUNX1, ETV6, and ANKRD26.
REFERENCE   4  (residues 1 to 1710)
  AUTHORS   Ovsyannikova,G.S., Fedorova,D.V., Tesakov,I.P., Martyanov,A.A.,
            Ignatova,A.A., Ponomarenko,E.A., Zharkov,P.A., Pavlova,A.V.,
            Raykina,E.V., Maschan,M.A., Panteleev,M.A., Novichkova,G.A.,
            Sveshnikova,A.N. and Smetanina,N.S.
  TITLE     Platelet functional abnormalities and clinical presentation in
            pediatric patients with germline RUNX1, ANKRD26, and ETV6 mutations
  JOURNAL   Haematologica 107 (10), 2511-2516 (2022)
   PUBMED   35796010
  REMARK    GeneRIF: Platelet functional abnormalities and clinical
            presentation in pediatric patients with germline RUNX1, ANKRD26,
            and ETV6 mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1710)
  AUTHORS   Sullivan,M.J., Palmer,E.L. and Botero,J.P.
  TITLE     ANKRD26-Related Thrombocytopenia and Predisposition to Myeloid
            Neoplasms
  JOURNAL   Curr Hematol Malig Rep 17 (5), 105-112 (2022)
   PUBMED   35751752
  REMARK    GeneRIF: ANKRD26-Related Thrombocytopenia and Predisposition to
            Myeloid Neoplasms.
            Review article
REFERENCE   6  (residues 1 to 1710)
  AUTHORS   Noris,P., Perrotta,S., Seri,M., Pecci,A., Gnan,C., Loffredo,G.,
            Pujol-Moix,N., Zecca,M., Scognamiglio,F., De Rocco,D., Punzo,F.,
            Melazzini,F., Scianguetta,S., Casale,M., Marconi,C., Pippucci,T.,
            Amendola,G., Notarangelo,L.D., Klersy,C., Civaschi,E.,
            Balduini,C.L. and Savoia,A.
  TITLE     Mutations in ANKRD26 are responsible for a frequent form of
            inherited thrombocytopenia: analysis of 78 patients from 21
            families
  JOURNAL   Blood 117 (24), 6673-6680 (2011)
   PUBMED   21467542
  REMARK    GeneRIF: The ANKRD26-related thrombocytopenia has to be taken into
            consideration in the differential diagnosis of isolated
            thrombocytopenias.
REFERENCE   7  (residues 1 to 1710)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   8  (residues 1 to 1710)
  AUTHORS   Pippucci,T., Savoia,A., Perrotta,S., Pujol-Moix,N., Noris,P.,
            Castegnaro,G., Pecci,A., Gnan,C., Punzo,F., Marconi,C.,
            Gherardi,S., Loffredo,G., De Rocco,D., Scianguetta,S., Barozzi,S.,
            Magini,P., Bozzi,V., Dezzani,L., Di Stazio,M., Ferraro,M.,
            Perini,G., Seri,M. and Balduini,C.L.
  TITLE     Mutations in the 5' UTR of ANKRD26, the ankirin repeat domain 26
            gene, cause an autosomal-dominant form of inherited
            thrombocytopenia, THC2
  JOURNAL   Am J Hum Genet 88 (1), 115-120 (2011)
   PUBMED   21211618
  REMARK    GeneRIF: mutations in the 5' UTR of ANKRD26 are implicated in
            thrombocytopenia 2.
REFERENCE   9  (residues 1 to 1710)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   10 (residues 1 to 1710)
  AUTHORS   Perez Botero,J., Dugan,S.N. and Anderson,M.W.
  TITLE     ANKRD26-Related Thrombocytopenia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29927566
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA712092.1, CD626319.1,
            AK001137.1, DB228067.1, AB028997.1 and AL137351.1.
            
            On Aug 1, 2007 this sequence version replaced NP_055730.1.
            
            Summary: This gene encodes a protein containing N-terminal ankyrin
            repeats which function in protein-protein interactions. Mutations
            in this gene are associated with autosomal dominant
            thrombocytopenia-2. Pseudogenes of this gene are found on
            chromosome 7, 10, 13 and 16. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Dec 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.187283.1,
                                           SRR14038197.2294305.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376087.5/ ENSP00000365255.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1710
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.1"
     Protein         1..1710
                     /product="ankyrin repeat domain-containing protein 26
                     isoform 1"
                     /note="ankyrin repeat domain-containing protein 26;
                     GNS/ANKRD26/NCKAP1L fusion; ankyrin repeat domain
                     containing 26"
                     /calculated_mol_wt=196280
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          44..>210
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          45..75
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Site            order(79,81,85..86,89..91,93..94,98,101,110,112,114,
                     118..119,122..124,126..127,131,134,143,145,147,151..152,
                     155..157,159..160,164,167,176)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          79..110
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          79..108
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          112..143
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          112..141
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          145..176
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          145..174
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          178..209
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          178..207
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          222..274
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q811D2; propagated from
                     UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          504..630
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          650..698
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          <747..1414
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          892..912
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          914..1217
                     /region_name="CCDC144C"
                     /note="CCDC144C protein coiled-coil region; pfam14915"
                     /db_xref="CDD:464371"
     Region          1394..>1567
                     /region_name="DR0291"
                     /note="Predicted nucleic acid-binding protein DR0291,
                     contains C4-type Zn-ribbon domain [General function
                     prediction only]; COG1579"
                     /db_xref="CDD:441187"
     Region          1523..1631
                     /region_name="DUF3496"
                     /note="Domain of unknown function (DUF3496); pfam12001"
                     /db_xref="CDD:463425"
     CDS             1..1710
                     /gene="ANKRD26"
                     /gene_synonym="bA145E8.1; THC2"
                     /coded_by="NM_014915.3:169..5301"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41499.1"
                     /db_xref="GeneID:22852"
                     /db_xref="HGNC:HGNC:29186"
                     /db_xref="MIM:610855"
ORIGIN      
        1 mkkifskkge splgsfarrq rssaggggep gegaysqpgy hvrdrdlgki hkaasagnva
       61 kvqqilllrk nglndrdkmn rtalhlacan ghpevvtllv drkcqlnvcd nenrtalmka
      121 vqcqeekcat illehgadpn ladvhgntal hyavynedis vatklllyda nieaknkddl
      181 tplllavsgk kqqmveflik kkanvnavdk lesshqlise ykeeripkhs sqnsnsvdes
      241 sedslsrlsg kpgvddswpt sddedlnfdt knvpkpslak lmtasqqsrk nleatygtvr
      301 tgnrtlfedr dsdsqdevvv eslpttsikv qcfshptyqs pdllpkpshk slanpglmke
      361 eptkpgiakk engidiiesa pleqtnndnl tyvdevhknn rsdmmsalgl gqeediespw
      421 dsesisenfp qkyvdplaga adgkeknign eqaedvfyip scmsgsrnfk makledtrnv
      481 gmpvahmesp erylhlkpti emkdsvpnka ggmkdvqtsk aaehdlevas eeeqeregse
      541 nnqpqveeer kkhrnnemev sanihdgatd daeddddddg liqkrksget dhqqfprken
      601 keyassgpal qmkevkstek ekrtskesvn spvfgkasll tggllqvddd sslseidede
      661 grptkktsne knkvknqiqs mddvddltqs setasedcel phssyknfml lieqlgmeck
      721 dsvsllkiqd aalscerlle lkknhcellt vkikkmedkv nvlqrelset keiksqlehq
      781 kvewerelcs lrfslnqeee krrnadtlye kireqlrrke eqyrkevevk qqlelslqtl
      841 emelrtvksn lnqvvqernd aqrqlsreqn armlqdgilt nhlskqkeie maqkkmnsen
      901 shsheeekdl shknsmlqee iamlrleidt iknqnqekek kcfedlkivk eknedlqkti
      961 kqneetltqt isqyngrlsv ltaenamlns klenekqske rleaevesyh srlaaaihdr
     1021 dqsetskrel elafqrarde csrlqdkmnf dvsnlkdnne ilsqqlfkte sklnsleief
     1081 hhtrdalrek tlglervqkd lsqtqcqmke meqkyqneqv kvnkyigkqe sveerlsqlq
     1141 senmllrqql ddahnkadnk ektviniqdq fhaivqklqa esekqsllle ernkelisec
     1201 nhlkerqyqy enekaerevv vrqlqqelad tlkkqsmsea slevtsryri nledetqdlk
     1261 kklgqirnql qeaqdrhtea vrcaekmqdh kqklekdnak lkvtvkkqmd kieelqknll
     1321 nanlsedeke qlkklmelkq slecnldqem kknvelerei tgfknllkmt rkklneyeng
     1381 efsfhgdlkt sqfemdiqin klkhkiddlt aeletagskc lhldtknqil qeellsmktv
     1441 qkkceklqkn kkkleqevin lrshiernmv elgqvkqykq eieerarqei aeklkevnlf
     1501 lqaqaasqen leqfrennfa smksqmelri kdleselski ktsqedfnkt elekykqlyl
     1561 eelkvrksls skltktnerl aevntkllve kqqsrslftt lttrpvmepp cvgnlnnsld
     1621 lnrklipren lvistsnpra snnsmenyls kmqqelekni trelkeaaae lesgsiaspl
     1681 gstdesnlnq dlvwkasrey vqvlkknymi
//
LOCUS       NP_003398                326 aa            linear   PRI 27-NOV-2025
DEFINITION  mRNA decay activator protein ZFP36 [Homo sapiens].
ACCESSION   NP_003398
VERSION     NP_003398.3
DBSOURCE    REFSEQ: accession NM_003407.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Pekovic,F., Lai,W.S., Corbo,J., Hicks,S.N., Luke,K.,
            Blackshear,P.J. and Valkov,E.
  TITLE     Multivalent interactions with CCR4-NOT and PABPC1 determine mRNA
            repression efficiency by tristetraprolin
  JOURNAL   Nat Commun 16 (1), 7528 (2025)
   PUBMED   40804313
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Saenz-Narciso,B., Bell,S.E., Matheson,L.S., Venigalla,R.K.C. and
            Turner,M.
  TITLE     ZFP36-family RNA-binding proteins in regulatory T cells reinforce
            immune homeostasis
  JOURNAL   Nat Commun 16 (1), 4192 (2025)
   PUBMED   40328742
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Lu,Z., Cao,R., Geng,F. and Pan,Y.
  TITLE     Persistent infection with Porphyromonas gingivalis increases the
            tumorigenic potential of human immortalised oral epithelial cells
            through ZFP36 inhibition
  JOURNAL   Cell Prolif 57 (6), e13609 (2024)
   PUBMED   38351596
  REMARK    GeneRIF: Persistent infection with Porphyromonas gingivalis
            increases the tumorigenic potential of human immortalised oral
            epithelial cells through ZFP36 inhibition.
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Schutt,W.R., Conde,J.N., Mladinich,M.C., Himmler,G.E. and
            Mackow,E.R.
  TITLE     ZIKV induction of tristetraprolin in endothelial and Sertoli cells
            post-transcriptionally inhibits IFNbeta/lambda expression and
            promotes ZIKV persistence
  JOURNAL   mBio 14 (5), e0174223 (2023)
   PUBMED   37707056
  REMARK    GeneRIF: ZIKV induction of tristetraprolin in endothelial and
            Sertoli cells post-transcriptionally inhibits IFNbeta/lambda
            expression and promotes ZIKV persistence.
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Zhang,T., Qiu,L., Cao,J., Li,Q., Zhang,L., An,G., Ni,J., Jia,H.,
            Li,S. and Li,K.
  TITLE     ZFP36 loss-mediated BARX1 stabilization promotes malignant
            phenotypes by transactivating master oncogenes in NSCLC
  JOURNAL   Cell Death Dis 14 (8), 527 (2023)
   PUBMED   37587140
  REMARK    GeneRIF: ZFP36 loss-mediated BARX1 stabilization promotes malignant
            phenotypes by transactivating master oncogenes in NSCLC.
            Erratum:[Cell Death Dis. 2025 May 22;16(1):410. doi:
            10.1038/s41419-025-07718-6. PMID: 40404626]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Taylor,G.A., Thompson,M.J., Lai,W.S. and Blackshear,P.J.
  TITLE     Phosphorylation of tristetraprolin, a potential zinc finger
            transcription factor, by mitogen stimulation in intact cells and by
            mitogen-activated protein kinase in vitro
  JOURNAL   J Biol Chem 270 (22), 13341-13347 (1995)
   PUBMED   7768935
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Heximer,S.P. and Forsdyke,D.R.
  TITLE     A human putative lymphocyte G0/G1 switch gene homologous to a
            rodent gene encoding a zinc-binding potential transcription factor
  JOURNAL   DNA Cell Biol 12 (1), 73-88 (1993)
   PUBMED   8422274
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Taylor,G.A., Lai,W.S., Oakey,R.J., Seldin,M.F., Shows,T.B.,
            Eddy,R.L. Jr. and Blackshear,P.J.
  TITLE     The human TTP protein: sequence, alignment with related proteins,
            and chromosomal localization of the mouse and human genes
  JOURNAL   Nucleic Acids Res 19 (12), 3454 (1991)
   PUBMED   2062660
REFERENCE   9  (residues 1 to 326)
  AUTHORS   DuBois,R.N., McLane,M.W., Ryder,K., Lau,L.F. and Nathans,D.
  TITLE     A growth factor-inducible nuclear protein with a novel
            cysteine/histidine repetitive sequence
  JOURNAL   J Biol Chem 265 (31), 19185-19191 (1990)
   PUBMED   1699942
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Lai,W.S., Stumpo,D.J. and Blackshear,P.J.
  TITLE     Rapid insulin-stimulated accumulation of an mRNA encoding a
            proline-rich protein
  JOURNAL   J Biol Chem 265 (27), 16556-16563 (1990)
   PUBMED   2204625
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            M92843.1 and AC011500.7.
            
            On Sep 18, 2018 this sequence version replaced NP_003398.2.
            
            Sequence Note:.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.647245.1,
                                           SRR3476690.665021.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000597629.3/
                                                ENSP00000469647.2
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..326
                     /product="mRNA decay activator protein ZFP36"
                     /note="tristetraprolin; tristetraproline; zinc finger
                     protein 36 homolog; G0/G1 switch regulatory protein 24;
                     growth factor-inducible nuclear protein NUP475; zinc
                     finger protein 36, C3H type, homolog; ZFP36 ring finger
                     protein"
                     /calculated_mol_wt=33872
     Region          1..174
                     /region_name="Necessary for localization of ARE-containing
                     mRNAs to processing bodies (PBs).
                     /evidence=ECO:0000269|PubMed:17369404"
                     /note="propagated from UniProtKB/Swiss-Prot (P26651.1)"
     Region          1..100
                     /region_name="Necessary and sufficient for the association
                     with mRNA decay enzymes and mRNA decay activation.
                     /evidence=ECO:0000269|PubMed:15687258"
                     /note="propagated from UniProtKB/Swiss-Prot (P26651.1)"
     Region          1..15
                     /region_name="Necessary for nuclear export.
                     /evidence=ECO:0000250|UniProtKB:P47973"
                     /note="propagated from UniProtKB/Swiss-Prot (P26651.1)"
     Region          13..66
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26651.1)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK2.
                     /evidence=ECO:0000250|UniProtKB:P22893; propagated from
                     UniProtKB/Swiss-Prot (P26651.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16262601,
                     ECO:0000269|PubMed:20221403; propagated from
                     UniProtKB/Swiss-Prot (P26651.1)"
     Region          78..102
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26651.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16262601; propagated from
                     UniProtKB/Swiss-Prot (P26651.1)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P22893; propagated from
                     UniProtKB/Swiss-Prot (P26651.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:16262601; propagated from
                     UniProtKB/Swiss-Prot (P26651.1)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20221403,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P26651.1)"
     Region          95..168
                     /region_name="Necessary for nuclear localization.
                     /evidence=ECO:0000250|UniProtKB:P47973"
                     /note="propagated from UniProtKB/Swiss-Prot (P26651.1)"
     Region          97..173
                     /region_name="Necessary for RNA-binding.
                     /evidence=ECO:0000269|PubMed:10751406,
                     ECO:0000269|PubMed:12748283"
                     /note="propagated from UniProtKB/Swiss-Prot (P26651.1)"
     Region          100..326
                     /region_name="Necessary for localization of ARE-containing
                     mRNAs to processing bodies (PBs).
                     /evidence=ECO:0000269|PubMed:17369404"
                     /note="propagated from UniProtKB/Swiss-Prot (P26651.1)"
     Region          103..194
                     /region_name="Necessary for interaction with PABPN1.
                     /evidence=ECO:0000250|UniProtKB:P22893"
                     /note="propagated from UniProtKB/Swiss-Prot (P26651.1)"
     Region          <104..>200
                     /region_name="CTH1"
                     /note="CCCH-type Zn-finger protein [General function
                     prediction only]; COG5063"
                     /db_xref="CDD:227395"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16262601; propagated from
                     UniProtKB/Swiss-Prot (P26651.1)"
     Region          174..326
                     /region_name="Necessary for mRNA decay activation.
                     /evidence=ECO:0000269|PubMed:15687258"
                     /note="propagated from UniProtKB/Swiss-Prot (P26651.1)"
     Region          175..245
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26651.1)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK2.
                     /evidence=ECO:0000269|PubMed:16262601,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P26651.1)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16262601; propagated from
                     UniProtKB/Swiss-Prot (P26651.1)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16262601; propagated from
                     UniProtKB/Swiss-Prot (P26651.1)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1, in vitro.
                     /evidence=ECO:0000269|PubMed:16262601; propagated from
                     UniProtKB/Swiss-Prot (P26651.1)"
     Region          273..292
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26651.1)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16262601; propagated from
                     UniProtKB/Swiss-Prot (P26651.1)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16262601; propagated from
                     UniProtKB/Swiss-Prot (P26651.1)"
     Region          312..326
                     /region_name="Interaction with CNOT1.
                     /evidence=ECO:0000269|PubMed:23644599"
                     /note="propagated from UniProtKB/Swiss-Prot (P26651.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P26651.1)"
     CDS             1..326
                     /gene="ZFP36"
                     /gene_synonym="G0S24; GOS24; NUP475; RNF162A; TIS11; TTP;
                     zfp-36"
                     /coded_by="NM_003407.5:59..1039"
                     /db_xref="CCDS:CCDS12534.3"
                     /db_xref="GeneID:7538"
                     /db_xref="HGNC:HGNC:12862"
                     /db_xref="MIM:190700"
ORIGIN      
        1 mdltaiyesl lslspdvpvp sdhggtessp gwgssgpwsl spsdsspsgv tsrlpgrsts
       61 lvegrscgwv ppppgfapla prlgpelsps ptsptatstt psryktelcr tfsesgrcry
      121 gakcqfahgl gelrqanrhp kyktelchkf ylqgrcpygs rchfihnpse dlaapghppv
      181 lrqsisfsgl psgrrtsppp pglagpslss ssfspssspp ppgdlplsps afsaapgtpl
      241 arrdptpvcc pscrratpis vwgplgglvr tpsvqslgsd pdeyassgss lggsdspvfe
      301 agvfappqpv aaprrlpifn risvse
//
LOCUS       NP_004584                288 aa            linear   PRI 27-NOV-2025
DEFINITION  transformer-2 protein homolog beta isoform 1 [Homo sapiens].
ACCESSION   NP_004584
VERSION     NP_004584.1
DBSOURCE    REFSEQ: accession NM_004593.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Karginov,T.A., Menoret,A., Leclair,N.K., Harrison,A.G.,
            Chandiran,K., Suarez-Ramirez,J.E., Yurieva,M., Karlinsey,K.,
            Wang,P., O'Neill,R.J., Murphy,P.A., Adler,A.J., Cauley,L.S.,
            Anczukow,O., Zhou,B. and Vella,A.T.
  TITLE     Autoregulated splicing of TRA2beta programs T cell fate in response
            to antigen-receptor stimulation
  JOURNAL   Science 385 (6714), eadj1979 (2024)
   PUBMED   39265028
  REMARK    GeneRIF: Autoregulated splicing of TRA2beta programs T cell fate in
            response to antigen-receptor stimulation.
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Chen,G., Chen,J., Qi,L., Yin,Y., Lin,Z., Wen,H., Zhang,S., Xiao,C.,
            Bello,S.F., Zhang,X., Nie,Q. and Luo,W.
  TITLE     Bulk and single-cell alternative splicing analyses reveal roles of
            TRA2B in myogenic differentiation
  JOURNAL   Cell Prolif 57 (2), e13545 (2024)
   PUBMED   37705195
  REMARK    GeneRIF: Bulk and single-cell alternative splicing analyses reveal
            roles of TRA2B in myogenic differentiation.
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Ramond,F., Dalgliesh,C., Grimmel,M., Wechsberg,O., Vetro,A.,
            Guerrini,R., FitzPatrick,D., Poole,R.L., Lebrun,M., Bayat,A.,
            Grasshoff,U., Bertrand,M., Witt,D., Turnpenny,P.D., Faundes,V.,
            Santa Maria,L., Mendoza Fuentes,C., Mabe,P., Hussain,S.A.,
            Mullegama,S.V., Torti,E., Oehl-Jaschkowitz,B., Salmon,L.B.,
            Orenstein,N., Shahar,N.R., Hagari,O., Bazak,L., Hoffjan,S.,
            Prada,C.E., Haack,T. and Elliott,D.J.
  TITLE     Clustered variants in the 5' coding region of TRA2B cause a
            distinctive neurodevelopmental syndrome
  JOURNAL   Genet Med 25 (4), 100003 (2023)
   PUBMED   36549593
  REMARK    GeneRIF: Clustered variants in the 5' coding region of TRA2B cause
            a distinctive neurodevelopmental syndrome.
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Li,M.J., Xiong,D., Wang,S. and Huang,H.
  TITLE     Tra2beta Enhances Cell Proliferation by Inducing the Expression of
            Transcription Factor SP1 in Cervical Cancer
  JOURNAL   Biomed Environ Sci 36 (2), 146-159 (2023)
   PUBMED   36861193
  REMARK    GeneRIF: Tra2beta Enhances Cell Proliferation by Inducing the
            Expression of Transcription Factor SP1 in Cervical Cancer.
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Nayler,O., Cap,C. and Stamm,S.
  TITLE     Human transformer-2-beta gene (SFRS10): complete nucleotide
            sequence, chromosomal localization, and generation of a
            tissue-specific isoform
  JOURNAL   Genomics 53 (2), 191-202 (1998)
   PUBMED   9790768
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Tacke,R., Tohyama,M., Ogawa,S. and Manley,J.L.
  TITLE     Human Tra2 proteins are sequence-specific activators of pre-mRNA
            splicing
  JOURNAL   Cell 93 (1), 139-148 (1998)
   PUBMED   9546399
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Imai,Y., Matsuo,N., Ogawa,S., Tohyama,M. and Takagi,T.
  TITLE     Cloning of a gene, YT521, for a novel RNA splicing-related protein
            induced by hypoxia/reoxygenation
  JOURNAL   Brain Res Mol Brain Res 53 (1-2), 33-40 (1998)
   PUBMED   9473574
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Beil,B., Screaton,G. and Stamm,S.
  TITLE     Molecular cloning of htra2-beta-1 and htra2-beta-2, two human
            homologs of tra-2 generated by alternative splicing
  JOURNAL   DNA Cell Biol 16 (6), 679-690 (1997)
   PUBMED   9212162
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Matsuo,N., Ogawa,S., Imai,Y., Takagi,T., Tohyama,M., Stern,D. and
            Wanaka,A.
  TITLE     Cloning of a novel RNA binding polypeptide (RA301) induced by
            hypoxia/reoxygenation
  JOURNAL   J Biol Chem 270 (47), 28216-28222 (1995)
   PUBMED   7499316
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA164444.1, BC000160.2,
            U61267.1 and AC009247.13.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a nuclear protein which functions as
            sequence-specific serine/arginine splicing factor which plays a
            role in mRNA processing, splicing patterns, and gene expression.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.73674.1,
                                           SRR1803617.17285.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267755, SAMN03267759
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000453386.7/ ENSP00000416959.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.2"
     Protein         1..288
                     /product="transformer-2 protein homolog beta isoform 1"
                     /note="transformer-2 protein homolog beta; TRA-2 beta;
                     transformer-2 protein homolog B; protein phosphatase 1,
                     regulatory subunit 156; splicing factor,
                     arginine/serine-rich 10 (transformer 2 homolog,
                     Drosophila)"
                     /calculated_mol_wt=33535
     Region          1..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62995.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P62995.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P62995.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P62995.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P62995.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62997; propagated from
                     UniProtKB/Swiss-Prot (P62995.1)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P62997; propagated from
                     UniProtKB/Swiss-Prot (P62995.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62995.1)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62995.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62995.1)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P62995.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P62995.1)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P62995.1)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P62995.1)"
     Region          117..196
                     /region_name="RRM_TRA2"
                     /note="RNA recognition motif (RRM) found in transformer-2
                     protein homolog TRA2-alpha, TRA2-beta and similar
                     proteins; cd12363"
                     /db_xref="CDD:409798"
     Site            order(119,123..124,148,150,159,161,163,165,187..190,
                     193..196)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409798"
     Region          193..230
                     /region_name="Linker"
                     /note="propagated from UniProtKB/Swiss-Prot (P62995.1)"
     Region          196..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62995.1)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62995.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P62995.1)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62995.1)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62995.1)"
     Site            241
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; Dimethylated
                     arginine, alternate. /evidence=ECO:0000269|Ref.7,
                     ECO:0007744|PubMed:15782174; Omega-N-methylarginine,
                     alternate. /evidence=ECO:0007744|PubMed:24129315;
                     propagated from UniProtKB/Swiss-Prot (P62995.1)"
     Region          242..288
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62995.1)"
     CDS             1..288
                     /gene="TRA2B"
                     /gene_synonym="Htra2-beta; PPP1R156; RAMELN; SFRS10;
                     SRFS10; TRA2-BETA; TRAN2B"
                     /coded_by="NM_004593.3:155..1021"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33905.1"
                     /db_xref="GeneID:6434"
                     /db_xref="HGNC:HGNC:10781"
                     /db_xref="MIM:602719"
ORIGIN      
        1 msdsgeqnyg eresrsasrs gsahgsgksa rhtparsrsk edsrrsrsks rsrsesrsrs
       61 rrssrrhytr srsrsrshrr srsrsysrdy rrrhshshsp mstrrrhvgn ranpdpnccl
      121 gvfglslytt erdlrevfsk ygpiadvsiv ydqqsrrsrg fafvyfenvd dakeakeran
      181 gmeldgrrir vdfsitkrph tptpgiymgr ptygssrrrd yydrgydrgy ddrdyysrsy
      241 rggggggggw raaqdrdqiy rrrspspyys rggyrsrsrs rsysprry
//
LOCUS       NP_001308642            1310 aa            linear   PRI 27-NOV-2025
DEFINITION  nuclear receptor coactivator 2 isoform c [Homo sapiens].
ACCESSION   NP_001308642 XP_011515742
VERSION     NP_001308642.1
DBSOURCE    REFSEQ: accession NM_001321713.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1310)
  AUTHORS   Yu,X., Wang,X., Ma,K., Gao,D., Deng,Y., Zhou,D., Ding,W., Zhao,Y.,
            Liu,Q. and Zhou,Z.
  TITLE     Tai/NCOA2 suppresses the Hedgehog pathway by directly targeting the
            transcription factor Ci/GLI
  JOURNAL   Proc Natl Acad Sci U S A 121 (47), e2409380121 (2024)
   PUBMED   39531503
REFERENCE   2  (residues 1 to 1310)
  AUTHORS   Warmke,L.M., Mustafa,A., Zou,Y.S., Davis,J.L., Ulbright,T.M. and
            Segura,S.E.
  TITLE     Myxoid epithelioid smooth muscle tumor of the vulva: A distinct
            entity with MEF2D::NCOA2 gene fusion
  JOURNAL   Genes Chromosomes Cancer 63 (1), e23209 (2024)
   PUBMED   37870842
  REMARK    GeneRIF: Myxoid epithelioid smooth muscle tumor of the vulva: A
            distinct entity with MEF2D::NCOA2 gene fusion.
REFERENCE   3  (residues 1 to 1310)
  AUTHORS   Watson,S., LaVigne,C.A., Xu,L., Surdez,D., Cyrta,J., Calderon,D.,
            Cannon,M.V., Kent,M.R., Silvius,K.M., Kucinski,J.P., Harrison,E.N.,
            Murchison,W., Rakheja,D., Tirode,F., Delattre,O., Amatruda,J.F. and
            Kendall,G.C.
  TITLE     VGLL2-NCOA2 leverages developmental programs for pediatric
            sarcomagenesis
  JOURNAL   Cell Rep 42 (1), 112013 (2023)
   PUBMED   36656711
  REMARK    GeneRIF: VGLL2-NCOA2 leverages developmental programs for pediatric
            sarcomagenesis.
REFERENCE   4  (residues 1 to 1310)
  AUTHORS   Wang,L., Motoi,T., Khanin,R., Olshen,A., Mertens,F., Bridge,J., Dal
            Cin,P., Antonescu,C.R., Singer,S., Hameed,M., Bovee,J.V.,
            Hogendoorn,P.C., Socci,N. and Ladanyi,M.
  TITLE     Identification of a novel, recurrent HEY1-NCOA2 fusion in
            mesenchymal chondrosarcoma based on a genome-wide screen of
            exon-level expression data
  JOURNAL   Genes Chromosomes Cancer 51 (2), 127-139 (2012)
   PUBMED   22034177
  REMARK    GeneRIF: The novel HEY1-NCOA2 fusion appears to be the defining and
            diagnostic gene fusion in mesenchymal chondrosarcomas
REFERENCE   5  (residues 1 to 1310)
  AUTHORS   Strehl,S., Nebral,K., Konig,M., Harbott,J., Strobl,H., Ratei,R.,
            Struski,S., Bielorai,B., Lessard,M., Zimmermann,M., Haas,O.A. and
            Izraeli,S.
  TITLE     ETV6-NCOA2: a novel fusion gene in acute leukemia associated with
            coexpression of T-lymphoid and myeloid markers and frequent NOTCH1
            mutations
  JOURNAL   Clin Cancer Res 14 (4), 977-983 (2008)
   PUBMED   18281529
  REMARK    GeneRIF: ETV6-NCOA2 fusion may define a novel subgroup of acute
            leukemia with T-lymphoid and myeloid features, which is associated
            with a high prevalence of NOTCH1 mutations.
REFERENCE   6  (residues 1 to 1310)
  AUTHORS   Fryer,C.J. and Archer,T.K.
  TITLE     Chromatin remodelling by the glucocorticoid receptor requires the
            BRG1 complex
  JOURNAL   Nature 393 (6680), 88-91 (1998)
   PUBMED   9590696
REFERENCE   7  (residues 1 to 1310)
  AUTHORS   Carapeti,M., Aguiar,R.C., Goldman,J.M. and Cross,N.C.
  TITLE     A novel fusion between MOZ and the nuclear receptor coactivator
            TIF2 in acute myeloid leukemia
  JOURNAL   Blood 91 (9), 3127-3133 (1998)
   PUBMED   9558366
REFERENCE   8  (residues 1 to 1310)
  AUTHORS   Voegel,J.J., Heine,M.J., Tini,M., Vivat,V., Chambon,P. and
            Gronemeyer,H.
  TITLE     The coactivator TIF2 contains three nuclear receptor-binding motifs
            and mediates transactivation through CBP binding-dependent and
            -independent pathways
  JOURNAL   EMBO J 17 (2), 507-519 (1998)
   PUBMED   9430642
REFERENCE   9  (residues 1 to 1310)
  AUTHORS   Hong,H., Kohli,K., Garabedian,M.J. and Stallcup,M.R.
  TITLE     GRIP1, a transcriptional coactivator for the AF-2 transactivation
            domain of steroid, thyroid, retinoid, and vitamin D receptors
  JOURNAL   Mol Cell Biol 17 (5), 2735-2744 (1997)
   PUBMED   9111344
REFERENCE   10 (residues 1 to 1310)
  AUTHORS   Voegel,J.J., Heine,M.J., Zechel,C., Chambon,P. and Gronemeyer,H.
  TITLE     TIF2, a 160 kDa transcriptional mediator for the ligand-dependent
            activation function AF-2 of nuclear receptors
  JOURNAL   EMBO J 15 (14), 3667-3675 (1996)
   PUBMED   8670870
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022730.7, CK002637.1,
            X97674.1, AW504723.1, DA691975.1, CN291204.1, CB270668.1,
            CK903771.1 and BC047111.1.
            
            On Mar 30, 2016 this sequence version replaced XP_011515742.1.
            
            Summary: The protein encoded by this gene functions as a
            transcriptional coactivator for nuclear hormone receptors,
            including steroid, thyroid, retinoid, and vitamin D receptors. The
            encoded protein acts as an intermediary factor for the
            ligand-dependent activity of these nuclear receptors, which
            regulate their target genes upon binding of cognate response
            elements. This gene has been found to be involved in translocations
            that result in fusions with other genes in various cancers,
            including the lysine acetyltransferase 6A (KAT6A) gene in acute
            myeloid leukemia, the ETS variant 6 (ETV6) gene in acute
            lymphoblastic leukemia, and the hes related family bHLH
            transcription factor with YRPW motif 1 (HEY1) gene in mesenchymal
            chondrosarcoma. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (6) contains alternate 5' exon
            structure, and it thus differs in the 5' UTR and initiates
            translation from a downstream in-frame start codon, compared to
            variant 1. The encoded isoform (c) is shorter at the N-terminus,
            compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.169402.1,
                                           SRR14038197.1079816.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1310
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.3"
     Protein         1..1310
                     /product="nuclear receptor coactivator 2 isoform c"
                     /note="glucocorticoid receptor-interacting protein-1;
                     transcriptional intermediary factor 2; class E basic
                     helix-loop-helix protein 75; p160 steroid receptor
                     coactivator 2"
                     /calculated_mol_wt=141520
     Region          114..224
                     /region_name="PAS_11"
                     /note="PAS domain; pfam14598"
                     /db_xref="CDD:464214"
     Region          309..433
                     /region_name="NCOA_u2"
                     /note="Unstructured region on nuclear receptor coactivator
                     protein; pfam16665"
                     /db_xref="CDD:465223"
     Region          482..555
                     /region_name="SRC-1"
                     /note="Steroid receptor coactivator; pfam08832"
                     /db_xref="CDD:462615"
     Region          577..662
                     /region_name="DUF4927"
                     /note="Domain of unknown function (DUF4927); pfam16279"
                     /db_xref="CDD:465083"
     Region          917..961
                     /region_name="Nuc_rec_co-act"
                     /note="Nuclear receptor coactivator; pfam08815"
                     /db_xref="CDD:462608"
     Region          1127..1184
                     /region_name="DUF1518"
                     /note="Nuclear receptor coactivator, DUF1518; pfam07469"
                     /db_xref="CDD:462174"
     CDS             1..1310
                     /gene="NCOA2"
                     /gene_synonym="bHLHe75; GRIP1; KAT13C; NCoA-2; SRC-2;
                     SRC2; TIF2"
                     /coded_by="NM_001321713.2:628..4560"
                     /note="isoform c is encoded by transcript variant 6"
                     /db_xref="GeneID:10499"
                     /db_xref="HGNC:HGNC:7669"
                     /db_xref="MIM:601993"
ORIGIN      
        1 mnksvysilh vgdhtefvkn llpksivngg swsgepprrn shtfncrmlv kplpdseeeg
       61 hdnqeahqky etmqcfavsq pksikeeged lqsclicvar rvpmkerpvl pssesfttrq
      121 dlqgkitsld tstmraamkp gwedlvrrci qkfhaqhege svsyakrhhh evlrqglafs
      181 qiyrfslsdg tlvaaqtksk lirsqttnep qlvislhmlh reqnvcvmnp dltgqtmgkp
      241 lnpissnspa hqalcsgnpg qdmtlssnin fpingpkeqm gmpmgrfggs ggmnhvsgmq
      301 attpqgsnya lkmnspsqss pgmnpgqpts mlsprhrmsp gvagspripp sqfspagslh
      361 spvgvcsstg nshsytnssl nalqalsegh gvslgsslas pdlkmgnlqn spvnmnpppl
      421 skmgsldskd cfglygepse gttgqaessc hpgeqketnd pnlppavsse radgqsrlhd
      481 skgqtkllql lttksdqmep splasslsdt nkdstgslpg sgsthgtslk ekhkilhrll
      541 qdssspvdla kltaeatgkd lsqessstap gsevtikqep vspkkkenal lrylldkddt
      601 kdiglpeitp klerldsktd pasntkliam ktekeemsfe pgdqpgseld nleeilddlq
      661 nsqlpqlfpd trpgapagsv dkqaiindlm qltaenspvt pvgaqktalr isqstfnnpr
      721 pgqlgrllpn qnlplditlq sptgagpfpp irnsspysvi pqpgmmgnqg mignqgnlgn
      781 sstgmignsa srptmpsgew apqssavrvt caattsamnr pvqggmirnp aasipmrpss
      841 qpgqrqtlqs qvmnigpsel emnmggpqys qqqappnqta pwpesilpid qasfasqnrq
      901 pfgsspddll cphpaaesps degalldqly lalrnfdgle eidralgipe lvsqsqavdp
      961 eqfssqdsni mleqkapvfp qqyasqaqma qgsyspmqdp nfhtmgqrps yatlrmqprp
     1021 glrptglvqn qpnqlrlqlq hrlqaqqnrq plmnqisnvs nvnltlrpgv ptqapinaqm
     1081 laqrqreiln qhlrqrqmhq qqqvqqrtlm mrgqglnmtp smvapsgmpa tmsnpripqa
     1141 naqqfpfppn ygisqqpdpg ftgattpqsp lmsprmahtq spmmqqsqan payqapsdin
     1201 gwaqgnmggn smfsqqspph fgqqantsmy snnmninvsm atntggmssm nqmtgqismt
     1261 svtsvptsgl ssmgpeqvnd palrggnlfp nqlpgmdmik qegdttrkyc
//
LOCUS       NP_001242982            1709 aa            linear   PRI 27-NOV-2025
DEFINITION  ankyrin repeat domain-containing protein 26 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001242982
VERSION     NP_001242982.1
DBSOURCE    REFSEQ: accession NM_001256053.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1709)
  AUTHORS   Trizuljak,J., Likavcova,P., Stano Kozubik,K., Vrzalova,Z.,
            Hynst,J., Deissova,T., Stika,J., Radova,L., Prudkova,M.,
            Vaculova,J., Blahakova,I., Smejkal,P., Kamelander,J.,
            Pospisilova,S. and Doubek,M.
  TITLE     Impact of thrombocytopenia-associated c.-118C>T and c.-140C>G
            ANKRD26 5'UTR variants in three-generational pedigree
  JOURNAL   Platelets 35 (1), 2388103 (2024)
   PUBMED   39212265
  REMARK    GeneRIF: Impact of thrombocytopenia-associated c.-118C>T and
            c.-140C>G ANKRD26 5'UTR variants in three-generational pedigree.
REFERENCE   2  (residues 1 to 1709)
  AUTHORS   Dunstan-Harrison,C., Morison,I.M. and Ledgerwood,E.C.
  TITLE     Inherited thrombocytopenia associated with a variant in the FLI1
            binding site in the 5' UTR of ANKRD26
  JOURNAL   Clin Genet 106 (3), 315-320 (2024)
   PUBMED   38757516
  REMARK    GeneRIF: Inherited thrombocytopenia associated with a variant in
            the FLI1 binding site in the 5' UTR of ANKRD26.
REFERENCE   3  (residues 1 to 1709)
  AUTHORS   Homan,C.C., Scott,H.S. and Brown,A.L.
  TITLE     Hereditary platelet disorders associated with germ line variants in
            RUNX1, ETV6, and ANKRD26
  JOURNAL   Blood 141 (13), 1533-1543 (2023)
   PUBMED   36626254
  REMARK    GeneRIF: Hereditary platelet disorders associated with germ line
            variants in RUNX1, ETV6, and ANKRD26.
REFERENCE   4  (residues 1 to 1709)
  AUTHORS   Ovsyannikova,G.S., Fedorova,D.V., Tesakov,I.P., Martyanov,A.A.,
            Ignatova,A.A., Ponomarenko,E.A., Zharkov,P.A., Pavlova,A.V.,
            Raykina,E.V., Maschan,M.A., Panteleev,M.A., Novichkova,G.A.,
            Sveshnikova,A.N. and Smetanina,N.S.
  TITLE     Platelet functional abnormalities and clinical presentation in
            pediatric patients with germline RUNX1, ANKRD26, and ETV6 mutations
  JOURNAL   Haematologica 107 (10), 2511-2516 (2022)
   PUBMED   35796010
  REMARK    GeneRIF: Platelet functional abnormalities and clinical
            presentation in pediatric patients with germline RUNX1, ANKRD26,
            and ETV6 mutations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1709)
  AUTHORS   Sullivan,M.J., Palmer,E.L. and Botero,J.P.
  TITLE     ANKRD26-Related Thrombocytopenia and Predisposition to Myeloid
            Neoplasms
  JOURNAL   Curr Hematol Malig Rep 17 (5), 105-112 (2022)
   PUBMED   35751752
  REMARK    GeneRIF: ANKRD26-Related Thrombocytopenia and Predisposition to
            Myeloid Neoplasms.
            Review article
REFERENCE   6  (residues 1 to 1709)
  AUTHORS   Noris,P., Perrotta,S., Seri,M., Pecci,A., Gnan,C., Loffredo,G.,
            Pujol-Moix,N., Zecca,M., Scognamiglio,F., De Rocco,D., Punzo,F.,
            Melazzini,F., Scianguetta,S., Casale,M., Marconi,C., Pippucci,T.,
            Amendola,G., Notarangelo,L.D., Klersy,C., Civaschi,E.,
            Balduini,C.L. and Savoia,A.
  TITLE     Mutations in ANKRD26 are responsible for a frequent form of
            inherited thrombocytopenia: analysis of 78 patients from 21
            families
  JOURNAL   Blood 117 (24), 6673-6680 (2011)
   PUBMED   21467542
  REMARK    GeneRIF: The ANKRD26-related thrombocytopenia has to be taken into
            consideration in the differential diagnosis of isolated
            thrombocytopenias.
REFERENCE   7  (residues 1 to 1709)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   8  (residues 1 to 1709)
  AUTHORS   Pippucci,T., Savoia,A., Perrotta,S., Pujol-Moix,N., Noris,P.,
            Castegnaro,G., Pecci,A., Gnan,C., Punzo,F., Marconi,C.,
            Gherardi,S., Loffredo,G., De Rocco,D., Scianguetta,S., Barozzi,S.,
            Magini,P., Bozzi,V., Dezzani,L., Di Stazio,M., Ferraro,M.,
            Perini,G., Seri,M. and Balduini,C.L.
  TITLE     Mutations in the 5' UTR of ANKRD26, the ankirin repeat domain 26
            gene, cause an autosomal-dominant form of inherited
            thrombocytopenia, THC2
  JOURNAL   Am J Hum Genet 88 (1), 115-120 (2011)
   PUBMED   21211618
  REMARK    GeneRIF: mutations in the 5' UTR of ANKRD26 are implicated in
            thrombocytopenia 2.
REFERENCE   9  (residues 1 to 1709)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   10 (residues 1 to 1709)
  AUTHORS   Perez Botero,J., Dugan,S.N. and Anderson,M.W.
  TITLE     ANKRD26-Related Thrombocytopenia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29927566
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162272.10 and AB028997.1.
            
            Summary: This gene encodes a protein containing N-terminal ankyrin
            repeats which function in protein-protein interactions. Mutations
            in this gene are associated with autosomal dominant
            thrombocytopenia-2. Pseudogenes of this gene are found on
            chromosome 7, 10, 13 and 16. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Dec 2011].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region compared to variant 1. The
            resulting protein (isoform 2) is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB028997.1, SRR1660807.16309.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1709
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.1"
     Protein         1..1709
                     /product="ankyrin repeat domain-containing protein 26
                     isoform 2"
                     /note="ankyrin repeat domain-containing protein 26;
                     GNS/ANKRD26/NCKAP1L fusion; ankyrin repeat domain
                     containing 26"
                     /calculated_mol_wt=196193
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          44..>210
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          45..75
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Site            order(79,81,85..86,89..91,93..94,98,101,110,112,114,
                     118..119,122..124,126..127,131,134,143,145,147,151..152,
                     155..157,159..160,164,167,176)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          79..110
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          79..108
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          112..143
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          112..141
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          145..176
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          145..174
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          178..209
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          178..207
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          222..274
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q811D2; propagated from
                     UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Site            630
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          649..697
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          <746..1413
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          891..911
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPS8.4)"
     Region          913..1216
                     /region_name="CCDC144C"
                     /note="CCDC144C protein coiled-coil region; pfam14915"
                     /db_xref="CDD:464371"
     Region          1393..>1566
                     /region_name="DR0291"
                     /note="Predicted nucleic acid-binding protein DR0291,
                     contains C4-type Zn-ribbon domain [General function
                     prediction only]; COG1579"
                     /db_xref="CDD:441187"
     Region          1522..1630
                     /region_name="DUF3496"
                     /note="Domain of unknown function (DUF3496); pfam12001"
                     /db_xref="CDD:463425"
     CDS             1..1709
                     /gene="ANKRD26"
                     /gene_synonym="bA145E8.1; THC2"
                     /coded_by="NM_001256053.2:169..5298"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS91225.1"
                     /db_xref="GeneID:22852"
                     /db_xref="HGNC:HGNC:29186"
                     /db_xref="MIM:610855"
ORIGIN      
        1 mkkifskkge splgsfarrq rssaggggep gegaysqpgy hvrdrdlgki hkaasagnva
       61 kvqqilllrk nglndrdkmn rtalhlacan ghpevvtllv drkcqlnvcd nenrtalmka
      121 vqcqeekcat illehgadpn ladvhgntal hyavynedis vatklllyda nieaknkddl
      181 tplllavsgk kqqmveflik kkanvnavdk lesshqlise ykeeripkhs sqnsnsvdes
      241 sedslsrlsg kpgvddswpt sddedlnfdt knvpkpslak lmtasqqsrk nleatygtvr
      301 tgnrtlfedr dsdsqdevvv eslpttsikv qcfshptyqs pdllpkpshk slanpglmke
      361 eptkpgiakk engidiiesa pleqtnndnl tyvdevhknn rsdmmsalgl gqeediespw
      421 dsesisenfp qkyvdplaga adgkeknign eqaedvfyip scmsgsrnfk makledtrnv
      481 gmpvahmesp erylhlkpti emkdsvpnka ggmkdvqtsk aaehdlevas eeeqeregse
      541 nnqpqveeer kkhrnnemev sanihdgatd daeddddddg liqkrksget dhqqfprken
      601 keyasgpalq mkevksteke krtskesvns pvfgkasllt ggllqvddds slseidedeg
      661 rptkktsnek nkvknqiqsm ddvddltqss etasedcelp hssyknfmll ieqlgmeckd
      721 svsllkiqda alscerllel kknhcelltv kikkmedkvn vlqrelsetk eiksqlehqk
      781 vewerelcsl rfslnqeeek rrnadtlyek ireqlrrkee qyrkevevkq qlelslqtle
      841 melrtvksnl nqvvqernda qrqlsreqna rmlqdgiltn hlskqkeiem aqkkmnsens
      901 hsheeekdls hknsmlqeei amlrleidti knqnqekekk cfedlkivke knedlqktik
      961 qneetltqti sqyngrlsvl taenamlnsk lenekqsker leaevesyhs rlaaaihdrd
     1021 qsetskrele lafqrardec srlqdkmnfd vsnlkdnnei lsqqlfktes klnsleiefh
     1081 htrdalrekt lglervqkdl sqtqcqmkem eqkyqneqvk vnkyigkqes veerlsqlqs
     1141 enmllrqqld dahnkadnke ktviniqdqf haivqklqae sekqslllee rnkelisecn
     1201 hlkerqyqye nekaerevvv rqlqqeladt lkkqsmseas levtsryrin ledetqdlkk
     1261 klgqirnqlq eaqdrhteav rcaekmqdhk qklekdnakl kvtvkkqmdk ieelqknlln
     1321 anlsedekeq lkklmelkqs lecnldqemk knvelereit gfknllkmtr kklneyenge
     1381 fsfhgdlkts qfemdiqink lkhkiddlta eletagskcl hldtknqilq eellsmktvq
     1441 kkceklqknk kkleqevinl rshiernmve lgqvkqykqe ieerarqeia eklkevnlfl
     1501 qaqaasqenl eqfrennfas mksqmelrik dleselskik tsqedfnkte lekykqlyle
     1561 elkvrkslss kltktnerla evntkllvek qqsrslfttl ttrpvmeppc vgnlnnsldl
     1621 nrkliprenl vistsnpras nnsmenylsk mqqeleknit relkeaaael esgsiasplg
     1681 stdesnlnqd lvwkasreyv qvlkknymi
//
LOCUS       NP_008818                494 aa            linear   PRI 27-NOV-2025
DEFINITION  mRNA decay activator protein ZFP36L2 [Homo sapiens].
ACCESSION   NP_008818
VERSION     NP_008818.3
DBSOURCE    REFSEQ: accession NM_006887.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Saenz-Narciso,B., Bell,S.E., Matheson,L.S., Venigalla,R.K.C. and
            Turner,M.
  TITLE     ZFP36-family RNA-binding proteins in regulatory T cells reinforce
            immune homeostasis
  JOURNAL   Nat Commun 16 (1), 4192 (2025)
   PUBMED   40328742
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Lin,R.J., Lin,L.H., Chen,Z.P., Liu,B.C., Ko,P.C. and Liao,C.L.
  TITLE     The zinc finger protein ZFP36L2 inhibits flavivirus infection via
            the 5'-3' XRN1-mediated RNA decay pathway in the replication
            complexes
  JOURNAL   J Biomed Sci 32 (1), 27 (2025)
   PUBMED   39972499
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Rui,X., Zhang,X., Jia,X., Han,J., Wang,C., Cao,Q., Zhong,O.,
            Ding,J., Zhao,C., Zhang,J., Ling,X., Li,H., Ma,X., Meng,Q. and
            Huo,R.
  TITLE     Variants in NLRP2 and ZFP36L2, non-core components of the human
            subcortical maternal complex, cause female infertility with
            embryonic development arrest
  JOURNAL   Mol Hum Reprod 30 (9) (2024)
   PUBMED   39178021
  REMARK    GeneRIF: Variants in NLRP2 and ZFP36L2, non-core components of the
            human subcortical maternal complex, cause female infertility with
            embryonic development arrest.
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Sun,J., Li,M., Sun,H., Lin,Z., Shi,B. and Jia,Z.
  TITLE     Genetic association and functional validation of ZFP36L2 in
            non-syndromic orofacial cleft subtypes
  JOURNAL   J Hum Genet 69 (3-4), 139-144 (2024)
   PUBMED   38321215
  REMARK    GeneRIF: Genetic association and functional validation of ZFP36L2
            in non-syndromic orofacial cleft subtypes.
            Erratum:[J Hum Genet. 2024 Apr;69(3-4):169. doi:
            10.1038/s10038-024-01239-4. PMID: 38443624]
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Balducci,E., Steimle,T., Smith,C., Villarese,P., Feroul,M.,
            Payet-Bornet,D., Kaltenbach,S., Couronne,L., Lhermitte,L.,
            Touzart,A., Dourthe,M.E., Simonin,M., Baruchel,A., Dombret,H.,
            Ifrah,N., Boissel,N., Nadel,B., Macintyre,E., Cieslak,A. and
            Asnafi,V.
  TITLE     TREC mediated oncogenesis in human immature T lymphoid malignancies
            preferentially involves ZFP36L2
  JOURNAL   Mol Cancer 22 (1), 108 (2023)
   PUBMED   37430263
  REMARK    GeneRIF: TREC mediated oncogenesis in human immature T lymphoid
            malignancies preferentially involves ZFP36L2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Jackson,R.S. 2nd, Cho,Y.J. and Liang,P.
  TITLE     TIS11D is a candidate pro-apoptotic p53 target gene
  JOURNAL   Cell Cycle 5 (24), 2889-2893 (2006)
   PUBMED   17172869
  REMARK    GeneRIF: These data suggest TIS11D as a candidate p53 target gene
            that may be part of the network of genes responsible for
            p53-dependent apoptosis.
REFERENCE   7  (residues 1 to 494)
  AUTHORS   Hudson,B.P., Martinez-Yamout,M.A., Dyson,H.J. and Wright,P.E.
  TITLE     Recognition of the mRNA AU-rich element by the zinc finger domain
            of TIS11d
  JOURNAL   Nat Struct Mol Biol 11 (3), 257-264 (2004)
   PUBMED   14981510
  REMARK    GeneRIF: Sequence specificity in RNA recognition is achieved by a
            network of intermolecular hydrogen bonds, mostly between TIS11d
            main-chain functional groups and the Watson-Crick edges of the
            bases
REFERENCE   8  (residues 1 to 494)
  AUTHORS   Blackshear,P.J., Phillips,R.S., Vazquez-Matias,J. and
            Mohrenweiser,H.
  TITLE     Polymorphisms in the genes encoding members of the tristetraprolin
            family of human tandem CCCH zinc finger proteins
  JOURNAL   Prog Nucleic Acid Res Mol Biol 75, 43-68 (2003)
   PUBMED   14604009
  REMARK    GeneRIF: polymorphisms sequenced in genomic DNA encoding the TTP
            protein (ZFP36) and those of its two known mammalian relatives,
            ZFP36L1 and ZFP36L2, from 72 to 92 anonymous human subjects from
            various geographical and ethnic backgrounds
REFERENCE   9  (residues 1 to 494)
  AUTHORS   Ino,T., Yasui,H., Hirano,M. and Kurosawa,Y.
  TITLE     Identification of a member of the TIS11 early response gene family
            at the insertion point of a DNA fragment containing a gene for the
            T-cell receptor beta chain in an acute T-cell leukemia
  JOURNAL   Oncogene 11 (12), 2705-2710 (1995)
   PUBMED   8545129
REFERENCE   10 (residues 1 to 494)
  AUTHORS   Nie,X.F., Maclean,K.N., Kumar,V., McKay,I.A. and Bustin,S.A.
  TITLE     ERF-2, the human homologue of the murine Tis11d early response gene
  JOURNAL   Gene 152 (2), 285-286 (1995)
   PUBMED   7835719
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010883.8 and N67537.1.
            
            On Oct 1, 2001 this sequence version replaced NP_008818.2.
            
            Summary: This gene is a member of the TIS11 family of early
            response genes. Family members are induced by various agonists such
            as the phorbol ester TPA and the polypeptide mitogen EGF. The
            encoded protein contains a distinguishing putative zinc finger
            domain with a repeating cys-his motif. This putative nuclear
            transcription factor most likely functions in regulating the
            response to growth factors. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HY062296.1, SRR3476690.434295.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000282388.4/ ENSP00000282388.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p21"
     Protein         1..494
                     /product="mRNA decay activator protein ZFP36L2"
                     /note="zinc finger protein 36, C3H type-like 1;
                     EGF-response factor 2; ZFP36 ring finger protein like 2;
                     zinc finger protein, C3H type, 36-like 2; zinc finger
                     protein 36, C3H1 type-like 2; ZFP36-like 2; zinc finger
                     protein 36, C3H type-like 2; TPA-induced sequence 11d;
                     butyrate response factor 2 (EGF-response factor 2)"
                     /calculated_mol_wt=50932
     Region          1..131
                     /region_name="Tis11B_N"
                     /note="Tis11B like protein, N terminus; pfam04553"
                     /db_xref="CDD:461350"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P47974.3)"
     Region          93..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P47974.3)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P47974.3)"
     Region          153..158
                     /region_name="RNA-binding.
                     /evidence=ECO:0000269|PubMed:14981510,
                     ECO:0000269|PubMed:20506496"
                     /note="propagated from UniProtKB/Swiss-Prot (P47974.3)"
     Region          <154..>216
                     /region_name="CTH1"
                     /note="CCCH-type Zn-finger protein [General function
                     prediction only]; COG5063"
                     /db_xref="CDD:227395"
     Region          170..211
                     /region_name="RNA-binding.
                     /evidence=ECO:0000269|PubMed:14981510,
                     ECO:0000269|PubMed:20506496"
                     /note="propagated from UniProtKB/Swiss-Prot (P47974.3)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P47974.3)"
     Region          257..293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P47974.3)"
     Region          397..494
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P47974.3)"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA1.
                     /evidence=ECO:0000269|PubMed:25106868; propagated from
                     UniProtKB/Swiss-Prot (P47974.3)"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA1.
                     /evidence=ECO:0000269|PubMed:25106868; propagated from
                     UniProtKB/Swiss-Prot (P47974.3)"
     CDS             1..494
                     /gene="ZFP36L2"
                     /gene_synonym="BRF2; ERF-2; ERF2; OOMD13; OZEMA13;
                     RNF162C; TIS11D"
                     /coded_by="NM_006887.5:292..1776"
                     /db_xref="CCDS:CCDS1811.1"
                     /db_xref="GeneID:678"
                     /db_xref="HGNC:HGNC:1108"
                     /db_xref="MIM:612053"
ORIGIN      
        1 msttllsafy dvdflcktek slanlnlnnm ldkkavgtpv aaapssgfap gflrrhsasn
       61 lhalahpaps pgscspkfpg aangsscgsa aaggptsygt lkepsggggt allnkenkfr
      121 drsfsengdr sqhllhlqqq qkggggsqin stryktelcr pfeesgtcky gekcqfahgf
      181 helrsltrhp kyktelcrtf htigfcpygp rchfihnade rrpapsggas gdlrafgtrd
      241 alhlgfprep rpklhhslsf sgfpsghhqp pgglesplll dsptsrtppp pscssasscs
      301 ssasscssas aastpsgapt ccasaaaaaa aallygtgga edllapgapc aacssascan
      361 nafafgpels slitplaiqt hnfaavaaaa yyrsqqqqqq qglappaqpp appsatlpag
      421 aaappsppfs fqlprrlsds pvfdappspp dslsdrdsyl sgslssgsls gsespsldpg
      481 rrlpifsrls isdd
//
LOCUS       NP_006531               1464 aa            linear   PRI 27-NOV-2025
DEFINITION  nuclear receptor coactivator 2 isoform a [Homo sapiens].
ACCESSION   NP_006531
VERSION     NP_006531.1
DBSOURCE    REFSEQ: accession NM_006540.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1464)
  AUTHORS   Yu,X., Wang,X., Ma,K., Gao,D., Deng,Y., Zhou,D., Ding,W., Zhao,Y.,
            Liu,Q. and Zhou,Z.
  TITLE     Tai/NCOA2 suppresses the Hedgehog pathway by directly targeting the
            transcription factor Ci/GLI
  JOURNAL   Proc Natl Acad Sci U S A 121 (47), e2409380121 (2024)
   PUBMED   39531503
REFERENCE   2  (residues 1 to 1464)
  AUTHORS   Warmke,L.M., Mustafa,A., Zou,Y.S., Davis,J.L., Ulbright,T.M. and
            Segura,S.E.
  TITLE     Myxoid epithelioid smooth muscle tumor of the vulva: A distinct
            entity with MEF2D::NCOA2 gene fusion
  JOURNAL   Genes Chromosomes Cancer 63 (1), e23209 (2024)
   PUBMED   37870842
  REMARK    GeneRIF: Myxoid epithelioid smooth muscle tumor of the vulva: A
            distinct entity with MEF2D::NCOA2 gene fusion.
REFERENCE   3  (residues 1 to 1464)
  AUTHORS   Watson,S., LaVigne,C.A., Xu,L., Surdez,D., Cyrta,J., Calderon,D.,
            Cannon,M.V., Kent,M.R., Silvius,K.M., Kucinski,J.P., Harrison,E.N.,
            Murchison,W., Rakheja,D., Tirode,F., Delattre,O., Amatruda,J.F. and
            Kendall,G.C.
  TITLE     VGLL2-NCOA2 leverages developmental programs for pediatric
            sarcomagenesis
  JOURNAL   Cell Rep 42 (1), 112013 (2023)
   PUBMED   36656711
  REMARK    GeneRIF: VGLL2-NCOA2 leverages developmental programs for pediatric
            sarcomagenesis.
REFERENCE   4  (residues 1 to 1464)
  AUTHORS   Wang,L., Motoi,T., Khanin,R., Olshen,A., Mertens,F., Bridge,J., Dal
            Cin,P., Antonescu,C.R., Singer,S., Hameed,M., Bovee,J.V.,
            Hogendoorn,P.C., Socci,N. and Ladanyi,M.
  TITLE     Identification of a novel, recurrent HEY1-NCOA2 fusion in
            mesenchymal chondrosarcoma based on a genome-wide screen of
            exon-level expression data
  JOURNAL   Genes Chromosomes Cancer 51 (2), 127-139 (2012)
   PUBMED   22034177
  REMARK    GeneRIF: The novel HEY1-NCOA2 fusion appears to be the defining and
            diagnostic gene fusion in mesenchymal chondrosarcomas
REFERENCE   5  (residues 1 to 1464)
  AUTHORS   Strehl,S., Nebral,K., Konig,M., Harbott,J., Strobl,H., Ratei,R.,
            Struski,S., Bielorai,B., Lessard,M., Zimmermann,M., Haas,O.A. and
            Izraeli,S.
  TITLE     ETV6-NCOA2: a novel fusion gene in acute leukemia associated with
            coexpression of T-lymphoid and myeloid markers and frequent NOTCH1
            mutations
  JOURNAL   Clin Cancer Res 14 (4), 977-983 (2008)
   PUBMED   18281529
  REMARK    GeneRIF: ETV6-NCOA2 fusion may define a novel subgroup of acute
            leukemia with T-lymphoid and myeloid features, which is associated
            with a high prevalence of NOTCH1 mutations.
REFERENCE   6  (residues 1 to 1464)
  AUTHORS   Fryer,C.J. and Archer,T.K.
  TITLE     Chromatin remodelling by the glucocorticoid receptor requires the
            BRG1 complex
  JOURNAL   Nature 393 (6680), 88-91 (1998)
   PUBMED   9590696
REFERENCE   7  (residues 1 to 1464)
  AUTHORS   Carapeti,M., Aguiar,R.C., Goldman,J.M. and Cross,N.C.
  TITLE     A novel fusion between MOZ and the nuclear receptor coactivator
            TIF2 in acute myeloid leukemia
  JOURNAL   Blood 91 (9), 3127-3133 (1998)
   PUBMED   9558366
REFERENCE   8  (residues 1 to 1464)
  AUTHORS   Voegel,J.J., Heine,M.J., Tini,M., Vivat,V., Chambon,P. and
            Gronemeyer,H.
  TITLE     The coactivator TIF2 contains three nuclear receptor-binding motifs
            and mediates transactivation through CBP binding-dependent and
            -independent pathways
  JOURNAL   EMBO J 17 (2), 507-519 (1998)
   PUBMED   9430642
REFERENCE   9  (residues 1 to 1464)
  AUTHORS   Hong,H., Kohli,K., Garabedian,M.J. and Stallcup,M.R.
  TITLE     GRIP1, a transcriptional coactivator for the AF-2 transactivation
            domain of steroid, thyroid, retinoid, and vitamin D receptors
  JOURNAL   Mol Cell Biol 17 (5), 2735-2744 (1997)
   PUBMED   9111344
REFERENCE   10 (residues 1 to 1464)
  AUTHORS   Voegel,J.J., Heine,M.J., Zechel,C., Chambon,P. and Gronemeyer,H.
  TITLE     TIF2, a 160 kDa transcriptional mediator for the ligand-dependent
            activation function AF-2 of nuclear receptors
  JOURNAL   EMBO J 15 (14), 3667-3675 (1996)
   PUBMED   8670870
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL712418.1, X97674.1,
            AW504723.1, DA691975.1, CN291204.1, CB270668.1, CK903771.1 and
            BC047111.1.
            
            Summary: The protein encoded by this gene functions as a
            transcriptional coactivator for nuclear hormone receptors,
            including steroid, thyroid, retinoid, and vitamin D receptors. The
            encoded protein acts as an intermediary factor for the
            ligand-dependent activity of these nuclear receptors, which
            regulate their target genes upon binding of cognate response
            elements. This gene has been found to be involved in translocations
            that result in fusions with other genes in various cancers,
            including the lysine acetyltransferase 6A (KAT6A) gene in acute
            myeloid leukemia, the ETS variant 6 (ETV6) gene in acute
            lymphoblastic leukemia, and the hes related family bHLH
            transcription factor with YRPW motif 1 (HEY1) gene in mesenchymal
            chondrosarcoma. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 all encode isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X97674.1, SRR11853566.26632.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000452400.7/ ENSP00000399968.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.3"
     Protein         1..1464
                     /product="nuclear receptor coactivator 2 isoform a"
                     /note="glucocorticoid receptor-interacting protein-1;
                     transcriptional intermediary factor 2; class E basic
                     helix-loop-helix protein 75; p160 steroid receptor
                     coactivator 2"
                     /calculated_mol_wt=159026
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          28..91
                     /region_name="bHLH-PAS_NCoA2_SRC2"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in nuclear receptor coactivator 2 (NCoA-2)
                     and similar proteins; cd18950"
                     /db_xref="CDD:381520"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            order(30..32,36,38..39,43,68..69)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381520"
     Site            order(41..42,45..46,48..49,70,73,77,79..80,84,86)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381520"
     Region          118..175
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Site            order(139,143,149,162..165,195)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(159,163,172,175..176,202,204)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          268..378
                     /region_name="PAS_11"
                     /note="PAS domain; pfam14598"
                     /db_xref="CDD:464214"
     Site            338
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q61026; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          463..587
                     /region_name="NCOA_u2"
                     /note="Unstructured region on nuclear receptor coactivator
                     protein; pfam16665"
                     /db_xref="CDD:465223"
     Region          468..513
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          557..683
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          636..709
                     /region_name="SRC-1"
                     /note="Steroid receptor coactivator; pfam08832"
                     /db_xref="CDD:462615"
     Site            636
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q61026; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            640
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          641..645
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            682
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          690..694
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          691..743
                     /region_name="CASP8AP2-binding.
                     /evidence=ECO:0000250|UniProtKB:Q61026"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            699
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          709..737
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          730..1121
                     /region_name="Interaction with BMAL1.
                     /evidence=ECO:0000250|UniProtKB:Q61026"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          731..816
                     /region_name="DUF4927"
                     /note="Domain of unknown function (DUF4927); pfam16279"
                     /db_xref="CDD:465083"
     Site            736
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          745..749
                     /region_name="LXXLL motif 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            771
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            780
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            785
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            864
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q61026; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            869..870
                     /site_type="other"
                     /note="Breakpoint for translocation to form KAT6A-NCOA2.
                     /evidence=ECO:0000269|PubMed:12676584,
                     ECO:0000269|PubMed:15657427, ECO:0000269|PubMed:9558366;
                     propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            874
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q61026; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          878..882
                     /region_name="LXXLL motif 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          973..1003
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          1017..1038
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          1051..1074
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          1071..1115
                     /region_name="Nuc_rec_co-act"
                     /note="Nuclear receptor coactivator; pfam08815"
                     /db_xref="CDD:462608"
     Region          1079..1087
                     /region_name="LLXXLXXXL motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1173
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1177
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1190
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1196
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1203
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1221
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1240
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q61026; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1261
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1266
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          1281..1338
                     /region_name="DUF1518"
                     /note="Nuclear receptor coactivator, DUF1518; pfam07469"
                     /db_xref="CDD:462174"
     Region          1441..1464
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     CDS             1..1464
                     /gene="NCOA2"
                     /gene_synonym="bHLHe75; GRIP1; KAT13C; NCoA-2; SRC-2;
                     SRC2; TIF2"
                     /coded_by="NM_006540.4:186..4580"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47872.1"
                     /db_xref="GeneID:10499"
                     /db_xref="HGNC:HGNC:7669"
                     /db_xref="MIM:601993"
ORIGIN      
        1 msgmgentsd psraetrkrk ecpdqlgpsp krntekrnre qenkyieela elifanfndi
       61 dnfnfkpdkc ailketvkqi rqikeqekaa aanidevqks dvsstgqgvi dkdalgpmml
      121 ealdgfffvv nlegnvvfvs envtqylryn qeelmnksvy silhvgdhte fvknllpksi
      181 vnggswsgep prrnshtfnc rmlvkplpds eeeghdnqea hqkyetmqcf avsqpksike
      241 egedlqscli cvarrvpmke rpvlpssesf ttrqdlqgki tsldtstmra amkpgwedlv
      301 rrciqkfhaq hegesvsyak rhhhevlrqg lafsqiyrfs lsdgtlvaaq tksklirsqt
      361 tnepqlvisl hmlhreqnvc vmnpdltgqt mgkplnpiss nspahqalcs gnpgqdmtls
      421 sninfpingp keqmgmpmgr fggsggmnhv sgmqattpqg snyalkmnsp sqsspgmnpg
      481 qptsmlsprh rmspgvagsp rippsqfspa gslhspvgvc sstgnshsyt nsslnalqal
      541 seghgvslgs slaspdlkmg nlqnspvnmn ppplskmgsl dskdcfglyg epsegttgqa
      601 esschpgeqk etndpnlppa vsseradgqs rlhdskgqtk llqllttksd qmepsplass
      661 lsdtnkdstg slpgsgsthg tslkekhkil hrllqdsssp vdlakltaea tgkdlsqess
      721 stapgsevti kqepvspkkk enallrylld kddtkdiglp eitpklerld sktdpasntk
      781 liamktekee msfepgdqpg seldnleeil ddlqnsqlpq lfpdtrpgap agsvdkqaii
      841 ndlmqltaen spvtpvgaqk talrisqstf nnprpgqlgr llpnqnlpld itlqsptgag
      901 pfppirnssp ysvipqpgmm gnqgmignqg nlgnsstgmi gnsasrptmp sgewapqssa
      961 vrvtcaatts amnrpvqggm irnpaasipm rpssqpgqrq tlqsqvmnig pselemnmgg
     1021 pqysqqqapp nqtapwpesi lpidqasfas qnrqpfgssp ddllcphpaa espsdegall
     1081 dqlylalrnf dgleeidral gipelvsqsq avdpeqfssq dsnimleqka pvfpqqyasq
     1141 aqmaqgsysp mqdpnfhtmg qrpsyatlrm qprpglrptg lvqnqpnqlr lqlqhrlqaq
     1201 qnrqplmnqi snvsnvnltl rpgvptqapi naqmlaqrqr eilnqhlrqr qmhqqqqvqq
     1261 rtlmmrgqgl nmtpsmvaps gmpatmsnpr ipqanaqqfp fppnygisqq pdpgftgatt
     1321 pqsplmsprm ahtqspmmqq sqanpayqap sdingwaqgn mggnsmfsqq spphfgqqan
     1381 tsmysnnmni nvsmatntgg mssmnqmtgq ismtsvtsvp tsglssmgpe qvndpalrgg
     1441 nlfpnqlpgm dmikqegdtt rkyc
//
LOCUS       NP_001231630             407 aa            linear   PRI 27-NOV-2025
DEFINITION  mRNA decay activator protein ZFP36L1 isoform 2 [Homo sapiens].
ACCESSION   NP_001231630
VERSION     NP_001231630.1
DBSOURCE    REFSEQ: accession NM_001244701.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Saenz-Narciso,B., Bell,S.E., Matheson,L.S., Venigalla,R.K.C. and
            Turner,M.
  TITLE     ZFP36-family RNA-binding proteins in regulatory T cells reinforce
            immune homeostasis
  JOURNAL   Nat Commun 16 (1), 4192 (2025)
   PUBMED   40328742
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Lu,F., Yao,L.P., Gao,D.D., Alinejad,T., Jiang,X.Q., Wu,Q.,
            Zhai,Q.C., Liu,M., Zhu,S.M., Qian,M.X., Xu,L.F., Chen,C.S. and
            Zhang,F.
  TITLE     MicroRNA-377-3p exacerbates chronic obstructive pulmonary disease
            through suppressing ZFP36L1 expression and inducing lung fibroblast
            senescence
  JOURNAL   Respir Res 25 (1), 67 (2024)
   PUBMED   38317146
  REMARK    GeneRIF: MicroRNA-377-3p exacerbates chronic obstructive pulmonary
            disease through suppressing ZFP36L1 expression and inducing lung
            fibroblast senescence.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Momin,T., Villasenor,A., Singh,A., Darweesh,M., Singh,A. and
            Rajput,M.
  TITLE     ZFP36 ring finger protein like 1 significantly suppresses human
            coronavirus OC43 replication
  JOURNAL   PeerJ 11, e14776 (2023)
   PUBMED   36846448
  REMARK    GeneRIF: ZFP36 ring finger protein like 1 significantly suppresses
            human coronavirus OC43 replication.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Chen,H.Y., Durmaz,Y.T., Li,Y., Sabet,A.H., Vajdi,A., Denize,T.,
            Walton,E., Laimon,Y.N., Doench,J.G., Mahadevan,N.R., Losman,J.A.,
            Barbie,D.A., Tolstorukov,M.Y., Rudin,C.M., Sen,T., Signoretti,S.
            and Oser,M.G.
  TITLE     Regulation of neuroendocrine plasticity by the RNA-binding protein
            ZFP36L1
  JOURNAL   Nat Commun 13 (1), 4998 (2022)
   PUBMED   36008402
  REMARK    GeneRIF: Regulation of neuroendocrine plasticity by the RNA-binding
            protein ZFP36L1.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Stoecklin,G., Colombi,M., Raineri,I., Leuenberger,S., Mallaun,M.,
            Schmidlin,M., Gross,B., Lu,M., Kitamura,T. and Moroni,C.
  TITLE     Functional cloning of BRF1, a regulator of ARE-dependent mRNA
            turnover
  JOURNAL   EMBO J 21 (17), 4709-4718 (2002)
   PUBMED   12198173
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Ning,Z.Q., Norton,J.D., Li,J. and Murphy,J.J.
  TITLE     Distinct mechanisms for rescue from apoptosis in Ramos human B
            cells by signaling through CD40 and interleukin-4 receptor: role
            for inhibition of an early response gene, Berg36
  JOURNAL   Eur J Immunol 26 (10), 2356-2363 (1996)
   PUBMED   8898945
REFERENCE   8  (residues 1 to 407)
  AUTHORS   Maclean,K.N., See,C.G., McKay,I.A. and Bustin,S.A.
  TITLE     The human immediate early gene BRF1 maps to chromosome 14q22-q24
  JOURNAL   Genomics 30 (1), 89-90 (1995)
   PUBMED   8595910
REFERENCE   9  (residues 1 to 407)
  AUTHORS   Bustin,S.A., Nie,X.F., Barnard,R.C., Kumar,V., Pascall,J.C.,
            Brown,K.D., Leigh,I.M., Williams,N.S. and McKay,I.A.
  TITLE     Cloning and characterization of ERF-1, a human member of the Tis11
            family of early-response genes
  JOURNAL   DNA Cell Biol 13 (5), 449-459 (1994)
   PUBMED   8024689
REFERENCE   10 (residues 1 to 407)
  AUTHORS   Barnard,R.C., Pascall,J.C., Brown,K.D., McKay,I.A., Williams,N.S.
            and Bustin,S.A.
  TITLE     Coding sequence of ERF-1, the human homologue of Tis11b/cMG1,
            members of the Tis11 family of early response genes
  JOURNAL   Nucleic Acids Res 21 (15), 3580 (1993)
   PUBMED   8346037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA633985.1, FY210721.1,
            BP353132.1, BC018340.1, BM712842.1, BQ894292.1, DR423896.1 and
            BQ004874.1.
            
            Summary: This gene is a member of the TIS11 family of early
            response genes, which are induced by various agonists such as the
            phorbol ester TPA and the polypeptide mitogen EGF. This gene is
            well conserved across species and has a promoter that contains
            motifs seen in other early-response genes. The encoded protein
            contains a distinguishing putative zinc finger domain with a
            repeating cys-his motif. This putative nuclear transcription factor
            most likely functions in regulating the response to growth factors.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2011].
            
            Transcript Variant: This variant (3) contains an additional exon at
            the 5' end compared to variant 1, that introduces an in-frame
            upstream AUG, translation from which results in an isoform (2) with
            a longer N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FY210721.1, FY212038.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145774 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.1"
     Protein         1..407
                     /product="mRNA decay activator protein ZFP36L1 isoform 2"
                     /note="EGF-response factor 1; early response factor
                     Berg36; zinc finger protein, C3H type, 36-like 1; butyrate
                     response factor 1; zinc finger protein 36, C3H1 type-like
                     1; zinc finger protein 36, C3H type-like 1; ZFP36-like 1;
                     TPA-induced sequence 11b; mRNA decay activator protein
                     ZFP36L1; ZFP36 ring finger protein like 1"
                     /calculated_mol_wt=43715
     Region          70..175
                     /region_name="Tis11B_N"
                     /note="Tis11B like protein, N terminus; pfam04553"
                     /db_xref="CDD:461350"
     Region          <184..>246
                     /region_name="CTH1"
                     /note="CCCH-type Zn-finger protein [General function
                     prediction only]; COG5063"
                     /db_xref="CDD:227395"
     CDS             1..407
                     /gene="ZFP36L1"
                     /gene_synonym="Berg36; BRF1; cMG1; ERF-1; ERF1; RNF162B;
                     TIS11B"
                     /coded_by="NM_001244701.1:95..1318"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:677"
                     /db_xref="HGNC:HGNC:1107"
                     /db_xref="MIM:601064"
ORIGIN      
        1 mgrarksglg qrsrptasrs eaavqpgvrk argagnwrvg lqtgeaapsp hrdlrdtpdp
       61 rpwlarthrm tttlvsatif dlsevlckgn kmlnysapsa ggclldrkav gtpagggfpr
      121 rhsvtlpssk fhqnqllssl kgepapalss rdsrfrdrsf seggerllpt qkqpgggqvn
      181 ssryktelcr pfeengacky gdkcqfahgi helrsltrhp kyktelcrtf htigfcpygp
      241 rchfihnaee rralagardl sadrprlqhs fsfagfpsaa ataaatglld sptsitpppi
      301 lsaddllgsp tlpdgtnnpf afssqelasl fapsmglpgg gspttflfrp msesphmfds
      361 ppspqdslsd qegylsssss shsgsdsptl dnsrrlpifs rlsisdd
//
LOCUS       NP_001308632            1464 aa            linear   PRI 27-NOV-2025
DEFINITION  nuclear receptor coactivator 2 isoform a [Homo sapiens].
ACCESSION   NP_001308632 XP_011515738
VERSION     NP_001308632.1
DBSOURCE    REFSEQ: accession NM_001321703.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1464)
  AUTHORS   Yu,X., Wang,X., Ma,K., Gao,D., Deng,Y., Zhou,D., Ding,W., Zhao,Y.,
            Liu,Q. and Zhou,Z.
  TITLE     Tai/NCOA2 suppresses the Hedgehog pathway by directly targeting the
            transcription factor Ci/GLI
  JOURNAL   Proc Natl Acad Sci U S A 121 (47), e2409380121 (2024)
   PUBMED   39531503
REFERENCE   2  (residues 1 to 1464)
  AUTHORS   Warmke,L.M., Mustafa,A., Zou,Y.S., Davis,J.L., Ulbright,T.M. and
            Segura,S.E.
  TITLE     Myxoid epithelioid smooth muscle tumor of the vulva: A distinct
            entity with MEF2D::NCOA2 gene fusion
  JOURNAL   Genes Chromosomes Cancer 63 (1), e23209 (2024)
   PUBMED   37870842
  REMARK    GeneRIF: Myxoid epithelioid smooth muscle tumor of the vulva: A
            distinct entity with MEF2D::NCOA2 gene fusion.
REFERENCE   3  (residues 1 to 1464)
  AUTHORS   Watson,S., LaVigne,C.A., Xu,L., Surdez,D., Cyrta,J., Calderon,D.,
            Cannon,M.V., Kent,M.R., Silvius,K.M., Kucinski,J.P., Harrison,E.N.,
            Murchison,W., Rakheja,D., Tirode,F., Delattre,O., Amatruda,J.F. and
            Kendall,G.C.
  TITLE     VGLL2-NCOA2 leverages developmental programs for pediatric
            sarcomagenesis
  JOURNAL   Cell Rep 42 (1), 112013 (2023)
   PUBMED   36656711
  REMARK    GeneRIF: VGLL2-NCOA2 leverages developmental programs for pediatric
            sarcomagenesis.
REFERENCE   4  (residues 1 to 1464)
  AUTHORS   Wang,L., Motoi,T., Khanin,R., Olshen,A., Mertens,F., Bridge,J., Dal
            Cin,P., Antonescu,C.R., Singer,S., Hameed,M., Bovee,J.V.,
            Hogendoorn,P.C., Socci,N. and Ladanyi,M.
  TITLE     Identification of a novel, recurrent HEY1-NCOA2 fusion in
            mesenchymal chondrosarcoma based on a genome-wide screen of
            exon-level expression data
  JOURNAL   Genes Chromosomes Cancer 51 (2), 127-139 (2012)
   PUBMED   22034177
  REMARK    GeneRIF: The novel HEY1-NCOA2 fusion appears to be the defining and
            diagnostic gene fusion in mesenchymal chondrosarcomas
REFERENCE   5  (residues 1 to 1464)
  AUTHORS   Strehl,S., Nebral,K., Konig,M., Harbott,J., Strobl,H., Ratei,R.,
            Struski,S., Bielorai,B., Lessard,M., Zimmermann,M., Haas,O.A. and
            Izraeli,S.
  TITLE     ETV6-NCOA2: a novel fusion gene in acute leukemia associated with
            coexpression of T-lymphoid and myeloid markers and frequent NOTCH1
            mutations
  JOURNAL   Clin Cancer Res 14 (4), 977-983 (2008)
   PUBMED   18281529
  REMARK    GeneRIF: ETV6-NCOA2 fusion may define a novel subgroup of acute
            leukemia with T-lymphoid and myeloid features, which is associated
            with a high prevalence of NOTCH1 mutations.
REFERENCE   6  (residues 1 to 1464)
  AUTHORS   Fryer,C.J. and Archer,T.K.
  TITLE     Chromatin remodelling by the glucocorticoid receptor requires the
            BRG1 complex
  JOURNAL   Nature 393 (6680), 88-91 (1998)
   PUBMED   9590696
REFERENCE   7  (residues 1 to 1464)
  AUTHORS   Carapeti,M., Aguiar,R.C., Goldman,J.M. and Cross,N.C.
  TITLE     A novel fusion between MOZ and the nuclear receptor coactivator
            TIF2 in acute myeloid leukemia
  JOURNAL   Blood 91 (9), 3127-3133 (1998)
   PUBMED   9558366
REFERENCE   8  (residues 1 to 1464)
  AUTHORS   Voegel,J.J., Heine,M.J., Tini,M., Vivat,V., Chambon,P. and
            Gronemeyer,H.
  TITLE     The coactivator TIF2 contains three nuclear receptor-binding motifs
            and mediates transactivation through CBP binding-dependent and
            -independent pathways
  JOURNAL   EMBO J 17 (2), 507-519 (1998)
   PUBMED   9430642
REFERENCE   9  (residues 1 to 1464)
  AUTHORS   Hong,H., Kohli,K., Garabedian,M.J. and Stallcup,M.R.
  TITLE     GRIP1, a transcriptional coactivator for the AF-2 transactivation
            domain of steroid, thyroid, retinoid, and vitamin D receptors
  JOURNAL   Mol Cell Biol 17 (5), 2735-2744 (1997)
   PUBMED   9111344
REFERENCE   10 (residues 1 to 1464)
  AUTHORS   Voegel,J.J., Heine,M.J., Zechel,C., Chambon,P. and Gronemeyer,H.
  TITLE     TIF2, a 160 kDa transcriptional mediator for the ligand-dependent
            activation function AF-2 of nuclear receptors
  JOURNAL   EMBO J 15 (14), 3667-3675 (1996)
   PUBMED   8670870
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022730.7, X97674.1,
            AW504723.1, DA691975.1, CN291204.1, CB270668.1, CK903771.1 and
            BC047111.1.
            
            On Mar 30, 2016 this sequence version replaced XP_011515738.1.
            
            Summary: The protein encoded by this gene functions as a
            transcriptional coactivator for nuclear hormone receptors,
            including steroid, thyroid, retinoid, and vitamin D receptors. The
            encoded protein acts as an intermediary factor for the
            ligand-dependent activity of these nuclear receptors, which
            regulate their target genes upon binding of cognate response
            elements. This gene has been found to be involved in translocations
            that result in fusions with other genes in various cancers,
            including the lysine acetyltransferase 6A (KAT6A) gene in acute
            myeloid leukemia, the ETS variant 6 (ETV6) gene in acute
            lymphoblastic leukemia, and the hes related family bHLH
            transcription factor with YRPW motif 1 (HEY1) gene in mesenchymal
            chondrosarcoma. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a). Variants 1, 2 and 3
            all encode isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3801353.1,
                                           SRR18074969.1305214.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.3"
     Protein         1..1464
                     /product="nuclear receptor coactivator 2 isoform a"
                     /note="glucocorticoid receptor-interacting protein-1;
                     transcriptional intermediary factor 2; class E basic
                     helix-loop-helix protein 75; p160 steroid receptor
                     coactivator 2"
                     /calculated_mol_wt=159026
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          28..91
                     /region_name="bHLH-PAS_NCoA2_SRC2"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in nuclear receptor coactivator 2 (NCoA-2)
                     and similar proteins; cd18950"
                     /db_xref="CDD:381520"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            order(30..32,36,38..39,43,68..69)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381520"
     Site            order(41..42,45..46,48..49,70,73,77,79..80,84,86)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381520"
     Region          118..175
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Site            order(139,143,149,162..165,195)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(159,163,172,175..176,202,204)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          268..378
                     /region_name="PAS_11"
                     /note="PAS domain; pfam14598"
                     /db_xref="CDD:464214"
     Site            338
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q61026; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          463..587
                     /region_name="NCOA_u2"
                     /note="Unstructured region on nuclear receptor coactivator
                     protein; pfam16665"
                     /db_xref="CDD:465223"
     Region          468..513
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          557..683
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          636..709
                     /region_name="SRC-1"
                     /note="Steroid receptor coactivator; pfam08832"
                     /db_xref="CDD:462615"
     Site            636
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q61026; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            640
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          641..645
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            682
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          690..694
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          691..743
                     /region_name="CASP8AP2-binding.
                     /evidence=ECO:0000250|UniProtKB:Q61026"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            699
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          709..737
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          730..1121
                     /region_name="Interaction with BMAL1.
                     /evidence=ECO:0000250|UniProtKB:Q61026"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          731..816
                     /region_name="DUF4927"
                     /note="Domain of unknown function (DUF4927); pfam16279"
                     /db_xref="CDD:465083"
     Site            736
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          745..749
                     /region_name="LXXLL motif 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            771
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            780
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            785
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            864
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q61026; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            869..870
                     /site_type="other"
                     /note="Breakpoint for translocation to form KAT6A-NCOA2.
                     /evidence=ECO:0000269|PubMed:12676584,
                     ECO:0000269|PubMed:15657427, ECO:0000269|PubMed:9558366;
                     propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            874
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q61026; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          878..882
                     /region_name="LXXLL motif 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          973..1003
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          1017..1038
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          1051..1074
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Region          1071..1115
                     /region_name="Nuc_rec_co-act"
                     /note="Nuclear receptor coactivator; pfam08815"
                     /db_xref="CDD:462608"
     Region          1079..1087
                     /region_name="LLXXLXXXL motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1173
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1177
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1190
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1196
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1203
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1221
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1240
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q61026; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1261
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Site            1266
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15596.2)"
     Region          1281..1338
                     /region_name="DUF1518"
                     /note="Nuclear receptor coactivator, DUF1518; pfam07469"
                     /db_xref="CDD:462174"
     Region          1441..1464
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15596.2)"
     CDS             1..1464
                     /gene="NCOA2"
                     /gene_synonym="bHLHe75; GRIP1; KAT13C; NCoA-2; SRC-2;
                     SRC2; TIF2"
                     /coded_by="NM_001321703.2:269..4663"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47872.1"
                     /db_xref="GeneID:10499"
                     /db_xref="HGNC:HGNC:7669"
                     /db_xref="MIM:601993"
ORIGIN      
        1 msgmgentsd psraetrkrk ecpdqlgpsp krntekrnre qenkyieela elifanfndi
       61 dnfnfkpdkc ailketvkqi rqikeqekaa aanidevqks dvsstgqgvi dkdalgpmml
      121 ealdgfffvv nlegnvvfvs envtqylryn qeelmnksvy silhvgdhte fvknllpksi
      181 vnggswsgep prrnshtfnc rmlvkplpds eeeghdnqea hqkyetmqcf avsqpksike
      241 egedlqscli cvarrvpmke rpvlpssesf ttrqdlqgki tsldtstmra amkpgwedlv
      301 rrciqkfhaq hegesvsyak rhhhevlrqg lafsqiyrfs lsdgtlvaaq tksklirsqt
      361 tnepqlvisl hmlhreqnvc vmnpdltgqt mgkplnpiss nspahqalcs gnpgqdmtls
      421 sninfpingp keqmgmpmgr fggsggmnhv sgmqattpqg snyalkmnsp sqsspgmnpg
      481 qptsmlsprh rmspgvagsp rippsqfspa gslhspvgvc sstgnshsyt nsslnalqal
      541 seghgvslgs slaspdlkmg nlqnspvnmn ppplskmgsl dskdcfglyg epsegttgqa
      601 esschpgeqk etndpnlppa vsseradgqs rlhdskgqtk llqllttksd qmepsplass
      661 lsdtnkdstg slpgsgsthg tslkekhkil hrllqdsssp vdlakltaea tgkdlsqess
      721 stapgsevti kqepvspkkk enallrylld kddtkdiglp eitpklerld sktdpasntk
      781 liamktekee msfepgdqpg seldnleeil ddlqnsqlpq lfpdtrpgap agsvdkqaii
      841 ndlmqltaen spvtpvgaqk talrisqstf nnprpgqlgr llpnqnlpld itlqsptgag
      901 pfppirnssp ysvipqpgmm gnqgmignqg nlgnsstgmi gnsasrptmp sgewapqssa
      961 vrvtcaatts amnrpvqggm irnpaasipm rpssqpgqrq tlqsqvmnig pselemnmgg
     1021 pqysqqqapp nqtapwpesi lpidqasfas qnrqpfgssp ddllcphpaa espsdegall
     1081 dqlylalrnf dgleeidral gipelvsqsq avdpeqfssq dsnimleqka pvfpqqyasq
     1141 aqmaqgsysp mqdpnfhtmg qrpsyatlrm qprpglrptg lvqnqpnqlr lqlqhrlqaq
     1201 qnrqplmnqi snvsnvnltl rpgvptqapi naqmlaqrqr eilnqhlrqr qmhqqqqvqq
     1261 rtlmmrgqgl nmtpsmvaps gmpatmsnpr ipqanaqqfp fppnygisqq pdpgftgatt
     1321 pqsplmsprm ahtqspmmqq sqanpayqap sdingwaqgn mggnsmfsqq spphfgqqan
     1381 tsmysnnmni nvsmatntgg mssmnqmtgq ismtsvtsvp tsglssmgpe qvndpalrgg
     1441 nlfpnqlpgm dmikqegdtt rkyc
//
LOCUS       NP_001231627             338 aa            linear   PRI 27-NOV-2025
DEFINITION  mRNA decay activator protein ZFP36L1 isoform 1 [Homo sapiens].
ACCESSION   NP_001231627
VERSION     NP_001231627.1
DBSOURCE    REFSEQ: accession NM_001244698.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Saenz-Narciso,B., Bell,S.E., Matheson,L.S., Venigalla,R.K.C. and
            Turner,M.
  TITLE     ZFP36-family RNA-binding proteins in regulatory T cells reinforce
            immune homeostasis
  JOURNAL   Nat Commun 16 (1), 4192 (2025)
   PUBMED   40328742
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Lu,F., Yao,L.P., Gao,D.D., Alinejad,T., Jiang,X.Q., Wu,Q.,
            Zhai,Q.C., Liu,M., Zhu,S.M., Qian,M.X., Xu,L.F., Chen,C.S. and
            Zhang,F.
  TITLE     MicroRNA-377-3p exacerbates chronic obstructive pulmonary disease
            through suppressing ZFP36L1 expression and inducing lung fibroblast
            senescence
  JOURNAL   Respir Res 25 (1), 67 (2024)
   PUBMED   38317146
  REMARK    GeneRIF: MicroRNA-377-3p exacerbates chronic obstructive pulmonary
            disease through suppressing ZFP36L1 expression and inducing lung
            fibroblast senescence.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Momin,T., Villasenor,A., Singh,A., Darweesh,M., Singh,A. and
            Rajput,M.
  TITLE     ZFP36 ring finger protein like 1 significantly suppresses human
            coronavirus OC43 replication
  JOURNAL   PeerJ 11, e14776 (2023)
   PUBMED   36846448
  REMARK    GeneRIF: ZFP36 ring finger protein like 1 significantly suppresses
            human coronavirus OC43 replication.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Chen,H.Y., Durmaz,Y.T., Li,Y., Sabet,A.H., Vajdi,A., Denize,T.,
            Walton,E., Laimon,Y.N., Doench,J.G., Mahadevan,N.R., Losman,J.A.,
            Barbie,D.A., Tolstorukov,M.Y., Rudin,C.M., Sen,T., Signoretti,S.
            and Oser,M.G.
  TITLE     Regulation of neuroendocrine plasticity by the RNA-binding protein
            ZFP36L1
  JOURNAL   Nat Commun 13 (1), 4998 (2022)
   PUBMED   36008402
  REMARK    GeneRIF: Regulation of neuroendocrine plasticity by the RNA-binding
            protein ZFP36L1.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Stoecklin,G., Colombi,M., Raineri,I., Leuenberger,S., Mallaun,M.,
            Schmidlin,M., Gross,B., Lu,M., Kitamura,T. and Moroni,C.
  TITLE     Functional cloning of BRF1, a regulator of ARE-dependent mRNA
            turnover
  JOURNAL   EMBO J 21 (17), 4709-4718 (2002)
   PUBMED   12198173
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Ning,Z.Q., Norton,J.D., Li,J. and Murphy,J.J.
  TITLE     Distinct mechanisms for rescue from apoptosis in Ramos human B
            cells by signaling through CD40 and interleukin-4 receptor: role
            for inhibition of an early response gene, Berg36
  JOURNAL   Eur J Immunol 26 (10), 2356-2363 (1996)
   PUBMED   8898945
REFERENCE   8  (residues 1 to 338)
  AUTHORS   Maclean,K.N., See,C.G., McKay,I.A. and Bustin,S.A.
  TITLE     The human immediate early gene BRF1 maps to chromosome 14q22-q24
  JOURNAL   Genomics 30 (1), 89-90 (1995)
   PUBMED   8595910
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Bustin,S.A., Nie,X.F., Barnard,R.C., Kumar,V., Pascall,J.C.,
            Brown,K.D., Leigh,I.M., Williams,N.S. and McKay,I.A.
  TITLE     Cloning and characterization of ERF-1, a human member of the Tis11
            family of early-response genes
  JOURNAL   DNA Cell Biol 13 (5), 449-459 (1994)
   PUBMED   8024689
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Barnard,R.C., Pascall,J.C., Brown,K.D., McKay,I.A., Williams,N.S.
            and Bustin,S.A.
  TITLE     Coding sequence of ERF-1, the human homologue of Tis11b/cMG1,
            members of the Tis11 family of early response genes
  JOURNAL   Nucleic Acids Res 21 (15), 3580 (1993)
   PUBMED   8346037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA876968.1, AK024202.1,
            BC018340.1, BQ894292.1, DR423896.1 and BQ004874.1.
            
            Summary: This gene is a member of the TIS11 family of early
            response genes, which are induced by various agonists such as the
            phorbol ester TPA and the polypeptide mitogen EGF. This gene is
            well conserved across species and has a promoter that contains
            motifs seen in other early-response genes. The encoded protein
            contains a distinguishing putative zinc finger domain with a
            repeating cys-his motif. This putative nuclear transcription factor
            most likely functions in regulating the response to growth factors.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2011].
            
            Transcript Variant: This variant (2) is alternatively spliced at
            the 3' end, and has a shorter 3' UTR compared to variant 1.
            Variants 1 and 2 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK024202.1, SRR18074968.2015932.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.1"
     Protein         1..338
                     /product="mRNA decay activator protein ZFP36L1 isoform 1"
                     /note="EGF-response factor 1; early response factor
                     Berg36; zinc finger protein, C3H type, 36-like 1; butyrate
                     response factor 1; zinc finger protein 36, C3H1 type-like
                     1; zinc finger protein 36, C3H type-like 1; ZFP36-like 1;
                     TPA-induced sequence 11b; mRNA decay activator protein
                     ZFP36L1; ZFP36 ring finger protein like 1"
                     /calculated_mol_wt=36183
     Region          1..111
                     /region_name="Necessary and sufficient for the association
                     with mRNA decay enzymes and mRNA decay activation.
                     /evidence=ECO:0000269|PubMed:15687258"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07352.1)"
     Region          1..106
                     /region_name="Tis11B_N"
                     /note="Tis11B like protein, N terminus; pfam04553"
                     /db_xref="CDD:461350"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK2.
                     /evidence=ECO:0000269|PubMed:18326031,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q07352.1)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:15538381; propagated from
                     UniProtKB/Swiss-Prot (Q07352.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1 and MAPKAPK2.
                     /evidence=ECO:0000269|PubMed:15538381,
                     ECO:0000269|PubMed:18326031; propagated from
                     UniProtKB/Swiss-Prot (Q07352.1)"
     Region          93..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07352.1)"
     Region          <115..>177
                     /region_name="CTH1"
                     /note="CCCH-type Zn-finger protein [General function
                     prediction only]; COG5063"
                     /db_xref="CDD:227395"
     Region          185..338
                     /region_name="Necessary for mRNA decay activation.
                     /evidence=ECO:0000269|PubMed:15687258"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07352.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1 and MAPKAPK2.
                     /evidence=ECO:0000269|PubMed:17030608,
                     ECO:0000269|PubMed:18326031; propagated from
                     UniProtKB/Swiss-Prot (Q07352.1)"
     Region          273..338
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07352.1)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q07352.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA1.
                     /evidence=ECO:0000269|PubMed:25106868; propagated from
                     UniProtKB/Swiss-Prot (Q07352.1)"
     CDS             1..338
                     /gene="ZFP36L1"
                     /gene_synonym="Berg36; BRF1; cMG1; ERF-1; ERF1; RNF162B;
                     TIS11B"
                     /coded_by="NM_001244698.2:479..1495"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9791.1"
                     /db_xref="GeneID:677"
                     /db_xref="HGNC:HGNC:1107"
                     /db_xref="MIM:601064"
ORIGIN      
        1 mtttlvsati fdlsevlckg nkmlnysaps aggclldrka vgtpagggfp rrhsvtlpss
       61 kfhqnqllss lkgepapals srdsrfrdrs fseggerllp tqkqpgggqv nssryktelc
      121 rpfeengack ygdkcqfahg ihelrsltrh pkyktelcrt fhtigfcpyg prchfihnae
      181 erralagard lsadrprlqh sfsfagfpsa aataaatgll dsptsitppp ilsaddllgs
      241 ptlpdgtnnp fafssqelas lfapsmglpg ggspttflfr pmsesphmfd sppspqdsls
      301 dqegylssss sshsgsdspt ldnsrrlpif srlsisdd
//
LOCUS       NP_116186                373 aa            linear   PRI 27-NOV-2025
DEFINITION  ferroptosis suppressor protein 1 [Homo sapiens].
ACCESSION   NP_116186
VERSION     NP_116186.1
DBSOURCE    REFSEQ: accession NM_032797.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Yang,J.S., Morris,A.J., Kamizaki,K., Chen,J., Stark,J.,
            Oldham,W.M., Nakamura,T., Mishima,E., Loscalzo,J., Minami,Y.,
            Conrad,M., Henry,W.S. and Hsu,V.W.
  TITLE     ALDH7A1 protects against ferroptosis by generating membrane NADH
            and regulating FSP1
  JOURNAL   Cell 188 (10), 2569-2585 (2025)
   PUBMED   40233740
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Lan,H., Gao,Y., Hong,T., Chang,Z., Zhao,Z., Wang,Y. and Wang,F.
  TITLE     Structural insight into 6-OH-FAD-dependent activation of hFSP1 for
            ferroptosis suppression
  JOURNAL   Cell Discov 10 (1), 88 (2024)
   PUBMED   39160155
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Tan,Y.R., Jiang,B.H., Feng,W.J., He,Z.L., Jiang,Y.L., Xun,Y.,
            Wu,X.P., Li,Y.H. and Zhu,H.B.
  TITLE     Circ0060467 sponges miR-6805 to promote hepatocellular carcinoma
            progression through regulating AIFM2 and GPX4 expression
  JOURNAL   Aging (Albany NY) 16 (2), 1796-1807 (2024)
   PUBMED   38244593
  REMARK    GeneRIF: Circ0060467 sponges miR-6805 to promote hepatocellular
            carcinoma progression through regulating AIFM2 and GPX4 expression.
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Yuan,S., Xi,S., Weng,H., Guo,M.M., Zhang,J.H., Yu,Z.P., Zhang,H.,
            Yu,Z., Xing,Z., Liu,M.Y., Ming,D.J., Sah,R.K., Zhou,Y., Li,G.,
            Zeng,T., Hong,X., Li,Y., Zeng,X.T. and Hu,H.
  TITLE     YTHDC1 as a tumor progression suppressor through modulating
            FSP1-dependent ferroptosis suppression in lung cancer
  JOURNAL   Cell Death Differ 30 (12), 2477-2490 (2023)
   PUBMED   37903990
  REMARK    GeneRIF: YTHDC1 as a tumor progression suppressor through
            modulating FSP1-dependent ferroptosis suppression in lung cancer.
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Nakamura,T., Mishima,E., Yamada,N., Mourao,A.S.D., Trumbach,D.,
            Doll,S., Wanninger,J., Lytton,E., Sennhenn,P., Nishida Xavier da
            Silva,T., Angeli,J.P.F., Sattler,M., Proneth,B. and Conrad,M.
  TITLE     Integrated chemical and genetic screens unveil FSP1 mechanisms of
            ferroptosis regulation
  JOURNAL   Nat Struct Mol Biol 30 (11), 1806-1815 (2023)
   PUBMED   37957306
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Wu,M., Xu,L.G., Su,T., Tian,Y., Zhai,Z. and Shu,H.B.
  TITLE     AMID is a p53-inducible gene downregulated in tumors
  JOURNAL   Oncogene 23 (40), 6815-6819 (2004)
   PUBMED   15273740
  REMARK    GeneRIF: AMID is a p53-downstream gene involved in tumorigenesis.
REFERENCE   7  (residues 1 to 373)
  AUTHORS   Fujimoto,Y., Itabe,H., Sakai,J., Makita,M., Noda,J., Mori,M.,
            Higashi,Y., Kojima,S. and Takano,T.
  TITLE     Identification of major proteins in the lipid droplet-enriched
            fraction isolated from the human hepatocyte cell line HuH7
  JOURNAL   Biochim Biophys Acta 1644 (1), 47-59 (2004)
   PUBMED   14741744
REFERENCE   8  (residues 1 to 373)
  AUTHORS   Ohiro,Y., Garkavtsev,I., Kobayashi,S., Sreekumar,K.R., Nantz,R.,
            Higashikubo,B.T., Duffy,S.L., Higashikubo,R., Usheva,A., Gius,D.,
            Kley,N. and Horikoshi,N.
  TITLE     A novel p53-inducible apoptogenic gene, PRG3, encodes a homologue
            of the apoptosis-inducing factor (AIF)
  JOURNAL   FEBS Lett 524 (1-3), 163-171 (2002)
   PUBMED   12135761
  REMARK    GeneRIF: encodes a homologue of the apoptosis-inducing factor
REFERENCE   9  (residues 1 to 373)
  AUTHORS   Wu,M., Xu,L.G., Li,X., Zhai,Z. and Shu,H.B.
  TITLE     AMID, an apoptosis-inducing factor-homologous
            mitochondrion-associated protein, induces caspase-independent
            apoptosis
  JOURNAL   J Biol Chem 277 (28), 25617-25623 (2002)
   PUBMED   11980907
  REMARK    GeneRIF: induces caspase-independent apoptosis
REFERENCE   10 (residues 1 to 373)
  AUTHORS   Horikoshi,N., Cong,J., Kley,N. and Shenk,T.
  TITLE     Isolation of differentially expressed cDNAs from p53-dependent
            apoptotic cells: activation of the human homologue of the
            Drosophila peroxidasin gene
  JOURNAL   Biochem Biophys Res Commun 261 (3), 864-869 (1999)
   PUBMED   10441517
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG332787.1, AL731540.4,
            BC023601.2 and AI922797.1.
            
            Summary: This gene encodes a flavoprotein oxidoreductase that binds
            single stranded DNA and is thought to contribute to apoptosis in
            the presence of bacterial and viral DNA. The expression of this
            gene is also found to be induced by tumor suppressor protein p53 in
            colon cancer cells. [provided by RefSeq, Nov 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK027403.1, SRR14038195.1414066.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307864.3/ ENSP00000312370.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..373
                     /product="ferroptosis suppressor protein 1"
                     /note="apoptosis-inducing factor (AIF)-like
                     mitochondrion-associated inducer of death;
                     apoptosis-inducing factor 2; p53-responsive gene 3
                     protein; apoptosis-inducing factor,
                     mitochondrion-associated, 2; ferroptosis suppressor 1;
                     apoptosis inducing factor mitochondria associated 2; AIF
                     family member 2"
                     /calculated_mol_wt=40396
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRQ8.1)"
     Region          76..355
                     /region_name="Ndh"
                     /note="NADH dehydrogenase, FAD-containing subunit [Energy
                     production and conversion]; COG1252"
                     /db_xref="CDD:440864"
     Site            168
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by KAT2B.
                     /evidence=ECO:0000269|PubMed:39881208; propagated from
                     UniProtKB/Swiss-Prot (Q9BRQ8.1)"
     Site            174
                     /site_type="other"
                     /note="4-hydroxy-2-nonenal adduction.
                     /evidence=ECO:0000250|UniProtKB:Q8BUE4; propagated from
                     UniProtKB/Swiss-Prot (Q9BRQ8.1)"
     CDS             1..373
                     /gene="AIFM2"
                     /gene_synonym="AMID; FSP1; PRG3"
                     /coded_by="NM_032797.6:106..1227"
                     /db_xref="CCDS:CCDS7297.1"
                     /db_xref="GeneID:84883"
                     /db_xref="HGNC:HGNC:21411"
                     /db_xref="MIM:605159"
ORIGIN      
        1 mgsqvsvesg alhvvivggg fggiaaasql qalnvpfmlv dmkdsfhhnv aalrasvetg
       61 fakktfisys vtfkdnfrqg lvvgidlknq mvllqggeal pfshlilatg stgpfpgkfn
      121 evssqqaaiq ayedmvrqvq rsrfivvvgg gsagvemaae ikteypekev tlihsqvala
      181 dkellpsvrq evkeillrkg vqlllservs nleelplney reyikvqtdk gtevatnlvi
      241 lctgikinss ayrkafesrl assgalrvne hlqveghsnv yaigdcadvr tpkmaylagl
      301 haniavaniv nsvkqrplqa ykpgaltfll smgrndgvgq isgfyvgrlm vrltksrdlf
      361 vstswktmrq spp
//
LOCUS       NP_079151                753 aa            linear   PRI 27-NOV-2025
DEFINITION  synaptopodin 2-like protein isoform b [Homo sapiens].
ACCESSION   NP_079151
VERSION     NP_079151.2
DBSOURCE    REFSEQ: accession NM_024875.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Wu,J., Ouyang,P., Huang,R., Cui,Y., Yang,Z., Xu,W., Ma,R.,
            Xiang,G., Zeng,W., Wu,W. and Li,J.
  TITLE     METTL16 Promotes Stability of SYNPO2L mRNA and leading to Cancer
            Cell Lung Metastasis by Secretion of COL10A1 and attract the
            Cancer-Associated Fibroblasts
  JOURNAL   Int J Biol Sci 20 (11), 4128-4145 (2024)
   PUBMED   39247832
  REMARK    GeneRIF: METTL16 Promotes Stability of SYNPO2L mRNA and leading to
            Cancer Cell Lung Metastasis by Secretion of COL10A1 and attract the
            Cancer-Associated Fibroblasts.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 753)
  AUTHORS   van Eldik,W., den Adel,B., Monshouwer-Kloots,J., Salvatori,D.,
            Maas,S., van der Made,I., Creemers,E.E., Frank,D., Frey,N.,
            Boontje,N., van der Velden,J., Steendijk,P., Mummery,C., Passier,R.
            and Beqqali,A.
  TITLE     Z-disc protein CHAPb induces cardiomyopathy and contractile
            dysfunction in the postnatal heart
  JOURNAL   PLoS One 12 (12), e0189139 (2017)
   PUBMED   29206857
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 753)
  AUTHORS   Lubitz,S.A., Brody,J.A., Bihlmeyer,N.A., Roselli,C., Weng,L.C.,
            Christophersen,I.E., Alonso,A., Boerwinkle,E., Gibbs,R.A.,
            Bis,J.C., Cupples,L.A., Mohler,P.J., Nickerson,D.A., Muzny,D.,
            Perez,M.V., Psaty,B.M., Soliman,E.Z., Sotoodehnia,N., Lunetta,K.L.,
            Benjamin,E.J., Heckbert,S.R., Arking,D.E., Ellinor,P.T. and Lin,H.
  CONSRTM   NHLBI GO Exome Sequencing Project
  TITLE     Whole Exome Sequencing in Atrial Fibrillation
  JOURNAL   PLoS Genet 12 (9), e1006284 (2016)
   PUBMED   27589061
  REMARK    GeneRIF: we did not observe associations between coding genetic
            variants and Atrial fibrillation (AF), suggesting that large-effect
            coding variation is not the predominant mechanism underlying AF. A
            coding variant in SYNPO2L requires further evaluation to determine
            whether it is causally related to AF
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 753)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 753)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 753)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073389.10, DA685385.1, BC142635.1, AB188489.1 and AK022983.1.
            
            On Jul 15, 2004 this sequence version replaced NP_079151.1.
            
            Transcript Variant: This variant (2) contains an alternate 5'
            terminal exon resulting in different 5' UTR and 5' coding regions,
            compared to variant 1. It encodes isoform b, which is shorter and
            has a distinct N-terminus, compared to isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK022983.1, DRR138525.728885.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147975, SAMEA2151741
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..753
                     /product="synaptopodin 2-like protein isoform b"
                     /note="synaptopodin 2-like protein"
                     /calculated_mol_wt=79016
     Region          <191..326
                     /region_name="PRK14954"
                     /note="DNA polymerase III subunits gamma and tau;
                     Provisional"
                     /db_xref="CDD:184918"
     CDS             1..753
                     /gene="SYNPO2L"
                     /gene_synonym="CHAP"
                     /coded_by="NM_024875.5:34..2295"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS7331.1"
                     /db_xref="GeneID:79933"
                     /db_xref="HGNC:HGNC:23532"
                     /db_xref="MIM:621429"
ORIGIN      
        1 metfepisqe plsqasydka pdpvpelqds fyaelqraes lqeksikeak tkcrtiasll
       61 taapnphskg vlmfkkrrqr akkytlvsfg aaagtgaeee dgvpptsese ldeeafsdar
      121 sltnqsdwds pyldmelara gsrasegqgs glggqlsevs grgvqlfeqq rqradsstqe
      181 larvepaaml ngeglqsppr aqsappeaav lppsplpapv asprpfqpgg gaptpapsif
      241 nrsarpftpg lqgqrpttts vifrplapkr andslgglsp apppflssqg ptplpsftsg
      301 vpshapvsgs pstprssgpv tatsslyipa psrpvtpgga peppappsaa amtstasifl
      361 saplrpsarp eapapgpgap eppsareqri svpaartgil qearrrgtrk qmfrpgkeet
      421 knspnpells lvqnldekpr aggaesgpee dalslgaeac nfmqpvgars yktlphvtpk
      481 tpppmapktp ppmtpktppp vapkppsrgl ldglvngaas sagipepprl qgrggelfak
      541 rqsradryvv egtpgpglgp rprspsptps lppswkyspn irapppiayn pllspffpqa
      601 artlpkaqsq gpratpkqgi kaldfmrhqp yqlktamfcf devpptpgpi asgspktarv
      661 qeirrfstpa pqptaeplap tvlapraatt ldepiwrtel asapvpspap ppeaprglga
      721 spsscgfqva rprfsatrtg lqahvwrpga ghq
//
LOCUS       NP_001230808             188 aa            linear   PRI 27-NOV-2025
DEFINITION  transformer-2 protein homolog beta isoform 2 [Homo sapiens].
ACCESSION   NP_001230808
VERSION     NP_001230808.1
DBSOURCE    REFSEQ: accession NM_001243879.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Karginov,T.A., Menoret,A., Leclair,N.K., Harrison,A.G.,
            Chandiran,K., Suarez-Ramirez,J.E., Yurieva,M., Karlinsey,K.,
            Wang,P., O'Neill,R.J., Murphy,P.A., Adler,A.J., Cauley,L.S.,
            Anczukow,O., Zhou,B. and Vella,A.T.
  TITLE     Autoregulated splicing of TRA2beta programs T cell fate in response
            to antigen-receptor stimulation
  JOURNAL   Science 385 (6714), eadj1979 (2024)
   PUBMED   39265028
  REMARK    GeneRIF: Autoregulated splicing of TRA2beta programs T cell fate in
            response to antigen-receptor stimulation.
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Chen,G., Chen,J., Qi,L., Yin,Y., Lin,Z., Wen,H., Zhang,S., Xiao,C.,
            Bello,S.F., Zhang,X., Nie,Q. and Luo,W.
  TITLE     Bulk and single-cell alternative splicing analyses reveal roles of
            TRA2B in myogenic differentiation
  JOURNAL   Cell Prolif 57 (2), e13545 (2024)
   PUBMED   37705195
  REMARK    GeneRIF: Bulk and single-cell alternative splicing analyses reveal
            roles of TRA2B in myogenic differentiation.
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Ramond,F., Dalgliesh,C., Grimmel,M., Wechsberg,O., Vetro,A.,
            Guerrini,R., FitzPatrick,D., Poole,R.L., Lebrun,M., Bayat,A.,
            Grasshoff,U., Bertrand,M., Witt,D., Turnpenny,P.D., Faundes,V.,
            Santa Maria,L., Mendoza Fuentes,C., Mabe,P., Hussain,S.A.,
            Mullegama,S.V., Torti,E., Oehl-Jaschkowitz,B., Salmon,L.B.,
            Orenstein,N., Shahar,N.R., Hagari,O., Bazak,L., Hoffjan,S.,
            Prada,C.E., Haack,T. and Elliott,D.J.
  TITLE     Clustered variants in the 5' coding region of TRA2B cause a
            distinctive neurodevelopmental syndrome
  JOURNAL   Genet Med 25 (4), 100003 (2023)
   PUBMED   36549593
  REMARK    GeneRIF: Clustered variants in the 5' coding region of TRA2B cause
            a distinctive neurodevelopmental syndrome.
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 188)
  AUTHORS   Li,M.J., Xiong,D., Wang,S. and Huang,H.
  TITLE     Tra2beta Enhances Cell Proliferation by Inducing the Expression of
            Transcription Factor SP1 in Cervical Cancer
  JOURNAL   Biomed Environ Sci 36 (2), 146-159 (2023)
   PUBMED   36861193
  REMARK    GeneRIF: Tra2beta Enhances Cell Proliferation by Inducing the
            Expression of Transcription Factor SP1 in Cervical Cancer.
REFERENCE   6  (residues 1 to 188)
  AUTHORS   Nayler,O., Cap,C. and Stamm,S.
  TITLE     Human transformer-2-beta gene (SFRS10): complete nucleotide
            sequence, chromosomal localization, and generation of a
            tissue-specific isoform
  JOURNAL   Genomics 53 (2), 191-202 (1998)
   PUBMED   9790768
REFERENCE   7  (residues 1 to 188)
  AUTHORS   Tacke,R., Tohyama,M., Ogawa,S. and Manley,J.L.
  TITLE     Human Tra2 proteins are sequence-specific activators of pre-mRNA
            splicing
  JOURNAL   Cell 93 (1), 139-148 (1998)
   PUBMED   9546399
REFERENCE   8  (residues 1 to 188)
  AUTHORS   Imai,Y., Matsuo,N., Ogawa,S., Tohyama,M. and Takagi,T.
  TITLE     Cloning of a gene, YT521, for a novel RNA splicing-related protein
            induced by hypoxia/reoxygenation
  JOURNAL   Brain Res Mol Brain Res 53 (1-2), 33-40 (1998)
   PUBMED   9473574
REFERENCE   9  (residues 1 to 188)
  AUTHORS   Beil,B., Screaton,G. and Stamm,S.
  TITLE     Molecular cloning of htra2-beta-1 and htra2-beta-2, two human
            homologs of tra-2 generated by alternative splicing
  JOURNAL   DNA Cell Biol 16 (6), 679-690 (1997)
   PUBMED   9212162
REFERENCE   10 (residues 1 to 188)
  AUTHORS   Matsuo,N., Ogawa,S., Imai,Y., Takagi,T., Tohyama,M., Stern,D. and
            Wanaka,A.
  TITLE     Cloning of a novel RNA binding polypeptide (RA301) induced by
            hypoxia/reoxygenation
  JOURNAL   J Biol Chem 270 (47), 28216-28222 (1995)
   PUBMED   7499316
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA164444.1, AK301118.1,
            U61267.1 and AC009247.13.
            
            Summary: This gene encodes a nuclear protein which functions as
            sequence-specific serine/arginine splicing factor which plays a
            role in mRNA processing, splicing patterns, and gene expression.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (2) lacks an alternate exon in the
            5' coding region and uses a downstream start codon, compared to
            variant 1. Isoform 2 has a shorter N-terminus, compared to isoform
            1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.132793.1,
                                           SRR1803617.202653.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267755, SAMN03267770
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.2"
     Protein         1..188
                     /product="transformer-2 protein homolog beta isoform 2"
                     /note="transformer-2 protein homolog beta; TRA-2 beta;
                     transformer-2 protein homolog B; protein phosphatase 1,
                     regulatory subunit 156; splicing factor,
                     arginine/serine-rich 10 (transformer 2 homolog,
                     Drosophila)"
                     /calculated_mol_wt=21804
     Region          11..97
                     /region_name="RRM_TRA2B"
                     /note="RNA recognition motif (RRM) found in Transformer-2
                     protein homolog beta (TRA-2 beta) and similar proteins;
                     cd12641"
                     /db_xref="CDD:410046"
     Site            order(11,19,23..24,48,50,59,61,63,65,87..90,93..97)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:410046"
     CDS             1..188
                     /gene="TRA2B"
                     /gene_synonym="Htra2-beta; PPP1R156; RAMELN; SFRS10;
                     SRFS10; TRA2-BETA; TRAN2B"
                     /coded_by="NM_001243879.2:321..887"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58872.1"
                     /db_xref="GeneID:6434"
                     /db_xref="HGNC:HGNC:10781"
                     /db_xref="MIM:602719"
ORIGIN      
        1 mstrrrhvgn ranpdpnccl gvfglslytt erdlrevfsk ygpiadvsiv ydqqsrrsrg
       61 fafvyfenvd dakeakeran gmeldgrrir vdfsitkrph tptpgiymgr ptygssrrrd
      121 yydrgydrgy ddrdyysrsy rggggggggw raaqdrdqiy rrrspspyys rggyrsrsrs
      181 rsysprry
//
LOCUS       NP_065070               1429 aa            linear   PRI 27-NOV-2025
DEFINITION  ankyrin repeat domain-containing protein 50 isoform 1 [Homo
            sapiens].
ACCESSION   NP_065070 XP_048747
VERSION     NP_065070.1
DBSOURCE    REFSEQ: accession NM_020337.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1429)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 1429)
  AUTHORS   Kvainickas,A., Orgaz,A.J., Nagele,H., Diedrich,B., Heesom,K.J.,
            Dengjel,J., Cullen,P.J. and Steinberg,F.
  TITLE     Retromer- and WASH-dependent sorting of nutrient transporters
            requires a multivalent interaction network with ANKRD50
  JOURNAL   J Cell Sci 130 (2), 382-395 (2017)
   PUBMED   27909246
  REMARK    GeneRIF: ANKRD50 simultaneously engages multiple parts of the
            SNX27-retromer-WASH complex machinery in a direct and co-operative
            interaction network that is needed to efficiently recycle the
            nutrient transporters.
REFERENCE   3  (residues 1 to 1429)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 1429)
  AUTHORS   McGough,I.J., Steinberg,F., Gallon,M., Yatsu,A., Ohbayashi,N.,
            Heesom,K.J., Fukuda,M. and Cullen,P.J.
  TITLE     Identification of molecular heterogeneity in
            SNX27-retromer-mediated endosome-to-plasma-membrane recycling
  JOURNAL   J Cell Sci 127 (Pt 22), 4940-4953 (2014)
   PUBMED   25278552
REFERENCE   5  (residues 1 to 1429)
  AUTHORS   Khadka,S., Vangeloff,A.D., Zhang,C., Siddavatam,P., Heaton,N.S.,
            Wang,L., Sengupta,R., Sahasrabudhe,S., Randall,G., Gribskov,M.,
            Kuhn,R.J., Perera,R. and LaCount,D.J.
  TITLE     A physical interaction network of dengue virus and human proteins
  JOURNAL   Mol Cell Proteomics 10 (12), M111.012187 (2011)
   PUBMED   21911577
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK295135.1, AK291068.1, CX871714.1, AK127496.1, AB033049.2 and
            AA628892.1.
            
            On May 1, 2005 this sequence version replaced XP_048747.4.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK291068.1, SRR1660807.63981.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000504087.6/ ENSP00000425658.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.1"
     Protein         1..1429
                     /product="ankyrin repeat domain-containing protein 50
                     isoform 1"
                     /note="ankyrin repeat domain-containing protein 50;
                     ankyrin repeat domain containing 50"
                     /calculated_mol_wt=155729
     Region          22..195
                     /region_name="AAA_16"
                     /note="AAA ATPase domain; pfam13191"
                     /db_xref="CDD:433025"
     Region          477..509
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          <495..>609
                     /region_name="PHA03100"
                     /note="ankyrin repeat protein; Provisional; cl39094"
                     /db_xref="CDD:476869"
     Region          511..540
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          544..575
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          544..573
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          558..851
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          577..608
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          577..606
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          610..641
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          610..639
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          643..674
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          643..672
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Site            order(676,678,682..683,686..688,690..691,695,698,707,709,
                     711,715..716,724..726,728..729,733,736,745,747,749,
                     753..754,757..759,761..762,766,769,778)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          676..707
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          676..705
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          709..745
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          709..743
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          747..778
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          747..776
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          780..811
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          780..809
                     /region_name="ANK 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          813..844
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          813..842
                     /region_name="ANK 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          833..1102
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          846..875
                     /region_name="ANK 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          847..877
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(848,852..853,856..858,860..861,865,868,877,879,881,
                     885..886,889..891,893..894,898,901,910,912,914,918..919,
                     922..924,926..927,931,934,943)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          879..910
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          879..908
                     /region_name="ANK 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          912..943
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          912..941
                     /region_name="ANK 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          945..976
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          945..974
                     /region_name="ANK 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Site            order(978,980,984..985,988..990,992..993,997,1000,1009,
                     1011,1013,1017..1018,1021..1023,1025..1026,1030,1033,1042,
                     1044,1046,1050..1051,1054..1056,1058..1059,1063,1066,1075)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          978..1009
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          978..1007
                     /region_name="ANK 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          1011..1042
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1011..1040
                     /region_name="ANK 17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          1044..1075
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1044..1073
                     /region_name="ANK 18"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          1077..1107
                     /region_name="ANK 19"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          1077..1102
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1108..1200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Site            1165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Site            1167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Region          <1210..1403
                     /region_name="Semenogelin"
                     /note="pfam05474"
                     /db_xref="CDD:368458"
     Region          1217..1296
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Site            1222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     Site            1400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULJ7.4)"
     CDS             1..1429
                     /gene="ANKRD50"
                     /coded_by="NM_020337.3:1039..5328"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34060.1"
                     /db_xref="GeneID:57182"
                     /db_xref="HGNC:HGNC:29223"
                     /db_xref="MIM:619856"
ORIGIN      
        1 mtnpweekvc kmaqtsllqg kqfycrewvf hklqhclqek snccnsavna pslvmnsgnn
       61 asgvsgkgaa wgvllvggpg sgktalctel lwpsspaslq rglhrqalaf hfckaqdsdt
      121 lcvggfirgl vaqicrsgll qgyedklrdp avqsllqpge cernpaeafk rcvllpllgm
      181 kppqqslyll vdsvdegcni tegeqtstsl sgtvaallag hheffppwll llcsarkqsk
      241 avtkmftgfr kislddlrka yivkdvqqyi lhrldqeeal rqhltketae mlnqlhikss
      301 gcflylervl dgvvenfiml reirdipgtl nglylwlcqr lfvrkqfakv qpilnvilaa
      361 crpltitely havwtknmsl tledfqrkld ilskllvdgl gntkilfhys faewlldvkh
      421 ctqkylcnaa eghrmlamsy tcqaknltpl eaqefalhli nsnlqletae lalwmiwngt
      481 pvrdslstli pkeqevlqll vkagahvnse ddrtscivrq aleredsirt lldngasvnq
      541 cdsngrtlla naaysgsldv vnllvsrgad leiedahght pltlaarqgh tkvvncligc
      601 ganinhtdqd gwtalrsaaw gghtevvsal lyagvkvdca dadsrtalra aawgghediv
      661 lnllqhgaev nkadnegrta liaaaymghr eivehlldhg aevnhedvdg rtalsvaalc
      721 vpaskghasv vsllidrgae vdhcdkdgmt pllvaayegh vdvvdllleg gadvdhtdnn
      781 grtpllaaas mghasvvntl lfwgaavdsi dsegrtvlsi asaqgnvevv rtlldrglde
      841 nhrddagwtp lhmaafeghr licealieqg artneidndg ripfilasqe ghydcvqill
      901 enksnidqrg ydgrnalrva aleghrdive llfshgadvn ckdadgrptl yilalenqlt
      961 maeyflenga nveasdaegr talhvscwqg hmemvqvlia yhadvnaadn ekrsalqsaa
     1021 wqghvkvvql liehgavvdh tcnqgatalc iaaqeghidv vqvllehgad pnhadqfgrt
     1081 amrvaakngh sqiiklleky gasslngcsp spvhtmeqkp lqslsskvqs ltiksnssgs
     1141 tgggdmqpsl rglpngptha fsspsespds tvdrqkssls nnslksskns slrttsstat
     1201 aqtvpidsfh nlsfteqiqq hslprsrsrq sivspssttq slgqshnsps sefewsqvkp
     1261 slkstkaskg gksensaksg sagkkakqsn ssqpkvleye mtqfdrrgpi aksgtaappk
     1321 qmpaesqcki mipsaqqeig rsqqqflihq qsgeqkkrng imtnpnyhlq snqvflgrvs
     1381 vprtmqdrgh qevlegypss etelslkqal klqiegsdps fnykketpl
//
LOCUS       NP_004917                338 aa            linear   PRI 27-NOV-2025
DEFINITION  mRNA decay activator protein ZFP36L1 isoform 1 [Homo sapiens].
ACCESSION   NP_004917
VERSION     NP_004917.2
DBSOURCE    REFSEQ: accession NM_004926.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Saenz-Narciso,B., Bell,S.E., Matheson,L.S., Venigalla,R.K.C. and
            Turner,M.
  TITLE     ZFP36-family RNA-binding proteins in regulatory T cells reinforce
            immune homeostasis
  JOURNAL   Nat Commun 16 (1), 4192 (2025)
   PUBMED   40328742
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Lu,F., Yao,L.P., Gao,D.D., Alinejad,T., Jiang,X.Q., Wu,Q.,
            Zhai,Q.C., Liu,M., Zhu,S.M., Qian,M.X., Xu,L.F., Chen,C.S. and
            Zhang,F.
  TITLE     MicroRNA-377-3p exacerbates chronic obstructive pulmonary disease
            through suppressing ZFP36L1 expression and inducing lung fibroblast
            senescence
  JOURNAL   Respir Res 25 (1), 67 (2024)
   PUBMED   38317146
  REMARK    GeneRIF: MicroRNA-377-3p exacerbates chronic obstructive pulmonary
            disease through suppressing ZFP36L1 expression and inducing lung
            fibroblast senescence.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Momin,T., Villasenor,A., Singh,A., Darweesh,M., Singh,A. and
            Rajput,M.
  TITLE     ZFP36 ring finger protein like 1 significantly suppresses human
            coronavirus OC43 replication
  JOURNAL   PeerJ 11, e14776 (2023)
   PUBMED   36846448
  REMARK    GeneRIF: ZFP36 ring finger protein like 1 significantly suppresses
            human coronavirus OC43 replication.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Chen,H.Y., Durmaz,Y.T., Li,Y., Sabet,A.H., Vajdi,A., Denize,T.,
            Walton,E., Laimon,Y.N., Doench,J.G., Mahadevan,N.R., Losman,J.A.,
            Barbie,D.A., Tolstorukov,M.Y., Rudin,C.M., Sen,T., Signoretti,S.
            and Oser,M.G.
  TITLE     Regulation of neuroendocrine plasticity by the RNA-binding protein
            ZFP36L1
  JOURNAL   Nat Commun 13 (1), 4998 (2022)
   PUBMED   36008402
  REMARK    GeneRIF: Regulation of neuroendocrine plasticity by the RNA-binding
            protein ZFP36L1.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Stoecklin,G., Colombi,M., Raineri,I., Leuenberger,S., Mallaun,M.,
            Schmidlin,M., Gross,B., Lu,M., Kitamura,T. and Moroni,C.
  TITLE     Functional cloning of BRF1, a regulator of ARE-dependent mRNA
            turnover
  JOURNAL   EMBO J 21 (17), 4709-4718 (2002)
   PUBMED   12198173
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Ning,Z.Q., Norton,J.D., Li,J. and Murphy,J.J.
  TITLE     Distinct mechanisms for rescue from apoptosis in Ramos human B
            cells by signaling through CD40 and interleukin-4 receptor: role
            for inhibition of an early response gene, Berg36
  JOURNAL   Eur J Immunol 26 (10), 2356-2363 (1996)
   PUBMED   8898945
REFERENCE   8  (residues 1 to 338)
  AUTHORS   Maclean,K.N., See,C.G., McKay,I.A. and Bustin,S.A.
  TITLE     The human immediate early gene BRF1 maps to chromosome 14q22-q24
  JOURNAL   Genomics 30 (1), 89-90 (1995)
   PUBMED   8595910
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Bustin,S.A., Nie,X.F., Barnard,R.C., Kumar,V., Pascall,J.C.,
            Brown,K.D., Leigh,I.M., Williams,N.S. and McKay,I.A.
  TITLE     Cloning and characterization of ERF-1, a human member of the Tis11
            family of early-response genes
  JOURNAL   DNA Cell Biol 13 (5), 449-459 (1994)
   PUBMED   8024689
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Barnard,R.C., Pascall,J.C., Brown,K.D., McKay,I.A., Williams,N.S.
            and Bustin,S.A.
  TITLE     Coding sequence of ERF-1, the human homologue of Tis11b/cMG1,
            members of the Tis11 family of early response genes
  JOURNAL   Nucleic Acids Res 21 (15), 3580 (1993)
   PUBMED   8346037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK024202.1, BC018340.1,
            BM712842.1, BQ894292.1, CN312799.1, DR423896.1, DB522201.1 and
            AI493871.1.
            
            On Oct 1, 2001 this sequence version replaced NP_004917.1.
            
            Summary: This gene is a member of the TIS11 family of early
            response genes, which are induced by various agonists such as the
            phorbol ester TPA and the polypeptide mitogen EGF. This gene is
            well conserved across species and has a promoter that contains
            motifs seen in other early-response genes. The encoded protein
            contains a distinguishing putative zinc finger domain with a
            repeating cys-his motif. This putative nuclear transcription factor
            most likely functions in regulating the response to growth factors.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes isoform 1. Variants 1 and 2 encode the same
            isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.246696.1,
                                           SRR11853567.9290.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000439696.3/ ENSP00000388402.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.1"
     Protein         1..338
                     /product="mRNA decay activator protein ZFP36L1 isoform 1"
                     /note="EGF-response factor 1; early response factor
                     Berg36; zinc finger protein, C3H type, 36-like 1; butyrate
                     response factor 1; zinc finger protein 36, C3H1 type-like
                     1; zinc finger protein 36, C3H type-like 1; ZFP36-like 1;
                     TPA-induced sequence 11b; mRNA decay activator protein
                     ZFP36L1; ZFP36 ring finger protein like 1"
                     /calculated_mol_wt=36183
     Region          1..111
                     /region_name="Necessary and sufficient for the association
                     with mRNA decay enzymes and mRNA decay activation.
                     /evidence=ECO:0000269|PubMed:15687258"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07352.1)"
     Region          1..106
                     /region_name="Tis11B_N"
                     /note="Tis11B like protein, N terminus; pfam04553"
                     /db_xref="CDD:461350"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK2.
                     /evidence=ECO:0000269|PubMed:18326031,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q07352.1)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:15538381; propagated from
                     UniProtKB/Swiss-Prot (Q07352.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1 and MAPKAPK2.
                     /evidence=ECO:0000269|PubMed:15538381,
                     ECO:0000269|PubMed:18326031; propagated from
                     UniProtKB/Swiss-Prot (Q07352.1)"
     Region          93..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07352.1)"
     Region          <115..>177
                     /region_name="CTH1"
                     /note="CCCH-type Zn-finger protein [General function
                     prediction only]; COG5063"
                     /db_xref="CDD:227395"
     Region          185..338
                     /region_name="Necessary for mRNA decay activation.
                     /evidence=ECO:0000269|PubMed:15687258"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07352.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1 and MAPKAPK2.
                     /evidence=ECO:0000269|PubMed:17030608,
                     ECO:0000269|PubMed:18326031; propagated from
                     UniProtKB/Swiss-Prot (Q07352.1)"
     Region          273..338
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07352.1)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q07352.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA1.
                     /evidence=ECO:0000269|PubMed:25106868; propagated from
                     UniProtKB/Swiss-Prot (Q07352.1)"
     CDS             1..338
                     /gene="ZFP36L1"
                     /gene_synonym="Berg36; BRF1; cMG1; ERF-1; ERF1; RNF162B;
                     TIS11B"
                     /coded_by="NM_004926.4:130..1146"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9791.1"
                     /db_xref="GeneID:677"
                     /db_xref="HGNC:HGNC:1107"
                     /db_xref="MIM:601064"
ORIGIN      
        1 mtttlvsati fdlsevlckg nkmlnysaps aggclldrka vgtpagggfp rrhsvtlpss
       61 kfhqnqllss lkgepapals srdsrfrdrs fseggerllp tqkqpgggqv nssryktelc
      121 rpfeengack ygdkcqfahg ihelrsltrh pkyktelcrt fhtigfcpyg prchfihnae
      181 erralagard lsadrprlqh sfsfagfpsa aataaatgll dsptsitppp ilsaddllgs
      241 ptlpdgtnnp fafssqelas lfapsmglpg ggspttflfr pmsesphmfd sppspqdsls
      301 dqegylssss sshsgsdspt ldnsrrlpif srlsisdd
//
LOCUS       NP_473454                187 aa            linear   PRI 27-NOV-2025
DEFINITION  calcium and integrin-binding family member 3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_473454
VERSION     NP_473454.1
DBSOURCE    REFSEQ: accession NM_054113.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Wang,X., Yi,Z., Shi,M. and Sun,Y.
  TITLE     The Diverse Functions of the Calcium- and Integrin-Binding Protein
            Family
  JOURNAL   Int J Mol Sci 26 (5), 2223 (2025)
   PUBMED   40076845
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Wijeratne,S.S., Marchan,M.F., Tresback,J.S. and Subramanian,R.
  TITLE     Atomic force microscopy reveals distinct protofilament-scale
            structural dynamics in depolymerizing microtubule arrays
  JOURNAL   Proc Natl Acad Sci U S A 119 (5) (2022)
   PUBMED   35101922
  REMARK    GeneRIF: Atomic force microscopy reveals distinct
            protofilament-scale structural dynamics in depolymerizing
            microtubule arrays.
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Liang,X., Qiu,X., Dionne,G., Cunningham,C.L., Pucak,M.L., Peng,G.,
            Kim,Y.H., Lauer,A., Shapiro,L. and Muller,U.
  TITLE     CIB2 and CIB3 are auxiliary subunits of the mechanotransduction
            channel of hair cells
  JOURNAL   Neuron 109 (13), 2131-2149 (2021)
   PUBMED   34089643
  REMARK    GeneRIF: CIB2 and CIB3 are auxiliary subunits of the
            mechanotransduction channel of hair cells.
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 187)
  AUTHORS   Huang,H., Bogstie,J.N. and Vogel,H.J.
  TITLE     Biophysical and structural studies of the human calcium- and
            integrin-binding protein family: understanding their functional
            similarities and differences
  JOURNAL   Biochem Cell Biol 90 (5), 646-656 (2012)
   PUBMED   22779914
  REMARK    GeneRIF: CIB3, as binding partners for the integrin alphaIIb
            subunit, which suggests that they are potentially involved in
            regulating integrin alphaIIb subunit activation.
REFERENCE   6  (residues 1 to 187)
  AUTHORS   Gentry,H.R., Singer,A.U., Betts,L., Yang,C., Ferrara,J.D.,
            Sondek,J. and Parise,L.V.
  TITLE     Structural and biochemical characterization of CIB1 delineates a
            new family of EF-hand-containing proteins
  JOURNAL   J Biol Chem 280 (9), 8407-8415 (2005)
   PUBMED   15574431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC112200.1, AB050868.1 and
            AW295492.1.
            
            Summary: This gene product shares a high degree of sequence
            similarity with DNA-dependent protein kinase catalytic
            subunit-interacting protein 2 in human and mouse, and like them may
            bind the catalytic subunit of DNA-dependent protein kinases. The
            exact function of this gene is not known. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jul
            2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC113591.1, AB050868.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000269878.8/ ENSP00000269878.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..187
                     /product="calcium and integrin-binding family member 3
                     isoform 1"
                     /note="DNA-dependent protein kinase catalytic
                     subunit-interacting protein 3"
                     /calculated_mol_wt=21671
     Region          107..174
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     CDS             1..187
                     /gene="CIB3"
                     /gene_synonym="KIP3"
                     /coded_by="NM_054113.4:51..614"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12340.1"
                     /db_xref="GeneID:117286"
                     /db_xref="HGNC:HGNC:24580"
                     /db_xref="MIM:610645"
ORIGIN      
        1 mgnkqtvfth eqleayqdct fftrkeimrl fyryqdlapq lvpldyttcp dvkvpyelig
       61 smpelkdnpf rqriaqvfse dgdghmtldn fldmfsvmse maprdlkayy afkiydfnnd
      121 dyicawdleq tvtkltrggl saeevslvce kvldeadgdh dgrlsledfq nmilrapdfl
      181 stfhiri
//
LOCUS       NP_001369232              98 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 40 isoform 10 [Homo sapiens].
ACCESSION   NP_001369232
VERSION     NP_001369232.1
DBSOURCE    REFSEQ: accession NM_001382303.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Mo,H., Li,R., Yang,N., Han,J., Xiao,X., Zhang,Y., Xiao,Z., Jiao,L.,
            Xu,Q. and Tu,K.
  TITLE     USP40 promotes hepatocellular carcinoma progression through a
            YAP/USP40 positive feedback loop
  JOURNAL   Cancer Lett 589, 216832 (2024)
   PUBMED   38537774
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma progression
            through a YAP/USP40 positive feedback loop.
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Wu,Q., Qiu,Y., Guo,J., Yuan,Z., Yang,Y., Zhu,Q., Zhang,Z., Guo,J.,
            Wu,Y., Zhang,J., Huang,D., Tu,K. and Hu,X.
  TITLE     USP40 promotes hepatocellular carcinoma cell proliferation,
            migration and stemness by deubiquitinating and stabilizing Claudin1
  JOURNAL   Biol Direct 19 (1), 13 (2024)
   PUBMED   38308285
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma cell
            proliferation, migration and stemness by deubiquitinating and
            stabilizing Claudin1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Miao,J., Li,L., Shaheen,N., Wei,J., Jacko,A.M., Sundd,P.,
            Taleb,S.J., Mallampalli,R.K., Zhao,Y. and Zhao,J.
  TITLE     The deubiquitinase USP40 preserves endothelial integrity by
            targeting the heat shock protein HSP90beta
  JOURNAL   Exp Mol Med 56 (2), 395-407 (2024)
   PUBMED   38307937
REFERENCE   4  (residues 1 to 98)
  AUTHORS   Takahashi,S., Fukuhara,D., Kimura,T., Fukutomi,T., Tanaka,E.,
            Mikami,N., Hada,I., Takematsu,H., Nishibori,Y., Akimoto,Y.,
            Kiyonari,H., Abe,T., Huber,O. and Yan,K.
  TITLE     USP40 deubiquitinates HINT1 and stabilizes p53 in podocyte damage
  JOURNAL   Biochem Biophys Res Commun 614, 198-206 (2022)
   PUBMED   35605301
REFERENCE   5  (residues 1 to 98)
  AUTHORS   An,W., Yao,S., Sun,X., Hou,Z., Lin,Y., Su,L. and Liu,X.
  TITLE     Glucocorticoid modulatory element-binding protein 1 (GMEB1)
            interacts with the de-ubiquitinase USP40 to stabilize CFLARL and
            inhibit apoptosis in human non-small cell lung cancer cells
  JOURNAL   J Exp Clin Cancer Res 38 (1), 181 (2019)
   PUBMED   31046799
  REMARK    GeneRIF: Our findings show the de-ubiquitinase USP40 regulates the
            ubiquitination and degradation of CFLARL; and GMEB1 acts as a
            bridge protein for USP40 and CFLARL. Mechanistically, we found
            GMEB1 inhibits the activation of CASP8 by modulating ubiquitination
            and degradation of CFLARL
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 98)
  AUTHORS   Li,Y., Schrodi,S., Rowland,C., Tacey,K., Catanese,J. and Grupe,A.
  TITLE     Genetic evidence for ubiquitin-specific proteases USP24 and USP40
            as candidate genes for late-onset Parkinson disease
  JOURNAL   Hum Mutat 27 (10), 1017-1023 (2006)
   PUBMED   16917932
  REMARK    GeneRIF: Da suggest that genetic variants in USP40 affect the risk
            for late-onset Parkinson disease (PD), which is consistent with the
            predicted role of the ubiquitination pathway in PD etiology.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 98)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   8  (residues 1 to 98)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   9  (residues 1 to 98)
  AUTHORS   Bass,B.L.
  TITLE     RNA editing by adenosine deaminases that act on RNA
  JOURNAL   Annu Rev Biochem 71, 817-846 (2002)
   PUBMED   12045112
  REMARK    Review article
REFERENCE   10 (residues 1 to 98)
  AUTHORS   Chen,X., Zhang,Y., Douglas,L. and Zhou,P.
  TITLE     UV-damaged DNA-binding proteins are targets of CUL-4A-mediated
            ubiquitination and degradation
  JOURNAL   J Biol Chem 276 (51), 48175-48182 (2001)
   PUBMED   11673459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019072.8.
            
            Summary: Modification of cellular proteins by ubiquitin is an
            essential regulatory mechanism controlled by the coordinated action
            of multiple ubiquitin-conjugating and deubiquitinating enzymes.
            USP40 belongs to a large family of cysteine proteases that function
            as deubiquitinating enzymes (Quesada et al., 2004 [PubMed
            14715245]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU738706.1, BM701644.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..98
                     /product="ubiquitin carboxyl-terminal hydrolase 40 isoform
                     10"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 40; ubiquitin
                     carboxyl-terminal hydrolase 40;
                     ubiquitin-specific-processing protease 40;
                     deubiquitinating enzyme 40; ubiquitin thioesterase 40;
                     ubiquitin thiolesterase 40"
                     /calculated_mol_wt=10956
     Region          39..>92
                     /region_name="Peptidase_C19"
                     /note="Peptidase C19 contains ubiquitinyl hydrolases. They
                     are intracellular peptidases that remove ubiquitin
                     molecules from polyubiquinated peptides by cleavage of
                     isopeptide bonds. They hydrolyse bonds involving the
                     carboxyl group of the C-terminal Gly...; cl02553"
                     /db_xref="CDD:470612"
     CDS             1..98
                     /gene="USP40"
                     /coded_by="NM_001382303.1:119..415"
                     /note="isoform 10 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS92973.1"
                     /db_xref="GeneID:55230"
                     /db_xref="HGNC:HGNC:20069"
                     /db_xref="MIM:610570"
ORIGIN      
        1 mfgdlfeeey stvsnnqygk gkklktkale ppapreftnl sgirnqggtc ylnsllqtlh
       61 ftpefrealf slgpeelglf edkdkpdakk vtwpipyg
//
LOCUS       NP_001243657             462 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 39 isoform 4 [Homo sapiens].
ACCESSION   NP_001243657
VERSION     NP_001243657.1
DBSOURCE    REFSEQ: accession NM_001256728.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Zhou,F., Li,X., Sun,Y., Wang,Y., Niu,K., Gao,X., Zhang,J., Chen,T.,
            Li,Y., Zhao,W., Mao,B., Xu,Q., Shi,Y. and He,Z.
  TITLE     USP39 at the crossroads of cancer immunity: regulating immune
            evasion and immunotherapy response through RNA splicing and
            ubiquitin signaling
  JOURNAL   Front Immunol 16, 1665775 (2025)
   PUBMED   40990019
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Lu,C., Cai,Y., Wu,S., Wang,Y., Li,J.B., Xu,G. and Ma,J.
  TITLE     Deubiquitinating enzyme USP39 promotes the growth and metastasis of
            gastric cancer cells by modulating the degradation of RNA-binding
            protein RBM39
  JOURNAL   J Biol Chem 300 (10), 107751 (2024)
   PUBMED   39260689
  REMARK    GeneRIF: Deubiquitinating enzyme USP39 promotes the growth and
            metastasis of gastric cancer cells by modulating the degradation of
            RNA-binding protein RBM39.
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Hu,Y., Wang,Y., Hu,W., Hu,C., Wang,B., Liu,C., Deng,A., Shen,B.,
            Wu,K. and Liu,Y.
  TITLE     USP39 Promotes the Viability and Migration of Head and Neck
            Squamous Cell Carcinoma Cell by Regulating STAT1
  JOURNAL   Technol Cancer Res Treat 23, 15330338241250298 (2024)
   PUBMED   38706215
  REMARK    GeneRIF: USP39 Promotes the Viability and Migration of Head and
            Neck Squamous Cell Carcinoma Cell by Regulating STAT1.
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   7  (residues 1 to 462)
  AUTHORS   van Leuken,R.J., Luna-Vargas,M.P., Sixma,T.K., Wolthuis,R.M. and
            Medema,R.H.
  TITLE     Usp39 is essential for mitotic spindle checkpoint integrity and
            controls mRNA-levels of aurora B
  JOURNAL   Cell Cycle 7 (17), 2710-2719 (2008)
   PUBMED   18728397
  REMARK    GeneRIF: These observations suggest Usp39 to be involved in
            splicing of Aurora B and other mRNAs that are essential for proper
            spindle checkpoint function.
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Makarova,O.V., Makarov,E.M. and Luhrmann,R.
  TITLE     The 65 and 110 kDa SR-related proteins of the U4/U6.U5 tri-snRNP
            are essential for the assembly of mature spliceosomes
  JOURNAL   EMBO J 20 (10), 2553-2563 (2001)
   PUBMED   11350945
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Lygerou,Z., Christophides,G. and Seraphin,B.
  TITLE     A novel genetic screen for snRNP assembly factors in yeast
            identifies a conserved protein, Sad1p, also required for pre-mRNA
            splicing
  JOURNAL   Mol Cell Biol 19 (3), 2008-2020 (1999)
   PUBMED   10022888
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK295257.1, AF161450.1 and BC001384.2.
            
            Transcript Variant: This variant (5) differs in the 5' UTR, lacks a
            portion of the 5' coding region, initiates translation at an
            alternate start codon, and lacks an in-frame exon in the 5' coding
            region, compared to variant 1. The encoded isoform (4) is shorter
            and has a distinct N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295257.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p11.2"
     Protein         1..462
                     /product="ubiquitin carboxyl-terminal hydrolase 39 isoform
                     4"
                     /EC_number="3.4.19.12"
                     /note="SnRNP assembly defective 1 homolog; small nuclear
                     ribonucleoprotein 65kDa (U4/U6.U5); ubiquitin specific
                     protease 39; U4/U6.U5 tri-snRNP-associated protein 2;
                     U4/U6.U5 tri-snRNP-associated 65 kDa protein; SAD1
                     homolog; inactive ubiquitin-specific peptidase 39;
                     ubiquitin carboxyl-terminal hydrolase 39"
                     /calculated_mol_wt=53379
     Region          28..450
                     /region_name="Peptidase_C19M"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02669"
                     /db_xref="CDD:239134"
     Site            order(126,131,410,428)
                     /site_type="active"
                     /db_xref="CDD:239134"
     CDS             1..462
                     /gene="USP39"
                     /gene_synonym="65K; CGI-21; HSPC332; SAD1; SNRNP65"
                     /coded_by="NM_001256728.2:222..1610"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS58716.1"
                     /db_xref="GeneID:10713"
                     /db_xref="HGNC:HGNC:20071"
                     /db_xref="MIM:611594"
ORIGIN      
        1 mltavpshlf sakngrvdse drrsrhcpyl dtinsfspfp tgrglkshay ihsvqfshhv
       61 flnlhtlkfy clpdnyeiid ssledityvl kptftkqqia nldkqaklsr aydgttylpg
      121 ivglnnikan dyanavlqal snvpplrnyf leednyknik rppgdimfll vqrfgelmrk
      181 lwnprnfkah vsphemlqav vlcskktfqi tkqgdgvdfl swflnalhsa lggtkkkkkt
      241 ivtdvfqgsm riftkklphp dlpaeekeql lhndeyqetm vestfmyltl dlptaplykd
      301 ekeqliipqv plfnilakfn gitekeykty kenflkrfql tklppylifc ikrftknnff
      361 veknptivnf pitnvdlrey lseevqavhk nttydliani vhdgkpsegs yrihvlhhgt
      421 gkwyelqdlq vtdilpqmit lseayiqiwk rrdndetnqq ga
//
LOCUS       NP_001369229            1071 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 40 isoform 7 [Homo sapiens].
ACCESSION   NP_001369229
VERSION     NP_001369229.1
DBSOURCE    REFSEQ: accession NM_001382300.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1071)
  AUTHORS   Mo,H., Li,R., Yang,N., Han,J., Xiao,X., Zhang,Y., Xiao,Z., Jiao,L.,
            Xu,Q. and Tu,K.
  TITLE     USP40 promotes hepatocellular carcinoma progression through a
            YAP/USP40 positive feedback loop
  JOURNAL   Cancer Lett 589, 216832 (2024)
   PUBMED   38537774
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma progression
            through a YAP/USP40 positive feedback loop.
REFERENCE   2  (residues 1 to 1071)
  AUTHORS   Wu,Q., Qiu,Y., Guo,J., Yuan,Z., Yang,Y., Zhu,Q., Zhang,Z., Guo,J.,
            Wu,Y., Zhang,J., Huang,D., Tu,K. and Hu,X.
  TITLE     USP40 promotes hepatocellular carcinoma cell proliferation,
            migration and stemness by deubiquitinating and stabilizing Claudin1
  JOURNAL   Biol Direct 19 (1), 13 (2024)
   PUBMED   38308285
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma cell
            proliferation, migration and stemness by deubiquitinating and
            stabilizing Claudin1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1071)
  AUTHORS   Miao,J., Li,L., Shaheen,N., Wei,J., Jacko,A.M., Sundd,P.,
            Taleb,S.J., Mallampalli,R.K., Zhao,Y. and Zhao,J.
  TITLE     The deubiquitinase USP40 preserves endothelial integrity by
            targeting the heat shock protein HSP90beta
  JOURNAL   Exp Mol Med 56 (2), 395-407 (2024)
   PUBMED   38307937
REFERENCE   4  (residues 1 to 1071)
  AUTHORS   Takahashi,S., Fukuhara,D., Kimura,T., Fukutomi,T., Tanaka,E.,
            Mikami,N., Hada,I., Takematsu,H., Nishibori,Y., Akimoto,Y.,
            Kiyonari,H., Abe,T., Huber,O. and Yan,K.
  TITLE     USP40 deubiquitinates HINT1 and stabilizes p53 in podocyte damage
  JOURNAL   Biochem Biophys Res Commun 614, 198-206 (2022)
   PUBMED   35605301
REFERENCE   5  (residues 1 to 1071)
  AUTHORS   An,W., Yao,S., Sun,X., Hou,Z., Lin,Y., Su,L. and Liu,X.
  TITLE     Glucocorticoid modulatory element-binding protein 1 (GMEB1)
            interacts with the de-ubiquitinase USP40 to stabilize CFLARL and
            inhibit apoptosis in human non-small cell lung cancer cells
  JOURNAL   J Exp Clin Cancer Res 38 (1), 181 (2019)
   PUBMED   31046799
  REMARK    GeneRIF: Our findings show the de-ubiquitinase USP40 regulates the
            ubiquitination and degradation of CFLARL; and GMEB1 acts as a
            bridge protein for USP40 and CFLARL. Mechanistically, we found
            GMEB1 inhibits the activation of CASP8 by modulating ubiquitination
            and degradation of CFLARL
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1071)
  AUTHORS   Li,Y., Schrodi,S., Rowland,C., Tacey,K., Catanese,J. and Grupe,A.
  TITLE     Genetic evidence for ubiquitin-specific proteases USP24 and USP40
            as candidate genes for late-onset Parkinson disease
  JOURNAL   Hum Mutat 27 (10), 1017-1023 (2006)
   PUBMED   16917932
  REMARK    GeneRIF: Da suggest that genetic variants in USP40 affect the risk
            for late-onset Parkinson disease (PD), which is consistent with the
            predicted role of the ubiquitination pathway in PD etiology.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1071)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   8  (residues 1 to 1071)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   9  (residues 1 to 1071)
  AUTHORS   Bass,B.L.
  TITLE     RNA editing by adenosine deaminases that act on RNA
  JOURNAL   Annu Rev Biochem 71, 817-846 (2002)
   PUBMED   12045112
  REMARK    Review article
REFERENCE   10 (residues 1 to 1071)
  AUTHORS   Chen,X., Zhang,Y., Douglas,L. and Zhou,P.
  TITLE     UV-damaged DNA-binding proteins are targets of CUL-4A-mediated
            ubiquitination and degradation
  JOURNAL   J Biol Chem 276 (51), 48175-48182 (2001)
   PUBMED   11673459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019072.8 and AC019221.4.
            
            Summary: Modification of cellular proteins by ubiquitin is an
            essential regulatory mechanism controlled by the coordinated action
            of multiple ubiquitin-conjugating and deubiquitinating enzymes.
            USP40 belongs to a large family of cysteine proteases that function
            as deubiquitinating enzymes (Quesada et al., 2004 [PubMed
            14715245]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4544380.1,
                                           SRR14038196.622721.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1071
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..1071
                     /product="ubiquitin carboxyl-terminal hydrolase 40 isoform
                     7"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 40; ubiquitin
                     carboxyl-terminal hydrolase 40;
                     ubiquitin-specific-processing protease 40;
                     deubiquitinating enzyme 40; ubiquitin thioesterase 40;
                     ubiquitin thiolesterase 40"
                     /calculated_mol_wt=121225
     Region          39..344
                     /region_name="peptidase_C19C"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02659"
                     /db_xref="CDD:239124"
     Site            order(45,50,305,323)
                     /site_type="active"
                     /db_xref="CDD:239124"
     CDS             1..1071
                     /gene="USP40"
                     /coded_by="NM_001382300.1:119..3334"
                     /note="isoform 7 is encoded by transcript variant 8"
                     /db_xref="GeneID:55230"
                     /db_xref="HGNC:HGNC:20069"
                     /db_xref="MIM:610570"
ORIGIN      
        1 mfgdlfeeey stvsnnqygk gkklktkale ppapreftnl sgirnqggtc ylnsllqtlh
       61 ftpefrealf slgpeelglf edkdkpdakv riiplqlqrl faqlllldqe aastadltds
      121 fgwtsneemr qhdvqelnri lfsaletslv gtsghdliyr lyhgtivnqi vckecknvse
      181 rqedfldltv avknvsgled alwnmyveee vfdcdnlyhc gtcdrlvkaa ksaklrklpp
      241 fltvsllrfn fdfvkceryk etscytfplr inlkpfceqs elddleyiyd lfsviihkgg
      301 cygghyhvyi kdvdhlgnwq fqeekskpdv nlkdlqseee idhplmilka illeeennli
      361 pvdqlgqkll kkigiswnkk yrkqhgplrk flqlhsqifl lssdestvrl lknsslqaes
      421 dfqrndqqif kmlppespgl nnsiscphwf dindskvqpi rekdieqqfq gkesaymlfy
      481 rksqlqrppe aranprygvp chllnemdaa nielqtkrae cdsanntfel hlhlgpqyhf
      541 fngalhpvvs qtesvwdltf dkrktlgdlr qsifqllefw egdmvlsvak lvpaglhiyq
      601 slggdeltlc eteiadgedi fvwngvevgg vhiqtgidce plllnvlhld tssdgekccq
      661 viesphvfpa naevgtvlta laipagvifi nsagcpggeg wtaipkedmr ktfreqglrn
      721 gssiliqdsh ddnslltkee kwvtsmneid wlhvknlcql eseekqvkis atvntmvfdi
      781 rikaikelkl mkeladnscl rpidrngkll cpvpdsytlk eaelkmgssl glclgkapss
      841 sqlflffamg sdvqpgteme ivveetisvr dclklmlkks glqgdawhlr kmdwcyeage
      901 plceedatlk ellicsgdtl lliegqlppl gflkvpiwwy qlqgpsghwe shqdqtncts
      961 swgrvwrats sqgasgnepa qvsllylgdi eisedatlae lksqamtlpp flefgvpspa
     1021 hlrawtverk rpgrllrtdr qplreyklgr rieicleplq kgenlgcilt p
//
LOCUS       NP_001369225            1256 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 40 isoform 3 [Homo sapiens].
ACCESSION   NP_001369225
VERSION     NP_001369225.1
DBSOURCE    REFSEQ: accession NM_001382296.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1256)
  AUTHORS   Mo,H., Li,R., Yang,N., Han,J., Xiao,X., Zhang,Y., Xiao,Z., Jiao,L.,
            Xu,Q. and Tu,K.
  TITLE     USP40 promotes hepatocellular carcinoma progression through a
            YAP/USP40 positive feedback loop
  JOURNAL   Cancer Lett 589, 216832 (2024)
   PUBMED   38537774
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma progression
            through a YAP/USP40 positive feedback loop.
REFERENCE   2  (residues 1 to 1256)
  AUTHORS   Wu,Q., Qiu,Y., Guo,J., Yuan,Z., Yang,Y., Zhu,Q., Zhang,Z., Guo,J.,
            Wu,Y., Zhang,J., Huang,D., Tu,K. and Hu,X.
  TITLE     USP40 promotes hepatocellular carcinoma cell proliferation,
            migration and stemness by deubiquitinating and stabilizing Claudin1
  JOURNAL   Biol Direct 19 (1), 13 (2024)
   PUBMED   38308285
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma cell
            proliferation, migration and stemness by deubiquitinating and
            stabilizing Claudin1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1256)
  AUTHORS   Miao,J., Li,L., Shaheen,N., Wei,J., Jacko,A.M., Sundd,P.,
            Taleb,S.J., Mallampalli,R.K., Zhao,Y. and Zhao,J.
  TITLE     The deubiquitinase USP40 preserves endothelial integrity by
            targeting the heat shock protein HSP90beta
  JOURNAL   Exp Mol Med 56 (2), 395-407 (2024)
   PUBMED   38307937
REFERENCE   4  (residues 1 to 1256)
  AUTHORS   Takahashi,S., Fukuhara,D., Kimura,T., Fukutomi,T., Tanaka,E.,
            Mikami,N., Hada,I., Takematsu,H., Nishibori,Y., Akimoto,Y.,
            Kiyonari,H., Abe,T., Huber,O. and Yan,K.
  TITLE     USP40 deubiquitinates HINT1 and stabilizes p53 in podocyte damage
  JOURNAL   Biochem Biophys Res Commun 614, 198-206 (2022)
   PUBMED   35605301
REFERENCE   5  (residues 1 to 1256)
  AUTHORS   An,W., Yao,S., Sun,X., Hou,Z., Lin,Y., Su,L. and Liu,X.
  TITLE     Glucocorticoid modulatory element-binding protein 1 (GMEB1)
            interacts with the de-ubiquitinase USP40 to stabilize CFLARL and
            inhibit apoptosis in human non-small cell lung cancer cells
  JOURNAL   J Exp Clin Cancer Res 38 (1), 181 (2019)
   PUBMED   31046799
  REMARK    GeneRIF: Our findings show the de-ubiquitinase USP40 regulates the
            ubiquitination and degradation of CFLARL; and GMEB1 acts as a
            bridge protein for USP40 and CFLARL. Mechanistically, we found
            GMEB1 inhibits the activation of CASP8 by modulating ubiquitination
            and degradation of CFLARL
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1256)
  AUTHORS   Li,Y., Schrodi,S., Rowland,C., Tacey,K., Catanese,J. and Grupe,A.
  TITLE     Genetic evidence for ubiquitin-specific proteases USP24 and USP40
            as candidate genes for late-onset Parkinson disease
  JOURNAL   Hum Mutat 27 (10), 1017-1023 (2006)
   PUBMED   16917932
  REMARK    GeneRIF: Da suggest that genetic variants in USP40 affect the risk
            for late-onset Parkinson disease (PD), which is consistent with the
            predicted role of the ubiquitination pathway in PD etiology.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1256)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   8  (residues 1 to 1256)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   9  (residues 1 to 1256)
  AUTHORS   Bass,B.L.
  TITLE     RNA editing by adenosine deaminases that act on RNA
  JOURNAL   Annu Rev Biochem 71, 817-846 (2002)
   PUBMED   12045112
  REMARK    Review article
REFERENCE   10 (residues 1 to 1256)
  AUTHORS   Chen,X., Zhang,Y., Douglas,L. and Zhou,P.
  TITLE     UV-damaged DNA-binding proteins are targets of CUL-4A-mediated
            ubiquitination and degradation
  JOURNAL   J Biol Chem 276 (51), 48175-48182 (2001)
   PUBMED   11673459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019072.8 and AC019221.4.
            
            Summary: Modification of cellular proteins by ubiquitin is an
            essential regulatory mechanism controlled by the coordinated action
            of multiple ubiquitin-conjugating and deubiquitinating enzymes.
            USP40 belongs to a large family of cysteine proteases that function
            as deubiquitinating enzymes (Quesada et al., 2004 [PubMed
            14715245]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (4) encodes the longest isoform
            (3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.195158.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..1256
                     /product="ubiquitin carboxyl-terminal hydrolase 40 isoform
                     3"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 40; ubiquitin
                     carboxyl-terminal hydrolase 40;
                     ubiquitin-specific-processing protease 40;
                     deubiquitinating enzyme 40; ubiquitin thioesterase 40;
                     ubiquitin thiolesterase 40"
                     /calculated_mol_wt=142266
     Region          39..344
                     /region_name="peptidase_C19C"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02659"
                     /db_xref="CDD:239124"
     Site            order(45,50,305,323)
                     /site_type="active"
                     /db_xref="CDD:239124"
     Region          1201..1256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVE5.3)"
     CDS             1..1256
                     /gene="USP40"
                     /coded_by="NM_001382296.1:119..3889"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:55230"
                     /db_xref="HGNC:HGNC:20069"
                     /db_xref="MIM:610570"
ORIGIN      
        1 mfgdlfeeey stvsnnqygk gkklktkale ppapreftnl sgirnqggtc ylnsllqtlh
       61 ftpefrealf slgpeelglf edkdkpdakv riiplqlqrl faqlllldqe aastadltds
      121 fgwtsneemr qhdvqelnri lfsaletslv gtsghdliyr lyhgtivnqi vckecknvse
      181 rqedfldltv avknvsgled alwnmyveee vfdcdnlyhc gtcdrlvkaa ksaklrklpp
      241 fltvsllrfn fdfvkceryk etscytfplr inlkpfceqs elddleyiyd lfsviihkgg
      301 cygghyhvyi kdvdhlgnwq fqeekskpdv nlkdlqseee idhplmilka illeeennli
      361 pvdqlgqkll kkigiswnkk yrkqhgplrk flqlhsqifl lssdestvrl lknsslqaes
      421 dfqrndqqif kmlppespgl nnsiscphwf dindskvqpi rekdieqqfq gkesaymlfy
      481 rksqlqrppe aranprygvp chllnemdaa nielqtkrae cdsanntfel hlhlgpqyhf
      541 fngalhpvvs qtesvwdltf dkrktlgdlr qsifqllefw egdmvlsvak lvpaglhiyq
      601 slggdeltlc eteiadgedi fvwngvevgg vhiqtgidce plllnvlhld tssdgekccq
      661 viesphvfpa naevgtvlta laipagvifi nsagcpggeg wtaipkedmr ktfreqglrn
      721 gssiliqdsh ddnslltkee kwvtsmneid wlhvknlcql eseekqvkis atvntmvfdi
      781 rikaikelkl mkeladnscl rpidrngkll cpvpdsytlk eaelkmgssl glclgkapss
      841 sqlflffamg sdvqpgteme ivveetisvr dclklmlkks glqgdawhlr kmdwcyeage
      901 plceensars qlitlgtgfs fqpcqdatlk ellicsgdtl lliegqlppl gflkvpiwwy
      961 qlqgpsghwe shqdqtncts swgrvwrats sqgasgnepa qvsllylgdi eisedatlae
     1021 lksqamtlpp flefgvpspa hlrawtverk rpgrllrtdr qplreyklgr rieicleplq
     1081 kgenlgpqdv llrtqvripg ertyapaldl vwnaaqggta gslrqrvadf yrlpvekiei
     1141 akyfpekfew lpisswnqqi tkrkkkkkqd ylqgapyylk dgdtigvknl lidddddfst
     1201 irddtgkekq kqralgrrks qealheqssy ilssaetpar prapetslsi hvgsfr
//
LOCUS       NP_001369227            1145 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 40 isoform 5 [Homo sapiens].
ACCESSION   NP_001369227
VERSION     NP_001369227.1
DBSOURCE    REFSEQ: accession NM_001382298.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1145)
  AUTHORS   Mo,H., Li,R., Yang,N., Han,J., Xiao,X., Zhang,Y., Xiao,Z., Jiao,L.,
            Xu,Q. and Tu,K.
  TITLE     USP40 promotes hepatocellular carcinoma progression through a
            YAP/USP40 positive feedback loop
  JOURNAL   Cancer Lett 589, 216832 (2024)
   PUBMED   38537774
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma progression
            through a YAP/USP40 positive feedback loop.
REFERENCE   2  (residues 1 to 1145)
  AUTHORS   Wu,Q., Qiu,Y., Guo,J., Yuan,Z., Yang,Y., Zhu,Q., Zhang,Z., Guo,J.,
            Wu,Y., Zhang,J., Huang,D., Tu,K. and Hu,X.
  TITLE     USP40 promotes hepatocellular carcinoma cell proliferation,
            migration and stemness by deubiquitinating and stabilizing Claudin1
  JOURNAL   Biol Direct 19 (1), 13 (2024)
   PUBMED   38308285
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma cell
            proliferation, migration and stemness by deubiquitinating and
            stabilizing Claudin1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1145)
  AUTHORS   Miao,J., Li,L., Shaheen,N., Wei,J., Jacko,A.M., Sundd,P.,
            Taleb,S.J., Mallampalli,R.K., Zhao,Y. and Zhao,J.
  TITLE     The deubiquitinase USP40 preserves endothelial integrity by
            targeting the heat shock protein HSP90beta
  JOURNAL   Exp Mol Med 56 (2), 395-407 (2024)
   PUBMED   38307937
REFERENCE   4  (residues 1 to 1145)
  AUTHORS   Takahashi,S., Fukuhara,D., Kimura,T., Fukutomi,T., Tanaka,E.,
            Mikami,N., Hada,I., Takematsu,H., Nishibori,Y., Akimoto,Y.,
            Kiyonari,H., Abe,T., Huber,O. and Yan,K.
  TITLE     USP40 deubiquitinates HINT1 and stabilizes p53 in podocyte damage
  JOURNAL   Biochem Biophys Res Commun 614, 198-206 (2022)
   PUBMED   35605301
REFERENCE   5  (residues 1 to 1145)
  AUTHORS   An,W., Yao,S., Sun,X., Hou,Z., Lin,Y., Su,L. and Liu,X.
  TITLE     Glucocorticoid modulatory element-binding protein 1 (GMEB1)
            interacts with the de-ubiquitinase USP40 to stabilize CFLARL and
            inhibit apoptosis in human non-small cell lung cancer cells
  JOURNAL   J Exp Clin Cancer Res 38 (1), 181 (2019)
   PUBMED   31046799
  REMARK    GeneRIF: Our findings show the de-ubiquitinase USP40 regulates the
            ubiquitination and degradation of CFLARL; and GMEB1 acts as a
            bridge protein for USP40 and CFLARL. Mechanistically, we found
            GMEB1 inhibits the activation of CASP8 by modulating ubiquitination
            and degradation of CFLARL
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1145)
  AUTHORS   Li,Y., Schrodi,S., Rowland,C., Tacey,K., Catanese,J. and Grupe,A.
  TITLE     Genetic evidence for ubiquitin-specific proteases USP24 and USP40
            as candidate genes for late-onset Parkinson disease
  JOURNAL   Hum Mutat 27 (10), 1017-1023 (2006)
   PUBMED   16917932
  REMARK    GeneRIF: Da suggest that genetic variants in USP40 affect the risk
            for late-onset Parkinson disease (PD), which is consistent with the
            predicted role of the ubiquitination pathway in PD etiology.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1145)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   8  (residues 1 to 1145)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   9  (residues 1 to 1145)
  AUTHORS   Bass,B.L.
  TITLE     RNA editing by adenosine deaminases that act on RNA
  JOURNAL   Annu Rev Biochem 71, 817-846 (2002)
   PUBMED   12045112
  REMARK    Review article
REFERENCE   10 (residues 1 to 1145)
  AUTHORS   Chen,X., Zhang,Y., Douglas,L. and Zhou,P.
  TITLE     UV-damaged DNA-binding proteins are targets of CUL-4A-mediated
            ubiquitination and degradation
  JOURNAL   J Biol Chem 276 (51), 48175-48182 (2001)
   PUBMED   11673459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019072.8 and AC019221.4.
            
            Summary: Modification of cellular proteins by ubiquitin is an
            essential regulatory mechanism controlled by the coordinated action
            of multiple ubiquitin-conjugating and deubiquitinating enzymes.
            USP40 belongs to a large family of cysteine proteases that function
            as deubiquitinating enzymes (Quesada et al., 2004 [PubMed
            14715245]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1145
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..1145
                     /product="ubiquitin carboxyl-terminal hydrolase 40 isoform
                     5"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 40; ubiquitin
                     carboxyl-terminal hydrolase 40;
                     ubiquitin-specific-processing protease 40;
                     deubiquitinating enzyme 40; ubiquitin thioesterase 40;
                     ubiquitin thiolesterase 40"
                     /calculated_mol_wt=129287
     Region          39..392
                     /region_name="Peptidase_C19"
                     /note="Peptidase C19 contains ubiquitinyl hydrolases. They
                     are intracellular peptidases that remove ubiquitin
                     molecules from polyubiquinated peptides by cleavage of
                     isopeptide bonds. They hydrolyse bonds involving the
                     carboxyl group of the C-terminal Gly...; cl02553"
                     /db_xref="CDD:470612"
     CDS             1..1145
                     /gene="USP40"
                     /coded_by="NM_001382298.1:456..3893"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:55230"
                     /db_xref="HGNC:HGNC:20069"
                     /db_xref="MIM:610570"
ORIGIN      
        1 mfgdlfeeey stvsnnqygk gkklktkale ppapreftnl sgirnqggtc ylnsllqtlh
       61 ftpefrealf slgpeelglf edkdkpdakv riiplqlqrl faqlllldqe aastadltds
      121 fgwtsneemr qhdvqelnri lfsaletslv gtsghdliyr lyhgtivnqi vckecknvse
      181 rqedfldltv avknvsgled alwnmyveee vfdcdnlyhc gtcdrlvkaa keekskpdvn
      241 lkdlqseeei dhplmilkai lleeennlip vdqlgqkllk kigiswnkky rkqhgplrkf
      301 lqlhsqifll ssdestvrll knsslqaesd fqrndqqifk mlppespgln nsiscphwfd
      361 indskvqpir ekdieqqfqg kesaymlfyr ksqlqrppea ranprygvpc hllnemdaan
      421 ielqtkraec dsanntfelh lhlgpqyhff ngalhpvvsq tesvwdltfd krktlgdlrq
      481 sifqllefwe gdmvlsvakl vpaglhiyqs lggdeltlce teiadgedif vwngvevggv
      541 hiqtgidcep lllnvlhldt ssdgekccqv iesphvfpan aevgtvltal aipagvifin
      601 sagcpggegw taipkedmrk tfreqglrng ssiliqdshd dnslltkeek wvtsmneidw
      661 lhvknlcqle seekqvkisa tvntmvfdir ikaikelklm keladnsclr pidrngkllc
      721 pvpdsytlke aelkmgsslg lclgkapsss qlflffamgs dvqpgtemei vveetisvrd
      781 clklmlkksg lqgdawhlrk mdwcyeagep lceedatlke llicsgdtll liegqlpplg
      841 flkvpiwwyq lqgpsghwes hqdqtnctss wgrvwratss qgasgnepaq vsllylgdie
      901 isedatlael ksqamtlppf lefgvpspah lrawtverkr pgrllrtdrq plreyklgrr
      961 ieicleplqk genlgpqdvl lrtqvripge rtyapaldlv wnaaqggtag slrqrvadfy
     1021 rlpvekieia kyfpekfewl pisswnqqit krkkkkkqdy lqgapyylkd gdtigvknll
     1081 idddddfsti rddtgkekqk qralgrrksq ealheqssyi lssaetparp rapetslsih
     1141 vgsfr
//
LOCUS       NP_073743                366 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 46 isoform 1 [Homo sapiens].
ACCESSION   NP_073743
VERSION     NP_073743.2
DBSOURCE    REFSEQ: accession NM_022832.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Yu,K., Wang,G.M., Guo,S.S., Bassermann,F. and Fassler,R.
  TITLE     The USP12/46 deubiquitinases protect integrins from ESCRT-mediated
            lysosomal degradation
  JOURNAL   EMBO Rep 25 (12), 5687-5718 (2024)
   PUBMED   39506038
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Jiang,L., Qi,X., Lai,M., Zhou,J., Yuan,M., You,J., Liu,Q., Pan,J.,
            Zhao,L., Ying,M., Ji,J., Li,K., Zhang,Y., Pan,W., He,Q., Yang,B.
            and Cao,J.
  TITLE     WDR20 prevents hepatocellular carcinoma senescence by orchestrating
            the simultaneous USP12/46-mediated deubiquitination of c-Myc
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2407904121 (2024)
   PUBMED   39432777
  REMARK    GeneRIF: WDR20 prevents hepatocellular carcinoma senescence by
            orchestrating the simultaneous USP12/46-mediated deubiquitination
            of c-Myc.
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Ng,V.H., Spencer,Z., Neitzel,L.R., Nayak,A., Loberg,M.A., Shen,C.,
            Kassel,S.N., Kroh,H.K., An,Z., Anthony,C.C., Bryant,J.M.,
            Lawson,A., Goldsmith,L., Benchabane,H., Hansen,A.G., Li,J.,
            D'Souza,S., Lebensohn,A.M., Rohatgi,R., Weiss,W.A., Weiss,V.L.,
            Williams,C., Hong,C.C., Robbins,D.J., Ahmed,Y. and Lee,E.
  TITLE     The USP46 complex deubiquitylates LRP6 to promote Wnt/beta-catenin
            signaling
  JOURNAL   Nat Commun 14 (1), 6173 (2023)
   PUBMED   37798301
  REMARK    GeneRIF: The USP46 complex deubiquitylates LRP6 to promote
            Wnt/beta-catenin signaling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Ke,L., Jia,Z., Gao,W. and Luo,L.
  TITLE     Ubiquitin specific protease 46 potentiates triple negative breast
            cancer development by stabilizing PGAM1-mediated glycolysis
  JOURNAL   Cell Biol Int 47 (1), 41-51 (2023)
   PUBMED   36335636
  REMARK    GeneRIF: Ubiquitin specific protease 46 potentiates triple negative
            breast cancer development by stabilizing PGAM1-mediated glycolysis.
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Cohn,M.A., Kee,Y., Haas,W., Gygi,S.P. and D'Andrea,A.D.
  TITLE     UAF1 is a subunit of multiple deubiquitinating enzyme complexes
  JOURNAL   J Biol Chem 284 (8), 5343-5351 (2009)
   PUBMED   19075014
  REMARK    GeneRIF: two novel multisubunit deubiquitinating enzyme complexes
            containing USP12 and USP46, respectively. Both complexes contain
            the UAF1 protein as a bona fide subunit. Interestingly, UAF1
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Zemunik,T., Boban,M., Lauc,G., Jankovic,S., Rotim,K., Vatavuk,Z.,
            Bencic,G., Dogas,Z., Boraska,V., Torlak,V., Susac,J., Zobic,I.,
            Rudan,D., Pulanic,D., Modun,D., Mudnic,I., Gunjaca,G., Budimir,D.,
            Hayward,C., Vitart,V., Wright,A.F., Campbell,H. and Rudan,I.
  TITLE     Genome-wide association study of biochemical traits in Korcula
            Island, Croatia
  JOURNAL   Croat Med J 50 (1), 23-33 (2009)
   PUBMED   19260141
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   10 (residues 1 to 366)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CN483539.1, BC037574.1, AC026448.5 and BU620990.1.
            
            On Jun 4, 2003 this sequence version replaced NP_073743.1.
            
            Summary: Modification of cellular proteins by ubiquitin is an
            essential regulatory mechanism controlled by the coordinated action
            of multiple ubiquitin-conjugating and deubiquitinating enzymes.
            USP46 belongs to a large family of cysteine proteases that function
            as deubiquitinating enzymes (Quesada et al., 2004 [PubMed
            14715245]).[supplied by OMIM, Jun 2009].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.45934.1,
                                           SRR1660803.141938.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000441222.8/ ENSP00000407818.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..366
                     /product="ubiquitin carboxyl-terminal hydrolase 46 isoform
                     1"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin carboxyl-terminal hydrolase 46; ubiquitin
                     thioesterase 46; deubiquitinating enzyme 46;
                     ubiquitin-specific-processing protease 46; ubiquitin
                     thiolesterase 46"
                     /calculated_mol_wt=42311
     Region          36..363
                     /region_name="Peptidase_C19G"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02663"
                     /db_xref="CDD:239128"
     Site            order(39,44,313,329)
                     /site_type="active"
                     /db_xref="CDD:239128"
     CDS             1..366
                     /gene="USP46"
                     /coded_by="NM_022832.4:152..1252"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47053.1"
                     /db_xref="GeneID:64854"
                     /db_xref="HGNC:HGNC:20075"
                     /db_xref="MIM:612849"
ORIGIN      
        1 mtvrniasic nmgtnasale kdigpeqfpi nehyfglvnf gntcycnsvl qalyfcrpfr
       61 envlaykaqq kkkenlltcl adlfhsiatq kkkvgvippk kfisrlrken dlfdnymqqd
      121 aheflnylln tiadilqeek kqekqngklk ngnmnepaen nkpeltwvhe ifqgtltnet
      181 rclncetvss kdedfldlsv dveqntsith clrdfsntet lcseqkyyce tccskqeaqk
      241 rmrvkklpmi lalhlkrfky meqlhrytkl syrvvfplel rlfntssdav nldrmydlva
      301 vvvhcgsgpn rghyitivks hgfwllfddd ivekidaqai eefygltsdi sknsesgyil
      361 fyqsre
//
LOCUS       NP_001369228            1097 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 40 isoform 6 [Homo sapiens].
ACCESSION   NP_001369228
VERSION     NP_001369228.1
DBSOURCE    REFSEQ: accession NM_001382299.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Mo,H., Li,R., Yang,N., Han,J., Xiao,X., Zhang,Y., Xiao,Z., Jiao,L.,
            Xu,Q. and Tu,K.
  TITLE     USP40 promotes hepatocellular carcinoma progression through a
            YAP/USP40 positive feedback loop
  JOURNAL   Cancer Lett 589, 216832 (2024)
   PUBMED   38537774
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma progression
            through a YAP/USP40 positive feedback loop.
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Wu,Q., Qiu,Y., Guo,J., Yuan,Z., Yang,Y., Zhu,Q., Zhang,Z., Guo,J.,
            Wu,Y., Zhang,J., Huang,D., Tu,K. and Hu,X.
  TITLE     USP40 promotes hepatocellular carcinoma cell proliferation,
            migration and stemness by deubiquitinating and stabilizing Claudin1
  JOURNAL   Biol Direct 19 (1), 13 (2024)
   PUBMED   38308285
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma cell
            proliferation, migration and stemness by deubiquitinating and
            stabilizing Claudin1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Miao,J., Li,L., Shaheen,N., Wei,J., Jacko,A.M., Sundd,P.,
            Taleb,S.J., Mallampalli,R.K., Zhao,Y. and Zhao,J.
  TITLE     The deubiquitinase USP40 preserves endothelial integrity by
            targeting the heat shock protein HSP90beta
  JOURNAL   Exp Mol Med 56 (2), 395-407 (2024)
   PUBMED   38307937
REFERENCE   4  (residues 1 to 1097)
  AUTHORS   Takahashi,S., Fukuhara,D., Kimura,T., Fukutomi,T., Tanaka,E.,
            Mikami,N., Hada,I., Takematsu,H., Nishibori,Y., Akimoto,Y.,
            Kiyonari,H., Abe,T., Huber,O. and Yan,K.
  TITLE     USP40 deubiquitinates HINT1 and stabilizes p53 in podocyte damage
  JOURNAL   Biochem Biophys Res Commun 614, 198-206 (2022)
   PUBMED   35605301
REFERENCE   5  (residues 1 to 1097)
  AUTHORS   An,W., Yao,S., Sun,X., Hou,Z., Lin,Y., Su,L. and Liu,X.
  TITLE     Glucocorticoid modulatory element-binding protein 1 (GMEB1)
            interacts with the de-ubiquitinase USP40 to stabilize CFLARL and
            inhibit apoptosis in human non-small cell lung cancer cells
  JOURNAL   J Exp Clin Cancer Res 38 (1), 181 (2019)
   PUBMED   31046799
  REMARK    GeneRIF: Our findings show the de-ubiquitinase USP40 regulates the
            ubiquitination and degradation of CFLARL; and GMEB1 acts as a
            bridge protein for USP40 and CFLARL. Mechanistically, we found
            GMEB1 inhibits the activation of CASP8 by modulating ubiquitination
            and degradation of CFLARL
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1097)
  AUTHORS   Li,Y., Schrodi,S., Rowland,C., Tacey,K., Catanese,J. and Grupe,A.
  TITLE     Genetic evidence for ubiquitin-specific proteases USP24 and USP40
            as candidate genes for late-onset Parkinson disease
  JOURNAL   Hum Mutat 27 (10), 1017-1023 (2006)
   PUBMED   16917932
  REMARK    GeneRIF: Da suggest that genetic variants in USP40 affect the risk
            for late-onset Parkinson disease (PD), which is consistent with the
            predicted role of the ubiquitination pathway in PD etiology.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1097)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   8  (residues 1 to 1097)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   9  (residues 1 to 1097)
  AUTHORS   Bass,B.L.
  TITLE     RNA editing by adenosine deaminases that act on RNA
  JOURNAL   Annu Rev Biochem 71, 817-846 (2002)
   PUBMED   12045112
  REMARK    Review article
REFERENCE   10 (residues 1 to 1097)
  AUTHORS   Chen,X., Zhang,Y., Douglas,L. and Zhou,P.
  TITLE     UV-damaged DNA-binding proteins are targets of CUL-4A-mediated
            ubiquitination and degradation
  JOURNAL   J Biol Chem 276 (51), 48175-48182 (2001)
   PUBMED   11673459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019072.8 and AC019221.4.
            
            Summary: Modification of cellular proteins by ubiquitin is an
            essential regulatory mechanism controlled by the coordinated action
            of multiple ubiquitin-conjugating and deubiquitinating enzymes.
            USP40 belongs to a large family of cysteine proteases that function
            as deubiquitinating enzymes (Quesada et al., 2004 [PubMed
            14715245]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..1097
                     /product="ubiquitin carboxyl-terminal hydrolase 40 isoform
                     6"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 40; ubiquitin
                     carboxyl-terminal hydrolase 40;
                     ubiquitin-specific-processing protease 40;
                     deubiquitinating enzyme 40; ubiquitin thioesterase 40;
                     ubiquitin thiolesterase 40"
                     /calculated_mol_wt=123779
     Region          39..344
                     /region_name="peptidase_C19C"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02659"
                     /db_xref="CDD:239124"
     Site            order(45,50,305,323)
                     /site_type="active"
                     /db_xref="CDD:239124"
     CDS             1..1097
                     /gene="USP40"
                     /coded_by="NM_001382299.1:119..3412"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="GeneID:55230"
                     /db_xref="HGNC:HGNC:20069"
                     /db_xref="MIM:610570"
ORIGIN      
        1 mfgdlfeeey stvsnnqygk gkklktkale ppapreftnl sgirnqggtc ylnsllqtlh
       61 ftpefrealf slgpeelglf edkdkpdakv riiplqlqrl faqlllldqe aastadltds
      121 fgwtsneemr qhdvqelnri lfsaletslv gtsghdliyr lyhgtivnqi vckecknvse
      181 rqedfldltv avknvsgled alwnmyveee vfdcdnlyhc gtcdrlvkaa ksaklrklpp
      241 fltvsllrfn fdfvkceryk etscytfplr inlkpfceqs elddleyiyd lfsviihkgg
      301 cygghyhvyi kdvdhlgnwq fqeekskpdv nlkdlqseee idhplmilka illeeennli
      361 pvdqlgqkll kkigiswnkk yrkqhgplrk flqlhsqifl lssdestvrl lknsslqaes
      421 dfqrndqqif kmlppespar anprygvpch llnemdaani elqtkraecd sanntfelhl
      481 hlgpqyhffn galhpvvsqt esvwdltfdk rktlgdlrqs ifqllefweg dmvlsvaklv
      541 paglhiyqsl ggdeltlcet eiadgedifv wngvevggvh iqtgidcepl llnvlhldts
      601 sdgekccqvi esphvfpana evgtvltala ipagvifins agcpggegwt aipkedmrkt
      661 freqglrngs siliqdshdd nslltkeekw vtsmneidwl hvknlcqles eekqvkisat
      721 vntmvfdiri kaikelklmk eladnsclrp idrngkllcp vpdsytlkea elkmgsslgl
      781 clgkapsssq lflffamgsd vqpgtemeiv veetisvrdc lklmlkksgl qgdawhlrkm
      841 dwcyeagepl ceedatlkel licsgdtlll iegqlpplgf lkvpiwwyql qgpsghwesh
      901 qdqtnctssw grvwratssq gasgnepaqv sllylgdiei sedatlaelk sqamtlppfl
      961 efgvpspahl rawtverkrp grllrtdrqp lreyklgrri eicleplqkg enlgnhqvhi
     1021 dpmmalkcqq eahpqllsvc sdslpsngfi iapvalppys tffilvspdi svltdlfvsi
     1081 clplleykyl vysllyp
//
LOCUS       NP_001352408            1236 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 40 isoform 1 [Homo sapiens].
ACCESSION   NP_001352408 XP_016859915
VERSION     NP_001352408.1
DBSOURCE    REFSEQ: accession NM_001365479.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1236)
  AUTHORS   Mo,H., Li,R., Yang,N., Han,J., Xiao,X., Zhang,Y., Xiao,Z., Jiao,L.,
            Xu,Q. and Tu,K.
  TITLE     USP40 promotes hepatocellular carcinoma progression through a
            YAP/USP40 positive feedback loop
  JOURNAL   Cancer Lett 589, 216832 (2024)
   PUBMED   38537774
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma progression
            through a YAP/USP40 positive feedback loop.
REFERENCE   2  (residues 1 to 1236)
  AUTHORS   Wu,Q., Qiu,Y., Guo,J., Yuan,Z., Yang,Y., Zhu,Q., Zhang,Z., Guo,J.,
            Wu,Y., Zhang,J., Huang,D., Tu,K. and Hu,X.
  TITLE     USP40 promotes hepatocellular carcinoma cell proliferation,
            migration and stemness by deubiquitinating and stabilizing Claudin1
  JOURNAL   Biol Direct 19 (1), 13 (2024)
   PUBMED   38308285
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma cell
            proliferation, migration and stemness by deubiquitinating and
            stabilizing Claudin1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1236)
  AUTHORS   Miao,J., Li,L., Shaheen,N., Wei,J., Jacko,A.M., Sundd,P.,
            Taleb,S.J., Mallampalli,R.K., Zhao,Y. and Zhao,J.
  TITLE     The deubiquitinase USP40 preserves endothelial integrity by
            targeting the heat shock protein HSP90beta
  JOURNAL   Exp Mol Med 56 (2), 395-407 (2024)
   PUBMED   38307937
REFERENCE   4  (residues 1 to 1236)
  AUTHORS   Takahashi,S., Fukuhara,D., Kimura,T., Fukutomi,T., Tanaka,E.,
            Mikami,N., Hada,I., Takematsu,H., Nishibori,Y., Akimoto,Y.,
            Kiyonari,H., Abe,T., Huber,O. and Yan,K.
  TITLE     USP40 deubiquitinates HINT1 and stabilizes p53 in podocyte damage
  JOURNAL   Biochem Biophys Res Commun 614, 198-206 (2022)
   PUBMED   35605301
REFERENCE   5  (residues 1 to 1236)
  AUTHORS   An,W., Yao,S., Sun,X., Hou,Z., Lin,Y., Su,L. and Liu,X.
  TITLE     Glucocorticoid modulatory element-binding protein 1 (GMEB1)
            interacts with the de-ubiquitinase USP40 to stabilize CFLARL and
            inhibit apoptosis in human non-small cell lung cancer cells
  JOURNAL   J Exp Clin Cancer Res 38 (1), 181 (2019)
   PUBMED   31046799
  REMARK    GeneRIF: Our findings show the de-ubiquitinase USP40 regulates the
            ubiquitination and degradation of CFLARL; and GMEB1 acts as a
            bridge protein for USP40 and CFLARL. Mechanistically, we found
            GMEB1 inhibits the activation of CASP8 by modulating ubiquitination
            and degradation of CFLARL
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1236)
  AUTHORS   Li,Y., Schrodi,S., Rowland,C., Tacey,K., Catanese,J. and Grupe,A.
  TITLE     Genetic evidence for ubiquitin-specific proteases USP24 and USP40
            as candidate genes for late-onset Parkinson disease
  JOURNAL   Hum Mutat 27 (10), 1017-1023 (2006)
   PUBMED   16917932
  REMARK    GeneRIF: Da suggest that genetic variants in USP40 affect the risk
            for late-onset Parkinson disease (PD), which is consistent with the
            predicted role of the ubiquitination pathway in PD etiology.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1236)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   8  (residues 1 to 1236)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   9  (residues 1 to 1236)
  AUTHORS   Bass,B.L.
  TITLE     RNA editing by adenosine deaminases that act on RNA
  JOURNAL   Annu Rev Biochem 71, 817-846 (2002)
   PUBMED   12045112
  REMARK    Review article
REFERENCE   10 (residues 1 to 1236)
  AUTHORS   Chen,X., Zhang,Y., Douglas,L. and Zhou,P.
  TITLE     UV-damaged DNA-binding proteins are targets of CUL-4A-mediated
            ubiquitination and degradation
  JOURNAL   J Biol Chem 276 (51), 48175-48182 (2001)
   PUBMED   11673459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019072.8 and AC019221.4.
            
            On Aug 29, 2018 this sequence version replaced XP_016859915.1.
            
            Summary: Modification of cellular proteins by ubiquitin is an
            essential regulatory mechanism controlled by the coordinated action
            of multiple ubiquitin-conjugating and deubiquitinating enzymes.
            USP40 belongs to a large family of cysteine proteases that function
            as deubiquitinating enzymes (Quesada et al., 2004 [PubMed
            14715245]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1), as well as variant 3, encodes
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2692259.1,
                                           SRR14038197.699721.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000678225.2/ ENSP00000502952.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1236
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..1236
                     /product="ubiquitin carboxyl-terminal hydrolase 40 isoform
                     1"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 40; ubiquitin
                     carboxyl-terminal hydrolase 40;
                     ubiquitin-specific-processing protease 40;
                     deubiquitinating enzyme 40; ubiquitin thioesterase 40;
                     ubiquitin thiolesterase 40"
                     /calculated_mol_wt=140128
     Region          39..344
                     /region_name="peptidase_C19C"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02659"
                     /db_xref="CDD:239124"
     Site            order(45,50,305,323)
                     /site_type="active"
                     /db_xref="CDD:239124"
     Region          1181..1236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVE5.3)"
     CDS             1..1236
                     /gene="USP40"
                     /coded_by="NM_001365479.2:119..3829"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS92972.1"
                     /db_xref="GeneID:55230"
                     /db_xref="HGNC:HGNC:20069"
                     /db_xref="MIM:610570"
ORIGIN      
        1 mfgdlfeeey stvsnnqygk gkklktkale ppapreftnl sgirnqggtc ylnsllqtlh
       61 ftpefrealf slgpeelglf edkdkpdakv riiplqlqrl faqlllldqe aastadltds
      121 fgwtsneemr qhdvqelnri lfsaletslv gtsghdliyr lyhgtivnqi vckecknvse
      181 rqedfldltv avknvsgled alwnmyveee vfdcdnlyhc gtcdrlvkaa ksaklrklpp
      241 fltvsllrfn fdfvkceryk etscytfplr inlkpfceqs elddleyiyd lfsviihkgg
      301 cygghyhvyi kdvdhlgnwq fqeekskpdv nlkdlqseee idhplmilka illeeennli
      361 pvdqlgqkll kkigiswnkk yrkqhgplrk flqlhsqifl lssdestvrl lknsslqaes
      421 dfqrndqqif kmlppespgl nnsiscphwf dindskvqpi rekdieqqfq gkesaymlfy
      481 rksqlqrppe aranprygvp chllnemdaa nielqtkrae cdsanntfel hlhlgpqyhf
      541 fngalhpvvs qtesvwdltf dkrktlgdlr qsifqllefw egdmvlsvak lvpaglhiyq
      601 slggdeltlc eteiadgedi fvwngvevgg vhiqtgidce plllnvlhld tssdgekccq
      661 viesphvfpa naevgtvlta laipagvifi nsagcpggeg wtaipkedmr ktfreqglrn
      721 gssiliqdsh ddnslltkee kwvtsmneid wlhvknlcql eseekqvkis atvntmvfdi
      781 rikaikelkl mkeladnscl rpidrngkll cpvpdsytlk eaelkmgssl glclgkapss
      841 sqlflffamg sdvqpgteme ivveetisvr dclklmlkks glqgdawhlr kmdwcyeage
      901 plceedatlk ellicsgdtl lliegqlppl gflkvpiwwy qlqgpsghwe shqdqtncts
      961 swgrvwrats sqgasgnepa qvsllylgdi eisedatlae lksqamtlpp flefgvpspa
     1021 hlrawtverk rpgrllrtdr qplreyklgr rieicleplq kgenlgpqdv llrtqvripg
     1081 ertyapaldl vwnaaqggta gslrqrvadf yrlpvekiei akyfpekfew lpisswnqqi
     1141 tkrkkkkkqd ylqgapyylk dgdtigvknl lidddddfst irddtgkekq kqralgrrks
     1201 qealheqssy ilssaetpar prapetslsi hvgsfr
//
LOCUS       NP_778236                666 aa            linear   PRI 27-NOV-2025
DEFINITION  ATP-dependent RNA helicase DDX51 [Homo sapiens].
ACCESSION   NP_778236
VERSION     NP_778236.2
DBSOURCE    REFSEQ: accession NM_175066.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Wang,X., Liu,H., Zhao,C., Li,W., Xu,H. and Chen,Y.
  TITLE     The DEAD-box RNA helicase 51 controls non-small cell lung cancer
            proliferation by regulating cell cycle progression via multiple
            pathways
  JOURNAL   Sci Rep 6, 26108 (2016)
   PUBMED   27198888
  REMARK    GeneRIF: these data suggest that DDX51 aids cell cancer
            proliferation by regulating multiple signaling pathways
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   4  (residues 1 to 666)
  AUTHORS   Oshikawa,M., Tsutsui,C., Ikegami,T., Fuchida,Y., Matsubara,M.,
            Toyama,S., Usami,R., Ohtoko,K. and Kato,S.
  TITLE     Full-length transcriptome analysis of human retina-derived cell
            lines ARPE-19 and Y79 using the vector-capping method
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6662-6670 (2011)
   PUBMED   21697133
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 666)
  AUTHORS   Srivastava,L., Lapik,Y.R., Wang,M. and Pestov,D.G.
  TITLE     Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S
            rRNA by promoting the release of U8 snoRNA
  JOURNAL   Mol Cell Biol 30 (12), 2947-2956 (2010)
   PUBMED   20404093
REFERENCE   6  (residues 1 to 666)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 666)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 666)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK097078.1, AC138466.12, BC029279.1, BC040185.2 and BC063603.1.
            
            On Aug 4, 2007 this sequence version replaced NP_778236.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC040185.2, AK097078.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397333.4/ ENSP00000380495.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.33"
     Protein         1..666
                     /product="ATP-dependent RNA helicase DDX51"
                     /EC_number="3.6.4.13"
                     /note="DEAD box protein 51; DEAD (Asp-Glu-Ala-Asp) box
                     polypeptide 51"
                     /calculated_mol_wt=72326
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q8N8A6.3)"
     Region          9..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A6.3)"
     Region          <78..149
                     /region_name="LGT"
                     /note="Prolipoprotein diacylglyceryl transferase; cl00478"
                     /db_xref="CDD:469786"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8N8A6.3)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8N8A6.3)"
     Region          209..453
                     /region_name="DEADc_DDX51"
                     /note="DEAD-box helicase domain of DEAD box protein 51;
                     cd17956"
                     /db_xref="CDD:350714"
     Site            order(217..218,220..222,225,257..264)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350714"
     Region          221..229
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A6.3)"
     Region          371..374
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A6.3)"
     Region          479..609
                     /region_name="SF2_C_DEAD"
                     /note="C-terminal helicase domain of the DEAD box
                     helicases; cd18787"
                     /db_xref="CDD:350174"
     Site            order(568,570,595,598..599)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350174"
     CDS             1..666
                     /gene="DDX51"
                     /coded_by="NM_175066.4:24..2024"
                     /db_xref="CCDS:CCDS41865.1"
                     /db_xref="GeneID:317781"
                     /db_xref="HGNC:HGNC:20082"
                     /db_xref="MIM:621408"
ORIGIN      
        1 malfyvaryp gpdaaaaagp egaeagahgr arallerlqs rarerqqqre paqteaaast
       61 epatrrrrrp rrrrrvndae pgspeapqgk rrkadgedag aesneeapge psagsseeap
      121 gepsagssee apgerstsas aeaapdgpal eeaagplvpg lvlggfgkrk apkvqpflpr
      181 wlaepncvrr nvtedlvpie dipdvhpdlq kqlrahgiss yfpvqaavip allesaacgf
      241 lvgrggyrps dlcvsaptgs gktlafvipv vqallsrvvc hiralvvlpt kelaqqvskv
      301 fniytdatpl rvslvtgqks lakeqeslvq ktadgyrcla divvatpgrl vdhidqtpgf
      361 slqqlrflii deadrmidsm hqswlprvva aafqsedpad pcallqrrqa qavtaastcc
      421 pqmplqkllf satltqnpek lqqlglhqpr lfstglahrg ledtdgdgds gkyafpvglt
      481 hhyvpcslss kplvvlhlvl emgfsrvlcf tnsrenshrl fllvqafggv dvaefssryg
      541 pgqrrmilkq feqgkiqlli stdatargid vqgvelvvny dapqylrtyv hrvgrtarag
      601 ktgqaftlll kvqerrflrm lteagapelq rhelsskllq plvpryeeal sqleesvkee
      661 rkqraa
//
LOCUS       NP_001264693             231 aa            linear   PRI 27-NOV-2025
DEFINITION  calcium and integrin-binding protein 1 isoform a [Homo sapiens].
ACCESSION   NP_001264693
VERSION     NP_001264693.1
DBSOURCE    REFSEQ: accession NM_001277764.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Wang,X., Yi,Z., Shi,M. and Sun,Y.
  TITLE     The Diverse Functions of the Calcium- and Integrin-Binding Protein
            Family
  JOURNAL   Int J Mol Sci 26 (5), 2223 (2025)
   PUBMED   40076845
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Xu,M.H., Zheng,Y.M., Liang,B.G., Xu,W.X., Cao,J., Wang,P.,
            Dong,Z.Y., Zhou,C.H., Sun,H.C., Ren,N., Ke,A.W. and Shen,Y.H.
  TITLE     Deubiquitination of CIB1 by USP14 promotes lenvatinib resistance
            via the PAK1-ERK1/2 axis in hepatocellular carcinoma
  JOURNAL   Int J Biol Sci 20 (9), 3269-3284 (2024)
   PUBMED   38993552
  REMARK    GeneRIF: Deubiquitination of CIB1 by USP14 promotes lenvatinib
            resistance via the PAK1-ERK1/2 axis in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Wang,C., Felli,E., Selicean,S., Nulan,Y., Lozano,J.J.,
            Guixe-Muntet,S., Bosch,J., Berzigotti,A. and Gracia-Sancho,J.
  TITLE     Role of calcium integrin-binding protein 1 in the mechanobiology of
            the liver endothelium
  JOURNAL   J Cell Physiol 239 (5), e31198 (2024)
   PUBMED   38451745
  REMARK    GeneRIF: Role of calcium integrin-binding protein 1 in the
            mechanobiology of the liver endothelium.
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Ma,J., Song,Y., Zhuang,T., Yang,H., Yang,X., Zheng,J., Luo,J.,
            Xia,Y., Fei,X., Chan,D.W., Wu,D., Xu,P., Ni,P., Dai,J., Xu,D. and
            Hu,Y.
  TITLE     Identification of calcium and integrin-binding protein 1 as a
            reprogrammed glucose metabolism mediator to restrict immune cell
            infiltration in the stromal compartment of pancreatic ductal
            adenocarcinoma
  JOURNAL   Front Immunol 14, 1158964 (2023)
   PUBMED   37187730
  REMARK    GeneRIF: Identification of calcium and integrin-binding protein 1
            as a reprogrammed glucose metabolism mediator to restrict immune
            cell infiltration in the stromal compartment of pancreatic ductal
            adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 231)
  AUTHORS   Jacob,S., Bosch,F., Schoenberg,M.B., Pretzsch,E., Lampert,C.,
            Haoyu,R., Renz,B.W., Michl,M., Kumbrink,J., Kirchner,T., Werner,J.,
            Angele,M.K. and Neumann,J.
  TITLE     Expression of CIB1 correlates with colorectal liver metastases but
            not with peritoneal carcinomatosis
  JOURNAL   BMC Cancer 21 (1), 1243 (2021)
   PUBMED   34794407
  REMARK    GeneRIF: Expression of CIB1 correlates with colorectal liver
            metastases but not with peritoneal carcinomatosis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 231)
  AUTHORS   Armacki,M., Joodi,G., Nimmagadda,S.C., de Kimpe,L., Pusapati,G.V.,
            Vandoninck,S., Van Lint,J., Illing,A. and Seufferlein,T.
  TITLE     A novel splice variant of calcium and integrin-binding protein 1
            mediates protein kinase D2-stimulated tumour growth by regulating
            angiogenesis
  JOURNAL   Oncogene 33 (9), 1167-1180 (2014)
   PUBMED   23503467
  REMARK    GeneRIF: CIB1a is a novel mediator of PKD2-driven carcinogenesis.
REFERENCE   7  (residues 1 to 231)
  AUTHORS   Stabler,S.M., Ostrowski,L.L., Janicki,S.M. and Monteiro,M.J.
  TITLE     A myristoylated calcium-binding protein that preferentially
            interacts with the Alzheimer's disease presenilin 2 protein
  JOURNAL   J Cell Biol 145 (6), 1277-1292 (1999)
   PUBMED   10366599
REFERENCE   8  (residues 1 to 231)
  AUTHORS   Seki,N., Hayashi,A., Abe,M., Araki,R., Fujimori,A., Fukumura,R.,
            Hattori,A., Kozuma,S., Ohhira,M., Hori,T. and Saito,T.
  TITLE     Chromosomal assignment of the gene for human DNA-PKcs interacting
            protein (KIP) on chromosome 15q25.3-q26.1 by somatic hybrid
            analysis and fluorescence in situ hybridization
  JOURNAL   J Hum Genet 43 (4), 275-277 (1998)
   PUBMED   9852683
REFERENCE   9  (residues 1 to 231)
  AUTHORS   Wu,X. and Lieber,M.R.
  TITLE     Interaction between DNA-dependent protein kinase and a novel
            protein, KIP
  JOURNAL   Mutat Res 385 (1), 13-20 (1997)
   PUBMED   9372844
REFERENCE   10 (residues 1 to 231)
  AUTHORS   Naik,U.P., Patel,P.M. and Parise,L.V.
  TITLE     Identification of a novel calcium-binding protein that interacts
            with the integrin alphaIIb cytoplasmic domain
  JOURNAL   J Biol Chem 272 (8), 4651-4654 (1997)
   PUBMED   9030514
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD622547.1, JQ246073.1,
            BG231771.1 and AC091167.19.
            
            Summary: This gene encodes a member of the EF-hand
            domain-containing calcium-binding superfamily. The encoded protein
            interacts with many other proteins, including the platelet integrin
            alpha-IIb-beta-3, DNA-dependent protein kinase, presenilin-2, focal
            adhesion kinase, p21 activated kinase, and protein kinase D. The
            encoded protein may be involved in cell survival and proliferation,
            and is associated with several disease states including cancer and
            Alzheimer's disease. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Apr 2013].
            
            Transcript Variant: This variant (a) represents the longest
            transcript and encodes the longer isoform (a, also known as CIB1a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU944719.1, JQ246073.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.1"
     Protein         1..231
                     /product="calcium and integrin-binding protein 1 isoform
                     a"
                     /note="DNA-dependent protein kinase interacting protein;
                     DNA-PKcs-interacting protein; SNK-interacting protein
                     2-28; testicular secretory protein Li 9; DNA-PK
                     interaction protein; calcium and integrin binding 1
                     (calmyrin)"
                     /calculated_mol_wt=25901
     Region          123..172
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cl08302"
                     /db_xref="CDD:415501"
     Region          151..218
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cd00051"
                     /db_xref="CDD:238008"
     Site            order(156,158,160,167,201,203,205,212)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238008"
     CDS             1..231
                     /gene="CIB1"
                     /gene_synonym="CIB; CIBP; EV3; KIP1; PRKDCIP; SIP2-28"
                     /coded_by="NM_001277764.2:57..752"
                     /note="isoform a is encoded by transcript variant a"
                     /db_xref="CCDS:CCDS73781.1"
                     /db_xref="GeneID:10519"
                     /db_xref="HGNC:HGNC:16920"
                     /db_xref="MIM:602293"
ORIGIN      
        1 mggsgsrlsk ellaeyqdlt fltkqeills vyvvlaphlv dneqqarsgn ehtgrpiaen
       61 tdssplstra hrrfcellpq eqrsvesslr aqvpfeqils lpelkanpfk ericrvfsts
      121 pakdslsfed fldllsvfsd tatpdikshy afrifdfddd gtlnredlsr lvncltgege
      181 dtrlsasemk qlidnilees didrdgtinl sefqhvisrs pdfassfkiv l
//
LOCUS       NP_065987                600 aa            linear   PRI 27-NOV-2025
DEFINITION  ATP-dependent RNA helicase DDX55 [Homo sapiens].
ACCESSION   NP_065987 XP_045520
VERSION     NP_065987.1
DBSOURCE    REFSEQ: accession NM_020936.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Gazzara,M.R., Cater,T., Mallory,M.J., Barash,Y. and Lynch,K.W.
  TITLE     Integrative analysis of RNA binding proteins identifies DDX55 as a
            novel regulator of 3'UTR isoform diversity
  JOURNAL   Genome Biol 26 (1), 386 (2025)
   PUBMED   41225606
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Choudhury,P., Kretschmer,J., Hackert,P., Bohnsack,K.E. and
            Bohnsack,M.T.
  TITLE     The DExD box ATPase DDX55 is recruited to domain IV of the 28S
            ribosomal RNA by its C-terminal region
  JOURNAL   RNA Biol 18 (8), 1124-1135 (2021)
   PUBMED   33048000
  REMARK    GeneRIF: The DExD box ATPase DDX55 is recruited to domain IV of the
            28S ribosomal RNA by its C-terminal region.
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 600)
  AUTHORS   Schmid,S.R. and Linder,P.
  TITLE     D-E-A-D protein family of putative RNA helicases
  JOURNAL   Mol Microbiol 6 (3), 283-291 (1992)
   PUBMED   1552844
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055713.29, BC030020.2,
            AB046815.1, BU619784.1 and AA403154.1.
            
            On Jan 30, 2004 this sequence version replaced XP_045520.7.
            
            Summary: This gene encodes a member of protein family containing a
            characteristic Asp-Glu-Ala-Asp (DEAD) motif. These proteins are
            putative RNA helicases, and may be involved in a range of nuclear
            processes including translational initiation, nuclear and
            mitochondrial splicing, and ribosome and spliceosome assembly.
            Multiple alternatively spliced transcript variants have been found
            for this gene. Pseudogenes have been identified on chromosomes 1
            and 12. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1) encodes the protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.78589.1,
                                           SRR1803615.3510.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000238146.9/ ENSP00000238146.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..600
                     /product="ATP-dependent RNA helicase DDX55"
                     /EC_number="3.6.4.13"
                     /note="DEAD box protein 55; DEAD (Asp-Glu-Ala-Asp) box
                     polypeptide 55; epididymis secretory sperm binding
                     protein"
                     /calculated_mol_wt=68416
     Region          9..37
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHQ9.3)"
     Region          20..224
                     /region_name="DEADc_DDX55"
                     /note="DEAD-box helicase domain of DEAD box protein 55;
                     cd17960"
                     /db_xref="CDD:350718"
     Site            order(28..29,31..33,36,54..61)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350718"
     Region          171..174
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHQ9.3)"
     Region          242..372
                     /region_name="SF2_C_DEAD"
                     /note="C-terminal helicase domain of the DEAD box
                     helicases; cd18787"
                     /db_xref="CDD:350174"
     Site            order(331,333,358,361..362)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350174"
     Region          405..462
                     /region_name="DUF4217"
                     /note="Domain of unknown function (DUF4217); pfam13959"
                     /db_xref="CDD:464056"
     Region          500..550
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHQ9.3)"
     Region          533..562
                     /region_name="Important for nuclear localization.
                     /evidence=ECO:0000269|PubMed:33048000"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHQ9.3)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NHQ9.3)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8NHQ9.3)"
     CDS             1..600
                     /gene="DDX55"
                     /coded_by="NM_020936.3:51..1853"
                     /db_xref="CCDS:CCDS9251.1"
                     /db_xref="GeneID:57696"
                     /db_xref="HGNC:HGNC:20085"
                     /db_xref="MIM:620176"
ORIGIN      
        1 mehvtegswe slpvplhpqv lgalrelgfp ymtpvqsati plfmrnkdva aeavtgsgkt
       61 lafvipilei llrreeklkk sqvgaiiitp trelaiqide vlshftkhfp efsqilwigg
      121 rnpgedverf kqqggniiva tpgrledmfr rkaegldlas cvrsldvlvl deadrlldmg
      181 feasintile flpkqrrtgl fsatqtqeve nlvraglrnp vrvsvkekgv aassaqktps
      241 rlenyymvck adekfnqlvh flrnhkqekh lvffstcacv eyygkalevl vkgvkimcih
      301 gkmkykrnki fmefrklqsg ilvctdvmar gidipevnwv lqydppsnas afvhrcgrta
      361 righggsalv fllpmeesyi nflainqkcp lqemkpqrnt adllpklksm aladravfek
      421 gmkafvsyvq ayakhecnli frlkdldfas largfallrm pkmpelrgkq fpdfvpvdvn
      481 tdtipfkdki rekqrqklle qqrrektene grrkfiknka wskqkakkek kkkmnekrkr
      541 eegsdieded meellndtrl lkklkkgkit eeefekgllt tgkrtiktvd lgisdleddc
//
LOCUS       NP_001369226            1149 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 40 isoform 4 [Homo sapiens].
ACCESSION   NP_001369226
VERSION     NP_001369226.1
DBSOURCE    REFSEQ: accession NM_001382297.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1149)
  AUTHORS   Mo,H., Li,R., Yang,N., Han,J., Xiao,X., Zhang,Y., Xiao,Z., Jiao,L.,
            Xu,Q. and Tu,K.
  TITLE     USP40 promotes hepatocellular carcinoma progression through a
            YAP/USP40 positive feedback loop
  JOURNAL   Cancer Lett 589, 216832 (2024)
   PUBMED   38537774
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma progression
            through a YAP/USP40 positive feedback loop.
REFERENCE   2  (residues 1 to 1149)
  AUTHORS   Wu,Q., Qiu,Y., Guo,J., Yuan,Z., Yang,Y., Zhu,Q., Zhang,Z., Guo,J.,
            Wu,Y., Zhang,J., Huang,D., Tu,K. and Hu,X.
  TITLE     USP40 promotes hepatocellular carcinoma cell proliferation,
            migration and stemness by deubiquitinating and stabilizing Claudin1
  JOURNAL   Biol Direct 19 (1), 13 (2024)
   PUBMED   38308285
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma cell
            proliferation, migration and stemness by deubiquitinating and
            stabilizing Claudin1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1149)
  AUTHORS   Miao,J., Li,L., Shaheen,N., Wei,J., Jacko,A.M., Sundd,P.,
            Taleb,S.J., Mallampalli,R.K., Zhao,Y. and Zhao,J.
  TITLE     The deubiquitinase USP40 preserves endothelial integrity by
            targeting the heat shock protein HSP90beta
  JOURNAL   Exp Mol Med 56 (2), 395-407 (2024)
   PUBMED   38307937
REFERENCE   4  (residues 1 to 1149)
  AUTHORS   Takahashi,S., Fukuhara,D., Kimura,T., Fukutomi,T., Tanaka,E.,
            Mikami,N., Hada,I., Takematsu,H., Nishibori,Y., Akimoto,Y.,
            Kiyonari,H., Abe,T., Huber,O. and Yan,K.
  TITLE     USP40 deubiquitinates HINT1 and stabilizes p53 in podocyte damage
  JOURNAL   Biochem Biophys Res Commun 614, 198-206 (2022)
   PUBMED   35605301
REFERENCE   5  (residues 1 to 1149)
  AUTHORS   An,W., Yao,S., Sun,X., Hou,Z., Lin,Y., Su,L. and Liu,X.
  TITLE     Glucocorticoid modulatory element-binding protein 1 (GMEB1)
            interacts with the de-ubiquitinase USP40 to stabilize CFLARL and
            inhibit apoptosis in human non-small cell lung cancer cells
  JOURNAL   J Exp Clin Cancer Res 38 (1), 181 (2019)
   PUBMED   31046799
  REMARK    GeneRIF: Our findings show the de-ubiquitinase USP40 regulates the
            ubiquitination and degradation of CFLARL; and GMEB1 acts as a
            bridge protein for USP40 and CFLARL. Mechanistically, we found
            GMEB1 inhibits the activation of CASP8 by modulating ubiquitination
            and degradation of CFLARL
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1149)
  AUTHORS   Li,Y., Schrodi,S., Rowland,C., Tacey,K., Catanese,J. and Grupe,A.
  TITLE     Genetic evidence for ubiquitin-specific proteases USP24 and USP40
            as candidate genes for late-onset Parkinson disease
  JOURNAL   Hum Mutat 27 (10), 1017-1023 (2006)
   PUBMED   16917932
  REMARK    GeneRIF: Da suggest that genetic variants in USP40 affect the risk
            for late-onset Parkinson disease (PD), which is consistent with the
            predicted role of the ubiquitination pathway in PD etiology.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1149)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   8  (residues 1 to 1149)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   9  (residues 1 to 1149)
  AUTHORS   Bass,B.L.
  TITLE     RNA editing by adenosine deaminases that act on RNA
  JOURNAL   Annu Rev Biochem 71, 817-846 (2002)
   PUBMED   12045112
  REMARK    Review article
REFERENCE   10 (residues 1 to 1149)
  AUTHORS   Chen,X., Zhang,Y., Douglas,L. and Zhou,P.
  TITLE     UV-damaged DNA-binding proteins are targets of CUL-4A-mediated
            ubiquitination and degradation
  JOURNAL   J Biol Chem 276 (51), 48175-48182 (2001)
   PUBMED   11673459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019072.8 and AC019221.4.
            
            Summary: Modification of cellular proteins by ubiquitin is an
            essential regulatory mechanism controlled by the coordinated action
            of multiple ubiquitin-conjugating and deubiquitinating enzymes.
            USP40 belongs to a large family of cysteine proteases that function
            as deubiquitinating enzymes (Quesada et al., 2004 [PubMed
            14715245]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3221822.1,
                                           SRR11853565.17830.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1149
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..1149
                     /product="ubiquitin carboxyl-terminal hydrolase 40 isoform
                     4"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 40; ubiquitin
                     carboxyl-terminal hydrolase 40;
                     ubiquitin-specific-processing protease 40;
                     deubiquitinating enzyme 40; ubiquitin thioesterase 40;
                     ubiquitin thiolesterase 40"
                     /calculated_mol_wt=129959
     Region          39..344
                     /region_name="peptidase_C19C"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02659"
                     /db_xref="CDD:239124"
     Site            order(45,50,305,323)
                     /site_type="active"
                     /db_xref="CDD:239124"
     CDS             1..1149
                     /gene="USP40"
                     /coded_by="NM_001382297.1:119..3568"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:55230"
                     /db_xref="HGNC:HGNC:20069"
                     /db_xref="MIM:610570"
ORIGIN      
        1 mfgdlfeeey stvsnnqygk gkklktkale ppapreftnl sgirnqggtc ylnsllqtlh
       61 ftpefrealf slgpeelglf edkdkpdakv riiplqlqrl faqlllldqe aastadltds
      121 fgwtsneemr qhdvqelnri lfsaletslv gtsghdliyr lyhgtivnqi vckecknvse
      181 rqedfldltv avknvsgled alwnmyveee vfdcdnlyhc gtcdrlvkaa ksaklrklpp
      241 fltvsllrfn fdfvkceryk etscytfplr inlkpfceqs elddleyiyd lfsviihkgg
      301 cygghyhvyi kdvdhlgnwq fqeekskpdv nlkdlqseee idhplmilka illeeennli
      361 pvdqlgqkll kkigiswnkk yrkqhgplrk flqlhsqifl lssdestvrl lknsslqaes
      421 dfqrndqqif kmlppespgl nnsiscphwf dindskvqpi rekdieqqfq gkesaymlfy
      481 rksqlqrppe aranprygvp chllnemdaa nielqtkrae cdsanntfel hlhlgpqyhf
      541 fngalhpvvs qtesvwdltf dkrktlgdlr qsifqllefw egdmvlsvak lvpaglhiyq
      601 slggdeltlc eteiadgedi fvwngvevgg vhiqtgidce plllnvlhld tssdgekccq
      661 viesphvfpa naevgtvlta laipagvifi nsagcpggeg wtaipkedmr ktfreqglrn
      721 gssiliqdsh ddnslltkee kwvtsmneid wlhvknlcql eseekqvkis atvntmvfdi
      781 rikaikelkl mkeladnscl rpidrngkll cpvpdsytlk eaelkmgssl glclgkapss
      841 sqlflffamg sdvqpgteme ivveetisvr dclklmlkks glqgdawhlr kmdwcyeage
      901 plceedatlk ellicsgdtl lliegqlppl gflkvpiwwy qlqgpsghwe shqdqtncts
      961 swgrvwrats sqgasgnepa qvsllylgdi eisedatlae lksqamtlpp flefgvpspa
     1021 hlrawtverk rpgrllrtdr qplreyklgr rieicleplq kgenlgnhqv hidpmmalkc
     1081 qqeahpqlls vcsdslpsng fiiapvalpp ystffilvsp disvltdlfv siclplleyk
     1141 ylvysllyp
//
LOCUS       NP_001258817             144 aa            linear   PRI 27-NOV-2025
DEFINITION  calcium and integrin-binding family member 2 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001258817
VERSION     NP_001258817.1
DBSOURCE    REFSEQ: accession NM_001271888.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Wang,X., Yi,Z., Shi,M. and Sun,Y.
  TITLE     The Diverse Functions of the Calcium- and Integrin-Binding Protein
            Family
  JOURNAL   Int J Mol Sci 26 (5), 2223 (2025)
   PUBMED   40076845
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Dal Cortivo,G. and Dell'Orco,D.
  TITLE     Calcium- and Integrin-Binding Protein 2 (CIB2) in Physiology and
            Disease: Bright and Dark Sides
  JOURNAL   Int J Mol Sci 23 (7), 3552 (2022)
   PUBMED   35408910
  REMARK    GeneRIF: Calcium- and Integrin-Binding Protein 2 (CIB2) in
            Physiology and Disease: Bright and Dark Sides.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Liang,X., Qiu,X., Dionne,G., Cunningham,C.L., Pucak,M.L., Peng,G.,
            Kim,Y.H., Lauer,A., Shapiro,L. and Muller,U.
  TITLE     CIB2 and CIB3 are auxiliary subunits of the mechanotransduction
            channel of hair cells
  JOURNAL   Neuron 109 (13), 2131-2149 (2021)
   PUBMED   34089643
  REMARK    GeneRIF: CIB2 and CIB3 are auxiliary subunits of the
            mechanotransduction channel of hair cells.
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Huang,H., Bogstie,J.N. and Vogel,H.J.
  TITLE     Biophysical and structural studies of the human calcium- and
            integrin-binding protein family: understanding their functional
            similarities and differences
  JOURNAL   Biochem Cell Biol 90 (5), 646-656 (2012)
   PUBMED   22779914
  REMARK    GeneRIF: CIB2, as binding partners for the integrin alphaIIb
            subunit, which suggests that they are potentially involved in
            regulating integrin alphaIIb subunit activation.
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   7  (residues 1 to 144)
  AUTHORS   Ahmad,J., Khan,S.N., Khan,S.Y., Ramzan,K., Riazuddin,S.,
            Ahmed,Z.M., Wilcox,E.R., Friedman,T.B. and Riazuddin,S.
  TITLE     DFNB48, a new nonsyndromic recessive deafness locus, maps to
            chromosome 15q23-q25.1
  JOURNAL   Hum Genet 116 (5), 407-412 (2005)
   PUBMED   15711797
REFERENCE   8  (residues 1 to 144)
  AUTHORS   Seki,N., Hattori,A., Hayashi,A., Kozuma,S., Ohira,M., Hori,T. and
            Saito,T.
  TITLE     Structure, expression profile and chromosomal location of an isolog
            of DNA-PKcs interacting protein (KIP) gene
  JOURNAL   Biochim Biophys Acta 1444 (1), 143-147 (1999)
   PUBMED   9931475
REFERENCE   9  (residues 1 to 144)
  AUTHORS   Li,M., Squire,J.A. and Weksberg,R.
  TITLE     Overgrowth syndromes and genomic imprinting: from mouse to man
  JOURNAL   Clin Genet 53 (3), 165-170 (1998)
   PUBMED   9630066
  REMARK    Review article
REFERENCE   10 (residues 1 to 144)
  AUTHORS   Koenekoop,R.K., Arriaga,M.A., Trzupek,K.M. and Lentz,J.J.
  TITLE     Usher Syndrome Type I
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301442
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC090260.13.
            
            Summary: The protein encoded by this gene is similar to that of
            KIP/CIB, calcineurin B, and calmodulin. The encoded protein is a
            calcium-binding regulatory protein that interacts with
            DNA-dependent protein kinase catalytic subunits (DNA-PKcs), and it
            is involved in photoreceptor cell maintenance. Mutations in this
            gene cause deafness, autosomal recessive, 48 (DFNB48), and also
            Usher syndrome 1J (USH1J). Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (2) lacks an alternate exon, and
            it thus differs in its 5' UTR and initiates translation at a
            downstream in-frame start codon, compared to variant 1. The encoded
            isoform (2) is shorter at the N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033108.1, SRR9304713.132987.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.1"
     Protein         1..144
                     /product="calcium and integrin-binding family member 2
                     isoform 2"
                     /note="DNA-dependent protein kinase catalytic
                     subunit-interacting protein 2"
                     /calculated_mol_wt=16380
     Region          64..130
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     CDS             1..144
                     /gene="CIB2"
                     /gene_synonym="DFNB48; KIP2; USH1J"
                     /coded_by="NM_001271888.2:325..759"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS61722.1"
                     /db_xref="GeneID:10518"
                     /db_xref="HGNC:HGNC:24579"
                     /db_xref="MIM:605564"
ORIGIN      
        1 mdyrkspivh vpmsliiqmp elrenpfker ivaafsedge gnltfndfvd mfsvlcesap
       61 relkanyafk iydfntdnfi ckedleltla rltkseldee evvlvcdkvi eeadldgdgk
      121 lgfadfedmi akapdflstf hiri
//
LOCUS       NP_001025052             185 aa            linear   PRI 27-NOV-2025
DEFINITION  calcium and integrin-binding family member 4 [Homo sapiens].
ACCESSION   NP_001025052 XP_059399
VERSION     NP_001025052.1
DBSOURCE    REFSEQ: accession NM_001029881.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Wang,X., Yi,Z., Shi,M. and Sun,Y.
  TITLE     The Diverse Functions of the Calcium- and Integrin-Binding Protein
            Family
  JOURNAL   Int J Mol Sci 26 (5), 2223 (2025)
   PUBMED   40076845
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 185)
  AUTHORS   Huang,H., Bogstie,J.N. and Vogel,H.J.
  TITLE     Biophysical and structural studies of the human calcium- and
            integrin-binding protein family: understanding their functional
            similarities and differences
  JOURNAL   Biochem Cell Biol 90 (5), 646-656 (2012)
   PUBMED   22779914
  REMARK    GeneRIF: CIB4, as binding partners for the integrin alphaIIb
            subunit, which suggests that they are potentially involved in
            regulating integrin alphaIIb subunit activation.
REFERENCE   6  (residues 1 to 185)
  AUTHORS   Divaris,K., Monda,K.L., North,K.E., Olshan,A.F., Lange,E.M.,
            Moss,K., Barros,S.P., Beck,J.D. and Offenbacher,S.
  TITLE     Genome-wide association study of periodontal pathogen colonization
  JOURNAL   J Dent Res 91 (7 Suppl), 21S-28S (2012)
   PUBMED   22699663
REFERENCE   7  (residues 1 to 185)
  AUTHORS   Gentry,H.R., Singer,A.U., Betts,L., Yang,C., Ferrara,J.D.,
            Sondek,J. and Parise,L.V.
  TITLE     Structural and biochemical characterization of CIB1 delineates a
            new family of EF-hand-containing proteins
  JOURNAL   J Biol Chem 280 (9), 8407-8415 (2005)
   PUBMED   15574431
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC127684.1, AC015977.9 and AW138422.1.
            
            On Jul 27, 2005 this sequence version replaced XP_059399.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.395462.1,
                                           SRR5189658.11248.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000288861.5/ ENSP00000288861.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..185
                     /product="calcium and integrin-binding family member 4"
                     /calculated_mol_wt=21614
     Region          101..168
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     CDS             1..185
                     /gene="CIB4"
                     /gene_synonym="KIP4"
                     /coded_by="NM_001029881.3:53..610"
                     /db_xref="CCDS:CCDS33160.1"
                     /db_xref="GeneID:130106"
                     /db_xref="HGNC:HGNC:33703"
                     /db_xref="MIM:610646"
ORIGIN      
        1 mgqclryqmh wedleeyqal tfltrneilc ihdtflklcp pgkyykeatl tmdqvsslpa
       61 lrvnpfrdri crvfshkgmf sfedvlgmas vfseqacpsl kieyafriyd fnengfidee
      121 dlqriilrll nsddmsedll mdltnhvlse sdldndnmls fsefehamak spdfmnsfri
      181 hfwgc
//
LOCUS       NP_001273697             225 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 46 isoform 4 [Homo sapiens].
ACCESSION   NP_001273697
VERSION     NP_001273697.1
DBSOURCE    REFSEQ: accession NM_001286768.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Yu,K., Wang,G.M., Guo,S.S., Bassermann,F. and Fassler,R.
  TITLE     The USP12/46 deubiquitinases protect integrins from ESCRT-mediated
            lysosomal degradation
  JOURNAL   EMBO Rep 25 (12), 5687-5718 (2024)
   PUBMED   39506038
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Jiang,L., Qi,X., Lai,M., Zhou,J., Yuan,M., You,J., Liu,Q., Pan,J.,
            Zhao,L., Ying,M., Ji,J., Li,K., Zhang,Y., Pan,W., He,Q., Yang,B.
            and Cao,J.
  TITLE     WDR20 prevents hepatocellular carcinoma senescence by orchestrating
            the simultaneous USP12/46-mediated deubiquitination of c-Myc
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2407904121 (2024)
   PUBMED   39432777
  REMARK    GeneRIF: WDR20 prevents hepatocellular carcinoma senescence by
            orchestrating the simultaneous USP12/46-mediated deubiquitination
            of c-Myc.
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Ng,V.H., Spencer,Z., Neitzel,L.R., Nayak,A., Loberg,M.A., Shen,C.,
            Kassel,S.N., Kroh,H.K., An,Z., Anthony,C.C., Bryant,J.M.,
            Lawson,A., Goldsmith,L., Benchabane,H., Hansen,A.G., Li,J.,
            D'Souza,S., Lebensohn,A.M., Rohatgi,R., Weiss,W.A., Weiss,V.L.,
            Williams,C., Hong,C.C., Robbins,D.J., Ahmed,Y. and Lee,E.
  TITLE     The USP46 complex deubiquitylates LRP6 to promote Wnt/beta-catenin
            signaling
  JOURNAL   Nat Commun 14 (1), 6173 (2023)
   PUBMED   37798301
  REMARK    GeneRIF: The USP46 complex deubiquitylates LRP6 to promote
            Wnt/beta-catenin signaling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Ke,L., Jia,Z., Gao,W. and Luo,L.
  TITLE     Ubiquitin specific protease 46 potentiates triple negative breast
            cancer development by stabilizing PGAM1-mediated glycolysis
  JOURNAL   Cell Biol Int 47 (1), 41-51 (2023)
   PUBMED   36335636
  REMARK    GeneRIF: Ubiquitin specific protease 46 potentiates triple negative
            breast cancer development by stabilizing PGAM1-mediated glycolysis.
REFERENCE   6  (residues 1 to 225)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Cohn,M.A., Kee,Y., Haas,W., Gygi,S.P. and D'Andrea,A.D.
  TITLE     UAF1 is a subunit of multiple deubiquitinating enzyme complexes
  JOURNAL   J Biol Chem 284 (8), 5343-5351 (2009)
   PUBMED   19075014
  REMARK    GeneRIF: two novel multisubunit deubiquitinating enzyme complexes
            containing USP12 and USP46, respectively. Both complexes contain
            the UAF1 protein as a bona fide subunit. Interestingly, UAF1
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Zemunik,T., Boban,M., Lauc,G., Jankovic,S., Rotim,K., Vatavuk,Z.,
            Bencic,G., Dogas,Z., Boraska,V., Torlak,V., Susac,J., Zobic,I.,
            Rudan,D., Pulanic,D., Modun,D., Mudnic,I., Gunjaca,G., Budimir,D.,
            Hayward,C., Vitart,V., Wright,A.F., Campbell,H. and Rudan,I.
  TITLE     Genome-wide association study of biochemical traits in Korcula
            Island, Croatia
  JOURNAL   Croat Med J 50 (1), 23-33 (2009)
   PUBMED   19260141
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   9  (residues 1 to 225)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   10 (residues 1 to 225)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CN483539.1, AK296493.1 and AC026448.5.
            
            Summary: Modification of cellular proteins by ubiquitin is an
            essential regulatory mechanism controlled by the coordinated action
            of multiple ubiquitin-conjugating and deubiquitinating enzymes.
            USP46 belongs to a large family of cysteine proteases that function
            as deubiquitinating enzymes (Quesada et al., 2004 [PubMed
            14715245]).[supplied by OMIM, Jun 2009].
            
            Transcript Variant: This variant (4) differs in its 5' UTR and
            initiates translation at a downstream start codon, compared to
            variant 1. The encoded isoform (4) has a shorter N-terminus,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296493.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..225
                     /product="ubiquitin carboxyl-terminal hydrolase 46 isoform
                     4"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin carboxyl-terminal hydrolase 46; ubiquitin
                     thioesterase 46; deubiquitinating enzyme 46;
                     ubiquitin-specific-processing protease 46; ubiquitin
                     thiolesterase 46"
                     /calculated_mol_wt=26112
     Region          <1..217
                     /region_name="Peptidase_C19"
                     /note="Peptidase C19 contains ubiquitinyl hydrolases. They
                     are intracellular peptidases that remove ubiquitin
                     molecules from polyubiquinated peptides by cleavage of
                     isopeptide bonds. They hydrolyse bonds involving the
                     carboxyl group of the C-terminal Gly...; cl02553"
                     /db_xref="CDD:470612"
     CDS             1..225
                     /gene="USP46"
                     /coded_by="NM_001286768.2:608..1285"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:64854"
                     /db_xref="HGNC:HGNC:20075"
                     /db_xref="MIM:612849"
ORIGIN      
        1 mqqdahefln yllntiadil qeekkqekqn gklkngnmne paennkpelt wvheifqgtl
       61 tnetrclnce tvsskdedfl dlsvdveqnt sithclrdfs ntetlcseqk yycetccskq
      121 eaqkrmrvkk lpmilalhlk rfkymeqlhr ytklsyrvvf plelrlfnts sdavnldrmy
      181 dlvavvvhcg sgpnrghyit ivkshgfwll fdddivevgl qiilq
//
LOCUS       NP_758953                422 aa            linear   PRI 27-NOV-2025
DEFINITION  protein phosphatase 1 regulatory subunit 36 [Homo sapiens].
ACCESSION   NP_758953
VERSION     NP_758953.1
DBSOURCE    REFSEQ: accession NM_172365.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Zhang,Q., Gao,M., Zhang,Y., Song,Y., Cheng,H. and Zhou,R.
  TITLE     The germline-enriched Ppp1r36 promotes autophagy
  JOURNAL   Sci Rep 6, 24609 (2016)
   PUBMED   27098880
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC068989.1 and AL049869.6.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.130813.1,
                                           SRR1803612.155454.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000298705.6/ ENSP00000298705.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..422
                     /product="protein phosphatase 1 regulatory subunit 36"
                     /calculated_mol_wt=49309
     Region          79..413
                     /region_name="PPPI_inhib"
                     /note="Protein phosphatase 1 inhibitor; pfam14895"
                     /db_xref="CDD:464358"
     CDS             1..422
                     /gene="PPP1R36"
                     /gene_synonym="C14orf50"
                     /coded_by="NM_172365.3:38..1306"
                     /db_xref="CCDS:CCDS9767.1"
                     /db_xref="GeneID:145376"
                     /db_xref="HGNC:HGNC:20097"
                     /db_xref="MIM:619923"
ORIGIN      
        1 myrvpefyar rkrlggqtpy lmdqlglrlg mwywkdetrt lefrrfaaed svqwllkhhp
       61 hftpaaevke kgkkgkavhf aetdgpasdr ltdkrlaakd dksakavekr gqqgtitldd
      121 vkfvtllllq dtemqricsf ttfmrnknld nflmallyyl shyleknsle kkpksymvgl
      181 vekkemelvl seleaaqryl aqkycilvlg lavpdkhhmc cgkekisdtq kdwkffesfy
      241 tfctyvawiv frrqhlteie eevgrlfrtn mfniprrrre deesggekkr mtfvqfrrmm
      301 akrpaikkai nmrspvmstl lpslrekaqn vfekkyhqvd vrfpaemqkh vgtldsvpmp
      361 vvgilgeprc lfnphtlhpl dpeentksfg rypslmennn mriqdtldlv mktlsshtsc
      421 pk
//
LOCUS       NP_997300                320 aa            linear   PRI 27-NOV-2025
DEFINITION  cilia- and flagella-associated protein 77 isoform 1 [Homo sapiens].
ACCESSION   NP_997300
VERSION     NP_997300.1
DBSOURCE    REFSEQ: accession NM_207417.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Xia,L., Yin,G.L., Long,Y., Sun,F., Wang,B.B., Zhu,Y. and Chen,S.R.
  TITLE     The core outer junction protein CFAP77 connects A- and B-tubules
            within doublet microtubules of cilia and flagella
  JOURNAL   PLoS Biol 23 (10), e3003442 (2025)
   PUBMED   41118442
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Gui,M., Croft,J.T., Zabeo,D., Acharya,V., Kollman,J.M.,
            Burgoyne,T., Hoog,J.L. and Brown,A.
  TITLE     SPACA9 is a lumenal protein of human ciliary singlet and doublet
            microtubules
  JOURNAL   Proc Natl Acad Sci U S A 119 (41), e2207605119 (2022)
   PUBMED   36191189
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Blackburn,K., Bustamante-Marin,X., Yin,W., Goshe,M.B. and
            Ostrowski,L.E.
  TITLE     Quantitative Proteomic Analysis of Human Airway Cilia Identifies
            Previously Uncharacterized Proteins of High Abundance
  JOURNAL   J Proteome Res 16 (4), 1579-1592 (2017)
   PUBMED   28282151
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Lindskog,C., Fagerberg,L., Hallstrom,B., Edlund,K., Hellwig,B.,
            Rahnenfuhrer,J., Kampf,C., Uhlen,M., Ponten,F. and Micke,P.
  TITLE     The lung-specific proteome defined by integration of
            transcriptomics and antibody-based profiling
  JOURNAL   FASEB J 28 (12), 5184-5196 (2014)
   PUBMED   25169055
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL353701.15, AK128819.1 and AL354735.14.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK128819.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..320
                     /product="cilia- and flagella-associated protein 77
                     isoform 1"
                     /calculated_mol_wt=36368
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZQR2.1)"
     Region          54..240
                     /region_name="CFAP77"
                     /note="Cilia- and flagella-associated protein 77;
                     pfam14825"
                     /db_xref="CDD:464337"
     CDS             1..320
                     /gene="CFAP77"
                     /gene_synonym="C9orf171"
                     /coded_by="NM_207417.3:62..1024"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6949.1"
                     /db_xref="GeneID:389799"
                     /db_xref="HGNC:HGNC:33776"
                     /db_xref="MIM:621136"
ORIGIN      
        1 mpearssgpd ltrwrkqqqp vrrtvsqvcp pprrpltvad irsgmenerl gvvrdsmfqn
       61 plivkaagpa svgtsysvyd ssavqkvips laghhikggp qaelgkprer syslpginfn
      121 yglyirgldg gvpeaigrwn vfkqqptcph eltrnyiamn rgavkaglvt arenllyrql
      181 ndirisdqdd rrmkkepppl ppnmtfgira rpstpffdll qhrylqlwvq eqkatqkaik
      241 lekkqkvvlg klyetrssql rkykppvkld tlwhmphfqk vgrhldtfpt eadrqralka
      301 hreecavrqg tlrmgnythp
//
LOCUS       NP_065186               1426 aa            linear   PRI 27-NOV-2025
DEFINITION  phospholipid-transporting ATPase VD [Homo sapiens].
ACCESSION   NP_065186
VERSION     NP_065186.3
DBSOURCE    REFSEQ: accession NM_020453.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1426)
  AUTHORS   Kita,N., Hamamoto,A., Gowda,S.G.B., Takatsu,H., Nakayama,K.,
            Arita,M., Hui,S.P. and Shin,H.W.
  TITLE     Glucosylceramide flippases contribute to cellular glucosylceramide
            homeostasis
  JOURNAL   J Lipid Res 65 (3), 100508 (2024)
   PUBMED   38280458
REFERENCE   2  (residues 1 to 1426)
  AUTHORS   Roland,B.P., Naito,T., Best,J.T., Arnaiz-Yepez,C., Takatsu,H.,
            Yu,R.J., Shin,H.W. and Graham,T.R.
  TITLE     Yeast and human P4-ATPases transport glycosphingolipids using
            conserved structural motifs
  JOURNAL   J Biol Chem 294 (6), 1794-1806 (2019)
   PUBMED   30530492
REFERENCE   3  (residues 1 to 1426)
  AUTHORS   Naito,T., Takatsu,H., Miyano,R., Takada,N., Nakayama,K. and
            Shin,H.W.
  TITLE     Phospholipid Flippase ATP10A Translocates Phosphatidylcholine and
            Is Involved in Plasma Membrane Dynamics
  JOURNAL   J Biol Chem 290 (24), 15004-15017 (2015)
   PUBMED   25947375
REFERENCE   4  (residues 1 to 1426)
  AUTHORS   Kengia,J.T., Ko,K.C., Ikeda,S., Hiraishi,A., Mieno-Naka,M.,
            Arai,T., Sato,N., Muramatsu,M. and Sawabe,M.
  TITLE     A gene variant in the Atp10d gene associates with atherosclerotic
            indices in Japanese elderly population
  JOURNAL   Atherosclerosis 231 (1), 158-162 (2013)
   PUBMED   24125428
  REMARK    GeneRIF: The rs2351791 SNP in the Atp10d gene affects the
            susceptibility for cardiac and intracranial vascular stenosis in
            the elderly Japanese population.
REFERENCE   5  (residues 1 to 1426)
  AUTHORS   Demirkan,A., van Duijn,C.M., Ugocsai,P., Isaacs,A.,
            Pramstaller,P.P., Liebisch,G., Wilson,J.F., Johansson,A., Rudan,I.,
            Aulchenko,Y.S., Kirichenko,A.V., Janssens,A.C., Jansen,R.C.,
            Gnewuch,C., Domingues,F.S., Pattaro,C., Wild,S.H., Jonasson,I.,
            Polasek,O., Zorkoltseva,I.V., Hofman,A., Karssen,L.C.,
            Struchalin,M., Floyd,J., Igl,W., Biloglav,Z., Broer,L., Pfeufer,A.,
            Pichler,I., Campbell,S., Zaboli,G., Kolcic,I., Rivadeneira,F.,
            Huffman,J., Hastie,N.D., Uitterlinden,A., Franke,L., Franklin,C.S.,
            Vitart,V., Nelson,C.P., Preuss,M., Bis,J.C., O'Donnell,C.J.,
            Franceschini,N., Witteman,J.C., Axenovich,T., Oostra,B.A.,
            Meitinger,T., Hicks,A.A., Hayward,C., Wright,A.F., Gyllensten,U.,
            Campbell,H. and Schmitz,G.
  CONSRTM   DIAGRAM Consortium; CARDIoGRAM Consortium; CHARGE Consortium;
            EUROSPAN consortium
  TITLE     Genome-wide association study identifies novel loci associated with
            circulating phospho- and sphingolipid concentrations
  JOURNAL   PLoS Genet 8 (2), e1002490 (2012)
   PUBMED   22359512
REFERENCE   6  (residues 1 to 1426)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1426)
  AUTHORS   Hicks,A.A., Pramstaller,P.P., Johansson,A., Vitart,V., Rudan,I.,
            Ugocsai,P., Aulchenko,Y., Franklin,C.S., Liebisch,G., Erdmann,J.,
            Jonasson,I., Zorkoltseva,I.V., Pattaro,C., Hayward,C., Isaacs,A.,
            Hengstenberg,C., Campbell,S., Gnewuch,C., Janssens,A.C.,
            Kirichenko,A.V., Konig,I.R., Marroni,F., Polasek,O., Demirkan,A.,
            Kolcic,I., Schwienbacher,C., Igl,W., Biloglav,Z., Witteman,J.C.,
            Pichler,I., Zaboli,G., Axenovich,T.I., Peters,A., Schreiber,S.,
            Wichmann,H.E., Schunkert,H., Hastie,N., Oostra,B.A., Wild,S.H.,
            Meitinger,T., Gyllensten,U., van Duijn,C.M., Wilson,J.F.,
            Wright,A., Schmitz,G. and Campbell,H.
  TITLE     Genetic determinants of circulating sphingolipid concentrations in
            European populations
  JOURNAL   PLoS Genet 5 (10), e1000672 (2009)
   PUBMED   19798445
REFERENCE   8  (residues 1 to 1426)
  AUTHORS   Paulusma,C.C. and Oude Elferink,R.P.
  TITLE     The type 4 subfamily of P-type ATPases, putative aminophospholipid
            translocases with a role in human disease
  JOURNAL   Biochim Biophys Acta 1741 (1-2), 11-24 (2005)
   PUBMED   15919184
  REMARK    Review article
REFERENCE   9  (residues 1 to 1426)
  AUTHORS   Kuhlbrandt,W.
  TITLE     Biology, structure and mechanism of P-type ATPases
  JOURNAL   Nat Rev Mol Cell Biol 5 (4), 282-295 (2004)
   PUBMED   15071553
  REMARK    Review article
REFERENCE   10 (residues 1 to 1426)
  AUTHORS   Flamant,S., Pescher,P., Lemercier,B., Clement-Ziza,M., Kepes,F.,
            Fellous,M., Milon,G., Marchal,G. and Besmond,C.
  TITLE     Characterization of a putative type IV aminophospholipid
            transporter P-type ATPase
  JOURNAL   Mamm Genome 14 (1), 21-30 (2003)
   PUBMED   12532265
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC107398.4, AJ441078.1 and BC131535.1.
            
            On Jan 31, 2009 this sequence version replaced NP_065186.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ441078.1, SRR1660807.234887.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000273859.8/ ENSP00000273859.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p12"
     Protein         1..1426
                     /product="phospholipid-transporting ATPase VD"
                     /EC_number="7.6.2.1"
                     /note="type IV aminophospholipid transporting ATPase;
                     probable phospholipid-transporting ATPase VD; P4-ATPase
                     flippase complex alpha subunit ATP10D; ATPase, class V,
                     type 10D"
                     /calculated_mol_wt=160144
     Region          73..1214
                     /region_name="P-type_ATPase_APLT_Dnf-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2,
                     -10D, -11B, -11C; cd02073"
                     /db_xref="CDD:319770"
     Site            98..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P241.3)"
     Site            122..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P241.3)"
     Site            322..342
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P241.3)"
     Site            366..386
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P241.3)"
     Site            order(438..440,772,796..798,873,920..922,1030,1033,1036,
                     1056,1059)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     Region          506..531
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P241.3)"
     Site            1114..1134
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P241.3)"
     Site            1146..1166
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P241.3)"
     Site            1196..1216
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P241.3)"
     Site            1225..1245
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P241.3)"
     Site            1253..1273
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P241.3)"
     Site            1293..1313
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P241.3)"
     CDS             1..1426
                     /gene="ATP10D"
                     /gene_synonym="ATPVD"
                     /coded_by="NM_020453.4:283..4563"
                     /db_xref="CCDS:CCDS3476.1"
                     /db_xref="GeneID:57205"
                     /db_xref="HGNC:HGNC:13549"
                     /db_xref="MIM:619815"
ORIGIN      
        1 mtealqwary hwrrlirgat rdddsgpyny ssllacgrks sqtpklsgrh rivvphiqpf
       61 kdeyekfsga yvnnrirttk ytllnfvprn lfeqfhraan lyflflvvln wvplveafqk
      121 eitmlplvvv ltiiaikdgl edyrkykidk qinnlitkvy srkekkyidr cwkdvtvgdf
      181 irlscnevip admvllfstd pdgichiets gldgesnlkq rqvvrgyaeq dsevdpekfs
      241 sriecespnn dlsrfrgfle hsnkervgls kenlllrgct irnteavvgi vvyaghetka
      301 mlnnsgpryk rsklerrant dvlwcvmllv imcltgavgh giwlsryekm hffnvpepdg
      361 hiispllagf ymfwtmiill qvlipislyv sieivklgqi yfiqsdvdfy nekmdsivqc
      421 ralniaedlg qiqylfsdkt gtltenkmvf rrcsvagfdy cheenarrle syqeavsede
      481 dfidtvsgsl snmakpraps crtvhngplg nkpsnhlags sftlgsgega sevphsrqaa
      541 fsspietdvv pdtrlldkfs qitprlfmpl detiqnppme tlyiidffia laicntvvvs
      601 apnqprqkir hpslgglpik sleeikslfq rwsvrrsssp slnsgkepss gvpnafvsrl
      661 plfsrmkpas pveeevsqvc espqcssssa cctetekqhg dagllngkae slpgqplacn
      721 lcyeaespde aalvyaaray qctlrsrtpe qvmvdfaalg pltfqllhil pfdsvrkrms
      781 vvvrhplsnq vvvytkgads vimellsvas pdgaslekqq mivrektqkh lddyakqglr
      841 tlciakkvms dteyaewlrn hflaetsidn reelllesam rlenkltllg atgiedrlqe
      901 gvpesiealh kagikiwmlt gdkqetavni ayackllepd dklfilntqs kdacgmlmst
      961 ilkelqkktq alpeqvslse dllqppvprd sglragliit gktlefalqe slqkqflelt
     1021 swcqavvccr atplqksevv klvrshlqvm tlaigdgand vsmiqvadig igvsgqegmq
     1081 avmasdfavs qfkhlsklll vhghwcytrl snmilyffyk nvayvnllfw yqffcgfsgt
     1141 smtdywvlif fnllftsapp viygvlekdv saetlmqlpe lyrsgqksea ylphtfwitl
     1201 ldafyqslvc ffvpyftyqg sdtdifafgn plntaalfiv llhlviesks ltwihllvii
     1261 gsilsyflfa ivfgamcvtc nppsnpywim qehmldpvfy lvcilttsia llprfvyrvl
     1321 qgslfpspil rakhfdrltp eertkalkkw rgagkmnqvt skyanqsagk sgrrpmpgps
     1381 avfamksass caieqgnlsl cetaldqgys etkafemagp skgkes
//
LOCUS       NP_001369231             209 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 40 isoform 9 [Homo sapiens].
ACCESSION   NP_001369231
VERSION     NP_001369231.1
DBSOURCE    REFSEQ: accession NM_001382302.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Mo,H., Li,R., Yang,N., Han,J., Xiao,X., Zhang,Y., Xiao,Z., Jiao,L.,
            Xu,Q. and Tu,K.
  TITLE     USP40 promotes hepatocellular carcinoma progression through a
            YAP/USP40 positive feedback loop
  JOURNAL   Cancer Lett 589, 216832 (2024)
   PUBMED   38537774
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma progression
            through a YAP/USP40 positive feedback loop.
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Wu,Q., Qiu,Y., Guo,J., Yuan,Z., Yang,Y., Zhu,Q., Zhang,Z., Guo,J.,
            Wu,Y., Zhang,J., Huang,D., Tu,K. and Hu,X.
  TITLE     USP40 promotes hepatocellular carcinoma cell proliferation,
            migration and stemness by deubiquitinating and stabilizing Claudin1
  JOURNAL   Biol Direct 19 (1), 13 (2024)
   PUBMED   38308285
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma cell
            proliferation, migration and stemness by deubiquitinating and
            stabilizing Claudin1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Miao,J., Li,L., Shaheen,N., Wei,J., Jacko,A.M., Sundd,P.,
            Taleb,S.J., Mallampalli,R.K., Zhao,Y. and Zhao,J.
  TITLE     The deubiquitinase USP40 preserves endothelial integrity by
            targeting the heat shock protein HSP90beta
  JOURNAL   Exp Mol Med 56 (2), 395-407 (2024)
   PUBMED   38307937
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Takahashi,S., Fukuhara,D., Kimura,T., Fukutomi,T., Tanaka,E.,
            Mikami,N., Hada,I., Takematsu,H., Nishibori,Y., Akimoto,Y.,
            Kiyonari,H., Abe,T., Huber,O. and Yan,K.
  TITLE     USP40 deubiquitinates HINT1 and stabilizes p53 in podocyte damage
  JOURNAL   Biochem Biophys Res Commun 614, 198-206 (2022)
   PUBMED   35605301
REFERENCE   5  (residues 1 to 209)
  AUTHORS   An,W., Yao,S., Sun,X., Hou,Z., Lin,Y., Su,L. and Liu,X.
  TITLE     Glucocorticoid modulatory element-binding protein 1 (GMEB1)
            interacts with the de-ubiquitinase USP40 to stabilize CFLARL and
            inhibit apoptosis in human non-small cell lung cancer cells
  JOURNAL   J Exp Clin Cancer Res 38 (1), 181 (2019)
   PUBMED   31046799
  REMARK    GeneRIF: Our findings show the de-ubiquitinase USP40 regulates the
            ubiquitination and degradation of CFLARL; and GMEB1 acts as a
            bridge protein for USP40 and CFLARL. Mechanistically, we found
            GMEB1 inhibits the activation of CASP8 by modulating ubiquitination
            and degradation of CFLARL
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 209)
  AUTHORS   Li,Y., Schrodi,S., Rowland,C., Tacey,K., Catanese,J. and Grupe,A.
  TITLE     Genetic evidence for ubiquitin-specific proteases USP24 and USP40
            as candidate genes for late-onset Parkinson disease
  JOURNAL   Hum Mutat 27 (10), 1017-1023 (2006)
   PUBMED   16917932
  REMARK    GeneRIF: Da suggest that genetic variants in USP40 affect the risk
            for late-onset Parkinson disease (PD), which is consistent with the
            predicted role of the ubiquitination pathway in PD etiology.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 209)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   8  (residues 1 to 209)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   9  (residues 1 to 209)
  AUTHORS   Bass,B.L.
  TITLE     RNA editing by adenosine deaminases that act on RNA
  JOURNAL   Annu Rev Biochem 71, 817-846 (2002)
   PUBMED   12045112
  REMARK    Review article
REFERENCE   10 (residues 1 to 209)
  AUTHORS   Chen,X., Zhang,Y., Douglas,L. and Zhou,P.
  TITLE     UV-damaged DNA-binding proteins are targets of CUL-4A-mediated
            ubiquitination and degradation
  JOURNAL   J Biol Chem 276 (51), 48175-48182 (2001)
   PUBMED   11673459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019221.4.
            
            Summary: Modification of cellular proteins by ubiquitin is an
            essential regulatory mechanism controlled by the coordinated action
            of multiple ubiquitin-conjugating and deubiquitinating enzymes.
            USP40 belongs to a large family of cysteine proteases that function
            as deubiquitinating enzymes (Quesada et al., 2004 [PubMed
            14715245]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.81485.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2142348,
                                           SAMEA2142670 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..209
                     /product="ubiquitin carboxyl-terminal hydrolase 40 isoform
                     9"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 40; ubiquitin
                     carboxyl-terminal hydrolase 40;
                     ubiquitin-specific-processing protease 40;
                     deubiquitinating enzyme 40; ubiquitin thioesterase 40;
                     ubiquitin thiolesterase 40"
                     /calculated_mol_wt=23827
     CDS             1..209
                     /gene="USP40"
                     /coded_by="NM_001382302.1:241..870"
                     /note="isoform 9 is encoded by transcript variant 10"
                     /db_xref="GeneID:55230"
                     /db_xref="HGNC:HGNC:20069"
                     /db_xref="MIM:610570"
ORIGIN      
        1 mtlppflefg vpspahlraw tverkrpgrl lrtdrqplsp qdvllrtqvr ipgertyapa
       61 ldlvwnaaqg gtagslrqrv adfyrlpvek ieiakyfpek fewlpisswn qqitkrkkkk
      121 kqdylqgapy ylkdgdtigv knlliddddd fstirddtgk ekqkqralgr rksqealheq
      181 ssyilssaet parprapets lsihvgsfr
//
LOCUS       NP_001369224            1236 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 40 isoform 1 [Homo sapiens].
ACCESSION   NP_001369224
VERSION     NP_001369224.1
DBSOURCE    REFSEQ: accession NM_001382295.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1236)
  AUTHORS   Mo,H., Li,R., Yang,N., Han,J., Xiao,X., Zhang,Y., Xiao,Z., Jiao,L.,
            Xu,Q. and Tu,K.
  TITLE     USP40 promotes hepatocellular carcinoma progression through a
            YAP/USP40 positive feedback loop
  JOURNAL   Cancer Lett 589, 216832 (2024)
   PUBMED   38537774
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma progression
            through a YAP/USP40 positive feedback loop.
REFERENCE   2  (residues 1 to 1236)
  AUTHORS   Wu,Q., Qiu,Y., Guo,J., Yuan,Z., Yang,Y., Zhu,Q., Zhang,Z., Guo,J.,
            Wu,Y., Zhang,J., Huang,D., Tu,K. and Hu,X.
  TITLE     USP40 promotes hepatocellular carcinoma cell proliferation,
            migration and stemness by deubiquitinating and stabilizing Claudin1
  JOURNAL   Biol Direct 19 (1), 13 (2024)
   PUBMED   38308285
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma cell
            proliferation, migration and stemness by deubiquitinating and
            stabilizing Claudin1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1236)
  AUTHORS   Miao,J., Li,L., Shaheen,N., Wei,J., Jacko,A.M., Sundd,P.,
            Taleb,S.J., Mallampalli,R.K., Zhao,Y. and Zhao,J.
  TITLE     The deubiquitinase USP40 preserves endothelial integrity by
            targeting the heat shock protein HSP90beta
  JOURNAL   Exp Mol Med 56 (2), 395-407 (2024)
   PUBMED   38307937
REFERENCE   4  (residues 1 to 1236)
  AUTHORS   Takahashi,S., Fukuhara,D., Kimura,T., Fukutomi,T., Tanaka,E.,
            Mikami,N., Hada,I., Takematsu,H., Nishibori,Y., Akimoto,Y.,
            Kiyonari,H., Abe,T., Huber,O. and Yan,K.
  TITLE     USP40 deubiquitinates HINT1 and stabilizes p53 in podocyte damage
  JOURNAL   Biochem Biophys Res Commun 614, 198-206 (2022)
   PUBMED   35605301
REFERENCE   5  (residues 1 to 1236)
  AUTHORS   An,W., Yao,S., Sun,X., Hou,Z., Lin,Y., Su,L. and Liu,X.
  TITLE     Glucocorticoid modulatory element-binding protein 1 (GMEB1)
            interacts with the de-ubiquitinase USP40 to stabilize CFLARL and
            inhibit apoptosis in human non-small cell lung cancer cells
  JOURNAL   J Exp Clin Cancer Res 38 (1), 181 (2019)
   PUBMED   31046799
  REMARK    GeneRIF: Our findings show the de-ubiquitinase USP40 regulates the
            ubiquitination and degradation of CFLARL; and GMEB1 acts as a
            bridge protein for USP40 and CFLARL. Mechanistically, we found
            GMEB1 inhibits the activation of CASP8 by modulating ubiquitination
            and degradation of CFLARL
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1236)
  AUTHORS   Li,Y., Schrodi,S., Rowland,C., Tacey,K., Catanese,J. and Grupe,A.
  TITLE     Genetic evidence for ubiquitin-specific proteases USP24 and USP40
            as candidate genes for late-onset Parkinson disease
  JOURNAL   Hum Mutat 27 (10), 1017-1023 (2006)
   PUBMED   16917932
  REMARK    GeneRIF: Da suggest that genetic variants in USP40 affect the risk
            for late-onset Parkinson disease (PD), which is consistent with the
            predicted role of the ubiquitination pathway in PD etiology.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1236)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   8  (residues 1 to 1236)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   9  (residues 1 to 1236)
  AUTHORS   Bass,B.L.
  TITLE     RNA editing by adenosine deaminases that act on RNA
  JOURNAL   Annu Rev Biochem 71, 817-846 (2002)
   PUBMED   12045112
  REMARK    Review article
REFERENCE   10 (residues 1 to 1236)
  AUTHORS   Chen,X., Zhang,Y., Douglas,L. and Zhou,P.
  TITLE     UV-damaged DNA-binding proteins are targets of CUL-4A-mediated
            ubiquitination and degradation
  JOURNAL   J Biol Chem 276 (51), 48175-48182 (2001)
   PUBMED   11673459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019072.8 and AC019221.4.
            
            Summary: Modification of cellular proteins by ubiquitin is an
            essential regulatory mechanism controlled by the coordinated action
            of multiple ubiquitin-conjugating and deubiquitinating enzymes.
            USP40 belongs to a large family of cysteine proteases that function
            as deubiquitinating enzymes (Quesada et al., 2004 [PubMed
            14715245]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (3), as well as variant 1, encodes
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3824226.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1236
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..1236
                     /product="ubiquitin carboxyl-terminal hydrolase 40 isoform
                     1"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 40; ubiquitin
                     carboxyl-terminal hydrolase 40;
                     ubiquitin-specific-processing protease 40;
                     deubiquitinating enzyme 40; ubiquitin thioesterase 40;
                     ubiquitin thiolesterase 40"
                     /calculated_mol_wt=140128
     Region          39..344
                     /region_name="peptidase_C19C"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02659"
                     /db_xref="CDD:239124"
     Site            order(45,50,305,323)
                     /site_type="active"
                     /db_xref="CDD:239124"
     Region          1181..1236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVE5.3)"
     CDS             1..1236
                     /gene="USP40"
                     /coded_by="NM_001382295.1:114..3824"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92972.1"
                     /db_xref="GeneID:55230"
                     /db_xref="HGNC:HGNC:20069"
                     /db_xref="MIM:610570"
ORIGIN      
        1 mfgdlfeeey stvsnnqygk gkklktkale ppapreftnl sgirnqggtc ylnsllqtlh
       61 ftpefrealf slgpeelglf edkdkpdakv riiplqlqrl faqlllldqe aastadltds
      121 fgwtsneemr qhdvqelnri lfsaletslv gtsghdliyr lyhgtivnqi vckecknvse
      181 rqedfldltv avknvsgled alwnmyveee vfdcdnlyhc gtcdrlvkaa ksaklrklpp
      241 fltvsllrfn fdfvkceryk etscytfplr inlkpfceqs elddleyiyd lfsviihkgg
      301 cygghyhvyi kdvdhlgnwq fqeekskpdv nlkdlqseee idhplmilka illeeennli
      361 pvdqlgqkll kkigiswnkk yrkqhgplrk flqlhsqifl lssdestvrl lknsslqaes
      421 dfqrndqqif kmlppespgl nnsiscphwf dindskvqpi rekdieqqfq gkesaymlfy
      481 rksqlqrppe aranprygvp chllnemdaa nielqtkrae cdsanntfel hlhlgpqyhf
      541 fngalhpvvs qtesvwdltf dkrktlgdlr qsifqllefw egdmvlsvak lvpaglhiyq
      601 slggdeltlc eteiadgedi fvwngvevgg vhiqtgidce plllnvlhld tssdgekccq
      661 viesphvfpa naevgtvlta laipagvifi nsagcpggeg wtaipkedmr ktfreqglrn
      721 gssiliqdsh ddnslltkee kwvtsmneid wlhvknlcql eseekqvkis atvntmvfdi
      781 rikaikelkl mkeladnscl rpidrngkll cpvpdsytlk eaelkmgssl glclgkapss
      841 sqlflffamg sdvqpgteme ivveetisvr dclklmlkks glqgdawhlr kmdwcyeage
      901 plceedatlk ellicsgdtl lliegqlppl gflkvpiwwy qlqgpsghwe shqdqtncts
      961 swgrvwrats sqgasgnepa qvsllylgdi eisedatlae lksqamtlpp flefgvpspa
     1021 hlrawtverk rpgrllrtdr qplreyklgr rieicleplq kgenlgpqdv llrtqvripg
     1081 ertyapaldl vwnaaqggta gslrqrvadf yrlpvekiei akyfpekfew lpisswnqqi
     1141 tkrkkkkkqd ylqgapyylk dgdtigvknl lidddddfst irddtgkekq kqralgrrks
     1201 qealheqssy ilssaetpar prapetslsi hvgsfr
//
LOCUS       NP_001369230             948 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 40 isoform 8 [Homo sapiens].
ACCESSION   NP_001369230
VERSION     NP_001369230.1
DBSOURCE    REFSEQ: accession NM_001382301.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 948)
  AUTHORS   Mo,H., Li,R., Yang,N., Han,J., Xiao,X., Zhang,Y., Xiao,Z., Jiao,L.,
            Xu,Q. and Tu,K.
  TITLE     USP40 promotes hepatocellular carcinoma progression through a
            YAP/USP40 positive feedback loop
  JOURNAL   Cancer Lett 589, 216832 (2024)
   PUBMED   38537774
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma progression
            through a YAP/USP40 positive feedback loop.
REFERENCE   2  (residues 1 to 948)
  AUTHORS   Wu,Q., Qiu,Y., Guo,J., Yuan,Z., Yang,Y., Zhu,Q., Zhang,Z., Guo,J.,
            Wu,Y., Zhang,J., Huang,D., Tu,K. and Hu,X.
  TITLE     USP40 promotes hepatocellular carcinoma cell proliferation,
            migration and stemness by deubiquitinating and stabilizing Claudin1
  JOURNAL   Biol Direct 19 (1), 13 (2024)
   PUBMED   38308285
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma cell
            proliferation, migration and stemness by deubiquitinating and
            stabilizing Claudin1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 948)
  AUTHORS   Miao,J., Li,L., Shaheen,N., Wei,J., Jacko,A.M., Sundd,P.,
            Taleb,S.J., Mallampalli,R.K., Zhao,Y. and Zhao,J.
  TITLE     The deubiquitinase USP40 preserves endothelial integrity by
            targeting the heat shock protein HSP90beta
  JOURNAL   Exp Mol Med 56 (2), 395-407 (2024)
   PUBMED   38307937
REFERENCE   4  (residues 1 to 948)
  AUTHORS   Takahashi,S., Fukuhara,D., Kimura,T., Fukutomi,T., Tanaka,E.,
            Mikami,N., Hada,I., Takematsu,H., Nishibori,Y., Akimoto,Y.,
            Kiyonari,H., Abe,T., Huber,O. and Yan,K.
  TITLE     USP40 deubiquitinates HINT1 and stabilizes p53 in podocyte damage
  JOURNAL   Biochem Biophys Res Commun 614, 198-206 (2022)
   PUBMED   35605301
REFERENCE   5  (residues 1 to 948)
  AUTHORS   An,W., Yao,S., Sun,X., Hou,Z., Lin,Y., Su,L. and Liu,X.
  TITLE     Glucocorticoid modulatory element-binding protein 1 (GMEB1)
            interacts with the de-ubiquitinase USP40 to stabilize CFLARL and
            inhibit apoptosis in human non-small cell lung cancer cells
  JOURNAL   J Exp Clin Cancer Res 38 (1), 181 (2019)
   PUBMED   31046799
  REMARK    GeneRIF: Our findings show the de-ubiquitinase USP40 regulates the
            ubiquitination and degradation of CFLARL; and GMEB1 acts as a
            bridge protein for USP40 and CFLARL. Mechanistically, we found
            GMEB1 inhibits the activation of CASP8 by modulating ubiquitination
            and degradation of CFLARL
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 948)
  AUTHORS   Li,Y., Schrodi,S., Rowland,C., Tacey,K., Catanese,J. and Grupe,A.
  TITLE     Genetic evidence for ubiquitin-specific proteases USP24 and USP40
            as candidate genes for late-onset Parkinson disease
  JOURNAL   Hum Mutat 27 (10), 1017-1023 (2006)
   PUBMED   16917932
  REMARK    GeneRIF: Da suggest that genetic variants in USP40 affect the risk
            for late-onset Parkinson disease (PD), which is consistent with the
            predicted role of the ubiquitination pathway in PD etiology.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 948)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   8  (residues 1 to 948)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   9  (residues 1 to 948)
  AUTHORS   Bass,B.L.
  TITLE     RNA editing by adenosine deaminases that act on RNA
  JOURNAL   Annu Rev Biochem 71, 817-846 (2002)
   PUBMED   12045112
  REMARK    Review article
REFERENCE   10 (residues 1 to 948)
  AUTHORS   Chen,X., Zhang,Y., Douglas,L. and Zhou,P.
  TITLE     UV-damaged DNA-binding proteins are targets of CUL-4A-mediated
            ubiquitination and degradation
  JOURNAL   J Biol Chem 276 (51), 48175-48182 (2001)
   PUBMED   11673459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019072.8 and AC019221.4.
            
            Summary: Modification of cellular proteins by ubiquitin is an
            essential regulatory mechanism controlled by the coordinated action
            of multiple ubiquitin-conjugating and deubiquitinating enzymes.
            USP40 belongs to a large family of cysteine proteases that function
            as deubiquitinating enzymes (Quesada et al., 2004 [PubMed
            14715245]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..948
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..948
                     /product="ubiquitin carboxyl-terminal hydrolase 40 isoform
                     8"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 40; ubiquitin
                     carboxyl-terminal hydrolase 40;
                     ubiquitin-specific-processing protease 40;
                     deubiquitinating enzyme 40; ubiquitin thioesterase 40;
                     ubiquitin thiolesterase 40"
                     /calculated_mol_wt=107381
     Region          39..344
                     /region_name="peptidase_C19C"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02659"
                     /db_xref="CDD:239124"
     Site            order(45,50,305,323)
                     /site_type="active"
                     /db_xref="CDD:239124"
     CDS             1..948
                     /gene="USP40"
                     /coded_by="NM_001382301.1:119..2965"
                     /note="isoform 8 is encoded by transcript variant 9"
                     /db_xref="GeneID:55230"
                     /db_xref="HGNC:HGNC:20069"
                     /db_xref="MIM:610570"
ORIGIN      
        1 mfgdlfeeey stvsnnqygk gkklktkale ppapreftnl sgirnqggtc ylnsllqtlh
       61 ftpefrealf slgpeelglf edkdkpdakv riiplqlqrl faqlllldqe aastadltds
      121 fgwtsneemr qhdvqelnri lfsaletslv gtsghdliyr lyhgtivnqi vckecknvse
      181 rqedfldltv avknvsgled alwnmyveee vfdcdnlyhc gtcdrlvkaa ksaklrklpp
      241 fltvsllrfn fdfvkceryk etscytfplr inlkpfceqs elddleyiyd lfsviihkgg
      301 cygghyhvyi kdvdhlgnwq fqeekskpdv nlkdlqseee idhplmilka illeeennli
      361 pvdqlgqkll kkigiswnkk yrkqhgplrk flqlhsqifl lssdestvrl lknsslqaes
      421 dfqrndqqif kmlppespgl nnsiscphwf dindskvqpi rekdieqqfq gkesaymlfy
      481 rksqlqrppe aranprygvp chllnemdaa nielqtkrae cdsanntfel hlhlgpqyhf
      541 fngalhpvvs qtesvwdltf dkrktlgdlr qsifqllefw egdmvlsvak lvpaglhiyq
      601 slggdeltlc eteiadgedi fvwngvevgg vhiqtgidce plllnvlhld tssdgekccq
      661 viesphvfpa naevgtvlta laipagvifi nsagcpggeg wtaipkedmr ktfreqglrn
      721 gssiliqdsh ddnslltkee kwvtsmneid wlhvknlcql eseekqvkis atvntmvfdi
      781 rikaikelkl mkeladnscl rpidrngkll cpvpdsytlk eaelkmgssl glclgkapss
      841 sqlflffamg sdvqpgteme ivveetisvr dlcpliqvgk sdqpgssrvp laprlwlpnt
      901 ifykqepghl rimagyisrs gnkmslkhlt itesseaaiq dhwnhqrd
//
LOCUS       NP_001243656             487 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 39 isoform 3 [Homo sapiens].
ACCESSION   NP_001243656
VERSION     NP_001243656.1
DBSOURCE    REFSEQ: accession NM_001256727.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Zhou,F., Li,X., Sun,Y., Wang,Y., Niu,K., Gao,X., Zhang,J., Chen,T.,
            Li,Y., Zhao,W., Mao,B., Xu,Q., Shi,Y. and He,Z.
  TITLE     USP39 at the crossroads of cancer immunity: regulating immune
            evasion and immunotherapy response through RNA splicing and
            ubiquitin signaling
  JOURNAL   Front Immunol 16, 1665775 (2025)
   PUBMED   40990019
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Lu,C., Cai,Y., Wu,S., Wang,Y., Li,J.B., Xu,G. and Ma,J.
  TITLE     Deubiquitinating enzyme USP39 promotes the growth and metastasis of
            gastric cancer cells by modulating the degradation of RNA-binding
            protein RBM39
  JOURNAL   J Biol Chem 300 (10), 107751 (2024)
   PUBMED   39260689
  REMARK    GeneRIF: Deubiquitinating enzyme USP39 promotes the growth and
            metastasis of gastric cancer cells by modulating the degradation of
            RNA-binding protein RBM39.
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Hu,Y., Wang,Y., Hu,W., Hu,C., Wang,B., Liu,C., Deng,A., Shen,B.,
            Wu,K. and Liu,Y.
  TITLE     USP39 Promotes the Viability and Migration of Head and Neck
            Squamous Cell Carcinoma Cell by Regulating STAT1
  JOURNAL   Technol Cancer Res Treat 23, 15330338241250298 (2024)
   PUBMED   38706215
  REMARK    GeneRIF: USP39 Promotes the Viability and Migration of Head and
            Neck Squamous Cell Carcinoma Cell by Regulating STAT1.
REFERENCE   6  (residues 1 to 487)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   7  (residues 1 to 487)
  AUTHORS   van Leuken,R.J., Luna-Vargas,M.P., Sixma,T.K., Wolthuis,R.M. and
            Medema,R.H.
  TITLE     Usp39 is essential for mitotic spindle checkpoint integrity and
            controls mRNA-levels of aurora B
  JOURNAL   Cell Cycle 7 (17), 2710-2719 (2008)
   PUBMED   18728397
  REMARK    GeneRIF: These observations suggest Usp39 to be involved in
            splicing of Aurora B and other mRNAs that are essential for proper
            spindle checkpoint function.
REFERENCE   8  (residues 1 to 487)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   9  (residues 1 to 487)
  AUTHORS   Makarova,O.V., Makarov,E.M. and Luhrmann,R.
  TITLE     The 65 and 110 kDa SR-related proteins of the U4/U6.U5 tri-snRNP
            are essential for the assembly of mature spliceosomes
  JOURNAL   EMBO J 20 (10), 2553-2563 (2001)
   PUBMED   11350945
REFERENCE   10 (residues 1 to 487)
  AUTHORS   Lygerou,Z., Christophides,G. and Seraphin,B.
  TITLE     A novel genetic screen for snRNP assembly factors in yeast
            identifies a conserved protein, Sad1p, also required for pre-mRNA
            splicing
  JOURNAL   Mol Cell Biol 19 (3), 2008-2020 (1999)
   PUBMED   10022888
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB444135.1, AK302236.1, AK001772.1 and BC001384.2.
            
            Transcript Variant: This variant (4) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (3) is shorter and has a distinct N-terminus, compared to isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302236.1, SRR14038195.578346.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p11.2"
     Protein         1..487
                     /product="ubiquitin carboxyl-terminal hydrolase 39 isoform
                     3"
                     /EC_number="3.4.19.12"
                     /note="SnRNP assembly defective 1 homolog; small nuclear
                     ribonucleoprotein 65kDa (U4/U6.U5); ubiquitin specific
                     protease 39; U4/U6.U5 tri-snRNP-associated protein 2;
                     U4/U6.U5 tri-snRNP-associated 65 kDa protein; SAD1
                     homolog; inactive ubiquitin-specific peptidase 39;
                     ubiquitin carboxyl-terminal hydrolase 39"
                     /calculated_mol_wt=56269
     Region          28..475
                     /region_name="Peptidase_C19M"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02669"
                     /db_xref="CDD:239134"
     Site            order(151,156,435,453)
                     /site_type="active"
                     /db_xref="CDD:239134"
     CDS             1..487
                     /gene="USP39"
                     /gene_synonym="65K; CGI-21; HSPC332; SAD1; SNRNP65"
                     /coded_by="NM_001256727.2:222..1685"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS74534.1"
                     /db_xref="GeneID:10713"
                     /db_xref="HGNC:HGNC:20071"
                     /db_xref="MIM:611594"
ORIGIN      
        1 mltavpshlf sakngrvdse drrsrhcpyl dtinrsvldf dfeklcsisl shinayaclv
       61 cgkyfqgrgl kshayihsvq fshhvflnlh tlkfyclpdn yeiidssled ityvlkptft
      121 kqqianldkq aklsraydgt tylpgivgln nikandyana vlqalsnvpp lrnyfleedn
      181 yknikrppgd imfllvqrfg elmrklwnpr nfkahvsphe mlqavvlcsk ktfqitkqgd
      241 gvdflswfln alhsalggtk kkkktivtdv fqgsmriftk klphpdlpae ekeqllhnde
      301 yqetmvestf myltldlpta plykdekeql iipqvplfni lakfngitek eyktykenfl
      361 krfqltklpp ylifcikrft knnffveknp tivnfpitnv dlreylseev qavhknttyd
      421 lianivhdgk psegsyrihv lhhgtgkwye lqdlqvtdil pqmitlseay iqiwkrrdnd
      481 etnqqga
//
LOCUS       NP_001371471             688 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 49 isoform a [Homo sapiens].
ACCESSION   NP_001371471
VERSION     NP_001371471.1
DBSOURCE    REFSEQ: accession NM_001384542.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Campos-Iglesias,D., Fraile,J.M., Bretones,G., Montero,A.A.,
            Bonzon-Kulichenko,E., Vazquez,J., Lopez-Otin,C. and Freije,J.M.P.
  TITLE     USP49 deubiquitinase regulates the mitotic spindle checkpoint and
            prevents aneuploidy
  JOURNAL   Cell Death Dis 14 (1), 60 (2023)
   PUBMED   36702832
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Kaushal,K., Kim,E.J., Tyagi,A., Karapurkar,J.K., Haq,S., Jung,H.S.,
            Kim,K.S. and Ramakrishna,S.
  TITLE     Genome-wide screening for deubiquitinase subfamily identifies
            ubiquitin-specific protease 49 as a novel regulator of
            odontogenesis
  JOURNAL   Cell Death Differ 29 (9), 1689-1704 (2022)
   PUBMED   35273362
  REMARK    GeneRIF: Genome-wide screening for deubiquitinase subfamily
            identifies ubiquitin-specific protease 49 as a novel regulator of
            odontogenesis.
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Matsui,M., Kajita,S., Tsuchiya,Y., Torii,W., Tamekuni,S. and
            Nishi,R.
  TITLE     USP49 is a novel deubiquitylating enzyme for gamma H2AX in DNA
            double-strand break repair
  JOURNAL   Gene 833, 146599 (2022)
   PUBMED   35598681
  REMARK    GeneRIF: USP49 is a novel deubiquitylating enzyme for gamma H2AX in
            DNA double-strand break repair.
REFERENCE   4  (residues 1 to 688)
  AUTHORS   Tu,R., Kang,W., Kang,Y., Chen,Z., Zhang,P., Xiong,X., Ma,J.,
            Du,R.L. and Zhang,C.
  TITLE     c-MYC-USP49-BAG2 axis promotes proliferation and chemoresistance of
            colorectal cancer cells in vitro
  JOURNAL   Biochem Biophys Res Commun 607, 117-123 (2022)
   PUBMED   35367823
  REMARK    GeneRIF: c-MYC-USP49-BAG2 axis promotes proliferation and
            chemoresistance of colorectal cancer cells in vitro.
REFERENCE   5  (residues 1 to 688)
  AUTHORS   Liu,Z., Li,J., Ding,Y., Ma,M., Chen,J., Lei,W., Li,L., Yao,Y.,
            Yu,X., Zhong,M., Liao,Q., Fang,W., Fan,L., Huang,C., Zhong,H.,
            Wen,Q., Fang,Z., Chen,J., Huang,S., Xiong,J., Xiang,X. and Deng,J.
  TITLE     USP49 mediates tumor progression and poor prognosis through a
            YAP1-dependent feedback loop in gastric cancer
  JOURNAL   Oncogene 41 (18), 2555-2570 (2022)
   PUBMED   35318441
  REMARK    GeneRIF: USP49 mediates tumor progression and poor prognosis
            through a YAP1-dependent feedback loop in gastric cancer.
REFERENCE   6  (residues 1 to 688)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   7  (residues 1 to 688)
  AUTHORS   Brognard,J., Sierecki,E., Gao,T. and Newton,A.C.
  TITLE     PHLPP and a second isoform, PHLPP2, differentially attenuate the
            amplitude of Akt signaling by regulating distinct Akt isoforms
  JOURNAL   Mol Cell 25 (6), 917-931 (2007)
   PUBMED   17386267
REFERENCE   8  (residues 1 to 688)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   9  (residues 1 to 688)
  AUTHORS   Sato,S., Tomomori-Sato,C., Banks,C.A., Parmely,T.J., Sorokina,I.,
            Brower,C.S., Conaway,R.C. and Conaway,J.W.
  TITLE     A mammalian homolog of Drosophila melanogaster transcriptional
            coactivator intersex is a subunit of the mammalian Mediator complex
  JOURNAL   J Biol Chem 278 (50), 49671-49674 (2003)
   PUBMED   14576168
REFERENCE   10 (residues 1 to 688)
  AUTHORS   Sato,S., Tomomori-Sato,C., Banks,C.A., Sorokina,I., Parmely,T.J.,
            Kong,S.E., Jin,J., Cai,Y., Lane,W.S., Brower,C.S., Conaway,R.C. and
            Conaway,J.W.
  TITLE     Identification of mammalian Mediator subunits with similarities to
            yeast Mediator subunits Srb5, Srb6, Med11, and Rox3
  JOURNAL   J Biol Chem 278 (17), 15123-15127 (2003)
   PUBMED   12584197
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL160163.24 and AL365205.35.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.802493.1,
                                           SRR14038191.3163549.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..688
                     /product="ubiquitin carboxyl-terminal hydrolase 49 isoform
                     a"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 49; deubiquitinating
                     enzyme 49; ubiquitin-specific-processing protease 49;
                     ubiquitin carboxyl-terminal hydrolase 49; ubiquitin
                     thioesterase 49; ubiquitin thiolesterase 49"
                     /calculated_mol_wt=79067
     Region          26..87
                     /region_name="zf-UBP"
                     /note="Zn-finger in ubiquitin-hydrolases and other
                     protein; pfam02148"
                     /db_xref="CDD:460464"
     Region          169..230
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70CQ1.1)"
     Region          253..654
                     /region_name="UCH"
                     /note="Ubiquitin carboxyl-terminal hydrolase; pfam00443"
                     /db_xref="CDD:425685"
     Site            order(257,262,615,633)
                     /site_type="active"
                     /db_xref="CDD:239125"
     Region          293..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70CQ1.1)"
     CDS             1..688
                     /gene="USP49"
                     /coded_by="NM_001384542.1:194..2260"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS69111.1"
                     /db_xref="GeneID:25862"
                     /db_xref="HGNC:HGNC:20078"
ORIGIN      
        1 mdrckhvgrl rlaqdhsiln pqkwccleca ttesvwaclk cshvacgryi edhalkhfee
       61 tghplamevr dlyvfcylck dyvlndnpeg dlkllrssll avrgqkqdtp vrrgrtlrsm
      121 asgedvvlpq rapqgqpqml talwyrrqrl lartlrlwfe kssrgqakle qrrqeealer
      181 kkeearrrrr evkrrlleel astpprksar lllhtprdag paasrpaalp tsrrvpaatl
      241 klrrqpamap gvtglrnlgn tcymnsilqv lshlqkfrec flnldpskte hlfpkatngk
      301 tqlsgkptns satelslrnd raeaceregf cwngrasisr sleliqnkep sskhislcre
      361 lhtlfrvmws gkwalvspfa mlhsvwslip afrgydqqda qeflcellhk vqqelesegt
      421 trrilipfsq rkltkqvlkv vntifhgqll sqvtciscny ksntiepfwd lslefperyh
      481 ciekgfvpln qtecllteml akfteteale griyacdqcn skrrksnpkp lvlsearkql
      541 miyrlpqvlr lhlkrfrwsg rnhrekigvh vvfdqvltme pyccrdmlss ldketfaydl
      601 savvmhhgkg fgsghytayc ynteggfwvh cndsklnvcs veevcktqay ilfytqrtvq
      661 gnarisethl qaqvqssnnd egrpqtfs
//
LOCUS       NP_874358                631 aa            linear   PRI 27-NOV-2025
DEFINITION  DEAD box protein 53 [Homo sapiens].
ACCESSION   NP_874358 XP_291343
VERSION     NP_874358.2
DBSOURCE    REFSEQ: accession NM_182699.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Scala,M., Bradley,C.A., Howe,J.L., Trost,B., Salazar,N.B., Shum,C.,
            Mendes,M., Reuter,M.S., Anagnostou,E., MacDonald,J.R., Ko,S.Y.,
            Frankland,P.W., Charlebois,J., Elsabbagh,M., Granger,L.,
            Anadiotis,G., Pullano,V., Brusco,A., Keller,R., Parisotto,S.,
            Pedro,H.F., Lusk,L., McDonnell,P.P., Helbig,I., Mullegama,S.V.,
            Douine,E.D., Corona,R.I., Russell,B.E., Nelson,S.F., Graziano,C.,
            Schwab,M., Simone,L., Zara,F. and Scherer,S.W.
  CONSRTM   Undiagnosed Diseases Network
  TITLE     Genetic variants in DDX53 contribute to autism spectrum disorder
            associated with the Xp22.11 locus
  JOURNAL   Am J Hum Genet 112 (1), 154-167 (2025)
   PUBMED   39706195
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Faheem,M., Deneault,E., Alexandrova,R., Rodrigues,D.C.,
            Pellecchia,G., Shum,C., Zarrei,M., Piekna,A., Wei,W., Howe,J.L.,
            Thiruvahindrapuram,B., Lamoureux,S., Ross,P.J., Bradley,C.A.,
            Ellis,J. and Scherer,S.W.
  TITLE     Disruption of DDX53 coding sequence has limited impact on
            iPSC-derived human NGN2 neurons
  JOURNAL   BMC Med Genomics 16 (1), 5 (2023)
   PUBMED   36635662
  REMARK    GeneRIF: Disruption of DDX53 coding sequence has limited impact on
            iPSC-derived human NGN2 neurons.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Park,S.Y., Kim,W.J., Byun,J.H., Lee,J.J., Jeoung,D., Park,S.T. and
            Kim,Y.
  TITLE     Role of DDX53 in taxol-resistance of cervix cancer cells in vitro
  JOURNAL   Biochem Biophys Res Commun 506 (3), 641-647 (2018)
   PUBMED   30454700
  REMARK    GeneRIF: DDX53 plays a critical role in taxol-resistance by
            activating autophagy and a potential therapeutic target for the
            treatment of taxol-resistant cervix cancer.
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Kim,Y., Yeon,M. and Jeoung,D.
  TITLE     DDX53 Regulates Cancer Stem Cell-Like Properties by Binding to
            SOX-2
  JOURNAL   Mol Cells 40 (5), 322-330 (2017)
   PUBMED   28535666
  REMARK    GeneRIF: A novel role of DDX53 in regulating cancer stem cell-like
            properties by binding to SOX-2.DDX53 directly regulates the SOX-2
            expression in drug-resistant melanoma cells.
REFERENCE   6  (residues 1 to 631)
  AUTHORS   Kim,Y. and Jeoung,D.
  TITLE     Role of CAGE, a novel cancer/testis antigen, in various cellular
            processes, including tumorigenesis, cytolytic T lymphocyte
            induction, and cell motility
  JOURNAL   J Microbiol Biotechnol 18 (3), 600-610 (2008)
   PUBMED   18388483
  REMARK    GeneRIF: The CAGE gene is widely expressed in various cancer
            tissues and cancer cell lines.
REFERENCE   7  (residues 1 to 631)
  AUTHORS   Lee,T.S., Kim,J.W., Kang,G.H., Park,N.H., Song,Y.S., Kang,S.B. and
            Lee,H.P.
  TITLE     DNA hypomethylation of CAGE promotors in squamous cell carcinoma of
            uterine cervix
  JOURNAL   Ann N Y Acad Sci 1091, 218-224 (2006)
   PUBMED   17341616
  REMARK    GeneRIF: Hypomethylated CAGE promoter CpG islands are frequently
            involved in uterine cervical carcinogenesis.
REFERENCE   8  (residues 1 to 631)
  AUTHORS   Shim,H., Lee,H. and Jeoung,D.
  TITLE     Cancer/testis antigen cancer-associated gene (CAGE) promotes
            motility of cancer cells through activation of focal adhesion
            kinase (FAK)
  JOURNAL   Biotechnol Lett 28 (24), 2057-2063 (2006)
   PUBMED   17028776
  REMARK    GeneRIF: CAGE promotes motility of cancer cells through activation
            of focal adhesion kinase (FAK).
REFERENCE   9  (residues 1 to 631)
  AUTHORS   Cho,B., Lee,H., Jeong,S., Bang,Y.J., Lee,H.J., Hwang,K.S.,
            Kim,H.Y., Lee,Y.S., Kang,G.H. and Jeoung,D.I.
  TITLE     Promoter hypomethylation of a novel cancer/testis antigen gene CAGE
            is correlated with its aberrant expression and is seen in
            premalignant stage of gastric carcinoma
  JOURNAL   Biochem Biophys Res Commun 307 (1), 52-63 (2003)
   PUBMED   12849980
  REMARK    GeneRIF: results suggest that the methylation status of the CpG
            sites of CAGE determines its expression, and that hypomethylation
            of CAGE precedes the development of gastric cancer and
            hepatocellular carcinoma
REFERENCE   10 (residues 1 to 631)
  AUTHORS   Cho,B., Lim,Y., Lee,D.Y., Park,S.Y., Lee,H., Kim,W.H., Yang,H.,
            Bang,Y.J. and Jeoung,D.I.
  TITLE     Identification and characterization of a novel cancer/testis
            antigen gene CAGE
  JOURNAL   Biochem Biophys Res Commun 292 (3), 715-726 (2002)
   PUBMED   11922625
  REMARK    GeneRIF: CAGE is expressed in a variety of cancers but not in
            normal tissues except testis, and might play a role in cellular
            proliferation.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC117517.7, AY039237.1 and
            BC067878.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 15, 2004 this sequence version replaced NP_874358.1.
            
            Summary: This intronless gene encodes a protein which contains
            several domains found in members of the DEAD-box helicase protein
            family. Other members of this protein family participate in
            ATP-dependent RNA unwinding. [provided by RefSeq, Sep 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC067878.1, AY039237.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327968.7/ ENSP00000368667.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.11"
     Protein         1..631
                     /product="DEAD box protein 53"
                     /EC_number="3.6.4.13"
                     /note="cancer/testis antigen 26; DEAD-box protein CAGE;
                     probable ATP-dependent RNA helicase DDX53;
                     cancer-associated gene protein; DEAD (Asp-Glu-Ala-Asp) box
                     polypeptide 53"
                     /calculated_mol_wt=71023
     Region          50..115
                     /region_name="KH-I_DDX43_DDX53"
                     /note="type I K homology (KH) RNA-binding domain found in
                     DEAD box protein 43 (DDX43), DEAD box protein 53 (DDX53)
                     and similar proteins; cd22430"
                     /db_xref="CDD:411858"
     Site            order(58,60..62,64..68,71..72,75..76,81..84)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411858"
     Region          222..250
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TM3.3)"
     Region          231..625
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Region          376..379
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TM3.3)"
     CDS             1..631
                     /gene="DDX53"
                     /gene_synonym="CAGE; CT26"
                     /coded_by="NM_182699.4:99..1994"
                     /db_xref="CCDS:CCDS35214.1"
                     /db_xref="GeneID:168400"
                     /db_xref="HGNC:HGNC:20083"
                     /db_xref="MIM:301079"
ORIGIN      
        1 mshwapewkr aeanprdlga swdvrgsrgs gwsgpfghqg praagsrepp lcfkiknnmv
       61 gvvigysgsk ikdlqhstnt kiqiingese akvrifgnre mkakakaaie tlirkqesyn
      121 sessvdnaas qtpigrnlgr ndivgeaepl snwdriraav vecekrkwad lppvkknfyi
      181 eskatscmse mqvinwrken fnitcddlks gekrlipkpt crfkdafqqy pdllksiirv
      241 givkptpiqs qawpiilqgi dlivvaqtgt gktlsylmpg fihldsqpis reqrngpgml
      301 vltptrelal hveaecskys ykglksiciy ggrnrngqie diskgvdiii atpgrlndlq
      361 mnnsvnlrsi tylvideadk mldmefepqi rkilldvrpd rqtvmtsatw pdtvrqlals
      421 ylkdpmivyv gnlnlvavnt vkqniivtte kekraltqef venmspndkv imfvsqkhia
      481 ddlssdfniq gisaeslhgn seqsdqerav edfksgniki littdivsrg ldlndvthvy
      541 nydfprnidv yvhrvgyigr tgktgtsvtl itqrdskmag elikildran qsvpedlvvm
      601 aeqyklnqqk rhretrsrkp gqrrkefyfl s
//
LOCUS       NP_001288153             192 aa            linear   PRI 27-NOV-2025
DEFINITION  calcium and integrin-binding family member 2 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001288153 XP_006720436
VERSION     NP_001288153.1
DBSOURCE    REFSEQ: accession NM_001301224.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Wang,X., Yi,Z., Shi,M. and Sun,Y.
  TITLE     The Diverse Functions of the Calcium- and Integrin-Binding Protein
            Family
  JOURNAL   Int J Mol Sci 26 (5), 2223 (2025)
   PUBMED   40076845
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Dal Cortivo,G. and Dell'Orco,D.
  TITLE     Calcium- and Integrin-Binding Protein 2 (CIB2) in Physiology and
            Disease: Bright and Dark Sides
  JOURNAL   Int J Mol Sci 23 (7), 3552 (2022)
   PUBMED   35408910
  REMARK    GeneRIF: Calcium- and Integrin-Binding Protein 2 (CIB2) in
            Physiology and Disease: Bright and Dark Sides.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Liang,X., Qiu,X., Dionne,G., Cunningham,C.L., Pucak,M.L., Peng,G.,
            Kim,Y.H., Lauer,A., Shapiro,L. and Muller,U.
  TITLE     CIB2 and CIB3 are auxiliary subunits of the mechanotransduction
            channel of hair cells
  JOURNAL   Neuron 109 (13), 2131-2149 (2021)
   PUBMED   34089643
  REMARK    GeneRIF: CIB2 and CIB3 are auxiliary subunits of the
            mechanotransduction channel of hair cells.
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Huang,H., Bogstie,J.N. and Vogel,H.J.
  TITLE     Biophysical and structural studies of the human calcium- and
            integrin-binding protein family: understanding their functional
            similarities and differences
  JOURNAL   Biochem Cell Biol 90 (5), 646-656 (2012)
   PUBMED   22779914
  REMARK    GeneRIF: CIB2, as binding partners for the integrin alphaIIb
            subunit, which suggests that they are potentially involved in
            regulating integrin alphaIIb subunit activation.
REFERENCE   6  (residues 1 to 192)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   7  (residues 1 to 192)
  AUTHORS   Ahmad,J., Khan,S.N., Khan,S.Y., Ramzan,K., Riazuddin,S.,
            Ahmed,Z.M., Wilcox,E.R., Friedman,T.B. and Riazuddin,S.
  TITLE     DFNB48, a new nonsyndromic recessive deafness locus, maps to
            chromosome 15q23-q25.1
  JOURNAL   Hum Genet 116 (5), 407-412 (2005)
   PUBMED   15711797
REFERENCE   8  (residues 1 to 192)
  AUTHORS   Seki,N., Hattori,A., Hayashi,A., Kozuma,S., Ohira,M., Hori,T. and
            Saito,T.
  TITLE     Structure, expression profile and chromosomal location of an isolog
            of DNA-PKcs interacting protein (KIP) gene
  JOURNAL   Biochim Biophys Acta 1444 (1), 143-147 (1999)
   PUBMED   9931475
REFERENCE   9  (residues 1 to 192)
  AUTHORS   Li,M., Squire,J.A. and Weksberg,R.
  TITLE     Overgrowth syndromes and genomic imprinting: from mouse to man
  JOURNAL   Clin Genet 53 (3), 165-170 (1998)
   PUBMED   9630066
  REMARK    Review article
REFERENCE   10 (residues 1 to 192)
  AUTHORS   Koenekoop,R.K., Arriaga,M.A., Trzupek,K.M. and Lentz,J.J.
  TITLE     Usher Syndrome Type I
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301442
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC090260.13.
            
            On Jul 29, 2014 this sequence version replaced XP_006720436.1.
            
            Summary: The protein encoded by this gene is similar to that of
            KIP/CIB, calcineurin B, and calmodulin. The encoded protein is a
            calcium-binding regulatory protein that interacts with
            DNA-dependent protein kinase catalytic subunits (DNA-PKcs), and it
            is involved in photoreceptor cell maintenance. Mutations in this
            gene cause deafness, autosomal recessive, 48 (DFNB48), and also
            Usher syndrome 1J (USH1J). Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (4) lacks an alternate exon and
            uses an alternate  in-frame splice site in the 5' coding region,
            compared to variant 1. The encoded isoform (4) is longer than
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.1"
     Protein         1..192
                     /product="calcium and integrin-binding family member 2
                     isoform 4"
                     /note="DNA-dependent protein kinase catalytic
                     subunit-interacting protein 2"
                     /calculated_mol_wt=21543
     Region          112..178
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     CDS             1..192
                     /gene="CIB2"
                     /gene_synonym="DFNB48; KIP2; USH1J"
                     /coded_by="NM_001301224.2:231..809"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:10518"
                     /db_xref="HGNC:HGNC:24579"
                     /db_xref="MIM:605564"
ORIGIN      
        1 mgnkqtifte eqldnyqdct ffnkkdilkw gnrgsegfgh ssrvtqavhs lapgpsclsc
       61 thsdccvcfl qenpfkeriv aafsedgegn ltfndfvdmf svlcesapre lkanyafkiy
      121 dfntdnfick edleltlarl tkseldeeev vlvcdkviee adldgdgklg fadfedmiak
      181 apdflstfhi ri
//
LOCUS       NP_001273483             688 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 49 isoform a [Homo sapiens].
ACCESSION   NP_001273483 XP_005249048
VERSION     NP_001273483.1
DBSOURCE    REFSEQ: accession NM_001286554.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Campos-Iglesias,D., Fraile,J.M., Bretones,G., Montero,A.A.,
            Bonzon-Kulichenko,E., Vazquez,J., Lopez-Otin,C. and Freije,J.M.P.
  TITLE     USP49 deubiquitinase regulates the mitotic spindle checkpoint and
            prevents aneuploidy
  JOURNAL   Cell Death Dis 14 (1), 60 (2023)
   PUBMED   36702832
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Kaushal,K., Kim,E.J., Tyagi,A., Karapurkar,J.K., Haq,S., Jung,H.S.,
            Kim,K.S. and Ramakrishna,S.
  TITLE     Genome-wide screening for deubiquitinase subfamily identifies
            ubiquitin-specific protease 49 as a novel regulator of
            odontogenesis
  JOURNAL   Cell Death Differ 29 (9), 1689-1704 (2022)
   PUBMED   35273362
  REMARK    GeneRIF: Genome-wide screening for deubiquitinase subfamily
            identifies ubiquitin-specific protease 49 as a novel regulator of
            odontogenesis.
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Matsui,M., Kajita,S., Tsuchiya,Y., Torii,W., Tamekuni,S. and
            Nishi,R.
  TITLE     USP49 is a novel deubiquitylating enzyme for gamma H2AX in DNA
            double-strand break repair
  JOURNAL   Gene 833, 146599 (2022)
   PUBMED   35598681
  REMARK    GeneRIF: USP49 is a novel deubiquitylating enzyme for gamma H2AX in
            DNA double-strand break repair.
REFERENCE   4  (residues 1 to 688)
  AUTHORS   Tu,R., Kang,W., Kang,Y., Chen,Z., Zhang,P., Xiong,X., Ma,J.,
            Du,R.L. and Zhang,C.
  TITLE     c-MYC-USP49-BAG2 axis promotes proliferation and chemoresistance of
            colorectal cancer cells in vitro
  JOURNAL   Biochem Biophys Res Commun 607, 117-123 (2022)
   PUBMED   35367823
  REMARK    GeneRIF: c-MYC-USP49-BAG2 axis promotes proliferation and
            chemoresistance of colorectal cancer cells in vitro.
REFERENCE   5  (residues 1 to 688)
  AUTHORS   Liu,Z., Li,J., Ding,Y., Ma,M., Chen,J., Lei,W., Li,L., Yao,Y.,
            Yu,X., Zhong,M., Liao,Q., Fang,W., Fan,L., Huang,C., Zhong,H.,
            Wen,Q., Fang,Z., Chen,J., Huang,S., Xiong,J., Xiang,X. and Deng,J.
  TITLE     USP49 mediates tumor progression and poor prognosis through a
            YAP1-dependent feedback loop in gastric cancer
  JOURNAL   Oncogene 41 (18), 2555-2570 (2022)
   PUBMED   35318441
  REMARK    GeneRIF: USP49 mediates tumor progression and poor prognosis
            through a YAP1-dependent feedback loop in gastric cancer.
REFERENCE   6  (residues 1 to 688)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   7  (residues 1 to 688)
  AUTHORS   Brognard,J., Sierecki,E., Gao,T. and Newton,A.C.
  TITLE     PHLPP and a second isoform, PHLPP2, differentially attenuate the
            amplitude of Akt signaling by regulating distinct Akt isoforms
  JOURNAL   Mol Cell 25 (6), 917-931 (2007)
   PUBMED   17386267
REFERENCE   8  (residues 1 to 688)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   9  (residues 1 to 688)
  AUTHORS   Sato,S., Tomomori-Sato,C., Banks,C.A., Parmely,T.J., Sorokina,I.,
            Brower,C.S., Conaway,R.C. and Conaway,J.W.
  TITLE     A mammalian homolog of Drosophila melanogaster transcriptional
            coactivator intersex is a subunit of the mammalian Mediator complex
  JOURNAL   J Biol Chem 278 (50), 49671-49674 (2003)
   PUBMED   14576168
REFERENCE   10 (residues 1 to 688)
  AUTHORS   Sato,S., Tomomori-Sato,C., Banks,C.A., Sorokina,I., Parmely,T.J.,
            Kong,S.E., Jin,J., Cai,Y., Lane,W.S., Brower,C.S., Conaway,R.C. and
            Conaway,J.W.
  TITLE     Identification of mammalian Mediator subunits with similarities to
            yeast Mediator subunits Srb5, Srb6, Med11, and Rox3
  JOURNAL   J Biol Chem 278 (17), 15123-15127 (2003)
   PUBMED   12584197
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL160163.24 and AL365205.35.
            
            On Nov 8, 2013 this sequence version replaced XP_005249048.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3945750.1,
                                           SRR14372079.2797058.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000682992.1/ ENSP00000507239.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..688
                     /product="ubiquitin carboxyl-terminal hydrolase 49 isoform
                     a"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 49; deubiquitinating
                     enzyme 49; ubiquitin-specific-processing protease 49;
                     ubiquitin carboxyl-terminal hydrolase 49; ubiquitin
                     thioesterase 49; ubiquitin thiolesterase 49"
                     /calculated_mol_wt=79067
     Region          26..87
                     /region_name="zf-UBP"
                     /note="Zn-finger in ubiquitin-hydrolases and other
                     protein; pfam02148"
                     /db_xref="CDD:460464"
     Region          169..230
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70CQ1.1)"
     Region          253..654
                     /region_name="UCH"
                     /note="Ubiquitin carboxyl-terminal hydrolase; pfam00443"
                     /db_xref="CDD:425685"
     Site            order(257,262,615,633)
                     /site_type="active"
                     /db_xref="CDD:239125"
     Region          293..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70CQ1.1)"
     CDS             1..688
                     /gene="USP49"
                     /coded_by="NM_001286554.2:237..2303"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS69111.1"
                     /db_xref="GeneID:25862"
                     /db_xref="HGNC:HGNC:20078"
ORIGIN      
        1 mdrckhvgrl rlaqdhsiln pqkwccleca ttesvwaclk cshvacgryi edhalkhfee
       61 tghplamevr dlyvfcylck dyvlndnpeg dlkllrssll avrgqkqdtp vrrgrtlrsm
      121 asgedvvlpq rapqgqpqml talwyrrqrl lartlrlwfe kssrgqakle qrrqeealer
      181 kkeearrrrr evkrrlleel astpprksar lllhtprdag paasrpaalp tsrrvpaatl
      241 klrrqpamap gvtglrnlgn tcymnsilqv lshlqkfrec flnldpskte hlfpkatngk
      301 tqlsgkptns satelslrnd raeaceregf cwngrasisr sleliqnkep sskhislcre
      361 lhtlfrvmws gkwalvspfa mlhsvwslip afrgydqqda qeflcellhk vqqelesegt
      421 trrilipfsq rkltkqvlkv vntifhgqll sqvtciscny ksntiepfwd lslefperyh
      481 ciekgfvpln qtecllteml akfteteale griyacdqcn skrrksnpkp lvlsearkql
      541 miyrlpqvlr lhlkrfrwsg rnhrekigvh vvfdqvltme pyccrdmlss ldketfaydl
      601 savvmhhgkg fgsghytayc ynteggfwvh cndsklnvcs veevcktqay ilfytqrtvq
      661 gnarisethl qaqvqssnnd egrpqtfs
//
LOCUS       NP_001269421             230 aa            linear   PRI 27-NOV-2025
DEFINITION  armadillo-like helical domain-containing protein 2 [Homo sapiens].
ACCESSION   NP_001269421 XP_005249567 XP_005276041 XP_005276329
VERSION     NP_001269421.1
DBSOURCE    REFSEQ: accession NM_001282492.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Zhao,Q., Lin,S., Kang,H., Ru,Y., Xu,Q., Yu,Z., Huang,X., De
            Rito,C., Sassi,G., Wang,S., Sun,S., Sun,R., Cheng,H., Zhu,Y.,
            Liu,M., Zhang,Y., Jiang,M., Percudani,R., Chung,J.J., Zeng,X.,
            Yan,Z. and Wu,J.
  TITLE     ARMH2 is a cytosolic component of CatSper crucial for sperm
            function
  JOURNAL   Nat Commun 16 (1), 10243 (2025)
   PUBMED   41271765
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL512428.13 and AL133264.10.
            
            On or before Sep 12, 2013 this sequence version replaced
            XP_005249567.1, XP_005276041.1, XP_005276329.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            CCDS Note: This CCDS representation lacks full-length human
            transcript support and it is therefore inferred. Th full-length
            exon combination is inferred from partial human transcripts and
            RNA-seq data.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.363521.1,
                                           SRR5189667.336606.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000565469.4/ ENSP00000454913.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.3"
     Protein         1..230
                     /product="armadillo-like helical domain-containing protein
                     2"
                     /note="uncharacterized protein C6orf229"
                     /calculated_mol_wt=26416
     Region          1..229
                     /region_name="ARMH2"
                     /note="Armadillo-like helical domain-containing protein 2;
                     pfam17822"
                     /db_xref="CDD:465520"
     CDS             1..230
                     /gene="ARMH2"
                     /gene_synonym="C6orf229"
                     /coded_by="NM_001282492.2:61..753"
                     /db_xref="CCDS:CCDS64366.1"
                     /db_xref="GeneID:101928603"
                     /db_xref="HGNC:HGNC:49394"
ORIGIN      
        1 mansrfsctq iwvkmygyfa glcrrlqkfw rvtvkgffvk kkekkipsae tyfheekivv
       61 lgqvlmnesl piekraqaaq kigllaftgg ppagnfaaey meevahllqd eelapkikil
      121 llqsvacwcy lnpvsqkrak slqfipilis ffegrfesti ksetnsylll kfwtcyvlsv
      181 mtcnnlscvk elkdhsalky hlqmlaaenw sgwtenfaev lyfligfhrn
//
LOCUS       NP_060224               1440 aa            linear   PRI 27-NOV-2025
DEFINITION  bridge-like lipid transfer protein family member 3A [Homo sapiens].
ACCESSION   NP_060224
VERSION     NP_060224.3
DBSOURCE    REFSEQ: accession NM_017754.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1440)
  AUTHORS   Hanna,M.G., Rodriguez Cruz,H.O., Fujise,K., Wu,Y., Xu,C.S.,
            Pang,S., Li,Z., Monetti,M. and De Camilli,P.
  TITLE     BLTP3A is associated with membranes of the late endocytic pathway
            and is an effector of CASM
  JOURNAL   EMBO J 44 (21), 6168-6195 (2025)
   PUBMED   40935891
REFERENCE   2  (residues 1 to 1440)
  AUTHORS   Hanna,M.G., Suen,P.H., Wu,Y., Reinisch,K.M. and De Camilli,P.
  TITLE     SHIP164 is a chorein motif lipid transfer protein that controls
            endosome-Golgi membrane traffic
  JOURNAL   J Cell Biol 221 (6) (2022)
   PUBMED   35499567
REFERENCE   3  (residues 1 to 1440)
  AUTHORS   Dan,W., Shi,L., Wang,L., Wu,D., Huang,X. and Zhong,Y.
  TITLE     PP7080 expedites the proliferation and migration of lung
            adenocarcinoma cells via sponging miR-670-3p and regulating
            UHRF1BP1
  JOURNAL   J Gene Med 23 (8), e3341 (2021)
   PUBMED   33844396
  REMARK    GeneRIF: PP7080 expedites the proliferation and migration of lung
            adenocarcinoma cells via sponging miR-670-3p and regulating
            UHRF1BP1.
REFERENCE   4  (residues 1 to 1440)
  AUTHORS   Wen,L., Liu,L., Shen,X., Li,H., Zhu,Z., Huang,H., Cai,M., Qian,D.,
            Shen,S., Qiu,Y., Cui,Y. and Sheng,Y.
  TITLE     The association of the UHRF1BP1 gene with systemic lupus
            erythematosus was replicated in a Han Chinese population from
            mainland China
  JOURNAL   Ann Hum Genet 84 (3), 221-228 (2020)
   PUBMED   31691269
  REMARK    GeneRIF: The association of the UHRF1BP1 gene with systemic lupus
            erythematosus was replicated in a Han Chinese population from
            mainland China.
REFERENCE   5  (residues 1 to 1440)
  AUTHORS   El Baroudi,M., Machiels,J.P. and Schmitz,S.
  TITLE     Expression of SESN1, UHRF1BP1, and miR-377-3p as prognostic markers
            in mutated TP53 squamous cell carcinoma of the head and neck
  JOURNAL   Cancer Biol Ther 18 (10), 775-782 (2017)
   PUBMED   28886272
  REMARK    GeneRIF: Study shows that SESN1 mRNA, UHRF1BP11 mRNA and
            miRNA-377-3p levels are prognostically relevant in human
            papillomavirus-negative head and neck squamous cell carcinoma
            patients.
            Review article
REFERENCE   6  (residues 1 to 1440)
  AUTHORS   Zhang,Y., Yang,W., Mok,C.C., Chan,T.M., Wong,R.W., Mok,M.Y.,
            Lee,K.W., Wong,S.N., Leung,A.M., Lee,T.L., Ho,M.H., Lee,P.P.,
            Wong,W.H., Yang,J., Zhang,J., Wong,C.M., Ng,I.O.,
            Garcia-Barcelo,M.M., Cherny,S.S., Tam,P.K., Sham,P.C., Lau,C.S. and
            Lau,Y.L.
  TITLE     Two missense variants in UHRF1BP1 are independently associated with
            systemic lupus erythematosus in Hong Kong Chinese
  JOURNAL   Genes Immun 12 (3), 231-234 (2011)
   PUBMED   21326321
  REMARK    GeneRIF: Cross-population confirmation establishes the involvement
            of UHRF1BP1 locus in SLE and indicates that distinct alleles are
            contributing to disease susceptibility.
REFERENCE   7  (residues 1 to 1440)
  AUTHORS   Orozco,G., Eyre,S., Hinks,A., Bowes,J., Morgan,A.W., Wilson,A.G.,
            Wordsworth,P., Steer,S., Hocking,L., Thomson,W., Worthington,J. and
            Barton,A.
  CONSRTM   UKRAG consortium
  TITLE     Study of the common genetic background for rheumatoid arthritis and
            systemic lupus erythematosus
  JOURNAL   Ann Rheum Dis 70 (3), 463-468 (2011)
   PUBMED   21068098
  REMARK    GeneRIF: Observational study and meta-analysis of gene-disease
            association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 1440)
  AUTHORS   Gateva,V., Sandling,J.K., Hom,G., Taylor,K.E., Chung,S.A., Sun,X.,
            Ortmann,W., Kosoy,R., Ferreira,R.C., Nordmark,G., Gunnarsson,I.,
            Svenungsson,E., Padyukov,L., Sturfelt,G., Jonsen,A.,
            Bengtsson,A.A., Rantapaa-Dahlqvist,S., Baechler,E.C., Brown,E.E.,
            Alarcon,G.S., Edberg,J.C., Ramsey-Goldman,R., McGwin,G. Jr.,
            Reveille,J.D., Vila,L.M., Kimberly,R.P., Manzi,S., Petri,M.A.,
            Lee,A., Gregersen,P.K., Seldin,M.F., Ronnblom,L., Criswell,L.A.,
            Syvanen,A.C., Behrens,T.W. and Graham,R.R.
  TITLE     A large-scale replication study identifies TNIP1, PRDM1, JAZF1,
            UHRF1BP1 and IL10 as risk loci for systemic lupus erythematosus
  JOURNAL   Nat Genet 41 (11), 1228-1233 (2009)
   PUBMED   19838195
  REMARK    GeneRIF: identified five new systemic lupus erythematosus
            susceptibility loci (P < 5 x 10(-8)): TNIP1 (odds ratio (OR) =
            1.27), PRDM1 (OR = 1.20), JAZF1 (OR = 1.20), UHRF1BP1 (OR = 1.17)
            and IL10 (OR = 1.19).
            GeneRIF: Observational study and meta-analysis of gene-disease
            association. (HuGE Navigator)
REFERENCE   9  (residues 1 to 1440)
  AUTHORS   Unoki,M., Nishidate,T. and Nakamura,Y.
  TITLE     ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG
            through its SRA domain
  JOURNAL   Oncogene 23 (46), 7601-7610 (2004)
   PUBMED   15361834
REFERENCE   10 (residues 1 to 1440)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB636320.1, AB126777.1, AL033520.16 and AA287944.1.
            
            On Mar 28, 2007 this sequence version replaced NP_060224.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.71702.1, AB126777.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000192788.6/ ENSP00000192788.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1440
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..1440
                     /product="bridge-like lipid transfer protein family member
                     3A"
                     /note="UHRF1 (ICBP90) binding protein 1; ICBP90 binding
                     protein 1; ubiquitin-like containing PHD and RING finger
                     domains 1-binding protein 1; UHRF1 binding protein 1"
                     /calculated_mol_wt=159355
     Region          1..>96
                     /region_name="Chorein_N"
                     /note="N-terminal region of Chorein or VPS13; pfam12624"
                     /db_xref="CDD:463646"
     Region          267..307
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6BDS2.1)"
     Region          430..456
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6BDS2.1)"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6BDS2.1)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6BDS2.1)"
     Region          751..780
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6BDS2.1)"
     Site            755
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6BDS2.1)"
     Site            758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6BDS2.1)"
     Region          891..1008
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6BDS2.1)"
     Site            988
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6BDS2.1)"
     Site            1103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6BDS2.1)"
     Region          1106..1180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6BDS2.1)"
     Site            1106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6BDS2.1)"
     CDS             1..1440
                     /gene="BLTP3A"
                     /gene_synonym="C6orf107; dJ349A12.1; ICBP90; SHIP164B;
                     UHRF1BP1"
                     /coded_by="NM_017754.4:169..4491"
                     /db_xref="CCDS:CCDS43455.1"
                     /db_xref="GeneID:54887"
                     /db_xref="HGNC:HGNC:21216"
                     /db_xref="MIM:619570"
ORIGIN      
        1 magiikkqil khlsrftknl spdkinlstl kgegqltnle ldeevlqnvl elptwlaitr
       61 vycnrasiri qwtklkthpi clcldkveve mktcedprpp ngqspialas gqseygfaek
      121 vvegmfiivn sitikihska fhasfelwql qgysvnpnwq qsdlrltrit dpcrgevltf
      181 keitwqtlri eadatdngdq dpvttplrli tnqgriqial krrtkdcnvi ssklmflldd
      241 llwvltdsql kammkyaesl seameksahq rkslapepvq itppapsaqq swaqafggsq
      301 gnsnssssrl sqyfekfdvk essyhllisr ldlhicddsq srepgvsanr lmggamqltf
      361 rkmafdyypf hwagdsckhw vrhceametr gqwaqklvme fqskmekwhe etglkppwhl
      421 gvdslfrrka dslssprknp lerspsqgrq pafqppawnr lrsscmvvrv ddldihqvst
      481 agqpskkpst llscsrklhn lptqvsaihi efteyyfpdn qelpvpcpnl yiqlngltft
      541 mdpvsllwgn lfcldlyrsl eqfkaiykle dssqkdehld irldafwlkv sfplekrera
      601 elhrpqalvf sasgmiatnt rhaphcscsd lqslfrgfaa aeffhsnydh fpkvpggfsl
      661 lhmlflhhaf qmdsclpqpn tlppqrpkas wdlwsvhftq isldfegten fkghtlnfva
      721 pfplsiwacl plrwqqaqar klllasegrl kpsasfgspv qsealapdsm shprsktehd
      781 lkslsgltev meilkegssg mdnkgpltel edvadvhmlv hspahvrvrl dhyqylallr
      841 lkevlqrlqe qltkdtesmt gsplqnqtac igvlfpsaev allmhpapga vdadsagsds
      901 tslvdselsp sedrelksda ssdqgpaspe kvleessien qdvsqerphs ngelqdsgpl
      961 aqqlagkghe aveslqakkl srtqassspa alkppagret avngqgelip lkniegelss
     1021 aihmtkdatk ealhatmdlt keavsltkda fslgrdrmts tmhkmlslpp akepmaktde
     1081 gvaapvsgga arlrffsmkr tvsqqsfdgv sldssgpedr isvdsdgsds fvmllesesg
     1141 pesvppgsls nvsdnagvqg splvnnygqg spaanssvsp sgedlifhpv svlvlkvnev
     1201 sfgievrged ltvalqaeel tlqqlgtvgl wqflhgqcpg tcfqesstlk tghirpavgl
     1261 rfevgpgaav hsplasqngf lhlllhgcdl elltsvlsgl gpfledeeip vvvpmqiell
     1321 nssitlkddi ppiyptspgp ipitlamehv vlkrsddgvf higaaaqdkp saevlksekr
     1381 qppkeqvflv ptgevfeqqv kelpilqkel ietkqalana nqdkekllqe irkynpffel
//
LOCUS       NP_006375                191 aa            linear   PRI 27-NOV-2025
DEFINITION  calcium and integrin-binding protein 1 isoform b [Homo sapiens].
ACCESSION   NP_006375
VERSION     NP_006375.2
DBSOURCE    REFSEQ: accession NM_006384.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Wang,X., Yi,Z., Shi,M. and Sun,Y.
  TITLE     The Diverse Functions of the Calcium- and Integrin-Binding Protein
            Family
  JOURNAL   Int J Mol Sci 26 (5), 2223 (2025)
   PUBMED   40076845
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Xu,M.H., Zheng,Y.M., Liang,B.G., Xu,W.X., Cao,J., Wang,P.,
            Dong,Z.Y., Zhou,C.H., Sun,H.C., Ren,N., Ke,A.W. and Shen,Y.H.
  TITLE     Deubiquitination of CIB1 by USP14 promotes lenvatinib resistance
            via the PAK1-ERK1/2 axis in hepatocellular carcinoma
  JOURNAL   Int J Biol Sci 20 (9), 3269-3284 (2024)
   PUBMED   38993552
  REMARK    GeneRIF: Deubiquitination of CIB1 by USP14 promotes lenvatinib
            resistance via the PAK1-ERK1/2 axis in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Wang,C., Felli,E., Selicean,S., Nulan,Y., Lozano,J.J.,
            Guixe-Muntet,S., Bosch,J., Berzigotti,A. and Gracia-Sancho,J.
  TITLE     Role of calcium integrin-binding protein 1 in the mechanobiology of
            the liver endothelium
  JOURNAL   J Cell Physiol 239 (5), e31198 (2024)
   PUBMED   38451745
  REMARK    GeneRIF: Role of calcium integrin-binding protein 1 in the
            mechanobiology of the liver endothelium.
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Ma,J., Song,Y., Zhuang,T., Yang,H., Yang,X., Zheng,J., Luo,J.,
            Xia,Y., Fei,X., Chan,D.W., Wu,D., Xu,P., Ni,P., Dai,J., Xu,D. and
            Hu,Y.
  TITLE     Identification of calcium and integrin-binding protein 1 as a
            reprogrammed glucose metabolism mediator to restrict immune cell
            infiltration in the stromal compartment of pancreatic ductal
            adenocarcinoma
  JOURNAL   Front Immunol 14, 1158964 (2023)
   PUBMED   37187730
  REMARK    GeneRIF: Identification of calcium and integrin-binding protein 1
            as a reprogrammed glucose metabolism mediator to restrict immune
            cell infiltration in the stromal compartment of pancreatic ductal
            adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Jacob,S., Bosch,F., Schoenberg,M.B., Pretzsch,E., Lampert,C.,
            Haoyu,R., Renz,B.W., Michl,M., Kumbrink,J., Kirchner,T., Werner,J.,
            Angele,M.K. and Neumann,J.
  TITLE     Expression of CIB1 correlates with colorectal liver metastases but
            not with peritoneal carcinomatosis
  JOURNAL   BMC Cancer 21 (1), 1243 (2021)
   PUBMED   34794407
  REMARK    GeneRIF: Expression of CIB1 correlates with colorectal liver
            metastases but not with peritoneal carcinomatosis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Armacki,M., Joodi,G., Nimmagadda,S.C., de Kimpe,L., Pusapati,G.V.,
            Vandoninck,S., Van Lint,J., Illing,A. and Seufferlein,T.
  TITLE     A novel splice variant of calcium and integrin-binding protein 1
            mediates protein kinase D2-stimulated tumour growth by regulating
            angiogenesis
  JOURNAL   Oncogene 33 (9), 1167-1180 (2014)
   PUBMED   23503467
  REMARK    GeneRIF: CIB1a is a novel mediator of PKD2-driven carcinogenesis.
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Stabler,S.M., Ostrowski,L.L., Janicki,S.M. and Monteiro,M.J.
  TITLE     A myristoylated calcium-binding protein that preferentially
            interacts with the Alzheimer's disease presenilin 2 protein
  JOURNAL   J Cell Biol 145 (6), 1277-1292 (1999)
   PUBMED   10366599
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Seki,N., Hayashi,A., Abe,M., Araki,R., Fujimori,A., Fukumura,R.,
            Hattori,A., Kozuma,S., Ohhira,M., Hori,T. and Saito,T.
  TITLE     Chromosomal assignment of the gene for human DNA-PKcs interacting
            protein (KIP) on chromosome 15q25.3-q26.1 by somatic hybrid
            analysis and fluorescence in situ hybridization
  JOURNAL   J Hum Genet 43 (4), 275-277 (1998)
   PUBMED   9852683
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Wu,X. and Lieber,M.R.
  TITLE     Interaction between DNA-dependent protein kinase and a novel
            protein, KIP
  JOURNAL   Mutat Res 385 (1), 13-20 (1997)
   PUBMED   9372844
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Naik,U.P., Patel,P.M. and Parise,L.V.
  TITLE     Identification of a novel calcium-binding protein that interacts
            with the integrin alphaIIb cytoplasmic domain
  JOURNAL   J Biol Chem 272 (8), 4651-4654 (1997)
   PUBMED   9030514
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD622547.1, U82226.1,
            AA769426.1 and AC091167.19.
            
            On Dec 20, 2007 this sequence version replaced NP_006375.1.
            
            Summary: This gene encodes a member of the EF-hand
            domain-containing calcium-binding superfamily. The encoded protein
            interacts with many other proteins, including the platelet integrin
            alpha-IIb-beta-3, DNA-dependent protein kinase, presenilin-2, focal
            adhesion kinase, p21 activated kinase, and protein kinase D. The
            encoded protein may be involved in cell survival and proliferation,
            and is associated with several disease states including cancer and
            Alzheimer's disease. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Apr 2013].
            
            Transcript Variant: This variant (b) uses an alternate splice site
            in the coding region, compared to variant a. The encoded isoform
            (b, also known as CIB1) is shorter, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.570233.1,
                                           SRR7346977.191440.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000328649.11/ ENSP00000333873.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.1"
     Protein         1..191
                     /product="calcium and integrin-binding protein 1 isoform
                     b"
                     /note="DNA-dependent protein kinase interacting protein;
                     DNA-PKcs-interacting protein; SNK-interacting protein
                     2-28; testicular secretory protein Li 9; DNA-PK
                     interaction protein; calcium and integrin binding 1
                     (calmyrin)"
                     /calculated_mol_wt=21572
     Region          83..132
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cl08302"
                     /db_xref="CDD:415501"
     Region          111..178
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cd00051"
                     /db_xref="CDD:238008"
     Site            order(116,118,120,127,161,163,165,172)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238008"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23503467; propagated from
                     UniProtKB/Swiss-Prot (Q99828.4)"
     CDS             1..191
                     /gene="CIB1"
                     /gene_synonym="CIB; CIBP; EV3; KIP1; PRKDCIP; SIP2-28"
                     /coded_by="NM_006384.4:57..632"
                     /note="isoform b is encoded by transcript variant b"
                     /db_xref="CCDS:CCDS10360.1"
                     /db_xref="GeneID:10519"
                     /db_xref="HGNC:HGNC:16920"
                     /db_xref="MIM:602293"
ORIGIN      
        1 mggsgsrlsk ellaeyqdlt fltkqeilla hrrfcellpq eqrsvesslr aqvpfeqils
       61 lpelkanpfk ericrvfsts pakdslsfed fldllsvfsd tatpdikshy afrifdfddd
      121 gtlnredlsr lvncltgege dtrlsasemk qlidnilees didrdgtinl sefqhvisrs
      181 pdfassfkiv l
//
LOCUS       NP_001243655             488 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 39 isoform 2 [Homo sapiens].
ACCESSION   NP_001243655
VERSION     NP_001243655.1
DBSOURCE    REFSEQ: accession NM_001256726.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Zhou,F., Li,X., Sun,Y., Wang,Y., Niu,K., Gao,X., Zhang,J., Chen,T.,
            Li,Y., Zhao,W., Mao,B., Xu,Q., Shi,Y. and He,Z.
  TITLE     USP39 at the crossroads of cancer immunity: regulating immune
            evasion and immunotherapy response through RNA splicing and
            ubiquitin signaling
  JOURNAL   Front Immunol 16, 1665775 (2025)
   PUBMED   40990019
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Lu,C., Cai,Y., Wu,S., Wang,Y., Li,J.B., Xu,G. and Ma,J.
  TITLE     Deubiquitinating enzyme USP39 promotes the growth and metastasis of
            gastric cancer cells by modulating the degradation of RNA-binding
            protein RBM39
  JOURNAL   J Biol Chem 300 (10), 107751 (2024)
   PUBMED   39260689
  REMARK    GeneRIF: Deubiquitinating enzyme USP39 promotes the growth and
            metastasis of gastric cancer cells by modulating the degradation of
            RNA-binding protein RBM39.
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   5  (residues 1 to 488)
  AUTHORS   Hu,Y., Wang,Y., Hu,W., Hu,C., Wang,B., Liu,C., Deng,A., Shen,B.,
            Wu,K. and Liu,Y.
  TITLE     USP39 Promotes the Viability and Migration of Head and Neck
            Squamous Cell Carcinoma Cell by Regulating STAT1
  JOURNAL   Technol Cancer Res Treat 23, 15330338241250298 (2024)
   PUBMED   38706215
  REMARK    GeneRIF: USP39 Promotes the Viability and Migration of Head and
            Neck Squamous Cell Carcinoma Cell by Regulating STAT1.
REFERENCE   6  (residues 1 to 488)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   7  (residues 1 to 488)
  AUTHORS   van Leuken,R.J., Luna-Vargas,M.P., Sixma,T.K., Wolthuis,R.M. and
            Medema,R.H.
  TITLE     Usp39 is essential for mitotic spindle checkpoint integrity and
            controls mRNA-levels of aurora B
  JOURNAL   Cell Cycle 7 (17), 2710-2719 (2008)
   PUBMED   18728397
  REMARK    GeneRIF: These observations suggest Usp39 to be involved in
            splicing of Aurora B and other mRNAs that are essential for proper
            spindle checkpoint function.
REFERENCE   8  (residues 1 to 488)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   9  (residues 1 to 488)
  AUTHORS   Makarova,O.V., Makarov,E.M. and Luhrmann,R.
  TITLE     The 65 and 110 kDa SR-related proteins of the U4/U6.U5 tri-snRNP
            are essential for the assembly of mature spliceosomes
  JOURNAL   EMBO J 20 (10), 2553-2563 (2001)
   PUBMED   11350945
REFERENCE   10 (residues 1 to 488)
  AUTHORS   Lygerou,Z., Christophides,G. and Seraphin,B.
  TITLE     A novel genetic screen for snRNP assembly factors in yeast
            identifies a conserved protein, Sad1p, also required for pre-mRNA
            splicing
  JOURNAL   Mol Cell Biol 19 (3), 2008-2020 (1999)
   PUBMED   10022888
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB124294.1, AK001047.1, AL519827.3 and AI201523.1.
            
            Transcript Variant: This variant (3) lacks an exon in the 3' coding
            region, which results in a frameshift, compared to variant 1. The
            encoded isoform (2) is shorter and has a distinct C-terminus,
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001047.1, SRR14038197.1636421.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p11.2"
     Protein         1..488
                     /product="ubiquitin carboxyl-terminal hydrolase 39 isoform
                     2"
                     /EC_number="3.4.19.12"
                     /note="SnRNP assembly defective 1 homolog; small nuclear
                     ribonucleoprotein 65kDa (U4/U6.U5); ubiquitin specific
                     protease 39; U4/U6.U5 tri-snRNP-associated protein 2;
                     U4/U6.U5 tri-snRNP-associated 65 kDa protein; SAD1
                     homolog; inactive ubiquitin-specific peptidase 39;
                     ubiquitin carboxyl-terminal hydrolase 39"
                     /calculated_mol_wt=56228
     Region          1..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GS9.2)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53GS9.2)"
     Region          75..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GS9.2)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q53GS9.2)"
     Region          106..477
                     /region_name="Peptidase_C19M"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02669"
                     /db_xref="CDD:239134"
     CDS             1..488
                     /gene="USP39"
                     /gene_synonym="65K; CGI-21; HSPC332; SAD1; SNRNP65"
                     /coded_by="NM_001256726.2:11..1477"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58717.1"
                     /db_xref="GeneID:10713"
                     /db_xref="HGNC:HGNC:20071"
                     /db_xref="MIM:611594"
ORIGIN      
        1 msgrskresr gstrgkrese srgssgrvkr erdrerepea assrgspvrv krefepasar
       61 eapasvvpfv rvkrerevde dseperevra kngrvdsedr rsrhcpyldt inrsvldfdf
      121 eklcsislsh inayaclvcg kyfqgrglks hayihsvqfs hhvflnlhtl kfyclpdnye
      181 iidssledit yvlkptftkq qianldkqak lsraydgtty lpgivglnni kandyanavl
      241 qalsnvpplr nyfleednyk nikrppgdim fllvqrfgel mrklwnprnf kahvspheml
      301 qavvlcskkt fqitkqgdgv dflswflnal hsalggtkkk kktivtdvfq gsmriftkkl
      361 phpdlpaeek eqllhndeyq etmvestfmy ltldlptapl ykdekeqlii pqvplfnila
      421 kfngitekey ktykenflkr fqltklppyl ifcikrftkn nffveknpti vnfpitgqan
      481 gmnyktsr
//
LOCUS       NP_001269886             284 aa            linear   PRI 27-NOV-2025
DEFINITION  cilia- and flagella-associated protein 77 isoform 2 [Homo sapiens].
ACCESSION   NP_001269886 XP_005272255
VERSION     NP_001269886.1
DBSOURCE    REFSEQ: accession NM_001282957.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Xia,L., Yin,G.L., Long,Y., Sun,F., Wang,B.B., Zhu,Y. and Chen,S.R.
  TITLE     The core outer junction protein CFAP77 connects A- and B-tubules
            within doublet microtubules of cilia and flagella
  JOURNAL   PLoS Biol 23 (10), e3003442 (2025)
   PUBMED   41118442
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Gui,M., Croft,J.T., Zabeo,D., Acharya,V., Kollman,J.M.,
            Burgoyne,T., Hoog,J.L. and Brown,A.
  TITLE     SPACA9 is a lumenal protein of human ciliary singlet and doublet
            microtubules
  JOURNAL   Proc Natl Acad Sci U S A 119 (41), e2207605119 (2022)
   PUBMED   36191189
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Blackburn,K., Bustamante-Marin,X., Yin,W., Goshe,M.B. and
            Ostrowski,L.E.
  TITLE     Quantitative Proteomic Analysis of Human Airway Cilia Identifies
            Previously Uncharacterized Proteins of High Abundance
  JOURNAL   J Proteome Res 16 (4), 1579-1592 (2017)
   PUBMED   28282151
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Lindskog,C., Fagerberg,L., Hallstrom,B., Edlund,K., Hellwig,B.,
            Rahnenfuhrer,J., Kampf,C., Uhlen,M., Ponten,F. and Micke,P.
  TITLE     The lung-specific proteome defined by integration of
            transcriptomics and antibody-based profiling
  JOURNAL   FASEB J 28 (12), 5184-5196 (2014)
   PUBMED   25169055
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY017665.1, BC118593.1 and AL354735.14.
            
            On Sep 24, 2013 this sequence version replaced XP_005272255.1.
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            5' coding region compared to variant 1. The encoded isoform (2) is
            shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.709894.1,
                                           SRR3476690.558478.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393216.3/ ENSP00000376909.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..284
                     /product="cilia- and flagella-associated protein 77
                     isoform 2"
                     /calculated_mol_wt=32848
     Region          54..204
                     /region_name="CFAP77"
                     /note="Cilia- and flagella-associated protein 77;
                     pfam14825"
                     /db_xref="CDD:464337"
     CDS             1..284
                     /gene="CFAP77"
                     /gene_synonym="C9orf171"
                     /coded_by="NM_001282957.2:62..916"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS65167.1"
                     /db_xref="GeneID:389799"
                     /db_xref="HGNC:HGNC:33776"
                     /db_xref="MIM:621136"
ORIGIN      
        1 mpearssgpd ltrwrkqqqp vrrtvsqvcp pprrpltvad irsgmenerl gvvrdsmfqn
       61 plivkaelgk prersyslpg infnyglyir gldggvpeai grwnvfkqqp tcpheltrny
      121 iamnrgavka glvtarenll yrqlndiris dqddrrmkke ppplppnmtf girarpstpf
      181 fdllqhrylq lwvqeqkatq kaiklekkqk vvlgklyetr ssqlrkykpp vkldtlwhmp
      241 hfqkvgrhld tfpteadrqr alkahreeca vrqgtlrmgn ythp
//
LOCUS       NP_060688               1235 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 40 isoform 2 [Homo sapiens].
ACCESSION   NP_060688 XP_291008
VERSION     NP_060688.2
DBSOURCE    REFSEQ: accession NM_018218.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1235)
  AUTHORS   Mo,H., Li,R., Yang,N., Han,J., Xiao,X., Zhang,Y., Xiao,Z., Jiao,L.,
            Xu,Q. and Tu,K.
  TITLE     USP40 promotes hepatocellular carcinoma progression through a
            YAP/USP40 positive feedback loop
  JOURNAL   Cancer Lett 589, 216832 (2024)
   PUBMED   38537774
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma progression
            through a YAP/USP40 positive feedback loop.
REFERENCE   2  (residues 1 to 1235)
  AUTHORS   Wu,Q., Qiu,Y., Guo,J., Yuan,Z., Yang,Y., Zhu,Q., Zhang,Z., Guo,J.,
            Wu,Y., Zhang,J., Huang,D., Tu,K. and Hu,X.
  TITLE     USP40 promotes hepatocellular carcinoma cell proliferation,
            migration and stemness by deubiquitinating and stabilizing Claudin1
  JOURNAL   Biol Direct 19 (1), 13 (2024)
   PUBMED   38308285
  REMARK    GeneRIF: USP40 promotes hepatocellular carcinoma cell
            proliferation, migration and stemness by deubiquitinating and
            stabilizing Claudin1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1235)
  AUTHORS   Miao,J., Li,L., Shaheen,N., Wei,J., Jacko,A.M., Sundd,P.,
            Taleb,S.J., Mallampalli,R.K., Zhao,Y. and Zhao,J.
  TITLE     The deubiquitinase USP40 preserves endothelial integrity by
            targeting the heat shock protein HSP90beta
  JOURNAL   Exp Mol Med 56 (2), 395-407 (2024)
   PUBMED   38307937
REFERENCE   4  (residues 1 to 1235)
  AUTHORS   Takahashi,S., Fukuhara,D., Kimura,T., Fukutomi,T., Tanaka,E.,
            Mikami,N., Hada,I., Takematsu,H., Nishibori,Y., Akimoto,Y.,
            Kiyonari,H., Abe,T., Huber,O. and Yan,K.
  TITLE     USP40 deubiquitinates HINT1 and stabilizes p53 in podocyte damage
  JOURNAL   Biochem Biophys Res Commun 614, 198-206 (2022)
   PUBMED   35605301
REFERENCE   5  (residues 1 to 1235)
  AUTHORS   An,W., Yao,S., Sun,X., Hou,Z., Lin,Y., Su,L. and Liu,X.
  TITLE     Glucocorticoid modulatory element-binding protein 1 (GMEB1)
            interacts with the de-ubiquitinase USP40 to stabilize CFLARL and
            inhibit apoptosis in human non-small cell lung cancer cells
  JOURNAL   J Exp Clin Cancer Res 38 (1), 181 (2019)
   PUBMED   31046799
  REMARK    GeneRIF: Our findings show the de-ubiquitinase USP40 regulates the
            ubiquitination and degradation of CFLARL; and GMEB1 acts as a
            bridge protein for USP40 and CFLARL. Mechanistically, we found
            GMEB1 inhibits the activation of CASP8 by modulating ubiquitination
            and degradation of CFLARL
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1235)
  AUTHORS   Li,Y., Schrodi,S., Rowland,C., Tacey,K., Catanese,J. and Grupe,A.
  TITLE     Genetic evidence for ubiquitin-specific proteases USP24 and USP40
            as candidate genes for late-onset Parkinson disease
  JOURNAL   Hum Mutat 27 (10), 1017-1023 (2006)
   PUBMED   16917932
  REMARK    GeneRIF: Da suggest that genetic variants in USP40 affect the risk
            for late-onset Parkinson disease (PD), which is consistent with the
            predicted role of the ubiquitination pathway in PD etiology.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1235)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   8  (residues 1 to 1235)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   9  (residues 1 to 1235)
  AUTHORS   Bass,B.L.
  TITLE     RNA editing by adenosine deaminases that act on RNA
  JOURNAL   Annu Rev Biochem 71, 817-846 (2002)
   PUBMED   12045112
  REMARK    Review article
REFERENCE   10 (residues 1 to 1235)
  AUTHORS   Chen,X., Zhang,Y., Douglas,L. and Zhou,P.
  TITLE     UV-damaged DNA-binding proteins are targets of CUL-4A-mediated
            ubiquitination and degradation
  JOURNAL   J Biol Chem 276 (51), 48175-48182 (2001)
   PUBMED   11673459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019072.8 and AC019221.4.
            
            On Aug 29, 2018 this sequence version replaced NP_060688.1.
            
            Summary: Modification of cellular proteins by ubiquitin is an
            essential regulatory mechanism controlled by the coordinated action
            of multiple ubiquitin-conjugating and deubiquitinating enzymes.
            USP40 belongs to a large family of cysteine proteases that function
            as deubiquitinating enzymes (Quesada et al., 2004 [PubMed
            14715245]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1258370.1,
                                           SRR14038191.1271911.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..1235
                     /product="ubiquitin carboxyl-terminal hydrolase 40 isoform
                     2"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 40; ubiquitin
                     carboxyl-terminal hydrolase 40;
                     ubiquitin-specific-processing protease 40;
                     deubiquitinating enzyme 40; ubiquitin thioesterase 40;
                     ubiquitin thiolesterase 40"
                     /calculated_mol_wt=139999
     Region          39..344
                     /region_name="peptidase_C19C"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02659"
                     /db_xref="CDD:239124"
     Site            order(45,50,305,323)
                     /site_type="active"
                     /db_xref="CDD:239124"
     Region          1180..1235
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVE5.3)"
     CDS             1..1235
                     /gene="USP40"
                     /coded_by="NM_018218.4:119..3826"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS46547.2"
                     /db_xref="GeneID:55230"
                     /db_xref="HGNC:HGNC:20069"
                     /db_xref="MIM:610570"
ORIGIN      
        1 mfgdlfeeey stvsnnqygk gkklktkale ppapreftnl sgirnqggtc ylnsllqtlh
       61 ftpefrealf slgpeelglf edkdkpdakv riiplqlqrl faqlllldqe aastadltds
      121 fgwtsneemr qhdvqelnri lfsaletslv gtsghdliyr lyhgtivnqi vckecknvse
      181 rqedfldltv avknvsgled alwnmyveee vfdcdnlyhc gtcdrlvkaa ksaklrklpp
      241 fltvsllrfn fdfvkceryk etscytfplr inlkpfceqs elddleyiyd lfsviihkgg
      301 cygghyhvyi kdvdhlgnwq fqeekskpdv nlkdlqseee idhplmilka illeennlip
      361 vdqlgqkllk kigiswnkky rkqhgplrkf lqlhsqifll ssdestvrll knsslqaesd
      421 fqrndqqifk mlppespgln nsiscphwfd indskvqpir ekdieqqfqg kesaymlfyr
      481 ksqlqrppea ranprygvpc hllnemdaan ielqtkraec dsanntfelh lhlgpqyhff
      541 ngalhpvvsq tesvwdltfd krktlgdlrq sifqllefwe gdmvlsvakl vpaglhiyqs
      601 lggdeltlce teiadgedif vwngvevggv hiqtgidcep lllnvlhldt ssdgekccqv
      661 iesphvfpan aevgtvltal aipagvifin sagcpggegw taipkedmrk tfreqglrng
      721 ssiliqdshd dnslltkeek wvtsmneidw lhvknlcqle seekqvkisa tvntmvfdir
      781 ikaikelklm keladnsclr pidrngkllc pvpdsytlke aelkmgsslg lclgkapsss
      841 qlflffamgs dvqpgtemei vveetisvrd clklmlkksg lqgdawhlrk mdwcyeagep
      901 lceedatlke llicsgdtll liegqlpplg flkvpiwwyq lqgpsghwes hqdqtnctss
      961 wgrvwratss qgasgnepaq vsllylgdie isedatlael ksqamtlppf lefgvpspah
     1021 lrawtverkr pgrllrtdrq plreyklgrr ieicleplqk genlgpqdvl lrtqvripge
     1081 rtyapaldlv wnaaqggtag slrqrvadfy rlpvekieia kyfpekfewl pisswnqqit
     1141 krkkkkkqdy lqgapyylkd gdtigvknll idddddfsti rddtgkekqk qralgrrksq
     1201 ealheqssyi lssaetparp rapetslsih vgsfr
//
LOCUS       NP_001258818             138 aa            linear   PRI 27-NOV-2025
DEFINITION  calcium and integrin-binding family member 2 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001258818
VERSION     NP_001258818.1
DBSOURCE    REFSEQ: accession NM_001271889.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Wang,X., Yi,Z., Shi,M. and Sun,Y.
  TITLE     The Diverse Functions of the Calcium- and Integrin-Binding Protein
            Family
  JOURNAL   Int J Mol Sci 26 (5), 2223 (2025)
   PUBMED   40076845
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Dal Cortivo,G. and Dell'Orco,D.
  TITLE     Calcium- and Integrin-Binding Protein 2 (CIB2) in Physiology and
            Disease: Bright and Dark Sides
  JOURNAL   Int J Mol Sci 23 (7), 3552 (2022)
   PUBMED   35408910
  REMARK    GeneRIF: Calcium- and Integrin-Binding Protein 2 (CIB2) in
            Physiology and Disease: Bright and Dark Sides.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Liang,X., Qiu,X., Dionne,G., Cunningham,C.L., Pucak,M.L., Peng,G.,
            Kim,Y.H., Lauer,A., Shapiro,L. and Muller,U.
  TITLE     CIB2 and CIB3 are auxiliary subunits of the mechanotransduction
            channel of hair cells
  JOURNAL   Neuron 109 (13), 2131-2149 (2021)
   PUBMED   34089643
  REMARK    GeneRIF: CIB2 and CIB3 are auxiliary subunits of the
            mechanotransduction channel of hair cells.
REFERENCE   5  (residues 1 to 138)
  AUTHORS   Huang,H., Bogstie,J.N. and Vogel,H.J.
  TITLE     Biophysical and structural studies of the human calcium- and
            integrin-binding protein family: understanding their functional
            similarities and differences
  JOURNAL   Biochem Cell Biol 90 (5), 646-656 (2012)
   PUBMED   22779914
  REMARK    GeneRIF: CIB2, as binding partners for the integrin alphaIIb
            subunit, which suggests that they are potentially involved in
            regulating integrin alphaIIb subunit activation.
REFERENCE   6  (residues 1 to 138)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   7  (residues 1 to 138)
  AUTHORS   Ahmad,J., Khan,S.N., Khan,S.Y., Ramzan,K., Riazuddin,S.,
            Ahmed,Z.M., Wilcox,E.R., Friedman,T.B. and Riazuddin,S.
  TITLE     DFNB48, a new nonsyndromic recessive deafness locus, maps to
            chromosome 15q23-q25.1
  JOURNAL   Hum Genet 116 (5), 407-412 (2005)
   PUBMED   15711797
REFERENCE   8  (residues 1 to 138)
  AUTHORS   Seki,N., Hattori,A., Hayashi,A., Kozuma,S., Ohira,M., Hori,T. and
            Saito,T.
  TITLE     Structure, expression profile and chromosomal location of an isolog
            of DNA-PKcs interacting protein (KIP) gene
  JOURNAL   Biochim Biophys Acta 1444 (1), 143-147 (1999)
   PUBMED   9931475
REFERENCE   9  (residues 1 to 138)
  AUTHORS   Li,M., Squire,J.A. and Weksberg,R.
  TITLE     Overgrowth syndromes and genomic imprinting: from mouse to man
  JOURNAL   Clin Genet 53 (3), 165-170 (1998)
   PUBMED   9630066
  REMARK    Review article
REFERENCE   10 (residues 1 to 138)
  AUTHORS   Koenekoop,R.K., Arriaga,M.A., Trzupek,K.M. and Lentz,J.J.
  TITLE     Usher Syndrome Type I
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301442
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC090260.13.
            
            Summary: The protein encoded by this gene is similar to that of
            KIP/CIB, calcineurin B, and calmodulin. The encoded protein is a
            calcium-binding regulatory protein that interacts with
            DNA-dependent protein kinase catalytic subunits (DNA-PKcs), and it
            is involved in photoreceptor cell maintenance. Mutations in this
            gene cause deafness, autosomal recessive, 48 (DFNB48), and also
            Usher syndrome 1J (USH1J). Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (3) lacks two alternate exons
            resulting in the loss of an in-frame segment in the 5' coding
            region, compared to variant 1. The encoded isoform (3) is shorter
            than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU556614.1, SRR12921934.894338.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.1"
     Protein         1..138
                     /product="calcium and integrin-binding family member 2
                     isoform 3"
                     /note="DNA-dependent protein kinase catalytic
                     subunit-interacting protein 2"
                     /calculated_mol_wt=15685
     Region          58..124
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     CDS             1..138
                     /gene="CIB2"
                     /gene_synonym="DFNB48; KIP2; USH1J"
                     /coded_by="NM_001271889.2:231..647"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS61723.1"
                     /db_xref="GeneID:10518"
                     /db_xref="HGNC:HGNC:24579"
                     /db_xref="MIM:605564"
ORIGIN      
        1 mgnkqtifte eqldnyqenp fkerivaafs edgegnltfn dfvdmfsvlc esaprelkan
       61 yafkiydfnt dnfickedle ltlarltkse ldeeevvlvc dkvieeadld gdgklgfadf
      121 edmiakapdf lstfhiri
//
LOCUS       NP_001273696             354 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 46 isoform 3 [Homo sapiens].
ACCESSION   NP_001273696 XP_005265821
VERSION     NP_001273696.1
DBSOURCE    REFSEQ: accession NM_001286767.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Yu,K., Wang,G.M., Guo,S.S., Bassermann,F. and Fassler,R.
  TITLE     The USP12/46 deubiquitinases protect integrins from ESCRT-mediated
            lysosomal degradation
  JOURNAL   EMBO Rep 25 (12), 5687-5718 (2024)
   PUBMED   39506038
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Jiang,L., Qi,X., Lai,M., Zhou,J., Yuan,M., You,J., Liu,Q., Pan,J.,
            Zhao,L., Ying,M., Ji,J., Li,K., Zhang,Y., Pan,W., He,Q., Yang,B.
            and Cao,J.
  TITLE     WDR20 prevents hepatocellular carcinoma senescence by orchestrating
            the simultaneous USP12/46-mediated deubiquitination of c-Myc
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2407904121 (2024)
   PUBMED   39432777
  REMARK    GeneRIF: WDR20 prevents hepatocellular carcinoma senescence by
            orchestrating the simultaneous USP12/46-mediated deubiquitination
            of c-Myc.
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Ng,V.H., Spencer,Z., Neitzel,L.R., Nayak,A., Loberg,M.A., Shen,C.,
            Kassel,S.N., Kroh,H.K., An,Z., Anthony,C.C., Bryant,J.M.,
            Lawson,A., Goldsmith,L., Benchabane,H., Hansen,A.G., Li,J.,
            D'Souza,S., Lebensohn,A.M., Rohatgi,R., Weiss,W.A., Weiss,V.L.,
            Williams,C., Hong,C.C., Robbins,D.J., Ahmed,Y. and Lee,E.
  TITLE     The USP46 complex deubiquitylates LRP6 to promote Wnt/beta-catenin
            signaling
  JOURNAL   Nat Commun 14 (1), 6173 (2023)
   PUBMED   37798301
  REMARK    GeneRIF: The USP46 complex deubiquitylates LRP6 to promote
            Wnt/beta-catenin signaling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 354)
  AUTHORS   Ke,L., Jia,Z., Gao,W. and Luo,L.
  TITLE     Ubiquitin specific protease 46 potentiates triple negative breast
            cancer development by stabilizing PGAM1-mediated glycolysis
  JOURNAL   Cell Biol Int 47 (1), 41-51 (2023)
   PUBMED   36335636
  REMARK    GeneRIF: Ubiquitin specific protease 46 potentiates triple negative
            breast cancer development by stabilizing PGAM1-mediated glycolysis.
REFERENCE   6  (residues 1 to 354)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   7  (residues 1 to 354)
  AUTHORS   Cohn,M.A., Kee,Y., Haas,W., Gygi,S.P. and D'Andrea,A.D.
  TITLE     UAF1 is a subunit of multiple deubiquitinating enzyme complexes
  JOURNAL   J Biol Chem 284 (8), 5343-5351 (2009)
   PUBMED   19075014
  REMARK    GeneRIF: two novel multisubunit deubiquitinating enzyme complexes
            containing USP12 and USP46, respectively. Both complexes contain
            the UAF1 protein as a bona fide subunit. Interestingly, UAF1
REFERENCE   8  (residues 1 to 354)
  AUTHORS   Zemunik,T., Boban,M., Lauc,G., Jankovic,S., Rotim,K., Vatavuk,Z.,
            Bencic,G., Dogas,Z., Boraska,V., Torlak,V., Susac,J., Zobic,I.,
            Rudan,D., Pulanic,D., Modun,D., Mudnic,I., Gunjaca,G., Budimir,D.,
            Hayward,C., Vitart,V., Wright,A.F., Campbell,H. and Rudan,I.
  TITLE     Genome-wide association study of biochemical traits in Korcula
            Island, Croatia
  JOURNAL   Croat Med J 50 (1), 23-33 (2009)
   PUBMED   19260141
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   9  (residues 1 to 354)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   10 (residues 1 to 354)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CN483539.1, AK299883.1, BC037574.1 and AC026448.5.
            
            On Nov 15, 2013 this sequence version replaced XP_005265821.1.
            
            Summary: Modification of cellular proteins by ubiquitin is an
            essential regulatory mechanism controlled by the coordinated action
            of multiple ubiquitin-conjugating and deubiquitinating enzymes.
            USP46 belongs to a large family of cysteine proteases that function
            as deubiquitinating enzymes (Quesada et al., 2004 [PubMed
            14715245]).[supplied by OMIM, Jun 2009].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice site in the central coding region, compared to variant 1.
            The encoded isoform (3) is shorter, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.81483.1,
                                           SRR1803615.40649.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..354
                     /product="ubiquitin carboxyl-terminal hydrolase 46 isoform
                     3"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin carboxyl-terminal hydrolase 46; ubiquitin
                     thioesterase 46; deubiquitinating enzyme 46;
                     ubiquitin-specific-processing protease 46; ubiquitin
                     thiolesterase 46"
                     /calculated_mol_wt=40981
     Region          62..351
                     /region_name="Peptidase_C19G"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02663"
                     /db_xref="CDD:239128"
     CDS             1..354
                     /gene="USP46"
                     /coded_by="NM_001286767.2:152..1216"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:64854"
                     /db_xref="HGNC:HGNC:20075"
                     /db_xref="MIM:612849"
ORIGIN      
        1 mtvrniasic nmgtnasale kdigpeqfpi nehyfglvna lyfcrpfren vlaykaqqkk
       61 kenlltclad lfhsiatqkk kvgvippkkf isrlrkendl fdnymqqdah eflnyllnti
      121 adilqeekkq ekqngklkng nmnepaennk peltwvheif qgtltnetrc lncetvsskd
      181 edfldlsvdv eqntsithcl rdfsntetlc seqkyycetc cskqeaqkrm rvkklpmila
      241 lhlkrfkyme qlhrytklsy rvvfplelrl fntssdavnl drmydlvavv vhcgsgpnrg
      301 hyitivkshg fwllfdddiv ekidaqaiee fygltsdisk nsesgyilfy qsre
//
LOCUS       NP_077816               1499 aa            linear   PRI 27-NOV-2025
DEFINITION  phospholipid-transporting ATPase VA [Homo sapiens].
ACCESSION   NP_077816
VERSION     NP_077816.1
DBSOURCE    REFSEQ: accession NM_024490.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1499)
  AUTHORS   Muranaka,Y., Shigetomi,R., Iwasaki,Y., Hamamoto,A., Nakayama,K.,
            Takatsu,H. and Shin,H.W.
  TITLE     Novel phosphatidylinositol flippases contribute to phosphoinositide
            homeostasis in the plasma membrane
  JOURNAL   Biochem J 481 (18), 1187-1202 (2024)
   PUBMED   39258799
REFERENCE   2  (residues 1 to 1499)
  AUTHORS   Tone,T., Nakayama,K., Takatsu,H. and Shin,H.W.
  TITLE     ATPase reaction cycle of P4-ATPases affects their transport from
            the endoplasmic reticulum
  JOURNAL   FEBS Lett 594 (3), 412-423 (2020)
   PUBMED   31571211
REFERENCE   3  (residues 1 to 1499)
  AUTHORS   Roland,B.P., Naito,T., Best,J.T., Arnaiz-Yepez,C., Takatsu,H.,
            Yu,R.J., Shin,H.W. and Graham,T.R.
  TITLE     Yeast and human P4-ATPases transport glycosphingolipids using
            conserved structural motifs
  JOURNAL   J Biol Chem 294 (6), 1794-1806 (2019)
   PUBMED   30530492
REFERENCE   4  (residues 1 to 1499)
  AUTHORS   Takada,N., Naito,T., Inoue,T., Nakayama,K., Takatsu,H. and
            Shin,H.W.
  TITLE     Phospholipid-flipping activity of P4-ATPase drives membrane
            curvature
  JOURNAL   EMBO J 37 (9) (2018)
   PUBMED   29599178
REFERENCE   5  (residues 1 to 1499)
  AUTHORS   Naito,T., Takatsu,H., Miyano,R., Takada,N., Nakayama,K. and
            Shin,H.W.
  TITLE     Phospholipid Flippase ATP10A Translocates Phosphatidylcholine and
            Is Involved in Plasma Membrane Dynamics
  JOURNAL   J Biol Chem 290 (24), 15004-15017 (2015)
   PUBMED   25947375
  REMARK    GeneRIF: results suggest that enhanced PC flipping activity due to
            exogenous ATP10A expression alters the lipid composition at the
            plasma membrane
REFERENCE   6  (residues 1 to 1499)
  AUTHORS   Kuhlbrandt,W.
  TITLE     Biology, structure and mechanism of P-type ATPases
  JOURNAL   Nat Rev Mol Cell Biol 5 (4), 282-295 (2004)
   PUBMED   15071553
  REMARK    Review article
REFERENCE   7  (residues 1 to 1499)
  AUTHORS   Herzing,L.B., Kim,S.J., Cook,E.H. Jr. and Ledbetter,D.H.
  TITLE     The human aminophospholipid-transporting ATPase gene ATP10C maps
            adjacent to UBE3A and exhibits similar imprinted expression
  JOURNAL   Am J Hum Genet 68 (6), 1501-1505 (2001)
   PUBMED   11353404
  REMARK    GeneRIF: ATP10A gene is imprinted, with preferential expression
            from the maternal allele in human brain.
REFERENCE   8  (residues 1 to 1499)
  AUTHORS   Meguro,M., Kashiwagi,A., Mitsuya,K., Nakao,M., Kondo,I., Saitoh,S.
            and Oshimura,M.
  TITLE     A novel maternally expressed gene, ATP10C, encodes a putative
            aminophospholipid translocase associated with Angelman syndrome
  JOURNAL   Nat Genet 28 (1), 19-20 (2001)
   PUBMED   11326269
REFERENCE   9  (residues 1 to 1499)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1499)
  AUTHORS   Gillessen-Kaesbach,G., Demuth,S., Thiele,H., Theile,U., Lich,C. and
            Horsthemke,B.
  TITLE     A previously unrecognised phenotype characterised by obesity,
            muscular hypotonia, and ability to speak in patients with Angelman
            syndrome caused by an imprinting defect
  JOURNAL   Eur J Hum Genet 7 (6), 638-644 (1999)
   PUBMED   10482951
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016266.14, AC109512.12 and
            AC023449.11.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type cation transport ATPases, and to the subfamily of
            aminophospholipid-transporting ATPases. The aminophospholipid
            translocases transport phosphatidylserine and
            phosphatidylethanolamine from one side of a bilayer to another.
            This gene is maternally expressed. It maps within the most common
            interval of deletion responsible for Angelman syndrome, also known
            as 'happy puppet syndrome'. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC052251.1, SRR14038193.3229077.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene         :: PMID: 10482951, 11353404, 11326269
            MANE Ensembl match     :: ENST00000555815.7/ ENSP00000450480.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q12"
     Protein         1..1499
                     /product="phospholipid-transporting ATPase VA"
                     /EC_number="7.6.2.1"
                     /note="ATPase, Class V, type 10C; aminophospholipid
                     translocase VA; ATPase, class V, type 10A; ATPase type IV,
                     phospholipid transporting (P-type); P4-ATPase flippase
                     complex alpha subunit ATP10A; probable
                     phospholipid-transporting ATPase VA"
                     /calculated_mol_wt=167558
     Region          1..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60312.2)"
     Region          61..1189
                     /region_name="P-type_ATPase_APLT_Dnf-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2,
                     -10D, -11B, -11C; cd02073"
                     /db_xref="CDD:319770"
     Site            87..106
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60312.2)"
     Site            111..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60312.2)"
     Site            310..332
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60312.2)"
     Site            363..384
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60312.2)"
     Site            order(427..429,742,766..768,842,889..891,1005,1008,1011,
                     1031,1034)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     Region          464..531
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60312.2)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O54827; propagated from
                     UniProtKB/Swiss-Prot (O60312.2)"
     Site            1088..1108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60312.2)"
     Site            1120..1140
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60312.2)"
     Site            1171..1192
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60312.2)"
     Site            1200..1222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60312.2)"
     Site            1229..1249
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60312.2)"
     Site            1268..1292
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60312.2)"
     Region          1311..1356
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60312.2)"
     Region          1464..1499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60312.2)"
     CDS             1..1499
                     /gene="ATP10A"
                     /gene_synonym="ATP10C; ATPVA; ATPVC"
                     /coded_by="NM_024490.4:232..4731"
                     /db_xref="CCDS:CCDS32178.1"
                     /db_xref="GeneID:57194"
                     /db_xref="HGNC:HGNC:13542"
                     /db_xref="MIM:605855"
ORIGIN      
        1 merepagtee pgppgrrrrr egrtrtvrsn llpppgaedp aagaakgerr rrrgcaqhla
       61 dnrlkttkyt llsflpknlf eqfhrpanvy fvfiallnfv pavnafqpgl alapvlfila
      121 itafrdlwed ysrhrsdhki nhlgclvfsr eekkyvnrfw keihvgdfvr lrcneifpad
      181 illlsssdpd glchietanl dgetnlkrrq vvrgfselvs efnpltftsv iecekpnndl
      241 srfrgciihd ngkkaglyke nlllrgctlr ntdavvgivi yaghetkall nnsgprykrs
      301 klerqmncdv lwcvlllvcm slfsavghgl wiwryqekks lfyvpksdgs slspvtaavy
      361 sfltmiivlq vlipislyvs ieivkacqvy finqdmqlyd eetdsqlqcr alnitedlgq
      421 iqyifsdktg tltenkmvfr rctvsgveys hdanaqrlar yqeadseeee vvprggsvsq
      481 rgsigshqsv rvvhrtqstk shrrtgsrae akrasmlskh tafsspmekd itpdpkllek
      541 vsecdkslav arhqehllah lspelsdvfd ffialticnt vvvtspdqpr tkvrvrfelk
      601 spvktiedfl rrftpsclts gcssigslaa nksshklgss fpstpssdgm llrleerlgq
      661 ptsaiasngy ssqadnwase laqeqesere lryeaespde aalvyaaray ncvlverlhd
      721 qvsvelphlg rltfellhtl gfdsvrkrms vvirhpltde invytkgads vvmdllqpcs
      781 svdargrhqk kirsktqnyl nvyaaeglrt lciakrvlsk eeyacwlqsh leaesslens
      841 eellfqsair letnlhllga tgiedrlqdg vpetisklrq aglqiwvltg dkqetavnia
      901 yacklldhde evitlnatsq eacaalldqc lcyvqsrglq rapektkgkv smrfsslcpp
      961 ststasgrrp slvidgrsla yaleknledk flflakqcrs vlccrstplq ksmvvklvrs
     1021 klkamtlaig dgandvsmiq vadvgvgisg qegmqavmas dfavpkfryl erllilhghw
     1081 cysrlanmvl yffykntmfv gllfwfqffc gfsastmidq wyliffnllf sslpplvtgv
     1141 ldrdvpanvl ltnpqlyksg qnmeeyrprt fwfnmadaaf qslvcfsipy layydsnvdl
     1201 ftwgtpivti alltfllhlg ietktwtwln witcgfsvll fftvaliyna scatcyppsn
     1261 pywtmqallg dpvfyltclm tpvaallprl ffrslqgrvf ptqlqlarql trksprrcsa
     1321 pketfaqgrl pkdsgtehss grtvktsvpl sqpswhtqqp vcsleasgep stvdmsmpvr
     1381 ehtlleglsa papmssapge avlrspggcp eeskvraast grvtplsslf slptfsllnw
     1441 isswslvsrl gsvlqfsrte qladgqagrg lpvqphsgrs glqgpdhrll igassrrsq
//
LOCUS       NP_006581                565 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 39 isoform 1 [Homo sapiens].
ACCESSION   NP_006581
VERSION     NP_006581.2
DBSOURCE    REFSEQ: accession NM_006590.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Zhou,F., Li,X., Sun,Y., Wang,Y., Niu,K., Gao,X., Zhang,J., Chen,T.,
            Li,Y., Zhao,W., Mao,B., Xu,Q., Shi,Y. and He,Z.
  TITLE     USP39 at the crossroads of cancer immunity: regulating immune
            evasion and immunotherapy response through RNA splicing and
            ubiquitin signaling
  JOURNAL   Front Immunol 16, 1665775 (2025)
   PUBMED   40990019
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Lu,C., Cai,Y., Wu,S., Wang,Y., Li,J.B., Xu,G. and Ma,J.
  TITLE     Deubiquitinating enzyme USP39 promotes the growth and metastasis of
            gastric cancer cells by modulating the degradation of RNA-binding
            protein RBM39
  JOURNAL   J Biol Chem 300 (10), 107751 (2024)
   PUBMED   39260689
  REMARK    GeneRIF: Deubiquitinating enzyme USP39 promotes the growth and
            metastasis of gastric cancer cells by modulating the degradation of
            RNA-binding protein RBM39.
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   4  (residues 1 to 565)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   5  (residues 1 to 565)
  AUTHORS   Hu,Y., Wang,Y., Hu,W., Hu,C., Wang,B., Liu,C., Deng,A., Shen,B.,
            Wu,K. and Liu,Y.
  TITLE     USP39 Promotes the Viability and Migration of Head and Neck
            Squamous Cell Carcinoma Cell by Regulating STAT1
  JOURNAL   Technol Cancer Res Treat 23, 15330338241250298 (2024)
   PUBMED   38706215
  REMARK    GeneRIF: USP39 Promotes the Viability and Migration of Head and
            Neck Squamous Cell Carcinoma Cell by Regulating STAT1.
REFERENCE   6  (residues 1 to 565)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   7  (residues 1 to 565)
  AUTHORS   van Leuken,R.J., Luna-Vargas,M.P., Sixma,T.K., Wolthuis,R.M. and
            Medema,R.H.
  TITLE     Usp39 is essential for mitotic spindle checkpoint integrity and
            controls mRNA-levels of aurora B
  JOURNAL   Cell Cycle 7 (17), 2710-2719 (2008)
   PUBMED   18728397
  REMARK    GeneRIF: These observations suggest Usp39 to be involved in
            splicing of Aurora B and other mRNAs that are essential for proper
            spindle checkpoint function.
REFERENCE   8  (residues 1 to 565)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   9  (residues 1 to 565)
  AUTHORS   Makarova,O.V., Makarov,E.M. and Luhrmann,R.
  TITLE     The 65 and 110 kDa SR-related proteins of the U4/U6.U5 tri-snRNP
            are essential for the assembly of mature spliceosomes
  JOURNAL   EMBO J 20 (10), 2553-2563 (2001)
   PUBMED   11350945
REFERENCE   10 (residues 1 to 565)
  AUTHORS   Lygerou,Z., Christophides,G. and Seraphin,B.
  TITLE     A novel genetic screen for snRNP assembly factors in yeast
            identifies a conserved protein, Sad1p, also required for pre-mRNA
            splicing
  JOURNAL   Mol Cell Biol 19 (3), 2008-2020 (1999)
   PUBMED   10022888
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK289451.1 and BC001384.2.
            
            On Dec 10, 2004 this sequence version replaced NP_006581.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1 and 2 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.260935.1,
                                           SRR1803616.57915.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323701.11/ ENSP00000312981.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p11.2"
     Protein         1..565
                     /product="ubiquitin carboxyl-terminal hydrolase 39 isoform
                     1"
                     /EC_number="3.4.19.12"
                     /note="SnRNP assembly defective 1 homolog; small nuclear
                     ribonucleoprotein 65kDa (U4/U6.U5); ubiquitin specific
                     protease 39; U4/U6.U5 tri-snRNP-associated protein 2;
                     U4/U6.U5 tri-snRNP-associated 65 kDa protein; SAD1
                     homolog; inactive ubiquitin-specific peptidase 39;
                     ubiquitin carboxyl-terminal hydrolase 39"
                     /calculated_mol_wt=65250
     Region          1..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GS9.2)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53GS9.2)"
     Region          75..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GS9.2)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q53GS9.2)"
     Region          106..553
                     /region_name="Peptidase_C19M"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02669"
                     /db_xref="CDD:239134"
     Site            order(229,234,513,531)
                     /site_type="active"
                     /db_xref="CDD:239134"
     CDS             1..565
                     /gene="USP39"
                     /gene_synonym="65K; CGI-21; HSPC332; SAD1; SNRNP65"
                     /coded_by="NM_006590.4:11..1708"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33234.1"
                     /db_xref="GeneID:10713"
                     /db_xref="HGNC:HGNC:20071"
                     /db_xref="MIM:611594"
ORIGIN      
        1 msgrskresr gstrgkrese srgssgrvkr erdrerepea assrgspvrv krefepasar
       61 eapasvvpfv rvkrerevde dseperevra kngrvdsedr rsrhcpyldt inrsvldfdf
      121 eklcsislsh inayaclvcg kyfqgrglks hayihsvqfs hhvflnlhtl kfyclpdnye
      181 iidssledit yvlkptftkq qianldkqak lsraydgtty lpgivglnni kandyanavl
      241 qalsnvpplr nyfleednyk nikrppgdim fllvqrfgel mrklwnprnf kahvspheml
      301 qavvlcskkt fqitkqgdgv dflswflnal hsalggtkkk kktivtdvfq gsmriftkkl
      361 phpdlpaeek eqllhndeyq etmvestfmy ltldlptapl ykdekeqlii pqvplfnila
      421 kfngitekey ktykenflkr fqltklppyl ifcikrftkn nffveknpti vnfpitnvdl
      481 reylseevqa vhknttydli anivhdgkps egsyrihvlh hgtgkwyelq dlqvtdilpq
      541 mitlseayiq iwkrrdndet nqqga
//
LOCUS       NP_001243654             565 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 39 isoform 1 [Homo sapiens].
ACCESSION   NP_001243654
VERSION     NP_001243654.1
DBSOURCE    REFSEQ: accession NM_001256725.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Zhou,F., Li,X., Sun,Y., Wang,Y., Niu,K., Gao,X., Zhang,J., Chen,T.,
            Li,Y., Zhao,W., Mao,B., Xu,Q., Shi,Y. and He,Z.
  TITLE     USP39 at the crossroads of cancer immunity: regulating immune
            evasion and immunotherapy response through RNA splicing and
            ubiquitin signaling
  JOURNAL   Front Immunol 16, 1665775 (2025)
   PUBMED   40990019
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Lu,C., Cai,Y., Wu,S., Wang,Y., Li,J.B., Xu,G. and Ma,J.
  TITLE     Deubiquitinating enzyme USP39 promotes the growth and metastasis of
            gastric cancer cells by modulating the degradation of RNA-binding
            protein RBM39
  JOURNAL   J Biol Chem 300 (10), 107751 (2024)
   PUBMED   39260689
  REMARK    GeneRIF: Deubiquitinating enzyme USP39 promotes the growth and
            metastasis of gastric cancer cells by modulating the degradation of
            RNA-binding protein RBM39.
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   4  (residues 1 to 565)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   5  (residues 1 to 565)
  AUTHORS   Hu,Y., Wang,Y., Hu,W., Hu,C., Wang,B., Liu,C., Deng,A., Shen,B.,
            Wu,K. and Liu,Y.
  TITLE     USP39 Promotes the Viability and Migration of Head and Neck
            Squamous Cell Carcinoma Cell by Regulating STAT1
  JOURNAL   Technol Cancer Res Treat 23, 15330338241250298 (2024)
   PUBMED   38706215
  REMARK    GeneRIF: USP39 Promotes the Viability and Migration of Head and
            Neck Squamous Cell Carcinoma Cell by Regulating STAT1.
REFERENCE   6  (residues 1 to 565)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   7  (residues 1 to 565)
  AUTHORS   van Leuken,R.J., Luna-Vargas,M.P., Sixma,T.K., Wolthuis,R.M. and
            Medema,R.H.
  TITLE     Usp39 is essential for mitotic spindle checkpoint integrity and
            controls mRNA-levels of aurora B
  JOURNAL   Cell Cycle 7 (17), 2710-2719 (2008)
   PUBMED   18728397
  REMARK    GeneRIF: These observations suggest Usp39 to be involved in
            splicing of Aurora B and other mRNAs that are essential for proper
            spindle checkpoint function.
REFERENCE   8  (residues 1 to 565)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   9  (residues 1 to 565)
  AUTHORS   Makarova,O.V., Makarov,E.M. and Luhrmann,R.
  TITLE     The 65 and 110 kDa SR-related proteins of the U4/U6.U5 tri-snRNP
            are essential for the assembly of mature spliceosomes
  JOURNAL   EMBO J 20 (10), 2553-2563 (2001)
   PUBMED   11350945
REFERENCE   10 (residues 1 to 565)
  AUTHORS   Lygerou,Z., Christophides,G. and Seraphin,B.
  TITLE     A novel genetic screen for snRNP assembly factors in yeast
            identifies a conserved protein, Sad1p, also required for pre-mRNA
            splicing
  JOURNAL   Mol Cell Biol 19 (3), 2008-2020 (1999)
   PUBMED   10022888
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC067273.1 and AI201523.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 3' UTR, compared to variant 1. Variants 1 and 2 encode the
            same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF353989.1, BC067273.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p11.2"
     Protein         1..565
                     /product="ubiquitin carboxyl-terminal hydrolase 39 isoform
                     1"
                     /EC_number="3.4.19.12"
                     /note="SnRNP assembly defective 1 homolog; small nuclear
                     ribonucleoprotein 65kDa (U4/U6.U5); ubiquitin specific
                     protease 39; U4/U6.U5 tri-snRNP-associated protein 2;
                     U4/U6.U5 tri-snRNP-associated 65 kDa protein; SAD1
                     homolog; inactive ubiquitin-specific peptidase 39;
                     ubiquitin carboxyl-terminal hydrolase 39"
                     /calculated_mol_wt=65250
     Region          1..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GS9.2)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53GS9.2)"
     Region          75..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53GS9.2)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q53GS9.2)"
     Region          106..553
                     /region_name="Peptidase_C19M"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02669"
                     /db_xref="CDD:239134"
     Site            order(229,234,513,531)
                     /site_type="active"
                     /db_xref="CDD:239134"
     CDS             1..565
                     /gene="USP39"
                     /gene_synonym="65K; CGI-21; HSPC332; SAD1; SNRNP65"
                     /coded_by="NM_001256725.2:11..1708"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS33234.1"
                     /db_xref="GeneID:10713"
                     /db_xref="HGNC:HGNC:20071"
                     /db_xref="MIM:611594"
ORIGIN      
        1 msgrskresr gstrgkrese srgssgrvkr erdrerepea assrgspvrv krefepasar
       61 eapasvvpfv rvkrerevde dseperevra kngrvdsedr rsrhcpyldt inrsvldfdf
      121 eklcsislsh inayaclvcg kyfqgrglks hayihsvqfs hhvflnlhtl kfyclpdnye
      181 iidssledit yvlkptftkq qianldkqak lsraydgtty lpgivglnni kandyanavl
      241 qalsnvpplr nyfleednyk nikrppgdim fllvqrfgel mrklwnprnf kahvspheml
      301 qavvlcskkt fqitkqgdgv dflswflnal hsalggtkkk kktivtdvfq gsmriftkkl
      361 phpdlpaeek eqllhndeyq etmvestfmy ltldlptapl ykdekeqlii pqvplfnila
      421 kfngitekey ktykenflkr fqltklppyl ifcikrftkn nffveknpti vnfpitnvdl
      481 reylseevqa vhknttydli anivhdgkps egsyrihvlh hgtgkwyelq dlqvtdilpq
      541 mitlseayiq iwkrrdndet nqqga
//
LOCUS       NP_001287851             138 aa            linear   PRI 27-NOV-2025
DEFINITION  calcium and integrin-binding family member 3 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001287851 XP_005259785
VERSION     NP_001287851.1
DBSOURCE    REFSEQ: accession NM_001300922.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Wang,X., Yi,Z., Shi,M. and Sun,Y.
  TITLE     The Diverse Functions of the Calcium- and Integrin-Binding Protein
            Family
  JOURNAL   Int J Mol Sci 26 (5), 2223 (2025)
   PUBMED   40076845
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Wijeratne,S.S., Marchan,M.F., Tresback,J.S. and Subramanian,R.
  TITLE     Atomic force microscopy reveals distinct protofilament-scale
            structural dynamics in depolymerizing microtubule arrays
  JOURNAL   Proc Natl Acad Sci U S A 119 (5) (2022)
   PUBMED   35101922
  REMARK    GeneRIF: Atomic force microscopy reveals distinct
            protofilament-scale structural dynamics in depolymerizing
            microtubule arrays.
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Liang,X., Qiu,X., Dionne,G., Cunningham,C.L., Pucak,M.L., Peng,G.,
            Kim,Y.H., Lauer,A., Shapiro,L. and Muller,U.
  TITLE     CIB2 and CIB3 are auxiliary subunits of the mechanotransduction
            channel of hair cells
  JOURNAL   Neuron 109 (13), 2131-2149 (2021)
   PUBMED   34089643
  REMARK    GeneRIF: CIB2 and CIB3 are auxiliary subunits of the
            mechanotransduction channel of hair cells.
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 138)
  AUTHORS   Huang,H., Bogstie,J.N. and Vogel,H.J.
  TITLE     Biophysical and structural studies of the human calcium- and
            integrin-binding protein family: understanding their functional
            similarities and differences
  JOURNAL   Biochem Cell Biol 90 (5), 646-656 (2012)
   PUBMED   22779914
  REMARK    GeneRIF: CIB3, as binding partners for the integrin alphaIIb
            subunit, which suggests that they are potentially involved in
            regulating integrin alphaIIb subunit activation.
REFERENCE   6  (residues 1 to 138)
  AUTHORS   Gentry,H.R., Singer,A.U., Betts,L., Yang,C., Ferrara,J.D.,
            Sondek,J. and Parise,L.V.
  TITLE     Structural and biochemical characterization of CIB1 delineates a
            new family of EF-hand-containing proteins
  JOURNAL   J Biol Chem 280 (9), 8407-8415 (2005)
   PUBMED   15574431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC112200.1, BC069428.1,
            AB050868.1 and AW295492.1.
            
            On Jul 16, 2014 this sequence version replaced XP_005259785.1.
            
            Summary: This gene product shares a high degree of sequence
            similarity with DNA-dependent protein kinase catalytic
            subunit-interacting protein 2 in human and mouse, and like them may
            bind the catalytic subunit of DNA-dependent protein kinases. The
            exact function of this gene is not known. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jul
            2014].
            
            Transcript Variant: This variant (2) lacks two consecutive
            alternate exons in the 5' coding region, compared to variant 1. It
            encodes isoform 2, which lacks an internal in-frame segment and is
            shorter, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC069428.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968968,
                                           SAMEA2146236 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..138
                     /product="calcium and integrin-binding family member 3
                     isoform 2"
                     /note="DNA-dependent protein kinase catalytic
                     subunit-interacting protein 3"
                     /calculated_mol_wt=15843
     Region          58..125
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     CDS             1..138
                     /gene="CIB3"
                     /gene_synonym="KIP3"
                     /coded_by="NM_001300922.2:51..467"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS74305.1"
                     /db_xref="GeneID:117286"
                     /db_xref="HGNC:HGNC:24580"
                     /db_xref="MIM:610645"
ORIGIN      
        1 mgnkqtvfth eqleayqdnp frqriaqvfs edgdghmtld nfldmfsvms emaprdlkay
       61 yafkiydfnn ddyicawdle qtvtkltrgg lsaeevslvc ekvldeadgd hdgrlsledf
      121 qnmilrapdf lstfhiri
//
LOCUS       NP_061031                640 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 49 isoform b [Homo sapiens].
ACCESSION   NP_061031
VERSION     NP_061031.2
DBSOURCE    REFSEQ: accession NM_018561.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Campos-Iglesias,D., Fraile,J.M., Bretones,G., Montero,A.A.,
            Bonzon-Kulichenko,E., Vazquez,J., Lopez-Otin,C. and Freije,J.M.P.
  TITLE     USP49 deubiquitinase regulates the mitotic spindle checkpoint and
            prevents aneuploidy
  JOURNAL   Cell Death Dis 14 (1), 60 (2023)
   PUBMED   36702832
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Kaushal,K., Kim,E.J., Tyagi,A., Karapurkar,J.K., Haq,S., Jung,H.S.,
            Kim,K.S. and Ramakrishna,S.
  TITLE     Genome-wide screening for deubiquitinase subfamily identifies
            ubiquitin-specific protease 49 as a novel regulator of
            odontogenesis
  JOURNAL   Cell Death Differ 29 (9), 1689-1704 (2022)
   PUBMED   35273362
  REMARK    GeneRIF: Genome-wide screening for deubiquitinase subfamily
            identifies ubiquitin-specific protease 49 as a novel regulator of
            odontogenesis.
REFERENCE   3  (residues 1 to 640)
  AUTHORS   Matsui,M., Kajita,S., Tsuchiya,Y., Torii,W., Tamekuni,S. and
            Nishi,R.
  TITLE     USP49 is a novel deubiquitylating enzyme for gamma H2AX in DNA
            double-strand break repair
  JOURNAL   Gene 833, 146599 (2022)
   PUBMED   35598681
  REMARK    GeneRIF: USP49 is a novel deubiquitylating enzyme for gamma H2AX in
            DNA double-strand break repair.
REFERENCE   4  (residues 1 to 640)
  AUTHORS   Tu,R., Kang,W., Kang,Y., Chen,Z., Zhang,P., Xiong,X., Ma,J.,
            Du,R.L. and Zhang,C.
  TITLE     c-MYC-USP49-BAG2 axis promotes proliferation and chemoresistance of
            colorectal cancer cells in vitro
  JOURNAL   Biochem Biophys Res Commun 607, 117-123 (2022)
   PUBMED   35367823
  REMARK    GeneRIF: c-MYC-USP49-BAG2 axis promotes proliferation and
            chemoresistance of colorectal cancer cells in vitro.
REFERENCE   5  (residues 1 to 640)
  AUTHORS   Liu,Z., Li,J., Ding,Y., Ma,M., Chen,J., Lei,W., Li,L., Yao,Y.,
            Yu,X., Zhong,M., Liao,Q., Fang,W., Fan,L., Huang,C., Zhong,H.,
            Wen,Q., Fang,Z., Chen,J., Huang,S., Xiong,J., Xiang,X. and Deng,J.
  TITLE     USP49 mediates tumor progression and poor prognosis through a
            YAP1-dependent feedback loop in gastric cancer
  JOURNAL   Oncogene 41 (18), 2555-2570 (2022)
   PUBMED   35318441
  REMARK    GeneRIF: USP49 mediates tumor progression and poor prognosis
            through a YAP1-dependent feedback loop in gastric cancer.
REFERENCE   6  (residues 1 to 640)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   7  (residues 1 to 640)
  AUTHORS   Brognard,J., Sierecki,E., Gao,T. and Newton,A.C.
  TITLE     PHLPP and a second isoform, PHLPP2, differentially attenuate the
            amplitude of Akt signaling by regulating distinct Akt isoforms
  JOURNAL   Mol Cell 25 (6), 917-931 (2007)
   PUBMED   17386267
REFERENCE   8  (residues 1 to 640)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   9  (residues 1 to 640)
  AUTHORS   Sato,S., Tomomori-Sato,C., Banks,C.A., Parmely,T.J., Sorokina,I.,
            Brower,C.S., Conaway,R.C. and Conaway,J.W.
  TITLE     A mammalian homolog of Drosophila melanogaster transcriptional
            coactivator intersex is a subunit of the mammalian Mediator complex
  JOURNAL   J Biol Chem 278 (50), 49671-49674 (2003)
   PUBMED   14576168
REFERENCE   10 (residues 1 to 640)
  AUTHORS   Sato,S., Tomomori-Sato,C., Banks,C.A., Sorokina,I., Parmely,T.J.,
            Kong,S.E., Jin,J., Cai,Y., Lane,W.S., Brower,C.S., Conaway,R.C. and
            Conaway,J.W.
  TITLE     Identification of mammalian Mediator subunits with similarities to
            yeast Mediator subunits Srb5, Srb6, Med11, and Rox3
  JOURNAL   J Biol Chem 278 (17), 15123-15127 (2003)
   PUBMED   12584197
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL160163.24, BC014176.2 and AJ586139.1.
            
            On Jun 10, 2002 this sequence version replaced NP_061031.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR, and it
            includes alternate 3' exon structure and thus differs in the 3'
            coding region and 3' UTR, compared to variant 1. The encoded
            isoform (b) has a distinct C-terminus and is shorter than isoform
            a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014176.2, SRR14038193.2348535.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..640
                     /product="ubiquitin carboxyl-terminal hydrolase 49 isoform
                     b"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 49; deubiquitinating
                     enzyme 49; ubiquitin-specific-processing protease 49;
                     ubiquitin carboxyl-terminal hydrolase 49; ubiquitin
                     thioesterase 49; ubiquitin thiolesterase 49"
                     /calculated_mol_wt=73324
     Region          26..87
                     /region_name="zf-UBP"
                     /note="Zn-finger in ubiquitin-hydrolases and other
                     protein; pfam02148"
                     /db_xref="CDD:460464"
     Region          169..230
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70CQ1.1)"
     Region          253..626
                     /region_name="UCH"
                     /note="Ubiquitin carboxyl-terminal hydrolase; pfam00443"
                     /db_xref="CDD:425685"
     Region          293..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70CQ1.1)"
     CDS             1..640
                     /gene="USP49"
                     /coded_by="NM_018561.5:237..2159"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4861.1"
                     /db_xref="GeneID:25862"
                     /db_xref="HGNC:HGNC:20078"
ORIGIN      
        1 mdrckhvgrl rlaqdhsiln pqkwccleca ttesvwaclk cshvacgryi edhalkhfee
       61 tghplamevr dlyvfcylck dyvlndnpeg dlkllrssll avrgqkqdtp vrrgrtlrsm
      121 asgedvvlpq rapqgqpqml talwyrrqrl lartlrlwfe kssrgqakle qrrqeealer
      181 kkeearrrrr evkrrlleel astpprksar lllhtprdag paasrpaalp tsrrvpaatl
      241 klrrqpamap gvtglrnlgn tcymnsilqv lshlqkfrec flnldpskte hlfpkatngk
      301 tqlsgkptns satelslrnd raeaceregf cwngrasisr sleliqnkep sskhislcre
      361 lhtlfrvmws gkwalvspfa mlhsvwslip afrgydqqda qeflcellhk vqqelesegt
      421 trrilipfsq rkltkqvlkv vntifhgqll sqvtciscny ksntiepfwd lslefperyh
      481 ciekgfvpln qtecllteml akfteteale griyacdqcn skrrksnpkp lvlsearkql
      541 miyrlpqvlr lhlkrfrwsg rnhrekigvh vvfdqvltme pyccrdmlss ldketfaydl
      601 savvmhhgkg fgsghytayc ynteggacal lcgvgdterg
//
LOCUS       NP_006374                187 aa            linear   PRI 27-NOV-2025
DEFINITION  calcium and integrin-binding family member 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_006374
VERSION     NP_006374.1
DBSOURCE    REFSEQ: accession NM_006383.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Wang,X., Yi,Z., Shi,M. and Sun,Y.
  TITLE     The Diverse Functions of the Calcium- and Integrin-Binding Protein
            Family
  JOURNAL   Int J Mol Sci 26 (5), 2223 (2025)
   PUBMED   40076845
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Dal Cortivo,G. and Dell'Orco,D.
  TITLE     Calcium- and Integrin-Binding Protein 2 (CIB2) in Physiology and
            Disease: Bright and Dark Sides
  JOURNAL   Int J Mol Sci 23 (7), 3552 (2022)
   PUBMED   35408910
  REMARK    GeneRIF: Calcium- and Integrin-Binding Protein 2 (CIB2) in
            Physiology and Disease: Bright and Dark Sides.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Liang,X., Qiu,X., Dionne,G., Cunningham,C.L., Pucak,M.L., Peng,G.,
            Kim,Y.H., Lauer,A., Shapiro,L. and Muller,U.
  TITLE     CIB2 and CIB3 are auxiliary subunits of the mechanotransduction
            channel of hair cells
  JOURNAL   Neuron 109 (13), 2131-2149 (2021)
   PUBMED   34089643
  REMARK    GeneRIF: CIB2 and CIB3 are auxiliary subunits of the
            mechanotransduction channel of hair cells.
REFERENCE   5  (residues 1 to 187)
  AUTHORS   Huang,H., Bogstie,J.N. and Vogel,H.J.
  TITLE     Biophysical and structural studies of the human calcium- and
            integrin-binding protein family: understanding their functional
            similarities and differences
  JOURNAL   Biochem Cell Biol 90 (5), 646-656 (2012)
   PUBMED   22779914
  REMARK    GeneRIF: CIB2, as binding partners for the integrin alphaIIb
            subunit, which suggests that they are potentially involved in
            regulating integrin alphaIIb subunit activation.
REFERENCE   6  (residues 1 to 187)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   7  (residues 1 to 187)
  AUTHORS   Ahmad,J., Khan,S.N., Khan,S.Y., Ramzan,K., Riazuddin,S.,
            Ahmed,Z.M., Wilcox,E.R., Friedman,T.B. and Riazuddin,S.
  TITLE     DFNB48, a new nonsyndromic recessive deafness locus, maps to
            chromosome 15q23-q25.1
  JOURNAL   Hum Genet 116 (5), 407-412 (2005)
   PUBMED   15711797
REFERENCE   8  (residues 1 to 187)
  AUTHORS   Seki,N., Hattori,A., Hayashi,A., Kozuma,S., Ohira,M., Hori,T. and
            Saito,T.
  TITLE     Structure, expression profile and chromosomal location of an isolog
            of DNA-PKcs interacting protein (KIP) gene
  JOURNAL   Biochim Biophys Acta 1444 (1), 143-147 (1999)
   PUBMED   9931475
REFERENCE   9  (residues 1 to 187)
  AUTHORS   Li,M., Squire,J.A. and Weksberg,R.
  TITLE     Overgrowth syndromes and genomic imprinting: from mouse to man
  JOURNAL   Clin Genet 53 (3), 165-170 (1998)
   PUBMED   9630066
  REMARK    Review article
REFERENCE   10 (residues 1 to 187)
  AUTHORS   Koenekoop,R.K., Arriaga,M.A., Trzupek,K.M. and Lentz,J.J.
  TITLE     Usher Syndrome Type I
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301442
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC090260.13.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is similar to that of
            KIP/CIB, calcineurin B, and calmodulin. The encoded protein is a
            calcium-binding regulatory protein that interacts with
            DNA-dependent protein kinase catalytic subunits (DNA-PKcs), and it
            is involved in photoreceptor cell maintenance. Mutations in this
            gene cause deafness, autosomal recessive, 48 (DFNB48), and also
            Usher syndrome 1J (USH1J). Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC057292.1, SRR1163655.478959.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000258930.8/ ENSP00000258930.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.1"
     Protein         1..187
                     /product="calcium and integrin-binding family member 2
                     isoform 1"
                     /note="DNA-dependent protein kinase catalytic
                     subunit-interacting protein 2"
                     /calculated_mol_wt=21513
     Region          107..173
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     CDS             1..187
                     /gene="CIB2"
                     /gene_synonym="DFNB48; KIP2; USH1J"
                     /coded_by="NM_006383.4:231..794"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10296.1"
                     /db_xref="GeneID:10518"
                     /db_xref="HGNC:HGNC:24579"
                     /db_xref="MIM:605564"
ORIGIN      
        1 mgnkqtifte eqldnyqdct ffnkkdilkl hsrfyelapn lvpmdyrksp ivhvpmslii
       61 qmpelrenpf kerivaafse dgegnltfnd fvdmfsvlce saprelkany afkiydfntd
      121 nfickedlel tlarltksel deeevvlvcd kvieeadldg dgklgfadfe dmiakapdfl
      181 stfhiri
//
LOCUS       NP_001127695             359 aa            linear   PRI 27-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 46 isoform 2 [Homo sapiens].
ACCESSION   NP_001127695
VERSION     NP_001127695.1
DBSOURCE    REFSEQ: accession NM_001134223.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Yu,K., Wang,G.M., Guo,S.S., Bassermann,F. and Fassler,R.
  TITLE     The USP12/46 deubiquitinases protect integrins from ESCRT-mediated
            lysosomal degradation
  JOURNAL   EMBO Rep 25 (12), 5687-5718 (2024)
   PUBMED   39506038
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Jiang,L., Qi,X., Lai,M., Zhou,J., Yuan,M., You,J., Liu,Q., Pan,J.,
            Zhao,L., Ying,M., Ji,J., Li,K., Zhang,Y., Pan,W., He,Q., Yang,B.
            and Cao,J.
  TITLE     WDR20 prevents hepatocellular carcinoma senescence by orchestrating
            the simultaneous USP12/46-mediated deubiquitination of c-Myc
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2407904121 (2024)
   PUBMED   39432777
  REMARK    GeneRIF: WDR20 prevents hepatocellular carcinoma senescence by
            orchestrating the simultaneous USP12/46-mediated deubiquitination
            of c-Myc.
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Ng,V.H., Spencer,Z., Neitzel,L.R., Nayak,A., Loberg,M.A., Shen,C.,
            Kassel,S.N., Kroh,H.K., An,Z., Anthony,C.C., Bryant,J.M.,
            Lawson,A., Goldsmith,L., Benchabane,H., Hansen,A.G., Li,J.,
            D'Souza,S., Lebensohn,A.M., Rohatgi,R., Weiss,W.A., Weiss,V.L.,
            Williams,C., Hong,C.C., Robbins,D.J., Ahmed,Y. and Lee,E.
  TITLE     The USP46 complex deubiquitylates LRP6 to promote Wnt/beta-catenin
            signaling
  JOURNAL   Nat Commun 14 (1), 6173 (2023)
   PUBMED   37798301
  REMARK    GeneRIF: The USP46 complex deubiquitylates LRP6 to promote
            Wnt/beta-catenin signaling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Ke,L., Jia,Z., Gao,W. and Luo,L.
  TITLE     Ubiquitin specific protease 46 potentiates triple negative breast
            cancer development by stabilizing PGAM1-mediated glycolysis
  JOURNAL   Cell Biol Int 47 (1), 41-51 (2023)
   PUBMED   36335636
  REMARK    GeneRIF: Ubiquitin specific protease 46 potentiates triple negative
            breast cancer development by stabilizing PGAM1-mediated glycolysis.
REFERENCE   6  (residues 1 to 359)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   7  (residues 1 to 359)
  AUTHORS   Cohn,M.A., Kee,Y., Haas,W., Gygi,S.P. and D'Andrea,A.D.
  TITLE     UAF1 is a subunit of multiple deubiquitinating enzyme complexes
  JOURNAL   J Biol Chem 284 (8), 5343-5351 (2009)
   PUBMED   19075014
  REMARK    GeneRIF: two novel multisubunit deubiquitinating enzyme complexes
            containing USP12 and USP46, respectively. Both complexes contain
            the UAF1 protein as a bona fide subunit. Interestingly, UAF1
REFERENCE   8  (residues 1 to 359)
  AUTHORS   Zemunik,T., Boban,M., Lauc,G., Jankovic,S., Rotim,K., Vatavuk,Z.,
            Bencic,G., Dogas,Z., Boraska,V., Torlak,V., Susac,J., Zobic,I.,
            Rudan,D., Pulanic,D., Modun,D., Mudnic,I., Gunjaca,G., Budimir,D.,
            Hayward,C., Vitart,V., Wright,A.F., Campbell,H. and Rudan,I.
  TITLE     Genome-wide association study of biochemical traits in Korcula
            Island, Croatia
  JOURNAL   Croat Med J 50 (1), 23-33 (2009)
   PUBMED   19260141
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   9  (residues 1 to 359)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   10 (residues 1 to 359)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP371221.1, BC037574.1, AC026448.5 and BU620990.1.
            
            Summary: Modification of cellular proteins by ubiquitin is an
            essential regulatory mechanism controlled by the coordinated action
            of multiple ubiquitin-conjugating and deubiquitinating enzymes.
            USP46 belongs to a large family of cysteine proteases that function
            as deubiquitinating enzymes (Quesada et al., 2004 [PubMed
            14715245]).[supplied by OMIM, Jun 2009].
            
            Transcript Variant: This variant (2) contains an alternate
            5'-terminal exon and initiates translation at an alternate start
            codon, compared to variant 1. The encoded isoform (2) has a shorter
            and distinct N-terminus, compared isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1466779.1, AK302438.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..359
                     /product="ubiquitin carboxyl-terminal hydrolase 46 isoform
                     2"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin carboxyl-terminal hydrolase 46; ubiquitin
                     thioesterase 46; deubiquitinating enzyme 46;
                     ubiquitin-specific-processing protease 46; ubiquitin
                     thiolesterase 46"
                     /calculated_mol_wt=41601
     Region          29..356
                     /region_name="Peptidase_C19G"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02663"
                     /db_xref="CDD:239128"
     Site            order(32,37,306,322)
                     /site_type="active"
                     /db_xref="CDD:239128"
     CDS             1..359
                     /gene="USP46"
                     /coded_by="NM_001134223.2:230..1309"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47054.1"
                     /db_xref="GeneID:64854"
                     /db_xref="HGNC:HGNC:20075"
                     /db_xref="MIM:612849"
ORIGIN      
        1 mncfqgtnas alekdigpeq fpinehyfgl vnfgntcycn svlqalyfcr pfrenvlayk
       61 aqqkkkenll tcladlfhsi atqkkkvgvi ppkkfisrlr kendlfdnym qqdaheflny
      121 llntiadilq eekkqekqng klkngnmnep aennkpeltw vheifqgtlt netrclncet
      181 vsskdedfld lsvdveqnts ithclrdfsn tetlcseqky ycetccskqe aqkrmrvkkl
      241 pmilalhlkr fkymeqlhry tklsyrvvfp lelrlfntss davnldrmyd lvavvvhcgs
      301 gpnrghyiti vkshgfwllf dddivekida qaieefyglt sdisknsesg yilfyqsre
//
LOCUS       NP_001355211             444 aa            linear   PRI 28-NOV-2025
DEFINITION  nuclear protein MDM1 isoform 7 [Homo sapiens].
ACCESSION   NP_001355211 XP_016875135
VERSION     NP_001355211.1
DBSOURCE    REFSEQ: accession NM_001368282.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Hensley,M.R., Chua,R.F., Leung,Y.F., Yang,J.Y. and Zhang,G.
  TITLE     Molecular Evolution of MDM1, a 'Duplication-Resistant' Gene in
            Vertebrates
  JOURNAL   PLoS One 11 (9), e0163229 (2016)
   PUBMED   27658201
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Van de Mark,D., Kong,D., Loncarek,J. and Stearns,T.
  TITLE     MDM1 is a microtubule-binding protein that negatively regulates
            centriole duplication
  JOURNAL   Mol Biol Cell 26 (21), 3788-3802 (2015)
   PUBMED   26337392
  REMARK    GeneRIF: Authorse propose that MDM1 is a negative regulator of
            centriole duplication and that its function is mediated through
            microtubule binding.
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Stangeland,B., Mughal,A.A., Grieg,Z., Sandberg,C.J., Joel,M.,
            Nygard,S., Meling,T., Murrell,W., Vik Mo,E.O. and Langmoen,I.A.
  TITLE     Combined expressional analysis, bioinformatics and targeted
            proteomics identify new potential therapeutic targets in
            glioblastoma stem cells
  JOURNAL   Oncotarget 6 (28), 26192-26215 (2015)
   PUBMED   26295306
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Greenwood,T.A., Akiskal,H.S., Akiskal,K.K. and Kelsoe,J.R.
  CONSRTM   Bipolar Genome Study
  TITLE     Genome-wide association study of temperament in bipolar disorder
            reveals significant associations with three novel Loci
  JOURNAL   Biol Psychiatry 72 (4), 303-310 (2012)
   PUBMED   22365631
REFERENCE   8  (residues 1 to 444)
  AUTHORS   Chang,B., Mandal,M.N., Chavali,V.R., Hawes,N.L., Khan,N.W.,
            Hurd,R.E., Smith,R.S., Davisson,M.L., Kopplin,L., Klein,B.E.,
            Klein,R., Iyengar,S.K., Heckenlively,J.R. and Ayyagari,R.
  TITLE     Age-related retinal degeneration (arrd2) in a novel mouse model due
            to a nonsense mutation in the Mdm1 gene
  JOURNAL   Hum Mol Genet 17 (24), 3929-3941 (2008)
   PUBMED   18805803
  REMARK    GeneRIF: Not associated with age-related retinal degeneration.
REFERENCE   9  (residues 1 to 444)
  AUTHORS   Snyder,L.C., Trusko,S.P., Freeman,N., Eshleman,J.R.,
            Fakharzadeh,S.S. and George,D.L.
  TITLE     A gene amplified in a transformed mouse cell line undergoes complex
            transcriptional processing and encodes a nuclear protein
  JOURNAL   J Biol Chem 263 (32), 17150-17158 (1988)
   PUBMED   3182840
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022511.22.
            
            On Feb 2, 2019 this sequence version replaced XP_016875135.1.
            
            Summary: This gene encodes a microtubule-binding nuclear protein
            that localizes to the centrioles of dividing cells and
            differentiating multiciliated cells and negatively regulates
            centriole duplication. The encoded protein is closely associated
            with the centriole barrel, and resides in the centriole lumen.
            Naturally-occurring mutations in the orthologous mouse gene are
            associated with age-related retinal degeneration. [provided by
            RefSeq, Feb 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.30870.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..444
                     /product="nuclear protein MDM1 isoform 7"
                     /note="nuclear protein double minute 1; nuclear protein
                     MDM1; Mdm4, transformed 3T3 cell double minute 1, p53
                     binding protein; Mdm1 nuclear protein"
                     /calculated_mol_wt=49844
     Region          <1..278
                     /region_name="MDM1"
                     /note="Nuclear protein MDM1; pfam15501"
                     /db_xref="CDD:464751"
     CDS             1..444
                     /gene="SAXO6"
                     /gene_synonym="MDM1"
                     /coded_by="NM_001368282.1:2308..3642"
                     /note="isoform 7 is encoded by transcript variant 11"
                     /db_xref="GeneID:56890"
                     /db_xref="HGNC:HGNC:29917"
                     /db_xref="MIM:613813"
ORIGIN      
        1 melkdlhqpk rkltpwkhqr lgkvnseyra kflspaqyly kagawthvkg nmpnqgslna
       61 mwyaevkelr ekaefyrkrv qgthfsrdhl nqilsdsncc wdvssttsse gtvssniral
      121 dlagdptshk tlqkcpstep eekgniveeq pqkntteklg vsaptipvrr rlawdtents
      181 edvqkqpgek eeeddneeeg drktgkqafm geqekldvre kskadkmkeg sdssvssekg
      241 grlptpklre lggiqrthhd lttpavggav lvspskmkpp apeqrkrmts qdcletsknd
      301 ftkkesravs lltspaagik tvdplplred sednihkfae atlpvskipk yptnppgqlp
      361 spphvpsywh psrriqgslr dpefqhnvgk armnnlqlpq heafndeded rlseisarsa
      421 asslrafqtl arakkrkenf wgkt
//
LOCUS       NP_064513                222 aa            linear   PRI 28-NOV-2025
DEFINITION  nuclear protein MDM1 isoform 2 [Homo sapiens].
ACCESSION   NP_064513
VERSION     NP_064513.1
DBSOURCE    REFSEQ: accession NM_020128.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Hensley,M.R., Chua,R.F., Leung,Y.F., Yang,J.Y. and Zhang,G.
  TITLE     Molecular Evolution of MDM1, a 'Duplication-Resistant' Gene in
            Vertebrates
  JOURNAL   PLoS One 11 (9), e0163229 (2016)
   PUBMED   27658201
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Van de Mark,D., Kong,D., Loncarek,J. and Stearns,T.
  TITLE     MDM1 is a microtubule-binding protein that negatively regulates
            centriole duplication
  JOURNAL   Mol Biol Cell 26 (21), 3788-3802 (2015)
   PUBMED   26337392
  REMARK    GeneRIF: Authorse propose that MDM1 is a negative regulator of
            centriole duplication and that its function is mediated through
            microtubule binding.
REFERENCE   6  (residues 1 to 222)
  AUTHORS   Stangeland,B., Mughal,A.A., Grieg,Z., Sandberg,C.J., Joel,M.,
            Nygard,S., Meling,T., Murrell,W., Vik Mo,E.O. and Langmoen,I.A.
  TITLE     Combined expressional analysis, bioinformatics and targeted
            proteomics identify new potential therapeutic targets in
            glioblastoma stem cells
  JOURNAL   Oncotarget 6 (28), 26192-26215 (2015)
   PUBMED   26295306
REFERENCE   7  (residues 1 to 222)
  AUTHORS   Greenwood,T.A., Akiskal,H.S., Akiskal,K.K. and Kelsoe,J.R.
  CONSRTM   Bipolar Genome Study
  TITLE     Genome-wide association study of temperament in bipolar disorder
            reveals significant associations with three novel Loci
  JOURNAL   Biol Psychiatry 72 (4), 303-310 (2012)
   PUBMED   22365631
REFERENCE   8  (residues 1 to 222)
  AUTHORS   Chang,B., Mandal,M.N., Chavali,V.R., Hawes,N.L., Khan,N.W.,
            Hurd,R.E., Smith,R.S., Davisson,M.L., Kopplin,L., Klein,B.E.,
            Klein,R., Iyengar,S.K., Heckenlively,J.R. and Ayyagari,R.
  TITLE     Age-related retinal degeneration (arrd2) in a novel mouse model due
            to a nonsense mutation in the Mdm1 gene
  JOURNAL   Hum Mol Genet 17 (24), 3929-3941 (2008)
   PUBMED   18805803
  REMARK    GeneRIF: Not associated with age-related retinal degeneration.
REFERENCE   9  (residues 1 to 222)
  AUTHORS   Snyder,L.C., Trusko,S.P., Freeman,N., Eshleman,J.R.,
            Fakharzadeh,S.S. and George,D.L.
  TITLE     A gene amplified in a transformed mouse cell line undergoes complex
            transcriptional processing and encodes a nuclear protein
  JOURNAL   J Biol Chem 263 (32), 17150-17158 (1988)
   PUBMED   3182840
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM787113.1, AF267851.1,
            BC010622.1 and AC022511.22.
            
            Summary: This gene encodes a microtubule-binding nuclear protein
            that localizes to the centrioles of dividing cells and
            differentiating multiciliated cells and negatively regulates
            centriole duplication. The encoded protein is closely associated
            with the centriole barrel, and resides in the centriole lumen.
            Naturally-occurring mutations in the orthologous mouse gene are
            associated with age-related retinal degeneration. [provided by
            RefSeq, Feb 2019].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.256927.1,
                                           SRR1660803.88255.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..222
                     /product="nuclear protein MDM1 isoform 2"
                     /note="nuclear protein double minute 1; nuclear protein
                     MDM1; Mdm4, transformed 3T3 cell double minute 1, p53
                     binding protein; Mdm1 nuclear protein"
                     /calculated_mol_wt=24938
     Region          9..>167
                     /region_name="MDM1"
                     /note="Nuclear protein MDM1; pfam15501"
                     /db_xref="CDD:464751"
     Region          9..15
                     /region_name="ST]-E-Y-X(3)-F motif 1, required for
                     efficient microtubule binding and stabilization.
                     /evidence=ECO:0000269|PubMed:26337392"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     Region          79..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D067; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D067; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     CDS             1..222
                     /gene="SAXO6"
                     /gene_synonym="MDM1"
                     /coded_by="NM_020128.4:118..786"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44938.1"
                     /db_xref="GeneID:56890"
                     /db_xref="HGNC:HGNC:29917"
                     /db_xref="MIM:613813"
ORIGIN      
        1 mpvrfkglse yqrnflwkks ylsescnssv grkypwaglr sdqlgitkep sfiskrrvpy
       61 hdpqisksle wngaisesnv vaspepeape tpksqeaeqk dvtqervhsl easrvpkrtr
      121 shsadsraeg asdvennegv tnhtpvnenv elehstkvls envdngvgif taflfksief
      181 figfivisvi lhfvfqnfpl lfsclmsiri vdnrlltlvi vn
//
LOCUS       NP_059136                714 aa            linear   PRI 28-NOV-2025
DEFINITION  nuclear protein MDM1 isoform 1 [Homo sapiens].
ACCESSION   NP_059136
VERSION     NP_059136.2
DBSOURCE    REFSEQ: accession NM_017440.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 714)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 714)
  AUTHORS   Hensley,M.R., Chua,R.F., Leung,Y.F., Yang,J.Y. and Zhang,G.
  TITLE     Molecular Evolution of MDM1, a 'Duplication-Resistant' Gene in
            Vertebrates
  JOURNAL   PLoS One 11 (9), e0163229 (2016)
   PUBMED   27658201
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 714)
  AUTHORS   Van de Mark,D., Kong,D., Loncarek,J. and Stearns,T.
  TITLE     MDM1 is a microtubule-binding protein that negatively regulates
            centriole duplication
  JOURNAL   Mol Biol Cell 26 (21), 3788-3802 (2015)
   PUBMED   26337392
  REMARK    GeneRIF: Authorse propose that MDM1 is a negative regulator of
            centriole duplication and that its function is mediated through
            microtubule binding.
REFERENCE   6  (residues 1 to 714)
  AUTHORS   Stangeland,B., Mughal,A.A., Grieg,Z., Sandberg,C.J., Joel,M.,
            Nygard,S., Meling,T., Murrell,W., Vik Mo,E.O. and Langmoen,I.A.
  TITLE     Combined expressional analysis, bioinformatics and targeted
            proteomics identify new potential therapeutic targets in
            glioblastoma stem cells
  JOURNAL   Oncotarget 6 (28), 26192-26215 (2015)
   PUBMED   26295306
REFERENCE   7  (residues 1 to 714)
  AUTHORS   Greenwood,T.A., Akiskal,H.S., Akiskal,K.K. and Kelsoe,J.R.
  CONSRTM   Bipolar Genome Study
  TITLE     Genome-wide association study of temperament in bipolar disorder
            reveals significant associations with three novel Loci
  JOURNAL   Biol Psychiatry 72 (4), 303-310 (2012)
   PUBMED   22365631
REFERENCE   8  (residues 1 to 714)
  AUTHORS   Chang,B., Mandal,M.N., Chavali,V.R., Hawes,N.L., Khan,N.W.,
            Hurd,R.E., Smith,R.S., Davisson,M.L., Kopplin,L., Klein,B.E.,
            Klein,R., Iyengar,S.K., Heckenlively,J.R. and Ayyagari,R.
  TITLE     Age-related retinal degeneration (arrd2) in a novel mouse model due
            to a nonsense mutation in the Mdm1 gene
  JOURNAL   Hum Mol Genet 17 (24), 3929-3941 (2008)
   PUBMED   18805803
  REMARK    GeneRIF: Not associated with age-related retinal degeneration.
REFERENCE   9  (residues 1 to 714)
  AUTHORS   Snyder,L.C., Trusko,S.P., Freeman,N., Eshleman,J.R.,
            Fakharzadeh,S.S. and George,D.L.
  TITLE     A gene amplified in a transformed mouse cell line undergoes complex
            transcriptional processing and encodes a nuclear protein
  JOURNAL   J Biol Chem 263 (32), 17150-17158 (1988)
   PUBMED   3182840
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD704611.1, AK314461.1,
            BC010622.1, BC028355.2 and AK026745.1.
            
            On Apr 11, 2008 this sequence version replaced NP_059136.1.
            
            Summary: This gene encodes a microtubule-binding nuclear protein
            that localizes to the centrioles of dividing cells and
            differentiating multiciliated cells and negatively regulates
            centriole duplication. The encoded protein is closely associated
            with the centriole barrel, and resides in the centriole lumen.
            Naturally-occurring mutations in the orthologous mouse gene are
            associated with age-related retinal degeneration. [provided by
            RefSeq, Feb 2019].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028355.2, SRR14038191.82244.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..714
                     /product="nuclear protein MDM1 isoform 1"
                     /note="nuclear protein double minute 1; nuclear protein
                     MDM1; Mdm4, transformed 3T3 cell double minute 1, p53
                     binding protein; Mdm1 nuclear protein"
                     /calculated_mol_wt=80604
     Region          9..548
                     /region_name="MDM1"
                     /note="Nuclear protein MDM1; pfam15501"
                     /db_xref="CDD:464751"
     Region          9..15
                     /region_name="ST]-E-Y-X(3)-F motif 1, required for
                     efficient microtubule binding and stabilization.
                     /evidence=ECO:0000269|PubMed:26337392"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     Region          79..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D067; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D067; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Region          189..195
                     /region_name="ST]-E-Y-X(3)-F motif 2, required for
                     efficient microtubule binding and stabilization.
                     /evidence=ECO:0000269|PubMed:26337392"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     Region          232..238
                     /region_name="ST]-E-Y-X(3)-F motif 3, required for
                     efficient microtubule binding and stabilization.
                     /evidence=ECO:0000269|PubMed:26337392"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Region          306..312
                     /region_name="ST]-E-Y-X(3)-F motif 4, required for
                     efficient microtubule binding and stabilization.
                     /evidence=ECO:0000269|PubMed:26337392"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D067; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Region          391..571
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D067; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Region          616..637
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     CDS             1..714
                     /gene="SAXO6"
                     /gene_synonym="MDM1"
                     /coded_by="NM_017440.6:118..2262"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8983.1"
                     /db_xref="GeneID:56890"
                     /db_xref="HGNC:HGNC:29917"
                     /db_xref="MIM:613813"
ORIGIN      
        1 mpvrfkglse yqrnflwkks ylsescnssv grkypwaglr sdqlgitkep sfiskrrvpy
       61 hdpqisksle wngaisesnv vaspepeape tpksqeaeqk dvtqervhsl easrvpkrtr
      121 shsadsraeg asdvennegv tnhtpvnenv elehstkvls envdngldrl lrkkagltvv
      181 psynalrnse yqrqfvwkts ketapafaan qvfhnksqfv ppfkgnsvih eteykrnfkg
      241 lspvkepklr ndlrenrnle tvsperksnk iddrlkleae melkdlhqpk rkltpwkhqr
      301 lgkvnseyra kflspaqyly kagawthvkg nmpnqvkelr ekaefyrkrv qgthfsrdhl
      361 nqilsdsncc wdvssttsse gtvssniral dlagdptshk tlqkcpstep eekgniveeq
      421 pqkntteklg vsaptipvrr rlawdtents edvqkqpgek eeeddneeeg drktgkqafm
      481 geqekldvre kskadkmkeg sdssvssekg grlptpklre lggiqrthhd lttpavggav
      541 lvspskmkpp apeqrkrmts qdcletsknd ftkkesravs lltspaagik tvdplplred
      601 sednihkfae atlpvskipk yptnppgqlp spphvpsywh psrriqgslr dpefqhnvgk
      661 armnnlqlpq heafndeded rlseisarsa asslrafqtl arakkrkenf wgkt
//
LOCUS       NP_001341901             444 aa            linear   PRI 28-NOV-2025
DEFINITION  nuclear protein MDM1 isoform 7 [Homo sapiens].
ACCESSION   NP_001341901 XP_016875137
VERSION     NP_001341901.1
DBSOURCE    REFSEQ: accession NM_001354972.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Hensley,M.R., Chua,R.F., Leung,Y.F., Yang,J.Y. and Zhang,G.
  TITLE     Molecular Evolution of MDM1, a 'Duplication-Resistant' Gene in
            Vertebrates
  JOURNAL   PLoS One 11 (9), e0163229 (2016)
   PUBMED   27658201
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Van de Mark,D., Kong,D., Loncarek,J. and Stearns,T.
  TITLE     MDM1 is a microtubule-binding protein that negatively regulates
            centriole duplication
  JOURNAL   Mol Biol Cell 26 (21), 3788-3802 (2015)
   PUBMED   26337392
  REMARK    GeneRIF: Authorse propose that MDM1 is a negative regulator of
            centriole duplication and that its function is mediated through
            microtubule binding.
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Stangeland,B., Mughal,A.A., Grieg,Z., Sandberg,C.J., Joel,M.,
            Nygard,S., Meling,T., Murrell,W., Vik Mo,E.O. and Langmoen,I.A.
  TITLE     Combined expressional analysis, bioinformatics and targeted
            proteomics identify new potential therapeutic targets in
            glioblastoma stem cells
  JOURNAL   Oncotarget 6 (28), 26192-26215 (2015)
   PUBMED   26295306
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Greenwood,T.A., Akiskal,H.S., Akiskal,K.K. and Kelsoe,J.R.
  CONSRTM   Bipolar Genome Study
  TITLE     Genome-wide association study of temperament in bipolar disorder
            reveals significant associations with three novel Loci
  JOURNAL   Biol Psychiatry 72 (4), 303-310 (2012)
   PUBMED   22365631
REFERENCE   8  (residues 1 to 444)
  AUTHORS   Chang,B., Mandal,M.N., Chavali,V.R., Hawes,N.L., Khan,N.W.,
            Hurd,R.E., Smith,R.S., Davisson,M.L., Kopplin,L., Klein,B.E.,
            Klein,R., Iyengar,S.K., Heckenlively,J.R. and Ayyagari,R.
  TITLE     Age-related retinal degeneration (arrd2) in a novel mouse model due
            to a nonsense mutation in the Mdm1 gene
  JOURNAL   Hum Mol Genet 17 (24), 3929-3941 (2008)
   PUBMED   18805803
  REMARK    GeneRIF: Not associated with age-related retinal degeneration.
REFERENCE   9  (residues 1 to 444)
  AUTHORS   Snyder,L.C., Trusko,S.P., Freeman,N., Eshleman,J.R.,
            Fakharzadeh,S.S. and George,D.L.
  TITLE     A gene amplified in a transformed mouse cell line undergoes complex
            transcriptional processing and encodes a nuclear protein
  JOURNAL   J Biol Chem 263 (32), 17150-17158 (1988)
   PUBMED   3182840
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022511.22 and AK026745.1.
            
            On Aug 31, 2017 this sequence version replaced XP_016875137.1.
            
            Summary: This gene encodes a microtubule-binding nuclear protein
            that localizes to the centrioles of dividing cells and
            differentiating multiciliated cells and negatively regulates
            centriole duplication. The encoded protein is closely associated
            with the centriole barrel, and resides in the centriole lumen.
            Naturally-occurring mutations in the orthologous mouse gene are
            associated with age-related retinal degeneration. [provided by
            RefSeq, Feb 2019].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.4854.1,
                                           SRR14372079.2014250.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..444
                     /product="nuclear protein MDM1 isoform 7"
                     /note="nuclear protein double minute 1; nuclear protein
                     MDM1; Mdm4, transformed 3T3 cell double minute 1, p53
                     binding protein; Mdm1 nuclear protein"
                     /calculated_mol_wt=49844
     Region          <1..278
                     /region_name="MDM1"
                     /note="Nuclear protein MDM1; pfam15501"
                     /db_xref="CDD:464751"
     CDS             1..444
                     /gene="SAXO6"
                     /gene_synonym="MDM1"
                     /coded_by="NM_001354972.2:1447..2781"
                     /note="isoform 7 is encoded by transcript variant 8"
                     /db_xref="GeneID:56890"
                     /db_xref="HGNC:HGNC:29917"
                     /db_xref="MIM:613813"
ORIGIN      
        1 melkdlhqpk rkltpwkhqr lgkvnseyra kflspaqyly kagawthvkg nmpnqgslna
       61 mwyaevkelr ekaefyrkrv qgthfsrdhl nqilsdsncc wdvssttsse gtvssniral
      121 dlagdptshk tlqkcpstep eekgniveeq pqkntteklg vsaptipvrr rlawdtents
      181 edvqkqpgek eeeddneeeg drktgkqafm geqekldvre kskadkmkeg sdssvssekg
      241 grlptpklre lggiqrthhd lttpavggav lvspskmkpp apeqrkrmts qdcletsknd
      301 ftkkesravs lltspaagik tvdplplred sednihkfae atlpvskipk yptnppgqlp
      361 spphvpsywh psrriqgslr dpefqhnvgk armnnlqlpq heafndeded rlseisarsa
      421 asslrafqtl arakkrkenf wgkt
//
LOCUS       NP_001341903             434 aa            linear   PRI 28-NOV-2025
DEFINITION  nuclear protein MDM1 isoform 8 [Homo sapiens].
ACCESSION   NP_001341903
VERSION     NP_001341903.1
DBSOURCE    REFSEQ: accession NM_001354974.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Hensley,M.R., Chua,R.F., Leung,Y.F., Yang,J.Y. and Zhang,G.
  TITLE     Molecular Evolution of MDM1, a 'Duplication-Resistant' Gene in
            Vertebrates
  JOURNAL   PLoS One 11 (9), e0163229 (2016)
   PUBMED   27658201
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Van de Mark,D., Kong,D., Loncarek,J. and Stearns,T.
  TITLE     MDM1 is a microtubule-binding protein that negatively regulates
            centriole duplication
  JOURNAL   Mol Biol Cell 26 (21), 3788-3802 (2015)
   PUBMED   26337392
  REMARK    GeneRIF: Authorse propose that MDM1 is a negative regulator of
            centriole duplication and that its function is mediated through
            microtubule binding.
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Stangeland,B., Mughal,A.A., Grieg,Z., Sandberg,C.J., Joel,M.,
            Nygard,S., Meling,T., Murrell,W., Vik Mo,E.O. and Langmoen,I.A.
  TITLE     Combined expressional analysis, bioinformatics and targeted
            proteomics identify new potential therapeutic targets in
            glioblastoma stem cells
  JOURNAL   Oncotarget 6 (28), 26192-26215 (2015)
   PUBMED   26295306
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Greenwood,T.A., Akiskal,H.S., Akiskal,K.K. and Kelsoe,J.R.
  CONSRTM   Bipolar Genome Study
  TITLE     Genome-wide association study of temperament in bipolar disorder
            reveals significant associations with three novel Loci
  JOURNAL   Biol Psychiatry 72 (4), 303-310 (2012)
   PUBMED   22365631
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Chang,B., Mandal,M.N., Chavali,V.R., Hawes,N.L., Khan,N.W.,
            Hurd,R.E., Smith,R.S., Davisson,M.L., Kopplin,L., Klein,B.E.,
            Klein,R., Iyengar,S.K., Heckenlively,J.R. and Ayyagari,R.
  TITLE     Age-related retinal degeneration (arrd2) in a novel mouse model due
            to a nonsense mutation in the Mdm1 gene
  JOURNAL   Hum Mol Genet 17 (24), 3929-3941 (2008)
   PUBMED   18805803
  REMARK    GeneRIF: Not associated with age-related retinal degeneration.
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Snyder,L.C., Trusko,S.P., Freeman,N., Eshleman,J.R.,
            Fakharzadeh,S.S. and George,D.L.
  TITLE     A gene amplified in a transformed mouse cell line undergoes complex
            transcriptional processing and encodes a nuclear protein
  JOURNAL   J Biol Chem 263 (32), 17150-17158 (1988)
   PUBMED   3182840
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022511.22, BC034945.1 and
            AK026745.1.
            
            Summary: This gene encodes a microtubule-binding nuclear protein
            that localizes to the centrioles of dividing cells and
            differentiating multiciliated cells and negatively regulates
            centriole duplication. The encoded protein is closely associated
            with the centriole barrel, and resides in the centriole lumen.
            Naturally-occurring mutations in the orthologous mouse gene are
            associated with age-related retinal degeneration. [provided by
            RefSeq, Feb 2019].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034945.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..434
                     /product="nuclear protein MDM1 isoform 8"
                     /note="nuclear protein double minute 1; nuclear protein
                     MDM1; Mdm4, transformed 3T3 cell double minute 1, p53
                     binding protein; Mdm1 nuclear protein"
                     /calculated_mol_wt=48721
     Region          <1..268
                     /region_name="MDM1"
                     /note="Nuclear protein MDM1; pfam15501"
                     /db_xref="CDD:464751"
     CDS             1..434
                     /gene="SAXO6"
                     /gene_synonym="MDM1"
                     /coded_by="NM_001354974.2:593..1897"
                     /note="isoform 8 is encoded by transcript variant 10"
                     /db_xref="GeneID:56890"
                     /db_xref="HGNC:HGNC:29917"
                     /db_xref="MIM:613813"
ORIGIN      
        1 melkdlhqpk rkltpwkhqr lgkvnseyra kflspaqyly kagawthvkg nmpnqvkelr
       61 ekaefyrkrv qgthfsrdhl nqilsdsncc wdvssttsse gtvssniral dlagdptshk
      121 tlqkcpstep eekgniveeq pqkntteklg vsaptipvrr rlawdtents edvqkqpgek
      181 eeeddneeeg drktgkqafm geqekldvre kskadkmkeg sdssvssekg grlptpklre
      241 lggiqrthhd lttpavggav lvspskmkpp apeqrkrmts qdcletsknd ftkkesravs
      301 lltspaagik tvdplplred sednihkfae atlpvskipk yptnppgqlp spphvpsywh
      361 psrriqgslr dpefqhnvgk armnnlqlpq heafndeded rlseisarsa asslrafqtl
      421 arakkrkenf wgkt
//
LOCUS       NP_001191957             679 aa            linear   PRI 28-NOV-2025
DEFINITION  nuclear protein MDM1 isoform 4 [Homo sapiens].
ACCESSION   NP_001191957
VERSION     NP_001191957.1
DBSOURCE    REFSEQ: accession NM_001205028.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 679)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 679)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 679)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 679)
  AUTHORS   Hensley,M.R., Chua,R.F., Leung,Y.F., Yang,J.Y. and Zhang,G.
  TITLE     Molecular Evolution of MDM1, a 'Duplication-Resistant' Gene in
            Vertebrates
  JOURNAL   PLoS One 11 (9), e0163229 (2016)
   PUBMED   27658201
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 679)
  AUTHORS   Van de Mark,D., Kong,D., Loncarek,J. and Stearns,T.
  TITLE     MDM1 is a microtubule-binding protein that negatively regulates
            centriole duplication
  JOURNAL   Mol Biol Cell 26 (21), 3788-3802 (2015)
   PUBMED   26337392
  REMARK    GeneRIF: Authorse propose that MDM1 is a negative regulator of
            centriole duplication and that its function is mediated through
            microtubule binding.
REFERENCE   6  (residues 1 to 679)
  AUTHORS   Stangeland,B., Mughal,A.A., Grieg,Z., Sandberg,C.J., Joel,M.,
            Nygard,S., Meling,T., Murrell,W., Vik Mo,E.O. and Langmoen,I.A.
  TITLE     Combined expressional analysis, bioinformatics and targeted
            proteomics identify new potential therapeutic targets in
            glioblastoma stem cells
  JOURNAL   Oncotarget 6 (28), 26192-26215 (2015)
   PUBMED   26295306
REFERENCE   7  (residues 1 to 679)
  AUTHORS   Greenwood,T.A., Akiskal,H.S., Akiskal,K.K. and Kelsoe,J.R.
  CONSRTM   Bipolar Genome Study
  TITLE     Genome-wide association study of temperament in bipolar disorder
            reveals significant associations with three novel Loci
  JOURNAL   Biol Psychiatry 72 (4), 303-310 (2012)
   PUBMED   22365631
REFERENCE   8  (residues 1 to 679)
  AUTHORS   Chang,B., Mandal,M.N., Chavali,V.R., Hawes,N.L., Khan,N.W.,
            Hurd,R.E., Smith,R.S., Davisson,M.L., Kopplin,L., Klein,B.E.,
            Klein,R., Iyengar,S.K., Heckenlively,J.R. and Ayyagari,R.
  TITLE     Age-related retinal degeneration (arrd2) in a novel mouse model due
            to a nonsense mutation in the Mdm1 gene
  JOURNAL   Hum Mol Genet 17 (24), 3929-3941 (2008)
   PUBMED   18805803
  REMARK    GeneRIF: Not associated with age-related retinal degeneration.
REFERENCE   9  (residues 1 to 679)
  AUTHORS   Snyder,L.C., Trusko,S.P., Freeman,N., Eshleman,J.R.,
            Fakharzadeh,S.S. and George,D.L.
  TITLE     A gene amplified in a transformed mouse cell line undergoes complex
            transcriptional processing and encodes a nuclear protein
  JOURNAL   J Biol Chem 263 (32), 17150-17158 (1988)
   PUBMED   3182840
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM787113.1, AF267851.1,
            AK297311.1 and AK026745.1.
            
            Summary: This gene encodes a microtubule-binding nuclear protein
            that localizes to the centrioles of dividing cells and
            differentiating multiciliated cells and negatively regulates
            centriole duplication. The encoded protein is closely associated
            with the centriole barrel, and resides in the centriole lumen.
            Naturally-occurring mutations in the orthologous mouse gene are
            associated with age-related retinal degeneration. [provided by
            RefSeq, Feb 2019].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297311.1, SRR14038195.65218.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..679
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..679
                     /product="nuclear protein MDM1 isoform 4"
                     /note="nuclear protein double minute 1; nuclear protein
                     MDM1; Mdm4, transformed 3T3 cell double minute 1, p53
                     binding protein; Mdm1 nuclear protein"
                     /calculated_mol_wt=76578
     Region          9..513
                     /region_name="MDM1"
                     /note="Nuclear protein MDM1; pfam15501"
                     /db_xref="CDD:464751"
     CDS             1..679
                     /gene="SAXO6"
                     /gene_synonym="MDM1"
                     /coded_by="NM_001205028.3:118..2157"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS55841.1"
                     /db_xref="GeneID:56890"
                     /db_xref="HGNC:HGNC:29917"
                     /db_xref="MIM:613813"
ORIGIN      
        1 mpvrfkglse yqrnflwkks ylsescnssv grkypwaglr sdqlgitkep sfiskrrvpy
       61 hdpqisksle wngaisesnv vaspepeape tpksqeaeqk dvtqervhsl easrvpkrtr
      121 shsadsraeg asdvennegv tnhtpvnenv elehstkvls envdngvfhn ksqfvppfkg
      181 nsviheteyk rnfkglspvk epklrndlre nrnletvspe rksnkiddrl kleaemelkd
      241 lhqpkrkltp wkhqrlgkvn seyrakflsp aqylykagaw thvkgnmpnq gslnamwyae
      301 vkelrekaef yrkrvqgthf srdhlnqils dsnccwdvss ttssegtvss niraldlagd
      361 ptshktlqkc pstepeekgn iveeqpqknt teklgvsapt ipvrrrlawd tentsedvqk
      421 qpgekeeedd neeegdrktg kqafmgeqek ldvrekskad kmkegsdssv ssekggrlpt
      481 pklrelggiq rthhdlttpa vggavlvsps kmkppapeqr krmtsqdcle tskndftkke
      541 sravslltsp aagiktvdpl plredsedni hkfaeatlpv skipkyptnp pgqlpspphv
      601 psywhpsrri qgslrdpefq hnvgkarmnn lqlpqheafn dededrlsei sarsaasslr
      661 afqtlarakk rkenfwgkt
//
LOCUS       NP_001341898             724 aa            linear   PRI 28-NOV-2025
DEFINITION  nuclear protein MDM1 isoform 5 [Homo sapiens].
ACCESSION   NP_001341898 XP_005269083
VERSION     NP_001341898.1
DBSOURCE    REFSEQ: accession NM_001354969.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 724)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 724)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 724)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 724)
  AUTHORS   Hensley,M.R., Chua,R.F., Leung,Y.F., Yang,J.Y. and Zhang,G.
  TITLE     Molecular Evolution of MDM1, a 'Duplication-Resistant' Gene in
            Vertebrates
  JOURNAL   PLoS One 11 (9), e0163229 (2016)
   PUBMED   27658201
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 724)
  AUTHORS   Van de Mark,D., Kong,D., Loncarek,J. and Stearns,T.
  TITLE     MDM1 is a microtubule-binding protein that negatively regulates
            centriole duplication
  JOURNAL   Mol Biol Cell 26 (21), 3788-3802 (2015)
   PUBMED   26337392
  REMARK    GeneRIF: Authorse propose that MDM1 is a negative regulator of
            centriole duplication and that its function is mediated through
            microtubule binding.
REFERENCE   6  (residues 1 to 724)
  AUTHORS   Stangeland,B., Mughal,A.A., Grieg,Z., Sandberg,C.J., Joel,M.,
            Nygard,S., Meling,T., Murrell,W., Vik Mo,E.O. and Langmoen,I.A.
  TITLE     Combined expressional analysis, bioinformatics and targeted
            proteomics identify new potential therapeutic targets in
            glioblastoma stem cells
  JOURNAL   Oncotarget 6 (28), 26192-26215 (2015)
   PUBMED   26295306
REFERENCE   7  (residues 1 to 724)
  AUTHORS   Greenwood,T.A., Akiskal,H.S., Akiskal,K.K. and Kelsoe,J.R.
  CONSRTM   Bipolar Genome Study
  TITLE     Genome-wide association study of temperament in bipolar disorder
            reveals significant associations with three novel Loci
  JOURNAL   Biol Psychiatry 72 (4), 303-310 (2012)
   PUBMED   22365631
REFERENCE   8  (residues 1 to 724)
  AUTHORS   Chang,B., Mandal,M.N., Chavali,V.R., Hawes,N.L., Khan,N.W.,
            Hurd,R.E., Smith,R.S., Davisson,M.L., Kopplin,L., Klein,B.E.,
            Klein,R., Iyengar,S.K., Heckenlively,J.R. and Ayyagari,R.
  TITLE     Age-related retinal degeneration (arrd2) in a novel mouse model due
            to a nonsense mutation in the Mdm1 gene
  JOURNAL   Hum Mol Genet 17 (24), 3929-3941 (2008)
   PUBMED   18805803
  REMARK    GeneRIF: Not associated with age-related retinal degeneration.
REFERENCE   9  (residues 1 to 724)
  AUTHORS   Snyder,L.C., Trusko,S.P., Freeman,N., Eshleman,J.R.,
            Fakharzadeh,S.S. and George,D.L.
  TITLE     A gene amplified in a transformed mouse cell line undergoes complex
            transcriptional processing and encodes a nuclear protein
  JOURNAL   J Biol Chem 263 (32), 17150-17158 (1988)
   PUBMED   3182840
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022511.22 and AK026745.1.
            
            On Aug 31, 2017 this sequence version replaced XP_005269083.1.
            
            Summary: This gene encodes a microtubule-binding nuclear protein
            that localizes to the centrioles of dividing cells and
            differentiating multiciliated cells and negatively regulates
            centriole duplication. The encoded protein is closely associated
            with the centriole barrel, and resides in the centriole lumen.
            Naturally-occurring mutations in the orthologous mouse gene are
            associated with age-related retinal degeneration. [provided by
            RefSeq, Feb 2019].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.7860.1,
                                           SRR14038195.1493172.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000682720.1/ ENSP00000507100.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..724
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..724
                     /product="nuclear protein MDM1 isoform 5"
                     /note="nuclear protein double minute 1; nuclear protein
                     MDM1; Mdm4, transformed 3T3 cell double minute 1, p53
                     binding protein; Mdm1 nuclear protein"
                     /calculated_mol_wt=81728
     Region          9..558
                     /region_name="MDM1"
                     /note="Nuclear protein MDM1; pfam15501"
                     /db_xref="CDD:464751"
     Region          9..15
                     /region_name="ST]-E-Y-X(3)-F motif 1, required for
                     efficient microtubule binding and stabilization.
                     /evidence=ECO:0000269|PubMed:26337392"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     Region          79..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D067; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D067; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Region          189..195
                     /region_name="ST]-E-Y-X(3)-F motif 2, required for
                     efficient microtubule binding and stabilization.
                     /evidence=ECO:0000269|PubMed:26337392"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     Region          232..238
                     /region_name="ST]-E-Y-X(3)-F motif 3, required for
                     efficient microtubule binding and stabilization.
                     /evidence=ECO:0000269|PubMed:26337392"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Region          306..312
                     /region_name="ST]-E-Y-X(3)-F motif 4, required for
                     efficient microtubule binding and stabilization.
                     /evidence=ECO:0000269|PubMed:26337392"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D067; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Region          401..581
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D067; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     Region          626..647
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     Site            658
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TC05.2)"
     CDS             1..724
                     /gene="SAXO6"
                     /gene_synonym="MDM1"
                     /coded_by="NM_001354969.2:118..2292"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS91723.1"
                     /db_xref="GeneID:56890"
                     /db_xref="HGNC:HGNC:29917"
                     /db_xref="MIM:613813"
ORIGIN      
        1 mpvrfkglse yqrnflwkks ylsescnssv grkypwaglr sdqlgitkep sfiskrrvpy
       61 hdpqisksle wngaisesnv vaspepeape tpksqeaeqk dvtqervhsl easrvpkrtr
      121 shsadsraeg asdvennegv tnhtpvnenv elehstkvls envdngldrl lrkkagltvv
      181 psynalrnse yqrqfvwkts ketapafaan qvfhnksqfv ppfkgnsvih eteykrnfkg
      241 lspvkepklr ndlrenrnle tvsperksnk iddrlkleae melkdlhqpk rkltpwkhqr
      301 lgkvnseyra kflspaqyly kagawthvkg nmpnqgslna mwyaevkelr ekaefyrkrv
      361 qgthfsrdhl nqilsdsncc wdvssttsse gtvssniral dlagdptshk tlqkcpstep
      421 eekgniveeq pqkntteklg vsaptipvrr rlawdtents edvqkqpgek eeeddneeeg
      481 drktgkqafm geqekldvre kskadkmkeg sdssvssekg grlptpklre lggiqrthhd
      541 lttpavggav lvspskmkpp apeqrkrmts qdcletsknd ftkkesravs lltspaagik
      601 tvdplplred sednihkfae atlpvskipk yptnppgqlp spphvpsywh psrriqgslr
      661 dpefqhnvgk armnnlqlpq heafndeded rlseisarsa asslrafqtl arakkrkenf
      721 wgkt
//
LOCUS       NP_001341899             674 aa            linear   PRI 28-NOV-2025
DEFINITION  nuclear protein MDM1 isoform 6 [Homo sapiens].
ACCESSION   NP_001341899
VERSION     NP_001341899.1
DBSOURCE    REFSEQ: accession NM_001354970.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 674)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 674)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 674)
  AUTHORS   Hensley,M.R., Chua,R.F., Leung,Y.F., Yang,J.Y. and Zhang,G.
  TITLE     Molecular Evolution of MDM1, a 'Duplication-Resistant' Gene in
            Vertebrates
  JOURNAL   PLoS One 11 (9), e0163229 (2016)
   PUBMED   27658201
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 674)
  AUTHORS   Van de Mark,D., Kong,D., Loncarek,J. and Stearns,T.
  TITLE     MDM1 is a microtubule-binding protein that negatively regulates
            centriole duplication
  JOURNAL   Mol Biol Cell 26 (21), 3788-3802 (2015)
   PUBMED   26337392
  REMARK    GeneRIF: Authorse propose that MDM1 is a negative regulator of
            centriole duplication and that its function is mediated through
            microtubule binding.
REFERENCE   6  (residues 1 to 674)
  AUTHORS   Stangeland,B., Mughal,A.A., Grieg,Z., Sandberg,C.J., Joel,M.,
            Nygard,S., Meling,T., Murrell,W., Vik Mo,E.O. and Langmoen,I.A.
  TITLE     Combined expressional analysis, bioinformatics and targeted
            proteomics identify new potential therapeutic targets in
            glioblastoma stem cells
  JOURNAL   Oncotarget 6 (28), 26192-26215 (2015)
   PUBMED   26295306
REFERENCE   7  (residues 1 to 674)
  AUTHORS   Greenwood,T.A., Akiskal,H.S., Akiskal,K.K. and Kelsoe,J.R.
  CONSRTM   Bipolar Genome Study
  TITLE     Genome-wide association study of temperament in bipolar disorder
            reveals significant associations with three novel Loci
  JOURNAL   Biol Psychiatry 72 (4), 303-310 (2012)
   PUBMED   22365631
REFERENCE   8  (residues 1 to 674)
  AUTHORS   Chang,B., Mandal,M.N., Chavali,V.R., Hawes,N.L., Khan,N.W.,
            Hurd,R.E., Smith,R.S., Davisson,M.L., Kopplin,L., Klein,B.E.,
            Klein,R., Iyengar,S.K., Heckenlively,J.R. and Ayyagari,R.
  TITLE     Age-related retinal degeneration (arrd2) in a novel mouse model due
            to a nonsense mutation in the Mdm1 gene
  JOURNAL   Hum Mol Genet 17 (24), 3929-3941 (2008)
   PUBMED   18805803
  REMARK    GeneRIF: Not associated with age-related retinal degeneration.
REFERENCE   9  (residues 1 to 674)
  AUTHORS   Snyder,L.C., Trusko,S.P., Freeman,N., Eshleman,J.R.,
            Fakharzadeh,S.S. and George,D.L.
  TITLE     A gene amplified in a transformed mouse cell line undergoes complex
            transcriptional processing and encodes a nuclear protein
  JOURNAL   J Biol Chem 263 (32), 17150-17158 (1988)
   PUBMED   3182840
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022511.22 and AK026745.1.
            
            Summary: This gene encodes a microtubule-binding nuclear protein
            that localizes to the centrioles of dividing cells and
            differentiating multiciliated cells and negatively regulates
            centriole duplication. The encoded protein is closely associated
            with the centriole barrel, and resides in the centriole lumen.
            Naturally-occurring mutations in the orthologous mouse gene are
            associated with age-related retinal degeneration. [provided by
            RefSeq, Feb 2019].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.104679.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..674
                     /product="nuclear protein MDM1 isoform 6"
                     /note="nuclear protein double minute 1; nuclear protein
                     MDM1; Mdm4, transformed 3T3 cell double minute 1, p53
                     binding protein; Mdm1 nuclear protein"
                     /calculated_mol_wt=75950
     Region          4..508
                     /region_name="MDM1"
                     /note="Nuclear protein MDM1; pfam15501"
                     /db_xref="CDD:464751"
     CDS             1..674
                     /gene="SAXO6"
                     /gene_synonym="MDM1"
                     /coded_by="NM_001354970.2:360..2384"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:56890"
                     /db_xref="HGNC:HGNC:29917"
                     /db_xref="MIM:613813"
ORIGIN      
        1 mglseyqrnf lwkksylses cnssvgrkyp waglrsdqlg itkepsfisk rrvpyhdpqi
       61 skslewngai sesnvvaspe peapetpksq eaeqkdvtqe rvhsleasrv pkrtrshsad
      121 sraegasdve nnegvtnhtp vnenvelehs tkvlsenvdn gvfhnksqfv ppfkgnsvih
      181 eteykrnfkg lspvkepklr ndlrenrnle tvsperksnk iddrlkleae melkdlhqpk
      241 rkltpwkhqr lgkvnseyra kflspaqyly kagawthvkg nmpnqgslna mwyaevkelr
      301 ekaefyrkrv qgthfsrdhl nqilsdsncc wdvssttsse gtvssniral dlagdptshk
      361 tlqkcpstep eekgniveeq pqkntteklg vsaptipvrr rlawdtents edvqkqpgek
      421 eeeddneeeg drktgkqafm geqekldvre kskadkmkeg sdssvssekg grlptpklre
      481 lggiqrthhd lttpavggav lvspskmkpp apeqrkrmts qdcletsknd ftkkesravs
      541 lltspaagik tvdplplred sednihkfae atlpvskipk yptnppgqlp spphvpsywh
      601 psrriqgslr dpefqhnvgk armnnlqlpq heafndeded rlseisarsa asslrafqtl
      661 arakkrkenf wgkt
//
LOCUS       NP_001191958              69 aa            linear   PRI 28-NOV-2025
DEFINITION  nuclear protein MDM1 isoform 3 [Homo sapiens].
ACCESSION   NP_001191958
VERSION     NP_001191958.1
DBSOURCE    REFSEQ: accession NM_001205029.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 69)
  AUTHORS   Hensley,M.R., Chua,R.F., Leung,Y.F., Yang,J.Y. and Zhang,G.
  TITLE     Molecular Evolution of MDM1, a 'Duplication-Resistant' Gene in
            Vertebrates
  JOURNAL   PLoS One 11 (9), e0163229 (2016)
   PUBMED   27658201
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 69)
  AUTHORS   Van de Mark,D., Kong,D., Loncarek,J. and Stearns,T.
  TITLE     MDM1 is a microtubule-binding protein that negatively regulates
            centriole duplication
  JOURNAL   Mol Biol Cell 26 (21), 3788-3802 (2015)
   PUBMED   26337392
  REMARK    GeneRIF: Authorse propose that MDM1 is a negative regulator of
            centriole duplication and that its function is mediated through
            microtubule binding.
REFERENCE   6  (residues 1 to 69)
  AUTHORS   Stangeland,B., Mughal,A.A., Grieg,Z., Sandberg,C.J., Joel,M.,
            Nygard,S., Meling,T., Murrell,W., Vik Mo,E.O. and Langmoen,I.A.
  TITLE     Combined expressional analysis, bioinformatics and targeted
            proteomics identify new potential therapeutic targets in
            glioblastoma stem cells
  JOURNAL   Oncotarget 6 (28), 26192-26215 (2015)
   PUBMED   26295306
REFERENCE   7  (residues 1 to 69)
  AUTHORS   Greenwood,T.A., Akiskal,H.S., Akiskal,K.K. and Kelsoe,J.R.
  CONSRTM   Bipolar Genome Study
  TITLE     Genome-wide association study of temperament in bipolar disorder
            reveals significant associations with three novel Loci
  JOURNAL   Biol Psychiatry 72 (4), 303-310 (2012)
   PUBMED   22365631
REFERENCE   8  (residues 1 to 69)
  AUTHORS   Chang,B., Mandal,M.N., Chavali,V.R., Hawes,N.L., Khan,N.W.,
            Hurd,R.E., Smith,R.S., Davisson,M.L., Kopplin,L., Klein,B.E.,
            Klein,R., Iyengar,S.K., Heckenlively,J.R. and Ayyagari,R.
  TITLE     Age-related retinal degeneration (arrd2) in a novel mouse model due
            to a nonsense mutation in the Mdm1 gene
  JOURNAL   Hum Mol Genet 17 (24), 3929-3941 (2008)
   PUBMED   18805803
  REMARK    GeneRIF: Not associated with age-related retinal degeneration.
REFERENCE   9  (residues 1 to 69)
  AUTHORS   Snyder,L.C., Trusko,S.P., Freeman,N., Eshleman,J.R.,
            Fakharzadeh,S.S. and George,D.L.
  TITLE     A gene amplified in a transformed mouse cell line undergoes complex
            transcriptional processing and encodes a nuclear protein
  JOURNAL   J Biol Chem 263 (32), 17150-17158 (1988)
   PUBMED   3182840
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM787113.1, DA958566.1,
            BC010622.1 and AC022511.22.
            
            Summary: This gene encodes a microtubule-binding nuclear protein
            that localizes to the centrioles of dividing cells and
            differentiating multiciliated cells and negatively regulates
            centriole duplication. The encoded protein is closely associated
            with the centriole barrel, and resides in the centriole lumen.
            Naturally-occurring mutations in the orthologous mouse gene are
            associated with age-related retinal degeneration. [provided by
            RefSeq, Feb 2019].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.73320.1, BC010622.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..69
                     /product="nuclear protein MDM1 isoform 3"
                     /note="nuclear protein double minute 1; nuclear protein
                     MDM1; Mdm4, transformed 3T3 cell double minute 1, p53
                     binding protein; Mdm1 nuclear protein"
                     /calculated_mol_wt=7795
     Region          9..>45
                     /region_name="MDM1"
                     /note="Nuclear protein MDM1; pfam15501"
                     /db_xref="CDD:464751"
     Region          9..15
                     /region_name="ST]-E-Y-X(3)-F motif 1, required for
                     efficient microtubule binding and stabilization.
                     /evidence=ECO:0000269|PubMed:26337392"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TC05.2)"
     CDS             1..69
                     /gene="SAXO6"
                     /gene_synonym="MDM1"
                     /coded_by="NM_001205029.3:118..327"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55842.1"
                     /db_xref="GeneID:56890"
                     /db_xref="HGNC:HGNC:29917"
                     /db_xref="MIM:613813"
ORIGIN      
        1 mpvrfkglse yqrnflwkks ylsescnssv grkypwaglr sdqlgnqgrc rtkiqhsdis
       61 sllilvcst
//
LOCUS       NP_001341902             444 aa            linear   PRI 28-NOV-2025
DEFINITION  nuclear protein MDM1 isoform 7 [Homo sapiens].
ACCESSION   NP_001341902 XP_016875138
VERSION     NP_001341902.1
DBSOURCE    REFSEQ: accession NM_001354973.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Hensley,M.R., Chua,R.F., Leung,Y.F., Yang,J.Y. and Zhang,G.
  TITLE     Molecular Evolution of MDM1, a 'Duplication-Resistant' Gene in
            Vertebrates
  JOURNAL   PLoS One 11 (9), e0163229 (2016)
   PUBMED   27658201
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Van de Mark,D., Kong,D., Loncarek,J. and Stearns,T.
  TITLE     MDM1 is a microtubule-binding protein that negatively regulates
            centriole duplication
  JOURNAL   Mol Biol Cell 26 (21), 3788-3802 (2015)
   PUBMED   26337392
  REMARK    GeneRIF: Authorse propose that MDM1 is a negative regulator of
            centriole duplication and that its function is mediated through
            microtubule binding.
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Stangeland,B., Mughal,A.A., Grieg,Z., Sandberg,C.J., Joel,M.,
            Nygard,S., Meling,T., Murrell,W., Vik Mo,E.O. and Langmoen,I.A.
  TITLE     Combined expressional analysis, bioinformatics and targeted
            proteomics identify new potential therapeutic targets in
            glioblastoma stem cells
  JOURNAL   Oncotarget 6 (28), 26192-26215 (2015)
   PUBMED   26295306
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Greenwood,T.A., Akiskal,H.S., Akiskal,K.K. and Kelsoe,J.R.
  CONSRTM   Bipolar Genome Study
  TITLE     Genome-wide association study of temperament in bipolar disorder
            reveals significant associations with three novel Loci
  JOURNAL   Biol Psychiatry 72 (4), 303-310 (2012)
   PUBMED   22365631
REFERENCE   8  (residues 1 to 444)
  AUTHORS   Chang,B., Mandal,M.N., Chavali,V.R., Hawes,N.L., Khan,N.W.,
            Hurd,R.E., Smith,R.S., Davisson,M.L., Kopplin,L., Klein,B.E.,
            Klein,R., Iyengar,S.K., Heckenlively,J.R. and Ayyagari,R.
  TITLE     Age-related retinal degeneration (arrd2) in a novel mouse model due
            to a nonsense mutation in the Mdm1 gene
  JOURNAL   Hum Mol Genet 17 (24), 3929-3941 (2008)
   PUBMED   18805803
  REMARK    GeneRIF: Not associated with age-related retinal degeneration.
REFERENCE   9  (residues 1 to 444)
  AUTHORS   Snyder,L.C., Trusko,S.P., Freeman,N., Eshleman,J.R.,
            Fakharzadeh,S.S. and George,D.L.
  TITLE     A gene amplified in a transformed mouse cell line undergoes complex
            transcriptional processing and encodes a nuclear protein
  JOURNAL   J Biol Chem 263 (32), 17150-17158 (1988)
   PUBMED   3182840
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022511.22 and AK026745.1.
            
            On Aug 31, 2017 this sequence version replaced XP_016875138.1.
            
            Summary: This gene encodes a microtubule-binding nuclear protein
            that localizes to the centrioles of dividing cells and
            differentiating multiciliated cells and negatively regulates
            centriole duplication. The encoded protein is closely associated
            with the centriole barrel, and resides in the centriole lumen.
            Naturally-occurring mutations in the orthologous mouse gene are
            associated with age-related retinal degeneration. [provided by
            RefSeq, Feb 2019].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.169655.1,
                                           SRR14038193.1325153.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..444
                     /product="nuclear protein MDM1 isoform 7"
                     /note="nuclear protein double minute 1; nuclear protein
                     MDM1; Mdm4, transformed 3T3 cell double minute 1, p53
                     binding protein; Mdm1 nuclear protein"
                     /calculated_mol_wt=49844
     Region          <1..278
                     /region_name="MDM1"
                     /note="Nuclear protein MDM1; pfam15501"
                     /db_xref="CDD:464751"
     CDS             1..444
                     /gene="SAXO6"
                     /gene_synonym="MDM1"
                     /coded_by="NM_001354973.2:899..2233"
                     /note="isoform 7 is encoded by transcript variant 9"
                     /db_xref="GeneID:56890"
                     /db_xref="HGNC:HGNC:29917"
                     /db_xref="MIM:613813"
ORIGIN      
        1 melkdlhqpk rkltpwkhqr lgkvnseyra kflspaqyly kagawthvkg nmpnqgslna
       61 mwyaevkelr ekaefyrkrv qgthfsrdhl nqilsdsncc wdvssttsse gtvssniral
      121 dlagdptshk tlqkcpstep eekgniveeq pqkntteklg vsaptipvrr rlawdtents
      181 edvqkqpgek eeeddneeeg drktgkqafm geqekldvre kskadkmkeg sdssvssekg
      241 grlptpklre lggiqrthhd lttpavggav lvspskmkpp apeqrkrmts qdcletsknd
      301 ftkkesravs lltspaagik tvdplplred sednihkfae atlpvskipk yptnppgqlp
      361 spphvpsywh psrriqgslr dpefqhnvgk armnnlqlpq heafndeded rlseisarsa
      421 asslrafqtl arakkrkenf wgkt
//
LOCUS       NP_001341900             444 aa            linear   PRI 28-NOV-2025
DEFINITION  nuclear protein MDM1 isoform 7 [Homo sapiens].
ACCESSION   NP_001341900 XP_016875136
VERSION     NP_001341900.1
DBSOURCE    REFSEQ: accession NM_001354971.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Hensley,M.R., Chua,R.F., Leung,Y.F., Yang,J.Y. and Zhang,G.
  TITLE     Molecular Evolution of MDM1, a 'Duplication-Resistant' Gene in
            Vertebrates
  JOURNAL   PLoS One 11 (9), e0163229 (2016)
   PUBMED   27658201
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Van de Mark,D., Kong,D., Loncarek,J. and Stearns,T.
  TITLE     MDM1 is a microtubule-binding protein that negatively regulates
            centriole duplication
  JOURNAL   Mol Biol Cell 26 (21), 3788-3802 (2015)
   PUBMED   26337392
  REMARK    GeneRIF: Authorse propose that MDM1 is a negative regulator of
            centriole duplication and that its function is mediated through
            microtubule binding.
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Stangeland,B., Mughal,A.A., Grieg,Z., Sandberg,C.J., Joel,M.,
            Nygard,S., Meling,T., Murrell,W., Vik Mo,E.O. and Langmoen,I.A.
  TITLE     Combined expressional analysis, bioinformatics and targeted
            proteomics identify new potential therapeutic targets in
            glioblastoma stem cells
  JOURNAL   Oncotarget 6 (28), 26192-26215 (2015)
   PUBMED   26295306
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Greenwood,T.A., Akiskal,H.S., Akiskal,K.K. and Kelsoe,J.R.
  CONSRTM   Bipolar Genome Study
  TITLE     Genome-wide association study of temperament in bipolar disorder
            reveals significant associations with three novel Loci
  JOURNAL   Biol Psychiatry 72 (4), 303-310 (2012)
   PUBMED   22365631
REFERENCE   8  (residues 1 to 444)
  AUTHORS   Chang,B., Mandal,M.N., Chavali,V.R., Hawes,N.L., Khan,N.W.,
            Hurd,R.E., Smith,R.S., Davisson,M.L., Kopplin,L., Klein,B.E.,
            Klein,R., Iyengar,S.K., Heckenlively,J.R. and Ayyagari,R.
  TITLE     Age-related retinal degeneration (arrd2) in a novel mouse model due
            to a nonsense mutation in the Mdm1 gene
  JOURNAL   Hum Mol Genet 17 (24), 3929-3941 (2008)
   PUBMED   18805803
  REMARK    GeneRIF: Not associated with age-related retinal degeneration.
REFERENCE   9  (residues 1 to 444)
  AUTHORS   Snyder,L.C., Trusko,S.P., Freeman,N., Eshleman,J.R.,
            Fakharzadeh,S.S. and George,D.L.
  TITLE     A gene amplified in a transformed mouse cell line undergoes complex
            transcriptional processing and encodes a nuclear protein
  JOURNAL   J Biol Chem 263 (32), 17150-17158 (1988)
   PUBMED   3182840
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022511.22 and AK026745.1.
            
            On Sep 2, 2017 this sequence version replaced XP_016875136.1.
            
            Summary: This gene encodes a microtubule-binding nuclear protein
            that localizes to the centrioles of dividing cells and
            differentiating multiciliated cells and negatively regulates
            centriole duplication. The encoded protein is closely associated
            with the centriole barrel, and resides in the centriole lumen.
            Naturally-occurring mutations in the orthologous mouse gene are
            associated with age-related retinal degeneration. [provided by
            RefSeq, Feb 2019].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.403598.1,
                                           SRR14038197.1404379.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..444
                     /product="nuclear protein MDM1 isoform 7"
                     /note="nuclear protein double minute 1; nuclear protein
                     MDM1; Mdm4, transformed 3T3 cell double minute 1, p53
                     binding protein; Mdm1 nuclear protein"
                     /calculated_mol_wt=49844
     Region          <1..278
                     /region_name="MDM1"
                     /note="Nuclear protein MDM1; pfam15501"
                     /db_xref="CDD:464751"
     CDS             1..444
                     /gene="SAXO6"
                     /gene_synonym="MDM1"
                     /coded_by="NM_001354971.2:1034..2368"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:56890"
                     /db_xref="HGNC:HGNC:29917"
                     /db_xref="MIM:613813"
ORIGIN      
        1 melkdlhqpk rkltpwkhqr lgkvnseyra kflspaqyly kagawthvkg nmpnqgslna
       61 mwyaevkelr ekaefyrkrv qgthfsrdhl nqilsdsncc wdvssttsse gtvssniral
      121 dlagdptshk tlqkcpstep eekgniveeq pqkntteklg vsaptipvrr rlawdtents
      181 edvqkqpgek eeeddneeeg drktgkqafm geqekldvre kskadkmkeg sdssvssekg
      241 grlptpklre lggiqrthhd lttpavggav lvspskmkpp apeqrkrmts qdcletsknd
      301 ftkkesravs lltspaagik tvdplplred sednihkfae atlpvskipk yptnppgqlp
      361 spphvpsywh psrriqgslr dpefqhnvgk armnnlqlpq heafndeded rlseisarsa
      421 asslrafqtl arakkrkenf wgkt
//
LOCUS       NP_116052                517 aa            linear   PRI 29-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 30 isoform 1 [Homo sapiens].
ACCESSION   NP_116052
VERSION     NP_116052.2
DBSOURCE    REFSEQ: accession NM_032663.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Kazi,N.H., Klink,N., Gallant,K., Kipka,G.M. and Gersch,M.
  TITLE     Chimeric deubiquitinase engineering reveals structural basis for
            specific inhibition of the mitophagy regulator USP30
  JOURNAL   Nat Struct Mol Biol 32 (9), 1776-1786 (2025)
   PUBMED   40325251
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Crunkhorn,S.
  TITLE     USP30 inhibition protects dopaminergic neurons
  JOURNAL   Nat Rev Drug Discov 23 (1), 22 (2024)
   PUBMED   38040789
  REMARK    GeneRIF: USP30 inhibition protects dopaminergic neurons.
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Zhou,W., Xu,S., Deng,T., Zhou,R. and Wang,C.
  TITLE     LncRNA USP30-AS1 promotes the survival of acute myeloid leukemia
            cells by cis-regulating USP30 and ANKRD13A
  JOURNAL   Hum Cell 35 (1), 360-378 (2022)
   PUBMED   34694569
  REMARK    GeneRIF: LncRNA USP30-AS1 promotes the survival of acute myeloid
            leukemia cells by cis-regulating USP30 and ANKRD13A.
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 517)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 517)
  AUTHORS   Cunningham,C.N., Baughman,J.M., Phu,L., Tea,J.S., Yu,C., Coons,M.,
            Kirkpatrick,D.S., Bingol,B. and Corn,J.E.
  TITLE     USP30 and parkin homeostatically regulate atypical ubiquitin chains
            on mitochondria
  JOURNAL   Nat Cell Biol 17 (2), 160-169 (2015)
   PUBMED   25621951
  REMARK    GeneRIF: The mechanism by which parkin, an E3 ubiquitin ligase, and
            USP30, a mitochondrion-localized deubiquitylase, regulate
            mitophagy, was investigated.
REFERENCE   7  (residues 1 to 517)
  AUTHORS   Bingol,B., Tea,J.S., Phu,L., Reichelt,M., Bakalarski,C.E., Song,Q.,
            Foreman,O., Kirkpatrick,D.S. and Sheng,M.
  TITLE     The mitochondrial deubiquitinase USP30 opposes parkin-mediated
            mitophagy
  JOURNAL   Nature 510 (7505), 370-375 (2014)
   PUBMED   24896179
  REMARK    GeneRIF: reducing USP30 activity enhances mitochondrial degradation
            in neurons
REFERENCE   8  (residues 1 to 517)
  AUTHORS   Nakamura,N. and Hirose,S.
  TITLE     Regulation of mitochondrial morphology by USP30, a deubiquitinating
            enzyme present in the mitochondrial outer membrane
  JOURNAL   Mol Biol Cell 19 (5), 1903-1911 (2008)
   PUBMED   18287522
  REMARK    GeneRIF: USP30 participates in the maintenance of mitochondrial
            morphology, a finding that provides new insight into the cellular
            function of deubiquitination.
REFERENCE   9  (residues 1 to 517)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   10 (residues 1 to 517)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY127211.1, BC004868.2, AC011596.27, AL834278.1 and BX095894.1.
            
            On Jan 11, 2008 this sequence version replaced NP_116052.1.
            
            Summary: USP30, a member of the ubiquitin-specific protease family
            (see USP1, MIM 603478), is a novel mitochondrial deubiquitinating
            (DUB) enzyme (Nakamura and Hirose, 2008 [PubMed
            18287522]).[supplied by OMIM, Dec 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.162478.1,
                                           SRR1803612.26615.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000257548.10/ ENSP00000257548.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..517
                     /product="ubiquitin carboxyl-terminal hydrolase 30 isoform
                     1"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin carboxyl-terminal hydrolase 30;
                     ub-specific protease 30; ubiquitin thioesterase 30;
                     deubiquitinating enzyme 30; ubiquitin-specific protease
                     30; ubiquitin-specific-processing protease 30; ubiquitin
                     thiolesterase 30"
                     /calculated_mol_wt=58372
     Site            36..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70CQ3.1)"
     Region          69..500
                     /region_name="Peptidase_C19F"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02662"
                     /db_xref="CDD:239127"
     Region          <69..>265
                     /region_name="UBP12"
                     /note="Ubiquitin C-terminal hydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG5560"
                     /db_xref="CDD:227847"
     Site            order(72,77,452,478)
                     /site_type="active"
                     /db_xref="CDD:239127"
     Region          364..395
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q70CQ3.1)"
     CDS             1..517
                     /gene="USP30"
                     /coded_by="NM_032663.5:104..1657"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9123.2"
                     /db_xref="GeneID:84749"
                     /db_xref="HGNC:HGNC:20065"
                     /db_xref="MIM:612492"
ORIGIN      
        1 mlssraeaam taadraiqrf lrtgaavryk vmknwgvigg iaaalaagiy viwgpiterk
       61 krrkglvpgl vnlgntcfmn sllqglsacp afirwleeft sqysrdqkep pshqylsltl
      121 lhllkalscq evtddevlda sclldvlrmy rwqissfeeq dahelfhvit sslederdrq
      181 prvthlfdvh sleqqseitp kqitcrtrgs phptsnhwks qhpfhgrlts nmvckhcehq
      241 spvrfdtfds lslsipaatw ghpltldhcl hhfissesvr dvvcdnctki eakgtlngek
      301 vehqrttfvk qlklgklpqc lcihlqrlsw sshgtplkrh ehvqfneflm mdiykyhllg
      361 hkpsqhnpkl nknpgptlel qdgpgaptpv lnqpgapktq ifmngacsps llptlsapmp
      421 fplpvvpdys sstylfrlma vvvhhgdmhs ghfvtyrrsp psarnplsts nqwlwvsddt
      481 vrkaslqevl sssayllfye rvlsrmqhqs qecksee
//
LOCUS       NP_001317171             685 aa            linear   PRI 29-NOV-2025
DEFINITION  acyl-CoA synthetase short-chain family member 3, mitochondrial
            isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001317171 XP_005269207
VERSION     NP_001317171.1
DBSOURCE    REFSEQ: accession NM_001330242.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Huo,P., Wang,S., Li,Z. and Jin,Z.
  TITLE     ACSS3 protein macromolecule regulates glycolysis in keloid through
            Wnt/beta-catenin signaling pathway: Bioinformatics, machine
            learning, and experimental validation
  JOURNAL   Cell Signal 135, 112056 (2025)
   PUBMED   40783148
REFERENCE   2  (residues 1 to 685)
  AUTHORS   Wang,L., Yuan,H., Li,W., Yan,P., Zhao,M., Li,Z., Zhao,H., Wang,S.,
            Wan,R., Li,Y., Yang,J., Pan,X., Rosas,I. and Yu,G.
  TITLE     ACSS3 regulates the metabolic homeostasis of epithelial cells and
            alleviates pulmonary fibrosis
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (2), 166960 (2024)
   PUBMED   37979225
  REMARK    GeneRIF: ACSS3 regulates the metabolic homeostasis of epithelial
            cells and alleviates pulmonary fibrosis.
REFERENCE   3  (residues 1 to 685)
  AUTHORS   Jo,J., Song,Y., Yoon,D., Lee,C.G. and Won,S.
  TITLE     Genome-wide assessment reveals a significant association between
            ACSS3 and physical activity
  JOURNAL   Genes Brain Behav 22 (1), e12834 (2023)
   PUBMED   36510703
  REMARK    GeneRIF: Genome-wide assessment reveals a significant association
            between ACSS3 and physical activity.
REFERENCE   4  (residues 1 to 685)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 685)
  AUTHORS   Zhou,L., Song,Z., Hu,J., Liu,L., Hou,Y., Zhang,X., Yang,X. and
            Chen,K.
  TITLE     ACSS3 represses prostate cancer progression through downregulating
            lipid droplet-associated protein PLIN3
  JOURNAL   Theranostics 11 (2), 841-860 (2021)
   PUBMED   33391508
  REMARK    GeneRIF: ACSS3 represses prostate cancer progression through
            downregulating lipid droplet-associated protein PLIN3.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 685)
  AUTHORS   Yoshimura,Y., Araki,A., Maruta,H., Takahashi,Y. and Yamashita,H.
  TITLE     Molecular cloning of rat acss3 and characterization of mammalian
            propionyl-CoA synthetase in the liver mitochondrial matrix
  JOURNAL   J Biochem 161 (3), 279-289 (2017)
   PUBMED   28003429
REFERENCE   7  (residues 1 to 685)
  AUTHORS   Chouraki,V., De Bruijn,R.F., Chapuis,J., Bis,J.C., Reitz,C.,
            Schraen,S., Ibrahim-Verbaas,C.A., Grenier-Boley,B., Delay,C.,
            Rogers,R., Demiautte,F., Mounier,A., Fitzpatrick,A.L., Berr,C.,
            Dartigues,J.F., Uitterlinden,A.G., Hofman,A., Breteler,M.,
            Becker,J.T., Lathrop,M., Schupf,N., Alperovitch,A., Mayeux,R., van
            Duijn,C.M., Buee,L., Amouyel,P., Lopez,O.L., Ikram,M.A., Tzourio,C.
            and Lambert,J.C.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative
  TITLE     A genome-wide association meta-analysis of plasma Abeta peptides
            concentrations in the elderly
  JOURNAL   Mol Psychiatry 19 (12), 1326-1335 (2014)
   PUBMED   24535457
REFERENCE   8  (residues 1 to 685)
  AUTHORS   Ritchie,M.D., Verma,S.S., Hall,M.A., Goodloe,R.J., Berg,R.L.,
            Carrell,D.S., Carlson,C.S., Chen,L., Crosslin,D.R., Denny,J.C.,
            Jarvik,G., Li,R., Linneman,J.G., Pathak,J., Peissig,P.,
            Rasmussen,L.V., Ramirez,A.H., Wang,X., Wilke,R.A., Wolf,W.A.,
            Torstenson,E.S., Turner,S.D. and McCarty,C.A.
  TITLE     Electronic medical records and genomics (eMERGE) network
            exploration in cataract: several new potential susceptibility loci
  JOURNAL   Mol Vis 20, 1281-1295 (2014)
   PUBMED   25352737
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 685)
  AUTHORS   Hunter,A.M., Leuchter,A.F., Power,R.A., Muthen,B., McGrath,P.J.,
            Lewis,C.M., Cook,I.A., Garriock,H.A., McGuffin,P., Uher,R. and
            Hamilton,S.P.
  TITLE     A genome-wide association study of a sustained pattern of
            antidepressant response
  JOURNAL   J Psychiatr Res 47 (9), 1157-1165 (2013)
   PUBMED   23726668
REFERENCE   10 (residues 1 to 685)
  AUTHORS   Watkins,P.A., Maiguel,D., Jia,Z. and Pevsner,J.
  TITLE     Evidence for 26 distinct acyl-coenzyme A synthetase genes in the
            human genome
  JOURNAL   J Lipid Res 48 (12), 2736-2750 (2007)
   PUBMED   17762044
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA756631.1, AK025616.1, AK074267.1, AK074938.1, AC078920.17 and
            AI022900.1.
            
            On Aug 20, 2016 this sequence version replaced XP_005269207.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 5' coding region, compared to variant 1. The
            encoded isoform (2) is one amino acid shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.168534.1,
                                           SRR1660805.113776.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.31"
     Protein         1..685
                     /product="acyl-CoA synthetase short-chain family member 3,
                     mitochondrial isoform 2 precursor"
                     /EC_number="6.2.1.1"
                     /EC_number="6.2.1.17"
                     /note="acyl-CoA synthetase short-chain family member 3,
                     mitochondrial; AMP-binding enzyme, 33217; acetate--CoA
                     ligase 3; propionate--CoA ligase"
                     /calculated_mol_wt=71714
     transit_peptide 1..29
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9H6R3.1)"
                     /calculated_mol_wt=2896
     Region          62..678
                     /region_name="PrpE"
                     /note="Propionyl-CoA synthetase (PrpE); cd05967"
                     /db_xref="CDD:341271"
     Site            order(295,298..303,305..306)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341271"
     Site            order(298,423..424,445..450,538,550,553,564,648)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341271"
     Site            order(298,339..340,392,394..395,398,423..424,445..450,538,
                     550,553,561..564,629)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341271"
     Site            order(339,394..395,398,423,561..563,623,629)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341271"
     Site            523
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q14DH7; propagated from
                     UniProtKB/Swiss-Prot (Q9H6R3.1)"
     CDS             1..685
                     /gene="ACSS3"
                     /coded_by="NM_001330242.2:43..2100"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS81716.1"
                     /db_xref="GeneID:79611"
                     /db_xref="HGNC:HGNC:24723"
                     /db_xref="MIM:614356"
ORIGIN      
        1 mkpswlqcrk vtsagglggp lpgssparga gaalralvvp gprgglggrg cralssgsgs
       61 eykthfaasv tdperfwgka aeqiswykpw tktlenkhsp strfvegmln icynavdrhi
      121 engkgdkiai iydspvtntk atftykevle qvsklagvlv khgikkgdtv viympmipqa
      181 mytmlacari gaihslifgg faskelssri dhvkpkvvvt asfgiepgrr veyvplveea
      241 lkigqhkpdk iliynrpnme avplapgrdl dwdeemakaq shdcvpvlse hplyilytsg
      301 ttglpkgvir ptggyavmlh wsmssiyglq pgevwwaasd lgwvvghsyi cygpllhgnt
      361 tvlyegkpvg tpdagayfrv laehgvaalf taptairair qqdpgaalgk qysltrfktl
      421 fvagercdve tlewsknvfr vpvldhwwqt etgspitasc vglgnsktpp pgqagksvpg
      481 ynvmilddnm qklkarclgn ivvklplppg afsglwknqe afkhlyfekf pgyydtmdag
      541 ymdeegylyv msrvddvinv aghrisagai eesilshgtv adcavvgked plkghvplal
      601 cvlrkdinat eeqvleeivk hvrqnigpva afrnavfvkq lpktrsgkip rsalsaivng
      661 kpykitstie dpsifghvee mlkqa
//
LOCUS       NP_001357256            1683 aa            linear   PRI 29-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase SHPRH isoform a [Homo sapiens].
ACCESSION   NP_001357256 XP_006715504
VERSION     NP_001357256.1
DBSOURCE    REFSEQ: accession NM_001370327.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1683)
  AUTHORS   Nagelberg,A.L., Sihota,T.S., Chuang,Y.C., Shi,R., Chow,J.L.M.,
            English,J., MacAulay,C., Lam,S., Lam,W.L. and Lockwood,W.W.
  TITLE     Integrative genomics identifies SHPRH as a tumor suppressor gene in
            lung adenocarcinoma that regulates DNA damage response
  JOURNAL   Br J Cancer 131 (3), 534-550 (2024)
   PUBMED   38890444
  REMARK    GeneRIF: Integrative genomics identifies SHPRH as a tumor
            suppressor gene in lung adenocarcinoma that regulates DNA damage
            response.
REFERENCE   2  (residues 1 to 1683)
  AUTHORS   Gao,J., Pan,H., Li,J., Jiang,J. and Wang,W.
  TITLE     A peptide encoded by the circular form of the SHPRH gene induces
            apoptosis in neuroblastoma cells
  JOURNAL   PeerJ 12, e16806 (2024)
   PUBMED   38282862
  REMARK    GeneRIF: A peptide encoded by the circular form of the SHPRH gene
            induces apoptosis in neuroblastoma cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1683)
  AUTHORS   Miller,A.K., Mao,G., Knicely,B.G., Daniels,H.G., Rahal,C.,
            Putnam,C.D., Kolodner,R.D. and Goellner,E.M.
  TITLE     Rad5 and Its Human Homologs, HLTF and SHPRH, Are Novel Interactors
            of Mismatch Repair
  JOURNAL   Front Cell Dev Biol 10, 843121 (2022)
   PUBMED   35784486
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1683)
  AUTHORS   Chen,W., Zhong,M., Yu,J., Xie,R., Zhou,T., Zhang,S., Xiong,C. and
            Huang,D.
  TITLE     KMT2B promotes SHPRH expression to regulate 131I sensitivity in
            thyroid carcinoma cells by affecting FYN protein stability
  JOURNAL   Cell Signal 88, 110165 (2021)
   PUBMED   34606908
  REMARK    GeneRIF: KMT2B promotes SHPRH expression to regulate (131)I
            sensitivity in thyroid carcinoma cells by affecting FYN protein
            stability.
REFERENCE   5  (residues 1 to 1683)
  AUTHORS   Seelinger,M., Sogaard,C.K. and Otterlei,M.
  TITLE     The Human RAD5 Homologs, HLTF and SHPRH, Have Separate Functions in
            DNA Damage Tolerance Dependent on The DNA Lesion Type
  JOURNAL   Biomolecules 10 (3), 463 (2020)
   PUBMED   32192191
  REMARK    GeneRIF: The Human RAD5 Homologs, HLTF and SHPRH, Have Separate
            Functions in DNA Damage Tolerance Dependent on The DNA Lesion Type.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1683)
  AUTHORS   Lin,J.R., Zeman,M.K., Chen,J.Y., Yee,M.C. and Cimprich,K.A.
  TITLE     SHPRH and HLTF act in a damage-specific manner to coordinate
            different forms of postreplication repair and prevent mutagenesis
  JOURNAL   Mol Cell 42 (2), 237-249 (2011)
   PUBMED   21396873
  REMARK    GeneRIF: HLTF and SHPRH suppress mutagenesis in a damage-specific
            manner, preventing mutations induced by UV rays and methyl
            methanesulfonate.
REFERENCE   7  (residues 1 to 1683)
  AUTHORS   Motegi,A., Liaw,H.J., Lee,K.Y., Roest,H.P., Maas,A., Wu,X.,
            Moinova,H., Markowitz,S.D., Ding,H., Hoeijmakers,J.H. and Myung,K.
  TITLE     Polyubiquitination of proliferating cell nuclear antigen by HLTF
            and SHPRH prevents genomic instability from stalled replication
            forks
  JOURNAL   Proc Natl Acad Sci U S A 105 (34), 12411-12416 (2008)
   PUBMED   18719106
  REMARK    GeneRIF: HLTF and SHPRH are functional homologues of yeast Rad5
            that cooperatively mediate PCNA polyubiquitination and maintain
            genomic stability.
REFERENCE   8  (residues 1 to 1683)
  AUTHORS   Motegi,A., Sood,R., Moinova,H., Markowitz,S.D., Liu,P.P. and
            Myung,K.
  TITLE     Human SHPRH suppresses genomic instability through proliferating
            cell nuclear antigen polyubiquitination
  JOURNAL   J Cell Biol 175 (5), 703-708 (2006)
   PUBMED   17130289
  REMARK    GeneRIF: We report that a putative tumor suppressor gene, SHPRH, is
            a human orthologue of yeast RAD5.The yRad5/SHPRH-dependent pathway
            is a conserved and fundamental DNA repair mechanism that protects
            the genome from genotoxic stress.
REFERENCE   9  (residues 1 to 1683)
  AUTHORS   Unk,I., Hajdu,I., Fatyol,K., Szakal,B., Blastyak,A., Bermudez,V.,
            Hurwitz,J., Prakash,L., Prakash,S. and Haracska,L.
  TITLE     Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent
            polyubiquitylation of proliferating cell nuclear antigen
  JOURNAL   Proc Natl Acad Sci U S A 103 (48), 18107-18112 (2006)
   PUBMED   17108083
  REMARK    GeneRIF: SHPRH function is an important deterrent to mutagenesis
            and carcinogenesis in humans
REFERENCE   10 (residues 1 to 1683)
  AUTHORS   Sood,R., Makalowska,I., Galdzicki,M., Hu,P., Eddings,E.,
            Robbins,C.M., Moses,T., Namkoong,J., Chen,S. and Trent,J.M.
  TITLE     Cloning and characterization of a novel gene, SHPRH, encoding a
            conserved putative protein with SNF2/helicase and PHD-finger
            domains from the 6q24 region
  JOURNAL   Genomics 82 (2), 153-161 (2003)
   PUBMED   12837266
  REMARK    GeneRIF: SHPRH maps to 6q24 and is a possible candidate for the
            tumor suppressor gene reported from that region.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL451145.15 and AL356599.19.
            
            On May 7, 2019 this sequence version replaced XP_006715504.1.
            
            Summary: SHPRH is a ubiquitously expressed protein that contains
            motifs characteristics of several DNA repair proteins,
            transcription factors, and helicases. SHPRH is a functional homolog
            of S. cerevisiae RAD5 (Unk et al., 2006 [PubMed
            17108083]).[supplied by OMIM, Mar 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1871625.1,
                                           SRR7346977.2765796.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1683
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.3"
     Protein         1..1683
                     /product="E3 ubiquitin-protein ligase SHPRH isoform a"
                     /EC_number="2.3.2.27"
                     /note="2610103K11Rik; E3 ubiquitin-protein ligase SHPRH;
                     SNF2, histone-linker, PHD and RING finger
                     domain-containing helicase; SNF2 histone linker PHD RING
                     helicase, E3 ubiquitin protein ligase; RING-type E3
                     ubiquitin transferase SHPRH"
                     /calculated_mol_wt=192949
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q149N8.2)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q149N8.2)"
     Region          <298..>388
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
     Region          304..>409
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Site            375..381
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350670"
     Region          440..508
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          525..607
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q149N8.2)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TPQ3; propagated from
                     UniProtKB/Swiss-Prot (Q149N8.2)"
     Region          660..706
                     /region_name="PHD_SHPRH"
                     /note="PHD finger found in E3 ubiquitin-protein ligase
                     SHPRH; cd15547"
                     /db_xref="CDD:277022"
     Site            order(660,673..677,681,701)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277022"
     Region          <702..903
                     /region_name="DEXQc_SHPRH"
                     /note="DEXQ-box helicase domain of SHPRH; cd18070"
                     /db_xref="CDD:350828"
     Region          819..822
                     /region_name="DEAQ box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q149N8.2)"
     Region          1429..1482
                     /region_name="RING-HC_SHPRH-like"
                     /note="RING finger, HC subclass, found in SNF2
                     histone-linker PHD finger RING finger helicase (SHPRH) and
                     similar proteins; cd16569"
                     /db_xref="CDD:438231"
     Region          1508..1633
                     /region_name="SF2_C_SNF"
                     /note="C-terminal helicase domain of the SNF family
                     helicases; cd18793"
                     /db_xref="CDD:350180"
     Site            order(1537..1538,1546,1585,1606..1607)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350180"
     Site            order(1591..1592,1594,1617,1620)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350180"
     CDS             1..1683
                     /gene="SHPRH"
                     /gene_synonym="bA545I5.2; RAD5"
                     /coded_by="NM_001370327.1:235..5286"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS43513.2"
                     /db_xref="GeneID:257218"
                     /db_xref="HGNC:HGNC:19336"
                     /db_xref="MIM:608048"
ORIGIN      
        1 mssrrkrapp vrvdeekrqq lhwnmhedrr nepiiisddd eqpcpgsdts sahyiilsds
       61 lkeevahrdk krcskvvsfs kpiekeetvg ifsplsvkln ivispyhfdn swkaflgelt
      121 lqllpaqsli enfsersitl mssessnqfl iyvhskgedv ekqkkepmsi cdkgilvess
      181 fsgemledlg wlqkkrrikl yqkpegnhii kvgiylleag lakldflsda nsrmkkfnql
      241 mkkvmeklhn siipdvleed eddpesepeg qdidelyhfv kqthqqetqs iqvdvqhpal
      301 ipvlrpyqre avnwmlqqec frsspatesa lhflwreivt seglklyynp ytgciireyp
      361 nsgpqllggi lademglgkt vevlalilth trqdvkqdal tlpegkvvny fipshyfggk
      421 lkkteiqnie fepkekvqcp ptrvmiltav kemngkkgvs ilsiykyvss iyrydvqrnr
      481 sllkrmlkcl ifeglvkqik ghgfsgtftl gknykeedic dktkkqavgs prkiqketrk
      541 sgnkdtdsey lpsdtsdddd dpyyyyyksr rnrsklrkkl vpstkkgksq pfinpdsqgh
      601 cpatsdsgit dvamskstci sefnqehete dcaeslnhad sdvppsntms pfntsdyrfe
      661 cicgeldqid rkprvqclkc hlwqhakcvn ydeknlkikp fycphclvam epvstratli
      721 ispssichqw vdeinrhvrs sslrvlvyqg vkkdgflqph flaeqdivii tydvlrseln
      781 yvdiphsnse dgrrlrnqkr ymaipsplva vewwriclde aqmvecptvk aaemaqrlsg
      841 inrwcisgtp vqrgledlfg lvvflgiepy cvkhwwvrll yrpyckknpq hlysfiakil
      901 wrsakkdvid qiqippqtee ihwlhfspve rhfyhrqhev ccqdvvvklr kisdwalkls
      961 sldrrtvtsi lypllrlrqa cchpqavrge flplqkstmt meelltslqk kcgteceeah
     1021 rqlvcalngl agihiikgey alaaelyrev lrsseehkgk lktdslqrlh athnlmelli
     1081 arhpgipptl rdgrleeeak qlrehymskc ntevaeaqqa lypvqqtihe lqrkihsnsp
     1141 wwlnvihrai eftideelvq rvrneitsny kqqtgklsms ekfrdcrglq fllttqmeel
     1201 nkcqklvrea vknlegppsr nviesatvch lrparlplnc cvfckadelf teyesklfsn
     1261 tvkgqtaife emiedeeglv ddraptttrg lwaiseters mkailsfaks hrfdvefvde
     1321 gstsmdlfea wkkeykllhe ywmalrnrvs avdelamate rlrvrdprep kpnppvlhii
     1381 epheveqnri kllndkavat sqlqkklgql lyltnleksq dktsggvnpe pcpicarqlg
     1441 kqwavltcgh cfcnecisii ieqysvgshr ssikcaicrq ttshkeisyv ftsekanqee
     1501 dipvkgshst kveavvrtlm kiqlrdpgak alvfstwqdv ldiiskaltd nnmefaqisr
     1561 vktfqenlsa fkrdpqinil llplhtgsng ltiieathvl lvepilnpah elqaigrvhr
     1621 igqtkptivh rflikatiee rmqamlktae rshtnssakh seasvltvad ladlftkete
     1681 ele
//
LOCUS       NP_001036148            1683 aa            linear   PRI 29-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase SHPRH isoform a [Homo sapiens].
ACCESSION   NP_001036148
VERSION     NP_001036148.2
DBSOURCE    REFSEQ: accession NM_001042683.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1683)
  AUTHORS   Nagelberg,A.L., Sihota,T.S., Chuang,Y.C., Shi,R., Chow,J.L.M.,
            English,J., MacAulay,C., Lam,S., Lam,W.L. and Lockwood,W.W.
  TITLE     Integrative genomics identifies SHPRH as a tumor suppressor gene in
            lung adenocarcinoma that regulates DNA damage response
  JOURNAL   Br J Cancer 131 (3), 534-550 (2024)
   PUBMED   38890444
  REMARK    GeneRIF: Integrative genomics identifies SHPRH as a tumor
            suppressor gene in lung adenocarcinoma that regulates DNA damage
            response.
REFERENCE   2  (residues 1 to 1683)
  AUTHORS   Gao,J., Pan,H., Li,J., Jiang,J. and Wang,W.
  TITLE     A peptide encoded by the circular form of the SHPRH gene induces
            apoptosis in neuroblastoma cells
  JOURNAL   PeerJ 12, e16806 (2024)
   PUBMED   38282862
  REMARK    GeneRIF: A peptide encoded by the circular form of the SHPRH gene
            induces apoptosis in neuroblastoma cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1683)
  AUTHORS   Miller,A.K., Mao,G., Knicely,B.G., Daniels,H.G., Rahal,C.,
            Putnam,C.D., Kolodner,R.D. and Goellner,E.M.
  TITLE     Rad5 and Its Human Homologs, HLTF and SHPRH, Are Novel Interactors
            of Mismatch Repair
  JOURNAL   Front Cell Dev Biol 10, 843121 (2022)
   PUBMED   35784486
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1683)
  AUTHORS   Chen,W., Zhong,M., Yu,J., Xie,R., Zhou,T., Zhang,S., Xiong,C. and
            Huang,D.
  TITLE     KMT2B promotes SHPRH expression to regulate 131I sensitivity in
            thyroid carcinoma cells by affecting FYN protein stability
  JOURNAL   Cell Signal 88, 110165 (2021)
   PUBMED   34606908
  REMARK    GeneRIF: KMT2B promotes SHPRH expression to regulate (131)I
            sensitivity in thyroid carcinoma cells by affecting FYN protein
            stability.
REFERENCE   5  (residues 1 to 1683)
  AUTHORS   Seelinger,M., Sogaard,C.K. and Otterlei,M.
  TITLE     The Human RAD5 Homologs, HLTF and SHPRH, Have Separate Functions in
            DNA Damage Tolerance Dependent on The DNA Lesion Type
  JOURNAL   Biomolecules 10 (3), 463 (2020)
   PUBMED   32192191
  REMARK    GeneRIF: The Human RAD5 Homologs, HLTF and SHPRH, Have Separate
            Functions in DNA Damage Tolerance Dependent on The DNA Lesion Type.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1683)
  AUTHORS   Lin,J.R., Zeman,M.K., Chen,J.Y., Yee,M.C. and Cimprich,K.A.
  TITLE     SHPRH and HLTF act in a damage-specific manner to coordinate
            different forms of postreplication repair and prevent mutagenesis
  JOURNAL   Mol Cell 42 (2), 237-249 (2011)
   PUBMED   21396873
  REMARK    GeneRIF: HLTF and SHPRH suppress mutagenesis in a damage-specific
            manner, preventing mutations induced by UV rays and methyl
            methanesulfonate.
REFERENCE   7  (residues 1 to 1683)
  AUTHORS   Motegi,A., Liaw,H.J., Lee,K.Y., Roest,H.P., Maas,A., Wu,X.,
            Moinova,H., Markowitz,S.D., Ding,H., Hoeijmakers,J.H. and Myung,K.
  TITLE     Polyubiquitination of proliferating cell nuclear antigen by HLTF
            and SHPRH prevents genomic instability from stalled replication
            forks
  JOURNAL   Proc Natl Acad Sci U S A 105 (34), 12411-12416 (2008)
   PUBMED   18719106
  REMARK    GeneRIF: HLTF and SHPRH are functional homologues of yeast Rad5
            that cooperatively mediate PCNA polyubiquitination and maintain
            genomic stability.
REFERENCE   8  (residues 1 to 1683)
  AUTHORS   Motegi,A., Sood,R., Moinova,H., Markowitz,S.D., Liu,P.P. and
            Myung,K.
  TITLE     Human SHPRH suppresses genomic instability through proliferating
            cell nuclear antigen polyubiquitination
  JOURNAL   J Cell Biol 175 (5), 703-708 (2006)
   PUBMED   17130289
  REMARK    GeneRIF: We report that a putative tumor suppressor gene, SHPRH, is
            a human orthologue of yeast RAD5.The yRad5/SHPRH-dependent pathway
            is a conserved and fundamental DNA repair mechanism that protects
            the genome from genotoxic stress.
REFERENCE   9  (residues 1 to 1683)
  AUTHORS   Unk,I., Hajdu,I., Fatyol,K., Szakal,B., Blastyak,A., Bermudez,V.,
            Hurwitz,J., Prakash,L., Prakash,S. and Haracska,L.
  TITLE     Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent
            polyubiquitylation of proliferating cell nuclear antigen
  JOURNAL   Proc Natl Acad Sci U S A 103 (48), 18107-18112 (2006)
   PUBMED   17108083
  REMARK    GeneRIF: SHPRH function is an important deterrent to mutagenesis
            and carcinogenesis in humans
REFERENCE   10 (residues 1 to 1683)
  AUTHORS   Sood,R., Makalowska,I., Galdzicki,M., Hu,P., Eddings,E.,
            Robbins,C.M., Moses,T., Namkoong,J., Chen,S. and Trent,J.M.
  TITLE     Cloning and characterization of a novel gene, SHPRH, encoding a
            conserved putative protein with SNF2/helicase and PHD-finger
            domains from the 6q24 region
  JOURNAL   Genomics 82 (2), 153-161 (2003)
   PUBMED   12837266
  REMARK    GeneRIF: SHPRH maps to 6q24 and is a possible candidate for the
            tumor suppressor gene reported from that region.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL451145.15, AY163808.1, AY161136.1, BC117686.1, AK126959.1,
            AA315737.1 and BX648322.1.
            
            On Feb 24, 2010 this sequence version replaced NP_001036148.1.
            
            Summary: SHPRH is a ubiquitously expressed protein that contains
            motifs characteristics of several DNA repair proteins,
            transcription factors, and helicases. SHPRH is a functional homolog
            of S. cerevisiae RAD5 (Unk et al., 2006 [PubMed
            17108083]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC117686.1, AY161136.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000275233.12/ ENSP00000275233.7
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1683
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.3"
     Protein         1..1683
                     /product="E3 ubiquitin-protein ligase SHPRH isoform a"
                     /EC_number="2.3.2.27"
                     /note="2610103K11Rik; E3 ubiquitin-protein ligase SHPRH;
                     SNF2, histone-linker, PHD and RING finger
                     domain-containing helicase; SNF2 histone linker PHD RING
                     helicase, E3 ubiquitin protein ligase; RING-type E3
                     ubiquitin transferase SHPRH"
                     /calculated_mol_wt=192949
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q149N8.2)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q149N8.2)"
     Region          <298..>388
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
     Region          304..>409
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Site            375..381
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350670"
     Region          440..508
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          525..607
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q149N8.2)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TPQ3; propagated from
                     UniProtKB/Swiss-Prot (Q149N8.2)"
     Region          660..706
                     /region_name="PHD_SHPRH"
                     /note="PHD finger found in E3 ubiquitin-protein ligase
                     SHPRH; cd15547"
                     /db_xref="CDD:277022"
     Site            order(660,673..677,681,701)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277022"
     Region          <702..903
                     /region_name="DEXQc_SHPRH"
                     /note="DEXQ-box helicase domain of SHPRH; cd18070"
                     /db_xref="CDD:350828"
     Region          819..822
                     /region_name="DEAQ box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q149N8.2)"
     Region          1429..1482
                     /region_name="RING-HC_SHPRH-like"
                     /note="RING finger, HC subclass, found in SNF2
                     histone-linker PHD finger RING finger helicase (SHPRH) and
                     similar proteins; cd16569"
                     /db_xref="CDD:438231"
     Region          1508..1633
                     /region_name="SF2_C_SNF"
                     /note="C-terminal helicase domain of the SNF family
                     helicases; cd18793"
                     /db_xref="CDD:350180"
     Site            order(1537..1538,1546,1585,1606..1607)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350180"
     Site            order(1591..1592,1594,1617,1620)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350180"
     CDS             1..1683
                     /gene="SHPRH"
                     /gene_synonym="bA545I5.2; RAD5"
                     /coded_by="NM_001042683.3:661..5712"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43513.2"
                     /db_xref="GeneID:257218"
                     /db_xref="HGNC:HGNC:19336"
                     /db_xref="MIM:608048"
ORIGIN      
        1 mssrrkrapp vrvdeekrqq lhwnmhedrr nepiiisddd eqpcpgsdts sahyiilsds
       61 lkeevahrdk krcskvvsfs kpiekeetvg ifsplsvkln ivispyhfdn swkaflgelt
      121 lqllpaqsli enfsersitl mssessnqfl iyvhskgedv ekqkkepmsi cdkgilvess
      181 fsgemledlg wlqkkrrikl yqkpegnhii kvgiylleag lakldflsda nsrmkkfnql
      241 mkkvmeklhn siipdvleed eddpesepeg qdidelyhfv kqthqqetqs iqvdvqhpal
      301 ipvlrpyqre avnwmlqqec frsspatesa lhflwreivt seglklyynp ytgciireyp
      361 nsgpqllggi lademglgkt vevlalilth trqdvkqdal tlpegkvvny fipshyfggk
      421 lkkteiqnie fepkekvqcp ptrvmiltav kemngkkgvs ilsiykyvss iyrydvqrnr
      481 sllkrmlkcl ifeglvkqik ghgfsgtftl gknykeedic dktkkqavgs prkiqketrk
      541 sgnkdtdsey lpsdtsdddd dpyyyyyksr rnrsklrkkl vpstkkgksq pfinpdsqgh
      601 cpatsdsgit dvamskstci sefnqehete dcaeslnhad sdvppsntms pfntsdyrfe
      661 cicgeldqid rkprvqclkc hlwqhakcvn ydeknlkikp fycphclvam epvstratli
      721 ispssichqw vdeinrhvrs sslrvlvyqg vkkdgflqph flaeqdivii tydvlrseln
      781 yvdiphsnse dgrrlrnqkr ymaipsplva vewwriclde aqmvecptvk aaemaqrlsg
      841 inrwcisgtp vqrgledlfg lvvflgiepy cvkhwwvrll yrpyckknpq hlysfiakil
      901 wrsakkdvid qiqippqtee ihwlhfspve rhfyhrqhev ccqdvvvklr kisdwalkls
      961 sldrrtvtsi lypllrlrqa cchpqavrge flplqkstmt meelltslqk kcgteceeah
     1021 rqlvcalngl agihiikgey alaaelyrev lrsseehkgk lktdslqrlh athnlmelli
     1081 arhpgipptl rdgrleeeak qlrehymskc ntevaeaqqa lypvqqtihe lqrkihsnsp
     1141 wwlnvihrai eftideelvq rvrneitsny kqqtgklsms ekfrdcrglq fllttqmeel
     1201 nkcqklvrea vknlegppsr nviesatvch lrparlplnc cvfckadelf teyesklfsn
     1261 tvkgqtaife emiedeeglv ddraptttrg lwaiseters mkailsfaks hrfdvefvde
     1321 gstsmdlfea wkkeykllhe ywmalrnrvs avdelamate rlrvrdprep kpnppvlhii
     1381 epheveqnri kllndkavat sqlqkklgql lyltnleksq dktsggvnpe pcpicarqlg
     1441 kqwavltcgh cfcnecisii ieqysvgshr ssikcaicrq ttshkeisyv ftsekanqee
     1501 dipvkgshst kveavvrtlm kiqlrdpgak alvfstwqdv ldiiskaltd nnmefaqisr
     1561 vktfqenlsa fkrdpqinil llplhtgsng ltiieathvl lvepilnpah elqaigrvhr
     1621 igqtkptivh rflikatiee rmqamlktae rshtnssakh seasvltvad ladlftkete
     1681 ele
//
LOCUS       NP_001357257            1202 aa            linear   PRI 29-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase SHPRH isoform c [Homo sapiens].
ACCESSION   NP_001357257
VERSION     NP_001357257.1
DBSOURCE    REFSEQ: accession NM_001370328.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1202)
  AUTHORS   Nagelberg,A.L., Sihota,T.S., Chuang,Y.C., Shi,R., Chow,J.L.M.,
            English,J., MacAulay,C., Lam,S., Lam,W.L. and Lockwood,W.W.
  TITLE     Integrative genomics identifies SHPRH as a tumor suppressor gene in
            lung adenocarcinoma that regulates DNA damage response
  JOURNAL   Br J Cancer 131 (3), 534-550 (2024)
   PUBMED   38890444
  REMARK    GeneRIF: Integrative genomics identifies SHPRH as a tumor
            suppressor gene in lung adenocarcinoma that regulates DNA damage
            response.
REFERENCE   2  (residues 1 to 1202)
  AUTHORS   Gao,J., Pan,H., Li,J., Jiang,J. and Wang,W.
  TITLE     A peptide encoded by the circular form of the SHPRH gene induces
            apoptosis in neuroblastoma cells
  JOURNAL   PeerJ 12, e16806 (2024)
   PUBMED   38282862
  REMARK    GeneRIF: A peptide encoded by the circular form of the SHPRH gene
            induces apoptosis in neuroblastoma cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1202)
  AUTHORS   Miller,A.K., Mao,G., Knicely,B.G., Daniels,H.G., Rahal,C.,
            Putnam,C.D., Kolodner,R.D. and Goellner,E.M.
  TITLE     Rad5 and Its Human Homologs, HLTF and SHPRH, Are Novel Interactors
            of Mismatch Repair
  JOURNAL   Front Cell Dev Biol 10, 843121 (2022)
   PUBMED   35784486
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1202)
  AUTHORS   Chen,W., Zhong,M., Yu,J., Xie,R., Zhou,T., Zhang,S., Xiong,C. and
            Huang,D.
  TITLE     KMT2B promotes SHPRH expression to regulate 131I sensitivity in
            thyroid carcinoma cells by affecting FYN protein stability
  JOURNAL   Cell Signal 88, 110165 (2021)
   PUBMED   34606908
  REMARK    GeneRIF: KMT2B promotes SHPRH expression to regulate (131)I
            sensitivity in thyroid carcinoma cells by affecting FYN protein
            stability.
REFERENCE   5  (residues 1 to 1202)
  AUTHORS   Seelinger,M., Sogaard,C.K. and Otterlei,M.
  TITLE     The Human RAD5 Homologs, HLTF and SHPRH, Have Separate Functions in
            DNA Damage Tolerance Dependent on The DNA Lesion Type
  JOURNAL   Biomolecules 10 (3), 463 (2020)
   PUBMED   32192191
  REMARK    GeneRIF: The Human RAD5 Homologs, HLTF and SHPRH, Have Separate
            Functions in DNA Damage Tolerance Dependent on The DNA Lesion Type.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1202)
  AUTHORS   Lin,J.R., Zeman,M.K., Chen,J.Y., Yee,M.C. and Cimprich,K.A.
  TITLE     SHPRH and HLTF act in a damage-specific manner to coordinate
            different forms of postreplication repair and prevent mutagenesis
  JOURNAL   Mol Cell 42 (2), 237-249 (2011)
   PUBMED   21396873
  REMARK    GeneRIF: HLTF and SHPRH suppress mutagenesis in a damage-specific
            manner, preventing mutations induced by UV rays and methyl
            methanesulfonate.
REFERENCE   7  (residues 1 to 1202)
  AUTHORS   Motegi,A., Liaw,H.J., Lee,K.Y., Roest,H.P., Maas,A., Wu,X.,
            Moinova,H., Markowitz,S.D., Ding,H., Hoeijmakers,J.H. and Myung,K.
  TITLE     Polyubiquitination of proliferating cell nuclear antigen by HLTF
            and SHPRH prevents genomic instability from stalled replication
            forks
  JOURNAL   Proc Natl Acad Sci U S A 105 (34), 12411-12416 (2008)
   PUBMED   18719106
  REMARK    GeneRIF: HLTF and SHPRH are functional homologues of yeast Rad5
            that cooperatively mediate PCNA polyubiquitination and maintain
            genomic stability.
REFERENCE   8  (residues 1 to 1202)
  AUTHORS   Motegi,A., Sood,R., Moinova,H., Markowitz,S.D., Liu,P.P. and
            Myung,K.
  TITLE     Human SHPRH suppresses genomic instability through proliferating
            cell nuclear antigen polyubiquitination
  JOURNAL   J Cell Biol 175 (5), 703-708 (2006)
   PUBMED   17130289
  REMARK    GeneRIF: We report that a putative tumor suppressor gene, SHPRH, is
            a human orthologue of yeast RAD5.The yRad5/SHPRH-dependent pathway
            is a conserved and fundamental DNA repair mechanism that protects
            the genome from genotoxic stress.
REFERENCE   9  (residues 1 to 1202)
  AUTHORS   Unk,I., Hajdu,I., Fatyol,K., Szakal,B., Blastyak,A., Bermudez,V.,
            Hurwitz,J., Prakash,L., Prakash,S. and Haracska,L.
  TITLE     Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent
            polyubiquitylation of proliferating cell nuclear antigen
  JOURNAL   Proc Natl Acad Sci U S A 103 (48), 18107-18112 (2006)
   PUBMED   17108083
  REMARK    GeneRIF: SHPRH function is an important deterrent to mutagenesis
            and carcinogenesis in humans
REFERENCE   10 (residues 1 to 1202)
  AUTHORS   Sood,R., Makalowska,I., Galdzicki,M., Hu,P., Eddings,E.,
            Robbins,C.M., Moses,T., Namkoong,J., Chen,S. and Trent,J.M.
  TITLE     Cloning and characterization of a novel gene, SHPRH, encoding a
            conserved putative protein with SNF2/helicase and PHD-finger
            domains from the 6q24 region
  JOURNAL   Genomics 82 (2), 153-161 (2003)
   PUBMED   12837266
  REMARK    GeneRIF: SHPRH maps to 6q24 and is a possible candidate for the
            tumor suppressor gene reported from that region.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL451145.15 and AL356599.19.
            
            Summary: SHPRH is a ubiquitously expressed protein that contains
            motifs characteristics of several DNA repair proteins,
            transcription factors, and helicases. SHPRH is a functional homolog
            of S. cerevisiae RAD5 (Unk et al., 2006 [PubMed
            17108083]).[supplied by OMIM, Mar 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.78154.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1202
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.3"
     Protein         1..1202
                     /product="E3 ubiquitin-protein ligase SHPRH isoform c"
                     /EC_number="2.3.2.27"
                     /note="2610103K11Rik; E3 ubiquitin-protein ligase SHPRH;
                     SNF2, histone-linker, PHD and RING finger
                     domain-containing helicase; SNF2 histone linker PHD RING
                     helicase, E3 ubiquitin protein ligase; RING-type E3
                     ubiquitin transferase SHPRH"
                     /calculated_mol_wt=137588
     Region          179..225
                     /region_name="PHD_SHPRH"
                     /note="PHD finger found in E3 ubiquitin-protein ligase
                     SHPRH; cd15547"
                     /db_xref="CDD:277022"
     Site            order(179,192..196,200,220)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277022"
     Region          <221..422
                     /region_name="DEXQc_SHPRH"
                     /note="DEXQ-box helicase domain of SHPRH; cd18070"
                     /db_xref="CDD:350828"
     Region          948..1001
                     /region_name="RING-HC_SHPRH-like"
                     /note="RING finger, HC subclass, found in SNF2
                     histone-linker PHD finger RING finger helicase (SHPRH) and
                     similar proteins; cd16569"
                     /db_xref="CDD:438231"
     Region          1027..1152
                     /region_name="SF2_C_SNF"
                     /note="C-terminal helicase domain of the SNF family
                     helicases; cd18793"
                     /db_xref="CDD:350180"
     Site            order(1056..1057,1065,1104,1125..1126)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350180"
     Site            order(1110..1111,1113,1136,1139)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350180"
     CDS             1..1202
                     /gene="SHPRH"
                     /gene_synonym="bA545I5.2; RAD5"
                     /coded_by="NM_001370328.1:1262..4870"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="GeneID:257218"
                     /db_xref="HGNC:HGNC:19336"
                     /db_xref="MIM:608048"
ORIGIN      
        1 mekkecpsfp sislvkqikg hgfsgtftlg knykeedicd ktkkqavgsp rkiqketrks
       61 gnkdtdseyl psdtsddddd pyyyyyksrr nrsklrkklv pstkkgksqp finpdsqghc
      121 patsdsgitd vamskstcis efnqeheted caeslnhads dvppsntmsp fntsdyrfec
      181 icgeldqidr kprvqclkch lwqhakcvny deknlkikpf ycphclvame pvstratlii
      241 spssichqwv deinrhvrss slrvlvyqgv kkdgflqphf laeqdiviit ydvlrselny
      301 vdiphsnsed grrlrnqkry maipsplvav ewwricldea qmvecptvka aemaqrlsgi
      361 nrwcisgtpv qrgledlfgl vvflgiepyc vkhwwvrlly rpyckknpqh lysfiakilw
      421 rsakkdvidq iqippqteei hwlhfspver hfyhrqhevc cqdvvvklrk isdwalklss
      481 ldrrtvtsil ypllrlrqac chpqavrgef lplqkstmtm eelltslqkk cgteceeahr
      541 qlvcalngla gihiikgeya laaelyrevl rsseehkgkl ktdslqrlha thnlmellia
      601 rhpgipptlr dgrleeeakq lrehymskcn tevaeaqqal ypvqqtihel qrkihsnspw
      661 wlnvihraie ftideelvqr vrneitsnyk qqtgklsmse kfrdcrglqf llttqmeeln
      721 kcqklvreav knlegppsrn viesatvchl rparlplncc vfckadelft eyesklfsnt
      781 vkgqtaifee miedeeglvd draptttrgl waisetersm kailsfaksh rfdvefvdeg
      841 stsmdlfeaw kkeykllhey wmalrnrvsa vdelamater lrvrdprepk pnppvlhiie
      901 pheveqnrik llndkavats qlqkklgqll yltnleksqd ktsggvnpep cpicarqlgk
      961 qwavltcghc fcnecisiii eqysvgshrs sikcaicrqt tshkeisyvf tsekanqeed
     1021 ipvkgshstk veavvrtlmk iqlrdpgaka lvfstwqdvl diiskaltdn nmefaqisrv
     1081 ktfqenlsaf krdpqinill lplhtgsngl tiieathvll vepilnpahe lqaigrvhri
     1141 gqtkptivhr flikatieer mqamlktaer shtnssakhs easvltvadl adlftketee
     1201 le
//
LOCUS       NP_001265533             335 aa            linear   PRI 29-NOV-2025
DEFINITION  la-related protein 1B isoform 4 [Homo sapiens].
ACCESSION   NP_001265533
VERSION     NP_001265533.1
DBSOURCE    REFSEQ: accession NM_001278604.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Werneck-de-Castro,J.P., Pecanha,F.L.M., Silvestre,D.H. and
            Bernal-Mizrachi,E.
  TITLE     The RNA-binding protein LARP1 is dispensable for pancreatic
            beta-cell function and mass
  JOURNAL   Sci Rep 11 (1), 2079 (2021)
   PUBMED   33483593
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Gao,T., Nie,Y. and Guo,J.
  TITLE     Hypermethylation of the gene LARP2 for noninvasive prenatal
            diagnosis of beta-thalassemia based on DNA methylation profile
  JOURNAL   Mol Biol Rep 39 (6), 6591-6598 (2012)
   PUBMED   22327645
  REMARK    GeneRIF: The promoter of the gene of La ribonucleoprotein domain
            family (LARP2) was significantly hypermethylated in
            beta-thalassemia, and the expression of LARP2 was significantly
            lower in beta-thalassemia.
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Orvedahl,A., Sumpter,R. Jr., Xiao,G., Ng,A., Zou,Z., Tang,Y.,
            Narimatsu,M., Gilpin,C., Sun,Q., Roth,M., Forst,C.V., Wrana,J.L.,
            Zhang,Y.E., Luby-Phelps,K., Xavier,R.J., Xie,Y. and Levine,B.
  TITLE     Image-based genome-wide siRNA screen identifies selective autophagy
            factors
  JOURNAL   Nature 480 (7375), 113-117 (2011)
   PUBMED   22020285
REFERENCE   6  (residues 1 to 335)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   7  (residues 1 to 335)
  AUTHORS   Wolin,S.L. and Cedervall,T.
  TITLE     The La protein
  JOURNAL   Annu Rev Biochem 71, 375-403 (2002)
   PUBMED   12045101
  REMARK    GeneRIF: Review discusses the La motif, found in this protein.
            Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA181086.1, BC110300.1 and
            AK092764.1.
            
            Summary: This gene encodes a protein containing domains found in
            the La related protein of Drosophila melanogaster. La
            motif-containing proteins are thought to be RNA-binding proteins,
            where the La motif and adjacent amino acids fold into an RNA
            recognition motif. The La motif is also found in proteins unrelated
            to the La protein. Alternative splicing has been observed at this
            locus and multiple variants, encoding distinct isoforms, are
            described. Additional splice variation has been identified but the
            full-length nature of these transcripts has not been determined.
            [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (4) lacks several exons and
            includes an alternate 3' terminal exon, compared to variant 1. It
            encodes isoform 4 which is shorter and has a distinct C-terminus,
            compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110300.1, SRR3476690.836649.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.2"
     Protein         1..335
                     /product="la-related protein 1B isoform 4"
                     /note="La ribonucleoprotein domain family, member 2;
                     la-related protein 1B; La ribonucleoprotein domain family
                     member 1B; la-related protein 2"
                     /calculated_mol_wt=38629
     Region          1..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Region          <110..>280
                     /region_name="LHP1"
                     /note="La protein, small RNA-binding pol III transcript
                     stabilizing protein and related La-motif-containing
                     proteins involved in translation [Posttranslational
                     modification, protein turnover, chaperones / Translation,
                     ribosomal structure and biogenesis]; COG5193"
                     /db_xref="CDD:227520"
     Region          216..288
                     /region_name="LAM"
                     /note="LA motif RNA-binding domain; cl02755"
                     /db_xref="CDD:470666"
     Site            order(222,225..226,231,234..235,237,256..258)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153396"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     CDS             1..335
                     /gene="LARP1B"
                     /gene_synonym="LARP2"
                     /coded_by="NM_001278604.2:168..1175"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS64057.1"
                     /db_xref="GeneID:55132"
                     /db_xref="HGNC:HGNC:24704"
                     /db_xref="MIM:620467"
ORIGIN      
        1 menwptpsel vntgfqsvls qgnkkpqnrk ekeekvekrs nsdskenret klngpgenvs
       61 edeaqssnqr krankhkwvp lhldvvrses qerpgsrnss rcqpeankpt hnnrrndtrs
      121 wkrdrekrdd qddvssvrse ggnirgsfrg rgrgrgrgrg rgrgnprlnf dysygyqehg
      181 ertdqpfqte lntsmmyyyd dgtgvqvypv eeallkeyik rqieyyfsve nlerdfflrg
      241 kmdeqgflpi sliagfqrvq alttnlnlil ealkdsteve ivdekmrkki epekwpipgp
      301 pprsvpptdf sqlidcpefv pgqafcshtv rvmif
//
LOCUS       NP_115615                358 aa            linear   PRI 29-NOV-2025
DEFINITION  la-related protein 1B isoform 3 [Homo sapiens].
ACCESSION   NP_115615
VERSION     NP_115615.2
DBSOURCE    REFSEQ: accession NM_032239.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Werneck-de-Castro,J.P., Pecanha,F.L.M., Silvestre,D.H. and
            Bernal-Mizrachi,E.
  TITLE     The RNA-binding protein LARP1 is dispensable for pancreatic
            beta-cell function and mass
  JOURNAL   Sci Rep 11 (1), 2079 (2021)
   PUBMED   33483593
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Gao,T., Nie,Y. and Guo,J.
  TITLE     Hypermethylation of the gene LARP2 for noninvasive prenatal
            diagnosis of beta-thalassemia based on DNA methylation profile
  JOURNAL   Mol Biol Rep 39 (6), 6591-6598 (2012)
   PUBMED   22327645
  REMARK    GeneRIF: The promoter of the gene of La ribonucleoprotein domain
            family (LARP2) was significantly hypermethylated in
            beta-thalassemia, and the expression of LARP2 was significantly
            lower in beta-thalassemia.
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Orvedahl,A., Sumpter,R. Jr., Xiao,G., Ng,A., Zou,Z., Tang,Y.,
            Narimatsu,M., Gilpin,C., Sun,Q., Roth,M., Forst,C.V., Wrana,J.L.,
            Zhang,Y.E., Luby-Phelps,K., Xavier,R.J., Xie,Y. and Levine,B.
  TITLE     Image-based genome-wide siRNA screen identifies selective autophagy
            factors
  JOURNAL   Nature 480 (7375), 113-117 (2011)
   PUBMED   22020285
REFERENCE   6  (residues 1 to 358)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Wolin,S.L. and Cedervall,T.
  TITLE     The La protein
  JOURNAL   Annu Rev Biochem 71, 375-403 (2002)
   PUBMED   12045101
  REMARK    GeneRIF: Review discusses the La motif, found in this protein.
            Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA181086.1, AL832170.1,
            AK092764.1, AC108045.3 and AA037692.1.
            
            On Apr 23, 2003 this sequence version replaced NP_115615.1.
            
            Summary: This gene encodes a protein containing domains found in
            the La related protein of Drosophila melanogaster. La
            motif-containing proteins are thought to be RNA-binding proteins,
            where the La motif and adjacent amino acids fold into an RNA
            recognition motif. The La motif is also found in proteins unrelated
            to the La protein. Alternative splicing has been observed at this
            locus and multiple variants, encoding distinct isoforms, are
            described. Additional splice variation has been identified but the
            full-length nature of these transcripts has not been determined.
            [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (3) lacks several exons and its
            transcription extends past a splice site that is used in variant 1,
            resulting in a novel 3' coding region and 3' UTR, compared to
            variant 1. It encodes isoform 3 which is much shorter and has a
            distinct C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL832170.1, SRR1803616.195115.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.2"
     Protein         1..358
                     /product="la-related protein 1B isoform 3"
                     /note="La ribonucleoprotein domain family, member 2;
                     la-related protein 1B; La ribonucleoprotein domain family
                     member 1B; la-related protein 2"
                     /calculated_mol_wt=41289
     Region          1..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Region          <110..>280
                     /region_name="LHP1"
                     /note="La protein, small RNA-binding pol III transcript
                     stabilizing protein and related La-motif-containing
                     proteins involved in translation [Posttranslational
                     modification, protein turnover, chaperones / Translation,
                     ribosomal structure and biogenesis]; COG5193"
                     /db_xref="CDD:227520"
     Region          216..288
                     /region_name="LAM"
                     /note="LA motif RNA-binding domain; cl02755"
                     /db_xref="CDD:470666"
     Site            order(222,225..226,231,234..235,237,256..258)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153396"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     CDS             1..358
                     /gene="LARP1B"
                     /gene_synonym="LARP2"
                     /coded_by="NM_032239.4:168..1244"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS47133.1"
                     /db_xref="GeneID:55132"
                     /db_xref="HGNC:HGNC:24704"
                     /db_xref="MIM:620467"
ORIGIN      
        1 menwptpsel vntgfqsvls qgnkkpqnrk ekeekvekrs nsdskenret klngpgenvs
       61 edeaqssnqr krankhkwvp lhldvvrses qerpgsrnss rcqpeankpt hnnrrndtrs
      121 wkrdrekrdd qddvssvrse ggnirgsfrg rgrgrgrgrg rgrgnprlnf dysygyqehg
      181 ertdqpfqte lntsmmyyyd dgtgvqvypv eeallkeyik rqieyyfsve nlerdfflrg
      241 kmdeqgflpi sliagfqrvq alttnlnlil ealkdsteve ivdekmrkki epekwpipgp
      301 pprsvpptdf sqlidcpefv pgqafcshtg nifssrandv tvgylvqfty lfiyfqfi
//
LOCUS       NP_001288104             486 aa            linear   PRI 29-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 30 isoform 2 [Homo sapiens].
ACCESSION   NP_001288104
VERSION     NP_001288104.1
DBSOURCE    REFSEQ: accession NM_001301175.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Kazi,N.H., Klink,N., Gallant,K., Kipka,G.M. and Gersch,M.
  TITLE     Chimeric deubiquitinase engineering reveals structural basis for
            specific inhibition of the mitophagy regulator USP30
  JOURNAL   Nat Struct Mol Biol 32 (9), 1776-1786 (2025)
   PUBMED   40325251
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Crunkhorn,S.
  TITLE     USP30 inhibition protects dopaminergic neurons
  JOURNAL   Nat Rev Drug Discov 23 (1), 22 (2024)
   PUBMED   38040789
  REMARK    GeneRIF: USP30 inhibition protects dopaminergic neurons.
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Zhou,W., Xu,S., Deng,T., Zhou,R. and Wang,C.
  TITLE     LncRNA USP30-AS1 promotes the survival of acute myeloid leukemia
            cells by cis-regulating USP30 and ANKRD13A
  JOURNAL   Hum Cell 35 (1), 360-378 (2022)
   PUBMED   34694569
  REMARK    GeneRIF: LncRNA USP30-AS1 promotes the survival of acute myeloid
            leukemia cells by cis-regulating USP30 and ANKRD13A.
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 486)
  AUTHORS   Cunningham,C.N., Baughman,J.M., Phu,L., Tea,J.S., Yu,C., Coons,M.,
            Kirkpatrick,D.S., Bingol,B. and Corn,J.E.
  TITLE     USP30 and parkin homeostatically regulate atypical ubiquitin chains
            on mitochondria
  JOURNAL   Nat Cell Biol 17 (2), 160-169 (2015)
   PUBMED   25621951
  REMARK    GeneRIF: The mechanism by which parkin, an E3 ubiquitin ligase, and
            USP30, a mitochondrion-localized deubiquitylase, regulate
            mitophagy, was investigated.
REFERENCE   7  (residues 1 to 486)
  AUTHORS   Bingol,B., Tea,J.S., Phu,L., Reichelt,M., Bakalarski,C.E., Song,Q.,
            Foreman,O., Kirkpatrick,D.S. and Sheng,M.
  TITLE     The mitochondrial deubiquitinase USP30 opposes parkin-mediated
            mitophagy
  JOURNAL   Nature 510 (7505), 370-375 (2014)
   PUBMED   24896179
  REMARK    GeneRIF: reducing USP30 activity enhances mitochondrial degradation
            in neurons
REFERENCE   8  (residues 1 to 486)
  AUTHORS   Nakamura,N. and Hirose,S.
  TITLE     Regulation of mitochondrial morphology by USP30, a deubiquitinating
            enzyme present in the mitochondrial outer membrane
  JOURNAL   Mol Biol Cell 19 (5), 1903-1911 (2008)
   PUBMED   18287522
  REMARK    GeneRIF: USP30 participates in the maintenance of mitochondrial
            morphology, a finding that provides new insight into the cellular
            function of deubiquitination.
REFERENCE   9  (residues 1 to 486)
  AUTHORS   Quesada,V., Diaz-Perales,A., Gutierrez-Fernandez,A., Garabaya,C.,
            Cal,S. and Lopez-Otin,C.
  TITLE     Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
            proteases
  JOURNAL   Biochem Biophys Res Commun 314 (1), 54-62 (2004)
   PUBMED   14715245
REFERENCE   10 (residues 1 to 486)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK097830.1, AC011596.27, AL834278.1 and BX095894.1.
            
            Summary: USP30, a member of the ubiquitin-specific protease family
            (see USP1, MIM 603478), is a novel mitochondrial deubiquitinating
            (DUB) enzyme (Nakamura and Hirose, 2008 [PubMed
            18287522]).[supplied by OMIM, Dec 2008].
            
            Transcript Variant: This variant (2) has a different 5' structure,
            resulting in the use of a downstream start codon, compared to
            variant 1. The encoded isoform (2) has a shorter N-terminus
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK097830.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..486
                     /product="ubiquitin carboxyl-terminal hydrolase 30 isoform
                     2"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin carboxyl-terminal hydrolase 30;
                     ub-specific protease 30; ubiquitin thioesterase 30;
                     deubiquitinating enzyme 30; ubiquitin-specific protease
                     30; ubiquitin-specific-processing protease 30; ubiquitin
                     thiolesterase 30"
                     /calculated_mol_wt=54978
     Region          38..469
                     /region_name="Peptidase_C19F"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02662"
                     /db_xref="CDD:239127"
     Region          <38..>234
                     /region_name="UBP12"
                     /note="Ubiquitin C-terminal hydrolase [Posttranslational
                     modification, protein turnover, chaperones]; COG5560"
                     /db_xref="CDD:227847"
     Site            order(41,46,421,447)
                     /site_type="active"
                     /db_xref="CDD:239127"
     CDS             1..486
                     /gene="USP30"
                     /coded_by="NM_001301175.2:577..2037"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS76599.1"
                     /db_xref="GeneID:84749"
                     /db_xref="HGNC:HGNC:20065"
                     /db_xref="MIM:612492"
ORIGIN      
        1 mknwgviggi aaalaagiyv iwgpiterkk rrkglvpglv nlgntcfmns llqglsacpa
       61 firwleefts qysrdqkepp shqylsltll hllkalscqe vtddevldas clldvlrmyr
      121 wqissfeeqd ahelfhvits slederdrqp rvthlfdvhs leqqseitpk qitcrtrgsp
      181 hptsnhwksq hpfhgrltsn mvckhcehqs pvrfdtfdsl slsipaatwg hpltldhclh
      241 hfissesvrd vvcdnctkie akgtlngekv ehqrttfvkq lklgklpqcl cihlqrlsws
      301 shgtplkrhe hvqfneflmm diykyhllgh kpsqhnpkln knpgptlelq dgpgaptpvl
      361 nqpgapktqi fmngacspsl lptlsapmpf plpvvpdyss stylfrlmav vvhhgdmhsg
      421 hfvtyrrspp sarnplstsn qwlwvsddtv rkaslqevls ssayllfyer vlsrmqhqsq
      481 ecksee
//
LOCUS       NP_775105               1659 aa            linear   PRI 29-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase SHPRH isoform b [Homo sapiens].
ACCESSION   NP_775105
VERSION     NP_775105.1
DBSOURCE    REFSEQ: accession NM_173082.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1659)
  AUTHORS   Nagelberg,A.L., Sihota,T.S., Chuang,Y.C., Shi,R., Chow,J.L.M.,
            English,J., MacAulay,C., Lam,S., Lam,W.L. and Lockwood,W.W.
  TITLE     Integrative genomics identifies SHPRH as a tumor suppressor gene in
            lung adenocarcinoma that regulates DNA damage response
  JOURNAL   Br J Cancer 131 (3), 534-550 (2024)
   PUBMED   38890444
  REMARK    GeneRIF: Integrative genomics identifies SHPRH as a tumor
            suppressor gene in lung adenocarcinoma that regulates DNA damage
            response.
REFERENCE   2  (residues 1 to 1659)
  AUTHORS   Gao,J., Pan,H., Li,J., Jiang,J. and Wang,W.
  TITLE     A peptide encoded by the circular form of the SHPRH gene induces
            apoptosis in neuroblastoma cells
  JOURNAL   PeerJ 12, e16806 (2024)
   PUBMED   38282862
  REMARK    GeneRIF: A peptide encoded by the circular form of the SHPRH gene
            induces apoptosis in neuroblastoma cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1659)
  AUTHORS   Miller,A.K., Mao,G., Knicely,B.G., Daniels,H.G., Rahal,C.,
            Putnam,C.D., Kolodner,R.D. and Goellner,E.M.
  TITLE     Rad5 and Its Human Homologs, HLTF and SHPRH, Are Novel Interactors
            of Mismatch Repair
  JOURNAL   Front Cell Dev Biol 10, 843121 (2022)
   PUBMED   35784486
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1659)
  AUTHORS   Chen,W., Zhong,M., Yu,J., Xie,R., Zhou,T., Zhang,S., Xiong,C. and
            Huang,D.
  TITLE     KMT2B promotes SHPRH expression to regulate 131I sensitivity in
            thyroid carcinoma cells by affecting FYN protein stability
  JOURNAL   Cell Signal 88, 110165 (2021)
   PUBMED   34606908
  REMARK    GeneRIF: KMT2B promotes SHPRH expression to regulate (131)I
            sensitivity in thyroid carcinoma cells by affecting FYN protein
            stability.
REFERENCE   5  (residues 1 to 1659)
  AUTHORS   Seelinger,M., Sogaard,C.K. and Otterlei,M.
  TITLE     The Human RAD5 Homologs, HLTF and SHPRH, Have Separate Functions in
            DNA Damage Tolerance Dependent on The DNA Lesion Type
  JOURNAL   Biomolecules 10 (3), 463 (2020)
   PUBMED   32192191
  REMARK    GeneRIF: The Human RAD5 Homologs, HLTF and SHPRH, Have Separate
            Functions in DNA Damage Tolerance Dependent on The DNA Lesion Type.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1659)
  AUTHORS   Lin,J.R., Zeman,M.K., Chen,J.Y., Yee,M.C. and Cimprich,K.A.
  TITLE     SHPRH and HLTF act in a damage-specific manner to coordinate
            different forms of postreplication repair and prevent mutagenesis
  JOURNAL   Mol Cell 42 (2), 237-249 (2011)
   PUBMED   21396873
  REMARK    GeneRIF: HLTF and SHPRH suppress mutagenesis in a damage-specific
            manner, preventing mutations induced by UV rays and methyl
            methanesulfonate.
REFERENCE   7  (residues 1 to 1659)
  AUTHORS   Motegi,A., Liaw,H.J., Lee,K.Y., Roest,H.P., Maas,A., Wu,X.,
            Moinova,H., Markowitz,S.D., Ding,H., Hoeijmakers,J.H. and Myung,K.
  TITLE     Polyubiquitination of proliferating cell nuclear antigen by HLTF
            and SHPRH prevents genomic instability from stalled replication
            forks
  JOURNAL   Proc Natl Acad Sci U S A 105 (34), 12411-12416 (2008)
   PUBMED   18719106
  REMARK    GeneRIF: HLTF and SHPRH are functional homologues of yeast Rad5
            that cooperatively mediate PCNA polyubiquitination and maintain
            genomic stability.
REFERENCE   8  (residues 1 to 1659)
  AUTHORS   Motegi,A., Sood,R., Moinova,H., Markowitz,S.D., Liu,P.P. and
            Myung,K.
  TITLE     Human SHPRH suppresses genomic instability through proliferating
            cell nuclear antigen polyubiquitination
  JOURNAL   J Cell Biol 175 (5), 703-708 (2006)
   PUBMED   17130289
  REMARK    GeneRIF: We report that a putative tumor suppressor gene, SHPRH, is
            a human orthologue of yeast RAD5.The yRad5/SHPRH-dependent pathway
            is a conserved and fundamental DNA repair mechanism that protects
            the genome from genotoxic stress.
REFERENCE   9  (residues 1 to 1659)
  AUTHORS   Unk,I., Hajdu,I., Fatyol,K., Szakal,B., Blastyak,A., Bermudez,V.,
            Hurwitz,J., Prakash,L., Prakash,S. and Haracska,L.
  TITLE     Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent
            polyubiquitylation of proliferating cell nuclear antigen
  JOURNAL   Proc Natl Acad Sci U S A 103 (48), 18107-18112 (2006)
   PUBMED   17108083
  REMARK    GeneRIF: SHPRH function is an important deterrent to mutagenesis
            and carcinogenesis in humans
REFERENCE   10 (residues 1 to 1659)
  AUTHORS   Sood,R., Makalowska,I., Galdzicki,M., Hu,P., Eddings,E.,
            Robbins,C.M., Moses,T., Namkoong,J., Chen,S. and Trent,J.M.
  TITLE     Cloning and characterization of a novel gene, SHPRH, encoding a
            conserved putative protein with SNF2/helicase and PHD-finger
            domains from the 6q24 region
  JOURNAL   Genomics 82 (2), 153-161 (2003)
   PUBMED   12837266
  REMARK    GeneRIF: SHPRH maps to 6q24 and is a possible candidate for the
            tumor suppressor gene reported from that region.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL451145.15, AY163808.1, AY161136.1, AA315737.1 and BX648322.1.
            
            Summary: SHPRH is a ubiquitously expressed protein that contains
            motifs characteristics of several DNA repair proteins,
            transcription factors, and helicases. SHPRH is a functional homolog
            of S. cerevisiae RAD5 (Unk et al., 2006 [PubMed
            17108083]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (2) uses three alternate splice
            sites in the coding region, one of which results in a frameshift,
            compared to variant 1. It encodes isoform b, which is shorter and
            has a distinct C-terminus, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY163808.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1659
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.3"
     Protein         1..1659
                     /product="E3 ubiquitin-protein ligase SHPRH isoform b"
                     /EC_number="2.3.2.27"
                     /note="2610103K11Rik; E3 ubiquitin-protein ligase SHPRH;
                     SNF2, histone-linker, PHD and RING finger
                     domain-containing helicase; SNF2 histone linker PHD RING
                     helicase, E3 ubiquitin protein ligase; RING-type E3
                     ubiquitin transferase SHPRH"
                     /calculated_mol_wt=190366
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q149N8.2)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q149N8.2)"
     Region          <298..>388
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
     Region          304..>409
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Site            375..381
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350670"
     Region          440..508
                     /region_name="Linker_histone"
                     /note="linker histone H1 and H5 family; pfam00538"
                     /db_xref="CDD:459846"
     Region          525..607
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q149N8.2)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TPQ3; propagated from
                     UniProtKB/Swiss-Prot (Q149N8.2)"
     Region          660..706
                     /region_name="PHD_SHPRH"
                     /note="PHD finger found in E3 ubiquitin-protein ligase
                     SHPRH; cd15547"
                     /db_xref="CDD:277022"
     Site            order(660,673..677,681,701)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277022"
     Region          <702..903
                     /region_name="DEXQc_SHPRH"
                     /note="DEXQ-box helicase domain of SHPRH; cd18070"
                     /db_xref="CDD:350828"
     Region          819..822
                     /region_name="DEAQ box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q149N8.2)"
     Region          1433..1486
                     /region_name="RING-HC_SHPRH-like"
                     /note="RING finger, HC subclass, found in SNF2
                     histone-linker PHD finger RING finger helicase (SHPRH) and
                     similar proteins; cd16569"
                     /db_xref="CDD:438231"
     Region          1512..1637
                     /region_name="SF2_C_SNF"
                     /note="C-terminal helicase domain of the SNF family
                     helicases; cd18793"
                     /db_xref="CDD:350180"
     Site            order(1541..1542,1550,1589,1610..1611)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350180"
     Site            order(1595..1596,1598,1621,1624)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350180"
     CDS             1..1659
                     /gene="SHPRH"
                     /gene_synonym="bA545I5.2; RAD5"
                     /coded_by="NM_173082.4:661..5640"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47496.1"
                     /db_xref="GeneID:257218"
                     /db_xref="HGNC:HGNC:19336"
                     /db_xref="MIM:608048"
ORIGIN      
        1 mssrrkrapp vrvdeekrqq lhwnmhedrr nepiiisddd eqpcpgsdts sahyiilsds
       61 lkeevahrdk krcskvvsfs kpiekeetvg ifsplsvkln ivispyhfdn swkaflgelt
      121 lqllpaqsli enfsersitl mssessnqfl iyvhskgedv ekqkkepmsi cdkgilvess
      181 fsgemledlg wlqkkrrikl yqkpegnhii kvgiylleag lakldflsda nsrmkkfnql
      241 mkkvmeklhn siipdvleed eddpesepeg qdidelyhfv kqthqqetqs iqvdvqhpal
      301 ipvlrpyqre avnwmlqqec frsspatesa lhflwreivt seglklyynp ytgciireyp
      361 nsgpqllggi lademglgkt vevlalilth trqdvkqdal tlpegkvvny fipshyfggk
      421 lkkteiqnie fepkekvqcp ptrvmiltav kemngkkgvs ilsiykyvss iyrydvqrnr
      481 sllkrmlkcl ifeglvkqik ghgfsgtftl gknykeedic dktkkqavgs prkiqketrk
      541 sgnkdtdsey lpsdtsdddd dpyyyyyksr rnrsklrkkl vpstkkgksq pfinpdsqgh
      601 cpatsdsgit dvamskstci sefnqehete dcaeslnhad sdvppsntms pfntsdyrfe
      661 cicgeldqid rkprvqclkc hlwqhakcvn ydeknlkikp fycphclvam epvstratli
      721 ispssichqw vdeinrhvrs sslrvlvyqg vkkdgflqph flaeqdivii tydvlrseln
      781 yvdiphsnse dgrrlrnqkr ymaipsplva vewwriclde aqmvecptvk aaemaqrlsg
      841 inrwcisgtp vqrgledlfg lvvflgiepy cvkhwwvrll yrpyckknpq hlysfiakil
      901 wrsakkdvid qiqippqtee ihwlhfspve rhfyhrqhev ccqdvvvklr kisdwalkls
      961 sldrrtvtsi lypllrlrqa cchpqavrge flplqksfeq stfsfstmtm eelltslqkk
     1021 cgteceeahr qlvcalngla gihiikgeya laaelyrevl rsseehkgkl ktdslqrlha
     1081 thnlmellia rhpgipptlr dgrleeeakq lrehymskcn tevaeaqqal ypvqqtihel
     1141 qrkihsnspw wlnvihraie ftideelvqr vrneitsnyk qqtgklsmse kglqfllttq
     1201 meelnkcqkl vreavknleg ppsrnviesa tvchlrparl plnccvfcka delfteyesk
     1261 lfsntvkgqt aifeemiede eglvddrapt ttrglwaise tersmkails fakshrfdve
     1321 fvdegstsmd lfeawkkeyk llheywmalr nrvsavdela materlrvrd prepkpnppv
     1381 lhiiepheve qnrikllndk avatsqlqkk lgqllyltnl eksqdktsgg vnpepcpica
     1441 rqlgkqwavl tcghcfcnec isiiieqysv gshrssikca icrqttshke isyvftseka
     1501 nqeedipvkg shstkveavv rtlmkiqlrd pgakalvfst wqdvldiisk altdnnmefa
     1561 qisrvktfqe nlsafkrdpq inilllplht gsngltiiea thvllvepil npahelqaig
     1621 rvhrigqtkp tivhrflika tieermqaml ktaersiyi
//
LOCUS       NP_835144                522 aa            linear   PRI 29-NOV-2025
DEFINITION  la-related protein 1B isoform 2 [Homo sapiens].
ACCESSION   NP_835144
VERSION     NP_835144.1
DBSOURCE    REFSEQ: accession NM_178043.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Werneck-de-Castro,J.P., Pecanha,F.L.M., Silvestre,D.H. and
            Bernal-Mizrachi,E.
  TITLE     The RNA-binding protein LARP1 is dispensable for pancreatic
            beta-cell function and mass
  JOURNAL   Sci Rep 11 (1), 2079 (2021)
   PUBMED   33483593
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Gao,T., Nie,Y. and Guo,J.
  TITLE     Hypermethylation of the gene LARP2 for noninvasive prenatal
            diagnosis of beta-thalassemia based on DNA methylation profile
  JOURNAL   Mol Biol Rep 39 (6), 6591-6598 (2012)
   PUBMED   22327645
  REMARK    GeneRIF: The promoter of the gene of La ribonucleoprotein domain
            family (LARP2) was significantly hypermethylated in
            beta-thalassemia, and the expression of LARP2 was significantly
            lower in beta-thalassemia.
REFERENCE   5  (residues 1 to 522)
  AUTHORS   Orvedahl,A., Sumpter,R. Jr., Xiao,G., Ng,A., Zou,Z., Tang,Y.,
            Narimatsu,M., Gilpin,C., Sun,Q., Roth,M., Forst,C.V., Wrana,J.L.,
            Zhang,Y.E., Luby-Phelps,K., Xavier,R.J., Xie,Y. and Levine,B.
  TITLE     Image-based genome-wide siRNA screen identifies selective autophagy
            factors
  JOURNAL   Nature 480 (7375), 113-117 (2011)
   PUBMED   22020285
REFERENCE   6  (residues 1 to 522)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   7  (residues 1 to 522)
  AUTHORS   Wolin,S.L. and Cedervall,T.
  TITLE     The La protein
  JOURNAL   Annu Rev Biochem 71, 375-403 (2002)
   PUBMED   12045101
  REMARK    GeneRIF: Review discusses the La motif, found in this protein.
            Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA181086.1, AK001240.1,
            AK092764.1 and BM129812.1.
            
            Summary: This gene encodes a protein containing domains found in
            the La related protein of Drosophila melanogaster. La
            motif-containing proteins are thought to be RNA-binding proteins,
            where the La motif and adjacent amino acids fold into an RNA
            recognition motif. The La motif is also found in proteins unrelated
            to the La protein. Alternative splicing has been observed at this
            locus and multiple variants, encoding distinct isoforms, are
            described. Additional splice variation has been identified but the
            full-length nature of these transcripts has not been determined.
            [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (2) lacks several exons and its
            transcription extends past a splice site that is used in variant 1,
            resulting in a novel 3' coding region and 3' UTR, compared to
            variant 1. It encodes isoform 2 which is shorter and has a distinct
            C-terminus, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.183759.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.2"
     Protein         1..522
                     /product="la-related protein 1B isoform 2"
                     /note="La ribonucleoprotein domain family, member 2;
                     la-related protein 1B; La ribonucleoprotein domain family
                     member 1B; la-related protein 2"
                     /calculated_mol_wt=59666
     Region          1..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Region          <110..>280
                     /region_name="LHP1"
                     /note="La protein, small RNA-binding pol III transcript
                     stabilizing protein and related La-motif-containing
                     proteins involved in translation [Posttranslational
                     modification, protein turnover, chaperones / Translation,
                     ribosomal structure and biogenesis]; COG5193"
                     /db_xref="CDD:227520"
     Region          216..288
                     /region_name="LAM"
                     /note="LA motif RNA-binding domain; cl02755"
                     /db_xref="CDD:470666"
     Site            order(222,225..226,231,234..235,237,256..258)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153396"
     Region          327..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     CDS             1..522
                     /gene="LARP1B"
                     /gene_synonym="LARP2"
                     /coded_by="NM_178043.3:168..1736"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:55132"
                     /db_xref="HGNC:HGNC:24704"
                     /db_xref="MIM:620467"
ORIGIN      
        1 menwptpsel vntgfqsvls qgnkkpqnrk ekeekvekrs nsdskenret klngpgenvs
       61 edeaqssnqr krankhkwvp lhldvvrses qerpgsrnss rcqpeankpt hnnrrndtrs
      121 wkrdrekrdd qddvssvrse ggnirgsfrg rgrgrgrgrg rgrgnprlnf dysygyqehg
      181 ertdqpfqte lntsmmyyyd dgtgvqvypv eeallkeyik rqieyyfsve nlerdfflrg
      241 kmdeqgflpi sliagfqrvq alttnlnlil ealkdsteve ivdekmrkki epekwpipgp
      301 pprsvpptdf sqlidcpefv pgqafcshte sapnsprigs plspkknset silqamsrgl
      361 stslpdldse pwievkkrhq papvklresv svpegslnql csseepeqee ldflfdeeie
      421 qigrkntftd wsdndsdyei ddqdlnkili vtqtppyvkk hpggdrtgth msrakitsel
      481 akvindglyy yeqdlwmeed enkhtaikvi vsgqhlstda lf
//
LOCUS       NP_995325                 82 aa            linear   PRI 29-NOV-2025
DEFINITION  musculoskeletal embryonic nuclear protein 1 [Homo sapiens].
ACCESSION   NP_995325 XP_371644
VERSION     NP_995325.4
DBSOURCE    REFSEQ: accession NM_205853.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Kim,C.J. and Hadjiargyrou,M.
  TITLE     Mustn1 in Skeletal Muscle: A Novel Regulator?
  JOURNAL   Genes (Basel) 15 (7), 829 (2024)
   PUBMED   39062608
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 82)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Ripke,S., O'Dushlaine,C., Chambert,K., Moran,J.L., Kahler,A.K.,
            Akterin,S., Bergen,S.E., Collins,A.L., Crowley,J.J., Fromer,M.,
            Kim,Y., Lee,S.H., Magnusson,P.K., Sanchez,N., Stahl,E.A.,
            Williams,S., Wray,N.R., Xia,K., Bettella,F., Borglum,A.D.,
            Bulik-Sullivan,B.K., Cormican,P., Craddock,N., de Leeuw,C.,
            Durmishi,N., Gill,M., Golimbet,V., Hamshere,M.L., Holmans,P.,
            Hougaard,D.M., Kendler,K.S., Lin,K., Morris,D.W., Mors,O.,
            Mortensen,P.B., Neale,B.M., O'Neill,F.A., Owen,M.J.,
            Milovancevic,M.P., Posthuma,D., Powell,J., Richards,A.L.,
            Riley,B.P., Ruderfer,D., Rujescu,D., Sigurdsson,E., Silagadze,T.,
            Smit,A.B., Stefansson,H., Steinberg,S., Suvisaari,J., Tosato,S.,
            Verhage,M., Walters,J.T., Levinson,D.F., Gejman,P.V., Kendler,K.S.,
            Laurent,C., Mowry,B.J., O'Donovan,M.C., Owen,M.J., Pulver,A.E.,
            Riley,B.P., Schwab,S.G., Wildenauer,D.B., Dudbridge,F., Holmans,P.,
            Shi,J., Albus,M., Alexander,M., Campion,D., Cohen,D., Dikeos,D.,
            Duan,J., Eichhammer,P., Godard,S., Hansen,M., Lerer,F.B.,
            Liang,K.Y., Maier,W., Mallet,J., Nertney,D.A., Nestadt,G.,
            Norton,N., O'Neill,F.A., Papadimitriou,G.N., Ribble,R.,
            Sanders,A.R., Silverman,J.M., Walsh,D., Williams,N.M., Wormley,B.,
            Arranz,M.J., Bakker,S., Bender,S., Bramon,E., Collier,D.,
            Crespo-Facorro,B., Hall,J., Iyegbe,C., Jablensky,A., Kahn,R.S.,
            Kalaydjieva,L., Lawrie,S., Lewis,C.M., Lin,K., Linszen,D.H.,
            Mata,I., McIntosh,A., Murray,R.M., Ophoff,R.A., Powell,J.,
            Rujescu,D., Van Os,J., Walshe,M., Weisbrod,M., Wiersma,D.,
            Donnelly,P., Barroso,I., Blackwell,J.M., Bramon,E., Brown,M.A.,
            Casas,J.P., Corvin,A.P., Deloukas,P., Duncanson,A., Jankowski,J.,
            Markus,H.S., Mathew,C.G., Palmer,C.N., Plomin,R., Rautanen,A.,
            Sawcer,S.J., Trembath,R.C., Viswanathan,A.C., Wood,N.W.,
            Spencer,C.C., Band,G., Bellenguez,C., Freeman,C., Hellenthal,G.,
            Giannoulatou,E., Pirinen,M., Pearson,R.D., Strange,A., Su,Z.,
            Vukcevic,D., Donnelly,P., Langford,C., Hunt,S.E., Edkins,S.,
            Gwilliam,R., Blackburn,H., Bumpstead,S.J., Dronov,S., Gillman,M.,
            Gray,E., Hammond,N., Jayakumar,A., McCann,O.T., Liddle,J.,
            Potter,S.C., Ravindrarajah,R., Ricketts,M.,
            Tashakkori-Ghanbaria,A., Waller,M.J., Weston,P., Widaa,S.,
            Whittaker,P., Barroso,I., Deloukas,P., Mathew,C.G., Blackwell,J.M.,
            Brown,M.A., Corvin,A.P., McCarthy,M.I., Spencer,C.C., Bramon,E.,
            Corvin,A.P., O'Donovan,M.C., Stefansson,K., Scolnick,E.,
            Purcell,S., McCarroll,S.A., Sklar,P., Hultman,C.M. and
            Sullivan,P.F.
  CONSRTM   Multicenter Genetic Studies of Schizophrenia Consortium; Psychosis
            Endophenotypes International Consortium; Wellcome Trust Case
            Control Consortium 2
  TITLE     Genome-wide association analysis identifies 13 new risk loci for
            schizophrenia
  JOURNAL   Nat Genet 45 (10), 1150-1159 (2013)
   PUBMED   23974872
REFERENCE   4  (residues 1 to 82)
  AUTHORS   Kottgen,A., Albrecht,E., Teumer,A., Vitart,V., Krumsiek,J.,
            Hundertmark,C., Pistis,G., Ruggiero,D., O'Seaghdha,C.M., Haller,T.,
            Yang,Q., Tanaka,T., Johnson,A.D., Kutalik,Z., Smith,A.V., Shi,J.,
            Struchalin,M., Middelberg,R.P., Brown,M.J., Gaffo,A.L., Pirastu,N.,
            Li,G., Hayward,C., Zemunik,T., Huffman,J., Yengo,L., Zhao,J.H.,
            Demirkan,A., Feitosa,M.F., Liu,X., Malerba,G., Lopez,L.M., van der
            Harst,P., Li,X., Kleber,M.E., Hicks,A.A., Nolte,I.M., Johansson,A.,
            Murgia,F., Wild,S.H., Bakker,S.J., Peden,J.F., Dehghan,A.,
            Steri,M., Tenesa,A., Lagou,V., Salo,P., Mangino,M., Rose,L.M.,
            Lehtimaki,T., Woodward,O.M., Okada,Y., Tin,A., Muller,C.,
            Oldmeadow,C., Putku,M., Czamara,D., Kraft,P., Frogheri,L.,
            Thun,G.A., Grotevendt,A., Gislason,G.K., Harris,T.B., Launer,L.J.,
            McArdle,P., Shuldiner,A.R., Boerwinkle,E., Coresh,J., Schmidt,H.,
            Schallert,M., Martin,N.G., Montgomery,G.W., Kubo,M., Nakamura,Y.,
            Tanaka,T., Munroe,P.B., Samani,N.J., Jacobs,D.R. Jr., Liu,K.,
            D'Adamo,P., Ulivi,S., Rotter,J.I., Psaty,B.M., Vollenweider,P.,
            Waeber,G., Campbell,S., Devuyst,O., Navarro,P., Kolcic,I.,
            Hastie,N., Balkau,B., Froguel,P., Esko,T., Salumets,A., Khaw,K.T.,
            Langenberg,C., Wareham,N.J., Isaacs,A., Kraja,A., Zhang,Q.,
            Wild,P.S., Scott,R.J., Holliday,E.G., Org,E., Viigimaa,M.,
            Bandinelli,S., Metter,J.E., Lupo,A., Trabetti,E., Sorice,R.,
            Doring,A., Lattka,E., Strauch,K., Theis,F., Waldenberger,M.,
            Wichmann,H.E., Davies,G., Gow,A.J., Bruinenberg,M., Stolk,R.P.,
            Kooner,J.S., Zhang,W., Winkelmann,B.R., Boehm,B.O., Lucae,S.,
            Penninx,B.W., Smit,J.H., Curhan,G., Mudgal,P., Plenge,R.M.,
            Portas,L., Persico,I., Kirin,M., Wilson,J.F., Mateo Leach,I., van
            Gilst,W.H., Goel,A., Ongen,H., Hofman,A., Rivadeneira,F.,
            Uitterlinden,A.G., Imboden,M., von Eckardstein,A., Cucca,F.,
            Nagaraja,R., Piras,M.G., Nauck,M., Schurmann,C., Budde,K.,
            Ernst,F., Farrington,S.M., Theodoratou,E., Prokopenko,I.,
            Stumvoll,M., Jula,A., Perola,M., Salomaa,V., Shin,S.Y.,
            Spector,T.D., Sala,C., Ridker,P.M., Kahonen,M., Viikari,J.,
            Hengstenberg,C., Nelson,C.P., Meschia,J.F., Nalls,M.A., Sharma,P.,
            Singleton,A.B., Kamatani,N., Zeller,T., Burnier,M., Attia,J.,
            Laan,M., Klopp,N., Hillege,H.L., Kloiber,S., Choi,H., Pirastu,M.,
            Tore,S., Probst-Hensch,N.M., Volzke,H., Gudnason,V., Parsa,A.,
            Schmidt,R., Whitfield,J.B., Fornage,M., Gasparini,P.,
            Siscovick,D.S., Polasek,O., Campbell,H., Rudan,I., Bouatia-Naji,N.,
            Metspalu,A., Loos,R.J., van Duijn,C.M., Borecki,I.B., Ferrucci,L.,
            Gambaro,G., Deary,I.J., Wolffenbuttel,B.H., Chambers,J.C., Marz,W.,
            Pramstaller,P.P., Snieder,H., Gyllensten,U., Wright,A.F., Navis,G.,
            Watkins,H., Witteman,J.C., Sanna,S., Schipf,S., Dunlop,M.G.,
            Tonjes,A., Ripatti,S., Soranzo,N., Toniolo,D., Chasman,D.I.,
            Raitakari,O., Kao,W.H., Ciullo,M., Fox,C.S., Caulfield,M.,
            Bochud,M. and Gieger,C.
  CONSRTM   LifeLines Cohort Study; CARDIoGRAM Consortium; DIAGRAM Consortium;
            ICBP Consortium; MAGIC Consortium
  TITLE     Genome-wide association analyses identify 18 new loci associated
            with serum urate concentrations
  JOURNAL   Nat Genet 45 (2), 145-154 (2013)
   PUBMED   23263486
REFERENCE   5  (residues 1 to 82)
  CONSRTM   Psychiatric GWAS Consortium Bipolar Disorder Working Group
  TITLE     Large-scale genome-wide association analysis of bipolar disorder
            identifies a new susceptibility locus near ODZ4
  JOURNAL   Nat Genet 43 (10), 977-983 (2011)
   PUBMED   21926972
  REMARK    Erratum:[Nat Genet. 2012 Sep;44(9):1072. Fullerton, Janice M
            [added]; Hyoun, Phil L [corrected to Lee, Phil H]; Meng, Fan Guo
            [corrected to Meng, Fan]]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 82)
  AUTHORS   Kostek,M.C., Chen,Y.W., Cuthbertson,D.J., Shi,R., Fedele,M.J.,
            Esser,K.A. and Rennie,M.J.
  TITLE     Gene expression responses over 24 h to lengthening and shortening
            contractions in human muscle: major changes in CSRP3, MUSTN1, SIX1,
            and FBXO32
  JOURNAL   Physiol Genomics 31 (1), 42-52 (2007)
   PUBMED   17519359
  REMARK    GeneRIF: CSRP3, MUSTN1, SIX1, and FBXO32 expression changes in
            response to lengthening and shortening contractions in human muscle
REFERENCE   7  (residues 1 to 82)
  AUTHORS   Lombardo,F., Komatsu,D. and Hadjiargyrou,M.
  TITLE     Molecular cloning and characterization of Mustang, a novel nuclear
            protein expressed during skeletal development and regeneration
  JOURNAL   FASEB J 18 (1), 52-61 (2004)
   PUBMED   14718386
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099667.2.
            
            On Nov 23, 2018 this sequence version replaced NP_995325.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX089772.1, DA324872.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2152568
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000446157.3/ ENSP00000410910.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.1"
     Protein         1..82
                     /product="musculoskeletal embryonic nuclear protein 1"
                     /note="musculoskeletal temporally activated novel"
                     /calculated_mol_wt=8780
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVN3.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XX4; propagated from
                     UniProtKB/Swiss-Prot (Q8IVN3.2)"
     Region          8..82
                     /region_name="Mustang"
                     /note="Musculoskeletal, temporally activated-embryonic
                     nuclear protein 1; pfam15682"
                     /db_xref="CDD:464800"
     Region          10..18
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVN3.2)"
     Region          49..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVN3.2)"
     CDS             1..82
                     /gene="MUSTN1"
                     /gene_synonym="MUSTANG"
                     /coded_by="NM_205853.4:72..320"
                     /db_xref="CCDS:CCDS46846.1"
                     /db_xref="GeneID:389125"
                     /db_xref="HGNC:HGNC:22144"
                     /db_xref="MIM:617195"
ORIGIN      
        1 msqagaqeap ikkkrppvkd edlkgargnl tknqeikskt yqvmreceqa gsaapsvfsr
       61 trtgtetvfe kpkagptksv fg
//
LOCUS       NP_060548                914 aa            linear   PRI 29-NOV-2025
DEFINITION  la-related protein 1B isoform 1 [Homo sapiens].
ACCESSION   NP_060548
VERSION     NP_060548.2
DBSOURCE    REFSEQ: accession NM_018078.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 914)
  AUTHORS   Werneck-de-Castro,J.P., Pecanha,F.L.M., Silvestre,D.H. and
            Bernal-Mizrachi,E.
  TITLE     The RNA-binding protein LARP1 is dispensable for pancreatic
            beta-cell function and mass
  JOURNAL   Sci Rep 11 (1), 2079 (2021)
   PUBMED   33483593
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 914)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 914)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 914)
  AUTHORS   Gao,T., Nie,Y. and Guo,J.
  TITLE     Hypermethylation of the gene LARP2 for noninvasive prenatal
            diagnosis of beta-thalassemia based on DNA methylation profile
  JOURNAL   Mol Biol Rep 39 (6), 6591-6598 (2012)
   PUBMED   22327645
  REMARK    GeneRIF: The promoter of the gene of La ribonucleoprotein domain
            family (LARP2) was significantly hypermethylated in
            beta-thalassemia, and the expression of LARP2 was significantly
            lower in beta-thalassemia.
REFERENCE   5  (residues 1 to 914)
  AUTHORS   Orvedahl,A., Sumpter,R. Jr., Xiao,G., Ng,A., Zou,Z., Tang,Y.,
            Narimatsu,M., Gilpin,C., Sun,Q., Roth,M., Forst,C.V., Wrana,J.L.,
            Zhang,Y.E., Luby-Phelps,K., Xavier,R.J., Xie,Y. and Levine,B.
  TITLE     Image-based genome-wide siRNA screen identifies selective autophagy
            factors
  JOURNAL   Nature 480 (7375), 113-117 (2011)
   PUBMED   22020285
REFERENCE   6  (residues 1 to 914)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   7  (residues 1 to 914)
  AUTHORS   Wolin,S.L. and Cedervall,T.
  TITLE     The La protein
  JOURNAL   Annu Rev Biochem 71, 375-403 (2002)
   PUBMED   12045101
  REMARK    GeneRIF: Review discusses the La motif, found in this protein.
            Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA181086.1, DB230609.1,
            AK092764.1, AL137759.1, AK027164.1, AI374914.1 and AC096898.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 23, 2003 this sequence version replaced NP_060548.1.
            
            Summary: This gene encodes a protein containing domains found in
            the La related protein of Drosophila melanogaster. La
            motif-containing proteins are thought to be RNA-binding proteins,
            where the La motif and adjacent amino acids fold into an RNA
            recognition motif. The La motif is also found in proteins unrelated
            to the La protein. Alternative splicing has been observed at this
            locus and multiple variants, encoding distinct isoforms, are
            described. Additional splice variation has been identified but the
            full-length nature of these transcripts has not been determined.
            [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA1970526 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000326639.11/ ENSP00000321997.6
            RefSeq Select criteria    :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..914
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.2"
     Protein         1..914
                     /product="la-related protein 1B isoform 1"
                     /note="La ribonucleoprotein domain family, member 2;
                     la-related protein 1B; La ribonucleoprotein domain family
                     member 1B; la-related protein 2"
                     /calculated_mol_wt=105192
     Region          1..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Region          <110..>280
                     /region_name="LHP1"
                     /note="La protein, small RNA-binding pol III transcript
                     stabilizing protein and related La-motif-containing
                     proteins involved in translation [Posttranslational
                     modification, protein turnover, chaperones / Translation,
                     ribosomal structure and biogenesis]; COG5193"
                     /db_xref="CDD:227520"
     Region          216..288
                     /region_name="LARP_2"
                     /note="La RNA-binding domain of La-related protein 2;
                     cd08038"
                     /db_xref="CDD:153407"
     Site            order(222,225..226,231,234..235,237,256..258)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153407"
     Region          327..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Region          590..681
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q659C4.2)"
     Region          707..747
                     /region_name="DM15"
                     /note="Tandem repeat in fly CG14066 (La related protein),
                     human KIAA0731 and worm R144.7. Unknown function;
                     smart00684"
                     /db_xref="CDD:128927"
     Region          748..786
                     /region_name="DM15"
                     /note="Tandem repeat in fly CG14066 (La related protein),
                     human KIAA0731 and worm R144.7. Unknown function;
                     smart00684"
                     /db_xref="CDD:128927"
     Region          852..914
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q659C4.2)"
     CDS             1..914
                     /gene="LARP1B"
                     /gene_synonym="LARP2"
                     /coded_by="NM_018078.4:168..2912"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3738.1"
                     /db_xref="GeneID:55132"
                     /db_xref="HGNC:HGNC:24704"
                     /db_xref="MIM:620467"
ORIGIN      
        1 menwptpsel vntgfqsvls qgnkkpqnrk ekeekvekrs nsdskenret klngpgenvs
       61 edeaqssnqr krankhkwvp lhldvvrses qerpgsrnss rcqpeankpt hnnrrndtrs
      121 wkrdrekrdd qddvssvrse ggnirgsfrg rgrgrgrgrg rgrgnprlnf dysygyqehg
      181 ertdqpfqte lntsmmyyyd dgtgvqvypv eeallkeyik rqieyyfsve nlerdfflrg
      241 kmdeqgflpi sliagfqrvq alttnlnlil ealkdsteve ivdekmrkki epekwpipgp
      301 pprsvpptdf sqlidcpefv pgqafcshte sapnsprigs plspkknset silqamsrgl
      361 stslpdldse pwievkkrhq papvklresv svpegslnql csseepeqee ldflfdeeie
      421 qigrkntftd wsdndsdyei ddqdlnkili vtqtppyvkk hpggdrtgth msrakitsel
      481 akvindglyy yeqdlwmeed enkhtaikqe venfkklnli skeqfenltp elpfepnqev
      541 pvapsqsrqg gvqgvlhipk kdltdelaqk lfdvseitsa amvhslptav pesprihptr
      601 tpktprtprl qdpnktprfy pvvkepkaid vksprkrktr hstnpplech vgwvmdsrdr
      661 gpgtssvsts naspsegapl agsygctphs fpkfqhpshe llkengftqq vyhkyrrrcl
      721 serkrlgigq sqemntlfrf wsfflrdhfn kkmyeefrql awedakenyr ygleclfrfy
      781 syglekkfrr eifqdfqeet kkdyesgqly glekfwaylk ysqsktqsid pklqeylcsf
      841 krledfrvdp pisdefgrkr hsstsgeesn rhrlppnsst kppnaakpts tselqvpins
      901 prrnispess dnsh
//
LOCUS       NP_001337460             634 aa            linear   PRI 29-NOV-2025
DEFINITION  la-related protein 1B isoform 5 [Homo sapiens].
ACCESSION   NP_001337460 XP_016863840
VERSION     NP_001337460.1
DBSOURCE    REFSEQ: accession NM_001350531.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Werneck-de-Castro,J.P., Pecanha,F.L.M., Silvestre,D.H. and
            Bernal-Mizrachi,E.
  TITLE     The RNA-binding protein LARP1 is dispensable for pancreatic
            beta-cell function and mass
  JOURNAL   Sci Rep 11 (1), 2079 (2021)
   PUBMED   33483593
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 634)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 634)
  AUTHORS   Gao,T., Nie,Y. and Guo,J.
  TITLE     Hypermethylation of the gene LARP2 for noninvasive prenatal
            diagnosis of beta-thalassemia based on DNA methylation profile
  JOURNAL   Mol Biol Rep 39 (6), 6591-6598 (2012)
   PUBMED   22327645
  REMARK    GeneRIF: The promoter of the gene of La ribonucleoprotein domain
            family (LARP2) was significantly hypermethylated in
            beta-thalassemia, and the expression of LARP2 was significantly
            lower in beta-thalassemia.
REFERENCE   5  (residues 1 to 634)
  AUTHORS   Orvedahl,A., Sumpter,R. Jr., Xiao,G., Ng,A., Zou,Z., Tang,Y.,
            Narimatsu,M., Gilpin,C., Sun,Q., Roth,M., Forst,C.V., Wrana,J.L.,
            Zhang,Y.E., Luby-Phelps,K., Xavier,R.J., Xie,Y. and Levine,B.
  TITLE     Image-based genome-wide siRNA screen identifies selective autophagy
            factors
  JOURNAL   Nature 480 (7375), 113-117 (2011)
   PUBMED   22020285
REFERENCE   6  (residues 1 to 634)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   7  (residues 1 to 634)
  AUTHORS   Wolin,S.L. and Cedervall,T.
  TITLE     The La protein
  JOURNAL   Annu Rev Biochem 71, 375-403 (2002)
   PUBMED   12045101
  REMARK    GeneRIF: Review discusses the La motif, found in this protein.
            Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK092764.1, BC018794.1,
            AL137759.1, BX537937.1, AK027164.1, AC096898.6 and BX103089.1.
            
            On Apr 20, 2017 this sequence version replaced XP_016863840.1.
            
            Summary: This gene encodes a protein containing domains found in
            the La related protein of Drosophila melanogaster. La
            motif-containing proteins are thought to be RNA-binding proteins,
            where the La motif and adjacent amino acids fold into an RNA
            recognition motif. The La motif is also found in proteins unrelated
            to the La protein. Alternative splicing has been observed at this
            locus and multiple variants, encoding distinct isoforms, are
            described. Additional splice variation has been identified but the
            full-length nature of these transcripts has not been determined.
            [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (5) differs in the 5' UTR,
            contains multiple coding region differences and uses a downstream
            start codon, compared to variant 1. It encodes isoform 5, which is
            shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.183228.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.2"
     Protein         1..634
                     /product="la-related protein 1B isoform 5"
                     /note="La ribonucleoprotein domain family, member 2;
                     la-related protein 1B; La ribonucleoprotein domain family
                     member 1B; la-related protein 2"
                     /calculated_mol_wt=72896
     Region          <1..47
                     /region_name="LAM"
                     /note="LA motif RNA-binding domain; cl02755"
                     /db_xref="CDD:470666"
     Region          427..467
                     /region_name="DM15"
                     /note="Tandem repeat in fly CG14066 (La related protein),
                     human KIAA0731 and worm R144.7. Unknown function;
                     smart00684"
                     /db_xref="CDD:128927"
     Region          468..506
                     /region_name="DM15"
                     /note="Tandem repeat in fly CG14066 (La related protein),
                     human KIAA0731 and worm R144.7. Unknown function;
                     smart00684"
                     /db_xref="CDD:128927"
     CDS             1..634
                     /gene="LARP1B"
                     /gene_synonym="LARP2"
                     /coded_by="NM_001350531.2:584..2488"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:55132"
                     /db_xref="HGNC:HGNC:24704"
                     /db_xref="MIM:620467"
ORIGIN      
        1 mdeqgflpis liagfqrvqa lttnlnlile alkdstevei vdekmrkkie pekwpipgpp
       61 prsvpptdfs qlidcpefvp gqafcshtes apnsprigsp lspkknsets ilqamsrgls
      121 tslpdldsep wievkkrhqp apvklresvs vpegslnqlc sseepeqeel dflfdeeieq
      181 igrkntftdw sdndsdyeid dqdlnkiliv tqtppyvkkh pggdrtgthm srakitsela
      241 kvindglyyy eqdlwmeede nkhtaikqev enfkklnlis keqfenltpe lpfepnqevp
      301 vapsqsrqav pesprihptr tpktprtprl qdpnktprfy pvvkepkaid vksprkrktr
      361 hstnpplech vgwvmdsrdr gpgtssvsts naspsegapl agsygctphs fpkfqhpshe
      421 llkengftqq vyhkyrrrcl serkrlgigq sqemntlfrf wsfflrdhfn kkmyeefrql
      481 awedakenyr ygleclfrfy syglekkfrr eifqdfqeet kkdyesgqly glekfwaylk
      541 ysqsktqsid pklqeylcsf krledfrvdp pisdefgrkr hsstsgeesn rhrlppnsst
      601 kppnaakpts tselqvpins prrnispess dnsh
//
LOCUS       NP_000465                202 aa            linear   PRI 29-NOV-2025
DEFINITION  twist-related protein 1 [Homo sapiens].
ACCESSION   NP_000465
VERSION     NP_000465.1
DBSOURCE    REFSEQ: accession NM_000474.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Geister,E., Ard,D., Patel,H., Findley,A., DeSouza,G., Martin,L.,
            Knox,H., Gavara,N., Lugea,A. and Sabbatini,M.E.
  TITLE     The Role of Twist1 in Chronic Pancreatitis-Associated Pancreatic
            Stellate Cells
  JOURNAL   Am J Pathol 194 (10), 1879-1897 (2024)
   PUBMED   39032603
  REMARK    GeneRIF: The Role of Twist1 in Chronic Pancreatitis-Associated
            Pancreatic Stellate Cells.
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Peng,X., Ma,L., Chen,X., Tang,F. and Zong,X.
  TITLE     Inhibition of FBP1 expression by KMT5A through TWIST1 methylation
            is one of the mechanisms leading to chemoresistance in breast
            cancer
  JOURNAL   Oncol Rep 52 (2) (2024)
   PUBMED   38963044
  REMARK    GeneRIF: Inhibition of FBP1 expression by KMT5A through TWIST1
            methylation is one of the mechanisms leading to chemoresistance in
            breast cancer.
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Zhang,Y., Wang,J., Sun,H., Xun,Z., He,Z., Zhao,Y., Qi,J., Sun,S.,
            Yang,Q., Gu,Y., Zhang,L., Zhou,C., Ye,Y., Wu,N., Zou,D. and Su,B.
  TITLE     TWIST1+FAP+ fibroblasts in the pathogenesis of intestinal fibrosis
            in Crohn's disease
  JOURNAL   J Clin Invest 134 (18), e179472 (2024)
   PUBMED   39024569
  REMARK    GeneRIF: TWIST1+FAP+ fibroblasts in the pathogenesis of intestinal
            fibrosis in Crohn's disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Dvorak,O., Slavickova,M., Laco,J., Stepan,M., Cermakova,E. and
            Spacek,J.
  TITLE     DNA hypermethylation of tumor suppressor genes TWIST1, GATA4, MUS81
            and NTRK1 in endometrial hyperplasia
  JOURNAL   Ceska Gynekol 89 (4), 261-268 (2024)
   PUBMED   39242200
  REMARK    GeneRIF: DNA hypermethylation of tumor suppressor genes TWIST1,
            GATA4, MUS81 and NTRK1 in endometrial hyperplasia.
REFERENCE   5  (residues 1 to 202)
  AUTHORS   Zhao,Z., Rahman,M.A., Chen,Z.G. and Shin,D.M.
  TITLE     Multiple biological functions of Twist1 in various cancers
  JOURNAL   Oncotarget 8 (12), 20380-20393 (2017)
   PUBMED   28099910
  REMARK    Review article
REFERENCE   6  (residues 1 to 202)
  AUTHORS   Wang,S.M., Coljee,V.W., Pignolo,R.J., Rotenberg,M.O.,
            Cristofalo,V.J. and Sierra,F.
  TITLE     Cloning of the human twist gene: its expression is retained in
            adult mesodermally-derived tissues
  JOURNAL   Gene 187 (1), 83-92 (1997)
   PUBMED   9073070
REFERENCE   7  (residues 1 to 202)
  AUTHORS   el Ghouzzi,V., Le Merrer,M., Perrin-Schmitt,F., Lajeunie,E.,
            Benit,P., Renier,D., Bourgeois,P., Bolcato-Bellemin,A.L.,
            Munnich,A. and Bonaventure,J.
  TITLE     Mutations of the TWIST gene in the Saethre-Chotzen syndrome
  JOURNAL   Nat Genet 15 (1), 42-46 (1997)
   PUBMED   8988167
REFERENCE   8  (residues 1 to 202)
  AUTHORS   Howard,T.D., Paznekas,W.A., Green,E.D., Chiang,L.C., Ma,N., Ortiz
            de Luna,R.I., Garcia Delgado,C., Gonzalez-Ramos,M., Kline,A.D. and
            Jabs,E.W.
  TITLE     Mutations in TWIST, a basic helix-loop-helix transcription factor,
            in Saethre-Chotzen syndrome
  JOURNAL   Nat Genet 15 (1), 36-41 (1997)
   PUBMED   8988166
REFERENCE   9  (residues 1 to 202)
  AUTHORS   Bourgeois,P., Stoetzel,C., Bolcato-Bellemin,A.L., Mattei,M.G. and
            Perrin-Schmitt,F.
  TITLE     The human H-twist gene is located at 7p21 and encodes a B-HLH
            protein that is 96% similar to its murine M-twist counterpart
  JOURNAL   Mamm Genome 7 (12), 915-917 (1996)
   PUBMED   8995765
REFERENCE   10 (residues 1 to 202)
  AUTHORS   Gallagher,E.R., Ratisoontorn,C. and Cunningham,M.L.
  TITLE     Saethre-Chotzen Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC036704.2 and AW173505.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a basic helix-loop-helix (bHLH)
            transcription factor that plays an important role in embryonic
            development. The encoded protein forms both homodimers and
            heterodimers that bind to DNA E box sequences and regulate the
            transcription of genes involved in cranial suture closure during
            skull development. This protein may also regulate neural tube
            closure, limb development and brown fat metabolism. This gene is
            hypermethylated and overexpressed in multiple human cancers, and
            the encoded protein promotes tumor cell invasion and metastasis, as
            well as metastatic recurrence. Mutations in this gene cause
            Saethre-Chotzen syndrome in human patients, which is characterized
            by craniosynostosis, ptosis and hypertelorism. [provided by RefSeq,
            Jul 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X99268.1, BC036704.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2467147
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000242261.6/ ENSP00000242261.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p21.1"
     Protein         1..202
                     /product="twist-related protein 1"
                     /note="twist homolog 1; twist basic helix-loop-helix
                     transcription factor 1; H-twist; TWIST homolog of
                     drosophila; B-HLH DNA binding protein; class A basic
                     helix-loop-helix protein 38"
                     /calculated_mol_wt=20823
     Region          1..105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15672.1)"
     Region          98..174
                     /region_name="bHLH_TS_TWIST1"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     twist-related protein 1 (TWIST1) and similar proteins;
                     cd11412"
                     /db_xref="CDD:381418"
     Site            order(110,114,116..118,120,125,142..145)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381418"
     Site            order(123..124,127..128,130..131,146,149,153,155..156,160,
                     162..163)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381418"
     Region          161..191
                     /region_name="Sufficient for transactivation activity.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15672.1)"
     CDS             1..202
                     /gene="TWIST1"
                     /gene_synonym="ACS3; bHLHa38; BPES2; BPES3; CRS; CRS1;
                     CSO; SCS; SWCOS; TWIST"
                     /coded_by="NM_000474.4:316..924"
                     /db_xref="CCDS:CCDS5367.1"
                     /db_xref="GeneID:7291"
                     /db_xref="HGNC:HGNC:12428"
                     /db_xref="MIM:601622"
ORIGIN      
        1 mmqdvssspv spaddslsns eeepdrqqpp sgkrggrkrr ssrrsaggga gpggaagggv
       61 gggdepgspa qgkrgkksag cgggggaggg ggsssgggsp qsyeelqtqr vmanvrerqr
      121 tqslneafaa lrkiiptlps dklskiqtlk laaryidfly qvlqsdelds kmascsyvah
      181 erlsyafsvw rmegawsmsa sh
//
LOCUS       NP_078836                686 aa            linear   PRI 29-NOV-2025
DEFINITION  acyl-CoA synthetase short-chain family member 3, mitochondrial
            isoform 1 precursor [Homo sapiens].
ACCESSION   NP_078836
VERSION     NP_078836.1
DBSOURCE    REFSEQ: accession NM_024560.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Huo,P., Wang,S., Li,Z. and Jin,Z.
  TITLE     ACSS3 protein macromolecule regulates glycolysis in keloid through
            Wnt/beta-catenin signaling pathway: Bioinformatics, machine
            learning, and experimental validation
  JOURNAL   Cell Signal 135, 112056 (2025)
   PUBMED   40783148
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Wang,L., Yuan,H., Li,W., Yan,P., Zhao,M., Li,Z., Zhao,H., Wang,S.,
            Wan,R., Li,Y., Yang,J., Pan,X., Rosas,I. and Yu,G.
  TITLE     ACSS3 regulates the metabolic homeostasis of epithelial cells and
            alleviates pulmonary fibrosis
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (2), 166960 (2024)
   PUBMED   37979225
  REMARK    GeneRIF: ACSS3 regulates the metabolic homeostasis of epithelial
            cells and alleviates pulmonary fibrosis.
REFERENCE   3  (residues 1 to 686)
  AUTHORS   Jo,J., Song,Y., Yoon,D., Lee,C.G. and Won,S.
  TITLE     Genome-wide assessment reveals a significant association between
            ACSS3 and physical activity
  JOURNAL   Genes Brain Behav 22 (1), e12834 (2023)
   PUBMED   36510703
  REMARK    GeneRIF: Genome-wide assessment reveals a significant association
            between ACSS3 and physical activity.
REFERENCE   4  (residues 1 to 686)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 686)
  AUTHORS   Zhou,L., Song,Z., Hu,J., Liu,L., Hou,Y., Zhang,X., Yang,X. and
            Chen,K.
  TITLE     ACSS3 represses prostate cancer progression through downregulating
            lipid droplet-associated protein PLIN3
  JOURNAL   Theranostics 11 (2), 841-860 (2021)
   PUBMED   33391508
  REMARK    GeneRIF: ACSS3 represses prostate cancer progression through
            downregulating lipid droplet-associated protein PLIN3.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 686)
  AUTHORS   Yoshimura,Y., Araki,A., Maruta,H., Takahashi,Y. and Yamashita,H.
  TITLE     Molecular cloning of rat acss3 and characterization of mammalian
            propionyl-CoA synthetase in the liver mitochondrial matrix
  JOURNAL   J Biochem 161 (3), 279-289 (2017)
   PUBMED   28003429
REFERENCE   7  (residues 1 to 686)
  AUTHORS   Chouraki,V., De Bruijn,R.F., Chapuis,J., Bis,J.C., Reitz,C.,
            Schraen,S., Ibrahim-Verbaas,C.A., Grenier-Boley,B., Delay,C.,
            Rogers,R., Demiautte,F., Mounier,A., Fitzpatrick,A.L., Berr,C.,
            Dartigues,J.F., Uitterlinden,A.G., Hofman,A., Breteler,M.,
            Becker,J.T., Lathrop,M., Schupf,N., Alperovitch,A., Mayeux,R., van
            Duijn,C.M., Buee,L., Amouyel,P., Lopez,O.L., Ikram,M.A., Tzourio,C.
            and Lambert,J.C.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative
  TITLE     A genome-wide association meta-analysis of plasma Abeta peptides
            concentrations in the elderly
  JOURNAL   Mol Psychiatry 19 (12), 1326-1335 (2014)
   PUBMED   24535457
REFERENCE   8  (residues 1 to 686)
  AUTHORS   Ritchie,M.D., Verma,S.S., Hall,M.A., Goodloe,R.J., Berg,R.L.,
            Carrell,D.S., Carlson,C.S., Chen,L., Crosslin,D.R., Denny,J.C.,
            Jarvik,G., Li,R., Linneman,J.G., Pathak,J., Peissig,P.,
            Rasmussen,L.V., Ramirez,A.H., Wang,X., Wilke,R.A., Wolf,W.A.,
            Torstenson,E.S., Turner,S.D. and McCarty,C.A.
  TITLE     Electronic medical records and genomics (eMERGE) network
            exploration in cataract: several new potential susceptibility loci
  JOURNAL   Mol Vis 20, 1281-1295 (2014)
   PUBMED   25352737
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 686)
  AUTHORS   Hunter,A.M., Leuchter,A.F., Power,R.A., Muthen,B., McGrath,P.J.,
            Lewis,C.M., Cook,I.A., Garriock,H.A., McGuffin,P., Uher,R. and
            Hamilton,S.P.
  TITLE     A genome-wide association study of a sustained pattern of
            antidepressant response
  JOURNAL   J Psychiatr Res 47 (9), 1157-1165 (2013)
   PUBMED   23726668
REFERENCE   10 (residues 1 to 686)
  AUTHORS   Watkins,P.A., Maiguel,D., Jia,Z. and Pevsner,J.
  TITLE     Evidence for 26 distinct acyl-coenzyme A synthetase genes in the
            human genome
  JOURNAL   J Lipid Res 48 (12), 2736-2750 (2007)
   PUBMED   17762044
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK025616.1, AK074938.1, AK074267.1, AC078920.17 and AI022900.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK025616.1, SRR1803612.162160.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000548058.6/ ENSP00000449535.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.31"
     Protein         1..686
                     /product="acyl-CoA synthetase short-chain family member 3,
                     mitochondrial isoform 1 precursor"
                     /EC_number="6.2.1.1"
                     /EC_number="6.2.1.17"
                     /note="acyl-CoA synthetase short-chain family member 3,
                     mitochondrial; AMP-binding enzyme, 33217; acetate--CoA
                     ligase 3; propionate--CoA ligase"
                     /calculated_mol_wt=71900
     transit_peptide 1..29
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9H6R3.1)"
                     /calculated_mol_wt=2896
     mat_peptide     30..686
                     /product="Acyl-CoA synthetase short-chain family member 3,
                     mitochondrial. /id=PRO_0000320624"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6R3.1)"
                     /calculated_mol_wt=71900
     Region          62..679
                     /region_name="PrpE"
                     /note="Propionyl-CoA synthetase (PrpE); cd05967"
                     /db_xref="CDD:341271"
     Site            order(296,299..304,306..307)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341271"
     Site            order(299,424..425,446..451,539,551,554,565,649)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341271"
     Site            order(299,340..341,393,395..396,399,424..425,446..451,539,
                     551,554,562..565,630)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341271"
     Site            order(340,395..396,399,424,562..564,624,630)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341271"
     Site            524
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q14DH7; propagated from
                     UniProtKB/Swiss-Prot (Q9H6R3.1)"
     CDS             1..686
                     /gene="ACSS3"
                     /coded_by="NM_024560.4:43..2103"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS9022.1"
                     /db_xref="GeneID:79611"
                     /db_xref="HGNC:HGNC:24723"
                     /db_xref="MIM:614356"
ORIGIN      
        1 mkpswlqcrk vtsagglggp lpgssparga gaalralvvp gprgglggrg cralssgsgs
       61 eykthfaasv tdperfwgka aeqiswykpw tktlenkhsp strwfvegml nicynavdrh
      121 iengkgdkia iiydspvtnt katftykevl eqvsklagvl vkhgikkgdt vviympmipq
      181 amytmlacar igaihslifg gfaskelssr idhvkpkvvv tasfgiepgr rveyvplvee
      241 alkigqhkpd kiliynrpnm eavplapgrd ldwdeemaka qshdcvpvls ehplyilyts
      301 gttglpkgvi rptggyavml hwsmssiygl qpgevwwaas dlgwvvghsy icygpllhgn
      361 ttvlyegkpv gtpdagayfr vlaehgvaal ftaptairai rqqdpgaalg kqysltrfkt
      421 lfvagercdv etlewsknvf rvpvldhwwq tetgspitas cvglgnsktp ppgqagksvp
      481 gynvmilddn mqklkarclg nivvklplpp gafsglwknq eafkhlyfek fpgyydtmda
      541 gymdeegyly vmsrvddvin vaghrisaga ieesilshgt vadcavvgke dplkghvpla
      601 lcvlrkdina teeqvleeiv khvrqnigpv aafrnavfvk qlpktrsgki prsalsaivn
      661 gkpykitsti edpsifghve emlkqa
//
LOCUS       NP_001397715             902 aa            linear   PRI 29-NOV-2025
DEFINITION  la-related protein 1B isoform 6 [Homo sapiens].
ACCESSION   NP_001397715 XP_016863833
VERSION     NP_001397715.1
DBSOURCE    REFSEQ: accession NM_001410786.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 902)
  AUTHORS   Werneck-de-Castro,J.P., Pecanha,F.L.M., Silvestre,D.H. and
            Bernal-Mizrachi,E.
  TITLE     The RNA-binding protein LARP1 is dispensable for pancreatic
            beta-cell function and mass
  JOURNAL   Sci Rep 11 (1), 2079 (2021)
   PUBMED   33483593
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 902)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 902)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 902)
  AUTHORS   Gao,T., Nie,Y. and Guo,J.
  TITLE     Hypermethylation of the gene LARP2 for noninvasive prenatal
            diagnosis of beta-thalassemia based on DNA methylation profile
  JOURNAL   Mol Biol Rep 39 (6), 6591-6598 (2012)
   PUBMED   22327645
  REMARK    GeneRIF: The promoter of the gene of La ribonucleoprotein domain
            family (LARP2) was significantly hypermethylated in
            beta-thalassemia, and the expression of LARP2 was significantly
            lower in beta-thalassemia.
REFERENCE   5  (residues 1 to 902)
  AUTHORS   Orvedahl,A., Sumpter,R. Jr., Xiao,G., Ng,A., Zou,Z., Tang,Y.,
            Narimatsu,M., Gilpin,C., Sun,Q., Roth,M., Forst,C.V., Wrana,J.L.,
            Zhang,Y.E., Luby-Phelps,K., Xavier,R.J., Xie,Y. and Levine,B.
  TITLE     Image-based genome-wide siRNA screen identifies selective autophagy
            factors
  JOURNAL   Nature 480 (7375), 113-117 (2011)
   PUBMED   22020285
REFERENCE   6  (residues 1 to 902)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   7  (residues 1 to 902)
  AUTHORS   Wolin,S.L. and Cedervall,T.
  TITLE     The La protein
  JOURNAL   Annu Rev Biochem 71, 375-403 (2002)
   PUBMED   12045101
  REMARK    GeneRIF: Review discusses the La motif, found in this protein.
            Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099340.3, AC108045.3,
            AC114735.4, AC124030.4 and AC096898.6.
            
            On Aug 16, 2022 this sequence version replaced XP_016863833.1.
            
            Summary: This gene encodes a protein containing domains found in
            the La related protein of Drosophila melanogaster. La
            motif-containing proteins are thought to be RNA-binding proteins,
            where the La motif and adjacent amino acids fold into an RNA
            recognition motif. The La motif is also found in proteins unrelated
            to the La protein. Alternative splicing has been observed at this
            locus and multiple variants, encoding distinct isoforms, are
            described. Additional splice variation has been identified but the
            full-length nature of these transcripts has not been determined.
            [provided by RefSeq, Jun 2013].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.120093.1,
                                           SRR1803611.129552.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.2"
     Protein         1..902
                     /product="la-related protein 1B isoform 6"
                     /note="La ribonucleoprotein domain family, member 2;
                     la-related protein 1B; La ribonucleoprotein domain family
                     member 1B; la-related protein 2"
                     /calculated_mol_wt=103977
     Region          1..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Region          <110..>280
                     /region_name="LHP1"
                     /note="La protein, small RNA-binding pol III transcript
                     stabilizing protein and related La-motif-containing
                     proteins involved in translation [Posttranslational
                     modification, protein turnover, chaperones / Translation,
                     ribosomal structure and biogenesis]; COG5193"
                     /db_xref="CDD:227520"
     Region          216..288
                     /region_name="LAM"
                     /note="LA motif RNA-binding domain; cl02755"
                     /db_xref="CDD:470666"
     Site            order(222,225..226,231,234..235,237,256..258)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153407"
     Region          327..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q659C4.2)"
     Region          578..669
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q659C4.2)"
     Region          695..735
                     /region_name="DM15"
                     /note="Tandem repeat in fly CG14066 (La related protein),
                     human KIAA0731 and worm R144.7. Unknown function;
                     smart00684"
                     /db_xref="CDD:128927"
     Region          736..774
                     /region_name="DM15"
                     /note="Tandem repeat in fly CG14066 (La related protein),
                     human KIAA0731 and worm R144.7. Unknown function;
                     smart00684"
                     /db_xref="CDD:128927"
     Region          840..902
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q659C4.2)"
     CDS             1..902
                     /gene="LARP1B"
                     /gene_synonym="LARP2"
                     /coded_by="NM_001410786.1:515..3223"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS93633.1"
                     /db_xref="GeneID:55132"
                     /db_xref="HGNC:HGNC:24704"
                     /db_xref="MIM:620467"
ORIGIN      
        1 menwptpsel vntgfqsvls qgnkkpqnrk ekeekvekrs nsdskenret klngpgenvs
       61 edeaqssnqr krankhkwvp lhldvvrses qerpgsrnss rcqpeankpt hnnrrndtrs
      121 wkrdrekrdd qddvssvrse ggnirgsfrg rgrgrgrgrg rgrgnprlnf dysygyqehg
      181 ertdqpfqte lntsmmyyyd dgtgvqvypv eeallkeyik rqieyyfsve nlerdfflrg
      241 kmdeqgflpi sliagfqrvq alttnlnlil ealkdsteve ivdekmrkki epekwpipgp
      301 pprsvpptdf sqlidcpefv pgqafcshte sapnsprigs plspkknset silqamsrgl
      361 stslpdldse pwievkkrhq papvklresv svpegslnql csseepeqee ldflfdeeie
      421 qigrkntftd wsdndsdyei ddqdlnkili vtqtppyvkk hpggdrtgth msrakitsel
      481 akvindglyy yeqdlwmeed enkhtaikqe venfkklnli skeqfenltp elpfepnqev
      541 pvapsqsrqd ltdelaqklf dvseitsaam vhslptavpe sprihptrtp ktprtprlqd
      601 pnktprfypv vkepkaidvk sprkrktrhs tnpplechvg wvmdsrdrgp gtssvstsna
      661 spsegaplag sygctphsfp kfqhpshell kengftqqvy hkyrrrclse rkrlgigqsq
      721 emntlfrfws fflrdhfnkk myeefrqlaw edakenyryg leclfrfysy glekkfrrei
      781 fqdfqeetkk dyesgqlygl ekfwaylkys qsktqsidpk lqeylcsfkr ledfrvdppi
      841 sdefgrkrhs stsgeesnrh rlppnsstkp pnaakptsts elqvpinspr rnispessdn
      901 sh
//
LOCUS       NP_060275                963 aa            linear   PRI 29-NOV-2025
DEFINITION  ras-interacting protein 1 [Homo sapiens].
ACCESSION   NP_060275
VERSION     NP_060275.2
DBSOURCE    REFSEQ: accession NM_017805.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 963)
  AUTHORS   Yin,J., Schellinx,N., Maggi,L., Gundel,K., Wiesner,C., Kotini,M.P.,
            Lee,M., Phng,L.K., Belting,H.G. and Affolter,M.
  TITLE     Initiation of lumen formation from junctions via differential
            actomyosin contractility regulated by dynamic recruitment of Rasip1
  JOURNAL   Nat Commun 15 (1), 9714 (2024)
   PUBMED   39521779
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 963)
  AUTHORS   Xing,X., Wang,X., Liu,M., Guo,Q. and Wang,H.
  TITLE     Ras interacting protein 1 facilitated proliferation and invasion of
            diffuse large B-cell lymphoma cells
  JOURNAL   Cancer Biol Ther 24 (1), 2193114 (2023)
   PUBMED   36967521
  REMARK    GeneRIF: Ras interacting protein 1 facilitated proliferation and
            invasion of diffuse large B-cell lymphoma cells.
REFERENCE   3  (residues 1 to 963)
  AUTHORS   Rossi,T., Pistoni,M., Sancisi,V., Gobbi,G., Torricelli,F.,
            Donati,B., Ribisi,S., Gugnoni,M. and Ciarrocchi,A.
  TITLE     RAIN Is a Novel Enhancer-Associated lncRNA That Controls RUNX2
            Expression and Promotes Breast and Thyroid Cancer
  JOURNAL   Mol Cancer Res 18 (1), 140-152 (2020)
   PUBMED   31624086
  REMARK    GeneRIF: RAIN Is a Novel Enhancer-Associated lncRNA That Controls
            RUNX2 Expression and Promotes Breast and Thyroid Cancer.
REFERENCE   4  (residues 1 to 963)
  AUTHORS   Gingras,A.R., Puzon-McLaughlin,W., Bobkov,A.A. and Ginsberg,M.H.
  TITLE     Structural Basis of Dimeric Rasip1 RA Domain Recognition of the Ras
            Subfamily of GTP-Binding Proteins
  JOURNAL   Structure 24 (12), 2152-2162 (2016)
   PUBMED   27839947
  REMARK    GeneRIF: Results show that Rasip1 RA domain formed a dimer that can
            bind two Rap1 or Ras molecules and solved the Rap1-RRA complex and
            found that Rasip1 binds Rap1 in the Switch I region, and Rap1
            binding induces few conformation changes to Rasip1 stabilizing a
            beta strand and an unstructured loop.
REFERENCE   5  (residues 1 to 963)
  AUTHORS   de Kreuk,B.J., Gingras,A.R., Knight,J.D., Liu,J.J., Gingras,A.C.
            and Ginsberg,M.H.
  TITLE     Heart of glass anchors Rasip1 at endothelial cell-cell junctions to
            support vascular integrity
  JOURNAL   Elife 5, e11394 (2016)
   PUBMED   26780829
  REMARK    GeneRIF: These studies establish that the binding of HEG1 to Rasip1
            mediates Rap1-dependent recruitment of Rasip1 to and stabilization
            of endothelial cell cell-cell junctions.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 963)
  AUTHORS   McKnight,N.C., Jefferies,H.B., Alemu,E.A., Saunders,R.E.,
            Howell,M., Johansen,T. and Tooze,S.A.
  TITLE     Genome-wide siRNA screen reveals amino acid starvation-induced
            autophagy requires SCOC and WAC
  JOURNAL   EMBO J 31 (8), 1931-1946 (2012)
   PUBMED   22354037
REFERENCE   7  (residues 1 to 963)
  CONSRTM   Psychiatric GWAS Consortium Bipolar Disorder Working Group
  TITLE     Large-scale genome-wide association analysis of bipolar disorder
            identifies a new susceptibility locus near ODZ4
  JOURNAL   Nat Genet 43 (10), 977-983 (2011)
   PUBMED   21926972
  REMARK    Erratum:[Nat Genet. 2012 Sep;44(9):1072. Fullerton, Janice M
            [added]; Hyoun, Phil L [corrected to Lee, Phil H]; Meng, Fan Guo
            [corrected to Meng, Fan]]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 963)
  AUTHORS   Franke,A., McGovern,D.P., Barrett,J.C., Wang,K.,
            Radford-Smith,G.L., Ahmad,T., Lees,C.W., Balschun,T., Lee,J.,
            Roberts,R., Anderson,C.A., Bis,J.C., Bumpstead,S., Ellinghaus,D.,
            Festen,E.M., Georges,M., Green,T., Haritunians,T., Jostins,L.,
            Latiano,A., Mathew,C.G., Montgomery,G.W., Prescott,N.J.,
            Raychaudhuri,S., Rotter,J.I., Schumm,P., Sharma,Y., Simms,L.A.,
            Taylor,K.D., Whiteman,D., Wijmenga,C., Baldassano,R.N., Barclay,M.,
            Bayless,T.M., Brand,S., Buning,C., Cohen,A., Colombel,J.F.,
            Cottone,M., Stronati,L., Denson,T., De Vos,M., D'Inca,R.,
            Dubinsky,M., Edwards,C., Florin,T., Franchimont,D., Gearry,R.,
            Glas,J., Van Gossum,A., Guthery,S.L., Halfvarson,J.,
            Verspaget,H.W., Hugot,J.P., Karban,A., Laukens,D., Lawrance,I.,
            Lemann,M., Levine,A., Libioulle,C., Louis,E., Mowat,C., Newman,W.,
            Panes,J., Phillips,A., Proctor,D.D., Regueiro,M., Russell,R.,
            Rutgeerts,P., Sanderson,J., Sans,M., Seibold,F., Steinhart,A.H.,
            Stokkers,P.C., Torkvist,L., Kullak-Ublick,G., Wilson,D.,
            Walters,T., Targan,S.R., Brant,S.R., Rioux,J.D., D'Amato,M.,
            Weersma,R.K., Kugathasan,S., Griffiths,A.M., Mansfield,J.C.,
            Vermeire,S., Duerr,R.H., Silverberg,M.S., Satsangi,J.,
            Schreiber,S., Cho,J.H., Annese,V., Hakonarson,H., Daly,M.J. and
            Parkes,M.
  TITLE     Genome-wide meta-analysis increases to 71 the number of confirmed
            Crohn's disease susceptibility loci
  JOURNAL   Nat Genet 42 (12), 1118-1125 (2010)
   PUBMED   21102463
REFERENCE   9  (residues 1 to 963)
  AUTHORS   Ikram,M.K., Sim,X., Jensen,R.A., Cotch,M.F., Hewitt,A.W.,
            Ikram,M.A., Wang,J.J., Klein,R., Klein,B.E., Breteler,M.M.,
            Cheung,N., Liew,G., Mitchell,P., Uitterlinden,A.G., Rivadeneira,F.,
            Hofman,A., de Jong,P.T., van Duijn,C.M., Kao,L., Cheng,C.Y.,
            Smith,A.V., Glazer,N.L., Lumley,T., McKnight,B., Psaty,B.M.,
            Jonasson,F., Eiriksdottir,G., Aspelund,T., Harris,T.B.,
            Launer,L.J., Taylor,K.D., Li,X., Iyengar,S.K., Xi,Q.,
            Sivakumaran,T.A., Mackey,D.A., Macgregor,S., Martin,N.G.,
            Young,T.L., Bis,J.C., Wiggins,K.L., Heckbert,S.R., Hammond,C.J.,
            Andrew,T., Fahy,S., Attia,J., Holliday,E.G., Scott,R.J.,
            Islam,F.M., Rotter,J.I., McAuley,A.K., Boerwinkle,E., Tai,E.S.,
            Gudnason,V., Siscovick,D.S., Vingerling,J.R. and Wong,T.Y.
  CONSRTM   Global BPgen Consortium
  TITLE     Four novel Loci (19q13, 6q24, 12q24, and 5q14) influence the
            microcirculation in vivo
  JOURNAL   PLoS Genet 6 (10), e1001184 (2010)
   PUBMED   21060863
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
            Erratum:[PLoS Genet. 2010;6(11). doi:
            10.1371/annotation/841bfadf-85d1-4059-894f-2863d73fa963. Xueling,
            Sim [corrected to Sim, Xueling]]
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 963)
  AUTHORS   Mitin,N.Y., Ramocki,M.B., Zullo,A.J., Der,C.J., Konieczny,S.F. and
            Taparowsky,E.J.
  TITLE     Identification and characterization of rain, a novel
            Ras-interacting protein with a unique subcellular localization
  JOURNAL   J Biol Chem 279 (21), 22353-22361 (2004)
   PUBMED   15031288
  REMARK    GeneRIF: Rain is a novel protein that can serve as an effector of
            endomembrane-localized Ras
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC042111.1, BC028614.1 and BC021860.1.
            
            On Dec 1, 2003 this sequence version replaced NP_060275.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028614.1, AY378097.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222145.9/ ENSP00000222145.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..963
                     /product="ras-interacting protein 1"
                     /calculated_mol_wt=103327
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U651.1)"
     Region          35..118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U651.1)"
     Site            94
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q3U0S6; propagated from
                     UniProtKB/Swiss-Prot (Q5U651.1)"
     Region          134..256
                     /region_name="RA_Radil_like"
                     /note="Ras-associating (RA) domain found in
                     ras-associating and dilute domain-containing protein
                     (Radil) and similar proteins; cd17116"
                     /db_xref="CDD:340636"
     Site            order(147,149,156..165,181..182,206,208,225,227,232..234,
                     237,240..246,248,250)
                     /site_type="other"
                     /note="RA-Rap1b interaction site [polypeptide binding]"
                     /db_xref="CDD:340636"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5U651.1)"
     Region          267..356
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U651.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3U0S6; propagated from
                     UniProtKB/Swiss-Prot (Q5U651.1)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3U0S6; propagated from
                     UniProtKB/Swiss-Prot (Q5U651.1)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3U0S6; propagated from
                     UniProtKB/Swiss-Prot (Q5U651.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3U0S6; propagated from
                     UniProtKB/Swiss-Prot (Q5U651.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3U0S6; propagated from
                     UniProtKB/Swiss-Prot (Q5U651.1)"
     Region          378..490
                     /region_name="FHA_RAIN"
                     /note="forkhead associated (FHA) domain found in
                     Ras-interacting protein 1 (Rain); cd22734"
                     /db_xref="CDD:438786"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5U651.1)"
     Region          551..913
                     /region_name="Myo5p-like_CBD_Rasip1"
                     /note="cargo binding domain of myosin 5-like of
                     Ras-interacting protein 1; cd15472"
                     /db_xref="CDD:271256"
     CDS             1..963
                     /gene="RASIP1"
                     /gene_synonym="RAIN"
                     /coded_by="NM_017805.3:95..2986"
                     /db_xref="CCDS:CCDS12731.1"
                     /db_xref="GeneID:54922"
                     /db_xref="HGNC:HGNC:24716"
                     /db_xref="MIM:609623"
ORIGIN      
        1 mlsgerkegg sprfgklhlp vglwinsprk qlaklgrrwp saasvkssss dtgsrssepl
       61 ppppphvelr rvgavkaagg asgsrakris qlfrgsgtgt tgssgaggpg tpggaqrwas
      121 ekklpelaag vapepplatr atappgvlki fgaglasgan yksvlatars tarelvaeal
      181 eryglagspg ggpgesscvd afalcdalgr paaagvgsge wraehlrvlg dserpllvqe
      241 lwrarpgwar rfelrgreea rrleqeafga adsegtgaps wrpqknrsra asggaalasp
      301 gpgtgsgapa gsggkersen lslrrsvsel slqgrrrrqq errqqalsma pgaadaqigt
      361 adpgdfdqlt qcliqapsnr pyflllqgyq daqdfvvyvm treqhvfgrg gnssgrggsp
      421 apyvdtflna pdilprhctv ragpehpamv rpsrgapvth ngclllreae lhpgdllglg
      481 ehflfmykdp rtggsgparp pwlparpgat ppgpgwafsc rlcgrglqer gealaayldg
      541 repvlrfrpr eeeallgeiv raaaagsgdl pplgpatlla lcvqhsarel elghlprllg
      601 rlarlikeav wekikeigdr qpenhpegvp evpltpeavs velrplmlwm anttellsfv
      661 qekvlemeke adqedpqlcn dlelcdeama lldevimctf qqsvyyltkt lystlpalld
      721 snpftagael pgpgaelgam ppglrptlgv fqaaleltsq celhpdlvsq tfgylfffsn
      781 asllnslmer gqgrpfyqws ravqirtnld lvldwlqgag lgdiateffr klsmavnllc
      841 vprtsllkas wsslrtdhpt ltpaqlhhll shyqlgpgrg ppaawdpppa ereavdtgdi
      901 fesfsshppl ilplgssrlr ltgpvtddal hrelrrlrrl lwdleqqelp anyrhgppva
      961 tsp
//
LOCUS       NP_001317172             368 aa            linear   PRI 29-NOV-2025
DEFINITION  acyl-CoA synthetase short-chain family member 3, mitochondrial
            isoform 3 [Homo sapiens].
ACCESSION   NP_001317172 XP_011537042
VERSION     NP_001317172.1
DBSOURCE    REFSEQ: accession NM_001330243.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Huo,P., Wang,S., Li,Z. and Jin,Z.
  TITLE     ACSS3 protein macromolecule regulates glycolysis in keloid through
            Wnt/beta-catenin signaling pathway: Bioinformatics, machine
            learning, and experimental validation
  JOURNAL   Cell Signal 135, 112056 (2025)
   PUBMED   40783148
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Wang,L., Yuan,H., Li,W., Yan,P., Zhao,M., Li,Z., Zhao,H., Wang,S.,
            Wan,R., Li,Y., Yang,J., Pan,X., Rosas,I. and Yu,G.
  TITLE     ACSS3 regulates the metabolic homeostasis of epithelial cells and
            alleviates pulmonary fibrosis
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (2), 166960 (2024)
   PUBMED   37979225
  REMARK    GeneRIF: ACSS3 regulates the metabolic homeostasis of epithelial
            cells and alleviates pulmonary fibrosis.
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Jo,J., Song,Y., Yoon,D., Lee,C.G. and Won,S.
  TITLE     Genome-wide assessment reveals a significant association between
            ACSS3 and physical activity
  JOURNAL   Genes Brain Behav 22 (1), e12834 (2023)
   PUBMED   36510703
  REMARK    GeneRIF: Genome-wide assessment reveals a significant association
            between ACSS3 and physical activity.
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Zhou,L., Song,Z., Hu,J., Liu,L., Hou,Y., Zhang,X., Yang,X. and
            Chen,K.
  TITLE     ACSS3 represses prostate cancer progression through downregulating
            lipid droplet-associated protein PLIN3
  JOURNAL   Theranostics 11 (2), 841-860 (2021)
   PUBMED   33391508
  REMARK    GeneRIF: ACSS3 represses prostate cancer progression through
            downregulating lipid droplet-associated protein PLIN3.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Yoshimura,Y., Araki,A., Maruta,H., Takahashi,Y. and Yamashita,H.
  TITLE     Molecular cloning of rat acss3 and characterization of mammalian
            propionyl-CoA synthetase in the liver mitochondrial matrix
  JOURNAL   J Biochem 161 (3), 279-289 (2017)
   PUBMED   28003429
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Chouraki,V., De Bruijn,R.F., Chapuis,J., Bis,J.C., Reitz,C.,
            Schraen,S., Ibrahim-Verbaas,C.A., Grenier-Boley,B., Delay,C.,
            Rogers,R., Demiautte,F., Mounier,A., Fitzpatrick,A.L., Berr,C.,
            Dartigues,J.F., Uitterlinden,A.G., Hofman,A., Breteler,M.,
            Becker,J.T., Lathrop,M., Schupf,N., Alperovitch,A., Mayeux,R., van
            Duijn,C.M., Buee,L., Amouyel,P., Lopez,O.L., Ikram,M.A., Tzourio,C.
            and Lambert,J.C.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative
  TITLE     A genome-wide association meta-analysis of plasma Abeta peptides
            concentrations in the elderly
  JOURNAL   Mol Psychiatry 19 (12), 1326-1335 (2014)
   PUBMED   24535457
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Ritchie,M.D., Verma,S.S., Hall,M.A., Goodloe,R.J., Berg,R.L.,
            Carrell,D.S., Carlson,C.S., Chen,L., Crosslin,D.R., Denny,J.C.,
            Jarvik,G., Li,R., Linneman,J.G., Pathak,J., Peissig,P.,
            Rasmussen,L.V., Ramirez,A.H., Wang,X., Wilke,R.A., Wolf,W.A.,
            Torstenson,E.S., Turner,S.D. and McCarty,C.A.
  TITLE     Electronic medical records and genomics (eMERGE) network
            exploration in cataract: several new potential susceptibility loci
  JOURNAL   Mol Vis 20, 1281-1295 (2014)
   PUBMED   25352737
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Hunter,A.M., Leuchter,A.F., Power,R.A., Muthen,B., McGrath,P.J.,
            Lewis,C.M., Cook,I.A., Garriock,H.A., McGuffin,P., Uher,R. and
            Hamilton,S.P.
  TITLE     A genome-wide association study of a sustained pattern of
            antidepressant response
  JOURNAL   J Psychiatr Res 47 (9), 1157-1165 (2013)
   PUBMED   23726668
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Watkins,P.A., Maiguel,D., Jia,Z. and Pevsner,J.
  TITLE     Evidence for 26 distinct acyl-coenzyme A synthetase genes in the
            human genome
  JOURNAL   J Lipid Res 48 (12), 2736-2750 (2007)
   PUBMED   17762044
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK025616.1, AC134506.2, AK074938.1, AK074267.1, AC078920.17 and
            AI022900.1.
            
            On Aug 20, 2016 this sequence version replaced XP_011537042.1.
            
            Transcript Variant: This variant (3) contains an alternate exon
            compared to variant 1. This variant represents translation
            initiation at a downstream start codon compared to variant 1; the
            5'-most initiation codon, as used in variant 1, is associated with
            a truncated ORF that would render the transcript a candidate for
            nonsense-mediated decay (NMD). Leaky scanning may allow translation
            initiation at the downstream start codon to encode an isoform (3)
            that has a shorter N-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3303922.1,
                                           SRR18074969.871995.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.31"
     Protein         1..368
                     /product="acyl-CoA synthetase short-chain family member 3,
                     mitochondrial isoform 3"
                     /EC_number="6.2.1.1"
                     /EC_number="6.2.1.17"
                     /note="acyl-CoA synthetase short-chain family member 3,
                     mitochondrial; AMP-binding enzyme, 33217; acetate--CoA
                     ligase 3; propionate--CoA ligase"
                     /calculated_mol_wt=40195
     Region          <1..361
                     /region_name="Adenylate forming domain, Class I
                     superfamily"
                     /note="This family includes acyl- and aryl-CoA ligases, as
                     well as the adenylation domain of nonribosomal peptide
                     synthetases and firefly luciferases. The adenylate-forming
                     enzymes catalyze an ATP-dependent two-step reaction to
                     first activate a carboxylate...; cl17068"
                     /db_xref="CDD:473059"
     Site            order(22..23,75,77..78,81,106..107,128..133,221,233,236,
                     244..247,312)
                     /site_type="active"
                     /db_xref="CDD:341228"
     Site            order(22,77..78,81,106,244..246,306,312)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Site            order(106..107,128..133,221,233,236,247,331)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341228"
     CDS             1..368
                     /gene="ACSS3"
                     /coded_by="NM_001330243.2:1048..2154"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:79611"
                     /db_xref="HGNC:HGNC:24723"
                     /db_xref="MIM:614356"
ORIGIN      
        1 mlhwsmssiy glqpgevwwa asdlgwvvgh syicygpllh gnttvlyegk pvgtpdagay
       61 frvlaehgva alftaptair airqqdpgaa lgkqysltrf ktlfvagerc dvetlewskn
      121 vfrvpvldhw wqtetgspit ascvglgnsk tpppgqagks vpgynvmild dnmqklkarc
      181 lgnivvklpl ppgafsglwk nqeafkhlyf ekfpgyydtm dagymdeegy lyvmsrvddv
      241 invaghrisa gaieesilsh gtvadcavvg kedplkghvp lalcvlrkdi nateeqvlee
      301 ivkhvrqnig pvaafrnavf vkqlpktrsg kiprsalsai vngkpykits tiedpsifgh
      361 veemlkqa
//
LOCUS       NP_001401827              16 aa            linear   PRI 01-DEC-2025
DEFINITION  uncharacterized LOC128092247 [Homo sapiens].
ACCESSION   NP_001401827
VERSION     NP_001401827.1
DBSOURCE    REFSEQ: accession NM_001414898.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC010973.7.
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000674552.1/ ENSP00000501917.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..16
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..16
                     /product="uncharacterized LOC128092247"
                     /calculated_mol_wt=1642
     CDS             1..16
                     /gene="LOC128092247"
                     /gene_synonym="SLC4A2uORF"
                     /coded_by="NM_001414898.1:1..51"
                     /db_xref="GeneID:128092247"
ORIGIN      
        1 mppprcpesr sdsekg
//
LOCUS       NP_001404532              13 aa            linear   PRI 01-DEC-2025
DEFINITION  uncharacterized LOC128462377 isoform 2 [Homo sapiens].
ACCESSION   NP_001404532
VERSION     NP_001404532.1
DBSOURCE    REFSEQ: accession NM_001417603.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092120.4 and AC137932.1.
FEATURES             Location/Qualifiers
     source          1..13
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..13
                     /product="uncharacterized LOC128462377 isoform 2"
                     /calculated_mol_wt=1260
     CDS             1..13
                     /gene="LOC128462377"
                     /coded_by="NM_001417603.1:1..42"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:128462377"
ORIGIN      
        1 mesqtvddea pav
//
LOCUS       NP_071387                704 aa            linear   PRI 01-DEC-2025
DEFINITION  mRNA (2'-O-methyladenosine-N(6)-)-methyltransferase [Homo sapiens].
ACCESSION   NP_071387
VERSION     NP_071387.1
DBSOURCE    REFSEQ: accession NM_022104.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Zhong,W., Wang,C. and Sun,Y.
  TITLE     LncRNA PCIF1 promotes aerobic glycolysis in A549/DDP cells by
            competitively binding miR-326 to regulate PKM expression
  JOURNAL   Mol Cell Probes 77, 101977 (2024)
   PUBMED   39074568
  REMARK    GeneRIF: LncRNA PCIF1 promotes aerobic glycolysis in A549/DDP cells
            by competitively binding miR-326 to regulate PKM expression.
REFERENCE   2  (residues 1 to 704)
  AUTHORS   Xie,S., Kuang,W., Guo,M., Yang,F., Jin,H., Chen,X., Yi,L., Huo,C.,
            Xu,Z., Lin,A., Liu,W., Mao,J., Shu,Q. and Zhou,T.
  TITLE     m6Am methyltransferase PCIF1 negatively regulates ciliation by
            inhibiting BICD2 expression
  JOURNAL   J Cell Biol 223 (6) (2024)
   PUBMED   38526325
  REMARK    GeneRIF: m6Am methyltransferase PCIF1 negatively regulates
            ciliation by inhibiting BICD2 expression.
REFERENCE   3  (residues 1 to 704)
  AUTHORS   Li,K., Chen,J., Zhang,C., Cheng,M., Chen,S., Song,W., Yang,C.,
            Ling,R., Chen,Z., Wang,X., Xiong,G., Ma,J., Zhu,Y., Yuan,Q.,
            Liu,Q., Peng,L., Chen,Q. and Chen,D.
  TITLE     The CTBP2-PCIF1 complex regulates m6Am modification of mRNA in head
            and neck squamous cell carcinoma
  JOURNAL   J Clin Invest 133 (20), e170173 (2023)
   PUBMED   37643007
  REMARK    GeneRIF: The CTBP2-PCIF1 complex regulates m6Am modification of
            mRNA in head and neck squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 704)
  AUTHORS   Wang,L., Wu,L., Zhu,Z., Zhang,Q., Li,W., Gonzalez,G.M., Wang,Y. and
            Rana,T.M.
  TITLE     Role of PCIF1-mediated 5'-cap N6-methyladeonsine mRNA methylation
            in colorectal cancer and anti-PD-1 immunotherapy
  JOURNAL   EMBO J 42 (2), e111673 (2023)
   PUBMED   36514940
  REMARK    GeneRIF: Role of PCIF1-mediated 5'-cap N6-methyladeonsine mRNA
            methylation in colorectal cancer and anti-PD-1 immunotherapy.
REFERENCE   5  (residues 1 to 704)
  AUTHORS   Gao,S., Zhou,J., Hu,Z., Zhang,S., Wu,Y., Musunuru,P.P., Zhang,T.,
            Yang,L., Luo,X., Bai,J., Meng,Q. and Yu,R.
  TITLE     Effects of the m6Am methyltransferase PCIF1 on cell proliferation
            and survival in gliomas
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1868 (11), 166498 (2022)
   PUBMED   35868483
  REMARK    GeneRIF: Effects of the m6Am methyltransferase PCIF1 on cell
            proliferation and survival in gliomas.
REFERENCE   6  (residues 1 to 704)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   7  (residues 1 to 704)
  AUTHORS   Kathiresan,S., Willer,C.J., Peloso,G.M., Demissie,S., Musunuru,K.,
            Schadt,E.E., Kaplan,L., Bennett,D., Li,Y., Tanaka,T., Voight,B.F.,
            Bonnycastle,L.L., Jackson,A.U., Crawford,G., Surti,A., Guiducci,C.,
            Burtt,N.P., Parish,S., Clarke,R., Zelenika,D., Kubalanza,K.A.,
            Morken,M.A., Scott,L.J., Stringham,H.M., Galan,P., Swift,A.J.,
            Kuusisto,J., Bergman,R.N., Sundvall,J., Laakso,M., Ferrucci,L.,
            Scheet,P., Sanna,S., Uda,M., Yang,Q., Lunetta,K.L., Dupuis,J., de
            Bakker,P.I., O'Donnell,C.J., Chambers,J.C., Kooner,J.S.,
            Hercberg,S., Meneton,P., Lakatta,E.G., Scuteri,A., Schlessinger,D.,
            Tuomilehto,J., Collins,F.S., Groop,L., Altshuler,D., Collins,R.,
            Lathrop,G.M., Melander,O., Salomaa,V., Peltonen,L.,
            Orho-Melander,M., Ordovas,J.M., Boehnke,M., Abecasis,G.R.,
            Mohlke,K.L. and Cupples,L.A.
  TITLE     Common variants at 30 loci contribute to polygenic dyslipidemia
  JOURNAL   Nat Genet 41 (1), 56-65 (2009)
   PUBMED   19060906
REFERENCE   8  (residues 1 to 704)
  AUTHORS   Hirose,Y., Iwamoto,Y., Sakuraba,K., Yunokuchi,I., Harada,F. and
            Ohkuma,Y.
  TITLE     Human phosphorylated CTD-interacting protein, PCIF1, negatively
            modulates gene expression by RNA polymerase II
  JOURNAL   Biochem Biophys Res Commun 369 (2), 449-455 (2008)
   PUBMED   18294453
  REMARK    GeneRIF: These data suggest that icariin exerts its potent
            osteogenic effect through induction of Runx2 expression, production
            of BMP-4 and activation of BMP signaling.
REFERENCE   9  (residues 1 to 704)
  AUTHORS   Fan,H., Sakuraba,K., Komuro,A., Kato,S., Harada,F. and Hirose,Y.
  TITLE     PCIF1, a novel human WW domain-containing protein, interacts with
            the phosphorylated RNA polymerase II
  JOURNAL   Biochem Biophys Res Commun 301 (2), 378-385 (2003)
   PUBMED   12565871
  REMARK    GeneRIF: Data suggest that phosphorylated CTD interacting factor 1
            (PCIF1) may play a role in mRNA synthesis by modulating RNA
            polymerase II activity.
REFERENCE   10 (residues 1 to 704)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BQ684226.1 and BC013365.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.66768.1,
                                           SRR1803611.132152.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372409.8/ ENSP00000361486.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..704
                     /product="mRNA
                     (2'-O-methyladenosine-N(6)-)-methyltransferase"
                     /EC_number="2.1.1.62"
                     /note="protein phosphatase 1, regulatory subunit 121;
                     cap-specific adenosine methyltransferase"
                     /calculated_mol_wt=80539
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4Z3.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H4Z3.1)"
     Region          47..77
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(61,72)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          88..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4Z3.1)"
     Region          109..113
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4Z3.1)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H4Z3.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9H4Z3.1)"
     Region          446..616
                     /region_name="PCIF1_WW"
                     /note="Phosphorylated CTD interacting factor 1 WW domain;
                     pfam12237"
                     /db_xref="CDD:463502"
     Region          663..704
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4Z3.1)"
     Region          669..684
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4Z3.1)"
     CDS             1..704
                     /gene="PCIF1"
                     /gene_synonym="C20orf67; CAPAM; hCAPAM; hPCIF1; MT-A70;
                     PPP1R121"
                     /coded_by="NM_022104.4:310..2424"
                     /db_xref="CCDS:CCDS13388.1"
                     /db_xref="GeneID:63935"
                     /db_xref="HGNC:HGNC:16200"
                     /db_xref="MIM:618626"
ORIGIN      
        1 manenhgspr eeasllshsp gtsnqsqpcs pkpirlvqdl peelvhagwe kcwsrrenrp
       61 yyfnrftnqs lwempvlgqh dvisdplgln atplpqdssl vetppaenkp rkrqlseeqp
      121 sgngvkkpki eipvtptgqs vpsspsipgt ptlkmwgtsp edkqqaallr ptevywdldi
      181 qtnavikhrg psevlpphpe vellrsqlil klrqhyrelc qqregieppr esfnrwmler
      241 kvvdkgsdpl lpsncepvvs psmfreimnd ipirlsrikf reeakrllfk yaeaarrlie
      301 srsaspdsrk vvkwnvedtf swlrkdhsas kedymdrleh lrrqcgphvs aaakdsvegi
      361 cskiyhisle yvkrirekhl ailkennise eveapevepr lvycypvrla vsappmpsve
      421 mhmennvvci rykgemvkvs rnyfsklwll yrysciddsa ferflprvwc llrryqmmfg
      481 vglyegtglq gslpvhvfea lhrlfgvsfe cfasplncyf rqycsafpdt dgyfgsrgpc
      541 ldfaplsgsf eanppfceel mdamvshfer llesspepls fivfipewre pptpaltrme
      601 qsrfkrhqli lpafeheyrs gsqhickkee mhykavhnta vlflqndpgf akwaptperl
      661 qelsaayrqs grshssgsss sssseakdrd sgreqgpsre phpt
//
LOCUS       NP_001403332              12 aa            linear   PRI 01-DEC-2025
DEFINITION  uncharacterized LOC128462377 isoform 1 [Homo sapiens].
ACCESSION   NP_001403332
VERSION     NP_001403332.1
DBSOURCE    REFSEQ: accession NM_001416403.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092120.4 and AC137932.1.
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000711617.1/ ENSP00000518812.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..12
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..12
                     /product="uncharacterized LOC128462377 isoform 1"
                     /calculated_mol_wt=1132
     CDS             1..12
                     /gene="LOC128462377"
                     /coded_by="NM_001416403.1:1..39"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:128462377"
ORIGIN      
        1 mestvddeap av
//
LOCUS       NP_001258851             185 aa            linear   PRI 01-DEC-2025
DEFINITION  signal peptidase complex catalytic subunit SEC11A isoform 3 [Homo
            sapiens].
ACCESSION   NP_001258851
VERSION     NP_001258851.1
DBSOURCE    REFSEQ: accession NM_001271922.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Suematsu,H., Sakamaki,K., Oue,N., Hiroshima,Y., Kimura,Y.,
            Onuma,S., Hashimoto,I., Nagasawa,S., Aoyama,T., Yamada,T.,
            Tamagawa,H., Ogata,T., Rino,Y., Masuda,M., Yasui,W., Miyagi,Y. and
            Oshima,T.
  TITLE     Clinical Significance of SEC11A Expression in Patients With Locally
            Advanced Gastric Cancer
  JOURNAL   Anticancer Res 42 (12), 5885-5890 (2022)
   PUBMED   36456166
  REMARK    GeneRIF: Clinical Significance of SEC11A Expression in Patients
            With Locally Advanced Gastric Cancer.
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Yao,Y., Liu,X.Q., Yang,F.Y. and Mu,J.W.
  TITLE     MiR-873-5p modulates progression of tongue squamous cell carcinoma
            via targeting SEC11A
  JOURNAL   Oral Dis 28 (6), 1509-1518 (2022)
   PUBMED   33675129
  REMARK    GeneRIF: MiR-873-5p modulates progression of tongue squamous cell
            carcinoma via targeting SEC11A.
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Liaci,A.M., Steigenberger,B., Telles de Souza,P.C., Tamara,S.,
            Grollers-Mulderij,M., Ogrissek,P., Marrink,S.J., Scheltema,R.A. and
            Forster,F.
  TITLE     Structure of the human signal peptidase complex reveals the
            determinants for signal peptide cleavage
  JOURNAL   Mol Cell 81 (19), 3934-3948 (2021)
   PUBMED   34388369
  REMARK    GeneRIF: Structure of the human signal peptidase complex reveals
            the determinants for signal peptide cleavage.
REFERENCE   5  (residues 1 to 185)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 185)
  AUTHORS   Oue,N., Naito,Y., Hayashi,T., Takigahira,M., Kawano-Nagatsuma,A.,
            Sentani,K., Sakamoto,N., Zarni Oo,H., Uraoka,N., Yanagihara,K.,
            Ochiai,A., Sasaki,H. and Yasui,W.
  TITLE     Signal peptidase complex 18, encoded by SEC11A, contributes to
            progression via TGF-alpha secretion in gastric cancer
  JOURNAL   Oncogene 33 (30), 3918-3926 (2014)
   PUBMED   23995782
  REMARK    GeneRIF: SPC18 contributes to malignant progression through
            promotion of TGF-alpha secretion in gastric cancer.
            Erratum:[Oncogene. 2019 Jul;38(28):5748. doi:
            10.1038/s41388-019-0837-z. PMID: 31175341]
REFERENCE   7  (residues 1 to 185)
  AUTHORS   Guffanti,A., Iacono,M., Pelucchi,P., Kim,N., Solda,G., Croft,L.J.,
            Taft,R.J., Rizzi,E., Askarian-Amiri,M., Bonnal,R.J., Callari,M.,
            Mignone,F., Pesole,G., Bertalot,G., Bernardi,L.R., Albertini,A.,
            Lee,C., Mattick,J.S., Zucchi,I. and De Bellis,G.
  TITLE     A transcriptional sketch of a primary human breast cancer by 454
            deep sequencing
  JOURNAL   BMC Genomics 10, 163 (2009)
   PUBMED   19379481
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 185)
  AUTHORS   Yasui,W., Oue,N., Sentani,K., Sakamoto,N. and Motoshita,J.
  TITLE     Transcriptome dissection of gastric cancer: identification of novel
            diagnostic and therapeutic targets from pathology specimens
  JOURNAL   Pathol Int 59 (3), 121-136 (2009)
   PUBMED   19261089
  REMARK    Review article
REFERENCE   9  (residues 1 to 185)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 185)
  AUTHORS   Shelness,G.S. and Blobel,G.
  TITLE     Two subunits of the canine signal peptidase complex are homologous
            to yeast SEC11 protein
  JOURNAL   J Biol Chem 265 (16), 9512-9519 (1990)
   PUBMED   2188978
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM763471.1, BM904189.1 and
            BC000359.2.
            
            Summary: This gene encodes a member of the peptidase S26B family.
            The encoded protein is an 18kDa subunit of the signal peptidase
            complex and has been linked to cell migration and invasion, gastric
            cancer and lymph node metastasis. Alternative splicing results in
            multiple transcript variants. A related pseudogene has been
            identified on chromosome 8. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            exon and lacks an exon in the 3' coding region which results in a
            frameshift, compared to variant 1. The encoded isoform (3) is
            longer and has a distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM904189.1, SRR18074967.3953866.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2-q25.3"
     Protein         1..185
                     /product="signal peptidase complex catalytic subunit
                     SEC11A isoform 3"
                     /EC_number="3.4.21.89"
                     /note="signal peptidase complex (18kD); signal peptidase
                     complex catalytic subunit SEC11A; endopeptidase SP18;
                     SEC11-like protein 1; SPase 18 kDa subunit; microsomal
                     signal peptidase 18 kDa subunit; signal peptidase complex
                     18"
                     /calculated_mol_wt=21323
     Site            17..36
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P67812.1)"
     Region          38..>122
                     /region_name="Peptidase_S24_S26"
                     /note="The S24, S26 LexA/signal peptidase superfamily
                     contains LexA-related and type I signal peptidase
                     families. The S24 LexA protein domains include: the lambda
                     repressor CI/C2 family and related bacterial prophage
                     repressor proteins; LexA (EC 3.4.21.88), the...; cl10465"
                     /db_xref="CDD:447902"
     Site            order(56,96)
                     /site_type="active"
                     /note="Catalytic site [active]"
                     /db_xref="CDD:119398"
     CDS             1..185
                     /gene="SEC11A"
                     /gene_synonym="1810012E07Rik; SEC11L1; sid2895; SPC18;
                     SPCS4A"
                     /coded_by="NM_001271922.2:65..622"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS61743.1"
                     /db_xref="GeneID:23478"
                     /db_xref="HGNC:HGNC:17718"
                     /db_xref="MIM:618258"
ORIGIN      
        1 mlsldflddv rrmnkrqlyy qvlnfgmivs salmiwkglm vitgsespiv vvlsgsmepa
       61 fhrgdllflt nrvedpirvg eivvfriegr eipivhrvlk ihekqnghik fltkgdnnav
      121 ddrglykqgq hwlekkdvvg rargmqfsfc wvyscwfivs kkpallflgr chsfrywmfg
      181 vdtgl
//
LOCUS       NP_001258850             129 aa            linear   PRI 01-DEC-2025
DEFINITION  signal peptidase complex catalytic subunit SEC11A isoform 1 [Homo
            sapiens].
ACCESSION   NP_001258850
VERSION     NP_001258850.1
DBSOURCE    REFSEQ: accession NM_001271921.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Suematsu,H., Sakamaki,K., Oue,N., Hiroshima,Y., Kimura,Y.,
            Onuma,S., Hashimoto,I., Nagasawa,S., Aoyama,T., Yamada,T.,
            Tamagawa,H., Ogata,T., Rino,Y., Masuda,M., Yasui,W., Miyagi,Y. and
            Oshima,T.
  TITLE     Clinical Significance of SEC11A Expression in Patients With Locally
            Advanced Gastric Cancer
  JOURNAL   Anticancer Res 42 (12), 5885-5890 (2022)
   PUBMED   36456166
  REMARK    GeneRIF: Clinical Significance of SEC11A Expression in Patients
            With Locally Advanced Gastric Cancer.
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Yao,Y., Liu,X.Q., Yang,F.Y. and Mu,J.W.
  TITLE     MiR-873-5p modulates progression of tongue squamous cell carcinoma
            via targeting SEC11A
  JOURNAL   Oral Dis 28 (6), 1509-1518 (2022)
   PUBMED   33675129
  REMARK    GeneRIF: MiR-873-5p modulates progression of tongue squamous cell
            carcinoma via targeting SEC11A.
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Liaci,A.M., Steigenberger,B., Telles de Souza,P.C., Tamara,S.,
            Grollers-Mulderij,M., Ogrissek,P., Marrink,S.J., Scheltema,R.A. and
            Forster,F.
  TITLE     Structure of the human signal peptidase complex reveals the
            determinants for signal peptide cleavage
  JOURNAL   Mol Cell 81 (19), 3934-3948 (2021)
   PUBMED   34388369
  REMARK    GeneRIF: Structure of the human signal peptidase complex reveals
            the determinants for signal peptide cleavage.
REFERENCE   5  (residues 1 to 129)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 129)
  AUTHORS   Oue,N., Naito,Y., Hayashi,T., Takigahira,M., Kawano-Nagatsuma,A.,
            Sentani,K., Sakamoto,N., Zarni Oo,H., Uraoka,N., Yanagihara,K.,
            Ochiai,A., Sasaki,H. and Yasui,W.
  TITLE     Signal peptidase complex 18, encoded by SEC11A, contributes to
            progression via TGF-alpha secretion in gastric cancer
  JOURNAL   Oncogene 33 (30), 3918-3926 (2014)
   PUBMED   23995782
  REMARK    GeneRIF: SPC18 contributes to malignant progression through
            promotion of TGF-alpha secretion in gastric cancer.
            Erratum:[Oncogene. 2019 Jul;38(28):5748. doi:
            10.1038/s41388-019-0837-z. PMID: 31175341]
REFERENCE   7  (residues 1 to 129)
  AUTHORS   Guffanti,A., Iacono,M., Pelucchi,P., Kim,N., Solda,G., Croft,L.J.,
            Taft,R.J., Rizzi,E., Askarian-Amiri,M., Bonnal,R.J., Callari,M.,
            Mignone,F., Pesole,G., Bertalot,G., Bernardi,L.R., Albertini,A.,
            Lee,C., Mattick,J.S., Zucchi,I. and De Bellis,G.
  TITLE     A transcriptional sketch of a primary human breast cancer by 454
            deep sequencing
  JOURNAL   BMC Genomics 10, 163 (2009)
   PUBMED   19379481
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 129)
  AUTHORS   Yasui,W., Oue,N., Sentani,K., Sakamoto,N. and Motoshita,J.
  TITLE     Transcriptome dissection of gastric cancer: identification of novel
            diagnostic and therapeutic targets from pathology specimens
  JOURNAL   Pathol Int 59 (3), 121-136 (2009)
   PUBMED   19261089
  REMARK    Review article
REFERENCE   9  (residues 1 to 129)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 129)
  AUTHORS   Shelness,G.S. and Blobel,G.
  TITLE     Two subunits of the canine signal peptidase complex are homologous
            to yeast SEC11 protein
  JOURNAL   J Biol Chem 265 (16), 9512-9519 (1990)
   PUBMED   2188978
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM763471.1, HY170714.1,
            AF061737.1 and AA151795.1.
            
            Summary: This gene encodes a member of the peptidase S26B family.
            The encoded protein is an 18kDa subunit of the signal peptidase
            complex and has been linked to cell migration and invasion, gastric
            cancer and lymph node metastasis. Alternative splicing results in
            multiple transcript variants. A related pseudogene has been
            identified on chromosome 8. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (1) represents the shortest
            transcript and encodes the shortest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14243140.2096557.1, HY170847.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144, SAMEA2467148
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2-q25.3"
     Protein         1..129
                     /product="signal peptidase complex catalytic subunit
                     SEC11A isoform 1"
                     /EC_number="3.4.21.89"
                     /note="signal peptidase complex (18kD); signal peptidase
                     complex catalytic subunit SEC11A; endopeptidase SP18;
                     SEC11-like protein 1; SPase 18 kDa subunit; microsomal
                     signal peptidase 18 kDa subunit; signal peptidase complex
                     18"
                     /calculated_mol_wt=14762
     CDS             1..129
                     /gene="SEC11A"
                     /gene_synonym="1810012E07Rik; SEC11L1; sid2895; SPC18;
                     SPCS4A"
                     /coded_by="NM_001271921.2:65..454"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS73776.1"
                     /db_xref="GeneID:23478"
                     /db_xref="HGNC:HGNC:17718"
                     /db_xref="MIM:618258"
ORIGIN      
        1 mlsldflddv rrmnkrqlyy qvlnfgmivs salmiwkglm vitgsespiv vvlrqnghik
       61 fltkgdnnav ddrglykqgq hwlekkdvvg rargfvpyig ivtilmndyp kfkyavlfll
      121 glfvlvhre
//
LOCUS       NP_001258847             153 aa            linear   PRI 01-DEC-2025
DEFINITION  signal peptidase complex catalytic subunit SEC11A isoform 5 [Homo
            sapiens].
ACCESSION   NP_001258847
VERSION     NP_001258847.1
DBSOURCE    REFSEQ: accession NM_001271918.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Suematsu,H., Sakamaki,K., Oue,N., Hiroshima,Y., Kimura,Y.,
            Onuma,S., Hashimoto,I., Nagasawa,S., Aoyama,T., Yamada,T.,
            Tamagawa,H., Ogata,T., Rino,Y., Masuda,M., Yasui,W., Miyagi,Y. and
            Oshima,T.
  TITLE     Clinical Significance of SEC11A Expression in Patients With Locally
            Advanced Gastric Cancer
  JOURNAL   Anticancer Res 42 (12), 5885-5890 (2022)
   PUBMED   36456166
  REMARK    GeneRIF: Clinical Significance of SEC11A Expression in Patients
            With Locally Advanced Gastric Cancer.
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Yao,Y., Liu,X.Q., Yang,F.Y. and Mu,J.W.
  TITLE     MiR-873-5p modulates progression of tongue squamous cell carcinoma
            via targeting SEC11A
  JOURNAL   Oral Dis 28 (6), 1509-1518 (2022)
   PUBMED   33675129
  REMARK    GeneRIF: MiR-873-5p modulates progression of tongue squamous cell
            carcinoma via targeting SEC11A.
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Liaci,A.M., Steigenberger,B., Telles de Souza,P.C., Tamara,S.,
            Grollers-Mulderij,M., Ogrissek,P., Marrink,S.J., Scheltema,R.A. and
            Forster,F.
  TITLE     Structure of the human signal peptidase complex reveals the
            determinants for signal peptide cleavage
  JOURNAL   Mol Cell 81 (19), 3934-3948 (2021)
   PUBMED   34388369
  REMARK    GeneRIF: Structure of the human signal peptidase complex reveals
            the determinants for signal peptide cleavage.
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 153)
  AUTHORS   Oue,N., Naito,Y., Hayashi,T., Takigahira,M., Kawano-Nagatsuma,A.,
            Sentani,K., Sakamoto,N., Zarni Oo,H., Uraoka,N., Yanagihara,K.,
            Ochiai,A., Sasaki,H. and Yasui,W.
  TITLE     Signal peptidase complex 18, encoded by SEC11A, contributes to
            progression via TGF-alpha secretion in gastric cancer
  JOURNAL   Oncogene 33 (30), 3918-3926 (2014)
   PUBMED   23995782
  REMARK    GeneRIF: SPC18 contributes to malignant progression through
            promotion of TGF-alpha secretion in gastric cancer.
            Erratum:[Oncogene. 2019 Jul;38(28):5748. doi:
            10.1038/s41388-019-0837-z. PMID: 31175341]
REFERENCE   7  (residues 1 to 153)
  AUTHORS   Guffanti,A., Iacono,M., Pelucchi,P., Kim,N., Solda,G., Croft,L.J.,
            Taft,R.J., Rizzi,E., Askarian-Amiri,M., Bonnal,R.J., Callari,M.,
            Mignone,F., Pesole,G., Bertalot,G., Bernardi,L.R., Albertini,A.,
            Lee,C., Mattick,J.S., Zucchi,I. and De Bellis,G.
  TITLE     A transcriptional sketch of a primary human breast cancer by 454
            deep sequencing
  JOURNAL   BMC Genomics 10, 163 (2009)
   PUBMED   19379481
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 153)
  AUTHORS   Yasui,W., Oue,N., Sentani,K., Sakamoto,N. and Motoshita,J.
  TITLE     Transcriptome dissection of gastric cancer: identification of novel
            diagnostic and therapeutic targets from pathology specimens
  JOURNAL   Pathol Int 59 (3), 121-136 (2009)
   PUBMED   19261089
  REMARK    Review article
REFERENCE   9  (residues 1 to 153)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 153)
  AUTHORS   Shelness,G.S. and Blobel,G.
  TITLE     Two subunits of the canine signal peptidase complex are homologous
            to yeast SEC11 protein
  JOURNAL   J Biol Chem 265 (16), 9512-9519 (1990)
   PUBMED   2188978
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP370483.1, AK300693.1 and
            BM985046.1.
            
            Summary: This gene encodes a member of the peptidase S26B family.
            The encoded protein is an 18kDa subunit of the signal peptidase
            complex and has been linked to cell migration and invasion, gastric
            cancer and lymph node metastasis. Alternative splicing results in
            multiple transcript variants. A related pseudogene has been
            identified on chromosome 8. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (5) uses an alternate exon in the
            5' coding region which results in initiation at a downstream start
            site and an alternate in-frame exon in the central coding region,
            compared to variant 1. The encoded isoform (5) is longer than
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF087906.1, AK300693.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2-q25.3"
     Protein         1..153
                     /product="signal peptidase complex catalytic subunit
                     SEC11A isoform 5"
                     /EC_number="3.4.21.89"
                     /note="signal peptidase complex (18kD); signal peptidase
                     complex catalytic subunit SEC11A; endopeptidase SP18;
                     SEC11-like protein 1; SPase 18 kDa subunit; microsomal
                     signal peptidase 18 kDa subunit; signal peptidase complex
                     18"
                     /calculated_mol_wt=17276
     Region          12..>124
                     /region_name="Peptidase_S24_S26"
                     /note="The S24, S26 LexA/signal peptidase superfamily
                     contains LexA-related and type I signal peptidase
                     families. The S24 LexA protein domains include: the lambda
                     repressor CI/C2 family and related bacterial prophage
                     repressor proteins; LexA (EC 3.4.21.88), the...; cl10465"
                     /db_xref="CDD:447902"
     Site            order(30,70)
                     /site_type="active"
                     /note="Catalytic site [active]"
                     /db_xref="CDD:119398"
     CDS             1..153
                     /gene="SEC11A"
                     /gene_synonym="1810012E07Rik; SEC11L1; sid2895; SPC18;
                     SPCS4A"
                     /coded_by="NM_001271918.2:279..740"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS61742.1"
                     /db_xref="GeneID:23478"
                     /db_xref="HGNC:HGNC:17718"
                     /db_xref="MIM:618258"
ORIGIN      
        1 mivssalmiw kglmvitgse spivvvlsgs mepafhrgdl lfltnrvedp irvgeivvfr
       61 iegreipivh rvlkihekqn ghikfltkgd nnavddrgly kqgqhwlekk dvvgrargfv
      121 pyigivtilm ndypkfkyav lfllglfvlv hre
//
LOCUS       NP_001258848             139 aa            linear   PRI 01-DEC-2025
DEFINITION  signal peptidase complex catalytic subunit SEC11A isoform 6 [Homo
            sapiens].
ACCESSION   NP_001258848
VERSION     NP_001258848.1
DBSOURCE    REFSEQ: accession NM_001271919.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Suematsu,H., Sakamaki,K., Oue,N., Hiroshima,Y., Kimura,Y.,
            Onuma,S., Hashimoto,I., Nagasawa,S., Aoyama,T., Yamada,T.,
            Tamagawa,H., Ogata,T., Rino,Y., Masuda,M., Yasui,W., Miyagi,Y. and
            Oshima,T.
  TITLE     Clinical Significance of SEC11A Expression in Patients With Locally
            Advanced Gastric Cancer
  JOURNAL   Anticancer Res 42 (12), 5885-5890 (2022)
   PUBMED   36456166
  REMARK    GeneRIF: Clinical Significance of SEC11A Expression in Patients
            With Locally Advanced Gastric Cancer.
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Yao,Y., Liu,X.Q., Yang,F.Y. and Mu,J.W.
  TITLE     MiR-873-5p modulates progression of tongue squamous cell carcinoma
            via targeting SEC11A
  JOURNAL   Oral Dis 28 (6), 1509-1518 (2022)
   PUBMED   33675129
  REMARK    GeneRIF: MiR-873-5p modulates progression of tongue squamous cell
            carcinoma via targeting SEC11A.
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Liaci,A.M., Steigenberger,B., Telles de Souza,P.C., Tamara,S.,
            Grollers-Mulderij,M., Ogrissek,P., Marrink,S.J., Scheltema,R.A. and
            Forster,F.
  TITLE     Structure of the human signal peptidase complex reveals the
            determinants for signal peptide cleavage
  JOURNAL   Mol Cell 81 (19), 3934-3948 (2021)
   PUBMED   34388369
  REMARK    GeneRIF: Structure of the human signal peptidase complex reveals
            the determinants for signal peptide cleavage.
REFERENCE   5  (residues 1 to 139)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 139)
  AUTHORS   Oue,N., Naito,Y., Hayashi,T., Takigahira,M., Kawano-Nagatsuma,A.,
            Sentani,K., Sakamoto,N., Zarni Oo,H., Uraoka,N., Yanagihara,K.,
            Ochiai,A., Sasaki,H. and Yasui,W.
  TITLE     Signal peptidase complex 18, encoded by SEC11A, contributes to
            progression via TGF-alpha secretion in gastric cancer
  JOURNAL   Oncogene 33 (30), 3918-3926 (2014)
   PUBMED   23995782
  REMARK    GeneRIF: SPC18 contributes to malignant progression through
            promotion of TGF-alpha secretion in gastric cancer.
            Erratum:[Oncogene. 2019 Jul;38(28):5748. doi:
            10.1038/s41388-019-0837-z. PMID: 31175341]
REFERENCE   7  (residues 1 to 139)
  AUTHORS   Guffanti,A., Iacono,M., Pelucchi,P., Kim,N., Solda,G., Croft,L.J.,
            Taft,R.J., Rizzi,E., Askarian-Amiri,M., Bonnal,R.J., Callari,M.,
            Mignone,F., Pesole,G., Bertalot,G., Bernardi,L.R., Albertini,A.,
            Lee,C., Mattick,J.S., Zucchi,I. and De Bellis,G.
  TITLE     A transcriptional sketch of a primary human breast cancer by 454
            deep sequencing
  JOURNAL   BMC Genomics 10, 163 (2009)
   PUBMED   19379481
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 139)
  AUTHORS   Yasui,W., Oue,N., Sentani,K., Sakamoto,N. and Motoshita,J.
  TITLE     Transcriptome dissection of gastric cancer: identification of novel
            diagnostic and therapeutic targets from pathology specimens
  JOURNAL   Pathol Int 59 (3), 121-136 (2009)
   PUBMED   19261089
  REMARK    Review article
REFERENCE   9  (residues 1 to 139)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 139)
  AUTHORS   Shelness,G.S. and Blobel,G.
  TITLE     Two subunits of the canine signal peptidase complex are homologous
            to yeast SEC11 protein
  JOURNAL   J Biol Chem 265 (16), 9512-9519 (1990)
   PUBMED   2188978
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD356160.1, CF455691.1 and
            AI051931.1.
            
            Summary: This gene encodes a member of the peptidase S26B family.
            The encoded protein is an 18kDa subunit of the signal peptidase
            complex and has been linked to cell migration and invasion, gastric
            cancer and lymph node metastasis. Alternative splicing results in
            multiple transcript variants. A related pseudogene has been
            identified on chromosome 8. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (6) uses an alternate in-frame
            exon and lacks an in-frame exon in the central coding region,
            compared to variant 1. The encoded isoform (6) is longer than
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF455691.1, SRR14038195.2534230.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2-q25.3"
     Protein         1..139
                     /product="signal peptidase complex catalytic subunit
                     SEC11A isoform 6"
                     /EC_number="3.4.21.89"
                     /note="signal peptidase complex (18kD); signal peptidase
                     complex catalytic subunit SEC11A; endopeptidase SP18;
                     SEC11-like protein 1; SPase 18 kDa subunit; microsomal
                     signal peptidase 18 kDa subunit; signal peptidase complex
                     18"
                     /calculated_mol_wt=15962
     Region          38..>103
                     /region_name="Peptidase_S24_S26"
                     /note="The S24, S26 LexA/signal peptidase superfamily
                     contains LexA-related and type I signal peptidase
                     families. The S24 LexA protein domains include: the lambda
                     repressor CI/C2 family and related bacterial prophage
                     repressor proteins; LexA (EC 3.4.21.88), the...; cl10465"
                     /db_xref="CDD:447902"
     Site            order(56,96)
                     /site_type="active"
                     /note="Catalytic site [active]"
                     /db_xref="CDD:119398"
     CDS             1..139
                     /gene="SEC11A"
                     /gene_synonym="1810012E07Rik; SEC11L1; sid2895; SPC18;
                     SPCS4A"
                     /coded_by="NM_001271919.2:65..484"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:23478"
                     /db_xref="HGNC:HGNC:17718"
                     /db_xref="MIM:618258"
ORIGIN      
        1 mlsldflddv rrmnkrqlyy qvlnfgmivs salmiwkglm vitgsespiv vvlsgsmepa
       61 fhrgdllflt nrvedpirvg eivvfriegr eipivhrvlk ihekfvpyig ivtilmndyp
      121 kfkyavlfll glfvlvhre
//
LOCUS       NP_055115                179 aa            linear   PRI 01-DEC-2025
DEFINITION  signal peptidase complex catalytic subunit SEC11A isoform 2 [Homo
            sapiens].
ACCESSION   NP_055115
VERSION     NP_055115.1
DBSOURCE    REFSEQ: accession NM_014300.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Suematsu,H., Sakamaki,K., Oue,N., Hiroshima,Y., Kimura,Y.,
            Onuma,S., Hashimoto,I., Nagasawa,S., Aoyama,T., Yamada,T.,
            Tamagawa,H., Ogata,T., Rino,Y., Masuda,M., Yasui,W., Miyagi,Y. and
            Oshima,T.
  TITLE     Clinical Significance of SEC11A Expression in Patients With Locally
            Advanced Gastric Cancer
  JOURNAL   Anticancer Res 42 (12), 5885-5890 (2022)
   PUBMED   36456166
  REMARK    GeneRIF: Clinical Significance of SEC11A Expression in Patients
            With Locally Advanced Gastric Cancer.
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Yao,Y., Liu,X.Q., Yang,F.Y. and Mu,J.W.
  TITLE     MiR-873-5p modulates progression of tongue squamous cell carcinoma
            via targeting SEC11A
  JOURNAL   Oral Dis 28 (6), 1509-1518 (2022)
   PUBMED   33675129
  REMARK    GeneRIF: MiR-873-5p modulates progression of tongue squamous cell
            carcinoma via targeting SEC11A.
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Liaci,A.M., Steigenberger,B., Telles de Souza,P.C., Tamara,S.,
            Grollers-Mulderij,M., Ogrissek,P., Marrink,S.J., Scheltema,R.A. and
            Forster,F.
  TITLE     Structure of the human signal peptidase complex reveals the
            determinants for signal peptide cleavage
  JOURNAL   Mol Cell 81 (19), 3934-3948 (2021)
   PUBMED   34388369
  REMARK    GeneRIF: Structure of the human signal peptidase complex reveals
            the determinants for signal peptide cleavage.
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 179)
  AUTHORS   Oue,N., Naito,Y., Hayashi,T., Takigahira,M., Kawano-Nagatsuma,A.,
            Sentani,K., Sakamoto,N., Zarni Oo,H., Uraoka,N., Yanagihara,K.,
            Ochiai,A., Sasaki,H. and Yasui,W.
  TITLE     Signal peptidase complex 18, encoded by SEC11A, contributes to
            progression via TGF-alpha secretion in gastric cancer
  JOURNAL   Oncogene 33 (30), 3918-3926 (2014)
   PUBMED   23995782
  REMARK    GeneRIF: SPC18 contributes to malignant progression through
            promotion of TGF-alpha secretion in gastric cancer.
            Erratum:[Oncogene. 2019 Jul;38(28):5748. doi:
            10.1038/s41388-019-0837-z. PMID: 31175341]
REFERENCE   7  (residues 1 to 179)
  AUTHORS   Guffanti,A., Iacono,M., Pelucchi,P., Kim,N., Solda,G., Croft,L.J.,
            Taft,R.J., Rizzi,E., Askarian-Amiri,M., Bonnal,R.J., Callari,M.,
            Mignone,F., Pesole,G., Bertalot,G., Bernardi,L.R., Albertini,A.,
            Lee,C., Mattick,J.S., Zucchi,I. and De Bellis,G.
  TITLE     A transcriptional sketch of a primary human breast cancer by 454
            deep sequencing
  JOURNAL   BMC Genomics 10, 163 (2009)
   PUBMED   19379481
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 179)
  AUTHORS   Yasui,W., Oue,N., Sentani,K., Sakamoto,N. and Motoshita,J.
  TITLE     Transcriptome dissection of gastric cancer: identification of novel
            diagnostic and therapeutic targets from pathology specimens
  JOURNAL   Pathol Int 59 (3), 121-136 (2009)
   PUBMED   19261089
  REMARK    Review article
REFERENCE   9  (residues 1 to 179)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 179)
  AUTHORS   Shelness,G.S. and Blobel,G.
  TITLE     Two subunits of the canine signal peptidase complex are homologous
            to yeast SEC11 protein
  JOURNAL   J Biol Chem 265 (16), 9512-9519 (1990)
   PUBMED   2188978
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC360846.1 and BC014508.1.
            
            Summary: This gene encodes a member of the peptidase S26B family.
            The encoded protein is an 18kDa subunit of the signal peptidase
            complex and has been linked to cell migration and invasion, gastric
            cancer and lymph node metastasis. Alternative splicing results in
            multiple transcript variants. A related pseudogene has been
            identified on chromosome 8. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            exon in the central coding region, compared to variant 1. It
            encodes a longer protein (isoform 2) compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014508.1, SRR5189664.106682.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144, SAMEA2467148
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268220.12/ ENSP00000268220.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2-q25.3"
     Protein         1..179
                     /product="signal peptidase complex catalytic subunit
                     SEC11A isoform 2"
                     /EC_number="3.4.21.89"
                     /note="signal peptidase complex (18kD); signal peptidase
                     complex catalytic subunit SEC11A; endopeptidase SP18;
                     SEC11-like protein 1; SPase 18 kDa subunit; microsomal
                     signal peptidase 18 kDa subunit; signal peptidase complex
                     18"
                     /calculated_mol_wt=20494
     Site            17..36
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P67812.1)"
     Region          38..>150
                     /region_name="Peptidase_S24_S26"
                     /note="The S24, S26 LexA/signal peptidase superfamily
                     contains LexA-related and type I signal peptidase
                     families. The S24 LexA protein domains include: the lambda
                     repressor CI/C2 family and related bacterial prophage
                     repressor proteins; LexA (EC 3.4.21.88), the...; cl10465"
                     /db_xref="CDD:447902"
     Site            order(56,96)
                     /site_type="active"
                     /note="Catalytic site [active]"
                     /db_xref="CDD:119398"
     Region          165..176
                     /region_name="C-terminal short (CTS) helix.
                     /evidence=ECO:0000269|PubMed:34388369"
                     /note="propagated from UniProtKB/Swiss-Prot (P67812.1)"
     CDS             1..179
                     /gene="SEC11A"
                     /gene_synonym="1810012E07Rik; SEC11L1; sid2895; SPC18;
                     SPCS4A"
                     /coded_by="NM_014300.4:65..604"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45340.1"
                     /db_xref="GeneID:23478"
                     /db_xref="HGNC:HGNC:17718"
                     /db_xref="MIM:618258"
ORIGIN      
        1 mlsldflddv rrmnkrqlyy qvlnfgmivs salmiwkglm vitgsespiv vvlsgsmepa
       61 fhrgdllflt nrvedpirvg eivvfriegr eipivhrvlk ihekqnghik fltkgdnnav
      121 ddrglykqgq hwlekkdvvg rargfvpyig ivtilmndyp kfkyavlfll glfvlvhre
//
LOCUS       NP_001258849             164 aa            linear   PRI 01-DEC-2025
DEFINITION  signal peptidase complex catalytic subunit SEC11A isoform 4 [Homo
            sapiens].
ACCESSION   NP_001258849
VERSION     NP_001258849.1
DBSOURCE    REFSEQ: accession NM_001271920.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Suematsu,H., Sakamaki,K., Oue,N., Hiroshima,Y., Kimura,Y.,
            Onuma,S., Hashimoto,I., Nagasawa,S., Aoyama,T., Yamada,T.,
            Tamagawa,H., Ogata,T., Rino,Y., Masuda,M., Yasui,W., Miyagi,Y. and
            Oshima,T.
  TITLE     Clinical Significance of SEC11A Expression in Patients With Locally
            Advanced Gastric Cancer
  JOURNAL   Anticancer Res 42 (12), 5885-5890 (2022)
   PUBMED   36456166
  REMARK    GeneRIF: Clinical Significance of SEC11A Expression in Patients
            With Locally Advanced Gastric Cancer.
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Yao,Y., Liu,X.Q., Yang,F.Y. and Mu,J.W.
  TITLE     MiR-873-5p modulates progression of tongue squamous cell carcinoma
            via targeting SEC11A
  JOURNAL   Oral Dis 28 (6), 1509-1518 (2022)
   PUBMED   33675129
  REMARK    GeneRIF: MiR-873-5p modulates progression of tongue squamous cell
            carcinoma via targeting SEC11A.
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Liaci,A.M., Steigenberger,B., Telles de Souza,P.C., Tamara,S.,
            Grollers-Mulderij,M., Ogrissek,P., Marrink,S.J., Scheltema,R.A. and
            Forster,F.
  TITLE     Structure of the human signal peptidase complex reveals the
            determinants for signal peptide cleavage
  JOURNAL   Mol Cell 81 (19), 3934-3948 (2021)
   PUBMED   34388369
  REMARK    GeneRIF: Structure of the human signal peptidase complex reveals
            the determinants for signal peptide cleavage.
REFERENCE   5  (residues 1 to 164)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 164)
  AUTHORS   Oue,N., Naito,Y., Hayashi,T., Takigahira,M., Kawano-Nagatsuma,A.,
            Sentani,K., Sakamoto,N., Zarni Oo,H., Uraoka,N., Yanagihara,K.,
            Ochiai,A., Sasaki,H. and Yasui,W.
  TITLE     Signal peptidase complex 18, encoded by SEC11A, contributes to
            progression via TGF-alpha secretion in gastric cancer
  JOURNAL   Oncogene 33 (30), 3918-3926 (2014)
   PUBMED   23995782
  REMARK    GeneRIF: SPC18 contributes to malignant progression through
            promotion of TGF-alpha secretion in gastric cancer.
            Erratum:[Oncogene. 2019 Jul;38(28):5748. doi:
            10.1038/s41388-019-0837-z. PMID: 31175341]
REFERENCE   7  (residues 1 to 164)
  AUTHORS   Guffanti,A., Iacono,M., Pelucchi,P., Kim,N., Solda,G., Croft,L.J.,
            Taft,R.J., Rizzi,E., Askarian-Amiri,M., Bonnal,R.J., Callari,M.,
            Mignone,F., Pesole,G., Bertalot,G., Bernardi,L.R., Albertini,A.,
            Lee,C., Mattick,J.S., Zucchi,I. and De Bellis,G.
  TITLE     A transcriptional sketch of a primary human breast cancer by 454
            deep sequencing
  JOURNAL   BMC Genomics 10, 163 (2009)
   PUBMED   19379481
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 164)
  AUTHORS   Yasui,W., Oue,N., Sentani,K., Sakamoto,N. and Motoshita,J.
  TITLE     Transcriptome dissection of gastric cancer: identification of novel
            diagnostic and therapeutic targets from pathology specimens
  JOURNAL   Pathol Int 59 (3), 121-136 (2009)
   PUBMED   19261089
  REMARK    Review article
REFERENCE   9  (residues 1 to 164)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 164)
  AUTHORS   Shelness,G.S. and Blobel,G.
  TITLE     Two subunits of the canine signal peptidase complex are homologous
            to yeast SEC11 protein
  JOURNAL   J Biol Chem 265 (16), 9512-9519 (1990)
   PUBMED   2188978
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP370483.1, BG703137.1,
            BI545042.1, BF920344.1 and BM985046.1.
            
            Summary: This gene encodes a member of the peptidase S26B family.
            The encoded protein is an 18kDa subunit of the signal peptidase
            complex and has been linked to cell migration and invasion, gastric
            cancer and lymph node metastasis. Alternative splicing results in
            multiple transcript variants. A related pseudogene has been
            identified on chromosome 8. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (4) uses two alternate exons in
            the central coding region which results in a frameshift and an
            early stop codon, compared to variant 1. The encoded isoform (4) is
            longer and has a distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.31855.1, BI602694.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2-q25.3"
     Protein         1..164
                     /product="signal peptidase complex catalytic subunit
                     SEC11A isoform 4"
                     /EC_number="3.4.21.89"
                     /note="signal peptidase complex (18kD); signal peptidase
                     complex catalytic subunit SEC11A; endopeptidase SP18;
                     SEC11-like protein 1; SPase 18 kDa subunit; microsomal
                     signal peptidase 18 kDa subunit; signal peptidase complex
                     18"
                     /calculated_mol_wt=18857
     Site            17..36
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P67812.1)"
     Region          38..>122
                     /region_name="Peptidase_S24_S26"
                     /note="The S24, S26 LexA/signal peptidase superfamily
                     contains LexA-related and type I signal peptidase
                     families. The S24 LexA protein domains include: the lambda
                     repressor CI/C2 family and related bacterial prophage
                     repressor proteins; LexA (EC 3.4.21.88), the...; cl10465"
                     /db_xref="CDD:447902"
     Site            order(56,96)
                     /site_type="active"
                     /note="Catalytic site [active]"
                     /db_xref="CDD:119398"
     CDS             1..164
                     /gene="SEC11A"
                     /gene_synonym="1810012E07Rik; SEC11L1; sid2895; SPC18;
                     SPCS4A"
                     /coded_by="NM_001271920.2:65..559"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS61744.1"
                     /db_xref="GeneID:23478"
                     /db_xref="HGNC:HGNC:17718"
                     /db_xref="MIM:618258"
ORIGIN      
        1 mlsldflddv rrmnkrqlyy qvlnfgmivs salmiwkglm vitgsespiv vvlsgsmepa
       61 fhrgdllflt nrvedpirvg eivvfriegr eipivhrvlk ihekqnghik fltkgdnnav
      121 ddrglykqgq hwlekkdvvg rargfyqens svedrnylfl ilel
//
LOCUS       NP_001354411            1091 aa            linear   PRI 03-DEC-2025
DEFINITION  WD repeat-containing protein 64 [Homo sapiens].
ACCESSION   NP_001354411 XP_006711799
VERSION     NP_001354411.1
DBSOURCE    REFSEQ: accession NM_001367482.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1091)
  AUTHORS   McGue,M., Zhang,Y., Miller,M.B., Basu,S., Vrieze,S., Hicks,B.,
            Malone,S., Oetting,W.S. and Iacono,W.G.
  TITLE     A genome-wide association study of behavioral disinhibition
  JOURNAL   Behav Genet 43 (5), 363-373 (2013)
   PUBMED   23942779
REFERENCE   2  (residues 1 to 1091)
  AUTHORS   Niu,N., Qin,Y., Fridley,B.L., Hou,J., Kalari,K.R., Zhu,M., Wu,T.Y.,
            Jenkins,G.D., Batzler,A. and Wang,L.
  TITLE     Radiation pharmacogenomics: a genome-wide association approach to
            identify radiation response biomarkers using human lymphoblastoid
            cell lines
  JOURNAL   Genome Res 20 (11), 1482-1492 (2010)
   PUBMED   20923822
REFERENCE   3  (residues 1 to 1091)
  AUTHORS   McCauley,J.L., Zuvich,R.L., Bradford,Y., Kenealy,S.J.,
            Schnetz-Boutaud,N., Gregory,S.G., Hauser,S.L., Oksenberg,J.R.,
            Mortlock,D.P., Pericak-Vance,M.A. and Haines,J.L.
  TITLE     Follow-up examination of linkage and association to chromosome 1q43
            in multiple sclerosis
  JOURNAL   Genes Immun 10 (7), 624-630 (2009)
   PUBMED   19626040
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX322532.3, BX248405.4 and AL365366.20.
            
            On Dec 1, 2018 this sequence version replaced XP_006711799.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2148874 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000437684.7/ ENSP00000402446.4
            RefSeq Select criteria    :: based on manual assertion,
                                         conservation, expression, longest
                                         protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1091
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..1091
                     /product="WD repeat-containing protein 64"
                     /calculated_mol_wt=124619
     Region          102..152
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (B1ANS9.1)"
     Region          177..216
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          209..275
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (B1ANS9.1)"
     Region          221..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          276..324
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (B1ANS9.1)"
     Region          284..538
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(285..286,304,308,320,335..336,349,354,360..361,375,
                     392,397,403..404,416..417,440,444,450..451,463..464,482,
                     492..493,508..509,527,531,537..538)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          291..335
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          325..366
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (B1ANS9.1)"
     Region          340..373
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          367..410
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (B1ANS9.1)"
     Region          411..454
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (B1ANS9.1)"
     Region          455..498
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (B1ANS9.1)"
     Region          468..505
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          499..542
                     /region_name="WD 9"
                     /note="propagated from UniProtKB/Swiss-Prot (B1ANS9.1)"
     Region          508..904
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(509,527,531,537..538,556..557,579,583,602..603,
                     622..623,673,678,684..685,715,721,757..758,797,801,
                     807..808,822..823,841,846,862..863,875..876,894,898,904)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          514..549
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          543..641
                     /region_name="WD 10"
                     /note="propagated from UniProtKB/Swiss-Prot (B1ANS9.1)"
     Region          642..750
                     /region_name="WD 11"
                     /note="propagated from UniProtKB/Swiss-Prot (B1ANS9.1)"
     Region          736..767
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1ANS9.1)"
     Region          751..813
                     /region_name="WD 12"
                     /note="propagated from UniProtKB/Swiss-Prot (B1ANS9.1)"
     Region          814..867
                     /region_name="WD 13"
                     /note="propagated from UniProtKB/Swiss-Prot (B1ANS9.1)"
     Region          868..905
                     /region_name="WD 14"
                     /note="propagated from UniProtKB/Swiss-Prot (B1ANS9.1)"
     Region          1046..1070
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1ANS9.1)"
     CDS             1..1091
                     /gene="WDR64"
                     /coded_by="NM_001367482.1:205..3480"
                     /db_xref="CCDS:CCDS91185.1"
                     /db_xref="GeneID:128025"
                     /db_xref="HGNC:HGNC:26570"
                     /db_xref="MIM:621432"
ORIGIN      
        1 mdirkekrln malqmsnfkk alnrfeklve qtaaqkrder aglfihkeda igydkfyasv
       61 qklfgpdvkn qdvkrfyrkl cnntdasadw ceifgyfsse edpiasqlde enlvffvsrk
      121 rrilisgsrr rdviksivki phldllitat qkglitvfnn qmrvqtstnv tdtswitgcd
      181 yllqlkriva ttertiivwd ykaqgssqen yfvikpmdhc llcvcvvplp dhlcrddill
      241 gddggfvnrf tvnsddfgik qakskrklqn qvldsknfks vkrklhndwv mkiryisaln
      301 cfgscsldsn hslvleslkr lednlpvref smprgantfc ycvkanvivt ggddkvirlw
      361 hpnistkpvg klvghmfsia eivtnekdqh vvslssakvf rvwdiqtlsl lqvfhdsqgg
      421 pgdmqiysmi ydanhgmlit gssvmdmypl trmiqdtkqv phthereinv mlynkyfhqv
      481 lticsesiir vweletglqv yqilephgfn tevtsaavde sgflfatgay ngtvriwdfg
      541 sgqemkvlpe gkdwkedehc lrrliflkaq ekhqqlvlal erngtikmiq gkeddiylmv
      601 iwelpdvvpf lqdgkhavhl rmstrdrnma ipfpdveliv ernfsqptdn ptmdllrvnc
      661 idllqvegyn liaagtlngv iilwnfvtst vkkvyrpedc ftvnpdlhpk hfkindilfl
      721 frtpecarrs sqdsicsssq cesskgpqss kgskqsihds evkgeqtdvm vgkqqpmdkk
      781 hpgianlpea qppilvtahe dghlrlwtle grllkdmlpf tkhsaislts lytdsctril
      841 lagnveghvi lcnissfldp phdekkfkql lswrahslei iqviyveekq vvltasidgs
      901 vrlwhalngh ycgyfgqrrl felsqtrdfi lpcdvteypi eikeeskfte kqkyeyplif
      961 drekwrkmss vsllfkrtpp kafeveqdfk ffkslsspki rryplegfvt enreagivfg
     1021 slpiysissp tslrflplig veaqkdssdg itgkkkgghv qrekaprrrs lkknlvpqin
     1081 lassffpaip k
//
LOCUS       NP_055270                304 aa            linear   PRI 03-DEC-2025
DEFINITION  E3 ubiquitin-protein ligase RNF115 [Homo sapiens].
ACCESSION   NP_055270
VERSION     NP_055270.1
DBSOURCE    REFSEQ: accession NM_014455.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Zheng,M., Liu,W., Zhang,R., Jiang,D., Shi,Y., Wu,Y., Ge,F. and
            Chen,C.
  TITLE     E3 ubiquitin ligase BCA2 promotes breast cancer stemness by
            up-regulation of SOX9 by LPS
  JOURNAL   Int J Biol Sci 20 (7), 2686-2697 (2024)
   PUBMED   38725852
  REMARK    GeneRIF: E3 ubiquitin ligase BCA2 promotes breast cancer stemness
            by up-regulation of SOX9 by LPS.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Zhu,J., Guo,L., Dai,H., Zheng,Z., Yan,J., Liu,J., Zhang,S., Li,X.,
            Sun,X., Zhao,Q. and Xu,C.
  TITLE     RNF115 aggravates tumor progression through regulation of CDK10
            degradation in thyroid carcinoma
  JOURNAL   Cell Biol Toxicol 40 (1), 14 (2024)
   PUBMED   38376606
  REMARK    GeneRIF: RNF115 aggravates tumor progression through regulation of
            CDK10 degradation in thyroid carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Zhang,Z.D., Li,H.X., Gan,H., Tang,Z., Guo,Y.Y., Yao,S.Q., Liuyu,T.,
            Zhong,B. and Lin,D.
  TITLE     RNF115 Inhibits the Post-ER Trafficking of TLRs and TLRs-Mediated
            Immune Responses by Catalyzing K11-Linked Ubiquitination of RAB1A
            and RAB13
  JOURNAL   Adv Sci (Weinh) 9 (16), e2105391 (2022)
   PUBMED   35343654
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Shi,Y., Castro-Gonzalez,S., Chen,Y. and Serra-Moreno,R.
  TITLE     Effects of the SUMO Ligase BCA2 on Metabolic Activity, Cell
            Proliferation, Cell Migration, Cell Cycle, and the Regulation of
            NF-kappaB and IRF1 in Different Breast Epithelial Cellular Contexts
  JOURNAL   Front Cell Dev Biol 9, 711481 (2021)
   PUBMED   34589482
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Burger,A., Amemiya,Y., Kitching,R. and Seth,A.K.
  TITLE     Novel RING E3 ubiquitin ligases in breast cancer
  JOURNAL   Neoplasia 8 (8), 689-695 (2006)
   PUBMED   16925951
  REMARK    GeneRIF: BCA2 E3 ligase is coregulated with estrogen receptor and
            plays a role in the regulation of epidermal growth factor receptor
            (EGF-R) trafficking
            Review article
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Burger,A.M., Gao,Y., Amemiya,Y., Kahn,H.J., Kitching,R., Yang,Y.,
            Sun,P., Narod,S.A., Hanna,W.M. and Seth,A.K.
  TITLE     A novel RING-type ubiquitin ligase breast cancer-associated gene 2
            correlates with outcome in invasive breast cancer
  JOURNAL   Cancer Res 65 (22), 10401-10412 (2005)
   PUBMED   16288031
  REMARK    GeneRIF: The autoubiquitination activity of BCA2 indicates that it
            is a novel RING-type E3 ligase.
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Mizuno,K., Kitamura,A. and Sasaki,T.
  TITLE     Rabring7, a novel Rab7 target protein with a RING finger motif
  JOURNAL   Mol Biol Cell 14 (9), 3741-3752 (2003)
   PUBMED   12972561
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Suzuki,H., Fukunishi,Y., Kagawa,I., Saito,R., Oda,H., Endo,T.,
            Kondo,S., Bono,H., Okazaki,Y. and Hayashizaki,Y.
  TITLE     Protein-protein interaction panel using mouse full-length cDNAs
  JOURNAL   Genome Res 11 (10), 1758-1765 (2001)
   PUBMED   11591653
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Chow,J.C., Young,D.W., Golenbock,D.T., Christ,W.J. and Gusovsky,F.
  TITLE     Toll-like receptor-4 mediates lipopolysaccharide-induced signal
            transduction
  JOURNAL   J Biol Chem 274 (16), 10689-10692 (1999)
   PUBMED   10196138
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG684824.1, AF419857.1, AC242845.1 and HY099262.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.91383.1,
                                           SRR1803611.197630.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000582693.5/ ENSP00000463650.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.1"
     Protein         1..304
                     /product="E3 ubiquitin-protein ligase RNF115"
                     /EC_number="2.3.2.27"
                     /note="zinc finger protein 364; rabring 7; RING-type E3
                     ubiquitin transferase RNF115; rab7-interacting RING finger
                     protein; Breast cancer-associated gene 2"
                     /calculated_mol_wt=33572
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4L5.2)"
     Region          19..49
                     /region_name="zinc_ribbon_9"
                     /note="zinc-ribbon; pfam14369"
                     /db_xref="CDD:433910"
     Region          95..138
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4L5.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:35343654; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4L5.2)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:35343654; propagated from
                     UniProtKB/Swiss-Prot (Q9Y4L5.2)"
     Region          226..275
                     /region_name="RING-H2_RNF115"
                     /note="RING finger, H2 subclass, found in RING finger
                     protein 115 (RNF115) and similar proteins; cd16800"
                     /db_xref="CDD:438452"
     Region          272..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4L5.2)"
     CDS             1..304
                     /gene="RNF115"
                     /gene_synonym="BCA2; RABRING7; ZFP364; ZNF364"
                     /coded_by="NM_014455.4:223..1137"
                     /db_xref="CCDS:CCDS72863.1"
                     /db_xref="GeneID:27246"
                     /db_xref="HGNC:HGNC:18154"
                     /db_xref="MIM:619535"
ORIGIN      
        1 maeasaagad sgaavaahrf fchfckgevs pklpeyicpr cesgfieevt ddssflgggg
       61 sridntttth faelwghldh tmffqdfrpf lssspldqdn ranerghqth tdfwgarppr
      121 lplgrryrsr gssrpdrspa iegilqhifa gffansaipg sphpfswsgm lhsnpgdyaw
      181 gqtgldaivt qllgqlentg pppadkekit slptvtvtqe qvdmglecpv ckedytveee
      241 vrqlpcnhff hsscivpwle lhdtcpvcrk slngedstrq sqsteasasn rfsndsqlhd
      301 rwtf
//
LOCUS       NP_653223                773 aa            linear   PRI 03-DEC-2025
DEFINITION  DC-STAMP domain-containing protein 2 [Homo sapiens].
ACCESSION   NP_653223
VERSION     NP_653223.2
DBSOURCE    REFSEQ: accession NM_144622.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Inoue,N., Hagihara,Y. and Wada,I.
  TITLE     Evolutionarily conserved sperm factors, DCST1 and DCST2, are
            required for gamete fusion
  JOURNAL   Elife 10, e66313 (2021)
   PUBMED   33871360
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 773)
  AUTHORS   van der Valk,R.J., Kreiner-Moller,E., Kooijman,M.N., Guxens,M.,
            Stergiakouli,E., Saaf,A., Bradfield,J.P., Geller,F., Hayes,M.G.,
            Cousminer,D.L., Korner,A., Thiering,E., Curtin,J.A., Myhre,R.,
            Huikari,V., Joro,R., Kerkhof,M., Warrington,N.M., Pitkanen,N.,
            Ntalla,I., Horikoshi,M., Veijola,R., Freathy,R.M., Teo,Y.Y.,
            Barton,S.J., Evans,D.M., Kemp,J.P., St Pourcain,B., Ring,S.M.,
            Davey Smith,G., Bergstrom,A., Kull,I., Hakonarson,H., Mentch,F.D.,
            Bisgaard,H., Chawes,B., Stokholm,J., Waage,J., Eriksen,P.,
            Sevelsted,A., Melbye,M., van Duijn,C.M., Medina-Gomez,C.,
            Hofman,A., de Jongste,J.C., Taal,H.R., Uitterlinden,A.G.,
            Armstrong,L.L., Eriksson,J., Palotie,A., Bustamante,M.,
            Estivill,X., Gonzalez,J.R., Llop,S., Kiess,W., Mahajan,A.,
            Flexeder,C., Tiesler,C.M., Murray,C.S., Simpson,A., Magnus,P.,
            Sengpiel,V., Hartikainen,A.L., Keinanen-Kiukaanniemi,S., Lewin,A.,
            Da Silva Couto Alves,A., Blakemore,A.I., Buxton,J.L., Kaakinen,M.,
            Rodriguez,A., Sebert,S., Vaarasmaki,M., Lakka,T., Lindi,V.,
            Gehring,U., Postma,D.S., Ang,W., Newnham,J.P., Lyytikainen,L.P.,
            Pahkala,K., Raitakari,O.T., Panoutsopoulou,K., Zeggini,E.,
            Boomsma,D.I., Groen-Blokhuis,M., Ilonen,J., Franke,L.,
            Hirschhorn,J.N., Pers,T.H., Liang,L., Huang,J., Hocher,B., Knip,M.,
            Saw,S.M., Holloway,J.W., Melen,E., Grant,S.F., Feenstra,B.,
            Lowe,W.L., Widen,E., Sergeyev,E., Grallert,H., Custovic,A.,
            Jacobsson,B., Jarvelin,M.R., Atalay,M., Koppelman,G.H.,
            Pennell,C.E., Niinikoski,H., Dedoussis,G.V., Mccarthy,M.I.,
            Frayling,T.M., Sunyer,J., Timpson,N.J., Rivadeneira,F.,
            Bonnelykke,K. and Jaddoe,V.W.
  CONSRTM   Early Genetics and Lifecourse Epidemiology (EAGLE) Consortium;
            Genetic Investigation of ANthropometric Traits (GIANT) Consortium;
            Early Growth Genetics (EGG) Consortium
  TITLE     A novel common variant in DCST2 is associated with length in early
            life and height in adulthood
  JOURNAL   Hum Mol Genet 24 (4), 1155-1168 (2015)
   PUBMED   25281659
  REMARK    GeneRIF: This study highlights that common variation in DCST2
            influences variation in early growth and adult height.
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Eeles,R.A., Olama,A.A., Benlloch,S., Saunders,E.J.,
            Leongamornlert,D.A., Tymrakiewicz,M., Ghoussaini,M., Luccarini,C.,
            Dennis,J., Jugurnauth-Little,S., Dadaev,T., Neal,D.E., Hamdy,F.C.,
            Donovan,J.L., Muir,K., Giles,G.G., Severi,G., Wiklund,F.,
            Gronberg,H., Haiman,C.A., Schumacher,F., Henderson,B.E., Le
            Marchand,L., Lindstrom,S., Kraft,P., Hunter,D.J., Gapstur,S.,
            Chanock,S.J., Berndt,S.I., Albanes,D., Andriole,G., Schleutker,J.,
            Weischer,M., Canzian,F., Riboli,E., Key,T.J., Travis,R.C.,
            Campa,D., Ingles,S.A., John,E.M., Hayes,R.B., Pharoah,P.D.,
            Pashayan,N., Khaw,K.T., Stanford,J.L., Ostrander,E.A.,
            Signorello,L.B., Thibodeau,S.N., Schaid,D., Maier,C., Vogel,W.,
            Kibel,A.S., Cybulski,C., Lubinski,J., Cannon-Albright,L.,
            Brenner,H., Park,J.Y., Kaneva,R., Batra,J., Spurdle,A.B.,
            Clements,J.A., Teixeira,M.R., Dicks,E., Lee,A., Dunning,A.M.,
            Baynes,C., Conroy,D., Maranian,M.J., Ahmed,S., Govindasami,K.,
            Guy,M., Wilkinson,R.A., Sawyer,E.J., Morgan,A., Dearnaley,D.P.,
            Horwich,A., Huddart,R.A., Khoo,V.S., Parker,C.C., Van As,N.J.,
            Woodhouse,C.J., Thompson,A., Dudderidge,T., Ogden,C., Cooper,C.S.,
            Lophatananon,A., Cox,A., Southey,M.C., Hopper,J.L., English,D.R.,
            Aly,M., Adolfsson,J., Xu,J., Zheng,S.L., Yeager,M., Kaaks,R.,
            Diver,W.R., Gaudet,M.M., Stern,M.C., Corral,R., Joshi,A.D.,
            Shahabi,A., Wahlfors,T., Tammela,T.L., Auvinen,A., Virtamo,J.,
            Klarskov,P., Nordestgaard,B.G., Roder,M.A., Nielsen,S.F.,
            Bojesen,S.E., Siddiq,A., Fitzgerald,L.M., Kolb,S., Kwon,E.M.,
            Karyadi,D.M., Blot,W.J., Zheng,W., Cai,Q., McDonnell,S.K.,
            Rinckleb,A.E., Drake,B., Colditz,G., Wokolorczyk,D.,
            Stephenson,R.A., Teerlink,C., Muller,H., Rothenbacher,D.,
            Sellers,T.A., Lin,H.Y., Slavov,C., Mitev,V., Lose,F.,
            Srinivasan,S., Maia,S., Paulo,P., Lange,E., Cooney,K.A.,
            Antoniou,A.C., Vincent,D., Bacot,F., Tessier,D.C., Kote-Jarai,Z.
            and Easton,D.F.
  CONSRTM   COGS-Cancer Research UK GWAS-ELLIPSE (part of GAME-ON) Initiative;
            Australian Prostate Cancer Bioresource; UK Genetic Prostate Cancer
            Study Collaborators/British Association of Urological Surgeons'
            Section of Oncology; UK ProtecT (Prostate testing for cancer and
            Treatment) Study Collaborators; PRACTICAL (Prostate Cancer
            Association Group to Investigate Cancer-Associated Alterations in
            the Genome) Consortium
  TITLE     Identification of 23 new prostate cancer susceptibility loci using
            the iCOGS custom genotyping array
  JOURNAL   Nat Genet 45 (4), 385-391 (2013)
   PUBMED   23535732
REFERENCE   4  (residues 1 to 773)
  AUTHORS   Jansen,B.J., Eleveld-Trancikova,D., Sanecka,A., van Hout-Kuijer,M.,
            Hendriks,I.A., Looman,M.G., Leusen,J.H. and Adema,G.J.
  TITLE     OS9 interacts with DC-STAMP and modulates its intracellular
            localization in response to TLR ligation
  JOURNAL   Mol Immunol 46 (4), 505-515 (2009)
   PUBMED   18952287
  REMARK    GeneRIF: OS9 is critically involved in the modulation of
            ER-to-Golgi transport of DC-STAMP in response to TLR triggering,
            suggesting a novel role for OS9 in myeloid differentiation and cell
            fusion.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB025590.1, BC111794.1 and AA401747.1.
            
            On Jun 17, 2006 this sequence version replaced NP_653223.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC111794.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368424.4/ ENSP00000357409.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..773
                     /product="DC-STAMP domain-containing protein 2"
                     /calculated_mol_wt=86099
     Site            27..47
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1A1.2)"
     Site            52..72
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1A1.2)"
     Site            234..254
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1A1.2)"
     Site            284
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5T1A1.2)"
     Site            296
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5T1A1.2)"
     Site            323..343
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1A1.2)"
     Region          354..544
                     /region_name="DC_STAMP"
                     /note="DC-STAMP-like protein; pfam07782"
                     /db_xref="CDD:462265"
     Site            416..436
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1A1.2)"
     Site            480
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5T1A1.2)"
     Site            500..520
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1A1.2)"
     Region          692..773
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1A1.2)"
     CDS             1..773
                     /gene="DCST2"
                     /gene_synonym="SPE42"
                     /coded_by="NM_144622.3:81..2402"
                     /db_xref="CCDS:CCDS1082.2"
                     /db_xref="GeneID:127579"
                     /db_xref="HGNC:HGNC:26562"
                     /db_xref="MIM:619861"
ORIGIN      
        1 mpkvmkdvvh plggeepsma ravvrsvggf tlglslatay gllellvegh spwgclvgtl
       61 tlaaflslgm gfsrqvratv llllpqafsr qgrtlllvaa fglvlqgpca ntlrnftras
      121 eavacgaela lnqtaevlqr akqplvsaln kikaiarktk evadrvrkff rsimdgvkhi
      181 aralrnvwqw llhigdvcns elgnpylkca rvfddakdsc mmvipqayhl cyvlmpfkla
      241 lcglaslvqv fcvipkyiqp flrqtigtpv iqllnrvrqe fefnmtathh fsvdlnasrs
      301 lsqvamdlhe avsmklhrvr ealalmgftt plllvllylq alfyrycyln wdhydniyit
      361 srflrmeavr staglptvlp lsahearryi ppgsiflsqw ekffyiletf nlirhlllvl
      421 flvfldyavf wvldlarhql qgeivarspv lvsltvegtg yagniyrdlv safdvlqqgn
      481 isilsrrcll rpsepdstgy ivigvmyglc ffitlfgsyv srlrrvicas yypsreqeri
      541 sylynvllsr rtnllaalhr svrrraadqg hrsaflvlas rcpclgpfvs hfwlhqaycl
      601 gcgqpqdegd mentvscstp gcqglycltc frlldntcsv casplsyqgd ldleldssde
      661 egpqlwlaaa qrkdpeqawl lqqqlqevlg rslsmestse ssdldeekgp qqrkhgqqpl
      721 peahqpvsil tspephrppe tssatkgapt pasepsvpls ppslpdpshp ppk
//
LOCUS       NP_004139                152 aa            linear   PRI 03-DEC-2025
DEFINITION  ninjurin-1 [Homo sapiens].
ACCESSION   NP_004139
VERSION     NP_004139.2
DBSOURCE    REFSEQ: accession NM_004148.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Wang,C., Dreyer,B., Teran,E. and Ruan,J.
  TITLE     From pores to rupture: Structural basis and regulation of lytic
            cell death by gasdermins and NINJ1
  JOURNAL   J Biol Chem 301 (10), 110698 (2025)
   PUBMED   40946739
  REMARK    Review article
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Sahoo,B., Mou,Z., Liu,W., Dubyak,G. and Dai,X.
  TITLE     How NINJ1 mediates plasma membrane rupture and why NINJ2 cannot
  JOURNAL   Cell 188 (2), 292-302 (2025)
   PUBMED   39667936
REFERENCE   3  (residues 1 to 152)
  AUTHORS   David,L., Borges,J.P., Hollingsworth,L.R., Volchuk,A., Jansen,I.,
            Garlick,E., Steinberg,B.E. and Wu,H.
  TITLE     NINJ1 mediates plasma membrane rupture by cutting and releasing
            membrane disks
  JOURNAL   Cell 187 (9), 2224-2235 (2024)
   PUBMED   38614101
REFERENCE   4  (residues 1 to 152)
  AUTHORS   Ramos,S., Hartenian,E., Santos,J.C., Walch,P. and Broz,P.
  TITLE     NINJ1 induces plasma membrane rupture and release of
            damage-associated molecular pattern molecules during ferroptosis
  JOURNAL   EMBO J 43 (7), 1164-1186 (2024)
   PUBMED   38396301
REFERENCE   5  (residues 1 to 152)
  AUTHORS   Sheng,Y., Wu,L., Chang,Y., Liu,W., Tao,M., Chen,X., Zhang,X.,
            Li,B., Zhang,N., Ye,D., Zhang,C., Zhu,D., Zhao,H., Chen,A., Chen,H.
            and Song,J.
  TITLE     Tomo-seq identifies NINJ1 as a potential target for
            anti-inflammatory strategy in thoracic aortic dissection
  JOURNAL   BMC Med 21 (1), 396 (2023)
   PUBMED   37858098
  REMARK    GeneRIF: Tomo-seq identifies NINJ1 as a potential target for
            anti-inflammatory strategy in thoracic aortic dissection.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 152)
  AUTHORS   Toyama,T., Sasaki,Y., Horimoto,M., Iyoda,K., Yakushijin,T.,
            Ohkawa,K., Takehara,T., Kasahara,A., Araki,T., Hori,M. and
            Hayashi,N.
  TITLE     Ninjurin1 increases p21 expression and induces cellular senescence
            in human hepatoma cells
  JOURNAL   J Hepatol 41 (4), 637-643 (2004)
   PUBMED   15464245
  REMARK    GeneRIF: Ninjurin1 is able to induce the senescence program.
            Ninjurin1 may be involved in the regulation of cellular senescence
            in the liver during carcinogenesis.
REFERENCE   7  (residues 1 to 152)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   8  (residues 1 to 152)
  AUTHORS   Chadwick,B.P., Heath,S.K., Williamson,J., Obermayr,F., Patel,L.,
            Sheer,D. and Frischauf,A.M.
  TITLE     The human homologue of the ninjurin gene maps to the candidate
            region of hereditary sensory neuropathy type I (HSNI)
  JOURNAL   Genomics 47 (1), 58-63 (1998)
   PUBMED   9465296
REFERENCE   9  (residues 1 to 152)
  AUTHORS   Araki,T., Zimonjic,D.B., Popescu,N.C. and Milbrandt,J.
  TITLE     Mechanism of homophilic binding mediated by ninjurin, a novel
            widely expressed adhesion molecule
  JOURNAL   J Biol Chem 272 (34), 21373-21380 (1997)
   PUBMED   9261151
REFERENCE   10 (residues 1 to 152)
  AUTHORS   Araki,T. and Milbrandt,J.
  TITLE     Ninjurin, a novel adhesion molecule, is induced by nerve injury and
            promotes axonal growth
  JOURNAL   Neuron 17 (2), 353-361 (1996)
   PUBMED   8780658
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL451065.13.
            
            On Jun 19, 2007 this sequence version replaced NP_004139.1.
            
            Summary: The ninjurin protein is upregulated after nerve injury
            both in dorsal root ganglion neurons and in Schwann cells (Araki
            and Milbrandt, 1996 [PubMed 8780658]). It demonstrates properties
            of a homophilic adhesion molecule and promotes neurite outgrowth
            from primary cultured dorsal root ganglion neurons.[supplied by
            OMIM, Aug 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.658452.1, BC048212.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375446.5/ ENSP00000364595.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.31"
     Protein         1..152
                     /product="ninjurin-1"
                     /note="nerve injury-induced protein-1"
                     /calculated_mol_wt=16214
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92982.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q92982.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70617; propagated from
                     UniProtKB/Swiss-Prot (Q92982.2)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70617; propagated from
                     UniProtKB/Swiss-Prot (Q92982.2)"
     Region          26..37
                     /region_name="N-terminal adhesion motif.
                     /evidence=ECO:0000269|PubMed:33028854"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92982.2)"
     Region          38..139
                     /region_name="Ninjurin"
                     /note="pfam04923"
                     /db_xref="CDD:461482"
     Region          40..69
                     /region_name="Required to induce plasma membrane rupture.
                     /evidence=ECO:0000250|UniProtKB:O70131"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92982.2)"
     Region          44..55
                     /region_name="Helix alpha1.
                     /evidence=ECO:0000269|PubMed:37198476,
                     ECO:0000269|PubMed:39667936, ECO:0007744|PDB:8SZA"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92982.2)"
     Site            56..57
                     /site_type="cleavage"
                     /note="Cleavage, by MMP9.
                     /evidence=ECO:0000250|UniProtKB:O70131; propagated from
                     UniProtKB/Swiss-Prot (Q92982.2)"
     Region          58..74
                     /region_name="Helix alpha2.
                     /evidence=ECO:0000269|PubMed:37198476,
                     ECO:0000269|PubMed:39667936, ECO:0007744|PDB:8SZA"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92982.2)"
     Site            60
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q92982.2)"
     Site            79..103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92982.2)"
     Site            114..138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92982.2)"
     CDS             1..152
                     /gene="NINJ1"
                     /gene_synonym="hNINJ1; NIN1; NINJURIN"
                     /coded_by="NM_004148.4:35..493"
                     /db_xref="CCDS:CCDS6703.1"
                     /db_xref="GeneID:4814"
                     /db_xref="HGNC:HGNC:7824"
                     /db_xref="MIM:602062"
ORIGIN      
        1 mdsgteeyel ngglppgtpg spdasparwg wrhgpinvnh yaskksaaes mldiallman
       61 asqlkavveq gpsfafyvpl vvlisislvl qigvgvllif lvkydlnnpa khakldflnn
      121 latglvfiiv vvnifitafg vqkplmdmap qq
//
LOCUS       NP_005592                165 aa            linear   PRI 03-DEC-2025
DEFINITION  protein NKG7 isoform 1 [Homo sapiens].
ACCESSION   NP_005592
VERSION     NP_005592.1
DBSOURCE    REFSEQ: accession NM_005601.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Ham,H., Hirdler,J.B., Bihnam,D.T., Mao,Z., Gicobi,J.K.,
            Macedo,B.G., Rodriguez-Quevedo,M.F., Schultz,D.F., Correia,C.,
            Zhong,J., Martinez,K.E., Banuelos,A., Ashton,D.S., Lagnado,A.B.,
            Guo,R., Pessoa,R., Pandey,A., Li,H., Lucien,F., Borges da Silva,H.,
            Dong,H. and Billadeau,D.D.
  TITLE     Lysosomal NKG7 restrains mTORC1 activity to promote CD8+ T cell
            durability and tumor control
  JOURNAL   Nat Commun 16 (1), 1628 (2025)
   PUBMED   39952956
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Ng,S.S., De Labastida Rivera,F., Yan,J., Corvino,D., Das,I.,
            Zhang,P., Kuns,R., Chauhan,S.B., Hou,J., Li,X.Y., Frame,T.C.M.,
            McEnroe,B.A., Moore,E., Na,J., Engel,J.A., Soon,M.S.F., Singh,B.,
            Kueh,A.J., Herold,M.J., Montes de Oca,M., Singh,S.S., Bunn,P.T.,
            Aguilera,A.R., Casey,M., Braun,M., Ghazanfari,N., Wani,S., Wang,Y.,
            Amante,F.H., Edwards,C.L., Haque,A., Dougall,W.C., Singh,O.P.,
            Baxter,A.G., Teng,M.W.L., Loukas,A., Daly,N.L., Cloonan,N.,
            Degli-Esposti,M.A., Uzonna,J., Heath,W.R., Bald,T., Tey,S.K.,
            Nakamura,K., Hill,G.R., Kumar,R., Sundar,S., Smyth,M.J. and
            Engwerda,C.R.
  TITLE     The NK cell granule protein NKG7 regulates cytotoxic granule
            exocytosis and inflammation
  JOURNAL   Nat Immunol 21 (10), 1205-1218 (2020)
   PUBMED   32839608
  REMARK    Erratum:[Nat Immunol. 2024 Apr;25(4):716. doi:
            10.1038/s41590-024-01770-8. PMID: 38360937]
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Medley,Q.G., Kedersha,N., O'Brien,S., Tian,Q., Schlossman,S.F.,
            Streuli,M. and Anderson,P.
  TITLE     Characterization of GMP-17, a granule membrane protein that moves
            to the plasma membrane of natural killer cells following target
            cell recognition
  JOURNAL   Proc Natl Acad Sci U S A 93 (2), 685-689 (1996)
   PUBMED   8570616
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Shimane,M., Tani,K., Maruyama,K., Takahashi,S., Ozawa,K. and
            Asano,S.
  TITLE     Molecular cloning and characterization of G-CSF induced gene cDNA
  JOURNAL   Biochem Biophys Res Commun 199 (1), 26-32 (1994)
   PUBMED   7510105
REFERENCE   7  (residues 1 to 165)
  AUTHORS   Turman,M.A., Yabe,T., McSherry,C., Bach,F.H. and Houchins,J.P.
  TITLE     Characterization of a novel gene (NKG7) on human chromosome 19 that
            is expressed in natural killer cells and T cells
  JOURNAL   Hum Immunol 36 (1), 34-40 (1993)
   PUBMED   8458737
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            S69115.1 and AI313472.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BQ052401.1, S69115.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144835, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221978.10/ ENSP00000221978.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..165
                     /product="protein NKG7 isoform 1"
                     /note="protein NKG7; GIG-1 protein; G-CSF-induced gene 1
                     protein; natural killer cell protein 7; granule membrane
                     protein of 17 kDa; granule membrane protein 17; natural
                     killer cell group 7 sequence"
                     /calculated_mol_wt=17533
     Site            9..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16617.1)"
     Region          21..149
                     /region_name="PMP22_Claudin"
                     /note="PMP-22/EMP/MP20/Claudin family; cl21598"
                     /db_xref="CDD:473919"
     Site            61..81
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16617.1)"
     Site            92..112
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16617.1)"
     Site            133..153
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16617.1)"
     CDS             1..165
                     /gene="NKG7"
                     /gene_synonym="GIG1; GMP-17; p15-TIA-1"
                     /coded_by="NM_005601.4:120..617"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12830.1"
                     /db_xref="GeneID:4818"
                     /db_xref="HGNC:HGNC:7830"
                     /db_xref="MIM:606008"
ORIGIN      
        1 melcrslall ggslglmfcl ialstdfwfe avgpthsahs glwptghgdi isgyihvtqt
       61 fsimavlwal vsvsflvlsc fpslfppghg plvsttaafa aaismvvama vytserwdqp
      121 phpqiqtffs wsfylgwvsa illlctgals lgahcggprp gyetl
//
LOCUS       NP_001335116             796 aa            linear   PRI 03-DEC-2025
DEFINITION  probable ATP-dependent RNA helicase DDX27 isoform 1 [Homo sapiens].
ACCESSION   NP_001335116 XP_011527190
VERSION     NP_001335116.2
DBSOURCE    REFSEQ: accession NM_001348187.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Li,G., Li,R., Wang,W., Sun,M. and Wang,X.
  TITLE     DDX27 regulates oral squamous cell carcinoma development through
            targeting CSE1L
  JOURNAL   Life Sci 340, 122479 (2024)
   PUBMED   38301874
  REMARK    GeneRIF: DDX27 regulates oral squamous cell carcinoma development
            through targeting CSE1L.
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Li,S., Ma,J., Zheng,A., Song,X., Chen,S. and Jin,F.
  TITLE     DEAD-box helicase 27 enhances stem cell-like properties with poor
            prognosis in breast cancer
  JOURNAL   J Transl Med 19 (1), 334 (2021)
   PUBMED   34362383
  REMARK    GeneRIF: DEAD-box helicase 27 enhances stem cell-like properties
            with poor prognosis in breast cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 796)
  AUTHORS   Xiaoqian,W., Bing,Z., Yangwei,L., Yafei,Z., Tingting,Z., Yi,W.,
            Qingjun,L., Suxia,L., Ling,Z., Bo,W. and Peng,Z.
  TITLE     DEAD-box Helicase 27 Promotes Hepatocellular Carcinoma Progression
            Through ERK Signaling
  JOURNAL   Technol Cancer Res Treat 20, 15330338211055953 (2021)
   PUBMED   34855554
  REMARK    GeneRIF: DEAD-box Helicase 27 Promotes Hepatocellular Carcinoma
            Progression Through ERK Signaling.
REFERENCE   5  (residues 1 to 796)
  AUTHORS   Tang,J., Chen,H., Wong,C.C., Liu,D., Li,T., Wang,X., Ji,J.,
            Sung,J.J., Fang,J.Y. and Yu,J.
  TITLE     DEAD-box helicase 27 promotes colorectal cancer growth and
            metastasis and predicts poor survival in CRC patients
  JOURNAL   Oncogene 37 (22), 3006-3021 (2018)
   PUBMED   29535419
  REMARK    GeneRIF: Data found that DDX27 expression is significantly
            up-regulated in colorectal cancer (CRC) at mRNA and protein levels.
            DDX27 mRNA overexpression was positively correlated with DNA copy
            number gain and associated with poor prognosis in CRC patients.
            Further evidences prove that DDX27 plays a pivotal oncogenic role
            in CRC.
REFERENCE   6  (residues 1 to 796)
  AUTHORS   Bennett,A.H., O'Donohue,M.F., Gundry,S.R., Chan,A.T., Widrick,J.,
            Draper,I., Chakraborty,A., Zhou,Y., Zon,L.I., Gleizes,P.E.,
            Beggs,A.H. and Gupta,V.A.
  TITLE     RNA helicase, DDX27 regulates skeletal muscle growth and
            regeneration by modulation of translational processes
  JOURNAL   PLoS Genet 14 (3), e1007226 (2018)
   PUBMED   29518074
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 796)
  AUTHORS   Tsukamoto,Y., Fumoto,S., Noguchi,T., Yanagihara,K., Hirashita,Y.,
            Nakada,C., Hijiya,N., Uchida,T., Matsuura,K., Hamanaka,R.,
            Murakami,K., Seto,M., Inomata,M. and Moriyama,M.
  TITLE     Expression of DDX27 contributes to colony-forming ability of
            gastric cancer cells and correlates with poor prognosis in gastric
            cancer
  JOURNAL   Am J Cancer Res 5 (10), 2998-3014 (2015)
   PUBMED   26693055
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 796)
  AUTHORS   Kellner,M., Rohrmoser,M., Forne,I., Voss,K., Burger,K., Muhl,B.,
            Gruber-Eber,A., Kremmer,E., Imhof,A. and Eick,D.
  TITLE     DEAD-box helicase DDX27 regulates 3' end formation of ribosomal 47S
            RNA and stably associates with the PeBoW-complex
  JOURNAL   Exp Cell Res 334 (1), 146-159 (2015)
   PUBMED   25825154
  REMARK    GeneRIF: The DDX27 can interact specifically with the Pes1 and Bop1
            but fulfils critical function(s) for proper 3' end formation of 47S
            rRNA independently of the PeBoW-complex.
REFERENCE   9  (residues 1 to 796)
  AUTHORS   Zhou,J., Yong,W.P., Yap,C.S., Vijayaraghavan,A., Sinha,R.A.,
            Singh,B.K., Xiu,S., Manesh,S., Ngo,A., Lim,A., Ang,C., Xie,C.,
            Wong,F.Y., Lin,S.J., Wan,W.K., Tan,I.B., Flotow,H., Tan,P.,
            Lim,K.H., Yen,P.M. and Goh,L.K.
  TITLE     An integrative approach identified genes associated with drug
            response in gastric cancer
  JOURNAL   Carcinogenesis 36 (4), 441-451 (2015)
   PUBMED   25742747
  REMARK    GeneRIF: Levels of DDX27 mRNA and protein were increased in
            early-stage gastric tumors, and may be a potential diagnostic and
            prognostic marker for Gastric cancer.
REFERENCE   10 (residues 1 to 796)
  AUTHORS   Ohta,S., Bukowski-Wills,J.C., Sanchez-Pulido,L., Alves Fde,L.,
            Wood,L., Chen,Z.A., Platani,M., Fischer,L., Hudson,D.F.,
            Ponting,C.P., Fukagawa,T., Earnshaw,W.C. and Rappsilber,J.
  TITLE     The protein composition of mitotic chromosomes determined using
            multiclassifier combinatorial proteomics
  JOURNAL   Cell 142 (5), 810-821 (2010)
   PUBMED   20813266
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL357560.11 and AL049766.14.
            
            On Jul 17, 2020 this sequence version replaced NP_001335116.1.
            
            Summary: DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this family
            are believed to be involved in embryogenesis, spermatogenesis, and
            cellular growth and division. This gene encodes a DEAD box protein
            involved in the processing of 5.8S and 28S ribosomal RNAs. More
            specifically, the encoded protein localizes to the nucleolus, where
            it interacts with the PeBoW complex to ensure proper 3' end
            formation of 47S rRNA. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2213992.1,
                                           SRR14038196.2895387.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.13"
     Protein         1..796
                     /product="probable ATP-dependent RNA helicase DDX27
                     isoform 1"
                     /EC_number="3.6.4.13"
                     /note="DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 27;
                     probable ATP-dependent RNA helicase DDX27; RNA
                     helicase-like protein; DEAD (Asp-Glu-Ala-Asp) box
                     polypeptide 27; DEAD box protein 27; Deficiency of
                     ribosomal subunits protein 1 homolog"
                     /calculated_mol_wt=89850
     Region          188..608
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     CDS             1..796
                     /gene="DDX27"
                     /gene_synonym="dJ686N3.1; DRS1; Drs1p; HSPC259; PP3241;
                     RHLP"
                     /coded_by="NM_001348187.2:34..2424"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:55661"
                     /db_xref="HGNC:HGNC:15837"
                     /db_xref="MIM:616621"
ORIGIN      
        1 mladlgligt igeddevpve pesdsgdeee egpivlgrrq kalgknrsad fnpdfvftek
       61 egtydgswal advmsqlkkk raattldeki ekvrkkrkte dkeaksgkle kekeakegse
      121 pkeqedlqen deegsedeas etdyssaden iltkadtlkv kdrkkkkkkg qeaggffeda
      181 sqydenlsfq dmnlsrpllk aitamgfkqp tpiqkacipv gllgkdicac aatgtgktaa
      241 falpvlerli ykprqapvtr vlvlvptrel giqvhsvtrq laqfcnittc lavggldvks
      301 qeaalraapd iliatpgrli dhlhncpsfh lssievlild eadsppvdta wphaptlwll
      361 hlpfpqpgai scpfrmldey feeqmkeiir mcshhrqtml fsatmtdevk dlasvslknp
      421 vrifvnsntd vapflrqefi rirpnregdr eaivaalltr tftdhvmlft qtkkqahrmh
      481 illglmglqv gelhgnlsqt qrlealrrfk deqidilvat dvaargldie gvktvinftm
      541 pntikhyvhr vgrtaragra grsvslvged erkmlkeivk aakapvkari lpqdvilkfr
      601 dkiekmekdv yavlqleaee kemqqseaqi ntakrllekg keavvqeper swfqtkeerk
      661 kekiakalqe fdlalrgkkk rkkfmkdakk kgemtaeers qfeilkaqmf aerlakrnrr
      721 akrarampee epvrgpakkq kqgkksvfde eltntskkal kqyragpsfe erkqlglphq
      781 rrggnfksks rykrrk
//
LOCUS       NP_001352821             402 aa            linear   PRI 03-DEC-2025
DEFINITION  coiled-coil domain-containing protein 188 [Homo sapiens].
ACCESSION   NP_001352821 XP_005261297
VERSION     NP_001352821.1
DBSOURCE    REFSEQ: accession NM_001365892.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Yang,X., Wang,Y., Yu,K., Xiang,M., Zhang,J., Duan,Z., Zhou,Y.,
            Zha,X., Li,H., Wang,F., Cao,Y. and Zhu,F.
  TITLE     Novel CCDC188 variants cause acephalic spermatozoa syndrome with
            poor intracytoplasmic sperm injection outcome
  JOURNAL   J Assist Reprod Genet 42 (11), 3755-3765 (2025)
   PUBMED   41004021
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Qiu,Y., Shimada,K., Yamamoto,K. and Ikawa,M.
  TITLE     Loss of CCDC188 causes male infertility with defects in the sperm
            head-neck connection in micedagger
  JOURNAL   Biol Reprod 112 (1), 169-178 (2025)
   PUBMED   39292630
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006547.9.
            
            On Sep 15, 2018 this sequence version replaced XP_005261297.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1968189
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000439765.4/ ENSP00000409542.2
            RefSeq Select criteria    :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..402
                     /product="coiled-coil domain-containing protein 188"
                     /calculated_mol_wt=43417
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (H7C350.2)"
     Region          50..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (H7C350.2)"
     Region          108..131
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (H7C350.2)"
     Region          <158..184
                     /region_name="bZIP"
                     /note="Basic leucine zipper (bZIP) domain of bZIP
                     transcription factors: a DNA-binding and dimerization
                     domain; cl21462"
                     /db_xref="CDD:473870"
     Site            order(159..160,162..163,166..167,169..170,173..174,
                     176..177,180..181,183..184)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269848"
     Site            347..363
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (H7C350.2)"
     Region          <359..401
                     /region_name="TMCO5"
                     /note="TMCO5 family; pfam14992"
                     /db_xref="CDD:464427"
     CDS             1..402
                     /gene="CCDC188"
                     /coded_by="NM_001365892.2:70..1278"
                     /db_xref="CCDS:CCDS93123.1"
                     /db_xref="GeneID:388849"
                     /db_xref="HGNC:HGNC:51899"
ORIGIN      
        1 meglktlgpc ghphpqcppt passshgggl dqpcqgfvgw pclgpissah svqsqrpfpv
       61 pgaggsgptv egeapglfls sqeqrardte gprqgdleag lgwgwplhpg snqgaprqgg
      121 sigsgtrpcp cpplsregga lasprvalsq lqcgllgsae qsflqleqen hslkrqnqel
      181 reqlgallgp gqqflplcpe hssctalawp pdpagtqplg nraplqllrr elcqgqeafv
      241 qqsqnelqqi rlcferkkmv itevwdnvae mhmalnnqat gllnlkkdir gvldqmediq
      301 leilreraqc rtrarkekqm asmskgrpkl gsskglagql wlltlrlllg allvwtaayv
      361 yvvnptpfeg lvppllsrat vwklralldp flrlkvdgfl pf
//
LOCUS       NP_001350622             142 aa            linear   PRI 03-DEC-2025
DEFINITION  protein NKG7 isoform 2 [Homo sapiens].
ACCESSION   NP_001350622 XP_024307291
VERSION     NP_001350622.1
DBSOURCE    REFSEQ: accession NM_001363693.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Ham,H., Hirdler,J.B., Bihnam,D.T., Mao,Z., Gicobi,J.K.,
            Macedo,B.G., Rodriguez-Quevedo,M.F., Schultz,D.F., Correia,C.,
            Zhong,J., Martinez,K.E., Banuelos,A., Ashton,D.S., Lagnado,A.B.,
            Guo,R., Pessoa,R., Pandey,A., Li,H., Lucien,F., Borges da Silva,H.,
            Dong,H. and Billadeau,D.D.
  TITLE     Lysosomal NKG7 restrains mTORC1 activity to promote CD8+ T cell
            durability and tumor control
  JOURNAL   Nat Commun 16 (1), 1628 (2025)
   PUBMED   39952956
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Ng,S.S., De Labastida Rivera,F., Yan,J., Corvino,D., Das,I.,
            Zhang,P., Kuns,R., Chauhan,S.B., Hou,J., Li,X.Y., Frame,T.C.M.,
            McEnroe,B.A., Moore,E., Na,J., Engel,J.A., Soon,M.S.F., Singh,B.,
            Kueh,A.J., Herold,M.J., Montes de Oca,M., Singh,S.S., Bunn,P.T.,
            Aguilera,A.R., Casey,M., Braun,M., Ghazanfari,N., Wani,S., Wang,Y.,
            Amante,F.H., Edwards,C.L., Haque,A., Dougall,W.C., Singh,O.P.,
            Baxter,A.G., Teng,M.W.L., Loukas,A., Daly,N.L., Cloonan,N.,
            Degli-Esposti,M.A., Uzonna,J., Heath,W.R., Bald,T., Tey,S.K.,
            Nakamura,K., Hill,G.R., Kumar,R., Sundar,S., Smyth,M.J. and
            Engwerda,C.R.
  TITLE     The NK cell granule protein NKG7 regulates cytotoxic granule
            exocytosis and inflammation
  JOURNAL   Nat Immunol 21 (10), 1205-1218 (2020)
   PUBMED   32839608
  REMARK    Erratum:[Nat Immunol. 2024 Apr;25(4):716. doi:
            10.1038/s41590-024-01770-8. PMID: 38360937]
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Medley,Q.G., Kedersha,N., O'Brien,S., Tian,Q., Schlossman,S.F.,
            Streuli,M. and Anderson,P.
  TITLE     Characterization of GMP-17, a granule membrane protein that moves
            to the plasma membrane of natural killer cells following target
            cell recognition
  JOURNAL   Proc Natl Acad Sci U S A 93 (2), 685-689 (1996)
   PUBMED   8570616
REFERENCE   6  (residues 1 to 142)
  AUTHORS   Shimane,M., Tani,K., Maruyama,K., Takahashi,S., Ozawa,K. and
            Asano,S.
  TITLE     Molecular cloning and characterization of G-CSF induced gene cDNA
  JOURNAL   Biochem Biophys Res Commun 199 (1), 26-32 (1994)
   PUBMED   7510105
REFERENCE   7  (residues 1 to 142)
  AUTHORS   Turman,M.A., Yabe,T., McSherry,C., Bach,F.H. and Houchins,J.P.
  TITLE     Characterization of a novel gene (NKG7) on human chromosome 19 that
            is expressed in natural killer cells and T cells
  JOURNAL   Hum Immunol 36 (1), 34-40 (1993)
   PUBMED   8458737
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG743982.1, S69115.1 and AI313472.1.
            
            On May 25, 2018 this sequence version replaced XP_024307291.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU687707.1, SRR1163657.560519.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..142
                     /product="protein NKG7 isoform 2"
                     /note="protein NKG7; GIG-1 protein; G-CSF-induced gene 1
                     protein; natural killer cell protein 7; granule membrane
                     protein of 17 kDa; granule membrane protein 17; natural
                     killer cell group 7 sequence"
                     /calculated_mol_wt=14776
     CDS             1..142
                     /gene="NKG7"
                     /gene_synonym="GIG1; GMP-17; p15-TIA-1"
                     /coded_by="NM_001363693.2:120..548"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS86796.1"
                     /db_xref="GeneID:4818"
                     /db_xref="HGNC:HGNC:7830"
                     /db_xref="MIM:606008"
ORIGIN      
        1 melcrslall ggslglmfcl ialstdfwfe avgpthsahs glwptghgdi isghgplvst
       61 taafaagkds gldwgiasqr ipaeelshls cpcpqpspww wpwrctpasg gtslhtprsr
      121 psspgpstwa gsqlsscsvq vp
//
LOCUS       NP_001317592             520 aa            linear   PRI 04-DEC-2025
DEFINITION  hydroxymethylglutaryl-CoA synthase, cytoplasmic isoform 1 [Homo
            sapiens].
ACCESSION   NP_001317592 XP_016864901
VERSION     NP_001317592.1
DBSOURCE    REFSEQ: accession NM_001330663.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Zhang,M., Du,G., Xie,L., Xu,Y. and Chen,W.
  TITLE     Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction
  JOURNAL   Elife 13, 97267 (2024)
   PUBMED   39235443
  REMARK    GeneRIF: Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Chen,L., Huang,D., Huang,Z., Liu,X., He,M., Luo,M., Tang,Z.,
            Tan,G., Guo,Q. and Xiong,H.
  TITLE     Decreased HMGCS1 inhibits proliferation and inflammatory response
            of keratinocytes and ameliorates imiquimod-induced psoriasis via
            the STAT3/IL-23 axis
  JOURNAL   Int Immunopharmacol 133, 112033 (2024)
   PUBMED   38608446
  REMARK    GeneRIF: Decreased HMGCS1 inhibits proliferation and inflammatory
            response of keratinocytes and ameliorates imiquimod-induced
            psoriasis via the STAT3/IL-23 axis.
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Li,K., Zhang,J., Lyu,H., Yang,J., Wei,W., Wang,Y., Luo,H.,
            Zhang,Y., Jiang,X., Yi,H., Wang,M., Zhang,C., Wu,K., Xiao,L.,
            Wen,W., Xu,H., Li,G., Wan,Y., Yang,F., Yang,R., Fu,X., Qin,B.,
            Zhou,Z., Zhang,H. and Lee,M.H.
  TITLE     CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma Progression
            via YAP1 Activation
  JOURNAL   Adv Sci (Weinh) 11 (14), e2306827 (2024)
   PUBMED   38308184
  REMARK    GeneRIF: CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma
            Progression via YAP1 Activation.
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Zhou,R., Qiu,L., Zhou,L., Geng,R., Yang,S. and Wu,J.
  TITLE     P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression
  JOURNAL   Cell Signal 105, 110609 (2023)
   PUBMED   36702290
  REMARK    GeneRIF: P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression.
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Shi,S.J., Han,D.H., Zhang,J.L., Li,Y., Yang,A.G. and Zhang,R.
  TITLE     VIM-AS1 promotes proliferation and drives enzalutamide resistance
            in prostate cancer via IGF2BP2-mediated HMGCS1 mRNA stabilization
  JOURNAL   Int J Oncol 62 (3) (2023)
   PUBMED   36734275
  REMARK    GeneRIF: VIMAS1 promotes proliferation and drives enzalutamide
            resistance in prostate cancer via IGF2BP2mediated HMGCS1 mRNA
            stabilization.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Russ,A.P., Ruzicka,V., Maerz,W., Appelhans,H. and Gross,W.
  TITLE     Amplification and direct sequencing of a cDNA encoding human
            cytosolic 3-hydroxy-3-methylglutaryl-coenzyme A synthase
  JOURNAL   Biochim Biophys Acta 1132 (3), 329-331 (1992)
   PUBMED   1358203
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Ayte,J., Gil-Gomez,G., Haro,D., Marrero,P.F. and Hegardt,F.G.
  TITLE     Rat mitochondrial and cytosolic 3-hydroxy-3-methylglutaryl-CoA
            synthases are encoded by two different genes
  JOURNAL   Proc Natl Acad Sci U S A 87 (10), 3874-3878 (1990)
   PUBMED   1971108
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Gil,G., Smith,J.R., Goldstein,J.L. and Brown,M.S.
  TITLE     Optional exon in the 5'-untranslated region of
            3-hydroxy-3-methylglutaryl coenzyme A synthase gene: conserved
            sequence and splicing pattern in humans and hamsters
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1863-1866 (1987)
   PUBMED   3470763
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Mehrabian,M., Callaway,K.A., Clarke,C.F., Tanaka,R.D.,
            Greenspan,M., Lusis,A.J., Sparkes,R.S., Mohandas,T., Edmond,J.,
            Fogelman,A.M. et al.
  TITLE     Regulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A
            synthase and the chromosomal localization of the human gene
  JOURNAL   J Biol Chem 261 (34), 16249-16255 (1986)
   PUBMED   2877984
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Leonard,S., Arbogast,D., Geyer,D., Jones,C. and Sinensky,M.
  TITLE     Localization of the gene encoding
            3-hydroxy-3-methylglutaryl-coenzyme A synthase to human chromosome
            5
  JOURNAL   Proc Natl Acad Sci U S A 83 (7), 2187-2189 (1986)
   PUBMED   2870496
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114947.2.
            
            On Sep 1, 2016 this sequence version replaced XP_016864901.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4234825.1,
                                           SRR14038193.1108827.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p12"
     Protein         1..520
                     /product="hydroxymethylglutaryl-CoA synthase, cytoplasmic
                     isoform 1"
                     /EC_number="2.3.3.10"
                     /note="3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA)
                     synthase; 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1
                     (soluble); hydroxymethylglutaryl-CoA synthase,
                     cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA synthase 1
                     (soluble)"
                     /calculated_mol_wt=57163
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Region          13..469
                     /region_name="HMG-CoA-S_euk"
                     /note="3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic
                     clade; TIGR01833"
                     /db_xref="CDD:273826"
     Site            46
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            273
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Region          492..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01581.2)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     CDS             1..520
                     /gene="HMGCS1"
                     /gene_synonym="CMYO28; HMGCS"
                     /coded_by="NM_001330663.2:230..1792"
                     /note="isoform 1 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS34154.1"
                     /db_xref="GeneID:3157"
                     /db_xref="HGNC:HGNC:5007"
                     /db_xref="MIM:142940"
ORIGIN      
        1 mpgslplnae acwpkdvgiv aleiyfpsqy vdqaelekyd gvdagkytig lgqakmgfct
       61 dredinslcm tvvqnlmern nlsydcigrl evgtetiidk sksvktnlmq lfeesgntdi
      121 egidttnacy ggtaavfnav nwiessswdg ryalvvagdi avyatgnarp tggvgavall
      181 igpnaplife rglrgthmqh aydfykpdml seypivdgkl siqcylsald rcysvyckki
      241 haqwqkegnd kdftlndfgf mifhspyckl vqkslarmll ndflndqnrd knsiysglea
      301 fgdvkledty fdrdvekafm kasselfsqk tkasllvsnq ngnmytssvy gslasvlaqy
      361 spqqlagkri gvfsygsgla atlyslkvtq datpgsaldk itaslcdlks rldsrtgvap
      421 dvfaenmklr edthhlvnyi pqgsidslfe gtwylvrvde khrrtyarrp tpnddtldeg
      481 vglvhsniat ehipspakkv prlpataaep eaavisngeh
//
LOCUS       NP_001351117             520 aa            linear   PRI 04-DEC-2025
DEFINITION  hydroxymethylglutaryl-CoA synthase, cytoplasmic isoform 1 [Homo
            sapiens].
ACCESSION   NP_001351117
VERSION     NP_001351117.1
DBSOURCE    REFSEQ: accession NM_001364188.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Zhang,M., Du,G., Xie,L., Xu,Y. and Chen,W.
  TITLE     Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction
  JOURNAL   Elife 13, 97267 (2024)
   PUBMED   39235443
  REMARK    GeneRIF: Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Chen,L., Huang,D., Huang,Z., Liu,X., He,M., Luo,M., Tang,Z.,
            Tan,G., Guo,Q. and Xiong,H.
  TITLE     Decreased HMGCS1 inhibits proliferation and inflammatory response
            of keratinocytes and ameliorates imiquimod-induced psoriasis via
            the STAT3/IL-23 axis
  JOURNAL   Int Immunopharmacol 133, 112033 (2024)
   PUBMED   38608446
  REMARK    GeneRIF: Decreased HMGCS1 inhibits proliferation and inflammatory
            response of keratinocytes and ameliorates imiquimod-induced
            psoriasis via the STAT3/IL-23 axis.
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Li,K., Zhang,J., Lyu,H., Yang,J., Wei,W., Wang,Y., Luo,H.,
            Zhang,Y., Jiang,X., Yi,H., Wang,M., Zhang,C., Wu,K., Xiao,L.,
            Wen,W., Xu,H., Li,G., Wan,Y., Yang,F., Yang,R., Fu,X., Qin,B.,
            Zhou,Z., Zhang,H. and Lee,M.H.
  TITLE     CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma Progression
            via YAP1 Activation
  JOURNAL   Adv Sci (Weinh) 11 (14), e2306827 (2024)
   PUBMED   38308184
  REMARK    GeneRIF: CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma
            Progression via YAP1 Activation.
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Zhou,R., Qiu,L., Zhou,L., Geng,R., Yang,S. and Wu,J.
  TITLE     P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression
  JOURNAL   Cell Signal 105, 110609 (2023)
   PUBMED   36702290
  REMARK    GeneRIF: P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression.
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Shi,S.J., Han,D.H., Zhang,J.L., Li,Y., Yang,A.G. and Zhang,R.
  TITLE     VIM-AS1 promotes proliferation and drives enzalutamide resistance
            in prostate cancer via IGF2BP2-mediated HMGCS1 mRNA stabilization
  JOURNAL   Int J Oncol 62 (3) (2023)
   PUBMED   36734275
  REMARK    GeneRIF: VIMAS1 promotes proliferation and drives enzalutamide
            resistance in prostate cancer via IGF2BP2mediated HMGCS1 mRNA
            stabilization.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Russ,A.P., Ruzicka,V., Maerz,W., Appelhans,H. and Gross,W.
  TITLE     Amplification and direct sequencing of a cDNA encoding human
            cytosolic 3-hydroxy-3-methylglutaryl-coenzyme A synthase
  JOURNAL   Biochim Biophys Acta 1132 (3), 329-331 (1992)
   PUBMED   1358203
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Ayte,J., Gil-Gomez,G., Haro,D., Marrero,P.F. and Hegardt,F.G.
  TITLE     Rat mitochondrial and cytosolic 3-hydroxy-3-methylglutaryl-CoA
            synthases are encoded by two different genes
  JOURNAL   Proc Natl Acad Sci U S A 87 (10), 3874-3878 (1990)
   PUBMED   1971108
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Gil,G., Smith,J.R., Goldstein,J.L. and Brown,M.S.
  TITLE     Optional exon in the 5'-untranslated region of
            3-hydroxy-3-methylglutaryl coenzyme A synthase gene: conserved
            sequence and splicing pattern in humans and hamsters
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1863-1866 (1987)
   PUBMED   3470763
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Mehrabian,M., Callaway,K.A., Clarke,C.F., Tanaka,R.D.,
            Greenspan,M., Lusis,A.J., Sparkes,R.S., Mohandas,T., Edmond,J.,
            Fogelman,A.M. et al.
  TITLE     Regulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A
            synthase and the chromosomal localization of the human gene
  JOURNAL   J Biol Chem 261 (34), 16249-16255 (1986)
   PUBMED   2877984
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Leonard,S., Arbogast,D., Geyer,D., Jones,C. and Sinensky,M.
  TITLE     Localization of the gene encoding
            3-hydroxy-3-methylglutaryl-coenzyme A synthase to human chromosome
            5
  JOURNAL   Proc Natl Acad Sci U S A 83 (7), 2187-2189 (1986)
   PUBMED   2870496
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114947.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.42317.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p12"
     Protein         1..520
                     /product="hydroxymethylglutaryl-CoA synthase, cytoplasmic
                     isoform 1"
                     /EC_number="2.3.3.10"
                     /note="3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA)
                     synthase; 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1
                     (soluble); hydroxymethylglutaryl-CoA synthase,
                     cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA synthase 1
                     (soluble)"
                     /calculated_mol_wt=57163
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Region          13..469
                     /region_name="HMG-CoA-S_euk"
                     /note="3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic
                     clade; TIGR01833"
                     /db_xref="CDD:273826"
     Site            46
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            273
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Region          492..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01581.2)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     CDS             1..520
                     /gene="HMGCS1"
                     /gene_synonym="CMYO28; HMGCS"
                     /coded_by="NM_001364188.2:250..1812"
                     /note="isoform 1 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS34154.1"
                     /db_xref="GeneID:3157"
                     /db_xref="HGNC:HGNC:5007"
                     /db_xref="MIM:142940"
ORIGIN      
        1 mpgslplnae acwpkdvgiv aleiyfpsqy vdqaelekyd gvdagkytig lgqakmgfct
       61 dredinslcm tvvqnlmern nlsydcigrl evgtetiidk sksvktnlmq lfeesgntdi
      121 egidttnacy ggtaavfnav nwiessswdg ryalvvagdi avyatgnarp tggvgavall
      181 igpnaplife rglrgthmqh aydfykpdml seypivdgkl siqcylsald rcysvyckki
      241 haqwqkegnd kdftlndfgf mifhspyckl vqkslarmll ndflndqnrd knsiysglea
      301 fgdvkledty fdrdvekafm kasselfsqk tkasllvsnq ngnmytssvy gslasvlaqy
      361 spqqlagkri gvfsygsgla atlyslkvtq datpgsaldk itaslcdlks rldsrtgvap
      421 dvfaenmklr edthhlvnyi pqgsidslfe gtwylvrvde khrrtyarrp tpnddtldeg
      481 vglvhsniat ehipspakkv prlpataaep eaavisngeh
//
LOCUS       NP_001311153             478 aa            linear   PRI 04-DEC-2025
DEFINITION  hydroxymethylglutaryl-CoA synthase, cytoplasmic isoform 2 [Homo
            sapiens].
ACCESSION   NP_001311153
VERSION     NP_001311153.1
DBSOURCE    REFSEQ: accession NM_001324224.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Zhang,M., Du,G., Xie,L., Xu,Y. and Chen,W.
  TITLE     Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction
  JOURNAL   Elife 13, 97267 (2024)
   PUBMED   39235443
  REMARK    GeneRIF: Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Chen,L., Huang,D., Huang,Z., Liu,X., He,M., Luo,M., Tang,Z.,
            Tan,G., Guo,Q. and Xiong,H.
  TITLE     Decreased HMGCS1 inhibits proliferation and inflammatory response
            of keratinocytes and ameliorates imiquimod-induced psoriasis via
            the STAT3/IL-23 axis
  JOURNAL   Int Immunopharmacol 133, 112033 (2024)
   PUBMED   38608446
  REMARK    GeneRIF: Decreased HMGCS1 inhibits proliferation and inflammatory
            response of keratinocytes and ameliorates imiquimod-induced
            psoriasis via the STAT3/IL-23 axis.
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Li,K., Zhang,J., Lyu,H., Yang,J., Wei,W., Wang,Y., Luo,H.,
            Zhang,Y., Jiang,X., Yi,H., Wang,M., Zhang,C., Wu,K., Xiao,L.,
            Wen,W., Xu,H., Li,G., Wan,Y., Yang,F., Yang,R., Fu,X., Qin,B.,
            Zhou,Z., Zhang,H. and Lee,M.H.
  TITLE     CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma Progression
            via YAP1 Activation
  JOURNAL   Adv Sci (Weinh) 11 (14), e2306827 (2024)
   PUBMED   38308184
  REMARK    GeneRIF: CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma
            Progression via YAP1 Activation.
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Zhou,R., Qiu,L., Zhou,L., Geng,R., Yang,S. and Wu,J.
  TITLE     P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression
  JOURNAL   Cell Signal 105, 110609 (2023)
   PUBMED   36702290
  REMARK    GeneRIF: P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression.
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Shi,S.J., Han,D.H., Zhang,J.L., Li,Y., Yang,A.G. and Zhang,R.
  TITLE     VIM-AS1 promotes proliferation and drives enzalutamide resistance
            in prostate cancer via IGF2BP2-mediated HMGCS1 mRNA stabilization
  JOURNAL   Int J Oncol 62 (3) (2023)
   PUBMED   36734275
  REMARK    GeneRIF: VIMAS1 promotes proliferation and drives enzalutamide
            resistance in prostate cancer via IGF2BP2mediated HMGCS1 mRNA
            stabilization.
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Russ,A.P., Ruzicka,V., Maerz,W., Appelhans,H. and Gross,W.
  TITLE     Amplification and direct sequencing of a cDNA encoding human
            cytosolic 3-hydroxy-3-methylglutaryl-coenzyme A synthase
  JOURNAL   Biochim Biophys Acta 1132 (3), 329-331 (1992)
   PUBMED   1358203
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Ayte,J., Gil-Gomez,G., Haro,D., Marrero,P.F. and Hegardt,F.G.
  TITLE     Rat mitochondrial and cytosolic 3-hydroxy-3-methylglutaryl-CoA
            synthases are encoded by two different genes
  JOURNAL   Proc Natl Acad Sci U S A 87 (10), 3874-3878 (1990)
   PUBMED   1971108
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Gil,G., Smith,J.R., Goldstein,J.L. and Brown,M.S.
  TITLE     Optional exon in the 5'-untranslated region of
            3-hydroxy-3-methylglutaryl coenzyme A synthase gene: conserved
            sequence and splicing pattern in humans and hamsters
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1863-1866 (1987)
   PUBMED   3470763
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Mehrabian,M., Callaway,K.A., Clarke,C.F., Tanaka,R.D.,
            Greenspan,M., Lusis,A.J., Sparkes,R.S., Mohandas,T., Edmond,J.,
            Fogelman,A.M. et al.
  TITLE     Regulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A
            synthase and the chromosomal localization of the human gene
  JOURNAL   J Biol Chem 261 (34), 16249-16255 (1986)
   PUBMED   2877984
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Leonard,S., Arbogast,D., Geyer,D., Jones,C. and Sinensky,M.
  TITLE     Localization of the gene encoding
            3-hydroxy-3-methylglutaryl-coenzyme A synthase to human chromosome
            5
  JOURNAL   Proc Natl Acad Sci U S A 83 (7), 2187-2189 (1986)
   PUBMED   2870496
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BJ995153.1, AK315593.1 and AC114947.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.92218.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p12"
     Protein         1..478
                     /product="hydroxymethylglutaryl-CoA synthase, cytoplasmic
                     isoform 2"
                     /EC_number="2.3.3.10"
                     /note="3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA)
                     synthase; 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1
                     (soluble); hydroxymethylglutaryl-CoA synthase,
                     cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA synthase 1
                     (soluble)"
                     /calculated_mol_wt=52999
     Region          13..427
                     /region_name="HMG-CoA-S_euk"
                     /note="3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic
                     clade; TIGR01833"
                     /db_xref="CDD:273826"
     CDS             1..478
                     /gene="HMGCS1"
                     /gene_synonym="CMYO28; HMGCS"
                     /coded_by="NM_001324224.2:147..1583"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:3157"
                     /db_xref="HGNC:HGNC:5007"
                     /db_xref="MIM:142940"
ORIGIN      
        1 mpgslplnae acwpkdvgiv aleiyfpsqy vdqaelekyd gvdagkytig lgqakmgfct
       61 dredinslcm tvvqnlmern nlsydcigrl evgtetiidk sksvktnlmq lfeesgntdi
      121 egidttnacy ggtaavfnav nwiessswdg lrgthmqhay dfykpdmlse ypivdgklsi
      181 qcylsaldrc ysvyckkiha qwqkegndkd ftlndfgfmi fhspycklvq kslarmllnd
      241 flndqnrdkn siysgleafg dvkledtyfd rdvekafmka sselfsqktk asllvsnqng
      301 nmytssvygs lasvlaqysp qqlagkrigv fsygsglaat lyslkvtqda tpgsaldkit
      361 aslcdlksrl dsrtgvapdv faenmklred thhlvnyipq gsidslfegt wylvrvdekh
      421 rrtyarrptp nddtldegvg lvhsniateh ipspakkvpr lpataaepea avisngeh
//
LOCUS       NP_001311152             478 aa            linear   PRI 04-DEC-2025
DEFINITION  hydroxymethylglutaryl-CoA synthase, cytoplasmic isoform 2 [Homo
            sapiens].
ACCESSION   NP_001311152
VERSION     NP_001311152.1
DBSOURCE    REFSEQ: accession NM_001324223.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Zhang,M., Du,G., Xie,L., Xu,Y. and Chen,W.
  TITLE     Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction
  JOURNAL   Elife 13, 97267 (2024)
   PUBMED   39235443
  REMARK    GeneRIF: Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Chen,L., Huang,D., Huang,Z., Liu,X., He,M., Luo,M., Tang,Z.,
            Tan,G., Guo,Q. and Xiong,H.
  TITLE     Decreased HMGCS1 inhibits proliferation and inflammatory response
            of keratinocytes and ameliorates imiquimod-induced psoriasis via
            the STAT3/IL-23 axis
  JOURNAL   Int Immunopharmacol 133, 112033 (2024)
   PUBMED   38608446
  REMARK    GeneRIF: Decreased HMGCS1 inhibits proliferation and inflammatory
            response of keratinocytes and ameliorates imiquimod-induced
            psoriasis via the STAT3/IL-23 axis.
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Li,K., Zhang,J., Lyu,H., Yang,J., Wei,W., Wang,Y., Luo,H.,
            Zhang,Y., Jiang,X., Yi,H., Wang,M., Zhang,C., Wu,K., Xiao,L.,
            Wen,W., Xu,H., Li,G., Wan,Y., Yang,F., Yang,R., Fu,X., Qin,B.,
            Zhou,Z., Zhang,H. and Lee,M.H.
  TITLE     CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma Progression
            via YAP1 Activation
  JOURNAL   Adv Sci (Weinh) 11 (14), e2306827 (2024)
   PUBMED   38308184
  REMARK    GeneRIF: CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma
            Progression via YAP1 Activation.
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Zhou,R., Qiu,L., Zhou,L., Geng,R., Yang,S. and Wu,J.
  TITLE     P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression
  JOURNAL   Cell Signal 105, 110609 (2023)
   PUBMED   36702290
  REMARK    GeneRIF: P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression.
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Shi,S.J., Han,D.H., Zhang,J.L., Li,Y., Yang,A.G. and Zhang,R.
  TITLE     VIM-AS1 promotes proliferation and drives enzalutamide resistance
            in prostate cancer via IGF2BP2-mediated HMGCS1 mRNA stabilization
  JOURNAL   Int J Oncol 62 (3) (2023)
   PUBMED   36734275
  REMARK    GeneRIF: VIMAS1 promotes proliferation and drives enzalutamide
            resistance in prostate cancer via IGF2BP2mediated HMGCS1 mRNA
            stabilization.
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Russ,A.P., Ruzicka,V., Maerz,W., Appelhans,H. and Gross,W.
  TITLE     Amplification and direct sequencing of a cDNA encoding human
            cytosolic 3-hydroxy-3-methylglutaryl-coenzyme A synthase
  JOURNAL   Biochim Biophys Acta 1132 (3), 329-331 (1992)
   PUBMED   1358203
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Ayte,J., Gil-Gomez,G., Haro,D., Marrero,P.F. and Hegardt,F.G.
  TITLE     Rat mitochondrial and cytosolic 3-hydroxy-3-methylglutaryl-CoA
            synthases are encoded by two different genes
  JOURNAL   Proc Natl Acad Sci U S A 87 (10), 3874-3878 (1990)
   PUBMED   1971108
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Gil,G., Smith,J.R., Goldstein,J.L. and Brown,M.S.
  TITLE     Optional exon in the 5'-untranslated region of
            3-hydroxy-3-methylglutaryl coenzyme A synthase gene: conserved
            sequence and splicing pattern in humans and hamsters
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1863-1866 (1987)
   PUBMED   3470763
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Mehrabian,M., Callaway,K.A., Clarke,C.F., Tanaka,R.D.,
            Greenspan,M., Lusis,A.J., Sparkes,R.S., Mohandas,T., Edmond,J.,
            Fogelman,A.M. et al.
  TITLE     Regulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A
            synthase and the chromosomal localization of the human gene
  JOURNAL   J Biol Chem 261 (34), 16249-16255 (1986)
   PUBMED   2877984
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Leonard,S., Arbogast,D., Geyer,D., Jones,C. and Sinensky,M.
  TITLE     Localization of the gene encoding
            3-hydroxy-3-methylglutaryl-coenzyme A synthase to human chromosome
            5
  JOURNAL   Proc Natl Acad Sci U S A 83 (7), 2187-2189 (1986)
   PUBMED   2870496
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB074885.1, AK315593.1 and AC114947.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.272420.1,
                                           SRR1660803.103675.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267761 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p12"
     Protein         1..478
                     /product="hydroxymethylglutaryl-CoA synthase, cytoplasmic
                     isoform 2"
                     /EC_number="2.3.3.10"
                     /note="3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA)
                     synthase; 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1
                     (soluble); hydroxymethylglutaryl-CoA synthase,
                     cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA synthase 1
                     (soluble)"
                     /calculated_mol_wt=52999
     Region          13..427
                     /region_name="HMG-CoA-S_euk"
                     /note="3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic
                     clade; TIGR01833"
                     /db_xref="CDD:273826"
     CDS             1..478
                     /gene="HMGCS1"
                     /gene_synonym="CMYO28; HMGCS"
                     /coded_by="NM_001324223.2:68..1504"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:3157"
                     /db_xref="HGNC:HGNC:5007"
                     /db_xref="MIM:142940"
ORIGIN      
        1 mpgslplnae acwpkdvgiv aleiyfpsqy vdqaelekyd gvdagkytig lgqakmgfct
       61 dredinslcm tvvqnlmern nlsydcigrl evgtetiidk sksvktnlmq lfeesgntdi
      121 egidttnacy ggtaavfnav nwiessswdg lrgthmqhay dfykpdmlse ypivdgklsi
      181 qcylsaldrc ysvyckkiha qwqkegndkd ftlndfgfmi fhspycklvq kslarmllnd
      241 flndqnrdkn siysgleafg dvkledtyfd rdvekafmka sselfsqktk asllvsnqng
      301 nmytssvygs lasvlaqysp qqlagkrigv fsygsglaat lyslkvtqda tpgsaldkit
      361 aslcdlksrl dsrtgvapdv faenmklred thhlvnyipq gsidslfegt wylvrvdekh
      421 rrtyarrptp nddtldegvg lvhsniateh ipspakkvpr lpataaepea avisngeh
//
LOCUS       NP_001311148             520 aa            linear   PRI 04-DEC-2025
DEFINITION  hydroxymethylglutaryl-CoA synthase, cytoplasmic isoform 1 [Homo
            sapiens].
ACCESSION   NP_001311148
VERSION     NP_001311148.1
DBSOURCE    REFSEQ: accession NM_001324219.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Zhang,M., Du,G., Xie,L., Xu,Y. and Chen,W.
  TITLE     Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction
  JOURNAL   Elife 13, 97267 (2024)
   PUBMED   39235443
  REMARK    GeneRIF: Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Chen,L., Huang,D., Huang,Z., Liu,X., He,M., Luo,M., Tang,Z.,
            Tan,G., Guo,Q. and Xiong,H.
  TITLE     Decreased HMGCS1 inhibits proliferation and inflammatory response
            of keratinocytes and ameliorates imiquimod-induced psoriasis via
            the STAT3/IL-23 axis
  JOURNAL   Int Immunopharmacol 133, 112033 (2024)
   PUBMED   38608446
  REMARK    GeneRIF: Decreased HMGCS1 inhibits proliferation and inflammatory
            response of keratinocytes and ameliorates imiquimod-induced
            psoriasis via the STAT3/IL-23 axis.
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Li,K., Zhang,J., Lyu,H., Yang,J., Wei,W., Wang,Y., Luo,H.,
            Zhang,Y., Jiang,X., Yi,H., Wang,M., Zhang,C., Wu,K., Xiao,L.,
            Wen,W., Xu,H., Li,G., Wan,Y., Yang,F., Yang,R., Fu,X., Qin,B.,
            Zhou,Z., Zhang,H. and Lee,M.H.
  TITLE     CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma Progression
            via YAP1 Activation
  JOURNAL   Adv Sci (Weinh) 11 (14), e2306827 (2024)
   PUBMED   38308184
  REMARK    GeneRIF: CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma
            Progression via YAP1 Activation.
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Zhou,R., Qiu,L., Zhou,L., Geng,R., Yang,S. and Wu,J.
  TITLE     P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression
  JOURNAL   Cell Signal 105, 110609 (2023)
   PUBMED   36702290
  REMARK    GeneRIF: P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression.
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Shi,S.J., Han,D.H., Zhang,J.L., Li,Y., Yang,A.G. and Zhang,R.
  TITLE     VIM-AS1 promotes proliferation and drives enzalutamide resistance
            in prostate cancer via IGF2BP2-mediated HMGCS1 mRNA stabilization
  JOURNAL   Int J Oncol 62 (3) (2023)
   PUBMED   36734275
  REMARK    GeneRIF: VIMAS1 promotes proliferation and drives enzalutamide
            resistance in prostate cancer via IGF2BP2mediated HMGCS1 mRNA
            stabilization.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Russ,A.P., Ruzicka,V., Maerz,W., Appelhans,H. and Gross,W.
  TITLE     Amplification and direct sequencing of a cDNA encoding human
            cytosolic 3-hydroxy-3-methylglutaryl-coenzyme A synthase
  JOURNAL   Biochim Biophys Acta 1132 (3), 329-331 (1992)
   PUBMED   1358203
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Ayte,J., Gil-Gomez,G., Haro,D., Marrero,P.F. and Hegardt,F.G.
  TITLE     Rat mitochondrial and cytosolic 3-hydroxy-3-methylglutaryl-CoA
            synthases are encoded by two different genes
  JOURNAL   Proc Natl Acad Sci U S A 87 (10), 3874-3878 (1990)
   PUBMED   1971108
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Gil,G., Smith,J.R., Goldstein,J.L. and Brown,M.S.
  TITLE     Optional exon in the 5'-untranslated region of
            3-hydroxy-3-methylglutaryl coenzyme A synthase gene: conserved
            sequence and splicing pattern in humans and hamsters
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1863-1866 (1987)
   PUBMED   3470763
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Mehrabian,M., Callaway,K.A., Clarke,C.F., Tanaka,R.D.,
            Greenspan,M., Lusis,A.J., Sparkes,R.S., Mohandas,T., Edmond,J.,
            Fogelman,A.M. et al.
  TITLE     Regulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A
            synthase and the chromosomal localization of the human gene
  JOURNAL   J Biol Chem 261 (34), 16249-16255 (1986)
   PUBMED   2877984
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Leonard,S., Arbogast,D., Geyer,D., Jones,C. and Sinensky,M.
  TITLE     Localization of the gene encoding
            3-hydroxy-3-methylglutaryl-coenzyme A synthase to human chromosome
            5
  JOURNAL   Proc Natl Acad Sci U S A 83 (7), 2187-2189 (1986)
   PUBMED   2870496
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA801434.1, AK315593.1 and AC114947.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.2816.1,
                                           SRR1803616.112840.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267755, SAMN03267761
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p12"
     Protein         1..520
                     /product="hydroxymethylglutaryl-CoA synthase, cytoplasmic
                     isoform 1"
                     /EC_number="2.3.3.10"
                     /note="3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA)
                     synthase; 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1
                     (soluble); hydroxymethylglutaryl-CoA synthase,
                     cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA synthase 1
                     (soluble)"
                     /calculated_mol_wt=57163
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Region          13..469
                     /region_name="HMG-CoA-S_euk"
                     /note="3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic
                     clade; TIGR01833"
                     /db_xref="CDD:273826"
     Site            46
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            273
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Region          492..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01581.2)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     CDS             1..520
                     /gene="HMGCS1"
                     /gene_synonym="CMYO28; HMGCS"
                     /coded_by="NM_001324219.2:171..1733"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS34154.1"
                     /db_xref="GeneID:3157"
                     /db_xref="HGNC:HGNC:5007"
                     /db_xref="MIM:142940"
ORIGIN      
        1 mpgslplnae acwpkdvgiv aleiyfpsqy vdqaelekyd gvdagkytig lgqakmgfct
       61 dredinslcm tvvqnlmern nlsydcigrl evgtetiidk sksvktnlmq lfeesgntdi
      121 egidttnacy ggtaavfnav nwiessswdg ryalvvagdi avyatgnarp tggvgavall
      181 igpnaplife rglrgthmqh aydfykpdml seypivdgkl siqcylsald rcysvyckki
      241 haqwqkegnd kdftlndfgf mifhspyckl vqkslarmll ndflndqnrd knsiysglea
      301 fgdvkledty fdrdvekafm kasselfsqk tkasllvsnq ngnmytssvy gslasvlaqy
      361 spqqlagkri gvfsygsgla atlyslkvtq datpgsaldk itaslcdlks rldsrtgvap
      421 dvfaenmklr edthhlvnyi pqgsidslfe gtwylvrvde khrrtyarrp tpnddtldeg
      481 vglvhsniat ehipspakkv prlpataaep eaavisngeh
//
LOCUS       NP_001311149             520 aa            linear   PRI 04-DEC-2025
DEFINITION  hydroxymethylglutaryl-CoA synthase, cytoplasmic isoform 1 [Homo
            sapiens].
ACCESSION   NP_001311149 XP_011512336
VERSION     NP_001311149.1
DBSOURCE    REFSEQ: accession NM_001324220.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Zhang,M., Du,G., Xie,L., Xu,Y. and Chen,W.
  TITLE     Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction
  JOURNAL   Elife 13, 97267 (2024)
   PUBMED   39235443
  REMARK    GeneRIF: Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Chen,L., Huang,D., Huang,Z., Liu,X., He,M., Luo,M., Tang,Z.,
            Tan,G., Guo,Q. and Xiong,H.
  TITLE     Decreased HMGCS1 inhibits proliferation and inflammatory response
            of keratinocytes and ameliorates imiquimod-induced psoriasis via
            the STAT3/IL-23 axis
  JOURNAL   Int Immunopharmacol 133, 112033 (2024)
   PUBMED   38608446
  REMARK    GeneRIF: Decreased HMGCS1 inhibits proliferation and inflammatory
            response of keratinocytes and ameliorates imiquimod-induced
            psoriasis via the STAT3/IL-23 axis.
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Li,K., Zhang,J., Lyu,H., Yang,J., Wei,W., Wang,Y., Luo,H.,
            Zhang,Y., Jiang,X., Yi,H., Wang,M., Zhang,C., Wu,K., Xiao,L.,
            Wen,W., Xu,H., Li,G., Wan,Y., Yang,F., Yang,R., Fu,X., Qin,B.,
            Zhou,Z., Zhang,H. and Lee,M.H.
  TITLE     CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma Progression
            via YAP1 Activation
  JOURNAL   Adv Sci (Weinh) 11 (14), e2306827 (2024)
   PUBMED   38308184
  REMARK    GeneRIF: CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma
            Progression via YAP1 Activation.
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Zhou,R., Qiu,L., Zhou,L., Geng,R., Yang,S. and Wu,J.
  TITLE     P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression
  JOURNAL   Cell Signal 105, 110609 (2023)
   PUBMED   36702290
  REMARK    GeneRIF: P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression.
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Shi,S.J., Han,D.H., Zhang,J.L., Li,Y., Yang,A.G. and Zhang,R.
  TITLE     VIM-AS1 promotes proliferation and drives enzalutamide resistance
            in prostate cancer via IGF2BP2-mediated HMGCS1 mRNA stabilization
  JOURNAL   Int J Oncol 62 (3) (2023)
   PUBMED   36734275
  REMARK    GeneRIF: VIMAS1 promotes proliferation and drives enzalutamide
            resistance in prostate cancer via IGF2BP2mediated HMGCS1 mRNA
            stabilization.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Russ,A.P., Ruzicka,V., Maerz,W., Appelhans,H. and Gross,W.
  TITLE     Amplification and direct sequencing of a cDNA encoding human
            cytosolic 3-hydroxy-3-methylglutaryl-coenzyme A synthase
  JOURNAL   Biochim Biophys Acta 1132 (3), 329-331 (1992)
   PUBMED   1358203
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Ayte,J., Gil-Gomez,G., Haro,D., Marrero,P.F. and Hegardt,F.G.
  TITLE     Rat mitochondrial and cytosolic 3-hydroxy-3-methylglutaryl-CoA
            synthases are encoded by two different genes
  JOURNAL   Proc Natl Acad Sci U S A 87 (10), 3874-3878 (1990)
   PUBMED   1971108
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Gil,G., Smith,J.R., Goldstein,J.L. and Brown,M.S.
  TITLE     Optional exon in the 5'-untranslated region of
            3-hydroxy-3-methylglutaryl coenzyme A synthase gene: conserved
            sequence and splicing pattern in humans and hamsters
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1863-1866 (1987)
   PUBMED   3470763
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Mehrabian,M., Callaway,K.A., Clarke,C.F., Tanaka,R.D.,
            Greenspan,M., Lusis,A.J., Sparkes,R.S., Mohandas,T., Edmond,J.,
            Fogelman,A.M. et al.
  TITLE     Regulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A
            synthase and the chromosomal localization of the human gene
  JOURNAL   J Biol Chem 261 (34), 16249-16255 (1986)
   PUBMED   2877984
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Leonard,S., Arbogast,D., Geyer,D., Jones,C. and Sinensky,M.
  TITLE     Localization of the gene encoding
            3-hydroxy-3-methylglutaryl-coenzyme A synthase to human chromosome
            5
  JOURNAL   Proc Natl Acad Sci U S A 83 (7), 2187-2189 (1986)
   PUBMED   2870496
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BJ995153.1, AK315593.1 and AC114947.2.
            
            On Apr 28, 2016 this sequence version replaced XP_011512336.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.2986787.1,
                                           SRR11853559.25713.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p12"
     Protein         1..520
                     /product="hydroxymethylglutaryl-CoA synthase, cytoplasmic
                     isoform 1"
                     /EC_number="2.3.3.10"
                     /note="3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA)
                     synthase; 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1
                     (soluble); hydroxymethylglutaryl-CoA synthase,
                     cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA synthase 1
                     (soluble)"
                     /calculated_mol_wt=57163
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Region          13..469
                     /region_name="HMG-CoA-S_euk"
                     /note="3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic
                     clade; TIGR01833"
                     /db_xref="CDD:273826"
     Site            46
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            273
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Region          492..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01581.2)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     CDS             1..520
                     /gene="HMGCS1"
                     /gene_synonym="CMYO28; HMGCS"
                     /coded_by="NM_001324220.2:147..1709"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS34154.1"
                     /db_xref="GeneID:3157"
                     /db_xref="HGNC:HGNC:5007"
                     /db_xref="MIM:142940"
ORIGIN      
        1 mpgslplnae acwpkdvgiv aleiyfpsqy vdqaelekyd gvdagkytig lgqakmgfct
       61 dredinslcm tvvqnlmern nlsydcigrl evgtetiidk sksvktnlmq lfeesgntdi
      121 egidttnacy ggtaavfnav nwiessswdg ryalvvagdi avyatgnarp tggvgavall
      181 igpnaplife rglrgthmqh aydfykpdml seypivdgkl siqcylsald rcysvyckki
      241 haqwqkegnd kdftlndfgf mifhspyckl vqkslarmll ndflndqnrd knsiysglea
      301 fgdvkledty fdrdvekafm kasselfsqk tkasllvsnq ngnmytssvy gslasvlaqy
      361 spqqlagkri gvfsygsgla atlyslkvtq datpgsaldk itaslcdlks rldsrtgvap
      421 dvfaenmklr edthhlvnyi pqgsidslfe gtwylvrvde khrrtyarrp tpnddtldeg
      481 vglvhsniat ehipspakkv prlpataaep eaavisngeh
//
LOCUS       NP_001091742             520 aa            linear   PRI 04-DEC-2025
DEFINITION  hydroxymethylglutaryl-CoA synthase, cytoplasmic isoform 1 [Homo
            sapiens].
ACCESSION   NP_001091742
VERSION     NP_001091742.1
DBSOURCE    REFSEQ: accession NM_001098272.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Zhang,M., Du,G., Xie,L., Xu,Y. and Chen,W.
  TITLE     Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction
  JOURNAL   Elife 13, 97267 (2024)
   PUBMED   39235443
  REMARK    GeneRIF: Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Chen,L., Huang,D., Huang,Z., Liu,X., He,M., Luo,M., Tang,Z.,
            Tan,G., Guo,Q. and Xiong,H.
  TITLE     Decreased HMGCS1 inhibits proliferation and inflammatory response
            of keratinocytes and ameliorates imiquimod-induced psoriasis via
            the STAT3/IL-23 axis
  JOURNAL   Int Immunopharmacol 133, 112033 (2024)
   PUBMED   38608446
  REMARK    GeneRIF: Decreased HMGCS1 inhibits proliferation and inflammatory
            response of keratinocytes and ameliorates imiquimod-induced
            psoriasis via the STAT3/IL-23 axis.
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Li,K., Zhang,J., Lyu,H., Yang,J., Wei,W., Wang,Y., Luo,H.,
            Zhang,Y., Jiang,X., Yi,H., Wang,M., Zhang,C., Wu,K., Xiao,L.,
            Wen,W., Xu,H., Li,G., Wan,Y., Yang,F., Yang,R., Fu,X., Qin,B.,
            Zhou,Z., Zhang,H. and Lee,M.H.
  TITLE     CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma Progression
            via YAP1 Activation
  JOURNAL   Adv Sci (Weinh) 11 (14), e2306827 (2024)
   PUBMED   38308184
  REMARK    GeneRIF: CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma
            Progression via YAP1 Activation.
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Zhou,R., Qiu,L., Zhou,L., Geng,R., Yang,S. and Wu,J.
  TITLE     P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression
  JOURNAL   Cell Signal 105, 110609 (2023)
   PUBMED   36702290
  REMARK    GeneRIF: P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression.
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Shi,S.J., Han,D.H., Zhang,J.L., Li,Y., Yang,A.G. and Zhang,R.
  TITLE     VIM-AS1 promotes proliferation and drives enzalutamide resistance
            in prostate cancer via IGF2BP2-mediated HMGCS1 mRNA stabilization
  JOURNAL   Int J Oncol 62 (3) (2023)
   PUBMED   36734275
  REMARK    GeneRIF: VIMAS1 promotes proliferation and drives enzalutamide
            resistance in prostate cancer via IGF2BP2mediated HMGCS1 mRNA
            stabilization.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Russ,A.P., Ruzicka,V., Maerz,W., Appelhans,H. and Gross,W.
  TITLE     Amplification and direct sequencing of a cDNA encoding human
            cytosolic 3-hydroxy-3-methylglutaryl-coenzyme A synthase
  JOURNAL   Biochim Biophys Acta 1132 (3), 329-331 (1992)
   PUBMED   1358203
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Ayte,J., Gil-Gomez,G., Haro,D., Marrero,P.F. and Hegardt,F.G.
  TITLE     Rat mitochondrial and cytosolic 3-hydroxy-3-methylglutaryl-CoA
            synthases are encoded by two different genes
  JOURNAL   Proc Natl Acad Sci U S A 87 (10), 3874-3878 (1990)
   PUBMED   1971108
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Gil,G., Smith,J.R., Goldstein,J.L. and Brown,M.S.
  TITLE     Optional exon in the 5'-untranslated region of
            3-hydroxy-3-methylglutaryl coenzyme A synthase gene: conserved
            sequence and splicing pattern in humans and hamsters
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1863-1866 (1987)
   PUBMED   3470763
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Mehrabian,M., Callaway,K.A., Clarke,C.F., Tanaka,R.D.,
            Greenspan,M., Lusis,A.J., Sparkes,R.S., Mohandas,T., Edmond,J.,
            Fogelman,A.M. et al.
  TITLE     Regulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A
            synthase and the chromosomal localization of the human gene
  JOURNAL   J Biol Chem 261 (34), 16249-16255 (1986)
   PUBMED   2877984
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Leonard,S., Arbogast,D., Geyer,D., Jones,C. and Sinensky,M.
  TITLE     Localization of the gene encoding
            3-hydroxy-3-methylglutaryl-coenzyme A synthase to human chromosome
            5
  JOURNAL   Proc Natl Acad Sci U S A 83 (7), 2187-2189 (1986)
   PUBMED   2870496
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK315593.1 and AC114947.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.216745.1,
                                           SRR1803615.11048.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325110.11/ ENSP00000322706.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p12"
     Protein         1..520
                     /product="hydroxymethylglutaryl-CoA synthase, cytoplasmic
                     isoform 1"
                     /EC_number="2.3.3.10"
                     /note="3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA)
                     synthase; 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1
                     (soluble); hydroxymethylglutaryl-CoA synthase,
                     cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA synthase 1
                     (soluble)"
                     /calculated_mol_wt=57163
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Region          13..469
                     /region_name="HMG-CoA-S_euk"
                     /note="3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic
                     clade; TIGR01833"
                     /db_xref="CDD:273826"
     Site            46
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            273
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Region          492..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01581.2)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     CDS             1..520
                     /gene="HMGCS1"
                     /gene_synonym="CMYO28; HMGCS"
                     /coded_by="NM_001098272.3:127..1689"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34154.1"
                     /db_xref="GeneID:3157"
                     /db_xref="HGNC:HGNC:5007"
                     /db_xref="MIM:142940"
ORIGIN      
        1 mpgslplnae acwpkdvgiv aleiyfpsqy vdqaelekyd gvdagkytig lgqakmgfct
       61 dredinslcm tvvqnlmern nlsydcigrl evgtetiidk sksvktnlmq lfeesgntdi
      121 egidttnacy ggtaavfnav nwiessswdg ryalvvagdi avyatgnarp tggvgavall
      181 igpnaplife rglrgthmqh aydfykpdml seypivdgkl siqcylsald rcysvyckki
      241 haqwqkegnd kdftlndfgf mifhspyckl vqkslarmll ndflndqnrd knsiysglea
      301 fgdvkledty fdrdvekafm kasselfsqk tkasllvsnq ngnmytssvy gslasvlaqy
      361 spqqlagkri gvfsygsgla atlyslkvtq datpgsaldk itaslcdlks rldsrtgvap
      421 dvfaenmklr edthhlvnyi pqgsidslfe gtwylvrvde khrrtyarrp tpnddtldeg
      481 vglvhsniat ehipspakkv prlpataaep eaavisngeh
//
LOCUS       NP_002121                520 aa            linear   PRI 04-DEC-2025
DEFINITION  hydroxymethylglutaryl-CoA synthase, cytoplasmic isoform 1 [Homo
            sapiens].
ACCESSION   NP_002121 XP_352962
VERSION     NP_002121.4
DBSOURCE    REFSEQ: accession NM_002130.8
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Zhang,M., Du,G., Xie,L., Xu,Y. and Chen,W.
  TITLE     Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction
  JOURNAL   Elife 13, 97267 (2024)
   PUBMED   39235443
  REMARK    GeneRIF: Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Chen,L., Huang,D., Huang,Z., Liu,X., He,M., Luo,M., Tang,Z.,
            Tan,G., Guo,Q. and Xiong,H.
  TITLE     Decreased HMGCS1 inhibits proliferation and inflammatory response
            of keratinocytes and ameliorates imiquimod-induced psoriasis via
            the STAT3/IL-23 axis
  JOURNAL   Int Immunopharmacol 133, 112033 (2024)
   PUBMED   38608446
  REMARK    GeneRIF: Decreased HMGCS1 inhibits proliferation and inflammatory
            response of keratinocytes and ameliorates imiquimod-induced
            psoriasis via the STAT3/IL-23 axis.
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Li,K., Zhang,J., Lyu,H., Yang,J., Wei,W., Wang,Y., Luo,H.,
            Zhang,Y., Jiang,X., Yi,H., Wang,M., Zhang,C., Wu,K., Xiao,L.,
            Wen,W., Xu,H., Li,G., Wan,Y., Yang,F., Yang,R., Fu,X., Qin,B.,
            Zhou,Z., Zhang,H. and Lee,M.H.
  TITLE     CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma Progression
            via YAP1 Activation
  JOURNAL   Adv Sci (Weinh) 11 (14), e2306827 (2024)
   PUBMED   38308184
  REMARK    GeneRIF: CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma
            Progression via YAP1 Activation.
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Zhou,R., Qiu,L., Zhou,L., Geng,R., Yang,S. and Wu,J.
  TITLE     P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression
  JOURNAL   Cell Signal 105, 110609 (2023)
   PUBMED   36702290
  REMARK    GeneRIF: P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression.
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Shi,S.J., Han,D.H., Zhang,J.L., Li,Y., Yang,A.G. and Zhang,R.
  TITLE     VIM-AS1 promotes proliferation and drives enzalutamide resistance
            in prostate cancer via IGF2BP2-mediated HMGCS1 mRNA stabilization
  JOURNAL   Int J Oncol 62 (3) (2023)
   PUBMED   36734275
  REMARK    GeneRIF: VIMAS1 promotes proliferation and drives enzalutamide
            resistance in prostate cancer via IGF2BP2mediated HMGCS1 mRNA
            stabilization.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Russ,A.P., Ruzicka,V., Maerz,W., Appelhans,H. and Gross,W.
  TITLE     Amplification and direct sequencing of a cDNA encoding human
            cytosolic 3-hydroxy-3-methylglutaryl-coenzyme A synthase
  JOURNAL   Biochim Biophys Acta 1132 (3), 329-331 (1992)
   PUBMED   1358203
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Ayte,J., Gil-Gomez,G., Haro,D., Marrero,P.F. and Hegardt,F.G.
  TITLE     Rat mitochondrial and cytosolic 3-hydroxy-3-methylglutaryl-CoA
            synthases are encoded by two different genes
  JOURNAL   Proc Natl Acad Sci U S A 87 (10), 3874-3878 (1990)
   PUBMED   1971108
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Gil,G., Smith,J.R., Goldstein,J.L. and Brown,M.S.
  TITLE     Optional exon in the 5'-untranslated region of
            3-hydroxy-3-methylglutaryl coenzyme A synthase gene: conserved
            sequence and splicing pattern in humans and hamsters
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1863-1866 (1987)
   PUBMED   3470763
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Mehrabian,M., Callaway,K.A., Clarke,C.F., Tanaka,R.D.,
            Greenspan,M., Lusis,A.J., Sparkes,R.S., Mohandas,T., Edmond,J.,
            Fogelman,A.M. et al.
  TITLE     Regulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A
            synthase and the chromosomal localization of the human gene
  JOURNAL   J Biol Chem 261 (34), 16249-16255 (1986)
   PUBMED   2877984
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Leonard,S., Arbogast,D., Geyer,D., Jones,C. and Sinensky,M.
  TITLE     Localization of the gene encoding
            3-hydroxy-3-methylglutaryl-coenzyme A synthase to human chromosome
            5
  JOURNAL   Proc Natl Acad Sci U S A 83 (7), 2187-2189 (1986)
   PUBMED   2870496
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114947.2.
            
            On May 25, 2007 this sequence version replaced NP_002121.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.92027.1,
                                           SRR1660807.236422.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267761 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p12"
     Protein         1..520
                     /product="hydroxymethylglutaryl-CoA synthase, cytoplasmic
                     isoform 1"
                     /EC_number="2.3.3.10"
                     /note="3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA)
                     synthase; 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1
                     (soluble); hydroxymethylglutaryl-CoA synthase,
                     cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA synthase 1
                     (soluble)"
                     /calculated_mol_wt=57163
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Region          13..469
                     /region_name="HMG-CoA-S_euk"
                     /note="3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic
                     clade; TIGR01833"
                     /db_xref="CDD:273826"
     Site            46
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            273
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Region          492..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01581.2)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01581.2)"
     CDS             1..520
                     /gene="HMGCS1"
                     /gene_synonym="CMYO28; HMGCS"
                     /coded_by="NM_002130.8:68..1630"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS34154.1"
                     /db_xref="GeneID:3157"
                     /db_xref="HGNC:HGNC:5007"
                     /db_xref="MIM:142940"
ORIGIN      
        1 mpgslplnae acwpkdvgiv aleiyfpsqy vdqaelekyd gvdagkytig lgqakmgfct
       61 dredinslcm tvvqnlmern nlsydcigrl evgtetiidk sksvktnlmq lfeesgntdi
      121 egidttnacy ggtaavfnav nwiessswdg ryalvvagdi avyatgnarp tggvgavall
      181 igpnaplife rglrgthmqh aydfykpdml seypivdgkl siqcylsald rcysvyckki
      241 haqwqkegnd kdftlndfgf mifhspyckl vqkslarmll ndflndqnrd knsiysglea
      301 fgdvkledty fdrdvekafm kasselfsqk tkasllvsnq ngnmytssvy gslasvlaqy
      361 spqqlagkri gvfsygsgla atlyslkvtq datpgsaldk itaslcdlks rldsrtgvap
      421 dvfaenmklr edthhlvnyi pqgsidslfe gtwylvrvde khrrtyarrp tpnddtldeg
      481 vglvhsniat ehipspakkv prlpataaep eaavisngeh
//
LOCUS       NP_001311151             478 aa            linear   PRI 04-DEC-2025
DEFINITION  hydroxymethylglutaryl-CoA synthase, cytoplasmic isoform 2 [Homo
            sapiens].
ACCESSION   NP_001311151 XP_011512337
VERSION     NP_001311151.1
DBSOURCE    REFSEQ: accession NM_001324222.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Zhang,M., Du,G., Xie,L., Xu,Y. and Chen,W.
  TITLE     Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction
  JOURNAL   Elife 13, 97267 (2024)
   PUBMED   39235443
  REMARK    GeneRIF: Circular RNA HMGCS1 sponges MIR4521 to aggravate type 2
            diabetes-induced vascular endothelial dysfunction.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Chen,L., Huang,D., Huang,Z., Liu,X., He,M., Luo,M., Tang,Z.,
            Tan,G., Guo,Q. and Xiong,H.
  TITLE     Decreased HMGCS1 inhibits proliferation and inflammatory response
            of keratinocytes and ameliorates imiquimod-induced psoriasis via
            the STAT3/IL-23 axis
  JOURNAL   Int Immunopharmacol 133, 112033 (2024)
   PUBMED   38608446
  REMARK    GeneRIF: Decreased HMGCS1 inhibits proliferation and inflammatory
            response of keratinocytes and ameliorates imiquimod-induced
            psoriasis via the STAT3/IL-23 axis.
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Li,K., Zhang,J., Lyu,H., Yang,J., Wei,W., Wang,Y., Luo,H.,
            Zhang,Y., Jiang,X., Yi,H., Wang,M., Zhang,C., Wu,K., Xiao,L.,
            Wen,W., Xu,H., Li,G., Wan,Y., Yang,F., Yang,R., Fu,X., Qin,B.,
            Zhou,Z., Zhang,H. and Lee,M.H.
  TITLE     CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma Progression
            via YAP1 Activation
  JOURNAL   Adv Sci (Weinh) 11 (14), e2306827 (2024)
   PUBMED   38308184
  REMARK    GeneRIF: CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma
            Progression via YAP1 Activation.
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Zhou,R., Qiu,L., Zhou,L., Geng,R., Yang,S. and Wu,J.
  TITLE     P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression
  JOURNAL   Cell Signal 105, 110609 (2023)
   PUBMED   36702290
  REMARK    GeneRIF: P4HA1 activates HMGCS1 to promote nasopharyngeal carcinoma
            ferroptosis resistance and progression.
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Shi,S.J., Han,D.H., Zhang,J.L., Li,Y., Yang,A.G. and Zhang,R.
  TITLE     VIM-AS1 promotes proliferation and drives enzalutamide resistance
            in prostate cancer via IGF2BP2-mediated HMGCS1 mRNA stabilization
  JOURNAL   Int J Oncol 62 (3) (2023)
   PUBMED   36734275
  REMARK    GeneRIF: VIMAS1 promotes proliferation and drives enzalutamide
            resistance in prostate cancer via IGF2BP2mediated HMGCS1 mRNA
            stabilization.
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Russ,A.P., Ruzicka,V., Maerz,W., Appelhans,H. and Gross,W.
  TITLE     Amplification and direct sequencing of a cDNA encoding human
            cytosolic 3-hydroxy-3-methylglutaryl-coenzyme A synthase
  JOURNAL   Biochim Biophys Acta 1132 (3), 329-331 (1992)
   PUBMED   1358203
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Ayte,J., Gil-Gomez,G., Haro,D., Marrero,P.F. and Hegardt,F.G.
  TITLE     Rat mitochondrial and cytosolic 3-hydroxy-3-methylglutaryl-CoA
            synthases are encoded by two different genes
  JOURNAL   Proc Natl Acad Sci U S A 87 (10), 3874-3878 (1990)
   PUBMED   1971108
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Gil,G., Smith,J.R., Goldstein,J.L. and Brown,M.S.
  TITLE     Optional exon in the 5'-untranslated region of
            3-hydroxy-3-methylglutaryl coenzyme A synthase gene: conserved
            sequence and splicing pattern in humans and hamsters
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1863-1866 (1987)
   PUBMED   3470763
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Mehrabian,M., Callaway,K.A., Clarke,C.F., Tanaka,R.D.,
            Greenspan,M., Lusis,A.J., Sparkes,R.S., Mohandas,T., Edmond,J.,
            Fogelman,A.M. et al.
  TITLE     Regulation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A
            synthase and the chromosomal localization of the human gene
  JOURNAL   J Biol Chem 261 (34), 16249-16255 (1986)
   PUBMED   2877984
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Leonard,S., Arbogast,D., Geyer,D., Jones,C. and Sinensky,M.
  TITLE     Localization of the gene encoding
            3-hydroxy-3-methylglutaryl-coenzyme A synthase to human chromosome
            5
  JOURNAL   Proc Natl Acad Sci U S A 83 (7), 2187-2189 (1986)
   PUBMED   2870496
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK315593.1 and AC114947.2.
            
            On Apr 28, 2016 this sequence version replaced XP_011512337.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.84804.1,
                                           SRR1803613.16109.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p12"
     Protein         1..478
                     /product="hydroxymethylglutaryl-CoA synthase, cytoplasmic
                     isoform 2"
                     /EC_number="2.3.3.10"
                     /note="3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA)
                     synthase; 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1
                     (soluble); hydroxymethylglutaryl-CoA synthase,
                     cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA synthase 1
                     (soluble)"
                     /calculated_mol_wt=52999
     Region          13..427
                     /region_name="HMG-CoA-S_euk"
                     /note="3-hydroxy-3-methylglutaryl-CoA-synthase, eukaryotic
                     clade; TIGR01833"
                     /db_xref="CDD:273826"
     CDS             1..478
                     /gene="HMGCS1"
                     /gene_synonym="CMYO28; HMGCS"
                     /coded_by="NM_001324222.2:127..1563"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:3157"
                     /db_xref="HGNC:HGNC:5007"
                     /db_xref="MIM:142940"
ORIGIN      
        1 mpgslplnae acwpkdvgiv aleiyfpsqy vdqaelekyd gvdagkytig lgqakmgfct
       61 dredinslcm tvvqnlmern nlsydcigrl evgtetiidk sksvktnlmq lfeesgntdi
      121 egidttnacy ggtaavfnav nwiessswdg lrgthmqhay dfykpdmlse ypivdgklsi
      181 qcylsaldrc ysvyckkiha qwqkegndkd ftlndfgfmi fhspycklvq kslarmllnd
      241 flndqnrdkn siysgleafg dvkledtyfd rdvekafmka sselfsqktk asllvsnqng
      301 nmytssvygs lasvlaqysp qqlagkrigv fsygsglaat lyslkvtqda tpgsaldkit
      361 aslcdlksrl dsrtgvapdv faenmklred thhlvnyipq gsidslfegt wylvrvdekh
      421 rrtyarrptp nddtldegvg lvhsniateh ipspakkvpr lpataaepea avisngeh
//
LOCUS       NP_001382880              68 aa            linear   PRI 05-DEC-2025
DEFINITION  small integral membrane protein 45 [Homo sapiens].
ACCESSION   NP_001382880
VERSION     NP_001382880.1
DBSOURCE    REFSEQ: accession NM_001395951.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Delihas,N.
  TITLE     Evolution of a Human-Specific De Novo Open Reading Frame and Its
            Linked Transcriptional Silencer
  JOURNAL   Int J Mol Sci 25 (7), 3924 (2024)
   PUBMED   38612733
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Liu,X., Xiao,C., Xu,X., Zhang,J., Mo,F., Chen,J.Y., Delihas,N.,
            Zhang,L., An,N.A. and Li,C.Y.
  TITLE     Origin of functional de novo genes in humans from 'hopeful
            monsters'
  JOURNAL   Wiley Interdiscip Rev RNA 15 (2), e1845 (2024)
   PUBMED   38605485
  REMARK    Review article
REFERENCE   3  (residues 1 to 68)
  AUTHORS   An,N.A., Zhang,J., Mo,F., Luan,X., Tian,L., Shen,Q.S., Li,X.,
            Li,C., Zhou,F., Zhang,B., Ji,M., Qi,J., Zhou,W.Z., Ding,W.,
            Chen,J.Y., Yu,J., Zhang,L., Shu,S., Hu,B. and Li,C.Y.
  TITLE     De novo genes with an lncRNA origin encode unique human brain
            developmental functionality
  JOURNAL   Nat Ecol Evol 7 (2), 264-278 (2023)
   PUBMED   36593289
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Zhang,X., Feng,Y., Gao,Y. and Hu,J.
  TITLE     Long Noncoding RNA LINC00634 Functions as an Oncogene in Esophageal
            Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1 Axis
  JOURNAL   Technol Cancer Res Treat 19, 1533033820928508 (2020)
   PUBMED   32583748
  REMARK    GeneRIF: Long Noncoding RNA LINC00634 Functions as an Oncogene in
            Esophageal Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1
            Axis.
REFERENCE   5  (residues 1 to 68)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z99716.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2151119,
                              SAMEA2163623 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..68
                     /product="small integral membrane protein 45"
                     /note="long intergenic non-protein coding RNA 634; protein
                     SMIM45"
                     /calculated_mol_wt=7834
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A590UK83.2)"
     Region          <29..>52
                     /region_name="PLN02960"
                     /note="alpha-amylase"
                     /db_xref="CDD:215519"
     CDS             1..68
                     /gene="SMIM45"
                     /gene_synonym="BK250D10.8; LINC00634"
                     /coded_by="NM_001395951.1:284..490"
                     /db_xref="CCDS:CCDS93175.1"
                     /db_xref="GeneID:339674"
                     /db_xref="HGNC:HGNC:27930"
ORIGIN      
        1 mphfldwfvp vylvisvlil vgfgaciyyf epglqeahkw rmqrplvdrd lrktlmvrdn
       61 lafggpev
//
LOCUS       NP_001382876              68 aa            linear   PRI 05-DEC-2025
DEFINITION  small integral membrane protein 45 [Homo sapiens].
ACCESSION   NP_001382876
VERSION     NP_001382876.1
DBSOURCE    REFSEQ: accession NM_001395947.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Delihas,N.
  TITLE     Evolution of a Human-Specific De Novo Open Reading Frame and Its
            Linked Transcriptional Silencer
  JOURNAL   Int J Mol Sci 25 (7), 3924 (2024)
   PUBMED   38612733
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Liu,X., Xiao,C., Xu,X., Zhang,J., Mo,F., Chen,J.Y., Delihas,N.,
            Zhang,L., An,N.A. and Li,C.Y.
  TITLE     Origin of functional de novo genes in humans from 'hopeful
            monsters'
  JOURNAL   Wiley Interdiscip Rev RNA 15 (2), e1845 (2024)
   PUBMED   38605485
  REMARK    Review article
REFERENCE   3  (residues 1 to 68)
  AUTHORS   An,N.A., Zhang,J., Mo,F., Luan,X., Tian,L., Shen,Q.S., Li,X.,
            Li,C., Zhou,F., Zhang,B., Ji,M., Qi,J., Zhou,W.Z., Ding,W.,
            Chen,J.Y., Yu,J., Zhang,L., Shu,S., Hu,B. and Li,C.Y.
  TITLE     De novo genes with an lncRNA origin encode unique human brain
            developmental functionality
  JOURNAL   Nat Ecol Evol 7 (2), 264-278 (2023)
   PUBMED   36593289
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Zhang,X., Feng,Y., Gao,Y. and Hu,J.
  TITLE     Long Noncoding RNA LINC00634 Functions as an Oncogene in Esophageal
            Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1 Axis
  JOURNAL   Technol Cancer Res Treat 19, 1533033820928508 (2020)
   PUBMED   32583748
  REMARK    GeneRIF: Long Noncoding RNA LINC00634 Functions as an Oncogene in
            Esophageal Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1
            Axis.
REFERENCE   5  (residues 1 to 68)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z99716.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..68
                     /product="small integral membrane protein 45"
                     /note="long intergenic non-protein coding RNA 634; protein
                     SMIM45"
                     /calculated_mol_wt=7834
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A590UK83.2)"
     Region          <29..>52
                     /region_name="PLN02960"
                     /note="alpha-amylase"
                     /db_xref="CDD:215519"
     CDS             1..68
                     /gene="SMIM45"
                     /gene_synonym="BK250D10.8; LINC00634"
                     /coded_by="NM_001395947.1:875..1081"
                     /db_xref="CCDS:CCDS93175.1"
                     /db_xref="GeneID:339674"
                     /db_xref="HGNC:HGNC:27930"
ORIGIN      
        1 mphfldwfvp vylvisvlil vgfgaciyyf epglqeahkw rmqrplvdrd lrktlmvrdn
       61 lafggpev
//
LOCUS       NP_001382881              68 aa            linear   PRI 05-DEC-2025
DEFINITION  small integral membrane protein 45 [Homo sapiens].
ACCESSION   NP_001382881
VERSION     NP_001382881.1
DBSOURCE    REFSEQ: accession NM_001395952.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Delihas,N.
  TITLE     Evolution of a Human-Specific De Novo Open Reading Frame and Its
            Linked Transcriptional Silencer
  JOURNAL   Int J Mol Sci 25 (7), 3924 (2024)
   PUBMED   38612733
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Liu,X., Xiao,C., Xu,X., Zhang,J., Mo,F., Chen,J.Y., Delihas,N.,
            Zhang,L., An,N.A. and Li,C.Y.
  TITLE     Origin of functional de novo genes in humans from 'hopeful
            monsters'
  JOURNAL   Wiley Interdiscip Rev RNA 15 (2), e1845 (2024)
   PUBMED   38605485
  REMARK    Review article
REFERENCE   3  (residues 1 to 68)
  AUTHORS   An,N.A., Zhang,J., Mo,F., Luan,X., Tian,L., Shen,Q.S., Li,X.,
            Li,C., Zhou,F., Zhang,B., Ji,M., Qi,J., Zhou,W.Z., Ding,W.,
            Chen,J.Y., Yu,J., Zhang,L., Shu,S., Hu,B. and Li,C.Y.
  TITLE     De novo genes with an lncRNA origin encode unique human brain
            developmental functionality
  JOURNAL   Nat Ecol Evol 7 (2), 264-278 (2023)
   PUBMED   36593289
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Zhang,X., Feng,Y., Gao,Y. and Hu,J.
  TITLE     Long Noncoding RNA LINC00634 Functions as an Oncogene in Esophageal
            Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1 Axis
  JOURNAL   Technol Cancer Res Treat 19, 1533033820928508 (2020)
   PUBMED   32583748
  REMARK    GeneRIF: Long Noncoding RNA LINC00634 Functions as an Oncogene in
            Esophageal Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1
            Axis.
REFERENCE   5  (residues 1 to 68)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z99716.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..68
                     /product="small integral membrane protein 45"
                     /note="long intergenic non-protein coding RNA 634; protein
                     SMIM45"
                     /calculated_mol_wt=7834
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A590UK83.2)"
     Region          <29..>52
                     /region_name="PLN02960"
                     /note="alpha-amylase"
                     /db_xref="CDD:215519"
     CDS             1..68
                     /gene="SMIM45"
                     /gene_synonym="BK250D10.8; LINC00634"
                     /coded_by="NM_001395952.1:561..767"
                     /db_xref="CCDS:CCDS93175.1"
                     /db_xref="GeneID:339674"
                     /db_xref="HGNC:HGNC:27930"
ORIGIN      
        1 mphfldwfvp vylvisvlil vgfgaciyyf epglqeahkw rmqrplvdrd lrktlmvrdn
       61 lafggpev
//
LOCUS       NP_001382878              68 aa            linear   PRI 05-DEC-2025
DEFINITION  small integral membrane protein 45 [Homo sapiens].
ACCESSION   NP_001382878
VERSION     NP_001382878.1
DBSOURCE    REFSEQ: accession NM_001395949.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Delihas,N.
  TITLE     Evolution of a Human-Specific De Novo Open Reading Frame and Its
            Linked Transcriptional Silencer
  JOURNAL   Int J Mol Sci 25 (7), 3924 (2024)
   PUBMED   38612733
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Liu,X., Xiao,C., Xu,X., Zhang,J., Mo,F., Chen,J.Y., Delihas,N.,
            Zhang,L., An,N.A. and Li,C.Y.
  TITLE     Origin of functional de novo genes in humans from 'hopeful
            monsters'
  JOURNAL   Wiley Interdiscip Rev RNA 15 (2), e1845 (2024)
   PUBMED   38605485
  REMARK    Review article
REFERENCE   3  (residues 1 to 68)
  AUTHORS   An,N.A., Zhang,J., Mo,F., Luan,X., Tian,L., Shen,Q.S., Li,X.,
            Li,C., Zhou,F., Zhang,B., Ji,M., Qi,J., Zhou,W.Z., Ding,W.,
            Chen,J.Y., Yu,J., Zhang,L., Shu,S., Hu,B. and Li,C.Y.
  TITLE     De novo genes with an lncRNA origin encode unique human brain
            developmental functionality
  JOURNAL   Nat Ecol Evol 7 (2), 264-278 (2023)
   PUBMED   36593289
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Zhang,X., Feng,Y., Gao,Y. and Hu,J.
  TITLE     Long Noncoding RNA LINC00634 Functions as an Oncogene in Esophageal
            Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1 Axis
  JOURNAL   Technol Cancer Res Treat 19, 1533033820928508 (2020)
   PUBMED   32583748
  REMARK    GeneRIF: Long Noncoding RNA LINC00634 Functions as an Oncogene in
            Esophageal Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1
            Axis.
REFERENCE   5  (residues 1 to 68)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z99716.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR3218377.448618.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..68
                     /product="small integral membrane protein 45"
                     /note="long intergenic non-protein coding RNA 634; protein
                     SMIM45"
                     /calculated_mol_wt=7834
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A590UK83.2)"
     Region          <29..>52
                     /region_name="PLN02960"
                     /note="alpha-amylase"
                     /db_xref="CDD:215519"
     CDS             1..68
                     /gene="SMIM45"
                     /gene_synonym="BK250D10.8; LINC00634"
                     /coded_by="NM_001395949.1:488..694"
                     /db_xref="CCDS:CCDS93175.1"
                     /db_xref="GeneID:339674"
                     /db_xref="HGNC:HGNC:27930"
ORIGIN      
        1 mphfldwfvp vylvisvlil vgfgaciyyf epglqeahkw rmqrplvdrd lrktlmvrdn
       61 lafggpev
//
LOCUS       NP_001382875              68 aa            linear   PRI 05-DEC-2025
DEFINITION  small integral membrane protein 45 [Homo sapiens].
ACCESSION   NP_001382875
VERSION     NP_001382875.1
DBSOURCE    REFSEQ: accession NM_001395946.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Delihas,N.
  TITLE     Evolution of a Human-Specific De Novo Open Reading Frame and Its
            Linked Transcriptional Silencer
  JOURNAL   Int J Mol Sci 25 (7), 3924 (2024)
   PUBMED   38612733
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Liu,X., Xiao,C., Xu,X., Zhang,J., Mo,F., Chen,J.Y., Delihas,N.,
            Zhang,L., An,N.A. and Li,C.Y.
  TITLE     Origin of functional de novo genes in humans from 'hopeful
            monsters'
  JOURNAL   Wiley Interdiscip Rev RNA 15 (2), e1845 (2024)
   PUBMED   38605485
  REMARK    Review article
REFERENCE   3  (residues 1 to 68)
  AUTHORS   An,N.A., Zhang,J., Mo,F., Luan,X., Tian,L., Shen,Q.S., Li,X.,
            Li,C., Zhou,F., Zhang,B., Ji,M., Qi,J., Zhou,W.Z., Ding,W.,
            Chen,J.Y., Yu,J., Zhang,L., Shu,S., Hu,B. and Li,C.Y.
  TITLE     De novo genes with an lncRNA origin encode unique human brain
            developmental functionality
  JOURNAL   Nat Ecol Evol 7 (2), 264-278 (2023)
   PUBMED   36593289
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Zhang,X., Feng,Y., Gao,Y. and Hu,J.
  TITLE     Long Noncoding RNA LINC00634 Functions as an Oncogene in Esophageal
            Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1 Axis
  JOURNAL   Technol Cancer Res Treat 19, 1533033820928508 (2020)
   PUBMED   32583748
  REMARK    GeneRIF: Long Noncoding RNA LINC00634 Functions as an Oncogene in
            Esophageal Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1
            Axis.
REFERENCE   5  (residues 1 to 68)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z99716.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR3218372.366480.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..68
                     /product="small integral membrane protein 45"
                     /note="long intergenic non-protein coding RNA 634; protein
                     SMIM45"
                     /calculated_mol_wt=7834
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A590UK83.2)"
     Region          <29..>52
                     /region_name="PLN02960"
                     /note="alpha-amylase"
                     /db_xref="CDD:215519"
     CDS             1..68
                     /gene="SMIM45"
                     /gene_synonym="BK250D10.8; LINC00634"
                     /coded_by="NM_001395946.1:373..579"
                     /db_xref="CCDS:CCDS93175.1"
                     /db_xref="GeneID:339674"
                     /db_xref="HGNC:HGNC:27930"
ORIGIN      
        1 mphfldwfvp vylvisvlil vgfgaciyyf epglqeahkw rmqrplvdrd lrktlmvrdn
       61 lafggpev
//
LOCUS       NP_001382869              68 aa            linear   PRI 05-DEC-2025
DEFINITION  small integral membrane protein 45 [Homo sapiens].
ACCESSION   NP_001382869 XP_001724244 XP_001725687 XP_001726873 XP_001726874
            XP_940010 XP_951088
VERSION     NP_001382869.1
DBSOURCE    REFSEQ: accession NM_001395940.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Delihas,N.
  TITLE     Evolution of a Human-Specific De Novo Open Reading Frame and Its
            Linked Transcriptional Silencer
  JOURNAL   Int J Mol Sci 25 (7), 3924 (2024)
   PUBMED   38612733
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Liu,X., Xiao,C., Xu,X., Zhang,J., Mo,F., Chen,J.Y., Delihas,N.,
            Zhang,L., An,N.A. and Li,C.Y.
  TITLE     Origin of functional de novo genes in humans from 'hopeful
            monsters'
  JOURNAL   Wiley Interdiscip Rev RNA 15 (2), e1845 (2024)
   PUBMED   38605485
  REMARK    Review article
REFERENCE   3  (residues 1 to 68)
  AUTHORS   An,N.A., Zhang,J., Mo,F., Luan,X., Tian,L., Shen,Q.S., Li,X.,
            Li,C., Zhou,F., Zhang,B., Ji,M., Qi,J., Zhou,W.Z., Ding,W.,
            Chen,J.Y., Yu,J., Zhang,L., Shu,S., Hu,B. and Li,C.Y.
  TITLE     De novo genes with an lncRNA origin encode unique human brain
            developmental functionality
  JOURNAL   Nat Ecol Evol 7 (2), 264-278 (2023)
   PUBMED   36593289
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Zhang,X., Feng,Y., Gao,Y. and Hu,J.
  TITLE     Long Noncoding RNA LINC00634 Functions as an Oncogene in Esophageal
            Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1 Axis
  JOURNAL   Technol Cancer Res Treat 19, 1533033820928508 (2020)
   PUBMED   32583748
  REMARK    GeneRIF: Long Noncoding RNA LINC00634 Functions as an Oncogene in
            Esophageal Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1
            Axis.
REFERENCE   5  (residues 1 to 68)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z99716.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC068568.1, SRR3476690.839781.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381348.5/ ENSP00000499702.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..68
                     /product="small integral membrane protein 45"
                     /note="long intergenic non-protein coding RNA 634; protein
                     SMIM45"
                     /calculated_mol_wt=7834
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A590UK83.2)"
     Region          <29..>52
                     /region_name="PLN02960"
                     /note="alpha-amylase"
                     /db_xref="CDD:215519"
     CDS             1..68
                     /gene="SMIM45"
                     /gene_synonym="BK250D10.8; LINC00634"
                     /coded_by="NM_001395940.1:287..493"
                     /db_xref="CCDS:CCDS93175.1"
                     /db_xref="GeneID:339674"
                     /db_xref="HGNC:HGNC:27930"
ORIGIN      
        1 mphfldwfvp vylvisvlil vgfgaciyyf epglqeahkw rmqrplvdrd lrktlmvrdn
       61 lafggpev
//
LOCUS       NP_001382870              68 aa            linear   PRI 05-DEC-2025
DEFINITION  small integral membrane protein 45 [Homo sapiens].
ACCESSION   NP_001382870
VERSION     NP_001382870.1
DBSOURCE    REFSEQ: accession NM_001395941.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Delihas,N.
  TITLE     Evolution of a Human-Specific De Novo Open Reading Frame and Its
            Linked Transcriptional Silencer
  JOURNAL   Int J Mol Sci 25 (7), 3924 (2024)
   PUBMED   38612733
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Liu,X., Xiao,C., Xu,X., Zhang,J., Mo,F., Chen,J.Y., Delihas,N.,
            Zhang,L., An,N.A. and Li,C.Y.
  TITLE     Origin of functional de novo genes in humans from 'hopeful
            monsters'
  JOURNAL   Wiley Interdiscip Rev RNA 15 (2), e1845 (2024)
   PUBMED   38605485
  REMARK    Review article
REFERENCE   3  (residues 1 to 68)
  AUTHORS   An,N.A., Zhang,J., Mo,F., Luan,X., Tian,L., Shen,Q.S., Li,X.,
            Li,C., Zhou,F., Zhang,B., Ji,M., Qi,J., Zhou,W.Z., Ding,W.,
            Chen,J.Y., Yu,J., Zhang,L., Shu,S., Hu,B. and Li,C.Y.
  TITLE     De novo genes with an lncRNA origin encode unique human brain
            developmental functionality
  JOURNAL   Nat Ecol Evol 7 (2), 264-278 (2023)
   PUBMED   36593289
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Zhang,X., Feng,Y., Gao,Y. and Hu,J.
  TITLE     Long Noncoding RNA LINC00634 Functions as an Oncogene in Esophageal
            Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1 Axis
  JOURNAL   Technol Cancer Res Treat 19, 1533033820928508 (2020)
   PUBMED   32583748
  REMARK    GeneRIF: Long Noncoding RNA LINC00634 Functions as an Oncogene in
            Esophageal Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1
            Axis.
REFERENCE   5  (residues 1 to 68)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z99716.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.496465.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..68
                     /product="small integral membrane protein 45"
                     /note="long intergenic non-protein coding RNA 634; protein
                     SMIM45"
                     /calculated_mol_wt=7834
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A590UK83.2)"
     Region          <29..>52
                     /region_name="PLN02960"
                     /note="alpha-amylase"
                     /db_xref="CDD:215519"
     CDS             1..68
                     /gene="SMIM45"
                     /gene_synonym="BK250D10.8; LINC00634"
                     /coded_by="NM_001395941.1:427..633"
                     /db_xref="CCDS:CCDS93175.1"
                     /db_xref="GeneID:339674"
                     /db_xref="HGNC:HGNC:27930"
ORIGIN      
        1 mphfldwfvp vylvisvlil vgfgaciyyf epglqeahkw rmqrplvdrd lrktlmvrdn
       61 lafggpev
//
LOCUS       NP_001382877              68 aa            linear   PRI 05-DEC-2025
DEFINITION  small integral membrane protein 45 [Homo sapiens].
ACCESSION   NP_001382877
VERSION     NP_001382877.1
DBSOURCE    REFSEQ: accession NM_001395948.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Delihas,N.
  TITLE     Evolution of a Human-Specific De Novo Open Reading Frame and Its
            Linked Transcriptional Silencer
  JOURNAL   Int J Mol Sci 25 (7), 3924 (2024)
   PUBMED   38612733
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Liu,X., Xiao,C., Xu,X., Zhang,J., Mo,F., Chen,J.Y., Delihas,N.,
            Zhang,L., An,N.A. and Li,C.Y.
  TITLE     Origin of functional de novo genes in humans from 'hopeful
            monsters'
  JOURNAL   Wiley Interdiscip Rev RNA 15 (2), e1845 (2024)
   PUBMED   38605485
  REMARK    Review article
REFERENCE   3  (residues 1 to 68)
  AUTHORS   An,N.A., Zhang,J., Mo,F., Luan,X., Tian,L., Shen,Q.S., Li,X.,
            Li,C., Zhou,F., Zhang,B., Ji,M., Qi,J., Zhou,W.Z., Ding,W.,
            Chen,J.Y., Yu,J., Zhang,L., Shu,S., Hu,B. and Li,C.Y.
  TITLE     De novo genes with an lncRNA origin encode unique human brain
            developmental functionality
  JOURNAL   Nat Ecol Evol 7 (2), 264-278 (2023)
   PUBMED   36593289
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Zhang,X., Feng,Y., Gao,Y. and Hu,J.
  TITLE     Long Noncoding RNA LINC00634 Functions as an Oncogene in Esophageal
            Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1 Axis
  JOURNAL   Technol Cancer Res Treat 19, 1533033820928508 (2020)
   PUBMED   32583748
  REMARK    GeneRIF: Long Noncoding RNA LINC00634 Functions as an Oncogene in
            Esophageal Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1
            Axis.
REFERENCE   5  (residues 1 to 68)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z99716.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC040153.1, ERR3218378.85177.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2152568 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..68
                     /product="small integral membrane protein 45"
                     /note="long intergenic non-protein coding RNA 634; protein
                     SMIM45"
                     /calculated_mol_wt=7834
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A590UK83.2)"
     Region          <29..>52
                     /region_name="PLN02960"
                     /note="alpha-amylase"
                     /db_xref="CDD:215519"
     CDS             1..68
                     /gene="SMIM45"
                     /gene_synonym="BK250D10.8; LINC00634"
                     /coded_by="NM_001395948.1:510..716"
                     /db_xref="CCDS:CCDS93175.1"
                     /db_xref="GeneID:339674"
                     /db_xref="HGNC:HGNC:27930"
ORIGIN      
        1 mphfldwfvp vylvisvlil vgfgaciyyf epglqeahkw rmqrplvdrd lrktlmvrdn
       61 lafggpev
//
LOCUS       NP_001382872              68 aa            linear   PRI 05-DEC-2025
DEFINITION  small integral membrane protein 45 [Homo sapiens].
ACCESSION   NP_001382872
VERSION     NP_001382872.1
DBSOURCE    REFSEQ: accession NM_001395943.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Delihas,N.
  TITLE     Evolution of a Human-Specific De Novo Open Reading Frame and Its
            Linked Transcriptional Silencer
  JOURNAL   Int J Mol Sci 25 (7), 3924 (2024)
   PUBMED   38612733
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Liu,X., Xiao,C., Xu,X., Zhang,J., Mo,F., Chen,J.Y., Delihas,N.,
            Zhang,L., An,N.A. and Li,C.Y.
  TITLE     Origin of functional de novo genes in humans from 'hopeful
            monsters'
  JOURNAL   Wiley Interdiscip Rev RNA 15 (2), e1845 (2024)
   PUBMED   38605485
  REMARK    Review article
REFERENCE   3  (residues 1 to 68)
  AUTHORS   An,N.A., Zhang,J., Mo,F., Luan,X., Tian,L., Shen,Q.S., Li,X.,
            Li,C., Zhou,F., Zhang,B., Ji,M., Qi,J., Zhou,W.Z., Ding,W.,
            Chen,J.Y., Yu,J., Zhang,L., Shu,S., Hu,B. and Li,C.Y.
  TITLE     De novo genes with an lncRNA origin encode unique human brain
            developmental functionality
  JOURNAL   Nat Ecol Evol 7 (2), 264-278 (2023)
   PUBMED   36593289
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Zhang,X., Feng,Y., Gao,Y. and Hu,J.
  TITLE     Long Noncoding RNA LINC00634 Functions as an Oncogene in Esophageal
            Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1 Axis
  JOURNAL   Technol Cancer Res Treat 19, 1533033820928508 (2020)
   PUBMED   32583748
  REMARK    GeneRIF: Long Noncoding RNA LINC00634 Functions as an Oncogene in
            Esophageal Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1
            Axis.
REFERENCE   5  (residues 1 to 68)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z99716.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.673253.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..68
                     /product="small integral membrane protein 45"
                     /note="long intergenic non-protein coding RNA 634; protein
                     SMIM45"
                     /calculated_mol_wt=7834
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A590UK83.2)"
     Region          <29..>52
                     /region_name="PLN02960"
                     /note="alpha-amylase"
                     /db_xref="CDD:215519"
     CDS             1..68
                     /gene="SMIM45"
                     /gene_synonym="BK250D10.8; LINC00634"
                     /coded_by="NM_001395943.1:546..752"
                     /db_xref="CCDS:CCDS93175.1"
                     /db_xref="GeneID:339674"
                     /db_xref="HGNC:HGNC:27930"
ORIGIN      
        1 mphfldwfvp vylvisvlil vgfgaciyyf epglqeahkw rmqrplvdrd lrktlmvrdn
       61 lafggpev
//
LOCUS       NP_001382871              68 aa            linear   PRI 05-DEC-2025
DEFINITION  small integral membrane protein 45 [Homo sapiens].
ACCESSION   NP_001382871
VERSION     NP_001382871.1
DBSOURCE    REFSEQ: accession NM_001395942.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Delihas,N.
  TITLE     Evolution of a Human-Specific De Novo Open Reading Frame and Its
            Linked Transcriptional Silencer
  JOURNAL   Int J Mol Sci 25 (7), 3924 (2024)
   PUBMED   38612733
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Liu,X., Xiao,C., Xu,X., Zhang,J., Mo,F., Chen,J.Y., Delihas,N.,
            Zhang,L., An,N.A. and Li,C.Y.
  TITLE     Origin of functional de novo genes in humans from 'hopeful
            monsters'
  JOURNAL   Wiley Interdiscip Rev RNA 15 (2), e1845 (2024)
   PUBMED   38605485
  REMARK    Review article
REFERENCE   3  (residues 1 to 68)
  AUTHORS   An,N.A., Zhang,J., Mo,F., Luan,X., Tian,L., Shen,Q.S., Li,X.,
            Li,C., Zhou,F., Zhang,B., Ji,M., Qi,J., Zhou,W.Z., Ding,W.,
            Chen,J.Y., Yu,J., Zhang,L., Shu,S., Hu,B. and Li,C.Y.
  TITLE     De novo genes with an lncRNA origin encode unique human brain
            developmental functionality
  JOURNAL   Nat Ecol Evol 7 (2), 264-278 (2023)
   PUBMED   36593289
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Zhang,X., Feng,Y., Gao,Y. and Hu,J.
  TITLE     Long Noncoding RNA LINC00634 Functions as an Oncogene in Esophageal
            Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1 Axis
  JOURNAL   Technol Cancer Res Treat 19, 1533033820928508 (2020)
   PUBMED   32583748
  REMARK    GeneRIF: Long Noncoding RNA LINC00634 Functions as an Oncogene in
            Esophageal Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1
            Axis.
REFERENCE   5  (residues 1 to 68)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z99716.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.175727.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..68
                     /product="small integral membrane protein 45"
                     /note="long intergenic non-protein coding RNA 634; protein
                     SMIM45"
                     /calculated_mol_wt=7834
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A590UK83.2)"
     Region          <29..>52
                     /region_name="PLN02960"
                     /note="alpha-amylase"
                     /db_xref="CDD:215519"
     CDS             1..68
                     /gene="SMIM45"
                     /gene_synonym="BK250D10.8; LINC00634"
                     /coded_by="NM_001395942.1:402..608"
                     /db_xref="CCDS:CCDS93175.1"
                     /db_xref="GeneID:339674"
                     /db_xref="HGNC:HGNC:27930"
ORIGIN      
        1 mphfldwfvp vylvisvlil vgfgaciyyf epglqeahkw rmqrplvdrd lrktlmvrdn
       61 lafggpev
//
LOCUS       NP_001382879              68 aa            linear   PRI 05-DEC-2025
DEFINITION  small integral membrane protein 45 [Homo sapiens].
ACCESSION   NP_001382879
VERSION     NP_001382879.1
DBSOURCE    REFSEQ: accession NM_001395950.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Delihas,N.
  TITLE     Evolution of a Human-Specific De Novo Open Reading Frame and Its
            Linked Transcriptional Silencer
  JOURNAL   Int J Mol Sci 25 (7), 3924 (2024)
   PUBMED   38612733
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Liu,X., Xiao,C., Xu,X., Zhang,J., Mo,F., Chen,J.Y., Delihas,N.,
            Zhang,L., An,N.A. and Li,C.Y.
  TITLE     Origin of functional de novo genes in humans from 'hopeful
            monsters'
  JOURNAL   Wiley Interdiscip Rev RNA 15 (2), e1845 (2024)
   PUBMED   38605485
  REMARK    Review article
REFERENCE   3  (residues 1 to 68)
  AUTHORS   An,N.A., Zhang,J., Mo,F., Luan,X., Tian,L., Shen,Q.S., Li,X.,
            Li,C., Zhou,F., Zhang,B., Ji,M., Qi,J., Zhou,W.Z., Ding,W.,
            Chen,J.Y., Yu,J., Zhang,L., Shu,S., Hu,B. and Li,C.Y.
  TITLE     De novo genes with an lncRNA origin encode unique human brain
            developmental functionality
  JOURNAL   Nat Ecol Evol 7 (2), 264-278 (2023)
   PUBMED   36593289
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Zhang,X., Feng,Y., Gao,Y. and Hu,J.
  TITLE     Long Noncoding RNA LINC00634 Functions as an Oncogene in Esophageal
            Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1 Axis
  JOURNAL   Technol Cancer Res Treat 19, 1533033820928508 (2020)
   PUBMED   32583748
  REMARK    GeneRIF: Long Noncoding RNA LINC00634 Functions as an Oncogene in
            Esophageal Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1
            Axis.
REFERENCE   5  (residues 1 to 68)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z99716.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..68
                     /product="small integral membrane protein 45"
                     /note="long intergenic non-protein coding RNA 634; protein
                     SMIM45"
                     /calculated_mol_wt=7834
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A590UK83.2)"
     Region          <29..>52
                     /region_name="PLN02960"
                     /note="alpha-amylase"
                     /db_xref="CDD:215519"
     CDS             1..68
                     /gene="SMIM45"
                     /gene_synonym="BK250D10.8; LINC00634"
                     /coded_by="NM_001395950.1:421..627"
                     /db_xref="CCDS:CCDS93175.1"
                     /db_xref="GeneID:339674"
                     /db_xref="HGNC:HGNC:27930"
ORIGIN      
        1 mphfldwfvp vylvisvlil vgfgaciyyf epglqeahkw rmqrplvdrd lrktlmvrdn
       61 lafggpev
//
LOCUS       NP_001382873              68 aa            linear   PRI 05-DEC-2025
DEFINITION  small integral membrane protein 45 [Homo sapiens].
ACCESSION   NP_001382873
VERSION     NP_001382873.1
DBSOURCE    REFSEQ: accession NM_001395944.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Delihas,N.
  TITLE     Evolution of a Human-Specific De Novo Open Reading Frame and Its
            Linked Transcriptional Silencer
  JOURNAL   Int J Mol Sci 25 (7), 3924 (2024)
   PUBMED   38612733
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Liu,X., Xiao,C., Xu,X., Zhang,J., Mo,F., Chen,J.Y., Delihas,N.,
            Zhang,L., An,N.A. and Li,C.Y.
  TITLE     Origin of functional de novo genes in humans from 'hopeful
            monsters'
  JOURNAL   Wiley Interdiscip Rev RNA 15 (2), e1845 (2024)
   PUBMED   38605485
  REMARK    Review article
REFERENCE   3  (residues 1 to 68)
  AUTHORS   An,N.A., Zhang,J., Mo,F., Luan,X., Tian,L., Shen,Q.S., Li,X.,
            Li,C., Zhou,F., Zhang,B., Ji,M., Qi,J., Zhou,W.Z., Ding,W.,
            Chen,J.Y., Yu,J., Zhang,L., Shu,S., Hu,B. and Li,C.Y.
  TITLE     De novo genes with an lncRNA origin encode unique human brain
            developmental functionality
  JOURNAL   Nat Ecol Evol 7 (2), 264-278 (2023)
   PUBMED   36593289
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Zhang,X., Feng,Y., Gao,Y. and Hu,J.
  TITLE     Long Noncoding RNA LINC00634 Functions as an Oncogene in Esophageal
            Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1 Axis
  JOURNAL   Technol Cancer Res Treat 19, 1533033820928508 (2020)
   PUBMED   32583748
  REMARK    GeneRIF: Long Noncoding RNA LINC00634 Functions as an Oncogene in
            Esophageal Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1
            Axis.
REFERENCE   5  (residues 1 to 68)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z99716.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.308420.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968968,
                                           SAMEA2148874 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..68
                     /product="small integral membrane protein 45"
                     /note="long intergenic non-protein coding RNA 634; protein
                     SMIM45"
                     /calculated_mol_wt=7834
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A590UK83.2)"
     Region          <29..>52
                     /region_name="PLN02960"
                     /note="alpha-amylase"
                     /db_xref="CDD:215519"
     CDS             1..68
                     /gene="SMIM45"
                     /gene_synonym="BK250D10.8; LINC00634"
                     /coded_by="NM_001395944.1:475..681"
                     /db_xref="CCDS:CCDS93175.1"
                     /db_xref="GeneID:339674"
                     /db_xref="HGNC:HGNC:27930"
ORIGIN      
        1 mphfldwfvp vylvisvlil vgfgaciyyf epglqeahkw rmqrplvdrd lrktlmvrdn
       61 lafggpev
//
LOCUS       NP_001382874              68 aa            linear   PRI 05-DEC-2025
DEFINITION  small integral membrane protein 45 [Homo sapiens].
ACCESSION   NP_001382874
VERSION     NP_001382874.1
DBSOURCE    REFSEQ: accession NM_001395945.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Delihas,N.
  TITLE     Evolution of a Human-Specific De Novo Open Reading Frame and Its
            Linked Transcriptional Silencer
  JOURNAL   Int J Mol Sci 25 (7), 3924 (2024)
   PUBMED   38612733
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Liu,X., Xiao,C., Xu,X., Zhang,J., Mo,F., Chen,J.Y., Delihas,N.,
            Zhang,L., An,N.A. and Li,C.Y.
  TITLE     Origin of functional de novo genes in humans from 'hopeful
            monsters'
  JOURNAL   Wiley Interdiscip Rev RNA 15 (2), e1845 (2024)
   PUBMED   38605485
  REMARK    Review article
REFERENCE   3  (residues 1 to 68)
  AUTHORS   An,N.A., Zhang,J., Mo,F., Luan,X., Tian,L., Shen,Q.S., Li,X.,
            Li,C., Zhou,F., Zhang,B., Ji,M., Qi,J., Zhou,W.Z., Ding,W.,
            Chen,J.Y., Yu,J., Zhang,L., Shu,S., Hu,B. and Li,C.Y.
  TITLE     De novo genes with an lncRNA origin encode unique human brain
            developmental functionality
  JOURNAL   Nat Ecol Evol 7 (2), 264-278 (2023)
   PUBMED   36593289
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Zhang,X., Feng,Y., Gao,Y. and Hu,J.
  TITLE     Long Noncoding RNA LINC00634 Functions as an Oncogene in Esophageal
            Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1 Axis
  JOURNAL   Technol Cancer Res Treat 19, 1533033820928508 (2020)
   PUBMED   32583748
  REMARK    GeneRIF: Long Noncoding RNA LINC00634 Functions as an Oncogene in
            Esophageal Squamous Cell Carcinoma Through the miR-342-3p/Bcl2L1
            Axis.
REFERENCE   5  (residues 1 to 68)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z99716.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1968968, SAMEA2145743
                              [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..68
                     /product="small integral membrane protein 45"
                     /note="long intergenic non-protein coding RNA 634; protein
                     SMIM45"
                     /calculated_mol_wt=7834
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A590UK83.2)"
     Region          <29..>52
                     /region_name="PLN02960"
                     /note="alpha-amylase"
                     /db_xref="CDD:215519"
     CDS             1..68
                     /gene="SMIM45"
                     /gene_synonym="BK250D10.8; LINC00634"
                     /coded_by="NM_001395945.1:467..673"
                     /db_xref="CCDS:CCDS93175.1"
                     /db_xref="GeneID:339674"
                     /db_xref="HGNC:HGNC:27930"
ORIGIN      
        1 mphfldwfvp vylvisvlil vgfgaciyyf epglqeahkw rmqrplvdrd lrktlmvrdn
       61 lafggpev
//
LOCUS       NP_001403005             184 aa            linear   PRI 06-DEC-2025
DEFINITION  testis-expressed protein 51 isoform 4 precursor [Homo sapiens].
ACCESSION   NP_001403005
VERSION     NP_001403005.1
DBSOURCE    REFSEQ: accession NM_001416076.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Dupuis,S., Le Beulze,M., Vance,T.D.R., Pierre,R., Lee,J.E.,
            Ziyyat,A. and Barbaux,S.
  TITLE     Spermatozoa lacking TEX51 display hypofertility and defects in
            morphology
  JOURNAL   Commun Biol 8 (1), 1563 (2025)
   PUBMED   41233479
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114783.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.112550.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..184
                     /product="testis-expressed protein 51 isoform 4 precursor"
                     /note="testis-expressed protein 51"
                     /calculated_mol_wt=19470
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1609
     CDS             1..184
                     /gene="TEX51"
                     /coded_by="NM_001416076.1:30..584"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:101929926"
                     /db_xref="HGNC:HGNC:52387"
ORIGIN      
        1 mlplliicll paiegknclr cwpelsalid ydlqilwvtp gpptelsqsi hslflednnf
       61 lkpwyldrdh leeetakfft qvhqaiktlr ddktvlleei ythknlfter lnkisdglke
      121 kdiqstlkvt scadcrthfl scndptfcpa rnrrtslwav slssalllai agdvsftgkg
      181 rrrq
//
LOCUS       NP_001403004             197 aa            linear   PRI 06-DEC-2025
DEFINITION  testis-expressed protein 51 isoform 3 precursor [Homo sapiens].
ACCESSION   NP_001403004 XP_047298838
VERSION     NP_001403004.1
DBSOURCE    REFSEQ: accession NM_001416075.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Dupuis,S., Le Beulze,M., Vance,T.D.R., Pierre,R., Lee,J.E.,
            Ziyyat,A. and Barbaux,S.
  TITLE     Spermatozoa lacking TEX51 display hypofertility and defects in
            morphology
  JOURNAL   Commun Biol 8 (1), 1563 (2025)
   PUBMED   41233479
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114783.5.
            
            On Jan 12, 2023 this sequence version replaced XP_047298838.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.69619.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..197
                     /product="testis-expressed protein 51 isoform 3 precursor"
                     /note="testis-expressed protein 51"
                     /calculated_mol_wt=21049
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1609
     CDS             1..197
                     /gene="TEX51"
                     /coded_by="NM_001416075.1:30..623"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:101929926"
                     /db_xref="HGNC:HGNC:52387"
ORIGIN      
        1 mlplliicll paiegknclr cwpelsalid ydlqilwvtp gpptelsqsi hslflednnf
       61 lkpwyldrdh leeetakfft qvhqaiktlr ddktvlleei ythknlfter lnkisdglke
      121 kdiqstlkvt scadcrthfl scndptfcpa rnrrtslwav slssalllai agggcffywq
      181 rkkeavkeqg sphvfqk
//
LOCUS       NP_001364407             280 aa            linear   PRI 06-DEC-2025
DEFINITION  proton-activated chloride channel isoform 3 [Homo sapiens].
ACCESSION   NP_001364407 XP_016857124
VERSION     NP_001364407.1
DBSOURCE    REFSEQ: accession NM_001377478.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Pissas,K.P., Grunder,S. and Tian,Y.
  TITLE     Functional expression of the proton sensors ASIC1a, TMEM206, and
            OGR1 together with BKCa channels is associated with cell volume
            changes and cell death under strongly acidic conditions in DAOY
            medulloblastoma cells
  JOURNAL   Pflugers Arch 476 (6), 923-937 (2024)
   PUBMED   38627262
  REMARK    GeneRIF: Functional expression of the proton sensors ASIC1a,
            TMEM206, and OGR1 together with BKCa channels is associated with
            cell volume changes and cell death under strongly acidic conditions
            in DAOY medulloblastoma cells.
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Kostritskaia,Y., Klussendorf,M., Pan,Y.E., Hassani Nia,F.,
            Kostova,S. and Stauber,T.
  TITLE     Physiological Functions of the Volume-Regulated Anion Channel
            VRAC/LRRC8 and the Proton-Activated Chloride Channel ASOR/TMEM206
  JOURNAL   Handb Exp Pharmacol 283, 181-218 (2024)
   PUBMED   37468723
  REMARK    GeneRIF: Physiological Functions of the Volume-Regulated Anion
            Channel VRAC/LRRC8 and the Proton-Activated Chloride Channel
            ASOR/TMEM206.
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Ruan,Z., Osei-Owusu,J., Du,J., Qiu,Z. and Lu,W.
  TITLE     Structures and pH-sensing mechanism of the proton-activated
            chloride channel
  JOURNAL   Nature 588 (7837), 350-354 (2020)
   PUBMED   33149300
  REMARK    GeneRIF: Structures and pH-sensing mechanism of the
            proton-activated chloride channel.
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Ullrich,F., Blin,S., Lazarow,K., Daubitz,T., von Kries,J.P. and
            Jentsch,T.J.
  TITLE     Identification of TMEM206 proteins as pore of PAORAC/ASOR
            acid-sensitive chloride channels
  JOURNAL   Elife 8, e49187 (2019)
   PUBMED   31318332
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Yang,J., Chen,J., Del Carmen Vitery,M., Osei-Owusu,J., Chu,J.,
            Yu,H., Sun,S. and Qiu,Z.
  TITLE     PAC, an evolutionarily conserved membrane protein, is a
            proton-activated chloride channel
  JOURNAL   Science 364 (6438), 395-399 (2019)
   PUBMED   31023925
  REMARK    GeneRIF: PAC (TMEM206) was indentified as being essential for the
            widely observed proton-activated Cl- (PAC) currents (ICl,H).
            GeneRIF: PACC1 encodes a new type of chloride channel activated by
            acid or proton; its wide expression suggests a broad role for this
            conserved chloride channel in physiological and pathological
            processes associated with acidic pH.
REFERENCE   8  (residues 1 to 280)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   9  (residues 1 to 280)
  AUTHORS   Teckchandani,A., Toida,N., Goodchild,J., Henderson,C., Watts,J.,
            Wollscheid,B. and Cooper,J.A.
  TITLE     Quantitative proteomics identifies a Dab2/integrin module
            regulating cell migration
  JOURNAL   J Cell Biol 186 (1), 99-111 (2009)
   PUBMED   19581412
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092803.2 and AL360091.28.
            
            On Jan 14, 2020 this sequence version replaced XP_016857124.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM800803.1, ERR3218374.18246.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..280
                     /product="proton-activated chloride channel isoform 3"
                     /note="transmembrane protein 206; proton-activated
                     chloride channel; acid-sensitive outwardly rectifying
                     channel; acid-sensitive outwardly-rectifying anion
                     channel; proton-activated outwardly rectifying anion
                     channel"
                     /calculated_mol_wt=31937
     Region          44..279
                     /region_name="TMEM206"
                     /note="TMEM206 protein family; pfam15122"
                     /db_xref="CDD:434477"
     CDS             1..280
                     /gene="PACC1"
                     /gene_synonym="ASOR; C1orf75; hPAC; hTMEM206; PAC; PAORAC;
                     TMEM206"
                     /coded_by="NM_001377478.1:130..972"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:55248"
                     /db_xref="HGNC:HGNC:25593"
                     /db_xref="MIM:618427"
ORIGIN      
        1 mirqerstsy qelseelvqv venseladeq dketvrvqgp gilpgialyp gqaqllsckh
       61 hyevipplts pgqpgdmnct tqrinytdpf snqtvksali vqgprevkkr elvflqfrln
      121 kssedfsaid yllfssfqef lqspnrvgfm qacesayssw kfsggfrtwv kmslvktkee
      181 dgreavefrq etsvvnyidq rpaakksaql ffvvfewkdp fiqkvqdivt anpwntiall
      241 cgaflalfka aefaklsikw mikirkrylk rrgqatshis
//
LOCUS       NP_001403009             180 aa            linear   PRI 06-DEC-2025
DEFINITION  testis-expressed protein 51 isoform 8 precursor [Homo sapiens].
ACCESSION   NP_001403009 XP_047298839
VERSION     NP_001403009.1
DBSOURCE    REFSEQ: accession NM_001416080.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Dupuis,S., Le Beulze,M., Vance,T.D.R., Pierre,R., Lee,J.E.,
            Ziyyat,A. and Barbaux,S.
  TITLE     Spermatozoa lacking TEX51 display hypofertility and defects in
            morphology
  JOURNAL   Commun Biol 8 (1), 1563 (2025)
   PUBMED   41233479
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114783.5.
            
            On Jan 12, 2023 this sequence version replaced XP_047298839.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.12348.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..180
                     /product="testis-expressed protein 51 isoform 8 precursor"
                     /note="testis-expressed protein 51"
                     /calculated_mol_wt=18958
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1609
     CDS             1..180
                     /gene="TEX51"
                     /coded_by="NM_001416080.1:30..572"
                     /note="isoform 8 precursor is encoded by transcript
                     variant 9"
                     /db_xref="GeneID:101929926"
                     /db_xref="HGNC:HGNC:52387"
ORIGIN      
        1 mlplliicll paiegknclr cwpelsalid ydlqilwvtp gpptelsqnr dhleeetakf
       61 ftqvhqaikt lrddktvlle eiythknlft erlnkisdgl kekdiqstlk vtscadcrth
      121 flscndptfc parnrrtslw avslssalll aiagggcffy wqrkkeavkq eqgsphvfqk
//
LOCUS       NP_001403010             193 aa            linear   PRI 06-DEC-2025
DEFINITION  testis-expressed protein 51 isoform 9 precursor [Homo sapiens].
ACCESSION   NP_001403010 XP_011510576
VERSION     NP_001403010.1
DBSOURCE    REFSEQ: accession NM_001416081.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Dupuis,S., Le Beulze,M., Vance,T.D.R., Pierre,R., Lee,J.E.,
            Ziyyat,A. and Barbaux,S.
  TITLE     Spermatozoa lacking TEX51 display hypofertility and defects in
            morphology
  JOURNAL   Commun Biol 8 (1), 1563 (2025)
   PUBMED   41233479
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114783.5.
            
            On Jan 12, 2023 this sequence version replaced XP_011510576.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.99661.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..193
                     /product="testis-expressed protein 51 isoform 9 precursor"
                     /note="testis-expressed protein 51"
                     /calculated_mol_wt=20167
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1609
     CDS             1..193
                     /gene="TEX51"
                     /coded_by="NM_001416081.1:30..611"
                     /note="isoform 9 precursor is encoded by transcript
                     variant 10"
                     /db_xref="GeneID:101929926"
                     /db_xref="HGNC:HGNC:52387"
ORIGIN      
        1 mlplliicll paiegknclr cwpelsalid ydlqilwvtp gpptelsqsi hslflednnf
       61 lkpwyldrdh leeetakfft qvhqaiktlr ddktvlleei ythknlfter lnkisdglke
      121 karnrrtslw avslssalll aiagagtgqp aclpevnrgr syhrhkvhss lgpgdpippy
      181 ppswvlgpqs sea
//
LOCUS       NP_001364408             273 aa            linear   PRI 06-DEC-2025
DEFINITION  proton-activated chloride channel isoform 4 [Homo sapiens].
ACCESSION   NP_001364408 XP_005273234
VERSION     NP_001364408.1
DBSOURCE    REFSEQ: accession NM_001377479.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Pissas,K.P., Grunder,S. and Tian,Y.
  TITLE     Functional expression of the proton sensors ASIC1a, TMEM206, and
            OGR1 together with BKCa channels is associated with cell volume
            changes and cell death under strongly acidic conditions in DAOY
            medulloblastoma cells
  JOURNAL   Pflugers Arch 476 (6), 923-937 (2024)
   PUBMED   38627262
  REMARK    GeneRIF: Functional expression of the proton sensors ASIC1a,
            TMEM206, and OGR1 together with BKCa channels is associated with
            cell volume changes and cell death under strongly acidic conditions
            in DAOY medulloblastoma cells.
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Kostritskaia,Y., Klussendorf,M., Pan,Y.E., Hassani Nia,F.,
            Kostova,S. and Stauber,T.
  TITLE     Physiological Functions of the Volume-Regulated Anion Channel
            VRAC/LRRC8 and the Proton-Activated Chloride Channel ASOR/TMEM206
  JOURNAL   Handb Exp Pharmacol 283, 181-218 (2024)
   PUBMED   37468723
  REMARK    GeneRIF: Physiological Functions of the Volume-Regulated Anion
            Channel VRAC/LRRC8 and the Proton-Activated Chloride Channel
            ASOR/TMEM206.
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Ruan,Z., Osei-Owusu,J., Du,J., Qiu,Z. and Lu,W.
  TITLE     Structures and pH-sensing mechanism of the proton-activated
            chloride channel
  JOURNAL   Nature 588 (7837), 350-354 (2020)
   PUBMED   33149300
  REMARK    GeneRIF: Structures and pH-sensing mechanism of the
            proton-activated chloride channel.
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Ullrich,F., Blin,S., Lazarow,K., Daubitz,T., von Kries,J.P. and
            Jentsch,T.J.
  TITLE     Identification of TMEM206 proteins as pore of PAORAC/ASOR
            acid-sensitive chloride channels
  JOURNAL   Elife 8, e49187 (2019)
   PUBMED   31318332
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 273)
  AUTHORS   Yang,J., Chen,J., Del Carmen Vitery,M., Osei-Owusu,J., Chu,J.,
            Yu,H., Sun,S. and Qiu,Z.
  TITLE     PAC, an evolutionarily conserved membrane protein, is a
            proton-activated chloride channel
  JOURNAL   Science 364 (6438), 395-399 (2019)
   PUBMED   31023925
  REMARK    GeneRIF: PAC (TMEM206) was indentified as being essential for the
            widely observed proton-activated Cl- (PAC) currents (ICl,H).
            GeneRIF: PACC1 encodes a new type of chloride channel activated by
            acid or proton; its wide expression suggests a broad role for this
            conserved chloride channel in physiological and pathological
            processes associated with acidic pH.
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   9  (residues 1 to 273)
  AUTHORS   Teckchandani,A., Toida,N., Goodchild,J., Henderson,C., Watts,J.,
            Wollscheid,B. and Cooper,J.A.
  TITLE     Quantitative proteomics identifies a Dab2/integrin module
            regulating cell migration
  JOURNAL   J Cell Biol 186 (1), 99-111 (2009)
   PUBMED   19581412
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092803.2, KF459533.1 and AL360091.28.
            
            On Jan 14, 2020 this sequence version replaced XP_005273234.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.125826.1,
                                           SRR3476690.50964.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..273
                     /product="proton-activated chloride channel isoform 4"
                     /note="transmembrane protein 206; proton-activated
                     chloride channel; acid-sensitive outwardly rectifying
                     channel; acid-sensitive outwardly-rectifying anion
                     channel; proton-activated outwardly rectifying anion
                     channel"
                     /calculated_mol_wt=31281
     Region          1..272
                     /region_name="TMEM206"
                     /note="TMEM206 protein family; pfam15122"
                     /db_xref="CDD:434477"
     CDS             1..273
                     /gene="PACC1"
                     /gene_synonym="ASOR; C1orf75; hPAC; hTMEM206; PAC; PAORAC;
                     TMEM206"
                     /coded_by="NM_001377479.1:238..1059"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:55248"
                     /db_xref="HGNC:HGNC:25593"
                     /db_xref="MIM:618427"
ORIGIN      
        1 mavavflvyr titdfreklk hpvmsvsyke vdrydapgia lypgqaqlls ckhhyevipp
       61 ltspgqpgdm ncttqrinyt dpfsnqtvks alivqgprev kkrelvflqf rlnkssedfs
      121 aidyllfssf qeflqspnrv gfmqacesay sswkfsggfr twvkmslvkt keedgreave
      181 frqetsvvny idqrpaakks aqlffvvfew kdpfiqkvqd ivtanpwnti allcgaflal
      241 fkaaefakls ikwmikirkr ylkrrgqats his
//
LOCUS       NP_001403007             176 aa            linear   PRI 06-DEC-2025
DEFINITION  testis-expressed protein 51 isoform 6 precursor [Homo sapiens].
ACCESSION   NP_001403007 XP_047298840
VERSION     NP_001403007.1
DBSOURCE    REFSEQ: accession NM_001416078.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Dupuis,S., Le Beulze,M., Vance,T.D.R., Pierre,R., Lee,J.E.,
            Ziyyat,A. and Barbaux,S.
  TITLE     Spermatozoa lacking TEX51 display hypofertility and defects in
            morphology
  JOURNAL   Commun Biol 8 (1), 1563 (2025)
   PUBMED   41233479
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114783.5.
            
            On Jan 12, 2023 this sequence version replaced XP_047298840.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.94087.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..176
                     /product="testis-expressed protein 51 isoform 6 precursor"
                     /note="testis-expressed protein 51"
                     /calculated_mol_wt=18699
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1609
     CDS             1..176
                     /gene="TEX51"
                     /coded_by="NM_001416078.1:30..560"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:101929926"
                     /db_xref="HGNC:HGNC:52387"
ORIGIN      
        1 mlplliicll paiegknclr cwpelsalid ydlqilwvtp gpptelsqsi hslflednnf
       61 lkpwyldrdh leeetakfft qvhqaiktlr ddktvlleei ythknlfter lnkisdglke
      121 kacnescarn rrtslwavsl ssalllaiag ggcffywqrk keavkqeqgs phvfqk
//
LOCUS       NP_001403008             166 aa            linear   PRI 06-DEC-2025
DEFINITION  testis-expressed protein 51 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001403008 XP_016858639
VERSION     NP_001403008.1
DBSOURCE    REFSEQ: accession NM_001416079.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Dupuis,S., Le Beulze,M., Vance,T.D.R., Pierre,R., Lee,J.E.,
            Ziyyat,A. and Barbaux,S.
  TITLE     Spermatozoa lacking TEX51 display hypofertility and defects in
            morphology
  JOURNAL   Commun Biol 8 (1), 1563 (2025)
   PUBMED   41233479
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114783.5.
            
            On Jan 12, 2023 this sequence version replaced XP_016858639.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.34805.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..166
                     /product="testis-expressed protein 51 isoform 1 precursor"
                     /note="testis-expressed protein 51"
                     /calculated_mol_wt=17251
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1609
     mat_peptide     16..166
                     /product="Testis-expressed protein 51.
                     /evidence=ECO:0000255. /id=PRO_0000441046"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A1B0GUA7.1)"
                     /calculated_mol_wt=17251
     Site            138..154
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A1B0GUA7.1)"
     CDS             1..166
                     /gene="TEX51"
                     /coded_by="NM_001416079.1:30..530"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 8"
                     /db_xref="GeneID:101929926"
                     /db_xref="HGNC:HGNC:52387"
ORIGIN      
        1 mlplliicll paiegknclr cwpelsalid ydlqilwvtp gpptelsqnr dhleeetakf
       61 ftqvhqaikt lrddktvlle eiythknlft erlnkisdgl kekdiqstlk vtscadcrth
      121 flscndptfc parnrrtslw avslssalll aiagdvsftg kgrrrq
//
LOCUS       NP_060722                350 aa            linear   PRI 06-DEC-2025
DEFINITION  proton-activated chloride channel isoform 2 [Homo sapiens].
ACCESSION   NP_060722
VERSION     NP_060722.2
DBSOURCE    REFSEQ: accession NM_018252.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Pissas,K.P., Grunder,S. and Tian,Y.
  TITLE     Functional expression of the proton sensors ASIC1a, TMEM206, and
            OGR1 together with BKCa channels is associated with cell volume
            changes and cell death under strongly acidic conditions in DAOY
            medulloblastoma cells
  JOURNAL   Pflugers Arch 476 (6), 923-937 (2024)
   PUBMED   38627262
  REMARK    GeneRIF: Functional expression of the proton sensors ASIC1a,
            TMEM206, and OGR1 together with BKCa channels is associated with
            cell volume changes and cell death under strongly acidic conditions
            in DAOY medulloblastoma cells.
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Kostritskaia,Y., Klussendorf,M., Pan,Y.E., Hassani Nia,F.,
            Kostova,S. and Stauber,T.
  TITLE     Physiological Functions of the Volume-Regulated Anion Channel
            VRAC/LRRC8 and the Proton-Activated Chloride Channel ASOR/TMEM206
  JOURNAL   Handb Exp Pharmacol 283, 181-218 (2024)
   PUBMED   37468723
  REMARK    GeneRIF: Physiological Functions of the Volume-Regulated Anion
            Channel VRAC/LRRC8 and the Proton-Activated Chloride Channel
            ASOR/TMEM206.
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Ruan,Z., Osei-Owusu,J., Du,J., Qiu,Z. and Lu,W.
  TITLE     Structures and pH-sensing mechanism of the proton-activated
            chloride channel
  JOURNAL   Nature 588 (7837), 350-354 (2020)
   PUBMED   33149300
  REMARK    GeneRIF: Structures and pH-sensing mechanism of the
            proton-activated chloride channel.
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Ullrich,F., Blin,S., Lazarow,K., Daubitz,T., von Kries,J.P. and
            Jentsch,T.J.
  TITLE     Identification of TMEM206 proteins as pore of PAORAC/ASOR
            acid-sensitive chloride channels
  JOURNAL   Elife 8, e49187 (2019)
   PUBMED   31318332
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Yang,J., Chen,J., Del Carmen Vitery,M., Osei-Owusu,J., Chu,J.,
            Yu,H., Sun,S. and Qiu,Z.
  TITLE     PAC, an evolutionarily conserved membrane protein, is a
            proton-activated chloride channel
  JOURNAL   Science 364 (6438), 395-399 (2019)
   PUBMED   31023925
  REMARK    GeneRIF: PAC (TMEM206) was indentified as being essential for the
            widely observed proton-activated Cl- (PAC) currents (ICl,H).
            GeneRIF: PACC1 encodes a new type of chloride channel activated by
            acid or proton; its wide expression suggests a broad role for this
            conserved chloride channel in physiological and pathological
            processes associated with acidic pH.
REFERENCE   8  (residues 1 to 350)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   9  (residues 1 to 350)
  AUTHORS   Teckchandani,A., Toida,N., Goodchild,J., Henderson,C., Watts,J.,
            Wollscheid,B. and Cooper,J.A.
  TITLE     Quantitative proteomics identifies a Dab2/integrin module
            regulating cell migration
  JOURNAL   J Cell Biol 186 (1), 99-111 (2009)
   PUBMED   19581412
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC411913.1, BC006320.2 and AL360091.28.
            
            On Jun 19, 2007 this sequence version replaced NP_060722.1.
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            5' CDS compared to variant 1. The resulting isoform (2) lacks an
            internal segment compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.186616.1, AK001736.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261455.9/ ENSP00000261455.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..350
                     /product="proton-activated chloride channel isoform 2"
                     /note="transmembrane protein 206; proton-activated
                     chloride channel; acid-sensitive outwardly rectifying
                     channel; acid-sensitive outwardly-rectifying anion
                     channel; proton-activated outwardly rectifying anion
                     channel"
                     /calculated_mol_wt=39912
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9H813.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9D771; propagated from
                     UniProtKB/Swiss-Prot (Q9H813.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D771; propagated from
                     UniProtKB/Swiss-Prot (Q9H813.1)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q66H28; propagated from
                     UniProtKB/Swiss-Prot (Q9H813.1)"
     Region          55..349
                     /region_name="TMEM206"
                     /note="TMEM206 protein family; pfam15122"
                     /db_xref="CDD:434477"
     Site            65..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H813.1)"
     Site            155
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q9H813.1)"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q9H813.1)"
     Site            302..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H813.1)"
     CDS             1..350
                     /gene="PACC1"
                     /gene_synonym="ASOR; C1orf75; hPAC; hTMEM206; PAC; PAORAC;
                     TMEM206"
                     /coded_by="NM_018252.3:130..1182"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1504.1"
                     /db_xref="GeneID:55248"
                     /db_xref="HGNC:HGNC:25593"
                     /db_xref="MIM:618427"
ORIGIN      
        1 mirqerstsy qelseelvqv venseladeq dketvrvqgp gilpgldses asssirfska
       61 clknvfsvll ifiylllmav avflvyrtit dfreklkhpv msvsykevdr ydapgialyp
      121 gqaqllsckh hyevipplts pgqpgdmnct tqrinytdpf snqtvksali vqgprevkkr
      181 elvflqfrln kssedfsaid yllfssfqef lqspnrvgfm qacesayssw kfsggfrtwv
      241 kmslvktkee dgreavefrq etsvvnyidq rpaakksaql ffvvfewkdp fiqkvqdivt
      301 anpwntiall cgaflalfka aefaklsikw mikirkrylk rrgqatshis
//
LOCUS       NP_001403011             190 aa            linear   PRI 06-DEC-2025
DEFINITION  testis-expressed protein 51 isoform 10 precursor [Homo sapiens].
ACCESSION   NP_001403011 XP_011510577
VERSION     NP_001403011.1
DBSOURCE    REFSEQ: accession NM_001416082.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Dupuis,S., Le Beulze,M., Vance,T.D.R., Pierre,R., Lee,J.E.,
            Ziyyat,A. and Barbaux,S.
  TITLE     Spermatozoa lacking TEX51 display hypofertility and defects in
            morphology
  JOURNAL   Commun Biol 8 (1), 1563 (2025)
   PUBMED   41233479
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114783.5.
            
            On Jan 12, 2023 this sequence version replaced XP_011510577.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..190
                     /product="testis-expressed protein 51 isoform 10
                     precursor"
                     /note="testis-expressed protein 51"
                     /calculated_mol_wt=20078
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1609
     CDS             1..190
                     /gene="TEX51"
                     /coded_by="NM_001416082.1:30..602"
                     /note="isoform 10 precursor is encoded by transcript
                     variant 11"
                     /db_xref="GeneID:101929926"
                     /db_xref="HGNC:HGNC:52387"
ORIGIN      
        1 mlplliicll paiegknclr cwpelsalid ydlqilwvtp gpptelsqsi hslflednnf
       61 lkpwyldrdh leeetakfft qvhqaiktlr ddktvlleei ythknlfter lnkisdglke
      121 kacnescdiq stlkvtscad crthflscnd ptfcparnrr tslwavslss alllaiagdv
      181 sftgkgrrrq
//
LOCUS       NP_001403006             172 aa            linear   PRI 06-DEC-2025
DEFINITION  testis-expressed protein 51 isoform 5 precursor [Homo sapiens].
ACCESSION   NP_001403006
VERSION     NP_001403006.1
DBSOURCE    REFSEQ: accession NM_001416077.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Dupuis,S., Le Beulze,M., Vance,T.D.R., Pierre,R., Lee,J.E.,
            Ziyyat,A. and Barbaux,S.
  TITLE     Spermatozoa lacking TEX51 display hypofertility and defects in
            morphology
  JOURNAL   Commun Biol 8 (1), 1563 (2025)
   PUBMED   41233479
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114783.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.384950.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..172
                     /product="testis-expressed protein 51 isoform 5 precursor"
                     /note="testis-expressed protein 51"
                     /calculated_mol_wt=17858
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1609
     CDS             1..172
                     /gene="TEX51"
                     /coded_by="NM_001416077.1:30..548"
                     /note="isoform 5 precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:101929926"
                     /db_xref="HGNC:HGNC:52387"
ORIGIN      
        1 mlplliicll paiegknclr cwpelsalid ydlqilwvtp gpptelsqnr dhleeetakf
       61 ftqvhqaikt lrddktvlle eiythknlft erlnkisdgl kekacnescd iqstlkvtsc
      121 adcrthflsc ndptfcparn rrtslwavsl ssalllaiag dvsftgkgrr rq
//
LOCUS       NP_001309173             166 aa            linear   PRI 06-DEC-2025
DEFINITION  testis-expressed protein 51 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001309173
VERSION     NP_001309173.1
DBSOURCE    REFSEQ: accession NM_001322244.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Dupuis,S., Le Beulze,M., Vance,T.D.R., Pierre,R., Lee,J.E.,
            Ziyyat,A. and Barbaux,S.
  TITLE     Spermatozoa lacking TEX51 display hypofertility and defects in
            morphology
  JOURNAL   Commun Biol 8 (1), 1563 (2025)
   PUBMED   41233479
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI461950.1, BI828150.1 and AI040972.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000568484.6/ ENSP00000489776.1
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..166
                     /product="testis-expressed protein 51 isoform 1 precursor"
                     /note="testis-expressed protein 51"
                     /calculated_mol_wt=17251
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1609
     mat_peptide     16..166
                     /product="Testis-expressed protein 51.
                     /evidence=ECO:0000255. /id=PRO_0000441046"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A1B0GUA7.1)"
                     /calculated_mol_wt=17251
     Site            138..154
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A1B0GUA7.1)"
     CDS             1..166
                     /gene="TEX51"
                     /coded_by="NM_001322244.2:30..530"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS82507.1"
                     /db_xref="GeneID:101929926"
                     /db_xref="HGNC:HGNC:52387"
ORIGIN      
        1 mlplliicll paiegknclr cwpelsalid ydlqilwvtp gpptelsqnr dhleeetakf
       61 ftqvhqaikt lrddktvlle eiythknlft erlnkisdgl kekdiqstlk vtscadcrth
      121 flscndptfc parnrrtslw avslssalll aiagdvsftg kgrrrq
//
LOCUS       NP_001185791             411 aa            linear   PRI 06-DEC-2025
DEFINITION  proton-activated chloride channel isoform 1 [Homo sapiens].
ACCESSION   NP_001185791
VERSION     NP_001185791.1
DBSOURCE    REFSEQ: accession NM_001198862.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Pissas,K.P., Grunder,S. and Tian,Y.
  TITLE     Functional expression of the proton sensors ASIC1a, TMEM206, and
            OGR1 together with BKCa channels is associated with cell volume
            changes and cell death under strongly acidic conditions in DAOY
            medulloblastoma cells
  JOURNAL   Pflugers Arch 476 (6), 923-937 (2024)
   PUBMED   38627262
  REMARK    GeneRIF: Functional expression of the proton sensors ASIC1a,
            TMEM206, and OGR1 together with BKCa channels is associated with
            cell volume changes and cell death under strongly acidic conditions
            in DAOY medulloblastoma cells.
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Kostritskaia,Y., Klussendorf,M., Pan,Y.E., Hassani Nia,F.,
            Kostova,S. and Stauber,T.
  TITLE     Physiological Functions of the Volume-Regulated Anion Channel
            VRAC/LRRC8 and the Proton-Activated Chloride Channel ASOR/TMEM206
  JOURNAL   Handb Exp Pharmacol 283, 181-218 (2024)
   PUBMED   37468723
  REMARK    GeneRIF: Physiological Functions of the Volume-Regulated Anion
            Channel VRAC/LRRC8 and the Proton-Activated Chloride Channel
            ASOR/TMEM206.
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Ruan,Z., Osei-Owusu,J., Du,J., Qiu,Z. and Lu,W.
  TITLE     Structures and pH-sensing mechanism of the proton-activated
            chloride channel
  JOURNAL   Nature 588 (7837), 350-354 (2020)
   PUBMED   33149300
  REMARK    GeneRIF: Structures and pH-sensing mechanism of the
            proton-activated chloride channel.
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Ullrich,F., Blin,S., Lazarow,K., Daubitz,T., von Kries,J.P. and
            Jentsch,T.J.
  TITLE     Identification of TMEM206 proteins as pore of PAORAC/ASOR
            acid-sensitive chloride channels
  JOURNAL   Elife 8, e49187 (2019)
   PUBMED   31318332
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 411)
  AUTHORS   Yang,J., Chen,J., Del Carmen Vitery,M., Osei-Owusu,J., Chu,J.,
            Yu,H., Sun,S. and Qiu,Z.
  TITLE     PAC, an evolutionarily conserved membrane protein, is a
            proton-activated chloride channel
  JOURNAL   Science 364 (6438), 395-399 (2019)
   PUBMED   31023925
  REMARK    GeneRIF: PAC (TMEM206) was indentified as being essential for the
            widely observed proton-activated Cl- (PAC) currents (ICl,H).
            GeneRIF: PACC1 encodes a new type of chloride channel activated by
            acid or proton; its wide expression suggests a broad role for this
            conserved chloride channel in physiological and pathological
            processes associated with acidic pH.
REFERENCE   8  (residues 1 to 411)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   9  (residues 1 to 411)
  AUTHORS   Teckchandani,A., Toida,N., Goodchild,J., Henderson,C., Watts,J.,
            Wollscheid,B. and Cooper,J.A.
  TITLE     Quantitative proteomics identifies a Dab2/integrin module
            regulating cell migration
  JOURNAL   J Cell Biol 186 (1), 99-111 (2009)
   PUBMED   19581412
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK297200.1, BC006320.2 and AL360091.28.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297200.1, AK295224.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..411
                     /product="proton-activated chloride channel isoform 1"
                     /note="transmembrane protein 206; proton-activated
                     chloride channel; acid-sensitive outwardly rectifying
                     channel; acid-sensitive outwardly-rectifying anion
                     channel; proton-activated outwardly rectifying anion
                     channel"
                     /calculated_mol_wt=46337
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9H813.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9D771; propagated from
                     UniProtKB/Swiss-Prot (Q9H813.1)"
     Region          116..410
                     /region_name="TMEM206"
                     /note="TMEM206 protein family; pfam15122"
                     /db_xref="CDD:434477"
     CDS             1..411
                     /gene="PACC1"
                     /gene_synonym="ASOR; C1orf75; hPAC; hTMEM206; PAC; PAORAC;
                     TMEM206"
                     /coded_by="NM_001198862.2:130..1365"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS55687.1"
                     /db_xref="GeneID:55248"
                     /db_xref="HGNC:HGNC:25593"
                     /db_xref="MIM:618427"
ORIGIN      
        1 mirqerstsy qeavrpalps skpclltspa vlvkllsssa stsrppnlgh lwqpsssvpl
       61 hraaslakvr qfqlseelvq vvenselade qdketvrvqg pgilpgldse sasssirfsk
      121 aclknvfsvl lifiylllma vavflvyrti tdfreklkhp vmsvsykevd rydapgialy
      181 pgqaqllsck hhyevipplt spgqpgdmnc ttqrinytdp fsnqtvksal ivqgprevkk
      241 relvflqfrl nkssedfsai dyllfssfqe flqspnrvgf mqacesayss wkfsggfrtw
      301 vkmslvktke edgreavefr qetsvvnyid qrpaakksaq lffvvfewkd pfiqkvqdiv
      361 tanpwntial lcgaflalfk aaefaklsik wmikirkryl krrgqatshi s
//
LOCUS       NP_001397850             198 aa            linear   PRI 06-DEC-2025
DEFINITION  testis-expressed protein 51 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001397850 XP_047298837
VERSION     NP_001397850.1
DBSOURCE    REFSEQ: accession NM_001410921.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Dupuis,S., Le Beulze,M., Vance,T.D.R., Pierre,R., Lee,J.E.,
            Ziyyat,A. and Barbaux,S.
  TITLE     Spermatozoa lacking TEX51 display hypofertility and defects in
            morphology
  JOURNAL   Commun Biol 8 (1), 1563 (2025)
   PUBMED   41233479
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114783.5.
            
            On Aug 17, 2022 this sequence version replaced XP_047298837.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.318041.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..198
                     /product="testis-expressed protein 51 isoform 2 precursor"
                     /note="testis-expressed protein 51"
                     /calculated_mol_wt=21177
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1609
     CDS             1..198
                     /gene="TEX51"
                     /coded_by="NM_001410921.1:30..626"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS92856.1"
                     /db_xref="GeneID:101929926"
                     /db_xref="HGNC:HGNC:52387"
ORIGIN      
        1 mlplliicll paiegknclr cwpelsalid ydlqilwvtp gpptelsqsi hslflednnf
       61 lkpwyldrdh leeetakfft qvhqaiktlr ddktvlleei ythknlfter lnkisdglke
      121 kdiqstlkvt scadcrthfl scndptfcpa rnrrtslwav slssalllai agggcffywq
      181 rkkeavkqeq gsphvfqk
//
LOCUS       NP_001364409             249 aa            linear   PRI 06-DEC-2025
DEFINITION  proton-activated chloride channel isoform 5 [Homo sapiens].
ACCESSION   NP_001364409 XP_016857126
VERSION     NP_001364409.1
DBSOURCE    REFSEQ: accession NM_001377480.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Pissas,K.P., Grunder,S. and Tian,Y.
  TITLE     Functional expression of the proton sensors ASIC1a, TMEM206, and
            OGR1 together with BKCa channels is associated with cell volume
            changes and cell death under strongly acidic conditions in DAOY
            medulloblastoma cells
  JOURNAL   Pflugers Arch 476 (6), 923-937 (2024)
   PUBMED   38627262
  REMARK    GeneRIF: Functional expression of the proton sensors ASIC1a,
            TMEM206, and OGR1 together with BKCa channels is associated with
            cell volume changes and cell death under strongly acidic conditions
            in DAOY medulloblastoma cells.
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Kostritskaia,Y., Klussendorf,M., Pan,Y.E., Hassani Nia,F.,
            Kostova,S. and Stauber,T.
  TITLE     Physiological Functions of the Volume-Regulated Anion Channel
            VRAC/LRRC8 and the Proton-Activated Chloride Channel ASOR/TMEM206
  JOURNAL   Handb Exp Pharmacol 283, 181-218 (2024)
   PUBMED   37468723
  REMARK    GeneRIF: Physiological Functions of the Volume-Regulated Anion
            Channel VRAC/LRRC8 and the Proton-Activated Chloride Channel
            ASOR/TMEM206.
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Ruan,Z., Osei-Owusu,J., Du,J., Qiu,Z. and Lu,W.
  TITLE     Structures and pH-sensing mechanism of the proton-activated
            chloride channel
  JOURNAL   Nature 588 (7837), 350-354 (2020)
   PUBMED   33149300
  REMARK    GeneRIF: Structures and pH-sensing mechanism of the
            proton-activated chloride channel.
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 249)
  AUTHORS   Ullrich,F., Blin,S., Lazarow,K., Daubitz,T., von Kries,J.P. and
            Jentsch,T.J.
  TITLE     Identification of TMEM206 proteins as pore of PAORAC/ASOR
            acid-sensitive chloride channels
  JOURNAL   Elife 8, e49187 (2019)
   PUBMED   31318332
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 249)
  AUTHORS   Yang,J., Chen,J., Del Carmen Vitery,M., Osei-Owusu,J., Chu,J.,
            Yu,H., Sun,S. and Qiu,Z.
  TITLE     PAC, an evolutionarily conserved membrane protein, is a
            proton-activated chloride channel
  JOURNAL   Science 364 (6438), 395-399 (2019)
   PUBMED   31023925
  REMARK    GeneRIF: PAC (TMEM206) was indentified as being essential for the
            widely observed proton-activated Cl- (PAC) currents (ICl,H).
            GeneRIF: PACC1 encodes a new type of chloride channel activated by
            acid or proton; its wide expression suggests a broad role for this
            conserved chloride channel in physiological and pathological
            processes associated with acidic pH.
REFERENCE   8  (residues 1 to 249)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   9  (residues 1 to 249)
  AUTHORS   Teckchandani,A., Toida,N., Goodchild,J., Henderson,C., Watts,J.,
            Wollscheid,B. and Cooper,J.A.
  TITLE     Quantitative proteomics identifies a Dab2/integrin module
            regulating cell migration
  JOURNAL   J Cell Biol 186 (1), 99-111 (2009)
   PUBMED   19581412
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092803.2, KF459533.1 and AL360091.28.
            
            On Jan 14, 2020 this sequence version replaced XP_016857126.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.109592.1,
                                           SRR3476690.188985.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..249
                     /product="proton-activated chloride channel isoform 5"
                     /note="transmembrane protein 206; proton-activated
                     chloride channel; acid-sensitive outwardly rectifying
                     channel; acid-sensitive outwardly-rectifying anion
                     channel; proton-activated outwardly rectifying anion
                     channel"
                     /calculated_mol_wt=28293
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9H813.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9D771; propagated from
                     UniProtKB/Swiss-Prot (Q9H813.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D771; propagated from
                     UniProtKB/Swiss-Prot (Q9H813.1)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q66H28; propagated from
                     UniProtKB/Swiss-Prot (Q9H813.1)"
     Region          55..>214
                     /region_name="TMEM206"
                     /note="TMEM206 protein family; pfam15122"
                     /db_xref="CDD:434477"
     Site            65..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H813.1)"
     Site            155
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q9H813.1)"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q9H813.1)"
     CDS             1..249
                     /gene="PACC1"
                     /gene_synonym="ASOR; C1orf75; hPAC; hTMEM206; PAC; PAORAC;
                     TMEM206"
                     /coded_by="NM_001377480.1:130..879"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:55248"
                     /db_xref="HGNC:HGNC:25593"
                     /db_xref="MIM:618427"
ORIGIN      
        1 mirqerstsy qelseelvqv venseladeq dketvrvqgp gilpgldses asssirfska
       61 clknvfsvll ifiylllmav avflvyrtit dfreklkhpv msvsykevdr ydapgialyp
      121 gqaqllsckh hyevipplts pgqpgdmnct tqrinytdpf snqtvksali vqgprevkkr
      181 elvflqfrln kssedfsaid yllfssfqef lqrqvwlttl trgqlpkkvl ncflwslngk
      241 ilssrkski
//
LOCUS       NP_001387121            1124 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 37 [Homo sapiens].
ACCESSION   NP_001387121 XP_011529766
VERSION     NP_001387121.1
DBSOURCE    REFSEQ: accession NM_001400192.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1124)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1124)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1124)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1124)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1124)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1124)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1124)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1124)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1124)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1124)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2 and AC010877.3.
            
            On Jan 20, 2022 this sequence version replaced XP_011529766.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612691.1, SRR18074969.1555619.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1124
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1124
                     /product="histone demethylase UTY isoform 37"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=122833
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..440
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..1124
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001400192.1:369..3743"
                     /note="isoform 37 is encoded by transcript variant 89"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq ngsdnwnggq slshhpvqqv yslcltpqkl qhleqlranr
      481 dnlnpaqkhq leqlesqfvl mqqmrhkeva qvrttgihng aitdsslptn svsnrqphga
      541 ltrvssvsqp gvrpacvekl lssgafsagc ipcgtskilg stdtillgsn ciagsesngn
      601 vpylqqntht lphnhtdlns steepwrkql snsaqglhks qssclsgpne eqplfstgsa
      661 qyhqatstgi kkanehltlp snsvpqgdad shlschtats ggqqgimftk eskpsknrsl
      721 vpetsrhtgd tsngcadvkg lsnhvhqlia davsspnhgd spnlliadnp qlsalligka
      781 ngnvgtgtcd kvnnihpavh tktdhsvass pssaistatp spksteqrsi nsvtslnsph
      841 sglhtvngeg lgksqsstkv dlplashrst sqilpsmsvs icpsstevlk acrnpgkngl
      901 snscilldkc ppprpptspy pplpkdklnp ptpsiylenk rdaffpplhq fctnpknpvt
      961 virglagalk ldlglfstkt lveannehmv evrtqllqpa denwdptgtk kiwrcesnrs
     1021 httiakyaqy qassfqeslr agmqwcdlss lqppppgfkr fshlslpnsw nyrhlpscpt
     1081 nfcifvetgf hhvgqaclel ltsggllasa sqsagitgvs hhar
//
LOCUS       NP_001369710             631 aa            linear   PRI 07-DEC-2025
DEFINITION  F-box/LRR-repeat protein 19 isoform 6 [Homo sapiens].
ACCESSION   NP_001369710
VERSION     NP_001369710.1
DBSOURCE    REFSEQ: accession NM_001382781.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Dong,H., Huang,C. and Huang,J.
  TITLE     FBXL19-AS1 promotes the progression of nasopharyngeal carcinoma by
            acting as a competing endogenous RNA to sponge miR-431 and
            upregulate PBOV1
  JOURNAL   Mol Med Rep 24 (3) (2021)
   PUBMED   34278444
  REMARK    GeneRIF: FBXL19AS1 promotes the progression of nasopharyngeal
            carcinoma by acting as a competing endogenous RNA to sponge miR431
            and upregulate PBOV1.
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Wang,L., Zhang,X., Liu,Y. and Xu,S.
  TITLE     Long noncoding RNA FBXL19-AS1 induces tumor growth and metastasis
            by sponging miR-203a-3p in lung adenocarcinoma
  JOURNAL   J Cell Physiol 235 (4), 3612-3625 (2020)
   PUBMED   31566718
  REMARK    GeneRIF: Long noncoding RNA FBXL19-AS1 induces tumor growth and
            metastasis by sponging miR-203a-3p in lung adenocarcinoma.
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Xu,C., Liu,K., Lei,M., Yang,A., Li,Y., Hughes,T.R. and Min,J.
  TITLE     DNA Sequence Recognition of Human CXXC Domains and Their Structural
            Determinants
  JOURNAL   Structure 26 (1), 85-95 (2018)
   PUBMED   29276034
REFERENCE   6  (residues 1 to 631)
  AUTHORS   Chandran,V.
  TITLE     The genetics of psoriasis and psoriatic arthritis
  JOURNAL   Clin Rev Allergy Immunol 44 (2), 149-156 (2013)
   PUBMED   22274791
  REMARK    Review article
REFERENCE   7  (residues 1 to 631)
  AUTHORS   Stuart,P.E., Nair,R.P., Ellinghaus,E., Ding,J., Tejasvi,T.,
            Gudjonsson,J.E., Li,Y., Weidinger,S., Eberlein,B., Gieger,C.,
            Wichmann,H.E., Kunz,M., Ike,R., Krueger,G.G., Bowcock,A.M.,
            Mrowietz,U., Lim,H.W., Voorhees,J.J., Abecasis,G.R.,
            Weichenthal,M., Franke,A., Rahman,P., Gladman,D.D. and Elder,J.T.
  TITLE     Genome-wide association analysis identifies three psoriasis
            susceptibility loci
  JOURNAL   Nat Genet 42 (11), 1000-1004 (2010)
   PUBMED   20953189
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 631)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   9  (residues 1 to 631)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of FBXL19 gene in silico
  JOURNAL   Int J Mol Med 14 (6), 1109-1114 (2004)
   PUBMED   15547684
REFERENCE   10 (residues 1 to 631)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC135048.2.
            
            Summary: This gene encodes a member of the Skp1-Cullin-F-box family
            of E3 ubiquitin ligases. The encoded protein is reported to bind to
            the transmembrane receptor interleukin 1 receptor-like 1 and
            regulate its ubiquitination and degradation. This protein has been
            linked to the regulation of pulmonary inflammation and psoriasis.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Aug 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3600763.1,
                                           SRR14038191.844369.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..631
                     /product="F-box/LRR-repeat protein 19 isoform 6"
                     /note="jumonji C domain-containing histone demethylase 1C;
                     F-box/LRR-repeat protein 19; jumonji C domain-containing
                     1C"
                     /calculated_mol_wt=69262
     Region          <30..57
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          67..128
                     /region_name="PHD_FXL19"
                     /note="PHD finger found in F-box and leucine-rich repeat
                     protein 19 (FBXL19); cd15645"
                     /db_xref="CDD:277115"
     Site            order(67,90..94,98,123)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277115"
     Region          358..400
                     /region_name="F-box_JHDM"
                     /note="F-box domain found in the JmjC domain-containing
                     histone demethylation protein (JHDM) family; cd22122"
                     /db_xref="CDD:438894"
     Site            order(361..362,364..366,368..369,371..373,375..376,
                     379..380,382..384,388)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438894"
     Region          398..422
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          403..602
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          423..445
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          447..470
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          471..510
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          511..535
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          536..560
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          566..590
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          591..623
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..631
                     /gene="FBXL19"
                     /gene_synonym="CXXC11; Fbl19; JHDM1C"
                     /coded_by="NM_001382781.1:913..2808"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:54620"
                     /db_xref="HGNC:HGNC:25300"
                     /db_xref="MIM:609085"
ORIGIN      
        1 mssssrgpga garrrrtrcr rcracvrtec gdchfcrdmk kfggpgrmkq scllrqctap
       61 vlphtavcll cgeagkedtv egeeekfgls lmecticnei vhpgclkmgk aegvinaeip
      121 ncwecprctq egrtskdsge gpgrrradng eegaslgsgw klteepplpp ppprrkgplp
      181 agpppedvpg ppkrkereag nepptprkkv kggrerhlkk kpkpplasae gpavpspspq
      241 reklerfkrm cqllervpdt sssssdsdsd sdssgtslse deapgearng rrpargssge
      301 kenrggrrav rpgsggplls wplgpapppr ppqlerhvvr ppprspepdt lplaagsdhp
      361 lpraawlrvf qhlgprelci cmrvcrtwsr wcydkrlwpr mdlsrrkslt ppmlsgvvrr
      421 qpraldlswt gvskkqlmwl lnrlqglqel vlsgcswlsv salgsaplpa lrlldlrwie
      481 dvkdsqlrel llpppdtkpg qtesrgrlqg vaelrlagle ltdaslrlll rhapqlsald
      541 lshcahvgdp svhlltapts plretlvhln lagchrltdh clplfrrcpr lrrldlrscr
      601 qlspeacarl aaagppgpfr cpeeklllkd s
//
LOCUS       NP_001245195            1367 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 21 [Homo sapiens].
ACCESSION   NP_001245195
VERSION     NP_001245195.1
DBSOURCE    REFSEQ: accession NM_001258266.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1367)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1367)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1367)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1367)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1367)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1367)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1367)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1367)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1367)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1367)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, EF653190.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (21) lacks two exons in the coding
            region, but maintains the reading frame, compared to variant 4. The
            encoded isoform (21) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF653190.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1367
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1367
                     /product="histone demethylase UTY isoform 21"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=151475
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..440
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1066..1130
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1100..1208
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1367
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258266.1:1006..5109"
                     /note="isoform 21 is encoded by transcript variant 21"
                     /db_xref="CCDS:CCDS76077.1"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq ngsdnwnggq slshhpvqqv yslcltpqkl qhleqlranr
      481 dnlnpaqkhq leqlesqfvl mqqmrhkeva qvrttgihng aitdsslptn svsnrqphga
      541 ltrvssvsqp gvrpacvekl lssgafsagc ipcgtskilg stdtillgsn ciagsesngn
      601 vpylqqntht lphnhtdlns steepwrkql snsaqglhks qssclsgpne eqplfstgsa
      661 qyhqatstgi kkanehltlp snsvpqgdad shlschtats ggqqgimftk eskpsknrsl
      721 vpetsrhtgd tsngcadvkg lsnhvhqlia davsspnhgd spnlliadnp qlsalligka
      781 ngnvgtgtcd kvnnihpavh tktdhsvass pssaistatp spksteqrsi nsvtslnsph
      841 sglhtvngeg lgksqsstkv dlplashrst sqilpsmsvs icpsstevlk acrnpgkngl
      901 snscilldkc ppprpptspy pplpkdklnp ptpsiylenk rdaffpplhq fctnpknpvt
      961 virglagalk ldlglfstkt lveannehmv evrtqllqpa denwdptgtk kiwrcesnrs
     1021 httiakyaqy qassfqeslr eenekrtqhk dhsdnestss ekwklqlhel tklpafarvv
     1081 sagnllthvg htilgmntvq lymkvpgsrt pghqennnfc svninigpgd cewfvvpedy
     1141 wgvlndfcek nnlnflmssw wpnledlyea nvpvyrfiqr pgdlvwinag tvhwvqavgw
     1201 cnniawnvgp ltacqyklav eryewnklks vkspvpmvhl swnmarnikv sdpklfemik
     1261 ycllkilkqy qtlrealvaa gkeviwhgrt ndepahycsi cevevfnllf vtnesntqkt
     1321 yivhchdcar ktskslenfv vleqykmedl iqvydqftla lslssss
//
LOCUS       NP_001387128            1095 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 39 [Homo sapiens].
ACCESSION   NP_001387128 XP_011529767
VERSION     NP_001387128.1
DBSOURCE    REFSEQ: accession NM_001400199.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1095)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1095)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1095)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1095)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1095)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1095)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1095)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1095)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1095)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1095)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2 and AC010877.3.
            
            On Jan 20, 2022 this sequence version replaced XP_011529767.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ341385.1, SRR18074969.2644939.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1095
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1095
                     /product="histone demethylase UTY isoform 39"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=119719
     Region          90..123
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..160
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          167..196
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          168..452
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..235
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..280
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          281..314
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          315..348
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..382
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          649..705
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          773..835
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            903
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24798337; propagated from
                     UniProtKB/Swiss-Prot (O14607.2)"
     CDS             1..1095
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001400199.1:369..3656"
                     /note="isoform 39 is encoded by transcript variant 91"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqngsdn wnggqslshh pvqqvyslcl
      421 tpqklqhleq lranrdnlnp aqkhqleqle sqfvlmqqmr hkevaqvrtt gihngaitds
      481 slptnsvsnr qphgaltrvs svsqpgvrpa cvekllssga fsagcipcgt skilgstdti
      541 llgsnciags esngnvpylq qnthtlphnh tdlnssteep wrkqlsnsaq aylghltgfi
      601 qdncnkglhk sqssclsgpn eeqplfstgs aqyhqatstg ikkanehltl psnsvpqgda
      661 dshlschtat sggqqgimft keskpsknrs lvpetsrhtg dtsngcadvk glsnhvhqli
      721 adavsspnhg dspnlliadn pqlsalligk angnvgtgtc dkvnnihpav htktdhsvas
      781 spssaistat pspksteqrs insvtslnsp hsglhtvnge glgksqsstk vdlplashrs
      841 tsqilpsmsv sicpsstevl kacrnpgkng lsnscilldk cppprpptsp ypplpkdkln
      901 pptpsiylen krdaffpplh qfctnpknpv tvirglagal kldlglfstk tlveannehm
      961 vevrtqllqp adenwdptgt kkiwrcesnr shttiakyaq yqassfqesl ragmqwcdls
     1021 slqppppgfk rfshlslpns wnyrhlpscp tnfcifvetg fhhvgqacle lltsggllas
     1081 asqsagitgv shhar
//
LOCUS       NP_001387102            1485 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 28 [Homo sapiens].
ACCESSION   NP_001387102 XP_011529754
VERSION     NP_001387102.1
DBSOURCE    REFSEQ: accession NM_001400173.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1485)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1485)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1485)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1485)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1485)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1485)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1485)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1485)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1485)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1485)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, AC010877.3 and
            AC244214.2.
            
            On Jan 20, 2022 this sequence version replaced XP_011529754.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1814240.1,
                                           SRR11853558.25551.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1485
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1485
                     /product="histone demethylase UTY isoform 28"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=164979
     Region          90..123
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..160
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          167..196
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          168..452
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..235
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..280
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          281..314
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          315..348
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..382
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          571..621
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          633..689
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          757..819
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            887
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24798337; propagated from
                     UniProtKB/Swiss-Prot (O14607.2)"
     Region          990..1026
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          1046..1110
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1080..1188
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1485
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001400173.1:369..4826"
                     /note="isoform 28 is encoded by transcript variant 80"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqngsdn wnggqslshh pvqqvyslcl
      421 tpqklqhleq lranrdnlnp aqkhqleqle sqfvlmqqmr hkevaqvrtt gihngaitds
      481 slptnsvsnr qphgaltrvs svsqpgvrpa cvekllssga fsagcipcgt skilgstdti
      541 llgsnciags esngnvpylq qnthtlphnh tdlnssteep wrkqlsnsaq glhksqsscl
      601 sgpneeqplf stgsaqyhqa tstgikkane hltlpsnsvp qgdadshlsc htatsggqqg
      661 imftkeskps knrslvpets rhtgdtsngc advkglsnhv hqliadavss pnhgdspnll
      721 iadnpqlsal ligkangnvg tgtcdkvnni hpavhtktdh svasspssai statpspkst
      781 eqrsinsvts lnsphsglht vngeglgksq sstkvdlpla shrstsqilp smsvsicpss
      841 tevlkacrnp gknglsnsci lldkcppprp ptspypplpk dklnpptpsi ylenkrdaff
      901 pplhqfctnp knpvtvirgl agalkldlgl fstktlvean nehmvevrtq llqpadenwd
      961 ptgtkkiwrc esnrshttia kyaqyqassf qeslreenek rtqhkdhsdn estssensgr
     1021 rrkgpfktik fgtnidlsdn kkwklqlhel tklpafarvv sagnllthvg htilgmntvq
     1081 lymkvpgsrt pghqennnfc svninigpgd cewfvvpedy wgvlndfcek nnlnflmssw
     1141 wpnledlyea nvpvyrfiqr pgdlvwinag tvhwvqavgw cnniawnvgp ltacqyklav
     1201 eryewnklks vkspvpmvhl swnmarnikv sdpklfemik ycllkilkqy qtlrealvaa
     1261 gkeviwhgrt ndepahycsi cevevfnllf vtnesntqkt yivhchdcar ktskslenfv
     1321 vleqykmedl iqvydqftla spwppmdqsa ftssllrpik algsgraeqt sgdqlqkgat
     1381 hsrassllra aemtrrpasr eelpdpglfc hsikllfvlf sfhlstflil pcqrrrtwel
     1441 ldggaesckt nrantpiahy lvseeerrav alqrvqtwel lepgl
//
LOCUS       NP_116267                238 aa            linear   PRI 07-DEC-2025
DEFINITION  probable RNA/DNA demethylase ALKBH6 isoform 3 [Homo sapiens].
ACCESSION   NP_116267
VERSION     NP_116267.4
DBSOURCE    REFSEQ: accession NM_032878.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Das,S., Rankawat,S., Shaji,U.P., Tuti,N., Shahnaz,N., Ray,S. and
            Anindya,R.
  TITLE     Identification of ALKBH6 as a nucleotide demethylase with a
            distinct substrate preference
  JOURNAL   J Biol Chem 301 (10), 110638 (2025)
   PUBMED   40885392
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Das,S., Shahnaz,N., Keerthana,C., Ranjan,S., Seenivasan,G.,
            Tuti,N., Shaji,U.P., Meur,G. and Anindya,R.
  TITLE     Functional and comparative analysis of the
            FeII/2-oxoglutarate-dependent dioxygenases without using any
            substrate
  JOURNAL   Biol Methods Protoc 10 (1), bpae096 (2024)
   PUBMED   39845104
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Ma,L., Lu,H., Tian,Z., Yang,M., Ma,J., Shang,G., Liu,Y., Xie,M.,
            Wang,G., Wu,W., Zhang,Z., Dai,S. and Chen,Z.
  TITLE     Structural insights into the interactions and epigenetic functions
            of human nucleic acid repair protein ALKBH6
  JOURNAL   J Biol Chem 298 (3), 101671 (2022)
   PUBMED   35120926
  REMARK    GeneRIF: Structural insights into the interactions and epigenetic
            functions of human nucleic acid repair protein ALKBH6.
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Kernstock,S., Davydova,E., Jakobsson,M., Moen,A., Pettersen,S.,
            Maelandsmo,G.M., Egge-Jacobsen,W. and Falnes,P.O.
  TITLE     Lysine methylation of VCP by a member of a novel human protein
            methyltransferase family
  JOURNAL   Nat Commun 3, 1038 (2012)
   PUBMED   22948820
REFERENCE   5  (residues 1 to 238)
  AUTHORS   Tsujikawa,K., Koike,K., Kitae,K., Shinkawa,A., Arima,H., Suzuki,T.,
            Tsuchiya,M., Makino,Y., Furukawa,T., Konishi,N. and Yamamoto,H.
  TITLE     Expression and sub-cellular localization of human ABH family
            molecules
  JOURNAL   J Cell Mol Med 11 (5), 1105-1116 (2007)
   PUBMED   17979886
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM713594.1, BC105801.1 and BU963363.1.
            
            On Apr 21, 2021 this sequence version replaced NP_116267.3.
            
            Transcript Variant: Variants 2, 3, and 5 encode the same isoform
            (3).
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB109556.1, CB109260.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398, SAMEA2155751
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000378875.8/
                                                ENSP00000368152.4
            RefSeq Select criteria           :: based on manual assertion,
                                                conservation, expression,
                                                longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..238
                     /product="probable RNA/DNA demethylase ALKBH6 isoform 3"
                     /EC_number="3.4.22.17"
                     /note="alkylated DNA repair protein alkB homolog 6;
                     probable alpha-ketoglutarate-dependent dioxygenase ABH6;
                     alkB, alkylation repair homolog 6;
                     alpha-ketoglutarate-dependent dioxygenase alkB homolog 6;
                     probable nucleic acid dioxygenase ALKBH6; probable RNA/DNA
                     demethylase ALKBH6"
                     /calculated_mol_wt=26352
     Region          23..224
                     /region_name="2OG-FeII_Oxy"
                     /note="2OG-Fe(II) oxygenase superfamily; cl21496"
                     /db_xref="CDD:473886"
     Region          138..161
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KRA9.2)"
     CDS             1..238
                     /gene="ALKBH6"
                     /gene_synonym="ABH6"
                     /coded_by="NM_032878.5:65..781"
                     /note="isoform 3 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS74342.1"
                     /db_xref="GeneID:84964"
                     /db_xref="HGNC:HGNC:28243"
                     /db_xref="MIM:613304"
ORIGIN      
        1 meeqdarvpa lepfrveqap pviyyvpdfi skeeeeyllr qvfnapkpkw tqlsgrklqn
       61 wgglphprgm vperlppwlq ryvdkvsnls lfgglpanhv lvnqylpgeg imphedgply
      121 yptvstislg shtvldfyep rrpedddpte qprppprptt sllleprsll vlrgpaytrl
      181 lhgiaaarvd aldaassppn aaacpsarpg aclvrgtrvs ltirrvprvl raglllgk
//
LOCUS       NP_001245182            1306 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 8 [Homo sapiens].
ACCESSION   NP_001245182
VERSION     NP_001245182.1
DBSOURCE    REFSEQ: accession NM_001258253.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1306)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1306)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1306)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1306)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1306)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1306)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1306)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1306)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1306)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1306)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, DQ350457.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (8) has multiple differences in
            the coding region, but maintains the reading frame, compared to
            variant 4. The encoded isoform (8) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ350457.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1306
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1306
                     /product="histone demethylase UTY isoform 8"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=144438
     Region          90..123
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..160
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          167..196
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          168..452
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..235
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..280
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          281..314
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          315..348
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..382
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          649..705
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          773..835
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            903
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24798337; propagated from
                     UniProtKB/Swiss-Prot (O14607.2)"
     Region          1006..1042
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          1062..1126
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1096..1204
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1306
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258253.1:1006..4926"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqngsdn wnggqslshh pvqqvyslcl
      421 tpqklqhleq lranrdnlnp aqkhqleqle sqfvlmqqmr hkevaqvrtt gihngaitds
      481 slptnsvsnr qphgaltrvs svsqpgvrpa cvekllssga fsagcipcgt skilgstdti
      541 llgsnciags esngnvpylq qnthtlphnh tdlnssteep wrkqlsnsaq aylghltgfi
      601 qdncnkglhk sqssclsgpn eeqplfstgs aqyhqatstg ikkanehltl psnsvpqgda
      661 dshlschtat sggqqgimft keskpsknrs lvpetsrhtg dtsngcadvk glsnhvhqli
      721 adavsspnhg dspnlliadn pqlsalligk angnvgtgtc dkvnnihpav htktdhsvas
      781 spssaistat pspksteqrs insvtslnsp hsglhtvnge glgksqsstk vdlplashrs
      841 tsqilpsmsv sicpsstevl kacrnpgkng lsnscilldk cppprpptsp ypplpkdkln
      901 pptpsiylen krdaffpplh qfctnpknpv tvirglagal kldlglfstk tlveannehm
      961 vevrtqllqp adenwdptgt kkiwrcesnr shttiakyaq yqassfqesl reenekrtqh
     1021 kdhsdnests sensgrrrkg pfktikfgtn idlsdnkkwk lqlheltklp afarvvsagn
     1081 llthvghtil gmntvqlymk vpgsrtpghq ennnfcsvni nigpgdcewf vvpedywgvl
     1141 ndfceknnln flmsswwpnl edlyeanvpv yrfiqrpgdl vwinagtvhw vqavgwcnni
     1201 awnvgpltac qyklaverye wnklksvksp vpmvhlswnm arnikvsdpk lfemikycll
     1261 kilkqyqtlr ealvaagkev iwhgrtndep ahycsiceal slssss
//
LOCUS       NP_005135               1189 aa            linear   PRI 07-DEC-2025
DEFINITION  lysine-specific demethylase hairless isoform a [Homo sapiens].
ACCESSION   NP_005135
VERSION     NP_005135.2
DBSOURCE    REFSEQ: accession NM_005144.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1189)
  AUTHORS   Saldanha,C., Vieira-Baptista,P., Costa,M., Silva,A.R., Picao,M. and
            Sousa,C.
  TITLE     Impact of a High Coverage Vaccination Rate on Human Papillomavirus
            Infection Prevalence in Young Women: A Cross-sectional Study
  JOURNAL   J Low Genit Tract Dis 24 (4), 363-366 (2020)
   PUBMED   32796265
  REMARK    GeneRIF: Impact of a High Coverage Vaccination Rate on Human
            Papillomavirus Infection Prevalence in Young Women: A
            Cross-sectional Study.
REFERENCE   2  (residues 1 to 1189)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1189)
  AUTHORS   Huang,Y., Cai,C., Ren,L., Cui,C., Zhang,X. and Liu,W.
  TITLE     Marie Unna hereditary hypotrichosis accompanied by multiple
            familial trichoepithelioma in a Chinese family
  JOURNAL   J Dermatol 46 (5), 413-417 (2019)
   PUBMED   30809827
  REMARK    GeneRIF: Study in a large, five-generation Han Chinese family with
            several patients presenting with Marie Unna hereditary
            hypotrichosis (MUHH) and multiple familial trichoepithelioma (MFT)
            revealed that the c.1A>G mutation in HR (U2HR) was present in all
            MUHH patients. No pathogenic variants were found in EPS8L3 or CYLD
            in any family members but FABP12 (rs536105592 G>A) was identified
            in the patients with both MUHH and MFT.
REFERENCE   4  (residues 1 to 1189)
  AUTHORS   Brook,L., Palade,P., Maatough,A., Whitfield,G.K., Emeterio,L.S.,
            Hsieh,D. and Hsieh,J.C.
  TITLE     Hairless regulates p53 target genes to exert tumor suppressive
            functions in glioblastoma
  JOURNAL   J Cell Biochem 120 (1), 533-543 (2019)
   PUBMED   30191601
  REMARK    GeneRIF: These results suggest that transcriptional repression or
            mutation of HR may contribute to glioblastoma pathogenesis, which
            uncovers a role of HR in brain and suggests that modulating HR
            activity in glioblastoma may be a therapeutic strategy.
REFERENCE   5  (residues 1 to 1189)
  AUTHORS   Duzenli,S., Redler,S., Muller,M., Polat,M., Dogruer,D.,
            Pasternack,S.M. and Betz,R.C.
  TITLE     Identification of a U2HR gene mutation in Turkish families with
            Marie Unna hereditary hypotrichosis
  JOURNAL   Clin Exp Dermatol 34 (8), e953-e956 (2009)
   PUBMED   20055871
  REMARK    GeneRIF: the first time that a mutation in U2HR has been identified
            in families from the Middle East
REFERENCE   6  (residues 1 to 1189)
  AUTHORS   Wen,Y., Liu,Y., Xu,Y., Zhao,Y., Hua,R., Wang,K., Sun,M., Li,Y.,
            Yang,S., Zhang,X.J., Kruse,R., Cichon,S., Betz,R.C., Nothen,M.M.,
            van Steensel,M.A., van Geel,M., Steijlen,P.M., Hohl,D., Huber,M.,
            Dunnill,G.S., Kennedy,C., Messenger,A., Munro,C.S., Terrinoni,A.,
            Hovnanian,A., Bodemer,C., de Prost,Y., Paller,A.S., Irvine,A.D.,
            Sinclair,R., Green,J., Shang,D., Liu,Q., Luo,Y., Jiang,L.,
            Chen,H.D., Lo,W.H., McLean,W.H., He,C.D. and Zhang,X.
  TITLE     Loss-of-function mutations of an inhibitory upstream ORF in the
            human hairless transcript cause Marie Unna hereditary hypotrichosis
  JOURNAL   Nat Genet 41 (2), 228-233 (2009)
   PUBMED   19122663
  REMARK    GeneRIF: A pathogenic initiation codon mutation in U2HR, an
            inhibitory upstream ORF in the 5' UTR of the gene encoding the
            human hairless homolog (HR).
            Erratum:[Nat Genet. 2009 Jun;41(6):762]
REFERENCE   7  (residues 1 to 1189)
  AUTHORS   Ahmad,W., Irvine,A.D., Lam,H., Buckley,C., Bingham,E.A.,
            Panteleyev,A.A., Ahmad,M., McGrath,J.A. and Christiano,A.M.
  TITLE     A missense mutation in the zinc-finger domain of the human hairless
            gene underlies congenital atrichia in a family of Irish travellers
  JOURNAL   Am J Hum Genet 63 (4), 984-991 (1998)
   PUBMED   9758627
REFERENCE   8  (residues 1 to 1189)
  AUTHORS   Cichon,S., Anker,M., Vogt,I.R., Rohleder,H., Putzstuck,M.,
            Hillmer,A., Farooq,S.A., Al-Dhafri,K.S., Ahmad,M., Haque,S.,
            Rietschel,M., Propping,P., Kruse,R. and Nothen,M.M.
  TITLE     Cloning, genomic organization, alternative transcripts and
            mutational analysis of the gene responsible for autosomal recessive
            universal congenital alopecia
  JOURNAL   Hum Mol Genet 7 (11), 1671-1679 (1998)
   PUBMED   9736769
  REMARK    Erratum:[Hum Mol Genet 1998 Nov;7(12):1987-8]
REFERENCE   9  (residues 1 to 1189)
  AUTHORS   Nothen,M.M., Cichon,S., Vogt,I.R., Hemmer,S., Kruse,R., Knapp,M.,
            Holler,T., Faiyaz ul Haque,M., Haque,S., Propping,P., Ahmad,M. and
            Rietschel,M.
  TITLE     A gene for universal congenital alopecia maps to chromosome 8p21-22
  JOURNAL   Am J Hum Genet 62 (2), 386-390 (1998)
   PUBMED   9463324
REFERENCE   10 (residues 1 to 1189)
  AUTHORS   Ahmad,W., Faiyaz ul Haque,M., Brancolini,V., Tsou,H.C., ul
            Haque,S., Lam,H., Aita,V.M., Owen,J., deBlaquiere,M., Frank,J.,
            Cserhalmi-Friedman,P.B., Leask,A., McGrath,J.A., Peacocke,M.,
            Ahmad,M., Ott,J. and Christiano,A.M.
  TITLE     Alopecia universalis associated with a mutation in the human
            hairless gene
  JOURNAL   Science 279 (5351), 720-724 (1998)
   PUBMED   9445480
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA114279.1, DA326731.1,
            AJ277165.2, AF039196.3, BM982749.1 and BX109092.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 29, 2002 this sequence version replaced NP_005135.1.
            
            Summary: This gene encodes a protein that is involved in hair
            growth. This protein functions as a transcriptional corepressor of
            multiple nuclear receptors, including thyroid hormone receptor, the
            retinoic acid receptor-related orphan receptors and the vitamin D
            receptors, and it interacts with histone deacetylases. The
            translation of this protein is modulated by a regulatory open
            reading frame (ORF) that exists upstream of the primary ORF.
            Mutations in this upstream ORF cause Marie Unna hereditary
            hypotrichosis (MUHH), an autosomal dominant form of genetic hair
            loss. Mutations in this gene also cause autosomal recessive
            congenital alopecia and atrichia with papular lesions, other
            diseases resulting in hair loss. Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Sequence Note: This RefSeq record represents the hairless protein
            encoded by the primary ORF. Four upstream ORFs (U1HR-U4HR), which
            may regulate translation of the primary ORF as described in
            PMID:19122663, are also annotated on this sequence.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF039196.3, BC067128.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381418.9/ ENSP00000370826.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            regulatory uORF        :: PMID: 19122663
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1189
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..1189
                     /product="lysine-specific demethylase hairless isoform a"
                     /EC_number="1.14.11.65"
                     /note="protein hairless; hairless homolog; hair growth
                     associated; lysine-specific demethylase hairless; [histone
                     H3]-dimethyl-L-lysine(9) demethylase hairless; lysine
                     demethylase 3D"
                     /calculated_mol_wt=127364
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43593.5)"
     Region          236..257
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43593.5)"
     Region          349..377
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43593.5)"
     Region          414..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43593.5)"
     Region          505..552
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43593.5)"
     Region          566..570
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O43593.5)"
     Region          598..>625
                     /region_name="FYVE_like_SF"
                     /note="FYVE domain like superfamily; cl28890"
                     /db_xref="CDD:333710"
     Site            order(610..615,620)
                     /site_type="other"
                     /note="phosphatidylinositol 3-phosphate binding site
                     [chemical binding]"
                     /db_xref="CDD:277249"
     Region          702..750
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43593.5)"
     Region          758..762
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O43593.5)"
     Region          <1095..1140
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     CDS             1..1189
                     /gene="HR"
                     /gene_synonym="ALUNC; AU; HSA277165; HYPT4; KDM3D; MUHH;
                     MUHH1"
                     /coded_by="NM_005144.5:624..4193"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6022.1"
                     /db_xref="GeneID:55806"
                     /db_xref="HGNC:HGNC:5172"
                     /db_xref="MIM:602302"
ORIGIN      
        1 mestpsflkg tptwektape ngivrqepgs pprdglhhgp lclgepapfw rgvlstpdsw
       61 lppgfpqgpk dmlplvegeg pqngerkvnw lgskeglrwk eamlthplaf cgpacpprcg
      121 plmpehsggh lksdpvafrp whcpflletk ilerapfwvp tclppylvsg lppehpcdwp
      181 ltphpwvysg gqpkvpsafs lgskgfyykd psiprlakep laaaepglfg lnsgghlqra
      241 geaerpslhq rdgemgagrq qnpcplflgq pdtvpwtswp acppglvhtl gnvwagpgdg
      301 nlgyqlgppa tprcpspepp vtqrgccssy pptkggglgp cgkcqegleg gasgasepse
      361 evnkasgpra cppshhtklk ktwltrhseq fecprgcpev eerpvarlra lkragspevq
      421 gamgspapkr ppdpfpgtae qgaggwqevr dtsignkdvd sgqhdeqkgp qdgqaslqdp
      481 glqdipclal paklaqcqsc aqaagegggh achsqqvrrs plggelqqee dtatnsssee
      541 gpgsgpdsrl stglakhlls glgdrlcrll rrerealawa qregqgpavt edspgiprcc
      601 srchhglfnt hwrcprcshr lcvacgrvag tgrarekagf qeqsaeectq eaghaacslm
      661 ltqfvssqal aelstamhqv wvkfdirghc pcqadarvwa pgdagqqkes tqktpptpqp
      721 scngdthrtk sikeetpdsa etpaedragr gplpcpslce llastavklc lgherihmaf
      781 apvtpalpsd dritnildsi iaqvverkiq ekalgpglra gpglrkglgl plspvrprlp
      841 ppgallwlqe pqpcprrgfh lfqehwrqgq pvlvsgiqrt lqgnlwgtea lgalggqvqa
      901 lsplgppqps slgsttfweg fswpelrpks degsvlllhr algdedtsrv enlaaslplp
      961 eycalhgkln lasylppgla lrplepqlwa aygvsphrgh lgtknlcvev adlvsilvha
     1021 dtplpawhra qkdflsgldg eglwspgsqv stvwhvfraq daqrirrflq mvcpagagal
     1081 epgapgscyl daglrrrlre ewgvscwtll qapgeavlvp agaphqvqgl vstvsvtqhf
     1141 lspetsalsa qlchqgpslp pdchllyaqm dwavfqavkv avgtlqeak
//
LOCUS       NP_001387106            1422 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 30 [Homo sapiens].
ACCESSION   NP_001387106 XP_011529760
VERSION     NP_001387106.1
DBSOURCE    REFSEQ: accession NM_001400177.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1422)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1422)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1422)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1422)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1422)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1422)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1422)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1422)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1422)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1422)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2 and AC010877.3.
            
            On Jan 20, 2022 this sequence version replaced XP_011529760.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.359804.1,
                                           SRR18074969.3645560.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1422
                     /product="histone demethylase UTY isoform 30"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=157504
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..441
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1121..1185
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1155..1263
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1422
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001400177.1:369..4637"
                     /note="isoform 30 is encoded by transcript variant 82"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq qslslhmits sqveglsspa kkkrtssptk ngsdnwnggq
      481 slshhpvqqv yslcltpqkl qhleqlranr dnlnpaqkhq leqlesqfvl mqqmrhkeva
      541 qvrttgihng aitdsslptn svsnrqphga ltrvssvsqp gvrpacvekl lssgafsagc
      601 ipcgtskilg stdtillgsn ciagsesngn vpylqqntht lphnhtdlns steepwrkql
      661 snsaqglhks qssclsgpne eqplfstgsa qyhqatstgi kkanehltlp snsvpqgdad
      721 shlschtats ggqqgimftk eskpsknrsl vpetsrhtgd tsngcadvkg lsnhvhqlia
      781 davsspnhgd spnlliadnp qlsalligka ngnvgtgtcd kvnnihpavh tktdhsvass
      841 pssaistatp spksteqrsi nsvtslnsph sglhtvngeg lgksqsstkv dlplashrst
      901 sqilpsmsvs icpsstevlk acrnpgkngl snscilldkc ppprpptspy pplpkdklnp
      961 ptpsiylenk rdaffpplhq fctnpknpvt virglagalk ldlglfstkt lveannehmv
     1021 evrtqllqpa denwdptgtk kiwrcesnrs httiakyaqy qassfqeslr eenekrtqhk
     1081 dhsdnestss ensgrrrkgp fktikfgtni dlsdnkkwkl qlheltklpa farvvsagnl
     1141 lthvghtilg mntvqlymkv pgsrtpghqe nnnfcsvnin igpgdcewfv vpedywgvln
     1201 dfceknnlnf lmsswwpnle dlyeanvpvy rfiqrpgdlv winagtvhwv qavgwcnnia
     1261 wnvgpltacq yklaveryew nklksvkspv pmvhlswnma rnikvsdpkl femikycllk
     1321 ilkqyqtlre alvaagkevi whgrtndepa hycsicevev fnllfvtnes ntqktyivhc
     1381 hdcarktsks lenfvvleqy kmedliqvyd qftlalslss ss
//
LOCUS       NP_001245185            1335 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 11 [Homo sapiens].
ACCESSION   NP_001245185
VERSION     NP_001245185.1
DBSOURCE    REFSEQ: accession NM_001258256.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1335)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1335)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1335)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1335)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1335)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1335)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1335)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1335)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1335)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1335)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, EF612663.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (11) lacks two exons in the coding
            region, but maintains the reading frame, compared to variant 4. The
            encoded isoform (11) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612663.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1335
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1335
                     /product="histone demethylase UTY isoform 11"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=147551
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..440
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1091..1155
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1125..1233
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1335
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258256.1:1006..5013"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS76078.1"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq ngsdnwnggq slshhpvqqv yslcltpqkl qhleqlranr
      481 dnlnpaqkhq leqlesqfvl mqqmrhkeva qvrttgihng aitdsslptn svsnrqphga
      541 ltrvssvsqp gvrpacvekl lssgafsagc ipcgtskilg stdtillgsn ciagsesngn
      601 vpylqqntht lphnhtdlns steepwrkql snsaqglhks qssclsgpne eqplfstgsa
      661 qyhqatstgi kkanehltlp snsvpqgdad shlschtats ggqqgimftk eskpsknrsl
      721 vpetsrhtgd tsngcadvkg lsnhvhqlia davsspnhgd spnlliadnp qlsalligka
      781 ngnvgtgtcd kvnnihpavh tktdhsvass pssaistatp spksteqrsi nsvtslnsph
      841 sglhtvngeg lgksqsstkv dlplashrst sqilpsmsvs icpsstevlk acrnpgkngl
      901 snscilldkc ppprpptspy pplpkdklnp ptpsiylenk rdaffpplhq fctnpknpvt
      961 virglagalk ldlglfstkt lveannehmv evrtqllqpa denwdptgtk kiwrcesnrs
     1021 httiakyaqy qassfqeslr eenekrtqhk dhsdnestss ensgrrrkgp fktikfgtni
     1081 dlsdnkkwkl qlheltklpa farvvsagnl lthvghtilg mntvqlymkv pgsrtpghqe
     1141 nnnfcsvnin igpgdcewfv vpedywgvln dfceknnlnf lmsswwpnle dlyeanvpvy
     1201 rfiqrpgdlv winagtvhwv qavgwcnnia wnvgpltacq yklaveryew nklksvkspv
     1261 pmvhlswnma rnikvsdpkl femikycllk ilkqyqtlre alvaagkevi whgrtndepa
     1321 hycsiceals lssss
//
LOCUS       NP_001245198            1293 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 24 [Homo sapiens].
ACCESSION   NP_001245198
VERSION     NP_001245198.1
DBSOURCE    REFSEQ: accession NM_001258269.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1293)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1293)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1293)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1293)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1293)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1293)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1293)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1293)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1293)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1293)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, EF612679.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (24) has multiple differences in
            the coding region, one of which results in a frameshift, compared
            to variant 4. The encoded isoform (24) is shorter and has a
            distinct C-terminus, compared to isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612679.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1293
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1293
                     /product="histone demethylase UTY isoform 24"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=144175
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..441
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          997..1061
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1031..1139
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1293
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258269.1:1006..4887"
                     /note="isoform 24 is encoded by transcript variant 24"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq qslslhmits sqveglsspa kkkrtssptk ngsdnwnggq
      481 slshhpvqqv yslcltpqkl qhleqlranr dnlnpaqkhq leqlesqfvl mqqmrhkeva
      541 qglhksqssc lsgpneeqpl fstgsaqyhq atstgikkan ehltlpsnsv pqgdadshls
      601 chtatsggqq gimftkeskp sknrslvpet srhtgdtsng cadvkglsnh vhqliadavs
      661 spnhgdspnl liadnpqlsa lligkangnv gtgtcdkvnn ihpavhtktd hsvasspssa
      721 istatpspks teqrsinsvt slnsphsglh tvngeglgks qsstkvdlpl ashrstsqil
      781 psmsvsicps stevlkacrn pgknglsnsc illdkcpppr pptspypplp kdklnpptps
      841 iylenkrdaf fpplhqfctn pknpvtvirg lagalkldlg lfstktlvea nnehmvevrt
      901 qllqpadenw dptgtkkiwr cesnrshtti akyaqyqass fqeslreene krtqhkdhsd
      961 nestssensg rrrkgpfkti kfgtnidlsd nkkwklqlhe ltklpafarv vsagnllthv
     1021 ghtilgmntv qlymkvpgsr tpghqennnf csvninigpg dcewfvvped ywgvlndfce
     1081 knnlnflmss wwpnledlye anvpvyrfiq rpgdlvwina gtvhwvqavg wcnniawnvg
     1141 pltacqykla veryewnklk svkspvpmvh lswnmarnik vsdpklfemi kycllkilkq
     1201 yqtlrealva agkeviwhgr tndepahycs icevevfnll fvtnesntqk tyivhchdca
     1261 rktskslenf vvleqykmed liqvydqftl vsh
//
LOCUS       NP_001245180            1363 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 6 [Homo sapiens].
ACCESSION   NP_001245180
VERSION     NP_001245180.1
DBSOURCE    REFSEQ: accession NM_001258251.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1363)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1363)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1363)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1363)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1363)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1363)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1363)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1363)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1363)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1363)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, DQ140388.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (6) has multiple differences in
            the coding region, but maintains the reading frame, compared to
            variant 4. The encoded isoform (6) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ140388.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1363
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1363
                     /product="histone demethylase UTY isoform 6"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=151193
     Region          90..123
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..160
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          167..196
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          168..452
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..235
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..280
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          281..314
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          315..348
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..382
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          649..705
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          773..835
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            903
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24798337; propagated from
                     UniProtKB/Swiss-Prot (O14607.2)"
     Region          1006..1042
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          1062..1126
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1096..1204
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1363
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258251.1:1006..5097"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS76075.1"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqngsdn wnggqslshh pvqqvyslcl
      421 tpqklqhleq lranrdnlnp aqkhqleqle sqfvlmqqmr hkevaqvrtt gihngaitds
      481 slptnsvsnr qphgaltrvs svsqpgvrpa cvekllssga fsagcipcgt skilgstdti
      541 llgsnciags esngnvpylq qnthtlphnh tdlnssteep wrkqlsnsaq aylghltgfi
      601 qdncnkglhk sqssclsgpn eeqplfstgs aqyhqatstg ikkanehltl psnsvpqgda
      661 dshlschtat sggqqgimft keskpsknrs lvpetsrhtg dtsngcadvk glsnhvhqli
      721 adavsspnhg dspnlliadn pqlsalligk angnvgtgtc dkvnnihpav htktdhsvas
      781 spssaistat pspksteqrs insvtslnsp hsglhtvnge glgksqsstk vdlplashrs
      841 tsqilpsmsv sicpsstevl kacrnpgkng lsnscilldk cppprpptsp ypplpkdkln
      901 pptpsiylen krdaffpplh qfctnpknpv tvirglagal kldlglfstk tlveannehm
      961 vevrtqllqp adenwdptgt kkiwrcesnr shttiakyaq yqassfqesl reenekrtqh
     1021 kdhsdnests sensgrrrkg pfktikfgtn idlsdnkkwk lqlheltklp afarvvsagn
     1081 llthvghtil gmntvqlymk vpgsrtpghq ennnfcsvni nigpgdcewf vvpedywgvl
     1141 ndfceknnln flmsswwpnl edlyeanvpv yrfiqrpgdl vwinagtvhw vqavgwcnni
     1201 awnvgpltac qyklaverye wnklksvksp vpmvhlswnm arnikvsdpk lfemikycll
     1261 kilkqyqtlr ealvaagkev iwhgrtndep ahycsiceve vfnllfvtne sntqktyivh
     1321 chdcarktsk slenfvvleq ykmedliqvy dqftlalsls sss
//
LOCUS       NP_009056               1347 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 3 [Homo sapiens].
ACCESSION   NP_009056
VERSION     NP_009056.3
DBSOURCE    REFSEQ: accession NM_007125.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1347)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1347)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1347)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1347)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1347)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1347)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1347)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1347)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1347)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1347)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF000994.1, AC006376.2 and
            AC010877.3.
            
            On Jul 24, 2003 this sequence version replaced NP_009056.2.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (3) lacks two consecutive exons in
            the coding region, but maintains the reading frame, compared to
            variant 4. The encoded isoform (3) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF000994.1, SRR1660809.218555.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1347
                     /product="histone demethylase UTY isoform 3"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=149417
     Region          90..123
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..160
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          167..196
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          168..452
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..235
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..280
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          281..314
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          315..348
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..382
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          571..621
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          633..689
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          757..819
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            887
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24798337; propagated from
                     UniProtKB/Swiss-Prot (O14607.2)"
     Region          990..1026
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          1046..1110
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1080..1188
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1347
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_007125.4:1006..5049"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS14783.1"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqngsdn wnggqslshh pvqqvyslcl
      421 tpqklqhleq lranrdnlnp aqkhqleqle sqfvlmqqmr hkevaqvrtt gihngaitds
      481 slptnsvsnr qphgaltrvs svsqpgvrpa cvekllssga fsagcipcgt skilgstdti
      541 llgsnciags esngnvpylq qnthtlphnh tdlnssteep wrkqlsnsaq glhksqsscl
      601 sgpneeqplf stgsaqyhqa tstgikkane hltlpsnsvp qgdadshlsc htatsggqqg
      661 imftkeskps knrslvpets rhtgdtsngc advkglsnhv hqliadavss pnhgdspnll
      721 iadnpqlsal ligkangnvg tgtcdkvnni hpavhtktdh svasspssai statpspkst
      781 eqrsinsvts lnsphsglht vngeglgksq sstkvdlpla shrstsqilp smsvsicpss
      841 tevlkacrnp gknglsnsci lldkcppprp ptspypplpk dklnpptpsi ylenkrdaff
      901 pplhqfctnp knpvtvirgl agalkldlgl fstktlvean nehmvevrtq llqpadenwd
      961 ptgtkkiwrc esnrshttia kyaqyqassf qeslreenek rtqhkdhsdn estssensgr
     1021 rrkgpfktik fgtnidlsdn kkwklqlhel tklpafarvv sagnllthvg htilgmntvq
     1081 lymkvpgsrt pghqennnfc svninigpgd cewfvvpedy wgvlndfcek nnlnflmssw
     1141 wpnledlyea nvpvyrfiqr pgdlvwinag tvhwvqavgw cnniawnvgp ltacqyklav
     1201 eryewnklks vkspvpmvhl swnmarnikv sdpklfemik ycllkilkqy qtlrealvaa
     1261 gkeviwhgrt ndepahycsi cevevfnllf vtnesntqkt yivhchdcar ktskslenfv
     1321 vleqykmedl iqvydqftla lslssss
//
LOCUS       NP_001269280             382 aa            linear   PRI 07-DEC-2025
DEFINITION  F-box/LRR-repeat protein 19 isoform 3 [Homo sapiens].
ACCESSION   NP_001269280
VERSION     NP_001269280.1
DBSOURCE    REFSEQ: accession NM_001282351.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Dong,H., Huang,C. and Huang,J.
  TITLE     FBXL19-AS1 promotes the progression of nasopharyngeal carcinoma by
            acting as a competing endogenous RNA to sponge miR-431 and
            upregulate PBOV1
  JOURNAL   Mol Med Rep 24 (3) (2021)
   PUBMED   34278444
  REMARK    GeneRIF: FBXL19AS1 promotes the progression of nasopharyngeal
            carcinoma by acting as a competing endogenous RNA to sponge miR431
            and upregulate PBOV1.
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Wang,L., Zhang,X., Liu,Y. and Xu,S.
  TITLE     Long noncoding RNA FBXL19-AS1 induces tumor growth and metastasis
            by sponging miR-203a-3p in lung adenocarcinoma
  JOURNAL   J Cell Physiol 235 (4), 3612-3625 (2020)
   PUBMED   31566718
  REMARK    GeneRIF: Long noncoding RNA FBXL19-AS1 induces tumor growth and
            metastasis by sponging miR-203a-3p in lung adenocarcinoma.
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Xu,C., Liu,K., Lei,M., Yang,A., Li,Y., Hughes,T.R. and Min,J.
  TITLE     DNA Sequence Recognition of Human CXXC Domains and Their Structural
            Determinants
  JOURNAL   Structure 26 (1), 85-95 (2018)
   PUBMED   29276034
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Chandran,V.
  TITLE     The genetics of psoriasis and psoriatic arthritis
  JOURNAL   Clin Rev Allergy Immunol 44 (2), 149-156 (2013)
   PUBMED   22274791
  REMARK    Review article
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Stuart,P.E., Nair,R.P., Ellinghaus,E., Ding,J., Tejasvi,T.,
            Gudjonsson,J.E., Li,Y., Weidinger,S., Eberlein,B., Gieger,C.,
            Wichmann,H.E., Kunz,M., Ike,R., Krueger,G.G., Bowcock,A.M.,
            Mrowietz,U., Lim,H.W., Voorhees,J.J., Abecasis,G.R.,
            Weichenthal,M., Franke,A., Rahman,P., Gladman,D.D. and Elder,J.T.
  TITLE     Genome-wide association analysis identifies three psoriasis
            susceptibility loci
  JOURNAL   Nat Genet 42 (11), 1000-1004 (2010)
   PUBMED   20953189
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 382)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   9  (residues 1 to 382)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of FBXL19 gene in silico
  JOURNAL   Int J Mol Med 14 (6), 1109-1114 (2004)
   PUBMED   15547684
REFERENCE   10 (residues 1 to 382)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA244744.1, AK127701.1 and
            AL137589.1.
            
            Summary: This gene encodes a member of the Skp1-Cullin-F-box family
            of E3 ubiquitin ligases. The encoded protein is reported to bind to
            the transmembrane receptor interleukin 1 receptor-like 1 and
            regulate its ubiquitination and degradation. This protein has been
            linked to the regulation of pulmonary inflammation and psoriasis.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (3) represents use of an alternate
            promoter and thus differs in the 5' UTR and 5' coding region
            compared to variant 1. These differences cause translation
            initiation at a downstream AUG, and the resulting isoform (3) has a
            shorter N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127701.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..382
                     /product="F-box/LRR-repeat protein 19 isoform 3"
                     /note="jumonji C domain-containing histone demethylase 1C;
                     F-box/LRR-repeat protein 19; jumonji C domain-containing
                     1C"
                     /calculated_mol_wt=42140
     Region          109..151
                     /region_name="F-box_JHDM"
                     /note="F-box domain found in the JmjC domain-containing
                     histone demethylation protein (JHDM) family; cd22122"
                     /db_xref="CDD:438894"
     Site            order(112..113,115..117,119..120,122..124,126..127,
                     130..131,133..135,139)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438894"
     Region          149..173
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          154..353
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          174..196
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          198..221
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          222..261
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          262..286
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          287..311
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          317..341
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          342..374
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..382
                     /gene="FBXL19"
                     /gene_synonym="CXXC11; Fbl19; JHDM1C"
                     /coded_by="NM_001282351.1:963..2111"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS73873.1"
                     /db_xref="GeneID:54620"
                     /db_xref="HGNC:HGNC:25300"
                     /db_xref="MIM:609085"
ORIGIN      
        1 mcqllervpd tsssssdsds dsdssgtsls edeapgearn grrpargssg ekenrggrra
       61 vrpgsggpll swplgpappp rppqlerhvv rppprspepd tlplaagsdh plpraawlrv
      121 fqhlgprelc icmrvcrtws rwcydkrlwp rmdlsrrksl tppmlsgvvr rqpraldlsw
      181 tgvskkqlmw llnrlqglqe lvlsgcswls vsalgsaplp alrlldlrwi edvkdsqlre
      241 lllpppdtkp gqtesrgrlq gvaelrlagl eltdaslrll lrhapqlsal dlshcahvgd
      301 psvhlltapt splretlvhl nlagchrltd hclplfrrcp rlrrldlrsc rqlspeacar
      361 laaagppgpf rcpeeklllk ds
//
LOCUS       NP_001245187            1399 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 13 [Homo sapiens].
ACCESSION   NP_001245187
VERSION     NP_001245187.1
DBSOURCE    REFSEQ: accession NM_001258258.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1399)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1399)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1399)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1399)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1399)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1399)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1399)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1399)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1399)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1399)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, EF612673.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (13) lacks an exon in the coding
            region, but maintains the reading frame, compared to variant 4. The
            encoded isoform (13) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612673.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1399
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1399
                     /product="histone demethylase UTY isoform 13"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=155138
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..399
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1098..1162
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1132..1240
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1399
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258258.1:1006..5205"
                     /note="isoform 13 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS76076.1"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqayrah dpntehvlnh sqtpilqqsl
      421 slhmitssqv eglsspakkk rtssptkngs dnwnggqsls hhpvqqvysl cltpqklqhl
      481 eqlranrdnl npaqkhqleq lesqfvlmqq mrhkevaqvr ttgihngait dsslptnsvs
      541 nrqphgaltr vssvsqpgvr pacvekllss gafsagcipc gtskilgstd tillgsncia
      601 gsesngnvpy lqqnthtlph nhtdlnsste epwrkqlsns aqglhksqss clsgpneeqp
      661 lfstgsaqyh qatstgikka nehltlpsns vpqgdadshl schtatsggq qgimftkesk
      721 psknrslvpe tsrhtgdtsn gcadvkglsn hvhqliadav sspnhgdspn lliadnpqls
      781 alligkangn vgtgtcdkvn nihpavhtkt dhsvasspss aistatpspk steqrsinsv
      841 tslnsphsgl htvngeglgk sqsstkvdlp lashrstsqi lpsmsvsicp sstevlkacr
      901 npgknglsns cilldkcppp rpptspyppl pkdklnpptp siylenkrda ffpplhqfct
      961 npknpvtvir glagalkldl glfstktlve annehmvevr tqllqpaden wdptgtkkiw
     1021 rcesnrshtt iakyaqyqas sfqeslreen ekrtqhkdhs dnestssens grrrkgpfkt
     1081 ikfgtnidls dnkkwklqlh eltklpafar vvsagnllth vghtilgmnt vqlymkvpgs
     1141 rtpghqennn fcsvninigp gdcewfvvpe dywgvlndfc eknnlnflms swwpnledly
     1201 eanvpvyrfi qrpgdlvwin agtvhwvqav gwcnniawnv gpltacqykl averyewnkl
     1261 ksvkspvpmv hlswnmarni kvsdpklfem ikycllkilk qyqtlrealv aagkeviwhg
     1321 rtndepahyc sicevevfnl lfvtnesntq ktyivhchdc arktskslen fvvleqykme
     1381 dliqvydqft lalslssss
//
LOCUS       NP_001034485             716 aa            linear   PRI 07-DEC-2025
DEFINITION  macrophage-expressed gene 1 protein precursor [Homo sapiens].
ACCESSION   NP_001034485 XP_166227 XP_948351
VERSION     NP_001034485.1
DBSOURCE    REFSEQ: accession NM_001039396.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Rodriguez-Silvestre,P., Laub,M., Krawczyk,P.A., Davies,A.K.,
            Schessner,J.P., Parveen,R., Tuck,B.J., McEwan,W.A., Borner,G.H.H.
            and Kozik,P.
  TITLE     Perforin-2 is a pore-forming effector of endocytic escape in
            cross-presenting dendritic cells
  JOURNAL   Science 380 (6651), 1258-1265 (2023)
   PUBMED   37347855
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Pastar,I., Sawaya,A.P., Marjanovic,J., Burgess,J.L., Strbo,N.,
            Rivas,K.E., Wikramanayake,T.C., Head,C.R., Stone,R.C., Jozic,I.,
            Stojadinovic,O., Kornfeld,E.Y., Kirsner,R.S., Lev-Tov,H. and
            Tomic-Canic,M.
  TITLE     Intracellular Staphylococcus aureus triggers pyroptosis and
            contributes to inhibition of healing due to perforin-2 suppression
  JOURNAL   J Clin Invest 131 (24) (2021)
   PUBMED   34730110
  REMARK    GeneRIF: Intracellular Staphylococcus aureus triggers pyroptosis
            and contributes to inhibition of healing due to perforin-2
            suppression.
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Merselis,L.C., Rivas,Z.P. and Munson,G.P.
  TITLE     Breaching the Bacterial Envelope: The Pivotal Role of Perforin-2
            (MPEG1) Within Phagocytes
  JOURNAL   Front Immunol 12, 597951 (2021)
   PUBMED   33692780
  REMARK    GeneRIF: Breaching the Bacterial Envelope: The Pivotal Role of
            Perforin-2 (MPEG1) Within Phagocytes.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 716)
  AUTHORS   Merselis,L.C., Jiang,S.Y., Nelson,S.F., Lee,H., Prabaker,K.K.,
            Baker,J.L., Munson,G.P. and Butte,M.J.
  TITLE     MPEG1/Perforin-2 Haploinsufficiency Associated Polymicrobial Skin
            Infections and Considerations for Interferon-gamma Therapy
  JOURNAL   Front Immunol 11, 601584 (2020)
   PUBMED   33224153
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 716)
  AUTHORS   Kattel,S., Bhatt,H., Xu,S., Gurung,S., Pokharel,S. and Sharma,U.C.
  TITLE     Macrophage-specific protein perforin-2 is associated with poor
            neurological recovery and reduced survival after sudden cardiac
            arrest
  JOURNAL   Resuscitation 155, 180-188 (2020)
   PUBMED   32828820
  REMARK    GeneRIF: Macrophage-specific protein perforin-2 is associated with
            poor neurological recovery and reduced survival after sudden
            cardiac arrest.
REFERENCE   6  (residues 1 to 716)
  AUTHORS   McCormack,R. and Podack,E.R.
  TITLE     Perforin-2/Mpeg1 and other pore-forming proteins throughout
            evolution
  JOURNAL   J Leukoc Biol 98 (5), 761-768 (2015)
   PUBMED   26307549
  REMARK    GeneRIF: the impact of Perforin-2/macrophage-expressed protein 1
            from the earliest multicellular organisms to modern vertebrates, as
            well as review the development of other membrane attack complexes
            of complement and Perforin domain member proteins
            Review article
REFERENCE   7  (residues 1 to 716)
  AUTHORS   Fields,K.A., McCormack,R., de Armas,L.R. and Podack,E.R.
  TITLE     Perforin-2 restricts growth of Chlamydia trachomatis in macrophages
  JOURNAL   Infect Immun 81 (8), 3045-3054 (2013)
   PUBMED   23753625
  REMARK    GeneRIF: Knockdown of perforin-2 in macrophages did not alter the
            invasion of host cells but did result in chlamydial growth that
            closely mirrored that detected in HeLa cells.
REFERENCE   8  (residues 1 to 716)
  AUTHORS   McCormack,R., de Armas,L.R., Shiratsuchi,M., Ramos,J.E. and
            Podack,E.R.
  TITLE     Inhibition of intracellular bacterial replication in fibroblasts is
            dependent on the perforin-like protein (perforin-2) encoded by
            macrophage-expressed gene 1
  JOURNAL   J Innate Immun 5 (2), 185-194 (2013)
   PUBMED   23257510
REFERENCE   9  (residues 1 to 716)
  AUTHORS   Grandea,A.G. 3rd, Comber,P.G., Wenderfer,S.E., Schoenhals,G.,
            Fruh,K., Monaco,J.J. and Spies,T.
  TITLE     Sequence, linkage to H2-K, and function of mouse tapasin in MHC
            class I assembly
  JOURNAL   Immunogenetics 48 (4), 260-265 (1998)
   PUBMED   9716645
REFERENCE   10 (residues 1 to 716)
  AUTHORS   Spilsbury,K., O'Mara,M.A., Wu,W.M., Rowe,P.B., Symonds,G. and
            Takayama,Y.
  TITLE     Isolation of a novel macrophage-specific gene by differential cDNA
            analysis
  JOURNAL   Blood 85 (6), 1620-1629 (1995)
   PUBMED   7888681
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA946058.1, BC104997.1, AP002358.3 and AW205154.1.
            
            On or before Mar 20, 2007 this sequence version replaced
            XP_166227.3, XP_948351.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR1803616.267486.1, AK097881.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361050.4/ ENSP00000354335.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..716
                     /product="macrophage-expressed gene 1 protein precursor"
                     /note="macrophage expressed gene 1; macrophage gene 1
                     protein; macrophage-expressed gene 1 protein; perforin 2;
                     macrophage proliferation speci fi c gene-1"
                     /calculated_mol_wt=76651
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1954
     mat_peptide     18..716
                     /product="Macrophage-expressed gene 1 protein.
                     /evidence=ECO:0000255. /id=PRO_0000324143"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M385.1)"
                     /calculated_mol_wt=76651
     Site            113..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M385.1)"
     Region          125..341
                     /region_name="MACPF"
                     /note="MAC/Perforin domain; pfam01823"
                     /db_xref="CDD:460349"
     Site            127..132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M385.1)"
     Site            185
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:31537793,
                     ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J,
                     ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L,
                     ECO:0007744|PDB:6U2W; propagated from UniProtKB/Swiss-Prot
                     (Q2M385.1)"
     Site            235..244
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M385.1)"
     Site            248..256
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M385.1)"
     Site            269
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:31537793,
                     ECO:0007744|PDB:6U23, ECO:0007744|PDB:6U2J,
                     ECO:0007744|PDB:6U2K, ECO:0007744|PDB:6U2L,
                     ECO:0007744|PDB:6U2W; propagated from UniProtKB/Swiss-Prot
                     (Q2M385.1)"
     Region          347..630
                     /region_name="MPEG1_P2"
                     /note="P2 domain of macrophage-expressed gene 1 protein
                     (MPEG1) and similar proteins; cd22579"
                     /db_xref="CDD:439345"
     Site            352..353
                     /site_type="cleavage"
                     /note="Cleavage, by LGMN.
                     /evidence=ECO:0000250|UniProtKB:A1L314; propagated from
                     UniProtKB/Swiss-Prot (Q2M385.1)"
     mat_peptide     353..632
                     /product="Macrophage-expressed gene 1 protein, processed
                     form. /evidence=ECO:0000250|UniProtKB:A1L314.
                     /id=PRO_0000459022"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M385.1)"
                     /calculated_mol_wt=30591
     Site            357..358
                     /site_type="cleavage"
                     /note="Cleavage, by LGMN.
                     /evidence=ECO:0000250|UniProtKB:A1L314; propagated from
                     UniProtKB/Swiss-Prot (Q2M385.1)"
     Site            359..360
                     /site_type="cleavage"
                     /note="Cleavage, by LGMN.
                     /evidence=ECO:0000250|UniProtKB:A1L314; propagated from
                     UniProtKB/Swiss-Prot (Q2M385.1)"
     Site            order(364..367,455,485,488,497,502..503)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:439345"
     Site            375
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2M385.1)"
     Region          413..656
                     /region_name="P2. /evidence=ECO:0000250|UniProtKB:A1L314"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M385.1)"
     Site            631..632
                     /site_type="cleavage"
                     /note="Cleavage, by trypsin.
                     /evidence=ECO:0000250|UniProtKB:A1L314; propagated from
                     UniProtKB/Swiss-Prot (Q2M385.1)"
     Site            656..676
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M385.1)"
     CDS             1..716
                     /gene="MPEG1"
                     /gene_synonym="IMD77; Mpg-1; MPG1; MPS-1; MPS1; P-2; P2"
                     /coded_by="NM_001039396.2:63..2213"
                     /db_xref="CCDS:CCDS41650.1"
                     /db_xref="GeneID:219972"
                     /db_xref="HGNC:HGNC:29619"
                     /db_xref="MIM:610390"
ORIGIN      
        1 mnnfratilf waaaawaksg kpsgemdevg vqkcknalkl pvlevlpggg wdnlrnvdmg
       61 rvmeltysnc rttedgqyii pdeiftipqk qsnlemnsei leswanyqss tsysintels
      121 lfskvngkfs tefqrmktlq vkdqaittrv qvrnlvytvk inptlelssg frkelldisd
      181 rlennqtrma tylaellvln ygthvttsvd agaaliqedh lrasflqdsq ssrsavtasa
      241 glafqntvnf kfeenytsqn vltksylsnr tnsrvqsigg vpfypgitlq awqqgitnhl
      301 vaidrsglpl hffinpnmlp dlpgplvkkv sktvetavkr yytfntypgc tdlnspnfnf
      361 qantddgsce gkmtnfsfgg vyqectqlsg nrdvllcqkl eqknpltgdf scpsgyspvh
      421 llsqiheegy nhlechrkct llvfcktvce dvfqvakaef rafwcvassq vpensgllfg
      481 glfssksinp mtnaqscpag yfplrlfenl kvcvsqdyel gsrfavpfgg ffsctvgnpl
      541 vdpaisrdlg apslkkcpgg fsqhpalisd gcqvsycvks glftggslpp arlppftrpp
      601 lmsqaatntv ivtnsenars wikdsqthqw rlgepielrr amnvihgdgg glsggaaagv
      661 tvgvttilav vitlaiygtr kfkkkayqai eerqslvpgt aatgdttyqe qgqspa
//
LOCUS       NP_001387118            1125 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 36 [Homo sapiens].
ACCESSION   NP_001387118 XP_016885561
VERSION     NP_001387118.1
DBSOURCE    REFSEQ: accession NM_001400189.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1125)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1125)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1125)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1125)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1125)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1125)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1125)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1125)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1125)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1125)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2 and AC010877.3.
            
            On Jan 20, 2022 this sequence version replaced XP_016885561.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF653181.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1125
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1125
                     /product="histone demethylase UTY isoform 36"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=122916
     Region          <72..158
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..401
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..1125
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001400189.1:369..3746"
                     /note="isoform 36 is encoded by transcript variant 88"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqqslsl hmitssqveg lsspakkkrt
      421 ssptkngsdn wnggqslshh pvqqvyslcl tpqklqhleq lranrdnlnp aqkhqleqle
      481 sqfvlmqqmr hkevaqvrtt gihngaitds slptnsvsnr qphgaltrvs svsqpgvrpa
      541 cvekllssga fsagcipcgt skilgstdti llgsnciags esngnvpylq qnthtlphnh
      601 tdlnssteep wrkqlsnsaq aylghltgfi qdncnkglhk sqssclsgpn eeqplfstgs
      661 aqyhqatstg ikkanehltl psnsvpqgda dshlschtat sggqqgimft keskpsknrs
      721 lvpetsrhtg dtsngcadvk glsnhvhqli adavsspnhg dspnlliadn pqlsalligk
      781 angnvgtgtc dkvnnihpav htktdhsvas spssaistat pspksteqrs insvtslnsp
      841 hsglhtvnge glgksqsstk vdlplashrs tsqilpsmsv sicpsstevl kacrnpgkng
      901 lsnscilldk cppprpptsp ypplpkdkln pptpsiylen krdaffpplh qfctnpknpv
      961 tvirglagal kldlglfstk tlveannehm vevrtqllqp adenwdptgt kkiwrcesnr
     1021 shttiakyaq yqassfqesl ragmqwcdls slqppppgfk rfshlslpns wnyrhlpscp
     1081 tnfcifvetg fhhvgqacle lltsggllas asqsagitgv shhar
//
LOCUS       NP_001245179            1207 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 5 [Homo sapiens].
ACCESSION   NP_001245179
VERSION     NP_001245179.1
DBSOURCE    REFSEQ: accession NM_001258250.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1207)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1207)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1207)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1207)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1207)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1207)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1207)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1207)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1207)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1207)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, AY934850.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (5) has multiple differences in
            the coding region, but maintains the reading frame, compared to
            variant 4. The encoded isoform (5) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY934850.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1207
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1207
                     /product="histone demethylase UTY isoform 5"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=134679
     Region          <72..158
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..436
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          201..231
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(241,244..245,248..249,251,300,303..304,307..308,
                     310..311,334,337..338,341..342,345)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          280..328
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          333..361
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          906..970
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          940..1048
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1207
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258250.1:1006..4629"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrq sidkseasad
      301 twcsigvlyq qqnqpmdalq ayicavqldh ghaaawmdlg tlyescnqpq daikcylnaa
      361 rskrcsntst laarikflqn gsdnwnggqs lshhpvqqvy slcltpqklq hleqlranrd
      421 nlnpaqkhql eqlesqfvlm qqmrhkevaq glhksqsscl sgpneeqplf stgsaqyhqa
      481 tstgikkane hltlpsnsvp qgdadshlsc htatsggqqg imftkeskps knrslvpets
      541 rhtgdtsngc advkglsnhv hqliadavss pnhgdspnll iadnpqlsal ligkangnvg
      601 tgtcdkvnni hpavhtktdh svasspssai statpspkst eqrsinsvts lnsphsglht
      661 vngeglgksq sstkvdlpla shrstsqilp smsvsicpss tevlkacrnp gknglsnsci
      721 lldkcppprp ptspypplpk dklnpptpsi ylenkrdaff pplhqfctnp knpvtvirgl
      781 agalkldlgl fstktlvean nehmvevrtq llqpadenwd ptgtkkiwrc esnrshttia
      841 kyaqyqassf qeslreenek rtqhkdhsdn estssensgr rrkgpfktik fgtnidlsdn
      901 kkwklqlhel tklpafarvv sagnllthvg htilgmntvq lymkvpgsrt pghqennnfc
      961 svninigpgd cewfvvpedy wgvlndfcek nnlnflmssw wpnledlyea nvpvyrfiqr
     1021 pgdlvwinag tvhwvqavgw cnniawnvgp ltacqyklav eryewnklks vkspvpmvhl
     1081 swnmarnikv sdpklfemik ycllkilkqy qtlrealvaa gkeviwhgrt ndepahycsi
     1141 cevevfnllf vtnesntqkt yivhchdcar ktskslenfv vleqykmedl iqvydqftla
     1201 lslssss
//
LOCUS       NP_001245191            1320 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 17 [Homo sapiens].
ACCESSION   NP_001245191
VERSION     NP_001245191.1
DBSOURCE    REFSEQ: accession NM_001258262.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1320)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1320)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1320)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1320)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1320)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1320)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1320)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1320)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1320)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1320)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, EF612684.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (17) uses an alternate splice site
            in the coding region, but maintains the reading frame, compared to
            variant 4. The encoded isoform (17) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612684.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1320
                     /product="histone demethylase UTY isoform 17"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=147108
     Region          90..123
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..160
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          167..196
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          168..445
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..235
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..280
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          281..314
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          315..348
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..382
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1019..1083
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1053..1161
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1320
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258262.1:1006..4968"
                     /note="isoform 17 is encoded by transcript variant 17"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq ayrahdpnte hvlnhsqtpi lqqslslhmi tssqveglss
      481 pakkkrtssp tkngsdnwng gqslshhpvq qvyslcltpq klqhleqlra nrdnlnpaqk
      541 hqleqlesqf vlmqqmrhke vaqglhksqs sclsgpneeq plfstgsaqy hqatstgikk
      601 anehltlpsn svpqgdadsh lschtatsgg qqgimftkes kpsknrslvp etsrhtgdts
      661 ngcadvkgls nhvhqliada vsspnhgdsp nlliadnpql salligkang nvgtgtcdkv
      721 nnihpavhtk tdhsvassps saistatpsp ksteqrsins vtslnsphsg lhtvngeglg
      781 ksqsstkvdl plashrstsq ilpsmsvsic psstevlkac rnpgknglsn scilldkcpp
      841 prpptspypp lpkdklnppt psiylenkrd affpplhqfc tnpknpvtvi rglagalkld
      901 lglfstktlv eannehmvev rtqllqpade nwdptgtkki wrcesnrsht tiakyaqyqa
      961 ssfqeslree nekrtqhkdh sdnestssen sgrrrkgpfk tikfgtnidl sdnkkwklql
     1021 heltklpafa rvvsagnllt hvghtilgmn tvqlymkvpg srtpghqenn nfcsvninig
     1081 pgdcewfvvp edywgvlndf ceknnlnflm sswwpnledl yeanvpvyrf iqrpgdlvwi
     1141 nagtvhwvqa vgwcnniawn vgpltacqyk laveryewnk lksvkspvpm vhlswnmarn
     1201 ikvsdpklfe mikycllkil kqyqtlreal vaagkeviwh grtndepahy csicevevfn
     1261 llfvtnesnt qktyivhchd carktsksle nfvvleqykm edliqvydqf tlalslssss
//
LOCUS       NP_001372985             169 aa            linear   PRI 07-DEC-2025
DEFINITION  probable RNA/DNA demethylase ALKBH6 isoform 4 [Homo sapiens].
ACCESSION   NP_001372985 XP_024307515
VERSION     NP_001372985.1
DBSOURCE    REFSEQ: accession NM_001386056.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Das,S., Rankawat,S., Shaji,U.P., Tuti,N., Shahnaz,N., Ray,S. and
            Anindya,R.
  TITLE     Identification of ALKBH6 as a nucleotide demethylase with a
            distinct substrate preference
  JOURNAL   J Biol Chem 301 (10), 110638 (2025)
   PUBMED   40885392
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Das,S., Shahnaz,N., Keerthana,C., Ranjan,S., Seenivasan,G.,
            Tuti,N., Shaji,U.P., Meur,G. and Anindya,R.
  TITLE     Functional and comparative analysis of the
            FeII/2-oxoglutarate-dependent dioxygenases without using any
            substrate
  JOURNAL   Biol Methods Protoc 10 (1), bpae096 (2024)
   PUBMED   39845104
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Ma,L., Lu,H., Tian,Z., Yang,M., Ma,J., Shang,G., Liu,Y., Xie,M.,
            Wang,G., Wu,W., Zhang,Z., Dai,S. and Chen,Z.
  TITLE     Structural insights into the interactions and epigenetic functions
            of human nucleic acid repair protein ALKBH6
  JOURNAL   J Biol Chem 298 (3), 101671 (2022)
   PUBMED   35120926
  REMARK    GeneRIF: Structural insights into the interactions and epigenetic
            functions of human nucleic acid repair protein ALKBH6.
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Kernstock,S., Davydova,E., Jakobsson,M., Moen,A., Pettersen,S.,
            Maelandsmo,G.M., Egge-Jacobsen,W. and Falnes,P.O.
  TITLE     Lysine methylation of VCP by a member of a novel human protein
            methyltransferase family
  JOURNAL   Nat Commun 3, 1038 (2012)
   PUBMED   22948820
REFERENCE   5  (residues 1 to 169)
  AUTHORS   Tsujikawa,K., Koike,K., Kitae,K., Shinkawa,A., Arima,H., Suzuki,T.,
            Tsuchiya,M., Makino,Y., Furukawa,T., Konishi,N. and Yamamoto,H.
  TITLE     Expression and sub-cellular localization of human ABH family
            molecules
  JOURNAL   J Cell Mol Med 11 (5), 1105-1116 (2007)
   PUBMED   17979886
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC002116.1 and BE257397.1.
            
            On Aug 5, 2020 this sequence version replaced XP_024307515.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC007601.1, BE257397.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398, SAMEA2155751
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..169
                     /product="probable RNA/DNA demethylase ALKBH6 isoform 4"
                     /EC_number="3.4.22.17"
                     /note="alkylated DNA repair protein alkB homolog 6;
                     probable alpha-ketoglutarate-dependent dioxygenase ABH6;
                     alkB, alkylation repair homolog 6;
                     alpha-ketoglutarate-dependent dioxygenase alkB homolog 6;
                     probable nucleic acid dioxygenase ALKBH6; probable RNA/DNA
                     demethylase ALKBH6"
                     /calculated_mol_wt=18292
     Region          <6..155
                     /region_name="2OG-FeII_Oxy"
                     /note="2OG-Fe(II) oxygenase superfamily; cl21496"
                     /db_xref="CDD:473886"
     CDS             1..169
                     /gene="ALKBH6"
                     /gene_synonym="ABH6"
                     /coded_by="NM_001386056.1:304..813"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:84964"
                     /db_xref="HGNC:HGNC:28243"
                     /db_xref="MIM:613304"
ORIGIN      
        1 mvperlppwl qryvdkvsnl slfgglpanh vlvnqylpge gimphedgpl yyptvstisl
       61 gshtvldfye prrpedddpt eqprppprpt tsllleprsl lvlrgpaytr llhgiaaarv
      121 daldaasspp naaacpsarp gaclvrgtrv sltirrvprv lraglllgk
//
LOCUS       NP_001245186            1223 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 12 [Homo sapiens].
ACCESSION   NP_001245186
VERSION     NP_001245186.1
DBSOURCE    REFSEQ: accession NM_001258257.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1223)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1223)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1223)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1223)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1223)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1223)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1223)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1223)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1223)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1223)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, EF612664.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (12) has multiple differences in
            the coding region, but maintains the reading frame, compared to
            variant 4. The encoded isoform (12) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612664.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1223
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1223
                     /product="histone demethylase UTY isoform 12"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=136498
     Region          90..123
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..160
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          167..196
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          168..452
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..235
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..280
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          281..314
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          315..348
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..382
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          922..986
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          956..1064
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1223
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258257.1:1006..4677"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqngsdn wnggqslshh pvqqvyslcl
      421 tpqklqhleq lranrdnlnp aqkhqleqle sqfvlmqqmr hkevaqglhk sqssclsgpn
      481 eeqplfstgs aqyhqatstg ikkanehltl psnsvpqgda dshlschtat sggqqgimft
      541 keskpsknrs lvpetsrhtg dtsngcadvk glsnhvhqli adavsspnhg dspnlliadn
      601 pqlsalligk angnvgtgtc dkvnnihpav htktdhsvas spssaistat pspksteqrs
      661 insvtslnsp hsglhtvnge glgksqsstk vdlplashrs tsqilpsmsv sicpsstevl
      721 kacrnpgkng lsnscilldk cppprpptsp ypplpkdkln pptpsiylen krdaffpplh
      781 qfctnpknpv tvirglagal kldlglfstk tlveannehm vevrtqllqp adenwdptgt
      841 kkiwrcesnr shttiakyaq yqassfqesl reenekrtqh kdhsdnests sensgrrrkg
      901 pfktikfgtn idlsdnkkwk lqlheltklp afarvvsagn llthvghtil gmntvqlymk
      961 vpgsrtpghq ennnfcsvni nigpgdcewf vvpedywgvl ndfceknnln flmsswwpnl
     1021 edlyeanvpv yrfiqrpgdl vwinagtvhw vqavgwcnni awnvgpltac qyklaverye
     1081 wnklksvksp vpmvhlswnm arnikvsdpk lfemikycll kilkqyqtlr ealvaagkev
     1141 iwhgrtndep ahycsiceve vfnllfvtne sntqktyivh chdcarktsk slenfvvleq
     1201 ykmedliqvy dqftlalsls sss
//
LOCUS       NP_005383               1096 aa            linear   PRI 07-DEC-2025
DEFINITION  lysine-specific demethylase PHF2 [Homo sapiens].
ACCESSION   NP_005383
VERSION     NP_005383.3
DBSOURCE    REFSEQ: accession NM_005392.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1096)
  AUTHORS   Aguirre,S., Pappa,S., Serna-Pujol,N., Padilla,N., Iacobucci,S.,
            Nacht,A.S., Vicent,G.P., Jordan,A., de la Cruz,X. and
            Martinez-Balbas,M.A.
  TITLE     PHF2-mediated H3K9me balance orchestrates heterochromatin stability
            and neural progenitor proliferation
  JOURNAL   EMBO Rep 25 (8), 3486-3505 (2024)
   PUBMED   38890452
  REMARK    GeneRIF: PHF2-mediated H3K9me balance orchestrates heterochromatin
            stability and neural progenitor proliferation.
REFERENCE   2  (residues 1 to 1096)
  AUTHORS   Jeong,D.W., Park,J.W., Kim,K.S., Kim,J., Huh,J., Seo,J., Kim,Y.L.,
            Cho,J.Y., Lee,K.W., Fukuda,J. and Chun,Y.S.
  TITLE     Palmitoylation-driven PHF2 ubiquitination remodels lipid metabolism
            through the SREBP1c axis in hepatocellular carcinoma
  JOURNAL   Nat Commun 14 (1), 6370 (2023)
   PUBMED   37828054
  REMARK    GeneRIF: Palmitoylation-driven PHF2 ubiquitination remodels lipid
            metabolism through the SREBP1c axis in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1096)
  AUTHORS   Peng,L., Chen,J., Li,M. and Wang,R.
  TITLE     Circ_MBNL3 Restrains Hepatocellular Carcinoma Progression by
            Sponging miR-873-5p to Release PHF2
  JOURNAL   Biochem Genet 61 (3), 1015-1034 (2023)
   PUBMED   36380035
  REMARK    GeneRIF: Circ_MBNL3 Restrains Hepatocellular Carcinoma Progression
            by Sponging miR-873-5p to Release PHF2.
REFERENCE   4  (residues 1 to 1096)
  AUTHORS   Luo,P., Zhang,Y.D., He,F., Tong,C.J., Liu,K., Liu,H., Zhu,S.Z.,
            Luo,J.Z. and Yuan,B.
  TITLE     HIF-1alpha-mediated augmentation of miRNA-18b-5p facilitates
            proliferation and metastasis in osteosarcoma through attenuation
            PHF2
  JOURNAL   Sci Rep 12 (1), 10398 (2022)
   PUBMED   35729160
  REMARK    GeneRIF: HIF-1alpha-mediated augmentation of miRNA-18b-5p
            facilitates proliferation and metastasis in osteosarcoma through
            attenuation PHF2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1096)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1096)
  AUTHORS   Horton,J.R., Upadhyay,A.K., Hashimoto,H., Zhang,X. and Cheng,X.
  TITLE     Structural basis for human PHF2 Jumonji domain interaction with
            metal ions
  JOURNAL   J Mol Biol 406 (1), 1-8 (2011)
   PUBMED   21167174
  REMARK    GeneRIF: the crystal structures of PHF2 Jumonji domain in the
            absence and presence of additional exogenous metal ions were
            determined.
REFERENCE   7  (residues 1 to 1096)
  AUTHORS   Ohta,S., Bukowski-Wills,J.C., Sanchez-Pulido,L., Alves Fde,L.,
            Wood,L., Chen,Z.A., Platani,M., Fischer,L., Hudson,D.F.,
            Ponting,C.P., Fukagawa,T., Earnshaw,W.C. and Rappsilber,J.
  TITLE     The protein composition of mitotic chromosomes determined using
            multiclassifier combinatorial proteomics
  JOURNAL   Cell 142 (5), 810-821 (2010)
   PUBMED   20813266
REFERENCE   8  (residues 1 to 1096)
  AUTHORS   Wen,H., Li,J., Song,T., Lu,M., Kan,P.Y., Lee,M.G., Sha,B. and
            Shi,X.
  TITLE     Recognition of histone H3K4 trimethylation by the plant homeodomain
            of PHF2 modulates histone demethylation
  JOURNAL   J Biol Chem 285 (13), 9322-9326 (2010)
   PUBMED   20129925
REFERENCE   9  (residues 1 to 1096)
  AUTHORS   Sinha,S., Singh,R.K., Alam,N., Roy,A., Roychoudhury,S. and
            Panda,C.K.
  TITLE     Alterations in candidate genes PHF2, FANCC, PTCH1 and XPA at
            chromosomal 9q22.3 region: pathological significance in early- and
            late-onset breast carcinoma
  JOURNAL   Mol Cancer 7, 84 (2008)
   PUBMED   18990233
  REMARK    GeneRIF: Differential association of alterations in FANCC and PTCH1
            with that of PHF2, XPA and two breast cancer susceptibility genes
            (BRCA1/BRCA2) in the two age groups suggests differences in their
            molecular pathogenesis.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1096)
  AUTHORS   Hasenpusch-Theil,K., Chadwick,B.P., Theil,T., Heath,S.K.,
            Wilkinson,D.G. and Frischauf,A.M.
  TITLE     PHF2, a novel PHD finger gene located on human chromosome 9q22
  JOURNAL   Mamm Genome 10 (3), 294-298 (1999)
   PUBMED   10051327
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL353629.22, CB990295.1,
            AL834263.1, BQ716020.1 and AL359181.28.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 1, 2006 this sequence version replaced NP_005383.2.
            
            Summary: This gene encodes a protein which contains a zinc
            finger-like PHD (plant homeodomain) finger, distinct from other
            classes of zinc finger motifs, and a hydrophobic and highly
            conserved domain. The PHD finger shows the typical Cys4-His-Cys3
            arrangement. PHD finger genes are thought to belong to a diverse
            group of transcriptional regulators possibly affecting eukaryotic
            gene expression by influencing chromatin structure. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL834263.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359246.9/ ENSP00000352185.4
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1096
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.31"
     Protein         1..1096
                     /product="lysine-specific demethylase PHF2"
                     /note="jumonji C domain-containing histone demethylase 1E;
                     centromere protein 35; lysine demethylase 7C"
                     /calculated_mol_wt=120644
     Region          7..53
                     /region_name="PHD_PHF2_like"
                     /note="PHD finger found in PHF2, PHF8 and KDM7; cd15554"
                     /db_xref="CDD:277029"
     Site            order(7,14,19..22,29,45..46)
                     /site_type="other"
                     /note="histone H3 binding site [polypeptide binding]"
                     /db_xref="CDD:277029"
     Region          201..264
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          236..336
                     /region_name="cupin_RmlC-like"
                     /note="RmlC-like cupin superfamily; cl40423"
                     /db_xref="CDD:477354"
     Region          340..443
                     /region_name="JHD"
                     /note="Jumonji helical domain; pfam17811"
                     /db_xref="CDD:465515"
     Region          447..634
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75151.4)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75151.4)"
     Site            479
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O75151.4)"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75151.4)"
     Region          646..674
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75151.4)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75151.4)"
     Site            681
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75151.4)"
     Site            705
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75151.4)"
     Region          719..799
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75151.4)"
     Site            720
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTU0; propagated from
                     UniProtKB/Swiss-Prot (O75151.4)"
     Site            728
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTU0; propagated from
                     UniProtKB/Swiss-Prot (O75151.4)"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTU0; propagated from
                     UniProtKB/Swiss-Prot (O75151.4)"
     Site            733
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTU0; propagated from
                     UniProtKB/Swiss-Prot (O75151.4)"
     Site            734
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTU0; propagated from
                     UniProtKB/Swiss-Prot (O75151.4)"
     Site            738
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTU0; propagated from
                     UniProtKB/Swiss-Prot (O75151.4)"
     Region          817..846
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75151.4)"
     Region          877..1078
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75151.4)"
     Site            879
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTU0; propagated from
                     UniProtKB/Swiss-Prot (O75151.4)"
     Site            882
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75151.4)"
     Site            899
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75151.4)"
     Site            1056
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:21532585; propagated from
                     UniProtKB/Swiss-Prot (O75151.4)"
     CDS             1..1096
                     /gene="PHF2"
                     /gene_synonym="CENP-35; GRC5; JHDM1E; KDM7C"
                     /coded_by="NM_005392.4:191..3481"
                     /db_xref="CCDS:CCDS35069.1"
                     /db_xref="GeneID:5253"
                     /db_xref="HGNC:HGNC:8920"
                     /db_xref="MIM:604351"
ORIGIN      
        1 matvpvycvc rlpydvtrfm iecdackdwf hgscvgveee eapdidiyhc pncekthgks
       61 tlkkkrtwhk hgpgqapdvk pvqngsqlfi kelrsrtfps aedvvarvpg sqltlgymee
      121 hgftepilvp kkdglglavp aptfyvsdve nyvgpersvd vtdvtkqkdc kmklkefvdy
      181 yystnrkrvl nvtnlefsdt rmssfveppd ivkklswven ywpddallak pkvtkyclic
      241 vkdsytdfhi dsggasawyh vlkgektfyl irpasanisl yerwrsasnh semffadqvd
      301 kcykcivkqg qtlfipsgwi yatltpvdcl afaghflhsl svemqmraye verrlklgsl
      361 tqfpnfetac wymgkhllea fkgshksgkq lpphlvqgak ilngafrswt kkqalaehed
      421 elpehfkpsq likdlakeir lsenaskavr pevntvassd evcdgdreke eppspieatp
      481 pqsllekvsk kktpktvkmp kpskipkppk ppkpprppkt lklkdggkkk gkksresasp
      541 tipnldllea htkealtkme ppkkgkatks vlsvpnkdvv hmqndverle ireqtkskse
      601 akwkyknskp dsllkmeeeq kleksplagn kdnkfsfsfs nkkllgskal rpptspgvfg
      661 alqnfkedkp kpvrdeyeyv sddgelkide fpirrkknap krdlsflldk kavlptpvtk
      721 pkldsaayks ddssdegslh idtdtkpgrn arvkkesgss aagildllqa seevgaleyn
      781 pssqppasps tqeaiqgmls manlqasdsc lqttwgagqa kgsslaahga rkngggsgks
      841 agkrllkraa knsvdlddye eeqdhldacf kdsdyvypsl esdednpifk srskkrkgsd
      901 dapysptarv gpsvprqdrp vregtrvasi etglaaaaak lsqqeeqksk kkksakrklt
      961 pnttspstst sisagttsts ttpasttpas ttpaststas sqasqegssp epppeshsss
     1021 ladheytaag tftgaqagrt sqpmapgvfl tqrrpsassp nnntaakgkr tkkgmatakq
     1081 rlgkilkihr ngklll
//
LOCUS       NP_001245192            1290 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 18 [Homo sapiens].
ACCESSION   NP_001245192
VERSION     NP_001245192.1
DBSOURCE    REFSEQ: accession NM_001258263.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1290)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1290)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1290)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1290)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1290)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1290)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1290)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1290)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1290)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1290)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, EF612693.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (18) lacks three exons in the
            coding region, but maintains the reading frame, compared to variant
            4. The encoded isoform (18) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612693.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1290
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1290
                     /product="histone demethylase UTY isoform 18"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=142662
     Region          90..123
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..160
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          167..196
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          168..452
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..235
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..280
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          281..314
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          315..348
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..382
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          571..621
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          633..689
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          757..819
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            887
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24798337; propagated from
                     UniProtKB/Swiss-Prot (O14607.2)"
     Region          990..1026
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          1046..1110
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1080..1188
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1290
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258263.1:1006..4878"
                     /note="isoform 18 is encoded by transcript variant 18"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqngsdn wnggqslshh pvqqvyslcl
      421 tpqklqhleq lranrdnlnp aqkhqleqle sqfvlmqqmr hkevaqvrtt gihngaitds
      481 slptnsvsnr qphgaltrvs svsqpgvrpa cvekllssga fsagcipcgt skilgstdti
      541 llgsnciags esngnvpylq qnthtlphnh tdlnssteep wrkqlsnsaq glhksqsscl
      601 sgpneeqplf stgsaqyhqa tstgikkane hltlpsnsvp qgdadshlsc htatsggqqg
      661 imftkeskps knrslvpets rhtgdtsngc advkglsnhv hqliadavss pnhgdspnll
      721 iadnpqlsal ligkangnvg tgtcdkvnni hpavhtktdh svasspssai statpspkst
      781 eqrsinsvts lnsphsglht vngeglgksq sstkvdlpla shrstsqilp smsvsicpss
      841 tevlkacrnp gknglsnsci lldkcppprp ptspypplpk dklnpptpsi ylenkrdaff
      901 pplhqfctnp knpvtvirgl agalkldlgl fstktlvean nehmvevrtq llqpadenwd
      961 ptgtkkiwrc esnrshttia kyaqyqassf qeslreenek rtqhkdhsdn estssensgr
     1021 rrkgpfktik fgtnidlsdn kkwklqlhel tklpafarvv sagnllthvg htilgmntvq
     1081 lymkvpgsrt pghqennnfc svninigpgd cewfvvpedy wgvlndfcek nnlnflmssw
     1141 wpnledlyea nvpvyrfiqr pgdlvwinag tvhwvqavgw cnniawnvgp ltacqyklav
     1201 eryewnklks vkspvpmvhl swnmarnikv sdpklfemik ycllkilkqy qtlrealvaa
     1261 gkeviwhgrt ndepahycsi cealslssss
//
LOCUS       NP_942567                161 aa            linear   PRI 07-DEC-2025
DEFINITION  probable RNA/DNA demethylase ALKBH6 isoform 1 [Homo sapiens].
ACCESSION   NP_942567
VERSION     NP_942567.1
DBSOURCE    REFSEQ: accession NM_198867.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Das,S., Rankawat,S., Shaji,U.P., Tuti,N., Shahnaz,N., Ray,S. and
            Anindya,R.
  TITLE     Identification of ALKBH6 as a nucleotide demethylase with a
            distinct substrate preference
  JOURNAL   J Biol Chem 301 (10), 110638 (2025)
   PUBMED   40885392
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Das,S., Shahnaz,N., Keerthana,C., Ranjan,S., Seenivasan,G.,
            Tuti,N., Shaji,U.P., Meur,G. and Anindya,R.
  TITLE     Functional and comparative analysis of the
            FeII/2-oxoglutarate-dependent dioxygenases without using any
            substrate
  JOURNAL   Biol Methods Protoc 10 (1), bpae096 (2024)
   PUBMED   39845104
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Ma,L., Lu,H., Tian,Z., Yang,M., Ma,J., Shang,G., Liu,Y., Xie,M.,
            Wang,G., Wu,W., Zhang,Z., Dai,S. and Chen,Z.
  TITLE     Structural insights into the interactions and epigenetic functions
            of human nucleic acid repair protein ALKBH6
  JOURNAL   J Biol Chem 298 (3), 101671 (2022)
   PUBMED   35120926
  REMARK    GeneRIF: Structural insights into the interactions and epigenetic
            functions of human nucleic acid repair protein ALKBH6.
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Kernstock,S., Davydova,E., Jakobsson,M., Moen,A., Pettersen,S.,
            Maelandsmo,G.M., Egge-Jacobsen,W. and Falnes,P.O.
  TITLE     Lysine methylation of VCP by a member of a novel human protein
            methyltransferase family
  JOURNAL   Nat Commun 3, 1038 (2012)
   PUBMED   22948820
REFERENCE   5  (residues 1 to 161)
  AUTHORS   Tsujikawa,K., Koike,K., Kitae,K., Shinkawa,A., Arima,H., Suzuki,T.,
            Tsuchiya,M., Makino,Y., Furukawa,T., Konishi,N. and Yamamoto,H.
  TITLE     Expression and sub-cellular localization of human ABH family
            molecules
  JOURNAL   J Cell Mol Med 11 (5), 1105-1116 (2007)
   PUBMED   17979886
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM713594.1 and BC007601.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK304805.1, CR983526.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..161
                     /product="probable RNA/DNA demethylase ALKBH6 isoform 1"
                     /EC_number="3.4.22.17"
                     /note="alkylated DNA repair protein alkB homolog 6;
                     probable alpha-ketoglutarate-dependent dioxygenase ABH6;
                     alkB, alkylation repair homolog 6;
                     alpha-ketoglutarate-dependent dioxygenase alkB homolog 6;
                     probable nucleic acid dioxygenase ALKBH6; probable RNA/DNA
                     demethylase ALKBH6"
                     /calculated_mol_wt=17805
     Region          51..>143
                     /region_name="2OG-FeII_Oxy"
                     /note="2OG-Fe(II) oxygenase superfamily; cl21496"
                     /db_xref="CDD:473886"
     CDS             1..161
                     /gene="ALKBH6"
                     /gene_synonym="ABH6"
                     /coded_by="NM_198867.1:7..492"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:84964"
                     /db_xref="HGNC:HGNC:28243"
                     /db_xref="MIM:613304"
ORIGIN      
        1 magrgmgmln leiggdaggr igckelvlme eqdarvpale pfrveqappv iyyvpdfisk
       61 eeeeyllrqv fnapkpkwtq lsgrklqnwg glphprgmvp erlppwlqry vdkvsnlslf
      121 gglpanhvlv nqylpgegim hhqpglphra gllraaaarg r
//
LOCUS       NP_001245189            1377 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 15 [Homo sapiens].
ACCESSION   NP_001245189
VERSION     NP_001245189.1
DBSOURCE    REFSEQ: accession NM_001258260.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1377)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1377)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1377)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1377)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1377)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1377)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1377)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1377)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1377)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1377)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, EF612680.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (15) has multiple differences in
            the coding region, but maintains the reading frame, compared to
            variant 4. The encoded isoform (15) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612680.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1377
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1377
                     /product="histone demethylase UTY isoform 15"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=152614
     Region          <72..158
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..401
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1076..1140
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1110..1218
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1377
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258260.1:1006..5139"
                     /note="isoform 15 is encoded by transcript variant 15"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqqslsl hmitssqveg lsspakkkrt
      421 ssptkngsdn wnggqslshh pvqqvyslcl tpqklqhleq lranrdnlnp aqkhqleqle
      481 sqfvlmqqmr hkevaqvrtt gihngaitds slptnsvsnr qphgaltrvs svsqpgvrpa
      541 cvekllssga fsagcipcgt skilgstdti llgsnciags esngnvpylq qnthtlphnh
      601 tdlnssteep wrkqlsnsaq glhksqsscl sgpneeqplf stgsaqyhqa tstgikkane
      661 hltlpsnsvp qgdadshlsc htatsggqqg imftkeskps knrslvpets rhtgdtsngc
      721 advkglsnhv hqliadavss pnhgdspnll iadnpqlsal ligkangnvg tgtcdkvnni
      781 hpavhtktdh svasspssai statpspkst eqrsinsvts lnsphsglht vngeglgksq
      841 sstkvdlpla shrstsqilp smsvsicpss tevlkacrnp gknglsnsci lldkcppprp
      901 ptspypplpk dklnpptpsi ylenkrdaff pplhqfctnp knpvtvirgl agalkldlgl
      961 fstktlvean nehmvevrtq llqpadenwd ptgtkkiwrc esnrshttia kyaqyqassf
     1021 qeslreenek rtqhkdhsdn estssensgr rrkgpfktik fgtnidlsdn kkwklqlhel
     1081 tklpafarvv sagnllthvg htilgmntvq lymkvpgsrt pghqennnfc svninigpgd
     1141 cewfvvpedy wgvlndfcek nnlnflmssw wpnledlyea nvpvyrfiqr pgdlvwinag
     1201 tvhwvqavgw cnniawnvgp ltacqyklav eryewnklks vkspvpmvhl swnmarnikv
     1261 sdpklfemik ycllkilkqy qtlrealvaa gkeviwhgrt ndepahycsi cevevfnllf
     1321 vtnesntqkt yivhchdcar ktskslenfv vleqykmedl iqvydqftla lslssss
//
LOCUS       NP_001387124            1109 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 38 [Homo sapiens].
ACCESSION   NP_001387124 XP_024308262
VERSION     NP_001387124.1
DBSOURCE    REFSEQ: accession NM_001400195.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1109)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1109)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1109)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1109)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1109)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1109)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1109)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1109)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1109)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1109)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2 and AC010877.3.
            
            On Jan 20, 2022 this sequence version replaced XP_024308262.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ345543.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1109
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1109
                     /product="histone demethylase UTY isoform 38"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=121140
     Region          <72..158
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..401
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..1109
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001400195.1:369..3698"
                     /note="isoform 38 is encoded by transcript variant 90"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqqslsl hmitssqveg lsspakkkrt
      421 ssptkngsdn wnggqslshh pvqqvyslcl tpqklqhleq lranrdnlnp aqkhqleqle
      481 sqfvlmqqmr hkevaqvrtt gihngaitds slptnsvsnr qphgaltrvs svsqpgvrpa
      541 cvekllssga fsagcipcgt skilgstdti llgsnciags esngnvpylq qnthtlphnh
      601 tdlnssteep wrkqlsnsaq glhksqsscl sgpneeqplf stgsaqyhqa tstgikkane
      661 hltlpsnsvp qgdadshlsc htatsggqqg imftkeskps knrslvpets rhtgdtsngc
      721 advkglsnhv hqliadavss pnhgdspnll iadnpqlsal ligkangnvg tgtcdkvnni
      781 hpavhtktdh svasspssai statpspkst eqrsinsvts lnsphsglht vngeglgksq
      841 sstkvdlpla shrstsqilp smsvsicpss tevlkacrnp gknglsnsci lldkcppprp
      901 ptspypplpk dklnpptpsi ylenkrdaff pplhqfctnp knpvtvirgl agalkldlgl
      961 fstktlvean nehmvevrtq llqpadenwd ptgtkkiwrc esnrshttia kyaqyqassf
     1021 qeslragmqw cdlsslqppp pgfkrfshls lpnswnyrhl pscptnfcif vetgfhhvgq
     1081 aclelltsgg llasasqsag itgvshhar
//
LOCUS       NP_001245181            1392 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 7 [Homo sapiens].
ACCESSION   NP_001245181
VERSION     NP_001245181.1
DBSOURCE    REFSEQ: accession NM_001258252.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1392)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1392)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1392)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1392)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1392)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1392)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1392)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1392)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1392)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1392)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, DQ140389.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (7) lacks an exon in the coding
            region, but maintains the reading frame, compared to variant 4. The
            encoded isoform (7) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ140389.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1392
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1392
                     /product="histone demethylase UTY isoform 7"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=154307
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..440
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1091..1155
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1125..1233
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1392
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258252.1:1006..5184"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS59184.1"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq ngsdnwnggq slshhpvqqv yslcltpqkl qhleqlranr
      481 dnlnpaqkhq leqlesqfvl mqqmrhkeva qvrttgihng aitdsslptn svsnrqphga
      541 ltrvssvsqp gvrpacvekl lssgafsagc ipcgtskilg stdtillgsn ciagsesngn
      601 vpylqqntht lphnhtdlns steepwrkql snsaqglhks qssclsgpne eqplfstgsa
      661 qyhqatstgi kkanehltlp snsvpqgdad shlschtats ggqqgimftk eskpsknrsl
      721 vpetsrhtgd tsngcadvkg lsnhvhqlia davsspnhgd spnlliadnp qlsalligka
      781 ngnvgtgtcd kvnnihpavh tktdhsvass pssaistatp spksteqrsi nsvtslnsph
      841 sglhtvngeg lgksqsstkv dlplashrst sqilpsmsvs icpsstevlk acrnpgkngl
      901 snscilldkc ppprpptspy pplpkdklnp ptpsiylenk rdaffpplhq fctnpknpvt
      961 virglagalk ldlglfstkt lveannehmv evrtqllqpa denwdptgtk kiwrcesnrs
     1021 httiakyaqy qassfqeslr eenekrtqhk dhsdnestss ensgrrrkgp fktikfgtni
     1081 dlsdnkkwkl qlheltklpa farvvsagnl lthvghtilg mntvqlymkv pgsrtpghqe
     1141 nnnfcsvnin igpgdcewfv vpedywgvln dfceknnlnf lmsswwpnle dlyeanvpvy
     1201 rfiqrpgdlv winagtvhwv qavgwcnnia wnvgpltacq yklaveryew nklksvkspv
     1261 pmvhlswnma rnikvsdpkl femikycllk ilkqyqtlre alvaagkevi whgrtndepa
     1321 hycsicevev fnllfvtnes ntqktyivhc hdcarktsks lenfvvleqy kmedliqvyd
     1381 qftlalslss ss
//
LOCUS       NP_001245196            1342 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 22 [Homo sapiens].
ACCESSION   NP_001245196
VERSION     NP_001245196.1
DBSOURCE    REFSEQ: accession NM_001258267.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1342)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1342)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1342)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1342)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1342)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1342)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1342)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1342)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1342)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1342)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, DQ341386.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (22) has multiple differences in
            the coding region, one of which results in a frameshift, compared
            to variant 4. The encoded isoform (22) is shorter and has a
            distinct C-terminus, compared to isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ341386.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1342
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1342
                     /product="histone demethylase UTY isoform 22"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=149008
     Region          90..123
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..160
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          167..196
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          168..452
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..235
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..280
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          281..314
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          315..348
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..382
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          571..621
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          633..689
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          757..819
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            887
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24798337; propagated from
                     UniProtKB/Swiss-Prot (O14607.2)"
     Region          990..1026
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          1046..1110
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1080..1188
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1342
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258267.1:1006..5034"
                     /note="isoform 22 is encoded by transcript variant 22"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqngsdn wnggqslshh pvqqvyslcl
      421 tpqklqhleq lranrdnlnp aqkhqleqle sqfvlmqqmr hkevaqvrtt gihngaitds
      481 slptnsvsnr qphgaltrvs svsqpgvrpa cvekllssga fsagcipcgt skilgstdti
      541 llgsnciags esngnvpylq qnthtlphnh tdlnssteep wrkqlsnsaq glhksqsscl
      601 sgpneeqplf stgsaqyhqa tstgikkane hltlpsnsvp qgdadshlsc htatsggqqg
      661 imftkeskps knrslvpets rhtgdtsngc advkglsnhv hqliadavss pnhgdspnll
      721 iadnpqlsal ligkangnvg tgtcdkvnni hpavhtktdh svasspssai statpspkst
      781 eqrsinsvts lnsphsglht vngeglgksq sstkvdlpla shrstsqilp smsvsicpss
      841 tevlkacrnp gknglsnsci lldkcppprp ptspypplpk dklnpptpsi ylenkrdaff
      901 pplhqfctnp knpvtvirgl agalkldlgl fstktlvean nehmvevrtq llqpadenwd
      961 ptgtkkiwrc esnrshttia kyaqyqassf qeslreenek rtqhkdhsdn estssensgr
     1021 rrkgpfktik fgtnidlsdn kkwklqlhel tklpafarvv sagnllthvg htilgmntvq
     1081 lymkvpgsrt pghqennnfc svninigpgd cewfvvpedy wgvlndfcek nnlnflmssw
     1141 wpnledlyea nvpvyrfiqr pgdlvwinag tvhwvqavgw cnniawnvgp ltacqyklav
     1201 eryewnklks vkspvpmvhl swnmarnikv sdpklfemik ycllkilkqy qtlrealvaa
     1261 gkeviwhgrt ndepahycsi cevevfnllf vtnesntqkt yivhchdcar ktskslenfv
     1321 vleqykmedl iqvydqftlv sh
//
LOCUS       NP_001093254             694 aa            linear   PRI 07-DEC-2025
DEFINITION  F-box/LRR-repeat protein 19 isoform 1 [Homo sapiens].
ACCESSION   NP_001093254
VERSION     NP_001093254.2
DBSOURCE    REFSEQ: accession NM_001099784.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Dong,H., Huang,C. and Huang,J.
  TITLE     FBXL19-AS1 promotes the progression of nasopharyngeal carcinoma by
            acting as a competing endogenous RNA to sponge miR-431 and
            upregulate PBOV1
  JOURNAL   Mol Med Rep 24 (3) (2021)
   PUBMED   34278444
  REMARK    GeneRIF: FBXL19AS1 promotes the progression of nasopharyngeal
            carcinoma by acting as a competing endogenous RNA to sponge miR431
            and upregulate PBOV1.
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 694)
  AUTHORS   Wang,L., Zhang,X., Liu,Y. and Xu,S.
  TITLE     Long noncoding RNA FBXL19-AS1 induces tumor growth and metastasis
            by sponging miR-203a-3p in lung adenocarcinoma
  JOURNAL   J Cell Physiol 235 (4), 3612-3625 (2020)
   PUBMED   31566718
  REMARK    GeneRIF: Long noncoding RNA FBXL19-AS1 induces tumor growth and
            metastasis by sponging miR-203a-3p in lung adenocarcinoma.
REFERENCE   5  (residues 1 to 694)
  AUTHORS   Xu,C., Liu,K., Lei,M., Yang,A., Li,Y., Hughes,T.R. and Min,J.
  TITLE     DNA Sequence Recognition of Human CXXC Domains and Their Structural
            Determinants
  JOURNAL   Structure 26 (1), 85-95 (2018)
   PUBMED   29276034
REFERENCE   6  (residues 1 to 694)
  AUTHORS   Chandran,V.
  TITLE     The genetics of psoriasis and psoriatic arthritis
  JOURNAL   Clin Rev Allergy Immunol 44 (2), 149-156 (2013)
   PUBMED   22274791
  REMARK    Review article
REFERENCE   7  (residues 1 to 694)
  AUTHORS   Stuart,P.E., Nair,R.P., Ellinghaus,E., Ding,J., Tejasvi,T.,
            Gudjonsson,J.E., Li,Y., Weidinger,S., Eberlein,B., Gieger,C.,
            Wichmann,H.E., Kunz,M., Ike,R., Krueger,G.G., Bowcock,A.M.,
            Mrowietz,U., Lim,H.W., Voorhees,J.J., Abecasis,G.R.,
            Weichenthal,M., Franke,A., Rahman,P., Gladman,D.D. and Elder,J.T.
  TITLE     Genome-wide association analysis identifies three psoriasis
            susceptibility loci
  JOURNAL   Nat Genet 42 (11), 1000-1004 (2010)
   PUBMED   20953189
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 694)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   9  (residues 1 to 694)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of FBXL19 gene in silico
  JOURNAL   Int J Mol Med 14 (6), 1109-1114 (2004)
   PUBMED   15547684
REFERENCE   10 (residues 1 to 694)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC401737.1, CX781342.1,
            AK098777.1 and BC059173.1.
            
            On Sep 13, 2007 this sequence version replaced NP_001093254.1.
            
            Summary: This gene encodes a member of the Skp1-Cullin-F-box family
            of E3 ubiquitin ligases. The encoded protein is reported to bind to
            the transmembrane receptor interleukin 1 receptor-like 1 and
            regulate its ubiquitination and degradation. This protein has been
            linked to the regulation of pulmonary inflammation and psoriasis.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302669.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2149178
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..694
                     /product="F-box/LRR-repeat protein 19 isoform 1"
                     /note="jumonji C domain-containing histone demethylase 1C;
                     F-box/LRR-repeat protein 19; jumonji C domain-containing
                     1C"
                     /calculated_mol_wt=75576
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCT2.3)"
     Region          <50..77
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          87..148
                     /region_name="PHD_FXL19"
                     /note="PHD finger found in F-box and leucine-rich repeat
                     protein 19 (FBXL19); cd15645"
                     /db_xref="CDD:277115"
     Site            order(87,110..114,118,143)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277115"
     Region          150..420
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCT2.3)"
     Region          421..463
                     /region_name="F-box_JHDM"
                     /note="F-box domain found in the JmjC domain-containing
                     histone demethylation protein (JHDM) family; cd22122"
                     /db_xref="CDD:438894"
     Site            order(424..425,427..429,431..432,434..436,438..439,
                     442..443,445..447,451)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438894"
     Region          461..485
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          466..665
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          486..508
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          492..517
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCT2.3)"
     Region          510..533
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          518..541
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCT2.3)"
     Region          534..573
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          574..598
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          581..606
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCT2.3)"
     Region          599..623
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          607..636
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCT2.3)"
     Region          629..653
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          637..661
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCT2.3)"
     Region          654..686
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          662..694
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PCT2.3)"
     CDS             1..694
                     /gene="FBXL19"
                     /gene_synonym="CXXC11; Fbl19; JHDM1C"
                     /coded_by="NM_001099784.3:159..2243"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45465.1"
                     /db_xref="GeneID:54620"
                     /db_xref="HGNC:HGNC:25300"
                     /db_xref="MIM:609085"
ORIGIN      
        1 mgmkvpgkge sgpsalltpp mssssrgpga garrrrtrcr rcracvrtec gdchfcrdmk
       61 kfggpgrmkq scllrqctap vlphtavcll cgeagkedtv egeeekfgls lmecticnei
      121 vhpgclkmgk aegvinaeip ncwecprctq egrtskdsge gpgrrradng eegaslgsgw
      181 klteepplpp ppprrkgplp agpppedvpg ppkrkereag nepptprkkv kggrerhlkk
      241 vggdacllrg sdpggpgllp prvlnpsqaf sschpglppe nwekpkppla saegpavpsp
      301 spqreklerf krmcqllerv pdtsssssds dsdsdssgts lsedeapgea rngrrpargs
      361 sgekenrggr ravrpgsggp llswplgpap pprppqlerh vvrppprspe pdtlplaags
      421 dhplpraawl rvfqhlgpre lcicmrvcrt wsrwcydkrl wprmdlsrrk sltppmlsgv
      481 vrrqpraldl swtgvskkql mwllnrlqgl qelvlsgcsw lsvsalgsap lpalrlldlr
      541 wiedvkdsql relllpppdt kpgqtesrgr lqgvaelrla gleltdaslr lllrhapqls
      601 aldlshcahv gdpsvhllta ptsplretlv hlnlagchrl tdhclplfrr cprlrrldlr
      661 scrqlspeac arlaaagppg pfrcpeekll lkds
//
LOCUS       NP_001387114            1154 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 34 [Homo sapiens].
ACCESSION   NP_001387114 XP_011529764
VERSION     NP_001387114.1
DBSOURCE    REFSEQ: accession NM_001400185.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1154)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1154)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1154)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1154)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1154)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1154)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1154)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1154)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1154)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1154)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2 and AC010877.3.
            
            On Jan 20, 2022 this sequence version replaced XP_011529764.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ345544.1, SRR18074969.360116.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1154
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1154
                     /product="histone demethylase UTY isoform 34"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=126029
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..191
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..441
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..1154
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001400185.1:369..3833"
                     /note="isoform 34 is encoded by transcript variant 86"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq qslslhmits sqveglsspa kkkrtssptk ngsdnwnggq
      481 slshhpvqqv yslcltpqkl qhleqlranr dnlnpaqkhq leqlesqfvl mqqmrhkeva
      541 qvrttgihng aitdsslptn svsnrqphga ltrvssvsqp gvrpacvekl lssgafsagc
      601 ipcgtskilg stdtillgsn ciagsesngn vpylqqntht lphnhtdlns steepwrkql
      661 snsaqglhks qssclsgpne eqplfstgsa qyhqatstgi kkanehltlp snsvpqgdad
      721 shlschtats ggqqgimftk eskpsknrsl vpetsrhtgd tsngcadvkg lsnhvhqlia
      781 davsspnhgd spnlliadnp qlsalligka ngnvgtgtcd kvnnihpavh tktdhsvass
      841 pssaistatp spksteqrsi nsvtslnsph sglhtvngeg lgksqsstkv dlplashrst
      901 sqilpsmsvs icpsstevlk acrnpgkngl snscilldkc ppprpptspy pplpkdklnp
      961 ptpsiylenk rdaffpplhq fctnpknpvt virglagalk ldlglfstkt lveannehmv
     1021 evrtqllqpa denwdptgtk kiwrcesnrs httiakyaqy qassfqeslr agmqwcdlss
     1081 lqppppgfkr fshlslpnsw nyrhlpscpt nfcifvetgf hhvgqaclel ltsggllasa
     1141 sqsagitgvs hhar
//
LOCUS       NP_001245183            1211 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 9 [Homo sapiens].
ACCESSION   NP_001245183
VERSION     NP_001245183.1
DBSOURCE    REFSEQ: accession NM_001258254.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1211)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1211)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1211)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1211)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1211)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1211)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1211)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1211)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1211)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1211)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, DQ140390.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (9) has multiple differences in
            the coding region, but maintains the reading frame, compared to
            variant 4. The encoded isoform (9) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ140390.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1211
                     /product="histone demethylase UTY isoform 9"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=134632
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..440
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          967..1031
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1001..1109
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1211
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258254.1:1006..4641"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS59185.1"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq ngsdnwnggq slshhpvqqv yslcltpqkl qhleqlranr
      481 dnlnpaqkhq leqlesqfvl mqqmrhkeva qglhksqssc lsgpneeqpl fstgsaqyhq
      541 atstgikkan ehltlpsnsv pqgdadshls chtatsggqq gimftkeskp sknrslvpet
      601 srhtgdtsng cadvkglsnh vhqliadavs spnhgdspnl liadnpqlsa lligkangnv
      661 gtgtcdkvnn ihpavhtktd hsvasspssa istatpspks teqrsinsvt slnsphsglh
      721 tvngeglgks qsstkvdlpl ashrstsqil psmsvsicps stevlkacrn pgknglsnsc
      781 illdkcpppr pptspypplp kdklnpptps iylenkrdaf fpplhqfctn pknpvtvirg
      841 lagalkldlg lfstktlvea nnehmvevrt qllqpadenw dptgtkkiwr cesnrshtti
      901 akyaqyqass fqeslreene krtqhkdhsd nestssensg rrrkgpfkti kfgtnidlsd
      961 nkkwklqlhe ltklpafarv vsagnllthv ghtilgmntv qlymkvpgsr tpghqennnf
     1021 csvninigpg dcewfvvped ywgvlndfce knnlnflmss wwpnledlye anvpvyrfiq
     1081 rpgdlvwina gtvhwvqavg wcnniawnvg pltacqykla veryewnklk svkspvpmvh
     1141 lswnmarnik vsdpklfemi kycllkilkq yqtlrealva agkeviwhgr tndepahycs
     1201 icealslsss s
//
LOCUS       NP_001372984             238 aa            linear   PRI 07-DEC-2025
DEFINITION  probable RNA/DNA demethylase ALKBH6 isoform 3 [Homo sapiens].
ACCESSION   NP_001372984 XP_005259414
VERSION     NP_001372984.1
DBSOURCE    REFSEQ: accession NM_001386055.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Das,S., Rankawat,S., Shaji,U.P., Tuti,N., Shahnaz,N., Ray,S. and
            Anindya,R.
  TITLE     Identification of ALKBH6 as a nucleotide demethylase with a
            distinct substrate preference
  JOURNAL   J Biol Chem 301 (10), 110638 (2025)
   PUBMED   40885392
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Das,S., Shahnaz,N., Keerthana,C., Ranjan,S., Seenivasan,G.,
            Tuti,N., Shaji,U.P., Meur,G. and Anindya,R.
  TITLE     Functional and comparative analysis of the
            FeII/2-oxoglutarate-dependent dioxygenases without using any
            substrate
  JOURNAL   Biol Methods Protoc 10 (1), bpae096 (2024)
   PUBMED   39845104
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Ma,L., Lu,H., Tian,Z., Yang,M., Ma,J., Shang,G., Liu,Y., Xie,M.,
            Wang,G., Wu,W., Zhang,Z., Dai,S. and Chen,Z.
  TITLE     Structural insights into the interactions and epigenetic functions
            of human nucleic acid repair protein ALKBH6
  JOURNAL   J Biol Chem 298 (3), 101671 (2022)
   PUBMED   35120926
  REMARK    GeneRIF: Structural insights into the interactions and epigenetic
            functions of human nucleic acid repair protein ALKBH6.
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Kernstock,S., Davydova,E., Jakobsson,M., Moen,A., Pettersen,S.,
            Maelandsmo,G.M., Egge-Jacobsen,W. and Falnes,P.O.
  TITLE     Lysine methylation of VCP by a member of a novel human protein
            methyltransferase family
  JOURNAL   Nat Commun 3, 1038 (2012)
   PUBMED   22948820
REFERENCE   5  (residues 1 to 238)
  AUTHORS   Tsujikawa,K., Koike,K., Kitae,K., Shinkawa,A., Arima,H., Suzuki,T.,
            Tsuchiya,M., Makino,Y., Furukawa,T., Konishi,N. and Yamamoto,H.
  TITLE     Expression and sub-cellular localization of human ABH family
            molecules
  JOURNAL   J Cell Mol Med 11 (5), 1105-1116 (2007)
   PUBMED   17979886
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC002116.1 and BX366961.2.
            
            On Aug 5, 2020 this sequence version replaced XP_005259414.1.
            
            Transcript Variant: Variants 2, 3, and 5 encode the same isoform
            (3).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX366961.2, SRR1163658.475480.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398, SAMEA2155751
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..238
                     /product="probable RNA/DNA demethylase ALKBH6 isoform 3"
                     /EC_number="3.4.22.17"
                     /note="alkylated DNA repair protein alkB homolog 6;
                     probable alpha-ketoglutarate-dependent dioxygenase ABH6;
                     alkB, alkylation repair homolog 6;
                     alpha-ketoglutarate-dependent dioxygenase alkB homolog 6;
                     probable nucleic acid dioxygenase ALKBH6; probable RNA/DNA
                     demethylase ALKBH6"
                     /calculated_mol_wt=26352
     Region          23..224
                     /region_name="2OG-FeII_Oxy"
                     /note="2OG-Fe(II) oxygenase superfamily; cl21496"
                     /db_xref="CDD:473886"
     Region          138..161
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KRA9.2)"
     CDS             1..238
                     /gene="ALKBH6"
                     /gene_synonym="ABH6"
                     /coded_by="NM_001386055.1:726..1442"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS74342.1"
                     /db_xref="GeneID:84964"
                     /db_xref="HGNC:HGNC:28243"
                     /db_xref="MIM:613304"
ORIGIN      
        1 meeqdarvpa lepfrveqap pviyyvpdfi skeeeeyllr qvfnapkpkw tqlsgrklqn
       61 wgglphprgm vperlppwlq ryvdkvsnls lfgglpanhv lvnqylpgeg imphedgply
      121 yptvstislg shtvldfyep rrpedddpte qprppprptt sllleprsll vlrgpaytrl
      181 lhgiaaarvd aldaassppn aaacpsarpg aclvrgtrvs ltirrvprvl raglllgk
//
LOCUS       NP_872601               1079 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 1 [Homo sapiens].
ACCESSION   NP_872601
VERSION     NP_872601.1
DBSOURCE    REFSEQ: accession NM_182660.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1079)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1079)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1079)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1079)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1079)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1079)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1079)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF000996.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (1) has multiple differences
            compared to variant 4, including the use of an alternate 3' UTR.
            The encoded isoform (1) is shorter and has a distinct C-terminus,
            compared to isoform 4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF000996.1, AK292858.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1079
                     /product="histone demethylase UTY isoform 1"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=117943
     Region          90..123
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..160
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          167..196
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          168..452
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..235
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..280
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          281..314
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          315..348
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..382
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          571..621
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          633..689
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          757..819
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            887
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24798337; propagated from
                     UniProtKB/Swiss-Prot (O14607.2)"
     CDS             1..1079
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_182660.1:1006..4245"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14785.1"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqngsdn wnggqslshh pvqqvyslcl
      421 tpqklqhleq lranrdnlnp aqkhqleqle sqfvlmqqmr hkevaqvrtt gihngaitds
      481 slptnsvsnr qphgaltrvs svsqpgvrpa cvekllssga fsagcipcgt skilgstdti
      541 llgsnciags esngnvpylq qnthtlphnh tdlnssteep wrkqlsnsaq glhksqsscl
      601 sgpneeqplf stgsaqyhqa tstgikkane hltlpsnsvp qgdadshlsc htatsggqqg
      661 imftkeskps knrslvpets rhtgdtsngc advkglsnhv hqliadavss pnhgdspnll
      721 iadnpqlsal ligkangnvg tgtcdkvnni hpavhtktdh svasspssai statpspkst
      781 eqrsinsvts lnsphsglht vngeglgksq sstkvdlpla shrstsqilp smsvsicpss
      841 tevlkacrnp gknglsnsci lldkcppprp ptspypplpk dklnpptpsi ylenkrdaff
      901 pplhqfctnp knpvtvirgl agalkldlgl fstktlvean nehmvevrtq llqpadenwd
      961 ptgtkkiwrc esnrshttia kyaqyqassf qeslragmqw cdlsslqppp pgfkrfshls
     1021 lpnswnyrhl pscptnfcif vetgfhhvgq aclelltsgg llasasqsag itgvshhar
//
LOCUS       NP_001406735            1501 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 40 [Homo sapiens].
ACCESSION   NP_001406735 XP_011529753 XP_054184316
VERSION     NP_001406735.1
DBSOURCE    REFSEQ: accession NM_001419806.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1501)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1501)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1501)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1501)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1501)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1501)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1501)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1501)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1501)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1501)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, AC010877.3 and
            AC244214.2.
            
            On or before Apr 19, 2023 this sequence version replaced
            XP_011529753.1, XP_054184316.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.145505.1,
                                           SRR14038196.3367906.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1501
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1501
                     /product="histone demethylase UTY isoform 40"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=166755
     Region          90..123
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..160
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          167..196
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          168..452
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..235
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..280
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          281..314
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          315..348
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..382
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          649..705
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          773..835
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            903
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24798337; propagated from
                     UniProtKB/Swiss-Prot (O14607.2)"
     Region          1006..1042
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          1062..1126
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1096..1204
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1501
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001419806.1:369..4874"
                     /note="isoform 40 is encoded by transcript variant 94"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqngsdn wnggqslshh pvqqvyslcl
      421 tpqklqhleq lranrdnlnp aqkhqleqle sqfvlmqqmr hkevaqvrtt gihngaitds
      481 slptnsvsnr qphgaltrvs svsqpgvrpa cvekllssga fsagcipcgt skilgstdti
      541 llgsnciags esngnvpylq qnthtlphnh tdlnssteep wrkqlsnsaq aylghltgfi
      601 qdncnkglhk sqssclsgpn eeqplfstgs aqyhqatstg ikkanehltl psnsvpqgda
      661 dshlschtat sggqqgimft keskpsknrs lvpetsrhtg dtsngcadvk glsnhvhqli
      721 adavsspnhg dspnlliadn pqlsalligk angnvgtgtc dkvnnihpav htktdhsvas
      781 spssaistat pspksteqrs insvtslnsp hsglhtvnge glgksqsstk vdlplashrs
      841 tsqilpsmsv sicpsstevl kacrnpgkng lsnscilldk cppprpptsp ypplpkdkln
      901 pptpsiylen krdaffpplh qfctnpknpv tvirglagal kldlglfstk tlveannehm
      961 vevrtqllqp adenwdptgt kkiwrcesnr shttiakyaq yqassfqesl reenekrtqh
     1021 kdhsdnests sensgrrrkg pfktikfgtn idlsdnkkwk lqlheltklp afarvvsagn
     1081 llthvghtil gmntvqlymk vpgsrtpghq ennnfcsvni nigpgdcewf vvpedywgvl
     1141 ndfceknnln flmsswwpnl edlyeanvpv yrfiqrpgdl vwinagtvhw vqavgwcnni
     1201 awnvgpltac qyklaverye wnklksvksp vpmvhlswnm arnikvsdpk lfemikycll
     1261 kilkqyqtlr ealvaagkev iwhgrtndep ahycsiceve vfnllfvtne sntqktyivh
     1321 chdcarktsk slenfvvleq ykmedliqvy dqftlaspwp pmdqsaftss llrpikalgs
     1381 graeqtsgdq lqkgathsra ssllraaemt rrpasreelp dpglfchsik llfvlfsfhl
     1441 stflilpcqr rrtwelldgg aescktnran tpiahylvse eerravalqr vqtwellepg
     1501 l
//
LOCUS       NP_001387116            1140 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 35 [Homo sapiens].
ACCESSION   NP_001387116 XP_011529765
VERSION     NP_001387116.1
DBSOURCE    REFSEQ: accession NM_001400187.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1140)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1140)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1140)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1140)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1140)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1140)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1140)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1140)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1140)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1140)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2 and AC010877.3.
            
            On Jan 20, 2022 this sequence version replaced XP_011529765.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612689.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1140
                     /product="histone demethylase UTY isoform 35"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=124609
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..440
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..1140
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001400187.1:369..3791"
                     /note="isoform 35 is encoded by transcript variant 87"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq ngsdnwnggq slshhpvqqv yslcltpqkl qhleqlranr
      481 dnlnpaqkhq leqlesqfvl mqqmrhkeva qvrttgihng aitdsslptn svsnrqphga
      541 ltrvssvsqp gvrpacvekl lssgafsagc ipcgtskilg stdtillgsn ciagsesngn
      601 vpylqqntht lphnhtdlns steepwrkql snsaqaylgh ltgfiqdncn kglhksqssc
      661 lsgpneeqpl fstgsaqyhq atstgikkan ehltlpsnsv pqgdadshls chtatsggqq
      721 gimftkeskp sknrslvpet srhtgdtsng cadvkglsnh vhqliadavs spnhgdspnl
      781 liadnpqlsa lligkangnv gtgtcdkvnn ihpavhtktd hsvasspssa istatpspks
      841 teqrsinsvt slnsphsglh tvngeglgks qsstkvdlpl ashrstsqil psmsvsicps
      901 stevlkacrn pgknglsnsc illdkcpppr pptspypplp kdklnpptps iylenkrdaf
      961 fpplhqfctn pknpvtvirg lagalkldlg lfstktlvea nnehmvevrt qllqpadenw
     1021 dptgtkkiwr cesnrshtti akyaqyqass fqeslragmq wcdlsslqpp ppgfkrfshl
     1081 slpnswnyrh lpscptnfci fvetgfhhvg qaclelltsg gllasasqsa gitgvshhar
//
LOCUS       NP_001369709             653 aa            linear   PRI 07-DEC-2025
DEFINITION  F-box/LRR-repeat protein 19 isoform 5 [Homo sapiens].
ACCESSION   NP_001369709
VERSION     NP_001369709.1
DBSOURCE    REFSEQ: accession NM_001382780.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Dong,H., Huang,C. and Huang,J.
  TITLE     FBXL19-AS1 promotes the progression of nasopharyngeal carcinoma by
            acting as a competing endogenous RNA to sponge miR-431 and
            upregulate PBOV1
  JOURNAL   Mol Med Rep 24 (3) (2021)
   PUBMED   34278444
  REMARK    GeneRIF: FBXL19AS1 promotes the progression of nasopharyngeal
            carcinoma by acting as a competing endogenous RNA to sponge miR431
            and upregulate PBOV1.
REFERENCE   2  (residues 1 to 653)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   3  (residues 1 to 653)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 653)
  AUTHORS   Wang,L., Zhang,X., Liu,Y. and Xu,S.
  TITLE     Long noncoding RNA FBXL19-AS1 induces tumor growth and metastasis
            by sponging miR-203a-3p in lung adenocarcinoma
  JOURNAL   J Cell Physiol 235 (4), 3612-3625 (2020)
   PUBMED   31566718
  REMARK    GeneRIF: Long noncoding RNA FBXL19-AS1 induces tumor growth and
            metastasis by sponging miR-203a-3p in lung adenocarcinoma.
REFERENCE   5  (residues 1 to 653)
  AUTHORS   Xu,C., Liu,K., Lei,M., Yang,A., Li,Y., Hughes,T.R. and Min,J.
  TITLE     DNA Sequence Recognition of Human CXXC Domains and Their Structural
            Determinants
  JOURNAL   Structure 26 (1), 85-95 (2018)
   PUBMED   29276034
REFERENCE   6  (residues 1 to 653)
  AUTHORS   Chandran,V.
  TITLE     The genetics of psoriasis and psoriatic arthritis
  JOURNAL   Clin Rev Allergy Immunol 44 (2), 149-156 (2013)
   PUBMED   22274791
  REMARK    Review article
REFERENCE   7  (residues 1 to 653)
  AUTHORS   Stuart,P.E., Nair,R.P., Ellinghaus,E., Ding,J., Tejasvi,T.,
            Gudjonsson,J.E., Li,Y., Weidinger,S., Eberlein,B., Gieger,C.,
            Wichmann,H.E., Kunz,M., Ike,R., Krueger,G.G., Bowcock,A.M.,
            Mrowietz,U., Lim,H.W., Voorhees,J.J., Abecasis,G.R.,
            Weichenthal,M., Franke,A., Rahman,P., Gladman,D.D. and Elder,J.T.
  TITLE     Genome-wide association analysis identifies three psoriasis
            susceptibility loci
  JOURNAL   Nat Genet 42 (11), 1000-1004 (2010)
   PUBMED   20953189
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 653)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   9  (residues 1 to 653)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of FBXL19 gene in silico
  JOURNAL   Int J Mol Med 14 (6), 1109-1114 (2004)
   PUBMED   15547684
REFERENCE   10 (residues 1 to 653)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC135048.2.
            
            Summary: This gene encodes a member of the Skp1-Cullin-F-box family
            of E3 ubiquitin ligases. The encoded protein is reported to bind to
            the transmembrane receptor interleukin 1 receptor-like 1 and
            regulate its ubiquitination and degradation. This protein has been
            linked to the regulation of pulmonary inflammation and psoriasis.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Aug 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1807959.1,
                                           SRR14038193.2003119.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..653
                     /product="F-box/LRR-repeat protein 19 isoform 5"
                     /note="jumonji C domain-containing histone demethylase 1C;
                     F-box/LRR-repeat protein 19; jumonji C domain-containing
                     1C"
                     /calculated_mol_wt=71618
     Region          <52..79
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          89..150
                     /region_name="PHD_FXL19"
                     /note="PHD finger found in F-box and leucine-rich repeat
                     protein 19 (FBXL19); cd15645"
                     /db_xref="CDD:277115"
     Site            order(89,112..116,120,145)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277115"
     Region          380..422
                     /region_name="F-box_JHDM"
                     /note="F-box domain found in the JmjC domain-containing
                     histone demethylation protein (JHDM) family; cd22122"
                     /db_xref="CDD:438894"
     Site            order(383..384,386..388,390..391,393..395,397..398,
                     401..402,404..406,410)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438894"
     Region          420..444
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          425..624
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          445..467
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          469..492
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          493..532
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          533..557
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          558..582
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          588..612
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          613..645
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..653
                     /gene="FBXL19"
                     /gene_synonym="CXXC11; Fbl19; JHDM1C"
                     /coded_by="NM_001382780.1:261..2222"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:54620"
                     /db_xref="HGNC:HGNC:25300"
                     /db_xref="MIM:609085"
ORIGIN      
        1 maagrqqmdc dsrqpsallt ppmssssrgp gagarrrrtr crrcracvrt ecgdchfcrd
       61 mkkfggpgrm kqscllrqct apvlphtavc llcgeagked tvegeeekfg lslmecticn
      121 eivhpgclkm gkaegvinae ipncwecprc tqegrtskds gegpgrrrad ngeegaslgs
      181 gwklteeppl ppppprrkgp lpagpppedv pgppkrkere agnepptprk kvkggrerhl
      241 kkkpkpplas aegpavpsps pqreklerfk rmcqllervp dtsssssdsd sdsdssgtsl
      301 sedeapgear ngrrpargss gekenrggrr avrpgsggpl lswplgpapp prppqlerhv
      361 vrppprspep dtlplaagsd hplpraawlr vfqhlgprel cicmrvcrtw srwcydkrlw
      421 prmdlsrrks ltppmlsgvv rrqpraldls wtgvskkqlm wllnrlqglq elvlsgcswl
      481 svsalgsapl palrlldlrw iedvkdsqlr elllpppdtk pgqtesrgrl qgvaelrlag
      541 leltdaslrl llrhapqlsa ldlshcahvg dpsvhlltap tsplretlvh lnlagchrlt
      601 dhclplfrrc prlrrldlrs crqlspeaca rlaaagppgp frcpeeklll kds
//
LOCUS       NP_001245184            1268 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 10 [Homo sapiens].
ACCESSION   NP_001245184
VERSION     NP_001245184.1
DBSOURCE    REFSEQ: accession NM_001258255.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1268)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1268)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1268)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1268)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1268)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1268)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1268)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1268)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1268)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1268)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, EF612660.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (10) has multiple differences in
            the coding region, but maintains the reading frame, compared to
            variant 4. The encoded isoform (10) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612660.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1268
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1268
                     /product="histone demethylase UTY isoform 10"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=141388
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..440
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          967..1031
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1001..1109
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1268
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258255.1:1006..4812"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq ngsdnwnggq slshhpvqqv yslcltpqkl qhleqlranr
      481 dnlnpaqkhq leqlesqfvl mqqmrhkeva qglhksqssc lsgpneeqpl fstgsaqyhq
      541 atstgikkan ehltlpsnsv pqgdadshls chtatsggqq gimftkeskp sknrslvpet
      601 srhtgdtsng cadvkglsnh vhqliadavs spnhgdspnl liadnpqlsa lligkangnv
      661 gtgtcdkvnn ihpavhtktd hsvasspssa istatpspks teqrsinsvt slnsphsglh
      721 tvngeglgks qsstkvdlpl ashrstsqil psmsvsicps stevlkacrn pgknglsnsc
      781 illdkcpppr pptspypplp kdklnpptps iylenkrdaf fpplhqfctn pknpvtvirg
      841 lagalkldlg lfstktlvea nnehmvevrt qllqpadenw dptgtkkiwr cesnrshtti
      901 akyaqyqass fqeslreene krtqhkdhsd nestssensg rrrkgpfkti kfgtnidlsd
      961 nkkwklqlhe ltklpafarv vsagnllthv ghtilgmntv qlymkvpgsr tpghqennnf
     1021 csvninigpg dcewfvvped ywgvlndfce knnlnflmss wwpnledlye anvpvyrfiq
     1081 rpgdlvwina gtvhwvqavg wcnniawnvg pltacqykla veryewnklk svkspvpmvh
     1141 lswnmarnik vsdpklfemi kycllkilkq yqtlrealva agkeviwhgr tndepahycs
     1201 icevevfnll fvtnesntqk tyivhchdca rktskslenf vvleqykmed liqvydqftl
     1261 alslssss
//
LOCUS       NP_001387100            1515 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 27 [Homo sapiens].
ACCESSION   NP_001387100 XP_011529752
VERSION     NP_001387100.1
DBSOURCE    REFSEQ: accession NM_001400171.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1515)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1515)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1515)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1515)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1515)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1515)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1515)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1515)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1515)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1515)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, AC010877.3 and
            AC244214.2.
            
            On Jan 20, 2022 this sequence version replaced XP_011529752.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.3167386.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1515
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1515
                     /product="histone demethylase UTY isoform 27"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=168176
     Region          <72..158
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..401
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1076..1140
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1110..1218
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1515
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001400171.1:369..4916"
                     /note="isoform 27 is encoded by transcript variant 79"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqqslsl hmitssqveg lsspakkkrt
      421 ssptkngsdn wnggqslshh pvqqvyslcl tpqklqhleq lranrdnlnp aqkhqleqle
      481 sqfvlmqqmr hkevaqvrtt gihngaitds slptnsvsnr qphgaltrvs svsqpgvrpa
      541 cvekllssga fsagcipcgt skilgstdti llgsnciags esngnvpylq qnthtlphnh
      601 tdlnssteep wrkqlsnsaq glhksqsscl sgpneeqplf stgsaqyhqa tstgikkane
      661 hltlpsnsvp qgdadshlsc htatsggqqg imftkeskps knrslvpets rhtgdtsngc
      721 advkglsnhv hqliadavss pnhgdspnll iadnpqlsal ligkangnvg tgtcdkvnni
      781 hpavhtktdh svasspssai statpspkst eqrsinsvts lnsphsglht vngeglgksq
      841 sstkvdlpla shrstsqilp smsvsicpss tevlkacrnp gknglsnsci lldkcppprp
      901 ptspypplpk dklnpptpsi ylenkrdaff pplhqfctnp knpvtvirgl agalkldlgl
      961 fstktlvean nehmvevrtq llqpadenwd ptgtkkiwrc esnrshttia kyaqyqassf
     1021 qeslreenek rtqhkdhsdn estssensgr rrkgpfktik fgtnidlsdn kkwklqlhel
     1081 tklpafarvv sagnllthvg htilgmntvq lymkvpgsrt pghqennnfc svninigpgd
     1141 cewfvvpedy wgvlndfcek nnlnflmssw wpnledlyea nvpvyrfiqr pgdlvwinag
     1201 tvhwvqavgw cnniawnvgp ltacqyklav eryewnklks vkspvpmvhl swnmarnikv
     1261 sdpklfemik ycllkilkqy qtlrealvaa gkeviwhgrt ndepahycsi cevevfnllf
     1321 vtnesntqkt yivhchdcar ktskslenfv vleqykmedl iqvydqftla spwppmdqsa
     1381 ftssllrpik algsgraeqt sgdqlqkgat hsrassllra aemtrrpasr eelpdpglfc
     1441 hsikllfvlf sfhlstflil pcqrrrtwel ldggaesckt nrantpiahy lvseeerrav
     1501 alqrvqtwel lepgl
//
LOCUS       NP_872600               1240 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 2 [Homo sapiens].
ACCESSION   NP_872600
VERSION     NP_872600.1
DBSOURCE    REFSEQ: accession NM_182659.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1240)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1240)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1240)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1240)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1240)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1240)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1240)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1240)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1240)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1240)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF000995.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (2) has multiple differences
            compared to variant 4, including the use of an alternate 3' UTR.
            The encoded isoform (2) is shorter than isoform 4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF000995.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1240
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1240
                     /product="histone demethylase UTY isoform 2"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=137082
     Region          90..123
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..160
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          167..196
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          168..452
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..235
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..280
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          281..314
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          315..348
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..382
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          571..621
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          633..689
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          757..819
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            887
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24798337; propagated from
                     UniProtKB/Swiss-Prot (O14607.2)"
     Region          990..1026
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          1046..1110
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1080..1188
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1240
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_182659.1:1006..4728"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS14784.1"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqngsdn wnggqslshh pvqqvyslcl
      421 tpqklqhleq lranrdnlnp aqkhqleqle sqfvlmqqmr hkevaqvrtt gihngaitds
      481 slptnsvsnr qphgaltrvs svsqpgvrpa cvekllssga fsagcipcgt skilgstdti
      541 llgsnciags esngnvpylq qnthtlphnh tdlnssteep wrkqlsnsaq glhksqsscl
      601 sgpneeqplf stgsaqyhqa tstgikkane hltlpsnsvp qgdadshlsc htatsggqqg
      661 imftkeskps knrslvpets rhtgdtsngc advkglsnhv hqliadavss pnhgdspnll
      721 iadnpqlsal ligkangnvg tgtcdkvnni hpavhtktdh svasspssai statpspkst
      781 eqrsinsvts lnsphsglht vngeglgksq sstkvdlpla shrstsqilp smsvsicpss
      841 tevlkacrnp gknglsnsci lldkcppprp ptspypplpk dklnpptpsi ylenkrdaff
      901 pplhqfctnp knpvtvirgl agalkldlgl fstktlvean nehmvevrtq llqpadenwd
      961 ptgtkkiwrc esnrshttia kyaqyqassf qeslreenek rtqhkdhsdn estssensgr
     1021 rrkgpfktik fgtnidlsdn kkwklqlhel tklpafarvv sagnllthvg htilgmntvq
     1081 lymkvpgsrt pghqennnfc svninigpgd cewfvvpedy wgvlndfcek nnlnflmssw
     1141 wpnledlyea nvpvyrfiqr pgdlvwinag tvhwvqavgw cnniawnvgp ltacqyklav
     1201 eryewnklks vkspvpmvhl swnmarnikv sdpklfemik
//
LOCUS       NP_001387104            1422 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 29 [Homo sapiens].
ACCESSION   NP_001387104 XP_016885555
VERSION     NP_001387104.1
DBSOURCE    REFSEQ: accession NM_001400175.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1422)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1422)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1422)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1422)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1422)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1422)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1422)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1422)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1422)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1422)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2 and AC010877.3.
            
            On Jan 20, 2022 this sequence version replaced XP_016885555.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.113803.1,
                                           SRR1803616.46341.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1422
                     /product="histone demethylase UTY isoform 29"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=157594
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..441
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1121..1185
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1155..1263
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1422
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001400175.1:369..4637"
                     /note="isoform 29 is encoded by transcript variant 81"
                     /db_xref="CCDS:CCDS94713.1"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq qslslhmits sqveglsspa kkkrtssptk ngsdnwnggq
      481 slshhpvqqv yslcltpqkl qhleqlranr dnlnpaqkhq leqlesqfvl mqqmrhkeva
      541 qvrttgihng aitdsslptn svsnrqphga ltrvssvsqp gvrpacvekl lssgafsagc
      601 ipcgtskilg stdtillgsn ciagsesngn vpylqqntht lphnhtdlns steepwrkql
      661 snsaqglhks qssclsgpne eqplfstgsa qyhqatstgi kkanehltlp snsvpqgdad
      721 shlschtats ggqqgimftk eskpsknrsl vpetsrhtgd tsngcadvkg lsnhvhqlia
      781 davsspnhgd spnlliadnp qlsalligka ngnvgtgtcd kvnnihpavh tktdhsvass
      841 pssaistatp spksteqrsi nsvtslnsph sglhtvngeg lgksqsstkv dlplashrst
      901 sqilpsmsvs icpsstevlk acrnpgkngl snscilldkc ppprpptspy pplpkdklnp
      961 ptpsiylenk rdaffpplhq fctnpknpvt virglagalk ldlglfstkt lveannehmv
     1021 evrtqllqpa denwdptgtk kiwrcesnrs httiakyaqy qassfqeslr eenekrtqhk
     1081 dhsdnestss ensgrrrkgp fktikfgtni dlsdnkkwkl qlheltklpa farvvsagnl
     1141 lthvghtilg mntvqlymkv pgsrtpghqe nnnfcsvnin igpgdcewfv vpedywgvln
     1201 dfceknnlnf lmsswwpnle dlyeanvpvy rfiqrpgdlv winagtvhwv qavgwcnnia
     1261 wnvgpltacq yklaveryew nklksvkspv pmvhlswnma rnikvsdpkl femikycllk
     1321 ilkqyqtlre alvaagkevi whgrtndepa hycsicevev fnllfvtnes ntqktyivhc
     1381 hdcarktsks lenfvvleqy kmedliqvyd qftleisapl vl
//
LOCUS       NP_001387110            1347 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 32 [Homo sapiens].
ACCESSION   NP_001387110 XP_016885557
VERSION     NP_001387110.1
DBSOURCE    REFSEQ: accession NM_001400181.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1347)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1347)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1347)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1347)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1347)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1347)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1347)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1347)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1347)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1347)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2 and AC010877.3.
            
            On Jan 20, 2022 this sequence version replaced XP_016885557.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1987829.1,
                                           SRR14038197.2462226.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1347
                     /product="histone demethylase UTY isoform 32"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=149507
     Region          90..123
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..160
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          167..196
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          168..452
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..235
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..280
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          281..314
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          315..348
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..382
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          571..621
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          633..689
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          757..819
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            887
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24798337; propagated from
                     UniProtKB/Swiss-Prot (O14607.2)"
     Region          990..1026
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          1046..1110
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1080..1188
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1347
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001400181.1:369..4412"
                     /note="isoform 32 is encoded by transcript variant 84"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqngsdn wnggqslshh pvqqvyslcl
      421 tpqklqhleq lranrdnlnp aqkhqleqle sqfvlmqqmr hkevaqvrtt gihngaitds
      481 slptnsvsnr qphgaltrvs svsqpgvrpa cvekllssga fsagcipcgt skilgstdti
      541 llgsnciags esngnvpylq qnthtlphnh tdlnssteep wrkqlsnsaq glhksqsscl
      601 sgpneeqplf stgsaqyhqa tstgikkane hltlpsnsvp qgdadshlsc htatsggqqg
      661 imftkeskps knrslvpets rhtgdtsngc advkglsnhv hqliadavss pnhgdspnll
      721 iadnpqlsal ligkangnvg tgtcdkvnni hpavhtktdh svasspssai statpspkst
      781 eqrsinsvts lnsphsglht vngeglgksq sstkvdlpla shrstsqilp smsvsicpss
      841 tevlkacrnp gknglsnsci lldkcppprp ptspypplpk dklnpptpsi ylenkrdaff
      901 pplhqfctnp knpvtvirgl agalkldlgl fstktlvean nehmvevrtq llqpadenwd
      961 ptgtkkiwrc esnrshttia kyaqyqassf qeslreenek rtqhkdhsdn estssensgr
     1021 rrkgpfktik fgtnidlsdn kkwklqlhel tklpafarvv sagnllthvg htilgmntvq
     1081 lymkvpgsrt pghqennnfc svninigpgd cewfvvpedy wgvlndfcek nnlnflmssw
     1141 wpnledlyea nvpvyrfiqr pgdlvwinag tvhwvqavgw cnniawnvgp ltacqyklav
     1201 eryewnklks vkspvpmvhl swnmarnikv sdpklfemik ycllkilkqy qtlrealvaa
     1261 gkeviwhgrt ndepahycsi cevevfnllf vtnesntqkt yivhchdcar ktskslenfv
     1321 vleqykmedl iqvydqftle isaplvl
//
LOCUS       NP_001245194            1264 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 20 [Homo sapiens].
ACCESSION   NP_001245194
VERSION     NP_001245194.1
DBSOURCE    REFSEQ: accession NM_001258265.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1264)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1264)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1264)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1264)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1264)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1264)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1264)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1264)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1264)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1264)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, EF653189.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (20) lacks six exons in the coding
            region, but maintains the reading frame, compared to variant 4. The
            encoded isoform (20) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF653189.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1264
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1264
                     /product="histone demethylase UTY isoform 20"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=139707
     Region          69..369
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          73..103
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          112..147
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          157..192
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(199,202..203,206..207,209,233,236..237,240..241,
                     243..244,267,270..271,274..275,278)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          199..226
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          231..261
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          266..294
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          963..1027
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          997..1105
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1264
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258265.1:1006..4800"
                     /note="isoform 20 is encoded by transcript variant 20"
                     /db_xref="CCDS:CCDS76073.1"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gknaaflygl glvyfyynaf hwaikafqdv lyvdpsfcra keihlrlglm
      121 fkvntdykss lkrkyhsake ayeqllqten lpaqvkatvl qqlgwmhhnm dlvgdkatke
      181 syaiqylqks leadpnsgqs wyflgrcyss igkvqdafis yrqsidksea sadtwcsigv
      241 lyqqqnqpmd alqayicavq ldhghaaawm dlgtlyescn qpqdaikcyl naarskrcsn
      301 tstlaarikf lqngsdnwng gqslshhpvq qvyslcltpq klqhleqlra nrdnlnpaqk
      361 hqleqlesqf vlmqqmrhke vaqvrttgih ngaitdsslp tnsvsnrqph galtrvssvs
      421 qpgvrpacve kllssgafsa gcipcgtski lgstdtillg snciagsesn gnvpylqqnt
      481 htlphnhtdl nssteepwrk qlsnsaqglh ksqssclsgp neeqplfstg saqyhqatst
      541 gikkanehlt lpsnsvpqgd adshlschta tsggqqgimf tkeskpsknr slvpetsrht
      601 gdtsngcadv kglsnhvhql iadavsspnh gdspnlliad npqlsallig kangnvgtgt
      661 cdkvnnihpa vhtktdhsva sspssaista tpspksteqr sinsvtslns phsglhtvng
      721 eglgksqsst kvdlplashr stsqilpsms vsicpsstev lkacrnpgkn glsnscilld
      781 kcppprppts pypplpkdkl npptpsiyle nkrdaffppl hqfctnpknp vtvirglaga
      841 lkldlglfst ktlveanneh mvevrtqllq padenwdptg tkkiwrcesn rshttiakya
      901 qyqassfqes lreenekrtq hkdhsdnest ssensgrrrk gpfktikfgt nidlsdnkkw
      961 klqlheltkl pafarvvsag nllthvghti lgmntvqlym kvpgsrtpgh qennnfcsvn
     1021 inigpgdcew fvvpedywgv lndfceknnl nflmsswwpn ledlyeanvp vyrfiqrpgd
     1081 lvwinagtvh wvqavgwcnn iawnvgplta cqyklavery ewnklksvks pvpmvhlswn
     1141 marnikvsdp klfemikycl lkilkqyqtl realvaagke viwhgrtnde pahycsicev
     1201 evfnllfvtn esntqktyiv hchdcarkts kslenfvvle qykmedliqv ydqftlalsl
     1261 ssss
//
LOCUS       NP_001245197            1263 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 23 [Homo sapiens].
ACCESSION   NP_001245197
VERSION     NP_001245197.1
DBSOURCE    REFSEQ: accession NM_001258268.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1263)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1263)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1263)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1263)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1263)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1263)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1263)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1263)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1263)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1263)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, EF612662.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (23) has multiple differences in
            the coding region, one of which results in a frameshift, compared
            to variant 4. The encoded isoform (23) is shorter and has a
            distinct C-terminus, compared to isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612662.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1263
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1263
                     /product="histone demethylase UTY isoform 23"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=140978
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..440
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          967..1031
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1001..1109
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1263
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258268.1:1006..4797"
                     /note="isoform 23 is encoded by transcript variant 23"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq ngsdnwnggq slshhpvqqv yslcltpqkl qhleqlranr
      481 dnlnpaqkhq leqlesqfvl mqqmrhkeva qglhksqssc lsgpneeqpl fstgsaqyhq
      541 atstgikkan ehltlpsnsv pqgdadshls chtatsggqq gimftkeskp sknrslvpet
      601 srhtgdtsng cadvkglsnh vhqliadavs spnhgdspnl liadnpqlsa lligkangnv
      661 gtgtcdkvnn ihpavhtktd hsvasspssa istatpspks teqrsinsvt slnsphsglh
      721 tvngeglgks qsstkvdlpl ashrstsqil psmsvsicps stevlkacrn pgknglsnsc
      781 illdkcpppr pptspypplp kdklnpptps iylenkrdaf fpplhqfctn pknpvtvirg
      841 lagalkldlg lfstktlvea nnehmvevrt qllqpadenw dptgtkkiwr cesnrshtti
      901 akyaqyqass fqeslreene krtqhkdhsd nestssensg rrrkgpfkti kfgtnidlsd
      961 nkkwklqlhe ltklpafarv vsagnllthv ghtilgmntv qlymkvpgsr tpghqennnf
     1021 csvninigpg dcewfvvped ywgvlndfce knnlnflmss wwpnledlye anvpvyrfiq
     1081 rpgdlvwina gtvhwvqavg wcnniawnvg pltacqykla veryewnklk svkspvpmvh
     1141 lswnmarnik vsdpklfemi kycllkilkq yqtlrealva agkeviwhgr tndepahycs
     1201 icevevfnll fvtnesntqk tyivhchdca rktskslenf vvleqykmed liqvydqftl
     1261 vsh
//
LOCUS       NP_001245190            1389 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 16 [Homo sapiens].
ACCESSION   NP_001245190
VERSION     NP_001245190.1
DBSOURCE    REFSEQ: accession NM_001258261.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1389)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1389)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1389)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1389)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1389)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1389)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1389)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1389)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1389)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1389)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, EF612683.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (16) has multiple differences in
            the coding region, but maintains the reading frame, compared to
            variant 4. The encoded isoform (16) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612683.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1389
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1389
                     /product="histone demethylase UTY isoform 16"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=153835
     Region          <72..158
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..408
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(241,244..245,248..249,251,282,285..286,290..291,
                     293..294,317,320..321,324..325,328)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          280..311
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          316..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1088..1152
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1122..1230
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1389
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258261.1:1006..5175"
                     /note="isoform 16 is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS76074.1"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgsv lyqqqnqpmd
      301 alqayicavq ldhghaaawm dlgtlyescn qpqdaikcyl naarskrcsn tstlaarikf
      361 lqaqlcnlpq sslqnktkll psieeawslp ipaeltsrqg amntaqqqsl slhmitssqv
      421 eglsspakkk rtssptkngs dnwnggqsls hhpvqqvysl cltpqklqhl eqlranrdnl
      481 npaqkhqleq lesqfvlmqq mrhkevaqvr ttgihngait dsslptnsvs nrqphgaltr
      541 vssvsqpgvr pacvekllss gafsagcipc gtskilgstd tillgsncia gsesngnvpy
      601 lqqnthtlph nhtdlnsste epwrkqlsns aqglhksqss clsgpneeqp lfstgsaqyh
      661 qatstgikka nehltlpsns vpqgdadshl schtatsggq qgimftkesk psknrslvpe
      721 tsrhtgdtsn gcadvkglsn hvhqliadav sspnhgdspn lliadnpqls alligkangn
      781 vgtgtcdkvn nihpavhtkt dhsvasspss aistatpspk steqrsinsv tslnsphsgl
      841 htvngeglgk sqsstkvdlp lashrstsqi lpsmsvsicp sstevlkacr npgknglsns
      901 cilldkcppp rpptspyppl pkdklnpptp siylenkrda ffpplhqfct npknpvtvir
      961 glagalkldl glfstktlve annehmvevr tqllqpaden wdptgtkkiw rcesnrshtt
     1021 iakyaqyqas sfqeslreen ekrtqhkdhs dnestssens grrrkgpfkt ikfgtnidls
     1081 dnkkwklqlh eltklpafar vvsagnllth vghtilgmnt vqlymkvpgs rtpghqennn
     1141 fcsvninigp gdcewfvvpe dywgvlndfc eknnlnflms swwpnledly eanvpvyrfi
     1201 qrpgdlvwin agtvhwvqav gwcnniawnv gpltacqykl averyewnkl ksvkspvpmv
     1261 hlswnmarni kvsdpklfem ikycllkilk qyqtlrealv aagkeviwhg rtndepahyc
     1321 sicevevfnl lfvtnesntq ktyivhchdc arktskslen fvvleqykme dliqvydqft
     1381 lalslssss
//
LOCUS       NP_001245193            1376 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 19 [Homo sapiens].
ACCESSION   NP_001245193
VERSION     NP_001245193.1
DBSOURCE    REFSEQ: accession NM_001258264.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1376)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1376)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1376)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1376)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1376)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1376)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1376)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1376)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1376)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1376)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, EF612695.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (19) has multiple differences in
            the coding region, but maintains the reading frame, compared to
            variant 4. The encoded isoform (19) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612695.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1376
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1376
                     /product="histone demethylase UTY isoform 19"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=152488
     Region          <72..158
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..424
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          201..231
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(241,244..245,248..249,251,300,303..304,307..308,
                     310..311,334,337..338,341..342,345)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          280..328
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          333..361
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1075..1139
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1109..1217
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1376
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258264.1:1006..5136"
                     /note="isoform 19 is encoded by transcript variant 19"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrq sidkseasad
      301 twcsigvlyq qqnqpmdalq ayicavqldh ghaaawmdlg tlyescnqpq daikcylnaa
      361 rskrcsntst laarikflqa qlcnlpqssl qnktkllpsi eeawslpipa eltsrqgamn
      421 taqqngsdnw nggqslshhp vqqvyslclt pqklqhleql ranrdnlnpa qkhqleqles
      481 qfvlmqqmrh kevaqvrttg ihngaitdss lptnsvsnrq phgaltrvss vsqpgvrpac
      541 vekllssgaf sagcipcgts kilgstdtil lgsnciagse sngnvpylqq nthtlphnht
      601 dlnssteepw rkqlsnsaqg lhksqsscls gpneeqplfs tgsaqyhqat stgikkaneh
      661 ltlpsnsvpq gdadshlsch tatsggqqgi mftkeskpsk nrslvpetsr htgdtsngca
      721 dvkglsnhvh qliadavssp nhgdspnlli adnpqlsall igkangnvgt gtcdkvnnih
      781 pavhtktdhs vasspssais tatpspkste qrsinsvtsl nsphsglhtv ngeglgksqs
      841 stkvdlplas hrstsqilps msvsicpsst evlkacrnpg knglsnscil ldkcppprpp
      901 tspypplpkd klnpptpsiy lenkrdaffp plhqfctnpk npvtvirgla galkldlglf
      961 stktlveann ehmvevrtql lqpadenwdp tgtkkiwrce snrshttiak yaqyqassfq
     1021 eslreenekr tqhkdhsdne stssensgrr rkgpfktikf gtnidlsdnk kwklqlhelt
     1081 klpafarvvs agnllthvgh tilgmntvql ymkvpgsrtp ghqennnfcs vninigpgdc
     1141 ewfvvpedyw gvlndfcekn nlnflmssww pnledlyean vpvyrfiqrp gdlvwinagt
     1201 vhwvqavgwc nniawnvgpl tacqyklave ryewnklksv kspvpmvhls wnmarnikvs
     1261 dpklfemiky cllkilkqyq tlrealvaag keviwhgrtn depahycsic evevfnllfv
     1321 tnesntqkty ivhchdcark tskslenfvv leqykmedli qvydqftlal slssss
//
LOCUS       NP_001245199            1218 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 25 [Homo sapiens].
ACCESSION   NP_001245199
VERSION     NP_001245199.1
DBSOURCE    REFSEQ: accession NM_001258270.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1218)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1218)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1218)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1218)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1218)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1218)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1218)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1218)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1218)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1218)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, EF612669.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (25) has multiple differences in
            the coding region, one of which results in a frameshift, compared
            to variant 4. The encoded isoform (25) is shorter and has a
            distinct C-terminus, compared to isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612669.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1218
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1218
                     /product="histone demethylase UTY isoform 25"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=136088
     Region          90..123
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..160
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          167..196
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          168..452
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..235
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          247..280
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          281..314
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          315..348
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..382
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          922..986
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          956..1064
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1218
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258270.1:1006..4662"
                     /note="isoform 25 is encoded by transcript variant 25"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqngsdn wnggqslshh pvqqvyslcl
      421 tpqklqhleq lranrdnlnp aqkhqleqle sqfvlmqqmr hkevaqglhk sqssclsgpn
      481 eeqplfstgs aqyhqatstg ikkanehltl psnsvpqgda dshlschtat sggqqgimft
      541 keskpsknrs lvpetsrhtg dtsngcadvk glsnhvhqli adavsspnhg dspnlliadn
      601 pqlsalligk angnvgtgtc dkvnnihpav htktdhsvas spssaistat pspksteqrs
      661 insvtslnsp hsglhtvnge glgksqsstk vdlplashrs tsqilpsmsv sicpsstevl
      721 kacrnpgkng lsnscilldk cppprpptsp ypplpkdkln pptpsiylen krdaffpplh
      781 qfctnpknpv tvirglagal kldlglfstk tlveannehm vevrtqllqp adenwdptgt
      841 kkiwrcesnr shttiakyaq yqassfqesl reenekrtqh kdhsdnests sensgrrrkg
      901 pfktikfgtn idlsdnkkwk lqlheltklp afarvvsagn llthvghtil gmntvqlymk
      961 vpgsrtpghq ennnfcsvni nigpgdcewf vvpedywgvl ndfceknnln flmsswwpnl
     1021 edlyeanvpv yrfiqrpgdl vwinagtvhw vqavgwcnni awnvgpltac qyklaverye
     1081 wnklksvksp vpmvhlswnm arnikvsdpk lfemikycll kilkqyqtlr ealvaagkev
     1141 iwhgrtndep ahycsiceve vfnllfvtne sntqktyivh chdcarktsk slenfvvleq
     1201 ykmedliqvy dqftlvsh
//
LOCUS       NP_001387112            1176 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 33 [Homo sapiens].
ACCESSION   NP_001387112 XP_011529763
VERSION     NP_001387112.1
DBSOURCE    REFSEQ: accession NM_001400183.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1176)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1176)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1176)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1176)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1176)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1176)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1176)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1176)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1176)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1176)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2 and AC010877.3.
            
            On Jan 20, 2022 this sequence version replaced XP_011529763.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612677.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1176
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1176
                     /product="histone demethylase UTY isoform 33"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=128553
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..191
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..445
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..1176
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001400183.1:369..3899"
                     /note="isoform 33 is encoded by transcript variant 85"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq ayrahdpnte hvlnhsqtpi lqqslslhmi tssqveglss
      481 pakkkrtssp tkngsdnwng gqslshhpvq qvyslcltpq klqhleqlra nrdnlnpaqk
      541 hqleqlesqf vlmqqmrhke vaqvrttgih ngaitdsslp tnsvsnrqph galtrvssvs
      601 qpgvrpacve kllssgafsa gcipcgtski lgstdtillg snciagsesn gnvpylqqnt
      661 htlphnhtdl nssteepwrk qlsnsaqglh ksqssclsgp neeqplfstg saqyhqatst
      721 gikkanehlt lpsnsvpqgd adshlschta tsggqqgimf tkeskpsknr slvpetsrht
      781 gdtsngcadv kglsnhvhql iadavsspnh gdspnlliad npqlsallig kangnvgtgt
      841 cdkvnnihpa vhtktdhsva sspssaista tpspksteqr sinsvtslns phsglhtvng
      901 eglgksqsst kvdlplashr stsqilpsms vsicpsstev lkacrnpgkn glsnscilld
      961 kcppprppts pypplpkdkl npptpsiyle nkrdaffppl hqfctnpknp vtvirglaga
     1021 lkldlglfst ktlveanneh mvevrtqllq padenwdptg tkkiwrcesn rshttiakya
     1081 qyqassfqes lragmqwcdl sslqppppgf krfshlslpn swnyrhlpsc ptnfcifvet
     1141 gfhhvgqacl elltsgglla sasqsagitg vshhar
//
LOCUS       NP_001284630             238 aa            linear   PRI 07-DEC-2025
DEFINITION  probable RNA/DNA demethylase ALKBH6 isoform 3 [Homo sapiens].
ACCESSION   NP_001284630 XP_005259415
VERSION     NP_001284630.1
DBSOURCE    REFSEQ: accession NM_001297701.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Das,S., Rankawat,S., Shaji,U.P., Tuti,N., Shahnaz,N., Ray,S. and
            Anindya,R.
  TITLE     Identification of ALKBH6 as a nucleotide demethylase with a
            distinct substrate preference
  JOURNAL   J Biol Chem 301 (10), 110638 (2025)
   PUBMED   40885392
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Das,S., Shahnaz,N., Keerthana,C., Ranjan,S., Seenivasan,G.,
            Tuti,N., Shaji,U.P., Meur,G. and Anindya,R.
  TITLE     Functional and comparative analysis of the
            FeII/2-oxoglutarate-dependent dioxygenases without using any
            substrate
  JOURNAL   Biol Methods Protoc 10 (1), bpae096 (2024)
   PUBMED   39845104
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Ma,L., Lu,H., Tian,Z., Yang,M., Ma,J., Shang,G., Liu,Y., Xie,M.,
            Wang,G., Wu,W., Zhang,Z., Dai,S. and Chen,Z.
  TITLE     Structural insights into the interactions and epigenetic functions
            of human nucleic acid repair protein ALKBH6
  JOURNAL   J Biol Chem 298 (3), 101671 (2022)
   PUBMED   35120926
  REMARK    GeneRIF: Structural insights into the interactions and epigenetic
            functions of human nucleic acid repair protein ALKBH6.
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Kernstock,S., Davydova,E., Jakobsson,M., Moen,A., Pettersen,S.,
            Maelandsmo,G.M., Egge-Jacobsen,W. and Falnes,P.O.
  TITLE     Lysine methylation of VCP by a member of a novel human protein
            methyltransferase family
  JOURNAL   Nat Commun 3, 1038 (2012)
   PUBMED   22948820
REFERENCE   5  (residues 1 to 238)
  AUTHORS   Tsujikawa,K., Koike,K., Kitae,K., Shinkawa,A., Arima,H., Suzuki,T.,
            Tsuchiya,M., Makino,Y., Furukawa,T., Konishi,N. and Yamamoto,H.
  TITLE     Expression and sub-cellular localization of human ABH family
            molecules
  JOURNAL   J Cell Mol Med 11 (5), 1105-1116 (2007)
   PUBMED   17979886
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB273714.1, AK304805.1 and BQ447659.1.
            
            On Jul 10, 2014 this sequence version replaced XP_005259415.1.
            
            Transcript Variant: Variants 2, 3, and 5 encode the same isoform
            (3).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.475480.1,
                                           ERR279837.1097.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398, SAMEA2159931
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..238
                     /product="probable RNA/DNA demethylase ALKBH6 isoform 3"
                     /EC_number="3.4.22.17"
                     /note="alkylated DNA repair protein alkB homolog 6;
                     probable alpha-ketoglutarate-dependent dioxygenase ABH6;
                     alkB, alkylation repair homolog 6;
                     alpha-ketoglutarate-dependent dioxygenase alkB homolog 6;
                     probable nucleic acid dioxygenase ALKBH6; probable RNA/DNA
                     demethylase ALKBH6"
                     /calculated_mol_wt=26352
     Region          23..224
                     /region_name="2OG-FeII_Oxy"
                     /note="2OG-Fe(II) oxygenase superfamily; cl21496"
                     /db_xref="CDD:473886"
     Region          138..161
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KRA9.2)"
     CDS             1..238
                     /gene="ALKBH6"
                     /gene_synonym="ABH6"
                     /coded_by="NM_001297701.2:140..856"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS74342.1"
                     /db_xref="GeneID:84964"
                     /db_xref="HGNC:HGNC:28243"
                     /db_xref="MIM:613304"
ORIGIN      
        1 meeqdarvpa lepfrveqap pviyyvpdfi skeeeeyllr qvfnapkpkw tqlsgrklqn
       61 wgglphprgm vperlppwlq ryvdkvsnls lfgglpanhv lvnqylpgeg imphedgply
      121 yptvstislg shtvldfyep rrpedddpte qprppprptt sllleprsll vlrgpaytrl
      181 lhgiaaarvd aldaassppn aaacpsarpg aclvrgtrvs ltirrvprvl raglllgk
//
LOCUS       NP_001245188            1331 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 14 [Homo sapiens].
ACCESSION   NP_001245188
VERSION     NP_001245188.1
DBSOURCE    REFSEQ: accession NM_001258259.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1331)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1331)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1331)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1331)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1331)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1331)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1331)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1331)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1331)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1331)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, EF612665.1 and
            AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (14) has multiple differences in
            the coding region, but maintains the reading frame, compared to
            variant 4. The encoded isoform (14) is shorter than isoform 4.
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612665.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1331
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1331
                     /product="histone demethylase UTY isoform 14"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=147598
     Region          <72..158
                     /region_name="TadD"
                     /note="Flp pilus assembly protein TadD, contains TPR
                     repeats [Intracellular trafficking, secretion, and
                     vesicular transport, Extracellular structures]; COG5010"
                     /db_xref="CDD:444034"
     Region          90..123
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          127..436
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          127..160
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          167..196
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          201..231
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          202..235
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(241,244..245,248..249,251,300,303..304,307..308,
                     310..311,334,337..338,341..342,345)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          247..280
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          280..328
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          299..332
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          333..366
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          333..361
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          555..605
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          617..673
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          741..803
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Site            871
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24798337; propagated from
                     UniProtKB/Swiss-Prot (O14607.2)"
     Region          974..1010
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14607.2)"
     Region          1030..1094
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1064..1172
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1331
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258259.1:1006..5001"
                     /note="isoform 14 is encoded by transcript variant 14"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrq sidkseasad
      301 twcsigvlyq qqnqpmdalq ayicavqldh ghaaawmdlg tlyescnqpq daikcylnaa
      361 rskrcsntst laarikflqn gsdnwnggqs lshhpvqqvy slcltpqklq hleqlranrd
      421 nlnpaqkhql eqlesqfvlm qqmrhkevaq vrttgihnga itdsslptns vsnrqphgal
      481 trvssvsqpg vrpacvekll ssgafsagci pcgtskilgs tdtillgsnc iagsesngnv
      541 pylqqnthtl phnhtdlnss teepwrkqls nsaqglhksq ssclsgpnee qplfstgsaq
      601 yhqatstgik kanehltlps nsvpqgdads hlschtatsg gqqgimftke skpsknrslv
      661 petsrhtgdt sngcadvkgl snhvhqliad avsspnhgds pnlliadnpq lsalligkan
      721 gnvgtgtcdk vnnihpavht ktdhsvassp ssaistatps pksteqrsin svtslnsphs
      781 glhtvngegl gksqsstkvd lplashrsts qilpsmsvsi cpsstevlka crnpgkngls
      841 nscilldkcp pprpptspyp plpkdklnpp tpsiylenkr daffpplhqf ctnpknpvtv
      901 irglagalkl dlglfstktl veannehmve vrtqllqpad enwdptgtkk iwrcesnrsh
      961 ttiakyaqyq assfqeslre enekrtqhkd hsdnestsse nsgrrrkgpf ktikfgtnid
     1021 lsdnkkwklq lheltklpaf arvvsagnll thvghtilgm ntvqlymkvp gsrtpghqen
     1081 nnfcsvnini gpgdcewfvv pedywgvlnd fceknnlnfl msswwpnled lyeanvpvyr
     1141 fiqrpgdlvw inagtvhwvq avgwcnniaw nvgpltacqy klaveryewn klksvkspvp
     1201 mvhlswnmar nikvsdpklf emikycllki lkqyqtlrea lvaagkeviw hgrtndepah
     1261 ycsicevevf nllfvtnesn tqktyivhch dcarktsksl enfvvleqyk medliqvydq
     1321 ftlalslsss s
//
LOCUS       NP_002282               1786 aa            linear   PRI 07-DEC-2025
DEFINITION  laminin subunit beta-1 precursor [Homo sapiens].
ACCESSION   NP_002282
VERSION     NP_002282.2
DBSOURCE    REFSEQ: accession NM_002291.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1786)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1786)
  AUTHORS   Li,M., Fu,H., Li,J., Meng,D., Zhang,Q. and Fei,D.
  TITLE     Compound variants of FKTN, POMGNT1, and LAMB1 gene identified by
            prenatal whole-exome sequencing in three fetuses with congenital
            hydrocephalus
  JOURNAL   J Obstet Gynaecol Res 48 (10), 2624-2629 (2022)
   PUBMED   35843586
  REMARK    GeneRIF: Compound variants of FKTN, POMGNT1, and LAMB1 gene
            identified by prenatal whole-exome sequencing in three fetuses with
            congenital hydrocephalus.
REFERENCE   3  (residues 1 to 1786)
  AUTHORS   Liu,T., Gan,H., He,S., Deng,J., Hu,X., Li,L., Cai,L., He,J.,
            Long,H., Cai,J., Li,H., Zhang,Q., Wang,L., Chen,F., Chen,Y.,
            Zhang,H., Li,J., Yang,L., Liu,Y., Yang,J.H., Kuang,D.M., Pang,P.,
            He,H. and Shan,H.
  TITLE     RNA Helicase DDX24 Stabilizes LAMB1 to Promote Hepatocellular
            Carcinoma Progression
  JOURNAL   Cancer Res 82 (17), 3074-3087 (2022)
   PUBMED   35763670
  REMARK    GeneRIF: RNA Helicase DDX24 Stabilizes LAMB1 to Promote
            Hepatocellular Carcinoma Progression.
REFERENCE   4  (residues 1 to 1786)
  AUTHORS   Wu,X., Dong,S., Xu,Y., Zhu,G. and Yan,M.
  TITLE     Evaluation of JUN, FN1 and LAMB1 polymorphisms in pterygium in a
            Chinese Han population
  JOURNAL   Ophthalmic Genet 43 (4), 488-495 (2022)
   PUBMED   35445627
  REMARK    GeneRIF: Evaluation of JUN, FN1 and LAMB1 polymorphisms in
            pterygium in a Chinese Han population.
REFERENCE   5  (residues 1 to 1786)
  AUTHORS   Yang,Y., Gao,L., Chen,J., Xiao,W., Liu,R. and Kan,H.
  TITLE     Lamin B1 is a potential therapeutic target and prognostic biomarker
            for hepatocellular carcinoma
  JOURNAL   Bioengineered 13 (4), 9211-9231 (2022)
   PUBMED   35436411
  REMARK    GeneRIF: Lamin B1 is a potential therapeutic target and prognostic
            biomarker for hepatocellular carcinoma.
REFERENCE   6  (residues 1 to 1786)
  AUTHORS   Aeschlimann,D. and Paulsson,M.
  TITLE     Cross-linking of laminin-nidogen complexes by tissue
            transglutaminase. A novel mechanism for basement membrane
            stabilization
  JOURNAL   J Biol Chem 266 (23), 15308-15317 (1991)
   PUBMED   1678389
REFERENCE   7  (residues 1 to 1786)
  AUTHORS   Bonneau,D., Huret,J.L., Godeau,G., Couet,D., Putterman,M.,
            Tanzer,J., Babin,P. and Larregue,M.
  TITLE     Recurrent ctb(7)(q31.3) and possible laminin involvement in a
            neonatal cutis laxa with a Marfan phenotype
  JOURNAL   Hum Genet 87 (3), 317-319 (1991)
   PUBMED   1864606
REFERENCE   8  (residues 1 to 1786)
  AUTHORS   Chung,A.E. and Durkin,M.E.
  TITLE     Entactin: structure and function
  JOURNAL   Am J Respir Cell Mol Biol 3 (4), 275-282 (1990)
   PUBMED   2119632
  REMARK    Review article
REFERENCE   9  (residues 1 to 1786)
  AUTHORS   Vuolteenaho,R., Chow,L.T. and Tryggvason,K.
  TITLE     Structure of the human laminin B1 chain gene
  JOURNAL   J Biol Chem 265 (26), 15611-15616 (1990)
   PUBMED   1975589
REFERENCE   10 (residues 1 to 1786)
  AUTHORS   Engvall,E., Earwicker,D., Haaparanta,T., Ruoslahti,E. and
            Sanes,J.R.
  TITLE     Distribution and isolation of four laminin variants; tissue
            restricted distribution of heterotrimers assembled from five
            different subunits
  JOURNAL   Cell Regul 1 (10), 731-740 (1990)
   PUBMED   2099832
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA861108.1, BC113455.1,
            BC026018.2 and AC005046.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 11, 2008 this sequence version replaced NP_002282.1.
            
            Summary: Laminins, a family of extracellular matrix glycoproteins,
            are the major noncollagenous constituent of basement membranes.
            They have been implicated in a wide variety of biological processes
            including cell adhesion, differentiation, migration, signaling,
            neurite outgrowth and metastasis. Laminins are composed of 3 non
            identical chains: laminin alpha, beta and gamma (formerly A, B1,
            and B2, respectively) and they form a cruciform structure
            consisting of 3 short arms, each formed by a different chain, and a
            long arm composed of all 3 chains. Each laminin chain is a
            multidomain protein encoded by a distinct gene. Several isoforms of
            each chain have been described. Different alpha, beta and gamma
            chain isomers combine to give rise to different heterotrimeric
            laminin isoforms which are designated by Arabic numerals in the
            order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is
            laminin 1. The biological functions of the different chains and
            trimer molecules are largely unknown, but some of the chains have
            been shown to differ with respect to their tissue distribution,
            presumably reflecting diverse functions in vivo. This gene encodes
            the beta chain isoform laminin, beta 1. The beta 1 chain has 7
            structurally distinct domains which it shares with other beta chain
            isomers. The C-terminal helical region containing domains I and II
            are separated by domain alpha, domains III and V contain several
            EGF-like repeats, and domains IV and VI have a globular
            conformation. Laminin, beta 1 is expressed in most tissues that
            produce basement membranes, and is one of the 3 chains constituting
            laminin 1, the first laminin isolated from Engelbreth-Holm-Swarm
            (EHS) tumor. A sequence in the beta 1 chain that is involved in
            cell attachment, chemotaxis, and binding to the laminin receptor
            was identified and shown to have the capacity to inhibit
            metastasis. [provided by RefSeq, Aug 2011].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by published experimental evidence.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M61916.1, SRR14038197.771538.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222399.11/ ENSP00000222399.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1786
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1786
                     /product="laminin subunit beta-1 precursor"
                     /note="laminin B1 chain; laminin, beta 1"
                     /calculated_mol_wt=195708
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2350
     mat_peptide     22..1786
                     /product="laminin subunit beta-1"
                     /calculated_mol_wt=195708
     Region          22..270
                     /region_name="Domain VI"
                     /note="N-terminal domain"
     Region          35..269
                     /region_name="Laminin_N"
                     /note="Laminin N-terminal (Domain VI); pfam00055"
                     /db_xref="CDD:459653"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07942.2)"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02469; propagated from
                     UniProtKB/Swiss-Prot (P07942.2)"
     Region          271..540
                     /region_name="Domain V"
                     /note="contains 5 EGF-like repeats"
     Region          271..323
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domain;
                     laminins are the major noncollagenous components of
                     basement membranes that mediate cell adhesion, growth
                     migration, and differentiation; the laminin-type epidermal
                     growth factor-like module occurs in...; cd00055"
                     /db_xref="CDD:238012"
     Site            order(271,273,280,298,300,309)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          335..387
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domain;
                     laminins are the major noncollagenous components of
                     basement membranes that mediate cell adhesion, growth
                     migration, and differentiation; the laminin-type epidermal
                     growth factor-like module occurs in...; cd00055"
                     /db_xref="CDD:238012"
     Site            order(335,337,344,362,365,374)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Site            356
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07942.2)"
     Region          398..455
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(398,400,411,426,428,437)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          458..512
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(458,460,472,479,481,490)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          509..>548
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domain;
                     laminins are the major noncollagenous components of
                     basement membranes that mediate cell adhesion, growth
                     migration, and differentiation; the laminin-type epidermal
                     growth factor-like module occurs in...; cd00055"
                     /db_xref="CDD:238012"
     Site            order(510,512,522,529,531,540)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Site            519
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07942.2)"
     Region          541..771
                     /region_name="Domain IV"
     Site            677
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07942.2)"
     Region          772..1178
                     /region_name="Domain III"
                     /note="contains 8 EGF-like repeats"
     Region          773..818
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domai;
                     smart00180"
                     /db_xref="CDD:214543"
     Site            order(773,775,785,792,794,803)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          821..869
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(821,823,833,840,842,851)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          867..914
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(867,869,876,883,886,895)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          917..973
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(917,919,933,944,946,955)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          976..1020
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(976,978,990,997,1000,1009)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          1028..1082
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(1028,1030,1047,1054,1056,1065)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Site            1041
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07942.2)"
     Region          1084..1132
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(1084,1086,1096,1103,1105,1114)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          1132..>1171
                     /region_name="Laminin_EGF"
                     /note="Laminin EGF domain; pfam00053"
                     /db_xref="CDD:395007"
     Site            order(1132,1134,1144,1151,1153,1162)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Region          1179..1397
                     /region_name="Domain II"
     Site            1195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07942.2)"
     Region          <1224..1778
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            1279
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P07942.2)"
     Site            1336
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07942.2)"
     Site            1343
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07942.2)"
     Region          1398..1430
                     /region_name="Domain alpha"
     Region          1431..1786
                     /region_name="Domain I"
                     /note="C-terminal domain"
     Site            1478
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P07942.2)"
     Site            1487
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07942.2)"
     Site            1496
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P07942.2)"
     Site            1542
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P07942.2)"
     Site            1666
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P07942.2)"
     Site            1682
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P07942.2)"
     Region          1714..1786
                     /region_name="cc_LAMB1_C"
                     /note="C-terminal coiled-coil domain found in laminin
                     subunit beta-1 (LAMB1); cd22300"
                     /db_xref="CDD:411971"
     Site            order(1718..1719,1722..1723,1725..1726,1729,1736..1737,
                     1739..1740,1743,1746..1747,1750..1751,1753..1755,
                     1757..1758,1761,1764..1765,1767..1769,1771..1772,
                     1774..1776,1778..1780,1782..1786)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:411971"
     CDS             1..1786
                     /gene="LAMB1"
                     /gene_synonym="CLM; LIS5; LKBMH; LUCAO"
                     /coded_by="NM_002291.3:138..5498"
                     /db_xref="CCDS:CCDS5750.1"
                     /db_xref="GeneID:3912"
                     /db_xref="HGNC:HGNC:6486"
                     /db_xref="MIM:150240"
ORIGIN      
        1 mgllqllafs flalcrarvr aqepefsygc aegscypatg dlligraqkl svtstcglhk
       61 pepycivshl qedkkcficn sqdpyhetln pdshlienvv ttfapnrlki wwqsengven
      121 vtiqldleae fhfthlimtf ktfrpaamli erssdfgktw gvyryfaydc easfpgistg
      181 pmkkvddiic dsrysdieps tegevifral dpafkiedpy spriqnllki tnlrikfvkl
      241 htlgdnllds rmeirekyyy avydmvvrgn cfcyghasec apvdgfneev egmvhghcmc
      301 rhntkglnce lcmdfyhdlp wrpaegrnsn ackkcncneh sischfdmav ylatgnvsgg
      361 vcddcqhntm grnceqckpf yyqhperdir dpnfcerctc dpagsqnegi cdsytdfstg
      421 liagqcrckl nvegehcdvc kegfydlsse dpfgckscac nplgtipggn pcdsetghcy
      481 ckrlvtgqhc dqclpehwgl sndldgcrpc dcdlggalnn scfaesgqcs crphmigrqc
      541 nevepgyyfa tldhylyeae eanlgpgvsi verqyiqdri pswtgagfvr vpegayleff
      601 idnipysmey diliryepql pdhwekavit vqrpgripts srcgntipdd dnqvvslspg
      661 sryvvlprpv cfekgtnytv rlelpqytss dsdvespytl idslvlmpyc ksldiftvgg
      721 sgdgvvtnsa wetfqryrcl ensrsvvktp mtdvcrniif sisallhqtg lacecdpqgs
      781 lssvcdpngg qcqcrpnvvg rtcnrcapgt fgfgpsgckp cechlqgsvn afcnpvtgqc
      841 hcfqgvyarq cdrclpghwg fpscqpcqcn ghaddcdpvt geclncqdyt mghncercla
      901 gyygdpiigs gdhcrpcpcp dgpdsgrqfa rscyqdpvtl qlacvcdpgy igsrcddcas
      961 gyfgnpsevg gscqpcqchn nidttdpeac dketgrclkc lyhtegehcq fcrfgyygda
     1021 lqqdcrkcvc nylgtvqehc ngsdcqcdka tgqclclpnv igqncdrcap ntwqlasgtg
     1081 cdpcncnaah sfgpscneft gqcqcmpgfg grtcsecqel fwgdpdvecr acdcdprgie
     1141 tpqcdqstgq cvcvegvegp rcdkctrgys gvfpdctpch qcfalwdvii aeltnrthrf
     1201 lekakalkis gvigpyretv dsverkvsei kdilaqspaa eplknignlf eeaeklikdv
     1261 temmaqvevk lsdttsqsns takeldslqt eaesldntvk elaeqlefik nsdirgalds
     1321 itkyfqmsle aeervnastt epnstveqsa lmrdrvedvm meresqfkek qeeqarllde
     1381 lagklqsldl saaaemtcgt ppgascsete cggpncrtde gerkcggpgc gglvtvahna
     1441 wqkamdldqd vlsalaeveq lskmvseakl radeakqsae dillktnatk ekmdksneel
     1501 rnlikqirnf ltqdsadlds ieavanevlk mempstpqql qnltedirer veslsqvevi
     1561 lqhsaadiar aemlleeakr asksatdvkv tadmvkeale eaekaqvaae kaikqadedi
     1621 qgtqnlltsi esetaaseet lfnasqrise lernveelkr kaaqnsgeae yiekvvytvk
     1681 qsaedvkktl dgeldekykk venliakkte esadarrkae mlqneaktll aqansklqll
     1741 kdlerkyedn qryledkaqe larlegevrs llkdisqkva vystcl
//
LOCUS       NP_001245178            1444 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 4 [Homo sapiens].
ACCESSION   NP_001245178
VERSION     NP_001245178.1
DBSOURCE    REFSEQ: accession NM_001258249.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1444)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1444)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1444)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1444)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1444)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1444)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1444)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1444)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1444)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1444)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2 and AC010877.3.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (4) encodes the longest isoform
            (4).
            
            Sequence Note: This RefSeq record was created based on a transcript
            variant reported in PMID: 21329462, and assembled from transcript
            and genomic sequence data to make the sequence consistent with the
            reference genome assembly.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF612668.1, SRR18074967.119551.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000545955.6/ ENSP00000442047.2
            RefSeq Select criteria :: based on manual assertion
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1444
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1444
                     /product="histone demethylase UTY isoform 4"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=160027
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..445
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1143..1207
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1177..1285
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1444
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001258249.2:369..4703"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS76079.1"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq ayrahdpnte hvlnhsqtpi lqqslslhmi tssqveglss
      481 pakkkrtssp tkngsdnwng gqslshhpvq qvyslcltpq klqhleqlra nrdnlnpaqk
      541 hqleqlesqf vlmqqmrhke vaqvrttgih ngaitdsslp tnsvsnrqph galtrvssvs
      601 qpgvrpacve kllssgafsa gcipcgtski lgstdtillg snciagsesn gnvpylqqnt
      661 htlphnhtdl nssteepwrk qlsnsaqglh ksqssclsgp neeqplfstg saqyhqatst
      721 gikkanehlt lpsnsvpqgd adshlschta tsggqqgimf tkeskpsknr slvpetsrht
      781 gdtsngcadv kglsnhvhql iadavsspnh gdspnlliad npqlsallig kangnvgtgt
      841 cdkvnnihpa vhtktdhsva sspssaista tpspksteqr sinsvtslns phsglhtvng
      901 eglgksqsst kvdlplashr stsqilpsms vsicpsstev lkacrnpgkn glsnscilld
      961 kcppprppts pypplpkdkl npptpsiyle nkrdaffppl hqfctnpknp vtvirglaga
     1021 lkldlglfst ktlveanneh mvevrtqllq padenwdptg tkkiwrcesn rshttiakya
     1081 qyqassfqes lreenekrtq hkdhsdnest ssensgrrrk gpfktikfgt nidlsdnkkw
     1141 klqlheltkl pafarvvsag nllthvghti lgmntvqlym kvpgsrtpgh qennnfcsvn
     1201 inigpgdcew fvvpedywgv lndfceknnl nflmsswwpn ledlyeanvp vyrfiqrpgd
     1261 lvwinagtvh wvqavgwcnn iawnvgplta cqyklavery ewnklksvks pvpmvhlswn
     1321 marnikvsdp klfemikycl lkilkqyqtl realvaagke viwhgrtnde pahycsicev
     1381 evfnllfvtn esntqktyiv hchdcarkts kslenfvvle qykmedliqv ydqftlalsl
     1441 ssss
//
LOCUS       NP_001387107            1387 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 31 [Homo sapiens].
ACCESSION   NP_001387107 XP_016885556
VERSION     NP_001387107.1
DBSOURCE    REFSEQ: accession NM_001400178.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1387)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1387)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1387)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1387)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1387)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1387)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1387)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1387)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1387)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1387)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2 and AC010877.3.
            
            On Jan 20, 2022 this sequence version replaced XP_016885556.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3597672.1,
                                           SRR18074968.1966094.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1387
                     /product="histone demethylase UTY isoform 31"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=153897
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..440
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1091..1155
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1125..1233
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1387
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001400178.1:369..4532"
                     /note="isoform 31 is encoded by transcript variant 83"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq ngsdnwnggq slshhpvqqv yslcltpqkl qhleqlranr
      481 dnlnpaqkhq leqlesqfvl mqqmrhkeva qvrttgihng aitdsslptn svsnrqphga
      541 ltrvssvsqp gvrpacvekl lssgafsagc ipcgtskilg stdtillgsn ciagsesngn
      601 vpylqqntht lphnhtdlns steepwrkql snsaqglhks qssclsgpne eqplfstgsa
      661 qyhqatstgi kkanehltlp snsvpqgdad shlschtats ggqqgimftk eskpsknrsl
      721 vpetsrhtgd tsngcadvkg lsnhvhqlia davsspnhgd spnlliadnp qlsalligka
      781 ngnvgtgtcd kvnnihpavh tktdhsvass pssaistatp spksteqrsi nsvtslnsph
      841 sglhtvngeg lgksqsstkv dlplashrst sqilpsmsvs icpsstevlk acrnpgkngl
      901 snscilldkc ppprpptspy pplpkdklnp ptpsiylenk rdaffpplhq fctnpknpvt
      961 virglagalk ldlglfstkt lveannehmv evrtqllqpa denwdptgtk kiwrcesnrs
     1021 httiakyaqy qassfqeslr eenekrtqhk dhsdnestss ensgrrrkgp fktikfgtni
     1081 dlsdnkkwkl qlheltklpa farvvsagnl lthvghtilg mntvqlymkv pgsrtpghqe
     1141 nnnfcsvnin igpgdcewfv vpedywgvln dfceknnlnf lmsswwpnle dlyeanvpvy
     1201 rfiqrpgdlv winagtvhwv qavgwcnnia wnvgpltacq yklaveryew nklksvkspv
     1261 pmvhlswnma rnikvsdpkl femikycllk ilkqyqtlre alvaagkevi whgrtndepa
     1321 hycsicevev fnllfvtnes ntqktyivhc hdcarktsks lenfvvleqy kmedliqvyd
     1381 qftlvsh
//
LOCUS       NP_001387099            1530 aa            linear   PRI 07-DEC-2025
DEFINITION  histone demethylase UTY isoform 26 [Homo sapiens].
ACCESSION   NP_001387099 XP_011529751
VERSION     NP_001387099.1
DBSOURCE    REFSEQ: accession NM_001400170.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1530)
  AUTHORS   Cunningham,C.M., Li,M., Ruffenach,G., Doshi,M., Aryan,L., Hong,J.,
            Park,J., Hrncir,H., Medzikovic,L., Umar,S., Arnold,A.P. and
            Eghbali,M.
  TITLE     Y-Chromosome Gene, Uty, Protects Against Pulmonary Hypertension by
            Reducing Proinflammatory Chemokines
  JOURNAL   Am J Respir Crit Care Med 206 (2), 186-196 (2022)
   PUBMED   35504005
  REMARK    GeneRIF: Y-Chromosome Gene, Uty, Protects Against Pulmonary
            Hypertension by Reducing Proinflammatory Chemokines.
REFERENCE   2  (residues 1 to 1530)
  AUTHORS   Pottmeier,P., Doszyn,O., Peuckert,C. and Jazin,E.
  TITLE     Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells
  JOURNAL   Stem Cells Dev 29 (23), 1497-1509 (2020)
   PUBMED   33040644
  REMARK    GeneRIF: Increased Expression of Y-Encoded Demethylases During
            Differentiation of Human Male Neural Stem Cells.
REFERENCE   3  (residues 1 to 1530)
  AUTHORS   Tricarico,R., Nicolas,E., Hall,M.J. and Golemis,E.A.
  TITLE     X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis
  JOURNAL   Clin Cancer Res 26 (21), 5567-5578 (2020)
   PUBMED   32732223
  REMARK    GeneRIF: X- and Y-Linked Chromatin-Modifying Genes as Regulators of
            Sex-Specific Cancer Incidence and Prognosis.
            Review article
REFERENCE   4  (residues 1 to 1530)
  AUTHORS   Fan,Z., Zhao,W., Fan,S., Li,C., Qiao,J. and Xu,Y.
  TITLE     Identification of Potential Biomarkers for Intervertebral Disc
            Degeneration Using the Genome-Wide Expression Analysis
  JOURNAL   J Comput Biol 27 (9), 1341-1349 (2020)
   PUBMED   31904996
  REMARK    GeneRIF: Identification of Potential Biomarkers for Intervertebral
            Disc Degeneration Using the Genome-Wide Expression Analysis.
REFERENCE   5  (residues 1 to 1530)
  AUTHORS   Gazova,I., Lengeling,A. and Summers,K.M.
  TITLE     Lysine demethylases KDM6A and UTY: The X and Y of histone
            demethylation
  JOURNAL   Mol Genet Metab 127 (1), 31-44 (2019)
   PUBMED   31097364
  REMARK    GeneRIF: UTY is co-regulated with KDM6A. UTY compensates for KDM6A
            in eutherian males and is responsible for the association between
            the loss of the Y chromosome and poor prognosis in a range of
            cancers. [review]
            Review article
REFERENCE   6  (residues 1 to 1530)
  AUTHORS   Laaser,I., Theis,F.J., de Angelis,M.H., Kolb,H.J. and Adamski,J.
  TITLE     Huge splicing frequency in human Y chromosomal UTY gene
  JOURNAL   OMICS 15 (3), 141-154 (2011)
   PUBMED   21329462
REFERENCE   7  (residues 1 to 1530)
  AUTHORS   Warren,E.H., Gavin,M.A., Simpson,E., Chandler,P., Page,D.C.,
            Disteche,C., Stankey,K.A., Greenberg,P.D. and Riddell,S.R.
  TITLE     The human UTY gene encodes a novel HLA-B8-restricted H-Y antigen
  JOURNAL   J Immunol 164 (5), 2807-2814 (2000)
   PUBMED   10679124
REFERENCE   8  (residues 1 to 1530)
  AUTHORS   Grbavec,D., Lo,R., Liu,Y., Greenfield,A. and Stifani,S.
  TITLE     Groucho/transducin-like enhancer of split (TLE) family members
            interact with the yeast transcriptional co-repressor SSN6 and
            mammalian SSN6-related proteins: implications for evolutionary
            conservation of transcription repression mechanisms
  JOURNAL   Biochem J 337 (Pt 1) (Pt 1), 13-17 (1999)
   PUBMED   9854018
REFERENCE   9  (residues 1 to 1530)
  AUTHORS   Greenfield,A., Carrel,L., Pennisi,D., Philippe,C., Quaderi,N.,
            Siggers,P., Steiner,K., Tam,P.P., Monaco,A.P., Willard,H.F. and
            Koopman,P.
  TITLE     The UTX gene escapes X inactivation in mice and humans
  JOURNAL   Hum Mol Genet 7 (4), 737-742 (1998)
   PUBMED   9499428
REFERENCE   10 (residues 1 to 1530)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
   PUBMED   9381176
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006376.2, AC010877.3 and
            AC244214.2.
            
            On Jan 20, 2022 this sequence version replaced XP_011529751.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeats which are thought to be involved in protein-protein
            interactions. The encoded protein is also a minor
            histocompatibility antigen which may induce graft rejection of male
            stem cell grafts. A large number of alternatively spliced
            transcripts have been observed for this gene, but the full length
            nature of some of these variants has not been determined. [provided
            by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1074049.1,
                                           SRR18074969.3482727.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1530
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.221"
     Protein         1..1530
                     /product="histone demethylase UTY isoform 26"
                     /EC_number="1.14.11.68"
                     /note="ubiquitously transcribed tetratricopeptide repeat
                     gene, Y chromosome; ubiquitously transcribed TPR gene on Y
                     chromosome; lysine demethylase 6C; histone demethylase
                     UTY; [histone H3]-trimethyl-L-lysine(27) demethylase UTY;
                     ubiquitous TPR motif protein UTY; ubiquitously-transcribed
                     TPR protein on the Y chromosome; ubiquitously-transcribed
                     Y chromosome tetratricopeptide repeat protein;
                     ubiquitously transcribed tetratricopeptide repeat gene,
                     Y-linked"
                     /calculated_mol_wt=169869
     Region          90..118
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(91,94..95,98..99,101,128,131..132,135..136,138..139,
                     162,168..169,172..173,176)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          95..230
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          126..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          161..191
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          168..440
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          202..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          240..275
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(282,285..286,289..290,292,316,319..320,323..324,
                     326..327,350,353..354,357..358,361)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          282..309
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          314..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          349..377
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1091..1155
                     /region_name="JmjC"
                     /note="A domain family that is part of the cupin
                     metalloenzyme superfamily; smart00558"
                     /db_xref="CDD:214721"
     Region          1125..1233
                     /region_name="JmjC"
                     /note="JmjC domain, hydroxylase; pfam02373"
                     /db_xref="CDD:396791"
     CDS             1..1530
                     /gene="UTY"
                     /gene_synonym="KDM6AL; KDM6C; UTY1"
                     /coded_by="NM_001400170.1:369..4961"
                     /note="isoform 26 is encoded by transcript variant 78"
                     /db_xref="GeneID:7404"
                     /db_xref="HGNC:HGNC:12638"
                     /db_xref="MIM:400009"
ORIGIN      
        1 mkscavsltt aavafgdeak kmaegkasre seeesvsltv eerealggmd srlfgfvrlh
       61 edgartktll gkavrcyesl ilkaegkves dffcqlghfn llledyskal sayqryyslq
      121 adywknaafl yglglvyfyy nafhwaikaf qdvlyvdpsf crakeihlrl glmfkvntdy
      181 ksslkhfqla lidcnpctls naeiqfhiah lyetqrkyhs akeayeqllq tenlpaqvka
      241 tvlqqlgwmh hnmdlvgdka tkesyaiqyl qksleadpns gqswyflgrc yssigkvqda
      301 fisyrqsidk seasadtwcs igvlyqqqnq pmdalqayic avqldhghaa awmdlgtlye
      361 scnqpqdaik cylnaarskr csntstlaar ikflqaqlcn lpqsslqnkt kllpsieeaw
      421 slpipaelts rqgamntaqq ngsdnwnggq slshhpvqqv yslcltpqkl qhleqlranr
      481 dnlnpaqkhq leqlesqfvl mqqmrhkeva qvrttgihng aitdsslptn svsnrqphga
      541 ltrvssvsqp gvrpacvekl lssgafsagc ipcgtskilg stdtillgsn ciagsesngn
      601 vpylqqntht lphnhtdlns steepwrkql snsaqglhks qssclsgpne eqplfstgsa
      661 qyhqatstgi kkanehltlp snsvpqgdad shlschtats ggqqgimftk eskpsknrsl
      721 vpetsrhtgd tsngcadvkg lsnhvhqlia davsspnhgd spnlliadnp qlsalligka
      781 ngnvgtgtcd kvnnihpavh tktdhsvass pssaistatp spksteqrsi nsvtslnsph
      841 sglhtvngeg lgksqsstkv dlplashrst sqilpsmsvs icpsstevlk acrnpgkngl
      901 snscilldkc ppprpptspy pplpkdklnp ptpsiylenk rdaffpplhq fctnpknpvt
      961 virglagalk ldlglfstkt lveannehmv evrtqllqpa denwdptgtk kiwrcesnrs
     1021 httiakyaqy qassfqeslr eenekrtqhk dhsdnestss ensgrrrkgp fktikfgtni
     1081 dlsdnkkwkl qlheltklpa farvvsagnl lthvghtilg mntvqlymkv pgsrtpghqe
     1141 nnnfcsvnin igpgdcewfv vpedywgvln dfceknnlnf lmsswwpnle dlyeanvpvy
     1201 rfiqrpgdlv winagtvhwv qavgwcnnia wnvgpltacq yklaveryew nklksvkspv
     1261 pmvhlswnma rnikvsdpkl femikycllk ilkqyqtlre alvaagkevi whgrtndepa
     1321 hycsicevev fnllfvtnes ntqktyivhc hdcarktsks lenfvvleqy kmedliqvyd
     1381 qftlaspwpp mdqsaftssl lrpikalgsg raeqtsgdql qkgathsras sllraaemtr
     1441 rpasreelpd pglfchsikl lfvlfsfhls tflilpcqrr rtwelldgga escktnrant
     1501 piahylvsee erravalqrv qtwellepgl
//
LOCUS       NP_060881               1134 aa            linear   PRI 07-DEC-2025
DEFINITION  lysine-specific demethylase hairless isoform b [Homo sapiens].
ACCESSION   NP_060881
VERSION     NP_060881.2
DBSOURCE    REFSEQ: accession NM_018411.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1134)
  AUTHORS   Saldanha,C., Vieira-Baptista,P., Costa,M., Silva,A.R., Picao,M. and
            Sousa,C.
  TITLE     Impact of a High Coverage Vaccination Rate on Human Papillomavirus
            Infection Prevalence in Young Women: A Cross-sectional Study
  JOURNAL   J Low Genit Tract Dis 24 (4), 363-366 (2020)
   PUBMED   32796265
  REMARK    GeneRIF: Impact of a High Coverage Vaccination Rate on Human
            Papillomavirus Infection Prevalence in Young Women: A
            Cross-sectional Study.
REFERENCE   2  (residues 1 to 1134)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1134)
  AUTHORS   Huang,Y., Cai,C., Ren,L., Cui,C., Zhang,X. and Liu,W.
  TITLE     Marie Unna hereditary hypotrichosis accompanied by multiple
            familial trichoepithelioma in a Chinese family
  JOURNAL   J Dermatol 46 (5), 413-417 (2019)
   PUBMED   30809827
  REMARK    GeneRIF: Study in a large, five-generation Han Chinese family with
            several patients presenting with Marie Unna hereditary
            hypotrichosis (MUHH) and multiple familial trichoepithelioma (MFT)
            revealed that the c.1A>G mutation in HR (U2HR) was present in all
            MUHH patients. No pathogenic variants were found in EPS8L3 or CYLD
            in any family members but FABP12 (rs536105592 G>A) was identified
            in the patients with both MUHH and MFT.
REFERENCE   4  (residues 1 to 1134)
  AUTHORS   Brook,L., Palade,P., Maatough,A., Whitfield,G.K., Emeterio,L.S.,
            Hsieh,D. and Hsieh,J.C.
  TITLE     Hairless regulates p53 target genes to exert tumor suppressive
            functions in glioblastoma
  JOURNAL   J Cell Biochem 120 (1), 533-543 (2019)
   PUBMED   30191601
  REMARK    GeneRIF: These results suggest that transcriptional repression or
            mutation of HR may contribute to glioblastoma pathogenesis, which
            uncovers a role of HR in brain and suggests that modulating HR
            activity in glioblastoma may be a therapeutic strategy.
REFERENCE   5  (residues 1 to 1134)
  AUTHORS   Duzenli,S., Redler,S., Muller,M., Polat,M., Dogruer,D.,
            Pasternack,S.M. and Betz,R.C.
  TITLE     Identification of a U2HR gene mutation in Turkish families with
            Marie Unna hereditary hypotrichosis
  JOURNAL   Clin Exp Dermatol 34 (8), e953-e956 (2009)
   PUBMED   20055871
  REMARK    GeneRIF: the first time that a mutation in U2HR has been identified
            in families from the Middle East
REFERENCE   6  (residues 1 to 1134)
  AUTHORS   Wen,Y., Liu,Y., Xu,Y., Zhao,Y., Hua,R., Wang,K., Sun,M., Li,Y.,
            Yang,S., Zhang,X.J., Kruse,R., Cichon,S., Betz,R.C., Nothen,M.M.,
            van Steensel,M.A., van Geel,M., Steijlen,P.M., Hohl,D., Huber,M.,
            Dunnill,G.S., Kennedy,C., Messenger,A., Munro,C.S., Terrinoni,A.,
            Hovnanian,A., Bodemer,C., de Prost,Y., Paller,A.S., Irvine,A.D.,
            Sinclair,R., Green,J., Shang,D., Liu,Q., Luo,Y., Jiang,L.,
            Chen,H.D., Lo,W.H., McLean,W.H., He,C.D. and Zhang,X.
  TITLE     Loss-of-function mutations of an inhibitory upstream ORF in the
            human hairless transcript cause Marie Unna hereditary hypotrichosis
  JOURNAL   Nat Genet 41 (2), 228-233 (2009)
   PUBMED   19122663
  REMARK    GeneRIF: A pathogenic initiation codon mutation in U2HR, an
            inhibitory upstream ORF in the 5' UTR of the gene encoding the
            human hairless homolog (HR).
            Erratum:[Nat Genet. 2009 Jun;41(6):762]
REFERENCE   7  (residues 1 to 1134)
  AUTHORS   Ahmad,W., Irvine,A.D., Lam,H., Buckley,C., Bingham,E.A.,
            Panteleyev,A.A., Ahmad,M., McGrath,J.A. and Christiano,A.M.
  TITLE     A missense mutation in the zinc-finger domain of the human hairless
            gene underlies congenital atrichia in a family of Irish travellers
  JOURNAL   Am J Hum Genet 63 (4), 984-991 (1998)
   PUBMED   9758627
REFERENCE   8  (residues 1 to 1134)
  AUTHORS   Cichon,S., Anker,M., Vogt,I.R., Rohleder,H., Putzstuck,M.,
            Hillmer,A., Farooq,S.A., Al-Dhafri,K.S., Ahmad,M., Haque,S.,
            Rietschel,M., Propping,P., Kruse,R. and Nothen,M.M.
  TITLE     Cloning, genomic organization, alternative transcripts and
            mutational analysis of the gene responsible for autosomal recessive
            universal congenital alopecia
  JOURNAL   Hum Mol Genet 7 (11), 1671-1679 (1998)
   PUBMED   9736769
  REMARK    Erratum:[Hum Mol Genet 1998 Nov;7(12):1987-8]
REFERENCE   9  (residues 1 to 1134)
  AUTHORS   Nothen,M.M., Cichon,S., Vogt,I.R., Hemmer,S., Kruse,R., Knapp,M.,
            Holler,T., Faiyaz ul Haque,M., Haque,S., Propping,P., Ahmad,M. and
            Rietschel,M.
  TITLE     A gene for universal congenital alopecia maps to chromosome 8p21-22
  JOURNAL   Am J Hum Genet 62 (2), 386-390 (1998)
   PUBMED   9463324
REFERENCE   10 (residues 1 to 1134)
  AUTHORS   Ahmad,W., Faiyaz ul Haque,M., Brancolini,V., Tsou,H.C., ul
            Haque,S., Lam,H., Aita,V.M., Owen,J., deBlaquiere,M., Frank,J.,
            Cserhalmi-Friedman,P.B., Leask,A., McGrath,J.A., Peacocke,M.,
            Ahmad,M., Ott,J. and Christiano,A.M.
  TITLE     Alopecia universalis associated with a mutation in the human
            hairless gene
  JOURNAL   Science 279 (5351), 720-724 (1998)
   PUBMED   9445480
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA114279.1, DA326731.1,
            AJ277165.2, AF039196.3, BM982749.1 and BX109092.1.
            
            On Aug 29, 2002 this sequence version replaced NP_060881.1.
            
            Summary: This gene encodes a protein that is involved in hair
            growth. This protein functions as a transcriptional corepressor of
            multiple nuclear receptors, including thyroid hormone receptor, the
            retinoic acid receptor-related orphan receptors and the vitamin D
            receptors, and it interacts with histone deacetylases. The
            translation of this protein is modulated by a regulatory open
            reading frame (ORF) that exists upstream of the primary ORF.
            Mutations in this upstream ORF cause Marie Unna hereditary
            hypotrichosis (MUHH), an autosomal dominant form of genetic hair
            loss. Mutations in this gene also cause autosomal recessive
            congenital alopecia and atrichia with papular lesions, other
            diseases resulting in hair loss. Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2014].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon, compared to variant 1, resulting in a protein (isoform 2)
            that has a shorter C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record represents the hairless protein
            encoded by the primary ORF. Four upstream ORFs (U1HR-U4HR), which
            may regulate translation of the primary ORF as described in
            PMID:19122663, are also annotated on this sequence.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            regulatory uORF :: PMID: 19122663
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1134
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..1134
                     /product="lysine-specific demethylase hairless isoform b"
                     /EC_number="1.14.11.65"
                     /note="protein hairless; hairless homolog; hair growth
                     associated; lysine-specific demethylase hairless; [histone
                     H3]-dimethyl-L-lysine(9) demethylase hairless; lysine
                     demethylase 3D"
                     /calculated_mol_wt=121727
     Region          598..>625
                     /region_name="FYVE_like_SF"
                     /note="FYVE domain like superfamily; cl28890"
                     /db_xref="CDD:333710"
     Site            order(610..615,620)
                     /site_type="other"
                     /note="phosphatidylinositol 3-phosphate binding site
                     [chemical binding]"
                     /db_xref="CDD:277249"
     CDS             1..1134
                     /gene="HR"
                     /gene_synonym="ALUNC; AU; HSA277165; HYPT4; KDM3D; MUHH;
                     MUHH1"
                     /coded_by="NM_018411.4:666..4070"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6023.1"
                     /db_xref="GeneID:55806"
                     /db_xref="HGNC:HGNC:5172"
                     /db_xref="MIM:602302"
ORIGIN      
        1 mestpsflkg tptwektape ngivrqepgs pprdglhhgp lclgepapfw rgvlstpdsw
       61 lppgfpqgpk dmlplvegeg pqngerkvnw lgskeglrwk eamlthplaf cgpacpprcg
      121 plmpehsggh lksdpvafrp whcpflletk ilerapfwvp tclppylvsg lppehpcdwp
      181 ltphpwvysg gqpkvpsafs lgskgfyykd psiprlakep laaaepglfg lnsgghlqra
      241 geaerpslhq rdgemgagrq qnpcplflgq pdtvpwtswp acppglvhtl gnvwagpgdg
      301 nlgyqlgppa tprcpspepp vtqrgccssy pptkggglgp cgkcqegleg gasgasepse
      361 evnkasgpra cppshhtklk ktwltrhseq fecprgcpev eerpvarlra lkragspevq
      421 gamgspapkr ppdpfpgtae qgaggwqevr dtsignkdvd sgqhdeqkgp qdgqaslqdp
      481 glqdipclal paklaqcqsc aqaagegggh achsqqvrrs plggelqqee dtatnsssee
      541 gpgsgpdsrl stglakhlls glgdrlcrll rrerealawa qregqgpavt edspgiprcc
      601 srchhglfnt hwrcprcshr lcvacgrvag tgrarekagf qeqsaeectq eaghaacslm
      661 ltqfvssqal aelstamhqv wvkfdirghc pcqadarvwa pgdagqqkes tqktpptpqp
      721 scngdthrtk sikeetpdsa etpaedragr gplpcpslce llastavklc lgherihmaf
      781 apvtpalpsd dritnildsi iaqvverkiq ekalgpglra gpglrkglgl plspvrprlp
      841 ppgallwlqe pqpcprrgfh lfqehwrqgq pvlvsgiqrt lqgnlwgtea lgalggqvqa
      901 lsplgppqps slgsttfweg fswpelrpks degsvlllhr algdedtsrv enlaaslplp
      961 eycalhgkln lasylppgla lrplepqlwa aygvsphrgh lgtknlcvev adlvsilvha
     1021 dtplpawhra qkdflsgldg eglwspgsqv stvwhvfraq daqrirrflq mvqglvstvs
     1081 vtqhflspet salsaqlchq gpslppdchl lyaqmdwavf qavkvavgtl qeak
//
LOCUS       NP_001369708             674 aa            linear   PRI 07-DEC-2025
DEFINITION  F-box/LRR-repeat protein 19 isoform 4 [Homo sapiens].
ACCESSION   NP_001369708
VERSION     NP_001369708.1
DBSOURCE    REFSEQ: accession NM_001382779.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   Dong,H., Huang,C. and Huang,J.
  TITLE     FBXL19-AS1 promotes the progression of nasopharyngeal carcinoma by
            acting as a competing endogenous RNA to sponge miR-431 and
            upregulate PBOV1
  JOURNAL   Mol Med Rep 24 (3) (2021)
   PUBMED   34278444
  REMARK    GeneRIF: FBXL19AS1 promotes the progression of nasopharyngeal
            carcinoma by acting as a competing endogenous RNA to sponge miR431
            and upregulate PBOV1.
REFERENCE   2  (residues 1 to 674)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   3  (residues 1 to 674)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 674)
  AUTHORS   Wang,L., Zhang,X., Liu,Y. and Xu,S.
  TITLE     Long noncoding RNA FBXL19-AS1 induces tumor growth and metastasis
            by sponging miR-203a-3p in lung adenocarcinoma
  JOURNAL   J Cell Physiol 235 (4), 3612-3625 (2020)
   PUBMED   31566718
  REMARK    GeneRIF: Long noncoding RNA FBXL19-AS1 induces tumor growth and
            metastasis by sponging miR-203a-3p in lung adenocarcinoma.
REFERENCE   5  (residues 1 to 674)
  AUTHORS   Xu,C., Liu,K., Lei,M., Yang,A., Li,Y., Hughes,T.R. and Min,J.
  TITLE     DNA Sequence Recognition of Human CXXC Domains and Their Structural
            Determinants
  JOURNAL   Structure 26 (1), 85-95 (2018)
   PUBMED   29276034
REFERENCE   6  (residues 1 to 674)
  AUTHORS   Chandran,V.
  TITLE     The genetics of psoriasis and psoriatic arthritis
  JOURNAL   Clin Rev Allergy Immunol 44 (2), 149-156 (2013)
   PUBMED   22274791
  REMARK    Review article
REFERENCE   7  (residues 1 to 674)
  AUTHORS   Stuart,P.E., Nair,R.P., Ellinghaus,E., Ding,J., Tejasvi,T.,
            Gudjonsson,J.E., Li,Y., Weidinger,S., Eberlein,B., Gieger,C.,
            Wichmann,H.E., Kunz,M., Ike,R., Krueger,G.G., Bowcock,A.M.,
            Mrowietz,U., Lim,H.W., Voorhees,J.J., Abecasis,G.R.,
            Weichenthal,M., Franke,A., Rahman,P., Gladman,D.D. and Elder,J.T.
  TITLE     Genome-wide association analysis identifies three psoriasis
            susceptibility loci
  JOURNAL   Nat Genet 42 (11), 1000-1004 (2010)
   PUBMED   20953189
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 674)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   9  (residues 1 to 674)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of FBXL19 gene in silico
  JOURNAL   Int J Mol Med 14 (6), 1109-1114 (2004)
   PUBMED   15547684
REFERENCE   10 (residues 1 to 674)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC135048.2.
            
            Summary: This gene encodes a member of the Skp1-Cullin-F-box family
            of E3 ubiquitin ligases. The encoded protein is reported to bind to
            the transmembrane receptor interleukin 1 receptor-like 1 and
            regulate its ubiquitination and degradation. This protein has been
            linked to the regulation of pulmonary inflammation and psoriasis.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Aug 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4352444.330220.1,
                                           ERR4352443.631166.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000338343.10/ ENSP00000339712.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..674
                     /product="F-box/LRR-repeat protein 19 isoform 4"
                     /note="jumonji C domain-containing histone demethylase 1C;
                     F-box/LRR-repeat protein 19; jumonji C domain-containing
                     1C"
                     /calculated_mol_wt=73640
     Region          <30..57
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          67..128
                     /region_name="PHD_FXL19"
                     /note="PHD finger found in F-box and leucine-rich repeat
                     protein 19 (FBXL19); cd15645"
                     /db_xref="CDD:277115"
     Site            order(67,90..94,98,123)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277115"
     Region          401..443
                     /region_name="F-box_JHDM"
                     /note="F-box domain found in the JmjC domain-containing
                     histone demethylation protein (JHDM) family; cd22122"
                     /db_xref="CDD:438894"
     Site            order(404..405,407..409,411..412,414..416,418..419,
                     422..423,425..427,431)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438894"
     Region          441..465
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          446..645
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          466..488
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          490..513
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          514..553
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          554..578
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          579..603
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          609..633
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          634..666
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..674
                     /gene="FBXL19"
                     /gene_synonym="CXXC11; Fbl19; JHDM1C"
                     /coded_by="NM_001382779.1:913..2937"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS92142.1"
                     /db_xref="GeneID:54620"
                     /db_xref="HGNC:HGNC:25300"
                     /db_xref="MIM:609085"
ORIGIN      
        1 mssssrgpga garrrrtrcr rcracvrtec gdchfcrdmk kfggpgrmkq scllrqctap
       61 vlphtavcll cgeagkedtv egeeekfgls lmecticnei vhpgclkmgk aegvinaeip
      121 ncwecprctq egrtskdsge gpgrrradng eegaslgsgw klteepplpp ppprrkgplp
      181 agpppedvpg ppkrkereag nepptprkkv kggrerhlkk vggdacllrg sdpggpgllp
      241 prvlnpsqaf sschpglppe nwekpkppla saegpavpsp spqreklerf krmcqllerv
      301 pdtsssssds dsdsdssgts lsedeapgea rngrrpargs sgekenrggr ravrpgsggp
      361 llswplgpap pprppqlerh vvrppprspe pdtlplaags dhplpraawl rvfqhlgpre
      421 lcicmrvcrt wsrwcydkrl wprmdlsrrk sltppmlsgv vrrqpraldl swtgvskkql
      481 mwllnrlqgl qelvlsgcsw lsvsalgsap lpalrlldlr wiedvkdsql relllpppdt
      541 kpgqtesrgr lqgvaelrla gleltdaslr lllrhapqls aldlshcahv gdpsvhllta
      601 ptsplretlv hlnlagchrl tdhclplfrr cprlrrldlr scrqlspeac arlaaagppg
      661 pfrcpeekll lkds
//
LOCUS       NP_001508                462 aa            linear   PRI 08-DEC-2025
DEFINITION  general transcription factor IIH subunit 4 [Homo sapiens].
ACCESSION   NP_001508 XP_378195
VERSION     NP_001508.1
DBSOURCE    REFSEQ: accession NM_001517.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Hoag,A., Duan,M. and Mao,P.
  TITLE     The role of Transcription Factor IIH complex in nucleotide excision
            repair
  JOURNAL   Environ Mol Mutagen 65 Suppl 1 (Suppl 1), 72-81 (2024)
   PUBMED   37545038
  REMARK    GeneRIF: The role of Transcription Factor IIH complex in nucleotide
            excision repair.
            Review article
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Zhou,Q. and Sharp,P.A.
  TITLE     Tat-SF1: cofactor for stimulation of transcriptional elongation by
            HIV-1 Tat
  JOURNAL   Science 274 (5287), 605-610 (1996)
   PUBMED   8849451
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Drapkin,R., Le Roy,G., Cho,H., Akoulitchev,S. and Reinberg,D.
  TITLE     Human cyclin-dependent kinase-activating kinase exists in three
            distinct complexes
  JOURNAL   Proc Natl Acad Sci U S A 93 (13), 6488-6493 (1996)
   PUBMED   8692842
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Blau,J., Xiao,H., McCracken,S., O'Hare,P., Greenblatt,J. and
            Bentley,D.
  TITLE     Three functional classes of transcriptional activation domain
  JOURNAL   Mol Cell Biol 16 (5), 2044-2055 (1996)
   PUBMED   8628270
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI460355.1, BC004935.1 and AL669830.9.
            
            On Oct 18, 2004 this sequence version replaced XP_378195.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.84695.1, BC004935.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000259895.9/ ENSP00000259895.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..462
                     /product="general transcription factor IIH subunit 4"
                     /note="TFIIH basal transcription factor complex p52
                     subunit; BTF2 p52; basic transcription factor 2 52 kDa
                     subunit; general transcription factor IIH polypeptide 4;
                     general transcription factor IIH, polypeptide 4, 52kDa"
                     /calculated_mol_wt=52055
     Region          18..460
                     /region_name="tfb2"
                     /note="Transcription factor tfb2; TIGR00625"
                     /db_xref="CDD:273180"
     CDS             1..462
                     /gene="GTF2H4"
                     /gene_synonym="P52; TFB2; TFIIH; XPJ"
                     /coded_by="NM_001517.5:201..1589"
                     /db_xref="CCDS:CCDS34386.1"
                     /db_xref="GeneID:2968"
                     /db_xref="HGNC:HGNC:4658"
                     /db_xref="MIM:601760"
ORIGIN      
        1 mestpsrgln rvhlqcrnlq eflgglspgv ldrlyghpat clavfrelps laknwvmrml
       61 fleqplpqaa valwvkkefs kaqeestgll sglriwhtql lpgglqglil npifrqnlri
      121 allgggkaws ddtsqlgpdk hardvpsldk yaeerwevvl hfmvgspsaa vsqdlaqlls
      181 qaglmkstep geppcitsag fqfllldtpa qlwyfmlqyl qtaqsrgmdl veilsflfql
      241 sfstlgkdys vegmsdslln flqhlrefgl vfqrkrksrr yyptrlainl ssgvsgaggt
      301 vhqpgfivve tnyrlyayte selqialial fsemlyrfpn mvvaqvtres vqqaiasgit
      361 aqqiihflrt rahpvmlkqt pvlpptitdq irlwelerdr lrftegvlyn qflsqvdfel
      421 llaharelgv lvfensakrl mvvtpaghsd vkrfwkrqkh ss
//
LOCUS       NP_001431233             188 aa            linear   PRI 09-DEC-2025
DEFINITION  molybdopterin synthase sulfur carrier subunit large subunit MOCS2B
            [Homo sapiens].
ACCESSION   NP_001431233
VERSION     NP_001431233.1
DBSOURCE    REFSEQ: accession NM_001444304.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    GeneRIF: Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and
            MOCS2.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Suganuma,T., Swanson,S.K., Florens,L., Washburn,M.P. and
            Workman,J.L.
  TITLE     Moco biosynthesis and the ATAC acetyltransferase engage translation
            initiation by inhibiting latent PKR activity
  JOURNAL   J Mol Cell Biol 8 (1), 44-50 (2016)
   PUBMED   26705305
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Edwards,M., Roeper,J., Allgood,C., Chin,R., Santamaria,J., Wong,F.,
            Schwarz,G. and Whitehall,J.
  TITLE     Investigation of molybdenum cofactor deficiency due to MOCS2
            deficiency in a newborn baby
  JOURNAL   Meta Gene 3, 43-49 (2015)
   PUBMED   25709896
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Hahnewald,R., Leimkuhler,S., Vilaseca,A., Acquaviva-Bourdain,C.,
            Lenz,U. and Reiss,J.
  TITLE     A novel MOCS2 mutation reveals coordinated expression of the small
            and large subunit of molybdopterin synthase
  JOURNAL   Mol Genet Metab 89 (3), 210-213 (2006)
   PUBMED   16737835
  REMARK    GeneRIF: There was undisturbed production of both transcripts,
            while Western blot analysis demonstrated that MOCS2B, the large
            subunit, is unstable in the absence of MOCS2A.
REFERENCE   5  (residues 1 to 188)
  AUTHORS   Stallmeyer,B., Drugeon,G., Reiss,J., Haenni,A.L. and Mendel,R.R.
  TITLE     Human molybdopterin synthase gene: identification of a bicistronic
            transcript with overlapping reading frames
  JOURNAL   Am J Hum Genet 64 (3), 698-705 (1999)
   PUBMED   10053003
REFERENCE   6  (residues 1 to 188)
  AUTHORS   Sloan,J., Kinghorn,J.R. and Unkles,S.E.
  TITLE     The two subunits of human molybdopterin synthase: evidence for a
            bicistronic messenger RNA with overlapping reading frames
  JOURNAL   Nucleic Acids Res 27 (3), 854-858 (1999)
   PUBMED   9889283
REFERENCE   7  (residues 1 to 188)
  AUTHORS   Feng,G., Tintrup,H., Kirsch,J., Nichol,M.C., Kuhse,J., Betz,H. and
            Sanes,J.R.
  TITLE     Dual requirement for gephyrin in glycine receptor clustering and
            molybdoenzyme activity
  JOURNAL   Science 282 (5392), 1321-1324 (1998)
   PUBMED   9812897
REFERENCE   8  (residues 1 to 188)
  AUTHORS   Reiss,J., Cohen,N., Dorche,C., Mandel,H., Mendel,R.R.,
            Stallmeyer,B., Zabot,M.T. and Dierks,T.
  TITLE     Mutations in a polycistronic nuclear gene associated with
            molybdenum cofactor deficiency
  JOURNAL   Nat Genet 20 (1), 51-53 (1998)
   PUBMED   9731530
REFERENCE   9  (residues 1 to 188)
  AUTHORS   Misko,A., Mahtani,K., Abbott,J., Schwarz,G. and Atwal,P.
  TITLE     Molybdenum Cofactor Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   34870926
REFERENCE   10 (residues 1 to 188)
  AUTHORS   Krawczak,M., Reiss,J. and Cooper,D.N.
  TITLE     The mutational spectrum of single base-pair substitutions in mRNA
            splice junctions of human genes: causes and consequences
  JOURNAL   Hum Genet 90 (1-2), 41-54 (1992)
   PUBMED   1427786
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008966.9.
            
            Summary: Eukaryotic molybdoenzymes use a unique molybdenum cofactor
            (MoCo) consisting of a pterin, termed molybdopterin, and the
            catalytically active metal molybdenum. MoCo is synthesized from
            precursor Z by the heterodimeric enzyme molybdopterin synthase. The
            large and small subunits of molybdopterin synthase are both encoded
            from this gene by overlapping open reading frames. The proteins
            were initially thought to be encoded from a bicistronic transcript.
            They are now thought to be encoded from monocistronic transcripts.
            Alternatively spliced transcripts have been found for this locus
            that encode the large and small subunits. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14243140.11025350.1,
                                           SRR14478891.1896129.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q11.2"
     Protein         1..188
                     /product="molybdopterin synthase sulfur carrier subunit
                     large subunit MOCS2B"
                     /EC_number="2.8.1.12"
                     /note="molybdenum cofactor biosynthesis protein E"
                     /calculated_mol_wt=20813
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O96007.1)"
     Region          54..177
                     /region_name="MoaE"
                     /note="MoaE family. Members of this family are involved in
                     biosynthesis of the molybdenum cofactor (Moco), an
                     essential cofactor for a diverse group of redox enzymes.
                     Moco biosynthesis is an evolutionarily conserved pathway
                     present in eubacteria, archaea and...; cd00756"
                     /db_xref="CDD:238385"
     Site            order(60,64,69,71..75,77,79,133,142,144,152,156)
                     /site_type="other"
                     /note="MoaE homodimer interface [polypeptide binding]"
                     /db_xref="CDD:238385"
     Site            order(93,95,98,101,105,123,159..160,162,164..166,176)
                     /site_type="other"
                     /note="MoaD interaction [polypeptide binding]"
                     /db_xref="CDD:238385"
     Site            order(159,166)
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:238385"
     CDS             1..188
                     /gene="MOCS2"
                     /gene_synonym="MCBPE; MOCO1; MOCODB; MOCODB1; MPTS"
                     /coded_by="NM_001444304.1:94..660"
                     /note="large subunit MOCS2B is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:4338"
                     /db_xref="HGNC:HGNC:7193"
                     /db_xref="MIM:603708"
ORIGIN      
        1 mssleisssc fsletklpls pplvedsafe psrkdmdeve ekskdvinft aeklsvdevs
       61 qlvisplcga islfvgttrn nfegkkvisl eyeaylpmae nevrkicsdi rqkwpvkhia
      121 vfhrlglvpv seasiiiavs sahraaslea vsyaidtlka kvpiwkkeiy eesstwkgnk
      181 ecfwasns
//
LOCUS       NP_001380963             103 aa            linear   PRI 09-DEC-2025
DEFINITION  SLC35A4 upstream microprotein [Homo sapiens].
ACCESSION   NP_001380963
VERSION     NP_001380963.1
DBSOURCE    REFSEQ: accession NM_001394034.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Rocha,A.L., Pai,V., Perkins,G., Chang,T., Ma,J., De Souza,E.V.,
            Chu,Q., Vaughan,J.M., Diedrich,J.K., Ellisman,M.H. and
            Saghatelian,A.
  TITLE     An Inner Mitochondrial Membrane Microprotein from the SLC35A4
            Upstream ORF Regulates Cellular Metabolism
  JOURNAL   J Mol Biol 436 (10), 168559 (2024)
   PUBMED   38580077
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Andreev,D.E., O'Connor,P.B., Fahey,C., Kenny,E.M., Terenin,I.M.,
            Dmitriev,S.E., Cormican,P., Morris,D.W., Shatsky,I.N. and
            Baranov,P.V.
  TITLE     Translation of 5' leaders is pervasive in genes resistant to eIF2
            repression
  JOURNAL   Elife 4, e03971 (2015)
   PUBMED   25621764
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Vanderperre,B., Lucier,J.F., Bissonnette,C., Motard,J.,
            Tremblay,G., Vanderperre,S., Wisztorski,M., Salzet,M.,
            Boisvert,F.M. and Roucou,X.
  TITLE     Direct detection of alternative open reading frames translation
            products in human significantly expands the proteome
  JOURNAL   PLoS One 8 (8), e70698 (2013)
   PUBMED   23950983
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Schmutz,J., Martin,J., Terry,A., Couronne,O., Grimwood,J.,
            Lowry,S., Gordon,L.A., Scott,D., Xie,G., Huang,W., Hellsten,U.,
            Tran-Gyamfi,M., She,X., Prabhakar,S., Aerts,A., Altherr,M.,
            Bajorek,E., Black,S., Branscomb,E., Caoile,C., Challacombe,J.F.,
            Chan,Y.M., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Grigoriev,I., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Israni,S.,
            Jett,J., Kadner,K., Kimball,H., Kobayashi,A., Lopez,F., Lou,Y.,
            Martinez,D., Medina,C., Morgan,J., Nandkeshwar,R., Noonan,J.P.,
            Pitluck,S., Pollard,M., Predki,P., Priest,J., Ramirez,L.,
            Retterer,J., Rodriguez,A., Rogers,S., Salamov,A., Salazar,A.,
            Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N., Wheeler,J.,
            Wu,K., Yang,J., Dickson,M., Cheng,J.F., Eichler,E.E., Olsen,A.,
            Pennacchio,L.A., Rokhsar,D.S., Richardson,P., Lucas,S.M.,
            Myers,R.M. and Rubin,E.M.
  TITLE     The DNA sequence and comparative analysis of human chromosome 5
  JOURNAL   Nature 431 (7006), 268-274 (2004)
   PUBMED   15372022
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011399.6 and AC116353.2.
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000715679.1/ ENSP00000520497.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.3"
     Protein         1..103
                     /product="SLC35A4 upstream microprotein"
                     /note="SLC35A4 microprotein"
                     /calculated_mol_wt=11002
     Site            62..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (L0R6Q1.1)"
     Region          66..100
                     /region_name="DUF4535"
                     /note="Domain of unknown function (DUF4535); pfam15054"
                     /db_xref="CDD:464473"
     CDS             1..103
                     /gene="LOC131768270"
                     /gene_synonym="SLC35A4-MP"
                     /coded_by="NM_001394034.2:17..328"
                     /db_xref="CCDS:CCDS93794.1"
                     /db_xref="GeneID:131768270"
ORIGIN      
        1 maddkdslpk lkdlaflknq leslqrrved evnsgvgqdg sllsspflkg flagyvvakl
       61 rasavlgfav gtctgiyaaq ayavpnvekt lrdylqllrk gpd
//
LOCUS       NP_001350448             264 aa            linear   PRI 09-DEC-2025
DEFINITION  PDZ domain-containing protein 9 isoform 3 [Homo sapiens].
ACCESSION   NP_001350448
VERSION     NP_001350448.1
DBSOURCE    REFSEQ: accession NM_001363519.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Martin,J., Han,C., Gordon,L.A., Terry,A., Prabhakar,S., She,X.,
            Xie,G., Hellsten,U., Chan,Y.M., Altherr,M., Couronne,O., Aerts,A.,
            Bajorek,E., Black,S., Blumer,H., Branscomb,E., Brown,N.C.,
            Bruno,W.J., Buckingham,J.M., Callen,D.F., Campbell,C.S.,
            Campbell,M.L., Campbell,E.W., Caoile,C., Challacombe,J.F.,
            Chasteen,L.A., Chertkov,O., Chi,H.C., Christensen,M., Clark,L.M.,
            Cohn,J.D., Denys,M., Detter,J.C., Dickson,M.,
            Dimitrijevic-Bussod,M., Escobar,J., Fawcett,J.J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Goodwin,L.A., Grady,D.L., Grigoriev,I., Groza,M., Hammon,N.,
            Hawkins,T., Haydu,L., Hildebrand,C.E., Huang,W., Israni,S.,
            Jett,J., Jewett,P.B., Kadner,K., Kimball,H., Kobayashi,A.,
            Krawczyk,M.C., Leyba,T., Longmire,J.L., Lopez,F., Lou,Y., Lowry,S.,
            Ludeman,T., Manohar,C.F., Mark,G.A., McMurray,K.L., Meincke,L.J.,
            Morgan,J., Moyzis,R.K., Mundt,M.O., Munk,A.C., Nandkeshwar,R.D.,
            Pitluck,S., Pollard,M., Predki,P., Parson-Quintana,B., Ramirez,L.,
            Rash,S., Retterer,J., Ricke,D.O., Robinson,D.L., Rodriguez,A.,
            Salamov,A., Saunders,E.H., Scott,D., Shough,T., Stallings,R.L.,
            Stalvey,M., Sutherland,R.D., Tapia,R., Tesmer,J.G., Thayer,N.,
            Thompson,L.S., Tice,H., Torney,D.C., Tran-Gyamfi,M., Tsai,M.,
            Ulanovsky,L.E., Ustaszewska,A., Vo,N., White,P.S., Williams,A.L.,
            Wills,P.L., Wu,J.R., Wu,K., Yang,J., Dejong,P., Bruce,D.,
            Doggett,N.A., Deaven,L., Schmutz,J., Grimwood,J., Richardson,P.,
            Rokhsar,D.S., Eichler,E.E., Gilna,P., Lucas,S.M., Myers,R.M.,
            Rubin,E.M. and Pennacchio,L.A.
  TITLE     The sequence and analysis of duplication-rich human chromosome 16
  JOURNAL   Nature 432 (7020), 988-994 (2004)
   PUBMED   15616553
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Smolen,C., Myers,S. and Girirajan,S.
  TITLE     16p12.2 Recurrent Deletion
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719193
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092119.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.346002.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000424898.3/ ENSP00000400514.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..264
                     /product="PDZ domain-containing protein 9 isoform 3"
                     /note="PDZ domain-containing protein C16orf65; PDZ
                     domain-containing protein 9"
                     /calculated_mol_wt=29773
     Region          31..109
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     Site            order(39..45,54,57,87,91,94..95)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467153"
     CDS             1..264
                     /gene="PDZD9"
                     /gene_synonym="C16orf65"
                     /coded_by="NM_001363519.1:70..864"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92124.1"
                     /db_xref="GeneID:255762"
                     /db_xref="HGNC:HGNC:28740"
ORIGIN      
        1 mqkashknkk ergvsnkvkt svhnlsktqq tkltvgslgl gliiiqhgpy lqithlirkg
       61 aaandgklqp gdvlisvgha nvlgytlref lqllqhitig tvlqikvyrd finipeewqe
      121 iydlipeakf pvtstpkkie lakdesftss ddnenvdldk rlqyyrypws tvhhparrpi
      181 sisrdwhgyk kknhtisvgk dincdvmihr ddkkevraps pywimvkqdn essssstsst
      241 sdafwledca qveegkaqlv skvg
//
LOCUS       NP_612639                310 aa            linear   PRI 09-DEC-2025
DEFINITION  transcription initiation factor TFIID subunit 8 isoform 1 [Homo
            sapiens].
ACCESSION   NP_612639
VERSION     NP_612639.2
DBSOURCE    REFSEQ: accession NM_138572.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Scheer,E., Luo,J., Bernardini,A., Ruffenach,F., Garnier,J.M.,
            Kolb-Cheynel,I., Gupta,K., Berger,I., Ranish,J. and Tora,L.
  TITLE     TAF8 regions important for TFIID lobe B assembly or for TAF2
            interactions are required for embryonic stem cell survival
  JOURNAL   J Biol Chem 297 (5), 101288 (2021)
   PUBMED   34634302
  REMARK    GeneRIF: TAF8 regions important for TFIID lobe B assembly or for
            TAF2 interactions are required for embryonic stem cell survival.
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 310)
  AUTHORS   El-Saafin,F., Curry,C., Ye,T., Garnier,J.M., Kolb-Cheynel,I.,
            Stierle,M., Downer,N.L., Dixon,M.P., Negroni,L., Berger,I.,
            Thomas,T., Voss,A.K., Dobyns,W., Devys,D. and Tora,L.
  TITLE     Homozygous TAF8 mutation in a patient with intellectual disability
            results in undetectable TAF8 protein, but preserved RNA polymerase
            II transcription
  JOURNAL   Hum Mol Genet 27 (12), 2171-2186 (2018)
   PUBMED   29648665
  REMARK    GeneRIF: TAF8 mutant protein with an unrelated C-terminus. The
            mutant TAF8 protein could not be detected in extracts from the
            patient's fibroblasts, indicating a loss of TAF8 function and that
            the mutation is most likely causative
REFERENCE   6  (residues 1 to 310)
  AUTHORS   Guermah,M., Ge,K., Chiang,C.M. and Roeder,R.G.
  TITLE     The TBN protein, which is essential for early embryonic mouse
            development, is an inducible TAFII implicated in adipogenesis
  JOURNAL   Mol Cell 12 (4), 991-1001 (2003)
   PUBMED   14580349
REFERENCE   7  (residues 1 to 310)
  AUTHORS   Tora,L.
  TITLE     A unified nomenclature for TATA box binding protein
            (TBP)-associated factors (TAFs) involved in RNA polymerase II
            transcription
  JOURNAL   Genes Dev 16 (6), 673-675 (2002)
   PUBMED   11963920
REFERENCE   8  (residues 1 to 310)
  AUTHORS   Guermah,M., Tao,Y. and Roeder,R.G.
  TITLE     Positive and negative TAF(II) functions that suggest a dynamic
            TFIID structure and elicit synergy with traps in activator-induced
            transcription
  JOURNAL   Mol Cell Biol 21 (20), 6882-6894 (2001)
   PUBMED   11564872
REFERENCE   9  (residues 1 to 310)
  AUTHORS   Purrello,M., Di Pietro,C., Viola,A., Rapisarda,A., Stevens,S.,
            Guermah,M., Tao,Y., Bonaiuto,C., Arcidiacono,A., Messina,A.,
            Sichel,G., Grzeschik,K.H. and Roeder,R.
  TITLE     Genomics and transcription analysis of human TFIID
  JOURNAL   Oncogene 16 (12), 1633-1638 (1998)
   PUBMED   9569032
REFERENCE   10 (residues 1 to 310)
  AUTHORS   Falik Zaccai,T.C. and Mesika,A.
  TITLE     TAF8-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41343687
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI828714.1, AF465841.1 and
            AL512274.9.
            
            On May 31, 2006 this sequence version replaced NP_612639.1.
            
            Summary: This gene encodes one of several TATA-binding protein
            (TBP)-associated factors (TAFs), which are integral subunits of the
            general transcription factor complex TFIID. TFIID recognizes the
            core promoter of many genes and nucleates the assembly of a
            transcription preinitiation complex containing RNA polymerase II
            and other initiation factors. The protein encoded by this gene
            contains an H4-like histone fold domain, and interacts with several
            subunits of TFIID including TBP and the histone-fold protein TAF10.
            Alternatively spliced transcript variants have been described, but
            their biological validity has not been determined. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.214491.1,
                                           SRR1803614.40703.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372977.8/ ENSP00000362068.3
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..310
                     /product="transcription initiation factor TFIID subunit 8
                     isoform 1"
                     /note="TATA box binding protein (TBP)-associated factor,
                     RNA polymerase II, A, 45/50kDa; TBP-associated factor 8;
                     TBP-associated factor, RNA polymerase II, 43 kD;
                     transcription initiation factor TFIID subunit 8;
                     TBP-associated factor TAFII43; hTAFII43; protein taube
                     nuss; TBP-associated factor 43 kDa; transcription
                     initiation factor TFIID 43 kDa subunit; taube nuss
                     homolog; TAF8 RNA polymerase II, TATA box binding protein
                     (TBP)-associated factor, 43kDa"
                     /calculated_mol_wt=34131
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Region          32..115
                     /region_name="HFD_TAF8"
                     /note="histone-fold domain found in transcription
                     initiation factor TFIID subunit 8 (TAF8) and similar
                     proteins; cd22918"
                     /db_xref="CDD:467043"
     Site            order(32,42,50..53,77,79,81..82,85,89,99)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467043"
     Site            order(33,36..37,40..41,43..45,48..51,54,56..57,60..61,
                     64..66,68..70,72..74,76..77,80,88..90,93..94,97,102,104,
                     106..108,110..115)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467043"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Region          144..197
                     /region_name="TAF8"
                     /note="TATA Binding Protein (TBP) Associated Factor 8;
                     cd08049"
                     /db_xref="CDD:176263"
     Region          262..310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Region          294..307
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     CDS             1..310
                     /gene="TAF8"
                     /gene_synonym="II; NEDMLHB; TAF; TAF(II)43; TAFII-43;
                     TAFII43; TBN"
                     /coded_by="NM_138572.3:19..951"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43462.1"
                     /db_xref="GeneID:129685"
                     /db_xref="HGNC:HGNC:17300"
                     /db_xref="MIM:609514"
ORIGIN      
        1 madaaataga ggsgtrsgsk qstnpadnyh larrrtlqvv vssllteagf esaekasvet
       61 ltemlqsyis eigrsaksyc ehtartqptl sdivvtlvem gfnvdtlpay akrsqrmvit
      121 appvtnqpvt pkaltagqnr phpphipshf pefpdphtyi ktptyrepvs dyqvlrekaa
      181 sqrrdveral trfmaktget qslfkddvst fpliaarpft ipyltallps elemqqmeet
      241 dsseqdeqtd tenlalhism edsgaekent svlqqnpsls gsrngeenii dnpylrpvkk
      301 pkirrkksls
//
LOCUS       NP_001397836             311 aa            linear   PRI 09-DEC-2025
DEFINITION  transcription initiation factor TFIID subunit 8 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001397836 XP_047274132
VERSION     NP_001397836.1
DBSOURCE    REFSEQ: accession NM_001410907.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Scheer,E., Luo,J., Bernardini,A., Ruffenach,F., Garnier,J.M.,
            Kolb-Cheynel,I., Gupta,K., Berger,I., Ranish,J. and Tora,L.
  TITLE     TAF8 regions important for TFIID lobe B assembly or for TAF2
            interactions are required for embryonic stem cell survival
  JOURNAL   J Biol Chem 297 (5), 101288 (2021)
   PUBMED   34634302
  REMARK    GeneRIF: TAF8 regions important for TFIID lobe B assembly or for
            TAF2 interactions are required for embryonic stem cell survival.
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 311)
  AUTHORS   El-Saafin,F., Curry,C., Ye,T., Garnier,J.M., Kolb-Cheynel,I.,
            Stierle,M., Downer,N.L., Dixon,M.P., Negroni,L., Berger,I.,
            Thomas,T., Voss,A.K., Dobyns,W., Devys,D. and Tora,L.
  TITLE     Homozygous TAF8 mutation in a patient with intellectual disability
            results in undetectable TAF8 protein, but preserved RNA polymerase
            II transcription
  JOURNAL   Hum Mol Genet 27 (12), 2171-2186 (2018)
   PUBMED   29648665
  REMARK    GeneRIF: TAF8 mutant protein with an unrelated C-terminus. The
            mutant TAF8 protein could not be detected in extracts from the
            patient's fibroblasts, indicating a loss of TAF8 function and that
            the mutation is most likely causative
REFERENCE   6  (residues 1 to 311)
  AUTHORS   Guermah,M., Ge,K., Chiang,C.M. and Roeder,R.G.
  TITLE     The TBN protein, which is essential for early embryonic mouse
            development, is an inducible TAFII implicated in adipogenesis
  JOURNAL   Mol Cell 12 (4), 991-1001 (2003)
   PUBMED   14580349
REFERENCE   7  (residues 1 to 311)
  AUTHORS   Tora,L.
  TITLE     A unified nomenclature for TATA box binding protein
            (TBP)-associated factors (TAFs) involved in RNA polymerase II
            transcription
  JOURNAL   Genes Dev 16 (6), 673-675 (2002)
   PUBMED   11963920
REFERENCE   8  (residues 1 to 311)
  AUTHORS   Guermah,M., Tao,Y. and Roeder,R.G.
  TITLE     Positive and negative TAF(II) functions that suggest a dynamic
            TFIID structure and elicit synergy with traps in activator-induced
            transcription
  JOURNAL   Mol Cell Biol 21 (20), 6882-6894 (2001)
   PUBMED   11564872
REFERENCE   9  (residues 1 to 311)
  AUTHORS   Purrello,M., Di Pietro,C., Viola,A., Rapisarda,A., Stevens,S.,
            Guermah,M., Tao,Y., Bonaiuto,C., Arcidiacono,A., Messina,A.,
            Sichel,G., Grzeschik,K.H. and Roeder,R.
  TITLE     Genomics and transcription analysis of human TFIID
  JOURNAL   Oncogene 16 (12), 1633-1638 (1998)
   PUBMED   9569032
REFERENCE   10 (residues 1 to 311)
  AUTHORS   Falik Zaccai,T.C. and Mesika,A.
  TITLE     TAF8-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41343687
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513008.14 and AL512274.9.
            
            On Aug 17, 2022 this sequence version replaced XP_047274132.1.
            
            Summary: This gene encodes one of several TATA-binding protein
            (TBP)-associated factors (TAFs), which are integral subunits of the
            general transcription factor complex TFIID. TFIID recognizes the
            core promoter of many genes and nucleates the assembly of a
            transcription preinitiation complex containing RNA polymerase II
            and other initiation factors. The protein encoded by this gene
            contains an H4-like histone fold domain, and interacts with several
            subunits of TFIID including TBP and the histone-fold protein TAF10.
            Alternatively spliced transcript variants have been described, but
            their biological validity has not been determined. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC119679.1, SRR14038197.1176270.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145122
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..311
                     /product="transcription initiation factor TFIID subunit 8
                     isoform 3"
                     /note="TATA box binding protein (TBP)-associated factor,
                     RNA polymerase II, A, 45/50kDa; TBP-associated factor 8;
                     TBP-associated factor, RNA polymerase II, 43 kD;
                     transcription initiation factor TFIID subunit 8;
                     TBP-associated factor TAFII43; hTAFII43; protein taube
                     nuss; TBP-associated factor 43 kDa; transcription
                     initiation factor TFIID 43 kDa subunit; taube nuss
                     homolog; TAF8 RNA polymerase II, TATA box binding protein
                     (TBP)-associated factor, 43kDa"
                     /calculated_mol_wt=34305
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Region          32..115
                     /region_name="HFD_TAF8"
                     /note="histone-fold domain found in transcription
                     initiation factor TFIID subunit 8 (TAF8) and similar
                     proteins; cd22918"
                     /db_xref="CDD:467043"
     Site            order(32,42,50..53,77,79,81..82,85,89,99)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467043"
     Site            order(33,36..37,40..41,43..45,48..51,54,56..57,60..61,
                     64..66,68..70,72..74,76..77,80,88..90,93..94,97,102,104,
                     106..108,110..115)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467043"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Region          144..197
                     /region_name="TAF8"
                     /note="TATA Binding Protein (TBP) Associated Factor 8;
                     cd08049"
                     /db_xref="CDD:176263"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Region          294..307
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     CDS             1..311
                     /gene="TAF8"
                     /gene_synonym="II; NEDMLHB; TAF; TAF(II)43; TAFII-43;
                     TAFII43; TBN"
                     /coded_by="NM_001410907.1:19..954"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS93919.1"
                     /db_xref="GeneID:129685"
                     /db_xref="HGNC:HGNC:17300"
                     /db_xref="MIM:609514"
ORIGIN      
        1 madaaataga ggsgtrsgsk qstnpadnyh larrrtlqvv vssllteagf esaekasvet
       61 ltemlqsyis eigrsaksyc ehtartqptl sdivvtlvem gfnvdtlpay akrsqrmvit
      121 appvtnqpvt pkaltagqnr phpphipshf pefpdphtyi ktptyrepvs dyqvlrekaa
      181 sqrrdveral trfmaktget qslfkddvst fpliaarpft ipyltallps elemqqmeet
      241 dsseqdeqtd tenlalhism edsgaekent svlqqnpsls gsrngeenii dnpylrpvkk
      301 pkirrkkpdt f
//
LOCUS       NP_001244964             672 aa            linear   PRI 09-DEC-2025
DEFINITION  DNA-directed RNA polymerase III subunit RPC5 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001244964
VERSION     NP_001244964.1
DBSOURCE    REFSEQ: accession NM_001258035.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   3  (residues 1 to 672)
  AUTHORS   Ramsay,E.P., Abascal-Palacios,G., Daiss,J.L., King,H., Gouge,J.,
            Pilsl,M., Beuron,F., Morris,E., Gunkel,P., Engel,C. and Vannini,A.
  TITLE     Structure of human RNA polymerase III
  JOURNAL   Nat Commun 11 (1), 6409 (2020)
   PUBMED   33335104
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 672)
  AUTHORS   Ramanathan,A., Weintraub,M., Orlovetskie,N., Serruya,R., Mani,D.,
            Marcu,O., Stepensky,P., Weisblum,Y., Djian,E., Shaag,A.,
            Revel-Vilk,S., Fried,I., Kotler,M., Rouvinski,A., Wolf,D.,
            Elpeleg,O. and Jarrous,N.
  TITLE     A mutation in POLR3E impairs antiviral immune response and RNA
            polymerase III
  JOURNAL   Proc Natl Acad Sci U S A 117 (36), 22113-22121 (2020)
   PUBMED   32843346
  REMARK    GeneRIF: A mutation in POLR3E impairs antiviral immune response and
            RNA polymerase III.
REFERENCE   5  (residues 1 to 672)
  AUTHORS   Carter-Timofte,M.E., Hansen,A.F., Christiansen,M., Paludan,S.R. and
            Mogensen,T.H.
  TITLE     Mutations in RNA Polymerase III genes and defective DNA sensing in
            adults with varicella-zoster virus CNS infection
  JOURNAL   Genes Immun 20 (3), 214-223 (2019)
   PUBMED   29728610
  REMARK    GeneRIF: Mutations in the coding region of POLR3E cause impaired
            expression of antiviral cytokines and susceptibility to
            varicella-zoster virus CNS infection.
REFERENCE   6  (residues 1 to 672)
  AUTHORS   Renaud,M., Praz,V., Vieu,E., Florens,L., Washburn,M.P., l'Hote,P.
            and Hernandez,N.
  TITLE     Gene duplication and neofunctionalization: POLR3G and POLR3GL
  JOURNAL   Genome Res 24 (1), 37-51 (2014)
   PUBMED   24107381
REFERENCE   7  (residues 1 to 672)
  AUTHORS   Hu,P., Wu,S., Sun,Y., Yuan,C.C., Kobayashi,R., Myers,M.P. and
            Hernandez,N.
  TITLE     Characterization of human RNA polymerase III identifies orthologues
            for Saccharomyces cerevisiae RNA polymerase III subunits
  JOURNAL   Mol Cell Biol 22 (22), 8044-8055 (2002)
   PUBMED   12391170
  REMARK    GeneRIF: Data describe the purification and identification of RNA
            polymerase III subunits RPC2 and RPC5.
REFERENCE   8  (residues 1 to 672)
  AUTHORS   Smolen,C., Myers,S. and Girirajan,S.
  TITLE     16p12.2 Recurrent Deletion
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719193
REFERENCE   9  (residues 1 to 672)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB047155.1, AK023231.1, AK001371.1, AK222671.1, AA282721.1,
            AC092338.4 and AW205673.1.
            
            Transcript Variant: This variant (3) lacks an exon in the 5' region
            compared to variant 1, which results in translation initiation from
            an in-frame downstream AUG, and an isoform (3) with a shorter
            N-terminus compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK023231.1, SRR18074967.1674796.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..672
                     /product="DNA-directed RNA polymerase III subunit RPC5
                     isoform 3"
                     /note="RNA polymerase III 80 kDa subunit RPC5;
                     DNA-directed RNA polymerase III subunit RPC5; RNA
                     polymerase III subunit C5; DNA-directed RNA polymerase III
                     80 kDa polypeptide; polymerase (RNA) III (DNA directed)
                     polypeptide E (80kD); polymerase (RNA) III subunit E"
                     /calculated_mol_wt=75643
     Region          1..396
                     /region_name="RPC5"
                     /note="RPC5 protein; pfam04801"
                     /db_xref="CDD:461434"
     Region          407..672
                     /region_name="RPC5_C"
                     /note="DNA-directed RNA polymerase III subunit RPC5
                     C-terminal; pfam19725"
                     /db_xref="CDD:466161"
     CDS             1..672
                     /gene="POLR3E"
                     /gene_synonym="C37; RPC5; SIN"
                     /coded_by="NM_001258035.2:202..2220"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS73845.1"
                     /db_xref="GeneID:55718"
                     /db_xref="HGNC:HGNC:30347"
                     /db_xref="MIM:617815"
ORIGIN      
        1 mtyddiphls akikpkqqkv elemaidtln pnycrskgeq ialnvdgaca detstysskl
       61 mdkqtfcssq ttsntsryaa alyrqgelhl tplhgilqlr psfsyldkad akhrereaan
      121 eagdssqdea eddvkqitvr fsrpeseqar qrrvqsyefl qkkhaeepwv hlhyyglrds
      181 rseherqyll cpgssgvent elvkspseyl mmlmppsqee ekdkpvapsn vlsmaqlrtl
      241 pladqikilm knvkvmpfan lmsllgpsid svavlrgiqk vamlvqgnwv vksdilypkd
      301 sssphsgvpa evlcrgrdfv mwkftqsrwv vrkevatvtk lcaedvkdfl ehmavvrink
      361 gwefilpydg efikkhpdvv qrqhmlwtgi qaklekvynl vketmpkkpd aqsgpaglvc
      421 gdqriqvakt kaqqnhalle relqrrkeql rvpavppgvr ikeepvseeg eedeeqeaee
      481 epmdtspsgl hsklanglpl graagtdsfn ghppqgcast pvarelkafv eatfqrqfvl
      541 tlselkrlfn lhlaslppgh tlfsgisdrm lqdtvlaagc kqilvpfppq taaspdeqkv
      601 falwesgdms dqhrqvllei fsknyrvrrn miqsrltqec gedlskqevd kvlkdccvsy
      661 ggmwylkgtv qs
//
LOCUS       NP_001425509             338 aa            linear   PRI 09-DEC-2025
DEFINITION  transcription initiation factor TFIID subunit 8 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001425509 XP_047274130 XP_054210182
VERSION     NP_001425509.1
DBSOURCE    REFSEQ: accession NM_001438580.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Scheer,E., Luo,J., Bernardini,A., Ruffenach,F., Garnier,J.M.,
            Kolb-Cheynel,I., Gupta,K., Berger,I., Ranish,J. and Tora,L.
  TITLE     TAF8 regions important for TFIID lobe B assembly or for TAF2
            interactions are required for embryonic stem cell survival
  JOURNAL   J Biol Chem 297 (5), 101288 (2021)
   PUBMED   34634302
  REMARK    GeneRIF: TAF8 regions important for TFIID lobe B assembly or for
            TAF2 interactions are required for embryonic stem cell survival.
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 338)
  AUTHORS   El-Saafin,F., Curry,C., Ye,T., Garnier,J.M., Kolb-Cheynel,I.,
            Stierle,M., Downer,N.L., Dixon,M.P., Negroni,L., Berger,I.,
            Thomas,T., Voss,A.K., Dobyns,W., Devys,D. and Tora,L.
  TITLE     Homozygous TAF8 mutation in a patient with intellectual disability
            results in undetectable TAF8 protein, but preserved RNA polymerase
            II transcription
  JOURNAL   Hum Mol Genet 27 (12), 2171-2186 (2018)
   PUBMED   29648665
  REMARK    GeneRIF: TAF8 mutant protein with an unrelated C-terminus. The
            mutant TAF8 protein could not be detected in extracts from the
            patient's fibroblasts, indicating a loss of TAF8 function and that
            the mutation is most likely causative
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Guermah,M., Ge,K., Chiang,C.M. and Roeder,R.G.
  TITLE     The TBN protein, which is essential for early embryonic mouse
            development, is an inducible TAFII implicated in adipogenesis
  JOURNAL   Mol Cell 12 (4), 991-1001 (2003)
   PUBMED   14580349
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Tora,L.
  TITLE     A unified nomenclature for TATA box binding protein
            (TBP)-associated factors (TAFs) involved in RNA polymerase II
            transcription
  JOURNAL   Genes Dev 16 (6), 673-675 (2002)
   PUBMED   11963920
REFERENCE   8  (residues 1 to 338)
  AUTHORS   Guermah,M., Tao,Y. and Roeder,R.G.
  TITLE     Positive and negative TAF(II) functions that suggest a dynamic
            TFIID structure and elicit synergy with traps in activator-induced
            transcription
  JOURNAL   Mol Cell Biol 21 (20), 6882-6894 (2001)
   PUBMED   11564872
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Purrello,M., Di Pietro,C., Viola,A., Rapisarda,A., Stevens,S.,
            Guermah,M., Tao,Y., Bonaiuto,C., Arcidiacono,A., Messina,A.,
            Sichel,G., Grzeschik,K.H. and Roeder,R.
  TITLE     Genomics and transcription analysis of human TFIID
  JOURNAL   Oncogene 16 (12), 1633-1638 (1998)
   PUBMED   9569032
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Falik Zaccai,T.C. and Mesika,A.
  TITLE     TAF8-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41343687
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513008.14 and AL512274.9.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047274130.1, XP_054210182.1.
            
            Summary: This gene encodes one of several TATA-binding protein
            (TBP)-associated factors (TAFs), which are integral subunits of the
            general transcription factor complex TFIID. TFIID recognizes the
            core promoter of many genes and nucleates the assembly of a
            transcription preinitiation complex containing RNA polymerase II
            and other initiation factors. The protein encoded by this gene
            contains an H4-like histone fold domain, and interacts with several
            subunits of TFIID including TBP and the histone-fold protein TAF10.
            Alternatively spliced transcript variants have been described, but
            their biological validity has not been determined. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK057383.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153946, SAMEA2158188
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..338
                     /product="transcription initiation factor TFIID subunit 8
                     isoform 5"
                     /note="TATA box binding protein (TBP)-associated factor,
                     RNA polymerase II, A, 45/50kDa; TBP-associated factor 8;
                     TBP-associated factor, RNA polymerase II, 43 kD;
                     transcription initiation factor TFIID subunit 8;
                     TBP-associated factor TAFII43; hTAFII43; protein taube
                     nuss; TBP-associated factor 43 kDa; transcription
                     initiation factor TFIID 43 kDa subunit; taube nuss
                     homolog; TAF8 RNA polymerase II, TATA box binding protein
                     (TBP)-associated factor, 43kDa"
                     /calculated_mol_wt=37280
     Region          32..115
                     /region_name="HFD_TAF8"
                     /note="histone-fold domain found in transcription
                     initiation factor TFIID subunit 8 (TAF8) and similar
                     proteins; cd22918"
                     /db_xref="CDD:467043"
     Site            order(32,42,50..53,77,79,81..82,85,89,99)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467043"
     Site            order(33,36..37,40..41,43..45,48..51,54,56..57,60..61,
                     64..66,68..70,72..74,76..77,80,88..90,93..94,97,102,104,
                     106..108,110..115)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467043"
     Region          144..197
                     /region_name="TAF8"
                     /note="TATA Binding Protein (TBP) Associated Factor 8;
                     cd08049"
                     /db_xref="CDD:176263"
     CDS             1..338
                     /gene="TAF8"
                     /gene_synonym="II; NEDMLHB; TAF; TAF(II)43; TAFII-43;
                     TAFII43; TBN"
                     /coded_by="NM_001438580.1:19..1035"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:129685"
                     /db_xref="HGNC:HGNC:17300"
                     /db_xref="MIM:609514"
ORIGIN      
        1 madaaataga ggsgtrsgsk qstnpadnyh larrrtlqvv vssllteagf esaekasvet
       61 ltemlqsyis eigrsaksyc ehtartqptl sdivvtlvem gfnvdtlpay akrsqrmvit
      121 appvtnqpvt pkaltagqnr phpphipshf pefpdphtyi ktptyrepvs dyqvlrekaa
      181 sqrrdveral trfmaktget qslfkddvst fpliaarpft ipyltallps elemqqmeet
      241 dsseqdeqtd tenlalhism iesrsvtqag vqwqdlgslq ppppgfkrfs slsllsswny
      301 rrileprrrt plscsrtppc rvagmgrrts sitlicgr
//
LOCUS       NP_789776                 88 aa            linear   PRI 09-DEC-2025
DEFINITION  molybdopterin synthase sulfur carrier subunit small subunit MOCS2A
            [Homo sapiens].
ACCESSION   NP_789776
VERSION     NP_789776.1
DBSOURCE    REFSEQ: accession NM_176806.4
KEYWORDS    RefSeq; MANE Plus Clinical.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 88)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    GeneRIF: Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and
            MOCS2.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 88)
  AUTHORS   Suganuma,T., Swanson,S.K., Florens,L., Washburn,M.P. and
            Workman,J.L.
  TITLE     Moco biosynthesis and the ATAC acetyltransferase engage translation
            initiation by inhibiting latent PKR activity
  JOURNAL   J Mol Cell Biol 8 (1), 44-50 (2016)
   PUBMED   26705305
REFERENCE   3  (residues 1 to 88)
  AUTHORS   Edwards,M., Roeper,J., Allgood,C., Chin,R., Santamaria,J., Wong,F.,
            Schwarz,G. and Whitehall,J.
  TITLE     Investigation of molybdenum cofactor deficiency due to MOCS2
            deficiency in a newborn baby
  JOURNAL   Meta Gene 3, 43-49 (2015)
   PUBMED   25709896
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 88)
  AUTHORS   Hahnewald,R., Leimkuhler,S., Vilaseca,A., Acquaviva-Bourdain,C.,
            Lenz,U. and Reiss,J.
  TITLE     A novel MOCS2 mutation reveals coordinated expression of the small
            and large subunit of molybdopterin synthase
  JOURNAL   Mol Genet Metab 89 (3), 210-213 (2006)
   PUBMED   16737835
  REMARK    GeneRIF: There was undisturbed production of both transcripts,
            while Western blot analysis demonstrated that MOCS2B, the large
            subunit, is unstable in the absence of MOCS2A.
REFERENCE   5  (residues 1 to 88)
  AUTHORS   Stallmeyer,B., Drugeon,G., Reiss,J., Haenni,A.L. and Mendel,R.R.
  TITLE     Human molybdopterin synthase gene: identification of a bicistronic
            transcript with overlapping reading frames
  JOURNAL   Am J Hum Genet 64 (3), 698-705 (1999)
   PUBMED   10053003
REFERENCE   6  (residues 1 to 88)
  AUTHORS   Sloan,J., Kinghorn,J.R. and Unkles,S.E.
  TITLE     The two subunits of human molybdopterin synthase: evidence for a
            bicistronic messenger RNA with overlapping reading frames
  JOURNAL   Nucleic Acids Res 27 (3), 854-858 (1999)
   PUBMED   9889283
REFERENCE   7  (residues 1 to 88)
  AUTHORS   Feng,G., Tintrup,H., Kirsch,J., Nichol,M.C., Kuhse,J., Betz,H. and
            Sanes,J.R.
  TITLE     Dual requirement for gephyrin in glycine receptor clustering and
            molybdoenzyme activity
  JOURNAL   Science 282 (5392), 1321-1324 (1998)
   PUBMED   9812897
REFERENCE   8  (residues 1 to 88)
  AUTHORS   Reiss,J., Cohen,N., Dorche,C., Mandel,H., Mendel,R.R.,
            Stallmeyer,B., Zabot,M.T. and Dierks,T.
  TITLE     Mutations in a polycistronic nuclear gene associated with
            molybdenum cofactor deficiency
  JOURNAL   Nat Genet 20 (1), 51-53 (1998)
   PUBMED   9731530
REFERENCE   9  (residues 1 to 88)
  AUTHORS   Misko,A., Mahtani,K., Abbott,J., Schwarz,G. and Atwal,P.
  TITLE     Molybdenum Cofactor Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   34870926
REFERENCE   10 (residues 1 to 88)
  AUTHORS   Krawczak,M., Reiss,J. and Cooper,D.N.
  TITLE     The mutational spectrum of single base-pair substitutions in mRNA
            splice junctions of human genes: causes and consequences
  JOURNAL   Hum Genet 90 (1-2), 41-54 (1992)
   PUBMED   1427786
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC095417.1, AC008966.9 and
            CB050849.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Eukaryotic molybdoenzymes use a unique molybdenum cofactor
            (MoCo) consisting of a pterin, termed molybdopterin, and the
            catalytically active metal molybdenum. MoCo is synthesized from
            precursor Z by the heterodimeric enzyme molybdopterin synthase. The
            large and small subunits of molybdopterin synthase are both encoded
            from this gene by overlapping open reading frames. The proteins
            were initially thought to be encoded from a bicistronic transcript.
            They are now thought to be encoded from monocistronic transcripts.
            Alternatively spliced transcripts have been found for this locus
            that encode the large and small subunits. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) has an alternate splice site
            in the 5' region, as compared to variant 3. This variant encodes
            the small subunit MOCS2A, also called MOCO1-A, which is derived
            from the upstream ORF and is supported by PMID 16737835.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            CCDS Note: This CCDS ID represents the protein described in PMIDs:
            10053003, 16737835  and 9889283. This transcript is supported by
            BC095417.1. It should be noted this transcript is predicted to
            undergo nonsense-mediated mRNA decay (NMD). However, the protein is
            represented because it was detected endogenously in PMID: 10053003
            and 16737835.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.212050.1,
                                           SRR1803612.23549.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155550 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match :: ENST00000450852.8/ ENSP00000411022.3
            NMD candidate      :: PMID: 16737835
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..88
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q11.2"
     Protein         1..88
                     /product="molybdopterin synthase sulfur carrier subunit
                     small subunit MOCS2A"
                     /EC_number="2.8.1.12"
                     /note="molybdenum cofactor biosynthesis protein E"
                     /calculated_mol_wt=9624
     Region          7..88
                     /region_name="Ubl_MoaD"
                     /note="ubiquitin-like (Ubl) domain found in molybdenum
                     cofactor biosynthesis protein D (MoaD) and similar
                     proteins; cd00754"
                     /db_xref="CDD:340452"
     Site            order(12..13,53,55..56,58,61..64,82..88)
                     /site_type="other"
                     /note="MoaD-MoeB interaction site [polypeptide binding]"
                     /db_xref="CDD:340452"
     Site            order(12..13,60..62,78,83..88)
                     /site_type="other"
                     /note="MoaD-MoaE interaction site [polypeptide binding]"
                     /db_xref="CDD:340452"
     Site            order(12..13,61..62,84..88)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:340452"
     Site            88
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:340452"
     CDS             1..88
                     /gene="MOCS2"
                     /gene_synonym="MCBPE; MOCO1; MOCODB; MOCODB1; MPTS"
                     /coded_by="NM_176806.4:29..295"
                     /note="small subunit MOCS2A is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS47205.1"
                     /db_xref="GeneID:4338"
                     /db_xref="HGNC:HGNC:7193"
                     /db_xref="MIM:603708"
ORIGIN      
        1 mvplcqvevl yfaksaeitg vrsetisvpq eikalqlwke ietrhpglad vrnqiifavr
       61 qeyvelgdql lvlqpgdeia vippisgg
//
LOCUS       NP_001244962             687 aa            linear   PRI 09-DEC-2025
DEFINITION  DNA-directed RNA polymerase III subunit RPC5 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001244962
VERSION     NP_001244962.1
DBSOURCE    REFSEQ: accession NM_001258033.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   3  (residues 1 to 687)
  AUTHORS   Ramsay,E.P., Abascal-Palacios,G., Daiss,J.L., King,H., Gouge,J.,
            Pilsl,M., Beuron,F., Morris,E., Gunkel,P., Engel,C. and Vannini,A.
  TITLE     Structure of human RNA polymerase III
  JOURNAL   Nat Commun 11 (1), 6409 (2020)
   PUBMED   33335104
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 687)
  AUTHORS   Ramanathan,A., Weintraub,M., Orlovetskie,N., Serruya,R., Mani,D.,
            Marcu,O., Stepensky,P., Weisblum,Y., Djian,E., Shaag,A.,
            Revel-Vilk,S., Fried,I., Kotler,M., Rouvinski,A., Wolf,D.,
            Elpeleg,O. and Jarrous,N.
  TITLE     A mutation in POLR3E impairs antiviral immune response and RNA
            polymerase III
  JOURNAL   Proc Natl Acad Sci U S A 117 (36), 22113-22121 (2020)
   PUBMED   32843346
  REMARK    GeneRIF: A mutation in POLR3E impairs antiviral immune response and
            RNA polymerase III.
REFERENCE   5  (residues 1 to 687)
  AUTHORS   Carter-Timofte,M.E., Hansen,A.F., Christiansen,M., Paludan,S.R. and
            Mogensen,T.H.
  TITLE     Mutations in RNA Polymerase III genes and defective DNA sensing in
            adults with varicella-zoster virus CNS infection
  JOURNAL   Genes Immun 20 (3), 214-223 (2019)
   PUBMED   29728610
  REMARK    GeneRIF: Mutations in the coding region of POLR3E cause impaired
            expression of antiviral cytokines and susceptibility to
            varicella-zoster virus CNS infection.
REFERENCE   6  (residues 1 to 687)
  AUTHORS   Renaud,M., Praz,V., Vieu,E., Florens,L., Washburn,M.P., l'Hote,P.
            and Hernandez,N.
  TITLE     Gene duplication and neofunctionalization: POLR3G and POLR3GL
  JOURNAL   Genome Res 24 (1), 37-51 (2014)
   PUBMED   24107381
REFERENCE   7  (residues 1 to 687)
  AUTHORS   Hu,P., Wu,S., Sun,Y., Yuan,C.C., Kobayashi,R., Myers,M.P. and
            Hernandez,N.
  TITLE     Characterization of human RNA polymerase III identifies orthologues
            for Saccharomyces cerevisiae RNA polymerase III subunits
  JOURNAL   Mol Cell Biol 22 (22), 8044-8055 (2002)
   PUBMED   12391170
  REMARK    GeneRIF: Data describe the purification and identification of RNA
            polymerase III subunits RPC2 and RPC5.
REFERENCE   8  (residues 1 to 687)
  AUTHORS   Smolen,C., Myers,S. and Girirajan,S.
  TITLE     16p12.2 Recurrent Deletion
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719193
REFERENCE   9  (residues 1 to 687)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK026645.1, AK001371.1, AK300735.1, AK222671.1, AA282721.1,
            AC092338.4 and AW205673.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            acceptor splice site in the 3' coding region compared to variant 1.
            The resulting isoform (2) is shorter, missing an internal protein
            segment, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK300735.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145122, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..687
                     /product="DNA-directed RNA polymerase III subunit RPC5
                     isoform 2"
                     /note="RNA polymerase III 80 kDa subunit RPC5;
                     DNA-directed RNA polymerase III subunit RPC5; RNA
                     polymerase III subunit C5; DNA-directed RNA polymerase III
                     80 kDa polypeptide; polymerase (RNA) III (DNA directed)
                     polypeptide E (80kD); polymerase (RNA) III subunit E"
                     /calculated_mol_wt=77084
     Region          5..432
                     /region_name="RPC5"
                     /note="RPC5 protein; pfam04801"
                     /db_xref="CDD:461434"
     Region          443..687
                     /region_name="RPC5_C"
                     /note="DNA-directed RNA polymerase III subunit RPC5
                     C-terminal; pfam19725"
                     /db_xref="CDD:466161"
     CDS             1..687
                     /gene="POLR3E"
                     /gene_synonym="C37; RPC5; SIN"
                     /coded_by="NM_001258033.2:168..2231"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58432.1"
                     /db_xref="GeneID:55718"
                     /db_xref="HGNC:HGNC:30347"
                     /db_xref="MIM:617815"
ORIGIN      
        1 maneeddpvv qeidvylaks laeklylfqy pvrpasmtyd diphlsakik pkqqkvelem
       61 aidtlnpnyc rskgeqialn vdgacadets tyssklmdkq tfcssqttsn tsryaaalyr
      121 qgelhltplh gilqlrpsfs yldkadakhr ereaaneagd ssqdeaeddv kqitvrfsrp
      181 eseqarqrrv qsyeflqkkh aeepwvhlhy yglrdsrseh erqyllcpgs sgventelvk
      241 spseylmmlm ppsqeeekdk pvapsnvlsm aqlrtlplad qikilmknvk vmpfanlmsl
      301 lgpsidsvav lrgiqkvaml vqgnwvvksd ilypkdsssp hsgvpaevlc rgrdfvmwkf
      361 tqsrwvvrke vatvtklcae dvkdflehma vvrinkgwef ilpydgefik khpdvvqrqh
      421 mlwtgiqakl ekvynlvket mpkkpdaqsg paglvcgdqr iqvaktkaqq nhallerelq
      481 rrkeqlrvpa vppgvrikee pvseegeede eqeaeeepmd tspsglhskl anglplgraa
      541 gtdsfnghpp qgcastpvar elkafveatf qrqfvltlse lkrlfnlhla slppghtlfs
      601 gisdrmlqdt vlaagckqil vpfppqtaas pdeqkvfalw esgdmsdqsr ltqecgedls
      661 kqevdkvlkd ccvsyggmwy lkgtvqs
//
LOCUS       NP_060589                708 aa            linear   PRI 09-DEC-2025
DEFINITION  DNA-directed RNA polymerase III subunit RPC5 isoform 1 [Homo
            sapiens].
ACCESSION   NP_060589
VERSION     NP_060589.1
DBSOURCE    REFSEQ: accession NM_018119.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   3  (residues 1 to 708)
  AUTHORS   Ramsay,E.P., Abascal-Palacios,G., Daiss,J.L., King,H., Gouge,J.,
            Pilsl,M., Beuron,F., Morris,E., Gunkel,P., Engel,C. and Vannini,A.
  TITLE     Structure of human RNA polymerase III
  JOURNAL   Nat Commun 11 (1), 6409 (2020)
   PUBMED   33335104
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 708)
  AUTHORS   Ramanathan,A., Weintraub,M., Orlovetskie,N., Serruya,R., Mani,D.,
            Marcu,O., Stepensky,P., Weisblum,Y., Djian,E., Shaag,A.,
            Revel-Vilk,S., Fried,I., Kotler,M., Rouvinski,A., Wolf,D.,
            Elpeleg,O. and Jarrous,N.
  TITLE     A mutation in POLR3E impairs antiviral immune response and RNA
            polymerase III
  JOURNAL   Proc Natl Acad Sci U S A 117 (36), 22113-22121 (2020)
   PUBMED   32843346
  REMARK    GeneRIF: A mutation in POLR3E impairs antiviral immune response and
            RNA polymerase III.
REFERENCE   5  (residues 1 to 708)
  AUTHORS   Carter-Timofte,M.E., Hansen,A.F., Christiansen,M., Paludan,S.R. and
            Mogensen,T.H.
  TITLE     Mutations in RNA Polymerase III genes and defective DNA sensing in
            adults with varicella-zoster virus CNS infection
  JOURNAL   Genes Immun 20 (3), 214-223 (2019)
   PUBMED   29728610
  REMARK    GeneRIF: Mutations in the coding region of POLR3E cause impaired
            expression of antiviral cytokines and susceptibility to
            varicella-zoster virus CNS infection.
REFERENCE   6  (residues 1 to 708)
  AUTHORS   Renaud,M., Praz,V., Vieu,E., Florens,L., Washburn,M.P., l'Hote,P.
            and Hernandez,N.
  TITLE     Gene duplication and neofunctionalization: POLR3G and POLR3GL
  JOURNAL   Genome Res 24 (1), 37-51 (2014)
   PUBMED   24107381
REFERENCE   7  (residues 1 to 708)
  AUTHORS   Hu,P., Wu,S., Sun,Y., Yuan,C.C., Kobayashi,R., Myers,M.P. and
            Hernandez,N.
  TITLE     Characterization of human RNA polymerase III identifies orthologues
            for Saccharomyces cerevisiae RNA polymerase III subunits
  JOURNAL   Mol Cell Biol 22 (22), 8044-8055 (2002)
   PUBMED   12391170
  REMARK    GeneRIF: Data describe the purification and identification of RNA
            polymerase III subunits RPC2 and RPC5.
REFERENCE   8  (residues 1 to 708)
  AUTHORS   Smolen,C., Myers,S. and Girirajan,S.
  TITLE     16p12.2 Recurrent Deletion
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719193
REFERENCE   9  (residues 1 to 708)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK026645.1, AK001371.1, AK222671.1, AA282721.1, AC092338.4 and
            AW205673.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026645.1, SRR1803614.117547.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000299853.10/ ENSP00000299853.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..708
                     /product="DNA-directed RNA polymerase III subunit RPC5
                     isoform 1"
                     /note="RNA polymerase III 80 kDa subunit RPC5;
                     DNA-directed RNA polymerase III subunit RPC5; RNA
                     polymerase III subunit C5; DNA-directed RNA polymerase III
                     80 kDa polypeptide; polymerase (RNA) III (DNA directed)
                     polypeptide E (80kD); polymerase (RNA) III subunit E"
                     /calculated_mol_wt=79767
     Region          5..432
                     /region_name="RPC5"
                     /note="RPC5 protein; pfam04801"
                     /db_xref="CDD:461434"
     Region          146..170
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVU0.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9NVU0.1)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NVU0.1)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NVU0.1)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NVU0.1)"
     Region          443..708
                     /region_name="RPC5_C"
                     /note="DNA-directed RNA polymerase III subunit RPC5
                     C-terminal; pfam19725"
                     /db_xref="CDD:466161"
     Region          485..552
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVU0.1)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NVU0.1)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NVU0.1)"
     Region          556..708
                     /region_name="Required for Pol III complex stability.
                     /evidence=ECO:0000269|PubMed:33335104"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVU0.1)"
     CDS             1..708
                     /gene="POLR3E"
                     /gene_synonym="C37; RPC5; SIN"
                     /coded_by="NM_018119.4:168..2294"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10605.1"
                     /db_xref="GeneID:55718"
                     /db_xref="HGNC:HGNC:30347"
                     /db_xref="MIM:617815"
ORIGIN      
        1 maneeddpvv qeidvylaks laeklylfqy pvrpasmtyd diphlsakik pkqqkvelem
       61 aidtlnpnyc rskgeqialn vdgacadets tyssklmdkq tfcssqttsn tsryaaalyr
      121 qgelhltplh gilqlrpsfs yldkadakhr ereaaneagd ssqdeaeddv kqitvrfsrp
      181 eseqarqrrv qsyeflqkkh aeepwvhlhy yglrdsrseh erqyllcpgs sgventelvk
      241 spseylmmlm ppsqeeekdk pvapsnvlsm aqlrtlplad qikilmknvk vmpfanlmsl
      301 lgpsidsvav lrgiqkvaml vqgnwvvksd ilypkdsssp hsgvpaevlc rgrdfvmwkf
      361 tqsrwvvrke vatvtklcae dvkdflehma vvrinkgwef ilpydgefik khpdvvqrqh
      421 mlwtgiqakl ekvynlvket mpkkpdaqsg paglvcgdqr iqvaktkaqq nhallerelq
      481 rrkeqlrvpa vppgvrikee pvseegeede eqeaeeepmd tspsglhskl anglplgraa
      541 gtdsfnghpp qgcastpvar elkafveatf qrqfvltlse lkrlfnlhla slppghtlfs
      601 gisdrmlqdt vlaagckqil vpfppqtaas pdeqkvfalw esgdmsdqhr qvlleifskn
      661 yrvrrnmiqs rltqecgedl skqevdkvlk dccvsyggmw ylkgtvqs
//
LOCUS       NP_001129665             710 aa            linear   PRI 09-DEC-2025
DEFINITION  FAST kinase domain-containing protein 2, mitochondrial [Homo
            sapiens].
ACCESSION   NP_001129665
VERSION     NP_001129665.1
DBSOURCE    REFSEQ: accession NM_001136193.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Wu,T., Mao,L., Chen,C., Yin,F. and Peng,J.
  TITLE     A novel homozygous missense mutation in the FASTKD2 gene leads to
            Lennox-Gastaut syndrome
  JOURNAL   J Hum Genet 67 (10), 589-594 (2022)
   PUBMED   35729327
  REMARK    GeneRIF: A novel homozygous missense mutation in the FASTKD2 gene
            leads to Lennox-Gastaut syndrome.
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Lim,S.H., Snider,J., Birimberg-Schwartz,L., Ip,W., Serralha,J.C.,
            Botelho,H.M., Lopes-Pacheco,M., Pinto,M.C., Moutaoufik,M.T.,
            Zilocchi,M., Laselva,O., Esmaeili,M., Kotlyar,M., Lyakisheva,A.,
            Tang,P., Lopez Vazquez,L., Akula,I., Aboualizadeh,F., Wong,V.,
            Grozavu,I., Opacak-Bernardi,T., Yao,Z., Mendoza,M., Babu,M.,
            Jurisica,I., Gonska,T., Bear,C.E., Amaral,M.D. and Stagljar,I.
  TITLE     CFTR interactome mapping using the mammalian membrane two-hybrid
            high-throughput screening system
  JOURNAL   Mol Syst Biol 18 (2), e10629 (2022)
   PUBMED   35156780
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 710)
  AUTHORS   Simarro,M., Gimenez-Cassina,A., Kedersha,N., Lazaro,J.B.,
            Adelmant,G.O., Marto,J.A., Rhee,K., Tisdale,S., Danial,N.,
            Benarafa,C., Orduna,A. and Anderson,P.
  TITLE     Fast kinase domain-containing protein 3 is a mitochondrial protein
            essential for cellular respiration
  JOURNAL   Biochem Biophys Res Commun 401 (3), 440-446 (2010)
   PUBMED   20869947
REFERENCE   6  (residues 1 to 710)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 710)
  AUTHORS   Ghezzi,D., Saada,A., D'Adamo,P., Fernandez-Vizarra,E.,
            Gasparini,P., Tiranti,V., Elpeleg,O. and Zeviani,M.
  TITLE     FASTKD2 nonsense mutation in an infantile mitochondrial
            encephalomyopathy associated with cytochrome c oxidase deficiency
  JOURNAL   Am J Hum Genet 83 (3), 415-423 (2008)
   PUBMED   18771761
  REMARK    GeneRIF: mutation in a gene segregating with a peculiar
            mitochondrial encephalomyopathy associated with COX deficiency in
            skeletal muscle. FASTKD2 is localized in the mitochondrial inner
            compartment.
REFERENCE   8  (residues 1 to 710)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
REFERENCE   9  (residues 1 to 710)
  AUTHORS   Patil,S.J., Kaur,N. and Shukla,A.
  TITLE     FASTKD2-Related Combined Oxidative Phosphorylation Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41343688
REFERENCE   10 (residues 1 to 710)
  AUTHORS   Rahman,S., Thorburn,D.R. and Ball,M.
  TITLE     Nuclear Gene-Encoded Leigh Syndrome Spectrum Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26425749
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA021045.1, BC001544.1 and
            AC008269.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that is localized in the
            mitochondrial inner compartment and that may play a role in
            mitochondrial apoptosis. Nonsense mutations have been reported to
            result in cytochrome c oxidase deficiency. [provided by RefSeq, Oct
            2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. All three variants encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.187060.1,
                                           SRR1803612.163016.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000402774.8/ ENSP00000385990.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.3"
     Protein         1..710
                     /product="FAST kinase domain-containing protein 2,
                     mitochondrial"
                     /calculated_mol_wt=81332
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NYY8.1)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NYY8.1)"
     Region          181..407
                     /region_name="RESC6-like"
                     /note="RNA-editing substrate-binding complex subunit 6
                     (RESC6) and related proteins; cl46254"
                     /db_xref="CDD:480594"
     Region          456..529
                     /region_name="FAST_1"
                     /note="FAST kinase-like protein, subdomain 1; pfam06743"
                     /db_xref="CDD:461999"
     Region          <578..619
                     /region_name="FAST_2"
                     /note="FAST kinase-like protein, subdomain 2; pfam08368"
                     /db_xref="CDD:462448"
     Region          636..692
                     /region_name="RAP"
                     /note="This domain is found in various eukaryotic species,
                     particularly in apicomplexans; smart00952"
                     /db_xref="CDD:214932"
     Site            708
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NYY8.1)"
     CDS             1..710
                     /gene="FASTKD2"
                     /gene_synonym="COXPD44; KIAA0971"
                     /coded_by="NM_001136193.2:193..2325"
                     /db_xref="CCDS:CCDS2371.1"
                     /db_xref="GeneID:22868"
                     /db_xref="HGNC:HGNC:29160"
                     /db_xref="MIM:612322"
ORIGIN      
        1 mlttlkpfgs vsveskmnnk agsffwnlrq fstlvstsrt mrlcclglck pkivhsnwni
       61 lnnfhnrmqs tdiirylfqd afifksdvgf qtkgistlta lrierllyak rlffdskqsl
      121 vpvdksddel kkvnlnhevs nedvltketk pnrissrkls eecnslsdvl dafskaptfp
      181 ssnyftamwt iakrlsddqk rfekrlmfsh pafnqlcehm mreakimqyk yllfslhaiv
      241 klgipqntil vqtllrvtqe rinecdeicl svlstvleam epcknvhvlr tgfrilvdqq
      301 vwkiedvftl qvvmkcigkd apialkrkle mkalreldrf svlnsqhmfe vlaamnhrsl
      361 illdecskvv ldnihgcplr iminilqsck dlqyhnldlf kgladyvaat fdiwkfrkvl
      421 fililfenlg frpvglmdlf mkrivedpes lnmknilsil htysslnhvy kcqnkeqfve
      481 vmasaltgyl htissenlld avysfclmny fplapfnqll qkdiisellt sddmknaykl
      541 htldtclkld dtvylrdial slpqlprelp sshtnakvae vlssllggeg hfskdvhlph
      601 nyhidfeirm dtnrnqvlpl sdvdttsatd iqrvavlcvs rsayclgssh prgflamkmr
      661 hlnamgfhvi lvnnwemdkl emedavtflk tkiysvealp vaavnvqstq
//
LOCUS       NP_001244963             672 aa            linear   PRI 09-DEC-2025
DEFINITION  DNA-directed RNA polymerase III subunit RPC5 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001244963
VERSION     NP_001244963.1
DBSOURCE    REFSEQ: accession NM_001258034.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 672)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 672)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   3  (residues 1 to 672)
  AUTHORS   Ramsay,E.P., Abascal-Palacios,G., Daiss,J.L., King,H., Gouge,J.,
            Pilsl,M., Beuron,F., Morris,E., Gunkel,P., Engel,C. and Vannini,A.
  TITLE     Structure of human RNA polymerase III
  JOURNAL   Nat Commun 11 (1), 6409 (2020)
   PUBMED   33335104
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 672)
  AUTHORS   Ramanathan,A., Weintraub,M., Orlovetskie,N., Serruya,R., Mani,D.,
            Marcu,O., Stepensky,P., Weisblum,Y., Djian,E., Shaag,A.,
            Revel-Vilk,S., Fried,I., Kotler,M., Rouvinski,A., Wolf,D.,
            Elpeleg,O. and Jarrous,N.
  TITLE     A mutation in POLR3E impairs antiviral immune response and RNA
            polymerase III
  JOURNAL   Proc Natl Acad Sci U S A 117 (36), 22113-22121 (2020)
   PUBMED   32843346
  REMARK    GeneRIF: A mutation in POLR3E impairs antiviral immune response and
            RNA polymerase III.
REFERENCE   5  (residues 1 to 672)
  AUTHORS   Carter-Timofte,M.E., Hansen,A.F., Christiansen,M., Paludan,S.R. and
            Mogensen,T.H.
  TITLE     Mutations in RNA Polymerase III genes and defective DNA sensing in
            adults with varicella-zoster virus CNS infection
  JOURNAL   Genes Immun 20 (3), 214-223 (2019)
   PUBMED   29728610
  REMARK    GeneRIF: Mutations in the coding region of POLR3E cause impaired
            expression of antiviral cytokines and susceptibility to
            varicella-zoster virus CNS infection.
REFERENCE   6  (residues 1 to 672)
  AUTHORS   Renaud,M., Praz,V., Vieu,E., Florens,L., Washburn,M.P., l'Hote,P.
            and Hernandez,N.
  TITLE     Gene duplication and neofunctionalization: POLR3G and POLR3GL
  JOURNAL   Genome Res 24 (1), 37-51 (2014)
   PUBMED   24107381
REFERENCE   7  (residues 1 to 672)
  AUTHORS   Hu,P., Wu,S., Sun,Y., Yuan,C.C., Kobayashi,R., Myers,M.P. and
            Hernandez,N.
  TITLE     Characterization of human RNA polymerase III identifies orthologues
            for Saccharomyces cerevisiae RNA polymerase III subunits
  JOURNAL   Mol Cell Biol 22 (22), 8044-8055 (2002)
   PUBMED   12391170
  REMARK    GeneRIF: Data describe the purification and identification of RNA
            polymerase III subunits RPC2 and RPC5.
REFERENCE   8  (residues 1 to 672)
  AUTHORS   Smolen,C., Myers,S. and Girirajan,S.
  TITLE     16p12.2 Recurrent Deletion
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719193
REFERENCE   9  (residues 1 to 672)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB047155.1, AK296813.1, AK001371.1, AK222671.1, AA282721.1,
            AC092338.4 and AW205673.1.
            
            Transcript Variant: This variant (4) lacks an exon and uses an
            alternate acceptor splice site in the 5' region compared to variant
            1, However, it maintains the reading frame, and encodes an isoform
            (4) missing an internal protein segment compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296813.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..672
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..672
                     /product="DNA-directed RNA polymerase III subunit RPC5
                     isoform 4"
                     /note="RNA polymerase III 80 kDa subunit RPC5;
                     DNA-directed RNA polymerase III subunit RPC5; RNA
                     polymerase III subunit C5; DNA-directed RNA polymerase III
                     80 kDa polypeptide; polymerase (RNA) III (DNA directed)
                     polypeptide E (80kD); polymerase (RNA) III subunit E"
                     /calculated_mol_wt=75627
     Region          5..396
                     /region_name="RPC5"
                     /note="RPC5 protein; pfam04801"
                     /db_xref="CDD:461434"
     Region          407..672
                     /region_name="RPC5_C"
                     /note="DNA-directed RNA polymerase III subunit RPC5
                     C-terminal; pfam19725"
                     /db_xref="CDD:466161"
     CDS             1..672
                     /gene="POLR3E"
                     /gene_synonym="C37; RPC5; SIN"
                     /coded_by="NM_001258034.2:168..2186"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS58434.1"
                     /db_xref="GeneID:55718"
                     /db_xref="HGNC:HGNC:30347"
                     /db_xref="MIM:617815"
ORIGIN      
        1 maneeddpvv qeikpkqqkv elemaidtln pnycrskgeq ialnvdgaca detstysskl
       61 mdkqtfcssq ttsntsryaa alyrqgelhl tplhgilqlr psfsyldkad akhrereaan
      121 eagdssqdea eddvkqitvr fsrpeseqar qrrvqsyefl qkkhaeepwv hlhyyglrds
      181 rseherqyll cpgssgvent elvkspseyl mmlmppsqee ekdkpvapsn vlsmaqlrtl
      241 pladqikilm knvkvmpfan lmsllgpsid svavlrgiqk vamlvqgnwv vksdilypkd
      301 sssphsgvpa evlcrgrdfv mwkftqsrwv vrkevatvtk lcaedvkdfl ehmavvrink
      361 gwefilpydg efikkhpdvv qrqhmlwtgi qaklekvynl vketmpkkpd aqsgpaglvc
      421 gdqriqvakt kaqqnhalle relqrrkeql rvpavppgvr ikeepvseeg eedeeqeaee
      481 epmdtspsgl hsklanglpl graagtdsfn ghppqgcast pvarelkafv eatfqrqfvl
      541 tlselkrlfn lhlaslppgh tlfsgisdrm lqdtvlaagc kqilvpfppq taaspdeqkv
      601 falwesgdms dqhrqvllei fsknyrvrrn miqsrltqec gedlskqevd kvlkdccvsy
      661 ggmwylkgtv qs
//
LOCUS       NP_001244965             666 aa            linear   PRI 09-DEC-2025
DEFINITION  DNA-directed RNA polymerase III subunit RPC5 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001244965
VERSION     NP_001244965.1
DBSOURCE    REFSEQ: accession NM_001258036.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Ramsay,E.P., Abascal-Palacios,G., Daiss,J.L., King,H., Gouge,J.,
            Pilsl,M., Beuron,F., Morris,E., Gunkel,P., Engel,C. and Vannini,A.
  TITLE     Structure of human RNA polymerase III
  JOURNAL   Nat Commun 11 (1), 6409 (2020)
   PUBMED   33335104
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 666)
  AUTHORS   Ramanathan,A., Weintraub,M., Orlovetskie,N., Serruya,R., Mani,D.,
            Marcu,O., Stepensky,P., Weisblum,Y., Djian,E., Shaag,A.,
            Revel-Vilk,S., Fried,I., Kotler,M., Rouvinski,A., Wolf,D.,
            Elpeleg,O. and Jarrous,N.
  TITLE     A mutation in POLR3E impairs antiviral immune response and RNA
            polymerase III
  JOURNAL   Proc Natl Acad Sci U S A 117 (36), 22113-22121 (2020)
   PUBMED   32843346
  REMARK    GeneRIF: A mutation in POLR3E impairs antiviral immune response and
            RNA polymerase III.
REFERENCE   5  (residues 1 to 666)
  AUTHORS   Carter-Timofte,M.E., Hansen,A.F., Christiansen,M., Paludan,S.R. and
            Mogensen,T.H.
  TITLE     Mutations in RNA Polymerase III genes and defective DNA sensing in
            adults with varicella-zoster virus CNS infection
  JOURNAL   Genes Immun 20 (3), 214-223 (2019)
   PUBMED   29728610
  REMARK    GeneRIF: Mutations in the coding region of POLR3E cause impaired
            expression of antiviral cytokines and susceptibility to
            varicella-zoster virus CNS infection.
REFERENCE   6  (residues 1 to 666)
  AUTHORS   Renaud,M., Praz,V., Vieu,E., Florens,L., Washburn,M.P., l'Hote,P.
            and Hernandez,N.
  TITLE     Gene duplication and neofunctionalization: POLR3G and POLR3GL
  JOURNAL   Genome Res 24 (1), 37-51 (2014)
   PUBMED   24107381
REFERENCE   7  (residues 1 to 666)
  AUTHORS   Hu,P., Wu,S., Sun,Y., Yuan,C.C., Kobayashi,R., Myers,M.P. and
            Hernandez,N.
  TITLE     Characterization of human RNA polymerase III identifies orthologues
            for Saccharomyces cerevisiae RNA polymerase III subunits
  JOURNAL   Mol Cell Biol 22 (22), 8044-8055 (2002)
   PUBMED   12391170
  REMARK    GeneRIF: Data describe the purification and identification of RNA
            polymerase III subunits RPC2 and RPC5.
REFERENCE   8  (residues 1 to 666)
  AUTHORS   Smolen,C., Myers,S. and Girirajan,S.
  TITLE     16p12.2 Recurrent Deletion
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719193
REFERENCE   9  (residues 1 to 666)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK026645.1, AK001371.1, AK222671.1, AA282721.1, AC092338.4 and
            AW205673.1.
            
            Transcript Variant: This variant (5) lacks an exon in the 3' coding
            region compared to variant 1. The resulting isoform (5) is shorter,
            missing an internal protein segment, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK023160.1, BC000285.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..666
                     /product="DNA-directed RNA polymerase III subunit RPC5
                     isoform 5"
                     /note="RNA polymerase III 80 kDa subunit RPC5;
                     DNA-directed RNA polymerase III subunit RPC5; RNA
                     polymerase III subunit C5; DNA-directed RNA polymerase III
                     80 kDa polypeptide; polymerase (RNA) III (DNA directed)
                     polypeptide E (80kD); polymerase (RNA) III subunit E"
                     /calculated_mol_wt=74696
     Region          5..432
                     /region_name="RPC5"
                     /note="RPC5 protein; pfam04801"
                     /db_xref="CDD:461434"
     Region          443..666
                     /region_name="RPC5_C"
                     /note="DNA-directed RNA polymerase III subunit RPC5
                     C-terminal; pfam19725"
                     /db_xref="CDD:466161"
     CDS             1..666
                     /gene="POLR3E"
                     /gene_synonym="C37; RPC5; SIN"
                     /coded_by="NM_001258036.2:168..2168"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS58433.1"
                     /db_xref="GeneID:55718"
                     /db_xref="HGNC:HGNC:30347"
                     /db_xref="MIM:617815"
ORIGIN      
        1 maneeddpvv qeidvylaks laeklylfqy pvrpasmtyd diphlsakik pkqqkvelem
       61 aidtlnpnyc rskgeqialn vdgacadets tyssklmdkq tfcssqttsn tsryaaalyr
      121 qgelhltplh gilqlrpsfs yldkadakhr ereaaneagd ssqdeaeddv kqitvrfsrp
      181 eseqarqrrv qsyeflqkkh aeepwvhlhy yglrdsrseh erqyllcpgs sgventelvk
      241 spseylmmlm ppsqeeekdk pvapsnvlsm aqlrtlplad qikilmknvk vmpfanlmsl
      301 lgpsidsvav lrgiqkvaml vqgnwvvksd ilypkdsssp hsgvpaevlc rgrdfvmwkf
      361 tqsrwvvrke vatvtklcae dvkdflehma vvrinkgwef ilpydgefik khpdvvqrqh
      421 mlwtgiqakl ekvynlvket mpkkpdaqsg paglvcgdqr iqvaktkaqq nhallerelq
      481 rrkeqlrvpa vppgvrikee pvseegeede eqeaeeepmd tspsglhskl anglplgraa
      541 gtdsfnghpp qgcastpvar elkafveatf qrqfvltlse lkrlfnlhla slppghtlfs
      601 gisdrmlqdt vlaagckqil vpfppqtaas pdeqkvfalw esgdmsdqdc cvsyggmwyl
      661 kgtvqs
//
LOCUS       NP_001352217             626 aa            linear   PRI 09-DEC-2025
DEFINITION  putative short-chain dehydrogenase/reductase family 42E member 2
            isoform 1 [Homo sapiens].
ACCESSION   NP_001352217
VERSION     NP_001352217.1
DBSOURCE    REFSEQ: accession NM_001365288.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Martin,J., Han,C., Gordon,L.A., Terry,A., Prabhakar,S., She,X.,
            Xie,G., Hellsten,U., Chan,Y.M., Altherr,M., Couronne,O., Aerts,A.,
            Bajorek,E., Black,S., Blumer,H., Branscomb,E., Brown,N.C.,
            Bruno,W.J., Buckingham,J.M., Callen,D.F., Campbell,C.S.,
            Campbell,M.L., Campbell,E.W., Caoile,C., Challacombe,J.F.,
            Chasteen,L.A., Chertkov,O., Chi,H.C., Christensen,M., Clark,L.M.,
            Cohn,J.D., Denys,M., Detter,J.C., Dickson,M.,
            Dimitrijevic-Bussod,M., Escobar,J., Fawcett,J.J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Goodwin,L.A., Grady,D.L., Grigoriev,I., Groza,M., Hammon,N.,
            Hawkins,T., Haydu,L., Hildebrand,C.E., Huang,W., Israni,S.,
            Jett,J., Jewett,P.B., Kadner,K., Kimball,H., Kobayashi,A.,
            Krawczyk,M.C., Leyba,T., Longmire,J.L., Lopez,F., Lou,Y., Lowry,S.,
            Ludeman,T., Manohar,C.F., Mark,G.A., McMurray,K.L., Meincke,L.J.,
            Morgan,J., Moyzis,R.K., Mundt,M.O., Munk,A.C., Nandkeshwar,R.D.,
            Pitluck,S., Pollard,M., Predki,P., Parson-Quintana,B., Ramirez,L.,
            Rash,S., Retterer,J., Ricke,D.O., Robinson,D.L., Rodriguez,A.,
            Salamov,A., Saunders,E.H., Scott,D., Shough,T., Stallings,R.L.,
            Stalvey,M., Sutherland,R.D., Tapia,R., Tesmer,J.G., Thayer,N.,
            Thompson,L.S., Tice,H., Torney,D.C., Tran-Gyamfi,M., Tsai,M.,
            Ulanovsky,L.E., Ustaszewska,A., Vo,N., White,P.S., Williams,A.L.,
            Wills,P.L., Wu,J.R., Wu,K., Yang,J., Dejong,P., Bruce,D.,
            Doggett,N.A., Deaven,L., Schmutz,J., Grimwood,J., Richardson,P.,
            Rokhsar,D.S., Eichler,E.E., Gilna,P., Lucas,S.M., Myers,R.M.,
            Rubin,E.M. and Pennacchio,L.A.
  TITLE     The sequence and analysis of duplication-rich human chromosome 16
  JOURNAL   Nature 432 (7020), 988-994 (2004)
   PUBMED   15616553
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Smolen,C., Myers,S. and Girirajan,S.
  TITLE     16p12.2 Recurrent Deletion
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719193
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009019.10.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1968189, SAMEA1968968
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..626
                     /product="putative short-chain dehydrogenase/reductase
                     family 42E member 2 isoform 1"
                     /EC_number="1.1.1.-"
                     /note="putative short-chain dehydrogenase/reductase family
                     42E member 2; putative 3-beta-HSD family protein
                     ENSP00000330812"
                     /calculated_mol_wt=64166
     Region          <31..222
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          239..577
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(244,246..247,249,268..270,306..308,348..350,380,384,
                     412..415)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187535"
     Site            order(326,350,380,384)
                     /site_type="active"
                     /db_xref="CDD:187535"
     CDS             1..626
                     /gene="SDR42E2"
                     /coded_by="NM_001365288.2:61..1941"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:100288072"
                     /db_xref="HGNC:HGNC:35414"
ORIGIN      
        1 mksnpprssl eackaagqge kscpvcqacg evsgprsgsg sesrpapkpg aipgpglgpk
       61 aipgpqagsg tvprpgaisg tgpglgpgpg agsvpgpgag svpglgarsv pgpgagsvpg
      121 pgagsvpgpg agsvpgpgag sgpglggglg pgvgagpgag svpgpgagsv pgpgagsvpg
      181 pgagsvpgag agstpepelg pglrqgsgtg prpsestttp tpapqqktqa kptkaarqkv
      241 lvtggggylg fslgshlaks gtsvilldrr rpqwelspet kfiqadvrde ealyrafegv
      301 dcvfhvasyg msgaeklqke qiesinvggt klvidvcvrr rvprliytst vnvafggkpi
      361 eqgdedsvpy fpldehvdhy srtkaiadql tlmangmplp gggtlrtcvl rppgiygpee
      421 qrhlprvagh ikkrlfmfrf gdhkarmnwv hvhnlvqahv laaealttak gyvasgqayy
      481 indgesvnlf ewmaplfekl gysqpwiqvp tswvyltaav merlhlalrp icslpplltr
      541 sevrsvavth tfqiakaraq lgyapdkfrf adavelyvqs ttrrprgsta rtllrlllrl
      601 llflgllala lhflglqplh aaverl
//
LOCUS       NP_055744                710 aa            linear   PRI 09-DEC-2025
DEFINITION  FAST kinase domain-containing protein 2, mitochondrial [Homo
            sapiens].
ACCESSION   NP_055744 XP_376168
VERSION     NP_055744.2
DBSOURCE    REFSEQ: accession NM_014929.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Wu,T., Mao,L., Chen,C., Yin,F. and Peng,J.
  TITLE     A novel homozygous missense mutation in the FASTKD2 gene leads to
            Lennox-Gastaut syndrome
  JOURNAL   J Hum Genet 67 (10), 589-594 (2022)
   PUBMED   35729327
  REMARK    GeneRIF: A novel homozygous missense mutation in the FASTKD2 gene
            leads to Lennox-Gastaut syndrome.
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Lim,S.H., Snider,J., Birimberg-Schwartz,L., Ip,W., Serralha,J.C.,
            Botelho,H.M., Lopes-Pacheco,M., Pinto,M.C., Moutaoufik,M.T.,
            Zilocchi,M., Laselva,O., Esmaeili,M., Kotlyar,M., Lyakisheva,A.,
            Tang,P., Lopez Vazquez,L., Akula,I., Aboualizadeh,F., Wong,V.,
            Grozavu,I., Opacak-Bernardi,T., Yao,Z., Mendoza,M., Babu,M.,
            Jurisica,I., Gonska,T., Bear,C.E., Amaral,M.D. and Stagljar,I.
  TITLE     CFTR interactome mapping using the mammalian membrane two-hybrid
            high-throughput screening system
  JOURNAL   Mol Syst Biol 18 (2), e10629 (2022)
   PUBMED   35156780
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 710)
  AUTHORS   Simarro,M., Gimenez-Cassina,A., Kedersha,N., Lazaro,J.B.,
            Adelmant,G.O., Marto,J.A., Rhee,K., Tisdale,S., Danial,N.,
            Benarafa,C., Orduna,A. and Anderson,P.
  TITLE     Fast kinase domain-containing protein 3 is a mitochondrial protein
            essential for cellular respiration
  JOURNAL   Biochem Biophys Res Commun 401 (3), 440-446 (2010)
   PUBMED   20869947
REFERENCE   6  (residues 1 to 710)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 710)
  AUTHORS   Ghezzi,D., Saada,A., D'Adamo,P., Fernandez-Vizarra,E.,
            Gasparini,P., Tiranti,V., Elpeleg,O. and Zeviani,M.
  TITLE     FASTKD2 nonsense mutation in an infantile mitochondrial
            encephalomyopathy associated with cytochrome c oxidase deficiency
  JOURNAL   Am J Hum Genet 83 (3), 415-423 (2008)
   PUBMED   18771761
  REMARK    GeneRIF: mutation in a gene segregating with a peculiar
            mitochondrial encephalomyopathy associated with COX deficiency in
            skeletal muscle. FASTKD2 is localized in the mitochondrial inner
            compartment.
REFERENCE   8  (residues 1 to 710)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
REFERENCE   9  (residues 1 to 710)
  AUTHORS   Patil,S.J., Kaur,N. and Shukla,A.
  TITLE     FASTKD2-Related Combined Oxidative Phosphorylation Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41343688
REFERENCE   10 (residues 1 to 710)
  AUTHORS   Rahman,S., Thorburn,D.R. and Ball,M.
  TITLE     Nuclear Gene-Encoded Leigh Syndrome Spectrum Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26425749
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA475994.1, BC001544.1 and
            AC008269.4.
            
            On or before Mar 10, 2004 this sequence version replaced
            XP_376168.1, NP_055744.1.
            
            Summary: This gene encodes a protein that is localized in the
            mitochondrial inner compartment and that may play a role in
            mitochondrial apoptosis. Nonsense mutations have been reported to
            result in cytochrome c oxidase deficiency. [provided by RefSeq, Oct
            2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. All three variants encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1142209.1,
                                           SRR7346977.2527510.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.3"
     Protein         1..710
                     /product="FAST kinase domain-containing protein 2,
                     mitochondrial"
                     /calculated_mol_wt=81332
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NYY8.1)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NYY8.1)"
     Region          181..407
                     /region_name="RESC6-like"
                     /note="RNA-editing substrate-binding complex subunit 6
                     (RESC6) and related proteins; cl46254"
                     /db_xref="CDD:480594"
     Region          456..529
                     /region_name="FAST_1"
                     /note="FAST kinase-like protein, subdomain 1; pfam06743"
                     /db_xref="CDD:461999"
     Region          <578..619
                     /region_name="FAST_2"
                     /note="FAST kinase-like protein, subdomain 2; pfam08368"
                     /db_xref="CDD:462448"
     Region          636..692
                     /region_name="RAP"
                     /note="This domain is found in various eukaryotic species,
                     particularly in apicomplexans; smart00952"
                     /db_xref="CDD:214932"
     Site            708
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NYY8.1)"
     CDS             1..710
                     /gene="FASTKD2"
                     /gene_synonym="COXPD44; KIAA0971"
                     /coded_by="NM_014929.4:100..2232"
                     /db_xref="CCDS:CCDS2371.1"
                     /db_xref="GeneID:22868"
                     /db_xref="HGNC:HGNC:29160"
                     /db_xref="MIM:612322"
ORIGIN      
        1 mlttlkpfgs vsveskmnnk agsffwnlrq fstlvstsrt mrlcclglck pkivhsnwni
       61 lnnfhnrmqs tdiirylfqd afifksdvgf qtkgistlta lrierllyak rlffdskqsl
      121 vpvdksddel kkvnlnhevs nedvltketk pnrissrkls eecnslsdvl dafskaptfp
      181 ssnyftamwt iakrlsddqk rfekrlmfsh pafnqlcehm mreakimqyk yllfslhaiv
      241 klgipqntil vqtllrvtqe rinecdeicl svlstvleam epcknvhvlr tgfrilvdqq
      301 vwkiedvftl qvvmkcigkd apialkrkle mkalreldrf svlnsqhmfe vlaamnhrsl
      361 illdecskvv ldnihgcplr iminilqsck dlqyhnldlf kgladyvaat fdiwkfrkvl
      421 fililfenlg frpvglmdlf mkrivedpes lnmknilsil htysslnhvy kcqnkeqfve
      481 vmasaltgyl htissenlld avysfclmny fplapfnqll qkdiisellt sddmknaykl
      541 htldtclkld dtvylrdial slpqlprelp sshtnakvae vlssllggeg hfskdvhlph
      601 nyhidfeirm dtnrnqvlpl sdvdttsatd iqrvavlcvs rsayclgssh prgflamkmr
      661 hlnamgfhvi lvnnwemdkl emedavtflk tkiysvealp vaavnvqstq
//
LOCUS       NP_037434                725 aa            linear   PRI 09-DEC-2025
DEFINITION  eukaryotic elongation factor 2 kinase [Homo sapiens].
ACCESSION   NP_037434
VERSION     NP_037434.2
DBSOURCE    REFSEQ: accession NM_013302.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Ma,T.
  TITLE     Roles of eukaryotic elongation factor 2 kinase (eEF2K) in neuronal
            plasticity, cognition, and Alzheimer disease
  JOURNAL   J Neurochem 166 (1), 47-57 (2023)
   PUBMED   34796967
  REMARK    GeneRIF: Roles of eukaryotic elongation factor 2 kinase (eEF2K) in
            neuronal plasticity, cognition, and Alzheimer disease.
            Review article
REFERENCE   2  (residues 1 to 725)
  AUTHORS   Piserchio,A., Isiorho,E.A., Dalby,K.N. and Ghose,R.
  TITLE     Structure of the complex between calmodulin and a functional
            construct of eukaryotic elongation factor 2 kinase bound to an
            ATP-competitive inhibitor
  JOURNAL   J Biol Chem 299 (6), 104813 (2023)
   PUBMED   37172726
  REMARK    GeneRIF: Structure of the complex between calmodulin and a
            functional construct of eukaryotic elongation factor 2 kinase bound
            to an ATP-competitive inhibitor.
REFERENCE   3  (residues 1 to 725)
  AUTHORS   Chen,X., Wang,K., Jiang,S., Sun,H., Che,X., Zhang,M., He,J.,
            Wen,Y., Liao,M., Li,X., Zhou,X., Song,J., Ren,X., Yi,W., Yang,J.,
            Chen,X., Yin,M. and Cheng,Y.
  TITLE     eEF2K promotes PD-L1 stabilization through inactivating GSK3beta in
            melanoma
  JOURNAL   J Immunother Cancer 10 (3) (2022)
   PUBMED   35347072
  REMARK    GeneRIF: eEF2K promotes PD-L1 stabilization through inactivating
            GSK3beta in melanoma.
REFERENCE   4  (residues 1 to 725)
  AUTHORS   Gurbuz,N., Kahraman,N., Sonmez,H.E., Mokhlis,H.A., Kosar,P.A. and
            Ozpolat,B.
  TITLE     miRNA-193b-5p Suppresses Pancreatic Cancer Cell Proliferation,
            Invasion, Epithelial Mesenchymal Transition, and Tumor Growth by
            Inhibiting eEF2K
  JOURNAL   Anticancer Agents Med Chem 22 (14), 2607-2618 (2022)
   PUBMED   35718922
  REMARK    GeneRIF: miRNA-193b-5p Suppresses Pancreatic Cancer Cell
            Proliferation, Invasion, Epithelial Mesenchymal Transition, and
            Tumor Growth by Inhibiting eEF2K.
REFERENCE   5  (residues 1 to 725)
  AUTHORS   Jiang,M., Qi,L., Jin,K., Li,L., Wu,Y., Song,D., Gan,J., Huang,M.,
            Li,Y. and Song,C.
  TITLE     eEF2K as a novel metastatic and prognostic biomarker in gastric
            cancer patients
  JOURNAL   Pathol Res Pract 225, 153568 (2021)
   PUBMED   34352439
  REMARK    GeneRIF: eEF2K as a novel metastatic and prognostic biomarker in
            gastric cancer patients.
REFERENCE   6  (residues 1 to 725)
  AUTHORS   Pavur,K.S., Petrov,A.N. and Ryazanov,A.G.
  TITLE     Mapping the functional domains of elongation factor-2 kinase
  JOURNAL   Biochemistry 39 (40), 12216-12224 (2000)
   PUBMED   11015200
REFERENCE   7  (residues 1 to 725)
  AUTHORS   Ryazanov,A.G., Ward,M.D., Mendola,C.E., Pavur,K.S., Dorovkov,M.V.,
            Wiedmann,M., Erdjument-Bromage,H., Tempst,P., Parmer,T.G.,
            Prostko,C.R., Germino,F.J. and Hait,W.N.
  TITLE     Identification of a new class of protein kinases represented by
            eukaryotic elongation factor-2 kinase
  JOURNAL   Proc Natl Acad Sci U S A 94 (10), 4884-4889 (1997)
   PUBMED   9144159
REFERENCE   8  (residues 1 to 725)
  AUTHORS   Redpath,N.T., Price,N.T., Severinov,K.V. and Proud,C.G.
  TITLE     Regulation of elongation factor-2 by multisite phosphorylation
  JOURNAL   Eur J Biochem 213 (2), 689-699 (1993)
   PUBMED   8386634
REFERENCE   9  (residues 1 to 725)
  AUTHORS   Smolen,C., Myers,S. and Girirajan,S.
  TITLE     16p12.2 Recurrent Deletion
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719193
REFERENCE   10 (residues 1 to 725)
  AUTHORS   Nairn,A.C. and Palfrey,H.C.
  TITLE     Identification of the major Mr 100,000 substrate for
            calmodulin-dependent protein kinase III in mammalian cells as
            elongation factor-2
  JOURNAL   J Biol Chem 262 (36), 17299-17303 (1987)
   PUBMED   3693353
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009034.10.
            
            On May 21, 2020 this sequence version replaced NP_037434.1.
            
            Summary: This gene encodes a highly conserved protein kinase in the
            calmodulin-mediated signaling pathway that links activation of cell
            surface receptors to cell division. This kinase is involved in the
            regulation of protein synthesis. It phosphorylates eukaryotic
            elongation factor 2 (EEF2) and thus inhibits the EEF2 function. The
            activity of this kinase is increased in many cancers and may be a
            valid target for anti-cancer treatment. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3774843.1,
                                           SRR11853566.10028.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263026.10/ ENSP00000263026.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..725
                     /product="eukaryotic elongation factor 2 kinase"
                     /EC_number="2.7.11.20"
                     /note="calmodulin-dependent protein kinase III; elongation
                     factor-2 kinase; calcium/calmodulin-dependent eukaryotic
                     elongation factor-2 kinase; eEF-2 kinase; eukaroytic
                     elongation factor 2 kinase; alternative protein EEF2K"
                     /calculated_mol_wt=82013
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00418.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O00418.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:22216903; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:22216903; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08796; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis and TRPM7.
                     /evidence=ECO:0000269|PubMed:21112387,
                     ECO:0000269|PubMed:22216903, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O00418.2)"
     Region          81..94
                     /region_name="Calmodulin-binding.
                     /evidence=ECO:0000269|PubMed:11015200"
                     /note="propagated from UniProtKB/Swiss-Prot (O00418.2)"
     Region          103..318
                     /region_name="Alpha_kinase_eEF2K"
                     /note="Alpha-kinase domain of eukaryotic elongation
                     factor-2 kinase; cd16967"
                     /db_xref="CDD:341217"
     Site            order(139..144,146,168,170,210,229..232,274,276,284)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:341217"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:22216903,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O00418.2)"
     Region          352..405
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00418.2)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:22216903,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK13 and CDK1.
                     /evidence=ECO:0000269|PubMed:11500363,
                     ECO:0000269|PubMed:18337751; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis, RPS6KA1 and
                     RPS6KB1. /evidence=ECO:0000269|PubMed:11500364,
                     ECO:0000269|PubMed:22216903; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08796; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:14709557; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Region          423..477
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00418.2)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:22216903,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O00418.2)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:22216903,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            491
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:22216903,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Site            500
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:P70531; propagated from
                     UniProtKB/Swiss-Prot (O00418.2)"
     Region          <532..695
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          547..576
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          593..622
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     CDS             1..725
                     /gene="EEF2K"
                     /gene_synonym="CaMKIII; eEF-2K; HSU93850"
                     /coded_by="NM_013302.5:479..2656"
                     /db_xref="CCDS:CCDS10604.1"
                     /db_xref="GeneID:29904"
                     /db_xref="HGNC:HGNC:24615"
                     /db_xref="MIM:606968"
ORIGIN      
        1 madedlifrl egvdggqspr aghdgdsdgd sddeegyfic pitddpssnq nvnskvnkyy
       61 snltkserys ssgspansfh fkeawkhaiq kakhmpdpwa efhlediate ratrhrynav
      121 tgewlddevl ikmasqpfgr gamrecfrtk klsnflhaqq wkgasnyvak ryiepvdrdv
      181 yfedvrlqme aklwgeeynr hkppkqvdim qmciielkdr pgkplfhleh yiegkyikyn
      241 snsgfvrddn irltpqafsh ftfersghql ivvdiqgvgd lytdpqihte tgtdfgdgnl
      301 gvrgmalffy shacnrices mglapfdlsp rerdavnqnt kllqsaktil rgteekcgsp
      361 qvrtlsgsrp pllrplsens gdenmsdvtf dslpsspssa tphsqkldhl hwpvfsdldn
      421 masrdhdhld nhresensgd sgypsekrge lddpeprehg hsysnrkyes dedslgssgr
      481 vcvekwnlln ssrlhlpras avalevqrln aldlekkigk silgkvhlam vryheggrfc
      541 ekgeewdqes avfhlehaan lgeleaivgl glmysqlphh iladvslket eenktkgfdy
      601 llkaaeagdr qsmilvaraf dsgqnlspdr cqdwlealhw yntalemtdc deggeydgmq
      661 deprymmlar eaemlftggy glekdpqrsg dlytqaaeaa meamkgrlan qyyqkaeeaw
      721 aqmee
//
LOCUS       NP_001381248             422 aa            linear   PRI 09-DEC-2025
DEFINITION  putative short-chain dehydrogenase/reductase family 42E member 2
            isoform 2 [Homo sapiens].
ACCESSION   NP_001381248
VERSION     NP_001381248.1
DBSOURCE    REFSEQ: accession NM_001394319.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Martin,J., Han,C., Gordon,L.A., Terry,A., Prabhakar,S., She,X.,
            Xie,G., Hellsten,U., Chan,Y.M., Altherr,M., Couronne,O., Aerts,A.,
            Bajorek,E., Black,S., Blumer,H., Branscomb,E., Brown,N.C.,
            Bruno,W.J., Buckingham,J.M., Callen,D.F., Campbell,C.S.,
            Campbell,M.L., Campbell,E.W., Caoile,C., Challacombe,J.F.,
            Chasteen,L.A., Chertkov,O., Chi,H.C., Christensen,M., Clark,L.M.,
            Cohn,J.D., Denys,M., Detter,J.C., Dickson,M.,
            Dimitrijevic-Bussod,M., Escobar,J., Fawcett,J.J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Goodwin,L.A., Grady,D.L., Grigoriev,I., Groza,M., Hammon,N.,
            Hawkins,T., Haydu,L., Hildebrand,C.E., Huang,W., Israni,S.,
            Jett,J., Jewett,P.B., Kadner,K., Kimball,H., Kobayashi,A.,
            Krawczyk,M.C., Leyba,T., Longmire,J.L., Lopez,F., Lou,Y., Lowry,S.,
            Ludeman,T., Manohar,C.F., Mark,G.A., McMurray,K.L., Meincke,L.J.,
            Morgan,J., Moyzis,R.K., Mundt,M.O., Munk,A.C., Nandkeshwar,R.D.,
            Pitluck,S., Pollard,M., Predki,P., Parson-Quintana,B., Ramirez,L.,
            Rash,S., Retterer,J., Ricke,D.O., Robinson,D.L., Rodriguez,A.,
            Salamov,A., Saunders,E.H., Scott,D., Shough,T., Stallings,R.L.,
            Stalvey,M., Sutherland,R.D., Tapia,R., Tesmer,J.G., Thayer,N.,
            Thompson,L.S., Tice,H., Torney,D.C., Tran-Gyamfi,M., Tsai,M.,
            Ulanovsky,L.E., Ustaszewska,A., Vo,N., White,P.S., Williams,A.L.,
            Wills,P.L., Wu,J.R., Wu,K., Yang,J., Dejong,P., Bruce,D.,
            Doggett,N.A., Deaven,L., Schmutz,J., Grimwood,J., Richardson,P.,
            Rokhsar,D.S., Eichler,E.E., Gilna,P., Lucas,S.M., Myers,R.M.,
            Rubin,E.M. and Pennacchio,L.A.
  TITLE     The sequence and analysis of duplication-rich human chromosome 16
  JOURNAL   Nature 432 (7020), 988-994 (2004)
   PUBMED   15616553
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Smolen,C., Myers,S. and Girirajan,S.
  TITLE     16p12.2 Recurrent Deletion
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719193
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009019.10.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1968968 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000602312.3/ ENSP00000473474.2
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..422
                     /product="putative short-chain dehydrogenase/reductase
                     family 42E member 2 isoform 2"
                     /EC_number="1.1.1.-"
                     /note="putative short-chain dehydrogenase/reductase family
                     42E member 2; putative 3-beta-HSD family protein
                     ENSP00000330812"
                     /calculated_mol_wt=46738
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NKP2.3)"
     Region          35..373
                     /region_name="3b-HSD_like_1_SDR_e"
                     /note="3beta-hydroxysteroid dehydrogenase (3b-HSD)-like,
                     subgroup1, extended (e) SDRs; cd09812"
                     /db_xref="CDD:187672"
     Site            order(40,42..45,64..66,102..104,121,144..146,176,180,
                     208..211)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187672"
     Site            order(122,146,176,180)
                     /site_type="active"
                     /db_xref="CDD:187672"
     Site            order(146,176,210,223,234,239)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187672"
     CDS             1..422
                     /gene="SDR42E2"
                     /coded_by="NM_001394319.2:96..1364"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS92125.1"
                     /db_xref="GeneID:100288072"
                     /db_xref="HGNC:HGNC:35414"
ORIGIN      
        1 mksnpprssl eackaagqap qqktqakptk aarqkvlvtg gggylgfslg shlaksgtsv
       61 illdrrrpqw elspetkfiq advrdeealy rafegvdcvf hvasygmsga eklqkeqies
      121 invggtklvi dvcvrrrvpr liytstvnva fggkpieqgd edsvpyfpld ehvdhysrtk
      181 aiadqltlma ngmplpgggt lrtcvlrppg iygpeeqrhl prvaghikkr lfmfrfgdhk
      241 armnwvhvhn lvqahvlaae alttakgyva sgqayyindg esvnlfewma plfeklgysq
      301 pwiqvptswv yltaavmerl hlalrpicsl pplltrsevr svavthtfqi akaraqlgya
      361 pdkfrfadav elyvqsttrr prgstartll rlllrlllfl gllalalhfl glqplhaave
      421 rl
//
LOCUS       NP_775886               1184 aa            linear   PRI 09-DEC-2025
DEFINITION  von Willebrand factor A domain-containing protein 3A precursor
            [Homo sapiens].
ACCESSION   NP_775886 XP_001128580 XP_001131261
VERSION     NP_775886.3
DBSOURCE    REFSEQ: accession NM_173615.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1184)
  AUTHORS   Grunin,M., Beykin,G., Rahmani,E., Schweiger,R., Barel,G.,
            Hagbi-Levi,S., Elbaz-Hayoun,S., Rinsky,B., Ganiel,M., Carmi,S.,
            Halperin,E. and Chowers,I.
  TITLE     Association of a Variant in VWA3A with Response to Anti-Vascular
            Endothelial Growth Factor Treatment in Neovascular AMD
  JOURNAL   Invest Ophthalmol Vis Sci 61 (2), 48 (2020)
   PUBMED   32106291
REFERENCE   2  (residues 1 to 1184)
  AUTHORS   Smolen,C., Myers,S. and Girirajan,S.
  TITLE     16p12.2 Recurrent Deletion
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719193
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA240074.1, AK307544.1, DA102773.1, BC109295.1, AC009019.10 and
            BC038400.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 19, 2008 this sequence version replaced NP_775886.2.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2144333 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000389398.10/ ENSP00000374049.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..1184
                     /product="von Willebrand factor A domain-containing
                     protein 3A precursor"
                     /note="von Willebrand factor A domain-containing protein
                     3A"
                     /calculated_mol_wt=131296
     sig_peptide     1..24
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (A6NCI4.3)"
                     /calculated_mol_wt=2742
     mat_peptide     25..1184
                     /product="von Willebrand factor A domain-containing
                     protein 3A. /id=PRO_0000324623"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NCI4.3)"
                     /calculated_mol_wt=131296
     Region          40..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NCI4.3)"
     Region          169..324
                     /region_name="VWA_3"
                     /note="von Willebrand factor type A domain; pfam13768"
                     /db_xref="CDD:372716"
     Region          510..>618
                     /region_name="vWFA"
                     /note="Von Willebrand factor type A (vWA) domain was
                     originally found in the blood coagulation protein von
                     Willebrand factor (vWF). Typically, the vWA domain is made
                     up of approximately 200 amino acid residues folded into a
                     classic a/b para-rossmann type of...; cl00057"
                     /db_xref="CDD:469594"
     Site            order(517,585,617)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238119"
     Site            709
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (A6NCI4.3)"
     Region          729..780
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NCI4.3)"
     Region          963..1109
                     /region_name="vWFA"
                     /note="Von Willebrand factor type A (vWA) domain was
                     originally found in the blood coagulation protein von
                     Willebrand factor (vWF). Typically, the vWA domain is made
                     up of approximately 200 amino acid residues folded into a
                     classic a/b para-rossmann type of...; cl00057"
                     /db_xref="CDD:469594"
     Site            order(965,1034,1059)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238119"
     CDS             1..1184
                     /gene="VWA3A"
                     /coded_by="NM_173615.5:98..3652"
                     /db_xref="CCDS:CCDS45441.1"
                     /db_xref="GeneID:146177"
                     /db_xref="HGNC:HGNC:27088"
                     /db_xref="MIM:621113"
ORIGIN      
        1 mkkyrkisig cfamatqtsh vfhgqenmfl enhcirrntg rdskkplkqk nmnglgqnsd
       61 ngllvthvnq tqdllrlqgs etqssdweds edwlsahslk cqkltladli sqgtevleeg
      121 tnvvqkicfs tqiirhfesk lsdtievyqe riqwltensk kafglikgar vsilidvsai
      181 ssgpqkeefq kdlmslideq lshkeklfvl sfgtnagslw pdpmevsast lqelklwvkt
      241 lqpdggsnll qalkkiftlk gldslvaimr scpdqpseil sdyiqqstmg rdliihfity
      301 rcddqmppav lknlaeavrg yyhcyspkme hytsrdmdel laeiqkaqsl lshvqalqhs
      361 spcealtctm eeisteitng plisllpkpp khdapltief pnldktsaew lkvnglkakk
      421 lslyqvlapn afspveefvp ilqktvssti hekamiqfew hdgtvknihv dppflykyqq
      481 qlsramrmye rriewlslas rriwgtvcek rvvvlldisa tnsmyiihiq hslrllleeq
      541 lsnkdcfnli afgstieswr pemvpvshnn lqsawrwaln lrcrgsrnvl salrkavevd
      601 fkdkdkhqsq giylftggip dqdmptlsay maeacggcdl qlnvclfyvg epkmdttppa
      661 ryashtdtaa aykevtraag grfhwfgdtg iyesddinsi msemekalny sqkcaflmas
      721 lknhsgkvlg ssalpkekpk tlqlrsqpkk lcpprptvpl garmsikddp drekspplks
      781 lkwrplssrv gispaaaqpt kegmmelrrk tksreaetsl llfytekgnd vgsvykkypq
      841 grglrrtsss idlprkdtvc ssqewvakyg lkklkleisr cmgpncthqk sgqrsasakh
      901 csifpsveih gvvrhiqwtp remevyirhl ekvlrryvqr lqwllsgsrr lfgtvleskv
      961 cilldtsgsm gpylqqvkte lvlliweqlr kccdsfnlls faesfqswqd tlvettdaac
     1021 heamqwvthl qaqgstsilq allkafsfhd leglylltdg kpdtscslvl nevqklrekr
     1081 dvkvhtisln csdraavefl rklasftggr yhcpvgedtl skihslltkg finekdptlp
     1141 pfegddlril aqeitkarsf lwqaqsfrsq lqkkndaepk vtls
//
LOCUS       NP_001424986             213 aa            linear   PRI 09-DEC-2025
DEFINITION  transcription initiation factor TFIID subunit 8 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001424986 XP_016865734 XP_054210187
VERSION     NP_001424986.1
DBSOURCE    REFSEQ: accession NM_001438057.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 213)
  AUTHORS   Scheer,E., Luo,J., Bernardini,A., Ruffenach,F., Garnier,J.M.,
            Kolb-Cheynel,I., Gupta,K., Berger,I., Ranish,J. and Tora,L.
  TITLE     TAF8 regions important for TFIID lobe B assembly or for TAF2
            interactions are required for embryonic stem cell survival
  JOURNAL   J Biol Chem 297 (5), 101288 (2021)
   PUBMED   34634302
  REMARK    GeneRIF: TAF8 regions important for TFIID lobe B assembly or for
            TAF2 interactions are required for embryonic stem cell survival.
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 213)
  AUTHORS   El-Saafin,F., Curry,C., Ye,T., Garnier,J.M., Kolb-Cheynel,I.,
            Stierle,M., Downer,N.L., Dixon,M.P., Negroni,L., Berger,I.,
            Thomas,T., Voss,A.K., Dobyns,W., Devys,D. and Tora,L.
  TITLE     Homozygous TAF8 mutation in a patient with intellectual disability
            results in undetectable TAF8 protein, but preserved RNA polymerase
            II transcription
  JOURNAL   Hum Mol Genet 27 (12), 2171-2186 (2018)
   PUBMED   29648665
  REMARK    GeneRIF: TAF8 mutant protein with an unrelated C-terminus. The
            mutant TAF8 protein could not be detected in extracts from the
            patient's fibroblasts, indicating a loss of TAF8 function and that
            the mutation is most likely causative
REFERENCE   6  (residues 1 to 213)
  AUTHORS   Guermah,M., Ge,K., Chiang,C.M. and Roeder,R.G.
  TITLE     The TBN protein, which is essential for early embryonic mouse
            development, is an inducible TAFII implicated in adipogenesis
  JOURNAL   Mol Cell 12 (4), 991-1001 (2003)
   PUBMED   14580349
REFERENCE   7  (residues 1 to 213)
  AUTHORS   Tora,L.
  TITLE     A unified nomenclature for TATA box binding protein
            (TBP)-associated factors (TAFs) involved in RNA polymerase II
            transcription
  JOURNAL   Genes Dev 16 (6), 673-675 (2002)
   PUBMED   11963920
REFERENCE   8  (residues 1 to 213)
  AUTHORS   Guermah,M., Tao,Y. and Roeder,R.G.
  TITLE     Positive and negative TAF(II) functions that suggest a dynamic
            TFIID structure and elicit synergy with traps in activator-induced
            transcription
  JOURNAL   Mol Cell Biol 21 (20), 6882-6894 (2001)
   PUBMED   11564872
REFERENCE   9  (residues 1 to 213)
  AUTHORS   Purrello,M., Di Pietro,C., Viola,A., Rapisarda,A., Stevens,S.,
            Guermah,M., Tao,Y., Bonaiuto,C., Arcidiacono,A., Messina,A.,
            Sichel,G., Grzeschik,K.H. and Roeder,R.
  TITLE     Genomics and transcription analysis of human TFIID
  JOURNAL   Oncogene 16 (12), 1633-1638 (1998)
   PUBMED   9569032
REFERENCE   10 (residues 1 to 213)
  AUTHORS   Falik Zaccai,T.C. and Mesika,A.
  TITLE     TAF8-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41343687
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513008.14 and AL512274.9.
            
            On or before Apr 15, 2025 this sequence version replaced
            XP_016865734.1, XP_054210187.1.
            
            Summary: This gene encodes one of several TATA-binding protein
            (TBP)-associated factors (TAFs), which are integral subunits of the
            general transcription factor complex TFIID. TFIID recognizes the
            core promoter of many genes and nucleates the assembly of a
            transcription preinitiation complex containing RNA polymerase II
            and other initiation factors. The protein encoded by this gene
            contains an H4-like histone fold domain, and interacts with several
            subunits of TFIID including TBP and the histone-fold protein TAF10.
            Alternatively spliced transcript variants have been described, but
            their biological validity has not been determined. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.159131.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..213
                     /product="transcription initiation factor TFIID subunit 8
                     isoform 4"
                     /note="TATA box binding protein (TBP)-associated factor,
                     RNA polymerase II, A, 45/50kDa; TBP-associated factor 8;
                     TBP-associated factor, RNA polymerase II, 43 kD;
                     transcription initiation factor TFIID subunit 8;
                     TBP-associated factor TAFII43; hTAFII43; protein taube
                     nuss; TBP-associated factor 43 kDa; transcription
                     initiation factor TFIID 43 kDa subunit; taube nuss
                     homolog; TAF8 RNA polymerase II, TATA box binding protein
                     (TBP)-associated factor, 43kDa"
                     /calculated_mol_wt=22990
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Region          32..115
                     /region_name="HFD_TAF8"
                     /note="histone-fold domain found in transcription
                     initiation factor TFIID subunit 8 (TAF8) and similar
                     proteins; cd22918"
                     /db_xref="CDD:467043"
     Site            order(32,42,50..53,77,79,81..82,85,89,99)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467043"
     Site            order(33,36..37,40..41,43..45,48..51,54,56..57,60..61,
                     64..66,68..70,72..74,76..77,80,88..90,93..94,97,102,104,
                     106..108,110..115)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467043"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Region          145..191
                     /region_name="TAF8_C"
                     /note="Transcription factor TFIID complex subunit 8
                     C-term; pfam10406"
                     /db_xref="CDD:431262"
     CDS             1..213
                     /gene="TAF8"
                     /gene_synonym="II; NEDMLHB; TAF; TAF(II)43; TAFII-43;
                     TAFII43; TBN"
                     /coded_by="NM_001438057.1:19..660"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:129685"
                     /db_xref="HGNC:HGNC:17300"
                     /db_xref="MIM:609514"
ORIGIN      
        1 madaaataga ggsgtrsgsk qstnpadnyh larrrtlqvv vssllteagf esaekasvet
       61 ltemlqsyis eigrsaksyc ehtartqptl sdivvtlvem gfnvdtlpay akrsqrmvit
      121 appvtnqpvt pkaltagqnr phpphipshf pefpdphtyi ktpedsgaek entsvlqqnp
      181 slsgsrngee niidnpylrp vkkpkirrkk sls
//
LOCUS       NP_001397835             319 aa            linear   PRI 09-DEC-2025
DEFINITION  transcription initiation factor TFIID subunit 8 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001397835 XP_016865730
VERSION     NP_001397835.1
DBSOURCE    REFSEQ: accession NM_001410906.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Scheer,E., Luo,J., Bernardini,A., Ruffenach,F., Garnier,J.M.,
            Kolb-Cheynel,I., Gupta,K., Berger,I., Ranish,J. and Tora,L.
  TITLE     TAF8 regions important for TFIID lobe B assembly or for TAF2
            interactions are required for embryonic stem cell survival
  JOURNAL   J Biol Chem 297 (5), 101288 (2021)
   PUBMED   34634302
  REMARK    GeneRIF: TAF8 regions important for TFIID lobe B assembly or for
            TAF2 interactions are required for embryonic stem cell survival.
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 319)
  AUTHORS   El-Saafin,F., Curry,C., Ye,T., Garnier,J.M., Kolb-Cheynel,I.,
            Stierle,M., Downer,N.L., Dixon,M.P., Negroni,L., Berger,I.,
            Thomas,T., Voss,A.K., Dobyns,W., Devys,D. and Tora,L.
  TITLE     Homozygous TAF8 mutation in a patient with intellectual disability
            results in undetectable TAF8 protein, but preserved RNA polymerase
            II transcription
  JOURNAL   Hum Mol Genet 27 (12), 2171-2186 (2018)
   PUBMED   29648665
  REMARK    GeneRIF: TAF8 mutant protein with an unrelated C-terminus. The
            mutant TAF8 protein could not be detected in extracts from the
            patient's fibroblasts, indicating a loss of TAF8 function and that
            the mutation is most likely causative
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Guermah,M., Ge,K., Chiang,C.M. and Roeder,R.G.
  TITLE     The TBN protein, which is essential for early embryonic mouse
            development, is an inducible TAFII implicated in adipogenesis
  JOURNAL   Mol Cell 12 (4), 991-1001 (2003)
   PUBMED   14580349
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Tora,L.
  TITLE     A unified nomenclature for TATA box binding protein
            (TBP)-associated factors (TAFs) involved in RNA polymerase II
            transcription
  JOURNAL   Genes Dev 16 (6), 673-675 (2002)
   PUBMED   11963920
REFERENCE   8  (residues 1 to 319)
  AUTHORS   Guermah,M., Tao,Y. and Roeder,R.G.
  TITLE     Positive and negative TAF(II) functions that suggest a dynamic
            TFIID structure and elicit synergy with traps in activator-induced
            transcription
  JOURNAL   Mol Cell Biol 21 (20), 6882-6894 (2001)
   PUBMED   11564872
REFERENCE   9  (residues 1 to 319)
  AUTHORS   Purrello,M., Di Pietro,C., Viola,A., Rapisarda,A., Stevens,S.,
            Guermah,M., Tao,Y., Bonaiuto,C., Arcidiacono,A., Messina,A.,
            Sichel,G., Grzeschik,K.H. and Roeder,R.
  TITLE     Genomics and transcription analysis of human TFIID
  JOURNAL   Oncogene 16 (12), 1633-1638 (1998)
   PUBMED   9569032
REFERENCE   10 (residues 1 to 319)
  AUTHORS   Falik Zaccai,T.C. and Mesika,A.
  TITLE     TAF8-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41343687
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513008.14 and AL512274.9.
            
            On Aug 17, 2022 this sequence version replaced XP_016865730.1.
            
            Summary: This gene encodes one of several TATA-binding protein
            (TBP)-associated factors (TAFs), which are integral subunits of the
            general transcription factor complex TFIID. TFIID recognizes the
            core promoter of many genes and nucleates the assembly of a
            transcription preinitiation complex containing RNA polymerase II
            and other initiation factors. The protein encoded by this gene
            contains an H4-like histone fold domain, and interacts with several
            subunits of TFIID including TBP and the histone-fold protein TAF10.
            Alternatively spliced transcript variants have been described, but
            their biological validity has not been determined. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3655563.1,
                                           SRR18074969.988072.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..319
                     /product="transcription initiation factor TFIID subunit 8
                     isoform 2"
                     /note="TATA box binding protein (TBP)-associated factor,
                     RNA polymerase II, A, 45/50kDa; TBP-associated factor 8;
                     TBP-associated factor, RNA polymerase II, 43 kD;
                     transcription initiation factor TFIID subunit 8;
                     TBP-associated factor TAFII43; hTAFII43; protein taube
                     nuss; TBP-associated factor 43 kDa; transcription
                     initiation factor TFIID 43 kDa subunit; taube nuss
                     homolog; TAF8 RNA polymerase II, TATA box binding protein
                     (TBP)-associated factor, 43kDa"
                     /calculated_mol_wt=35154
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Region          32..115
                     /region_name="HFD_TAF8"
                     /note="histone-fold domain found in transcription
                     initiation factor TFIID subunit 8 (TAF8) and similar
                     proteins; cd22918"
                     /db_xref="CDD:467043"
     Site            order(32,42,50..53,77,79,81..82,85,89,99)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467043"
     Site            order(33,36..37,40..41,43..45,48..51,54,56..57,60..61,
                     64..66,68..70,72..74,76..77,80,88..90,93..94,97,102,104,
                     106..108,110..115)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467043"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Region          144..197
                     /region_name="TAF8"
                     /note="TATA Binding Protein (TBP) Associated Factor 8;
                     cd08049"
                     /db_xref="CDD:176263"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     CDS             1..319
                     /gene="TAF8"
                     /gene_synonym="II; NEDMLHB; TAF; TAF(II)43; TAFII-43;
                     TAFII43; TBN"
                     /coded_by="NM_001410906.1:19..978"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS93918.1"
                     /db_xref="GeneID:129685"
                     /db_xref="HGNC:HGNC:17300"
                     /db_xref="MIM:609514"
ORIGIN      
        1 madaaataga ggsgtrsgsk qstnpadnyh larrrtlqvv vssllteagf esaekasvet
       61 ltemlqsyis eigrsaksyc ehtartqptl sdivvtlvem gfnvdtlpay akrsqrmvit
      121 appvtnqpvt pkaltagqnr phpphipshf pefpdphtyi ktptyrepvs dyqvlrekaa
      181 sqrrdveral trfmaktget qslfkddvst fpliaarpft ipyltallps elemqqmeet
      241 dsseqdeqtd tenlalhism edsgaekent svlqqnpsls gsrngeenii dnpylrpvkk
      301 pkirrknrhg illccpgws
//
LOCUS       NP_001425510             222 aa            linear   PRI 09-DEC-2025
DEFINITION  transcription initiation factor TFIID subunit 8 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001425510 XP_016865733 XP_054210185
VERSION     NP_001425510.1
DBSOURCE    REFSEQ: accession NM_001438581.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Scheer,E., Luo,J., Bernardini,A., Ruffenach,F., Garnier,J.M.,
            Kolb-Cheynel,I., Gupta,K., Berger,I., Ranish,J. and Tora,L.
  TITLE     TAF8 regions important for TFIID lobe B assembly or for TAF2
            interactions are required for embryonic stem cell survival
  JOURNAL   J Biol Chem 297 (5), 101288 (2021)
   PUBMED   34634302
  REMARK    GeneRIF: TAF8 regions important for TFIID lobe B assembly or for
            TAF2 interactions are required for embryonic stem cell survival.
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 222)
  AUTHORS   El-Saafin,F., Curry,C., Ye,T., Garnier,J.M., Kolb-Cheynel,I.,
            Stierle,M., Downer,N.L., Dixon,M.P., Negroni,L., Berger,I.,
            Thomas,T., Voss,A.K., Dobyns,W., Devys,D. and Tora,L.
  TITLE     Homozygous TAF8 mutation in a patient with intellectual disability
            results in undetectable TAF8 protein, but preserved RNA polymerase
            II transcription
  JOURNAL   Hum Mol Genet 27 (12), 2171-2186 (2018)
   PUBMED   29648665
  REMARK    GeneRIF: TAF8 mutant protein with an unrelated C-terminus. The
            mutant TAF8 protein could not be detected in extracts from the
            patient's fibroblasts, indicating a loss of TAF8 function and that
            the mutation is most likely causative
REFERENCE   6  (residues 1 to 222)
  AUTHORS   Guermah,M., Ge,K., Chiang,C.M. and Roeder,R.G.
  TITLE     The TBN protein, which is essential for early embryonic mouse
            development, is an inducible TAFII implicated in adipogenesis
  JOURNAL   Mol Cell 12 (4), 991-1001 (2003)
   PUBMED   14580349
REFERENCE   7  (residues 1 to 222)
  AUTHORS   Tora,L.
  TITLE     A unified nomenclature for TATA box binding protein
            (TBP)-associated factors (TAFs) involved in RNA polymerase II
            transcription
  JOURNAL   Genes Dev 16 (6), 673-675 (2002)
   PUBMED   11963920
REFERENCE   8  (residues 1 to 222)
  AUTHORS   Guermah,M., Tao,Y. and Roeder,R.G.
  TITLE     Positive and negative TAF(II) functions that suggest a dynamic
            TFIID structure and elicit synergy with traps in activator-induced
            transcription
  JOURNAL   Mol Cell Biol 21 (20), 6882-6894 (2001)
   PUBMED   11564872
REFERENCE   9  (residues 1 to 222)
  AUTHORS   Purrello,M., Di Pietro,C., Viola,A., Rapisarda,A., Stevens,S.,
            Guermah,M., Tao,Y., Bonaiuto,C., Arcidiacono,A., Messina,A.,
            Sichel,G., Grzeschik,K.H. and Roeder,R.
  TITLE     Genomics and transcription analysis of human TFIID
  JOURNAL   Oncogene 16 (12), 1633-1638 (1998)
   PUBMED   9569032
REFERENCE   10 (residues 1 to 222)
  AUTHORS   Falik Zaccai,T.C. and Mesika,A.
  TITLE     TAF8-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41343687
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513008.14 and AL512274.9.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_016865733.1, XP_054210185.1.
            
            Summary: This gene encodes one of several TATA-binding protein
            (TBP)-associated factors (TAFs), which are integral subunits of the
            general transcription factor complex TFIID. TFIID recognizes the
            core promoter of many genes and nucleates the assembly of a
            transcription preinitiation complex containing RNA polymerase II
            and other initiation factors. The protein encoded by this gene
            contains an H4-like histone fold domain, and interacts with several
            subunits of TFIID including TBP and the histone-fold protein TAF10.
            Alternatively spliced transcript variants have been described, but
            their biological validity has not been determined. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2252143.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245, SAMEA2145313
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..222
                     /product="transcription initiation factor TFIID subunit 8
                     isoform 6"
                     /note="TATA box binding protein (TBP)-associated factor,
                     RNA polymerase II, A, 45/50kDa; TBP-associated factor 8;
                     TBP-associated factor, RNA polymerase II, 43 kD;
                     transcription initiation factor TFIID subunit 8;
                     TBP-associated factor TAFII43; hTAFII43; protein taube
                     nuss; TBP-associated factor 43 kDa; transcription
                     initiation factor TFIID 43 kDa subunit; taube nuss
                     homolog; TAF8 RNA polymerase II, TATA box binding protein
                     (TBP)-associated factor, 43kDa"
                     /calculated_mol_wt=24012
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Region          32..115
                     /region_name="HFD_TAF8"
                     /note="histone-fold domain found in transcription
                     initiation factor TFIID subunit 8 (TAF8) and similar
                     proteins; cd22918"
                     /db_xref="CDD:467043"
     Site            order(32,42,50..53,77,79,81..82,85,89,99)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467043"
     Site            order(33,36..37,40..41,43..45,48..51,54,56..57,60..61,
                     64..66,68..70,72..74,76..77,80,88..90,93..94,97,102,104,
                     106..108,110..115)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467043"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Region          145..193
                     /region_name="TAF8_C"
                     /note="Transcription factor TFIID complex subunit 8
                     C-term; pfam10406"
                     /db_xref="CDD:431262"
     CDS             1..222
                     /gene="TAF8"
                     /gene_synonym="II; NEDMLHB; TAF; TAF(II)43; TAFII-43;
                     TAFII43; TBN"
                     /coded_by="NM_001438581.1:19..687"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:129685"
                     /db_xref="HGNC:HGNC:17300"
                     /db_xref="MIM:609514"
ORIGIN      
        1 madaaataga ggsgtrsgsk qstnpadnyh larrrtlqvv vssllteagf esaekasvet
       61 ltemlqsyis eigrsaksyc ehtartqptl sdivvtlvem gfnvdtlpay akrsqrmvit
      121 appvtnqpvt pkaltagqnr phpphipshf pefpdphtyi ktpedsgaek entsvlqqnp
      181 slsgsrngee niidnpylrp vkkpkirrkn rhgillccpg ws
//
LOCUS       NP_001425511             214 aa            linear   PRI 09-DEC-2025
DEFINITION  transcription initiation factor TFIID subunit 8 isoform 7 [Homo
            sapiens].
ACCESSION   NP_001425511 XP_047274134 XP_054210186
VERSION     NP_001425511.1
DBSOURCE    REFSEQ: accession NM_001438582.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Scheer,E., Luo,J., Bernardini,A., Ruffenach,F., Garnier,J.M.,
            Kolb-Cheynel,I., Gupta,K., Berger,I., Ranish,J. and Tora,L.
  TITLE     TAF8 regions important for TFIID lobe B assembly or for TAF2
            interactions are required for embryonic stem cell survival
  JOURNAL   J Biol Chem 297 (5), 101288 (2021)
   PUBMED   34634302
  REMARK    GeneRIF: TAF8 regions important for TFIID lobe B assembly or for
            TAF2 interactions are required for embryonic stem cell survival.
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 214)
  AUTHORS   El-Saafin,F., Curry,C., Ye,T., Garnier,J.M., Kolb-Cheynel,I.,
            Stierle,M., Downer,N.L., Dixon,M.P., Negroni,L., Berger,I.,
            Thomas,T., Voss,A.K., Dobyns,W., Devys,D. and Tora,L.
  TITLE     Homozygous TAF8 mutation in a patient with intellectual disability
            results in undetectable TAF8 protein, but preserved RNA polymerase
            II transcription
  JOURNAL   Hum Mol Genet 27 (12), 2171-2186 (2018)
   PUBMED   29648665
  REMARK    GeneRIF: TAF8 mutant protein with an unrelated C-terminus. The
            mutant TAF8 protein could not be detected in extracts from the
            patient's fibroblasts, indicating a loss of TAF8 function and that
            the mutation is most likely causative
REFERENCE   6  (residues 1 to 214)
  AUTHORS   Guermah,M., Ge,K., Chiang,C.M. and Roeder,R.G.
  TITLE     The TBN protein, which is essential for early embryonic mouse
            development, is an inducible TAFII implicated in adipogenesis
  JOURNAL   Mol Cell 12 (4), 991-1001 (2003)
   PUBMED   14580349
REFERENCE   7  (residues 1 to 214)
  AUTHORS   Tora,L.
  TITLE     A unified nomenclature for TATA box binding protein
            (TBP)-associated factors (TAFs) involved in RNA polymerase II
            transcription
  JOURNAL   Genes Dev 16 (6), 673-675 (2002)
   PUBMED   11963920
REFERENCE   8  (residues 1 to 214)
  AUTHORS   Guermah,M., Tao,Y. and Roeder,R.G.
  TITLE     Positive and negative TAF(II) functions that suggest a dynamic
            TFIID structure and elicit synergy with traps in activator-induced
            transcription
  JOURNAL   Mol Cell Biol 21 (20), 6882-6894 (2001)
   PUBMED   11564872
REFERENCE   9  (residues 1 to 214)
  AUTHORS   Purrello,M., Di Pietro,C., Viola,A., Rapisarda,A., Stevens,S.,
            Guermah,M., Tao,Y., Bonaiuto,C., Arcidiacono,A., Messina,A.,
            Sichel,G., Grzeschik,K.H. and Roeder,R.
  TITLE     Genomics and transcription analysis of human TFIID
  JOURNAL   Oncogene 16 (12), 1633-1638 (1998)
   PUBMED   9569032
REFERENCE   10 (residues 1 to 214)
  AUTHORS   Falik Zaccai,T.C. and Mesika,A.
  TITLE     TAF8-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41343687
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL513008.14 and AL512274.9.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047274134.1, XP_054210186.1.
            
            Summary: This gene encodes one of several TATA-binding protein
            (TBP)-associated factors (TAFs), which are integral subunits of the
            general transcription factor complex TFIID. TFIID recognizes the
            core promoter of many genes and nucleates the assembly of a
            transcription preinitiation complex containing RNA polymerase II
            and other initiation factors. The protein encoded by this gene
            contains an H4-like histone fold domain, and interacts with several
            subunits of TFIID including TBP and the histone-fold protein TAF10.
            Alternatively spliced transcript variants have been described, but
            their biological validity has not been determined. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1031323.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146236, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..214
                     /product="transcription initiation factor TFIID subunit 8
                     isoform 7"
                     /note="TATA box binding protein (TBP)-associated factor,
                     RNA polymerase II, A, 45/50kDa; TBP-associated factor 8;
                     TBP-associated factor, RNA polymerase II, 43 kD;
                     transcription initiation factor TFIID subunit 8;
                     TBP-associated factor TAFII43; hTAFII43; protein taube
                     nuss; TBP-associated factor 43 kDa; transcription
                     initiation factor TFIID 43 kDa subunit; taube nuss
                     homolog; TAF8 RNA polymerase II, TATA box binding protein
                     (TBP)-associated factor, 43kDa"
                     /calculated_mol_wt=23163
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Region          32..115
                     /region_name="HFD_TAF8"
                     /note="histone-fold domain found in transcription
                     initiation factor TFIID subunit 8 (TAF8) and similar
                     proteins; cd22918"
                     /db_xref="CDD:467043"
     Site            order(32,42,50..53,77,79,81..82,85,89,99)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467043"
     Site            order(33,36..37,40..41,43..45,48..51,54,56..57,60..61,
                     64..66,68..70,72..74,76..77,80,88..90,93..94,97,102,104,
                     106..108,110..115)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:467043"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z7C8.1)"
     Region          145..193
                     /region_name="TAF8_C"
                     /note="Transcription factor TFIID complex subunit 8
                     C-term; pfam10406"
                     /db_xref="CDD:431262"
     CDS             1..214
                     /gene="TAF8"
                     /gene_synonym="II; NEDMLHB; TAF; TAF(II)43; TAFII-43;
                     TAFII43; TBN"
                     /coded_by="NM_001438582.1:19..663"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:129685"
                     /db_xref="HGNC:HGNC:17300"
                     /db_xref="MIM:609514"
ORIGIN      
        1 madaaataga ggsgtrsgsk qstnpadnyh larrrtlqvv vssllteagf esaekasvet
       61 ltemlqsyis eigrsaksyc ehtartqptl sdivvtlvem gfnvdtlpay akrsqrmvit
      121 appvtnqpvt pkaltagqnr phpphipshf pefpdphtyi ktpedsgaek entsvlqqnp
      181 slsgsrngee niidnpylrp vkkpkirrkk pdtf
//
LOCUS       NP_001793                454 aa            linear   PRI 09-DEC-2025
DEFINITION  cerebellar degeneration-related protein 2 [Homo sapiens].
ACCESSION   NP_001793 XP_071866
VERSION     NP_001793.1
DBSOURCE    REFSEQ: accession NM_001802.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Erikstad,K.I., Herdlevaer,I., Peter,E., Haugen,M., Totland,C. and
            Vedeler,C.
  TITLE     A cerebellar degeneration-related protein 2-like cell-based assay
            for anti-Yo detection in patients with paraneoplastic cerebellar
            degeneration
  JOURNAL   Eur J Neurol 30 (6), 1727-1733 (2023)
   PUBMED   36912432
  REMARK    GeneRIF: A cerebellar degeneration-related protein 2-like
            cell-based assay for anti-Yo detection in patients with
            paraneoplastic cerebellar degeneration.
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Mo,J.S. and Chae,S.C.
  TITLE     MicroRNA 452 regulates ASB8, NOL8, and CDR2 expression in
            colorectal cancer cells
  JOURNAL   Genes Genomics 43 (1), 33-41 (2021)
   PUBMED   33398662
  REMARK    GeneRIF: MicroRNA 452 regulates ASB8, NOL8, and CDR2 expression in
            colorectal cancer cells.
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 454)
  AUTHORS   Smolen,C., Myers,S. and Girirajan,S.
  TITLE     16p12.2 Recurrent Deletion
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719193
REFERENCE   7  (residues 1 to 454)
  AUTHORS   Gress,T., Baldini,A., Rocchi,M., Furneaux,H., Posner,J.B. and
            Siniscalco,M.
  TITLE     In situ mapping of the gene coding for a leucine zipper DNA binding
            protein (CDR62) to 16p12-16p13.1
  JOURNAL   Genomics 13 (4), 1340-1342 (1992)
   PUBMED   1505970
REFERENCE   8  (residues 1 to 454)
  AUTHORS   Sakai,K., Mitchell,D.J., Tsukamoto,T. and Steinman,L.
  TITLE     Isolation of a complementary DNA clone encoding an autoantigen
            recognized by an anti-neuronal cell antibody from a patient with
            paraneoplastic cerebellar degeneration
  JOURNAL   Ann Neurol 30 (5), 738 (1991)
   PUBMED   1763903
  REMARK    Correction to:[Ann Neurol. 1990 Nov;28(5):692-8. doi:
            10.1002/ana.410280515. PMID: 2260856]
REFERENCE   9  (residues 1 to 454)
  AUTHORS   Fathallah-Shaykh,H., Wolf,S., Wong,E., Posner,J.B. and
            Furneaux,H.M.
  TITLE     Cloning of a leucine-zipper protein recognized by the sera of
            patients with antibody-associated paraneoplastic cerebellar
            degeneration
  JOURNAL   Proc Natl Acad Sci U S A 88 (8), 3451-3454 (1991)
   PUBMED   2014264
REFERENCE   10 (residues 1 to 454)
  AUTHORS   Sakai,K., Mitchell,D.J., Tsukamoto,T. and Steinman,L.
  TITLE     Isolation of a complementary DNA clone encoding an autoantigen
            recognized by an anti-neuronal cell antibody from a patient with
            paraneoplastic cerebellar degeneration
  JOURNAL   Ann Neurol 28 (5), 692-698 (1990)
   PUBMED   2260856
  REMARK    Erratum:[Ann Neurol. 1991 Nov;30(5):738. doi:
            10.1002/ana.410300523. PMID: 1763903]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092338.4, CB990819.1, BG386156.1, BG750955.1, BC017503.1,
            M63256.1 and BM714067.1.
            
            On Nov 22, 2004 this sequence version replaced XP_071866.5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017503.1, SRR1163658.234190.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268383.7/ ENSP00000268383.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..454
                     /product="cerebellar degeneration-related protein 2"
                     /note="Yo paraneoplastic antigen; major Yo paraneoplastic
                     antigen; paraneoplastic cerebellar degeneration-associated
                     antigen; cerebellar degeneration-related protein 2, 62kDa"
                     /calculated_mol_wt=51724
     Region          <8..>263
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          134..153
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01850.2)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01850.2)"
     CDS             1..454
                     /gene="CDR2"
                     /gene_synonym="CDR62; Yo"
                     /coded_by="NM_001802.2:311..1675"
                     /db_xref="CCDS:CCDS32404.1"
                     /db_xref="GeneID:1039"
                     /db_xref="HGNC:HGNC:1799"
                     /db_xref="MIM:117340"
ORIGIN      
        1 mlaenlveef emkedepwyd hqdlqqdlql aaelgktlld rnteledsvq qmyttnqeql
       61 qeieyltkqv ellrqmneqh akvyeqldvt areleetnqk lvadskasqq kilsltetie
      121 clqtnidhlq sqveelkssg qgrrspgkcd qekpapsfac lkelydlrqh fvydhvfaek
      181 itslqgqpsp deeenehlkk tvtmlqaqls lerqkrvtme eeyglvlken seleqqlgat
      241 gayraralel eaevaemrqm lqsehpfvng veklvpdsly vpfkepsqsl leemfltvpe
      301 shrkplkrss setilsslag sdivkgheet cirrakavkq rgisllhevd tqysalkvky
      361 eellkkcqee qdslshkavq tsraaakdlt gvnaqsepva sgwelasvnp epvsspttpp
      421 eykalfkeif scikktkqei deqrtkyrsl sshs
//
LOCUS       NP_001129666             710 aa            linear   PRI 09-DEC-2025
DEFINITION  FAST kinase domain-containing protein 2, mitochondrial [Homo
            sapiens].
ACCESSION   NP_001129666
VERSION     NP_001129666.1
DBSOURCE    REFSEQ: accession NM_001136194.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Wu,T., Mao,L., Chen,C., Yin,F. and Peng,J.
  TITLE     A novel homozygous missense mutation in the FASTKD2 gene leads to
            Lennox-Gastaut syndrome
  JOURNAL   J Hum Genet 67 (10), 589-594 (2022)
   PUBMED   35729327
  REMARK    GeneRIF: A novel homozygous missense mutation in the FASTKD2 gene
            leads to Lennox-Gastaut syndrome.
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Lim,S.H., Snider,J., Birimberg-Schwartz,L., Ip,W., Serralha,J.C.,
            Botelho,H.M., Lopes-Pacheco,M., Pinto,M.C., Moutaoufik,M.T.,
            Zilocchi,M., Laselva,O., Esmaeili,M., Kotlyar,M., Lyakisheva,A.,
            Tang,P., Lopez Vazquez,L., Akula,I., Aboualizadeh,F., Wong,V.,
            Grozavu,I., Opacak-Bernardi,T., Yao,Z., Mendoza,M., Babu,M.,
            Jurisica,I., Gonska,T., Bear,C.E., Amaral,M.D. and Stagljar,I.
  TITLE     CFTR interactome mapping using the mammalian membrane two-hybrid
            high-throughput screening system
  JOURNAL   Mol Syst Biol 18 (2), e10629 (2022)
   PUBMED   35156780
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 710)
  AUTHORS   Simarro,M., Gimenez-Cassina,A., Kedersha,N., Lazaro,J.B.,
            Adelmant,G.O., Marto,J.A., Rhee,K., Tisdale,S., Danial,N.,
            Benarafa,C., Orduna,A. and Anderson,P.
  TITLE     Fast kinase domain-containing protein 3 is a mitochondrial protein
            essential for cellular respiration
  JOURNAL   Biochem Biophys Res Commun 401 (3), 440-446 (2010)
   PUBMED   20869947
REFERENCE   6  (residues 1 to 710)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 710)
  AUTHORS   Ghezzi,D., Saada,A., D'Adamo,P., Fernandez-Vizarra,E.,
            Gasparini,P., Tiranti,V., Elpeleg,O. and Zeviani,M.
  TITLE     FASTKD2 nonsense mutation in an infantile mitochondrial
            encephalomyopathy associated with cytochrome c oxidase deficiency
  JOURNAL   Am J Hum Genet 83 (3), 415-423 (2008)
   PUBMED   18771761
  REMARK    GeneRIF: mutation in a gene segregating with a peculiar
            mitochondrial encephalomyopathy associated with COX deficiency in
            skeletal muscle. FASTKD2 is localized in the mitochondrial inner
            compartment.
REFERENCE   8  (residues 1 to 710)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
REFERENCE   9  (residues 1 to 710)
  AUTHORS   Patil,S.J., Kaur,N. and Shukla,A.
  TITLE     FASTKD2-Related Combined Oxidative Phosphorylation Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41343688
REFERENCE   10 (residues 1 to 710)
  AUTHORS   Rahman,S., Thorburn,D.R. and Ball,M.
  TITLE     Nuclear Gene-Encoded Leigh Syndrome Spectrum Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26425749
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA756417.1, BC001544.1 and
            AC008269.4.
            
            Summary: This gene encodes a protein that is localized in the
            mitochondrial inner compartment and that may play a role in
            mitochondrial apoptosis. Nonsense mutations have been reported to
            result in cytochrome c oxidase deficiency. [provided by RefSeq, Oct
            2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. All three variants encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4526326.1,
                                           SRR14038193.1421259.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.3"
     Protein         1..710
                     /product="FAST kinase domain-containing protein 2,
                     mitochondrial"
                     /calculated_mol_wt=81332
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NYY8.1)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NYY8.1)"
     Region          181..407
                     /region_name="RESC6-like"
                     /note="RNA-editing substrate-binding complex subunit 6
                     (RESC6) and related proteins; cl46254"
                     /db_xref="CDD:480594"
     Region          456..529
                     /region_name="FAST_1"
                     /note="FAST kinase-like protein, subdomain 1; pfam06743"
                     /db_xref="CDD:461999"
     Region          <578..619
                     /region_name="FAST_2"
                     /note="FAST kinase-like protein, subdomain 2; pfam08368"
                     /db_xref="CDD:462448"
     Region          636..692
                     /region_name="RAP"
                     /note="This domain is found in various eukaryotic species,
                     particularly in apicomplexans; smart00952"
                     /db_xref="CDD:214932"
     Site            708
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NYY8.1)"
     CDS             1..710
                     /gene="FASTKD2"
                     /gene_synonym="COXPD44; KIAA0971"
                     /coded_by="NM_001136194.2:208..2340"
                     /db_xref="CCDS:CCDS2371.1"
                     /db_xref="GeneID:22868"
                     /db_xref="HGNC:HGNC:29160"
                     /db_xref="MIM:612322"
ORIGIN      
        1 mlttlkpfgs vsveskmnnk agsffwnlrq fstlvstsrt mrlcclglck pkivhsnwni
       61 lnnfhnrmqs tdiirylfqd afifksdvgf qtkgistlta lrierllyak rlffdskqsl
      121 vpvdksddel kkvnlnhevs nedvltketk pnrissrkls eecnslsdvl dafskaptfp
      181 ssnyftamwt iakrlsddqk rfekrlmfsh pafnqlcehm mreakimqyk yllfslhaiv
      241 klgipqntil vqtllrvtqe rinecdeicl svlstvleam epcknvhvlr tgfrilvdqq
      301 vwkiedvftl qvvmkcigkd apialkrkle mkalreldrf svlnsqhmfe vlaamnhrsl
      361 illdecskvv ldnihgcplr iminilqsck dlqyhnldlf kgladyvaat fdiwkfrkvl
      421 fililfenlg frpvglmdlf mkrivedpes lnmknilsil htysslnhvy kcqnkeqfve
      481 vmasaltgyl htissenlld avysfclmny fplapfnqll qkdiisellt sddmknaykl
      541 htldtclkld dtvylrdial slpqlprelp sshtnakvae vlssllggeg hfskdvhlph
      601 nyhidfeirm dtnrnqvlpl sdvdttsatd iqrvavlcvs rsayclgssh prgflamkmr
      661 hlnamgfhvi lvnnwemdkl emedavtflk tkiysvealp vaavnvqstq
//
LOCUS       NP_001158051             167 aa            linear   PRI 09-DEC-2025
DEFINITION  modulator of smoothened protein precursor [Homo sapiens].
ACCESSION   NP_001158051
VERSION     NP_001158051.1
DBSOURCE    REFSEQ: accession NM_001164579.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Pusapati,G.V., Kong,J.H., Patel,B.B., Krishnan,A., Sagner,A.,
            Kinnebrew,M., Briscoe,J., Aravind,L. and Rohatgi,R.
  TITLE     CRISPR Screens Uncover Genes that Regulate Target Cell Sensitivity
            to the Morphogen Sonic Hedgehog
  JOURNAL   Dev Cell 44 (1), 113-129 (2018)
   PUBMED   29290584
  REMARK    Erratum:[Dev Cell. 2018 Jan 22;44(2):271. doi:
            10.1016/j.devcel.2018.01.002. PMID: 29401421]
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Martin,J., Han,C., Gordon,L.A., Terry,A., Prabhakar,S., She,X.,
            Xie,G., Hellsten,U., Chan,Y.M., Altherr,M., Couronne,O., Aerts,A.,
            Bajorek,E., Black,S., Blumer,H., Branscomb,E., Brown,N.C.,
            Bruno,W.J., Buckingham,J.M., Callen,D.F., Campbell,C.S.,
            Campbell,M.L., Campbell,E.W., Caoile,C., Challacombe,J.F.,
            Chasteen,L.A., Chertkov,O., Chi,H.C., Christensen,M., Clark,L.M.,
            Cohn,J.D., Denys,M., Detter,J.C., Dickson,M.,
            Dimitrijevic-Bussod,M., Escobar,J., Fawcett,J.J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Goodwin,L.A., Grady,D.L., Grigoriev,I., Groza,M., Hammon,N.,
            Hawkins,T., Haydu,L., Hildebrand,C.E., Huang,W., Israni,S.,
            Jett,J., Jewett,P.B., Kadner,K., Kimball,H., Kobayashi,A.,
            Krawczyk,M.C., Leyba,T., Longmire,J.L., Lopez,F., Lou,Y., Lowry,S.,
            Ludeman,T., Manohar,C.F., Mark,G.A., McMurray,K.L., Meincke,L.J.,
            Morgan,J., Moyzis,R.K., Mundt,M.O., Munk,A.C., Nandkeshwar,R.D.,
            Pitluck,S., Pollard,M., Predki,P., Parson-Quintana,B., Ramirez,L.,
            Rash,S., Retterer,J., Ricke,D.O., Robinson,D.L., Rodriguez,A.,
            Salamov,A., Saunders,E.H., Scott,D., Shough,T., Stallings,R.L.,
            Stalvey,M., Sutherland,R.D., Tapia,R., Tesmer,J.G., Thayer,N.,
            Thompson,L.S., Tice,H., Torney,D.C., Tran-Gyamfi,M., Tsai,M.,
            Ulanovsky,L.E., Ustaszewska,A., Vo,N., White,P.S., Williams,A.L.,
            Wills,P.L., Wu,J.R., Wu,K., Yang,J., Dejong,P., Bruce,D.,
            Doggett,N.A., Deaven,L., Schmutz,J., Grimwood,J., Richardson,P.,
            Rokhsar,D.S., Eichler,E.E., Gilna,P., Lucas,S.M., Myers,R.M.,
            Rubin,E.M. and Pennacchio,L.A.
  TITLE     The sequence and analysis of duplication-rich human chromosome 16
  JOURNAL   Nature 432 (7020), 988-994 (2004)
   PUBMED   15616553
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Smolen,C., Myers,S. and Girirajan,S.
  TITLE     16p12.2 Recurrent Deletion
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719193
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092119.3 and AC009019.10.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.156092.1,
                                           SRR1803611.296302.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000542527.7/ ENSP00000454926.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..167
                     /product="modulator of smoothened protein precursor"
                     /note="uncharacterized protein C16orf52; Attenuator of
                     Hedgehog; modulator of smoothened protein"
                     /calculated_mol_wt=16041
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2227
     Site            7..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHV5.3)"
     Region          25..166
                     /region_name="Atthog"
                     /note="Attenuator of Hedgehog; pfam18800"
                     /db_xref="CDD:436747"
     Site            68..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHV5.3)"
     Site            101..121
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHV5.3)"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NHV5.3)"
     Site            139..159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHV5.3)"
     CDS             1..167
                     /gene="MOSMO"
                     /gene_synonym="ATTHOG; BC030336; C16orf52"
                     /coded_by="NM_001164579.2:192..695"
                     /db_xref="CCDS:CCDS58431.1"
                     /db_xref="GeneID:730094"
                     /db_xref="HGNC:HGNC:27087"
ORIGIN      
        1 mdkltiisgc lflaadifai asianpdwin tgesagaltv glvrqcqtih grdrtcippr
       61 lppewvttlf fiimgiislt vtcgllvash wrreatkyar wiaftgmilf cmaalifpig
      121 fyinevggqp yklpnntvvg ssyvlfvlsi fftivgllfa gkvclpg
//
LOCUS       NP_001357459             202 aa            linear   PRI 09-DEC-2025
DEFINITION  PDZ domain-containing protein 9 isoform 2 [Homo sapiens].
ACCESSION   NP_001357459
VERSION     NP_001357459.1
DBSOURCE    REFSEQ: accession NM_001370530.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Martin,J., Han,C., Gordon,L.A., Terry,A., Prabhakar,S., She,X.,
            Xie,G., Hellsten,U., Chan,Y.M., Altherr,M., Couronne,O., Aerts,A.,
            Bajorek,E., Black,S., Blumer,H., Branscomb,E., Brown,N.C.,
            Bruno,W.J., Buckingham,J.M., Callen,D.F., Campbell,C.S.,
            Campbell,M.L., Campbell,E.W., Caoile,C., Challacombe,J.F.,
            Chasteen,L.A., Chertkov,O., Chi,H.C., Christensen,M., Clark,L.M.,
            Cohn,J.D., Denys,M., Detter,J.C., Dickson,M.,
            Dimitrijevic-Bussod,M., Escobar,J., Fawcett,J.J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Goodwin,L.A., Grady,D.L., Grigoriev,I., Groza,M., Hammon,N.,
            Hawkins,T., Haydu,L., Hildebrand,C.E., Huang,W., Israni,S.,
            Jett,J., Jewett,P.B., Kadner,K., Kimball,H., Kobayashi,A.,
            Krawczyk,M.C., Leyba,T., Longmire,J.L., Lopez,F., Lou,Y., Lowry,S.,
            Ludeman,T., Manohar,C.F., Mark,G.A., McMurray,K.L., Meincke,L.J.,
            Morgan,J., Moyzis,R.K., Mundt,M.O., Munk,A.C., Nandkeshwar,R.D.,
            Pitluck,S., Pollard,M., Predki,P., Parson-Quintana,B., Ramirez,L.,
            Rash,S., Retterer,J., Ricke,D.O., Robinson,D.L., Rodriguez,A.,
            Salamov,A., Saunders,E.H., Scott,D., Shough,T., Stallings,R.L.,
            Stalvey,M., Sutherland,R.D., Tapia,R., Tesmer,J.G., Thayer,N.,
            Thompson,L.S., Tice,H., Torney,D.C., Tran-Gyamfi,M., Tsai,M.,
            Ulanovsky,L.E., Ustaszewska,A., Vo,N., White,P.S., Williams,A.L.,
            Wills,P.L., Wu,J.R., Wu,K., Yang,J., Dejong,P., Bruce,D.,
            Doggett,N.A., Deaven,L., Schmutz,J., Grimwood,J., Richardson,P.,
            Rokhsar,D.S., Eichler,E.E., Gilna,P., Lucas,S.M., Myers,R.M.,
            Rubin,E.M. and Pennacchio,L.A.
  TITLE     The sequence and analysis of duplication-rich human chromosome 16
  JOURNAL   Nature 432 (7020), 988-994 (2004)
   PUBMED   15616553
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Smolen,C., Myers,S. and Girirajan,S.
  TITLE     16p12.2 Recurrent Deletion
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719193
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092119.3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028605.1, SRR5189661.187968.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..202
                     /product="PDZ domain-containing protein 9 isoform 2"
                     /note="PDZ domain-containing protein C16orf65; PDZ
                     domain-containing protein 9"
                     /calculated_mol_wt=23013
     Region          <9..47
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     CDS             1..202
                     /gene="PDZD9"
                     /gene_synonym="C16orf65"
                     /coded_by="NM_001370530.1:327..935"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:255762"
                     /db_xref="HGNC:HGNC:28740"
ORIGIN      
        1 maegeeeggd vlisvghanv lgytlreflq llqhitigtv lqikvyrdfi nipeewqeiy
       61 dlipeakfpv tstpkkiela kdesftssdd nenvdldkrl qyyrypwstv hhparrpisi
      121 srdwhgykkk nhtisvgkdi ncdvmihrdd kkevrapspy wimvkqdnes sssstsstsd
      181 afwledcaqv eegkaqlvsk vg
//
LOCUS       NP_776167                204 aa            linear   PRI 09-DEC-2025
DEFINITION  PDZ domain-containing protein 9 isoform 1 [Homo sapiens].
ACCESSION   NP_776167
VERSION     NP_776167.2
DBSOURCE    REFSEQ: accession NM_173806.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Martin,J., Han,C., Gordon,L.A., Terry,A., Prabhakar,S., She,X.,
            Xie,G., Hellsten,U., Chan,Y.M., Altherr,M., Couronne,O., Aerts,A.,
            Bajorek,E., Black,S., Blumer,H., Branscomb,E., Brown,N.C.,
            Bruno,W.J., Buckingham,J.M., Callen,D.F., Campbell,C.S.,
            Campbell,M.L., Campbell,E.W., Caoile,C., Challacombe,J.F.,
            Chasteen,L.A., Chertkov,O., Chi,H.C., Christensen,M., Clark,L.M.,
            Cohn,J.D., Denys,M., Detter,J.C., Dickson,M.,
            Dimitrijevic-Bussod,M., Escobar,J., Fawcett,J.J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Goodwin,L.A., Grady,D.L., Grigoriev,I., Groza,M., Hammon,N.,
            Hawkins,T., Haydu,L., Hildebrand,C.E., Huang,W., Israni,S.,
            Jett,J., Jewett,P.B., Kadner,K., Kimball,H., Kobayashi,A.,
            Krawczyk,M.C., Leyba,T., Longmire,J.L., Lopez,F., Lou,Y., Lowry,S.,
            Ludeman,T., Manohar,C.F., Mark,G.A., McMurray,K.L., Meincke,L.J.,
            Morgan,J., Moyzis,R.K., Mundt,M.O., Munk,A.C., Nandkeshwar,R.D.,
            Pitluck,S., Pollard,M., Predki,P., Parson-Quintana,B., Ramirez,L.,
            Rash,S., Retterer,J., Ricke,D.O., Robinson,D.L., Rodriguez,A.,
            Salamov,A., Saunders,E.H., Scott,D., Shough,T., Stallings,R.L.,
            Stalvey,M., Sutherland,R.D., Tapia,R., Tesmer,J.G., Thayer,N.,
            Thompson,L.S., Tice,H., Torney,D.C., Tran-Gyamfi,M., Tsai,M.,
            Ulanovsky,L.E., Ustaszewska,A., Vo,N., White,P.S., Williams,A.L.,
            Wills,P.L., Wu,J.R., Wu,K., Yang,J., Dejong,P., Bruce,D.,
            Doggett,N.A., Deaven,L., Schmutz,J., Grimwood,J., Richardson,P.,
            Rokhsar,D.S., Eichler,E.E., Gilna,P., Lucas,S.M., Myers,R.M.,
            Rubin,E.M. and Pennacchio,L.A.
  TITLE     The sequence and analysis of duplication-rich human chromosome 16
  JOURNAL   Nature 432 (7020), 988-994 (2004)
   PUBMED   15616553
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Smolen,C., Myers,S. and Girirajan,S.
  TITLE     16p12.2 Recurrent Deletion
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719193
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092119.3.
            
            On May 26, 2010 this sequence version replaced NP_776167.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.133989.1,
                                           SRR5189667.349075.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..204
                     /product="PDZ domain-containing protein 9 isoform 1"
                     /note="PDZ domain-containing protein C16orf65; PDZ
                     domain-containing protein 9"
                     /calculated_mol_wt=23361
     Region          <11..49
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     CDS             1..204
                     /gene="PDZD9"
                     /gene_synonym="C16orf65"
                     /coded_by="NM_173806.4:70..684"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10602.2"
                     /db_xref="GeneID:255762"
                     /db_xref="HGNC:HGNC:28740"
ORIGIN      
        1 mqkashknkk gdvlisvgha nvlgytlref lqllqhitig tvlqikvyrd finipeewqe
       61 iydlipeakf pvtstpkkie lakdesftss ddnenvdldk rlqyyrypws tvhhparrpi
      121 sisrdwhgyk kknhtisvgk dincdvmihr ddkkevraps pywimvkqdn essssstsst
      181 sdafwledca qveegkaqlv skvg
//
LOCUS       NP_004522                188 aa            linear   PRI 09-DEC-2025
DEFINITION  molybdopterin synthase catalytic subunit large subunit MOCS2B [Homo
            sapiens].
ACCESSION   NP_004522 NP_904327
VERSION     NP_004522.1
DBSOURCE    REFSEQ: accession NM_004531.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Suganuma,T.
  TITLE     Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and MOCS2
  JOURNAL   Molecules 27 (12), 3733 (2022)
   PUBMED   35744859
  REMARK    GeneRIF: Beyond Moco Biosynthesis-Moonlighting Roles of MoaE and
            MOCS2.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Suganuma,T., Swanson,S.K., Florens,L., Washburn,M.P. and
            Workman,J.L.
  TITLE     Moco biosynthesis and the ATAC acetyltransferase engage translation
            initiation by inhibiting latent PKR activity
  JOURNAL   J Mol Cell Biol 8 (1), 44-50 (2016)
   PUBMED   26705305
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Edwards,M., Roeper,J., Allgood,C., Chin,R., Santamaria,J., Wong,F.,
            Schwarz,G. and Whitehall,J.
  TITLE     Investigation of molybdenum cofactor deficiency due to MOCS2
            deficiency in a newborn baby
  JOURNAL   Meta Gene 3, 43-49 (2015)
   PUBMED   25709896
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Hahnewald,R., Leimkuhler,S., Vilaseca,A., Acquaviva-Bourdain,C.,
            Lenz,U. and Reiss,J.
  TITLE     A novel MOCS2 mutation reveals coordinated expression of the small
            and large subunit of molybdopterin synthase
  JOURNAL   Mol Genet Metab 89 (3), 210-213 (2006)
   PUBMED   16737835
  REMARK    GeneRIF: There was undisturbed production of both transcripts,
            while Western blot analysis demonstrated that MOCS2B, the large
            subunit, is unstable in the absence of MOCS2A.
REFERENCE   5  (residues 1 to 188)
  AUTHORS   Stallmeyer,B., Drugeon,G., Reiss,J., Haenni,A.L. and Mendel,R.R.
  TITLE     Human molybdopterin synthase gene: identification of a bicistronic
            transcript with overlapping reading frames
  JOURNAL   Am J Hum Genet 64 (3), 698-705 (1999)
   PUBMED   10053003
REFERENCE   6  (residues 1 to 188)
  AUTHORS   Sloan,J., Kinghorn,J.R. and Unkles,S.E.
  TITLE     The two subunits of human molybdopterin synthase: evidence for a
            bicistronic messenger RNA with overlapping reading frames
  JOURNAL   Nucleic Acids Res 27 (3), 854-858 (1999)
   PUBMED   9889283
REFERENCE   7  (residues 1 to 188)
  AUTHORS   Feng,G., Tintrup,H., Kirsch,J., Nichol,M.C., Kuhse,J., Betz,H. and
            Sanes,J.R.
  TITLE     Dual requirement for gephyrin in glycine receptor clustering and
            molybdoenzyme activity
  JOURNAL   Science 282 (5392), 1321-1324 (1998)
   PUBMED   9812897
REFERENCE   8  (residues 1 to 188)
  AUTHORS   Reiss,J., Cohen,N., Dorche,C., Mandel,H., Mendel,R.R.,
            Stallmeyer,B., Zabot,M.T. and Dierks,T.
  TITLE     Mutations in a polycistronic nuclear gene associated with
            molybdenum cofactor deficiency
  JOURNAL   Nat Genet 20 (1), 51-53 (1998)
   PUBMED   9731530
REFERENCE   9  (residues 1 to 188)
  AUTHORS   Misko,A., Mahtani,K., Abbott,J., Schwarz,G. and Atwal,P.
  TITLE     Molybdenum Cofactor Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   34870926
REFERENCE   10 (residues 1 to 188)
  AUTHORS   Krawczak,M., Reiss,J. and Cooper,D.N.
  TITLE     The mutational spectrum of single base-pair substitutions in mRNA
            splice junctions of human genes: causes and consequences
  JOURNAL   Hum Genet 90 (1-2), 41-54 (1992)
   PUBMED   1427786
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC095417.1, DA967651.1,
            BC046097.1, AC008966.9 and CB050849.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 22, 2006 this sequence version replaced NP_904327.1.
            
            Summary: Eukaryotic molybdoenzymes use a unique molybdenum cofactor
            (MoCo) consisting of a pterin, termed molybdopterin, and the
            catalytically active metal molybdenum. MoCo is synthesized from
            precursor Z by the heterodimeric enzyme molybdopterin synthase. The
            large and small subunits of molybdopterin synthase are both encoded
            from this gene by overlapping open reading frames. The proteins
            were initially thought to be encoded from a bicistronic transcript.
            They are now thought to be encoded from monocistronic transcripts.
            Alternatively spliced transcripts have been found for this locus
            that encode the large and small subunits. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (3) encodes the large subunit
            MOCS2B, also called MOCO1-B.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.92737.1,
                                           SRR1660805.212585.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155550 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396954.8/ ENSP00000380157.3
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q11.2"
     Protein         1..188
                     /product="molybdopterin synthase catalytic subunit large
                     subunit MOCS2B"
                     /EC_number="2.8.1.12"
                     /note="molybdenum cofactor biosynthesis protein E"
                     /calculated_mol_wt=20813
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O96007.1)"
     Region          54..177
                     /region_name="MoaE"
                     /note="MoaE family. Members of this family are involved in
                     biosynthesis of the molybdenum cofactor (Moco), an
                     essential cofactor for a diverse group of redox enzymes.
                     Moco biosynthesis is an evolutionarily conserved pathway
                     present in eubacteria, archaea and...; cd00756"
                     /db_xref="CDD:238385"
     Site            order(60,64,69,71..75,77,79,133,142,144,152,156)
                     /site_type="other"
                     /note="MoaE homodimer interface [polypeptide binding]"
                     /db_xref="CDD:238385"
     Site            order(93,95,98,101,105,123,159..160,162,164..166,176)
                     /site_type="other"
                     /note="MoaD interaction [polypeptide binding]"
                     /db_xref="CDD:238385"
     Site            order(159,166)
                     /site_type="active"
                     /note="active site residues [active]"
                     /db_xref="CDD:238385"
     CDS             1..188
                     /gene="MOCS2"
                     /gene_synonym="MCBPE; MOCO1; MOCODB; MOCODB1; MPTS"
                     /coded_by="NM_004531.5:677..1243"
                     /note="large subunit MOCS2B is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS3958.1"
                     /db_xref="GeneID:4338"
                     /db_xref="HGNC:HGNC:7193"
                     /db_xref="MIM:603708"
ORIGIN      
        1 mssleisssc fsletklpls pplvedsafe psrkdmdeve ekskdvinft aeklsvdevs
       61 qlvisplcga islfvgttrn nfegkkvisl eyeaylpmae nevrkicsdi rqkwpvkhia
      121 vfhrlglvpv seasiiiavs sahraaslea vsyaidtlka kvpiwkkeiy eesstwkgnk
      181 ecfwasns
//
LOCUS       NP_001073892            1043 aa            linear   PRI 10-DEC-2025
DEFINITION  glutamate receptor-interacting protein 2 [Homo sapiens].
ACCESSION   NP_001073892 XP_005265558 XP_042936
VERSION     NP_001073892.3
DBSOURCE    REFSEQ: accession NM_001080423.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Garrido-Urbani,S., Garg,P., Ghossoub,R., Arnold,R., Lembo,F.,
            Sundell,G.N., Kim,P.M., Lopez,M., Zimmermann,P., Sidhu,S.S. and
            Ivarsson,Y.
  TITLE     Proteomic peptide phage display uncovers novel interactions of the
            PDZ1-2 supramodule of syntenin
  JOURNAL   FEBS Lett 590 (1), 3-12 (2016)
   PUBMED   26787460
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Lu,W. and Ziff,E.B.
  TITLE     PICK1 interacts with ABP/GRIP to regulate AMPA receptor trafficking
  JOURNAL   Neuron 47 (3), 407-421 (2005)
   PUBMED   16055064
REFERENCE   4  (residues 1 to 1043)
  AUTHORS   Lin,S.H., Arai,A.C., Wang,Z., Nothacker,H.P. and Civelli,O.
  TITLE     The carboxyl terminus of the prolactin-releasing peptide receptor
            interacts with PDZ domain proteins involved in
            alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor
            clustering
  JOURNAL   Mol Pharmacol 60 (5), 916-923 (2001)
   PUBMED   11641419
REFERENCE   5  (residues 1 to 1043)
  AUTHORS   Hattori,A., Okumura,K., Nagase,T., Kikuno,R., Hirosawa,M. and
            Ohara,O.
  TITLE     Characterization of long cDNA clones from human adult spleen
  JOURNAL   DNA Res 7 (6), 357-366 (2000)
   PUBMED   11214971
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK095762.1, AB051506.2, AC090952.3 and AK024507.1.
            
            On Apr 24, 2014 this sequence version replaced NP_001073892.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB051506.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000621039.5/ ENSP00000478352.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.1"
     Protein         1..1043
                     /product="glutamate receptor-interacting protein 2"
                     /calculated_mol_wt=112443
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0E4.4)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WTW1; propagated from
                     UniProtKB/Swiss-Prot (Q9C0E4.4)"
     Region          47..129
                     /region_name="PDZ1_GRIP1-2-like"
                     /note="PDZ domain 1 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06687"
                     /db_xref="CDD:467175"
     Site            order(58..64,76,79,109,113,116..117)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467175"
     Region          145..233
                     /region_name="PDZ2_GRIP1-2-like"
                     /note="PDZ domain 2 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06681"
                     /db_xref="CDD:467169"
     Site            order(157..163,179,182,212,216,219..220)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467169"
     Region          245..330
                     /region_name="PDZ3_GRIP1-2-like"
                     /note="PDZ domain 3 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06684"
                     /db_xref="CDD:467172"
     Site            order(258..264,277,280,310,314,317..318)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467172"
     Region          373..448
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0E4.4)"
     Region          448..548
                     /region_name="PDZ4_GRIP1-2-like"
                     /note="PDZ domain 4 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06686"
                     /db_xref="CDD:467174"
     Site            order(453..456,497..498,500..502,541,543..548)
                     /site_type="other"
                     /note="PDZ5 interface [polypeptide binding]"
                     /db_xref="CDD:467174"
     Site            order(466..472,488,491,521,525,528..529)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467174"
     Region          556..639
                     /region_name="PDZ5_GRIP1-2-like"
                     /note="PDZ domain 5 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06682"
                     /db_xref="CDD:467170"
     Site            order(567..573,586,589,619,623,626..627)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467170"
     Region          652..736
                     /region_name="PDZ6_GRIP1-2-like"
                     /note="PDZ domain 6 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06683"
                     /db_xref="CDD:467171"
     Site            order(665..671,683,686,716,720,723..724)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467171"
     Region          743..866
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0E4.4)"
     Region          937..1021
                     /region_name="PDZ7_GRIP1-2-like"
                     /note="PDZ domain 7 of glutamate receptor-interacting
                     protein 1 (GRIP1) and GRIP2, and related domains; cd06685"
                     /db_xref="CDD:467173"
     Site            order(952..958,969,972,1001,1005,1008..1009)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467173"
     Site            order(991,994,999,1002..1003,1006..1007)
                     /site_type="other"
                     /note="GRASP-1 binding site [polypeptide binding]"
                     /db_xref="CDD:467173"
     Region          1023..1043
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0E4.4)"
     CDS             1..1043
                     /gene="GRIP2"
                     /gene_synonym="ABP"
                     /coded_by="NM_001080423.4:35..3166"
                     /db_xref="CCDS:CCDS46766.2"
                     /db_xref="GeneID:80852"
                     /db_xref="HGNC:HGNC:23841"
                     /db_xref="MIM:621438"
ORIGIN      
        1 mlcglsretp geaddgpysk ggkdaggadv slacrrqsip eefrgitvve likkegstlg
       61 ltisggtdkd gkprvsnlrp gglaarsdll nigdyirsvn gihltrlrhd eiitllknvg
      121 ervvleveye lpppapennp riisktvdvs lykegnsfgf vlrggahedg hksrplvlty
      181 vrpggpadre gslkvgdrll svdgiplhga shatalatlr qcshealfqv eydvatpdtv
      241 anasgplmve ivktpgsalg isltttslrn ksvitidrik pasvvdrsga lhpgdhilsi
      301 dgtsmehcsl leatkllasi sekvrleilp vpqsqrplrp seavkvqrse qlhrwdpcvp
      361 schsprpghc rmptwatpag qdqsrslsst pfssptlnha fscnnpstlp rgsqpmsprt
      421 tmgrrrqrrr ehksslslas stvgpggqiv htettevvlc gdplsgfglq lqggifatet
      481 lsspplvcfi epdspaercg llqvgdrvls ingiatedgt meeanqllrd aalahkvvle
      541 vefdvaesvi pssgtfhvkl pkkrsvelgi tissasrkrg epliisdikk gsvahrtgtl
      601 epgdkllaid nirldncpme davqilrqce dlvklkirkd ednsdelett gavsytvelk
      661 ryggplgiti sgteepfdpi visgltkrgl aertgaihvg drilainnvs lkgrplseai
      721 hllqvagetv tlkikkqldr pllprksgsl setsdadedp adalkgglpa arfspavpsv
      781 dsaveswdss ateggfggpg sytpqaaarg ttpqerrpgw lrgsppptep rrtsytptpa
      841 desfpeeeee ddwepptspa pgpareegfw rmfgealedl escgqsellr eleasimtgt
      901 vqrvalegrp ghrpwqrgre vraspaemee lllptplemh kvtlhkdpmr hdfgfsvsdg
      961 llekgvyvht vrpdgpahrg glqpfdrvlq vnhvrtrdfd cclavpllae agdvleliis
     1021 rkphtahssr aprspgpssp rml
//
LOCUS       NP_001374678             390 aa            linear   PRI 11-DEC-2025
DEFINITION  dematin isoform 5 [Homo sapiens].
ACCESSION   NP_001374678
VERSION     NP_001374678.1
DBSOURCE    REFSEQ: accession NM_001387749.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Wang,M., Chen,B., Zhang,W., Zhang,F., Qiu,Y., Lin,Y. and Yang,S.
  TITLE     Dematin inhibits glioblastoma malignancy through RhoA-mediated CDKs
            downregulation and cytoskeleton remodeling
  JOURNAL   Exp Cell Res 417 (1), 113196 (2022)
   PUBMED   35561787
  REMARK    GeneRIF: Dematin inhibits glioblastoma malignancy through
            RhoA-mediated CDKs downregulation and cytoskeleton remodeling.
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Brandt,G.S. and Bailey,S.
  TITLE     Dematin, a human erythrocyte cytoskeletal protein, is a substrate
            for a recombinant FIKK kinase from Plasmodium falciparum
  JOURNAL   Mol Biochem Parasitol 191 (1), 20-23 (2013)
   PUBMED   23973789
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Chen,L., Brown,J.W., Mok,Y.F., Hatters,D.M. and McKnight,C.J.
  TITLE     The allosteric mechanism induced by protein kinase A (PKA)
            phosphorylation of dematin (band 4.9)
  JOURNAL   J Biol Chem 288 (12), 8313-8320 (2013)
   PUBMED   23355471
  REMARK    GeneRIF: When unphosphorylated, dematin's two F-actin binding
            domains move independent of one another permitting them to bind
            different F-actin filaments.
            Erratum:[J Biol Chem. 2015 Jul 17;290(29):17808. doi:
            10.1074/jbc.A112.438861. PMID: 26188045]
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Mohseni,M. and Chishti,A.H.
  TITLE     Erythrocyte dematin is a candidate gene for Marie Unna hereditary
            hypotrichosis and related hairloss disorders
  JOURNAL   Am J Hematol 83 (5), 430-432 (2008)
   PUBMED   18273904
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Lutchman,M., Kim,A.C., Cheng,L., Whitehead,I.P., Oh,S.S.,
            Hanspal,M., Boukharov,A.A., Hanada,T. and Chishti,A.H.
  TITLE     Dematin interacts with the Ras-guanine nucleotide exchange factor
            Ras-GRF2 and modulates mitogen-activated protein kinase pathways
  JOURNAL   Eur J Biochem 269 (2), 638-649 (2002)
   PUBMED   11856323
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Lutchman,M., Pack,S., Kim,A.C., Azim,A., Emmert-Buck,M., van
            Huffel,C., Zhuang,Z. and Chishti,A.H.
  TITLE     Loss of heterozygosity on 8p in prostate cancer implicates a role
            for dematin in tumor progression
  JOURNAL   Cancer Genet Cytogenet 115 (1), 65-69 (1999)
   PUBMED   10565303
REFERENCE   8  (residues 1 to 390)
  AUTHORS   Azim,A.C., Marfatia,S.M., Korsgren,C., Dotimas,E., Cohen,C.M. and
            Chishti,A.H.
  TITLE     Human erythrocyte dematin and protein 4.2 (pallidin) are ATP
            binding proteins
  JOURNAL   Biochemistry 35 (9), 3001-3006 (1996)
   PUBMED   8608138
REFERENCE   9  (residues 1 to 390)
  AUTHORS   Azim,A.C., Knoll,J.H., Beggs,A.H. and Chishti,A.H.
  TITLE     Isoform cloning, actin binding, and chromosomal localization of
            human erythroid dematin, a member of the villin superfamily
  JOURNAL   J Biol Chem 270 (29), 17407-17413 (1995)
   PUBMED   7615546
REFERENCE   10 (residues 1 to 390)
  AUTHORS   Rana,A.P., Ruff,P., Maalouf,G.J., Speicher,D.W. and Chishti,A.H.
  TITLE     Cloning of human erythroid dematin reveals another member of the
            villin family
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6651-6655 (1993)
   PUBMED   8341682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091171.15.
            
            Summary: The protein encoded by this gene is an actin binding and
            bundling protein that plays a structural role in erythrocytes, by
            stabilizing and attaching the spectrin/actin cytoskeleton to the
            erythrocyte membrane in a phosphorylation-dependent manner. This
            protein contains a core domain in the N-terminus, and a headpiece
            domain in the C-terminus that binds F-actin. When purified from
            erythrocytes, this protein exists as a trimer composed of two 48
            kDa polypeptides and a 52 kDa polypeptide. The different subunits
            arise from alternative splicing in the 3' coding region, where the
            headpiece domain is located. Disruption of this gene has been
            correlated with the autosomal dominant Marie Unna hereditary
            hypotrichosis disease, while loss of heterozygosity of this gene is
            thought to play a role in prostate cancer progression. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..390
                     /product="dematin isoform 5"
                     /note="erythrocyte membrane protein band 4.9 (dematin)"
                     /calculated_mol_wt=43835
     Region          8..340
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          355..390
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..390
                     /gene="DMTN"
                     /gene_synonym="DMT; EPB49"
                     /coded_by="NM_001387749.1:495..1667"
                     /note="isoform 5 is encoded by transcript variant 59"
                     /db_xref="GeneID:2039"
                     /db_xref="HGNC:HGNC:3382"
                     /db_xref="MIM:125305"
ORIGIN      
        1 merlqkqplt spgsvspsrd ssvpgspssi vakmdnqvlg ykdlaaipkd kaildierpd
       61 lmiyephfty sllehvelpr srevwadsrs pgiisqasap rttgtprtsl phfhhpetsr
      121 pdsniykkpp iykqresvgg spqtkhlied liiesskfpa aqppdpnqpa kietdywpcp
      181 pslavvetew rkrkasrrga eeeeeeeddd sgeemkalre rqreelskvt snlgkmilke
      241 emekslpirr ktrslpdrtp fhtslhqgts kssslpaygr ttlsrlqste fspsgsetgs
      301 pglqngegqr grmdrgnslp cvleqkiypy emlvvtnkgr tklppgvdrm rlerhlsaed
      361 fsrvfamspe efgklalwkr nelkkkaslf
//
LOCUS       NP_001374651             365 aa            linear   PRI 11-DEC-2025
DEFINITION  dematin isoform 4 [Homo sapiens].
ACCESSION   NP_001374651
VERSION     NP_001374651.1
DBSOURCE    REFSEQ: accession NM_001387722.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Wang,M., Chen,B., Zhang,W., Zhang,F., Qiu,Y., Lin,Y. and Yang,S.
  TITLE     Dematin inhibits glioblastoma malignancy through RhoA-mediated CDKs
            downregulation and cytoskeleton remodeling
  JOURNAL   Exp Cell Res 417 (1), 113196 (2022)
   PUBMED   35561787
  REMARK    GeneRIF: Dematin inhibits glioblastoma malignancy through
            RhoA-mediated CDKs downregulation and cytoskeleton remodeling.
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Brandt,G.S. and Bailey,S.
  TITLE     Dematin, a human erythrocyte cytoskeletal protein, is a substrate
            for a recombinant FIKK kinase from Plasmodium falciparum
  JOURNAL   Mol Biochem Parasitol 191 (1), 20-23 (2013)
   PUBMED   23973789
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Chen,L., Brown,J.W., Mok,Y.F., Hatters,D.M. and McKnight,C.J.
  TITLE     The allosteric mechanism induced by protein kinase A (PKA)
            phosphorylation of dematin (band 4.9)
  JOURNAL   J Biol Chem 288 (12), 8313-8320 (2013)
   PUBMED   23355471
  REMARK    GeneRIF: When unphosphorylated, dematin's two F-actin binding
            domains move independent of one another permitting them to bind
            different F-actin filaments.
            Erratum:[J Biol Chem. 2015 Jul 17;290(29):17808. doi:
            10.1074/jbc.A112.438861. PMID: 26188045]
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Mohseni,M. and Chishti,A.H.
  TITLE     Erythrocyte dematin is a candidate gene for Marie Unna hereditary
            hypotrichosis and related hairloss disorders
  JOURNAL   Am J Hematol 83 (5), 430-432 (2008)
   PUBMED   18273904
REFERENCE   6  (residues 1 to 365)
  AUTHORS   Lutchman,M., Kim,A.C., Cheng,L., Whitehead,I.P., Oh,S.S.,
            Hanspal,M., Boukharov,A.A., Hanada,T. and Chishti,A.H.
  TITLE     Dematin interacts with the Ras-guanine nucleotide exchange factor
            Ras-GRF2 and modulates mitogen-activated protein kinase pathways
  JOURNAL   Eur J Biochem 269 (2), 638-649 (2002)
   PUBMED   11856323
REFERENCE   7  (residues 1 to 365)
  AUTHORS   Lutchman,M., Pack,S., Kim,A.C., Azim,A., Emmert-Buck,M., van
            Huffel,C., Zhuang,Z. and Chishti,A.H.
  TITLE     Loss of heterozygosity on 8p in prostate cancer implicates a role
            for dematin in tumor progression
  JOURNAL   Cancer Genet Cytogenet 115 (1), 65-69 (1999)
   PUBMED   10565303
REFERENCE   8  (residues 1 to 365)
  AUTHORS   Azim,A.C., Marfatia,S.M., Korsgren,C., Dotimas,E., Cohen,C.M. and
            Chishti,A.H.
  TITLE     Human erythrocyte dematin and protein 4.2 (pallidin) are ATP
            binding proteins
  JOURNAL   Biochemistry 35 (9), 3001-3006 (1996)
   PUBMED   8608138
REFERENCE   9  (residues 1 to 365)
  AUTHORS   Azim,A.C., Knoll,J.H., Beggs,A.H. and Chishti,A.H.
  TITLE     Isoform cloning, actin binding, and chromosomal localization of
            human erythroid dematin, a member of the villin superfamily
  JOURNAL   J Biol Chem 270 (29), 17407-17413 (1995)
   PUBMED   7615546
REFERENCE   10 (residues 1 to 365)
  AUTHORS   Rana,A.P., Ruff,P., Maalouf,G.J., Speicher,D.W. and Chishti,A.H.
  TITLE     Cloning of human erythroid dematin reveals another member of the
            villin family
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6651-6655 (1993)
   PUBMED   8341682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091171.15.
            
            Summary: The protein encoded by this gene is an actin binding and
            bundling protein that plays a structural role in erythrocytes, by
            stabilizing and attaching the spectrin/actin cytoskeleton to the
            erythrocyte membrane in a phosphorylation-dependent manner. This
            protein contains a core domain in the N-terminus, and a headpiece
            domain in the C-terminus that binds F-actin. When purified from
            erythrocytes, this protein exists as a trimer composed of two 48
            kDa polypeptides and a 52 kDa polypeptide. The different subunits
            arise from alternative splicing in the 3' coding region, where the
            headpiece domain is located. Disruption of this gene has been
            correlated with the autosomal dominant Marie Unna hereditary
            hypotrichosis disease, while loss of heterozygosity of this gene is
            thought to play a role in prostate cancer progression. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..365
                     /product="dematin isoform 4"
                     /note="erythrocyte membrane protein band 4.9 (dematin)"
                     /calculated_mol_wt=41427
     Region          7..315
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          330..365
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..365
                     /gene="DMTN"
                     /gene_synonym="DMT; EPB49"
                     /coded_by="NM_001387722.1:333..1430"
                     /note="isoform 4 is encoded by transcript variant 32"
                     /db_xref="GeneID:2039"
                     /db_xref="HGNC:HGNC:3382"
                     /db_xref="MIM:125305"
ORIGIN      
        1 merlqkakmd nqvlgykdla aipkdkaild ierpdlmiye phftyslleh velprsrevw
       61 adsrspgiis qasaprttgt prtslphfhh petsrpdsni ykkppiykqr esvggspqtk
      121 hliedliies skfpaaqppd pnqpakietd ywpcppslav vetewrkrka srrgaeeeee
      181 eedddsgeem kalrerqree lskvtsnlgk milkeemeks lpirrktrsl pdrtpfhtsl
      241 hqgtsksssl paygrttlsr lqstefspsg setgspglqn gegqrgrmdr gnslpcvleq
      301 kiypyemlvv tnkgrtklpp gvdrmrlerh lsaedfsrvf amspeefgkl alwkrnelkk
      361 kaslf
//
LOCUS       NP_001374669             358 aa            linear   PRI 11-DEC-2025
DEFINITION  dematin isoform 3 [Homo sapiens].
ACCESSION   NP_001374669 XP_016868687
VERSION     NP_001374669.1
DBSOURCE    REFSEQ: accession NM_001387740.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wang,M., Chen,B., Zhang,W., Zhang,F., Qiu,Y., Lin,Y. and Yang,S.
  TITLE     Dematin inhibits glioblastoma malignancy through RhoA-mediated CDKs
            downregulation and cytoskeleton remodeling
  JOURNAL   Exp Cell Res 417 (1), 113196 (2022)
   PUBMED   35561787
  REMARK    GeneRIF: Dematin inhibits glioblastoma malignancy through
            RhoA-mediated CDKs downregulation and cytoskeleton remodeling.
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Brandt,G.S. and Bailey,S.
  TITLE     Dematin, a human erythrocyte cytoskeletal protein, is a substrate
            for a recombinant FIKK kinase from Plasmodium falciparum
  JOURNAL   Mol Biochem Parasitol 191 (1), 20-23 (2013)
   PUBMED   23973789
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Chen,L., Brown,J.W., Mok,Y.F., Hatters,D.M. and McKnight,C.J.
  TITLE     The allosteric mechanism induced by protein kinase A (PKA)
            phosphorylation of dematin (band 4.9)
  JOURNAL   J Biol Chem 288 (12), 8313-8320 (2013)
   PUBMED   23355471
  REMARK    GeneRIF: When unphosphorylated, dematin's two F-actin binding
            domains move independent of one another permitting them to bind
            different F-actin filaments.
            Erratum:[J Biol Chem. 2015 Jul 17;290(29):17808. doi:
            10.1074/jbc.A112.438861. PMID: 26188045]
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Mohseni,M. and Chishti,A.H.
  TITLE     Erythrocyte dematin is a candidate gene for Marie Unna hereditary
            hypotrichosis and related hairloss disorders
  JOURNAL   Am J Hematol 83 (5), 430-432 (2008)
   PUBMED   18273904
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Lutchman,M., Kim,A.C., Cheng,L., Whitehead,I.P., Oh,S.S.,
            Hanspal,M., Boukharov,A.A., Hanada,T. and Chishti,A.H.
  TITLE     Dematin interacts with the Ras-guanine nucleotide exchange factor
            Ras-GRF2 and modulates mitogen-activated protein kinase pathways
  JOURNAL   Eur J Biochem 269 (2), 638-649 (2002)
   PUBMED   11856323
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Lutchman,M., Pack,S., Kim,A.C., Azim,A., Emmert-Buck,M., van
            Huffel,C., Zhuang,Z. and Chishti,A.H.
  TITLE     Loss of heterozygosity on 8p in prostate cancer implicates a role
            for dematin in tumor progression
  JOURNAL   Cancer Genet Cytogenet 115 (1), 65-69 (1999)
   PUBMED   10565303
REFERENCE   8  (residues 1 to 358)
  AUTHORS   Azim,A.C., Marfatia,S.M., Korsgren,C., Dotimas,E., Cohen,C.M. and
            Chishti,A.H.
  TITLE     Human erythrocyte dematin and protein 4.2 (pallidin) are ATP
            binding proteins
  JOURNAL   Biochemistry 35 (9), 3001-3006 (1996)
   PUBMED   8608138
REFERENCE   9  (residues 1 to 358)
  AUTHORS   Azim,A.C., Knoll,J.H., Beggs,A.H. and Chishti,A.H.
  TITLE     Isoform cloning, actin binding, and chromosomal localization of
            human erythroid dematin, a member of the villin superfamily
  JOURNAL   J Biol Chem 270 (29), 17407-17413 (1995)
   PUBMED   7615546
REFERENCE   10 (residues 1 to 358)
  AUTHORS   Rana,A.P., Ruff,P., Maalouf,G.J., Speicher,D.W. and Chishti,A.H.
  TITLE     Cloning of human erythroid dematin reveals another member of the
            villin family
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6651-6655 (1993)
   PUBMED   8341682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091171.15.
            
            On Dec 11, 2025 this sequence version replaced XP_016868687.1.
            
            Summary: The protein encoded by this gene is an actin binding and
            bundling protein that plays a structural role in erythrocytes, by
            stabilizing and attaching the spectrin/actin cytoskeleton to the
            erythrocyte membrane in a phosphorylation-dependent manner. This
            protein contains a core domain in the N-terminus, and a headpiece
            domain in the C-terminus that binds F-actin. When purified from
            erythrocytes, this protein exists as a trimer composed of two 48
            kDa polypeptides and a 52 kDa polypeptide. The different subunits
            arise from alternative splicing in the 3' coding region, where the
            headpiece domain is located. Disruption of this gene has been
            correlated with the autosomal dominant Marie Unna hereditary
            hypotrichosis disease, while loss of heterozygosity of this gene is
            thought to play a role in prostate cancer progression. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1970526,
                              SAMEA2145544 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..358
                     /product="dematin isoform 3"
                     /note="erythrocyte membrane protein band 4.9 (dematin)"
                     /calculated_mol_wt=40549
     Region          7..308
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          323..358
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..358
                     /gene="DMTN"
                     /gene_synonym="DMT; EPB49"
                     /coded_by="NM_001387740.1:362..1438"
                     /note="isoform 3 is encoded by transcript variant 50"
                     /db_xref="GeneID:2039"
                     /db_xref="HGNC:HGNC:3382"
                     /db_xref="MIM:125305"
ORIGIN      
        1 merlqkakmd nqvlgykdla aipkdkaild ierpdlmiye phftyslleh velprsrers
       61 lspkstsppp spevwadsrs pgiisqasap rttgtprtsl phfhhpetsr pdsniykkpp
      121 iykqresvgg spqtkhlied liiesskfpa aqppdpnqpa kietdywpcp pslavvetew
      181 rkrkasrrga eeeeeeeddd sgeemkalre rqreelskvt snlgkmilke emekslpirr
      241 ktrslpdrtp fhtslhqgts kssslpaygr ttlsrlqste fspsgsetgs pglqiypyem
      301 lvvtnkgrtk lppgvdrmrl erhlsaedfs rvfamspeef gklalwkrne lkkkaslf
//
LOCUS       NP_001374670             365 aa            linear   PRI 11-DEC-2025
DEFINITION  dematin isoform 4 [Homo sapiens].
ACCESSION   NP_001374670 XP_016868683 XP_054216000
VERSION     NP_001374670.1
DBSOURCE    REFSEQ: accession NM_001387741.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Wang,M., Chen,B., Zhang,W., Zhang,F., Qiu,Y., Lin,Y. and Yang,S.
  TITLE     Dematin inhibits glioblastoma malignancy through RhoA-mediated CDKs
            downregulation and cytoskeleton remodeling
  JOURNAL   Exp Cell Res 417 (1), 113196 (2022)
   PUBMED   35561787
  REMARK    GeneRIF: Dematin inhibits glioblastoma malignancy through
            RhoA-mediated CDKs downregulation and cytoskeleton remodeling.
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Brandt,G.S. and Bailey,S.
  TITLE     Dematin, a human erythrocyte cytoskeletal protein, is a substrate
            for a recombinant FIKK kinase from Plasmodium falciparum
  JOURNAL   Mol Biochem Parasitol 191 (1), 20-23 (2013)
   PUBMED   23973789
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Chen,L., Brown,J.W., Mok,Y.F., Hatters,D.M. and McKnight,C.J.
  TITLE     The allosteric mechanism induced by protein kinase A (PKA)
            phosphorylation of dematin (band 4.9)
  JOURNAL   J Biol Chem 288 (12), 8313-8320 (2013)
   PUBMED   23355471
  REMARK    GeneRIF: When unphosphorylated, dematin's two F-actin binding
            domains move independent of one another permitting them to bind
            different F-actin filaments.
            Erratum:[J Biol Chem. 2015 Jul 17;290(29):17808. doi:
            10.1074/jbc.A112.438861. PMID: 26188045]
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Mohseni,M. and Chishti,A.H.
  TITLE     Erythrocyte dematin is a candidate gene for Marie Unna hereditary
            hypotrichosis and related hairloss disorders
  JOURNAL   Am J Hematol 83 (5), 430-432 (2008)
   PUBMED   18273904
REFERENCE   6  (residues 1 to 365)
  AUTHORS   Lutchman,M., Kim,A.C., Cheng,L., Whitehead,I.P., Oh,S.S.,
            Hanspal,M., Boukharov,A.A., Hanada,T. and Chishti,A.H.
  TITLE     Dematin interacts with the Ras-guanine nucleotide exchange factor
            Ras-GRF2 and modulates mitogen-activated protein kinase pathways
  JOURNAL   Eur J Biochem 269 (2), 638-649 (2002)
   PUBMED   11856323
REFERENCE   7  (residues 1 to 365)
  AUTHORS   Lutchman,M., Pack,S., Kim,A.C., Azim,A., Emmert-Buck,M., van
            Huffel,C., Zhuang,Z. and Chishti,A.H.
  TITLE     Loss of heterozygosity on 8p in prostate cancer implicates a role
            for dematin in tumor progression
  JOURNAL   Cancer Genet Cytogenet 115 (1), 65-69 (1999)
   PUBMED   10565303
REFERENCE   8  (residues 1 to 365)
  AUTHORS   Azim,A.C., Marfatia,S.M., Korsgren,C., Dotimas,E., Cohen,C.M. and
            Chishti,A.H.
  TITLE     Human erythrocyte dematin and protein 4.2 (pallidin) are ATP
            binding proteins
  JOURNAL   Biochemistry 35 (9), 3001-3006 (1996)
   PUBMED   8608138
REFERENCE   9  (residues 1 to 365)
  AUTHORS   Azim,A.C., Knoll,J.H., Beggs,A.H. and Chishti,A.H.
  TITLE     Isoform cloning, actin binding, and chromosomal localization of
            human erythroid dematin, a member of the villin superfamily
  JOURNAL   J Biol Chem 270 (29), 17407-17413 (1995)
   PUBMED   7615546
REFERENCE   10 (residues 1 to 365)
  AUTHORS   Rana,A.P., Ruff,P., Maalouf,G.J., Speicher,D.W. and Chishti,A.H.
  TITLE     Cloning of human erythroid dematin reveals another member of the
            villin family
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6651-6655 (1993)
   PUBMED   8341682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091171.15.
            
            On or before Dec 11, 2025 this sequence version replaced
            XP_016868683.1, XP_054216000.1.
            
            Summary: The protein encoded by this gene is an actin binding and
            bundling protein that plays a structural role in erythrocytes, by
            stabilizing and attaching the spectrin/actin cytoskeleton to the
            erythrocyte membrane in a phosphorylation-dependent manner. This
            protein contains a core domain in the N-terminus, and a headpiece
            domain in the C-terminus that binds F-actin. When purified from
            erythrocytes, this protein exists as a trimer composed of two 48
            kDa polypeptides and a 52 kDa polypeptide. The different subunits
            arise from alternative splicing in the 3' coding region, where the
            headpiece domain is located. Disruption of this gene has been
            correlated with the autosomal dominant Marie Unna hereditary
            hypotrichosis disease, while loss of heterozygosity of this gene is
            thought to play a role in prostate cancer progression. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1970526,
                              SAMEA2145544 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..365
                     /product="dematin isoform 4"
                     /note="erythrocyte membrane protein band 4.9 (dematin)"
                     /calculated_mol_wt=41427
     Region          7..315
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          330..365
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..365
                     /gene="DMTN"
                     /gene_synonym="DMT; EPB49"
                     /coded_by="NM_001387741.1:362..1459"
                     /note="isoform 4 is encoded by transcript variant 51"
                     /db_xref="GeneID:2039"
                     /db_xref="HGNC:HGNC:3382"
                     /db_xref="MIM:125305"
ORIGIN      
        1 merlqkakmd nqvlgykdla aipkdkaild ierpdlmiye phftyslleh velprsrevw
       61 adsrspgiis qasaprttgt prtslphfhh petsrpdsni ykkppiykqr esvggspqtk
      121 hliedliies skfpaaqppd pnqpakietd ywpcppslav vetewrkrka srrgaeeeee
      181 eedddsgeem kalrerqree lskvtsnlgk milkeemeks lpirrktrsl pdrtpfhtsl
      241 hqgtsksssl paygrttlsr lqstefspsg setgspglqn gegqrgrmdr gnslpcvleq
      301 kiypyemlvv tnkgrtklpp gvdrmrlerh lsaedfsrvf amspeefgkl alwkrnelkk
      361 kaslf
//
LOCUS       NP_001374658             343 aa            linear   PRI 11-DEC-2025
DEFINITION  dematin isoform 9 [Homo sapiens].
ACCESSION   NP_001374658
VERSION     NP_001374658.1
DBSOURCE    REFSEQ: accession NM_001387729.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wang,M., Chen,B., Zhang,W., Zhang,F., Qiu,Y., Lin,Y. and Yang,S.
  TITLE     Dematin inhibits glioblastoma malignancy through RhoA-mediated CDKs
            downregulation and cytoskeleton remodeling
  JOURNAL   Exp Cell Res 417 (1), 113196 (2022)
   PUBMED   35561787
  REMARK    GeneRIF: Dematin inhibits glioblastoma malignancy through
            RhoA-mediated CDKs downregulation and cytoskeleton remodeling.
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Brandt,G.S. and Bailey,S.
  TITLE     Dematin, a human erythrocyte cytoskeletal protein, is a substrate
            for a recombinant FIKK kinase from Plasmodium falciparum
  JOURNAL   Mol Biochem Parasitol 191 (1), 20-23 (2013)
   PUBMED   23973789
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Chen,L., Brown,J.W., Mok,Y.F., Hatters,D.M. and McKnight,C.J.
  TITLE     The allosteric mechanism induced by protein kinase A (PKA)
            phosphorylation of dematin (band 4.9)
  JOURNAL   J Biol Chem 288 (12), 8313-8320 (2013)
   PUBMED   23355471
  REMARK    GeneRIF: When unphosphorylated, dematin's two F-actin binding
            domains move independent of one another permitting them to bind
            different F-actin filaments.
            Erratum:[J Biol Chem. 2015 Jul 17;290(29):17808. doi:
            10.1074/jbc.A112.438861. PMID: 26188045]
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Mohseni,M. and Chishti,A.H.
  TITLE     Erythrocyte dematin is a candidate gene for Marie Unna hereditary
            hypotrichosis and related hairloss disorders
  JOURNAL   Am J Hematol 83 (5), 430-432 (2008)
   PUBMED   18273904
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Lutchman,M., Kim,A.C., Cheng,L., Whitehead,I.P., Oh,S.S.,
            Hanspal,M., Boukharov,A.A., Hanada,T. and Chishti,A.H.
  TITLE     Dematin interacts with the Ras-guanine nucleotide exchange factor
            Ras-GRF2 and modulates mitogen-activated protein kinase pathways
  JOURNAL   Eur J Biochem 269 (2), 638-649 (2002)
   PUBMED   11856323
REFERENCE   7  (residues 1 to 343)
  AUTHORS   Lutchman,M., Pack,S., Kim,A.C., Azim,A., Emmert-Buck,M., van
            Huffel,C., Zhuang,Z. and Chishti,A.H.
  TITLE     Loss of heterozygosity on 8p in prostate cancer implicates a role
            for dematin in tumor progression
  JOURNAL   Cancer Genet Cytogenet 115 (1), 65-69 (1999)
   PUBMED   10565303
REFERENCE   8  (residues 1 to 343)
  AUTHORS   Azim,A.C., Marfatia,S.M., Korsgren,C., Dotimas,E., Cohen,C.M. and
            Chishti,A.H.
  TITLE     Human erythrocyte dematin and protein 4.2 (pallidin) are ATP
            binding proteins
  JOURNAL   Biochemistry 35 (9), 3001-3006 (1996)
   PUBMED   8608138
REFERENCE   9  (residues 1 to 343)
  AUTHORS   Azim,A.C., Knoll,J.H., Beggs,A.H. and Chishti,A.H.
  TITLE     Isoform cloning, actin binding, and chromosomal localization of
            human erythroid dematin, a member of the villin superfamily
  JOURNAL   J Biol Chem 270 (29), 17407-17413 (1995)
   PUBMED   7615546
REFERENCE   10 (residues 1 to 343)
  AUTHORS   Rana,A.P., Ruff,P., Maalouf,G.J., Speicher,D.W. and Chishti,A.H.
  TITLE     Cloning of human erythroid dematin reveals another member of the
            villin family
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6651-6655 (1993)
   PUBMED   8341682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091171.15.
            
            Summary: The protein encoded by this gene is an actin binding and
            bundling protein that plays a structural role in erythrocytes, by
            stabilizing and attaching the spectrin/actin cytoskeleton to the
            erythrocyte membrane in a phosphorylation-dependent manner. This
            protein contains a core domain in the N-terminus, and a headpiece
            domain in the C-terminus that binds F-actin. When purified from
            erythrocytes, this protein exists as a trimer composed of two 48
            kDa polypeptides and a 52 kDa polypeptide. The different subunits
            arise from alternative splicing in the 3' coding region, where the
            headpiece domain is located. Disruption of this gene has been
            correlated with the autosomal dominant Marie Unna hereditary
            hypotrichosis disease, while loss of heterozygosity of this gene is
            thought to play a role in prostate cancer progression. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1970526,
                              SAMEA2159080 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..343
                     /product="dematin isoform 9"
                     /note="erythrocyte membrane protein band 4.9 (dematin)"
                     /calculated_mol_wt=39000
     Region          7..293
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          308..343
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..343
                     /gene="DMTN"
                     /gene_synonym="DMT; EPB49"
                     /coded_by="NM_001387729.1:404..1435"
                     /note="isoform 9 is encoded by transcript variant 39"
                     /db_xref="GeneID:2039"
                     /db_xref="HGNC:HGNC:3382"
                     /db_xref="MIM:125305"
ORIGIN      
        1 merlqkakmd nqvlgykdla aipkdkaild ierpdlmiye phftyslleh velprsrevw
       61 adsrspgiis qasaprttgt prtslphfhh petsrpdsni ykkppiykqr esvggspqtk
      121 hliedliies skfpaaqppd pnqpakietd ywpcppslav vetewrkrka srrgaeeeee
      181 eedddsgeem kalrerqree lskvtsnlgk milkeemeks lpirrktrsl pdrtpfhtsl
      241 hqgtsksssl paygrttlsr lqstefspsg setgspglqi ypyemlvvtn kgrtklppgv
      301 drmrlerhls aedfsrvfam speefgklal wkrnelkkka slf
//
LOCUS       NP_001374653             390 aa            linear   PRI 11-DEC-2025
DEFINITION  dematin isoform 5 [Homo sapiens].
ACCESSION   NP_001374653
VERSION     NP_001374653.1
DBSOURCE    REFSEQ: accession NM_001387724.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Wang,M., Chen,B., Zhang,W., Zhang,F., Qiu,Y., Lin,Y. and Yang,S.
  TITLE     Dematin inhibits glioblastoma malignancy through RhoA-mediated CDKs
            downregulation and cytoskeleton remodeling
  JOURNAL   Exp Cell Res 417 (1), 113196 (2022)
   PUBMED   35561787
  REMARK    GeneRIF: Dematin inhibits glioblastoma malignancy through
            RhoA-mediated CDKs downregulation and cytoskeleton remodeling.
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Brandt,G.S. and Bailey,S.
  TITLE     Dematin, a human erythrocyte cytoskeletal protein, is a substrate
            for a recombinant FIKK kinase from Plasmodium falciparum
  JOURNAL   Mol Biochem Parasitol 191 (1), 20-23 (2013)
   PUBMED   23973789
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Chen,L., Brown,J.W., Mok,Y.F., Hatters,D.M. and McKnight,C.J.
  TITLE     The allosteric mechanism induced by protein kinase A (PKA)
            phosphorylation of dematin (band 4.9)
  JOURNAL   J Biol Chem 288 (12), 8313-8320 (2013)
   PUBMED   23355471
  REMARK    GeneRIF: When unphosphorylated, dematin's two F-actin binding
            domains move independent of one another permitting them to bind
            different F-actin filaments.
            Erratum:[J Biol Chem. 2015 Jul 17;290(29):17808. doi:
            10.1074/jbc.A112.438861. PMID: 26188045]
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Mohseni,M. and Chishti,A.H.
  TITLE     Erythrocyte dematin is a candidate gene for Marie Unna hereditary
            hypotrichosis and related hairloss disorders
  JOURNAL   Am J Hematol 83 (5), 430-432 (2008)
   PUBMED   18273904
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Lutchman,M., Kim,A.C., Cheng,L., Whitehead,I.P., Oh,S.S.,
            Hanspal,M., Boukharov,A.A., Hanada,T. and Chishti,A.H.
  TITLE     Dematin interacts with the Ras-guanine nucleotide exchange factor
            Ras-GRF2 and modulates mitogen-activated protein kinase pathways
  JOURNAL   Eur J Biochem 269 (2), 638-649 (2002)
   PUBMED   11856323
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Lutchman,M., Pack,S., Kim,A.C., Azim,A., Emmert-Buck,M., van
            Huffel,C., Zhuang,Z. and Chishti,A.H.
  TITLE     Loss of heterozygosity on 8p in prostate cancer implicates a role
            for dematin in tumor progression
  JOURNAL   Cancer Genet Cytogenet 115 (1), 65-69 (1999)
   PUBMED   10565303
REFERENCE   8  (residues 1 to 390)
  AUTHORS   Azim,A.C., Marfatia,S.M., Korsgren,C., Dotimas,E., Cohen,C.M. and
            Chishti,A.H.
  TITLE     Human erythrocyte dematin and protein 4.2 (pallidin) are ATP
            binding proteins
  JOURNAL   Biochemistry 35 (9), 3001-3006 (1996)
   PUBMED   8608138
REFERENCE   9  (residues 1 to 390)
  AUTHORS   Azim,A.C., Knoll,J.H., Beggs,A.H. and Chishti,A.H.
  TITLE     Isoform cloning, actin binding, and chromosomal localization of
            human erythroid dematin, a member of the villin superfamily
  JOURNAL   J Biol Chem 270 (29), 17407-17413 (1995)
   PUBMED   7615546
REFERENCE   10 (residues 1 to 390)
  AUTHORS   Rana,A.P., Ruff,P., Maalouf,G.J., Speicher,D.W. and Chishti,A.H.
  TITLE     Cloning of human erythroid dematin reveals another member of the
            villin family
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6651-6655 (1993)
   PUBMED   8341682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091171.15.
            
            Summary: The protein encoded by this gene is an actin binding and
            bundling protein that plays a structural role in erythrocytes, by
            stabilizing and attaching the spectrin/actin cytoskeleton to the
            erythrocyte membrane in a phosphorylation-dependent manner. This
            protein contains a core domain in the N-terminus, and a headpiece
            domain in the C-terminus that binds F-actin. When purified from
            erythrocytes, this protein exists as a trimer composed of two 48
            kDa polypeptides and a 52 kDa polypeptide. The different subunits
            arise from alternative splicing in the 3' coding region, where the
            headpiece domain is located. Disruption of this gene has been
            correlated with the autosomal dominant Marie Unna hereditary
            hypotrichosis disease, while loss of heterozygosity of this gene is
            thought to play a role in prostate cancer progression. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..390
                     /product="dematin isoform 5"
                     /note="erythrocyte membrane protein band 4.9 (dematin)"
                     /calculated_mol_wt=43835
     Region          8..340
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          355..390
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..390
                     /gene="DMTN"
                     /gene_synonym="DMT; EPB49"
                     /coded_by="NM_001387724.1:333..1505"
                     /note="isoform 5 is encoded by transcript variant 34"
                     /db_xref="GeneID:2039"
                     /db_xref="HGNC:HGNC:3382"
                     /db_xref="MIM:125305"
ORIGIN      
        1 merlqkqplt spgsvspsrd ssvpgspssi vakmdnqvlg ykdlaaipkd kaildierpd
       61 lmiyephfty sllehvelpr srevwadsrs pgiisqasap rttgtprtsl phfhhpetsr
      121 pdsniykkpp iykqresvgg spqtkhlied liiesskfpa aqppdpnqpa kietdywpcp
      181 pslavvetew rkrkasrrga eeeeeeeddd sgeemkalre rqreelskvt snlgkmilke
      241 emekslpirr ktrslpdrtp fhtslhqgts kssslpaygr ttlsrlqste fspsgsetgs
      301 pglqngegqr grmdrgnslp cvleqkiypy emlvvtnkgr tklppgvdrm rlerhlsaed
      361 fsrvfamspe efgklalwkr nelkkkaslf
//
LOCUS       NP_001374676             380 aa            linear   PRI 11-DEC-2025
DEFINITION  dematin isoform 6 [Homo sapiens].
ACCESSION   NP_001374676 XP_047277462 XP_054215996
VERSION     NP_001374676.1
DBSOURCE    REFSEQ: accession NM_001387747.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Wang,M., Chen,B., Zhang,W., Zhang,F., Qiu,Y., Lin,Y. and Yang,S.
  TITLE     Dematin inhibits glioblastoma malignancy through RhoA-mediated CDKs
            downregulation and cytoskeleton remodeling
  JOURNAL   Exp Cell Res 417 (1), 113196 (2022)
   PUBMED   35561787
  REMARK    GeneRIF: Dematin inhibits glioblastoma malignancy through
            RhoA-mediated CDKs downregulation and cytoskeleton remodeling.
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Brandt,G.S. and Bailey,S.
  TITLE     Dematin, a human erythrocyte cytoskeletal protein, is a substrate
            for a recombinant FIKK kinase from Plasmodium falciparum
  JOURNAL   Mol Biochem Parasitol 191 (1), 20-23 (2013)
   PUBMED   23973789
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Chen,L., Brown,J.W., Mok,Y.F., Hatters,D.M. and McKnight,C.J.
  TITLE     The allosteric mechanism induced by protein kinase A (PKA)
            phosphorylation of dematin (band 4.9)
  JOURNAL   J Biol Chem 288 (12), 8313-8320 (2013)
   PUBMED   23355471
  REMARK    GeneRIF: When unphosphorylated, dematin's two F-actin binding
            domains move independent of one another permitting them to bind
            different F-actin filaments.
            Erratum:[J Biol Chem. 2015 Jul 17;290(29):17808. doi:
            10.1074/jbc.A112.438861. PMID: 26188045]
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Mohseni,M. and Chishti,A.H.
  TITLE     Erythrocyte dematin is a candidate gene for Marie Unna hereditary
            hypotrichosis and related hairloss disorders
  JOURNAL   Am J Hematol 83 (5), 430-432 (2008)
   PUBMED   18273904
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Lutchman,M., Kim,A.C., Cheng,L., Whitehead,I.P., Oh,S.S.,
            Hanspal,M., Boukharov,A.A., Hanada,T. and Chishti,A.H.
  TITLE     Dematin interacts with the Ras-guanine nucleotide exchange factor
            Ras-GRF2 and modulates mitogen-activated protein kinase pathways
  JOURNAL   Eur J Biochem 269 (2), 638-649 (2002)
   PUBMED   11856323
REFERENCE   7  (residues 1 to 380)
  AUTHORS   Lutchman,M., Pack,S., Kim,A.C., Azim,A., Emmert-Buck,M., van
            Huffel,C., Zhuang,Z. and Chishti,A.H.
  TITLE     Loss of heterozygosity on 8p in prostate cancer implicates a role
            for dematin in tumor progression
  JOURNAL   Cancer Genet Cytogenet 115 (1), 65-69 (1999)
   PUBMED   10565303
REFERENCE   8  (residues 1 to 380)
  AUTHORS   Azim,A.C., Marfatia,S.M., Korsgren,C., Dotimas,E., Cohen,C.M. and
            Chishti,A.H.
  TITLE     Human erythrocyte dematin and protein 4.2 (pallidin) are ATP
            binding proteins
  JOURNAL   Biochemistry 35 (9), 3001-3006 (1996)
   PUBMED   8608138
REFERENCE   9  (residues 1 to 380)
  AUTHORS   Azim,A.C., Knoll,J.H., Beggs,A.H. and Chishti,A.H.
  TITLE     Isoform cloning, actin binding, and chromosomal localization of
            human erythroid dematin, a member of the villin superfamily
  JOURNAL   J Biol Chem 270 (29), 17407-17413 (1995)
   PUBMED   7615546
REFERENCE   10 (residues 1 to 380)
  AUTHORS   Rana,A.P., Ruff,P., Maalouf,G.J., Speicher,D.W. and Chishti,A.H.
  TITLE     Cloning of human erythroid dematin reveals another member of the
            villin family
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6651-6655 (1993)
   PUBMED   8341682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091171.15.
            
            On or before Dec 11, 2025 this sequence version replaced
            XP_047277462.1, XP_054215996.1.
            
            Summary: The protein encoded by this gene is an actin binding and
            bundling protein that plays a structural role in erythrocytes, by
            stabilizing and attaching the spectrin/actin cytoskeleton to the
            erythrocyte membrane in a phosphorylation-dependent manner. This
            protein contains a core domain in the N-terminus, and a headpiece
            domain in the C-terminus that binds F-actin. When purified from
            erythrocytes, this protein exists as a trimer composed of two 48
            kDa polypeptides and a 52 kDa polypeptide. The different subunits
            arise from alternative splicing in the 3' coding region, where the
            headpiece domain is located. Disruption of this gene has been
            correlated with the autosomal dominant Marie Unna hereditary
            hypotrichosis disease, while loss of heterozygosity of this gene is
            thought to play a role in prostate cancer progression. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..380
                     /product="dematin isoform 6"
                     /note="erythrocyte membrane protein band 4.9 (dematin)"
                     /calculated_mol_wt=42976
     Region          7..330
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          345..380
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..380
                     /gene="DMTN"
                     /gene_synonym="DMT; EPB49"
                     /coded_by="NM_001387747.1:495..1637"
                     /note="isoform 6 is encoded by transcript variant 57"
                     /db_xref="GeneID:2039"
                     /db_xref="HGNC:HGNC:3382"
                     /db_xref="MIM:125305"
ORIGIN      
        1 merlqkakmd nqvlgykdla aipkdkaild ierpdlmiye phftyslleh velprsrers
       61 lspkstsppp spevwadsrs pgiisqasap rttgtprtsl phfhhpetsr pdsniykkpp
      121 iykqresvgg spqtkhlied liiesskfpa aqppdpnqpa kietdywpcp pslavvetew
      181 rkrkasrrga eeeeeeeddd sgeemkalre rqreelskvt snlgkmilke emekslpirr
      241 ktrslpdrtp fhtslhqgts kssslpaygr ttlsrlqste fspsgsetgs pglqngegqr
      301 grmdrgnslp cvleqkiypy emlvvtnkgr tklppgvdrm rlerhlsaed fsrvfamspe
      361 efgklalwkr nelkkkaslf
//
LOCUS       NP_001374660             383 aa            linear   PRI 11-DEC-2025
DEFINITION  dematin isoform 2 [Homo sapiens].
ACCESSION   NP_001374660
VERSION     NP_001374660.1
DBSOURCE    REFSEQ: accession NM_001387731.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Wang,M., Chen,B., Zhang,W., Zhang,F., Qiu,Y., Lin,Y. and Yang,S.
  TITLE     Dematin inhibits glioblastoma malignancy through RhoA-mediated CDKs
            downregulation and cytoskeleton remodeling
  JOURNAL   Exp Cell Res 417 (1), 113196 (2022)
   PUBMED   35561787
  REMARK    GeneRIF: Dematin inhibits glioblastoma malignancy through
            RhoA-mediated CDKs downregulation and cytoskeleton remodeling.
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Brandt,G.S. and Bailey,S.
  TITLE     Dematin, a human erythrocyte cytoskeletal protein, is a substrate
            for a recombinant FIKK kinase from Plasmodium falciparum
  JOURNAL   Mol Biochem Parasitol 191 (1), 20-23 (2013)
   PUBMED   23973789
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Chen,L., Brown,J.W., Mok,Y.F., Hatters,D.M. and McKnight,C.J.
  TITLE     The allosteric mechanism induced by protein kinase A (PKA)
            phosphorylation of dematin (band 4.9)
  JOURNAL   J Biol Chem 288 (12), 8313-8320 (2013)
   PUBMED   23355471
  REMARK    GeneRIF: When unphosphorylated, dematin's two F-actin binding
            domains move independent of one another permitting them to bind
            different F-actin filaments.
            Erratum:[J Biol Chem. 2015 Jul 17;290(29):17808. doi:
            10.1074/jbc.A112.438861. PMID: 26188045]
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Mohseni,M. and Chishti,A.H.
  TITLE     Erythrocyte dematin is a candidate gene for Marie Unna hereditary
            hypotrichosis and related hairloss disorders
  JOURNAL   Am J Hematol 83 (5), 430-432 (2008)
   PUBMED   18273904
REFERENCE   6  (residues 1 to 383)
  AUTHORS   Lutchman,M., Kim,A.C., Cheng,L., Whitehead,I.P., Oh,S.S.,
            Hanspal,M., Boukharov,A.A., Hanada,T. and Chishti,A.H.
  TITLE     Dematin interacts with the Ras-guanine nucleotide exchange factor
            Ras-GRF2 and modulates mitogen-activated protein kinase pathways
  JOURNAL   Eur J Biochem 269 (2), 638-649 (2002)
   PUBMED   11856323
REFERENCE   7  (residues 1 to 383)
  AUTHORS   Lutchman,M., Pack,S., Kim,A.C., Azim,A., Emmert-Buck,M., van
            Huffel,C., Zhuang,Z. and Chishti,A.H.
  TITLE     Loss of heterozygosity on 8p in prostate cancer implicates a role
            for dematin in tumor progression
  JOURNAL   Cancer Genet Cytogenet 115 (1), 65-69 (1999)
   PUBMED   10565303
REFERENCE   8  (residues 1 to 383)
  AUTHORS   Azim,A.C., Marfatia,S.M., Korsgren,C., Dotimas,E., Cohen,C.M. and
            Chishti,A.H.
  TITLE     Human erythrocyte dematin and protein 4.2 (pallidin) are ATP
            binding proteins
  JOURNAL   Biochemistry 35 (9), 3001-3006 (1996)
   PUBMED   8608138
REFERENCE   9  (residues 1 to 383)
  AUTHORS   Azim,A.C., Knoll,J.H., Beggs,A.H. and Chishti,A.H.
  TITLE     Isoform cloning, actin binding, and chromosomal localization of
            human erythroid dematin, a member of the villin superfamily
  JOURNAL   J Biol Chem 270 (29), 17407-17413 (1995)
   PUBMED   7615546
REFERENCE   10 (residues 1 to 383)
  AUTHORS   Rana,A.P., Ruff,P., Maalouf,G.J., Speicher,D.W. and Chishti,A.H.
  TITLE     Cloning of human erythroid dematin reveals another member of the
            villin family
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6651-6655 (1993)
   PUBMED   8341682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091171.15.
            
            Summary: The protein encoded by this gene is an actin binding and
            bundling protein that plays a structural role in erythrocytes, by
            stabilizing and attaching the spectrin/actin cytoskeleton to the
            erythrocyte membrane in a phosphorylation-dependent manner. This
            protein contains a core domain in the N-terminus, and a headpiece
            domain in the C-terminus that binds F-actin. When purified from
            erythrocytes, this protein exists as a trimer composed of two 48
            kDa polypeptides and a 52 kDa polypeptide. The different subunits
            arise from alternative splicing in the 3' coding region, where the
            headpiece domain is located. Disruption of this gene has been
            correlated with the autosomal dominant Marie Unna hereditary
            hypotrichosis disease, while loss of heterozygosity of this gene is
            thought to play a role in prostate cancer progression. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2145774,
                              SAMEA2159080 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..383
                     /product="dematin isoform 2"
                     /note="erythrocyte membrane protein band 4.9 (dematin)"
                     /calculated_mol_wt=42957
     Region          8..333
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          348..383
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..383
                     /gene="DMTN"
                     /gene_synonym="DMT; EPB49"
                     /coded_by="NM_001387731.1:359..1510"
                     /note="isoform 2 is encoded by transcript variant 41"
                     /db_xref="GeneID:2039"
                     /db_xref="HGNC:HGNC:3382"
                     /db_xref="MIM:125305"
ORIGIN      
        1 merlqkqplt spgsvspsrd ssvpgspssi vakmdnqvlg ykdlaaipkd kaildierpd
       61 lmiyephfty sllehvelpr srerslspks tspppspevw adsrspgiis qasaprttgt
      121 prtslphfhh petsrpdsni ykkppiykqr esvggspqtk hliedliies skfpaaqppd
      181 pnqpakietd ywpcppslav vetewrkrka srrgaeeeee eedddsgeem kalrerqree
      241 lskvtsnlgk milkeemeks lpirrktrsl pdrtpfhtsl hqgtsksssl paygrttlsr
      301 lqstefspsg setgspglqi ypyemlvvtn kgrtklppgv drmrlerhls aedfsrvfam
      361 speefgklal wkrnelkkka slf
//
LOCUS       NP_001374662             383 aa            linear   PRI 11-DEC-2025
DEFINITION  dematin isoform 2 [Homo sapiens].
ACCESSION   NP_001374662
VERSION     NP_001374662.1
DBSOURCE    REFSEQ: accession NM_001387733.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Wang,M., Chen,B., Zhang,W., Zhang,F., Qiu,Y., Lin,Y. and Yang,S.
  TITLE     Dematin inhibits glioblastoma malignancy through RhoA-mediated CDKs
            downregulation and cytoskeleton remodeling
  JOURNAL   Exp Cell Res 417 (1), 113196 (2022)
   PUBMED   35561787
  REMARK    GeneRIF: Dematin inhibits glioblastoma malignancy through
            RhoA-mediated CDKs downregulation and cytoskeleton remodeling.
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Brandt,G.S. and Bailey,S.
  TITLE     Dematin, a human erythrocyte cytoskeletal protein, is a substrate
            for a recombinant FIKK kinase from Plasmodium falciparum
  JOURNAL   Mol Biochem Parasitol 191 (1), 20-23 (2013)
   PUBMED   23973789
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Chen,L., Brown,J.W., Mok,Y.F., Hatters,D.M. and McKnight,C.J.
  TITLE     The allosteric mechanism induced by protein kinase A (PKA)
            phosphorylation of dematin (band 4.9)
  JOURNAL   J Biol Chem 288 (12), 8313-8320 (2013)
   PUBMED   23355471
  REMARK    GeneRIF: When unphosphorylated, dematin's two F-actin binding
            domains move independent of one another permitting them to bind
            different F-actin filaments.
            Erratum:[J Biol Chem. 2015 Jul 17;290(29):17808. doi:
            10.1074/jbc.A112.438861. PMID: 26188045]
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Mohseni,M. and Chishti,A.H.
  TITLE     Erythrocyte dematin is a candidate gene for Marie Unna hereditary
            hypotrichosis and related hairloss disorders
  JOURNAL   Am J Hematol 83 (5), 430-432 (2008)
   PUBMED   18273904
REFERENCE   6  (residues 1 to 383)
  AUTHORS   Lutchman,M., Kim,A.C., Cheng,L., Whitehead,I.P., Oh,S.S.,
            Hanspal,M., Boukharov,A.A., Hanada,T. and Chishti,A.H.
  TITLE     Dematin interacts with the Ras-guanine nucleotide exchange factor
            Ras-GRF2 and modulates mitogen-activated protein kinase pathways
  JOURNAL   Eur J Biochem 269 (2), 638-649 (2002)
   PUBMED   11856323
REFERENCE   7  (residues 1 to 383)
  AUTHORS   Lutchman,M., Pack,S., Kim,A.C., Azim,A., Emmert-Buck,M., van
            Huffel,C., Zhuang,Z. and Chishti,A.H.
  TITLE     Loss of heterozygosity on 8p in prostate cancer implicates a role
            for dematin in tumor progression
  JOURNAL   Cancer Genet Cytogenet 115 (1), 65-69 (1999)
   PUBMED   10565303
REFERENCE   8  (residues 1 to 383)
  AUTHORS   Azim,A.C., Marfatia,S.M., Korsgren,C., Dotimas,E., Cohen,C.M. and
            Chishti,A.H.
  TITLE     Human erythrocyte dematin and protein 4.2 (pallidin) are ATP
            binding proteins
  JOURNAL   Biochemistry 35 (9), 3001-3006 (1996)
   PUBMED   8608138
REFERENCE   9  (residues 1 to 383)
  AUTHORS   Azim,A.C., Knoll,J.H., Beggs,A.H. and Chishti,A.H.
  TITLE     Isoform cloning, actin binding, and chromosomal localization of
            human erythroid dematin, a member of the villin superfamily
  JOURNAL   J Biol Chem 270 (29), 17407-17413 (1995)
   PUBMED   7615546
REFERENCE   10 (residues 1 to 383)
  AUTHORS   Rana,A.P., Ruff,P., Maalouf,G.J., Speicher,D.W. and Chishti,A.H.
  TITLE     Cloning of human erythroid dematin reveals another member of the
            villin family
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6651-6655 (1993)
   PUBMED   8341682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091171.15.
            
            Summary: The protein encoded by this gene is an actin binding and
            bundling protein that plays a structural role in erythrocytes, by
            stabilizing and attaching the spectrin/actin cytoskeleton to the
            erythrocyte membrane in a phosphorylation-dependent manner. This
            protein contains a core domain in the N-terminus, and a headpiece
            domain in the C-terminus that binds F-actin. When purified from
            erythrocytes, this protein exists as a trimer composed of two 48
            kDa polypeptides and a 52 kDa polypeptide. The different subunits
            arise from alternative splicing in the 3' coding region, where the
            headpiece domain is located. Disruption of this gene has been
            correlated with the autosomal dominant Marie Unna hereditary
            hypotrichosis disease, while loss of heterozygosity of this gene is
            thought to play a role in prostate cancer progression. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1970526,
                              SAMEA2145774 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..383
                     /product="dematin isoform 2"
                     /note="erythrocyte membrane protein band 4.9 (dematin)"
                     /calculated_mol_wt=42957
     Region          8..333
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          348..383
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..383
                     /gene="DMTN"
                     /gene_synonym="DMT; EPB49"
                     /coded_by="NM_001387733.1:492..1643"
                     /note="isoform 2 is encoded by transcript variant 43"
                     /db_xref="GeneID:2039"
                     /db_xref="HGNC:HGNC:3382"
                     /db_xref="MIM:125305"
ORIGIN      
        1 merlqkqplt spgsvspsrd ssvpgspssi vakmdnqvlg ykdlaaipkd kaildierpd
       61 lmiyephfty sllehvelpr srerslspks tspppspevw adsrspgiis qasaprttgt
      121 prtslphfhh petsrpdsni ykkppiykqr esvggspqtk hliedliies skfpaaqppd
      181 pnqpakietd ywpcppslav vetewrkrka srrgaeeeee eedddsgeem kalrerqree
      241 lskvtsnlgk milkeemeks lpirrktrsl pdrtpfhtsl hqgtsksssl paygrttlsr
      301 lqstefspsg setgspglqi ypyemlvvtn kgrtklppgv drmrlerhls aedfsrvfam
      361 speefgklal wkrnelkkka slf
//
LOCUS       NP_001374675             383 aa            linear   PRI 11-DEC-2025
DEFINITION  dematin isoform 2 [Homo sapiens].
ACCESSION   NP_001374675
VERSION     NP_001374675.1
DBSOURCE    REFSEQ: accession NM_001387746.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Wang,M., Chen,B., Zhang,W., Zhang,F., Qiu,Y., Lin,Y. and Yang,S.
  TITLE     Dematin inhibits glioblastoma malignancy through RhoA-mediated CDKs
            downregulation and cytoskeleton remodeling
  JOURNAL   Exp Cell Res 417 (1), 113196 (2022)
   PUBMED   35561787
  REMARK    GeneRIF: Dematin inhibits glioblastoma malignancy through
            RhoA-mediated CDKs downregulation and cytoskeleton remodeling.
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Brandt,G.S. and Bailey,S.
  TITLE     Dematin, a human erythrocyte cytoskeletal protein, is a substrate
            for a recombinant FIKK kinase from Plasmodium falciparum
  JOURNAL   Mol Biochem Parasitol 191 (1), 20-23 (2013)
   PUBMED   23973789
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Chen,L., Brown,J.W., Mok,Y.F., Hatters,D.M. and McKnight,C.J.
  TITLE     The allosteric mechanism induced by protein kinase A (PKA)
            phosphorylation of dematin (band 4.9)
  JOURNAL   J Biol Chem 288 (12), 8313-8320 (2013)
   PUBMED   23355471
  REMARK    GeneRIF: When unphosphorylated, dematin's two F-actin binding
            domains move independent of one another permitting them to bind
            different F-actin filaments.
            Erratum:[J Biol Chem. 2015 Jul 17;290(29):17808. doi:
            10.1074/jbc.A112.438861. PMID: 26188045]
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Mohseni,M. and Chishti,A.H.
  TITLE     Erythrocyte dematin is a candidate gene for Marie Unna hereditary
            hypotrichosis and related hairloss disorders
  JOURNAL   Am J Hematol 83 (5), 430-432 (2008)
   PUBMED   18273904
REFERENCE   6  (residues 1 to 383)
  AUTHORS   Lutchman,M., Kim,A.C., Cheng,L., Whitehead,I.P., Oh,S.S.,
            Hanspal,M., Boukharov,A.A., Hanada,T. and Chishti,A.H.
  TITLE     Dematin interacts with the Ras-guanine nucleotide exchange factor
            Ras-GRF2 and modulates mitogen-activated protein kinase pathways
  JOURNAL   Eur J Biochem 269 (2), 638-649 (2002)
   PUBMED   11856323
REFERENCE   7  (residues 1 to 383)
  AUTHORS   Lutchman,M., Pack,S., Kim,A.C., Azim,A., Emmert-Buck,M., van
            Huffel,C., Zhuang,Z. and Chishti,A.H.
  TITLE     Loss of heterozygosity on 8p in prostate cancer implicates a role
            for dematin in tumor progression
  JOURNAL   Cancer Genet Cytogenet 115 (1), 65-69 (1999)
   PUBMED   10565303
REFERENCE   8  (residues 1 to 383)
  AUTHORS   Azim,A.C., Marfatia,S.M., Korsgren,C., Dotimas,E., Cohen,C.M. and
            Chishti,A.H.
  TITLE     Human erythrocyte dematin and protein 4.2 (pallidin) are ATP
            binding proteins
  JOURNAL   Biochemistry 35 (9), 3001-3006 (1996)
   PUBMED   8608138
REFERENCE   9  (residues 1 to 383)
  AUTHORS   Azim,A.C., Knoll,J.H., Beggs,A.H. and Chishti,A.H.
  TITLE     Isoform cloning, actin binding, and chromosomal localization of
            human erythroid dematin, a member of the villin superfamily
  JOURNAL   J Biol Chem 270 (29), 17407-17413 (1995)
   PUBMED   7615546
REFERENCE   10 (residues 1 to 383)
  AUTHORS   Rana,A.P., Ruff,P., Maalouf,G.J., Speicher,D.W. and Chishti,A.H.
  TITLE     Cloning of human erythroid dematin reveals another member of the
            villin family
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6651-6655 (1993)
   PUBMED   8341682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091171.15.
            
            Summary: The protein encoded by this gene is an actin binding and
            bundling protein that plays a structural role in erythrocytes, by
            stabilizing and attaching the spectrin/actin cytoskeleton to the
            erythrocyte membrane in a phosphorylation-dependent manner. This
            protein contains a core domain in the N-terminus, and a headpiece
            domain in the C-terminus that binds F-actin. When purified from
            erythrocytes, this protein exists as a trimer composed of two 48
            kDa polypeptides and a 52 kDa polypeptide. The different subunits
            arise from alternative splicing in the 3' coding region, where the
            headpiece domain is located. Disruption of this gene has been
            correlated with the autosomal dominant Marie Unna hereditary
            hypotrichosis disease, while loss of heterozygosity of this gene is
            thought to play a role in prostate cancer progression. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2149004 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..383
                     /product="dematin isoform 2"
                     /note="erythrocyte membrane protein band 4.9 (dematin)"
                     /calculated_mol_wt=42957
     Region          8..333
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          348..383
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..383
                     /gene="DMTN"
                     /gene_synonym="DMT; EPB49"
                     /coded_by="NM_001387746.1:486..1637"
                     /note="isoform 2 is encoded by transcript variant 56"
                     /db_xref="GeneID:2039"
                     /db_xref="HGNC:HGNC:3382"
                     /db_xref="MIM:125305"
ORIGIN      
        1 merlqkqplt spgsvspsrd ssvpgspssi vakmdnqvlg ykdlaaipkd kaildierpd
       61 lmiyephfty sllehvelpr srerslspks tspppspevw adsrspgiis qasaprttgt
      121 prtslphfhh petsrpdsni ykkppiykqr esvggspqtk hliedliies skfpaaqppd
      181 pnqpakietd ywpcppslav vetewrkrka srrgaeeeee eedddsgeem kalrerqree
      241 lskvtsnlgk milkeemeks lpirrktrsl pdrtpfhtsl hqgtsksssl paygrttlsr
      301 lqstefspsg setgspglqi ypyemlvvtn kgrtklppgv drmrlerhls aedfsrvfam
      361 speefgklal wkrnelkkka slf
//
LOCUS       NP_001374677             383 aa            linear   PRI 11-DEC-2025
DEFINITION  dematin isoform 2 [Homo sapiens].
ACCESSION   NP_001374677
VERSION     NP_001374677.1
DBSOURCE    REFSEQ: accession NM_001387748.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 383)
  AUTHORS   Wang,M., Chen,B., Zhang,W., Zhang,F., Qiu,Y., Lin,Y. and Yang,S.
  TITLE     Dematin inhibits glioblastoma malignancy through RhoA-mediated CDKs
            downregulation and cytoskeleton remodeling
  JOURNAL   Exp Cell Res 417 (1), 113196 (2022)
   PUBMED   35561787
  REMARK    GeneRIF: Dematin inhibits glioblastoma malignancy through
            RhoA-mediated CDKs downregulation and cytoskeleton remodeling.
REFERENCE   2  (residues 1 to 383)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 383)
  AUTHORS   Brandt,G.S. and Bailey,S.
  TITLE     Dematin, a human erythrocyte cytoskeletal protein, is a substrate
            for a recombinant FIKK kinase from Plasmodium falciparum
  JOURNAL   Mol Biochem Parasitol 191 (1), 20-23 (2013)
   PUBMED   23973789
REFERENCE   4  (residues 1 to 383)
  AUTHORS   Chen,L., Brown,J.W., Mok,Y.F., Hatters,D.M. and McKnight,C.J.
  TITLE     The allosteric mechanism induced by protein kinase A (PKA)
            phosphorylation of dematin (band 4.9)
  JOURNAL   J Biol Chem 288 (12), 8313-8320 (2013)
   PUBMED   23355471
  REMARK    GeneRIF: When unphosphorylated, dematin's two F-actin binding
            domains move independent of one another permitting them to bind
            different F-actin filaments.
            Erratum:[J Biol Chem. 2015 Jul 17;290(29):17808. doi:
            10.1074/jbc.A112.438861. PMID: 26188045]
REFERENCE   5  (residues 1 to 383)
  AUTHORS   Mohseni,M. and Chishti,A.H.
  TITLE     Erythrocyte dematin is a candidate gene for Marie Unna hereditary
            hypotrichosis and related hairloss disorders
  JOURNAL   Am J Hematol 83 (5), 430-432 (2008)
   PUBMED   18273904
REFERENCE   6  (residues 1 to 383)
  AUTHORS   Lutchman,M., Kim,A.C., Cheng,L., Whitehead,I.P., Oh,S.S.,
            Hanspal,M., Boukharov,A.A., Hanada,T. and Chishti,A.H.
  TITLE     Dematin interacts with the Ras-guanine nucleotide exchange factor
            Ras-GRF2 and modulates mitogen-activated protein kinase pathways
  JOURNAL   Eur J Biochem 269 (2), 638-649 (2002)
   PUBMED   11856323
REFERENCE   7  (residues 1 to 383)
  AUTHORS   Lutchman,M., Pack,S., Kim,A.C., Azim,A., Emmert-Buck,M., van
            Huffel,C., Zhuang,Z. and Chishti,A.H.
  TITLE     Loss of heterozygosity on 8p in prostate cancer implicates a role
            for dematin in tumor progression
  JOURNAL   Cancer Genet Cytogenet 115 (1), 65-69 (1999)
   PUBMED   10565303
REFERENCE   8  (residues 1 to 383)
  AUTHORS   Azim,A.C., Marfatia,S.M., Korsgren,C., Dotimas,E., Cohen,C.M. and
            Chishti,A.H.
  TITLE     Human erythrocyte dematin and protein 4.2 (pallidin) are ATP
            binding proteins
  JOURNAL   Biochemistry 35 (9), 3001-3006 (1996)
   PUBMED   8608138
REFERENCE   9  (residues 1 to 383)
  AUTHORS   Azim,A.C., Knoll,J.H., Beggs,A.H. and Chishti,A.H.
  TITLE     Isoform cloning, actin binding, and chromosomal localization of
            human erythroid dematin, a member of the villin superfamily
  JOURNAL   J Biol Chem 270 (29), 17407-17413 (1995)
   PUBMED   7615546
REFERENCE   10 (residues 1 to 383)
  AUTHORS   Rana,A.P., Ruff,P., Maalouf,G.J., Speicher,D.W. and Chishti,A.H.
  TITLE     Cloning of human erythroid dematin reveals another member of the
            villin family
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6651-6655 (1993)
   PUBMED   8341682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091171.15.
            
            Summary: The protein encoded by this gene is an actin binding and
            bundling protein that plays a structural role in erythrocytes, by
            stabilizing and attaching the spectrin/actin cytoskeleton to the
            erythrocyte membrane in a phosphorylation-dependent manner. This
            protein contains a core domain in the N-terminus, and a headpiece
            domain in the C-terminus that binds F-actin. When purified from
            erythrocytes, this protein exists as a trimer composed of two 48
            kDa polypeptides and a 52 kDa polypeptide. The different subunits
            arise from alternative splicing in the 3' coding region, where the
            headpiece domain is located. Disruption of this gene has been
            correlated with the autosomal dominant Marie Unna hereditary
            hypotrichosis disease, while loss of heterozygosity of this gene is
            thought to play a role in prostate cancer progression. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..383
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..383
                     /product="dematin isoform 2"
                     /note="erythrocyte membrane protein band 4.9 (dematin)"
                     /calculated_mol_wt=42957
     Region          8..333
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          348..383
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..383
                     /gene="DMTN"
                     /gene_synonym="DMT; EPB49"
                     /coded_by="NM_001387748.1:495..1646"
                     /note="isoform 2 is encoded by transcript variant 58"
                     /db_xref="GeneID:2039"
                     /db_xref="HGNC:HGNC:3382"
                     /db_xref="MIM:125305"
ORIGIN      
        1 merlqkqplt spgsvspsrd ssvpgspssi vakmdnqvlg ykdlaaipkd kaildierpd
       61 lmiyephfty sllehvelpr srerslspks tspppspevw adsrspgiis qasaprttgt
      121 prtslphfhh petsrpdsni ykkppiykqr esvggspqtk hliedliies skfpaaqppd
      181 pnqpakietd ywpcppslav vetewrkrka srrgaeeeee eedddsgeem kalrerqree
      241 lskvtsnlgk milkeemeks lpirrktrsl pdrtpfhtsl hqgtsksssl paygrttlsr
      301 lqstefspsg setgspglqi ypyemlvvtn kgrtklppgv drmrlerhls aedfsrvfam
      361 speefgklal wkrnelkkka slf
//
LOCUS       NP_001374687             368 aa            linear   PRI 11-DEC-2025
DEFINITION  dematin isoform 8 [Homo sapiens].
ACCESSION   NP_001374687 XP_016868679
VERSION     NP_001374687.1
DBSOURCE    REFSEQ: accession NM_001387758.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Wang,M., Chen,B., Zhang,W., Zhang,F., Qiu,Y., Lin,Y. and Yang,S.
  TITLE     Dematin inhibits glioblastoma malignancy through RhoA-mediated CDKs
            downregulation and cytoskeleton remodeling
  JOURNAL   Exp Cell Res 417 (1), 113196 (2022)
   PUBMED   35561787
  REMARK    GeneRIF: Dematin inhibits glioblastoma malignancy through
            RhoA-mediated CDKs downregulation and cytoskeleton remodeling.
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Brandt,G.S. and Bailey,S.
  TITLE     Dematin, a human erythrocyte cytoskeletal protein, is a substrate
            for a recombinant FIKK kinase from Plasmodium falciparum
  JOURNAL   Mol Biochem Parasitol 191 (1), 20-23 (2013)
   PUBMED   23973789
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Chen,L., Brown,J.W., Mok,Y.F., Hatters,D.M. and McKnight,C.J.
  TITLE     The allosteric mechanism induced by protein kinase A (PKA)
            phosphorylation of dematin (band 4.9)
  JOURNAL   J Biol Chem 288 (12), 8313-8320 (2013)
   PUBMED   23355471
  REMARK    GeneRIF: When unphosphorylated, dematin's two F-actin binding
            domains move independent of one another permitting them to bind
            different F-actin filaments.
            Erratum:[J Biol Chem. 2015 Jul 17;290(29):17808. doi:
            10.1074/jbc.A112.438861. PMID: 26188045]
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Mohseni,M. and Chishti,A.H.
  TITLE     Erythrocyte dematin is a candidate gene for Marie Unna hereditary
            hypotrichosis and related hairloss disorders
  JOURNAL   Am J Hematol 83 (5), 430-432 (2008)
   PUBMED   18273904
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Lutchman,M., Kim,A.C., Cheng,L., Whitehead,I.P., Oh,S.S.,
            Hanspal,M., Boukharov,A.A., Hanada,T. and Chishti,A.H.
  TITLE     Dematin interacts with the Ras-guanine nucleotide exchange factor
            Ras-GRF2 and modulates mitogen-activated protein kinase pathways
  JOURNAL   Eur J Biochem 269 (2), 638-649 (2002)
   PUBMED   11856323
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Lutchman,M., Pack,S., Kim,A.C., Azim,A., Emmert-Buck,M., van
            Huffel,C., Zhuang,Z. and Chishti,A.H.
  TITLE     Loss of heterozygosity on 8p in prostate cancer implicates a role
            for dematin in tumor progression
  JOURNAL   Cancer Genet Cytogenet 115 (1), 65-69 (1999)
   PUBMED   10565303
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Azim,A.C., Marfatia,S.M., Korsgren,C., Dotimas,E., Cohen,C.M. and
            Chishti,A.H.
  TITLE     Human erythrocyte dematin and protein 4.2 (pallidin) are ATP
            binding proteins
  JOURNAL   Biochemistry 35 (9), 3001-3006 (1996)
   PUBMED   8608138
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Azim,A.C., Knoll,J.H., Beggs,A.H. and Chishti,A.H.
  TITLE     Isoform cloning, actin binding, and chromosomal localization of
            human erythroid dematin, a member of the villin superfamily
  JOURNAL   J Biol Chem 270 (29), 17407-17413 (1995)
   PUBMED   7615546
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Rana,A.P., Ruff,P., Maalouf,G.J., Speicher,D.W. and Chishti,A.H.
  TITLE     Cloning of human erythroid dematin reveals another member of the
            villin family
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6651-6655 (1993)
   PUBMED   8341682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091171.15.
            
            On Dec 11, 2025 this sequence version replaced XP_016868679.1.
            
            Summary: The protein encoded by this gene is an actin binding and
            bundling protein that plays a structural role in erythrocytes, by
            stabilizing and attaching the spectrin/actin cytoskeleton to the
            erythrocyte membrane in a phosphorylation-dependent manner. This
            protein contains a core domain in the N-terminus, and a headpiece
            domain in the C-terminus that binds F-actin. When purified from
            erythrocytes, this protein exists as a trimer composed of two 48
            kDa polypeptides and a 52 kDa polypeptide. The different subunits
            arise from alternative splicing in the 3' coding region, where the
            headpiece domain is located. Disruption of this gene has been
            correlated with the autosomal dominant Marie Unna hereditary
            hypotrichosis disease, while loss of heterozygosity of this gene is
            thought to play a role in prostate cancer progression. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2145544 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..368
                     /product="dematin isoform 8"
                     /note="erythrocyte membrane protein band 4.9 (dematin)"
                     /calculated_mol_wt=41408
     Region          8..318
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          333..368
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..368
                     /gene="DMTN"
                     /gene_synonym="DMT; EPB49"
                     /coded_by="NM_001387758.1:464..1570"
                     /note="isoform 8 is encoded by transcript variant 68"
                     /db_xref="GeneID:2039"
                     /db_xref="HGNC:HGNC:3382"
                     /db_xref="MIM:125305"
ORIGIN      
        1 merlqkqplt spgsvspsrd ssvpgspssi vakmdnqvlg ykdlaaipkd kaildierpd
       61 lmiyephfty sllehvelpr srevwadsrs pgiisqasap rttgtprtsl phfhhpetsr
      121 pdsniykkpp iykqresvgg spqtkhlied liiesskfpa aqppdpnqpa kietdywpcp
      181 pslavvetew rkrkasrrga eeeeeeeddd sgeemkalre rqreelskvt snlgkmilke
      241 emekslpirr ktrslpdrtp fhtslhqgts kssslpaygr ttlsrlqste fspsgsetgs
      301 pglqiypyem lvvtnkgrtk lppgvdrmrl erhlsaedfs rvfamspeef gklalwkrne
      361 lkkkaslf
//
LOCUS       NP_001374668             343 aa            linear   PRI 11-DEC-2025
DEFINITION  dematin isoform 7 [Homo sapiens].
ACCESSION   NP_001374668
VERSION     NP_001374668.1
DBSOURCE    REFSEQ: accession NM_001387739.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Wang,M., Chen,B., Zhang,W., Zhang,F., Qiu,Y., Lin,Y. and Yang,S.
  TITLE     Dematin inhibits glioblastoma malignancy through RhoA-mediated CDKs
            downregulation and cytoskeleton remodeling
  JOURNAL   Exp Cell Res 417 (1), 113196 (2022)
   PUBMED   35561787
  REMARK    GeneRIF: Dematin inhibits glioblastoma malignancy through
            RhoA-mediated CDKs downregulation and cytoskeleton remodeling.
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Brandt,G.S. and Bailey,S.
  TITLE     Dematin, a human erythrocyte cytoskeletal protein, is a substrate
            for a recombinant FIKK kinase from Plasmodium falciparum
  JOURNAL   Mol Biochem Parasitol 191 (1), 20-23 (2013)
   PUBMED   23973789
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Chen,L., Brown,J.W., Mok,Y.F., Hatters,D.M. and McKnight,C.J.
  TITLE     The allosteric mechanism induced by protein kinase A (PKA)
            phosphorylation of dematin (band 4.9)
  JOURNAL   J Biol Chem 288 (12), 8313-8320 (2013)
   PUBMED   23355471
  REMARK    GeneRIF: When unphosphorylated, dematin's two F-actin binding
            domains move independent of one another permitting them to bind
            different F-actin filaments.
            Erratum:[J Biol Chem. 2015 Jul 17;290(29):17808. doi:
            10.1074/jbc.A112.438861. PMID: 26188045]
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Mohseni,M. and Chishti,A.H.
  TITLE     Erythrocyte dematin is a candidate gene for Marie Unna hereditary
            hypotrichosis and related hairloss disorders
  JOURNAL   Am J Hematol 83 (5), 430-432 (2008)
   PUBMED   18273904
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Lutchman,M., Kim,A.C., Cheng,L., Whitehead,I.P., Oh,S.S.,
            Hanspal,M., Boukharov,A.A., Hanada,T. and Chishti,A.H.
  TITLE     Dematin interacts with the Ras-guanine nucleotide exchange factor
            Ras-GRF2 and modulates mitogen-activated protein kinase pathways
  JOURNAL   Eur J Biochem 269 (2), 638-649 (2002)
   PUBMED   11856323
REFERENCE   7  (residues 1 to 343)
  AUTHORS   Lutchman,M., Pack,S., Kim,A.C., Azim,A., Emmert-Buck,M., van
            Huffel,C., Zhuang,Z. and Chishti,A.H.
  TITLE     Loss of heterozygosity on 8p in prostate cancer implicates a role
            for dematin in tumor progression
  JOURNAL   Cancer Genet Cytogenet 115 (1), 65-69 (1999)
   PUBMED   10565303
REFERENCE   8  (residues 1 to 343)
  AUTHORS   Azim,A.C., Marfatia,S.M., Korsgren,C., Dotimas,E., Cohen,C.M. and
            Chishti,A.H.
  TITLE     Human erythrocyte dematin and protein 4.2 (pallidin) are ATP
            binding proteins
  JOURNAL   Biochemistry 35 (9), 3001-3006 (1996)
   PUBMED   8608138
REFERENCE   9  (residues 1 to 343)
  AUTHORS   Azim,A.C., Knoll,J.H., Beggs,A.H. and Chishti,A.H.
  TITLE     Isoform cloning, actin binding, and chromosomal localization of
            human erythroid dematin, a member of the villin superfamily
  JOURNAL   J Biol Chem 270 (29), 17407-17413 (1995)
   PUBMED   7615546
REFERENCE   10 (residues 1 to 343)
  AUTHORS   Rana,A.P., Ruff,P., Maalouf,G.J., Speicher,D.W. and Chishti,A.H.
  TITLE     Cloning of human erythroid dematin reveals another member of the
            villin family
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6651-6655 (1993)
   PUBMED   8341682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091171.15.
            
            Summary: The protein encoded by this gene is an actin binding and
            bundling protein that plays a structural role in erythrocytes, by
            stabilizing and attaching the spectrin/actin cytoskeleton to the
            erythrocyte membrane in a phosphorylation-dependent manner. This
            protein contains a core domain in the N-terminus, and a headpiece
            domain in the C-terminus that binds F-actin. When purified from
            erythrocytes, this protein exists as a trimer composed of two 48
            kDa polypeptides and a 52 kDa polypeptide. The different subunits
            arise from alternative splicing in the 3' coding region, where the
            headpiece domain is located. Disruption of this gene has been
            correlated with the autosomal dominant Marie Unna hereditary
            hypotrichosis disease, while loss of heterozygosity of this gene is
            thought to play a role in prostate cancer progression. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1970526,
                              SAMEA2145544 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..343
                     /product="dematin isoform 7"
                     /note="erythrocyte membrane protein band 4.9 (dematin)"
                     /calculated_mol_wt=39000
     Region          7..293
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          308..343
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..343
                     /gene="DMTN"
                     /gene_synonym="DMT; EPB49"
                     /coded_by="NM_001387739.1:362..1393"
                     /note="isoform 7 is encoded by transcript variant 49"
                     /db_xref="GeneID:2039"
                     /db_xref="HGNC:HGNC:3382"
                     /db_xref="MIM:125305"
ORIGIN      
        1 merlqkakmd nqvlgykdla aipkdkaild ierpdlmiye phftyslleh velprsrevw
       61 adsrspgiis qasaprttgt prtslphfhh petsrpdsni ykkppiykqr esvggspqtk
      121 hliedliies skfpaaqppd pnqpakietd ywpcppslav vetewrkrka srrgaeeeee
      181 eedddsgeem kalrerqree lskvtsnlgk milkeemeks lpirrktrsl pdrtpfhtsl
      241 hqgtsksssl paygrttlsr lqstefspsg setgspglqi ypyemlvvtn kgrtklppgv
      301 drmrlerhls aedfsrvfam speefgklal wkrnelkkka slf
//
LOCUS       NP_001374667             368 aa            linear   PRI 11-DEC-2025
DEFINITION  dematin isoform 8 [Homo sapiens].
ACCESSION   NP_001374667 XP_016868680
VERSION     NP_001374667.1
DBSOURCE    REFSEQ: accession NM_001387738.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Wang,M., Chen,B., Zhang,W., Zhang,F., Qiu,Y., Lin,Y. and Yang,S.
  TITLE     Dematin inhibits glioblastoma malignancy through RhoA-mediated CDKs
            downregulation and cytoskeleton remodeling
  JOURNAL   Exp Cell Res 417 (1), 113196 (2022)
   PUBMED   35561787
  REMARK    GeneRIF: Dematin inhibits glioblastoma malignancy through
            RhoA-mediated CDKs downregulation and cytoskeleton remodeling.
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Brandt,G.S. and Bailey,S.
  TITLE     Dematin, a human erythrocyte cytoskeletal protein, is a substrate
            for a recombinant FIKK kinase from Plasmodium falciparum
  JOURNAL   Mol Biochem Parasitol 191 (1), 20-23 (2013)
   PUBMED   23973789
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Chen,L., Brown,J.W., Mok,Y.F., Hatters,D.M. and McKnight,C.J.
  TITLE     The allosteric mechanism induced by protein kinase A (PKA)
            phosphorylation of dematin (band 4.9)
  JOURNAL   J Biol Chem 288 (12), 8313-8320 (2013)
   PUBMED   23355471
  REMARK    GeneRIF: When unphosphorylated, dematin's two F-actin binding
            domains move independent of one another permitting them to bind
            different F-actin filaments.
            Erratum:[J Biol Chem. 2015 Jul 17;290(29):17808. doi:
            10.1074/jbc.A112.438861. PMID: 26188045]
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Mohseni,M. and Chishti,A.H.
  TITLE     Erythrocyte dematin is a candidate gene for Marie Unna hereditary
            hypotrichosis and related hairloss disorders
  JOURNAL   Am J Hematol 83 (5), 430-432 (2008)
   PUBMED   18273904
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Lutchman,M., Kim,A.C., Cheng,L., Whitehead,I.P., Oh,S.S.,
            Hanspal,M., Boukharov,A.A., Hanada,T. and Chishti,A.H.
  TITLE     Dematin interacts with the Ras-guanine nucleotide exchange factor
            Ras-GRF2 and modulates mitogen-activated protein kinase pathways
  JOURNAL   Eur J Biochem 269 (2), 638-649 (2002)
   PUBMED   11856323
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Lutchman,M., Pack,S., Kim,A.C., Azim,A., Emmert-Buck,M., van
            Huffel,C., Zhuang,Z. and Chishti,A.H.
  TITLE     Loss of heterozygosity on 8p in prostate cancer implicates a role
            for dematin in tumor progression
  JOURNAL   Cancer Genet Cytogenet 115 (1), 65-69 (1999)
   PUBMED   10565303
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Azim,A.C., Marfatia,S.M., Korsgren,C., Dotimas,E., Cohen,C.M. and
            Chishti,A.H.
  TITLE     Human erythrocyte dematin and protein 4.2 (pallidin) are ATP
            binding proteins
  JOURNAL   Biochemistry 35 (9), 3001-3006 (1996)
   PUBMED   8608138
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Azim,A.C., Knoll,J.H., Beggs,A.H. and Chishti,A.H.
  TITLE     Isoform cloning, actin binding, and chromosomal localization of
            human erythroid dematin, a member of the villin superfamily
  JOURNAL   J Biol Chem 270 (29), 17407-17413 (1995)
   PUBMED   7615546
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Rana,A.P., Ruff,P., Maalouf,G.J., Speicher,D.W. and Chishti,A.H.
  TITLE     Cloning of human erythroid dematin reveals another member of the
            villin family
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6651-6655 (1993)
   PUBMED   8341682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091171.15.
            
            On Dec 11, 2025 this sequence version replaced XP_016868680.1.
            
            Summary: The protein encoded by this gene is an actin binding and
            bundling protein that plays a structural role in erythrocytes, by
            stabilizing and attaching the spectrin/actin cytoskeleton to the
            erythrocyte membrane in a phosphorylation-dependent manner. This
            protein contains a core domain in the N-terminus, and a headpiece
            domain in the C-terminus that binds F-actin. When purified from
            erythrocytes, this protein exists as a trimer composed of two 48
            kDa polypeptides and a 52 kDa polypeptide. The different subunits
            arise from alternative splicing in the 3' coding region, where the
            headpiece domain is located. Disruption of this gene has been
            correlated with the autosomal dominant Marie Unna hereditary
            hypotrichosis disease, while loss of heterozygosity of this gene is
            thought to play a role in prostate cancer progression. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1970526 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..368
                     /product="dematin isoform 8"
                     /note="erythrocyte membrane protein band 4.9 (dematin)"
                     /calculated_mol_wt=41408
     Region          8..318
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          333..368
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..368
                     /gene="DMTN"
                     /gene_synonym="DMT; EPB49"
                     /coded_by="NM_001387738.1:273..1379"
                     /note="isoform 8 is encoded by transcript variant 48"
                     /db_xref="GeneID:2039"
                     /db_xref="HGNC:HGNC:3382"
                     /db_xref="MIM:125305"
ORIGIN      
        1 merlqkqplt spgsvspsrd ssvpgspssi vakmdnqvlg ykdlaaipkd kaildierpd
       61 lmiyephfty sllehvelpr srevwadsrs pgiisqasap rttgtprtsl phfhhpetsr
      121 pdsniykkpp iykqresvgg spqtkhlied liiesskfpa aqppdpnqpa kietdywpcp
      181 pslavvetew rkrkasrrga eeeeeeeddd sgeemkalre rqreelskvt snlgkmilke
      241 emekslpirr ktrslpdrtp fhtslhqgts kssslpaygr ttlsrlqste fspsgsetgs
      301 pglqiypyem lvvtnkgrtk lppgvdrmrl erhlsaedfs rvfamspeef gklalwkrne
      361 lkkkaslf
//
LOCUS       NP_001374654             358 aa            linear   PRI 11-DEC-2025
DEFINITION  dematin isoform 3 [Homo sapiens].
ACCESSION   NP_001374654
VERSION     NP_001374654.1
DBSOURCE    REFSEQ: accession NM_001387725.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Wang,M., Chen,B., Zhang,W., Zhang,F., Qiu,Y., Lin,Y. and Yang,S.
  TITLE     Dematin inhibits glioblastoma malignancy through RhoA-mediated CDKs
            downregulation and cytoskeleton remodeling
  JOURNAL   Exp Cell Res 417 (1), 113196 (2022)
   PUBMED   35561787
  REMARK    GeneRIF: Dematin inhibits glioblastoma malignancy through
            RhoA-mediated CDKs downregulation and cytoskeleton remodeling.
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Brandt,G.S. and Bailey,S.
  TITLE     Dematin, a human erythrocyte cytoskeletal protein, is a substrate
            for a recombinant FIKK kinase from Plasmodium falciparum
  JOURNAL   Mol Biochem Parasitol 191 (1), 20-23 (2013)
   PUBMED   23973789
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Chen,L., Brown,J.W., Mok,Y.F., Hatters,D.M. and McKnight,C.J.
  TITLE     The allosteric mechanism induced by protein kinase A (PKA)
            phosphorylation of dematin (band 4.9)
  JOURNAL   J Biol Chem 288 (12), 8313-8320 (2013)
   PUBMED   23355471
  REMARK    GeneRIF: When unphosphorylated, dematin's two F-actin binding
            domains move independent of one another permitting them to bind
            different F-actin filaments.
            Erratum:[J Biol Chem. 2015 Jul 17;290(29):17808. doi:
            10.1074/jbc.A112.438861. PMID: 26188045]
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Mohseni,M. and Chishti,A.H.
  TITLE     Erythrocyte dematin is a candidate gene for Marie Unna hereditary
            hypotrichosis and related hairloss disorders
  JOURNAL   Am J Hematol 83 (5), 430-432 (2008)
   PUBMED   18273904
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Lutchman,M., Kim,A.C., Cheng,L., Whitehead,I.P., Oh,S.S.,
            Hanspal,M., Boukharov,A.A., Hanada,T. and Chishti,A.H.
  TITLE     Dematin interacts with the Ras-guanine nucleotide exchange factor
            Ras-GRF2 and modulates mitogen-activated protein kinase pathways
  JOURNAL   Eur J Biochem 269 (2), 638-649 (2002)
   PUBMED   11856323
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Lutchman,M., Pack,S., Kim,A.C., Azim,A., Emmert-Buck,M., van
            Huffel,C., Zhuang,Z. and Chishti,A.H.
  TITLE     Loss of heterozygosity on 8p in prostate cancer implicates a role
            for dematin in tumor progression
  JOURNAL   Cancer Genet Cytogenet 115 (1), 65-69 (1999)
   PUBMED   10565303
REFERENCE   8  (residues 1 to 358)
  AUTHORS   Azim,A.C., Marfatia,S.M., Korsgren,C., Dotimas,E., Cohen,C.M. and
            Chishti,A.H.
  TITLE     Human erythrocyte dematin and protein 4.2 (pallidin) are ATP
            binding proteins
  JOURNAL   Biochemistry 35 (9), 3001-3006 (1996)
   PUBMED   8608138
REFERENCE   9  (residues 1 to 358)
  AUTHORS   Azim,A.C., Knoll,J.H., Beggs,A.H. and Chishti,A.H.
  TITLE     Isoform cloning, actin binding, and chromosomal localization of
            human erythroid dematin, a member of the villin superfamily
  JOURNAL   J Biol Chem 270 (29), 17407-17413 (1995)
   PUBMED   7615546
REFERENCE   10 (residues 1 to 358)
  AUTHORS   Rana,A.P., Ruff,P., Maalouf,G.J., Speicher,D.W. and Chishti,A.H.
  TITLE     Cloning of human erythroid dematin reveals another member of the
            villin family
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6651-6655 (1993)
   PUBMED   8341682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091171.15.
            
            Summary: The protein encoded by this gene is an actin binding and
            bundling protein that plays a structural role in erythrocytes, by
            stabilizing and attaching the spectrin/actin cytoskeleton to the
            erythrocyte membrane in a phosphorylation-dependent manner. This
            protein contains a core domain in the N-terminus, and a headpiece
            domain in the C-terminus that binds F-actin. When purified from
            erythrocytes, this protein exists as a trimer composed of two 48
            kDa polypeptides and a 52 kDa polypeptide. The different subunits
            arise from alternative splicing in the 3' coding region, where the
            headpiece domain is located. Disruption of this gene has been
            correlated with the autosomal dominant Marie Unna hereditary
            hypotrichosis disease, while loss of heterozygosity of this gene is
            thought to play a role in prostate cancer progression. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1970526 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..358
                     /product="dematin isoform 3"
                     /note="erythrocyte membrane protein band 4.9 (dematin)"
                     /calculated_mol_wt=40549
     Region          7..308
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Region          323..358
                     /region_name="VHP"
                     /note="Villin headpiece domain; smart00153"
                     /db_xref="CDD:128458"
     CDS             1..358
                     /gene="DMTN"
                     /gene_synonym="DMT; EPB49"
                     /coded_by="NM_001387725.1:466..1542"
                     /note="isoform 3 is encoded by transcript variant 35"
                     /db_xref="GeneID:2039"
                     /db_xref="HGNC:HGNC:3382"
                     /db_xref="MIM:125305"
ORIGIN      
        1 merlqkakmd nqvlgykdla aipkdkaild ierpdlmiye phftyslleh velprsrers
       61 lspkstsppp spevwadsrs pgiisqasap rttgtprtsl phfhhpetsr pdsniykkpp
      121 iykqresvgg spqtkhlied liiesskfpa aqppdpnqpa kietdywpcp pslavvetew
      181 rkrkasrrga eeeeeeeddd sgeemkalre rqreelskvt snlgkmilke emekslpirr
      241 ktrslpdrtp fhtslhqgts kssslpaygr ttlsrlqste fspsgsetgs pglqiypyem
      301 lvvtnkgrtk lppgvdrmrl erhlsaedfs rvfamspeef gklalwkrne lkkkaslf
//
LOCUS       NP_001375365             431 aa            linear   PRI 11-DEC-2025
DEFINITION  coronin-6 isoform 5 [Homo sapiens].
ACCESSION   NP_001375365
VERSION     NP_001375365.1
DBSOURCE    REFSEQ: accession NM_001388436.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Cardinali,B., Cappella,M., Provenzano,C., Garcia-Manteiga,J.M.,
            Lazarevic,D., Cittaro,D., Martelli,F. and Falcone,G.
  TITLE     MicroRNA-222 regulates muscle alternative splicing through Rbm24
            during differentiation of skeletal muscle cells
  JOURNAL   Cell Death Dis 7 (2), e2086 (2016)
   PUBMED   26844700
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Morris,M.R., Ricketts,C.J., Gentle,D., McRonald,F., Carli,N.,
            Khalili,H., Brown,M., Kishida,T., Yao,M., Banks,R.E., Clarke,N.,
            Latif,F. and Maher,E.R.
  TITLE     Genome-wide methylation analysis identifies epigenetically
            inactivated candidate tumour suppressor genes in renal cell
            carcinoma
  JOURNAL   Oncogene 30 (12), 1390-1401 (2011)
   PUBMED   21132003
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Zody,M.C., Garber,M., Adams,D.J., Sharpe,T., Harrow,J.,
            Lupski,J.R., Nicholson,C., Searle,S.M., Wilming,L., Young,S.K.,
            Abouelleil,A., Allen,N.R., Bi,W., Bloom,T., Borowsky,M.L.,
            Bugalter,B.E., Butler,J., Chang,J.L., Chen,C.K., Cook,A., Corum,B.,
            Cuomo,C.A., de Jong,P.J., DeCaprio,D., Dewar,K., FitzGerald,M.,
            Gilbert,J., Gibson,R., Gnerre,S., Goldstein,S., Grafham,D.V.,
            Grocock,R., Hafez,N., Hagopian,D.S., Hart,E., Norman,C.H.,
            Humphray,S., Jaffe,D.B., Jones,M., Kamal,M., Khodiyar,V.K.,
            LaButti,K., Laird,G., Lehoczky,J., Liu,X., Lokyitsang,T.,
            Loveland,J., Lui,A., Macdonald,P., Major,J.E., Matthews,L.,
            Mauceli,E., McCarroll,S.A., Mihalev,A.H., Mudge,J., Nguyen,C.,
            Nicol,R., O'Leary,S.B., Osoegawa,K., Schwartz,D.C., Shaw-Smith,C.,
            Stankiewicz,P., Steward,C., Swarbreck,D., Venkataraman,V.,
            Whittaker,C.A., Yang,X., Zimmer,A.R., Bradley,A., Hubbard,T.,
            Birren,B.W., Rogers,J., Lander,E.S. and Nusbaum,C.
  TITLE     DNA sequence of human chromosome 17 and analysis of rearrangement
            in the human lineage
  JOURNAL   Nature 440 (7087), 1045-1049 (2006)
   PUBMED   16625196
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104564.11.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1058555.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..431
                     /product="coronin-6 isoform 5"
                     /note="coronin, actin binding protein 6; clipin-E;
                     coronin-like protein E"
                     /calculated_mol_wt=48025
     Region          9..425
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          37..79
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          85..129
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          134..171
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          179..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          229..270
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..431
                     /gene="CORO6"
                     /gene_synonym="ClipinE"
                     /coded_by="NM_001388436.1:228..1523"
                     /note="isoform 5 is encoded by transcript variant 8"
                     /db_xref="GeneID:84940"
                     /db_xref="HGNC:HGNC:21356"
                     /db_xref="MIM:621442"
ORIGIN      
        1 msrrvvrqsk frhvfgqaak adqayedirv skvtwdssfc avnpkflaii veaggggafi
       61 vlplaktgrv dknyplvtgh tapvldidwc phndnviasa sddttimvwq ipdytpmrni
      121 tepiitlegh skrvgilswh ptarnvllsa ggdnviiiwn vgtgevllsl ddmhpdvihs
      181 vcwnsngsll attckdktlr iidprkgqvv annfeepval qemdtsngvl lpfydpdssi
      241 vylcgkgdss iryfeitdep pfvhylntfs skepqrgmgf mpkrgldvsk ceiarfyklh
      301 erkcepiimt vprksdlfqd dlypdtpgpe paleadewls gqdaepvlis lrdgyvppkh
      361 relrvtkrni ldvrppsgpr rsqsasdapl sqhtletlle eikalrervq aqeqritale
      421 nmlcelvdgt d
//
LOCUS       NP_085053                127 aa            linear   PRI 11-DEC-2025
DEFINITION  LIM domain-containing protein 2 [Homo sapiens].
ACCESSION   NP_085053
VERSION     NP_085053.1
DBSOURCE    REFSEQ: accession NM_030576.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Tao,P., Chen,X., Xu,L., Chen,J., Nie,Q., Xu,M. and Feng,J.
  TITLE     LIMD2 is the Signature of Cell Aging-immune/Inflammation in Acute
            Myocardial Infarction
  JOURNAL   Curr Med Chem 31 (17), 2400-2413 (2024)
   PUBMED   37936458
  REMARK    GeneRIF: LIMD2 is the Signature of Cell Aging-immune/Inflammation
            in Acute Myocardial Infarction.
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Chen,L., Qian,J., You,Q. and Ma,J.
  TITLE     LIM domain-containing 2 (LIMD2) promotes the progress of ovarian
            cancer via the focal adhesion signaling pathway
  JOURNAL   Bioengineered 12 (2), 10089-10100 (2021)
   PUBMED   34724866
  REMARK    GeneRIF: LIM domain-containing 2 (LIMD2) promotes the progress of
            ovarian cancer via the focal adhesion signaling pathway.
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Wang,F., Li,Z., Xu,L., Li,Y., Li,Y., Zhang,X., Wang,Y. and Liu,D.
  TITLE     LIMD2 targeted by miR-34a promotes the proliferation and invasion
            of non-small cell lung cancer cells
  JOURNAL   Mol Med Rep 18 (5), 4760-4766 (2018)
   PUBMED   30221696
  REMARK    GeneRIF: the results of the present study revealed that LIMD2
            promoted nonsmall cell lung cancer (NSCLC)progression and was
            regulated by miR34a.
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Pinheiro Dos Santos,M.J.C., Bastos,A.U., da Costa,V.R., Delcelo,R.,
            Lindsey,S.C., Colozza-Gama,G.A., Peng,H., Rauscher,F.J. 3rd,
            Oler,G. and Cerutti,J.M.
  TITLE     LIMD2 Is Overexpressed in BRAF V600E-Positive Papillary Thyroid
            Carcinomas and Matched Lymph Node Metastases
  JOURNAL   Endocr Pathol 29 (3), 222-230 (2018)
   PUBMED   29560564
  REMARK    GeneRIF: Our data suggest that LIMD2 may play an important role in
            the metastatic process of papillary thyroid carcinoma
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Peng,H., Talebzadeh-Farrooji,M., Osborne,M.J., Prokop,J.W.,
            McDonald,P.C., Karar,J., Hou,Z., He,M., Kebebew,E., Orntoft,T.,
            Herlyn,M., Caton,A.J., Fredericks,W., Malkowicz,B., Paterno,C.S.,
            Carolin,A.S., Speicher,D.W., Skordalakes,E., Huang,Q., Dedhar,S.,
            Borden,K.L.B. and Rauscher,F.J. 3rd.
  TITLE     LIMD2 is a small LIM-only protein overexpressed in metastatic
            lesions that regulates cell motility and tumor progression by
            directly binding to and activating the integrin-linked kinase
  JOURNAL   Cancer Res 74 (5), 1390-1403 (2014)
   PUBMED   24590809
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   7  (residues 1 to 127)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   8  (residues 1 to 127)
  AUTHORS   Fu,G.K., Wang,J.T., Yang,J., Au-Young,J. and Stuve,L.L.
  TITLE     Circular rapid amplification of cDNA ends for high-throughput
            extension cloning of partial genes
  JOURNAL   Genomics 84 (1), 205-210 (2004)
   PUBMED   15203218
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK092301.1, CD632650.1, AA251318.1 and AC046185.14.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK092301.1, BC004400.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000259006.8/ ENSP00000259006.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.3"
     Protein         1..127
                     /product="LIM domain-containing protein 2"
                     /note="testicular tissue protein Li 106"
                     /calculated_mol_wt=13939
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BT23.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9BT23.1)"
     Region          40..92
                     /region_name="LIM_Eplin_like_1"
                     /note="a LIM domain subfamily on a group of proteins with
                     unknown function; cd09486"
                     /db_xref="CDD:188870"
     Site            order(40,43,61,64,67,70,88,91)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188870"
     CDS             1..127
                     /gene="LIMD2"
                     /coded_by="NM_030576.4:145..528"
                     /db_xref="CCDS:CCDS11641.1"
                     /db_xref="GeneID:80774"
                     /db_xref="HGNC:HGNC:28142"
                     /db_xref="MIM:621443"
ORIGIN      
        1 mfqaagaaqa tpshdakggg sstvqrsksf slraqvketc aacqktvypm erlvadklif
       61 hnscfcckhc htklslgsya alhgefyckp hfqqlfkskg nydegfgrkq hkelwahkev
      121 dpgtkta
//
LOCUS       NP_001375363             471 aa            linear   PRI 11-DEC-2025
DEFINITION  coronin-6 isoform 3 [Homo sapiens].
ACCESSION   NP_001375363
VERSION     NP_001375363.1
DBSOURCE    REFSEQ: accession NM_001388434.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Cardinali,B., Cappella,M., Provenzano,C., Garcia-Manteiga,J.M.,
            Lazarevic,D., Cittaro,D., Martelli,F. and Falcone,G.
  TITLE     MicroRNA-222 regulates muscle alternative splicing through Rbm24
            during differentiation of skeletal muscle cells
  JOURNAL   Cell Death Dis 7 (2), e2086 (2016)
   PUBMED   26844700
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Morris,M.R., Ricketts,C.J., Gentle,D., McRonald,F., Carli,N.,
            Khalili,H., Brown,M., Kishida,T., Yao,M., Banks,R.E., Clarke,N.,
            Latif,F. and Maher,E.R.
  TITLE     Genome-wide methylation analysis identifies epigenetically
            inactivated candidate tumour suppressor genes in renal cell
            carcinoma
  JOURNAL   Oncogene 30 (12), 1390-1401 (2011)
   PUBMED   21132003
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Zody,M.C., Garber,M., Adams,D.J., Sharpe,T., Harrow,J.,
            Lupski,J.R., Nicholson,C., Searle,S.M., Wilming,L., Young,S.K.,
            Abouelleil,A., Allen,N.R., Bi,W., Bloom,T., Borowsky,M.L.,
            Bugalter,B.E., Butler,J., Chang,J.L., Chen,C.K., Cook,A., Corum,B.,
            Cuomo,C.A., de Jong,P.J., DeCaprio,D., Dewar,K., FitzGerald,M.,
            Gilbert,J., Gibson,R., Gnerre,S., Goldstein,S., Grafham,D.V.,
            Grocock,R., Hafez,N., Hagopian,D.S., Hart,E., Norman,C.H.,
            Humphray,S., Jaffe,D.B., Jones,M., Kamal,M., Khodiyar,V.K.,
            LaButti,K., Laird,G., Lehoczky,J., Liu,X., Lokyitsang,T.,
            Loveland,J., Lui,A., Macdonald,P., Major,J.E., Matthews,L.,
            Mauceli,E., McCarroll,S.A., Mihalev,A.H., Mudge,J., Nguyen,C.,
            Nicol,R., O'Leary,S.B., Osoegawa,K., Schwartz,D.C., Shaw-Smith,C.,
            Stankiewicz,P., Steward,C., Swarbreck,D., Venkataraman,V.,
            Whittaker,C.A., Yang,X., Zimmer,A.R., Bradley,A., Hubbard,T.,
            Birren,B.W., Rogers,J., Lander,E.S. and Nusbaum,C.
  TITLE     DNA sequence of human chromosome 17 and analysis of rearrangement
            in the human lineage
  JOURNAL   Nature 440 (7087), 1045-1049 (2006)
   PUBMED   16625196
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104564.11.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138518.54748.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..471
                     /product="coronin-6 isoform 3"
                     /note="coronin, actin binding protein 6; clipin-E;
                     coronin-like protein E"
                     /calculated_mol_wt=52729
     Region          9..465
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          37..79
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          85..129
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          134..171
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          179..215
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          222..262
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          269..310
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..471
                     /gene="CORO6"
                     /gene_synonym="ClipinE"
                     /coded_by="NM_001388434.1:289..1704"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="GeneID:84940"
                     /db_xref="HGNC:HGNC:21356"
                     /db_xref="MIM:621442"
ORIGIN      
        1 msrrvvrqsk frhvfgqaak adqayedirv skvtwdssfc avnpkflaii veaggggafi
       61 vlplaktgrv dknyplvtgh tapvldidwc phndnviasa sddttimvwq ipdytpmrni
      121 tepiitlegh skrvgilswh ptarnvllsa ggdnviiiwn vgtgevllsl ddmhpdvihs
      181 vcwnsngsll attckdktlr iidprkgqvv aerfaahegm rpmravftrq ghifttgftr
      241 msqrelglwd pnnfeepval qemdtsngvl lpfydpdssi vylcgkgdss iryfeitdep
      301 pfvhylntfs skepqrgmgf mpkrgldvsk ceiarfyklh erkcepiimt vprksdlfqd
      361 dlypdtpgpe paleadewls gqdaepvlis lrdgyvppkh relrvtkrni ldvrppsgpr
      421 rsqsasdapl sqhtletlle eikalrervq aqeqritale nmlcelvdgt d
//
LOCUS       NP_689556                384 aa            linear   PRI 11-DEC-2025
DEFINITION  spermatogenesis-associated protein 32 [Homo sapiens].
ACCESSION   NP_689556
VERSION     NP_689556.2
DBSOURCE    REFSEQ: accession NM_152343.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 384)
  AUTHORS   Casabonne,D., Reina,O., Benavente,Y., Becker,N., Maynadie,M.,
            Foretova,L., Cocco,P., Gonzalez-Neira,A., Nieters,A., Boffetta,P.,
            Middeldorp,J.M. and de Sanjose,S.
  TITLE     Single nucleotide polymorphisms of matrix metalloproteinase 9
            (MMP9) and tumor protein 73 (TP73) interact with Epstein-Barr virus
            in chronic lymphocytic leukemia: results from the European
            case-control study EpiLymph
  JOURNAL   Haematologica 96 (2), 323-327 (2011)
   PUBMED   21048031
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   3  (residues 1 to 384)
  AUTHORS   Lee,K.F., Tam,Y.T., Zuo,Y., Cheong,A.W., Pang,R.T., Lee,N.P.,
            Shum,C.K., Tam,P.C., Cheung,A.N., Yang,Z.M., Yeung,W.S. and
            Luk,J.M.
  TITLE     Characterization of an acrosome protein VAD1.2/AEP2 which is
            differentially expressed in spermatogenesis
  JOURNAL   Mol Hum Reprod 14 (8), 465-474 (2008)
   PUBMED   18621766
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP369808.1, BP370574.1 and BC028124.1.
            
            On Jun 22, 2007 this sequence version replaced NP_689556.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028124.1, AK058143.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA2144333 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331780.5/ ENSP00000331532.4
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..384
                     /product="spermatogenesis-associated protein 32"
                     /note="testis-expressed sequence 34 protein; testis
                     expressed 34; acrosome expressed 2; CTD-2020K17.4;
                     testis-expressed protein 34"
                     /calculated_mol_wt=42194
     Region          23..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LK8.3)"
     Region          138..384
                     /region_name="VAD1-2"
                     /note="Vitamin A-deficiency (VAD) rat model signalling;
                     pfam15310"
                     /db_xref="CDD:464635"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q66H17; propagated from
                     UniProtKB/Swiss-Prot (Q96LK8.3)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q66H17; propagated from
                     UniProtKB/Swiss-Prot (Q96LK8.3)"
     Region          211..232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LK8.3)"
     Region          284..310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LK8.3)"
     Region          340..366
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LK8.3)"
     CDS             1..384
                     /gene="SPATA32"
                     /gene_synonym="AEP2; C17orf46; TEX34; VAD1.2"
                     /coded_by="NM_152343.3:79..1233"
                     /db_xref="CCDS:CCDS32669.1"
                     /db_xref="GeneID:124783"
                     /db_xref="HGNC:HGNC:26349"
                     /db_xref="MIM:621441"
ORIGIN      
        1 mgvtgahgfp ccgkgsveva emrddlsqhq iqeeqelead mleqkpqlqv dldldpdpdp
       61 dpeleigqvp alleselypa lkleaeldte ansneesdfe epmqlvckie svhsnmglpt
      121 pqtfrpwsln sncrsfteen hvsachhsis aqtskhlfwa nkliqasehs lqrainmqln
      181 ngsagqpirs plreaiptna lcseeqlqip dahsapptts sqapspllss dlpppidlte
      241 litfasslam asssrmdlps lehmmkappq ealepstepl lttveerepe nhaetlpekp
      301 rearaplksw sqedknfaqs yfdfskpgik ratikgqiql lqppatspll qgskedsvpp
      361 gkekenpllv kihfklsapt ipek
//
LOCUS       NP_001338230             237 aa            linear   PRI 11-DEC-2025
DEFINITION  coronin-6 isoform 2 [Homo sapiens].
ACCESSION   NP_001338230
VERSION     NP_001338230.1
DBSOURCE    REFSEQ: accession NM_001351301.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Cardinali,B., Cappella,M., Provenzano,C., Garcia-Manteiga,J.M.,
            Lazarevic,D., Cittaro,D., Martelli,F. and Falcone,G.
  TITLE     MicroRNA-222 regulates muscle alternative splicing through Rbm24
            during differentiation of skeletal muscle cells
  JOURNAL   Cell Death Dis 7 (2), e2086 (2016)
   PUBMED   26844700
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Morris,M.R., Ricketts,C.J., Gentle,D., McRonald,F., Carli,N.,
            Khalili,H., Brown,M., Kishida,T., Yao,M., Banks,R.E., Clarke,N.,
            Latif,F. and Maher,E.R.
  TITLE     Genome-wide methylation analysis identifies epigenetically
            inactivated candidate tumour suppressor genes in renal cell
            carcinoma
  JOURNAL   Oncogene 30 (12), 1390-1401 (2011)
   PUBMED   21132003
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Zody,M.C., Garber,M., Adams,D.J., Sharpe,T., Harrow,J.,
            Lupski,J.R., Nicholson,C., Searle,S.M., Wilming,L., Young,S.K.,
            Abouelleil,A., Allen,N.R., Bi,W., Bloom,T., Borowsky,M.L.,
            Bugalter,B.E., Butler,J., Chang,J.L., Chen,C.K., Cook,A., Corum,B.,
            Cuomo,C.A., de Jong,P.J., DeCaprio,D., Dewar,K., FitzGerald,M.,
            Gilbert,J., Gibson,R., Gnerre,S., Goldstein,S., Grafham,D.V.,
            Grocock,R., Hafez,N., Hagopian,D.S., Hart,E., Norman,C.H.,
            Humphray,S., Jaffe,D.B., Jones,M., Kamal,M., Khodiyar,V.K.,
            LaButti,K., Laird,G., Lehoczky,J., Liu,X., Lokyitsang,T.,
            Loveland,J., Lui,A., Macdonald,P., Major,J.E., Matthews,L.,
            Mauceli,E., McCarroll,S.A., Mihalev,A.H., Mudge,J., Nguyen,C.,
            Nicol,R., O'Leary,S.B., Osoegawa,K., Schwartz,D.C., Shaw-Smith,C.,
            Stankiewicz,P., Steward,C., Swarbreck,D., Venkataraman,V.,
            Whittaker,C.A., Yang,X., Zimmer,A.R., Bradley,A., Hubbard,T.,
            Birren,B.W., Rogers,J., Lander,E.S. and Nusbaum,C.
  TITLE     DNA sequence of human chromosome 17 and analysis of rearrangement
            in the human lineage
  JOURNAL   Nature 440 (7087), 1045-1049 (2006)
   PUBMED   16625196
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104564.11.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064514.1, BE560100.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..237
                     /product="coronin-6 isoform 2"
                     /note="coronin, actin binding protein 6; clipin-E;
                     coronin-like protein E"
                     /calculated_mol_wt=26752
     Region          <21..231
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     CDS             1..237
                     /gene="CORO6"
                     /gene_synonym="ClipinE"
                     /coded_by="NM_001351301.3:116..829"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:84940"
                     /db_xref="HGNC:HGNC:21356"
                     /db_xref="MIM:621442"
ORIGIN      
        1 mpspwgwfav tacgaqrnnf eepvalqemd tsngvllpfy dpdssivylc gkgdssiryf
       61 eitdeppfvh ylntfsskep qrgmgfmpkr gldvskceia rfyklherkc epiimtvprk
      121 sdlfqddlyp dtpgpepale adewlsgqda epvlislrdg yvppkhrelr vtkrnildvr
      181 ppsgprrsqs asdaplsqht letlleeika lrervqaqeq ritalenmlc elvdgtd
//
LOCUS       NP_001375367             397 aa            linear   PRI 11-DEC-2025
DEFINITION  coronin-6 isoform 7 [Homo sapiens].
ACCESSION   NP_001375367
VERSION     NP_001375367.1
DBSOURCE    REFSEQ: accession NM_001388438.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Cardinali,B., Cappella,M., Provenzano,C., Garcia-Manteiga,J.M.,
            Lazarevic,D., Cittaro,D., Martelli,F. and Falcone,G.
  TITLE     MicroRNA-222 regulates muscle alternative splicing through Rbm24
            during differentiation of skeletal muscle cells
  JOURNAL   Cell Death Dis 7 (2), e2086 (2016)
   PUBMED   26844700
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Morris,M.R., Ricketts,C.J., Gentle,D., McRonald,F., Carli,N.,
            Khalili,H., Brown,M., Kishida,T., Yao,M., Banks,R.E., Clarke,N.,
            Latif,F. and Maher,E.R.
  TITLE     Genome-wide methylation analysis identifies epigenetically
            inactivated candidate tumour suppressor genes in renal cell
            carcinoma
  JOURNAL   Oncogene 30 (12), 1390-1401 (2011)
   PUBMED   21132003
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Zody,M.C., Garber,M., Adams,D.J., Sharpe,T., Harrow,J.,
            Lupski,J.R., Nicholson,C., Searle,S.M., Wilming,L., Young,S.K.,
            Abouelleil,A., Allen,N.R., Bi,W., Bloom,T., Borowsky,M.L.,
            Bugalter,B.E., Butler,J., Chang,J.L., Chen,C.K., Cook,A., Corum,B.,
            Cuomo,C.A., de Jong,P.J., DeCaprio,D., Dewar,K., FitzGerald,M.,
            Gilbert,J., Gibson,R., Gnerre,S., Goldstein,S., Grafham,D.V.,
            Grocock,R., Hafez,N., Hagopian,D.S., Hart,E., Norman,C.H.,
            Humphray,S., Jaffe,D.B., Jones,M., Kamal,M., Khodiyar,V.K.,
            LaButti,K., Laird,G., Lehoczky,J., Liu,X., Lokyitsang,T.,
            Loveland,J., Lui,A., Macdonald,P., Major,J.E., Matthews,L.,
            Mauceli,E., McCarroll,S.A., Mihalev,A.H., Mudge,J., Nguyen,C.,
            Nicol,R., O'Leary,S.B., Osoegawa,K., Schwartz,D.C., Shaw-Smith,C.,
            Stankiewicz,P., Steward,C., Swarbreck,D., Venkataraman,V.,
            Whittaker,C.A., Yang,X., Zimmer,A.R., Bradley,A., Hubbard,T.,
            Birren,B.W., Rogers,J., Lander,E.S. and Nusbaum,C.
  TITLE     DNA sequence of human chromosome 17 and analysis of rearrangement
            in the human lineage
  JOURNAL   Nature 440 (7087), 1045-1049 (2006)
   PUBMED   16625196
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104564.11.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..397
                     /product="coronin-6 isoform 7"
                     /note="coronin, actin binding protein 6; clipin-E;
                     coronin-like protein E"
                     /calculated_mol_wt=44265
     Region          9..379
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          37..79
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          85..129
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          134..171
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          179..211
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..397
                     /gene="CORO6"
                     /gene_synonym="ClipinE"
                     /coded_by="NM_001388438.1:289..1482"
                     /note="isoform 7 is encoded by transcript variant 10"
                     /db_xref="GeneID:84940"
                     /db_xref="HGNC:HGNC:21356"
                     /db_xref="MIM:621442"
ORIGIN      
        1 msrrvvrqsk frhvfgqaak adqayedirv skvtwdssfc avnpkflaii veaggggafi
       61 vlplaktgrv dknyplvtgh tapvldidwc phndnviasa sddttimvwq ipdytpmrni
      121 tepiitlegh skrvgilswh ptarnvllsa ggdnviiiwn vgtgevllsl ddmhpdvihs
      181 vcwnsngsll attckdktlr iidprkgqvv agdssiryfe itdeppfvhy lntfsskepq
      241 rgmgfmpkrg ldvskceiar fyklherkce piimtvprks dlfqddlypd tpgpepalea
      301 dewlsgqdae pvlislrdgy vppkhrelrv tkrnildvrp psgprrsqsa sdaplsqqht
      361 letlleeika lrervqaqeq ritalenmlc elvdgtd
//
LOCUS       NP_116243                472 aa            linear   PRI 11-DEC-2025
DEFINITION  coronin-6 isoform 1 [Homo sapiens].
ACCESSION   NP_116243 XP_005258104
VERSION     NP_116243.2
DBSOURCE    REFSEQ: accession NM_032854.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Cardinali,B., Cappella,M., Provenzano,C., Garcia-Manteiga,J.M.,
            Lazarevic,D., Cittaro,D., Martelli,F. and Falcone,G.
  TITLE     MicroRNA-222 regulates muscle alternative splicing through Rbm24
            during differentiation of skeletal muscle cells
  JOURNAL   Cell Death Dis 7 (2), e2086 (2016)
   PUBMED   26844700
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Morris,M.R., Ricketts,C.J., Gentle,D., McRonald,F., Carli,N.,
            Khalili,H., Brown,M., Kishida,T., Yao,M., Banks,R.E., Clarke,N.,
            Latif,F. and Maher,E.R.
  TITLE     Genome-wide methylation analysis identifies epigenetically
            inactivated candidate tumour suppressor genes in renal cell
            carcinoma
  JOURNAL   Oncogene 30 (12), 1390-1401 (2011)
   PUBMED   21132003
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Zody,M.C., Garber,M., Adams,D.J., Sharpe,T., Harrow,J.,
            Lupski,J.R., Nicholson,C., Searle,S.M., Wilming,L., Young,S.K.,
            Abouelleil,A., Allen,N.R., Bi,W., Bloom,T., Borowsky,M.L.,
            Bugalter,B.E., Butler,J., Chang,J.L., Chen,C.K., Cook,A., Corum,B.,
            Cuomo,C.A., de Jong,P.J., DeCaprio,D., Dewar,K., FitzGerald,M.,
            Gilbert,J., Gibson,R., Gnerre,S., Goldstein,S., Grafham,D.V.,
            Grocock,R., Hafez,N., Hagopian,D.S., Hart,E., Norman,C.H.,
            Humphray,S., Jaffe,D.B., Jones,M., Kamal,M., Khodiyar,V.K.,
            LaButti,K., Laird,G., Lehoczky,J., Liu,X., Lokyitsang,T.,
            Loveland,J., Lui,A., Macdonald,P., Major,J.E., Matthews,L.,
            Mauceli,E., McCarroll,S.A., Mihalev,A.H., Mudge,J., Nguyen,C.,
            Nicol,R., O'Leary,S.B., Osoegawa,K., Schwartz,D.C., Shaw-Smith,C.,
            Stankiewicz,P., Steward,C., Swarbreck,D., Venkataraman,V.,
            Whittaker,C.A., Yang,X., Zimmer,A.R., Bradley,A., Hubbard,T.,
            Birren,B.W., Rogers,J., Lander,E.S. and Nusbaum,C.
  TITLE     DNA sequence of human chromosome 17 and analysis of rearrangement
            in the human lineage
  JOURNAL   Nature 440 (7087), 1045-1049 (2006)
   PUBMED   16625196
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104564.11.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Oct 30, 2020 this sequence version replaced
            XP_005258104.1, NP_116243.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138525.2512.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000388767.8/ ENSP00000373419.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..472
                     /product="coronin-6 isoform 1"
                     /note="coronin, actin binding protein 6; clipin-E;
                     coronin-like protein E"
                     /calculated_mol_wt=52857
     Region          9..454
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          37..79
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          85..129
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          134..171
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          179..215
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          222..262
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          269..310
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..472
                     /gene="CORO6"
                     /gene_synonym="ClipinE"
                     /coded_by="NM_032854.4:289..1707"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11252.2"
                     /db_xref="GeneID:84940"
                     /db_xref="HGNC:HGNC:21356"
                     /db_xref="MIM:621442"
ORIGIN      
        1 msrrvvrqsk frhvfgqaak adqayedirv skvtwdssfc avnpkflaii veaggggafi
       61 vlplaktgrv dknyplvtgh tapvldidwc phndnviasa sddttimvwq ipdytpmrni
      121 tepiitlegh skrvgilswh ptarnvllsa ggdnviiiwn vgtgevllsl ddmhpdvihs
      181 vcwnsngsll attckdktlr iidprkgqvv aerfaahegm rpmravftrq ghifttgftr
      241 msqrelglwd pnnfeepval qemdtsngvl lpfydpdssi vylcgkgdss iryfeitdep
      301 pfvhylntfs skepqrgmgf mpkrgldvsk ceiarfyklh erkcepiimt vprksdlfqd
      361 dlypdtpgpe paleadewls gqdaepvlis lrdgyvppkh relrvtkrni ldvrppsgpr
      421 rsqsasdapl sqqhtletll eeikalrerv qaqeqrital enmlcelvdg td
//
LOCUS       NP_001375366             430 aa            linear   PRI 11-DEC-2025
DEFINITION  coronin-6 isoform 6 [Homo sapiens].
ACCESSION   NP_001375366
VERSION     NP_001375366.1
DBSOURCE    REFSEQ: accession NM_001388437.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Cardinali,B., Cappella,M., Provenzano,C., Garcia-Manteiga,J.M.,
            Lazarevic,D., Cittaro,D., Martelli,F. and Falcone,G.
  TITLE     MicroRNA-222 regulates muscle alternative splicing through Rbm24
            during differentiation of skeletal muscle cells
  JOURNAL   Cell Death Dis 7 (2), e2086 (2016)
   PUBMED   26844700
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Morris,M.R., Ricketts,C.J., Gentle,D., McRonald,F., Carli,N.,
            Khalili,H., Brown,M., Kishida,T., Yao,M., Banks,R.E., Clarke,N.,
            Latif,F. and Maher,E.R.
  TITLE     Genome-wide methylation analysis identifies epigenetically
            inactivated candidate tumour suppressor genes in renal cell
            carcinoma
  JOURNAL   Oncogene 30 (12), 1390-1401 (2011)
   PUBMED   21132003
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Zody,M.C., Garber,M., Adams,D.J., Sharpe,T., Harrow,J.,
            Lupski,J.R., Nicholson,C., Searle,S.M., Wilming,L., Young,S.K.,
            Abouelleil,A., Allen,N.R., Bi,W., Bloom,T., Borowsky,M.L.,
            Bugalter,B.E., Butler,J., Chang,J.L., Chen,C.K., Cook,A., Corum,B.,
            Cuomo,C.A., de Jong,P.J., DeCaprio,D., Dewar,K., FitzGerald,M.,
            Gilbert,J., Gibson,R., Gnerre,S., Goldstein,S., Grafham,D.V.,
            Grocock,R., Hafez,N., Hagopian,D.S., Hart,E., Norman,C.H.,
            Humphray,S., Jaffe,D.B., Jones,M., Kamal,M., Khodiyar,V.K.,
            LaButti,K., Laird,G., Lehoczky,J., Liu,X., Lokyitsang,T.,
            Loveland,J., Lui,A., Macdonald,P., Major,J.E., Matthews,L.,
            Mauceli,E., McCarroll,S.A., Mihalev,A.H., Mudge,J., Nguyen,C.,
            Nicol,R., O'Leary,S.B., Osoegawa,K., Schwartz,D.C., Shaw-Smith,C.,
            Stankiewicz,P., Steward,C., Swarbreck,D., Venkataraman,V.,
            Whittaker,C.A., Yang,X., Zimmer,A.R., Bradley,A., Hubbard,T.,
            Birren,B.W., Rogers,J., Lander,E.S. and Nusbaum,C.
  TITLE     DNA sequence of human chromosome 17 and analysis of rearrangement
            in the human lineage
  JOURNAL   Nature 440 (7087), 1045-1049 (2006)
   PUBMED   16625196
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104564.11.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.383898.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..430
                     /product="coronin-6 isoform 6"
                     /note="coronin, actin binding protein 6; clipin-E;
                     coronin-like protein E"
                     /calculated_mol_wt=48293
     Region          9..424
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          31..88
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          93..130
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          138..174
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          181..221
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          228..269
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..430
                     /gene="CORO6"
                     /gene_synonym="ClipinE"
                     /coded_by="NM_001388437.1:228..1520"
                     /note="isoform 6 is encoded by transcript variant 9"
                     /db_xref="GeneID:84940"
                     /db_xref="HGNC:HGNC:21356"
                     /db_xref="MIM:621442"
ORIGIN      
        1 msrrvvrqsk frhvfgqaak adqayedirv skvtwdssfc avnpkflaii veaggggafi
       61 vlplakvwqi pdytpmrnit epiitleghs krvgilswhp tarnvllsag gdnviiiwnv
      121 gtgevllsld dmhpdvihsv cwnsngslla ttckdktlri idprkgqvva erfaahegmr
      181 pmravftrqg hifttgftrm sqrelglwdp nnfeepvalq emdtsngvll pfydpdssiv
      241 ylcgkgdssi ryfeitdepp fvhylntfss kepqrgmgfm pkrgldvskc eiarfyklhe
      301 rkcepiimtv prksdlfqdd lypdtpgpep aleadewlsg qdaepvlisl rdgyvppkhr
      361 elrvtkrnil dvrppsgprr sqsasdapls qhtletllee ikalrervqa qeqritalen
      421 mlcelvdgtd
//
LOCUS       NP_001375362             471 aa            linear   PRI 11-DEC-2025
DEFINITION  coronin-6 isoform 3 [Homo sapiens].
ACCESSION   NP_001375362
VERSION     NP_001375362.1
DBSOURCE    REFSEQ: accession NM_001388433.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Cardinali,B., Cappella,M., Provenzano,C., Garcia-Manteiga,J.M.,
            Lazarevic,D., Cittaro,D., Martelli,F. and Falcone,G.
  TITLE     MicroRNA-222 regulates muscle alternative splicing through Rbm24
            during differentiation of skeletal muscle cells
  JOURNAL   Cell Death Dis 7 (2), e2086 (2016)
   PUBMED   26844700
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Morris,M.R., Ricketts,C.J., Gentle,D., McRonald,F., Carli,N.,
            Khalili,H., Brown,M., Kishida,T., Yao,M., Banks,R.E., Clarke,N.,
            Latif,F. and Maher,E.R.
  TITLE     Genome-wide methylation analysis identifies epigenetically
            inactivated candidate tumour suppressor genes in renal cell
            carcinoma
  JOURNAL   Oncogene 30 (12), 1390-1401 (2011)
   PUBMED   21132003
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Zody,M.C., Garber,M., Adams,D.J., Sharpe,T., Harrow,J.,
            Lupski,J.R., Nicholson,C., Searle,S.M., Wilming,L., Young,S.K.,
            Abouelleil,A., Allen,N.R., Bi,W., Bloom,T., Borowsky,M.L.,
            Bugalter,B.E., Butler,J., Chang,J.L., Chen,C.K., Cook,A., Corum,B.,
            Cuomo,C.A., de Jong,P.J., DeCaprio,D., Dewar,K., FitzGerald,M.,
            Gilbert,J., Gibson,R., Gnerre,S., Goldstein,S., Grafham,D.V.,
            Grocock,R., Hafez,N., Hagopian,D.S., Hart,E., Norman,C.H.,
            Humphray,S., Jaffe,D.B., Jones,M., Kamal,M., Khodiyar,V.K.,
            LaButti,K., Laird,G., Lehoczky,J., Liu,X., Lokyitsang,T.,
            Loveland,J., Lui,A., Macdonald,P., Major,J.E., Matthews,L.,
            Mauceli,E., McCarroll,S.A., Mihalev,A.H., Mudge,J., Nguyen,C.,
            Nicol,R., O'Leary,S.B., Osoegawa,K., Schwartz,D.C., Shaw-Smith,C.,
            Stankiewicz,P., Steward,C., Swarbreck,D., Venkataraman,V.,
            Whittaker,C.A., Yang,X., Zimmer,A.R., Bradley,A., Hubbard,T.,
            Birren,B.W., Rogers,J., Lander,E.S. and Nusbaum,C.
  TITLE     DNA sequence of human chromosome 17 and analysis of rearrangement
            in the human lineage
  JOURNAL   Nature 440 (7087), 1045-1049 (2006)
   PUBMED   16625196
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104564.11.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138518.6004.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..471
                     /product="coronin-6 isoform 3"
                     /note="coronin, actin binding protein 6; clipin-E;
                     coronin-like protein E"
                     /calculated_mol_wt=52729
     Region          9..465
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          37..79
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          85..129
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          134..171
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          179..215
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          222..262
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          269..310
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..471
                     /gene="CORO6"
                     /gene_synonym="ClipinE"
                     /coded_by="NM_001388433.1:228..1643"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:84940"
                     /db_xref="HGNC:HGNC:21356"
                     /db_xref="MIM:621442"
ORIGIN      
        1 msrrvvrqsk frhvfgqaak adqayedirv skvtwdssfc avnpkflaii veaggggafi
       61 vlplaktgrv dknyplvtgh tapvldidwc phndnviasa sddttimvwq ipdytpmrni
      121 tepiitlegh skrvgilswh ptarnvllsa ggdnviiiwn vgtgevllsl ddmhpdvihs
      181 vcwnsngsll attckdktlr iidprkgqvv aerfaahegm rpmravftrq ghifttgftr
      241 msqrelglwd pnnfeepval qemdtsngvl lpfydpdssi vylcgkgdss iryfeitdep
      301 pfvhylntfs skepqrgmgf mpkrgldvsk ceiarfyklh erkcepiimt vprksdlfqd
      361 dlypdtpgpe paleadewls gqdaepvlis lrdgyvppkh relrvtkrni ldvrppsgpr
      421 rsqsasdapl sqhtletlle eikalrervq aqeqritale nmlcelvdgt d
//
LOCUS       NP_001375364             431 aa            linear   PRI 11-DEC-2025
DEFINITION  coronin-6 isoform 4 [Homo sapiens].
ACCESSION   NP_001375364 XP_016880724
VERSION     NP_001375364.1
DBSOURCE    REFSEQ: accession NM_001388435.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Cardinali,B., Cappella,M., Provenzano,C., Garcia-Manteiga,J.M.,
            Lazarevic,D., Cittaro,D., Martelli,F. and Falcone,G.
  TITLE     MicroRNA-222 regulates muscle alternative splicing through Rbm24
            during differentiation of skeletal muscle cells
  JOURNAL   Cell Death Dis 7 (2), e2086 (2016)
   PUBMED   26844700
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Morris,M.R., Ricketts,C.J., Gentle,D., McRonald,F., Carli,N.,
            Khalili,H., Brown,M., Kishida,T., Yao,M., Banks,R.E., Clarke,N.,
            Latif,F. and Maher,E.R.
  TITLE     Genome-wide methylation analysis identifies epigenetically
            inactivated candidate tumour suppressor genes in renal cell
            carcinoma
  JOURNAL   Oncogene 30 (12), 1390-1401 (2011)
   PUBMED   21132003
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Zody,M.C., Garber,M., Adams,D.J., Sharpe,T., Harrow,J.,
            Lupski,J.R., Nicholson,C., Searle,S.M., Wilming,L., Young,S.K.,
            Abouelleil,A., Allen,N.R., Bi,W., Bloom,T., Borowsky,M.L.,
            Bugalter,B.E., Butler,J., Chang,J.L., Chen,C.K., Cook,A., Corum,B.,
            Cuomo,C.A., de Jong,P.J., DeCaprio,D., Dewar,K., FitzGerald,M.,
            Gilbert,J., Gibson,R., Gnerre,S., Goldstein,S., Grafham,D.V.,
            Grocock,R., Hafez,N., Hagopian,D.S., Hart,E., Norman,C.H.,
            Humphray,S., Jaffe,D.B., Jones,M., Kamal,M., Khodiyar,V.K.,
            LaButti,K., Laird,G., Lehoczky,J., Liu,X., Lokyitsang,T.,
            Loveland,J., Lui,A., Macdonald,P., Major,J.E., Matthews,L.,
            Mauceli,E., McCarroll,S.A., Mihalev,A.H., Mudge,J., Nguyen,C.,
            Nicol,R., O'Leary,S.B., Osoegawa,K., Schwartz,D.C., Shaw-Smith,C.,
            Stankiewicz,P., Steward,C., Swarbreck,D., Venkataraman,V.,
            Whittaker,C.A., Yang,X., Zimmer,A.R., Bradley,A., Hubbard,T.,
            Birren,B.W., Rogers,J., Lander,E.S. and Nusbaum,C.
  TITLE     DNA sequence of human chromosome 17 and analysis of rearrangement
            in the human lineage
  JOURNAL   Nature 440 (7087), 1045-1049 (2006)
   PUBMED   16625196
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104564.11.
            
            On Oct 30, 2020 this sequence version replaced XP_016880724.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138518.292115.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..431
                     /product="coronin-6 isoform 4"
                     /note="coronin, actin binding protein 6; clipin-E;
                     coronin-like protein E"
                     /calculated_mol_wt=48422
     Region          9..413
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          31..88
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          93..130
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          138..174
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          181..221
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          228..269
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..431
                     /gene="CORO6"
                     /gene_synonym="ClipinE"
                     /coded_by="NM_001388435.1:289..1584"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:84940"
                     /db_xref="HGNC:HGNC:21356"
                     /db_xref="MIM:621442"
ORIGIN      
        1 msrrvvrqsk frhvfgqaak adqayedirv skvtwdssfc avnpkflaii veaggggafi
       61 vlplakvwqi pdytpmrnit epiitleghs krvgilswhp tarnvllsag gdnviiiwnv
      121 gtgevllsld dmhpdvihsv cwnsngslla ttckdktlri idprkgqvva erfaahegmr
      181 pmravftrqg hifttgftrm sqrelglwdp nnfeepvalq emdtsngvll pfydpdssiv
      241 ylcgkgdssi ryfeitdepp fvhylntfss kepqrgmgfm pkrgldvskc eiarfyklhe
      301 rkcepiimtv prksdlfqdd lypdtpgpep aleadewlsg qdaepvlisl rdgyvppkhr
      361 elrvtkrnil dvrppsgprr sqsasdapls qqhtletlle eikalrervq aqeqritale
      421 nmlcelvdgt d
//
LOCUS       NP_001375360             472 aa            linear   PRI 11-DEC-2025
DEFINITION  coronin-6 isoform 1 [Homo sapiens].
ACCESSION   NP_001375360
VERSION     NP_001375360.1
DBSOURCE    REFSEQ: accession NM_001388431.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Cardinali,B., Cappella,M., Provenzano,C., Garcia-Manteiga,J.M.,
            Lazarevic,D., Cittaro,D., Martelli,F. and Falcone,G.
  TITLE     MicroRNA-222 regulates muscle alternative splicing through Rbm24
            during differentiation of skeletal muscle cells
  JOURNAL   Cell Death Dis 7 (2), e2086 (2016)
   PUBMED   26844700
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Morris,M.R., Ricketts,C.J., Gentle,D., McRonald,F., Carli,N.,
            Khalili,H., Brown,M., Kishida,T., Yao,M., Banks,R.E., Clarke,N.,
            Latif,F. and Maher,E.R.
  TITLE     Genome-wide methylation analysis identifies epigenetically
            inactivated candidate tumour suppressor genes in renal cell
            carcinoma
  JOURNAL   Oncogene 30 (12), 1390-1401 (2011)
   PUBMED   21132003
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Zody,M.C., Garber,M., Adams,D.J., Sharpe,T., Harrow,J.,
            Lupski,J.R., Nicholson,C., Searle,S.M., Wilming,L., Young,S.K.,
            Abouelleil,A., Allen,N.R., Bi,W., Bloom,T., Borowsky,M.L.,
            Bugalter,B.E., Butler,J., Chang,J.L., Chen,C.K., Cook,A., Corum,B.,
            Cuomo,C.A., de Jong,P.J., DeCaprio,D., Dewar,K., FitzGerald,M.,
            Gilbert,J., Gibson,R., Gnerre,S., Goldstein,S., Grafham,D.V.,
            Grocock,R., Hafez,N., Hagopian,D.S., Hart,E., Norman,C.H.,
            Humphray,S., Jaffe,D.B., Jones,M., Kamal,M., Khodiyar,V.K.,
            LaButti,K., Laird,G., Lehoczky,J., Liu,X., Lokyitsang,T.,
            Loveland,J., Lui,A., Macdonald,P., Major,J.E., Matthews,L.,
            Mauceli,E., McCarroll,S.A., Mihalev,A.H., Mudge,J., Nguyen,C.,
            Nicol,R., O'Leary,S.B., Osoegawa,K., Schwartz,D.C., Shaw-Smith,C.,
            Stankiewicz,P., Steward,C., Swarbreck,D., Venkataraman,V.,
            Whittaker,C.A., Yang,X., Zimmer,A.R., Bradley,A., Hubbard,T.,
            Birren,B.W., Rogers,J., Lander,E.S. and Nusbaum,C.
  TITLE     DNA sequence of human chromosome 17 and analysis of rearrangement
            in the human lineage
  JOURNAL   Nature 440 (7087), 1045-1049 (2006)
   PUBMED   16625196
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104564.11.
            
            ##Evidence-Data-START##
            CDS exon combination :: AK096431.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..472
                     /product="coronin-6 isoform 1"
                     /note="coronin, actin binding protein 6; clipin-E;
                     coronin-like protein E"
                     /calculated_mol_wt=52857
     Region          9..454
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          37..79
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          85..129
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          134..171
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          179..215
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          222..262
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          269..310
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..472
                     /gene="CORO6"
                     /gene_synonym="ClipinE"
                     /coded_by="NM_001388431.1:228..1646"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS11252.2"
                     /db_xref="GeneID:84940"
                     /db_xref="HGNC:HGNC:21356"
                     /db_xref="MIM:621442"
ORIGIN      
        1 msrrvvrqsk frhvfgqaak adqayedirv skvtwdssfc avnpkflaii veaggggafi
       61 vlplaktgrv dknyplvtgh tapvldidwc phndnviasa sddttimvwq ipdytpmrni
      121 tepiitlegh skrvgilswh ptarnvllsa ggdnviiiwn vgtgevllsl ddmhpdvihs
      181 vcwnsngsll attckdktlr iidprkgqvv aerfaahegm rpmravftrq ghifttgftr
      241 msqrelglwd pnnfeepval qemdtsngvl lpfydpdssi vylcgkgdss iryfeitdep
      301 pfvhylntfs skepqrgmgf mpkrgldvsk ceiarfyklh erkcepiimt vprksdlfqd
      361 dlypdtpgpe paleadewls gqdaepvlis lrdgyvppkh relrvtkrni ldvrppsgpr
      421 rsqsasdapl sqqhtletll eeikalrerv qaqeqrital enmlcelvdg td
//
LOCUS       NP_001338231             237 aa            linear   PRI 11-DEC-2025
DEFINITION  coronin-6 isoform 2 [Homo sapiens].
ACCESSION   NP_001338231
VERSION     NP_001338231.1
DBSOURCE    REFSEQ: accession NM_001351302.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Cardinali,B., Cappella,M., Provenzano,C., Garcia-Manteiga,J.M.,
            Lazarevic,D., Cittaro,D., Martelli,F. and Falcone,G.
  TITLE     MicroRNA-222 regulates muscle alternative splicing through Rbm24
            during differentiation of skeletal muscle cells
  JOURNAL   Cell Death Dis 7 (2), e2086 (2016)
   PUBMED   26844700
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Morris,M.R., Ricketts,C.J., Gentle,D., McRonald,F., Carli,N.,
            Khalili,H., Brown,M., Kishida,T., Yao,M., Banks,R.E., Clarke,N.,
            Latif,F. and Maher,E.R.
  TITLE     Genome-wide methylation analysis identifies epigenetically
            inactivated candidate tumour suppressor genes in renal cell
            carcinoma
  JOURNAL   Oncogene 30 (12), 1390-1401 (2011)
   PUBMED   21132003
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Zody,M.C., Garber,M., Adams,D.J., Sharpe,T., Harrow,J.,
            Lupski,J.R., Nicholson,C., Searle,S.M., Wilming,L., Young,S.K.,
            Abouelleil,A., Allen,N.R., Bi,W., Bloom,T., Borowsky,M.L.,
            Bugalter,B.E., Butler,J., Chang,J.L., Chen,C.K., Cook,A., Corum,B.,
            Cuomo,C.A., de Jong,P.J., DeCaprio,D., Dewar,K., FitzGerald,M.,
            Gilbert,J., Gibson,R., Gnerre,S., Goldstein,S., Grafham,D.V.,
            Grocock,R., Hafez,N., Hagopian,D.S., Hart,E., Norman,C.H.,
            Humphray,S., Jaffe,D.B., Jones,M., Kamal,M., Khodiyar,V.K.,
            LaButti,K., Laird,G., Lehoczky,J., Liu,X., Lokyitsang,T.,
            Loveland,J., Lui,A., Macdonald,P., Major,J.E., Matthews,L.,
            Mauceli,E., McCarroll,S.A., Mihalev,A.H., Mudge,J., Nguyen,C.,
            Nicol,R., O'Leary,S.B., Osoegawa,K., Schwartz,D.C., Shaw-Smith,C.,
            Stankiewicz,P., Steward,C., Swarbreck,D., Venkataraman,V.,
            Whittaker,C.A., Yang,X., Zimmer,A.R., Bradley,A., Hubbard,T.,
            Birren,B.W., Rogers,J., Lander,E.S. and Nusbaum,C.
  TITLE     DNA sequence of human chromosome 17 and analysis of rearrangement
            in the human lineage
  JOURNAL   Nature 440 (7087), 1045-1049 (2006)
   PUBMED   16625196
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104564.11.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1316117.1,
                                           SRR18074968.1220656.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..237
                     /product="coronin-6 isoform 2"
                     /note="coronin, actin binding protein 6; clipin-E;
                     coronin-like protein E"
                     /calculated_mol_wt=26752
     Region          <21..231
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     CDS             1..237
                     /gene="CORO6"
                     /gene_synonym="ClipinE"
                     /coded_by="NM_001351302.3:686..1399"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:84940"
                     /db_xref="HGNC:HGNC:21356"
                     /db_xref="MIM:621442"
ORIGIN      
        1 mpspwgwfav tacgaqrnnf eepvalqemd tsngvllpfy dpdssivylc gkgdssiryf
       61 eitdeppfvh ylntfsskep qrgmgfmpkr gldvskceia rfyklherkc epiimtvprk
      121 sdlfqddlyp dtpgpepale adewlsgqda epvlislrdg yvppkhrelr vtkrnildvr
      181 ppsgprrsqs asdaplsqht letlleeika lrervqaqeq ritalenmlc elvdgtd
//
LOCUS       NP_001280162             112 aa            linear   PRI 11-DEC-2025
DEFINITION  N-myc proto-oncogene protein isoform 3 [Homo sapiens].
ACCESSION   NP_001280162
VERSION     NP_001280162.1
DBSOURCE    REFSEQ: accession NM_001293233.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Vempuluru,V.S., Maniar,A., Bakal,K. and Kaliki,S.
  TITLE     Role of MYCN in retinoblastoma: A review of current literature
  JOURNAL   Surv Ophthalmol 69 (5), 697-706 (2024)
   PUBMED   38796108
  REMARK    GeneRIF: Role of MYCN in retinoblastoma: A review of current
            literature.
            Review article
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Sundaramoorthy,S., Colombo,D.F., Sanalkumar,R., Broye,L., Balmas
            Bourloud,K., Boulay,G., Cironi,L., Stamenkovic,I., Renella,R.,
            Kuttler,F., Turcatti,G., Rivera,M.N., Muhlethaler-Mottet,A.,
            Bardet,A.F. and Riggi,N.
  TITLE     Preclinical spheroid models identify BMX as a therapeutic target
            for metastatic MYCN nonamplified neuroblastoma
  JOURNAL   JCI Insight 9 (14), e169647 (2024)
   PUBMED   39133652
  REMARK    GeneRIF: Preclinical spheroid models identify BMX as a therapeutic
            target for metastatic MYCN nonamplified neuroblastoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Murray,J.E., Valli,E., Milazzo,G., Mayoh,C., Gifford,A.J.,
            Fletcher,J.I., Xue,C., Jayatilleke,N., Salehzadeh,F., Gamble,L.D.,
            Rouaen,J.R.C., Carter,D.R., Forgham,H., Sekyere,E.O., Keating,J.,
            Eden,G., Allan,S., Alfred,S., Kusuma,F.K., Clark,A., Webber,H.,
            Russell,A.J., de Weck,A., Kile,B.T., Santulli,M., De Rosa,P.,
            Fleuren,E.D.G., Gao,W., Wilkinson-White,L., Low,J.K.K.,
            Mackay,J.P., Marshall,G.M., Hilton,D.J., Giorgi,F.M., Koster,J.,
            Perini,G., Haber,M. and Norris,M.D.
  TITLE     The transcriptional co-repressor Runx1t1 is essential for
            MYCN-driven neuroblastoma tumorigenesis
  JOURNAL   Nat Commun 15 (1), 5585 (2024)
   PUBMED   38992040
  REMARK    GeneRIF: The transcriptional co-repressor Runx1t1 is essential for
            MYCN-driven neuroblastoma tumorigenesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Besancon,R., Valsesia-Wittmann,S., Locher,C., Delloye-Bourgeois,C.,
            Furhman,L., Tutrone,G., Bertrand,C., Jallas,A.C., Garin,E. and
            Puisieux,A.
  TITLE     Upstream ORF affects MYCN translation depending on exon 1b
            alternative splicing
  JOURNAL   BMC Cancer 9, 445 (2009)
   PUBMED   20017904
  REMARK    GeneRIF: Existence of upstream ORF in MYCN transcripts leads to a
            new level of MYCN regulation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 112)
  AUTHORS   Marcelis,C.L.M. and de Brouwer,A.P.M.
  TITLE     Feingold Syndrome 1
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301770
REFERENCE   6  (residues 1 to 112)
  AUTHORS   Scott,D.A.
  TITLE     Esophageal Atresia / Tracheoesophageal Fistula Overview - RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301753
REFERENCE   7  (residues 1 to 112)
  AUTHORS   Hagiwara,T., Nakaya,K., Nakamura,Y., Nakajima,H., Nishimura,S. and
            Taya,Y.
  TITLE     Specific phosphorylation of the acidic central region of the N-myc
            protein by casein kinase II
  JOURNAL   Eur J Biochem 209 (3), 945-950 (1992)
   PUBMED   1425701
REFERENCE   8  (residues 1 to 112)
  AUTHORS   Armstrong,B.C. and Krystal,G.W.
  TITLE     Isolation and characterization of complementary DNA for N-cym, a
            gene encoded by the DNA strand opposite to N-myc
  JOURNAL   Cell Growth Differ 3 (6), 385-390 (1992)
   PUBMED   1419902
REFERENCE   9  (residues 1 to 112)
  AUTHORS   Fougerousse,F., Meloni,R., Roudaut,C. and Beckmann,J.S.
  TITLE     Dinucleotide repeat polymorphism at the human hemoglobin alpha-1
            pseudo-gene (HBAP1)
  JOURNAL   Nucleic Acids Res 20 (5), 1165 (1992)
   PUBMED   1549498
REFERENCE   10 (residues 1 to 112)
  AUTHORS   Stanton,L.W. and Bishop,J.M.
  TITLE     Alternative processing of RNA transcribed from NMYC
  JOURNAL   Mol Cell Biol 7 (12), 4266-4272 (1987)
   PUBMED   3437890
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010145.10 and BC002712.2.
            
            Summary: This gene is a member of the MYC family and encodes a
            protein with a basic helix-loop-helix (bHLH) domain. This protein
            is located in the nucleus and must dimerize with another bHLH
            protein in order to bind DNA. Amplification of this gene is
            associated with a variety of tumors, most notably neuroblastomas.
            Multiple alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jun 2014].
            
            Transcript Variant: This variant (2) lacks segment 1b in the 5'
            region, compared to variant 1. This variant includes two open
            reading frames; the isoform (3, also known as MYCNOT, see PMID:
            20017904) represented by this Refseq is translated from the
            upstream open reading frame. The isoform 3 has an identical
            N-terminus to that of the isoform 2, and the function of the
            isoform 3 is currently unknown.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BX353859.2, BX393747.2 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1970526 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: PMID: 20017904
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p24.3"
     Protein         1..112
                     /product="N-myc proto-oncogene protein isoform 3"
                     /note="neuroblastoma MYC oncogene; N-myc proto-oncogene
                     protein; oncogene NMYC; neuroblastoma-derived v-myc avian
                     myelocytomatosis viral related oncogene; class E basic
                     helix-loop-helix protein 37; v-myc avian myelocytomatosis
                     viral oncogene neuroblastoma derived homolog"
                     /calculated_mol_wt=11634
     CDS             1..112
                     /gene="MYCN"
                     /gene_synonym="bHLHe37; FGLDS1; MODED; MPAPA; MYCNsORF;
                     MYCNsPEP; N-myc; NMYC; ODED"
                     /coded_by="NM_001293233.2:38..376"
                     /note="isoform 3 is encoded by transcript variant 2"
                     /db_xref="GeneID:4613"
                     /db_xref="HGNC:HGNC:7559"
                     /db_xref="MIM:164840"
ORIGIN      
        1 mrgapgncvg aeqalarrkr aqtvairghp rppgppgdtr aesppdplqs agvlevgagp
       61 rlprppregs tpgiktngae rspqspagrr adaellhvhh aghdlqeprp rv
//
LOCUS       NP_005369                464 aa            linear   PRI 11-DEC-2025
DEFINITION  N-myc proto-oncogene protein isoform 1 [Homo sapiens].
ACCESSION   NP_005369
VERSION     NP_005369.2
DBSOURCE    REFSEQ: accession NM_005378.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Vempuluru,V.S., Maniar,A., Bakal,K. and Kaliki,S.
  TITLE     Role of MYCN in retinoblastoma: A review of current literature
  JOURNAL   Surv Ophthalmol 69 (5), 697-706 (2024)
   PUBMED   38796108
  REMARK    GeneRIF: Role of MYCN in retinoblastoma: A review of current
            literature.
            Review article
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Sundaramoorthy,S., Colombo,D.F., Sanalkumar,R., Broye,L., Balmas
            Bourloud,K., Boulay,G., Cironi,L., Stamenkovic,I., Renella,R.,
            Kuttler,F., Turcatti,G., Rivera,M.N., Muhlethaler-Mottet,A.,
            Bardet,A.F. and Riggi,N.
  TITLE     Preclinical spheroid models identify BMX as a therapeutic target
            for metastatic MYCN nonamplified neuroblastoma
  JOURNAL   JCI Insight 9 (14), e169647 (2024)
   PUBMED   39133652
  REMARK    GeneRIF: Preclinical spheroid models identify BMX as a therapeutic
            target for metastatic MYCN nonamplified neuroblastoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Murray,J.E., Valli,E., Milazzo,G., Mayoh,C., Gifford,A.J.,
            Fletcher,J.I., Xue,C., Jayatilleke,N., Salehzadeh,F., Gamble,L.D.,
            Rouaen,J.R.C., Carter,D.R., Forgham,H., Sekyere,E.O., Keating,J.,
            Eden,G., Allan,S., Alfred,S., Kusuma,F.K., Clark,A., Webber,H.,
            Russell,A.J., de Weck,A., Kile,B.T., Santulli,M., De Rosa,P.,
            Fleuren,E.D.G., Gao,W., Wilkinson-White,L., Low,J.K.K.,
            Mackay,J.P., Marshall,G.M., Hilton,D.J., Giorgi,F.M., Koster,J.,
            Perini,G., Haber,M. and Norris,M.D.
  TITLE     The transcriptional co-repressor Runx1t1 is essential for
            MYCN-driven neuroblastoma tumorigenesis
  JOURNAL   Nat Commun 15 (1), 5585 (2024)
   PUBMED   38992040
  REMARK    GeneRIF: The transcriptional co-repressor Runx1t1 is essential for
            MYCN-driven neuroblastoma tumorigenesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Besancon,R., Valsesia-Wittmann,S., Locher,C., Delloye-Bourgeois,C.,
            Furhman,L., Tutrone,G., Bertrand,C., Jallas,A.C., Garin,E. and
            Puisieux,A.
  TITLE     Upstream ORF affects MYCN translation depending on exon 1b
            alternative splicing
  JOURNAL   BMC Cancer 9, 445 (2009)
   PUBMED   20017904
  REMARK    GeneRIF: Existence of upstream ORF in MYCN transcripts leads to a
            new level of MYCN regulation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Marcelis,C.L.M. and de Brouwer,A.P.M.
  TITLE     Feingold Syndrome 1
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301770
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Scott,D.A.
  TITLE     Esophageal Atresia / Tracheoesophageal Fistula Overview - RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301753
REFERENCE   7  (residues 1 to 464)
  AUTHORS   Hagiwara,T., Nakaya,K., Nakamura,Y., Nakajima,H., Nishimura,S. and
            Taya,Y.
  TITLE     Specific phosphorylation of the acidic central region of the N-myc
            protein by casein kinase II
  JOURNAL   Eur J Biochem 209 (3), 945-950 (1992)
   PUBMED   1425701
REFERENCE   8  (residues 1 to 464)
  AUTHORS   Armstrong,B.C. and Krystal,G.W.
  TITLE     Isolation and characterization of complementary DNA for N-cym, a
            gene encoded by the DNA strand opposite to N-myc
  JOURNAL   Cell Growth Differ 3 (6), 385-390 (1992)
   PUBMED   1419902
REFERENCE   9  (residues 1 to 464)
  AUTHORS   Fougerousse,F., Meloni,R., Roudaut,C. and Beckmann,J.S.
  TITLE     Dinucleotide repeat polymorphism at the human hemoglobin alpha-1
            pseudo-gene (HBAP1)
  JOURNAL   Nucleic Acids Res 20 (5), 1165 (1992)
   PUBMED   1549498
REFERENCE   10 (residues 1 to 464)
  AUTHORS   Stanton,L.W. and Bishop,J.M.
  TITLE     Alternative processing of RNA transcribed from NMYC
  JOURNAL   Mol Cell Biol 7 (12), 4266-4272 (1987)
   PUBMED   3437890
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010145.10 and BC002712.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 4, 2002 this sequence version replaced NP_005369.1.
            
            Summary: This gene is a member of the MYC family and encodes a
            protein with a basic helix-loop-helix (bHLH) domain. This protein
            is located in the nucleus and must dimerize with another bHLH
            protein in order to bind DNA. Amplification of this gene is
            associated with a variety of tumors, most notably neuroblastomas.
            Multiple alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jun 2014].
            
            Transcript Variant: This variant (2) lacks segment 1b in the 5'
            region, compared to variant 1. This variant includes two open
            reading frames; the isoform 1 represented by this RefSeq is
            translated from the downstream open reading frame. This transcript
            and variant 1 encode the same isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC002712.2, BT007384.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1970526 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000281043.4/ ENSP00000281043.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p24.3"
     Protein         1..464
                     /product="N-myc proto-oncogene protein isoform 1"
                     /note="neuroblastoma MYC oncogene; N-myc proto-oncogene
                     protein; oncogene NMYC; neuroblastoma-derived v-myc avian
                     myelocytomatosis viral related oncogene; class E basic
                     helix-loop-helix protein 37; v-myc avian myelocytomatosis
                     viral oncogene neuroblastoma derived homolog"
                     /calculated_mol_wt=49430
     Region          10..372
                     /region_name="Myc_N"
                     /note="Myc amino-terminal region; pfam01056"
                     /db_xref="CDD:460045"
     Region          19..47
                     /region_name="Interaction with AURKA.
                     /evidence=ECO:0000269|PubMed:27837025"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:30573562; propagated from
                     UniProtKB/Swiss-Prot (P04198.2)"
     Region          61..89
                     /region_name="Interaction with AURKA and FBXW7.
                     /evidence=ECO:0000269|PubMed:27837025"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Region          76..84
                     /region_name="9aaTAD.
                     /evidence=ECO:0000269|PubMed:34342803"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Region          129..172
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Region          196..294
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:1425701; propagated from
                     UniProtKB/Swiss-Prot (P04198.2)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:1425701; propagated from
                     UniProtKB/Swiss-Prot (P04198.2)"
     Region          334..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Region          378..464
                     /region_name="bHLHzip_N-Myc_like"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in N-Myc and similar proteins; cd11456"
                     /db_xref="CDD:381462"
     Site            order(378,382..383,386..387,389..391,393..394,398,
                     418..419)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381462"
     Site            order(397,400..401,403..404,407,420,423..424,427,429..431,
                     433..434,436..437,440,443..444,447..448,450..452,454..455,
                     457..464)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381462"
     Site            order(397,400..401,403..404,407,420,423..424,427,429..431,
                     433..434,436..437,440,443..444,447..448,450..451,454,
                     457..458,461..462,464)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381462"
     Region          433..454
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     CDS             1..464
                     /gene="MYCN"
                     /gene_synonym="bHLHe37; FGLDS1; MODED; MPAPA; MYCNsORF;
                     MYCNsPEP; N-myc; NMYC; ODED"
                     /coded_by="NM_005378.6:312..1706"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1687.1"
                     /db_xref="GeneID:4613"
                     /db_xref="HGNC:HGNC:7559"
                     /db_xref="MIM:164840"
ORIGIN      
        1 mpscststmp gmicknpdle fdslqpcfyp deddfyfggp dstppgediw kkfellptpp
       61 lspsrgfaeh sseppswvte mllenelwgs paeedafglg glggltpnpv ilqdcmwsgf
      121 sareklerav seklqhgrgp ptagstaqsp gagaaspagr ghggaagagr agaalpaela
      181 hpaaecvdpa vvfpfpvnkr epapvpaapa sapaagpava sgagiaapag apgvapprpg
      241 grqtsggdhk alstsgedtl sdsddeddee edeeeeidvv tvekrrsssn tkavttftit
      301 vrpknaalgp graqsselil krclpihqqh nyaapspyve sedappqkki kseasprplk
      361 svippkaksl sprnsdseds errrnhnile rqrrndlrss fltlrdhvpe lvknekaakv
      421 vilkkateyv hslqaeehql llekeklqar qqqllkkieh artc
//
LOCUS       NP_001280157             464 aa            linear   PRI 11-DEC-2025
DEFINITION  N-myc proto-oncogene protein isoform 1 [Homo sapiens].
ACCESSION   NP_001280157 XP_006711949
VERSION     NP_001280157.1
DBSOURCE    REFSEQ: accession NM_001293228.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Vempuluru,V.S., Maniar,A., Bakal,K. and Kaliki,S.
  TITLE     Role of MYCN in retinoblastoma: A review of current literature
  JOURNAL   Surv Ophthalmol 69 (5), 697-706 (2024)
   PUBMED   38796108
  REMARK    GeneRIF: Role of MYCN in retinoblastoma: A review of current
            literature.
            Review article
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Sundaramoorthy,S., Colombo,D.F., Sanalkumar,R., Broye,L., Balmas
            Bourloud,K., Boulay,G., Cironi,L., Stamenkovic,I., Renella,R.,
            Kuttler,F., Turcatti,G., Rivera,M.N., Muhlethaler-Mottet,A.,
            Bardet,A.F. and Riggi,N.
  TITLE     Preclinical spheroid models identify BMX as a therapeutic target
            for metastatic MYCN nonamplified neuroblastoma
  JOURNAL   JCI Insight 9 (14), e169647 (2024)
   PUBMED   39133652
  REMARK    GeneRIF: Preclinical spheroid models identify BMX as a therapeutic
            target for metastatic MYCN nonamplified neuroblastoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Murray,J.E., Valli,E., Milazzo,G., Mayoh,C., Gifford,A.J.,
            Fletcher,J.I., Xue,C., Jayatilleke,N., Salehzadeh,F., Gamble,L.D.,
            Rouaen,J.R.C., Carter,D.R., Forgham,H., Sekyere,E.O., Keating,J.,
            Eden,G., Allan,S., Alfred,S., Kusuma,F.K., Clark,A., Webber,H.,
            Russell,A.J., de Weck,A., Kile,B.T., Santulli,M., De Rosa,P.,
            Fleuren,E.D.G., Gao,W., Wilkinson-White,L., Low,J.K.K.,
            Mackay,J.P., Marshall,G.M., Hilton,D.J., Giorgi,F.M., Koster,J.,
            Perini,G., Haber,M. and Norris,M.D.
  TITLE     The transcriptional co-repressor Runx1t1 is essential for
            MYCN-driven neuroblastoma tumorigenesis
  JOURNAL   Nat Commun 15 (1), 5585 (2024)
   PUBMED   38992040
  REMARK    GeneRIF: The transcriptional co-repressor Runx1t1 is essential for
            MYCN-driven neuroblastoma tumorigenesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Besancon,R., Valsesia-Wittmann,S., Locher,C., Delloye-Bourgeois,C.,
            Furhman,L., Tutrone,G., Bertrand,C., Jallas,A.C., Garin,E. and
            Puisieux,A.
  TITLE     Upstream ORF affects MYCN translation depending on exon 1b
            alternative splicing
  JOURNAL   BMC Cancer 9, 445 (2009)
   PUBMED   20017904
  REMARK    GeneRIF: Existence of upstream ORF in MYCN transcripts leads to a
            new level of MYCN regulation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Marcelis,C.L.M. and de Brouwer,A.P.M.
  TITLE     Feingold Syndrome 1
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301770
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Scott,D.A.
  TITLE     Esophageal Atresia / Tracheoesophageal Fistula Overview - RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301753
REFERENCE   7  (residues 1 to 464)
  AUTHORS   Hagiwara,T., Nakaya,K., Nakamura,Y., Nakajima,H., Nishimura,S. and
            Taya,Y.
  TITLE     Specific phosphorylation of the acidic central region of the N-myc
            protein by casein kinase II
  JOURNAL   Eur J Biochem 209 (3), 945-950 (1992)
   PUBMED   1425701
REFERENCE   8  (residues 1 to 464)
  AUTHORS   Armstrong,B.C. and Krystal,G.W.
  TITLE     Isolation and characterization of complementary DNA for N-cym, a
            gene encoded by the DNA strand opposite to N-myc
  JOURNAL   Cell Growth Differ 3 (6), 385-390 (1992)
   PUBMED   1419902
REFERENCE   9  (residues 1 to 464)
  AUTHORS   Fougerousse,F., Meloni,R., Roudaut,C. and Beckmann,J.S.
  TITLE     Dinucleotide repeat polymorphism at the human hemoglobin alpha-1
            pseudo-gene (HBAP1)
  JOURNAL   Nucleic Acids Res 20 (5), 1165 (1992)
   PUBMED   1549498
REFERENCE   10 (residues 1 to 464)
  AUTHORS   Stanton,L.W. and Bishop,J.M.
  TITLE     Alternative processing of RNA transcribed from NMYC
  JOURNAL   Mol Cell Biol 7 (12), 4266-4272 (1987)
   PUBMED   3437890
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010145.10 and BC002712.2.
            
            On Jun 7, 2014 this sequence version replaced XP_006711949.1.
            
            Summary: This gene is a member of the MYC family and encodes a
            protein with a basic helix-loop-helix (bHLH) domain. This protein
            is located in the nucleus and must dimerize with another bHLH
            protein in order to bind DNA. Amplification of this gene is
            associated with a variety of tumors, most notably neuroblastomas.
            Multiple alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jun 2014].
            
            Transcript Variant: This variant (1) represents the full-length
            transcript. Its exon 1 includes segments 1a and 1b (also known as
            exon 1a and exon 1b, PMID: 20017904). This variant encodes isoform
            1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BT007384.1, CV811888.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2145245, SAMEA2148874 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p24.3"
     Protein         1..464
                     /product="N-myc proto-oncogene protein isoform 1"
                     /note="neuroblastoma MYC oncogene; N-myc proto-oncogene
                     protein; oncogene NMYC; neuroblastoma-derived v-myc avian
                     myelocytomatosis viral related oncogene; class E basic
                     helix-loop-helix protein 37; v-myc avian myelocytomatosis
                     viral oncogene neuroblastoma derived homolog"
                     /calculated_mol_wt=49430
     Region          10..372
                     /region_name="Myc_N"
                     /note="Myc amino-terminal region; pfam01056"
                     /db_xref="CDD:460045"
     Region          19..47
                     /region_name="Interaction with AURKA.
                     /evidence=ECO:0000269|PubMed:27837025"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:30573562; propagated from
                     UniProtKB/Swiss-Prot (P04198.2)"
     Region          61..89
                     /region_name="Interaction with AURKA and FBXW7.
                     /evidence=ECO:0000269|PubMed:27837025"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Region          76..84
                     /region_name="9aaTAD.
                     /evidence=ECO:0000269|PubMed:34342803"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Region          129..172
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Region          196..294
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:1425701; propagated from
                     UniProtKB/Swiss-Prot (P04198.2)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:1425701; propagated from
                     UniProtKB/Swiss-Prot (P04198.2)"
     Region          334..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     Region          378..464
                     /region_name="bHLHzip_N-Myc_like"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in N-Myc and similar proteins; cd11456"
                     /db_xref="CDD:381462"
     Site            order(378,382..383,386..387,389..391,393..394,398,
                     418..419)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381462"
     Site            order(397,400..401,403..404,407,420,423..424,427,429..431,
                     433..434,436..437,440,443..444,447..448,450..452,454..455,
                     457..464)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381462"
     Site            order(397,400..401,403..404,407,420,423..424,427,429..431,
                     433..434,436..437,440,443..444,447..448,450..451,454,
                     457..458,461..462,464)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381462"
     Region          433..454
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (P04198.2)"
     CDS             1..464
                     /gene="MYCN"
                     /gene_synonym="bHLHe37; FGLDS1; MODED; MPAPA; MYCNsORF;
                     MYCNsPEP; N-myc; NMYC; ODED"
                     /coded_by="NM_001293228.2:622..2016"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1687.1"
                     /db_xref="GeneID:4613"
                     /db_xref="HGNC:HGNC:7559"
                     /db_xref="MIM:164840"
ORIGIN      
        1 mpscststmp gmicknpdle fdslqpcfyp deddfyfggp dstppgediw kkfellptpp
       61 lspsrgfaeh sseppswvte mllenelwgs paeedafglg glggltpnpv ilqdcmwsgf
      121 sareklerav seklqhgrgp ptagstaqsp gagaaspagr ghggaagagr agaalpaela
      181 hpaaecvdpa vvfpfpvnkr epapvpaapa sapaagpava sgagiaapag apgvapprpg
      241 grqtsggdhk alstsgedtl sdsddeddee edeeeeidvv tvekrrsssn tkavttftit
      301 vrpknaalgp graqsselil krclpihqqh nyaapspyve sedappqkki kseasprplk
      361 svippkaksl sprnsdseds errrnhnile rqrrndlrss fltlrdhvpe lvknekaakv
      421 vilkkateyv hslqaeehql llekeklqar qqqllkkieh artc
//
LOCUS       NP_001280160             253 aa            linear   PRI 11-DEC-2025
DEFINITION  N-myc proto-oncogene protein isoform 2 [Homo sapiens].
ACCESSION   NP_001280160
VERSION     NP_001280160.1
DBSOURCE    REFSEQ: accession NM_001293231.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Vempuluru,V.S., Maniar,A., Bakal,K. and Kaliki,S.
  TITLE     Role of MYCN in retinoblastoma: A review of current literature
  JOURNAL   Surv Ophthalmol 69 (5), 697-706 (2024)
   PUBMED   38796108
  REMARK    GeneRIF: Role of MYCN in retinoblastoma: A review of current
            literature.
            Review article
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Sundaramoorthy,S., Colombo,D.F., Sanalkumar,R., Broye,L., Balmas
            Bourloud,K., Boulay,G., Cironi,L., Stamenkovic,I., Renella,R.,
            Kuttler,F., Turcatti,G., Rivera,M.N., Muhlethaler-Mottet,A.,
            Bardet,A.F. and Riggi,N.
  TITLE     Preclinical spheroid models identify BMX as a therapeutic target
            for metastatic MYCN nonamplified neuroblastoma
  JOURNAL   JCI Insight 9 (14), e169647 (2024)
   PUBMED   39133652
  REMARK    GeneRIF: Preclinical spheroid models identify BMX as a therapeutic
            target for metastatic MYCN nonamplified neuroblastoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Murray,J.E., Valli,E., Milazzo,G., Mayoh,C., Gifford,A.J.,
            Fletcher,J.I., Xue,C., Jayatilleke,N., Salehzadeh,F., Gamble,L.D.,
            Rouaen,J.R.C., Carter,D.R., Forgham,H., Sekyere,E.O., Keating,J.,
            Eden,G., Allan,S., Alfred,S., Kusuma,F.K., Clark,A., Webber,H.,
            Russell,A.J., de Weck,A., Kile,B.T., Santulli,M., De Rosa,P.,
            Fleuren,E.D.G., Gao,W., Wilkinson-White,L., Low,J.K.K.,
            Mackay,J.P., Marshall,G.M., Hilton,D.J., Giorgi,F.M., Koster,J.,
            Perini,G., Haber,M. and Norris,M.D.
  TITLE     The transcriptional co-repressor Runx1t1 is essential for
            MYCN-driven neuroblastoma tumorigenesis
  JOURNAL   Nat Commun 15 (1), 5585 (2024)
   PUBMED   38992040
  REMARK    GeneRIF: The transcriptional co-repressor Runx1t1 is essential for
            MYCN-driven neuroblastoma tumorigenesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Besancon,R., Valsesia-Wittmann,S., Locher,C., Delloye-Bourgeois,C.,
            Furhman,L., Tutrone,G., Bertrand,C., Jallas,A.C., Garin,E. and
            Puisieux,A.
  TITLE     Upstream ORF affects MYCN translation depending on exon 1b
            alternative splicing
  JOURNAL   BMC Cancer 9, 445 (2009)
   PUBMED   20017904
  REMARK    GeneRIF: Existence of upstream ORF in MYCN transcripts leads to a
            new level of MYCN regulation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Marcelis,C.L.M. and de Brouwer,A.P.M.
  TITLE     Feingold Syndrome 1
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301770
REFERENCE   6  (residues 1 to 253)
  AUTHORS   Scott,D.A.
  TITLE     Esophageal Atresia / Tracheoesophageal Fistula Overview - RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301753
REFERENCE   7  (residues 1 to 253)
  AUTHORS   Hagiwara,T., Nakaya,K., Nakamura,Y., Nakajima,H., Nishimura,S. and
            Taya,Y.
  TITLE     Specific phosphorylation of the acidic central region of the N-myc
            protein by casein kinase II
  JOURNAL   Eur J Biochem 209 (3), 945-950 (1992)
   PUBMED   1425701
REFERENCE   8  (residues 1 to 253)
  AUTHORS   Armstrong,B.C. and Krystal,G.W.
  TITLE     Isolation and characterization of complementary DNA for N-cym, a
            gene encoded by the DNA strand opposite to N-myc
  JOURNAL   Cell Growth Differ 3 (6), 385-390 (1992)
   PUBMED   1419902
REFERENCE   9  (residues 1 to 253)
  AUTHORS   Fougerousse,F., Meloni,R., Roudaut,C. and Beckmann,J.S.
  TITLE     Dinucleotide repeat polymorphism at the human hemoglobin alpha-1
            pseudo-gene (HBAP1)
  JOURNAL   Nucleic Acids Res 20 (5), 1165 (1992)
   PUBMED   1549498
REFERENCE   10 (residues 1 to 253)
  AUTHORS   Stanton,L.W. and Bishop,J.M.
  TITLE     Alternative processing of RNA transcribed from NMYC
  JOURNAL   Mol Cell Biol 7 (12), 4266-4272 (1987)
   PUBMED   3437890
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010145.10 and BC002712.2.
            
            Summary: This gene is a member of the MYC family and encodes a
            protein with a basic helix-loop-helix (bHLH) domain. This protein
            is located in the nucleus and must dimerize with another bHLH
            protein in order to bind DNA. Amplification of this gene is
            associated with a variety of tumors, most notably neuroblastomas.
            Multiple alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jun 2014].
            
            Transcript Variant: This variant (3) lacks segment 1b and exon 2,
            which results in an upstream AUG start codon, compared to variant
            1. The resulting isoform (2) has a shorter and distinct N-terminus,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BE382888.1, BI194921.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p24.3"
     Protein         1..253
                     /product="N-myc proto-oncogene protein isoform 2"
                     /note="neuroblastoma MYC oncogene; N-myc proto-oncogene
                     protein; oncogene NMYC; neuroblastoma-derived v-myc avian
                     myelocytomatosis viral related oncogene; class E basic
                     helix-loop-helix protein 37; v-myc avian myelocytomatosis
                     viral oncogene neuroblastoma derived homolog"
                     /calculated_mol_wt=28229
     Region          <66..161
                     /region_name="Myc_N"
                     /note="Myc amino-terminal region; pfam01056"
                     /db_xref="CDD:460045"
     Region          167..253
                     /region_name="bHLHzip_N-Myc_like"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in N-Myc and similar proteins; cd11456"
                     /db_xref="CDD:381462"
     Site            order(167,171..172,175..176,178..180,182..183,187,
                     207..208)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381462"
     Site            order(186,189..190,192..193,196,209,212..213,216,218..220,
                     222..223,225..226,229,232..233,236..237,239..241,243..244,
                     246..253)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381462"
     Site            order(186,189..190,192..193,196,209,212..213,216,218..220,
                     222..223,225..226,229,232..233,236..237,239..240,243,
                     246..247,250..251,253)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381462"
     CDS             1..253
                     /gene="MYCN"
                     /gene_synonym="bHLHe37; FGLDS1; MODED; MPAPA; MYCNsORF;
                     MYCNsPEP; N-myc; NMYC; ODED"
                     /coded_by="NM_001293231.2:38..799"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS86823.1"
                     /db_xref="GeneID:4613"
                     /db_xref="HGNC:HGNC:7559"
                     /db_xref="MIM:164840"
ORIGIN      
        1 mrgapgncvg aeqalarrkr aqtvairghp rppgppgdtr aesppdplqs agddeddeee
       61 deeeeidvvt vekrrsssnt kavttftitv rpknaalgpg raqsselilk rclpihqqhn
      121 yaapspyves edappqkkik seasprplks vippkaksls prnsdsedse rrrnhniler
      181 qrrndlrssf ltlrdhvpel vknekaakvv ilkkateyvh slqaeehqll lekeklqarq
      241 qqllkkieha rtc
//
LOCUS       NP_115758                612 aa            linear   PRI 14-DEC-2025
DEFINITION  conserved oligomeric Golgi complex subunit 8 isoform 1 [Homo
            sapiens].
ACCESSION   NP_115758
VERSION     NP_115758.3
DBSOURCE    REFSEQ: accession NM_032382.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Climer,L.K., Pokrovskaya,I.D., Blackburn,J.B. and Lupashin,V.V.
  TITLE     Membrane detachment is not essential for COG complex function
  JOURNAL   Mol Biol Cell 29 (8), 964-974 (2018)
   PUBMED   29467253
  REMARK    GeneRIF: TMEM-COG4, COG7 and COG8 subunits restore endogenous COG
            localization to the Golgi membranes
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Yang,A., Cho,S.Y., Jang,J.H., Kim,J., Kim,S.Z., Lee,B.H., Yoo,H.W.
            and Jin,D.K.
  TITLE     Further delineation of COG8-CDG: A case with novel compound
            heterozygous mutations diagnosed by targeted exome sequencing
  JOURNAL   Clin Chim Acta 471, 191-195 (2017)
   PUBMED   28619360
  REMARK    GeneRIF: The exome sequencing was performed to screen all CDG type
            II-related genes, and two novel frameshift mutations were found:
            c.171dupG (p.Leu58Alafs*29) and c.1656dupC (p.Ala553Argfs*15) in
            COG8.
REFERENCE   4  (residues 1 to 612)
  AUTHORS   Bailey Blackburn,J., Pokrovskaya,I., Fisher,P., Ungar,D. and
            Lupashin,V.V.
  TITLE     COG Complex Complexities: Detailed Characterization of a Complete
            Set of HEK293T Cells Lacking Individual COG Subunits
  JOURNAL   Front Cell Dev Biol 4, 23 (2016)
   PUBMED   27066481
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 612)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 612)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     The binary interacting network of the conserved oligomeric Golgi
            tethering complex
  JOURNAL   J Biol Chem 279 (23), 24640-24648 (2004)
   PUBMED   15047703
REFERENCE   7  (residues 1 to 612)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     Sec34 is implicated in traffic from the endoplasmic reticulum to
            the Golgi and exists in a complex with GTC-90 and ldlBp
  JOURNAL   J Biol Chem 277 (24), 21955-21961 (2002)
   PUBMED   11929878
REFERENCE   8  (residues 1 to 612)
  AUTHORS   Ungar,D., Oka,T., Brittle,E.E., Vasile,E., Lupashin,V.V.,
            Chatterton,J.E., Heuser,J.E., Krieger,M. and Waters,M.G.
  TITLE     Characterization of a mammalian Golgi-localized protein complex,
            COG, that is required for normal Golgi morphology and function
  JOURNAL   J Cell Biol 157 (3), 405-415 (2002)
   PUBMED   11980916
REFERENCE   9  (residues 1 to 612)
  AUTHORS   Whyte,J.R. and Munro,S.
  TITLE     The Sec34/35 Golgi transport complex is related to the exocyst,
            defining a family of complexes involved in multiple steps of
            membrane traffic
  JOURNAL   Dev Cell 1 (4), 527-537 (2001)
   PUBMED   11703943
REFERENCE   10 (residues 1 to 612)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC121022.1, BC017492.1 and
            AC026464.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 29, 2008 this sequence version replaced NP_115758.2.
            
            Summary: This gene encodes a protein that is a component of the
            conserved oligomeric Golgi (COG) complex, a multiprotein complex
            that plays a structural role in the Golgi apparatus, and is
            involved in intracellular membrane trafficking and glycoprotein
            modification. Mutations in this gene cause congenital disorder of
            glycosylation, type IIh, a disease that is characterized by
            under-glycosylated serum proteins, and whose symptoms include
            severe psychomotor retardation, failure to thrive, seizures, and
            dairy and wheat product intolerance. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853566.10473.1,
                                           SRR11853565.11394.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306875.10/ ENSP00000305459.6
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..612
                     /product="conserved oligomeric Golgi complex subunit 8
                     isoform 1"
                     /EC_number="3.5.1.88"
                     /note="dependent on RIC1; conserved oligomeric Golgi
                     complex subunit 8; conserved oligomeric golgi complex
                     component 8; COG complex subunit 8"
                     /calculated_mol_wt=68293
     Region          50..364
                     /region_name="Dor1"
                     /note="Dor1-like family; pfam04124"
                     /db_xref="CDD:427729"
     Region          568..612
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MW5.2)"
     CDS             1..612
                     /gene="COG8"
                     /gene_synonym="CDG2H; DOR1"
                     /coded_by="NM_032382.5:13..1851"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10876.1"
                     /db_xref="GeneID:84342"
                     /db_xref="HGNC:HGNC:18623"
                     /db_xref="MIM:606979"
ORIGIN      
        1 mataatipsv atataaalge vedegllasl frdrfpeaqw rerpdvgryl relsgsgler
       61 lrreperlae eraqllqqtr dlafanyktf irgaecteri hrlfgdveas lgrlldrlps
      121 fqqscrnfvk eaeeissnrr mnsltlnrht eileileipq lmdtcvrnsy yeealelaay
      181 vrrlerkyss ipviqgivne vrqsmqlmls qliqqlrtni qlpaclrvig ylrrmdvfte
      241 aelrvkflqa rdawlrsilt aipnddpyfh itktieasrv hlfdiitqyr aifsdedpll
      301 ppamgehtvn esaifhgwvl qkvsqflqvl etdlyrgigg hldsllgqcm yfglsfsrvg
      361 adfrgqlapv fqrvaistfq kaiqetvekf qeemnsymli sapailgtsn mpaavpatqp
      421 gtlqppmvll dfpplacfln nilvafndlr lccpvalaqd vtgaledala kvtkiilafh
      481 raeeaafssg eqelfvqfct vfledlvpyl nrclqvlfpp aqiaqtlgip ptqlskygnl
      541 ghvnigaiqe plafilpkre tlftlddqal gpeltapape ppaeeprlep agpacpeggr
      601 aetqaeppsv gp
//
LOCUS       NP_001361800             534 aa            linear   PRI 14-DEC-2025
DEFINITION  conserved oligomeric Golgi complex subunit 8 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001361800
VERSION     NP_001361800.1
DBSOURCE    REFSEQ: accession NM_001374871.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Climer,L.K., Pokrovskaya,I.D., Blackburn,J.B. and Lupashin,V.V.
  TITLE     Membrane detachment is not essential for COG complex function
  JOURNAL   Mol Biol Cell 29 (8), 964-974 (2018)
   PUBMED   29467253
  REMARK    GeneRIF: TMEM-COG4, COG7 and COG8 subunits restore endogenous COG
            localization to the Golgi membranes
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Yang,A., Cho,S.Y., Jang,J.H., Kim,J., Kim,S.Z., Lee,B.H., Yoo,H.W.
            and Jin,D.K.
  TITLE     Further delineation of COG8-CDG: A case with novel compound
            heterozygous mutations diagnosed by targeted exome sequencing
  JOURNAL   Clin Chim Acta 471, 191-195 (2017)
   PUBMED   28619360
  REMARK    GeneRIF: The exome sequencing was performed to screen all CDG type
            II-related genes, and two novel frameshift mutations were found:
            c.171dupG (p.Leu58Alafs*29) and c.1656dupC (p.Ala553Argfs*15) in
            COG8.
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Bailey Blackburn,J., Pokrovskaya,I., Fisher,P., Ungar,D. and
            Lupashin,V.V.
  TITLE     COG Complex Complexities: Detailed Characterization of a Complete
            Set of HEK293T Cells Lacking Individual COG Subunits
  JOURNAL   Front Cell Dev Biol 4, 23 (2016)
   PUBMED   27066481
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     The binary interacting network of the conserved oligomeric Golgi
            tethering complex
  JOURNAL   J Biol Chem 279 (23), 24640-24648 (2004)
   PUBMED   15047703
REFERENCE   7  (residues 1 to 534)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     Sec34 is implicated in traffic from the endoplasmic reticulum to
            the Golgi and exists in a complex with GTC-90 and ldlBp
  JOURNAL   J Biol Chem 277 (24), 21955-21961 (2002)
   PUBMED   11929878
REFERENCE   8  (residues 1 to 534)
  AUTHORS   Ungar,D., Oka,T., Brittle,E.E., Vasile,E., Lupashin,V.V.,
            Chatterton,J.E., Heuser,J.E., Krieger,M. and Waters,M.G.
  TITLE     Characterization of a mammalian Golgi-localized protein complex,
            COG, that is required for normal Golgi morphology and function
  JOURNAL   J Cell Biol 157 (3), 405-415 (2002)
   PUBMED   11980916
REFERENCE   9  (residues 1 to 534)
  AUTHORS   Whyte,J.R. and Munro,S.
  TITLE     The Sec34/35 Golgi transport complex is related to the exocyst,
            defining a family of complexes involved in multiple steps of
            membrane traffic
  JOURNAL   Dev Cell 1 (4), 527-537 (2001)
   PUBMED   11703943
REFERENCE   10 (residues 1 to 534)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026464.7.
            
            Summary: This gene encodes a protein that is a component of the
            conserved oligomeric Golgi (COG) complex, a multiprotein complex
            that plays a structural role in the Golgi apparatus, and is
            involved in intracellular membrane trafficking and glycoprotein
            modification. Mutations in this gene cause congenital disorder of
            glycosylation, type IIh, a disease that is characterized by
            under-glycosylated serum proteins, and whose symptoms include
            severe psychomotor retardation, failure to thrive, seizures, and
            dairy and wheat product intolerance. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3321235.1,
                                           SRR14038193.937449.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..534
                     /product="conserved oligomeric Golgi complex subunit 8
                     isoform 2"
                     /EC_number="3.5.1.88"
                     /note="dependent on RIC1; conserved oligomeric Golgi
                     complex subunit 8; conserved oligomeric golgi complex
                     component 8; COG complex subunit 8"
                     /calculated_mol_wt=60308
     Region          50..364
                     /region_name="Dor1"
                     /note="Dor1-like family; pfam04124"
                     /db_xref="CDD:427729"
     CDS             1..534
                     /gene="COG8"
                     /gene_synonym="CDG2H; DOR1"
                     /coded_by="NM_001374871.1:13..1617"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS92189.1"
                     /db_xref="GeneID:84342"
                     /db_xref="HGNC:HGNC:18623"
                     /db_xref="MIM:606979"
ORIGIN      
        1 mataatipsv atataaalge vedegllasl frdrfpeaqw rerpdvgryl relsgsgler
       61 lrreperlae eraqllqqtr dlafanyktf irgaecteri hrlfgdveas lgrlldrlps
      121 fqqscrnfvk eaeeissnrr mnsltlnrht eileileipq lmdtcvrnsy yeealelaay
      181 vrrlerkyss ipviqgivne vrqsmqlmls qliqqlrtni qlpaclrvig ylrrmdvfte
      241 aelrvkflqa rdawlrsilt aipnddpyfh itktieasrv hlfdiitqyr aifsdedpll
      301 ppamgehtvn esaifhgwvl qkvsqflqvl etdlyrgigg hldsllgqcm yfglsfsrvg
      361 adfrgqlapv fqrvaistfq kaiqetvekf qeemnsymli sapailgtsn mpaavpatqp
      421 gtlqppmvll dfpplacfln nilvafndlr lccpvalaqd vtgaledala kvtkiilafh
      481 raeeaafssg eqelfvqfct vfledlvpyl nrclqvlfpp aqiaqtlgkr mkil
//
LOCUS       NP_004958                317 aa            linear   PRI 14-DEC-2025
DEFINITION  integrin-binding sialoprotein precursor [Homo sapiens].
ACCESSION   NP_004958
VERSION     NP_004958.2
DBSOURCE    REFSEQ: accession NM_004967.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Ma,Y., Chen,B., Zhang,B., Zhang,C., Zhu,Q., Wang,X., Liu,Z. and
            Liu,H.
  TITLE     High expression of integrin-binding sialoprotein (IBSP) is
            associated with poor prognosis of osteosarcoma
  JOURNAL   Aging (Albany NY) 16 (1), 28-42 (2023)
   PUBMED   38006395
  REMARK    GeneRIF: High expression of integrin-binding sialoprotein (IBSP) is
            associated with poor prognosis of osteosarcoma.
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Fonseca,J.M., Martins,M.D., Vargas,P.A., Silva,W.G.,
            Normando,A.G.C., Palmier,N.R., Ribeiro,A.C.P., Brandao,T.B.,
            Lopes,M.A., Goes,M.F. and Santos-Silva,A.R.
  TITLE     Preservation of immunoexpression of type I collagen, BSP and BMP4
            in the dentin-pulp complex of head and neck cancer patients after
            radiotherapy
  JOURNAL   Braz Oral Res 36, e012 (2022)
   PUBMED   35081229
  REMARK    GeneRIF: Preservation of immunoexpression of type I collagen, BSP
            and BMP4 in the dentin-pulp complex of head and neck cancer
            patients after radiotherapy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Chen,Y., Qin,Y., Dai,M., Liu,L., Ni,Y., Sun,Q., Li,L., Zhou,Y.,
            Qiu,C. and Jiang,Y.
  TITLE     IBSP, a potential recurrence biomarker, promotes the progression of
            colorectal cancer via Fyn/beta-catenin signaling pathway
  JOURNAL   Cancer Med 10 (12), 4030-4045 (2021)
   PUBMED   33987980
  REMARK    GeneRIF: IBSP, a potential recurrence biomarker, promotes the
            progression of colorectal cancer via Fyn/beta-catenin signaling
            pathway.
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Benz,F., Bogen,A., Praktiknjo,M., Jansen,C., Meyer,C., Wree,A.,
            Demir,M., Loosen,S., Vucur,M., Schierwagen,R., Tacke,F.,
            Trebicka,J. and Roderburg,C.
  TITLE     Serum levels of bone sialoprotein correlate with portal pressure in
            patients with liver cirrhosis
  JOURNAL   PLoS One 15 (4), e0231701 (2020)
   PUBMED   32302330
  REMARK    GeneRIF: Study analyzed circulating bone sialoprotein (BSP) in a
            large cohort of patients with liver cirrhosis. Serum levels of BSP
            were similar in patients with different disease stages and were not
            indicative for prognosis. BSP serum levels did correlate inversely
            with portal pressure. BSP might represent a previously unrecognized
            marker for portal hypertension in patients with liver cirrhosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Maaroufi,A., Khadem-Ansari,M.H., Khalkhali,H.R. and Rasmi,Y.
  TITLE     Serum levels of bone sialoprotein, osteopontin, and
            beta2-microglobulin in stage I of multiple myeloma
  JOURNAL   J Cancer Res Ther 16 (1), 98-101 (2020)
   PUBMED   32362616
  REMARK    GeneRIF: Serum levels of bone sialoprotein, osteopontin, and
            beta2-microglobulin in stage I of multiple myeloma.
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Kim,R.H., Shapiro,H.S., Li,J.J., Wrana,J.L. and Sodek,J.
  TITLE     Characterization of the human bone sialoprotein (BSP) gene and its
            promoter sequence
  JOURNAL   Matrix Biol 14 (1), 31-40 (1994)
   PUBMED   8061918
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Goold,R.D., diSibio,G.L., Xu,H., Lang,D.B., Dadgar,J.,
            Magrane,G.G., Dugaiczyk,A., Smith,K.A., Cox,D.R., Masters,S.B. et
            al.
  TITLE     The development of sequence-tagged sites for human chromosome 4
  JOURNAL   Hum Mol Genet 2 (8), 1271-1288 (1993)
   PUBMED   8401509
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Fisher,L.W., McBride,O.W., Termine,J.D. and Young,M.F.
  TITLE     Human bone sialoprotein. Deduced protein sequence and chromosomal
            localization
  JOURNAL   J Biol Chem 265 (4), 2347-2351 (1990)
   PUBMED   2404984
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Oldberg,A., Franzen,A., Heinegard,D., Pierschbacher,M. and
            Ruoslahti,E.
  TITLE     Identification of a bone sialoprotein receptor in osteosarcoma
            cells
  JOURNAL   J Biol Chem 263 (36), 19433-19436 (1988)
   PUBMED   2461939
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Fisher,L.W., Hawkins,G.R., Tuross,N. and Termine,J.D.
  TITLE     Purification and partial characterization of small proteoglycans I
            and II, bone sialoproteins I and II, and osteonectin from the
            mineral compartment of developing human bone
  JOURNAL   J Biol Chem 262 (20), 9702-9708 (1987)
   PUBMED   3597437
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093768.3, AI751848.1,
            J05213.1, DV462680.1, BQ573754.1 and AA452255.1.
            
            On Feb 8, 2008 this sequence version replaced NP_004958.1.
            
            Summary: The protein encoded by this gene is a major structural
            protein of the bone matrix. It constitutes approximately 12% of the
            noncollagenous proteins in human bone and is synthesized by
            skeletal-associated cell types, including hypertrophic
            chondrocytes, osteoblasts, osteocytes, and osteoclasts. The only
            extraskeletal site of its synthesis is the trophoblast. This
            protein binds to calcium and hydroxyapatite via its acidic amino
            acid clusters, and mediates cell attachment through an RGD sequence
            that recognizes the vitronectin receptor. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.193979.1,
                                           SRR1660807.136311.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000226284.7/ ENSP00000226284.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q22.1"
     Protein         1..317
                     /product="integrin-binding sialoprotein precursor"
                     /note="bone sialoprotein II; bone sialoprotein 2;
                     cell-binding sialoprotein"
                     /calculated_mol_wt=33517
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1649
     mat_peptide     17..317
                     /product="integrin-binding sialoprotein"
                     /calculated_mol_wt=33517
     Region          17..314
                     /region_name="BSP_II"
                     /note="Bone sialoprotein II (BSP-II); pfam05432"
                     /db_xref="CDD:461651"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11669636; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Region          58..254
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21815.4)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q28862; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q28862; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q28862; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q28862; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q28862; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            119
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000305|PubMed:11459848; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            122
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000305|PubMed:11459848; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q28862; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            182
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            227
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000305|PubMed:11459848; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            228
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000305|PubMed:11459848; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            229
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000305|PubMed:11459848; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            238
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000305|PubMed:11459848; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            239
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000305|PubMed:11459848; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q28862; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Region          286..288
                     /region_name="cell-attachment tripeptide"
     Site            313
                     /site_type="sulfatation"
                     /note="Sulfotyrosine.
                     /evidence=ECO:0000269|PubMed:11669636; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     Site            314
                     /site_type="sulfatation"
                     /note="Sulfotyrosine.
                     /evidence=ECO:0000269|PubMed:11669636; propagated from
                     UniProtKB/Swiss-Prot (P21815.4)"
     CDS             1..317
                     /gene="IBSP"
                     /gene_synonym="BNSP; BSP; BSP II; BSP-II; SP-II"
                     /coded_by="NM_004967.4:95..1048"
                     /db_xref="CCDS:CCDS3624.1"
                     /db_xref="GeneID:3381"
                     /db_xref="HGNC:HGNC:5341"
                     /db_xref="MIM:147563"
ORIGIN      
        1 mktalillsi lgmacafsmk nlhrrvkied seengvfkyr pryylykhay fyphlkrfpv
       61 qgssdsseen gddsseeeee eeetsnegen neesnededs eaenttlsat tlgygedatp
      121 gtgytglaai qlpkkagdit nkatkekesd eeeeeeeegn eneeseaevd eneqgingts
      181 tnsteaengn gssggdngee geeesvtgan aedttetgrq gkgtskttts pnggfepttp
      241 pqvyrttspp fgktttveye geyeytgane ydngyeiyes engeprgdny rayedeysyf
      301 kgqgydgydg qnyyhhq
//
LOCUS       NP_001366191             638 aa            linear   PRI 14-DEC-2025
DEFINITION  conserved oligomeric Golgi complex subunit 8 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001366191
VERSION     NP_001366191.1
DBSOURCE    REFSEQ: accession NM_001379262.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Climer,L.K., Pokrovskaya,I.D., Blackburn,J.B. and Lupashin,V.V.
  TITLE     Membrane detachment is not essential for COG complex function
  JOURNAL   Mol Biol Cell 29 (8), 964-974 (2018)
   PUBMED   29467253
  REMARK    GeneRIF: TMEM-COG4, COG7 and COG8 subunits restore endogenous COG
            localization to the Golgi membranes
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Yang,A., Cho,S.Y., Jang,J.H., Kim,J., Kim,S.Z., Lee,B.H., Yoo,H.W.
            and Jin,D.K.
  TITLE     Further delineation of COG8-CDG: A case with novel compound
            heterozygous mutations diagnosed by targeted exome sequencing
  JOURNAL   Clin Chim Acta 471, 191-195 (2017)
   PUBMED   28619360
  REMARK    GeneRIF: The exome sequencing was performed to screen all CDG type
            II-related genes, and two novel frameshift mutations were found:
            c.171dupG (p.Leu58Alafs*29) and c.1656dupC (p.Ala553Argfs*15) in
            COG8.
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Bailey Blackburn,J., Pokrovskaya,I., Fisher,P., Ungar,D. and
            Lupashin,V.V.
  TITLE     COG Complex Complexities: Detailed Characterization of a Complete
            Set of HEK293T Cells Lacking Individual COG Subunits
  JOURNAL   Front Cell Dev Biol 4, 23 (2016)
   PUBMED   27066481
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 638)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 638)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     The binary interacting network of the conserved oligomeric Golgi
            tethering complex
  JOURNAL   J Biol Chem 279 (23), 24640-24648 (2004)
   PUBMED   15047703
REFERENCE   7  (residues 1 to 638)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     Sec34 is implicated in traffic from the endoplasmic reticulum to
            the Golgi and exists in a complex with GTC-90 and ldlBp
  JOURNAL   J Biol Chem 277 (24), 21955-21961 (2002)
   PUBMED   11929878
REFERENCE   8  (residues 1 to 638)
  AUTHORS   Ungar,D., Oka,T., Brittle,E.E., Vasile,E., Lupashin,V.V.,
            Chatterton,J.E., Heuser,J.E., Krieger,M. and Waters,M.G.
  TITLE     Characterization of a mammalian Golgi-localized protein complex,
            COG, that is required for normal Golgi morphology and function
  JOURNAL   J Cell Biol 157 (3), 405-415 (2002)
   PUBMED   11980916
REFERENCE   9  (residues 1 to 638)
  AUTHORS   Whyte,J.R. and Munro,S.
  TITLE     The Sec34/35 Golgi transport complex is related to the exocyst,
            defining a family of complexes involved in multiple steps of
            membrane traffic
  JOURNAL   Dev Cell 1 (4), 527-537 (2001)
   PUBMED   11703943
REFERENCE   10 (residues 1 to 638)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026464.7.
            
            Summary: This gene encodes a protein that is a component of the
            conserved oligomeric Golgi (COG) complex, a multiprotein complex
            that plays a structural role in the Golgi apparatus, and is
            involved in intracellular membrane trafficking and glycoprotein
            modification. Mutations in this gene cause congenital disorder of
            glycosylation, type IIh, a disease that is characterized by
            under-glycosylated serum proteins, and whose symptoms include
            severe psychomotor retardation, failure to thrive, seizures, and
            dairy and wheat product intolerance. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1960195.1,
                                           SRR1660809.61551.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..638
                     /product="conserved oligomeric Golgi complex subunit 8
                     isoform 4"
                     /EC_number="3.5.1.88"
                     /note="dependent on RIC1; conserved oligomeric Golgi
                     complex subunit 8; conserved oligomeric golgi complex
                     component 8; COG complex subunit 8"
                     /calculated_mol_wt=71871
     Region          50..364
                     /region_name="Dor1"
                     /note="Dor1-like family; pfam04124"
                     /db_xref="CDD:427729"
     Region          <588..626
                     /region_name="Def"
                     /note="Peptide deformylase [Translation, ribosomal
                     structure and biogenesis]; COG0242"
                     /db_xref="CDD:440012"
     CDS             1..638
                     /gene="COG8"
                     /gene_synonym="CDG2H; DOR1"
                     /coded_by="NM_001379262.1:13..1929"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:84342"
                     /db_xref="HGNC:HGNC:18623"
                     /db_xref="MIM:606979"
ORIGIN      
        1 mataatipsv atataaalge vedegllasl frdrfpeaqw rerpdvgryl relsgsgler
       61 lrreperlae eraqllqqtr dlafanyktf irgaecteri hrlfgdveas lgrlldrlps
      121 fqqscrnfvk eaeeissnrr mnsltlnrht eileileipq lmdtcvrnsy yeealelaay
      181 vrrlerkyss ipviqgivne vrqsmqlmls qliqqlrtni qlpaclrvig ylrrmdvfte
      241 aelrvkflqa rdawlrsilt aipnddpyfh itktieasrv hlfdiitqyr aifsdedpll
      301 ppamgehtvn esaifhgwvl qkvsqflqvl etdlyrgigg hldsllgqcm yfglsfsrvg
      361 adfrgqlapv fqrvaistfq kaiqetvekf qeemnsymli sapailgtsn mpaavpatqp
      421 gtlqppmvll dfpplacfln nilvafndlr lccpvalaqd vtgaledala kvtkiilafh
      481 raeeaafssg eqelfvqfct vfledlvpyl nrclqvlfpp aqiaqtlgip ptqlskygnl
      541 ghvnigaiqe plafilpkre tlftlddqal gpeltapape ppaeeprldp ngeqvvwqas
      601 gwaariiqhe mdhlqgclfi dkmdsrtftn vywmkvnd
//
LOCUS       NP_001366192             625 aa            linear   PRI 14-DEC-2025
DEFINITION  conserved oligomeric Golgi complex subunit 8 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001366192
VERSION     NP_001366192.1
DBSOURCE    REFSEQ: accession NM_001379263.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Climer,L.K., Pokrovskaya,I.D., Blackburn,J.B. and Lupashin,V.V.
  TITLE     Membrane detachment is not essential for COG complex function
  JOURNAL   Mol Biol Cell 29 (8), 964-974 (2018)
   PUBMED   29467253
  REMARK    GeneRIF: TMEM-COG4, COG7 and COG8 subunits restore endogenous COG
            localization to the Golgi membranes
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Yang,A., Cho,S.Y., Jang,J.H., Kim,J., Kim,S.Z., Lee,B.H., Yoo,H.W.
            and Jin,D.K.
  TITLE     Further delineation of COG8-CDG: A case with novel compound
            heterozygous mutations diagnosed by targeted exome sequencing
  JOURNAL   Clin Chim Acta 471, 191-195 (2017)
   PUBMED   28619360
  REMARK    GeneRIF: The exome sequencing was performed to screen all CDG type
            II-related genes, and two novel frameshift mutations were found:
            c.171dupG (p.Leu58Alafs*29) and c.1656dupC (p.Ala553Argfs*15) in
            COG8.
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Bailey Blackburn,J., Pokrovskaya,I., Fisher,P., Ungar,D. and
            Lupashin,V.V.
  TITLE     COG Complex Complexities: Detailed Characterization of a Complete
            Set of HEK293T Cells Lacking Individual COG Subunits
  JOURNAL   Front Cell Dev Biol 4, 23 (2016)
   PUBMED   27066481
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     The binary interacting network of the conserved oligomeric Golgi
            tethering complex
  JOURNAL   J Biol Chem 279 (23), 24640-24648 (2004)
   PUBMED   15047703
REFERENCE   7  (residues 1 to 625)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     Sec34 is implicated in traffic from the endoplasmic reticulum to
            the Golgi and exists in a complex with GTC-90 and ldlBp
  JOURNAL   J Biol Chem 277 (24), 21955-21961 (2002)
   PUBMED   11929878
REFERENCE   8  (residues 1 to 625)
  AUTHORS   Ungar,D., Oka,T., Brittle,E.E., Vasile,E., Lupashin,V.V.,
            Chatterton,J.E., Heuser,J.E., Krieger,M. and Waters,M.G.
  TITLE     Characterization of a mammalian Golgi-localized protein complex,
            COG, that is required for normal Golgi morphology and function
  JOURNAL   J Cell Biol 157 (3), 405-415 (2002)
   PUBMED   11980916
REFERENCE   9  (residues 1 to 625)
  AUTHORS   Whyte,J.R. and Munro,S.
  TITLE     The Sec34/35 Golgi transport complex is related to the exocyst,
            defining a family of complexes involved in multiple steps of
            membrane traffic
  JOURNAL   Dev Cell 1 (4), 527-537 (2001)
   PUBMED   11703943
REFERENCE   10 (residues 1 to 625)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026464.7.
            
            Summary: This gene encodes a protein that is a component of the
            conserved oligomeric Golgi (COG) complex, a multiprotein complex
            that plays a structural role in the Golgi apparatus, and is
            involved in intracellular membrane trafficking and glycoprotein
            modification. Mutations in this gene cause congenital disorder of
            glycosylation, type IIh, a disease that is characterized by
            under-glycosylated serum proteins, and whose symptoms include
            severe psychomotor retardation, failure to thrive, seizures, and
            dairy and wheat product intolerance. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.1582833.1,
                                           SRR18074967.2420470.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2159368
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..625
                     /product="conserved oligomeric Golgi complex subunit 8
                     isoform 5"
                     /EC_number="3.5.1.88"
                     /note="dependent on RIC1; conserved oligomeric Golgi
                     complex subunit 8; conserved oligomeric golgi complex
                     component 8; COG complex subunit 8"
                     /calculated_mol_wt=69697
     Region          50..364
                     /region_name="Dor1"
                     /note="Dor1-like family; pfam04124"
                     /db_xref="CDD:427729"
     CDS             1..625
                     /gene="COG8"
                     /gene_synonym="CDG2H; DOR1"
                     /coded_by="NM_001379263.1:13..1890"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:84342"
                     /db_xref="HGNC:HGNC:18623"
                     /db_xref="MIM:606979"
ORIGIN      
        1 mataatipsv atataaalge vedegllasl frdrfpeaqw rerpdvgryl relsgsgler
       61 lrreperlae eraqllqqtr dlafanyktf irgaecteri hrlfgdveas lgrlldrlps
      121 fqqscrnfvk eaeeissnrr mnsltlnrht eileileipq lmdtcvrnsy yeealelaay
      181 vrrlerkyss ipviqgivne vrqsmqlmls qliqqlrtni qlpaclrvig ylrrmdvfte
      241 aelrvkflqa rdawlrsilt aipnddpyfh itktieasrv hlfdiitqyr aifsdedpll
      301 ppamgehtvn esaifhgwvl qkvsqflqvl etdlyrgigg hldsllgqcm yfglsfsrvg
      361 adfrgqlapv fqrvaistfq kaiqetvekf qeemnsymli sapailgtsn mpaavpatqp
      421 gtlqppmvll dfpplacfln nilvafndlr lccpvalaqd vtgaledala kvtkiilafh
      481 raeeaafssg eqelfvqfct vfledlvpyl nrclqvlfpp aqiaqtlvtv fhfafptsgl
      541 gipptqlsky gnlghvniga iqeplafilp kretlftldd qalgpeltap apeppaeepr
      601 lepagpacpe ggraetqaep psvgp
//
LOCUS       NP_001366190             659 aa            linear   PRI 14-DEC-2025
DEFINITION  conserved oligomeric Golgi complex subunit 8 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001366190
VERSION     NP_001366190.1
DBSOURCE    REFSEQ: accession NM_001379261.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Climer,L.K., Pokrovskaya,I.D., Blackburn,J.B. and Lupashin,V.V.
  TITLE     Membrane detachment is not essential for COG complex function
  JOURNAL   Mol Biol Cell 29 (8), 964-974 (2018)
   PUBMED   29467253
  REMARK    GeneRIF: TMEM-COG4, COG7 and COG8 subunits restore endogenous COG
            localization to the Golgi membranes
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Yang,A., Cho,S.Y., Jang,J.H., Kim,J., Kim,S.Z., Lee,B.H., Yoo,H.W.
            and Jin,D.K.
  TITLE     Further delineation of COG8-CDG: A case with novel compound
            heterozygous mutations diagnosed by targeted exome sequencing
  JOURNAL   Clin Chim Acta 471, 191-195 (2017)
   PUBMED   28619360
  REMARK    GeneRIF: The exome sequencing was performed to screen all CDG type
            II-related genes, and two novel frameshift mutations were found:
            c.171dupG (p.Leu58Alafs*29) and c.1656dupC (p.Ala553Argfs*15) in
            COG8.
REFERENCE   4  (residues 1 to 659)
  AUTHORS   Bailey Blackburn,J., Pokrovskaya,I., Fisher,P., Ungar,D. and
            Lupashin,V.V.
  TITLE     COG Complex Complexities: Detailed Characterization of a Complete
            Set of HEK293T Cells Lacking Individual COG Subunits
  JOURNAL   Front Cell Dev Biol 4, 23 (2016)
   PUBMED   27066481
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 659)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 659)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     The binary interacting network of the conserved oligomeric Golgi
            tethering complex
  JOURNAL   J Biol Chem 279 (23), 24640-24648 (2004)
   PUBMED   15047703
REFERENCE   7  (residues 1 to 659)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     Sec34 is implicated in traffic from the endoplasmic reticulum to
            the Golgi and exists in a complex with GTC-90 and ldlBp
  JOURNAL   J Biol Chem 277 (24), 21955-21961 (2002)
   PUBMED   11929878
REFERENCE   8  (residues 1 to 659)
  AUTHORS   Ungar,D., Oka,T., Brittle,E.E., Vasile,E., Lupashin,V.V.,
            Chatterton,J.E., Heuser,J.E., Krieger,M. and Waters,M.G.
  TITLE     Characterization of a mammalian Golgi-localized protein complex,
            COG, that is required for normal Golgi morphology and function
  JOURNAL   J Cell Biol 157 (3), 405-415 (2002)
   PUBMED   11980916
REFERENCE   9  (residues 1 to 659)
  AUTHORS   Whyte,J.R. and Munro,S.
  TITLE     The Sec34/35 Golgi transport complex is related to the exocyst,
            defining a family of complexes involved in multiple steps of
            membrane traffic
  JOURNAL   Dev Cell 1 (4), 527-537 (2001)
   PUBMED   11703943
REFERENCE   10 (residues 1 to 659)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026464.7.
            
            Summary: This gene encodes a protein that is a component of the
            conserved oligomeric Golgi (COG) complex, a multiprotein complex
            that plays a structural role in the Golgi apparatus, and is
            involved in intracellular membrane trafficking and glycoprotein
            modification. Mutations in this gene cause congenital disorder of
            glycosylation, type IIh, a disease that is characterized by
            under-glycosylated serum proteins, and whose symptoms include
            severe psychomotor retardation, failure to thrive, seizures, and
            dairy and wheat product intolerance. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1613157.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2144333,
                                           SAMN03465413 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..659
                     /product="conserved oligomeric Golgi complex subunit 8
                     isoform 3"
                     /EC_number="3.5.1.88"
                     /note="dependent on RIC1; conserved oligomeric Golgi
                     complex subunit 8; conserved oligomeric golgi complex
                     component 8; COG complex subunit 8"
                     /calculated_mol_wt=73301
     Region          50..364
                     /region_name="Dor1"
                     /note="Dor1-like family; pfam04124"
                     /db_xref="CDD:427729"
     CDS             1..659
                     /gene="COG8"
                     /gene_synonym="CDG2H; DOR1"
                     /coded_by="NM_001379261.1:13..1992"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:84342"
                     /db_xref="HGNC:HGNC:18623"
                     /db_xref="MIM:606979"
ORIGIN      
        1 mataatipsv atataaalge vedegllasl frdrfpeaqw rerpdvgryl relsgsgler
       61 lrreperlae eraqllqqtr dlafanyktf irgaecteri hrlfgdveas lgrlldrlps
      121 fqqscrnfvk eaeeissnrr mnsltlnrht eileileipq lmdtcvrnsy yeealelaay
      181 vrrlerkyss ipviqgivne vrqsmqlmls qliqqlrtni qlpaclrvig ylrrmdvfte
      241 aelrvkflqa rdawlrsilt aipnddpyfh itktieasrv hlfdiitqyr aifsdedpll
      301 ppamgehtvn esaifhgwvl qkvsqflqvl etdlyrgigg hldsllgqcm yfglsfsrvg
      361 adfrgqlapv fqrvaistfq kaiqetvekf qeemnsymli sapailgtsn mpaavpatqp
      421 gtlqppmvll dfpplacfln nilvafndlr lccpvalaqd vtgaledala kvtkiilafh
      481 raeeaafssg eqelfvqfct vfledlvpyl nrclqvlfpp aqiaqtlgss dspalafpss
      541 wdyrpappsp anvvflremg flrvgqagle fltsgipptq lskygnlghv nigaiqepla
      601 filpkretlf tlddqalgpe ltapapeppa eeprlepagp acpeggraet qaeppsvgp
//
LOCUS       NP_001366194             579 aa            linear   PRI 14-DEC-2025
DEFINITION  conserved oligomeric Golgi complex subunit 8 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001366194
VERSION     NP_001366194.1
DBSOURCE    REFSEQ: accession NM_001379265.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Climer,L.K., Pokrovskaya,I.D., Blackburn,J.B. and Lupashin,V.V.
  TITLE     Membrane detachment is not essential for COG complex function
  JOURNAL   Mol Biol Cell 29 (8), 964-974 (2018)
   PUBMED   29467253
  REMARK    GeneRIF: TMEM-COG4, COG7 and COG8 subunits restore endogenous COG
            localization to the Golgi membranes
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Yang,A., Cho,S.Y., Jang,J.H., Kim,J., Kim,S.Z., Lee,B.H., Yoo,H.W.
            and Jin,D.K.
  TITLE     Further delineation of COG8-CDG: A case with novel compound
            heterozygous mutations diagnosed by targeted exome sequencing
  JOURNAL   Clin Chim Acta 471, 191-195 (2017)
   PUBMED   28619360
  REMARK    GeneRIF: The exome sequencing was performed to screen all CDG type
            II-related genes, and two novel frameshift mutations were found:
            c.171dupG (p.Leu58Alafs*29) and c.1656dupC (p.Ala553Argfs*15) in
            COG8.
REFERENCE   4  (residues 1 to 579)
  AUTHORS   Bailey Blackburn,J., Pokrovskaya,I., Fisher,P., Ungar,D. and
            Lupashin,V.V.
  TITLE     COG Complex Complexities: Detailed Characterization of a Complete
            Set of HEK293T Cells Lacking Individual COG Subunits
  JOURNAL   Front Cell Dev Biol 4, 23 (2016)
   PUBMED   27066481
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 579)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 579)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     The binary interacting network of the conserved oligomeric Golgi
            tethering complex
  JOURNAL   J Biol Chem 279 (23), 24640-24648 (2004)
   PUBMED   15047703
REFERENCE   7  (residues 1 to 579)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     Sec34 is implicated in traffic from the endoplasmic reticulum to
            the Golgi and exists in a complex with GTC-90 and ldlBp
  JOURNAL   J Biol Chem 277 (24), 21955-21961 (2002)
   PUBMED   11929878
REFERENCE   8  (residues 1 to 579)
  AUTHORS   Ungar,D., Oka,T., Brittle,E.E., Vasile,E., Lupashin,V.V.,
            Chatterton,J.E., Heuser,J.E., Krieger,M. and Waters,M.G.
  TITLE     Characterization of a mammalian Golgi-localized protein complex,
            COG, that is required for normal Golgi morphology and function
  JOURNAL   J Cell Biol 157 (3), 405-415 (2002)
   PUBMED   11980916
REFERENCE   9  (residues 1 to 579)
  AUTHORS   Whyte,J.R. and Munro,S.
  TITLE     The Sec34/35 Golgi transport complex is related to the exocyst,
            defining a family of complexes involved in multiple steps of
            membrane traffic
  JOURNAL   Dev Cell 1 (4), 527-537 (2001)
   PUBMED   11703943
REFERENCE   10 (residues 1 to 579)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026464.7.
            
            Summary: This gene encodes a protein that is a component of the
            conserved oligomeric Golgi (COG) complex, a multiprotein complex
            that plays a structural role in the Golgi apparatus, and is
            involved in intracellular membrane trafficking and glycoprotein
            modification. Mutations in this gene cause congenital disorder of
            glycosylation, type IIh, a disease that is characterized by
            under-glycosylated serum proteins, and whose symptoms include
            severe psychomotor retardation, failure to thrive, seizures, and
            dairy and wheat product intolerance. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3787811.1,
                                           SRR14038191.3500782.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146982, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..579
                     /product="conserved oligomeric Golgi complex subunit 8
                     isoform 6"
                     /EC_number="3.5.1.88"
                     /note="dependent on RIC1; conserved oligomeric Golgi
                     complex subunit 8; conserved oligomeric golgi complex
                     component 8; COG complex subunit 8"
                     /calculated_mol_wt=65516
     Region          50..364
                     /region_name="Dor1"
                     /note="Dor1-like family; pfam04124"
                     /db_xref="CDD:427729"
     Region          <528..567
                     /region_name="Def"
                     /note="Peptide deformylase [Translation, ribosomal
                     structure and biogenesis]; COG0242"
                     /db_xref="CDD:440012"
     CDS             1..579
                     /gene="COG8"
                     /gene_synonym="CDG2H; DOR1"
                     /coded_by="NM_001379265.1:13..1752"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:84342"
                     /db_xref="HGNC:HGNC:18623"
                     /db_xref="MIM:606979"
ORIGIN      
        1 mataatipsv atataaalge vedegllasl frdrfpeaqw rerpdvgryl relsgsgler
       61 lrreperlae eraqllqqtr dlafanyktf irgaecteri hrlfgdveas lgrlldrlps
      121 fqqscrnfvk eaeeissnrr mnsltlnrht eileileipq lmdtcvrnsy yeealelaay
      181 vrrlerkyss ipviqgivne vrqsmqlmls qliqqlrtni qlpaclrvig ylrrmdvfte
      241 aelrvkflqa rdawlrsilt aipnddpyfh itktieasrv hlfdiitqyr aifsdedpll
      301 ppamgehtvn esaifhgwvl qkvsqflqvl etdlyrgigg hldsllgqcm yfglsfsrvg
      361 adfrgqlapv fqrvaistfq kaiqetvekf qeemnsymli sapailgtsn mpaavpatqp
      421 gtlqppmvll dfpplacfln nilvafndlr lccpvalaqd vtgaledala kvtkiilafh
      481 raeeaafssg eqelfvqfct vfledlvpyl nrclqvlfpp aqiaqtlgld pngeqvvwqa
      541 sgwaariiqh emdhlqgclf idkmdsrtft nvywmkvnd
//
LOCUS       NP_001366193             612 aa            linear   PRI 14-DEC-2025
DEFINITION  conserved oligomeric Golgi complex subunit 8 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001366193
VERSION     NP_001366193.1
DBSOURCE    REFSEQ: accession NM_001379264.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Climer,L.K., Pokrovskaya,I.D., Blackburn,J.B. and Lupashin,V.V.
  TITLE     Membrane detachment is not essential for COG complex function
  JOURNAL   Mol Biol Cell 29 (8), 964-974 (2018)
   PUBMED   29467253
  REMARK    GeneRIF: TMEM-COG4, COG7 and COG8 subunits restore endogenous COG
            localization to the Golgi membranes
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Yang,A., Cho,S.Y., Jang,J.H., Kim,J., Kim,S.Z., Lee,B.H., Yoo,H.W.
            and Jin,D.K.
  TITLE     Further delineation of COG8-CDG: A case with novel compound
            heterozygous mutations diagnosed by targeted exome sequencing
  JOURNAL   Clin Chim Acta 471, 191-195 (2017)
   PUBMED   28619360
  REMARK    GeneRIF: The exome sequencing was performed to screen all CDG type
            II-related genes, and two novel frameshift mutations were found:
            c.171dupG (p.Leu58Alafs*29) and c.1656dupC (p.Ala553Argfs*15) in
            COG8.
REFERENCE   4  (residues 1 to 612)
  AUTHORS   Bailey Blackburn,J., Pokrovskaya,I., Fisher,P., Ungar,D. and
            Lupashin,V.V.
  TITLE     COG Complex Complexities: Detailed Characterization of a Complete
            Set of HEK293T Cells Lacking Individual COG Subunits
  JOURNAL   Front Cell Dev Biol 4, 23 (2016)
   PUBMED   27066481
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 612)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 612)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     The binary interacting network of the conserved oligomeric Golgi
            tethering complex
  JOURNAL   J Biol Chem 279 (23), 24640-24648 (2004)
   PUBMED   15047703
REFERENCE   7  (residues 1 to 612)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     Sec34 is implicated in traffic from the endoplasmic reticulum to
            the Golgi and exists in a complex with GTC-90 and ldlBp
  JOURNAL   J Biol Chem 277 (24), 21955-21961 (2002)
   PUBMED   11929878
REFERENCE   8  (residues 1 to 612)
  AUTHORS   Ungar,D., Oka,T., Brittle,E.E., Vasile,E., Lupashin,V.V.,
            Chatterton,J.E., Heuser,J.E., Krieger,M. and Waters,M.G.
  TITLE     Characterization of a mammalian Golgi-localized protein complex,
            COG, that is required for normal Golgi morphology and function
  JOURNAL   J Cell Biol 157 (3), 405-415 (2002)
   PUBMED   11980916
REFERENCE   9  (residues 1 to 612)
  AUTHORS   Whyte,J.R. and Munro,S.
  TITLE     The Sec34/35 Golgi transport complex is related to the exocyst,
            defining a family of complexes involved in multiple steps of
            membrane traffic
  JOURNAL   Dev Cell 1 (4), 527-537 (2001)
   PUBMED   11703943
REFERENCE   10 (residues 1 to 612)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026464.7.
            
            Summary: This gene encodes a protein that is a component of the
            conserved oligomeric Golgi (COG) complex, a multiprotein complex
            that plays a structural role in the Golgi apparatus, and is
            involved in intracellular membrane trafficking and glycoprotein
            modification. Mutations in this gene cause congenital disorder of
            glycosylation, type IIh, a disease that is characterized by
            under-glycosylated serum proteins, and whose symptoms include
            severe psychomotor retardation, failure to thrive, seizures, and
            dairy and wheat product intolerance. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803616.151947.1, SRR1803614.255256.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..612
                     /product="conserved oligomeric Golgi complex subunit 8
                     isoform 1"
                     /EC_number="3.5.1.88"
                     /note="dependent on RIC1; conserved oligomeric Golgi
                     complex subunit 8; conserved oligomeric golgi complex
                     component 8; COG complex subunit 8"
                     /calculated_mol_wt=68293
     Region          50..364
                     /region_name="Dor1"
                     /note="Dor1-like family; pfam04124"
                     /db_xref="CDD:427729"
     Region          568..612
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MW5.2)"
     CDS             1..612
                     /gene="COG8"
                     /gene_synonym="CDG2H; DOR1"
                     /coded_by="NM_001379264.1:13..1851"
                     /note="isoform 1 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS10876.1"
                     /db_xref="GeneID:84342"
                     /db_xref="HGNC:HGNC:18623"
                     /db_xref="MIM:606979"
ORIGIN      
        1 mataatipsv atataaalge vedegllasl frdrfpeaqw rerpdvgryl relsgsgler
       61 lrreperlae eraqllqqtr dlafanyktf irgaecteri hrlfgdveas lgrlldrlps
      121 fqqscrnfvk eaeeissnrr mnsltlnrht eileileipq lmdtcvrnsy yeealelaay
      181 vrrlerkyss ipviqgivne vrqsmqlmls qliqqlrtni qlpaclrvig ylrrmdvfte
      241 aelrvkflqa rdawlrsilt aipnddpyfh itktieasrv hlfdiitqyr aifsdedpll
      301 ppamgehtvn esaifhgwvl qkvsqflqvl etdlyrgigg hldsllgqcm yfglsfsrvg
      361 adfrgqlapv fqrvaistfq kaiqetvekf qeemnsymli sapailgtsn mpaavpatqp
      421 gtlqppmvll dfpplacfln nilvafndlr lccpvalaqd vtgaledala kvtkiilafh
      481 raeeaafssg eqelfvqfct vfledlvpyl nrclqvlfpp aqiaqtlgip ptqlskygnl
      541 ghvnigaiqe plafilpkre tlftlddqal gpeltapape ppaeeprlep agpacpeggr
      601 aetqaeppsv gp
//
LOCUS       NP_001366195             518 aa            linear   PRI 14-DEC-2025
DEFINITION  conserved oligomeric Golgi complex subunit 8 isoform 7 [Homo
            sapiens].
ACCESSION   NP_001366195
VERSION     NP_001366195.1
DBSOURCE    REFSEQ: accession NM_001379266.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Climer,L.K., Pokrovskaya,I.D., Blackburn,J.B. and Lupashin,V.V.
  TITLE     Membrane detachment is not essential for COG complex function
  JOURNAL   Mol Biol Cell 29 (8), 964-974 (2018)
   PUBMED   29467253
  REMARK    GeneRIF: TMEM-COG4, COG7 and COG8 subunits restore endogenous COG
            localization to the Golgi membranes
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Yang,A., Cho,S.Y., Jang,J.H., Kim,J., Kim,S.Z., Lee,B.H., Yoo,H.W.
            and Jin,D.K.
  TITLE     Further delineation of COG8-CDG: A case with novel compound
            heterozygous mutations diagnosed by targeted exome sequencing
  JOURNAL   Clin Chim Acta 471, 191-195 (2017)
   PUBMED   28619360
  REMARK    GeneRIF: The exome sequencing was performed to screen all CDG type
            II-related genes, and two novel frameshift mutations were found:
            c.171dupG (p.Leu58Alafs*29) and c.1656dupC (p.Ala553Argfs*15) in
            COG8.
REFERENCE   4  (residues 1 to 518)
  AUTHORS   Bailey Blackburn,J., Pokrovskaya,I., Fisher,P., Ungar,D. and
            Lupashin,V.V.
  TITLE     COG Complex Complexities: Detailed Characterization of a Complete
            Set of HEK293T Cells Lacking Individual COG Subunits
  JOURNAL   Front Cell Dev Biol 4, 23 (2016)
   PUBMED   27066481
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 518)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 518)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     The binary interacting network of the conserved oligomeric Golgi
            tethering complex
  JOURNAL   J Biol Chem 279 (23), 24640-24648 (2004)
   PUBMED   15047703
REFERENCE   7  (residues 1 to 518)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     Sec34 is implicated in traffic from the endoplasmic reticulum to
            the Golgi and exists in a complex with GTC-90 and ldlBp
  JOURNAL   J Biol Chem 277 (24), 21955-21961 (2002)
   PUBMED   11929878
REFERENCE   8  (residues 1 to 518)
  AUTHORS   Ungar,D., Oka,T., Brittle,E.E., Vasile,E., Lupashin,V.V.,
            Chatterton,J.E., Heuser,J.E., Krieger,M. and Waters,M.G.
  TITLE     Characterization of a mammalian Golgi-localized protein complex,
            COG, that is required for normal Golgi morphology and function
  JOURNAL   J Cell Biol 157 (3), 405-415 (2002)
   PUBMED   11980916
REFERENCE   9  (residues 1 to 518)
  AUTHORS   Whyte,J.R. and Munro,S.
  TITLE     The Sec34/35 Golgi transport complex is related to the exocyst,
            defining a family of complexes involved in multiple steps of
            membrane traffic
  JOURNAL   Dev Cell 1 (4), 527-537 (2001)
   PUBMED   11703943
REFERENCE   10 (residues 1 to 518)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026464.7.
            
            Summary: This gene encodes a protein that is a component of the
            conserved oligomeric Golgi (COG) complex, a multiprotein complex
            that plays a structural role in the Golgi apparatus, and is
            involved in intracellular membrane trafficking and glycoprotein
            modification. Mutations in this gene cause congenital disorder of
            glycosylation, type IIh, a disease that is characterized by
            under-glycosylated serum proteins, and whose symptoms include
            severe psychomotor retardation, failure to thrive, seizures, and
            dairy and wheat product intolerance. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.54719.1,
                                           SRR18074968.1747480.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142363, SAMEA2145774
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..518
                     /product="conserved oligomeric Golgi complex subunit 8
                     isoform 7"
                     /EC_number="3.5.1.88"
                     /note="dependent on RIC1; conserved oligomeric Golgi
                     complex subunit 8; conserved oligomeric golgi complex
                     component 8; COG complex subunit 8"
                     /calculated_mol_wt=58267
     Region          50..364
                     /region_name="Dor1"
                     /note="Dor1-like family; pfam04124"
                     /db_xref="CDD:427729"
     CDS             1..518
                     /gene="COG8"
                     /gene_synonym="CDG2H; DOR1"
                     /coded_by="NM_001379266.1:13..1569"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:84342"
                     /db_xref="HGNC:HGNC:18623"
                     /db_xref="MIM:606979"
ORIGIN      
        1 mataatipsv atataaalge vedegllasl frdrfpeaqw rerpdvgryl relsgsgler
       61 lrreperlae eraqllqqtr dlafanyktf irgaecteri hrlfgdveas lgrlldrlps
      121 fqqscrnfvk eaeeissnrr mnsltlnrht eileileipq lmdtcvrnsy yeealelaay
      181 vrrlerkyss ipviqgivne vrqsmqlmls qliqqlrtni qlpaclrvig ylrrmdvfte
      241 aelrvkflqa rdawlrsilt aipnddpyfh itktieasrv hlfdiitqyr aifsdedpll
      301 ppamgehtvn esaifhgwvl qkvsqflqvl etdlyrgigg hldsllgqcm yfglsfsrvg
      361 adfrgqlapv fqrvaistfq kaiqetvekf qeemnsymli sapailgtsn mpaavpatqp
      421 gtlqppmvll dfpplacfln nilvafndlr lccpvalaqd vtgaledala kgwtpmenrw
      481 cgrraggqpa ssstrwttcr aaclltkwta grsqtsig
//
LOCUS       NP_001350083             865 aa            linear   PRI 15-DEC-2025
DEFINITION  TBC1 domain family member 31 isoform 10 [Homo sapiens].
ACCESSION   NP_001350083 XP_016869478
VERSION     NP_001350083.1
DBSOURCE    REFSEQ: accession NM_001363154.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 865)
  AUTHORS   Cao,P., Chen,H., Zhang,Y., Zhang,Q., Shi,M., Han,H., Wang,X.,
            Jin,L., Guo,B., Hao,R., Zhao,X., Li,Y., Gao,C., Liu,X., Wang,Y.,
            Yang,A., Yang,C., Si,A., Li,H., Song,Q., He,F. and Zhou,G.
  TITLE     Genomic Amplification of TBC1D31 Promotes Hepatocellular Carcinoma
            Through Reducing the Rab22A-Mediated Endolysosomal Trafficking and
            Degradation of EGFR
  JOURNAL   Adv Sci (Weinh) 11 (40), e2405459 (2024)
   PUBMED   39206796
  REMARK    GeneRIF: Genomic Amplification of TBC1D31 Promotes Hepatocellular
            Carcinoma Through Reducing the Rab22A-Mediated Endolysosomal
            Trafficking and Degradation of EGFR.
REFERENCE   2  (residues 1 to 865)
  AUTHORS   Saygili,S., Kosukcu,C., Bastug,T., Dogan,O.A., Yilmaz,E.K.,
            Kalyoncu,A.U., Agbas,A., Canpolat,N., Caliskan,S. and Ozaltin,F.
  TITLE     A novel homozygous missense variant in TBC1D31 in a consanguineous
            family with congenital anomalies of the kidney and urinary tract
            (CAKUT)
  JOURNAL   Clin Genet 104 (6), 679-685 (2023)
   PUBMED   37468454
  REMARK    GeneRIF: A novel homozygous missense variant in TBC1D31 in a
            consanguineous family with congenital anomalies of the kidney and
            urinary tract (CAKUT).
REFERENCE   3  (residues 1 to 865)
  AUTHORS   Senatore,E., Chiuso,F., Rinaldi,L., Intartaglia,D., Delle Donne,R.,
            Pedone,E., Catalanotti,B., Pirone,L., Fiorillo,B., Moraca,F.,
            Giamundo,G., Scala,G., Raffeiner,A., Torres-Quesada,O., Stefan,E.,
            Kwiatkowski,M., van Pijkeren,A., Morleo,M., Franco,B., Garbi,C.,
            Conte,I. and Feliciello,A.
  TITLE     The TBC1D31/praja2 complex controls primary ciliogenesis through
            PKA-directed OFD1 ubiquitylation
  JOURNAL   EMBO J 40 (10), e106503 (2021)
   PUBMED   33934390
REFERENCE   4  (residues 1 to 865)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   5  (residues 1 to 865)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100873.2.
            
            On May 9, 2018 this sequence version replaced XP_016869478.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.82878.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2152798, SAMEA2153031
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..865
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..865
                     /product="TBC1 domain family member 31 isoform 10"
                     /note="WD repeat-containing protein 67; WD repeat domain
                     67"
                     /calculated_mol_wt=100879
     Region          <10..235
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          25..60
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          66..102
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          108..148
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          156..196
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          204..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          357..500
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; cl46302"
                     /db_xref="CDD:480642"
     Region          <585..>749
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     Region          <656..846
                     /region_name="Nup88"
                     /note="Nuclear pore component; pfam10168"
                     /db_xref="CDD:462975"
     CDS             1..865
                     /gene="TBC1D31"
                     /gene_synonym="Gm85; WDR67"
                     /coded_by="NM_001363154.1:263..2860"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:93594"
                     /db_xref="HGNC:HGNC:30888"
                     /db_xref="MIM:621444"
ORIGIN      
        1 mfltymetvt kelvswmrgh essvfsisvh asgkyaitts sdtaqlwdld tfqrkrklni
       61 rqsvgiqkvf flplsntils cfkdnsifaw ecdtlfckyq lpappesssi lykvfavtrd
      121 grilaaggks nhlhlwclea rqlfriiqmp tkvrairhle flpdsfdags nqvlgvlsqd
      181 gimrfinmqt ckllfeigsl degisssais phgryiasim engslniysv qaltqeinkp
      241 ppplvkvied lpknklsssd lkmkvtsgrv qqpaksresk mqtrilkqdl tgdfeskkne
      301 lpdglnkkrl qillkgygey ptkyrmfiwr sllqlpenht afstlidkgt hvaflnlqkk
      361 ypiksrkllr vlqrtlsala hwsvifsdtp ylpllafpfv klfqnnqlic feviatliin
      421 wcqhwfeyfp nppinilsmi envlafhdke llqhfidhdi tsqlyawpll etvfsevltr
      481 eewlklfdni fsnhpsfllm tvvaynicsr tpllscnlkd dfefffhhrn nldinvvirq
      541 vyhlmettpt dihpdsmlnv fvaltkgqyp vfnqypkfiv dyqtqereri rndeldylre
      601 rqtvedmqak vdqqrvedea wyqkqellrk aeetrremll qeeekmiqqr qrlaavkrel
      661 kvkemhlqda arrrflklqq dqqemelrrl ddeigrknlt enqealakem radadayrrk
      721 vdleehmfhk lieagetqsq ktqkwkeaeg kefrlrsakk asalsdasrk wflkqeinaa
      781 vehaenpchk eeprfqneqd ssclprtsql ndssemdpst qislnrrave wdttgqnlik
      841 kvrnlrqrlt ararhrcqtp hllaa
//
LOCUS       NP_001350078            1056 aa            linear   PRI 15-DEC-2025
DEFINITION  TBC1 domain family member 31 isoform 5 [Homo sapiens].
ACCESSION   NP_001350078 XP_011515680
VERSION     NP_001350078.1
DBSOURCE    REFSEQ: accession NM_001363149.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Cao,P., Chen,H., Zhang,Y., Zhang,Q., Shi,M., Han,H., Wang,X.,
            Jin,L., Guo,B., Hao,R., Zhao,X., Li,Y., Gao,C., Liu,X., Wang,Y.,
            Yang,A., Yang,C., Si,A., Li,H., Song,Q., He,F. and Zhou,G.
  TITLE     Genomic Amplification of TBC1D31 Promotes Hepatocellular Carcinoma
            Through Reducing the Rab22A-Mediated Endolysosomal Trafficking and
            Degradation of EGFR
  JOURNAL   Adv Sci (Weinh) 11 (40), e2405459 (2024)
   PUBMED   39206796
  REMARK    GeneRIF: Genomic Amplification of TBC1D31 Promotes Hepatocellular
            Carcinoma Through Reducing the Rab22A-Mediated Endolysosomal
            Trafficking and Degradation of EGFR.
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Saygili,S., Kosukcu,C., Bastug,T., Dogan,O.A., Yilmaz,E.K.,
            Kalyoncu,A.U., Agbas,A., Canpolat,N., Caliskan,S. and Ozaltin,F.
  TITLE     A novel homozygous missense variant in TBC1D31 in a consanguineous
            family with congenital anomalies of the kidney and urinary tract
            (CAKUT)
  JOURNAL   Clin Genet 104 (6), 679-685 (2023)
   PUBMED   37468454
  REMARK    GeneRIF: A novel homozygous missense variant in TBC1D31 in a
            consanguineous family with congenital anomalies of the kidney and
            urinary tract (CAKUT).
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Senatore,E., Chiuso,F., Rinaldi,L., Intartaglia,D., Delle Donne,R.,
            Pedone,E., Catalanotti,B., Pirone,L., Fiorillo,B., Moraca,F.,
            Giamundo,G., Scala,G., Raffeiner,A., Torres-Quesada,O., Stefan,E.,
            Kwiatkowski,M., van Pijkeren,A., Morleo,M., Franco,B., Garbi,C.,
            Conte,I. and Feliciello,A.
  TITLE     The TBC1D31/praja2 complex controls primary ciliogenesis through
            PKA-directed OFD1 ubiquitylation
  JOURNAL   EMBO J 40 (10), e106503 (2021)
   PUBMED   33934390
REFERENCE   4  (residues 1 to 1056)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   5  (residues 1 to 1056)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BQ436515.1 and AC100873.2.
            
            On May 9, 2018 this sequence version replaced XP_011515680.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.122398.1,
                                           SRR7346977.1957122.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..1056
                     /product="TBC1 domain family member 31 isoform 5"
                     /note="WD repeat-containing protein 67; WD repeat domain
                     67"
                     /calculated_mol_wt=122999
     Region          34..330
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          36..71
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          76..113
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          120..154
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          161..197
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          205..243
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          251..281
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          299..325
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          452..595
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; cl46302"
                     /db_xref="CDD:480642"
     Region          <674..>952
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     CDS             1..1056
                     /gene="TBC1D31"
                     /gene_synonym="Gm85; WDR67"
                     /coded_by="NM_001363149.1:137..3307"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:93594"
                     /db_xref="HGNC:HGNC:30888"
                     /db_xref="MIM:621444"
ORIGIN      
        1 meqntlpvlw slhigviivn iihntsdyhp kvlrflnvaf dgtgdcliag dhqgniyvfd
       61 lhgnrfnlvq rtaqactala fnlrrksefl valadysikc fdtvtkelvs wmrghessvf
      121 sisvhasgky aittssdtaq lwdldtfqrk rklnirqsvg iqkvfflpls ntilscfkdn
      181 sifawecdtl fckyqlpapp esssilykvf avtrdgrila aggksnhlhl wclearqlfr
      241 iiqmptkvra irhleflpds fdagsnqvlg vlsqdgimrf inmqtckllf eigsldegis
      301 ssaisphgry iasimengsl niysvqaltq einkpppplv kviedlpknk lsssdlkmkv
      361 tsgrvqqpak sreskmqtri lkqdltgdfe skknelpdgl nkkrlqillk gygeyptkyr
      421 mfiwrsllql penhtafstl idkgthvafl nlqkkypiks rkllrvlqrt lsalahwsvi
      481 fsdtpylpll afpfvklfqn nqlicfevia tliinwcqhw feyfpnppin ilsmienvla
      541 fhdkellqhf idhditsqly awplletvfs evltreewlk lfdnifsnhp sfllmtvvay
      601 nicsrtplls cnlkddfeff fhhrnnldin vvirqvyhlm ettptdihpd smlnvfvalt
      661 kgqypvfnqy pkfivdyqtq ererirndel dylrerqtve dmqakvdqqr vedeawyqkq
      721 ellrkaeetr remllqeeek miqqrqrlaa vkrelkvkem hlqdaarrrf lklqqdqqem
      781 elrrlddeig rkvymrdrei aatardlemr qlelesqkrl yeknltenqe alakemrada
      841 dayrrkvdle ehmfhkliea getqsqktqk vikenlakae qaclntdwqi qslhkqkcdd
      901 lqrnkcyqev akllrenrrk eieiinamve eeakkwkeae gkefrlrsak kasalsdasr
      961 kwflkqeina avehaenpch keeprfqneq dssclprtsq lndssemdps tqislnrrav
     1021 ewdttgqnli kkvrnlrqrl tararhrcqt phllaa
//
LOCUS       NP_001350077            1001 aa            linear   PRI 15-DEC-2025
DEFINITION  TBC1 domain family member 31 isoform 4 [Homo sapiens].
ACCESSION   NP_001350077 XP_005251160
VERSION     NP_001350077.1
DBSOURCE    REFSEQ: accession NM_001363148.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1001)
  AUTHORS   Cao,P., Chen,H., Zhang,Y., Zhang,Q., Shi,M., Han,H., Wang,X.,
            Jin,L., Guo,B., Hao,R., Zhao,X., Li,Y., Gao,C., Liu,X., Wang,Y.,
            Yang,A., Yang,C., Si,A., Li,H., Song,Q., He,F. and Zhou,G.
  TITLE     Genomic Amplification of TBC1D31 Promotes Hepatocellular Carcinoma
            Through Reducing the Rab22A-Mediated Endolysosomal Trafficking and
            Degradation of EGFR
  JOURNAL   Adv Sci (Weinh) 11 (40), e2405459 (2024)
   PUBMED   39206796
  REMARK    GeneRIF: Genomic Amplification of TBC1D31 Promotes Hepatocellular
            Carcinoma Through Reducing the Rab22A-Mediated Endolysosomal
            Trafficking and Degradation of EGFR.
REFERENCE   2  (residues 1 to 1001)
  AUTHORS   Saygili,S., Kosukcu,C., Bastug,T., Dogan,O.A., Yilmaz,E.K.,
            Kalyoncu,A.U., Agbas,A., Canpolat,N., Caliskan,S. and Ozaltin,F.
  TITLE     A novel homozygous missense variant in TBC1D31 in a consanguineous
            family with congenital anomalies of the kidney and urinary tract
            (CAKUT)
  JOURNAL   Clin Genet 104 (6), 679-685 (2023)
   PUBMED   37468454
  REMARK    GeneRIF: A novel homozygous missense variant in TBC1D31 in a
            consanguineous family with congenital anomalies of the kidney and
            urinary tract (CAKUT).
REFERENCE   3  (residues 1 to 1001)
  AUTHORS   Senatore,E., Chiuso,F., Rinaldi,L., Intartaglia,D., Delle Donne,R.,
            Pedone,E., Catalanotti,B., Pirone,L., Fiorillo,B., Moraca,F.,
            Giamundo,G., Scala,G., Raffeiner,A., Torres-Quesada,O., Stefan,E.,
            Kwiatkowski,M., van Pijkeren,A., Morleo,M., Franco,B., Garbi,C.,
            Conte,I. and Feliciello,A.
  TITLE     The TBC1D31/praja2 complex controls primary ciliogenesis through
            PKA-directed OFD1 ubiquitylation
  JOURNAL   EMBO J 40 (10), e106503 (2021)
   PUBMED   33934390
REFERENCE   4  (residues 1 to 1001)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   5  (residues 1 to 1001)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100873.2.
            
            On May 9, 2018 this sequence version replaced XP_005251160.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1001
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..1001
                     /product="TBC1 domain family member 31 isoform 4"
                     /note="WD repeat-containing protein 67; WD repeat domain
                     67"
                     /calculated_mol_wt=116350
     Region          44..340
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          46..81
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          86..123
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          130..164
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          171..207
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          215..253
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          261..291
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          309..335
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          462..605
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; cl46302"
                     /db_xref="CDD:480642"
     Region          <684..>992
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     CDS             1..1001
                     /gene="TBC1D31"
                     /gene_synonym="Gm85; WDR67"
                     /coded_by="NM_001363148.1:64..3069"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:93594"
                     /db_xref="HGNC:HGNC:30888"
                     /db_xref="MIM:621444"
ORIGIN      
        1 mqstdlgnke sgkiwhrkps patrdgiivn iihntsdyhp kvlrflnvaf dgtgdcliag
       61 dhqgniyvfd lhgnrfnlvq rtaqactala fnlrrksefl valadysikc fdtvtkelvs
      121 wmrghessvf sisvhasgky aittssdtaq lwdldtfqrk rklnirqsvg iqkvfflpls
      181 ntilscfkdn sifawecdtl fckyqlpapp esssilykvf avtrdgrila aggksnhlhl
      241 wclearqlfr iiqmptkvra irhleflpds fdagsnqvlg vlsqdgimrf inmqtckllf
      301 eigsldegis ssaisphgry iasimengsl niysvqaltq einkpppplv kviedlpknk
      361 lsssdlkmkv tsgrvqqpak sreskmqtri lkqdltgdfe skknelpdgl nkkrlqillk
      421 gygeyptkyr mfiwrsllql penhtafstl idkgthvafl nlqkkypiks rkllrvlqrt
      481 lsalahwsvi fsdtpylpll afpfvklfqn nqlicfevia tliinwcqhw feyfpnppin
      541 ilsmienvla fhdkellqhf idhditsqly awplletvfs evltreewlk lfdnifsnhp
      601 sfllmtvvay nicsrtplls cnlkddfeff fhhrnnldin vvirqvyhlm ettptdihpd
      661 smlnvfvalt kgqypvfnqy pkfivdyqtq ererirndel dylrerqtve dmqakvdqqr
      721 vedeawyqkq ellrkaeetr remllqeeek miqqrqrlaa vkrelkvkem hlqdaarrrf
      781 lklqqdqqem elrrlddeig rkvymrdrei aatardlemr qlelesqkrl yeknltenqe
      841 alakemrada dayrrkvdle ehmfhkliea getqsqktqk wkeaegkefr lrsakkasal
      901 sdasrkwflk qeinaaveha enpchkeepr fqneqdsscl prtsqlndss emdpstqisl
      961 nrravewdtt gqnlikkvrn lrqrltarar hrcqtphlla a
//
LOCUS       NP_001350079            1035 aa            linear   PRI 15-DEC-2025
DEFINITION  TBC1 domain family member 31 isoform 6 [Homo sapiens].
ACCESSION   NP_001350079 XP_005251159
VERSION     NP_001350079.1
DBSOURCE    REFSEQ: accession NM_001363150.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Cao,P., Chen,H., Zhang,Y., Zhang,Q., Shi,M., Han,H., Wang,X.,
            Jin,L., Guo,B., Hao,R., Zhao,X., Li,Y., Gao,C., Liu,X., Wang,Y.,
            Yang,A., Yang,C., Si,A., Li,H., Song,Q., He,F. and Zhou,G.
  TITLE     Genomic Amplification of TBC1D31 Promotes Hepatocellular Carcinoma
            Through Reducing the Rab22A-Mediated Endolysosomal Trafficking and
            Degradation of EGFR
  JOURNAL   Adv Sci (Weinh) 11 (40), e2405459 (2024)
   PUBMED   39206796
  REMARK    GeneRIF: Genomic Amplification of TBC1D31 Promotes Hepatocellular
            Carcinoma Through Reducing the Rab22A-Mediated Endolysosomal
            Trafficking and Degradation of EGFR.
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Saygili,S., Kosukcu,C., Bastug,T., Dogan,O.A., Yilmaz,E.K.,
            Kalyoncu,A.U., Agbas,A., Canpolat,N., Caliskan,S. and Ozaltin,F.
  TITLE     A novel homozygous missense variant in TBC1D31 in a consanguineous
            family with congenital anomalies of the kidney and urinary tract
            (CAKUT)
  JOURNAL   Clin Genet 104 (6), 679-685 (2023)
   PUBMED   37468454
  REMARK    GeneRIF: A novel homozygous missense variant in TBC1D31 in a
            consanguineous family with congenital anomalies of the kidney and
            urinary tract (CAKUT).
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Senatore,E., Chiuso,F., Rinaldi,L., Intartaglia,D., Delle Donne,R.,
            Pedone,E., Catalanotti,B., Pirone,L., Fiorillo,B., Moraca,F.,
            Giamundo,G., Scala,G., Raffeiner,A., Torres-Quesada,O., Stefan,E.,
            Kwiatkowski,M., van Pijkeren,A., Morleo,M., Franco,B., Garbi,C.,
            Conte,I. and Feliciello,A.
  TITLE     The TBC1D31/praja2 complex controls primary ciliogenesis through
            PKA-directed OFD1 ubiquitylation
  JOURNAL   EMBO J 40 (10), e106503 (2021)
   PUBMED   33934390
REFERENCE   4  (residues 1 to 1035)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   5  (residues 1 to 1035)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100873.2.
            
            On May 9, 2018 this sequence version replaced XP_005251159.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.82133.1,
                                           SRR1660805.36036.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..1035
                     /product="TBC1 domain family member 31 isoform 6"
                     /note="WD repeat-containing protein 67; WD repeat domain
                     67"
                     /calculated_mol_wt=120234
     Region          44..340
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          46..81
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          86..123
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          130..164
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          171..207
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          215..253
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          261..291
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          309..335
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          462..605
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; cl46302"
                     /db_xref="CDD:480642"
     Region          <684..>1026
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     CDS             1..1035
                     /gene="TBC1D31"
                     /gene_synonym="Gm85; WDR67"
                     /coded_by="NM_001363150.1:64..3171"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:93594"
                     /db_xref="HGNC:HGNC:30888"
                     /db_xref="MIM:621444"
ORIGIN      
        1 mqstdlgnke sgkiwhrkps patrdgiivn iihntsdyhp kvlrflnvaf dgtgdcliag
       61 dhqgniyvfd lhgnrfnlvq rtaqactala fnlrrksefl valadysikc fdtvtkelvs
      121 wmrghessvf sisvhasgky aittssdtaq lwdldtfqrk rklnirqsvg iqkvfflpls
      181 ntilscfkdn sifawecdtl fckyqlpapp esssilykvf avtrdgrila aggksnhlhl
      241 wclearqlfr iiqmptkvra irhleflpds fdagsnqvlg vlsqdgimrf inmqtckllf
      301 eigsldegis ssaisphgry iasimengsl niysvqaltq einkpppplv kviedlpknk
      361 lsssdlkmkv tsgrvqqpak sreskmqtri lkqdltgdfe skknelpdgl nkkrlqillk
      421 gygeyptkyr mfiwrsllql penhtafstl idkgthvafl nlqkkypiks rkllrvlqrt
      481 lsalahwsvi fsdtpylpll afpfvklfqn nqlicfevia tliinwcqhw feyfpnppin
      541 ilsmienvla fhdkellqhf idhditsqly awplletvfs evltreewlk lfdnifsnhp
      601 sfllmtvvay nicsrtplls cnlkddfeff fhhrnnldin vvirqvyhlm ettptdihpd
      661 smlnvfvalt kgqypvfnqy pkfivdyqtq ererirndel dylrerqtve dmqakvdqqr
      721 vedeawyqkq ellrkaeetr remllqeeek miqqrqrlaa vkrelkvkem hlqdaarrrf
      781 lklqqdqqem elrrlddeig rknltenqea lakemradad ayrrkvdlee hmfhklieag
      841 etqsqktqkv ikenlakaeq aclntdwqiq slhkqkcddl qrnkcyqeva kllrenrrke
      901 ieiinamvee eakkwkeaeg kefrlrsakk asalsdasrk wflkqeinaa vehaenpchk
      961 eeprfqneqd ssclprtsql ndssemdpst qislnrrave wdttgqnlik kvrnlrqrlt
     1021 ararhrcqtp hllaa
//
LOCUS       NP_001350084             896 aa            linear   PRI 15-DEC-2025
DEFINITION  TBC1 domain family member 31 isoform 11 [Homo sapiens].
ACCESSION   NP_001350084 XP_016869477
VERSION     NP_001350084.1
DBSOURCE    REFSEQ: accession NM_001363155.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 896)
  AUTHORS   Cao,P., Chen,H., Zhang,Y., Zhang,Q., Shi,M., Han,H., Wang,X.,
            Jin,L., Guo,B., Hao,R., Zhao,X., Li,Y., Gao,C., Liu,X., Wang,Y.,
            Yang,A., Yang,C., Si,A., Li,H., Song,Q., He,F. and Zhou,G.
  TITLE     Genomic Amplification of TBC1D31 Promotes Hepatocellular Carcinoma
            Through Reducing the Rab22A-Mediated Endolysosomal Trafficking and
            Degradation of EGFR
  JOURNAL   Adv Sci (Weinh) 11 (40), e2405459 (2024)
   PUBMED   39206796
  REMARK    GeneRIF: Genomic Amplification of TBC1D31 Promotes Hepatocellular
            Carcinoma Through Reducing the Rab22A-Mediated Endolysosomal
            Trafficking and Degradation of EGFR.
REFERENCE   2  (residues 1 to 896)
  AUTHORS   Saygili,S., Kosukcu,C., Bastug,T., Dogan,O.A., Yilmaz,E.K.,
            Kalyoncu,A.U., Agbas,A., Canpolat,N., Caliskan,S. and Ozaltin,F.
  TITLE     A novel homozygous missense variant in TBC1D31 in a consanguineous
            family with congenital anomalies of the kidney and urinary tract
            (CAKUT)
  JOURNAL   Clin Genet 104 (6), 679-685 (2023)
   PUBMED   37468454
  REMARK    GeneRIF: A novel homozygous missense variant in TBC1D31 in a
            consanguineous family with congenital anomalies of the kidney and
            urinary tract (CAKUT).
REFERENCE   3  (residues 1 to 896)
  AUTHORS   Senatore,E., Chiuso,F., Rinaldi,L., Intartaglia,D., Delle Donne,R.,
            Pedone,E., Catalanotti,B., Pirone,L., Fiorillo,B., Moraca,F.,
            Giamundo,G., Scala,G., Raffeiner,A., Torres-Quesada,O., Stefan,E.,
            Kwiatkowski,M., van Pijkeren,A., Morleo,M., Franco,B., Garbi,C.,
            Conte,I. and Feliciello,A.
  TITLE     The TBC1D31/praja2 complex controls primary ciliogenesis through
            PKA-directed OFD1 ubiquitylation
  JOURNAL   EMBO J 40 (10), e106503 (2021)
   PUBMED   33934390
REFERENCE   4  (residues 1 to 896)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   5  (residues 1 to 896)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100873.2.
            
            On May 9, 2018 this sequence version replaced XP_016869477.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.119454.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..896
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..896
                     /product="TBC1 domain family member 31 isoform 11"
                     /note="WD repeat-containing protein 67; WD repeat domain
                     67"
                     /calculated_mol_wt=104704
     Region          <10..235
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          25..60
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          66..102
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          108..148
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          156..196
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          204..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          357..500
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; cl46302"
                     /db_xref="CDD:480642"
     Region          <583..>811
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..896
                     /gene="TBC1D31"
                     /gene_synonym="Gm85; WDR67"
                     /coded_by="NM_001363155.1:263..2953"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:93594"
                     /db_xref="HGNC:HGNC:30888"
                     /db_xref="MIM:621444"
ORIGIN      
        1 mfltymetvt kelvswmrgh essvfsisvh asgkyaitts sdtaqlwdld tfqrkrklni
       61 rqsvgiqkvf flplsntils cfkdnsifaw ecdtlfckyq lpappesssi lykvfavtrd
      121 grilaaggks nhlhlwclea rqlfriiqmp tkvrairhle flpdsfdags nqvlgvlsqd
      181 gimrfinmqt ckllfeigsl degisssais phgryiasim engslniysv qaltqeinkp
      241 ppplvkvied lpknklsssd lkmkvtsgrv qqpaksresk mqtrilkqdl tgdfeskkne
      301 lpdglnkkrl qillkgygey ptkyrmfiwr sllqlpenht afstlidkgt hvaflnlqkk
      361 ypiksrkllr vlqrtlsala hwsvifsdtp ylpllafpfv klfqnnqlic feviatliin
      421 wcqhwfeyfp nppinilsmi envlafhdke llqhfidhdi tsqlyawpll etvfsevltr
      481 eewlklfdni fsnhpsfllm tvvaynicsr tpllscnlkd dfefffhhrn nldinvvirq
      541 vyhlmettpt dihpdsmlnv fvaltkgqyp vfnqypkfiv dyqtqereri rndeldylre
      601 rqtvedmqak vdqqrvedea wyqkqellrk aeetrremll qeeekmiqqr qrlaavkrel
      661 kvkemhlqda arrrflklqq dqqemelrrl ddeigrkvym rdreiaatar dlemrqlele
      721 sqkrlyeknl tenqealake mradadayrr kvdleehmfh klieagetqs qktqkwkeae
      781 gkefrlrsak kasalsdasr kwflkqeina avehaenpch keeprfqneq dssclprtsq
      841 lndssemdps tqislnrrav ewdttgqnli kkvrnlrqrl tararhrcqt phllaa
//
LOCUS       NP_001350082             922 aa            linear   PRI 15-DEC-2025
DEFINITION  TBC1 domain family member 31 isoform 9 [Homo sapiens].
ACCESSION   NP_001350082 XP_016869476
VERSION     NP_001350082.1
DBSOURCE    REFSEQ: accession NM_001363153.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 922)
  AUTHORS   Cao,P., Chen,H., Zhang,Y., Zhang,Q., Shi,M., Han,H., Wang,X.,
            Jin,L., Guo,B., Hao,R., Zhao,X., Li,Y., Gao,C., Liu,X., Wang,Y.,
            Yang,A., Yang,C., Si,A., Li,H., Song,Q., He,F. and Zhou,G.
  TITLE     Genomic Amplification of TBC1D31 Promotes Hepatocellular Carcinoma
            Through Reducing the Rab22A-Mediated Endolysosomal Trafficking and
            Degradation of EGFR
  JOURNAL   Adv Sci (Weinh) 11 (40), e2405459 (2024)
   PUBMED   39206796
  REMARK    GeneRIF: Genomic Amplification of TBC1D31 Promotes Hepatocellular
            Carcinoma Through Reducing the Rab22A-Mediated Endolysosomal
            Trafficking and Degradation of EGFR.
REFERENCE   2  (residues 1 to 922)
  AUTHORS   Saygili,S., Kosukcu,C., Bastug,T., Dogan,O.A., Yilmaz,E.K.,
            Kalyoncu,A.U., Agbas,A., Canpolat,N., Caliskan,S. and Ozaltin,F.
  TITLE     A novel homozygous missense variant in TBC1D31 in a consanguineous
            family with congenital anomalies of the kidney and urinary tract
            (CAKUT)
  JOURNAL   Clin Genet 104 (6), 679-685 (2023)
   PUBMED   37468454
  REMARK    GeneRIF: A novel homozygous missense variant in TBC1D31 in a
            consanguineous family with congenital anomalies of the kidney and
            urinary tract (CAKUT).
REFERENCE   3  (residues 1 to 922)
  AUTHORS   Senatore,E., Chiuso,F., Rinaldi,L., Intartaglia,D., Delle Donne,R.,
            Pedone,E., Catalanotti,B., Pirone,L., Fiorillo,B., Moraca,F.,
            Giamundo,G., Scala,G., Raffeiner,A., Torres-Quesada,O., Stefan,E.,
            Kwiatkowski,M., van Pijkeren,A., Morleo,M., Franco,B., Garbi,C.,
            Conte,I. and Feliciello,A.
  TITLE     The TBC1D31/praja2 complex controls primary ciliogenesis through
            PKA-directed OFD1 ubiquitylation
  JOURNAL   EMBO J 40 (10), e106503 (2021)
   PUBMED   33934390
REFERENCE   4  (residues 1 to 922)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   5  (residues 1 to 922)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100873.2.
            
            On May 9, 2018 this sequence version replaced XP_016869476.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..922
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..922
                     /product="TBC1 domain family member 31 isoform 9"
                     /note="WD repeat-containing protein 67; WD repeat domain
                     67"
                     /calculated_mol_wt=106653
     Region          44..340
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          46..81
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          86..123
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          130..164
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          171..207
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          215..253
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          261..291
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          309..335
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          462..605
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; cl46302"
                     /db_xref="CDD:480642"
     Region          <624..>913
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     CDS             1..922
                     /gene="TBC1D31"
                     /gene_synonym="Gm85; WDR67"
                     /coded_by="NM_001363153.1:64..2832"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:93594"
                     /db_xref="HGNC:HGNC:30888"
                     /db_xref="MIM:621444"
ORIGIN      
        1 mqstdlgnke sgkiwhrkps patrdgiivn iihntsdyhp kvlrflnvaf dgtgdcliag
       61 dhqgniyvfd lhgnrfnlvq rtaqactala fnlrrksefl valadysikc fdtvtkelvs
      121 wmrghessvf sisvhasgky aittssdtaq lwdldtfqrk rklnirqsvg iqkvfflpls
      181 ntilscfkdn sifawecdtl fckyqlpapp esssilykvf avtrdgrila aggksnhlhl
      241 wclearqlfr iiqmptkvra irhleflpds fdagsnqvlg vlsqdgimrf inmqtckllf
      301 eigsldegis ssaisphgry iasimengsl niysvqaltq einkpppplv kviedlpknk
      361 lsssdlkmkv tsgrvqqpak sreskmqtri lkqdltgdfe skknelpdgl nkkrlqillk
      421 gygeyptkyr mfiwrsllql penhtafstl idkgthvafl nlqkkypiks rkllrvlqrt
      481 lsalahwsvi fsdtpylpll afpfvklfqn nqlicfevia tliinwcqhw feyfpnppin
      541 ilsmienvla fhdkellqhf idhditsqly awplletvfs evltreewlk lfdnifsnhp
      601 sfllmtvvay nicsrtplls cnlkddfetv edmqakvdqq rvedeawyqk qellrkaeet
      661 rremllqeee kmiqqrqrla avkrelkvke mhlqdaarrr flklqqdqqe melrrlddei
      721 grkvymrdre iaatardlem rqlelesqkr lyeknltenq ealakemrad adayrrkvdl
      781 eehmfhklie agetqsqktq kwkeaegkef rlrsakkasa lsdasrkwfl kqeinaaveh
      841 aenpchkeep rfqneqdssc lprtsqlnds semdpstqis lnrravewdt tgqnlikkvr
      901 nlrqrltara rhrcqtphll aa
//
LOCUS       NP_001350085             566 aa            linear   PRI 15-DEC-2025
DEFINITION  TBC1 domain family member 31 isoform 12 [Homo sapiens].
ACCESSION   NP_001350085 XP_016869479
VERSION     NP_001350085.1
DBSOURCE    REFSEQ: accession NM_001363156.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Cao,P., Chen,H., Zhang,Y., Zhang,Q., Shi,M., Han,H., Wang,X.,
            Jin,L., Guo,B., Hao,R., Zhao,X., Li,Y., Gao,C., Liu,X., Wang,Y.,
            Yang,A., Yang,C., Si,A., Li,H., Song,Q., He,F. and Zhou,G.
  TITLE     Genomic Amplification of TBC1D31 Promotes Hepatocellular Carcinoma
            Through Reducing the Rab22A-Mediated Endolysosomal Trafficking and
            Degradation of EGFR
  JOURNAL   Adv Sci (Weinh) 11 (40), e2405459 (2024)
   PUBMED   39206796
  REMARK    GeneRIF: Genomic Amplification of TBC1D31 Promotes Hepatocellular
            Carcinoma Through Reducing the Rab22A-Mediated Endolysosomal
            Trafficking and Degradation of EGFR.
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Saygili,S., Kosukcu,C., Bastug,T., Dogan,O.A., Yilmaz,E.K.,
            Kalyoncu,A.U., Agbas,A., Canpolat,N., Caliskan,S. and Ozaltin,F.
  TITLE     A novel homozygous missense variant in TBC1D31 in a consanguineous
            family with congenital anomalies of the kidney and urinary tract
            (CAKUT)
  JOURNAL   Clin Genet 104 (6), 679-685 (2023)
   PUBMED   37468454
  REMARK    GeneRIF: A novel homozygous missense variant in TBC1D31 in a
            consanguineous family with congenital anomalies of the kidney and
            urinary tract (CAKUT).
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Senatore,E., Chiuso,F., Rinaldi,L., Intartaglia,D., Delle Donne,R.,
            Pedone,E., Catalanotti,B., Pirone,L., Fiorillo,B., Moraca,F.,
            Giamundo,G., Scala,G., Raffeiner,A., Torres-Quesada,O., Stefan,E.,
            Kwiatkowski,M., van Pijkeren,A., Morleo,M., Franco,B., Garbi,C.,
            Conte,I. and Feliciello,A.
  TITLE     The TBC1D31/praja2 complex controls primary ciliogenesis through
            PKA-directed OFD1 ubiquitylation
  JOURNAL   EMBO J 40 (10), e106503 (2021)
   PUBMED   33934390
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100873.2.
            
            On May 9, 2018 this sequence version replaced XP_016869479.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1933292.1,
                                           SRR1660803.102553.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153031, SAMEA2153733
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..566
                     /product="TBC1 domain family member 31 isoform 12"
                     /note="WD repeat-containing protein 67; WD repeat domain
                     67"
                     /calculated_mol_wt=67710
     Region          <33..105
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; cl46302"
                     /db_xref="CDD:480642"
     Region          <196..>500
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     CDS             1..566
                     /gene="TBC1D31"
                     /gene_synonym="Gm85; WDR67"
                     /coded_by="NM_001363156.1:1314..3014"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="GeneID:93594"
                     /db_xref="HGNC:HGNC:30888"
                     /db_xref="MIM:621444"
ORIGIN      
        1 mwhfstfrrn tpskvgsyse yyrvnwcqhw feyfpnppin ilsmienvla fhdkellqhf
       61 idhditsqly awplletvfs evltreewlk lfdnifsnhp sfllmtvvay nicsrtplls
      121 cnlkddfeff fhhrnnldin vvirqvyhlm ettptdihpd smlnvfvalt kgqypvfnqy
      181 pkfivdyqtq ererirndel dylrerqtve dmqakvdqqr vedeawyqkq ellrkaeetr
      241 remllqeeek miqqrqrlaa vkrelkvkem hlqdaarrrf lklqqdqqem elrrlddeig
      301 rkvymrdrei aatardlemr qlelesqkrl yeknltenqe alakemrada dayrrkvdle
      361 ehmfhkliea getqsqktqk vikenlakae qaclntdwqi qslhkqkcdd lqrnkcyqev
      421 akllrenrrk eieiinamve eeakkwkeae gkefrlrsak kasalsdasr kwflkqeina
      481 avehaenpch keeprfqneq dssclprtsq lndssemdps tqislnrrav ewdttgqnli
      541 kkvrnlrqrl tararhrcqt phllaa
//
LOCUS       NP_001317535             961 aa            linear   PRI 15-DEC-2025
DEFINITION  TBC1 domain family member 31 isoform 3 [Homo sapiens].
ACCESSION   NP_001317535 XP_016869474
VERSION     NP_001317535.1
DBSOURCE    REFSEQ: accession NM_001330606.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 961)
  AUTHORS   Cao,P., Chen,H., Zhang,Y., Zhang,Q., Shi,M., Han,H., Wang,X.,
            Jin,L., Guo,B., Hao,R., Zhao,X., Li,Y., Gao,C., Liu,X., Wang,Y.,
            Yang,A., Yang,C., Si,A., Li,H., Song,Q., He,F. and Zhou,G.
  TITLE     Genomic Amplification of TBC1D31 Promotes Hepatocellular Carcinoma
            Through Reducing the Rab22A-Mediated Endolysosomal Trafficking and
            Degradation of EGFR
  JOURNAL   Adv Sci (Weinh) 11 (40), e2405459 (2024)
   PUBMED   39206796
  REMARK    GeneRIF: Genomic Amplification of TBC1D31 Promotes Hepatocellular
            Carcinoma Through Reducing the Rab22A-Mediated Endolysosomal
            Trafficking and Degradation of EGFR.
REFERENCE   2  (residues 1 to 961)
  AUTHORS   Saygili,S., Kosukcu,C., Bastug,T., Dogan,O.A., Yilmaz,E.K.,
            Kalyoncu,A.U., Agbas,A., Canpolat,N., Caliskan,S. and Ozaltin,F.
  TITLE     A novel homozygous missense variant in TBC1D31 in a consanguineous
            family with congenital anomalies of the kidney and urinary tract
            (CAKUT)
  JOURNAL   Clin Genet 104 (6), 679-685 (2023)
   PUBMED   37468454
  REMARK    GeneRIF: A novel homozygous missense variant in TBC1D31 in a
            consanguineous family with congenital anomalies of the kidney and
            urinary tract (CAKUT).
REFERENCE   3  (residues 1 to 961)
  AUTHORS   Senatore,E., Chiuso,F., Rinaldi,L., Intartaglia,D., Delle Donne,R.,
            Pedone,E., Catalanotti,B., Pirone,L., Fiorillo,B., Moraca,F.,
            Giamundo,G., Scala,G., Raffeiner,A., Torres-Quesada,O., Stefan,E.,
            Kwiatkowski,M., van Pijkeren,A., Morleo,M., Franco,B., Garbi,C.,
            Conte,I. and Feliciello,A.
  TITLE     The TBC1D31/praja2 complex controls primary ciliogenesis through
            PKA-directed OFD1 ubiquitylation
  JOURNAL   EMBO J 40 (10), e106503 (2021)
   PUBMED   33934390
REFERENCE   4  (residues 1 to 961)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   5  (residues 1 to 961)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100873.2, BC143523.1, BG771416.1 and U43374.1.
            
            On Aug 30, 2016 this sequence version replaced XP_016869474.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143523.1, SRR1660807.25263.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2152798
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..961
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..961
                     /product="TBC1 domain family member 31 isoform 3"
                     /note="WD repeat-containing protein 67; WD repeat domain
                     67"
                     /calculated_mol_wt=112413
     Region          <10..235
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          25..60
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          66..102
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          108..148
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          156..196
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          204..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          357..500
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; cl46302"
                     /db_xref="CDD:480642"
     Region          <579..>857
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     CDS             1..961
                     /gene="TBC1D31"
                     /gene_synonym="Gm85; WDR67"
                     /coded_by="NM_001330606.2:263..3148"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS83320.1"
                     /db_xref="GeneID:93594"
                     /db_xref="HGNC:HGNC:30888"
                     /db_xref="MIM:621444"
ORIGIN      
        1 mfltymetvt kelvswmrgh essvfsisvh asgkyaitts sdtaqlwdld tfqrkrklni
       61 rqsvgiqkvf flplsntils cfkdnsifaw ecdtlfckyq lpappesssi lykvfavtrd
      121 grilaaggks nhlhlwclea rqlfriiqmp tkvrairhle flpdsfdags nqvlgvlsqd
      181 gimrfinmqt ckllfeigsl degisssais phgryiasim engslniysv qaltqeinkp
      241 ppplvkvied lpknklsssd lkmkvtsgrv qqpaksresk mqtrilkqdl tgdfeskkne
      301 lpdglnkkrl qillkgygey ptkyrmfiwr sllqlpenht afstlidkgt hvaflnlqkk
      361 ypiksrkllr vlqrtlsala hwsvifsdtp ylpllafpfv klfqnnqlic feviatliin
      421 wcqhwfeyfp nppinilsmi envlafhdke llqhfidhdi tsqlyawpll etvfsevltr
      481 eewlklfdni fsnhpsfllm tvvaynicsr tpllscnlkd dfefffhhrn nldinvvirq
      541 vyhlmettpt dihpdsmlnv fvaltkgqyp vfnqypkfiv dyqtqereri rndeldylre
      601 rqtvedmqak vdqqrvedea wyqkqellrk aeetrremll qeeekmiqqr qrlaavkrel
      661 kvkemhlqda arrrflklqq dqqemelrrl ddeigrkvym rdreiaatar dlemrqlele
      721 sqkrlyeknl tenqealake mradadayrr kvdleehmfh klieagetqs qktqkviken
      781 lakaeqacln tdwqiqslhk qkcddlqrnk cyqevakllr enrrkeieii namveeeakk
      841 wkeaegkefr lrsakkasal sdasrkwflk qeinaaveha enpchkeepr fqneqdsscl
      901 prtsqlndss emdpstqisl nrravewdtt gqnlikkvrn lrqrltarar hrcqtphlla
      961 a
//
LOCUS       NP_001138560             970 aa            linear   PRI 15-DEC-2025
DEFINITION  TBC1 domain family member 31 isoform 2 [Homo sapiens].
ACCESSION   NP_001138560
VERSION     NP_001138560.1
DBSOURCE    REFSEQ: accession NM_001145088.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 970)
  AUTHORS   Cao,P., Chen,H., Zhang,Y., Zhang,Q., Shi,M., Han,H., Wang,X.,
            Jin,L., Guo,B., Hao,R., Zhao,X., Li,Y., Gao,C., Liu,X., Wang,Y.,
            Yang,A., Yang,C., Si,A., Li,H., Song,Q., He,F. and Zhou,G.
  TITLE     Genomic Amplification of TBC1D31 Promotes Hepatocellular Carcinoma
            Through Reducing the Rab22A-Mediated Endolysosomal Trafficking and
            Degradation of EGFR
  JOURNAL   Adv Sci (Weinh) 11 (40), e2405459 (2024)
   PUBMED   39206796
  REMARK    GeneRIF: Genomic Amplification of TBC1D31 Promotes Hepatocellular
            Carcinoma Through Reducing the Rab22A-Mediated Endolysosomal
            Trafficking and Degradation of EGFR.
REFERENCE   2  (residues 1 to 970)
  AUTHORS   Saygili,S., Kosukcu,C., Bastug,T., Dogan,O.A., Yilmaz,E.K.,
            Kalyoncu,A.U., Agbas,A., Canpolat,N., Caliskan,S. and Ozaltin,F.
  TITLE     A novel homozygous missense variant in TBC1D31 in a consanguineous
            family with congenital anomalies of the kidney and urinary tract
            (CAKUT)
  JOURNAL   Clin Genet 104 (6), 679-685 (2023)
   PUBMED   37468454
  REMARK    GeneRIF: A novel homozygous missense variant in TBC1D31 in a
            consanguineous family with congenital anomalies of the kidney and
            urinary tract (CAKUT).
REFERENCE   3  (residues 1 to 970)
  AUTHORS   Senatore,E., Chiuso,F., Rinaldi,L., Intartaglia,D., Delle Donne,R.,
            Pedone,E., Catalanotti,B., Pirone,L., Fiorillo,B., Moraca,F.,
            Giamundo,G., Scala,G., Raffeiner,A., Torres-Quesada,O., Stefan,E.,
            Kwiatkowski,M., van Pijkeren,A., Morleo,M., Franco,B., Garbi,C.,
            Conte,I. and Feliciello,A.
  TITLE     The TBC1D31/praja2 complex controls primary ciliogenesis through
            PKA-directed OFD1 ubiquitylation
  JOURNAL   EMBO J 40 (10), e106503 (2021)
   PUBMED   33934390
REFERENCE   4  (residues 1 to 970)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   5  (residues 1 to 970)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK056434.1, BC143525.1 and CA429516.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143525.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..970
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..970
                     /product="TBC1 domain family member 31 isoform 2"
                     /note="WD repeat-containing protein 67; WD repeat domain
                     67"
                     /calculated_mol_wt=112526
     Region          44..340
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          46..81
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          86..123
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          130..164
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          171..207
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          215..253
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          261..291
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          309..335
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          462..605
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; cl46302"
                     /db_xref="CDD:480642"
     Region          <690..>854
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     Region          <761..951
                     /region_name="Nup88"
                     /note="Nuclear pore component; pfam10168"
                     /db_xref="CDD:462975"
     CDS             1..970
                     /gene="TBC1D31"
                     /gene_synonym="Gm85; WDR67"
                     /coded_by="NM_001145088.2:64..2976"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47916.1"
                     /db_xref="GeneID:93594"
                     /db_xref="HGNC:HGNC:30888"
                     /db_xref="MIM:621444"
ORIGIN      
        1 mqstdlgnke sgkiwhrkps patrdgiivn iihntsdyhp kvlrflnvaf dgtgdcliag
       61 dhqgniyvfd lhgnrfnlvq rtaqactala fnlrrksefl valadysikc fdtvtkelvs
      121 wmrghessvf sisvhasgky aittssdtaq lwdldtfqrk rklnirqsvg iqkvfflpls
      181 ntilscfkdn sifawecdtl fckyqlpapp esssilykvf avtrdgrila aggksnhlhl
      241 wclearqlfr iiqmptkvra irhleflpds fdagsnqvlg vlsqdgimrf inmqtckllf
      301 eigsldegis ssaisphgry iasimengsl niysvqaltq einkpppplv kviedlpknk
      361 lsssdlkmkv tsgrvqqpak sreskmqtri lkqdltgdfe skknelpdgl nkkrlqillk
      421 gygeyptkyr mfiwrsllql penhtafstl idkgthvafl nlqkkypiks rkllrvlqrt
      481 lsalahwsvi fsdtpylpll afpfvklfqn nqlicfevia tliinwcqhw feyfpnppin
      541 ilsmienvla fhdkellqhf idhditsqly awplletvfs evltreewlk lfdnifsnhp
      601 sfllmtvvay nicsrtplls cnlkddfeff fhhrnnldin vvirqvyhlm ettptdihpd
      661 smlnvfvalt kgqypvfnqy pkfivdyqtq ererirndel dylrerqtve dmqakvdqqr
      721 vedeawyqkq ellrkaeetr remllqeeek miqqrqrlaa vkrelkvkem hlqdaarrrf
      781 lklqqdqqem elrrlddeig rknltenqea lakemradad ayrrkvdlee hmfhklieag
      841 etqsqktqkw keaegkefrl rsakkasals dasrkwflkq einaavehae npchkeeprf
      901 qneqdssclp rtsqlndsse mdpstqisln rravewdttg qnlikkvrnl rqrltararh
      961 rcqtphllaa
//
LOCUS       NP_663622               1066 aa            linear   PRI 15-DEC-2025
DEFINITION  TBC1 domain family member 31 isoform 1 [Homo sapiens].
ACCESSION   NP_663622
VERSION     NP_663622.2
DBSOURCE    REFSEQ: accession NM_145647.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Cao,P., Chen,H., Zhang,Y., Zhang,Q., Shi,M., Han,H., Wang,X.,
            Jin,L., Guo,B., Hao,R., Zhao,X., Li,Y., Gao,C., Liu,X., Wang,Y.,
            Yang,A., Yang,C., Si,A., Li,H., Song,Q., He,F. and Zhou,G.
  TITLE     Genomic Amplification of TBC1D31 Promotes Hepatocellular Carcinoma
            Through Reducing the Rab22A-Mediated Endolysosomal Trafficking and
            Degradation of EGFR
  JOURNAL   Adv Sci (Weinh) 11 (40), e2405459 (2024)
   PUBMED   39206796
  REMARK    GeneRIF: Genomic Amplification of TBC1D31 Promotes Hepatocellular
            Carcinoma Through Reducing the Rab22A-Mediated Endolysosomal
            Trafficking and Degradation of EGFR.
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Saygili,S., Kosukcu,C., Bastug,T., Dogan,O.A., Yilmaz,E.K.,
            Kalyoncu,A.U., Agbas,A., Canpolat,N., Caliskan,S. and Ozaltin,F.
  TITLE     A novel homozygous missense variant in TBC1D31 in a consanguineous
            family with congenital anomalies of the kidney and urinary tract
            (CAKUT)
  JOURNAL   Clin Genet 104 (6), 679-685 (2023)
   PUBMED   37468454
  REMARK    GeneRIF: A novel homozygous missense variant in TBC1D31 in a
            consanguineous family with congenital anomalies of the kidney and
            urinary tract (CAKUT).
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Senatore,E., Chiuso,F., Rinaldi,L., Intartaglia,D., Delle Donne,R.,
            Pedone,E., Catalanotti,B., Pirone,L., Fiorillo,B., Moraca,F.,
            Giamundo,G., Scala,G., Raffeiner,A., Torres-Quesada,O., Stefan,E.,
            Kwiatkowski,M., van Pijkeren,A., Morleo,M., Franco,B., Garbi,C.,
            Conte,I. and Feliciello,A.
  TITLE     The TBC1D31/praja2 complex controls primary ciliogenesis through
            PKA-directed OFD1 ubiquitylation
  JOURNAL   EMBO J 40 (10), e106503 (2021)
   PUBMED   33934390
REFERENCE   4  (residues 1 to 1066)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   5  (residues 1 to 1066)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK056434.1, BC143525.1, BC101724.1 and CA429516.1.
            
            On Feb 9, 2009 this sequence version replaced NP_663622.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056434.1, SRR1803615.254251.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000287380.6/ ENSP00000287380.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..1066
                     /product="TBC1 domain family member 31 isoform 1"
                     /note="WD repeat-containing protein 67; WD repeat domain
                     67"
                     /calculated_mol_wt=124059
     Region          33..74
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          44..340
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          46..81
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          75..116
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          86..123
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          117..157
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          130..164
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          158..200
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          171..207
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          201..248
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          215..253
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          249..296
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          261..291
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          297..334
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          309..335
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          462..605
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; cl46302"
                     /db_xref="CDD:480642"
     Region          <684..>962
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     Region          989..1020
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          1053..1056
                     /region_name="Mediates direct interaction with PJA2.
                     /evidence=ECO:0000269|PubMed:33934390"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     CDS             1..1066
                     /gene="TBC1D31"
                     /gene_synonym="Gm85; WDR67"
                     /coded_by="NM_145647.4:64..3264"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6338.1"
                     /db_xref="GeneID:93594"
                     /db_xref="HGNC:HGNC:30888"
                     /db_xref="MIM:621444"
ORIGIN      
        1 mqstdlgnke sgkiwhrkps patrdgiivn iihntsdyhp kvlrflnvaf dgtgdcliag
       61 dhqgniyvfd lhgnrfnlvq rtaqactala fnlrrksefl valadysikc fdtvtkelvs
      121 wmrghessvf sisvhasgky aittssdtaq lwdldtfqrk rklnirqsvg iqkvfflpls
      181 ntilscfkdn sifawecdtl fckyqlpapp esssilykvf avtrdgrila aggksnhlhl
      241 wclearqlfr iiqmptkvra irhleflpds fdagsnqvlg vlsqdgimrf inmqtckllf
      301 eigsldegis ssaisphgry iasimengsl niysvqaltq einkpppplv kviedlpknk
      361 lsssdlkmkv tsgrvqqpak sreskmqtri lkqdltgdfe skknelpdgl nkkrlqillk
      421 gygeyptkyr mfiwrsllql penhtafstl idkgthvafl nlqkkypiks rkllrvlqrt
      481 lsalahwsvi fsdtpylpll afpfvklfqn nqlicfevia tliinwcqhw feyfpnppin
      541 ilsmienvla fhdkellqhf idhditsqly awplletvfs evltreewlk lfdnifsnhp
      601 sfllmtvvay nicsrtplls cnlkddfeff fhhrnnldin vvirqvyhlm ettptdihpd
      661 smlnvfvalt kgqypvfnqy pkfivdyqtq ererirndel dylrerqtve dmqakvdqqr
      721 vedeawyqkq ellrkaeetr remllqeeek miqqrqrlaa vkrelkvkem hlqdaarrrf
      781 lklqqdqqem elrrlddeig rkvymrdrei aatardlemr qlelesqkrl yeknltenqe
      841 alakemrada dayrrkvdle ehmfhkliea getqsqktqk vikenlakae qaclntdwqi
      901 qslhkqkcdd lqrnkcyqev akllrenrrk eieiinamve eeakkwkeae gkefrlrsak
      961 kasalsdasr kwflkqeina avehaenpch keeprfqneq dssclprtsq lndssemdps
     1021 tqislnrrav ewdttgqnli kkvrnlrqrl tararhrcqt phllaa
//
LOCUS       NP_001350081             930 aa            linear   PRI 15-DEC-2025
DEFINITION  TBC1 domain family member 31 isoform 8 [Homo sapiens].
ACCESSION   NP_001350081 XP_016869475
VERSION     NP_001350081.1
DBSOURCE    REFSEQ: accession NM_001363152.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 930)
  AUTHORS   Cao,P., Chen,H., Zhang,Y., Zhang,Q., Shi,M., Han,H., Wang,X.,
            Jin,L., Guo,B., Hao,R., Zhao,X., Li,Y., Gao,C., Liu,X., Wang,Y.,
            Yang,A., Yang,C., Si,A., Li,H., Song,Q., He,F. and Zhou,G.
  TITLE     Genomic Amplification of TBC1D31 Promotes Hepatocellular Carcinoma
            Through Reducing the Rab22A-Mediated Endolysosomal Trafficking and
            Degradation of EGFR
  JOURNAL   Adv Sci (Weinh) 11 (40), e2405459 (2024)
   PUBMED   39206796
  REMARK    GeneRIF: Genomic Amplification of TBC1D31 Promotes Hepatocellular
            Carcinoma Through Reducing the Rab22A-Mediated Endolysosomal
            Trafficking and Degradation of EGFR.
REFERENCE   2  (residues 1 to 930)
  AUTHORS   Saygili,S., Kosukcu,C., Bastug,T., Dogan,O.A., Yilmaz,E.K.,
            Kalyoncu,A.U., Agbas,A., Canpolat,N., Caliskan,S. and Ozaltin,F.
  TITLE     A novel homozygous missense variant in TBC1D31 in a consanguineous
            family with congenital anomalies of the kidney and urinary tract
            (CAKUT)
  JOURNAL   Clin Genet 104 (6), 679-685 (2023)
   PUBMED   37468454
  REMARK    GeneRIF: A novel homozygous missense variant in TBC1D31 in a
            consanguineous family with congenital anomalies of the kidney and
            urinary tract (CAKUT).
REFERENCE   3  (residues 1 to 930)
  AUTHORS   Senatore,E., Chiuso,F., Rinaldi,L., Intartaglia,D., Delle Donne,R.,
            Pedone,E., Catalanotti,B., Pirone,L., Fiorillo,B., Moraca,F.,
            Giamundo,G., Scala,G., Raffeiner,A., Torres-Quesada,O., Stefan,E.,
            Kwiatkowski,M., van Pijkeren,A., Morleo,M., Franco,B., Garbi,C.,
            Conte,I. and Feliciello,A.
  TITLE     The TBC1D31/praja2 complex controls primary ciliogenesis through
            PKA-directed OFD1 ubiquitylation
  JOURNAL   EMBO J 40 (10), e106503 (2021)
   PUBMED   33934390
REFERENCE   4  (residues 1 to 930)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   5  (residues 1 to 930)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100873.2.
            
            On May 9, 2018 this sequence version replaced XP_016869475.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.249274.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2152798, SAMEA2153031
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..930
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..930
                     /product="TBC1 domain family member 31 isoform 8"
                     /note="WD repeat-containing protein 67; WD repeat domain
                     67"
                     /calculated_mol_wt=108588
     Region          <10..235
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          25..60
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          66..102
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          108..148
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          156..196
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          204..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          357..500
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; cl46302"
                     /db_xref="CDD:480642"
     Region          <579..>921
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     CDS             1..930
                     /gene="TBC1D31"
                     /gene_synonym="Gm85; WDR67"
                     /coded_by="NM_001363152.1:263..3055"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:93594"
                     /db_xref="HGNC:HGNC:30888"
                     /db_xref="MIM:621444"
ORIGIN      
        1 mfltymetvt kelvswmrgh essvfsisvh asgkyaitts sdtaqlwdld tfqrkrklni
       61 rqsvgiqkvf flplsntils cfkdnsifaw ecdtlfckyq lpappesssi lykvfavtrd
      121 grilaaggks nhlhlwclea rqlfriiqmp tkvrairhle flpdsfdags nqvlgvlsqd
      181 gimrfinmqt ckllfeigsl degisssais phgryiasim engslniysv qaltqeinkp
      241 ppplvkvied lpknklsssd lkmkvtsgrv qqpaksresk mqtrilkqdl tgdfeskkne
      301 lpdglnkkrl qillkgygey ptkyrmfiwr sllqlpenht afstlidkgt hvaflnlqkk
      361 ypiksrkllr vlqrtlsala hwsvifsdtp ylpllafpfv klfqnnqlic feviatliin
      421 wcqhwfeyfp nppinilsmi envlafhdke llqhfidhdi tsqlyawpll etvfsevltr
      481 eewlklfdni fsnhpsfllm tvvaynicsr tpllscnlkd dfefffhhrn nldinvvirq
      541 vyhlmettpt dihpdsmlnv fvaltkgqyp vfnqypkfiv dyqtqereri rndeldylre
      601 rqtvedmqak vdqqrvedea wyqkqellrk aeetrremll qeeekmiqqr qrlaavkrel
      661 kvkemhlqda arrrflklqq dqqemelrrl ddeigrknlt enqealakem radadayrrk
      721 vdleehmfhk lieagetqsq ktqkvikenl akaeqaclnt dwqiqslhkq kcddlqrnkc
      781 yqevakllre nrrkeieiin amveeeakkw keaegkefrl rsakkasals dasrkwflkq
      841 einaavehae npchkeeprf qneqdssclp rtsqlndsse mdpstqisln rravewdttg
      901 qnlikkvrnl rqrltararh rcqtphllaa
//
LOCUS       NP_001350080             983 aa            linear   PRI 15-DEC-2025
DEFINITION  TBC1 domain family member 31 isoform 7 [Homo sapiens].
ACCESSION   NP_001350080 XP_016869472
VERSION     NP_001350080.1
DBSOURCE    REFSEQ: accession NM_001363151.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 983)
  AUTHORS   Cao,P., Chen,H., Zhang,Y., Zhang,Q., Shi,M., Han,H., Wang,X.,
            Jin,L., Guo,B., Hao,R., Zhao,X., Li,Y., Gao,C., Liu,X., Wang,Y.,
            Yang,A., Yang,C., Si,A., Li,H., Song,Q., He,F. and Zhou,G.
  TITLE     Genomic Amplification of TBC1D31 Promotes Hepatocellular Carcinoma
            Through Reducing the Rab22A-Mediated Endolysosomal Trafficking and
            Degradation of EGFR
  JOURNAL   Adv Sci (Weinh) 11 (40), e2405459 (2024)
   PUBMED   39206796
  REMARK    GeneRIF: Genomic Amplification of TBC1D31 Promotes Hepatocellular
            Carcinoma Through Reducing the Rab22A-Mediated Endolysosomal
            Trafficking and Degradation of EGFR.
REFERENCE   2  (residues 1 to 983)
  AUTHORS   Saygili,S., Kosukcu,C., Bastug,T., Dogan,O.A., Yilmaz,E.K.,
            Kalyoncu,A.U., Agbas,A., Canpolat,N., Caliskan,S. and Ozaltin,F.
  TITLE     A novel homozygous missense variant in TBC1D31 in a consanguineous
            family with congenital anomalies of the kidney and urinary tract
            (CAKUT)
  JOURNAL   Clin Genet 104 (6), 679-685 (2023)
   PUBMED   37468454
  REMARK    GeneRIF: A novel homozygous missense variant in TBC1D31 in a
            consanguineous family with congenital anomalies of the kidney and
            urinary tract (CAKUT).
REFERENCE   3  (residues 1 to 983)
  AUTHORS   Senatore,E., Chiuso,F., Rinaldi,L., Intartaglia,D., Delle Donne,R.,
            Pedone,E., Catalanotti,B., Pirone,L., Fiorillo,B., Moraca,F.,
            Giamundo,G., Scala,G., Raffeiner,A., Torres-Quesada,O., Stefan,E.,
            Kwiatkowski,M., van Pijkeren,A., Morleo,M., Franco,B., Garbi,C.,
            Conte,I. and Feliciello,A.
  TITLE     The TBC1D31/praja2 complex controls primary ciliogenesis through
            PKA-directed OFD1 ubiquitylation
  JOURNAL   EMBO J 40 (10), e106503 (2021)
   PUBMED   33934390
REFERENCE   4  (residues 1 to 983)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   5  (residues 1 to 983)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC100873.2 and AC068228.8.
            
            On May 9, 2018 this sequence version replaced XP_016869472.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2708480.1,
                                           SRR14038196.609688.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..983
                     /product="TBC1 domain family member 31 isoform 7"
                     /note="WD repeat-containing protein 67; WD repeat domain
                     67"
                     /calculated_mol_wt=114256
     Region          33..74
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          44..340
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          46..81
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          75..116
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          86..123
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          117..157
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          130..164
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          158..200
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          171..207
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          201..248
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          215..253
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          249..296
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          261..291
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          297..334
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN5.2)"
     Region          309..335
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          462..605
                     /region_name="RabGAP-TBC"
                     /note="Rab-GTPase-TBC domain; cl46302"
                     /db_xref="CDD:480642"
     Region          <684..>967
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     CDS             1..983
                     /gene="TBC1D31"
                     /gene_synonym="Gm85; WDR67"
                     /coded_by="NM_001363151.2:64..3015"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:93594"
                     /db_xref="HGNC:HGNC:30888"
                     /db_xref="MIM:621444"
ORIGIN      
        1 mqstdlgnke sgkiwhrkps patrdgiivn iihntsdyhp kvlrflnvaf dgtgdcliag
       61 dhqgniyvfd lhgnrfnlvq rtaqactala fnlrrksefl valadysikc fdtvtkelvs
      121 wmrghessvf sisvhasgky aittssdtaq lwdldtfqrk rklnirqsvg iqkvfflpls
      181 ntilscfkdn sifawecdtl fckyqlpapp esssilykvf avtrdgrila aggksnhlhl
      241 wclearqlfr iiqmptkvra irhleflpds fdagsnqvlg vlsqdgimrf inmqtckllf
      301 eigsldegis ssaisphgry iasimengsl niysvqaltq einkpppplv kviedlpknk
      361 lsssdlkmkv tsgrvqqpak sreskmqtri lkqdltgdfe skknelpdgl nkkrlqillk
      421 gygeyptkyr mfiwrsllql penhtafstl idkgthvafl nlqkkypiks rkllrvlqrt
      481 lsalahwsvi fsdtpylpll afpfvklfqn nqlicfevia tliinwcqhw feyfpnppin
      541 ilsmienvla fhdkellqhf idhditsqly awplletvfs evltreewlk lfdnifsnhp
      601 sfllmtvvay nicsrtplls cnlkddfeff fhhrnnldin vvirqvyhlm ettptdihpd
      661 smlnvfvalt kgqypvfnqy pkfivdyqtq ererirndel dylrerqtve dmqakvdqqr
      721 vedeawyqkq ellrkaeetr remllqeeek miqqrqrlaa vkrelkvkem hlqdaarrrf
      781 lklqqdqqem elrrlddeig rkvymrdrei aatardlemr qlelesqkrl yeknltenqe
      841 alakemrada dayrrkvdle ehmfhkliea getqsqktqk wkeaegkefr lrsakkasal
      901 sdasrkwflk qeinaaveha enpchkvtav vslrrgdldt dthrekmirr prrkaaiykp
      961 rrenaeetnp vntfnlassi vqe
//
LOCUS       NP_001372991             712 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 6 [Homo sapiens].
ACCESSION   NP_001372991
VERSION     NP_001372991.1
DBSOURCE    REFSEQ: accession NM_001386062.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 712)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 712)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 712)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 712)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 712)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 712)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 712)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 712)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157936.12, AL353768.28 and
            AL354893.14.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..712
                     /product="aminopeptidase O isoform 6"
                     /calculated_mol_wt=81486
     Region          <317..545
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     Region          614..711
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
     CDS             1..712
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_001386062.2:189..2327"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mdiqldpard dlplmantsh ilvkhyvldl dvdfesqvie gtivlfledg nrfkkqnssi
       61 eeacqsesnk ackfgmpepc hipvtnartf ssemeyndfa icskgekdts dkdgnhdnqe
      121 hasgisssky ccdtgnhgse dfllvldccd lsvlkveevd vaavpglekf trspeltvvs
      181 eefrnqivre lvtlpanrwr eqldyyarcs qapgcgellf dtdtwslqir ktgaqtatdf
      241 phairiwykt kpegrsvtwt sdqsgrhvgv cshmeypcrf qnasattqei iphrvfapvc
      301 ltgacqetll rlippclsaa hsvlgahpfs rldvlivpan fpslgmasph imflsqsilt
      361 ggnhlcgtrl cheiahawfg laigardwte ewlsegfath ledvfwataq qlapyeareq
      421 qelraclrwr rlqdemqcsp eemqvlrpsk dktghtsdsg asvikhglnp ekifmqvhyl
      481 kgyfllrfla krlgdetyfs flrkfvhtfh gqlilsqdfl qmllenipee krlelsveni
      541 yqdwlessgi pkplqrerra gaecglarqv raevtkwigv nrrprkrkrr ekeevfekll
      601 pdqlvllleh lleqktlspr tlqslqrtyh lqdqdaevrh rwcelivkhk ftkayksver
      661 flqedqamgv ylygelmvse darqqqlarr cfertkeqmd rssaqvvaem lf
//
LOCUS       NP_001373001             555 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 11 [Homo sapiens].
ACCESSION   NP_001373001 XP_011517431
VERSION     NP_001373001.1
DBSOURCE    REFSEQ: accession NM_001386072.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 555)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 555)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 555)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 555)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 555)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 555)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 555)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157936.12 and AL353768.28.
            
            On Aug 6, 2020 this sequence version replaced XP_011517431.1.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.2944615.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2153932
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..555
                     /product="aminopeptidase O isoform 11"
                     /calculated_mol_wt=62086
     Region          <244..>509
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     CDS             1..555
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_001386072.1:189..1856"
                     /note="isoform 11 is encoded by transcript variant 14"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mdiqldpard dlplmantsh ilvkhyvldl dvdfesqvie gtivlfledg nrfkkqnssi
       61 eeacqsesnk ackfgmpepc hipvtnartf ssemeyndfa icskgekdts dkdgnhdnqe
      121 hasgisssky ccdtgnhgse dfllvldccd lsvlkveevd vaavpglekf trspeltvvs
      181 eefrnqivre lvtlpanrwr eqldyyarcs qapgcgellf dtdtwslqir ktgaqtatdf
      241 phairiwykt kpegrsvtwt sdqsgrpcvy tvgspinnra lfpcqeppva mstwqatvra
      301 aasfvvlmsg ensakptqlw eecsswyyyv tmpmpastft iavgcwtemk metwssndla
      361 terpfspsea nfrhvgvcsh meypcrfqna sattqeiiph rvfapvcltg acqetllrli
      421 ppclsaahsv lgahpfsrld vlivpanfps lgmasphimf lsqsiltggn hlcgtrlche
      481 iahawfglai gardwteewl segfathled vfwataqqla pyeareqqel raclrwrrlq
      541 demqcspeem qvlss
//
LOCUS       NP_001373003             798 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 13 [Homo sapiens].
ACCESSION   NP_001373003
VERSION     NP_001373003.1
DBSOURCE    REFSEQ: accession NM_001386074.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157936.12, AL353768.28 and
            AL354893.14.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.246957.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2149398
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..798
                     /product="aminopeptidase O isoform 13"
                     /calculated_mol_wt=90740
     Region          <244..652
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     Site            586
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:P15144; propagated from
                     UniProtKB/Swiss-Prot (Q8N6M6.2)"
     Region          689..699
                     /region_name="Nucleolar localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q8BXQ6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6M6.2)"
     Region          721..>771
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
     CDS             1..798
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_001386074.1:189..2585"
                     /note="isoform 13 is encoded by transcript variant 16"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mdiqldpard dlplmantsh ilvkhyvldl dvdfesqvie gtivlfledg nrfkkqnssi
       61 eeacqsesnk ackfgmpepc hipvtnartf ssemeyndfa icskgekdts dkdgnhdnqe
      121 hasgisssky ccdtgnhgse dfllvldccd lsvlkveevd vaavpglekf trspeltvvs
      181 eefrnqivre lvtlpanrwr eqldyyarcs qapgcgellf dtdtwslqir ktgaqtatdf
      241 phairiwykt kpegrsvtwt sdqsgrpcvy tvgspinnra lfpcqeppva mstwqatvra
      301 aasfvvlmsg ensakptqlw eecsswyyyv tmpmpastft iavgcwtemk metwssndla
      361 terpfspsea nfrhvgvcsh meypcrfqna sattqeiiph rvfapvcltg acqetllrli
      421 ppclsaahsv lgahpfsrld vlivpanfps lgmasphimf lsqsiltggn hlcgtrlche
      481 iahawfglai gardwteewl segfathled vfwataqqla pyeareqqel raclrwrrlq
      541 demqcspeem qvlrpskdkt ghtsdsgasv ikhglnpeki fmqvhylkgy fllrflakrl
      601 gdetyfsflr kfvhtfhgql ilsqdflqml lenipeekrl elsveniyqd wlessgipkp
      661 lqrerragae cglarqvrae vtkwigvnrr prkrkrreke evfekllpdq lvlllehlle
      721 qktlsprtlq slqrtyhlqd qdaevrhrwc elivkhkftk ayksverflq edqvkdfpde
      781 lrpatprdtl cgagvpcl
//
LOCUS       NP_001372990             429 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 5 [Homo sapiens].
ACCESSION   NP_001372990
VERSION     NP_001372990.1
DBSOURCE    REFSEQ: accession NM_001386061.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 429)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157936.12, AL353768.28 and
            AL354893.14.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN03465411
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..429
                     /product="aminopeptidase O isoform 5"
                     /calculated_mol_wt=49122
     Region          <141..222
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     Region          291..>341
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
     CDS             1..429
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_001386061.1:83..1372"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mpmpastfti avgcwtemkm etwssndlat erpfspsean frhvgvcshm eypcrfqnas
       61 attqeiiphr vfapvcltga cqetllrlip pclsaahsvl gahpfsrldv livpanfpsl
      121 gmarpskdkt ghtsdsgasv ikhglnpeki fmqvhylkgy fllrflakrl gdetyfsflr
      181 kfvhtfhgql ilsqdflqml lenipeekrl elsveniyqd wlessgipkp lqrerragae
      241 cglarqvrae vtkwigvnrr prkrkrreke evfekllpdq lvlllehlle qktlsprtlq
      301 slqrtyhlqd qdaevrhrwc elivkhkftk ayksverflq edqerpqqds firlllawgt
      361 rleltldikg gimwllkpsa hspvhilvll fprgwsqpgt hkrqilvnaa slpggcllpw
      421 iwsgaalrf
//
LOCUS       NP_001276059             372 aa            linear   PRI 15-DEC-2025
DEFINITION  tubulin beta-4A chain isoform 4 [Homo sapiens].
ACCESSION   NP_001276059 XP_005259534
VERSION     NP_001276059.1
DBSOURCE    REFSEQ: accession NM_001289130.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Garg,D., Holla,V.V., Ganguly,J., Rajan,R., Saini,A., Agarwal,A.,
            Radhakrishnan,D.M., Basu,P., Mondal,B., Dhar,D., Kamble,N.,
            Yadav,R., Muthusamy,B., Kumar,H., Srivastava,A.K. and Pal,P.K.
  TITLE     Expanding the phenotypic and genotypic spectrum of DYT-TUBB4A with
            seven patients from India
  JOURNAL   Parkinsonism Relat Disord 124, 107012 (2024)
   PUBMED   38762926
  REMARK    GeneRIF: Expanding the phenotypic and genotypic spectrum of
            DYT-TUBB4A with seven patients from India.
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Ben Jdila,M., Kammoun,F., Abdelmaksoud-Dammak,R., Triki,C. and
            Fakhfakh,F.
  TITLE     Mutation in the beta-tubulin gene TUBB4A results in epileptic
            encephalopathy associated with hypomyelinated leucodystrophy:
            Unexpected findings reveal genetic mosaicism
  JOURNAL   Int J Dev Neurosci 83 (6), 532-545 (2023)
   PUBMED   37529938
  REMARK    GeneRIF: Mutation in the beta-tubulin gene TUBB4A results in
            epileptic encephalopathy associated with hypomyelinated
            leucodystrophy: Unexpected findings reveal genetic mosaicism.
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Simons,C., Wolf,N.I., McNeil,N., Caldovic,L., Devaney,J.M.,
            Takanohashi,A., Crawford,J., Ru,K., Grimmond,S.M., Miller,D.,
            Tonduti,D., Schmidt,J.L., Chudnow,R.S., van Coster,R., Lagae,L.,
            Kisler,J., Sperner,J., van der Knaap,M.S., Schiffmann,R., Taft,R.J.
            and Vanderver,A.
  TITLE     A de novo mutation in the beta-tubulin gene TUBB4A results in the
            leukoencephalopathy hypomyelination with atrophy of the basal
            ganglia and cerebellum
  JOURNAL   Am J Hum Genet 92 (5), 767-773 (2013)
   PUBMED   23582646
  REMARK    GeneRIF: A de novo mutation in the beta-tubulin gene TUBB4A results
            in the leukoencephalopathy hypomyelination with atrophy of the
            basal ganglia and cerebellum.
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Hersheson,J., Mencacci,N.E., Davis,M., MacDonald,N., Trabzuni,D.,
            Ryten,M., Pittman,A., Paudel,R., Kara,E., Fawcett,K., Plagnol,V.,
            Bhatia,K.P., Medlar,A.J., Stanescu,H.C., Hardy,J., Kleta,R.,
            Wood,N.W. and Houlden,H.
  TITLE     Mutations in the autoregulatory domain of beta-tubulin 4a cause
            hereditary dystonia
  JOURNAL   Ann Neurol 73 (4), 546-553 (2013)
   PUBMED   23424103
  REMARK    GeneRIF: This study demonistrated that TUBB4A mutation in the
            autoregulatory domain cause hereditary dystonia.
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Nahhas,N., Conant,A., Hamilton,E., Curiel,J., Simons,C., van der
            Knaap,M. and Vanderver,A.
  TITLE     TUBB4A-Related Leukodystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27809427
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Wang,D., Villasante,A., Lewis,S.A. and Cowan,N.J.
  TITLE     The mammalian beta-tubulin repertoire: hematopoietic expression of
            a novel, heterologous beta-tubulin isotype
  JOURNAL   J Cell Biol 103 (5), 1903-1910 (1986)
   PUBMED   3782288
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Lee,M.G., Loomis,C. and Cowan,N.J.
  TITLE     Sequence of an expressed human beta-tubulin gene containing ten Alu
            family members
  JOURNAL   Nucleic Acids Res 12 (14), 5823-5836 (1984)
   PUBMED   6462917
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA265791.1 and BC013683.1.
            
            On Jan 16, 2014 this sequence version replaced XP_005259534.1.
            
            Summary: This gene encodes a member of the beta tubulin family.
            Beta tubulins are one of two core protein families (alpha and beta
            tubulins) that heterodimerize and assemble to form microtubules.
            Mutations in this gene cause hypomyelinating leukodystrophy-6 and
            autosomal dominant torsion dystonia-4. Alternate splicing results
            in multiple transcript variants encoding different isoforms. A
            pseudogene of this gene is found on chromosome X. [provided by
            RefSeq, Jan 2014].
            
            Transcript Variant: This variant (5) has multiple differences,
            compared to variant 1. These differences result in a distinct 5'
            UTR and translation initiation at a downstream start codon,
            compared to variant 1. The resulting isoform (4) has a shorter
            N-terminus, compared to isoform 1. Both variants 5 and 6 encode the
            same isoform 4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1498827.1,
                                           SRR18074969.3245446.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..372
                     /product="tubulin beta-4A chain isoform 4"
                     /note="tubulin, beta, 5; dystonia 4, torsion (autosomal
                     dominant); tubulin beta-4 chain; tubulin, beta 4"
                     /calculated_mol_wt=41513
     Region          1..355
                     /region_name="PLN00220"
                     /note="tubulin beta chain; Provisional"
                     /db_xref="CDD:215107"
     CDS             1..372
                     /gene="TUBB4A"
                     /gene_synonym="beta-5; DYT4; TUBB4"
                     /coded_by="NM_001289130.2:271..1389"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:10382"
                     /db_xref="HGNC:HGNC:20774"
                     /db_xref="MIM:602662"
ORIGIN      
        1 mdsvrsgpfg qifrpdnfvf gqsgagnnwa kghytegael vdavldvvrk eaescdclqg
       61 fqlthslggg tgsgmgtlli skireefpdr imntfsvvps pkvsdtvvep ynatlsvhql
      121 ventdetyci dnealydicf rtlklttpty gdlnhlvsat msgvttclrf pgqlnadlrk
      181 lavnmvpfpr lhffmpgfap ltsrgsqqyr altvpeltqq mfdaknmmaa cdprhgrylt
      241 vaavfrgrms mkevdeqmls vqsknssyfv ewipnnvkta vcdipprglk maatfignst
      301 aiqelfkris eqftamfrrk aflhwytgeg mdemefteae snmndlvsey qqyqdataee
      361 gefeeeaeee va
//
LOCUS       NP_001372997             859 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 3 [Homo sapiens].
ACCESSION   NP_001372997
VERSION     NP_001372997.1
DBSOURCE    REFSEQ: accession NM_001386068.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 859)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 859)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 859)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 859)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 859)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 859)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 859)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 859)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157936.12, AL353768.28 and
            AL354893.14.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..859
                     /product="aminopeptidase O isoform 3"
                     /calculated_mol_wt=97717
     Region          <244..652
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     Site            586
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:P15144; propagated from
                     UniProtKB/Swiss-Prot (Q8N6M6.2)"
     Region          689..699
                     /region_name="Nucleolar localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q8BXQ6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6M6.2)"
     Region          721..>771
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
     CDS             1..859
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_001386068.1:370..2949"
                     /note="isoform 3 is encoded by transcript variant 10"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mdiqldpard dlplmantsh ilvkhyvldl dvdfesqvie gtivlfledg nrfkkqnssi
       61 eeacqsesnk ackfgmpepc hipvtnartf ssemeyndfa icskgekdts dkdgnhdnqe
      121 hasgisssky ccdtgnhgse dfllvldccd lsvlkveevd vaavpglekf trspeltvvs
      181 eefrnqivre lvtlpanrwr eqldyyarcs qapgcgellf dtdtwslqir ktgaqtatdf
      241 phairiwykt kpegrsvtwt sdqsgrpcvy tvgspinnra lfpcqeppva mstwqatvra
      301 aasfvvlmsg ensakptqlw eecsswyyyv tmpmpastft iavgcwtemk metwssndla
      361 terpfspsea nfrhvgvcsh meypcrfqna sattqeiiph rvfapvcltg acqetllrli
      421 ppclsaahsv lgahpfsrld vlivpanfps lgmasphimf lsqsiltggn hlcgtrlche
      481 iahawfglai gardwteewl segfathled vfwataqqla pyeareqqel raclrwrrlq
      541 demqcspeem qvlrpskdkt ghtsdsgasv ikhglnpeki fmqvhylkgy fllrflakrl
      601 gdetyfsflr kfvhtfhgql ilsqdflqml lenipeekrl elsveniyqd wlessgipkp
      661 lqrerragae cglarqvrae vtkwigvnrr prkrkrreke evfekllpdq lvlllehlle
      721 qktlsprtlq slqrtyhlqd qdaevrhrwc elivkhkftk ayksverflq edqerpqqds
      781 firlllawgt rleltldikg gimwllkpsa hspvhilvll fprgwsqpgt hkrqilvnaa
      841 slpggcllpw iwsgaalrf
//
LOCUS       NP_001373005             732 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 14 [Homo sapiens].
ACCESSION   NP_001373005
VERSION     NP_001373005.1
DBSOURCE    REFSEQ: accession NM_001386076.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 732)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 732)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 732)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 732)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 732)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 732)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 732)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 732)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 732)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 732)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157936.12 and AL353768.28.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1968968, SAMEA2142853
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..732
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..732
                     /product="aminopeptidase O isoform 14"
                     /calculated_mol_wt=82971
     Region          <244..652
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     Site            586
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:P15144; propagated from
                     UniProtKB/Swiss-Prot (Q8N6M6.2)"
     Region          689..699
                     /region_name="Nucleolar localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q8BXQ6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6M6.2)"
     CDS             1..732
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_001386076.1:189..2387"
                     /note="isoform 14 is encoded by transcript variant 18"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mdiqldpard dlplmantsh ilvkhyvldl dvdfesqvie gtivlfledg nrfkkqnssi
       61 eeacqsesnk ackfgmpepc hipvtnartf ssemeyndfa icskgekdts dkdgnhdnqe
      121 hasgisssky ccdtgnhgse dfllvldccd lsvlkveevd vaavpglekf trspeltvvs
      181 eefrnqivre lvtlpanrwr eqldyyarcs qapgcgellf dtdtwslqir ktgaqtatdf
      241 phairiwykt kpegrsvtwt sdqsgrpcvy tvgspinnra lfpcqeppva mstwqatvra
      301 aasfvvlmsg ensakptqlw eecsswyyyv tmpmpastft iavgcwtemk metwssndla
      361 terpfspsea nfrhvgvcsh meypcrfqna sattqeiiph rvfapvcltg acqetllrli
      421 ppclsaahsv lgahpfsrld vlivpanfps lgmasphimf lsqsiltggn hlcgtrlche
      481 iahawfglai gardwteewl segfathled vfwataqqla pyeareqqel raclrwrrlq
      541 demqcspeem qvlrpskdkt ghtsdsgasv ikhglnpeki fmqvhylkgy fllrflakrl
      601 gdetyfsflr kfvhtfhgql ilsqdflqml lenipeekrl elsveniyqd wlessgipkp
      661 lqrerragae cglarqvrae vtkwigvnrr prkrkrreke evfektesrs vaqaevqwrd
      721 ldslqppppr fe
//
LOCUS       NP_001958                407 aa            linear   PRI 15-DEC-2025
DEFINITION  eukaryotic initiation factor 4A-II [Homo sapiens].
ACCESSION   NP_001958
VERSION     NP_001958.2
DBSOURCE    REFSEQ: accession NM_001967.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Harrer,P., Skorvanek,M., Kittke,V., Dzinovic,I., Borngraber,F.,
            Thomsen,M., Mandel,V., Svorenova,T., Ostrozovicova,M.,
            Kulcsarova,K., Berutti,R., Busch,H., Ott,F., Kopajtich,R.,
            Prokisch,H., Kumar,K.R., Mencacci,N.E., Kurian,M.A., Di Fonzo,A.,
            Boesch,S., Kuhn,A.A., Blumlein,U., Lohmann,K., Haslinger,B.,
            Weise,D., Jech,R., Winkelmann,J. and Zech,M.
  TITLE     Dystonia Linked to EIF4A2 Haploinsufficiency: A Disorder of Protein
            Translation Dysfunction
  JOURNAL   Mov Disord 38 (10), 1914-1924 (2023)
   PUBMED   37485550
  REMARK    GeneRIF: Dystonia Linked to EIF4A2 Haploinsufficiency: A Disorder
            of Protein Translation Dysfunction.
REFERENCE   2  (residues 1 to 407)
  AUTHORS   O'Sullivan,M.H. and Fraser,C.S.
  TITLE     Monitoring RNA restructuring in a human cell-free extract reveals
            eIF4A-dependent and eIF4A-independent unwinding activity
  JOURNAL   J Biol Chem 299 (7), 104936 (2023)
   PUBMED   37331603
  REMARK    GeneRIF: Monitoring RNA restructuring in a human cell-free extract
            reveals eIF4A-dependent and eIF4A-independent unwinding activity.
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Paul,M.S., Duncan,A.R., Genetti,C.A., Pan,H., Jackson,A.,
            Grant,P.E., Shi,J., Pinelli,M., Brunetti-Pierri,N.,
            Garza-Flores,A., Shahani,D., Saneto,R.P., Zampino,G., Leoni,C.,
            Agolini,E., Novelli,A., Blumlein,U., Haack,T.B., Heinritz,W.,
            Matzker,E., Alhaddad,B., Abou Jamra,R., Bartolomaeus,T.,
            AlHamdan,S., Carapito,R., Isidor,B., Bahram,S., Ritter,A.,
            Izumi,K., Shakked,B.P., Barel,O., Ben Zeev,B., Begtrup,A.,
            Carere,D.A., Mullegama,S.V., Palculict,T.B., Calame,D.G.,
            Schwan,K., Aycinena,A.R.P., Traberg,R., Douzgou,S., Pirt,H.,
            Ismayilova,N., Banka,S., Chao,H.T. and Agrawal,P.B.
  CONSRTM   Genomics England Research Consortium
  TITLE     Rare EIF4A2 variants are associated with a neurodevelopmental
            disorder characterized by intellectual disability, hypotonia, and
            epilepsy
  JOURNAL   Am J Hum Genet 110 (1), 120-145 (2023)
   PUBMED   36528028
  REMARK    GeneRIF: Rare EIF4A2 variants are associated with a
            neurodevelopmental disorder characterized by intellectual
            disability, hypotonia, and epilepsy.
            Erratum:[Am J Hum Genet. 2023 Mar 2;110(3):548. doi:
            10.1016/j.ajhg.2023.02.010. PMID: 36868207]
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Li,W., Belsham,G.J. and Proud,C.G.
  TITLE     Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually
            interact in a 1:1 ratio in vivo
  JOURNAL   J Biol Chem 276 (31), 29111-29115 (2001)
   PUBMED   11408474
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Marcotrigiano,J., Lomakin,I.B., Sonenberg,N., Pestova,T.V.,
            Hellen,C.U. and Burley,S.K.
  TITLE     A conserved HEAT domain within eIF4G directs assembly of the
            translation initiation machinery
  JOURNAL   Mol Cell 7 (1), 193-203 (2001)
   PUBMED   11172724
REFERENCE   8  (residues 1 to 407)
  AUTHORS   Sudo,K., Takahashi,E. and Nakamura,Y.
  TITLE     Isolation and mapping of the human EIF4A2 gene homologous to the
            murine protein synthesis initiation factor 4A-II gene Eif4a2
  JOURNAL   Cytogenet Cell Genet 71 (4), 385-388 (1995)
   PUBMED   8521730
REFERENCE   9  (residues 1 to 407)
  AUTHORS   Yoder-Hill,J., Pause,A., Sonenberg,N. and Merrick,W.C.
  TITLE     The p46 subunit of eukaryotic initiation factor (eIF)-4F exchanges
            with eIF-4A
  JOURNAL   J Biol Chem 268 (8), 5566-5573 (1993)
   PUBMED   8449919
REFERENCE   10 (residues 1 to 407)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AL556981.3, D30655.1, BC015842.1 and BC013708.1.
            
            On Dec 16, 2005 this sequence version replaced NP_001958.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.451881.1,
                                           SRR3476690.1008.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323963.10/ ENSP00000326381.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.3"
     Protein         1..407
                     /product="eukaryotic initiation factor 4A-II"
                     /EC_number="3.6.4.13"
                     /note="ATP-dependent RNA helicase eIF4A-2"
                     /calculated_mol_wt=46271
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14240.2)"
     Region          21..407
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Region          33..61
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14240.2)"
     Site            order(35,53,55,60,79..85)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350804"
     Site            order(36,46,49,54)
                     /site_type="other"
                     /note="eIF4G interface [polypeptide binding]"
                     /db_xref="CDD:350804"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14240.2)"
     Region          183..186
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14240.2)"
     CDS             1..407
                     /gene="EIF4A2"
                     /gene_synonym="BM-010; DDX2B; eIF-4A-II; EIF4A; eIF4A-II;
                     EIF4F; NEDHSS"
                     /coded_by="NM_001967.4:35..1258"
                     /db_xref="CCDS:CCDS3282.1"
                     /db_xref="GeneID:1974"
                     /db_xref="HGNC:HGNC:3284"
                     /db_xref="MIM:601102"
ORIGIN      
        1 msggsadynr ehggpegmdp dgviesnwne ivdnfddmnl kesllrgiya ygfekpsaiq
       61 qraiipcikg ydviaqaqsg tgktatfais ilqqleiefk etqalvlapt relaqqiqkv
      121 ilalgdymga tchaciggtn vrnemqklqa eaphivvgtp grvfdmlnrr ylspkwikmf
      181 vldeademls rgfkdqiyei fqklntsiqv vllsatmptd vlevtkkfmr dpirilvkke
      241 eltlegikqf yinvereewk ldtlcdlyet ltitqavifl ntrrkvdwlt ekmhardftv
      301 salhgdmdqk erdvimrefr sgssrvlitt dllargidvq qvslvinydl ptnrenyihr
      361 igrggrfgrk gvainfvtee dkrilrdiet fynttveemp mnvadli
//
LOCUS       NP_536338                695 aa            linear   PRI 15-DEC-2025
DEFINITION  vacuolar protein sorting-associated protein 16 homolog isoform 3
            [Homo sapiens].
ACCESSION   NP_536338
VERSION     NP_536338.1
DBSOURCE    REFSEQ: accession NM_080413.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Monfrini,E., Avanzino,L., Palermo,G., Bonato,G., Brescia,G.,
            Ceravolo,R., Cantarella,G., Mandich,P., Prokisch,H., Storm Van's
            Gravesande,K., Straccia,G., Elia,A., Reale,C., Panteghini,C.,
            Zorzi,G., Eleopra,R., Erro,R., Carecchio,M., Garavaglia,B.,
            Zech,M., Romito,L. and Di Fonzo,A.
  TITLE     Dominant VPS16 Pathogenic Variants: Not Only Isolated Dystonia
  JOURNAL   Mov Disord Clin Pract 11 (1), 87-93 (2024)
   PUBMED   38291845
  REMARK    GeneRIF: Dominant VPS16 Pathogenic Variants: Not Only Isolated
            Dystonia.
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Zhang,S., Tong,M., Zheng,D., Huang,H., Li,L., Ungermann,C., Pan,Y.,
            Luo,H., Lei,M., Tang,Z., Fu,W., Chen,S., Liu,X. and Zhong,Q.
  TITLE     C9orf72-catalyzed GTP loading of Rab39A enables HOPS-mediated
            membrane tethering and fusion in mammalian autophagy
  JOURNAL   Nat Commun 14 (1), 6360 (2023)
   PUBMED   37821429
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Gong,X., Chen,T., Lin,C., Ping,H., Tong,X., Zhang,K., Chen,Z.,
            Cai,C., Lu,Z. and Ke,H.
  TITLE     Bioinformatics Analysis of the Prognostic Significance of VPS16 in
            Hepatocellular Carcinoma and Its Role in Drug Screening
  JOURNAL   Biomed Res Int 2023, 2501596 (2023)
   PUBMED   37124933
  REMARK    GeneRIF: Bioinformatics Analysis of the Prognostic Significance of
            VPS16 in Hepatocellular Carcinoma and Its Role in Drug Screening.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 695)
  AUTHORS   Zhang,B., Ma,Y., Niu,H. and Liu,Z.
  TITLE     Overexpression of VPS16 correlates with tumor progression and
            chemoresistance in colorectal cancer
  JOURNAL   Biochem Biophys Res Commun 607, 81-88 (2022)
   PUBMED   35367832
  REMARK    GeneRIF: Overexpression of VPS16 correlates with tumor progression
            and chemoresistance in colorectal cancer.
REFERENCE   6  (residues 1 to 695)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   7  (residues 1 to 695)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   8  (residues 1 to 695)
  AUTHORS   Kim,B.Y., Kramer,H., Yamamoto,A., Kominami,E., Kohsaka,S. and
            Akazawa,C.
  TITLE     Molecular characterization of mammalian homologues of class C Vps
            proteins that interact with syntaxin-7
  JOURNAL   J Biol Chem 276 (31), 29393-29402 (2001)
   PUBMED   11382755
REFERENCE   9  (residues 1 to 695)
  AUTHORS   Huizing,M., Didier,A., Walenta,J., Anikster,Y., Gahl,W.A. and
            Kramer,H.
  TITLE     Molecular cloning and characterization of human VPS18, VPS 11,
            VPS16, and VPS33
  JOURNAL   Gene 264 (2), 241-247 (2001)
   PUBMED   11250079
REFERENCE   10 (residues 1 to 695)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN483115.1, AK055787.1 and
            BC021291.2.
            
            Summary: Vesicle mediated protein sorting plays an important role
            in segregation of intracellular molecules into distinct organelles.
            Genetic studies in yeast have identified more than 40 vacuolar
            protein sorting (VPS) genes involved in vesicle transport to
            vacuoles. This gene encodes the human homolog of yeast class C
            Vps16 protein. The mammalian class C Vps proteins are predominantly
            associated with late endosomes/lysosomes, and like their yeast
            counterparts, may mediate vesicle trafficking steps in the
            endosome/lysosome pathway. Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2009].
            
            Transcript Variant: This variant (3) lacks an internal sequence
            segment compared to transcript variant 1. It thus encodes a shorter
            isoform (3) which is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK055787.1, SRR14038194.4468983.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..695
                     /product="vacuolar protein sorting-associated protein 16
                     homolog isoform 3"
                     /note="vacuolar protein sorting protein 16; vacuolar
                     protein sorting-associated protein 16 homolog; vacuolar
                     protein sorting 16 homolog; VPS16, CORVET/HOPS core
                     subunit"
                     /calculated_mol_wt=78169
     Region          4..>301
                     /region_name="Vps16_N"
                     /note="Vps16, N-terminal region; pfam04841"
                     /db_xref="CDD:252829"
     Region          373..691
                     /region_name="Vps16_C"
                     /note="Vps16, C-terminal region; pfam04840"
                     /db_xref="CDD:282668"
     CDS             1..695
                     /gene="VPS16"
                     /gene_synonym="DYT30; hVPS16"
                     /coded_by="NM_080413.3:31..2118"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS13037.1"
                     /db_xref="GeneID:64601"
                     /db_xref="HGNC:HGNC:14584"
                     /db_xref="MIM:608550"
ORIGIN      
        1 mdcytanwnp lgdsafyrky elysmdwdlk eelrdclvaa apyggpiall rnpwrkekaa
       61 svrpvldiys asgmplasll wksgpvvslg wsaeeellcv qedgavlvyg lhgdfrrhfs
      121 mgnevlqnrv ldarifhtef gsgvailtga hrftlsanvg dlklrrmpev pglqsapscw
      181 tvlcqdrvah illavgpdly lldhaacsav tppglapgvs sflqmavsft yrhlalftdt
      241 gyiwmgtasl keklcefncn irappkqmvw csrprskera vvvawerrlm vvgdapesiq
      301 ykqltiqvll drlvlrrlyp laiqiceylr lpevqgvsri lahwacykvq qkdvsdedva
      361 rainqklgdt pgvsysdiaa raygcgrtel aiklleyepr sgeqvplllk mkrsklalsk
      421 aiesgdtdlv ftvllhlkne lnrgdffmtl rnqpmalsly rqfckhqele tlkdlynqdd
      481 nhqelgsfhi rasyaaeeri egrvaalqta adafykakne faakatedqm rllrlqrrle
      541 delggqfldl slhdtvttli lgghnkraeq lardfripdk rlwwlkltal adledweele
      601 kfskskkspi gylpfveicm kqhnkyeakk yasrvgpeqk vkalllvgdv aqaadvaieh
      661 rneaelslvl shctgatdga tadkiqrara qaqkk
//
LOCUS       NP_116212                720 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 2 [Homo sapiens].
ACCESSION   NP_116212
VERSION     NP_116212.3
DBSOURCE    REFSEQ: accession NM_032823.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 720)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 720)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 720)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 720)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 720)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 720)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 720)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 720)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 720)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 720)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA521148.1, BC029616.1,
            AL354893.14 and AI982632.1.
            
            On Oct 31, 2002 this sequence version replaced NP_116212.2.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Transcript Variant: This variant (2) lacks two consecutive in-frame
            exons in the CDS, as compared to variant 1. The resulting isoform
            (2) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC029616.1, SRR14038192.3383625.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..720
                     /product="aminopeptidase O isoform 2"
                     /calculated_mol_wt=81975
     Region          <244..553
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     Region          622..719
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
     CDS             1..720
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_032823.6:189..2351"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6713.1"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mdiqldpard dlplmantsh ilvkhyvldl dvdfesqvie gtivlfledg nrfkkqnssi
       61 eeacqsesnk ackfgmpepc hipvtnartf ssemeyndfa icskgekdts dkdgnhdnqe
      121 hasgisssky ccdtgnhgse dfllvldccd lsvlkveevd vaavpglekf trspeltvvs
      181 eefrnqivre lvtlpanrwr eqldyyarcs qapgcgellf dtdtwslqir ktgaqtatdf
      241 phairiwykt kpegrsvtwt sdqsgrpcvy tvgspinnra lfpcqeppva mstwqatvra
      301 aasfvvlmsg ensakptqlw eecsswyyyv tmpmpastft iavgcwtemk metwssndla
      361 terpfspsea nfrhvgvcsh meypcrfqna sattqeiiph rvfapvcltg acqetllrli
      421 ppclsaahsv lgahpfsrld vlivpanfps lgmarpskdk tghtsdsgas vikhglnpek
      481 ifmqvhylkg yfllrflakr lgdetyfsfl rkfvhtfhgq lilsqdflqm llenipeekr
      541 lelsveniyq dwlessgipk plqrerraga ecglarqvra evtkwigvnr rprkrkrrek
      601 eevfekllpd qlvlllehll eqktlsprtl qslqrtyhlq dqdaevrhrw celivkhkft
      661 kayksverfl qedqamgvyl ygelmvseda rqqqlarrcf ertkeqmdrs saqvvaemlf
//
LOCUS       NP_001372992             773 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 7 [Homo sapiens].
ACCESSION   NP_001372992
VERSION     NP_001372992.1
DBSOURCE    REFSEQ: accession NM_001386063.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 773)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 773)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 773)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 773)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 773)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 773)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 773)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 773)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 773)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 773)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157936.12, AL353768.28 and
            AL354893.14.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2330791.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465421
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..773
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..773
                     /product="aminopeptidase O isoform 7"
                     /calculated_mol_wt=87885
     Region          <244..652
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     Region          675..772
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
     CDS             1..773
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_001386063.2:189..2510"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mdiqldpard dlplmantsh ilvkhyvldl dvdfesqvie gtivlfledg nrfkkqnssi
       61 eeacqsesnk ackfgmpepc hipvtnartf ssemeyndfa icskgekdts dkdgnhdnqe
      121 hasgisssky ccdtgnhgse dfllvldccd lsvlkveevd vaavpglekf trspeltvvs
      181 eefrnqivre lvtlpanrwr eqldyyarcs qapgcgellf dtdtwslqir ktgaqtatdf
      241 phairiwykt kpegrsvtwt sdqsgrpcvy tvgspinnra lfpcqeppva mstwqatvra
      301 aasfvvlmsg ensakptqlw eecsswyyyv tmpmpastft iavgcwtemk metwssndla
      361 terpfspsea nfrhvgvcsh meypcrfqna sattqeiiph rvfapvcltg acqetllrli
      421 ppclsaahsv lgahpfsrld vlivpanfps lgmasphimf lsqsiltggn hlcgtrlche
      481 iahawfglai gardwteewl segfathled vfwataqqla pyeareqqel raclrwrrlq
      541 demqcspeem qvlrpskdkt ghtsdsgasv ikhglnpeki fmqvhylkgy fllrflakrl
      601 gdetyfsflr kfvhtfhgql ilsqdflqml lenipeekrl elsveniyqd wlessgipkl
      661 lpdqlvllle hlleqktlsp rtlqslqrty hlqdqdaevr hrwcelivkh kftkayksve
      721 rflqedqamg vylygelmvs edarqqqlar rcfertkeqm drssaqvvae mlf
//
LOCUS       NP_001276056             489 aa            linear   PRI 15-DEC-2025
DEFINITION  tubulin beta-4A chain isoform 2 [Homo sapiens].
ACCESSION   NP_001276056
VERSION     NP_001276056.1
DBSOURCE    REFSEQ: accession NM_001289127.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Garg,D., Holla,V.V., Ganguly,J., Rajan,R., Saini,A., Agarwal,A.,
            Radhakrishnan,D.M., Basu,P., Mondal,B., Dhar,D., Kamble,N.,
            Yadav,R., Muthusamy,B., Kumar,H., Srivastava,A.K. and Pal,P.K.
  TITLE     Expanding the phenotypic and genotypic spectrum of DYT-TUBB4A with
            seven patients from India
  JOURNAL   Parkinsonism Relat Disord 124, 107012 (2024)
   PUBMED   38762926
  REMARK    GeneRIF: Expanding the phenotypic and genotypic spectrum of
            DYT-TUBB4A with seven patients from India.
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Ben Jdila,M., Kammoun,F., Abdelmaksoud-Dammak,R., Triki,C. and
            Fakhfakh,F.
  TITLE     Mutation in the beta-tubulin gene TUBB4A results in epileptic
            encephalopathy associated with hypomyelinated leucodystrophy:
            Unexpected findings reveal genetic mosaicism
  JOURNAL   Int J Dev Neurosci 83 (6), 532-545 (2023)
   PUBMED   37529938
  REMARK    GeneRIF: Mutation in the beta-tubulin gene TUBB4A results in
            epileptic encephalopathy associated with hypomyelinated
            leucodystrophy: Unexpected findings reveal genetic mosaicism.
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Simons,C., Wolf,N.I., McNeil,N., Caldovic,L., Devaney,J.M.,
            Takanohashi,A., Crawford,J., Ru,K., Grimmond,S.M., Miller,D.,
            Tonduti,D., Schmidt,J.L., Chudnow,R.S., van Coster,R., Lagae,L.,
            Kisler,J., Sperner,J., van der Knaap,M.S., Schiffmann,R., Taft,R.J.
            and Vanderver,A.
  TITLE     A de novo mutation in the beta-tubulin gene TUBB4A results in the
            leukoencephalopathy hypomyelination with atrophy of the basal
            ganglia and cerebellum
  JOURNAL   Am J Hum Genet 92 (5), 767-773 (2013)
   PUBMED   23582646
  REMARK    GeneRIF: A de novo mutation in the beta-tubulin gene TUBB4A results
            in the leukoencephalopathy hypomyelination with atrophy of the
            basal ganglia and cerebellum.
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Hersheson,J., Mencacci,N.E., Davis,M., MacDonald,N., Trabzuni,D.,
            Ryten,M., Pittman,A., Paudel,R., Kara,E., Fawcett,K., Plagnol,V.,
            Bhatia,K.P., Medlar,A.J., Stanescu,H.C., Hardy,J., Kleta,R.,
            Wood,N.W. and Houlden,H.
  TITLE     Mutations in the autoregulatory domain of beta-tubulin 4a cause
            hereditary dystonia
  JOURNAL   Ann Neurol 73 (4), 546-553 (2013)
   PUBMED   23424103
  REMARK    GeneRIF: This study demonistrated that TUBB4A mutation in the
            autoregulatory domain cause hereditary dystonia.
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Nahhas,N., Conant,A., Hamilton,E., Curiel,J., Simons,C., van der
            Knaap,M. and Vanderver,A.
  TITLE     TUBB4A-Related Leukodystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27809427
REFERENCE   6  (residues 1 to 489)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   7  (residues 1 to 489)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   8  (residues 1 to 489)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   9  (residues 1 to 489)
  AUTHORS   Wang,D., Villasante,A., Lewis,S.A. and Cowan,N.J.
  TITLE     The mammalian beta-tubulin repertoire: hematopoietic expression of
            a novel, heterologous beta-tubulin isotype
  JOURNAL   J Cell Biol 103 (5), 1903-1910 (1986)
   PUBMED   3782288
REFERENCE   10 (residues 1 to 489)
  AUTHORS   Lee,M.G., Loomis,C. and Cowan,N.J.
  TITLE     Sequence of an expressed human beta-tubulin gene containing ten Alu
            family members
  JOURNAL   Nucleic Acids Res 12 (14), 5823-5836 (1984)
   PUBMED   6462917
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010503.8, DC354036.1,
            AK075307.1 and BC013683.1.
            
            Summary: This gene encodes a member of the beta tubulin family.
            Beta tubulins are one of two core protein families (alpha and beta
            tubulins) that heterodimerize and assemble to form microtubules.
            Mutations in this gene cause hypomyelinating leukodystrophy-6 and
            autosomal dominant torsion dystonia-4. Alternate splicing results
            in multiple transcript variants encoding different isoforms. A
            pseudogene of this gene is found on chromosome X. [provided by
            RefSeq, Jan 2014].
            
            Transcript Variant: This variant (2) has an alternate splice site
            in the 5' coding region, compared to variant 1. The resulting
            isoform (2) lacks an internal segment, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.216870.1,
                                           SRR1803615.177865.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN03267753
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..489
                     /product="tubulin beta-4A chain isoform 2"
                     /note="tubulin, beta, 5; dystonia 4, torsion (autosomal
                     dominant); tubulin beta-4 chain; tubulin, beta 4"
                     /calculated_mol_wt=53714
     Region          46..472
                     /region_name="PLN00220"
                     /note="tubulin beta chain; Provisional"
                     /db_xref="CDD:215107"
     CDS             1..489
                     /gene="TUBB4A"
                     /gene_synonym="beta-5; DYT4; TUBB4"
                     /coded_by="NM_001289127.2:138..1607"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:10382"
                     /db_xref="HGNC:HGNC:20774"
                     /db_xref="MIM:602662"
ORIGIN      
        1 mrrgaadret egpcsavsaa sstlaaaaap rarataaast lsatamreiv hlqagqcgnq
       61 igakfwevis dehgidptgt yhgdsdlqle rinvyyneat ggnyvpravl vdlepgtmds
      121 vrsgpfgqif rpdnfvfgqs gagnnwakgh ytegaelvda vldvvrkeae scdclqgfql
      181 thslgggtgs gmgtlliski reefpdrimn tfsvvpspkv sdtvvepyna tlsvhqlven
      241 tdetycidne alydicfrtl klttptygdl nhlvsatmsg vttclrfpgq lnadlrklav
      301 nmvpfprlhf fmpgfaplts rgsqqyralt vpeltqqmfd aknmmaacdp rhgryltvaa
      361 vfrgrmsmke vdeqmlsvqs knssyfvewi pnnvktavcd ipprglkmaa tfignstaiq
      421 elfkriseqf tamfrrkafl hwytgegmde mefteaesnm ndlvseyqqy qdataeegef
      481 eeeaeeeva
//
LOCUS       NP_001180260             566 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 4 [Homo sapiens].
ACCESSION   NP_001180260
VERSION     NP_001180260.1
DBSOURCE    REFSEQ: accession NM_001193331.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 566)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 566)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 566)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 566)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 566)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA521148.1, AK057450.1,
            AK098242.1, AL353768.28 and BX099259.1.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Transcript Variant: This variant (4) lacks multiple 3' exons, but
            has an alternate 3' exon, as compared to variant 1. The resulting
            isoform (4) is much shorter and has a different C-terminus, as
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.609784.1,
                                           SRR14038194.2193331.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..566
                     /product="aminopeptidase O isoform 4"
                     /calculated_mol_wt=63232
     Region          <244..>509
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     CDS             1..566
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_001193331.3:189..1889"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS55327.1"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mdiqldpard dlplmantsh ilvkhyvldl dvdfesqvie gtivlfledg nrfkkqnssi
       61 eeacqsesnk ackfgmpepc hipvtnartf ssemeyndfa icskgekdts dkdgnhdnqe
      121 hasgisssky ccdtgnhgse dfllvldccd lsvlkveevd vaavpglekf trspeltvvs
      181 eefrnqivre lvtlpanrwr eqldyyarcs qapgcgellf dtdtwslqir ktgaqtatdf
      241 phairiwykt kpegrsvtwt sdqsgrpcvy tvgspinnra lfpcqeppva mstwqatvra
      301 aasfvvlmsg ensakptqlw eecsswyyyv tmpmpastft iavgcwtemk metwssndla
      361 terpfspsea nfrhvgvcsh meypcrfqna sattqeiiph rvfapvcltg acqetllrli
      421 ppclsaahsv lgahpfsrld vlivpanfps lgmasphimf lsqsiltggn hlcgtrlche
      481 iahawfglai gardwteewl segfathled vfwataqqla pyeareqqel raclrwrrlq
      541 demqcspeem qvlrfphvgg csgsfs
//
LOCUS       NP_072097                839 aa            linear   PRI 15-DEC-2025
DEFINITION  vacuolar protein sorting-associated protein 16 homolog isoform 1
            [Homo sapiens].
ACCESSION   NP_072097
VERSION     NP_072097.2
DBSOURCE    REFSEQ: accession NM_022575.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 839)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 839)
  AUTHORS   Monfrini,E., Avanzino,L., Palermo,G., Bonato,G., Brescia,G.,
            Ceravolo,R., Cantarella,G., Mandich,P., Prokisch,H., Storm Van's
            Gravesande,K., Straccia,G., Elia,A., Reale,C., Panteghini,C.,
            Zorzi,G., Eleopra,R., Erro,R., Carecchio,M., Garavaglia,B.,
            Zech,M., Romito,L. and Di Fonzo,A.
  TITLE     Dominant VPS16 Pathogenic Variants: Not Only Isolated Dystonia
  JOURNAL   Mov Disord Clin Pract 11 (1), 87-93 (2024)
   PUBMED   38291845
  REMARK    GeneRIF: Dominant VPS16 Pathogenic Variants: Not Only Isolated
            Dystonia.
REFERENCE   3  (residues 1 to 839)
  AUTHORS   Zhang,S., Tong,M., Zheng,D., Huang,H., Li,L., Ungermann,C., Pan,Y.,
            Luo,H., Lei,M., Tang,Z., Fu,W., Chen,S., Liu,X. and Zhong,Q.
  TITLE     C9orf72-catalyzed GTP loading of Rab39A enables HOPS-mediated
            membrane tethering and fusion in mammalian autophagy
  JOURNAL   Nat Commun 14 (1), 6360 (2023)
   PUBMED   37821429
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 839)
  AUTHORS   Gong,X., Chen,T., Lin,C., Ping,H., Tong,X., Zhang,K., Chen,Z.,
            Cai,C., Lu,Z. and Ke,H.
  TITLE     Bioinformatics Analysis of the Prognostic Significance of VPS16 in
            Hepatocellular Carcinoma and Its Role in Drug Screening
  JOURNAL   Biomed Res Int 2023, 2501596 (2023)
   PUBMED   37124933
  REMARK    GeneRIF: Bioinformatics Analysis of the Prognostic Significance of
            VPS16 in Hepatocellular Carcinoma and Its Role in Drug Screening.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 839)
  AUTHORS   Zhang,B., Ma,Y., Niu,H. and Liu,Z.
  TITLE     Overexpression of VPS16 correlates with tumor progression and
            chemoresistance in colorectal cancer
  JOURNAL   Biochem Biophys Res Commun 607, 81-88 (2022)
   PUBMED   35367832
  REMARK    GeneRIF: Overexpression of VPS16 correlates with tumor progression
            and chemoresistance in colorectal cancer.
REFERENCE   6  (residues 1 to 839)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   7  (residues 1 to 839)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   8  (residues 1 to 839)
  AUTHORS   Kim,B.Y., Kramer,H., Yamamoto,A., Kominami,E., Kohsaka,S. and
            Akazawa,C.
  TITLE     Molecular characterization of mammalian homologues of class C Vps
            proteins that interact with syntaxin-7
  JOURNAL   J Biol Chem 276 (31), 29393-29402 (2001)
   PUBMED   11382755
REFERENCE   9  (residues 1 to 839)
  AUTHORS   Huizing,M., Didier,A., Walenta,J., Anikster,Y., Gahl,W.A. and
            Kramer,H.
  TITLE     Molecular cloning and characterization of human VPS18, VPS 11,
            VPS16, and VPS33
  JOURNAL   Gene 264 (2), 241-247 (2001)
   PUBMED   11250079
REFERENCE   10 (residues 1 to 839)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU845142.1, AF308801.1 and
            BM468030.1.
            
            On Dec 26, 2001 this sequence version replaced NP_072097.1.
            
            Summary: Vesicle mediated protein sorting plays an important role
            in segregation of intracellular molecules into distinct organelles.
            Genetic studies in yeast have identified more than 40 vacuolar
            protein sorting (VPS) genes involved in vesicle transport to
            vacuoles. This gene encodes the human homolog of yeast class C
            Vps16 protein. The mammalian class C Vps proteins are predominantly
            associated with late endosomes/lysosomes, and like their yeast
            counterparts, may mediate vesicle trafficking steps in the
            endosome/lysosome pathway. Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2009].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.940372.1,
                                           SRR1163655.61091.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380445.8/ ENSP00000369810.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..839
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..839
                     /product="vacuolar protein sorting-associated protein 16
                     homolog isoform 1"
                     /note="vacuolar protein sorting protein 16; vacuolar
                     protein sorting-associated protein 16 homolog; vacuolar
                     protein sorting 16 homolog; VPS16, CORVET/HOPS core
                     subunit"
                     /calculated_mol_wt=94563
     Region          4..420
                     /region_name="Vps16_N"
                     /note="Vps16, N-terminal region; pfam04841"
                     /db_xref="CDD:252829"
     Region          517..835
                     /region_name="Vps16_C"
                     /note="Vps16, C-terminal region; pfam04840"
                     /db_xref="CDD:282668"
     Region          642..736
                     /region_name="Interaction with VPS33A.
                     /evidence=ECO:0000269|PubMed:23901104"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H269.2)"
     CDS             1..839
                     /gene="VPS16"
                     /gene_synonym="DYT30; hVPS16"
                     /coded_by="NM_022575.4:31..2550"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13036.1"
                     /db_xref="GeneID:64601"
                     /db_xref="HGNC:HGNC:14584"
                     /db_xref="MIM:608550"
ORIGIN      
        1 mdcytanwnp lgdsafyrky elysmdwdlk eelrdclvaa apyggpiall rnpwrkekaa
       61 svrpvldiys asgmplasll wksgpvvslg wsaeeellcv qedgavlvyg lhgdfrrhfs
      121 mgnevlqnrv ldarifhtef gsgvailtga hrftlsanvg dlklrrmpev pglqsapscw
      181 tvlcqdrvah illavgpdly lldhaacsav tppglapgvs sflqmavsft yrhlalftdt
      241 gyiwmgtasl keklcefncn irappkqmvw csrprskera vvvawerrlm vvgdapesiq
      301 fvldedsylv peldgvrifs rstheflhev paaseeifki asmapgalll eaqkeyekes
      361 qkadeylrei qelgqltqav qqcieaaghe hqpdmqksll raasfgkcfl drfppdsfvh
      421 mcqdlrvlna vrdyhigipl tysqykqlti qvlldrlvlr rlyplaiqic eylrlpevqg
      481 vsrilahwac ykvqqkdvsd edvarainqk lgdtpgvsys diaaraygcg rtelaiklle
      541 yeprsgeqvp lllkmkrskl alskaiesgd tdlvftvllh lknelnrgdf fmtlrnqpma
      601 lslyrqfckh qeletlkdly nqddnhqelg sfhirasyaa eeriegrvaa lqtaadafyk
      661 aknefaakat edqmrllrlq rrledelggq fldlslhdtv ttlilgghnk raeqlardfr
      721 ipdkrlwwlk ltaladledw eelekfsksk kspigylpfv eicmkqhnky eakkyasrvg
      781 peqkvkalll vgdvaqaadv aiehrneael slvlshctga tdgatadkiq raraqaqkk
//
LOCUS       NP_001372995             859 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 3 [Homo sapiens].
ACCESSION   NP_001372995 XP_011517421
VERSION     NP_001372995.1
DBSOURCE    REFSEQ: accession NM_001386066.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 859)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 859)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 859)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 859)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 859)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 859)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 859)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 859)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 859)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 859)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157936.12, AL353768.28 and
            AL354893.14.
            
            On Aug 6, 2020 this sequence version replaced XP_011517421.1.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.117521.1,
                                           SRR14038194.1408268.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..859
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..859
                     /product="aminopeptidase O isoform 3"
                     /calculated_mol_wt=97717
     Region          <244..652
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     Site            586
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:P15144; propagated from
                     UniProtKB/Swiss-Prot (Q8N6M6.2)"
     Region          689..699
                     /region_name="Nucleolar localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q8BXQ6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6M6.2)"
     Region          721..>771
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
     CDS             1..859
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_001386066.1:189..2768"
                     /note="isoform 3 is encoded by transcript variant 8"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mdiqldpard dlplmantsh ilvkhyvldl dvdfesqvie gtivlfledg nrfkkqnssi
       61 eeacqsesnk ackfgmpepc hipvtnartf ssemeyndfa icskgekdts dkdgnhdnqe
      121 hasgisssky ccdtgnhgse dfllvldccd lsvlkveevd vaavpglekf trspeltvvs
      181 eefrnqivre lvtlpanrwr eqldyyarcs qapgcgellf dtdtwslqir ktgaqtatdf
      241 phairiwykt kpegrsvtwt sdqsgrpcvy tvgspinnra lfpcqeppva mstwqatvra
      301 aasfvvlmsg ensakptqlw eecsswyyyv tmpmpastft iavgcwtemk metwssndla
      361 terpfspsea nfrhvgvcsh meypcrfqna sattqeiiph rvfapvcltg acqetllrli
      421 ppclsaahsv lgahpfsrld vlivpanfps lgmasphimf lsqsiltggn hlcgtrlche
      481 iahawfglai gardwteewl segfathled vfwataqqla pyeareqqel raclrwrrlq
      541 demqcspeem qvlrpskdkt ghtsdsgasv ikhglnpeki fmqvhylkgy fllrflakrl
      601 gdetyfsflr kfvhtfhgql ilsqdflqml lenipeekrl elsveniyqd wlessgipkp
      661 lqrerragae cglarqvrae vtkwigvnrr prkrkrreke evfekllpdq lvlllehlle
      721 qktlsprtlq slqrtyhlqd qdaevrhrwc elivkhkftk ayksverflq edqerpqqds
      781 firlllawgt rleltldikg gimwllkpsa hspvhilvll fprgwsqpgt hkrqilvnaa
      841 slpggcllpw iwsgaalrf
//
LOCUS       NP_001372999             820 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 10 [Homo sapiens].
ACCESSION   NP_001372999 XP_011517422
VERSION     NP_001372999.1
DBSOURCE    REFSEQ: accession NM_001386070.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 820)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 820)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 820)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 820)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 820)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 820)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 820)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 820)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 820)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157936.12, AL353768.28 and
            AL354893.14.
            
            On Aug 6, 2020 this sequence version replaced XP_011517422.1.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.217996.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..820
                     /product="aminopeptidase O isoform 10"
                     /calculated_mol_wt=93138
     Region          <244..652
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     Region          <706..>732
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
     CDS             1..820
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_001386070.1:189..2651"
                     /note="isoform 10 is encoded by transcript variant 12"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mdiqldpard dlplmantsh ilvkhyvldl dvdfesqvie gtivlfledg nrfkkqnssi
       61 eeacqsesnk ackfgmpepc hipvtnartf ssemeyndfa icskgekdts dkdgnhdnqe
      121 hasgisssky ccdtgnhgse dfllvldccd lsvlkveevd vaavpglekf trspeltvvs
      181 eefrnqivre lvtlpanrwr eqldyyarcs qapgcgellf dtdtwslqir ktgaqtatdf
      241 phairiwykt kpegrsvtwt sdqsgrpcvy tvgspinnra lfpcqeppva mstwqatvra
      301 aasfvvlmsg ensakptqlw eecsswyyyv tmpmpastft iavgcwtemk metwssndla
      361 terpfspsea nfrhvgvcsh meypcrfqna sattqeiiph rvfapvcltg acqetllrli
      421 ppclsaahsv lgahpfsrld vlivpanfps lgmasphimf lsqsiltggn hlcgtrlche
      481 iahawfglai gardwteewl segfathled vfwataqqla pyeareqqel raclrwrrlq
      541 demqcspeem qvlrpskdkt ghtsdsgasv ikhglnpeki fmqvhylkgy fllrflakrl
      601 gdetyfsflr kfvhtfhgql ilsqdflqml lenipeekrl elsveniyqd wlessgipkp
      661 lqrerragae cglarqvrae vtkwigvnrr prkrkrreke evfekvrhrw celivkhkft
      721 kayksverfl qedqerpqqd sfirlllawg trleltldik ggimwllkps ahspvhilvl
      781 lfprgwsqpg thkrqilvna aslpggcllp wiwsgaalrf
//
LOCUS       NP_001373004             819 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 1 [Homo sapiens].
ACCESSION   NP_001373004 XP_016870719
VERSION     NP_001373004.1
DBSOURCE    REFSEQ: accession NM_001386075.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 819)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 819)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 819)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 819)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 819)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 819)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 819)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157936.12, AL353768.28 and
            AL354893.14.
            
            On Aug 6, 2020 this sequence version replaced XP_016870719.1.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.324793.1,
                                           SRR14038193.2154021.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..819
                     /product="aminopeptidase O isoform 1"
                     /calculated_mol_wt=93442
     Region          <244..652
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     Site            586
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:P15144; propagated from
                     UniProtKB/Swiss-Prot (Q8N6M6.2)"
     Region          689..699
                     /region_name="Nucleolar localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q8BXQ6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6M6.2)"
     Region          721..818
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
     CDS             1..819
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_001386075.1:189..2648"
                     /note="isoform 1 is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS55328.1"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mdiqldpard dlplmantsh ilvkhyvldl dvdfesqvie gtivlfledg nrfkkqnssi
       61 eeacqsesnk ackfgmpepc hipvtnartf ssemeyndfa icskgekdts dkdgnhdnqe
      121 hasgisssky ccdtgnhgse dfllvldccd lsvlkveevd vaavpglekf trspeltvvs
      181 eefrnqivre lvtlpanrwr eqldyyarcs qapgcgellf dtdtwslqir ktgaqtatdf
      241 phairiwykt kpegrsvtwt sdqsgrpcvy tvgspinnra lfpcqeppva mstwqatvra
      301 aasfvvlmsg ensakptqlw eecsswyyyv tmpmpastft iavgcwtemk metwssndla
      361 terpfspsea nfrhvgvcsh meypcrfqna sattqeiiph rvfapvcltg acqetllrli
      421 ppclsaahsv lgahpfsrld vlivpanfps lgmasphimf lsqsiltggn hlcgtrlche
      481 iahawfglai gardwteewl segfathled vfwataqqla pyeareqqel raclrwrrlq
      541 demqcspeem qvlrpskdkt ghtsdsgasv ikhglnpeki fmqvhylkgy fllrflakrl
      601 gdetyfsflr kfvhtfhgql ilsqdflqml lenipeekrl elsveniyqd wlessgipkp
      661 lqrerragae cglarqvrae vtkwigvnrr prkrkrreke evfekllpdq lvlllehlle
      721 qktlsprtlq slqrtyhlqd qdaevrhrwc elivkhkftk ayksverflq edqamgvyly
      781 gelmvsedar qqqlarrcfe rtkeqmdrss aqvvaemlf
//
LOCUS       NP_001276058             444 aa            linear   PRI 15-DEC-2025
DEFINITION  tubulin beta-4A chain isoform 3 [Homo sapiens].
ACCESSION   NP_001276058
VERSION     NP_001276058.1
DBSOURCE    REFSEQ: accession NM_001289129.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Garg,D., Holla,V.V., Ganguly,J., Rajan,R., Saini,A., Agarwal,A.,
            Radhakrishnan,D.M., Basu,P., Mondal,B., Dhar,D., Kamble,N.,
            Yadav,R., Muthusamy,B., Kumar,H., Srivastava,A.K. and Pal,P.K.
  TITLE     Expanding the phenotypic and genotypic spectrum of DYT-TUBB4A with
            seven patients from India
  JOURNAL   Parkinsonism Relat Disord 124, 107012 (2024)
   PUBMED   38762926
  REMARK    GeneRIF: Expanding the phenotypic and genotypic spectrum of
            DYT-TUBB4A with seven patients from India.
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Ben Jdila,M., Kammoun,F., Abdelmaksoud-Dammak,R., Triki,C. and
            Fakhfakh,F.
  TITLE     Mutation in the beta-tubulin gene TUBB4A results in epileptic
            encephalopathy associated with hypomyelinated leucodystrophy:
            Unexpected findings reveal genetic mosaicism
  JOURNAL   Int J Dev Neurosci 83 (6), 532-545 (2023)
   PUBMED   37529938
  REMARK    GeneRIF: Mutation in the beta-tubulin gene TUBB4A results in
            epileptic encephalopathy associated with hypomyelinated
            leucodystrophy: Unexpected findings reveal genetic mosaicism.
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Simons,C., Wolf,N.I., McNeil,N., Caldovic,L., Devaney,J.M.,
            Takanohashi,A., Crawford,J., Ru,K., Grimmond,S.M., Miller,D.,
            Tonduti,D., Schmidt,J.L., Chudnow,R.S., van Coster,R., Lagae,L.,
            Kisler,J., Sperner,J., van der Knaap,M.S., Schiffmann,R., Taft,R.J.
            and Vanderver,A.
  TITLE     A de novo mutation in the beta-tubulin gene TUBB4A results in the
            leukoencephalopathy hypomyelination with atrophy of the basal
            ganglia and cerebellum
  JOURNAL   Am J Hum Genet 92 (5), 767-773 (2013)
   PUBMED   23582646
  REMARK    GeneRIF: A de novo mutation in the beta-tubulin gene TUBB4A results
            in the leukoencephalopathy hypomyelination with atrophy of the
            basal ganglia and cerebellum.
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Hersheson,J., Mencacci,N.E., Davis,M., MacDonald,N., Trabzuni,D.,
            Ryten,M., Pittman,A., Paudel,R., Kara,E., Fawcett,K., Plagnol,V.,
            Bhatia,K.P., Medlar,A.J., Stanescu,H.C., Hardy,J., Kleta,R.,
            Wood,N.W. and Houlden,H.
  TITLE     Mutations in the autoregulatory domain of beta-tubulin 4a cause
            hereditary dystonia
  JOURNAL   Ann Neurol 73 (4), 546-553 (2013)
   PUBMED   23424103
  REMARK    GeneRIF: This study demonistrated that TUBB4A mutation in the
            autoregulatory domain cause hereditary dystonia.
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Nahhas,N., Conant,A., Hamilton,E., Curiel,J., Simons,C., van der
            Knaap,M. and Vanderver,A.
  TITLE     TUBB4A-Related Leukodystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27809427
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   8  (residues 1 to 444)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   9  (residues 1 to 444)
  AUTHORS   Wang,D., Villasante,A., Lewis,S.A. and Cowan,N.J.
  TITLE     The mammalian beta-tubulin repertoire: hematopoietic expression of
            a novel, heterologous beta-tubulin isotype
  JOURNAL   J Cell Biol 103 (5), 1903-1910 (1986)
   PUBMED   3782288
REFERENCE   10 (residues 1 to 444)
  AUTHORS   Lee,M.G., Loomis,C. and Cowan,N.J.
  TITLE     Sequence of an expressed human beta-tubulin gene containing ten Alu
            family members
  JOURNAL   Nucleic Acids Res 12 (14), 5823-5836 (1984)
   PUBMED   6462917
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010503.8, DC353527.1 and
            BC013683.1.
            
            Summary: This gene encodes a member of the beta tubulin family.
            Beta tubulins are one of two core protein families (alpha and beta
            tubulins) that heterodimerize and assemble to form microtubules.
            Mutations in this gene cause hypomyelinating leukodystrophy-6 and
            autosomal dominant torsion dystonia-4. Alternate splicing results
            in multiple transcript variants encoding different isoforms. A
            pseudogene of this gene is found on chromosome X. [provided by
            RefSeq, Jan 2014].
            
            Transcript Variant: This variant (4) has an alternate splice site
            in the 5' region, which results in translation initiation at a
            downstream AUG codon, compared to variant 1. The resulting isoform
            (3) has a shorter N-terminus, compared to isoform 1. Both variants
            3 and 4 encode the same isoform 3.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DC353527.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN03267753
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..444
                     /product="tubulin beta-4A chain isoform 3"
                     /note="tubulin, beta, 5; dystonia 4, torsion (autosomal
                     dominant); tubulin beta-4 chain; tubulin, beta 4"
                     /calculated_mol_wt=49455
     Region          1..427
                     /region_name="PLN00220"
                     /note="tubulin beta chain; Provisional"
                     /db_xref="CDD:215107"
     Region          1..4
                     /region_name="MREI motif.
                     /evidence=ECO:0000250|UniProtKB:P07437"
                     /note="propagated from UniProtKB/Swiss-Prot (P04350.2)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:16371510; propagated from
                     UniProtKB/Swiss-Prot (P04350.2)"
     CDS             1..444
                     /gene="TUBB4A"
                     /gene_synonym="beta-5; DYT4; TUBB4"
                     /coded_by="NM_001289129.2:221..1555"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS12168.1"
                     /db_xref="GeneID:10382"
                     /db_xref="HGNC:HGNC:20774"
                     /db_xref="MIM:602662"
ORIGIN      
        1 mreivhlqag qcgnqigakf wevisdehgi dptgtyhgds dlqlerinvy yneatggnyv
       61 pravlvdlep gtmdsvrsgp fgqifrpdnf vfgqsgagnn wakghytega elvdavldvv
      121 rkeaescdcl qgfqlthslg ggtgsgmgtl liskireefp drimntfsvv pspkvsdtvv
      181 epynatlsvh qlventdety cidnealydi cfrtlklttp tygdlnhlvs atmsgvttcl
      241 rfpgqlnadl rklavnmvpf prlhffmpgf apltsrgsqq yraltvpelt qqmfdaknmm
      301 aacdprhgry ltvaavfrgr msmkevdeqm lsvqsknssy fvewipnnvk tavcdipprg
      361 lkmaatfign staiqelfkr iseqftamfr rkaflhwytg egmdemefte aesnmndlvs
      421 eyqqyqdata eegefeeeae eeva
//
LOCUS       NP_001180258             819 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 1 [Homo sapiens].
ACCESSION   NP_001180258 XP_006717369
VERSION     NP_001180258.1
DBSOURCE    REFSEQ: accession NM_001193329.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 819)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 819)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 819)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 819)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 819)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 819)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 819)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157936.12, AL353768.28 and
            AL354893.14.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 5, 2020 this sequence version replaced XP_006717369.1.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1455886.1,
                                           SRR18074969.245806.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375315.8/ ENSP00000364464.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..819
                     /product="aminopeptidase O isoform 1"
                     /calculated_mol_wt=93442
     Region          <244..652
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     Site            586
                     /site_type="other"
                     /note="Transition state stabilizer.
                     /evidence=ECO:0000250|UniProtKB:P15144; propagated from
                     UniProtKB/Swiss-Prot (Q8N6M6.2)"
     Region          689..699
                     /region_name="Nucleolar localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q8BXQ6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6M6.2)"
     Region          721..818
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
     CDS             1..819
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_001193329.3:189..2648"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS55328.1"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mdiqldpard dlplmantsh ilvkhyvldl dvdfesqvie gtivlfledg nrfkkqnssi
       61 eeacqsesnk ackfgmpepc hipvtnartf ssemeyndfa icskgekdts dkdgnhdnqe
      121 hasgisssky ccdtgnhgse dfllvldccd lsvlkveevd vaavpglekf trspeltvvs
      181 eefrnqivre lvtlpanrwr eqldyyarcs qapgcgellf dtdtwslqir ktgaqtatdf
      241 phairiwykt kpegrsvtwt sdqsgrpcvy tvgspinnra lfpcqeppva mstwqatvra
      301 aasfvvlmsg ensakptqlw eecsswyyyv tmpmpastft iavgcwtemk metwssndla
      361 terpfspsea nfrhvgvcsh meypcrfqna sattqeiiph rvfapvcltg acqetllrli
      421 ppclsaahsv lgahpfsrld vlivpanfps lgmasphimf lsqsiltggn hlcgtrlche
      481 iahawfglai gardwteewl segfathled vfwataqqla pyeareqqel raclrwrrlq
      541 demqcspeem qvlrpskdkt ghtsdsgasv ikhglnpeki fmqvhylkgy fllrflakrl
      601 gdetyfsflr kfvhtfhgql ilsqdflqml lenipeekrl elsveniyqd wlessgipkp
      661 lqrerragae cglarqvrae vtkwigvnrr prkrkrreke evfekllpdq lvlllehlle
      721 qktlsprtlq slqrtyhlqd qdaevrhrwc elivkhkftk ayksverflq edqamgvyly
      781 gelmvsedar qqqlarrcfe rtkeqmdrss aqvvaemlf
//
LOCUS       NP_001300655            1042 aa            linear   PRI 15-DEC-2025
DEFINITION  anoctamin-3 isoform 1 [Homo sapiens].
ACCESSION   NP_001300655 XP_011518585
VERSION     NP_001300655.1
DBSOURCE    REFSEQ: accession NM_001313726.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Ousingsawat,J., Talbi,K., Gomez-Martin,H., Koy,A.,
            Fernandez-Jaen,A., Tekgul,H., Serdaroglu,E., Schreiber,R.,
            Ortigoza-Escobar,J.D. and Kunzelmann,K.
  TITLE     Broadening the clinical spectrum: molecular mechanisms and new
            phenotypes of ANO3-dystonia
  JOURNAL   Brain 147 (6), 1982-1995 (2024)
   PUBMED   38079528
  REMARK    GeneRIF: Broadening the clinical spectrum: molecular mechanisms and
            new phenotypes of ANO3-dystonia.
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Percetti,M., Zini,M., Soliveri,P., Cogiamanian,F., Ferrara,M.,
            Orunesu,E., Ranghetti,A., Ferrarese,C., Pezzoli,G., Garavaglia,B.,
            Isaias,I.U. and Sacilotto,G.
  TITLE     The Clinical Spectrum of ANO3-Report of a New Family and Literature
            Review
  JOURNAL   Mov Disord Clin Pract 11 (3), 289-297 (2024)
   PUBMED   38284143
  REMARK    GeneRIF: The Clinical Spectrum of ANO3-Report of a New Family and
            Literature Review.
            Review article
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Esposito,M., Trinchillo,A., Piceci-Sparascio,F., D'Asdia,M.C.,
            Consoli,F. and De Luca,A.
  TITLE     A novel ANO3 variant in two siblings with different phenotypes
  JOURNAL   Parkinsonism Relat Disord 111, 105413 (2023)
   PUBMED   37116293
  REMARK    GeneRIF: A novel ANO3 variant in two siblings with different
            phenotypes.
REFERENCE   4  (residues 1 to 1042)
  AUTHORS   Ma,L.Y., Wang,L., Yang,Y.M., Feng,T. and Wan,X.H.
  TITLE     Mutations in ANO3 and GNAL gene in thirty-three isolated dystonia
            families
  JOURNAL   Mov Disord 30 (5), 743-744 (2015)
   PUBMED   25847575
  REMARK    GeneRIF: This study demonstrated that Mutations in ANO3 may cause
            Dystonia.
REFERENCE   5  (residues 1 to 1042)
  AUTHORS   Huang,F., Wang,X., Ostertag,E.M., Nuwal,T., Huang,B., Jan,Y.N.,
            Basbaum,A.I. and Jan,L.Y.
  TITLE     TMEM16C facilitates Na(+)-activated K+ currents in rat sensory
            neurons and regulates pain processing
  JOURNAL   Nat Neurosci 16 (9), 1284-1290 (2013)
   PUBMED   23872594
  REMARK    GeneRIF: rat Ano3 (also known as Tmem16c) interacts with, and
            alters the activity of the sodium-activated potassium channel
            Slack. Reduced expression of Ano3 in rat models results in
            increased pain sensitivity.
REFERENCE   6  (residues 1 to 1042)
  AUTHORS   Charlesworth,G., Plagnol,V., Holmstrom,K.M., Bras,J., Sheerin,U.M.,
            Preza,E., Rubio-Agusti,I., Ryten,M., Schneider,S.A., Stamelou,M.,
            Trabzuni,D., Abramov,A.Y., Bhatia,K.P. and Wood,N.W.
  TITLE     Mutations in ANO3 cause dominant craniocervical dystonia: ion
            channel implicated in pathogenesis
  JOURNAL   Am J Hum Genet 91 (6), 1041-1050 (2012)
   PUBMED   23200863
  REMARK    GeneRIF: Mutations in ANO3 are a cause of autosomal-dominant
            craniocervical dystonia.
REFERENCE   7  (residues 1 to 1042)
  AUTHORS   Hartzell,H.C., Yu,K., Xiao,Q., Chien,L.T. and Qu,Z.
  TITLE     Anoctamin/TMEM16 family members are Ca2+-activated Cl- channels
  JOURNAL   J Physiol 587 (Pt 10), 2127-2139 (2009)
   PUBMED   19015192
  REMARK    Review article
REFERENCE   8  (residues 1 to 1042)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of TMEM16E and TMEM16F genes in
            silico
  JOURNAL   Int J Oncol 24 (5), 1345-1349 (2004)
   PUBMED   15067359
REFERENCE   9  (residues 1 to 1042)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     FLJ10261 gene, located within the CCND1-EMS1 locus on human
            chromosome 11q13, encodes the eight-transmembrane protein
            homologous to C12orf3, C11orf25 and FLJ34272 gene products
  JOURNAL   Int J Oncol 22 (6), 1375-1381 (2003)
   PUBMED   12739008
  REMARK    GeneRIF: C11orf25, FLJ10261 (ORAOV2), C12orf3 and FLJ34272
            constitute a family of eight-transmembrane proteins with N- and
            C-terminal tails facing the cytoplasm.
REFERENCE   10 (residues 1 to 1042)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099687.5, BF591994.1,
            AK304781.1, AJ300461.1, DA247850.1, AC079064.6, BQ430769.1,
            AC083755.10 and X81896.1.
            
            On Sep 1, 2015 this sequence version replaced XP_011518585.1.
            
            Summary: The protein encoded by this gene belongs to the TMEM16
            family of predicted membrane proteins, that are also known as
            anoctamins. While little is known about the function of this gene,
            mutations in this gene have been associated with some cases of
            autosomal dominant craniocervical dystonia. Cells from individuals
            with a mutation in this gene exhibited abnormalities in endoplasmic
            reticulum-dependent calcium signaling. Studies in rat show that the
            rat ortholog of this protein interacts with, and modulates the
            activity of a sodium-activated potassium channel. Deletion of this
            gene caused increased pain sensitivity in the rat model system.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Aug 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1304754.1, AK304781.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154125 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p14.3-p14.2"
     Protein         1..1042
                     /product="anoctamin-3 isoform 1"
                     /note="transmembrane protein 16C (eight membrane-spanning
                     domains); dystonia 23"
                     /calculated_mol_wt=121300
     Region          218..442
                     /region_name="Anoct_dimer"
                     /note="dimerization domain of Ca+-activated
                     chloride-channel, anoctamin; pfam16178"
                     /db_xref="CDD:465044"
     Region          445..1010
                     /region_name="Anoctamin"
                     /note="Calcium-activated chloride channel; pfam04547"
                     /db_xref="CDD:461349"
     CDS             1..1042
                     /gene="ANO3"
                     /gene_synonym="C11orf25; DYT23; DYT24; GENX-3947; TMEM16C"
                     /coded_by="NM_001313726.2:370..3498"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS91452.1"
                     /db_xref="GeneID:63982"
                     /db_xref="HGNC:HGNC:14004"
                     /db_xref="MIM:610110"
ORIGIN      
        1 msvlkfeldn fspegfrheh asnscfalpc ltelsgdssq lelqhsssvp tglqklcfsh
       61 releksvwaa kgkynegmni skseitkets lkpsrrslpc laqsyaysks lsqstslfqs
      121 tesesqapts itlistdkae qvnteenknd svlrcsfadl sdfclalgkd kdytdeseha
      181 tydrsrlind fvikdksefk tklskndmny iassgplfkd gkkridyilv yrktniqydk
      241 rntfeknlra eglmlekepa iaspdimfik ihipwdtlck yaerlnirmp frkkcyytdg
      301 rsksmgrmqt yfrriknwma qnpmvldksa fpdleesdcy tgpfsrarih hfiinnkdtf
      361 fsnatrsriv yhmlertkye ngiskvgirk linngsyiaa fpphegayks sqpikthgpq
      421 nnrhllyerw arwgmwykhq pldlirlyfg ekiglyfawl gwytgmlipa aivglcvffy
      481 glftmnnsqv sqeickatev fmcplcdknc slqrlndsci yakvtylfdn ggtvffaifm
      541 aiwatvflef wkrrrsilty twdlieweee eetlrpqfea kyykmeivnp itgkpephqp
      601 ssdkvtrllv svsgiffmis lvitavfgvv vyrlvvmeqf asfkwnfikq ywqfatsaaa
      661 vcinfiiiml lnlayekiay lltnleyprt esewensfal kmflfqfvnl nssifyiaff
      721 lgrfvghpgk ynklfdrwrl eechpsgcli dlclqmgvim flkqiwnnfm elgypliqnw
      781 wsrhkikrgi hdasipqwen dwnlqpmnlh glmdeylemv lqfgfttifv aafplaplla
      841 llnniieirl daykfvtqwr rplparatdi giwlgilegi gilavitnaf viaitsdyip
      901 rfvyeykygp canhvepsen clkgyvnnsl sffdlselgm gksgycryrd yrgppwsskp
      961 yeftlqywhi laarlafiiv fehlvfgiks fiaylipdvp kglhdrirre kylvqemmye
     1021 aelehlqqqr rksgqpvhhe wp
//
LOCUS       NP_001276052             495 aa            linear   PRI 15-DEC-2025
DEFINITION  tubulin beta-4A chain isoform 1 [Homo sapiens].
ACCESSION   NP_001276052
VERSION     NP_001276052.1
DBSOURCE    REFSEQ: accession NM_001289123.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Garg,D., Holla,V.V., Ganguly,J., Rajan,R., Saini,A., Agarwal,A.,
            Radhakrishnan,D.M., Basu,P., Mondal,B., Dhar,D., Kamble,N.,
            Yadav,R., Muthusamy,B., Kumar,H., Srivastava,A.K. and Pal,P.K.
  TITLE     Expanding the phenotypic and genotypic spectrum of DYT-TUBB4A with
            seven patients from India
  JOURNAL   Parkinsonism Relat Disord 124, 107012 (2024)
   PUBMED   38762926
  REMARK    GeneRIF: Expanding the phenotypic and genotypic spectrum of
            DYT-TUBB4A with seven patients from India.
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Ben Jdila,M., Kammoun,F., Abdelmaksoud-Dammak,R., Triki,C. and
            Fakhfakh,F.
  TITLE     Mutation in the beta-tubulin gene TUBB4A results in epileptic
            encephalopathy associated with hypomyelinated leucodystrophy:
            Unexpected findings reveal genetic mosaicism
  JOURNAL   Int J Dev Neurosci 83 (6), 532-545 (2023)
   PUBMED   37529938
  REMARK    GeneRIF: Mutation in the beta-tubulin gene TUBB4A results in
            epileptic encephalopathy associated with hypomyelinated
            leucodystrophy: Unexpected findings reveal genetic mosaicism.
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Simons,C., Wolf,N.I., McNeil,N., Caldovic,L., Devaney,J.M.,
            Takanohashi,A., Crawford,J., Ru,K., Grimmond,S.M., Miller,D.,
            Tonduti,D., Schmidt,J.L., Chudnow,R.S., van Coster,R., Lagae,L.,
            Kisler,J., Sperner,J., van der Knaap,M.S., Schiffmann,R., Taft,R.J.
            and Vanderver,A.
  TITLE     A de novo mutation in the beta-tubulin gene TUBB4A results in the
            leukoencephalopathy hypomyelination with atrophy of the basal
            ganglia and cerebellum
  JOURNAL   Am J Hum Genet 92 (5), 767-773 (2013)
   PUBMED   23582646
  REMARK    GeneRIF: A de novo mutation in the beta-tubulin gene TUBB4A results
            in the leukoencephalopathy hypomyelination with atrophy of the
            basal ganglia and cerebellum.
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Hersheson,J., Mencacci,N.E., Davis,M., MacDonald,N., Trabzuni,D.,
            Ryten,M., Pittman,A., Paudel,R., Kara,E., Fawcett,K., Plagnol,V.,
            Bhatia,K.P., Medlar,A.J., Stanescu,H.C., Hardy,J., Kleta,R.,
            Wood,N.W. and Houlden,H.
  TITLE     Mutations in the autoregulatory domain of beta-tubulin 4a cause
            hereditary dystonia
  JOURNAL   Ann Neurol 73 (4), 546-553 (2013)
   PUBMED   23424103
  REMARK    GeneRIF: This study demonistrated that TUBB4A mutation in the
            autoregulatory domain cause hereditary dystonia.
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Nahhas,N., Conant,A., Hamilton,E., Curiel,J., Simons,C., van der
            Knaap,M. and Vanderver,A.
  TITLE     TUBB4A-Related Leukodystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27809427
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Wang,D., Villasante,A., Lewis,S.A. and Cowan,N.J.
  TITLE     The mammalian beta-tubulin repertoire: hematopoietic expression of
            a novel, heterologous beta-tubulin isotype
  JOURNAL   J Cell Biol 103 (5), 1903-1910 (1986)
   PUBMED   3782288
REFERENCE   10 (residues 1 to 495)
  AUTHORS   Lee,M.G., Loomis,C. and Cowan,N.J.
  TITLE     Sequence of an expressed human beta-tubulin gene containing ten Alu
            family members
  JOURNAL   Nucleic Acids Res 12 (14), 5823-5836 (1984)
   PUBMED   6462917
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010503.8, DC303150.1 and
            BC013683.1.
            
            Summary: This gene encodes a member of the beta tubulin family.
            Beta tubulins are one of two core protein families (alpha and beta
            tubulins) that heterodimerize and assemble to form microtubules.
            Mutations in this gene cause hypomyelinating leukodystrophy-6 and
            autosomal dominant torsion dystonia-4. Alternate splicing results
            in multiple transcript variants encoding different isoforms. A
            pseudogene of this gene is found on chromosome X. [provided by
            RefSeq, Jan 2014].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.2585631.1, DC303150.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN03267753
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..495
                     /product="tubulin beta-4A chain isoform 1"
                     /note="tubulin, beta, 5; dystonia 4, torsion (autosomal
                     dominant); tubulin beta-4 chain; tubulin, beta 4"
                     /calculated_mol_wt=54336
     Region          52..478
                     /region_name="PLN00220"
                     /note="tubulin beta chain; Provisional"
                     /db_xref="CDD:215107"
     CDS             1..495
                     /gene="TUBB4A"
                     /gene_synonym="beta-5; DYT4; TUBB4"
                     /coded_by="NM_001289123.2:138..1625"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:10382"
                     /db_xref="HGNC:HGNC:20774"
                     /db_xref="MIM:602662"
ORIGIN      
        1 mrrgaadret erlpgaqgpc savsaasstl aaaaaprara taaastlsat amreivhlqa
       61 gqcgnqigak fwevisdehg idptgtyhgd sdlqlerinv yyneatggny vpravlvdle
      121 pgtmdsvrsg pfgqifrpdn fvfgqsgagn nwakghyteg aelvdavldv vrkeaescdc
      181 lqgfqlthsl gggtgsgmgt lliskireef pdrimntfsv vpspkvsdtv vepynatlsv
      241 hqlventdet ycidnealyd icfrtlkltt ptygdlnhlv satmsgvttc lrfpgqlnad
      301 lrklavnmvp fprlhffmpg fapltsrgsq qyraltvpel tqqmfdaknm maacdprhgr
      361 yltvaavfrg rmsmkevdeq mlsvqsknss yfvewipnnv ktavcdippr glkmaatfig
      421 nstaiqelfk riseqftamf rrkaflhwyt gegmdemeft eaesnmndlv seyqqyqdat
      481 aeegefeeea eeeva
//
LOCUS       NP_001372998             760 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 9 [Homo sapiens].
ACCESSION   NP_001372998 XP_005252341
VERSION     NP_001372998.1
DBSOURCE    REFSEQ: accession NM_001386069.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 760)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 760)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 760)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 760)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 760)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 760)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 760)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 760)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 760)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 760)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157936.12, AL353768.28 and
            AL354893.14.
            
            On Aug 6, 2020 this sequence version replaced XP_005252341.1.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.166724.1,
                                           SRR14038196.1994712.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..760
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..760
                     /product="aminopeptidase O isoform 9"
                     /calculated_mol_wt=86250
     Region          <244..553
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     Region          622..>672
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
     CDS             1..760
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_001386069.1:189..2471"
                     /note="isoform 9 is encoded by transcript variant 11"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mdiqldpard dlplmantsh ilvkhyvldl dvdfesqvie gtivlfledg nrfkkqnssi
       61 eeacqsesnk ackfgmpepc hipvtnartf ssemeyndfa icskgekdts dkdgnhdnqe
      121 hasgisssky ccdtgnhgse dfllvldccd lsvlkveevd vaavpglekf trspeltvvs
      181 eefrnqivre lvtlpanrwr eqldyyarcs qapgcgellf dtdtwslqir ktgaqtatdf
      241 phairiwykt kpegrsvtwt sdqsgrpcvy tvgspinnra lfpcqeppva mstwqatvra
      301 aasfvvlmsg ensakptqlw eecsswyyyv tmpmpastft iavgcwtemk metwssndla
      361 terpfspsea nfrhvgvcsh meypcrfqna sattqeiiph rvfapvcltg acqetllrli
      421 ppclsaahsv lgahpfsrld vlivpanfps lgmarpskdk tghtsdsgas vikhglnpek
      481 ifmqvhylkg yfllrflakr lgdetyfsfl rkfvhtfhgq lilsqdflqm llenipeekr
      541 lelsveniyq dwlessgipk plqrerraga ecglarqvra evtkwigvnr rprkrkrrek
      601 eevfekllpd qlvlllehll eqktlsprtl qslqrtyhlq dqdaevrhrw celivkhkft
      661 kayksverfl qedqerpqqd sfirlllawg trleltldik ggimwllkps ahspvhilvl
      721 lfprgwsqpg thkrqilvna aslpggcllp wiwsgaalrf
//
LOCUS       NP_113606                981 aa            linear   PRI 15-DEC-2025
DEFINITION  anoctamin-3 isoform 2 [Homo sapiens].
ACCESSION   NP_113606
VERSION     NP_113606.2
DBSOURCE    REFSEQ: accession NM_031418.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 981)
  AUTHORS   Ousingsawat,J., Talbi,K., Gomez-Martin,H., Koy,A.,
            Fernandez-Jaen,A., Tekgul,H., Serdaroglu,E., Schreiber,R.,
            Ortigoza-Escobar,J.D. and Kunzelmann,K.
  TITLE     Broadening the clinical spectrum: molecular mechanisms and new
            phenotypes of ANO3-dystonia
  JOURNAL   Brain 147 (6), 1982-1995 (2024)
   PUBMED   38079528
  REMARK    GeneRIF: Broadening the clinical spectrum: molecular mechanisms and
            new phenotypes of ANO3-dystonia.
REFERENCE   2  (residues 1 to 981)
  AUTHORS   Percetti,M., Zini,M., Soliveri,P., Cogiamanian,F., Ferrara,M.,
            Orunesu,E., Ranghetti,A., Ferrarese,C., Pezzoli,G., Garavaglia,B.,
            Isaias,I.U. and Sacilotto,G.
  TITLE     The Clinical Spectrum of ANO3-Report of a New Family and Literature
            Review
  JOURNAL   Mov Disord Clin Pract 11 (3), 289-297 (2024)
   PUBMED   38284143
  REMARK    GeneRIF: The Clinical Spectrum of ANO3-Report of a New Family and
            Literature Review.
            Review article
REFERENCE   3  (residues 1 to 981)
  AUTHORS   Esposito,M., Trinchillo,A., Piceci-Sparascio,F., D'Asdia,M.C.,
            Consoli,F. and De Luca,A.
  TITLE     A novel ANO3 variant in two siblings with different phenotypes
  JOURNAL   Parkinsonism Relat Disord 111, 105413 (2023)
   PUBMED   37116293
  REMARK    GeneRIF: A novel ANO3 variant in two siblings with different
            phenotypes.
REFERENCE   4  (residues 1 to 981)
  AUTHORS   Ma,L.Y., Wang,L., Yang,Y.M., Feng,T. and Wan,X.H.
  TITLE     Mutations in ANO3 and GNAL gene in thirty-three isolated dystonia
            families
  JOURNAL   Mov Disord 30 (5), 743-744 (2015)
   PUBMED   25847575
  REMARK    GeneRIF: This study demonstrated that Mutations in ANO3 may cause
            Dystonia.
REFERENCE   5  (residues 1 to 981)
  AUTHORS   Huang,F., Wang,X., Ostertag,E.M., Nuwal,T., Huang,B., Jan,Y.N.,
            Basbaum,A.I. and Jan,L.Y.
  TITLE     TMEM16C facilitates Na(+)-activated K+ currents in rat sensory
            neurons and regulates pain processing
  JOURNAL   Nat Neurosci 16 (9), 1284-1290 (2013)
   PUBMED   23872594
  REMARK    GeneRIF: rat Ano3 (also known as Tmem16c) interacts with, and
            alters the activity of the sodium-activated potassium channel
            Slack. Reduced expression of Ano3 in rat models results in
            increased pain sensitivity.
REFERENCE   6  (residues 1 to 981)
  AUTHORS   Charlesworth,G., Plagnol,V., Holmstrom,K.M., Bras,J., Sheerin,U.M.,
            Preza,E., Rubio-Agusti,I., Ryten,M., Schneider,S.A., Stamelou,M.,
            Trabzuni,D., Abramov,A.Y., Bhatia,K.P. and Wood,N.W.
  TITLE     Mutations in ANO3 cause dominant craniocervical dystonia: ion
            channel implicated in pathogenesis
  JOURNAL   Am J Hum Genet 91 (6), 1041-1050 (2012)
   PUBMED   23200863
  REMARK    GeneRIF: Mutations in ANO3 are a cause of autosomal-dominant
            craniocervical dystonia.
REFERENCE   7  (residues 1 to 981)
  AUTHORS   Hartzell,H.C., Yu,K., Xiao,Q., Chien,L.T. and Qu,Z.
  TITLE     Anoctamin/TMEM16 family members are Ca2+-activated Cl- channels
  JOURNAL   J Physiol 587 (Pt 10), 2127-2139 (2009)
   PUBMED   19015192
  REMARK    Review article
REFERENCE   8  (residues 1 to 981)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of TMEM16E and TMEM16F genes in
            silico
  JOURNAL   Int J Oncol 24 (5), 1345-1349 (2004)
   PUBMED   15067359
REFERENCE   9  (residues 1 to 981)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     FLJ10261 gene, located within the CCND1-EMS1 locus on human
            chromosome 11q13, encodes the eight-transmembrane protein
            homologous to C12orf3, C11orf25 and FLJ34272 gene products
  JOURNAL   Int J Oncol 22 (6), 1375-1381 (2003)
   PUBMED   12739008
  REMARK    GeneRIF: C11orf25, FLJ10261 (ORAOV2), C12orf3 and FLJ34272
            constitute a family of eight-transmembrane proteins with N- and
            C-terminal tails facing the cytoplasm.
REFERENCE   10 (residues 1 to 981)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021698.12, AJ300461.1,
            DA247850.1, AC079064.6, BQ430769.1, AC083755.10 and X81896.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 5, 2007 this sequence version replaced NP_113606.1.
            
            Summary: The protein encoded by this gene belongs to the TMEM16
            family of predicted membrane proteins, that are also known as
            anoctamins. While little is known about the function of this gene,
            mutations in this gene have been associated with some cases of
            autosomal dominant craniocervical dystonia. Cells from individuals
            with a mutation in this gene exhibited abnormalities in endoplasmic
            reticulum-dependent calcium signaling. Studies in rat show that the
            rat ortholog of this protein interacts with, and modulates the
            activity of a sodium-activated potassium channel. Deletion of this
            gene caused increased pain sensitivity in the rat model system.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Aug 2015].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, contains an alternate 5' terminal
            exon, and initiates translation at an alternate start codon,
            compared to variant 1. The encoded isoform (2) has a distinct
            N-terminus and is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.53332.1,
                                           SRR1803611.60310.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256737.8/ ENSP00000256737.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..981
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p14.3-p14.2"
     Protein         1..981
                     /product="anoctamin-3 isoform 2"
                     /note="transmembrane protein 16C (eight membrane-spanning
                     domains); dystonia 23"
                     /calculated_mol_wt=114526
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYT9.2)"
     Region          157..381
                     /region_name="Anoct_dimer"
                     /note="dimerization domain of Ca+-activated
                     chloride-channel, anoctamin; pfam16178"
                     /db_xref="CDD:465044"
     Region          384..949
                     /region_name="Anoctamin"
                     /note="Calcium-activated chloride channel; pfam04547"
                     /db_xref="CDD:461349"
     Site            404..424
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYT9.2)"
     Site            425
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BYT9.2)"
     Site            448
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BYT9.2)"
     Site            455
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BYT9.2)"
     Site            470..490
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYT9.2)"
     Site            551..571
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYT9.2)"
     Site            593..613
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYT9.2)"
     Site            641..661
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYT9.2)"
     Site            762..782
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYT9.2)"
     Site            811..831
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYT9.2)"
     Site            866
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BYT9.2)"
     Site            915..935
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYT9.2)"
     CDS             1..981
                     /gene="ANO3"
                     /gene_synonym="C11orf25; DYT23; DYT24; GENX-3947; TMEM16C"
                     /coded_by="NM_031418.4:147..3092"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS31447.1"
                     /db_xref="GeneID:63982"
                     /db_xref="HGNC:HGNC:14004"
                     /db_xref="MIM:610110"
ORIGIN      
        1 mvhhsgsiqs fkqqkgmnis kseitketsl kpsrrslpcl aqsyaysksl sqstslfqst
       61 esesqaptsi tlistdkaeq vnteenknds vlrcsfadls dfclalgkdk dytdesehat
      121 ydrsrlindf vikdksefkt klskndmnyi assgplfkdg kkridyilvy rktniqydkr
      181 ntfeknlrae glmlekepai aspdimfiki hipwdtlcky aerlnirmpf rkkcyytdgr
      241 sksmgrmqty frriknwmaq npmvldksaf pdleesdcyt gpfsrarihh fiinnkdtff
      301 snatrsrivy hmlertkyen giskvgirkl inngsyiaaf pphegaykss qpikthgpqn
      361 nrhllyerwa rwgmwykhqp ldlirlyfge kiglyfawlg wytgmlipaa ivglcvffyg
      421 lftmnnsqvs qeickatevf mcplcdkncs lqrlndsciy akvtylfdng gtvffaifma
      481 iwatvflefw krrrsiltyt wdlieweeee etlrpqfeak yykmeivnpi tgkpephqps
      541 sdkvtrllvs vsgiffmisl vitavfgvvv yrlvvmeqfa sfkwnfikqy wqfatsaaav
      601 cinfiiimll nlayekiayl ltnleyprte sewensfalk mflfqfvnln ssifyiaffl
      661 grfvghpgky nklfdrwrle echpsgclid lclqmgvimf lkqiwnnfme lgypliqnww
      721 srhkikrgih dasipqwend wnlqpmnlhg lmdeylemvl qfgfttifva afplapllal
      781 lnniieirld aykfvtqwrr plparatdig iwlgilegig ilavitnafv iaitsdyipr
      841 fvyeykygpc anhvepsenc lkgyvnnsls ffdlselgmg ksgycryrdy rgppwsskpy
      901 eftlqywhil aarlafiivf ehlvfgiksf iaylipdvpk glhdrirrek ylvqemmyea
      961 elehlqqqrr ksgqpvhhew p
//
LOCUS       NP_001372996             685 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 8 [Homo sapiens].
ACCESSION   NP_001372996
VERSION     NP_001372996.1
DBSOURCE    REFSEQ: accession NM_001386067.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 685)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 685)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 685)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 685)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 685)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 685)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 685)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 685)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 685)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 685)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157936.12, AL353768.28 and
            AL354893.14.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.251383.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968968,
                                           SAMEA2142680 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..685
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..685
                     /product="aminopeptidase O isoform 8"
                     /calculated_mol_wt=77365
     Region          <244..>453
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     Region          547..>597
                     /region_name="Leuk-A4-hydro_C"
                     /note="Leukotriene A4 hydrolase, C-terminal; pfam09127"
                     /db_xref="CDD:462686"
     CDS             1..685
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_001386067.1:189..2246"
                     /note="isoform 8 is encoded by transcript variant 9"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mdiqldpard dlplmantsh ilvkhyvldl dvdfesqvie gtivlfledg nrfkkqnssi
       61 eeacqsesnk ackfgmpepc hipvtnartf ssemeyndfa icskgekdts dkdgnhdnqe
      121 hasgisssky ccdtgnhgse dfllvldccd lsvlkveevd vaavpglekf trspeltvvs
      181 eefrnqivre lvtlpanrwr eqldyyarcs qapgcgellf dtdtwslqir ktgaqtatdf
      241 phairiwykt kpegrsvtwt sdqsgrpcvy tvgspinnra lfpcqeppva mstwqatvra
      301 aasfvvlmsg ensakptqlw eecsswyyyv tmpmpastft iavgcwtemk metwssndla
      361 terpfspsea nfrhvgvcsh meypcrfqna sattqeiiph rvfapvcltg acqetllrli
      421 ppclsaahsv lgahpfsrld vlivpanfps lgmarlelsv eniyqdwles sgipkirplt
      481 tvgaqplqre rragaecgla rqvraevtkw igvnrrprkr krrekeevfe kllpdqlvll
      541 lehlleqktl sprtlqslqr tyhlqdqdae vrhrwceliv khkftkayks verflqedqe
      601 rpqqdsfirl llawgtrlel tldikggimw llkpsahspv hilvllfprg wsqpgthkrq
      661 ilvnaaslpg gcllpwiwsg aalrf
//
LOCUS       NP_001276060             372 aa            linear   PRI 15-DEC-2025
DEFINITION  tubulin beta-4A chain isoform 4 [Homo sapiens].
ACCESSION   NP_001276060
VERSION     NP_001276060.1
DBSOURCE    REFSEQ: accession NM_001289131.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Garg,D., Holla,V.V., Ganguly,J., Rajan,R., Saini,A., Agarwal,A.,
            Radhakrishnan,D.M., Basu,P., Mondal,B., Dhar,D., Kamble,N.,
            Yadav,R., Muthusamy,B., Kumar,H., Srivastava,A.K. and Pal,P.K.
  TITLE     Expanding the phenotypic and genotypic spectrum of DYT-TUBB4A with
            seven patients from India
  JOURNAL   Parkinsonism Relat Disord 124, 107012 (2024)
   PUBMED   38762926
  REMARK    GeneRIF: Expanding the phenotypic and genotypic spectrum of
            DYT-TUBB4A with seven patients from India.
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Ben Jdila,M., Kammoun,F., Abdelmaksoud-Dammak,R., Triki,C. and
            Fakhfakh,F.
  TITLE     Mutation in the beta-tubulin gene TUBB4A results in epileptic
            encephalopathy associated with hypomyelinated leucodystrophy:
            Unexpected findings reveal genetic mosaicism
  JOURNAL   Int J Dev Neurosci 83 (6), 532-545 (2023)
   PUBMED   37529938
  REMARK    GeneRIF: Mutation in the beta-tubulin gene TUBB4A results in
            epileptic encephalopathy associated with hypomyelinated
            leucodystrophy: Unexpected findings reveal genetic mosaicism.
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Simons,C., Wolf,N.I., McNeil,N., Caldovic,L., Devaney,J.M.,
            Takanohashi,A., Crawford,J., Ru,K., Grimmond,S.M., Miller,D.,
            Tonduti,D., Schmidt,J.L., Chudnow,R.S., van Coster,R., Lagae,L.,
            Kisler,J., Sperner,J., van der Knaap,M.S., Schiffmann,R., Taft,R.J.
            and Vanderver,A.
  TITLE     A de novo mutation in the beta-tubulin gene TUBB4A results in the
            leukoencephalopathy hypomyelination with atrophy of the basal
            ganglia and cerebellum
  JOURNAL   Am J Hum Genet 92 (5), 767-773 (2013)
   PUBMED   23582646
  REMARK    GeneRIF: A de novo mutation in the beta-tubulin gene TUBB4A results
            in the leukoencephalopathy hypomyelination with atrophy of the
            basal ganglia and cerebellum.
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Hersheson,J., Mencacci,N.E., Davis,M., MacDonald,N., Trabzuni,D.,
            Ryten,M., Pittman,A., Paudel,R., Kara,E., Fawcett,K., Plagnol,V.,
            Bhatia,K.P., Medlar,A.J., Stanescu,H.C., Hardy,J., Kleta,R.,
            Wood,N.W. and Houlden,H.
  TITLE     Mutations in the autoregulatory domain of beta-tubulin 4a cause
            hereditary dystonia
  JOURNAL   Ann Neurol 73 (4), 546-553 (2013)
   PUBMED   23424103
  REMARK    GeneRIF: This study demonistrated that TUBB4A mutation in the
            autoregulatory domain cause hereditary dystonia.
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Nahhas,N., Conant,A., Hamilton,E., Curiel,J., Simons,C., van der
            Knaap,M. and Vanderver,A.
  TITLE     TUBB4A-Related Leukodystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27809427
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Wang,D., Villasante,A., Lewis,S.A. and Cowan,N.J.
  TITLE     The mammalian beta-tubulin repertoire: hematopoietic expression of
            a novel, heterologous beta-tubulin isotype
  JOURNAL   J Cell Biol 103 (5), 1903-1910 (1986)
   PUBMED   3782288
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Lee,M.G., Loomis,C. and Cowan,N.J.
  TITLE     Sequence of an expressed human beta-tubulin gene containing ten Alu
            family members
  JOURNAL   Nucleic Acids Res 12 (14), 5823-5836 (1984)
   PUBMED   6462917
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC314277.1, DA302559.1 and
            BC013683.1.
            
            Summary: This gene encodes a member of the beta tubulin family.
            Beta tubulins are one of two core protein families (alpha and beta
            tubulins) that heterodimerize and assemble to form microtubules.
            Mutations in this gene cause hypomyelinating leukodystrophy-6 and
            autosomal dominant torsion dystonia-4. Alternate splicing results
            in multiple transcript variants encoding different isoforms. A
            pseudogene of this gene is found on chromosome X. [provided by
            RefSeq, Jan 2014].
            
            Transcript Variant: This variant (6) has multiple differences,
            compared to variant 1. These differences result in a distinct 5'
            UTR and translation initiation at a downstream start codon,
            compared to variant 1. The resulting isoform (4) has a shorter
            N-terminus, compared to isoform 1. Both variants 5 and 6 encode the
            same isoform 4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA350532.1, DA302559.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1968540 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..372
                     /product="tubulin beta-4A chain isoform 4"
                     /note="tubulin, beta, 5; dystonia 4, torsion (autosomal
                     dominant); tubulin beta-4 chain; tubulin, beta 4"
                     /calculated_mol_wt=41513
     Region          1..355
                     /region_name="PLN00220"
                     /note="tubulin beta chain; Provisional"
                     /db_xref="CDD:215107"
     CDS             1..372
                     /gene="TUBB4A"
                     /gene_synonym="beta-5; DYT4; TUBB4"
                     /coded_by="NM_001289131.2:238..1356"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:10382"
                     /db_xref="HGNC:HGNC:20774"
                     /db_xref="MIM:602662"
ORIGIN      
        1 mdsvrsgpfg qifrpdnfvf gqsgagnnwa kghytegael vdavldvvrk eaescdclqg
       61 fqlthslggg tgsgmgtlli skireefpdr imntfsvvps pkvsdtvvep ynatlsvhql
      121 ventdetyci dnealydicf rtlklttpty gdlnhlvsat msgvttclrf pgqlnadlrk
      181 lavnmvpfpr lhffmpgfap ltsrgsqqyr altvpeltqq mfdaknmmaa cdprhgrylt
      241 vaavfrgrms mkevdeqmls vqsknssyfv ewipnnvkta vcdipprglk maatfignst
      301 aiqelfkris eqftamfrrk aflhwytgeg mdemefteae snmndlvsey qqyqdataee
      361 gefeeeaeee va
//
LOCUS       NP_002134                193 aa            linear   PRI 15-DEC-2025
DEFINITION  neuron-specific calcium-binding protein hippocalcin [Homo sapiens].
ACCESSION   NP_002134
VERSION     NP_002134.2
DBSOURCE    REFSEQ: accession NM_002143.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Kang,M.J., Park,S.Y. and Han,J.S.
  TITLE     MicroRNA-24-3p regulates neuronal differentiation by controlling
            hippocalcin expression
  JOURNAL   Cell Mol Life Sci 76 (22), 4569-4580 (2019)
   PUBMED   31486848
  REMARK    GeneRIF: MiR-24-3p is an important miRNA that regulates neuronal
            differentiation by controlling HPCA expression.
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Atasu,B., Hanagasi,H., Bilgic,B., Pak,M., Erginel-Unaltuna,N.,
            Hauser,A.K., Guven,G., Simon-Sanchez,J., Heutink,P., Gasser,T. and
            Lohmann,E.
  TITLE     HPCA confirmed as a genetic cause of DYT2-like dystonia phenotype
  JOURNAL   Mov Disord 33 (8), 1354-1358 (2018)
   PUBMED   30145809
  REMARK    GeneRIF: HPCA mutations lead to recessively inherited dystonia
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Helassa,N., Antonyuk,S.V., Lian,L.Y., Haynes,L.P. and Burgoyne,R.D.
  TITLE     Biophysical and functional characterization of hippocalcin mutants
            responsible for human dystonia
  JOURNAL   Hum Mol Genet 26 (13), 2426-2435 (2017)
   PUBMED   28398555
  REMARK    GeneRIF: hippocalcin forms oligomers upon calcium binding and
            directly interacts with VGCCs. The dystonia-causing mutations did
            not affect protein stability or folding. In common for both T71N
            and A190T mutants was an impaired calcium-dependent oligomerisation
            and increased intracellular calcium influx after KCl
            depolarisation.
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Takamatsu,K., Kobayashi,M., Saitoh,S., Fujishiro,M. and Noguchi,T.
  TITLE     Molecular cloning of human hippocalcin cDNA and chromosomal mapping
            of its gene
  JOURNAL   Biochem Biophys Res Commun 200 (1), 606-611 (1994)
   PUBMED   8166736
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Kobayashi,M., Takamatsu,K., Saitoh,S., Miura,M. and Noguchi,T.
  TITLE     Molecular cloning of hippocalcin, a novel calcium-binding protein
            of the recoverin family exclusively expressed in hippocampus
  JOURNAL   Biochem Biophys Res Commun 189 (1), 511-517 (1992)
   PUBMED   1280427
  REMARK    Erratum:[Biochem Biophys Res Commun. 1993 Oct 29;196(2):1017. doi:
            10.1006/bbrc.1993.2351. PMID: 8240319]
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Fletcher,N.A.
  TITLE     The genetics of idiopathic torsion dystonia
  JOURNAL   J Med Genet 27 (7), 409-412 (1990)
   PUBMED   2203908
  REMARK    Review article
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Gimenez-Roldan,S., Delgado,G., Marin,M., Villanueva,J.A. and
            Mateo,D.
  TITLE     Hereditary torsion dystonia in gypsies
  JOURNAL   Adv Neurol 50, 73-81 (1988)
   PUBMED   3400517
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC114493.3 and BC001777.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 3, 2002 this sequence version replaced NP_002134.1.
            
            Summary: The protein encoded by this gene is a member of
            neuron-specific calcium-binding proteins family found in the retina
            and brain. This protein is associated with the plasma membrane. It
            has similarities to proteins located in the photoreceptor cells
            that regulate photosignal transduction in a calcium-sensitive
            manner. This protein displays recoverin activity and a
            calcium-dependent inhibition of rhodopsin kinase. It is identical
            to the rat and mouse hippocalcin proteins and thought to play an
            important role in neurons of the central nervous system in a number
            of species. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.170379.1,
                                           SRR3476690.961056.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373467.4/ ENSP00000362566.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..193
                     /product="neuron-specific calcium-binding protein
                     hippocalcin"
                     /note="calcium-binding protein BDR-2; dystonia 2, torsion
                     (autosomal recessive)"
                     /calculated_mol_wt=22296
     Region          41..175
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..193
                     /gene="HPCA"
                     /gene_synonym="BDR2; DYT2"
                     /coded_by="NM_002143.3:47..628"
                     /db_xref="CCDS:CCDS370.1"
                     /db_xref="GeneID:3208"
                     /db_xref="HGNC:HGNC:5144"
                     /db_xref="MIM:142622"
ORIGIN      
        1 mgkqnsklrp emlqdlrent efselelqew ykgflkdcpt gilnvdefkk iyanffpygd
       61 askfaehvfr tfdtnsdgti dfrefiials vtsrgrleqk lmwafsmydl dgngyisree
      121 mleivqaiyk mvssvmkmpe destpekrte kifrqmdtnn dgklsleefi rgaksdpsiv
      181 rllqcdpssa sqf
//
LOCUS       NP_001373002             265 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 12 [Homo sapiens].
ACCESSION   NP_001373002
VERSION     NP_001373002.1
DBSOURCE    REFSEQ: accession NM_001386073.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 265)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 265)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 265)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 265)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 265)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157936.12 and AL353768.28.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..265
                     /product="aminopeptidase O isoform 12"
                     /calculated_mol_wt=29621
     Region          <2..>219
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     CDS             1..265
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_001386073.1:127..924"
                     /note="isoform 12 is encoded by transcript variant 15"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mstwqatvra aasfvvlmsg ensakptqlw eecsswyyyv tmpmpastft iavgcwtemk
       61 metwssndla terpfspsea nfrhvgvcsh meypcrfqna sattqeiiph rvfapvcltg
      121 acqetllrli ppclsaahsv lgahpfsrld vlivpanfps lgmasphimf lsqsiltggn
      181 hlcgtrlche iahawfglai gardwteewl segfathled vfwataqqla pyeareqqel
      241 raclrwrrlq demqcspeem qvlss
//
LOCUS       NP_001300656             835 aa            linear   PRI 15-DEC-2025
DEFINITION  anoctamin-3 isoform 3 [Homo sapiens].
ACCESSION   NP_001300656
VERSION     NP_001300656.1
DBSOURCE    REFSEQ: accession NM_001313727.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Ousingsawat,J., Talbi,K., Gomez-Martin,H., Koy,A.,
            Fernandez-Jaen,A., Tekgul,H., Serdaroglu,E., Schreiber,R.,
            Ortigoza-Escobar,J.D. and Kunzelmann,K.
  TITLE     Broadening the clinical spectrum: molecular mechanisms and new
            phenotypes of ANO3-dystonia
  JOURNAL   Brain 147 (6), 1982-1995 (2024)
   PUBMED   38079528
  REMARK    GeneRIF: Broadening the clinical spectrum: molecular mechanisms and
            new phenotypes of ANO3-dystonia.
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Percetti,M., Zini,M., Soliveri,P., Cogiamanian,F., Ferrara,M.,
            Orunesu,E., Ranghetti,A., Ferrarese,C., Pezzoli,G., Garavaglia,B.,
            Isaias,I.U. and Sacilotto,G.
  TITLE     The Clinical Spectrum of ANO3-Report of a New Family and Literature
            Review
  JOURNAL   Mov Disord Clin Pract 11 (3), 289-297 (2024)
   PUBMED   38284143
  REMARK    GeneRIF: The Clinical Spectrum of ANO3-Report of a New Family and
            Literature Review.
            Review article
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Esposito,M., Trinchillo,A., Piceci-Sparascio,F., D'Asdia,M.C.,
            Consoli,F. and De Luca,A.
  TITLE     A novel ANO3 variant in two siblings with different phenotypes
  JOURNAL   Parkinsonism Relat Disord 111, 105413 (2023)
   PUBMED   37116293
  REMARK    GeneRIF: A novel ANO3 variant in two siblings with different
            phenotypes.
REFERENCE   4  (residues 1 to 835)
  AUTHORS   Ma,L.Y., Wang,L., Yang,Y.M., Feng,T. and Wan,X.H.
  TITLE     Mutations in ANO3 and GNAL gene in thirty-three isolated dystonia
            families
  JOURNAL   Mov Disord 30 (5), 743-744 (2015)
   PUBMED   25847575
  REMARK    GeneRIF: This study demonstrated that Mutations in ANO3 may cause
            Dystonia.
REFERENCE   5  (residues 1 to 835)
  AUTHORS   Huang,F., Wang,X., Ostertag,E.M., Nuwal,T., Huang,B., Jan,Y.N.,
            Basbaum,A.I. and Jan,L.Y.
  TITLE     TMEM16C facilitates Na(+)-activated K+ currents in rat sensory
            neurons and regulates pain processing
  JOURNAL   Nat Neurosci 16 (9), 1284-1290 (2013)
   PUBMED   23872594
  REMARK    GeneRIF: rat Ano3 (also known as Tmem16c) interacts with, and
            alters the activity of the sodium-activated potassium channel
            Slack. Reduced expression of Ano3 in rat models results in
            increased pain sensitivity.
REFERENCE   6  (residues 1 to 835)
  AUTHORS   Charlesworth,G., Plagnol,V., Holmstrom,K.M., Bras,J., Sheerin,U.M.,
            Preza,E., Rubio-Agusti,I., Ryten,M., Schneider,S.A., Stamelou,M.,
            Trabzuni,D., Abramov,A.Y., Bhatia,K.P. and Wood,N.W.
  TITLE     Mutations in ANO3 cause dominant craniocervical dystonia: ion
            channel implicated in pathogenesis
  JOURNAL   Am J Hum Genet 91 (6), 1041-1050 (2012)
   PUBMED   23200863
  REMARK    GeneRIF: Mutations in ANO3 are a cause of autosomal-dominant
            craniocervical dystonia.
REFERENCE   7  (residues 1 to 835)
  AUTHORS   Hartzell,H.C., Yu,K., Xiao,Q., Chien,L.T. and Qu,Z.
  TITLE     Anoctamin/TMEM16 family members are Ca2+-activated Cl- channels
  JOURNAL   J Physiol 587 (Pt 10), 2127-2139 (2009)
   PUBMED   19015192
  REMARK    Review article
REFERENCE   8  (residues 1 to 835)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of TMEM16E and TMEM16F genes in
            silico
  JOURNAL   Int J Oncol 24 (5), 1345-1349 (2004)
   PUBMED   15067359
REFERENCE   9  (residues 1 to 835)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     FLJ10261 gene, located within the CCND1-EMS1 locus on human
            chromosome 11q13, encodes the eight-transmembrane protein
            homologous to C12orf3, C11orf25 and FLJ34272 gene products
  JOURNAL   Int J Oncol 22 (6), 1375-1381 (2003)
   PUBMED   12739008
  REMARK    GeneRIF: C11orf25, FLJ10261 (ORAOV2), C12orf3 and FLJ34272
            constitute a family of eight-transmembrane proteins with N- and
            C-terminal tails facing the cytoplasm.
REFERENCE   10 (residues 1 to 835)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP219022.1, AJ300461.1,
            AC079064.6, BQ430769.1, AC083755.10 and X81896.1.
            
            Summary: The protein encoded by this gene belongs to the TMEM16
            family of predicted membrane proteins, that are also known as
            anoctamins. While little is known about the function of this gene,
            mutations in this gene have been associated with some cases of
            autosomal dominant craniocervical dystonia. Cells from individuals
            with a mutation in this gene exhibited abnormalities in endoplasmic
            reticulum-dependent calcium signaling. Studies in rat show that the
            rat ortholog of this protein interacts with, and modulates the
            activity of a sodium-activated potassium channel. Deletion of this
            gene caused increased pain sensitivity in the rat model system.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Aug 2015].
            
            Transcript Variant: This variant (3) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at a
            downstream start codon, compared to variant 1. The encoded isoform
            (3) has a shorter N-terminus than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295816.1, AK316018.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2163459, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p14.3-p14.2"
     Protein         1..835
                     /product="anoctamin-3 isoform 3"
                     /note="transmembrane protein 16C (eight membrane-spanning
                     domains); dystonia 23"
                     /calculated_mol_wt=98154
     Region          11..235
                     /region_name="Anoct_dimer"
                     /note="dimerization domain of Ca+-activated
                     chloride-channel, anoctamin; pfam16178"
                     /db_xref="CDD:465044"
     Region          238..803
                     /region_name="Anoctamin"
                     /note="Calcium-activated chloride channel; pfam04547"
                     /db_xref="CDD:461349"
     CDS             1..835
                     /gene="ANO3"
                     /gene_synonym="C11orf25; DYT23; DYT24; GENX-3947; TMEM16C"
                     /coded_by="NM_001313727.2:181..2688"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS81557.1"
                     /db_xref="GeneID:63982"
                     /db_xref="HGNC:HGNC:14004"
                     /db_xref="MIM:610110"
ORIGIN      
        1 mnyiassgpl fkdgkkridy ilvyrktniq ydkrntfekn lraeglmlek epaiaspdim
       61 fikihipwdt lckyaerlni rmpfrkkcyy tdgrsksmgr mqtyfrrikn wmaqnpmvld
      121 ksafpdlees dcytgpfsra rihhfiinnk dtffsnatrs rivyhmlert kyengiskvg
      181 irklinngsy iaafpphega ykssqpikth gpqnnrhlly erwarwgmwy khqpldlirl
      241 yfgekiglyf awlgwytgml ipaaivglcv ffyglftmnn sqvsqeicka tevfmcplcd
      301 kncslqrlnd sciyakvtyl fdnggtvffa ifmaiwatvf lefwkrrrsi ltytwdliew
      361 eeeeetlrpq feakyykmei vnpitgkpep hqpssdkvtr llvsvsgiff mislvitavf
      421 gvvvyrlvvm eqfasfkwnf ikqywqfats aaavcinfii imllnlayek iaylltnley
      481 prtesewens falkmflfqf vnlnssifyi afflgrfvgh pgkynklfdr wrleechpsg
      541 clidlclqmg vimflkqiwn nfmelgypli qnwwsrhkik rgihdasipq wendwnlqpm
      601 nlhglmdeyl emvlqfgftt ifvaafplap llallnniie irldaykfvt qwrrplpara
      661 tdigiwlgil egigilavit nafviaitsd yiprfvyeyk ygpcanhvep senclkgyvn
      721 nslsffdlse lgmgksgycr yrdyrgppws skpyeftlqy whilaarlaf iivfehlvfg
      781 iksfiaylip dvpkglhdri rrekylvqem myeaelehlq qqrrksgqpv hhewp
//
LOCUS       NP_055542               2715 aa            linear   PRI 15-DEC-2025
DEFINITION  histone-lysine N-methyltransferase 2B [Homo sapiens].
ACCESSION   NP_055542
VERSION     NP_055542.1
DBSOURCE    REFSEQ: accession NM_014727.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2715)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2715)
  AUTHORS   Becht,D.C., Mohid,S.A., Lee,J.E., Zandian,M., Benz,C., Biswas,S.,
            Sinha,V.K., Ivarsson,Y., Ge,K., Zhang,Y. and Kutateladze,T.G.
  TITLE     MLL4 binds TET3
  JOURNAL   Structure 32 (6), 706-714 (2024)
   PUBMED   38579707
  REMARK    GeneRIF: MLL4 binds TET3.
REFERENCE   3  (residues 1 to 2715)
  AUTHORS   Ramon-Gomez,J.L., Bernal-Pacheco,O., Zarante-Bahamon,A.M.,
            Martinez-Cordoba,N. and Lince-Rivera,I.
  TITLE     [Phenotypic and genotypic spectrum of KMT2B dystonia. Description
            of three Colombian patients]
  JOURNAL   Rev Neurol 78 (10), 285-291 (2024)
   PUBMED   38743022
  REMARK    GeneRIF: [Phenotypic and genotypic spectrum of KMT2B dystonia.
            Description of three Colombian patients].
REFERENCE   4  (residues 1 to 2715)
  AUTHORS   Lee,S., Lee,D.K., Dou,Y., Lee,J., Lee,B., Kwak,E., Kong,Y.Y.,
            Lee,S.K., Roeder,R.G. and Lee,J.W.
  TITLE     Coactivator as a target gene specificity determinant for histone H3
            lysine 4 methyltransferases
  JOURNAL   Proc Natl Acad Sci U S A 103 (42), 15392-15397 (2006)
   PUBMED   17021013
REFERENCE   5  (residues 1 to 2715)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   6  (residues 1 to 2715)
  AUTHORS   Milne,T.A., Dou,Y., Martin,M.E., Brock,H.W., Roeder,R.G. and
            Hess,J.L.
  TITLE     MLL associates specifically with a subset of transcriptionally
            active target genes
  JOURNAL   Proc Natl Acad Sci U S A 102 (41), 14765-14770 (2005)
   PUBMED   16199523
REFERENCE   7  (residues 1 to 2715)
  AUTHORS   Huntsman,D.G., Chin,S.F., Muleris,M., Batley,S.J., Collins,V.P.,
            Wiedemann,L.M., Aparicio,S. and Caldas,C.
  TITLE     MLL2, the second human homolog of the Drosophila trithorax gene,
            maps to 19q13.1 and is amplified in solid tumor cell lines
  JOURNAL   Oncogene 18 (56), 7975-7984 (1999)
   PUBMED   10637508
REFERENCE   8  (residues 1 to 2715)
  AUTHORS   FitzGerald,K.T. and Diaz,M.O.
  TITLE     MLL2: A new mammalian member of the trx/MLL family of genes
  JOURNAL   Genomics 59 (2), 187-192 (1999)
   PUBMED   10409430
REFERENCE   9  (residues 1 to 2715)
  AUTHORS   Abela,L. and Kurian,M.A.
  TITLE     KMT2B-Related Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29697234
REFERENCE   10 (residues 1 to 2715)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AD000671.1 and AJ007041.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein which contains multiple
            domains including a CXXC zinc finger, three PHD zinc fingers, two
            FY-rich domains, and a SET (suppressor of variegation, enhancer of
            zeste, and trithorax) domain. The SET domain is a conserved
            C-terminal domain that characterizes proteins of the MLL
            (mixed-lineage leukemia) family. This gene is ubiquitously
            expressed in adult tissues. It is also amplified in solid tumor
            cell lines, and may be involved in human cancer. Two alternatively
            spliced transcript variants encoding distinct isoforms have been
            reported for this gene, however, the full length nature of the
            shorter transcript is not known. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ007041.1, AF186605.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000420124.4/ ENSP00000398837.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2715
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..2715
                     /product="histone-lysine N-methyltransferase 2B"
                     /EC_number="2.1.1.364"
                     /note="histone-lysine N-methyltransferase MLL4; trithorax
                     homologue 2; WW domain binding protein 7; myeloid/lymphoid
                     or mixed-lineage leukemia (trithorax homolog, Drosophila)
                     4; mixed lineage leukemia gene homolog 2; myeloid/lymphoid
                     or mixed-lineage leukemia protein 4; lysine (K)-specific
                     methyltransferase 2B"
                     /calculated_mol_wt=293385
     Region          1..65
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Region          17..36
                     /region_name="Menin-binding motif (MBM).
                     /evidence=ECO:0000269|PubMed:22327296"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Region          81..302
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08550; propagated from
                     UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08550; propagated from
                     UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08550; propagated from
                     UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Region          320..518
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Region          532..771
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Region          819..868
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            844
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            861
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Region          894..959
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            936
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Region          958..1005
                     /region_name="zf-CXXC"
                     /note="CXXC zinc finger domain; pfam02008"
                     /db_xref="CDD:366873"
     Region          1027..1132
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            1032
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            1035
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            1092
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            1095
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Region          1146..1166
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Region          1203..1249
                     /region_name="PHD1_KMT2B"
                     /note="PHD finger 1 found in Histone-lysine
                     N-methyltransferase 2B (KMT2B); cd15589"
                     /db_xref="CDD:277064"
     Site            order(1203,1214..1218,1222,1244)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277064"
     Region          1251..1300
                     /region_name="PHD2_KMT2B"
                     /note="PHD domain 2 found in Histone-lysine
                     N-methyltransferase 2B (KMT2B); cd15591"
                     /db_xref="CDD:277066"
     Site            order(1251,1264..1268,1272,1295)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277066"
     Region          1337..1393
                     /region_name="PHD3_KMT2B"
                     /note="PHD finger 3 found in Histone-lysine
                     N-methyltransferase 2B (KMT2B); cd15593"
                     /db_xref="CDD:277068"
     Site            order(1337,1353..1357,1361,1388)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277068"
     Region          1374..1516
                     /region_name="Bromo_ALL-1"
                     /note="Bromodomain, ALL-1 like proteins. ALL-1 is a
                     vertebrate homologue of Drosophila trithorax and is often
                     affected in chromosomal rearrangements that are linked to
                     acute leukemias, such as acute lymphocytic leukemia (ALL).
                     Bromodomains are found in many...; cd05493"
                     /db_xref="CDD:99925"
     Site            order(1415,1422,1425,1480,1498)
                     /site_type="other"
                     /note="putative acetyllysine binding site [chemical
                     binding]"
                     /db_xref="CDD:99925"
     Region          1545..1567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Region          1581..1685
                     /region_name="ePHD_KMT2B"
                     /note="Extended PHD finger found in histone-lysine
                     N-methyltransferase 2B (KMT2B); cd15694"
                     /db_xref="CDD:277164"
     Site            order(1640,1649..1653,1659,1680)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277164"
     Region          1733..1780
                     /region_name="FYRN"
                     /note="F/Y-rich N-terminus; pfam05964"
                     /db_xref="CDD:461787"
     Region          1806..1978
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            1930
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            1936
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Region          2008..2093
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            2068
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            2083
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Region          2118..2162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Region          2280..2412
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            2288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Site            2348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Region          2413..2497
                     /region_name="FYRC"
                     /note="FY-rich domain, C-terminal region; smart00542"
                     /db_xref="CDD:197781"
     Region          2508..2513
                     /region_name="WDR5 interaction motif (WIN).
                     /evidence=ECO:0000269|PubMed:22266653,
                     ECO:0000269|PubMed:22665483"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMN6.1)"
     Region          2562..2715
                     /region_name="SET_KMT2A_2B"
                     /note="SET domain (including post-SET domain) found in
                     histone-lysine N-methyltransferase 2A (KMT2A), 2B (KMT2B)
                     and similar proteins; cd19170"
                     /db_xref="CDD:380947"
     Site            order(2584..2587,2604,2629..2634,2648..2653,2661..2663,
                     2672,2688..2693,2702..2705,2714)
                     /site_type="active"
                     /db_xref="CDD:380947"
     Site            order(2584..2587,2629,2649..2653,2690,2702..2705)
                     /site_type="other"
                     /note="SAM binding site"
                     /db_xref="CDD:380947"
     Site            order(2604,2629..2634,2648..2649,2651,2661..2663,2672,
                     2688..2693)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:380947"
     Site            order(2655,2703,2705,2710)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380947"
     CDS             1..2715
                     /gene="KMT2B"
                     /gene_synonym="CXXC10; DYT28; HRX2; MLL1B; MLL2; MLL4;
                     MRD68; TRX2; WBP-7; WBP7"
                     /coded_by="NM_014727.3:17..8164"
                     /db_xref="CCDS:CCDS46055.1"
                     /db_xref="GeneID:9757"
                     /db_xref="HGNC:HGNC:15840"
                     /db_xref="MIM:606834"
ORIGIN      
        1 maaaagggsc pgpgsargrf pgrprgaggg ggrggrgnga ervrvalrrg ggatgpggae
       61 pgedtallrl lglrrglrrl rrlwagprvq rgrgrgrgrg wgpsrgcvpe eessdgesde
      121 eefqgfhsde dvapsslrsa lrsqrgrapr grgrkhkttp lppprladva ptppktpark
      181 rgeegtermv qaltellrra qapqaprsra cepstprrsr grppgrpagp crrkqqavvv
      241 aeaavtipkp eppppvvpvk hqtgswkcke gpgpgpgtpr rggqssrggr ggrgrgrggg
      301 lpfvikfvsr akkvkmgqls lglesgqgqg qheeswqdvp qrrvgsgqgg spcwkkqeqk
      361 lddeeeekke eeekdkegee keeravaeem mpaaekeeak lppppltppa pspppplppp
      421 stspppplcp pppppvsppp lpspppppaq eeqeespppv vpatcsrkrg rppltpsqra
      481 ereaaragpe gtspptptps tatggppeds ptvapksttf lknirqfimp vvsarssrvi
      541 ktprrfmded ppkppkvevs pvlrppitts ppvpqepapv psppraptpp stpvplpekr
      601 rsilreptfr wtsltrelpp pppapppppa pspppapats srrplllrap qftpseahlk
      661 iyesvltppp lgapeapepe pppaddspae pepravgrtn hlslprfapv vttpvkaevs
      721 phgapalsng pqtqaqllqp lqalqtqllp qalpppqpql qpppspqqmp plekariagv
      781 gslplsgvee kmfsllkrak vqlfkidqqq qqkvaasmpl spggqmeeva gavkqisdrg
      841 pvrsedesve akrerpsgpe spvqgprikh vcrhaavalg qaramvpedv prlsalplrd
      901 rqdlatedts sasetesvps rsrrgkveaa gpggeseptg sggtlahtpr rslpshhgkk
      961 mrmarcghcr gclrvqdcgs cvncldkpkf ggpntkkqcc vyrkcdkiea rkmerlakkg
     1021 rtivktllpw dsdespeasp gppgprrgag aggpreevva hpgpeeqdsl lqrksarrcv
     1081 kqrpsydife dsddsepggp paprrrtpre nelplpepee qsrprkptlq pvlqlkarrr
     1141 ldkdalapgp fasfpngwtg kqkspdgvhr vrvdfkedcd lenvwlmggl svltsvpggp
     1201 pmvcllcask glhelvfcqv ccdpfhpfcl eeaerplpqh hdtwccrrck fchvcgrkgr
     1261 gskhllecer crhayhpacl gpsyptratr krrhwicsac vrckscgatp gknwdvewsg
     1321 dyslcprctq lyekgnycpi ctrcyedndy eskmmqcaqc dhwvhakceg lsdedyeils
     1381 glpdsvlytc gpcagaaqpr wrealsgalq gglrqvlqgl lsskvvgpll lctqcgpdgk
     1441 qlhpgpcglq avsqrfedgh yksvhsfmed mvgilmrhse egetpdrrag gqmkglllkl
     1501 lesafgwfda hdpkywrrst rlpngvlpna vlppsldhvy aqwrqqepet pesgqppgdp
     1561 saafqgkdpa afshledprq calclkygda dskeagrlly igqnewthvn caiwsaevfe
     1621 endgslknvh aavargrqmr celclkpgat vgcclsscls nfhfmcaras ycifqddkkv
     1681 fcqkhtdlld gkeivnpdgf dvlrrvyvdf eginfkrkfl tglepdainv ligsiridsl
     1741 gtlsdlsdce grlfpigyqc srlywstvda rrrcwyrcri leyrpwgpre epahleaaee
     1801 nqtivhspap sseppggedp pldtdvlvpg aperhspiqn ldpplrpdsg sapppaprsf
     1861 sgarikvpny spsrrplggv sfgplpspgs psslthhipt vgdpdfpapp rrsrrpspla
     1921 prpppsrwas pplktspqlr vppptsvvta ltptsgelap pgpapspppp edlgpdfedm
     1981 evvsglsaad ldfaasllgt epfqeeivaa gamgsshggp gdsseeessp tsryihfpvt
     2041 vvsapglaps atpgaprieq ldgvddgtds eaeavqqprg qgtppsgpgv vragvlgaag
     2101 drarppedlp seivdfvlkn lggpgdggag preeslppap plangsqpsq gltaspadpt
     2161 rtfawlpgap gvrvlslgpa peppkpatsk iilvnklgqv fvkmagegep vpppvkqppl
     2221 pptisptapt swtlppgpll gvlpvvgvvr papppppppl tlvlssgpas pprqairvkr
     2281 vstfsgrspp apppykaprl dedgeasedt pqvpglgsgg fsrvrmktpt vrgvldldrp
     2341 gepageespg plqerspllp lpedgppqvp dgppdllles qwhhysgeas sseeeppspd
     2401 dkenqapkrt gphlrfeiss edgfsveaes legawrtlie kvqearghar lrhlsfsgms
     2461 garllgihhd aviflaeqlp gaqrcqhykf ryhqqgegqe epplnphgaa raevylrkct
     2521 fdmfnflasq hrvlpegatc deeedevqlr strratslel pmamrfrhlk ktskeavgvy
     2581 rsaihgrglf ckrnidagem vieysgivir svltdkrekf ydgkgigcym frmddfdvvd
     2641 atmhgnaarf inhscepncf srvihvegqk hivifalrri lrgeeltydy kfpiedasnk
     2701 lpcncgakrc rrfln
//
LOCUS       NP_006078                444 aa            linear   PRI 15-DEC-2025
DEFINITION  tubulin beta-4A chain isoform 3 [Homo sapiens].
ACCESSION   NP_006078
VERSION     NP_006078.2
DBSOURCE    REFSEQ: accession NM_006087.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Garg,D., Holla,V.V., Ganguly,J., Rajan,R., Saini,A., Agarwal,A.,
            Radhakrishnan,D.M., Basu,P., Mondal,B., Dhar,D., Kamble,N.,
            Yadav,R., Muthusamy,B., Kumar,H., Srivastava,A.K. and Pal,P.K.
  TITLE     Expanding the phenotypic and genotypic spectrum of DYT-TUBB4A with
            seven patients from India
  JOURNAL   Parkinsonism Relat Disord 124, 107012 (2024)
   PUBMED   38762926
  REMARK    GeneRIF: Expanding the phenotypic and genotypic spectrum of
            DYT-TUBB4A with seven patients from India.
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Ben Jdila,M., Kammoun,F., Abdelmaksoud-Dammak,R., Triki,C. and
            Fakhfakh,F.
  TITLE     Mutation in the beta-tubulin gene TUBB4A results in epileptic
            encephalopathy associated with hypomyelinated leucodystrophy:
            Unexpected findings reveal genetic mosaicism
  JOURNAL   Int J Dev Neurosci 83 (6), 532-545 (2023)
   PUBMED   37529938
  REMARK    GeneRIF: Mutation in the beta-tubulin gene TUBB4A results in
            epileptic encephalopathy associated with hypomyelinated
            leucodystrophy: Unexpected findings reveal genetic mosaicism.
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Simons,C., Wolf,N.I., McNeil,N., Caldovic,L., Devaney,J.M.,
            Takanohashi,A., Crawford,J., Ru,K., Grimmond,S.M., Miller,D.,
            Tonduti,D., Schmidt,J.L., Chudnow,R.S., van Coster,R., Lagae,L.,
            Kisler,J., Sperner,J., van der Knaap,M.S., Schiffmann,R., Taft,R.J.
            and Vanderver,A.
  TITLE     A de novo mutation in the beta-tubulin gene TUBB4A results in the
            leukoencephalopathy hypomyelination with atrophy of the basal
            ganglia and cerebellum
  JOURNAL   Am J Hum Genet 92 (5), 767-773 (2013)
   PUBMED   23582646
  REMARK    GeneRIF: A de novo mutation in the beta-tubulin gene TUBB4A results
            in the leukoencephalopathy hypomyelination with atrophy of the
            basal ganglia and cerebellum.
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Hersheson,J., Mencacci,N.E., Davis,M., MacDonald,N., Trabzuni,D.,
            Ryten,M., Pittman,A., Paudel,R., Kara,E., Fawcett,K., Plagnol,V.,
            Bhatia,K.P., Medlar,A.J., Stanescu,H.C., Hardy,J., Kleta,R.,
            Wood,N.W. and Houlden,H.
  TITLE     Mutations in the autoregulatory domain of beta-tubulin 4a cause
            hereditary dystonia
  JOURNAL   Ann Neurol 73 (4), 546-553 (2013)
   PUBMED   23424103
  REMARK    GeneRIF: This study demonistrated that TUBB4A mutation in the
            autoregulatory domain cause hereditary dystonia.
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Nahhas,N., Conant,A., Hamilton,E., Curiel,J., Simons,C., van der
            Knaap,M. and Vanderver,A.
  TITLE     TUBB4A-Related Leukodystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27809427
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   8  (residues 1 to 444)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   9  (residues 1 to 444)
  AUTHORS   Wang,D., Villasante,A., Lewis,S.A. and Cowan,N.J.
  TITLE     The mammalian beta-tubulin repertoire: hematopoietic expression of
            a novel, heterologous beta-tubulin isotype
  JOURNAL   J Cell Biol 103 (5), 1903-1910 (1986)
   PUBMED   3782288
REFERENCE   10 (residues 1 to 444)
  AUTHORS   Lee,M.G., Loomis,C. and Cowan,N.J.
  TITLE     Sequence of an expressed human beta-tubulin gene containing ten Alu
            family members
  JOURNAL   Nucleic Acids Res 12 (14), 5823-5836 (1984)
   PUBMED   6462917
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC013683.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 10, 2002 this sequence version replaced NP_006078.1.
            
            Summary: This gene encodes a member of the beta tubulin family.
            Beta tubulins are one of two core protein families (alpha and beta
            tubulins) that heterodimerize and assemble to form microtubules.
            Mutations in this gene cause hypomyelinating leukodystrophy-6 and
            autosomal dominant torsion dystonia-4. Alternate splicing results
            in multiple transcript variants encoding different isoforms. A
            pseudogene of this gene is found on chromosome X. [provided by
            RefSeq, Jan 2014].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            lacks a portion of the 5' coding region, compared to variant 1. The
            resulting isoform (3) has a shorter N-terminus, compared to isoform
            1. Both variants 3 and 4 encode the same isoform 3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC013683.1, AK075307.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267753 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264071.7/ ENSP00000264071.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..444
                     /product="tubulin beta-4A chain isoform 3"
                     /note="tubulin, beta, 5; dystonia 4, torsion (autosomal
                     dominant); tubulin beta-4 chain; tubulin, beta 4"
                     /calculated_mol_wt=49455
     Region          1..427
                     /region_name="PLN00220"
                     /note="tubulin beta chain; Provisional"
                     /db_xref="CDD:215107"
     Region          1..4
                     /region_name="MREI motif.
                     /evidence=ECO:0000250|UniProtKB:P07437"
                     /note="propagated from UniProtKB/Swiss-Prot (P04350.2)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:16371510; propagated from
                     UniProtKB/Swiss-Prot (P04350.2)"
     CDS             1..444
                     /gene="TUBB4A"
                     /gene_synonym="beta-5; DYT4; TUBB4"
                     /coded_by="NM_006087.4:98..1432"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS12168.1"
                     /db_xref="GeneID:10382"
                     /db_xref="HGNC:HGNC:20774"
                     /db_xref="MIM:602662"
ORIGIN      
        1 mreivhlqag qcgnqigakf wevisdehgi dptgtyhgds dlqlerinvy yneatggnyv
       61 pravlvdlep gtmdsvrsgp fgqifrpdnf vfgqsgagnn wakghytega elvdavldvv
      121 rkeaescdcl qgfqlthslg ggtgsgmgtl liskireefp drimntfsvv pspkvsdtvv
      181 epynatlsvh qlventdety cidnealydi cfrtlklttp tygdlnhlvs atmsgvttcl
      241 rfpgqlnadl rklavnmvpf prlhffmpgf apltsrgsqq yraltvpelt qqmfdaknmm
      301 aacdprhgry ltvaavfrgr msmkevdeqm lsvqsknssy fvewipnnvk tavcdipprg
      361 lkmaatfign staiqelfkr iseqftamfr rkaflhwytg egmdemefte aesnmndlvs
      421 eyqqyqdata eegefeeeae eeva
//
LOCUS       NP_001373000             566 aa            linear   PRI 15-DEC-2025
DEFINITION  aminopeptidase O isoform 4 [Homo sapiens].
ACCESSION   NP_001373000
VERSION     NP_001373000.1
DBSOURCE    REFSEQ: accession NM_001386071.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Lin,J., Li,C., Cui,Y., Hou,Y., Zhang,L., Ou,R., Wei,Q., Liu,K.,
            Huang,R., Yang,T., Xiao,Y., Jiang,Q., Yang,J., Chen,X. and Shang,H.
  TITLE     Mutation screening of AOPEP variants in a large dystonia cohort
  JOURNAL   J Neurol 270 (6), 3225-3233 (2023)
   PUBMED   36933031
  REMARK    GeneRIF: Mutation screening of AOPEP variants in a large dystonia
            cohort.
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Garavaglia,B., Vallian,S., Romito,L.M., Straccia,G., Capecci,M.,
            Invernizzi,F., Andrenelli,E., Kazemi,A., Boesch,S., Kopajtich,R.,
            Olfati,N., Shariati,M., Shoeibi,A., Sadr-Nabavi,A., Prokisch,H.,
            Winkelmann,J. and Zech,M.
  TITLE     AOPEP variants as a novel cause of recessive dystonia: Generalized
            dystonia and dystonia-parkinsonism
  JOURNAL   Parkinsonism Relat Disord 97, 52-56 (2022)
   PUBMED   35306330
  REMARK    GeneRIF: AOPEP variants as a novel cause of recessive dystonia:
            Generalized dystonia and dystonia-parkinsonism.
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Zech,M., Kumar,K.R., Reining,S., Reunert,J., Tchan,M., Riley,L.G.,
            Drew,A.P., Adam,R.J., Berutti,R., Biskup,S., Derive,N.,
            Bakhtiari,S., Jin,S.C., Kruer,M.C., Bardakjian,T.,
            Gonzalez-Alegre,P., Keller Sarmiento,I.J., Mencacci,N.E.,
            Lubbe,S.J., Kurian,M.A., Clot,F., Meneret,A., de Sainte
            Agathe,J.M., Fung,V.S.C., Vidailhet,M., Baumann,M., Marquardt,T.,
            Winkelmann,J. and Boesch,S.
  TITLE     Biallelic AOPEP Loss-of-Function Variants Cause Progressive
            Dystonia with Prominent Limb Involvement
  JOURNAL   Mov Disord 37 (1), 137-147 (2022)
   PUBMED   34596301
  REMARK    GeneRIF: Biallelic AOPEP Loss-of-Function Variants Cause
            Progressive Dystonia with Prominent Limb Involvement.
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Lybech,L.K.M., Calabro,M., Briuglia,S., Drago,A. and Crisafulli,C.
  TITLE     Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings
  JOURNAL   Genes (Basel) 12 (10), 1482 (2021)
   PUBMED   34680877
  REMARK    GeneRIF: Suicide Related Phenotypes in a Bipolar Sample: Genetic
            Underpinnings.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Ichikawa,M., Konoshita,T., Makino,Y., Suzuki,J., Ishizuka,T. and
            Nakamura,H.
  TITLE     An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes
  JOURNAL   Sci Rep 10 (1), 16111 (2020)
   PUBMED   32999396
  REMARK    GeneRIF: An association study of C9orf3, a novel component of the
            renin-angiotensin system, and hypertension in diabetes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 566)
  AUTHORS   Shi,Y., Zhao,H., Shi,Y., Cao,Y., Yang,D., Li,Z., Zhang,B.,
            Liang,X., Li,T., Chen,J., Shen,J., Zhao,J., You,L., Gao,X., Zhu,D.,
            Zhao,X., Yan,Y., Qin,Y., Li,W., Yan,J., Wang,Q., Zhao,J., Geng,L.,
            Ma,J., Zhao,Y., He,G., Zhang,A., Zou,S., Yang,A., Liu,J., Li,W.,
            Li,B., Wan,C., Qin,Y., Shi,J., Yang,J., Jiang,H., Xu,J.E., Qi,X.,
            Sun,Y., Zhang,Y., Hao,C., Ju,X., Zhao,D., Ren,C.E., Li,X.,
            Zhang,W., Zhang,Y., Zhang,J., Wu,D., Zhang,C., He,L. and Chen,Z.J.
  TITLE     Genome-wide association study identifies eight new risk loci for
            polycystic ovary syndrome
  JOURNAL   Nat Genet 44 (9), 1020-1025 (2012)
   PUBMED   22885925
REFERENCE   7  (residues 1 to 566)
  AUTHORS   Ellinor,P.T., Lunetta,K.L., Albert,C.M., Glazer,N.L., Ritchie,M.D.,
            Smith,A.V., Arking,D.E., Muller-Nurasyid,M., Krijthe,B.P.,
            Lubitz,S.A., Bis,J.C., Chung,M.K., Dorr,M., Ozaki,K., Roberts,J.D.,
            Smith,J.G., Pfeufer,A., Sinner,M.F., Lohman,K., Ding,J.,
            Smith,N.L., Smith,J.D., Rienstra,M., Rice,K.M., Van Wagoner,D.R.,
            Magnani,J.W., Wakili,R., Clauss,S., Rotter,J.I., Steinbeck,G.,
            Launer,L.J., Davies,R.W., Borkovich,M., Harris,T.B., Lin,H.,
            Volker,U., Volzke,H., Milan,D.J., Hofman,A., Boerwinkle,E.,
            Chen,L.Y., Soliman,E.Z., Voight,B.F., Li,G., Chakravarti,A.,
            Kubo,M., Tedrow,U.B., Rose,L.M., Ridker,P.M., Conen,D., Tsunoda,T.,
            Furukawa,T., Sotoodehnia,N., Xu,S., Kamatani,N., Levy,D.,
            Nakamura,Y., Parvez,B., Mahida,S., Furie,K.L., Rosand,J.,
            Muhammad,R., Psaty,B.M., Meitinger,T., Perz,S., Wichmann,H.E.,
            Witteman,J.C., Kao,W.H., Kathiresan,S., Roden,D.M.,
            Uitterlinden,A.G., Rivadeneira,F., McKnight,B., Sjogren,M.,
            Newman,A.B., Liu,Y., Gollob,M.H., Melander,O., Tanaka,T.,
            Stricker,B.H., Felix,S.B., Alonso,A., Darbar,D., Barnard,J.,
            Chasman,D.I., Heckbert,S.R., Benjamin,E.J., Gudnason,V. and Kaab,S.
  TITLE     Meta-analysis identifies six new susceptibility loci for atrial
            fibrillation
  JOURNAL   Nat Genet 44 (6), 670-675 (2012)
   PUBMED   22544366
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 566)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   9  (residues 1 to 566)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 566)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157936.12 and AL353768.28.
            
            Summary: This gene encodes a member of the M1 zinc aminopeptidase
            family. The encoded protein is a zinc-dependent metallopeptidase
            that catalyzes the removal of an amino acid from the amino terminus
            of a protein or peptide. This protein may play a role in the
            generation of angiotensin IV. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1433691.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..566
                     /product="aminopeptidase O isoform 4"
                     /calculated_mol_wt=63232
     Region          <244..>509
                     /region_name="GluZincin"
                     /note="Gluzincin Peptidase family (thermolysin-like
                     proteinases, TLPs) which includes peptidases M1, M2, M3,
                     M4, M13, M32 and M36 (fungalysins); cl14813"
                     /db_xref="CDD:472708"
     CDS             1..566
                     /gene="AOPEP"
                     /gene_synonym="AP-O; APO; C90RF3; C9orf3; DYT31; ONPEP"
                     /coded_by="NM_001386071.1:370..2070"
                     /note="isoform 4 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS55327.1"
                     /db_xref="GeneID:84909"
                     /db_xref="HGNC:HGNC:1361"
                     /db_xref="MIM:619600"
ORIGIN      
        1 mdiqldpard dlplmantsh ilvkhyvldl dvdfesqvie gtivlfledg nrfkkqnssi
       61 eeacqsesnk ackfgmpepc hipvtnartf ssemeyndfa icskgekdts dkdgnhdnqe
      121 hasgisssky ccdtgnhgse dfllvldccd lsvlkveevd vaavpglekf trspeltvvs
      181 eefrnqivre lvtlpanrwr eqldyyarcs qapgcgellf dtdtwslqir ktgaqtatdf
      241 phairiwykt kpegrsvtwt sdqsgrpcvy tvgspinnra lfpcqeppva mstwqatvra
      301 aasfvvlmsg ensakptqlw eecsswyyyv tmpmpastft iavgcwtemk metwssndla
      361 terpfspsea nfrhvgvcsh meypcrfqna sattqeiiph rvfapvcltg acqetllrli
      421 ppclsaahsv lgahpfsrld vlivpanfps lgmasphimf lsqsiltggn hlcgtrlche
      481 iahawfglai gardwteewl segfathled vfwataqqla pyeareqqel raclrwrrlq
      541 demqcspeem qvlrfphvgg csgsfs
//
LOCUS       NP_001155967             219 aa            linear   PRI 16-DEC-2025
DEFINITION  exosomal polycystin-1-interacting protein precursor [Homo sapiens].
ACCESSION   NP_001155967
VERSION     NP_001155967.2
DBSOURCE    REFSEQ: accession NM_001162495.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Lea,W.A., Winklhofer,T., Zelenchuk,L., Sharma,M.,
            Rossol-Allison,J., Fields,T.A., Reif,G., Calvet,J.P.,
            Bakeberg,J.L., Wallace,D.P. and Ward,C.J.
  TITLE     Polycystin-1 Interacting Protein-1 (CU062) Interacts with the
            Ectodomain of Polycystin-1 (PC1)
  JOURNAL   Cells 12 (17), 2166 (2023)
   PUBMED   37681898
  REMARK    GeneRIF: Polycystin-1 Interacting Protein-1 (CU062) Interacts with
            the Ectodomain of Polycystin-1 (PC1).
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Kang,T.W., Kim,H.J., Ju,H., Kim,J.H., Jeon,Y.J., Lee,H.C.,
            Kim,K.K., Kim,J.W., Lee,S., Kim,J.Y., Kim,S.Y. and Kim,Y.S.
  TITLE     Genome-wide association of serum bilirubin levels in Korean
            population
  JOURNAL   Hum Mol Genet 19 (18), 3672-3678 (2010)
   PUBMED   20639394
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Denoeud,F., Kapranov,P., Ucla,C., Frankish,A., Castelo,R.,
            Drenkow,J., Lagarde,J., Alioto,T., Manzano,C., Chrast,J., Dike,S.,
            Wyss,C., Henrichsen,C.N., Holroyd,N., Dickson,M.C., Taylor,R.,
            Hance,Z., Foissac,S., Myers,R.M., Rogers,J., Hubbard,T., Harrow,J.,
            Guigo,R., Gingeras,T.R., Antonarakis,S.E. and Reymond,A.
  TITLE     Prominent use of distal 5' transcription start sites and discovery
            of a large number of additional exons in ENCODE regions
  JOURNAL   Genome Res 17 (6), 746-759 (2007)
   PUBMED   17567994
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Gardiner,K., Slavov,D., Bechtel,L. and Davisson,M.
  TITLE     Annotation of human chromosome 21 for relevance to Down syndrome:
            gene structure and expression analysis
  JOURNAL   Genomics 79 (6), 833-843 (2002)
   PUBMED   12036298
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Slavov,D., Hattori,M., Sakaki,Y., Rosenthal,A., Shimizu,N.,
            Minoshima,S., Kudoh,J., Yaspo,M.L., Ramser,J., Reinhardt,R.,
            Reimer,C., Clancy,K., Rynditch,A. and Gardiner,K.
  TITLE     Criteria for gene identification and features of genome
            organization: analysis of 6.5 Mb of DNA sequence from human
            chromosome 21
  JOURNAL   Gene 247 (1-2), 215-232 (2000)
   PUBMED   10773462
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DQ656042.2, BC069779.1, BC069689.1, AP000280.3 and BE466137.1.
            
            On Jul 30, 2009 this sequence version replaced NP_001155967.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC069779.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245, SAMEA2145774
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000479548.2/ ENSP00000418653.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.11"
     Protein         1..219
                     /product="exosomal polycystin-1-interacting protein
                     precursor"
                     /note="uncharacterized protein C21orf62;
                     polycystin-1-interacting protein 1"
                     /calculated_mol_wt=22079
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2790
     Region          2..219
                     /region_name="DUF4571"
                     /note="Domain of unknown function (DUF4571); pfam15137"
                     /db_xref="CDD:464523"
     CDS             1..219
                     /gene="EPCIP"
                     /gene_synonym="B37; C21orf120; C21orf62; CU062; PRED81"
                     /coded_by="NM_001162495.3:333..992"
                     /db_xref="CCDS:CCDS42919.2"
                     /db_xref="GeneID:56245"
                     /db_xref="HGNC:HGNC:1305"
                     /db_xref="MIM:621445"
ORIGIN      
        1 mappsrhcll listlgvfal ncftkgqkns tliftrenti rncscsadir dcdyslanlm
       61 cncktvlpla vertsynghl tiwftdtsal ghllnftlvq dlklslcstn tlpteylaic
      121 glkrlrinme akhpfpeqsl lihsggdsds rekpmwlhkg wqpcmyisfl dmalfnrdsa
      181 lksysienvt siannfpdfs yfrtfpmpsn ksyvvtfiy
//
LOCUS       NP_001428628             186 aa            linear   PRI 16-DEC-2025
DEFINITION  regulated endocrine-specific protein 18 precursor [Homo sapiens].
ACCESSION   NP_001428628
VERSION     NP_001428628.1
DBSOURCE    REFSEQ: accession NM_001441699.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Zhong,X., Han,X., Xie,Q., Chen,W., Geng,D., Guo,G., Chen,X.,
            Zhang,W., Chen,J. and Tang,S.
  TITLE     Identification of RESP18 Gene Mutations Linked to Hereditary
            Non-Syndromic Cleft Lip and Palate in a Southern Chinese Family
  JOURNAL   Med Sci Monit 30, e944294 (2024)
   PUBMED   38970244
  REMARK    GeneRIF: Identification of RESP18 Gene Mutations Linked to
            Hereditary Non-Syndromic Cleft Lip and Palate in a Southern Chinese
            Family.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Sosa,L., Torkko,J.M., Primo,M.E., Llovera,R.E., Toledo,P.L.,
            Rios,A.S., Flecha,F.L., Trabucchi,A., Valdez,S.N., Poskus,E.,
            Solimena,M. and Ermacora,M.R.
  TITLE     Biochemical, biophysical, and functional properties of ICA512/IA-2
            RESP18 homology domain
  JOURNAL   Biochim Biophys Acta 1864 (5), 511-522 (2016)
   PUBMED   26836020
  REMARK    GeneRIF: RESP18HD is required for efficient sorting of ICA512 to
            secretory granules: RESP18HD is a key determinant for ICA512
            granule targeting.
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Huang,Y., Xu,J., Liang,M., Hong,X., Suo,H., Liu,J., Yu,M. and
            Huang,F.
  TITLE     RESP18 is involved in the cytotoxicity of dopaminergic neurotoxins
            in MN9D cells
  JOURNAL   Neurotox Res 24 (2), 164-175 (2013)
   PUBMED   23319378
  REMARK    GeneRIF: Over-expression of RESP18 resulted in aggravated cell
            death induced by dopaminergic neurotoxins.
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Zhang,G., Hirai,H., Cai,T., Miura,J., Yu,P., Huang,H.,
            Schiller,M.R., Swaim,W.D., Leapman,R.D. and Notkins,A.L.
  TITLE     RESP18, a homolog of the luminal domain IA-2, is found in dense
            core vesicles in pancreatic islet cells and is induced by high
            glucose
  JOURNAL   J Endocrinol 195 (2), 313-321 (2007)
   PUBMED   17951542
  REMARK    GeneRIF: RESP18 is a luminal protein of DCVs and its expression is
            regulated by exposure to glucose.
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Bloomquist,B.T., Darlington,D.N., Mueller,G.P., Mains,R.E. and
            Eipper,B.A.
  TITLE     Regulated endocrine-specific protein-18: a short-lived novel
            glucocorticoid-regulated endocrine protein
  JOURNAL   Endocrinology 135 (6), 2714-2722 (1994)
   PUBMED   7988462
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114803.5.
            
            Sequence Note: This transcript uses a non-AUG start codon.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3282523.1,
                                           SRR7410570.213331.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            non-AUG initiation codon :: inferred from conservation
            RefSeq Select criteria   :: based on single protein-coding
                                        transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..186
                     /product="regulated endocrine-specific protein 18
                     precursor"
                     /note="regulated endocrine-specific protein 18 homolog"
                     /calculated_mol_wt=17416
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3188
     Region          37..124
                     /region_name="RESP18"
                     /note="RESP18 domain; pfam14948"
                     /db_xref="CDD:464394"
     CDS             1..186
                     /gene="RESP18"
                     /coded_by="NM_001441699.1:116..676"
                     /note="non-AUG (AUA) translation initiation codon"
                     /db_xref="GeneID:389075"
                     /db_xref="HGNC:HGNC:33762"
                     /db_xref="MIM:612721"
ORIGIN      
        1 mqhplwpgss eglqllvcfl llnscpggcs dtsahdgqdq vgvgqlwplq gfatpvfqhl
       61 qvvlqqiipq glfwkdditq damiqkmeha srlhpqepcl kdgkalfptk ttesplakvn
      121 rdqcftsevv skalkqevan pvkityrcsy ggldmmqapg pskeeiiyki mrllwatsyc
      181 gpqpcg
//
LOCUS       NP_001155968             219 aa            linear   PRI 16-DEC-2025
DEFINITION  exosomal polycystin-1-interacting protein precursor [Homo sapiens].
ACCESSION   NP_001155968
VERSION     NP_001155968.2
DBSOURCE    REFSEQ: accession NM_001162496.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Lea,W.A., Winklhofer,T., Zelenchuk,L., Sharma,M.,
            Rossol-Allison,J., Fields,T.A., Reif,G., Calvet,J.P.,
            Bakeberg,J.L., Wallace,D.P. and Ward,C.J.
  TITLE     Polycystin-1 Interacting Protein-1 (CU062) Interacts with the
            Ectodomain of Polycystin-1 (PC1)
  JOURNAL   Cells 12 (17), 2166 (2023)
   PUBMED   37681898
  REMARK    GeneRIF: Polycystin-1 Interacting Protein-1 (CU062) Interacts with
            the Ectodomain of Polycystin-1 (PC1).
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Kang,T.W., Kim,H.J., Ju,H., Kim,J.H., Jeon,Y.J., Lee,H.C.,
            Kim,K.K., Kim,J.W., Lee,S., Kim,J.Y., Kim,S.Y. and Kim,Y.S.
  TITLE     Genome-wide association of serum bilirubin levels in Korean
            population
  JOURNAL   Hum Mol Genet 19 (18), 3672-3678 (2010)
   PUBMED   20639394
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Denoeud,F., Kapranov,P., Ucla,C., Frankish,A., Castelo,R.,
            Drenkow,J., Lagarde,J., Alioto,T., Manzano,C., Chrast,J., Dike,S.,
            Wyss,C., Henrichsen,C.N., Holroyd,N., Dickson,M.C., Taylor,R.,
            Hance,Z., Foissac,S., Myers,R.M., Rogers,J., Hubbard,T., Harrow,J.,
            Guigo,R., Gingeras,T.R., Antonarakis,S.E. and Reymond,A.
  TITLE     Prominent use of distal 5' transcription start sites and discovery
            of a large number of additional exons in ENCODE regions
  JOURNAL   Genome Res 17 (6), 746-759 (2007)
   PUBMED   17567994
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Gardiner,K., Slavov,D., Bechtel,L. and Davisson,M.
  TITLE     Annotation of human chromosome 21 for relevance to Down syndrome:
            gene structure and expression analysis
  JOURNAL   Genomics 79 (6), 833-843 (2002)
   PUBMED   12036298
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Slavov,D., Hattori,M., Sakaki,Y., Rosenthal,A., Shimizu,N.,
            Minoshima,S., Kudoh,J., Yaspo,M.L., Ramser,J., Reinhardt,R.,
            Reimer,C., Clancy,K., Rynditch,A. and Gardiner,K.
  TITLE     Criteria for gene identification and features of genome
            organization: analysis of 6.5 Mb of DNA sequence from human
            chromosome 21
  JOURNAL   Gene 247 (1-2), 215-232 (2000)
   PUBMED   10773462
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DQ656042.2, BC069709.1, BC069689.1, AP000280.3 and BE466137.1.
            
            On Jul 30, 2009 this sequence version replaced NP_001155968.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.258189.1,
                                           SRR1803615.208250.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.11"
     Protein         1..219
                     /product="exosomal polycystin-1-interacting protein
                     precursor"
                     /note="uncharacterized protein C21orf62;
                     polycystin-1-interacting protein 1"
                     /calculated_mol_wt=22079
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2790
     Region          2..219
                     /region_name="DUF4571"
                     /note="Domain of unknown function (DUF4571); pfam15137"
                     /db_xref="CDD:464523"
     CDS             1..219
                     /gene="EPCIP"
                     /gene_synonym="B37; C21orf120; C21orf62; CU062; PRED81"
                     /coded_by="NM_001162496.3:177..836"
                     /db_xref="CCDS:CCDS42919.2"
                     /db_xref="GeneID:56245"
                     /db_xref="HGNC:HGNC:1305"
                     /db_xref="MIM:621445"
ORIGIN      
        1 mappsrhcll listlgvfal ncftkgqkns tliftrenti rncscsadir dcdyslanlm
       61 cncktvlpla vertsynghl tiwftdtsal ghllnftlvq dlklslcstn tlpteylaic
      121 glkrlrinme akhpfpeqsl lihsggdsds rekpmwlhkg wqpcmyisfl dmalfnrdsa
      181 lksysienvt siannfpdfs yfrtfpmpsn ksyvvtfiy
//
LOCUS       NP_001338611             126 aa            linear   PRI 16-DEC-2025
DEFINITION  zinc finger protein 787 isoform 2 [Homo sapiens].
ACCESSION   NP_001338611
VERSION     NP_001338611.1
DBSOURCE    REFSEQ: accession NM_001351682.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Zhang,L., Zhu,B., Zhou,X., Ning,H., Zhang,F., Yan,B., Chen,J. and
            Ma,T.
  TITLE     ZNF787 and HDAC1 Mediate Blood-Brain Barrier Permeability in an In
            Vitro Model of Alzheimer's Disease Microenvironment
  JOURNAL   Neurotox Res 42 (1), 12 (2024)
   PUBMED   38329647
  REMARK    GeneRIF: ZNF787 and HDAC1 Mediate Blood-Brain Barrier Permeability
            in an In Vitro Model of Alzheimer's Disease Microenvironment.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY059733.1, BC037737.1 and AC024580.6.
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            coding sequence compared to variant 1. The resulting isoform (2)
            has a shorter and distinct C-terminus compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.937134.1,
                                           SRR1163658.373823.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..126
                     /product="zinc finger protein 787 isoform 2"
                     /note="transcription termination factor I interacting
                     peptide 20; TTF-I-interacting peptide 20"
                     /calculated_mol_wt=13223
     CDS             1..126
                     /gene="ZNF787"
                     /gene_synonym="TIP20"
                     /coded_by="NM_001351682.2:135..515"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS86810.1"
                     /db_xref="GeneID:126208"
                     /db_xref="HGNC:HGNC:26998"
                     /db_xref="MIM:621447"
ORIGIN      
        1 melreeawsp gpldsedqqm ashenpgeqp eafpadpaas hltlasfasg weetplpcfp
       61 llgpwdhptl asppalglal lavegglvlw lqvsfllddl gdpwgppslp dflcpcpssl
      121 gstpvc
//
LOCUS       NP_001002836             382 aa            linear   PRI 16-DEC-2025
DEFINITION  zinc finger protein 787 isoform 1 [Homo sapiens].
ACCESSION   NP_001002836 XP_058999
VERSION     NP_001002836.2
DBSOURCE    REFSEQ: accession NM_001002836.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Zhang,L., Zhu,B., Zhou,X., Ning,H., Zhang,F., Yan,B., Chen,J. and
            Ma,T.
  TITLE     ZNF787 and HDAC1 Mediate Blood-Brain Barrier Permeability in an In
            Vitro Model of Alzheimer's Disease Microenvironment
  JOURNAL   Neurotox Res 42 (1), 12 (2024)
   PUBMED   38329647
  REMARK    GeneRIF: ZNF787 and HDAC1 Mediate Blood-Brain Barrier Permeability
            in an In Vitro Model of Alzheimer's Disease Microenvironment.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC024580.6, BC077728.1, KF573663.1 and AI037960.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 24, 2007 this sequence version replaced NP_001002836.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC077728.1, SRR1163655.155293.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2152474
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000610935.2/ ENSP00000478557.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..382
                     /product="zinc finger protein 787 isoform 1"
                     /note="transcription termination factor I interacting
                     peptide 20; TTF-I-interacting peptide 20"
                     /calculated_mol_wt=40297
     mat_peptide     1..381
                     /product="Zinc finger protein 787. /id=PRO_0000287606"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DD87.4)"
                     /calculated_mol_wt=40272
     Region          1..65
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DD87.4)"
     Region          <67..200
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          68..88
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(73,75,77,79..80,83..84,87,101,103,107..108,111..112,
                     115,129,131,133,135..136,139..140,143)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          96..116
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6DD87.4)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q6DD87.4)"
     Region          124..144
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6DD87.4)"
     Region          152..172
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          180..200
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          282..302
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          319..339
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          357..382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6DD87.4)"
     CDS             1..382
                     /gene="ZNF787"
                     /gene_synonym="TIP20"
                     /coded_by="NM_001002836.4:135..1283"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42634.1"
                     /db_xref="GeneID:126208"
                     /db_xref="HGNC:HGNC:26998"
                     /db_xref="MIM:621447"
ORIGIN      
        1 melreeawsp gpldsedqqm ashenpvdil imddddvpsw pptklsppqs appagppprp
       61 rppapyicne cgksfshwsk ltrhqrthtg erpnacadcg ktfsqsshlv qhrrihtgek
      121 pyaclecgkr fswssnlmqh qrihtgekpy tcpdcgrsft qskslakhrr shsglkpfvc
      181 prcgrgfsqp kslarhlrlh pelsgpgvaa kvlaasvrra kgpeeavaad geiaipvgdg
      241 egiivvgapg egaaaaaama gagakaagpr srrapapkpy vclecgkgfg hgagllahqr
      301 aqhgdglgaa ggeepahicv ecgegfvqga alrrhkkiha vgapsvcssc gqsyyragge
      361 eeddddeaag grcpecrgge gr
//
LOCUS       NP_062542                219 aa            linear   PRI 16-DEC-2025
DEFINITION  exosomal polycystin-1-interacting protein precursor [Homo sapiens].
ACCESSION   NP_062542
VERSION     NP_062542.5
DBSOURCE    REFSEQ: accession NM_019596.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Lea,W.A., Winklhofer,T., Zelenchuk,L., Sharma,M.,
            Rossol-Allison,J., Fields,T.A., Reif,G., Calvet,J.P.,
            Bakeberg,J.L., Wallace,D.P. and Ward,C.J.
  TITLE     Polycystin-1 Interacting Protein-1 (CU062) Interacts with the
            Ectodomain of Polycystin-1 (PC1)
  JOURNAL   Cells 12 (17), 2166 (2023)
   PUBMED   37681898
  REMARK    GeneRIF: Polycystin-1 Interacting Protein-1 (CU062) Interacts with
            the Ectodomain of Polycystin-1 (PC1).
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Kang,T.W., Kim,H.J., Ju,H., Kim,J.H., Jeon,Y.J., Lee,H.C.,
            Kim,K.K., Kim,J.W., Lee,S., Kim,J.Y., Kim,S.Y. and Kim,Y.S.
  TITLE     Genome-wide association of serum bilirubin levels in Korean
            population
  JOURNAL   Hum Mol Genet 19 (18), 3672-3678 (2010)
   PUBMED   20639394
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Denoeud,F., Kapranov,P., Ucla,C., Frankish,A., Castelo,R.,
            Drenkow,J., Lagarde,J., Alioto,T., Manzano,C., Chrast,J., Dike,S.,
            Wyss,C., Henrichsen,C.N., Holroyd,N., Dickson,M.C., Taylor,R.,
            Hance,Z., Foissac,S., Myers,R.M., Rogers,J., Hubbard,T., Harrow,J.,
            Guigo,R., Gingeras,T.R., Antonarakis,S.E. and Reymond,A.
  TITLE     Prominent use of distal 5' transcription start sites and discovery
            of a large number of additional exons in ENCODE regions
  JOURNAL   Genome Res 17 (6), 746-759 (2007)
   PUBMED   17567994
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Gardiner,K., Slavov,D., Bechtel,L. and Davisson,M.
  TITLE     Annotation of human chromosome 21 for relevance to Down syndrome:
            gene structure and expression analysis
  JOURNAL   Genomics 79 (6), 833-843 (2002)
   PUBMED   12036298
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Slavov,D., Hattori,M., Sakaki,Y., Rosenthal,A., Shimizu,N.,
            Minoshima,S., Kudoh,J., Yaspo,M.L., Ramser,J., Reinhardt,R.,
            Reimer,C., Clancy,K., Rynditch,A. and Gardiner,K.
  TITLE     Criteria for gene identification and features of genome
            organization: analysis of 6.5 Mb of DNA sequence from human
            chromosome 21
  JOURNAL   Gene 247 (1-2), 215-232 (2000)
   PUBMED   10773462
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DQ656042.2, BC069689.1, AP000280.3 and BE466137.1.
            
            On Jul 30, 2009 this sequence version replaced NP_062542.4.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.217744.1,
                                           SRR1660803.167266.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.11"
     Protein         1..219
                     /product="exosomal polycystin-1-interacting protein
                     precursor"
                     /note="uncharacterized protein C21orf62;
                     polycystin-1-interacting protein 1"
                     /calculated_mol_wt=22079
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2790
     Region          2..219
                     /region_name="DUF4571"
                     /note="Domain of unknown function (DUF4571); pfam15137"
                     /db_xref="CDD:464523"
     CDS             1..219
                     /gene="EPCIP"
                     /gene_synonym="B37; C21orf120; C21orf62; CU062; PRED81"
                     /coded_by="NM_019596.6:258..917"
                     /db_xref="CCDS:CCDS42919.2"
                     /db_xref="GeneID:56245"
                     /db_xref="HGNC:HGNC:1305"
                     /db_xref="MIM:621445"
ORIGIN      
        1 mappsrhcll listlgvfal ncftkgqkns tliftrenti rncscsadir dcdyslanlm
       61 cncktvlpla vertsynghl tiwftdtsal ghllnftlvq dlklslcstn tlpteylaic
      121 glkrlrinme akhpfpeqsl lihsggdsds rekpmwlhkg wqpcmyisfl dmalfnrdsa
      181 lksysienvt siannfpdfs yfrtfpmpsn ksyvvtfiy
//
LOCUS       NP_110424                323 aa            linear   PRI 16-DEC-2025
DEFINITION  CYFIP-related Rac1 interactor A [Homo sapiens].
ACCESSION   NP_110424 XP_005262686
VERSION     NP_110424.1
DBSOURCE    REFSEQ: accession NM_030797.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Le,A.H., Yelland,T., Paul,N.R., Fort,L., Nikolaou,S., Ismail,S. and
            Machesky,L.M.
  TITLE     CYRI-A limits invasive migration through macropinosome formation
            and integrin uptake regulation
  JOURNAL   J Cell Biol 220 (9) (2021)
   PUBMED   34165494
  REMARK    GeneRIF: CYRI-A limits invasive migration through macropinosome
            formation and integrin uptake regulation.
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Whitelaw,J.A., Lilla,S., Paul,N.R., Fort,L., Zanivan,S. and
            Machesky,L.M.
  TITLE     CYRI/ Fam49 Proteins Represent a New Class of Rac1 Interactors
  JOURNAL   Commun Integr Biol 12 (1), 112-118 (2019)
   PUBMED   31413787
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Chen,C., Guo,Q., Shi,J., Jiao,X., Lv,K., Liu,X., Jiang,Y., Hui,X.
            and Song,T.
  TITLE     Genetic variants of MGMT, RHPN2, and FAM49A contributed to
            susceptibility of nonsyndromic orofacial clefts in a Chinese
            population
  JOURNAL   J Oral Pathol Med 47 (8), 796-801 (2018)
   PUBMED   29949196
  REMARK    GeneRIF: confirmed that three genes (rs7922405 of MGMT, rs73039426
            of RHPN2, and rs7552 of FAM49A) may contribute to nonsyndromic
            orofacial clefts in Chinese populations
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Leger,P.D., Johnson,D.H., Robbins,G.K., Shafer,R.W., Clifford,D.B.,
            Li,J., McLaren,P.J. and Haas,D.W.
  TITLE     Genome-wide association study of peripheral neuropathy with
            D-drug-containing regimens in AIDS Clinical Trials Group protocol
            384
  JOURNAL   J Neurovirol 20 (3), 304-308 (2014)
   PUBMED   24554482
REFERENCE   8  (residues 1 to 323)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA188616.1, BC038971.1 and AC104623.4.
            
            On Aug 31, 2013 this sequence version replaced XP_005262686.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1660803.209069.1, SRR1803611.248031.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381323.7/ ENSP00000370724.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p24.2"
     Protein         1..323
                     /product="CYFIP-related Rac1 interactor A"
                     /note="protein FAM49A; family with sequence similarity 49
                     member A"
                     /calculated_mol_wt=37182
     Region          17..319
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..323
                     /gene="CYRIA"
                     /gene_synonym="CYRI-A; FAM49A"
                     /coded_by="NM_030797.4:222..1193"
                     /db_xref="CCDS:CCDS1688.1"
                     /db_xref="GeneID:81553"
                     /db_xref="HGNC:HGNC:25373"
                     /db_xref="MIM:621448"
ORIGIN      
        1 mgnllkvltr eienyphffl dfenaqpteg ereiwnqisa vlqdsesila dlqaykgagp
       61 eirdaiqnpn diqlqekawn avcplvvrlk rfyefsirle kalqsllesl tcppytptqh
      121 lereqalake faeilhftlr fdelkmrnpa iqndfsyyrr tisrnrinnm hldienevnn
      181 emanrmslfy aeatpmlktl snatmhfvse nktlpientt dclstmtsvc kvmletpeyr
      241 srftseetlm fcmrvmvgvi ilydhvhpvg afcktskidm kgcikvlkeq apdsveglln
      301 alrfttkhln destskqira mlq
//
LOCUS       NP_689565                272 aa            linear   PRI 17-DEC-2025
DEFINITION  protein FAM210A [Homo sapiens].
ACCESSION   NP_689565
VERSION     NP_689565.2
DBSOURCE    REFSEQ: accession NM_152352.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Wang,Y. and Yue,F.
  TITLE     FAM210A: An emerging regulator of mitochondrial homeostasis
  JOURNAL   Bioessays 46 (10), e2400090 (2024)
   PUBMED   39159484
  REMARK    Review article
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Yu,J., Li,W., Hou,G.J., Sun,D.P., Yang,Y., Yuan,S.X., Dai,Z.H.,
            Yin,H.Z., Sun,S.H., Huang,G., Zhou,W.P. and Yang,F.
  TITLE     Circular RNA cFAM210A, degradable by HBx, inhibits HCC
            tumorigenesis by suppressing YBX1 transactivation
  JOURNAL   Exp Mol Med 55 (11), 2390-2401 (2023)
   PUBMED   37907737
  REMARK    GeneRIF: Circular RNA cFAM210A, degradable by HBx, inhibits HCC
            tumorigenesis by suppressing YBX1 transactivation.
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Tanaka,K.I., Xue,Y., Nguyen-Yamamoto,L., Morris,J.A., Kanazawa,I.,
            Sugimoto,T., Wing,S.S., Richards,J.B. and Goltzman,D.
  TITLE     FAM210A is a novel determinant of bone and muscle structure and
            strength
  JOURNAL   Proc Natl Acad Sci U S A 115 (16), E3759-E3768 (2018)
   PUBMED   29618611
  REMARK    GeneRIF: Genetic variation near FAM210A, a gene of previously
            unknown function, was strongly associated with both appendicular
            and whole body lean mass, as well as bone mineral density.
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Estrada,K., Styrkarsdottir,U., Evangelou,E., Hsu,Y.H., Duncan,E.L.,
            Ntzani,E.E., Oei,L., Albagha,O.M., Amin,N., Kemp,J.P., Koller,D.L.,
            Li,G., Liu,C.T., Minster,R.L., Moayyeri,A., Vandenput,L.,
            Willner,D., Xiao,S.M., Yerges-Armstrong,L.M., Zheng,H.F.,
            Alonso,N., Eriksson,J., Kammerer,C.M., Kaptoge,S.K., Leo,P.J.,
            Thorleifsson,G., Wilson,S.G., Wilson,J.F., Aalto,V., Alen,M.,
            Aragaki,A.K., Aspelund,T., Center,J.R., Dailiana,Z., Duggan,D.J.,
            Garcia,M., Garcia-Giralt,N., Giroux,S., Hallmans,G., Hocking,L.J.,
            Husted,L.B., Jameson,K.A., Khusainova,R., Kim,G.S., Kooperberg,C.,
            Koromila,T., Kruk,M., Laaksonen,M., Lacroix,A.Z., Lee,S.H.,
            Leung,P.C., Lewis,J.R., Masi,L., Mencej-Bedrac,S., Nguyen,T.V.,
            Nogues,X., Patel,M.S., Prezelj,J., Rose,L.M., Scollen,S.,
            Siggeirsdottir,K., Smith,A.V., Svensson,O., Trompet,S., Trummer,O.,
            van Schoor,N.M., Woo,J., Zhu,K., Balcells,S., Brandi,M.L.,
            Buckley,B.M., Cheng,S., Christiansen,C., Cooper,C., Dedoussis,G.,
            Ford,I., Frost,M., Goltzman,D., Gonzalez-Macias,J., Kahonen,M.,
            Karlsson,M., Khusnutdinova,E., Koh,J.M., Kollia,P., Langdahl,B.L.,
            Leslie,W.D., Lips,P., Ljunggren,O., Lorenc,R.S., Marc,J.,
            Mellstrom,D., Obermayer-Pietsch,B., Olmos,J.M.,
            Pettersson-Kymmer,U., Reid,D.M., Riancho,J.A., Ridker,P.M.,
            Rousseau,F., Slagboom,P.E., Tang,N.L., Urreizti,R., Van Hul,W.,
            Viikari,J., Zarrabeitia,M.T., Aulchenko,Y.S.,
            Castano-Betancourt,M., Grundberg,E., Herrera,L., Ingvarsson,T.,
            Johannsdottir,H., Kwan,T., Li,R., Luben,R., Medina-Gomez,C.,
            Palsson,S.T., Reppe,S., Rotter,J.I., Sigurdsson,G., van Meurs,J.B.,
            Verlaan,D., Williams,F.M., Wood,A.R., Zhou,Y., Gautvik,K.M.,
            Pastinen,T., Raychaudhuri,S., Cauley,J.A., Chasman,D.I.,
            Clark,G.R., Cummings,S.R., Danoy,P., Dennison,E.M., Eastell,R.,
            Eisman,J.A., Gudnason,V., Hofman,A., Jackson,R.D., Jones,G.,
            Jukema,J.W., Khaw,K.T., Lehtimaki,T., Liu,Y., Lorentzon,M.,
            McCloskey,E., Mitchell,B.D., Nandakumar,K., Nicholson,G.C.,
            Oostra,B.A., Peacock,M., Pols,H.A., Prince,R.L., Raitakari,O.,
            Reid,I.R., Robbins,J., Sambrook,P.N., Sham,P.C., Shuldiner,A.R.,
            Tylavsky,F.A., van Duijn,C.M., Wareham,N.J., Cupples,L.A.,
            Econs,M.J., Evans,D.M., Harris,T.B., Kung,A.W., Psaty,B.M.,
            Reeve,J., Spector,T.D., Streeten,E.A., Zillikens,M.C.,
            Thorsteinsdottir,U., Ohlsson,C., Karasik,D., Richards,J.B.,
            Brown,M.A., Stefansson,K., Uitterlinden,A.G., Ralston,S.H.,
            Ioannidis,J.P., Kiel,D.P. and Rivadeneira,F.
  TITLE     Genome-wide meta-analysis identifies 56 bone mineral density loci
            and reveals 14 loci associated with risk of fracture
  JOURNAL   Nat Genet 44 (5), 491-501 (2012)
   PUBMED   22504420
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA573992.1, DA895646.1, BU189118.1, AP001010.4 and AA602175.1.
            
            On Oct 19, 2006 this sequence version replaced NP_689565.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.241640.1,
                                           SRR1803615.13708.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000651643.1/
                                                  ENSP00000498370.1
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.21"
     Protein         1..272
                     /product="protein FAM210A"
                     /note="uncharacterized protein C18orf19; family with
                     sequence similarity 210 member A"
                     /calculated_mol_wt=30646
     Region          124..211
                     /region_name="FAM210A-B_dom"
                     /note="FAM210A/B-like domain; pfam06916"
                     /db_xref="CDD:429191"
     Site            136..156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ND0.2)"
     Region          <237..272
                     /region_name="YtxH"
                     /note="YtxH-like protein; pfam12732"
                     /db_xref="CDD:432750"
     Region          246..272
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ND0.2)"
     CDS             1..272
                     /gene="MIMS1"
                     /gene_synonym="C18orf19; FAM210A; HsT2329"
                     /coded_by="NM_152352.4:259..1077"
                     /db_xref="CCDS:CCDS11866.1"
                     /db_xref="GeneID:125228"
                     /db_xref="HGNC:HGNC:28346"
                     /db_xref="MIM:617975"
ORIGIN      
        1 mqwnvprtvs rlarrtclep hnaglfghcq nvkgplllyn aeskvvlvqg pqkqwlhlsa
       61 aqcvakerrp ldahppqpgv lrhkqgkqhv sfrrvfsssa taqgtpekke epdplqdksi
      121 slyqrfkktf rqygkvlipv hlitsgvwfg tfyyaalkgv nvvpflelig lpdsvvsilk
      181 nsqsgnalta yalfkiatpa rytvtlggts vtvkylrshg ymstpppvke ylqdrmeetk
      241 elitekmeet kdrlteklqe tkekvsfkkk ve
//
LOCUS       NP_001092271             272 aa            linear   PRI 17-DEC-2025
DEFINITION  protein FAM210A [Homo sapiens].
ACCESSION   NP_001092271
VERSION     NP_001092271.1
DBSOURCE    REFSEQ: accession NM_001098801.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Wang,Y. and Yue,F.
  TITLE     FAM210A: An emerging regulator of mitochondrial homeostasis
  JOURNAL   Bioessays 46 (10), e2400090 (2024)
   PUBMED   39159484
  REMARK    Review article
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Yu,J., Li,W., Hou,G.J., Sun,D.P., Yang,Y., Yuan,S.X., Dai,Z.H.,
            Yin,H.Z., Sun,S.H., Huang,G., Zhou,W.P. and Yang,F.
  TITLE     Circular RNA cFAM210A, degradable by HBx, inhibits HCC
            tumorigenesis by suppressing YBX1 transactivation
  JOURNAL   Exp Mol Med 55 (11), 2390-2401 (2023)
   PUBMED   37907737
  REMARK    GeneRIF: Circular RNA cFAM210A, degradable by HBx, inhibits HCC
            tumorigenesis by suppressing YBX1 transactivation.
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Tanaka,K.I., Xue,Y., Nguyen-Yamamoto,L., Morris,J.A., Kanazawa,I.,
            Sugimoto,T., Wing,S.S., Richards,J.B. and Goltzman,D.
  TITLE     FAM210A is a novel determinant of bone and muscle structure and
            strength
  JOURNAL   Proc Natl Acad Sci U S A 115 (16), E3759-E3768 (2018)
   PUBMED   29618611
  REMARK    GeneRIF: Genetic variation near FAM210A, a gene of previously
            unknown function, was strongly associated with both appendicular
            and whole body lean mass, as well as bone mineral density.
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Estrada,K., Styrkarsdottir,U., Evangelou,E., Hsu,Y.H., Duncan,E.L.,
            Ntzani,E.E., Oei,L., Albagha,O.M., Amin,N., Kemp,J.P., Koller,D.L.,
            Li,G., Liu,C.T., Minster,R.L., Moayyeri,A., Vandenput,L.,
            Willner,D., Xiao,S.M., Yerges-Armstrong,L.M., Zheng,H.F.,
            Alonso,N., Eriksson,J., Kammerer,C.M., Kaptoge,S.K., Leo,P.J.,
            Thorleifsson,G., Wilson,S.G., Wilson,J.F., Aalto,V., Alen,M.,
            Aragaki,A.K., Aspelund,T., Center,J.R., Dailiana,Z., Duggan,D.J.,
            Garcia,M., Garcia-Giralt,N., Giroux,S., Hallmans,G., Hocking,L.J.,
            Husted,L.B., Jameson,K.A., Khusainova,R., Kim,G.S., Kooperberg,C.,
            Koromila,T., Kruk,M., Laaksonen,M., Lacroix,A.Z., Lee,S.H.,
            Leung,P.C., Lewis,J.R., Masi,L., Mencej-Bedrac,S., Nguyen,T.V.,
            Nogues,X., Patel,M.S., Prezelj,J., Rose,L.M., Scollen,S.,
            Siggeirsdottir,K., Smith,A.V., Svensson,O., Trompet,S., Trummer,O.,
            van Schoor,N.M., Woo,J., Zhu,K., Balcells,S., Brandi,M.L.,
            Buckley,B.M., Cheng,S., Christiansen,C., Cooper,C., Dedoussis,G.,
            Ford,I., Frost,M., Goltzman,D., Gonzalez-Macias,J., Kahonen,M.,
            Karlsson,M., Khusnutdinova,E., Koh,J.M., Kollia,P., Langdahl,B.L.,
            Leslie,W.D., Lips,P., Ljunggren,O., Lorenc,R.S., Marc,J.,
            Mellstrom,D., Obermayer-Pietsch,B., Olmos,J.M.,
            Pettersson-Kymmer,U., Reid,D.M., Riancho,J.A., Ridker,P.M.,
            Rousseau,F., Slagboom,P.E., Tang,N.L., Urreizti,R., Van Hul,W.,
            Viikari,J., Zarrabeitia,M.T., Aulchenko,Y.S.,
            Castano-Betancourt,M., Grundberg,E., Herrera,L., Ingvarsson,T.,
            Johannsdottir,H., Kwan,T., Li,R., Luben,R., Medina-Gomez,C.,
            Palsson,S.T., Reppe,S., Rotter,J.I., Sigurdsson,G., van Meurs,J.B.,
            Verlaan,D., Williams,F.M., Wood,A.R., Zhou,Y., Gautvik,K.M.,
            Pastinen,T., Raychaudhuri,S., Cauley,J.A., Chasman,D.I.,
            Clark,G.R., Cummings,S.R., Danoy,P., Dennison,E.M., Eastell,R.,
            Eisman,J.A., Gudnason,V., Hofman,A., Jackson,R.D., Jones,G.,
            Jukema,J.W., Khaw,K.T., Lehtimaki,T., Liu,Y., Lorentzon,M.,
            McCloskey,E., Mitchell,B.D., Nandakumar,K., Nicholson,G.C.,
            Oostra,B.A., Peacock,M., Pols,H.A., Prince,R.L., Raitakari,O.,
            Reid,I.R., Robbins,J., Sambrook,P.N., Sham,P.C., Shuldiner,A.R.,
            Tylavsky,F.A., van Duijn,C.M., Wareham,N.J., Cupples,L.A.,
            Econs,M.J., Evans,D.M., Harris,T.B., Kung,A.W., Psaty,B.M.,
            Reeve,J., Spector,T.D., Streeten,E.A., Zillikens,M.C.,
            Thorsteinsdottir,U., Ohlsson,C., Karasik,D., Richards,J.B.,
            Brown,M.A., Stefansson,K., Uitterlinden,A.G., Ralston,S.H.,
            Ioannidis,J.P., Kiel,D.P. and Rivadeneira,F.
  TITLE     Genome-wide meta-analysis identifies 56 bone mineral density loci
            and reveals 14 loci associated with risk of fracture
  JOURNAL   Nat Genet 44 (5), 491-501 (2012)
   PUBMED   22504420
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA573992.1, DA560663.1, BU189118.1, AP001010.4 and AA602175.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.151885.1,
                                           SRR1163658.343525.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.21"
     Protein         1..272
                     /product="protein FAM210A"
                     /note="uncharacterized protein C18orf19; family with
                     sequence similarity 210 member A"
                     /calculated_mol_wt=30646
     Region          124..211
                     /region_name="FAM210A-B_dom"
                     /note="FAM210A/B-like domain; pfam06916"
                     /db_xref="CDD:429191"
     Site            136..156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ND0.2)"
     Region          <237..272
                     /region_name="YtxH"
                     /note="YtxH-like protein; pfam12732"
                     /db_xref="CDD:432750"
     Region          246..272
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ND0.2)"
     CDS             1..272
                     /gene="MIMS1"
                     /gene_synonym="C18orf19; FAM210A; HsT2329"
                     /coded_by="NM_001098801.2:399..1217"
                     /db_xref="CCDS:CCDS11866.1"
                     /db_xref="GeneID:125228"
                     /db_xref="HGNC:HGNC:28346"
                     /db_xref="MIM:617975"
ORIGIN      
        1 mqwnvprtvs rlarrtclep hnaglfghcq nvkgplllyn aeskvvlvqg pqkqwlhlsa
       61 aqcvakerrp ldahppqpgv lrhkqgkqhv sfrrvfsssa taqgtpekke epdplqdksi
      121 slyqrfkktf rqygkvlipv hlitsgvwfg tfyyaalkgv nvvpflelig lpdsvvsilk
      181 nsqsgnalta yalfkiatpa rytvtlggts vtvkylrshg ymstpppvke ylqdrmeetk
      241 elitekmeet kdrlteklqe tkekvsfkkk ve
//
LOCUS       NP_543011                192 aa            linear   PRI 17-DEC-2025
DEFINITION  protein FAM210B, mitochondrial [Homo sapiens].
ACCESSION   NP_543011
VERSION     NP_543011.2
DBSOURCE    REFSEQ: accession NM_080821.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Pan,X., Xu,J. and Zhou,Y.
  TITLE     Multifaceted role of FAM210B in hepatocellular carcinoma:
            Implications for tumour progression, microenvironment modulation
            and therapeutic selection
  JOURNAL   J Cell Mol Med 28 (16), e70031 (2024)
   PUBMED   39198940
  REMARK    GeneRIF: Multifaceted role of FAM210B in hepatocellular carcinoma:
            Implications for tumour progression, microenvironment modulation
            and therapeutic selection.
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Xu,Y., Gao,R., Zhang,M., Zeng,Q., Zhou,S., Zhu,G., Su,W. and
            Wang,R.
  TITLE     Mendelian randomization study on causal association of FAM210B with
            drug-induced lupus
  JOURNAL   Clin Rheumatol 43 (5), 1513-1520 (2024)
   PUBMED   38436771
  REMARK    GeneRIF: Mendelian randomization study on causal association of
            FAM210B with drug-induced lupus.
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Suzuki,C., Fujiwara,T., Shima,H., Ono,K., Saito,K., Kato,H.,
            Onodera,K., Ichikawa,S., Fukuhara,N., Onishi,Y., Yokoyama,H.,
            Nakamura,Y., Igarashi,K. and Harigae,H.
  TITLE     Elucidation of the Role of FAM210B in Mitochondrial Metabolism and
            Erythropoiesis
  JOURNAL   Mol Cell Biol 42 (12), e0014322 (2022)
   PUBMED   36374104
  REMARK    GeneRIF: Elucidation of the Role of FAM210B in Mitochondrial
            Metabolism and Erythropoiesis.
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 192)
  AUTHORS   Sun,S., Liu,J., Zhao,M., Han,Y., Chen,P., Mo,Q., Wang,B., Chen,G.,
            Fang,Y., Tian,Y., Zhou,J., Ma,D., Gao,Q. and Wu,P.
  TITLE     Loss of the novel mitochondrial protein FAM210B promotes metastasis
            via PDK4-dependent metabolic reprogramming
  JOURNAL   Cell Death Dis 8 (6), e2870 (2017)
   PUBMED   28594398
  REMARK    GeneRIF: it was found that low expression of FAM210B was
            significantly correlated with decreased survival and enhanced
            metastasis in vivo and in vitro, and the loss of FAM210B led to an
            increased mitochondrial respiratory capacity and reduced glycolysis
            through the downregulation of pyruvate dehydrogenase kinase 4
            (PDK4).
            Erratum:[Cell Death Dis. 2019 Sep 23;10(10):707. doi:
            10.1038/s41419-019-1945-y. PMID: 31548594]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 192)
  AUTHORS   Kondo,A., Fujiwara,T., Okitsu,Y., Fukuhara,N., Onishi,Y.,
            Nakamura,Y., Sawada,K. and Harigae,H.
  TITLE     Identification of a novel putative mitochondrial protein FAM210B
            associated with erythroid differentiation
  JOURNAL   Int J Hematol 103 (4), 387-395 (2016)
   PUBMED   26968549
  REMARK    GeneRIF: Both human and murine FAM210B are abundantly expressed in
            the later stages of erythroblast development. Moreover, the deduced
            amino acid sequence predicted that FAM210B is a membrane protein,
            and Western blot analysis demonstrated its mitochondrial
            localization. Loss-of-function analysis in erythroid cells
            suggested that FAM210B may be involved in erythroid
            differentiation.
REFERENCE   8  (residues 1 to 192)
  AUTHORS   Palmieri,R.T., Wilson,M.A., Iversen,E.S., Clyde,M.A.,
            Calingaert,B., Moorman,P.G., Poole,C., Anderson,A.R., Anderson,S.,
            Anton-Culver,H., Beesley,J., Hogdall,E., Brewster,W., Carney,M.E.,
            Chen,X., Chenevix-Trench,G., Chang-Claude,J., Cunningham,J.M.,
            Dicioccio,R.A., Doherty,J.A., Easton,D.F., Edlund,C.K.,
            Gayther,S.A., Gentry-Maharaj,A., Goode,E.L., Goodman,M.T.,
            Kjaer,S.K., Hogdall,C.K., Hopkins,M.P., Jenison,E.L., Blaakaer,J.,
            Lurie,G., McGuire,V., Menon,U., Moysich,K.B., Ness,R.B.,
            Pearce,C.L., Pharoah,P.D., Pike,M.C., Ramus,S.J., Rossing,M.A.,
            Song,H., Terada,K.Y., Vandenberg,D., Vierkant,R.A., Wang-Gohrke,S.,
            Webb,P.M., Whittemore,A.S., Wu,A.H., Ziogas,A., Berchuck,A. and
            Schildkraut,J.M.
  CONSRTM   Ovarian Cancer Association Consortium; Australian Cancer Study
            (Ovarian Cancer Group); Australian Ovarian Cancer Study Group
  TITLE     Polymorphism in the IL18 gene and epithelial ovarian cancer in
            non-Hispanic white women
  JOURNAL   Cancer Epidemiol Biomarkers Prev 17 (12), 3567-3572 (2008)
   PUBMED   19064572
  REMARK    GeneRIF: Observational study and meta-analysis of gene-disease
            association. (HuGE Navigator)
REFERENCE   9  (residues 1 to 192)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   10 (residues 1 to 192)
  AUTHORS   Ranes-Goldberg,M.G., Hori,T., Mohan-Peterson,S. and Spits,H.
  TITLE     Identification of human pre-T/NK cell-associated genes
  JOURNAL   J Immunol 151 (10), 5810-5821 (1993)
   PUBMED   8228263
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB500825.1, AK075565.1 and AL133555.1.
            
            On Apr 25, 2006 this sequence version replaced NP_543011.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ311123.1, BC017725.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000371384.4/
                                                  ENSP00000360437.3
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.2"
     Protein         1..192
                     /product="protein FAM210B, mitochondrial"
                     /note="transmembrane protein C20orf108; family with
                     sequence similarity 210 member B"
                     /calculated_mol_wt=14476
     transit_peptide 1..58
                     /note="Mitochondrion. /evidence=ECO:0000255,
                     ECO:0000269|PubMed:28594398; propagated from
                     UniProtKB/Swiss-Prot (Q96KR6.2)"
                     /calculated_mol_wt=5966
     Region          57..80
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KR6.2)"
     mat_peptide     59..192
                     /product="Protein FAM210B, mitochondrial.
                     /id=PRO_0000079451"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KR6.2)"
                     /calculated_mol_wt=14476
     Region          87..174
                     /region_name="FAM210A-B_dom"
                     /note="FAM210A/B-like domain; pfam06916"
                     /db_xref="CDD:429191"
     Site            99..119
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KR6.2)"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KR6.2)"
     CDS             1..192
                     /gene="MIMS2"
                     /gene_synonym="5A3; C20orf108; dJ1167H4.1; FAM210B"
                     /coded_by="NM_080821.3:33..611"
                     /db_xref="CCDS:CCDS13450.1"
                     /db_xref="GeneID:116151"
                     /db_xref="HGNC:HGNC:16102"
                     /db_xref="MIM:618722"
ORIGIN      
        1 magllallgp agrvgarvrp ratwllgata pcappplala llpprldarl lrtargdcrg
       61 hqdpsqatgt tgssvsctee kkqsksqqlk kifqeygtvg vslhigisli slgifymvvs
      121 sgvdmpaill klgfkeslvq skmaagtstf vvayaihklf apvrisitlv svplivryfr
      181 kvgffkppaa kp
//
LOCUS       NP_001275562             562 aa            linear   PRI 17-DEC-2025
DEFINITION  protein FAM222B isoform 2 [Homo sapiens].
ACCESSION   NP_001275562
VERSION     NP_001275562.1
DBSOURCE    REFSEQ: accession NM_001288633.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Calvario,E., Segovia,L. and Zurita,M.
  TITLE     Evolutionary analysis through structural modeling of FAM222
            proteins reveals a novel disordered conserved domain in vertebrates
            that interacts with NLK
  JOURNAL   Sci Rep 15 (1), 43372 (2025)
   PUBMED   41365991
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Spiegler,S., Kirchmaier,B., Rath,M., Korenke,G.C., Tetzlaff,F., van
            de Vorst,M., Neveling,K., Acker-Palmer,A., Kuss,A.W., Gilissen,C.,
            Fischer,A., Schulte-Merker,S. and Felbor,U.
  TITLE     FAM222B Is Not a Likely Novel Candidate Gene for Cerebral Cavernous
            Malformations
  JOURNAL   Mol Syndromol 7 (3), 144-152 (2016)
   PUBMED   27587990
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY012898.1, BC021228.2 and AC010761.10.
            
            Transcript Variant: This variant (5) differs in the 5' UTR, lacks
            an exon in the 5' coding region and initiates translation at an
            alternate start codon, compared to variant 3. Variants 1, 2, 4, 5,
            6, and 7 encode the same isoform (2), which is shorter and has a
            distinct N-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HY012898.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968968,
                                           SAMEA2150385 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..562
                     /product="protein FAM222B isoform 2"
                     /note="uncharacterized protein C17orf63; protein FAM222B"
                     /calculated_mol_wt=59521
     Region          27..562
                     /region_name="FAM222A"
                     /note="Protein family of FAM222A; pfam15258"
                     /db_xref="CDD:464598"
     Region          155..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     Region          219..245
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     Region          537..562
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     CDS             1..562
                     /gene="FAM222B"
                     /gene_synonym="C17orf63"
                     /coded_by="NM_001288633.2:226..1914"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS45637.1"
                     /db_xref="GeneID:55731"
                     /db_xref="HGNC:HGNC:25563"
ORIGIN      
        1 mlaclpgpgd lsfqllshtq mntglqkwdt tqkmrtahyp tpaeldayak kvannpltik
       61 ifpnsvkvpq rkhvrrtvng ldtsaqrysp yptqaatkag llaivkvpak silkdfdgtr
      121 arllpeaimn ppvapyatva pstlahpqaq alarqqalqh aqtlahappq tlqhpqgipp
      181 pqalshpqsl qqpqglghpq pmaqtqglvh pqalahqglq hphnpllhgg rkmpdsdapp
      241 nvtvststip lsmaatlqhs qppdlssivh qinqfcqtra gisttsvceg qianpspisr
      301 sllinastrv sthsvptpmp scvvnpmeht haataalpaa gpvnlptgis rvptgypsdl
      361 kpvtwnqhql ahlqqmcsea sgtpapgltg khaagrelag pgfvgkapay pqelclaqsf
      421 hlkpplekpt psppvngmaa playpnghyf qplwnnilpt pnsdssgsqd lampfhggqp
      481 tgapldcaaa pgahyragtg ggpvasqnsl mqtvdylsgd fqqacfreqs lamlskahra
      541 pgnrapdpte srslhiqhpg yr
//
LOCUS       NP_001275560             564 aa            linear   PRI 17-DEC-2025
DEFINITION  protein FAM222B isoform 1 [Homo sapiens].
ACCESSION   NP_001275560
VERSION     NP_001275560.1
DBSOURCE    REFSEQ: accession NM_001288631.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Calvario,E., Segovia,L. and Zurita,M.
  TITLE     Evolutionary analysis through structural modeling of FAM222
            proteins reveals a novel disordered conserved domain in vertebrates
            that interacts with NLK
  JOURNAL   Sci Rep 15 (1), 43372 (2025)
   PUBMED   41365991
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Spiegler,S., Kirchmaier,B., Rath,M., Korenke,G.C., Tetzlaff,F., van
            de Vorst,M., Neveling,K., Acker-Palmer,A., Kuss,A.W., Gilissen,C.,
            Fischer,A., Schulte-Merker,S. and Felbor,U.
  TITLE     FAM222B Is Not a Likely Novel Candidate Gene for Cerebral Cavernous
            Malformations
  JOURNAL   Mol Syndromol 7 (3), 144-152 (2016)
   PUBMED   27587990
REFERENCE   5  (residues 1 to 564)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA789853.1, BC021228.2 and AC010761.10.
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA789853.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..564
                     /product="protein FAM222B isoform 1"
                     /note="uncharacterized protein C17orf63; protein FAM222B"
                     /calculated_mol_wt=59750
     Region          31..564
                     /region_name="FAM222A"
                     /note="Protein family of FAM222A; pfam15258"
                     /db_xref="CDD:464598"
     CDS             1..564
                     /gene="FAM222B"
                     /gene_synonym="C17orf63"
                     /coded_by="NM_001288631.2:315..2009"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:55731"
                     /db_xref="HGNC:HGNC:25563"
ORIGIN      
        1 mrssfplasa kknlrvgtnl eqrdssthqg dttqkmrtah yptpaelday akkvannplt
       61 ikifpnsvkv pqrkhvrrtv ngldtsaqry spyptqaatk agllaivkvp aksilkdfdg
      121 trarllpeai mnppvapyat vapstlahpq aqalarqqal qhaqtlahap pqtlqhpqgi
      181 pppqalshpq slqqpqglgh pqpmaqtqgl vhpqalahqg lqhphnpllh ggrkmpdsda
      241 ppnvtvstst iplsmaatlq hsqppdlssi vhqinqfcqt ragisttsvc egqianpspi
      301 srsllinast rvsthsvptp mpscvvnpme hthaataalp aagpvnlptg isrvptgyps
      361 dlkpvtwnqh qlahlqqmcs easgtpapgl tgkhaagrel agpgfvgkap aypqelclaq
      421 sfhlkpplek ptpsppvngm aaplaypngh yfqplwnnil ptpnsdssgs qdlampfhgg
      481 qptgapldca aapgahyrag tgggpvasqn slmqtvdyls gdfqqacfre qslamlskah
      541 rapgnrapdp tesrslhiqh pgyr
//
LOCUS       NP_001275561             562 aa            linear   PRI 17-DEC-2025
DEFINITION  protein FAM222B isoform 2 [Homo sapiens].
ACCESSION   NP_001275561
VERSION     NP_001275561.1
DBSOURCE    REFSEQ: accession NM_001288632.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Calvario,E., Segovia,L. and Zurita,M.
  TITLE     Evolutionary analysis through structural modeling of FAM222
            proteins reveals a novel disordered conserved domain in vertebrates
            that interacts with NLK
  JOURNAL   Sci Rep 15 (1), 43372 (2025)
   PUBMED   41365991
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Spiegler,S., Kirchmaier,B., Rath,M., Korenke,G.C., Tetzlaff,F., van
            de Vorst,M., Neveling,K., Acker-Palmer,A., Kuss,A.W., Gilissen,C.,
            Fischer,A., Schulte-Merker,S. and Felbor,U.
  TITLE     FAM222B Is Not a Likely Novel Candidate Gene for Cerebral Cavernous
            Malformations
  JOURNAL   Mol Syndromol 7 (3), 144-152 (2016)
   PUBMED   27587990
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY040104.1, DB453514.1, BC021228.2 and AC010761.10.
            
            Transcript Variant: This variant (4) differs in the 5' UTR, lacks
            an exon in the 5' coding region and initiates translation at an
            alternate start codon, compared to variant 3. Variants 1, 2, 4, 5,
            6, and 7 encode the same isoform (2), which is shorter and has a
            distinct N-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.17099.1,
                                           SRR1660803.310222.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..562
                     /product="protein FAM222B isoform 2"
                     /note="uncharacterized protein C17orf63; protein FAM222B"
                     /calculated_mol_wt=59521
     Region          27..562
                     /region_name="FAM222A"
                     /note="Protein family of FAM222A; pfam15258"
                     /db_xref="CDD:464598"
     Region          155..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     Region          219..245
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     Region          537..562
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     CDS             1..562
                     /gene="FAM222B"
                     /gene_synonym="C17orf63"
                     /coded_by="NM_001288632.2:232..1920"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS45637.1"
                     /db_xref="GeneID:55731"
                     /db_xref="HGNC:HGNC:25563"
ORIGIN      
        1 mlaclpgpgd lsfqllshtq mntglqkwdt tqkmrtahyp tpaeldayak kvannpltik
       61 ifpnsvkvpq rkhvrrtvng ldtsaqrysp yptqaatkag llaivkvpak silkdfdgtr
      121 arllpeaimn ppvapyatva pstlahpqaq alarqqalqh aqtlahappq tlqhpqgipp
      181 pqalshpqsl qqpqglghpq pmaqtqglvh pqalahqglq hphnpllhgg rkmpdsdapp
      241 nvtvststip lsmaatlqhs qppdlssivh qinqfcqtra gisttsvceg qianpspisr
      301 sllinastrv sthsvptpmp scvvnpmeht haataalpaa gpvnlptgis rvptgypsdl
      361 kpvtwnqhql ahlqqmcsea sgtpapgltg khaagrelag pgfvgkapay pqelclaqsf
      421 hlkpplekpt psppvngmaa playpnghyf qplwnnilpt pnsdssgsqd lampfhggqp
      481 tgapldcaaa pgahyragtg ggpvasqnsl mqtvdylsgd fqqacfreqs lamlskahra
      541 pgnrapdpte srslhiqhpg yr
//
LOCUS       NP_001275566             434 aa            linear   PRI 17-DEC-2025
DEFINITION  protein FAM222B isoform 3 [Homo sapiens].
ACCESSION   NP_001275566
VERSION     NP_001275566.1
DBSOURCE    REFSEQ: accession NM_001288637.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Calvario,E., Segovia,L. and Zurita,M.
  TITLE     Evolutionary analysis through structural modeling of FAM222
            proteins reveals a novel disordered conserved domain in vertebrates
            that interacts with NLK
  JOURNAL   Sci Rep 15 (1), 43372 (2025)
   PUBMED   41365991
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Spiegler,S., Kirchmaier,B., Rath,M., Korenke,G.C., Tetzlaff,F., van
            de Vorst,M., Neveling,K., Acker-Palmer,A., Kuss,A.W., Gilissen,C.,
            Fischer,A., Schulte-Merker,S. and Felbor,U.
  TITLE     FAM222B Is Not a Likely Novel Candidate Gene for Cerebral Cavernous
            Malformations
  JOURNAL   Mol Syndromol 7 (3), 144-152 (2016)
   PUBMED   27587990
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA887444.1, BC021228.2 and AC010761.10.
            
            Transcript Variant: This variant (9) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream start codon, compared to variant 3. Variants 8 through
            12 encode the same isoform (3), which is shorter at the N-terminus,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038194.1573719.1, SRR6380200.15723.17
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1968968,
                                    SAMEA2142348 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..434
                     /product="protein FAM222B isoform 3"
                     /note="uncharacterized protein C17orf63; protein FAM222B"
                     /calculated_mol_wt=45427
     Region          1..434
                     /region_name="FAM222A"
                     /note="Protein family of FAM222A; pfam15258"
                     /db_xref="CDD:464598"
     CDS             1..434
                     /gene="FAM222B"
                     /gene_synonym="C17orf63"
                     /coded_by="NM_001288637.2:572..1876"
                     /note="isoform 3 is encoded by transcript variant 9"
                     /db_xref="GeneID:55731"
                     /db_xref="HGNC:HGNC:25563"
ORIGIN      
        1 mnppvapyat vapstlahpq aqalarqqal qhaqtlahap pqtlqhpqgi pppqalshpq
       61 slqqpqglgh pqpmaqtqgl vhpqalahqg lqhphnpllh ggrkmpdsda ppnvtvstst
      121 iplsmaatlq hsqppdlssi vhqinqfcqt ragisttsvc egqianpspi srsllinast
      181 rvsthsvptp mpscvvnpme hthaataalp aagpvnlptg isrvptgyps dlkpvtwnqh
      241 qlahlqqmcs easgtpapgl tgkhaagrel agpgfvgkap aypqelclaq sfhlkpplek
      301 ptpsppvngm aaplaypngh yfqplwnnil ptpnsdssgs qdlampfhgg qptgapldca
      361 aapgahyrag tgggpvasqn slmqtvdyls gdfqqacfre qslamlskah rapgnrapdp
      421 tesrslhiqh pgyr
//
LOCUS       NP_001275563             562 aa            linear   PRI 17-DEC-2025
DEFINITION  protein FAM222B isoform 2 [Homo sapiens].
ACCESSION   NP_001275563 XP_005258059
VERSION     NP_001275563.1
DBSOURCE    REFSEQ: accession NM_001288634.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Calvario,E., Segovia,L. and Zurita,M.
  TITLE     Evolutionary analysis through structural modeling of FAM222
            proteins reveals a novel disordered conserved domain in vertebrates
            that interacts with NLK
  JOURNAL   Sci Rep 15 (1), 43372 (2025)
   PUBMED   41365991
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Spiegler,S., Kirchmaier,B., Rath,M., Korenke,G.C., Tetzlaff,F., van
            de Vorst,M., Neveling,K., Acker-Palmer,A., Kuss,A.W., Gilissen,C.,
            Fischer,A., Schulte-Merker,S. and Felbor,U.
  TITLE     FAM222B Is Not a Likely Novel Candidate Gene for Cerebral Cavernous
            Malformations
  JOURNAL   Mol Syndromol 7 (3), 144-152 (2016)
   PUBMED   27587990
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC010761.10, AK095569.1 and BC021228.2.
            
            On Dec 25, 2013 this sequence version replaced XP_005258059.1.
            
            Transcript Variant: This variant (6) includes an alternate 5'
            terminal exon, lacks an exon in the 5' coding region and initiates
            translation at an alternate start codon, compared to variant 3.
            Variants 1, 2, 4, 5, 6, and 7 encode the same isoform (2), which is
            shorter and has a distinct N-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.170735.1, AK095569.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..562
                     /product="protein FAM222B isoform 2"
                     /note="uncharacterized protein C17orf63; protein FAM222B"
                     /calculated_mol_wt=59521
     Region          27..562
                     /region_name="FAM222A"
                     /note="Protein family of FAM222A; pfam15258"
                     /db_xref="CDD:464598"
     Region          155..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     Region          219..245
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     Region          537..562
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     CDS             1..562
                     /gene="FAM222B"
                     /gene_synonym="C17orf63"
                     /coded_by="NM_001288634.2:304..1992"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS45637.1"
                     /db_xref="GeneID:55731"
                     /db_xref="HGNC:HGNC:25563"
ORIGIN      
        1 mlaclpgpgd lsfqllshtq mntglqkwdt tqkmrtahyp tpaeldayak kvannpltik
       61 ifpnsvkvpq rkhvrrtvng ldtsaqrysp yptqaatkag llaivkvpak silkdfdgtr
      121 arllpeaimn ppvapyatva pstlahpqaq alarqqalqh aqtlahappq tlqhpqgipp
      181 pqalshpqsl qqpqglghpq pmaqtqglvh pqalahqglq hphnpllhgg rkmpdsdapp
      241 nvtvststip lsmaatlqhs qppdlssivh qinqfcqtra gisttsvceg qianpspisr
      301 sllinastrv sthsvptpmp scvvnpmeht haataalpaa gpvnlptgis rvptgypsdl
      361 kpvtwnqhql ahlqqmcsea sgtpapgltg khaagrelag pgfvgkapay pqelclaqsf
      421 hlkpplekpt psppvngmaa playpnghyf qplwnnilpt pnsdssgsqd lampfhggqp
      481 tgapldcaaa pgahyragtg ggpvasqnsl mqtvdylsgd fqqacfreqs lamlskahra
      541 pgnrapdpte srslhiqhpg yr
//
LOCUS       NP_001275569             434 aa            linear   PRI 17-DEC-2025
DEFINITION  protein FAM222B isoform 3 [Homo sapiens].
ACCESSION   NP_001275569 XP_005258060
VERSION     NP_001275569.1
DBSOURCE    REFSEQ: accession NM_001288640.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Calvario,E., Segovia,L. and Zurita,M.
  TITLE     Evolutionary analysis through structural modeling of FAM222
            proteins reveals a novel disordered conserved domain in vertebrates
            that interacts with NLK
  JOURNAL   Sci Rep 15 (1), 43372 (2025)
   PUBMED   41365991
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Spiegler,S., Kirchmaier,B., Rath,M., Korenke,G.C., Tetzlaff,F., van
            de Vorst,M., Neveling,K., Acker-Palmer,A., Kuss,A.W., Gilissen,C.,
            Fischer,A., Schulte-Merker,S. and Felbor,U.
  TITLE     FAM222B Is Not a Likely Novel Candidate Gene for Cerebral Cavernous
            Malformations
  JOURNAL   Mol Syndromol 7 (3), 144-152 (2016)
   PUBMED   27587990
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY040104.1, AK299477.1, BC021228.2 and AC010761.10.
            
            On Dec 25, 2013 this sequence version replaced XP_005258060.1.
            
            Transcript Variant: This variant (12) differs in the 5' UTR, lacks
            a portion of the 5' coding region and initiates translation at a
            downstream start codon, compared to variant 3. Variants 8 through
            12 encode the same isoform (3), which is shorter at the N-terminus,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.153829.1, BX647766.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162568, SAMN03267771
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..434
                     /product="protein FAM222B isoform 3"
                     /note="uncharacterized protein C17orf63; protein FAM222B"
                     /calculated_mol_wt=45427
     Region          1..434
                     /region_name="FAM222A"
                     /note="Protein family of FAM222A; pfam15258"
                     /db_xref="CDD:464598"
     CDS             1..434
                     /gene="FAM222B"
                     /gene_synonym="C17orf63"
                     /coded_by="NM_001288640.2:422..1726"
                     /note="isoform 3 is encoded by transcript variant 12"
                     /db_xref="GeneID:55731"
                     /db_xref="HGNC:HGNC:25563"
ORIGIN      
        1 mnppvapyat vapstlahpq aqalarqqal qhaqtlahap pqtlqhpqgi pppqalshpq
       61 slqqpqglgh pqpmaqtqgl vhpqalahqg lqhphnpllh ggrkmpdsda ppnvtvstst
      121 iplsmaatlq hsqppdlssi vhqinqfcqt ragisttsvc egqianpspi srsllinast
      181 rvsthsvptp mpscvvnpme hthaataalp aagpvnlptg isrvptgyps dlkpvtwnqh
      241 qlahlqqmcs easgtpapgl tgkhaagrel agpgfvgkap aypqelclaq sfhlkpplek
      301 ptpsppvngm aaplaypngh yfqplwnnil ptpnsdssgs qdlampfhgg qptgapldca
      361 aapgahyrag tgggpvasqn slmqtvdyls gdfqqacfre qslamlskah rapgnrapdp
      421 tesrslhiqh pgyr
//
LOCUS       NP_001275568             434 aa            linear   PRI 17-DEC-2025
DEFINITION  protein FAM222B isoform 3 [Homo sapiens].
ACCESSION   NP_001275568 XP_005258063
VERSION     NP_001275568.1
DBSOURCE    REFSEQ: accession NM_001288639.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Calvario,E., Segovia,L. and Zurita,M.
  TITLE     Evolutionary analysis through structural modeling of FAM222
            proteins reveals a novel disordered conserved domain in vertebrates
            that interacts with NLK
  JOURNAL   Sci Rep 15 (1), 43372 (2025)
   PUBMED   41365991
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Spiegler,S., Kirchmaier,B., Rath,M., Korenke,G.C., Tetzlaff,F., van
            de Vorst,M., Neveling,K., Acker-Palmer,A., Kuss,A.W., Gilissen,C.,
            Fischer,A., Schulte-Merker,S. and Felbor,U.
  TITLE     FAM222B Is Not a Likely Novel Candidate Gene for Cerebral Cavernous
            Malformations
  JOURNAL   Mol Syndromol 7 (3), 144-152 (2016)
   PUBMED   27587990
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY040104.1, DC376581.1, BC021228.2 and AC010761.10.
            
            On Dec 25, 2013 this sequence version replaced XP_005258063.1.
            
            Transcript Variant: This variant (11) differs in the 5' UTR, lacks
            a portion of the 5' coding region and initiates translation at a
            downstream start codon, compared to variant 3. Variants 8 through
            12 encode the same isoform (3), which is shorter at the N-terminus,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.130993.1,
                                           SRR7346977.945006.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162568, SAMN03267771
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..434
                     /product="protein FAM222B isoform 3"
                     /note="uncharacterized protein C17orf63; protein FAM222B"
                     /calculated_mol_wt=45427
     Region          1..434
                     /region_name="FAM222A"
                     /note="Protein family of FAM222A; pfam15258"
                     /db_xref="CDD:464598"
     CDS             1..434
                     /gene="FAM222B"
                     /gene_synonym="C17orf63"
                     /coded_by="NM_001288639.2:456..1760"
                     /note="isoform 3 is encoded by transcript variant 11"
                     /db_xref="GeneID:55731"
                     /db_xref="HGNC:HGNC:25563"
ORIGIN      
        1 mnppvapyat vapstlahpq aqalarqqal qhaqtlahap pqtlqhpqgi pppqalshpq
       61 slqqpqglgh pqpmaqtqgl vhpqalahqg lqhphnpllh ggrkmpdsda ppnvtvstst
      121 iplsmaatlq hsqppdlssi vhqinqfcqt ragisttsvc egqianpspi srsllinast
      181 rvsthsvptp mpscvvnpme hthaataalp aagpvnlptg isrvptgyps dlkpvtwnqh
      241 qlahlqqmcs easgtpapgl tgkhaagrel agpgfvgkap aypqelclaq sfhlkpplek
      301 ptpsppvngm aaplaypngh yfqplwnnil ptpnsdssgs qdlampfhgg qptgapldca
      361 aapgahyrag tgggpvasqn slmqtvdyls gdfqqacfre qslamlskah rapgnrapdp
      421 tesrslhiqh pgyr
//
LOCUS       NP_060652                562 aa            linear   PRI 17-DEC-2025
DEFINITION  protein FAM222B isoform 2 [Homo sapiens].
ACCESSION   NP_060652
VERSION     NP_060652.2
DBSOURCE    REFSEQ: accession NM_018182.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Calvario,E., Segovia,L. and Zurita,M.
  TITLE     Evolutionary analysis through structural modeling of FAM222
            proteins reveals a novel disordered conserved domain in vertebrates
            that interacts with NLK
  JOURNAL   Sci Rep 15 (1), 43372 (2025)
   PUBMED   41365991
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Spiegler,S., Kirchmaier,B., Rath,M., Korenke,G.C., Tetzlaff,F., van
            de Vorst,M., Neveling,K., Acker-Palmer,A., Kuss,A.W., Gilissen,C.,
            Fischer,A., Schulte-Merker,S. and Felbor,U.
  TITLE     FAM222B Is Not a Likely Novel Candidate Gene for Cerebral Cavernous
            Malformations
  JOURNAL   Mol Syndromol 7 (3), 144-152 (2016)
   PUBMED   27587990
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY040104.1, DC374179.1, BC021228.2 and AC010761.10.
            
            On Nov 1, 2006 this sequence version replaced NP_060652.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks
            an exon in the 5' coding region and initiates translation at an
            alternate start codon, compared to variant 3. Variants 1, 2, 4, 5,
            6, and 7 encode the same isoform (2), which is shorter and has a
            distinct N-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001562.1, SRR1660805.247721.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..562
                     /product="protein FAM222B isoform 2"
                     /note="uncharacterized protein C17orf63; protein FAM222B"
                     /calculated_mol_wt=59521
     Region          27..562
                     /region_name="FAM222A"
                     /note="Protein family of FAM222A; pfam15258"
                     /db_xref="CDD:464598"
     Region          155..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     Region          219..245
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     Region          537..562
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     CDS             1..562
                     /gene="FAM222B"
                     /gene_synonym="C17orf63"
                     /coded_by="NM_018182.4:184..1872"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45637.1"
                     /db_xref="GeneID:55731"
                     /db_xref="HGNC:HGNC:25563"
ORIGIN      
        1 mlaclpgpgd lsfqllshtq mntglqkwdt tqkmrtahyp tpaeldayak kvannpltik
       61 ifpnsvkvpq rkhvrrtvng ldtsaqrysp yptqaatkag llaivkvpak silkdfdgtr
      121 arllpeaimn ppvapyatva pstlahpqaq alarqqalqh aqtlahappq tlqhpqgipp
      181 pqalshpqsl qqpqglghpq pmaqtqglvh pqalahqglq hphnpllhgg rkmpdsdapp
      241 nvtvststip lsmaatlqhs qppdlssivh qinqfcqtra gisttsvceg qianpspisr
      301 sllinastrv sthsvptpmp scvvnpmeht haataalpaa gpvnlptgis rvptgypsdl
      361 kpvtwnqhql ahlqqmcsea sgtpapgltg khaagrelag pgfvgkapay pqelclaqsf
      421 hlkpplekpt psppvngmaa playpnghyf qplwnnilpt pnsdssgsqd lampfhggqp
      481 tgapldcaaa pgahyragtg ggpvasqnsl mqtvdylsgd fqqacfreqs lamlskahra
      541 pgnrapdpte srslhiqhpg yr
//
LOCUS       NP_001070966             562 aa            linear   PRI 17-DEC-2025
DEFINITION  protein FAM222B isoform 2 [Homo sapiens].
ACCESSION   NP_001070966
VERSION     NP_001070966.1
DBSOURCE    REFSEQ: accession NM_001077498.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Calvario,E., Segovia,L. and Zurita,M.
  TITLE     Evolutionary analysis through structural modeling of FAM222
            proteins reveals a novel disordered conserved domain in vertebrates
            that interacts with NLK
  JOURNAL   Sci Rep 15 (1), 43372 (2025)
   PUBMED   41365991
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Spiegler,S., Kirchmaier,B., Rath,M., Korenke,G.C., Tetzlaff,F., van
            de Vorst,M., Neveling,K., Acker-Palmer,A., Kuss,A.W., Gilissen,C.,
            Fischer,A., Schulte-Merker,S. and Felbor,U.
  TITLE     FAM222B Is Not a Likely Novel Candidate Gene for Cerebral Cavernous
            Malformations
  JOURNAL   Mol Syndromol 7 (3), 144-152 (2016)
   PUBMED   27587990
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK057665.1, BC021228.2 and AC010761.10.
            
            Transcript Variant: This variant (1) differs in the 5' UTR, lacks
            an exon in the 5' coding region and initiates translation at an
            alternate start codon, compared to variant 3. Variants 1, 2, 4, 5,
            6, and 7 encode the same isoform (2), which is shorter and has a
            distinct N-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.149768.1,
                                           SRR1803612.131232.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000581407.6/ ENSP00000462419.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..562
                     /product="protein FAM222B isoform 2"
                     /note="uncharacterized protein C17orf63; protein FAM222B"
                     /calculated_mol_wt=59521
     Region          27..562
                     /region_name="FAM222A"
                     /note="Protein family of FAM222A; pfam15258"
                     /db_xref="CDD:464598"
     Region          155..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     Region          219..245
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     Region          537..562
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     CDS             1..562
                     /gene="FAM222B"
                     /gene_synonym="C17orf63"
                     /coded_by="NM_001077498.3:150..1838"
                     /note="isoform 2 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45637.1"
                     /db_xref="GeneID:55731"
                     /db_xref="HGNC:HGNC:25563"
ORIGIN      
        1 mlaclpgpgd lsfqllshtq mntglqkwdt tqkmrtahyp tpaeldayak kvannpltik
       61 ifpnsvkvpq rkhvrrtvng ldtsaqrysp yptqaatkag llaivkvpak silkdfdgtr
      121 arllpeaimn ppvapyatva pstlahpqaq alarqqalqh aqtlahappq tlqhpqgipp
      181 pqalshpqsl qqpqglghpq pmaqtqglvh pqalahqglq hphnpllhgg rkmpdsdapp
      241 nvtvststip lsmaatlqhs qppdlssivh qinqfcqtra gisttsvceg qianpspisr
      301 sllinastrv sthsvptpmp scvvnpmeht haataalpaa gpvnlptgis rvptgypsdl
      361 kpvtwnqhql ahlqqmcsea sgtpapgltg khaagrelag pgfvgkapay pqelclaqsf
      421 hlkpplekpt psppvngmaa playpnghyf qplwnnilpt pnsdssgsqd lampfhggqp
      481 tgapldcaaa pgahyragtg ggpvasqnsl mqtvdylsgd fqqacfreqs lamlskahra
      541 pgnrapdpte srslhiqhpg yr
//
LOCUS       NP_001275565             434 aa            linear   PRI 17-DEC-2025
DEFINITION  protein FAM222B isoform 3 [Homo sapiens].
ACCESSION   NP_001275565
VERSION     NP_001275565.1
DBSOURCE    REFSEQ: accession NM_001288636.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Calvario,E., Segovia,L. and Zurita,M.
  TITLE     Evolutionary analysis through structural modeling of FAM222
            proteins reveals a novel disordered conserved domain in vertebrates
            that interacts with NLK
  JOURNAL   Sci Rep 15 (1), 43372 (2025)
   PUBMED   41365991
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Spiegler,S., Kirchmaier,B., Rath,M., Korenke,G.C., Tetzlaff,F., van
            de Vorst,M., Neveling,K., Acker-Palmer,A., Kuss,A.W., Gilissen,C.,
            Fischer,A., Schulte-Merker,S. and Felbor,U.
  TITLE     FAM222B Is Not a Likely Novel Candidate Gene for Cerebral Cavernous
            Malformations
  JOURNAL   Mol Syndromol 7 (3), 144-152 (2016)
   PUBMED   27587990
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY006495.1, BC021228.2 and AC010761.10.
            
            Transcript Variant: This variant (8) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream start codon, compared to variant 3. Variants 8 through
            12 encode the same isoform (3), which is shorter at the N-terminus,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038194.1573719.1, SRR6380200.15723.17
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..434
                     /product="protein FAM222B isoform 3"
                     /note="uncharacterized protein C17orf63; protein FAM222B"
                     /calculated_mol_wt=45427
     Region          1..434
                     /region_name="FAM222A"
                     /note="Protein family of FAM222A; pfam15258"
                     /db_xref="CDD:464598"
     CDS             1..434
                     /gene="FAM222B"
                     /gene_synonym="C17orf63"
                     /coded_by="NM_001288636.2:606..1910"
                     /note="isoform 3 is encoded by transcript variant 8"
                     /db_xref="GeneID:55731"
                     /db_xref="HGNC:HGNC:25563"
ORIGIN      
        1 mnppvapyat vapstlahpq aqalarqqal qhaqtlahap pqtlqhpqgi pppqalshpq
       61 slqqpqglgh pqpmaqtqgl vhpqalahqg lqhphnpllh ggrkmpdsda ppnvtvstst
      121 iplsmaatlq hsqppdlssi vhqinqfcqt ragisttsvc egqianpspi srsllinast
      181 rvsthsvptp mpscvvnpme hthaataalp aagpvnlptg isrvptgyps dlkpvtwnqh
      241 qlahlqqmcs easgtpapgl tgkhaagrel agpgfvgkap aypqelclaq sfhlkpplek
      301 ptpsppvngm aaplaypngh yfqplwnnil ptpnsdssgs qdlampfhgg qptgapldca
      361 aapgahyrag tgggpvasqn slmqtvdyls gdfqqacfre qslamlskah rapgnrapdp
      421 tesrslhiqh pgyr
//
LOCUS       NP_116218                452 aa            linear   PRI 17-DEC-2025
DEFINITION  protein FAM222A [Homo sapiens].
ACCESSION   NP_116218
VERSION     NP_116218.2
DBSOURCE    REFSEQ: accession NM_032829.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Calvario,E., Segovia,L. and Zurita,M.
  TITLE     Evolutionary analysis through structural modeling of FAM222
            proteins reveals a novel disordered conserved domain in vertebrates
            that interacts with NLK
  JOURNAL   Sci Rep 15 (1), 43372 (2025)
   PUBMED   41365991
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Tzani,A., Haemmig,S., Cheng,H.S., Perez-Cremades,D.,
            Heuschkel,M.A., Jamaiyar,A., Singh,S.A., Aikawa,M., Yu,P.B.,
            Wang,T., Sun,Y., Feinberg,M.W. and Plutzky,J.
  TITLE     FAM222A, Part of the BET-Regulated Basal Endothelial Transcriptome,
            Is a Novel Determinant of Endothelial Biology and
            Angiogenesis-Brief Report
  JOURNAL   Arterioscler Thromb Vasc Biol 44 (1), 143-155 (2024)
   PUBMED   37942611
  REMARK    GeneRIF: FAM222A, Part of the BET-Regulated Basal Endothelial
            Transcriptome, Is a Novel Determinant of Endothelial Biology and
            Angiogenesis-Brief Report.
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Yan,T., Liang,J., Gao,J., Wang,L., Fujioka,H., Zhu,X. and Wang,X.
  CONSRTM   Alzheimer Disease Neuroimaging Initiative
  TITLE     FAM222A encodes a protein which accumulates in plaques in
            Alzheimer's disease
  JOURNAL   Nat Commun 11 (1), 411 (2020)
   PUBMED   31964863
  REMARK    GeneRIF: Study reports FAM222A as a putative brain atrophy
            susceptibility gene. The protein encoded by FAM222A is
            predominantly expressed in the CNS and is increased in brains of
            patients with Alzheimer's disease (AD) and in an AD mouse model. It
            accumulates within amyloid deposits, physically interacts with
            amyloid-beta (Abeta) via its N-terminal Abeta binding domain and
            facilitates Abeta aggregation.
            Erratum:[Nat Commun. 2022 Jul 11;13(1):4006. doi:
            10.1038/s41467-022-31711-8. PMID: 35817794]
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007834.40, DN994281.1 and BC020193.1.
            
            On Jan 6, 2010 this sequence version replaced NP_116218.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC020193.1, SRR14038194.3886010.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000538780.2/ ENSP00000443292.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..452
                     /product="protein FAM222A"
                     /note="aggregatin"
                     /calculated_mol_wt=46661
     Region          35..>275
                     /region_name="FAM222A"
                     /note="Protein family of FAM222A; pfam15258"
                     /db_xref="CDD:464598"
     CDS             1..452
                     /gene="FAM222A"
                     /gene_synonym="C12orf34"
                     /coded_by="NM_032829.3:1120..2478"
                     /db_xref="CCDS:CCDS9133.1"
                     /db_xref="GeneID:84915"
                     /db_xref="HGNC:HGNC:25915"
ORIGIN      
        1 mlaclqrtqn apgqhlacps kslelrkcea vasamhssry pspaeldaya ekvansplsi
       61 kifptnirvp qhkhlsrtvn gydtsgqrys pypqhtagyq gllaivkaav sssstaapag
      121 paksvlksae gkrtklspaa vqvgiapypv pstlgplayp kppeapappp glpaaataas
      181 viplpgrglp lppsnlpsih sllyqlnqqc qapgaappac qgmaiphpsp akhgpvpsfp
      241 smaysaaagl pdcrkgtelg qgatqaltla gaakpagyad sgldyllwpq kppppppqpl
      301 raysgstvas kspeacggra yerasgspln cgvglptsft vgqyfaapwn svlvtptsdc
      361 ynpaaavvvt elgpgaarel agppadalsg lpsksvcnts vlssslqsle ylindirppc
      421 ikeqmlgkgy etvavprlld hqhahirlpv yr
//
LOCUS       NP_001275564             562 aa            linear   PRI 17-DEC-2025
DEFINITION  protein FAM222B isoform 2 [Homo sapiens].
ACCESSION   NP_001275564
VERSION     NP_001275564.1
DBSOURCE    REFSEQ: accession NM_001288635.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Calvario,E., Segovia,L. and Zurita,M.
  TITLE     Evolutionary analysis through structural modeling of FAM222
            proteins reveals a novel disordered conserved domain in vertebrates
            that interacts with NLK
  JOURNAL   Sci Rep 15 (1), 43372 (2025)
   PUBMED   41365991
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Spiegler,S., Kirchmaier,B., Rath,M., Korenke,G.C., Tetzlaff,F., van
            de Vorst,M., Neveling,K., Acker-Palmer,A., Kuss,A.W., Gilissen,C.,
            Fischer,A., Schulte-Merker,S. and Felbor,U.
  TITLE     FAM222B Is Not a Likely Novel Candidate Gene for Cerebral Cavernous
            Malformations
  JOURNAL   Mol Syndromol 7 (3), 144-152 (2016)
   PUBMED   27587990
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY040104.1, DC381712.1, BC021228.2 and AC010761.10.
            
            Transcript Variant: This variant (7) differs in the 5' UTR, lacks
            an exon in the 5' coding region and initiates translation at an
            alternate start codon, compared to variant 3. Variants 1, 2, 4, 5,
            6, and 7 encode the same isoform (2), which is shorter and has a
            distinct N-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DC381712.1, DA661826.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..562
                     /product="protein FAM222B isoform 2"
                     /note="uncharacterized protein C17orf63; protein FAM222B"
                     /calculated_mol_wt=59521
     Region          27..562
                     /region_name="FAM222A"
                     /note="Protein family of FAM222A; pfam15258"
                     /db_xref="CDD:464598"
     Region          155..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     Region          219..245
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     Region          537..562
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU58.1)"
     CDS             1..562
                     /gene="FAM222B"
                     /gene_synonym="C17orf63"
                     /coded_by="NM_001288635.2:198..1886"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS45637.1"
                     /db_xref="GeneID:55731"
                     /db_xref="HGNC:HGNC:25563"
ORIGIN      
        1 mlaclpgpgd lsfqllshtq mntglqkwdt tqkmrtahyp tpaeldayak kvannpltik
       61 ifpnsvkvpq rkhvrrtvng ldtsaqrysp yptqaatkag llaivkvpak silkdfdgtr
      121 arllpeaimn ppvapyatva pstlahpqaq alarqqalqh aqtlahappq tlqhpqgipp
      181 pqalshpqsl qqpqglghpq pmaqtqglvh pqalahqglq hphnpllhgg rkmpdsdapp
      241 nvtvststip lsmaatlqhs qppdlssivh qinqfcqtra gisttsvceg qianpspisr
      301 sllinastrv sthsvptpmp scvvnpmeht haataalpaa gpvnlptgis rvptgypsdl
      361 kpvtwnqhql ahlqqmcsea sgtpapgltg khaagrelag pgfvgkapay pqelclaqsf
      421 hlkpplekpt psppvngmaa playpnghyf qplwnnilpt pnsdssgsqd lampfhggqp
      481 tgapldcaaa pgahyragtg ggpvasqnsl mqtvdylsgd fqqacfreqs lamlskahra
      541 pgnrapdpte srslhiqhpg yr
//
LOCUS       NP_001275567             434 aa            linear   PRI 17-DEC-2025
DEFINITION  protein FAM222B isoform 3 [Homo sapiens].
ACCESSION   NP_001275567 XP_005258062
VERSION     NP_001275567.1
DBSOURCE    REFSEQ: accession NM_001288638.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Calvario,E., Segovia,L. and Zurita,M.
  TITLE     Evolutionary analysis through structural modeling of FAM222
            proteins reveals a novel disordered conserved domain in vertebrates
            that interacts with NLK
  JOURNAL   Sci Rep 15 (1), 43372 (2025)
   PUBMED   41365991
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Spiegler,S., Kirchmaier,B., Rath,M., Korenke,G.C., Tetzlaff,F., van
            de Vorst,M., Neveling,K., Acker-Palmer,A., Kuss,A.W., Gilissen,C.,
            Fischer,A., Schulte-Merker,S. and Felbor,U.
  TITLE     FAM222B Is Not a Likely Novel Candidate Gene for Cerebral Cavernous
            Malformations
  JOURNAL   Mol Syndromol 7 (3), 144-152 (2016)
   PUBMED   27587990
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY040104.1, DC400943.1, BC021228.2 and AC010761.10.
            
            On Dec 25, 2013 this sequence version replaced XP_005258062.1.
            
            Transcript Variant: This variant (10) differs in the 5' UTR, lacks
            a portion of the 5' coding region and initiates translation at a
            downstream start codon, compared to variant 3. Variants 8 through
            12 encode the same isoform (3), which is shorter at the N-terminus,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1291563.1,
                                           SRR14038195.2659519.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..434
                     /product="protein FAM222B isoform 3"
                     /note="uncharacterized protein C17orf63; protein FAM222B"
                     /calculated_mol_wt=45427
     Region          1..434
                     /region_name="FAM222A"
                     /note="Protein family of FAM222A; pfam15258"
                     /db_xref="CDD:464598"
     CDS             1..434
                     /gene="FAM222B"
                     /gene_synonym="C17orf63"
                     /coded_by="NM_001288638.2:504..1808"
                     /note="isoform 3 is encoded by transcript variant 10"
                     /db_xref="GeneID:55731"
                     /db_xref="HGNC:HGNC:25563"
ORIGIN      
        1 mnppvapyat vapstlahpq aqalarqqal qhaqtlahap pqtlqhpqgi pppqalshpq
       61 slqqpqglgh pqpmaqtqgl vhpqalahqg lqhphnpllh ggrkmpdsda ppnvtvstst
      121 iplsmaatlq hsqppdlssi vhqinqfcqt ragisttsvc egqianpspi srsllinast
      181 rvsthsvptp mpscvvnpme hthaataalp aagpvnlptg isrvptgyps dlkpvtwnqh
      241 qlahlqqmcs easgtpapgl tgkhaagrel agpgfvgkap aypqelclaq sfhlkpplek
      301 ptpsppvngm aaplaypngh yfqplwnnil ptpnsdssgs qdlampfhgg qptgapldca
      361 aapgahyrag tgggpvasqn slmqtvdyls gdfqqacfre qslamlskah rapgnrapdp
      421 tesrslhiqh pgyr
//
LOCUS       NP_001428612             260 aa            linear   PRI 18-DEC-2025
DEFINITION  fibronectin type III domain-containing protein 5 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001428612
VERSION     NP_001428612.1
DBSOURCE    REFSEQ: accession NM_001441683.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Chen,Q., Wang,J., Li,K., Luan,J.Q., Li,J.M. and Wang,Y.T.
  TITLE     Irisin in thyroid diseases
  JOURNAL   Clin Chim Acta 564, 119929 (2025)
   PUBMED   39154700
  REMARK    GeneRIF: Irisin in thyroid diseases.
            Review article
            Erratum:[Clin Chim Acta. 2025 Jan 30;566:120034. doi:
            10.1016/j.cca.2024.120034. PMID: 39550251]
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Zhao,F., Xu,D., Wang,X. and Wang,X.
  TITLE     FNDC5 affects invasion and migration of oral cancer by inhibiting
            PI3K/Akt/Snail signaling pathway
  JOURNAL   Sci Rep 14 (1), 26881 (2024)
   PUBMED   39505986
  REMARK    GeneRIF: FNDC5 affects invasion and migration of oral cancer by
            inhibiting PI3K/Akt/Snail signaling pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Gliwinska,A., Badenska,M., Dworak,M., Swietochowska,E.,
            Badenski,A., Bjanid,O., Trembecka-Dubel,E., Morawiec-Knysak,A. and
            Szczepanska,M.
  TITLE     Assessment of brain-derived neurotrophic factor and irisin
            concentration in children with chronic kidney disease: a pilot
            study
  JOURNAL   BMC Nephrol 25 (1), 318 (2024)
   PUBMED   39334009
  REMARK    GeneRIF: Assessment of brain-derived neurotrophic factor and irisin
            concentration in children with chronic kidney disease: a pilot
            study.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Radikova,Z., Mosna,L., Eckerstorfer,C., Bajer,B., Havranova,A.,
            Imrich,R., Vlcek,M. and Penesova,A.
  TITLE     Plasma irisin and the brain-derived neurotrophic factor levels in
            sedentary subjects: effect of 8-weeks lifestyle intervention
  JOURNAL   Endocr Regul 58 (1), 115-128 (2024)
   PUBMED   38861537
  REMARK    GeneRIF: Plasma irisin and the brain-derived neurotrophic factor
            levels in sedentary subjects: effect of 8-weeks lifestyle
            intervention.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Lecker,S.H., Zavin,A., Cao,P., Arena,R., Allsup,K., Daniels,K.M.,
            Joseph,J., Schulze,P.C. and Forman,D.E.
  TITLE     Expression of the irisin precursor FNDC5 in skeletal muscle
            correlates with aerobic exercise performance in patients with heart
            failure
  JOURNAL   Circ Heart Fail 5 (6), 812-818 (2012)
   PUBMED   23001918
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Wu,J., Bostrom,P., Sparks,L.M., Ye,L., Choi,J.H., Giang,A.H.,
            Khandekar,M., Virtanen,K.A., Nuutila,P., Schaart,G., Huang,K.,
            Tu,H., van Marken Lichtenbelt,W.D., Hoeks,J., Enerback,S.,
            Schrauwen,P. and Spiegelman,B.M.
  TITLE     Beige adipocytes are a distinct type of thermogenic fat cell in
            mouse and human
  JOURNAL   Cell 150 (2), 366-376 (2012)
   PUBMED   22796012
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Kelly,D.P.
  TITLE     Medicine. Irisin, light my fire
  JOURNAL   Science 336 (6077), 42-43 (2012)
   PUBMED   22491843
REFERENCE   8  (residues 1 to 260)
  AUTHORS   Bostrom,P., Wu,J., Jedrychowski,M.P., Korde,A., Ye,L., Lo,J.C.,
            Rasbach,K.A., Bostrom,E.A., Choi,J.H., Long,J.Z., Kajimura,S.,
            Zingaretti,M.C., Vind,B.F., Tu,H., Cinti,S., Hojlund,K., Gygi,S.P.
            and Spiegelman,B.M.
  TITLE     A PGC1-alpha-dependent myokine that drives brown-fat-like
            development of white fat and thermogenesis
  JOURNAL   Nature 481 (7382), 463-468 (2012)
   PUBMED   22237023
  REMARK    GeneRIF: Experimental evidence (Western and mass spectrometry) of
            mouse and human secreted irisin peptide
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 260)
  AUTHORS   Ivanov,I.P., Firth,A.E., Michel,A.M., Atkins,J.F. and Baranov,P.V.
  TITLE     Identification of evolutionarily conserved non-AUG-initiated
            N-terminal extensions in human coding sequences
  JOURNAL   Nucleic Acids Res 39 (10), 4220-4234 (2011)
   PUBMED   21266472
  REMARK    GeneRIF: infers non-AUG translation initiation codon for FNDC5
            based on evolutionary comparisons; only human has an ''ATA'' at a
            position that is ''ATG'' in other mammals
REFERENCE   10 (residues 1 to 260)
  AUTHORS   Teufel,A., Malik,N., Mukhopadhyay,M. and Westphal,H.
  TITLE     Frcp1 and Frcp2, two novel fibronectin type III repeat containing
            genes
  JOURNAL   Gene 297 (1-2), 79-83 (2002)
   PUBMED   12384288
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC114493.3.
            
            Summary: This gene encodes a secreted protein that is released from
            muscle cells during exercise. The encoded protein may participate
            in the development of brown fat. Translation of the precursor
            protein initiates at a non-AUG start codon at a position that is
            conserved as an AUG start codon in other organisms. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jun 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK092102.1, ERR4352443.293130.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..260
                     /product="fibronectin type III domain-containing protein 5
                     isoform 5"
                     /note="fibronectin type III repeat-containing protein 2"
                     /calculated_mol_wt=28152
     mat_peptide     1..191
                     /product="Irisin. /id=PRO_0000415857"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAU1.4)"
                     /calculated_mol_wt=20557
     Region          1..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAU1.4)"
     Region          82..172
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(82,145,160)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            87
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NAU1.4)"
     Site            126
                     /site_type="other"
                     /note="Required for dimerization.
                     /evidence=ECO:0000269|PubMed:24114836; propagated from
                     UniProtKB/Swiss-Prot (Q8NAU1.4)"
     Site            132
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NAU1.4)"
     Site            order(161..162,164..165)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          199..>232
                     /region_name="DUF4808"
                     /note="Domain of unknown function (DUF4808); pfam16066"
                     /db_xref="CDD:374343"
     Site            201..221
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAU1.4)"
     Region          230..260
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAU1.4)"
     Region          258..260
                     /region_name="Microbody targeting signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAU1.4)"
     CDS             1..260
                     /gene="FNDC5"
                     /gene_synonym="FRCP2; irisin"
                     /coded_by="NM_001441683.1:23..805"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:252995"
                     /db_xref="HGNC:HGNC:20240"
                     /db_xref="MIM:611906"
ORIGIN      
        1 mqaarggagr perpgrpgrg perererppg agaaspcaap glpaggatih pgspsawppr
       61 araalrlwlg cvcfalvqad spsapvnvtv rhlkansavv swdvledevv igfaisqqkk
      121 dvrmlrfiqe vntttrscal wdleedteyi vhvqaisiqg qspasepvlf ktpreaekma
      181 sknkdevtmk emgrnqqlrt gevliivvvl fmwagvialf crqydiikdn epnnnkektk
      241 sasetstpeh qgggllrski
//
LOCUS       NP_001265554             836 aa            linear   PRI 18-DEC-2025
DEFINITION  crooked neck-like protein 1 isoform b [Homo sapiens].
ACCESSION   NP_001265554
VERSION     NP_001265554.1
DBSOURCE    REFSEQ: accession NM_001278625.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 836)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 836)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   3  (residues 1 to 836)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 836)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   5  (residues 1 to 836)
  AUTHORS   Xiao,H., Wyler,E., Milek,M., Grewe,B., Kirchner,P., Ekici,A.,
            Silva,A.B.O.V., Jungnickl,D., Full,F., Thomas,M., Landthaler,M.,
            Ensser,A. and Uberla,K.
  TITLE     CRNKL1 Is a Highly Selective Regulator of Intron-Retaining HIV-1
            and Cellular mRNAs
  JOURNAL   mBio 12 (1), e02525-20 (2021)
   PUBMED   33468685
  REMARK    GeneRIF: CRNKL1 Is a Highly Selective Regulator of Intron-Retaining
            HIV-1 and Cellular mRNAs.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 836)
  AUTHORS   Hillman,R.T., Green,R.E. and Brenner,S.E.
  TITLE     An unappreciated role for RNA surveillance
  JOURNAL   Genome Biol 5 (2), R8 (2004)
   PUBMED   14759258
REFERENCE   7  (residues 1 to 836)
  AUTHORS   Chung,S., Zhou,Z., Huddleston,K.A., Harrison,D.A., Reed,R.,
            Coleman,T.A. and Rymond,B.C.
  TITLE     Crooked neck is a component of the human spliceosome and implicated
            in the splicing process
  JOURNAL   Biochim Biophys Acta 1576 (3), 287-297 (2002)
   PUBMED   12084575
  REMARK    GeneRIF: Data show that crooked neck activity appears essential as
            extracts depleted of hcrn fail to splice pre-mRNA. These and
            related data support the view that crooked neck is a
            phylogenetically conserved pre-mRNA splicing factor.
REFERENCE   8  (residues 1 to 836)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   9  (residues 1 to 836)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   10 (residues 1 to 836)
  AUTHORS   Lai,C.H., Chiu,J.Y. and Lin,W.
  TITLE     Identification of the human crooked neck gene by comparative gene
            identification
  JOURNAL   Biochim Biophys Acta 1517 (3), 449-454 (2001)
   PUBMED   11342225
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF255443.2, BC144222.1,
            AL832435.1 and AA255987.1.
            
            Summary: The crooked neck (crn) gene of Drosophila is essential for
            embryogenesis and is thought to be involved in cell cycle
            progression and pre-mRNA splicing. A protein encoded by this human
            locus has been found to localize to pre-mRNA splicing complexes in
            the nucleus and is necessary for pre-mRNA splicing. Alternatively
            spliced transcript variants have been described. [provided by
            RefSeq, Jul 2013].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 5' coding region, compared to variant 1. This
            results in a shorter protein (isoform b), compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF255443.2, BC144222.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..836
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.23"
     Protein         1..836
                     /product="crooked neck-like protein 1 isoform b"
                     /note="crooked neck-like 1; crooked neck-like protein 1;
                     crooked neck homolog; Crn, crooked neck-like 1; SYF3
                     pre-mRNA-splicing factor; crooked neck pre-mRNA splicing
                     factor-like 1"
                     /calculated_mol_wt=99043
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          69..94
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          210..242
                     /region_name="HAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          233..258
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(234..235,238..239,241,265,268..269,272..273,
                     275..276,299,302..303,306..307,310)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          241..430
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          244..276
                     /region_name="HAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          263..293
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          278..310
                     /region_name="HAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          298..326
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          312..343
                     /region_name="HAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          345..376
                     /region_name="HAT"
                     /note="HAT (Half-A-TPR) repeat; pfam02184"
                     /db_xref="CDD:111114"
     Region          345..376
                     /region_name="HAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          378..413
                     /region_name="HAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          399..616
                     /region_name="Mediates interaction with HSP90.
                     /evidence=ECO:0000250|UniProtKB:P63154"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          468..712
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            491
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          561..589
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(562,565..566,569..570,572,595,598..599,602..603,
                     605..606,629,632..633,636..637,640)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          594..623
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          608..640
                     /region_name="HAT 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          628..656
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          642..676
                     /region_name="HAT 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          678..709
                     /region_name="HAT 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          714..755
                     /region_name="HAT 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          757..795
                     /region_name="HAT 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          797..822
                     /region_name="HAT 17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          815..836
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     CDS             1..836
                     /gene="CRNKL1"
                     /gene_synonym="CLF; Clf1; CRN; HCRN; MGCH; MSTP021; SYF3"
                     /coded_by="NM_001278625.2:33..2543"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS63239.1"
                     /db_xref="GeneID:51340"
                     /db_xref="HGNC:HGNC:15762"
                     /db_xref="MIM:610952"
ORIGIN      
        1 mtatvenltf qkdtlgnavd knrrhgstep lvlawssqfr rltwgcalda lhrspcvaas
       61 qhgvthlirs srtphstrcr kedaqpghhg ngaasvtaqa rgqrsvlqvp lpvprsclfs
      121 esfvvsvssq srflasvpgt gvqrstaadm aastaagkqr ipkvakvknk apaevqitae
      181 qllreakere lellppppqq kitdeeelnd yklrkrktfe dnirknrtvi snwikyaqwe
      241 eslkeiqrar siyeraldvd yrnitlwlky aememknrqv nharniwdra ittlprvnqf
      301 wykytymeem lgnvagarqv ferwmewqpe eqawhsyinf elrykevdra rtiyerfvlv
      361 hpdvknwiky arfeekhayf aharkvyera veffgdehmd ehlyvafakf eenqkeferv
      421 rviykyaldr iskqdaqelf knytifekkf gdrrgiedii vskrrfqyee evkanphnyd
      481 awfdylrlve sdaeaeavre vyeraianvp piqekrhwkr yiylwinyal yeeleakdpe
      541 rtrqvyqasl eliphkkftf akmwilyaqf eirqknlsla rralgtsigk cpknklfkvy
      601 ielelqlref drcrklyekf lefgpencts wikfaeleti lgdidrarai yelaisqprl
      661 dmpevlwksy idfeieqeet ertrnlyrrl lqrtqhvkvw isfaqfelss gkegsltkcr
      721 qiyeeanktm rnceekeerl mlleswrsfe eefgtasdke rvdklmpekv kkrrkvqtdd
      781 gsdagweeyf dyifpedaan qpnlkllama klwkkqqqek edaehhpded vdeses
//
LOCUS       NP_001265557             687 aa            linear   PRI 18-DEC-2025
DEFINITION  crooked neck-like protein 1 isoform d [Homo sapiens].
ACCESSION   NP_001265557
VERSION     NP_001265557.1
DBSOURCE    REFSEQ: accession NM_001278628.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   3  (residues 1 to 687)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 687)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   5  (residues 1 to 687)
  AUTHORS   Xiao,H., Wyler,E., Milek,M., Grewe,B., Kirchner,P., Ekici,A.,
            Silva,A.B.O.V., Jungnickl,D., Full,F., Thomas,M., Landthaler,M.,
            Ensser,A. and Uberla,K.
  TITLE     CRNKL1 Is a Highly Selective Regulator of Intron-Retaining HIV-1
            and Cellular mRNAs
  JOURNAL   mBio 12 (1), e02525-20 (2021)
   PUBMED   33468685
  REMARK    GeneRIF: CRNKL1 Is a Highly Selective Regulator of Intron-Retaining
            HIV-1 and Cellular mRNAs.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 687)
  AUTHORS   Hillman,R.T., Green,R.E. and Brenner,S.E.
  TITLE     An unappreciated role for RNA surveillance
  JOURNAL   Genome Biol 5 (2), R8 (2004)
   PUBMED   14759258
REFERENCE   7  (residues 1 to 687)
  AUTHORS   Chung,S., Zhou,Z., Huddleston,K.A., Harrison,D.A., Reed,R.,
            Coleman,T.A. and Rymond,B.C.
  TITLE     Crooked neck is a component of the human spliceosome and implicated
            in the splicing process
  JOURNAL   Biochim Biophys Acta 1576 (3), 287-297 (2002)
   PUBMED   12084575
  REMARK    GeneRIF: Data show that crooked neck activity appears essential as
            extracts depleted of hcrn fail to splice pre-mRNA. These and
            related data support the view that crooked neck is a
            phylogenetically conserved pre-mRNA splicing factor.
REFERENCE   8  (residues 1 to 687)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   9  (residues 1 to 687)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   10 (residues 1 to 687)
  AUTHORS   Lai,C.H., Chiu,J.Y. and Lin,W.
  TITLE     Identification of the human crooked neck gene by comparative gene
            identification
  JOURNAL   Biochim Biophys Acta 1517 (3), 449-454 (2001)
   PUBMED   11342225
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB040881.1, BI550198.1,
            AL832435.1 and AA255987.1.
            
            Summary: The crooked neck (crn) gene of Drosophila is essential for
            embryogenesis and is thought to be involved in cell cycle
            progression and pre-mRNA splicing. A protein encoded by this human
            locus has been found to localize to pre-mRNA splicing complexes in
            the nucleus and is necessary for pre-mRNA splicing. Alternatively
            spliced transcript variants have been described. [provided by
            RefSeq, Jul 2013].
            
            Transcript Variant: This variant (5) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at a
            downstream start codon, compared to variant 1. This variant
            represents use of an alternate promoter, compared to variant 1. The
            encoded isoform (d) is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL832435.1, AF111802.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000536226.2/ ENSP00000440733.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.23"
     Protein         1..687
                     /product="crooked neck-like protein 1 isoform d"
                     /note="crooked neck-like 1; crooked neck-like protein 1;
                     crooked neck homolog; Crn, crooked neck-like 1; SYF3
                     pre-mRNA-splicing factor; crooked neck pre-mRNA splicing
                     factor-like 1"
                     /calculated_mol_wt=83018
     Region          84..109
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(85..86,89..90,92,116,119..120,123..124,126..127,150,
                     153..154,157..158,161)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          92..281
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          114..144
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          149..177
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          196..227
                     /region_name="HAT"
                     /note="HAT (Half-A-TPR) repeat; pfam02184"
                     /db_xref="CDD:111114"
     Region          319..563
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          412..440
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(413,416..417,420..421,423,446,449..450,453..454,
                     456..457,480,483..484,487..488,491)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          445..474
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          479..507
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..687
                     /gene="CRNKL1"
                     /gene_synonym="CLF; Clf1; CRN; HCRN; MGCH; MSTP021; SYF3"
                     /coded_by="NM_001278628.2:125..2188"
                     /note="isoform d is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS63238.1"
                     /db_xref="GeneID:51340"
                     /db_xref="HGNC:HGNC:15762"
                     /db_xref="MIM:610952"
ORIGIN      
        1 maastaagkq ripkvakvkn kapaevqita eqllreaker elellppppq qkitdeeeln
       61 dyklrkrktf ednirknrtv isnwikyaqw eeslkeiqra rsiyeraldv dyrnitlwlk
      121 yaememknrq vnharniwdr aittlprvnq fwykytymee mlgnvagarq vferwmewqp
      181 eeqawhsyin felrykevdr artiyerfvl vhpdvknwik yarfeekhay faharkvyer
      241 aveffgdehm dehlyvafak feenqkefer vrviykyald riskqdaqel fknytifekk
      301 fgdrrgiedi ivskrrfqye eevkanphny dawfdylrlv esdaeaeavr evyeraianv
      361 ppiqekrhwk ryiylwinya lyeeleakdp ertrqvyqas leliphkkft fakmwilyaq
      421 feirqknlsl arralgtsig kcpknklfkv yielelqlre fdrcrklyek flefgpenct
      481 swikfaelet ilgdidrara iyelaisqpr ldmpevlwks yidfeieqee tertrnlyrr
      541 llqrtqhvkv wisfaqfels sgkegsltkc rqiyeeankt mrnceekeer lmlleswrsf
      601 eeefgtasdk ervdklmpek vkkrrkvqtd dgsdagweey fdyifpedaa nqpnlkllam
      661 aklwkkqqqe kedaehhpde dvdeses
//
LOCUS       NP_001265555             564 aa            linear   PRI 18-DEC-2025
DEFINITION  crooked neck-like protein 1 isoform c [Homo sapiens].
ACCESSION   NP_001265555
VERSION     NP_001265555.1
DBSOURCE    REFSEQ: accession NM_001278626.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   5  (residues 1 to 564)
  AUTHORS   Xiao,H., Wyler,E., Milek,M., Grewe,B., Kirchner,P., Ekici,A.,
            Silva,A.B.O.V., Jungnickl,D., Full,F., Thomas,M., Landthaler,M.,
            Ensser,A. and Uberla,K.
  TITLE     CRNKL1 Is a Highly Selective Regulator of Intron-Retaining HIV-1
            and Cellular mRNAs
  JOURNAL   mBio 12 (1), e02525-20 (2021)
   PUBMED   33468685
  REMARK    GeneRIF: CRNKL1 Is a Highly Selective Regulator of Intron-Retaining
            HIV-1 and Cellular mRNAs.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 564)
  AUTHORS   Hillman,R.T., Green,R.E. and Brenner,S.E.
  TITLE     An unappreciated role for RNA surveillance
  JOURNAL   Genome Biol 5 (2), R8 (2004)
   PUBMED   14759258
REFERENCE   7  (residues 1 to 564)
  AUTHORS   Chung,S., Zhou,Z., Huddleston,K.A., Harrison,D.A., Reed,R.,
            Coleman,T.A. and Rymond,B.C.
  TITLE     Crooked neck is a component of the human spliceosome and implicated
            in the splicing process
  JOURNAL   Biochim Biophys Acta 1576 (3), 287-297 (2002)
   PUBMED   12084575
  REMARK    GeneRIF: Data show that crooked neck activity appears essential as
            extracts depleted of hcrn fail to splice pre-mRNA. These and
            related data support the view that crooked neck is a
            phylogenetically conserved pre-mRNA splicing factor.
REFERENCE   8  (residues 1 to 564)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   9  (residues 1 to 564)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   10 (residues 1 to 564)
  AUTHORS   Lai,C.H., Chiu,J.Y. and Lin,W.
  TITLE     Identification of the human crooked neck gene by comparative gene
            identification
  JOURNAL   Biochim Biophys Acta 1517 (3), 449-454 (2001)
   PUBMED   11342225
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF318304.1, BC144222.1,
            AL832435.1 and AA255987.1.
            
            Summary: The crooked neck (crn) gene of Drosophila is essential for
            embryogenesis and is thought to be involved in cell cycle
            progression and pre-mRNA splicing. A protein encoded by this human
            locus has been found to localize to pre-mRNA splicing complexes in
            the nucleus and is necessary for pre-mRNA splicing. Alternatively
            spliced transcript variants have been described. [provided by
            RefSeq, Jul 2013].
            
            Transcript Variant: This variant (3) uses two alternate splice
            sites in the 5' UTR, compared to variant 1. These differences
            result in predicted translation initiation at a downstream in-frame
            start site through ribosomal re-initiation and/or leaky scanning.
            The encoded isoform (c) is shorter than isoform a. Both variants 3
            and 4 encode the same isoform (c).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF318304.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.23"
     Protein         1..564
                     /product="crooked neck-like protein 1 isoform c"
                     /note="crooked neck-like 1; crooked neck-like protein 1;
                     crooked neck homolog; Crn, crooked neck-like 1; SYF3
                     pre-mRNA-splicing factor; crooked neck pre-mRNA splicing
                     factor-like 1"
                     /calculated_mol_wt=68481
     Region          3..125
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          73..104
                     /region_name="HAT"
                     /note="HAT (Half-A-TPR) repeat; pfam02184"
                     /db_xref="CDD:111114"
     Region          196..440
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          289..317
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(290,293..294,297..298,300,323,326..327,330..331,
                     333..334,357,360..361,364..365,368)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          322..351
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          356..384
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..564
                     /gene="CRNKL1"
                     /gene_synonym="CLF; Clf1; CRN; HCRN; MGCH; MSTP021; SYF3"
                     /coded_by="NM_001278626.2:662..2356"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:51340"
                     /db_xref="HGNC:HGNC:15762"
                     /db_xref="MIM:610952"
ORIGIN      
        1 memknrqvnh arniwdrait tlprvnqfwy kytymeemlg nvagarqvfe rwmewqpeeq
       61 awhsyinfel rykevdrart iyerfvlvhp dvknwikyar feekhayfah arkvyerave
      121 ffgdehmdeh lyvafakfee nqkefervrv iykyaldris kqdaqelfkn ytifekkfgd
      181 rrgiediivs krrfqyeeev kanphnydaw fdylrlvesd aeaeavrevy eraianvppi
      241 qekrhwkryi ylwinyalye eleakdpert rqvyqaslel iphkkftfak mwilyaqfei
      301 rqknlslarr algtsigkcp knklfkvyie lelqlrefdr crklyekfle fgpenctswi
      361 kfaeletilg didraraiye laisqprldm pevlwksyid feieqeeter trnlyrrllq
      421 rtqhvkvwis faqfelssgk egsltkcrqi yeeanktmrn ceekeerlml leswrsfeee
      481 fgtasdkerv dklmpekvkk rrkvqtddgs dagweeyfdy ifpedaanqp nlkllamakl
      541 wkkqqqeked aehhpdedvd eses
//
LOCUS       NP_057736                848 aa            linear   PRI 18-DEC-2025
DEFINITION  crooked neck-like protein 1 isoform a [Homo sapiens].
ACCESSION   NP_057736
VERSION     NP_057736.4
DBSOURCE    REFSEQ: accession NM_016652.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 848)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 848)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   3  (residues 1 to 848)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 848)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   5  (residues 1 to 848)
  AUTHORS   Xiao,H., Wyler,E., Milek,M., Grewe,B., Kirchner,P., Ekici,A.,
            Silva,A.B.O.V., Jungnickl,D., Full,F., Thomas,M., Landthaler,M.,
            Ensser,A. and Uberla,K.
  TITLE     CRNKL1 Is a Highly Selective Regulator of Intron-Retaining HIV-1
            and Cellular mRNAs
  JOURNAL   mBio 12 (1), e02525-20 (2021)
   PUBMED   33468685
  REMARK    GeneRIF: CRNKL1 Is a Highly Selective Regulator of Intron-Retaining
            HIV-1 and Cellular mRNAs.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 848)
  AUTHORS   Hillman,R.T., Green,R.E. and Brenner,S.E.
  TITLE     An unappreciated role for RNA surveillance
  JOURNAL   Genome Biol 5 (2), R8 (2004)
   PUBMED   14759258
REFERENCE   7  (residues 1 to 848)
  AUTHORS   Chung,S., Zhou,Z., Huddleston,K.A., Harrison,D.A., Reed,R.,
            Coleman,T.A. and Rymond,B.C.
  TITLE     Crooked neck is a component of the human spliceosome and implicated
            in the splicing process
  JOURNAL   Biochim Biophys Acta 1576 (3), 287-297 (2002)
   PUBMED   12084575
  REMARK    GeneRIF: Data show that crooked neck activity appears essential as
            extracts depleted of hcrn fail to splice pre-mRNA. These and
            related data support the view that crooked neck is a
            phylogenetically conserved pre-mRNA splicing factor.
REFERENCE   8  (residues 1 to 848)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   9  (residues 1 to 848)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   10 (residues 1 to 848)
  AUTHORS   Lai,C.H., Chiu,J.Y. and Lin,W.
  TITLE     Identification of the human crooked neck gene by comparative gene
            identification
  JOURNAL   Biochim Biophys Acta 1517 (3), 449-454 (2001)
   PUBMED   11342225
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF318303.1, AL035454.18,
            BC144222.1, AL832435.1 and AA255987.1.
            
            On Jan 29, 2007 this sequence version replaced NP_057736.3.
            
            Summary: The crooked neck (crn) gene of Drosophila is essential for
            embryogenesis and is thought to be involved in cell cycle
            progression and pre-mRNA splicing. A protein encoded by this human
            locus has been found to localize to pre-mRNA splicing complexes in
            the nucleus and is necessary for pre-mRNA splicing. Alternatively
            spliced transcript variants have been described. [provided by
            RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF318303.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..848
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.23"
     Protein         1..848
                     /product="crooked neck-like protein 1 isoform a"
                     /note="crooked neck-like 1; crooked neck-like protein 1;
                     crooked neck homolog; Crn, crooked neck-like 1; SYF3
                     pre-mRNA-splicing factor; crooked neck pre-mRNA splicing
                     factor-like 1"
                     /calculated_mol_wt=100321
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          81..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          222..254
                     /region_name="HAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          245..270
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(246..247,250..251,253,277,280..281,284..285,
                     287..288,311,314..315,318..319,322)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          253..442
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          256..288
                     /region_name="HAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          275..305
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          290..322
                     /region_name="HAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          310..338
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          324..355
                     /region_name="HAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          357..388
                     /region_name="HAT"
                     /note="HAT (Half-A-TPR) repeat; pfam02184"
                     /db_xref="CDD:111114"
     Region          357..388
                     /region_name="HAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          390..425
                     /region_name="HAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          411..628
                     /region_name="Mediates interaction with HSP90.
                     /evidence=ECO:0000250|UniProtKB:P63154"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          480..724
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          573..601
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(574,577..578,581..582,584,607,610..611,614..615,
                     617..618,641,644..645,648..649,652)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          606..635
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          620..652
                     /region_name="HAT 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          640..668
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          654..688
                     /region_name="HAT 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          690..721
                     /region_name="HAT 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          726..767
                     /region_name="HAT 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          769..807
                     /region_name="HAT 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          809..834
                     /region_name="HAT 17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     Region          827..848
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZJ0.4)"
     CDS             1..848
                     /gene="CRNKL1"
                     /gene_synonym="CLF; Clf1; CRN; HCRN; MGCH; MSTP021; SYF3"
                     /coded_by="NM_016652.6:33..2579"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33446.1"
                     /db_xref="GeneID:51340"
                     /db_xref="HGNC:HGNC:15762"
                     /db_xref="MIM:610952"
ORIGIN      
        1 mtatvenltf qkdtlgnavd kntsrlelrs yslagrhgst eplvlawssq frrltwgcal
       61 dalhrspcva asqhgvthli rssrtphstr crkedaqpgh hgngaasvta qargqrsvlq
      121 vplpvprscl fsesfvvsvs sqsrflasvp gtgvqrstaa dmaastaagk qripkvakvk
      181 nkapaevqit aeqllreake relellpppp qqkitdeeel ndyklrkrkt fednirknrt
      241 visnwikyaq weeslkeiqr arsiyerald vdyrnitlwl kyaememknr qvnharniwd
      301 raittlprvn qfwykytyme emlgnvagar qvferwmewq peeqawhsyi nfelrykevd
      361 rartiyerfv lvhpdvknwi kyarfeekha yfaharkvye raveffgdeh mdehlyvafa
      421 kfeenqkefe rvrviykyal driskqdaqe lfknytifek kfgdrrgied iivskrrfqy
      481 eeevkanphn ydawfdylrl vesdaeaeav revyeraian vppiqekrhw kryiylwiny
      541 alyeeleakd pertrqvyqa sleliphkkf tfakmwilya qfeirqknls larralgtsi
      601 gkcpknklfk vyielelqlr efdrcrklye kflefgpenc tswikfaele tilgdidrar
      661 aiyelaisqp rldmpevlwk syidfeieqe etertrnlyr rllqrtqhvk vwisfaqfel
      721 ssgkegsltk crqiyeeank tmrnceekee rlmlleswrs feeefgtasd kervdklmpe
      781 kvkkrrkvqt ddgsdagwee yfdyifpeda anqpnlklla maklwkkqqq ekedaehhpd
      841 edvdeses
//
LOCUS       NP_001265556             564 aa            linear   PRI 18-DEC-2025
DEFINITION  crooked neck-like protein 1 isoform c [Homo sapiens].
ACCESSION   NP_001265556
VERSION     NP_001265556.1
DBSOURCE    REFSEQ: accession NM_001278627.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   5  (residues 1 to 564)
  AUTHORS   Xiao,H., Wyler,E., Milek,M., Grewe,B., Kirchner,P., Ekici,A.,
            Silva,A.B.O.V., Jungnickl,D., Full,F., Thomas,M., Landthaler,M.,
            Ensser,A. and Uberla,K.
  TITLE     CRNKL1 Is a Highly Selective Regulator of Intron-Retaining HIV-1
            and Cellular mRNAs
  JOURNAL   mBio 12 (1), e02525-20 (2021)
   PUBMED   33468685
  REMARK    GeneRIF: CRNKL1 Is a Highly Selective Regulator of Intron-Retaining
            HIV-1 and Cellular mRNAs.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 564)
  AUTHORS   Hillman,R.T., Green,R.E. and Brenner,S.E.
  TITLE     An unappreciated role for RNA surveillance
  JOURNAL   Genome Biol 5 (2), R8 (2004)
   PUBMED   14759258
REFERENCE   7  (residues 1 to 564)
  AUTHORS   Chung,S., Zhou,Z., Huddleston,K.A., Harrison,D.A., Reed,R.,
            Coleman,T.A. and Rymond,B.C.
  TITLE     Crooked neck is a component of the human spliceosome and implicated
            in the splicing process
  JOURNAL   Biochim Biophys Acta 1576 (3), 287-297 (2002)
   PUBMED   12084575
  REMARK    GeneRIF: Data show that crooked neck activity appears essential as
            extracts depleted of hcrn fail to splice pre-mRNA. These and
            related data support the view that crooked neck is a
            phylogenetically conserved pre-mRNA splicing factor.
REFERENCE   8  (residues 1 to 564)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   9  (residues 1 to 564)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   10 (residues 1 to 564)
  AUTHORS   Lai,C.H., Chiu,J.Y. and Lin,W.
  TITLE     Identification of the human crooked neck gene by comparative gene
            identification
  JOURNAL   Biochim Biophys Acta 1517 (3), 449-454 (2001)
   PUBMED   11342225
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF318305.1, BC144222.1,
            AL832435.1 and AA255987.1.
            
            Summary: The crooked neck (crn) gene of Drosophila is essential for
            embryogenesis and is thought to be involved in cell cycle
            progression and pre-mRNA splicing. A protein encoded by this human
            locus has been found to localize to pre-mRNA splicing complexes in
            the nucleus and is necessary for pre-mRNA splicing. Alternatively
            spliced transcript variants have been described. [provided by
            RefSeq, Jul 2013].
            
            Transcript Variant: This variant (4) uses two alternate splice
            sites in the 5' UTR, compared to variant 1. These differences
            result in predicted translation initiation at a downstream in-frame
            start site through ribosomal re-initiation and/or leaky scanning.
            The encoded isoform (c) is shorter than isoform a. Both variants 3
            and 4 encode the same isoform (c).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF318305.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.23"
     Protein         1..564
                     /product="crooked neck-like protein 1 isoform c"
                     /note="crooked neck-like 1; crooked neck-like protein 1;
                     crooked neck homolog; Crn, crooked neck-like 1; SYF3
                     pre-mRNA-splicing factor; crooked neck pre-mRNA splicing
                     factor-like 1"
                     /calculated_mol_wt=68481
     Region          3..125
                     /region_name="BepA"
                     /note="Outer membrane protein chaperone/metalloprotease
                     BepA/YfgC, contains M48 and TPR domains [Cell
                     wall/membrane/envelope biogenesis, Posttranslational
                     modification, protein turnover, chaperones]; COG4783"
                     /db_xref="CDD:443813"
     Region          73..104
                     /region_name="HAT"
                     /note="HAT (Half-A-TPR) repeat; pfam02184"
                     /db_xref="CDD:111114"
     Region          196..440
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          289..317
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(290,293..294,297..298,300,323,326..327,330..331,
                     333..334,357,360..361,364..365,368)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          322..351
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          356..384
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..564
                     /gene="CRNKL1"
                     /gene_synonym="CLF; Clf1; CRN; HCRN; MGCH; MSTP021; SYF3"
                     /coded_by="NM_001278627.2:572..2266"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="GeneID:51340"
                     /db_xref="HGNC:HGNC:15762"
                     /db_xref="MIM:610952"
ORIGIN      
        1 memknrqvnh arniwdrait tlprvnqfwy kytymeemlg nvagarqvfe rwmewqpeeq
       61 awhsyinfel rykevdrart iyerfvlvhp dvknwikyar feekhayfah arkvyerave
      121 ffgdehmdeh lyvafakfee nqkefervrv iykyaldris kqdaqelfkn ytifekkfgd
      181 rrgiediivs krrfqyeeev kanphnydaw fdylrlvesd aeaeavrevy eraianvppi
      241 qekrhwkryi ylwinyalye eleakdpert rqvyqaslel iphkkftfak mwilyaqfei
      301 rqknlslarr algtsigkcp knklfkvyie lelqlrefdr crklyekfle fgpenctswi
      361 kfaeletilg didraraiye laisqprldm pevlwksyid feieqeeter trnlyrrllq
      421 rtqhvkvwis faqfelssgk egsltkcrqi yeeanktmrn ceekeerlml leswrsfeee
      481 fgtasdkerv dklmpekvkk rrkvqtddgs dagweeyfdy ifpedaanqp nlkllamakl
      541 wkkqqqeked aehhpdedvd eses
//
LOCUS       NP_001162588             599 aa            linear   PRI 18-DEC-2025
DEFINITION  stromal interaction molecule 2 isoform 3 precursor [Homo sapiens].
ACCESSION   NP_001162588
VERSION     NP_001162588.1
DBSOURCE    REFSEQ: accession NM_001169117.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Djordjevic,S., Itzykson,R., Hague,F., Lebon,D., Legrand,J.,
            Ouled-Haddou,H., Jedraszak,G., Harbonnier,J., Collet,L.,
            Paubelle,E., Marolleau,J.P., Garcon,L. and Boyer,T.
  TITLE     STIM2 is involved in the regulation of apoptosis and the cell cycle
            in normal and malignant monocytic cells
  JOURNAL   Mol Oncol 18 (6), 1571-1592 (2024)
   PUBMED   38234211
  REMARK    GeneRIF: STIM2 is involved in the regulation of apoptosis and the
            cell cycle in normal and malignant monocytic cells.
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 599)
  AUTHORS   Cheng,H., Chen,L., Fang,Z., Wan,Q., Du,Z., Ma,N., Guo,G. and Lu,W.
  TITLE     STIM2 promotes the invasion and metastasis of breast cancer cells
            through the NFAT1/TGF-beta1 pathway
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 67 (6), 55-61 (2022)
   PUBMED   35818214
  REMARK    GeneRIF: STIM2 promotes the invasion and metastasis of breast
            cancer cells through the NFAT1/TGF-beta1 pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 599)
  AUTHORS   Ahmad,M., Ong,H.L., Saadi,H., Son,G.Y., Shokatian,Z., Terry,L.E.,
            Trebak,M., Yule,D.I. and Ambudkar,I.
  TITLE     Functional communication between IP3R and STIM2 at subthreshold
            stimuli is a critical checkpoint for initiation of SOCE
  JOURNAL   Proc Natl Acad Sci U S A 119 (3) (2022)
   PUBMED   35022238
  REMARK    GeneRIF: Functional communication between IP3R and STIM2 at
            subthreshold stimuli is a critical checkpoint for initiation of
            SOCE.
REFERENCE   5  (residues 1 to 599)
  AUTHORS   Rana,A., Yen,M., Sadaghiani,A.M., Malmersjo,S., Park,C.Y.,
            Dolmetsch,R.E. and Lewis,R.S.
  TITLE     Alternative splicing converts STIM2 from an activator to an
            inhibitor of store-operated calcium channels
  JOURNAL   J Cell Biol 209 (5), 653-669 (2015)
   PUBMED   26033257
  REMARK    GeneRIF: STIM2beta does not by itself strongly bind Orai1, it is
            recruited to Orai1 channels by forming heterodimers with other STIM
            isoforms.
REFERENCE   6  (residues 1 to 599)
  AUTHORS   Miederer,A.M., Alansary,D., Schwar,G., Lee,P.H., Jung,M., Helms,V.
            and Niemeyer,B.A.
  TITLE     A STIM2 splice variant negatively regulates store-operated calcium
            entry
  JOURNAL   Nat Commun 6, 6899 (2015)
   PUBMED   25896806
  REMARK    GeneRIF: These results imply that the splice variant STIM2.1 is an
            additional player tuning Orai1 activation in vivo.
            GeneRIF: STIM2.1 cannot activate Orai1 due to splicing in residues
            within the channel-activating domain (CAD). STIM2.1 confers a
            calcium dependent dominant-negative function on both STIM1 and
            STIM2 (STIM2.2). Affinity of the STIM2.1 calmodulin binding site
            within the CAD domain is increased compared to STIM2.2.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 599)
  AUTHORS   Soboloff,J., Spassova,M.A., Hewavitharana,T., He,L.P., Xu,W.,
            Johnstone,L.S., Dziadek,M.A. and Gill,D.L.
  TITLE     STIM2 is an inhibitor of STIM1-mediated store-operated Ca2+ Entry
  JOURNAL   Curr Biol 16 (14), 1465-1470 (2006)
   PUBMED   16860747
  REMARK    GeneRIF: STIM2 is an inhibitor of store-operated channel (SOC)
            activation and plays a coordinated role with STIM1 in controlling
            SOC-mediated Ca(2+) entry signals.
REFERENCE   8  (residues 1 to 599)
  AUTHORS   Liou,J., Kim,M.L., Heo,W.D., Jones,J.T., Myers,J.W., Ferrell,J.E.
            Jr. and Meyer,T.
  TITLE     STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered
            Ca2+ influx
  JOURNAL   Curr Biol 15 (13), 1235-1241 (2005)
   PUBMED   16005298
  REMARK    GeneRIF: STIM proteins function as Ca(2+) store sensors in the
            signaling pathway connecting Ca(2+) store depletion to Ca(2+)
            influx.
REFERENCE   9  (residues 1 to 599)
  AUTHORS   Williams,R.T., Manji,S.S., Parker,N.J., Hancock,M.S., Van
            Stekelenburg,L., Eid,J.P., Senior,P.V., Kazenwadel,J.S.,
            Shandala,T., Saint,R., Smith,P.J. and Dziadek,M.A.
  TITLE     Identification and characterization of the STIM (stromal
            interaction molecule) gene family: coding for a novel class of
            transmembrane proteins
  JOURNAL   Biochem J 357 (Pt 3), 673-685 (2001)
   PUBMED   11463338
  REMARK    GeneRIF: Translation initiation from a non-AUG (UUG) start site.
REFERENCE   10 (residues 1 to 599)
  AUTHORS   Irvin,A.D., Young,E.R., Luther,P.D. and Collins,A.P.
  TITLE     Interspecific fusion of bovine and other cells with parainfluenza
            viruses (Sendai and Pi-3)
  JOURNAL   J Comp Pathol 87 (3), 393-404 (1977)
   PUBMED   198439
  REMARK    GeneRIF: STIM2 is involved in spatial learning and plays an
            important role in ischemic-induced neuronal cell death during brain
            hypoxia. The absence of STIM2 reduces life expectancy in mice by
            sudden death.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106047.5 and AC006928.15.
            
            Summary: This gene is a member of the stromal interaction molecule
            (STIM) family and likely arose, along with related family member
            STIM1, from a common ancestral gene. The encoded protein functions
            to regulate calcium concentrations in the cytosol and endoplasmic
            reticulum, and is involved in the activation of plasma membrane
            Orai Ca(2+) entry channels. This gene initiates translation from a
            non-AUG (UUG) start site. A signal peptide is cleaved from the
            resulting protein. Multiple transcript variants result from
            alternative splicing. [provided by RefSeq, Dec 2009].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon in the central coding region, and differs in the 3' coding
            region and 3' UTR, compared to variant 1. The resulting isoform (3)
            has a distinct C-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC152554.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:11463338)
            non-AUG initiation codon         :: PMID: 11463338
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.2"
     Protein         1..599
                     /product="stromal interaction molecule 2 isoform 3
                     precursor"
                     /calculated_mol_wt=66745
     sig_peptide     1..14
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1300
     mat_peptide     15..599
                     /product="stromal interaction molecule 2 isoform 3"
                     /calculated_mol_wt=66745
     Region          132..205
                     /region_name="SAM_STIM2"
                     /note="SAM domain of STIM2 subfamily proteins; cd09574"
                     /db_xref="CDD:188973"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            order(136,156,167,183,196,202)
                     /site_type="other"
                     /note="putative oligomer interface [polypeptide binding]"
                     /db_xref="CDD:188973"
     Site            219..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P246.2)"
     Region          <250..>340
                     /region_name="PRK00409"
                     /note="recombination and DNA strand exchange inhibitor
                     protein; Reviewed"
                     /db_xref="CDD:234750"
     Region          346..445
                     /region_name="SOAR"
                     /note="STIM1 Orai1-activating region; pfam16533"
                     /db_xref="CDD:465164"
     Region          483..562
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     CDS             1..599
                     /gene="STIM2"
                     /coded_by="NM_001169117.2:379..2178"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3; non-AUG (UUG) translation initiation codon"
                     /db_xref="CCDS:CCDS54752.1"
                     /db_xref="GeneID:57620"
                     /db_xref="HGNC:HGNC:19205"
                     /db_xref="MIM:610841"
ORIGIN      
        1 mlvlgllvag aadgcelvpr hlrgrratgs aataasspaa aagdspalmt dpcmslsppc
       61 fteedrfsle alqtihkqmd ddkdggieve esdefiredm kykdatnkhs hlhredkhit
      121 iedlwkrwkt sevhnwtled tlqwliefve lpqyeknfrd nnvkgttlpr iavhepsfmi
      181 sqlkisdrsh rqklqlkald vvlfgpltrp phnwmkdfil tvsivigvgg cwfaytqnkt
      241 skehvakmmk dleslqtaeq slmdlqerle kaqeenrnva vekqnlerkm mdeinyakee
      301 acrlrelreg aecelsrrqy aeqeleqvrm alkkaekefe lrsswsvpda lqkwlqlthe
      361 vevqyynikr qnaemqlaia kdeaekikkk rstvfgtlhv ahsssldevd hkileakkal
      421 selttclrer lfrwqqieki cgfqiahnsg lpsltsslys dhswvvmprv sippypiagg
      481 vddldedtpp ivsqfpgtma kppgslarss slcrsrrsiv psspqpqraq laphaphpsh
      541 prhphhpqht phslpspdpd ilsvsscpal yrneeeeeai yfsaekqcih lglgackse
//
LOCUS       NP_001162589             754 aa            linear   PRI 18-DEC-2025
DEFINITION  stromal interaction molecule 2 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001162589
VERSION     NP_001162589.1
DBSOURCE    REFSEQ: accession NM_001169118.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Djordjevic,S., Itzykson,R., Hague,F., Lebon,D., Legrand,J.,
            Ouled-Haddou,H., Jedraszak,G., Harbonnier,J., Collet,L.,
            Paubelle,E., Marolleau,J.P., Garcon,L. and Boyer,T.
  TITLE     STIM2 is involved in the regulation of apoptosis and the cell cycle
            in normal and malignant monocytic cells
  JOURNAL   Mol Oncol 18 (6), 1571-1592 (2024)
   PUBMED   38234211
  REMARK    GeneRIF: STIM2 is involved in the regulation of apoptosis and the
            cell cycle in normal and malignant monocytic cells.
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Cheng,H., Chen,L., Fang,Z., Wan,Q., Du,Z., Ma,N., Guo,G. and Lu,W.
  TITLE     STIM2 promotes the invasion and metastasis of breast cancer cells
            through the NFAT1/TGF-beta1 pathway
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 67 (6), 55-61 (2022)
   PUBMED   35818214
  REMARK    GeneRIF: STIM2 promotes the invasion and metastasis of breast
            cancer cells through the NFAT1/TGF-beta1 pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 754)
  AUTHORS   Ahmad,M., Ong,H.L., Saadi,H., Son,G.Y., Shokatian,Z., Terry,L.E.,
            Trebak,M., Yule,D.I. and Ambudkar,I.
  TITLE     Functional communication between IP3R and STIM2 at subthreshold
            stimuli is a critical checkpoint for initiation of SOCE
  JOURNAL   Proc Natl Acad Sci U S A 119 (3) (2022)
   PUBMED   35022238
  REMARK    GeneRIF: Functional communication between IP3R and STIM2 at
            subthreshold stimuli is a critical checkpoint for initiation of
            SOCE.
REFERENCE   5  (residues 1 to 754)
  AUTHORS   Rana,A., Yen,M., Sadaghiani,A.M., Malmersjo,S., Park,C.Y.,
            Dolmetsch,R.E. and Lewis,R.S.
  TITLE     Alternative splicing converts STIM2 from an activator to an
            inhibitor of store-operated calcium channels
  JOURNAL   J Cell Biol 209 (5), 653-669 (2015)
   PUBMED   26033257
  REMARK    GeneRIF: STIM2beta does not by itself strongly bind Orai1, it is
            recruited to Orai1 channels by forming heterodimers with other STIM
            isoforms.
REFERENCE   6  (residues 1 to 754)
  AUTHORS   Miederer,A.M., Alansary,D., Schwar,G., Lee,P.H., Jung,M., Helms,V.
            and Niemeyer,B.A.
  TITLE     A STIM2 splice variant negatively regulates store-operated calcium
            entry
  JOURNAL   Nat Commun 6, 6899 (2015)
   PUBMED   25896806
  REMARK    GeneRIF: These results imply that the splice variant STIM2.1 is an
            additional player tuning Orai1 activation in vivo.
            GeneRIF: STIM2.1 cannot activate Orai1 due to splicing in residues
            within the channel-activating domain (CAD). STIM2.1 confers a
            calcium dependent dominant-negative function on both STIM1 and
            STIM2 (STIM2.2). Affinity of the STIM2.1 calmodulin binding site
            within the CAD domain is increased compared to STIM2.2.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 754)
  AUTHORS   Soboloff,J., Spassova,M.A., Hewavitharana,T., He,L.P., Xu,W.,
            Johnstone,L.S., Dziadek,M.A. and Gill,D.L.
  TITLE     STIM2 is an inhibitor of STIM1-mediated store-operated Ca2+ Entry
  JOURNAL   Curr Biol 16 (14), 1465-1470 (2006)
   PUBMED   16860747
  REMARK    GeneRIF: STIM2 is an inhibitor of store-operated channel (SOC)
            activation and plays a coordinated role with STIM1 in controlling
            SOC-mediated Ca(2+) entry signals.
REFERENCE   8  (residues 1 to 754)
  AUTHORS   Liou,J., Kim,M.L., Heo,W.D., Jones,J.T., Myers,J.W., Ferrell,J.E.
            Jr. and Meyer,T.
  TITLE     STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered
            Ca2+ influx
  JOURNAL   Curr Biol 15 (13), 1235-1241 (2005)
   PUBMED   16005298
  REMARK    GeneRIF: STIM proteins function as Ca(2+) store sensors in the
            signaling pathway connecting Ca(2+) store depletion to Ca(2+)
            influx.
REFERENCE   9  (residues 1 to 754)
  AUTHORS   Williams,R.T., Manji,S.S., Parker,N.J., Hancock,M.S., Van
            Stekelenburg,L., Eid,J.P., Senior,P.V., Kazenwadel,J.S.,
            Shandala,T., Saint,R., Smith,P.J. and Dziadek,M.A.
  TITLE     Identification and characterization of the STIM (stromal
            interaction molecule) gene family: coding for a novel class of
            transmembrane proteins
  JOURNAL   Biochem J 357 (Pt 3), 673-685 (2001)
   PUBMED   11463338
  REMARK    GeneRIF: Translation initiation from a non-AUG (UUG) start site.
REFERENCE   10 (residues 1 to 754)
  AUTHORS   Irvin,A.D., Young,E.R., Luther,P.D. and Collins,A.P.
  TITLE     Interspecific fusion of bovine and other cells with parainfluenza
            viruses (Sendai and Pi-3)
  JOURNAL   J Comp Pathol 87 (3), 393-404 (1977)
   PUBMED   198439
  REMARK    GeneRIF: STIM2 is involved in spatial learning and plays an
            important role in ischemic-induced neuronal cell death during brain
            hypoxia. The absence of STIM2 reduces life expectancy in mice by
            sudden death.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106047.5 and AC006928.15.
            
            Summary: This gene is a member of the stromal interaction molecule
            (STIM) family and likely arose, along with related family member
            STIM1, from a common ancestral gene. The encoded protein functions
            to regulate calcium concentrations in the cytosol and endoplasmic
            reticulum, and is involved in the activation of plasma membrane
            Orai Ca(2+) entry channels. This gene initiates translation from a
            non-AUG (UUG) start site. A signal peptide is cleaved from the
            resulting protein. Multiple transcript variants result from
            alternative splicing. [provided by RefSeq, Dec 2009].
            
            Transcript Variant: This variant (1, also known as STIM2.1 or
            STIM2beta) encodes the longest isoform (1). This isoform functions
            as a negative regulator of store-operated calcium entry (SOCE).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK096846.1, SRR1660805.25422.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:11463338)
            non-AUG initiation codon         :: PMID: 11463338
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.2"
     Protein         1..754
                     /product="stromal interaction molecule 2 isoform 1
                     precursor"
                     /calculated_mol_wt=83536
     sig_peptide     1..14
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1300
     mat_peptide     15..754
                     /product="stromal interaction molecule 2 isoform 1"
                     /calculated_mol_wt=83536
     Region          132..205
                     /region_name="SAM_STIM2"
                     /note="SAM domain of STIM2 subfamily proteins; cd09574"
                     /db_xref="CDD:188973"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            order(136,156,167,183,196,202)
                     /site_type="other"
                     /note="putative oligomer interface [polypeptide binding]"
                     /db_xref="CDD:188973"
     Site            219..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P246.2)"
     Region          <250..430
                     /region_name="PRK00409"
                     /note="recombination and DNA strand exchange inhibitor
                     protein; Reviewed"
                     /db_xref="CDD:234750"
     Region          346..453
                     /region_name="SOAR"
                     /note="STIM1 Orai1-activating region; pfam16533"
                     /db_xref="CDD:465164"
     Region          491..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            617
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            629
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P83093; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            658
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P83093; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            669
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            673
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Region          693..754
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            705
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     CDS             1..754
                     /gene="STIM2"
                     /coded_by="NM_001169118.2:379..2643"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1; non-AUG (UUG) translation initiation codon"
                     /db_xref="CCDS:CCDS54751.1"
                     /db_xref="GeneID:57620"
                     /db_xref="HGNC:HGNC:19205"
                     /db_xref="MIM:610841"
ORIGIN      
        1 mlvlgllvag aadgcelvpr hlrgrratgs aataasspaa aagdspalmt dpcmslsppc
       61 fteedrfsle alqtihkqmd ddkdggieve esdefiredm kykdatnkhs hlhredkhit
      121 iedlwkrwkt sevhnwtled tlqwliefve lpqyeknfrd nnvkgttlpr iavhepsfmi
      181 sqlkisdrsh rqklqlkald vvlfgpltrp phnwmkdfil tvsivigvgg cwfaytqnkt
      241 skehvakmmk dleslqtaeq slmdlqerle kaqeenrnva vekqnlerkm mdeinyakee
      301 acrlrelreg aecelsrrqy aeqeleqvrm alkkaekefe lrsswsvpda lqkwlqlthe
      361 vevqyynikr qnaemqlaia kdevaasyli qaekikkkrs tvfgtlhvah sssldevdhk
      421 ileakkalse lttclrerlf rwqqiekicg fqiahnsglp sltsslysdh swvvmprvsi
      481 ppypiaggvd dldedtppiv sqfpgtmakp pgslarsssl crsrrsivps spqpqraqla
      541 phaphpshpr hphhpqhtph slpspdpdil svsscpalyr neeeeeaiyf saekqwevpd
      601 tasecdslns sigrkqsppl sleiyqtlsp rkisrdevsl edssrgdspv tvdvswgspd
      661 cvgltetksm ifspaskvyn gilekscsmn qlssgipvpk prhtscssag ndskpvqeap
      721 svarissiph dlchngeksk kpskikslfk kksk
//
LOCUS       NP_065911                746 aa            linear   PRI 18-DEC-2025
DEFINITION  stromal interaction molecule 2 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_065911
VERSION     NP_065911.3
DBSOURCE    REFSEQ: accession NM_020860.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Djordjevic,S., Itzykson,R., Hague,F., Lebon,D., Legrand,J.,
            Ouled-Haddou,H., Jedraszak,G., Harbonnier,J., Collet,L.,
            Paubelle,E., Marolleau,J.P., Garcon,L. and Boyer,T.
  TITLE     STIM2 is involved in the regulation of apoptosis and the cell cycle
            in normal and malignant monocytic cells
  JOURNAL   Mol Oncol 18 (6), 1571-1592 (2024)
   PUBMED   38234211
  REMARK    GeneRIF: STIM2 is involved in the regulation of apoptosis and the
            cell cycle in normal and malignant monocytic cells.
REFERENCE   2  (residues 1 to 746)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 746)
  AUTHORS   Cheng,H., Chen,L., Fang,Z., Wan,Q., Du,Z., Ma,N., Guo,G. and Lu,W.
  TITLE     STIM2 promotes the invasion and metastasis of breast cancer cells
            through the NFAT1/TGF-beta1 pathway
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 67 (6), 55-61 (2022)
   PUBMED   35818214
  REMARK    GeneRIF: STIM2 promotes the invasion and metastasis of breast
            cancer cells through the NFAT1/TGF-beta1 pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 746)
  AUTHORS   Ahmad,M., Ong,H.L., Saadi,H., Son,G.Y., Shokatian,Z., Terry,L.E.,
            Trebak,M., Yule,D.I. and Ambudkar,I.
  TITLE     Functional communication between IP3R and STIM2 at subthreshold
            stimuli is a critical checkpoint for initiation of SOCE
  JOURNAL   Proc Natl Acad Sci U S A 119 (3) (2022)
   PUBMED   35022238
  REMARK    GeneRIF: Functional communication between IP3R and STIM2 at
            subthreshold stimuli is a critical checkpoint for initiation of
            SOCE.
REFERENCE   5  (residues 1 to 746)
  AUTHORS   Rana,A., Yen,M., Sadaghiani,A.M., Malmersjo,S., Park,C.Y.,
            Dolmetsch,R.E. and Lewis,R.S.
  TITLE     Alternative splicing converts STIM2 from an activator to an
            inhibitor of store-operated calcium channels
  JOURNAL   J Cell Biol 209 (5), 653-669 (2015)
   PUBMED   26033257
  REMARK    GeneRIF: STIM2beta does not by itself strongly bind Orai1, it is
            recruited to Orai1 channels by forming heterodimers with other STIM
            isoforms.
REFERENCE   6  (residues 1 to 746)
  AUTHORS   Miederer,A.M., Alansary,D., Schwar,G., Lee,P.H., Jung,M., Helms,V.
            and Niemeyer,B.A.
  TITLE     A STIM2 splice variant negatively regulates store-operated calcium
            entry
  JOURNAL   Nat Commun 6, 6899 (2015)
   PUBMED   25896806
  REMARK    GeneRIF: These results imply that the splice variant STIM2.1 is an
            additional player tuning Orai1 activation in vivo.
            GeneRIF: STIM2.1 cannot activate Orai1 due to splicing in residues
            within the channel-activating domain (CAD). STIM2.1 confers a
            calcium dependent dominant-negative function on both STIM1 and
            STIM2 (STIM2.2). Affinity of the STIM2.1 calmodulin binding site
            within the CAD domain is increased compared to STIM2.2.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 746)
  AUTHORS   Soboloff,J., Spassova,M.A., Hewavitharana,T., He,L.P., Xu,W.,
            Johnstone,L.S., Dziadek,M.A. and Gill,D.L.
  TITLE     STIM2 is an inhibitor of STIM1-mediated store-operated Ca2+ Entry
  JOURNAL   Curr Biol 16 (14), 1465-1470 (2006)
   PUBMED   16860747
  REMARK    GeneRIF: STIM2 is an inhibitor of store-operated channel (SOC)
            activation and plays a coordinated role with STIM1 in controlling
            SOC-mediated Ca(2+) entry signals.
REFERENCE   8  (residues 1 to 746)
  AUTHORS   Liou,J., Kim,M.L., Heo,W.D., Jones,J.T., Myers,J.W., Ferrell,J.E.
            Jr. and Meyer,T.
  TITLE     STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered
            Ca2+ influx
  JOURNAL   Curr Biol 15 (13), 1235-1241 (2005)
   PUBMED   16005298
  REMARK    GeneRIF: STIM proteins function as Ca(2+) store sensors in the
            signaling pathway connecting Ca(2+) store depletion to Ca(2+)
            influx.
REFERENCE   9  (residues 1 to 746)
  AUTHORS   Williams,R.T., Manji,S.S., Parker,N.J., Hancock,M.S., Van
            Stekelenburg,L., Eid,J.P., Senior,P.V., Kazenwadel,J.S.,
            Shandala,T., Saint,R., Smith,P.J. and Dziadek,M.A.
  TITLE     Identification and characterization of the STIM (stromal
            interaction molecule) gene family: coding for a novel class of
            transmembrane proteins
  JOURNAL   Biochem J 357 (Pt 3), 673-685 (2001)
   PUBMED   11463338
  REMARK    GeneRIF: Translation initiation from a non-AUG (UUG) start site.
REFERENCE   10 (residues 1 to 746)
  AUTHORS   Irvin,A.D., Young,E.R., Luther,P.D. and Collins,A.P.
  TITLE     Interspecific fusion of bovine and other cells with parainfluenza
            viruses (Sendai and Pi-3)
  JOURNAL   J Comp Pathol 87 (3), 393-404 (1977)
   PUBMED   198439
  REMARK    GeneRIF: STIM2 is involved in spatial learning and plays an
            important role in ischemic-induced neuronal cell death during brain
            hypoxia. The absence of STIM2 reduces life expectancy in mice by
            sudden death.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106047.5 and AC006928.15.
            
            On Dec 15, 2009 this sequence version replaced NP_065911.2.
            
            Summary: This gene is a member of the stromal interaction molecule
            (STIM) family and likely arose, along with related family member
            STIM1, from a common ancestral gene. The encoded protein functions
            to regulate calcium concentrations in the cytosol and endoplasmic
            reticulum, and is involved in the activation of plasma membrane
            Orai Ca(2+) entry channels. This gene initiates translation from a
            non-AUG (UUG) start site. A signal peptide is cleaved from the
            resulting protein. Multiple transcript variants result from
            alternative splicing. [provided by RefSeq, Dec 2009].
            
            Transcript Variant: This variant (2, also known as STIM2.2 or
            STIM2alpha) lacks an alternate in-frame exon in the central coding
            region, compared to variant 1, resulting in an isoform (2) that is
            shorter than isoform 1. This isoform functions as a positive
            regulator of store-operated calcium entry (SOCE).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB040915.1, SRR1803617.151765.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:11463338)
            MANE Ensembl match               :: ENST00000467087.7/
                                                ENSP00000419073.2
            non-AUG initiation codon         :: PMID: 11463338
            RefSeq Select criteria           :: based on conservation,
                                                expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.2"
     Protein         1..746
                     /product="stromal interaction molecule 2 isoform 2
                     precursor"
                     /calculated_mol_wt=82690
     sig_peptide     1..14
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1300
     mat_peptide     15..746
                     /product="stromal interaction molecule 2 isoform 2"
                     /calculated_mol_wt=82690
     Region          132..205
                     /region_name="SAM_STIM2"
                     /note="SAM domain of STIM2 subfamily proteins; cd09574"
                     /db_xref="CDD:188973"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            order(136,156,167,183,196,202)
                     /site_type="other"
                     /note="putative oligomer interface [polypeptide binding]"
                     /db_xref="CDD:188973"
     Site            219..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P246.2)"
     Region          <250..>340
                     /region_name="PRK00409"
                     /note="recombination and DNA strand exchange inhibitor
                     protein; Reviewed"
                     /db_xref="CDD:234750"
     Region          346..445
                     /region_name="SOAR"
                     /note="STIM1 Orai1-activating region; pfam16533"
                     /db_xref="CDD:465164"
     Region          483..562
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            609
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P83093; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P83093; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            665
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            680
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     Region          685..746
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P246.2)"
     Site            697
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P246.2)"
     CDS             1..746
                     /gene="STIM2"
                     /coded_by="NM_020860.4:379..2619"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2; non-AUG (UUG) translation initiation codon"
                     /db_xref="CCDS:CCDS3440.2"
                     /db_xref="GeneID:57620"
                     /db_xref="HGNC:HGNC:19205"
                     /db_xref="MIM:610841"
ORIGIN      
        1 mlvlgllvag aadgcelvpr hlrgrratgs aataasspaa aagdspalmt dpcmslsppc
       61 fteedrfsle alqtihkqmd ddkdggieve esdefiredm kykdatnkhs hlhredkhit
      121 iedlwkrwkt sevhnwtled tlqwliefve lpqyeknfrd nnvkgttlpr iavhepsfmi
      181 sqlkisdrsh rqklqlkald vvlfgpltrp phnwmkdfil tvsivigvgg cwfaytqnkt
      241 skehvakmmk dleslqtaeq slmdlqerle kaqeenrnva vekqnlerkm mdeinyakee
      301 acrlrelreg aecelsrrqy aeqeleqvrm alkkaekefe lrsswsvpda lqkwlqlthe
      361 vevqyynikr qnaemqlaia kdeaekikkk rstvfgtlhv ahsssldevd hkileakkal
      421 selttclrer lfrwqqieki cgfqiahnsg lpsltsslys dhswvvmprv sippypiagg
      481 vddldedtpp ivsqfpgtma kppgslarss slcrsrrsiv psspqpqraq laphaphpsh
      541 prhphhpqht phslpspdpd ilsvsscpal yrneeeeeai yfsaekqwev pdtasecdsl
      601 nssigrkqsp plsleiyqtl sprkisrdev sledssrgds pvtvdvswgs pdcvgltetk
      661 smifspaskv yngilekscs mnqlssgipv pkprhtscss agndskpvqe apsvarissi
      721 phdlchngek skkpskiksl fkkksk
//
LOCUS       NP_258257                319 aa            linear   PRI 19-DEC-2025
DEFINITION  multivesicular body subunit 12B isoform 1 [Homo sapiens].
ACCESSION   NP_258257 XP_088525
VERSION     NP_258257.1
DBSOURCE    REFSEQ: accession NM_033446.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Flower,T.G., Takahashi,Y., Hudait,A., Rose,K., Tjahjono,N.,
            Pak,A.J., Yokom,A.L., Liang,X., Wang,H.G., Bouamr,F., Voth,G.A. and
            Hurley,J.H.
  TITLE     A helical assembly of human ESCRT-I scaffolds reverse-topology
            membrane scission
  JOURNAL   Nat Struct Mol Biol 27 (6), 570-580 (2020)
   PUBMED   32424346
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Nag,A., Venturini,C., Small,K.S., Young,T.L., Viswanathan,A.C.,
            Mackey,D.A., Hysi,P.G. and Hammond,C.
  CONSRTM   International Glaucoma Genetics Consortium
  TITLE     A genome-wide association study of intra-ocular pressure suggests a
            novel association in the gene FAM125B in the TwinsUK cohort
  JOURNAL   Hum Mol Genet 23 (12), 3343-3348 (2014)
   PUBMED   24518671
  REMARK    GeneRIF: Study suggests a novel association between SNPs in FAM125B
            andintra-ocular pressure in the TwinsUK cohort.
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Letra,A., Menezes,R., Govil,M., Fonseca,R.F., McHenry,T.,
            Granjeiro,J.M., Castilla,E.E., Orioli,I.M., Marazita,M.L. and
            Vieira,A.R.
  TITLE     Follow-up association studies of chromosome region 9q and
            nonsyndromic cleft lip/palate
  JOURNAL   Am J Med Genet A 152A (7), 1701-1710 (2010)
   PUBMED   20583170
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   8  (residues 1 to 319)
  AUTHORS   Audhya,A., McLeod,I.X., Yates,J.R. and Oegema,K.
  TITLE     MVB-12, a fourth subunit of metazoan ESCRT-I, functions in receptor
            downregulation
  JOURNAL   PLoS One 2 (9), e956 (2007)
   PUBMED   17895996
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 319)
  AUTHORS   Morita,E., Sandrin,V., Alam,S.L., Eckert,D.M., Gygi,S.P. and
            Sundquist,W.I.
  TITLE     Identification of human MVB12 proteins as ESCRT-I subunits that
            function in HIV budding
  JOURNAL   Cell Host Microbe 2 (1), 41-53 (2007)
   PUBMED   18005716
REFERENCE   10 (residues 1 to 319)
  AUTHORS   Hattori,A., Okumura,K., Nagase,T., Kikuno,R., Hirosawa,M. and
            Ohara,O.
  TITLE     Characterization of long cDNA clones from human adult spleen
  JOURNAL   DNA Res 7 (6), 357-366 (2000)
   PUBMED   11214971
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006443.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 9, 2005 this sequence version replaced XP_088525.5.
            
            Summary: The protein encoded by this gene is a component of the
            ESCRT-I complex, a heterotetramer, which mediates the sorting of
            ubiquitinated cargo protein from the plasma membrane to the
            endosomal vesicle. ESCRT-I complex plays an essential role in HIV
            budding and endosomal protein sorting. Depletion and overexpression
            of this and related protein (MVB12A) inhibit HIV-1 infectivity and
            induce unusual viral assembly defects, indicating a role for MVB12
            subunits in regulating ESCRT-mediated virus budding. Alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK024432.1, SRR1803611.109826.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361171.8/ ENSP00000354772.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..319
                     /product="multivesicular body subunit 12B isoform 1"
                     /note="ESCRT-I complex subunit MVB12B; family with
                     sequence similarity 125, member B"
                     /calculated_mol_wt=35489
     Region          1..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H7P6.2)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18005716; propagated from
                     UniProtKB/Swiss-Prot (Q9H7P6.2)"
     Region          48..299
                     /region_name="DUF2464"
                     /note="Multivesicular body subunit 12; pfam10240"
                     /db_xref="CDD:463017"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18005716; propagated from
                     UniProtKB/Swiss-Prot (Q9H7P6.2)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:18005716; propagated from
                     UniProtKB/Swiss-Prot (Q9H7P6.2)"
     Region          195..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H7P6.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:18005716; propagated from
                     UniProtKB/Swiss-Prot (Q9H7P6.2)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:18005716; propagated from
                     UniProtKB/Swiss-Prot (Q9H7P6.2)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6KAU4; propagated from
                     UniProtKB/Swiss-Prot (Q9H7P6.2)"
     Region          299..319
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H7P6.2)"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18005716; propagated from
                     UniProtKB/Swiss-Prot (Q9H7P6.2)"
     CDS             1..319
                     /gene="MVB12B"
                     /gene_synonym="C9orf28; FAM125B"
                     /coded_by="NM_033446.3:102..1061"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS35142.1"
                     /db_xref="GeneID:89853"
                     /db_xref="HGNC:HGNC:23368"
                     /db_xref="MIM:621454"
ORIGIN      
        1 mrscfcvrrs rdppppqppp pppqrgtdqs tmpevkdlse alpetsmdpi tgvgvvasrn
       61 raptgydvva qtadgvdadl wkdglfkskv trylcftrsf skenshlgnv lvdmklidik
      121 dtlpvgfipi qetvdtqeva frkkrlcikf iprdsteaai cdirimgrtk qappqytfig
      181 elnsmgiwyr mgrvprnhds sqpttpsqss aastpapnlp rhisltlpat frgrnstrtd
      241 yeyqhsnlya isamdgvpfm isekfscvpe smqpfdllgi tikslaeiek eyeysfrteq
      301 saaarlppsp trcqqipqs
//
LOCUS       NP_612410                273 aa            linear   PRI 19-DEC-2025
DEFINITION  multivesicular body subunit 12A isoform 1 [Homo sapiens].
ACCESSION   NP_612410
VERSION     NP_612410.1
DBSOURCE    REFSEQ: accession NM_138401.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Flower,T.G., Takahashi,Y., Hudait,A., Rose,K., Tjahjono,N.,
            Pak,A.J., Yokom,A.L., Liang,X., Wang,H.G., Bouamr,F., Voth,G.A. and
            Hurley,J.H.
  TITLE     A helical assembly of human ESCRT-I scaffolds reverse-topology
            membrane scission
  JOURNAL   Nat Struct Mol Biol 27 (6), 570-580 (2020)
   PUBMED   32424346
  REMARK    GeneRIF: A helical assembly of human ESCRT-I scaffolds
            reverse-topology membrane scission.
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Boura,E. and Hurley,J.H.
  TITLE     Structural basis for membrane targeting by the MVB12-associated
            beta-prism domain of the human ESCRT-I MVB12 subunit
  JOURNAL   Proc Natl Acad Sci U S A 109 (6), 1901-1906 (2012)
   PUBMED   22232651
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Tsunematsu,T., Yamauchi,E., Shibata,H., Maki,M., Ohta,T. and
            Konishi,H.
  TITLE     Distinct functions of human MVB12A and MVB12B in the ESCRT-I
            dependent on their posttranslational modifications
  JOURNAL   Biochem Biophys Res Commun 399 (2), 232-237 (2010)
   PUBMED   20654576
  REMARK    GeneRIF: These results suggest that the expression of MVB12B may be
            normally suppressed through the ubiquitin-proteasome pathway that
            simultaneously regulates the fate of MVB12A and the functions of
            ESCRT-I.
            Erratum:[Biochem Biophys Res Commun. 2011 Mar 4;406(1):158-9]
REFERENCE   7  (residues 1 to 273)
  AUTHORS   Hurley,J.H. and Hanson,P.I.
  TITLE     Membrane budding and scission by the ESCRT machinery: it's all in
            the neck
  JOURNAL   Nat Rev Mol Cell Biol 11 (8), 556-566 (2010)
   PUBMED   20588296
  REMARK    Review article
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Morita,E., Sandrin,V., Alam,S.L., Eckert,D.M., Gygi,S.P. and
            Sundquist,W.I.
  TITLE     Identification of human MVB12 proteins as ESCRT-I subunits that
            function in HIV budding
  JOURNAL   Cell Host Microbe 2 (1), 41-53 (2007)
   PUBMED   18005716
REFERENCE   9  (residues 1 to 273)
  AUTHORS   Konishi,H., Tashiro,K., Murata,Y., Nabeshi,H., Yamauchi,E. and
            Taniguchi,H.
  TITLE     CFBP is a novel tyrosine-phosphorylated protein that might function
            as a regulator of CIN85/CD2AP
  JOURNAL   J Biol Chem 281 (39), 28919-28931 (2006)
   PUBMED   16895919
  REMARK    GeneRIF: CFBP is a novel tyrosine-phosphorylated protein that might
            function as a regulator of CIN85/CD2AP
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Wistow,G., Bernstein,S.L., Ray,S., Wyatt,M.K., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human iris for the NEIBank
            Project: steroid-response factors and similarities with retinal
            pigment epithelium
  JOURNAL   Mol Vis 8, 185-195 (2002)
   PUBMED   12107412
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CD672349.1, BC011840.2 and BP394542.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK289487.1, SRR1163655.242545.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000317040.12/ ENSP00000324810.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..273
                     /product="multivesicular body subunit 12A isoform 1"
                     /note="CIN85/CD2AP family binding protein; ESCRT-I complex
                     subunit MVB12A; family with sequence similarity 125,
                     member A"
                     /calculated_mol_wt=28652
     Region          11..261
                     /region_name="DUF2464"
                     /note="Multivesicular body subunit 12; pfam10240"
                     /db_xref="CDD:463017"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:18005716; propagated from
                     UniProtKB/Swiss-Prot (Q96EY5.1)"
     Region          155..160
                     /region_name="SH3-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EY5.1)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18005716; propagated from
                     UniProtKB/Swiss-Prot (Q96EY5.1)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18005716,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96EY5.1)"
     Region          192..273
                     /region_name="Interaction with TSG101, VPS37B and VPS28.
                     /evidence=ECO:0000269|PubMed:18005716"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EY5.1)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96EY5.1)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96EY5.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:16895919; propagated from
                     UniProtKB/Swiss-Prot (Q96EY5.1)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18005716; propagated from
                     UniProtKB/Swiss-Prot (Q96EY5.1)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18005716; propagated from
                     UniProtKB/Swiss-Prot (Q96EY5.1)"
     CDS             1..273
                     /gene="MVB12A"
                     /gene_synonym="CFBP; FAM125A"
                     /coded_by="NM_138401.4:90..911"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12359.1"
                     /db_xref="GeneID:93343"
                     /db_xref="HGNC:HGNC:25153"
                     /db_xref="MIM:621453"
ORIGIN      
        1 mdpvpgtdsa plaglawssa sappprgfsa isctvegapa sfgksfaqks gyflclsslg
       61 slenpqenvv adiqivvdks plplgfspvc dpmdskasvs kkkrmcvkll plgatdtavf
      121 dvrlsgktkt vpgylrigdm ggfaiwckka kaprpvpkpr glsrdmqgls ldaasqpskg
      181 gllertasrl gsrastlrrn dsiyeassly gisamdgvpf tlhprfegks csplafsafg
      241 dltiksladi eeeynygfvv ektaaarlpp svs
//
LOCUS       NP_001011703             221 aa            linear   PRI 19-DEC-2025
DEFINITION  multivesicular body subunit 12B isoform 2 [Homo sapiens].
ACCESSION   NP_001011703
VERSION     NP_001011703.1
DBSOURCE    REFSEQ: accession NM_001011703.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Flower,T.G., Takahashi,Y., Hudait,A., Rose,K., Tjahjono,N.,
            Pak,A.J., Yokom,A.L., Liang,X., Wang,H.G., Bouamr,F., Voth,G.A. and
            Hurley,J.H.
  TITLE     A helical assembly of human ESCRT-I scaffolds reverse-topology
            membrane scission
  JOURNAL   Nat Struct Mol Biol 27 (6), 570-580 (2020)
   PUBMED   32424346
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Nag,A., Venturini,C., Small,K.S., Young,T.L., Viswanathan,A.C.,
            Mackey,D.A., Hysi,P.G. and Hammond,C.
  CONSRTM   International Glaucoma Genetics Consortium
  TITLE     A genome-wide association study of intra-ocular pressure suggests a
            novel association in the gene FAM125B in the TwinsUK cohort
  JOURNAL   Hum Mol Genet 23 (12), 3343-3348 (2014)
   PUBMED   24518671
  REMARK    GeneRIF: Study suggests a novel association between SNPs in FAM125B
            andintra-ocular pressure in the TwinsUK cohort.
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Letra,A., Menezes,R., Govil,M., Fonseca,R.F., McHenry,T.,
            Granjeiro,J.M., Castilla,E.E., Orioli,I.M., Marazita,M.L. and
            Vieira,A.R.
  TITLE     Follow-up association studies of chromosome region 9q and
            nonsyndromic cleft lip/palate
  JOURNAL   Am J Med Genet A 152A (7), 1701-1710 (2010)
   PUBMED   20583170
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 221)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   8  (residues 1 to 221)
  AUTHORS   Audhya,A., McLeod,I.X., Yates,J.R. and Oegema,K.
  TITLE     MVB-12, a fourth subunit of metazoan ESCRT-I, functions in receptor
            downregulation
  JOURNAL   PLoS One 2 (9), e956 (2007)
   PUBMED   17895996
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 221)
  AUTHORS   Morita,E., Sandrin,V., Alam,S.L., Eckert,D.M., Gygi,S.P. and
            Sundquist,W.I.
  TITLE     Identification of human MVB12 proteins as ESCRT-I subunits that
            function in HIV budding
  JOURNAL   Cell Host Microbe 2 (1), 41-53 (2007)
   PUBMED   18005716
REFERENCE   10 (residues 1 to 221)
  AUTHORS   Hattori,A., Okumura,K., Nagase,T., Kikuno,R., Hirosawa,M. and
            Ohara,O.
  TITLE     Characterization of long cDNA clones from human adult spleen
  JOURNAL   DNA Res 7 (6), 357-366 (2000)
   PUBMED   11214971
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006443.1, DA339911.1,
            BC028675.1, BC000122.1 and BC041601.1.
            
            Summary: The protein encoded by this gene is a component of the
            ESCRT-I complex, a heterotetramer, which mediates the sorting of
            ubiquitinated cargo protein from the plasma membrane to the
            endosomal vesicle. ESCRT-I complex plays an essential role in HIV
            budding and endosomal protein sorting. Depletion and overexpression
            of this and related protein (MVB12A) inhibit HIV-1 infectivity and
            induce unusual viral assembly defects, indicating a role for MVB12
            subunits in regulating ESCRT-mediated virus budding. Alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (2) differs at the 3' end compared
            to variant 1. This results in a shorter isoform (2) with a distinct
            C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028675.1, SRR1803615.161663.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..221
                     /product="multivesicular body subunit 12B isoform 2"
                     /note="ESCRT-I complex subunit MVB12B; family with
                     sequence similarity 125, member B"
                     /calculated_mol_wt=24385
     Region          1..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H7P6.2)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18005716; propagated from
                     UniProtKB/Swiss-Prot (Q9H7P6.2)"
     Region          48..>220
                     /region_name="DUF2464"
                     /note="Multivesicular body subunit 12; pfam10240"
                     /db_xref="CDD:463017"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18005716; propagated from
                     UniProtKB/Swiss-Prot (Q9H7P6.2)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:18005716; propagated from
                     UniProtKB/Swiss-Prot (Q9H7P6.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:18005716; propagated from
                     UniProtKB/Swiss-Prot (Q9H7P6.2)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:18005716; propagated from
                     UniProtKB/Swiss-Prot (Q9H7P6.2)"
     CDS             1..221
                     /gene="MVB12B"
                     /gene_synonym="C9orf28; FAM125B"
                     /coded_by="NM_001011703.3:102..767"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS48022.1"
                     /db_xref="GeneID:89853"
                     /db_xref="HGNC:HGNC:23368"
                     /db_xref="MIM:621454"
ORIGIN      
        1 mrscfcvrrs rdppppqppp pppqrgtdqs tmpevkdlse alpetsmdpi tgvgvvasrn
       61 raptgydvva qtadgvdadl wkdglfkskv trylcftrsf skenshlgnv lvdmklidik
      121 dtlpvgfipi qetvdtqeva frkkrlcikf iprdsteaai cdirimgrtk qappqytfig
      181 elnsmgiwyr mgrvprnhds sqpttpsqss aastpapnlp r
//
LOCUS       NP_001291476             181 aa            linear   PRI 19-DEC-2025
DEFINITION  multivesicular body subunit 12A isoform 2 [Homo sapiens].
ACCESSION   NP_001291476
VERSION     NP_001291476.1
DBSOURCE    REFSEQ: accession NM_001304547.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Flower,T.G., Takahashi,Y., Hudait,A., Rose,K., Tjahjono,N.,
            Pak,A.J., Yokom,A.L., Liang,X., Wang,H.G., Bouamr,F., Voth,G.A. and
            Hurley,J.H.
  TITLE     A helical assembly of human ESCRT-I scaffolds reverse-topology
            membrane scission
  JOURNAL   Nat Struct Mol Biol 27 (6), 570-580 (2020)
   PUBMED   32424346
  REMARK    GeneRIF: A helical assembly of human ESCRT-I scaffolds
            reverse-topology membrane scission.
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Boura,E. and Hurley,J.H.
  TITLE     Structural basis for membrane targeting by the MVB12-associated
            beta-prism domain of the human ESCRT-I MVB12 subunit
  JOURNAL   Proc Natl Acad Sci U S A 109 (6), 1901-1906 (2012)
   PUBMED   22232651
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Tsunematsu,T., Yamauchi,E., Shibata,H., Maki,M., Ohta,T. and
            Konishi,H.
  TITLE     Distinct functions of human MVB12A and MVB12B in the ESCRT-I
            dependent on their posttranslational modifications
  JOURNAL   Biochem Biophys Res Commun 399 (2), 232-237 (2010)
   PUBMED   20654576
  REMARK    GeneRIF: These results suggest that the expression of MVB12B may be
            normally suppressed through the ubiquitin-proteasome pathway that
            simultaneously regulates the fate of MVB12A and the functions of
            ESCRT-I.
            Erratum:[Biochem Biophys Res Commun. 2011 Mar 4;406(1):158-9]
REFERENCE   7  (residues 1 to 181)
  AUTHORS   Hurley,J.H. and Hanson,P.I.
  TITLE     Membrane budding and scission by the ESCRT machinery: it's all in
            the neck
  JOURNAL   Nat Rev Mol Cell Biol 11 (8), 556-566 (2010)
   PUBMED   20588296
  REMARK    Review article
REFERENCE   8  (residues 1 to 181)
  AUTHORS   Morita,E., Sandrin,V., Alam,S.L., Eckert,D.M., Gygi,S.P. and
            Sundquist,W.I.
  TITLE     Identification of human MVB12 proteins as ESCRT-I subunits that
            function in HIV budding
  JOURNAL   Cell Host Microbe 2 (1), 41-53 (2007)
   PUBMED   18005716
REFERENCE   9  (residues 1 to 181)
  AUTHORS   Konishi,H., Tashiro,K., Murata,Y., Nabeshi,H., Yamauchi,E. and
            Taniguchi,H.
  TITLE     CFBP is a novel tyrosine-phosphorylated protein that might function
            as a regulator of CIN85/CD2AP
  JOURNAL   J Biol Chem 281 (39), 28919-28931 (2006)
   PUBMED   16895919
  REMARK    GeneRIF: CFBP is a novel tyrosine-phosphorylated protein that might
            function as a regulator of CIN85/CD2AP
REFERENCE   10 (residues 1 to 181)
  AUTHORS   Wistow,G., Bernstein,S.L., Ray,S., Wyatt,M.K., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human iris for the NEIBank
            Project: steroid-response factors and similarities with retinal
            pigment epithelium
  JOURNAL   Mol Vis 8, 185-195 (2002)
   PUBMED   12107412
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG684013.1, BY996463.1, AC010319.10 and BP394542.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            lacks exons in the 5' coding region which results in the use of a
            downstream start codon compared to variant 1. The encoded isoform
            (2) has a shorter N-terminus compared to isoform 1. This variant is
            a read-through transcript between the upstream non-coding locus
            (GeneID: 105221694) and the downstream MVB12A locus (GeneID:
            93343).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1163658.73743.1, SRR1163655.235270.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA2142853 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            readthrough transcript    :: includes exons from GeneID 105221694
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..181
                     /product="multivesicular body subunit 12A isoform 2"
                     /note="CIN85/CD2AP family binding protein; ESCRT-I complex
                     subunit MVB12A; family with sequence similarity 125,
                     member A"
                     /calculated_mol_wt=19317
     Region          <1..169
                     /region_name="DUF2464"
                     /note="Multivesicular body subunit 12; pfam10240"
                     /db_xref="CDD:463017"
     CDS             1..181
                     /gene="MVB12A"
                     /gene_synonym="CFBP; FAM125A"
                     /coded_by="NM_001304547.2:438..983"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:93343"
                     /db_xref="HGNC:HGNC:25153"
                     /db_xref="MIM:621453"
ORIGIN      
        1 mdskasvskk krmcvkllpl gatdtavfdv rlsgktktvp gylrigdmgg faiwckkaka
       61 prpvpkprgl srdmqglsld aasqpskggl lertasrlgs rastlrrnds iyeasslygi
      121 samdgvpftl hprfegkscs plafsafgdl tiksladiee eynygfvvek taaarlppsv
      181 s
//
LOCUS       NP_001381918             900 aa            linear   PRI 20-DEC-2025
DEFINITION  neuronal PAS domain-containing protein 3 isoform 6 [Homo sapiens].
ACCESSION   NP_001381918 XP_011535374
VERSION     NP_001381918.1
DBSOURCE    REFSEQ: accession NM_001394989.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 900)
  AUTHORS   Caporale,A.L., Cinalli,A.R., Rubinstein,M. and Franchini,L.F.
  TITLE     The Human Accelerated Region HAR202 Controls NPAS3 Expression in
            the Developing Forebrain Displaying Differential Enhancer Activity
            Between Modern and Archaic Human Sequences
  JOURNAL   Mol Biol Evol 41 (10) (2024)
   PUBMED   39241178
REFERENCE   2  (residues 1 to 900)
  AUTHORS   Pavesic Radonja,A., Blazevic Zelic,S., Rubesa,G. and Bradshaw,N.J.
  TITLE     SYMPTOM SEVERITY IN SCHIZOPHRENIA PATIENTS WITH NPAS3, DYSBINDIN-1
            AND/OR TRIOBP PROTEIN PATHOLOGY IN THEIR BLOOD SERUM: A PANSS-BASED
            FOLLOW UP STUDY
  JOURNAL   Psychiatr Danub 35 (2), 180-186 (2023)
   PUBMED   37480305
  REMARK    GeneRIF: SYMPTOM SEVERITY IN SCHIZOPHRENIA PATIENTS WITH NPAS3,
            DYSBINDIN-1 AND/OR TRIOBP PROTEIN PATHOLOGY IN THEIR BLOOD SERUM: A
            PANSS-BASED FOLLOW UP STUDY.
REFERENCE   3  (residues 1 to 900)
  AUTHORS   Li,Y., Fan,T., Li,X., Liu,L., Mao,F., Li,Y., Miao,Z., Zeng,C.,
            Song,W., Pan,J., Zhou,S., Wang,H., Wang,Y. and Sun,Z.S.
  TITLE     Npas3 deficiency impairs cortical astrogenesis and induces
            autistic-like behaviors
  JOURNAL   Cell Rep 40 (9), 111289 (2022)
   PUBMED   36044858
  REMARK    GeneRIF: Npas3 deficiency impairs cortical astrogenesis and induces
            autistic-like behaviors.
            Erratum:[Cell Rep. 2022 Nov 8;41(6):111551. doi:
            10.1016/j.celrep.2022.111551. PMID: 36351396]
REFERENCE   4  (residues 1 to 900)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 900)
  AUTHORS   Rossi,J.J., Rosenfeld,J.A., Chan,K.M., Streff,H., Nankivell,V.,
            Peet,D.J., Whitelaw,M.L. and Bersten,D.C.
  TITLE     Molecular characterisation of rare loss-of-function NPAS3 and NPAS4
            variants identified in individuals with neurodevelopmental
            disorders
  JOURNAL   Sci Rep 11 (1), 6602 (2021)
   PUBMED   33758288
  REMARK    GeneRIF: Molecular characterisation of rare loss-of-function NPAS3
            and NPAS4 variants identified in individuals with
            neurodevelopmental disorders.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 900)
  AUTHORS   Pickard,B.S., Christoforou,A., Thomson,P.A., Fawkes,A., Evans,K.L.,
            Morris,S.W., Porteous,D.J., Blackwood,D.H. and Muir,W.J.
  TITLE     Interacting haplotypes at the NPAS3 locus alter risk of
            schizophrenia and bipolar disorder
  JOURNAL   Mol Psychiatry 14 (9), 874-884 (2009)
   PUBMED   18317462
  REMARK    GeneRIF: This study demonstrated that these risk and protective
            effects act combinatorially, potentially multiplicatively, to
            determine NPAS3 gene-wide susceptibility in bipolar disorder and
            schizophrenia.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 900)
  AUTHORS   Uhl,G.R., Liu,Q.R., Drgon,T., Johnson,C., Walther,D., Rose,J.E.,
            David,S.P., Niaura,R. and Lerman,C.
  TITLE     Molecular genetics of successful smoking cessation: convergent
            genome-wide association study results
  JOURNAL   Arch Gen Psychiatry 65 (6), 683-693 (2008)
   PUBMED   18519826
  REMARK    GeneRIF: Clinical trial and genome-wide association study of
            gene-disease association, gene-environment interaction, and
            pharmacogenomic / toxicogenomic. (HuGE Navigator)
REFERENCE   8  (residues 1 to 900)
  AUTHORS   Pickard,B.S., Pieper,A.A., Porteous,D.J., Blackwood,D.H. and
            Muir,W.J.
  TITLE     The NPAS3 gene--emerging evidence for a role in psychiatric illness
  JOURNAL   Ann Med 38 (6), 439-448 (2006)
   PUBMED   17008307
  REMARK    Review article
REFERENCE   9  (residues 1 to 900)
  AUTHORS   Kamnasaran,D., Chen,C.P., Devriendt,K., Mehta,L. and Cox,D.W.
  TITLE     Defining a holoprosencephaly locus on human chromosome 14q13 and
            characterization of potential candidate genes
  JOURNAL   Genomics 85 (5), 608-621 (2005)
   PUBMED   15820313
REFERENCE   10 (residues 1 to 900)
  AUTHORS   Kamnasaran,D., Muir,W.J., Ferguson-Smith,M.A. and Cox,D.W.
  TITLE     Disruption of the neuronal PAS3 gene in a family affected with
            schizophrenia
  JOURNAL   J Med Genet 40 (5), 325-332 (2003)
   PUBMED   12746393
  REMARK    GeneRIF: haploinsufficiency of NPAS3 contributes to the cause of
            schizophrenia
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109769.5, AL139296.4,
            AL158802.1, AL161851.4 and AL157689.3.
            
            On May 13, 2021 this sequence version replaced XP_011535374.1.
            
            Summary: This gene encodes a member of the basic helix-loop-helix
            and PAS domain-containing family of transcription factors. The
            encoded protein is localized to the nucleus and may regulate genes
            involved in neurogenesis. Chromosomal abnormalities that affect the
            coding potential of this gene are associated with schizophrenia and
            cognitive disability. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: KJ534895.1, SRR18074967.1670629.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145240, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..900
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.1"
     Protein         1..900
                     /product="neuronal PAS domain-containing protein 3 isoform
                     6"
                     /note="neuronal PAS domain-containing protein 3; member of
                     PAS protein 6; neuronal PAS3; PAS domain-containing
                     protein 6; basic-helix-loop-helix-PAS protein MOP6; class
                     E basic helix-loop-helix protein 12"
                     /calculated_mol_wt=96829
     Region          17..94
                     /region_name="bHLH-PAS_NPAS3_PASD6"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in neuronal PAS domain-containing protein 3
                     (NPAS3) and similar proteins; cd19732"
                     /db_xref="CDD:381575"
     Site            order(23,25..27,31,33..34,38,59..60)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381575"
     Site            order(33,36..37,40,43..44,47,49..50,61,64..66,68,70..74)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381575"
     Region          122..180
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Region          124..>383
                     /region_name="KinE"
                     /note="Sporulation sensor histidine kinase E [Cell cycle
                     control, cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG5809"
                     /db_xref="CDD:444511"
     Region          313..400
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(316,320,326,339..342,368,373)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(336,340,348,351..352,380,382)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          <442..562
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     CDS             1..900
                     /gene="NPAS3"
                     /gene_synonym="bHLHe12; MOP6; PASD6"
                     /coded_by="NM_001394989.1:439..3141"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:64067"
                     /db_xref="HGNC:HGNC:19311"
                     /db_xref="MIM:609430"
ORIGIN      
        1 maptkpsfqq dpsrrerlqa lrkeksrdaa rsrrgkenfe fyelakllpl paaitsqldk
       61 asiirltisy lkmrdfanqg dppwnlrmeg pppntsvkvi gaqrrrspsa laievfeahl
      121 gshilqsldg fvfalnqegk flyisetvsi ylglsqvelt gssvfdyvhp gdhvemaeql
      181 gmklppgrgl lsqgtaedga ssassssqse tpepvestsp sllttdntle rsffirmkst
      241 ltkrgvhiks sgykvihitg rlrlrvslsh grtvpsqimg lvvvahalpp ptinevridc
      301 hmfvtrvnmd lniiycenri sdymdltpvd ivgkrcyhfi haedvegirh shldllnkgq
      361 cvtkyyrwmq knggyiwiqs satiainakn anekniiwvn yllsnpeykd tpmdiaqlph
      421 lpektsesse tsdsesdskd tsednensks dekgnqsens edpepdrkks gnacdndmnc
      481 nddghsssnp dsrdsddsfe hsdfenpkag edgfgalgam qikveryves esdlrlqnce
      541 sltsdsakds dsageagaqa sskhqkrkkr rkrqkggsas rrrlssassp ggldaglvep
      601 prllsspnsa svlkikteis epinfdndss iwnyppnrei srnespysmt kppssehfps
      661 pqgggggggg ggglhvaipd svltppgadg aaarktqfga sataalapva sdplspplsa
      721 sprdkhpgng ggggggggga ggggpsasns llytgdleal qrlqagnvvl plvhrvtgtl
      781 aatstaaqrv yttgtiryap aevtlamqsn llpnahavnf vdvnspgfgl dpktpmemly
      841 hhvhrlnmsg pfggavsaas ltqmpagnvf ttaeglfstl pfpvysngih aaqtlerked
//
LOCUS       NP_775182                920 aa            linear   PRI 20-DEC-2025
DEFINITION  neuronal PAS domain-containing protein 3 isoform 3 [Homo sapiens].
ACCESSION   NP_775182
VERSION     NP_775182.1
DBSOURCE    REFSEQ: accession NM_173159.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Caporale,A.L., Cinalli,A.R., Rubinstein,M. and Franchini,L.F.
  TITLE     The Human Accelerated Region HAR202 Controls NPAS3 Expression in
            the Developing Forebrain Displaying Differential Enhancer Activity
            Between Modern and Archaic Human Sequences
  JOURNAL   Mol Biol Evol 41 (10) (2024)
   PUBMED   39241178
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Pavesic Radonja,A., Blazevic Zelic,S., Rubesa,G. and Bradshaw,N.J.
  TITLE     SYMPTOM SEVERITY IN SCHIZOPHRENIA PATIENTS WITH NPAS3, DYSBINDIN-1
            AND/OR TRIOBP PROTEIN PATHOLOGY IN THEIR BLOOD SERUM: A PANSS-BASED
            FOLLOW UP STUDY
  JOURNAL   Psychiatr Danub 35 (2), 180-186 (2023)
   PUBMED   37480305
  REMARK    GeneRIF: SYMPTOM SEVERITY IN SCHIZOPHRENIA PATIENTS WITH NPAS3,
            DYSBINDIN-1 AND/OR TRIOBP PROTEIN PATHOLOGY IN THEIR BLOOD SERUM: A
            PANSS-BASED FOLLOW UP STUDY.
REFERENCE   3  (residues 1 to 920)
  AUTHORS   Li,Y., Fan,T., Li,X., Liu,L., Mao,F., Li,Y., Miao,Z., Zeng,C.,
            Song,W., Pan,J., Zhou,S., Wang,H., Wang,Y. and Sun,Z.S.
  TITLE     Npas3 deficiency impairs cortical astrogenesis and induces
            autistic-like behaviors
  JOURNAL   Cell Rep 40 (9), 111289 (2022)
   PUBMED   36044858
  REMARK    GeneRIF: Npas3 deficiency impairs cortical astrogenesis and induces
            autistic-like behaviors.
            Erratum:[Cell Rep. 2022 Nov 8;41(6):111551. doi:
            10.1016/j.celrep.2022.111551. PMID: 36351396]
REFERENCE   4  (residues 1 to 920)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 920)
  AUTHORS   Rossi,J.J., Rosenfeld,J.A., Chan,K.M., Streff,H., Nankivell,V.,
            Peet,D.J., Whitelaw,M.L. and Bersten,D.C.
  TITLE     Molecular characterisation of rare loss-of-function NPAS3 and NPAS4
            variants identified in individuals with neurodevelopmental
            disorders
  JOURNAL   Sci Rep 11 (1), 6602 (2021)
   PUBMED   33758288
  REMARK    GeneRIF: Molecular characterisation of rare loss-of-function NPAS3
            and NPAS4 variants identified in individuals with
            neurodevelopmental disorders.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 920)
  AUTHORS   Pickard,B.S., Christoforou,A., Thomson,P.A., Fawkes,A., Evans,K.L.,
            Morris,S.W., Porteous,D.J., Blackwood,D.H. and Muir,W.J.
  TITLE     Interacting haplotypes at the NPAS3 locus alter risk of
            schizophrenia and bipolar disorder
  JOURNAL   Mol Psychiatry 14 (9), 874-884 (2009)
   PUBMED   18317462
  REMARK    GeneRIF: This study demonstrated that these risk and protective
            effects act combinatorially, potentially multiplicatively, to
            determine NPAS3 gene-wide susceptibility in bipolar disorder and
            schizophrenia.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 920)
  AUTHORS   Uhl,G.R., Liu,Q.R., Drgon,T., Johnson,C., Walther,D., Rose,J.E.,
            David,S.P., Niaura,R. and Lerman,C.
  TITLE     Molecular genetics of successful smoking cessation: convergent
            genome-wide association study results
  JOURNAL   Arch Gen Psychiatry 65 (6), 683-693 (2008)
   PUBMED   18519826
  REMARK    GeneRIF: Clinical trial and genome-wide association study of
            gene-disease association, gene-environment interaction, and
            pharmacogenomic / toxicogenomic. (HuGE Navigator)
REFERENCE   8  (residues 1 to 920)
  AUTHORS   Pickard,B.S., Pieper,A.A., Porteous,D.J., Blackwood,D.H. and
            Muir,W.J.
  TITLE     The NPAS3 gene--emerging evidence for a role in psychiatric illness
  JOURNAL   Ann Med 38 (6), 439-448 (2006)
   PUBMED   17008307
  REMARK    Review article
REFERENCE   9  (residues 1 to 920)
  AUTHORS   Kamnasaran,D., Chen,C.P., Devriendt,K., Mehta,L. and Cox,D.W.
  TITLE     Defining a holoprosencephaly locus on human chromosome 14q13 and
            characterization of potential candidate genes
  JOURNAL   Genomics 85 (5), 608-621 (2005)
   PUBMED   15820313
REFERENCE   10 (residues 1 to 920)
  AUTHORS   Kamnasaran,D., Muir,W.J., Ferguson-Smith,M.A. and Cox,D.W.
  TITLE     Disruption of the neuronal PAS3 gene in a family affected with
            schizophrenia
  JOURNAL   J Med Genet 40 (5), 325-332 (2003)
   PUBMED   12746393
  REMARK    GeneRIF: haploinsufficiency of NPAS3 contributes to the cause of
            schizophrenia
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109769.5, AF164438.1,
            AB054576.1, AL157689.3 and AI811363.1.
            
            Summary: This gene encodes a member of the basic helix-loop-helix
            and PAS domain-containing family of transcription factors. The
            encoded protein is localized to the nucleus and may regulate genes
            involved in neurogenesis. Chromosomal abnormalities that affect the
            coding potential of this gene are associated with schizophrenia and
            cognitive disability. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (3) has multiple differences in
            the coding region but maintains the reading frame, compared to
            variant 1. This variant encodes isoform 3, which is shorter than
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB054576.1, KJ535019.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.1"
     Protein         1..920
                     /product="neuronal PAS domain-containing protein 3 isoform
                     3"
                     /note="neuronal PAS domain-containing protein 3; member of
                     PAS protein 6; neuronal PAS3; PAS domain-containing
                     protein 6; basic-helix-loop-helix-PAS protein MOP6; class
                     E basic helix-loop-helix protein 12"
                     /calculated_mol_wt=99123
     Region          17..94
                     /region_name="bHLH-PAS_NPAS3_PASD6"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in neuronal PAS domain-containing protein 3
                     (NPAS3) and similar proteins; cd19732"
                     /db_xref="CDD:381575"
     Site            order(23,25..27,31,33..34,38,59..60)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381575"
     Site            order(33,36..37,40,43..44,47,49..50,61,64..66,68,70..74)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381575"
     Region          139..197
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Region          141..>400
                     /region_name="KinE"
                     /note="Sporulation sensor histidine kinase E [Cell cycle
                     control, cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG5809"
                     /db_xref="CDD:444511"
     Region          330..417
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(333,337,343,356..359,385,390)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(353,357,365,368..369,397,399)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          <423..>582
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     CDS             1..920
                     /gene="NPAS3"
                     /gene_synonym="bHLHe12; MOP6; PASD6"
                     /coded_by="NM_173159.3:439..3201"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS53892.1"
                     /db_xref="GeneID:64067"
                     /db_xref="HGNC:HGNC:19311"
                     /db_xref="MIM:609430"
ORIGIN      
        1 maptkpsfqq dpsrrerlqa lrkeksrdaa rsrrgkenfe fyelakllpl paaitsqldk
       61 asiirltisy lkmrdfanqg dppwnlrmeg pppntsvkgi qmwkselcmr ktpcevigaq
      121 rrrspsalai evfeahlgsh ilqsldgfvf alnqegkfly isetvsiylg lsqveltgss
      181 vfdyvhpgdh vemaeqlgmk lppgrgllsq gtaedgassa ssssqsetpe pvestspsll
      241 ttdntlersf firmkstltk rgvhikssgy kvihitgrlr lrvslshgrt vpsqimglvv
      301 vahalpppti nevridchmf vtrvnmdlni iycenrisdy mdltpvdivg krcyhfihae
      361 dvegirhshl dllnkgqcvt kyyrwmqkng gyiwiqssat iainaknane kniiwvnyll
      421 snpeykdtpm diaqlphlpe ktsessetsd sesdskdtsg itednensks dekgnqsens
      481 edpepdrkks gnacdndmnc nddghsssnp dsrdsddsfe hsdfenpkag edgfgalgam
      541 qikveryves esdlrlqnce sltsdsakds dsageagaqa sskhqkrkkr rkrqkggsas
      601 rrrlssassp ggldaglvep prllsspnsa svlkikteis epinfdndss iwnyppnrei
      661 srnespysmt kppssehfps pqgggggggg ggglhvaipd svltppgadg aaarktqfga
      721 sataalapva sdplspplsa sprdkhpgng ggggggggga ggggpsasns llytgdleal
      781 qrlqagnvvl plvhrvtgtl aatstaaqrv yttgtiryap aevtlamqsn llpnahavnf
      841 vdvnspgfgl dpktpmemly hhvhrlnmsg pfggavsaas ltqmpagnvf ttaeglfstl
      901 pfpvysngih aaqtlerked
//
LOCUS       NP_001159365             903 aa            linear   PRI 20-DEC-2025
DEFINITION  neuronal PAS domain-containing protein 3 isoform 4 [Homo sapiens].
ACCESSION   NP_001159365
VERSION     NP_001159365.1
DBSOURCE    REFSEQ: accession NM_001165893.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 903)
  AUTHORS   Caporale,A.L., Cinalli,A.R., Rubinstein,M. and Franchini,L.F.
  TITLE     The Human Accelerated Region HAR202 Controls NPAS3 Expression in
            the Developing Forebrain Displaying Differential Enhancer Activity
            Between Modern and Archaic Human Sequences
  JOURNAL   Mol Biol Evol 41 (10) (2024)
   PUBMED   39241178
REFERENCE   2  (residues 1 to 903)
  AUTHORS   Pavesic Radonja,A., Blazevic Zelic,S., Rubesa,G. and Bradshaw,N.J.
  TITLE     SYMPTOM SEVERITY IN SCHIZOPHRENIA PATIENTS WITH NPAS3, DYSBINDIN-1
            AND/OR TRIOBP PROTEIN PATHOLOGY IN THEIR BLOOD SERUM: A PANSS-BASED
            FOLLOW UP STUDY
  JOURNAL   Psychiatr Danub 35 (2), 180-186 (2023)
   PUBMED   37480305
  REMARK    GeneRIF: SYMPTOM SEVERITY IN SCHIZOPHRENIA PATIENTS WITH NPAS3,
            DYSBINDIN-1 AND/OR TRIOBP PROTEIN PATHOLOGY IN THEIR BLOOD SERUM: A
            PANSS-BASED FOLLOW UP STUDY.
REFERENCE   3  (residues 1 to 903)
  AUTHORS   Li,Y., Fan,T., Li,X., Liu,L., Mao,F., Li,Y., Miao,Z., Zeng,C.,
            Song,W., Pan,J., Zhou,S., Wang,H., Wang,Y. and Sun,Z.S.
  TITLE     Npas3 deficiency impairs cortical astrogenesis and induces
            autistic-like behaviors
  JOURNAL   Cell Rep 40 (9), 111289 (2022)
   PUBMED   36044858
  REMARK    GeneRIF: Npas3 deficiency impairs cortical astrogenesis and induces
            autistic-like behaviors.
            Erratum:[Cell Rep. 2022 Nov 8;41(6):111551. doi:
            10.1016/j.celrep.2022.111551. PMID: 36351396]
REFERENCE   4  (residues 1 to 903)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 903)
  AUTHORS   Rossi,J.J., Rosenfeld,J.A., Chan,K.M., Streff,H., Nankivell,V.,
            Peet,D.J., Whitelaw,M.L. and Bersten,D.C.
  TITLE     Molecular characterisation of rare loss-of-function NPAS3 and NPAS4
            variants identified in individuals with neurodevelopmental
            disorders
  JOURNAL   Sci Rep 11 (1), 6602 (2021)
   PUBMED   33758288
  REMARK    GeneRIF: Molecular characterisation of rare loss-of-function NPAS3
            and NPAS4 variants identified in individuals with
            neurodevelopmental disorders.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 903)
  AUTHORS   Pickard,B.S., Christoforou,A., Thomson,P.A., Fawkes,A., Evans,K.L.,
            Morris,S.W., Porteous,D.J., Blackwood,D.H. and Muir,W.J.
  TITLE     Interacting haplotypes at the NPAS3 locus alter risk of
            schizophrenia and bipolar disorder
  JOURNAL   Mol Psychiatry 14 (9), 874-884 (2009)
   PUBMED   18317462
  REMARK    GeneRIF: This study demonstrated that these risk and protective
            effects act combinatorially, potentially multiplicatively, to
            determine NPAS3 gene-wide susceptibility in bipolar disorder and
            schizophrenia.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 903)
  AUTHORS   Uhl,G.R., Liu,Q.R., Drgon,T., Johnson,C., Walther,D., Rose,J.E.,
            David,S.P., Niaura,R. and Lerman,C.
  TITLE     Molecular genetics of successful smoking cessation: convergent
            genome-wide association study results
  JOURNAL   Arch Gen Psychiatry 65 (6), 683-693 (2008)
   PUBMED   18519826
  REMARK    GeneRIF: Clinical trial and genome-wide association study of
            gene-disease association, gene-environment interaction, and
            pharmacogenomic / toxicogenomic. (HuGE Navigator)
REFERENCE   8  (residues 1 to 903)
  AUTHORS   Pickard,B.S., Pieper,A.A., Porteous,D.J., Blackwood,D.H. and
            Muir,W.J.
  TITLE     The NPAS3 gene--emerging evidence for a role in psychiatric illness
  JOURNAL   Ann Med 38 (6), 439-448 (2006)
   PUBMED   17008307
  REMARK    Review article
REFERENCE   9  (residues 1 to 903)
  AUTHORS   Kamnasaran,D., Chen,C.P., Devriendt,K., Mehta,L. and Cox,D.W.
  TITLE     Defining a holoprosencephaly locus on human chromosome 14q13 and
            characterization of potential candidate genes
  JOURNAL   Genomics 85 (5), 608-621 (2005)
   PUBMED   15820313
REFERENCE   10 (residues 1 to 903)
  AUTHORS   Kamnasaran,D., Muir,W.J., Ferguson-Smith,M.A. and Cox,D.W.
  TITLE     Disruption of the neuronal PAS3 gene in a family affected with
            schizophrenia
  JOURNAL   J Med Genet 40 (5), 325-332 (2003)
   PUBMED   12746393
  REMARK    GeneRIF: haploinsufficiency of NPAS3 contributes to the cause of
            schizophrenia
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109769.5, AB054575.1,
            AL157689.3 and AI811363.1.
            
            Summary: This gene encodes a member of the basic helix-loop-helix
            and PAS domain-containing family of transcription factors. The
            encoded protein is localized to the nucleus and may regulate genes
            involved in neurogenesis. Chromosomal abnormalities that affect the
            coding potential of this gene are associated with schizophrenia and
            cognitive disability. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (4) lacks an in-frame exon in the
            coding region, compared to variant 1. The encoded isoform (4) is
            shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB054575.1, KJ534898.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145240, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..903
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.1"
     Protein         1..903
                     /product="neuronal PAS domain-containing protein 3 isoform
                     4"
                     /note="neuronal PAS domain-containing protein 3; member of
                     PAS protein 6; neuronal PAS3; PAS domain-containing
                     protein 6; basic-helix-loop-helix-PAS protein MOP6; class
                     E basic helix-loop-helix protein 12"
                     /calculated_mol_wt=97101
     Region          17..94
                     /region_name="bHLH-PAS_NPAS3_PASD6"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in neuronal PAS domain-containing protein 3
                     (NPAS3) and similar proteins; cd19732"
                     /db_xref="CDD:381575"
     Site            order(23,25..27,31,33..34,38,59..60)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381575"
     Site            order(33,36..37,40,43..44,47,49..50,61,64..66,68,70..74)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381575"
     Region          122..180
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Region          124..>383
                     /region_name="KinE"
                     /note="Sporulation sensor histidine kinase E [Cell cycle
                     control, cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG5809"
                     /db_xref="CDD:444511"
     Region          313..400
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(316,320,326,339..342,368,373)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(336,340,348,351..352,380,382)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          <406..>565
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     CDS             1..903
                     /gene="NPAS3"
                     /gene_synonym="bHLHe12; MOP6; PASD6"
                     /coded_by="NM_001165893.2:439..3150"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS55912.1"
                     /db_xref="GeneID:64067"
                     /db_xref="HGNC:HGNC:19311"
                     /db_xref="MIM:609430"
ORIGIN      
        1 maptkpsfqq dpsrrerlqa lrkeksrdaa rsrrgkenfe fyelakllpl paaitsqldk
       61 asiirltisy lkmrdfanqg dppwnlrmeg pppntsvkvi gaqrrrspsa laievfeahl
      121 gshilqsldg fvfalnqegk flyisetvsi ylglsqvelt gssvfdyvhp gdhvemaeql
      181 gmklppgrgl lsqgtaedga ssassssqse tpepvestsp sllttdntle rsffirmkst
      241 ltkrgvhiks sgykvihitg rlrlrvslsh grtvpsqimg lvvvahalpp ptinevridc
      301 hmfvtrvnmd lniiycenri sdymdltpvd ivgkrcyhfi haedvegirh shldllnkgq
      361 cvtkyyrwmq knggyiwiqs satiainakn anekniiwvn yllsnpeykd tpmdiaqlph
      421 lpektsesse tsdsesdskd tsgitednen sksdekgnqs ensedpepdr kksgnacdnd
      481 mncnddghss snpdsrdsdd sfehsdfenp kagedgfgal gamqikvery vesesdlrlq
      541 ncesltsdsa kdsdsageag aqasskhqkr kkrrkrqkgg sasrrrlssa sspggldagl
      601 vepprllssp nsasvlkikt eisepinfdn dssiwnyppn reisrnespy smtkppsseh
      661 fpspqggggg gggggglhva ipdsvltppg adgaaarktq fgasataala pvasdplspp
      721 lsasprdkhp gngggggggg ggaggggpsa snsllytgdl ealqrlqagn vvlplvhrvt
      781 gtlaatstaa qrvyttgtir yapaevtlam qsnllpnaha vnfvdvnspg fgldpktpme
      841 mlyhhvhrln msgpfggavs aasltqmpag nvfttaeglf stlpfpvysn gihaaqtler
      901 ked
//
LOCUS       NP_001158221             933 aa            linear   PRI 20-DEC-2025
DEFINITION  neuronal PAS domain-containing protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_001158221
VERSION     NP_001158221.1
DBSOURCE    REFSEQ: accession NM_001164749.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 933)
  AUTHORS   Caporale,A.L., Cinalli,A.R., Rubinstein,M. and Franchini,L.F.
  TITLE     The Human Accelerated Region HAR202 Controls NPAS3 Expression in
            the Developing Forebrain Displaying Differential Enhancer Activity
            Between Modern and Archaic Human Sequences
  JOURNAL   Mol Biol Evol 41 (10) (2024)
   PUBMED   39241178
REFERENCE   2  (residues 1 to 933)
  AUTHORS   Pavesic Radonja,A., Blazevic Zelic,S., Rubesa,G. and Bradshaw,N.J.
  TITLE     SYMPTOM SEVERITY IN SCHIZOPHRENIA PATIENTS WITH NPAS3, DYSBINDIN-1
            AND/OR TRIOBP PROTEIN PATHOLOGY IN THEIR BLOOD SERUM: A PANSS-BASED
            FOLLOW UP STUDY
  JOURNAL   Psychiatr Danub 35 (2), 180-186 (2023)
   PUBMED   37480305
  REMARK    GeneRIF: SYMPTOM SEVERITY IN SCHIZOPHRENIA PATIENTS WITH NPAS3,
            DYSBINDIN-1 AND/OR TRIOBP PROTEIN PATHOLOGY IN THEIR BLOOD SERUM: A
            PANSS-BASED FOLLOW UP STUDY.
REFERENCE   3  (residues 1 to 933)
  AUTHORS   Li,Y., Fan,T., Li,X., Liu,L., Mao,F., Li,Y., Miao,Z., Zeng,C.,
            Song,W., Pan,J., Zhou,S., Wang,H., Wang,Y. and Sun,Z.S.
  TITLE     Npas3 deficiency impairs cortical astrogenesis and induces
            autistic-like behaviors
  JOURNAL   Cell Rep 40 (9), 111289 (2022)
   PUBMED   36044858
  REMARK    GeneRIF: Npas3 deficiency impairs cortical astrogenesis and induces
            autistic-like behaviors.
            Erratum:[Cell Rep. 2022 Nov 8;41(6):111551. doi:
            10.1016/j.celrep.2022.111551. PMID: 36351396]
REFERENCE   4  (residues 1 to 933)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 933)
  AUTHORS   Rossi,J.J., Rosenfeld,J.A., Chan,K.M., Streff,H., Nankivell,V.,
            Peet,D.J., Whitelaw,M.L. and Bersten,D.C.
  TITLE     Molecular characterisation of rare loss-of-function NPAS3 and NPAS4
            variants identified in individuals with neurodevelopmental
            disorders
  JOURNAL   Sci Rep 11 (1), 6602 (2021)
   PUBMED   33758288
  REMARK    GeneRIF: Molecular characterisation of rare loss-of-function NPAS3
            and NPAS4 variants identified in individuals with
            neurodevelopmental disorders.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 933)
  AUTHORS   Pickard,B.S., Christoforou,A., Thomson,P.A., Fawkes,A., Evans,K.L.,
            Morris,S.W., Porteous,D.J., Blackwood,D.H. and Muir,W.J.
  TITLE     Interacting haplotypes at the NPAS3 locus alter risk of
            schizophrenia and bipolar disorder
  JOURNAL   Mol Psychiatry 14 (9), 874-884 (2009)
   PUBMED   18317462
  REMARK    GeneRIF: This study demonstrated that these risk and protective
            effects act combinatorially, potentially multiplicatively, to
            determine NPAS3 gene-wide susceptibility in bipolar disorder and
            schizophrenia.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 933)
  AUTHORS   Uhl,G.R., Liu,Q.R., Drgon,T., Johnson,C., Walther,D., Rose,J.E.,
            David,S.P., Niaura,R. and Lerman,C.
  TITLE     Molecular genetics of successful smoking cessation: convergent
            genome-wide association study results
  JOURNAL   Arch Gen Psychiatry 65 (6), 683-693 (2008)
   PUBMED   18519826
  REMARK    GeneRIF: Clinical trial and genome-wide association study of
            gene-disease association, gene-environment interaction, and
            pharmacogenomic / toxicogenomic. (HuGE Navigator)
REFERENCE   8  (residues 1 to 933)
  AUTHORS   Pickard,B.S., Pieper,A.A., Porteous,D.J., Blackwood,D.H. and
            Muir,W.J.
  TITLE     The NPAS3 gene--emerging evidence for a role in psychiatric illness
  JOURNAL   Ann Med 38 (6), 439-448 (2006)
   PUBMED   17008307
  REMARK    Review article
REFERENCE   9  (residues 1 to 933)
  AUTHORS   Kamnasaran,D., Chen,C.P., Devriendt,K., Mehta,L. and Cox,D.W.
  TITLE     Defining a holoprosencephaly locus on human chromosome 14q13 and
            characterization of potential candidate genes
  JOURNAL   Genomics 85 (5), 608-621 (2005)
   PUBMED   15820313
REFERENCE   10 (residues 1 to 933)
  AUTHORS   Kamnasaran,D., Muir,W.J., Ferguson-Smith,M.A. and Cox,D.W.
  TITLE     Disruption of the neuronal PAS3 gene in a family affected with
            schizophrenia
  JOURNAL   J Med Genet 40 (5), 325-332 (2003)
   PUBMED   12746393
  REMARK    GeneRIF: haploinsufficiency of NPAS3 contributes to the cause of
            schizophrenia
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109769.5, AY157302.1,
            AB055962.1, AL157689.3 and AI811363.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the basic helix-loop-helix
            and PAS domain-containing family of transcription factors. The
            encoded protein is localized to the nucleus and may regulate genes
            involved in neurogenesis. Chromosomal abnormalities that affect the
            coding potential of this gene are associated with schizophrenia and
            cognitive disability. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB055962.1, KJ534894.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356141.9/ ENSP00000348460.4
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.1"
     Protein         1..933
                     /product="neuronal PAS domain-containing protein 3 isoform
                     1"
                     /note="neuronal PAS domain-containing protein 3; member of
                     PAS protein 6; neuronal PAS3; PAS domain-containing
                     protein 6; basic-helix-loop-helix-PAS protein MOP6; class
                     E basic helix-loop-helix protein 12"
                     /calculated_mol_wt=100675
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXF0.1)"
     Region          48..124
                     /region_name="bHLH-PAS_NPAS3_PASD6"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in neuronal PAS domain-containing protein 3
                     (NPAS3) and similar proteins; cd19732"
                     /db_xref="CDD:381575"
     Site            order(53,55..57,61,63..64,68,89..90)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381575"
     Region          53..64
                     /region_name="DNA-binding.
                     /evidence=ECO:0000250|UniProtKB:Q9QZQ0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXF0.1)"
     Site            order(63,66..67,70,73..74,77,79..80,91,94..96,98,100..104)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381575"
     Region          152..210
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Region          154..>413
                     /region_name="KinE"
                     /note="Sporulation sensor histidine kinase E [Cell cycle
                     control, cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG5809"
                     /db_xref="CDD:444511"
     Region          215..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXF0.1)"
     Region          343..430
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(346,350,356,369..372,398,403)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(366,370,378,381..382,410,412)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          <436..>595
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     Region          452..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXF0.1)"
     Region          562..641
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXF0.1)"
     Region          657..725
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXF0.1)"
     Region          742..780
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IXF0.1)"
     CDS             1..933
                     /gene="NPAS3"
                     /gene_synonym="bHLHe12; MOP6; PASD6"
                     /coded_by="NM_001164749.2:439..3240"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS53891.1"
                     /db_xref="GeneID:64067"
                     /db_xref="HGNC:HGNC:19311"
                     /db_xref="MIM:609430"
ORIGIN      
        1 maptkpsfqq dpsrrerita qhplpnqsec rkiyrydgiy cestyqnlqa lrkeksrdaa
       61 rsrrgkenfe fyelakllpl paaitsqldk asiirltisy lkmrdfanqg dppwnlrmeg
      121 pppntsvkvi gaqrrrspsa laievfeahl gshilqsldg fvfalnqegk flyisetvsi
      181 ylglsqvelt gssvfdyvhp gdhvemaeql gmklppgrgl lsqgtaedga ssassssqse
      241 tpepvestsp sllttdntle rsffirmkst ltkrgvhiks sgykvihitg rlrlrvslsh
      301 grtvpsqimg lvvvahalpp ptinevridc hmfvtrvnmd lniiycenri sdymdltpvd
      361 ivgkrcyhfi haedvegirh shldllnkgq cvtkyyrwmq knggyiwiqs satiainakn
      421 anekniiwvn yllsnpeykd tpmdiaqlph lpektsesse tsdsesdskd tsgitednen
      481 sksdekgnqs ensedpepdr kksgnacdnd mncnddghss snpdsrdsdd sfehsdfenp
      541 kagedgfgal gamqikvery vesesdlrlq ncesltsdsa kdsdsageag aqasskhqkr
      601 kkrrkrqkgg sasrrrlssa sspggldagl vepprllssp nsasvlkikt eisepinfdn
      661 dssiwnyppn reisrnespy smtkppsseh fpspqggggg gggggglhva ipdsvltppg
      721 adgaaarktq fgasataala pvasdplspp lsasprdkhp gngggggggg ggaggggpsa
      781 snsllytgdl ealqrlqagn vvlplvhrvt gtlaatstaa qrvyttgtir yapaevtlam
      841 qsnllpnaha vnfvdvnspg fgldpktpme mlyhhvhrln msgpfggavs aasltqmpag
      901 nvfttaeglf stlpfpvysn gihaaqtler ked
//
LOCUS       NP_071406                901 aa            linear   PRI 20-DEC-2025
DEFINITION  neuronal PAS domain-containing protein 3 isoform 2 [Homo sapiens].
ACCESSION   NP_071406
VERSION     NP_071406.1
DBSOURCE    REFSEQ: accession NM_022123.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 901)
  AUTHORS   Caporale,A.L., Cinalli,A.R., Rubinstein,M. and Franchini,L.F.
  TITLE     The Human Accelerated Region HAR202 Controls NPAS3 Expression in
            the Developing Forebrain Displaying Differential Enhancer Activity
            Between Modern and Archaic Human Sequences
  JOURNAL   Mol Biol Evol 41 (10) (2024)
   PUBMED   39241178
REFERENCE   2  (residues 1 to 901)
  AUTHORS   Pavesic Radonja,A., Blazevic Zelic,S., Rubesa,G. and Bradshaw,N.J.
  TITLE     SYMPTOM SEVERITY IN SCHIZOPHRENIA PATIENTS WITH NPAS3, DYSBINDIN-1
            AND/OR TRIOBP PROTEIN PATHOLOGY IN THEIR BLOOD SERUM: A PANSS-BASED
            FOLLOW UP STUDY
  JOURNAL   Psychiatr Danub 35 (2), 180-186 (2023)
   PUBMED   37480305
  REMARK    GeneRIF: SYMPTOM SEVERITY IN SCHIZOPHRENIA PATIENTS WITH NPAS3,
            DYSBINDIN-1 AND/OR TRIOBP PROTEIN PATHOLOGY IN THEIR BLOOD SERUM: A
            PANSS-BASED FOLLOW UP STUDY.
REFERENCE   3  (residues 1 to 901)
  AUTHORS   Li,Y., Fan,T., Li,X., Liu,L., Mao,F., Li,Y., Miao,Z., Zeng,C.,
            Song,W., Pan,J., Zhou,S., Wang,H., Wang,Y. and Sun,Z.S.
  TITLE     Npas3 deficiency impairs cortical astrogenesis and induces
            autistic-like behaviors
  JOURNAL   Cell Rep 40 (9), 111289 (2022)
   PUBMED   36044858
  REMARK    GeneRIF: Npas3 deficiency impairs cortical astrogenesis and induces
            autistic-like behaviors.
            Erratum:[Cell Rep. 2022 Nov 8;41(6):111551. doi:
            10.1016/j.celrep.2022.111551. PMID: 36351396]
REFERENCE   4  (residues 1 to 901)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 901)
  AUTHORS   Rossi,J.J., Rosenfeld,J.A., Chan,K.M., Streff,H., Nankivell,V.,
            Peet,D.J., Whitelaw,M.L. and Bersten,D.C.
  TITLE     Molecular characterisation of rare loss-of-function NPAS3 and NPAS4
            variants identified in individuals with neurodevelopmental
            disorders
  JOURNAL   Sci Rep 11 (1), 6602 (2021)
   PUBMED   33758288
  REMARK    GeneRIF: Molecular characterisation of rare loss-of-function NPAS3
            and NPAS4 variants identified in individuals with
            neurodevelopmental disorders.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 901)
  AUTHORS   Pickard,B.S., Christoforou,A., Thomson,P.A., Fawkes,A., Evans,K.L.,
            Morris,S.W., Porteous,D.J., Blackwood,D.H. and Muir,W.J.
  TITLE     Interacting haplotypes at the NPAS3 locus alter risk of
            schizophrenia and bipolar disorder
  JOURNAL   Mol Psychiatry 14 (9), 874-884 (2009)
   PUBMED   18317462
  REMARK    GeneRIF: This study demonstrated that these risk and protective
            effects act combinatorially, potentially multiplicatively, to
            determine NPAS3 gene-wide susceptibility in bipolar disorder and
            schizophrenia.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 901)
  AUTHORS   Uhl,G.R., Liu,Q.R., Drgon,T., Johnson,C., Walther,D., Rose,J.E.,
            David,S.P., Niaura,R. and Lerman,C.
  TITLE     Molecular genetics of successful smoking cessation: convergent
            genome-wide association study results
  JOURNAL   Arch Gen Psychiatry 65 (6), 683-693 (2008)
   PUBMED   18519826
  REMARK    GeneRIF: Clinical trial and genome-wide association study of
            gene-disease association, gene-environment interaction, and
            pharmacogenomic / toxicogenomic. (HuGE Navigator)
REFERENCE   8  (residues 1 to 901)
  AUTHORS   Pickard,B.S., Pieper,A.A., Porteous,D.J., Blackwood,D.H. and
            Muir,W.J.
  TITLE     The NPAS3 gene--emerging evidence for a role in psychiatric illness
  JOURNAL   Ann Med 38 (6), 439-448 (2006)
   PUBMED   17008307
  REMARK    Review article
REFERENCE   9  (residues 1 to 901)
  AUTHORS   Kamnasaran,D., Chen,C.P., Devriendt,K., Mehta,L. and Cox,D.W.
  TITLE     Defining a holoprosencephaly locus on human chromosome 14q13 and
            characterization of potential candidate genes
  JOURNAL   Genomics 85 (5), 608-621 (2005)
   PUBMED   15820313
REFERENCE   10 (residues 1 to 901)
  AUTHORS   Kamnasaran,D., Muir,W.J., Ferguson-Smith,M.A. and Cox,D.W.
  TITLE     Disruption of the neuronal PAS3 gene in a family affected with
            schizophrenia
  JOURNAL   J Med Genet 40 (5), 325-332 (2003)
   PUBMED   12746393
  REMARK    GeneRIF: haploinsufficiency of NPAS3 contributes to the cause of
            schizophrenia
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109769.5, AF164438.1,
            AL157689.3 and AI811363.1.
            
            Summary: This gene encodes a member of the basic helix-loop-helix
            and PAS domain-containing family of transcription factors. The
            encoded protein is localized to the nucleus and may regulate genes
            involved in neurogenesis. Chromosomal abnormalities that affect the
            coding potential of this gene are associated with schizophrenia and
            cognitive disability. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (2) has multiple differences in
            the coding region but maintains the reading frame, compared to
            variant 1. This variant encodes isoform 2, which is shorter than
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY157302.1, AF164438.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245, SAMEA2155371
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..901
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.1"
     Protein         1..901
                     /product="neuronal PAS domain-containing protein 3 isoform
                     2"
                     /note="neuronal PAS domain-containing protein 3; member of
                     PAS protein 6; neuronal PAS3; PAS domain-containing
                     protein 6; basic-helix-loop-helix-PAS protein MOP6; class
                     E basic helix-loop-helix protein 12"
                     /calculated_mol_wt=96888
     Region          17..94
                     /region_name="bHLH-PAS_NPAS3_PASD6"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in neuronal PAS domain-containing protein 3
                     (NPAS3) and similar proteins; cd19732"
                     /db_xref="CDD:381575"
     Site            order(23,25..27,31,33..34,38,59..60)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381575"
     Site            order(33,36..37,40,43..44,47,49..50,61,64..66,68,70..74)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381575"
     Region          120..178
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Region          122..>381
                     /region_name="KinE"
                     /note="Sporulation sensor histidine kinase E [Cell cycle
                     control, cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG5809"
                     /db_xref="CDD:444511"
     Region          311..398
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(314,318,324,337..340,366,371)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(334,338,346,349..350,378,380)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          <404..>563
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     CDS             1..901
                     /gene="NPAS3"
                     /gene_synonym="bHLHe12; MOP6; PASD6"
                     /coded_by="NM_022123.3:439..3144"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9645.1"
                     /db_xref="GeneID:64067"
                     /db_xref="HGNC:HGNC:19311"
                     /db_xref="MIM:609430"
ORIGIN      
        1 maptkpsfqq dpsrrerlqa lrkeksrdaa rsrrgkenfe fyelakllpl paaitsqldk
       61 asiirltisy lkmrdfanqg dppwnlrmeg pppntsvkga qrrrspsala ievfeahlgs
      121 hilqsldgfv falnqegkfl yisetvsiyl glsqveltgs svfdyvhpgd hvemaeqlgm
      181 klppgrglls qgtaedgass assssqsetp epvestspsl lttdntlers ffirmkstlt
      241 krgvhikssg ykvihitgrl rlrvslshgr tvpsqimglv vvahalpppt inevridchm
      301 fvtrvnmdln iiycenrisd ymdltpvdiv gkrcyhfiha edvegirhsh ldllnkgqcv
      361 tkyyrwmqkn ggyiwiqssa tiainaknan ekniiwvnyl lsnpeykdtp mdiaqlphlp
      421 ektsessets dsesdskdts gitednensk sdekgnqsen sedpepdrkk sgnacdndmn
      481 cnddghsssn pdsrdsddsf ehsdfenpka gedgfgalga mqikveryve sesdlrlqnc
      541 esltsdsakd sdsageagaq asskhqkrkk rrkrqkggsa srrrlssass pggldaglve
      601 pprllsspns asvlkiktei sepinfdnds siwnyppnre isrnespysm tkppssehfp
      661 spqggggggg gggglhvaip dsvltppgad gaaarktqfg asataalapv asdplsppls
      721 asprdkhpgn gggggggggg aggggpsasn sllytgdlea lqrlqagnvv lplvhrvtgt
      781 laatstaaqr vyttgtirya paevtlamqs nllpnahavn fvdvnspgfg ldpktpmeml
      841 yhhvhrlnms gpfggavsaa sltqmpagnv fttaeglfst lpfpvysngi haaqtlerke
      901 d
//
LOCUS       NP_001381917             918 aa            linear   PRI 20-DEC-2025
DEFINITION  neuronal PAS domain-containing protein 3 isoform 5 [Homo sapiens].
ACCESSION   NP_001381917 XP_011535372
VERSION     NP_001381917.1
DBSOURCE    REFSEQ: accession NM_001394988.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 918)
  AUTHORS   Caporale,A.L., Cinalli,A.R., Rubinstein,M. and Franchini,L.F.
  TITLE     The Human Accelerated Region HAR202 Controls NPAS3 Expression in
            the Developing Forebrain Displaying Differential Enhancer Activity
            Between Modern and Archaic Human Sequences
  JOURNAL   Mol Biol Evol 41 (10) (2024)
   PUBMED   39241178
REFERENCE   2  (residues 1 to 918)
  AUTHORS   Pavesic Radonja,A., Blazevic Zelic,S., Rubesa,G. and Bradshaw,N.J.
  TITLE     SYMPTOM SEVERITY IN SCHIZOPHRENIA PATIENTS WITH NPAS3, DYSBINDIN-1
            AND/OR TRIOBP PROTEIN PATHOLOGY IN THEIR BLOOD SERUM: A PANSS-BASED
            FOLLOW UP STUDY
  JOURNAL   Psychiatr Danub 35 (2), 180-186 (2023)
   PUBMED   37480305
  REMARK    GeneRIF: SYMPTOM SEVERITY IN SCHIZOPHRENIA PATIENTS WITH NPAS3,
            DYSBINDIN-1 AND/OR TRIOBP PROTEIN PATHOLOGY IN THEIR BLOOD SERUM: A
            PANSS-BASED FOLLOW UP STUDY.
REFERENCE   3  (residues 1 to 918)
  AUTHORS   Li,Y., Fan,T., Li,X., Liu,L., Mao,F., Li,Y., Miao,Z., Zeng,C.,
            Song,W., Pan,J., Zhou,S., Wang,H., Wang,Y. and Sun,Z.S.
  TITLE     Npas3 deficiency impairs cortical astrogenesis and induces
            autistic-like behaviors
  JOURNAL   Cell Rep 40 (9), 111289 (2022)
   PUBMED   36044858
  REMARK    GeneRIF: Npas3 deficiency impairs cortical astrogenesis and induces
            autistic-like behaviors.
            Erratum:[Cell Rep. 2022 Nov 8;41(6):111551. doi:
            10.1016/j.celrep.2022.111551. PMID: 36351396]
REFERENCE   4  (residues 1 to 918)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 918)
  AUTHORS   Rossi,J.J., Rosenfeld,J.A., Chan,K.M., Streff,H., Nankivell,V.,
            Peet,D.J., Whitelaw,M.L. and Bersten,D.C.
  TITLE     Molecular characterisation of rare loss-of-function NPAS3 and NPAS4
            variants identified in individuals with neurodevelopmental
            disorders
  JOURNAL   Sci Rep 11 (1), 6602 (2021)
   PUBMED   33758288
  REMARK    GeneRIF: Molecular characterisation of rare loss-of-function NPAS3
            and NPAS4 variants identified in individuals with
            neurodevelopmental disorders.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 918)
  AUTHORS   Pickard,B.S., Christoforou,A., Thomson,P.A., Fawkes,A., Evans,K.L.,
            Morris,S.W., Porteous,D.J., Blackwood,D.H. and Muir,W.J.
  TITLE     Interacting haplotypes at the NPAS3 locus alter risk of
            schizophrenia and bipolar disorder
  JOURNAL   Mol Psychiatry 14 (9), 874-884 (2009)
   PUBMED   18317462
  REMARK    GeneRIF: This study demonstrated that these risk and protective
            effects act combinatorially, potentially multiplicatively, to
            determine NPAS3 gene-wide susceptibility in bipolar disorder and
            schizophrenia.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 918)
  AUTHORS   Uhl,G.R., Liu,Q.R., Drgon,T., Johnson,C., Walther,D., Rose,J.E.,
            David,S.P., Niaura,R. and Lerman,C.
  TITLE     Molecular genetics of successful smoking cessation: convergent
            genome-wide association study results
  JOURNAL   Arch Gen Psychiatry 65 (6), 683-693 (2008)
   PUBMED   18519826
  REMARK    GeneRIF: Clinical trial and genome-wide association study of
            gene-disease association, gene-environment interaction, and
            pharmacogenomic / toxicogenomic. (HuGE Navigator)
REFERENCE   8  (residues 1 to 918)
  AUTHORS   Pickard,B.S., Pieper,A.A., Porteous,D.J., Blackwood,D.H. and
            Muir,W.J.
  TITLE     The NPAS3 gene--emerging evidence for a role in psychiatric illness
  JOURNAL   Ann Med 38 (6), 439-448 (2006)
   PUBMED   17008307
  REMARK    Review article
REFERENCE   9  (residues 1 to 918)
  AUTHORS   Kamnasaran,D., Chen,C.P., Devriendt,K., Mehta,L. and Cox,D.W.
  TITLE     Defining a holoprosencephaly locus on human chromosome 14q13 and
            characterization of potential candidate genes
  JOURNAL   Genomics 85 (5), 608-621 (2005)
   PUBMED   15820313
REFERENCE   10 (residues 1 to 918)
  AUTHORS   Kamnasaran,D., Muir,W.J., Ferguson-Smith,M.A. and Cox,D.W.
  TITLE     Disruption of the neuronal PAS3 gene in a family affected with
            schizophrenia
  JOURNAL   J Med Genet 40 (5), 325-332 (2003)
   PUBMED   12746393
  REMARK    GeneRIF: haploinsufficiency of NPAS3 contributes to the cause of
            schizophrenia
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109769.5, AL139296.4,
            AL158802.1, AL161851.4 and AL157689.3.
            
            On May 13, 2021 this sequence version replaced XP_011535372.1.
            
            Summary: This gene encodes a member of the basic helix-loop-helix
            and PAS domain-containing family of transcription factors. The
            encoded protein is localized to the nucleus and may regulate genes
            involved in neurogenesis. Chromosomal abnormalities that affect the
            coding potential of this gene are associated with schizophrenia and
            cognitive disability. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: KJ534897.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155371, SAMEA2156099
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..918
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.1"
     Protein         1..918
                     /product="neuronal PAS domain-containing protein 3 isoform
                     5"
                     /note="neuronal PAS domain-containing protein 3; member of
                     PAS protein 6; neuronal PAS3; PAS domain-containing
                     protein 6; basic-helix-loop-helix-PAS protein MOP6; class
                     E basic helix-loop-helix protein 12"
                     /calculated_mol_wt=98911
     Region          17..94
                     /region_name="bHLH-PAS_NPAS3_PASD6"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in neuronal PAS domain-containing protein 3
                     (NPAS3) and similar proteins; cd19732"
                     /db_xref="CDD:381575"
     Site            order(23,25..27,31,33..34,38,59..60)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381575"
     Site            order(33,36..37,40,43..44,47,49..50,61,64..66,68,70..74)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381575"
     Region          137..195
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Region          139..>398
                     /region_name="KinE"
                     /note="Sporulation sensor histidine kinase E [Cell cycle
                     control, cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG5809"
                     /db_xref="CDD:444511"
     Region          328..415
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(331,335,341,354..357,383,388)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(351,355,363,366..367,395,397)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          <421..>580
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     CDS             1..918
                     /gene="NPAS3"
                     /gene_synonym="bHLHe12; MOP6; PASD6"
                     /coded_by="NM_001394988.1:439..3195"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:64067"
                     /db_xref="HGNC:HGNC:19311"
                     /db_xref="MIM:609430"
ORIGIN      
        1 maptkpsfqq dpsrrerlqa lrkeksrdaa rsrrgkenfe fyelakllpl paaitsqldk
       61 asiirltisy lkmrdfanqg dppwnlrmeg pppntsvkgi qmwkselcmr ktpcegaqrr
      121 rspsalaiev feahlgshil qsldgfvfal nqegkflyis etvsiylgls qveltgssvf
      181 dyvhpgdhve maeqlgmklp pgrgllsqgt aedgassass ssqsetpepv estspslltt
      241 dntlersffi rmkstltkrg vhikssgykv ihitgrlrlr vslshgrtvp sqimglvvva
      301 halppptine vridchmfvt rvnmdlniiy cenrisdymd ltpvdivgkr cyhfihaedv
      361 egirhshldl lnkgqcvtky yrwmqknggy iwiqssatia inaknanekn iiwvnyllsn
      421 peykdtpmdi aqlphlpekt sessetsdse sdskdtsgit ednensksde kgnqsensed
      481 pepdrkksgn acdndmncnd dghsssnpds rdsddsfehs dfenpkaged gfgalgamqi
      541 kveryveses dlrlqncesl tsdsakdsds ageagaqass khqkrkkrrk rqkggsasrr
      601 rlssasspgg ldaglveppr llsspnsasv lkikteisep infdndssiw nyppnreisr
      661 nespysmtkp pssehfpspq gggggggggg glhvaipdsv ltppgadgaa arktqfgasa
      721 taalapvasd plspplsasp rdkhpgnggg gggggggagg ggpsasnsll ytgdlealqr
      781 lqagnvvlpl vhrvtgtlaa tstaaqrvyt tgtiryapae vtlamqsnll pnahavnfvd
      841 vnspgfgldp ktpmemlyhh vhrlnmsgpf ggavsaaslt qmpagnvftt aeglfstlpf
      901 pvysngihaa qtlerked
//
LOCUS       NP_996772                889 aa            linear   PRI 21-DEC-2025
DEFINITION  disco-interacting protein 2 homolog A isoform b [Homo sapiens].
ACCESSION   NP_996772
VERSION     NP_996772.1
DBSOURCE    REFSEQ: accession NM_206889.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 889)
  AUTHORS   Zhang,B., Zhang,X., Omorou,M., Zhao,K., Ruan,Y. and Luan,H.
  TITLE     Disco interacting protein 2 homolog A (DIP2A): A key component in
            the regulation of brain disorders
  JOURNAL   Biomed Pharmacother 168, 115771 (2023)
   PUBMED   37897975
  REMARK    GeneRIF: Disco interacting protein 2 homolog A (DIP2A): A key
            component in the regulation of brain disorders.
            Review article
REFERENCE   2  (residues 1 to 889)
  AUTHORS   Mondal,S., Kinatukara,P., Singh,S., Shambhavi,S., Patil,G.S.,
            Dubey,N., Singh,S.H., Pal,B., Shekar,P.C., Kamat,S.S. and
            Sankaranarayanan,R.
  TITLE     DIP2 is a unique regulator of diacylglycerol lipid homeostasis in
            eukaryotes
  JOURNAL   Elife 11, e77665 (2022)
   PUBMED   35766356
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 889)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 889)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 889)
  AUTHORS   Ma,J., Zhang,L.Q., He,Z.X., He,X.X., Wang,Y.J., Jian,Y.L., Wang,X.,
            Zhang,B.B., Su,C., Lu,J., Huang,B.Q., Zhang,Y., Wang,G.Y.,
            Guo,W.X., Qiu,D.L., Mei,L., Xiong,W.C., Zheng,Y.W. and Zhu,X.J.
  TITLE     Autism candidate gene DIP2A regulates spine morphogenesis via
            acetylation of cortactin
  JOURNAL   PLoS Biol 17 (10), e3000461 (2019)
   PUBMED   31600191
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 889)
  AUTHORS   Winnepenninckx,B., Debacker,K., Ramsay,J., Smeets,D., Smits,A.,
            FitzPatrick,D.R. and Kooy,R.F.
  TITLE     CGG-repeat expansion in the DIP2B gene is associated with the
            fragile site FRA12A on chromosome 12q13.1
  JOURNAL   Am J Hum Genet 80 (2), 221-231 (2007)
   PUBMED   17236128
REFERENCE   7  (residues 1 to 889)
  AUTHORS   Casadei,R., Strippoli,P., D'Addabbo,P., Canaider,S., Lenzi,L.,
            Vitale,L., Giannone,S., Frabetti,F., Facchin,F., Carinci,P. and
            Zannotti,M.
  TITLE     mRNA 5' region sequence incompleteness: a potential source of
            systematic errors in translation initiation codon assignment in
            human mRNAs
  JOURNAL   Gene 321, 185-193 (2003)
   PUBMED   14637006
REFERENCE   8  (residues 1 to 889)
  AUTHORS   Mukhopadhyay,M., Pelka,P., DeSousa,D., Kablar,B., Schindler,A.,
            Rudnicki,M.A. and Campos,A.R.
  TITLE     Cloning, genomic organization and expression pattern of a novel
            Drosophila gene, the disco-interacting protein 2 (dip2), and its
            murine homolog
  JOURNAL   Gene 293 (1-2), 59-65 (2002)
   PUBMED   12137943
REFERENCE   9  (residues 1 to 889)
  AUTHORS   Gardiner,K., Slavov,D., Bechtel,L. and Davisson,M.
  TITLE     Annotation of human chromosome 21 for relevance to Down syndrome:
            gene structure and expression analysis
  JOURNAL   Genomics 79 (6), 833-843 (2002)
   PUBMED   12036298
REFERENCE   10 (residues 1 to 889)
  AUTHORS   Wang,Z., Tseng,C.P., Pong,R.C., Chen,H., McConnell,J.D., Navone,N.
            and Hsieh,J.T.
  TITLE     The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate
            cancer. Characterization of a novel GTPase-activating protein
            associated with N-terminal domain of DOC-2/DAB2
  JOURNAL   J Biol Chem 277 (15), 12622-12631 (2002)
   PUBMED   11812785
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000337.1, DA326960.1,
            AB273729.1 and BC038443.1.
            
            Summary: The protein encoded by this gene may be involved in axon
            patterning in the central nervous system. This gene is not highly
            expressed. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            coding region compared to variant 1, that causes a frameshift. The
            resulting isoform (b) is shorter and has a distinct C-terminus
            compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC038443.1, SRR9304717.741296.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..889
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..889
                     /product="disco-interacting protein 2 homolog A isoform b"
                     /EC_number="6.2.1.1"
                     /note="disco-interacting protein 2A; DIP2 homolog A; DIP2
                     disco-interacting protein 2 homolog A; disconnected
                     interacting protein 2 homolog A; disco interacting protein
                     2 homolog A"
                     /calculated_mol_wt=95870
     Region          10..123
                     /region_name="DMAP_binding"
                     /note="DMAP1-binding Domain; pfam06464"
                     /db_xref="CDD:368923"
     Region          60..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT5; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Region          283..286
                     /region_name="PXXP motif, required for interaction with
                     CTTN. /evidence=ECO:0000250|UniProtKB:Q8BWT5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          302..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          307..310
                     /region_name="PXXP motif, required for interaction with
                     CTTN. /evidence=ECO:0000250|UniProtKB:Q8BWT5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          351..880
                     /region_name="Dip2"
                     /note="Disco-interacting protein 2 (Dip2); cd05905"
                     /db_xref="CDD:341231"
     Site            order(512,515..520,522..523)
                     /site_type="other"
                     /note="putative acyl-activating enzyme (AAE) consensus
                     motif"
                     /db_xref="CDD:341231"
     Site            order(515,556..557,607,609..610,613,635..636,654..659,792,
                     804,807,815..818)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341231"
     Site            order(515,635..636,694..699,792,804,807,818)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Site            order(556,609..610,613,635,815..817,875)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341231"
     CDS             1..889
                     /gene="DIP2A"
                     /gene_synonym="C21orf106; DIP2"
                     /coded_by="NM_206889.3:242..2911"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS46656.1"
                     /db_xref="GeneID:23181"
                     /db_xref="HGNC:HGNC:17217"
                     /db_xref="MIM:607711"
ORIGIN      
        1 madrgcplea aplpaevres laelelelse gditqkgyek krakllaryi pliqgidpsl
       61 qaenripgps qttaaapkqq ksrptasrde rfrsdvhtea vqaalakyke rkmpmpskrr
      121 svlvhssvet ytppdtssas edegslrrpg rltstplqsh ssvepwldrv iqgsstsssa
      181 sstsshpggr pttapsaaat pgaaattala gleahthidl hsappdvttg lvehsyferp
      241 qvasvrsvpr gcsgsmleta dgvpvnsrvs skiqqllntl krpkrpplke ffvddfeell
      301 evqqpdpnqp kpegsetsvl rgepltagvp rppsllatlq rwgttqpksp cltaldttgk
      361 avytltygkl wsrslklayt llnkltskne pllkpgdrva lvfpnsdpvm fmvafygcll
      421 aelvpvpiev pltrkdagsq qvgfllgscg vflalttdac qkglpkaqtg evaafkgwpp
      481 lswlvidgkh lakppkdwhp laqdtgtgta yieyktskeg stvgvtvsha sllaqcralt
      541 qacgyseaet ltnvldfkrd aglwhgvlts vmnrmhvvsv pyalmkanpl swiqkvcfyk
      601 araalvksrd mhwsllaqrg qrdvslsslr mlivadganp wsisscdafl nvfqsrglrp
      661 evicpcassp ealtvairrp pdlggppprk avlsmnglsy gvirvdteek lsvltvqdvg
      721 qvmpganvcv vklegtpylc ktdevgeicv sssatgtayy gllgitknvf eavpvttgga
      781 pifdrpftrt gllgfigpdn lvfivgkldg lmvtgvrrhn addvvatala vepmkfvyrg
      841 riavfsvtvl hddrivlvae qrpdaseeds fqwmsrvlqv gaparpmvr
//
LOCUS       NP_996774                812 aa            linear   PRI 21-DEC-2025
DEFINITION  disco-interacting protein 2 homolog A isoform d [Homo sapiens].
ACCESSION   NP_996774
VERSION     NP_996774.1
DBSOURCE    REFSEQ: accession NM_206891.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 812)
  AUTHORS   Zhang,B., Zhang,X., Omorou,M., Zhao,K., Ruan,Y. and Luan,H.
  TITLE     Disco interacting protein 2 homolog A (DIP2A): A key component in
            the regulation of brain disorders
  JOURNAL   Biomed Pharmacother 168, 115771 (2023)
   PUBMED   37897975
  REMARK    GeneRIF: Disco interacting protein 2 homolog A (DIP2A): A key
            component in the regulation of brain disorders.
            Review article
REFERENCE   2  (residues 1 to 812)
  AUTHORS   Mondal,S., Kinatukara,P., Singh,S., Shambhavi,S., Patil,G.S.,
            Dubey,N., Singh,S.H., Pal,B., Shekar,P.C., Kamat,S.S. and
            Sankaranarayanan,R.
  TITLE     DIP2 is a unique regulator of diacylglycerol lipid homeostasis in
            eukaryotes
  JOURNAL   Elife 11, e77665 (2022)
   PUBMED   35766356
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 812)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 812)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 812)
  AUTHORS   Ma,J., Zhang,L.Q., He,Z.X., He,X.X., Wang,Y.J., Jian,Y.L., Wang,X.,
            Zhang,B.B., Su,C., Lu,J., Huang,B.Q., Zhang,Y., Wang,G.Y.,
            Guo,W.X., Qiu,D.L., Mei,L., Xiong,W.C., Zheng,Y.W. and Zhu,X.J.
  TITLE     Autism candidate gene DIP2A regulates spine morphogenesis via
            acetylation of cortactin
  JOURNAL   PLoS Biol 17 (10), e3000461 (2019)
   PUBMED   31600191
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 812)
  AUTHORS   Winnepenninckx,B., Debacker,K., Ramsay,J., Smeets,D., Smits,A.,
            FitzPatrick,D.R. and Kooy,R.F.
  TITLE     CGG-repeat expansion in the DIP2B gene is associated with the
            fragile site FRA12A on chromosome 12q13.1
  JOURNAL   Am J Hum Genet 80 (2), 221-231 (2007)
   PUBMED   17236128
REFERENCE   7  (residues 1 to 812)
  AUTHORS   Casadei,R., Strippoli,P., D'Addabbo,P., Canaider,S., Lenzi,L.,
            Vitale,L., Giannone,S., Frabetti,F., Facchin,F., Carinci,P. and
            Zannotti,M.
  TITLE     mRNA 5' region sequence incompleteness: a potential source of
            systematic errors in translation initiation codon assignment in
            human mRNAs
  JOURNAL   Gene 321, 185-193 (2003)
   PUBMED   14637006
REFERENCE   8  (residues 1 to 812)
  AUTHORS   Mukhopadhyay,M., Pelka,P., DeSousa,D., Kablar,B., Schindler,A.,
            Rudnicki,M.A. and Campos,A.R.
  TITLE     Cloning, genomic organization and expression pattern of a novel
            Drosophila gene, the disco-interacting protein 2 (dip2), and its
            murine homolog
  JOURNAL   Gene 293 (1-2), 59-65 (2002)
   PUBMED   12137943
REFERENCE   9  (residues 1 to 812)
  AUTHORS   Gardiner,K., Slavov,D., Bechtel,L. and Davisson,M.
  TITLE     Annotation of human chromosome 21 for relevance to Down syndrome:
            gene structure and expression analysis
  JOURNAL   Genomics 79 (6), 833-843 (2002)
   PUBMED   12036298
REFERENCE   10 (residues 1 to 812)
  AUTHORS   Wang,Z., Tseng,C.P., Pong,R.C., Chen,H., McConnell,J.D., Navone,N.
            and Hsieh,J.T.
  TITLE     The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate
            cancer. Characterization of a novel GTPase-activating protein
            associated with N-terminal domain of DOC-2/DAB2
  JOURNAL   J Biol Chem 277 (15), 12622-12631 (2002)
   PUBMED   11812785
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000337.1, DA326960.1,
            AB273729.1, AF432263.1 and CK821329.1.
            
            Summary: The protein encoded by this gene may be involved in axon
            patterning in the central nervous system. This gene is not highly
            expressed. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (4) differs in the 3' UTR and
            coding region compared to variant 1, that causes a frameshift. The
            resulting isoform (d) is shorter and has a distinct C-terminus
            compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.135789.1,
                                           SRR1660807.201991.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..812
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..812
                     /product="disco-interacting protein 2 homolog A isoform d"
                     /EC_number="6.2.1.1"
                     /note="disco-interacting protein 2A; DIP2 homolog A; DIP2
                     disco-interacting protein 2 homolog A; disconnected
                     interacting protein 2 homolog A; disco interacting protein
                     2 homolog A"
                     /calculated_mol_wt=87207
     Region          10..123
                     /region_name="DMAP_binding"
                     /note="DMAP1-binding Domain; pfam06464"
                     /db_xref="CDD:368923"
     Region          60..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT5; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Region          283..286
                     /region_name="PXXP motif, required for interaction with
                     CTTN. /evidence=ECO:0000250|UniProtKB:Q8BWT5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          302..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          307..310
                     /region_name="PXXP motif, required for interaction with
                     CTTN. /evidence=ECO:0000250|UniProtKB:Q8BWT5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          351..>802
                     /region_name="Adenylate forming domain, Class I
                     superfamily"
                     /note="This family includes acyl- and aryl-CoA ligases, as
                     well as the adenylation domain of nonribosomal peptide
                     synthetases and firefly luciferases. The adenylate-forming
                     enzymes catalyze an ATP-dependent two-step reaction to
                     first activate a carboxylate...; cl17068"
                     /db_xref="CDD:473059"
     Site            order(512,515..520,522..523)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341228"
     CDS             1..812
                     /gene="DIP2A"
                     /gene_synonym="C21orf106; DIP2"
                     /coded_by="NM_206891.3:242..2680"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:23181"
                     /db_xref="HGNC:HGNC:17217"
                     /db_xref="MIM:607711"
ORIGIN      
        1 madrgcplea aplpaevres laelelelse gditqkgyek krakllaryi pliqgidpsl
       61 qaenripgps qttaaapkqq ksrptasrde rfrsdvhtea vqaalakyke rkmpmpskrr
      121 svlvhssvet ytppdtssas edegslrrpg rltstplqsh ssvepwldrv iqgsstsssa
      181 sstsshpggr pttapsaaat pgaaattala gleahthidl hsappdvttg lvehsyferp
      241 qvasvrsvpr gcsgsmleta dgvpvnsrvs skiqqllntl krpkrpplke ffvddfeell
      301 evqqpdpnqp kpegsetsvl rgepltagvp rppsllatlq rwgttqpksp cltaldttgk
      361 avytltygkl wsrslklayt llnkltskne pllkpgdrva lvfpnsdpvm fmvafygcll
      421 aelvpvpiev pltrkdagsq qvgfllgscg vflalttdac qkglpkaqtg evaafkgwpp
      481 lswlvidgkh lakppkdwhp laqdtgtgta yieyktskeg stvgvtvsha sllaqcralt
      541 qacgyseaet ltnvldfkrd aglwhgvlts vmnrmhvvsv pyalmkanpl swiqkvcfyk
      601 araalvksrd mhwsllaqrg qrdvslsslr mlivadganp wsisscdafl nvfqsrglrp
      661 evicpcassp ealtvairrp pdlggppprk avlsmnglsy gvirvdteek lsvltvqdvg
      721 qvmpganvcv vklegtpylc ktdevgeicv sssatgtayy gllgitknvf eavpvttgga
      781 pifdrpftrt gllgfigpvs mssctstgsq rr
//
LOCUS       NP_001340871            1572 aa            linear   PRI 21-DEC-2025
DEFINITION  disco-interacting protein 2 homolog A isoform h [Homo sapiens].
ACCESSION   NP_001340871
VERSION     NP_001340871.1
DBSOURCE    REFSEQ: accession NM_001353942.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1572)
  AUTHORS   Zhang,B., Zhang,X., Omorou,M., Zhao,K., Ruan,Y. and Luan,H.
  TITLE     Disco interacting protein 2 homolog A (DIP2A): A key component in
            the regulation of brain disorders
  JOURNAL   Biomed Pharmacother 168, 115771 (2023)
   PUBMED   37897975
  REMARK    GeneRIF: Disco interacting protein 2 homolog A (DIP2A): A key
            component in the regulation of brain disorders.
            Review article
REFERENCE   2  (residues 1 to 1572)
  AUTHORS   Mondal,S., Kinatukara,P., Singh,S., Shambhavi,S., Patil,G.S.,
            Dubey,N., Singh,S.H., Pal,B., Shekar,P.C., Kamat,S.S. and
            Sankaranarayanan,R.
  TITLE     DIP2 is a unique regulator of diacylglycerol lipid homeostasis in
            eukaryotes
  JOURNAL   Elife 11, e77665 (2022)
   PUBMED   35766356
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1572)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 1572)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1572)
  AUTHORS   Ma,J., Zhang,L.Q., He,Z.X., He,X.X., Wang,Y.J., Jian,Y.L., Wang,X.,
            Zhang,B.B., Su,C., Lu,J., Huang,B.Q., Zhang,Y., Wang,G.Y.,
            Guo,W.X., Qiu,D.L., Mei,L., Xiong,W.C., Zheng,Y.W. and Zhu,X.J.
  TITLE     Autism candidate gene DIP2A regulates spine morphogenesis via
            acetylation of cortactin
  JOURNAL   PLoS Biol 17 (10), e3000461 (2019)
   PUBMED   31600191
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1572)
  AUTHORS   Winnepenninckx,B., Debacker,K., Ramsay,J., Smeets,D., Smits,A.,
            FitzPatrick,D.R. and Kooy,R.F.
  TITLE     CGG-repeat expansion in the DIP2B gene is associated with the
            fragile site FRA12A on chromosome 12q13.1
  JOURNAL   Am J Hum Genet 80 (2), 221-231 (2007)
   PUBMED   17236128
REFERENCE   7  (residues 1 to 1572)
  AUTHORS   Casadei,R., Strippoli,P., D'Addabbo,P., Canaider,S., Lenzi,L.,
            Vitale,L., Giannone,S., Frabetti,F., Facchin,F., Carinci,P. and
            Zannotti,M.
  TITLE     mRNA 5' region sequence incompleteness: a potential source of
            systematic errors in translation initiation codon assignment in
            human mRNAs
  JOURNAL   Gene 321, 185-193 (2003)
   PUBMED   14637006
REFERENCE   8  (residues 1 to 1572)
  AUTHORS   Mukhopadhyay,M., Pelka,P., DeSousa,D., Kablar,B., Schindler,A.,
            Rudnicki,M.A. and Campos,A.R.
  TITLE     Cloning, genomic organization and expression pattern of a novel
            Drosophila gene, the disco-interacting protein 2 (dip2), and its
            murine homolog
  JOURNAL   Gene 293 (1-2), 59-65 (2002)
   PUBMED   12137943
REFERENCE   9  (residues 1 to 1572)
  AUTHORS   Gardiner,K., Slavov,D., Bechtel,L. and Davisson,M.
  TITLE     Annotation of human chromosome 21 for relevance to Down syndrome:
            gene structure and expression analysis
  JOURNAL   Genomics 79 (6), 833-843 (2002)
   PUBMED   12036298
REFERENCE   10 (residues 1 to 1572)
  AUTHORS   Wang,Z., Tseng,C.P., Pong,R.C., Chen,H., McConnell,J.D., Navone,N.
            and Hsieh,J.T.
  TITLE     The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate
            cancer. Characterization of a novel GTPase-activating protein
            associated with N-terminal domain of DOC-2/DAB2
  JOURNAL   J Biol Chem 277 (15), 12622-12631 (2002)
   PUBMED   11812785
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000337.1 and AP000338.3.
            
            Summary: The protein encoded by this gene may be involved in axon
            patterning in the central nervous system. This gene is not highly
            expressed. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (8) represents the longest
            transcript and encodes the longest isoform (h).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2630694.1,
                                           SRR1660809.10423.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1572
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..1572
                     /product="disco-interacting protein 2 homolog A isoform h"
                     /EC_number="6.2.1.1"
                     /note="disco-interacting protein 2A; DIP2 homolog A; DIP2
                     disco-interacting protein 2 homolog A; disconnected
                     interacting protein 2 homolog A; disco interacting protein
                     2 homolog A"
                     /calculated_mol_wt=170310
     Region          10..123
                     /region_name="DMAP_binding"
                     /note="DMAP1-binding Domain; pfam06464"
                     /db_xref="CDD:368923"
     Region          60..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT5; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Region          284..287
                     /region_name="PXXP motif, required for interaction with
                     CTTN. /evidence=ECO:0000250|UniProtKB:Q8BWT5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          303..328
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          308..311
                     /region_name="PXXP motif, required for interaction with
                     CTTN. /evidence=ECO:0000250|UniProtKB:Q8BWT5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          352..928
                     /region_name="Dip2"
                     /note="Disco-interacting protein 2 (Dip2); cd05905"
                     /db_xref="CDD:341231"
     Site            order(513,516..521,523..524)
                     /site_type="other"
                     /note="putative acyl-activating enzyme (AAE) consensus
                     motif"
                     /db_xref="CDD:341231"
     Site            order(516,636..637,695..700,793,805,808,819,908)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Site            order(516,557..558,608,610..611,614,636..637,655..660,793,
                     805,808,816..819,889)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341231"
     Site            order(557,610..611,614,636,816..818,876,889)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Region          1004..1568
                     /region_name="Dip2"
                     /note="Disco-interacting protein 2 (Dip2); cd05905"
                     /db_xref="CDD:341231"
     Site            order(1153,1156..1161,1163..1164)
                     /site_type="other"
                     /note="putative acyl-activating enzyme (AAE) consensus
                     motif"
                     /db_xref="CDD:341231"
     Site            order(1156,1282..1283,1337..1342,1433,1455,1458,1469,1548)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Site            order(1156,1197..1198,1248,1250..1251,1254,1282..1283,
                     1300..1305,1433,1455,1458,1466..1469,1529)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341231"
     Site            order(1197,1250..1251,1254,1282,1466..1468,1516,1529)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341231"
     CDS             1..1572
                     /gene="DIP2A"
                     /gene_synonym="C21orf106; DIP2"
                     /coded_by="NM_001353942.2:242..4960"
                     /note="isoform h is encoded by transcript variant 8"
                     /db_xref="GeneID:23181"
                     /db_xref="HGNC:HGNC:17217"
                     /db_xref="MIM:607711"
ORIGIN      
        1 madrgcplea aplpaevres laelelelse gditqkgyek krakllaryi pliqgidpsl
       61 qaenripgps qttaaapkqq ksrptasrde rfrsdvhtea vqaalakyke rkmpmpskrr
      121 svlvhssvet ytppdtssas edegslrrpg rltstplqsh ssvepwldrv iqgsstsssa
      181 sstsshpggr pttapsaaat pgaaattala gleahthiad lhsappdvtt glvehsyfer
      241 pqvasvrsvp rgcsgsmlet adgvpvnsrv sskiqqllnt lkrpkrpplk effvddfeel
      301 levqqpdpnq pkpegsetsv lrgepltagv prppsllatl qrwgttqpks pcltaldttg
      361 kavytltygk lwsrslklay tllnkltskn epllkpgdrv alvfpnsdpv mfmvafygcl
      421 laelvpvpie vpltrkdags qqvgfllgsc gvflalttda cqkglpkaqt gevaafkgwp
      481 plswlvidgk hlakppkdwh plaqdtgtgt ayieyktske gstvgvtvsh asllaqcral
      541 tqacgyseae tltnvldfkr daglwhgvlt svmnrmhvvs vpyalmkanp lswiqkvcfy
      601 karaalvksr dmhwsllaqr gqrdvslssl rmlivadgan pwsisscdaf lnvfqsrglr
      661 pevicpcass pealtvairr ppdlggpppr kavlsmngls ygvirvdtee klsvltvqdv
      721 gqvmpganvc vvklegtpyl cktdevgeic vsssatgtay ygllgitknv feavpvttgg
      781 apifdrpftr tgllgfigpd nlvfivgkld glmvtgvrrh naddvvatal avepmkfvyr
      841 griavfsvtv lhddrivlva eqrpdaseed sfqwmsrvlq aidsihqvgv yclalvpant
      901 lpkaplggih isetkqrfle gtlhpcnvlm cphtcvtnlp kprqkqpevg pasmivgnlv
      961 agkriaqasg relahledsd qarkflflad vlqwrahttp dhplflllna kgtvtstatc
     1021 vqlhkraerv aaalmekgrl svgdhvalvy ppgvdliaaf ygclycgcvp vtvrpphpqn
     1081 lgttlptvkm ivevsksacv lttqavtrll rskeaaaavd irtwptildt ddipkkkias
     1141 vfrppspdvl ayldfsvstt gilagvkmsh aatsalcrsi klqcelypsr qiaicldpyc
     1201 glgfalwclc svysghqsvl vpplelesnv slwlsavsqy karvtfcsys vmemctkglg
     1261 aqtgvlrmkg vnlscvrtcm vvaeerpria ltqsfsklfk dlglparavs ttfgcrvnva
     1321 iclqgtagpd pttvyvdmra lrhdrvrlve rgsphslplm esgkilpgvk viiahtetkg
     1381 plgdshlgei wvssphnatg yytvygeeal hadhfsarls fgdtqtiwar tgylgflrrt
     1441 eltdasggrh dalyvvgsld etlelrgmry hpidietsvi rahrsiaeca vftwtnllvv
     1501 vveldgleqd aldlvalvtn vvleehylvv gvvvivdpgv ipinsrgekq rmhlrdgfla
     1561 dqldpiyvay nm
//
LOCUS       NP_001350827             467 aa            linear   PRI 21-DEC-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase FTO isoform 6 [Homo
            sapiens].
ACCESSION   NP_001350827
VERSION     NP_001350827.1
DBSOURCE    REFSEQ: accession NM_001363898.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Li,B., Wang,L., Du,M. and He,H.
  TITLE     FTO in oral diseases: Functions, mechanisms, and therapeutic
            potential
  JOURNAL   FASEB J 38 (20), e70115 (2024)
   PUBMED   39436191
  REMARK    GeneRIF: FTO in oral diseases: Functions, mechanisms, and
            therapeutic potential.
            Review article
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Li,Q. and Mu,S.
  TITLE     FTO mediates the diabetic kidney disease progression through
            regulating the m6A modification of NLRP3
  JOURNAL   BMC Nephrol 25 (1), 345 (2024)
   PUBMED   39390397
  REMARK    GeneRIF: FTO mediates the diabetic kidney disease progression
            through regulating the m[6]A modification of NLRP3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Shan,L., Tao,M., Zhang,W., Zhao,J.D., Liu,X.C., Fang,Z.H. and
            Gao,J.R.
  TITLE     Comprehensive analysis of the m6A demethylase FTO in endothelial
            dysfunction by MeRIP sequencing
  JOURNAL   Exp Cell Res 442 (2), 114268 (2024)
   PUBMED   39343042
  REMARK    GeneRIF: Comprehensive analysis of the m[6]A demethylase FTO in
            endothelial dysfunction by MeRIP sequencing.
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Nabeel-Shah,S., Pu,S., Burke,G.L., Ahmed,N., Braunschweig,U.,
            Farhangmehr,S., Lee,H., Wu,M., Ni,Z., Tang,H., Zhong,G., Marcon,E.,
            Zhang,Z., Blencowe,B.J. and Greenblatt,J.F.
  TITLE     Recruitment of the m6A/m6Am demethylase FTO to target RNAs by the
            telomeric zinc finger protein ZBTB48
  JOURNAL   Genome Biol 25 (1), 246 (2024)
   PUBMED   39300486
  REMARK    GeneRIF: Recruitment of the m[6]A/m6Am demethylase FTO to target
            RNAs by the telomeric zinc finger protein ZBTB48.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Hussain,M., Waheed,A., Elahi,A. and Mustafa,G.
  TITLE     Fat Mass and Obesity-Related (FTO) Gene Variant Is a Predictor of
            CVD in T2DM Patients
  JOURNAL   J Diabetes Res 2024, 5914316 (2024)
   PUBMED   39257882
  REMARK    GeneRIF: Fat Mass and Obesity-Related (FTO) Gene Variant Is a
            Predictor of CVD in T2DM Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Zeggini,E., Weedon,M.N., Lindgren,C.M., Frayling,T.M.,
            Elliott,K.S., Lango,H., Timpson,N.J., Perry,J.R., Rayner,N.W.,
            Freathy,R.M., Barrett,J.C., Shields,B., Morris,A.P., Ellard,S.,
            Groves,C.J., Harries,L.W., Marchini,J.L., Owen,K.R., Knight,B.,
            Cardon,L.R., Walker,M., Hitman,G.A., Morris,A.D., Doney,A.S.,
            McCarthy,M.I. and Hattersley,A.T.
  CONSRTM   Wellcome Trust Case Control Consortium (WTCCC)
  TITLE     Replication of genome-wide association signals in UK samples
            reveals risk loci for type 2 diabetes
  JOURNAL   Science 316 (5829), 1336-1341 (2007)
   PUBMED   17463249
  REMARK    Erratum:[Science. 2007 Aug 24;317(5841):1035-6]
REFERENCE   7  (residues 1 to 467)
  AUTHORS   Scott,L.J., Mohlke,K.L., Bonnycastle,L.L., Willer,C.J., Li,Y.,
            Duren,W.L., Erdos,M.R., Stringham,H.M., Chines,P.S., Jackson,A.U.,
            Prokunina-Olsson,L., Ding,C.J., Swift,A.J., Narisu,N., Hu,T.,
            Pruim,R., Xiao,R., Li,X.Y., Conneely,K.N., Riebow,N.L., Sprau,A.G.,
            Tong,M., White,P.P., Hetrick,K.N., Barnhart,M.W., Bark,C.W.,
            Goldstein,J.L., Watkins,L., Xiang,F., Saramies,J., Buchanan,T.A.,
            Watanabe,R.M., Valle,T.T., Kinnunen,L., Abecasis,G.R., Pugh,E.W.,
            Doheny,K.F., Bergman,R.N., Tuomilehto,J., Collins,F.S. and
            Boehnke,M.
  TITLE     A genome-wide association study of type 2 diabetes in Finns detects
            multiple susceptibility variants
  JOURNAL   Science 316 (5829), 1341-1345 (2007)
   PUBMED   17463248
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 467)
  AUTHORS   Dina,C., Meyre,D., Gallina,S., Durand,E., Korner,A., Jacobson,P.,
            Carlsson,L.M., Kiess,W., Vatin,V., Lecoeur,C., Delplanque,J.,
            Vaillant,E., Pattou,F., Ruiz,J., Weill,J., Levy-Marchal,C.,
            Horber,F., Potoczna,N., Hercberg,S., Le Stunff,C., Bougneres,P.,
            Kovacs,P., Marre,M., Balkau,B., Cauchi,S., Chevre,J.C. and
            Froguel,P.
  TITLE     Variation in FTO contributes to childhood obesity and severe adult
            obesity
  JOURNAL   Nat Genet 39 (6), 724-726 (2007)
   PUBMED   17496892
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            GeneRIF: Association with obesity in adult and childre.
            Interestingly, this association receives clear confirmation under a
            Transmission Disequilibrium Test design which is robust to
            population stratification.
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Frayling,T.M., Timpson,N.J., Weedon,M.N., Zeggini,E., Freathy,R.M.,
            Lindgren,C.M., Perry,J.R., Elliott,K.S., Lango,H., Rayner,N.W.,
            Shields,B., Harries,L.W., Barrett,J.C., Ellard,S., Groves,C.J.,
            Knight,B., Patch,A.M., Ness,A.R., Ebrahim,S., Lawlor,D.A.,
            Ring,S.M., Ben-Shlomo,Y., Jarvelin,M.R., Sovio,U., Bennett,A.J.,
            Melzer,D., Ferrucci,L., Loos,R.J., Barroso,I., Wareham,N.J.,
            Karpe,F., Owen,K.R., Cardon,L.R., Walker,M., Hitman,G.A.,
            Palmer,C.N., Doney,A.S., Morris,A.D., Smith,G.D., Hattersley,A.T.
            and McCarthy,M.I.
  TITLE     A common variant in the FTO gene is associated with body mass index
            and predisposes to childhood and adult obesity
  JOURNAL   Science 316 (5826), 889-894 (2007)
   PUBMED   17434869
  REMARK    GeneRIF: A genome-wide search for type 2 diabetes-susceptibility
            genes identified a common variant in the FTO gene that predisposes
            to diabetes through an effect on body mass index
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-environment interaction. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 467)
  AUTHORS   Peters,T., Ausmeier,K. and Ruther,U.
  TITLE     Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft)
            mouse mutation
  JOURNAL   Mamm Genome 10 (10), 983-986 (1999)
   PUBMED   10501967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007909.8, AC007496.6 and
            AC007347.3.
            
            Summary: This gene is a nuclear protein of the AlkB related
            non-haem iron and 2-oxoglutarate-dependent oxygenase superfamily
            but the exact physiological function of this gene is not known.
            Other non-heme iron enzymes function to reverse alkylated DNA and
            RNA damage by oxidative demethylation. Studies in mice and humans
            indicate a role in nervous and cardiovascular systems and a strong
            association with body mass index, obesity risk, and type 2
            diabetes. [provided by RefSeq, Jul 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.91779.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151741, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..467
                     /product="alpha-ketoglutarate-dependent dioxygenase FTO
                     isoform 6"
                     /EC_number="1.14.11.53"
                     /note="alpha-ketoglutarate-dependent dioxygenase FTO; fat
                     mass and obesity-associated protein; AlkB homolog 9; fat
                     mass and obesity associated; m6A(m)-demethylase FTO; tRNA
                     N1-methyl adenine demethylase FTO; mRNA
                     N(6)-methyladenosine demethylase FTO; mRNA
                     (2'-O-methyladenosine-N(6)-)-demethylase FTO; U6 small
                     nuclear RNA N(6)-methyladenosine-demethylase FTO; U6 small
                     nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO;
                     intragenic FTO exon 9 containing transcript; mRNA
                     N(6)-methyladenine demethylase"
                     /calculated_mol_wt=53963
     Region          36..335
                     /region_name="FTO_NTD"
                     /note="FTO catalytic domain; pfam12933"
                     /db_xref="CDD:463755"
     Region          <330..460
                     /region_name="FTO_CTD"
                     /note="FTO C-terminal domain; pfam12934"
                     /db_xref="CDD:432887"
     CDS             1..467
                     /gene="FTO"
                     /gene_synonym="ALKBH9; BMIQ14; GDFD; IFEX9"
                     /coded_by="NM_001363898.2:30..1433"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:79068"
                     /db_xref="HGNC:HGNC:24678"
                     /db_xref="MIM:610966"
ORIGIN      
        1 mkrtptaeer ereakklrll eeledtwlpy ltpkddefyq qwqlkypkli lreassvsee
       61 lhkevqeafl tlhkhgclfr dlvriqgkdl ltpvsrilig npgctykyln trlftvpwpv
      121 kgsnikhtea eiaaacetfl klndylqiet iqaleelaak ekanedavpl cmsadfprvg
      181 mgssyngqde vdiksraayn vtllnfmdpq kmpylkeepy fgmgkmavsw hhdenlvdrs
      241 avavysysce gtvcswkkqp cpeeesedds hlegrdpdiw hvgfkiswdi etpglaiplh
      301 qgdcyfmldd lnathqhcvl agsqprfsst hrvaevefew lrqfwfqgnr yrkctdwwcq
      361 pmaqlealwk kmegvtnavl hevkreglpv eqrneiltai lasltarqnl rrewharcqs
      421 riartlpadq kpecrpywek ddasmplpfd ltdivselrg qlleakp
//
LOCUS       NP_001401183            1462 aa            linear   PRI 21-DEC-2025
DEFINITION  low-density lipoprotein receptor-related protein 6 isoform i [Homo
            sapiens].
ACCESSION   NP_001401183
VERSION     NP_001401183.1
DBSOURCE    REFSEQ: accession NM_001414254.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1462)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1462)
  AUTHORS   Zhong,S., Guo,Q., Chen,X., Luo,X., Long,Y., Chong,T., Ye,M., He,H.,
            Lu,A., Ao,K., Yin,M., Xu,A., Li,X., Hao,Y. and Guo,X.
  TITLE     The inhibition of YTHDF3/m6A/LRP6 reprograms fatty acid metabolism
            and suppresses lymph node metastasis in cervical cancer
  JOURNAL   Int J Biol Sci 20 (3), 916-936 (2024)
   PUBMED   38250152
  REMARK    GeneRIF: The inhibition of YTHDF3/m[6]A/LRP6 reprograms fatty acid
            metabolism and suppresses lymph node metastasis in cervical cancer.
            Erratum:[Int J Biol Sci. 2025 Jun 5;21(8):3825-3826. doi:
            10.7150/ijbs.115928. PMID: 40520018]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1462)
  AUTHORS   Li,J., Liu,Z., Ren,Y., Shao,H. and Li,S.
  TITLE     LRP5-/6 gene polymorphisms and its association with risk of
            abnormal bone mass in postmenopausal women
  JOURNAL   J Orthop Surg Res 18 (1), 369 (2023)
   PUBMED   37202775
  REMARK    GeneRIF: LRP5-/6 gene polymorphisms and its association with risk
            of abnormal bone mass in postmenopausal women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1462)
  AUTHORS   Hao,H., Liu,Q., Chen,J. and Zhou,H.
  TITLE     Overexpression of circRNAs LRP6 in gestational diabetes mellitus
            predicts foetal malformation and intrauterine death
  JOURNAL   Endocrinol Diabetes Nutr (Engl Ed) 70 (2), 124-129 (2023)
   PUBMED   36925229
  REMARK    GeneRIF: Overexpression of circRNAs LRP6 in gestational diabetes
            mellitus predicts foetal malformation and intrauterine death.
REFERENCE   5  (residues 1 to 1462)
  AUTHORS   Wang,J., Yang,H., Ma,X., Liu,J., Li,L., Chen,L. and Wei,F.
  TITLE     LRP6/filamentous-actin signaling facilitates osteogenic commitment
            in mechanically induced periodontal ligament stem cells
  JOURNAL   Cell Mol Biol Lett 28 (1), 7 (2023)
   PUBMED   36694134
  REMARK    GeneRIF: LRP6/filamentous-actin signaling facilitates osteogenic
            commitment in mechanically induced periodontal ligament stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1462)
  AUTHORS   Bafico,A., Liu,G., Yaniv,A., Gazit,A. and Aaronson,S.A.
  TITLE     Novel mechanism of Wnt signalling inhibition mediated by Dickkopf-1
            interaction with LRP6/Arrow
  JOURNAL   Nat Cell Biol 3 (7), 683-686 (2001)
   PUBMED   11433302
REFERENCE   7  (residues 1 to 1462)
  AUTHORS   Mao,B., Wu,W., Li,Y., Hoppe,D., Stannek,P., Glinka,A. and Niehrs,C.
  TITLE     LDL-receptor-related protein 6 is a receptor for Dickkopf proteins
  JOURNAL   Nature 411 (6835), 321-325 (2001)
   PUBMED   11357136
REFERENCE   8  (residues 1 to 1462)
  AUTHORS   Tamai,K., Semenov,M., Kato,Y., Spokony,R., Liu,C., Katsuyama,Y.,
            Hess,F., Saint-Jeannet,J.P. and He,X.
  TITLE     LDL-receptor-related proteins in Wnt signal transduction
  JOURNAL   Nature 407 (6803), 530-535 (2000)
   PUBMED   11029007
REFERENCE   9  (residues 1 to 1462)
  AUTHORS   Baens,M., Wlodarska,I., Corveleyn,A., Hoornaert,I., Hagemeijer,A.
            and Marynen,P.
  TITLE     A physical, transcript, and deletion map of chromosome region
            12p12.3 flanked by ETV6 and CDKN1B: hypermethylation of the LRP6
            CpG island in two leukemia patients with hemizygous del(12p)
  JOURNAL   Genomics 56 (1), 40-50 (1999)
   PUBMED   10036184
REFERENCE   10 (residues 1 to 1462)
  AUTHORS   Brown,S.D., Twells,R.C., Hey,P.J., Cox,R.D., Levy,E.R.,
            Soderman,A.R., Metzker,M.L., Caskey,C.T., Todd,J.A. and Hess,J.F.
  TITLE     Isolation and characterization of LRP6, a novel member of the low
            density lipoprotein receptor gene family
  JOURNAL   Biochem Biophys Res Commun 248 (3), 879-888 (1998)
   PUBMED   9704021
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007621.34, AC007537.3 and
            KF455603.1.
            
            Summary: This gene encodes a member of the low density lipoprotein
            (LDL) receptor gene family. LDL receptors are transmembrane cell
            surface proteins involved in receptor-mediated endocytosis of
            lipoprotein and protein ligands. The protein encoded by this gene
            functions as a receptor or, with Frizzled, a co-receptor for Wnt
            and thereby transmits the canonical Wnt/beta-catenin signaling
            cascade. Through its interaction with the Wnt/beta-catenin
            signaling cascade this gene plays a role in the regulation of cell
            differentiation, proliferation, and migration and the development
            of many cancer types. This protein undergoes gamma-secretase
            dependent RIP- (regulated intramembrane proteolysis) processing but
            the precise locations of the cleavage sites have not been
            determined.[provided by RefSeq, Dec 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1514145.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..1462
                     /product="low-density lipoprotein receptor-related protein
                     6 isoform i"
                     /note="low-density lipoprotein receptor-related protein 6;
                     LRP-6"
                     /calculated_mol_wt=163681
     Region          1..40
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          24..65
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          66..100
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          135..172
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          202..242
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          246..286
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          307..348
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          332..373
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          374..407
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          441..476
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          <503..662
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          546..588
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          676..715
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          742..778
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          807..847
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          <817..924
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          943..985
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1056..1092
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1098..1134
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1103,1113,1124..1125)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1117,1120,1124,1130..1131)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1127..1131
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1137..1171
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1142,1150,1161..1162)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1154,1157,1161,1167..1168)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1164..1168
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1175..1209
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1180,1188,1199..1200)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1192,1195,1199,1205..1206)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1202..1206
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     CDS             1..1462
                     /gene="LRP6"
                     /gene_synonym="ADCAD2; EVR8; OPTA4; STHAG7"
                     /coded_by="NM_001414254.1:759..5147"
                     /note="isoform i is encoded by transcript variant 12"
                     /db_xref="GeneID:4040"
                     /db_xref="HGNC:HGNC:6698"
                     /db_xref="MIM:603507"
ORIGIN      
        1 mywtdwgevp kieragmdgs srfiiinsei ywpngltldy eeqklywada klnfihksnl
       61 dgtnrqavvk gslphpfalt lfedilywtd wsthsilacn kytgeglrei hsdifspmdi
      121 hafsqqrqpn atnpcgidng gcshlclmsp vkpfyqcacp tgvkllengk tckdgatell
      181 llarrtdlrr isldtpdftd ivlqledirh aiaidydpve gyiywtddev rairrsfidg
      241 sgsqfvvtaq iahpdgiavd wvarnlywtd tgtdrievtr lngtmrkili sedleeprai
      301 vldpmvgymy wtdwgeipki eraaldgsdr vvlvntslgw pnglaldyde gkiywgdakt
      361 dkievmntdg tgrrvlvedk iphifgftll gdyvywtdwq rrsiervhkr saereviidq
      421 lpdlmglkat nvhrvigsnp caeenggcsh lclyrpqglr cacpigfeli sdmktcivpe
      481 afllfsrrad irrisletnn nnvaipltgv keasaldfdv tdnriywtdi slktisrafm
      541 ngsalehvve fgldypegma vdwlgknlyw adtgtnriev skldgqhrqv lvwkdldspr
      601 alaldpaegf mywtewggkp kidraamdgs erttlvpnvg rangltidya krrlywtdld
      661 tnliessnml glnreviadd lphpfgltqy qdyiywtdws rrsierankt sgqnrtiiqg
      721 hldyvmdilv fhssrqsgwn ecassnghcs hlclavpvgg fvcgcpahys lnadnrtcsa
      781 pttfllfsqk sainrmvide qqspdiilpi hslrnvraid ydpldkqlyw idsrqnmirk
      841 aqedgsqgft vvvssvpsqn leiqpydlsi diysryiywt ceatnvinvt rldgrsvgvv
      901 lkgeqdrpra vvvnpekgym yftnlqersp kieraaldgt erevlffsgl skpialalds
      961 rlgklfwads dlrriessdl sganrivled snilqpvglt vfenwlywid kqqqmiekid
     1021 mtgregrtkv qariaqlsdi havkelnlqe yrqhpcaqdn ggcshiclvk gdgttrcscp
     1081 mhlvllqdel scgepptcsp qqftcftgei dcipvawrcd gftecedhsd elncpvcses
     1141 qfqcasgqci dgalrcngda ncqdksdekn cevlclidqf rcangqcigk hkkcdhnvdc
     1201 sdksdeldcy pteepapqat ntvgsvigvi vtifvsgtvy ficqrmlcpr mkgdgetmtn
     1261 dyvvhgpasv plgyvphpss lsgslpgmsr gksmisslsi mggssgppyd rahvtgasss
     1321 sssstkgtyf pailnpppsp atershytme fgyssnspst hrsysyrpys yrhfappttp
     1381 cstdvcdsdy apsrrmtsva takgytsdln ydsepvpppp tprsqylsae enyescppsp
     1441 ytersyshhl yppppspctd ss
//
LOCUS       NP_996773                841 aa            linear   PRI 21-DEC-2025
DEFINITION  disco-interacting protein 2 homolog A isoform c [Homo sapiens].
ACCESSION   NP_996773
VERSION     NP_996773.1
DBSOURCE    REFSEQ: accession NM_206890.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Zhang,B., Zhang,X., Omorou,M., Zhao,K., Ruan,Y. and Luan,H.
  TITLE     Disco interacting protein 2 homolog A (DIP2A): A key component in
            the regulation of brain disorders
  JOURNAL   Biomed Pharmacother 168, 115771 (2023)
   PUBMED   37897975
  REMARK    GeneRIF: Disco interacting protein 2 homolog A (DIP2A): A key
            component in the regulation of brain disorders.
            Review article
REFERENCE   2  (residues 1 to 841)
  AUTHORS   Mondal,S., Kinatukara,P., Singh,S., Shambhavi,S., Patil,G.S.,
            Dubey,N., Singh,S.H., Pal,B., Shekar,P.C., Kamat,S.S. and
            Sankaranarayanan,R.
  TITLE     DIP2 is a unique regulator of diacylglycerol lipid homeostasis in
            eukaryotes
  JOURNAL   Elife 11, e77665 (2022)
   PUBMED   35766356
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 841)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 841)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 841)
  AUTHORS   Ma,J., Zhang,L.Q., He,Z.X., He,X.X., Wang,Y.J., Jian,Y.L., Wang,X.,
            Zhang,B.B., Su,C., Lu,J., Huang,B.Q., Zhang,Y., Wang,G.Y.,
            Guo,W.X., Qiu,D.L., Mei,L., Xiong,W.C., Zheng,Y.W. and Zhu,X.J.
  TITLE     Autism candidate gene DIP2A regulates spine morphogenesis via
            acetylation of cortactin
  JOURNAL   PLoS Biol 17 (10), e3000461 (2019)
   PUBMED   31600191
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 841)
  AUTHORS   Winnepenninckx,B., Debacker,K., Ramsay,J., Smeets,D., Smits,A.,
            FitzPatrick,D.R. and Kooy,R.F.
  TITLE     CGG-repeat expansion in the DIP2B gene is associated with the
            fragile site FRA12A on chromosome 12q13.1
  JOURNAL   Am J Hum Genet 80 (2), 221-231 (2007)
   PUBMED   17236128
REFERENCE   7  (residues 1 to 841)
  AUTHORS   Casadei,R., Strippoli,P., D'Addabbo,P., Canaider,S., Lenzi,L.,
            Vitale,L., Giannone,S., Frabetti,F., Facchin,F., Carinci,P. and
            Zannotti,M.
  TITLE     mRNA 5' region sequence incompleteness: a potential source of
            systematic errors in translation initiation codon assignment in
            human mRNAs
  JOURNAL   Gene 321, 185-193 (2003)
   PUBMED   14637006
REFERENCE   8  (residues 1 to 841)
  AUTHORS   Mukhopadhyay,M., Pelka,P., DeSousa,D., Kablar,B., Schindler,A.,
            Rudnicki,M.A. and Campos,A.R.
  TITLE     Cloning, genomic organization and expression pattern of a novel
            Drosophila gene, the disco-interacting protein 2 (dip2), and its
            murine homolog
  JOURNAL   Gene 293 (1-2), 59-65 (2002)
   PUBMED   12137943
REFERENCE   9  (residues 1 to 841)
  AUTHORS   Gardiner,K., Slavov,D., Bechtel,L. and Davisson,M.
  TITLE     Annotation of human chromosome 21 for relevance to Down syndrome:
            gene structure and expression analysis
  JOURNAL   Genomics 79 (6), 833-843 (2002)
   PUBMED   12036298
REFERENCE   10 (residues 1 to 841)
  AUTHORS   Wang,Z., Tseng,C.P., Pong,R.C., Chen,H., McConnell,J.D., Navone,N.
            and Hsieh,J.T.
  TITLE     The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate
            cancer. Characterization of a novel GTPase-activating protein
            associated with N-terminal domain of DOC-2/DAB2
  JOURNAL   J Biol Chem 277 (15), 12622-12631 (2002)
   PUBMED   11812785
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000337.1, DA326960.1,
            AB273729.1, BC033718.1 and BQ017399.1.
            
            Summary: The protein encoded by this gene may be involved in axon
            patterning in the central nervous system. This gene is not highly
            expressed. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (3) differs in the 3' UTR and
            coding region compared to variant 1. The resulting isoform (c) has
            a shorter C-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.230700.1,
                                           SRR1803614.172816.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..841
                     /product="disco-interacting protein 2 homolog A isoform c"
                     /EC_number="6.2.1.1"
                     /note="disco-interacting protein 2A; DIP2 homolog A; DIP2
                     disco-interacting protein 2 homolog A; disconnected
                     interacting protein 2 homolog A; disco interacting protein
                     2 homolog A"
                     /calculated_mol_wt=90465
     Region          10..123
                     /region_name="DMAP_binding"
                     /note="DMAP1-binding Domain; pfam06464"
                     /db_xref="CDD:368923"
     Region          60..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT5; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Region          283..286
                     /region_name="PXXP motif, required for interaction with
                     CTTN. /evidence=ECO:0000250|UniProtKB:Q8BWT5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          302..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          307..310
                     /region_name="PXXP motif, required for interaction with
                     CTTN. /evidence=ECO:0000250|UniProtKB:Q8BWT5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          351..841
                     /region_name="Adenylate forming domain, Class I
                     superfamily"
                     /note="This family includes acyl- and aryl-CoA ligases, as
                     well as the adenylation domain of nonribosomal peptide
                     synthetases and firefly luciferases. The adenylate-forming
                     enzymes catalyze an ATP-dependent two-step reaction to
                     first activate a carboxylate...; cl17068"
                     /db_xref="CDD:473059"
     Site            order(512,515..520,522..523)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341228"
     Site            order(515,556..557,607,609..610,613,635..636,654..659,792,
                     804,807,815..818)
                     /site_type="active"
                     /db_xref="CDD:341228"
     Site            order(515,635..636,654..659,792,804,807,818)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Site            order(556,609..610,613,635,815..817)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341228"
     CDS             1..841
                     /gene="DIP2A"
                     /gene_synonym="C21orf106; DIP2"
                     /coded_by="NM_206890.3:242..2767"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS46657.1"
                     /db_xref="GeneID:23181"
                     /db_xref="HGNC:HGNC:17217"
                     /db_xref="MIM:607711"
ORIGIN      
        1 madrgcplea aplpaevres laelelelse gditqkgyek krakllaryi pliqgidpsl
       61 qaenripgps qttaaapkqq ksrptasrde rfrsdvhtea vqaalakyke rkmpmpskrr
      121 svlvhssvet ytppdtssas edegslrrpg rltstplqsh ssvepwldrv iqgsstsssa
      181 sstsshpggr pttapsaaat pgaaattala gleahthidl hsappdvttg lvehsyferp
      241 qvasvrsvpr gcsgsmleta dgvpvnsrvs skiqqllntl krpkrpplke ffvddfeell
      301 evqqpdpnqp kpegsetsvl rgepltagvp rppsllatlq rwgttqpksp cltaldttgk
      361 avytltygkl wsrslklayt llnkltskne pllkpgdrva lvfpnsdpvm fmvafygcll
      421 aelvpvpiev pltrkdagsq qvgfllgscg vflalttdac qkglpkaqtg evaafkgwpp
      481 lswlvidgkh lakppkdwhp laqdtgtgta yieyktskeg stvgvtvsha sllaqcralt
      541 qacgyseaet ltnvldfkrd aglwhgvlts vmnrmhvvsv pyalmkanpl swiqkvcfyk
      601 araalvksrd mhwsllaqrg qrdvslsslr mlivadganp wsisscdafl nvfqsrglrp
      661 evicpcassp ealtvairrp pdlggppprk avlsmnglsy gvirvdteek lsvltvqdvg
      721 qvmpganvcv vklegtpylc ktdevgeicv sssatgtayy gllgitknvf eavpvttgga
      781 pifdrpftrt gllgfigpdn lvfivgkldg lmvtgvrrhn addvvatala vepmkfvyrg
      841 r
//
LOCUS       NP_001340872            1571 aa            linear   PRI 21-DEC-2025
DEFINITION  disco-interacting protein 2 homolog A isoform a [Homo sapiens].
ACCESSION   NP_001340872 XP_016883785
VERSION     NP_001340872.1
DBSOURCE    REFSEQ: accession NM_001353943.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1571)
  AUTHORS   Zhang,B., Zhang,X., Omorou,M., Zhao,K., Ruan,Y. and Luan,H.
  TITLE     Disco interacting protein 2 homolog A (DIP2A): A key component in
            the regulation of brain disorders
  JOURNAL   Biomed Pharmacother 168, 115771 (2023)
   PUBMED   37897975
  REMARK    GeneRIF: Disco interacting protein 2 homolog A (DIP2A): A key
            component in the regulation of brain disorders.
            Review article
REFERENCE   2  (residues 1 to 1571)
  AUTHORS   Mondal,S., Kinatukara,P., Singh,S., Shambhavi,S., Patil,G.S.,
            Dubey,N., Singh,S.H., Pal,B., Shekar,P.C., Kamat,S.S. and
            Sankaranarayanan,R.
  TITLE     DIP2 is a unique regulator of diacylglycerol lipid homeostasis in
            eukaryotes
  JOURNAL   Elife 11, e77665 (2022)
   PUBMED   35766356
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1571)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 1571)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1571)
  AUTHORS   Ma,J., Zhang,L.Q., He,Z.X., He,X.X., Wang,Y.J., Jian,Y.L., Wang,X.,
            Zhang,B.B., Su,C., Lu,J., Huang,B.Q., Zhang,Y., Wang,G.Y.,
            Guo,W.X., Qiu,D.L., Mei,L., Xiong,W.C., Zheng,Y.W. and Zhu,X.J.
  TITLE     Autism candidate gene DIP2A regulates spine morphogenesis via
            acetylation of cortactin
  JOURNAL   PLoS Biol 17 (10), e3000461 (2019)
   PUBMED   31600191
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1571)
  AUTHORS   Winnepenninckx,B., Debacker,K., Ramsay,J., Smeets,D., Smits,A.,
            FitzPatrick,D.R. and Kooy,R.F.
  TITLE     CGG-repeat expansion in the DIP2B gene is associated with the
            fragile site FRA12A on chromosome 12q13.1
  JOURNAL   Am J Hum Genet 80 (2), 221-231 (2007)
   PUBMED   17236128
REFERENCE   7  (residues 1 to 1571)
  AUTHORS   Casadei,R., Strippoli,P., D'Addabbo,P., Canaider,S., Lenzi,L.,
            Vitale,L., Giannone,S., Frabetti,F., Facchin,F., Carinci,P. and
            Zannotti,M.
  TITLE     mRNA 5' region sequence incompleteness: a potential source of
            systematic errors in translation initiation codon assignment in
            human mRNAs
  JOURNAL   Gene 321, 185-193 (2003)
   PUBMED   14637006
REFERENCE   8  (residues 1 to 1571)
  AUTHORS   Mukhopadhyay,M., Pelka,P., DeSousa,D., Kablar,B., Schindler,A.,
            Rudnicki,M.A. and Campos,A.R.
  TITLE     Cloning, genomic organization and expression pattern of a novel
            Drosophila gene, the disco-interacting protein 2 (dip2), and its
            murine homolog
  JOURNAL   Gene 293 (1-2), 59-65 (2002)
   PUBMED   12137943
REFERENCE   9  (residues 1 to 1571)
  AUTHORS   Gardiner,K., Slavov,D., Bechtel,L. and Davisson,M.
  TITLE     Annotation of human chromosome 21 for relevance to Down syndrome:
            gene structure and expression analysis
  JOURNAL   Genomics 79 (6), 833-843 (2002)
   PUBMED   12036298
REFERENCE   10 (residues 1 to 1571)
  AUTHORS   Wang,Z., Tseng,C.P., Pong,R.C., Chen,H., McConnell,J.D., Navone,N.
            and Hsieh,J.T.
  TITLE     The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate
            cancer. Characterization of a novel GTPase-activating protein
            associated with N-terminal domain of DOC-2/DAB2
  JOURNAL   J Biol Chem 277 (15), 12622-12631 (2002)
   PUBMED   11812785
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000337.1 and AP000338.3.
            
            On Aug 1, 2017 this sequence version replaced XP_016883785.1.
            
            Summary: The protein encoded by this gene may be involved in axon
            patterning in the central nervous system. This gene is not highly
            expressed. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (9), as well as variant 1, encodes
            isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.68501.1,
                                           SRR11853563.21257.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1571
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..1571
                     /product="disco-interacting protein 2 homolog A isoform a"
                     /EC_number="6.2.1.1"
                     /note="disco-interacting protein 2A; DIP2 homolog A; DIP2
                     disco-interacting protein 2 homolog A; disconnected
                     interacting protein 2 homolog A; disco interacting protein
                     2 homolog A"
                     /calculated_mol_wt=170239
     Region          10..123
                     /region_name="DMAP_binding"
                     /note="DMAP1-binding Domain; pfam06464"
                     /db_xref="CDD:368923"
     Region          60..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT5; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Region          283..286
                     /region_name="PXXP motif, required for interaction with
                     CTTN. /evidence=ECO:0000250|UniProtKB:Q8BWT5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          302..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          307..310
                     /region_name="PXXP motif, required for interaction with
                     CTTN. /evidence=ECO:0000250|UniProtKB:Q8BWT5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          351..927
                     /region_name="Dip2"
                     /note="Disco-interacting protein 2 (Dip2); cd05905"
                     /db_xref="CDD:341231"
     Site            order(512,515..520,522..523)
                     /site_type="other"
                     /note="putative acyl-activating enzyme (AAE) consensus
                     motif"
                     /db_xref="CDD:341231"
     Site            order(515,635..636,694..699,792,804,807,818,907)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Site            order(515,556..557,607,609..610,613,635..636,654..659,792,
                     804,807,815..818,888)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341231"
     Site            order(556,609..610,613,635,815..817,875,888)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Region          1003..1567
                     /region_name="Dip2"
                     /note="Disco-interacting protein 2 (Dip2); cd05905"
                     /db_xref="CDD:341231"
     Site            order(1152,1155..1160,1162..1163)
                     /site_type="other"
                     /note="putative acyl-activating enzyme (AAE) consensus
                     motif"
                     /db_xref="CDD:341231"
     Site            order(1155,1281..1282,1336..1341,1432,1454,1457,1468,1547)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Site            order(1155,1196..1197,1247,1249..1250,1253,1281..1282,
                     1299..1304,1432,1454,1457,1465..1468,1528)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341231"
     Site            order(1196,1249..1250,1253,1281,1465..1467,1515,1528)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341231"
     CDS             1..1571
                     /gene="DIP2A"
                     /gene_synonym="C21orf106; DIP2"
                     /coded_by="NM_001353943.2:242..4957"
                     /note="isoform a is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS46655.1"
                     /db_xref="GeneID:23181"
                     /db_xref="HGNC:HGNC:17217"
                     /db_xref="MIM:607711"
ORIGIN      
        1 madrgcplea aplpaevres laelelelse gditqkgyek krakllaryi pliqgidpsl
       61 qaenripgps qttaaapkqq ksrptasrde rfrsdvhtea vqaalakyke rkmpmpskrr
      121 svlvhssvet ytppdtssas edegslrrpg rltstplqsh ssvepwldrv iqgsstsssa
      181 sstsshpggr pttapsaaat pgaaattala gleahthidl hsappdvttg lvehsyferp
      241 qvasvrsvpr gcsgsmleta dgvpvnsrvs skiqqllntl krpkrpplke ffvddfeell
      301 evqqpdpnqp kpegsetsvl rgepltagvp rppsllatlq rwgttqpksp cltaldttgk
      361 avytltygkl wsrslklayt llnkltskne pllkpgdrva lvfpnsdpvm fmvafygcll
      421 aelvpvpiev pltrkdagsq qvgfllgscg vflalttdac qkglpkaqtg evaafkgwpp
      481 lswlvidgkh lakppkdwhp laqdtgtgta yieyktskeg stvgvtvsha sllaqcralt
      541 qacgyseaet ltnvldfkrd aglwhgvlts vmnrmhvvsv pyalmkanpl swiqkvcfyk
      601 araalvksrd mhwsllaqrg qrdvslsslr mlivadganp wsisscdafl nvfqsrglrp
      661 evicpcassp ealtvairrp pdlggppprk avlsmnglsy gvirvdteek lsvltvqdvg
      721 qvmpganvcv vklegtpylc ktdevgeicv sssatgtayy gllgitknvf eavpvttgga
      781 pifdrpftrt gllgfigpdn lvfivgkldg lmvtgvrrhn addvvatala vepmkfvyrg
      841 riavfsvtvl hddrivlvae qrpdaseeds fqwmsrvlqa idsihqvgvy clalvpantl
      901 pkaplggihi setkqrfleg tlhpcnvlmc phtcvtnlpk prqkqpevgp asmivgnlva
      961 gkriaqasgr elahledsdq arkflfladv lqwrahttpd hplflllnak gtvtstatcv
     1021 qlhkraerva aalmekgrls vgdhvalvyp pgvdliaafy gclycgcvpv tvrpphpqnl
     1081 gttlptvkmi vevsksacvl ttqavtrllr skeaaaavdi rtwptildtd dipkkkiasv
     1141 frppspdvla yldfsvsttg ilagvkmsha atsalcrsik lqcelypsrq iaicldpycg
     1201 lgfalwclcs vysghqsvlv pplelesnvs lwlsavsqyk arvtfcsysv memctkglga
     1261 qtgvlrmkgv nlscvrtcmv vaeerprial tqsfsklfkd lglparavst tfgcrvnvai
     1321 clqgtagpdp ttvyvdmral rhdrvrlver gsphslplme sgkilpgvkv iiahtetkgp
     1381 lgdshlgeiw vssphnatgy ytvygeealh adhfsarlsf gdtqtiwart gylgflrrte
     1441 ltdasggrhd alyvvgslde tlelrgmryh pidietsvir ahrsiaecav ftwtnllvvv
     1501 veldgleqda ldlvalvtnv vleehylvvg vvvivdpgvi pinsrgekqr mhlrdgflad
     1561 qldpiyvayn m
//
LOCUS       NP_001401176            1547 aa            linear   PRI 21-DEC-2025
DEFINITION  low-density lipoprotein receptor-related protein 6 isoform d [Homo
            sapiens].
ACCESSION   NP_001401176
VERSION     NP_001401176.1
DBSOURCE    REFSEQ: accession NM_001414247.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1547)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1547)
  AUTHORS   Zhong,S., Guo,Q., Chen,X., Luo,X., Long,Y., Chong,T., Ye,M., He,H.,
            Lu,A., Ao,K., Yin,M., Xu,A., Li,X., Hao,Y. and Guo,X.
  TITLE     The inhibition of YTHDF3/m6A/LRP6 reprograms fatty acid metabolism
            and suppresses lymph node metastasis in cervical cancer
  JOURNAL   Int J Biol Sci 20 (3), 916-936 (2024)
   PUBMED   38250152
  REMARK    GeneRIF: The inhibition of YTHDF3/m[6]A/LRP6 reprograms fatty acid
            metabolism and suppresses lymph node metastasis in cervical cancer.
            Erratum:[Int J Biol Sci. 2025 Jun 5;21(8):3825-3826. doi:
            10.7150/ijbs.115928. PMID: 40520018]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1547)
  AUTHORS   Li,J., Liu,Z., Ren,Y., Shao,H. and Li,S.
  TITLE     LRP5-/6 gene polymorphisms and its association with risk of
            abnormal bone mass in postmenopausal women
  JOURNAL   J Orthop Surg Res 18 (1), 369 (2023)
   PUBMED   37202775
  REMARK    GeneRIF: LRP5-/6 gene polymorphisms and its association with risk
            of abnormal bone mass in postmenopausal women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1547)
  AUTHORS   Hao,H., Liu,Q., Chen,J. and Zhou,H.
  TITLE     Overexpression of circRNAs LRP6 in gestational diabetes mellitus
            predicts foetal malformation and intrauterine death
  JOURNAL   Endocrinol Diabetes Nutr (Engl Ed) 70 (2), 124-129 (2023)
   PUBMED   36925229
  REMARK    GeneRIF: Overexpression of circRNAs LRP6 in gestational diabetes
            mellitus predicts foetal malformation and intrauterine death.
REFERENCE   5  (residues 1 to 1547)
  AUTHORS   Wang,J., Yang,H., Ma,X., Liu,J., Li,L., Chen,L. and Wei,F.
  TITLE     LRP6/filamentous-actin signaling facilitates osteogenic commitment
            in mechanically induced periodontal ligament stem cells
  JOURNAL   Cell Mol Biol Lett 28 (1), 7 (2023)
   PUBMED   36694134
  REMARK    GeneRIF: LRP6/filamentous-actin signaling facilitates osteogenic
            commitment in mechanically induced periodontal ligament stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1547)
  AUTHORS   Bafico,A., Liu,G., Yaniv,A., Gazit,A. and Aaronson,S.A.
  TITLE     Novel mechanism of Wnt signalling inhibition mediated by Dickkopf-1
            interaction with LRP6/Arrow
  JOURNAL   Nat Cell Biol 3 (7), 683-686 (2001)
   PUBMED   11433302
REFERENCE   7  (residues 1 to 1547)
  AUTHORS   Mao,B., Wu,W., Li,Y., Hoppe,D., Stannek,P., Glinka,A. and Niehrs,C.
  TITLE     LDL-receptor-related protein 6 is a receptor for Dickkopf proteins
  JOURNAL   Nature 411 (6835), 321-325 (2001)
   PUBMED   11357136
REFERENCE   8  (residues 1 to 1547)
  AUTHORS   Tamai,K., Semenov,M., Kato,Y., Spokony,R., Liu,C., Katsuyama,Y.,
            Hess,F., Saint-Jeannet,J.P. and He,X.
  TITLE     LDL-receptor-related proteins in Wnt signal transduction
  JOURNAL   Nature 407 (6803), 530-535 (2000)
   PUBMED   11029007
REFERENCE   9  (residues 1 to 1547)
  AUTHORS   Baens,M., Wlodarska,I., Corveleyn,A., Hoornaert,I., Hagemeijer,A.
            and Marynen,P.
  TITLE     A physical, transcript, and deletion map of chromosome region
            12p12.3 flanked by ETV6 and CDKN1B: hypermethylation of the LRP6
            CpG island in two leukemia patients with hemizygous del(12p)
  JOURNAL   Genomics 56 (1), 40-50 (1999)
   PUBMED   10036184
REFERENCE   10 (residues 1 to 1547)
  AUTHORS   Brown,S.D., Twells,R.C., Hey,P.J., Cox,R.D., Levy,E.R.,
            Soderman,A.R., Metzker,M.L., Caskey,C.T., Todd,J.A. and Hess,J.F.
  TITLE     Isolation and characterization of LRP6, a novel member of the low
            density lipoprotein receptor gene family
  JOURNAL   Biochem Biophys Res Commun 248 (3), 879-888 (1998)
   PUBMED   9704021
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007621.34, AC007537.3 and
            KF455603.1.
            
            Summary: This gene encodes a member of the low density lipoprotein
            (LDL) receptor gene family. LDL receptors are transmembrane cell
            surface proteins involved in receptor-mediated endocytosis of
            lipoprotein and protein ligands. The protein encoded by this gene
            functions as a receptor or, with Frizzled, a co-receptor for Wnt
            and thereby transmits the canonical Wnt/beta-catenin signaling
            cascade. Through its interaction with the Wnt/beta-catenin
            signaling cascade this gene plays a role in the regulation of cell
            differentiation, proliferation, and migration and the development
            of many cancer types. This protein undergoes gamma-secretase
            dependent RIP- (regulated intramembrane proteolysis) processing but
            the precise locations of the cleavage sites have not been
            determined.[provided by RefSeq, Dec 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.6834.1,
                                           SRR18074969.1721158.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1547
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..1547
                     /product="low-density lipoprotein receptor-related protein
                     6 isoform d"
                     /note="low-density lipoprotein receptor-related protein 6;
                     LRP-6"
                     /calculated_mol_wt=172471
     Region          <24..154
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          89..127
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          151..185
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          220..257
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          287..327
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          331..371
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          392..433
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          417..458
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          459..492
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          526..561
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          <588..747
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          631..673
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          761..800
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          827..863
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          892..932
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          <902..1009
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          1028..1070
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1141..1177
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1183..1219
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1188,1198,1209..1210)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1202,1205,1209,1215..1216)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1212..1216
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1222..1256
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1227,1235,1246..1247)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1239,1242,1246,1252..1253)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1249..1253
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1260..1294
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1265,1273,1284..1285)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1277,1280,1284,1290..1291)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1287..1291
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     CDS             1..1547
                     /gene="LRP6"
                     /gene_synonym="ADCAD2; EVR8; OPTA4; STHAG7"
                     /coded_by="NM_001414247.1:310..4953"
                     /note="isoform d is encoded by transcript variant 5"
                     /db_xref="GeneID:4040"
                     /db_xref="HGNC:HGNC:6698"
                     /db_xref="MIM:603507"
ORIGIN      
        1 mgavlrslla csfcvllraa plllyanrrd lrlvdatngk enativvggl edaaavdfvf
       61 shgliywsdv seeaikrtef nktesvqnvv vsgllspdgl acdwlgekly wtdsetnrie
      121 vsnldgslrk vlfwqeldqp raialdpssg qavvkgslph pfaltlfedi lywtdwsths
      181 ilacnkytge glreihsdif spmdihafsq qrqpnatnpc gidnggcshl clmspvkpfy
      241 qcacptgvkl lengktckdg atellllarr tdlrrisldt pdftdivlql edirhaiaid
      301 ydpvegyiyw tddevrairr sfidgsgsqf vvtaqiahpd giavdwvarn lywtdtgtdr
      361 ievtrlngtm rkilisedle epraivldpm vgymywtdwg eipkieraal dgsdrvvlvn
      421 tslgwpngla ldydegkiyw gdaktdkiev mntdgtgrrv lvedkiphif gftllgdyvy
      481 wtdwqrrsie rvhkrsaere viidqlpdlm glkatnvhrv igsnpcaeen ggcshlclyr
      541 pqglrcacpi gfelisdmkt civpeafllf srradirris letnnnnvai pltgvkeasa
      601 ldfdvtdnri ywtdislkti srafmngsal ehvvefgldy pegmavdwlg knlywadtgt
      661 nrievskldg qhrqvlvwkd ldspralald paegfmywte wggkpkidra amdgserttl
      721 vpnvgrangl tidyakrrly wtdldtnlie ssnmlglnre viaddlphpf gltqyqdyiy
      781 wtdwsrrsie ranktsgqnr tiiqghldyv mdilvfhssr qsgwnecass nghcshlcla
      841 vpvggfvcgc pahyslnadn rtcsapttfl lfsqksainr mvideqqspd iilpihslrn
      901 vraidydpld kqlywidsrq nmirkaqedg sqgftvvvss vpsqnleiqp ydlsidiysr
      961 yiywtceatn vinvtrldgr svgvvlkgeq drpravvvnp ekgymyftnl qerspkiera
     1021 aldgterevl ffsglskpia laldsrlgkl fwadsdlrri essdlsganr ivledsnilq
     1081 pvgltvfenw lywidkqqqm iekidmtgre grtkvqaria qlsdihavke lnlqeyrqhp
     1141 caqdnggcsh iclvkgdgtt rcscpmhlvl lqdelscgep ptcspqqftc ftgeidcipv
     1201 awrcdgftec edhsdelncp vcsesqfqca sgqcidgalr cngdancqdk sdekncevlc
     1261 lidqfrcang qcigkhkkcd hnvdcsdksd eldcypteep apqatntvgs vigvivtifv
     1321 sgtvyficqr mlcprmkgdg etmtndyvvh gpasvplgyv phpsslsgsl pgmsrgksmi
     1381 sslsimggss gppydrahvt gassssssst kgtyfpailn pppspaters hytmefgyss
     1441 nspsthrsys yrpysyrhfa ppttpcstdv cdsdyapsrr mtsvatakgy tsdlnydsep
     1501 vpppptprsq ylsaeenyes cppspyters yshhlypppp spctdss
//
LOCUS       NP_055789               1556 aa            linear   PRI 21-DEC-2025
DEFINITION  disco-interacting protein 2 homolog C [Homo sapiens].
ACCESSION   NP_055789 XP_034536
VERSION     NP_055789.1
DBSOURCE    REFSEQ: accession NM_014974.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1556)
  AUTHORS   Chai,W., Wang,Y., Hao,W., Liu,X., Hou,X., Wan,Z., Chen,L., Han,Y.,
            Ma,J., Feng,X., Zhu,X. and Yu,H.
  TITLE     DIP2C Deficiency Leads to Abnormal Sphingolipid Metabolism in Mice
  JOURNAL   Ann N Y Acad Sci 1553 (1), 437-448 (2025)
   PUBMED   41054236
REFERENCE   2  (residues 1 to 1556)
  AUTHORS   Xia,Y., Zhang,M., Song,R., Wu,H., Deng,J., Huang,S. and Yang,Y.
  TITLE     The deficiency of DIP2C leads to congenital heart defects in
            patients with 10p15.3 microdeletion syndrome
  JOURNAL   Gene 969, 149753 (2025)
   PUBMED   40915331
REFERENCE   3  (residues 1 to 1556)
  AUTHORS   Ha,T., Morgan,A., Bartos,M.N., Beatty,K., Cogne,B., Braun,D.,
            Gerber,C.B., Gaspar,H., Kopps,A.M., Rieubland,C., Hurst,A.C.E.,
            Amor,D.J., Nizon,M., Pasquier,L., Pfundt,R., Reis,A., Siu,V.M.,
            Tessarech,M., Thompson,M.L., Vincent,M., de Vries,B.B.A.,
            Walsh,M.B., Wechsler,S.B., Zweier,C., Schnur,R.E., Guillen
            Sacoto,M.J., Margot,H., Masotto,B., Palafoll,M.I.V., Nawaz,U.,
            Voineagu,I. and Slavotinek,A.
  TITLE     De novo variants predicting haploinsufficiency for DIP2C are
            associated with expressive speech delay
  JOURNAL   Am J Med Genet A 194 (7), e63559 (2024)
   PUBMED   38421105
  REMARK    GeneRIF: De novo variants predicting haploinsufficiency for DIP2C
            are associated with expressive speech delay.
REFERENCE   4  (residues 1 to 1556)
  AUTHORS   Li,Y., Sun,C., Guo,Y., Qiu,S., Li,Y., Liu,Y., Zhong,W., Wang,H.,
            Cheng,Y. and Liu,Y.
  TITLE     DIP2C polymorphisms are implicated in susceptibility and clinical
            phenotypes of autism spectrum disorder
  JOURNAL   Psychiatry Res 316, 114792 (2022)
   PUBMED   35987071
  REMARK    GeneRIF: DIP2C polymorphisms are implicated in susceptibility and
            clinical phenotypes of autism spectrum disorder.
REFERENCE   5  (residues 1 to 1556)
  AUTHORS   Li,J., Ping,J.L., Ma,B., Chen,Y.R. and Li,L.Q.
  TITLE     DIP2C expression in breast cancer and its clinical significance
  JOURNAL   Pathol Res Pract 213 (11), 1394-1399 (2017)
   PUBMED   28964575
  REMARK    GeneRIF: The data revealed DIP2C expression level decreased in
            breast cancer, especially in basal-like and HER-2 subtypes, and
            could be a valuable target for diagnosis on specific subtype of
            breast cancer
REFERENCE   6  (residues 1 to 1556)
  AUTHORS   Yoshida,T., Kato,K., Yokoi,K., Oguri,M., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Association of genetic variants with hemorrhagic stroke in Japanese
            individuals
  JOURNAL   Int J Mol Med 25 (4), 649-656 (2010)
   PUBMED   20198315
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1556)
  AUTHORS   Oguri,M., Kato,K., Yokoi,K., Yoshida,T., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Assessment of a polymorphism of SDK1 with hypertension in Japanese
            Individuals
  JOURNAL   Am J Hypertens 23 (1), 70-77 (2010)
   PUBMED   19851296
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 1556)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1556)
  AUTHORS   Winnepenninckx,B., Debacker,K., Ramsay,J., Smeets,D., Smits,A.,
            FitzPatrick,D.R. and Kooy,R.F.
  TITLE     CGG-repeat expansion in the DIP2B gene is associated with the
            fragile site FRA12A on chromosome 12q13.1
  JOURNAL   Am J Hum Genet 80 (2), 221-231 (2007)
   PUBMED   17236128
REFERENCE   10 (residues 1 to 1556)
  AUTHORS   Mukhopadhyay,M., Pelka,P., DeSousa,D., Kablar,B., Schindler,A.,
            Rudnicki,M.A. and Campos,A.R.
  TITLE     Cloning, genomic organization and expression pattern of a novel
            Drosophila gene, the disco-interacting protein 2 (dip2), and its
            murine homolog
  JOURNAL   Gene 293 (1-2), 59-65 (2002)
   PUBMED   12137943
  REMARK    GeneRIF: This publication discusses the expression pattern and
            potential function of similar genes in Drosophila and mouse.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC063313.1, AL603831.23,
            BC048327.1, AK311679.1, BX537672.1, AB023151.2, BC035216.1 and
            N27959.1.
            
            On Mar 22, 2004 this sequence version replaced XP_034536.6.
            
            Summary: This gene encodes a member of the disco-interacting
            protein homolog 2 family. The protein shares strong similarity with
            a Drosophila protein which interacts with the transcription factor
            disco and is expressed in the nervous system. [provided by RefSeq,
            Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC063313.1, AB023151.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000280886.12/ ENSP00000280886.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1556
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p15.3"
     Protein         1..1556
                     /product="disco-interacting protein 2 homolog C"
                     /note="DIP2 homolog C; DIP2 disco-interacting protein 2
                     homolog C; disconnected interacting protein 2 homolog C;
                     disco interacting protein 2 homolog C"
                     /calculated_mol_wt=170637
     Region          8..118
                     /region_name="DMAP_binding"
                     /note="DMAP1-binding Domain; pfam06464"
                     /db_xref="CDD:368923"
     Region          47..157
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2E4.2)"
     Region          170..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2E4.2)"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2E4.2)"
     Region          336..912
                     /region_name="Dip2"
                     /note="Disco-interacting protein 2 (Dip2); cd05905"
                     /db_xref="CDD:341231"
     Site            order(497,500..505,507..508)
                     /site_type="other"
                     /note="putative acyl-activating enzyme (AAE) consensus
                     motif"
                     /db_xref="CDD:341231"
     Site            order(500,620..621,679..684,777,789,792,803,892)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Site            order(500,541..542,592,594..595,598,620..621,639..644,777,
                     789,792,800..803,873)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341231"
     Site            order(541,594..595,598,620,800..802,860,873)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Region          988..1552
                     /region_name="Dip2"
                     /note="Disco-interacting protein 2 (Dip2); cd05905"
                     /db_xref="CDD:341231"
     Site            order(1137,1140..1145,1147..1148)
                     /site_type="other"
                     /note="putative acyl-activating enzyme (AAE) consensus
                     motif"
                     /db_xref="CDD:341231"
     Site            order(1140,1266..1267,1321..1326,1417,1439,1442,1453,1532)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Site            order(1140,1181..1182,1232,1234..1235,1238,1266..1267,
                     1284..1289,1417,1439,1442,1450..1453,1513)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341231"
     Site            order(1181,1234..1235,1238,1266,1450..1452,1500,1513)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341231"
     CDS             1..1556
                     /gene="DIP2C"
                     /gene_synonym="KIAA0934"
                     /coded_by="NM_014974.3:91..4761"
                     /db_xref="CCDS:CCDS7054.1"
                     /db_xref="GeneID:22982"
                     /db_xref="HGNC:HGNC:29150"
                     /db_xref="MIM:611380"
ORIGIN      
        1 madrslegma lplevrarla elelelsegd itqkgyekkr skligaylpq pprvdqalpq
       61 errapvtpss asryhrrrss gsrderyrsd vhteavqaal akhkerkmav pmpskrrslv
      121 vqtsmdaytp pdtssgsede gsvqgdsqgt ptssqgsinm ehwisqaihg sttsttssss
      181 tqsggsgaah rladvmaqth ienhsappdv ttytsehsiq verpqgstgs rtapkygnae
      241 lmetgdgvpv ssrvsakiqq lvntlkrpkr pplreffvdd feellevqqp dpnqpkpega
      301 qmlamrgeql gvvtnwppsl eaalqrwgti spkapclttm dtngkplyil tygklwtrsm
      361 kvaysilhkl gtkqepmvrp gdrvalvfpn ndpaafmaaf ygcllaevvp vpievpltrk
      421 dagsqqigfl lgscgvtval tsdachkglp ksptgeipqf kgwpkllwfv teskhlskpp
      481 rdwfphikda nndtayieyk tckdgsvlgv tvtrtallth cqaltqacgy teaetivnvl
      541 dfkkdvglwh giltsvmnmm hvisipyslm kvnplswiqk vcqykakvac vksrdmhwal
      601 vahrdqrdin lsslrmliva dganpwsiss cdaflnvfqs kglrqevicp casspealtv
      661 airrptddsn qppgrgvlsm hgltygvirv dseeklsvlt vqdvglvmpg aimcsvkpdg
      721 vpqlcrtdei gelcvcavat gtsyyglsgm tkntfevfpm tssgapisey pfirtgllgf
      781 vgpgglvfvv gkmdglmvvs grrhnaddiv atalavepmk fvyrgriavf svtvlhderi
      841 vivaeqrpds teedsfqwms rvlqaidsih qvgvyclalv pantlpktpl ggihlsetkq
      901 lflegslhpc nvlmcphtcv tnlpkprqkq peigpasvmv gnlvsgkria qasgrdlgqi
      961 edndqarkfl flsevlqwra qttpdhilyt llncrgaian sltcvqlhkr aekiavmlme
     1021 rghlqdgdhv alvyppgidl iaafygclya gcvpitvrpp hpqniattlp tvkmivevsr
     1081 saclmttqli ckllrsreaa aavdvrtwpl ildtddlpkk rpaqickpcn pdtlayldfs
     1141 vsttgmlagv kmshaatsaf crsiklqcel ypsrevaicl dpycglgfvl wclcsvysgh
     1201 qsilippsel etnpalwlla vsqykvrdtf csysvmelct kglgsqtesl kargldlsrv
     1261 rtcvvvaeer prialtqsfs klfkdlglhp ravstsfgcr vnlaiclqgt sgpdpttvyv
     1321 dmralrhdrv rlvergsphs lplmesgkil pgvriiianp etkgplgdsh lgeiwvhsah
     1381 nasgyftiyg deslqsdhfn srlsfgdtqt iwartgylgf lrrteltdan gerhdalyvv
     1441 galdeamelr gmryhpidie tsvirahksv tecavftwtn llvvvveldg seqealdlvp
     1501 lvtnvvleeh ylivgvvvvv digvipinsr gekqrmhlrd gfladqldpi yvaynm
//
LOCUS       NP_001073901             505 aa            linear   PRI 21-DEC-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase FTO isoform 3 [Homo
            sapiens].
ACCESSION   NP_001073901 XP_051200
VERSION     NP_001073901.1
DBSOURCE    REFSEQ: accession NM_001080432.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Li,B., Wang,L., Du,M. and He,H.
  TITLE     FTO in oral diseases: Functions, mechanisms, and therapeutic
            potential
  JOURNAL   FASEB J 38 (20), e70115 (2024)
   PUBMED   39436191
  REMARK    GeneRIF: FTO in oral diseases: Functions, mechanisms, and
            therapeutic potential.
            Review article
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Li,Q. and Mu,S.
  TITLE     FTO mediates the diabetic kidney disease progression through
            regulating the m6A modification of NLRP3
  JOURNAL   BMC Nephrol 25 (1), 345 (2024)
   PUBMED   39390397
  REMARK    GeneRIF: FTO mediates the diabetic kidney disease progression
            through regulating the m[6]A modification of NLRP3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Shan,L., Tao,M., Zhang,W., Zhao,J.D., Liu,X.C., Fang,Z.H. and
            Gao,J.R.
  TITLE     Comprehensive analysis of the m6A demethylase FTO in endothelial
            dysfunction by MeRIP sequencing
  JOURNAL   Exp Cell Res 442 (2), 114268 (2024)
   PUBMED   39343042
  REMARK    GeneRIF: Comprehensive analysis of the m[6]A demethylase FTO in
            endothelial dysfunction by MeRIP sequencing.
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Nabeel-Shah,S., Pu,S., Burke,G.L., Ahmed,N., Braunschweig,U.,
            Farhangmehr,S., Lee,H., Wu,M., Ni,Z., Tang,H., Zhong,G., Marcon,E.,
            Zhang,Z., Blencowe,B.J. and Greenblatt,J.F.
  TITLE     Recruitment of the m6A/m6Am demethylase FTO to target RNAs by the
            telomeric zinc finger protein ZBTB48
  JOURNAL   Genome Biol 25 (1), 246 (2024)
   PUBMED   39300486
  REMARK    GeneRIF: Recruitment of the m[6]A/m6Am demethylase FTO to target
            RNAs by the telomeric zinc finger protein ZBTB48.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Hussain,M., Waheed,A., Elahi,A. and Mustafa,G.
  TITLE     Fat Mass and Obesity-Related (FTO) Gene Variant Is a Predictor of
            CVD in T2DM Patients
  JOURNAL   J Diabetes Res 2024, 5914316 (2024)
   PUBMED   39257882
  REMARK    GeneRIF: Fat Mass and Obesity-Related (FTO) Gene Variant Is a
            Predictor of CVD in T2DM Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Zeggini,E., Weedon,M.N., Lindgren,C.M., Frayling,T.M.,
            Elliott,K.S., Lango,H., Timpson,N.J., Perry,J.R., Rayner,N.W.,
            Freathy,R.M., Barrett,J.C., Shields,B., Morris,A.P., Ellard,S.,
            Groves,C.J., Harries,L.W., Marchini,J.L., Owen,K.R., Knight,B.,
            Cardon,L.R., Walker,M., Hitman,G.A., Morris,A.D., Doney,A.S.,
            McCarthy,M.I. and Hattersley,A.T.
  CONSRTM   Wellcome Trust Case Control Consortium (WTCCC)
  TITLE     Replication of genome-wide association signals in UK samples
            reveals risk loci for type 2 diabetes
  JOURNAL   Science 316 (5829), 1336-1341 (2007)
   PUBMED   17463249
  REMARK    Erratum:[Science. 2007 Aug 24;317(5841):1035-6]
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Scott,L.J., Mohlke,K.L., Bonnycastle,L.L., Willer,C.J., Li,Y.,
            Duren,W.L., Erdos,M.R., Stringham,H.M., Chines,P.S., Jackson,A.U.,
            Prokunina-Olsson,L., Ding,C.J., Swift,A.J., Narisu,N., Hu,T.,
            Pruim,R., Xiao,R., Li,X.Y., Conneely,K.N., Riebow,N.L., Sprau,A.G.,
            Tong,M., White,P.P., Hetrick,K.N., Barnhart,M.W., Bark,C.W.,
            Goldstein,J.L., Watkins,L., Xiang,F., Saramies,J., Buchanan,T.A.,
            Watanabe,R.M., Valle,T.T., Kinnunen,L., Abecasis,G.R., Pugh,E.W.,
            Doheny,K.F., Bergman,R.N., Tuomilehto,J., Collins,F.S. and
            Boehnke,M.
  TITLE     A genome-wide association study of type 2 diabetes in Finns detects
            multiple susceptibility variants
  JOURNAL   Science 316 (5829), 1341-1345 (2007)
   PUBMED   17463248
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 505)
  AUTHORS   Dina,C., Meyre,D., Gallina,S., Durand,E., Korner,A., Jacobson,P.,
            Carlsson,L.M., Kiess,W., Vatin,V., Lecoeur,C., Delplanque,J.,
            Vaillant,E., Pattou,F., Ruiz,J., Weill,J., Levy-Marchal,C.,
            Horber,F., Potoczna,N., Hercberg,S., Le Stunff,C., Bougneres,P.,
            Kovacs,P., Marre,M., Balkau,B., Cauchi,S., Chevre,J.C. and
            Froguel,P.
  TITLE     Variation in FTO contributes to childhood obesity and severe adult
            obesity
  JOURNAL   Nat Genet 39 (6), 724-726 (2007)
   PUBMED   17496892
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            GeneRIF: Association with obesity in adult and childre.
            Interestingly, this association receives clear confirmation under a
            Transmission Disequilibrium Test design which is robust to
            population stratification.
REFERENCE   9  (residues 1 to 505)
  AUTHORS   Frayling,T.M., Timpson,N.J., Weedon,M.N., Zeggini,E., Freathy,R.M.,
            Lindgren,C.M., Perry,J.R., Elliott,K.S., Lango,H., Rayner,N.W.,
            Shields,B., Harries,L.W., Barrett,J.C., Ellard,S., Groves,C.J.,
            Knight,B., Patch,A.M., Ness,A.R., Ebrahim,S., Lawlor,D.A.,
            Ring,S.M., Ben-Shlomo,Y., Jarvelin,M.R., Sovio,U., Bennett,A.J.,
            Melzer,D., Ferrucci,L., Loos,R.J., Barroso,I., Wareham,N.J.,
            Karpe,F., Owen,K.R., Cardon,L.R., Walker,M., Hitman,G.A.,
            Palmer,C.N., Doney,A.S., Morris,A.D., Smith,G.D., Hattersley,A.T.
            and McCarthy,M.I.
  TITLE     A common variant in the FTO gene is associated with body mass index
            and predisposes to childhood and adult obesity
  JOURNAL   Science 316 (5826), 889-894 (2007)
   PUBMED   17434869
  REMARK    GeneRIF: A genome-wide search for type 2 diabetes-susceptibility
            genes identified a common variant in the FTO gene that predisposes
            to diabetes through an effect on body mass index
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-environment interaction. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 505)
  AUTHORS   Peters,T., Ausmeier,K. and Ruther,U.
  TITLE     Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft)
            mouse mutation
  JOURNAL   Mamm Genome 10 (10), 983-986 (1999)
   PUBMED   10501967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA324897.1, AK096554.1,
            AB051539.1, BC001284.1, BC030798.1, U79260.1 and AC007347.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 18, 2007 this sequence version replaced XP_051200.6.
            
            Summary: This gene is a nuclear protein of the AlkB related
            non-haem iron and 2-oxoglutarate-dependent oxygenase superfamily
            but the exact physiological function of this gene is not known.
            Other non-heme iron enzymes function to reverse alkylated DNA and
            RNA damage by oxidative demethylation. Studies in mice and humans
            indicate a role in nervous and cardiovascular systems and a strong
            association with body mass index, obesity risk, and type 2
            diabetes. [provided by RefSeq, Jul 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.127247.1,
                                           SRR1803614.160619.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000471389.6/ ENSP00000418823.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..505
                     /product="alpha-ketoglutarate-dependent dioxygenase FTO
                     isoform 3"
                     /EC_number="1.14.11.53"
                     /note="alpha-ketoglutarate-dependent dioxygenase FTO; fat
                     mass and obesity-associated protein; AlkB homolog 9; fat
                     mass and obesity associated; m6A(m)-demethylase FTO; tRNA
                     N1-methyl adenine demethylase FTO; mRNA
                     N(6)-methyladenosine demethylase FTO; mRNA
                     (2'-O-methyladenosine-N(6)-)-demethylase FTO; U6 small
                     nuclear RNA N(6)-methyladenosine-demethylase FTO; U6 small
                     nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO;
                     intragenic FTO exon 9 containing transcript; mRNA
                     N(6)-methyladenine demethylase"
                     /calculated_mol_wt=58151
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          32..327
                     /region_name="Fe2OG dioxygenase domain.
                     /evidence=ECO:0000269|PubMed:20376003"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          36..325
                     /region_name="FTO_NTD"
                     /note="FTO catalytic domain; pfam12933"
                     /db_xref="CDD:463755"
     Region          213..224
                     /region_name="Loop L1, predicted to block binding of
                     double-stranded DNA or RNA.
                     /evidence=ECO:0000269|PubMed:20376003"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Site            216
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          329..498
                     /region_name="FTO_CTD"
                     /note="FTO C-terminal domain; pfam12934"
                     /db_xref="CDD:432887"
     CDS             1..505
                     /gene="FTO"
                     /gene_synonym="ALKBH9; BMIQ14; GDFD; IFEX9"
                     /coded_by="NM_001080432.3:30..1547"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS32448.1"
                     /db_xref="GeneID:79068"
                     /db_xref="HGNC:HGNC:24678"
                     /db_xref="MIM:610966"
ORIGIN      
        1 mkrtptaeer ereakklrll eeledtwlpy ltpkddefyq qwqlkypkli lreassvsee
       61 lhkevqeafl tlhkhgclfr dlvriqgkdl ltpvsrilig npgctykyln trlftvpwpv
      121 kgsnikhtea eiaaacetfl klndylqiet iqaleelaak ekanedavpl cmsadfprvg
      181 mgssyngqde vdiksraayn vtllnfmdpq kmpylkeepy fgmgkmavsw hhdenlvdrs
      241 avavysysce gpeeesedds hlegrdpdiw hvgfkiswdi etpglaiplh qgdcyfmldd
      301 lnathqhcvl agsqprfsst hrvaecstgt ldyilqrcql alqnvcddvd nddvslksfe
      361 pavlkqgeei hnevefewlr qfwfqgnryr kctdwwcqpm aqlealwkkm egvtnavlhe
      421 vkreglpveq rneiltaila sltarqnlrr ewharcqsri artlpadqkp ecrpywekdd
      481 asmplpfdlt divselrgql leakp
//
LOCUS       NP_001401173            1644 aa            linear   PRI 21-DEC-2025
DEFINITION  low-density lipoprotein receptor-related protein 6 isoform a
            precursor [Homo sapiens].
ACCESSION   NP_001401173
VERSION     NP_001401173.1
DBSOURCE    REFSEQ: accession NM_001414244.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1644)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1644)
  AUTHORS   Zhong,S., Guo,Q., Chen,X., Luo,X., Long,Y., Chong,T., Ye,M., He,H.,
            Lu,A., Ao,K., Yin,M., Xu,A., Li,X., Hao,Y. and Guo,X.
  TITLE     The inhibition of YTHDF3/m6A/LRP6 reprograms fatty acid metabolism
            and suppresses lymph node metastasis in cervical cancer
  JOURNAL   Int J Biol Sci 20 (3), 916-936 (2024)
   PUBMED   38250152
  REMARK    GeneRIF: The inhibition of YTHDF3/m[6]A/LRP6 reprograms fatty acid
            metabolism and suppresses lymph node metastasis in cervical cancer.
            Erratum:[Int J Biol Sci. 2025 Jun 5;21(8):3825-3826. doi:
            10.7150/ijbs.115928. PMID: 40520018]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1644)
  AUTHORS   Li,J., Liu,Z., Ren,Y., Shao,H. and Li,S.
  TITLE     LRP5-/6 gene polymorphisms and its association with risk of
            abnormal bone mass in postmenopausal women
  JOURNAL   J Orthop Surg Res 18 (1), 369 (2023)
   PUBMED   37202775
  REMARK    GeneRIF: LRP5-/6 gene polymorphisms and its association with risk
            of abnormal bone mass in postmenopausal women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1644)
  AUTHORS   Hao,H., Liu,Q., Chen,J. and Zhou,H.
  TITLE     Overexpression of circRNAs LRP6 in gestational diabetes mellitus
            predicts foetal malformation and intrauterine death
  JOURNAL   Endocrinol Diabetes Nutr (Engl Ed) 70 (2), 124-129 (2023)
   PUBMED   36925229
  REMARK    GeneRIF: Overexpression of circRNAs LRP6 in gestational diabetes
            mellitus predicts foetal malformation and intrauterine death.
REFERENCE   5  (residues 1 to 1644)
  AUTHORS   Wang,J., Yang,H., Ma,X., Liu,J., Li,L., Chen,L. and Wei,F.
  TITLE     LRP6/filamentous-actin signaling facilitates osteogenic commitment
            in mechanically induced periodontal ligament stem cells
  JOURNAL   Cell Mol Biol Lett 28 (1), 7 (2023)
   PUBMED   36694134
  REMARK    GeneRIF: LRP6/filamentous-actin signaling facilitates osteogenic
            commitment in mechanically induced periodontal ligament stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1644)
  AUTHORS   Bafico,A., Liu,G., Yaniv,A., Gazit,A. and Aaronson,S.A.
  TITLE     Novel mechanism of Wnt signalling inhibition mediated by Dickkopf-1
            interaction with LRP6/Arrow
  JOURNAL   Nat Cell Biol 3 (7), 683-686 (2001)
   PUBMED   11433302
REFERENCE   7  (residues 1 to 1644)
  AUTHORS   Mao,B., Wu,W., Li,Y., Hoppe,D., Stannek,P., Glinka,A. and Niehrs,C.
  TITLE     LDL-receptor-related protein 6 is a receptor for Dickkopf proteins
  JOURNAL   Nature 411 (6835), 321-325 (2001)
   PUBMED   11357136
REFERENCE   8  (residues 1 to 1644)
  AUTHORS   Tamai,K., Semenov,M., Kato,Y., Spokony,R., Liu,C., Katsuyama,Y.,
            Hess,F., Saint-Jeannet,J.P. and He,X.
  TITLE     LDL-receptor-related proteins in Wnt signal transduction
  JOURNAL   Nature 407 (6803), 530-535 (2000)
   PUBMED   11029007
REFERENCE   9  (residues 1 to 1644)
  AUTHORS   Baens,M., Wlodarska,I., Corveleyn,A., Hoornaert,I., Hagemeijer,A.
            and Marynen,P.
  TITLE     A physical, transcript, and deletion map of chromosome region
            12p12.3 flanked by ETV6 and CDKN1B: hypermethylation of the LRP6
            CpG island in two leukemia patients with hemizygous del(12p)
  JOURNAL   Genomics 56 (1), 40-50 (1999)
   PUBMED   10036184
REFERENCE   10 (residues 1 to 1644)
  AUTHORS   Brown,S.D., Twells,R.C., Hey,P.J., Cox,R.D., Levy,E.R.,
            Soderman,A.R., Metzker,M.L., Caskey,C.T., Todd,J.A. and Hess,J.F.
  TITLE     Isolation and characterization of LRP6, a novel member of the low
            density lipoprotein receptor gene family
  JOURNAL   Biochem Biophys Res Commun 248 (3), 879-888 (1998)
   PUBMED   9704021
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007621.34, AC007537.3 and
            KF455603.1.
            
            Summary: This gene encodes a member of the low density lipoprotein
            (LDL) receptor gene family. LDL receptors are transmembrane cell
            surface proteins involved in receptor-mediated endocytosis of
            lipoprotein and protein ligands. The protein encoded by this gene
            functions as a receptor or, with Frizzled, a co-receptor for Wnt
            and thereby transmits the canonical Wnt/beta-catenin signaling
            cascade. Through its interaction with the Wnt/beta-catenin
            signaling cascade this gene plays a role in the regulation of cell
            differentiation, proliferation, and migration and the development
            of many cancer types. This protein undergoes gamma-secretase
            dependent RIP- (regulated intramembrane proteolysis) processing but
            the precise locations of the cleavage sites have not been
            determined.[provided by RefSeq, Dec 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3211559.1,
                                           SRR14038193.1627029.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1644
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..1644
                     /product="low-density lipoprotein receptor-related protein
                     6 isoform a precursor"
                     /note="low-density lipoprotein receptor-related protein 6;
                     LRP-6"
                     /calculated_mol_wt=181695
     Region          1..204
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
                     /calculated_mol_wt=2024
     Region          20..275
                     /region_name="Beta-propeller 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            42
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            81
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          89..127
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          150..191
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          175..216
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          217..251
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          237..276
                     /region_name="LDL-receptor class B 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          286..323
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          328..589
                     /region_name="Beta-propeller 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          353..393
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          397..437
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          458..499
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          483..524
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            486
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          525..558
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          592..627
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          631..890
                     /region_name="Beta-propeller 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          <654..813
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Site            692
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          697..739
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          827..866
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            859
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            865
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          893..929
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            926
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          958..998
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          <968..1075
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Site            1039
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          1094..1132
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1238..1274
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1280..1316
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1285,1295,1306..1307)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1299,1302,1306,1312..1313)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1309..1313
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1319..1353
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1324,1332,1343..1344)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1336,1339,1343,1349..1350)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1346..1350
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1357..1391
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1362,1370,1381..1382)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1374,1377,1381,1387..1388)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1384..1388
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            1402..1424
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            1451
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:16513652; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1461
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:16513652; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1510
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17569865; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          1518..1524
                     /region_name="PPPSP motif A"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            1521
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK14, GRK5 and GRK6.
                     /evidence=ECO:0000269|PubMed:16341017,
                     ECO:0000269|PubMed:17698587, ECO:0000269|PubMed:18762581,
                     ECO:0000269|PubMed:19801552, ECO:0000269|PubMed:20059949,
                     ECO:0000269|PubMed:25331957, ECO:0000269|PubMed:27821587,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1524
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK1.
                     /evidence=ECO:0000269|PubMed:16341017; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          1558..1565
                     /region_name="PPPSP motif B"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          1587..1644
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          1599..1606
                     /region_name="PPPSP motif C"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          1619..1624
                     /region_name="PPPSP motif D"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          1634..1641
                     /region_name="PPPSP motif E"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     CDS             1..1644
                     /gene="LRP6"
                     /gene_synonym="ADCAD2; EVR8; OPTA4; STHAG7"
                     /coded_by="NM_001414244.1:310..5244"
                     /note="isoform a precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:4040"
                     /db_xref="HGNC:HGNC:6698"
                     /db_xref="MIM:603507"
ORIGIN      
        1 mgavlrslla csfcvllraa plllyanrrd lrlvdatngk enativvggl edaaavdfvf
       61 shgliywsdv seeaikrtef nktesvqnvv vsgllspdgl acdwlgekly wtdsetnrie
      121 vsnldgslrk vlfwqeldqp raialdpssg fmywtdwgev pkieragmdg ssrfiiinse
      181 iywpngltld yeeqklywad aklnfihksn ldgtnrqavv kgslphpfal tlfedilywt
      241 dwsthsilac nkytgeglre ihsdifspmd ihafsqqrqp natnpcgidn ggcshlclms
      301 pvkpfyqcac ptgvklleng ktckdgatel lllarrtdlr risldtpdft divlqledir
      361 haiaidydpv egyiywtdde vrairrsfid gsgsqfvvta qiahpdgiav dwvarnlywt
      421 dtgtdrievt rlngtmrkil isedleepra ivldpmvgym ywtdwgeipk ieraaldgsd
      481 rvvlvntslg wpnglaldyd egkiywgdak tdkievmntd gtgrrvlved kiphifgftl
      541 lgdyvywtdw qrrsiervhk rsaereviid qlpdlmglka tnvhrvigsn pcaeenggcs
      601 hlclyrpqgl rcacpigfel isdmktcivp eafllfsrra dirrisletn nnnvaipltg
      661 vkeasaldfd vtdnriywtd islktisraf mngsalehvv efgldypegm avdwlgknly
      721 wadtgtnrie vskldgqhrq vlvwkdldsp ralaldpaeg fmywtewggk pkidraamdg
      781 serttlvpnv grangltidy akrrlywtdl dtnliessnm lglnreviad dlphpfgltq
      841 yqdyiywtdw srrsierank tsgqnrtiiq ghldyvmdil vfhssrqsgw necassnghc
      901 shlclavpvg gfvcgcpahy slnadnrtcs apttfllfsq ksainrmvid eqqspdiilp
      961 ihslrnvrai dydpldkqly widsrqnmir kaqedgsqgf tvvvssvpsq nleiqpydls
     1021 idiysryiyw tceatnvinv trldgrsvgv vlkgeqdrpr avvvnpekgy myftnlqers
     1081 pkieraaldg terevlffsg lskpialald srlgklfwad sdlrriessd lsemafchva
     1141 qadvellgsr dppasasqit eitganrivl edsnilqpvg ltvfenwlyw idkqqqmiek
     1201 idmtgregrt kvqariaqls dihavkelnl qeyrqhpcaq dnggcshicl vkgdgttrcs
     1261 cpmhlvllqd elscgepptc spqqftcftg eidcipvawr cdgftecedh sdelncpvcs
     1321 esqfqcasgq cidgalrcng dancqdksde kncevlclid qfrcangqci gkhkkcdhnv
     1381 dcsdksdeld cypteepapq atntvgsvig vivtifvsgt vyficqrmlc prmkgdgetm
     1441 tndyvvhgpa svplgyvphp sslsgslpgm srgksmissl simggssgpp ydrahvtgas
     1501 sssssstkgt yfpailnppp spatershyt mefgyssnsp sthrsysyrp ysyrhfappt
     1561 tpcstdvcds dyapsrrmts vatakgytsd lnydsepvpp pptprsqyls aeenyescpp
     1621 spytersysh hlyppppspc tdss
//
LOCUS       NP_001401179            1519 aa            linear   PRI 21-DEC-2025
DEFINITION  low-density lipoprotein receptor-related protein 6 isoform g
            precursor [Homo sapiens].
ACCESSION   NP_001401179
VERSION     NP_001401179.1
DBSOURCE    REFSEQ: accession NM_001414250.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1519)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1519)
  AUTHORS   Zhong,S., Guo,Q., Chen,X., Luo,X., Long,Y., Chong,T., Ye,M., He,H.,
            Lu,A., Ao,K., Yin,M., Xu,A., Li,X., Hao,Y. and Guo,X.
  TITLE     The inhibition of YTHDF3/m6A/LRP6 reprograms fatty acid metabolism
            and suppresses lymph node metastasis in cervical cancer
  JOURNAL   Int J Biol Sci 20 (3), 916-936 (2024)
   PUBMED   38250152
  REMARK    GeneRIF: The inhibition of YTHDF3/m[6]A/LRP6 reprograms fatty acid
            metabolism and suppresses lymph node metastasis in cervical cancer.
            Erratum:[Int J Biol Sci. 2025 Jun 5;21(8):3825-3826. doi:
            10.7150/ijbs.115928. PMID: 40520018]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1519)
  AUTHORS   Li,J., Liu,Z., Ren,Y., Shao,H. and Li,S.
  TITLE     LRP5-/6 gene polymorphisms and its association with risk of
            abnormal bone mass in postmenopausal women
  JOURNAL   J Orthop Surg Res 18 (1), 369 (2023)
   PUBMED   37202775
  REMARK    GeneRIF: LRP5-/6 gene polymorphisms and its association with risk
            of abnormal bone mass in postmenopausal women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1519)
  AUTHORS   Hao,H., Liu,Q., Chen,J. and Zhou,H.
  TITLE     Overexpression of circRNAs LRP6 in gestational diabetes mellitus
            predicts foetal malformation and intrauterine death
  JOURNAL   Endocrinol Diabetes Nutr (Engl Ed) 70 (2), 124-129 (2023)
   PUBMED   36925229
  REMARK    GeneRIF: Overexpression of circRNAs LRP6 in gestational diabetes
            mellitus predicts foetal malformation and intrauterine death.
REFERENCE   5  (residues 1 to 1519)
  AUTHORS   Wang,J., Yang,H., Ma,X., Liu,J., Li,L., Chen,L. and Wei,F.
  TITLE     LRP6/filamentous-actin signaling facilitates osteogenic commitment
            in mechanically induced periodontal ligament stem cells
  JOURNAL   Cell Mol Biol Lett 28 (1), 7 (2023)
   PUBMED   36694134
  REMARK    GeneRIF: LRP6/filamentous-actin signaling facilitates osteogenic
            commitment in mechanically induced periodontal ligament stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1519)
  AUTHORS   Bafico,A., Liu,G., Yaniv,A., Gazit,A. and Aaronson,S.A.
  TITLE     Novel mechanism of Wnt signalling inhibition mediated by Dickkopf-1
            interaction with LRP6/Arrow
  JOURNAL   Nat Cell Biol 3 (7), 683-686 (2001)
   PUBMED   11433302
REFERENCE   7  (residues 1 to 1519)
  AUTHORS   Mao,B., Wu,W., Li,Y., Hoppe,D., Stannek,P., Glinka,A. and Niehrs,C.
  TITLE     LDL-receptor-related protein 6 is a receptor for Dickkopf proteins
  JOURNAL   Nature 411 (6835), 321-325 (2001)
   PUBMED   11357136
REFERENCE   8  (residues 1 to 1519)
  AUTHORS   Tamai,K., Semenov,M., Kato,Y., Spokony,R., Liu,C., Katsuyama,Y.,
            Hess,F., Saint-Jeannet,J.P. and He,X.
  TITLE     LDL-receptor-related proteins in Wnt signal transduction
  JOURNAL   Nature 407 (6803), 530-535 (2000)
   PUBMED   11029007
REFERENCE   9  (residues 1 to 1519)
  AUTHORS   Baens,M., Wlodarska,I., Corveleyn,A., Hoornaert,I., Hagemeijer,A.
            and Marynen,P.
  TITLE     A physical, transcript, and deletion map of chromosome region
            12p12.3 flanked by ETV6 and CDKN1B: hypermethylation of the LRP6
            CpG island in two leukemia patients with hemizygous del(12p)
  JOURNAL   Genomics 56 (1), 40-50 (1999)
   PUBMED   10036184
REFERENCE   10 (residues 1 to 1519)
  AUTHORS   Brown,S.D., Twells,R.C., Hey,P.J., Cox,R.D., Levy,E.R.,
            Soderman,A.R., Metzker,M.L., Caskey,C.T., Todd,J.A. and Hess,J.F.
  TITLE     Isolation and characterization of LRP6, a novel member of the low
            density lipoprotein receptor gene family
  JOURNAL   Biochem Biophys Res Commun 248 (3), 879-888 (1998)
   PUBMED   9704021
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007621.34, AC007537.3 and
            KF455603.1.
            
            Summary: This gene encodes a member of the low density lipoprotein
            (LDL) receptor gene family. LDL receptors are transmembrane cell
            surface proteins involved in receptor-mediated endocytosis of
            lipoprotein and protein ligands. The protein encoded by this gene
            functions as a receptor or, with Frizzled, a co-receptor for Wnt
            and thereby transmits the canonical Wnt/beta-catenin signaling
            cascade. Through its interaction with the Wnt/beta-catenin
            signaling cascade this gene plays a role in the regulation of cell
            differentiation, proliferation, and migration and the development
            of many cancer types. This protein undergoes gamma-secretase
            dependent RIP- (regulated intramembrane proteolysis) processing but
            the precise locations of the cleavage sites have not been
            determined.[provided by RefSeq, Dec 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1349859.1,
                                           SRR14038193.1589278.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1519
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..1519
                     /product="low-density lipoprotein receptor-related protein
                     6 isoform g precursor"
                     /note="low-density lipoprotein receptor-related protein 6;
                     LRP-6"
                     /calculated_mol_wt=168014
     Region          1..204
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
                     /calculated_mol_wt=2024
     Region          20..275
                     /region_name="Beta-propeller 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            42
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            81
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          89..127
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          150..191
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          175..216
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          217..251
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          237..276
                     /region_name="LDL-receptor class B 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          286..323
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          328..589
                     /region_name="Beta-propeller 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          353..393
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          397..437
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          458..499
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          483..524
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            486
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          525..558
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          592..627
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          631..890
                     /region_name="Beta-propeller 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          <654..813
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Site            692
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          697..739
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          827..866
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            859
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            865
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          893..929
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            926
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          933..1202
                     /region_name="Beta-propeller 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          958..998
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          <968..1075
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Site            1039
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          1094..1136
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1207..1243
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1249..1285
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1254,1264,1275..1276)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1268,1271,1275,1281..1282)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1278..1282
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1288..1322
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1293,1301,1312..1313)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1305,1308,1312,1318..1319)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1315..1319
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1326..1360
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1331,1339,1350..1351)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1343,1346,1350,1356..1357)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1353..1357
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            1371..1393
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            1420
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:16513652; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1430
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:16513652; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1479
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17569865; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          1487..1493
                     /region_name="PPPSP motif A"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            1490
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK14, GRK5 and GRK6.
                     /evidence=ECO:0000269|PubMed:16341017,
                     ECO:0000269|PubMed:17698587, ECO:0000269|PubMed:18762581,
                     ECO:0000269|PubMed:19801552, ECO:0000269|PubMed:20059949,
                     ECO:0000269|PubMed:25331957, ECO:0000269|PubMed:27821587,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1493
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK1.
                     /evidence=ECO:0000269|PubMed:16341017; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     CDS             1..1519
                     /gene="LRP6"
                     /gene_synonym="ADCAD2; EVR8; OPTA4; STHAG7"
                     /coded_by="NM_001414250.1:310..4869"
                     /note="isoform g precursor is encoded by transcript
                     variant 8"
                     /db_xref="GeneID:4040"
                     /db_xref="HGNC:HGNC:6698"
                     /db_xref="MIM:603507"
ORIGIN      
        1 mgavlrslla csfcvllraa plllyanrrd lrlvdatngk enativvggl edaaavdfvf
       61 shgliywsdv seeaikrtef nktesvqnvv vsgllspdgl acdwlgekly wtdsetnrie
      121 vsnldgslrk vlfwqeldqp raialdpssg fmywtdwgev pkieragmdg ssrfiiinse
      181 iywpngltld yeeqklywad aklnfihksn ldgtnrqavv kgslphpfal tlfedilywt
      241 dwsthsilac nkytgeglre ihsdifspmd ihafsqqrqp natnpcgidn ggcshlclms
      301 pvkpfyqcac ptgvklleng ktckdgatel lllarrtdlr risldtpdft divlqledir
      361 haiaidydpv egyiywtdde vrairrsfid gsgsqfvvta qiahpdgiav dwvarnlywt
      421 dtgtdrievt rlngtmrkil isedleepra ivldpmvgym ywtdwgeipk ieraaldgsd
      481 rvvlvntslg wpnglaldyd egkiywgdak tdkievmntd gtgrrvlved kiphifgftl
      541 lgdyvywtdw qrrsiervhk rsaereviid qlpdlmglka tnvhrvigsn pcaeenggcs
      601 hlclyrpqgl rcacpigfel isdmktcivp eafllfsrra dirrisletn nnnvaipltg
      661 vkeasaldfd vtdnriywtd islktisraf mngsalehvv efgldypegm avdwlgknly
      721 wadtgtnrie vskldgqhrq vlvwkdldsp ralaldpaeg fmywtewggk pkidraamdg
      781 serttlvpnv grangltidy akrrlywtdl dtnliessnm lglnreviad dlphpfgltq
      841 yqdyiywtdw srrsierank tsgqnrtiiq ghldyvmdil vfhssrqsgw necassnghc
      901 shlclavpvg gfvcgcpahy slnadnrtcs apttfllfsq ksainrmvid eqqspdiilp
      961 ihslrnvrai dydpldkqly widsrqnmir kaqedgsqgf tvvvssvpsq nleiqpydls
     1021 idiysryiyw tceatnvinv trldgrsvgv vlkgeqdrpr avvvnpekgy myftnlqers
     1081 pkieraaldg terevlffsg lskpialald srlgklfwad sdlrriessd lsganrivle
     1141 dsnilqpvgl tvfenwlywi dkqqqmieki dmtgregrtk vqariaqlsd ihavkelnlq
     1201 eyrqhpcaqd nggcshiclv kgdgttrcsc pmhlvllqde lscgepptcs pqqftcftge
     1261 idcipvawrc dgftecedhs delncpvcse sqfqcasgqc idgalrcngd ancqdksdek
     1321 ncevlclidq frcangqcig khkkcdhnvd csdksdeldc ypteepapqa tntvgsvigv
     1381 ivtifvsgtv yficqrmlcp rmkgdgetmt ndyvvhgpas vplgyvphps slsgslpgms
     1441 rgksmissls imggssgppy drahvtgass ssssstkgty fpailnppps patershytm
     1501 efgyssnsps thrsysfff
//
LOCUS       NP_001350825             499 aa            linear   PRI 21-DEC-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase FTO isoform 4 [Homo
            sapiens].
ACCESSION   NP_001350825
VERSION     NP_001350825.1
DBSOURCE    REFSEQ: accession NM_001363896.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Li,B., Wang,L., Du,M. and He,H.
  TITLE     FTO in oral diseases: Functions, mechanisms, and therapeutic
            potential
  JOURNAL   FASEB J 38 (20), e70115 (2024)
   PUBMED   39436191
  REMARK    GeneRIF: FTO in oral diseases: Functions, mechanisms, and
            therapeutic potential.
            Review article
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Li,Q. and Mu,S.
  TITLE     FTO mediates the diabetic kidney disease progression through
            regulating the m6A modification of NLRP3
  JOURNAL   BMC Nephrol 25 (1), 345 (2024)
   PUBMED   39390397
  REMARK    GeneRIF: FTO mediates the diabetic kidney disease progression
            through regulating the m[6]A modification of NLRP3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Shan,L., Tao,M., Zhang,W., Zhao,J.D., Liu,X.C., Fang,Z.H. and
            Gao,J.R.
  TITLE     Comprehensive analysis of the m6A demethylase FTO in endothelial
            dysfunction by MeRIP sequencing
  JOURNAL   Exp Cell Res 442 (2), 114268 (2024)
   PUBMED   39343042
  REMARK    GeneRIF: Comprehensive analysis of the m[6]A demethylase FTO in
            endothelial dysfunction by MeRIP sequencing.
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Nabeel-Shah,S., Pu,S., Burke,G.L., Ahmed,N., Braunschweig,U.,
            Farhangmehr,S., Lee,H., Wu,M., Ni,Z., Tang,H., Zhong,G., Marcon,E.,
            Zhang,Z., Blencowe,B.J. and Greenblatt,J.F.
  TITLE     Recruitment of the m6A/m6Am demethylase FTO to target RNAs by the
            telomeric zinc finger protein ZBTB48
  JOURNAL   Genome Biol 25 (1), 246 (2024)
   PUBMED   39300486
  REMARK    GeneRIF: Recruitment of the m[6]A/m6Am demethylase FTO to target
            RNAs by the telomeric zinc finger protein ZBTB48.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Hussain,M., Waheed,A., Elahi,A. and Mustafa,G.
  TITLE     Fat Mass and Obesity-Related (FTO) Gene Variant Is a Predictor of
            CVD in T2DM Patients
  JOURNAL   J Diabetes Res 2024, 5914316 (2024)
   PUBMED   39257882
  REMARK    GeneRIF: Fat Mass and Obesity-Related (FTO) Gene Variant Is a
            Predictor of CVD in T2DM Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Zeggini,E., Weedon,M.N., Lindgren,C.M., Frayling,T.M.,
            Elliott,K.S., Lango,H., Timpson,N.J., Perry,J.R., Rayner,N.W.,
            Freathy,R.M., Barrett,J.C., Shields,B., Morris,A.P., Ellard,S.,
            Groves,C.J., Harries,L.W., Marchini,J.L., Owen,K.R., Knight,B.,
            Cardon,L.R., Walker,M., Hitman,G.A., Morris,A.D., Doney,A.S.,
            McCarthy,M.I. and Hattersley,A.T.
  CONSRTM   Wellcome Trust Case Control Consortium (WTCCC)
  TITLE     Replication of genome-wide association signals in UK samples
            reveals risk loci for type 2 diabetes
  JOURNAL   Science 316 (5829), 1336-1341 (2007)
   PUBMED   17463249
  REMARK    Erratum:[Science. 2007 Aug 24;317(5841):1035-6]
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Scott,L.J., Mohlke,K.L., Bonnycastle,L.L., Willer,C.J., Li,Y.,
            Duren,W.L., Erdos,M.R., Stringham,H.M., Chines,P.S., Jackson,A.U.,
            Prokunina-Olsson,L., Ding,C.J., Swift,A.J., Narisu,N., Hu,T.,
            Pruim,R., Xiao,R., Li,X.Y., Conneely,K.N., Riebow,N.L., Sprau,A.G.,
            Tong,M., White,P.P., Hetrick,K.N., Barnhart,M.W., Bark,C.W.,
            Goldstein,J.L., Watkins,L., Xiang,F., Saramies,J., Buchanan,T.A.,
            Watanabe,R.M., Valle,T.T., Kinnunen,L., Abecasis,G.R., Pugh,E.W.,
            Doheny,K.F., Bergman,R.N., Tuomilehto,J., Collins,F.S. and
            Boehnke,M.
  TITLE     A genome-wide association study of type 2 diabetes in Finns detects
            multiple susceptibility variants
  JOURNAL   Science 316 (5829), 1341-1345 (2007)
   PUBMED   17463248
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Dina,C., Meyre,D., Gallina,S., Durand,E., Korner,A., Jacobson,P.,
            Carlsson,L.M., Kiess,W., Vatin,V., Lecoeur,C., Delplanque,J.,
            Vaillant,E., Pattou,F., Ruiz,J., Weill,J., Levy-Marchal,C.,
            Horber,F., Potoczna,N., Hercberg,S., Le Stunff,C., Bougneres,P.,
            Kovacs,P., Marre,M., Balkau,B., Cauchi,S., Chevre,J.C. and
            Froguel,P.
  TITLE     Variation in FTO contributes to childhood obesity and severe adult
            obesity
  JOURNAL   Nat Genet 39 (6), 724-726 (2007)
   PUBMED   17496892
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            GeneRIF: Association with obesity in adult and childre.
            Interestingly, this association receives clear confirmation under a
            Transmission Disequilibrium Test design which is robust to
            population stratification.
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Frayling,T.M., Timpson,N.J., Weedon,M.N., Zeggini,E., Freathy,R.M.,
            Lindgren,C.M., Perry,J.R., Elliott,K.S., Lango,H., Rayner,N.W.,
            Shields,B., Harries,L.W., Barrett,J.C., Ellard,S., Groves,C.J.,
            Knight,B., Patch,A.M., Ness,A.R., Ebrahim,S., Lawlor,D.A.,
            Ring,S.M., Ben-Shlomo,Y., Jarvelin,M.R., Sovio,U., Bennett,A.J.,
            Melzer,D., Ferrucci,L., Loos,R.J., Barroso,I., Wareham,N.J.,
            Karpe,F., Owen,K.R., Cardon,L.R., Walker,M., Hitman,G.A.,
            Palmer,C.N., Doney,A.S., Morris,A.D., Smith,G.D., Hattersley,A.T.
            and McCarthy,M.I.
  TITLE     A common variant in the FTO gene is associated with body mass index
            and predisposes to childhood and adult obesity
  JOURNAL   Science 316 (5826), 889-894 (2007)
   PUBMED   17434869
  REMARK    GeneRIF: A genome-wide search for type 2 diabetes-susceptibility
            genes identified a common variant in the FTO gene that predisposes
            to diabetes through an effect on body mass index
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-environment interaction. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Peters,T., Ausmeier,K. and Ruther,U.
  TITLE     Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft)
            mouse mutation
  JOURNAL   Mamm Genome 10 (10), 983-986 (1999)
   PUBMED   10501967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007909.8, AC007496.6 and
            AC007347.3.
            
            Summary: This gene is a nuclear protein of the AlkB related
            non-haem iron and 2-oxoglutarate-dependent oxygenase superfamily
            but the exact physiological function of this gene is not known.
            Other non-heme iron enzymes function to reverse alkylated DNA and
            RNA damage by oxidative demethylation. Studies in mice and humans
            indicate a role in nervous and cardiovascular systems and a strong
            association with body mass index, obesity risk, and type 2
            diabetes. [provided by RefSeq, Jul 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.176441.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..499
                     /product="alpha-ketoglutarate-dependent dioxygenase FTO
                     isoform 4"
                     /EC_number="1.14.11.53"
                     /note="alpha-ketoglutarate-dependent dioxygenase FTO; fat
                     mass and obesity-associated protein; AlkB homolog 9; fat
                     mass and obesity associated; m6A(m)-demethylase FTO; tRNA
                     N1-methyl adenine demethylase FTO; mRNA
                     N(6)-methyladenosine demethylase FTO; mRNA
                     (2'-O-methyladenosine-N(6)-)-demethylase FTO; U6 small
                     nuclear RNA N(6)-methyladenosine-demethylase FTO; U6 small
                     nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO;
                     intragenic FTO exon 9 containing transcript; mRNA
                     N(6)-methyladenine demethylase"
                     /calculated_mol_wt=57331
     Region          36..325
                     /region_name="FTO_NTD"
                     /note="FTO catalytic domain; pfam12933"
                     /db_xref="CDD:463755"
     Region          329..492
                     /region_name="FTO_CTD"
                     /note="FTO C-terminal domain; pfam12934"
                     /db_xref="CDD:432887"
     CDS             1..499
                     /gene="FTO"
                     /gene_synonym="ALKBH9; BMIQ14; GDFD; IFEX9"
                     /coded_by="NM_001363896.2:30..1529"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:79068"
                     /db_xref="HGNC:HGNC:24678"
                     /db_xref="MIM:610966"
ORIGIN      
        1 mkrtptaeer ereakklrll eeledtwlpy ltpkddefyq qwqlkypkli lreassvsee
       61 lhkevqeafl tlhkhgclfr dlvriqgkdl ltpvsrilig npgctykyln trlftvpwpv
      121 kgsnikhtea eiaaacetfl klndylqiet iqaleelaak ekanedavpl cmsadfprvg
      181 mgssyngqde vdiksraayn vtllnfmdpq kmpylkeepy fgmgkmavsw hhdenlvdrs
      241 avavysysce gpeeesedds hlegrdpdiw hvgfkiswdi etpglaiplh qgdcyfmldd
      301 lnathqhcvl agsqprfsst hrvaecstgt ldyilqrcql alqnvcddvd nddvslksfe
      361 pavlkqgeei hnevefewlr qfwfqgnryr kctdwwcqpm aqlealwkkm egvmefhsrc
      421 pgwsamaqsw ltatstsrvq villpqpprc qsriartlpa dqkpecrpyw ekddasmplp
      481 fdltdivsel rgqlleakp
//
LOCUS       NP_001401181            1462 aa            linear   PRI 21-DEC-2025
DEFINITION  low-density lipoprotein receptor-related protein 6 isoform i [Homo
            sapiens].
ACCESSION   NP_001401181 XP_011518973
VERSION     NP_001401181.1
DBSOURCE    REFSEQ: accession NM_001414252.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1462)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1462)
  AUTHORS   Zhong,S., Guo,Q., Chen,X., Luo,X., Long,Y., Chong,T., Ye,M., He,H.,
            Lu,A., Ao,K., Yin,M., Xu,A., Li,X., Hao,Y. and Guo,X.
  TITLE     The inhibition of YTHDF3/m6A/LRP6 reprograms fatty acid metabolism
            and suppresses lymph node metastasis in cervical cancer
  JOURNAL   Int J Biol Sci 20 (3), 916-936 (2024)
   PUBMED   38250152
  REMARK    GeneRIF: The inhibition of YTHDF3/m[6]A/LRP6 reprograms fatty acid
            metabolism and suppresses lymph node metastasis in cervical cancer.
            Erratum:[Int J Biol Sci. 2025 Jun 5;21(8):3825-3826. doi:
            10.7150/ijbs.115928. PMID: 40520018]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1462)
  AUTHORS   Li,J., Liu,Z., Ren,Y., Shao,H. and Li,S.
  TITLE     LRP5-/6 gene polymorphisms and its association with risk of
            abnormal bone mass in postmenopausal women
  JOURNAL   J Orthop Surg Res 18 (1), 369 (2023)
   PUBMED   37202775
  REMARK    GeneRIF: LRP5-/6 gene polymorphisms and its association with risk
            of abnormal bone mass in postmenopausal women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1462)
  AUTHORS   Hao,H., Liu,Q., Chen,J. and Zhou,H.
  TITLE     Overexpression of circRNAs LRP6 in gestational diabetes mellitus
            predicts foetal malformation and intrauterine death
  JOURNAL   Endocrinol Diabetes Nutr (Engl Ed) 70 (2), 124-129 (2023)
   PUBMED   36925229
  REMARK    GeneRIF: Overexpression of circRNAs LRP6 in gestational diabetes
            mellitus predicts foetal malformation and intrauterine death.
REFERENCE   5  (residues 1 to 1462)
  AUTHORS   Wang,J., Yang,H., Ma,X., Liu,J., Li,L., Chen,L. and Wei,F.
  TITLE     LRP6/filamentous-actin signaling facilitates osteogenic commitment
            in mechanically induced periodontal ligament stem cells
  JOURNAL   Cell Mol Biol Lett 28 (1), 7 (2023)
   PUBMED   36694134
  REMARK    GeneRIF: LRP6/filamentous-actin signaling facilitates osteogenic
            commitment in mechanically induced periodontal ligament stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1462)
  AUTHORS   Bafico,A., Liu,G., Yaniv,A., Gazit,A. and Aaronson,S.A.
  TITLE     Novel mechanism of Wnt signalling inhibition mediated by Dickkopf-1
            interaction with LRP6/Arrow
  JOURNAL   Nat Cell Biol 3 (7), 683-686 (2001)
   PUBMED   11433302
REFERENCE   7  (residues 1 to 1462)
  AUTHORS   Mao,B., Wu,W., Li,Y., Hoppe,D., Stannek,P., Glinka,A. and Niehrs,C.
  TITLE     LDL-receptor-related protein 6 is a receptor for Dickkopf proteins
  JOURNAL   Nature 411 (6835), 321-325 (2001)
   PUBMED   11357136
REFERENCE   8  (residues 1 to 1462)
  AUTHORS   Tamai,K., Semenov,M., Kato,Y., Spokony,R., Liu,C., Katsuyama,Y.,
            Hess,F., Saint-Jeannet,J.P. and He,X.
  TITLE     LDL-receptor-related proteins in Wnt signal transduction
  JOURNAL   Nature 407 (6803), 530-535 (2000)
   PUBMED   11029007
REFERENCE   9  (residues 1 to 1462)
  AUTHORS   Baens,M., Wlodarska,I., Corveleyn,A., Hoornaert,I., Hagemeijer,A.
            and Marynen,P.
  TITLE     A physical, transcript, and deletion map of chromosome region
            12p12.3 flanked by ETV6 and CDKN1B: hypermethylation of the LRP6
            CpG island in two leukemia patients with hemizygous del(12p)
  JOURNAL   Genomics 56 (1), 40-50 (1999)
   PUBMED   10036184
REFERENCE   10 (residues 1 to 1462)
  AUTHORS   Brown,S.D., Twells,R.C., Hey,P.J., Cox,R.D., Levy,E.R.,
            Soderman,A.R., Metzker,M.L., Caskey,C.T., Todd,J.A. and Hess,J.F.
  TITLE     Isolation and characterization of LRP6, a novel member of the low
            density lipoprotein receptor gene family
  JOURNAL   Biochem Biophys Res Commun 248 (3), 879-888 (1998)
   PUBMED   9704021
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007621.34, AC007537.3 and
            KF455603.1.
            
            On Nov 16, 2022 this sequence version replaced XP_011518973.1.
            
            Summary: This gene encodes a member of the low density lipoprotein
            (LDL) receptor gene family. LDL receptors are transmembrane cell
            surface proteins involved in receptor-mediated endocytosis of
            lipoprotein and protein ligands. The protein encoded by this gene
            functions as a receptor or, with Frizzled, a co-receptor for Wnt
            and thereby transmits the canonical Wnt/beta-catenin signaling
            cascade. Through its interaction with the Wnt/beta-catenin
            signaling cascade this gene plays a role in the regulation of cell
            differentiation, proliferation, and migration and the development
            of many cancer types. This protein undergoes gamma-secretase
            dependent RIP- (regulated intramembrane proteolysis) processing but
            the precise locations of the cleavage sites have not been
            determined.[provided by RefSeq, Dec 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.6566.1,
                                           SRR11853563.6833.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..1462
                     /product="low-density lipoprotein receptor-related protein
                     6 isoform i"
                     /note="low-density lipoprotein receptor-related protein 6;
                     LRP-6"
                     /calculated_mol_wt=163681
     Region          1..40
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          24..65
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          66..100
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          135..172
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          202..242
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          246..286
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          307..348
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          332..373
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          374..407
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          441..476
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          <503..662
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          546..588
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          676..715
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          742..778
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          807..847
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          <817..924
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          943..985
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1056..1092
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1098..1134
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1103,1113,1124..1125)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1117,1120,1124,1130..1131)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1127..1131
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1137..1171
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1142,1150,1161..1162)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1154,1157,1161,1167..1168)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1164..1168
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1175..1209
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1180,1188,1199..1200)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1192,1195,1199,1205..1206)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1202..1206
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     CDS             1..1462
                     /gene="LRP6"
                     /gene_synonym="ADCAD2; EVR8; OPTA4; STHAG7"
                     /coded_by="NM_001414252.1:369..4757"
                     /note="isoform i is encoded by transcript variant 10"
                     /db_xref="GeneID:4040"
                     /db_xref="HGNC:HGNC:6698"
                     /db_xref="MIM:603507"
ORIGIN      
        1 mywtdwgevp kieragmdgs srfiiinsei ywpngltldy eeqklywada klnfihksnl
       61 dgtnrqavvk gslphpfalt lfedilywtd wsthsilacn kytgeglrei hsdifspmdi
      121 hafsqqrqpn atnpcgidng gcshlclmsp vkpfyqcacp tgvkllengk tckdgatell
      181 llarrtdlrr isldtpdftd ivlqledirh aiaidydpve gyiywtddev rairrsfidg
      241 sgsqfvvtaq iahpdgiavd wvarnlywtd tgtdrievtr lngtmrkili sedleeprai
      301 vldpmvgymy wtdwgeipki eraaldgsdr vvlvntslgw pnglaldyde gkiywgdakt
      361 dkievmntdg tgrrvlvedk iphifgftll gdyvywtdwq rrsiervhkr saereviidq
      421 lpdlmglkat nvhrvigsnp caeenggcsh lclyrpqglr cacpigfeli sdmktcivpe
      481 afllfsrrad irrisletnn nnvaipltgv keasaldfdv tdnriywtdi slktisrafm
      541 ngsalehvve fgldypegma vdwlgknlyw adtgtnriev skldgqhrqv lvwkdldspr
      601 alaldpaegf mywtewggkp kidraamdgs erttlvpnvg rangltidya krrlywtdld
      661 tnliessnml glnreviadd lphpfgltqy qdyiywtdws rrsierankt sgqnrtiiqg
      721 hldyvmdilv fhssrqsgwn ecassnghcs hlclavpvgg fvcgcpahys lnadnrtcsa
      781 pttfllfsqk sainrmvide qqspdiilpi hslrnvraid ydpldkqlyw idsrqnmirk
      841 aqedgsqgft vvvssvpsqn leiqpydlsi diysryiywt ceatnvinvt rldgrsvgvv
      901 lkgeqdrpra vvvnpekgym yftnlqersp kieraaldgt erevlffsgl skpialalds
      961 rlgklfwads dlrriessdl sganrivled snilqpvglt vfenwlywid kqqqmiekid
     1021 mtgregrtkv qariaqlsdi havkelnlqe yrqhpcaqdn ggcshiclvk gdgttrcscp
     1081 mhlvllqdel scgepptcsp qqftcftgei dcipvawrcd gftecedhsd elncpvcses
     1141 qfqcasgqci dgalrcngda ncqdksdekn cevlclidqf rcangqcigk hkkcdhnvdc
     1201 sdksdeldcy pteepapqat ntvgsvigvi vtifvsgtvy ficqrmlcpr mkgdgetmtn
     1261 dyvvhgpasv plgyvphpss lsgslpgmsr gksmisslsi mggssgppyd rahvtgasss
     1321 sssstkgtyf pailnpppsp atershytme fgyssnspst hrsysyrpys yrhfappttp
     1381 cstdvcdsdy apsrrmtsva takgytsdln ydsepvpppp tprsqylsae enyescppsp
     1441 ytersyshhl yppppspctd ss
//
LOCUS       NP_112240                153 aa            linear   PRI 21-DEC-2025
DEFINITION  actin-related protein 2/3 complex subunit 5-like protein [Homo
            sapiens].
ACCESSION   NP_112240 XP_005252307
VERSION     NP_112240.1
DBSOURCE    REFSEQ: accession NM_030978.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Sindram,E., Caballero-Oteyza,A., Kogata,N., Chor Mei Huang,S.,
            Alizadeh,Z., Gamez-Diaz,L., Fazlollhi,M.R., Peng,X., Grimbacher,B.,
            Way,M. and Proietti,M.
  TITLE     ARPC5 deficiency leads to severe early-onset systemic inflammation
            and mortality
  JOURNAL   Dis Model Mech 16 (7) (2023)
   PUBMED   37382373
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Abella,J.V., Galloni,C., Pernier,J., Barry,D.J., Kjaer,S.,
            Carlier,M.F. and Way,M.
  TITLE     Isoform diversity in the Arp2/3 complex determines actin filament
            dynamics
  JOURNAL   Nat Cell Biol 18 (1), 76-86 (2016)
   PUBMED   26655834
REFERENCE   6  (residues 1 to 153)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 153)
  AUTHORS   Kuo,J.C., Han,X., Hsiao,C.T., Yates,J.R. 3rd and Waterman,C.M.
  TITLE     Analysis of the myosin-II-responsive focal adhesion proteome
            reveals a role for beta-Pix in negative regulation of focal
            adhesion maturation
  JOURNAL   Nat Cell Biol 13 (4), 383-393 (2011)
   PUBMED   21423176
REFERENCE   8  (residues 1 to 153)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   9  (residues 1 to 153)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   10 (residues 1 to 153)
  AUTHORS   Millard,T.H., Behrendt,B., Launay,S., Futterer,K. and Machesky,L.M.
  TITLE     Identification and characterisation of a novel human isoform of
            Arp2/3 complex subunit p16-ARC/ARPC5
  JOURNAL   Cell Motil Cytoskeleton 54 (1), 81-90 (2003)
   PUBMED   12451597
  REMARK    Erratum:[Cell Motil Cytoskeleton. 2003 Mar;54(3):266]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK056174.1, AL354928.9 and AA731112.1.
            
            On Dec 18, 2015 this sequence version replaced XP_005252307.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056174.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000353214.6/ ENSP00000345361.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..153
                     /product="actin-related protein 2/3 complex subunit 5-like
                     protein"
                     /note="arp2/3 complex 16 kDa subunit 2; epididymis
                     secretory sperm binding protein"
                     /calculated_mol_wt=16810
     Region          9..151
                     /region_name="P16-Arc"
                     /note="ARP2/3 complex 16 kDa subunit (p16-Arc); pfam04699"
                     /db_xref="CDD:461399"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BPX5.1)"
     CDS             1..153
                     /gene="ARPC5L"
                     /gene_synonym="ARC16-2; ARPC5B"
                     /coded_by="NM_030978.3:1253..1714"
                     /db_xref="CCDS:CCDS6859.1"
                     /db_xref="GeneID:81873"
                     /db_xref="HGNC:HGNC:23366"
                     /db_xref="MIM:621450"
ORIGIN      
        1 marntlssrf rrvdidefde nkfvdeqeea aaaaaepgpd psevdgllrq gdmlrafhaa
       61 lrnspvntkn qavkeraqgv vlkvltnfks seieqavqsl drngvdllmk yiykgfekpt
      121 enssavllqw hekalavggl gsiirvltar ktv
//
LOCUS       NP_001401180            1492 aa            linear   PRI 21-DEC-2025
DEFINITION  low-density lipoprotein receptor-related protein 6 isoform h [Homo
            sapiens].
ACCESSION   NP_001401180
VERSION     NP_001401180.1
DBSOURCE    REFSEQ: accession NM_001414251.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1492)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1492)
  AUTHORS   Zhong,S., Guo,Q., Chen,X., Luo,X., Long,Y., Chong,T., Ye,M., He,H.,
            Lu,A., Ao,K., Yin,M., Xu,A., Li,X., Hao,Y. and Guo,X.
  TITLE     The inhibition of YTHDF3/m6A/LRP6 reprograms fatty acid metabolism
            and suppresses lymph node metastasis in cervical cancer
  JOURNAL   Int J Biol Sci 20 (3), 916-936 (2024)
   PUBMED   38250152
  REMARK    GeneRIF: The inhibition of YTHDF3/m[6]A/LRP6 reprograms fatty acid
            metabolism and suppresses lymph node metastasis in cervical cancer.
            Erratum:[Int J Biol Sci. 2025 Jun 5;21(8):3825-3826. doi:
            10.7150/ijbs.115928. PMID: 40520018]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1492)
  AUTHORS   Li,J., Liu,Z., Ren,Y., Shao,H. and Li,S.
  TITLE     LRP5-/6 gene polymorphisms and its association with risk of
            abnormal bone mass in postmenopausal women
  JOURNAL   J Orthop Surg Res 18 (1), 369 (2023)
   PUBMED   37202775
  REMARK    GeneRIF: LRP5-/6 gene polymorphisms and its association with risk
            of abnormal bone mass in postmenopausal women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1492)
  AUTHORS   Hao,H., Liu,Q., Chen,J. and Zhou,H.
  TITLE     Overexpression of circRNAs LRP6 in gestational diabetes mellitus
            predicts foetal malformation and intrauterine death
  JOURNAL   Endocrinol Diabetes Nutr (Engl Ed) 70 (2), 124-129 (2023)
   PUBMED   36925229
  REMARK    GeneRIF: Overexpression of circRNAs LRP6 in gestational diabetes
            mellitus predicts foetal malformation and intrauterine death.
REFERENCE   5  (residues 1 to 1492)
  AUTHORS   Wang,J., Yang,H., Ma,X., Liu,J., Li,L., Chen,L. and Wei,F.
  TITLE     LRP6/filamentous-actin signaling facilitates osteogenic commitment
            in mechanically induced periodontal ligament stem cells
  JOURNAL   Cell Mol Biol Lett 28 (1), 7 (2023)
   PUBMED   36694134
  REMARK    GeneRIF: LRP6/filamentous-actin signaling facilitates osteogenic
            commitment in mechanically induced periodontal ligament stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1492)
  AUTHORS   Bafico,A., Liu,G., Yaniv,A., Gazit,A. and Aaronson,S.A.
  TITLE     Novel mechanism of Wnt signalling inhibition mediated by Dickkopf-1
            interaction with LRP6/Arrow
  JOURNAL   Nat Cell Biol 3 (7), 683-686 (2001)
   PUBMED   11433302
REFERENCE   7  (residues 1 to 1492)
  AUTHORS   Mao,B., Wu,W., Li,Y., Hoppe,D., Stannek,P., Glinka,A. and Niehrs,C.
  TITLE     LDL-receptor-related protein 6 is a receptor for Dickkopf proteins
  JOURNAL   Nature 411 (6835), 321-325 (2001)
   PUBMED   11357136
REFERENCE   8  (residues 1 to 1492)
  AUTHORS   Tamai,K., Semenov,M., Kato,Y., Spokony,R., Liu,C., Katsuyama,Y.,
            Hess,F., Saint-Jeannet,J.P. and He,X.
  TITLE     LDL-receptor-related proteins in Wnt signal transduction
  JOURNAL   Nature 407 (6803), 530-535 (2000)
   PUBMED   11029007
REFERENCE   9  (residues 1 to 1492)
  AUTHORS   Baens,M., Wlodarska,I., Corveleyn,A., Hoornaert,I., Hagemeijer,A.
            and Marynen,P.
  TITLE     A physical, transcript, and deletion map of chromosome region
            12p12.3 flanked by ETV6 and CDKN1B: hypermethylation of the LRP6
            CpG island in two leukemia patients with hemizygous del(12p)
  JOURNAL   Genomics 56 (1), 40-50 (1999)
   PUBMED   10036184
REFERENCE   10 (residues 1 to 1492)
  AUTHORS   Brown,S.D., Twells,R.C., Hey,P.J., Cox,R.D., Levy,E.R.,
            Soderman,A.R., Metzker,M.L., Caskey,C.T., Todd,J.A. and Hess,J.F.
  TITLE     Isolation and characterization of LRP6, a novel member of the low
            density lipoprotein receptor gene family
  JOURNAL   Biochem Biophys Res Commun 248 (3), 879-888 (1998)
   PUBMED   9704021
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007621.34, AC007537.3 and
            KF455603.1.
            
            Summary: This gene encodes a member of the low density lipoprotein
            (LDL) receptor gene family. LDL receptors are transmembrane cell
            surface proteins involved in receptor-mediated endocytosis of
            lipoprotein and protein ligands. The protein encoded by this gene
            functions as a receptor or, with Frizzled, a co-receptor for Wnt
            and thereby transmits the canonical Wnt/beta-catenin signaling
            cascade. Through its interaction with the Wnt/beta-catenin
            signaling cascade this gene plays a role in the regulation of cell
            differentiation, proliferation, and migration and the development
            of many cancer types. This protein undergoes gamma-secretase
            dependent RIP- (regulated intramembrane proteolysis) processing but
            the precise locations of the cleavage sites have not been
            determined.[provided by RefSeq, Dec 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2824924.1,
                                           SRR18074967.1774489.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1492
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..1492
                     /product="low-density lipoprotein receptor-related protein
                     6 isoform h"
                     /note="low-density lipoprotein receptor-related protein 6;
                     LRP-6"
                     /calculated_mol_wt=167222
     Region          1..204
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          89..127
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          150..191
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          175..216
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          217..251
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          286..323
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          353..393
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          397..437
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          458..499
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          483..524
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          525..558
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          592..627
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          <654..813
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          697..739
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          827..866
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          893..929
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          958..998
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          <968..1075
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          1069..1110
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          1094..1136
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1205..1239
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1210,1218,1229..1230)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1222,1225,1229,1235..1236)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1232..1236
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     CDS             1..1492
                     /gene="LRP6"
                     /gene_synonym="ADCAD2; EVR8; OPTA4; STHAG7"
                     /coded_by="NM_001414251.1:310..4788"
                     /note="isoform h is encoded by transcript variant 9"
                     /db_xref="GeneID:4040"
                     /db_xref="HGNC:HGNC:6698"
                     /db_xref="MIM:603507"
ORIGIN      
        1 mgavlrslla csfcvllraa plllyanrrd lrlvdatngk enativvggl edaaavdfvf
       61 shgliywsdv seeaikrtef nktesvqnvv vsgllspdgl acdwlgekly wtdsetnrie
      121 vsnldgslrk vlfwqeldqp raialdpssg fmywtdwgev pkieragmdg ssrfiiinse
      181 iywpngltld yeeqklywad aklnfihksn ldgtnrqavv kgslphpfal tlfedilywt
      241 dwsthsilac nkytgeglre ihsdifspmd ihafsqqrqp natnpcgidn ggcshlclms
      301 pvkpfyqcac ptgvklleng ktckdgatel lllarrtdlr risldtpdft divlqledir
      361 haiaidydpv egyiywtdde vrairrsfid gsgsqfvvta qiahpdgiav dwvarnlywt
      421 dtgtdrievt rlngtmrkil isedleepra ivldpmvgym ywtdwgeipk ieraaldgsd
      481 rvvlvntslg wpnglaldyd egkiywgdak tdkievmntd gtgrrvlved kiphifgftl
      541 lgdyvywtdw qrrsiervhk rsaereviid qlpdlmglka tnvhrvigsn pcaeenggcs
      601 hlclyrpqgl rcacpigfel isdmktcivp eafllfsrra dirrisletn nnnvaipltg
      661 vkeasaldfd vtdnriywtd islktisraf mngsalehvv efgldypegm avdwlgknly
      721 wadtgtnrie vskldgqhrq vlvwkdldsp ralaldpaeg fmywtewggk pkidraamdg
      781 serttlvpnv grangltidy akrrlywtdl dtnliessnm lglnreviad dlphpfgltq
      841 yqdyiywtdw srrsierank tsgqnrtiiq ghldyvmdil vfhssrqsgw necassnghc
      901 shlclavpvg gfvcgcpahy slnadnrtcs apttfllfsq ksainrmvid eqqspdiilp
      961 ihslrnvrai dydpldkqly widsrqnmir kaqedgsqgf tvvvssvpsq nleiqpydls
     1021 idiysryiyw tceatnvinv trldgrsvgv vlkgeqdrpr avvvnpekgy myftnlqers
     1081 pkieraaldg terevlffsg lskpialald srlgklfwad sdlrriessd lsganrivle
     1141 dsnilqpvgl tvfenwlywi dkqqqmieki dmtgregrtk vqariaqlsd ihavkelnlq
     1201 eymlclidqf rcangqcigk hkkcdhnvdc sdksdeldcy pteepapqat ntvgsvigvi
     1261 vtifvsgtvy ficqrmlcpr mkgdgetmtn dyvvhgpasv plgyvphpss lsgslpgmsr
     1321 gksmisslsi mggssgppyd rahvtgasss sssstkgtyf pailnpppsp atershytme
     1381 fgyssnspst hrsysyrpys yrhfappttp cstdvcdsdy apsrrmtsva takgytsdln
     1441 ydsepvpppp tprsqylsae enyescppsp ytersyshhl yppppspctd ss
//
LOCUS       NP_001350834             334 aa            linear   PRI 21-DEC-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase FTO isoform 11 [Homo
            sapiens].
ACCESSION   NP_001350834
VERSION     NP_001350834.1
DBSOURCE    REFSEQ: accession NM_001363905.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Li,B., Wang,L., Du,M. and He,H.
  TITLE     FTO in oral diseases: Functions, mechanisms, and therapeutic
            potential
  JOURNAL   FASEB J 38 (20), e70115 (2024)
   PUBMED   39436191
  REMARK    GeneRIF: FTO in oral diseases: Functions, mechanisms, and
            therapeutic potential.
            Review article
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Li,Q. and Mu,S.
  TITLE     FTO mediates the diabetic kidney disease progression through
            regulating the m6A modification of NLRP3
  JOURNAL   BMC Nephrol 25 (1), 345 (2024)
   PUBMED   39390397
  REMARK    GeneRIF: FTO mediates the diabetic kidney disease progression
            through regulating the m[6]A modification of NLRP3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Shan,L., Tao,M., Zhang,W., Zhao,J.D., Liu,X.C., Fang,Z.H. and
            Gao,J.R.
  TITLE     Comprehensive analysis of the m6A demethylase FTO in endothelial
            dysfunction by MeRIP sequencing
  JOURNAL   Exp Cell Res 442 (2), 114268 (2024)
   PUBMED   39343042
  REMARK    GeneRIF: Comprehensive analysis of the m[6]A demethylase FTO in
            endothelial dysfunction by MeRIP sequencing.
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Nabeel-Shah,S., Pu,S., Burke,G.L., Ahmed,N., Braunschweig,U.,
            Farhangmehr,S., Lee,H., Wu,M., Ni,Z., Tang,H., Zhong,G., Marcon,E.,
            Zhang,Z., Blencowe,B.J. and Greenblatt,J.F.
  TITLE     Recruitment of the m6A/m6Am demethylase FTO to target RNAs by the
            telomeric zinc finger protein ZBTB48
  JOURNAL   Genome Biol 25 (1), 246 (2024)
   PUBMED   39300486
  REMARK    GeneRIF: Recruitment of the m[6]A/m6Am demethylase FTO to target
            RNAs by the telomeric zinc finger protein ZBTB48.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Hussain,M., Waheed,A., Elahi,A. and Mustafa,G.
  TITLE     Fat Mass and Obesity-Related (FTO) Gene Variant Is a Predictor of
            CVD in T2DM Patients
  JOURNAL   J Diabetes Res 2024, 5914316 (2024)
   PUBMED   39257882
  REMARK    GeneRIF: Fat Mass and Obesity-Related (FTO) Gene Variant Is a
            Predictor of CVD in T2DM Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 334)
  AUTHORS   Zeggini,E., Weedon,M.N., Lindgren,C.M., Frayling,T.M.,
            Elliott,K.S., Lango,H., Timpson,N.J., Perry,J.R., Rayner,N.W.,
            Freathy,R.M., Barrett,J.C., Shields,B., Morris,A.P., Ellard,S.,
            Groves,C.J., Harries,L.W., Marchini,J.L., Owen,K.R., Knight,B.,
            Cardon,L.R., Walker,M., Hitman,G.A., Morris,A.D., Doney,A.S.,
            McCarthy,M.I. and Hattersley,A.T.
  CONSRTM   Wellcome Trust Case Control Consortium (WTCCC)
  TITLE     Replication of genome-wide association signals in UK samples
            reveals risk loci for type 2 diabetes
  JOURNAL   Science 316 (5829), 1336-1341 (2007)
   PUBMED   17463249
  REMARK    Erratum:[Science. 2007 Aug 24;317(5841):1035-6]
REFERENCE   7  (residues 1 to 334)
  AUTHORS   Scott,L.J., Mohlke,K.L., Bonnycastle,L.L., Willer,C.J., Li,Y.,
            Duren,W.L., Erdos,M.R., Stringham,H.M., Chines,P.S., Jackson,A.U.,
            Prokunina-Olsson,L., Ding,C.J., Swift,A.J., Narisu,N., Hu,T.,
            Pruim,R., Xiao,R., Li,X.Y., Conneely,K.N., Riebow,N.L., Sprau,A.G.,
            Tong,M., White,P.P., Hetrick,K.N., Barnhart,M.W., Bark,C.W.,
            Goldstein,J.L., Watkins,L., Xiang,F., Saramies,J., Buchanan,T.A.,
            Watanabe,R.M., Valle,T.T., Kinnunen,L., Abecasis,G.R., Pugh,E.W.,
            Doheny,K.F., Bergman,R.N., Tuomilehto,J., Collins,F.S. and
            Boehnke,M.
  TITLE     A genome-wide association study of type 2 diabetes in Finns detects
            multiple susceptibility variants
  JOURNAL   Science 316 (5829), 1341-1345 (2007)
   PUBMED   17463248
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 334)
  AUTHORS   Dina,C., Meyre,D., Gallina,S., Durand,E., Korner,A., Jacobson,P.,
            Carlsson,L.M., Kiess,W., Vatin,V., Lecoeur,C., Delplanque,J.,
            Vaillant,E., Pattou,F., Ruiz,J., Weill,J., Levy-Marchal,C.,
            Horber,F., Potoczna,N., Hercberg,S., Le Stunff,C., Bougneres,P.,
            Kovacs,P., Marre,M., Balkau,B., Cauchi,S., Chevre,J.C. and
            Froguel,P.
  TITLE     Variation in FTO contributes to childhood obesity and severe adult
            obesity
  JOURNAL   Nat Genet 39 (6), 724-726 (2007)
   PUBMED   17496892
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            GeneRIF: Association with obesity in adult and childre.
            Interestingly, this association receives clear confirmation under a
            Transmission Disequilibrium Test design which is robust to
            population stratification.
REFERENCE   9  (residues 1 to 334)
  AUTHORS   Frayling,T.M., Timpson,N.J., Weedon,M.N., Zeggini,E., Freathy,R.M.,
            Lindgren,C.M., Perry,J.R., Elliott,K.S., Lango,H., Rayner,N.W.,
            Shields,B., Harries,L.W., Barrett,J.C., Ellard,S., Groves,C.J.,
            Knight,B., Patch,A.M., Ness,A.R., Ebrahim,S., Lawlor,D.A.,
            Ring,S.M., Ben-Shlomo,Y., Jarvelin,M.R., Sovio,U., Bennett,A.J.,
            Melzer,D., Ferrucci,L., Loos,R.J., Barroso,I., Wareham,N.J.,
            Karpe,F., Owen,K.R., Cardon,L.R., Walker,M., Hitman,G.A.,
            Palmer,C.N., Doney,A.S., Morris,A.D., Smith,G.D., Hattersley,A.T.
            and McCarthy,M.I.
  TITLE     A common variant in the FTO gene is associated with body mass index
            and predisposes to childhood and adult obesity
  JOURNAL   Science 316 (5826), 889-894 (2007)
   PUBMED   17434869
  REMARK    GeneRIF: A genome-wide search for type 2 diabetes-susceptibility
            genes identified a common variant in the FTO gene that predisposes
            to diabetes through an effect on body mass index
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-environment interaction. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 334)
  AUTHORS   Peters,T., Ausmeier,K. and Ruther,U.
  TITLE     Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft)
            mouse mutation
  JOURNAL   Mamm Genome 10 (10), 983-986 (1999)
   PUBMED   10501967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007909.8, AC007496.6 and
            AC007347.3.
            
            Summary: This gene is a nuclear protein of the AlkB related
            non-haem iron and 2-oxoglutarate-dependent oxygenase superfamily
            but the exact physiological function of this gene is not known.
            Other non-heme iron enzymes function to reverse alkylated DNA and
            RNA damage by oxidative demethylation. Studies in mice and humans
            indicate a role in nervous and cardiovascular systems and a strong
            association with body mass index, obesity risk, and type 2
            diabetes. [provided by RefSeq, Jul 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2527379.1,
                                           SRR1803616.199235.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2467143
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..334
                     /product="alpha-ketoglutarate-dependent dioxygenase FTO
                     isoform 11"
                     /EC_number="1.14.11.53"
                     /note="alpha-ketoglutarate-dependent dioxygenase FTO; fat
                     mass and obesity-associated protein; AlkB homolog 9; fat
                     mass and obesity associated; m6A(m)-demethylase FTO; tRNA
                     N1-methyl adenine demethylase FTO; mRNA
                     N(6)-methyladenosine demethylase FTO; mRNA
                     (2'-O-methyladenosine-N(6)-)-demethylase FTO; U6 small
                     nuclear RNA N(6)-methyladenosine-demethylase FTO; U6 small
                     nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO;
                     intragenic FTO exon 9 containing transcript; mRNA
                     N(6)-methyladenine demethylase"
                     /calculated_mol_wt=38312
     Region          <11..154
                     /region_name="FTO_NTD"
                     /note="FTO catalytic domain; pfam12933"
                     /db_xref="CDD:463755"
     Region          158..327
                     /region_name="FTO_CTD"
                     /note="FTO C-terminal domain; pfam12934"
                     /db_xref="CDD:432887"
     CDS             1..334
                     /gene="FTO"
                     /gene_synonym="ALKBH9; BMIQ14; GDFD; IFEX9"
                     /coded_by="NM_001363905.2:722..1726"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:79068"
                     /db_xref="HGNC:HGNC:24678"
                     /db_xref="MIM:610966"
ORIGIN      
        1 msadfprvgm gssyngqdev diksraaynv tllnfmdpqk mpylkeepyf gmgkmavswh
       61 hdenlvdrsa vavysysceg peeeseddsh legrdpdiwh vgfkiswdie tpglaiplhq
      121 gdcyfmlddl nathqhcvla gsqprfssth rvaecstgtl dyilqrcqla lqnvcddvdn
      181 ddvslksfep avlkqgeeih nevefewlrq fwfqgnryrk ctdwwcqpma qlealwkkme
      241 gvtnavlhev kreglpveqr neiltailas ltarqnlrre wharcqsria rtlpadqkpe
      301 crpywekdda smplpfdltd ivselrgqll eakp
//
LOCUS       NP_001350917             482 aa            linear   PRI 21-DEC-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase FTO isoform 12 [Homo
            sapiens].
ACCESSION   NP_001350917
VERSION     NP_001350917.1
DBSOURCE    REFSEQ: accession NM_001363988.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Li,B., Wang,L., Du,M. and He,H.
  TITLE     FTO in oral diseases: Functions, mechanisms, and therapeutic
            potential
  JOURNAL   FASEB J 38 (20), e70115 (2024)
   PUBMED   39436191
  REMARK    GeneRIF: FTO in oral diseases: Functions, mechanisms, and
            therapeutic potential.
            Review article
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Li,Q. and Mu,S.
  TITLE     FTO mediates the diabetic kidney disease progression through
            regulating the m6A modification of NLRP3
  JOURNAL   BMC Nephrol 25 (1), 345 (2024)
   PUBMED   39390397
  REMARK    GeneRIF: FTO mediates the diabetic kidney disease progression
            through regulating the m[6]A modification of NLRP3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Shan,L., Tao,M., Zhang,W., Zhao,J.D., Liu,X.C., Fang,Z.H. and
            Gao,J.R.
  TITLE     Comprehensive analysis of the m6A demethylase FTO in endothelial
            dysfunction by MeRIP sequencing
  JOURNAL   Exp Cell Res 442 (2), 114268 (2024)
   PUBMED   39343042
  REMARK    GeneRIF: Comprehensive analysis of the m[6]A demethylase FTO in
            endothelial dysfunction by MeRIP sequencing.
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Nabeel-Shah,S., Pu,S., Burke,G.L., Ahmed,N., Braunschweig,U.,
            Farhangmehr,S., Lee,H., Wu,M., Ni,Z., Tang,H., Zhong,G., Marcon,E.,
            Zhang,Z., Blencowe,B.J. and Greenblatt,J.F.
  TITLE     Recruitment of the m6A/m6Am demethylase FTO to target RNAs by the
            telomeric zinc finger protein ZBTB48
  JOURNAL   Genome Biol 25 (1), 246 (2024)
   PUBMED   39300486
  REMARK    GeneRIF: Recruitment of the m[6]A/m6Am demethylase FTO to target
            RNAs by the telomeric zinc finger protein ZBTB48.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Hussain,M., Waheed,A., Elahi,A. and Mustafa,G.
  TITLE     Fat Mass and Obesity-Related (FTO) Gene Variant Is a Predictor of
            CVD in T2DM Patients
  JOURNAL   J Diabetes Res 2024, 5914316 (2024)
   PUBMED   39257882
  REMARK    GeneRIF: Fat Mass and Obesity-Related (FTO) Gene Variant Is a
            Predictor of CVD in T2DM Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Zeggini,E., Weedon,M.N., Lindgren,C.M., Frayling,T.M.,
            Elliott,K.S., Lango,H., Timpson,N.J., Perry,J.R., Rayner,N.W.,
            Freathy,R.M., Barrett,J.C., Shields,B., Morris,A.P., Ellard,S.,
            Groves,C.J., Harries,L.W., Marchini,J.L., Owen,K.R., Knight,B.,
            Cardon,L.R., Walker,M., Hitman,G.A., Morris,A.D., Doney,A.S.,
            McCarthy,M.I. and Hattersley,A.T.
  CONSRTM   Wellcome Trust Case Control Consortium (WTCCC)
  TITLE     Replication of genome-wide association signals in UK samples
            reveals risk loci for type 2 diabetes
  JOURNAL   Science 316 (5829), 1336-1341 (2007)
   PUBMED   17463249
  REMARK    Erratum:[Science. 2007 Aug 24;317(5841):1035-6]
REFERENCE   7  (residues 1 to 482)
  AUTHORS   Scott,L.J., Mohlke,K.L., Bonnycastle,L.L., Willer,C.J., Li,Y.,
            Duren,W.L., Erdos,M.R., Stringham,H.M., Chines,P.S., Jackson,A.U.,
            Prokunina-Olsson,L., Ding,C.J., Swift,A.J., Narisu,N., Hu,T.,
            Pruim,R., Xiao,R., Li,X.Y., Conneely,K.N., Riebow,N.L., Sprau,A.G.,
            Tong,M., White,P.P., Hetrick,K.N., Barnhart,M.W., Bark,C.W.,
            Goldstein,J.L., Watkins,L., Xiang,F., Saramies,J., Buchanan,T.A.,
            Watanabe,R.M., Valle,T.T., Kinnunen,L., Abecasis,G.R., Pugh,E.W.,
            Doheny,K.F., Bergman,R.N., Tuomilehto,J., Collins,F.S. and
            Boehnke,M.
  TITLE     A genome-wide association study of type 2 diabetes in Finns detects
            multiple susceptibility variants
  JOURNAL   Science 316 (5829), 1341-1345 (2007)
   PUBMED   17463248
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 482)
  AUTHORS   Dina,C., Meyre,D., Gallina,S., Durand,E., Korner,A., Jacobson,P.,
            Carlsson,L.M., Kiess,W., Vatin,V., Lecoeur,C., Delplanque,J.,
            Vaillant,E., Pattou,F., Ruiz,J., Weill,J., Levy-Marchal,C.,
            Horber,F., Potoczna,N., Hercberg,S., Le Stunff,C., Bougneres,P.,
            Kovacs,P., Marre,M., Balkau,B., Cauchi,S., Chevre,J.C. and
            Froguel,P.
  TITLE     Variation in FTO contributes to childhood obesity and severe adult
            obesity
  JOURNAL   Nat Genet 39 (6), 724-726 (2007)
   PUBMED   17496892
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            GeneRIF: Association with obesity in adult and childre.
            Interestingly, this association receives clear confirmation under a
            Transmission Disequilibrium Test design which is robust to
            population stratification.
REFERENCE   9  (residues 1 to 482)
  AUTHORS   Frayling,T.M., Timpson,N.J., Weedon,M.N., Zeggini,E., Freathy,R.M.,
            Lindgren,C.M., Perry,J.R., Elliott,K.S., Lango,H., Rayner,N.W.,
            Shields,B., Harries,L.W., Barrett,J.C., Ellard,S., Groves,C.J.,
            Knight,B., Patch,A.M., Ness,A.R., Ebrahim,S., Lawlor,D.A.,
            Ring,S.M., Ben-Shlomo,Y., Jarvelin,M.R., Sovio,U., Bennett,A.J.,
            Melzer,D., Ferrucci,L., Loos,R.J., Barroso,I., Wareham,N.J.,
            Karpe,F., Owen,K.R., Cardon,L.R., Walker,M., Hitman,G.A.,
            Palmer,C.N., Doney,A.S., Morris,A.D., Smith,G.D., Hattersley,A.T.
            and McCarthy,M.I.
  TITLE     A common variant in the FTO gene is associated with body mass index
            and predisposes to childhood and adult obesity
  JOURNAL   Science 316 (5826), 889-894 (2007)
   PUBMED   17434869
  REMARK    GeneRIF: A genome-wide search for type 2 diabetes-susceptibility
            genes identified a common variant in the FTO gene that predisposes
            to diabetes through an effect on body mass index
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-environment interaction. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 482)
  AUTHORS   Peters,T., Ausmeier,K. and Ruther,U.
  TITLE     Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft)
            mouse mutation
  JOURNAL   Mamm Genome 10 (10), 983-986 (1999)
   PUBMED   10501967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007909.8, AC007496.6 and
            AC007347.3.
            
            Summary: This gene is a nuclear protein of the AlkB related
            non-haem iron and 2-oxoglutarate-dependent oxygenase superfamily
            but the exact physiological function of this gene is not known.
            Other non-heme iron enzymes function to reverse alkylated DNA and
            RNA damage by oxidative demethylation. Studies in mice and humans
            indicate a role in nervous and cardiovascular systems and a strong
            association with body mass index, obesity risk, and type 2
            diabetes. [provided by RefSeq, Jul 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2090897.1,
                                           SRR14038197.2556458.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2145774,
                                           SAMEA2146982 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..482
                     /product="alpha-ketoglutarate-dependent dioxygenase FTO
                     isoform 12"
                     /EC_number="1.14.11.53"
                     /note="alpha-ketoglutarate-dependent dioxygenase FTO; fat
                     mass and obesity-associated protein; AlkB homolog 9; fat
                     mass and obesity associated; m6A(m)-demethylase FTO; tRNA
                     N1-methyl adenine demethylase FTO; mRNA
                     N(6)-methyladenosine demethylase FTO; mRNA
                     (2'-O-methyladenosine-N(6)-)-demethylase FTO; U6 small
                     nuclear RNA N(6)-methyladenosine-demethylase FTO; U6 small
                     nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO;
                     intragenic FTO exon 9 containing transcript; mRNA
                     N(6)-methyladenine demethylase"
                     /calculated_mol_wt=55397
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          32..327
                     /region_name="Fe2OG dioxygenase domain.
                     /evidence=ECO:0000269|PubMed:20376003"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          36..325
                     /region_name="FTO_NTD"
                     /note="FTO catalytic domain; pfam12933"
                     /db_xref="CDD:463755"
     Region          213..224
                     /region_name="Loop L1, predicted to block binding of
                     double-stranded DNA or RNA.
                     /evidence=ECO:0000269|PubMed:20376003"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Site            216
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          329..>457
                     /region_name="FTO_CTD"
                     /note="FTO C-terminal domain; pfam12934"
                     /db_xref="CDD:432887"
     CDS             1..482
                     /gene="FTO"
                     /gene_synonym="ALKBH9; BMIQ14; GDFD; IFEX9"
                     /coded_by="NM_001363988.2:30..1478"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="GeneID:79068"
                     /db_xref="HGNC:HGNC:24678"
                     /db_xref="MIM:610966"
ORIGIN      
        1 mkrtptaeer ereakklrll eeledtwlpy ltpkddefyq qwqlkypkli lreassvsee
       61 lhkevqeafl tlhkhgclfr dlvriqgkdl ltpvsrilig npgctykyln trlftvpwpv
      121 kgsnikhtea eiaaacetfl klndylqiet iqaleelaak ekanedavpl cmsadfprvg
      181 mgssyngqde vdiksraayn vtllnfmdpq kmpylkeepy fgmgkmavsw hhdenlvdrs
      241 avavysysce gpeeesedds hlegrdpdiw hvgfkiswdi etpglaiplh qgdcyfmldd
      301 lnathqhcvl agsqprfsst hrvaecstgt ldyilqrcql alqnvcddvd nddvslksfe
      361 pavlkqgeei hnevefewlr qfwfqgnryr kctdwwcqpm aqlealwkkm egvtnavlhe
      421 vkreglpveq rneiltaila sltarqnlrr ewharwsfil vaqagvqwhn lgslqppppg
      481 fk
//
LOCUS       NP_001425057             481 aa            linear   PRI 21-DEC-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase FTO isoform 14 [Homo
            sapiens].
ACCESSION   NP_001425057 XP_047290563 XP_054169860
VERSION     NP_001425057.1
DBSOURCE    REFSEQ: accession NM_001438128.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Li,B., Wang,L., Du,M. and He,H.
  TITLE     FTO in oral diseases: Functions, mechanisms, and therapeutic
            potential
  JOURNAL   FASEB J 38 (20), e70115 (2024)
   PUBMED   39436191
  REMARK    GeneRIF: FTO in oral diseases: Functions, mechanisms, and
            therapeutic potential.
            Review article
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Li,Q. and Mu,S.
  TITLE     FTO mediates the diabetic kidney disease progression through
            regulating the m6A modification of NLRP3
  JOURNAL   BMC Nephrol 25 (1), 345 (2024)
   PUBMED   39390397
  REMARK    GeneRIF: FTO mediates the diabetic kidney disease progression
            through regulating the m[6]A modification of NLRP3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Shan,L., Tao,M., Zhang,W., Zhao,J.D., Liu,X.C., Fang,Z.H. and
            Gao,J.R.
  TITLE     Comprehensive analysis of the m6A demethylase FTO in endothelial
            dysfunction by MeRIP sequencing
  JOURNAL   Exp Cell Res 442 (2), 114268 (2024)
   PUBMED   39343042
  REMARK    GeneRIF: Comprehensive analysis of the m[6]A demethylase FTO in
            endothelial dysfunction by MeRIP sequencing.
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Nabeel-Shah,S., Pu,S., Burke,G.L., Ahmed,N., Braunschweig,U.,
            Farhangmehr,S., Lee,H., Wu,M., Ni,Z., Tang,H., Zhong,G., Marcon,E.,
            Zhang,Z., Blencowe,B.J. and Greenblatt,J.F.
  TITLE     Recruitment of the m6A/m6Am demethylase FTO to target RNAs by the
            telomeric zinc finger protein ZBTB48
  JOURNAL   Genome Biol 25 (1), 246 (2024)
   PUBMED   39300486
  REMARK    GeneRIF: Recruitment of the m[6]A/m6Am demethylase FTO to target
            RNAs by the telomeric zinc finger protein ZBTB48.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Hussain,M., Waheed,A., Elahi,A. and Mustafa,G.
  TITLE     Fat Mass and Obesity-Related (FTO) Gene Variant Is a Predictor of
            CVD in T2DM Patients
  JOURNAL   J Diabetes Res 2024, 5914316 (2024)
   PUBMED   39257882
  REMARK    GeneRIF: Fat Mass and Obesity-Related (FTO) Gene Variant Is a
            Predictor of CVD in T2DM Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Zeggini,E., Weedon,M.N., Lindgren,C.M., Frayling,T.M.,
            Elliott,K.S., Lango,H., Timpson,N.J., Perry,J.R., Rayner,N.W.,
            Freathy,R.M., Barrett,J.C., Shields,B., Morris,A.P., Ellard,S.,
            Groves,C.J., Harries,L.W., Marchini,J.L., Owen,K.R., Knight,B.,
            Cardon,L.R., Walker,M., Hitman,G.A., Morris,A.D., Doney,A.S.,
            McCarthy,M.I. and Hattersley,A.T.
  CONSRTM   Wellcome Trust Case Control Consortium (WTCCC)
  TITLE     Replication of genome-wide association signals in UK samples
            reveals risk loci for type 2 diabetes
  JOURNAL   Science 316 (5829), 1336-1341 (2007)
   PUBMED   17463249
  REMARK    Erratum:[Science. 2007 Aug 24;317(5841):1035-6]
REFERENCE   7  (residues 1 to 481)
  AUTHORS   Scott,L.J., Mohlke,K.L., Bonnycastle,L.L., Willer,C.J., Li,Y.,
            Duren,W.L., Erdos,M.R., Stringham,H.M., Chines,P.S., Jackson,A.U.,
            Prokunina-Olsson,L., Ding,C.J., Swift,A.J., Narisu,N., Hu,T.,
            Pruim,R., Xiao,R., Li,X.Y., Conneely,K.N., Riebow,N.L., Sprau,A.G.,
            Tong,M., White,P.P., Hetrick,K.N., Barnhart,M.W., Bark,C.W.,
            Goldstein,J.L., Watkins,L., Xiang,F., Saramies,J., Buchanan,T.A.,
            Watanabe,R.M., Valle,T.T., Kinnunen,L., Abecasis,G.R., Pugh,E.W.,
            Doheny,K.F., Bergman,R.N., Tuomilehto,J., Collins,F.S. and
            Boehnke,M.
  TITLE     A genome-wide association study of type 2 diabetes in Finns detects
            multiple susceptibility variants
  JOURNAL   Science 316 (5829), 1341-1345 (2007)
   PUBMED   17463248
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 481)
  AUTHORS   Dina,C., Meyre,D., Gallina,S., Durand,E., Korner,A., Jacobson,P.,
            Carlsson,L.M., Kiess,W., Vatin,V., Lecoeur,C., Delplanque,J.,
            Vaillant,E., Pattou,F., Ruiz,J., Weill,J., Levy-Marchal,C.,
            Horber,F., Potoczna,N., Hercberg,S., Le Stunff,C., Bougneres,P.,
            Kovacs,P., Marre,M., Balkau,B., Cauchi,S., Chevre,J.C. and
            Froguel,P.
  TITLE     Variation in FTO contributes to childhood obesity and severe adult
            obesity
  JOURNAL   Nat Genet 39 (6), 724-726 (2007)
   PUBMED   17496892
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            GeneRIF: Association with obesity in adult and childre.
            Interestingly, this association receives clear confirmation under a
            Transmission Disequilibrium Test design which is robust to
            population stratification.
REFERENCE   9  (residues 1 to 481)
  AUTHORS   Frayling,T.M., Timpson,N.J., Weedon,M.N., Zeggini,E., Freathy,R.M.,
            Lindgren,C.M., Perry,J.R., Elliott,K.S., Lango,H., Rayner,N.W.,
            Shields,B., Harries,L.W., Barrett,J.C., Ellard,S., Groves,C.J.,
            Knight,B., Patch,A.M., Ness,A.R., Ebrahim,S., Lawlor,D.A.,
            Ring,S.M., Ben-Shlomo,Y., Jarvelin,M.R., Sovio,U., Bennett,A.J.,
            Melzer,D., Ferrucci,L., Loos,R.J., Barroso,I., Wareham,N.J.,
            Karpe,F., Owen,K.R., Cardon,L.R., Walker,M., Hitman,G.A.,
            Palmer,C.N., Doney,A.S., Morris,A.D., Smith,G.D., Hattersley,A.T.
            and McCarthy,M.I.
  TITLE     A common variant in the FTO gene is associated with body mass index
            and predisposes to childhood and adult obesity
  JOURNAL   Science 316 (5826), 889-894 (2007)
   PUBMED   17434869
  REMARK    GeneRIF: A genome-wide search for type 2 diabetes-susceptibility
            genes identified a common variant in the FTO gene that predisposes
            to diabetes through an effect on body mass index
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-environment interaction. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 481)
  AUTHORS   Peters,T., Ausmeier,K. and Ruther,U.
  TITLE     Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft)
            mouse mutation
  JOURNAL   Mamm Genome 10 (10), 983-986 (1999)
   PUBMED   10501967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007909.8, AC007496.6 and
            AC007347.3.
            
            On or before Apr 15, 2025 this sequence version replaced
            XP_047290563.1, XP_054169860.1.
            
            Summary: This gene is a nuclear protein of the AlkB related
            non-haem iron and 2-oxoglutarate-dependent oxygenase superfamily
            but the exact physiological function of this gene is not known.
            Other non-heme iron enzymes function to reverse alkylated DNA and
            RNA damage by oxidative demethylation. Studies in mice and humans
            indicate a role in nervous and cardiovascular systems and a strong
            association with body mass index, obesity risk, and type 2
            diabetes. [provided by RefSeq, Jul 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3089501.1,
                                           SRR14038191.2129679.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..481
                     /product="alpha-ketoglutarate-dependent dioxygenase FTO
                     isoform 14"
                     /EC_number="1.14.11.53"
                     /note="alpha-ketoglutarate-dependent dioxygenase FTO; fat
                     mass and obesity-associated protein; AlkB homolog 9; fat
                     mass and obesity associated; m6A(m)-demethylase FTO; tRNA
                     N1-methyl adenine demethylase FTO; mRNA
                     N(6)-methyladenosine demethylase FTO; mRNA
                     (2'-O-methyladenosine-N(6)-)-demethylase FTO; U6 small
                     nuclear RNA N(6)-methyladenosine-demethylase FTO; U6 small
                     nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO;
                     intragenic FTO exon 9 containing transcript; mRNA
                     N(6)-methyladenine demethylase"
                     /calculated_mol_wt=55484
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          32..327
                     /region_name="Fe2OG dioxygenase domain.
                     /evidence=ECO:0000269|PubMed:20376003"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          36..325
                     /region_name="FTO_NTD"
                     /note="FTO catalytic domain; pfam12933"
                     /db_xref="CDD:463755"
     Region          213..224
                     /region_name="Loop L1, predicted to block binding of
                     double-stranded DNA or RNA.
                     /evidence=ECO:0000269|PubMed:20376003"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Site            216
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          329..>455
                     /region_name="FTO_CTD"
                     /note="FTO C-terminal domain; pfam12934"
                     /db_xref="CDD:432887"
     CDS             1..481
                     /gene="FTO"
                     /gene_synonym="ALKBH9; BMIQ14; GDFD; IFEX9"
                     /coded_by="NM_001438128.1:30..1475"
                     /note="isoform 14 is encoded by transcript variant 15"
                     /db_xref="GeneID:79068"
                     /db_xref="HGNC:HGNC:24678"
                     /db_xref="MIM:610966"
ORIGIN      
        1 mkrtptaeer ereakklrll eeledtwlpy ltpkddefyq qwqlkypkli lreassvsee
       61 lhkevqeafl tlhkhgclfr dlvriqgkdl ltpvsrilig npgctykyln trlftvpwpv
      121 kgsnikhtea eiaaacetfl klndylqiet iqaleelaak ekanedavpl cmsadfprvg
      181 mgssyngqde vdiksraayn vtllnfmdpq kmpylkeepy fgmgkmavsw hhdenlvdrs
      241 avavysysce gpeeesedds hlegrdpdiw hvgfkiswdi etpglaiplh qgdcyfmldd
      301 lnathqhcvl agsqprfsst hrvaecstgt ldyilqrcql alqnvcddvd nddvslksfe
      361 pavlkqgeei hnevefewlr qfwfqgnryr kctdwwcqpm aqlealwkkm egvtnavlhe
      421 vkreglpveq rneiltaila sltarqnlrr ewharvdieg wkkeakilcf lqeaieikke
      481 t
//
LOCUS       NP_001401177            1545 aa            linear   PRI 21-DEC-2025
DEFINITION  low-density lipoprotein receptor-related protein 6 isoform e
            precursor [Homo sapiens].
ACCESSION   NP_001401177
VERSION     NP_001401177.1
DBSOURCE    REFSEQ: accession NM_001414248.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1545)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1545)
  AUTHORS   Zhong,S., Guo,Q., Chen,X., Luo,X., Long,Y., Chong,T., Ye,M., He,H.,
            Lu,A., Ao,K., Yin,M., Xu,A., Li,X., Hao,Y. and Guo,X.
  TITLE     The inhibition of YTHDF3/m6A/LRP6 reprograms fatty acid metabolism
            and suppresses lymph node metastasis in cervical cancer
  JOURNAL   Int J Biol Sci 20 (3), 916-936 (2024)
   PUBMED   38250152
  REMARK    GeneRIF: The inhibition of YTHDF3/m[6]A/LRP6 reprograms fatty acid
            metabolism and suppresses lymph node metastasis in cervical cancer.
            Erratum:[Int J Biol Sci. 2025 Jun 5;21(8):3825-3826. doi:
            10.7150/ijbs.115928. PMID: 40520018]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1545)
  AUTHORS   Li,J., Liu,Z., Ren,Y., Shao,H. and Li,S.
  TITLE     LRP5-/6 gene polymorphisms and its association with risk of
            abnormal bone mass in postmenopausal women
  JOURNAL   J Orthop Surg Res 18 (1), 369 (2023)
   PUBMED   37202775
  REMARK    GeneRIF: LRP5-/6 gene polymorphisms and its association with risk
            of abnormal bone mass in postmenopausal women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1545)
  AUTHORS   Hao,H., Liu,Q., Chen,J. and Zhou,H.
  TITLE     Overexpression of circRNAs LRP6 in gestational diabetes mellitus
            predicts foetal malformation and intrauterine death
  JOURNAL   Endocrinol Diabetes Nutr (Engl Ed) 70 (2), 124-129 (2023)
   PUBMED   36925229
  REMARK    GeneRIF: Overexpression of circRNAs LRP6 in gestational diabetes
            mellitus predicts foetal malformation and intrauterine death.
REFERENCE   5  (residues 1 to 1545)
  AUTHORS   Wang,J., Yang,H., Ma,X., Liu,J., Li,L., Chen,L. and Wei,F.
  TITLE     LRP6/filamentous-actin signaling facilitates osteogenic commitment
            in mechanically induced periodontal ligament stem cells
  JOURNAL   Cell Mol Biol Lett 28 (1), 7 (2023)
   PUBMED   36694134
  REMARK    GeneRIF: LRP6/filamentous-actin signaling facilitates osteogenic
            commitment in mechanically induced periodontal ligament stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1545)
  AUTHORS   Bafico,A., Liu,G., Yaniv,A., Gazit,A. and Aaronson,S.A.
  TITLE     Novel mechanism of Wnt signalling inhibition mediated by Dickkopf-1
            interaction with LRP6/Arrow
  JOURNAL   Nat Cell Biol 3 (7), 683-686 (2001)
   PUBMED   11433302
REFERENCE   7  (residues 1 to 1545)
  AUTHORS   Mao,B., Wu,W., Li,Y., Hoppe,D., Stannek,P., Glinka,A. and Niehrs,C.
  TITLE     LDL-receptor-related protein 6 is a receptor for Dickkopf proteins
  JOURNAL   Nature 411 (6835), 321-325 (2001)
   PUBMED   11357136
REFERENCE   8  (residues 1 to 1545)
  AUTHORS   Tamai,K., Semenov,M., Kato,Y., Spokony,R., Liu,C., Katsuyama,Y.,
            Hess,F., Saint-Jeannet,J.P. and He,X.
  TITLE     LDL-receptor-related proteins in Wnt signal transduction
  JOURNAL   Nature 407 (6803), 530-535 (2000)
   PUBMED   11029007
REFERENCE   9  (residues 1 to 1545)
  AUTHORS   Baens,M., Wlodarska,I., Corveleyn,A., Hoornaert,I., Hagemeijer,A.
            and Marynen,P.
  TITLE     A physical, transcript, and deletion map of chromosome region
            12p12.3 flanked by ETV6 and CDKN1B: hypermethylation of the LRP6
            CpG island in two leukemia patients with hemizygous del(12p)
  JOURNAL   Genomics 56 (1), 40-50 (1999)
   PUBMED   10036184
REFERENCE   10 (residues 1 to 1545)
  AUTHORS   Brown,S.D., Twells,R.C., Hey,P.J., Cox,R.D., Levy,E.R.,
            Soderman,A.R., Metzker,M.L., Caskey,C.T., Todd,J.A. and Hess,J.F.
  TITLE     Isolation and characterization of LRP6, a novel member of the low
            density lipoprotein receptor gene family
  JOURNAL   Biochem Biophys Res Commun 248 (3), 879-888 (1998)
   PUBMED   9704021
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007621.34, AC007537.3 and
            KF455603.1.
            
            Summary: This gene encodes a member of the low density lipoprotein
            (LDL) receptor gene family. LDL receptors are transmembrane cell
            surface proteins involved in receptor-mediated endocytosis of
            lipoprotein and protein ligands. The protein encoded by this gene
            functions as a receptor or, with Frizzled, a co-receptor for Wnt
            and thereby transmits the canonical Wnt/beta-catenin signaling
            cascade. Through its interaction with the Wnt/beta-catenin
            signaling cascade this gene plays a role in the regulation of cell
            differentiation, proliferation, and migration and the development
            of many cancer types. This protein undergoes gamma-secretase
            dependent RIP- (regulated intramembrane proteolysis) processing but
            the precise locations of the cleavage sites have not been
            determined.[provided by RefSeq, Dec 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2825676.1,
                                           SRR14038193.2712859.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1545
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..1545
                     /product="low-density lipoprotein receptor-related protein
                     6 isoform e precursor"
                     /note="low-density lipoprotein receptor-related protein 6;
                     LRP-6"
                     /calculated_mol_wt=170953
     Region          1..204
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
                     /calculated_mol_wt=2024
     Region          20..275
                     /region_name="Beta-propeller 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            42
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            81
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          89..127
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          150..191
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          175..216
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          217..251
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          237..276
                     /region_name="LDL-receptor class B 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          286..323
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          328..589
                     /region_name="Beta-propeller 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          353..393
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          397..437
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          458..499
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          483..524
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            486
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          525..558
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          592..627
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          631..890
                     /region_name="Beta-propeller 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          <654..813
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Site            692
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          697..739
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          827..866
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            859
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            865
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          893..929
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            926
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          933..1202
                     /region_name="Beta-propeller 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          958..998
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          <968..1075
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Site            1039
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          1094..1136
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1207..1243
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1249..1285
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1254,1264,1275..1276)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1268,1271,1275,1281..1282)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1278..1282
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1288..1322
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1293,1301,1312..1313)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1305,1308,1312,1318..1319)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1315..1319
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1326..1360
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1331,1339,1350..1351)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1343,1346,1350,1356..1357)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1353..1357
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            1371..1393
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            1420
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:16513652; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1430
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:16513652; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1479
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17569865; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          1487..1493
                     /region_name="PPPSP motif A"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            1490
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK14, GRK5 and GRK6.
                     /evidence=ECO:0000269|PubMed:16341017,
                     ECO:0000269|PubMed:17698587, ECO:0000269|PubMed:18762581,
                     ECO:0000269|PubMed:19801552, ECO:0000269|PubMed:20059949,
                     ECO:0000269|PubMed:25331957, ECO:0000269|PubMed:27821587,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1493
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK1.
                     /evidence=ECO:0000269|PubMed:16341017; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     CDS             1..1545
                     /gene="LRP6"
                     /gene_synonym="ADCAD2; EVR8; OPTA4; STHAG7"
                     /coded_by="NM_001414248.1:310..4947"
                     /note="isoform e precursor is encoded by transcript
                     variant 6"
                     /db_xref="GeneID:4040"
                     /db_xref="HGNC:HGNC:6698"
                     /db_xref="MIM:603507"
ORIGIN      
        1 mgavlrslla csfcvllraa plllyanrrd lrlvdatngk enativvggl edaaavdfvf
       61 shgliywsdv seeaikrtef nktesvqnvv vsgllspdgl acdwlgekly wtdsetnrie
      121 vsnldgslrk vlfwqeldqp raialdpssg fmywtdwgev pkieragmdg ssrfiiinse
      181 iywpngltld yeeqklywad aklnfihksn ldgtnrqavv kgslphpfal tlfedilywt
      241 dwsthsilac nkytgeglre ihsdifspmd ihafsqqrqp natnpcgidn ggcshlclms
      301 pvkpfyqcac ptgvklleng ktckdgatel lllarrtdlr risldtpdft divlqledir
      361 haiaidydpv egyiywtdde vrairrsfid gsgsqfvvta qiahpdgiav dwvarnlywt
      421 dtgtdrievt rlngtmrkil isedleepra ivldpmvgym ywtdwgeipk ieraaldgsd
      481 rvvlvntslg wpnglaldyd egkiywgdak tdkievmntd gtgrrvlved kiphifgftl
      541 lgdyvywtdw qrrsiervhk rsaereviid qlpdlmglka tnvhrvigsn pcaeenggcs
      601 hlclyrpqgl rcacpigfel isdmktcivp eafllfsrra dirrisletn nnnvaipltg
      661 vkeasaldfd vtdnriywtd islktisraf mngsalehvv efgldypegm avdwlgknly
      721 wadtgtnrie vskldgqhrq vlvwkdldsp ralaldpaeg fmywtewggk pkidraamdg
      781 serttlvpnv grangltidy akrrlywtdl dtnliessnm lglnreviad dlphpfgltq
      841 yqdyiywtdw srrsierank tsgqnrtiiq ghldyvmdil vfhssrqsgw necassnghc
      901 shlclavpvg gfvcgcpahy slnadnrtcs apttfllfsq ksainrmvid eqqspdiilp
      961 ihslrnvrai dydpldkqly widsrqnmir kaqedgsqgf tvvvssvpsq nleiqpydls
     1021 idiysryiyw tceatnvinv trldgrsvgv vlkgeqdrpr avvvnpekgy myftnlqers
     1081 pkieraaldg terevlffsg lskpialald srlgklfwad sdlrriessd lsganrivle
     1141 dsnilqpvgl tvfenwlywi dkqqqmieki dmtgregrtk vqariaqlsd ihavkelnlq
     1201 eyrqhpcaqd nggcshiclv kgdgttrcsc pmhlvllqde lscgepptcs pqqftcftge
     1261 idcipvawrc dgftecedhs delncpvcse sqfqcasgqc idgalrcngd ancqdksdek
     1321 ncevlclidq frcangqcig khkkcdhnvd csdksdeldc ypteepapqa tntvgsvigv
     1381 ivtifvsgtv yficqrmlcp rmkgdgetmt ndyvvhgpas vplgyvphps slsgslpgms
     1441 rgksmissls imggssgppy drahvtgass ssssstkgty fpailnppps patershytm
     1501 efgyssnsps thrsyrlikc sskkgrqsrt rnlicdceqs gshff
//
LOCUS       NP_001401182            1462 aa            linear   PRI 21-DEC-2025
DEFINITION  low-density lipoprotein receptor-related protein 6 isoform i [Homo
            sapiens].
ACCESSION   NP_001401182
VERSION     NP_001401182.1
DBSOURCE    REFSEQ: accession NM_001414253.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1462)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1462)
  AUTHORS   Zhong,S., Guo,Q., Chen,X., Luo,X., Long,Y., Chong,T., Ye,M., He,H.,
            Lu,A., Ao,K., Yin,M., Xu,A., Li,X., Hao,Y. and Guo,X.
  TITLE     The inhibition of YTHDF3/m6A/LRP6 reprograms fatty acid metabolism
            and suppresses lymph node metastasis in cervical cancer
  JOURNAL   Int J Biol Sci 20 (3), 916-936 (2024)
   PUBMED   38250152
  REMARK    GeneRIF: The inhibition of YTHDF3/m[6]A/LRP6 reprograms fatty acid
            metabolism and suppresses lymph node metastasis in cervical cancer.
            Erratum:[Int J Biol Sci. 2025 Jun 5;21(8):3825-3826. doi:
            10.7150/ijbs.115928. PMID: 40520018]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1462)
  AUTHORS   Li,J., Liu,Z., Ren,Y., Shao,H. and Li,S.
  TITLE     LRP5-/6 gene polymorphisms and its association with risk of
            abnormal bone mass in postmenopausal women
  JOURNAL   J Orthop Surg Res 18 (1), 369 (2023)
   PUBMED   37202775
  REMARK    GeneRIF: LRP5-/6 gene polymorphisms and its association with risk
            of abnormal bone mass in postmenopausal women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1462)
  AUTHORS   Hao,H., Liu,Q., Chen,J. and Zhou,H.
  TITLE     Overexpression of circRNAs LRP6 in gestational diabetes mellitus
            predicts foetal malformation and intrauterine death
  JOURNAL   Endocrinol Diabetes Nutr (Engl Ed) 70 (2), 124-129 (2023)
   PUBMED   36925229
  REMARK    GeneRIF: Overexpression of circRNAs LRP6 in gestational diabetes
            mellitus predicts foetal malformation and intrauterine death.
REFERENCE   5  (residues 1 to 1462)
  AUTHORS   Wang,J., Yang,H., Ma,X., Liu,J., Li,L., Chen,L. and Wei,F.
  TITLE     LRP6/filamentous-actin signaling facilitates osteogenic commitment
            in mechanically induced periodontal ligament stem cells
  JOURNAL   Cell Mol Biol Lett 28 (1), 7 (2023)
   PUBMED   36694134
  REMARK    GeneRIF: LRP6/filamentous-actin signaling facilitates osteogenic
            commitment in mechanically induced periodontal ligament stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1462)
  AUTHORS   Bafico,A., Liu,G., Yaniv,A., Gazit,A. and Aaronson,S.A.
  TITLE     Novel mechanism of Wnt signalling inhibition mediated by Dickkopf-1
            interaction with LRP6/Arrow
  JOURNAL   Nat Cell Biol 3 (7), 683-686 (2001)
   PUBMED   11433302
REFERENCE   7  (residues 1 to 1462)
  AUTHORS   Mao,B., Wu,W., Li,Y., Hoppe,D., Stannek,P., Glinka,A. and Niehrs,C.
  TITLE     LDL-receptor-related protein 6 is a receptor for Dickkopf proteins
  JOURNAL   Nature 411 (6835), 321-325 (2001)
   PUBMED   11357136
REFERENCE   8  (residues 1 to 1462)
  AUTHORS   Tamai,K., Semenov,M., Kato,Y., Spokony,R., Liu,C., Katsuyama,Y.,
            Hess,F., Saint-Jeannet,J.P. and He,X.
  TITLE     LDL-receptor-related proteins in Wnt signal transduction
  JOURNAL   Nature 407 (6803), 530-535 (2000)
   PUBMED   11029007
REFERENCE   9  (residues 1 to 1462)
  AUTHORS   Baens,M., Wlodarska,I., Corveleyn,A., Hoornaert,I., Hagemeijer,A.
            and Marynen,P.
  TITLE     A physical, transcript, and deletion map of chromosome region
            12p12.3 flanked by ETV6 and CDKN1B: hypermethylation of the LRP6
            CpG island in two leukemia patients with hemizygous del(12p)
  JOURNAL   Genomics 56 (1), 40-50 (1999)
   PUBMED   10036184
REFERENCE   10 (residues 1 to 1462)
  AUTHORS   Brown,S.D., Twells,R.C., Hey,P.J., Cox,R.D., Levy,E.R.,
            Soderman,A.R., Metzker,M.L., Caskey,C.T., Todd,J.A. and Hess,J.F.
  TITLE     Isolation and characterization of LRP6, a novel member of the low
            density lipoprotein receptor gene family
  JOURNAL   Biochem Biophys Res Commun 248 (3), 879-888 (1998)
   PUBMED   9704021
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007621.34, AC007537.3 and
            KF455603.1.
            
            Summary: This gene encodes a member of the low density lipoprotein
            (LDL) receptor gene family. LDL receptors are transmembrane cell
            surface proteins involved in receptor-mediated endocytosis of
            lipoprotein and protein ligands. The protein encoded by this gene
            functions as a receptor or, with Frizzled, a co-receptor for Wnt
            and thereby transmits the canonical Wnt/beta-catenin signaling
            cascade. Through its interaction with the Wnt/beta-catenin
            signaling cascade this gene plays a role in the regulation of cell
            differentiation, proliferation, and migration and the development
            of many cancer types. This protein undergoes gamma-secretase
            dependent RIP- (regulated intramembrane proteolysis) processing but
            the precise locations of the cleavage sites have not been
            determined.[provided by RefSeq, Dec 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4425271.1,
                                           SRR18074967.2652367.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..1462
                     /product="low-density lipoprotein receptor-related protein
                     6 isoform i"
                     /note="low-density lipoprotein receptor-related protein 6;
                     LRP-6"
                     /calculated_mol_wt=163681
     Region          1..40
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          24..65
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          66..100
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          135..172
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          202..242
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          246..286
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          307..348
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          332..373
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          374..407
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          441..476
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          <503..662
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          546..588
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          676..715
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          742..778
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          807..847
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          <817..924
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          943..985
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1056..1092
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1098..1134
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1103,1113,1124..1125)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1117,1120,1124,1130..1131)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1127..1131
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1137..1171
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1142,1150,1161..1162)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1154,1157,1161,1167..1168)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1164..1168
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1175..1209
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1180,1188,1199..1200)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1192,1195,1199,1205..1206)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1202..1206
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     CDS             1..1462
                     /gene="LRP6"
                     /gene_synonym="ADCAD2; EVR8; OPTA4; STHAG7"
                     /coded_by="NM_001414253.1:680..5068"
                     /note="isoform i is encoded by transcript variant 11"
                     /db_xref="GeneID:4040"
                     /db_xref="HGNC:HGNC:6698"
                     /db_xref="MIM:603507"
ORIGIN      
        1 mywtdwgevp kieragmdgs srfiiinsei ywpngltldy eeqklywada klnfihksnl
       61 dgtnrqavvk gslphpfalt lfedilywtd wsthsilacn kytgeglrei hsdifspmdi
      121 hafsqqrqpn atnpcgidng gcshlclmsp vkpfyqcacp tgvkllengk tckdgatell
      181 llarrtdlrr isldtpdftd ivlqledirh aiaidydpve gyiywtddev rairrsfidg
      241 sgsqfvvtaq iahpdgiavd wvarnlywtd tgtdrievtr lngtmrkili sedleeprai
      301 vldpmvgymy wtdwgeipki eraaldgsdr vvlvntslgw pnglaldyde gkiywgdakt
      361 dkievmntdg tgrrvlvedk iphifgftll gdyvywtdwq rrsiervhkr saereviidq
      421 lpdlmglkat nvhrvigsnp caeenggcsh lclyrpqglr cacpigfeli sdmktcivpe
      481 afllfsrrad irrisletnn nnvaipltgv keasaldfdv tdnriywtdi slktisrafm
      541 ngsalehvve fgldypegma vdwlgknlyw adtgtnriev skldgqhrqv lvwkdldspr
      601 alaldpaegf mywtewggkp kidraamdgs erttlvpnvg rangltidya krrlywtdld
      661 tnliessnml glnreviadd lphpfgltqy qdyiywtdws rrsierankt sgqnrtiiqg
      721 hldyvmdilv fhssrqsgwn ecassnghcs hlclavpvgg fvcgcpahys lnadnrtcsa
      781 pttfllfsqk sainrmvide qqspdiilpi hslrnvraid ydpldkqlyw idsrqnmirk
      841 aqedgsqgft vvvssvpsqn leiqpydlsi diysryiywt ceatnvinvt rldgrsvgvv
      901 lkgeqdrpra vvvnpekgym yftnlqersp kieraaldgt erevlffsgl skpialalds
      961 rlgklfwads dlrriessdl sganrivled snilqpvglt vfenwlywid kqqqmiekid
     1021 mtgregrtkv qariaqlsdi havkelnlqe yrqhpcaqdn ggcshiclvk gdgttrcscp
     1081 mhlvllqdel scgepptcsp qqftcftgei dcipvawrcd gftecedhsd elncpvcses
     1141 qfqcasgqci dgalrcngda ncqdksdekn cevlclidqf rcangqcigk hkkcdhnvdc
     1201 sdksdeldcy pteepapqat ntvgsvigvi vtifvsgtvy ficqrmlcpr mkgdgetmtn
     1261 dyvvhgpasv plgyvphpss lsgslpgmsr gksmisslsi mggssgppyd rahvtgasss
     1321 sssstkgtyf pailnpppsp atershytme fgyssnspst hrsysyrpys yrhfappttp
     1381 cstdvcdsdy apsrrmtsva takgytsdln ydsepvpppp tprsqylsae enyescppsp
     1441 ytersyshhl yppppspctd ss
//
LOCUS       NP_001350826             479 aa            linear   PRI 21-DEC-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase FTO isoform 5 [Homo
            sapiens].
ACCESSION   NP_001350826
VERSION     NP_001350826.1
DBSOURCE    REFSEQ: accession NM_001363897.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Li,B., Wang,L., Du,M. and He,H.
  TITLE     FTO in oral diseases: Functions, mechanisms, and therapeutic
            potential
  JOURNAL   FASEB J 38 (20), e70115 (2024)
   PUBMED   39436191
  REMARK    GeneRIF: FTO in oral diseases: Functions, mechanisms, and
            therapeutic potential.
            Review article
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Li,Q. and Mu,S.
  TITLE     FTO mediates the diabetic kidney disease progression through
            regulating the m6A modification of NLRP3
  JOURNAL   BMC Nephrol 25 (1), 345 (2024)
   PUBMED   39390397
  REMARK    GeneRIF: FTO mediates the diabetic kidney disease progression
            through regulating the m[6]A modification of NLRP3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Shan,L., Tao,M., Zhang,W., Zhao,J.D., Liu,X.C., Fang,Z.H. and
            Gao,J.R.
  TITLE     Comprehensive analysis of the m6A demethylase FTO in endothelial
            dysfunction by MeRIP sequencing
  JOURNAL   Exp Cell Res 442 (2), 114268 (2024)
   PUBMED   39343042
  REMARK    GeneRIF: Comprehensive analysis of the m[6]A demethylase FTO in
            endothelial dysfunction by MeRIP sequencing.
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Nabeel-Shah,S., Pu,S., Burke,G.L., Ahmed,N., Braunschweig,U.,
            Farhangmehr,S., Lee,H., Wu,M., Ni,Z., Tang,H., Zhong,G., Marcon,E.,
            Zhang,Z., Blencowe,B.J. and Greenblatt,J.F.
  TITLE     Recruitment of the m6A/m6Am demethylase FTO to target RNAs by the
            telomeric zinc finger protein ZBTB48
  JOURNAL   Genome Biol 25 (1), 246 (2024)
   PUBMED   39300486
  REMARK    GeneRIF: Recruitment of the m[6]A/m6Am demethylase FTO to target
            RNAs by the telomeric zinc finger protein ZBTB48.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Hussain,M., Waheed,A., Elahi,A. and Mustafa,G.
  TITLE     Fat Mass and Obesity-Related (FTO) Gene Variant Is a Predictor of
            CVD in T2DM Patients
  JOURNAL   J Diabetes Res 2024, 5914316 (2024)
   PUBMED   39257882
  REMARK    GeneRIF: Fat Mass and Obesity-Related (FTO) Gene Variant Is a
            Predictor of CVD in T2DM Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Zeggini,E., Weedon,M.N., Lindgren,C.M., Frayling,T.M.,
            Elliott,K.S., Lango,H., Timpson,N.J., Perry,J.R., Rayner,N.W.,
            Freathy,R.M., Barrett,J.C., Shields,B., Morris,A.P., Ellard,S.,
            Groves,C.J., Harries,L.W., Marchini,J.L., Owen,K.R., Knight,B.,
            Cardon,L.R., Walker,M., Hitman,G.A., Morris,A.D., Doney,A.S.,
            McCarthy,M.I. and Hattersley,A.T.
  CONSRTM   Wellcome Trust Case Control Consortium (WTCCC)
  TITLE     Replication of genome-wide association signals in UK samples
            reveals risk loci for type 2 diabetes
  JOURNAL   Science 316 (5829), 1336-1341 (2007)
   PUBMED   17463249
  REMARK    Erratum:[Science. 2007 Aug 24;317(5841):1035-6]
REFERENCE   7  (residues 1 to 479)
  AUTHORS   Scott,L.J., Mohlke,K.L., Bonnycastle,L.L., Willer,C.J., Li,Y.,
            Duren,W.L., Erdos,M.R., Stringham,H.M., Chines,P.S., Jackson,A.U.,
            Prokunina-Olsson,L., Ding,C.J., Swift,A.J., Narisu,N., Hu,T.,
            Pruim,R., Xiao,R., Li,X.Y., Conneely,K.N., Riebow,N.L., Sprau,A.G.,
            Tong,M., White,P.P., Hetrick,K.N., Barnhart,M.W., Bark,C.W.,
            Goldstein,J.L., Watkins,L., Xiang,F., Saramies,J., Buchanan,T.A.,
            Watanabe,R.M., Valle,T.T., Kinnunen,L., Abecasis,G.R., Pugh,E.W.,
            Doheny,K.F., Bergman,R.N., Tuomilehto,J., Collins,F.S. and
            Boehnke,M.
  TITLE     A genome-wide association study of type 2 diabetes in Finns detects
            multiple susceptibility variants
  JOURNAL   Science 316 (5829), 1341-1345 (2007)
   PUBMED   17463248
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 479)
  AUTHORS   Dina,C., Meyre,D., Gallina,S., Durand,E., Korner,A., Jacobson,P.,
            Carlsson,L.M., Kiess,W., Vatin,V., Lecoeur,C., Delplanque,J.,
            Vaillant,E., Pattou,F., Ruiz,J., Weill,J., Levy-Marchal,C.,
            Horber,F., Potoczna,N., Hercberg,S., Le Stunff,C., Bougneres,P.,
            Kovacs,P., Marre,M., Balkau,B., Cauchi,S., Chevre,J.C. and
            Froguel,P.
  TITLE     Variation in FTO contributes to childhood obesity and severe adult
            obesity
  JOURNAL   Nat Genet 39 (6), 724-726 (2007)
   PUBMED   17496892
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            GeneRIF: Association with obesity in adult and childre.
            Interestingly, this association receives clear confirmation under a
            Transmission Disequilibrium Test design which is robust to
            population stratification.
REFERENCE   9  (residues 1 to 479)
  AUTHORS   Frayling,T.M., Timpson,N.J., Weedon,M.N., Zeggini,E., Freathy,R.M.,
            Lindgren,C.M., Perry,J.R., Elliott,K.S., Lango,H., Rayner,N.W.,
            Shields,B., Harries,L.W., Barrett,J.C., Ellard,S., Groves,C.J.,
            Knight,B., Patch,A.M., Ness,A.R., Ebrahim,S., Lawlor,D.A.,
            Ring,S.M., Ben-Shlomo,Y., Jarvelin,M.R., Sovio,U., Bennett,A.J.,
            Melzer,D., Ferrucci,L., Loos,R.J., Barroso,I., Wareham,N.J.,
            Karpe,F., Owen,K.R., Cardon,L.R., Walker,M., Hitman,G.A.,
            Palmer,C.N., Doney,A.S., Morris,A.D., Smith,G.D., Hattersley,A.T.
            and McCarthy,M.I.
  TITLE     A common variant in the FTO gene is associated with body mass index
            and predisposes to childhood and adult obesity
  JOURNAL   Science 316 (5826), 889-894 (2007)
   PUBMED   17434869
  REMARK    GeneRIF: A genome-wide search for type 2 diabetes-susceptibility
            genes identified a common variant in the FTO gene that predisposes
            to diabetes through an effect on body mass index
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-environment interaction. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 479)
  AUTHORS   Peters,T., Ausmeier,K. and Ruther,U.
  TITLE     Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft)
            mouse mutation
  JOURNAL   Mamm Genome 10 (10), 983-986 (1999)
   PUBMED   10501967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007909.8, AC007496.6 and
            AC007347.3.
            
            Summary: This gene is a nuclear protein of the AlkB related
            non-haem iron and 2-oxoglutarate-dependent oxygenase superfamily
            but the exact physiological function of this gene is not known.
            Other non-heme iron enzymes function to reverse alkylated DNA and
            RNA damage by oxidative demethylation. Studies in mice and humans
            indicate a role in nervous and cardiovascular systems and a strong
            association with body mass index, obesity risk, and type 2
            diabetes. [provided by RefSeq, Jul 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3398660.1,
                                           SRR14038195.1591153.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153347, SAMEA2156670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..479
                     /product="alpha-ketoglutarate-dependent dioxygenase FTO
                     isoform 5"
                     /EC_number="1.14.11.53"
                     /note="alpha-ketoglutarate-dependent dioxygenase FTO; fat
                     mass and obesity-associated protein; AlkB homolog 9; fat
                     mass and obesity associated; m6A(m)-demethylase FTO; tRNA
                     N1-methyl adenine demethylase FTO; mRNA
                     N(6)-methyladenosine demethylase FTO; mRNA
                     (2'-O-methyladenosine-N(6)-)-demethylase FTO; U6 small
                     nuclear RNA N(6)-methyladenosine-demethylase FTO; U6 small
                     nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO;
                     intragenic FTO exon 9 containing transcript; mRNA
                     N(6)-methyladenine demethylase"
                     /calculated_mol_wt=54885
     Region          10..299
                     /region_name="FTO_NTD"
                     /note="FTO catalytic domain; pfam12933"
                     /db_xref="CDD:463755"
     Region          303..472
                     /region_name="FTO_CTD"
                     /note="FTO C-terminal domain; pfam12934"
                     /db_xref="CDD:432887"
     CDS             1..479
                     /gene="FTO"
                     /gene_synonym="ALKBH9; BMIQ14; GDFD; IFEX9"
                     /coded_by="NM_001363897.2:30..1469"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:79068"
                     /db_xref="HGNC:HGNC:24678"
                     /db_xref="MIM:610966"
ORIGIN      
        1 mkrtptaeer ereakwqlky pklilreass vseelhkevq eafltlhkhg clfrdlvriq
       61 gkdlltpvsr ilignpgcty kylntrlftv pwpvkgsnik hteaeiaaac etflklndyl
      121 qietiqalee laakekaned avplcmsadf prvgmgssyn gqdevdiksr aaynvtllnf
      181 mdpqkmpylk eepyfgmgkm avswhhdenl vdrsavavys yscegpeees eddshlegrd
      241 pdiwhvgfki swdietpgla iplhqgdcyf mlddlnathq hcvlagsqpr fssthrvaec
      301 stgtldyilq rcqlalqnvc ddvdnddvsl ksfepavlkq geeihnevef ewlrqfwfqg
      361 nryrkctdww cqpmaqleal wkkmegvtna vlhevkregl pveqrneilt ailasltarq
      421 nlrrewharc qsriartlpa dqkpecrpyw ekddasmplp fdltdivsel rgqlleakp
//
LOCUS       NP_001401174            1613 aa            linear   PRI 21-DEC-2025
DEFINITION  low-density lipoprotein receptor-related protein 6 isoform b
            precursor [Homo sapiens].
ACCESSION   NP_001401174 XP_006719141
VERSION     NP_001401174.1
DBSOURCE    REFSEQ: accession NM_001414245.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1613)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1613)
  AUTHORS   Zhong,S., Guo,Q., Chen,X., Luo,X., Long,Y., Chong,T., Ye,M., He,H.,
            Lu,A., Ao,K., Yin,M., Xu,A., Li,X., Hao,Y. and Guo,X.
  TITLE     The inhibition of YTHDF3/m6A/LRP6 reprograms fatty acid metabolism
            and suppresses lymph node metastasis in cervical cancer
  JOURNAL   Int J Biol Sci 20 (3), 916-936 (2024)
   PUBMED   38250152
  REMARK    GeneRIF: The inhibition of YTHDF3/m[6]A/LRP6 reprograms fatty acid
            metabolism and suppresses lymph node metastasis in cervical cancer.
            Erratum:[Int J Biol Sci. 2025 Jun 5;21(8):3825-3826. doi:
            10.7150/ijbs.115928. PMID: 40520018]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1613)
  AUTHORS   Li,J., Liu,Z., Ren,Y., Shao,H. and Li,S.
  TITLE     LRP5-/6 gene polymorphisms and its association with risk of
            abnormal bone mass in postmenopausal women
  JOURNAL   J Orthop Surg Res 18 (1), 369 (2023)
   PUBMED   37202775
  REMARK    GeneRIF: LRP5-/6 gene polymorphisms and its association with risk
            of abnormal bone mass in postmenopausal women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1613)
  AUTHORS   Hao,H., Liu,Q., Chen,J. and Zhou,H.
  TITLE     Overexpression of circRNAs LRP6 in gestational diabetes mellitus
            predicts foetal malformation and intrauterine death
  JOURNAL   Endocrinol Diabetes Nutr (Engl Ed) 70 (2), 124-129 (2023)
   PUBMED   36925229
  REMARK    GeneRIF: Overexpression of circRNAs LRP6 in gestational diabetes
            mellitus predicts foetal malformation and intrauterine death.
REFERENCE   5  (residues 1 to 1613)
  AUTHORS   Wang,J., Yang,H., Ma,X., Liu,J., Li,L., Chen,L. and Wei,F.
  TITLE     LRP6/filamentous-actin signaling facilitates osteogenic commitment
            in mechanically induced periodontal ligament stem cells
  JOURNAL   Cell Mol Biol Lett 28 (1), 7 (2023)
   PUBMED   36694134
  REMARK    GeneRIF: LRP6/filamentous-actin signaling facilitates osteogenic
            commitment in mechanically induced periodontal ligament stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1613)
  AUTHORS   Bafico,A., Liu,G., Yaniv,A., Gazit,A. and Aaronson,S.A.
  TITLE     Novel mechanism of Wnt signalling inhibition mediated by Dickkopf-1
            interaction with LRP6/Arrow
  JOURNAL   Nat Cell Biol 3 (7), 683-686 (2001)
   PUBMED   11433302
REFERENCE   7  (residues 1 to 1613)
  AUTHORS   Mao,B., Wu,W., Li,Y., Hoppe,D., Stannek,P., Glinka,A. and Niehrs,C.
  TITLE     LDL-receptor-related protein 6 is a receptor for Dickkopf proteins
  JOURNAL   Nature 411 (6835), 321-325 (2001)
   PUBMED   11357136
REFERENCE   8  (residues 1 to 1613)
  AUTHORS   Tamai,K., Semenov,M., Kato,Y., Spokony,R., Liu,C., Katsuyama,Y.,
            Hess,F., Saint-Jeannet,J.P. and He,X.
  TITLE     LDL-receptor-related proteins in Wnt signal transduction
  JOURNAL   Nature 407 (6803), 530-535 (2000)
   PUBMED   11029007
REFERENCE   9  (residues 1 to 1613)
  AUTHORS   Baens,M., Wlodarska,I., Corveleyn,A., Hoornaert,I., Hagemeijer,A.
            and Marynen,P.
  TITLE     A physical, transcript, and deletion map of chromosome region
            12p12.3 flanked by ETV6 and CDKN1B: hypermethylation of the LRP6
            CpG island in two leukemia patients with hemizygous del(12p)
  JOURNAL   Genomics 56 (1), 40-50 (1999)
   PUBMED   10036184
REFERENCE   10 (residues 1 to 1613)
  AUTHORS   Brown,S.D., Twells,R.C., Hey,P.J., Cox,R.D., Levy,E.R.,
            Soderman,A.R., Metzker,M.L., Caskey,C.T., Todd,J.A. and Hess,J.F.
  TITLE     Isolation and characterization of LRP6, a novel member of the low
            density lipoprotein receptor gene family
  JOURNAL   Biochem Biophys Res Commun 248 (3), 879-888 (1998)
   PUBMED   9704021
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007621.34, AC007537.3 and
            KF455603.1.
            
            On Nov 16, 2022 this sequence version replaced XP_006719141.1.
            
            Summary: This gene encodes a member of the low density lipoprotein
            (LDL) receptor gene family. LDL receptors are transmembrane cell
            surface proteins involved in receptor-mediated endocytosis of
            lipoprotein and protein ligands. The protein encoded by this gene
            functions as a receptor or, with Frizzled, a co-receptor for Wnt
            and thereby transmits the canonical Wnt/beta-catenin signaling
            cascade. Through its interaction with the Wnt/beta-catenin
            signaling cascade this gene plays a role in the regulation of cell
            differentiation, proliferation, and migration and the development
            of many cancer types. This protein undergoes gamma-secretase
            dependent RIP- (regulated intramembrane proteolysis) processing but
            the precise locations of the cleavage sites have not been
            determined.[provided by RefSeq, Dec 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1487870.1,
                                           SRR14038196.1789988.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1613
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..1613
                     /product="low-density lipoprotein receptor-related protein
                     6 isoform b precursor"
                     /note="low-density lipoprotein receptor-related protein 6;
                     LRP-6"
                     /calculated_mol_wt=178425
     Region          1..204
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
                     /calculated_mol_wt=2024
     mat_peptide     20..1613
                     /product="Low-density lipoprotein receptor-related protein
                     6. /id=PRO_0000017330"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
                     /calculated_mol_wt=178425
     Region          20..275
                     /region_name="Beta-propeller 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            42
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            81
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          89..127
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          150..191
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          175..216
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          217..251
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          237..276
                     /region_name="LDL-receptor class B 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          286..323
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          328..589
                     /region_name="Beta-propeller 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          353..393
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          397..437
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          458..499
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          483..524
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            486
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          525..558
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          592..627
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          631..890
                     /region_name="Beta-propeller 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          <654..813
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Site            692
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          697..739
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          827..866
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            859
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            865
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          893..929
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            926
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          933..1202
                     /region_name="Beta-propeller 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          958..998
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          <968..1075
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Site            1039
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          1094..1136
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1207..1243
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1249..1285
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1254,1264,1275..1276)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1268,1271,1275,1281..1282)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1278..1282
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1288..1322
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1293,1301,1312..1313)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1305,1308,1312,1318..1319)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1315..1319
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1326..1360
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1331,1339,1350..1351)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1343,1346,1350,1356..1357)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1353..1357
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            1371..1393
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            1420
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:16513652; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1430
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:16513652; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1479
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17569865; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          1487..1493
                     /region_name="PPPSP motif A"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            1490
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK14, GRK5 and GRK6.
                     /evidence=ECO:0000269|PubMed:16341017,
                     ECO:0000269|PubMed:17698587, ECO:0000269|PubMed:18762581,
                     ECO:0000269|PubMed:19801552, ECO:0000269|PubMed:20059949,
                     ECO:0000269|PubMed:25331957, ECO:0000269|PubMed:27821587,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1493
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK1.
                     /evidence=ECO:0000269|PubMed:16341017; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          1527..1534
                     /region_name="PPPSP motif B"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          1556..1613
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          1568..1575
                     /region_name="PPPSP motif C"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          1588..1593
                     /region_name="PPPSP motif D"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          1603..1610
                     /region_name="PPPSP motif E"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     CDS             1..1613
                     /gene="LRP6"
                     /gene_synonym="ADCAD2; EVR8; OPTA4; STHAG7"
                     /coded_by="NM_001414245.1:310..5151"
                     /note="isoform b precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:4040"
                     /db_xref="HGNC:HGNC:6698"
                     /db_xref="MIM:603507"
ORIGIN      
        1 mgavlrslla csfcvllraa plllyanrrd lrlvdatngk enativvggl edaaavdfvf
       61 shgliywsdv seeaikrtef nktesvqnvv vsgllspdgl acdwlgekly wtdsetnrie
      121 vsnldgslrk vlfwqeldqp raialdpssg fmywtdwgev pkieragmdg ssrfiiinse
      181 iywpngltld yeeqklywad aklnfihksn ldgtnrqavv kgslphpfal tlfedilywt
      241 dwsthsilac nkytgeglre ihsdifspmd ihafsqqrqp natnpcgidn ggcshlclms
      301 pvkpfyqcac ptgvklleng ktckdgatel lllarrtdlr risldtpdft divlqledir
      361 haiaidydpv egyiywtdde vrairrsfid gsgsqfvvta qiahpdgiav dwvarnlywt
      421 dtgtdrievt rlngtmrkil isedleepra ivldpmvgym ywtdwgeipk ieraaldgsd
      481 rvvlvntslg wpnglaldyd egkiywgdak tdkievmntd gtgrrvlved kiphifgftl
      541 lgdyvywtdw qrrsiervhk rsaereviid qlpdlmglka tnvhrvigsn pcaeenggcs
      601 hlclyrpqgl rcacpigfel isdmktcivp eafllfsrra dirrisletn nnnvaipltg
      661 vkeasaldfd vtdnriywtd islktisraf mngsalehvv efgldypegm avdwlgknly
      721 wadtgtnrie vskldgqhrq vlvwkdldsp ralaldpaeg fmywtewggk pkidraamdg
      781 serttlvpnv grangltidy akrrlywtdl dtnliessnm lglnreviad dlphpfgltq
      841 yqdyiywtdw srrsierank tsgqnrtiiq ghldyvmdil vfhssrqsgw necassnghc
      901 shlclavpvg gfvcgcpahy slnadnrtcs apttfllfsq ksainrmvid eqqspdiilp
      961 ihslrnvrai dydpldkqly widsrqnmir kaqedgsqgf tvvvssvpsq nleiqpydls
     1021 idiysryiyw tceatnvinv trldgrsvgv vlkgeqdrpr avvvnpekgy myftnlqers
     1081 pkieraaldg terevlffsg lskpialald srlgklfwad sdlrriessd lsganrivle
     1141 dsnilqpvgl tvfenwlywi dkqqqmieki dmtgregrtk vqariaqlsd ihavkelnlq
     1201 eyrqhpcaqd nggcshiclv kgdgttrcsc pmhlvllqde lscgepptcs pqqftcftge
     1261 idcipvawrc dgftecedhs delncpvcse sqfqcasgqc idgalrcngd ancqdksdek
     1321 ncevlclidq frcangqcig khkkcdhnvd csdksdeldc ypteepapqa tntvgsvigv
     1381 ivtifvsgtv yficqrmlcp rmkgdgetmt ndyvvhgpas vplgyvphps slsgslpgms
     1441 rgksmissls imggssgppy drahvtgass ssssstkgty fpailnppps patershytm
     1501 efgyssnsps thrsysyrpy syrhfapptt pcstdvcdsd yapsrrmtsv atakgytsdl
     1561 nydsepvppp ptprsqylsa eenyescpps pytersyshh lyppppspct dss
//
LOCUS       NP_775873               1576 aa            linear   PRI 21-DEC-2025
DEFINITION  disco-interacting protein 2 homolog B [Homo sapiens].
ACCESSION   NP_775873 XP_498447
VERSION     NP_775873.2
DBSOURCE    REFSEQ: accession NM_173602.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1576)
  AUTHORS   Theberge,E.T., Durbano,K., Demailly,D., Huby,S., Mitina,A., Yin,Y.,
            Mohajeri,A., van Karnebeek,C., Horvath,G.A., Yuen,R.K.C., Usdin,K.,
            Lehman,A., Cif,L. and Richmond,P.A.
  CONSRTM   Care4Rare Canada Consortium
  TITLE     Disco-Interacting Protein 2 Homolog B CGG Repeat Expansion in
            Siblings with Neurodevelopmental Disability and Progressive
            Movement Disorder
  JOURNAL   Mov Disord 40 (3), 567-578 (2025)
   PUBMED   39854091
REFERENCE   2  (residues 1 to 1576)
  AUTHORS   Yuan,Y., Bao,J., Chen,Z., Villanueva,A.D., Wen,W., Wang,F.,
            Zhao,D., Fu,X., Cai,Q., Long,J., Shu,X.O., Zheng,D., Moreno,V.,
            Zheng,W., Lin,W. and Guo,X.
  TITLE     Multi-omics analysis to identify susceptibility genes for
            colorectal cancer
  JOURNAL   Hum Mol Genet 30 (5), 321-330 (2021)
   PUBMED   33481017
  REMARK    GeneRIF: Multi-omics analysis to identify susceptibility genes for
            colorectal cancer.
REFERENCE   3  (residues 1 to 1576)
  AUTHORS   Whiffin,N., Hosking,F.J., Farrington,S.M., Palles,C., Dobbins,S.E.,
            Zgaga,L., Lloyd,A., Kinnersley,B., Gorman,M., Tenesa,A.,
            Broderick,P., Wang,Y., Barclay,E., Hayward,C., Martin,L.,
            Buchanan,D.D., Win,A.K., Hopper,J., Jenkins,M., Lindor,N.M.,
            Newcomb,P.A., Gallinger,S., Conti,D., Schumacher,F., Casey,G.,
            Liu,T., Campbell,H., Lindblom,A., Houlston,R.S., Tomlinson,I.P. and
            Dunlop,M.G.
  CONSRTM   Swedish Low-Risk Colorectal Cancer Study Group
  TITLE     Identification of susceptibility loci for colorectal cancer in a
            genome-wide meta-analysis
  JOURNAL   Hum Mol Genet 23 (17), 4729-4737 (2014)
   PUBMED   24737748
REFERENCE   4  (residues 1 to 1576)
  AUTHORS   Sabater-Lleal,M., Huang,J., Chasman,D., Naitza,S., Dehghan,A.,
            Johnson,A.D., Teumer,A., Reiner,A.P., Folkersen,L., Basu,S.,
            Rudnicka,A.R., Trompet,S., Malarstig,A., Baumert,J., Bis,J.C.,
            Guo,X., Hottenga,J.J., Shin,S.Y., Lopez,L.M., Lahti,J., Tanaka,T.,
            Yanek,L.R., Oudot-Mellakh,T., Wilson,J.F., Navarro,P.,
            Huffman,J.E., Zemunik,T., Redline,S., Mehra,R., Pulanic,D.,
            Rudan,I., Wright,A.F., Kolcic,I., Polasek,O., Wild,S.H.,
            Campbell,H., Curb,J.D., Wallace,R., Liu,S., Eaton,C.B.,
            Becker,D.M., Becker,L.C., Bandinelli,S., Raikkonen,K., Widen,E.,
            Palotie,A., Fornage,M., Green,D., Gross,M., Davies,G., Harris,S.E.,
            Liewald,D.C., Starr,J.M., Williams,F.M., Grant,P.J., Spector,T.D.,
            Strawbridge,R.J., Silveira,A., Sennblad,B., Rivadeneira,F.,
            Uitterlinden,A.G., Franco,O.H., Hofman,A., van Dongen,J.,
            Willemsen,G., Boomsma,D.I., Yao,J., Swords Jenny,N.,
            Haritunians,T., McKnight,B., Lumley,T., Taylor,K.D., Rotter,J.I.,
            Psaty,B.M., Peters,A., Gieger,C., Illig,T., Grotevendt,A.,
            Homuth,G., Volzke,H., Kocher,T., Goel,A., Franzosi,M.G.,
            Seedorf,U., Clarke,R., Steri,M., Tarasov,K.V., Sanna,S.,
            Schlessinger,D., Stott,D.J., Sattar,N., Buckley,B.M., Rumley,A.,
            Lowe,G.D., McArdle,W.L., Chen,M.H., Tofler,G.H., Song,J.,
            Boerwinkle,E., Folsom,A.R., Rose,L.M., Franco-Cereceda,A.,
            Teichert,M., Ikram,M.A., Mosley,T.H., Bevan,S., Dichgans,M.,
            Rothwell,P.M., Sudlow,C.L., Hopewell,J.C., Chambers,J.C.,
            Saleheen,D., Kooner,J.S., Danesh,J., Nelson,C.P., Erdmann,J.,
            Reilly,M.P., Kathiresan,S., Schunkert,H., Morange,P.E.,
            Ferrucci,L., Eriksson,J.G., Jacobs,D., Deary,I.J., Soranzo,N.,
            Witteman,J.C., de Geus,E.J., Tracy,R.P., Hayward,C., Koenig,W.,
            Cucca,F., Jukema,J.W., Eriksson,P., Seshadri,S., Markus,H.S.,
            Watkins,H., Samani,N.J., Wallaschofski,H., Smith,N.L., Tregouet,D.,
            Ridker,P.M., Tang,W., Strachan,D.P., Hamsten,A. and O'Donnell,C.J.
  CONSRTM   VTE Consortium; STROKE Consortium; Wellcome Trust Case Control
            Consortium 2 (WTCCC2); C4D Consortium; CARDIoGRAM Consortium
  TITLE     Multiethnic meta-analysis of genome-wide association studies in
            >100 000 subjects identifies 23 fibrinogen-associated Loci but no
            strong evidence of a causal association between circulating
            fibrinogen and cardiovascular disease
  JOURNAL   Circulation 128 (12), 1310-1324 (2013)
   PUBMED   23969696
REFERENCE   5  (residues 1 to 1576)
  AUTHORS   Houlston,R.S., Cheadle,J., Dobbins,S.E., Tenesa,A., Jones,A.M.,
            Howarth,K., Spain,S.L., Broderick,P., Domingo,E., Farrington,S.,
            Prendergast,J.G., Pittman,A.M., Theodoratou,E., Smith,C.G.,
            Olver,B., Walther,A., Barnetson,R.A., Churchman,M., Jaeger,E.E.,
            Penegar,S., Barclay,E., Martin,L., Gorman,M., Mager,R.,
            Johnstone,E., Midgley,R., Niittymaki,I., Tuupanen,S., Colley,J.,
            Idziaszczyk,S., Thomas,H.J., Lucassen,A.M., Evans,D.G., Maher,E.R.,
            Maughan,T., Dimas,A., Dermitzakis,E., Cazier,J.B., Aaltonen,L.A.,
            Pharoah,P., Kerr,D.J., Carvajal-Carmona,L.G., Campbell,H.,
            Dunlop,M.G. and Tomlinson,I.P.
  CONSRTM   COGENT Consortium; CORGI Consortium; COIN Collaborative Group;
            COINB Collaborative Group
  TITLE     Meta-analysis of three genome-wide association studies identifies
            susceptibility loci for colorectal cancer at 1q41, 3q26.2, 12q13.13
            and 20q13.33
  JOURNAL   Nat Genet 42 (11), 973-977 (2010)
   PUBMED   20972440
REFERENCE   6  (residues 1 to 1576)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   7  (residues 1 to 1576)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 1576)
  AUTHORS   Winnepenninckx,B., Debacker,K., Ramsay,J., Smeets,D., Smits,A.,
            FitzPatrick,D.R. and Kooy,R.F.
  TITLE     CGG-repeat expansion in the DIP2B gene is associated with the
            fragile site FRA12A on chromosome 12q13.1
  JOURNAL   Am J Hum Genet 80 (2), 221-231 (2007)
   PUBMED   17236128
  REMARK    GeneRIF: Deficiency of DIP2B, a brain-expressed gene, may mediate
            the neurocognitive problems associated with FRA12A.
REFERENCE   9  (residues 1 to 1576)
  AUTHORS   Khorram,O., Garthwaite,M., Johnson,M.S., Denessiouk,K.A., Han,G.,
            Guo,T., McPhaul,L.W., Magee,T.R., Westerman,B. and Golos,T.G.
  TITLE     Identification and characterization of a novel luciferase-like
            protein in the human female reproductive tract
  JOURNAL   J Clin Endocrinol Metab 89 (11), 5837-5846 (2004)
   PUBMED   15531550
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK091597.1, BX537905.1,
            BU101773.1, BU102128.1, AB040896.2, BC030156.2, BU429622.1,
            AK097369.1 and AC078818.19.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Nov 22, 2004 this sequence version replaced
            XP_498447.1, NP_775873.1.
            
            Summary: This gene encodes a member of the disco-interacting
            protein homolog 2 protein family. The encoded protein contains a
            binding site for the transcriptional regulator DNA
            methyltransferase 1 associated protein 1 as well as AMP-binding
            sites. The presence of these sites suggests that the encoded
            protein may participate in DNA methylation. This gene is located
            near a folate-sensitive fragile site, and CGG-repeat expansion in
            the promoter of this gene which affects transcription has been
            detected in individuals containing this fragile site on chromosome
            12. [provided by RefSeq, Aug 2011].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.250003.1,
                                           SRR1660803.112122.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301180.10/ ENSP00000301180.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1576
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..1576
                     /product="disco-interacting protein 2 homolog B"
                     /note="DIP2 disco-interacting protein 2 homolog B;
                     disconnected interacting protein 2 homolog B; disco
                     interacting protein 2 homolog B"
                     /calculated_mol_wt=171361
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P265.3)"
     Region          14..131
                     /region_name="DMAP_binding"
                     /note="DMAP1-binding Domain; pfam06464"
                     /db_xref="CDD:368923"
     Region          31..167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P265.3)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P265.3)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9P265.3)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P265.3)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9P265.3)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P265.3)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P265.3)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P265.3)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UH60; propagated from
                     UniProtKB/Swiss-Prot (Q9P265.3)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P265.3)"
     Region          179..201
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P265.3)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P265.3)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P265.3)"
     Region          217..246
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P265.3)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P265.3)"
     Region          355..931
                     /region_name="Dip2"
                     /note="Disco-interacting protein 2 (Dip2); cd05905"
                     /db_xref="CDD:341231"
     Site            order(516,519..524,526..527)
                     /site_type="other"
                     /note="putative acyl-activating enzyme (AAE) consensus
                     motif"
                     /db_xref="CDD:341231"
     Site            order(519,639..640,698..703,796,808,811,822,911)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Site            order(519,560..561,611,613..614,617,639..640,658..663,796,
                     808,811,819..822,892)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341231"
     Site            order(560,613..614,617,639,819..821,879,892)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Region          1007..1572
                     /region_name="Dip2"
                     /note="Disco-interacting protein 2 (Dip2); cd05905"
                     /db_xref="CDD:341231"
     Site            order(1156,1159..1164,1166..1167)
                     /site_type="other"
                     /note="putative acyl-activating enzyme (AAE) consensus
                     motif"
                     /db_xref="CDD:341231"
     Site            order(1159,1285..1286,1340..1345,1437,1459,1462,1473,1552)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Site            order(1159,1200..1201,1251,1253..1254,1257,1285..1286,
                     1303..1308,1437,1459,1462,1470..1473,1533)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341231"
     Site            order(1200,1253..1254,1257,1285,1470..1472,1520,1533)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341231"
     CDS             1..1576
                     /gene="DIP2B"
                     /coded_by="NM_173602.3:157..4887"
                     /db_xref="CCDS:CCDS31799.1"
                     /db_xref="GeneID:57609"
                     /db_xref="HGNC:HGNC:29284"
                     /db_xref="MIM:611379"
ORIGIN      
        1 maerglepsp aavaalppev raqlaelele lsegditqkg yekkrsklls pyspqtqetd
       61 savqkelrnq tpapsaaqts apskyhrtrs ggarderyrs dihteavqaa lakhkeqkma
      121 lpmptkrrst fvqspadact ppdtssased egslrrqaal saalqqslqn aeswinrsiq
      181 gsstsssass tlshgevkgt sgsladvfan trienfsapp dvttttssss ssssirpani
      241 dlppsgivkg mhkgsnrssl mdtadgvpvs srvstkiqql lntlkrpkrp plkeffvdds
      301 eeivevpqpd pnqpkpegrq mtpvkgeplg vicnwppale salqrwgttq akcscltald
      361 mtgkpvytlt ygklwsrslk laytllnklg tknepvlkpg drvalvypnn dpvmfmvafy
      421 gcllaevipv pievpltrkd aggqqigfll gscgialalt sevclkglpk tqngeivqfk
      481 gwprlkwvvt dskylskppk dwqphispag tepayieykt skegsvmgvt vsrlamlshc
      541 qalsqacnys egetivnvld fkkdaglwhg mfanvmnkmh tisvpysvmk tcplswvqrv
      601 hahkakvalv kcrdlhwamm ahrdqrdvsl sslrmlivtd ganpwsvssc daflslfqsh
      661 glkpeaicpc atsaeamtva irrpgvpgap lpgrailsmn glsygvirvn tedknsaltv
      721 qdvghvmpgg mmcivkpdgp pqlcktdeig eicvssrtgg mmyfglagvt kntfevipvn
      781 sagspvgdvp firsgllgfv gpgslvfvvg kmdgllmvsg rrhnaddiva tglavesikt
      841 vyrgriavfs vsvfyderiv vvaeqrpdas eedsfqwmsr vlqaidsihq vgvyclalvp
      901 antlpktplg gihisqtkql flegslhpcn ilmcphtcvt nlpkprqkqp gvgpasvmvg
      961 nlvagkriaq aagrdlgqie endlvrkhqf laeilqwraq atpdhvlfml lnakgttvct
     1021 asclqlhkra eriasvlgdk ghlnagdnvv llyppgieli aafygclyag cipvtvrpph
     1081 aqnltatlpt vrmivdvska aciltsqtlm rllrsreaaa avdvktwpti idtddlprkr
     1141 lpqlykpptp emlayldfsv sttgmltgvk mshsavnalc raiklqcely ssrqiaicld
     1201 pycglgfalw clcsvysghq svlippmele nnlflwlstv nqykirdtfc sysvmelctk
     1261 glgnqvevlk trginlscvr tcvvvaeerp rvalqqsfsk lfkdiglspr avsttfgsrv
     1321 nvaiclqgts gpdpttvyvd lkslrhdrvr lvergapqsl llsesgkilp gvkvvivnpe
     1381 tkgpvgdshl geiwvnspht asgyytiyds etlqadhfnt rlsfgdaaqt lwartgylgf
     1441 vrrteltaat gerhdalyvv galdetlelr glryhpidie tsvsrihrsi aecavftwtn
     1501 llvvvvelcg seqealdlvp lvtnvvleeh ylivgvvvvv dpgvipinsr gekqrmhlrd
     1561 sfladqldpi yvaynm
//
LOCUS       NP_001401184            1444 aa            linear   PRI 21-DEC-2025
DEFINITION  low-density lipoprotein receptor-related protein 6 isoform j [Homo
            sapiens].
ACCESSION   NP_001401184
VERSION     NP_001401184.1
DBSOURCE    REFSEQ: accession NM_001414255.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1444)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1444)
  AUTHORS   Zhong,S., Guo,Q., Chen,X., Luo,X., Long,Y., Chong,T., Ye,M., He,H.,
            Lu,A., Ao,K., Yin,M., Xu,A., Li,X., Hao,Y. and Guo,X.
  TITLE     The inhibition of YTHDF3/m6A/LRP6 reprograms fatty acid metabolism
            and suppresses lymph node metastasis in cervical cancer
  JOURNAL   Int J Biol Sci 20 (3), 916-936 (2024)
   PUBMED   38250152
  REMARK    GeneRIF: The inhibition of YTHDF3/m[6]A/LRP6 reprograms fatty acid
            metabolism and suppresses lymph node metastasis in cervical cancer.
            Erratum:[Int J Biol Sci. 2025 Jun 5;21(8):3825-3826. doi:
            10.7150/ijbs.115928. PMID: 40520018]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1444)
  AUTHORS   Li,J., Liu,Z., Ren,Y., Shao,H. and Li,S.
  TITLE     LRP5-/6 gene polymorphisms and its association with risk of
            abnormal bone mass in postmenopausal women
  JOURNAL   J Orthop Surg Res 18 (1), 369 (2023)
   PUBMED   37202775
  REMARK    GeneRIF: LRP5-/6 gene polymorphisms and its association with risk
            of abnormal bone mass in postmenopausal women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1444)
  AUTHORS   Hao,H., Liu,Q., Chen,J. and Zhou,H.
  TITLE     Overexpression of circRNAs LRP6 in gestational diabetes mellitus
            predicts foetal malformation and intrauterine death
  JOURNAL   Endocrinol Diabetes Nutr (Engl Ed) 70 (2), 124-129 (2023)
   PUBMED   36925229
  REMARK    GeneRIF: Overexpression of circRNAs LRP6 in gestational diabetes
            mellitus predicts foetal malformation and intrauterine death.
REFERENCE   5  (residues 1 to 1444)
  AUTHORS   Wang,J., Yang,H., Ma,X., Liu,J., Li,L., Chen,L. and Wei,F.
  TITLE     LRP6/filamentous-actin signaling facilitates osteogenic commitment
            in mechanically induced periodontal ligament stem cells
  JOURNAL   Cell Mol Biol Lett 28 (1), 7 (2023)
   PUBMED   36694134
  REMARK    GeneRIF: LRP6/filamentous-actin signaling facilitates osteogenic
            commitment in mechanically induced periodontal ligament stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1444)
  AUTHORS   Bafico,A., Liu,G., Yaniv,A., Gazit,A. and Aaronson,S.A.
  TITLE     Novel mechanism of Wnt signalling inhibition mediated by Dickkopf-1
            interaction with LRP6/Arrow
  JOURNAL   Nat Cell Biol 3 (7), 683-686 (2001)
   PUBMED   11433302
REFERENCE   7  (residues 1 to 1444)
  AUTHORS   Mao,B., Wu,W., Li,Y., Hoppe,D., Stannek,P., Glinka,A. and Niehrs,C.
  TITLE     LDL-receptor-related protein 6 is a receptor for Dickkopf proteins
  JOURNAL   Nature 411 (6835), 321-325 (2001)
   PUBMED   11357136
REFERENCE   8  (residues 1 to 1444)
  AUTHORS   Tamai,K., Semenov,M., Kato,Y., Spokony,R., Liu,C., Katsuyama,Y.,
            Hess,F., Saint-Jeannet,J.P. and He,X.
  TITLE     LDL-receptor-related proteins in Wnt signal transduction
  JOURNAL   Nature 407 (6803), 530-535 (2000)
   PUBMED   11029007
REFERENCE   9  (residues 1 to 1444)
  AUTHORS   Baens,M., Wlodarska,I., Corveleyn,A., Hoornaert,I., Hagemeijer,A.
            and Marynen,P.
  TITLE     A physical, transcript, and deletion map of chromosome region
            12p12.3 flanked by ETV6 and CDKN1B: hypermethylation of the LRP6
            CpG island in two leukemia patients with hemizygous del(12p)
  JOURNAL   Genomics 56 (1), 40-50 (1999)
   PUBMED   10036184
REFERENCE   10 (residues 1 to 1444)
  AUTHORS   Brown,S.D., Twells,R.C., Hey,P.J., Cox,R.D., Levy,E.R.,
            Soderman,A.R., Metzker,M.L., Caskey,C.T., Todd,J.A. and Hess,J.F.
  TITLE     Isolation and characterization of LRP6, a novel member of the low
            density lipoprotein receptor gene family
  JOURNAL   Biochem Biophys Res Commun 248 (3), 879-888 (1998)
   PUBMED   9704021
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007621.34, AC007537.3 and
            KF455603.1.
            
            Summary: This gene encodes a member of the low density lipoprotein
            (LDL) receptor gene family. LDL receptors are transmembrane cell
            surface proteins involved in receptor-mediated endocytosis of
            lipoprotein and protein ligands. The protein encoded by this gene
            functions as a receptor or, with Frizzled, a co-receptor for Wnt
            and thereby transmits the canonical Wnt/beta-catenin signaling
            cascade. Through its interaction with the Wnt/beta-catenin
            signaling cascade this gene plays a role in the regulation of cell
            differentiation, proliferation, and migration and the development
            of many cancer types. This protein undergoes gamma-secretase
            dependent RIP- (regulated intramembrane proteolysis) processing but
            the precise locations of the cleavage sites have not been
            determined.[provided by RefSeq, Dec 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1279281.1,
                                           SRR14038194.2022782.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1444
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..1444
                     /product="low-density lipoprotein receptor-related protein
                     6 isoform j"
                     /note="low-density lipoprotein receptor-related protein 6;
                     LRP-6"
                     /calculated_mol_wt=161122
     Region          1..204
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          89..127
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          150..191
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          175..216
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          217..251
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          286..323
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          353..393
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          402..>600
                     /region_name="NHL"
                     /note="NHL repeat unit of beta-propeller proteins;
                     cl18310"
                     /db_xref="CDD:302697"
     Region          405..442
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271322"
     Region          448..489
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271322"
     Region          492..533
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271322"
     Region          535..576
                     /region_name="NHL repeat"
                     /note="NHL repeat [structural motif]"
                     /db_xref="CDD:271322"
     Region          614..656
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          658..697
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          724..760
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          789..829
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          <799..906
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          925..967
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1038..1074
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1080..1116
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1085,1095,1106..1107)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1099,1102,1106,1112..1113)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1109..1113
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1119..1153
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1124,1132,1143..1144)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1136,1139,1143,1149..1150)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1146..1150
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1157..1191
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1162,1170,1181..1182)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1174,1177,1181,1187..1188)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1184..1188
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     CDS             1..1444
                     /gene="LRP6"
                     /gene_synonym="ADCAD2; EVR8; OPTA4; STHAG7"
                     /coded_by="NM_001414255.1:310..4644"
                     /note="isoform j is encoded by transcript variant 13"
                     /db_xref="GeneID:4040"
                     /db_xref="HGNC:HGNC:6698"
                     /db_xref="MIM:603507"
ORIGIN      
        1 mgavlrslla csfcvllraa plllyanrrd lrlvdatngk enativvggl edaaavdfvf
       61 shgliywsdv seeaikrtef nktesvqnvv vsgllspdgl acdwlgekly wtdsetnrie
      121 vsnldgslrk vlfwqeldqp raialdpssg fmywtdwgev pkieragmdg ssrfiiinse
      181 iywpngltld yeeqklywad aklnfihksn ldgtnrqavv kgslphpfal tlfedilywt
      241 dwsthsilac nkytgeglre ihsdifspmd ihafsqqrqp natnpcgidn ggcshlclms
      301 pvkpfyqcac ptgvklleng ktckdgatel lllarrtdlr risldtpdft divlqledir
      361 haiaidydpv egyiywtdde vrairrsfid gsgsqfvvta qiahpdgiav dwvarnlywt
      421 dtgtdrievt rlngtmrkil isedleepra ivldpmvgym ywtdwgeipk ieraaldgsd
      481 rvvlvntslg wpnglaldyd egkiywgdak tdkietisra fmngsalehv vefgldypeg
      541 mavdwlgknl ywadtgtnri evskldgqhr qvlvwkdlds pralaldpae gfmywtewgg
      601 kpkidraamd gserttlvpn vgrangltid yakrrlywtd ldtnliessn mlglnrevia
      661 ddlphpfglt qyqdyiywtd wsrrsieran ktsgqnrtii qghldyvmdi lvfhssrqsg
      721 wnecassngh cshlclavpv ggfvcgcpah yslnadnrtc sapttfllfs qksainrmvi
      781 deqqspdiil pihslrnvra idydpldkql ywidsrqnmi rkaqedgsqg ftvvvssvps
      841 qnleiqpydl sidiysryiy wtceatnvin vtrldgrsvg vvlkgeqdrp ravvvnpekg
      901 ymyftnlqer spkieraald gterevlffs glskpialal dsrlgklfwa dsdlrriess
      961 dlsganrivl edsnilqpvg ltvfenwlyw idkqqqmiek idmtgregrt kvqariaqls
     1021 dihavkelnl qeyrqhpcaq dnggcshicl vkgdgttrcs cpmhlvllqd elscgepptc
     1081 spqqftcftg eidcipvawr cdgftecedh sdelncpvcs esqfqcasgq cidgalrcng
     1141 dancqdksde kncevlclid qfrcangqci gkhkkcdhnv dcsdksdeld cypteepapq
     1201 atntvgsvig vivtifvsgt vyficqrmlc prmkgdgetm tndyvvhgpa svplgyvphp
     1261 sslsgslpgm srgksmissl simggssgpp ydrahvtgas sssssstkgt yfpailnppp
     1321 spatershyt mefgyssnsp sthrsysyrp ysyrhfappt tpcstdvcds dyapsrrmts
     1381 vatakgytsd lnydsepvpp pptprsqyls aeenyescpp spytersysh hlyppppspc
     1441 tdss
//
LOCUS       NP_001350829             457 aa            linear   PRI 21-DEC-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase FTO isoform 8 [Homo
            sapiens].
ACCESSION   NP_001350829
VERSION     NP_001350829.1
DBSOURCE    REFSEQ: accession NM_001363900.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Li,B., Wang,L., Du,M. and He,H.
  TITLE     FTO in oral diseases: Functions, mechanisms, and therapeutic
            potential
  JOURNAL   FASEB J 38 (20), e70115 (2024)
   PUBMED   39436191
  REMARK    GeneRIF: FTO in oral diseases: Functions, mechanisms, and
            therapeutic potential.
            Review article
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Li,Q. and Mu,S.
  TITLE     FTO mediates the diabetic kidney disease progression through
            regulating the m6A modification of NLRP3
  JOURNAL   BMC Nephrol 25 (1), 345 (2024)
   PUBMED   39390397
  REMARK    GeneRIF: FTO mediates the diabetic kidney disease progression
            through regulating the m[6]A modification of NLRP3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Shan,L., Tao,M., Zhang,W., Zhao,J.D., Liu,X.C., Fang,Z.H. and
            Gao,J.R.
  TITLE     Comprehensive analysis of the m6A demethylase FTO in endothelial
            dysfunction by MeRIP sequencing
  JOURNAL   Exp Cell Res 442 (2), 114268 (2024)
   PUBMED   39343042
  REMARK    GeneRIF: Comprehensive analysis of the m[6]A demethylase FTO in
            endothelial dysfunction by MeRIP sequencing.
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Nabeel-Shah,S., Pu,S., Burke,G.L., Ahmed,N., Braunschweig,U.,
            Farhangmehr,S., Lee,H., Wu,M., Ni,Z., Tang,H., Zhong,G., Marcon,E.,
            Zhang,Z., Blencowe,B.J. and Greenblatt,J.F.
  TITLE     Recruitment of the m6A/m6Am demethylase FTO to target RNAs by the
            telomeric zinc finger protein ZBTB48
  JOURNAL   Genome Biol 25 (1), 246 (2024)
   PUBMED   39300486
  REMARK    GeneRIF: Recruitment of the m[6]A/m6Am demethylase FTO to target
            RNAs by the telomeric zinc finger protein ZBTB48.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 457)
  AUTHORS   Hussain,M., Waheed,A., Elahi,A. and Mustafa,G.
  TITLE     Fat Mass and Obesity-Related (FTO) Gene Variant Is a Predictor of
            CVD in T2DM Patients
  JOURNAL   J Diabetes Res 2024, 5914316 (2024)
   PUBMED   39257882
  REMARK    GeneRIF: Fat Mass and Obesity-Related (FTO) Gene Variant Is a
            Predictor of CVD in T2DM Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 457)
  AUTHORS   Zeggini,E., Weedon,M.N., Lindgren,C.M., Frayling,T.M.,
            Elliott,K.S., Lango,H., Timpson,N.J., Perry,J.R., Rayner,N.W.,
            Freathy,R.M., Barrett,J.C., Shields,B., Morris,A.P., Ellard,S.,
            Groves,C.J., Harries,L.W., Marchini,J.L., Owen,K.R., Knight,B.,
            Cardon,L.R., Walker,M., Hitman,G.A., Morris,A.D., Doney,A.S.,
            McCarthy,M.I. and Hattersley,A.T.
  CONSRTM   Wellcome Trust Case Control Consortium (WTCCC)
  TITLE     Replication of genome-wide association signals in UK samples
            reveals risk loci for type 2 diabetes
  JOURNAL   Science 316 (5829), 1336-1341 (2007)
   PUBMED   17463249
  REMARK    Erratum:[Science. 2007 Aug 24;317(5841):1035-6]
REFERENCE   7  (residues 1 to 457)
  AUTHORS   Scott,L.J., Mohlke,K.L., Bonnycastle,L.L., Willer,C.J., Li,Y.,
            Duren,W.L., Erdos,M.R., Stringham,H.M., Chines,P.S., Jackson,A.U.,
            Prokunina-Olsson,L., Ding,C.J., Swift,A.J., Narisu,N., Hu,T.,
            Pruim,R., Xiao,R., Li,X.Y., Conneely,K.N., Riebow,N.L., Sprau,A.G.,
            Tong,M., White,P.P., Hetrick,K.N., Barnhart,M.W., Bark,C.W.,
            Goldstein,J.L., Watkins,L., Xiang,F., Saramies,J., Buchanan,T.A.,
            Watanabe,R.M., Valle,T.T., Kinnunen,L., Abecasis,G.R., Pugh,E.W.,
            Doheny,K.F., Bergman,R.N., Tuomilehto,J., Collins,F.S. and
            Boehnke,M.
  TITLE     A genome-wide association study of type 2 diabetes in Finns detects
            multiple susceptibility variants
  JOURNAL   Science 316 (5829), 1341-1345 (2007)
   PUBMED   17463248
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 457)
  AUTHORS   Dina,C., Meyre,D., Gallina,S., Durand,E., Korner,A., Jacobson,P.,
            Carlsson,L.M., Kiess,W., Vatin,V., Lecoeur,C., Delplanque,J.,
            Vaillant,E., Pattou,F., Ruiz,J., Weill,J., Levy-Marchal,C.,
            Horber,F., Potoczna,N., Hercberg,S., Le Stunff,C., Bougneres,P.,
            Kovacs,P., Marre,M., Balkau,B., Cauchi,S., Chevre,J.C. and
            Froguel,P.
  TITLE     Variation in FTO contributes to childhood obesity and severe adult
            obesity
  JOURNAL   Nat Genet 39 (6), 724-726 (2007)
   PUBMED   17496892
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            GeneRIF: Association with obesity in adult and childre.
            Interestingly, this association receives clear confirmation under a
            Transmission Disequilibrium Test design which is robust to
            population stratification.
REFERENCE   9  (residues 1 to 457)
  AUTHORS   Frayling,T.M., Timpson,N.J., Weedon,M.N., Zeggini,E., Freathy,R.M.,
            Lindgren,C.M., Perry,J.R., Elliott,K.S., Lango,H., Rayner,N.W.,
            Shields,B., Harries,L.W., Barrett,J.C., Ellard,S., Groves,C.J.,
            Knight,B., Patch,A.M., Ness,A.R., Ebrahim,S., Lawlor,D.A.,
            Ring,S.M., Ben-Shlomo,Y., Jarvelin,M.R., Sovio,U., Bennett,A.J.,
            Melzer,D., Ferrucci,L., Loos,R.J., Barroso,I., Wareham,N.J.,
            Karpe,F., Owen,K.R., Cardon,L.R., Walker,M., Hitman,G.A.,
            Palmer,C.N., Doney,A.S., Morris,A.D., Smith,G.D., Hattersley,A.T.
            and McCarthy,M.I.
  TITLE     A common variant in the FTO gene is associated with body mass index
            and predisposes to childhood and adult obesity
  JOURNAL   Science 316 (5826), 889-894 (2007)
   PUBMED   17434869
  REMARK    GeneRIF: A genome-wide search for type 2 diabetes-susceptibility
            genes identified a common variant in the FTO gene that predisposes
            to diabetes through an effect on body mass index
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-environment interaction. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 457)
  AUTHORS   Peters,T., Ausmeier,K. and Ruther,U.
  TITLE     Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft)
            mouse mutation
  JOURNAL   Mamm Genome 10 (10), 983-986 (1999)
   PUBMED   10501967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007909.8, AC007496.6 and
            AC007347.3.
            
            Summary: This gene is a nuclear protein of the AlkB related
            non-haem iron and 2-oxoglutarate-dependent oxygenase superfamily
            but the exact physiological function of this gene is not known.
            Other non-heme iron enzymes function to reverse alkylated DNA and
            RNA damage by oxidative demethylation. Studies in mice and humans
            indicate a role in nervous and cardiovascular systems and a strong
            association with body mass index, obesity risk, and type 2
            diabetes. [provided by RefSeq, Jul 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.135902.1,
                                           SRR14038197.728155.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..457
                     /product="alpha-ketoglutarate-dependent dioxygenase FTO
                     isoform 8"
                     /EC_number="1.14.11.53"
                     /note="alpha-ketoglutarate-dependent dioxygenase FTO; fat
                     mass and obesity-associated protein; AlkB homolog 9; fat
                     mass and obesity associated; m6A(m)-demethylase FTO; tRNA
                     N1-methyl adenine demethylase FTO; mRNA
                     N(6)-methyladenosine demethylase FTO; mRNA
                     (2'-O-methyladenosine-N(6)-)-demethylase FTO; U6 small
                     nuclear RNA N(6)-methyladenosine-demethylase FTO; U6 small
                     nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO;
                     intragenic FTO exon 9 containing transcript; mRNA
                     N(6)-methyladenine demethylase"
                     /calculated_mol_wt=52801
     Region          36..325
                     /region_name="FTO_NTD"
                     /note="FTO catalytic domain; pfam12933"
                     /db_xref="CDD:463755"
     Region          <320..450
                     /region_name="FTO_CTD"
                     /note="FTO C-terminal domain; pfam12934"
                     /db_xref="CDD:432887"
     CDS             1..457
                     /gene="FTO"
                     /gene_synonym="ALKBH9; BMIQ14; GDFD; IFEX9"
                     /coded_by="NM_001363900.2:30..1403"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:79068"
                     /db_xref="HGNC:HGNC:24678"
                     /db_xref="MIM:610966"
ORIGIN      
        1 mkrtptaeer ereakklrll eeledtwlpy ltpkddefyq qwqlkypkli lreassvsee
       61 lhkevqeafl tlhkhgclfr dlvriqgkdl ltpvsrilig npgctykyln trlftvpwpv
      121 kgsnikhtea eiaaacetfl klndylqiet iqaleelaak ekanedavpl cmsadfprvg
      181 mgssyngqde vdiksraayn vtllnfmdpq kmpylkeepy fgmgkmavsw hhdenlvdrs
      241 avavysysce gpeeesedds hlegrdpdiw hvgfkiswdi etpglaiplh qgdcyfmldd
      301 lnathqhcvl agsqprfsst hrvaevefew lrqfwfqgnr yrkctdwwcq pmaqlealwk
      361 kmegvtnavl hevkreglpv eqrneiltai lasltarqnl rrewharcqs riartlpadq
      421 kpecrpywek ddasmplpfd ltdivselrg qlleakp
//
LOCUS       NP_001350830             457 aa            linear   PRI 21-DEC-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase FTO isoform 9 [Homo
            sapiens].
ACCESSION   NP_001350830
VERSION     NP_001350830.1
DBSOURCE    REFSEQ: accession NM_001363901.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Li,B., Wang,L., Du,M. and He,H.
  TITLE     FTO in oral diseases: Functions, mechanisms, and therapeutic
            potential
  JOURNAL   FASEB J 38 (20), e70115 (2024)
   PUBMED   39436191
  REMARK    GeneRIF: FTO in oral diseases: Functions, mechanisms, and
            therapeutic potential.
            Review article
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Li,Q. and Mu,S.
  TITLE     FTO mediates the diabetic kidney disease progression through
            regulating the m6A modification of NLRP3
  JOURNAL   BMC Nephrol 25 (1), 345 (2024)
   PUBMED   39390397
  REMARK    GeneRIF: FTO mediates the diabetic kidney disease progression
            through regulating the m[6]A modification of NLRP3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Shan,L., Tao,M., Zhang,W., Zhao,J.D., Liu,X.C., Fang,Z.H. and
            Gao,J.R.
  TITLE     Comprehensive analysis of the m6A demethylase FTO in endothelial
            dysfunction by MeRIP sequencing
  JOURNAL   Exp Cell Res 442 (2), 114268 (2024)
   PUBMED   39343042
  REMARK    GeneRIF: Comprehensive analysis of the m[6]A demethylase FTO in
            endothelial dysfunction by MeRIP sequencing.
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Nabeel-Shah,S., Pu,S., Burke,G.L., Ahmed,N., Braunschweig,U.,
            Farhangmehr,S., Lee,H., Wu,M., Ni,Z., Tang,H., Zhong,G., Marcon,E.,
            Zhang,Z., Blencowe,B.J. and Greenblatt,J.F.
  TITLE     Recruitment of the m6A/m6Am demethylase FTO to target RNAs by the
            telomeric zinc finger protein ZBTB48
  JOURNAL   Genome Biol 25 (1), 246 (2024)
   PUBMED   39300486
  REMARK    GeneRIF: Recruitment of the m[6]A/m6Am demethylase FTO to target
            RNAs by the telomeric zinc finger protein ZBTB48.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 457)
  AUTHORS   Hussain,M., Waheed,A., Elahi,A. and Mustafa,G.
  TITLE     Fat Mass and Obesity-Related (FTO) Gene Variant Is a Predictor of
            CVD in T2DM Patients
  JOURNAL   J Diabetes Res 2024, 5914316 (2024)
   PUBMED   39257882
  REMARK    GeneRIF: Fat Mass and Obesity-Related (FTO) Gene Variant Is a
            Predictor of CVD in T2DM Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 457)
  AUTHORS   Zeggini,E., Weedon,M.N., Lindgren,C.M., Frayling,T.M.,
            Elliott,K.S., Lango,H., Timpson,N.J., Perry,J.R., Rayner,N.W.,
            Freathy,R.M., Barrett,J.C., Shields,B., Morris,A.P., Ellard,S.,
            Groves,C.J., Harries,L.W., Marchini,J.L., Owen,K.R., Knight,B.,
            Cardon,L.R., Walker,M., Hitman,G.A., Morris,A.D., Doney,A.S.,
            McCarthy,M.I. and Hattersley,A.T.
  CONSRTM   Wellcome Trust Case Control Consortium (WTCCC)
  TITLE     Replication of genome-wide association signals in UK samples
            reveals risk loci for type 2 diabetes
  JOURNAL   Science 316 (5829), 1336-1341 (2007)
   PUBMED   17463249
  REMARK    Erratum:[Science. 2007 Aug 24;317(5841):1035-6]
REFERENCE   7  (residues 1 to 457)
  AUTHORS   Scott,L.J., Mohlke,K.L., Bonnycastle,L.L., Willer,C.J., Li,Y.,
            Duren,W.L., Erdos,M.R., Stringham,H.M., Chines,P.S., Jackson,A.U.,
            Prokunina-Olsson,L., Ding,C.J., Swift,A.J., Narisu,N., Hu,T.,
            Pruim,R., Xiao,R., Li,X.Y., Conneely,K.N., Riebow,N.L., Sprau,A.G.,
            Tong,M., White,P.P., Hetrick,K.N., Barnhart,M.W., Bark,C.W.,
            Goldstein,J.L., Watkins,L., Xiang,F., Saramies,J., Buchanan,T.A.,
            Watanabe,R.M., Valle,T.T., Kinnunen,L., Abecasis,G.R., Pugh,E.W.,
            Doheny,K.F., Bergman,R.N., Tuomilehto,J., Collins,F.S. and
            Boehnke,M.
  TITLE     A genome-wide association study of type 2 diabetes in Finns detects
            multiple susceptibility variants
  JOURNAL   Science 316 (5829), 1341-1345 (2007)
   PUBMED   17463248
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 457)
  AUTHORS   Dina,C., Meyre,D., Gallina,S., Durand,E., Korner,A., Jacobson,P.,
            Carlsson,L.M., Kiess,W., Vatin,V., Lecoeur,C., Delplanque,J.,
            Vaillant,E., Pattou,F., Ruiz,J., Weill,J., Levy-Marchal,C.,
            Horber,F., Potoczna,N., Hercberg,S., Le Stunff,C., Bougneres,P.,
            Kovacs,P., Marre,M., Balkau,B., Cauchi,S., Chevre,J.C. and
            Froguel,P.
  TITLE     Variation in FTO contributes to childhood obesity and severe adult
            obesity
  JOURNAL   Nat Genet 39 (6), 724-726 (2007)
   PUBMED   17496892
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            GeneRIF: Association with obesity in adult and childre.
            Interestingly, this association receives clear confirmation under a
            Transmission Disequilibrium Test design which is robust to
            population stratification.
REFERENCE   9  (residues 1 to 457)
  AUTHORS   Frayling,T.M., Timpson,N.J., Weedon,M.N., Zeggini,E., Freathy,R.M.,
            Lindgren,C.M., Perry,J.R., Elliott,K.S., Lango,H., Rayner,N.W.,
            Shields,B., Harries,L.W., Barrett,J.C., Ellard,S., Groves,C.J.,
            Knight,B., Patch,A.M., Ness,A.R., Ebrahim,S., Lawlor,D.A.,
            Ring,S.M., Ben-Shlomo,Y., Jarvelin,M.R., Sovio,U., Bennett,A.J.,
            Melzer,D., Ferrucci,L., Loos,R.J., Barroso,I., Wareham,N.J.,
            Karpe,F., Owen,K.R., Cardon,L.R., Walker,M., Hitman,G.A.,
            Palmer,C.N., Doney,A.S., Morris,A.D., Smith,G.D., Hattersley,A.T.
            and McCarthy,M.I.
  TITLE     A common variant in the FTO gene is associated with body mass index
            and predisposes to childhood and adult obesity
  JOURNAL   Science 316 (5826), 889-894 (2007)
   PUBMED   17434869
  REMARK    GeneRIF: A genome-wide search for type 2 diabetes-susceptibility
            genes identified a common variant in the FTO gene that predisposes
            to diabetes through an effect on body mass index
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-environment interaction. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 457)
  AUTHORS   Peters,T., Ausmeier,K. and Ruther,U.
  TITLE     Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft)
            mouse mutation
  JOURNAL   Mamm Genome 10 (10), 983-986 (1999)
   PUBMED   10501967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007909.8, AC007496.6 and
            AC007347.3.
            
            Summary: This gene is a nuclear protein of the AlkB related
            non-haem iron and 2-oxoglutarate-dependent oxygenase superfamily
            but the exact physiological function of this gene is not known.
            Other non-heme iron enzymes function to reverse alkylated DNA and
            RNA damage by oxidative demethylation. Studies in mice and humans
            indicate a role in nervous and cardiovascular systems and a strong
            association with body mass index, obesity risk, and type 2
            diabetes. [provided by RefSeq, Jul 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.12576.1,
                                           SRR14038196.2540042.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..457
                     /product="alpha-ketoglutarate-dependent dioxygenase FTO
                     isoform 9"
                     /EC_number="1.14.11.53"
                     /note="alpha-ketoglutarate-dependent dioxygenase FTO; fat
                     mass and obesity-associated protein; AlkB homolog 9; fat
                     mass and obesity associated; m6A(m)-demethylase FTO; tRNA
                     N1-methyl adenine demethylase FTO; mRNA
                     N(6)-methyladenosine demethylase FTO; mRNA
                     (2'-O-methyladenosine-N(6)-)-demethylase FTO; U6 small
                     nuclear RNA N(6)-methyladenosine-demethylase FTO; U6 small
                     nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO;
                     intragenic FTO exon 9 containing transcript; mRNA
                     N(6)-methyladenine demethylase"
                     /calculated_mol_wt=52686
     Region          36..277
                     /region_name="FTO_NTD"
                     /note="FTO catalytic domain; pfam12933"
                     /db_xref="CDD:463755"
     Region          281..450
                     /region_name="FTO_CTD"
                     /note="FTO C-terminal domain; pfam12934"
                     /db_xref="CDD:432887"
     CDS             1..457
                     /gene="FTO"
                     /gene_synonym="ALKBH9; BMIQ14; GDFD; IFEX9"
                     /coded_by="NM_001363901.2:30..1403"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:79068"
                     /db_xref="HGNC:HGNC:24678"
                     /db_xref="MIM:610966"
ORIGIN      
        1 mkrtptaeer ereakklrll eeledtwlpy ltpkddefyq qwqlkypkli lreassvsee
       61 lhkevqeafl tlhkhgclfr dlvriqgkdl ltpvsrilig npgctykyln trlftvpwpv
      121 kgsnikhtea eiaaacetfl klndylqiet iqaleelaak ekanedavpl cmsadfprvg
      181 mgssyngqde vdiksraayn vtllnfmdpq kmpylkeepy fgmgkmavsw hhdenlvdrs
      241 avavysysce ddlnathqhc vlagsqprfs sthrvaecst gtldyilqrc qlalqnvcdd
      301 vdnddvslks fepavlkqge eihnevefew lrqfwfqgnr yrkctdwwcq pmaqlealwk
      361 kmegvtnavl hevkreglpv eqrneiltai lasltarqnl rrewharcqs riartlpadq
      421 kpecrpywek ddasmplpfd ltdivselrg qlleakp
//
LOCUS       NP_001425059             457 aa            linear   PRI 21-DEC-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase FTO isoform 13 [Homo
            sapiens].
ACCESSION   NP_001425059 XP_047290565 XP_054169867
VERSION     NP_001425059.1
DBSOURCE    REFSEQ: accession NM_001438130.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Li,B., Wang,L., Du,M. and He,H.
  TITLE     FTO in oral diseases: Functions, mechanisms, and therapeutic
            potential
  JOURNAL   FASEB J 38 (20), e70115 (2024)
   PUBMED   39436191
  REMARK    GeneRIF: FTO in oral diseases: Functions, mechanisms, and
            therapeutic potential.
            Review article
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Li,Q. and Mu,S.
  TITLE     FTO mediates the diabetic kidney disease progression through
            regulating the m6A modification of NLRP3
  JOURNAL   BMC Nephrol 25 (1), 345 (2024)
   PUBMED   39390397
  REMARK    GeneRIF: FTO mediates the diabetic kidney disease progression
            through regulating the m[6]A modification of NLRP3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Shan,L., Tao,M., Zhang,W., Zhao,J.D., Liu,X.C., Fang,Z.H. and
            Gao,J.R.
  TITLE     Comprehensive analysis of the m6A demethylase FTO in endothelial
            dysfunction by MeRIP sequencing
  JOURNAL   Exp Cell Res 442 (2), 114268 (2024)
   PUBMED   39343042
  REMARK    GeneRIF: Comprehensive analysis of the m[6]A demethylase FTO in
            endothelial dysfunction by MeRIP sequencing.
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Nabeel-Shah,S., Pu,S., Burke,G.L., Ahmed,N., Braunschweig,U.,
            Farhangmehr,S., Lee,H., Wu,M., Ni,Z., Tang,H., Zhong,G., Marcon,E.,
            Zhang,Z., Blencowe,B.J. and Greenblatt,J.F.
  TITLE     Recruitment of the m6A/m6Am demethylase FTO to target RNAs by the
            telomeric zinc finger protein ZBTB48
  JOURNAL   Genome Biol 25 (1), 246 (2024)
   PUBMED   39300486
  REMARK    GeneRIF: Recruitment of the m[6]A/m6Am demethylase FTO to target
            RNAs by the telomeric zinc finger protein ZBTB48.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 457)
  AUTHORS   Hussain,M., Waheed,A., Elahi,A. and Mustafa,G.
  TITLE     Fat Mass and Obesity-Related (FTO) Gene Variant Is a Predictor of
            CVD in T2DM Patients
  JOURNAL   J Diabetes Res 2024, 5914316 (2024)
   PUBMED   39257882
  REMARK    GeneRIF: Fat Mass and Obesity-Related (FTO) Gene Variant Is a
            Predictor of CVD in T2DM Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 457)
  AUTHORS   Zeggini,E., Weedon,M.N., Lindgren,C.M., Frayling,T.M.,
            Elliott,K.S., Lango,H., Timpson,N.J., Perry,J.R., Rayner,N.W.,
            Freathy,R.M., Barrett,J.C., Shields,B., Morris,A.P., Ellard,S.,
            Groves,C.J., Harries,L.W., Marchini,J.L., Owen,K.R., Knight,B.,
            Cardon,L.R., Walker,M., Hitman,G.A., Morris,A.D., Doney,A.S.,
            McCarthy,M.I. and Hattersley,A.T.
  CONSRTM   Wellcome Trust Case Control Consortium (WTCCC)
  TITLE     Replication of genome-wide association signals in UK samples
            reveals risk loci for type 2 diabetes
  JOURNAL   Science 316 (5829), 1336-1341 (2007)
   PUBMED   17463249
  REMARK    Erratum:[Science. 2007 Aug 24;317(5841):1035-6]
REFERENCE   7  (residues 1 to 457)
  AUTHORS   Scott,L.J., Mohlke,K.L., Bonnycastle,L.L., Willer,C.J., Li,Y.,
            Duren,W.L., Erdos,M.R., Stringham,H.M., Chines,P.S., Jackson,A.U.,
            Prokunina-Olsson,L., Ding,C.J., Swift,A.J., Narisu,N., Hu,T.,
            Pruim,R., Xiao,R., Li,X.Y., Conneely,K.N., Riebow,N.L., Sprau,A.G.,
            Tong,M., White,P.P., Hetrick,K.N., Barnhart,M.W., Bark,C.W.,
            Goldstein,J.L., Watkins,L., Xiang,F., Saramies,J., Buchanan,T.A.,
            Watanabe,R.M., Valle,T.T., Kinnunen,L., Abecasis,G.R., Pugh,E.W.,
            Doheny,K.F., Bergman,R.N., Tuomilehto,J., Collins,F.S. and
            Boehnke,M.
  TITLE     A genome-wide association study of type 2 diabetes in Finns detects
            multiple susceptibility variants
  JOURNAL   Science 316 (5829), 1341-1345 (2007)
   PUBMED   17463248
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 457)
  AUTHORS   Dina,C., Meyre,D., Gallina,S., Durand,E., Korner,A., Jacobson,P.,
            Carlsson,L.M., Kiess,W., Vatin,V., Lecoeur,C., Delplanque,J.,
            Vaillant,E., Pattou,F., Ruiz,J., Weill,J., Levy-Marchal,C.,
            Horber,F., Potoczna,N., Hercberg,S., Le Stunff,C., Bougneres,P.,
            Kovacs,P., Marre,M., Balkau,B., Cauchi,S., Chevre,J.C. and
            Froguel,P.
  TITLE     Variation in FTO contributes to childhood obesity and severe adult
            obesity
  JOURNAL   Nat Genet 39 (6), 724-726 (2007)
   PUBMED   17496892
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            GeneRIF: Association with obesity in adult and childre.
            Interestingly, this association receives clear confirmation under a
            Transmission Disequilibrium Test design which is robust to
            population stratification.
REFERENCE   9  (residues 1 to 457)
  AUTHORS   Frayling,T.M., Timpson,N.J., Weedon,M.N., Zeggini,E., Freathy,R.M.,
            Lindgren,C.M., Perry,J.R., Elliott,K.S., Lango,H., Rayner,N.W.,
            Shields,B., Harries,L.W., Barrett,J.C., Ellard,S., Groves,C.J.,
            Knight,B., Patch,A.M., Ness,A.R., Ebrahim,S., Lawlor,D.A.,
            Ring,S.M., Ben-Shlomo,Y., Jarvelin,M.R., Sovio,U., Bennett,A.J.,
            Melzer,D., Ferrucci,L., Loos,R.J., Barroso,I., Wareham,N.J.,
            Karpe,F., Owen,K.R., Cardon,L.R., Walker,M., Hitman,G.A.,
            Palmer,C.N., Doney,A.S., Morris,A.D., Smith,G.D., Hattersley,A.T.
            and McCarthy,M.I.
  TITLE     A common variant in the FTO gene is associated with body mass index
            and predisposes to childhood and adult obesity
  JOURNAL   Science 316 (5826), 889-894 (2007)
   PUBMED   17434869
  REMARK    GeneRIF: A genome-wide search for type 2 diabetes-susceptibility
            genes identified a common variant in the FTO gene that predisposes
            to diabetes through an effect on body mass index
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-environment interaction. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 457)
  AUTHORS   Peters,T., Ausmeier,K. and Ruther,U.
  TITLE     Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft)
            mouse mutation
  JOURNAL   Mamm Genome 10 (10), 983-986 (1999)
   PUBMED   10501967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007909.8 and AC007496.6.
            
            On or before Apr 15, 2025 this sequence version replaced
            XP_047290565.1, XP_054169867.1.
            
            Summary: This gene is a nuclear protein of the AlkB related
            non-haem iron and 2-oxoglutarate-dependent oxygenase superfamily
            but the exact physiological function of this gene is not known.
            Other non-heme iron enzymes function to reverse alkylated DNA and
            RNA damage by oxidative demethylation. Studies in mice and humans
            indicate a role in nervous and cardiovascular systems and a strong
            association with body mass index, obesity risk, and type 2
            diabetes. [provided by RefSeq, Jul 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.301559.1,
                                           SRR14243140.1285981.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2153932
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..457
                     /product="alpha-ketoglutarate-dependent dioxygenase FTO
                     isoform 13"
                     /EC_number="1.14.11.53"
                     /note="alpha-ketoglutarate-dependent dioxygenase FTO; fat
                     mass and obesity-associated protein; AlkB homolog 9; fat
                     mass and obesity associated; m6A(m)-demethylase FTO; tRNA
                     N1-methyl adenine demethylase FTO; mRNA
                     N(6)-methyladenosine demethylase FTO; mRNA
                     (2'-O-methyladenosine-N(6)-)-demethylase FTO; U6 small
                     nuclear RNA N(6)-methyladenosine-demethylase FTO; U6 small
                     nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO;
                     intragenic FTO exon 9 containing transcript; mRNA
                     N(6)-methyladenine demethylase"
                     /calculated_mol_wt=52668
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          32..327
                     /region_name="Fe2OG dioxygenase domain.
                     /evidence=ECO:0000269|PubMed:20376003"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          36..325
                     /region_name="FTO_NTD"
                     /note="FTO catalytic domain; pfam12933"
                     /db_xref="CDD:463755"
     Region          213..224
                     /region_name="Loop L1, predicted to block binding of
                     double-stranded DNA or RNA.
                     /evidence=ECO:0000269|PubMed:20376003"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Site            216
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          329..>455
                     /region_name="FTO_CTD"
                     /note="FTO C-terminal domain; pfam12934"
                     /db_xref="CDD:432887"
     CDS             1..457
                     /gene="FTO"
                     /gene_synonym="ALKBH9; BMIQ14; GDFD; IFEX9"
                     /coded_by="NM_001438130.1:30..1403"
                     /note="isoform 13 is encoded by transcript variant 16"
                     /db_xref="GeneID:79068"
                     /db_xref="HGNC:HGNC:24678"
                     /db_xref="MIM:610966"
ORIGIN      
        1 mkrtptaeer ereakklrll eeledtwlpy ltpkddefyq qwqlkypkli lreassvsee
       61 lhkevqeafl tlhkhgclfr dlvriqgkdl ltpvsrilig npgctykyln trlftvpwpv
      121 kgsnikhtea eiaaacetfl klndylqiet iqaleelaak ekanedavpl cmsadfprvg
      181 mgssyngqde vdiksraayn vtllnfmdpq kmpylkeepy fgmgkmavsw hhdenlvdrs
      241 avavysysce gpeeesedds hlegrdpdiw hvgfkiswdi etpglaiplh qgdcyfmldd
      301 lnathqhcvl agsqprfsst hrvaecstgt ldyilqrcql alqnvcddvd nddvslksfe
      361 pavlkqgeei hnevefewlr qfwfqgnryr kctdwwcqpm aqlealwkkm egvtnavlhe
      421 vkreglpveq rneiltaila sltarqnlrr ewharve
//
LOCUS       NP_001425058             457 aa            linear   PRI 21-DEC-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase FTO isoform 13 [Homo
            sapiens].
ACCESSION   NP_001425058 XP_016879146 XP_054169866
VERSION     NP_001425058.1
DBSOURCE    REFSEQ: accession NM_001438129.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Li,B., Wang,L., Du,M. and He,H.
  TITLE     FTO in oral diseases: Functions, mechanisms, and therapeutic
            potential
  JOURNAL   FASEB J 38 (20), e70115 (2024)
   PUBMED   39436191
  REMARK    GeneRIF: FTO in oral diseases: Functions, mechanisms, and
            therapeutic potential.
            Review article
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Li,Q. and Mu,S.
  TITLE     FTO mediates the diabetic kidney disease progression through
            regulating the m6A modification of NLRP3
  JOURNAL   BMC Nephrol 25 (1), 345 (2024)
   PUBMED   39390397
  REMARK    GeneRIF: FTO mediates the diabetic kidney disease progression
            through regulating the m[6]A modification of NLRP3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Shan,L., Tao,M., Zhang,W., Zhao,J.D., Liu,X.C., Fang,Z.H. and
            Gao,J.R.
  TITLE     Comprehensive analysis of the m6A demethylase FTO in endothelial
            dysfunction by MeRIP sequencing
  JOURNAL   Exp Cell Res 442 (2), 114268 (2024)
   PUBMED   39343042
  REMARK    GeneRIF: Comprehensive analysis of the m[6]A demethylase FTO in
            endothelial dysfunction by MeRIP sequencing.
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Nabeel-Shah,S., Pu,S., Burke,G.L., Ahmed,N., Braunschweig,U.,
            Farhangmehr,S., Lee,H., Wu,M., Ni,Z., Tang,H., Zhong,G., Marcon,E.,
            Zhang,Z., Blencowe,B.J. and Greenblatt,J.F.
  TITLE     Recruitment of the m6A/m6Am demethylase FTO to target RNAs by the
            telomeric zinc finger protein ZBTB48
  JOURNAL   Genome Biol 25 (1), 246 (2024)
   PUBMED   39300486
  REMARK    GeneRIF: Recruitment of the m[6]A/m6Am demethylase FTO to target
            RNAs by the telomeric zinc finger protein ZBTB48.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 457)
  AUTHORS   Hussain,M., Waheed,A., Elahi,A. and Mustafa,G.
  TITLE     Fat Mass and Obesity-Related (FTO) Gene Variant Is a Predictor of
            CVD in T2DM Patients
  JOURNAL   J Diabetes Res 2024, 5914316 (2024)
   PUBMED   39257882
  REMARK    GeneRIF: Fat Mass and Obesity-Related (FTO) Gene Variant Is a
            Predictor of CVD in T2DM Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 457)
  AUTHORS   Zeggini,E., Weedon,M.N., Lindgren,C.M., Frayling,T.M.,
            Elliott,K.S., Lango,H., Timpson,N.J., Perry,J.R., Rayner,N.W.,
            Freathy,R.M., Barrett,J.C., Shields,B., Morris,A.P., Ellard,S.,
            Groves,C.J., Harries,L.W., Marchini,J.L., Owen,K.R., Knight,B.,
            Cardon,L.R., Walker,M., Hitman,G.A., Morris,A.D., Doney,A.S.,
            McCarthy,M.I. and Hattersley,A.T.
  CONSRTM   Wellcome Trust Case Control Consortium (WTCCC)
  TITLE     Replication of genome-wide association signals in UK samples
            reveals risk loci for type 2 diabetes
  JOURNAL   Science 316 (5829), 1336-1341 (2007)
   PUBMED   17463249
  REMARK    Erratum:[Science. 2007 Aug 24;317(5841):1035-6]
REFERENCE   7  (residues 1 to 457)
  AUTHORS   Scott,L.J., Mohlke,K.L., Bonnycastle,L.L., Willer,C.J., Li,Y.,
            Duren,W.L., Erdos,M.R., Stringham,H.M., Chines,P.S., Jackson,A.U.,
            Prokunina-Olsson,L., Ding,C.J., Swift,A.J., Narisu,N., Hu,T.,
            Pruim,R., Xiao,R., Li,X.Y., Conneely,K.N., Riebow,N.L., Sprau,A.G.,
            Tong,M., White,P.P., Hetrick,K.N., Barnhart,M.W., Bark,C.W.,
            Goldstein,J.L., Watkins,L., Xiang,F., Saramies,J., Buchanan,T.A.,
            Watanabe,R.M., Valle,T.T., Kinnunen,L., Abecasis,G.R., Pugh,E.W.,
            Doheny,K.F., Bergman,R.N., Tuomilehto,J., Collins,F.S. and
            Boehnke,M.
  TITLE     A genome-wide association study of type 2 diabetes in Finns detects
            multiple susceptibility variants
  JOURNAL   Science 316 (5829), 1341-1345 (2007)
   PUBMED   17463248
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 457)
  AUTHORS   Dina,C., Meyre,D., Gallina,S., Durand,E., Korner,A., Jacobson,P.,
            Carlsson,L.M., Kiess,W., Vatin,V., Lecoeur,C., Delplanque,J.,
            Vaillant,E., Pattou,F., Ruiz,J., Weill,J., Levy-Marchal,C.,
            Horber,F., Potoczna,N., Hercberg,S., Le Stunff,C., Bougneres,P.,
            Kovacs,P., Marre,M., Balkau,B., Cauchi,S., Chevre,J.C. and
            Froguel,P.
  TITLE     Variation in FTO contributes to childhood obesity and severe adult
            obesity
  JOURNAL   Nat Genet 39 (6), 724-726 (2007)
   PUBMED   17496892
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            GeneRIF: Association with obesity in adult and childre.
            Interestingly, this association receives clear confirmation under a
            Transmission Disequilibrium Test design which is robust to
            population stratification.
REFERENCE   9  (residues 1 to 457)
  AUTHORS   Frayling,T.M., Timpson,N.J., Weedon,M.N., Zeggini,E., Freathy,R.M.,
            Lindgren,C.M., Perry,J.R., Elliott,K.S., Lango,H., Rayner,N.W.,
            Shields,B., Harries,L.W., Barrett,J.C., Ellard,S., Groves,C.J.,
            Knight,B., Patch,A.M., Ness,A.R., Ebrahim,S., Lawlor,D.A.,
            Ring,S.M., Ben-Shlomo,Y., Jarvelin,M.R., Sovio,U., Bennett,A.J.,
            Melzer,D., Ferrucci,L., Loos,R.J., Barroso,I., Wareham,N.J.,
            Karpe,F., Owen,K.R., Cardon,L.R., Walker,M., Hitman,G.A.,
            Palmer,C.N., Doney,A.S., Morris,A.D., Smith,G.D., Hattersley,A.T.
            and McCarthy,M.I.
  TITLE     A common variant in the FTO gene is associated with body mass index
            and predisposes to childhood and adult obesity
  JOURNAL   Science 316 (5826), 889-894 (2007)
   PUBMED   17434869
  REMARK    GeneRIF: A genome-wide search for type 2 diabetes-susceptibility
            genes identified a common variant in the FTO gene that predisposes
            to diabetes through an effect on body mass index
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-environment interaction. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 457)
  AUTHORS   Peters,T., Ausmeier,K. and Ruther,U.
  TITLE     Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft)
            mouse mutation
  JOURNAL   Mamm Genome 10 (10), 983-986 (1999)
   PUBMED   10501967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007909.8 and AC007496.6.
            
            On or before Apr 15, 2025 this sequence version replaced
            XP_016879146.1, XP_054169866.1.
            
            Summary: This gene is a nuclear protein of the AlkB related
            non-haem iron and 2-oxoglutarate-dependent oxygenase superfamily
            but the exact physiological function of this gene is not known.
            Other non-heme iron enzymes function to reverse alkylated DNA and
            RNA damage by oxidative demethylation. Studies in mice and humans
            indicate a role in nervous and cardiovascular systems and a strong
            association with body mass index, obesity risk, and type 2
            diabetes. [provided by RefSeq, Jul 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3683058.1,
                                           SRR1803617.202460.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..457
                     /product="alpha-ketoglutarate-dependent dioxygenase FTO
                     isoform 13"
                     /EC_number="1.14.11.53"
                     /note="alpha-ketoglutarate-dependent dioxygenase FTO; fat
                     mass and obesity-associated protein; AlkB homolog 9; fat
                     mass and obesity associated; m6A(m)-demethylase FTO; tRNA
                     N1-methyl adenine demethylase FTO; mRNA
                     N(6)-methyladenosine demethylase FTO; mRNA
                     (2'-O-methyladenosine-N(6)-)-demethylase FTO; U6 small
                     nuclear RNA N(6)-methyladenosine-demethylase FTO; U6 small
                     nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO;
                     intragenic FTO exon 9 containing transcript; mRNA
                     N(6)-methyladenine demethylase"
                     /calculated_mol_wt=52668
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          32..327
                     /region_name="Fe2OG dioxygenase domain.
                     /evidence=ECO:0000269|PubMed:20376003"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          36..325
                     /region_name="FTO_NTD"
                     /note="FTO catalytic domain; pfam12933"
                     /db_xref="CDD:463755"
     Region          213..224
                     /region_name="Loop L1, predicted to block binding of
                     double-stranded DNA or RNA.
                     /evidence=ECO:0000269|PubMed:20376003"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Site            216
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          329..>455
                     /region_name="FTO_CTD"
                     /note="FTO C-terminal domain; pfam12934"
                     /db_xref="CDD:432887"
     CDS             1..457
                     /gene="FTO"
                     /gene_synonym="ALKBH9; BMIQ14; GDFD; IFEX9"
                     /coded_by="NM_001438129.1:30..1403"
                     /note="isoform 13 is encoded by transcript variant 14"
                     /db_xref="GeneID:79068"
                     /db_xref="HGNC:HGNC:24678"
                     /db_xref="MIM:610966"
ORIGIN      
        1 mkrtptaeer ereakklrll eeledtwlpy ltpkddefyq qwqlkypkli lreassvsee
       61 lhkevqeafl tlhkhgclfr dlvriqgkdl ltpvsrilig npgctykyln trlftvpwpv
      121 kgsnikhtea eiaaacetfl klndylqiet iqaleelaak ekanedavpl cmsadfprvg
      181 mgssyngqde vdiksraayn vtllnfmdpq kmpylkeepy fgmgkmavsw hhdenlvdrs
      241 avavysysce gpeeesedds hlegrdpdiw hvgfkiswdi etpglaiplh qgdcyfmldd
      301 lnathqhcvl agsqprfsst hrvaecstgt ldyilqrcql alqnvcddvd nddvslksfe
      361 pavlkqgeei hnevefewlr qfwfqgnryr kctdwwcqpm aqlealwkkm egvtnavlhe
      421 vkreglpveq rneiltaila sltarqnlrr ewharve
//
LOCUS       NP_001350823             526 aa            linear   PRI 21-DEC-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase FTO isoform 1 [Homo
            sapiens].
ACCESSION   NP_001350823
VERSION     NP_001350823.1
DBSOURCE    REFSEQ: accession NM_001363894.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Li,B., Wang,L., Du,M. and He,H.
  TITLE     FTO in oral diseases: Functions, mechanisms, and therapeutic
            potential
  JOURNAL   FASEB J 38 (20), e70115 (2024)
   PUBMED   39436191
  REMARK    GeneRIF: FTO in oral diseases: Functions, mechanisms, and
            therapeutic potential.
            Review article
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Li,Q. and Mu,S.
  TITLE     FTO mediates the diabetic kidney disease progression through
            regulating the m6A modification of NLRP3
  JOURNAL   BMC Nephrol 25 (1), 345 (2024)
   PUBMED   39390397
  REMARK    GeneRIF: FTO mediates the diabetic kidney disease progression
            through regulating the m[6]A modification of NLRP3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Shan,L., Tao,M., Zhang,W., Zhao,J.D., Liu,X.C., Fang,Z.H. and
            Gao,J.R.
  TITLE     Comprehensive analysis of the m6A demethylase FTO in endothelial
            dysfunction by MeRIP sequencing
  JOURNAL   Exp Cell Res 442 (2), 114268 (2024)
   PUBMED   39343042
  REMARK    GeneRIF: Comprehensive analysis of the m[6]A demethylase FTO in
            endothelial dysfunction by MeRIP sequencing.
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Nabeel-Shah,S., Pu,S., Burke,G.L., Ahmed,N., Braunschweig,U.,
            Farhangmehr,S., Lee,H., Wu,M., Ni,Z., Tang,H., Zhong,G., Marcon,E.,
            Zhang,Z., Blencowe,B.J. and Greenblatt,J.F.
  TITLE     Recruitment of the m6A/m6Am demethylase FTO to target RNAs by the
            telomeric zinc finger protein ZBTB48
  JOURNAL   Genome Biol 25 (1), 246 (2024)
   PUBMED   39300486
  REMARK    GeneRIF: Recruitment of the m[6]A/m6Am demethylase FTO to target
            RNAs by the telomeric zinc finger protein ZBTB48.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Hussain,M., Waheed,A., Elahi,A. and Mustafa,G.
  TITLE     Fat Mass and Obesity-Related (FTO) Gene Variant Is a Predictor of
            CVD in T2DM Patients
  JOURNAL   J Diabetes Res 2024, 5914316 (2024)
   PUBMED   39257882
  REMARK    GeneRIF: Fat Mass and Obesity-Related (FTO) Gene Variant Is a
            Predictor of CVD in T2DM Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 526)
  AUTHORS   Zeggini,E., Weedon,M.N., Lindgren,C.M., Frayling,T.M.,
            Elliott,K.S., Lango,H., Timpson,N.J., Perry,J.R., Rayner,N.W.,
            Freathy,R.M., Barrett,J.C., Shields,B., Morris,A.P., Ellard,S.,
            Groves,C.J., Harries,L.W., Marchini,J.L., Owen,K.R., Knight,B.,
            Cardon,L.R., Walker,M., Hitman,G.A., Morris,A.D., Doney,A.S.,
            McCarthy,M.I. and Hattersley,A.T.
  CONSRTM   Wellcome Trust Case Control Consortium (WTCCC)
  TITLE     Replication of genome-wide association signals in UK samples
            reveals risk loci for type 2 diabetes
  JOURNAL   Science 316 (5829), 1336-1341 (2007)
   PUBMED   17463249
  REMARK    Erratum:[Science. 2007 Aug 24;317(5841):1035-6]
REFERENCE   7  (residues 1 to 526)
  AUTHORS   Scott,L.J., Mohlke,K.L., Bonnycastle,L.L., Willer,C.J., Li,Y.,
            Duren,W.L., Erdos,M.R., Stringham,H.M., Chines,P.S., Jackson,A.U.,
            Prokunina-Olsson,L., Ding,C.J., Swift,A.J., Narisu,N., Hu,T.,
            Pruim,R., Xiao,R., Li,X.Y., Conneely,K.N., Riebow,N.L., Sprau,A.G.,
            Tong,M., White,P.P., Hetrick,K.N., Barnhart,M.W., Bark,C.W.,
            Goldstein,J.L., Watkins,L., Xiang,F., Saramies,J., Buchanan,T.A.,
            Watanabe,R.M., Valle,T.T., Kinnunen,L., Abecasis,G.R., Pugh,E.W.,
            Doheny,K.F., Bergman,R.N., Tuomilehto,J., Collins,F.S. and
            Boehnke,M.
  TITLE     A genome-wide association study of type 2 diabetes in Finns detects
            multiple susceptibility variants
  JOURNAL   Science 316 (5829), 1341-1345 (2007)
   PUBMED   17463248
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 526)
  AUTHORS   Dina,C., Meyre,D., Gallina,S., Durand,E., Korner,A., Jacobson,P.,
            Carlsson,L.M., Kiess,W., Vatin,V., Lecoeur,C., Delplanque,J.,
            Vaillant,E., Pattou,F., Ruiz,J., Weill,J., Levy-Marchal,C.,
            Horber,F., Potoczna,N., Hercberg,S., Le Stunff,C., Bougneres,P.,
            Kovacs,P., Marre,M., Balkau,B., Cauchi,S., Chevre,J.C. and
            Froguel,P.
  TITLE     Variation in FTO contributes to childhood obesity and severe adult
            obesity
  JOURNAL   Nat Genet 39 (6), 724-726 (2007)
   PUBMED   17496892
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            GeneRIF: Association with obesity in adult and childre.
            Interestingly, this association receives clear confirmation under a
            Transmission Disequilibrium Test design which is robust to
            population stratification.
REFERENCE   9  (residues 1 to 526)
  AUTHORS   Frayling,T.M., Timpson,N.J., Weedon,M.N., Zeggini,E., Freathy,R.M.,
            Lindgren,C.M., Perry,J.R., Elliott,K.S., Lango,H., Rayner,N.W.,
            Shields,B., Harries,L.W., Barrett,J.C., Ellard,S., Groves,C.J.,
            Knight,B., Patch,A.M., Ness,A.R., Ebrahim,S., Lawlor,D.A.,
            Ring,S.M., Ben-Shlomo,Y., Jarvelin,M.R., Sovio,U., Bennett,A.J.,
            Melzer,D., Ferrucci,L., Loos,R.J., Barroso,I., Wareham,N.J.,
            Karpe,F., Owen,K.R., Cardon,L.R., Walker,M., Hitman,G.A.,
            Palmer,C.N., Doney,A.S., Morris,A.D., Smith,G.D., Hattersley,A.T.
            and McCarthy,M.I.
  TITLE     A common variant in the FTO gene is associated with body mass index
            and predisposes to childhood and adult obesity
  JOURNAL   Science 316 (5826), 889-894 (2007)
   PUBMED   17434869
  REMARK    GeneRIF: A genome-wide search for type 2 diabetes-susceptibility
            genes identified a common variant in the FTO gene that predisposes
            to diabetes through an effect on body mass index
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-environment interaction. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 526)
  AUTHORS   Peters,T., Ausmeier,K. and Ruther,U.
  TITLE     Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft)
            mouse mutation
  JOURNAL   Mamm Genome 10 (10), 983-986 (1999)
   PUBMED   10501967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007909.8, AC007496.6 and
            AC007347.3.
            
            Summary: This gene is a nuclear protein of the AlkB related
            non-haem iron and 2-oxoglutarate-dependent oxygenase superfamily
            but the exact physiological function of this gene is not known.
            Other non-heme iron enzymes function to reverse alkylated DNA and
            RNA damage by oxidative demethylation. Studies in mice and humans
            indicate a role in nervous and cardiovascular systems and a strong
            association with body mass index, obesity risk, and type 2
            diabetes. [provided by RefSeq, Jul 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.139678.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..526
                     /product="alpha-ketoglutarate-dependent dioxygenase FTO
                     isoform 1"
                     /EC_number="1.14.11.53"
                     /note="alpha-ketoglutarate-dependent dioxygenase FTO; fat
                     mass and obesity-associated protein; AlkB homolog 9; fat
                     mass and obesity associated; m6A(m)-demethylase FTO; tRNA
                     N1-methyl adenine demethylase FTO; mRNA
                     N(6)-methyladenosine demethylase FTO; mRNA
                     (2'-O-methyladenosine-N(6)-)-demethylase FTO; U6 small
                     nuclear RNA N(6)-methyladenosine-demethylase FTO; U6 small
                     nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO;
                     intragenic FTO exon 9 containing transcript; mRNA
                     N(6)-methyladenine demethylase"
                     /calculated_mol_wt=60587
     Region          36..325
                     /region_name="FTO_NTD"
                     /note="FTO catalytic domain; pfam12933"
                     /db_xref="CDD:463755"
     Region          329..519
                     /region_name="FTO_CTD"
                     /note="FTO C-terminal domain; pfam12934"
                     /db_xref="CDD:432887"
     CDS             1..526
                     /gene="FTO"
                     /gene_synonym="ALKBH9; BMIQ14; GDFD; IFEX9"
                     /coded_by="NM_001363894.2:30..1610"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:79068"
                     /db_xref="HGNC:HGNC:24678"
                     /db_xref="MIM:610966"
ORIGIN      
        1 mkrtptaeer ereakklrll eeledtwlpy ltpkddefyq qwqlkypkli lreassvsee
       61 lhkevqeafl tlhkhgclfr dlvriqgkdl ltpvsrilig npgctykyln trlftvpwpv
      121 kgsnikhtea eiaaacetfl klndylqiet iqaleelaak ekanedavpl cmsadfprvg
      181 mgssyngqde vdiksraayn vtllnfmdpq kmpylkeepy fgmgkmavsw hhdenlvdrs
      241 avavysysce gpeeesedds hlegrdpdiw hvgfkiswdi etpglaiplh qgdcyfmldd
      301 lnathqhcvl agsqprfsst hrvaecstgt ldyilqrcql alqnvcddvd nddvslksfe
      361 pavlkqgeei hnevefewlr qfwfqgnryr kctdwwcqpm aqlealwkkm egvisvelyk
      421 elglmsprli rhkatnavlh evkreglpve qrneiltail asltarqnlr rewharcqsr
      481 iartlpadqk pecrpywekd dasmplpfdl tdivselrgq lleakp
//
LOCUS       NP_002327               1613 aa            linear   PRI 21-DEC-2025
DEFINITION  low-density lipoprotein receptor-related protein 6 isoform b
            precursor [Homo sapiens].
ACCESSION   NP_002327
VERSION     NP_002327.2
DBSOURCE    REFSEQ: accession NM_002336.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1613)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1613)
  AUTHORS   Zhong,S., Guo,Q., Chen,X., Luo,X., Long,Y., Chong,T., Ye,M., He,H.,
            Lu,A., Ao,K., Yin,M., Xu,A., Li,X., Hao,Y. and Guo,X.
  TITLE     The inhibition of YTHDF3/m6A/LRP6 reprograms fatty acid metabolism
            and suppresses lymph node metastasis in cervical cancer
  JOURNAL   Int J Biol Sci 20 (3), 916-936 (2024)
   PUBMED   38250152
  REMARK    GeneRIF: The inhibition of YTHDF3/m[6]A/LRP6 reprograms fatty acid
            metabolism and suppresses lymph node metastasis in cervical cancer.
            Erratum:[Int J Biol Sci. 2025 Jun 5;21(8):3825-3826. doi:
            10.7150/ijbs.115928. PMID: 40520018]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1613)
  AUTHORS   Li,J., Liu,Z., Ren,Y., Shao,H. and Li,S.
  TITLE     LRP5-/6 gene polymorphisms and its association with risk of
            abnormal bone mass in postmenopausal women
  JOURNAL   J Orthop Surg Res 18 (1), 369 (2023)
   PUBMED   37202775
  REMARK    GeneRIF: LRP5-/6 gene polymorphisms and its association with risk
            of abnormal bone mass in postmenopausal women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1613)
  AUTHORS   Hao,H., Liu,Q., Chen,J. and Zhou,H.
  TITLE     Overexpression of circRNAs LRP6 in gestational diabetes mellitus
            predicts foetal malformation and intrauterine death
  JOURNAL   Endocrinol Diabetes Nutr (Engl Ed) 70 (2), 124-129 (2023)
   PUBMED   36925229
  REMARK    GeneRIF: Overexpression of circRNAs LRP6 in gestational diabetes
            mellitus predicts foetal malformation and intrauterine death.
REFERENCE   5  (residues 1 to 1613)
  AUTHORS   Wang,J., Yang,H., Ma,X., Liu,J., Li,L., Chen,L. and Wei,F.
  TITLE     LRP6/filamentous-actin signaling facilitates osteogenic commitment
            in mechanically induced periodontal ligament stem cells
  JOURNAL   Cell Mol Biol Lett 28 (1), 7 (2023)
   PUBMED   36694134
  REMARK    GeneRIF: LRP6/filamentous-actin signaling facilitates osteogenic
            commitment in mechanically induced periodontal ligament stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1613)
  AUTHORS   Bafico,A., Liu,G., Yaniv,A., Gazit,A. and Aaronson,S.A.
  TITLE     Novel mechanism of Wnt signalling inhibition mediated by Dickkopf-1
            interaction with LRP6/Arrow
  JOURNAL   Nat Cell Biol 3 (7), 683-686 (2001)
   PUBMED   11433302
REFERENCE   7  (residues 1 to 1613)
  AUTHORS   Mao,B., Wu,W., Li,Y., Hoppe,D., Stannek,P., Glinka,A. and Niehrs,C.
  TITLE     LDL-receptor-related protein 6 is a receptor for Dickkopf proteins
  JOURNAL   Nature 411 (6835), 321-325 (2001)
   PUBMED   11357136
REFERENCE   8  (residues 1 to 1613)
  AUTHORS   Tamai,K., Semenov,M., Kato,Y., Spokony,R., Liu,C., Katsuyama,Y.,
            Hess,F., Saint-Jeannet,J.P. and He,X.
  TITLE     LDL-receptor-related proteins in Wnt signal transduction
  JOURNAL   Nature 407 (6803), 530-535 (2000)
   PUBMED   11029007
REFERENCE   9  (residues 1 to 1613)
  AUTHORS   Baens,M., Wlodarska,I., Corveleyn,A., Hoornaert,I., Hagemeijer,A.
            and Marynen,P.
  TITLE     A physical, transcript, and deletion map of chromosome region
            12p12.3 flanked by ETV6 and CDKN1B: hypermethylation of the LRP6
            CpG island in two leukemia patients with hemizygous del(12p)
  JOURNAL   Genomics 56 (1), 40-50 (1999)
   PUBMED   10036184
REFERENCE   10 (residues 1 to 1613)
  AUTHORS   Brown,S.D., Twells,R.C., Hey,P.J., Cox,R.D., Levy,E.R.,
            Soderman,A.R., Metzker,M.L., Caskey,C.T., Todd,J.A. and Hess,J.F.
  TITLE     Isolation and characterization of LRP6, a novel member of the low
            density lipoprotein receptor gene family
  JOURNAL   Biochem Biophys Res Commun 248 (3), 879-888 (1998)
   PUBMED   9704021
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007621.34, BP229563.1,
            AF074264.1, BC126405.1, AC007537.3 and AA126261.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 8, 2007 this sequence version replaced NP_002327.1.
            
            Summary: This gene encodes a member of the low density lipoprotein
            (LDL) receptor gene family. LDL receptors are transmembrane cell
            surface proteins involved in receptor-mediated endocytosis of
            lipoprotein and protein ligands. The protein encoded by this gene
            functions as a receptor or, with Frizzled, a co-receptor for Wnt
            and thereby transmits the canonical Wnt/beta-catenin signaling
            cascade. Through its interaction with the Wnt/beta-catenin
            signaling cascade this gene plays a role in the regulation of cell
            differentiation, proliferation, and migration and the development
            of many cancer types. This protein undergoes gamma-secretase
            dependent RIP- (regulated intramembrane proteolysis) processing but
            the precise locations of the cleavage sites have not been
            determined.[provided by RefSeq, Dec 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2563509.1, AF074264.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261349.9/ ENSP00000261349.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1613
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..1613
                     /product="low-density lipoprotein receptor-related protein
                     6 isoform b precursor"
                     /note="low-density lipoprotein receptor-related protein 6;
                     LRP-6"
                     /calculated_mol_wt=180299
     Region          1..204
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     mat_peptide     20..1613
                     /product="low-density lipoprotein receptor-related protein
                     6 isoform b"
                     /calculated_mol_wt=178425
     Region          20..275
                     /region_name="Beta-propeller 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            42
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            81
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          89..127
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          150..191
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          175..216
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          217..251
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          237..276
                     /region_name="LDL-receptor class B 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          286..323
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          328..589
                     /region_name="Beta-propeller 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          353..393
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          397..437
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          458..499
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          483..524
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            486
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          525..558
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          592..627
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          631..890
                     /region_name="Beta-propeller 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          <654..813
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Site            692
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          697..739
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          827..866
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            859
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            865
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          893..929
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            926
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          933..1202
                     /region_name="Beta-propeller 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          958..998
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          <968..1075
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Site            1039
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          1094..1136
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1207..1243
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1249..1285
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1254,1264,1275..1276)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1268,1271,1275,1281..1282)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1278..1282
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1288..1322
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1293,1301,1312..1313)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1305,1308,1312,1318..1319)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1315..1319
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1326..1360
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1331,1339,1350..1351)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1343,1346,1350,1356..1357)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1353..1357
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            1371..1393
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            1420
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:16513652; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1430
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:16513652; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1479
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17569865; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          1487..1493
                     /region_name="PPPSP motif A"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            1490
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK14, GRK5 and GRK6.
                     /evidence=ECO:0000269|PubMed:16341017,
                     ECO:0000269|PubMed:17698587, ECO:0000269|PubMed:18762581,
                     ECO:0000269|PubMed:19801552, ECO:0000269|PubMed:20059949,
                     ECO:0000269|PubMed:25331957, ECO:0000269|PubMed:27821587,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1493
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK1.
                     /evidence=ECO:0000269|PubMed:16341017; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          1527..1534
                     /region_name="PPPSP motif B"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          1556..1613
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          1568..1575
                     /region_name="PPPSP motif C"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          1588..1593
                     /region_name="PPPSP motif D"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          1603..1610
                     /region_name="PPPSP motif E"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     CDS             1..1613
                     /gene="LRP6"
                     /gene_synonym="ADCAD2; EVR8; OPTA4; STHAG7"
                     /coded_by="NM_002336.3:310..5151"
                     /note="isoform b precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS8647.1"
                     /db_xref="GeneID:4040"
                     /db_xref="HGNC:HGNC:6698"
                     /db_xref="MIM:603507"
ORIGIN      
        1 mgavlrslla csfcvllraa plllyanrrd lrlvdatngk enativvggl edaaavdfvf
       61 shgliywsdv seeaikrtef nktesvqnvv vsgllspdgl acdwlgekly wtdsetnrie
      121 vsnldgslrk vlfwqeldqp raialdpssg fmywtdwgev pkieragmdg ssrfiiinse
      181 iywpngltld yeeqklywad aklnfihksn ldgtnrqavv kgslphpfal tlfedilywt
      241 dwsthsilac nkytgeglre ihsdifspmd ihafsqqrqp natnpcgidn ggcshlclms
      301 pvkpfyqcac ptgvklleng ktckdgatel lllarrtdlr risldtpdft divlqledir
      361 haiaidydpv egyiywtdde vrairrsfid gsgsqfvvta qiahpdgiav dwvarnlywt
      421 dtgtdrievt rlngtmrkil isedleepra ivldpmvgym ywtdwgeipk ieraaldgsd
      481 rvvlvntslg wpnglaldyd egkiywgdak tdkievmntd gtgrrvlved kiphifgftl
      541 lgdyvywtdw qrrsiervhk rsaereviid qlpdlmglka tnvhrvigsn pcaeenggcs
      601 hlclyrpqgl rcacpigfel isdmktcivp eafllfsrra dirrisletn nnnvaipltg
      661 vkeasaldfd vtdnriywtd islktisraf mngsalehvv efgldypegm avdwlgknly
      721 wadtgtnrie vskldgqhrq vlvwkdldsp ralaldpaeg fmywtewggk pkidraamdg
      781 serttlvpnv grangltidy akrrlywtdl dtnliessnm lglnreviad dlphpfgltq
      841 yqdyiywtdw srrsierank tsgqnrtiiq ghldyvmdil vfhssrqsgw necassnghc
      901 shlclavpvg gfvcgcpahy slnadnrtcs apttfllfsq ksainrmvid eqqspdiilp
      961 ihslrnvrai dydpldkqly widsrqnmir kaqedgsqgf tvvvssvpsq nleiqpydls
     1021 idiysryiyw tceatnvinv trldgrsvgv vlkgeqdrpr avvvnpekgy myftnlqers
     1081 pkieraaldg terevlffsg lskpialald srlgklfwad sdlrriessd lsganrivle
     1141 dsnilqpvgl tvfenwlywi dkqqqmieki dmtgregrtk vqariaqlsd ihavkelnlq
     1201 eyrqhpcaqd nggcshiclv kgdgttrcsc pmhlvllqde lscgepptcs pqqftcftge
     1261 idcipvawrc dgftecedhs delncpvcse sqfqcasgqc idgalrcngd ancqdksdek
     1321 ncevlclidq frcangqcig khkkcdhnvd csdksdeldc ypteepapqa tntvgsvigv
     1381 ivtifvsgtv yficqrmlcp rmkgdgetmt ndyvvhgpas vplgyvphps slsgslpgms
     1441 rgksmissls imggssgppy drahvtgass ssssstkgty fpailnppps patershytm
     1501 efgyssnsps thrsysyrpy syrhfapptt pcstdvcdsd yapsrrmtsv atakgytsdl
     1561 nydsepvppp ptprsqylsa eenyescpps pytersyshh lyppppspct dss
//
LOCUS       NP_001401175            1568 aa            linear   PRI 21-DEC-2025
DEFINITION  low-density lipoprotein receptor-related protein 6 isoform c [Homo
            sapiens].
ACCESSION   NP_001401175
VERSION     NP_001401175.1
DBSOURCE    REFSEQ: accession NM_001414246.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1568)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1568)
  AUTHORS   Zhong,S., Guo,Q., Chen,X., Luo,X., Long,Y., Chong,T., Ye,M., He,H.,
            Lu,A., Ao,K., Yin,M., Xu,A., Li,X., Hao,Y. and Guo,X.
  TITLE     The inhibition of YTHDF3/m6A/LRP6 reprograms fatty acid metabolism
            and suppresses lymph node metastasis in cervical cancer
  JOURNAL   Int J Biol Sci 20 (3), 916-936 (2024)
   PUBMED   38250152
  REMARK    GeneRIF: The inhibition of YTHDF3/m[6]A/LRP6 reprograms fatty acid
            metabolism and suppresses lymph node metastasis in cervical cancer.
            Erratum:[Int J Biol Sci. 2025 Jun 5;21(8):3825-3826. doi:
            10.7150/ijbs.115928. PMID: 40520018]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1568)
  AUTHORS   Li,J., Liu,Z., Ren,Y., Shao,H. and Li,S.
  TITLE     LRP5-/6 gene polymorphisms and its association with risk of
            abnormal bone mass in postmenopausal women
  JOURNAL   J Orthop Surg Res 18 (1), 369 (2023)
   PUBMED   37202775
  REMARK    GeneRIF: LRP5-/6 gene polymorphisms and its association with risk
            of abnormal bone mass in postmenopausal women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1568)
  AUTHORS   Hao,H., Liu,Q., Chen,J. and Zhou,H.
  TITLE     Overexpression of circRNAs LRP6 in gestational diabetes mellitus
            predicts foetal malformation and intrauterine death
  JOURNAL   Endocrinol Diabetes Nutr (Engl Ed) 70 (2), 124-129 (2023)
   PUBMED   36925229
  REMARK    GeneRIF: Overexpression of circRNAs LRP6 in gestational diabetes
            mellitus predicts foetal malformation and intrauterine death.
REFERENCE   5  (residues 1 to 1568)
  AUTHORS   Wang,J., Yang,H., Ma,X., Liu,J., Li,L., Chen,L. and Wei,F.
  TITLE     LRP6/filamentous-actin signaling facilitates osteogenic commitment
            in mechanically induced periodontal ligament stem cells
  JOURNAL   Cell Mol Biol Lett 28 (1), 7 (2023)
   PUBMED   36694134
  REMARK    GeneRIF: LRP6/filamentous-actin signaling facilitates osteogenic
            commitment in mechanically induced periodontal ligament stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1568)
  AUTHORS   Bafico,A., Liu,G., Yaniv,A., Gazit,A. and Aaronson,S.A.
  TITLE     Novel mechanism of Wnt signalling inhibition mediated by Dickkopf-1
            interaction with LRP6/Arrow
  JOURNAL   Nat Cell Biol 3 (7), 683-686 (2001)
   PUBMED   11433302
REFERENCE   7  (residues 1 to 1568)
  AUTHORS   Mao,B., Wu,W., Li,Y., Hoppe,D., Stannek,P., Glinka,A. and Niehrs,C.
  TITLE     LDL-receptor-related protein 6 is a receptor for Dickkopf proteins
  JOURNAL   Nature 411 (6835), 321-325 (2001)
   PUBMED   11357136
REFERENCE   8  (residues 1 to 1568)
  AUTHORS   Tamai,K., Semenov,M., Kato,Y., Spokony,R., Liu,C., Katsuyama,Y.,
            Hess,F., Saint-Jeannet,J.P. and He,X.
  TITLE     LDL-receptor-related proteins in Wnt signal transduction
  JOURNAL   Nature 407 (6803), 530-535 (2000)
   PUBMED   11029007
REFERENCE   9  (residues 1 to 1568)
  AUTHORS   Baens,M., Wlodarska,I., Corveleyn,A., Hoornaert,I., Hagemeijer,A.
            and Marynen,P.
  TITLE     A physical, transcript, and deletion map of chromosome region
            12p12.3 flanked by ETV6 and CDKN1B: hypermethylation of the LRP6
            CpG island in two leukemia patients with hemizygous del(12p)
  JOURNAL   Genomics 56 (1), 40-50 (1999)
   PUBMED   10036184
REFERENCE   10 (residues 1 to 1568)
  AUTHORS   Brown,S.D., Twells,R.C., Hey,P.J., Cox,R.D., Levy,E.R.,
            Soderman,A.R., Metzker,M.L., Caskey,C.T., Todd,J.A. and Hess,J.F.
  TITLE     Isolation and characterization of LRP6, a novel member of the low
            density lipoprotein receptor gene family
  JOURNAL   Biochem Biophys Res Commun 248 (3), 879-888 (1998)
   PUBMED   9704021
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007621.34, AC007537.3 and
            KF455603.1.
            
            Summary: This gene encodes a member of the low density lipoprotein
            (LDL) receptor gene family. LDL receptors are transmembrane cell
            surface proteins involved in receptor-mediated endocytosis of
            lipoprotein and protein ligands. The protein encoded by this gene
            functions as a receptor or, with Frizzled, a co-receptor for Wnt
            and thereby transmits the canonical Wnt/beta-catenin signaling
            cascade. Through its interaction with the Wnt/beta-catenin
            signaling cascade this gene plays a role in the regulation of cell
            differentiation, proliferation, and migration and the development
            of many cancer types. This protein undergoes gamma-secretase
            dependent RIP- (regulated intramembrane proteolysis) processing but
            the precise locations of the cleavage sites have not been
            determined.[provided by RefSeq, Dec 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143725.1, SRR14038197.929948.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1568
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..1568
                     /product="low-density lipoprotein receptor-related protein
                     6 isoform c"
                     /note="low-density lipoprotein receptor-related protein 6;
                     LRP-6"
                     /calculated_mol_wt=175306
     Region          1..204
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          89..127
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          150..191
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          175..216
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          217..251
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          286..323
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          353..393
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          397..437
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          458..499
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          483..524
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          525..558
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          592..627
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          <654..813
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          697..739
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          827..866
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          893..929
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          958..998
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          <968..1075
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Region          1094..1136
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1207..1243
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1243..1277
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1248,1256,1267..1268)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1260,1263,1267,1273..1274)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1270..1274
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1281..1315
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1286,1294,1305..1306)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1298,1301,1305,1311..1312)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1308..1312
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     CDS             1..1568
                     /gene="LRP6"
                     /gene_synonym="ADCAD2; EVR8; OPTA4; STHAG7"
                     /coded_by="NM_001414246.1:310..5016"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="GeneID:4040"
                     /db_xref="HGNC:HGNC:6698"
                     /db_xref="MIM:603507"
ORIGIN      
        1 mgavlrslla csfcvllraa plllyanrrd lrlvdatngk enativvggl edaaavdfvf
       61 shgliywsdv seeaikrtef nktesvqnvv vsgllspdgl acdwlgekly wtdsetnrie
      121 vsnldgslrk vlfwqeldqp raialdpssg fmywtdwgev pkieragmdg ssrfiiinse
      181 iywpngltld yeeqklywad aklnfihksn ldgtnrqavv kgslphpfal tlfedilywt
      241 dwsthsilac nkytgeglre ihsdifspmd ihafsqqrqp natnpcgidn ggcshlclms
      301 pvkpfyqcac ptgvklleng ktckdgatel lllarrtdlr risldtpdft divlqledir
      361 haiaidydpv egyiywtdde vrairrsfid gsgsqfvvta qiahpdgiav dwvarnlywt
      421 dtgtdrievt rlngtmrkil isedleepra ivldpmvgym ywtdwgeipk ieraaldgsd
      481 rvvlvntslg wpnglaldyd egkiywgdak tdkievmntd gtgrrvlved kiphifgftl
      541 lgdyvywtdw qrrsiervhk rsaereviid qlpdlmglka tnvhrvigsn pcaeenggcs
      601 hlclyrpqgl rcacpigfel isdmktcivp eafllfsrra dirrisletn nnnvaipltg
      661 vkeasaldfd vtdnriywtd islktisraf mngsalehvv efgldypegm avdwlgknly
      721 wadtgtnrie vskldgqhrq vlvwkdldsp ralaldpaeg fmywtewggk pkidraamdg
      781 serttlvpnv grangltidy akrrlywtdl dtnliessnm lglnreviad dlphpfgltq
      841 yqdyiywtdw srrsierank tsgqnrtiiq ghldyvmdil vfhssrqsgw necassnghc
      901 shlclavpvg gfvcgcpahy slnadnrtcs apttfllfsq ksainrmvid eqqspdiilp
      961 ihslrnvrai dydpldkqly widsrqnmir kaqedgsqgf tvvvssvpsq nleiqpydls
     1021 idiysryiyw tceatnvinv trldgrsvgv vlkgeqdrpr avvvnpekgy myftnlqers
     1081 pkieraaldg terevlffsg lskpialald srlgklfwad sdlrriessd lsganrivle
     1141 dsnilqpvgl tvfenwlywi dkqqqmieki dmtgregrtk vqariaqlsd ihavkelnlq
     1201 eyrqhpcaqd nggcshiclv kgdgttrcsc pmhlvllqde lscgesqfqc asgqcidgal
     1261 rcngdancqd ksdekncevl clidqfrcan gqcigkhkkc dhnvdcsdks deldcyptee
     1321 papqatntvg svigvivtif vsgtvyficq rmlcprmkgd getmtndyvv hgpasvplgy
     1381 vphpsslsgs lpgmsrgksm isslsimggs sgppydrahv tgasssssss tkgtyfpail
     1441 npppspater shytmefgys snspsthrsy syrpysyrhf appttpcstd vcdsdyapsr
     1501 rmtsvatakg ytsdlnydse pvpppptprs qylsaeenye scppspyter syshhlyppp
     1561 pspctdss
//
LOCUS       NP_001350820             515 aa            linear   PRI 21-DEC-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase FTO isoform 2 [Homo
            sapiens].
ACCESSION   NP_001350820 XP_011521615
VERSION     NP_001350820.1
DBSOURCE    REFSEQ: accession NM_001363891.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Li,B., Wang,L., Du,M. and He,H.
  TITLE     FTO in oral diseases: Functions, mechanisms, and therapeutic
            potential
  JOURNAL   FASEB J 38 (20), e70115 (2024)
   PUBMED   39436191
  REMARK    GeneRIF: FTO in oral diseases: Functions, mechanisms, and
            therapeutic potential.
            Review article
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Li,Q. and Mu,S.
  TITLE     FTO mediates the diabetic kidney disease progression through
            regulating the m6A modification of NLRP3
  JOURNAL   BMC Nephrol 25 (1), 345 (2024)
   PUBMED   39390397
  REMARK    GeneRIF: FTO mediates the diabetic kidney disease progression
            through regulating the m[6]A modification of NLRP3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Shan,L., Tao,M., Zhang,W., Zhao,J.D., Liu,X.C., Fang,Z.H. and
            Gao,J.R.
  TITLE     Comprehensive analysis of the m6A demethylase FTO in endothelial
            dysfunction by MeRIP sequencing
  JOURNAL   Exp Cell Res 442 (2), 114268 (2024)
   PUBMED   39343042
  REMARK    GeneRIF: Comprehensive analysis of the m[6]A demethylase FTO in
            endothelial dysfunction by MeRIP sequencing.
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Nabeel-Shah,S., Pu,S., Burke,G.L., Ahmed,N., Braunschweig,U.,
            Farhangmehr,S., Lee,H., Wu,M., Ni,Z., Tang,H., Zhong,G., Marcon,E.,
            Zhang,Z., Blencowe,B.J. and Greenblatt,J.F.
  TITLE     Recruitment of the m6A/m6Am demethylase FTO to target RNAs by the
            telomeric zinc finger protein ZBTB48
  JOURNAL   Genome Biol 25 (1), 246 (2024)
   PUBMED   39300486
  REMARK    GeneRIF: Recruitment of the m[6]A/m6Am demethylase FTO to target
            RNAs by the telomeric zinc finger protein ZBTB48.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 515)
  AUTHORS   Hussain,M., Waheed,A., Elahi,A. and Mustafa,G.
  TITLE     Fat Mass and Obesity-Related (FTO) Gene Variant Is a Predictor of
            CVD in T2DM Patients
  JOURNAL   J Diabetes Res 2024, 5914316 (2024)
   PUBMED   39257882
  REMARK    GeneRIF: Fat Mass and Obesity-Related (FTO) Gene Variant Is a
            Predictor of CVD in T2DM Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 515)
  AUTHORS   Zeggini,E., Weedon,M.N., Lindgren,C.M., Frayling,T.M.,
            Elliott,K.S., Lango,H., Timpson,N.J., Perry,J.R., Rayner,N.W.,
            Freathy,R.M., Barrett,J.C., Shields,B., Morris,A.P., Ellard,S.,
            Groves,C.J., Harries,L.W., Marchini,J.L., Owen,K.R., Knight,B.,
            Cardon,L.R., Walker,M., Hitman,G.A., Morris,A.D., Doney,A.S.,
            McCarthy,M.I. and Hattersley,A.T.
  CONSRTM   Wellcome Trust Case Control Consortium (WTCCC)
  TITLE     Replication of genome-wide association signals in UK samples
            reveals risk loci for type 2 diabetes
  JOURNAL   Science 316 (5829), 1336-1341 (2007)
   PUBMED   17463249
  REMARK    Erratum:[Science. 2007 Aug 24;317(5841):1035-6]
REFERENCE   7  (residues 1 to 515)
  AUTHORS   Scott,L.J., Mohlke,K.L., Bonnycastle,L.L., Willer,C.J., Li,Y.,
            Duren,W.L., Erdos,M.R., Stringham,H.M., Chines,P.S., Jackson,A.U.,
            Prokunina-Olsson,L., Ding,C.J., Swift,A.J., Narisu,N., Hu,T.,
            Pruim,R., Xiao,R., Li,X.Y., Conneely,K.N., Riebow,N.L., Sprau,A.G.,
            Tong,M., White,P.P., Hetrick,K.N., Barnhart,M.W., Bark,C.W.,
            Goldstein,J.L., Watkins,L., Xiang,F., Saramies,J., Buchanan,T.A.,
            Watanabe,R.M., Valle,T.T., Kinnunen,L., Abecasis,G.R., Pugh,E.W.,
            Doheny,K.F., Bergman,R.N., Tuomilehto,J., Collins,F.S. and
            Boehnke,M.
  TITLE     A genome-wide association study of type 2 diabetes in Finns detects
            multiple susceptibility variants
  JOURNAL   Science 316 (5829), 1341-1345 (2007)
   PUBMED   17463248
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 515)
  AUTHORS   Dina,C., Meyre,D., Gallina,S., Durand,E., Korner,A., Jacobson,P.,
            Carlsson,L.M., Kiess,W., Vatin,V., Lecoeur,C., Delplanque,J.,
            Vaillant,E., Pattou,F., Ruiz,J., Weill,J., Levy-Marchal,C.,
            Horber,F., Potoczna,N., Hercberg,S., Le Stunff,C., Bougneres,P.,
            Kovacs,P., Marre,M., Balkau,B., Cauchi,S., Chevre,J.C. and
            Froguel,P.
  TITLE     Variation in FTO contributes to childhood obesity and severe adult
            obesity
  JOURNAL   Nat Genet 39 (6), 724-726 (2007)
   PUBMED   17496892
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            GeneRIF: Association with obesity in adult and childre.
            Interestingly, this association receives clear confirmation under a
            Transmission Disequilibrium Test design which is robust to
            population stratification.
REFERENCE   9  (residues 1 to 515)
  AUTHORS   Frayling,T.M., Timpson,N.J., Weedon,M.N., Zeggini,E., Freathy,R.M.,
            Lindgren,C.M., Perry,J.R., Elliott,K.S., Lango,H., Rayner,N.W.,
            Shields,B., Harries,L.W., Barrett,J.C., Ellard,S., Groves,C.J.,
            Knight,B., Patch,A.M., Ness,A.R., Ebrahim,S., Lawlor,D.A.,
            Ring,S.M., Ben-Shlomo,Y., Jarvelin,M.R., Sovio,U., Bennett,A.J.,
            Melzer,D., Ferrucci,L., Loos,R.J., Barroso,I., Wareham,N.J.,
            Karpe,F., Owen,K.R., Cardon,L.R., Walker,M., Hitman,G.A.,
            Palmer,C.N., Doney,A.S., Morris,A.D., Smith,G.D., Hattersley,A.T.
            and McCarthy,M.I.
  TITLE     A common variant in the FTO gene is associated with body mass index
            and predisposes to childhood and adult obesity
  JOURNAL   Science 316 (5826), 889-894 (2007)
   PUBMED   17434869
  REMARK    GeneRIF: A genome-wide search for type 2 diabetes-susceptibility
            genes identified a common variant in the FTO gene that predisposes
            to diabetes through an effect on body mass index
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-environment interaction. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 515)
  AUTHORS   Peters,T., Ausmeier,K. and Ruther,U.
  TITLE     Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft)
            mouse mutation
  JOURNAL   Mamm Genome 10 (10), 983-986 (1999)
   PUBMED   10501967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007909.8, AC007496.6 and
            AC007347.3.
            
            On Jun 3, 2018 this sequence version replaced XP_011521615.1.
            
            Summary: This gene is a nuclear protein of the AlkB related
            non-haem iron and 2-oxoglutarate-dependent oxygenase superfamily
            but the exact physiological function of this gene is not known.
            Other non-heme iron enzymes function to reverse alkylated DNA and
            RNA damage by oxidative demethylation. Studies in mice and humans
            indicate a role in nervous and cardiovascular systems and a strong
            association with body mass index, obesity risk, and type 2
            diabetes. [provided by RefSeq, Jul 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853564.10771.1,
                                           SRR11853566.10305.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..515
                     /product="alpha-ketoglutarate-dependent dioxygenase FTO
                     isoform 2"
                     /EC_number="1.14.11.53"
                     /note="alpha-ketoglutarate-dependent dioxygenase FTO; fat
                     mass and obesity-associated protein; AlkB homolog 9; fat
                     mass and obesity associated; m6A(m)-demethylase FTO; tRNA
                     N1-methyl adenine demethylase FTO; mRNA
                     N(6)-methyladenosine demethylase FTO; mRNA
                     (2'-O-methyladenosine-N(6)-)-demethylase FTO; U6 small
                     nuclear RNA N(6)-methyladenosine-demethylase FTO; U6 small
                     nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO;
                     intragenic FTO exon 9 containing transcript; mRNA
                     N(6)-methyladenine demethylase"
                     /calculated_mol_wt=59313
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          36..335
                     /region_name="FTO_NTD"
                     /note="FTO catalytic domain; pfam12933"
                     /db_xref="CDD:463755"
     Region          213..224
                     /region_name="Loop L1, predicted to block binding of
                     double-stranded DNA or RNA.
                     /evidence=ECO:0000269|PubMed:20376003"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Site            216
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          339..508
                     /region_name="FTO_CTD"
                     /note="FTO C-terminal domain; pfam12934"
                     /db_xref="CDD:432887"
     CDS             1..515
                     /gene="FTO"
                     /gene_synonym="ALKBH9; BMIQ14; GDFD; IFEX9"
                     /coded_by="NM_001363891.2:30..1577"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:79068"
                     /db_xref="HGNC:HGNC:24678"
                     /db_xref="MIM:610966"
ORIGIN      
        1 mkrtptaeer ereakklrll eeledtwlpy ltpkddefyq qwqlkypkli lreassvsee
       61 lhkevqeafl tlhkhgclfr dlvriqgkdl ltpvsrilig npgctykyln trlftvpwpv
      121 kgsnikhtea eiaaacetfl klndylqiet iqaleelaak ekanedavpl cmsadfprvg
      181 mgssyngqde vdiksraayn vtllnfmdpq kmpylkeepy fgmgkmavsw hhdenlvdrs
      241 avavysysce gtvcswkkqp cpeeesedds hlegrdpdiw hvgfkiswdi etpglaiplh
      301 qgdcyfmldd lnathqhcvl agsqprfsst hrvaecstgt ldyilqrcql alqnvcddvd
      361 nddvslksfe pavlkqgeei hnevefewlr qfwfqgnryr kctdwwcqpm aqlealwkkm
      421 egvtnavlhe vkreglpveq rneiltaila sltarqnlrr ewharcqsri artlpadqkp
      481 ecrpywekdd asmplpfdlt divselrgql leakp
//
LOCUS       NP_001139588            1567 aa            linear   PRI 21-DEC-2025
DEFINITION  disco-interacting protein 2 homolog A isoform g [Homo sapiens].
ACCESSION   NP_001139588
VERSION     NP_001139588.1
DBSOURCE    REFSEQ: accession NM_001146116.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1567)
  AUTHORS   Zhang,B., Zhang,X., Omorou,M., Zhao,K., Ruan,Y. and Luan,H.
  TITLE     Disco interacting protein 2 homolog A (DIP2A): A key component in
            the regulation of brain disorders
  JOURNAL   Biomed Pharmacother 168, 115771 (2023)
   PUBMED   37897975
  REMARK    GeneRIF: Disco interacting protein 2 homolog A (DIP2A): A key
            component in the regulation of brain disorders.
            Review article
REFERENCE   2  (residues 1 to 1567)
  AUTHORS   Mondal,S., Kinatukara,P., Singh,S., Shambhavi,S., Patil,G.S.,
            Dubey,N., Singh,S.H., Pal,B., Shekar,P.C., Kamat,S.S. and
            Sankaranarayanan,R.
  TITLE     DIP2 is a unique regulator of diacylglycerol lipid homeostasis in
            eukaryotes
  JOURNAL   Elife 11, e77665 (2022)
   PUBMED   35766356
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1567)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 1567)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1567)
  AUTHORS   Ma,J., Zhang,L.Q., He,Z.X., He,X.X., Wang,Y.J., Jian,Y.L., Wang,X.,
            Zhang,B.B., Su,C., Lu,J., Huang,B.Q., Zhang,Y., Wang,G.Y.,
            Guo,W.X., Qiu,D.L., Mei,L., Xiong,W.C., Zheng,Y.W. and Zhu,X.J.
  TITLE     Autism candidate gene DIP2A regulates spine morphogenesis via
            acetylation of cortactin
  JOURNAL   PLoS Biol 17 (10), e3000461 (2019)
   PUBMED   31600191
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1567)
  AUTHORS   Winnepenninckx,B., Debacker,K., Ramsay,J., Smeets,D., Smits,A.,
            FitzPatrick,D.R. and Kooy,R.F.
  TITLE     CGG-repeat expansion in the DIP2B gene is associated with the
            fragile site FRA12A on chromosome 12q13.1
  JOURNAL   Am J Hum Genet 80 (2), 221-231 (2007)
   PUBMED   17236128
REFERENCE   7  (residues 1 to 1567)
  AUTHORS   Casadei,R., Strippoli,P., D'Addabbo,P., Canaider,S., Lenzi,L.,
            Vitale,L., Giannone,S., Frabetti,F., Facchin,F., Carinci,P. and
            Zannotti,M.
  TITLE     mRNA 5' region sequence incompleteness: a potential source of
            systematic errors in translation initiation codon assignment in
            human mRNAs
  JOURNAL   Gene 321, 185-193 (2003)
   PUBMED   14637006
REFERENCE   8  (residues 1 to 1567)
  AUTHORS   Mukhopadhyay,M., Pelka,P., DeSousa,D., Kablar,B., Schindler,A.,
            Rudnicki,M.A. and Campos,A.R.
  TITLE     Cloning, genomic organization and expression pattern of a novel
            Drosophila gene, the disco-interacting protein 2 (dip2), and its
            murine homolog
  JOURNAL   Gene 293 (1-2), 59-65 (2002)
   PUBMED   12137943
REFERENCE   9  (residues 1 to 1567)
  AUTHORS   Gardiner,K., Slavov,D., Bechtel,L. and Davisson,M.
  TITLE     Annotation of human chromosome 21 for relevance to Down syndrome:
            gene structure and expression analysis
  JOURNAL   Genomics 79 (6), 833-843 (2002)
   PUBMED   12036298
REFERENCE   10 (residues 1 to 1567)
  AUTHORS   Wang,Z., Tseng,C.P., Pong,R.C., Chen,H., McConnell,J.D., Navone,N.
            and Hsieh,J.T.
  TITLE     The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate
            cancer. Characterization of a novel GTPase-activating protein
            associated with N-terminal domain of DOC-2/DAB2
  JOURNAL   J Biol Chem 277 (15), 12622-12631 (2002)
   PUBMED   11812785
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000337.1, DA326960.1,
            AF490768.1, AB273729.1 and AP000338.3.
            
            Summary: The protein encoded by this gene may be involved in axon
            patterning in the central nervous system. This gene is not highly
            expressed. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (7) uses an alternate in-frame
            splice junction at the 5' end of an exon compared to variant 1. The
            resulting isoform (g) has the same N- and C-termini but is 4 aa
            shorter compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF490768.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1567
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..1567
                     /product="disco-interacting protein 2 homolog A isoform g"
                     /EC_number="6.2.1.1"
                     /note="disco-interacting protein 2A; DIP2 homolog A; DIP2
                     disco-interacting protein 2 homolog A; disconnected
                     interacting protein 2 homolog A; disco interacting protein
                     2 homolog A"
                     /calculated_mol_wt=169787
     Region          10..123
                     /region_name="DMAP_binding"
                     /note="DMAP1-binding Domain; pfam06464"
                     /db_xref="CDD:368923"
     Region          60..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT5; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Region          283..286
                     /region_name="PXXP motif, required for interaction with
                     CTTN. /evidence=ECO:0000250|UniProtKB:Q8BWT5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          303..306
                     /region_name="PXXP motif, required for interaction with
                     CTTN. /evidence=ECO:0000250|UniProtKB:Q8BWT5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          347..923
                     /region_name="Dip2"
                     /note="Disco-interacting protein 2 (Dip2); cd05905"
                     /db_xref="CDD:341231"
     Site            order(508,511..516,518..519)
                     /site_type="other"
                     /note="putative acyl-activating enzyme (AAE) consensus
                     motif"
                     /db_xref="CDD:341231"
     Site            order(511,631..632,690..695,788,800,803,814,903)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Site            order(511,552..553,603,605..606,609,631..632,650..655,788,
                     800,803,811..814,884)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341231"
     Site            order(552,605..606,609,631,811..813,871,884)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Region          999..1563
                     /region_name="Dip2"
                     /note="Disco-interacting protein 2 (Dip2); cd05905"
                     /db_xref="CDD:341231"
     Site            order(1148,1151..1156,1158..1159)
                     /site_type="other"
                     /note="putative acyl-activating enzyme (AAE) consensus
                     motif"
                     /db_xref="CDD:341231"
     Site            order(1151,1277..1278,1332..1337,1428,1450,1453,1464,1543)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Site            order(1151,1192..1193,1243,1245..1246,1249,1277..1278,
                     1295..1300,1428,1450,1453,1461..1464,1524)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341231"
     Site            order(1192,1245..1246,1249,1277,1461..1463,1511,1524)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341231"
     CDS             1..1567
                     /gene="DIP2A"
                     /gene_synonym="C21orf106; DIP2"
                     /coded_by="NM_001146116.2:242..4945"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS54490.1"
                     /db_xref="GeneID:23181"
                     /db_xref="HGNC:HGNC:17217"
                     /db_xref="MIM:607711"
ORIGIN      
        1 madrgcplea aplpaevres laelelelse gditqkgyek krakllaryi pliqgidpsl
       61 qaenripgps qttaaapkqq ksrptasrde rfrsdvhtea vqaalakyke rkmpmpskrr
      121 svlvhssvet ytppdtssas edegslrrpg rltstplqsh ssvepwldrv iqgsstsssa
      181 sstsshpggr pttapsaaat pgaaattala gleahthidl hsappdvttg lvehsyferp
      241 qvasvrsvpr gcsgsmleta dgvpvnsrvs skiqqllntl krpkrpplke ffvddfeell
      301 edpnqpkpeg setsvlrgep ltagvprpps llatlqrwgt tqpkspclta ldttgkavyt
      361 ltygklwsrs lklaytllnk ltsknepllk pgdrvalvfp nsdpvmfmva fygcllaelv
      421 pvpievpltr kdagsqqvgf llgscgvfla lttdacqkgl pkaqtgevaa fkgwpplswl
      481 vidgkhlakp pkdwhplaqd tgtgtayiey ktskegstvg vtvshaslla qcraltqacg
      541 yseaetltnv ldfkrdaglw hgvltsvmnr mhvvsvpyal mkanplswiq kvcfykaraa
      601 lvksrdmhws llaqrgqrdv slsslrmliv adganpwsis scdaflnvfq srglrpevic
      661 pcasspealt vairrppdlg gppprkavls mnglsygvir vdteeklsvl tvqdvgqvmp
      721 ganvcvvkle gtpylcktde vgeicvsssa tgtayygllg itknvfeavp vttggapifd
      781 rpftrtgllg figpdnlvfi vgkldglmvt gvrrhnaddv vatalavepm kfvyrgriav
      841 fsvtvlhddr ivlvaeqrpd aseedsfqwm srvlqaidsi hqvgvyclal vpantlpkap
      901 lggihisetk qrflegtlhp cnvlmcphtc vtnlpkprqk qpevgpasmi vgnlvagkri
      961 aqasgrelah ledsdqarkf lfladvlqwr ahttpdhplf lllnakgtvt statcvqlhk
     1021 raervaaalm ekgrlsvgdh valvyppgvd liaafygcly cgcvpvtvrp phpqnlgttl
     1081 ptvkmivevs ksacvlttqa vtrllrskea aaavdirtwp tildtddipk kkiasvfrpp
     1141 spdvlayldf svsttgilag vkmshaatsa lcrsiklqce lypsrqiaic ldpycglgfa
     1201 lwclcsvysg hqsvlvpple lesnvslwls avsqykarvt fcsysvmemc tkglgaqtgv
     1261 lrmkgvnlsc vrtcmvvaee rprialtqsf sklfkdlglp aravsttfgc rvnvaiclqg
     1321 tagpdpttvy vdmralrhdr vrlvergsph slplmesgki lpgvkviiah tetkgplgds
     1381 hlgeiwvssp hnatgyytvy geealhadhf sarlsfgdtq tiwartgylg flrrteltda
     1441 sggrhdalyv vgsldetlel rgmryhpidi etsvirahrs iaecavftwt nllvvvveld
     1501 gleqdaldlv alvtnvvlee hylvvgvvvi vdpgvipins rgekqrmhlr dgfladqldp
     1561 iyvaynm
//
LOCUS       NP_001397680            1581 aa            linear   PRI 21-DEC-2025
DEFINITION  disco-interacting protein 2 homolog A isoform j [Homo sapiens].
ACCESSION   NP_001397680 XP_047296665
VERSION     NP_001397680.1
DBSOURCE    REFSEQ: accession NM_001410751.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1581)
  AUTHORS   Zhang,B., Zhang,X., Omorou,M., Zhao,K., Ruan,Y. and Luan,H.
  TITLE     Disco interacting protein 2 homolog A (DIP2A): A key component in
            the regulation of brain disorders
  JOURNAL   Biomed Pharmacother 168, 115771 (2023)
   PUBMED   37897975
  REMARK    GeneRIF: Disco interacting protein 2 homolog A (DIP2A): A key
            component in the regulation of brain disorders.
            Review article
REFERENCE   2  (residues 1 to 1581)
  AUTHORS   Mondal,S., Kinatukara,P., Singh,S., Shambhavi,S., Patil,G.S.,
            Dubey,N., Singh,S.H., Pal,B., Shekar,P.C., Kamat,S.S. and
            Sankaranarayanan,R.
  TITLE     DIP2 is a unique regulator of diacylglycerol lipid homeostasis in
            eukaryotes
  JOURNAL   Elife 11, e77665 (2022)
   PUBMED   35766356
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1581)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 1581)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1581)
  AUTHORS   Ma,J., Zhang,L.Q., He,Z.X., He,X.X., Wang,Y.J., Jian,Y.L., Wang,X.,
            Zhang,B.B., Su,C., Lu,J., Huang,B.Q., Zhang,Y., Wang,G.Y.,
            Guo,W.X., Qiu,D.L., Mei,L., Xiong,W.C., Zheng,Y.W. and Zhu,X.J.
  TITLE     Autism candidate gene DIP2A regulates spine morphogenesis via
            acetylation of cortactin
  JOURNAL   PLoS Biol 17 (10), e3000461 (2019)
   PUBMED   31600191
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1581)
  AUTHORS   Winnepenninckx,B., Debacker,K., Ramsay,J., Smeets,D., Smits,A.,
            FitzPatrick,D.R. and Kooy,R.F.
  TITLE     CGG-repeat expansion in the DIP2B gene is associated with the
            fragile site FRA12A on chromosome 12q13.1
  JOURNAL   Am J Hum Genet 80 (2), 221-231 (2007)
   PUBMED   17236128
REFERENCE   7  (residues 1 to 1581)
  AUTHORS   Casadei,R., Strippoli,P., D'Addabbo,P., Canaider,S., Lenzi,L.,
            Vitale,L., Giannone,S., Frabetti,F., Facchin,F., Carinci,P. and
            Zannotti,M.
  TITLE     mRNA 5' region sequence incompleteness: a potential source of
            systematic errors in translation initiation codon assignment in
            human mRNAs
  JOURNAL   Gene 321, 185-193 (2003)
   PUBMED   14637006
REFERENCE   8  (residues 1 to 1581)
  AUTHORS   Mukhopadhyay,M., Pelka,P., DeSousa,D., Kablar,B., Schindler,A.,
            Rudnicki,M.A. and Campos,A.R.
  TITLE     Cloning, genomic organization and expression pattern of a novel
            Drosophila gene, the disco-interacting protein 2 (dip2), and its
            murine homolog
  JOURNAL   Gene 293 (1-2), 59-65 (2002)
   PUBMED   12137943
REFERENCE   9  (residues 1 to 1581)
  AUTHORS   Gardiner,K., Slavov,D., Bechtel,L. and Davisson,M.
  TITLE     Annotation of human chromosome 21 for relevance to Down syndrome:
            gene structure and expression analysis
  JOURNAL   Genomics 79 (6), 833-843 (2002)
   PUBMED   12036298
REFERENCE   10 (residues 1 to 1581)
  AUTHORS   Wang,Z., Tseng,C.P., Pong,R.C., Chen,H., McConnell,J.D., Navone,N.
            and Hsieh,J.T.
  TITLE     The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate
            cancer. Characterization of a novel GTPase-activating protein
            associated with N-terminal domain of DOC-2/DAB2
  JOURNAL   J Biol Chem 277 (15), 12622-12631 (2002)
   PUBMED   11812785
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000337.1 and AP000338.3.
            
            On Aug 15, 2022 this sequence version replaced XP_047296665.1.
            
            Summary: The protein encoded by this gene may be involved in axon
            patterning in the central nervous system. This gene is not highly
            expressed. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Mar 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.112155.1,
                                           SRR1803613.286940.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1581
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..1581
                     /product="disco-interacting protein 2 homolog A isoform j"
                     /EC_number="6.2.1.1"
                     /note="disco-interacting protein 2A; DIP2 homolog A; DIP2
                     disco-interacting protein 2 homolog A; disconnected
                     interacting protein 2 homolog A; disco interacting protein
                     2 homolog A"
                     /calculated_mol_wt=171346
     Region          10..123
                     /region_name="DMAP_binding"
                     /note="DMAP1-binding Domain; pfam06464"
                     /db_xref="CDD:368923"
     Region          60..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT5; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Region          283..286
                     /region_name="PXXP motif, required for interaction with
                     CTTN. /evidence=ECO:0000250|UniProtKB:Q8BWT5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          302..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          307..310
                     /region_name="PXXP motif, required for interaction with
                     CTTN. /evidence=ECO:0000250|UniProtKB:Q8BWT5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          351..927
                     /region_name="Dip2"
                     /note="Disco-interacting protein 2 (Dip2); cd05905"
                     /db_xref="CDD:341231"
     Site            order(512,515..520,522..523)
                     /site_type="other"
                     /note="putative acyl-activating enzyme (AAE) consensus
                     motif"
                     /db_xref="CDD:341231"
     Site            order(515,635..636,694..699,792,804,807,818,907)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Site            order(515,556..557,607,609..610,613,635..636,654..659,792,
                     804,807,815..818,888)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341231"
     Site            order(556,609..610,613,635,815..817,875,888)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Region          1003..1577
                     /region_name="Dip2"
                     /note="Disco-interacting protein 2 (Dip2); cd05905"
                     /db_xref="CDD:341231"
     Site            order(1152,1155..1160,1162..1163)
                     /site_type="other"
                     /note="putative acyl-activating enzyme (AAE) consensus
                     motif"
                     /db_xref="CDD:341231"
     Site            order(1155,1281..1282,1346..1351,1442,1464,1467,1478,1557)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Site            order(1155,1196..1197,1247,1249..1250,1253,1281..1282,
                     1299..1304,1442,1464,1467,1475..1478,1538)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341231"
     Site            order(1196,1249..1250,1253,1281,1475..1477,1525,1538)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341231"
     CDS             1..1581
                     /gene="DIP2A"
                     /gene_synonym="C21orf106; DIP2"
                     /coded_by="NM_001410751.1:242..4987"
                     /note="isoform j is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS93110.1"
                     /db_xref="GeneID:23181"
                     /db_xref="HGNC:HGNC:17217"
                     /db_xref="MIM:607711"
ORIGIN      
        1 madrgcplea aplpaevres laelelelse gditqkgyek krakllaryi pliqgidpsl
       61 qaenripgps qttaaapkqq ksrptasrde rfrsdvhtea vqaalakyke rkmpmpskrr
      121 svlvhssvet ytppdtssas edegslrrpg rltstplqsh ssvepwldrv iqgsstsssa
      181 sstsshpggr pttapsaaat pgaaattala gleahthidl hsappdvttg lvehsyferp
      241 qvasvrsvpr gcsgsmleta dgvpvnsrvs skiqqllntl krpkrpplke ffvddfeell
      301 evqqpdpnqp kpegsetsvl rgepltagvp rppsllatlq rwgttqpksp cltaldttgk
      361 avytltygkl wsrslklayt llnkltskne pllkpgdrva lvfpnsdpvm fmvafygcll
      421 aelvpvpiev pltrkdagsq qvgfllgscg vflalttdac qkglpkaqtg evaafkgwpp
      481 lswlvidgkh lakppkdwhp laqdtgtgta yieyktskeg stvgvtvsha sllaqcralt
      541 qacgyseaet ltnvldfkrd aglwhgvlts vmnrmhvvsv pyalmkanpl swiqkvcfyk
      601 araalvksrd mhwsllaqrg qrdvslsslr mlivadganp wsisscdafl nvfqsrglrp
      661 evicpcassp ealtvairrp pdlggppprk avlsmnglsy gvirvdteek lsvltvqdvg
      721 qvmpganvcv vklegtpylc ktdevgeicv sssatgtayy gllgitknvf eavpvttgga
      781 pifdrpftrt gllgfigpdn lvfivgkldg lmvtgvrrhn addvvatala vepmkfvyrg
      841 riavfsvtvl hddrivlvae qrpdaseeds fqwmsrvlqa idsihqvgvy clalvpantl
      901 pkaplggihi setkqrfleg tlhpcnvlmc phtcvtnlpk prqkqpevgp asmivgnlva
      961 gkriaqasgr elahledsdq arkflfladv lqwrahttpd hplflllnak gtvtstatcv
     1021 qlhkraerva aalmekgrls vgdhvalvyp pgvdliaafy gclycgcvpv tvrpphpqnl
     1081 gttlptvkmi vevsksacvl ttqavtrllr skeaaaavdi rtwptildtd dipkkkiasv
     1141 frppspdvla yldfsvsttg ilagvkmsha atsalcrsik lqcelypsrq iaicldpycg
     1201 lgfalwclcs vysghqsvlv pplelesnvs lwlsavsqyk arvtfcsysv memctkglga
     1261 qtgvlrmkgv nlscvrtcmv vaeerprial tqsfsklfkd lglparavst tfgcrvnvai
     1321 clqpnrlgkl aeqgtagpdp ttvyvdmral rhdrvrlver gsphslplme sgkilpgvkv
     1381 iiahtetkgp lgdshlgeiw vssphnatgy ytvygeealh adhfsarlsf gdtqtiwart
     1441 gylgflrrte ltdasggrhd alyvvgslde tlelrgmryh pidietsvir ahrsiaecav
     1501 ftwtnllvvv veldgleqda ldlvalvtnv vleehylvvg vvvivdpgvi pinsrgekqr
     1561 mhlrdgflad qldpiyvayn m
//
LOCUS       NP_001401178            1527 aa            linear   PRI 21-DEC-2025
DEFINITION  low-density lipoprotein receptor-related protein 6 isoform f
            precursor [Homo sapiens].
ACCESSION   NP_001401178
VERSION     NP_001401178.1
DBSOURCE    REFSEQ: accession NM_001414249.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1527)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1527)
  AUTHORS   Zhong,S., Guo,Q., Chen,X., Luo,X., Long,Y., Chong,T., Ye,M., He,H.,
            Lu,A., Ao,K., Yin,M., Xu,A., Li,X., Hao,Y. and Guo,X.
  TITLE     The inhibition of YTHDF3/m6A/LRP6 reprograms fatty acid metabolism
            and suppresses lymph node metastasis in cervical cancer
  JOURNAL   Int J Biol Sci 20 (3), 916-936 (2024)
   PUBMED   38250152
  REMARK    GeneRIF: The inhibition of YTHDF3/m[6]A/LRP6 reprograms fatty acid
            metabolism and suppresses lymph node metastasis in cervical cancer.
            Erratum:[Int J Biol Sci. 2025 Jun 5;21(8):3825-3826. doi:
            10.7150/ijbs.115928. PMID: 40520018]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1527)
  AUTHORS   Li,J., Liu,Z., Ren,Y., Shao,H. and Li,S.
  TITLE     LRP5-/6 gene polymorphisms and its association with risk of
            abnormal bone mass in postmenopausal women
  JOURNAL   J Orthop Surg Res 18 (1), 369 (2023)
   PUBMED   37202775
  REMARK    GeneRIF: LRP5-/6 gene polymorphisms and its association with risk
            of abnormal bone mass in postmenopausal women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1527)
  AUTHORS   Hao,H., Liu,Q., Chen,J. and Zhou,H.
  TITLE     Overexpression of circRNAs LRP6 in gestational diabetes mellitus
            predicts foetal malformation and intrauterine death
  JOURNAL   Endocrinol Diabetes Nutr (Engl Ed) 70 (2), 124-129 (2023)
   PUBMED   36925229
  REMARK    GeneRIF: Overexpression of circRNAs LRP6 in gestational diabetes
            mellitus predicts foetal malformation and intrauterine death.
REFERENCE   5  (residues 1 to 1527)
  AUTHORS   Wang,J., Yang,H., Ma,X., Liu,J., Li,L., Chen,L. and Wei,F.
  TITLE     LRP6/filamentous-actin signaling facilitates osteogenic commitment
            in mechanically induced periodontal ligament stem cells
  JOURNAL   Cell Mol Biol Lett 28 (1), 7 (2023)
   PUBMED   36694134
  REMARK    GeneRIF: LRP6/filamentous-actin signaling facilitates osteogenic
            commitment in mechanically induced periodontal ligament stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1527)
  AUTHORS   Bafico,A., Liu,G., Yaniv,A., Gazit,A. and Aaronson,S.A.
  TITLE     Novel mechanism of Wnt signalling inhibition mediated by Dickkopf-1
            interaction with LRP6/Arrow
  JOURNAL   Nat Cell Biol 3 (7), 683-686 (2001)
   PUBMED   11433302
REFERENCE   7  (residues 1 to 1527)
  AUTHORS   Mao,B., Wu,W., Li,Y., Hoppe,D., Stannek,P., Glinka,A. and Niehrs,C.
  TITLE     LDL-receptor-related protein 6 is a receptor for Dickkopf proteins
  JOURNAL   Nature 411 (6835), 321-325 (2001)
   PUBMED   11357136
REFERENCE   8  (residues 1 to 1527)
  AUTHORS   Tamai,K., Semenov,M., Kato,Y., Spokony,R., Liu,C., Katsuyama,Y.,
            Hess,F., Saint-Jeannet,J.P. and He,X.
  TITLE     LDL-receptor-related proteins in Wnt signal transduction
  JOURNAL   Nature 407 (6803), 530-535 (2000)
   PUBMED   11029007
REFERENCE   9  (residues 1 to 1527)
  AUTHORS   Baens,M., Wlodarska,I., Corveleyn,A., Hoornaert,I., Hagemeijer,A.
            and Marynen,P.
  TITLE     A physical, transcript, and deletion map of chromosome region
            12p12.3 flanked by ETV6 and CDKN1B: hypermethylation of the LRP6
            CpG island in two leukemia patients with hemizygous del(12p)
  JOURNAL   Genomics 56 (1), 40-50 (1999)
   PUBMED   10036184
REFERENCE   10 (residues 1 to 1527)
  AUTHORS   Brown,S.D., Twells,R.C., Hey,P.J., Cox,R.D., Levy,E.R.,
            Soderman,A.R., Metzker,M.L., Caskey,C.T., Todd,J.A. and Hess,J.F.
  TITLE     Isolation and characterization of LRP6, a novel member of the low
            density lipoprotein receptor gene family
  JOURNAL   Biochem Biophys Res Commun 248 (3), 879-888 (1998)
   PUBMED   9704021
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007621.34, AC007537.3 and
            KF455603.1.
            
            Summary: This gene encodes a member of the low density lipoprotein
            (LDL) receptor gene family. LDL receptors are transmembrane cell
            surface proteins involved in receptor-mediated endocytosis of
            lipoprotein and protein ligands. The protein encoded by this gene
            functions as a receptor or, with Frizzled, a co-receptor for Wnt
            and thereby transmits the canonical Wnt/beta-catenin signaling
            cascade. Through its interaction with the Wnt/beta-catenin
            signaling cascade this gene plays a role in the regulation of cell
            differentiation, proliferation, and migration and the development
            of many cancer types. This protein undergoes gamma-secretase
            dependent RIP- (regulated intramembrane proteolysis) processing but
            the precise locations of the cleavage sites have not been
            determined.[provided by RefSeq, Dec 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3489343.1,
                                           SRR18074969.2911113.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1527
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..1527
                     /product="low-density lipoprotein receptor-related protein
                     6 isoform f precursor"
                     /note="low-density lipoprotein receptor-related protein 6;
                     LRP-6"
                     /calculated_mol_wt=168976
     Region          1..204
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
                     /calculated_mol_wt=2024
     Region          20..275
                     /region_name="Beta-propeller 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            42
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            81
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          89..127
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          150..191
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          175..216
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          217..251
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          237..276
                     /region_name="LDL-receptor class B 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          286..323
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          328..589
                     /region_name="Beta-propeller 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          353..393
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          397..437
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          458..499
                     /region_name="Ldl_recept_b"
                     /note="Low-density lipoprotein receptor repeat class B;
                     pfam00058"
                     /db_xref="CDD:459654"
     Region          483..524
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            486
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          525..558
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          592..627
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          631..890
                     /region_name="Beta-propeller 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          <654..813
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Site            692
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          697..739
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          827..866
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Site            859
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            865
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          893..929
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            926
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          933..1202
                     /region_name="Beta-propeller 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Region          958..998
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          <968..1075
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     Site            1039
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22000856; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          1094..1136
                     /region_name="LY"
                     /note="Low-density lipoprotein-receptor YWTD domain;
                     smart00135"
                     /db_xref="CDD:214531"
     Region          1207..1243
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          1249..1285
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1254,1264,1275..1276)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1268,1271,1275,1281..1282)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1278..1282
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1288..1322
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1293,1301,1312..1313)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1305,1308,1312,1318..1319)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1315..1319
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          1326..1360
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(1331,1339,1350..1351)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(1343,1346,1350,1356..1357)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            1353..1357
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Site            1371..1393
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            1420
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:16513652; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1430
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:16513652; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1479
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17569865; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Region          1487..1493
                     /region_name="PPPSP motif A"
                     /note="propagated from UniProtKB/Swiss-Prot (O75581.2)"
     Site            1490
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK14, GRK5 and GRK6.
                     /evidence=ECO:0000269|PubMed:16341017,
                     ECO:0000269|PubMed:17698587, ECO:0000269|PubMed:18762581,
                     ECO:0000269|PubMed:19801552, ECO:0000269|PubMed:20059949,
                     ECO:0000269|PubMed:25331957, ECO:0000269|PubMed:27821587,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     Site            1493
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK1.
                     /evidence=ECO:0000269|PubMed:16341017; propagated from
                     UniProtKB/Swiss-Prot (O75581.2)"
     CDS             1..1527
                     /gene="LRP6"
                     /gene_synonym="ADCAD2; EVR8; OPTA4; STHAG7"
                     /coded_by="NM_001414249.1:310..4893"
                     /note="isoform f precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:4040"
                     /db_xref="HGNC:HGNC:6698"
                     /db_xref="MIM:603507"
ORIGIN      
        1 mgavlrslla csfcvllraa plllyanrrd lrlvdatngk enativvggl edaaavdfvf
       61 shgliywsdv seeaikrtef nktesvqnvv vsgllspdgl acdwlgekly wtdsetnrie
      121 vsnldgslrk vlfwqeldqp raialdpssg fmywtdwgev pkieragmdg ssrfiiinse
      181 iywpngltld yeeqklywad aklnfihksn ldgtnrqavv kgslphpfal tlfedilywt
      241 dwsthsilac nkytgeglre ihsdifspmd ihafsqqrqp natnpcgidn ggcshlclms
      301 pvkpfyqcac ptgvklleng ktckdgatel lllarrtdlr risldtpdft divlqledir
      361 haiaidydpv egyiywtdde vrairrsfid gsgsqfvvta qiahpdgiav dwvarnlywt
      421 dtgtdrievt rlngtmrkil isedleepra ivldpmvgym ywtdwgeipk ieraaldgsd
      481 rvvlvntslg wpnglaldyd egkiywgdak tdkievmntd gtgrrvlved kiphifgftl
      541 lgdyvywtdw qrrsiervhk rsaereviid qlpdlmglka tnvhrvigsn pcaeenggcs
      601 hlclyrpqgl rcacpigfel isdmktcivp eafllfsrra dirrisletn nnnvaipltg
      661 vkeasaldfd vtdnriywtd islktisraf mngsalehvv efgldypegm avdwlgknly
      721 wadtgtnrie vskldgqhrq vlvwkdldsp ralaldpaeg fmywtewggk pkidraamdg
      781 serttlvpnv grangltidy akrrlywtdl dtnliessnm lglnreviad dlphpfgltq
      841 yqdyiywtdw srrsierank tsgqnrtiiq ghldyvmdil vfhssrqsgw necassnghc
      901 shlclavpvg gfvcgcpahy slnadnrtcs apttfllfsq ksainrmvid eqqspdiilp
      961 ihslrnvrai dydpldkqly widsrqnmir kaqedgsqgf tvvvssvpsq nleiqpydls
     1021 idiysryiyw tceatnvinv trldgrsvgv vlkgeqdrpr avvvnpekgy myftnlqers
     1081 pkieraaldg terevlffsg lskpialald srlgklfwad sdlrriessd lsganrivle
     1141 dsnilqpvgl tvfenwlywi dkqqqmieki dmtgregrtk vqariaqlsd ihavkelnlq
     1201 eyrqhpcaqd nggcshiclv kgdgttrcsc pmhlvllqde lscgepptcs pqqftcftge
     1261 idcipvawrc dgftecedhs delncpvcse sqfqcasgqc idgalrcngd ancqdksdek
     1321 ncevlclidq frcangqcig khkkcdhnvd csdksdeldc ypteepapqa tntvgsvigv
     1381 ivtifvsgtv yficqrmlcp rmkgdgetmt ndyvvhgpas vplgyvphps slsgslpgms
     1441 rgksmissls imggssgppy drahvtgass ssssstkgty fpailnppps patershytm
     1501 efgyssnsps thrsyrkpkq kkqkpen
//
LOCUS       NP_055966               1571 aa            linear   PRI 21-DEC-2025
DEFINITION  disco-interacting protein 2 homolog A isoform a [Homo sapiens].
ACCESSION   NP_055966
VERSION     NP_055966.2
DBSOURCE    REFSEQ: accession NM_015151.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1571)
  AUTHORS   Zhang,B., Zhang,X., Omorou,M., Zhao,K., Ruan,Y. and Luan,H.
  TITLE     Disco interacting protein 2 homolog A (DIP2A): A key component in
            the regulation of brain disorders
  JOURNAL   Biomed Pharmacother 168, 115771 (2023)
   PUBMED   37897975
  REMARK    GeneRIF: Disco interacting protein 2 homolog A (DIP2A): A key
            component in the regulation of brain disorders.
            Review article
REFERENCE   2  (residues 1 to 1571)
  AUTHORS   Mondal,S., Kinatukara,P., Singh,S., Shambhavi,S., Patil,G.S.,
            Dubey,N., Singh,S.H., Pal,B., Shekar,P.C., Kamat,S.S. and
            Sankaranarayanan,R.
  TITLE     DIP2 is a unique regulator of diacylglycerol lipid homeostasis in
            eukaryotes
  JOURNAL   Elife 11, e77665 (2022)
   PUBMED   35766356
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1571)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 1571)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1571)
  AUTHORS   Ma,J., Zhang,L.Q., He,Z.X., He,X.X., Wang,Y.J., Jian,Y.L., Wang,X.,
            Zhang,B.B., Su,C., Lu,J., Huang,B.Q., Zhang,Y., Wang,G.Y.,
            Guo,W.X., Qiu,D.L., Mei,L., Xiong,W.C., Zheng,Y.W. and Zhu,X.J.
  TITLE     Autism candidate gene DIP2A regulates spine morphogenesis via
            acetylation of cortactin
  JOURNAL   PLoS Biol 17 (10), e3000461 (2019)
   PUBMED   31600191
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1571)
  AUTHORS   Winnepenninckx,B., Debacker,K., Ramsay,J., Smeets,D., Smits,A.,
            FitzPatrick,D.R. and Kooy,R.F.
  TITLE     CGG-repeat expansion in the DIP2B gene is associated with the
            fragile site FRA12A on chromosome 12q13.1
  JOURNAL   Am J Hum Genet 80 (2), 221-231 (2007)
   PUBMED   17236128
REFERENCE   7  (residues 1 to 1571)
  AUTHORS   Casadei,R., Strippoli,P., D'Addabbo,P., Canaider,S., Lenzi,L.,
            Vitale,L., Giannone,S., Frabetti,F., Facchin,F., Carinci,P. and
            Zannotti,M.
  TITLE     mRNA 5' region sequence incompleteness: a potential source of
            systematic errors in translation initiation codon assignment in
            human mRNAs
  JOURNAL   Gene 321, 185-193 (2003)
   PUBMED   14637006
REFERENCE   8  (residues 1 to 1571)
  AUTHORS   Mukhopadhyay,M., Pelka,P., DeSousa,D., Kablar,B., Schindler,A.,
            Rudnicki,M.A. and Campos,A.R.
  TITLE     Cloning, genomic organization and expression pattern of a novel
            Drosophila gene, the disco-interacting protein 2 (dip2), and its
            murine homolog
  JOURNAL   Gene 293 (1-2), 59-65 (2002)
   PUBMED   12137943
REFERENCE   9  (residues 1 to 1571)
  AUTHORS   Gardiner,K., Slavov,D., Bechtel,L. and Davisson,M.
  TITLE     Annotation of human chromosome 21 for relevance to Down syndrome:
            gene structure and expression analysis
  JOURNAL   Genomics 79 (6), 833-843 (2002)
   PUBMED   12036298
REFERENCE   10 (residues 1 to 1571)
  AUTHORS   Wang,Z., Tseng,C.P., Pong,R.C., Chen,H., McConnell,J.D., Navone,N.
            and Hsieh,J.T.
  TITLE     The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate
            cancer. Characterization of a novel GTPase-activating protein
            associated with N-terminal domain of DOC-2/DAB2
  JOURNAL   J Biol Chem 277 (15), 12622-12631 (2002)
   PUBMED   11812785
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000337.1, DA326960.1,
            AB273729.1, AF490768.1 and AP000338.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 30, 2004 this sequence version replaced NP_055966.1.
            
            Summary: The protein encoded by this gene may be involved in axon
            patterning in the central nervous system. This gene is not highly
            expressed. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (1), as well as variant 9, encodes
            isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.140916.1, AB273729.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000417564.3/ ENSP00000392066.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1571
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..1571
                     /product="disco-interacting protein 2 homolog A isoform a"
                     /EC_number="6.2.1.1"
                     /note="disco-interacting protein 2A; DIP2 homolog A; DIP2
                     disco-interacting protein 2 homolog A; disconnected
                     interacting protein 2 homolog A; disco interacting protein
                     2 homolog A"
                     /calculated_mol_wt=170239
     Region          10..123
                     /region_name="DMAP_binding"
                     /note="DMAP1-binding Domain; pfam06464"
                     /db_xref="CDD:368923"
     Region          60..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWT5; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14689.2)"
     Region          283..286
                     /region_name="PXXP motif, required for interaction with
                     CTTN. /evidence=ECO:0000250|UniProtKB:Q8BWT5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          302..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          307..310
                     /region_name="PXXP motif, required for interaction with
                     CTTN. /evidence=ECO:0000250|UniProtKB:Q8BWT5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14689.2)"
     Region          351..927
                     /region_name="Dip2"
                     /note="Disco-interacting protein 2 (Dip2); cd05905"
                     /db_xref="CDD:341231"
     Site            order(512,515..520,522..523)
                     /site_type="other"
                     /note="putative acyl-activating enzyme (AAE) consensus
                     motif"
                     /db_xref="CDD:341231"
     Site            order(515,635..636,694..699,792,804,807,818,907)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Site            order(515,556..557,607,609..610,613,635..636,654..659,792,
                     804,807,815..818,888)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341231"
     Site            order(556,609..610,613,635,815..817,875,888)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Region          1003..1567
                     /region_name="Dip2"
                     /note="Disco-interacting protein 2 (Dip2); cd05905"
                     /db_xref="CDD:341231"
     Site            order(1152,1155..1160,1162..1163)
                     /site_type="other"
                     /note="putative acyl-activating enzyme (AAE) consensus
                     motif"
                     /db_xref="CDD:341231"
     Site            order(1155,1281..1282,1336..1341,1432,1454,1457,1468,1547)
                     /site_type="other"
                     /note="putative AMP binding site [chemical binding]"
                     /db_xref="CDD:341231"
     Site            order(1155,1196..1197,1247,1249..1250,1253,1281..1282,
                     1299..1304,1432,1454,1457,1465..1468,1528)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:341231"
     Site            order(1196,1249..1250,1253,1281,1465..1467,1515,1528)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:341231"
     CDS             1..1571
                     /gene="DIP2A"
                     /gene_synonym="C21orf106; DIP2"
                     /coded_by="NM_015151.4:242..4957"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46655.1"
                     /db_xref="GeneID:23181"
                     /db_xref="HGNC:HGNC:17217"
                     /db_xref="MIM:607711"
ORIGIN      
        1 madrgcplea aplpaevres laelelelse gditqkgyek krakllaryi pliqgidpsl
       61 qaenripgps qttaaapkqq ksrptasrde rfrsdvhtea vqaalakyke rkmpmpskrr
      121 svlvhssvet ytppdtssas edegslrrpg rltstplqsh ssvepwldrv iqgsstsssa
      181 sstsshpggr pttapsaaat pgaaattala gleahthidl hsappdvttg lvehsyferp
      241 qvasvrsvpr gcsgsmleta dgvpvnsrvs skiqqllntl krpkrpplke ffvddfeell
      301 evqqpdpnqp kpegsetsvl rgepltagvp rppsllatlq rwgttqpksp cltaldttgk
      361 avytltygkl wsrslklayt llnkltskne pllkpgdrva lvfpnsdpvm fmvafygcll
      421 aelvpvpiev pltrkdagsq qvgfllgscg vflalttdac qkglpkaqtg evaafkgwpp
      481 lswlvidgkh lakppkdwhp laqdtgtgta yieyktskeg stvgvtvsha sllaqcralt
      541 qacgyseaet ltnvldfkrd aglwhgvlts vmnrmhvvsv pyalmkanpl swiqkvcfyk
      601 araalvksrd mhwsllaqrg qrdvslsslr mlivadganp wsisscdafl nvfqsrglrp
      661 evicpcassp ealtvairrp pdlggppprk avlsmnglsy gvirvdteek lsvltvqdvg
      721 qvmpganvcv vklegtpylc ktdevgeicv sssatgtayy gllgitknvf eavpvttgga
      781 pifdrpftrt gllgfigpdn lvfivgkldg lmvtgvrrhn addvvatala vepmkfvyrg
      841 riavfsvtvl hddrivlvae qrpdaseeds fqwmsrvlqa idsihqvgvy clalvpantl
      901 pkaplggihi setkqrfleg tlhpcnvlmc phtcvtnlpk prqkqpevgp asmivgnlva
      961 gkriaqasgr elahledsdq arkflfladv lqwrahttpd hplflllnak gtvtstatcv
     1021 qlhkraerva aalmekgrls vgdhvalvyp pgvdliaafy gclycgcvpv tvrpphpqnl
     1081 gttlptvkmi vevsksacvl ttqavtrllr skeaaaavdi rtwptildtd dipkkkiasv
     1141 frppspdvla yldfsvsttg ilagvkmsha atsalcrsik lqcelypsrq iaicldpycg
     1201 lgfalwclcs vysghqsvlv pplelesnvs lwlsavsqyk arvtfcsysv memctkglga
     1261 qtgvlrmkgv nlscvrtcmv vaeerprial tqsfsklfkd lglparavst tfgcrvnvai
     1321 clqgtagpdp ttvyvdmral rhdrvrlver gsphslplme sgkilpgvkv iiahtetkgp
     1381 lgdshlgeiw vssphnatgy ytvygeealh adhfsarlsf gdtqtiwart gylgflrrte
     1441 ltdasggrhd alyvvgslde tlelrgmryh pidietsvir ahrsiaecav ftwtnllvvv
     1501 veldgleqda ldlvalvtnv vleehylvvg vvvivdpgvi pinsrgekqr mhlrdgflad
     1561 qldpiyvayn m
//
LOCUS       NP_001350832             424 aa            linear   PRI 21-DEC-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase FTO isoform 10 [Homo
            sapiens].
ACCESSION   NP_001350832
VERSION     NP_001350832.1
DBSOURCE    REFSEQ: accession NM_001363903.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Li,B., Wang,L., Du,M. and He,H.
  TITLE     FTO in oral diseases: Functions, mechanisms, and therapeutic
            potential
  JOURNAL   FASEB J 38 (20), e70115 (2024)
   PUBMED   39436191
  REMARK    GeneRIF: FTO in oral diseases: Functions, mechanisms, and
            therapeutic potential.
            Review article
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Li,Q. and Mu,S.
  TITLE     FTO mediates the diabetic kidney disease progression through
            regulating the m6A modification of NLRP3
  JOURNAL   BMC Nephrol 25 (1), 345 (2024)
   PUBMED   39390397
  REMARK    GeneRIF: FTO mediates the diabetic kidney disease progression
            through regulating the m[6]A modification of NLRP3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Shan,L., Tao,M., Zhang,W., Zhao,J.D., Liu,X.C., Fang,Z.H. and
            Gao,J.R.
  TITLE     Comprehensive analysis of the m6A demethylase FTO in endothelial
            dysfunction by MeRIP sequencing
  JOURNAL   Exp Cell Res 442 (2), 114268 (2024)
   PUBMED   39343042
  REMARK    GeneRIF: Comprehensive analysis of the m[6]A demethylase FTO in
            endothelial dysfunction by MeRIP sequencing.
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Nabeel-Shah,S., Pu,S., Burke,G.L., Ahmed,N., Braunschweig,U.,
            Farhangmehr,S., Lee,H., Wu,M., Ni,Z., Tang,H., Zhong,G., Marcon,E.,
            Zhang,Z., Blencowe,B.J. and Greenblatt,J.F.
  TITLE     Recruitment of the m6A/m6Am demethylase FTO to target RNAs by the
            telomeric zinc finger protein ZBTB48
  JOURNAL   Genome Biol 25 (1), 246 (2024)
   PUBMED   39300486
  REMARK    GeneRIF: Recruitment of the m[6]A/m6Am demethylase FTO to target
            RNAs by the telomeric zinc finger protein ZBTB48.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Hussain,M., Waheed,A., Elahi,A. and Mustafa,G.
  TITLE     Fat Mass and Obesity-Related (FTO) Gene Variant Is a Predictor of
            CVD in T2DM Patients
  JOURNAL   J Diabetes Res 2024, 5914316 (2024)
   PUBMED   39257882
  REMARK    GeneRIF: Fat Mass and Obesity-Related (FTO) Gene Variant Is a
            Predictor of CVD in T2DM Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Zeggini,E., Weedon,M.N., Lindgren,C.M., Frayling,T.M.,
            Elliott,K.S., Lango,H., Timpson,N.J., Perry,J.R., Rayner,N.W.,
            Freathy,R.M., Barrett,J.C., Shields,B., Morris,A.P., Ellard,S.,
            Groves,C.J., Harries,L.W., Marchini,J.L., Owen,K.R., Knight,B.,
            Cardon,L.R., Walker,M., Hitman,G.A., Morris,A.D., Doney,A.S.,
            McCarthy,M.I. and Hattersley,A.T.
  CONSRTM   Wellcome Trust Case Control Consortium (WTCCC)
  TITLE     Replication of genome-wide association signals in UK samples
            reveals risk loci for type 2 diabetes
  JOURNAL   Science 316 (5829), 1336-1341 (2007)
   PUBMED   17463249
  REMARK    Erratum:[Science. 2007 Aug 24;317(5841):1035-6]
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Scott,L.J., Mohlke,K.L., Bonnycastle,L.L., Willer,C.J., Li,Y.,
            Duren,W.L., Erdos,M.R., Stringham,H.M., Chines,P.S., Jackson,A.U.,
            Prokunina-Olsson,L., Ding,C.J., Swift,A.J., Narisu,N., Hu,T.,
            Pruim,R., Xiao,R., Li,X.Y., Conneely,K.N., Riebow,N.L., Sprau,A.G.,
            Tong,M., White,P.P., Hetrick,K.N., Barnhart,M.W., Bark,C.W.,
            Goldstein,J.L., Watkins,L., Xiang,F., Saramies,J., Buchanan,T.A.,
            Watanabe,R.M., Valle,T.T., Kinnunen,L., Abecasis,G.R., Pugh,E.W.,
            Doheny,K.F., Bergman,R.N., Tuomilehto,J., Collins,F.S. and
            Boehnke,M.
  TITLE     A genome-wide association study of type 2 diabetes in Finns detects
            multiple susceptibility variants
  JOURNAL   Science 316 (5829), 1341-1345 (2007)
   PUBMED   17463248
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 424)
  AUTHORS   Dina,C., Meyre,D., Gallina,S., Durand,E., Korner,A., Jacobson,P.,
            Carlsson,L.M., Kiess,W., Vatin,V., Lecoeur,C., Delplanque,J.,
            Vaillant,E., Pattou,F., Ruiz,J., Weill,J., Levy-Marchal,C.,
            Horber,F., Potoczna,N., Hercberg,S., Le Stunff,C., Bougneres,P.,
            Kovacs,P., Marre,M., Balkau,B., Cauchi,S., Chevre,J.C. and
            Froguel,P.
  TITLE     Variation in FTO contributes to childhood obesity and severe adult
            obesity
  JOURNAL   Nat Genet 39 (6), 724-726 (2007)
   PUBMED   17496892
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            GeneRIF: Association with obesity in adult and childre.
            Interestingly, this association receives clear confirmation under a
            Transmission Disequilibrium Test design which is robust to
            population stratification.
REFERENCE   9  (residues 1 to 424)
  AUTHORS   Frayling,T.M., Timpson,N.J., Weedon,M.N., Zeggini,E., Freathy,R.M.,
            Lindgren,C.M., Perry,J.R., Elliott,K.S., Lango,H., Rayner,N.W.,
            Shields,B., Harries,L.W., Barrett,J.C., Ellard,S., Groves,C.J.,
            Knight,B., Patch,A.M., Ness,A.R., Ebrahim,S., Lawlor,D.A.,
            Ring,S.M., Ben-Shlomo,Y., Jarvelin,M.R., Sovio,U., Bennett,A.J.,
            Melzer,D., Ferrucci,L., Loos,R.J., Barroso,I., Wareham,N.J.,
            Karpe,F., Owen,K.R., Cardon,L.R., Walker,M., Hitman,G.A.,
            Palmer,C.N., Doney,A.S., Morris,A.D., Smith,G.D., Hattersley,A.T.
            and McCarthy,M.I.
  TITLE     A common variant in the FTO gene is associated with body mass index
            and predisposes to childhood and adult obesity
  JOURNAL   Science 316 (5826), 889-894 (2007)
   PUBMED   17434869
  REMARK    GeneRIF: A genome-wide search for type 2 diabetes-susceptibility
            genes identified a common variant in the FTO gene that predisposes
            to diabetes through an effect on body mass index
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-environment interaction. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Peters,T., Ausmeier,K. and Ruther,U.
  TITLE     Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft)
            mouse mutation
  JOURNAL   Mamm Genome 10 (10), 983-986 (1999)
   PUBMED   10501967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007909.8, AC007496.6 and
            AC007347.3.
            
            Summary: This gene is a nuclear protein of the AlkB related
            non-haem iron and 2-oxoglutarate-dependent oxygenase superfamily
            but the exact physiological function of this gene is not known.
            Other non-heme iron enzymes function to reverse alkylated DNA and
            RNA damage by oxidative demethylation. Studies in mice and humans
            indicate a role in nervous and cardiovascular systems and a strong
            association with body mass index, obesity risk, and type 2
            diabetes. [provided by RefSeq, Jul 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.75736.1,
                                           SRR18074969.1371701.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..424
                     /product="alpha-ketoglutarate-dependent dioxygenase FTO
                     isoform 10"
                     /EC_number="1.14.11.53"
                     /note="alpha-ketoglutarate-dependent dioxygenase FTO; fat
                     mass and obesity-associated protein; AlkB homolog 9; fat
                     mass and obesity associated; m6A(m)-demethylase FTO; tRNA
                     N1-methyl adenine demethylase FTO; mRNA
                     N(6)-methyladenosine demethylase FTO; mRNA
                     (2'-O-methyladenosine-N(6)-)-demethylase FTO; U6 small
                     nuclear RNA N(6)-methyladenosine-demethylase FTO; U6 small
                     nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO;
                     intragenic FTO exon 9 containing transcript; mRNA
                     N(6)-methyladenine demethylase"
                     /calculated_mol_wt=48709
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          32..327
                     /region_name="Fe2OG dioxygenase domain.
                     /evidence=ECO:0000269|PubMed:20376003"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          36..325
                     /region_name="FTO_NTD"
                     /note="FTO catalytic domain; pfam12933"
                     /db_xref="CDD:463755"
     Region          213..224
                     /region_name="Loop L1, predicted to block binding of
                     double-stranded DNA or RNA.
                     /evidence=ECO:0000269|PubMed:20376003"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Site            216
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9C0B1.3)"
     Region          329..>411
                     /region_name="FTO_CTD"
                     /note="FTO C-terminal domain; pfam12934"
                     /db_xref="CDD:432887"
     CDS             1..424
                     /gene="FTO"
                     /gene_synonym="ALKBH9; BMIQ14; GDFD; IFEX9"
                     /coded_by="NM_001363903.2:30..1304"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:79068"
                     /db_xref="HGNC:HGNC:24678"
                     /db_xref="MIM:610966"
ORIGIN      
        1 mkrtptaeer ereakklrll eeledtwlpy ltpkddefyq qwqlkypkli lreassvsee
       61 lhkevqeafl tlhkhgclfr dlvriqgkdl ltpvsrilig npgctykyln trlftvpwpv
      121 kgsnikhtea eiaaacetfl klndylqiet iqaleelaak ekanedavpl cmsadfprvg
      181 mgssyngqde vdiksraayn vtllnfmdpq kmpylkeepy fgmgkmavsw hhdenlvdrs
      241 avavysysce gpeeesedds hlegrdpdiw hvgfkiswdi etpglaiplh qgdcyfmldd
      301 lnathqhcvl agsqprfsst hrvaecstgt ldyilqrcql alqnvcddvd nddvslksfe
      361 pavlkqgeei hnevefewlr qfwfqgnryr kctdwwcqpm aqlealwkkm egvvpvtncp
      421 nitc
//
LOCUS       NP_001350828             467 aa            linear   PRI 21-DEC-2025
DEFINITION  alpha-ketoglutarate-dependent dioxygenase FTO isoform 7 [Homo
            sapiens].
ACCESSION   NP_001350828
VERSION     NP_001350828.1
DBSOURCE    REFSEQ: accession NM_001363899.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Li,B., Wang,L., Du,M. and He,H.
  TITLE     FTO in oral diseases: Functions, mechanisms, and therapeutic
            potential
  JOURNAL   FASEB J 38 (20), e70115 (2024)
   PUBMED   39436191
  REMARK    GeneRIF: FTO in oral diseases: Functions, mechanisms, and
            therapeutic potential.
            Review article
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Li,Q. and Mu,S.
  TITLE     FTO mediates the diabetic kidney disease progression through
            regulating the m6A modification of NLRP3
  JOURNAL   BMC Nephrol 25 (1), 345 (2024)
   PUBMED   39390397
  REMARK    GeneRIF: FTO mediates the diabetic kidney disease progression
            through regulating the m[6]A modification of NLRP3.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Shan,L., Tao,M., Zhang,W., Zhao,J.D., Liu,X.C., Fang,Z.H. and
            Gao,J.R.
  TITLE     Comprehensive analysis of the m6A demethylase FTO in endothelial
            dysfunction by MeRIP sequencing
  JOURNAL   Exp Cell Res 442 (2), 114268 (2024)
   PUBMED   39343042
  REMARK    GeneRIF: Comprehensive analysis of the m[6]A demethylase FTO in
            endothelial dysfunction by MeRIP sequencing.
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Nabeel-Shah,S., Pu,S., Burke,G.L., Ahmed,N., Braunschweig,U.,
            Farhangmehr,S., Lee,H., Wu,M., Ni,Z., Tang,H., Zhong,G., Marcon,E.,
            Zhang,Z., Blencowe,B.J. and Greenblatt,J.F.
  TITLE     Recruitment of the m6A/m6Am demethylase FTO to target RNAs by the
            telomeric zinc finger protein ZBTB48
  JOURNAL   Genome Biol 25 (1), 246 (2024)
   PUBMED   39300486
  REMARK    GeneRIF: Recruitment of the m[6]A/m6Am demethylase FTO to target
            RNAs by the telomeric zinc finger protein ZBTB48.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Hussain,M., Waheed,A., Elahi,A. and Mustafa,G.
  TITLE     Fat Mass and Obesity-Related (FTO) Gene Variant Is a Predictor of
            CVD in T2DM Patients
  JOURNAL   J Diabetes Res 2024, 5914316 (2024)
   PUBMED   39257882
  REMARK    GeneRIF: Fat Mass and Obesity-Related (FTO) Gene Variant Is a
            Predictor of CVD in T2DM Patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Zeggini,E., Weedon,M.N., Lindgren,C.M., Frayling,T.M.,
            Elliott,K.S., Lango,H., Timpson,N.J., Perry,J.R., Rayner,N.W.,
            Freathy,R.M., Barrett,J.C., Shields,B., Morris,A.P., Ellard,S.,
            Groves,C.J., Harries,L.W., Marchini,J.L., Owen,K.R., Knight,B.,
            Cardon,L.R., Walker,M., Hitman,G.A., Morris,A.D., Doney,A.S.,
            McCarthy,M.I. and Hattersley,A.T.
  CONSRTM   Wellcome Trust Case Control Consortium (WTCCC)
  TITLE     Replication of genome-wide association signals in UK samples
            reveals risk loci for type 2 diabetes
  JOURNAL   Science 316 (5829), 1336-1341 (2007)
   PUBMED   17463249
  REMARK    Erratum:[Science. 2007 Aug 24;317(5841):1035-6]
REFERENCE   7  (residues 1 to 467)
  AUTHORS   Scott,L.J., Mohlke,K.L., Bonnycastle,L.L., Willer,C.J., Li,Y.,
            Duren,W.L., Erdos,M.R., Stringham,H.M., Chines,P.S., Jackson,A.U.,
            Prokunina-Olsson,L., Ding,C.J., Swift,A.J., Narisu,N., Hu,T.,
            Pruim,R., Xiao,R., Li,X.Y., Conneely,K.N., Riebow,N.L., Sprau,A.G.,
            Tong,M., White,P.P., Hetrick,K.N., Barnhart,M.W., Bark,C.W.,
            Goldstein,J.L., Watkins,L., Xiang,F., Saramies,J., Buchanan,T.A.,
            Watanabe,R.M., Valle,T.T., Kinnunen,L., Abecasis,G.R., Pugh,E.W.,
            Doheny,K.F., Bergman,R.N., Tuomilehto,J., Collins,F.S. and
            Boehnke,M.
  TITLE     A genome-wide association study of type 2 diabetes in Finns detects
            multiple susceptibility variants
  JOURNAL   Science 316 (5829), 1341-1345 (2007)
   PUBMED   17463248
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 467)
  AUTHORS   Dina,C., Meyre,D., Gallina,S., Durand,E., Korner,A., Jacobson,P.,
            Carlsson,L.M., Kiess,W., Vatin,V., Lecoeur,C., Delplanque,J.,
            Vaillant,E., Pattou,F., Ruiz,J., Weill,J., Levy-Marchal,C.,
            Horber,F., Potoczna,N., Hercberg,S., Le Stunff,C., Bougneres,P.,
            Kovacs,P., Marre,M., Balkau,B., Cauchi,S., Chevre,J.C. and
            Froguel,P.
  TITLE     Variation in FTO contributes to childhood obesity and severe adult
            obesity
  JOURNAL   Nat Genet 39 (6), 724-726 (2007)
   PUBMED   17496892
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            GeneRIF: Association with obesity in adult and childre.
            Interestingly, this association receives clear confirmation under a
            Transmission Disequilibrium Test design which is robust to
            population stratification.
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Frayling,T.M., Timpson,N.J., Weedon,M.N., Zeggini,E., Freathy,R.M.,
            Lindgren,C.M., Perry,J.R., Elliott,K.S., Lango,H., Rayner,N.W.,
            Shields,B., Harries,L.W., Barrett,J.C., Ellard,S., Groves,C.J.,
            Knight,B., Patch,A.M., Ness,A.R., Ebrahim,S., Lawlor,D.A.,
            Ring,S.M., Ben-Shlomo,Y., Jarvelin,M.R., Sovio,U., Bennett,A.J.,
            Melzer,D., Ferrucci,L., Loos,R.J., Barroso,I., Wareham,N.J.,
            Karpe,F., Owen,K.R., Cardon,L.R., Walker,M., Hitman,G.A.,
            Palmer,C.N., Doney,A.S., Morris,A.D., Smith,G.D., Hattersley,A.T.
            and McCarthy,M.I.
  TITLE     A common variant in the FTO gene is associated with body mass index
            and predisposes to childhood and adult obesity
  JOURNAL   Science 316 (5826), 889-894 (2007)
   PUBMED   17434869
  REMARK    GeneRIF: A genome-wide search for type 2 diabetes-susceptibility
            genes identified a common variant in the FTO gene that predisposes
            to diabetes through an effect on body mass index
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association and gene-environment interaction. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 467)
  AUTHORS   Peters,T., Ausmeier,K. and Ruther,U.
  TITLE     Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft)
            mouse mutation
  JOURNAL   Mamm Genome 10 (10), 983-986 (1999)
   PUBMED   10501967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007909.8, AC007496.6 and
            AC007347.3.
            
            Summary: This gene is a nuclear protein of the AlkB related
            non-haem iron and 2-oxoglutarate-dependent oxygenase superfamily
            but the exact physiological function of this gene is not known.
            Other non-heme iron enzymes function to reverse alkylated DNA and
            RNA damage by oxidative demethylation. Studies in mice and humans
            indicate a role in nervous and cardiovascular systems and a strong
            association with body mass index, obesity risk, and type 2
            diabetes. [provided by RefSeq, Jul 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1496311.1,
                                           SRR1803613.231532.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267763 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..467
                     /product="alpha-ketoglutarate-dependent dioxygenase FTO
                     isoform 7"
                     /EC_number="1.14.11.53"
                     /note="alpha-ketoglutarate-dependent dioxygenase FTO; fat
                     mass and obesity-associated protein; AlkB homolog 9; fat
                     mass and obesity associated; m6A(m)-demethylase FTO; tRNA
                     N1-methyl adenine demethylase FTO; mRNA
                     N(6)-methyladenosine demethylase FTO; mRNA
                     (2'-O-methyladenosine-N(6)-)-demethylase FTO; U6 small
                     nuclear RNA N(6)-methyladenosine-demethylase FTO; U6 small
                     nuclear RNA (2'-O-methyladenosine-N(6)-)-demethylase FTO;
                     intragenic FTO exon 9 containing transcript; mRNA
                     N(6)-methyladenine demethylase"
                     /calculated_mol_wt=53850
     Region          36..287
                     /region_name="FTO_NTD"
                     /note="FTO catalytic domain; pfam12933"
                     /db_xref="CDD:463755"
     Region          291..460
                     /region_name="FTO_CTD"
                     /note="FTO C-terminal domain; pfam12934"
                     /db_xref="CDD:432887"
     CDS             1..467
                     /gene="FTO"
                     /gene_synonym="ALKBH9; BMIQ14; GDFD; IFEX9"
                     /coded_by="NM_001363899.2:30..1433"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:79068"
                     /db_xref="HGNC:HGNC:24678"
                     /db_xref="MIM:610966"
ORIGIN      
        1 mkrtptaeer ereakklrll eeledtwlpy ltpkddefyq qwqlkypkli lreassvsee
       61 lhkevqeafl tlhkhgclfr dlvriqgkdl ltpvsrilig npgctykyln trlftvpwpv
      121 kgsnikhtea eiaaacetfl klndylqiet iqaleelaak ekanedavpl cmsadfprvg
      181 mgssyngqde vdiksraayn vtllnfmdpq kmpylkeepy fgmgkmavsw hhdenlvdrs
      241 avavysysce gtvcswkkqp ydlnathqhc vlagsqprfs sthrvaecst gtldyilqrc
      301 qlalqnvcdd vdnddvslks fepavlkqge eihnevefew lrqfwfqgnr yrkctdwwcq
      361 pmaqlealwk kmegvtnavl hevkreglpv eqrneiltai lasltarqnl rrewharcqs
      421 riartlpadq kpecrpywek ddasmplpfd ltdivselrg qlleakp
//
LOCUS       NP_001340873             758 aa            linear   PRI 21-DEC-2025
DEFINITION  disco-interacting protein 2 homolog A isoform i [Homo sapiens].
ACCESSION   NP_001340873
VERSION     NP_001340873.1
DBSOURCE    REFSEQ: accession NM_001353944.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Zhang,B., Zhang,X., Omorou,M., Zhao,K., Ruan,Y. and Luan,H.
  TITLE     Disco interacting protein 2 homolog A (DIP2A): A key component in
            the regulation of brain disorders
  JOURNAL   Biomed Pharmacother 168, 115771 (2023)
   PUBMED   37897975
  REMARK    GeneRIF: Disco interacting protein 2 homolog A (DIP2A): A key
            component in the regulation of brain disorders.
            Review article
REFERENCE   2  (residues 1 to 758)
  AUTHORS   Mondal,S., Kinatukara,P., Singh,S., Shambhavi,S., Patil,G.S.,
            Dubey,N., Singh,S.H., Pal,B., Shekar,P.C., Kamat,S.S. and
            Sankaranarayanan,R.
  TITLE     DIP2 is a unique regulator of diacylglycerol lipid homeostasis in
            eukaryotes
  JOURNAL   Elife 11, e77665 (2022)
   PUBMED   35766356
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 758)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 758)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 758)
  AUTHORS   Ma,J., Zhang,L.Q., He,Z.X., He,X.X., Wang,Y.J., Jian,Y.L., Wang,X.,
            Zhang,B.B., Su,C., Lu,J., Huang,B.Q., Zhang,Y., Wang,G.Y.,
            Guo,W.X., Qiu,D.L., Mei,L., Xiong,W.C., Zheng,Y.W. and Zhu,X.J.
  TITLE     Autism candidate gene DIP2A regulates spine morphogenesis via
            acetylation of cortactin
  JOURNAL   PLoS Biol 17 (10), e3000461 (2019)
   PUBMED   31600191
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 758)
  AUTHORS   Winnepenninckx,B., Debacker,K., Ramsay,J., Smeets,D., Smits,A.,
            FitzPatrick,D.R. and Kooy,R.F.
  TITLE     CGG-repeat expansion in the DIP2B gene is associated with the
            fragile site FRA12A on chromosome 12q13.1
  JOURNAL   Am J Hum Genet 80 (2), 221-231 (2007)
   PUBMED   17236128
REFERENCE   7  (residues 1 to 758)
  AUTHORS   Casadei,R., Strippoli,P., D'Addabbo,P., Canaider,S., Lenzi,L.,
            Vitale,L., Giannone,S., Frabetti,F., Facchin,F., Carinci,P. and
            Zannotti,M.
  TITLE     mRNA 5' region sequence incompleteness: a potential source of
            systematic errors in translation initiation codon assignment in
            human mRNAs
  JOURNAL   Gene 321, 185-193 (2003)
   PUBMED   14637006
REFERENCE   8  (residues 1 to 758)
  AUTHORS   Mukhopadhyay,M., Pelka,P., DeSousa,D., Kablar,B., Schindler,A.,
            Rudnicki,M.A. and Campos,A.R.
  TITLE     Cloning, genomic organization and expression pattern of a novel
            Drosophila gene, the disco-interacting protein 2 (dip2), and its
            murine homolog
  JOURNAL   Gene 293 (1-2), 59-65 (2002)
   PUBMED   12137943
REFERENCE   9  (residues 1 to 758)
  AUTHORS   Gardiner,K., Slavov,D., Bechtel,L. and Davisson,M.
  TITLE     Annotation of human chromosome 21 for relevance to Down syndrome:
            gene structure and expression analysis
  JOURNAL   Genomics 79 (6), 833-843 (2002)
   PUBMED   12036298
REFERENCE   10 (residues 1 to 758)
  AUTHORS   Wang,Z., Tseng,C.P., Pong,R.C., Chen,H., McConnell,J.D., Navone,N.
            and Hsieh,J.T.
  TITLE     The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate
            cancer. Characterization of a novel GTPase-activating protein
            associated with N-terminal domain of DOC-2/DAB2
  JOURNAL   J Biol Chem 277 (15), 12622-12631 (2002)
   PUBMED   11812785
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000337.1 and AP000338.3.
            
            Summary: The protein encoded by this gene may be involved in axon
            patterning in the central nervous system. This gene is not highly
            expressed. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Mar 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.211565.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2153031
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..758
                     /product="disco-interacting protein 2 homolog A isoform i"
                     /EC_number="6.2.1.1"
                     /note="disco-interacting protein 2A; DIP2 homolog A; DIP2
                     disco-interacting protein 2 homolog A; disconnected
                     interacting protein 2 homolog A; disco interacting protein
                     2 homolog A"
                     /calculated_mol_wt=82187
     Region          10..123
                     /region_name="DMAP_binding"
                     /note="DMAP1-binding Domain; pfam06464"
                     /db_xref="CDD:368923"
     Region          268..758
                     /region_name="Adenylate forming domain, Class I
                     superfamily"
                     /note="This family includes acyl- and aryl-CoA ligases, as
                     well as the adenylation domain of nonribosomal peptide
                     synthetases and firefly luciferases. The adenylate-forming
                     enzymes catalyze an ATP-dependent two-step reaction to
                     first activate a carboxylate...; cl17068"
                     /db_xref="CDD:473059"
     Site            order(429,432..437,439..440)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341228"
     Site            order(432,473..474,524,526..527,530,552..553,571..576,709,
                     721,724,732..735)
                     /site_type="active"
                     /db_xref="CDD:341228"
     Site            order(432,552..553,571..576,709,721,724,735)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Site            order(473,526..527,530,552,732..734)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341228"
     CDS             1..758
                     /gene="DIP2A"
                     /gene_synonym="C21orf106; DIP2"
                     /coded_by="NM_001353944.2:242..2518"
                     /note="isoform i is encoded by transcript variant 10"
                     /db_xref="GeneID:23181"
                     /db_xref="HGNC:HGNC:17217"
                     /db_xref="MIM:607711"
ORIGIN      
        1 madrgcplea aplpaevres laelelelse gditqkgyek krakllaryi pliqgidpsl
       61 qaenripgps qttaaapkqq ksrptasrde rfrsdvhtea vqaalakyke rkmpmpskrr
      121 svlvhssvet ytppadlhsa ppdvttglve hsyferpqva svrsvprgcs gsmletadgv
      181 pvnsrvsski qqllntlkrp krpplkeffv ddfeellevq qpdpnqpkpe gsetsvlrge
      241 pltagvprpp sllatlqrwg ttqpkspclt aldttgkavy tltygklwsr slklaytlln
      301 kltsknepll kpgdrvalvf pnsdpvmfmv afygcllael vpvpievplt rkdagsqqvg
      361 fllgscgvfl alttdacqkg lpkaqtgeva afkgwpplsw lvidgkhlak ppkdwhplaq
      421 dtgtgtayie yktskegstv gvtvshasll aqcraltqac gyseaetltn vldfkrdagl
      481 whgvltsvmn rmhvvsvpya lmkanplswi qkvcfykara alvksrdmhw sllaqrgqrd
      541 vslsslrmli vadganpwsi sscdaflnvf qsrglrpevi cpcasspeal tvairrppdl
      601 ggppprkavl smnglsygvi rvdteeklsv ltvqdvgqvm pganvcvvkl egtpylcktd
      661 evgeicvsss atgtayygll gitknvfeav pvttggapif drpftrtgll gfigpdnlvf
      721 ivgkldglmv tgvrrhnadd vvatalavep mkfvyrgr
//
LOCUS       NP_001139587             798 aa            linear   PRI 21-DEC-2025
DEFINITION  disco-interacting protein 2 homolog A isoform f [Homo sapiens].
ACCESSION   NP_001139587
VERSION     NP_001139587.1
DBSOURCE    REFSEQ: accession NM_001146115.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Zhang,B., Zhang,X., Omorou,M., Zhao,K., Ruan,Y. and Luan,H.
  TITLE     Disco interacting protein 2 homolog A (DIP2A): A key component in
            the regulation of brain disorders
  JOURNAL   Biomed Pharmacother 168, 115771 (2023)
   PUBMED   37897975
  REMARK    GeneRIF: Disco interacting protein 2 homolog A (DIP2A): A key
            component in the regulation of brain disorders.
            Review article
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Mondal,S., Kinatukara,P., Singh,S., Shambhavi,S., Patil,G.S.,
            Dubey,N., Singh,S.H., Pal,B., Shekar,P.C., Kamat,S.S. and
            Sankaranarayanan,R.
  TITLE     DIP2 is a unique regulator of diacylglycerol lipid homeostasis in
            eukaryotes
  JOURNAL   Elife 11, e77665 (2022)
   PUBMED   35766356
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Ma,J., Zhang,L.Q., He,Z.X., He,X.X., Wang,Y.J., Jian,Y.L., Wang,X.,
            Zhang,B.B., Su,C., Lu,J., Huang,B.Q., Zhang,Y., Wang,G.Y.,
            Guo,W.X., Qiu,D.L., Mei,L., Xiong,W.C., Zheng,Y.W. and Zhu,X.J.
  TITLE     Autism candidate gene DIP2A regulates spine morphogenesis via
            acetylation of cortactin
  JOURNAL   PLoS Biol 17 (10), e3000461 (2019)
   PUBMED   31600191
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Winnepenninckx,B., Debacker,K., Ramsay,J., Smeets,D., Smits,A.,
            FitzPatrick,D.R. and Kooy,R.F.
  TITLE     CGG-repeat expansion in the DIP2B gene is associated with the
            fragile site FRA12A on chromosome 12q13.1
  JOURNAL   Am J Hum Genet 80 (2), 221-231 (2007)
   PUBMED   17236128
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Casadei,R., Strippoli,P., D'Addabbo,P., Canaider,S., Lenzi,L.,
            Vitale,L., Giannone,S., Frabetti,F., Facchin,F., Carinci,P. and
            Zannotti,M.
  TITLE     mRNA 5' region sequence incompleteness: a potential source of
            systematic errors in translation initiation codon assignment in
            human mRNAs
  JOURNAL   Gene 321, 185-193 (2003)
   PUBMED   14637006
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Mukhopadhyay,M., Pelka,P., DeSousa,D., Kablar,B., Schindler,A.,
            Rudnicki,M.A. and Campos,A.R.
  TITLE     Cloning, genomic organization and expression pattern of a novel
            Drosophila gene, the disco-interacting protein 2 (dip2), and its
            murine homolog
  JOURNAL   Gene 293 (1-2), 59-65 (2002)
   PUBMED   12137943
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Gardiner,K., Slavov,D., Bechtel,L. and Davisson,M.
  TITLE     Annotation of human chromosome 21 for relevance to Down syndrome:
            gene structure and expression analysis
  JOURNAL   Genomics 79 (6), 833-843 (2002)
   PUBMED   12036298
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Wang,Z., Tseng,C.P., Pong,R.C., Chen,H., McConnell,J.D., Navone,N.
            and Hsieh,J.T.
  TITLE     The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate
            cancer. Characterization of a novel GTPase-activating protein
            associated with N-terminal domain of DOC-2/DAB2
  JOURNAL   J Biol Chem 277 (15), 12622-12631 (2002)
   PUBMED   11812785
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000337.1, DA326960.1,
            BC033718.1 and BQ017399.1.
            
            Summary: The protein encoded by this gene may be involved in axon
            patterning in the central nervous system. This gene is not highly
            expressed. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (6) lacks an alternate in-frame
            exon and differs in the 3' UTR and coding region compared to
            variant 1, that causes a frameshift. The resulting isoform (f) is
            shorter and has a distinct C-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033718.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..798
                     /product="disco-interacting protein 2 homolog A isoform f"
                     /EC_number="6.2.1.1"
                     /note="disco-interacting protein 2A; DIP2 homolog A; DIP2
                     disco-interacting protein 2 homolog A; disconnected
                     interacting protein 2 homolog A; disco interacting protein
                     2 homolog A"
                     /calculated_mol_wt=85883
     Region          10..123
                     /region_name="DMAP_binding"
                     /note="DMAP1-binding Domain; pfam06464"
                     /db_xref="CDD:368923"
     Region          308..798
                     /region_name="Adenylate forming domain, Class I
                     superfamily"
                     /note="This family includes acyl- and aryl-CoA ligases, as
                     well as the adenylation domain of nonribosomal peptide
                     synthetases and firefly luciferases. The adenylate-forming
                     enzymes catalyze an ATP-dependent two-step reaction to
                     first activate a carboxylate...; cl17068"
                     /db_xref="CDD:473059"
     Site            order(469,472..477,479..480)
                     /site_type="other"
                     /note="acyl-activating enzyme (AAE) consensus motif"
                     /db_xref="CDD:341228"
     Site            order(472,513..514,564,566..567,570,592..593,611..616,749,
                     761,764,772..775)
                     /site_type="active"
                     /db_xref="CDD:341228"
     Site            order(472,592..593,611..616,749,761,764,775)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:341228"
     Site            order(513,566..567,570,592,772..774)
                     /site_type="other"
                     /note="CoA binding site [chemical binding]"
                     /db_xref="CDD:341228"
     CDS             1..798
                     /gene="DIP2A"
                     /gene_synonym="C21orf106; DIP2"
                     /coded_by="NM_001146115.2:242..2638"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS54491.1"
                     /db_xref="GeneID:23181"
                     /db_xref="HGNC:HGNC:17217"
                     /db_xref="MIM:607711"
ORIGIN      
        1 madrgcplea aplpaevres laelelelse gditqkgyek krakllaryi pliqgidpsl
       61 qaenripgps qttaaapkqq ksrptasrde rfrsdvhtea vqaalakyke rkmpmpskrr
      121 svlvhssvet ytppdtssas edegslrrpg rltstplqsh ssvepwldrv iqgsstsssa
      181 sstsshpggr pttapsaaat pgaaattala gleahthigv pvnsrvsski qqllntlkrp
      241 krpplkeffv ddfeellevq qpdpnqpkpe gsetsvlrge pltagvprpp sllatlqrwg
      301 ttqpkspclt aldttgkavy tltygklwsr slklaytlln kltsknepll kpgdrvalvf
      361 pnsdpvmfmv afygcllael vpvpievplt rkdagsqqvg fllgscgvfl alttdacqkg
      421 lpkaqtgeva afkgwpplsw lvidgkhlak ppkdwhplaq dtgtgtayie yktskegstv
      481 gvtvshasll aqcraltqac gyseaetltn vldfkrdagl whgvltsvmn rmhvvsvpya
      541 lmkanplswi qkvcfykara alvksrdmhw sllaqrgqrd vslsslrmli vadganpwsi
      601 sscdaflnvf qsrglrpevi cpcasspeal tvairrppdl ggppprkavl smnglsygvi
      661 rvdteeklsv ltvqdvgqvm pganvcvvkl egtpylcktd evgeicvsss atgtayygll
      721 gitknvfeav pvttggapif drpftrtgll gfigpdnlvf ivgkldglmv tgvrrhnadd
      781 vvatalavep mkfvyrgr
//
LOCUS       NP_001138586            1236 aa            linear   PRI 22-DEC-2025
DEFINITION  RRP12-like protein isoform 2 [Homo sapiens].
ACCESSION   NP_001138586
VERSION     NP_001138586.1
DBSOURCE    REFSEQ: accession NM_001145114.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1236)
  AUTHORS   Ameismeier,M., Cheng,J., Berninghausen,O. and Beckmann,R.
  TITLE     Visualizing late states of human 40S ribosomal subunit maturation
  JOURNAL   Nature 558 (7709), 249-253 (2018)
   PUBMED   29875412
REFERENCE   2  (residues 1 to 1236)
  AUTHORS   Choi,Y.J., Lee,H.W., Lee,Y.S., Shim da,M. and Seo,S.W.
  TITLE     RRP12 is a crucial nucleolar protein that regulates p53 activity in
            osteosarcoma cells
  JOURNAL   Tumour Biol 37 (4), 4351-4358 (2016)
   PUBMED   26499779
  REMARK    GeneRIF: This study demonstrated that RRP12 was crucial for cell
            survival during cytotoxic stress via the repression of p53
            stability. Thus, targeting RRP12 may enhance chemotherapeutic
            effect in cancers
REFERENCE   3  (residues 1 to 1236)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 1236)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 1236)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   6  (residues 1 to 1236)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   7  (residues 1 to 1236)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   8  (residues 1 to 1236)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   9  (residues 1 to 1236)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   10 (residues 1 to 1236)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL355490.24, AK296315.1, BC012745.2 and AK022496.1.
            
            Transcript Variant: This variant (2) lacks two alternate in-frame
            exons in the 5' coding region, compared to variant 1. This results
            in a shorter protein (isoform 2), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296315.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1236
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.1"
     Protein         1..1236
                     /product="RRP12-like protein isoform 2"
                     /note="RRP12-like protein"
                     /calculated_mol_wt=136984
     Region          410..610
                     /region_name="NUC173"
                     /note="NUC173 domain; pfam08161"
                     /db_xref="CDD:462386"
     CDS             1..1236
                     /gene="RRP12"
                     /gene_synonym="IBGC11; KIAA0690"
                     /coded_by="NM_001145114.1:140..3850"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44467.1"
                     /db_xref="GeneID:23223"
                     /db_xref="HGNC:HGNC:29100"
                     /db_xref="MIM:617723"
ORIGIN      
        1 mgrsgklpsg vsaklkrwkk ghssdsnpai crhrqaarsr ffsrpsgrsd ltvdavklhn
       61 elqsgslrlg kseapetpme eeaelvltek ssgtflsgls dctnvtfskv qrfwesnsaa
      121 hkeicavlaa vtevirsqgg keteteyfaa lvlsclatll rkqdleawgy pvtlqvyhgl
      181 lsftvhpkpk irkaaqhgvc svlkgsefmf ekapahhpaa istakfciqe ieksggskea
      241 tttlhmltll kdllpcfpeg lvkscsetll rvmtlshvlv tacamqafhs lfharpglst
      301 lsaelnaqii talydyvpse ndlqpllawl kvmekahinl vrlqwdlglg hlprffgtav
      361 tcllsphsqv ltaatqslke ilkecvaphm adigsvtssa sgpaqsvakm fraveeglty
      421 kfhaawssvl qllcvffeac grqahpvmrk clqslcdlrl sphfphtaal dqavgaavts
      481 mgpevvlqav pleidgseet ldfprswllp virdhvqetr lgffttyflp lantlkskam
      541 dlaqagstve skiydtlqwq mwtllpgfct rptdvaisfk glartlgmai serpdlrvtv
      601 cqalrtlitk gcqaeadrae vsrfaknflp ilfnlygqpv aagdtpaprr avletirtyl
      661 titdtqlvns llekasekvl dpassdftrl svldlvvala pcadeaaisk lystirpyle
      721 skahgvqkka yrvleevcas pqgpgalfvq shledlkktl ldslrstssp akrprlkcll
      781 hivrklsaeh kefitalipe vilctkevsv garknafall vemghaflrf gsnqeealqc
      841 ylvliypglv gavtmvscsi lalthllfef kglmgtstve qllenvclll asrtrdvvks
      901 algfikvavt vmdvahlakh vqlvmeaigk lsddmrrhfr mklrnlftkf irkfgfelvk
      961 rllpeeyhrv lvnirkaear akrhralsqa aveeeeeeee eeepaqgkgd sieeiladse
     1021 deedneeeer srgkeqrkla rqrsrawlke gggdeplnfl dpkvaqrvla tqpgpgrgrk
     1081 kdhgfkvsad grliireead gnkmeeeega kgedeemadp medviirnkk hqklkhqkea
     1141 eeeeleippq yqaggsgihr pvakkampga eykakkakgd vkkkgrpdpy ayiplnrskl
     1201 nrrkkmklqg qfkglvkaar rgsqvghknr rkdrrp
//
LOCUS       NP_071421                457 aa            linear   PRI 22-DEC-2025
DEFINITION  SPARC-related modular calcium-binding protein 2 isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_071421
VERSION     NP_071421.1
DBSOURCE    REFSEQ: accession NM_022138.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Huang,Q., Sun,Y., Huang,W., Zhang,F., He,H., He,Y. and Huang,F.
  TITLE     FTO Positively Regulates Odontoblastic Differentiation via SMOC2 in
            Human Stem Cells from the Apical Papilla under Inflammatory
            Microenvironment
  JOURNAL   Int J Mol Sci 25 (7), 4045 (2024)
   PUBMED   38612855
  REMARK    GeneRIF: FTO Positively Regulates Odontoblastic Differentiation via
            SMOC2 in Human Stem Cells from the Apical Papilla under
            Inflammatory Microenvironment.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Xu,H., Lu,G., Zhou,S. and Fang,F.
  TITLE     MicroRNA-19a-3p Acts as an Oncogene in Gastric Cancer and Exerts
            the Effect by Targeting SMOC2
  JOURNAL   Appl Biochem Biotechnol 194 (9), 3833-3842 (2022)
   PUBMED   35543855
  REMARK    GeneRIF: MicroRNA-19a-3p Acts as an Oncogene in Gastric Cancer and
            Exerts the Effect by Targeting SMOC2.
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Feng,D., Gao,P., Henley,N., Dubuissez,M., Chen,N., Laurin,L.P.,
            Royal,V., Pichette,V. and Gerarduzzi,C.
  TITLE     SMOC2 promotes an epithelial-mesenchymal transition and a
            pro-metastatic phenotype in epithelial cells of renal cell
            carcinoma origin
  JOURNAL   Cell Death Dis 13 (7), 639 (2022)
   PUBMED   35869056
  REMARK    GeneRIF: SMOC2 promotes an epithelial-mesenchymal transition and a
            pro-metastatic phenotype in epithelial cells of renal cell
            carcinoma origin.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Alabiad,M.A., Harb,O.A., Hefzi,N., Ahmed,R.Z., Osman,G.,
            Shalaby,A.M., Alnemr,A.A. and Saraya,Y.S.
  TITLE     Prognostic and clinicopathological significance of TMEFF2, SMOC-2,
            and SOX17 expression in endometrial carcinoma
  JOURNAL   Exp Mol Pathol 122, 104670 (2021)
   PUBMED   34339705
  REMARK    GeneRIF: Prognostic and clinicopathological significance of TMEFF2,
            SMOC-2, and SOX17 expression in endometrial carcinoma.
REFERENCE   5  (residues 1 to 457)
  AUTHORS   Hyun,C.L., Park,S.J., Kim,H.S., Song,H.J., Kim,H.U., Lee,C.,
            Lee,D.H., Maeng,Y.H., Kim,Y.S. and Jang,B.
  TITLE     The Intestinal Stem Cell Marker SMOC2 Is an Independent Prognostic
            Marker Associated With Better Survival in Gastric Cancer
  JOURNAL   Anticancer Res 41 (7), 3689-3698 (2021)
   PUBMED   34230168
  REMARK    GeneRIF: The Intestinal Stem Cell Marker SMOC2 Is an Independent
            Prognostic Marker Associated With Better Survival in Gastric
            Cancer.
REFERENCE   6  (residues 1 to 457)
  AUTHORS   Birlea,S.A., Gowan,K., Fain,P.R. and Spritz,R.A.
  TITLE     Genome-wide association study of generalized vitiligo in an
            isolated European founder population identifies SMOC2, in close
            proximity to IDDM8
  JOURNAL   J Invest Dermatol 130 (3), 798-803 (2010)
   PUBMED   19890347
  REMARK    GeneRIF: SMOC2 is a risk locus for generalized vitiligo and perhaps
            other autoimmune diseases
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   7  (residues 1 to 457)
  AUTHORS   Wilk,J.B., Herbert,A., Shoemaker,C.M., Gottlieb,D.J. and
            Karamohamed,S.
  TITLE     Secreted modular calcium-binding protein 2 haplotypes are
            associated with pulmonary function
  JOURNAL   Am J Respir Crit Care Med 175 (6), 554-560 (2007)
   PUBMED   17204727
  REMARK    GeneRIF: We tested association between SMOC2 polymorphisms and
            FEV(1) and FVC. SMOC2 might play an important role in the
            determination of FEV(1) and FVC
REFERENCE   8  (residues 1 to 457)
  AUTHORS   Rocnik,E.F., Liu,P., Sato,K., Walsh,K. and Vaziri,C.
  TITLE     The novel SPARC family member SMOC-2 potentiates angiogenic growth
            factor activity
  JOURNAL   J Biol Chem 281 (32), 22855-22864 (2006)
   PUBMED   16774925
  REMARK    GeneRIF: SMOC-2 is a novel angiogenic factor that potentiates
            angiogenic effects of growth factors
REFERENCE   9  (residues 1 to 457)
  AUTHORS   Vannahme,C., Gosling,S., Paulsson,M., Maurer,P. and Hartmann,U.
  TITLE     Characterization of SMOC-2, a modular extracellular calcium-binding
            protein
  JOURNAL   Biochem J 373 (Pt 3), 805-814 (2003)
   PUBMED   12741954
  REMARK    GeneRIF: identification of gene, chromosome mapping
REFERENCE   10 (residues 1 to 457)
  AUTHORS   Nishimoto,S., Hamajima,Y., Toda,Y., Toyoda,H., Kitamura,K. and
            Komurasaki,T.
  TITLE     Identification of a novel smooth muscle associated protein, smap2,
            upregulated during neointima formation in a rat carotid
            endarterectomy model
  JOURNAL   Biochim Biophys Acta 1576 (1-2), 225-230 (2002)
   PUBMED   12031507
  REMARK    GeneRIF: Although this study specifies rat, the authors studied and
            discussed the human gene in this study as well.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC028420.1, AB014737.1,
            AL136099.11 and AI032288.1.
            
            Summary: This gene encodes a member of the SPARC family (secreted
            protein acidic and rich in cysteine/osteonectin/BM-40), which are
            highly expressed during embryogenesis and wound healing. The gene
            product is a matricellular protein which promotes matrix assembly
            and can stimulate endothelial cell proliferation and migration, as
            well as angiogenic activity. Associated with pulmonary function,
            this secretory gene product contains a Kazal domain, two
            thymoglobulin type-1 domains, and two EF-hand calcium-binding
            domains. The encoded protein may serve as a target for controlling
            angiogenesis in tumor growth and myocardial ischemia. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL832303.1, SRR1803616.138356.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q27"
     Protein         1..457
                     /product="SPARC-related modular calcium-binding protein 2
                     isoform 1 precursor"
                     /note="smooth muscle associated protein 2; thyroglobulin
                     type-1 repeat containing protein; secreted modular
                     calcium-binding protein 2; SPARC-related modular
                     calcium-binding protein 2; SMAP-2; SMOC-2"
                     /calculated_mol_wt=48625
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2256
     Region          39..84
                     /region_name="KAZAL"
                     /note="Kazal type serine protease inhibitors; smart00280"
                     /db_xref="CDD:197624"
     Region          90..153
                     /region_name="Thyroglobulin_1"
                     /note="Thyroglobulin type-1 repeat; pfam00086"
                     /db_xref="CDD:459665"
     Site            order(94,108,126,130)
                     /site_type="active"
                     /note="protease interaction site [active]"
                     /db_xref="CDD:238114"
     Region          154..225
                     /region_name="Thyroglob_assoc"
                     /note="Thyroglobulin_1 repeat associated disordered
                     domain; pfam16597"
                     /db_xref="CDD:435450"
     Region          226..292
                     /region_name="TY"
                     /note="Thyroglobulin type I repeats.; The N-terminal
                     region of human thyroglobulin contains 11 type-1 repeats
                     TY repeats are proposed to be inhibitors of cysteine
                     proteases; cd00191"
                     /db_xref="CDD:238114"
     Site            order(231,246,264,268)
                     /site_type="active"
                     /note="protease interaction site [active]"
                     /db_xref="CDD:238114"
     Region          315..428
                     /region_name="EFh_SPARC_SMOC2"
                     /note="EF-hand, extracellular calcium-binding (EC) motif,
                     found in secreted modular calcium-binding protein 2
                     (SMOC-2); cd16241"
                     /db_xref="CDD:320020"
     Region          359..391
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320020"
     Site            order(371,373,375,382,408,410,412,419)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320020"
     Region          396..428
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320020"
     CDS             1..457
                     /gene="SMOC2"
                     /gene_synonym="bA270C4A.1; bA37D8.1; dJ421D16.1; DTDP1;
                     DTDP1A; MST117; MSTP117; MSTP140; SMAP2"
                     /coded_by="NM_022138.3:188..1561"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS5307.1"
                     /db_xref="GeneID:64094"
                     /db_xref="HGNC:HGNC:20323"
                     /db_xref="MIM:607223"
ORIGIN      
        1 mllpqlcwlp llagllppvp aqkfsaltfl rvdqdkdkdc sldcagspqk plcasdgrtf
       61 lsrcefqrak ckdpqleiay rgnckdvsrc vaerkytqeq arkefqqvfi pecnddgtys
      121 qvqchsytgy cwcvtpngrp isgtavahkt prcpgsvnek lpqregtgkt vslqifsvln
      181 sddaaapale tqpqgdeedi asryptlwte qvksrqnktn knsvsscdqe hqsaleeakq
      241 pkndnvvipe cahgglykpv qchpstgycw cvlvdtgrpi pgtstryeqp kcdntarahp
      301 akardlykgr qlqgcpgakk hefltsvlda lstdmvhaas dpssssgrls epdpshtlee
      361 rvvhwyfkll dknssgdigk keikpfkrfl rkkskpkkcv kkfveycdvn ndksisvqel
      421 mgclgvaked gkadtkkrht prghaestsn rqprkqg
//
LOCUS       NP_004860                444 aa            linear   PRI 22-DEC-2025
DEFINITION  vacuolar protein sorting-associated protein 4B [Homo sapiens].
ACCESSION   NP_004860
VERSION     NP_004860.2
DBSOURCE    REFSEQ: accession NM_004869.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Lai,W.Q., Xia,H.F., Chen,G.H., Wang,X.L., Yang,J.G., Wu,L.Z.,
            Zhao,Y.F., Jia,Y.L. and Chen,G.
  TITLE     p-AKT/VPS4B regulates the small extracellular vesicle size in
            venous malformation endothelial cells
  JOURNAL   Oral Dis 30 (3), 1273-1285 (2024)
   PUBMED   37154262
  REMARK    GeneRIF: p-AKT/VPS4B regulates the small extracellular vesicle size
            in venous malformation endothelial cells.
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Harel,S., Altaras,Y., Nachmias,D., Rotem-Dai,N., Dvilansky,I.,
            Elia,N. and Rousso,I.
  TITLE     Analysis of individual HIV-1 budding event using fast AFM reveals a
            multiplexed role for VPS4
  JOURNAL   Biophys J 121 (21), 4229-4238 (2022)
   PUBMED   36042696
  REMARK    GeneRIF: Analysis of individual HIV-1 budding event using fast AFM
            reveals a multiplexed role for VPS4.
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Neggers,J.E., Paolella,B.R., Asfaw,A., Rothberg,M.V., Skipper,T.A.,
            Yang,A., Kalekar,R.L., Krill-Burger,J.M., Dharia,N.V., Kugener,G.,
            Kalfon,J., Yuan,C., Dumont,N., Gonzalez,A., Abdusamad,M., Li,Y.Y.,
            Spurr,L.F., Wu,W.W., Durbin,A.D., Wolpin,B.M., Piccioni,F.,
            Root,D.E., Boehm,J.S., Cherniack,A.D., Tsherniak,A., Hong,A.L.,
            Hahn,W.C., Stegmaier,K., Golub,T.R., Vazquez,F. and Aguirre,A.J.
  TITLE     Synthetic Lethal Interaction between the ESCRT Paralog Enzymes
            VPS4A and VPS4B in Cancers Harboring Loss of Chromosome 18q or 16q
  JOURNAL   Cell Rep 33 (11), 108493 (2020)
   PUBMED   33326793
  REMARK    GeneRIF: Synthetic Lethal Interaction between the ESCRT Paralog
            Enzymes VPS4A and VPS4B in Cancers Harboring Loss of Chromosome 18q
            or 16q.
            Erratum:[Cell Rep. 2021 Jul 13;36(2):109367. doi:
            10.1016/j.celrep.2021.109367. PMID: 34260938]
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Li,Q., Lu,F., Chen,T., Zhang,K., Lu,Y., Li,X., Wang,Y., Liu,L.,
            Tian,Q., Xiong,F. and Chen,D.
  TITLE     VPS4B mutation impairs the osteogenic differentiation of dental
            follicle cells derived from a patient with dentin dysplasia type I
  JOURNAL   Int J Oral Sci 12 (1), 22 (2020)
   PUBMED   32737282
  REMARK    GeneRIF: VPS4B mutation impairs the osteogenic differentiation of
            dental follicle cells derived from a patient with dentin dysplasia
            type I.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Bishop,N. and Woodman,P.
  TITLE     ATPase-defective mammalian VPS4 localizes to aberrant endosomes and
            impairs cholesterol trafficking
  JOURNAL   Mol Biol Cell 11 (1), 227-239 (2000)
   PUBMED   10637304
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
REFERENCE   8  (residues 1 to 444)
  AUTHORS   Scheuring,S., Bodor,O., Rohricht,R.A., Muller,S., Beyer,A. and
            Kohrer,K.
  TITLE     Cloning, characterisation, and functional expression of the Mus
            musculus SKD1 gene in yeast demonstrates that the mouse SKD1 and
            the yeast VPS4 genes are orthologues and involved in intracellular
            protein trafficking
  JOURNAL   Gene 234 (1), 149-159 (1999)
   PUBMED   10393249
REFERENCE   9  (residues 1 to 444)
  AUTHORS   Mao,M., Fu,G., Wu,J.S., Zhang,Q.H., Zhou,J., Kan,L.X., Huang,Q.H.,
            He,K.L., Gu,B.W., Han,Z.G., Shen,Y., Gu,J., Yu,Y.P., Xu,S.H.,
            Wang,Y.X., Chen,S.J. and Chen,Z.
  TITLE     Identification of genes expressed in human CD34(+) hematopoietic
            stem/progenitor cells by expressed sequence tags and efficient
            full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 8175-8180 (1998)
   PUBMED   9653160
REFERENCE   10 (residues 1 to 444)
  AUTHORS   Finken-Eigen,M., Rohricht,R.A. and Kohrer,K.
  TITLE     The VPS4 gene is involved in protein transport out of a yeast
            pre-vacuolar endosome-like compartment
  JOURNAL   Curr Genet 31 (6), 469-480 (1997)
   PUBMED   9211789
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA306069.1 and AF195514.1.
            
            On Dec 17, 2001 this sequence version replaced NP_004860.1.
            
            Summary: The protein encoded by this gene is a member of the AAA
            protein family (ATPases associated with diverse cellular
            activities), and is the homolog of the yeast Vps4 protein. In
            humans, two paralogs of the yeast protein have been identified. The
            former share a high degree of aa sequence similarity with each
            other, and also with yeast Vps4 and mouse Skd1 proteins. Mouse Skd1
            (suppressor of K+ transport defect 1) has been shown to be a yeast
            Vps4 ortholog. Functional studies indicate that both human paralogs
            associate with the endosomal compartments, and are involved in
            intracellular protein trafficking, similar to Vps4 protein in
            yeast. The gene encoding this paralog has been mapped to chromosome
            18; the gene for the other resides on chromosome 16. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF195514.1, ERR4643909.5451.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000238497.10/ ENSP00000238497.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.33"
     Protein         1..444
                     /product="vacuolar protein sorting-associated protein 4B"
                     /EC_number="3.6.4.6"
                     /note="suppressor of K+ transport defect 1; cell
                     migration-inducing 1; cell migration-inducing gene 1
                     protein; suppressor of K(+) transport growth defect 1;
                     vacuolar protein sorting 4B"
                     /calculated_mol_wt=49171
     Region          6..81
                     /region_name="MIT_VPS4"
                     /note="MIT: domain contained within Microtubule
                     Interacting and Trafficking molecules. This sub-family of
                     MIT domains is found in intracellular protein transport
                     proteins of the AAA-ATPase family. The molecular function
                     of the MIT domain is unclear; cd02678"
                     /db_xref="CDD:239141"
     Region          77..117
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75351.2)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75351.2)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75351.2)"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75351.2)"
     Region          128..298
                     /region_name="RecA-like_VPS4"
                     /note="ATPase domain of vacuolar protein
                     sorting-associated protein 4; cd19521"
                     /db_xref="CDD:410929"
     Site            order(129,148,152,155..156,160,164,176..177,181,185,196,
                     198,200..202,205,213,234..235,238,243,245,247..249,
                     251..253,256..257,280,283)
                     /site_type="other"
                     /note="hexamer interface [polypeptide binding]"
                     /db_xref="CDD:410929"
     Site            order(135..137,139,176..182,234,279)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:410929"
     Region          325..366
                     /region_name="AAA_lid_3"
                     /note="AAA+ lid domain; pfam17862"
                     /db_xref="CDD:465537"
     Region          381..441
                     /region_name="Vps4_C"
                     /note="Vps4 C terminal oligomerization domain; pfam09336"
                     /db_xref="CDD:462762"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75351.2)"
     CDS             1..444
                     /gene="VPS4B"
                     /gene_synonym="DTDP1B; MIG1; SKD1; SKD1B; VPS4-2"
                     /coded_by="NM_004869.4:218..1552"
                     /db_xref="CCDS:CCDS11983.1"
                     /db_xref="GeneID:9525"
                     /db_xref="HGNC:HGNC:10895"
                     /db_xref="MIM:609983"
ORIGIN      
        1 msstspnlqk aidlaskaaq edkagnyeea lqlyqhavqy flhvvkyeaq gdkakqsira
       61 kcteyldrae klkeylknke kkaqkpvkeg qpspadekgn dsdgegesdd pekkklqnql
      121 qgaivierpn vkwsdvagle gakealkeav ilpikfphlf tgkrtpwrgi llfgppgtgk
      181 sylakavate annstffsis ssdlvskwlg eseklvknlf qlarenkpsi ifideidslc
      241 gsrsenesea arrikteflv qmqgvgvdnd gilvlgatni pwvldsairr rfekriyipl
      301 pepharaamf klhlgttqns lteadfrelg rktdgysgad isiivrdalm qpvrkvqsat
      361 hfkkvrgpsr adpnhlvddl ltpcspgdpg aiemtwmdvp gdkllepvvs msdmlrslsn
      421 tkptvnehdl lklkkftedf gqeg
//
LOCUS       NP_116185                352 aa            linear   PRI 22-DEC-2025
DEFINITION  synapse-associated protein 1 [Homo sapiens].
ACCESSION   NP_116185
VERSION     NP_116185.2
DBSOURCE    REFSEQ: accession NM_032796.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Sanderson,M.R., Badior,K.E., Fahlman,R.P. and Wevrick,R.
  TITLE     The necdin interactome: evaluating the effects of amino acid
            substitutions and cell stress using proximity-dependent
            biotinylation (BioID) and mass spectrometry
  JOURNAL   Hum Genet 139 (12), 1513-1529 (2020)
   PUBMED   32529326
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Lee,O.H., Kim,H., He,Q., Baek,H.J., Yang,D., Chen,L.Y., Liang,J.,
            Chae,H.K., Safari,A., Liu,D. and Songyang,Z.
  TITLE     Genome-wide YFP fluorescence complementation screen identifies new
            regulators for telomere signaling in human cells
  JOURNAL   Mol Cell Proteomics 10 (2), M110.001628 (2011)
   PUBMED   21044950
REFERENCE   7  (residues 1 to 352)
  AUTHORS   Kang,D., Oh,S., Ahn,S.M., Lee,B.H. and Moon,M.H.
  TITLE     Proteomic analysis of exosomes from human neural stem cells by flow
            field-flow fractionation and nanoflow liquid chromatography-tandem
            mass spectrometry
  JOURNAL   J Proteome Res 7 (8), 3475-3480 (2008)
   PUBMED   18570454
REFERENCE   8  (residues 1 to 352)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 352)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 352)
  AUTHORS   Chang,Y.C., Yu,Y.L., Wang,N. and Xu,Y.H.
  TITLE     [Cloning and characterization of syap1, a down regulated gene in
            human hepatocellular carcinoma]
  JOURNAL   Shi Yan Sheng Wu Xue Bao 34 (4), 319-322 (2001)
   PUBMED   12549212
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB047379.1, AF168955.1, AF305828.1, DB577454.1, AL445467.6 and
            AA829759.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 4, 2002 this sequence version replaced NP_116185.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the functional protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314675.1, SRR1803613.16409.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380155.4/ ENSP00000369500.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..352
                     /product="synapse-associated protein 1"
                     /note="SAP47 homolog; synapse associated protein 1, SAP47
                     homolog; BSD domain-containing signal transducer and Akt
                     interactor protein"
                     /calculated_mol_wt=39802
     Region          1..45
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96A49.1)"
     Region          160..210
                     /region_name="BSD"
                     /note="domain in transcription factors and
                     synapse-associated proteins; smart00751"
                     /db_xref="CDD:128990"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96A49.1)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96A49.1)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96A49.1)"
     CDS             1..352
                     /gene="SYAP1"
                     /gene_synonym="BSTA; PRO3113; SAP47"
                     /coded_by="NM_032796.4:114..1172"
                     /db_xref="CCDS:CCDS14177.1"
                     /db_xref="GeneID:94056"
                     /db_xref="HGNC:HGNC:16273"
                     /db_xref="MIM:301161"
ORIGIN      
        1 mfrglsswlg lqqpvagggq pngdappeqp setvaesaee elqqagdqel lhqakdfgny
       61 lfnfasaatk kitesvaeta qtikksveeg kidgiidkti igdfqkeqkk fveeqhtkks
      121 eaavppwvdt ndeetiqqqi lalsadkrnf lrdppagvqf nfdfdqmypv alvmlqedel
      181 lskmrfalvp klvkeevfwr nyfyrvslik qsaqltalaa qqqaagkeek sngreqdlpl
      241 aeavrpktpp vviksqlktq edeeeistsp gvsefvsdaf dacnlnqedl rkemeqlvld
      301 kkqeetavle edsadwekel qqelqeyevv tesekrdenw dkeiekmlqe en
//
LOCUS       NP_001271266            1197 aa            linear   PRI 22-DEC-2025
DEFINITION  RRP12-like protein isoform 3 [Homo sapiens].
ACCESSION   NP_001271266 XP_005269716
VERSION     NP_001271266.1
DBSOURCE    REFSEQ: accession NM_001284337.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1197)
  AUTHORS   Ameismeier,M., Cheng,J., Berninghausen,O. and Beckmann,R.
  TITLE     Visualizing late states of human 40S ribosomal subunit maturation
  JOURNAL   Nature 558 (7709), 249-253 (2018)
   PUBMED   29875412
REFERENCE   2  (residues 1 to 1197)
  AUTHORS   Choi,Y.J., Lee,H.W., Lee,Y.S., Shim da,M. and Seo,S.W.
  TITLE     RRP12 is a crucial nucleolar protein that regulates p53 activity in
            osteosarcoma cells
  JOURNAL   Tumour Biol 37 (4), 4351-4358 (2016)
   PUBMED   26499779
  REMARK    GeneRIF: This study demonstrated that RRP12 was crucial for cell
            survival during cytotoxic stress via the repression of p53
            stability. Thus, targeting RRP12 may enhance chemotherapeutic
            effect in cancers
REFERENCE   3  (residues 1 to 1197)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 1197)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 1197)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   6  (residues 1 to 1197)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   7  (residues 1 to 1197)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   8  (residues 1 to 1197)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   9  (residues 1 to 1197)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   10 (residues 1 to 1197)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA227012.1, AB014590.1, AK022496.1, BC012745.2 and AL355490.24.
            
            On Sep 28, 2013 this sequence version replaced XP_005269716.1.
            
            Transcript Variant: This variant (3) lacks three alternate in-frame
            exons in the 5' coding region, compared to variant 1. This results
            in a shorter protein (isoform 3), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB014590.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1197
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.1"
     Protein         1..1197
                     /product="RRP12-like protein isoform 3"
                     /note="RRP12-like protein"
                     /calculated_mol_wt=132579
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Region          371..571
                     /region_name="NUC173"
                     /note="NUC173 domain; pfam08161"
                     /db_xref="CDD:462386"
     CDS             1..1197
                     /gene="RRP12"
                     /gene_synonym="IBGC11; KIAA0690"
                     /coded_by="NM_001284337.2:110..3703"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS60605.1"
                     /db_xref="GeneID:23223"
                     /db_xref="HGNC:HGNC:29100"
                     /db_xref="MIM:617723"
ORIGIN      
        1 mgrsgklpsg vsaklkrwkk ghssdsnpai crhrqaarsr ffsrpsgrsd ltvdavklhn
       61 elqsgslrlg kseapetpme eeaelvltek ssgtflsgls dctnvtfskv qrfwesnsaa
      121 hkeicavlaa vtevirsqgg keteteyfaa lirkaaqhgv csvlkgsefm fekapahhpa
      181 aistakfciq eieksggske atttlhmltl lkdllpcfpe glvkscsetl lrvmtlshvl
      241 vtacamqafh slfharpgls tlsaelnaqi italydyvps endlqpllaw lkvmekahin
      301 lvrlqwdlgl ghlprffgta vtcllsphsq vltaatqslk eilkecvaph madigsvtss
      361 asgpaqsvak mfraveeglt ykfhaawssv lqllcvffea cgrqahpvmr kclqslcdlr
      421 lsphfphtaa ldqavgaavt smgpevvlqa vpleidgsee tldfprswll pvirdhvqet
      481 rlgffttyfl plantlkska mdlaqagstv eskiydtlqw qmwtllpgfc trptdvaisf
      541 kglartlgma iserpdlrvt vcqalrtlit kgcqaeadra evsrfaknfl pilfnlygqp
      601 vaagdtpapr ravletirty ltitdtqlvn sllekasekv ldpassdftr lsvldlvval
      661 apcadeaais klystirpyl eskahgvqkk ayrvleevca spqgpgalfv qshledlkkt
      721 lldslrstss pakrprlkcl lhivrklsae hkefitalip evilctkevs vgarknafal
      781 lvemghaflr fgsnqeealq cylvliypgl vgavtmvscs ilalthllfe fkglmgtstv
      841 eqllenvcll lasrtrdvvk salgfikvav tvmdvahlak hvqlvmeaig klsddmrrhf
      901 rmklrnlftk firkfgfelv krllpeeyhr vlvnirkaea rakrhralsq aaveeeeeee
      961 eeeepaqgkg dsieeilads edeedneeee rsrgkeqrkl arqrsrawlk egggdeplnf
     1021 ldpkvaqrvl atqpgpgrgr kkdhgfkvsa dgrliireea dgnkmeeeeg akgedeemad
     1081 pmedviirnk khqklkhqke aeeeeleipp qyqaggsgih rpvakkampg aeykakkakg
     1141 dvkkkgrpdp yayiplnrsk lnrrkkmklq gqfkglvkaa rrgsqvghkn rrkdrrp
//
LOCUS       NP_001159884             446 aa            linear   PRI 22-DEC-2025
DEFINITION  SPARC-related modular calcium-binding protein 2 isoform 2 precursor
            [Homo sapiens].
ACCESSION   NP_001159884
VERSION     NP_001159884.1
DBSOURCE    REFSEQ: accession NM_001166412.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Huang,Q., Sun,Y., Huang,W., Zhang,F., He,H., He,Y. and Huang,F.
  TITLE     FTO Positively Regulates Odontoblastic Differentiation via SMOC2 in
            Human Stem Cells from the Apical Papilla under Inflammatory
            Microenvironment
  JOURNAL   Int J Mol Sci 25 (7), 4045 (2024)
   PUBMED   38612855
  REMARK    GeneRIF: FTO Positively Regulates Odontoblastic Differentiation via
            SMOC2 in Human Stem Cells from the Apical Papilla under
            Inflammatory Microenvironment.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Xu,H., Lu,G., Zhou,S. and Fang,F.
  TITLE     MicroRNA-19a-3p Acts as an Oncogene in Gastric Cancer and Exerts
            the Effect by Targeting SMOC2
  JOURNAL   Appl Biochem Biotechnol 194 (9), 3833-3842 (2022)
   PUBMED   35543855
  REMARK    GeneRIF: MicroRNA-19a-3p Acts as an Oncogene in Gastric Cancer and
            Exerts the Effect by Targeting SMOC2.
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Feng,D., Gao,P., Henley,N., Dubuissez,M., Chen,N., Laurin,L.P.,
            Royal,V., Pichette,V. and Gerarduzzi,C.
  TITLE     SMOC2 promotes an epithelial-mesenchymal transition and a
            pro-metastatic phenotype in epithelial cells of renal cell
            carcinoma origin
  JOURNAL   Cell Death Dis 13 (7), 639 (2022)
   PUBMED   35869056
  REMARK    GeneRIF: SMOC2 promotes an epithelial-mesenchymal transition and a
            pro-metastatic phenotype in epithelial cells of renal cell
            carcinoma origin.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Alabiad,M.A., Harb,O.A., Hefzi,N., Ahmed,R.Z., Osman,G.,
            Shalaby,A.M., Alnemr,A.A. and Saraya,Y.S.
  TITLE     Prognostic and clinicopathological significance of TMEFF2, SMOC-2,
            and SOX17 expression in endometrial carcinoma
  JOURNAL   Exp Mol Pathol 122, 104670 (2021)
   PUBMED   34339705
  REMARK    GeneRIF: Prognostic and clinicopathological significance of TMEFF2,
            SMOC-2, and SOX17 expression in endometrial carcinoma.
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Hyun,C.L., Park,S.J., Kim,H.S., Song,H.J., Kim,H.U., Lee,C.,
            Lee,D.H., Maeng,Y.H., Kim,Y.S. and Jang,B.
  TITLE     The Intestinal Stem Cell Marker SMOC2 Is an Independent Prognostic
            Marker Associated With Better Survival in Gastric Cancer
  JOURNAL   Anticancer Res 41 (7), 3689-3698 (2021)
   PUBMED   34230168
  REMARK    GeneRIF: The Intestinal Stem Cell Marker SMOC2 Is an Independent
            Prognostic Marker Associated With Better Survival in Gastric
            Cancer.
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Birlea,S.A., Gowan,K., Fain,P.R. and Spritz,R.A.
  TITLE     Genome-wide association study of generalized vitiligo in an
            isolated European founder population identifies SMOC2, in close
            proximity to IDDM8
  JOURNAL   J Invest Dermatol 130 (3), 798-803 (2010)
   PUBMED   19890347
  REMARK    GeneRIF: SMOC2 is a risk locus for generalized vitiligo and perhaps
            other autoimmune diseases
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Wilk,J.B., Herbert,A., Shoemaker,C.M., Gottlieb,D.J. and
            Karamohamed,S.
  TITLE     Secreted modular calcium-binding protein 2 haplotypes are
            associated with pulmonary function
  JOURNAL   Am J Respir Crit Care Med 175 (6), 554-560 (2007)
   PUBMED   17204727
  REMARK    GeneRIF: We tested association between SMOC2 polymorphisms and
            FEV(1) and FVC. SMOC2 might play an important role in the
            determination of FEV(1) and FVC
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Rocnik,E.F., Liu,P., Sato,K., Walsh,K. and Vaziri,C.
  TITLE     The novel SPARC family member SMOC-2 potentiates angiogenic growth
            factor activity
  JOURNAL   J Biol Chem 281 (32), 22855-22864 (2006)
   PUBMED   16774925
  REMARK    GeneRIF: SMOC-2 is a novel angiogenic factor that potentiates
            angiogenic effects of growth factors
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Vannahme,C., Gosling,S., Paulsson,M., Maurer,P. and Hartmann,U.
  TITLE     Characterization of SMOC-2, a modular extracellular calcium-binding
            protein
  JOURNAL   Biochem J 373 (Pt 3), 805-814 (2003)
   PUBMED   12741954
  REMARK    GeneRIF: identification of gene, chromosome mapping
REFERENCE   10 (residues 1 to 446)
  AUTHORS   Nishimoto,S., Hamajima,Y., Toda,Y., Toyoda,H., Kitamura,K. and
            Komurasaki,T.
  TITLE     Identification of a novel smooth muscle associated protein, smap2,
            upregulated during neointima formation in a rat carotid
            endarterectomy model
  JOURNAL   Biochim Biophys Acta 1576 (1-2), 225-230 (2002)
   PUBMED   12031507
  REMARK    GeneRIF: Although this study specifies rat, the authors studied and
            discussed the human gene in this study as well.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC028420.1 and AI032288.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the SPARC family (secreted
            protein acidic and rich in cysteine/osteonectin/BM-40), which are
            highly expressed during embryogenesis and wound healing. The gene
            product is a matricellular protein which promotes matrix assembly
            and can stimulate endothelial cell proliferation and migration, as
            well as angiogenic activity. Associated with pulmonary function,
            this secretory gene product contains a Kazal domain, two
            thymoglobulin type-1 domains, and two EF-hand calcium-binding
            domains. The encoded protein may serve as a target for controlling
            angiogenesis in tumor growth and myocardial ischemia. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Oct 2009].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the central coding region, compared to variant 1.
            This results in a shorter protein (isoform 2), compared to isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.210283.1, BC047583.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356284.7/ ENSP00000348630.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q27"
     Protein         1..446
                     /product="SPARC-related modular calcium-binding protein 2
                     isoform 2 precursor"
                     /note="smooth muscle associated protein 2; thyroglobulin
                     type-1 repeat containing protein; secreted modular
                     calcium-binding protein 2; SPARC-related modular
                     calcium-binding protein 2; SMAP-2; SMOC-2"
                     /calculated_mol_wt=47437
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2256
     Region          39..84
                     /region_name="KAZAL"
                     /note="Kazal type serine protease inhibitors; smart00280"
                     /db_xref="CDD:197624"
     Region          90..153
                     /region_name="Thyroglobulin_1"
                     /note="Thyroglobulin type-1 repeat; pfam00086"
                     /db_xref="CDD:459665"
     Site            order(94,108,126,130)
                     /site_type="active"
                     /note="protease interaction site [active]"
                     /db_xref="CDD:238114"
     Region          147..228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3U7.2)"
     Region          154..214
                     /region_name="Thyroglob_assoc"
                     /note="Thyroglobulin_1 repeat associated disordered
                     domain; pfam16597"
                     /db_xref="CDD:435450"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3U7.2)"
     Region          215..281
                     /region_name="TY"
                     /note="Thyroglobulin type I repeats.; The N-terminal
                     region of human thyroglobulin contains 11 type-1 repeats
                     TY repeats are proposed to be inhibitors of cysteine
                     proteases; cd00191"
                     /db_xref="CDD:238114"
     Site            order(220,235,253,257)
                     /site_type="active"
                     /note="protease interaction site [active]"
                     /db_xref="CDD:238114"
     Region          304..417
                     /region_name="EFh_SPARC_SMOC2"
                     /note="EF-hand, extracellular calcium-binding (EC) motif,
                     found in secreted modular calcium-binding protein 2
                     (SMOC-2); cd16241"
                     /db_xref="CDD:320020"
     Region          348..380
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320020"
     Site            order(360,362,364,371,397,399,401,408)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320020"
     Site            362
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3U7.2)"
     Region          385..417
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320020"
     Region          416..446
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3U7.2)"
     CDS             1..446
                     /gene="SMOC2"
                     /gene_synonym="bA270C4A.1; bA37D8.1; dJ421D16.1; DTDP1;
                     DTDP1A; MST117; MSTP117; MSTP140; SMAP2"
                     /coded_by="NM_001166412.2:188..1528"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS55076.1"
                     /db_xref="GeneID:64094"
                     /db_xref="HGNC:HGNC:20323"
                     /db_xref="MIM:607223"
ORIGIN      
        1 mllpqlcwlp llagllppvp aqkfsaltfl rvdqdkdkdc sldcagspqk plcasdgrtf
       61 lsrcefqrak ckdpqleiay rgnckdvsrc vaerkytqeq arkefqqvfi pecnddgtys
      121 qvqchsytgy cwcvtpngrp isgtavahkt prcpgsvnek lpqregtgkt ddaaapalet
      181 qpqgdeedia sryptlwteq vksrqnktnk nsvsscdqeh qsaleeakqp kndnvvipec
      241 ahgglykpvq chpstgycwc vlvdtgrpip gtstryeqpk cdntarahpa kardlykgrq
      301 lqgcpgakkh efltsvldal stdmvhaasd pssssgrlse pdpshtleer vvhwyfklld
      361 knssgdigkk eikpfkrflr kkskpkkcvk kfveycdvnn dksisvqelm gclgvakedg
      421 kadtkkrhtp rghaestsnr qprkqg
//
LOCUS       NP_055994               1297 aa            linear   PRI 22-DEC-2025
DEFINITION  RRP12-like protein isoform 1 [Homo sapiens].
ACCESSION   NP_055994
VERSION     NP_055994.2
DBSOURCE    REFSEQ: accession NM_015179.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1297)
  AUTHORS   Ameismeier,M., Cheng,J., Berninghausen,O. and Beckmann,R.
  TITLE     Visualizing late states of human 40S ribosomal subunit maturation
  JOURNAL   Nature 558 (7709), 249-253 (2018)
   PUBMED   29875412
REFERENCE   2  (residues 1 to 1297)
  AUTHORS   Choi,Y.J., Lee,H.W., Lee,Y.S., Shim da,M. and Seo,S.W.
  TITLE     RRP12 is a crucial nucleolar protein that regulates p53 activity in
            osteosarcoma cells
  JOURNAL   Tumour Biol 37 (4), 4351-4358 (2016)
   PUBMED   26499779
  REMARK    GeneRIF: This study demonstrated that RRP12 was crucial for cell
            survival during cytotoxic stress via the repression of p53
            stability. Thus, targeting RRP12 may enhance chemotherapeutic
            effect in cancers
REFERENCE   3  (residues 1 to 1297)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 1297)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 1297)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   6  (residues 1 to 1297)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   7  (residues 1 to 1297)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   8  (residues 1 to 1297)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   9  (residues 1 to 1297)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   10 (residues 1 to 1297)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK022496.1, DA231457.1, BC012745.2 and AK056614.1.
            
            On Feb 11, 2009 this sequence version replaced NP_055994.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012745.2, AK022496.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370992.9/ ENSP00000360031.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1297
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.1"
     Protein         1..1297
                     /product="RRP12-like protein isoform 1"
                     /note="RRP12-like protein"
                     /calculated_mol_wt=143572
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Region          471..671
                     /region_name="NUC173"
                     /note="NUC173 domain; pfam08161"
                     /db_xref="CDD:462386"
     Site            903..923
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Region          1047..1101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Site            1049
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Site            1072
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Site            1080
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5JTH9.2)"
     Region          1131..1297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JTH9.2)"
     CDS             1..1297
                     /gene="RRP12"
                     /gene_synonym="IBGC11; KIAA0690"
                     /coded_by="NM_015179.4:110..4003"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7457.1"
                     /db_xref="GeneID:23223"
                     /db_xref="HGNC:HGNC:29100"
                     /db_xref="MIM:617723"
ORIGIN      
        1 mgrsgklpsg vsaklkrwkk ghssdsnpai crhrqaarsr ffsrpsgrsd ltvdavklhn
       61 elqsgslrlg kseapetpme eeaelvltek ssgtflsgls dctnvtfskv qrfwesnsaa
      121 hkeicavlaa vtevirsqgg keteteyfaa lmttmeaves peslaavayl lnlvlkrvps
      181 pvlikkfsdt skafmdimsa qassgstsvl rwvlsclatl lrkqdleawg ypvtlqvyhg
      241 llsftvhpkp kirkaaqhgv csvlkgsefm fekapahhpa aistakfciq eieksggske
      301 atttlhmltl lkdllpcfpe glvkscsetl lrvmtlshvl vtacamqafh slfharpgls
      361 tlsaelnaqi italydyvps endlqpllaw lkvmekahin lvrlqwdlgl ghlprffgta
      421 vtcllsphsq vltaatqslk eilkecvaph madigsvtss asgpaqsvak mfraveeglt
      481 ykfhaawssv lqllcvffea cgrqahpvmr kclqslcdlr lsphfphtaa ldqavgaavt
      541 smgpevvlqa vpleidgsee tldfprswll pvirdhvqet rlgffttyfl plantlkska
      601 mdlaqagstv eskiydtlqw qmwtllpgfc trptdvaisf kglartlgma iserpdlrvt
      661 vcqalrtlit kgcqaeadra evsrfaknfl pilfnlygqp vaagdtpapr ravletirty
      721 ltitdtqlvn sllekasekv ldpassdftr lsvldlvval apcadeaais klystirpyl
      781 eskahgvqkk ayrvleevca spqgpgalfv qshledlkkt lldslrstss pakrprlkcl
      841 lhivrklsae hkefitalip evilctkevs vgarknafal lvemghaflr fgsnqeealq
      901 cylvliypgl vgavtmvscs ilalthllfe fkglmgtstv eqllenvcll lasrtrdvvk
      961 salgfikvav tvmdvahlak hvqlvmeaig klsddmrrhf rmklrnlftk firkfgfelv
     1021 krllpeeyhr vlvnirkaea rakrhralsq aaveeeeeee eeeepaqgkg dsieeilads
     1081 edeedneeee rsrgkeqrkl arqrsrawlk egggdeplnf ldpkvaqrvl atqpgpgrgr
     1141 kkdhgfkvsa dgrliireea dgnkmeeeeg akgedeemad pmedviirnk khqklkhqke
     1201 aeeeeleipp qyqaggsgih rpvakkampg aeykakkakg dvkkkgrpdp yayiplnrsk
     1261 lnrrkkmklq gqfkglvkaa rrgsqvghkn rrkdrrp
//
LOCUS       NP_001106212             585 aa            linear   PRI 22-DEC-2025
DEFINITION  voltage-gated potassium channel KCNC1 isoform 1 [Homo sapiens].
ACCESSION   NP_001106212
VERSION     NP_001106212.1
DBSOURCE    REFSEQ: accession NM_001112741.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Clatot,J., Ginn,N., Costain,G. and Goldberg,E.M.
  TITLE     A KCNC1-related neurological disorder due to gain of Kv3.1 function
  JOURNAL   Ann Clin Transl Neurol 10 (1), 111-117 (2023)
   PUBMED   36419348
  REMARK    GeneRIF: A KCNC1-related neurological disorder due to gain of Kv3.1
            function.
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Chi,G., Liang,Q., Sridhar,A., Cowgill,J.B., Sader,K., Radjainia,M.,
            Qian,P., Castro-Hartmann,P., Venkaya,S., Singh,N.K., McKinley,G.,
            Fernandez-Cid,A., Mukhopadhyay,S.M.M., Burgess-Brown,N.A.,
            Delemotte,L., Covarrubias,M. and Durr,K.L.
  TITLE     Cryo-EM structure of the human Kv3.1 channel reveals gating control
            by the cytoplasmic T1 domain
  JOURNAL   Nat Commun 13 (1), 4087 (2022)
   PUBMED   35840580
  REMARK    GeneRIF: Cryo-EM structure of the human Kv3.1 channel reveals
            gating control by the cytoplasmic T1 domain.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Maatoug,S., Cheikh,A., Khamessi,O., Tabka,H., Landoulsi,Z.,
            Guigonis,J.M., Diochot,S., Bendahhou,S. and Benkhalifa,R.
  TITLE     Cross Pharmacological, Biochemical and Computational Studies of a
            Human Kv3.1b Inhibitor from Androctonus australis Venom
  JOURNAL   Int J Mol Sci 22 (22), 12290 (2021)
   PUBMED   34830172
  REMARK    GeneRIF: Cross Pharmacological, Biochemical and Computational
            Studies of a Human Kv3.1b Inhibitor from Androctonus australis
            Venom.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 585)
  AUTHORS   Zhang,Y., Ali,S.R., Nabbout,R., Barcia,G. and Kaczmarek,L.K.
  TITLE     A KCNC1 mutation in epilepsy of infancy with focal migrating
            seizures produces functional channels that fail to be regulated by
            PKC phosphorylation
  JOURNAL   J Neurophysiol 126 (2), 532-539 (2021)
   PUBMED   34232791
  REMARK    GeneRIF: A KCNC1 mutation in epilepsy of infancy with focal
            migrating seizures produces functional channels that fail to be
            regulated by PKC phosphorylation.
REFERENCE   5  (residues 1 to 585)
  AUTHORS   Chen,S., Xiao,L., Peng,H., Wang,Z. and Xie,J.
  TITLE     Methylation gene KCNC1 is associated with overall survival in
            patients with seminoma
  JOURNAL   Oncol Rep 45 (5) (2021)
   PUBMED   34105734
  REMARK    GeneRIF: Methylation gene KCNC1 is associated with overall survival
            in patients with seminoma.
REFERENCE   6  (residues 1 to 585)
  AUTHORS   Xu,J., Yu,W., Jan,Y.N., Jan,L.Y. and Li,M.
  TITLE     Assembly of voltage-gated potassium channels. Conserved hydrophilic
            motifs determine subfamily-specific interactions between the
            alpha-subunits
  JOURNAL   J Biol Chem 270 (42), 24761-24768 (1995)
   PUBMED   7559593
REFERENCE   7  (residues 1 to 585)
  AUTHORS   Ried,T., Rudy,B., Vega-Saenz de Miera,E., Lau,D., Ward,D.C. and
            Sen,K.
  TITLE     Localization of a highly conserved human potassium channel gene
            (NGK2-KV4; KCNC1) to chromosome 11p15
  JOURNAL   Genomics 15 (2), 405-411 (1993)
   PUBMED   8449507
REFERENCE   8  (residues 1 to 585)
  AUTHORS   Ginn,N. and Goldberg,E.M.
  TITLE     KCNC1-Related Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41411464
REFERENCE   9  (residues 1 to 585)
  AUTHORS   Grissmer,S., Ghanshani,S., Dethlefs,B., McPherson,J.D.,
            Wasmuth,J.J., Gutman,G.A., Cahalan,M.D. and Chandy,K.G.
  TITLE     The Shaw-related potassium channel gene, Kv3.1, on human chromosome
            11, encodes the type l K+ channel in T cells
  JOURNAL   J Biol Chem 267 (29), 20971-20979 (1992)
   PUBMED   1400413
REFERENCE   10 (residues 1 to 585)
  AUTHORS   Perney,T.M., Marshall,J., Martin,K.A., Hockfield,S. and
            Kaczmarek,L.K.
  TITLE     Expression of the mRNAs for the Kv3.1 potassium channel gene in the
            adult and developing rat brain
  JOURNAL   J Neurophysiol 68 (3), 756-766 (1992)
   PUBMED   1432046
  REMARK    GeneRIF: Describes two rat isoforms of Kv3.1, alpha is the longer
            one and beta is the shorter one
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124301.6, AC124056.8 and
            AC124078.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of a family of integral
            membrane proteins that mediate the voltage-dependent potassium ion
            permeability of excitable membranes. Alternative splicing is
            thought to result in two transcript variants encoding isoforms that
            differ at their C-termini. These isoforms have had conflicting
            names in the literature: the longer isoform has been called both
            'b' and 'alpha', while the shorter isoform has been called both 'a'
            and 'beta' (PMIDs 1432046, 12091563). [provided by RefSeq, Oct
            2014].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments and orthologous data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.879985.1,
                                           SRR1803617.159507.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265969.8/ ENSP00000265969.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.1"
     Protein         1..585
                     /product="voltage-gated potassium channel KCNC1 isoform 1"
                     /note="voltage-gated potassium channel protein KV3.1;
                     voltage-gated potassium channel subunit Kv4; voltage-gated
                     potassium channel KCNC1; potassium channel, voltage gated
                     Shaw related subfamily C, member 1"
                     /calculated_mol_wt=65740
     Region          6..122
                     /region_name="BTB_KCNC1_3"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in potassium
                     voltage-gated channel subfamily C members KCNC1 and KCNC3;
                     cd18414"
                     /db_xref="CDD:349721"
     Site            order(13,15..22,25,56,58..59,62,65,69,72,75,77,85..86,89)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:349721"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25122; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     Region          121..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48547.1)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25122; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25122; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25122; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P15388; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     Region          189..447
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            191..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48547.1)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     Site            229
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     Site            248..267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48547.1)"
     Site            277..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48547.1)"
     Site            309..331
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48547.1)"
     Site            345..366
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48547.1)"
     Region          400..405
                     /region_name="Selectivity filter. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P48547.1)"
     Site            415..436
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48547.1)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P15388; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P15388; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     CDS             1..585
                     /gene="KCNC1"
                     /gene_synonym="EPM7; KV3.1; KV4; NGK2"
                     /coded_by="NM_001112741.2:1223..2980"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44547.1"
                     /db_xref="GeneID:3746"
                     /db_xref="HGNC:HGNC:6233"
                     /db_xref="MIM:176258"
ORIGIN      
        1 mgqgdeseri vinvggtrhq tyrstlrtlp gtrlawlaep dahshfdydp radefffdrh
       61 pgvfahilny yrtgklhcpa dvcgplyeee lafwgidetd vepccwmtyr qhrdaeeald
      121 sfggapldns addadadgpg dsgdgedele mtkrlalsds pdgrpggfwr rwqpriwalf
      181 edpyssryar yvafaslffi lvsittfcle therfnpivn kteienvrng tqvryyreae
      241 teafltyieg vcvvwftfef lmrvifcpnk vefiknslni idfvailpfy levglsglss
      301 kaakdvlgfl rvvrfvrilr ifkltrhfvg lrvlghtlra stneflllii flalgvlifa
      361 tmiyyaerig aqpndpsase hthfknipig fwwavvtmtt lgygdmypqt wsgmlvgalc
      421 alagvltiam pvpvivnnfg myyslamakq klpkkkkkhi prppqlgspn ycksvvnsph
      481 hstqsdtcpl aqeeileinr adsklngeva kaalanedcp hidqaltpde glpftrsgtr
      541 erygpcflls tgeyacppgg gmrkdlckes pviakympte avrvt
//
LOCUS       NP_004967                511 aa            linear   PRI 22-DEC-2025
DEFINITION  voltage-gated potassium channel KCNC1 isoform 2 [Homo sapiens].
ACCESSION   NP_004967
VERSION     NP_004967.1
DBSOURCE    REFSEQ: accession NM_004976.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Clatot,J., Ginn,N., Costain,G. and Goldberg,E.M.
  TITLE     A KCNC1-related neurological disorder due to gain of Kv3.1 function
  JOURNAL   Ann Clin Transl Neurol 10 (1), 111-117 (2023)
   PUBMED   36419348
  REMARK    GeneRIF: A KCNC1-related neurological disorder due to gain of Kv3.1
            function.
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Chi,G., Liang,Q., Sridhar,A., Cowgill,J.B., Sader,K., Radjainia,M.,
            Qian,P., Castro-Hartmann,P., Venkaya,S., Singh,N.K., McKinley,G.,
            Fernandez-Cid,A., Mukhopadhyay,S.M.M., Burgess-Brown,N.A.,
            Delemotte,L., Covarrubias,M. and Durr,K.L.
  TITLE     Cryo-EM structure of the human Kv3.1 channel reveals gating control
            by the cytoplasmic T1 domain
  JOURNAL   Nat Commun 13 (1), 4087 (2022)
   PUBMED   35840580
  REMARK    GeneRIF: Cryo-EM structure of the human Kv3.1 channel reveals
            gating control by the cytoplasmic T1 domain.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Maatoug,S., Cheikh,A., Khamessi,O., Tabka,H., Landoulsi,Z.,
            Guigonis,J.M., Diochot,S., Bendahhou,S. and Benkhalifa,R.
  TITLE     Cross Pharmacological, Biochemical and Computational Studies of a
            Human Kv3.1b Inhibitor from Androctonus australis Venom
  JOURNAL   Int J Mol Sci 22 (22), 12290 (2021)
   PUBMED   34830172
  REMARK    GeneRIF: Cross Pharmacological, Biochemical and Computational
            Studies of a Human Kv3.1b Inhibitor from Androctonus australis
            Venom.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Zhang,Y., Ali,S.R., Nabbout,R., Barcia,G. and Kaczmarek,L.K.
  TITLE     A KCNC1 mutation in epilepsy of infancy with focal migrating
            seizures produces functional channels that fail to be regulated by
            PKC phosphorylation
  JOURNAL   J Neurophysiol 126 (2), 532-539 (2021)
   PUBMED   34232791
  REMARK    GeneRIF: A KCNC1 mutation in epilepsy of infancy with focal
            migrating seizures produces functional channels that fail to be
            regulated by PKC phosphorylation.
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Chen,S., Xiao,L., Peng,H., Wang,Z. and Xie,J.
  TITLE     Methylation gene KCNC1 is associated with overall survival in
            patients with seminoma
  JOURNAL   Oncol Rep 45 (5) (2021)
   PUBMED   34105734
  REMARK    GeneRIF: Methylation gene KCNC1 is associated with overall survival
            in patients with seminoma.
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Xu,J., Yu,W., Jan,Y.N., Jan,L.Y. and Li,M.
  TITLE     Assembly of voltage-gated potassium channels. Conserved hydrophilic
            motifs determine subfamily-specific interactions between the
            alpha-subunits
  JOURNAL   J Biol Chem 270 (42), 24761-24768 (1995)
   PUBMED   7559593
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Ried,T., Rudy,B., Vega-Saenz de Miera,E., Lau,D., Ward,D.C. and
            Sen,K.
  TITLE     Localization of a highly conserved human potassium channel gene
            (NGK2-KV4; KCNC1) to chromosome 11p15
  JOURNAL   Genomics 15 (2), 405-411 (1993)
   PUBMED   8449507
REFERENCE   8  (residues 1 to 511)
  AUTHORS   Ginn,N. and Goldberg,E.M.
  TITLE     KCNC1-Related Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   41411464
REFERENCE   9  (residues 1 to 511)
  AUTHORS   Grissmer,S., Ghanshani,S., Dethlefs,B., McPherson,J.D.,
            Wasmuth,J.J., Gutman,G.A., Cahalan,M.D. and Chandy,K.G.
  TITLE     The Shaw-related potassium channel gene, Kv3.1, on human chromosome
            11, encodes the type l K+ channel in T cells
  JOURNAL   J Biol Chem 267 (29), 20971-20979 (1992)
   PUBMED   1400413
REFERENCE   10 (residues 1 to 511)
  AUTHORS   Perney,T.M., Marshall,J., Martin,K.A., Hockfield,S. and
            Kaczmarek,L.K.
  TITLE     Expression of the mRNAs for the Kv3.1 potassium channel gene in the
            adult and developing rat brain
  JOURNAL   J Neurophysiol 68 (3), 756-766 (1992)
   PUBMED   1432046
  REMARK    GeneRIF: Describes two rat isoforms of Kv3.1, alpha is the longer
            one and beta is the shorter one
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DN993192.1, BC107129.2,
            AC124056.8, AK125480.1 and AW452561.1.
            
            Summary: This gene encodes a member of a family of integral
            membrane proteins that mediate the voltage-dependent potassium ion
            permeability of excitable membranes. Alternative splicing is
            thought to result in two transcript variants encoding isoforms that
            differ at their C-termini. These isoforms have had conflicting
            names in the literature: the longer isoform has been called both
            'b' and 'alpha', while the shorter isoform has been called both 'a'
            and 'beta' (PMIDs 1432046, 12091563). [provided by RefSeq, Oct
            2014].
            
            Transcript Variant: This variant (2) lacks two exons and its 3'
            exon extends past a splice site used in variant 1, resulting in a
            distinct 3' coding region and 3' UTR, compared to variant 1. The
            encoded isoform (2) has a shorter and distinct C-terminus, compared
            to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.250966.1,
                                           SRR1803614.44334.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.1"
     Protein         1..511
                     /product="voltage-gated potassium channel KCNC1 isoform 2"
                     /note="voltage-gated potassium channel protein KV3.1;
                     voltage-gated potassium channel subunit Kv4; voltage-gated
                     potassium channel KCNC1; potassium channel, voltage gated
                     Shaw related subfamily C, member 1"
                     /calculated_mol_wt=57812
     Region          6..122
                     /region_name="BTB_KCNC1_3"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in potassium
                     voltage-gated channel subfamily C members KCNC1 and KCNC3;
                     cd18414"
                     /db_xref="CDD:349721"
     Site            order(13,15..22,25,56,58..59,62,65,69,72,75,77,85..86,89)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:349721"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25122; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     Region          121..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48547.1)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25122; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25122; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25122; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P15388; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     Region          189..447
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            191..209
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48547.1)"
     Site            220
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     Site            229
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     Site            248..267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48547.1)"
     Site            277..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48547.1)"
     Site            309..331
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48547.1)"
     Site            345..366
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48547.1)"
     Region          400..405
                     /region_name="Selectivity filter. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P48547.1)"
     Site            415..436
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48547.1)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P15388; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P15388; propagated from
                     UniProtKB/Swiss-Prot (P48547.1)"
     CDS             1..511
                     /gene="KCNC1"
                     /gene_synonym="EPM7; KV3.1; KV4; NGK2"
                     /coded_by="NM_004976.4:56..1591"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS7827.1"
                     /db_xref="GeneID:3746"
                     /db_xref="HGNC:HGNC:6233"
                     /db_xref="MIM:176258"
ORIGIN      
        1 mgqgdeseri vinvggtrhq tyrstlrtlp gtrlawlaep dahshfdydp radefffdrh
       61 pgvfahilny yrtgklhcpa dvcgplyeee lafwgidetd vepccwmtyr qhrdaeeald
      121 sfggapldns addadadgpg dsgdgedele mtkrlalsds pdgrpggfwr rwqpriwalf
      181 edpyssryar yvafaslffi lvsittfcle therfnpivn kteienvrng tqvryyreae
      241 teafltyieg vcvvwftfef lmrvifcpnk vefiknslni idfvailpfy levglsglss
      301 kaakdvlgfl rvvrfvrilr ifkltrhfvg lrvlghtlra stneflllii flalgvlifa
      361 tmiyyaerig aqpndpsase hthfknipig fwwavvtmtt lgygdmypqt wsgmlvgalc
      421 alagvltiam pvpvivnnfg myyslamakq klpkkkkkhi prppqlgspn ycksvvnsph
      481 hstqsdtcpl aqeeileinr agrkplrgms i
//
LOCUS       NP_065169               1053 aa            linear   PRI 23-DEC-2025
DEFINITION  sal-like protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_065169
VERSION     NP_065169.1
DBSOURCE    REFSEQ: accession NM_020436.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1053)
  AUTHORS   Wang,T., Jin,Y., Wang,M., Chen,B., Sun,J., Zhang,J., Yang,H.,
            Deng,X., Cao,X., Wang,L. and Tang,Y.
  TITLE     SALL4 in gastrointestinal tract cancers: upstream and downstream
            regulatory mechanisms
  JOURNAL   Mol Med 30 (1), 46 (2024)
   PUBMED   38584262
  REMARK    GeneRIF: SALL4 in gastrointestinal tract cancers: upstream and
            downstream regulatory mechanisms.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1053)
  AUTHORS   Lospinoso Severini,L., Loricchio,E., Navacci,S., Basili,I.,
            Alfonsi,R., Bernardi,F., Moretti,M., Conenna,M., Cucinotta,A.,
            Coni,S., Petroni,M., De Smaele,E., Giannini,G., Maroder,M.,
            Canettieri,G., Mastronuzzi,A., Guardavaccaro,D., Ayrault,O.,
            Infante,P., Bufalieri,F. and Di Marcotullio,L.
  TITLE     SALL4 is a CRL3REN/KCTD11 substrate that drives Sonic
            Hedgehog-dependent medulloblastoma
  JOURNAL   Cell Death Differ 31 (2), 170-187 (2024)
   PUBMED   38062245
  REMARK    GeneRIF: SALL4 is a CRL3[REN/KCTD11] substrate that drives Sonic
            Hedgehog-dependent medulloblastoma.
REFERENCE   3  (residues 1 to 1053)
  AUTHORS   Jiang,Y. and Tang,Y.
  TITLE     SALL4 advances the proliferation and tumor cell stemness of colon
            cancer cells through the transcription and regulation of ROBO2
  JOURNAL   Nucleosides Nucleotides Nucleic Acids 43 (3), 249-263 (2024)
   PUBMED   37660281
  REMARK    GeneRIF: SALL4 advances the proliferation and tumor cell stemness
            of colon cancer cells through the transcription and regulation of
            ROBO2.
REFERENCE   4  (residues 1 to 1053)
  AUTHORS   Kodytkova,A., Amaratunga,S.A., Zemkova,D., Maratova,K.,
            Dusatkova,P., Plachy,L., Pruhova,S., Kolouskova,S. and Lebl,J.
  TITLE     SALL4 Phenotype in Four Generations of One Family: An Interplay of
            the Upper Limb, Kidneys, and the Pituitary
  JOURNAL   Horm Res Paediatr 97 (2), 203-210 (2024)
   PUBMED   37611564
  REMARK    GeneRIF: SALL4 Phenotype in Four Generations of One Family: An
            Interplay of the Upper Limb, Kidneys, and the Pituitary.
REFERENCE   5  (residues 1 to 1053)
  AUTHORS   Kohlhase,J., Chitayat,D., Kotzot,D., Ceylaner,S., Froster,U.G.,
            Fuchs,S., Montgomery,T. and Rosler,B.
  TITLE     SALL4 mutations in Okihiro syndrome (Duane-radial ray syndrome),
            acro-renal-ocular syndrome, and related disorders
  JOURNAL   Hum Mutat 26 (3), 176-183 (2005)
   PUBMED   16086360
  REMARK    GeneRIF: analysis of SALL4 defects and associated syndromes
            (including Okihiro syndrome (Duane-radial ray syndrome),
            acro-renal-ocular syndrome) and description of the clinical
            distinctions with similar phenotypes caused by other gene defects
REFERENCE   6  (residues 1 to 1053)
  AUTHORS   Kohlhase,J., Schubert,L., Liebers,M., Rauch,A., Becker,K.,
            Mohammed,S.N., Newbury-Ecob,R. and Reardon,W.
  TITLE     Mutations at the SALL4 locus on chromosome 20 result in a range of
            clinically overlapping phenotypes, including Okihiro syndrome,
            Holt-Oram syndrome, acro-renal-ocular syndrome, and patients
            previously reported to represent thalidomide embryopathy
  JOURNAL   J Med Genet 40 (7), 473-478 (2003)
   PUBMED   12843316
REFERENCE   7  (residues 1 to 1053)
  AUTHORS   Kohlhase,J., Heinrich,M., Schubert,L., Liebers,M., Kispert,A.,
            Laccone,F., Turnpenny,P., Winter,R.M. and Reardon,W.
  TITLE     Okihiro syndrome is caused by SALL4 mutations
  JOURNAL   Hum Mol Genet 11 (23), 2979-2987 (2002)
   PUBMED   12393809
  REMARK    GeneRIF: Okihiro syndrome is caused by SALL4 mutations
REFERENCE   8  (residues 1 to 1053)
  AUTHORS   Al-Baradie,R., Yamada,K., St Hilaire,C., Chan,W.M., Andrews,C.,
            McIntosh,N., Nakano,M., Martonyi,E.J., Raymond,W.R., Okumura,S.,
            Okihiro,M.M. and Engle,E.C.
  TITLE     Duane radial ray syndrome (Okihiro syndrome) maps to 20q13 and
            results from mutations in SALL4, a new member of the SAL family
  JOURNAL   Am J Hum Genet 71 (5), 1195-1199 (2002)
   PUBMED   12395297
  REMARK    GeneRIF: The first identified Duane syndrome gene and the second
            malformation syndrome resulting from mutations in SAL genes.
REFERENCE   9  (residues 1 to 1053)
  AUTHORS   Kohlhase,J.
  TITLE     SALL4-Related Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301547
REFERENCE   10 (residues 1 to 1053)
  AUTHORS   Barry,B.J., Whitman,M.C., Hunter,D.G. and Engle,E.C.
  TITLE     Duane Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301369
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL034420.16, DA666635.1,
            AY172738.1, AA419623.1, AI638036.1, DA747867.1, CN271900.1,
            BE549760.1 and AA854044.1.
            
            Summary: This gene encodes a zinc finger transcription factor
            thought to play a role in the development of abducens motor
            neurons. Defects in this gene are a cause of Duane-radial ray
            syndrome (DRRS). Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001666.1, BC111714.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000217086.9/ ENSP00000217086.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1053
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.2"
     Protein         1..1053
                     /product="sal-like protein 4 isoform 1"
                     /note="sal-like protein 4; zinc finger protein SALL4; zinc
                     finger protein 797"
                     /calculated_mol_wt=112101
     Region          1..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJQ4.1)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23012367; propagated from
                     UniProtKB/Swiss-Prot (Q9UJQ4.1)"
     Region          116..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJQ4.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UJQ4.1)"
     Region          381..>429
                     /region_name="SUF4-like"
                     /note="N-terminal domain of Oryza sativa transcription
                     factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana
                     SUF4 (AtSUF4), and similar proteins; cd20908"
                     /db_xref="CDD:411020"
     Region          384..405
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          384..404
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(389,395,402,404,411,418)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411020"
     Region          412..432
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          412..429
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          483..546
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJQ4.1)"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UJQ4.1)"
     Region          568..588
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(568,571,584,588)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Site            order(573,575,577,579..580,583..584,587,601,603,607..608,
                     611..612,618,633,635,637,639..640,643..644,647)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          580..605
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          596..619
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          626..648
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          628..648
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          694..714
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJQ4.1)"
     Region          736..776
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJQ4.1)"
     Site            776
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UJQ4.1)"
     Region          788..828
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJQ4.1)"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UJQ4.1)"
     Site            852
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23012367; propagated from
                     UniProtKB/Swiss-Prot (Q9UJQ4.1)"
     Region          872..>919
                     /region_name="SUF4-like"
                     /note="N-terminal domain of Oryza sativa transcription
                     factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana
                     SUF4 (AtSUF4), and similar proteins; cd20908"
                     /db_xref="CDD:411020"
     Region          872..893
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          872..892
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(877,883,890,892,899,906)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411020"
     Region          900..920
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          900..919
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          1018..1039
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJQ4.1)"
     Site            1019
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UJQ4.1)"
     CDS             1..1053
                     /gene="SALL4"
                     /gene_synonym="DRRS; HSAL4; IVIC; ZNF797"
                     /coded_by="NM_020436.5:114..3275"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13438.1"
                     /db_xref="GeneID:57167"
                     /db_xref="HGNC:HGNC:15924"
                     /db_xref="MIM:607343"
ORIGIN      
        1 msrrkqakpq hinseedqge qqpqqqtpef adaapaapaa gelgapvnhp gndevasede
       61 atvkrlrree thvcekccae ffsisefleh kknctknppv limndsegpv psedfsgavl
      121 shqptspgsk dchrenggss edmkekpdae svvylkteta lpptpqdisy lakgkvantn
      181 vtlqalrgtk vavnqrsada lpapvpgans ipwvleqilc lqqqqlqqiq lteqiriqvn
      241 mwashalhss gagadtlktl gshmsqqvsa avallsqkag sqglsldalk qaklphanip
      301 satsslspgl apftlkpdgt rvlpnvmsrl psallpqapg svlfqspfst valdtskkgk
      361 gkppnisavd vkpkdeaaly khkckycskv fgtdsslqih lrshtgerpf vcsvcghrft
      421 tkgnlkvhfh rhpqvkanpq lfaefqdkva agngipyals vpdpidepsl sldskpvlvt
      481 tsvglpqnls sgtnpkdltg gslpgdlqpg pspeseggpt lpgvgpnyns praggfqgsg
      541 tpepgsetlk lqqlvenidk attdpnecli chrvlscqss lkmhyrthtg erpfqckicg
      601 rafstkgnlk thlgvhrtnt siktqhscpi cqkkftnavm lqqhirmhmg gqipntplpe
      661 npcdftgsep mtvgengstg aichddvies idveevssqe apsssskvpt plpsihsasp
      721 tlgfammasl dapgkvgpap fnlqrqgsre ngsvesdglt ndssslmgdq eyqsrspdil
      781 ettsfqalsp ansqaesiks kspdagskae ssensrteme grsslpstfi rapptyvkve
      841 vpgtfvgpst lspgmtplla aqprrqakqh gctrcgknfs sasalqiher thtgekpfvc
      901 nicgrafttk gnlkvhymth gannnsarrg rklaientma llgtdgkrvs eifpkeilap
      961 svnvdpvvwn qytsmlnggl avktneisvi qsggvptlpv slgatsvvnn atvskmdgsq
     1021 sgisadvekp satdgvpkhq fphfleenki avs
//
LOCUS       NP_001304960             616 aa            linear   PRI 23-DEC-2025
DEFINITION  sal-like protein 4 isoform 2 [Homo sapiens].
ACCESSION   NP_001304960 XP_011527225
VERSION     NP_001304960.1
DBSOURCE    REFSEQ: accession NM_001318031.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Wang,T., Jin,Y., Wang,M., Chen,B., Sun,J., Zhang,J., Yang,H.,
            Deng,X., Cao,X., Wang,L. and Tang,Y.
  TITLE     SALL4 in gastrointestinal tract cancers: upstream and downstream
            regulatory mechanisms
  JOURNAL   Mol Med 30 (1), 46 (2024)
   PUBMED   38584262
  REMARK    GeneRIF: SALL4 in gastrointestinal tract cancers: upstream and
            downstream regulatory mechanisms.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Lospinoso Severini,L., Loricchio,E., Navacci,S., Basili,I.,
            Alfonsi,R., Bernardi,F., Moretti,M., Conenna,M., Cucinotta,A.,
            Coni,S., Petroni,M., De Smaele,E., Giannini,G., Maroder,M.,
            Canettieri,G., Mastronuzzi,A., Guardavaccaro,D., Ayrault,O.,
            Infante,P., Bufalieri,F. and Di Marcotullio,L.
  TITLE     SALL4 is a CRL3REN/KCTD11 substrate that drives Sonic
            Hedgehog-dependent medulloblastoma
  JOURNAL   Cell Death Differ 31 (2), 170-187 (2024)
   PUBMED   38062245
  REMARK    GeneRIF: SALL4 is a CRL3[REN/KCTD11] substrate that drives Sonic
            Hedgehog-dependent medulloblastoma.
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Jiang,Y. and Tang,Y.
  TITLE     SALL4 advances the proliferation and tumor cell stemness of colon
            cancer cells through the transcription and regulation of ROBO2
  JOURNAL   Nucleosides Nucleotides Nucleic Acids 43 (3), 249-263 (2024)
   PUBMED   37660281
  REMARK    GeneRIF: SALL4 advances the proliferation and tumor cell stemness
            of colon cancer cells through the transcription and regulation of
            ROBO2.
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Kodytkova,A., Amaratunga,S.A., Zemkova,D., Maratova,K.,
            Dusatkova,P., Plachy,L., Pruhova,S., Kolouskova,S. and Lebl,J.
  TITLE     SALL4 Phenotype in Four Generations of One Family: An Interplay of
            the Upper Limb, Kidneys, and the Pituitary
  JOURNAL   Horm Res Paediatr 97 (2), 203-210 (2024)
   PUBMED   37611564
  REMARK    GeneRIF: SALL4 Phenotype in Four Generations of One Family: An
            Interplay of the Upper Limb, Kidneys, and the Pituitary.
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Kohlhase,J., Chitayat,D., Kotzot,D., Ceylaner,S., Froster,U.G.,
            Fuchs,S., Montgomery,T. and Rosler,B.
  TITLE     SALL4 mutations in Okihiro syndrome (Duane-radial ray syndrome),
            acro-renal-ocular syndrome, and related disorders
  JOURNAL   Hum Mutat 26 (3), 176-183 (2005)
   PUBMED   16086360
  REMARK    GeneRIF: analysis of SALL4 defects and associated syndromes
            (including Okihiro syndrome (Duane-radial ray syndrome),
            acro-renal-ocular syndrome) and description of the clinical
            distinctions with similar phenotypes caused by other gene defects
REFERENCE   6  (residues 1 to 616)
  AUTHORS   Kohlhase,J., Schubert,L., Liebers,M., Rauch,A., Becker,K.,
            Mohammed,S.N., Newbury-Ecob,R. and Reardon,W.
  TITLE     Mutations at the SALL4 locus on chromosome 20 result in a range of
            clinically overlapping phenotypes, including Okihiro syndrome,
            Holt-Oram syndrome, acro-renal-ocular syndrome, and patients
            previously reported to represent thalidomide embryopathy
  JOURNAL   J Med Genet 40 (7), 473-478 (2003)
   PUBMED   12843316
REFERENCE   7  (residues 1 to 616)
  AUTHORS   Kohlhase,J., Heinrich,M., Schubert,L., Liebers,M., Kispert,A.,
            Laccone,F., Turnpenny,P., Winter,R.M. and Reardon,W.
  TITLE     Okihiro syndrome is caused by SALL4 mutations
  JOURNAL   Hum Mol Genet 11 (23), 2979-2987 (2002)
   PUBMED   12393809
  REMARK    GeneRIF: Okihiro syndrome is caused by SALL4 mutations
REFERENCE   8  (residues 1 to 616)
  AUTHORS   Al-Baradie,R., Yamada,K., St Hilaire,C., Chan,W.M., Andrews,C.,
            McIntosh,N., Nakano,M., Martonyi,E.J., Raymond,W.R., Okumura,S.,
            Okihiro,M.M. and Engle,E.C.
  TITLE     Duane radial ray syndrome (Okihiro syndrome) maps to 20q13 and
            results from mutations in SALL4, a new member of the SAL family
  JOURNAL   Am J Hum Genet 71 (5), 1195-1199 (2002)
   PUBMED   12395297
  REMARK    GeneRIF: The first identified Duane syndrome gene and the second
            malformation syndrome resulting from mutations in SAL genes.
REFERENCE   9  (residues 1 to 616)
  AUTHORS   Kohlhase,J.
  TITLE     SALL4-Related Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301547
REFERENCE   10 (residues 1 to 616)
  AUTHORS   Barry,B.J., Whitman,M.C., Hunter,D.G. and Engle,E.C.
  TITLE     Duane Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301369
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL034420.16, DA666635.1,
            AY170621.1, AY172738.1, AA419623.1, AI638036.1, DA747867.1,
            CN271900.1, BE549760.1 and AA854044.1.
            
            On Jan 8, 2016 this sequence version replaced XP_011527225.1.
            
            Summary: This gene encodes a zinc finger transcription factor
            thought to play a role in the development of abducens motor
            neurons. Defects in this gene are a cause of Duane-radial ray
            syndrome (DRRS). Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Dec 2015].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region compared to variant 1. The
            encoded isoform (2) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1864606.1,
                                           SRR14038194.3314141.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.2"
     Protein         1..616
                     /product="sal-like protein 4 isoform 2"
                     /note="sal-like protein 4; zinc finger protein SALL4; zinc
                     finger protein 797"
                     /calculated_mol_wt=65578
     Region          435..>482
                     /region_name="SUF4-like"
                     /note="N-terminal domain of Oryza sativa transcription
                     factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana
                     SUF4 (AtSUF4), and similar proteins; cd20908"
                     /db_xref="CDD:411020"
     Region          435..456
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          435..455
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(440,446,453,455,462,469)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411020"
     Region          463..483
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          463..482
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     CDS             1..616
                     /gene="SALL4"
                     /gene_synonym="DRRS; HSAL4; IVIC; ZNF797"
                     /coded_by="NM_001318031.2:114..1964"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS82629.1"
                     /db_xref="GeneID:57167"
                     /db_xref="HGNC:HGNC:15924"
                     /db_xref="MIM:607343"
ORIGIN      
        1 msrrkqakpq hinseedqge qqpqqqtpef adaapaapaa gelgapvnhp gndevasede
       61 atvkrlrree thvcekccae ffsisefleh kknctknppv limndsegpv psedfsgavl
      121 shqptspgsk dchrenggss edmkekpdae svvylkteta lpptpqdisy lakgkvantn
      181 vtlqalrgtk vavnqrsada lpapvpgans ipwvleqilc lqqqqlqqiq lteqiriqvn
      241 mwashalhss gagadtlktl gshmsqqvsa avallsqkag sqglsldalk qaklphanip
      301 satsslspgl apftlkpdgt rvlpnvmsrl psallpqapg svlfqspfst valdtskkgk
      361 gkppnisavd vkpkdeaaly khkcrsslps tfirapptyv kvevpgtfvg pstlspgmtp
      421 llaaqprrqa kqhgctrcgk nfssasalqi herthtgekp fvcnicgraf ttkgnlkvhy
      481 mthgannnsa rrgrklaien tmallgtdgk rvseifpkei lapsvnvdpv vwnqytsmln
      541 gglavktnei sviqsggvpt lpvslgatsv vnnatvskmd gsqsgisadv ekpsatdgvp
      601 khqfphflee nkiavs
//
LOCUS       NP_004450               2903 aa            linear   PRI 24-DEC-2025
DEFINITION  nucleosome-remodeling factor subunit BPTF isoform 2 [Homo sapiens].
ACCESSION   NP_004450
VERSION     NP_004450.3
DBSOURCE    REFSEQ: accession NM_004459.7
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2903)
  AUTHORS   Noura,M., Tomita,S., Yasuda,T., Tsuzuki,S., Kiyoi,H. and
            Hayakawa,F.
  TITLE     NUP98-BPTF promotes oncogenic transformation through PIM1
            upregulation
  JOURNAL   Cancer Med 13 (13), e7445 (2024)
   PUBMED   38940430
  REMARK    GeneRIF: NUP98-BPTF promotes oncogenic transformation through PIM1
            upregulation.
REFERENCE   2  (residues 1 to 2903)
  AUTHORS   Yogev,Y., Schaffer,M., Shlapobersky,M., Jean,M.M., Wormser,O.,
            Drabkin,M., Halperin,D., Kassem,R., Livoff,A., Tsitrina,A.A.,
            Asna,N. and Birk,O.S.
  TITLE     A role of BPTF in viral oncogenicity delineated through studies of
            heritable Kaposi sarcoma
  JOURNAL   J Med Virol 96 (2), e29436 (2024)
   PUBMED   38380509
  REMARK    GeneRIF: A role of BPTF in viral oncogenicity delineated through
            studies of heritable Kaposi sarcoma.
REFERENCE   3  (residues 1 to 2903)
  AUTHORS   Gao,S., Zhang,W., Ma,J. and Ni,X.
  TITLE     PHF6 recruits BPTF to promote HIF-dependent pathway and progression
            in YAP-high breast cancer
  JOURNAL   J Transl Med 21 (1), 220 (2023)
   PUBMED   36967443
  REMARK    GeneRIF: PHF6 recruits BPTF to promote HIF-dependent pathway and
            progression in YAP-high breast cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2903)
  AUTHORS   Wu,W. and Chen,R.
  TITLE     The effect of growth hormone treatment in children with novel BPTF
            gene variants: A report of two cases and literature review
  JOURNAL   Mol Genet Genomic Med 11 (1), e2066 (2023)
   PUBMED   36153657
  REMARK    GeneRIF: The effect of growth hormone treatment in children with
            novel BPTF gene variants: A report of two cases and literature
            review.
            Review article
REFERENCE   5  (residues 1 to 2903)
  AUTHORS   Dai,M., Hua,C., Wang,M., Gao,L., Jiang,L. and Liu,Y.
  TITLE     Targeting regulation of VEGF by BPTF in non-small cell lung cancer
            and its potential clinical significance
  JOURNAL   Eur J Med Res 27 (1), 299 (2022)
   PUBMED   36529788
  REMARK    GeneRIF: Targeting regulation of VEGF by BPTF in non-small cell
            lung cancer and its potential clinical significance.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2903)
  AUTHORS   Jordan-Sciutto,K.L., Dragich,J.M. and Bowser,R.
  TITLE     DNA binding activity of the fetal Alz-50 clone 1 (FAC1) protein is
            enhanced by phosphorylation
  JOURNAL   Biochem Biophys Res Commun 260 (3), 785-789 (1999)
   PUBMED   10403843
REFERENCE   7  (residues 1 to 2903)
  AUTHORS   Mu,X., Springer,J.E. and Bowser,R.
  TITLE     FAC1 expression and localization in motor neurons of developing,
            adult, and amyotrophic lateral sclerosis spinal cord
  JOURNAL   Exp Neurol 146 (1), 17-24 (1997)
   PUBMED   9225734
REFERENCE   8  (residues 1 to 2903)
  AUTHORS   Bowser,R.
  TITLE     Assignment of the human FAC1 gene to chromosome 17q24 by
            fluorescence in situ hybridization
  JOURNAL   Genomics 38 (3), 455-457 (1996)
   PUBMED   8975731
REFERENCE   9  (residues 1 to 2903)
  AUTHORS   Zhu,P. and Bowser,R.
  TITLE     Identification and analysis of the complete cDNA sequence for the
            human FAC1 gene
  JOURNAL   Biochim Biophys Acta 1309 (1-2), 5-8 (1996)
   PUBMED   8950167
REFERENCE   10 (residues 1 to 2903)
  AUTHORS   Bowser,R., Giambrone,A. and Davies,P.
  TITLE     FAC1, a novel gene identified with the monoclonal antibody Alz50,
            is developmentally regulated in human brain
  JOURNAL   Dev Neurosci 17 (1), 20-37 (1995)
   PUBMED   7621746
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006534.10, BC037422.1,
            AY282495.1, AB032251.1, AK025776.1, AK022570.1, AL833375.1 and
            AC134407.6.
            
            On Dec 5, 2003 this sequence version replaced NP_004450.2.
            
            Summary: This gene was identified by the reactivity of its encoded
            protein to a monoclonal antibody prepared against brain homogenates
            from patients with Alzheimer's disease. Analysis of the original
            protein (fetal Alz-50 reactive clone 1, or FAC1), identified as an
            810 aa protein containing a DNA-binding domain and a zinc finger
            motif, suggested it might play a role in the regulation of
            transcription. High levels of FAC1 were detected in fetal brain and
            in patients with neurodegenerative diseases. The protein encoded by
            this gene is actually much larger than originally thought, and it
            also contains a C-terminal bromodomain characteristic of proteins
            that regulate transcription during proliferation. The encoded
            protein is highly similar to the largest subunit of the Drosophila
            NURF (nucleosome remodeling factor) complex. In Drosophila, the
            NURF complex, which catalyzes nucleosome sliding on DNA and
            interacts with sequence-specific transcription factors, is
            necessary for the chromatin remodeling required for transcription.
            Two alternative transcripts encoding different isoforms have been
            described completely. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) contains two additional
            in-frame exons in the 5' coding region and uses an alternate
            in-frame splice site in the 3' coding region, compared to variant
            1. The encoded isoform (2) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY282495.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2903
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..2903
                     /product="nucleosome-remodeling factor subunit BPTF
                     isoform 2"
                     /note="fetal Alzheimer antigen; fetal Alz-50 reactive
                     clone 1; nucleosome-remodeling factor subunit BPTF;
                     nucleosome remodeling factor, large subunit; bromodomain
                     and PHD domain transcription factor; fetal Alz-50 clone 1
                     protein; bromodomain and PHD finger-containing
                     transcription factor"
                     /calculated_mol_wt=322088
     Region          240..299
                     /region_name="DDT"
                     /note="domain in different transcription and chromosome
                     remodeling factors; smart00571"
                     /db_xref="CDD:214726"
     Region          392..434
                     /region_name="PHD1_BPTF"
                     /note="PHD finger 1 found in bromodomain and PHD
                     finger-containing transcription factor (BPTF); cd15559"
                     /db_xref="CDD:277034"
     Site            order(392,401..405,409,429)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277034"
     Region          456..522
                     /region_name="WSD"
                     /note="Williams-Beuren syndrome DDT (WSD), D-TOX E motif;
                     pfam15613"
                     /db_xref="CDD:464775"
     Region          <2120..2500
                     /region_name="Glutenin_hmw"
                     /note="High molecular weight glutenin subunit; pfam03157"
                     /db_xref="CDD:367362"
     Region          2726..2772
                     /region_name="PHD2_3_BPTF"
                     /note="PHD finger 2 and 3 found in bromodomain and PHD
                     finger-containing transcription factor (BPTF); cd15560"
                     /db_xref="CDD:277035"
     Site            order(2726,2733,2735,2738..2743,2746,2748,2758,2761,
                     2764..2765)
                     /site_type="other"
                     /note="histone H3 binding site [polypeptide binding]"
                     /db_xref="CDD:277035"
     Region          2788..2888
                     /region_name="Bromo_gcn5_like"
                     /note="Bromodomain; Gcn5_like subfamily. Gcn5p is a
                     histone acetyltransferase (HAT) which mediates acetylation
                     of histones at lysine residues; such acetylation is
                     generally correlated with the activation of transcription.
                     Bromodomains are 110 amino acid long...; cd05509"
                     /db_xref="CDD:99941"
     Site            order(2813,2818,2821,2860,2864,2870)
                     /site_type="active"
                     /note="acetyllysine binding site [active]"
                     /db_xref="CDD:99941"
     CDS             1..2903
                     /gene="BPTF"
                     /gene_synonym="FAC1; FALZ; NEDDFL; NURF301"
                     /coded_by="NM_004459.7:223..8934"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:2186"
                     /db_xref="HGNC:HGNC:3581"
                     /db_xref="MIM:601819"
ORIGIN      
        1 mrgrrgrppk qpaapaaerc apappppppp ptsgpigglr srhrgssrgr waaaqaevap
       61 ktrlssprgg sssrrkpppp ppappstsap grggrggggg rtgggggggh larttaarra
      121 vnkvvyddhe seeeeeeedm vseeeeeedg daeetqdsed deedemeedd ddsdypeeme
      181 dddddasyct essfrshsty sstpgrrkpr vhrprspile ekdipplefp kssedlmvpn
      241 ehimnviaiy evlrnfgtvl rlspfrfedf caalvsqeqc tlmaemhvvl lkavlreedt
      301 snttfgpadl kdsvnstlyf idgmtwpevl rvycesdkey hhvlpyqeae dypygpvenk
      361 ikvlqflvdq flttniaree lmsegviqyd dhcrvchklg dllccetcsa vyhlecvkpp
      421 leevpedewq cevcvahkvp gvtdcvaeiq knkpyirhep igydrsrrky wflnrrliie
      481 edtenenekk iwyystkvql aelidcldkd yweaelckil eemreeihrh mditedltnk
      541 argsnksfla aaneeilesi rakkgdidnv kspeetekdk netendskda eknreefedq
      601 slekdsddkt pdddpeqgks eeptevgdkg nsvsanlgdn ttnatseets psegrspvgc
      661 lsetpdssnm aekkvaselp qdvpeepnkt cessntsatt tsiqpnlens nssselnssq
      721 sesakaaddp engereshtp vsiqeeivgd fkseksngel sespgagkga sgstriitrl
      781 rnpdsklsql ksqqvaaaah eanklfkegk evlvvnsqge isrlstkkev imkgninnyf
      841 klgqegkyrv yhnqystnsf alnkhqhred hdkrrhlahk fcltpagefk wngsvhgskv
      901 ltistlrlti tqlennipss flhpnwashr anwikavqmc skprefalal ailecavkpv
      961 vmlpiwresl ghtrlhrmts iereekekvk kkekkqeeee tmqqatwvky tfpvkhqvwk
     1021 qkgeeyrvtg yggwswiskt hvyrfvpklp gntnvnyrks legtknnmde nmdesdkrkc
     1081 srspkkikie pdsekdevkg sdaakgadqn emdiskitek kdqdvkelld sdsdkpckee
     1141 pmevdddmkt eshvncqess qvdvvnvseg fhlrtsykkk tksskldgll errikqftle
     1201 ekqrlekikl eggikgigkt stnssknlse spvitkakeg cqsdsmrqeq spnanndqpe
     1261 dliqgcsesd ssvlrmsdps httnklypkd rvlddvsirs petkcpkqns iendieekvs
     1321 dlasrgqeps ksktkgndff iddsklasad digtlicknk kpliqeesdt ivsssksalh
     1381 ssvpkstndr datplsramd fegklgcdse snstlenssd tvsiqdssee dmivqnsnes
     1441 iseqfrtreq dvevleplkc elvsgestgn cedrlpvkgt eangkkpsqq kkleerpvnk
     1501 csdqiklknt tdkknnenre sekkgqrtst fqingkdnkp kiylkgeclk eisesrvvsg
     1561 nvepkvnnin kiipendiks ltvkesairp fingdvimed fnernssetk shllsssdae
     1621 gnyrdsletl pstkesdstq tttpsascpe snsvnqvedm eietsevkkv tsspitseee
     1681 snlsndfide nglpinknen vngeskrktv itevttmtst vatesktvik vekgdkqtvv
     1741 sstencakst vttttttvtk lstpstggsv diisvkeqsk tvvtttvtds ltttggtlvt
     1801 smtvskeyst rdkvklmkfs rpkktrsgta lpsyrkfvtk sskksifvlp nddlkklark
     1861 ggirevpyfn ynakpaldiw pypsprptfg itwryrlqtv kslagvslml rllwaslrwd
     1921 dmaakappgg gttrtetset eittteiikr rdvgpygirs eycirkiicp igvpetpket
     1981 ptpqrkglrs salrpkrpet pkqtgpviie twvaeeelel weirafaerv ekekaqaveq
     2041 qakkrleqqk ptviatstts ptssttstis paqkvmvapi sgsvttgtkm vlttkvgspa
     2101 tvtfqqnknf hqtfatwvkq gqsnsgvvqv qqkvlgiips stgtsqqtft sfqprtatvt
     2161 irpntsgsgg ttsnsqvitg pqirpgmtvi rtplqqstlg kaiirtpvmv qpgapqqvmt
     2221 qiirgqpvst avsapntvss tpgqksltsa tstsniqssa sqpprpqqgq vkltmaqltq
     2281 ltqghggnqg ltvviqgqgq ttgqlqlipq gvtvlpgpgq qlmqaampng tvqrflftpl
     2341 attattastt tttvsttaag tgeqrqskls pqmqvhqdkt lppaqsssvg paeaqpqtaq
     2401 psaqpqpqtq pqspaqpevq tqpevqtqtt vsshvpseaq pthaqsskpq vaaqsqpqsn
     2461 vqgqspvrvq spsqtrirps tpsqlspgqq sqvqtttsqp ipiqphtslq ipsqgqpqsq
     2521 pqvvmkhnav iehlkqkksm tpaereenqr mivcnqvmky ildkidkeek qaakkrkree
     2581 sveqkrskqn atklsallfk hkeqlraeil kkralldkdl qievqeelkr dlkikkekdl
     2641 mqlaqatava apcppvtpap pappapppsp ppppavqhtg llstptlpaa sqkrkreeek
     2701 dssskskkkk misttsketk kdtklycick tpydeskfyi gcdrcqnwyh grcvgilqse
     2761 aelideyvcp qcqstedamt vltpltekdy eglkrvlrsl qahkmawpfl epvdpndapd
     2821 yygvikepmd latmeervqr ryyekltefv admtkifdnc ryynpsdspf yqcaevlesf
     2881 fvqklkgfka srshnnklqs tas
//
LOCUS       NP_998820               2634 aa            linear   PRI 24-DEC-2025
DEFINITION  serine/threonine-protein kinase WNK1 isoform 3 [Homo sapiens].
ACCESSION   NP_998820
VERSION     NP_998820.3
DBSOURCE    REFSEQ: accession NM_213655.5
KEYWORDS    RefSeq; MANE Plus Clinical.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2634)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2634)
  AUTHORS   Li,L., Xie,D., Yu,S., Ma,M., Fan,K., Chen,J., Xiu,M., Xie,K., Li,Y.
            and Gao,Y.
  TITLE     WNK1 Interaction with KEAP1 Promotes NRF2 Stabilization to Enhance
            the Oxidative Stress Response in Hepatocellular Carcinoma
  JOURNAL   Cancer Res 84 (17), 2776-2791 (2024)
   PUBMED   38885324
  REMARK    GeneRIF: WNK1 Interaction with KEAP1 Promotes NRF2 Stabilization to
            Enhance the Oxidative Stress Response in Hepatocellular Carcinoma.
REFERENCE   3  (residues 1 to 2634)
  AUTHORS   Ma,Y., Zong,H., Pan,P., Shang,H. and Yang,X.
  TITLE     The CREB1/WNK1 axis promotes the tumorigenesis of ovarian cancer
            via regulating HIF-1
  JOURNAL   Exp Cell Res 438 (1), 114006 (2024)
   PUBMED   38599542
  REMARK    GeneRIF: The CREB1/WNK1 axis promotes the tumorigenesis of ovarian
            cancer via regulating HIF-1.
REFERENCE   4  (residues 1 to 2634)
  AUTHORS   Newhouse,S., Farrall,M., Wallace,C., Hoti,M., Burke,B., Howard,P.,
            Onipinla,A., Lee,K., Shaw-Hawkins,S., Dobson,R., Brown,M.,
            Samani,N.J., Dominiczak,A.F., Connell,J.M., Lathrop,G.M.,
            Kooner,J., Chambers,J., Elliott,P., Clarke,R., Collins,R., Laan,M.,
            Org,E., Juhanson,P., Veldre,G., Viigimaa,M., Eyheramendy,S.,
            Cappuccio,F.P., Ji,C., Iacone,R., Strazzullo,P., Kumari,M.,
            Marmot,M., Brunner,E., Caulfield,M. and Munroe,P.B.
  TITLE     Polymorphisms in the WNK1 gene are associated with blood pressure
            variation and urinary potassium excretion
  JOURNAL   PLoS One 4 (4), e5003 (2009)
   PUBMED   19347040
  REMARK    GeneRIF: data indicates that multiple rare and common WNK1 variants
            contribute to BP variation and hypertension, and provide compelling
            evidence to initiate further genetic and functional studies to
            explore the role of WNK1 in BP regulation and EH
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 2634)
  AUTHORS   Shekarabi,M., Girard,N., Riviere,J.B., Dion,P., Houle,M.,
            Toulouse,A., Lafreniere,R.G., Vercauteren,F., Hince,P.,
            Laganiere,J., Rochefort,D., Faivre,L., Samuels,M. and Rouleau,G.A.
  TITLE     Mutations in the nervous system--specific HSN2 exon of WNK1 cause
            hereditary sensory neuropathy type II
  JOURNAL   J Clin Invest 118 (7), 2496-2505 (2008)
   PUBMED   18521183
  REMARK    GeneRIF: HSN2 is a nervous system-specific exon of the WNK1 gene
            (WNK1/HSN2 isoform).
REFERENCE   6  (residues 1 to 2634)
  AUTHORS   Disse-Nicodeme,S., Achard,J.M., Desitter,I., Houot,A.M.,
            Fournier,A., Corvol,P. and Jeunemaitre,X.
  TITLE     A new locus on chromosome 12p13.3 for pseudohypoaldosteronism type
            II, an autosomal dominant form of hypertension
  JOURNAL   Am J Hum Genet 67 (2), 302-310 (2000)
   PUBMED   10869238
REFERENCE   7  (residues 1 to 2634)
  AUTHORS   Moore,T.M., Garg,R., Johnson,C., Coptcoat,M.J., Ridley,A.J. and
            Morris,J.D.
  TITLE     PSK, a novel STE20-like kinase derived from prostatic carcinoma
            that activates the c-Jun N-terminal kinase mitogen-activated
            protein kinase pathway and regulates actin cytoskeletal
            organization
  JOURNAL   J Biol Chem 275 (6), 4311-4322 (2000)
   PUBMED   10660600
REFERENCE   8  (residues 1 to 2634)
  AUTHORS   Ellison,D.H.
  TITLE     Pseudohypoaldosteronism Type II
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22073419
REFERENCE   9  (residues 1 to 2634)
  AUTHORS   Kurth,I.
  TITLE     Hereditary Sensory and Autonomic Neuropathy Type II
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21089229
REFERENCE   10 (residues 1 to 2634)
  AUTHORS   Ota,M., Ellefson,R.D., Lambert,E.H. and Dyck,P.J.
  TITLE     Hereditary sensory neuropathy, type II. Clinical,
            electrophysiologic, histologic, and biochemical studies of a Quebec
            kinship
  JOURNAL   Arch Neurol 29 (1), 23-37 (1973)
   PUBMED   4351257
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004765.2 and AC004803.11.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 17, 2010 this sequence version replaced NP_998820.2.
            
            Summary: This gene encodes a member of the WNK subfamily of
            serine/threonine protein kinases. The encoded protein may be a key
            regulator of blood pressure by controlling the transport of sodium
            and chloride ions. Mutations in this gene have been associated with
            pseudohypoaldosteronism type II and hereditary sensory neuropathy
            type II. Alternatively spliced transcript variants encoding
            different isoforms have been described but the full-length nature
            of all of them has yet to be determined.[provided by RefSeq, May
            2010].
            
            Transcript Variant: This variant (3) has multiple differences in
            the coding region but maintains the reading frame compared to
            variant 1. This variant represents the exon combination of the
            brain and spinal cord variant described in Figure 2F of PubMed ID
            18521183. This variant encodes isoform 3, which is longer than
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments. The
            combination of alternatively spliced exons within the coding region
            is inferred based on experimental evidence reported in Figures 2F
            and 3 from PubMed ID 18521183.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2156670
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match :: ENST00000340908.9/ ENSP00000341292.5
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2634
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..2634
                     /product="serine/threonine-protein kinase WNK1 isoform 3"
                     /EC_number="2.7.11.1"
                     /note="prostate-derived sterile 20-like kinase;
                     erythrocyte 65 kDa protein; protein kinase with no lysine
                     1; protein phosphatase 1, regulatory subunit 167;
                     serine/threonine-protein kinase WNK1 1;
                     serine/threonine-protein kinase WNK1 2"
                     /calculated_mol_wt=279408
     Region          1..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17190791; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH7; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          95..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17190791,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          195..483
                     /region_name="STKc_WNK1"
                     /note="Catalytic domain of the Serine/Threonine protein
                     kinase, With No Lysine (WNK) 1; cd14030"
                     /db_xref="CDD:270932"
     Site            order(227..231,233,235,248,250,281,301..304,308,310,349,
                     351,353..354,356,368,371,385..388)
                     /site_type="active"
                     /db_xref="CDD:270932"
     Site            order(227..231,233,235,248,250,281,301..304,308,349,351,
                     353..354,356,368)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270932"
     Site            order(231,308,310,349,351,353,371,385..388)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270932"
     Site            367..388
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270932"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:31656913; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15883153,
                     ECO:0000269|PubMed:16263722, ECO:0000269|PubMed:16832045,
                     ECO:0000269|PubMed:17190791, ECO:0000269|PubMed:31656913,
                     ECO:0000269|PubMed:34289367; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          488..555
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          500..563
                     /region_name="OSR1_C"
                     /note="Oxidative-stress-responsive kinase 1 C-terminal
                     domain; pfam12202"
                     /db_xref="CDD:463491"
     Region          628..638
                     /region_name="Interaction with KLHL3.
                     /evidence=ECO:0000250|UniProtKB:Q96J92"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          <1825..2119
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..2634
                     /gene="WNK1"
                     /gene_synonym="HSAN2; HSN2; KDP; p65; PPP1R167; PRKWNK1;
                     PSK"
                     /coded_by="NM_213655.5:988..8892"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS73419.1"
                     /db_xref="GeneID:65125"
                     /db_xref="HGNC:HGNC:14540"
                     /db_xref="MIM:605232"
ORIGIN      
        1 msggaaekqs stpgslflsp papapkngss sdssvgeklg aaaadavtgr teeyrrrrht
       61 mdkdsrgaaa tttttehrff rrsvicdsna talelpglpl slpqpsipaa vpqsappeph
      121 reetvtatat sqvaqqppaa aapgeqavag papstvpsst skdrpvsqps lvgskeeppp
      181 arsgsgggsa kepqeersqq qddieeletk avgmsndgrf lkfdieigrg sfktvykgld
      241 tettvevawc elqdrkltks erqrfkeeae mlkglqhpni vrfydswest vkgkkcivlv
      301 telmtsgtlk tylkrfkvmk ikvlrswcrq ilkglqflht rtppiihrdl kcdnifitgp
      361 tgsvkigdlg latlkrasfa ksvigtpefm apemyeekyd esvdvyafgm cmlematsey
      421 pysecqnaaq iyrrvtsgvk pasfdkvaip evkeiiegci rqnkderysi kdllnhaffq
      481 eetgvrvela eeddgekiai klwlriedik klkgkykdne aiefsfdler dvpedvaqem
      541 vesgyvcegd hktmakaikd rvslikrkre qrqlvreeqe kkkqeesslk qqveqssasq
      601 tgikqlpsas tgiptastts asvstqvepe epeadqhqql qyqqpsisvl sdgtvdsgqg
      661 ssvftesrvs sqqtvsygsq heqahstgtv pghipstvqa qsqphgvypp ssvprrgrsm
      721 svcvpiflll plcpaslpvl fhptastvct sfsfpppdcp eetfaeklsk alesvlpmhs
      781 asqrkhrrss lpslfvstpq smahpcggtp typesqiffp tiherpvsfs ppptcppkva
      841 isqrrkstsf leaqthhfqp llrtvgqsll ppggsptnwt peavvmlgtt asrvtgesce
      901 iqvhpmfeps qvysdyrpgl vlpeeahyfi pqeavyvagv hyqarvaeqy egipynssvl
      961 sspmkqipeq kpvqggptss svfefpsgqa flvghlqnlr ldsglgpgsp lssisapist
     1021 datrlkfhpv fvphsapavl thnnesrsnc vfefhvhtps sssgegggil pqrvyrnrqv
     1081 avdlnqeelp pqsvglhgyl qpvteekhny hapeltvsvv epigqnwpig speyssdssq
     1141 itssdpsdfq sppptggaaa pfgsdvsmpf ihlpqtvlqe splffcfpqg ttsqqvltas
     1201 fssggsalhp qaqgqsqgqp ssssltgvss sqpiqhpqqq qgiqqtappq qtvqyslsqt
     1261 stsseattaq pvsqpqapqv lpqvsagkqs tqgvsqvapa epvavaqtqa tqpttlassv
     1321 dsahsdvasg msdgnenvps ssgrhegrtt krhyrksvrs rsrhektsrp klrilnvsnk
     1381 gdrvvecqle thnrkmvtfk fdldgdnpee iatimvnndf ilaieresfv dqvreiieka
     1441 demlsedvsv epegdqgles lqgkddygfs gsqklegefk qpipassmpq qigiptsslt
     1501 qvvhsagrrf ivspvpesrl reskvfpsei tdtvaastaq spgmnlshsa sslslqqafs
     1561 elrraqmteg pntappnfsh tgptfpvvpp flssiagvpt taaatapvpa tssppndist
     1621 sviqsevtvp teegiagvat stgvvtsggl pippvsespv lssvvssiti pavvsistts
     1681 pslqvptsts eivvsstaly psvtvsatsa saggstatpg pkppavvsqq aagsttvgat
     1741 ltsvstttsf pstasqlciq lssststptl aetvvvsahs ldktshsstt glafslsaps
     1801 sssspgagvs syisqpgglh plvipsvias tpilpqaagp tstpllpqvp sipplvqpva
     1861 nvpavqqtli hsqpqpallp nqphthcpev dsdtqpkapg iddiktleek lrslfsehss
     1921 sgaqhasvsl etslviestv tpgipttava psklltstts tclpptnlpl gtvalpvtpv
     1981 vtpgqvstpv stttsgvkpg tapskppltk apvlpvgtel pagtlpseql ppfpgpsltq
     2041 sqqpledlda qlrrtlspem itvtsavgpv smaaptaite agtqpqkgvs qvkegpvlat
     2101 ssgagvfkmg rfqvsvaadg aqkegknkse daksvhfess tsessvlsss spestlvkpe
     2161 pngitipgis sdvpesahkt taseaksdtg qptkvgrfqv tttankvgrf svsktedkit
     2221 dtkkegpvas ppfmdleqav lpavipkkek pelsepshln gpssdpeaaf lsrdvddgsg
     2281 sphsphqlss kslpsqnlsq slsnsfnssy mssdnesdie dedlklelrr lrdkhlkeiq
     2341 dlqsrqkhei eslytklgkv ppaviippaa plsgrrrrpt kskgskssrs sslgnkspql
     2401 sgnlsgqsaa svlhpqqtlh ppgnipesgq nqllqplkps pssdnlysaf tsdgaisvps
     2461 lsapgqgtss tntvgatvns qaaqaqppam tssrkgtftd dlhklvdnwa rdamnlsgrr
     2521 gskghmnyeg pgmarkfsap gqlcismtsn lggsapisaa satslghftk smcppqqygf
     2581 patpfgaqws gtggpapqpl gqfqpvgtas lqnfnisnlq ksisnppgsn lrtt
//
LOCUS       NP_055638               2134 aa            linear   PRI 24-DEC-2025
DEFINITION  serine/threonine-protein kinase WNK1 isoform 2 [Homo sapiens].
ACCESSION   NP_055638
VERSION     NP_055638.2
DBSOURCE    REFSEQ: accession NM_014823.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2134)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2134)
  AUTHORS   Li,L., Xie,D., Yu,S., Ma,M., Fan,K., Chen,J., Xiu,M., Xie,K., Li,Y.
            and Gao,Y.
  TITLE     WNK1 Interaction with KEAP1 Promotes NRF2 Stabilization to Enhance
            the Oxidative Stress Response in Hepatocellular Carcinoma
  JOURNAL   Cancer Res 84 (17), 2776-2791 (2024)
   PUBMED   38885324
  REMARK    GeneRIF: WNK1 Interaction with KEAP1 Promotes NRF2 Stabilization to
            Enhance the Oxidative Stress Response in Hepatocellular Carcinoma.
REFERENCE   3  (residues 1 to 2134)
  AUTHORS   Ma,Y., Zong,H., Pan,P., Shang,H. and Yang,X.
  TITLE     The CREB1/WNK1 axis promotes the tumorigenesis of ovarian cancer
            via regulating HIF-1
  JOURNAL   Exp Cell Res 438 (1), 114006 (2024)
   PUBMED   38599542
  REMARK    GeneRIF: The CREB1/WNK1 axis promotes the tumorigenesis of ovarian
            cancer via regulating HIF-1.
REFERENCE   4  (residues 1 to 2134)
  AUTHORS   Newhouse,S., Farrall,M., Wallace,C., Hoti,M., Burke,B., Howard,P.,
            Onipinla,A., Lee,K., Shaw-Hawkins,S., Dobson,R., Brown,M.,
            Samani,N.J., Dominiczak,A.F., Connell,J.M., Lathrop,G.M.,
            Kooner,J., Chambers,J., Elliott,P., Clarke,R., Collins,R., Laan,M.,
            Org,E., Juhanson,P., Veldre,G., Viigimaa,M., Eyheramendy,S.,
            Cappuccio,F.P., Ji,C., Iacone,R., Strazzullo,P., Kumari,M.,
            Marmot,M., Brunner,E., Caulfield,M. and Munroe,P.B.
  TITLE     Polymorphisms in the WNK1 gene are associated with blood pressure
            variation and urinary potassium excretion
  JOURNAL   PLoS One 4 (4), e5003 (2009)
   PUBMED   19347040
  REMARK    GeneRIF: data indicates that multiple rare and common WNK1 variants
            contribute to BP variation and hypertension, and provide compelling
            evidence to initiate further genetic and functional studies to
            explore the role of WNK1 in BP regulation and EH
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 2134)
  AUTHORS   Shekarabi,M., Girard,N., Riviere,J.B., Dion,P., Houle,M.,
            Toulouse,A., Lafreniere,R.G., Vercauteren,F., Hince,P.,
            Laganiere,J., Rochefort,D., Faivre,L., Samuels,M. and Rouleau,G.A.
  TITLE     Mutations in the nervous system--specific HSN2 exon of WNK1 cause
            hereditary sensory neuropathy type II
  JOURNAL   J Clin Invest 118 (7), 2496-2505 (2008)
   PUBMED   18521183
  REMARK    GeneRIF: HSN2 is a nervous system-specific exon of the WNK1 gene
            (WNK1/HSN2 isoform).
REFERENCE   6  (residues 1 to 2134)
  AUTHORS   Disse-Nicodeme,S., Achard,J.M., Desitter,I., Houot,A.M.,
            Fournier,A., Corvol,P. and Jeunemaitre,X.
  TITLE     A new locus on chromosome 12p13.3 for pseudohypoaldosteronism type
            II, an autosomal dominant form of hypertension
  JOURNAL   Am J Hum Genet 67 (2), 302-310 (2000)
   PUBMED   10869238
REFERENCE   7  (residues 1 to 2134)
  AUTHORS   Moore,T.M., Garg,R., Johnson,C., Coptcoat,M.J., Ridley,A.J. and
            Morris,J.D.
  TITLE     PSK, a novel STE20-like kinase derived from prostatic carcinoma
            that activates the c-Jun N-terminal kinase mitogen-activated
            protein kinase pathway and regulates actin cytoskeletal
            organization
  JOURNAL   J Biol Chem 275 (6), 4311-4322 (2000)
   PUBMED   10660600
REFERENCE   8  (residues 1 to 2134)
  AUTHORS   Ellison,D.H.
  TITLE     Pseudohypoaldosteronism Type II
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22073419
REFERENCE   9  (residues 1 to 2134)
  AUTHORS   Kurth,I.
  TITLE     Hereditary Sensory and Autonomic Neuropathy Type II
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21089229
REFERENCE   10 (residues 1 to 2134)
  AUTHORS   Ota,M., Ellefson,R.D., Lambert,E.H. and Dyck,P.J.
  TITLE     Hereditary sensory neuropathy, type II. Clinical,
            electrophysiologic, histologic, and biochemical studies of a Quebec
            kinship
  JOURNAL   Arch Neurol 29 (1), 23-37 (1973)
   PUBMED   4351257
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004765.2, AJ296290.1,
            CD629562.1, AB002342.2, AC004803.11, BX644268.1, DA720959.1,
            BC141881.1 and AI074334.1.
            
            On May 27, 2010 this sequence version replaced NP_055638.1.
            
            Summary: This gene encodes a member of the WNK subfamily of
            serine/threonine protein kinases. The encoded protein may be a key
            regulator of blood pressure by controlling the transport of sodium
            and chloride ions. Mutations in this gene have been associated with
            pseudohypoaldosteronism type II and hereditary sensory neuropathy
            type II. Alternatively spliced transcript variants encoding
            different isoforms have been described but the full-length nature
            of all of them has yet to be determined.[provided by RefSeq, May
            2010].
            
            Transcript Variant: This variant (2) uses two alternative splice
            sites and lacks two exons in the coding region compared to variant
            1. The resulting protein (isoform 2) is shorter but has the same N-
            and C-termini compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB002342.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2134
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..2134
                     /product="serine/threonine-protein kinase WNK1 isoform 2"
                     /EC_number="2.7.11.1"
                     /note="prostate-derived sterile 20-like kinase;
                     erythrocyte 65 kDa protein; protein kinase with no lysine
                     1; protein phosphatase 1, regulatory subunit 167;
                     serine/threonine-protein kinase WNK1 1;
                     serine/threonine-protein kinase WNK1 2"
                     /calculated_mol_wt=225373
     Region          1..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17190791; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH7; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          95..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17190791,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          195..483
                     /region_name="STKc_WNK1"
                     /note="Catalytic domain of the Serine/Threonine protein
                     kinase, With No Lysine (WNK) 1; cd14030"
                     /db_xref="CDD:270932"
     Site            order(227..231,233,235,248,250,281,301..304,308,310,349,
                     351,353..354,356,368,371,385..388)
                     /site_type="active"
                     /db_xref="CDD:270932"
     Site            order(227..231,233,235,248,250,281,301..304,308,349,351,
                     353..354,356,368)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270932"
     Site            order(231,308,310,349,351,353,371,385..388)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270932"
     Site            367..388
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270932"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:31656913; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15883153,
                     ECO:0000269|PubMed:16263722, ECO:0000269|PubMed:16832045,
                     ECO:0000269|PubMed:17190791, ECO:0000269|PubMed:31656913,
                     ECO:0000269|PubMed:34289367; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          488..555
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          500..563
                     /region_name="OSR1_C"
                     /note="Oxidative-stress-responsive kinase 1 C-terminal
                     domain; pfam12202"
                     /db_xref="CDD:463491"
     Region          628..638
                     /region_name="Interaction with KLHL3.
                     /evidence=ECO:0000250|UniProtKB:Q96J92"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          <1326..1619
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..2134
                     /gene="WNK1"
                     /gene_synonym="HSAN2; HSN2; KDP; p65; PPP1R167; PRKWNK1;
                     PSK"
                     /coded_by="NM_014823.3:988..7392"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS53731.1"
                     /db_xref="GeneID:65125"
                     /db_xref="HGNC:HGNC:14540"
                     /db_xref="MIM:605232"
ORIGIN      
        1 msggaaekqs stpgslflsp papapkngss sdssvgeklg aaaadavtgr teeyrrrrht
       61 mdkdsrgaaa tttttehrff rrsvicdsna talelpglpl slpqpsipaa vpqsappeph
      121 reetvtatat sqvaqqppaa aapgeqavag papstvpsst skdrpvsqps lvgskeeppp
      181 arsgsgggsa kepqeersqq qddieeletk avgmsndgrf lkfdieigrg sfktvykgld
      241 tettvevawc elqdrkltks erqrfkeeae mlkglqhpni vrfydswest vkgkkcivlv
      301 telmtsgtlk tylkrfkvmk ikvlrswcrq ilkglqflht rtppiihrdl kcdnifitgp
      361 tgsvkigdlg latlkrasfa ksvigtpefm apemyeekyd esvdvyafgm cmlematsey
      421 pysecqnaaq iyrrvtsgvk pasfdkvaip evkeiiegci rqnkderysi kdllnhaffq
      481 eetgvrvela eeddgekiai klwlriedik klkgkykdne aiefsfdler dvpedvaqem
      541 vesgyvcegd hktmakaikd rvslikrkre qrqlvreeqe kkkqeesslk qqveqssasq
      601 tgikqlpsas tgiptastts asvstqvepe epeadqhqql qyqqpsisvl sdgtvdsgqg
      661 ssvftesrvs sqqtvsygsq heqahstgtv pghipstvqa qsqphgvypp ssvaqgqsqg
      721 qpssssltgv sssqpiqhpq qqgiqqtapp qqtvqyslsq tstsseatta qpvsqpqapq
      781 vlpqvsagkq stqgvsqvap aepvavaqtq atqpttlass vdsahsdvas gmsdgnenvp
      841 sssgrhegrt tkrhyrksvr srsrhektsr pklrilnvsn kgdrvvecql ethnrkmvtf
      901 kfdldgdnpe eiatimvnnd filaieresf vdqvreiiek ademlsedvs vepegdqgle
      961 slqgkddygf sgsqklegef kqpipassmp qqigiptssl tqvvhsagrr fivspvpesr
     1021 lreskvfpse itdtvaasta qspgmnlshs asslslqqaf selrraqmte gpntappnfs
     1081 htgptfpvvp pflssiagvp ttaaatapvp atssppndis tsviqsevtv pteegiagva
     1141 tstgvvtsgg lpippvsesp vlssvvssit ipavvsistt spslqvptst seivvsstal
     1201 ypsvtvsats asaggstatp gpkppavvsq qaagsttvga tltsvsttts fpstasqlci
     1261 qlssststpt laetvvvsah sldktshsst tglafslsap ssssspgagv ssyisqpggl
     1321 hplvipsvia stpilpqaag ptstpllpqv psipplvqpv anvpavqqtl ihsqpqpall
     1381 pnqphthcpe vdsdtqpkap giddiktlee klrslfsehs ssgaqhasvs letslviest
     1441 vtpgipttav apsklltstt stclpptnlp lgtvalpvtp vvtpgqvstp vstttsgvkp
     1501 gtapskpplt kapvlpvgte lpagtlpseq lppfpgpslt qsqqpledld aqlrrtlspe
     1561 mitvtsavgp vsmaaptait eagtqpqkvs qvkegpvlat ssgagvfkmg rfqvsvaadg
     1621 aqkegknkse daksvhfess tsessvlsss spestlvkpe pngitipgis sdvpesahkt
     1681 taseaksdtg qptkvgrfqv tttankvgrf svsktedkit dtkkegpvas ppfmdleqav
     1741 lpavipkkek pelsepshln gpssdpeaaf lsrdvddgsg sphsphqlss kslpsqnlsq
     1801 slsnsfnssy mssdnesdie dedlklelrr lrdkhlkeiq dlqsrqkhei eslytklgkv
     1861 ppaviippaa plsgrrrrpt kskgskssrs sslgnkspql sgnlsgqsaa svlhpqqtlh
     1921 ppgnipesgq nqllqplkps pssdnlysaf tsdgaisvps lsapgqgtss tntvgatvns
     1981 qaaqaqppam tssrkgtftd dlhklvdnwa rdamnlsgrr gskghmnyeg pgmarkfsap
     2041 gqlcismtsn lggsapisaa satslghftk smcppqqygf patpfgaqws gtggpapqpl
     2101 gqfqpvgtas lqnfnisnlq ksisnppgsn lrtt
//
LOCUS       NP_937983               1132 aa            linear   PRI 24-DEC-2025
DEFINITION  telomerase reverse transcriptase isoform 1 [Homo sapiens].
ACCESSION   NP_937983 NP_003210
VERSION     NP_937983.2
DBSOURCE    REFSEQ: accession NM_198253.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1132)
  AUTHORS   Karna,D., Liang,L., Sharma,G., Mandal,S., Asamitsu,S., Kawamoto,Y.,
            Hashiya,K., Bando,T., Sugiyama,H. and Mao,H.
  TITLE     Modulation of dynamic DNA G-quadruplex structures in the hTERT
            promoter region by ligands
  JOURNAL   Nucleic Acids Res 52 (18), 10775-10787 (2024)
   PUBMED   39217470
  REMARK    GeneRIF: Modulation of dynamic DNA G-quadruplex structures in the
            hTERT promoter region by ligands.
REFERENCE   2  (residues 1 to 1132)
  AUTHORS   Sergeeva,S.V., Loshchenova,P.S., Oshchepkov,D.Y. and
            Orishchenko,K.E.
  TITLE     Crosstalk between BER and NHEJ in XRCC4-Deficient Cells Depending
            on hTERT Overexpression
  JOURNAL   Int J Mol Sci 25 (19), 10405 (2024)
   PUBMED   39408734
  REMARK    GeneRIF: Crosstalk between BER and NHEJ in XRCC4-Deficient Cells
            Depending on hTERT Overexpression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1132)
  AUTHORS   Song,Y., Xu,J., Geng,W., Yin,L., Wang,J. and Zhao,J.
  TITLE     Association and causal impact of TERT genetic variants on
            peripheral blood leukocyte telomere length and cerebral small
            vessel disease risk in a Chinese Han population: a mendelian
            randomization analysis
  JOURNAL   Orphanet J Rare Dis 19 (1), 309 (2024)
   PUBMED   39180127
  REMARK    GeneRIF: Association and causal impact of TERT genetic variants on
            peripheral blood leukocyte telomere length and cerebral small
            vessel disease risk in a Chinese Han population: a mendelian
            randomization analysis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1132)
  AUTHORS   Marczyk,V.R., Maia,A.L. and Goemann,I.M.
  TITLE     Distinct transcriptional and prognostic impacts of TERT promoter
            mutations C228T and C250T in papillary thyroid carcinoma
  JOURNAL   Endocr Relat Cancer 31 (9), e240058 (2024)
   PUBMED   38973620
  REMARK    GeneRIF: Distinct transcriptional and prognostic impacts of TERT
            promoter mutations C228T and C250T in papillary thyroid carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1132)
  AUTHORS   Meyerson,M., Counter,C.M., Eaton,E.N., Ellisen,L.W., Steiner,P.,
            Caddle,S.D., Ziaugra,L., Beijersbergen,R.L., Davidoff,M.J., Liu,Q.,
            Bacchetti,S., Haber,D.A. and Weinberg,R.A.
  TITLE     hEST2, the putative human telomerase catalytic subunit gene, is
            up-regulated in tumor cells and during immortalization
  JOURNAL   Cell 90 (4), 785-795 (1997)
   PUBMED   9288757
REFERENCE   6  (residues 1 to 1132)
  AUTHORS   Nakamura,T.M., Morin,G.B., Chapman,K.B., Weinrich,S.L.,
            Andrews,W.H., Lingner,J., Harley,C.B. and Cech,T.R.
  TITLE     Telomerase catalytic subunit homologs from fission yeast and human
  JOURNAL   Science 277 (5328), 955-959 (1997)
   PUBMED   9252327
REFERENCE   7  (residues 1 to 1132)
  AUTHORS   Lingner,J., Hughes,T.R., Shevchenko,A., Mann,M., Lundblad,V. and
            Cech,T.R.
  TITLE     Reverse transcriptase motifs in the catalytic subunit of telomerase
  JOURNAL   Science 276 (5312), 561-567 (1997)
   PUBMED   9110970
REFERENCE   8  (residues 1 to 1132)
  AUTHORS   Savage,S.A. and Niewisch,M.R.
  TITLE     Dyskeratosis Congenita and Related Telomere Biology Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301779
REFERENCE   9  (residues 1 to 1132)
  AUTHORS   Garcia,C.K. and Talbert,J.L.
  TITLE     Pulmonary Fibrosis Predisposition Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301408
REFERENCE   10 (residues 1 to 1132)
  AUTHORS   Morin,G.B.
  TITLE     The human telomere terminal transferase enzyme is a
            ribonucleoprotein that synthesizes TTAGGG repeats
  JOURNAL   Cell 59 (3), 521-529 (1989)
   PUBMED   2805070
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC114291.2, AF018167.1 and
            AF015950.1.
            
            On or before Jun 23, 2006 this sequence version replaced
            NP_003210.1, NP_937983.1.
            
            Summary: Telomerase is a ribonucleoprotein polymerase that
            maintains telomere ends by addition of the telomere repeat TTAGGG.
            The enzyme consists of a protein component with reverse
            transcriptase activity, encoded by this gene, and an RNA component
            which serves as a template for the telomere repeat. Telomerase
            expression plays a role in cellular senescence, as it is normally
            repressed in postnatal somatic cells resulting in progressive
            shortening of telomeres. Deregulation of telomerase expression in
            somatic cells may be involved in oncogenesis. Studies in mouse
            suggest that telomerase also participates in chromosomal repair,
            since de novo synthesis of telomere repeats may occur at
            double-stranded breaks. Alternatively spliced variants encoding
            different isoforms of telomerase reverse transcriptase have been
            identified; the full-length sequence of some variants has not been
            determined. Alternative splicing at this locus is thought to be one
            mechanism of regulation of telomerase activity. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF015950.1, AF018167.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310581.10/ ENSP00000309572.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1132
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.33"
     Protein         1..1132
                     /product="telomerase reverse transcriptase isoform 1"
                     /EC_number="2.7.7.49"
                     /note="telomerase catalytic subunit; telomerase-associated
                     protein 2"
                     /calculated_mol_wt=126866
     Region          1..230
                     /region_name="RNA-interacting domain 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14746.1)"
     Region          <22..482
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          58..197
                     /region_name="GQ motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O14746.1)"
     Region          137..141
                     /region_name="Required for regulating specificity for
                     telomeric DNA and for processivity for primer elongation"
                     /note="propagated from UniProtKB/Swiss-Prot (O14746.1)"
     Site            169
                     /site_type="other"
                     /note="Required for optimal binding of telomeric ssDNA and
                     incorporation of nucleotides at the second position of the
                     template; propagated from UniProtKB/Swiss-Prot (O14746.1)"
     Region          210..320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14746.1)"
     Region          222..240
                     /region_name="Bipartite nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (O14746.1)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:22366458; propagated from
                     UniProtKB/Swiss-Prot (O14746.1)"
     Region          231..324
                     /region_name="Linker"
                     /note="propagated from UniProtKB/Swiss-Prot (O14746.1)"
     Region          301..538
                     /region_name="Required for oligomerization"
                     /note="propagated from UniProtKB/Swiss-Prot (O14746.1)"
     Region          325..550
                     /region_name="RNA-interacting domain 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14746.1)"
     Region          328..333
                     /region_name="TFLY, involved in RNA binding.
                     /evidence=ECO:0000250|UniProtKB:Q4KTA7"
                     /note="propagated from UniProtKB/Swiss-Prot (O14746.1)"
     Region          376..521
                     /region_name="QFP motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O14746.1)"
     Region          397..417
                     /region_name="CP motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O14746.1)"
     Site            457
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by DYRK2.
                     /evidence=ECO:0000269|PubMed:23362280; propagated from
                     UniProtKB/Swiss-Prot (O14746.1)"
     Region          460..592
                     /region_name="Telomerase_RBD"
                     /note="Telomerase ribonucleoprotein complex - RNA binding
                     domain; pfam12009"
                     /db_xref="CDD:463428"
     Region          618..>729
                     /region_name="ps-ssRNAv_RdRp-like"
                     /note="conserved catalytic core domain of RNA-dependent
                     RNA polymerase (RdRp) from the positive-sense
                     single-stranded RNA [(+)ssRNA] viruses and closely related
                     viruses; cl40470"
                     /db_xref="CDD:477363"
     Site            707
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC-type Tyr-kinases.
                     /evidence=ECO:0000269|PubMed:12808100,
                     ECO:0000269|PubMed:18829466; propagated from
                     UniProtKB/Swiss-Prot (O14746.1)"
     Region          825..936
                     /region_name="TERT"
                     /note="Telomerase reverse transcriptase (TERT). Telomerase
                     is a ribonucleoprotein (RNP) that synthesizes telomeric
                     DNA repeats. The telomerase RNA subunit provides the
                     template for synthesis of these repeats. The catalytic
                     subunit of RNP is known as telomerase...; cd01648"
                     /db_xref="CDD:238826"
     Site            834
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238826"
     Site            867
                     /site_type="other"
                     /note="Required for nucleotide incorporation and primer
                     extension rate; propagated from UniProtKB/Swiss-Prot
                     (O14746.1)"
     Region          914..928
                     /region_name="Required for oligomerization"
                     /note="propagated from UniProtKB/Swiss-Prot (O14746.1)"
     Region          930..934
                     /region_name="Primer grip sequence"
                     /note="propagated from UniProtKB/Swiss-Prot (O14746.1)"
     Region          936..1132
                     /region_name="CTE"
                     /note="propagated from UniProtKB/Swiss-Prot (O14746.1)"
     CDS             1..1132
                     /gene="TERT"
                     /gene_synonym="CMM9; DKCA2; DKCB4; EST2; hEST2; hTRT;
                     PFBMFT1; TCS1; TP2; TRT"
                     /coded_by="NM_198253.3:80..3478"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3861.2"
                     /db_xref="GeneID:7015"
                     /db_xref="HGNC:HGNC:11730"
                     /db_xref="MIM:187270"
ORIGIN      
        1 mpraprcrav rsllrshyre vlplatfvrr lgpqgwrlvq rgdpaafral vaqclvcvpw
       61 darpppaaps frqvsclkel varvlqrlce rgaknvlafg falldgargg ppeafttsvr
      121 sylpntvtda lrgsgawgll lrrvgddvlv hllarcalfv lvapscayqv cgpplyqlga
      181 atqarpppha sgprrrlgce rawnhsvrea gvplglpapg arrrggsasr slplpkrprr
      241 gaapepertp vgqgswahpg rtrgpsdrgf cvvsparpae eatslegals gtrhshpsvg
      301 rqhhagppst srpprpwdtp cppvyaetkh flyssgdkeq lrpsfllssl rpsltgarrl
      361 vetiflgsrp wmpgtprrlp rlpqrywqmr plflellgnh aqcpygvllk thcplraavt
      421 paagvcarek pqgsvaapee edtdprrlvq llrqhsspwq vygfvraclr rlvppglwgs
      481 rhnerrflrn tkkfislgkh aklslqeltw kmsvrdcawl rrspgvgcvp aaehrlreei
      541 lakflhwlms vyvvellrsf fyvtettfqk nrlffyrksv wsklqsigir qhlkrvqlre
      601 lseaevrqhr earpalltsr lrfipkpdgl rpivnmdyvv gartfrrekr aerltsrvka
      661 lfsvlnyera rrpgllgasv lglddihraw rtfvlrvraq dpppelyfvk vdvtgaydti
      721 pqdrltevia siikpqntyc vrryavvqka ahghvrkafk shvstltdlq pymrqfvahl
      781 qetsplrdav vieqssslne assglfdvfl rfmchhavri rgksyvqcqg ipqgsilstl
      841 lcslcygdme nklfagirrd glllrlvddf llvtphltha ktflrtlvrg vpeygcvvnl
      901 rktvvnfpve dealggtafv qmpahglfpw cgllldtrtl evqsdyssya rtsirasltf
      961 nrgfkagrnm rrklfgvlrl kchslfldlq vnslqtvctn iykilllqay rfhacvlqlp
     1021 fhqqvwknpt fflrvisdta slcysilkak nagmslgakg aagplpseav qwlchqafll
     1081 kltrhrvtyv pllgslrtaq tqlsrklpgt tltaleaaan palpsdfkti ld
//
LOCUS       NP_067648                135 aa            linear   PRI 24-DEC-2025
DEFINITION  prostate and breast cancer overexpressed gene 1 protein [Homo
            sapiens].
ACCESSION   NP_067648
VERSION     NP_067648.1
DBSOURCE    REFSEQ: accession NM_021635.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Dong,H., Huang,C. and Huang,J.
  TITLE     FBXL19-AS1 promotes the progression of nasopharyngeal carcinoma by
            acting as a competing endogenous RNA to sponge miR-431 and
            upregulate PBOV1
  JOURNAL   Mol Med Rep 24 (3) (2021)
   PUBMED   34278444
  REMARK    GeneRIF: FBXL19AS1 promotes the progression of nasopharyngeal
            carcinoma by acting as a competing endogenous RNA to sponge miR431
            and upregulate PBOV1.
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Kong,Q., Han,J., Deng,H., Wu,F., Guo,S. and Ye,Z.
  TITLE     miR-431-5p alters the epithelial-to-mesenchymal transition markers
            by targeting UROC28 in hepatoma cells
  JOURNAL   Onco Targets Ther 11, 6489-6503 (2018)
   PUBMED   30323624
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Yang,C.A., Li,J.P., Yen,J.C., Lai,I.L., Ho,Y.C., Chen,Y.C.,
            Lan,J.L. and Chang,J.G.
  TITLE     lncRNA NTT/PBOV1 Axis Promotes Monocyte Differentiation and Is
            Elevated in Rheumatoid Arthritis
  JOURNAL   Int J Mol Sci 19 (9), 2806 (2018)
   PUBMED   30231487
  REMARK    GeneRIF: Overexpression of PBOV1 in THP-1 cells resulted in cell
            cycle G1 arrest, differentiation into macrophages, a marked
            increase in IL-10 and CXCL10 mRNA levels, and upregulation of the
            costimulatory molecules.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 135)
  AUTHORS   Wang,L., Niu,C.H., Wu,S., Wu,H.M., Ouyang,F., He,M. and He,S.Y.
  TITLE     PBOV1 correlates with progression of ovarian cancer and inhibits
            proliferation of ovarian cancer cells
  JOURNAL   Oncol Rep 35 (1), 488-496 (2016)
   PUBMED   26549570
  REMARK    GeneRIF: Study shows that patients with high PBOV1 expression had
            longer overall survival; patients with low PBOV1 expression had
            shorter survival suggesting that PBOV1 may play an important role
            in suppressing ovarian cancer proliferation and carcinogenesis.
REFERENCE   5  (residues 1 to 135)
  AUTHORS   Samusik,N., Krukovskaya,L., Meln,I., Shilov,E. and Kozlov,A.P.
  TITLE     PBOV1 is a human de novo gene with tumor-specific expression that
            is associated with a positive clinical outcome of cancer
  JOURNAL   PLoS One 8 (2), e56162 (2013)
   PUBMED   23418531
  REMARK    GeneRIF: Data indicate that analysis of public microarray data
            suggests that PBOV1 activation in tumors could be dependent on the
            Hedgehog signaling pathway.
REFERENCE   6  (residues 1 to 135)
  AUTHORS   Loizidou,M.A., Cariolou,M.A., Neuhausen,S.L., Newbold,R.F.,
            Bashiardes,E., Marcou,Y., Michael,T., Daniel,M., Kakouri,E.,
            Papadopoulos,P., Malas,S., Hadjisavvas,A. and Kyriacou,K.
  TITLE     Genetic variation in genes interacting with BRCA1/2 and risk of
            breast cancer in the Cypriot population
  JOURNAL   Breast Cancer Res Treat 121 (1), 147-156 (2010)
   PUBMED   19714462
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   7  (residues 1 to 135)
  AUTHORS   Doak,S.H., Jenkins,S.A., Hurle,R.A., Varma,M., Hawizy,A.,
            Kynaston,H.G. and Parry,J.M.
  TITLE     Bone morphogenic factor gene dosage abnormalities in prostatic
            intraepithelial neoplasia and prostate cancer
  JOURNAL   Cancer Genet Cytogenet 176 (2), 161-165 (2007)
   PUBMED   17656261
  REMARK    GeneRIF: Approximately half of the prostate tumors displayed
            increased copy numbers of the BMP2, BMP5, BMP7, and UC28 gene loci,
            which may account for their abnormal gene expression patterns in
            neoplastic prostate tissue.
REFERENCE   8  (residues 1 to 135)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   9  (residues 1 to 135)
  AUTHORS   Kamagata,C., Tsuji,N., Kondoh,K., Sasaki,M., Kobayashi,D.,
            Yagihashi,A. and Watanabe,N.
  TITLE     Enhanced expression of the UROC28 gene in human breast cancer:
            relationship to ERBB2 gene expression
  JOURNAL   Anticancer Res 22 (6C), 4087-4091 (2002)
   PUBMED   12553037
  REMARK    GeneRIF: UROC28 mRNA expression was greater in breast cancers than
            in noncancerous tissues (p < 0.0001), as was ERBB2 mRNA.
REFERENCE   10 (residues 1 to 135)
  AUTHORS   An,G., Ng,A.Y., Meka,C.S., Luo,G., Bright,S.P., Cazares,L.,
            Wright,G.L. Jr. and Veltri,R.W.
  TITLE     Cloning and characterization of UROC28, a novel gene overexpressed
            in prostate, breast, and bladder cancers
  JOURNAL   Cancer Res 60 (24), 7014-7020 (2000)
   PUBMED   11156405
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031433.4, BC069109.1 and
            AF189269.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This intronless gene encodes a protein of unknown
            function. Its expression is up-regulated in some types of cancer,
            including prostate, breast, and bladder cancer. [provided by
            RefSeq, Aug 2011].
            
            ##Evidence-Data-START##
            Transcript is intronless :: AF189269.1, AF189270.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000527246.3/ ENSP00000432353.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q23.3"
     Protein         1..135
                     /product="prostate and breast cancer overexpressed gene 1
                     protein"
                     /calculated_mol_wt=15591
     CDS             1..135
                     /gene="PBOV1"
                     /gene_synonym="dJ171N11.2; UC28; UROC28"
                     /coded_by="NM_021635.3:97..504"
                     /db_xref="CCDS:CCDS5190.1"
                     /db_xref="GeneID:59351"
                     /db_xref="HGNC:HGNC:21079"
                     /db_xref="MIM:605669"
ORIGIN      
        1 mraflrnqky edmhniihil qirklrhrls nfprlpgila petvllpfcy kvfrkkekvk
       61 rsqkatefid ysieqshhai ltplqthltm kgssmkcssl sseailftlt lqltqtlgle
      121 ccllylskti hpqii
//
LOCUS       NP_001180305            1069 aa            linear   PRI 24-DEC-2025
DEFINITION  telomerase reverse transcriptase isoform 2 [Homo sapiens].
ACCESSION   NP_001180305
VERSION     NP_001180305.1
DBSOURCE    REFSEQ: accession NM_001193376.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1069)
  AUTHORS   Karna,D., Liang,L., Sharma,G., Mandal,S., Asamitsu,S., Kawamoto,Y.,
            Hashiya,K., Bando,T., Sugiyama,H. and Mao,H.
  TITLE     Modulation of dynamic DNA G-quadruplex structures in the hTERT
            promoter region by ligands
  JOURNAL   Nucleic Acids Res 52 (18), 10775-10787 (2024)
   PUBMED   39217470
  REMARK    GeneRIF: Modulation of dynamic DNA G-quadruplex structures in the
            hTERT promoter region by ligands.
REFERENCE   2  (residues 1 to 1069)
  AUTHORS   Sergeeva,S.V., Loshchenova,P.S., Oshchepkov,D.Y. and
            Orishchenko,K.E.
  TITLE     Crosstalk between BER and NHEJ in XRCC4-Deficient Cells Depending
            on hTERT Overexpression
  JOURNAL   Int J Mol Sci 25 (19), 10405 (2024)
   PUBMED   39408734
  REMARK    GeneRIF: Crosstalk between BER and NHEJ in XRCC4-Deficient Cells
            Depending on hTERT Overexpression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1069)
  AUTHORS   Song,Y., Xu,J., Geng,W., Yin,L., Wang,J. and Zhao,J.
  TITLE     Association and causal impact of TERT genetic variants on
            peripheral blood leukocyte telomere length and cerebral small
            vessel disease risk in a Chinese Han population: a mendelian
            randomization analysis
  JOURNAL   Orphanet J Rare Dis 19 (1), 309 (2024)
   PUBMED   39180127
  REMARK    GeneRIF: Association and causal impact of TERT genetic variants on
            peripheral blood leukocyte telomere length and cerebral small
            vessel disease risk in a Chinese Han population: a mendelian
            randomization analysis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1069)
  AUTHORS   Marczyk,V.R., Maia,A.L. and Goemann,I.M.
  TITLE     Distinct transcriptional and prognostic impacts of TERT promoter
            mutations C228T and C250T in papillary thyroid carcinoma
  JOURNAL   Endocr Relat Cancer 31 (9), e240058 (2024)
   PUBMED   38973620
  REMARK    GeneRIF: Distinct transcriptional and prognostic impacts of TERT
            promoter mutations C228T and C250T in papillary thyroid carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1069)
  AUTHORS   Meyerson,M., Counter,C.M., Eaton,E.N., Ellisen,L.W., Steiner,P.,
            Caddle,S.D., Ziaugra,L., Beijersbergen,R.L., Davidoff,M.J., Liu,Q.,
            Bacchetti,S., Haber,D.A. and Weinberg,R.A.
  TITLE     hEST2, the putative human telomerase catalytic subunit gene, is
            up-regulated in tumor cells and during immortalization
  JOURNAL   Cell 90 (4), 785-795 (1997)
   PUBMED   9288757
REFERENCE   6  (residues 1 to 1069)
  AUTHORS   Nakamura,T.M., Morin,G.B., Chapman,K.B., Weinrich,S.L.,
            Andrews,W.H., Lingner,J., Harley,C.B. and Cech,T.R.
  TITLE     Telomerase catalytic subunit homologs from fission yeast and human
  JOURNAL   Science 277 (5328), 955-959 (1997)
   PUBMED   9252327
REFERENCE   7  (residues 1 to 1069)
  AUTHORS   Lingner,J., Hughes,T.R., Shevchenko,A., Mann,M., Lundblad,V. and
            Cech,T.R.
  TITLE     Reverse transcriptase motifs in the catalytic subunit of telomerase
  JOURNAL   Science 276 (5312), 561-567 (1997)
   PUBMED   9110970
REFERENCE   8  (residues 1 to 1069)
  AUTHORS   Savage,S.A. and Niewisch,M.R.
  TITLE     Dyskeratosis Congenita and Related Telomere Biology Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301779
REFERENCE   9  (residues 1 to 1069)
  AUTHORS   Garcia,C.K. and Talbert,J.L.
  TITLE     Pulmonary Fibrosis Predisposition Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301408
REFERENCE   10 (residues 1 to 1069)
  AUTHORS   Morin,G.B.
  TITLE     The human telomere terminal transferase enzyme is a
            ribonucleoprotein that synthesizes TTAGGG repeats
  JOURNAL   Cell 59 (3), 521-529 (1989)
   PUBMED   2805070
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC114291.2, AB085628.1 and
            AF015950.1.
            
            Summary: Telomerase is a ribonucleoprotein polymerase that
            maintains telomere ends by addition of the telomere repeat TTAGGG.
            The enzyme consists of a protein component with reverse
            transcriptase activity, encoded by this gene, and an RNA component
            which serves as a template for the telomere repeat. Telomerase
            expression plays a role in cellular senescence, as it is normally
            repressed in postnatal somatic cells resulting in progressive
            shortening of telomeres. Deregulation of telomerase expression in
            somatic cells may be involved in oncogenesis. Studies in mouse
            suggest that telomerase also participates in chromosomal repair,
            since de novo synthesis of telomere repeats may occur at
            double-stranded breaks. Alternatively spliced variants encoding
            different isoforms of telomerase reverse transcriptase have been
            identified; the full-length sequence of some variants has not been
            determined. Alternative splicing at this locus is thought to be one
            mechanism of regulation of telomerase activity. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the middle portion of the coding region, compared to
            variant 1. This results in a shorter protein (isoform 2), compared
            to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB085628.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1968968 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1069
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.33"
     Protein         1..1069
                     /product="telomerase reverse transcriptase isoform 2"
                     /EC_number="2.7.7.49"
                     /note="telomerase catalytic subunit; telomerase-associated
                     protein 2"
                     /calculated_mol_wt=119917
     Region          <22..482
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          460..592
                     /region_name="Telomerase_RBD"
                     /note="Telomerase ribonucleoprotein complex - RNA binding
                     domain; pfam12009"
                     /db_xref="CDD:463428"
     Region          618..>729
                     /region_name="ps-ssRNAv_RdRp-like"
                     /note="conserved catalytic core domain of RNA-dependent
                     RNA polymerase (RdRp) from the positive-sense
                     single-stranded RNA [(+)ssRNA] viruses and closely related
                     viruses; cl40470"
                     /db_xref="CDD:477363"
     Region          825..>884
                     /region_name="TERT"
                     /note="Telomerase reverse transcriptase (TERT). Telomerase
                     is a ribonucleoprotein (RNP) that synthesizes telomeric
                     DNA repeats. The telomerase RNA subunit provides the
                     template for synthesis of these repeats. The catalytic
                     subunit of RNP is known as telomerase...; cd01648"
                     /db_xref="CDD:238826"
     Site            834
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:238826"
     CDS             1..1069
                     /gene="TERT"
                     /gene_synonym="CMM9; DKCA2; DKCB4; EST2; hEST2; hTRT;
                     PFBMFT1; TCS1; TP2; TRT"
                     /coded_by="NM_001193376.3:80..3289"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54831.1"
                     /db_xref="GeneID:7015"
                     /db_xref="HGNC:HGNC:11730"
                     /db_xref="MIM:187270"
ORIGIN      
        1 mpraprcrav rsllrshyre vlplatfvrr lgpqgwrlvq rgdpaafral vaqclvcvpw
       61 darpppaaps frqvsclkel varvlqrlce rgaknvlafg falldgargg ppeafttsvr
      121 sylpntvtda lrgsgawgll lrrvgddvlv hllarcalfv lvapscayqv cgpplyqlga
      181 atqarpppha sgprrrlgce rawnhsvrea gvplglpapg arrrggsasr slplpkrprr
      241 gaapepertp vgqgswahpg rtrgpsdrgf cvvsparpae eatslegals gtrhshpsvg
      301 rqhhagppst srpprpwdtp cppvyaetkh flyssgdkeq lrpsfllssl rpsltgarrl
      361 vetiflgsrp wmpgtprrlp rlpqrywqmr plflellgnh aqcpygvllk thcplraavt
      421 paagvcarek pqgsvaapee edtdprrlvq llrqhsspwq vygfvraclr rlvppglwgs
      481 rhnerrflrn tkkfislgkh aklslqeltw kmsvrdcawl rrspgvgcvp aaehrlreei
      541 lakflhwlms vyvvellrsf fyvtettfqk nrlffyrksv wsklqsigir qhlkrvqlre
      601 lseaevrqhr earpalltsr lrfipkpdgl rpivnmdyvv gartfrrekr aerltsrvka
      661 lfsvlnyera rrpgllgasv lglddihraw rtfvlrvraq dpppelyfvk vdvtgaydti
      721 pqdrltevia siikpqntyc vrryavvqka ahghvrkafk shvstltdlq pymrqfvahl
      781 qetsplrdav vieqssslne assglfdvfl rfmchhavri rgksyvqcqg ipqgsilstl
      841 lcslcygdme nklfagirrd glllrlvddf llvtphltha ktflsyarts irasltfnrg
      901 fkagrnmrrk lfgvlrlkch slfldlqvns lqtvctniyk illlqayrfh acvlqlpfhq
      961 qvwknptffl rvisdtaslc ysilkaknag mslgakgaag plpseavqwl chqafllklt
     1021 rhrvtyvpll gslrtaqtql srklpgttlt aleaaanpal psdfktild
//
LOCUS       NP_001128243            1139 aa            linear   PRI 24-DEC-2025
DEFINITION  solute carrier family 12 member 5 isoform 1 [Homo sapiens].
ACCESSION   NP_001128243
VERSION     NP_001128243.1
DBSOURCE    REFSEQ: accession NM_001134771.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1139)
  AUTHORS   Pearson,A.C. and Ostroumov,A.
  TITLE     Midbrain KCC2 downregulation: Implications for stress-related and
            substance use behaviors
  JOURNAL   Curr Opin Neurobiol 88, 102901 (2024)
   PUBMED   39142020
  REMARK    GeneRIF: Midbrain KCC2 downregulation: Implications for
            stress-related and substance use behaviors.
            Review article
REFERENCE   2  (residues 1 to 1139)
  AUTHORS   Kok,M., Hartnett-Scott,K., Happe,C.L., MacDonald,M.L., Aizenman,E.
            and Brodsky,J.L.
  TITLE     The expression system influences stability, maturation efficiency,
            and oligomeric properties of the potassium-chloride co-transporter
            KCC2
  JOURNAL   Neurochem Int 174, 105695 (2024)
   PUBMED   38373478
  REMARK    GeneRIF: The expression system influences stability, maturation
            efficiency, and oligomeric properties of the potassium-chloride
            co-transporter KCC2.
REFERENCE   3  (residues 1 to 1139)
  AUTHORS   Chen,J., Wang,H., Deng,C. and Fei,M.
  TITLE     SLC12A5 as a novel potential biomarker of glioblastoma multiforme
  JOURNAL   Mol Biol Rep 50 (5), 4285-4299 (2023)
   PUBMED   36917367
  REMARK    GeneRIF: SLC12A5 as a novel potential biomarker of glioblastoma
            multiforme.
REFERENCE   4  (residues 1 to 1139)
  AUTHORS   Tong,Q., Qin,W., Li,Z.H., Liu,C., Wang,Z.C., Chu,Y. and Xu,X.D.
  TITLE     SLC12A5 promotes hepatocellular carcinoma growth and ferroptosis
            resistance by inducing ER stress and cystine transport changes
  JOURNAL   Cancer Med 12 (7), 8526-8541 (2023)
   PUBMED   36645171
  REMARK    GeneRIF: SLC12A5 promotes hepatocellular carcinoma growth and
            ferroptosis resistance by inducing ER stress and cystine transport
            changes.
REFERENCE   5  (residues 1 to 1139)
  AUTHORS   Li,Y., Li,Y.L., Liu,Y.L., Fu,J., Zhang,W.W. and Piao,Y.S.
  TITLE     [Expression of cation chloride cotransporter (NKCC1/KCC2) in brain
            tissue of children with focal cortical dysplasia type ]
  JOURNAL   Zhonghua Bing Li Xue Za Zhi 51 (11), 1123-1128 (2022)
   PUBMED   36323541
  REMARK    GeneRIF: [Expression of cation chloride cotransporter (NKCC1/KCC2)
            in brain tissue of children with focal cortical dysplasia type ].
REFERENCE   6  (residues 1 to 1139)
  AUTHORS   Hebert,S.C., Mount,D.B. and Gamba,G.
  TITLE     Molecular physiology of cation-coupled Cl- cotransport: the SLC12
            family
  JOURNAL   Pflugers Arch 447 (5), 580-593 (2004)
   PUBMED   12739168
  REMARK    Review article
REFERENCE   7  (residues 1 to 1139)
  AUTHORS   Brauer,M., Frei,E., Claes,L., Grissmer,S. and Jager,H.
  TITLE     Influence of K-Cl cotransporter activity on activation of
            volume-sensitive Cl- channels in human osteoblasts
  JOURNAL   Am J Physiol Cell Physiol 285 (1), C22-C30 (2003)
   PUBMED   12637262
  REMARK    GeneRIF: human osteoblasts express functional K-Cl cotransporters
            in their cell membrane that seem to be able to induce the indirect
            activation of volume-sensitive Cl- channels by KCl through an
            increase in the intracellular ions, water influx and cell swelling.
REFERENCE   8  (residues 1 to 1139)
  AUTHORS   Song,L., Mercado,A., Vazquez,N., Xie,Q., Desai,R., George,A.L. Jr.,
            Gamba,G. and Mount,D.B.
  TITLE     Molecular, functional, and genomic characterization of human KCC2,
            the neuronal K-Cl cotransporter
  JOURNAL   Brain Res Mol Brain Res 103 (1-2), 91-105 (2002)
   PUBMED   12106695
  REMARK    GeneRIF: Expression of hKCC2 cRNA in Xenopus laevis oocytes results
            in significant Cl(-)-dependent (86)Rb(+) uptake under isotonic
            conditions
REFERENCE   9  (residues 1 to 1139)
  AUTHORS   Sallinen,R., Tornberg,J., Putkiranta,M., Horelli-Kuitunen,N.,
            Airaksinen,M.S. and Wessman,M.
  TITLE     Chromosomal localization of SLC12A5/Slc12a5, the human and mouse
            genes for the neuron-specific K(+)-Cl(-) cotransporter (KCC2)
            defines a new region of conserved homology
  JOURNAL   Cytogenet Cell Genet 94 (1-2), 67-70 (2001)
   PUBMED   11701957
  REMARK    GeneRIF: chromosome 20 mapping
            Erratum:[Cytogenet Cell Genet. 2002;98(2-3):232]
REFERENCE   10 (residues 1 to 1139)
  AUTHORS   McTague,A. and Kurian,M.A.
  TITLE     SLC12A5-Related Epilepsy of Infancy with Migrating Focal Seizures
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30763027
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162458.10.
            
            Summary: K-Cl cotransporters are proteins that lower intracellular
            chloride concentrations below the electrochemical equilibrium
            potential. The protein encoded by this gene is an integral membrane
            K-Cl cotransporter that can function in either a net efflux or
            influx pathway, depending on the chemical concentration gradients
            of potassium and chloride. The encoded protein can act as a
            homomultimer, or as a heteromultimer with other K-Cl
            cotransporters, to maintain chloride homeostasis in neurons.
            Alternative splicing results in two transcript variants encoding
            different isoforms. [provided by RefSeq, Sep 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform (1,
            also known as KCC2a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2145743,
                              SAMEA2154665 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1139
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..1139
                     /product="solute carrier family 12 member 5 isoform 1"
                     /note="erythroid K-Cl cotransporter 2; neuronal K-Cl
                     cotransporter; solute carrier family 12
                     (potassium/chloride transporter), member 5; electroneutral
                     potassium-chloride cotransporter 2"
                     /calculated_mol_wt=126053
     Region          1..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Region          44..1139
                     /region_name="2a30"
                     /note="K-Cl cotransporter; TIGR00930"
                     /db_xref="CDD:273347"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q63633; propagated from
                     UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Region          92..116
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            99..120
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            130..151
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            175..203
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            230..250
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            251..276
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            314
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            351
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            362
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            403..420
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            430..453
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            486..513
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            535..555
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            556..578
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            593..615
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            616..632
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Region          667..681
                     /region_name="Scissor helix.
                     /evidence=ECO:0000269|PubMed:33199848,
                     ECO:0000269|PubMed:33310850, ECO:0007744|PDB:6M23,
                     ECO:0007744|PDB:7D8Z"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            929
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by OXSR1 and STK39.
                     /evidence=ECO:0000269|PubMed:19665974; propagated from
                     UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Region          942..1052
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            1030
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by OXSR1 and STK39.
                     /evidence=ECO:0000269|PubMed:19665974; propagated from
                     UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            1045
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91V14; propagated from
                     UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            1048
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91V14; propagated from
                     UniProtKB/Swiss-Prot (Q9H2X9.3)"
     Site            1049
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q91V14; propagated from
                     UniProtKB/Swiss-Prot (Q9H2X9.3)"
     CDS             1..1139
                     /gene="SLC12A5"
                     /gene_synonym="DEE34; EIEE34; EIG14; hKCC2; KCC2"
                     /coded_by="NM_001134771.2:81..3500"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46610.1"
                     /db_xref="GeneID:57468"
                     /db_xref="HGNC:HGNC:13818"
                     /db_xref="MIM:606726"
ORIGIN      
        1 msrrftvtsl ppagparspd pesrrhsvad prhlpgedvk gdgnpkessp finstdtekg
       61 keydgknmal feeemdtspm vssllsglan ytnlpqgsre heeaennegg kkkpvqaprm
      121 gtfmgvylpc lqnifgvilf lrltwvvgia gimesfcmvf iccsctmlta ismsaiatng
      181 vvpaggsyym isrslgpefg gavglcfylg ttfagamyil gtieillayl fpamaifkae
      241 dasgeaaaml nnmrvygtcv ltcmatvvfv gvkyvnkfal vflgcvilsi laiyagviks
      301 afdppnfpic llgnrtlsrh gfdvcaklaw egnetvttrl wglfcssrfl natcdeyftr
      361 nnvteiqgip gaasgliken lwssyltkgv iversgmtsv gladgtpidm dhpyvfsdmt
      421 syftllvgiy fpsvtgimag snrsgdlrda qksiptgtil aiattsavyi ssvvlfgaci
      481 egvvlrdkfg eavngnlvvg tlawpspwvi vigsffstcg aglqsltgap rllqaisrdg
      541 ivpflqvfgh gkangeptwa llltacicei giliasldev apilsmfflm cymfvnlaca
      601 vqtllrtpnw rprfryyhwt lsflgmslcl almficswyy alvamliagl iykyieyrga
      661 ekewgdgirg lslsaaryal lrleegppht knwrpqllvl vrvdqdqnvv hpqllsltsq
      721 lkagkgltiv gsvlegtfle nhpqaqraee sirrlmeaek vkgfcqvvis snlrdgvshl
      781 iqsgglgglq hntvlvgwpr nwrqkedhqt wrnfielvre ttaghlallv tknvsmfpgn
      841 perfsegsid vwwivhdggm lmllpfllrh hkvwrkckmr iftvaqmddn siqmkkdltt
      901 flyhlritae vevvemhesd isaytyektl vmeqrsqilk qmhltknere reiqsitdes
      961 rgsirrknpa ntrlrlnvpe etagdseekp eeevqlihdq sapscpsssp spgeepegeg
     1021 etdpekvhlt wtkdksvaek nkgpspvsse gikdffsmkp ewenlnqsnv rrmhtavrln
     1081 evivkksrda klvllnmpgp prnrngdeny meflevlteh ldrvmlvrgg grevitiys
//
LOCUS       NP_065759               1116 aa            linear   PRI 24-DEC-2025
DEFINITION  solute carrier family 12 member 5 isoform 2 [Homo sapiens].
ACCESSION   NP_065759
VERSION     NP_065759.1
DBSOURCE    REFSEQ: accession NM_020708.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1116)
  AUTHORS   Pearson,A.C. and Ostroumov,A.
  TITLE     Midbrain KCC2 downregulation: Implications for stress-related and
            substance use behaviors
  JOURNAL   Curr Opin Neurobiol 88, 102901 (2024)
   PUBMED   39142020
  REMARK    GeneRIF: Midbrain KCC2 downregulation: Implications for
            stress-related and substance use behaviors.
            Review article
REFERENCE   2  (residues 1 to 1116)
  AUTHORS   Kok,M., Hartnett-Scott,K., Happe,C.L., MacDonald,M.L., Aizenman,E.
            and Brodsky,J.L.
  TITLE     The expression system influences stability, maturation efficiency,
            and oligomeric properties of the potassium-chloride co-transporter
            KCC2
  JOURNAL   Neurochem Int 174, 105695 (2024)
   PUBMED   38373478
  REMARK    GeneRIF: The expression system influences stability, maturation
            efficiency, and oligomeric properties of the potassium-chloride
            co-transporter KCC2.
REFERENCE   3  (residues 1 to 1116)
  AUTHORS   Chen,J., Wang,H., Deng,C. and Fei,M.
  TITLE     SLC12A5 as a novel potential biomarker of glioblastoma multiforme
  JOURNAL   Mol Biol Rep 50 (5), 4285-4299 (2023)
   PUBMED   36917367
  REMARK    GeneRIF: SLC12A5 as a novel potential biomarker of glioblastoma
            multiforme.
REFERENCE   4  (residues 1 to 1116)
  AUTHORS   Tong,Q., Qin,W., Li,Z.H., Liu,C., Wang,Z.C., Chu,Y. and Xu,X.D.
  TITLE     SLC12A5 promotes hepatocellular carcinoma growth and ferroptosis
            resistance by inducing ER stress and cystine transport changes
  JOURNAL   Cancer Med 12 (7), 8526-8541 (2023)
   PUBMED   36645171
  REMARK    GeneRIF: SLC12A5 promotes hepatocellular carcinoma growth and
            ferroptosis resistance by inducing ER stress and cystine transport
            changes.
REFERENCE   5  (residues 1 to 1116)
  AUTHORS   Li,Y., Li,Y.L., Liu,Y.L., Fu,J., Zhang,W.W. and Piao,Y.S.
  TITLE     [Expression of cation chloride cotransporter (NKCC1/KCC2) in brain
            tissue of children with focal cortical dysplasia type ]
  JOURNAL   Zhonghua Bing Li Xue Za Zhi 51 (11), 1123-1128 (2022)
   PUBMED   36323541
  REMARK    GeneRIF: [Expression of cation chloride cotransporter (NKCC1/KCC2)
            in brain tissue of children with focal cortical dysplasia type ].
REFERENCE   6  (residues 1 to 1116)
  AUTHORS   Hebert,S.C., Mount,D.B. and Gamba,G.
  TITLE     Molecular physiology of cation-coupled Cl- cotransport: the SLC12
            family
  JOURNAL   Pflugers Arch 447 (5), 580-593 (2004)
   PUBMED   12739168
  REMARK    Review article
REFERENCE   7  (residues 1 to 1116)
  AUTHORS   Brauer,M., Frei,E., Claes,L., Grissmer,S. and Jager,H.
  TITLE     Influence of K-Cl cotransporter activity on activation of
            volume-sensitive Cl- channels in human osteoblasts
  JOURNAL   Am J Physiol Cell Physiol 285 (1), C22-C30 (2003)
   PUBMED   12637262
  REMARK    GeneRIF: human osteoblasts express functional K-Cl cotransporters
            in their cell membrane that seem to be able to induce the indirect
            activation of volume-sensitive Cl- channels by KCl through an
            increase in the intracellular ions, water influx and cell swelling.
REFERENCE   8  (residues 1 to 1116)
  AUTHORS   Song,L., Mercado,A., Vazquez,N., Xie,Q., Desai,R., George,A.L. Jr.,
            Gamba,G. and Mount,D.B.
  TITLE     Molecular, functional, and genomic characterization of human KCC2,
            the neuronal K-Cl cotransporter
  JOURNAL   Brain Res Mol Brain Res 103 (1-2), 91-105 (2002)
   PUBMED   12106695
  REMARK    GeneRIF: Expression of hKCC2 cRNA in Xenopus laevis oocytes results
            in significant Cl(-)-dependent (86)Rb(+) uptake under isotonic
            conditions
REFERENCE   9  (residues 1 to 1116)
  AUTHORS   Sallinen,R., Tornberg,J., Putkiranta,M., Horelli-Kuitunen,N.,
            Airaksinen,M.S. and Wessman,M.
  TITLE     Chromosomal localization of SLC12A5/Slc12a5, the human and mouse
            genes for the neuron-specific K(+)-Cl(-) cotransporter (KCC2)
            defines a new region of conserved homology
  JOURNAL   Cytogenet Cell Genet 94 (1-2), 67-70 (2001)
   PUBMED   11701957
  REMARK    GeneRIF: chromosome 20 mapping
            Erratum:[Cytogenet Cell Genet. 2002;98(2-3):232]
REFERENCE   10 (residues 1 to 1116)
  AUTHORS   McTague,A. and Kurian,M.A.
  TITLE     SLC12A5-Related Epilepsy of Infancy with Migrating Focal Seizures
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30763027
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162458.10.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: K-Cl cotransporters are proteins that lower intracellular
            chloride concentrations below the electrochemical equilibrium
            potential. The protein encoded by this gene is an integral membrane
            K-Cl cotransporter that can function in either a net efflux or
            influx pathway, depending on the chemical concentration gradients
            of potassium and chloride. The encoded protein can act as a
            homomultimer, or as a heteromultimer with other K-Cl
            cotransporters, to maintain chloride homeostasis in neurons.
            Alternative splicing results in two transcript variants encoding
            different isoforms. [provided by RefSeq, Sep 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and 5'
            coding region, compared to variant 1. The resulting isoform (2,
            also known as KCC2b) has a distinct N-terminus and is shorter than
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC132670.1, AF208159.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000243964.7/ ENSP00000243964.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1116
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..1116
                     /product="solute carrier family 12 member 5 isoform 2"
                     /note="erythroid K-Cl cotransporter 2; neuronal K-Cl
                     cotransporter; solute carrier family 12
                     (potassium/chloride transporter), member 5; electroneutral
                     potassium-chloride cotransporter 2"
                     /calculated_mol_wt=123381
     Region          21..1116
                     /region_name="2a30"
                     /note="K-Cl cotransporter; TIGR00930"
                     /db_xref="CDD:273347"
     CDS             1..1116
                     /gene="SLC12A5"
                     /gene_synonym="DEE34; EIEE34; EIG14; hKCC2; KCC2"
                     /coded_by="NM_020708.5:131..3481"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS13391.1"
                     /db_xref="GeneID:57468"
                     /db_xref="HGNC:HGNC:13818"
                     /db_xref="MIM:606726"
ORIGIN      
        1 mlnnltdced gdgganpgdg npkesspfin stdtekgkey dgknmalfee emdtspmvss
       61 llsglanytn lpqgsrehee aenneggkkk pvqaprmgtf mgvylpclqn ifgvilflrl
      121 twvvgiagim esfcmvficc sctmltaism saiatngvvp aggsyymisr slgpefggav
      181 glcfylgttf agamyilgti eillaylfpa maifkaedas geaaamlnnm rvygtcvltc
      241 matvvfvgvk yvnkfalvfl gcvilsilai yagviksafd ppnfpicllg nrtlsrhgfd
      301 vcaklawegn etvttrlwgl fcssrflnat cdeyftrnnv teiqgipgaa sglikenlws
      361 syltkgvive rsgmtsvgla dgtpidmdhp yvfsdmtsyf tllvgiyfps vtgimagsnr
      421 sgdlrdaqks iptgtilaia ttsavyissv vlfgaciegv vlrdkfgeav ngnlvvgtla
      481 wpspwvivig sffstcgagl qsltgaprll qaisrdgivp flqvfghgka ngeptwalll
      541 taciceigil iasldevapi lsmfflmcym fvnlacavqt llrtpnwrpr fryyhwtlsf
      601 lgmslclalm ficswyyalv amliagliyk yieyrgaeke wgdgirglsl saaryallrl
      661 eegpphtknw rpqllvlvrv dqdqnvvhpq llsltsqlka gkgltivgsv legtflenhp
      721 qaqraeesir rlmeaekvkg fcqvvissnl rdgvshliqs gglgglqhnt vlvgwprnwr
      781 qkedhqtwrn fielvretta ghlallvtkn vsmfpgnper fsegsidvww ivhdggmlml
      841 lpfllrhhkv wrkckmrift vaqmddnsiq mkkdlttfly hlritaevev vemhesdisa
      901 ytyektlvme qrsqilkqmh ltknererei qsitdesrgs irrknpantr lrlnvpeeta
      961 gdseekpeee vqlihdqsap scpssspspg eepegegetd pekvhltwtk dksvaeknkg
     1021 pspvssegik dffsmkpewe nlnqsnvrrm htavrlnevi vkksrdaklv llnmpgpprn
     1081 rngdenymef levltehldr vmlvrgggre vitiys
//
LOCUS       NP_001171914            2642 aa            linear   PRI 24-DEC-2025
DEFINITION  serine/threonine-protein kinase WNK1 isoform 4 [Homo sapiens].
ACCESSION   NP_001171914
VERSION     NP_001171914.1
DBSOURCE    REFSEQ: accession NM_001184985.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2642)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2642)
  AUTHORS   Li,L., Xie,D., Yu,S., Ma,M., Fan,K., Chen,J., Xiu,M., Xie,K., Li,Y.
            and Gao,Y.
  TITLE     WNK1 Interaction with KEAP1 Promotes NRF2 Stabilization to Enhance
            the Oxidative Stress Response in Hepatocellular Carcinoma
  JOURNAL   Cancer Res 84 (17), 2776-2791 (2024)
   PUBMED   38885324
  REMARK    GeneRIF: WNK1 Interaction with KEAP1 Promotes NRF2 Stabilization to
            Enhance the Oxidative Stress Response in Hepatocellular Carcinoma.
REFERENCE   3  (residues 1 to 2642)
  AUTHORS   Ma,Y., Zong,H., Pan,P., Shang,H. and Yang,X.
  TITLE     The CREB1/WNK1 axis promotes the tumorigenesis of ovarian cancer
            via regulating HIF-1
  JOURNAL   Exp Cell Res 438 (1), 114006 (2024)
   PUBMED   38599542
  REMARK    GeneRIF: The CREB1/WNK1 axis promotes the tumorigenesis of ovarian
            cancer via regulating HIF-1.
REFERENCE   4  (residues 1 to 2642)
  AUTHORS   Newhouse,S., Farrall,M., Wallace,C., Hoti,M., Burke,B., Howard,P.,
            Onipinla,A., Lee,K., Shaw-Hawkins,S., Dobson,R., Brown,M.,
            Samani,N.J., Dominiczak,A.F., Connell,J.M., Lathrop,G.M.,
            Kooner,J., Chambers,J., Elliott,P., Clarke,R., Collins,R., Laan,M.,
            Org,E., Juhanson,P., Veldre,G., Viigimaa,M., Eyheramendy,S.,
            Cappuccio,F.P., Ji,C., Iacone,R., Strazzullo,P., Kumari,M.,
            Marmot,M., Brunner,E., Caulfield,M. and Munroe,P.B.
  TITLE     Polymorphisms in the WNK1 gene are associated with blood pressure
            variation and urinary potassium excretion
  JOURNAL   PLoS One 4 (4), e5003 (2009)
   PUBMED   19347040
  REMARK    GeneRIF: data indicates that multiple rare and common WNK1 variants
            contribute to BP variation and hypertension, and provide compelling
            evidence to initiate further genetic and functional studies to
            explore the role of WNK1 in BP regulation and EH
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 2642)
  AUTHORS   Shekarabi,M., Girard,N., Riviere,J.B., Dion,P., Houle,M.,
            Toulouse,A., Lafreniere,R.G., Vercauteren,F., Hince,P.,
            Laganiere,J., Rochefort,D., Faivre,L., Samuels,M. and Rouleau,G.A.
  TITLE     Mutations in the nervous system--specific HSN2 exon of WNK1 cause
            hereditary sensory neuropathy type II
  JOURNAL   J Clin Invest 118 (7), 2496-2505 (2008)
   PUBMED   18521183
  REMARK    GeneRIF: HSN2 is a nervous system-specific exon of the WNK1 gene
            (WNK1/HSN2 isoform).
REFERENCE   6  (residues 1 to 2642)
  AUTHORS   Disse-Nicodeme,S., Achard,J.M., Desitter,I., Houot,A.M.,
            Fournier,A., Corvol,P. and Jeunemaitre,X.
  TITLE     A new locus on chromosome 12p13.3 for pseudohypoaldosteronism type
            II, an autosomal dominant form of hypertension
  JOURNAL   Am J Hum Genet 67 (2), 302-310 (2000)
   PUBMED   10869238
REFERENCE   7  (residues 1 to 2642)
  AUTHORS   Moore,T.M., Garg,R., Johnson,C., Coptcoat,M.J., Ridley,A.J. and
            Morris,J.D.
  TITLE     PSK, a novel STE20-like kinase derived from prostatic carcinoma
            that activates the c-Jun N-terminal kinase mitogen-activated
            protein kinase pathway and regulates actin cytoskeletal
            organization
  JOURNAL   J Biol Chem 275 (6), 4311-4322 (2000)
   PUBMED   10660600
REFERENCE   8  (residues 1 to 2642)
  AUTHORS   Ellison,D.H.
  TITLE     Pseudohypoaldosteronism Type II
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22073419
REFERENCE   9  (residues 1 to 2642)
  AUTHORS   Kurth,I.
  TITLE     Hereditary Sensory and Autonomic Neuropathy Type II
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21089229
REFERENCE   10 (residues 1 to 2642)
  AUTHORS   Ota,M., Ellefson,R.D., Lambert,E.H. and Dyck,P.J.
  TITLE     Hereditary sensory neuropathy, type II. Clinical,
            electrophysiologic, histologic, and biochemical studies of a Quebec
            kinship
  JOURNAL   Arch Neurol 29 (1), 23-37 (1973)
   PUBMED   4351257
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004765.2 and AC004803.11.
            
            Summary: This gene encodes a member of the WNK subfamily of
            serine/threonine protein kinases. The encoded protein may be a key
            regulator of blood pressure by controlling the transport of sodium
            and chloride ions. Mutations in this gene have been associated with
            pseudohypoaldosteronism type II and hereditary sensory neuropathy
            type II. Alternatively spliced transcript variants encoding
            different isoforms have been described but the full-length nature
            of all of them has yet to be determined.[provided by RefSeq, May
            2010].
            
            Transcript Variant: This variant (4) has multiple differences in
            the coding region but maintains the reading frame compared to
            variant 1. This variant represents the exon combination of the
            dorsal root ganglia and sciatic nerve variant described in Figure
            2F of PubMed ID 18521183. This variant encodes isoform 4, which is
            longer than isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments. The combination of alternatively
            spliced exons within the coding region is inferred based on
            experimental evidence reported in Figures 2F and 3 from PubMed ID
            18521183.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.981891.1,
                                           SRR14038193.3450639.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2642
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..2642
                     /product="serine/threonine-protein kinase WNK1 isoform 4"
                     /EC_number="2.7.11.1"
                     /note="prostate-derived sterile 20-like kinase;
                     erythrocyte 65 kDa protein; protein kinase with no lysine
                     1; protein phosphatase 1, regulatory subunit 167;
                     serine/threonine-protein kinase WNK1 1;
                     serine/threonine-protein kinase WNK1 2"
                     /calculated_mol_wt=279583
     Region          1..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17190791; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH7; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          95..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17190791,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          195..483
                     /region_name="STKc_WNK1"
                     /note="Catalytic domain of the Serine/Threonine protein
                     kinase, With No Lysine (WNK) 1; cd14030"
                     /db_xref="CDD:270932"
     Site            order(227..231,233,235,248,250,281,301..304,308,310,349,
                     351,353..354,356,368,371,385..388)
                     /site_type="active"
                     /db_xref="CDD:270932"
     Site            order(227..231,233,235,248,250,281,301..304,308,349,351,
                     353..354,356,368)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270932"
     Site            order(231,308,310,349,351,353,371,385..388)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270932"
     Site            367..388
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270932"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:31656913; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15883153,
                     ECO:0000269|PubMed:16263722, ECO:0000269|PubMed:16832045,
                     ECO:0000269|PubMed:17190791, ECO:0000269|PubMed:31656913,
                     ECO:0000269|PubMed:34289367; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          488..555
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          500..563
                     /region_name="OSR1_C"
                     /note="Oxidative-stress-responsive kinase 1 C-terminal
                     domain; pfam12202"
                     /db_xref="CDD:463491"
     Region          628..638
                     /region_name="Interaction with KLHL3.
                     /evidence=ECO:0000250|UniProtKB:Q96J92"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          <1833..2127
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..2642
                     /gene="WNK1"
                     /gene_synonym="HSAN2; HSN2; KDP; p65; PPP1R167; PRKWNK1;
                     PSK"
                     /coded_by="NM_001184985.2:988..8916"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:65125"
                     /db_xref="HGNC:HGNC:14540"
                     /db_xref="MIM:605232"
ORIGIN      
        1 msggaaekqs stpgslflsp papapkngss sdssvgeklg aaaadavtgr teeyrrrrht
       61 mdkdsrgaaa tttttehrff rrsvicdsna talelpglpl slpqpsipaa vpqsappeph
      121 reetvtatat sqvaqqppaa aapgeqavag papstvpsst skdrpvsqps lvgskeeppp
      181 arsgsgggsa kepqeersqq qddieeletk avgmsndgrf lkfdieigrg sfktvykgld
      241 tettvevawc elqdrkltks erqrfkeeae mlkglqhpni vrfydswest vkgkkcivlv
      301 telmtsgtlk tylkrfkvmk ikvlrswcrq ilkglqflht rtppiihrdl kcdnifitgp
      361 tgsvkigdlg latlkrasfa ksvigtpefm apemyeekyd esvdvyafgm cmlematsey
      421 pysecqnaaq iyrrvtsgvk pasfdkvaip evkeiiegci rqnkderysi kdllnhaffq
      481 eetgvrvela eeddgekiai klwlriedik klkgkykdne aiefsfdler dvpedvaqem
      541 vesgyvcegd hktmakaikd rvslikrkre qrqlvreeqe kkkqeesslk qqveqssasq
      601 tgikqlpsas tgiptastts asvstqvepe epeadqhqql qyqqpsisvl sdgtvdsgqg
      661 ssvftesrvs sqqtvsygsq heqahstgtv pghipstvqa qsqphgvypp ssvpqsmahp
      721 cggtptypes qiffptiher pvsfsppptc ppkvaisqrr kstsfleaqt hhfqpllrtv
      781 gqsllppggs ptnwtpeavv mlgttasrvt gesceiqvhp mfepsqvysd yrpglvlpee
      841 ahyfipqeav yvagvhyqar vaeqyegipy nssvlsspmk qipeqkpvqg gptsssvfef
      901 psgqaflvgh lqnlrldsgl gpgsplssis apistdatrl kfhpvfvphs apavlthnne
      961 srsncvfefh vhtpssssge gggilpqrvy rnrqvavdln qeelppqsvg lhgylqpvte
     1021 ekhnyhapel tvsvvepigq nwpigspeys sdssqitssd psdfqspppt ggaaapfgsd
     1081 vsmpfihlpq tvlqesplff cfpqgttsqq vltasfssgg salhpqaqgq sqgqpssssl
     1141 tgvsssqpiq hpqqqqgiqq tappqqtvqy slsqtstsse attaqpvsqp qapqvlpqvs
     1201 agkqgfpprl ppqypgdsni apssnvasvc ihstvlsppm ptevlatpgy fptvvqpyve
     1261 snllvpmggv ggqvqvsqpg gslaqaptts sqqavlestq gvsqvapaep vavaqtqatq
     1321 pttlassvds ahsdvasgms dgnenvpsss grhegrttkr hyrksvrsrs rhektsrpkl
     1381 rilnvsnkgd rvvecqleth nrkmvtfkfd ldgdnpeeia timvnndfil aieresfvdq
     1441 vreiiekade mlsedvsvep egdqgleslq gkddygfsgs qklegefkqp ipassmpqqi
     1501 giptssltqv vhsagrrfiv spvpesrlre skvfpseitd tvaastaqsp gmnlshsass
     1561 lslqqafsel rraqmtegpn tappnfshtg ptfpvvppfl ssiagvptta aatapvpats
     1621 sppndistsv iqsevtvpte egiagvatst gvvtsgglpi ppvsespvls svvssitipa
     1681 vvsisttsps lqvptstsei vvsstalyps vtvsatsasa ggstatpgpk ppavvsqqaa
     1741 gsttvgatlt svstttsfps tasqlciqls sststptlae tvvvsahsld ktshssttgl
     1801 afslsapsss sspgagvssy isqpgglhpl vipsviastp ilpqaagpts tpllpqvpsi
     1861 pplvqpvanv pavqqtlihs qpqpallpnq phthcpevds dtqpkapgid diktleeklr
     1921 slfsehsssg aqhasvslet slviestvtp gipttavaps klltsttstc lpptnlplgt
     1981 valpvtpvvt pgqvstpvst ttsgvkpgta pskppltkap vlpvgtelpa gtlpseqlpp
     2041 fpgpsltqsq qpledldaql rrtlspemit vtsavgpvsm aaptaiteag tqpqkgvsqv
     2101 kegpvlatss gagvfkmgrf qvsvaadgaq kegknkseda ksvhfessts essvlssssp
     2161 estlvkpepn gitipgissd vpesahktta seaksdtgqp tkvgrfqvtt tankvgrfsv
     2221 sktedkitdt kkegpvaspp fmdleqavlp avipkkekpe lsepshlngp ssdpeaafls
     2281 rdvddgsgsp hsphqlssks lpsqnlsqsl snsfnssyms sdnesdiede dlklelrrlr
     2341 dkhlkeiqdl qsrqkheies lytklgkvpp aviippaapl sgrrrrptks kgskssrsss
     2401 lgnkspqlsg nlsgqsaasv lhpqqtlhpp gnipesgqnq llqplkpsps sdnlysafts
     2461 dgaisvpsls apgqgtsstn tvgatvnsqa aqaqppamts srkgtftddl hklvdnward
     2521 amnlsgrrgs kghmnyegpg markfsapgq lcismtsnlg gsapisaasa tslghftksm
     2581 cppqqygfpa tpfgaqwsgt ggpapqplgq fqpvgtaslq nfnisnlqks isnppgsnlr
     2641 tt
//
LOCUS       NP_061852               2382 aa            linear   PRI 24-DEC-2025
DEFINITION  serine/threonine-protein kinase WNK1 isoform 1 [Homo sapiens].
ACCESSION   NP_061852
VERSION     NP_061852.3
DBSOURCE    REFSEQ: accession NM_018979.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2382)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2382)
  AUTHORS   Li,L., Xie,D., Yu,S., Ma,M., Fan,K., Chen,J., Xiu,M., Xie,K., Li,Y.
            and Gao,Y.
  TITLE     WNK1 Interaction with KEAP1 Promotes NRF2 Stabilization to Enhance
            the Oxidative Stress Response in Hepatocellular Carcinoma
  JOURNAL   Cancer Res 84 (17), 2776-2791 (2024)
   PUBMED   38885324
  REMARK    GeneRIF: WNK1 Interaction with KEAP1 Promotes NRF2 Stabilization to
            Enhance the Oxidative Stress Response in Hepatocellular Carcinoma.
REFERENCE   3  (residues 1 to 2382)
  AUTHORS   Ma,Y., Zong,H., Pan,P., Shang,H. and Yang,X.
  TITLE     The CREB1/WNK1 axis promotes the tumorigenesis of ovarian cancer
            via regulating HIF-1
  JOURNAL   Exp Cell Res 438 (1), 114006 (2024)
   PUBMED   38599542
  REMARK    GeneRIF: The CREB1/WNK1 axis promotes the tumorigenesis of ovarian
            cancer via regulating HIF-1.
REFERENCE   4  (residues 1 to 2382)
  AUTHORS   Newhouse,S., Farrall,M., Wallace,C., Hoti,M., Burke,B., Howard,P.,
            Onipinla,A., Lee,K., Shaw-Hawkins,S., Dobson,R., Brown,M.,
            Samani,N.J., Dominiczak,A.F., Connell,J.M., Lathrop,G.M.,
            Kooner,J., Chambers,J., Elliott,P., Clarke,R., Collins,R., Laan,M.,
            Org,E., Juhanson,P., Veldre,G., Viigimaa,M., Eyheramendy,S.,
            Cappuccio,F.P., Ji,C., Iacone,R., Strazzullo,P., Kumari,M.,
            Marmot,M., Brunner,E., Caulfield,M. and Munroe,P.B.
  TITLE     Polymorphisms in the WNK1 gene are associated with blood pressure
            variation and urinary potassium excretion
  JOURNAL   PLoS One 4 (4), e5003 (2009)
   PUBMED   19347040
  REMARK    GeneRIF: data indicates that multiple rare and common WNK1 variants
            contribute to BP variation and hypertension, and provide compelling
            evidence to initiate further genetic and functional studies to
            explore the role of WNK1 in BP regulation and EH
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 2382)
  AUTHORS   Shekarabi,M., Girard,N., Riviere,J.B., Dion,P., Houle,M.,
            Toulouse,A., Lafreniere,R.G., Vercauteren,F., Hince,P.,
            Laganiere,J., Rochefort,D., Faivre,L., Samuels,M. and Rouleau,G.A.
  TITLE     Mutations in the nervous system--specific HSN2 exon of WNK1 cause
            hereditary sensory neuropathy type II
  JOURNAL   J Clin Invest 118 (7), 2496-2505 (2008)
   PUBMED   18521183
  REMARK    GeneRIF: HSN2 is a nervous system-specific exon of the WNK1 gene
            (WNK1/HSN2 isoform).
REFERENCE   6  (residues 1 to 2382)
  AUTHORS   Disse-Nicodeme,S., Achard,J.M., Desitter,I., Houot,A.M.,
            Fournier,A., Corvol,P. and Jeunemaitre,X.
  TITLE     A new locus on chromosome 12p13.3 for pseudohypoaldosteronism type
            II, an autosomal dominant form of hypertension
  JOURNAL   Am J Hum Genet 67 (2), 302-310 (2000)
   PUBMED   10869238
REFERENCE   7  (residues 1 to 2382)
  AUTHORS   Moore,T.M., Garg,R., Johnson,C., Coptcoat,M.J., Ridley,A.J. and
            Morris,J.D.
  TITLE     PSK, a novel STE20-like kinase derived from prostatic carcinoma
            that activates the c-Jun N-terminal kinase mitogen-activated
            protein kinase pathway and regulates actin cytoskeletal
            organization
  JOURNAL   J Biol Chem 275 (6), 4311-4322 (2000)
   PUBMED   10660600
REFERENCE   8  (residues 1 to 2382)
  AUTHORS   Ellison,D.H.
  TITLE     Pseudohypoaldosteronism Type II
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22073419
REFERENCE   9  (residues 1 to 2382)
  AUTHORS   Kurth,I.
  TITLE     Hereditary Sensory and Autonomic Neuropathy Type II
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21089229
REFERENCE   10 (residues 1 to 2382)
  AUTHORS   Ota,M., Ellefson,R.D., Lambert,E.H. and Dyck,P.J.
  TITLE     Hereditary sensory neuropathy, type II. Clinical,
            electrophysiologic, histologic, and biochemical studies of a Quebec
            kinship
  JOURNAL   Arch Neurol 29 (1), 23-37 (1973)
   PUBMED   4351257
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004765.2, AJ296290.1,
            CD629562.1, AB002342.2, BX644268.1, DA720959.1, AC004803.11,
            BC141881.1 and AI074334.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 27, 2010 this sequence version replaced NP_061852.2.
            
            Summary: This gene encodes a member of the WNK subfamily of
            serine/threonine protein kinases. The encoded protein may be a key
            regulator of blood pressure by controlling the transport of sodium
            and chloride ions. Mutations in this gene have been associated with
            pseudohypoaldosteronism type II and hereditary sensory neuropathy
            type II. Alternatively spliced transcript variants encoding
            different isoforms have been described but the full-length nature
            of all of them has yet to be determined.[provided by RefSeq, May
            2010].
            
            Transcript Variant: This variant (1) encodes the most common
            isoform (1), as indicated in PubMed ID 18521183.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ296290.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000315939.11/ ENSP00000313059.6
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..2382
                     /product="serine/threonine-protein kinase WNK1 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="prostate-derived sterile 20-like kinase;
                     erythrocyte 65 kDa protein; protein kinase with no lysine
                     1; protein phosphatase 1, regulatory subunit 167;
                     serine/threonine-protein kinase WNK1 1;
                     serine/threonine-protein kinase WNK1 2"
                     /calculated_mol_wt=250664
     Region          1..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17190791; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH7; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          95..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17190791,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          195..483
                     /region_name="STKc_WNK1"
                     /note="Catalytic domain of the Serine/Threonine protein
                     kinase, With No Lysine (WNK) 1; cd14030"
                     /db_xref="CDD:270932"
     Site            order(227..231,233,235,248,250,281,301..304,308,310,349,
                     351,353..354,356,368,371,385..388)
                     /site_type="active"
                     /db_xref="CDD:270932"
     Site            order(227..231,233,235,248,250,281,301..304,308,349,351,
                     353..354,356,368)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270932"
     Site            order(231,308,310,349,351,353,371,385..388)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270932"
     Site            367..388
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270932"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:31656913; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15883153,
                     ECO:0000269|PubMed:16263722, ECO:0000269|PubMed:16832045,
                     ECO:0000269|PubMed:17190791, ECO:0000269|PubMed:31656913,
                     ECO:0000269|PubMed:34289367; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          488..555
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          500..563
                     /region_name="OSR1_C"
                     /note="Oxidative-stress-responsive kinase 1 C-terminal
                     domain; pfam12202"
                     /db_xref="CDD:463491"
     Region          573..779
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          628..638
                     /region_name="Interaction with KLHL3.
                     /evidence=ECO:0000250|UniProtKB:Q96J92"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          <765..1094
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1018..1041
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          1053..1119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          1257..1260
                     /region_name="RFXV motif 1.
                     /evidence=ECO:0000269|PubMed:16263722"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            1261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17190791,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          1457..1476
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          <1573..1867
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1733..1790
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            1848
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17190791; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          1859..1862
                     /region_name="RFXV motif 2.
                     /evidence=ECO:0000269|PubMed:16263722"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          1866..1948
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          1945..1948
                     /region_name="RFXV motif 3.
                     /evidence=ECO:0000269|PubMed:16263722"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          1957..1960
                     /region_name="RFXV motif 4.
                     /evidence=ECO:0000269|PubMed:16263722"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            1978
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          1994..2069
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            2002
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            2011
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            2012
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17190791,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            2027
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            2029
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17190791,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            2032
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17190791,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          2101..2196
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            2121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          2241..2261
                     /region_name="Amphipathic alpha-helix.
                     /evidence=ECO:0000269|PubMed:33964204"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            2270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P83741; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            2286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P83741; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Region          2332..2352
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            2370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     Site            2372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17190791,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H4A3.2)"
     CDS             1..2382
                     /gene="WNK1"
                     /gene_synonym="HSAN2; HSN2; KDP; p65; PPP1R167; PRKWNK1;
                     PSK"
                     /coded_by="NM_018979.4:988..8136"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8506.1"
                     /db_xref="GeneID:65125"
                     /db_xref="HGNC:HGNC:14540"
                     /db_xref="MIM:605232"
ORIGIN      
        1 msggaaekqs stpgslflsp papapkngss sdssvgeklg aaaadavtgr teeyrrrrht
       61 mdkdsrgaaa tttttehrff rrsvicdsna talelpglpl slpqpsipaa vpqsappeph
      121 reetvtatat sqvaqqppaa aapgeqavag papstvpsst skdrpvsqps lvgskeeppp
      181 arsgsgggsa kepqeersqq qddieeletk avgmsndgrf lkfdieigrg sfktvykgld
      241 tettvevawc elqdrkltks erqrfkeeae mlkglqhpni vrfydswest vkgkkcivlv
      301 telmtsgtlk tylkrfkvmk ikvlrswcrq ilkglqflht rtppiihrdl kcdnifitgp
      361 tgsvkigdlg latlkrasfa ksvigtpefm apemyeekyd esvdvyafgm cmlematsey
      421 pysecqnaaq iyrrvtsgvk pasfdkvaip evkeiiegci rqnkderysi kdllnhaffq
      481 eetgvrvela eeddgekiai klwlriedik klkgkykdne aiefsfdler dvpedvaqem
      541 vesgyvcegd hktmakaikd rvslikrkre qrqlvreeqe kkkqeesslk qqveqssasq
      601 tgikqlpsas tgiptastts asvstqvepe epeadqhqql qyqqpsisvl sdgtvdsgqg
      661 ssvftesrvs sqqtvsygsq heqahstgtv pghipstvqa qsqphgvypp ssvaqgqsqg
      721 qpssssltgv sssqpiqhpq qqqgiqqtap pqqtvqysls qtstsseatt aqpvsqpqap
      781 qvlpqvsagk qlpvsqpvpt iqgepqipva tqpsvvpvhs gahflpvgqp lptpllpqyp
      841 vsqipistph vstaqtgfss lpitmaagit qplltlassa ttaaipgvst vvpsqlptll
      901 qpvtqlpsqv hpqllqpavq smgipanlgq aaevplssgd vlyqgfpprl ppqypgdsni
      961 apssnvasvc ihstvlsppm ptevlatpgy fptvvqpyve snllvpmggv ggqvqvsqpg
     1021 gslaqaptts sqqavlestq gvsqvapaep vavaqtqatq pttlassvds ahsdvasgms
     1081 dgnenvpsss grhegrttkr hyrksvrsrs rhektsrpkl rilnvsnkgd rvvecqleth
     1141 nrkmvtfkfd ldgdnpeeia timvnndfil aieresfvdq vreiiekade mlsedvsvep
     1201 egdqgleslq gkddygfsgs qklegefkqp ipassmpqqi giptssltqv vhsagrrfiv
     1261 spvpesrlre skvfpseitd tvaastaqsp gmnlshsass lslqqafsel rraqmtegpn
     1321 tappnfshtg ptfpvvppfl ssiagvptta aatapvpats sppndistsv iqsevtvpte
     1381 egiagvatst gvvtsgglpi ppvsespvls svvssitipa vvsisttsps lqvptstsei
     1441 vvsstalyps vtvsatsasa ggstatpgpk ppavvsqqaa gsttvgatlt svstttsfps
     1501 tasqlciqls sststptlae tvvvsahsld ktshssttgl afslsapsss sspgagvssy
     1561 isqpgglhpl vipsviastp ilpqaagpts tpllpqvpsi pplvqpvanv pavqqtlihs
     1621 qpqpallpnq phthcpevds dtqpkapgid diktleeklr slfsehsssg aqhasvslet
     1681 slviestvtp gipttavaps klltsttstc lpptnlplgt valpvtpvvt pgqvstpvst
     1741 ttsgvkpgta pskppltkap vlpvgtelpa gtlpseqlpp fpgpsltqsq qpledldaql
     1801 rrtlspemit vtsavgpvsm aaptaiteag tqpqkgvsqv kegpvlatss gagvfkmgrf
     1861 qvsvaadgaq kegknkseda ksvhfessts essvlssssp estlvkpepn gitipgissd
     1921 vpesahktta seaksdtgqp tkvgrfqvtt tankvgrfsv sktedkitdt kkegpvaspp
     1981 fmdleqavlp avipkkekpe lsepshlngp ssdpeaafls rdvddgsgsp hsphqlssks
     2041 lpsqnlsqsl snsfnssyms sdnesdiede dlklelrrlr dkhlkeiqdl qsrqkheies
     2101 lytklgkvpp aviippaapl sgrrrrptks kgskssrsss lgnkspqlsg nlsgqsaasv
     2161 lhpqqtlhpp gnipesgqnq llqplkpsps sdnlysafts dgaisvpsls apgqgtsstn
     2221 tvgatvnsqa aqaqppamts srkgtftddl hklvdnward amnlsgrrgs kghmnyegpg
     2281 markfsapgq lcismtsnlg gsapisaasa tslghftksm cppqqygfpa tpfgaqwsgt
     2341 ggpapqplgq fqpvgtaslq nfnisnlqks isnppgsnlr tt
//
LOCUS       NP_001431734            1441 aa            linear   PRI 29-DEC-2025
DEFINITION  uncharacterized protein C1orf167 isoform 2 [Homo sapiens].
ACCESSION   NP_001431734
VERSION     NP_001431734.1
DBSOURCE    REFSEQ: accession NM_001444805.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1441)
  AUTHORS   Mo,X.B., Lei,S.F., Zhang,Y.H. and Zhang,H.
  TITLE     Examination of the associations between m6A-associated
            single-nucleotide polymorphisms and blood pressure
  JOURNAL   Hypertens Res 42 (10), 1582-1589 (2019)
   PUBMED   31175347
REFERENCE   2  (residues 1 to 1441)
  AUTHORS   Genno,P.G., Nemer,G.M., Zein Eddine,S.B., Macari,A.T. and
            Ghafari,J.G.
  TITLE     Three novel genes tied to mandibular prognathism in eastern
            Mediterranean families
  JOURNAL   Am J Orthod Dentofacial Orthop 156 (1), 104-112 (2019)
   PUBMED   31256822
REFERENCE   3  (residues 1 to 1441)
  AUTHORS   van Meurs,J.B., Pare,G., Schwartz,S.M., Hazra,A., Tanaka,T.,
            Vermeulen,S.H., Cotlarciuc,I., Yuan,X., Malarstig,A.,
            Bandinelli,S., Bis,J.C., Blom,H., Brown,M.J., Chen,C., Chen,Y.D.,
            Clarke,R.J., Dehghan,A., Erdmann,J., Ferrucci,L., Hamsten,A.,
            Hofman,A., Hunter,D.J., Goel,A., Johnson,A.D., Kathiresan,S.,
            Kampman,E., Kiel,D.P., Kiemeney,L.A., Chambers,J.C., Kraft,P.,
            Lindemans,J., McKnight,B., Nelson,C.P., O'Donnell,C.J., Psaty,B.M.,
            Ridker,P.M., Rivadeneira,F., Rose,L.M., Seedorf,U., Siscovick,D.S.,
            Schunkert,H., Selhub,J., Ueland,P.M., Vollenweider,P., Waeber,G.,
            Waterworth,D.M., Watkins,H., Witteman,J.C., den Heijer,M.,
            Jacques,P., Uitterlinden,A.G., Kooner,J.S., Rader,D.J.,
            Reilly,M.P., Mooser,V., Chasman,D.I., Samani,N.J. and Ahmadi,K.R.
  TITLE     Common genetic loci influencing plasma homocysteine concentrations
            and their effect on risk of coronary artery disease
  JOURNAL   Am J Clin Nutr 98 (3), 668-676 (2013)
   PUBMED   23824729
REFERENCE   4  (residues 1 to 1441)
  AUTHORS   Ban,H.J., Heo,J.Y., Oh,K.S. and Park,K.J.
  TITLE     Identification of type 2 diabetes-associated combination of SNPs
            using support vector machine
  JOURNAL   BMC Genet 11, 26 (2010)
   PUBMED   20416077
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1441)
  AUTHORS   Matarin,M., Brown,W.M., Dena,H., Britton,A., De Vrieze,F.W.,
            Brott,T.G., Brown,R.D. Jr., Worrall,B.B., Case,L.D., Chanock,S.J.,
            Metter,E.J., Ferrucci,L., Gamble,D., Hardy,J.A., Rich,S.S.,
            Singleton,A. and Meschia,J.F.
  TITLE     Candidate gene polymorphisms for ischemic stroke
  JOURNAL   Stroke 40 (11), 3436-3442 (2009)
   PUBMED   19729601
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 1441)
  AUTHORS   Tran,P., Leclerc,D., Chan,M., Pai,A., Hiou-Tim,F., Wu,Q.,
            Goyette,P., Artigas,C., Milos,R. and Rozen,R.
  TITLE     Multiple transcription start sites and alternative splicing in the
            methylenetetrahydrofolate reductase gene result in two enzyme
            isoforms
  JOURNAL   Mamm Genome 13 (9), 483-492 (2002)
   PUBMED   12370778
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL953897.6.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3640303.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1441
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..1441
                     /product="uncharacterized protein C1orf167 isoform 2"
                     /note="uncharacterized protein C1orf167"
                     /calculated_mol_wt=160599
     Region          936..1406
                     /region_name="DUF4684"
                     /note="Domain of unknown function (DUF4684); pfam15736"
                     /db_xref="CDD:464833"
     CDS             1..1441
                     /gene="C1orf167"
                     /coded_by="NM_001444805.1:184..4509"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:284498"
                     /db_xref="HGNC:HGNC:25262"
ORIGIN      
        1 melrsdashk envspkpaal pkpeqrrfrr slgiglsgrh dqwvpgcqve rggpaatpsp
       61 gavldqepcr vqtnlaspgp rlglalkdtt gqlvnssfwq qsnlqslarr rqgkarefai
      121 qqsnlsinet ssphlcpepg gssgphklpw gpllsqepla rpssclrqsg lpapgtpsgd
      181 frpteafapl dghtqpglrs wgglgswrsr lvgepltled lavpsqnqtq apsraavhql
      241 lasvhclaqe aarlrcqapq eppgavqqdl wtgggqpfsa hpqpsqpvla ssdgrrrrlr
      301 ghretaafle tpaslsdswa qsklmspett lgtrtkdsln peqglppahp lgsgdscspw
      361 sqdgraqrgd pslprgvgsr gtdpcssafs ntawgvspkq kgeegaprer vhreeertaf
      421 hlsdtvpass asknkaqnit apeseaicwq llsrcfrswr hlvkrqrepa aaavalgrwq
      481 llrkclqalw lreaqleaaw gqytkvllvr sfrewrnlal qqkqvqphmq agpgsppsrr
      541 aqgkglslgr stvvdpaqrs rlehtrqrtd srhervqilq alqlavfflw cqqkkrarqe
      601 retlrkatra tqrtgsfpqa whstaagvaw vaplspqhqr awlcrcfgaw qqfvqrgsry
      661 rdhladrrtg tlrkcleqwv rmkqlresdg akvtqlslcr qkagreavyt agpgacglga
      721 vgqaqgqqeq grgslqdacw tlalcwalll wkmrlfqrqw ansffqglqq rmlqrslrww
      781 hlralgpdat ssctktpsal eplssstlqd slekvprapt lpdtlqgsll waagqrqqgq
      841 clllwqaraq qfqgtarwyq htrqrrifls wsrwataqwa wrelashraw drtcravlgl
      901 wrqrllqsrl vewwaqergw rlardalchw hscwqgqqfl hekcqtwvqv hlqglqkvvf
      961 rswqqaaahq rctvtrpeql llqsyfqawc evvrdtgvlr aqhqafqdgl rrralgavfa
     1021 twreaqevaa gaqeqrvaqa slarwrscgq qgqedgqqkk arapqafpaw pvapgmhhea
     1081 qqqagesaga qaaqcwtwcw alwvhescrg qvsrahaswk prawvleasv qsavrggvqr
     1141 ailtqlrpae lrrflrtvql rvrlglpgag ktrscwtqat elvppapslq cslggrrkpr
     1201 gtawaqrcre hslcpafqlw pqwpgqsswv pglplwtrdq gprahsspep rackaqskah
     1261 krrlrrkylq rrcleallhg lrgsqqarcl avawqhwvda qgaeqlvrtl mtppchspft
     1321 lvqqcrgrka eglgtagere hkrpslptvp kaqgvapemg ladvvaadpa tasgsavtaa
     1381 grwafkkwhq rlaarsprrg aassprpwsk pgpkgpesgq eaaraprgwg lgaehgaqlq
     1441 l
//
LOCUS       NP_001010881            1449 aa            linear   PRI 29-DEC-2025
DEFINITION  uncharacterized protein C1orf167 isoform 1 [Homo sapiens].
ACCESSION   NP_001010881
VERSION     NP_001010881.1
DBSOURCE    REFSEQ: accession NM_001010881.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1449)
  AUTHORS   Mo,X.B., Lei,S.F., Zhang,Y.H. and Zhang,H.
  TITLE     Examination of the associations between m6A-associated
            single-nucleotide polymorphisms and blood pressure
  JOURNAL   Hypertens Res 42 (10), 1582-1589 (2019)
   PUBMED   31175347
REFERENCE   2  (residues 1 to 1449)
  AUTHORS   Genno,P.G., Nemer,G.M., Zein Eddine,S.B., Macari,A.T. and
            Ghafari,J.G.
  TITLE     Three novel genes tied to mandibular prognathism in eastern
            Mediterranean families
  JOURNAL   Am J Orthod Dentofacial Orthop 156 (1), 104-112 (2019)
   PUBMED   31256822
REFERENCE   3  (residues 1 to 1449)
  AUTHORS   van Meurs,J.B., Pare,G., Schwartz,S.M., Hazra,A., Tanaka,T.,
            Vermeulen,S.H., Cotlarciuc,I., Yuan,X., Malarstig,A.,
            Bandinelli,S., Bis,J.C., Blom,H., Brown,M.J., Chen,C., Chen,Y.D.,
            Clarke,R.J., Dehghan,A., Erdmann,J., Ferrucci,L., Hamsten,A.,
            Hofman,A., Hunter,D.J., Goel,A., Johnson,A.D., Kathiresan,S.,
            Kampman,E., Kiel,D.P., Kiemeney,L.A., Chambers,J.C., Kraft,P.,
            Lindemans,J., McKnight,B., Nelson,C.P., O'Donnell,C.J., Psaty,B.M.,
            Ridker,P.M., Rivadeneira,F., Rose,L.M., Seedorf,U., Siscovick,D.S.,
            Schunkert,H., Selhub,J., Ueland,P.M., Vollenweider,P., Waeber,G.,
            Waterworth,D.M., Watkins,H., Witteman,J.C., den Heijer,M.,
            Jacques,P., Uitterlinden,A.G., Kooner,J.S., Rader,D.J.,
            Reilly,M.P., Mooser,V., Chasman,D.I., Samani,N.J. and Ahmadi,K.R.
  TITLE     Common genetic loci influencing plasma homocysteine concentrations
            and their effect on risk of coronary artery disease
  JOURNAL   Am J Clin Nutr 98 (3), 668-676 (2013)
   PUBMED   23824729
REFERENCE   4  (residues 1 to 1449)
  AUTHORS   Ban,H.J., Heo,J.Y., Oh,K.S. and Park,K.J.
  TITLE     Identification of type 2 diabetes-associated combination of SNPs
            using support vector machine
  JOURNAL   BMC Genet 11, 26 (2010)
   PUBMED   20416077
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1449)
  AUTHORS   Matarin,M., Brown,W.M., Dena,H., Britton,A., De Vrieze,F.W.,
            Brott,T.G., Brown,R.D. Jr., Worrall,B.B., Case,L.D., Chanock,S.J.,
            Metter,E.J., Ferrucci,L., Gamble,D., Hardy,J.A., Rich,S.S.,
            Singleton,A. and Meschia,J.F.
  TITLE     Candidate gene polymorphisms for ischemic stroke
  JOURNAL   Stroke 40 (11), 3436-3442 (2009)
   PUBMED   19729601
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 1449)
  AUTHORS   Tran,P., Leclerc,D., Chan,M., Pai,A., Hiou-Tim,F., Wu,Q.,
            Goyette,P., Artigas,C., Milos,R. and Rozen,R.
  TITLE     Multiple transcription start sites and alternative splicing in the
            methylenetetrahydrofolate reductase gene result in two enzyme
            isoforms
  JOURNAL   Mamm Genome 13 (9), 483-492 (2002)
   PUBMED   12370778
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY031308.1, HY056181.1, BC128091.1, AL953897.6, AL833920.1,
            AL834308.1, AL833926.1 and AF398935.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000688073.1/ ENSP00000510540.1
            RefSeq Select criteria    :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1449
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..1449
                     /product="uncharacterized protein C1orf167 isoform 1"
                     /note="uncharacterized protein C1orf167"
                     /calculated_mol_wt=160351
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNV9.3)"
     Region          123..201
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNV9.3)"
     Region          258..298
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNV9.3)"
     Region          315..437
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNV9.3)"
     Region          523..551
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNV9.3)"
     Region          954..1414
                     /region_name="DUF4684"
                     /note="Domain of unknown function (DUF4684); pfam15736"
                     /db_xref="CDD:464833"
     Region          1257..1278
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNV9.3)"
     Region          1399..1449
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SNV9.3)"
     CDS             1..1449
                     /gene="C1orf167"
                     /coded_by="NM_001010881.2:184..4533"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS90862.1"
                     /db_xref="GeneID:284498"
                     /db_xref="HGNC:HGNC:25262"
ORIGIN      
        1 melrsdashk envspkpaal pkpeqrrfrr slgiglsgrh dqwvpgcqve rggpaatpsp
       61 gavldqepcr vqtnlaspgp rlglalkdtt gqlvnssfwq qsnlqslarr rqgkarefai
      121 qqsnlsinet ssphlcpepg gssgphklpw gpllsqepla rpssclrqsg lpapgtpsgd
      181 frpteafapl dghtqpglrs wgglgswrsr lvgepltled lavpsqnqtq apsraavhql
      241 lasvhclaqe aarlrcqapq eppgavqqdl wtgggqpfsa hpqpsqpvla ssdgrrrrlr
      301 ghretaafle tpaslsdswa qsklmspett lgtrtkdsln peqglppahp lgsgdscspw
      361 sqdgraqrgd pslprgvgsr gtdpcssafs ntawgvspkq kgeegaprer vhreeertaf
      421 hlsdtvpass asknkaqnit apeseaicwq llsrcfrswr hlvkrqrepa aaavalgrwq
      481 llrkclqalw lreaqleaaw gqytkvllvr sfrewrnlal qqkqvqphmq agpgsppsrr
      541 aqgkglslgr stvvdpaqrs rlehtspgsl reeeiaqrll shprqrtdsr hervqilqal
      601 qlavfflwcq qkkrarqere tlrkatratq rtgsfpqawh staagvawva plspqhqraw
      661 lcrcfgawqq fvqrgsryrd hladrrtgtl rkcleqwvrm kqlresdgak vtqlslcrqk
      721 agreavytag pgacglgavg qaqgqqeqgr gslqdacwtl alcwalllwk mrlfqrqwan
      781 sffqglqqrm lqrslrwwhl ralgpdatss ctktpsalep lssstlqdsl ekvpraptlp
      841 dtlqgsllwa agqrqqgqcl llwqaraqqf qgtarwyqht rqrriflsws rwataqwawr
      901 elashrawdr tcravlglwr qrllqsrlve wwaqergwrl ardalchwhs cwqgqqflhe
      961 kcqtwvqvhl qglqkvvfrs wqqaaahqrc tvtrpeqlll qsyfqawcev vrdtgvlraq
     1021 hqafqdglrr ralgavfatw reaqevaaga qeqrvaqasl arwrscgqqg qedgqqkkar
     1081 apqafpawpv apgmhheaqq qagesagaqa aqcwtwcwal wvhescrgqv srahaswkpr
     1141 awvleasvqs avrggvqrai ltqlrpaelr rflrtvqlrv rlglpgagkt rscwtqatel
     1201 vppapslqcs lggrrkprgt awaqrcrehs lcpafqlwpq wpgqsswvpg lplwtrdqgp
     1261 rahsspepra ckaqskahkr rlrarscril ekqaqahgsa lllalkghda lghqeevpaa
     1321 pvprgtasra agfpagqvpg sgmaalggcp rgraagadpa qgvapemgla dvvaadpata
     1381 sgsavtaagr wafkkwhqrl aarsprrgaa ssprpwskpg pkgpesgqea araprgwglg
     1441 aehgaqlql
//
LOCUS       NP_002849                659 aa            linear   PRI 31-DEC-2025
DEFINITION  ATP-binding cassette sub-family D member 3 isoform a [Homo
            sapiens].
ACCESSION   NP_002849
VERSION     NP_002849.1
DBSOURCE    REFSEQ: accession NM_002858.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Tawbeh,A., Gondcaille,C., Trompier,D. and Savary,S.
  TITLE     Peroxisomal ABC Transporters: An Update
  JOURNAL   Int J Mol Sci 22 (11), 6093 (2021)
   PUBMED   34198763
  REMARK    GeneRIF: Peroxisomal ABC Transporters: An Update.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Violante,S., Achetib,N., van Roermund,C.W.T., Hagen,J., Dodatko,T.,
            Vaz,F.M., Waterham,H.R., Chen,H., Baes,M., Yu,C., Argmann,C.A. and
            Houten,S.M.
  TITLE     Peroxisomes can oxidize medium- and long-chain fatty acids through
            a pathway involving ABCD3 and HSD17B4
  JOURNAL   FASEB J 33 (3), 4355-4364 (2019)
   PUBMED   30540494
  REMARK    GeneRIF: In HEK293 cells, the D-bifunctional protein (HSD17B4) and
            the peroxisomal ABC transporter ABCD3 are essential in peroxisomal
            oxidation of lauric and palmitic acid.
REFERENCE   4  (residues 1 to 659)
  AUTHORS   Okamoto,T., Kawaguchi,K., Watanabe,S., Agustina,R., Ikejima,T.,
            Ikeda,K., Nakano,M., Morita,M. and Imanaka,T.
  TITLE     Characterization of human ATP-binding cassette protein subfamily D
            reconstituted into proteoliposomes
  JOURNAL   Biochem Biophys Res Commun 496 (4), 1122-1127 (2018)
   PUBMED   29397936
REFERENCE   5  (residues 1 to 659)
  AUTHORS   Kawaguchi,K. and Morita,M.
  TITLE     ABC Transporter Subfamily D: Distinct Differences in Behavior
            between ABCD1-3 and ABCD4 in Subcellular Localization, Function,
            and Human Disease
  JOURNAL   Biomed Res Int 2016, 6786245 (2016)
   PUBMED   27766264
  REMARK    GeneRIF: ABCD1 and ABCD2 are involved in the transport of long and
            very long chain fatty acids (VLCFA) or their CoA-derivatives into
            peroxisomes with different substrate specificities, while ABCD3 is
            involved in the transport of branched chain acyl-CoA into
            peroxisomes.ABCD4 is deduced to take part in the transport of
            vitamin B12 from lysosomes into the cytosol.
            Review article
REFERENCE   6  (residues 1 to 659)
  AUTHORS   Gartner,J. and Valle,D.
  TITLE     The 70 kDa peroxisomal membrane protein: an ATP-binding cassette
            transporter protein involved in peroxisome biogenesis
  JOURNAL   Semin Cell Biol 4 (1), 45-52 (1993)
   PUBMED   8453064
  REMARK    Review article
REFERENCE   7  (residues 1 to 659)
  AUTHORS   Gartner,J., Kearns,W., Rosenberg,C., Pearson,P., Copeland,N.G.,
            Gilbert,D.J., Jenkins,N.A. and Valle,D.
  TITLE     Localization of the 70-kDa peroxisomal membrane protein to human
            1p21-p22 and mouse 3
  JOURNAL   Genomics 15 (2), 412-414 (1993)
   PUBMED   8449508
REFERENCE   8  (residues 1 to 659)
  AUTHORS   Gartner,J., Obie,C., Moser,H. and Valle,D.
  TITLE     A polymorphic synonymous mutation (K54K) in the human 70 kD
            peroxisomal membrane protein gene (PMP1)
  JOURNAL   Hum Mol Genet 1 (8), 654 (1992)
   PUBMED   1301179
REFERENCE   9  (residues 1 to 659)
  AUTHORS   Gartner,J., Moser,H. and Valle,D.
  TITLE     Mutations in the 70K peroxisomal membrane protein gene in Zellweger
            syndrome
  JOURNAL   Nat Genet 1 (1), 16-23 (1992)
   PUBMED   1301993
REFERENCE   10 (residues 1 to 659)
  AUTHORS   Kamijo,K., Kamijo,T., Ueno,I., Osumi,T. and Hashimoto,T.
  TITLE     Nucleotide sequence of the human 70 kDa peroxisomal membrane
            protein: a member of ATP-binding cassette transporters
  JOURNAL   Biochim Biophys Acta 1129 (3), 323-327 (1992)
   PUBMED   1536884
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC317792.1, M81182.1 and
            BC068509.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. This
            peroxisomal membrane protein likely plays an important role in
            peroxisome biogenesis. Mutations have been associated with some
            forms of Zellweger syndrome, a heterogeneous group of peroxisome
            assembly disorders. Alternative splicing results in multiple
            transcript variants encoding distinct isoforms. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.189353.1,
                                           SRR1660809.189092.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370214.9/ ENSP00000359233.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p21.3"
     Protein         1..659
                     /product="ATP-binding cassette sub-family D member 3
                     isoform a"
                     /note="Peroxisomal membrane protein-1 (70kD); peroxisomal
                     membrane protein 1 (70kD, Zellweger syndrome); ATP-binding
                     cassette sub-family D member 3; dJ824O18.1 (ATP-binding
                     cassette, sub-family D (ALD), member 3 (PMP70, PXMP1)); 70
                     kDa peroxisomal membrane protein; peroxisomal membrane
                     protein 70 kDa"
                     /calculated_mol_wt=75345
     Region          1..647
                     /region_name="3a01203"
                     /note="Peroxysomal Fatty Acyl CoA Transporter (FAT) Family
                     protein; TIGR00954"
                     /db_xref="CDD:273360"
     Region          1..61
                     /region_name="Interaction with PEX19.
                     /evidence=ECO:0000269|PubMed:16344115,
                     ECO:0000269|PubMed:17761678"
                     /note="propagated from UniProtKB/Swiss-Prot (P28288.1)"
     Site            12
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28288.1)"
     Site            61
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P55096; propagated from
                     UniProtKB/Swiss-Prot (P28288.1)"
     Site            84..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28288.1)"
     Site            106
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28288.1)"
     Site            126..146
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28288.1)"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28288.1)"
     Site            224..244
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28288.1)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P28288.1)"
     Site            313..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28288.1)"
     Site            399
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P28288.1)"
     Site            533
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P55096; propagated from
                     UniProtKB/Swiss-Prot (P28288.1)"
     Site            659
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P55096; propagated from
                     UniProtKB/Swiss-Prot (P28288.1)"
     CDS             1..659
                     /gene="ABCD3"
                     /gene_synonym="ABC43; CBAS5; OPDM5; PMP70; PXMP1; ZWS2"
                     /coded_by="NM_002858.4:91..2070"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS749.1"
                     /db_xref="GeneID:5825"
                     /db_xref="HGNC:HGNC:67"
                     /db_xref="MIM:170995"
ORIGIN      
        1 maafskylta rnsslagaaf lllcllhkrr ralglhgkks gkpplqnnek egkkeravvd
       61 kvffsrliqi lkimvprtfc ketgylvlia vmlvsrtycd vwmiqngtli esgiigrsrk
      121 dfkryllnfi aamplislvn nflkyglnel klcfrvrltk ylyeeylqaf tyykmgnldn
      181 rianpdqllt qdvekfcnsv vdlysnlskp fldivlyifk ltsaigaqgp asmmaylvvs
      241 glfltrlrrp igkmtiteqk yegeyryvns rlitnseeia fyngnkrekq tvhsvfrklv
      301 ehlhnfilfr fsmgfidsii akylatvvgy lvvsrpfldl shprhlksth selledyyqs
      361 grmllrmsqa lgrivlagre mtrlagftar itelmqvlkd lnhgkyertm vsqqekgieg
      421 vqviplipga geiiiadnii kfdhvplatp ngdvlirdln fevrsganvl icgpngcgks
      481 slfrvlgelw plfggrltkp ergklfyvpq rpymtlgtlr dqviypdgre dqkrkgisdl
      541 vlkeyldnvq lghileregg wdsvqdwmdv lsggekqrma marlfyhkpq faildectsa
      601 vsvdvegyiy shcrkvgitl ftvshrkslw khheyylhmd grgnyefkqi tedtvefgs
//
LOCUS       NP_001116146             236 aa            linear   PRI 31-DEC-2025
DEFINITION  ATP-binding cassette sub-family D member 3 isoform b [Homo
            sapiens].
ACCESSION   NP_001116146
VERSION     NP_001116146.1
DBSOURCE    REFSEQ: accession NM_001122674.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Tawbeh,A., Gondcaille,C., Trompier,D. and Savary,S.
  TITLE     Peroxisomal ABC Transporters: An Update
  JOURNAL   Int J Mol Sci 22 (11), 6093 (2021)
   PUBMED   34198763
  REMARK    GeneRIF: Peroxisomal ABC Transporters: An Update.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Violante,S., Achetib,N., van Roermund,C.W.T., Hagen,J., Dodatko,T.,
            Vaz,F.M., Waterham,H.R., Chen,H., Baes,M., Yu,C., Argmann,C.A. and
            Houten,S.M.
  TITLE     Peroxisomes can oxidize medium- and long-chain fatty acids through
            a pathway involving ABCD3 and HSD17B4
  JOURNAL   FASEB J 33 (3), 4355-4364 (2019)
   PUBMED   30540494
  REMARK    GeneRIF: In HEK293 cells, the D-bifunctional protein (HSD17B4) and
            the peroxisomal ABC transporter ABCD3 are essential in peroxisomal
            oxidation of lauric and palmitic acid.
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Okamoto,T., Kawaguchi,K., Watanabe,S., Agustina,R., Ikejima,T.,
            Ikeda,K., Nakano,M., Morita,M. and Imanaka,T.
  TITLE     Characterization of human ATP-binding cassette protein subfamily D
            reconstituted into proteoliposomes
  JOURNAL   Biochem Biophys Res Commun 496 (4), 1122-1127 (2018)
   PUBMED   29397936
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Kawaguchi,K. and Morita,M.
  TITLE     ABC Transporter Subfamily D: Distinct Differences in Behavior
            between ABCD1-3 and ABCD4 in Subcellular Localization, Function,
            and Human Disease
  JOURNAL   Biomed Res Int 2016, 6786245 (2016)
   PUBMED   27766264
  REMARK    GeneRIF: ABCD1 and ABCD2 are involved in the transport of long and
            very long chain fatty acids (VLCFA) or their CoA-derivatives into
            peroxisomes with different substrate specificities, while ABCD3 is
            involved in the transport of branched chain acyl-CoA into
            peroxisomes.ABCD4 is deduced to take part in the transport of
            vitamin B12 from lysosomes into the cytosol.
            Review article
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Gartner,J. and Valle,D.
  TITLE     The 70 kDa peroxisomal membrane protein: an ATP-binding cassette
            transporter protein involved in peroxisome biogenesis
  JOURNAL   Semin Cell Biol 4 (1), 45-52 (1993)
   PUBMED   8453064
  REMARK    Review article
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Gartner,J., Kearns,W., Rosenberg,C., Pearson,P., Copeland,N.G.,
            Gilbert,D.J., Jenkins,N.A. and Valle,D.
  TITLE     Localization of the 70-kDa peroxisomal membrane protein to human
            1p21-p22 and mouse 3
  JOURNAL   Genomics 15 (2), 412-414 (1993)
   PUBMED   8449508
REFERENCE   8  (residues 1 to 236)
  AUTHORS   Gartner,J., Obie,C., Moser,H. and Valle,D.
  TITLE     A polymorphic synonymous mutation (K54K) in the human 70 kD
            peroxisomal membrane protein gene (PMP1)
  JOURNAL   Hum Mol Genet 1 (8), 654 (1992)
   PUBMED   1301179
REFERENCE   9  (residues 1 to 236)
  AUTHORS   Gartner,J., Moser,H. and Valle,D.
  TITLE     Mutations in the 70K peroxisomal membrane protein gene in Zellweger
            syndrome
  JOURNAL   Nat Genet 1 (1), 16-23 (1992)
   PUBMED   1301993
REFERENCE   10 (residues 1 to 236)
  AUTHORS   Kamijo,K., Kamijo,T., Ueno,I., Osumi,T. and Hashimoto,T.
  TITLE     Nucleotide sequence of the human 70 kDa peroxisomal membrane
            protein: a member of ATP-binding cassette transporters
  JOURNAL   Biochim Biophys Acta 1129 (3), 323-327 (1992)
   PUBMED   1536884
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC317792.1, BC009712.2 and
            AC118469.2.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. This
            peroxisomal membrane protein likely plays an important role in
            peroxisome biogenesis. Mutations have been associated with some
            forms of Zellweger syndrome, a heterogeneous group of peroxisome
            assembly disorders. Alternative splicing results in multiple
            transcript variants encoding distinct isoforms. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) has multiple differences in
            the 3' coding region and 3' UTR and contains an alternate exon in
            the central coding region, compared to variant 1, that results in a
            protein (isoform b) with a shorter, distinct C-terminus when
            compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC009712.2, BT006644.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p21.3"
     Protein         1..236
                     /product="ATP-binding cassette sub-family D member 3
                     isoform b"
                     /note="Peroxisomal membrane protein-1 (70kD); peroxisomal
                     membrane protein 1 (70kD, Zellweger syndrome); ATP-binding
                     cassette sub-family D member 3; dJ824O18.1 (ATP-binding
                     cassette, sub-family D (ALD), member 3 (PMP70, PXMP1)); 70
                     kDa peroxisomal membrane protein; peroxisomal membrane
                     protein 70 kDa"
                     /calculated_mol_wt=26990
     Region          1..>234
                     /region_name="3a01203"
                     /note="Peroxysomal Fatty Acyl CoA Transporter (FAT) Family
                     protein; TIGR00954"
                     /db_xref="CDD:273360"
     Region          1..61
                     /region_name="Interaction with PEX19.
                     /evidence=ECO:0000269|PubMed:16344115,
                     ECO:0000269|PubMed:17761678"
                     /note="propagated from UniProtKB/Swiss-Prot (P28288.1)"
     Site            12
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28288.1)"
     Site            61
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P55096; propagated from
                     UniProtKB/Swiss-Prot (P28288.1)"
     Site            84..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28288.1)"
     Site            106
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28288.1)"
     Site            126..146
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P28288.1)"
     Site            206
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P28288.1)"
     CDS             1..236
                     /gene="ABCD3"
                     /gene_synonym="ABC43; CBAS5; OPDM5; PMP70; PXMP1; ZWS2"
                     /coded_by="NM_001122674.2:91..801"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44175.1"
                     /db_xref="GeneID:5825"
                     /db_xref="HGNC:HGNC:67"
                     /db_xref="MIM:170995"
ORIGIN      
        1 maafskylta rnsslagaaf lllcllhkrr ralglhgkks gkpplqnnek egkkeravvd
       61 kvffsrliqi lkimvprtfc ketgylvlia vmlvsrtycd vwmiqngtli esgiigrsrk
      121 dfkryllnfi aamplislvn nflkyglnel klcfrvrltk ylyeeylqaf tyykmgnldn
      181 rianpdqllt qdvekfcnsv vdlysnlskp fldivlyifk ltsaigaqvl gkilwh
//
LOCUS       NP_001425507             301 aa            linear   PRI 01-JAN-2026
DEFINITION  heterogeneous nuclear ribonucleoproteins A2/B1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001425507 XP_047276262 XP_054214042
VERSION     NP_001425507.1
DBSOURCE    REFSEQ: accession NM_001438578.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Zhang,X., Yan,L.-n., Liu,B.-y., Zhou,C.-m. and Yu,X.-j.
  TITLE     The hnRNP A2B1 is important for the replication of SFTSV and other
            RNA viruses
  JOURNAL   Microbiol Spectr 12 (10), e0082924 (2024)
   PUBMED   39166862
  REMARK    GeneRIF: The hnRNP A2B1 is important for the replication of SFTSV
            and other RNA viruses.
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Huang,T., Zhu,G. and Chen,F.
  TITLE     The Potential Impact of HNRNPA2B1 on Human Cancers Prognosis and
            Immune Microenvironment
  JOURNAL   J Immunol Res 2024, 5515307 (2024)
   PUBMED   39268079
  REMARK    GeneRIF: The Potential Impact of HNRNPA2B1 on Human Cancers
            Prognosis and Immune Microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Jin,T., Yang,L., Chang,C., Luo,H., Wang,R., Gan,Y., Sun,Y., Guo,Y.,
            Tang,R., Chen,S., Meng,D., Dai,P. and Liu,M.
  TITLE     HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective Export via
            ALYREF/NXF1 Complex to Foster Breast Cancer Development
  JOURNAL   Adv Sci (Weinh) 11 (24), e2307639 (2024)
   PUBMED   38626369
  REMARK    GeneRIF: HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective
            Export via ALYREF/NXF1 Complex to Foster Breast Cancer Development.
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Yang,Y., Zhang,Y., Feng,T. and Zhu,C.
  TITLE     HNRNPA2B1 induces cell proliferation and acts as biomarker in
            breast cancer
  JOURNAL   Cancer Biomark 40 (3-4), 285-296 (2024)
   PUBMED   39177591
  REMARK    GeneRIF: HNRNPA2B1 induces cell proliferation and acts as biomarker
            in breast cancer.
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Wilk,H.E., Schaefer,K.P., Agris,P.F., Boak,A.M. and Kovacs,S.A.
  TITLE     U1 SnRNP association with HnRNP involves an initial non-specific
            splice-site independent interaction of U1 SnRNP protein with HnRNA
  JOURNAL   Mol Cell Biochem 106 (1), 55-66 (1991)
   PUBMED   1833625
REFERENCE   8  (residues 1 to 301)
  AUTHORS   Bauw,G., Rasmussen,H.H., van den Bulcke,M., van Damme,J., Puype,M.,
            Gesser,B., Celis,J.E. and Vandekerckhove,J.
  TITLE     Two-dimensional gel electrophoresis, protein electroblotting and
            microsequencing: a direct link between proteins and genes
  JOURNAL   Electrophoresis 11 (7), 528-536 (1990)
   PUBMED   1699755
REFERENCE   9  (residues 1 to 301)
  AUTHORS   Burd,C.G., Swanson,M.S., Gorlach,M. and Dreyfuss,G.
  TITLE     Primary structures of the heterogeneous nuclear ribonucleoprotein
            A2, B1, and C2 proteins: a diversity of RNA binding proteins is
            generated by small peptide inserts
  JOURNAL   Proc Natl Acad Sci U S A 86 (24), 9788-9792 (1989)
   PUBMED   2557628
REFERENCE   10 (residues 1 to 301)
  AUTHORS   Kumar,A., Williams,K.R. and Szer,W.
  TITLE     Purification and domain structure of core hnRNP proteins A1 and A2
            and their relationship to single-stranded DNA-binding proteins
  JOURNAL   J Biol Chem 261 (24), 11266-11273 (1986)
   PUBMED   3733753
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010677.4 and AC004520.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047276262.1, XP_054214042.1.
            
            Summary: This gene belongs to the A/B subfamily of ubiquitously
            expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The
            hnRNPs are RNA binding proteins and they complex with heterogeneous
            nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs
            in the nucleus and appear to influence pre-mRNA processing and
            other aspects of mRNA metabolism and transport. While all of the
            hnRNPs are present in the nucleus, some seem to shuttle between the
            nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic
            acid binding properties. The protein encoded by this gene has two
            repeats of quasi-RRM domains that bind to RNAs. This gene has been
            described to generate two alternatively spliced transcript variants
            which encode different isoforms. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.26859.1,
                                           SRR14038197.109374.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.2"
     Protein         1..301
                     /product="heterogeneous nuclear ribonucleoproteins A2/B1
                     isoform 4"
                     /note="nuclear ribonucleoprotein particle A2 protein;
                     heterogeneous nuclear ribonucleoproteins A2/B1; hnRNP A2 /
                     hnRNP B1; HNRNPA2B1/MYC fusion; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=32356
     Region          7..87
                     /region_name="RRM1_hnRNPA2B1"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12762"
                     /db_xref="CDD:410155"
     Site            order(10,12,14..15,37,39,41,50..52,54,77,80,82..87)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410155"
     Region          100..179
                     /region_name="RRM2_hnRNPA2B1"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12581"
                     /db_xref="CDD:409995"
     Region          248..274
                     /region_name="HnRNPA1"
                     /note="Nuclear factor hnRNPA1; pfam11627"
                     /db_xref="CDD:463312"
     CDS             1..301
                     /gene="HNRNPA2B1"
                     /gene_synonym="HNRNPA2; HNRNPB1; HNRPA2; HNRPA2B1; HNRPB1;
                     IBMPFD2; OPDM2; OPMD2; RNPA2; SNRPB1"
                     /coded_by="NM_001438578.1:170..1075"
                     /note="isoform 4 is encoded by transcript variant 14"
                     /db_xref="GeneID:3181"
                     /db_xref="HGNC:HGNC:5033"
                     /db_xref="MIM:600124"
ORIGIN      
        1 merekeqfrk lfigglsfet teeslrnyye qwgkltdcvv mrdpaskrsr gfgfvtfssm
       61 aevdaamaar phsidgrvve pkravarees gkpgahvtvk klfvggiked teehhlrdyf
      121 eeygkidtie iitdrqsgkk rgfgfvtfdd hdpvdkivlq kyhtinghna evrkalsrqe
      181 mqevqssrsg rggnfgfgds rggggnfgpg pgsnfrggsd gygsgrgfgd gyngygggpg
      241 gnygsgnynd fgnynqqpsn ygpmksgnfg gsrnmggpyg ggnygpggsg gsggyggrsr
      301 y
//
LOCUS       NP_001424992             341 aa            linear   PRI 01-JAN-2026
DEFINITION  heterogeneous nuclear ribonucleoproteins A2/B1 isoform A2 [Homo
            sapiens].
ACCESSION   NP_001424992 XP_016867598 XP_054214034
VERSION     NP_001424992.1
DBSOURCE    REFSEQ: accession NM_001438063.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Zhang,X., Yan,L.-n., Liu,B.-y., Zhou,C.-m. and Yu,X.-j.
  TITLE     The hnRNP A2B1 is important for the replication of SFTSV and other
            RNA viruses
  JOURNAL   Microbiol Spectr 12 (10), e0082924 (2024)
   PUBMED   39166862
  REMARK    GeneRIF: The hnRNP A2B1 is important for the replication of SFTSV
            and other RNA viruses.
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Huang,T., Zhu,G. and Chen,F.
  TITLE     The Potential Impact of HNRNPA2B1 on Human Cancers Prognosis and
            Immune Microenvironment
  JOURNAL   J Immunol Res 2024, 5515307 (2024)
   PUBMED   39268079
  REMARK    GeneRIF: The Potential Impact of HNRNPA2B1 on Human Cancers
            Prognosis and Immune Microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Jin,T., Yang,L., Chang,C., Luo,H., Wang,R., Gan,Y., Sun,Y., Guo,Y.,
            Tang,R., Chen,S., Meng,D., Dai,P. and Liu,M.
  TITLE     HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective Export via
            ALYREF/NXF1 Complex to Foster Breast Cancer Development
  JOURNAL   Adv Sci (Weinh) 11 (24), e2307639 (2024)
   PUBMED   38626369
  REMARK    GeneRIF: HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective
            Export via ALYREF/NXF1 Complex to Foster Breast Cancer Development.
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Yang,Y., Zhang,Y., Feng,T. and Zhu,C.
  TITLE     HNRNPA2B1 induces cell proliferation and acts as biomarker in
            breast cancer
  JOURNAL   Cancer Biomark 40 (3-4), 285-296 (2024)
   PUBMED   39177591
  REMARK    GeneRIF: HNRNPA2B1 induces cell proliferation and acts as biomarker
            in breast cancer.
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Wilk,H.E., Schaefer,K.P., Agris,P.F., Boak,A.M. and Kovacs,S.A.
  TITLE     U1 SnRNP association with HnRNP involves an initial non-specific
            splice-site independent interaction of U1 SnRNP protein with HnRNA
  JOURNAL   Mol Cell Biochem 106 (1), 55-66 (1991)
   PUBMED   1833625
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Bauw,G., Rasmussen,H.H., van den Bulcke,M., van Damme,J., Puype,M.,
            Gesser,B., Celis,J.E. and Vandekerckhove,J.
  TITLE     Two-dimensional gel electrophoresis, protein electroblotting and
            microsequencing: a direct link between proteins and genes
  JOURNAL   Electrophoresis 11 (7), 528-536 (1990)
   PUBMED   1699755
REFERENCE   9  (residues 1 to 341)
  AUTHORS   Burd,C.G., Swanson,M.S., Gorlach,M. and Dreyfuss,G.
  TITLE     Primary structures of the heterogeneous nuclear ribonucleoprotein
            A2, B1, and C2 proteins: a diversity of RNA binding proteins is
            generated by small peptide inserts
  JOURNAL   Proc Natl Acad Sci U S A 86 (24), 9788-9792 (1989)
   PUBMED   2557628
REFERENCE   10 (residues 1 to 341)
  AUTHORS   Kumar,A., Williams,K.R. and Szer,W.
  TITLE     Purification and domain structure of core hnRNP proteins A1 and A2
            and their relationship to single-stranded DNA-binding proteins
  JOURNAL   J Biol Chem 261 (24), 11266-11273 (1986)
   PUBMED   3733753
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010677.4 and AC004520.2.
            
            On or before Apr 15, 2025 this sequence version replaced
            XP_016867598.1, XP_054214034.1.
            
            Summary: This gene belongs to the A/B subfamily of ubiquitously
            expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The
            hnRNPs are RNA binding proteins and they complex with heterogeneous
            nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs
            in the nucleus and appear to influence pre-mRNA processing and
            other aspects of mRNA metabolism and transport. While all of the
            hnRNPs are present in the nucleus, some seem to shuttle between the
            nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic
            acid binding properties. The protein encoded by this gene has two
            repeats of quasi-RRM domains that bind to RNAs. This gene has been
            described to generate two alternatively spliced transcript variants
            which encode different isoforms. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1274050.1,
                                           SRR14038191.2417213.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.2"
     Protein         1..341
                     /product="heterogeneous nuclear ribonucleoproteins A2/B1
                     isoform A2"
                     /note="nuclear ribonucleoprotein particle A2 protein;
                     heterogeneous nuclear ribonucleoproteins A2/B1; hnRNP A2 /
                     hnRNP B1; HNRNPA2B1/MYC fusion; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=35875
     Region          7..87
                     /region_name="RRM1_hnRNPA2B1"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12762"
                     /db_xref="CDD:410155"
     Site            order(10,12,14..15,37,39,41,50..52,54,77,80,82..87)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410155"
     Region          100..179
                     /region_name="RRM2_hnRNPA2B1"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12581"
                     /db_xref="CDD:409995"
     Region          290..314
                     /region_name="HnRNPA1"
                     /note="Nuclear factor hnRNPA1; pfam11627"
                     /db_xref="CDD:463312"
     CDS             1..341
                     /gene="HNRNPA2B1"
                     /gene_synonym="HNRNPA2; HNRNPB1; HNRPA2; HNRPA2B1; HNRPB1;
                     IBMPFD2; OPDM2; OPMD2; RNPA2; SNRPB1"
                     /coded_by="NM_001438063.1:170..1195"
                     /note="isoform A2 is encoded by transcript variant 3"
                     /db_xref="GeneID:3181"
                     /db_xref="HGNC:HGNC:5033"
                     /db_xref="MIM:600124"
ORIGIN      
        1 merekeqfrk lfigglsfet teeslrnyye qwgkltdcvv mrdpaskrsr gfgfvtfssm
       61 aevdaamaar phsidgrvve pkravarees gkpgahvtvk klfvggiked teehhlrdyf
      121 eeygkidtie iitdrqsgkk rgfgfvtfdd hdpvdkivlq kyhtinghna evrkalsrqe
      181 mqevqssrsg rggnfgfgds rggggnfgpg pgsnfrggsd gygsgrgfgd gyngygggpg
      241 ggnfggspgy gggrggyggg gpgygnqggg ygggydnygg gnygsgnynd fgnynqqpsn
      301 ygpmksgnfg gsrnmggpyg ggnygpggsg gsggyggrsr y
//
LOCUS       NP_001425497             353 aa            linear   PRI 01-JAN-2026
DEFINITION  heterogeneous nuclear ribonucleoproteins A2/B1 isoform B1 [Homo
            sapiens].
ACCESSION   NP_001425497 XP_005249786 XP_054214033
VERSION     NP_001425497.1
DBSOURCE    REFSEQ: accession NM_001438568.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Zhang,X., Yan,L.-n., Liu,B.-y., Zhou,C.-m. and Yu,X.-j.
  TITLE     The hnRNP A2B1 is important for the replication of SFTSV and other
            RNA viruses
  JOURNAL   Microbiol Spectr 12 (10), e0082924 (2024)
   PUBMED   39166862
  REMARK    GeneRIF: The hnRNP A2B1 is important for the replication of SFTSV
            and other RNA viruses.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Huang,T., Zhu,G. and Chen,F.
  TITLE     The Potential Impact of HNRNPA2B1 on Human Cancers Prognosis and
            Immune Microenvironment
  JOURNAL   J Immunol Res 2024, 5515307 (2024)
   PUBMED   39268079
  REMARK    GeneRIF: The Potential Impact of HNRNPA2B1 on Human Cancers
            Prognosis and Immune Microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Jin,T., Yang,L., Chang,C., Luo,H., Wang,R., Gan,Y., Sun,Y., Guo,Y.,
            Tang,R., Chen,S., Meng,D., Dai,P. and Liu,M.
  TITLE     HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective Export via
            ALYREF/NXF1 Complex to Foster Breast Cancer Development
  JOURNAL   Adv Sci (Weinh) 11 (24), e2307639 (2024)
   PUBMED   38626369
  REMARK    GeneRIF: HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective
            Export via ALYREF/NXF1 Complex to Foster Breast Cancer Development.
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Yang,Y., Zhang,Y., Feng,T. and Zhu,C.
  TITLE     HNRNPA2B1 induces cell proliferation and acts as biomarker in
            breast cancer
  JOURNAL   Cancer Biomark 40 (3-4), 285-296 (2024)
   PUBMED   39177591
  REMARK    GeneRIF: HNRNPA2B1 induces cell proliferation and acts as biomarker
            in breast cancer.
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Wilk,H.E., Schaefer,K.P., Agris,P.F., Boak,A.M. and Kovacs,S.A.
  TITLE     U1 SnRNP association with HnRNP involves an initial non-specific
            splice-site independent interaction of U1 SnRNP protein with HnRNA
  JOURNAL   Mol Cell Biochem 106 (1), 55-66 (1991)
   PUBMED   1833625
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Bauw,G., Rasmussen,H.H., van den Bulcke,M., van Damme,J., Puype,M.,
            Gesser,B., Celis,J.E. and Vandekerckhove,J.
  TITLE     Two-dimensional gel electrophoresis, protein electroblotting and
            microsequencing: a direct link between proteins and genes
  JOURNAL   Electrophoresis 11 (7), 528-536 (1990)
   PUBMED   1699755
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Burd,C.G., Swanson,M.S., Gorlach,M. and Dreyfuss,G.
  TITLE     Primary structures of the heterogeneous nuclear ribonucleoprotein
            A2, B1, and C2 proteins: a diversity of RNA binding proteins is
            generated by small peptide inserts
  JOURNAL   Proc Natl Acad Sci U S A 86 (24), 9788-9792 (1989)
   PUBMED   2557628
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Kumar,A., Williams,K.R. and Szer,W.
  TITLE     Purification and domain structure of core hnRNP proteins A1 and A2
            and their relationship to single-stranded DNA-binding proteins
  JOURNAL   J Biol Chem 261 (24), 11266-11273 (1986)
   PUBMED   3733753
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010677.4 and AC004520.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_005249786.1, XP_054214033.1.
            
            Summary: This gene belongs to the A/B subfamily of ubiquitously
            expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The
            hnRNPs are RNA binding proteins and they complex with heterogeneous
            nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs
            in the nucleus and appear to influence pre-mRNA processing and
            other aspects of mRNA metabolism and transport. While all of the
            hnRNPs are present in the nucleus, some seem to shuttle between the
            nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic
            acid binding properties. The protein encoded by this gene has two
            repeats of quasi-RRM domains that bind to RNAs. This gene has been
            described to generate two alternatively spliced transcript variants
            which encode different isoforms. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1493120.1,
                                           SRR14038193.2365498.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.2"
     Protein         1..353
                     /product="heterogeneous nuclear ribonucleoproteins A2/B1
                     isoform B1"
                     /note="nuclear ribonucleoprotein particle A2 protein;
                     heterogeneous nuclear ribonucleoproteins A2/B1; hnRNP A2 /
                     hnRNP B1; HNRNPA2B1/MYC fusion; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=37299
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Region          9..15
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Region          19..99
                     /region_name="RRM1_hnRNPA2B1"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12762"
                     /db_xref="CDD:410155"
     Site            order(22,24,26..27,49,51,53,62..64,66,89,92,94..99)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410155"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            38
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            104
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|Ref.6; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Region          112..191
                     /region_name="RRM2_hnRNPA2B1"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12581"
                     /db_xref="CDD:409995"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            168
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            173
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Region          193..353
                     /region_name="Disordered.
                     /evidence=ECO:0000269|PubMed:26544936"
                     /note="propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            203
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O88569; Dimethylated
                     arginine, alternate. /evidence=ECO:0000269|Ref.6;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|Ref.6, ECO:0007744|PubMed:15782174,
                     ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            213
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O88569; Dimethylated
                     arginine, alternate. /evidence=ECO:0000269|Ref.6;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|Ref.6, ECO:0007744|PubMed:24129315;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            228
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000269|PubMed:31320558,
                     ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            238
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            266
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:A7VJC2;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Region          302..326
                     /region_name="HnRNPA1"
                     /note="Nuclear factor hnRNPA1; pfam11627"
                     /db_xref="CDD:463312"
     Region          308..347
                     /region_name="Nuclear targeting sequence.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            325
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            350
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     CDS             1..353
                     /gene="HNRNPA2B1"
                     /gene_synonym="HNRNPA2; HNRNPB1; HNRPA2; HNRPA2B1; HNRPB1;
                     IBMPFD2; OPDM2; OPMD2; RNPA2; SNRPB1"
                     /coded_by="NM_001438568.1:170..1231"
                     /note="isoform B1 is encoded by transcript variant 4"
                     /db_xref="GeneID:3181"
                     /db_xref="HGNC:HGNC:5033"
                     /db_xref="MIM:600124"
ORIGIN      
        1 mektletvpl erkkrekeqf rklfigglsf etteeslrny yeqwgkltdc vvmrdpaskr
       61 srgfgfvtfs smaevdaama arphsidgrv vepkravare esgkpgahvt vkklfvggik
      121 edteehhlrd yfeeygkidt ieiitdrqsg kkrgfgfvtf ddhdpvdkiv lqkyhtingh
      181 naevrkalsr qemqevqssr sgrggnfgfg dsrggggnfg pgpgsnfrgg sdgygsgrgf
      241 gdgyngyggg pgggnfggsp gygggrggyg gggpgygnqg ggygggydny gggnygsgny
      301 ndfgnynqqp snygpmksgn fggsrnmggp ygggnygpgg sggsggyggr sry
//
LOCUS       NP_001425500             341 aa            linear   PRI 01-JAN-2026
DEFINITION  heterogeneous nuclear ribonucleoproteins A2/B1 isoform A2 [Homo
            sapiens].
ACCESSION   NP_001425500 XP_016867599 XP_054214036
VERSION     NP_001425500.1
DBSOURCE    REFSEQ: accession NM_001438571.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Zhang,X., Yan,L.-n., Liu,B.-y., Zhou,C.-m. and Yu,X.-j.
  TITLE     The hnRNP A2B1 is important for the replication of SFTSV and other
            RNA viruses
  JOURNAL   Microbiol Spectr 12 (10), e0082924 (2024)
   PUBMED   39166862
  REMARK    GeneRIF: The hnRNP A2B1 is important for the replication of SFTSV
            and other RNA viruses.
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Huang,T., Zhu,G. and Chen,F.
  TITLE     The Potential Impact of HNRNPA2B1 on Human Cancers Prognosis and
            Immune Microenvironment
  JOURNAL   J Immunol Res 2024, 5515307 (2024)
   PUBMED   39268079
  REMARK    GeneRIF: The Potential Impact of HNRNPA2B1 on Human Cancers
            Prognosis and Immune Microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Jin,T., Yang,L., Chang,C., Luo,H., Wang,R., Gan,Y., Sun,Y., Guo,Y.,
            Tang,R., Chen,S., Meng,D., Dai,P. and Liu,M.
  TITLE     HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective Export via
            ALYREF/NXF1 Complex to Foster Breast Cancer Development
  JOURNAL   Adv Sci (Weinh) 11 (24), e2307639 (2024)
   PUBMED   38626369
  REMARK    GeneRIF: HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective
            Export via ALYREF/NXF1 Complex to Foster Breast Cancer Development.
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Yang,Y., Zhang,Y., Feng,T. and Zhu,C.
  TITLE     HNRNPA2B1 induces cell proliferation and acts as biomarker in
            breast cancer
  JOURNAL   Cancer Biomark 40 (3-4), 285-296 (2024)
   PUBMED   39177591
  REMARK    GeneRIF: HNRNPA2B1 induces cell proliferation and acts as biomarker
            in breast cancer.
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Wilk,H.E., Schaefer,K.P., Agris,P.F., Boak,A.M. and Kovacs,S.A.
  TITLE     U1 SnRNP association with HnRNP involves an initial non-specific
            splice-site independent interaction of U1 SnRNP protein with HnRNA
  JOURNAL   Mol Cell Biochem 106 (1), 55-66 (1991)
   PUBMED   1833625
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Bauw,G., Rasmussen,H.H., van den Bulcke,M., van Damme,J., Puype,M.,
            Gesser,B., Celis,J.E. and Vandekerckhove,J.
  TITLE     Two-dimensional gel electrophoresis, protein electroblotting and
            microsequencing: a direct link between proteins and genes
  JOURNAL   Electrophoresis 11 (7), 528-536 (1990)
   PUBMED   1699755
REFERENCE   9  (residues 1 to 341)
  AUTHORS   Burd,C.G., Swanson,M.S., Gorlach,M. and Dreyfuss,G.
  TITLE     Primary structures of the heterogeneous nuclear ribonucleoprotein
            A2, B1, and C2 proteins: a diversity of RNA binding proteins is
            generated by small peptide inserts
  JOURNAL   Proc Natl Acad Sci U S A 86 (24), 9788-9792 (1989)
   PUBMED   2557628
REFERENCE   10 (residues 1 to 341)
  AUTHORS   Kumar,A., Williams,K.R. and Szer,W.
  TITLE     Purification and domain structure of core hnRNP proteins A1 and A2
            and their relationship to single-stranded DNA-binding proteins
  JOURNAL   J Biol Chem 261 (24), 11266-11273 (1986)
   PUBMED   3733753
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010677.4 and AC004520.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_016867599.1, XP_054214036.1.
            
            Summary: This gene belongs to the A/B subfamily of ubiquitously
            expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The
            hnRNPs are RNA binding proteins and they complex with heterogeneous
            nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs
            in the nucleus and appear to influence pre-mRNA processing and
            other aspects of mRNA metabolism and transport. While all of the
            hnRNPs are present in the nucleus, some seem to shuttle between the
            nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic
            acid binding properties. The protein encoded by this gene has two
            repeats of quasi-RRM domains that bind to RNAs. This gene has been
            described to generate two alternatively spliced transcript variants
            which encode different isoforms. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.116751.1,
                                           SRR14038196.509698.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.2"
     Protein         1..341
                     /product="heterogeneous nuclear ribonucleoproteins A2/B1
                     isoform A2"
                     /note="nuclear ribonucleoprotein particle A2 protein;
                     heterogeneous nuclear ribonucleoproteins A2/B1; hnRNP A2 /
                     hnRNP B1; HNRNPA2B1/MYC fusion; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=35875
     Region          7..87
                     /region_name="RRM1_hnRNPA2B1"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12762"
                     /db_xref="CDD:410155"
     Site            order(10,12,14..15,37,39,41,50..52,54,77,80,82..87)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410155"
     Region          100..179
                     /region_name="RRM2_hnRNPA2B1"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12581"
                     /db_xref="CDD:409995"
     Region          290..314
                     /region_name="HnRNPA1"
                     /note="Nuclear factor hnRNPA1; pfam11627"
                     /db_xref="CDD:463312"
     CDS             1..341
                     /gene="HNRNPA2B1"
                     /gene_synonym="HNRNPA2; HNRNPB1; HNRPA2; HNRPA2B1; HNRPB1;
                     IBMPFD2; OPDM2; OPMD2; RNPA2; SNRPB1"
                     /coded_by="NM_001438571.1:170..1195"
                     /note="isoform A2 is encoded by transcript variant 7"
                     /db_xref="GeneID:3181"
                     /db_xref="HGNC:HGNC:5033"
                     /db_xref="MIM:600124"
ORIGIN      
        1 merekeqfrk lfigglsfet teeslrnyye qwgkltdcvv mrdpaskrsr gfgfvtfssm
       61 aevdaamaar phsidgrvve pkravarees gkpgahvtvk klfvggiked teehhlrdyf
      121 eeygkidtie iitdrqsgkk rgfgfvtfdd hdpvdkivlq kyhtinghna evrkalsrqe
      181 mqevqssrsg rggnfgfgds rggggnfgpg pgsnfrggsd gygsgrgfgd gyngygggpg
      241 ggnfggspgy gggrggyggg gpgygnqggg ygggydnygg gnygsgnynd fgnynqqpsn
      301 ygpmksgnfg gsrnmggpyg ggnygpggsg gsggyggrsr y
//
LOCUS       NP_001425506             301 aa            linear   PRI 01-JAN-2026
DEFINITION  heterogeneous nuclear ribonucleoproteins A2/B1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001425506 XP_047276259 XP_054214039
VERSION     NP_001425506.1
DBSOURCE    REFSEQ: accession NM_001438577.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Zhang,X., Yan,L.-n., Liu,B.-y., Zhou,C.-m. and Yu,X.-j.
  TITLE     The hnRNP A2B1 is important for the replication of SFTSV and other
            RNA viruses
  JOURNAL   Microbiol Spectr 12 (10), e0082924 (2024)
   PUBMED   39166862
  REMARK    GeneRIF: The hnRNP A2B1 is important for the replication of SFTSV
            and other RNA viruses.
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Huang,T., Zhu,G. and Chen,F.
  TITLE     The Potential Impact of HNRNPA2B1 on Human Cancers Prognosis and
            Immune Microenvironment
  JOURNAL   J Immunol Res 2024, 5515307 (2024)
   PUBMED   39268079
  REMARK    GeneRIF: The Potential Impact of HNRNPA2B1 on Human Cancers
            Prognosis and Immune Microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Jin,T., Yang,L., Chang,C., Luo,H., Wang,R., Gan,Y., Sun,Y., Guo,Y.,
            Tang,R., Chen,S., Meng,D., Dai,P. and Liu,M.
  TITLE     HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective Export via
            ALYREF/NXF1 Complex to Foster Breast Cancer Development
  JOURNAL   Adv Sci (Weinh) 11 (24), e2307639 (2024)
   PUBMED   38626369
  REMARK    GeneRIF: HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective
            Export via ALYREF/NXF1 Complex to Foster Breast Cancer Development.
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Yang,Y., Zhang,Y., Feng,T. and Zhu,C.
  TITLE     HNRNPA2B1 induces cell proliferation and acts as biomarker in
            breast cancer
  JOURNAL   Cancer Biomark 40 (3-4), 285-296 (2024)
   PUBMED   39177591
  REMARK    GeneRIF: HNRNPA2B1 induces cell proliferation and acts as biomarker
            in breast cancer.
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Wilk,H.E., Schaefer,K.P., Agris,P.F., Boak,A.M. and Kovacs,S.A.
  TITLE     U1 SnRNP association with HnRNP involves an initial non-specific
            splice-site independent interaction of U1 SnRNP protein with HnRNA
  JOURNAL   Mol Cell Biochem 106 (1), 55-66 (1991)
   PUBMED   1833625
REFERENCE   8  (residues 1 to 301)
  AUTHORS   Bauw,G., Rasmussen,H.H., van den Bulcke,M., van Damme,J., Puype,M.,
            Gesser,B., Celis,J.E. and Vandekerckhove,J.
  TITLE     Two-dimensional gel electrophoresis, protein electroblotting and
            microsequencing: a direct link between proteins and genes
  JOURNAL   Electrophoresis 11 (7), 528-536 (1990)
   PUBMED   1699755
REFERENCE   9  (residues 1 to 301)
  AUTHORS   Burd,C.G., Swanson,M.S., Gorlach,M. and Dreyfuss,G.
  TITLE     Primary structures of the heterogeneous nuclear ribonucleoprotein
            A2, B1, and C2 proteins: a diversity of RNA binding proteins is
            generated by small peptide inserts
  JOURNAL   Proc Natl Acad Sci U S A 86 (24), 9788-9792 (1989)
   PUBMED   2557628
REFERENCE   10 (residues 1 to 301)
  AUTHORS   Kumar,A., Williams,K.R. and Szer,W.
  TITLE     Purification and domain structure of core hnRNP proteins A1 and A2
            and their relationship to single-stranded DNA-binding proteins
  JOURNAL   J Biol Chem 261 (24), 11266-11273 (1986)
   PUBMED   3733753
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010677.4 and AC004520.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047276259.1, XP_054214039.1.
            
            Summary: This gene belongs to the A/B subfamily of ubiquitously
            expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The
            hnRNPs are RNA binding proteins and they complex with heterogeneous
            nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs
            in the nucleus and appear to influence pre-mRNA processing and
            other aspects of mRNA metabolism and transport. While all of the
            hnRNPs are present in the nucleus, some seem to shuttle between the
            nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic
            acid binding properties. The protein encoded by this gene has two
            repeats of quasi-RRM domains that bind to RNAs. This gene has been
            described to generate two alternatively spliced transcript variants
            which encode different isoforms. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1142657.1,
                                           SRR18074969.1782091.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.2"
     Protein         1..301
                     /product="heterogeneous nuclear ribonucleoproteins A2/B1
                     isoform 4"
                     /note="nuclear ribonucleoprotein particle A2 protein;
                     heterogeneous nuclear ribonucleoproteins A2/B1; hnRNP A2 /
                     hnRNP B1; HNRNPA2B1/MYC fusion; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=32356
     Region          7..87
                     /region_name="RRM1_hnRNPA2B1"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12762"
                     /db_xref="CDD:410155"
     Site            order(10,12,14..15,37,39,41,50..52,54,77,80,82..87)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410155"
     Region          100..179
                     /region_name="RRM2_hnRNPA2B1"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12581"
                     /db_xref="CDD:409995"
     Region          248..274
                     /region_name="HnRNPA1"
                     /note="Nuclear factor hnRNPA1; pfam11627"
                     /db_xref="CDD:463312"
     CDS             1..301
                     /gene="HNRNPA2B1"
                     /gene_synonym="HNRNPA2; HNRNPB1; HNRPA2; HNRPA2B1; HNRPB1;
                     IBMPFD2; OPDM2; OPMD2; RNPA2; SNRPB1"
                     /coded_by="NM_001438577.1:170..1075"
                     /note="isoform 4 is encoded by transcript variant 13"
                     /db_xref="GeneID:3181"
                     /db_xref="HGNC:HGNC:5033"
                     /db_xref="MIM:600124"
ORIGIN      
        1 merekeqfrk lfigglsfet teeslrnyye qwgkltdcvv mrdpaskrsr gfgfvtfssm
       61 aevdaamaar phsidgrvve pkravarees gkpgahvtvk klfvggiked teehhlrdyf
      121 eeygkidtie iitdrqsgkk rgfgfvtfdd hdpvdkivlq kyhtinghna evrkalsrqe
      181 mqevqssrsg rggnfgfgds rggggnfgpg pgsnfrggsd gygsgrgfgd gyngygggpg
      241 gnygsgnynd fgnynqqpsn ygpmksgnfg gsrnmggpyg ggnygpggsg gsggyggrsr
      301 y
//
LOCUS       NP_001425503             313 aa            linear   PRI 01-JAN-2026
DEFINITION  heterogeneous nuclear ribonucleoproteins A2/B1 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001425503 XP_047276258 XP_054214038
VERSION     NP_001425503.1
DBSOURCE    REFSEQ: accession NM_001438574.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Zhang,X., Yan,L.-n., Liu,B.-y., Zhou,C.-m. and Yu,X.-j.
  TITLE     The hnRNP A2B1 is important for the replication of SFTSV and other
            RNA viruses
  JOURNAL   Microbiol Spectr 12 (10), e0082924 (2024)
   PUBMED   39166862
  REMARK    GeneRIF: The hnRNP A2B1 is important for the replication of SFTSV
            and other RNA viruses.
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Huang,T., Zhu,G. and Chen,F.
  TITLE     The Potential Impact of HNRNPA2B1 on Human Cancers Prognosis and
            Immune Microenvironment
  JOURNAL   J Immunol Res 2024, 5515307 (2024)
   PUBMED   39268079
  REMARK    GeneRIF: The Potential Impact of HNRNPA2B1 on Human Cancers
            Prognosis and Immune Microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Jin,T., Yang,L., Chang,C., Luo,H., Wang,R., Gan,Y., Sun,Y., Guo,Y.,
            Tang,R., Chen,S., Meng,D., Dai,P. and Liu,M.
  TITLE     HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective Export via
            ALYREF/NXF1 Complex to Foster Breast Cancer Development
  JOURNAL   Adv Sci (Weinh) 11 (24), e2307639 (2024)
   PUBMED   38626369
  REMARK    GeneRIF: HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective
            Export via ALYREF/NXF1 Complex to Foster Breast Cancer Development.
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Yang,Y., Zhang,Y., Feng,T. and Zhu,C.
  TITLE     HNRNPA2B1 induces cell proliferation and acts as biomarker in
            breast cancer
  JOURNAL   Cancer Biomark 40 (3-4), 285-296 (2024)
   PUBMED   39177591
  REMARK    GeneRIF: HNRNPA2B1 induces cell proliferation and acts as biomarker
            in breast cancer.
REFERENCE   6  (residues 1 to 313)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 313)
  AUTHORS   Wilk,H.E., Schaefer,K.P., Agris,P.F., Boak,A.M. and Kovacs,S.A.
  TITLE     U1 SnRNP association with HnRNP involves an initial non-specific
            splice-site independent interaction of U1 SnRNP protein with HnRNA
  JOURNAL   Mol Cell Biochem 106 (1), 55-66 (1991)
   PUBMED   1833625
REFERENCE   8  (residues 1 to 313)
  AUTHORS   Bauw,G., Rasmussen,H.H., van den Bulcke,M., van Damme,J., Puype,M.,
            Gesser,B., Celis,J.E. and Vandekerckhove,J.
  TITLE     Two-dimensional gel electrophoresis, protein electroblotting and
            microsequencing: a direct link between proteins and genes
  JOURNAL   Electrophoresis 11 (7), 528-536 (1990)
   PUBMED   1699755
REFERENCE   9  (residues 1 to 313)
  AUTHORS   Burd,C.G., Swanson,M.S., Gorlach,M. and Dreyfuss,G.
  TITLE     Primary structures of the heterogeneous nuclear ribonucleoprotein
            A2, B1, and C2 proteins: a diversity of RNA binding proteins is
            generated by small peptide inserts
  JOURNAL   Proc Natl Acad Sci U S A 86 (24), 9788-9792 (1989)
   PUBMED   2557628
REFERENCE   10 (residues 1 to 313)
  AUTHORS   Kumar,A., Williams,K.R. and Szer,W.
  TITLE     Purification and domain structure of core hnRNP proteins A1 and A2
            and their relationship to single-stranded DNA-binding proteins
  JOURNAL   J Biol Chem 261 (24), 11266-11273 (1986)
   PUBMED   3733753
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010677.4 and AC004520.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047276258.1, XP_054214038.1.
            
            Summary: This gene belongs to the A/B subfamily of ubiquitously
            expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The
            hnRNPs are RNA binding proteins and they complex with heterogeneous
            nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs
            in the nucleus and appear to influence pre-mRNA processing and
            other aspects of mRNA metabolism and transport. While all of the
            hnRNPs are present in the nucleus, some seem to shuttle between the
            nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic
            acid binding properties. The protein encoded by this gene has two
            repeats of quasi-RRM domains that bind to RNAs. This gene has been
            described to generate two alternatively spliced transcript variants
            which encode different isoforms. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1360566.1,
                                           SRR14243140.1906210.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.2"
     Protein         1..313
                     /product="heterogeneous nuclear ribonucleoproteins A2/B1
                     isoform 3"
                     /note="nuclear ribonucleoprotein particle A2 protein;
                     heterogeneous nuclear ribonucleoproteins A2/B1; hnRNP A2 /
                     hnRNP B1; HNRNPA2B1/MYC fusion; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=33780
     Region          19..99
                     /region_name="RRM1_hnRNPA2B1"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12762"
                     /db_xref="CDD:410155"
     Site            order(22,24,26..27,49,51,53,62..64,66,89,92,94..99)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410155"
     Region          112..191
                     /region_name="RRM2_hnRNPA2B1"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12581"
                     /db_xref="CDD:409995"
     Region          260..286
                     /region_name="HnRNPA1"
                     /note="Nuclear factor hnRNPA1; pfam11627"
                     /db_xref="CDD:463312"
     CDS             1..313
                     /gene="HNRNPA2B1"
                     /gene_synonym="HNRNPA2; HNRNPB1; HNRPA2; HNRPA2B1; HNRPB1;
                     IBMPFD2; OPDM2; OPMD2; RNPA2; SNRPB1"
                     /coded_by="NM_001438574.1:170..1111"
                     /note="isoform 3 is encoded by transcript variant 10"
                     /db_xref="GeneID:3181"
                     /db_xref="HGNC:HGNC:5033"
                     /db_xref="MIM:600124"
ORIGIN      
        1 mektletvpl erkkrekeqf rklfigglsf etteeslrny yeqwgkltdc vvmrdpaskr
       61 srgfgfvtfs smaevdaama arphsidgrv vepkravare esgkpgahvt vkklfvggik
      121 edteehhlrd yfeeygkidt ieiitdrqsg kkrgfgfvtf ddhdpvdkiv lqkyhtingh
      181 naevrkalsr qemqevqssr sgrggnfgfg dsrggggnfg pgpgsnfrgg sdgygsgrgf
      241 gdgyngyggg pggnygsgny ndfgnynqqp snygpmksgn fggsrnmggp ygggnygpgg
      301 sggsggyggr sry
//
LOCUS       NP_001425498             353 aa            linear   PRI 01-JAN-2026
DEFINITION  heterogeneous nuclear ribonucleoproteins A2/B1 isoform B1 [Homo
            sapiens].
ACCESSION   NP_001425498 XP_047276254 XP_054214031
VERSION     NP_001425498.1
DBSOURCE    REFSEQ: accession NM_001438569.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Zhang,X., Yan,L.-n., Liu,B.-y., Zhou,C.-m. and Yu,X.-j.
  TITLE     The hnRNP A2B1 is important for the replication of SFTSV and other
            RNA viruses
  JOURNAL   Microbiol Spectr 12 (10), e0082924 (2024)
   PUBMED   39166862
  REMARK    GeneRIF: The hnRNP A2B1 is important for the replication of SFTSV
            and other RNA viruses.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Huang,T., Zhu,G. and Chen,F.
  TITLE     The Potential Impact of HNRNPA2B1 on Human Cancers Prognosis and
            Immune Microenvironment
  JOURNAL   J Immunol Res 2024, 5515307 (2024)
   PUBMED   39268079
  REMARK    GeneRIF: The Potential Impact of HNRNPA2B1 on Human Cancers
            Prognosis and Immune Microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Jin,T., Yang,L., Chang,C., Luo,H., Wang,R., Gan,Y., Sun,Y., Guo,Y.,
            Tang,R., Chen,S., Meng,D., Dai,P. and Liu,M.
  TITLE     HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective Export via
            ALYREF/NXF1 Complex to Foster Breast Cancer Development
  JOURNAL   Adv Sci (Weinh) 11 (24), e2307639 (2024)
   PUBMED   38626369
  REMARK    GeneRIF: HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective
            Export via ALYREF/NXF1 Complex to Foster Breast Cancer Development.
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Yang,Y., Zhang,Y., Feng,T. and Zhu,C.
  TITLE     HNRNPA2B1 induces cell proliferation and acts as biomarker in
            breast cancer
  JOURNAL   Cancer Biomark 40 (3-4), 285-296 (2024)
   PUBMED   39177591
  REMARK    GeneRIF: HNRNPA2B1 induces cell proliferation and acts as biomarker
            in breast cancer.
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Wilk,H.E., Schaefer,K.P., Agris,P.F., Boak,A.M. and Kovacs,S.A.
  TITLE     U1 SnRNP association with HnRNP involves an initial non-specific
            splice-site independent interaction of U1 SnRNP protein with HnRNA
  JOURNAL   Mol Cell Biochem 106 (1), 55-66 (1991)
   PUBMED   1833625
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Bauw,G., Rasmussen,H.H., van den Bulcke,M., van Damme,J., Puype,M.,
            Gesser,B., Celis,J.E. and Vandekerckhove,J.
  TITLE     Two-dimensional gel electrophoresis, protein electroblotting and
            microsequencing: a direct link between proteins and genes
  JOURNAL   Electrophoresis 11 (7), 528-536 (1990)
   PUBMED   1699755
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Burd,C.G., Swanson,M.S., Gorlach,M. and Dreyfuss,G.
  TITLE     Primary structures of the heterogeneous nuclear ribonucleoprotein
            A2, B1, and C2 proteins: a diversity of RNA binding proteins is
            generated by small peptide inserts
  JOURNAL   Proc Natl Acad Sci U S A 86 (24), 9788-9792 (1989)
   PUBMED   2557628
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Kumar,A., Williams,K.R. and Szer,W.
  TITLE     Purification and domain structure of core hnRNP proteins A1 and A2
            and their relationship to single-stranded DNA-binding proteins
  JOURNAL   J Biol Chem 261 (24), 11266-11273 (1986)
   PUBMED   3733753
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010677.4 and AC004520.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047276254.1, XP_054214031.1.
            
            Summary: This gene belongs to the A/B subfamily of ubiquitously
            expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The
            hnRNPs are RNA binding proteins and they complex with heterogeneous
            nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs
            in the nucleus and appear to influence pre-mRNA processing and
            other aspects of mRNA metabolism and transport. While all of the
            hnRNPs are present in the nucleus, some seem to shuttle between the
            nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic
            acid binding properties. The protein encoded by this gene has two
            repeats of quasi-RRM domains that bind to RNAs. This gene has been
            described to generate two alternatively spliced transcript variants
            which encode different isoforms. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1268708.1,
                                           SRR14038191.3670673.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.2"
     Protein         1..353
                     /product="heterogeneous nuclear ribonucleoproteins A2/B1
                     isoform B1"
                     /note="nuclear ribonucleoprotein particle A2 protein;
                     heterogeneous nuclear ribonucleoproteins A2/B1; hnRNP A2 /
                     hnRNP B1; HNRNPA2B1/MYC fusion; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=37299
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Region          9..15
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Region          19..99
                     /region_name="RRM1_hnRNPA2B1"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12762"
                     /db_xref="CDD:410155"
     Site            order(22,24,26..27,49,51,53,62..64,66,89,92,94..99)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410155"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            38
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            104
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|Ref.6; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Region          112..191
                     /region_name="RRM2_hnRNPA2B1"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12581"
                     /db_xref="CDD:409995"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            168
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            173
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Region          193..353
                     /region_name="Disordered.
                     /evidence=ECO:0000269|PubMed:26544936"
                     /note="propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            203
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O88569; Dimethylated
                     arginine, alternate. /evidence=ECO:0000269|Ref.6;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|Ref.6, ECO:0007744|PubMed:15782174,
                     ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            213
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O88569; Dimethylated
                     arginine, alternate. /evidence=ECO:0000269|Ref.6;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|Ref.6, ECO:0007744|PubMed:24129315;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            228
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000269|PubMed:31320558,
                     ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            238
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            266
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:A7VJC2;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Region          302..326
                     /region_name="HnRNPA1"
                     /note="Nuclear factor hnRNPA1; pfam11627"
                     /db_xref="CDD:463312"
     Region          308..347
                     /region_name="Nuclear targeting sequence.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            325
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            350
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     CDS             1..353
                     /gene="HNRNPA2B1"
                     /gene_synonym="HNRNPA2; HNRNPB1; HNRPA2; HNRPA2B1; HNRPB1;
                     IBMPFD2; OPDM2; OPMD2; RNPA2; SNRPB1"
                     /coded_by="NM_001438569.1:170..1231"
                     /note="isoform B1 is encoded by transcript variant 5"
                     /db_xref="GeneID:3181"
                     /db_xref="HGNC:HGNC:5033"
                     /db_xref="MIM:600124"
ORIGIN      
        1 mektletvpl erkkrekeqf rklfigglsf etteeslrny yeqwgkltdc vvmrdpaskr
       61 srgfgfvtfs smaevdaama arphsidgrv vepkravare esgkpgahvt vkklfvggik
      121 edteehhlrd yfeeygkidt ieiitdrqsg kkrgfgfvtf ddhdpvdkiv lqkyhtingh
      181 naevrkalsr qemqevqssr sgrggnfgfg dsrggggnfg pgpgsnfrgg sdgygsgrgf
      241 gdgyngyggg pgggnfggsp gygggrggyg gggpgygnqg ggygggydny gggnygsgny
      301 ndfgnynqqp snygpmksgn fggsrnmggp ygggnygpgg sggsggyggr sry
//
LOCUS       NP_001425504             301 aa            linear   PRI 01-JAN-2026
DEFINITION  heterogeneous nuclear ribonucleoproteins A2/B1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001425504 XP_047276260 XP_054214040
VERSION     NP_001425504.1
DBSOURCE    REFSEQ: accession NM_001438575.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Zhang,X., Yan,L.-n., Liu,B.-y., Zhou,C.-m. and Yu,X.-j.
  TITLE     The hnRNP A2B1 is important for the replication of SFTSV and other
            RNA viruses
  JOURNAL   Microbiol Spectr 12 (10), e0082924 (2024)
   PUBMED   39166862
  REMARK    GeneRIF: The hnRNP A2B1 is important for the replication of SFTSV
            and other RNA viruses.
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Huang,T., Zhu,G. and Chen,F.
  TITLE     The Potential Impact of HNRNPA2B1 on Human Cancers Prognosis and
            Immune Microenvironment
  JOURNAL   J Immunol Res 2024, 5515307 (2024)
   PUBMED   39268079
  REMARK    GeneRIF: The Potential Impact of HNRNPA2B1 on Human Cancers
            Prognosis and Immune Microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Jin,T., Yang,L., Chang,C., Luo,H., Wang,R., Gan,Y., Sun,Y., Guo,Y.,
            Tang,R., Chen,S., Meng,D., Dai,P. and Liu,M.
  TITLE     HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective Export via
            ALYREF/NXF1 Complex to Foster Breast Cancer Development
  JOURNAL   Adv Sci (Weinh) 11 (24), e2307639 (2024)
   PUBMED   38626369
  REMARK    GeneRIF: HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective
            Export via ALYREF/NXF1 Complex to Foster Breast Cancer Development.
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Yang,Y., Zhang,Y., Feng,T. and Zhu,C.
  TITLE     HNRNPA2B1 induces cell proliferation and acts as biomarker in
            breast cancer
  JOURNAL   Cancer Biomark 40 (3-4), 285-296 (2024)
   PUBMED   39177591
  REMARK    GeneRIF: HNRNPA2B1 induces cell proliferation and acts as biomarker
            in breast cancer.
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Wilk,H.E., Schaefer,K.P., Agris,P.F., Boak,A.M. and Kovacs,S.A.
  TITLE     U1 SnRNP association with HnRNP involves an initial non-specific
            splice-site independent interaction of U1 SnRNP protein with HnRNA
  JOURNAL   Mol Cell Biochem 106 (1), 55-66 (1991)
   PUBMED   1833625
REFERENCE   8  (residues 1 to 301)
  AUTHORS   Bauw,G., Rasmussen,H.H., van den Bulcke,M., van Damme,J., Puype,M.,
            Gesser,B., Celis,J.E. and Vandekerckhove,J.
  TITLE     Two-dimensional gel electrophoresis, protein electroblotting and
            microsequencing: a direct link between proteins and genes
  JOURNAL   Electrophoresis 11 (7), 528-536 (1990)
   PUBMED   1699755
REFERENCE   9  (residues 1 to 301)
  AUTHORS   Burd,C.G., Swanson,M.S., Gorlach,M. and Dreyfuss,G.
  TITLE     Primary structures of the heterogeneous nuclear ribonucleoprotein
            A2, B1, and C2 proteins: a diversity of RNA binding proteins is
            generated by small peptide inserts
  JOURNAL   Proc Natl Acad Sci U S A 86 (24), 9788-9792 (1989)
   PUBMED   2557628
REFERENCE   10 (residues 1 to 301)
  AUTHORS   Kumar,A., Williams,K.R. and Szer,W.
  TITLE     Purification and domain structure of core hnRNP proteins A1 and A2
            and their relationship to single-stranded DNA-binding proteins
  JOURNAL   J Biol Chem 261 (24), 11266-11273 (1986)
   PUBMED   3733753
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010677.4 and AC004520.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047276260.1, XP_054214040.1.
            
            Summary: This gene belongs to the A/B subfamily of ubiquitously
            expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The
            hnRNPs are RNA binding proteins and they complex with heterogeneous
            nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs
            in the nucleus and appear to influence pre-mRNA processing and
            other aspects of mRNA metabolism and transport. While all of the
            hnRNPs are present in the nucleus, some seem to shuttle between the
            nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic
            acid binding properties. The protein encoded by this gene has two
            repeats of quasi-RRM domains that bind to RNAs. This gene has been
            described to generate two alternatively spliced transcript variants
            which encode different isoforms. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.4296424.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.2"
     Protein         1..301
                     /product="heterogeneous nuclear ribonucleoproteins A2/B1
                     isoform 4"
                     /note="nuclear ribonucleoprotein particle A2 protein;
                     heterogeneous nuclear ribonucleoproteins A2/B1; hnRNP A2 /
                     hnRNP B1; HNRNPA2B1/MYC fusion; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=32356
     Region          7..87
                     /region_name="RRM1_hnRNPA2B1"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12762"
                     /db_xref="CDD:410155"
     Site            order(10,12,14..15,37,39,41,50..52,54,77,80,82..87)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410155"
     Region          100..179
                     /region_name="RRM2_hnRNPA2B1"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12581"
                     /db_xref="CDD:409995"
     Region          248..274
                     /region_name="HnRNPA1"
                     /note="Nuclear factor hnRNPA1; pfam11627"
                     /db_xref="CDD:463312"
     CDS             1..301
                     /gene="HNRNPA2B1"
                     /gene_synonym="HNRNPA2; HNRNPB1; HNRPA2; HNRPA2B1; HNRPB1;
                     IBMPFD2; OPDM2; OPMD2; RNPA2; SNRPB1"
                     /coded_by="NM_001438575.1:170..1075"
                     /note="isoform 4 is encoded by transcript variant 11"
                     /db_xref="GeneID:3181"
                     /db_xref="HGNC:HGNC:5033"
                     /db_xref="MIM:600124"
ORIGIN      
        1 merekeqfrk lfigglsfet teeslrnyye qwgkltdcvv mrdpaskrsr gfgfvtfssm
       61 aevdaamaar phsidgrvve pkravarees gkpgahvtvk klfvggiked teehhlrdyf
      121 eeygkidtie iitdrqsgkk rgfgfvtfdd hdpvdkivlq kyhtinghna evrkalsrqe
      181 mqevqssrsg rggnfgfgds rggggnfgpg pgsnfrggsd gygsgrgfgd gyngygggpg
      241 gnygsgnynd fgnynqqpsn ygpmksgnfg gsrnmggpyg ggnygpggsg gsggyggrsr
      301 y
//
LOCUS       NP_001425501             341 aa            linear   PRI 01-JAN-2026
DEFINITION  heterogeneous nuclear ribonucleoproteins A2/B1 isoform A2 [Homo
            sapiens].
ACCESSION   NP_001425501 XP_047276256 XP_054214035
VERSION     NP_001425501.1
DBSOURCE    REFSEQ: accession NM_001438572.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Zhang,X., Yan,L.-n., Liu,B.-y., Zhou,C.-m. and Yu,X.-j.
  TITLE     The hnRNP A2B1 is important for the replication of SFTSV and other
            RNA viruses
  JOURNAL   Microbiol Spectr 12 (10), e0082924 (2024)
   PUBMED   39166862
  REMARK    GeneRIF: The hnRNP A2B1 is important for the replication of SFTSV
            and other RNA viruses.
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Huang,T., Zhu,G. and Chen,F.
  TITLE     The Potential Impact of HNRNPA2B1 on Human Cancers Prognosis and
            Immune Microenvironment
  JOURNAL   J Immunol Res 2024, 5515307 (2024)
   PUBMED   39268079
  REMARK    GeneRIF: The Potential Impact of HNRNPA2B1 on Human Cancers
            Prognosis and Immune Microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Jin,T., Yang,L., Chang,C., Luo,H., Wang,R., Gan,Y., Sun,Y., Guo,Y.,
            Tang,R., Chen,S., Meng,D., Dai,P. and Liu,M.
  TITLE     HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective Export via
            ALYREF/NXF1 Complex to Foster Breast Cancer Development
  JOURNAL   Adv Sci (Weinh) 11 (24), e2307639 (2024)
   PUBMED   38626369
  REMARK    GeneRIF: HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective
            Export via ALYREF/NXF1 Complex to Foster Breast Cancer Development.
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Yang,Y., Zhang,Y., Feng,T. and Zhu,C.
  TITLE     HNRNPA2B1 induces cell proliferation and acts as biomarker in
            breast cancer
  JOURNAL   Cancer Biomark 40 (3-4), 285-296 (2024)
   PUBMED   39177591
  REMARK    GeneRIF: HNRNPA2B1 induces cell proliferation and acts as biomarker
            in breast cancer.
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Wilk,H.E., Schaefer,K.P., Agris,P.F., Boak,A.M. and Kovacs,S.A.
  TITLE     U1 SnRNP association with HnRNP involves an initial non-specific
            splice-site independent interaction of U1 SnRNP protein with HnRNA
  JOURNAL   Mol Cell Biochem 106 (1), 55-66 (1991)
   PUBMED   1833625
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Bauw,G., Rasmussen,H.H., van den Bulcke,M., van Damme,J., Puype,M.,
            Gesser,B., Celis,J.E. and Vandekerckhove,J.
  TITLE     Two-dimensional gel electrophoresis, protein electroblotting and
            microsequencing: a direct link between proteins and genes
  JOURNAL   Electrophoresis 11 (7), 528-536 (1990)
   PUBMED   1699755
REFERENCE   9  (residues 1 to 341)
  AUTHORS   Burd,C.G., Swanson,M.S., Gorlach,M. and Dreyfuss,G.
  TITLE     Primary structures of the heterogeneous nuclear ribonucleoprotein
            A2, B1, and C2 proteins: a diversity of RNA binding proteins is
            generated by small peptide inserts
  JOURNAL   Proc Natl Acad Sci U S A 86 (24), 9788-9792 (1989)
   PUBMED   2557628
REFERENCE   10 (residues 1 to 341)
  AUTHORS   Kumar,A., Williams,K.R. and Szer,W.
  TITLE     Purification and domain structure of core hnRNP proteins A1 and A2
            and their relationship to single-stranded DNA-binding proteins
  JOURNAL   J Biol Chem 261 (24), 11266-11273 (1986)
   PUBMED   3733753
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010677.4 and AC004520.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047276256.1, XP_054214035.1.
            
            Summary: This gene belongs to the A/B subfamily of ubiquitously
            expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The
            hnRNPs are RNA binding proteins and they complex with heterogeneous
            nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs
            in the nucleus and appear to influence pre-mRNA processing and
            other aspects of mRNA metabolism and transport. While all of the
            hnRNPs are present in the nucleus, some seem to shuttle between the
            nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic
            acid binding properties. The protein encoded by this gene has two
            repeats of quasi-RRM domains that bind to RNAs. This gene has been
            described to generate two alternatively spliced transcript variants
            which encode different isoforms. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3425971.1,
                                           SRR18074969.2870618.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.2"
     Protein         1..341
                     /product="heterogeneous nuclear ribonucleoproteins A2/B1
                     isoform A2"
                     /note="nuclear ribonucleoprotein particle A2 protein;
                     heterogeneous nuclear ribonucleoproteins A2/B1; hnRNP A2 /
                     hnRNP B1; HNRNPA2B1/MYC fusion; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=35875
     Region          7..87
                     /region_name="RRM1_hnRNPA2B1"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12762"
                     /db_xref="CDD:410155"
     Site            order(10,12,14..15,37,39,41,50..52,54,77,80,82..87)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410155"
     Region          100..179
                     /region_name="RRM2_hnRNPA2B1"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12581"
                     /db_xref="CDD:409995"
     Region          290..314
                     /region_name="HnRNPA1"
                     /note="Nuclear factor hnRNPA1; pfam11627"
                     /db_xref="CDD:463312"
     CDS             1..341
                     /gene="HNRNPA2B1"
                     /gene_synonym="HNRNPA2; HNRNPB1; HNRPA2; HNRPA2B1; HNRPB1;
                     IBMPFD2; OPDM2; OPMD2; RNPA2; SNRPB1"
                     /coded_by="NM_001438572.1:170..1195"
                     /note="isoform A2 is encoded by transcript variant 8"
                     /db_xref="GeneID:3181"
                     /db_xref="HGNC:HGNC:5033"
                     /db_xref="MIM:600124"
ORIGIN      
        1 merekeqfrk lfigglsfet teeslrnyye qwgkltdcvv mrdpaskrsr gfgfvtfssm
       61 aevdaamaar phsidgrvve pkravarees gkpgahvtvk klfvggiked teehhlrdyf
      121 eeygkidtie iitdrqsgkk rgfgfvtfdd hdpvdkivlq kyhtinghna evrkalsrqe
      181 mqevqssrsg rggnfgfgds rggggnfgpg pgsnfrggsd gygsgrgfgd gyngygggpg
      241 ggnfggspgy gggrggyggg gpgygnqggg ygggydnygg gnygsgnynd fgnynqqpsn
      301 ygpmksgnfg gsrnmggpyg ggnygpggsg gsggyggrsr y
//
LOCUS       NP_001425502             313 aa            linear   PRI 01-JAN-2026
DEFINITION  heterogeneous nuclear ribonucleoproteins A2/B1 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001425502 XP_047276257 XP_054214037
VERSION     NP_001425502.1
DBSOURCE    REFSEQ: accession NM_001438573.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Zhang,X., Yan,L.-n., Liu,B.-y., Zhou,C.-m. and Yu,X.-j.
  TITLE     The hnRNP A2B1 is important for the replication of SFTSV and other
            RNA viruses
  JOURNAL   Microbiol Spectr 12 (10), e0082924 (2024)
   PUBMED   39166862
  REMARK    GeneRIF: The hnRNP A2B1 is important for the replication of SFTSV
            and other RNA viruses.
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Huang,T., Zhu,G. and Chen,F.
  TITLE     The Potential Impact of HNRNPA2B1 on Human Cancers Prognosis and
            Immune Microenvironment
  JOURNAL   J Immunol Res 2024, 5515307 (2024)
   PUBMED   39268079
  REMARK    GeneRIF: The Potential Impact of HNRNPA2B1 on Human Cancers
            Prognosis and Immune Microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Jin,T., Yang,L., Chang,C., Luo,H., Wang,R., Gan,Y., Sun,Y., Guo,Y.,
            Tang,R., Chen,S., Meng,D., Dai,P. and Liu,M.
  TITLE     HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective Export via
            ALYREF/NXF1 Complex to Foster Breast Cancer Development
  JOURNAL   Adv Sci (Weinh) 11 (24), e2307639 (2024)
   PUBMED   38626369
  REMARK    GeneRIF: HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective
            Export via ALYREF/NXF1 Complex to Foster Breast Cancer Development.
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Yang,Y., Zhang,Y., Feng,T. and Zhu,C.
  TITLE     HNRNPA2B1 induces cell proliferation and acts as biomarker in
            breast cancer
  JOURNAL   Cancer Biomark 40 (3-4), 285-296 (2024)
   PUBMED   39177591
  REMARK    GeneRIF: HNRNPA2B1 induces cell proliferation and acts as biomarker
            in breast cancer.
REFERENCE   6  (residues 1 to 313)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 313)
  AUTHORS   Wilk,H.E., Schaefer,K.P., Agris,P.F., Boak,A.M. and Kovacs,S.A.
  TITLE     U1 SnRNP association with HnRNP involves an initial non-specific
            splice-site independent interaction of U1 SnRNP protein with HnRNA
  JOURNAL   Mol Cell Biochem 106 (1), 55-66 (1991)
   PUBMED   1833625
REFERENCE   8  (residues 1 to 313)
  AUTHORS   Bauw,G., Rasmussen,H.H., van den Bulcke,M., van Damme,J., Puype,M.,
            Gesser,B., Celis,J.E. and Vandekerckhove,J.
  TITLE     Two-dimensional gel electrophoresis, protein electroblotting and
            microsequencing: a direct link between proteins and genes
  JOURNAL   Electrophoresis 11 (7), 528-536 (1990)
   PUBMED   1699755
REFERENCE   9  (residues 1 to 313)
  AUTHORS   Burd,C.G., Swanson,M.S., Gorlach,M. and Dreyfuss,G.
  TITLE     Primary structures of the heterogeneous nuclear ribonucleoprotein
            A2, B1, and C2 proteins: a diversity of RNA binding proteins is
            generated by small peptide inserts
  JOURNAL   Proc Natl Acad Sci U S A 86 (24), 9788-9792 (1989)
   PUBMED   2557628
REFERENCE   10 (residues 1 to 313)
  AUTHORS   Kumar,A., Williams,K.R. and Szer,W.
  TITLE     Purification and domain structure of core hnRNP proteins A1 and A2
            and their relationship to single-stranded DNA-binding proteins
  JOURNAL   J Biol Chem 261 (24), 11266-11273 (1986)
   PUBMED   3733753
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010677.4 and AC004520.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047276257.1, XP_054214037.1.
            
            Summary: This gene belongs to the A/B subfamily of ubiquitously
            expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The
            hnRNPs are RNA binding proteins and they complex with heterogeneous
            nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs
            in the nucleus and appear to influence pre-mRNA processing and
            other aspects of mRNA metabolism and transport. While all of the
            hnRNPs are present in the nucleus, some seem to shuttle between the
            nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic
            acid binding properties. The protein encoded by this gene has two
            repeats of quasi-RRM domains that bind to RNAs. This gene has been
            described to generate two alternatively spliced transcript variants
            which encode different isoforms. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4474714.1,
                                           SRR14038196.222742.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.2"
     Protein         1..313
                     /product="heterogeneous nuclear ribonucleoproteins A2/B1
                     isoform 3"
                     /note="nuclear ribonucleoprotein particle A2 protein;
                     heterogeneous nuclear ribonucleoproteins A2/B1; hnRNP A2 /
                     hnRNP B1; HNRNPA2B1/MYC fusion; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=33780
     Region          19..99
                     /region_name="RRM1_hnRNPA2B1"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12762"
                     /db_xref="CDD:410155"
     Site            order(22,24,26..27,49,51,53,62..64,66,89,92,94..99)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410155"
     Region          112..191
                     /region_name="RRM2_hnRNPA2B1"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12581"
                     /db_xref="CDD:409995"
     Region          260..286
                     /region_name="HnRNPA1"
                     /note="Nuclear factor hnRNPA1; pfam11627"
                     /db_xref="CDD:463312"
     CDS             1..313
                     /gene="HNRNPA2B1"
                     /gene_synonym="HNRNPA2; HNRNPB1; HNRPA2; HNRPA2B1; HNRPB1;
                     IBMPFD2; OPDM2; OPMD2; RNPA2; SNRPB1"
                     /coded_by="NM_001438573.1:170..1111"
                     /note="isoform 3 is encoded by transcript variant 9"
                     /db_xref="GeneID:3181"
                     /db_xref="HGNC:HGNC:5033"
                     /db_xref="MIM:600124"
ORIGIN      
        1 mektletvpl erkkrekeqf rklfigglsf etteeslrny yeqwgkltdc vvmrdpaskr
       61 srgfgfvtfs smaevdaama arphsidgrv vepkravare esgkpgahvt vkklfvggik
      121 edteehhlrd yfeeygkidt ieiitdrqsg kkrgfgfvtf ddhdpvdkiv lqkyhtingh
      181 naevrkalsr qemqevqssr sgrggnfgfg dsrggggnfg pgpgsnfrgg sdgygsgrgf
      241 gdgyngyggg pggnygsgny ndfgnynqqp snygpmksgn fggsrnmggp ygggnygpgg
      301 sggsggyggr sry
//
LOCUS       NP_001425499             353 aa            linear   PRI 01-JAN-2026
DEFINITION  heterogeneous nuclear ribonucleoproteins A2/B1 isoform B1 [Homo
            sapiens].
ACCESSION   NP_001425499 XP_047276255 XP_054214032
VERSION     NP_001425499.1
DBSOURCE    REFSEQ: accession NM_001438570.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Zhang,X., Yan,L.-n., Liu,B.-y., Zhou,C.-m. and Yu,X.-j.
  TITLE     The hnRNP A2B1 is important for the replication of SFTSV and other
            RNA viruses
  JOURNAL   Microbiol Spectr 12 (10), e0082924 (2024)
   PUBMED   39166862
  REMARK    GeneRIF: The hnRNP A2B1 is important for the replication of SFTSV
            and other RNA viruses.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Huang,T., Zhu,G. and Chen,F.
  TITLE     The Potential Impact of HNRNPA2B1 on Human Cancers Prognosis and
            Immune Microenvironment
  JOURNAL   J Immunol Res 2024, 5515307 (2024)
   PUBMED   39268079
  REMARK    GeneRIF: The Potential Impact of HNRNPA2B1 on Human Cancers
            Prognosis and Immune Microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Jin,T., Yang,L., Chang,C., Luo,H., Wang,R., Gan,Y., Sun,Y., Guo,Y.,
            Tang,R., Chen,S., Meng,D., Dai,P. and Liu,M.
  TITLE     HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective Export via
            ALYREF/NXF1 Complex to Foster Breast Cancer Development
  JOURNAL   Adv Sci (Weinh) 11 (24), e2307639 (2024)
   PUBMED   38626369
  REMARK    GeneRIF: HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective
            Export via ALYREF/NXF1 Complex to Foster Breast Cancer Development.
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Yang,Y., Zhang,Y., Feng,T. and Zhu,C.
  TITLE     HNRNPA2B1 induces cell proliferation and acts as biomarker in
            breast cancer
  JOURNAL   Cancer Biomark 40 (3-4), 285-296 (2024)
   PUBMED   39177591
  REMARK    GeneRIF: HNRNPA2B1 induces cell proliferation and acts as biomarker
            in breast cancer.
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Wilk,H.E., Schaefer,K.P., Agris,P.F., Boak,A.M. and Kovacs,S.A.
  TITLE     U1 SnRNP association with HnRNP involves an initial non-specific
            splice-site independent interaction of U1 SnRNP protein with HnRNA
  JOURNAL   Mol Cell Biochem 106 (1), 55-66 (1991)
   PUBMED   1833625
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Bauw,G., Rasmussen,H.H., van den Bulcke,M., van Damme,J., Puype,M.,
            Gesser,B., Celis,J.E. and Vandekerckhove,J.
  TITLE     Two-dimensional gel electrophoresis, protein electroblotting and
            microsequencing: a direct link between proteins and genes
  JOURNAL   Electrophoresis 11 (7), 528-536 (1990)
   PUBMED   1699755
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Burd,C.G., Swanson,M.S., Gorlach,M. and Dreyfuss,G.
  TITLE     Primary structures of the heterogeneous nuclear ribonucleoprotein
            A2, B1, and C2 proteins: a diversity of RNA binding proteins is
            generated by small peptide inserts
  JOURNAL   Proc Natl Acad Sci U S A 86 (24), 9788-9792 (1989)
   PUBMED   2557628
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Kumar,A., Williams,K.R. and Szer,W.
  TITLE     Purification and domain structure of core hnRNP proteins A1 and A2
            and their relationship to single-stranded DNA-binding proteins
  JOURNAL   J Biol Chem 261 (24), 11266-11273 (1986)
   PUBMED   3733753
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010677.4 and AC004520.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047276255.1, XP_054214032.1.
            
            Summary: This gene belongs to the A/B subfamily of ubiquitously
            expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The
            hnRNPs are RNA binding proteins and they complex with heterogeneous
            nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs
            in the nucleus and appear to influence pre-mRNA processing and
            other aspects of mRNA metabolism and transport. While all of the
            hnRNPs are present in the nucleus, some seem to shuttle between the
            nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic
            acid binding properties. The protein encoded by this gene has two
            repeats of quasi-RRM domains that bind to RNAs. This gene has been
            described to generate two alternatively spliced transcript variants
            which encode different isoforms. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.2579085.1,
                                           SRR14038195.389786.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.2"
     Protein         1..353
                     /product="heterogeneous nuclear ribonucleoproteins A2/B1
                     isoform B1"
                     /note="nuclear ribonucleoprotein particle A2 protein;
                     heterogeneous nuclear ribonucleoproteins A2/B1; hnRNP A2 /
                     hnRNP B1; HNRNPA2B1/MYC fusion; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=37299
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Region          9..15
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Region          19..99
                     /region_name="RRM1_hnRNPA2B1"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12762"
                     /db_xref="CDD:410155"
     Site            order(22,24,26..27,49,51,53,62..64,66,89,92,94..99)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410155"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            38
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            104
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|Ref.6; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Region          112..191
                     /region_name="RRM2_hnRNPA2B1"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12581"
                     /db_xref="CDD:409995"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            168
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            173
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Region          193..353
                     /region_name="Disordered.
                     /evidence=ECO:0000269|PubMed:26544936"
                     /note="propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            203
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O88569; Dimethylated
                     arginine, alternate. /evidence=ECO:0000269|Ref.6;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|Ref.6, ECO:0007744|PubMed:15782174,
                     ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            213
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O88569; Dimethylated
                     arginine, alternate. /evidence=ECO:0000269|Ref.6;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|Ref.6, ECO:0007744|PubMed:24129315;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            228
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000269|PubMed:31320558,
                     ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            238
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            266
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:A7VJC2;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Region          302..326
                     /region_name="HnRNPA1"
                     /note="Nuclear factor hnRNPA1; pfam11627"
                     /db_xref="CDD:463312"
     Region          308..347
                     /region_name="Nuclear targeting sequence.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            325
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            350
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     CDS             1..353
                     /gene="HNRNPA2B1"
                     /gene_synonym="HNRNPA2; HNRNPB1; HNRPA2; HNRPA2B1; HNRPB1;
                     IBMPFD2; OPDM2; OPMD2; RNPA2; SNRPB1"
                     /coded_by="NM_001438570.1:170..1231"
                     /note="isoform B1 is encoded by transcript variant 6"
                     /db_xref="GeneID:3181"
                     /db_xref="HGNC:HGNC:5033"
                     /db_xref="MIM:600124"
ORIGIN      
        1 mektletvpl erkkrekeqf rklfigglsf etteeslrny yeqwgkltdc vvmrdpaskr
       61 srgfgfvtfs smaevdaama arphsidgrv vepkravare esgkpgahvt vkklfvggik
      121 edteehhlrd yfeeygkidt ieiitdrqsg kkrgfgfvtf ddhdpvdkiv lqkyhtingh
      181 naevrkalsr qemqevqssr sgrggnfgfg dsrggggnfg pgpgsnfrgg sdgygsgrgf
      241 gdgyngyggg pgggnfggsp gygggrggyg gggpgygnqg ggygggydny gggnygsgny
      301 ndfgnynqqp snygpmksgn fggsrnmggp ygggnygpgg sggsggyggr sry
//
LOCUS       NP_112533                353 aa            linear   PRI 01-JAN-2026
DEFINITION  heterogeneous nuclear ribonucleoproteins A2/B1 isoform B1 [Homo
            sapiens].
ACCESSION   NP_112533
VERSION     NP_112533.1
DBSOURCE    REFSEQ: accession NM_031243.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Zhang,X., Yan,L.-n., Liu,B.-y., Zhou,C.-m. and Yu,X.-j.
  TITLE     The hnRNP A2B1 is important for the replication of SFTSV and other
            RNA viruses
  JOURNAL   Microbiol Spectr 12 (10), e0082924 (2024)
   PUBMED   39166862
  REMARK    GeneRIF: The hnRNP A2B1 is important for the replication of SFTSV
            and other RNA viruses.
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Huang,T., Zhu,G. and Chen,F.
  TITLE     The Potential Impact of HNRNPA2B1 on Human Cancers Prognosis and
            Immune Microenvironment
  JOURNAL   J Immunol Res 2024, 5515307 (2024)
   PUBMED   39268079
  REMARK    GeneRIF: The Potential Impact of HNRNPA2B1 on Human Cancers
            Prognosis and Immune Microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Jin,T., Yang,L., Chang,C., Luo,H., Wang,R., Gan,Y., Sun,Y., Guo,Y.,
            Tang,R., Chen,S., Meng,D., Dai,P. and Liu,M.
  TITLE     HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective Export via
            ALYREF/NXF1 Complex to Foster Breast Cancer Development
  JOURNAL   Adv Sci (Weinh) 11 (24), e2307639 (2024)
   PUBMED   38626369
  REMARK    GeneRIF: HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective
            Export via ALYREF/NXF1 Complex to Foster Breast Cancer Development.
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Yang,Y., Zhang,Y., Feng,T. and Zhu,C.
  TITLE     HNRNPA2B1 induces cell proliferation and acts as biomarker in
            breast cancer
  JOURNAL   Cancer Biomark 40 (3-4), 285-296 (2024)
   PUBMED   39177591
  REMARK    GeneRIF: HNRNPA2B1 induces cell proliferation and acts as biomarker
            in breast cancer.
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Wilk,H.E., Schaefer,K.P., Agris,P.F., Boak,A.M. and Kovacs,S.A.
  TITLE     U1 SnRNP association with HnRNP involves an initial non-specific
            splice-site independent interaction of U1 SnRNP protein with HnRNA
  JOURNAL   Mol Cell Biochem 106 (1), 55-66 (1991)
   PUBMED   1833625
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Bauw,G., Rasmussen,H.H., van den Bulcke,M., van Damme,J., Puype,M.,
            Gesser,B., Celis,J.E. and Vandekerckhove,J.
  TITLE     Two-dimensional gel electrophoresis, protein electroblotting and
            microsequencing: a direct link between proteins and genes
  JOURNAL   Electrophoresis 11 (7), 528-536 (1990)
   PUBMED   1699755
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Burd,C.G., Swanson,M.S., Gorlach,M. and Dreyfuss,G.
  TITLE     Primary structures of the heterogeneous nuclear ribonucleoprotein
            A2, B1, and C2 proteins: a diversity of RNA binding proteins is
            generated by small peptide inserts
  JOURNAL   Proc Natl Acad Sci U S A 86 (24), 9788-9792 (1989)
   PUBMED   2557628
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Kumar,A., Williams,K.R. and Szer,W.
  TITLE     Purification and domain structure of core hnRNP proteins A1 and A2
            and their relationship to single-stranded DNA-binding proteins
  JOURNAL   J Biol Chem 261 (24), 11266-11273 (1986)
   PUBMED   3733753
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010677.4 and AC004520.2.
            
            Summary: This gene belongs to the A/B subfamily of ubiquitously
            expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The
            hnRNPs are RNA binding proteins and they complex with heterogeneous
            nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs
            in the nucleus and appear to influence pre-mRNA processing and
            other aspects of mRNA metabolism and transport. While all of the
            hnRNPs are present in the nucleus, some seem to shuttle between the
            nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic
            acid binding properties. The protein encoded by this gene has two
            repeats of quasi-RRM domains that bind to RNAs. This gene has been
            described to generate two alternatively spliced transcript variants
            which encode different isoforms. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (B1) contains an additional 36
            bases compared to variant A2. This additional region affects only
            the beginning of the coding region. The N-terminus of isoform B1 is
            thus different from isoform A2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4444023.1,
                                           SRR14038191.2873484.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.2"
     Protein         1..353
                     /product="heterogeneous nuclear ribonucleoproteins A2/B1
                     isoform B1"
                     /note="nuclear ribonucleoprotein particle A2 protein;
                     heterogeneous nuclear ribonucleoproteins A2/B1; hnRNP A2 /
                     hnRNP B1; HNRNPA2B1/MYC fusion; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=37299
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Region          9..15
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Region          19..99
                     /region_name="RRM1_hnRNPA2B1"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12762"
                     /db_xref="CDD:410155"
     Site            order(22,24,26..27,49,51,53,62..64,66,89,92,94..99)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410155"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            38
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            104
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|Ref.6; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Region          112..191
                     /region_name="RRM2_hnRNPA2B1"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12581"
                     /db_xref="CDD:409995"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            168
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            173
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Region          193..353
                     /region_name="Disordered.
                     /evidence=ECO:0000269|PubMed:26544936"
                     /note="propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            203
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O88569; Dimethylated
                     arginine, alternate. /evidence=ECO:0000269|Ref.6;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|Ref.6, ECO:0007744|PubMed:15782174,
                     ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            213
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O88569; Dimethylated
                     arginine, alternate. /evidence=ECO:0000269|Ref.6;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|Ref.6, ECO:0007744|PubMed:24129315;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            228
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000269|PubMed:31320558,
                     ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            238
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            266
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:A7VJC2;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Region          302..326
                     /region_name="HnRNPA1"
                     /note="Nuclear factor hnRNPA1; pfam11627"
                     /db_xref="CDD:463312"
     Region          308..347
                     /region_name="Nuclear targeting sequence.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P22626.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            325
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     Site            350
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P22626.2)"
     CDS             1..353
                     /gene="HNRNPA2B1"
                     /gene_synonym="HNRNPA2; HNRNPB1; HNRPA2; HNRPA2B1; HNRPB1;
                     IBMPFD2; OPDM2; OPMD2; RNPA2; SNRPB1"
                     /coded_by="NM_031243.4:170..1231"
                     /note="isoform B1 is encoded by transcript variant B1"
                     /db_xref="CCDS:CCDS43557.1"
                     /db_xref="GeneID:3181"
                     /db_xref="HGNC:HGNC:5033"
                     /db_xref="MIM:600124"
ORIGIN      
        1 mektletvpl erkkrekeqf rklfigglsf etteeslrny yeqwgkltdc vvmrdpaskr
       61 srgfgfvtfs smaevdaama arphsidgrv vepkravare esgkpgahvt vkklfvggik
      121 edteehhlrd yfeeygkidt ieiitdrqsg kkrgfgfvtf ddhdpvdkiv lqkyhtingh
      181 naevrkalsr qemqevqssr sgrggnfgfg dsrggggnfg pgpgsnfrgg sdgygsgrgf
      241 gdgyngyggg pgggnfggsp gygggrggyg gggpgygnqg ggygggydny gggnygsgny
      301 ndfgnynqqp snygpmksgn fggsrnmggp ygggnygpgg sggsggyggr sry
//
LOCUS       NP_001425505             301 aa            linear   PRI 01-JAN-2026
DEFINITION  heterogeneous nuclear ribonucleoproteins A2/B1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001425505 XP_047276261 XP_054214041
VERSION     NP_001425505.1
DBSOURCE    REFSEQ: accession NM_001438576.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 301)
  AUTHORS   Zhang,X., Yan,L.-n., Liu,B.-y., Zhou,C.-m. and Yu,X.-j.
  TITLE     The hnRNP A2B1 is important for the replication of SFTSV and other
            RNA viruses
  JOURNAL   Microbiol Spectr 12 (10), e0082924 (2024)
   PUBMED   39166862
  REMARK    GeneRIF: The hnRNP A2B1 is important for the replication of SFTSV
            and other RNA viruses.
REFERENCE   2  (residues 1 to 301)
  AUTHORS   Huang,T., Zhu,G. and Chen,F.
  TITLE     The Potential Impact of HNRNPA2B1 on Human Cancers Prognosis and
            Immune Microenvironment
  JOURNAL   J Immunol Res 2024, 5515307 (2024)
   PUBMED   39268079
  REMARK    GeneRIF: The Potential Impact of HNRNPA2B1 on Human Cancers
            Prognosis and Immune Microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 301)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 301)
  AUTHORS   Jin,T., Yang,L., Chang,C., Luo,H., Wang,R., Gan,Y., Sun,Y., Guo,Y.,
            Tang,R., Chen,S., Meng,D., Dai,P. and Liu,M.
  TITLE     HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective Export via
            ALYREF/NXF1 Complex to Foster Breast Cancer Development
  JOURNAL   Adv Sci (Weinh) 11 (24), e2307639 (2024)
   PUBMED   38626369
  REMARK    GeneRIF: HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective
            Export via ALYREF/NXF1 Complex to Foster Breast Cancer Development.
REFERENCE   5  (residues 1 to 301)
  AUTHORS   Yang,Y., Zhang,Y., Feng,T. and Zhu,C.
  TITLE     HNRNPA2B1 induces cell proliferation and acts as biomarker in
            breast cancer
  JOURNAL   Cancer Biomark 40 (3-4), 285-296 (2024)
   PUBMED   39177591
  REMARK    GeneRIF: HNRNPA2B1 induces cell proliferation and acts as biomarker
            in breast cancer.
REFERENCE   6  (residues 1 to 301)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 301)
  AUTHORS   Wilk,H.E., Schaefer,K.P., Agris,P.F., Boak,A.M. and Kovacs,S.A.
  TITLE     U1 SnRNP association with HnRNP involves an initial non-specific
            splice-site independent interaction of U1 SnRNP protein with HnRNA
  JOURNAL   Mol Cell Biochem 106 (1), 55-66 (1991)
   PUBMED   1833625
REFERENCE   8  (residues 1 to 301)
  AUTHORS   Bauw,G., Rasmussen,H.H., van den Bulcke,M., van Damme,J., Puype,M.,
            Gesser,B., Celis,J.E. and Vandekerckhove,J.
  TITLE     Two-dimensional gel electrophoresis, protein electroblotting and
            microsequencing: a direct link between proteins and genes
  JOURNAL   Electrophoresis 11 (7), 528-536 (1990)
   PUBMED   1699755
REFERENCE   9  (residues 1 to 301)
  AUTHORS   Burd,C.G., Swanson,M.S., Gorlach,M. and Dreyfuss,G.
  TITLE     Primary structures of the heterogeneous nuclear ribonucleoprotein
            A2, B1, and C2 proteins: a diversity of RNA binding proteins is
            generated by small peptide inserts
  JOURNAL   Proc Natl Acad Sci U S A 86 (24), 9788-9792 (1989)
   PUBMED   2557628
REFERENCE   10 (residues 1 to 301)
  AUTHORS   Kumar,A., Williams,K.R. and Szer,W.
  TITLE     Purification and domain structure of core hnRNP proteins A1 and A2
            and their relationship to single-stranded DNA-binding proteins
  JOURNAL   J Biol Chem 261 (24), 11266-11273 (1986)
   PUBMED   3733753
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010677.4 and AC004520.2.
            
            On or before Apr 22, 2025 this sequence version replaced
            XP_047276261.1, XP_054214041.1.
            
            Summary: This gene belongs to the A/B subfamily of ubiquitously
            expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The
            hnRNPs are RNA binding proteins and they complex with heterogeneous
            nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs
            in the nucleus and appear to influence pre-mRNA processing and
            other aspects of mRNA metabolism and transport. While all of the
            hnRNPs are present in the nucleus, some seem to shuttle between the
            nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic
            acid binding properties. The protein encoded by this gene has two
            repeats of quasi-RRM domains that bind to RNAs. This gene has been
            described to generate two alternatively spliced transcript variants
            which encode different isoforms. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.4712734.1,
                                           SRR14038191.1230720.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..301
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.2"
     Protein         1..301
                     /product="heterogeneous nuclear ribonucleoproteins A2/B1
                     isoform 4"
                     /note="nuclear ribonucleoprotein particle A2 protein;
                     heterogeneous nuclear ribonucleoproteins A2/B1; hnRNP A2 /
                     hnRNP B1; HNRNPA2B1/MYC fusion; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=32356
     Region          7..87
                     /region_name="RRM1_hnRNPA2B1"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12762"
                     /db_xref="CDD:410155"
     Site            order(10,12,14..15,37,39,41,50..52,54,77,80,82..87)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410155"
     Region          100..179
                     /region_name="RRM2_hnRNPA2B1"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12581"
                     /db_xref="CDD:409995"
     Region          248..274
                     /region_name="HnRNPA1"
                     /note="Nuclear factor hnRNPA1; pfam11627"
                     /db_xref="CDD:463312"
     CDS             1..301
                     /gene="HNRNPA2B1"
                     /gene_synonym="HNRNPA2; HNRNPB1; HNRPA2; HNRPA2B1; HNRPB1;
                     IBMPFD2; OPDM2; OPMD2; RNPA2; SNRPB1"
                     /coded_by="NM_001438576.1:170..1075"
                     /note="isoform 4 is encoded by transcript variant 12"
                     /db_xref="GeneID:3181"
                     /db_xref="HGNC:HGNC:5033"
                     /db_xref="MIM:600124"
ORIGIN      
        1 merekeqfrk lfigglsfet teeslrnyye qwgkltdcvv mrdpaskrsr gfgfvtfssm
       61 aevdaamaar phsidgrvve pkravarees gkpgahvtvk klfvggiked teehhlrdyf
      121 eeygkidtie iitdrqsgkk rgfgfvtfdd hdpvdkivlq kyhtinghna evrkalsrqe
      181 mqevqssrsg rggnfgfgds rggggnfgpg pgsnfrggsd gygsgrgfgd gyngygggpg
      241 gnygsgnynd fgnynqqpsn ygpmksgnfg gsrnmggpyg ggnygpggsg gsggyggrsr
      301 y
//
LOCUS       NP_002128                341 aa            linear   PRI 01-JAN-2026
DEFINITION  heterogeneous nuclear ribonucleoproteins A2/B1 isoform A2 [Homo
            sapiens].
ACCESSION   NP_002128
VERSION     NP_002128.1
DBSOURCE    REFSEQ: accession NM_002137.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Zhang,X., Yan,L.-n., Liu,B.-y., Zhou,C.-m. and Yu,X.-j.
  TITLE     The hnRNP A2B1 is important for the replication of SFTSV and other
            RNA viruses
  JOURNAL   Microbiol Spectr 12 (10), e0082924 (2024)
   PUBMED   39166862
  REMARK    GeneRIF: The hnRNP A2B1 is important for the replication of SFTSV
            and other RNA viruses.
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Huang,T., Zhu,G. and Chen,F.
  TITLE     The Potential Impact of HNRNPA2B1 on Human Cancers Prognosis and
            Immune Microenvironment
  JOURNAL   J Immunol Res 2024, 5515307 (2024)
   PUBMED   39268079
  REMARK    GeneRIF: The Potential Impact of HNRNPA2B1 on Human Cancers
            Prognosis and Immune Microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Jin,T., Yang,L., Chang,C., Luo,H., Wang,R., Gan,Y., Sun,Y., Guo,Y.,
            Tang,R., Chen,S., Meng,D., Dai,P. and Liu,M.
  TITLE     HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective Export via
            ALYREF/NXF1 Complex to Foster Breast Cancer Development
  JOURNAL   Adv Sci (Weinh) 11 (24), e2307639 (2024)
   PUBMED   38626369
  REMARK    GeneRIF: HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective
            Export via ALYREF/NXF1 Complex to Foster Breast Cancer Development.
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Yang,Y., Zhang,Y., Feng,T. and Zhu,C.
  TITLE     HNRNPA2B1 induces cell proliferation and acts as biomarker in
            breast cancer
  JOURNAL   Cancer Biomark 40 (3-4), 285-296 (2024)
   PUBMED   39177591
  REMARK    GeneRIF: HNRNPA2B1 induces cell proliferation and acts as biomarker
            in breast cancer.
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Wilk,H.E., Schaefer,K.P., Agris,P.F., Boak,A.M. and Kovacs,S.A.
  TITLE     U1 SnRNP association with HnRNP involves an initial non-specific
            splice-site independent interaction of U1 SnRNP protein with HnRNA
  JOURNAL   Mol Cell Biochem 106 (1), 55-66 (1991)
   PUBMED   1833625
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Bauw,G., Rasmussen,H.H., van den Bulcke,M., van Damme,J., Puype,M.,
            Gesser,B., Celis,J.E. and Vandekerckhove,J.
  TITLE     Two-dimensional gel electrophoresis, protein electroblotting and
            microsequencing: a direct link between proteins and genes
  JOURNAL   Electrophoresis 11 (7), 528-536 (1990)
   PUBMED   1699755
REFERENCE   9  (residues 1 to 341)
  AUTHORS   Burd,C.G., Swanson,M.S., Gorlach,M. and Dreyfuss,G.
  TITLE     Primary structures of the heterogeneous nuclear ribonucleoprotein
            A2, B1, and C2 proteins: a diversity of RNA binding proteins is
            generated by small peptide inserts
  JOURNAL   Proc Natl Acad Sci U S A 86 (24), 9788-9792 (1989)
   PUBMED   2557628
REFERENCE   10 (residues 1 to 341)
  AUTHORS   Kumar,A., Williams,K.R. and Szer,W.
  TITLE     Purification and domain structure of core hnRNP proteins A1 and A2
            and their relationship to single-stranded DNA-binding proteins
  JOURNAL   J Biol Chem 261 (24), 11266-11273 (1986)
   PUBMED   3733753
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB244417.1, M29065.1 and
            AC004520.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene belongs to the A/B subfamily of ubiquitously
            expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The
            hnRNPs are RNA binding proteins and they complex with heterogeneous
            nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs
            in the nucleus and appear to influence pre-mRNA processing and
            other aspects of mRNA metabolism and transport. While all of the
            hnRNPs are present in the nucleus, some seem to shuttle between the
            nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic
            acid binding properties. The protein encoded by this gene has two
            repeats of quasi-RRM domains that bind to RNAs. This gene has been
            described to generate two alternatively spliced transcript variants
            which encode different isoforms. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (A2) lacks 36 bases at the
            beginning of the coding region compared to variant B1. The
            N-terminus of isoform A2 is thus different from isoform B1. This
            isoform (A2) is the predominant protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.114214.1,
                                           SRR1803612.96491.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000618183.5/ ENSP00000478691.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p15.2"
     Protein         1..341
                     /product="heterogeneous nuclear ribonucleoproteins A2/B1
                     isoform A2"
                     /note="nuclear ribonucleoprotein particle A2 protein;
                     heterogeneous nuclear ribonucleoproteins A2/B1; hnRNP A2 /
                     hnRNP B1; HNRNPA2B1/MYC fusion; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=35875
     Region          7..87
                     /region_name="RRM1_hnRNPA2B1"
                     /note="RNA recognition motif 1 (RRM1) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12762"
                     /db_xref="CDD:410155"
     Site            order(10,12,14..15,37,39,41,50..52,54,77,80,82..87)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410155"
     Region          100..179
                     /region_name="RRM2_hnRNPA2B1"
                     /note="RNA recognition motif 2 (RRM2) found in
                     heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP
                     A2/B1) and similar proteins; cd12581"
                     /db_xref="CDD:409995"
     Region          290..314
                     /region_name="HnRNPA1"
                     /note="Nuclear factor hnRNPA1; pfam11627"
                     /db_xref="CDD:463312"
     CDS             1..341
                     /gene="HNRNPA2B1"
                     /gene_synonym="HNRNPA2; HNRNPB1; HNRPA2; HNRPA2B1; HNRPB1;
                     IBMPFD2; OPDM2; OPMD2; RNPA2; SNRPB1"
                     /coded_by="NM_002137.4:170..1195"
                     /note="isoform A2 is encoded by transcript variant A2"
                     /db_xref="CCDS:CCDS5397.1"
                     /db_xref="GeneID:3181"
                     /db_xref="HGNC:HGNC:5033"
                     /db_xref="MIM:600124"
ORIGIN      
        1 merekeqfrk lfigglsfet teeslrnyye qwgkltdcvv mrdpaskrsr gfgfvtfssm
       61 aevdaamaar phsidgrvve pkravarees gkpgahvtvk klfvggiked teehhlrdyf
      121 eeygkidtie iitdrqsgkk rgfgfvtfdd hdpvdkivlq kyhtinghna evrkalsrqe
      181 mqevqssrsg rggnfgfgds rggggnfgpg pgsnfrggsd gygsgrgfgd gyngygggpg
      241 ggnfggspgy gggrggyggg gpgygnqggg ygggydnygg gnygsgnynd fgnynqqpsn
      301 ygpmksgnfg gsrnmggpyg ggnygpggsg gsggyggrsr y
//
LOCUS       NP_001381291             341 aa            linear   PRI 02-JAN-2026
DEFINITION  single-stranded DNA-binding protein 3 isoform f [Homo sapiens].
ACCESSION   NP_001381291 XP_006710608
VERSION     NP_001381291.1
DBSOURCE    REFSEQ: accession NM_001394362.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Toren,E., Kepple,J.D., Coutinho,K.V., Poole,S.O., Deeba,I.M.,
            Pierre,T.H., Liu,Y., Bethea,M.M. and Hunter,C.S.
  TITLE     The SSBP3 co-regulator is required for glucose homeostasis,
            pancreatic islet architecture, and beta-cell identity
  JOURNAL   Mol Metab 76, 101785 (2023)
   PUBMED   37536498
  REMARK    GeneRIF: The SSBP3 co-regulator is required for glucose
            homeostasis, pancreatic islet architecture, and beta-cell identity.
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Hubel,P., Urban,C., Bergant,V., Schneider,W.M., Knauer,B.,
            Stukalov,A., Scaturro,P., Mann,A., Brunotte,L., Hoffmann,H.H.,
            Schoggins,J.W., Schwemmle,M., Mann,M., Rice,C.M. and Pichlmair,A.
  TITLE     A protein-interaction network of interferon-stimulated genes
            extends the innate immune system landscape
  JOURNAL   Nat Immunol 20 (4), 493-502 (2019)
   PUBMED   30833792
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Dey-Guha,I., Malik,N., Lesourne,R., Love,P.E. and Westphal,H.
  TITLE     Tyrosine phosphorylation controls nuclear localization and
            transcriptional activity of Ssdp1 in mammalian cells
  JOURNAL   J Cell Biochem 103 (6), 1856-1865 (2008)
   PUBMED   18080319
  REMARK    GeneRIF: phosphorylation involving N-terminal tyrosine residues of
            Ssdp1 is a means of regulating its nuclear localization and
            subsequent transcriptional activation of LIM-HD complexes.
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Wu,L.
  TITLE     Structure and functional characterization of single-strand DNA
            binding protein SSDP1: carboxyl-terminal of SSDP1 has transcription
            activity
  JOURNAL   Biochem Biophys Res Commun 339 (3), 977-984 (2006)
   PUBMED   16325762
  REMARK    GeneRIF: Thus, biochemical data of SSDP1 presented by this study
            provides biochemical evidence for a better understanding of
            transcriptional regulation.
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Chen,L., Segal,D., Hukriede,N.A., Podtelejnikov,A.V.,
            Bayarsaihan,D., Kennison,J.A., Ogryzko,V.V., Dawid,I.B. and
            Westphal,H.
  TITLE     Ssdp proteins interact with the LIM-domain-binding protein Ldb1 to
            regulate development
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14320-14325 (2002)
   PUBMED   12381786
  REMARK    GeneRIF: Ssdp proteins interact with the LIM-domain-binding protein
            Ldb1 to regulate development
REFERENCE   9  (residues 1 to 341)
  AUTHORS   Castro,P., Liang,H., Liang,J.C. and Nagarajan,L.
  TITLE     A novel, evolutionarily conserved gene family with putative
            sequence-specific single-stranded DNA-binding activity
  JOURNAL   Genomics 80 (1), 78-85 (2002)
   PUBMED   12079286
REFERENCE   10 (residues 1 to 341)
  AUTHORS   Raval-Fernandes,S., Kickhoefer,V.A. and Rome,L.H.
  TITLE     Cloning of a cDNA encoding a sequence-specific
            single-stranded-DNA-binding protein from Rattus norvegicus
  JOURNAL   Gene 237 (1), 201-207 (1999)
   PUBMED   10524251
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL035415.22 and AL161644.6.
            
            On Apr 15, 2021 this sequence version replaced XP_006710608.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1394059.1,
                                           SRR14038191.3641366.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..341
                     /product="single-stranded DNA-binding protein 3 isoform f"
                     /note="sequence-specific single-stranded-DNA-binding
                     protein"
                     /calculated_mol_wt=35355
     Region          17..43
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          81..318
                     /region_name="SSDP"
                     /note="Single-stranded DNA binding protein, SSDP;
                     pfam04503"
                     /db_xref="CDD:461334"
     CDS             1..341
                     /gene="SSBP3"
                     /gene_synonym="CSDP; SSDP; SSDP1"
                     /coded_by="NM_001394362.1:387..1412"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="GeneID:23648"
                     /db_xref="HGNC:HGNC:15674"
                     /db_xref="MIM:607390"
ORIGIN      
        1 mfakgkgsav psdgqarekl alyvyeyllh vgaqksaqtf lseirwekni tlgeppgflh
       61 swwcvfwdly caaperrdtc ehsseakafh dysaaaapsp vlgnippndg mpggpippgf
      121 fqppggvpgt qpllpnsmdp trqqghpnmg gsmqrmnppr gmgpmgpgpq nygsgmrppp
      181 nslgpampgi nmgpgagrpw pnpnsansip ysssspgtyv gppggggppg tpimpspads
      241 tnssdniytm inpvppggsr snfpmgpgsd gpmggmggme phhmngslgs gdidglpkns
      301 pnnisgisnp pgtprddgel ggnflhsfqn dnyspsmtms v
//
LOCUS       NP_001431902             293 aa            linear   PRI 05-JAN-2026
DEFINITION  translocon-associated protein subunit alpha isoform 3 precursor
            [Homo sapiens].
ACCESSION   NP_001431902
VERSION     NP_001431902.1
DBSOURCE    REFSEQ: accession NM_001444973.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Gemmer,M., Chaillet,M.L., van Loenhout,J., Cuevas Arenas,R.,
            Vismpas,D., Grollers-Mulderij,M., Koh,F.A., Albanese,P.,
            Scheltema,R.A., Howes,S.C., Kotecha,A., Fedry,J. and Forster,F.
  TITLE     Visualization of translation and protein biogenesis at the ER
            membrane
  JOURNAL   Nature 614 (7946), 160-167 (2023)
   PUBMED   36697828
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Yan,J., Wang,Z.H., Yan,Y., Luo,H.N., Ren,X.Y., Li,N., Zheng,G.X.
            and Hou,J.
  TITLE     RP11-156L14.1 regulates SSR1 expression by competitively binding to
            miR-548ao-3p in hypopharyngeal squamous cell carcinoma
  JOURNAL   Oncol Rep 44 (5), 2080-2092 (2020)
   PUBMED   33000261
  REMARK    GeneRIF: RP11156L14.1 regulates SSR1 expression by competitively
            binding to miR548ao3p in hypopharyngeal squamous cell carcinoma.
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Liu,X., Salokas,K., Tamene,F., Jiu,Y., Weldatsadik,R.G., Ohman,T.
            and Varjosalo,M.
  TITLE     An AP-MS- and BioID-compatible MAC-tag enables comprehensive
            mapping of protein interactions and subcellular localizations
  JOURNAL   Nat Commun 9 (1), 1188 (2018)
   PUBMED   29568061
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Mahajan,A., Go,M.J., Zhang,W., Below,J.E., Gaulton,K.J.,
            Ferreira,T., Horikoshi,M., Johnson,A.D., Ng,M.C., Prokopenko,I.,
            Saleheen,D., Wang,X., Zeggini,E., Abecasis,G.R., Adair,L.S.,
            Almgren,P., Atalay,M., Aung,T., Baldassarre,D., Balkau,B., Bao,Y.,
            Barnett,A.H., Barroso,I., Basit,A., Been,L.F., Beilby,J.,
            Bell,G.I., Benediktsson,R., Bergman,R.N., Boehm,B.O.,
            Boerwinkle,E., Bonnycastle,L.L., Burtt,N., Cai,Q., Campbell,H.,
            Carey,J., Cauchi,S., Caulfield,M., Chan,J.C., Chang,L.C.,
            Chang,T.J., Chang,Y.C., Charpentier,G., Chen,C.H., Chen,H.,
            Chen,Y.T., Chia,K.S., Chidambaram,M., Chines,P.S., Cho,N.H.,
            Cho,Y.M., Chuang,L.M., Collins,F.S., Cornelis,M.C., Couper,D.J.,
            Crenshaw,A.T., van Dam,R.M., Danesh,J., Das,D., de Faire,U.,
            Dedoussis,G., Deloukas,P., Dimas,A.S., Dina,C., Doney,A.S.,
            Donnelly,P.J., Dorkhan,M., van Duijn,C., Dupuis,J., Edkins,S.,
            Elliott,P., Emilsson,V., Erbel,R., Eriksson,J.G., Escobedo,J.,
            Esko,T., Eury,E., Florez,J.C., Fontanillas,P., Forouhi,N.G.,
            Forsen,T., Fox,C., Fraser,R.M., Frayling,T.M., Froguel,P.,
            Frossard,P., Gao,Y., Gertow,K., Gieger,C., Gigante,B., Grallert,H.,
            Grant,G.B., Grrop,L.C., Groves,C.J., Grundberg,E., Guiducci,C.,
            Hamsten,A., Han,B.G., Hara,K., Hassanali,N., Hattersley,A.T.,
            Hayward,C., Hedman,A.K., Herder,C., Hofman,A., Holmen,O.L.,
            Hovingh,K., Hreidarsson,A.B., Hu,C., Hu,F.B., Hui,J.,
            Humphries,S.E., Hunt,S.E., Hunter,D.J., Hveem,K., Hydrie,Z.I.,
            Ikegami,H., Illig,T., Ingelsson,E., Islam,M., Isomaa,B.,
            Jackson,A.U., Jafar,T., James,A., Jia,W., Jockel,K.H., Jonsson,A.,
            Jowett,J.B., Kadowaki,T., Kang,H.M., Kanoni,S., Kao,W.H.,
            Kathiresan,S., Kato,N., Katulanda,P., Keinanen-Kiukaanniemi,K.M.,
            Kelly,A.M., Khan,H., Khaw,K.T., Khor,C.C., Kim,H.L., Kim,S.,
            Kim,Y.J., Kinnunen,L., Klopp,N., Kong,A., Korpi-Hyovalti,E.,
            Kowlessur,S., Kraft,P., Kravic,J., Kristensen,M.M., Krithika,S.,
            Kumar,A., Kumate,J., Kuusisto,J., Kwak,S.H., Laakso,M., Lagou,V.,
            Lakka,T.A., Langenberg,C., Langford,C., Lawrence,R., Leander,K.,
            Lee,J.M., Lee,N.R., Li,M., Li,X., Li,Y., Liang,J., Liju,S.,
            Lim,W.Y., Lind,L., Lindgren,C.M., Lindholm,E., Liu,C.T., Liu,J.J.,
            Lobbens,S., Long,J., Loos,R.J., Lu,W., Luan,J., Lyssenko,V.,
            Ma,R.C., Maeda,S., Magi,R., Mannisto,S., Matthews,D.R., Meigs,J.B.,
            Melander,O., Metspalu,A., Meyer,J., Mirza,G., Mihailov,E.,
            Moebus,S., Mohan,V., Mohlke,K.L., Morris,A.D., Muhleisen,T.W.,
            Muller-Nurasyid,M., Musk,B., Nakamura,J., Nakashima,E., Navarro,P.,
            Ng,P.K., Nica,A.C., Nilsson,P.M., Njolstad,I., Nothen,M.M.,
            Ohnaka,K., Ong,T.H., Owen,K.R., Palmer,C.N., Pankow,J.S.,
            Park,K.S., Parkin,M., Pechlivanis,S., Pedersen,N.L., Peltonen,L.,
            Perry,J.R., Peters,A., Pinidiyapathirage,J.M., Platou,C.G.,
            Potter,S., Price,J.F., Qi,L., Radha,V., Rallidis,L., Rasheed,A.,
            Rathman,W., Rauramaa,R., Raychaudhuri,S., Rayner,N.W., Rees,S.D.,
            Rehnberg,E., Ripatti,S., Robertson,N., Roden,M., Rossin,E.J.,
            Rudan,I., Rybin,D., Saaristo,T.E., Salomaa,V., Saltevo,J.,
            Samuel,M., Sanghera,D.K., Saramies,J., Scott,J., Scott,L.J.,
            Scott,R.A., Segre,A.V., Sehmi,J., Sennblad,B., Shah,N., Shah,S.,
            Shera,A.S., Shu,X.O., Shuldiner,A.R., Sigurdsson,G., Sijbrands,E.,
            Silveira,A., Sim,X., Sivapalaratnam,S., Small,K.S., So,W.Y.,
            Stancakova,A., Stefansson,K., Steinbach,G., Steinthorsdottir,V.,
            Stirrups,K., Strawbridge,R.J., Stringham,H.M., Sun,Q., Suo,C.,
            Syvanen,A.C., Takayanagi,R., Takeuchi,F., Tay,W.T., Teslovich,T.M.,
            Thorand,B., Thorleifsson,G., Thorsteinsdottir,U., Tikkanen,E.,
            Trakalo,J., Tremoli,E., Trip,M.D., Tsai,F.J., Tuomi,T.,
            Tuomilehto,J., Uitterlinden,A.G., Valladares-Salgado,A.,
            Vedantam,S., Veglia,F., Voight,B.F., Wang,C., Wareham,N.J.,
            Wennauer,R., Wickremasinghe,A.R., Wilsgaard,T., Wilson,J.F.,
            Wiltshire,S., Winckler,W., Wong,T.Y., Wood,A.R., Wu,J.Y., Wu,Y.,
            Yamamoto,K., Yamauchi,T., Yang,M., Yengo,L., Yokota,M., Young,R.,
            Zabaneh,D., Zhang,F., Zhang,R., Zheng,W., Zimmet,P.Z.,
            Altshuler,D., Bowden,D.W., Cho,Y.S., Cox,N.J., Cruz,M., Hanis,C.L.,
            Kooner,J., Lee,J.Y., Seielstad,M., Teo,Y.Y., Boehnke,M.,
            Parra,E.J., Chambers,J.C., Tai,E.S., McCarthy,M.I. and Morris,A.P.
  CONSRTM   DIAbetes Genetics Replication And Meta-analysis (DIAGRAM)
            Consortium; Asian Genetic Epidemiology Network Type 2 Diabetes
            (AGEN-T2D) Consortium; South Asian Type 2 Diabetes (SAT2D)
            Consortium; Mexican American Type 2 Diabetes (MAT2D) Consortium;
            Type 2 Diabetes Genetic Exploration by Nex-generation sequencing in
            muylti-Ethnic Samples (T2D-GENES) Consortium
  TITLE     Genome-wide trans-ancestry meta-analysis provides insight into the
            genetic architecture of type 2 diabetes susceptibility
  JOURNAL   Nat Genet 46 (3), 234-244 (2014)
   PUBMED   24509480
REFERENCE   6  (residues 1 to 293)
  AUTHORS   Hu,T., Guan,T. and Gerace,L.
  TITLE     Molecular and functional characterization of the p62 complex, an
            assembly of nuclear pore complex glycoproteins
  JOURNAL   J Cell Biol 134 (3), 589-601 (1996)
   PUBMED   8707840
REFERENCE   7  (residues 1 to 293)
  AUTHORS   Hartmann,E. and Prehn,S.
  TITLE     The N-terminal region of the alpha-subunit of the TRAP complex has
            a conserved cluster of negative charges
  JOURNAL   FEBS Lett 349 (3), 324-326 (1994)
   PUBMED   8050590
REFERENCE   8  (residues 1 to 293)
  AUTHORS   Hartmann,E., Gorlich,D., Kostka,S., Otto,A., Kraft,R., Knespel,S.,
            Burger,E., Rapoport,T.A. and Prehn,S.
  TITLE     A tetrameric complex of membrane proteins in the endoplasmic
            reticulum
  JOURNAL   Eur J Biochem 214 (2), 375-381 (1993)
   PUBMED   7916687
REFERENCE   9  (residues 1 to 293)
  AUTHORS   Wei,M.L. and Cresswell,P.
  TITLE     HLA-A2 molecules in an antigen-processing mutant cell contain
            signal sequence-derived peptides
  JOURNAL   Nature 356 (6368), 443-446 (1992)
   PUBMED   1557127
REFERENCE   10 (residues 1 to 293)
  AUTHORS   Vogel,F., Hartmann,E., Gorlich,D. and Rapoport,T.A.
  TITLE     Segregation of the signal sequence receptor protein in the rough
            endoplasmic reticulum membrane
  JOURNAL   Eur J Cell Biol 53 (2), 197-202 (1990)
   PUBMED   1964414
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139095.15.
            
            Summary: The signal sequence receptor (SSR) is a glycosylated
            endoplasmic reticulum (ER) membrane receptor associated with
            protein translocation across the ER membrane. The SSR consists of 2
            subunits, a 34-kD glycoprotein encoded by this gene and a 22-kD
            glycoprotein. This gene generates several mRNA species as a result
            of complex alternative polyadenylation. This gene is unusual in
            that it utilizes arrays of polyA signal sequences that are mostly
            non-canonical. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, May
            2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3055608.1,
                                           SRR18074969.1293165.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.3"
     Protein         1..293
                     /product="translocon-associated protein subunit alpha
                     isoform 3 precursor"
                     /note="TRAP alpha; translocon-associated protein subunit
                     alpha; translocon-associated protein alpha subunit; SSR
                     alpha subunit; SSR-alpha; signal sequence receptor subunit
                     alpha; signal sequence receptor, alpha"
                     /calculated_mol_wt=30793
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2452
     Region          14..285
                     /region_name="TRAP_alpha"
                     /note="Translocon-associated protein (TRAP), alpha
                     subunit; pfam03896"
                     /db_xref="CDD:461085"
     Region          39..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43307.3)"
     Site            136
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P43307.3)"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P43307.3)"
     Site            208..228
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43307.3)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P43307.3)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P43307.3)"
     Region          261..286
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43307.3)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P43307.3)"
     CDS             1..293
                     /gene="SSR1"
                     /gene_synonym="TRAPA"
                     /coded_by="NM_001444973.1:80..961"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:6745"
                     /db_xref="HGNC:HGNC:11323"
                     /db_xref="MIM:600868"
ORIGIN      
        1 mrllprllll lllvfpatvl frggprglla vaqdltedee tvedsiiede ddeaeveede
       61 ptdlvedkee edvsgepeas psadttilfv kgedfpanni vkflvgftnk gtedfivesl
      121 dasfrypqdy qfyiqnftal plntvvppqr qatfeysfip aepmggrpfg lvinlnykdl
      181 ngnvfqdavf nqtvtviere dgldgetifm ymflaglgll vivglhqlle srkrkrpiqk
      241 vemgtssqnd vdmswipqet lnqinkaspr rlprkraqkr svgsderrrr eth
//
LOCUS       NP_001431909             424 aa            linear   PRI 05-JAN-2026
DEFINITION  aldehyde dehydrogenase family 3 member A2 isoform 3 [Homo sapiens].
ACCESSION   NP_001431909 XP_047291578 XP_054171453
VERSION     NP_001431909.1
DBSOURCE    REFSEQ: accession NM_001444980.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Dong,H., He,L., Sun,Q., Zhan,J., Li,J., Xiong,X., Zhuang,L., Wu,S.,
            Li,Y., Yin,C. and He,Q.
  TITLE     Inhibit ALDH3A2 reduce ovarian cancer cells survival via elevating
            ferroptosis sensitivity
  JOURNAL   Gene 876, 147515 (2023)
   PUBMED   37247796
  REMARK    GeneRIF: Inhibit ALDH3A2 reduce ovarian cancer cells survival via
            elevating ferroptosis sensitivity.
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Rajeshwari,M., Karthi,S., Singh,R., Efthymiou,S., Gowda,V.K.,
            Varalakshmi,P., Srinivasan,V.M., Houlden,H., Keller,M.A.,
            Rizzo,W.B. and Ashokkumar,B.
  TITLE     Novel ALDH3A2 mutations in structural and functional domains of
            FALDH causing diverse clinical phenotypes in Sjogren-Larsson
            syndrome patients
  JOURNAL   Hum Mutat 42 (8), 1015-1029 (2021)
   PUBMED   34082469
  REMARK    GeneRIF: Novel ALDH3A2 mutations in structural and functional
            domains of FALDH causing diverse clinical phenotypes in
            Sjogren-Larsson syndrome patients.
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Yin,Z., Wu,D., Shi,J., Wei,X., Jin,N., Lu,X. and Ren,X.
  TITLE     Identification of ALDH3A2 as a novel prognostic biomarker in
            gastric adenocarcinoma using integrated bioinformatics analysis
  JOURNAL   BMC Cancer 20 (1), 1062 (2020)
   PUBMED   33148208
  REMARK    GeneRIF: Identification of ALDH3A2 as a novel prognostic biomarker
            in gastric adenocarcinoma using integrated bioinformatics analysis.
            Erratum:[BMC Cancer. 2020 Nov 24;20(1):1141. doi:
            10.1186/s12885-020-07659-7. PMID: 33234125]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Abidi,K.T., Kamal,N.M., Bakkar,A. AA, Alotaibi,M., Asseri,H. and
            Bokari,K.A.
  TITLE     Sjogren-Larsson Syndrome: A case series of five members from an
            extended family with a novel mutation
  JOURNAL   Mol Genet Genomic Med 8 (11), e1487 (2020)
   PUBMED   32930514
  REMARK    GeneRIF: Sjogren-Larsson Syndrome: A case series of five members
            from an extended family with a novel mutation.
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Rogers,G.R., Markova,N.G., De Laurenzi,V., Rizzo,W.B. and
            Compton,J.G.
  TITLE     Genomic organization and expression of the human fatty aldehyde
            dehydrogenase gene (FALDH)
  JOURNAL   Genomics 39 (2), 127-135 (1997)
   PUBMED   9027499
REFERENCE   6  (residues 1 to 424)
  AUTHORS   De Laurenzi,V., Rogers,G.R., Hamrock,D.J., Marekov,L.N.,
            Steinert,P.M., Compton,J.G., Markova,N. and Rizzo,W.B.
  TITLE     Sjogren-Larsson syndrome is caused by mutations in the fatty
            aldehyde dehydrogenase gene
  JOURNAL   Nat Genet 12 (1), 52-57 (1996)
   PUBMED   8528251
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Rogers,G.R., Rizzo,W.B., Zlotogorski,A., Hashem,N., Lee,M.,
            Compton,J.G. and Bale,S.J.
  TITLE     Genetic homogeneity in Sjogren-Larsson syndrome: linkage to
            chromosome 17p in families of different non-Swedish ethnic origins
  JOURNAL   Am J Hum Genet 57 (5), 1123-1129 (1995)
   PUBMED   7485163
REFERENCE   8  (residues 1 to 424)
  AUTHORS   Pigg,M., Jagell,S., Sillen,A., Weissenbach,J., Gustavson,K.H. and
            Wadelius,C.
  TITLE     The Sjogren-Larsson syndrome gene is close to D17S805 as determined
            by linkage analysis and allelic association
  JOURNAL   Nat Genet 8 (4), 361-364 (1994)
   PUBMED   7894487
  REMARK    Erratum:[Nat Genet 1995 Apr;9(4):451]
REFERENCE   9  (residues 1 to 424)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC115989.6 and AC005722.1.
            
            On or before Jan 5, 2026 this sequence version replaced
            XP_047291578.1, XP_054171453.1.
            
            Summary: Aldehyde dehydrogenase isozymes are thought to play a
            major role in the detoxification of aldehydes generated by alcohol
            metabolism and lipid peroxidation. This gene product catalyzes the
            oxidation of long-chain aliphatic aldehydes to fatty acid.
            Mutations in the gene cause Sjogren-Larsson syndrome. Alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.101827.1,
                                           SRR18074967.3247224.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..424
                     /product="aldehyde dehydrogenase family 3 member A2
                     isoform 3"
                     /EC_number="1.2.1.3"
                     /EC_number="1.2.1.94"
                     /note="aldehyde dehydrogenase 10; fatty aldehyde
                     dehydrogenase; microsomal aldehyde dehydrogenase; aldehyde
                     dehydrogenase family 3 member A2"
                     /calculated_mol_wt=47756
     Region          5..403
                     /region_name="ALDH-SF"
                     /note="NAD(P)+-dependent aldehyde dehydrogenase
                     superfamily; cl11961"
                     /db_xref="CDD:448367"
     Site            order(108..112,120,135,137..138,183..186,189,192..193,
                     207..209,241,331,333,359,399)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:143450"
     Site            order(112,207,238,241)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:143450"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51648.1)"
     CDS             1..424
                     /gene="ALDH3A2"
                     /gene_synonym="ALDH10; FALDH; SLS"
                     /coded_by="NM_001444980.1:222..1496"
                     /note="isoform 3 is encoded by transcript variant 9"
                     /db_xref="GeneID:224"
                     /db_xref="HGNC:HGNC:403"
                     /db_xref="MIM:609523"
ORIGIN      
        1 melevrrvrq aflsgrsrpl rfrlqqleal rrmvqerekd iltaiaadlc ksefnvysqe
       61 vitvlgeidf mlenlpewvt akpvkknvlt mldeayiqpq plgvvliiga wnypfvltiq
      121 pligaiaagn aviikpsels entakilakl lpqyldqdly ivinggveet tellkqrfdh
      181 ifytgntavg kivmeaaakh ltpvtlelgg kspcyidkdc dldivcrrit wgkymncgqt
      241 ciapdyilce aslqnqivwk iketvkefyg enikespdye riinlrhfkr ilsllegqki
      301 afggetdeat ryiaptvltd vdpktkvmqe eifgpilpiv pvknvdeain finerekpla
      361 lyvfshnhkl ikrmidetss ggvtgndvim hftlnsfpfg gvgrillknd pvqppsaste
      421 lflf
//
LOCUS       NP_001014796             855 aa            linear   PRI 05-JAN-2026
DEFINITION  discoidin domain-containing receptor 2 precursor [Homo sapiens].
ACCESSION   NP_001014796 XP_005245279
VERSION     NP_001014796.1
DBSOURCE    REFSEQ: accession NM_001014796.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Audun Klingen,T., Chen,Y., Aas,H. and Akslen,L.A.
  TITLE     DDR2 expression in breast cancer is associated with blood vessel
            invasion, basal-like tumors, tumor associated macrophages,
            regulatory T cells, detection mode and prognosis
  JOURNAL   Hum Pathol 150, 29-35 (2024)
   PUBMED   38914168
  REMARK    GeneRIF: DDR2 expression in breast cancer is associated with blood
            vessel invasion, basal-like tumors, tumor associated macrophages,
            regulatory T cells, detection mode and prognosis.
REFERENCE   2  (residues 1 to 855)
  AUTHORS   Vessella,T., Xiang,S., Xiao,C., Stilwell,M., Fok,J., Shohet,J.,
            Rozen,E., Zhou,H.S. and Wen,Q.
  TITLE     DDR2 signaling and mechanosensing orchestrate neuroblastoma cell
            fate through different transcriptome mechanisms
  JOURNAL   FEBS Open Bio 14 (5), 867-882 (2024)
   PUBMED   38538106
  REMARK    GeneRIF: DDR2 signaling and mechanosensing orchestrate
            neuroblastoma cell fate through different transcriptome mechanisms.
REFERENCE   3  (residues 1 to 855)
  AUTHORS   Zhi,D., Zhou,K., Liu,S., Yu,W., Dong,M. and Yan,C.
  TITLE     METTL3/YTHDF1 m6A axis promotes tumorigenesis by enhancing DDR2
            expression in ovarian cancer
  JOURNAL   Pathol Res Pract 253, 155047 (2024)
   PUBMED   38154356
  REMARK    GeneRIF: METTL3/YTHDF1 m[6]A axis promotes tumorigenesis by
            enhancing DDR2 expression in ovarian cancer.
REFERENCE   4  (residues 1 to 855)
  AUTHORS   Akinjiyan,F.A., Ibitoye,Z., Zhao,P., Shriver,L.P., Patti,G.J.,
            Longmore,G.D. and Fuh,K.C.
  TITLE     DDR2-regulated arginase activity in ovarian cancer-associated
            fibroblasts promotes collagen production and tumor progression
  JOURNAL   Oncogene 43 (3), 189-201 (2024)
   PUBMED   37996700
  REMARK    GeneRIF: DDR2-regulated arginase activity in ovarian
            cancer-associated fibroblasts promotes collagen production and
            tumor progression.
REFERENCE   5  (residues 1 to 855)
  AUTHORS   Mitchell,A.V., Wu,J., Meng,F., Dong,L., Block,C.J., Song,W.M.,
            Zhang,B., Li,J. and Wu,G.
  TITLE     DDR2 coordinates EMT and metabolic reprogramming as a shared
            effector of FOXQ1 and SNAI1
  JOURNAL   Cancer Res Commun 2 (11), 1388-1403 (2022)
   PUBMED   36713812
  REMARK    GeneRIF: DDR2 coordinates EMT and metabolic reprogramming as a
            shared effector of FOXQ1 and SNAI1.
REFERENCE   6  (residues 1 to 855)
  AUTHORS   Mohan,R.R., Mohan,R.R. and Wilson,S.E.
  TITLE     Discoidin domain receptor (DDR) 1 and 2: collagen-activated
            tyrosine kinase receptors in the cornea
  JOURNAL   Exp Eye Res 72 (1), 87-92 (2001)
   PUBMED   11133186
REFERENCE   7  (residues 1 to 855)
  AUTHORS   Vogel,W., Gish,G.D., Alves,F. and Pawson,T.
  TITLE     The discoidin domain receptor tyrosine kinases are activated by
            collagen
  JOURNAL   Mol Cell 1 (1), 13-23 (1997)
   PUBMED   9659899
REFERENCE   8  (residues 1 to 855)
  AUTHORS   Karn,T., Holtrich,U., Brauninger,A., Bohme,B., Wolf,G.,
            Rubsamen-Waigmann,H. and Strebhardt,K.
  TITLE     Structure, expression and chromosomal mapping of TKT from man and
            mouse: a new subclass of receptor tyrosine kinases with a factor
            VIII-like domain
  JOURNAL   Oncogene 8 (12), 3433-3440 (1993)
   PUBMED   8247548
REFERENCE   9  (residues 1 to 855)
  AUTHORS   Abedinia,M., Layfield,R., Jones,S.M., Nixon,P.F. and Mattick,J.S.
  TITLE     Nucleotide and predicted amino acid sequence of a cDNA clone
            encoding part of human transketolase
  JOURNAL   Biochem Biophys Res Commun 183 (3), 1159-1166 (1992)
   PUBMED   1567394
REFERENCE   10 (residues 1 to 855)
  AUTHORS   Lapsys,N.M., Layfield,R., Baker,E., Callen,D.F., Sutherland,G.R.,
            Abedinia,M., Nixon,P.F. and Mattick,J.S.
  TITLE     Chromosomal location of the human transketolase gene
  JOURNAL   Cytogenet Cell Genet 61 (4), 274-275 (1992)
   PUBMED   1486804
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA852104.1, BC052998.2,
            AL596325.5, AL445197.4 and BX537651.1.
            
            On Aug 31, 2013 this sequence version replaced XP_005245279.1.
            
            Summary: This gene encodes a member of the discoidin domain
            receptor subclass of the receptor tyrosine kinase (RTKs) protein
            family. RTKs play a key role in the communication of cells with
            their microenvironment. The encoded protein is a collagen-induced
            receptor that activates signal transduction pathways involved in
            cell adhesion, proliferation, and extracellular matrix remodeling.
            This protein is expressed in numerous cell types and may alos be
            involved in wound repair and regulate tumor growth and
            invasiveness. Mutations in this gene are the cause of short
            limb-hand type spondylometaepiphyseal dysplasia. [provided by
            RefSeq, Aug 2017].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1-4 encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX640899.1, AK095975.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..855
                     /product="discoidin domain-containing receptor 2
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="neurotrophic tyrosine kinase receptor related 3;
                     discoidin domain receptor family, member 2;
                     hydroxyaryl-protein kinase; cell migration-inducing
                     protein 20; migration-inducing gene 16 protein;
                     tyrosine-protein kinase TYRO10; CD167 antigen-like family
                     member B; receptor protein-tyrosine kinase TKT; discoidin
                     domain-containing receptor tyrosine kinase 2; discoidin
                     domain receptor 2; discoidin domain-containing receptor 2"
                     /calculated_mol_wt=94388
     sig_peptide     1..21
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
                     /calculated_mol_wt=2367
     mat_peptide     22..855
                     /product="Discoidin domain-containing receptor 2.
                     /id=PRO_0000016746"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16832.2)"
                     /calculated_mol_wt=94388
     Region          32..184
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Site            order(73,105,113)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            213
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            261
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            372
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            400..421
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16832.2)"
     Region          452..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16832.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q62371; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Region          557..851
                     /region_name="PTKc_DDR2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Discoidin Domain Receptor 2; cd05095"
                     /db_xref="CDD:270677"
     Site            order(569..573,577,606,608,654..657,660..661,710,714..715,
                     717,728,746..750,759,794)
                     /site_type="active"
                     /db_xref="CDD:270677"
     Site            order(569..570,572..573,577,606,608,654..657,660..661,
                     714..715,717,728)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270677"
     Site            order(710,714,746..750,759,794)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270677"
     Site            727..752
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270677"
     Site            736
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000269|PubMed:16186108; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000269|PubMed:16186108; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            741
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000269|PubMed:16186108; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     CDS             1..855
                     /gene="DDR2"
                     /gene_synonym="DDR2-N; MIG20a; NTRKR3; TKT; TYRO10; WRCN"
                     /coded_by="NM_001014796.3:440..3007"
                     /db_xref="CCDS:CCDS1241.1"
                     /db_xref="GeneID:4921"
                     /db_xref="HGNC:HGNC:2731"
                     /db_xref="MIM:191311"
ORIGIN      
        1 miliprmllv lflllpilss akaqvnpaic ryplgmsggq ipdeditass qwsestaaky
       61 grldseegdg awcpeipvep ddlkeflqid lhtlhfitlv gtqgrhaggh giefapmyki
      121 nysrdgtrwi swrnrhgkqv ldgnsnpydi flkdleppiv arfvrfipvt dhsmnvcmrv
      181 elygcvwldg lvsynapagq qfvlpggsii ylndsvydga vgysmteglg qltdgvsgld
      241 dftqtheyhv wpgydyvgwr nesatngyie imfefdrirn fttmkvhcnn mfakgvkifk
      301 evqcyfrsea sewepnaisf plvlddvnps arfvtvplhh rmasaikcqy hfadtwmmfs
      361 eitfqsdaam ynnsealpts pmapttydpm lkvddsntri ligclvaiif illaiiviil
      421 wrqfwqkmle kasrrmldde mtvslslpsd ssmfnnnrss spseqgsnst ydrifplrpd
      481 yqepsrlirk lpefapgeee sgcsgvvkpv qpsgpegvph yaeadivnlq gvtggntysv
      541 pavtmdllsg kdvaveefpr klltfkeklg egqfgevhlc evegmekfkd kdfaldvsan
      601 qpvlvavkml radanknarn dflkeikims rlkdpniihl lavcitddpl cmiteymeng
      661 dlnqflsrhe ppnssssdvr tvsytnlkfm atqiasgmky lsslnfvhrd latrnclvgk
      721 nytikiadfg msrnlysgdy yriqgravlp irwmswesil lgkfttasdv wafgvtlwet
      781 ftfcqeqpys qlsdeqvien tgeffrdqgr qtylpqpaic pdsvyklmls cwrrdtknrp
      841 sfqeihllll qqgde
//
LOCUS       NP_001341912             855 aa            linear   PRI 05-JAN-2026
DEFINITION  discoidin domain-containing receptor 2 precursor [Homo sapiens].
ACCESSION   NP_001341912
VERSION     NP_001341912.1
DBSOURCE    REFSEQ: accession NM_001354983.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Audun Klingen,T., Chen,Y., Aas,H. and Akslen,L.A.
  TITLE     DDR2 expression in breast cancer is associated with blood vessel
            invasion, basal-like tumors, tumor associated macrophages,
            regulatory T cells, detection mode and prognosis
  JOURNAL   Hum Pathol 150, 29-35 (2024)
   PUBMED   38914168
  REMARK    GeneRIF: DDR2 expression in breast cancer is associated with blood
            vessel invasion, basal-like tumors, tumor associated macrophages,
            regulatory T cells, detection mode and prognosis.
REFERENCE   2  (residues 1 to 855)
  AUTHORS   Vessella,T., Xiang,S., Xiao,C., Stilwell,M., Fok,J., Shohet,J.,
            Rozen,E., Zhou,H.S. and Wen,Q.
  TITLE     DDR2 signaling and mechanosensing orchestrate neuroblastoma cell
            fate through different transcriptome mechanisms
  JOURNAL   FEBS Open Bio 14 (5), 867-882 (2024)
   PUBMED   38538106
  REMARK    GeneRIF: DDR2 signaling and mechanosensing orchestrate
            neuroblastoma cell fate through different transcriptome mechanisms.
REFERENCE   3  (residues 1 to 855)
  AUTHORS   Zhi,D., Zhou,K., Liu,S., Yu,W., Dong,M. and Yan,C.
  TITLE     METTL3/YTHDF1 m6A axis promotes tumorigenesis by enhancing DDR2
            expression in ovarian cancer
  JOURNAL   Pathol Res Pract 253, 155047 (2024)
   PUBMED   38154356
  REMARK    GeneRIF: METTL3/YTHDF1 m[6]A axis promotes tumorigenesis by
            enhancing DDR2 expression in ovarian cancer.
REFERENCE   4  (residues 1 to 855)
  AUTHORS   Akinjiyan,F.A., Ibitoye,Z., Zhao,P., Shriver,L.P., Patti,G.J.,
            Longmore,G.D. and Fuh,K.C.
  TITLE     DDR2-regulated arginase activity in ovarian cancer-associated
            fibroblasts promotes collagen production and tumor progression
  JOURNAL   Oncogene 43 (3), 189-201 (2024)
   PUBMED   37996700
  REMARK    GeneRIF: DDR2-regulated arginase activity in ovarian
            cancer-associated fibroblasts promotes collagen production and
            tumor progression.
REFERENCE   5  (residues 1 to 855)
  AUTHORS   Mitchell,A.V., Wu,J., Meng,F., Dong,L., Block,C.J., Song,W.M.,
            Zhang,B., Li,J. and Wu,G.
  TITLE     DDR2 coordinates EMT and metabolic reprogramming as a shared
            effector of FOXQ1 and SNAI1
  JOURNAL   Cancer Res Commun 2 (11), 1388-1403 (2022)
   PUBMED   36713812
  REMARK    GeneRIF: DDR2 coordinates EMT and metabolic reprogramming as a
            shared effector of FOXQ1 and SNAI1.
REFERENCE   6  (residues 1 to 855)
  AUTHORS   Mohan,R.R., Mohan,R.R. and Wilson,S.E.
  TITLE     Discoidin domain receptor (DDR) 1 and 2: collagen-activated
            tyrosine kinase receptors in the cornea
  JOURNAL   Exp Eye Res 72 (1), 87-92 (2001)
   PUBMED   11133186
REFERENCE   7  (residues 1 to 855)
  AUTHORS   Vogel,W., Gish,G.D., Alves,F. and Pawson,T.
  TITLE     The discoidin domain receptor tyrosine kinases are activated by
            collagen
  JOURNAL   Mol Cell 1 (1), 13-23 (1997)
   PUBMED   9659899
REFERENCE   8  (residues 1 to 855)
  AUTHORS   Karn,T., Holtrich,U., Brauninger,A., Bohme,B., Wolf,G.,
            Rubsamen-Waigmann,H. and Strebhardt,K.
  TITLE     Structure, expression and chromosomal mapping of TKT from man and
            mouse: a new subclass of receptor tyrosine kinases with a factor
            VIII-like domain
  JOURNAL   Oncogene 8 (12), 3433-3440 (1993)
   PUBMED   8247548
REFERENCE   9  (residues 1 to 855)
  AUTHORS   Abedinia,M., Layfield,R., Jones,S.M., Nixon,P.F. and Mattick,J.S.
  TITLE     Nucleotide and predicted amino acid sequence of a cDNA clone
            encoding part of human transketolase
  JOURNAL   Biochem Biophys Res Commun 183 (3), 1159-1166 (1992)
   PUBMED   1567394
REFERENCE   10 (residues 1 to 855)
  AUTHORS   Lapsys,N.M., Layfield,R., Baker,E., Callen,D.F., Sutherland,G.R.,
            Abedinia,M., Nixon,P.F. and Mattick,J.S.
  TITLE     Chromosomal location of the human transketolase gene
  JOURNAL   Cytogenet Cell Genet 61 (4), 274-275 (1992)
   PUBMED   1486804
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596325.5, DA919943.1,
            AL445197.4 and BX537651.1.
            
            Summary: This gene encodes a member of the discoidin domain
            receptor subclass of the receptor tyrosine kinase (RTKs) protein
            family. RTKs play a key role in the communication of cells with
            their microenvironment. The encoded protein is a collagen-induced
            receptor that activates signal transduction pathways involved in
            cell adhesion, proliferation, and extracellular matrix remodeling.
            This protein is expressed in numerous cell types and may alos be
            involved in wound repair and regulate tumor growth and
            invasiveness. Mutations in this gene are the cause of short
            limb-hand type spondylometaepiphyseal dysplasia. [provided by
            RefSeq, Aug 2017].
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. Variants 1-4 encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.69091.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..855
                     /product="discoidin domain-containing receptor 2
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="neurotrophic tyrosine kinase receptor related 3;
                     discoidin domain receptor family, member 2;
                     hydroxyaryl-protein kinase; cell migration-inducing
                     protein 20; migration-inducing gene 16 protein;
                     tyrosine-protein kinase TYRO10; CD167 antigen-like family
                     member B; receptor protein-tyrosine kinase TKT; discoidin
                     domain-containing receptor tyrosine kinase 2; discoidin
                     domain receptor 2; discoidin domain-containing receptor 2"
                     /calculated_mol_wt=94388
     sig_peptide     1..21
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
                     /calculated_mol_wt=2367
     mat_peptide     22..855
                     /product="Discoidin domain-containing receptor 2.
                     /id=PRO_0000016746"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16832.2)"
                     /calculated_mol_wt=94388
     Region          32..184
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Site            order(73,105,113)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            213
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            261
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            372
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            400..421
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16832.2)"
     Region          452..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16832.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q62371; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Region          557..851
                     /region_name="PTKc_DDR2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Discoidin Domain Receptor 2; cd05095"
                     /db_xref="CDD:270677"
     Site            order(569..573,577,606,608,654..657,660..661,710,714..715,
                     717,728,746..750,759,794)
                     /site_type="active"
                     /db_xref="CDD:270677"
     Site            order(569..570,572..573,577,606,608,654..657,660..661,
                     714..715,717,728)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270677"
     Site            order(710,714,746..750,759,794)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270677"
     Site            727..752
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270677"
     Site            736
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000269|PubMed:16186108; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000269|PubMed:16186108; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            741
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000269|PubMed:16186108; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     CDS             1..855
                     /gene="DDR2"
                     /gene_synonym="DDR2-N; MIG20a; NTRKR3; TKT; TYRO10; WRCN"
                     /coded_by="NM_001354983.2:777..3344"
                     /db_xref="CCDS:CCDS1241.1"
                     /db_xref="GeneID:4921"
                     /db_xref="HGNC:HGNC:2731"
                     /db_xref="MIM:191311"
ORIGIN      
        1 miliprmllv lflllpilss akaqvnpaic ryplgmsggq ipdeditass qwsestaaky
       61 grldseegdg awcpeipvep ddlkeflqid lhtlhfitlv gtqgrhaggh giefapmyki
      121 nysrdgtrwi swrnrhgkqv ldgnsnpydi flkdleppiv arfvrfipvt dhsmnvcmrv
      181 elygcvwldg lvsynapagq qfvlpggsii ylndsvydga vgysmteglg qltdgvsgld
      241 dftqtheyhv wpgydyvgwr nesatngyie imfefdrirn fttmkvhcnn mfakgvkifk
      301 evqcyfrsea sewepnaisf plvlddvnps arfvtvplhh rmasaikcqy hfadtwmmfs
      361 eitfqsdaam ynnsealpts pmapttydpm lkvddsntri ligclvaiif illaiiviil
      421 wrqfwqkmle kasrrmldde mtvslslpsd ssmfnnnrss spseqgsnst ydrifplrpd
      481 yqepsrlirk lpefapgeee sgcsgvvkpv qpsgpegvph yaeadivnlq gvtggntysv
      541 pavtmdllsg kdvaveefpr klltfkeklg egqfgevhlc evegmekfkd kdfaldvsan
      601 qpvlvavkml radanknarn dflkeikims rlkdpniihl lavcitddpl cmiteymeng
      661 dlnqflsrhe ppnssssdvr tvsytnlkfm atqiasgmky lsslnfvhrd latrnclvgk
      721 nytikiadfg msrnlysgdy yriqgravlp irwmswesil lgkfttasdv wafgvtlwet
      781 ftfcqeqpys qlsdeqvien tgeffrdqgr qtylpqpaic pdsvyklmls cwrrdtknrp
      841 sfqeihllll qqgde
//
LOCUS       NP_006173                855 aa            linear   PRI 05-JAN-2026
DEFINITION  discoidin domain-containing receptor 2 precursor [Homo sapiens].
ACCESSION   NP_006173
VERSION     NP_006173.2
DBSOURCE    REFSEQ: accession NM_006182.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Audun Klingen,T., Chen,Y., Aas,H. and Akslen,L.A.
  TITLE     DDR2 expression in breast cancer is associated with blood vessel
            invasion, basal-like tumors, tumor associated macrophages,
            regulatory T cells, detection mode and prognosis
  JOURNAL   Hum Pathol 150, 29-35 (2024)
   PUBMED   38914168
  REMARK    GeneRIF: DDR2 expression in breast cancer is associated with blood
            vessel invasion, basal-like tumors, tumor associated macrophages,
            regulatory T cells, detection mode and prognosis.
REFERENCE   2  (residues 1 to 855)
  AUTHORS   Vessella,T., Xiang,S., Xiao,C., Stilwell,M., Fok,J., Shohet,J.,
            Rozen,E., Zhou,H.S. and Wen,Q.
  TITLE     DDR2 signaling and mechanosensing orchestrate neuroblastoma cell
            fate through different transcriptome mechanisms
  JOURNAL   FEBS Open Bio 14 (5), 867-882 (2024)
   PUBMED   38538106
  REMARK    GeneRIF: DDR2 signaling and mechanosensing orchestrate
            neuroblastoma cell fate through different transcriptome mechanisms.
REFERENCE   3  (residues 1 to 855)
  AUTHORS   Zhi,D., Zhou,K., Liu,S., Yu,W., Dong,M. and Yan,C.
  TITLE     METTL3/YTHDF1 m6A axis promotes tumorigenesis by enhancing DDR2
            expression in ovarian cancer
  JOURNAL   Pathol Res Pract 253, 155047 (2024)
   PUBMED   38154356
  REMARK    GeneRIF: METTL3/YTHDF1 m[6]A axis promotes tumorigenesis by
            enhancing DDR2 expression in ovarian cancer.
REFERENCE   4  (residues 1 to 855)
  AUTHORS   Akinjiyan,F.A., Ibitoye,Z., Zhao,P., Shriver,L.P., Patti,G.J.,
            Longmore,G.D. and Fuh,K.C.
  TITLE     DDR2-regulated arginase activity in ovarian cancer-associated
            fibroblasts promotes collagen production and tumor progression
  JOURNAL   Oncogene 43 (3), 189-201 (2024)
   PUBMED   37996700
  REMARK    GeneRIF: DDR2-regulated arginase activity in ovarian
            cancer-associated fibroblasts promotes collagen production and
            tumor progression.
REFERENCE   5  (residues 1 to 855)
  AUTHORS   Mitchell,A.V., Wu,J., Meng,F., Dong,L., Block,C.J., Song,W.M.,
            Zhang,B., Li,J. and Wu,G.
  TITLE     DDR2 coordinates EMT and metabolic reprogramming as a shared
            effector of FOXQ1 and SNAI1
  JOURNAL   Cancer Res Commun 2 (11), 1388-1403 (2022)
   PUBMED   36713812
  REMARK    GeneRIF: DDR2 coordinates EMT and metabolic reprogramming as a
            shared effector of FOXQ1 and SNAI1.
REFERENCE   6  (residues 1 to 855)
  AUTHORS   Mohan,R.R., Mohan,R.R. and Wilson,S.E.
  TITLE     Discoidin domain receptor (DDR) 1 and 2: collagen-activated
            tyrosine kinase receptors in the cornea
  JOURNAL   Exp Eye Res 72 (1), 87-92 (2001)
   PUBMED   11133186
REFERENCE   7  (residues 1 to 855)
  AUTHORS   Vogel,W., Gish,G.D., Alves,F. and Pawson,T.
  TITLE     The discoidin domain receptor tyrosine kinases are activated by
            collagen
  JOURNAL   Mol Cell 1 (1), 13-23 (1997)
   PUBMED   9659899
REFERENCE   8  (residues 1 to 855)
  AUTHORS   Karn,T., Holtrich,U., Brauninger,A., Bohme,B., Wolf,G.,
            Rubsamen-Waigmann,H. and Strebhardt,K.
  TITLE     Structure, expression and chromosomal mapping of TKT from man and
            mouse: a new subclass of receptor tyrosine kinases with a factor
            VIII-like domain
  JOURNAL   Oncogene 8 (12), 3433-3440 (1993)
   PUBMED   8247548
REFERENCE   9  (residues 1 to 855)
  AUTHORS   Abedinia,M., Layfield,R., Jones,S.M., Nixon,P.F. and Mattick,J.S.
  TITLE     Nucleotide and predicted amino acid sequence of a cDNA clone
            encoding part of human transketolase
  JOURNAL   Biochem Biophys Res Commun 183 (3), 1159-1166 (1992)
   PUBMED   1567394
REFERENCE   10 (residues 1 to 855)
  AUTHORS   Lapsys,N.M., Layfield,R., Baker,E., Callen,D.F., Sutherland,G.R.,
            Abedinia,M., Nixon,P.F. and Mattick,J.S.
  TITLE     Chromosomal location of the human transketolase gene
  JOURNAL   Cytogenet Cell Genet 61 (4), 274-275 (1992)
   PUBMED   1486804
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA852104.1, AK314388.1,
            AL596325.5, AL445197.4 and BX537651.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 8, 2005 this sequence version replaced NP_006173.1.
            
            Summary: This gene encodes a member of the discoidin domain
            receptor subclass of the receptor tyrosine kinase (RTKs) protein
            family. RTKs play a key role in the communication of cells with
            their microenvironment. The encoded protein is a collagen-induced
            receptor that activates signal transduction pathways involved in
            cell adhesion, proliferation, and extracellular matrix remodeling.
            This protein is expressed in numerous cell types and may alos be
            involved in wound repair and regulate tumor growth and
            invasiveness. Mutations in this gene are the cause of short
            limb-hand type spondylometaepiphyseal dysplasia. [provided by
            RefSeq, Aug 2017].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1-4 encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.185646.1,
                                           SRR1803613.136417.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367921.8/ ENSP00000356898.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..855
                     /product="discoidin domain-containing receptor 2
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="neurotrophic tyrosine kinase receptor related 3;
                     discoidin domain receptor family, member 2;
                     hydroxyaryl-protein kinase; cell migration-inducing
                     protein 20; migration-inducing gene 16 protein;
                     tyrosine-protein kinase TYRO10; CD167 antigen-like family
                     member B; receptor protein-tyrosine kinase TKT; discoidin
                     domain-containing receptor tyrosine kinase 2; discoidin
                     domain receptor 2; discoidin domain-containing receptor 2"
                     /calculated_mol_wt=94388
     sig_peptide     1..21
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
                     /calculated_mol_wt=2367
     mat_peptide     22..855
                     /product="Discoidin domain-containing receptor 2.
                     /id=PRO_0000016746"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16832.2)"
                     /calculated_mol_wt=94388
     Region          32..184
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Site            order(73,105,113)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            213
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            261
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            372
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            400..421
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16832.2)"
     Region          452..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16832.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q62371; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Region          557..851
                     /region_name="PTKc_DDR2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Discoidin Domain Receptor 2; cd05095"
                     /db_xref="CDD:270677"
     Site            order(569..573,577,606,608,654..657,660..661,710,714..715,
                     717,728,746..750,759,794)
                     /site_type="active"
                     /db_xref="CDD:270677"
     Site            order(569..570,572..573,577,606,608,654..657,660..661,
                     714..715,717,728)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270677"
     Site            order(710,714,746..750,759,794)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270677"
     Site            727..752
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270677"
     Site            736
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000269|PubMed:16186108; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000269|PubMed:16186108; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            741
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000269|PubMed:16186108; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     CDS             1..855
                     /gene="DDR2"
                     /gene_synonym="DDR2-N; MIG20a; NTRKR3; TKT; TYRO10; WRCN"
                     /coded_by="NM_006182.4:360..2927"
                     /db_xref="CCDS:CCDS1241.1"
                     /db_xref="GeneID:4921"
                     /db_xref="HGNC:HGNC:2731"
                     /db_xref="MIM:191311"
ORIGIN      
        1 miliprmllv lflllpilss akaqvnpaic ryplgmsggq ipdeditass qwsestaaky
       61 grldseegdg awcpeipvep ddlkeflqid lhtlhfitlv gtqgrhaggh giefapmyki
      121 nysrdgtrwi swrnrhgkqv ldgnsnpydi flkdleppiv arfvrfipvt dhsmnvcmrv
      181 elygcvwldg lvsynapagq qfvlpggsii ylndsvydga vgysmteglg qltdgvsgld
      241 dftqtheyhv wpgydyvgwr nesatngyie imfefdrirn fttmkvhcnn mfakgvkifk
      301 evqcyfrsea sewepnaisf plvlddvnps arfvtvplhh rmasaikcqy hfadtwmmfs
      361 eitfqsdaam ynnsealpts pmapttydpm lkvddsntri ligclvaiif illaiiviil
      421 wrqfwqkmle kasrrmldde mtvslslpsd ssmfnnnrss spseqgsnst ydrifplrpd
      481 yqepsrlirk lpefapgeee sgcsgvvkpv qpsgpegvph yaeadivnlq gvtggntysv
      541 pavtmdllsg kdvaveefpr klltfkeklg egqfgevhlc evegmekfkd kdfaldvsan
      601 qpvlvavkml radanknarn dflkeikims rlkdpniihl lavcitddpl cmiteymeng
      661 dlnqflsrhe ppnssssdvr tvsytnlkfm atqiasgmky lsslnfvhrd latrnclvgk
      721 nytikiadfg msrnlysgdy yriqgravlp irwmswesil lgkfttasdv wafgvtlwet
      781 ftfcqeqpys qlsdeqvien tgeffrdqgr qtylpqpaic pdsvyklmls cwrrdtknrp
      841 sfqeihllll qqgde
//
LOCUS       NP_001341911             855 aa            linear   PRI 05-JAN-2026
DEFINITION  discoidin domain-containing receptor 2 precursor [Homo sapiens].
ACCESSION   NP_001341911
VERSION     NP_001341911.1
DBSOURCE    REFSEQ: accession NM_001354982.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Audun Klingen,T., Chen,Y., Aas,H. and Akslen,L.A.
  TITLE     DDR2 expression in breast cancer is associated with blood vessel
            invasion, basal-like tumors, tumor associated macrophages,
            regulatory T cells, detection mode and prognosis
  JOURNAL   Hum Pathol 150, 29-35 (2024)
   PUBMED   38914168
  REMARK    GeneRIF: DDR2 expression in breast cancer is associated with blood
            vessel invasion, basal-like tumors, tumor associated macrophages,
            regulatory T cells, detection mode and prognosis.
REFERENCE   2  (residues 1 to 855)
  AUTHORS   Vessella,T., Xiang,S., Xiao,C., Stilwell,M., Fok,J., Shohet,J.,
            Rozen,E., Zhou,H.S. and Wen,Q.
  TITLE     DDR2 signaling and mechanosensing orchestrate neuroblastoma cell
            fate through different transcriptome mechanisms
  JOURNAL   FEBS Open Bio 14 (5), 867-882 (2024)
   PUBMED   38538106
  REMARK    GeneRIF: DDR2 signaling and mechanosensing orchestrate
            neuroblastoma cell fate through different transcriptome mechanisms.
REFERENCE   3  (residues 1 to 855)
  AUTHORS   Zhi,D., Zhou,K., Liu,S., Yu,W., Dong,M. and Yan,C.
  TITLE     METTL3/YTHDF1 m6A axis promotes tumorigenesis by enhancing DDR2
            expression in ovarian cancer
  JOURNAL   Pathol Res Pract 253, 155047 (2024)
   PUBMED   38154356
  REMARK    GeneRIF: METTL3/YTHDF1 m[6]A axis promotes tumorigenesis by
            enhancing DDR2 expression in ovarian cancer.
REFERENCE   4  (residues 1 to 855)
  AUTHORS   Akinjiyan,F.A., Ibitoye,Z., Zhao,P., Shriver,L.P., Patti,G.J.,
            Longmore,G.D. and Fuh,K.C.
  TITLE     DDR2-regulated arginase activity in ovarian cancer-associated
            fibroblasts promotes collagen production and tumor progression
  JOURNAL   Oncogene 43 (3), 189-201 (2024)
   PUBMED   37996700
  REMARK    GeneRIF: DDR2-regulated arginase activity in ovarian
            cancer-associated fibroblasts promotes collagen production and
            tumor progression.
REFERENCE   5  (residues 1 to 855)
  AUTHORS   Mitchell,A.V., Wu,J., Meng,F., Dong,L., Block,C.J., Song,W.M.,
            Zhang,B., Li,J. and Wu,G.
  TITLE     DDR2 coordinates EMT and metabolic reprogramming as a shared
            effector of FOXQ1 and SNAI1
  JOURNAL   Cancer Res Commun 2 (11), 1388-1403 (2022)
   PUBMED   36713812
  REMARK    GeneRIF: DDR2 coordinates EMT and metabolic reprogramming as a
            shared effector of FOXQ1 and SNAI1.
REFERENCE   6  (residues 1 to 855)
  AUTHORS   Mohan,R.R., Mohan,R.R. and Wilson,S.E.
  TITLE     Discoidin domain receptor (DDR) 1 and 2: collagen-activated
            tyrosine kinase receptors in the cornea
  JOURNAL   Exp Eye Res 72 (1), 87-92 (2001)
   PUBMED   11133186
REFERENCE   7  (residues 1 to 855)
  AUTHORS   Vogel,W., Gish,G.D., Alves,F. and Pawson,T.
  TITLE     The discoidin domain receptor tyrosine kinases are activated by
            collagen
  JOURNAL   Mol Cell 1 (1), 13-23 (1997)
   PUBMED   9659899
REFERENCE   8  (residues 1 to 855)
  AUTHORS   Karn,T., Holtrich,U., Brauninger,A., Bohme,B., Wolf,G.,
            Rubsamen-Waigmann,H. and Strebhardt,K.
  TITLE     Structure, expression and chromosomal mapping of TKT from man and
            mouse: a new subclass of receptor tyrosine kinases with a factor
            VIII-like domain
  JOURNAL   Oncogene 8 (12), 3433-3440 (1993)
   PUBMED   8247548
REFERENCE   9  (residues 1 to 855)
  AUTHORS   Abedinia,M., Layfield,R., Jones,S.M., Nixon,P.F. and Mattick,J.S.
  TITLE     Nucleotide and predicted amino acid sequence of a cDNA clone
            encoding part of human transketolase
  JOURNAL   Biochem Biophys Res Commun 183 (3), 1159-1166 (1992)
   PUBMED   1567394
REFERENCE   10 (residues 1 to 855)
  AUTHORS   Lapsys,N.M., Layfield,R., Baker,E., Callen,D.F., Sutherland,G.R.,
            Abedinia,M., Nixon,P.F. and Mattick,J.S.
  TITLE     Chromosomal location of the human transketolase gene
  JOURNAL   Cytogenet Cell Genet 61 (4), 274-275 (1992)
   PUBMED   1486804
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596325.5, AL445197.4 and
            BX537651.1.
            
            Summary: This gene encodes a member of the discoidin domain
            receptor subclass of the receptor tyrosine kinase (RTKs) protein
            family. RTKs play a key role in the communication of cells with
            their microenvironment. The encoded protein is a collagen-induced
            receptor that activates signal transduction pathways involved in
            cell adhesion, proliferation, and extracellular matrix remodeling.
            This protein is expressed in numerous cell types and may alos be
            involved in wound repair and regulate tumor growth and
            invasiveness. Mutations in this gene are the cause of short
            limb-hand type spondylometaepiphyseal dysplasia. [provided by
            RefSeq, Aug 2017].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1-4 encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.156558.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..855
                     /product="discoidin domain-containing receptor 2
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="neurotrophic tyrosine kinase receptor related 3;
                     discoidin domain receptor family, member 2;
                     hydroxyaryl-protein kinase; cell migration-inducing
                     protein 20; migration-inducing gene 16 protein;
                     tyrosine-protein kinase TYRO10; CD167 antigen-like family
                     member B; receptor protein-tyrosine kinase TKT; discoidin
                     domain-containing receptor tyrosine kinase 2; discoidin
                     domain receptor 2; discoidin domain-containing receptor 2"
                     /calculated_mol_wt=94388
     sig_peptide     1..21
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
                     /calculated_mol_wt=2367
     mat_peptide     22..855
                     /product="Discoidin domain-containing receptor 2.
                     /id=PRO_0000016746"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16832.2)"
                     /calculated_mol_wt=94388
     Region          32..184
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Site            order(73,105,113)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            213
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            261
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            280
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            372
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            400..421
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16832.2)"
     Region          452..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16832.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q62371; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Region          557..851
                     /region_name="PTKc_DDR2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Discoidin Domain Receptor 2; cd05095"
                     /db_xref="CDD:270677"
     Site            order(569..573,577,606,608,654..657,660..661,710,714..715,
                     717,728,746..750,759,794)
                     /site_type="active"
                     /db_xref="CDD:270677"
     Site            order(569..570,572..573,577,606,608,654..657,660..661,
                     714..715,717,728)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270677"
     Site            order(710,714,746..750,759,794)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270677"
     Site            727..752
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270677"
     Site            736
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000269|PubMed:16186108; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000269|PubMed:16186108; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     Site            741
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC and autocatalysis.
                     /evidence=ECO:0000269|PubMed:16186108; propagated from
                     UniProtKB/Swiss-Prot (Q16832.2)"
     CDS             1..855
                     /gene="DDR2"
                     /gene_synonym="DDR2-N; MIG20a; NTRKR3; TKT; TYRO10; WRCN"
                     /coded_by="NM_001354982.2:311..2878"
                     /db_xref="CCDS:CCDS1241.1"
                     /db_xref="GeneID:4921"
                     /db_xref="HGNC:HGNC:2731"
                     /db_xref="MIM:191311"
ORIGIN      
        1 miliprmllv lflllpilss akaqvnpaic ryplgmsggq ipdeditass qwsestaaky
       61 grldseegdg awcpeipvep ddlkeflqid lhtlhfitlv gtqgrhaggh giefapmyki
      121 nysrdgtrwi swrnrhgkqv ldgnsnpydi flkdleppiv arfvrfipvt dhsmnvcmrv
      181 elygcvwldg lvsynapagq qfvlpggsii ylndsvydga vgysmteglg qltdgvsgld
      241 dftqtheyhv wpgydyvgwr nesatngyie imfefdrirn fttmkvhcnn mfakgvkifk
      301 evqcyfrsea sewepnaisf plvlddvnps arfvtvplhh rmasaikcqy hfadtwmmfs
      361 eitfqsdaam ynnsealpts pmapttydpm lkvddsntri ligclvaiif illaiiviil
      421 wrqfwqkmle kasrrmldde mtvslslpsd ssmfnnnrss spseqgsnst ydrifplrpd
      481 yqepsrlirk lpefapgeee sgcsgvvkpv qpsgpegvph yaeadivnlq gvtggntysv
      541 pavtmdllsg kdvaveefpr klltfkeklg egqfgevhlc evegmekfkd kdfaldvsan
      601 qpvlvavkml radanknarn dflkeikims rlkdpniihl lavcitddpl cmiteymeng
      661 dlnqflsrhe ppnssssdvr tvsytnlkfm atqiasgmky lsslnfvhrd latrnclvgk
      721 nytikiadfg msrnlysgdy yriqgravlp irwmswesil lgkfttasdv wafgvtlwet
      781 ftfcqeqpys qlsdeqvien tgeffrdqgr qtylpqpaic pdsvyklmls cwrrdtknrp
      841 sfqeihllll qqgde
//
LOCUS       NP_001073981             974 aa            linear   PRI 05-JAN-2026
DEFINITION  protein bicaudal C homolog 1 [Homo sapiens].
ACCESSION   NP_001073981 XP_498431
VERSION     NP_001073981.1
DBSOURCE    REFSEQ: accession NM_001080512.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 974)
  AUTHORS   Meng,F., Hua,S., Chen,X., Meng,N. and Lan,T.
  TITLE     Lymph node metastasis related gene BICC1 promotes tumor progression
            by promoting EMT and immune infiltration in pancreatic cancer
  JOURNAL   BMC Med Genomics 16 (1), 263 (2023)
   PUBMED   37880742
  REMARK    GeneRIF: Lymph node metastasis related gene BICC1 promotes tumor
            progression by promoting EMT and immune infiltration in pancreatic
            cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 974)
  AUTHORS   Zhao,R., Peng,C., Song,C., Zhao,Q., Rong,J., Wang,H., Ding,W.,
            Wang,F. and Xie,Y.
  TITLE     BICC1 as a novel prognostic biomarker in gastric cancer correlating
            with immune infiltrates
  JOURNAL   Int Immunopharmacol 87, 106828 (2020)
   PUBMED   32736193
  REMARK    GeneRIF: BICC1 as a novel prognostic biomarker in gastric cancer
            correlating with immune infiltrates.
REFERENCE   3  (residues 1 to 974)
  AUTHORS   Wang,H., Guo,Y., Mi,N. and Zhou,L.
  TITLE     miR-101-3p and miR-199b-5p promote cell apoptosis in oral cancer by
            targeting BICC1
  JOURNAL   Mol Cell Probes 52, 101567 (2020)
   PUBMED   32259627
  REMARK    GeneRIF: miR-101-3p and miR-199b-5p promote cell apoptosis in oral
            cancer by targeting BICC1.
REFERENCE   4  (residues 1 to 974)
  AUTHORS   Xu,Z., Lie,R.T., Wilcox,A.J., Saugstad,O.D. and Taylor,J.A.
  TITLE     A comparison of DNA methylation in newborn blood samples from
            infants with and without orofacial clefts
  JOURNAL   Clin Epigenetics 11 (1), 40 (2019)
   PUBMED   30832715
  REMARK    GeneRIF: Data identified a significantly differentially methylated
            cg09696939 near gene BICC1 to be associated with cleft lip and
            cleft palate.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 974)
  AUTHORS   Hepei,L., Mingkun,X., Li,W. and Jin,W.
  TITLE     Assessment of BicC family RNA binding protein 1 and Ras protein
            specific guanine nucleotide releasing factor 1 as candidate genes
            for high myopia: A case-control study
  JOURNAL   Indian J Ophthalmol 65 (10), 926-930 (2017)
   PUBMED   29044055
  REMARK    GeneRIF: genetic variants in BICC1 and RASGRF1 are closely
            associated with high myopia, which appears to be a potential
            candidate for high myopia in Chinese Han population.
REFERENCE   6  (residues 1 to 974)
  AUTHORS   Kraus,M.R., Clauin,S., Pfister,Y., Di Maio,M., Ulinski,T.,
            Constam,D., Bellanne-Chantelot,C. and Grapin-Botton,A.
  TITLE     Two mutations in human BICC1 resulting in Wnt pathway hyperactivity
            associated with cystic renal dysplasia
  JOURNAL   Hum Mutat 33 (1), 86-90 (2012)
   PUBMED   21922595
  REMARK    GeneRIF: The nonsense mutation identified in BICC1 and associated
            with cystic renal dysplasia results in a complete loss of Wnt
            inhibitory activity. The point mutation in the SAM domain results
            in a 22% loss of activity.
REFERENCE   7  (residues 1 to 974)
  AUTHORS   Lewis,C.M., Ng,M.Y., Butler,A.W., Cohen-Woods,S., Uher,R.,
            Pirlo,K., Weale,M.E., Schosser,A., Paredes,U.M., Rivera,M.,
            Craddock,N., Owen,M.J., Jones,L., Jones,I., Korszun,A.,
            Aitchison,K.J., Shi,J., Quinn,J.P., Mackenzie,A., Vollenweider,P.,
            Waeber,G., Heath,S., Lathrop,M., Muglia,P., Barnes,M.R.,
            Whittaker,J.C., Tozzi,F., Holsboer,F., Preisig,M., Farmer,A.E.,
            Breen,G., Craig,I.W. and McGuffin,P.
  TITLE     Genome-wide association study of major recurrent depression in the
            U.K. population
  JOURNAL   Am J Psychiatry 167 (8), 949-957 (2010)
   PUBMED   20516156
  REMARK    GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 974)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 974)
  AUTHORS   Riemenschneider,M., Mahmoodzadeh,S., Eisele,T., Klopp,N.,
            Schwarz,S., Wagenpfeil,S., Diehl,J., Mueller,U., Foerstl,H.,
            Illig,T. and Kurz,A.
  TITLE     Association analysis of genes involved in cholesterol metabolism
            located within the linkage region on chromosome 10 and Alzheimer's
            disease
  JOURNAL   Neurobiol Aging 25 (10), 1305-1308 (2004)
   PUBMED   15465627
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 974)
  AUTHORS   Wessely,O., Tran,U., Zakin,L. and De Robertis,E.M.
  TITLE     Identification and expression of the mammalian homologue of
            Bicaudal-C
  JOURNAL   Mech Dev 101 (1-2), 267-270 (2001)
   PUBMED   11231089
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC023170.10, AY726586.1,
            AC012168.10, AK225427.1, BM972104.1 and BQ014634.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 18, 2007 this sequence version replaced XP_498431.3.
            
            Summary: This gene encodes an RNA-binding protein that is active in
            regulating gene expression by modulating protein translation during
            embryonic development. Mouse studies identified the corresponding
            protein to be under strict control during cell differentiation and
            to be a maternally provided gene product. [provided by RefSeq, Apr
            2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and orthologous data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373886.8/ ENSP00000362993.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..974
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.1"
     Protein         1..974
                     /product="protein bicaudal C homolog 1"
                     /note="FGFR2-BICC1 fusion kinase protein; bicaudal C
                     homolog 1"
                     /calculated_mol_wt=104713
     Region          1..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H694.2)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9H694.2)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9H694.2)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9H694.2)"
     Region          46..126
                     /region_name="KH-I_BICC1_rpt1"
                     /note="first type I K homology (KH) RNA-binding domain
                     found in protein bicaudal C homolog 1 (BICC1) and similar
                     proteins; cd22420"
                     /db_xref="CDD:411848"
     Site            order(62,69..73,76..77,80..81,87..90)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411848"
     Region          131..200
                     /region_name="KH-I_BICC1_rpt2"
                     /note="second type I K homology (KH) RNA-binding domain
                     found in protein bicaudal C homolog 1 (BICC1) and similar
                     proteins; cd22421"
                     /db_xref="CDD:411849"
     Site            order(142,144..146,148..152,155..156,159..160,165..168)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411849"
     Region          284..349
                     /region_name="KH-I_BICC1_rpt3"
                     /note="third type I K homology (KH) RNA-binding domain
                     found in protein bicaudal C homolog 1 (BICC1) and similar
                     proteins; cd22422"
                     /db_xref="CDD:411850"
     Site            order(294,296..298,300..304,307..308,311..312,317..320)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411850"
     Site            398
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9H694.2)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H694.2)"
     Region          593..644
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H694.2)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9H694.2)"
     Region          665..719
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H694.2)"
     Site            679
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9H694.2)"
     Region          783..846
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H694.2)"
     Region          872..936
                     /region_name="SAM_BICC1"
                     /note="SAM domain of BICC1 (bicaudal) subfamily; cd09520"
                     /db_xref="CDD:188919"
     CDS             1..974
                     /gene="BICC1"
                     /gene_synonym="BICC"
                     /coded_by="NM_001080512.3:273..3197"
                     /db_xref="CCDS:CCDS31206.1"
                     /db_xref="GeneID:80114"
                     /db_xref="HGNC:HGNC:19351"
                     /db_xref="MIM:614295"
ORIGIN      
        1 maaqgepgyl aaqsdpgsns erstdspvpg seddlvagat lhspewseer frvdrkklea
       61 mlqaaaegkg rsgedffqki meetntqiaw psklkigaks kkdphikvsg kkedvkeake
      121 mimsvldtks nrvtlkmdvs htehshvigk ggnnikkvme etgchihfpd snrnnqaeks
      181 nqvsiagqpa gvesarvrir ellplvlmfe lpiagilqpv pdpnspsiqh isqtynisvs
      241 fkqrsrmyga tvivrgsqnn tsavkegtam llehlagsla saipvstqld iaaqhhlfmm
      301 grngsnikhi mqrtgaqihf pdpsnpqkks tvylqgties vclarqylmg clplvlmfdm
      361 keeievdpqf iaqlmeqldv fisikpkpkq psksvivksv ernalnmyea rkcllgless
      421 gvtiatspsp ascpaglacp sldilasagl gltglgllgp ttlslntstt pnsllnalns
      481 svsplqspss gtpsptlwap plantssatg fsaiphlmip staqatltni llsgvptygh
      541 tapspppglt pvdvhinsmq tegkkisaal nghaqspdik ygaistsslg ekvlsanhgd
      601 psiqtsgseq tspksspteg cndafvevgm prspshsgna gdlkqmmcps kvscakrqtv
      661 ellqgtknsh lhstdrllsd pelsatespl adkkapgser aaeraaaaqq nserahlapr
      721 ssyvnmqafd yeqkkllatk amlkkpvvte vrtptntwsg lgfsksmpae tikelrranh
      781 vsykptmttt yegssmslsr snsrehlggg sesdnwrdrn gigpgshsef aasigspkrk
      841 qnkstehyls ssnymdciss ltgsngcnln ssfkgsdlpe lfsklglgky tdvfqqqeid
      901 lqtfltltdq dlkelgittf garrkmllai selnknrrkl fespnartsf leggasgrlp
      961 rqyhsdiasv sgrw
//
LOCUS       NP_055055                676 aa            linear   PRI 05-JAN-2026
DEFINITION  LIM domain-containing protein 1 [Homo sapiens].
ACCESSION   NP_055055
VERSION     NP_055055.1
DBSOURCE    REFSEQ: accession NM_014240.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Mukhopadhyay,D., Chakraborty,B., Sarkar,S., Alam,N. and Panda,C.K.
  TITLE     Clinical implications of activation of the LIMD1-VHL-HIF1alpha
            pathway during head-&-neck squamous cell carcinoma development
  JOURNAL   Indian J Med Res 159 (5), 479-493 (2024)
   PUBMED   39382421
  REMARK    GeneRIF: Clinical implications of activation of the
            LIMD1-VHL-HIF1alpha pathway during head-&-neck squamous cell
            carcinoma development.
REFERENCE   2  (residues 1 to 676)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 676)
  AUTHORS   Wang,Y., Zhang,C., Yang,W., Shao,S., Xu,X., Sun,Y., Li,P., Liang,L.
            and Wu,C.
  TITLE     LIMD1 phase separation contributes to cellular mechanics and
            durotaxis by regulating focal adhesion dynamics in response to
            force
  JOURNAL   Dev Cell 56 (9), 1313-1325 (2021)
   PUBMED   33891898
  REMARK    GeneRIF: LIMD1 phase separation contributes to cellular mechanics
            and durotaxis by regulating focal adhesion dynamics in response to
            force.
REFERENCE   4  (residues 1 to 676)
  AUTHORS   Zhou,J., Zhang,L., Zhou,W., Chen,Y., Cheng,Y. and Dong,J.
  TITLE     LIMD1 phosphorylation in mitosis is required for mitotic
            progression and its tumor-suppressing activity
  JOURNAL   FEBS J 286 (5), 963-974 (2019)
   PUBMED   30600590
  REMARK    GeneRIF: findings suggest that LIMD1 is a key regulator of mitotic
            progression, and that dysregulation of LIMD1 contributes to
            tumorigenesis
REFERENCE   5  (residues 1 to 676)
  AUTHORS   Mendez,A.S., Vogt,C., Bohne,J. and Glaunsinger,B.A.
  TITLE     Site specific target binding controls RNA cleavage efficiency by
            the Kaposi's sarcoma-associated herpesvirus endonuclease SOX
  JOURNAL   Nucleic Acids Res 46 (22), 11968-11979 (2018)
   PUBMED   30321376
  REMARK    GeneRIF: Kaposi's sarcoma-associated herpesvirus SOX binds to LIMD1
            and shows RNA substrate selectivity
REFERENCE   6  (residues 1 to 676)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   7  (residues 1 to 676)
  AUTHORS   Brill,L.M., Salomon,A.R., Ficarro,S.B., Mukherji,M.,
            Stettler-Gill,M. and Peters,E.C.
  TITLE     Robust phosphoproteomic profiling of tyrosine phosphorylation sites
            from human T cells using immobilized metal affinity chromatography
            and tandem mass spectrometry
  JOURNAL   Anal Chem 76 (10), 2763-2772 (2004)
   PUBMED   15144186
REFERENCE   8  (residues 1 to 676)
  AUTHORS   Kiss,H., Kedra,D., Kiss,C., Kost-Alimova,M., Yang,Y., Klein,G.,
            Imreh,S. and Dumanski,J.P.
  TITLE     The LZTFL1 gene is a part of a transcriptional map covering 250 kb
            within the common eliminated region 1 (C3CER1) in 3p21.3
  JOURNAL   Genomics 73 (1), 10-19 (2001)
   PUBMED   11352561
REFERENCE   9  (residues 1 to 676)
  AUTHORS   Jiang,T. and Altman,S.
  TITLE     Protein-protein interactions with subunits of human nuclear RNase P
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 920-925 (2001)
   PUBMED   11158571
REFERENCE   10 (residues 1 to 676)
  AUTHORS   Kiss,H., Kedra,D., Yang,Y., Kost-Alimova,M., Kiss,C., O'Brien,K.P.,
            Fransson,I., Klein,G., Imreh,S. and Dumanski,J.P.
  TITLE     A novel gene containing LIM domains (LIMD1) is located within the
            common eliminated region 1 (C3CER1) in 3p21.3
  JOURNAL   Hum Genet 105 (6), 552-559 (1999)
   PUBMED   10647888
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099539.2, BC117236.1, BU428864.1, AJ132408.1 and AC098476.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.205164.1, AJ132408.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000273317.5/ ENSP00000273317.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..676
                     /product="LIM domain-containing protein 1"
                     /note="LIM domains containing 1"
                     /calculated_mol_wt=72059
     Region          54..134
                     /region_name="Mediates nuclear export"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGP4.1)"
     Region          <69..443
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          104..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGP4.1)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UGP4.1)"
     Region          186..260
                     /region_name="Interaction with EGLN1/PHD2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGP4.1)"
     Region          189..389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGP4.1)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UGP4.1)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B5DEH0; propagated from
                     UniProtKB/Swiss-Prot (Q9UGP4.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UGP4.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UGP4.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UGP4.1)"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B5DEH0; propagated from
                     UniProtKB/Swiss-Prot (Q9UGP4.1)"
     Region          404..442
                     /region_name="Interaction with RB1.
                     /evidence=ECO:0000269|PubMed:15542589"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGP4.1)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UGP4.1)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UGP4.1)"
     Region          472..676
                     /region_name="Necessary for nuclear localization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGP4.1)"
     Region          472..525
                     /region_name="LIM1_Ajuba_like"
                     /note="The first LIM domain of Ajuba-like proteins;
                     cd09352"
                     /db_xref="CDD:188738"
     Site            order(472,475,494,497,500,503,521,524)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188738"
     Region          537..589
                     /region_name="LIM2_Ajuba_like"
                     /note="The second LIM domain of Ajuba-like proteins;
                     cd09355"
                     /db_xref="CDD:188741"
     Site            order(537,540,557,560,563,566,585,588)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188741"
     Region          597..658
                     /region_name="LIM3_Ajuba_like"
                     /note="The third LIM domain of Ajuba-like proteins;
                     cd09438"
                     /db_xref="CDD:188822"
     Site            order(597,600,624,627,630,633,654,657)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188822"
     CDS             1..676
                     /gene="LIMD1"
                     /coded_by="NM_014240.3:130..2160"
                     /db_xref="CCDS:CCDS2729.1"
                     /db_xref="GeneID:8994"
                     /db_xref="HGNC:HGNC:6612"
                     /db_xref="MIM:604543"
ORIGIN      
        1 mdkyddlgle askfiedlnm yeaskdglfr vdkgagnnpe feetrrvfat kmakihlqqq
       61 qqqllqeetl prgsrgpvng ggrlgpqarw evvgskltvd gaakpplaas tgapgavttl
      121 aagqppyppq eqrsrpylhg trhgsqdcgs reslatsems afhqpgpced psclthgdyy
      181 dnlslaspkw gdkpgvspsi glsvgsgwps spgsdpplpk pcgdhplnhr qlslsssrss
      241 egslggqnsg iggrssekpt glwstassqr vspglpspnl engapavgpv qprtpsvsap
      301 lalscprqgg lprsnsglgg evsgvmskpn vdpqpwfqdg pksylsssap ssspagldgs
      361 qqgavpglgp kpgctdlgtg pklsptslvh pvmstlpels ckegplgwss dgslgsvlld
      421 spssprvrlp cqplvpgpel rpsaaelkle altqrlerem dahpkadyfg acvkcskgvf
      481 gagqacqamg nlyhdtcftc aacsrklrgk afyfvngkvf ceedflysgf qqsadrcflc
      541 ghlimdmilq algksyhpgc frcvicnecl dgvpftvdse nkiycvrdyh kvlapkcaac
      601 glpilppegs detirvvsmd rdyhvecyhc edcglelnde dghrcypled hlfchschvk
      661 rlekrpssta lhqhhf
//
LOCUS       NP_001431956            1295 aa            linear   PRI 07-JAN-2026
DEFINITION  protein flightless-1 homolog isoform 5 [Homo sapiens].
ACCESSION   NP_001431956 XP_005256613 XP_054171548 XP_054188065
VERSION     NP_001431956.1
DBSOURCE    REFSEQ: accession NM_001445027.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1295)
  AUTHORS   Kuwabara,Y., York,A.J., Lin,S.C., Sargent,M.A., Grimes,K.M.,
            Pirruccello,J.P. and Molkentin,J.D.
  TITLE     A human FLII gene variant alters sarcomeric actin thin filament
            length and predisposes to cardiomyopathy
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2213696120 (2023)
   PUBMED   37126682
  REMARK    GeneRIF: A human FLII gene variant alters sarcomeric actin thin
            filament length and predisposes to cardiomyopathy.
REFERENCE   2  (residues 1 to 1295)
  AUTHORS   Yang,G.N., Strudwick,X.L., Bonder,C.S., Kopecki,Z. and Cowin,A.J.
  TITLE     Increased Expression of Flightless I in Cutaneous Squamous Cell
            Carcinoma Affects Wnt/beta-Catenin Signaling Pathway
  JOURNAL   Int J Mol Sci 22 (24), 13203 (2021)
   PUBMED   34948000
  REMARK    GeneRIF: Increased Expression of Flightless I in Cutaneous Squamous
            Cell Carcinoma Affects Wnt/beta-Catenin Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1295)
  AUTHORS   Jeong,K.W.
  TITLE     FLII and MLL1 Cooperatively Regulate Aryl Hydrocarbon
            Receptor-Mediated Transcription in ARPE-19 Cells
  JOURNAL   Curr Issues Mol Biol 43 (3), 1623-1631 (2021)
   PUBMED   34698116
  REMARK    GeneRIF: FLII and MLL1 Cooperatively Regulate Aryl Hydrocarbon
            Receptor-Mediated Transcription in ARPE-19 Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1295)
  AUTHORS   Ruan,H., Bao,L., Tao,Z. and Chen,K.
  TITLE     Flightless I Homolog Reverses Enzalutamide Resistance through
            PD-L1-Mediated Immune Evasion in Prostate Cancer
  JOURNAL   Cancer Immunol Res 9 (7), 838-852 (2021)
   PUBMED   34011528
  REMARK    GeneRIF: Flightless I Homolog Reverses Enzalutamide Resistance
            through PD-L1-Mediated Immune Evasion in Prostate Cancer.
REFERENCE   5  (residues 1 to 1295)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1295)
  AUTHORS   Wilson,S.A., Brown,E.C., Kingsman,A.J. and Kingsman,S.M.
  TITLE     TRIP: a novel double stranded RNA binding protein which interacts
            with the leucine rich repeat of flightless I
  JOURNAL   Nucleic Acids Res 26 (15), 3460-3467 (1998)
   PUBMED   9671805
REFERENCE   7  (residues 1 to 1295)
  AUTHORS   Liu,Y.T. and Yin,H.L.
  TITLE     Identification of the binding partners for flightless I, A novel
            protein bridging the leucine-rich repeat and the gelsolin
            superfamilies
  JOURNAL   J Biol Chem 273 (14), 7920-7927 (1998)
   PUBMED   9525888
REFERENCE   8  (residues 1 to 1295)
  AUTHORS   Campbell,H.D., Fountain,S., Young,I.G., Claudianos,C.,
            Hoheisel,J.D., Chen,K.S. and Lupski,J.R.
  TITLE     Genomic structure, evolution, and expression of human FLII, a
            gelsolin and leucine-rich-repeat family member: overlap with LLGL
  JOURNAL   Genomics 42 (1), 46-54 (1997)
   PUBMED   9177775
REFERENCE   9  (residues 1 to 1295)
  AUTHORS   Chen,K.S., Gunaratne,P.H., Hoheisel,J.D., Young,I.G., Miklos,G.L.,
            Greenberg,F., Shaffer,L.G., Campbell,H.D. and Lupski,J.R.
  TITLE     The human homologue of the Drosophila melanogaster flightless-I
            gene (flil) maps within the Smith-Magenis microdeletion critical
            region in 17p11.2
  JOURNAL   Am J Hum Genet 56 (1), 175-182 (1995)
   PUBMED   7825574
REFERENCE   10 (residues 1 to 1295)
  AUTHORS   Campbell,H.D., Schimansky,T., Claudianos,C., Ozsarac,N.,
            Kasprzak,A.B., Cotsell,J.N., Young,I.G., de Couet,H.G. and
            Miklos,G.L.
  TITLE     The Drosophila melanogaster flightless-I gene involved in
            gastrulation and muscle degeneration encodes gelsolin-like and
            leucine-rich repeat domains and is conserved in Caenorhabditis
            elegans and humans
  JOURNAL   Proc Natl Acad Sci U S A 90 (23), 11386-11390 (1993)
   PUBMED   8248259
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC127537.8.
            
            On or before Jan 7, 2026 this sequence version replaced
            XP_054188065.1, XP_005256613.1, XP_054171548.1.
            
            Summary: This gene encodes a protein with a gelsolin-like actin
            binding domain and an N-terminal leucine-rich repeat-protein
            protein interaction domain. The protein is similar to a Drosophila
            protein involved in early embryogenesis and the structural
            organization of indirect flight muscle. The gene is located within
            the Smith-Magenis syndrome region on chromosome 17. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.920902.1,
                                           SRR18074967.2849359.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1295
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..1295
                     /product="protein flightless-1 homolog isoform 5"
                     /note="protein flightless-1 homolog; flightless I homolog;
                     flightless I actin binding protein"
                     /calculated_mol_wt=147417
     Region          10..34
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <24..375
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          35..57
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          58..80
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          83..105
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          106..128
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          129..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          176..199
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          200..224
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          225..247
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          248..270
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          271..293
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          294..318
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          319..339
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          342..355
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          491..603
                     /region_name="gelsolin_S1_like"
                     /note="Gelsolin sub-domain 1-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11290"
                     /db_xref="CDD:200446"
     Site            order(508..509,548,554..555,557..559,561..563,565..566,
                     577,579)
                     /site_type="other"
                     /note="putative actin binding interface [polypeptide
                     binding]"
                     /db_xref="CDD:200446"
     Region          618..705
                     /region_name="gelsolin_like"
                     /note="Tandemly repeated domains found in gelsolin,
                     severin, villin, and related proteins; cd11280"
                     /db_xref="CDD:200436"
     Region          722..836
                     /region_name="gelsolin_S3_like"
                     /note="Gelsolin sub-domain 3-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11292"
                     /db_xref="CDD:200448"
     Site            order(831,836)
                     /site_type="other"
                     /note="putative nucleotide binding site [chemical
                     binding]"
                     /db_xref="CDD:200448"
     Region          <973..1033
                     /region_name="gelsolin_like"
                     /note="Tandemly repeated domains found in gelsolin,
                     severin, villin, and related proteins; cd11280"
                     /db_xref="CDD:200436"
     Region          1052..1151
                     /region_name="gelsolin_S5_like"
                     /note="Gelsolin sub-domain 5-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11288"
                     /db_xref="CDD:200444"
     Site            1059
                     /site_type="other"
                     /note="putative nucleotide binding residue [chemical
                     binding]"
                     /db_xref="CDD:200444"
     Region          1162..1288
                     /region_name="gelsolin_S6_like"
                     /note="Gelsolin sub-domain 6-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11291"
                     /db_xref="CDD:200447"
     CDS             1..1295
                     /gene="FLII"
                     /gene_synonym="CMD2J; FLI; Fli1; FLIL"
                     /coded_by="NM_001445027.1:49..3936"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:2314"
                     /db_xref="HGNC:HGNC:3750"
                     /db_xref="MIM:600362"
ORIGIN      
        1 meatgvlpfv rgvdlsgndf kggyfpenvk amtslrwlkl nrtglcylpe elaalqkleh
       61 lsvshnnltt lhgelsslps lraivarans lknsgvpddi fklddlsvld lshnqltecp
      121 relenaknml vlnlshnsid tipnqlfinl tdllyldlse nrleslppqm rrlvhlqtlv
      181 lngnpllhaq lrqlpamtal qtlhlrstqr tqsnlptsle glsnladvdl scndltrvpe
      241 clytlpslrr lnlssnqite lslcidqwvh vetlnlsrnq ltslpsaick lsklkklyln
      301 snkldfdglp sgigkltnle efmaannnle lvpeslcrcp klrklvlnkn hlvtlpeaih
      361 flteievldv renpnlvmpp kpadraaewy nidfslqnql rlagaspatv aaaaagsgpk
      421 dpmarkmrlr rrkdsaqddq akqvlkgmsd vaqeknkkqe esadarapsg kvrrwdqgle
      481 kprldyseff tedvgqlpgl tiwqienfvp vlveeafhgk fyeadcyivl ktflddsgsl
      541 nweiyywigg eatldkkacs aihavnlrny lgaecrtvre emgdeseefl qvfdndisyi
      601 eggtasgfyt vedthyvtrm yrvygkknik lepvplkgts ldprfvflld rgldiyvwrg
      661 aqatlssttk arlfaekink nerkgkaeit llvqgqelpe fwealggeps eikkhvpedf
      721 wppqpklykv glglgylelp qinyklsveh kqrpkvelmp rmrllqslld trcvyildcw
      781 sdvfiwlgrk sprlvraaal klgqelcgml hrprhatvsr slegteaqvf kakfknwddv
      841 ltvdytrnae avlqspglsg kvkrdaekkd qmkadltalf lprqppmsla eaeqlmeewn
      901 edldgmegfv legkkfarlp eeefghfytq dcyvflcryw vpveyeeeek kedkeekaeg
      961 kegeeataea eekqpeedfq civyfwqgre asnmgwltft fslqkkfesl fpgklevvrm
     1021 tqqqenpkfl shfkrkfiih rgkrkavqga qqpslyqirt ngsalctrci qintdsslln
     1081 sefcfilkvp fesednqgiv yawvgrasdp deaklaedil ntmfdtsysk qvinegeepe
     1141 nffwvgigaq kpydddaeym khtrlfrcsn ekgyfavtek csdfcqddla dddimlldng
     1201 qevymwvgtq tsqveiklsl kacqviwveg gprwacgqgr vitqgslspc qvyiqhmrsk
     1261 eherprrlrl vrkgneqhaf trcfhawsaf ckala
//
LOCUS       NP_001431914             363 aa            linear   PRI 07-JAN-2026
DEFINITION  lymphocyte antigen 6 complex locus protein G6f isoform 3 [Homo
            sapiens].
ACCESSION   NP_001431914
VERSION     NP_001431914.1
DBSOURCE    REFSEQ: accession NM_001444985.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 363)
  AUTHORS   Ucisik-Akkaya,E., Davis,C.F., Do,T.N., Morrison,B.A., Stemmer,S.M.,
            Amadio,W.J. and Dorak,M.T.
  TITLE     Examination of genetic polymorphisms in newborns for signatures of
            sex-specific prenatal selection
  JOURNAL   Mol Hum Reprod 16 (10), 770-777 (2010)
   PUBMED   20587610
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   2  (residues 1 to 363)
  AUTHORS   Barcellos,L.F., May,S.L., Ramsay,P.P., Quach,H.L., Lane,J.A.,
            Nititham,J., Noble,J.A., Taylor,K.E., Quach,D.L., Chung,S.A.,
            Kelly,J.A., Moser,K.L., Behrens,T.W., Seldin,M.F., Thomson,G.,
            Harley,J.B., Gaffney,P.M. and Criswell,L.A.
  TITLE     High-density SNP screening of the major histocompatibility complex
            in systemic lupus erythematosus demonstrates strong evidence for
            independent susceptibility regions
  JOURNAL   PLoS Genet 5 (10), e1000696 (2009)
   PUBMED   19851445
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   3  (residues 1 to 363)
  AUTHORS   Macaulay,I.C., Tijssen,M.R., Thijssen-Timmer,D.C., Gusnanto,A.,
            Steward,M., Burns,P., Langford,C.F., Ellis,P.D., Dudbridge,F.,
            Zwaginga,J.J., Watkins,N.A., van der Schoot,C.E. and Ouwehand,W.H.
  TITLE     Comparative gene expression profiling of in vitro differentiated
            megakaryocytes and erythroblasts identifies novel activatory and
            inhibitory platelet membrane proteins
  JOURNAL   Blood 109 (8), 3260-3269 (2007)
   PUBMED   17192395
REFERENCE   4  (residues 1 to 363)
  AUTHORS   De Vet,E.C., Aguado,B. and Campbell,R.D.
  TITLE     Adaptor signalling proteins Grb2 and Grb7 are recruited by human
            G6f, a novel member of the immunoglobulin superfamily encoded in
            the MHC
  JOURNAL   Biochem J 375 (Pt 1), 207-213 (2003)
   PUBMED   12852788
  REMARK    GeneRIF: G6f recruits adaptor signalling proteins Grb2 and Grb7.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL662899.5.
            
            Summary: The human G6f protein is a type I transmembrane protein
            belonging to the immunoglobin (Ig) superfamily, which is comprised
            of cell-surface proteins involved in the immune system and cellular
            recognition (de Vet et al., 2003 [PubMed 12852788]).[supplied by
            OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.131661.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968968,
                                           SAMEA2148093 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..363
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..363
                     /product="lymphocyte antigen 6 complex locus protein G6f
                     isoform 3"
                     /note="lymphocyte antigen 6 complex locus protein G6f;
                     lymphocyte antigen 6 complex, locus G6D; lymphocyte
                     antigen 6 complex, locus G6F"
                     /calculated_mol_wt=38742
     Region          1..97
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          12..16
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          26..32
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          70..74
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          84..89
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          249..335
                     /region_name="TFP_LU_ECD_Ly6G6d"
                     /note="extracellular domain (ECD) found in lymphocyte
                     antigen 6 complex locus protein G6d (Ly6G6d) and similar
                     proteins; cd23547"
                     /db_xref="CDD:467077"
     CDS             1..363
                     /gene="LY6G6F"
                     /gene_synonym="C6orf21; G6f; LY6G6; LY6G6D; NG32"
                     /coded_by="NM_001444985.1:175..1266"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:259215"
                     /db_xref="HGNC:HGNC:13933"
                     /db_xref="MIM:611404"
ORIGIN      
        1 mqaiyvalge avelpcpspp tlhgdehlsw fcspaagsft tlvaqvqvgr papdpgkpgr
       61 esrlrllgny slwlegskee dagrywcavl gqhhnyqnwr vydvlvlkgs qlsaraadgs
      121 pcnvllcsvv psrrmdsvtw qegkgpvrgr vqsfwgseaa lllvcpgegl seprsrrpri
      181 irclmthnkg vsfslaasid aspalcapst gwdmpwilml lltmgqgvvi lalsivlwrq
      241 rvrgapgrgn rmrcyncggs psssckeavt tcgegrpqpg leqiklpgnp pvtlihqhpa
      301 cvaahhcnqv etesvgdvty pahrdcylgd lcnsavashv apagilaaaa taltcllpgl
      361 wsg
//
LOCUS       NP_001431955            1268 aa            linear   PRI 07-JAN-2026
DEFINITION  protein flightless-1 homolog isoform 4 [Homo sapiens].
ACCESSION   NP_001431955 XP_005256615 XP_054171549 XP_054188066
VERSION     NP_001431955.1
DBSOURCE    REFSEQ: accession NM_001445026.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1268)
  AUTHORS   Kuwabara,Y., York,A.J., Lin,S.C., Sargent,M.A., Grimes,K.M.,
            Pirruccello,J.P. and Molkentin,J.D.
  TITLE     A human FLII gene variant alters sarcomeric actin thin filament
            length and predisposes to cardiomyopathy
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2213696120 (2023)
   PUBMED   37126682
  REMARK    GeneRIF: A human FLII gene variant alters sarcomeric actin thin
            filament length and predisposes to cardiomyopathy.
REFERENCE   2  (residues 1 to 1268)
  AUTHORS   Yang,G.N., Strudwick,X.L., Bonder,C.S., Kopecki,Z. and Cowin,A.J.
  TITLE     Increased Expression of Flightless I in Cutaneous Squamous Cell
            Carcinoma Affects Wnt/beta-Catenin Signaling Pathway
  JOURNAL   Int J Mol Sci 22 (24), 13203 (2021)
   PUBMED   34948000
  REMARK    GeneRIF: Increased Expression of Flightless I in Cutaneous Squamous
            Cell Carcinoma Affects Wnt/beta-Catenin Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1268)
  AUTHORS   Jeong,K.W.
  TITLE     FLII and MLL1 Cooperatively Regulate Aryl Hydrocarbon
            Receptor-Mediated Transcription in ARPE-19 Cells
  JOURNAL   Curr Issues Mol Biol 43 (3), 1623-1631 (2021)
   PUBMED   34698116
  REMARK    GeneRIF: FLII and MLL1 Cooperatively Regulate Aryl Hydrocarbon
            Receptor-Mediated Transcription in ARPE-19 Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1268)
  AUTHORS   Ruan,H., Bao,L., Tao,Z. and Chen,K.
  TITLE     Flightless I Homolog Reverses Enzalutamide Resistance through
            PD-L1-Mediated Immune Evasion in Prostate Cancer
  JOURNAL   Cancer Immunol Res 9 (7), 838-852 (2021)
   PUBMED   34011528
  REMARK    GeneRIF: Flightless I Homolog Reverses Enzalutamide Resistance
            through PD-L1-Mediated Immune Evasion in Prostate Cancer.
REFERENCE   5  (residues 1 to 1268)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1268)
  AUTHORS   Wilson,S.A., Brown,E.C., Kingsman,A.J. and Kingsman,S.M.
  TITLE     TRIP: a novel double stranded RNA binding protein which interacts
            with the leucine rich repeat of flightless I
  JOURNAL   Nucleic Acids Res 26 (15), 3460-3467 (1998)
   PUBMED   9671805
REFERENCE   7  (residues 1 to 1268)
  AUTHORS   Liu,Y.T. and Yin,H.L.
  TITLE     Identification of the binding partners for flightless I, A novel
            protein bridging the leucine-rich repeat and the gelsolin
            superfamilies
  JOURNAL   J Biol Chem 273 (14), 7920-7927 (1998)
   PUBMED   9525888
REFERENCE   8  (residues 1 to 1268)
  AUTHORS   Campbell,H.D., Fountain,S., Young,I.G., Claudianos,C.,
            Hoheisel,J.D., Chen,K.S. and Lupski,J.R.
  TITLE     Genomic structure, evolution, and expression of human FLII, a
            gelsolin and leucine-rich-repeat family member: overlap with LLGL
  JOURNAL   Genomics 42 (1), 46-54 (1997)
   PUBMED   9177775
REFERENCE   9  (residues 1 to 1268)
  AUTHORS   Chen,K.S., Gunaratne,P.H., Hoheisel,J.D., Young,I.G., Miklos,G.L.,
            Greenberg,F., Shaffer,L.G., Campbell,H.D. and Lupski,J.R.
  TITLE     The human homologue of the Drosophila melanogaster flightless-I
            gene (flil) maps within the Smith-Magenis microdeletion critical
            region in 17p11.2
  JOURNAL   Am J Hum Genet 56 (1), 175-182 (1995)
   PUBMED   7825574
REFERENCE   10 (residues 1 to 1268)
  AUTHORS   Campbell,H.D., Schimansky,T., Claudianos,C., Ozsarac,N.,
            Kasprzak,A.B., Cotsell,J.N., Young,I.G., de Couet,H.G. and
            Miklos,G.L.
  TITLE     The Drosophila melanogaster flightless-I gene involved in
            gastrulation and muscle degeneration encodes gelsolin-like and
            leucine-rich repeat domains and is conserved in Caenorhabditis
            elegans and humans
  JOURNAL   Proc Natl Acad Sci U S A 90 (23), 11386-11390 (1993)
   PUBMED   8248259
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC127537.8.
            
            On or before Jan 7, 2026 this sequence version replaced
            XP_054188066.1, XP_005256615.1, XP_054171549.1.
            
            Summary: This gene encodes a protein with a gelsolin-like actin
            binding domain and an N-terminal leucine-rich repeat-protein
            protein interaction domain. The protein is similar to a Drosophila
            protein involved in early embryogenesis and the structural
            organization of indirect flight muscle. The gene is located within
            the Smith-Magenis syndrome region on chromosome 17. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.75332.1,
                                           SRR18074969.1650304.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1268
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..1268
                     /product="protein flightless-1 homolog isoform 4"
                     /note="protein flightless-1 homolog; flightless I homolog;
                     flightless I actin binding protein"
                     /calculated_mol_wt=144550
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:12665801,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q13045.2)"
     Region          10..34
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13045.2)"
     Region          <24..375
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          35..57
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          58..80
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          83..105
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          106..128
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          129..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          176..199
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          200..224
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          225..247
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          248..270
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          271..293
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          294..318
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          319..339
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          342..355
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13045.2)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by SGK3.
                     /evidence=ECO:0000269|PubMed:19293151,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13045.2)"
     Region          451..472
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13045.2)"
     Region          491..603
                     /region_name="gelsolin_S1_like"
                     /note="Gelsolin sub-domain 1-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11290"
                     /db_xref="CDD:200446"
     Region          494..826
                     /region_name="Interaction with ACTL6A.
                     /evidence=ECO:0000269|PubMed:14966289"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13045.2)"
     Site            order(508..509,548,554..555,557..559,561..563,565..566,
                     577,579)
                     /site_type="other"
                     /note="putative actin binding interface [polypeptide
                     binding]"
                     /db_xref="CDD:200446"
     Region          618..705
                     /region_name="gelsolin_like"
                     /note="Tandemly repeated domains found in gelsolin,
                     severin, villin, and related proteins; cd11280"
                     /db_xref="CDD:200436"
     Region          722..836
                     /region_name="gelsolin_S3_like"
                     /note="Gelsolin sub-domain 3-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11292"
                     /db_xref="CDD:200448"
     Region          757..830
                     /region_name="Gelsolin-like 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13045.2)"
     Site            817
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by SGK3.
                     /evidence=ECO:0000269|PubMed:19293151; propagated from
                     UniProtKB/Swiss-Prot (Q13045.2)"
     Site            order(831,836)
                     /site_type="other"
                     /note="putative nucleotide binding site [chemical
                     binding]"
                     /db_xref="CDD:200448"
     Site            855
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q13045.2)"
     Site            859
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13045.2)"
     Region          950..974
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13045.2)"
     Region          <973..1033
                     /region_name="gelsolin_like"
                     /note="Tandemly repeated domains found in gelsolin,
                     severin, villin, and related proteins; cd11280"
                     /db_xref="CDD:200436"
     Region          1052..1151
                     /region_name="gelsolin_S5_like"
                     /note="Gelsolin sub-domain 5-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11288"
                     /db_xref="CDD:200444"
     Site            1059
                     /site_type="other"
                     /note="putative nucleotide binding residue [chemical
                     binding]"
                     /db_xref="CDD:200444"
     Region          1074..1142
                     /region_name="Gelsolin-like 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13045.2)"
     Region          1162..1261
                     /region_name="gelsolin_S6_like"
                     /note="Gelsolin sub-domain 6-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11291"
                     /db_xref="CDD:200447"
     Region          1180..1253
                     /region_name="Gelsolin-like 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13045.2)"
     CDS             1..1268
                     /gene="FLII"
                     /gene_synonym="CMD2J; FLI; Fli1; FLIL"
                     /coded_by="NM_001445026.1:49..3855"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:2314"
                     /db_xref="HGNC:HGNC:3750"
                     /db_xref="MIM:600362"
ORIGIN      
        1 meatgvlpfv rgvdlsgndf kggyfpenvk amtslrwlkl nrtglcylpe elaalqkleh
       61 lsvshnnltt lhgelsslps lraivarans lknsgvpddi fklddlsvld lshnqltecp
      121 relenaknml vlnlshnsid tipnqlfinl tdllyldlse nrleslppqm rrlvhlqtlv
      181 lngnpllhaq lrqlpamtal qtlhlrstqr tqsnlptsle glsnladvdl scndltrvpe
      241 clytlpslrr lnlssnqite lslcidqwvh vetlnlsrnq ltslpsaick lsklkklyln
      301 snkldfdglp sgigkltnle efmaannnle lvpeslcrcp klrklvlnkn hlvtlpeaih
      361 flteievldv renpnlvmpp kpadraaewy nidfslqnql rlagaspatv aaaaagsgpk
      421 dpmarkmrlr rrkdsaqddq akqvlkgmsd vaqeknkkqe esadarapsg kvrrwdqgle
      481 kprldyseff tedvgqlpgl tiwqienfvp vlveeafhgk fyeadcyivl ktflddsgsl
      541 nweiyywigg eatldkkacs aihavnlrny lgaecrtvre emgdeseefl qvfdndisyi
      601 eggtasgfyt vedthyvtrm yrvygkknik lepvplkgts ldprfvflld rgldiyvwrg
      661 aqatlssttk arlfaekink nerkgkaeit llvqgqelpe fwealggeps eikkhvpedf
      721 wppqpklykv glglgylelp qinyklsveh kqrpkvelmp rmrllqslld trcvyildcw
      781 sdvfiwlgrk sprlvraaal klgqelcgml hrprhatvsr slegteaqvf kakfknwddv
      841 ltvdytrnae avlqspglsg kvkrdaekkd qmkadltalf lprqppmsla eaeqlmeewn
      901 edldgmegfv legkkfarlp eeefghfytq dcyvflcryw vpveyeeeek kedkeekaeg
      961 kegeeataea eekqpeedfq civyfwqgre asnmgwltft fslqkkfesl fpgklevvrm
     1021 tqqqenpkfl shfkrkfiih rgkrkavqga qqpslyqirt ngsalctrci qintdsslln
     1081 sefcfilkvp fesednqgiv yawvgrasdp deaklaedil ntmfdtsysk qvinegeepe
     1141 nffwvgigaq kpydddaeym khtrlfrcsn ekgyfavtek csdfcqddla dddimlldng
     1201 qevymwvgtq tsqveiklsl kacqvyiqhm rskeherprr lrlvrkgneq haftrcfhaw
     1261 safckala
//
LOCUS       NP_001431951             291 aa            linear   PRI 07-JAN-2026
DEFINITION  asialoglycoprotein receptor 1 isoform a [Homo sapiens].
ACCESSION   NP_001431951 XP_011522163 XP_054172134
VERSION     NP_001431951.1
DBSOURCE    REFSEQ: accession NM_001445022.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Zhang,Z., Leng,X.K., Zhai,Y.Y., Zhang,X., Sun,Z.W., Xiao,J.Y.,
            Lu,J.F., Liu,K., Xia,B., Gao,Q., Jia,M., Xu,C.Q., Jiang,Y.N.,
            Zhang,X.G., Tao,K.S. and Wu,J.W.
  TITLE     Deficiency of ASGR1 promotes liver injury by increasing
            GP73-mediated hepatic endoplasmic reticulum stress
  JOURNAL   Nat Commun 15 (1), 1908 (2024)
   PUBMED   38459023
  REMARK    GeneRIF: Deficiency of ASGR1 promotes liver injury by increasing
            GP73-mediated hepatic endoplasmic reticulum stress.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Yang,X., Zheng,X., Zhu,Y., Zhao,X., Liu,J., Xun,J., Yuan,S.,
            Chen,J., Pan,H., Yang,J., Wang,J., Liang,Z., Shen,X., Liang,Y.,
            Lin,Q., Liang,H., Li,M., Peng,F., Lu,D., Xu,J., Lu,H., Jiang,S.,
            Zhao,P. and Zhu,H.
  TITLE     Asialoglycoprotein receptor 1 promotes SARS-CoV-2 infection of
            human normal hepatocytes
  JOURNAL   Signal Transduct Target Ther 9 (1), 42 (2024)
   PUBMED   38355848
  REMARK    GeneRIF: Asialoglycoprotein receptor 1 promotes SARS-CoV-2
            infection of human normal hepatocytes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Hoffmann,M. and Pohlmann,S.
  TITLE     Novel SARS-CoV-2 receptors: ASGR1 and KREMEN1
  JOURNAL   Cell Res 32 (1), 1-2 (2022)
   PUBMED   34903854
  REMARK    GeneRIF: Novel SARS-CoV-2 receptors: ASGR1 and KREMEN1.
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Hu,B., Yang,Y., Liu,J., Ma,Z., Huang,H., Liu,S., Yu,Y., Hao,Y.,
            Wang,B., Lu,M. and Yang,D.
  TITLE     Establishment of a functional cell line expressing both subunits of
            H1a and H2c of human hepatocyte surface molecule ASGPR
  JOURNAL   J Huazhong Univ Sci Technolog Med Sci 30 (5), 556-561 (2010)
   PUBMED   21063834
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Liu,J., Hu,B., Yang,Y., Ma,Z., Yu,Y., Liu,S., Wang,B., Zhao,X.,
            Lu,M. and Yang,D.
  TITLE     A new splice variant of the major subunit of human
            asialoglycoprotein receptor encodes a secreted form in hepatocytes
  JOURNAL   PLoS One 5 (9), e12934 (2010)
   PUBMED   20886072
  REMARK    GeneRIF: Two naturally occurring ASGPR1 splice variants are
            produced in human hepatocytes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Beltzer,J.P. and Spiess,M.
  TITLE     In vitro binding of the asialoglycoprotein receptor to the beta
            adaptin of plasma membrane coated vesicles
  JOURNAL   EMBO J 10 (12), 3735-3742 (1991)
   PUBMED   1935897
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Sanford,J.P., Eddy,R.L., Doyle,D. and Shows,T.B.
  TITLE     Assignment of human asialoglycoprotein receptor gene (ASGR1) to
            chromosome 17p11-13
  JOURNAL   Genomics 11 (3), 779-781 (1991)
   PUBMED   1774077
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Geffen,I., Fuhrer,C. and Spiess,M.
  TITLE     Endocytosis by the asialoglycoprotein receptor is independent of
            cytoplasmic serine residues
  JOURNAL   Proc Natl Acad Sci U S A 88 (19), 8425-8429 (1991)
   PUBMED   1924301
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Bischoff,J., Libresco,S., Shia,M.A. and Lodish,H.F.
  TITLE     The H1 and H2 polypeptides associate to form the asialoglycoprotein
            receptor in human hepatoma cells
  JOURNAL   J Cell Biol 106 (4), 1067-1074 (1988)
   PUBMED   2834401
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Spiess,M., Schwartz,A.L. and Lodish,H.F.
  TITLE     Sequence of human asialoglycoprotein receptor cDNA. An internal
            signal sequence for membrane insertion
  JOURNAL   J Biol Chem 260 (4), 1979-1982 (1985)
   PUBMED   2982798
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC120057.9.
            
            On or before Jan 7, 2026 this sequence version replaced
            XP_011522163.1, XP_054172134.1.
            
            Summary: This gene encodes a subunit of the asialoglycoprotein
            receptor. This receptor is a transmembrane protein that plays a
            critical role in serum glycoprotein homeostasis by mediating the
            endocytosis and lysosomal degradation of glycoproteins with exposed
            terminal galactose or N-acetylgalactosamine residues. The
            asialoglycoprotein receptor may facilitate hepatic infection by
            multiple viruses including hepatitis B, and is also a target for
            liver-specific drug delivery. The asialoglycoprotein receptor is a
            hetero-oligomeric protein composed of major and minor subunits,
            which are encoded by different genes. The protein encoded by this
            gene is the more abundant major subunit. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene. [provided by RefSeq, Jan 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.3171807.1,
                                           SRR14038194.2828730.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in SARS-CoV-2 infection
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..291
                     /product="asialoglycoprotein receptor 1 isoform a"
                     /note="hepatic lectin H1; C-type lectin domain family 4
                     member H1"
                     /calculated_mol_wt=33055
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07306.2)"
     Region          4..144
                     /region_name="Lectin_N"
                     /note="Hepatic lectin, N-terminal domain; pfam03954"
                     /db_xref="CDD:461106"
     Region          5..8
                     /region_name="Endocytosis signal. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P07306.2)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P07306.2)"
     Site            41..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P07306.2)"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P07306.2)"
     Site            147
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P07306.2)"
     Region          154..279
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Site            order(209,240,242,253,259,265..268)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(216,243,253..254)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P07306.2)"
     CDS             1..291
                     /gene="ASGR1"
                     /gene_synonym="ASGPR; ASGPR1; CLEC4H1; HL-1"
                     /coded_by="NM_001445022.1:252..1127"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:432"
                     /db_xref="HGNC:HGNC:742"
                     /db_xref="MIM:108360"
ORIGIN      
        1 mtkeyqdlqh ldneesdhhq lrkgppppqp llqrlcsgpr llllslglsl lllvvvcvig
       61 sqnsqlqeel rglretfsnf tasteaqvkg lstqggnvgr kmkslesqle kqqkdlsedh
      121 sslllhvkqf vsdlrslscq maalqgngse rtccpvnwve herscywfsr sgkawadadn
      181 ycrledahlv vvtsweeqkf vqhhigpvnt wmglhdqngp wkwvdgtdye tgfknwrpeq
      241 pddwyghglg ggedcahftd dgrwnddvcq rpyrwvcete ldkasqeppl l
//
LOCUS       NP_001431957            1296 aa            linear   PRI 07-JAN-2026
DEFINITION  protein flightless-1 homolog isoform 6 [Homo sapiens].
ACCESSION   NP_001431957 XP_005256612 XP_054171547 XP_054188064
VERSION     NP_001431957.1
DBSOURCE    REFSEQ: accession NM_001445028.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1296)
  AUTHORS   Kuwabara,Y., York,A.J., Lin,S.C., Sargent,M.A., Grimes,K.M.,
            Pirruccello,J.P. and Molkentin,J.D.
  TITLE     A human FLII gene variant alters sarcomeric actin thin filament
            length and predisposes to cardiomyopathy
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2213696120 (2023)
   PUBMED   37126682
  REMARK    GeneRIF: A human FLII gene variant alters sarcomeric actin thin
            filament length and predisposes to cardiomyopathy.
REFERENCE   2  (residues 1 to 1296)
  AUTHORS   Yang,G.N., Strudwick,X.L., Bonder,C.S., Kopecki,Z. and Cowin,A.J.
  TITLE     Increased Expression of Flightless I in Cutaneous Squamous Cell
            Carcinoma Affects Wnt/beta-Catenin Signaling Pathway
  JOURNAL   Int J Mol Sci 22 (24), 13203 (2021)
   PUBMED   34948000
  REMARK    GeneRIF: Increased Expression of Flightless I in Cutaneous Squamous
            Cell Carcinoma Affects Wnt/beta-Catenin Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1296)
  AUTHORS   Jeong,K.W.
  TITLE     FLII and MLL1 Cooperatively Regulate Aryl Hydrocarbon
            Receptor-Mediated Transcription in ARPE-19 Cells
  JOURNAL   Curr Issues Mol Biol 43 (3), 1623-1631 (2021)
   PUBMED   34698116
  REMARK    GeneRIF: FLII and MLL1 Cooperatively Regulate Aryl Hydrocarbon
            Receptor-Mediated Transcription in ARPE-19 Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1296)
  AUTHORS   Ruan,H., Bao,L., Tao,Z. and Chen,K.
  TITLE     Flightless I Homolog Reverses Enzalutamide Resistance through
            PD-L1-Mediated Immune Evasion in Prostate Cancer
  JOURNAL   Cancer Immunol Res 9 (7), 838-852 (2021)
   PUBMED   34011528
  REMARK    GeneRIF: Flightless I Homolog Reverses Enzalutamide Resistance
            through PD-L1-Mediated Immune Evasion in Prostate Cancer.
REFERENCE   5  (residues 1 to 1296)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1296)
  AUTHORS   Wilson,S.A., Brown,E.C., Kingsman,A.J. and Kingsman,S.M.
  TITLE     TRIP: a novel double stranded RNA binding protein which interacts
            with the leucine rich repeat of flightless I
  JOURNAL   Nucleic Acids Res 26 (15), 3460-3467 (1998)
   PUBMED   9671805
REFERENCE   7  (residues 1 to 1296)
  AUTHORS   Liu,Y.T. and Yin,H.L.
  TITLE     Identification of the binding partners for flightless I, A novel
            protein bridging the leucine-rich repeat and the gelsolin
            superfamilies
  JOURNAL   J Biol Chem 273 (14), 7920-7927 (1998)
   PUBMED   9525888
REFERENCE   8  (residues 1 to 1296)
  AUTHORS   Campbell,H.D., Fountain,S., Young,I.G., Claudianos,C.,
            Hoheisel,J.D., Chen,K.S. and Lupski,J.R.
  TITLE     Genomic structure, evolution, and expression of human FLII, a
            gelsolin and leucine-rich-repeat family member: overlap with LLGL
  JOURNAL   Genomics 42 (1), 46-54 (1997)
   PUBMED   9177775
REFERENCE   9  (residues 1 to 1296)
  AUTHORS   Chen,K.S., Gunaratne,P.H., Hoheisel,J.D., Young,I.G., Miklos,G.L.,
            Greenberg,F., Shaffer,L.G., Campbell,H.D. and Lupski,J.R.
  TITLE     The human homologue of the Drosophila melanogaster flightless-I
            gene (flil) maps within the Smith-Magenis microdeletion critical
            region in 17p11.2
  JOURNAL   Am J Hum Genet 56 (1), 175-182 (1995)
   PUBMED   7825574
REFERENCE   10 (residues 1 to 1296)
  AUTHORS   Campbell,H.D., Schimansky,T., Claudianos,C., Ozsarac,N.,
            Kasprzak,A.B., Cotsell,J.N., Young,I.G., de Couet,H.G. and
            Miklos,G.L.
  TITLE     The Drosophila melanogaster flightless-I gene involved in
            gastrulation and muscle degeneration encodes gelsolin-like and
            leucine-rich repeat domains and is conserved in Caenorhabditis
            elegans and humans
  JOURNAL   Proc Natl Acad Sci U S A 90 (23), 11386-11390 (1993)
   PUBMED   8248259
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC127537.8.
            
            On or before Jan 7, 2026 this sequence version replaced
            XP_054188064.1, XP_005256612.1, XP_054171547.1.
            
            Summary: This gene encodes a protein with a gelsolin-like actin
            binding domain and an N-terminal leucine-rich repeat-protein
            protein interaction domain. The protein is similar to a Drosophila
            protein involved in early embryogenesis and the structural
            organization of indirect flight muscle. The gene is located within
            the Smith-Magenis syndrome region on chromosome 17. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1707774.1,
                                           SRR14038193.645140.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1296
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..1296
                     /product="protein flightless-1 homolog isoform 6"
                     /note="protein flightless-1 homolog; flightless I homolog;
                     flightless I actin binding protein"
                     /calculated_mol_wt=147488
     Region          10..34
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <24..375
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          35..57
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          58..80
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          83..105
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          106..128
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          129..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          176..199
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          200..224
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          225..247
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          248..270
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          271..293
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          294..318
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          319..339
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          342..355
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          492..604
                     /region_name="gelsolin_S1_like"
                     /note="Gelsolin sub-domain 1-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11290"
                     /db_xref="CDD:200446"
     Site            order(509..510,549,555..556,558..560,562..564,566..567,
                     578,580)
                     /site_type="other"
                     /note="putative actin binding interface [polypeptide
                     binding]"
                     /db_xref="CDD:200446"
     Region          619..706
                     /region_name="gelsolin_like"
                     /note="Tandemly repeated domains found in gelsolin,
                     severin, villin, and related proteins; cd11280"
                     /db_xref="CDD:200436"
     Region          723..837
                     /region_name="gelsolin_S3_like"
                     /note="Gelsolin sub-domain 3-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11292"
                     /db_xref="CDD:200448"
     Site            order(832,837)
                     /site_type="other"
                     /note="putative nucleotide binding site [chemical
                     binding]"
                     /db_xref="CDD:200448"
     Region          <974..1034
                     /region_name="gelsolin_like"
                     /note="Tandemly repeated domains found in gelsolin,
                     severin, villin, and related proteins; cd11280"
                     /db_xref="CDD:200436"
     Region          1053..1152
                     /region_name="gelsolin_S5_like"
                     /note="Gelsolin sub-domain 5-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11288"
                     /db_xref="CDD:200444"
     Site            1060
                     /site_type="other"
                     /note="putative nucleotide binding residue [chemical
                     binding]"
                     /db_xref="CDD:200444"
     Region          1163..1289
                     /region_name="gelsolin_S6_like"
                     /note="Gelsolin sub-domain 6-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11291"
                     /db_xref="CDD:200447"
     CDS             1..1296
                     /gene="FLII"
                     /gene_synonym="CMD2J; FLI; Fli1; FLIL"
                     /coded_by="NM_001445028.1:49..3939"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:2314"
                     /db_xref="HGNC:HGNC:3750"
                     /db_xref="MIM:600362"
ORIGIN      
        1 meatgvlpfv rgvdlsgndf kggyfpenvk amtslrwlkl nrtglcylpe elaalqkleh
       61 lsvshnnltt lhgelsslps lraivarans lknsgvpddi fklddlsvld lshnqltecp
      121 relenaknml vlnlshnsid tipnqlfinl tdllyldlse nrleslppqm rrlvhlqtlv
      181 lngnpllhaq lrqlpamtal qtlhlrstqr tqsnlptsle glsnladvdl scndltrvpe
      241 clytlpslrr lnlssnqite lslcidqwvh vetlnlsrnq ltslpsaick lsklkklyln
      301 snkldfdglp sgigkltnle efmaannnle lvpeslcrcp klrklvlnkn hlvtlpeaih
      361 flteievldv renpnlvmpp kpadraaewy nidfslqnql rlagaspatv aaaaaagsgp
      421 kdpmarkmrl rrrkdsaqdd qakqvlkgms dvaqeknkkq eesadaraps gkvrrwdqgl
      481 ekprldysef ftedvgqlpg ltiwqienfv pvlveeafhg kfyeadcyiv lktflddsgs
      541 lnweiyywig geatldkkac saihavnlrn ylgaecrtvr eemgdeseef lqvfdndisy
      601 ieggtasgfy tvedthyvtr myrvygkkni klepvplkgt sldprfvfll drgldiyvwr
      661 gaqatlsstt karlfaekin knerkgkaei tllvqgqelp efwealggep seikkhvped
      721 fwppqpklyk vglglgylel pqinyklsve hkqrpkvelm prmrllqsll dtrcvyildc
      781 wsdvfiwlgr ksprlvraaa lklgqelcgm lhrprhatvs rslegteaqv fkakfknwdd
      841 vltvdytrna eavlqspgls gkvkrdaekk dqmkadltal flprqppmsl aeaeqlmeew
      901 nedldgmegf vlegkkfarl peeefghfyt qdcyvflcry wvpveyeeee kkedkeekae
      961 gkegeeatae aeekqpeedf qcivyfwqgr easnmgwltf tfslqkkfes lfpgklevvr
     1021 mtqqqenpkf lshfkrkfii hrgkrkavqg aqqpslyqir tngsalctrc iqintdssll
     1081 nsefcfilkv pfesednqgi vyawvgrasd pdeaklaedi lntmfdtsys kqvinegeep
     1141 enffwvgiga qkpydddaey mkhtrlfrcs nekgyfavte kcsdfcqddl adddimlldn
     1201 gqevymwvgt qtsqveikls lkacqviwve ggprwacgqg rvitqgslsp cqvyiqhmrs
     1261 keherprrlr lvrkgneqha ftrcfhawsa fckala
//
LOCUS       NP_001431952             594 aa            linear   PRI 07-JAN-2026
DEFINITION  polyunsaturated fatty acid lipoxygenase ALOX12 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001431952 XP_011522082
VERSION     NP_001431952.1
DBSOURCE    REFSEQ: accession NM_001445023.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 594)
  AUTHORS   Canyelles-Nino,M., Gonzalez-Lafont,A. and Lluch,J.M.
  TITLE     Hydroperoxidation of Docosahexaenoic Acid by Human ALOX12 and
            pigALOX15-mini-LOX
  JOURNAL   Int J Mol Sci 24 (7), 6064 (2023)
   PUBMED   37047037
  REMARK    GeneRIF: Hydroperoxidation of Docosahexaenoic Acid by Human ALOX12
            and pigALOX15-mini-LOX.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 594)
  AUTHORS   Tran,M., Signorelli,R.L., Yamaguchi,A., Chen,E., Holinstat,M.,
            Iavarone,A.T., Offenbacher,A.R. and Holman,T.
  TITLE     Biochemical and hydrogen-deuterium exchange studies of the single
            nucleotide polymorphism Y649C in human platelet 12-lipoxygenase
            linked to a bleeding disorder
  JOURNAL   Arch Biochem Biophys 733, 109472 (2023)
   PUBMED   36442529
  REMARK    GeneRIF: Biochemical and hydrogen-deuterium exchange studies of the
            single nucleotide polymorphism Y649C in human platelet
            12-lipoxygenase linked to a bleeding disorder.
REFERENCE   3  (residues 1 to 594)
  AUTHORS   Weng,S., Liu,Z., Xu,H., Ge,X., Ren,Y., Dang,Q., Liu,L., Zhang,J.,
            Luo,P., Ren,J. and Han,X.
  TITLE     ALOX12: A Novel Insight in Bevacizumab Response, Immunotherapy
            Effect, and Prognosis of Colorectal Cancer
  JOURNAL   Front Immunol 13, 910582 (2022)
   PUBMED   35833141
  REMARK    GeneRIF: ALOX12: A Novel Insight in Bevacizumab Response,
            Immunotherapy Effect, and Prognosis of Colorectal Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 594)
  AUTHORS   Chen,S. and Zou,H.
  TITLE     Key Role of 12-Lipoxygenase and Its Metabolite
            12-Hydroxyeicosatetraenoic Acid (12-HETE) in Diabetic Retinopathy
  JOURNAL   Curr Eye Res 47 (3), 329-335 (2022)
   PUBMED   35129022
  REMARK    GeneRIF: Key Role of 12-Lipoxygenase and Its Metabolite
            12-Hydroxyeicosatetraenoic Acid (12-HETE) in Diabetic Retinopathy.
            Review article
REFERENCE   5  (residues 1 to 594)
  AUTHORS   Contursi,A., Schiavone,S., Dovizio,M., Hinz,C., Fullone,R.,
            Tacconelli,S., Tyrrell,V.J., Grande,R., Lanuti,P., Marchisio,M.,
            Zucchelli,M., Ballerini,P., Lanas,A., O'Donnell,V.B. and
            Patrignani,P.
  TITLE     Platelets induce free and phospholipid-esterified
            12-hydroxyeicosatetraenoic acid generation in colon cancer cells by
            delivering 12-lipoxygenase
  JOURNAL   J Lipid Res 62, 100109 (2021)
   PUBMED   34428433
  REMARK    GeneRIF: Platelets induce free and phospholipid-esterified
            12-hydroxyeicosatetraenoic acid generation in colon cancer cells by
            delivering 12-lipoxygenase.
REFERENCE   6  (residues 1 to 594)
  AUTHORS   Yoshimoto,T., Arakawa,T., Hada,T., Yamamoto,S. and Takahashi,E.
  TITLE     Structure and chromosomal localization of human arachidonate
            12-lipoxygenase gene
  JOURNAL   J Biol Chem 267 (34), 24805-24809 (1992)
   PUBMED   1447217
REFERENCE   7  (residues 1 to 594)
  AUTHORS   Funk,C.D., Funk,L.B., FitzGerald,G.A. and Samuelsson,B.
  TITLE     Characterization of human 12-lipoxygenase genes
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3962-3966 (1992)
   PUBMED   1570320
REFERENCE   8  (residues 1 to 594)
  AUTHORS   Hada,T., Ueda,N., Takahashi,Y. and Yamamoto,S.
  TITLE     Catalytic properties of human platelet 12-lipoxygenase as compared
            with the enzymes of other origins
  JOURNAL   Biochim Biophys Acta 1083 (1), 89-93 (1991)
   PUBMED   1851637
REFERENCE   9  (residues 1 to 594)
  AUTHORS   Yoshimoto,T., Yamamoto,Y., Arakawa,T., Suzuki,H., Yamamoto,S.,
            Yokoyama,C., Tanabe,T. and Toh,H.
  TITLE     Molecular cloning and expression of human arachidonate
            12-lipoxygenase
  JOURNAL   Biochem Biophys Res Commun 172 (3), 1230-1235 (1990)
   PUBMED   2244907
REFERENCE   10 (residues 1 to 594)
  AUTHORS   Izumi,T., Hoshiko,S., Radmark,O. and Samuelsson,B.
  TITLE     Cloning of the cDNA for human 12-lipoxygenase
  JOURNAL   Proc Natl Acad Sci U S A 87 (19), 7477-7481 (1990)
   PUBMED   2217179
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC040977.10.
            
            On Jan 7, 2026 this sequence version replaced XP_011522082.2.
            
            Summary: This gene encodes a member of the lipoxygenase family of
            proteins. The encoded enzyme acts on different polyunsaturated
            fatty acid substrates to generate bioactive lipid mediators
            including eicosanoids and lipoxins. The encoded enzyme and its
            reaction products have been shown to regulate platelet function.
            Elevated expression of this gene has been observed in pancreatic
            islets derived from human diabetes patients. Allelic variants in
            this gene may be associated with susceptibility to toxoplasmosis.
            Multiple pseudogenes of this gene have been identified in the human
            genome. [provided by RefSeq, Aug 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.129033.1,
                                           SRR14038196.1172379.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145893, SAMEA2147975
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..594
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..594
                     /product="polyunsaturated fatty acid lipoxygenase ALOX12
                     isoform 2"
                     /EC_number="1.13.11.31"
                     /EC_number="1.13.11.33"
                     /note="platelet 12-LOX; platelet-type 12-lipoxygenase;
                     12S-lipoxygenase; platelet-type lipoxygenase 12;
                     Arachidonate 12-lipoxygenase, 12S-type; lipoxin synthase
                     12-LO; linoleate 13S-lipoxygenase; arachidonate
                     15-lipoxygenase,15S-type; arachidonate (12S)-lipoxygenase;
                     arachidonate (15S)-lipoxygenase; polyunsaturated fatty
                     acid lipoxygenase ALOX12"
                     /calculated_mol_wt=67464
     Region          2..111
                     /region_name="PLAT_LOX"
                     /note="PLAT domain of 12/15-lipoxygenase. As a unique
                     subfamily of the mammalian lipoxygenases, they catalyze
                     enzymatic lipid peroxidation in complex biological
                     structures via direct dioxygenation of phospholipids and
                     cholesterol esters of biomembranes and...; cd01753"
                     /db_xref="CDD:238851"
     Region          <271..585
                     /region_name="Lipoxygenase"
                     /note="pfam00305"
                     /db_xref="CDD:459754"
     CDS             1..594
                     /gene="ALOX12"
                     /gene_synonym="12-LOX; 12S-LOX; LOG12"
                     /coded_by="NM_001445023.1:70..1854"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:239"
                     /db_xref="HGNC:HGNC:429"
                     /db_xref="MIM:152391"
ORIGIN      
        1 mgryrirvat gawlfsgsyn rvqlwlvgtr geaelelqlr pargeeeefd hdvaedlgll
       61 qfvrlrkhhw lvddawfcdr itvqgpgaca evafpcyrwv qgedilslpe gtarlpgdna
      121 ldmfqkhrek elkdrqqiyc watwkeglpl tiaadrkddl ppnmrfheek rldfewtlka
      181 glvlpsgmee lqaqlekelq ngslfeadfi lldgipanvi rgekqylaap lvmlkmepng
      241 klqpmviqiq ppnpssptpt lflpsdppla wllakswvrn sdfqlheiqy hllnthlvae
      301 viavatmrcl pglhpifkfl iphirytmei ntrartqlis dggifdkavs tgggghvqll
      361 rraaaqltyc slcppddlad rgllglpgal yahdalrlwe iiaryvegiv hlfyqrddiv
      421 kgdpelqawc reitevglcq aqdrgfpvsf qsqsqlchfl tmcvftctaq haainqgqld
      481 wyawvpnapc tmrmpppttk edvtmatvmg slpdvrqacl qmaiswhlsr rqpdmvplgh
      541 hkekyfsgpk pkavlnqfrt dleklekeit arneqldwpy eylkpscien svti
//
LOCUS       NP_001431913             406 aa            linear   PRI 07-JAN-2026
DEFINITION  lymphocyte antigen 6 complex locus protein G6f isoform 2 [Homo
            sapiens].
ACCESSION   NP_001431913
VERSION     NP_001431913.1
DBSOURCE    REFSEQ: accession NM_001444984.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Ucisik-Akkaya,E., Davis,C.F., Do,T.N., Morrison,B.A., Stemmer,S.M.,
            Amadio,W.J. and Dorak,M.T.
  TITLE     Examination of genetic polymorphisms in newborns for signatures of
            sex-specific prenatal selection
  JOURNAL   Mol Hum Reprod 16 (10), 770-777 (2010)
   PUBMED   20587610
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Barcellos,L.F., May,S.L., Ramsay,P.P., Quach,H.L., Lane,J.A.,
            Nititham,J., Noble,J.A., Taylor,K.E., Quach,D.L., Chung,S.A.,
            Kelly,J.A., Moser,K.L., Behrens,T.W., Seldin,M.F., Thomson,G.,
            Harley,J.B., Gaffney,P.M. and Criswell,L.A.
  TITLE     High-density SNP screening of the major histocompatibility complex
            in systemic lupus erythematosus demonstrates strong evidence for
            independent susceptibility regions
  JOURNAL   PLoS Genet 5 (10), e1000696 (2009)
   PUBMED   19851445
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Macaulay,I.C., Tijssen,M.R., Thijssen-Timmer,D.C., Gusnanto,A.,
            Steward,M., Burns,P., Langford,C.F., Ellis,P.D., Dudbridge,F.,
            Zwaginga,J.J., Watkins,N.A., van der Schoot,C.E. and Ouwehand,W.H.
  TITLE     Comparative gene expression profiling of in vitro differentiated
            megakaryocytes and erythroblasts identifies novel activatory and
            inhibitory platelet membrane proteins
  JOURNAL   Blood 109 (8), 3260-3269 (2007)
   PUBMED   17192395
REFERENCE   4  (residues 1 to 406)
  AUTHORS   De Vet,E.C., Aguado,B. and Campbell,R.D.
  TITLE     Adaptor signalling proteins Grb2 and Grb7 are recruited by human
            G6f, a novel member of the immunoglobulin superfamily encoded in
            the MHC
  JOURNAL   Biochem J 375 (Pt 1), 207-213 (2003)
   PUBMED   12852788
  REMARK    GeneRIF: G6f recruits adaptor signalling proteins Grb2 and Grb7.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL662899.5.
            
            Summary: The human G6f protein is a type I transmembrane protein
            belonging to the immunoglobin (Ig) superfamily, which is comprised
            of cell-surface proteins involved in the immune system and cellular
            recognition (de Vet et al., 2003 [PubMed 12852788]).[supplied by
            OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.104710.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968968,
                                           SAMEA2148874 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..406
                     /product="lymphocyte antigen 6 complex locus protein G6f
                     isoform 2"
                     /note="lymphocyte antigen 6 complex locus protein G6f;
                     lymphocyte antigen 6 complex, locus G6D; lymphocyte
                     antigen 6 complex, locus G6F"
                     /calculated_mol_wt=44467
     Region          1..97
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          12..16
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          26..32
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          70..74
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          84..89
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..406
                     /gene="LY6G6F"
                     /gene_synonym="C6orf21; G6f; LY6G6; LY6G6D; NG32"
                     /coded_by="NM_001444984.1:175..1395"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:259215"
                     /db_xref="HGNC:HGNC:13933"
                     /db_xref="MIM:611404"
ORIGIN      
        1 mqaiyvalge avelpcpspp tlhgdehlsw fcspaagsft tlvaqvqvgr papdpgkpgr
       61 esrlrllgny slwlegskee dagrywcavl gqhhnyqnwr vydvlvlkgs qlsaraadgs
      121 pcnvllcsvv psrrmdsvtw qegkgpvrgr vqsfwgseaa lllvcpgegl seprsrrpri
      181 irclmthnkg vsfslaasid aspalcapst gwdmpwilml lltmgqgvvi lalsivlwrq
      241 rvrgapgrda sipqfkpeiq vyenihlarl gkpnavlqlw wkpqqflqrg rdhlwrgqtp
      301 arpgtdqatw kppsdldspt sslrrspslq ssgdrvggrr dlsspqgllp grpvqqrrgk
      361 pcgpcrhfgc ssyrpdlsla rtveriggvg vekgtreqgn kghlni
//
LOCUS       NP_001431959             271 aa            linear   PRI 07-JAN-2026
DEFINITION  reticulon-2 isoform E [Homo sapiens].
ACCESSION   NP_001431959
VERSION     NP_001431959.1
DBSOURCE    REFSEQ: accession NM_001445030.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wang,G., Xu,Z., Sun,J., Liu,B., Ruan,Y., Gu,J. and Song,S.
  TITLE     O-GlcNAcylation enhances Reticulon 2 protein stability and its
            promotive effects on gastric cancer progression
  JOURNAL   Cell Signal 108, 110718 (2023)
   PUBMED   37196774
  REMARK    GeneRIF: O-GlcNAcylation enhances Reticulon 2 protein stability and
            its promotive effects on gastric cancer progression.
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Zheng,X., Lv,X., Chai,J., Huang,Y., Zhu,L. and Zhang,X.
  TITLE     RTN2, a new member of circadian clock genes identified by database
            mining and bioinformatics prediction, is highly expressed in
            ovarian cancer
  JOURNAL   Mol Med Rep 26 (5) (2022)
   PUBMED   36177918
  REMARK    GeneRIF: RTN2, a new member of circadian clock genes identified by
            database mining and bioinformatics prediction, is highly expressed
            in ovarian cancer.
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Tian,W., Zheng,H., Zhu,Z., Zhang,C., Luan,X. and Cao,L.
  TITLE     New phenotype of RTN2-related spectrum: Complicated form of spastic
            paraplegia-12
  JOURNAL   Ann Clin Transl Neurol 9 (8), 1108-1115 (2022)
   PUBMED   35684947
  REMARK    GeneRIF: New phenotype of RTN2-related spectrum: Complicated form
            of spastic paraplegia-12.
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Reid,E., Dearlove,A.M., Osborn,O., Rogers,M.T. and Rubinsztein,D.C.
  TITLE     A locus for autosomal dominant 'pure' hereditary spastic paraplegia
            maps to chromosome 19q13
  JOURNAL   Am J Hum Genet 66 (2), 728-732 (2000)
   PUBMED   10677333
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Geisler,J.G., Palmer,R.J., Stubbs,L.J. and Mucenski,M.L.
  TITLE     Nspl1, a new Z-band-associated protein
  JOURNAL   J Muscle Res Cell Motil 20 (7), 661-668 (1999)
   PUBMED   10672514
REFERENCE   8  (residues 1 to 271)
  AUTHORS   Roebroek,A.J., Contreras,B., Pauli,I.G. and Van de Ven,W.J.
  TITLE     cDNA cloning, genomic organization, and expression of the human
            RTN2 gene, a member of a gene family encoding reticulons
  JOURNAL   Genomics 51 (1), 98-106 (1998)
   PUBMED   9693037
REFERENCE   9  (residues 1 to 271)
  AUTHORS   Geisler,J.G., Stubbs,L.J., Wasserman,W.W. and Mucenski,M.L.
  TITLE     Molecular cloning of a novel mouse gene with predominant muscle and
            neural expression
  JOURNAL   Mamm Genome 9 (4), 274-282 (1998)
   PUBMED   9530622
  REMARK    GeneRIF: Discusses cloning of mouse neuroendocrine-specific
            protein-like 1, in addition to partial cloning of the human
            ortholog. Also studies expression of both the mouse and human
            genes.
REFERENCE   10 (residues 1 to 271)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC138534.2.
            
            Summary: This gene belongs to the family of reticulon encoding
            genes. Reticulons are associated with the endoplasmic reticulum,
            and are involved in neuroendocrine secretion or in membrane
            trafficking in neuroendocrine cells. Reticulon proteins also play
            an important role in the replication of positive-strand RNA (ssRNA)
            viruses. Mutations at this locus have been associated with
            autosomal dominant spastic paraplegia-12. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4352444.476995.1,
                                           ERR4352441.74305.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..271
                     /product="reticulon-2 isoform E"
                     /note="NSP-like protein 1; NSP-like protein I;
                     neuroendocrine-specific protein-like I"
                     /calculated_mol_wt=29388
     Region          71..235
                     /region_name="Reticulon"
                     /note="pfam02453"
                     /db_xref="CDD:460562"
     CDS             1..271
                     /gene="RTN2"
                     /gene_synonym="HMNR11; NSP2; NSPL1; NSPLI; SPG12"
                     /coded_by="NM_001445030.1:1093..1908"
                     /note="isoform E is encoded by transcript variant 5"
                     /db_xref="GeneID:6253"
                     /db_xref="HGNC:HGNC:10468"
                     /db_xref="MIM:603183"
ORIGIN      
        1 mewlktslll avyktvpile lspplwtaig wvqrgptppt pvlrvllkwa ksprssgvps
       61 lslgadmgsk vadllywkdt rtsgvvftgl mvsllcllhf sivsvaahla llllcgtisl
      121 rvyrkvlqav hrgdganpfq ayldvdltlt reqterlshq itsrvvsaat qlrhfflved
      181 lvdslklall fyiltfvgai fngltllilg viglftipll yrqhqaqidq yvglvtnqls
      241 hikakiraki pgtgalasaa aavsgskaka e
//
LOCUS       NP_001431958             181 aa            linear   PRI 07-JAN-2026
DEFINITION  reticulon-2 isoform D [Homo sapiens].
ACCESSION   NP_001431958
VERSION     NP_001431958.1
DBSOURCE    REFSEQ: accession NM_001445029.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Wang,G., Xu,Z., Sun,J., Liu,B., Ruan,Y., Gu,J. and Song,S.
  TITLE     O-GlcNAcylation enhances Reticulon 2 protein stability and its
            promotive effects on gastric cancer progression
  JOURNAL   Cell Signal 108, 110718 (2023)
   PUBMED   37196774
  REMARK    GeneRIF: O-GlcNAcylation enhances Reticulon 2 protein stability and
            its promotive effects on gastric cancer progression.
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Zheng,X., Lv,X., Chai,J., Huang,Y., Zhu,L. and Zhang,X.
  TITLE     RTN2, a new member of circadian clock genes identified by database
            mining and bioinformatics prediction, is highly expressed in
            ovarian cancer
  JOURNAL   Mol Med Rep 26 (5) (2022)
   PUBMED   36177918
  REMARK    GeneRIF: RTN2, a new member of circadian clock genes identified by
            database mining and bioinformatics prediction, is highly expressed
            in ovarian cancer.
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Tian,W., Zheng,H., Zhu,Z., Zhang,C., Luan,X. and Cao,L.
  TITLE     New phenotype of RTN2-related spectrum: Complicated form of spastic
            paraplegia-12
  JOURNAL   Ann Clin Transl Neurol 9 (8), 1108-1115 (2022)
   PUBMED   35684947
  REMARK    GeneRIF: New phenotype of RTN2-related spectrum: Complicated form
            of spastic paraplegia-12.
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Reid,E., Dearlove,A.M., Osborn,O., Rogers,M.T. and Rubinsztein,D.C.
  TITLE     A locus for autosomal dominant 'pure' hereditary spastic paraplegia
            maps to chromosome 19q13
  JOURNAL   Am J Hum Genet 66 (2), 728-732 (2000)
   PUBMED   10677333
REFERENCE   7  (residues 1 to 181)
  AUTHORS   Geisler,J.G., Palmer,R.J., Stubbs,L.J. and Mucenski,M.L.
  TITLE     Nspl1, a new Z-band-associated protein
  JOURNAL   J Muscle Res Cell Motil 20 (7), 661-668 (1999)
   PUBMED   10672514
REFERENCE   8  (residues 1 to 181)
  AUTHORS   Roebroek,A.J., Contreras,B., Pauli,I.G. and Van de Ven,W.J.
  TITLE     cDNA cloning, genomic organization, and expression of the human
            RTN2 gene, a member of a gene family encoding reticulons
  JOURNAL   Genomics 51 (1), 98-106 (1998)
   PUBMED   9693037
REFERENCE   9  (residues 1 to 181)
  AUTHORS   Geisler,J.G., Stubbs,L.J., Wasserman,W.W. and Mucenski,M.L.
  TITLE     Molecular cloning of a novel mouse gene with predominant muscle and
            neural expression
  JOURNAL   Mamm Genome 9 (4), 274-282 (1998)
   PUBMED   9530622
  REMARK    GeneRIF: Discusses cloning of mouse neuroendocrine-specific
            protein-like 1, in addition to partial cloning of the human
            ortholog. Also studies expression of both the mouse and human
            genes.
REFERENCE   10 (residues 1 to 181)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC138534.2.
            
            Summary: This gene belongs to the family of reticulon encoding
            genes. Reticulons are associated with the endoplasmic reticulum,
            and are involved in neuroendocrine secretion or in membrane
            trafficking in neuroendocrine cells. Reticulon proteins also play
            an important role in the replication of positive-strand RNA (ssRNA)
            viruses. Mutations at this locus have been associated with
            autosomal dominant spastic paraplegia-12. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.984756.1,
                                           ERR4352444.93388.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..181
                     /product="reticulon-2 isoform D"
                     /note="NSP-like protein 1; NSP-like protein I;
                     neuroendocrine-specific protein-like I"
                     /calculated_mol_wt=19558
     Region          4..145
                     /region_name="Reticulon"
                     /note="pfam02453"
                     /db_xref="CDD:460562"
     CDS             1..181
                     /gene="RTN2"
                     /gene_synonym="HMNR11; NSP2; NSPL1; NSPLI; SPG12"
                     /coded_by="NM_001445029.1:1171..1716"
                     /note="isoform D is encoded by transcript variant 4"
                     /db_xref="GeneID:6253"
                     /db_xref="HGNC:HGNC:10468"
                     /db_xref="MIM:603183"
ORIGIN      
        1 mvsllcllhf sivsvaahla llllcgtisl rvyrkvlqav hrgdganpfq ayldvdltlt
       61 reqterlshq itsrvvsaat qlrhfflved lvdslklall fyiltfvgai fngltllilg
      121 viglftipll yrqhqaqidq yvglvtnqls hikakiraki pgtgalasaa aavsgskaka
      181 e
//
LOCUS       NP_001431960             662 aa            linear   PRI 07-JAN-2026
DEFINITION  reticulon-2 isoform F [Homo sapiens].
ACCESSION   NP_001431960 XP_054177679
VERSION     NP_001431960.1
DBSOURCE    REFSEQ: accession NM_001445031.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Wang,G., Xu,Z., Sun,J., Liu,B., Ruan,Y., Gu,J. and Song,S.
  TITLE     O-GlcNAcylation enhances Reticulon 2 protein stability and its
            promotive effects on gastric cancer progression
  JOURNAL   Cell Signal 108, 110718 (2023)
   PUBMED   37196774
  REMARK    GeneRIF: O-GlcNAcylation enhances Reticulon 2 protein stability and
            its promotive effects on gastric cancer progression.
REFERENCE   2  (residues 1 to 662)
  AUTHORS   Zheng,X., Lv,X., Chai,J., Huang,Y., Zhu,L. and Zhang,X.
  TITLE     RTN2, a new member of circadian clock genes identified by database
            mining and bioinformatics prediction, is highly expressed in
            ovarian cancer
  JOURNAL   Mol Med Rep 26 (5) (2022)
   PUBMED   36177918
  REMARK    GeneRIF: RTN2, a new member of circadian clock genes identified by
            database mining and bioinformatics prediction, is highly expressed
            in ovarian cancer.
REFERENCE   3  (residues 1 to 662)
  AUTHORS   Tian,W., Zheng,H., Zhu,Z., Zhang,C., Luan,X. and Cao,L.
  TITLE     New phenotype of RTN2-related spectrum: Complicated form of spastic
            paraplegia-12
  JOURNAL   Ann Clin Transl Neurol 9 (8), 1108-1115 (2022)
   PUBMED   35684947
  REMARK    GeneRIF: New phenotype of RTN2-related spectrum: Complicated form
            of spastic paraplegia-12.
REFERENCE   4  (residues 1 to 662)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 662)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 662)
  AUTHORS   Reid,E., Dearlove,A.M., Osborn,O., Rogers,M.T. and Rubinsztein,D.C.
  TITLE     A locus for autosomal dominant 'pure' hereditary spastic paraplegia
            maps to chromosome 19q13
  JOURNAL   Am J Hum Genet 66 (2), 728-732 (2000)
   PUBMED   10677333
REFERENCE   7  (residues 1 to 662)
  AUTHORS   Geisler,J.G., Palmer,R.J., Stubbs,L.J. and Mucenski,M.L.
  TITLE     Nspl1, a new Z-band-associated protein
  JOURNAL   J Muscle Res Cell Motil 20 (7), 661-668 (1999)
   PUBMED   10672514
REFERENCE   8  (residues 1 to 662)
  AUTHORS   Roebroek,A.J., Contreras,B., Pauli,I.G. and Van de Ven,W.J.
  TITLE     cDNA cloning, genomic organization, and expression of the human
            RTN2 gene, a member of a gene family encoding reticulons
  JOURNAL   Genomics 51 (1), 98-106 (1998)
   PUBMED   9693037
REFERENCE   9  (residues 1 to 662)
  AUTHORS   Geisler,J.G., Stubbs,L.J., Wasserman,W.W. and Mucenski,M.L.
  TITLE     Molecular cloning of a novel mouse gene with predominant muscle and
            neural expression
  JOURNAL   Mamm Genome 9 (4), 274-282 (1998)
   PUBMED   9530622
  REMARK    GeneRIF: Discusses cloning of mouse neuroendocrine-specific
            protein-like 1, in addition to partial cloning of the human
            ortholog. Also studies expression of both the mouse and human
            genes.
REFERENCE   10 (residues 1 to 662)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC138534.2.
            
            On Jan 7, 2026 this sequence version replaced XP_054177679.1.
            
            Summary: This gene belongs to the family of reticulon encoding
            genes. Reticulons are associated with the endoplasmic reticulum,
            and are involved in neuroendocrine secretion or in membrane
            trafficking in neuroendocrine cells. Reticulon proteins also play
            an important role in the replication of positive-strand RNA (ssRNA)
            viruses. Mutations at this locus have been associated with
            autosomal dominant spastic paraplegia-12. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1559215.1,
                                           SRR14038192.129577.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..662
                     /product="reticulon-2 isoform F"
                     /note="NSP-like protein 1; NSP-like protein I;
                     neuroendocrine-specific protein-like I"
                     /calculated_mol_wt=72005
     Region          <99..304
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          462..626
                     /region_name="Reticulon"
                     /note="pfam02453"
                     /db_xref="CDD:460562"
     CDS             1..662
                     /gene="RTN2"
                     /gene_synonym="HMNR11; NSP2; NSPL1; NSPLI; SPG12"
                     /coded_by="NM_001445031.1:255..2243"
                     /note="isoform F is encoded by transcript variant 6"
                     /db_xref="GeneID:6253"
                     /db_xref="HGNC:HGNC:10468"
                     /db_xref="MIM:603183"
ORIGIN      
        1 mvppaawmrs rsrgrrgrws svlkatapar lstarespqc aryrnrgets nttavqppvs
       61 trgqrerrrs salkkarrsa srtpsgslgs gpsswstwpg kwrapkraar appwpsrtan
      121 kaqpggrpee apstasstpd steggnddsd frelhtaref seedeeetts qdwgtprelt
      181 fsyiafdgvv gsggrrdsta rrprpqgrsv seprdqhpqp slgdslesip slsqspepgr
      241 rgdpdtapps erpledlrlr ldhlgwvarg tgsgedssts sstpledeep qepnrletge
      301 ageeldlrlr laqpsspevl tpqlspgsgt pqagtpspsr srdsnsgpee plleeeekqw
      361 gplerepvrg qcldstdqle ftveprllgt amewlktsll lavyktvpil elspplwtai
      421 gwvqrgptpp tpvlrvllkw aksprssgvp slslgadmgs kvadllywkd trtsgvvftg
      481 lmvsllcllh fsivsvaahl allllcgtis lrvyrkvlqa vhrgdganpf qayldvdltl
      541 treqterlsh qitsrvvsaa tqlrhfflve dlvdslklal lfyiltfvga ifngltllil
      601 gviglftipl lyrqhqaqid qyvglvtnql shikakirak ipgtgalasa aaavsgskak
      661 ae
//
LOCUS       NP_001431963             271 aa            linear   PRI 07-JAN-2026
DEFINITION  reticulon-2 isoform E [Homo sapiens].
ACCESSION   NP_001431963
VERSION     NP_001431963.1
DBSOURCE    REFSEQ: accession NM_001445034.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Wang,G., Xu,Z., Sun,J., Liu,B., Ruan,Y., Gu,J. and Song,S.
  TITLE     O-GlcNAcylation enhances Reticulon 2 protein stability and its
            promotive effects on gastric cancer progression
  JOURNAL   Cell Signal 108, 110718 (2023)
   PUBMED   37196774
  REMARK    GeneRIF: O-GlcNAcylation enhances Reticulon 2 protein stability and
            its promotive effects on gastric cancer progression.
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Zheng,X., Lv,X., Chai,J., Huang,Y., Zhu,L. and Zhang,X.
  TITLE     RTN2, a new member of circadian clock genes identified by database
            mining and bioinformatics prediction, is highly expressed in
            ovarian cancer
  JOURNAL   Mol Med Rep 26 (5) (2022)
   PUBMED   36177918
  REMARK    GeneRIF: RTN2, a new member of circadian clock genes identified by
            database mining and bioinformatics prediction, is highly expressed
            in ovarian cancer.
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Tian,W., Zheng,H., Zhu,Z., Zhang,C., Luan,X. and Cao,L.
  TITLE     New phenotype of RTN2-related spectrum: Complicated form of spastic
            paraplegia-12
  JOURNAL   Ann Clin Transl Neurol 9 (8), 1108-1115 (2022)
   PUBMED   35684947
  REMARK    GeneRIF: New phenotype of RTN2-related spectrum: Complicated form
            of spastic paraplegia-12.
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Reid,E., Dearlove,A.M., Osborn,O., Rogers,M.T. and Rubinsztein,D.C.
  TITLE     A locus for autosomal dominant 'pure' hereditary spastic paraplegia
            maps to chromosome 19q13
  JOURNAL   Am J Hum Genet 66 (2), 728-732 (2000)
   PUBMED   10677333
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Geisler,J.G., Palmer,R.J., Stubbs,L.J. and Mucenski,M.L.
  TITLE     Nspl1, a new Z-band-associated protein
  JOURNAL   J Muscle Res Cell Motil 20 (7), 661-668 (1999)
   PUBMED   10672514
REFERENCE   8  (residues 1 to 271)
  AUTHORS   Roebroek,A.J., Contreras,B., Pauli,I.G. and Van de Ven,W.J.
  TITLE     cDNA cloning, genomic organization, and expression of the human
            RTN2 gene, a member of a gene family encoding reticulons
  JOURNAL   Genomics 51 (1), 98-106 (1998)
   PUBMED   9693037
REFERENCE   9  (residues 1 to 271)
  AUTHORS   Geisler,J.G., Stubbs,L.J., Wasserman,W.W. and Mucenski,M.L.
  TITLE     Molecular cloning of a novel mouse gene with predominant muscle and
            neural expression
  JOURNAL   Mamm Genome 9 (4), 274-282 (1998)
   PUBMED   9530622
  REMARK    GeneRIF: Discusses cloning of mouse neuroendocrine-specific
            protein-like 1, in addition to partial cloning of the human
            ortholog. Also studies expression of both the mouse and human
            genes.
REFERENCE   10 (residues 1 to 271)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC138534.2.
            
            Summary: This gene belongs to the family of reticulon encoding
            genes. Reticulons are associated with the endoplasmic reticulum,
            and are involved in neuroendocrine secretion or in membrane
            trafficking in neuroendocrine cells. Reticulon proteins also play
            an important role in the replication of positive-strand RNA (ssRNA)
            viruses. Mutations at this locus have been associated with
            autosomal dominant spastic paraplegia-12. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2157512.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2145743,
                                           SAMEA2162568 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..271
                     /product="reticulon-2 isoform E"
                     /note="NSP-like protein 1; NSP-like protein I;
                     neuroendocrine-specific protein-like I"
                     /calculated_mol_wt=29388
     Region          71..235
                     /region_name="Reticulon"
                     /note="pfam02453"
                     /db_xref="CDD:460562"
     CDS             1..271
                     /gene="RTN2"
                     /gene_synonym="HMNR11; NSP2; NSPL1; NSPLI; SPG12"
                     /coded_by="NM_001445034.1:1273..2088"
                     /note="isoform E is encoded by transcript variant 9"
                     /db_xref="GeneID:6253"
                     /db_xref="HGNC:HGNC:10468"
                     /db_xref="MIM:603183"
ORIGIN      
        1 mewlktslll avyktvpile lspplwtaig wvqrgptppt pvlrvllkwa ksprssgvps
       61 lslgadmgsk vadllywkdt rtsgvvftgl mvsllcllhf sivsvaahla llllcgtisl
      121 rvyrkvlqav hrgdganpfq ayldvdltlt reqterlshq itsrvvsaat qlrhfflved
      181 lvdslklall fyiltfvgai fngltllilg viglftipll yrqhqaqidq yvglvtnqls
      241 hikakiraki pgtgalasaa aavsgskaka e
//
LOCUS       NP_001431961             589 aa            linear   PRI 07-JAN-2026
DEFINITION  reticulon-2 isoform G [Homo sapiens].
ACCESSION   NP_001431961 XP_054177680
VERSION     NP_001431961.1
DBSOURCE    REFSEQ: accession NM_001445032.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Wang,G., Xu,Z., Sun,J., Liu,B., Ruan,Y., Gu,J. and Song,S.
  TITLE     O-GlcNAcylation enhances Reticulon 2 protein stability and its
            promotive effects on gastric cancer progression
  JOURNAL   Cell Signal 108, 110718 (2023)
   PUBMED   37196774
  REMARK    GeneRIF: O-GlcNAcylation enhances Reticulon 2 protein stability and
            its promotive effects on gastric cancer progression.
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Zheng,X., Lv,X., Chai,J., Huang,Y., Zhu,L. and Zhang,X.
  TITLE     RTN2, a new member of circadian clock genes identified by database
            mining and bioinformatics prediction, is highly expressed in
            ovarian cancer
  JOURNAL   Mol Med Rep 26 (5) (2022)
   PUBMED   36177918
  REMARK    GeneRIF: RTN2, a new member of circadian clock genes identified by
            database mining and bioinformatics prediction, is highly expressed
            in ovarian cancer.
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Tian,W., Zheng,H., Zhu,Z., Zhang,C., Luan,X. and Cao,L.
  TITLE     New phenotype of RTN2-related spectrum: Complicated form of spastic
            paraplegia-12
  JOURNAL   Ann Clin Transl Neurol 9 (8), 1108-1115 (2022)
   PUBMED   35684947
  REMARK    GeneRIF: New phenotype of RTN2-related spectrum: Complicated form
            of spastic paraplegia-12.
REFERENCE   4  (residues 1 to 589)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 589)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 589)
  AUTHORS   Reid,E., Dearlove,A.M., Osborn,O., Rogers,M.T. and Rubinsztein,D.C.
  TITLE     A locus for autosomal dominant 'pure' hereditary spastic paraplegia
            maps to chromosome 19q13
  JOURNAL   Am J Hum Genet 66 (2), 728-732 (2000)
   PUBMED   10677333
REFERENCE   7  (residues 1 to 589)
  AUTHORS   Geisler,J.G., Palmer,R.J., Stubbs,L.J. and Mucenski,M.L.
  TITLE     Nspl1, a new Z-band-associated protein
  JOURNAL   J Muscle Res Cell Motil 20 (7), 661-668 (1999)
   PUBMED   10672514
REFERENCE   8  (residues 1 to 589)
  AUTHORS   Roebroek,A.J., Contreras,B., Pauli,I.G. and Van de Ven,W.J.
  TITLE     cDNA cloning, genomic organization, and expression of the human
            RTN2 gene, a member of a gene family encoding reticulons
  JOURNAL   Genomics 51 (1), 98-106 (1998)
   PUBMED   9693037
REFERENCE   9  (residues 1 to 589)
  AUTHORS   Geisler,J.G., Stubbs,L.J., Wasserman,W.W. and Mucenski,M.L.
  TITLE     Molecular cloning of a novel mouse gene with predominant muscle and
            neural expression
  JOURNAL   Mamm Genome 9 (4), 274-282 (1998)
   PUBMED   9530622
  REMARK    GeneRIF: Discusses cloning of mouse neuroendocrine-specific
            protein-like 1, in addition to partial cloning of the human
            ortholog. Also studies expression of both the mouse and human
            genes.
REFERENCE   10 (residues 1 to 589)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC138534.2.
            
            On Jan 7, 2026 this sequence version replaced XP_054177680.1.
            
            Summary: This gene belongs to the family of reticulon encoding
            genes. Reticulons are associated with the endoplasmic reticulum,
            and are involved in neuroendocrine secretion or in membrane
            trafficking in neuroendocrine cells. Reticulon proteins also play
            an important role in the replication of positive-strand RNA (ssRNA)
            viruses. Mutations at this locus have been associated with
            autosomal dominant spastic paraplegia-12. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3223471.1,
                                           SRR18074967.3367774.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..589
                     /product="reticulon-2 isoform G"
                     /note="NSP-like protein 1; NSP-like protein I;
                     neuroendocrine-specific protein-like I"
                     /calculated_mol_wt=64170
     Region          <99..304
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          389..553
                     /region_name="Reticulon"
                     /note="pfam02453"
                     /db_xref="CDD:460562"
     CDS             1..589
                     /gene="RTN2"
                     /gene_synonym="HMNR11; NSP2; NSPL1; NSPLI; SPG12"
                     /coded_by="NM_001445032.1:255..2024"
                     /note="isoform G is encoded by transcript variant 7"
                     /db_xref="GeneID:6253"
                     /db_xref="HGNC:HGNC:10468"
                     /db_xref="MIM:603183"
ORIGIN      
        1 mvppaawmrs rsrgrrgrws svlkatapar lstarespqc aryrnrgets nttavqppvs
       61 trgqrerrrs salkkarrsa srtpsgslgs gpsswstwpg kwrapkraar appwpsrtan
      121 kaqpggrpee apstasstpd steggnddsd frelhtaref seedeeetts qdwgtprelt
      181 fsyiafdgvv gsggrrdsta rrprpqgrsv seprdqhpqp slgdslesip slsqspepgr
      241 rgdpdtapps erpledlrlr ldhlgwvarg tgsgedssts sstpledeep qepnrletge
      301 ageeldlrlr laqpsspevl tpqlspgsgt pqagtpspsr srdsnsgpee plleeeekqw
      361 gplerepvrg qcldstdqle ftveprllva dllywkdtrt sgvvftglmv sllcllhfsi
      421 vsvaahlall llcgtislrv yrkvlqavhr gdganpfqay ldvdltltre qterlshqit
      481 srvvsaatql rhfflvedlv dslklallfy iltfvgaifn gltllilgvi glftipllyr
      541 qhqaqidqyv glvtnqlshi kakirakipg tgalasaaaa vsgskakae
//
LOCUS       NP_001431962             181 aa            linear   PRI 07-JAN-2026
DEFINITION  reticulon-2 isoform D [Homo sapiens].
ACCESSION   NP_001431962
VERSION     NP_001431962.1
DBSOURCE    REFSEQ: accession NM_001445033.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Wang,G., Xu,Z., Sun,J., Liu,B., Ruan,Y., Gu,J. and Song,S.
  TITLE     O-GlcNAcylation enhances Reticulon 2 protein stability and its
            promotive effects on gastric cancer progression
  JOURNAL   Cell Signal 108, 110718 (2023)
   PUBMED   37196774
  REMARK    GeneRIF: O-GlcNAcylation enhances Reticulon 2 protein stability and
            its promotive effects on gastric cancer progression.
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Zheng,X., Lv,X., Chai,J., Huang,Y., Zhu,L. and Zhang,X.
  TITLE     RTN2, a new member of circadian clock genes identified by database
            mining and bioinformatics prediction, is highly expressed in
            ovarian cancer
  JOURNAL   Mol Med Rep 26 (5) (2022)
   PUBMED   36177918
  REMARK    GeneRIF: RTN2, a new member of circadian clock genes identified by
            database mining and bioinformatics prediction, is highly expressed
            in ovarian cancer.
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Tian,W., Zheng,H., Zhu,Z., Zhang,C., Luan,X. and Cao,L.
  TITLE     New phenotype of RTN2-related spectrum: Complicated form of spastic
            paraplegia-12
  JOURNAL   Ann Clin Transl Neurol 9 (8), 1108-1115 (2022)
   PUBMED   35684947
  REMARK    GeneRIF: New phenotype of RTN2-related spectrum: Complicated form
            of spastic paraplegia-12.
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Reid,E., Dearlove,A.M., Osborn,O., Rogers,M.T. and Rubinsztein,D.C.
  TITLE     A locus for autosomal dominant 'pure' hereditary spastic paraplegia
            maps to chromosome 19q13
  JOURNAL   Am J Hum Genet 66 (2), 728-732 (2000)
   PUBMED   10677333
REFERENCE   7  (residues 1 to 181)
  AUTHORS   Geisler,J.G., Palmer,R.J., Stubbs,L.J. and Mucenski,M.L.
  TITLE     Nspl1, a new Z-band-associated protein
  JOURNAL   J Muscle Res Cell Motil 20 (7), 661-668 (1999)
   PUBMED   10672514
REFERENCE   8  (residues 1 to 181)
  AUTHORS   Roebroek,A.J., Contreras,B., Pauli,I.G. and Van de Ven,W.J.
  TITLE     cDNA cloning, genomic organization, and expression of the human
            RTN2 gene, a member of a gene family encoding reticulons
  JOURNAL   Genomics 51 (1), 98-106 (1998)
   PUBMED   9693037
REFERENCE   9  (residues 1 to 181)
  AUTHORS   Geisler,J.G., Stubbs,L.J., Wasserman,W.W. and Mucenski,M.L.
  TITLE     Molecular cloning of a novel mouse gene with predominant muscle and
            neural expression
  JOURNAL   Mamm Genome 9 (4), 274-282 (1998)
   PUBMED   9530622
  REMARK    GeneRIF: Discusses cloning of mouse neuroendocrine-specific
            protein-like 1, in addition to partial cloning of the human
            ortholog. Also studies expression of both the mouse and human
            genes.
REFERENCE   10 (residues 1 to 181)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC138534.2.
            
            Summary: This gene belongs to the family of reticulon encoding
            genes. Reticulons are associated with the endoplasmic reticulum,
            and are involved in neuroendocrine secretion or in membrane
            trafficking in neuroendocrine cells. Reticulon proteins also play
            an important role in the replication of positive-strand RNA (ssRNA)
            viruses. Mutations at this locus have been associated with
            autosomal dominant spastic paraplegia-12. [provided by RefSeq, Aug
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR12921934.4434015.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2145743,
                                           SAMEA2162568 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..181
                     /product="reticulon-2 isoform D"
                     /note="NSP-like protein 1; NSP-like protein I;
                     neuroendocrine-specific protein-like I"
                     /calculated_mol_wt=19558
     Region          4..145
                     /region_name="Reticulon"
                     /note="pfam02453"
                     /db_xref="CDD:460562"
     CDS             1..181
                     /gene="RTN2"
                     /gene_synonym="HMNR11; NSP2; NSPL1; NSPLI; SPG12"
                     /coded_by="NM_001445033.1:1095..1640"
                     /note="isoform D is encoded by transcript variant 8"
                     /db_xref="GeneID:6253"
                     /db_xref="HGNC:HGNC:10468"
                     /db_xref="MIM:603183"
ORIGIN      
        1 mvsllcllhf sivsvaahla llllcgtisl rvyrkvlqav hrgdganpfq ayldvdltlt
       61 reqterlshq itsrvvsaat qlrhfflved lvdslklall fyiltfvgai fngltllilg
      121 viglftipll yrqhqaqidq yvglvtnqls hikakiraki pgtgalasaa aavsgskaka
      181 e
//
LOCUS       NP_001431964             181 aa            linear   PRI 07-JAN-2026
DEFINITION  OPA3-RTN2 readthrough [Homo sapiens].
ACCESSION   NP_001431964
VERSION     NP_001431964.1
DBSOURCE    REFSEQ: accession NM_001445035.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011480.3, AC006117.1 and AC138534.2.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..181
                     /product="OPA3-RTN2 readthrough"
                     /calculated_mol_wt=19558
     Region          4..145
                     /region_name="Reticulon"
                     /note="pfam02453"
                     /db_xref="CDD:460562"
     CDS             1..181
                     /gene="OPA3-RTN2"
                     /coded_by="NM_001445035.1:1884..2429"
                     /db_xref="GeneID:144667540"
ORIGIN      
        1 mvsllcllhf sivsvaahla llllcgtisl rvyrkvlqav hrgdganpfq ayldvdltlt
       61 reqterlshq itsrvvsaat qlrhfflved lvdslklall fyiltfvgai fngltllilg
      121 viglftipll yrqhqaqidq yvglvtnqls hikakiraki pgtgalasaa aavsgskaka
      181 e
//
LOCUS       NP_001431965             181 aa            linear   PRI 07-JAN-2026
DEFINITION  OPA3-RTN2 readthrough [Homo sapiens].
ACCESSION   NP_001431965
VERSION     NP_001431965.1
DBSOURCE    REFSEQ: accession NM_001445036.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011480.3, AC006117.1 and AC138534.2.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..181
                     /product="OPA3-RTN2 readthrough"
                     /calculated_mol_wt=19558
     Region          4..145
                     /region_name="Reticulon"
                     /note="pfam02453"
                     /db_xref="CDD:460562"
     CDS             1..181
                     /gene="OPA3-RTN2"
                     /coded_by="NM_001445036.1:1242..1787"
                     /db_xref="GeneID:144667540"
ORIGIN      
        1 mvsllcllhf sivsvaahla llllcgtisl rvyrkvlqav hrgdganpfq ayldvdltlt
       61 reqterlshq itsrvvsaat qlrhfflved lvdslklall fyiltfvgai fngltllilg
      121 viglftipll yrqhqaqidq yvglvtnqls hikakiraki pgtgalasaa aavsgskaka
      181 e
//
LOCUS       NP_001382167             218 aa            linear   PRI 07-JAN-2026
DEFINITION  transmembrane protein 217 isoform 4 [Homo sapiens].
ACCESSION   NP_001382167
VERSION     NP_001382167.1
DBSOURCE    REFSEQ: accession NM_001395238.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Goes,F.S., Hamshere,M.L., Seifuddin,F., Pirooznia,M.,
            Belmonte-Mahon,P., Breuer,R., Schulze,T., Nothen,M., Cichon,S.,
            Rietschel,M., Holmans,P., Zandi,P.P., Craddock,N. and Potash,J.B.
  CONSRTM   Bipolar Genome Study (BiGS)
  TITLE     Genome-wide association of mood-incongruent psychotic bipolar
            disorder
  JOURNAL   Transl Psychiatry 2 (10), e180 (2012)
   PUBMED   23092984
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Chapuis,J., Hot,D., Hansmannel,F., Kerdraon,O., Ferreira,S.,
            Hubans,C., Maurage,C.A., Huot,L., Bensemain,F., Laumet,G.,
            Ayral,A.M., Fievet,N., Hauw,J.J., DeKosky,S.T., Lemoine,Y.,
            Iwatsubo,T., Wavrant-Devrieze,F., Dartigues,J.F., Tzourio,C.,
            Buee,L., Pasquier,F., Berr,C., Mann,D., Lendon,C., Alperovitch,A.,
            Kamboh,M.I., Amouyel,P. and Lambert,J.C.
  TITLE     Transcriptomic and genetic studies identify IL-33 as a candidate
            gene for Alzheimer's disease
  JOURNAL   Mol Psychiatry 14 (11), 1004-1016 (2009)
   PUBMED   19204726
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Dailey,H.A. and Strittmatter,P.
  TITLE     Modification and identification of cytochrome b5 carboxyl groups
            involved in protein-protein interaction with cytochrome b5
            reductase
  JOURNAL   J Biol Chem 254 (12), 5388-5396 (1979)
   PUBMED   221468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL353579.17.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803617.314414.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968968, SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..218
                     /product="transmembrane protein 217 isoform 4"
                     /calculated_mol_wt=25246
     Region          11..171
                     /region_name="DUF4534"
                     /note="Protein of unknown function (DUF4534); pfam15049"
                     /db_xref="CDD:464470"
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            67..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     CDS             1..218
                     /gene="TMEM217"
                     /gene_synonym="C6orf128; dJ355M6.2"
                     /coded_by="NM_001395238.1:594..1250"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:221468"
                     /db_xref="HGNC:HGNC:21238"
                     /db_xref="MIM:621459"
ORIGIN      
        1 mkqqqwcgmt akmgtvlsgv ftimavdmyl ifeqkhlgng scteitpkyr gasniinnfi
       61 icwsfkivlf lsfitilisc fllysvyaqi frglviyivw iffyetanvv iqiltnndfd
      121 ikevrimrwf glvsrtvmhc fwmffvinya hityknrsqg niisykrris taeilhsrnk
      181 rlsissgfsg shlesqyfer qretstwlva ggalvkqv
//
LOCUS       NP_001358484             211 aa            linear   PRI 07-JAN-2026
DEFINITION  transmembrane protein 217 isoform 3 [Homo sapiens].
ACCESSION   NP_001358484 XP_024302121
VERSION     NP_001358484.1
DBSOURCE    REFSEQ: accession NM_001371555.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Goes,F.S., Hamshere,M.L., Seifuddin,F., Pirooznia,M.,
            Belmonte-Mahon,P., Breuer,R., Schulze,T., Nothen,M., Cichon,S.,
            Rietschel,M., Holmans,P., Zandi,P.P., Craddock,N. and Potash,J.B.
  CONSRTM   Bipolar Genome Study (BiGS)
  TITLE     Genome-wide association of mood-incongruent psychotic bipolar
            disorder
  JOURNAL   Transl Psychiatry 2 (10), e180 (2012)
   PUBMED   23092984
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Chapuis,J., Hot,D., Hansmannel,F., Kerdraon,O., Ferreira,S.,
            Hubans,C., Maurage,C.A., Huot,L., Bensemain,F., Laumet,G.,
            Ayral,A.M., Fievet,N., Hauw,J.J., DeKosky,S.T., Lemoine,Y.,
            Iwatsubo,T., Wavrant-Devrieze,F., Dartigues,J.F., Tzourio,C.,
            Buee,L., Pasquier,F., Berr,C., Mann,D., Lendon,C., Alperovitch,A.,
            Kamboh,M.I., Amouyel,P. and Lambert,J.C.
  TITLE     Transcriptomic and genetic studies identify IL-33 as a candidate
            gene for Alzheimer's disease
  JOURNAL   Mol Psychiatry 14 (11), 1004-1016 (2009)
   PUBMED   19204726
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Dailey,H.A. and Strittmatter,P.
  TITLE     Modification and identification of cytochrome b5 carboxyl groups
            involved in protein-protein interaction with cytochrome b5
            reductase
  JOURNAL   J Biol Chem 254 (12), 5388-5396 (1979)
   PUBMED   221468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL353579.17.
            
            On Jul 18, 2019 this sequence version replaced XP_024302121.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.141756.1,
                                           SRR6380200.55936.9 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..211
                     /product="transmembrane protein 217 isoform 3"
                     /calculated_mol_wt=24566
     Region          11..171
                     /region_name="DUF4534"
                     /note="Protein of unknown function (DUF4534); pfam15049"
                     /db_xref="CDD:464470"
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            67..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     CDS             1..211
                     /gene="TMEM217"
                     /gene_synonym="C6orf128; dJ355M6.2"
                     /coded_by="NM_001371555.1:49..684"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS69102.1"
                     /db_xref="GeneID:221468"
                     /db_xref="HGNC:HGNC:21238"
                     /db_xref="MIM:621459"
ORIGIN      
        1 mkqqqwcgmt akmgtvlsgv ftimavdmyl ifeqkhlgng scteitpkyr gasniinnfi
       61 icwsfkivlf lsfitilisc fllysvyaqi frglviyivw iffyetanvv iqiltnndfd
      121 ikevrimrwf glvsrtvmhc fwmffvinya hityknrsqg niisykrris taeilhsrnk
      181 rlsissgfsg shlesqyfer qrrcsgktsi k
//
LOCUS       NP_660359                229 aa            linear   PRI 07-JAN-2026
DEFINITION  transmembrane protein 217 isoform 1 [Homo sapiens].
ACCESSION   NP_660359
VERSION     NP_660359.2
DBSOURCE    REFSEQ: accession NM_145316.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Goes,F.S., Hamshere,M.L., Seifuddin,F., Pirooznia,M.,
            Belmonte-Mahon,P., Breuer,R., Schulze,T., Nothen,M., Cichon,S.,
            Rietschel,M., Holmans,P., Zandi,P.P., Craddock,N. and Potash,J.B.
  CONSRTM   Bipolar Genome Study (BiGS)
  TITLE     Genome-wide association of mood-incongruent psychotic bipolar
            disorder
  JOURNAL   Transl Psychiatry 2 (10), e180 (2012)
   PUBMED   23092984
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Chapuis,J., Hot,D., Hansmannel,F., Kerdraon,O., Ferreira,S.,
            Hubans,C., Maurage,C.A., Huot,L., Bensemain,F., Laumet,G.,
            Ayral,A.M., Fievet,N., Hauw,J.J., DeKosky,S.T., Lemoine,Y.,
            Iwatsubo,T., Wavrant-Devrieze,F., Dartigues,J.F., Tzourio,C.,
            Buee,L., Pasquier,F., Berr,C., Mann,D., Lendon,C., Alperovitch,A.,
            Kamboh,M.I., Amouyel,P. and Lambert,J.C.
  TITLE     Transcriptomic and genetic studies identify IL-33 as a candidate
            gene for Alzheimer's disease
  JOURNAL   Mol Psychiatry 14 (11), 1004-1016 (2009)
   PUBMED   19204726
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Dailey,H.A. and Strittmatter,P.
  TITLE     Modification and identification of cytochrome b5 carboxyl groups
            involved in protein-protein interaction with cytochrome b5
            reductase
  JOURNAL   J Biol Chem 254 (12), 5388-5396 (1979)
   PUBMED   221468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB458508.1, AK098666.1 and AL353579.17.
            
            On Jun 9, 2003 this sequence version replaced NP_660359.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.363785.1, AK098666.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..229
                     /product="transmembrane protein 217 isoform 1"
                     /calculated_mol_wt=26451
     Region          11..171
                     /region_name="DUF4534"
                     /note="Protein of unknown function (DUF4534); pfam15049"
                     /db_xref="CDD:464470"
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            67..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     CDS             1..229
                     /gene="TMEM217"
                     /gene_synonym="C6orf128; dJ355M6.2"
                     /coded_by="NM_145316.4:44..733"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4831.1"
                     /db_xref="GeneID:221468"
                     /db_xref="HGNC:HGNC:21238"
                     /db_xref="MIM:621459"
ORIGIN      
        1 mkqqqwcgmt akmgtvlsgv ftimavdmyl ifeqkhlgng scteitpkyr gasniinnfi
       61 icwsfkivlf lsfitilisc fllysvyaqi frglviyivw iffyetanvv iqiltnndfd
      121 ikevrimrwf glvsrtvmhc fwmffvinya hityknrsqg niisykrris taeilhsrnk
      181 rlsissgfsg shlesqyfer qsfhtsiftc lspvpssaps tcrytidvc
//
LOCUS       NP_001156372             202 aa            linear   PRI 07-JAN-2026
DEFINITION  transmembrane protein 217 isoform 2 [Homo sapiens].
ACCESSION   NP_001156372
VERSION     NP_001156372.1
DBSOURCE    REFSEQ: accession NM_001162900.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Goes,F.S., Hamshere,M.L., Seifuddin,F., Pirooznia,M.,
            Belmonte-Mahon,P., Breuer,R., Schulze,T., Nothen,M., Cichon,S.,
            Rietschel,M., Holmans,P., Zandi,P.P., Craddock,N. and Potash,J.B.
  CONSRTM   Bipolar Genome Study (BiGS)
  TITLE     Genome-wide association of mood-incongruent psychotic bipolar
            disorder
  JOURNAL   Transl Psychiatry 2 (10), e180 (2012)
   PUBMED   23092984
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Chapuis,J., Hot,D., Hansmannel,F., Kerdraon,O., Ferreira,S.,
            Hubans,C., Maurage,C.A., Huot,L., Bensemain,F., Laumet,G.,
            Ayral,A.M., Fievet,N., Hauw,J.J., DeKosky,S.T., Lemoine,Y.,
            Iwatsubo,T., Wavrant-Devrieze,F., Dartigues,J.F., Tzourio,C.,
            Buee,L., Pasquier,F., Berr,C., Mann,D., Lendon,C., Alperovitch,A.,
            Kamboh,M.I., Amouyel,P. and Lambert,J.C.
  TITLE     Transcriptomic and genetic studies identify IL-33 as a candidate
            gene for Alzheimer's disease
  JOURNAL   Mol Psychiatry 14 (11), 1004-1016 (2009)
   PUBMED   19204726
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Dailey,H.A. and Strittmatter,P.
  TITLE     Modification and identification of cytochrome b5 carboxyl groups
            involved in protein-protein interaction with cytochrome b5
            reductase
  JOURNAL   J Biol Chem 254 (12), 5388-5396 (1979)
   PUBMED   221468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL353579.17.
            
            Transcript Variant: This variant (2) uses an alternate splice
            pattern in the 3' coding region, compared to variant 1. The
            resulting isoform (2) has a shorter and distinct C-terminus,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC009625.1, BG285024.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..202
                     /product="transmembrane protein 217 isoform 2"
                     /calculated_mol_wt=23605
     Region          11..171
                     /region_name="DUF4534"
                     /note="Protein of unknown function (DUF4534); pfam15049"
                     /db_xref="CDD:464470"
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            67..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     CDS             1..202
                     /gene="TMEM217"
                     /gene_synonym="C6orf128; dJ355M6.2"
                     /coded_by="NM_001162900.3:594..1202"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS93908.1"
                     /db_xref="GeneID:221468"
                     /db_xref="HGNC:HGNC:21238"
                     /db_xref="MIM:621459"
ORIGIN      
        1 mkqqqwcgmt akmgtvlsgv ftimavdmyl ifeqkhlgng scteitpkyr gasniinnfi
       61 icwsfkivlf lsfitilisc fllysvyaqi frglviyivw iffyetanvv iqiltnndfd
      121 ikevrimrwf glvsrtvmhc fwmffvinya hityknrsqg niisykrris taeilhsrnk
      181 rlsissgfsg shlesqyfer qr
//
LOCUS       NP_001382171             127 aa            linear   PRI 07-JAN-2026
DEFINITION  transmembrane protein 217 isoform 5 [Homo sapiens].
ACCESSION   NP_001382171
VERSION     NP_001382171.1
DBSOURCE    REFSEQ: accession NM_001395242.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Goes,F.S., Hamshere,M.L., Seifuddin,F., Pirooznia,M.,
            Belmonte-Mahon,P., Breuer,R., Schulze,T., Nothen,M., Cichon,S.,
            Rietschel,M., Holmans,P., Zandi,P.P., Craddock,N. and Potash,J.B.
  CONSRTM   Bipolar Genome Study (BiGS)
  TITLE     Genome-wide association of mood-incongruent psychotic bipolar
            disorder
  JOURNAL   Transl Psychiatry 2 (10), e180 (2012)
   PUBMED   23092984
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Chapuis,J., Hot,D., Hansmannel,F., Kerdraon,O., Ferreira,S.,
            Hubans,C., Maurage,C.A., Huot,L., Bensemain,F., Laumet,G.,
            Ayral,A.M., Fievet,N., Hauw,J.J., DeKosky,S.T., Lemoine,Y.,
            Iwatsubo,T., Wavrant-Devrieze,F., Dartigues,J.F., Tzourio,C.,
            Buee,L., Pasquier,F., Berr,C., Mann,D., Lendon,C., Alperovitch,A.,
            Kamboh,M.I., Amouyel,P. and Lambert,J.C.
  TITLE     Transcriptomic and genetic studies identify IL-33 as a candidate
            gene for Alzheimer's disease
  JOURNAL   Mol Psychiatry 14 (11), 1004-1016 (2009)
   PUBMED   19204726
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Dailey,H.A. and Strittmatter,P.
  TITLE     Modification and identification of cytochrome b5 carboxyl groups
            involved in protein-protein interaction with cytochrome b5
            reductase
  JOURNAL   J Biol Chem 254 (12), 5388-5396 (1979)
   PUBMED   221468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL353579.17.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..127
                     /product="transmembrane protein 217 isoform 5"
                     /calculated_mol_wt=14618
     Region          11..>123
                     /region_name="DUF4534"
                     /note="Protein of unknown function (DUF4534); pfam15049"
                     /db_xref="CDD:464470"
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            67..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     CDS             1..127
                     /gene="TMEM217"
                     /gene_synonym="C6orf128; dJ355M6.2"
                     /coded_by="NM_001395242.1:589..972"
                     /note="isoform 5 is encoded by transcript variant 10"
                     /db_xref="GeneID:221468"
                     /db_xref="HGNC:HGNC:21238"
                     /db_xref="MIM:621459"
ORIGIN      
        1 mkqqqwcgmt akmgtvlsgv ftimavdmyl ifeqkhlgng scteitpkyr gasniinnfi
       61 icwsfkivlf lsfitilisc fllysvyaqi frglviyivw iffyetanvv iqiltnndfd
      121 ikeevlw
//
LOCUS       NP_001382169             202 aa            linear   PRI 07-JAN-2026
DEFINITION  transmembrane protein 217 isoform 2 [Homo sapiens].
ACCESSION   NP_001382169
VERSION     NP_001382169.1
DBSOURCE    REFSEQ: accession NM_001395240.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Goes,F.S., Hamshere,M.L., Seifuddin,F., Pirooznia,M.,
            Belmonte-Mahon,P., Breuer,R., Schulze,T., Nothen,M., Cichon,S.,
            Rietschel,M., Holmans,P., Zandi,P.P., Craddock,N. and Potash,J.B.
  CONSRTM   Bipolar Genome Study (BiGS)
  TITLE     Genome-wide association of mood-incongruent psychotic bipolar
            disorder
  JOURNAL   Transl Psychiatry 2 (10), e180 (2012)
   PUBMED   23092984
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Chapuis,J., Hot,D., Hansmannel,F., Kerdraon,O., Ferreira,S.,
            Hubans,C., Maurage,C.A., Huot,L., Bensemain,F., Laumet,G.,
            Ayral,A.M., Fievet,N., Hauw,J.J., DeKosky,S.T., Lemoine,Y.,
            Iwatsubo,T., Wavrant-Devrieze,F., Dartigues,J.F., Tzourio,C.,
            Buee,L., Pasquier,F., Berr,C., Mann,D., Lendon,C., Alperovitch,A.,
            Kamboh,M.I., Amouyel,P. and Lambert,J.C.
  TITLE     Transcriptomic and genetic studies identify IL-33 as a candidate
            gene for Alzheimer's disease
  JOURNAL   Mol Psychiatry 14 (11), 1004-1016 (2009)
   PUBMED   19204726
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Dailey,H.A. and Strittmatter,P.
  TITLE     Modification and identification of cytochrome b5 carboxyl groups
            involved in protein-protein interaction with cytochrome b5
            reductase
  JOURNAL   J Biol Chem 254 (12), 5388-5396 (1979)
   PUBMED   221468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL353579.17.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1286468.1,
                                           SRR14038196.1285373.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..202
                     /product="transmembrane protein 217 isoform 2"
                     /calculated_mol_wt=23605
     Region          11..171
                     /region_name="DUF4534"
                     /note="Protein of unknown function (DUF4534); pfam15049"
                     /db_xref="CDD:464470"
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            67..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     CDS             1..202
                     /gene="TMEM217"
                     /gene_synonym="C6orf128; dJ355M6.2"
                     /coded_by="NM_001395240.1:589..1197"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS93908.1"
                     /db_xref="GeneID:221468"
                     /db_xref="HGNC:HGNC:21238"
                     /db_xref="MIM:621459"
ORIGIN      
        1 mkqqqwcgmt akmgtvlsgv ftimavdmyl ifeqkhlgng scteitpkyr gasniinnfi
       61 icwsfkivlf lsfitilisc fllysvyaqi frglviyivw iffyetanvv iqiltnndfd
      121 ikevrimrwf glvsrtvmhc fwmffvinya hityknrsqg niisykrris taeilhsrnk
      181 rlsissgfsg shlesqyfer qr
//
LOCUS       NP_001382172             193 aa            linear   PRI 07-JAN-2026
DEFINITION  transmembrane protein 217 isoform 6 [Homo sapiens].
ACCESSION   NP_001382172
VERSION     NP_001382172.1
DBSOURCE    REFSEQ: accession NM_001395243.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Goes,F.S., Hamshere,M.L., Seifuddin,F., Pirooznia,M.,
            Belmonte-Mahon,P., Breuer,R., Schulze,T., Nothen,M., Cichon,S.,
            Rietschel,M., Holmans,P., Zandi,P.P., Craddock,N. and Potash,J.B.
  CONSRTM   Bipolar Genome Study (BiGS)
  TITLE     Genome-wide association of mood-incongruent psychotic bipolar
            disorder
  JOURNAL   Transl Psychiatry 2 (10), e180 (2012)
   PUBMED   23092984
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Chapuis,J., Hot,D., Hansmannel,F., Kerdraon,O., Ferreira,S.,
            Hubans,C., Maurage,C.A., Huot,L., Bensemain,F., Laumet,G.,
            Ayral,A.M., Fievet,N., Hauw,J.J., DeKosky,S.T., Lemoine,Y.,
            Iwatsubo,T., Wavrant-Devrieze,F., Dartigues,J.F., Tzourio,C.,
            Buee,L., Pasquier,F., Berr,C., Mann,D., Lendon,C., Alperovitch,A.,
            Kamboh,M.I., Amouyel,P. and Lambert,J.C.
  TITLE     Transcriptomic and genetic studies identify IL-33 as a candidate
            gene for Alzheimer's disease
  JOURNAL   Mol Psychiatry 14 (11), 1004-1016 (2009)
   PUBMED   19204726
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Dailey,H.A. and Strittmatter,P.
  TITLE     Modification and identification of cytochrome b5 carboxyl groups
            involved in protein-protein interaction with cytochrome b5
            reductase
  JOURNAL   J Biol Chem 254 (12), 5388-5396 (1979)
   PUBMED   221468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL353579.17.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.189770.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2161674 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..193
                     /product="transmembrane protein 217 isoform 6"
                     /calculated_mol_wt=22460
     Region          11..171
                     /region_name="DUF4534"
                     /note="Protein of unknown function (DUF4534); pfam15049"
                     /db_xref="CDD:464470"
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            67..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     CDS             1..193
                     /gene="TMEM217"
                     /gene_synonym="C6orf128; dJ355M6.2"
                     /coded_by="NM_001395243.1:589..1170"
                     /note="isoform 6 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS93910.1"
                     /db_xref="GeneID:221468"
                     /db_xref="HGNC:HGNC:21238"
                     /db_xref="MIM:621459"
ORIGIN      
        1 mkqqqwcgmt akmgtvlsgv ftimavdmyl ifeqkhlgng scteitpkyr gasniinnfi
       61 icwsfkivlf lsfitilisc fllysvyaqi frglviyivw iffyetanvv iqiltnndfd
      121 ikevrimrwf glvsrtvmhc fwmffvinya hityknrsqg niisykrris taeilhsrnk
      181 rlsisrgalv kqv
//
LOCUS       NP_001273330             211 aa            linear   PRI 07-JAN-2026
DEFINITION  transmembrane protein 217 isoform 3 [Homo sapiens].
ACCESSION   NP_001273330 XP_005248964
VERSION     NP_001273330.1
DBSOURCE    REFSEQ: accession NM_001286401.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Goes,F.S., Hamshere,M.L., Seifuddin,F., Pirooznia,M.,
            Belmonte-Mahon,P., Breuer,R., Schulze,T., Nothen,M., Cichon,S.,
            Rietschel,M., Holmans,P., Zandi,P.P., Craddock,N. and Potash,J.B.
  CONSRTM   Bipolar Genome Study (BiGS)
  TITLE     Genome-wide association of mood-incongruent psychotic bipolar
            disorder
  JOURNAL   Transl Psychiatry 2 (10), e180 (2012)
   PUBMED   23092984
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Chapuis,J., Hot,D., Hansmannel,F., Kerdraon,O., Ferreira,S.,
            Hubans,C., Maurage,C.A., Huot,L., Bensemain,F., Laumet,G.,
            Ayral,A.M., Fievet,N., Hauw,J.J., DeKosky,S.T., Lemoine,Y.,
            Iwatsubo,T., Wavrant-Devrieze,F., Dartigues,J.F., Tzourio,C.,
            Buee,L., Pasquier,F., Berr,C., Mann,D., Lendon,C., Alperovitch,A.,
            Kamboh,M.I., Amouyel,P. and Lambert,J.C.
  TITLE     Transcriptomic and genetic studies identify IL-33 as a candidate
            gene for Alzheimer's disease
  JOURNAL   Mol Psychiatry 14 (11), 1004-1016 (2009)
   PUBMED   19204726
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Dailey,H.A. and Strittmatter,P.
  TITLE     Modification and identification of cytochrome b5 carboxyl groups
            involved in protein-protein interaction with cytochrome b5
            reductase
  JOURNAL   J Biol Chem 254 (12), 5388-5396 (1979)
   PUBMED   221468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG285024.1, BC009625.1, BC026012.1, AL353579.17 and AW188099.1.
            
            On Nov 5, 2013 this sequence version replaced XP_005248964.1.
            
            Transcript Variant: This variant (3) lacks an alternate exon in the
            3' coding region, compared to variant 1. The encoded isoform (3)
            has a distinct C-terminus and is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4453968.1,
                                           SRR14038192.3396649.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000651039.2/ ENSP00000499204.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..211
                     /product="transmembrane protein 217 isoform 3"
                     /calculated_mol_wt=24566
     Region          11..171
                     /region_name="DUF4534"
                     /note="Protein of unknown function (DUF4534); pfam15049"
                     /db_xref="CDD:464470"
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            67..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     CDS             1..211
                     /gene="TMEM217"
                     /gene_synonym="C6orf128; dJ355M6.2"
                     /coded_by="NM_001286401.2:589..1224"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS69102.1"
                     /db_xref="GeneID:221468"
                     /db_xref="HGNC:HGNC:21238"
                     /db_xref="MIM:621459"
ORIGIN      
        1 mkqqqwcgmt akmgtvlsgv ftimavdmyl ifeqkhlgng scteitpkyr gasniinnfi
       61 icwsfkivlf lsfitilisc fllysvyaqi frglviyivw iffyetanvv iqiltnndfd
      121 ikevrimrwf glvsrtvmhc fwmffvinya hityknrsqg niisykrris taeilhsrnk
      181 rlsissgfsg shlesqyfer qrrcsgktsi k
//
LOCUS       NP_001382170             127 aa            linear   PRI 07-JAN-2026
DEFINITION  transmembrane protein 217 isoform 5 [Homo sapiens].
ACCESSION   NP_001382170
VERSION     NP_001382170.1
DBSOURCE    REFSEQ: accession NM_001395241.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Goes,F.S., Hamshere,M.L., Seifuddin,F., Pirooznia,M.,
            Belmonte-Mahon,P., Breuer,R., Schulze,T., Nothen,M., Cichon,S.,
            Rietschel,M., Holmans,P., Zandi,P.P., Craddock,N. and Potash,J.B.
  CONSRTM   Bipolar Genome Study (BiGS)
  TITLE     Genome-wide association of mood-incongruent psychotic bipolar
            disorder
  JOURNAL   Transl Psychiatry 2 (10), e180 (2012)
   PUBMED   23092984
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Chapuis,J., Hot,D., Hansmannel,F., Kerdraon,O., Ferreira,S.,
            Hubans,C., Maurage,C.A., Huot,L., Bensemain,F., Laumet,G.,
            Ayral,A.M., Fievet,N., Hauw,J.J., DeKosky,S.T., Lemoine,Y.,
            Iwatsubo,T., Wavrant-Devrieze,F., Dartigues,J.F., Tzourio,C.,
            Buee,L., Pasquier,F., Berr,C., Mann,D., Lendon,C., Alperovitch,A.,
            Kamboh,M.I., Amouyel,P. and Lambert,J.C.
  TITLE     Transcriptomic and genetic studies identify IL-33 as a candidate
            gene for Alzheimer's disease
  JOURNAL   Mol Psychiatry 14 (11), 1004-1016 (2009)
   PUBMED   19204726
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Dailey,H.A. and Strittmatter,P.
  TITLE     Modification and identification of cytochrome b5 carboxyl groups
            involved in protein-protein interaction with cytochrome b5
            reductase
  JOURNAL   J Biol Chem 254 (12), 5388-5396 (1979)
   PUBMED   221468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL353579.17.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..127
                     /product="transmembrane protein 217 isoform 5"
                     /calculated_mol_wt=14618
     Region          11..>123
                     /region_name="DUF4534"
                     /note="Protein of unknown function (DUF4534); pfam15049"
                     /db_xref="CDD:464470"
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            67..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     CDS             1..127
                     /gene="TMEM217"
                     /gene_synonym="C6orf128; dJ355M6.2"
                     /coded_by="NM_001395241.1:594..977"
                     /note="isoform 5 is encoded by transcript variant 9"
                     /db_xref="GeneID:221468"
                     /db_xref="HGNC:HGNC:21238"
                     /db_xref="MIM:621459"
ORIGIN      
        1 mkqqqwcgmt akmgtvlsgv ftimavdmyl ifeqkhlgng scteitpkyr gasniinnfi
       61 icwsfkivlf lsfitilisc fllysvyaqi frglviyivw iffyetanvv iqiltnndfd
      121 ikeevlw
//
LOCUS       NP_001382173             207 aa            linear   PRI 07-JAN-2026
DEFINITION  transmembrane protein 217 isoform 8 [Homo sapiens].
ACCESSION   NP_001382173
VERSION     NP_001382173.1
DBSOURCE    REFSEQ: accession NM_001395244.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Goes,F.S., Hamshere,M.L., Seifuddin,F., Pirooznia,M.,
            Belmonte-Mahon,P., Breuer,R., Schulze,T., Nothen,M., Cichon,S.,
            Rietschel,M., Holmans,P., Zandi,P.P., Craddock,N. and Potash,J.B.
  CONSRTM   Bipolar Genome Study (BiGS)
  TITLE     Genome-wide association of mood-incongruent psychotic bipolar
            disorder
  JOURNAL   Transl Psychiatry 2 (10), e180 (2012)
   PUBMED   23092984
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Chapuis,J., Hot,D., Hansmannel,F., Kerdraon,O., Ferreira,S.,
            Hubans,C., Maurage,C.A., Huot,L., Bensemain,F., Laumet,G.,
            Ayral,A.M., Fievet,N., Hauw,J.J., DeKosky,S.T., Lemoine,Y.,
            Iwatsubo,T., Wavrant-Devrieze,F., Dartigues,J.F., Tzourio,C.,
            Buee,L., Pasquier,F., Berr,C., Mann,D., Lendon,C., Alperovitch,A.,
            Kamboh,M.I., Amouyel,P. and Lambert,J.C.
  TITLE     Transcriptomic and genetic studies identify IL-33 as a candidate
            gene for Alzheimer's disease
  JOURNAL   Mol Psychiatry 14 (11), 1004-1016 (2009)
   PUBMED   19204726
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Dailey,H.A. and Strittmatter,P.
  TITLE     Modification and identification of cytochrome b5 carboxyl groups
            involved in protein-protein interaction with cytochrome b5
            reductase
  JOURNAL   J Biol Chem 254 (12), 5388-5396 (1979)
   PUBMED   221468
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL353579.17.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.376311.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..207
                     /product="transmembrane protein 217 isoform 8"
                     /calculated_mol_wt=24011
     Region          11..171
                     /region_name="DUF4534"
                     /note="Protein of unknown function (DUF4534); pfam15049"
                     /db_xref="CDD:464470"
     Site            13..33
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            67..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N7C4.1)"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N7C4.1)"
     CDS             1..207
                     /gene="TMEM217"
                     /gene_synonym="C6orf128; dJ355M6.2"
                     /coded_by="NM_001395244.1:589..1212"
                     /note="isoform 8 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS93909.1"
                     /db_xref="GeneID:221468"
                     /db_xref="HGNC:HGNC:21238"
                     /db_xref="MIM:621459"
ORIGIN      
        1 mkqqqwcgmt akmgtvlsgv ftimavdmyl ifeqkhlgng scteitpkyr gasniinnfi
       61 icwsfkivlf lsfitilisc fllysvyaqi frglviyivw iffyetanvv iqiltnndfd
      121 ikevrimrwf glvsrtvmhc fwmffvinya hityknrsqg niisykrris taeilhsrnk
      181 rlsissgfsg shlesqyfer qsssslt
//
LOCUS       NP_996850                 76 aa            linear   PRI 07-JAN-2026
DEFINITION  uncharacterized protein C16orf74 [Homo sapiens].
ACCESSION   NP_996850
VERSION     NP_996850.1
DBSOURCE    REFSEQ: accession NM_206967.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Bradburn,D.A., Reis,J.C., Moreno,R.Y., Qayyum,S., Viennet,T.,
            Arthanari,H. and Cyert,M.S.
  TITLE     A composite motif in calcimembrin/C16orf74 dictates multimeric
            dephosphorylation by calcineurin
  JOURNAL   Nat Commun 16 (1), 9941 (2025)
   PUBMED   41224739
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Dinh,J., Yi,D., Lin,F., Xue,P., Holloway,N.D., Xie,Y., Ibe,N.U.,
            Nguyen,H.P., Viscarra,J.A., Wang,Y. and Sul,H.S.
  TITLE     The microprotein C16orf74/MICT1 promotes thermogenesis in brown
            adipose tissue
  JOURNAL   EMBO J 44 (12), 3381-3412 (2025)
   PUBMED   40355556
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Huang,L., Liu,P., Du,Y., Bazan,J.F., Pan,D., Chen,Q., Lee,A.,
            Kola,V.S.R., Wolfe,S.A. and Wang,Y.X.
  TITLE     A brown fat-enriched adipokine, ASRA, is a leptin receptor
            antagonist that stimulates appetite
  JOURNAL   bioRxiv (2024)
   PUBMED   37745491
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 76)
  AUTHORS   Gong,J., Fan,H., Deng,J. and Zhang,Q.
  TITLE     LncRNA HAND2-AS1 represses cervical cancer progression by
            interaction with transcription factor E2F4 at the promoter of
            C16orf74
  JOURNAL   J Cell Mol Med 24 (11), 6015-6027 (2020)
   PUBMED   32314545
  REMARK    GeneRIF: LncRNA HAND2-AS1 represses cervical cancer progression by
            interaction with transcription factor E2F4 at the promoter of
            C16orf74.
REFERENCE   5  (residues 1 to 76)
  AUTHORS   Kushibiki,T., Nakamura,T., Tsuda,M., Tsuchikawa,T., Hontani,K.,
            Inoko,K., Takahashi,M., Asano,T., Okamura,K., Murakami,S.,
            Kurashima,Y., Ebihara,Y., Noji,T., Nakanishi,Y., Tanaka,K.,
            Maishi,N., Sasaki,K., Park,W.R., Shichinohe,T., Hida,K., Tanaka,S.
            and Hirano,S.
  TITLE     Role of Dimerized C16orf74 in Aggressive Pancreatic Cancer: A Novel
            Therapeutic Target
  JOURNAL   Mol Cancer Ther 19 (1), 187-198 (2020)
   PUBMED   31597713
  REMARK    GeneRIF: Role of Dimerized C16orf74 in Aggressive Pancreatic
            Cancer: A Novel Therapeutic Target.
REFERENCE   6  (residues 1 to 76)
  AUTHORS   Sato,S., Nakamura,T., Katagiri,T., Tsuchikawa,T., Kushibiki,T.,
            Hontani,K., Takahashi,M., Inoko,K., Takano,H., Abe,H., Takeuchi,S.,
            Ono,M., Kuwabara,S., Umemoto,K., Suzuki,T., Sato,O., Nakamura,Y.
            and Hirano,S.
  TITLE     Molecular targeting of cell-permeable peptide inhibits pancreatic
            ductal adenocarcinoma cell proliferation
  JOURNAL   Oncotarget 8 (69), 113662-113672 (2017)
   PUBMED   29371937
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 76)
  AUTHORS   Nakamura,T., Katagiri,T., Sato,S., Kushibiki,T., Hontani,K.,
            Tsuchikawa,T., Hirano,S. and Nakamura,Y.
  TITLE     Overexpression of C16orf74 is involved in aggressive pancreatic
            cancers
  JOURNAL   Oncotarget 8 (31), 50460-50475 (2016)
   PUBMED   28881575
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 76)
  AUTHORS   Quemener-Redon,S., Benech,C., Audebert-Bellanger,S., Friocourt,G.,
            Planes,M., Parent,P. and Ferec,C.
  TITLE     A small de novo 16q24.1 duplication in a woman with severe clinical
            features
  JOURNAL   Eur J Med Genet 56 (4), 211-215 (2013)
   PUBMED   23333879
REFERENCE   9  (residues 1 to 76)
  AUTHORS   Kim,W.T., Yun,S.J., Park,C., Kim,I.Y., Moon,S.K., Kwon,T.G.,
            Choi,Y.H. and Kim,W.J.
  TITLE     Identification of C16orf74 as a marker of progression in primary
            non-muscle invasive bladder cancer
  JOURNAL   PLoS One 5 (12), e15260 (2010)
   PUBMED   21203532
  REMARK    GeneRIF: C16orf74 expression level represents a potentially useful
            marker for predicting progression in primary non-muscle invasive
            bladder cancer patients
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 76)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC018695.6, CD674248.1 and AW072412.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB115764.1, SRR1163655.251942.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000284245.9/ ENSP00000284245.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.1"
     Protein         1..76
                     /product="uncharacterized protein C16orf74"
                     /note="hypothetical protein 1; hypothetical protein 2;
                     hypothetical protein 3; adipose-secreted regulator of
                     appetite; microprotein for thermogenesis 1"
                     /calculated_mol_wt=7987
     Region          13..75
                     /region_name="DUF4597"
                     /note="Domain of unknown function (DUF4597); pfam15366"
                     /db_xref="CDD:464676"
     Region          36..41
                     /region_name="Required for interaction with PPP3CA.
                     /evidence=ECO:0000269|PubMed:28881575"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96GX8.2)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:28881575,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96GX8.2)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96GX8.2)"
     CDS             1..76
                     /gene="CLMB"
                     /gene_synonym="ASRA; C16orf74; MICT1"
                     /coded_by="NM_206967.3:190..420"
                     /db_xref="CCDS:CCDS45540.1"
                     /db_xref="GeneID:404550"
                     /db_xref="HGNC:HGNC:23362"
ORIGIN      
        1 mglkmsclkg fqmcvsssss shdeapvlnd khldvpdiii tpptptgmml prdlgstvwl
       61 detgscpddg eidpea
//
LOCUS       NP_003135                286 aa            linear   PRI 07-JAN-2026
DEFINITION  translocon-associated protein subunit alpha isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_003135
VERSION     NP_003135.2
DBSOURCE    REFSEQ: accession NM_003144.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Gemmer,M., Chaillet,M.L., van Loenhout,J., Cuevas Arenas,R.,
            Vismpas,D., Grollers-Mulderij,M., Koh,F.A., Albanese,P.,
            Scheltema,R.A., Howes,S.C., Kotecha,A., Fedry,J. and Forster,F.
  TITLE     Visualization of translation and protein biogenesis at the ER
            membrane
  JOURNAL   Nature 614 (7946), 160-167 (2023)
   PUBMED   36697828
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Yan,J., Wang,Z.H., Yan,Y., Luo,H.N., Ren,X.Y., Li,N., Zheng,G.X.
            and Hou,J.
  TITLE     RP11-156L14.1 regulates SSR1 expression by competitively binding to
            miR-548ao-3p in hypopharyngeal squamous cell carcinoma
  JOURNAL   Oncol Rep 44 (5), 2080-2092 (2020)
   PUBMED   33000261
  REMARK    GeneRIF: RP11156L14.1 regulates SSR1 expression by competitively
            binding to miR548ao3p in hypopharyngeal squamous cell carcinoma.
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Liu,X., Salokas,K., Tamene,F., Jiu,Y., Weldatsadik,R.G., Ohman,T.
            and Varjosalo,M.
  TITLE     An AP-MS- and BioID-compatible MAC-tag enables comprehensive
            mapping of protein interactions and subcellular localizations
  JOURNAL   Nat Commun 9 (1), 1188 (2018)
   PUBMED   29568061
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Mahajan,A., Go,M.J., Zhang,W., Below,J.E., Gaulton,K.J.,
            Ferreira,T., Horikoshi,M., Johnson,A.D., Ng,M.C., Prokopenko,I.,
            Saleheen,D., Wang,X., Zeggini,E., Abecasis,G.R., Adair,L.S.,
            Almgren,P., Atalay,M., Aung,T., Baldassarre,D., Balkau,B., Bao,Y.,
            Barnett,A.H., Barroso,I., Basit,A., Been,L.F., Beilby,J.,
            Bell,G.I., Benediktsson,R., Bergman,R.N., Boehm,B.O.,
            Boerwinkle,E., Bonnycastle,L.L., Burtt,N., Cai,Q., Campbell,H.,
            Carey,J., Cauchi,S., Caulfield,M., Chan,J.C., Chang,L.C.,
            Chang,T.J., Chang,Y.C., Charpentier,G., Chen,C.H., Chen,H.,
            Chen,Y.T., Chia,K.S., Chidambaram,M., Chines,P.S., Cho,N.H.,
            Cho,Y.M., Chuang,L.M., Collins,F.S., Cornelis,M.C., Couper,D.J.,
            Crenshaw,A.T., van Dam,R.M., Danesh,J., Das,D., de Faire,U.,
            Dedoussis,G., Deloukas,P., Dimas,A.S., Dina,C., Doney,A.S.,
            Donnelly,P.J., Dorkhan,M., van Duijn,C., Dupuis,J., Edkins,S.,
            Elliott,P., Emilsson,V., Erbel,R., Eriksson,J.G., Escobedo,J.,
            Esko,T., Eury,E., Florez,J.C., Fontanillas,P., Forouhi,N.G.,
            Forsen,T., Fox,C., Fraser,R.M., Frayling,T.M., Froguel,P.,
            Frossard,P., Gao,Y., Gertow,K., Gieger,C., Gigante,B., Grallert,H.,
            Grant,G.B., Grrop,L.C., Groves,C.J., Grundberg,E., Guiducci,C.,
            Hamsten,A., Han,B.G., Hara,K., Hassanali,N., Hattersley,A.T.,
            Hayward,C., Hedman,A.K., Herder,C., Hofman,A., Holmen,O.L.,
            Hovingh,K., Hreidarsson,A.B., Hu,C., Hu,F.B., Hui,J.,
            Humphries,S.E., Hunt,S.E., Hunter,D.J., Hveem,K., Hydrie,Z.I.,
            Ikegami,H., Illig,T., Ingelsson,E., Islam,M., Isomaa,B.,
            Jackson,A.U., Jafar,T., James,A., Jia,W., Jockel,K.H., Jonsson,A.,
            Jowett,J.B., Kadowaki,T., Kang,H.M., Kanoni,S., Kao,W.H.,
            Kathiresan,S., Kato,N., Katulanda,P., Keinanen-Kiukaanniemi,K.M.,
            Kelly,A.M., Khan,H., Khaw,K.T., Khor,C.C., Kim,H.L., Kim,S.,
            Kim,Y.J., Kinnunen,L., Klopp,N., Kong,A., Korpi-Hyovalti,E.,
            Kowlessur,S., Kraft,P., Kravic,J., Kristensen,M.M., Krithika,S.,
            Kumar,A., Kumate,J., Kuusisto,J., Kwak,S.H., Laakso,M., Lagou,V.,
            Lakka,T.A., Langenberg,C., Langford,C., Lawrence,R., Leander,K.,
            Lee,J.M., Lee,N.R., Li,M., Li,X., Li,Y., Liang,J., Liju,S.,
            Lim,W.Y., Lind,L., Lindgren,C.M., Lindholm,E., Liu,C.T., Liu,J.J.,
            Lobbens,S., Long,J., Loos,R.J., Lu,W., Luan,J., Lyssenko,V.,
            Ma,R.C., Maeda,S., Magi,R., Mannisto,S., Matthews,D.R., Meigs,J.B.,
            Melander,O., Metspalu,A., Meyer,J., Mirza,G., Mihailov,E.,
            Moebus,S., Mohan,V., Mohlke,K.L., Morris,A.D., Muhleisen,T.W.,
            Muller-Nurasyid,M., Musk,B., Nakamura,J., Nakashima,E., Navarro,P.,
            Ng,P.K., Nica,A.C., Nilsson,P.M., Njolstad,I., Nothen,M.M.,
            Ohnaka,K., Ong,T.H., Owen,K.R., Palmer,C.N., Pankow,J.S.,
            Park,K.S., Parkin,M., Pechlivanis,S., Pedersen,N.L., Peltonen,L.,
            Perry,J.R., Peters,A., Pinidiyapathirage,J.M., Platou,C.G.,
            Potter,S., Price,J.F., Qi,L., Radha,V., Rallidis,L., Rasheed,A.,
            Rathman,W., Rauramaa,R., Raychaudhuri,S., Rayner,N.W., Rees,S.D.,
            Rehnberg,E., Ripatti,S., Robertson,N., Roden,M., Rossin,E.J.,
            Rudan,I., Rybin,D., Saaristo,T.E., Salomaa,V., Saltevo,J.,
            Samuel,M., Sanghera,D.K., Saramies,J., Scott,J., Scott,L.J.,
            Scott,R.A., Segre,A.V., Sehmi,J., Sennblad,B., Shah,N., Shah,S.,
            Shera,A.S., Shu,X.O., Shuldiner,A.R., Sigurdsson,G., Sijbrands,E.,
            Silveira,A., Sim,X., Sivapalaratnam,S., Small,K.S., So,W.Y.,
            Stancakova,A., Stefansson,K., Steinbach,G., Steinthorsdottir,V.,
            Stirrups,K., Strawbridge,R.J., Stringham,H.M., Sun,Q., Suo,C.,
            Syvanen,A.C., Takayanagi,R., Takeuchi,F., Tay,W.T., Teslovich,T.M.,
            Thorand,B., Thorleifsson,G., Thorsteinsdottir,U., Tikkanen,E.,
            Trakalo,J., Tremoli,E., Trip,M.D., Tsai,F.J., Tuomi,T.,
            Tuomilehto,J., Uitterlinden,A.G., Valladares-Salgado,A.,
            Vedantam,S., Veglia,F., Voight,B.F., Wang,C., Wareham,N.J.,
            Wennauer,R., Wickremasinghe,A.R., Wilsgaard,T., Wilson,J.F.,
            Wiltshire,S., Winckler,W., Wong,T.Y., Wood,A.R., Wu,J.Y., Wu,Y.,
            Yamamoto,K., Yamauchi,T., Yang,M., Yengo,L., Yokota,M., Young,R.,
            Zabaneh,D., Zhang,F., Zhang,R., Zheng,W., Zimmet,P.Z.,
            Altshuler,D., Bowden,D.W., Cho,Y.S., Cox,N.J., Cruz,M., Hanis,C.L.,
            Kooner,J., Lee,J.Y., Seielstad,M., Teo,Y.Y., Boehnke,M.,
            Parra,E.J., Chambers,J.C., Tai,E.S., McCarthy,M.I. and Morris,A.P.
  CONSRTM   DIAbetes Genetics Replication And Meta-analysis (DIAGRAM)
            Consortium; Asian Genetic Epidemiology Network Type 2 Diabetes
            (AGEN-T2D) Consortium; South Asian Type 2 Diabetes (SAT2D)
            Consortium; Mexican American Type 2 Diabetes (MAT2D) Consortium;
            Type 2 Diabetes Genetic Exploration by Nex-generation sequencing in
            muylti-Ethnic Samples (T2D-GENES) Consortium
  TITLE     Genome-wide trans-ancestry meta-analysis provides insight into the
            genetic architecture of type 2 diabetes susceptibility
  JOURNAL   Nat Genet 46 (3), 234-244 (2014)
   PUBMED   24509480
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Hu,T., Guan,T. and Gerace,L.
  TITLE     Molecular and functional characterization of the p62 complex, an
            assembly of nuclear pore complex glycoproteins
  JOURNAL   J Cell Biol 134 (3), 589-601 (1996)
   PUBMED   8707840
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Hartmann,E. and Prehn,S.
  TITLE     The N-terminal region of the alpha-subunit of the TRAP complex has
            a conserved cluster of negative charges
  JOURNAL   FEBS Lett 349 (3), 324-326 (1994)
   PUBMED   8050590
REFERENCE   8  (residues 1 to 286)
  AUTHORS   Hartmann,E., Gorlich,D., Kostka,S., Otto,A., Kraft,R., Knespel,S.,
            Burger,E., Rapoport,T.A. and Prehn,S.
  TITLE     A tetrameric complex of membrane proteins in the endoplasmic
            reticulum
  JOURNAL   Eur J Biochem 214 (2), 375-381 (1993)
   PUBMED   7916687
REFERENCE   9  (residues 1 to 286)
  AUTHORS   Wei,M.L. and Cresswell,P.
  TITLE     HLA-A2 molecules in an antigen-processing mutant cell contain
            signal sequence-derived peptides
  JOURNAL   Nature 356 (6368), 443-446 (1992)
   PUBMED   1557127
REFERENCE   10 (residues 1 to 286)
  AUTHORS   Vogel,F., Hartmann,E., Gorlich,D. and Rapoport,T.A.
  TITLE     Segregation of the signal sequence receptor protein in the rough
            endoplasmic reticulum membrane
  JOURNAL   Eur J Cell Biol 53 (2), 197-202 (1990)
   PUBMED   1964414
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC007710.2, AL139095.15 and
            BM685131.1.
            
            On Mar 5, 2008 this sequence version replaced NP_003135.1.
            
            Summary: The signal sequence receptor (SSR) is a glycosylated
            endoplasmic reticulum (ER) membrane receptor associated with
            protein translocation across the ER membrane. The SSR consists of 2
            subunits, a 34-kD glycoprotein encoded by this gene and a 22-kD
            glycoprotein. This gene generates several mRNA species as a result
            of complex alternative polyadenylation. This gene is unusual in
            that it utilizes arrays of polyA signal sequences that are mostly
            non-canonical. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, May
            2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.54577.1,
                                           SRR1660803.67255.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000244763.9/ ENSP00000244763.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.3"
     Protein         1..286
                     /product="translocon-associated protein subunit alpha
                     isoform 1 precursor"
                     /note="TRAP alpha; translocon-associated protein subunit
                     alpha; translocon-associated protein alpha subunit; SSR
                     alpha subunit; SSR-alpha; signal sequence receptor subunit
                     alpha; signal sequence receptor, alpha"
                     /calculated_mol_wt=30161
     sig_peptide     1..18
                     /note="/evidence=ECO:0000269|PubMed:1557127; propagated
                     from UniProtKB/Swiss-Prot (P43307.3)"
                     /calculated_mol_wt=2093
     Region          14..285
                     /region_name="TRAP_alpha"
                     /note="Translocon-associated protein (TRAP), alpha
                     subunit; pfam03896"
                     /db_xref="CDD:461085"
     mat_peptide     19..286
                     /product="Translocon-associated protein subunit alpha.
                     /id=PRO_0000033281"
                     /note="propagated from UniProtKB/Swiss-Prot (P43307.3)"
                     /calculated_mol_wt=30161
     Region          39..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43307.3)"
     Site            136
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P43307.3)"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P43307.3)"
     Site            208..228
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43307.3)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P43307.3)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P43307.3)"
     Region          261..286
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43307.3)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P43307.3)"
     CDS             1..286
                     /gene="SSR1"
                     /gene_synonym="TRAPA"
                     /coded_by="NM_003144.5:80..940"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4499.1"
                     /db_xref="GeneID:6745"
                     /db_xref="HGNC:HGNC:11323"
                     /db_xref="MIM:600868"
ORIGIN      
        1 mrllprllll lllvfpatvl frggprglla vaqdltedee tvedsiiede ddeaeveede
       61 ptdlvedkee edvsgepeas psadttilfv kgedfpanni vkflvgftnk gtedfivesl
      121 dasfrypqdy qfyiqnftal plntvvppqr qatfeysfip aepmggrpfg lvinlnykdl
      181 ngnvfqdavf nqtvtviere dgldgetifm ymflaglgll vivglhqlle srkrkrpiqk
      241 vemgtssqnd vdmswipqet lnqinkaspr rlprkraqkr svgsde
//
LOCUS       NP_001316687             107 aa            linear   PRI 07-JAN-2026
DEFINITION  protein FAM136A isoform 4 [Homo sapiens].
ACCESSION   NP_001316687 XP_005264677
VERSION     NP_001316687.1
DBSOURCE    REFSEQ: accession NM_001329758.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Otsuka,Y. and Yano,M.
  TITLE     FAM136A depletion induces mitochondrial stress and reduces
            mitochondrial membrane potential and ATP production
  JOURNAL   FEBS Open Bio 15 (5), 738-753 (2025)
   PUBMED   39821719
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 107)
  AUTHORS   Zhao,L., Ge,C., Zhang,Z., Hu,H., Zhang,Y., Zhao,W., Li,R., Zeng,B.,
            Song,X. and Li,G.
  TITLE     FAM136A immunoreactivity is associated with nodal involvement and
            survival in lung adenocarcinoma in a Chinese case series
  JOURNAL   Bioengineered 11 (1), 261-271 (2020)
   PUBMED   32098576
  REMARK    GeneRIF: FAM136A immunoreactivity is associated with nodal
            involvement and survival in lung adenocarcinoma in a Chinese case
            series.
REFERENCE   6  (residues 1 to 107)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 107)
  AUTHORS   Frejo,L., Giegling,I., Teggi,R., Lopez-Escamez,J.A. and Rujescu,D.
  TITLE     Genetics of vestibular disorders: pathophysiological insights
  JOURNAL   J Neurol 263 Suppl 1, S45-S53 (2016)
   PUBMED   27083884
  REMARK    GeneRIF: This study showed that FAM136A genes have been identified
            in familial Meniere's disease.
            Review article
REFERENCE   8  (residues 1 to 107)
  AUTHORS   Requena,T., Cabrera,S., Martin-Sierra,C., Price,S.D., Lysakowski,A.
            and Lopez-Escamez,J.A.
  TITLE     Identification of two novel mutations in FAM136A and DTNA genes in
            autosomal-dominant familial Meniere's disease
  JOURNAL   Hum Mol Genet 24 (4), 1119-1126 (2015)
   PUBMED   25305078
  REMARK    GeneRIF: our findings suggest that novel mutations in FAM136A and
            DTNA genes are probably causal variants in FMD.
REFERENCE   9  (residues 1 to 107)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP334741.1, CB108776.1,
            AK225151.1 and BC026293.1.
            
            On Jul 28, 2016 this sequence version replaced XP_005264677.1.
            
            Summary: This gene encodes a mitochondrially localized protein that
            is highly conserved across species. The gene is expressed in a
            variety of tissues including human lymphoblast cells and rat
            neurosensorial epithelium of the cristaampullaris. A mutation in
            this gene has been associated with familial Meniere's disease, a
            chronic disorder of the inner ear. Several pseudogenes of this gene
            are found on other chromosomes. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Aug 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.241387.1,
                                           SRR3476690.39252.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 25305078; reported by
                                                  MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..107
                     /product="protein FAM136A isoform 4"
                     /note="protein FAM136A; family with sequence similarity
                     136 member A"
                     /calculated_mol_wt=11883
     Region          <1..96
                     /region_name="DUF842"
                     /note="Eukaryotic protein of unknown function (DUF842);
                     pfam05811"
                     /db_xref="CDD:461747"
     CDS             1..107
                     /gene="TIMCC"
                     /gene_synonym="FAM136A"
                     /coded_by="NM_001329758.2:232..555"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:84908"
                     /db_xref="HGNC:HGNC:25911"
                     /db_xref="MIM:616275"
ORIGIN      
        1 mfrcsascce dsqasmkqvh qcierchvpl aqaqalvtse lekfqdrlar ctmhcndkak
       61 dsidagskel qvkqqldscv tkcvddhmhl iptmtkkmke allsigk
//
LOCUS       NP_001316681             245 aa            linear   PRI 07-JAN-2026
DEFINITION  protein FAM136A isoform 2 [Homo sapiens].
ACCESSION   NP_001316681
VERSION     NP_001316681.1
DBSOURCE    REFSEQ: accession NM_001329752.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Otsuka,Y. and Yano,M.
  TITLE     FAM136A depletion induces mitochondrial stress and reduces
            mitochondrial membrane potential and ATP production
  JOURNAL   FEBS Open Bio 15 (5), 738-753 (2025)
   PUBMED   39821719
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Zhao,L., Ge,C., Zhang,Z., Hu,H., Zhang,Y., Zhao,W., Li,R., Zeng,B.,
            Song,X. and Li,G.
  TITLE     FAM136A immunoreactivity is associated with nodal involvement and
            survival in lung adenocarcinoma in a Chinese case series
  JOURNAL   Bioengineered 11 (1), 261-271 (2020)
   PUBMED   32098576
  REMARK    GeneRIF: FAM136A immunoreactivity is associated with nodal
            involvement and survival in lung adenocarcinoma in a Chinese case
            series.
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Frejo,L., Giegling,I., Teggi,R., Lopez-Escamez,J.A. and Rujescu,D.
  TITLE     Genetics of vestibular disorders: pathophysiological insights
  JOURNAL   J Neurol 263 Suppl 1, S45-S53 (2016)
   PUBMED   27083884
  REMARK    GeneRIF: This study showed that FAM136A genes have been identified
            in familial Meniere's disease.
            Review article
REFERENCE   8  (residues 1 to 245)
  AUTHORS   Requena,T., Cabrera,S., Martin-Sierra,C., Price,S.D., Lysakowski,A.
            and Lopez-Escamez,J.A.
  TITLE     Identification of two novel mutations in FAM136A and DTNA genes in
            autosomal-dominant familial Meniere's disease
  JOURNAL   Hum Mol Genet 24 (4), 1119-1126 (2015)
   PUBMED   25305078
  REMARK    GeneRIF: our findings suggest that novel mutations in FAM136A and
            DTNA genes are probably causal variants in FMD.
REFERENCE   9  (residues 1 to 245)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022201.4, BU186527.1,
            CB108776.1, AK225151.1 and BC026293.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a mitochondrially localized protein that
            is highly conserved across species. The gene is expressed in a
            variety of tissues including human lymphoblast cells and rat
            neurosensorial epithelium of the cristaampullaris. A mutation in
            this gene has been associated with familial Meniere's disease, a
            chronic disorder of the inner ear. Several pseudogenes of this gene
            are found on other chromosomes. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Aug 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU186527.1, SRR9304717.382096.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 25305078; reported by
                                                  MitoCarta
            MANE Ensembl match                 :: ENST00000430566.6/
                                                  ENSP00000397269.1
            RefSeq Select criteria             :: based on conservation,
                                                  longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..245
                     /product="protein FAM136A isoform 2"
                     /note="protein FAM136A; family with sequence similarity
                     136 member A"
                     /calculated_mol_wt=26645
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q96C01.1)"
     Region          132..234
                     /region_name="DUF842"
                     /note="Eukaryotic protein of unknown function (DUF842);
                     pfam05811"
                     /db_xref="CDD:461747"
     CDS             1..245
                     /gene="TIMCC"
                     /gene_synonym="FAM136A"
                     /coded_by="NM_001329752.2:57..794"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS86849.1"
                     /db_xref="GeneID:84908"
                     /db_xref="HGNC:HGNC:25911"
                     /db_xref="MIM:616275"
ORIGIN      
        1 maelqqlrvq eavesmvksl erenirkmqv aglgpnqdpl lsgwvpgpsl shhatpctaa
       61 aspqtgcgrp wgrrgglgqd fgsfggsdei rvplpcarlf sapsspgqer prrqvgspww
      121 qalapppspl trplpqglmf rcsascceds qasmkqvhqc ierchvplaq aqalvtsele
      181 kfqdrlarct mhcndkakds idagskelqv kqqldscvtk cvddhmhlip tmtkkmkeal
      241 lsigk
//
LOCUS       NP_001316686             107 aa            linear   PRI 07-JAN-2026
DEFINITION  protein FAM136A isoform 4 [Homo sapiens].
ACCESSION   NP_001316686
VERSION     NP_001316686.1
DBSOURCE    REFSEQ: accession NM_001329757.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Otsuka,Y. and Yano,M.
  TITLE     FAM136A depletion induces mitochondrial stress and reduces
            mitochondrial membrane potential and ATP production
  JOURNAL   FEBS Open Bio 15 (5), 738-753 (2025)
   PUBMED   39821719
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 107)
  AUTHORS   Zhao,L., Ge,C., Zhang,Z., Hu,H., Zhang,Y., Zhao,W., Li,R., Zeng,B.,
            Song,X. and Li,G.
  TITLE     FAM136A immunoreactivity is associated with nodal involvement and
            survival in lung adenocarcinoma in a Chinese case series
  JOURNAL   Bioengineered 11 (1), 261-271 (2020)
   PUBMED   32098576
  REMARK    GeneRIF: FAM136A immunoreactivity is associated with nodal
            involvement and survival in lung adenocarcinoma in a Chinese case
            series.
REFERENCE   6  (residues 1 to 107)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 107)
  AUTHORS   Frejo,L., Giegling,I., Teggi,R., Lopez-Escamez,J.A. and Rujescu,D.
  TITLE     Genetics of vestibular disorders: pathophysiological insights
  JOURNAL   J Neurol 263 Suppl 1, S45-S53 (2016)
   PUBMED   27083884
  REMARK    GeneRIF: This study showed that FAM136A genes have been identified
            in familial Meniere's disease.
            Review article
REFERENCE   8  (residues 1 to 107)
  AUTHORS   Requena,T., Cabrera,S., Martin-Sierra,C., Price,S.D., Lysakowski,A.
            and Lopez-Escamez,J.A.
  TITLE     Identification of two novel mutations in FAM136A and DTNA genes in
            autosomal-dominant familial Meniere's disease
  JOURNAL   Hum Mol Genet 24 (4), 1119-1126 (2015)
   PUBMED   25305078
  REMARK    GeneRIF: our findings suggest that novel mutations in FAM136A and
            DTNA genes are probably causal variants in FMD.
REFERENCE   9  (residues 1 to 107)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP334741.1, AK315877.1,
            BC026293.1 and AK225151.1.
            
            Summary: This gene encodes a mitochondrially localized protein that
            is highly conserved across species. The gene is expressed in a
            variety of tissues including human lymphoblast cells and rat
            neurosensorial epithelium of the cristaampullaris. A mutation in
            this gene has been associated with familial Meniere's disease, a
            chronic disorder of the inner ear. Several pseudogenes of this gene
            are found on other chromosomes. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Aug 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.65846.1,
                                           SRR1803611.254905.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 25305078; reported by
                                                  MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..107
                     /product="protein FAM136A isoform 4"
                     /note="protein FAM136A; family with sequence similarity
                     136 member A"
                     /calculated_mol_wt=11883
     Region          <1..96
                     /region_name="DUF842"
                     /note="Eukaryotic protein of unknown function (DUF842);
                     pfam05811"
                     /db_xref="CDD:461747"
     CDS             1..107
                     /gene="TIMCC"
                     /gene_synonym="FAM136A"
                     /coded_by="NM_001329757.2:346..669"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:84908"
                     /db_xref="HGNC:HGNC:25911"
                     /db_xref="MIM:616275"
ORIGIN      
        1 mfrcsascce dsqasmkqvh qcierchvpl aqaqalvtse lekfqdrlar ctmhcndkak
       61 dsidagskel qvkqqldscv tkcvddhmhl iptmtkkmke allsigk
//
LOCUS       NP_003866                693 aa            linear   PRI 07-JAN-2026
DEFINITION  GMP synthase [glutamine-hydrolyzing] [Homo sapiens].
ACCESSION   NP_003866
VERSION     NP_003866.1
DBSOURCE    REFSEQ: accession NM_003875.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Wang,J., Luo,F.F., Huang,T.J., Mei,Y., Peng,L.X., Qian,C.N. and
            Huang,B.J.
  TITLE     The upregulated expression of RFC4 and GMPS mediated by DNA copy
            number alteration is associated with the early diagnosis and immune
            escape of ESCC based on a bioinformatic analysis
  JOURNAL   Aging (Albany NY) 13 (17), 21758-21777 (2021)
   PUBMED   34520390
  REMARK    GeneRIF: The upregulated expression of RFC4 and GMPS mediated by
            DNA copy number alteration is associated with the early diagnosis
            and immune escape of ESCC based on a bioinformatic analysis.
REFERENCE   2  (residues 1 to 693)
  AUTHORS   Wang,J., Wu,Y., Li,Y., Wang,Y., Shen,F., Zhou,J. and Chen,Y.
  TITLE     Guanosine monophosphate synthase upregulation mediates cervical
            cancer progression by inhibiting the apoptosis of cervical cancer
            cells via the Stat3/P53 pathway
  JOURNAL   Int J Oncol 58 (4) (2021)
   PUBMED   33649833
  REMARK    GeneRIF: Guanosine monophosphate synthase upregulation mediates
            cervical cancer progression by inhibiting the apoptosis of cervical
            cancer cells via the Stat3/P53 pathway.
REFERENCE   3  (residues 1 to 693)
  AUTHORS   Mechoud,M.A., Pujol-Carrion,N., Montella-Manuel,S. and de la
            Torre-Ruiz,M.A.
  TITLE     Interactions of GMP with Human Glrx3 and with Saccharomyces
            cerevisiae Grx3 and Grx4 Converge in the Regulation of the Gcn2
            Pathway
  JOURNAL   Appl Environ Microbiol 86 (14), e00221-20 (2020)
   PUBMED   32414791
  REMARK    GeneRIF: Interactions of GMP with Human Glrx3 and with
            Saccharomyces cerevisiae Grx3 and Grx4 Converge in the Regulation
            of the Gcn2 Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 693)
  AUTHORS   Roberts,R.L., Wallace,M.C., Seinen,M.L., van Bodegraven,A.A.,
            Krishnaprasad,K., Jones,G.T., van Rij,A.M., Baird,A.,
            Lawrance,I.C., Prosser,R., Bampton,P., Grafton,R., Simms,L.A.,
            Studd,C., Bell,S.J., Kennedy,M.A., Halliwell,J., Gearry,R.B.,
            Radford-Smith,G., Andrews,J.M., McHugh,P.C. and Barclay,M.L.
  TITLE     Nonsynonymous Polymorphism in Guanine Monophosphate Synthetase Is a
            Risk Factor for Unfavorable Thiopurine Metabolite Ratios in
            Patients With Inflammatory Bowel Disease
  JOURNAL   Inflamm Bowel Dis 24 (12), 2606-2612 (2018)
   PUBMED   29788244
  REMARK    GeneRIF: The GMPS SNP rs61750370 may be a reliable risk factor for
            extreme 6MMP preferential metabolism in patients with inflammatory
            bowel disease
REFERENCE   5  (residues 1 to 693)
  AUTHORS   Davidsson,J. and Johansson,B.
  TITLE     Methylation and expression analyses of Pallister-Killian syndrome
            reveal partial dosage compensation of tetrasomy 12p and
            hypomethylation of gene-poor regions on 12p
  JOURNAL   Epigenetics 11 (3), 194-204 (2016)
   PUBMED   26890086
  REMARK    GeneRIF: Three genes-ATP6V1G1 in 9q32, GMPS in 3q25.31, and TBX5 in
            12q24.21-exhibited concomitant hypermethylation and decreased
            expression. The i(12p)-positive cells displayed global
            hypomethylation of gene-poor regions on 12p, a footprint previously
            associated with constitutional and acquired gains of whole
            chromosomes as well as with X-chromosome inactivation in females
REFERENCE   6  (residues 1 to 693)
  AUTHORS   Nakamura,J., Straub,K., Wu,J. and Lou,L.
  TITLE     The glutamine hydrolysis function of human GMP synthetase.
            Identification of an essential active site cysteine
  JOURNAL   J Biol Chem 270 (40), 23450-23455 (1995)
   PUBMED   7559506
REFERENCE   7  (residues 1 to 693)
  AUTHORS   Nakamura,J. and Lou,L.
  TITLE     Biochemical characterization of human GMP synthetase
  JOURNAL   J Biol Chem 270 (13), 7347-7353 (1995)
   PUBMED   7706277
REFERENCE   8  (residues 1 to 693)
  AUTHORS   Harendza,S.G., Thaiss,F. and Stahl,R.A.
  TITLE     Enhanced in vitro growth of glomerular cells derived from rats with
            immune-mediated mesangial injury
  JOURNAL   Exp Nephrol 1 (1), 55-61 (1993)
   PUBMED   8081953
REFERENCE   9  (residues 1 to 693)
  AUTHORS   Zalkin,H. and Dixon,J.E.
  TITLE     De novo purine nucleotide biosynthesis
  JOURNAL   Prog Nucleic Acid Res Mol Biol 42, 259-287 (1992)
   PUBMED   1574589
  REMARK    Review article
REFERENCE   10 (residues 1 to 693)
  AUTHORS   Page,T., Bakay,B. and Nyhan,W.L.
  TITLE     Human GMP synthetase
  JOURNAL   Int J Biochem 16 (1), 117-120 (1984)
   PUBMED   6698284
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG721087.1, BC012178.1,
            CB159072.1 and AC067721.22.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: In the de novo synthesis of purine nucleotides, IMP is the
            branch point metabolite at which point the pathway diverges to the
            synthesis of either guanine or adenine nucleotides. In the guanine
            nucleotide pathway, there are 2 enzymes involved in converting IMP
            to GMP, namely IMP dehydrogenase (IMPD1), which catalyzes the
            oxidation of IMP to XMP, and GMP synthetase, which catalyzes the
            amination of XMP to GMP. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.185387.1,
                                           SRR1803614.158947.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000496455.7/ ENSP00000419851.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.31"
     Protein         1..693
                     /product="GMP synthase [glutamine-hydrolyzing]"
                     /EC_number="6.3.5.2"
                     /note="GMP synthase; guanosine 5'-monophosphate synthase;
                     GMP synthetase; glutamine amidotransferase; MLL/GMPS
                     fusion protein; guanine monophosphate synthetase;
                     testicular tissue protein Li 82; guanine monophosphate
                     synthase"
                     /calculated_mol_wt=76585
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P49915.1)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49915.1)"
     Site            9
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P49915.1)"
     Region          28..693
                     /region_name="guaA"
                     /note="GMP synthase; Reviewed; PRK00074"
                     /db_xref="CDD:234614"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P49915.1)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P49915.1)"
     CDS             1..693
                     /gene="GMPS"
                     /gene_synonym="GATD7"
                     /coded_by="NM_003875.3:222..2303"
                     /db_xref="CCDS:CCDS46941.1"
                     /db_xref="GeneID:8833"
                     /db_xref="HGNC:HGNC:4378"
                     /db_xref="MIM:600358"
ORIGIN      
        1 malcngdskl enaggdlkdg hhhyegavvi ldagaqygkv idrrvrelfv qseifpletp
       61 afaikeqgfr aiiisggpns vyaedapwfd paiftigkpv lgicygmqmm nkvfggtvhk
      121 ksvredgvfn isvdntcslf rglqkeevvl lthgdsvdkv adgfkvvars gnivagiane
      181 skklygaqfh pevgltengk vilknflydi agcsgtftvq nrelecirei kervgtskvl
      241 vllsggvdst vctallnral nqeqviavhi dngfmrkres qsveealkkl giqvkvinaa
      301 hsfyngtttl pisdedrtpr krisktlnmt tspeekrkii gdtfvkiane vigemnlkpe
      361 evflaqgtlr pdliesaslv asgkaelikt hhndtelirk lreegkviep lkdfhkdevr
      421 ilgrelglpe elvsrhpfpg pglairvica eepyickdfp etnnilkiva dfsasvkkph
      481 tllqrvkact teedqeklmq itslhslnaf llpiktvgvq gdcrsysyvc gisskdepdw
      541 esliflarli prmchnvnrv vyifgppvke pptdvtptfl ttgvlstlrq adfeahnilr
      601 esgyagkisq mpviltplhf drdplqkqps cqrsvvirtf itsdfmtgip atpgneipve
      661 vvlkmvteik kipgisrimy dltskppgtt ewe
//
LOCUS       NP_001316682             223 aa            linear   PRI 07-JAN-2026
DEFINITION  protein FAM136A isoform 3 [Homo sapiens].
ACCESSION   NP_001316682
VERSION     NP_001316682.1
DBSOURCE    REFSEQ: accession NM_001329753.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Otsuka,Y. and Yano,M.
  TITLE     FAM136A depletion induces mitochondrial stress and reduces
            mitochondrial membrane potential and ATP production
  JOURNAL   FEBS Open Bio 15 (5), 738-753 (2025)
   PUBMED   39821719
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Zhao,L., Ge,C., Zhang,Z., Hu,H., Zhang,Y., Zhao,W., Li,R., Zeng,B.,
            Song,X. and Li,G.
  TITLE     FAM136A immunoreactivity is associated with nodal involvement and
            survival in lung adenocarcinoma in a Chinese case series
  JOURNAL   Bioengineered 11 (1), 261-271 (2020)
   PUBMED   32098576
  REMARK    GeneRIF: FAM136A immunoreactivity is associated with nodal
            involvement and survival in lung adenocarcinoma in a Chinese case
            series.
REFERENCE   6  (residues 1 to 223)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 223)
  AUTHORS   Frejo,L., Giegling,I., Teggi,R., Lopez-Escamez,J.A. and Rujescu,D.
  TITLE     Genetics of vestibular disorders: pathophysiological insights
  JOURNAL   J Neurol 263 Suppl 1, S45-S53 (2016)
   PUBMED   27083884
  REMARK    GeneRIF: This study showed that FAM136A genes have been identified
            in familial Meniere's disease.
            Review article
REFERENCE   8  (residues 1 to 223)
  AUTHORS   Requena,T., Cabrera,S., Martin-Sierra,C., Price,S.D., Lysakowski,A.
            and Lopez-Escamez,J.A.
  TITLE     Identification of two novel mutations in FAM136A and DTNA genes in
            autosomal-dominant familial Meniere's disease
  JOURNAL   Hum Mol Genet 24 (4), 1119-1126 (2015)
   PUBMED   25305078
  REMARK    GeneRIF: our findings suggest that novel mutations in FAM136A and
            DTNA genes are probably causal variants in FMD.
REFERENCE   9  (residues 1 to 223)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY161689.1, AK225151.1,
            BE313508.1 and BC026293.1.
            
            Summary: This gene encodes a mitochondrially localized protein that
            is highly conserved across species. The gene is expressed in a
            variety of tissues including human lymphoblast cells and rat
            neurosensorial epithelium of the cristaampullaris. A mutation in
            this gene has been associated with familial Meniere's disease, a
            chronic disorder of the inner ear. Several pseudogenes of this gene
            are found on other chromosomes. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Aug 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.84385.1,
                                           SRR1803612.157864.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153031, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 25305078; reported by
                                                  MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..223
                     /product="protein FAM136A isoform 3"
                     /note="protein FAM136A; family with sequence similarity
                     136 member A"
                     /calculated_mol_wt=24267
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q96C01.1)"
     Region          114..212
                     /region_name="DUF842"
                     /note="Eukaryotic protein of unknown function (DUF842);
                     pfam05811"
                     /db_xref="CDD:461747"
     CDS             1..223
                     /gene="TIMCC"
                     /gene_synonym="FAM136A"
                     /coded_by="NM_001329753.2:57..728"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:84908"
                     /db_xref="HGNC:HGNC:25911"
                     /db_xref="MIM:616275"
ORIGIN      
        1 maelqqlrvq eavesmvksl erenirkmqv aglgpnqdpl lsgwvpgpsl shhatpctaa
       61 aspqtgcgrp wgrrgglgqd fgsfggsdei rvplpcarlf sapsspgqer prrqglmfrc
      121 sasccedsqa smkqvhqcie rchvplaqaq alvtselekf qdrlarctmh cndkakdsid
      181 agskelqvkq qldscvtkcv ddhmhliptm tkkmkealls igk
//
LOCUS       NP_001316684             107 aa            linear   PRI 07-JAN-2026
DEFINITION  protein FAM136A isoform 4 [Homo sapiens].
ACCESSION   NP_001316684
VERSION     NP_001316684.1
DBSOURCE    REFSEQ: accession NM_001329755.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 107)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 107)
  AUTHORS   Otsuka,Y. and Yano,M.
  TITLE     FAM136A depletion induces mitochondrial stress and reduces
            mitochondrial membrane potential and ATP production
  JOURNAL   FEBS Open Bio 15 (5), 738-753 (2025)
   PUBMED   39821719
REFERENCE   3  (residues 1 to 107)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 107)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 107)
  AUTHORS   Zhao,L., Ge,C., Zhang,Z., Hu,H., Zhang,Y., Zhao,W., Li,R., Zeng,B.,
            Song,X. and Li,G.
  TITLE     FAM136A immunoreactivity is associated with nodal involvement and
            survival in lung adenocarcinoma in a Chinese case series
  JOURNAL   Bioengineered 11 (1), 261-271 (2020)
   PUBMED   32098576
  REMARK    GeneRIF: FAM136A immunoreactivity is associated with nodal
            involvement and survival in lung adenocarcinoma in a Chinese case
            series.
REFERENCE   6  (residues 1 to 107)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 107)
  AUTHORS   Frejo,L., Giegling,I., Teggi,R., Lopez-Escamez,J.A. and Rujescu,D.
  TITLE     Genetics of vestibular disorders: pathophysiological insights
  JOURNAL   J Neurol 263 Suppl 1, S45-S53 (2016)
   PUBMED   27083884
  REMARK    GeneRIF: This study showed that FAM136A genes have been identified
            in familial Meniere's disease.
            Review article
REFERENCE   8  (residues 1 to 107)
  AUTHORS   Requena,T., Cabrera,S., Martin-Sierra,C., Price,S.D., Lysakowski,A.
            and Lopez-Escamez,J.A.
  TITLE     Identification of two novel mutations in FAM136A and DTNA genes in
            autosomal-dominant familial Meniere's disease
  JOURNAL   Hum Mol Genet 24 (4), 1119-1126 (2015)
   PUBMED   25305078
  REMARK    GeneRIF: our findings suggest that novel mutations in FAM136A and
            DTNA genes are probably causal variants in FMD.
REFERENCE   9  (residues 1 to 107)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP334741.1, BC026293.1,
            CB108776.1 and AK225151.1.
            
            Summary: This gene encodes a mitochondrially localized protein that
            is highly conserved across species. The gene is expressed in a
            variety of tissues including human lymphoblast cells and rat
            neurosensorial epithelium of the cristaampullaris. A mutation in
            this gene has been associated with familial Meniere's disease, a
            chronic disorder of the inner ear. Several pseudogenes of this gene
            are found on other chromosomes. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Aug 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC026293.1, SRR7346977.948978.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 25305078; reported by
                                                  MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..107
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..107
                     /product="protein FAM136A isoform 4"
                     /note="protein FAM136A; family with sequence similarity
                     136 member A"
                     /calculated_mol_wt=11883
     Region          <1..96
                     /region_name="DUF842"
                     /note="Eukaryotic protein of unknown function (DUF842);
                     pfam05811"
                     /db_xref="CDD:461747"
     CDS             1..107
                     /gene="TIMCC"
                     /gene_synonym="FAM136A"
                     /coded_by="NM_001329755.2:773..1096"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:84908"
                     /db_xref="HGNC:HGNC:25911"
                     /db_xref="MIM:616275"
ORIGIN      
        1 mfrcsascce dsqasmkqvh qcierchvpl aqaqalvtse lekfqdrlar ctmhcndkak
       61 dsidagskel qvkqqldscv tkcvddhmhl iptmtkkmke allsigk
//
LOCUS       NP_116211                138 aa            linear   PRI 07-JAN-2026
DEFINITION  protein FAM136A isoform 1 [Homo sapiens].
ACCESSION   NP_116211
VERSION     NP_116211.2
DBSOURCE    REFSEQ: accession NM_032822.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Otsuka,Y. and Yano,M.
  TITLE     FAM136A depletion induces mitochondrial stress and reduces
            mitochondrial membrane potential and ATP production
  JOURNAL   FEBS Open Bio 15 (5), 738-753 (2025)
   PUBMED   39821719
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 138)
  AUTHORS   Zhao,L., Ge,C., Zhang,Z., Hu,H., Zhang,Y., Zhao,W., Li,R., Zeng,B.,
            Song,X. and Li,G.
  TITLE     FAM136A immunoreactivity is associated with nodal involvement and
            survival in lung adenocarcinoma in a Chinese case series
  JOURNAL   Bioengineered 11 (1), 261-271 (2020)
   PUBMED   32098576
  REMARK    GeneRIF: FAM136A immunoreactivity is associated with nodal
            involvement and survival in lung adenocarcinoma in a Chinese case
            series.
REFERENCE   6  (residues 1 to 138)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 138)
  AUTHORS   Frejo,L., Giegling,I., Teggi,R., Lopez-Escamez,J.A. and Rujescu,D.
  TITLE     Genetics of vestibular disorders: pathophysiological insights
  JOURNAL   J Neurol 263 Suppl 1, S45-S53 (2016)
   PUBMED   27083884
  REMARK    GeneRIF: This study showed that FAM136A genes have been identified
            in familial Meniere's disease.
            Review article
REFERENCE   8  (residues 1 to 138)
  AUTHORS   Requena,T., Cabrera,S., Martin-Sierra,C., Price,S.D., Lysakowski,A.
            and Lopez-Escamez,J.A.
  TITLE     Identification of two novel mutations in FAM136A and DTNA genes in
            autosomal-dominant familial Meniere's disease
  JOURNAL   Hum Mol Genet 24 (4), 1119-1126 (2015)
   PUBMED   25305078
  REMARK    GeneRIF: our findings suggest that novel mutations in FAM136A and
            DTNA genes are probably causal variants in FMD.
REFERENCE   9  (residues 1 to 138)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB266394.1, AK225151.1,
            AK027574.1 and CB853567.1.
            
            On Jun 7, 2008 this sequence version replaced NP_116211.1.
            
            Summary: This gene encodes a mitochondrially localized protein that
            is highly conserved across species. The gene is expressed in a
            variety of tissues including human lymphoblast cells and rat
            neurosensorial epithelium of the cristaampullaris. A mutation in
            this gene has been associated with familial Meniere's disease, a
            chronic disorder of the inner ear. Several pseudogenes of this gene
            are found on other chromosomes. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Aug 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.300755.1,
                                           SRR5189658.219773.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 25305078; reported by
                                                  MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..138
                     /product="protein FAM136A isoform 1"
                     /note="protein FAM136A; family with sequence similarity
                     136 member A"
                     /calculated_mol_wt=15510
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q96C01.1)"
     Region          5..127
                     /region_name="DUF842"
                     /note="Eukaryotic protein of unknown function (DUF842);
                     pfam05811"
                     /db_xref="CDD:461747"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:B0BN94; propagated from
                     UniProtKB/Swiss-Prot (Q96C01.1)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:B0BN94; propagated from
                     UniProtKB/Swiss-Prot (Q96C01.1)"
     CDS             1..138
                     /gene="TIMCC"
                     /gene_synonym="FAM136A"
                     /coded_by="NM_032822.3:57..473"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1904.1"
                     /db_xref="GeneID:84908"
                     /db_xref="HGNC:HGNC:25911"
                     /db_xref="MIM:616275"
ORIGIN      
        1 maelqqlrvq eavesmvksl erenirkmqg lmfrcsascc edsqasmkqv hqcierchvp
       61 laqaqalvts elekfqdrla rctmhcndka kdsidagske lqvkqqldsc vtkcvddhmh
      121 liptmtkkmk eallsigk
//
LOCUS       NP_001091970            1264 aa            linear   PRI 07-JAN-2026
DEFINITION  sickle tail protein homolog isoform 2 [Homo sapiens].
ACCESSION   NP_001091970
VERSION     NP_001091970.1
DBSOURCE    REFSEQ: accession NM_001098500.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1264)
  AUTHORS   Morellato,A., De Gregorio,M., Angelini,C., Torelli,F., Belmonte,V.,
            Alfieri,A., Bersia,B., Cravero,T., Gai,M., Bianciotto,O.T.,
            Oddone,R., Salemme,V., Natalini,D., Centonze,G., Nigrelli,F.,
            Raspanti,A., Gurgone,A., D'Attanasio,G., Mele,P., Eva,C., Lodi,A.,
            Gavello,D., Carabelli,V., Hidisoglu,E., Chiantia,G., Carbone,E.,
            Becchetti,A., Giustetto,M., Marcantoni,A., Turco,E., Bertocchi,I.
            and Defilippi,P.
  TITLE     The adaptor protein SKT interacts with PSD-95 and SHANK3 and
            affects synaptic functions
  JOURNAL   Cell Rep 44 (9), 116206 (2025)
   PUBMED   40892546
REFERENCE   2  (residues 1 to 1264)
  AUTHORS   Dai,J., Jiang,H., Cheng,Z., Li,Y. and Tang,X.
  TITLE     Genetic polymorphism of KIAA1217 is functionally associated with
            lumbar disc herniation in the Chinese population
  JOURNAL   Neurochirurgie 70 (2), 101538 (2024)
   PUBMED   38311218
  REMARK    GeneRIF: Genetic polymorphism of KIAA1217 is functionally
            associated with lumbar disc herniation in the Chinese population.
REFERENCE   3  (residues 1 to 1264)
  AUTHORS   Wang,Y., Li,N., Zheng,Y., Wang,A., Yu,C., Song,Z., Wang,S., Sun,Y.,
            Zheng,L., Wang,G., Liu,L., Yi,J., Huang,Y., Zhang,M., Bao,Y. and
            Sun,L.
  TITLE     KIAA1217 Promotes Epithelial-Mesenchymal Transition and
            Hepatocellular Carcinoma Metastasis by Interacting with and
            Activating STAT3
  JOURNAL   Int J Mol Sci 23 (1), 104 (2021)
   PUBMED   35008530
  REMARK    GeneRIF: KIAA1217 Promotes Epithelial-Mesenchymal Transition and
            Hepatocellular Carcinoma Metastasis by Interacting with and
            Activating STAT3.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1264)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 1264)
  AUTHORS   Al Dhaheri,N., Wu,N., Zhao,S., Wu,Z., Blank,R.D., Zhang,J.,
            Raggio,C., Halanski,M., Shen,J., Noonan,K., Qiu,G., Nemeth,B.,
            Sund,S., Dunwoodie,S.L., Chapman,G., Glurich,I., Steiner,R.D.,
            Wohler,E., Martin,R., Sobreira,N.L. and Giampietro,P.F.
  TITLE     KIAA1217: A novel candidate gene associated with isolated and
            syndromic vertebral malformations
  JOURNAL   Am J Med Genet A 182 (7), 1664-1672 (2020)
   PUBMED   32369272
  REMARK    GeneRIF: KIAA1217: A novel candidate gene associated with isolated
            and syndromic vertebral malformations.
REFERENCE   6  (residues 1 to 1264)
  AUTHORS   Wheeler,E., Huang,N., Bochukova,E.G., Keogh,J.M., Lindsay,S.,
            Garg,S., Henning,E., Blackburn,H., Loos,R.J., Wareham,N.J.,
            O'Rahilly,S., Hurles,M.E., Barroso,I. and Farooqi,I.S.
  TITLE     Genome-wide SNP and CNV analysis identifies common and
            low-frequency variants associated with severe early-onset obesity
  JOURNAL   Nat Genet 45 (5), 513-517 (2013)
   PUBMED   23563609
REFERENCE   7  (residues 1 to 1264)
  AUTHORS   Kelempisioti,A., Eskola,P.J., Okuloff,A., Karjalainen,U.,
            Takatalo,J., Daavittila,I., Niinimaki,J., Sequeiros,R.B.,
            Tervonen,O., Solovieva,S., Kao,P.Y., Song,Y.Q., Cheung,K.M.,
            Chan,D., Ala-Kokko,L., Jarvelin,M.R., Karppinen,J. and Mannikko,M.
  TITLE     Genetic susceptibility of intervertebral disc degeneration among
            young Finnish adults
  JOURNAL   BMC Med Genet 12, 153 (2011)
   PUBMED   22107760
  REMARK    GeneRIF: SKT is involved in the etiology of intervertebral disc
            degeneration among young adults.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1264)
  AUTHORS   Cirulli,E.T., Kasperaviciute,D., Attix,D.K., Need,A.C., Ge,D.,
            Gibson,G. and Goldstein,D.B.
  TITLE     Common genetic variation and performance on standardized cognitive
            tests
  JOURNAL   Eur J Hum Genet 18 (7), 815-820 (2010)
   PUBMED   20125193
  REMARK    Erratum:[Eur J Hum Genet. 2010 Jul;18(7):820]
REFERENCE   9  (residues 1 to 1264)
  AUTHORS   Eriksson,N., Macpherson,J.M., Tung,J.Y., Hon,L.S., Naughton,B.,
            Saxonov,S., Avey,L., Wojcicki,A., Pe'er,I. and Mountain,J.
  TITLE     Web-based, participant-driven studies yield novel genetic
            associations for common traits
  JOURNAL   PLoS Genet 6 (6), e1000993 (2010)
   PUBMED   20585627
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1264)
  AUTHORS   Karasugi,T., Semba,K., Hirose,Y., Kelempisioti,A., Nakajima,M.,
            Miyake,A., Furuichi,T., Kawaguchi,Y., Mikami,Y., Chiba,K.,
            Kamata,M., Ozaki,K., Takahashi,A., Makela,P., Karppinen,J.,
            Kimura,T., Kubo,T., Toyama,Y., Yamamura,K., Mannikko,M., Mizuta,H.
            and Ikegawa,S.
  TITLE     Association of the tag SNPs in the human SKT gene (KIAA1217) with
            lumbar disc herniation
  JOURNAL   J Bone Miner Res 24 (9), 1537-1543 (2009)
   PUBMED   19338451
  REMARK    GeneRIF: Using tag SNPs, we examined the association in two
            independent Japanese case-control populations and found a
            significant association of lumbar herniation with SKT rs16924573 in
            the allele frequency model
            GeneRIF: Observational study and meta-analysis of gene-disease
            association. (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL353650.5, AB033043.2 and AB291616.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at a
            downstream start codon, compared to variant 1. It also lacks three
            in-frame exons at the 3' end of the coding region compared to
            variant 1. The encoded isoform (2) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB033043.2, SRR1803615.167221.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1264
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.2-p12.1"
     Protein         1..1264
                     /product="sickle tail protein homolog isoform 2"
                     /note="sickle tail protein homolog; likely orthologue of
                     Mus musculus enhancer trap locus 4"
                     /calculated_mol_wt=137782
     Region          108..>239
                     /region_name="AIP3"
                     /note="Actin interacting protein 3; pfam03915"
                     /db_xref="CDD:427585"
     CDS             1..1264
                     /gene="KIAA1217"
                     /gene_synonym="ETL4; SKT"
                     /coded_by="NM_001098500.3:829..4623"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS41496.1"
                     /db_xref="GeneID:56243"
                     /db_xref="HGNC:HGNC:25428"
                     /db_xref="MIM:617367"
ORIGIN      
        1 mqtsemdrkr eaflehlkqk yphhasaimg hqerlrdqtr spklshspqp pslgdpvehl
       61 setsadslea msegdaptpf srgsrtrasl pvvrstnqtk erslgvlylq ygdetkqlrm
      121 pneitsadti ralfvsafpq qltmkmlesp svaiyikdes rnvyyelndv rniqdrsllk
      181 vynkdpahaf nhtpktmngd mrmqrelvya rgdgpgaprp gstahpphai pnsppstpvp
      241 hsmppspsri pyggtrsmvv pgnatiprdr isslpvsrpi spspsailer rdvkpdedms
      301 gkniamyrne gfyadpylyh egrmsiassh gghpldvpdh iiayhrtair sasaycnpsm
      361 qaemhmeqsl yrqksrkypd shlptlgskt ppasphrvsd lrmidmhahy nahgpphtmq
      421 pdraspsrqa fkkepgtlvy iekprsaagl sslvdlgppl mekqvfayst atipkdretr
      481 ermqamekqi asltglvqsa lfkgpitsys kdassekmmk ttanrnhtds agtphvsggk
      541 mlsalestvp psqpppvgts aihmsllemr rsvaelrlql qqmrqlqlqn qellrammkk
      601 aeleisgkvm etmkrledpv qrqrvlveqe rqkylheeek ivkklceled fvedlkkdst
      661 aasrlvtlkd vedgafllrq vgeavatlkg efptlqnkmr ailrieveav rflkeephkl
      721 dsllkrvrsm tdvltmlrrh vtdgllkgtd aaqaaqymam ekataaevlk sqeeaahtsg
      781 qpfhstgapg daksevvpls gmmvrhaqss pvviqpsqhs vallnpaqnl phvasspavp
      841 qeatstlqms qapqspqipm ngsamqslfi eeihsvsakn ravsiekaek kweekrqnld
      901 hyngkefekl leeaqanimk sipnlemppa tgplprgdap vdkvelseds pnseqdlekl
      961 ggkspppppp pprrsylpgs gltttrsgdv vytgrkenit akassedagp spqtratkyp
     1021 aeepasawtp spppvttsss kdeeeeeeeg dkimaelqgs sgapqtsrmp vpmsaknrpg
     1081 tldkpgkqsk lqdprqyrqa ngsakksggd fkptspslpa skipalspss gkssslpsss
     1141 gdssnlpnpp atkpsiasnp lspqtgppah saslipsvsn gslkfqslth tgkghhlsfs
     1201 pqsqngrapp plsfssspps passvslnqg akgtrtihtp sltsykaqng ssskatpsta
     1261 kets
//
LOCUS       NP_955382                431 aa            linear   PRI 07-JAN-2026
DEFINITION  uncharacterized protein C9orf50 [Homo sapiens].
ACCESSION   NP_955382 XP_351853
VERSION     NP_955382.3
DBSOURCE    REFSEQ: accession NM_199350.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Shao,T., Liu,C., Kuang,J., Xie,S., Qu,Y., Li,Y., Zhang,L., Liu,F.,
            Qi,Y., Hou,T., Li,M., Zhang,S., Liu,Y., Yuan,Z., Liu,J., Hu,Y.,
            Wang,J., Song,C., Zhang,S., Zhu,L., Shao,J., Lin,A., Mao,W.,
            Wang,G. and Zhu,L.
  TITLE     Genome-wide CRISPR screen reveals an uncharacterized spliceosome
            regulator as new candidate immunotherapy target
  JOURNAL   Imeta 4 (6), e70096 (2025)
   PUBMED   41472851
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Pineau,C., Hikmet,F., Zhang,C., Oksvold,P., Chen,S., Fagerberg,L.,
            Uhlen,M. and Lindskog,C.
  TITLE     Cell Type-Specific Expression of Testis Elevated Genes Based on
            Transcriptomics and Antibody-Based Proteomics
  JOURNAL   J Proteome Res 18 (12), 4215-4230 (2019)
   PUBMED   31429579
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Yu,B., Zheng,Y., Alexander,D., Manolio,T.A., Alonso,A.,
            Nettleton,J.A. and Boerwinkle,E.
  TITLE     Genome-wide association study of a heart failure related
            metabolomic profile among African Americans in the Atherosclerosis
            Risk in Communities (ARIC) study
  JOURNAL   Genet Epidemiol 37 (8), 840-845 (2013)
   PUBMED   23934736
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Clark,S.L., Adkins,D.E., Aberg,K., Hettema,J.M., McClay,J.L.,
            Souza,R.P. and van den Oord,E.J.
  TITLE     Pharmacogenomic study of side-effects for antidepressant treatment
            options in STAR*D
  JOURNAL   Psychol Med 42 (6), 1151-1162 (2012)
   PUBMED   22041458
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Fardilha,M., Esteves,S.L., Korrodi-Gregorio,L., Vintem,A.P.,
            Domingues,S.C., Rebelo,S., Morrice,N., Cohen,P.T., da Cruz e
            Silva,O.A. and da Cruz e Silva,E.F.
  TITLE     Identification of the human testis protein phosphatase 1
            interactome
  JOURNAL   Biochem Pharmacol 82 (10), 1403-1415 (2011)
   PUBMED   21382349
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL590369.18 and AL391056.25.
            
            On Apr 25, 2007 this sequence version replaced NP_955382.2.
            
            Sequence Note:.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK093122.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372478.5/ ENSP00000361556.4
            RefSeq Select criteria :: based on manual assertion, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..431
                     /product="uncharacterized protein C9orf50"
                     /calculated_mol_wt=47508
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SZB4.1)"
     Region          102..132
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SZB4.1)"
     Region          193..301
                     /region_name="DUF4685"
                     /note="Domain of unknown function (DUF4685); pfam15737"
                     /db_xref="CDD:464834"
     CDS             1..431
                     /gene="C9orf50"
                     /coded_by="NM_199350.4:528..1823"
                     /db_xref="CCDS:CCDS35159.1"
                     /db_xref="GeneID:375759"
                     /db_xref="HGNC:HGNC:23677"
ORIGIN      
        1 mfwrrlrpga qdlapkglpg dgdfrrssdp rlpkltppal raalgargsg dwripgggaa
       61 wwpegdakpg vgvgrlpprl palltatrra vrkrgllrsl lpppllsaga sresaprqpg
      121 pgererprrr varedpdflg aflgellpsr freflhqlqe kcaeepeplt spapqhqrgv
      181 lehcpgsprc pncsflpdlw gqsshlqdsl tkislqqtpi lgplkgdhsq fttvrkanhr
      241 phgaqvprlk aalthnpsge gsrpcrqrcp frvrfadetl qdttlrywer rrsvqqsviv
      301 nqkaalpvas ervfgsvgkr leslpkalyp gakeetlass scwdcaglst qktqgylsed
      361 tsmnsslpfc swkkaaaqrp rsslrafldp hrnleqesll pnrvlqsvlk qgcpkgyhll
      421 lasatlqpdk r
//
LOCUS       NP_001308610            1061 aa            linear   PRI 07-JAN-2026
DEFINITION  sickle tail protein homolog isoform 8 [Homo sapiens].
ACCESSION   NP_001308610
VERSION     NP_001308610.1
DBSOURCE    REFSEQ: accession NM_001321681.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1061)
  AUTHORS   Morellato,A., De Gregorio,M., Angelini,C., Torelli,F., Belmonte,V.,
            Alfieri,A., Bersia,B., Cravero,T., Gai,M., Bianciotto,O.T.,
            Oddone,R., Salemme,V., Natalini,D., Centonze,G., Nigrelli,F.,
            Raspanti,A., Gurgone,A., D'Attanasio,G., Mele,P., Eva,C., Lodi,A.,
            Gavello,D., Carabelli,V., Hidisoglu,E., Chiantia,G., Carbone,E.,
            Becchetti,A., Giustetto,M., Marcantoni,A., Turco,E., Bertocchi,I.
            and Defilippi,P.
  TITLE     The adaptor protein SKT interacts with PSD-95 and SHANK3 and
            affects synaptic functions
  JOURNAL   Cell Rep 44 (9), 116206 (2025)
   PUBMED   40892546
REFERENCE   2  (residues 1 to 1061)
  AUTHORS   Dai,J., Jiang,H., Cheng,Z., Li,Y. and Tang,X.
  TITLE     Genetic polymorphism of KIAA1217 is functionally associated with
            lumbar disc herniation in the Chinese population
  JOURNAL   Neurochirurgie 70 (2), 101538 (2024)
   PUBMED   38311218
  REMARK    GeneRIF: Genetic polymorphism of KIAA1217 is functionally
            associated with lumbar disc herniation in the Chinese population.
REFERENCE   3  (residues 1 to 1061)
  AUTHORS   Wang,Y., Li,N., Zheng,Y., Wang,A., Yu,C., Song,Z., Wang,S., Sun,Y.,
            Zheng,L., Wang,G., Liu,L., Yi,J., Huang,Y., Zhang,M., Bao,Y. and
            Sun,L.
  TITLE     KIAA1217 Promotes Epithelial-Mesenchymal Transition and
            Hepatocellular Carcinoma Metastasis by Interacting with and
            Activating STAT3
  JOURNAL   Int J Mol Sci 23 (1), 104 (2021)
   PUBMED   35008530
  REMARK    GeneRIF: KIAA1217 Promotes Epithelial-Mesenchymal Transition and
            Hepatocellular Carcinoma Metastasis by Interacting with and
            Activating STAT3.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1061)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 1061)
  AUTHORS   Al Dhaheri,N., Wu,N., Zhao,S., Wu,Z., Blank,R.D., Zhang,J.,
            Raggio,C., Halanski,M., Shen,J., Noonan,K., Qiu,G., Nemeth,B.,
            Sund,S., Dunwoodie,S.L., Chapman,G., Glurich,I., Steiner,R.D.,
            Wohler,E., Martin,R., Sobreira,N.L. and Giampietro,P.F.
  TITLE     KIAA1217: A novel candidate gene associated with isolated and
            syndromic vertebral malformations
  JOURNAL   Am J Med Genet A 182 (7), 1664-1672 (2020)
   PUBMED   32369272
  REMARK    GeneRIF: KIAA1217: A novel candidate gene associated with isolated
            and syndromic vertebral malformations.
REFERENCE   6  (residues 1 to 1061)
  AUTHORS   Wheeler,E., Huang,N., Bochukova,E.G., Keogh,J.M., Lindsay,S.,
            Garg,S., Henning,E., Blackburn,H., Loos,R.J., Wareham,N.J.,
            O'Rahilly,S., Hurles,M.E., Barroso,I. and Farooqi,I.S.
  TITLE     Genome-wide SNP and CNV analysis identifies common and
            low-frequency variants associated with severe early-onset obesity
  JOURNAL   Nat Genet 45 (5), 513-517 (2013)
   PUBMED   23563609
REFERENCE   7  (residues 1 to 1061)
  AUTHORS   Kelempisioti,A., Eskola,P.J., Okuloff,A., Karjalainen,U.,
            Takatalo,J., Daavittila,I., Niinimaki,J., Sequeiros,R.B.,
            Tervonen,O., Solovieva,S., Kao,P.Y., Song,Y.Q., Cheung,K.M.,
            Chan,D., Ala-Kokko,L., Jarvelin,M.R., Karppinen,J. and Mannikko,M.
  TITLE     Genetic susceptibility of intervertebral disc degeneration among
            young Finnish adults
  JOURNAL   BMC Med Genet 12, 153 (2011)
   PUBMED   22107760
  REMARK    GeneRIF: SKT is involved in the etiology of intervertebral disc
            degeneration among young adults.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1061)
  AUTHORS   Cirulli,E.T., Kasperaviciute,D., Attix,D.K., Need,A.C., Ge,D.,
            Gibson,G. and Goldstein,D.B.
  TITLE     Common genetic variation and performance on standardized cognitive
            tests
  JOURNAL   Eur J Hum Genet 18 (7), 815-820 (2010)
   PUBMED   20125193
  REMARK    Erratum:[Eur J Hum Genet. 2010 Jul;18(7):820]
REFERENCE   9  (residues 1 to 1061)
  AUTHORS   Eriksson,N., Macpherson,J.M., Tung,J.Y., Hon,L.S., Naughton,B.,
            Saxonov,S., Avey,L., Wojcicki,A., Pe'er,I. and Mountain,J.
  TITLE     Web-based, participant-driven studies yield novel genetic
            associations for common traits
  JOURNAL   PLoS Genet 6 (6), e1000993 (2010)
   PUBMED   20585627
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1061)
  AUTHORS   Karasugi,T., Semba,K., Hirose,Y., Kelempisioti,A., Nakajima,M.,
            Miyake,A., Furuichi,T., Kawaguchi,Y., Mikami,Y., Chiba,K.,
            Kamata,M., Ozaki,K., Takahashi,A., Makela,P., Karppinen,J.,
            Kimura,T., Kubo,T., Toyama,Y., Yamamura,K., Mannikko,M., Mizuta,H.
            and Ikegawa,S.
  TITLE     Association of the tag SNPs in the human SKT gene (KIAA1217) with
            lumbar disc herniation
  JOURNAL   J Bone Miner Res 24 (9), 1537-1543 (2009)
   PUBMED   19338451
  REMARK    GeneRIF: Using tag SNPs, we examined the association in two
            independent Japanese case-control populations and found a
            significant association of lumbar herniation with SKT rs16924573 in
            the allele frequency model
            GeneRIF: Observational study and meta-analysis of gene-disease
            association. (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL353583.15 and AL392104.19.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.207988.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1061
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.2-p12.1"
     Protein         1..1061
                     /product="sickle tail protein homolog isoform 8"
                     /note="sickle tail protein homolog; likely orthologue of
                     Mus musculus enhancer trap locus 4"
                     /calculated_mol_wt=114643
     CDS             1..1061
                     /gene="KIAA1217"
                     /gene_synonym="ETL4; SKT"
                     /coded_by="NM_001321681.2:352..3537"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:56243"
                     /db_xref="HGNC:HGNC:25428"
                     /db_xref="MIM:617367"
ORIGIN      
        1 mqrelvyarg dgpgaprpgs tahpphaipn sppstpvphs mppspsripy ggtrsmvvpg
       61 natiprdris slpvsrpisp spsailerrd vkpdedmsgk niamyrnegf yadpylyheg
      121 rmsiasshgg hpldvpdhii ayhrtairsa saycnpsmqa emhmeqslyr qksrkypdsh
      181 lptlgsktpp asphrvsdlr midmhahyna hgpphtmqpd raspsrqafk kepgtlvyie
      241 kprsaaglss lvdlgpplme kqvfaystat ipkdretrer mqamekqias ltglvqsalf
      301 kgpitsyskd assekmmktt anrnhtdsag tphvsggkml salestvpps qpppvgtsai
      361 hmsllemrrs vaelrlqlqq mrqlqlqnqe llrammkkae leisgkvmet mkrledpvqr
      421 qrvlveqerq kylheeekiv kklceledfv edlkkdstaa srlvtlkdve dgafllrqvg
      481 eavatlkgef ptlqnkmrai lrieveavrf lkeephklds llkrvrsmtd vltmlrrhvt
      541 dgllkgtdaa qaaqymamek ataaevlksq eeaahtsgqp fhstgapgda ksevvplsgm
      601 mvrhaqsspv viqpsqhsva llnpaqnlph vasspavpqe atstlqmsqa pqspqipmng
      661 samqslfiee ihsvsaknra vsiekaekkw eekrqnldhy ngkefeklle eaqanimksi
      721 pnlemppatg plprgdapvd kvelsdspns eqdleklggk sppppppppr rsylpgsglt
      781 ttrsgdvvyt grkenitaka ssedagpspq tratkypaee pasawtpspp pvttssskde
      841 eeeeeegdki maelqgssga pqtsrmpvpm saknrpgtld kpgkqsklqd prqyrqangs
      901 akksggdfkp tspslpaski palspssgks sslpsssgds snlpnppatk psiasnplsp
      961 qtgppahsas lipsvsngsl kfqslthtgk ghhlsfspqs qngrapppls fsssppspas
     1021 svslnqgakg trtihtpslt sykaqngsss katpstaket s
//
LOCUS       NP_001269699             866 aa            linear   PRI 07-JAN-2026
DEFINITION  sickle tail protein homolog isoform 7 [Homo sapiens].
ACCESSION   NP_001269699 XP_005252583
VERSION     NP_001269699.1
DBSOURCE    REFSEQ: accession NM_001282770.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 866)
  AUTHORS   Morellato,A., De Gregorio,M., Angelini,C., Torelli,F., Belmonte,V.,
            Alfieri,A., Bersia,B., Cravero,T., Gai,M., Bianciotto,O.T.,
            Oddone,R., Salemme,V., Natalini,D., Centonze,G., Nigrelli,F.,
            Raspanti,A., Gurgone,A., D'Attanasio,G., Mele,P., Eva,C., Lodi,A.,
            Gavello,D., Carabelli,V., Hidisoglu,E., Chiantia,G., Carbone,E.,
            Becchetti,A., Giustetto,M., Marcantoni,A., Turco,E., Bertocchi,I.
            and Defilippi,P.
  TITLE     The adaptor protein SKT interacts with PSD-95 and SHANK3 and
            affects synaptic functions
  JOURNAL   Cell Rep 44 (9), 116206 (2025)
   PUBMED   40892546
REFERENCE   2  (residues 1 to 866)
  AUTHORS   Dai,J., Jiang,H., Cheng,Z., Li,Y. and Tang,X.
  TITLE     Genetic polymorphism of KIAA1217 is functionally associated with
            lumbar disc herniation in the Chinese population
  JOURNAL   Neurochirurgie 70 (2), 101538 (2024)
   PUBMED   38311218
  REMARK    GeneRIF: Genetic polymorphism of KIAA1217 is functionally
            associated with lumbar disc herniation in the Chinese population.
REFERENCE   3  (residues 1 to 866)
  AUTHORS   Wang,Y., Li,N., Zheng,Y., Wang,A., Yu,C., Song,Z., Wang,S., Sun,Y.,
            Zheng,L., Wang,G., Liu,L., Yi,J., Huang,Y., Zhang,M., Bao,Y. and
            Sun,L.
  TITLE     KIAA1217 Promotes Epithelial-Mesenchymal Transition and
            Hepatocellular Carcinoma Metastasis by Interacting with and
            Activating STAT3
  JOURNAL   Int J Mol Sci 23 (1), 104 (2021)
   PUBMED   35008530
  REMARK    GeneRIF: KIAA1217 Promotes Epithelial-Mesenchymal Transition and
            Hepatocellular Carcinoma Metastasis by Interacting with and
            Activating STAT3.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 866)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 866)
  AUTHORS   Al Dhaheri,N., Wu,N., Zhao,S., Wu,Z., Blank,R.D., Zhang,J.,
            Raggio,C., Halanski,M., Shen,J., Noonan,K., Qiu,G., Nemeth,B.,
            Sund,S., Dunwoodie,S.L., Chapman,G., Glurich,I., Steiner,R.D.,
            Wohler,E., Martin,R., Sobreira,N.L. and Giampietro,P.F.
  TITLE     KIAA1217: A novel candidate gene associated with isolated and
            syndromic vertebral malformations
  JOURNAL   Am J Med Genet A 182 (7), 1664-1672 (2020)
   PUBMED   32369272
  REMARK    GeneRIF: KIAA1217: A novel candidate gene associated with isolated
            and syndromic vertebral malformations.
REFERENCE   6  (residues 1 to 866)
  AUTHORS   Wheeler,E., Huang,N., Bochukova,E.G., Keogh,J.M., Lindsay,S.,
            Garg,S., Henning,E., Blackburn,H., Loos,R.J., Wareham,N.J.,
            O'Rahilly,S., Hurles,M.E., Barroso,I. and Farooqi,I.S.
  TITLE     Genome-wide SNP and CNV analysis identifies common and
            low-frequency variants associated with severe early-onset obesity
  JOURNAL   Nat Genet 45 (5), 513-517 (2013)
   PUBMED   23563609
REFERENCE   7  (residues 1 to 866)
  AUTHORS   Kelempisioti,A., Eskola,P.J., Okuloff,A., Karjalainen,U.,
            Takatalo,J., Daavittila,I., Niinimaki,J., Sequeiros,R.B.,
            Tervonen,O., Solovieva,S., Kao,P.Y., Song,Y.Q., Cheung,K.M.,
            Chan,D., Ala-Kokko,L., Jarvelin,M.R., Karppinen,J. and Mannikko,M.
  TITLE     Genetic susceptibility of intervertebral disc degeneration among
            young Finnish adults
  JOURNAL   BMC Med Genet 12, 153 (2011)
   PUBMED   22107760
  REMARK    GeneRIF: SKT is involved in the etiology of intervertebral disc
            degeneration among young adults.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 866)
  AUTHORS   Cirulli,E.T., Kasperaviciute,D., Attix,D.K., Need,A.C., Ge,D.,
            Gibson,G. and Goldstein,D.B.
  TITLE     Common genetic variation and performance on standardized cognitive
            tests
  JOURNAL   Eur J Hum Genet 18 (7), 815-820 (2010)
   PUBMED   20125193
  REMARK    Erratum:[Eur J Hum Genet. 2010 Jul;18(7):820]
REFERENCE   9  (residues 1 to 866)
  AUTHORS   Eriksson,N., Macpherson,J.M., Tung,J.Y., Hon,L.S., Naughton,B.,
            Saxonov,S., Avey,L., Wojcicki,A., Pe'er,I. and Mountain,J.
  TITLE     Web-based, participant-driven studies yield novel genetic
            associations for common traits
  JOURNAL   PLoS Genet 6 (6), e1000993 (2010)
   PUBMED   20585627
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 866)
  AUTHORS   Karasugi,T., Semba,K., Hirose,Y., Kelempisioti,A., Nakajima,M.,
            Miyake,A., Furuichi,T., Kawaguchi,Y., Mikami,Y., Chiba,K.,
            Kamata,M., Ozaki,K., Takahashi,A., Makela,P., Karppinen,J.,
            Kimura,T., Kubo,T., Toyama,Y., Yamamura,K., Mannikko,M., Mizuta,H.
            and Ikegawa,S.
  TITLE     Association of the tag SNPs in the human SKT gene (KIAA1217) with
            lumbar disc herniation
  JOURNAL   J Bone Miner Res 24 (9), 1537-1543 (2009)
   PUBMED   19338451
  REMARK    GeneRIF: Using tag SNPs, we examined the association in two
            independent Japanese case-control populations and found a
            significant association of lumbar herniation with SKT rs16924573 in
            the allele frequency model
            GeneRIF: Observational study and meta-analysis of gene-disease
            association. (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC387942.1, BC098577.1, AL833280.1 and AL392104.19.
            
            On Sep 19, 2013 this sequence version replaced XP_005252583.1.
            
            Transcript Variant: This variant (7) has multiple differences
            compared to variant 1. These differences result in distinct 5' and
            3' UTRs, in addition to translation initiation at a downstream
            start codon, compared to variant 1. The encoded protein (isoform 7)
            is shorter and has a distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098577.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..866
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.2-p12.1"
     Protein         1..866
                     /product="sickle tail protein homolog isoform 7"
                     /note="sickle tail protein homolog; likely orthologue of
                     Mus musculus enhancer trap locus 4"
                     /calculated_mol_wt=94992
     CDS             1..866
                     /gene="KIAA1217"
                     /gene_synonym="ETL4; SKT"
                     /coded_by="NM_001282770.2:261..2861"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS60505.1"
                     /db_xref="GeneID:56243"
                     /db_xref="HGNC:HGNC:25428"
                     /db_xref="MIM:617367"
ORIGIN      
        1 mqrelvyarg dgpgaprpgs tahpphaipn sppstpvphs mppspsripy ggtrsmvvpg
       61 natiprdris slpvsrpisp spsailerrd vkpdedmsgk niamyrnegf yadpylyheg
      121 rmsiasshgg hpldvpdhii ayhrtairsa saycnpsmqa emhmeqslyr qksrkypdsh
      181 lptlgsktpp asphrvsdlr midmhahyna hgpphtmqpd raspsrqafk kepgtlvyie
      241 kprsaaglss lvdlgpplme kqvfaystat ipkdretsek mmkttanrnh tdsagtphvs
      301 ggkmlsales tvppsqpppv gtsaihmsll emrrsvaelr lqlqqmrqlq lqnqellram
      361 mkkaeleisg kvmetmkrle dpvqrqrvlv eqerqkylhe eekivkklce ledfvedlkk
      421 dstaasrlvt lkdvedgafl lrqvgeavat lkgefptlqn kmrailriev eavrflkeep
      481 hkldsllkrv rsmtdvltml rrhvtdgllk gtdaaqaaqy mamekataae vlksqeeaah
      541 tsgqpfhstg apgdaksevv plsgmmvrha qsspvviqps qhsvallnpa qnlphvassp
      601 avpqeatstl qmsqapqspq ipmngsamqs lfieeihsvs aknravsiek aekkweekrq
      661 nldhyngkef eklleeaqan imksipnlem ppatgplprg dapvdkvels edspnseqdl
      721 eklggksppp ppppprrsyl pgsgltttrs gdvvytgrke nitakassed agpspqtrat
      781 kypaeepasa wtpspppvtt ssskdeeeee eegdkimael qgssgapqts rmpvpmsakn
      841 rpgtldkpgk qsklqdprqy rqvvlp
//
LOCUS       NP_001121100             338 aa            linear   PRI 07-JAN-2026
DEFINITION  fructose-1,6-bisphosphatase 1 [Homo sapiens].
ACCESSION   NP_001121100
VERSION     NP_001121100.1
DBSOURCE    REFSEQ: accession NM_001127628.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Li,M., Wang,Z., Tao,J., Jiang,H., Yang,H., Guo,D., Zhao,H., He,X.,
            Luo,S., Jiang,X., Yuan,L., Xiao,L., He,H., Yu,R., Fang,J.,
            Liang,T., Mao,Z., Xu,D. and Lu,Z.
  TITLE     Fructose-1,6-bisphosphatase 1 dephosphorylates and inhibits TERT
            for tumor suppression
  JOURNAL   Nat Chem Biol 20 (11), 1505-1513 (2024)
   PUBMED   38538923
  REMARK    GeneRIF: Fructose-1,6-bisphosphatase 1 dephosphorylates and
            inhibits TERT for tumor suppression.
            Erratum:[Nat Chem Biol. 2024 Nov;20(11):1547. doi:
            10.1038/s41589-024-01623-3. PMID: 38649455]
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Peng,X., Ma,L., Chen,X., Tang,F. and Zong,X.
  TITLE     Inhibition of FBP1 expression by KMT5A through TWIST1 methylation
            is one of the mechanisms leading to chemoresistance in breast
            cancer
  JOURNAL   Oncol Rep 52 (2) (2024)
   PUBMED   38963044
  REMARK    GeneRIF: Inhibition of FBP1 expression by KMT5A through TWIST1
            methylation is one of the mechanisms leading to chemoresistance in
            breast cancer.
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Zhang,P., Yang,J., Liu,X., Huang,C., Tao,Y., Shen,P., Bai,Z.,
            Xiao,C., Zhou,L., Li,G., Zhang,L., Zhou,W. and Gao,Y.
  TITLE     FBP1 orchestrates keratinocyte proliferation/differentiation and
            suppresses psoriasis through metabolic control of histone
            acetylation
  JOURNAL   Cell Death Dis 15 (6), 392 (2024)
   PUBMED   38834617
  REMARK    GeneRIF: FBP1 orchestrates keratinocyte
            proliferation/differentiation and suppresses psoriasis through
            metabolic control of histone acetylation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 338)
  AUTHORS   He,T., Wang,Y., Lv,W., Wang,Y., Li,X., Zhang,Q., Shen,H.M. and
            Hu,J.
  TITLE     FBP1 inhibits NSCLC stemness by promoting ubiquitination of Notch1
            intracellular domain and accelerating degradation
  JOURNAL   Cell Mol Life Sci 81 (1), 87 (2024)
   PUBMED   38349431
  REMARK    GeneRIF: FBP1 inhibits NSCLC stemness by promoting ubiquitination
            of Notch1 intracellular domain and accelerating degradation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Wang,Z., Wang,X., Liu,L., Guo,X., Zhang,H., Yin,J., Lin,R., Shao,Y.
            and Cai,D.
  TITLE     Fructose-bisphosphatase1 (FBP1) alleviates experimental
            osteoarthritis by regulating Protein crumbs homolog 3 (CRB3)
  JOURNAL   Arthritis Res Ther 25 (1), 235 (2023)
   PUBMED   38049890
  REMARK    GeneRIF: Fructose-bisphosphatase1 (FBP1) alleviates experimental
            osteoarthritis by regulating Protein crumbs homolog 3 (CRB3).
            Erratum:[Arthritis Res Ther. 2023 Dec 28;25(1):250. doi:
            10.1186/s13075-023-03247-9. PMID: 38155346]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 338)
  AUTHORS   el-Maghrabi,M.R., Lange,A.J., Jiang,W., Yamagata,K., Stoffel,M.,
            Takeda,J., Fernald,A.A., Le Beau,M.M., Bell,G.I., Baker,L. et al.
  TITLE     Human fructose-1,6-bisphosphatase gene (FBP1): exon-intron
            organization, localization to chromosome bands 9q22.2-q22.3, and
            mutation screening in subjects with fructose-1,6-bisphosphatase
            deficiency
  JOURNAL   Genomics 27 (3), 520-525 (1995)
   PUBMED   7558035
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Bijarnia-Mahay,S., Bhatia,S. and Arora,V.
  TITLE     Fructose-1,6-Bisphosphatase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31804789
REFERENCE   8  (residues 1 to 338)
  AUTHORS   el-Maghrabi,M.R., Lange,A.J., Kummel,L. and Pilkis,S.J.
  TITLE     The rat fructose-1,6-bisphosphatase gene. Structure and regulation
            of expression
  JOURNAL   J Biol Chem 266 (4), 2115-2120 (1991)
   PUBMED   1846613
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Ke,H.M., Zhang,Y.P. and Lipscomb,W.N.
  TITLE     Crystal structure of fructose-1,6-bisphosphatase complexed with
            fructose 6-phosphate, AMP, and magnesium
  JOURNAL   Proc Natl Acad Sci U S A 87 (14), 5243-5247 (1990)
   PUBMED   2164670
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Solomon,D.H., Raynal,M.C., Tejwani,G.A. and Cayre,Y.E.
  TITLE     Activation of the fructose 1,6-bisphosphatase gene by
            1,25-dihydroxyvitamin D3 during monocytic differentiation
  JOURNAL   Proc Natl Acad Sci U S A 85 (18), 6904-6908 (1988)
   PUBMED   2842796
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL161728.25.
            
            Summary: Fructose-1,6-bisphosphatase 1, a gluconeogenesis
            regulatory enzyme, catalyzes the hydrolysis of fructose
            1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate.
            Fructose-1,6-diphosphatase deficiency is associated with
            hypoglycemia and metabolic acidosis. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK292199.1, SRR11853567.30541.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..338
                     /product="fructose-1,6-bisphosphatase 1"
                     /EC_number="3.1.3.11"
                     /note="FBPase 1; D-fructose-1,6-bisphosphate
                     1-phosphohydrolase 1; liver FBPase; growth-inhibiting
                     protein 17"
                     /calculated_mol_wt=36711
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P00637; propagated from
                     UniProtKB/Swiss-Prot (P09467.5)"
     Region          18..332
                     /region_name="FBPase"
                     /note="Fructose-1,6-bisphosphatase, an enzyme that
                     catalyzes the hydrolysis of fructose-1,6-biphosphate into
                     fructose-6-phosphate and is critical in gluconeogenesis
                     pathway. The alignment model also includes chloroplastic
                     FBPases and sedoheptulose-1; cd00354"
                     /db_xref="CDD:238214"
     Site            order(18,21,28,30..32,113..114,141)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:238214"
     Site            order(75,98..99,119,121,281)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:238214"
     Site            order(122,124..125,216,244..245,249,265,275)
                     /site_type="active"
                     /db_xref="CDD:238214"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXD6; propagated from
                     UniProtKB/Swiss-Prot (P09467.5)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXD6; propagated from
                     UniProtKB/Swiss-Prot (P09467.5)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P09467.5)"
     CDS             1..338
                     /gene="FBP1"
                     /gene_synonym="FBP"
                     /coded_by="NM_001127628.2:245..1261"
                     /db_xref="CCDS:CCDS6712.1"
                     /db_xref="GeneID:2203"
                     /db_xref="HGNC:HGNC:3606"
                     /db_xref="MIM:611570"
ORIGIN      
        1 madqapfdtd vntltrfvme egrkargtge ltqllnslct avkaissavr kagiahlygi
       61 agstnvtgdq vkkldvlsnd lvmnmlkssf atcvlvseed khaiivepek rgkyvvcfdp
      121 ldgssnidcl vsvgtifgiy rkkstdepse kdalqpgrnl vaagyalygs atmlvlamdc
      181 gvncfmldpa igefilvdkd vkikkkgkiy slnegyardf dpavteyiqr kkfppdnsap
      241 ygaryvgsmv advhrtlvyg giflypankk spngklrlly ecnpmayvme kaggmattgk
      301 eavldviptd ihqrapvilg spddvleflk vyekhsaq
//
LOCUS       NP_062536               1943 aa            linear   PRI 07-JAN-2026
DEFINITION  sickle tail protein homolog isoform 1 [Homo sapiens].
ACCESSION   NP_062536 XP_166112
VERSION     NP_062536.2
DBSOURCE    REFSEQ: accession NM_019590.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1943)
  AUTHORS   Morellato,A., De Gregorio,M., Angelini,C., Torelli,F., Belmonte,V.,
            Alfieri,A., Bersia,B., Cravero,T., Gai,M., Bianciotto,O.T.,
            Oddone,R., Salemme,V., Natalini,D., Centonze,G., Nigrelli,F.,
            Raspanti,A., Gurgone,A., D'Attanasio,G., Mele,P., Eva,C., Lodi,A.,
            Gavello,D., Carabelli,V., Hidisoglu,E., Chiantia,G., Carbone,E.,
            Becchetti,A., Giustetto,M., Marcantoni,A., Turco,E., Bertocchi,I.
            and Defilippi,P.
  TITLE     The adaptor protein SKT interacts with PSD-95 and SHANK3 and
            affects synaptic functions
  JOURNAL   Cell Rep 44 (9), 116206 (2025)
   PUBMED   40892546
REFERENCE   2  (residues 1 to 1943)
  AUTHORS   Dai,J., Jiang,H., Cheng,Z., Li,Y. and Tang,X.
  TITLE     Genetic polymorphism of KIAA1217 is functionally associated with
            lumbar disc herniation in the Chinese population
  JOURNAL   Neurochirurgie 70 (2), 101538 (2024)
   PUBMED   38311218
  REMARK    GeneRIF: Genetic polymorphism of KIAA1217 is functionally
            associated with lumbar disc herniation in the Chinese population.
REFERENCE   3  (residues 1 to 1943)
  AUTHORS   Wang,Y., Li,N., Zheng,Y., Wang,A., Yu,C., Song,Z., Wang,S., Sun,Y.,
            Zheng,L., Wang,G., Liu,L., Yi,J., Huang,Y., Zhang,M., Bao,Y. and
            Sun,L.
  TITLE     KIAA1217 Promotes Epithelial-Mesenchymal Transition and
            Hepatocellular Carcinoma Metastasis by Interacting with and
            Activating STAT3
  JOURNAL   Int J Mol Sci 23 (1), 104 (2021)
   PUBMED   35008530
  REMARK    GeneRIF: KIAA1217 Promotes Epithelial-Mesenchymal Transition and
            Hepatocellular Carcinoma Metastasis by Interacting with and
            Activating STAT3.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1943)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 1943)
  AUTHORS   Al Dhaheri,N., Wu,N., Zhao,S., Wu,Z., Blank,R.D., Zhang,J.,
            Raggio,C., Halanski,M., Shen,J., Noonan,K., Qiu,G., Nemeth,B.,
            Sund,S., Dunwoodie,S.L., Chapman,G., Glurich,I., Steiner,R.D.,
            Wohler,E., Martin,R., Sobreira,N.L. and Giampietro,P.F.
  TITLE     KIAA1217: A novel candidate gene associated with isolated and
            syndromic vertebral malformations
  JOURNAL   Am J Med Genet A 182 (7), 1664-1672 (2020)
   PUBMED   32369272
  REMARK    GeneRIF: KIAA1217: A novel candidate gene associated with isolated
            and syndromic vertebral malformations.
REFERENCE   6  (residues 1 to 1943)
  AUTHORS   Wheeler,E., Huang,N., Bochukova,E.G., Keogh,J.M., Lindsay,S.,
            Garg,S., Henning,E., Blackburn,H., Loos,R.J., Wareham,N.J.,
            O'Rahilly,S., Hurles,M.E., Barroso,I. and Farooqi,I.S.
  TITLE     Genome-wide SNP and CNV analysis identifies common and
            low-frequency variants associated with severe early-onset obesity
  JOURNAL   Nat Genet 45 (5), 513-517 (2013)
   PUBMED   23563609
REFERENCE   7  (residues 1 to 1943)
  AUTHORS   Kelempisioti,A., Eskola,P.J., Okuloff,A., Karjalainen,U.,
            Takatalo,J., Daavittila,I., Niinimaki,J., Sequeiros,R.B.,
            Tervonen,O., Solovieva,S., Kao,P.Y., Song,Y.Q., Cheung,K.M.,
            Chan,D., Ala-Kokko,L., Jarvelin,M.R., Karppinen,J. and Mannikko,M.
  TITLE     Genetic susceptibility of intervertebral disc degeneration among
            young Finnish adults
  JOURNAL   BMC Med Genet 12, 153 (2011)
   PUBMED   22107760
  REMARK    GeneRIF: SKT is involved in the etiology of intervertebral disc
            degeneration among young adults.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1943)
  AUTHORS   Cirulli,E.T., Kasperaviciute,D., Attix,D.K., Need,A.C., Ge,D.,
            Gibson,G. and Goldstein,D.B.
  TITLE     Common genetic variation and performance on standardized cognitive
            tests
  JOURNAL   Eur J Hum Genet 18 (7), 815-820 (2010)
   PUBMED   20125193
  REMARK    Erratum:[Eur J Hum Genet. 2010 Jul;18(7):820]
REFERENCE   9  (residues 1 to 1943)
  AUTHORS   Eriksson,N., Macpherson,J.M., Tung,J.Y., Hon,L.S., Naughton,B.,
            Saxonov,S., Avey,L., Wojcicki,A., Pe'er,I. and Mountain,J.
  TITLE     Web-based, participant-driven studies yield novel genetic
            associations for common traits
  JOURNAL   PLoS Genet 6 (6), e1000993 (2010)
   PUBMED   20585627
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1943)
  AUTHORS   Karasugi,T., Semba,K., Hirose,Y., Kelempisioti,A., Nakajima,M.,
            Miyake,A., Furuichi,T., Kawaguchi,Y., Mikami,Y., Chiba,K.,
            Kamata,M., Ozaki,K., Takahashi,A., Makela,P., Karppinen,J.,
            Kimura,T., Kubo,T., Toyama,Y., Yamamura,K., Mannikko,M., Mizuta,H.
            and Ikegawa,S.
  TITLE     Association of the tag SNPs in the human SKT gene (KIAA1217) with
            lumbar disc herniation
  JOURNAL   J Bone Miner Res 24 (9), 1537-1543 (2009)
   PUBMED   19338451
  REMARK    GeneRIF: Using tag SNPs, we examined the association in two
            independent Japanese case-control populations and found a
            significant association of lumbar herniation with SKT rs16924573 in
            the allele frequency model
            GeneRIF: Observational study and meta-analysis of gene-disease
            association. (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK091142.1, AL833280.1, AB033043.2, DB164876.1 and AB291616.1.
            
            On Jul 30, 2004 this sequence version replaced NP_062536.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL833280.1, SRR14372079.3488401.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376454.8/ ENSP00000365637.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1943
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.2-p12.1"
     Protein         1..1943
                     /product="sickle tail protein homolog isoform 1"
                     /note="sickle tail protein homolog; likely orthologue of
                     Mus musculus enhancer trap locus 4"
                     /calculated_mol_wt=213986
     Region          1..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Region          112..177
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AQ25; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Region          188..>319
                     /region_name="AIP3"
                     /note="Actin interacting protein 3; pfam03915"
                     /db_xref="CDD:427585"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:A2AQ25; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Region          290..331
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            357
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000250|UniProtKB:A2AQ25; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AQ25; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15951569; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Region          456..476
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AQ25; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            809
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AQ25; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Region          848..874
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Region          1003..1230
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            1027
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AQ25; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            1030
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AQ25; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            1033
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AQ25; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            1044
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Region          1305..1329
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Region          1352..1377
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            1461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AQ25; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Region          1481..1572
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Region          1606..1660
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Region          1677..1943
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Region          <1697..1860
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1739
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            1841
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AQ25; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            1896
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AQ25; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            1899
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AQ25; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     Site            1902
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AQ25; propagated from
                     UniProtKB/Swiss-Prot (Q5T5P2.2)"
     CDS             1..1943
                     /gene="KIAA1217"
                     /gene_synonym="ETL4; SKT"
                     /coded_by="NM_019590.5:57..5888"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31165.1"
                     /db_xref="GeneID:56243"
                     /db_xref="HGNC:HGNC:25428"
                     /db_xref="MIM:617367"
ORIGIN      
        1 meenesqkce pclpysadrr qmqeqgkgnl hvtspedaec rrtkerlsng nsrgsvskss
       61 rniprrhtlg gprsskeilg mqtsemdrkr eaflehlkqk yphhasaimg hqerlrdqtr
      121 spklshspqp pslgdpvehl setsadslea msegdaptpf srgsrtrasl pvvrstnqtk
      181 erslgvlylq ygdetkqlrm pneitsadti ralfvsafpq qltmkmlesp svaiyikdes
      241 rnvyyelndv rniqdrsllk vynkdpahaf nhtpktmngd mrmqrelvya rgdgpgaprp
      301 gstahpphai pnsppstpvp hsmppspsri pyggtrsmvv pgnatiprdr isslpvsrpi
      361 spspsailer rdvkpdedms gkniamyrne gfyadpylyh egrmsiassh gghpldvpdh
      421 iiayhrtair sasaycnpsm qaemhmeqsl yrqksrkypd shlptlgskt ppasphrvsd
      481 lrmidmhahy nahgpphtmq pdraspsrqa fkkepgtlvy iekprsaagl sslvdlgppl
      541 mekqvfayst atipkdretr ermqamekqi asltglvqsa lfkgpitsys kdassekmmk
      601 ttanrnhtds agtphvsggk mlsalestvp psqpppvgts aihmsllemr rsvaelrlql
      661 qqmrqlqlqn qellrammkk aeleisgkvm etmkrledpv qrqrvlveqe rqkylheeek
      721 ivkklceled fvedlkkdst aasrlvtlkd vedgafllrq vgeavatlkg efptlqnkmr
      781 ailrieveav rflkeephkl dsllkrvrsm tdvltmlrrh vtdgllkgtd aaqaaqymam
      841 ekataaevlk sqeeaahtsg qpfhstgapg daksevvpls gmmvrhaqss pvviqpsqhs
      901 vallnpaqnl phvasspavp qeatstlqms qapqspqipm ngsamqslfi eeihsvsakn
      961 ravsiekaek kweekrqnld hyngkefekl leeaqanimk sipnlemppa tgplprgdap
     1021 vdkvelseds pnseqdlekl ggkspppppp pprrsylpgs gltttrsgdv vytgrkenit
     1081 akassedagp spqtratkyp aeepasawtp spppvttsss kdeeeeeeeg dkimaelqaf
     1141 qkcsfmdvns nshaepsrad shvkdtrsga tvppkekknl effhedvrks dveyengpqm
     1201 efqkvttgav rpsdppkwer gmensisdas rtseykteii mkensisnms llrdsrnysq
     1261 etvpkasfgf sgispledei nkgskisglq ysipdtenqt lnygktkeme kqntdkchvs
     1321 shtrltessv hdfktedqev ittdfgqvvl rpkearhanv npnedgesss sspteenaat
     1381 dniafmitet tvqvlssgev hdivsqkged iqtvnidark emtprqegtd nedpvvcldk
     1441 kpviiifdep mdirsaykrl stifeecdee lermmmeeki eeeeeeengd svvqnnntsq
     1501 mshkkvapgn lrtgqqvetk sqphslatet rnpggqemnr telnkfshvd spnseckged
     1561 atddqfespk kkfkfkfpkk qlaaltqair tgtktgkktl qvvvyeeeee dgtlkqhkea
     1621 krfeiarsqp edtpentvrr qeqpsiests pisrtdeirk ntyrtldsle qtikqlenti
     1681 semspkalvd tscssnrdsv assshiaqea sprpllvpde gptaleppts ipsasrkgss
     1741 gapqtsrmpv pmsaknrpgt ldkpgkqskl qdprqyrqan gsakksggdf kptspslpas
     1801 kipalspssg kssslpsssg dssnlpnppa tkpsiasnpl spqtgppahs aslipsvsng
     1861 slkfqsltht gkghhlsfsp qsqngrappp lsfsssppsp assvslnqga kgtrtihtps
     1921 ltsykaqngs sskatpstak ets
//
LOCUS       NP_001138490             210 aa            linear   PRI 07-JAN-2026
DEFINITION  dynein regulatory complex protein 12 [Homo sapiens].
ACCESSION   NP_001138490 XP_002347306
VERSION     NP_001138490.1
DBSOURCE    REFSEQ: accession NM_001145018.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Nai,S., Zheng,Y., Liu,X. and Zhao,H.
  TITLE     The New Nexin-Dynein Regulatory Complex Component CCDC153 Is
            Dispensable for Ciliary Motility and Fertility in Mice
  JOURNAL   Cytoskeleton (Hoboken) (2025) In press
   PUBMED   41059749
  REMARK    Publication Status: Available-Online prior to print
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Ghanaeian,A., Majhi,S., McCafferty,C.L., Nami,B., Black,C.S.,
            Yang,S.K., Legal,T., Papoulas,O., Janowska,M., Valente-Paterno,M.,
            Marcotte,E.M., Wloga,D. and Bui,K.H.
  TITLE     Integrated modeling of the Nexin-dynein regulatory complex reveals
            its regulatory mechanism
  JOURNAL   Nat Commun 14 (1), 5741 (2023)
   PUBMED   37714832
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP002956.1, AA909102.1 and AA782908.1.
            
            On Jul 18, 2009 this sequence version replaced XP_002347306.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14478891.121879.1,
                                           DRR138524.491964.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000503566.7/ ENSP00000423567.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..210
                     /product="dynein regulatory complex protein 12"
                     /note="coiled-coil domain-containing protein 153;
                     coiled-coil domain containing 153"
                     /calculated_mol_wt=23727
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q494R4.2)"
     Region          <28..>194
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          188..210
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q494R4.2)"
     CDS             1..210
                     /gene="DRC12"
                     /gene_synonym="CCDC153"
                     /coded_by="NM_001145018.3:56..688"
                     /db_xref="CCDS:CCDS44753.1"
                     /db_xref="GeneID:283152"
                     /db_xref="HGNC:HGNC:27446"
ORIGIN      
        1 mppknkekgk ksgaqkkkkn wgadvvaesr hrlvvlekel lrdhlalrrd earrakased
       61 qlrqrlqgve aelegarseg kaiyaemsrq chalqedmqt rskqleeevk glrgqleacq
      121 reaaaareea eqalgerdqa laqlrahmad meakyeeilh dsldrllakl raikqqwdga
      181 alrlharhke qqrqfgltpp gslrppapsl
//
LOCUS       NP_001120688             422 aa            linear   PRI 07-JAN-2026
DEFINITION  zinc finger protein Gfi-1 [Homo sapiens].
ACCESSION   NP_001120688
VERSION     NP_001120688.1
DBSOURCE    REFSEQ: accession NM_001127216.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Yao,Q., He,X., Wang,J., Liu,J., Zhang,Q., Zhang,J., Bo,Y. and Lu,L.
  TITLE     DLEU2/EZH2/GFI1 Axis Regulates the Proliferation and Apoptosis of
            Human Bone Marrow Mesenchymal Stem Cells
  JOURNAL   Crit Rev Eukaryot Gene Expr 34 (3), 61-71 (2024)
   PUBMED   38305289
  REMARK    GeneRIF: DLEU2/EZH2/GFI1 Axis Regulates the Proliferation and
            Apoptosis of Human Bone Marrow Mesenchymal Stem Cells.
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Patnana,P.K., Liu,L., Frank,D., Nimmagadda,S.C., Behrens,M.,
            Ahmed,H., Xie,X., Liebmann,M., Wei,L., Gerdemann,A., Thivakaran,A.,
            Humpf,H.U., Klotz,L., Dugas,M., Varghese,J., Trajkovic-Arsic,M.,
            Siveke,J.T., Hanenberg,H., Opalka,B., Duhrsen,U., Reinhardt,H.C.,
            Guenther,U., von Bubnoff,N. and Khandanpour,C.
  TITLE     Dose-dependent expression of GFI1 alters metabolism in the
            haematopoietic progenitors and MLL::AF9-induced leukaemic cells
  JOURNAL   Br J Haematol 202 (5), 1033-1048 (2023)
   PUBMED   37423893
  REMARK    GeneRIF: Dose-dependent expression of GFI1 alters metabolism in the
            haematopoietic progenitors and MLL::AF9-induced leukaemic cells.
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Wang,H., Lin,Z., Nian,Z., Zhang,W., Liu,W., Yan,F., Xiao,Z.,
            Wang,X., Zhang,Z., Ma,Z. and Liu,Z.
  TITLE     Hematopoietic transcription factor GFI1 promotes anchorage
            independence by sustaining ERK activity in cancer cells
  JOURNAL   J Clin Invest 132 (17) (2022)
   PUBMED   35819844
  REMARK    GeneRIF: Hematopoietic transcription factor GFI1 promotes anchorage
            independence by sustaining ERK activity in cancer cells.
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Kang,B., Zhang,T., Huang,K., Wang,T., Li,Y., Mai,Y., Li,J.,
            Dang,S., Zhang,Z., Huang,W., Wang,J., Gao,M., Wang,Y. and Pan,G.
  TITLE     GFI1 regulates chromatin state essential in human
            endothelial-to-haematopoietic transition
  JOURNAL   Cell Prolif 55 (5), e13244 (2022)
   PUBMED   35504619
  REMARK    GeneRIF: GFI1 regulates chromatin state essential in human
            endothelial-to-haematopoietic transition.
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Velinder,M., Singer,J., Bareyan,D., Meznarich,J., Tracy,C.M.,
            Fulcher,J.M., McClellan,D., Lucente,H., Franklin,S., Sharma,S. and
            Engel,M.E.
  TITLE     GFI1 functions in transcriptional control and cell fate
            determination require SNAG domain methylation to recruit LSD1
  JOURNAL   Biochem J 473 (19), 3355-3369 (2016)
   PUBMED   27480105
  REMARK    GeneRIF: combination of the sequence-specific and nonspecific
            DNA-binding modes of SATB1 should be advantageous in a search for
            target loci during transcriptional regulation
            Erratum:[Biochem J. 2017 Aug 11;474(17):2951. doi:
            10.1042/BCJ-2016-0558_COR. PMID: 28801480]
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Botezatu,L., Michel,L.C., Makishima,H., Schroeder,T., Germing,U.,
            Haas,R., van der Reijden,B., Marneth,A.E., Bergevoet,S.M.,
            Jansen,J.H., Przychodzen,B., Wlodarski,M., Niemeyer,C.,
            Platzbecker,U., Ehninger,G., Unnikrishnan,A., Beck,D., Pimanda,J.,
            Hellstrom-Lindberg,E., Malcovati,L., Boultwood,J., Pellagatti,A.,
            Papaemmanuil,E., Le Coutre,P., Kaeda,J., Opalka,B., Moroy,T.,
            Duhrsen,U., Maciejewski,J. and Khandanpour,C.
  TITLE     GFI1(36N) as a therapeutic and prognostic marker for
            myelodysplastic syndrome
  JOURNAL   Exp Hematol 44 (7), 590-595 (2016)
   PUBMED   27080012
  REMARK    GeneRIF: GFI1(36S) homozygous patients exhibited a sustained
            response to treatment with hypomethylating agents, whereas
            GFI1(36N) patients had a poor sustained response to this therapy.
            Because allele status of GFI1(36N) is readily determined using
            basic molecular techniques, we propose inclusion of GFI1(36N)
            status in future prospective studies for MDS patients to better
            predict prognosis and guide therapeutic decisions.
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Person,R.E., Li,F.Q., Duan,Z., Benson,K.F., Wechsler,J.,
            Papadaki,H.A., Eliopoulos,G., Kaufman,C., Bertolone,S.J.,
            Nakamoto,B., Papayannopoulou,T., Grimes,H.L. and Horwitz,M.
  TITLE     Mutations in proto-oncogene GFI1 cause human neutropenia and target
            ELA2
  JOURNAL   Nat Genet 34 (3), 308-312 (2003)
   PUBMED   12778173
  REMARK    GeneRIF: Mutations in proto-oncogene GFI1 cause human neutropenia
            and target ELA2
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Rodel,B., Tavassoli,K., Karsunky,H., Schmidt,T., Bachmann,M.,
            Schaper,F., Heinrich,P., Shuai,K., Elsasser,H.P. and Moroy,T.
  TITLE     The zinc finger protein Gfi-1 can enhance STAT3 signaling by
            interacting with the STAT3 inhibitor PIAS3
  JOURNAL   EMBO J 19 (21), 5845-5855 (2000)
   PUBMED   11060035
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Roberts,T. and Cowell,J.K.
  TITLE     Cloning of the human Gfi-1 gene and its mapping to chromosome
            region 1p22
  JOURNAL   Oncogene 14 (8), 1003-1005 (1997)
   PUBMED   9051000
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Bell,D.W., Taguchi,T., Jenkins,N.A., Gilbert,D.J., Copeland,N.G.,
            Gilks,C.B., Zweidler-McKay,P., Grimes,H.L., Tsichlis,P.N. and
            Testa,J.R.
  TITLE     Chromosomal localization of a gene, GF1, encoding a novel zinc
            finger protein reveals a new syntenic region between man and
            rodents
  JOURNAL   Cytogenet Cell Genet 70 (3-4), 263-267 (1995)
   PUBMED   7789186
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA938896.1, DA927584.1,
            BC032751.1, BQ336135.1, AK123009.1, AC104456.2 and AW086150.1.
            
            Summary: This gene encodes a nuclear zinc finger protein that
            functions as a transcriptional repressor. This protein plays a role
            in diverse developmental contexts, including hematopoiesis and
            oncogenesis. It functions as part of a complex along with other
            cofactors to control histone modifications that lead to silencing
            of the target gene promoters. Mutations in this gene cause
            autosomal dominant severe congenital neutropenia, and also dominant
            nonimmune chronic idiopathic neutropenia of adults, which are
            heterogeneous hematopoietic disorders that cause predispositions to
            leukemias and infections. Multiple alternatively spliced variants,
            encoding the same protein, have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.423255.1,
                                           SRR14038196.3560931.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.1"
     Protein         1..422
                     /product="zinc finger protein Gfi-1"
                     /note="growth factor independence-1; zinc finger protein
                     163; growth factor independent protein 1; growth factor
                     independent 1 transcription repressor"
                     /calculated_mol_wt=45166
     Region          1..109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99684.2)"
     Region          1..20
                     /region_name="SNAG domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99684.2)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07120; propagated from
                     UniProtKB/Swiss-Prot (Q99684.2)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07120; propagated from
                     UniProtKB/Swiss-Prot (Q99684.2)"
     Region          140..257
                     /region_name="Required for interaction with RELA.
                     /evidence=ECO:0000269|PubMed:20547752"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99684.2)"
     Region          <254..416
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          257..278
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          286..306
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          314..334
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(319,321,323,325..326,329..330,333,347,349,353..354,
                     357..358,361,375,377,379,381..382,385..386,389)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          342..362
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          370..390
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          398..417
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..422
                     /gene="GFI1"
                     /gene_synonym="GFI-1; GFI1A; SCN2; ZNF163"
                     /coded_by="NM_001127216.3:186..1454"
                     /db_xref="CCDS:CCDS30773.1"
                     /db_xref="GeneID:2672"
                     /db_xref="HGNC:HGNC:4237"
                     /db_xref="MIM:600871"
ORIGIN      
        1 mprsflvksk kahsyhqprs pgpdyslrle nvpapsrads tsnaggakae prdrlspesq
       61 lteapdrasa spdscegsvc erssefedfw rppspsaspa seksmcpsld eaqpfplpfk
      121 pyswsglags dlrhlvqsyr pcgalergag lglfcepape pghpaalygp kraaggagag
      181 apgscsagag atagpglgly gdfgsaaagl yerptaaagl lyperghglh adkgagvkve
      241 sellctrlll gggsykcikc skvfstphgl evhvrrshsg trpfacemcg ktfghavsle
      301 qhkavhsqer sfdckicgks fkrsstlsth llihsdtrpy pcqycgkrfh qksdmkkhtf
      361 ihtgekphkc qvcgkafsqs snlithsrkh tgfkpfgcdl cgkgfqrkvd lrrhretqhg
      421 lk
//
LOCUS       NP_001269696            1374 aa            linear   PRI 07-JAN-2026
DEFINITION  sickle tail protein homolog isoform 4 [Homo sapiens].
ACCESSION   NP_001269696 XP_005252576
VERSION     NP_001269696.1
DBSOURCE    REFSEQ: accession NM_001282767.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1374)
  AUTHORS   Morellato,A., De Gregorio,M., Angelini,C., Torelli,F., Belmonte,V.,
            Alfieri,A., Bersia,B., Cravero,T., Gai,M., Bianciotto,O.T.,
            Oddone,R., Salemme,V., Natalini,D., Centonze,G., Nigrelli,F.,
            Raspanti,A., Gurgone,A., D'Attanasio,G., Mele,P., Eva,C., Lodi,A.,
            Gavello,D., Carabelli,V., Hidisoglu,E., Chiantia,G., Carbone,E.,
            Becchetti,A., Giustetto,M., Marcantoni,A., Turco,E., Bertocchi,I.
            and Defilippi,P.
  TITLE     The adaptor protein SKT interacts with PSD-95 and SHANK3 and
            affects synaptic functions
  JOURNAL   Cell Rep 44 (9), 116206 (2025)
   PUBMED   40892546
REFERENCE   2  (residues 1 to 1374)
  AUTHORS   Dai,J., Jiang,H., Cheng,Z., Li,Y. and Tang,X.
  TITLE     Genetic polymorphism of KIAA1217 is functionally associated with
            lumbar disc herniation in the Chinese population
  JOURNAL   Neurochirurgie 70 (2), 101538 (2024)
   PUBMED   38311218
  REMARK    GeneRIF: Genetic polymorphism of KIAA1217 is functionally
            associated with lumbar disc herniation in the Chinese population.
REFERENCE   3  (residues 1 to 1374)
  AUTHORS   Wang,Y., Li,N., Zheng,Y., Wang,A., Yu,C., Song,Z., Wang,S., Sun,Y.,
            Zheng,L., Wang,G., Liu,L., Yi,J., Huang,Y., Zhang,M., Bao,Y. and
            Sun,L.
  TITLE     KIAA1217 Promotes Epithelial-Mesenchymal Transition and
            Hepatocellular Carcinoma Metastasis by Interacting with and
            Activating STAT3
  JOURNAL   Int J Mol Sci 23 (1), 104 (2021)
   PUBMED   35008530
  REMARK    GeneRIF: KIAA1217 Promotes Epithelial-Mesenchymal Transition and
            Hepatocellular Carcinoma Metastasis by Interacting with and
            Activating STAT3.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1374)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 1374)
  AUTHORS   Al Dhaheri,N., Wu,N., Zhao,S., Wu,Z., Blank,R.D., Zhang,J.,
            Raggio,C., Halanski,M., Shen,J., Noonan,K., Qiu,G., Nemeth,B.,
            Sund,S., Dunwoodie,S.L., Chapman,G., Glurich,I., Steiner,R.D.,
            Wohler,E., Martin,R., Sobreira,N.L. and Giampietro,P.F.
  TITLE     KIAA1217: A novel candidate gene associated with isolated and
            syndromic vertebral malformations
  JOURNAL   Am J Med Genet A 182 (7), 1664-1672 (2020)
   PUBMED   32369272
  REMARK    GeneRIF: KIAA1217: A novel candidate gene associated with isolated
            and syndromic vertebral malformations.
REFERENCE   6  (residues 1 to 1374)
  AUTHORS   Wheeler,E., Huang,N., Bochukova,E.G., Keogh,J.M., Lindsay,S.,
            Garg,S., Henning,E., Blackburn,H., Loos,R.J., Wareham,N.J.,
            O'Rahilly,S., Hurles,M.E., Barroso,I. and Farooqi,I.S.
  TITLE     Genome-wide SNP and CNV analysis identifies common and
            low-frequency variants associated with severe early-onset obesity
  JOURNAL   Nat Genet 45 (5), 513-517 (2013)
   PUBMED   23563609
REFERENCE   7  (residues 1 to 1374)
  AUTHORS   Kelempisioti,A., Eskola,P.J., Okuloff,A., Karjalainen,U.,
            Takatalo,J., Daavittila,I., Niinimaki,J., Sequeiros,R.B.,
            Tervonen,O., Solovieva,S., Kao,P.Y., Song,Y.Q., Cheung,K.M.,
            Chan,D., Ala-Kokko,L., Jarvelin,M.R., Karppinen,J. and Mannikko,M.
  TITLE     Genetic susceptibility of intervertebral disc degeneration among
            young Finnish adults
  JOURNAL   BMC Med Genet 12, 153 (2011)
   PUBMED   22107760
  REMARK    GeneRIF: SKT is involved in the etiology of intervertebral disc
            degeneration among young adults.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1374)
  AUTHORS   Cirulli,E.T., Kasperaviciute,D., Attix,D.K., Need,A.C., Ge,D.,
            Gibson,G. and Goldstein,D.B.
  TITLE     Common genetic variation and performance on standardized cognitive
            tests
  JOURNAL   Eur J Hum Genet 18 (7), 815-820 (2010)
   PUBMED   20125193
  REMARK    Erratum:[Eur J Hum Genet. 2010 Jul;18(7):820]
REFERENCE   9  (residues 1 to 1374)
  AUTHORS   Eriksson,N., Macpherson,J.M., Tung,J.Y., Hon,L.S., Naughton,B.,
            Saxonov,S., Avey,L., Wojcicki,A., Pe'er,I. and Mountain,J.
  TITLE     Web-based, participant-driven studies yield novel genetic
            associations for common traits
  JOURNAL   PLoS Genet 6 (6), e1000993 (2010)
   PUBMED   20585627
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1374)
  AUTHORS   Karasugi,T., Semba,K., Hirose,Y., Kelempisioti,A., Nakajima,M.,
            Miyake,A., Furuichi,T., Kawaguchi,Y., Mikami,Y., Chiba,K.,
            Kamata,M., Ozaki,K., Takahashi,A., Makela,P., Karppinen,J.,
            Kimura,T., Kubo,T., Toyama,Y., Yamamura,K., Mannikko,M., Mizuta,H.
            and Ikegawa,S.
  TITLE     Association of the tag SNPs in the human SKT gene (KIAA1217) with
            lumbar disc herniation
  JOURNAL   J Bone Miner Res 24 (9), 1537-1543 (2009)
   PUBMED   19338451
  REMARK    GeneRIF: Using tag SNPs, we examined the association in two
            independent Japanese case-control populations and found a
            significant association of lumbar herniation with SKT rs16924573 in
            the allele frequency model
            GeneRIF: Observational study and meta-analysis of gene-disease
            association. (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK091142.1, BC136521.1, AB033043.2, AL833280.1 and AB291616.1.
            
            On Sep 19, 2013 this sequence version replaced XP_005252576.1.
            
            Transcript Variant: This variant (4) lacks two in-frame exons and
            uses an alternate in-frame splice site in the 3' coding region,
            compared to variant 1. This results in a shorter protein (isoform
            4), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC136521.1, SRR14038193.4348742.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1374
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.2-p12.1"
     Protein         1..1374
                     /product="sickle tail protein homolog isoform 4"
                     /note="sickle tail protein homolog; likely orthologue of
                     Mus musculus enhancer trap locus 4"
                     /calculated_mol_wt=150363
     Region          188..>319
                     /region_name="AIP3"
                     /note="Actin interacting protein 3; pfam03915"
                     /db_xref="CDD:427585"
     CDS             1..1374
                     /gene="KIAA1217"
                     /gene_synonym="ETL4; SKT"
                     /coded_by="NM_001282767.2:57..4181"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS60502.1"
                     /db_xref="GeneID:56243"
                     /db_xref="HGNC:HGNC:25428"
                     /db_xref="MIM:617367"
ORIGIN      
        1 meenesqkce pclpysadrr qmqeqgkgnl hvtspedaec rrtkerlsng nsrgsvskss
       61 rniprrhtlg gprsskeilg mqtsemdrkr eaflehlkqk yphhasaimg hqerlrdqtr
      121 spklshspqp pslgdpvehl setsadslea msegdaptpf srgsrtrasl pvvrstnqtk
      181 erslgvlylq ygdetkqlrm pneitsadti ralfvsafpq qltmkmlesp svaiyikdes
      241 rnvyyelndv rniqdrsllk vynkdpahaf nhtpktmngd mrmqrelvya rgdgpgaprp
      301 gstahpphai pnsppstpvp hsmppspsri pyggtrsmvv pgnatiprdr isslpvsrpi
      361 spspsailer rdvkpdedms gkniamyrne gfyadpylyh egrmsiassh gghpldvpdh
      421 iiayhrtair sasaycnpsm qaemhmeqsl yrqksrkypd shlptlgskt ppasphrvsd
      481 lrmidmhahy nahgpphtmq pdraspsrqa fkkepgtlvy iekprsaagl sslvdlgppl
      541 mekqvfayst atipkdrets ekmmkttanr nhtdsagtph vsggkmlsal estvppsqpp
      601 pvgtsaihms llemrrsvae lrlqlqqmrq lqlqnqellr ammkkaelei sgkvmetmkr
      661 ledpvqrqrv lveqerqkyl heeekivkkl celedfvedl kkdstaasrl vtlkdvedga
      721 fllrqvgeav atlkgefptl qnkmrailri eveavrflke ephkldsllk rvrsmtdvlt
      781 mlrrhvtdgl lkgtdaaqaa qymamekata aevlksqeea ahtsgqpfhs tgapgdakse
      841 vvplsgmmvr haqsspvviq psqhsvalln paqnlphvas spavpqeats tlqmsqapqs
      901 pqipmngsam qslfieeihs vsaknravsi ekaekkweek rqnldhyngk efeklleeaq
      961 animksipnl emppatgplp rgdapvdkve lsdspnseqd leklggkspp pppppprrsy
     1021 lpgsgltttr sgdvvytgrk enitakasse dagpspqtra tkypaeepas awtpspppvt
     1081 tssskdeeee eeegdkimae lqafqkcsfm dvnsnshaep sradshvkdt rsgatvppke
     1141 kknleffhed vrksdveyen gpqmefqkgs sgapqtsrmp vpmsaknrpg tldkpgkqsk
     1201 lqdprqyrqa ngsakksggd fkptspslpa skipalspss gkssslpsss gdssnlpnpp
     1261 atkpsiasnp lspqtgppah saslipsvsn gslkfqslth tgkghhlsfs pqsqngrapp
     1321 plsfssspps passvslnqg akgtrtihtp sltsykaqng ssskatpsta kets
//
LOCUS       NP_001120687             422 aa            linear   PRI 07-JAN-2026
DEFINITION  zinc finger protein Gfi-1 [Homo sapiens].
ACCESSION   NP_001120687
VERSION     NP_001120687.1
DBSOURCE    REFSEQ: accession NM_001127215.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Yao,Q., He,X., Wang,J., Liu,J., Zhang,Q., Zhang,J., Bo,Y. and Lu,L.
  TITLE     DLEU2/EZH2/GFI1 Axis Regulates the Proliferation and Apoptosis of
            Human Bone Marrow Mesenchymal Stem Cells
  JOURNAL   Crit Rev Eukaryot Gene Expr 34 (3), 61-71 (2024)
   PUBMED   38305289
  REMARK    GeneRIF: DLEU2/EZH2/GFI1 Axis Regulates the Proliferation and
            Apoptosis of Human Bone Marrow Mesenchymal Stem Cells.
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Patnana,P.K., Liu,L., Frank,D., Nimmagadda,S.C., Behrens,M.,
            Ahmed,H., Xie,X., Liebmann,M., Wei,L., Gerdemann,A., Thivakaran,A.,
            Humpf,H.U., Klotz,L., Dugas,M., Varghese,J., Trajkovic-Arsic,M.,
            Siveke,J.T., Hanenberg,H., Opalka,B., Duhrsen,U., Reinhardt,H.C.,
            Guenther,U., von Bubnoff,N. and Khandanpour,C.
  TITLE     Dose-dependent expression of GFI1 alters metabolism in the
            haematopoietic progenitors and MLL::AF9-induced leukaemic cells
  JOURNAL   Br J Haematol 202 (5), 1033-1048 (2023)
   PUBMED   37423893
  REMARK    GeneRIF: Dose-dependent expression of GFI1 alters metabolism in the
            haematopoietic progenitors and MLL::AF9-induced leukaemic cells.
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Wang,H., Lin,Z., Nian,Z., Zhang,W., Liu,W., Yan,F., Xiao,Z.,
            Wang,X., Zhang,Z., Ma,Z. and Liu,Z.
  TITLE     Hematopoietic transcription factor GFI1 promotes anchorage
            independence by sustaining ERK activity in cancer cells
  JOURNAL   J Clin Invest 132 (17) (2022)
   PUBMED   35819844
  REMARK    GeneRIF: Hematopoietic transcription factor GFI1 promotes anchorage
            independence by sustaining ERK activity in cancer cells.
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Kang,B., Zhang,T., Huang,K., Wang,T., Li,Y., Mai,Y., Li,J.,
            Dang,S., Zhang,Z., Huang,W., Wang,J., Gao,M., Wang,Y. and Pan,G.
  TITLE     GFI1 regulates chromatin state essential in human
            endothelial-to-haematopoietic transition
  JOURNAL   Cell Prolif 55 (5), e13244 (2022)
   PUBMED   35504619
  REMARK    GeneRIF: GFI1 regulates chromatin state essential in human
            endothelial-to-haematopoietic transition.
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Velinder,M., Singer,J., Bareyan,D., Meznarich,J., Tracy,C.M.,
            Fulcher,J.M., McClellan,D., Lucente,H., Franklin,S., Sharma,S. and
            Engel,M.E.
  TITLE     GFI1 functions in transcriptional control and cell fate
            determination require SNAG domain methylation to recruit LSD1
  JOURNAL   Biochem J 473 (19), 3355-3369 (2016)
   PUBMED   27480105
  REMARK    GeneRIF: combination of the sequence-specific and nonspecific
            DNA-binding modes of SATB1 should be advantageous in a search for
            target loci during transcriptional regulation
            Erratum:[Biochem J. 2017 Aug 11;474(17):2951. doi:
            10.1042/BCJ-2016-0558_COR. PMID: 28801480]
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Botezatu,L., Michel,L.C., Makishima,H., Schroeder,T., Germing,U.,
            Haas,R., van der Reijden,B., Marneth,A.E., Bergevoet,S.M.,
            Jansen,J.H., Przychodzen,B., Wlodarski,M., Niemeyer,C.,
            Platzbecker,U., Ehninger,G., Unnikrishnan,A., Beck,D., Pimanda,J.,
            Hellstrom-Lindberg,E., Malcovati,L., Boultwood,J., Pellagatti,A.,
            Papaemmanuil,E., Le Coutre,P., Kaeda,J., Opalka,B., Moroy,T.,
            Duhrsen,U., Maciejewski,J. and Khandanpour,C.
  TITLE     GFI1(36N) as a therapeutic and prognostic marker for
            myelodysplastic syndrome
  JOURNAL   Exp Hematol 44 (7), 590-595 (2016)
   PUBMED   27080012
  REMARK    GeneRIF: GFI1(36S) homozygous patients exhibited a sustained
            response to treatment with hypomethylating agents, whereas
            GFI1(36N) patients had a poor sustained response to this therapy.
            Because allele status of GFI1(36N) is readily determined using
            basic molecular techniques, we propose inclusion of GFI1(36N)
            status in future prospective studies for MDS patients to better
            predict prognosis and guide therapeutic decisions.
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Person,R.E., Li,F.Q., Duan,Z., Benson,K.F., Wechsler,J.,
            Papadaki,H.A., Eliopoulos,G., Kaufman,C., Bertolone,S.J.,
            Nakamoto,B., Papayannopoulou,T., Grimes,H.L. and Horwitz,M.
  TITLE     Mutations in proto-oncogene GFI1 cause human neutropenia and target
            ELA2
  JOURNAL   Nat Genet 34 (3), 308-312 (2003)
   PUBMED   12778173
  REMARK    GeneRIF: Mutations in proto-oncogene GFI1 cause human neutropenia
            and target ELA2
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Rodel,B., Tavassoli,K., Karsunky,H., Schmidt,T., Bachmann,M.,
            Schaper,F., Heinrich,P., Shuai,K., Elsasser,H.P. and Moroy,T.
  TITLE     The zinc finger protein Gfi-1 can enhance STAT3 signaling by
            interacting with the STAT3 inhibitor PIAS3
  JOURNAL   EMBO J 19 (21), 5845-5855 (2000)
   PUBMED   11060035
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Roberts,T. and Cowell,J.K.
  TITLE     Cloning of the human Gfi-1 gene and its mapping to chromosome
            region 1p22
  JOURNAL   Oncogene 14 (8), 1003-1005 (1997)
   PUBMED   9051000
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Bell,D.W., Taguchi,T., Jenkins,N.A., Gilbert,D.J., Copeland,N.G.,
            Gilks,C.B., Zweidler-McKay,P., Grimes,H.L., Tsichlis,P.N. and
            Testa,J.R.
  TITLE     Chromosomal localization of a gene, GF1, encoding a novel zinc
            finger protein reveals a new syntenic region between man and
            rodents
  JOURNAL   Cytogenet Cell Genet 70 (3-4), 263-267 (1995)
   PUBMED   7789186
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK123009.1, AK313876.1,
            DA927584.1, BC032751.1, BQ336135.1, AC104456.2 and AW086150.1.
            
            Summary: This gene encodes a nuclear zinc finger protein that
            functions as a transcriptional repressor. This protein plays a role
            in diverse developmental contexts, including hematopoiesis and
            oncogenesis. It functions as part of a complex along with other
            cofactors to control histone modifications that lead to silencing
            of the target gene promoters. Mutations in this gene cause
            autosomal dominant severe congenital neutropenia, and also dominant
            nonimmune chronic idiopathic neutropenia of adults, which are
            heterogeneous hematopoietic disorders that cause predispositions to
            leukemias and infections. Multiple alternatively spliced variants,
            encoding the same protein, have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK123009.1, SRR14038192.827480.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.1"
     Protein         1..422
                     /product="zinc finger protein Gfi-1"
                     /note="growth factor independence-1; zinc finger protein
                     163; growth factor independent protein 1; growth factor
                     independent 1 transcription repressor"
                     /calculated_mol_wt=45166
     Region          1..109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99684.2)"
     Region          1..20
                     /region_name="SNAG domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99684.2)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07120; propagated from
                     UniProtKB/Swiss-Prot (Q99684.2)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07120; propagated from
                     UniProtKB/Swiss-Prot (Q99684.2)"
     Region          140..257
                     /region_name="Required for interaction with RELA.
                     /evidence=ECO:0000269|PubMed:20547752"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99684.2)"
     Region          <254..416
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          257..278
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          286..306
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          314..334
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(319,321,323,325..326,329..330,333,347,349,353..354,
                     357..358,361,375,377,379,381..382,385..386,389)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          342..362
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          370..390
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          398..417
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..422
                     /gene="GFI1"
                     /gene_synonym="GFI-1; GFI1A; SCN2; ZNF163"
                     /coded_by="NM_001127215.3:180..1448"
                     /db_xref="CCDS:CCDS30773.1"
                     /db_xref="GeneID:2672"
                     /db_xref="HGNC:HGNC:4237"
                     /db_xref="MIM:600871"
ORIGIN      
        1 mprsflvksk kahsyhqprs pgpdyslrle nvpapsrads tsnaggakae prdrlspesq
       61 lteapdrasa spdscegsvc erssefedfw rppspsaspa seksmcpsld eaqpfplpfk
      121 pyswsglags dlrhlvqsyr pcgalergag lglfcepape pghpaalygp kraaggagag
      181 apgscsagag atagpglgly gdfgsaaagl yerptaaagl lyperghglh adkgagvkve
      241 sellctrlll gggsykcikc skvfstphgl evhvrrshsg trpfacemcg ktfghavsle
      301 qhkavhsqer sfdckicgks fkrsstlsth llihsdtrpy pcqycgkrfh qksdmkkhtf
      361 ihtgekphkc qvcgkafsqs snlithsrkh tgfkpfgcdl cgkgfqrkvd lrrhretqhg
      421 lk
//
LOCUS       NP_000498                338 aa            linear   PRI 07-JAN-2026
DEFINITION  fructose-1,6-bisphosphatase 1 [Homo sapiens].
ACCESSION   NP_000498
VERSION     NP_000498.2
DBSOURCE    REFSEQ: accession NM_000507.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Li,M., Wang,Z., Tao,J., Jiang,H., Yang,H., Guo,D., Zhao,H., He,X.,
            Luo,S., Jiang,X., Yuan,L., Xiao,L., He,H., Yu,R., Fang,J.,
            Liang,T., Mao,Z., Xu,D. and Lu,Z.
  TITLE     Fructose-1,6-bisphosphatase 1 dephosphorylates and inhibits TERT
            for tumor suppression
  JOURNAL   Nat Chem Biol 20 (11), 1505-1513 (2024)
   PUBMED   38538923
  REMARK    GeneRIF: Fructose-1,6-bisphosphatase 1 dephosphorylates and
            inhibits TERT for tumor suppression.
            Erratum:[Nat Chem Biol. 2024 Nov;20(11):1547. doi:
            10.1038/s41589-024-01623-3. PMID: 38649455]
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Peng,X., Ma,L., Chen,X., Tang,F. and Zong,X.
  TITLE     Inhibition of FBP1 expression by KMT5A through TWIST1 methylation
            is one of the mechanisms leading to chemoresistance in breast
            cancer
  JOURNAL   Oncol Rep 52 (2) (2024)
   PUBMED   38963044
  REMARK    GeneRIF: Inhibition of FBP1 expression by KMT5A through TWIST1
            methylation is one of the mechanisms leading to chemoresistance in
            breast cancer.
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Zhang,P., Yang,J., Liu,X., Huang,C., Tao,Y., Shen,P., Bai,Z.,
            Xiao,C., Zhou,L., Li,G., Zhang,L., Zhou,W. and Gao,Y.
  TITLE     FBP1 orchestrates keratinocyte proliferation/differentiation and
            suppresses psoriasis through metabolic control of histone
            acetylation
  JOURNAL   Cell Death Dis 15 (6), 392 (2024)
   PUBMED   38834617
  REMARK    GeneRIF: FBP1 orchestrates keratinocyte
            proliferation/differentiation and suppresses psoriasis through
            metabolic control of histone acetylation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 338)
  AUTHORS   He,T., Wang,Y., Lv,W., Wang,Y., Li,X., Zhang,Q., Shen,H.M. and
            Hu,J.
  TITLE     FBP1 inhibits NSCLC stemness by promoting ubiquitination of Notch1
            intracellular domain and accelerating degradation
  JOURNAL   Cell Mol Life Sci 81 (1), 87 (2024)
   PUBMED   38349431
  REMARK    GeneRIF: FBP1 inhibits NSCLC stemness by promoting ubiquitination
            of Notch1 intracellular domain and accelerating degradation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Wang,Z., Wang,X., Liu,L., Guo,X., Zhang,H., Yin,J., Lin,R., Shao,Y.
            and Cai,D.
  TITLE     Fructose-bisphosphatase1 (FBP1) alleviates experimental
            osteoarthritis by regulating Protein crumbs homolog 3 (CRB3)
  JOURNAL   Arthritis Res Ther 25 (1), 235 (2023)
   PUBMED   38049890
  REMARK    GeneRIF: Fructose-bisphosphatase1 (FBP1) alleviates experimental
            osteoarthritis by regulating Protein crumbs homolog 3 (CRB3).
            Erratum:[Arthritis Res Ther. 2023 Dec 28;25(1):250. doi:
            10.1186/s13075-023-03247-9. PMID: 38155346]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 338)
  AUTHORS   el-Maghrabi,M.R., Lange,A.J., Jiang,W., Yamagata,K., Stoffel,M.,
            Takeda,J., Fernald,A.A., Le Beau,M.M., Bell,G.I., Baker,L. et al.
  TITLE     Human fructose-1,6-bisphosphatase gene (FBP1): exon-intron
            organization, localization to chromosome bands 9q22.2-q22.3, and
            mutation screening in subjects with fructose-1,6-bisphosphatase
            deficiency
  JOURNAL   Genomics 27 (3), 520-525 (1995)
   PUBMED   7558035
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Bijarnia-Mahay,S., Bhatia,S. and Arora,V.
  TITLE     Fructose-1,6-Bisphosphatase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31804789
REFERENCE   8  (residues 1 to 338)
  AUTHORS   el-Maghrabi,M.R., Lange,A.J., Kummel,L. and Pilkis,S.J.
  TITLE     The rat fructose-1,6-bisphosphatase gene. Structure and regulation
            of expression
  JOURNAL   J Biol Chem 266 (4), 2115-2120 (1991)
   PUBMED   1846613
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Ke,H.M., Zhang,Y.P. and Lipscomb,W.N.
  TITLE     Crystal structure of fructose-1,6-bisphosphatase complexed with
            fructose 6-phosphate, AMP, and magnesium
  JOURNAL   Proc Natl Acad Sci U S A 87 (14), 5243-5247 (1990)
   PUBMED   2164670
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Solomon,D.H., Raynal,M.C., Tejwani,G.A. and Cayre,Y.E.
  TITLE     Activation of the fructose 1,6-bisphosphatase gene by
            1,25-dihydroxyvitamin D3 during monocytic differentiation
  JOURNAL   Proc Natl Acad Sci U S A 85 (18), 6904-6908 (1988)
   PUBMED   2842796
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA962803.1 and BC012927.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 1, 2001 this sequence version replaced NP_000498.1.
            
            Summary: Fructose-1,6-bisphosphatase 1, a gluconeogenesis
            regulatory enzyme, catalyzes the hydrolysis of fructose
            1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate.
            Fructose-1,6-diphosphatase deficiency is associated with
            hypoglycemia and metabolic acidosis. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012927.1, AK223395.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375326.9/ ENSP00000364475.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.32"
     Protein         1..338
                     /product="fructose-1,6-bisphosphatase 1"
                     /EC_number="3.1.3.11"
                     /note="FBPase 1; D-fructose-1,6-bisphosphate
                     1-phosphohydrolase 1; liver FBPase; growth-inhibiting
                     protein 17"
                     /calculated_mol_wt=36711
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P00637; propagated from
                     UniProtKB/Swiss-Prot (P09467.5)"
     Region          18..332
                     /region_name="FBPase"
                     /note="Fructose-1,6-bisphosphatase, an enzyme that
                     catalyzes the hydrolysis of fructose-1,6-biphosphate into
                     fructose-6-phosphate and is critical in gluconeogenesis
                     pathway. The alignment model also includes chloroplastic
                     FBPases and sedoheptulose-1; cd00354"
                     /db_xref="CDD:238214"
     Site            order(18,21,28,30..32,113..114,141)
                     /site_type="other"
                     /note="AMP binding site [chemical binding]"
                     /db_xref="CDD:238214"
     Site            order(75,98..99,119,121,281)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:238214"
     Site            order(122,124..125,216,244..245,249,265,275)
                     /site_type="active"
                     /db_xref="CDD:238214"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXD6; propagated from
                     UniProtKB/Swiss-Prot (P09467.5)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXD6; propagated from
                     UniProtKB/Swiss-Prot (P09467.5)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P09467.5)"
     CDS             1..338
                     /gene="FBP1"
                     /gene_synonym="FBP"
                     /coded_by="NM_000507.4:209..1225"
                     /db_xref="CCDS:CCDS6712.1"
                     /db_xref="GeneID:2203"
                     /db_xref="HGNC:HGNC:3606"
                     /db_xref="MIM:611570"
ORIGIN      
        1 madqapfdtd vntltrfvme egrkargtge ltqllnslct avkaissavr kagiahlygi
       61 agstnvtgdq vkkldvlsnd lvmnmlkssf atcvlvseed khaiivepek rgkyvvcfdp
      121 ldgssnidcl vsvgtifgiy rkkstdepse kdalqpgrnl vaagyalygs atmlvlamdc
      181 gvncfmldpa igefilvdkd vkikkkgkiy slnegyardf dpavteyiqr kkfppdnsap
      241 ygaryvgsmv advhrtlvyg giflypankk spngklrlly ecnpmayvme kaggmattgk
      301 eavldviptd ihqrapvilg spddvleflk vyekhsaq
//
LOCUS       NP_001269697            1349 aa            linear   PRI 07-JAN-2026
DEFINITION  sickle tail protein homolog isoform 5 [Homo sapiens].
ACCESSION   NP_001269697 XP_005252578
VERSION     NP_001269697.1
DBSOURCE    REFSEQ: accession NM_001282768.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1349)
  AUTHORS   Morellato,A., De Gregorio,M., Angelini,C., Torelli,F., Belmonte,V.,
            Alfieri,A., Bersia,B., Cravero,T., Gai,M., Bianciotto,O.T.,
            Oddone,R., Salemme,V., Natalini,D., Centonze,G., Nigrelli,F.,
            Raspanti,A., Gurgone,A., D'Attanasio,G., Mele,P., Eva,C., Lodi,A.,
            Gavello,D., Carabelli,V., Hidisoglu,E., Chiantia,G., Carbone,E.,
            Becchetti,A., Giustetto,M., Marcantoni,A., Turco,E., Bertocchi,I.
            and Defilippi,P.
  TITLE     The adaptor protein SKT interacts with PSD-95 and SHANK3 and
            affects synaptic functions
  JOURNAL   Cell Rep 44 (9), 116206 (2025)
   PUBMED   40892546
REFERENCE   2  (residues 1 to 1349)
  AUTHORS   Dai,J., Jiang,H., Cheng,Z., Li,Y. and Tang,X.
  TITLE     Genetic polymorphism of KIAA1217 is functionally associated with
            lumbar disc herniation in the Chinese population
  JOURNAL   Neurochirurgie 70 (2), 101538 (2024)
   PUBMED   38311218
  REMARK    GeneRIF: Genetic polymorphism of KIAA1217 is functionally
            associated with lumbar disc herniation in the Chinese population.
REFERENCE   3  (residues 1 to 1349)
  AUTHORS   Wang,Y., Li,N., Zheng,Y., Wang,A., Yu,C., Song,Z., Wang,S., Sun,Y.,
            Zheng,L., Wang,G., Liu,L., Yi,J., Huang,Y., Zhang,M., Bao,Y. and
            Sun,L.
  TITLE     KIAA1217 Promotes Epithelial-Mesenchymal Transition and
            Hepatocellular Carcinoma Metastasis by Interacting with and
            Activating STAT3
  JOURNAL   Int J Mol Sci 23 (1), 104 (2021)
   PUBMED   35008530
  REMARK    GeneRIF: KIAA1217 Promotes Epithelial-Mesenchymal Transition and
            Hepatocellular Carcinoma Metastasis by Interacting with and
            Activating STAT3.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1349)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 1349)
  AUTHORS   Al Dhaheri,N., Wu,N., Zhao,S., Wu,Z., Blank,R.D., Zhang,J.,
            Raggio,C., Halanski,M., Shen,J., Noonan,K., Qiu,G., Nemeth,B.,
            Sund,S., Dunwoodie,S.L., Chapman,G., Glurich,I., Steiner,R.D.,
            Wohler,E., Martin,R., Sobreira,N.L. and Giampietro,P.F.
  TITLE     KIAA1217: A novel candidate gene associated with isolated and
            syndromic vertebral malformations
  JOURNAL   Am J Med Genet A 182 (7), 1664-1672 (2020)
   PUBMED   32369272
  REMARK    GeneRIF: KIAA1217: A novel candidate gene associated with isolated
            and syndromic vertebral malformations.
REFERENCE   6  (residues 1 to 1349)
  AUTHORS   Wheeler,E., Huang,N., Bochukova,E.G., Keogh,J.M., Lindsay,S.,
            Garg,S., Henning,E., Blackburn,H., Loos,R.J., Wareham,N.J.,
            O'Rahilly,S., Hurles,M.E., Barroso,I. and Farooqi,I.S.
  TITLE     Genome-wide SNP and CNV analysis identifies common and
            low-frequency variants associated with severe early-onset obesity
  JOURNAL   Nat Genet 45 (5), 513-517 (2013)
   PUBMED   23563609
REFERENCE   7  (residues 1 to 1349)
  AUTHORS   Kelempisioti,A., Eskola,P.J., Okuloff,A., Karjalainen,U.,
            Takatalo,J., Daavittila,I., Niinimaki,J., Sequeiros,R.B.,
            Tervonen,O., Solovieva,S., Kao,P.Y., Song,Y.Q., Cheung,K.M.,
            Chan,D., Ala-Kokko,L., Jarvelin,M.R., Karppinen,J. and Mannikko,M.
  TITLE     Genetic susceptibility of intervertebral disc degeneration among
            young Finnish adults
  JOURNAL   BMC Med Genet 12, 153 (2011)
   PUBMED   22107760
  REMARK    GeneRIF: SKT is involved in the etiology of intervertebral disc
            degeneration among young adults.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1349)
  AUTHORS   Cirulli,E.T., Kasperaviciute,D., Attix,D.K., Need,A.C., Ge,D.,
            Gibson,G. and Goldstein,D.B.
  TITLE     Common genetic variation and performance on standardized cognitive
            tests
  JOURNAL   Eur J Hum Genet 18 (7), 815-820 (2010)
   PUBMED   20125193
  REMARK    Erratum:[Eur J Hum Genet. 2010 Jul;18(7):820]
REFERENCE   9  (residues 1 to 1349)
  AUTHORS   Eriksson,N., Macpherson,J.M., Tung,J.Y., Hon,L.S., Naughton,B.,
            Saxonov,S., Avey,L., Wojcicki,A., Pe'er,I. and Mountain,J.
  TITLE     Web-based, participant-driven studies yield novel genetic
            associations for common traits
  JOURNAL   PLoS Genet 6 (6), e1000993 (2010)
   PUBMED   20585627
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1349)
  AUTHORS   Karasugi,T., Semba,K., Hirose,Y., Kelempisioti,A., Nakajima,M.,
            Miyake,A., Furuichi,T., Kawaguchi,Y., Mikami,Y., Chiba,K.,
            Kamata,M., Ozaki,K., Takahashi,A., Makela,P., Karppinen,J.,
            Kimura,T., Kubo,T., Toyama,Y., Yamamura,K., Mannikko,M., Mizuta,H.
            and Ikegawa,S.
  TITLE     Association of the tag SNPs in the human SKT gene (KIAA1217) with
            lumbar disc herniation
  JOURNAL   J Bone Miner Res 24 (9), 1537-1543 (2009)
   PUBMED   19338451
  REMARK    GeneRIF: Using tag SNPs, we examined the association in two
            independent Japanese case-control populations and found a
            significant association of lumbar herniation with SKT rs16924573 in
            the allele frequency model
            GeneRIF: Observational study and meta-analysis of gene-disease
            association. (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK091142.1, BC144227.1, AL833280.1 and AB291616.1.
            
            On Sep 19, 2013 this sequence version replaced XP_005252578.1.
            
            Transcript Variant: This variant (5) lacks three in-frame exons in
            the coding region, compared to variant 1. This results in a shorter
            protein (isoform 5), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC144227.1, SRR14038191.1718352.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1349
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.2-p12.1"
     Protein         1..1349
                     /product="sickle tail protein homolog isoform 5"
                     /note="sickle tail protein homolog; likely orthologue of
                     Mus musculus enhancer trap locus 4"
                     /calculated_mol_wt=147294
     Region          188..>319
                     /region_name="AIP3"
                     /note="Actin interacting protein 3; pfam03915"
                     /db_xref="CDD:427585"
     CDS             1..1349
                     /gene="KIAA1217"
                     /gene_synonym="ETL4; SKT"
                     /coded_by="NM_001282768.2:57..4106"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS60501.1"
                     /db_xref="GeneID:56243"
                     /db_xref="HGNC:HGNC:25428"
                     /db_xref="MIM:617367"
ORIGIN      
        1 meenesqkce pclpysadrr qmqeqgkgnl hvtspedaec rrtkerlsng nsrgsvskss
       61 rniprrhtlg gprsskeilg mqtsemdrkr eaflehlkqk yphhasaimg hqerlrdqtr
      121 spklshspqp pslgdpvehl setsadslea msegdaptpf srgsrtrasl pvvrstnqtk
      181 erslgvlylq ygdetkqlrm pneitsadti ralfvsafpq qltmkmlesp svaiyikdes
      241 rnvyyelndv rniqdrsllk vynkdpahaf nhtpktmngd mrmqrelvya rgdgpgaprp
      301 gstahpphai pnsppstpvp hsmppspsri pyggtrsmvv pgnatiprdr isslpvsrpi
      361 spspsailer rdvkpdedms gkniamyrne gfyadpylyh egrmsiassh gghpldvpdh
      421 iiayhrtair sasaycnpsm qaemhmeqsl yrqksrkypd shlptlgskt ppasphrvsd
      481 lrmidmhahy nahgpphtmq pdraspsrqa fkkepgtlvy iekprsaagl sslvdlgppl
      541 mekqvfayst atipkdrets ekmmkttanr nhtdsagtph vsggkmlsal estvppsqpp
      601 pvgtsaihms llemrrsvae lrlqlqqmrq lqlqnqellr ammkkaelei sgkvmetmkr
      661 ledpvqrqrv lveqerqkyl heeekivkkl celedfvedl kkdstaasrl vtlkdvedga
      721 fllrqvgeav atlkgefptl qnkmrailri eveavrflke ephkldsllk rvrsmtdvlt
      781 mlrrhvtdgl lkgtdaaqaa qymamekata aevlksqeea ahtsgqpfhs tgapgdakse
      841 vvplsgmmvr haqsspvviq psqhsvalln paqnlphvas spavpqeats tlqmsqapqs
      901 pqipmngsam qslfieeihs vsaknravsi ekaekkweek rqnldhyngk efeklleeaq
      961 animksipnl emppatgplp rgdapvdkve lsedspnseq dleklggksp ppppppprrs
     1021 ylpgsglttt rsgdvvytgr kenitakass edagpspqtr atkypaeepa sawtpspppv
     1081 ttssskdeee eeeegdkima elqafqkcsf mdvnsnshae psradshvkd trsgatvppk
     1141 ekkgssgapq tsrmpvpmsa knrpgtldkp gkqsklqdpr qyrqangsak ksggdfkpts
     1201 pslpaskipa lspssgksss lpsssgdssn lpnppatkps iasnplspqt gppahsasli
     1261 psvsngslkf qslthtgkgh hlsfspqsqn grappplsfs ssppspassv slnqgakgtr
     1321 tihtpsltsy kaqngssska tpstakets
//
LOCUS       NP_005254                422 aa            linear   PRI 07-JAN-2026
DEFINITION  zinc finger protein Gfi-1 [Homo sapiens].
ACCESSION   NP_005254
VERSION     NP_005254.2
DBSOURCE    REFSEQ: accession NM_005263.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Yao,Q., He,X., Wang,J., Liu,J., Zhang,Q., Zhang,J., Bo,Y. and Lu,L.
  TITLE     DLEU2/EZH2/GFI1 Axis Regulates the Proliferation and Apoptosis of
            Human Bone Marrow Mesenchymal Stem Cells
  JOURNAL   Crit Rev Eukaryot Gene Expr 34 (3), 61-71 (2024)
   PUBMED   38305289
  REMARK    GeneRIF: DLEU2/EZH2/GFI1 Axis Regulates the Proliferation and
            Apoptosis of Human Bone Marrow Mesenchymal Stem Cells.
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Patnana,P.K., Liu,L., Frank,D., Nimmagadda,S.C., Behrens,M.,
            Ahmed,H., Xie,X., Liebmann,M., Wei,L., Gerdemann,A., Thivakaran,A.,
            Humpf,H.U., Klotz,L., Dugas,M., Varghese,J., Trajkovic-Arsic,M.,
            Siveke,J.T., Hanenberg,H., Opalka,B., Duhrsen,U., Reinhardt,H.C.,
            Guenther,U., von Bubnoff,N. and Khandanpour,C.
  TITLE     Dose-dependent expression of GFI1 alters metabolism in the
            haematopoietic progenitors and MLL::AF9-induced leukaemic cells
  JOURNAL   Br J Haematol 202 (5), 1033-1048 (2023)
   PUBMED   37423893
  REMARK    GeneRIF: Dose-dependent expression of GFI1 alters metabolism in the
            haematopoietic progenitors and MLL::AF9-induced leukaemic cells.
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Wang,H., Lin,Z., Nian,Z., Zhang,W., Liu,W., Yan,F., Xiao,Z.,
            Wang,X., Zhang,Z., Ma,Z. and Liu,Z.
  TITLE     Hematopoietic transcription factor GFI1 promotes anchorage
            independence by sustaining ERK activity in cancer cells
  JOURNAL   J Clin Invest 132 (17) (2022)
   PUBMED   35819844
  REMARK    GeneRIF: Hematopoietic transcription factor GFI1 promotes anchorage
            independence by sustaining ERK activity in cancer cells.
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Kang,B., Zhang,T., Huang,K., Wang,T., Li,Y., Mai,Y., Li,J.,
            Dang,S., Zhang,Z., Huang,W., Wang,J., Gao,M., Wang,Y. and Pan,G.
  TITLE     GFI1 regulates chromatin state essential in human
            endothelial-to-haematopoietic transition
  JOURNAL   Cell Prolif 55 (5), e13244 (2022)
   PUBMED   35504619
  REMARK    GeneRIF: GFI1 regulates chromatin state essential in human
            endothelial-to-haematopoietic transition.
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Velinder,M., Singer,J., Bareyan,D., Meznarich,J., Tracy,C.M.,
            Fulcher,J.M., McClellan,D., Lucente,H., Franklin,S., Sharma,S. and
            Engel,M.E.
  TITLE     GFI1 functions in transcriptional control and cell fate
            determination require SNAG domain methylation to recruit LSD1
  JOURNAL   Biochem J 473 (19), 3355-3369 (2016)
   PUBMED   27480105
  REMARK    GeneRIF: combination of the sequence-specific and nonspecific
            DNA-binding modes of SATB1 should be advantageous in a search for
            target loci during transcriptional regulation
            Erratum:[Biochem J. 2017 Aug 11;474(17):2951. doi:
            10.1042/BCJ-2016-0558_COR. PMID: 28801480]
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Botezatu,L., Michel,L.C., Makishima,H., Schroeder,T., Germing,U.,
            Haas,R., van der Reijden,B., Marneth,A.E., Bergevoet,S.M.,
            Jansen,J.H., Przychodzen,B., Wlodarski,M., Niemeyer,C.,
            Platzbecker,U., Ehninger,G., Unnikrishnan,A., Beck,D., Pimanda,J.,
            Hellstrom-Lindberg,E., Malcovati,L., Boultwood,J., Pellagatti,A.,
            Papaemmanuil,E., Le Coutre,P., Kaeda,J., Opalka,B., Moroy,T.,
            Duhrsen,U., Maciejewski,J. and Khandanpour,C.
  TITLE     GFI1(36N) as a therapeutic and prognostic marker for
            myelodysplastic syndrome
  JOURNAL   Exp Hematol 44 (7), 590-595 (2016)
   PUBMED   27080012
  REMARK    GeneRIF: GFI1(36S) homozygous patients exhibited a sustained
            response to treatment with hypomethylating agents, whereas
            GFI1(36N) patients had a poor sustained response to this therapy.
            Because allele status of GFI1(36N) is readily determined using
            basic molecular techniques, we propose inclusion of GFI1(36N)
            status in future prospective studies for MDS patients to better
            predict prognosis and guide therapeutic decisions.
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Person,R.E., Li,F.Q., Duan,Z., Benson,K.F., Wechsler,J.,
            Papadaki,H.A., Eliopoulos,G., Kaufman,C., Bertolone,S.J.,
            Nakamoto,B., Papayannopoulou,T., Grimes,H.L. and Horwitz,M.
  TITLE     Mutations in proto-oncogene GFI1 cause human neutropenia and target
            ELA2
  JOURNAL   Nat Genet 34 (3), 308-312 (2003)
   PUBMED   12778173
  REMARK    GeneRIF: Mutations in proto-oncogene GFI1 cause human neutropenia
            and target ELA2
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Rodel,B., Tavassoli,K., Karsunky,H., Schmidt,T., Bachmann,M.,
            Schaper,F., Heinrich,P., Shuai,K., Elsasser,H.P. and Moroy,T.
  TITLE     The zinc finger protein Gfi-1 can enhance STAT3 signaling by
            interacting with the STAT3 inhibitor PIAS3
  JOURNAL   EMBO J 19 (21), 5845-5855 (2000)
   PUBMED   11060035
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Roberts,T. and Cowell,J.K.
  TITLE     Cloning of the human Gfi-1 gene and its mapping to chromosome
            region 1p22
  JOURNAL   Oncogene 14 (8), 1003-1005 (1997)
   PUBMED   9051000
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Bell,D.W., Taguchi,T., Jenkins,N.A., Gilbert,D.J., Copeland,N.G.,
            Gilks,C.B., Zweidler-McKay,P., Grimes,H.L., Tsichlis,P.N. and
            Testa,J.R.
  TITLE     Chromosomal localization of a gene, GF1, encoding a novel zinc
            finger protein reveals a new syntenic region between man and
            rodents
  JOURNAL   Cytogenet Cell Genet 70 (3-4), 263-267 (1995)
   PUBMED   7789186
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104456.2, BE242676.1,
            DB129173.1, DA927584.1, AK123009.1, BQ336135.1 and AW086150.1.
            
            On Jul 20, 2005 this sequence version replaced NP_005254.1.
            
            Summary: This gene encodes a nuclear zinc finger protein that
            functions as a transcriptional repressor. This protein plays a role
            in diverse developmental contexts, including hematopoiesis and
            oncogenesis. It functions as part of a complex along with other
            cofactors to control histone modifications that lead to silencing
            of the target gene promoters. Mutations in this gene cause
            autosomal dominant severe congenital neutropenia, and also dominant
            nonimmune chronic idiopathic neutropenia of adults, which are
            heterogeneous hematopoietic disorders that cause predispositions to
            leukemias and infections. Multiple alternatively spliced variants,
            encoding the same protein, have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1533516.1,
                                           SRR14038192.2729114.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000294702.6/ ENSP00000294702.5
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.1"
     Protein         1..422
                     /product="zinc finger protein Gfi-1"
                     /note="growth factor independence-1; zinc finger protein
                     163; growth factor independent protein 1; growth factor
                     independent 1 transcription repressor"
                     /calculated_mol_wt=45166
     Region          1..109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99684.2)"
     Region          1..20
                     /region_name="SNAG domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99684.2)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07120; propagated from
                     UniProtKB/Swiss-Prot (Q99684.2)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07120; propagated from
                     UniProtKB/Swiss-Prot (Q99684.2)"
     Region          140..257
                     /region_name="Required for interaction with RELA.
                     /evidence=ECO:0000269|PubMed:20547752"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99684.2)"
     Region          <254..416
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          257..278
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          286..306
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          314..334
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(319,321,323,325..326,329..330,333,347,349,353..354,
                     357..358,361,375,377,379,381..382,385..386,389)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          342..362
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          370..390
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          398..417
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..422
                     /gene="GFI1"
                     /gene_synonym="GFI-1; GFI1A; SCN2; ZNF163"
                     /coded_by="NM_005263.5:300..1568"
                     /db_xref="CCDS:CCDS30773.1"
                     /db_xref="GeneID:2672"
                     /db_xref="HGNC:HGNC:4237"
                     /db_xref="MIM:600871"
ORIGIN      
        1 mprsflvksk kahsyhqprs pgpdyslrle nvpapsrads tsnaggakae prdrlspesq
       61 lteapdrasa spdscegsvc erssefedfw rppspsaspa seksmcpsld eaqpfplpfk
      121 pyswsglags dlrhlvqsyr pcgalergag lglfcepape pghpaalygp kraaggagag
      181 apgscsagag atagpglgly gdfgsaaagl yerptaaagl lyperghglh adkgagvkve
      241 sellctrlll gggsykcikc skvfstphgl evhvrrshsg trpfacemcg ktfghavsle
      301 qhkavhsqer sfdckicgks fkrsstlsth llihsdtrpy pcqycgkrfh qksdmkkhtf
      361 ihtgekphkc qvcgkafsqs snlithsrkh tgfkpfgcdl cgkgfqrkvd lrrhretqhg
      421 lk
//
LOCUS       NP_001269698             932 aa            linear   PRI 07-JAN-2026
DEFINITION  sickle tail protein homolog isoform 6 [Homo sapiens].
ACCESSION   NP_001269698 XP_005252582
VERSION     NP_001269698.1
DBSOURCE    REFSEQ: accession NM_001282769.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 932)
  AUTHORS   Morellato,A., De Gregorio,M., Angelini,C., Torelli,F., Belmonte,V.,
            Alfieri,A., Bersia,B., Cravero,T., Gai,M., Bianciotto,O.T.,
            Oddone,R., Salemme,V., Natalini,D., Centonze,G., Nigrelli,F.,
            Raspanti,A., Gurgone,A., D'Attanasio,G., Mele,P., Eva,C., Lodi,A.,
            Gavello,D., Carabelli,V., Hidisoglu,E., Chiantia,G., Carbone,E.,
            Becchetti,A., Giustetto,M., Marcantoni,A., Turco,E., Bertocchi,I.
            and Defilippi,P.
  TITLE     The adaptor protein SKT interacts with PSD-95 and SHANK3 and
            affects synaptic functions
  JOURNAL   Cell Rep 44 (9), 116206 (2025)
   PUBMED   40892546
REFERENCE   2  (residues 1 to 932)
  AUTHORS   Dai,J., Jiang,H., Cheng,Z., Li,Y. and Tang,X.
  TITLE     Genetic polymorphism of KIAA1217 is functionally associated with
            lumbar disc herniation in the Chinese population
  JOURNAL   Neurochirurgie 70 (2), 101538 (2024)
   PUBMED   38311218
  REMARK    GeneRIF: Genetic polymorphism of KIAA1217 is functionally
            associated with lumbar disc herniation in the Chinese population.
REFERENCE   3  (residues 1 to 932)
  AUTHORS   Wang,Y., Li,N., Zheng,Y., Wang,A., Yu,C., Song,Z., Wang,S., Sun,Y.,
            Zheng,L., Wang,G., Liu,L., Yi,J., Huang,Y., Zhang,M., Bao,Y. and
            Sun,L.
  TITLE     KIAA1217 Promotes Epithelial-Mesenchymal Transition and
            Hepatocellular Carcinoma Metastasis by Interacting with and
            Activating STAT3
  JOURNAL   Int J Mol Sci 23 (1), 104 (2021)
   PUBMED   35008530
  REMARK    GeneRIF: KIAA1217 Promotes Epithelial-Mesenchymal Transition and
            Hepatocellular Carcinoma Metastasis by Interacting with and
            Activating STAT3.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 932)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 932)
  AUTHORS   Al Dhaheri,N., Wu,N., Zhao,S., Wu,Z., Blank,R.D., Zhang,J.,
            Raggio,C., Halanski,M., Shen,J., Noonan,K., Qiu,G., Nemeth,B.,
            Sund,S., Dunwoodie,S.L., Chapman,G., Glurich,I., Steiner,R.D.,
            Wohler,E., Martin,R., Sobreira,N.L. and Giampietro,P.F.
  TITLE     KIAA1217: A novel candidate gene associated with isolated and
            syndromic vertebral malformations
  JOURNAL   Am J Med Genet A 182 (7), 1664-1672 (2020)
   PUBMED   32369272
  REMARK    GeneRIF: KIAA1217: A novel candidate gene associated with isolated
            and syndromic vertebral malformations.
REFERENCE   6  (residues 1 to 932)
  AUTHORS   Wheeler,E., Huang,N., Bochukova,E.G., Keogh,J.M., Lindsay,S.,
            Garg,S., Henning,E., Blackburn,H., Loos,R.J., Wareham,N.J.,
            O'Rahilly,S., Hurles,M.E., Barroso,I. and Farooqi,I.S.
  TITLE     Genome-wide SNP and CNV analysis identifies common and
            low-frequency variants associated with severe early-onset obesity
  JOURNAL   Nat Genet 45 (5), 513-517 (2013)
   PUBMED   23563609
REFERENCE   7  (residues 1 to 932)
  AUTHORS   Kelempisioti,A., Eskola,P.J., Okuloff,A., Karjalainen,U.,
            Takatalo,J., Daavittila,I., Niinimaki,J., Sequeiros,R.B.,
            Tervonen,O., Solovieva,S., Kao,P.Y., Song,Y.Q., Cheung,K.M.,
            Chan,D., Ala-Kokko,L., Jarvelin,M.R., Karppinen,J. and Mannikko,M.
  TITLE     Genetic susceptibility of intervertebral disc degeneration among
            young Finnish adults
  JOURNAL   BMC Med Genet 12, 153 (2011)
   PUBMED   22107760
  REMARK    GeneRIF: SKT is involved in the etiology of intervertebral disc
            degeneration among young adults.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 932)
  AUTHORS   Cirulli,E.T., Kasperaviciute,D., Attix,D.K., Need,A.C., Ge,D.,
            Gibson,G. and Goldstein,D.B.
  TITLE     Common genetic variation and performance on standardized cognitive
            tests
  JOURNAL   Eur J Hum Genet 18 (7), 815-820 (2010)
   PUBMED   20125193
  REMARK    Erratum:[Eur J Hum Genet. 2010 Jul;18(7):820]
REFERENCE   9  (residues 1 to 932)
  AUTHORS   Eriksson,N., Macpherson,J.M., Tung,J.Y., Hon,L.S., Naughton,B.,
            Saxonov,S., Avey,L., Wojcicki,A., Pe'er,I. and Mountain,J.
  TITLE     Web-based, participant-driven studies yield novel genetic
            associations for common traits
  JOURNAL   PLoS Genet 6 (6), e1000993 (2010)
   PUBMED   20585627
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 932)
  AUTHORS   Karasugi,T., Semba,K., Hirose,Y., Kelempisioti,A., Nakajima,M.,
            Miyake,A., Furuichi,T., Kawaguchi,Y., Mikami,Y., Chiba,K.,
            Kamata,M., Ozaki,K., Takahashi,A., Makela,P., Karppinen,J.,
            Kimura,T., Kubo,T., Toyama,Y., Yamamura,K., Mannikko,M., Mizuta,H.
            and Ikegawa,S.
  TITLE     Association of the tag SNPs in the human SKT gene (KIAA1217) with
            lumbar disc herniation
  JOURNAL   J Bone Miner Res 24 (9), 1537-1543 (2009)
   PUBMED   19338451
  REMARK    GeneRIF: Using tag SNPs, we examined the association in two
            independent Japanese case-control populations and found a
            significant association of lumbar herniation with SKT rs16924573 in
            the allele frequency model
            GeneRIF: Observational study and meta-analysis of gene-disease
            association. (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL353583.15, DA408335.1, BC018764.1, BC098577.1 and AL392104.19.
            
            On Sep 19, 2013 this sequence version replaced XP_005252582.1.
            
            Transcript Variant: This variant (6) has multiple differences
            compared to variant 1. These differences result in distinct 5' and
            3' UTRs, in addition to translation initiation at a downstream
            start codon, compared to variant 1. The encoded protein (isoform 6)
            is shorter and has a disctinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC018764.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.2-p12.1"
     Protein         1..932
                     /product="sickle tail protein homolog isoform 6"
                     /note="sickle tail protein homolog; likely orthologue of
                     Mus musculus enhancer trap locus 4"
                     /calculated_mol_wt=102562
     CDS             1..932
                     /gene="KIAA1217"
                     /gene_synonym="ETL4; SKT"
                     /coded_by="NM_001282769.2:352..3150"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS60504.1"
                     /db_xref="GeneID:56243"
                     /db_xref="HGNC:HGNC:25428"
                     /db_xref="MIM:617367"
ORIGIN      
        1 mqrelvyarg dgpgaprpgs tahpphaipn sppstpvphs mppspsripy ggtrsmvvpg
       61 natiprdris slpvsrpisp spsailerrd vkpdedmsgk niamyrnegf yadpylyheg
      121 rmsiasshgg hpldvpdhii ayhrtairsa saycnpsmqa emhmeqslyr qksrkypdsh
      181 lptlgsktpp asphrvsdlr midmhahyna hgpphtmqpd raspsrqafk kepgtlvyie
      241 kprsaaglss lvdlgpplme kqvfaystat ipkdretsek mmkttanrnh tdsagtphvs
      301 ggkmlsales tvppsqpppv gtsaihmsll emrrsvaelr lqlqqmrqlq lqnqellram
      361 mkkaeleisg kvmetmkrle dpvqrqrvlv eqerqkylhe eekivkklce ledfvedlkk
      421 dstaasrlvt lkdvedgafl lrqvgeavat lkgefptlqn kmrailriev eavrflkeep
      481 hkldsllkrv rsmtdvltml rrhvtdgllk gtdaaqaaqy mamekataae vlksqeeaah
      541 tsgqpfhstg apgdaksevv plsgmmvrha qsspvviqps qhsvallnpa qnlphvassp
      601 avpqeatstl qmsqapqspq ipmngsamqs lfieeihsvs aknravsiek aekkweekrq
      661 nldhyngkef eklleeaqan imksipnlem ppatgplprg dapvdkvels edspnseqdl
      721 eklggksppp ppppprrsyl pgsgltttrs gdvvytgrke nitakassed agpspqtrat
      781 kypaeepasa wtpspppvtt ssskdeeeee eegdkimael qafqkcsfmd vnsnshaeps
      841 radshvkdtr sgatvppkek knleffhedv rksdveyeng pqmefqkgss gapqtsrmpv
      901 pmsaknrpgt ldkpgkqskl qdprqyrqvv lp
//
LOCUS       NP_001309265             226 aa            linear   PRI 08-JAN-2026
DEFINITION  RWD domain-containing protein 2A isoform c [Homo sapiens].
ACCESSION   NP_001309265 XP_011533707
VERSION     NP_001309265.1
DBSOURCE    REFSEQ: accession NM_001322336.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC377982.1, CD108545.1, BC104816.1, DA032938.1, CN414510.1,
            AJ420581.1 and AW197622.1.
            
            On Apr 9, 2016 this sequence version replaced XP_011533707.1.
            
            Transcript Variant: This variant (3) contains an additional
            internal exon and thus differs in its 5' UTR and initiates
            translation from an alternate start codon, compared to variant 1.
            The encoded isoform (c) has a distinct N-terminus and is shorter
            than isoform a. Variants 3, 4 and 5 all encode isoform c.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD108545.1, DA149305.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..226
                     /product="RWD domain-containing protein 2A isoform c"
                     /note="RWD domain containing 2; RWD domain-containing
                     protein 2A"
                     /calculated_mol_wt=26201
     Region          <1..69
                     /region_name="RWD_DRWD_ELF-like"
                     /note="RWD, DRWD, and ELF domain family; cl45901"
                     /db_xref="CDD:480265"
     Region          89..218
                     /region_name="RWDD2_C"
                     /note="C-terminal domain of RWD domain-containing protein
                     2; cd24163"
                     /db_xref="CDD:467814"
     CDS             1..226
                     /gene="RWDD2A"
                     /gene_synonym="dJ747H23.2; RWDD2"
                     /coded_by="NM_001322336.2:518..1198"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:112611"
                     /db_xref="HGNC:HGNC:21385"
                     /db_xref="MIM:621461"
ORIGIN      
        1 mvkidlqvtm phsypyvalq lfgrsseldr hqqlllnkgl tsyigtfdpg elcvcaaiqw
       61 lqdnsasyfl nrklvyepst qakpvkntfl rmwiyshhiy qqdlrkkild vgkrldvtgf
      121 cmtgkpgiic vegfkehcee fwhtirypnw khisckhaes vetegngedl rlfhsfeell
      181 leahgdyglr ndyhmnlgqf leflkkhkse hvfqilfgie skssds
//
LOCUS       NP_001309266             226 aa            linear   PRI 08-JAN-2026
DEFINITION  RWD domain-containing protein 2A isoform c [Homo sapiens].
ACCESSION   NP_001309266 XP_011533709
VERSION     NP_001309266.1
DBSOURCE    REFSEQ: accession NM_001322337.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC377982.1, BG676907.1, BC104816.1, DA032938.1, CN414510.1,
            AJ420581.1 and AW197622.1.
            
            On Apr 9, 2016 this sequence version replaced XP_011533709.1.
            
            Transcript Variant: This variant (4) contains an additional
            internal exon and thus differs in its 5' UTR and initiates
            translation from an alternate start codon, compared to variant 1.
            The encoded isoform (c) has a distinct N-terminus and is shorter
            than isoform a. Variants 3, 4 and 5 all encode isoform c.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.132792.1,
                                           SRR1803615.165074.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..226
                     /product="RWD domain-containing protein 2A isoform c"
                     /note="RWD domain containing 2; RWD domain-containing
                     protein 2A"
                     /calculated_mol_wt=26201
     Region          <1..69
                     /region_name="RWD_DRWD_ELF-like"
                     /note="RWD, DRWD, and ELF domain family; cl45901"
                     /db_xref="CDD:480265"
     Region          89..218
                     /region_name="RWDD2_C"
                     /note="C-terminal domain of RWD domain-containing protein
                     2; cd24163"
                     /db_xref="CDD:467814"
     CDS             1..226
                     /gene="RWDD2A"
                     /gene_synonym="dJ747H23.2; RWDD2"
                     /coded_by="NM_001322337.2:503..1183"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="GeneID:112611"
                     /db_xref="HGNC:HGNC:21385"
                     /db_xref="MIM:621461"
ORIGIN      
        1 mvkidlqvtm phsypyvalq lfgrsseldr hqqlllnkgl tsyigtfdpg elcvcaaiqw
       61 lqdnsasyfl nrklvyepst qakpvkntfl rmwiyshhiy qqdlrkkild vgkrldvtgf
      121 cmtgkpgiic vegfkehcee fwhtirypnw khisckhaes vetegngedl rlfhsfeell
      181 leahgdyglr ndyhmnlgqf leflkkhkse hvfqilfgie skssds
//
LOCUS       NP_542397                387 aa            linear   PRI 08-JAN-2026
DEFINITION  WD repeat-containing protein 89 [Homo sapiens].
ACCESSION   NP_542397
VERSION     NP_542397.1
DBSOURCE    REFSEQ: accession NM_080666.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA882425.1 and BC010698.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.171491.1,
                                           SRR1660809.23882.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000620954.2/ ENSP00000480112.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..387
                     /product="WD repeat-containing protein 89"
                     /calculated_mol_wt=43084
     Region          21..65
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          41..349
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(45,49,55..56,68..69,87,91,97..98,112..113,131,140,
                     146..147,169,187,192,198..199,215,234,238,244..245,
                     260..261,292,297,303..304,319..320,338,342,348..349)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          68..107
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          74..112
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          112..156
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          118..160
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          168..208
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          174..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..254
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          219..259
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          267..317
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          319..358
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          324..348
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..387
                     /gene="WDR89"
                     /gene_synonym="C14orf150; MSTP050"
                     /coded_by="NM_080666.4:206..1369"
                     /db_xref="CCDS:CCDS9759.1"
                     /db_xref="GeneID:112840"
                     /db_xref="HGNC:HGNC:20489"
                     /db_xref="MIM:621458"
ORIGIN      
        1 mekieeqfan lhivkcslgt keptyllgid tsktvqagke nlvavlcsng siriydkerl
       61 nvlrefsgyp gllngvrfan scdsvysact dgtvkcwdar varekpvqlf kgypsnifis
      121 fdincndhii cagtekvddd allvfwdarm nsqnlsttkd slgayseths ddvtqvrfhp
      181 snpnmvvsgs sdglvnvfdi nidneedalv ttcnsissvs cigwsgkgyk qiycmthdeg
      241 fywwdlnhld tdepvtrlni qdvrevvnmk edaldyligg lyhektdtlh viggtnkgri
      301 hlmncsmsgl thvtslqggh aatvrsfcwn vqddslltgg edaqlllwkp gaiektftkk
      361 esmkiassvh qrvrvhsnds ykrrkkq
//
LOCUS       NP_001369353             387 aa            linear   PRI 08-JAN-2026
DEFINITION  WD repeat-containing protein 89 [Homo sapiens].
ACCESSION   NP_001369353
VERSION     NP_001369353.1
DBSOURCE    REFSEQ: accession NM_001382424.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136038.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2349342.1,
                                           SRR14038193.2382286.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2153932,
                                           SAMN03267758 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..387
                     /product="WD repeat-containing protein 89"
                     /calculated_mol_wt=43084
     Region          21..65
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          41..349
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(45,49,55..56,68..69,87,91,97..98,112..113,131,140,
                     146..147,169,187,192,198..199,215,234,238,244..245,
                     260..261,292,297,303..304,319..320,338,342,348..349)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          68..107
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          74..112
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          112..156
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          118..160
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          168..208
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          174..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..254
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          219..259
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          267..317
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          319..358
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          324..348
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..387
                     /gene="WDR89"
                     /gene_synonym="C14orf150; MSTP050"
                     /coded_by="NM_001382424.1:336..1499"
                     /db_xref="CCDS:CCDS9759.1"
                     /db_xref="GeneID:112840"
                     /db_xref="HGNC:HGNC:20489"
                     /db_xref="MIM:621458"
ORIGIN      
        1 mekieeqfan lhivkcslgt keptyllgid tsktvqagke nlvavlcsng siriydkerl
       61 nvlrefsgyp gllngvrfan scdsvysact dgtvkcwdar varekpvqlf kgypsnifis
      121 fdincndhii cagtekvddd allvfwdarm nsqnlsttkd slgayseths ddvtqvrfhp
      181 snpnmvvsgs sdglvnvfdi nidneedalv ttcnsissvs cigwsgkgyk qiycmthdeg
      241 fywwdlnhld tdepvtrlni qdvrevvnmk edaldyligg lyhektdtlh viggtnkgri
      301 hlmncsmsgl thvtslqggh aatvrsfcwn vqddslltgg edaqlllwkp gaiektftkk
      361 esmkiassvh qrvrvhsnds ykrrkkq
//
LOCUS       NP_219479                292 aa            linear   PRI 08-JAN-2026
DEFINITION  RWD domain-containing protein 2A isoform a [Homo sapiens].
ACCESSION   NP_219479
VERSION     NP_219479.2
DBSOURCE    REFSEQ: accession NM_033411.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC377982.1, AK313083.1, BC104816.1, DA032938.1, CN414510.1,
            AJ420581.1 and AW197622.1.
            
            On Aug 28, 2007 this sequence version replaced NP_219479.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.398838.1,
                                           SRR1803612.268688.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369724.5/ ENSP00000358739.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..292
                     /product="RWD domain-containing protein 2A isoform a"
                     /note="RWD domain containing 2; RWD domain-containing
                     protein 2A"
                     /calculated_mol_wt=33762
     Region          8..135
                     /region_name="RWD_RWDD2"
                     /note="RWD domain of RWD domain-containing protein 2A
                     (RWDD2A), 2B (RWDD2B) and related proteins; cd23829"
                     /db_xref="CDD:467663"
     Region          155..284
                     /region_name="RWDD2_C"
                     /note="C-terminal domain of RWD domain-containing protein
                     2; cd24163"
                     /db_xref="CDD:467814"
     CDS             1..292
                     /gene="RWDD2A"
                     /gene_synonym="dJ747H23.2; RWDD2"
                     /coded_by="NM_033411.5:228..1106"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4998.1"
                     /db_xref="GeneID:112611"
                     /db_xref="HGNC:HGNC:21385"
                     /db_xref="MIM:621461"
ORIGIN      
        1 msasvkeslq lqllememlf smfpnqgevk ledvnaltni krylegtrea lppkiefvit
       61 lqieepkvki dlqvtmphsy pyvalqlfgr sseldrhqql llnkgltsyi gtfdpgelcv
      121 caaiqwlqdn sasyflnrkl vyepstqakp vkntflrmwi yshhiyqqdl rkkildvgkr
      181 ldvtgfcmtg kpgiicvegf kehceefwht irypnwkhis ckhaesvete gngedlrlfh
      241 sfeellleah gdyglrndyh mnlgqflefl kkhksehvfq ilfgieskss ds
//
LOCUS       NP_001309264             217 aa            linear   PRI 08-JAN-2026
DEFINITION  RWD domain-containing protein 2A isoform b [Homo sapiens].
ACCESSION   NP_001309264 XP_005248705
VERSION     NP_001309264.1
DBSOURCE    REFSEQ: accession NM_001322335.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC377982.1, AK302978.1, BC104816.1, DA032938.1, CN414510.1,
            AJ420581.1 and AW197622.1.
            
            On Apr 9, 2016 this sequence version replaced XP_005248705.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 5' region, and it thus differs in its 5' UTR and initiates
            translation from a downstream in-frame start codon, compared to
            variant 1. The encoded isoform (b) is shorter at the N-terminus,
            compared to isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.57091.1,
                                           SRR1803613.185256.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..217
                     /product="RWD domain-containing protein 2A isoform b"
                     /note="RWD domain containing 2; RWD domain-containing
                     protein 2A"
                     /calculated_mol_wt=25173
     Region          <1..60
                     /region_name="RWD_DRWD_ELF-like"
                     /note="RWD, DRWD, and ELF domain family; cl45901"
                     /db_xref="CDD:480265"
     Region          80..209
                     /region_name="RWDD2_C"
                     /note="C-terminal domain of RWD domain-containing protein
                     2; cd24163"
                     /db_xref="CDD:467814"
     CDS             1..217
                     /gene="RWDD2A"
                     /gene_synonym="dJ747H23.2; RWDD2"
                     /coded_by="NM_001322335.2:234..887"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:112611"
                     /db_xref="HGNC:HGNC:21385"
                     /db_xref="MIM:621461"
ORIGIN      
        1 mphsypyval qlfgrsseld rhqqlllnkg ltsyigtfdp gelcvcaaiq wlqdnsasyf
       61 lnrklvyeps tqakpvkntf lrmwiyshhi yqqdlrkkil dvgkrldvtg fcmtgkpgii
      121 cvegfkehce efwhtirypn wkhisckhae svetegnged lrlfhsfeel lleahgdygl
      181 rndyhmnlgq fleflkkhks ehvfqilfgi eskssds
//
LOCUS       NP_001369357             387 aa            linear   PRI 08-JAN-2026
DEFINITION  WD repeat-containing protein 89 [Homo sapiens].
ACCESSION   NP_001369357
VERSION     NP_001369357.1
DBSOURCE    REFSEQ: accession NM_001382428.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136038.5.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA2153932, SAMN03267758
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..387
                     /product="WD repeat-containing protein 89"
                     /calculated_mol_wt=43084
     Region          21..65
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          41..349
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(45,49,55..56,68..69,87,91,97..98,112..113,131,140,
                     146..147,169,187,192,198..199,215,234,238,244..245,
                     260..261,292,297,303..304,319..320,338,342,348..349)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          68..107
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          74..112
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          112..156
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          118..160
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          168..208
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          174..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..254
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          219..259
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          267..317
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          319..358
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          324..348
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..387
                     /gene="WDR89"
                     /gene_synonym="C14orf150; MSTP050"
                     /coded_by="NM_001382428.1:479..1642"
                     /db_xref="CCDS:CCDS9759.1"
                     /db_xref="GeneID:112840"
                     /db_xref="HGNC:HGNC:20489"
                     /db_xref="MIM:621458"
ORIGIN      
        1 mekieeqfan lhivkcslgt keptyllgid tsktvqagke nlvavlcsng siriydkerl
       61 nvlrefsgyp gllngvrfan scdsvysact dgtvkcwdar varekpvqlf kgypsnifis
      121 fdincndhii cagtekvddd allvfwdarm nsqnlsttkd slgayseths ddvtqvrfhp
      181 snpnmvvsgs sdglvnvfdi nidneedalv ttcnsissvs cigwsgkgyk qiycmthdeg
      241 fywwdlnhld tdepvtrlni qdvrevvnmk edaldyligg lyhektdtlh viggtnkgri
      301 hlmncsmsgl thvtslqggh aatvrsfcwn vqddslltgg edaqlllwkp gaiektftkk
      361 esmkiassvh qrvrvhsnds ykrrkkq
//
LOCUS       NP_001369352             387 aa            linear   PRI 08-JAN-2026
DEFINITION  WD repeat-containing protein 89 [Homo sapiens].
ACCESSION   NP_001369352 XP_011534687
VERSION     NP_001369352.1
DBSOURCE    REFSEQ: accession NM_001382423.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136038.5.
            
            On May 6, 2020 this sequence version replaced XP_011534687.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4559415.1,
                                           SRR18074968.2415272.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..387
                     /product="WD repeat-containing protein 89"
                     /calculated_mol_wt=43084
     Region          21..65
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          41..349
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(45,49,55..56,68..69,87,91,97..98,112..113,131,140,
                     146..147,169,187,192,198..199,215,234,238,244..245,
                     260..261,292,297,303..304,319..320,338,342,348..349)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          68..107
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          74..112
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          112..156
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          118..160
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          168..208
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          174..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..254
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          219..259
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          267..317
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          319..358
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          324..348
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..387
                     /gene="WDR89"
                     /gene_synonym="C14orf150; MSTP050"
                     /coded_by="NM_001382423.1:240..1403"
                     /db_xref="CCDS:CCDS9759.1"
                     /db_xref="GeneID:112840"
                     /db_xref="HGNC:HGNC:20489"
                     /db_xref="MIM:621458"
ORIGIN      
        1 mekieeqfan lhivkcslgt keptyllgid tsktvqagke nlvavlcsng siriydkerl
       61 nvlrefsgyp gllngvrfan scdsvysact dgtvkcwdar varekpvqlf kgypsnifis
      121 fdincndhii cagtekvddd allvfwdarm nsqnlsttkd slgayseths ddvtqvrfhp
      181 snpnmvvsgs sdglvnvfdi nidneedalv ttcnsissvs cigwsgkgyk qiycmthdeg
      241 fywwdlnhld tdepvtrlni qdvrevvnmk edaldyligg lyhektdtlh viggtnkgri
      301 hlmncsmsgl thvtslqggh aatvrsfcwn vqddslltgg edaqlllwkp gaiektftkk
      361 esmkiassvh qrvrvhsnds ykrrkkq
//
LOCUS       NP_001369354             387 aa            linear   PRI 08-JAN-2026
DEFINITION  WD repeat-containing protein 89 [Homo sapiens].
ACCESSION   NP_001369354
VERSION     NP_001369354.1
DBSOURCE    REFSEQ: accession NM_001382425.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136038.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1609322.1,
                                           SRR1803617.17540.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146236, SAMEA2467146
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..387
                     /product="WD repeat-containing protein 89"
                     /calculated_mol_wt=43084
     Region          21..65
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          41..349
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(45,49,55..56,68..69,87,91,97..98,112..113,131,140,
                     146..147,169,187,192,198..199,215,234,238,244..245,
                     260..261,292,297,303..304,319..320,338,342,348..349)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          68..107
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          74..112
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          112..156
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          118..160
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          168..208
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          174..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..254
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          219..259
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          267..317
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          319..358
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          324..348
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..387
                     /gene="WDR89"
                     /gene_synonym="C14orf150; MSTP050"
                     /coded_by="NM_001382425.1:558..1721"
                     /db_xref="CCDS:CCDS9759.1"
                     /db_xref="GeneID:112840"
                     /db_xref="HGNC:HGNC:20489"
                     /db_xref="MIM:621458"
ORIGIN      
        1 mekieeqfan lhivkcslgt keptyllgid tsktvqagke nlvavlcsng siriydkerl
       61 nvlrefsgyp gllngvrfan scdsvysact dgtvkcwdar varekpvqlf kgypsnifis
      121 fdincndhii cagtekvddd allvfwdarm nsqnlsttkd slgayseths ddvtqvrfhp
      181 snpnmvvsgs sdglvnvfdi nidneedalv ttcnsissvs cigwsgkgyk qiycmthdeg
      241 fywwdlnhld tdepvtrlni qdvrevvnmk edaldyligg lyhektdtlh viggtnkgri
      301 hlmncsmsgl thvtslqggh aatvrsfcwn vqddslltgg edaqlllwkp gaiektftkk
      361 esmkiassvh qrvrvhsnds ykrrkkq
//
LOCUS       NP_001373950            1699 aa            linear   PRI 08-JAN-2026
DEFINITION  protein unc-13 homolog A isoform 2 [Homo sapiens].
ACCESSION   NP_001373950
VERSION     NP_001373950.1
DBSOURCE    REFSEQ: accession NM_001387021.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1699)
  AUTHORS   Agra Almeida Quadros,A.R., Li,Z., Wang,X., Ndayambaje,I.S.,
            Aryal,S., Ramesh,N., Nolan,M., Jayakumar,R., Han,Y., Stillman,H.,
            Aguilar,C., Wheeler,H.J., Connors,T., Lopez-Erauskin,J.,
            Baughn,M.W., Melamed,Z., Beccari,M.S., Olmedo Martinez,L.,
            Canori,M., Lee,C.Z., Moran,L., Draper,I., Kopin,A.S., Oakley,D.H.,
            Dickson,D.W., Cleveland,D.W., Hyman,B.T., Das,S., Ertekin-Taner,N.
            and Lagier-Tourenne,C.
  TITLE     Cryptic splicing of stathmin-2 and UNC13A mRNAs is a pathological
            hallmark of TDP-43-associated Alzheimer's disease
  JOURNAL   Acta Neuropathol 147 (1), 9 (2024)
   PUBMED   38175301
  REMARK    GeneRIF: Cryptic splicing of stathmin-2 and UNC13A mRNAs is a
            pathological hallmark of TDP-43-associated Alzheimer's disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1699)
  AUTHORS   Fu,R.H., Chen,H.J. and Hong,S.Y.
  TITLE     Interaction of the C9orf72-Amyotrophic Lateral Sclerosis-Related
            Proline-Arginine Dipeptide Repeat Protein with the RNA-Binding
            Protein NOVA1 Causes Decreased Expression of UNC13A Due to Enhanced
            Inclusion of Cryptic Exons, Which Is Reversed by Betulin Treatment
  JOURNAL   Cells 12 (20), 2476 (2023)
   PUBMED   37887320
  REMARK    GeneRIF: Interaction of the C9orf72-Amyotrophic Lateral
            Sclerosis-Related Proline-Arginine Dipeptide Repeat Protein with
            the RNA-Binding Protein NOVA1 Causes Decreased Expression of UNC13A
            Due to Enhanced Inclusion of Cryptic Exons, Which Is Reversed by
            Betulin Treatment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1699)
  AUTHORS   Brown,A.L., Wilkins,O.G., Keuss,M.J., Kargbo-Hill,S.E.,
            Zanovello,M., Lee,W.C., Bampton,A., Lee,F.C.Y., Masino,L., Qi,Y.A.,
            Bryce-Smith,S., Gatt,A., Hallegger,M., Fagegaltier,D., Phatnani,H.,
            Newcombe,J., Gustavsson,E.K., Seddighi,S., Reyes,J.F., Coon,S.L.,
            Ramos,D., Schiavo,G., Fisher,E.M.C., Raj,T., Secrier,M.,
            Lashley,T., Ule,J., Buratti,E., Humphrey,J., Ward,M.E. and
            Fratta,P.
  CONSRTM   NYGC ALS Consortium
  TITLE     TDP-43 loss and ALS-risk SNPs drive mis-splicing and depletion of
            UNC13A
  JOURNAL   Nature 603 (7899), 131-137 (2022)
   PUBMED   35197628
  REMARK    GeneRIF: TDP-43 loss and ALS-risk SNPs drive mis-splicing and
            depletion of UNC13A.
            Erratum:[Nature. 2024 Jul;631(8020):E7. doi:
            10.1038/s41586-024-07577-9. PMID: 38890465]
REFERENCE   4  (residues 1 to 1699)
  AUTHORS   Ma,X.R., Prudencio,M., Koike,Y., Vatsavayai,S.C., Kim,G.,
            Harbinski,F., Briner,A., Rodriguez,C.M., Guo,C., Akiyama,T.,
            Schmidt,H.B., Cummings,B.B., Wyatt,D.W., Kurylo,K., Miller,G.,
            Mekhoubad,S., Sallee,N., Mekonnen,G., Ganser,L., Rubien,J.D.,
            Jansen-West,K., Cook,C.N., Pickles,S., Oskarsson,B.,
            Graff-Radford,N.R., Boeve,B.F., Knopman,D.S., Petersen,R.C.,
            Dickson,D.W., Shorter,J., Myong,S., Green,E.M., Seeley,W.W.,
            Petrucelli,L. and Gitler,A.D.
  TITLE     TDP-43 represses cryptic exon inclusion in the FTD-ALS gene UNC13A
  JOURNAL   Nature 603 (7899), 124-130 (2022)
   PUBMED   35197626
  REMARK    GeneRIF: TDP-43 represses cryptic exon inclusion in the FTD-ALS
            gene UNC13A.
REFERENCE   5  (residues 1 to 1699)
  AUTHORS   You,Y., Katti,S., Yu,B., Igumenova,T.I. and Das,J.
  TITLE     Probing the Diacylglycerol Binding Site of Presynaptic Munc13-1
  JOURNAL   Biochemistry 60 (16), 1286-1298 (2021)
   PUBMED   33818064
  REMARK    GeneRIF: Probing the Diacylglycerol Binding Site of Presynaptic
            Munc13-1.
REFERENCE   6  (residues 1 to 1699)
  AUTHORS   Diekstra,F.P., van Vught,P.W., van Rheenen,W., Koppers,M.,
            Pasterkamp,R.J., van Es,M.A., Schelhaas,H.J., de Visser,M.,
            Robberecht,W., Van Damme,P., Andersen,P.M., van den Berg,L.H. and
            Veldink,J.H.
  TITLE     UNC13A is a modifier of survival in amyotrophic lateral sclerosis
  JOURNAL   Neurobiol Aging 33 (3), 630 (2012)
   PUBMED   22118904
  REMARK    GeneRIF: Our results further corroborate the role of UNC13A in
            amyotrophic lateral sclerosis pathogenesis.
REFERENCE   7  (residues 1 to 1699)
  AUTHORS   van Es,M.A., Veldink,J.H., Saris,C.G., Blauw,H.M., van Vught,P.W.,
            Birve,A., Lemmens,R., Schelhaas,H.J., Groen,E.J., Huisman,M.H., van
            der Kooi,A.J., de Visser,M., Dahlberg,C., Estrada,K.,
            Rivadeneira,F., Hofman,A., Zwarts,M.J., van Doormaal,P.T.,
            Rujescu,D., Strengman,E., Giegling,I., Muglia,P., Tomik,B.,
            Slowik,A., Uitterlinden,A.G., Hendrich,C., Waibel,S., Meyer,T.,
            Ludolph,A.C., Glass,J.D., Purcell,S., Cichon,S., Nothen,M.M.,
            Wichmann,H.E., Schreiber,S., Vermeulen,S.H., Kiemeney,L.A.,
            Wokke,J.H., Cronin,S., McLaughlin,R.L., Hardiman,O., Fumoto,K.,
            Pasterkamp,R.J., Meininger,V., Melki,J., Leigh,P.N., Shaw,C.E.,
            Landers,J.E., Al-Chalabi,A., Brown,R.H. Jr., Robberecht,W.,
            Andersen,P.M., Ophoff,R.A. and van den Berg,L.H.
  TITLE     Genome-wide association study identifies 19p13.3 (UNC13A) and
            9p21.2 as susceptibility loci for sporadic amyotrophic lateral
            sclerosis
  JOURNAL   Nat Genet 41 (10), 1083-1087 (2009)
   PUBMED   19734901
  REMARK    GeneRIF: rs12608932 Single Nucleotide Polymorphism is located at
            19p13.3 and maps to a haplotype block within the boundaries of
            UNC13A, which regulates the release of neurotransmitters such as
            glutamate at neuromuscular synapses.
            GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 1699)
  AUTHORS   Rossner,S., Fuchsbrunner,K., Lange-Dohna,C., Hartlage-Rubsamen,M.,
            Bigl,V., Betz,A., Reim,K. and Brose,N.
  TITLE     Munc13-1-mediated vesicle priming contributes to secretory amyloid
            precursor protein processing
  JOURNAL   J Biol Chem 279 (27), 27841-27844 (2004)
   PUBMED   15123597
REFERENCE   9  (residues 1 to 1699)
  AUTHORS   Sudhof,T.C.
  TITLE     The synaptic vesicle cycle
  JOURNAL   Annu Rev Neurosci 27, 509-547 (2004)
   PUBMED   15217342
  REMARK    Review article
REFERENCE   10 (residues 1 to 1699)
  AUTHORS   Sheu,L., Pasyk,E.A., Ji,J., Huang,X., Gao,X., Varoqueaux,F.,
            Brose,N. and Gaisano,H.Y.
  TITLE     Regulation of insulin exocytosis by Munc13-1
  JOURNAL   J Biol Chem 278 (30), 27556-27563 (2003)
   PUBMED   12871971
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008761.8.
            
            Summary: This gene encodes a member of the UNC13 family. UNC13
            proteins bind to phorbol esters and diacylglycerol and play
            important roles in neurotransmitter release at synapses. Single
            nucleotide polymorphisms in this gene may be associated with
            sporadic amyotrophic lateral sclerosis. [provided by RefSeq, Feb
            2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1699
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..1699
                     /product="protein unc-13 homolog A isoform 2"
                     /note="protein unc-13 homolog A"
                     /calculated_mol_wt=192437
     Region          1..127
                     /region_name="C2A_Munc13"
                     /note="C2 domain first repeat in Munc13 (mammalian
                     uncoordinated) proteins; cd08394"
                     /db_xref="CDD:176040"
     Site            order(23,25,27,31..34,63,65,71..74)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:176040"
     Region          186..445
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62768; propagated from
                     UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62768; propagated from
                     UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62768; propagated from
                     UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62768; propagated from
                     UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Region          533..614
                     /region_name="C1_Munc13-2-like"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in Munc13-2, Munc13-3 and similar proteins; cd20859"
                     /db_xref="CDD:410409"
     Site            order(557..563,571..575,578)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410409"
     Region          674..800
                     /region_name="C2B_Munc13"
                     /note="C2 domain second repeat in Munc13 (mammalian
                     uncoordinated) proteins; cd04027"
                     /db_xref="CDD:175993"
     Site            order(690,696,742,744,761)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175993"
     Region          992..1508
                     /region_name="MUN"
                     /note="MUN domain; pfam06292"
                     /db_xref="CDD:461870"
     Region          1542..1661
                     /region_name="C2C_Munc13"
                     /note="C2 domain third repeat in Munc13 (mammalian
                     uncoordinated) proteins; cd08395"
                     /db_xref="CDD:176041"
     CDS             1..1699
                     /gene="UNC13A"
                     /gene_synonym="IDDSF; Munc13-1; NEDHES; NEDSMS"
                     /coded_by="NM_001387021.1:156..5255"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:23025"
                     /db_xref="HGNC:HGNC:23150"
                     /db_xref="MIM:609894"
ORIGIN      
        1 msllcvgvkk akfdgaqekf ntyvtlkvqn vksttiavrg sqpsweqdfm feinrldlgl
       61 tvevwnkgli wdtmvgtvwi plrtirqsne egpgewltld sqvimadsei cgtkdptfhr
      121 illdtrfelp ldipeeeary wakkleqlna mrdqdeysfq deqdkplpvp snqccnwnyf
      181 gwgeqhnddp dsavddrdsd yrsetsnsip ppyyttsqpn asvhqysvrp pplgsresys
      241 dsmhsyeefs epqalsptgs sryassgels qgssqlsedf dpdehslqgs dmederdrds
      301 yhschssvsy hkdsprwdqd eeeleedled fleeeelped eeeleeeeee vpddlgsyaq
      361 redvavaepk dfkrislppa apgkedkapv apteapdmak vapkpatpdk vpaaeqipea
      421 eppkdeesfr predeegqeg qdsmsrakan wlrafnkvrm qlqeargege mskslwfkgg
      481 pgggliiids mpdirkrkpi plvsdlslvq srkagitsal asstlnneel knhvykktlq
      541 aliypisctt phnfevwtat tptycyeceg llwgiarqgm rctecgvkch ekcqdllnad
      601 clqraaekss khgaedrtqn iimvlkdrmk irernkpeif eliqeifavt ktahtqqmka
      661 vkqsvldgts kwsakisitv vcaqglqakd ktgssdpyvt vqvgktkkrt ktiygnlnpv
      721 weenfhfech nssdrikvrv wdedddiksr vkqrfkresd dflgqtiiev rtlsgemdvw
      781 ynldkrtdks avsgairlhi sveikgeekv apyhvqytcl henlfhfvtd vqnngvvkip
      841 dakgddawkv yydetaqeiv defamrygve siyqamthfa clsskymcpg vpavmstlla
      901 ninayyahtt astnvsasdr faasnfgker fvklldqlhn slridlsmyr nnfpassper
      961 lqdlkstvdl ltsitffrmk vqelqsppra sqvvkdcvka clnstyeyif nnchelysre
     1021 yqtdpakkge vlpeeqgpsi knldfwskli tlivsiieed knsytpclnq fpqelnvgki
     1081 saevmwnlfa qdmkyameeh dkhrlcksad ymnlhfkvkw lyneyvtelp afkdrvpeyp
     1141 awfepfviqw ldeneevsrd flhgalerdk kdgfqqtseh alfscsvvdv fsqlnqsfei
     1201 ikklecpdpq ivghymrrfa ktisnvllqy adiiskdfas ycskekekvp cilmnntqql
     1261 rvqlekmfea mggkeldaea sdilkelqvk lnnvldelsr vfatsfqphi eecvkqmgdi
     1321 lsqvkgtgnv pasacssvaq dadnvlqpim dlldsnltlf akicektvlk rvlkelwklv
     1381 mntmektivl ppltdqtgnl lrkhgkglek grvklpshsd gtqmifnaak elgqlsklkd
     1441 hmvreeaksl tpkqcavvel aldtikqyfh aggvglkktf lekspdlqsl ryalslytqa
     1501 tdlliktfvq tqsaqglgve dpvgevsvhv elfthpgtge hkvtvkvvaa ndlkwqtsgi
     1561 frpfievnii gpqlsdkkrk fatksknnsw apkynesfqf tlsadagpec yelqvcvkdy
     1621 cfaredrtvg lavlqlrela qrgsaacwlp lgrrihmddt gltvlrilsq rsndevakef
     1681 vklksdtrsa eeggaapap
//
LOCUS       NP_001309268             226 aa            linear   PRI 08-JAN-2026
DEFINITION  RWD domain-containing protein 2A isoform c [Homo sapiens].
ACCESSION   NP_001309268 XP_011533710 XP_011533711
VERSION     NP_001309268.1
DBSOURCE    REFSEQ: accession NM_001322339.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC377982.1, CD108545.1, BC104816.1, DA032938.1, CN414510.1,
            AJ420581.1 and AW197622.1.
            
            On or before Apr 9, 2016 this sequence version replaced
            XP_011533710.1, XP_011533711.1.
            
            Transcript Variant: This variant (5) uses an alternate splice site
            in the 5' region and contains an additional internal exon, and it
            thus differs in its 5' UTR and initiates translation from an
            alternate start codon, compared to variant 1. The encoded isoform
            (c) has a distinct N-terminus and is shorter than isoform a.
            Variants 3, 4 and 5 all encode isoform c.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2144120 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..226
                     /product="RWD domain-containing protein 2A isoform c"
                     /note="RWD domain containing 2; RWD domain-containing
                     protein 2A"
                     /calculated_mol_wt=26201
     Region          <1..69
                     /region_name="RWD_DRWD_ELF-like"
                     /note="RWD, DRWD, and ELF domain family; cl45901"
                     /db_xref="CDD:480265"
     Region          89..218
                     /region_name="RWDD2_C"
                     /note="C-terminal domain of RWD domain-containing protein
                     2; cd24163"
                     /db_xref="CDD:467814"
     CDS             1..226
                     /gene="RWDD2A"
                     /gene_synonym="dJ747H23.2; RWDD2"
                     /coded_by="NM_001322339.2:299..979"
                     /note="isoform c is encoded by transcript variant 5"
                     /db_xref="GeneID:112611"
                     /db_xref="HGNC:HGNC:21385"
                     /db_xref="MIM:621461"
ORIGIN      
        1 mvkidlqvtm phsypyvalq lfgrsseldr hqqlllnkgl tsyigtfdpg elcvcaaiqw
       61 lqdnsasyfl nrklvyepst qakpvkntfl rmwiyshhiy qqdlrkkild vgkrldvtgf
      121 cmtgkpgiic vegfkehcee fwhtirypnw khisckhaes vetegngedl rlfhsfeell
      181 leahgdyglr ndyhmnlgqf leflkkhkse hvfqilfgie skssds
//
LOCUS       NP_001373952            1676 aa            linear   PRI 08-JAN-2026
DEFINITION  protein unc-13 homolog A isoform 4 [Homo sapiens].
ACCESSION   NP_001373952
VERSION     NP_001373952.1
DBSOURCE    REFSEQ: accession NM_001387023.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1676)
  AUTHORS   Agra Almeida Quadros,A.R., Li,Z., Wang,X., Ndayambaje,I.S.,
            Aryal,S., Ramesh,N., Nolan,M., Jayakumar,R., Han,Y., Stillman,H.,
            Aguilar,C., Wheeler,H.J., Connors,T., Lopez-Erauskin,J.,
            Baughn,M.W., Melamed,Z., Beccari,M.S., Olmedo Martinez,L.,
            Canori,M., Lee,C.Z., Moran,L., Draper,I., Kopin,A.S., Oakley,D.H.,
            Dickson,D.W., Cleveland,D.W., Hyman,B.T., Das,S., Ertekin-Taner,N.
            and Lagier-Tourenne,C.
  TITLE     Cryptic splicing of stathmin-2 and UNC13A mRNAs is a pathological
            hallmark of TDP-43-associated Alzheimer's disease
  JOURNAL   Acta Neuropathol 147 (1), 9 (2024)
   PUBMED   38175301
  REMARK    GeneRIF: Cryptic splicing of stathmin-2 and UNC13A mRNAs is a
            pathological hallmark of TDP-43-associated Alzheimer's disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1676)
  AUTHORS   Fu,R.H., Chen,H.J. and Hong,S.Y.
  TITLE     Interaction of the C9orf72-Amyotrophic Lateral Sclerosis-Related
            Proline-Arginine Dipeptide Repeat Protein with the RNA-Binding
            Protein NOVA1 Causes Decreased Expression of UNC13A Due to Enhanced
            Inclusion of Cryptic Exons, Which Is Reversed by Betulin Treatment
  JOURNAL   Cells 12 (20), 2476 (2023)
   PUBMED   37887320
  REMARK    GeneRIF: Interaction of the C9orf72-Amyotrophic Lateral
            Sclerosis-Related Proline-Arginine Dipeptide Repeat Protein with
            the RNA-Binding Protein NOVA1 Causes Decreased Expression of UNC13A
            Due to Enhanced Inclusion of Cryptic Exons, Which Is Reversed by
            Betulin Treatment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1676)
  AUTHORS   Brown,A.L., Wilkins,O.G., Keuss,M.J., Kargbo-Hill,S.E.,
            Zanovello,M., Lee,W.C., Bampton,A., Lee,F.C.Y., Masino,L., Qi,Y.A.,
            Bryce-Smith,S., Gatt,A., Hallegger,M., Fagegaltier,D., Phatnani,H.,
            Newcombe,J., Gustavsson,E.K., Seddighi,S., Reyes,J.F., Coon,S.L.,
            Ramos,D., Schiavo,G., Fisher,E.M.C., Raj,T., Secrier,M.,
            Lashley,T., Ule,J., Buratti,E., Humphrey,J., Ward,M.E. and
            Fratta,P.
  CONSRTM   NYGC ALS Consortium
  TITLE     TDP-43 loss and ALS-risk SNPs drive mis-splicing and depletion of
            UNC13A
  JOURNAL   Nature 603 (7899), 131-137 (2022)
   PUBMED   35197628
  REMARK    GeneRIF: TDP-43 loss and ALS-risk SNPs drive mis-splicing and
            depletion of UNC13A.
            Erratum:[Nature. 2024 Jul;631(8020):E7. doi:
            10.1038/s41586-024-07577-9. PMID: 38890465]
REFERENCE   4  (residues 1 to 1676)
  AUTHORS   Ma,X.R., Prudencio,M., Koike,Y., Vatsavayai,S.C., Kim,G.,
            Harbinski,F., Briner,A., Rodriguez,C.M., Guo,C., Akiyama,T.,
            Schmidt,H.B., Cummings,B.B., Wyatt,D.W., Kurylo,K., Miller,G.,
            Mekhoubad,S., Sallee,N., Mekonnen,G., Ganser,L., Rubien,J.D.,
            Jansen-West,K., Cook,C.N., Pickles,S., Oskarsson,B.,
            Graff-Radford,N.R., Boeve,B.F., Knopman,D.S., Petersen,R.C.,
            Dickson,D.W., Shorter,J., Myong,S., Green,E.M., Seeley,W.W.,
            Petrucelli,L. and Gitler,A.D.
  TITLE     TDP-43 represses cryptic exon inclusion in the FTD-ALS gene UNC13A
  JOURNAL   Nature 603 (7899), 124-130 (2022)
   PUBMED   35197626
  REMARK    GeneRIF: TDP-43 represses cryptic exon inclusion in the FTD-ALS
            gene UNC13A.
REFERENCE   5  (residues 1 to 1676)
  AUTHORS   You,Y., Katti,S., Yu,B., Igumenova,T.I. and Das,J.
  TITLE     Probing the Diacylglycerol Binding Site of Presynaptic Munc13-1
  JOURNAL   Biochemistry 60 (16), 1286-1298 (2021)
   PUBMED   33818064
  REMARK    GeneRIF: Probing the Diacylglycerol Binding Site of Presynaptic
            Munc13-1.
REFERENCE   6  (residues 1 to 1676)
  AUTHORS   Diekstra,F.P., van Vught,P.W., van Rheenen,W., Koppers,M.,
            Pasterkamp,R.J., van Es,M.A., Schelhaas,H.J., de Visser,M.,
            Robberecht,W., Van Damme,P., Andersen,P.M., van den Berg,L.H. and
            Veldink,J.H.
  TITLE     UNC13A is a modifier of survival in amyotrophic lateral sclerosis
  JOURNAL   Neurobiol Aging 33 (3), 630 (2012)
   PUBMED   22118904
  REMARK    GeneRIF: Our results further corroborate the role of UNC13A in
            amyotrophic lateral sclerosis pathogenesis.
REFERENCE   7  (residues 1 to 1676)
  AUTHORS   van Es,M.A., Veldink,J.H., Saris,C.G., Blauw,H.M., van Vught,P.W.,
            Birve,A., Lemmens,R., Schelhaas,H.J., Groen,E.J., Huisman,M.H., van
            der Kooi,A.J., de Visser,M., Dahlberg,C., Estrada,K.,
            Rivadeneira,F., Hofman,A., Zwarts,M.J., van Doormaal,P.T.,
            Rujescu,D., Strengman,E., Giegling,I., Muglia,P., Tomik,B.,
            Slowik,A., Uitterlinden,A.G., Hendrich,C., Waibel,S., Meyer,T.,
            Ludolph,A.C., Glass,J.D., Purcell,S., Cichon,S., Nothen,M.M.,
            Wichmann,H.E., Schreiber,S., Vermeulen,S.H., Kiemeney,L.A.,
            Wokke,J.H., Cronin,S., McLaughlin,R.L., Hardiman,O., Fumoto,K.,
            Pasterkamp,R.J., Meininger,V., Melki,J., Leigh,P.N., Shaw,C.E.,
            Landers,J.E., Al-Chalabi,A., Brown,R.H. Jr., Robberecht,W.,
            Andersen,P.M., Ophoff,R.A. and van den Berg,L.H.
  TITLE     Genome-wide association study identifies 19p13.3 (UNC13A) and
            9p21.2 as susceptibility loci for sporadic amyotrophic lateral
            sclerosis
  JOURNAL   Nat Genet 41 (10), 1083-1087 (2009)
   PUBMED   19734901
  REMARK    GeneRIF: rs12608932 Single Nucleotide Polymorphism is located at
            19p13.3 and maps to a haplotype block within the boundaries of
            UNC13A, which regulates the release of neurotransmitters such as
            glutamate at neuromuscular synapses.
            GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 1676)
  AUTHORS   Rossner,S., Fuchsbrunner,K., Lange-Dohna,C., Hartlage-Rubsamen,M.,
            Bigl,V., Betz,A., Reim,K. and Brose,N.
  TITLE     Munc13-1-mediated vesicle priming contributes to secretory amyloid
            precursor protein processing
  JOURNAL   J Biol Chem 279 (27), 27841-27844 (2004)
   PUBMED   15123597
REFERENCE   9  (residues 1 to 1676)
  AUTHORS   Sudhof,T.C.
  TITLE     The synaptic vesicle cycle
  JOURNAL   Annu Rev Neurosci 27, 509-547 (2004)
   PUBMED   15217342
  REMARK    Review article
REFERENCE   10 (residues 1 to 1676)
  AUTHORS   Sheu,L., Pasyk,E.A., Ji,J., Huang,X., Gao,X., Varoqueaux,F.,
            Brose,N. and Gaisano,H.Y.
  TITLE     Regulation of insulin exocytosis by Munc13-1
  JOURNAL   J Biol Chem 278 (30), 27556-27563 (2003)
   PUBMED   12871971
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008761.8.
            
            Summary: This gene encodes a member of the UNC13 family. UNC13
            proteins bind to phorbol esters and diacylglycerol and play
            important roles in neurotransmitter release at synapses. Single
            nucleotide polymorphisms in this gene may be associated with
            sporadic amyotrophic lateral sclerosis. [provided by RefSeq, Feb
            2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1676
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..1676
                     /product="protein unc-13 homolog A isoform 4"
                     /note="protein unc-13 homolog A"
                     /calculated_mol_wt=189928
     Region          1..127
                     /region_name="C2A_Munc13"
                     /note="C2 domain first repeat in Munc13 (mammalian
                     uncoordinated) proteins; cd08394"
                     /db_xref="CDD:176040"
     Site            order(23,25,27,31..34,63,65,71..74)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:176040"
     Region          186..445
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62768; propagated from
                     UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62768; propagated from
                     UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62768; propagated from
                     UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62768; propagated from
                     UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Region          533..614
                     /region_name="C1_Munc13-2-like"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in Munc13-2, Munc13-3 and similar proteins; cd20859"
                     /db_xref="CDD:410409"
     Site            order(557..563,571..575,578)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410409"
     Region          674..800
                     /region_name="C2B_Munc13"
                     /note="C2 domain second repeat in Munc13 (mammalian
                     uncoordinated) proteins; cd04027"
                     /db_xref="CDD:175993"
     Site            order(690,696,742,744,761)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175993"
     Region          992..1485
                     /region_name="MUN"
                     /note="MUN domain; pfam06292"
                     /db_xref="CDD:461870"
     Region          1519..1638
                     /region_name="C2C_Munc13"
                     /note="C2 domain third repeat in Munc13 (mammalian
                     uncoordinated) proteins; cd08395"
                     /db_xref="CDD:176041"
     CDS             1..1676
                     /gene="UNC13A"
                     /gene_synonym="IDDSF; Munc13-1; NEDHES; NEDSMS"
                     /coded_by="NM_001387023.1:156..5186"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS92557.1"
                     /db_xref="GeneID:23025"
                     /db_xref="HGNC:HGNC:23150"
                     /db_xref="MIM:609894"
ORIGIN      
        1 msllcvgvkk akfdgaqekf ntyvtlkvqn vksttiavrg sqpsweqdfm feinrldlgl
       61 tvevwnkgli wdtmvgtvwi plrtirqsne egpgewltld sqvimadsei cgtkdptfhr
      121 illdtrfelp ldipeeeary wakkleqlna mrdqdeysfq deqdkplpvp snqccnwnyf
      181 gwgeqhnddp dsavddrdsd yrsetsnsip ppyyttsqpn asvhqysvrp pplgsresys
      241 dsmhsyeefs epqalsptgs sryassgels qgssqlsedf dpdehslqgs dmederdrds
      301 yhschssvsy hkdsprwdqd eeeleedled fleeeelped eeeleeeeee vpddlgsyaq
      361 redvavaepk dfkrislppa apgkedkapv apteapdmak vapkpatpdk vpaaeqipea
      421 eppkdeesfr predeegqeg qdsmsrakan wlrafnkvrm qlqeargege mskslwfkgg
      481 pgggliiids mpdirkrkpi plvsdlslvq srkagitsal asstlnneel knhvykktlq
      541 aliypisctt phnfevwtat tptycyeceg llwgiarqgm rctecgvkch ekcqdllnad
      601 clqraaekss khgaedrtqn iimvlkdrmk irernkpeif eliqeifavt ktahtqqmka
      661 vkqsvldgts kwsakisitv vcaqglqakd ktgssdpyvt vqvgktkkrt ktiygnlnpv
      721 weenfhfech nssdrikvrv wdedddiksr vkqrfkresd dflgqtiiev rtlsgemdvw
      781 ynldkrtdks avsgairlhi sveikgeekv apyhvqytcl henlfhfvtd vqnngvvkip
      841 dakgddawkv yydetaqeiv defamrygve siyqamthfa clsskymcpg vpavmstlla
      901 ninayyahtt astnvsasdr faasnfgker fvklldqlhn slridlsmyr nnfpassper
      961 lqdlkstvdl ltsitffrmk vqelqsppra sqvvkdcvka clnstyeyif nnchelysre
     1021 yqtdpakkge vlpeeqgpsi knldfwskli tlivsiieed knsytpclnq fpqelnvgki
     1081 saevmwnlfa qdmkyameeh dkhrlcksad ymnlhfkvkw lyneyvtelp afkdrvpeyp
     1141 awfepfviqw ldeneevsrd flhgalerdk kdgfqqtseh alfscsvvdv fsqlnqsfei
     1201 ikklecpdpq ivghymrrfa ktisnvllqy adiiskdfas ycskekekvp cilmnntqql
     1261 rvqlekmfea mggkeldaea sdilkelqvk lnnvldelsr vfatsfqphi eecvkqmgdi
     1321 lsqvkgtgnv pasacssvaq dadnvlqpim dlldsnltlf akicektvlk rvlkelwklv
     1381 mntmektivl ppltdqtgtq mifnaakelg qlsklkdhmv reeaksltpk qcavvelald
     1441 tikqyfhagg vglkktflek spdlqslrya lslytqatdl liktfvqtqs aqglgvedpv
     1501 gevsvhvelf thpgtgehkv tvkvvaandl kwqtsgifrp fievniigpq lsdkkrkfat
     1561 ksknnswapk ynesfqftls adagpecyel qvcvkdycfa redrtvglav lqlrelaqrg
     1621 saacwlplgr rihmddtglt vlrilsqrsn devakefvkl ksdtrsaeeg gaapap
//
LOCUS       NP_001073890            1703 aa            linear   PRI 08-JAN-2026
DEFINITION  protein unc-13 homolog A isoform 1 [Homo sapiens].
ACCESSION   NP_001073890 XP_038604
VERSION     NP_001073890.2
DBSOURCE    REFSEQ: accession NM_001080421.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1703)
  AUTHORS   Agra Almeida Quadros,A.R., Li,Z., Wang,X., Ndayambaje,I.S.,
            Aryal,S., Ramesh,N., Nolan,M., Jayakumar,R., Han,Y., Stillman,H.,
            Aguilar,C., Wheeler,H.J., Connors,T., Lopez-Erauskin,J.,
            Baughn,M.W., Melamed,Z., Beccari,M.S., Olmedo Martinez,L.,
            Canori,M., Lee,C.Z., Moran,L., Draper,I., Kopin,A.S., Oakley,D.H.,
            Dickson,D.W., Cleveland,D.W., Hyman,B.T., Das,S., Ertekin-Taner,N.
            and Lagier-Tourenne,C.
  TITLE     Cryptic splicing of stathmin-2 and UNC13A mRNAs is a pathological
            hallmark of TDP-43-associated Alzheimer's disease
  JOURNAL   Acta Neuropathol 147 (1), 9 (2024)
   PUBMED   38175301
  REMARK    GeneRIF: Cryptic splicing of stathmin-2 and UNC13A mRNAs is a
            pathological hallmark of TDP-43-associated Alzheimer's disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1703)
  AUTHORS   Fu,R.H., Chen,H.J. and Hong,S.Y.
  TITLE     Interaction of the C9orf72-Amyotrophic Lateral Sclerosis-Related
            Proline-Arginine Dipeptide Repeat Protein with the RNA-Binding
            Protein NOVA1 Causes Decreased Expression of UNC13A Due to Enhanced
            Inclusion of Cryptic Exons, Which Is Reversed by Betulin Treatment
  JOURNAL   Cells 12 (20), 2476 (2023)
   PUBMED   37887320
  REMARK    GeneRIF: Interaction of the C9orf72-Amyotrophic Lateral
            Sclerosis-Related Proline-Arginine Dipeptide Repeat Protein with
            the RNA-Binding Protein NOVA1 Causes Decreased Expression of UNC13A
            Due to Enhanced Inclusion of Cryptic Exons, Which Is Reversed by
            Betulin Treatment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1703)
  AUTHORS   Brown,A.L., Wilkins,O.G., Keuss,M.J., Kargbo-Hill,S.E.,
            Zanovello,M., Lee,W.C., Bampton,A., Lee,F.C.Y., Masino,L., Qi,Y.A.,
            Bryce-Smith,S., Gatt,A., Hallegger,M., Fagegaltier,D., Phatnani,H.,
            Newcombe,J., Gustavsson,E.K., Seddighi,S., Reyes,J.F., Coon,S.L.,
            Ramos,D., Schiavo,G., Fisher,E.M.C., Raj,T., Secrier,M.,
            Lashley,T., Ule,J., Buratti,E., Humphrey,J., Ward,M.E. and
            Fratta,P.
  CONSRTM   NYGC ALS Consortium
  TITLE     TDP-43 loss and ALS-risk SNPs drive mis-splicing and depletion of
            UNC13A
  JOURNAL   Nature 603 (7899), 131-137 (2022)
   PUBMED   35197628
  REMARK    GeneRIF: TDP-43 loss and ALS-risk SNPs drive mis-splicing and
            depletion of UNC13A.
            Erratum:[Nature. 2024 Jul;631(8020):E7. doi:
            10.1038/s41586-024-07577-9. PMID: 38890465]
REFERENCE   4  (residues 1 to 1703)
  AUTHORS   Ma,X.R., Prudencio,M., Koike,Y., Vatsavayai,S.C., Kim,G.,
            Harbinski,F., Briner,A., Rodriguez,C.M., Guo,C., Akiyama,T.,
            Schmidt,H.B., Cummings,B.B., Wyatt,D.W., Kurylo,K., Miller,G.,
            Mekhoubad,S., Sallee,N., Mekonnen,G., Ganser,L., Rubien,J.D.,
            Jansen-West,K., Cook,C.N., Pickles,S., Oskarsson,B.,
            Graff-Radford,N.R., Boeve,B.F., Knopman,D.S., Petersen,R.C.,
            Dickson,D.W., Shorter,J., Myong,S., Green,E.M., Seeley,W.W.,
            Petrucelli,L. and Gitler,A.D.
  TITLE     TDP-43 represses cryptic exon inclusion in the FTD-ALS gene UNC13A
  JOURNAL   Nature 603 (7899), 124-130 (2022)
   PUBMED   35197626
  REMARK    GeneRIF: TDP-43 represses cryptic exon inclusion in the FTD-ALS
            gene UNC13A.
REFERENCE   5  (residues 1 to 1703)
  AUTHORS   You,Y., Katti,S., Yu,B., Igumenova,T.I. and Das,J.
  TITLE     Probing the Diacylglycerol Binding Site of Presynaptic Munc13-1
  JOURNAL   Biochemistry 60 (16), 1286-1298 (2021)
   PUBMED   33818064
  REMARK    GeneRIF: Probing the Diacylglycerol Binding Site of Presynaptic
            Munc13-1.
REFERENCE   6  (residues 1 to 1703)
  AUTHORS   Diekstra,F.P., van Vught,P.W., van Rheenen,W., Koppers,M.,
            Pasterkamp,R.J., van Es,M.A., Schelhaas,H.J., de Visser,M.,
            Robberecht,W., Van Damme,P., Andersen,P.M., van den Berg,L.H. and
            Veldink,J.H.
  TITLE     UNC13A is a modifier of survival in amyotrophic lateral sclerosis
  JOURNAL   Neurobiol Aging 33 (3), 630 (2012)
   PUBMED   22118904
  REMARK    GeneRIF: Our results further corroborate the role of UNC13A in
            amyotrophic lateral sclerosis pathogenesis.
REFERENCE   7  (residues 1 to 1703)
  AUTHORS   van Es,M.A., Veldink,J.H., Saris,C.G., Blauw,H.M., van Vught,P.W.,
            Birve,A., Lemmens,R., Schelhaas,H.J., Groen,E.J., Huisman,M.H., van
            der Kooi,A.J., de Visser,M., Dahlberg,C., Estrada,K.,
            Rivadeneira,F., Hofman,A., Zwarts,M.J., van Doormaal,P.T.,
            Rujescu,D., Strengman,E., Giegling,I., Muglia,P., Tomik,B.,
            Slowik,A., Uitterlinden,A.G., Hendrich,C., Waibel,S., Meyer,T.,
            Ludolph,A.C., Glass,J.D., Purcell,S., Cichon,S., Nothen,M.M.,
            Wichmann,H.E., Schreiber,S., Vermeulen,S.H., Kiemeney,L.A.,
            Wokke,J.H., Cronin,S., McLaughlin,R.L., Hardiman,O., Fumoto,K.,
            Pasterkamp,R.J., Meininger,V., Melki,J., Leigh,P.N., Shaw,C.E.,
            Landers,J.E., Al-Chalabi,A., Brown,R.H. Jr., Robberecht,W.,
            Andersen,P.M., Ophoff,R.A. and van den Berg,L.H.
  TITLE     Genome-wide association study identifies 19p13.3 (UNC13A) and
            9p21.2 as susceptibility loci for sporadic amyotrophic lateral
            sclerosis
  JOURNAL   Nat Genet 41 (10), 1083-1087 (2009)
   PUBMED   19734901
  REMARK    GeneRIF: rs12608932 Single Nucleotide Polymorphism is located at
            19p13.3 and maps to a haplotype block within the boundaries of
            UNC13A, which regulates the release of neurotransmitters such as
            glutamate at neuromuscular synapses.
            GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 1703)
  AUTHORS   Rossner,S., Fuchsbrunner,K., Lange-Dohna,C., Hartlage-Rubsamen,M.,
            Bigl,V., Betz,A., Reim,K. and Brose,N.
  TITLE     Munc13-1-mediated vesicle priming contributes to secretory amyloid
            precursor protein processing
  JOURNAL   J Biol Chem 279 (27), 27841-27844 (2004)
   PUBMED   15123597
REFERENCE   9  (residues 1 to 1703)
  AUTHORS   Sudhof,T.C.
  TITLE     The synaptic vesicle cycle
  JOURNAL   Annu Rev Neurosci 27, 509-547 (2004)
   PUBMED   15217342
  REMARK    Review article
REFERENCE   10 (residues 1 to 1703)
  AUTHORS   Sheu,L., Pasyk,E.A., Ji,J., Huang,X., Gao,X., Varoqueaux,F.,
            Brose,N. and Gaisano,H.Y.
  TITLE     Regulation of insulin exocytosis by Munc13-1
  JOURNAL   J Biol Chem 278 (30), 27556-27563 (2003)
   PUBMED   12871971
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008761.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 14, 2010 this sequence version replaced NP_001073890.1.
            
            Summary: This gene encodes a member of the UNC13 family. UNC13
            proteins bind to phorbol esters and diacylglycerol and play
            important roles in neurotransmitter release at synapses. Single
            nucleotide polymorphisms in this gene may be associated with
            sporadic amyotrophic lateral sclerosis. [provided by RefSeq, Feb
            2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB028955.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000519716.7/ ENSP00000429562.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1703
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..1703
                     /product="protein unc-13 homolog A isoform 1"
                     /note="protein unc-13 homolog A"
                     /calculated_mol_wt=192884
     Region          1..127
                     /region_name="C2A_Munc13"
                     /note="C2 domain first repeat in Munc13 (mammalian
                     uncoordinated) proteins; cd08394"
                     /db_xref="CDD:176040"
     Site            order(23,25,27,31..34,63,65,71..74)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:176040"
     Region          186..445
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62768; propagated from
                     UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62768; propagated from
                     UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62768; propagated from
                     UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62768; propagated from
                     UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Region          535..616
                     /region_name="C1_Munc13-2-like"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in Munc13-2, Munc13-3 and similar proteins; cd20859"
                     /db_xref="CDD:410409"
     Site            order(559..565,573..577,580)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410409"
     Region          676..802
                     /region_name="C2B_Munc13"
                     /note="C2 domain second repeat in Munc13 (mammalian
                     uncoordinated) proteins; cd04027"
                     /db_xref="CDD:175993"
     Site            order(692,698,744,746,763)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175993"
     Region          994..1512
                     /region_name="MUN"
                     /note="MUN domain; pfam06292"
                     /db_xref="CDD:461870"
     Region          1546..1665
                     /region_name="C2C_Munc13"
                     /note="C2 domain third repeat in Munc13 (mammalian
                     uncoordinated) proteins; cd08395"
                     /db_xref="CDD:176041"
     CDS             1..1703
                     /gene="UNC13A"
                     /gene_synonym="IDDSF; Munc13-1; NEDHES; NEDSMS"
                     /coded_by="NM_001080421.3:156..5267"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46013.2"
                     /db_xref="GeneID:23025"
                     /db_xref="HGNC:HGNC:23150"
                     /db_xref="MIM:609894"
ORIGIN      
        1 msllcvgvkk akfdgaqekf ntyvtlkvqn vksttiavrg sqpsweqdfm feinrldlgl
       61 tvevwnkgli wdtmvgtvwi plrtirqsne egpgewltld sqvimadsei cgtkdptfhr
      121 illdtrfelp ldipeeeary wakkleqlna mrdqdeysfq deqdkplpvp snqccnwnyf
      181 gwgeqhnddp dsavddrdsd yrsetsnsip ppyyttsqpn asvhqysvrp pplgsresys
      241 dsmhsyeefs epqalsptgs sryassgels qgssqlsedf dpdehslqgs dmederdrds
      301 yhschssvsy hkdsprwdqd eeeleedled fleeeelped eeeleeeeee vpddlgsyaq
      361 redvavaepk dfkrislppa apgkedkapv apteapdmak vapkpatpdk vpaaeqipea
      421 eppkdeesfr predeegqeg qdsmsrakan wlrafnkvrm qlqeargege mskslwfkgg
      481 pgggliiids mpdirkrkpi plvsdlamsl vqsrkagits alasstlnne elknhvykkt
      541 lqaliypisc ttphnfevwt attptycyec egllwgiarq gmrctecgvk chekcqdlln
      601 adclqraaek sskhgaedrt qniimvlkdr mkirernkpe ifeliqeifa vtktahtqqm
      661 kavkqsvldg tskwsakisi tvvcaqglqa kdktgssdpy vtvqvgktkk rtktiygnln
      721 pvweenfhfe chnssdrikv rvwdedddik srvkqrfkre sddflgqtii evrtlsgemd
      781 vwynldkrtd ksavsgairl hisveikgee kvapyhvqyt clhenlfhfv tdvqnngvvk
      841 ipdakgddaw kvyydetaqe ivdefamryg vesiyqamth faclsskymc pgvpavmstl
      901 laninayyah ttastnvsas drfaasnfgk erfvklldql hnslridlsm yrnnfpassp
      961 erlqdlkstv dlltsitffr mkvqelqspp rasqvvkdcv kaclnstyey ifnnchelys
     1021 reyqtdpakk gevlpeeqgp siknldfwsk litlivsiie edknsytpcl nqfpqelnvg
     1081 kisaevmwnl faqdmkyame ehdkhrlcks adymnlhfkv kwlyneyvte lpafkdrvpe
     1141 ypawfepfvi qwldeneevs rdflhgaler dkkdgfqqts ehalfscsvv dvfsqlnqsf
     1201 eiikklecpd pqivghymrr faktisnvll qyadiiskdf asycskekek vpcilmnntq
     1261 qlrvqlekmf eamggkelda easdilkelq vklnnvldel srvfatsfqp hieecvkqmg
     1321 dilsqvkgtg nvpasacssv aqdadnvlqp imdlldsnlt lfakicektv lkrvlkelwk
     1381 lvmntmekti vlppltdqtm ignllrkhgk glekgrvklp shsdgtqmif naakelgqls
     1441 klkdhmvree aksltpkqca vvelaldtik qyfhaggvgl kktflekspd lqslryalsl
     1501 ytqatdllik tfvqtqsaqg lgvedpvgev svhvelfthp gtgehkvtvk vvaandlkwq
     1561 tsgifrpfie vniigpqlsd kkrkfatksk nnswapkyne sfqftlsada gpecyelqvc
     1621 vkdycfared rtvglavlql relaqrgsaa cwlplgrrih mddtgltvlr ilsqrsndev
     1681 akefvklksd trsaeeggaa pap
//
LOCUS       NP_001369358             387 aa            linear   PRI 08-JAN-2026
DEFINITION  WD repeat-containing protein 89 [Homo sapiens].
ACCESSION   NP_001369358
VERSION     NP_001369358.1
DBSOURCE    REFSEQ: accession NM_001382429.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136038.5.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..387
                     /product="WD repeat-containing protein 89"
                     /calculated_mol_wt=43084
     Region          21..65
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          41..349
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(45,49,55..56,68..69,87,91,97..98,112..113,131,140,
                     146..147,169,187,192,198..199,215,234,238,244..245,
                     260..261,292,297,303..304,319..320,338,342,348..349)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          68..107
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          74..112
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          112..156
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          118..160
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          168..208
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          174..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..254
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          219..259
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          267..317
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          319..358
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          324..348
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..387
                     /gene="WDR89"
                     /gene_synonym="C14orf150; MSTP050"
                     /coded_by="NM_001382429.1:386..1549"
                     /db_xref="CCDS:CCDS9759.1"
                     /db_xref="GeneID:112840"
                     /db_xref="HGNC:HGNC:20489"
                     /db_xref="MIM:621458"
ORIGIN      
        1 mekieeqfan lhivkcslgt keptyllgid tsktvqagke nlvavlcsng siriydkerl
       61 nvlrefsgyp gllngvrfan scdsvysact dgtvkcwdar varekpvqlf kgypsnifis
      121 fdincndhii cagtekvddd allvfwdarm nsqnlsttkd slgayseths ddvtqvrfhp
      181 snpnmvvsgs sdglvnvfdi nidneedalv ttcnsissvs cigwsgkgyk qiycmthdeg
      241 fywwdlnhld tdepvtrlni qdvrevvnmk edaldyligg lyhektdtlh viggtnkgri
      301 hlmncsmsgl thvtslqggh aatvrsfcwn vqddslltgg edaqlllwkp gaiektftkk
      361 esmkiassvh qrvrvhsnds ykrrkkq
//
LOCUS       NP_001373951            1698 aa            linear   PRI 08-JAN-2026
DEFINITION  protein unc-13 homolog A isoform 3 [Homo sapiens].
ACCESSION   NP_001373951
VERSION     NP_001373951.1
DBSOURCE    REFSEQ: accession NM_001387022.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1698)
  AUTHORS   Agra Almeida Quadros,A.R., Li,Z., Wang,X., Ndayambaje,I.S.,
            Aryal,S., Ramesh,N., Nolan,M., Jayakumar,R., Han,Y., Stillman,H.,
            Aguilar,C., Wheeler,H.J., Connors,T., Lopez-Erauskin,J.,
            Baughn,M.W., Melamed,Z., Beccari,M.S., Olmedo Martinez,L.,
            Canori,M., Lee,C.Z., Moran,L., Draper,I., Kopin,A.S., Oakley,D.H.,
            Dickson,D.W., Cleveland,D.W., Hyman,B.T., Das,S., Ertekin-Taner,N.
            and Lagier-Tourenne,C.
  TITLE     Cryptic splicing of stathmin-2 and UNC13A mRNAs is a pathological
            hallmark of TDP-43-associated Alzheimer's disease
  JOURNAL   Acta Neuropathol 147 (1), 9 (2024)
   PUBMED   38175301
  REMARK    GeneRIF: Cryptic splicing of stathmin-2 and UNC13A mRNAs is a
            pathological hallmark of TDP-43-associated Alzheimer's disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1698)
  AUTHORS   Fu,R.H., Chen,H.J. and Hong,S.Y.
  TITLE     Interaction of the C9orf72-Amyotrophic Lateral Sclerosis-Related
            Proline-Arginine Dipeptide Repeat Protein with the RNA-Binding
            Protein NOVA1 Causes Decreased Expression of UNC13A Due to Enhanced
            Inclusion of Cryptic Exons, Which Is Reversed by Betulin Treatment
  JOURNAL   Cells 12 (20), 2476 (2023)
   PUBMED   37887320
  REMARK    GeneRIF: Interaction of the C9orf72-Amyotrophic Lateral
            Sclerosis-Related Proline-Arginine Dipeptide Repeat Protein with
            the RNA-Binding Protein NOVA1 Causes Decreased Expression of UNC13A
            Due to Enhanced Inclusion of Cryptic Exons, Which Is Reversed by
            Betulin Treatment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1698)
  AUTHORS   Brown,A.L., Wilkins,O.G., Keuss,M.J., Kargbo-Hill,S.E.,
            Zanovello,M., Lee,W.C., Bampton,A., Lee,F.C.Y., Masino,L., Qi,Y.A.,
            Bryce-Smith,S., Gatt,A., Hallegger,M., Fagegaltier,D., Phatnani,H.,
            Newcombe,J., Gustavsson,E.K., Seddighi,S., Reyes,J.F., Coon,S.L.,
            Ramos,D., Schiavo,G., Fisher,E.M.C., Raj,T., Secrier,M.,
            Lashley,T., Ule,J., Buratti,E., Humphrey,J., Ward,M.E. and
            Fratta,P.
  CONSRTM   NYGC ALS Consortium
  TITLE     TDP-43 loss and ALS-risk SNPs drive mis-splicing and depletion of
            UNC13A
  JOURNAL   Nature 603 (7899), 131-137 (2022)
   PUBMED   35197628
  REMARK    GeneRIF: TDP-43 loss and ALS-risk SNPs drive mis-splicing and
            depletion of UNC13A.
            Erratum:[Nature. 2024 Jul;631(8020):E7. doi:
            10.1038/s41586-024-07577-9. PMID: 38890465]
REFERENCE   4  (residues 1 to 1698)
  AUTHORS   Ma,X.R., Prudencio,M., Koike,Y., Vatsavayai,S.C., Kim,G.,
            Harbinski,F., Briner,A., Rodriguez,C.M., Guo,C., Akiyama,T.,
            Schmidt,H.B., Cummings,B.B., Wyatt,D.W., Kurylo,K., Miller,G.,
            Mekhoubad,S., Sallee,N., Mekonnen,G., Ganser,L., Rubien,J.D.,
            Jansen-West,K., Cook,C.N., Pickles,S., Oskarsson,B.,
            Graff-Radford,N.R., Boeve,B.F., Knopman,D.S., Petersen,R.C.,
            Dickson,D.W., Shorter,J., Myong,S., Green,E.M., Seeley,W.W.,
            Petrucelli,L. and Gitler,A.D.
  TITLE     TDP-43 represses cryptic exon inclusion in the FTD-ALS gene UNC13A
  JOURNAL   Nature 603 (7899), 124-130 (2022)
   PUBMED   35197626
  REMARK    GeneRIF: TDP-43 represses cryptic exon inclusion in the FTD-ALS
            gene UNC13A.
REFERENCE   5  (residues 1 to 1698)
  AUTHORS   You,Y., Katti,S., Yu,B., Igumenova,T.I. and Das,J.
  TITLE     Probing the Diacylglycerol Binding Site of Presynaptic Munc13-1
  JOURNAL   Biochemistry 60 (16), 1286-1298 (2021)
   PUBMED   33818064
  REMARK    GeneRIF: Probing the Diacylglycerol Binding Site of Presynaptic
            Munc13-1.
REFERENCE   6  (residues 1 to 1698)
  AUTHORS   Diekstra,F.P., van Vught,P.W., van Rheenen,W., Koppers,M.,
            Pasterkamp,R.J., van Es,M.A., Schelhaas,H.J., de Visser,M.,
            Robberecht,W., Van Damme,P., Andersen,P.M., van den Berg,L.H. and
            Veldink,J.H.
  TITLE     UNC13A is a modifier of survival in amyotrophic lateral sclerosis
  JOURNAL   Neurobiol Aging 33 (3), 630 (2012)
   PUBMED   22118904
  REMARK    GeneRIF: Our results further corroborate the role of UNC13A in
            amyotrophic lateral sclerosis pathogenesis.
REFERENCE   7  (residues 1 to 1698)
  AUTHORS   van Es,M.A., Veldink,J.H., Saris,C.G., Blauw,H.M., van Vught,P.W.,
            Birve,A., Lemmens,R., Schelhaas,H.J., Groen,E.J., Huisman,M.H., van
            der Kooi,A.J., de Visser,M., Dahlberg,C., Estrada,K.,
            Rivadeneira,F., Hofman,A., Zwarts,M.J., van Doormaal,P.T.,
            Rujescu,D., Strengman,E., Giegling,I., Muglia,P., Tomik,B.,
            Slowik,A., Uitterlinden,A.G., Hendrich,C., Waibel,S., Meyer,T.,
            Ludolph,A.C., Glass,J.D., Purcell,S., Cichon,S., Nothen,M.M.,
            Wichmann,H.E., Schreiber,S., Vermeulen,S.H., Kiemeney,L.A.,
            Wokke,J.H., Cronin,S., McLaughlin,R.L., Hardiman,O., Fumoto,K.,
            Pasterkamp,R.J., Meininger,V., Melki,J., Leigh,P.N., Shaw,C.E.,
            Landers,J.E., Al-Chalabi,A., Brown,R.H. Jr., Robberecht,W.,
            Andersen,P.M., Ophoff,R.A. and van den Berg,L.H.
  TITLE     Genome-wide association study identifies 19p13.3 (UNC13A) and
            9p21.2 as susceptibility loci for sporadic amyotrophic lateral
            sclerosis
  JOURNAL   Nat Genet 41 (10), 1083-1087 (2009)
   PUBMED   19734901
  REMARK    GeneRIF: rs12608932 Single Nucleotide Polymorphism is located at
            19p13.3 and maps to a haplotype block within the boundaries of
            UNC13A, which regulates the release of neurotransmitters such as
            glutamate at neuromuscular synapses.
            GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 1698)
  AUTHORS   Rossner,S., Fuchsbrunner,K., Lange-Dohna,C., Hartlage-Rubsamen,M.,
            Bigl,V., Betz,A., Reim,K. and Brose,N.
  TITLE     Munc13-1-mediated vesicle priming contributes to secretory amyloid
            precursor protein processing
  JOURNAL   J Biol Chem 279 (27), 27841-27844 (2004)
   PUBMED   15123597
REFERENCE   9  (residues 1 to 1698)
  AUTHORS   Sudhof,T.C.
  TITLE     The synaptic vesicle cycle
  JOURNAL   Annu Rev Neurosci 27, 509-547 (2004)
   PUBMED   15217342
  REMARK    Review article
REFERENCE   10 (residues 1 to 1698)
  AUTHORS   Sheu,L., Pasyk,E.A., Ji,J., Huang,X., Gao,X., Varoqueaux,F.,
            Brose,N. and Gaisano,H.Y.
  TITLE     Regulation of insulin exocytosis by Munc13-1
  JOURNAL   J Biol Chem 278 (30), 27556-27563 (2003)
   PUBMED   12871971
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008761.8.
            
            Summary: This gene encodes a member of the UNC13 family. UNC13
            proteins bind to phorbol esters and diacylglycerol and play
            important roles in neurotransmitter release at synapses. Single
            nucleotide polymorphisms in this gene may be associated with
            sporadic amyotrophic lateral sclerosis. [provided by RefSeq, Feb
            2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1698
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..1698
                     /product="protein unc-13 homolog A isoform 3"
                     /note="protein unc-13 homolog A"
                     /calculated_mol_wt=192338
     Region          1..127
                     /region_name="C2A_Munc13"
                     /note="C2 domain first repeat in Munc13 (mammalian
                     uncoordinated) proteins; cd08394"
                     /db_xref="CDD:176040"
     Site            order(23,25,27,31..34,63,65,71..74)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:176040"
     Region          186..445
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62768; propagated from
                     UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62768; propagated from
                     UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62768; propagated from
                     UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62768; propagated from
                     UniProtKB/Swiss-Prot (Q9UPW8.4)"
     Region          533..614
                     /region_name="C1_Munc13-2-like"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     found in Munc13-2, Munc13-3 and similar proteins; cd20859"
                     /db_xref="CDD:410409"
     Site            order(557..563,571..575,578)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410409"
     Region          674..800
                     /region_name="C2B_Munc13"
                     /note="C2 domain second repeat in Munc13 (mammalian
                     uncoordinated) proteins; cd04027"
                     /db_xref="CDD:175993"
     Site            order(690,696,742,744,761)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175993"
     Region          992..1507
                     /region_name="MUN"
                     /note="MUN domain; pfam06292"
                     /db_xref="CDD:461870"
     Region          1541..1660
                     /region_name="C2C_Munc13"
                     /note="C2 domain third repeat in Munc13 (mammalian
                     uncoordinated) proteins; cd08395"
                     /db_xref="CDD:176041"
     CDS             1..1698
                     /gene="UNC13A"
                     /gene_synonym="IDDSF; Munc13-1; NEDHES; NEDSMS"
                     /coded_by="NM_001387022.1:156..5252"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:23025"
                     /db_xref="HGNC:HGNC:23150"
                     /db_xref="MIM:609894"
ORIGIN      
        1 msllcvgvkk akfdgaqekf ntyvtlkvqn vksttiavrg sqpsweqdfm feinrldlgl
       61 tvevwnkgli wdtmvgtvwi plrtirqsne egpgewltld sqvimadsei cgtkdptfhr
      121 illdtrfelp ldipeeeary wakkleqlna mrdqdeysfq deqdkplpvp snqccnwnyf
      181 gwgeqhnddp dsavddrdsd yrsetsnsip ppyyttsqpn asvhqysvrp pplgsresys
      241 dsmhsyeefs epqalsptgs sryassgels qgssqlsedf dpdehslqgs dmederdrds
      301 yhschssvsy hkdsprwdqd eeeleedled fleeeelped eeeleeeeee vpddlgsyaq
      361 redvavaepk dfkrislppa apgkedkapv apteapdmak vapkpatpdk vpaaeqipea
      421 eppkdeesfr predeegqeg qdsmsrakan wlrafnkvrm qlqeargege mskslwfkgg
      481 pgggliiids mpdirkrkpi plvsdlslvq srkagitsal asstlnneel knhvykktlq
      541 aliypisctt phnfevwtat tptycyeceg llwgiarqgm rctecgvkch ekcqdllnad
      601 clqraaekss khgaedrtqn iimvlkdrmk irernkpeif eliqeifavt ktahtqqmka
      661 vkqsvldgts kwsakisitv vcaqglqakd ktgssdpyvt vqvgktkkrt ktiygnlnpv
      721 weenfhfech nssdrikvrv wdedddiksr vkqrfkresd dflgqtiiev rtlsgemdvw
      781 ynldkrtdks avsgairlhi sveikgeekv apyhvqytcl henlfhfvtd vqnngvvkip
      841 dakgddawkv yydetaqeiv defamrygve siyqamthfa clsskymcpg vpavmstlla
      901 ninayyahtt astnvsasdr faasnfgker fvklldqlhn slridlsmyr nnfpassper
      961 lqdlkstvdl ltsitffrmk vqelqsppra sqvvkdcvka clnstyeyif nnchelysre
     1021 yqtdpakkge vlpeeqgpsi knldfwskli tlivsiieed knsytpclnq fpqelnvgki
     1081 saevmwnlfa qdmkyameeh dkhrlcksad ymnlhfkvkw lyneyvtelp afkdrvpeyp
     1141 awfepfviqw ldeneevsrd flhgalerdk kdgfqqtseh alfscsvvdv fsqlnqsfei
     1201 ikklecpdpq ivghymrrfa ktisnvllqy adiiskdfas ycskekekpc ilmnntqqlr
     1261 vqlekmfeam ggkeldaeas dilkelqvkl nnvldelsrv fatsfqphie ecvkqmgdil
     1321 sqvkgtgnvp asacssvaqd adnvlqpimd lldsnltlfa kicektvlkr vlkelwklvm
     1381 ntmektivlp pltdqtgnll rkhgkglekg rvklpshsdg tqmifnaake lgqlsklkdh
     1441 mvreeakslt pkqcavvela ldtikqyfha ggvglkktfl ekspdlqslr yalslytqat
     1501 dlliktfvqt qsaqglgved pvgevsvhve lfthpgtgeh kvtvkvvaan dlkwqtsgif
     1561 rpfievniig pqlsdkkrkf atksknnswa pkynesfqft lsadagpecy elqvcvkdyc
     1621 faredrtvgl avlqlrelaq rgsaacwlpl grrihmddtg ltvlrilsqr sndevakefv
     1681 klksdtrsae eggaapap
//
LOCUS       NP_001369355             387 aa            linear   PRI 08-JAN-2026
DEFINITION  WD repeat-containing protein 89 [Homo sapiens].
ACCESSION   NP_001369355
VERSION     NP_001369355.1
DBSOURCE    REFSEQ: accession NM_001382426.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136038.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1089697.1,
                                           SRR14038196.2993816.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..387
                     /product="WD repeat-containing protein 89"
                     /calculated_mol_wt=43084
     Region          21..65
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          41..349
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(45,49,55..56,68..69,87,91,97..98,112..113,131,140,
                     146..147,169,187,192,198..199,215,234,238,244..245,
                     260..261,292,297,303..304,319..320,338,342,348..349)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          68..107
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          74..112
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          112..156
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          118..160
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          168..208
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          174..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..254
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          219..259
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          267..317
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          319..358
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          324..348
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..387
                     /gene="WDR89"
                     /gene_synonym="C14orf150; MSTP050"
                     /coded_by="NM_001382426.1:398..1561"
                     /db_xref="CCDS:CCDS9759.1"
                     /db_xref="GeneID:112840"
                     /db_xref="HGNC:HGNC:20489"
                     /db_xref="MIM:621458"
ORIGIN      
        1 mekieeqfan lhivkcslgt keptyllgid tsktvqagke nlvavlcsng siriydkerl
       61 nvlrefsgyp gllngvrfan scdsvysact dgtvkcwdar varekpvqlf kgypsnifis
      121 fdincndhii cagtekvddd allvfwdarm nsqnlsttkd slgayseths ddvtqvrfhp
      181 snpnmvvsgs sdglvnvfdi nidneedalv ttcnsissvs cigwsgkgyk qiycmthdeg
      241 fywwdlnhld tdepvtrlni qdvrevvnmk edaldyligg lyhektdtlh viggtnkgri
      301 hlmncsmsgl thvtslqggh aatvrsfcwn vqddslltgg edaqlllwkp gaiektftkk
      361 esmkiassvh qrvrvhsnds ykrrkkq
//
LOCUS       NP_001245201             387 aa            linear   PRI 08-JAN-2026
DEFINITION  WD repeat-containing protein 89 [Homo sapiens].
ACCESSION   NP_001245201
VERSION     NP_001245201.1
DBSOURCE    REFSEQ: accession NM_001258272.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA882425.1, DB178690.1, BP278550.1 and BC010698.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.72343.1,
                                           SRR1660809.257990.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..387
                     /product="WD repeat-containing protein 89"
                     /calculated_mol_wt=43084
     Region          21..65
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          41..349
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(45,49,55..56,68..69,87,91,97..98,112..113,131,140,
                     146..147,169,187,192,198..199,215,234,238,244..245,
                     260..261,292,297,303..304,319..320,338,342,348..349)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          68..107
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          74..112
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          112..156
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          118..160
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          168..208
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          174..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..254
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          219..259
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          267..317
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          319..358
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          324..348
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..387
                     /gene="WDR89"
                     /gene_synonym="C14orf150; MSTP050"
                     /coded_by="NM_001258272.2:711..1874"
                     /db_xref="CCDS:CCDS9759.1"
                     /db_xref="GeneID:112840"
                     /db_xref="HGNC:HGNC:20489"
                     /db_xref="MIM:621458"
ORIGIN      
        1 mekieeqfan lhivkcslgt keptyllgid tsktvqagke nlvavlcsng siriydkerl
       61 nvlrefsgyp gllngvrfan scdsvysact dgtvkcwdar varekpvqlf kgypsnifis
      121 fdincndhii cagtekvddd allvfwdarm nsqnlsttkd slgayseths ddvtqvrfhp
      181 snpnmvvsgs sdglvnvfdi nidneedalv ttcnsissvs cigwsgkgyk qiycmthdeg
      241 fywwdlnhld tdepvtrlni qdvrevvnmk edaldyligg lyhektdtlh viggtnkgri
      301 hlmncsmsgl thvtslqggh aatvrsfcwn vqddslltgg edaqlllwkp gaiektftkk
      361 esmkiassvh qrvrvhsnds ykrrkkq
//
LOCUS       NP_001369356             387 aa            linear   PRI 08-JAN-2026
DEFINITION  WD repeat-containing protein 89 [Homo sapiens].
ACCESSION   NP_001369356
VERSION     NP_001369356.1
DBSOURCE    REFSEQ: accession NM_001382427.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136038.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.1235096.1,
                                           SRR1803611.155395.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004, SAMN03267750
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..387
                     /product="WD repeat-containing protein 89"
                     /calculated_mol_wt=43084
     Region          21..65
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          41..349
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(45,49,55..56,68..69,87,91,97..98,112..113,131,140,
                     146..147,169,187,192,198..199,215,234,238,244..245,
                     260..261,292,297,303..304,319..320,338,342,348..349)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          68..107
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          74..112
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          112..156
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          118..160
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          168..208
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          174..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..254
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          219..259
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          267..317
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          319..358
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          324..348
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..387
                     /gene="WDR89"
                     /gene_synonym="C14orf150; MSTP050"
                     /coded_by="NM_001382427.1:352..1515"
                     /db_xref="CCDS:CCDS9759.1"
                     /db_xref="GeneID:112840"
                     /db_xref="HGNC:HGNC:20489"
                     /db_xref="MIM:621458"
ORIGIN      
        1 mekieeqfan lhivkcslgt keptyllgid tsktvqagke nlvavlcsng siriydkerl
       61 nvlrefsgyp gllngvrfan scdsvysact dgtvkcwdar varekpvqlf kgypsnifis
      121 fdincndhii cagtekvddd allvfwdarm nsqnlsttkd slgayseths ddvtqvrfhp
      181 snpnmvvsgs sdglvnvfdi nidneedalv ttcnsissvs cigwsgkgyk qiycmthdeg
      241 fywwdlnhld tdepvtrlni qdvrevvnmk edaldyligg lyhektdtlh viggtnkgri
      301 hlmncsmsgl thvtslqggh aatvrsfcwn vqddslltgg edaqlllwkp gaiektftkk
      361 esmkiassvh qrvrvhsnds ykrrkkq
//
LOCUS       NP_001008726             387 aa            linear   PRI 08-JAN-2026
DEFINITION  WD repeat-containing protein 89 [Homo sapiens].
ACCESSION   NP_001008726
VERSION     NP_001008726.1
DBSOURCE    REFSEQ: accession NM_001008726.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA882425.1, BP278550.1 and BC010698.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.54854.1,
                                           SRR1803614.147111.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..387
                     /product="WD repeat-containing protein 89"
                     /calculated_mol_wt=43084
     Region          21..65
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          41..349
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(45,49,55..56,68..69,87,91,97..98,112..113,131,140,
                     146..147,169,187,192,198..199,215,234,238,244..245,
                     260..261,292,297,303..304,319..320,338,342,348..349)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          68..107
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          74..112
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          112..156
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          118..160
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          168..208
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          174..212
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..254
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          219..259
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          267..317
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          319..358
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FK6.1)"
     Region          324..348
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..387
                     /gene="WDR89"
                     /gene_synonym="C14orf150; MSTP050"
                     /coded_by="NM_001008726.3:315..1478"
                     /db_xref="CCDS:CCDS9759.1"
                     /db_xref="GeneID:112840"
                     /db_xref="HGNC:HGNC:20489"
                     /db_xref="MIM:621458"
ORIGIN      
        1 mekieeqfan lhivkcslgt keptyllgid tsktvqagke nlvavlcsng siriydkerl
       61 nvlrefsgyp gllngvrfan scdsvysact dgtvkcwdar varekpvqlf kgypsnifis
      121 fdincndhii cagtekvddd allvfwdarm nsqnlsttkd slgayseths ddvtqvrfhp
      181 snpnmvvsgs sdglvnvfdi nidneedalv ttcnsissvs cigwsgkgyk qiycmthdeg
      241 fywwdlnhld tdepvtrlni qdvrevvnmk edaldyligg lyhektdtlh viggtnkgri
      301 hlmncsmsgl thvtslqggh aatvrsfcwn vqddslltgg edaqlllwkp gaiektftkk
      361 esmkiassvh qrvrvhsnds ykrrkkq
//
LOCUS       NP_001397860             489 aa            linear   PRI 08-JAN-2026
DEFINITION  E3 SUMO-protein ligase EGR2 isoform c [Homo sapiens].
ACCESSION   NP_001397860 XP_011537729
VERSION     NP_001397860.1
DBSOURCE    REFSEQ: accession NM_001410931.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Li,W., He,S., Tan,J., Li,N., Zhao,C., Wang,X., Zhang,Z., Liu,J.,
            Huang,J., Li,X., Zhou,Q., Hu,K., Yang,P. and Hou,S.
  TITLE     Transcription factor EGR2 alleviates autoimmune uveitis via
            activation of GDF15 to modulate the retinal microglial phenotype
  JOURNAL   Proc Natl Acad Sci U S A 121 (39), e2316161121 (2024)
   PUBMED   39298490
  REMARK    GeneRIF: Transcription factor EGR2 alleviates autoimmune uveitis
            via activation of GDF15 to modulate the retinal microglial
            phenotype.
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Song,A., Yan,R., Xiong,W., Xiang,H., Huang,J., Jiang,A. and
            Zhang,C.
  TITLE     Early growth response protein 2 promotes partial
            epithelial-mesenchymal transition by phosphorylating Smad3 during
            renal fibrosis
  JOURNAL   Transl Res 271, 13-25 (2024)
   PUBMED   38679230
  REMARK    GeneRIF: Early growth response protein 2 promotes partial
            epithelial-mesenchymal transition by phosphorylating Smad3 during
            renal fibrosis.
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Jian,H., Feng,H., Zhu,L., Li,X. and Ma,Z.
  TITLE     MicroRNA-150-5P regulates Th1/Th2 cytokines expression levels by
            targeting EGR2 in allergic rhinitis
  JOURNAL   Rhinology 62 (2), 250-256 (2024)
   PUBMED   38165680
  REMARK    GeneRIF: MicroRNA-150-5P regulates Th1/Th2 cytokines expression
            levels by targeting EGR2 in allergic rhinitis.
REFERENCE   4  (residues 1 to 489)
  AUTHORS   .
  TITLE     EGR2 drives TH17 cell pathogenicity in autoimmune neuroinflammation
  JOURNAL   Nat Immunol 24 (8), 1230-1231 (2023)
   PUBMED   37474655
  REMARK    GeneRIF: EGR2 drives TH17 cell pathogenicity in autoimmune
            neuroinflammation.
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 4 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301641
REFERENCE   6  (residues 1 to 489)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   7  (residues 1 to 489)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301384
REFERENCE   8  (residues 1 to 489)
  AUTHORS   Rangnekar,V.M., Aplin,A.C. and Sukhatme,V.P.
  TITLE     The serum and TPA responsive promoter and intron-exon structure of
            EGR2, a human early growth response gene encoding a zinc finger
            protein
  JOURNAL   Nucleic Acids Res 18 (9), 2749-2757 (1990)
   PUBMED   2111009
REFERENCE   9  (residues 1 to 489)
  AUTHORS   Chavrier,P., Janssen-Timmen,U., Mattei,M.G., Zerial,M., Bravo,R.
            and Charnay,P.
  TITLE     Structure, chromosome location, and expression of the mouse zinc
            finger gene Krox-20: multiple gene products and coregulation with
            the proto-oncogene c-fos
  JOURNAL   Mol Cell Biol 9 (2), 787-797 (1989)
   PUBMED   2496302
REFERENCE   10 (residues 1 to 489)
  AUTHORS   Joseph,L.J., Le Beau,M.M., Jamieson,G.A. Jr., Acharya,S.,
            Shows,T.B., Rowley,J.D. and Sukhatme,V.P.
  TITLE     Molecular cloning, sequencing, and mapping of EGR2, a human early
            growth response gene encoding a protein with 'zinc-binding finger'
            structure
  JOURNAL   Proc Natl Acad Sci U S A 85 (19), 7164-7168 (1988)
   PUBMED   3140236
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1989 Jan;86(2):515]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133417.11 and KF459538.1.
            
            On Aug 18, 2022 this sequence version replaced XP_011537729.1.
            
            Summary: The protein encoded by this gene is a transcription factor
            with three tandem C2H2-type zinc fingers. Defects in this gene are
            associated with Charcot-Marie-Tooth disease type 1D (CMT1D),
            Charcot-Marie-Tooth disease type 4E (CMT4E), and with
            Dejerine-Sottas syndrome (DSS). Multiple transcript variants
            encoding two different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2391086.1,
                                           SRR18074968.1881401.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA2145743 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.3"
     Protein         1..489
                     /product="E3 SUMO-protein ligase EGR2 isoform c"
                     /note="KROX-20, Drosophila, homolog (early growth
                     response-2); early growth response protein 2; zinc finger
                     protein Krox-20; E3 SUMO-protein ligase EGR2; E3
                     SUMO-protein transferase ERG2"
                     /calculated_mol_wt=51613
     Region          107..201
                     /region_name="DUF3446"
                     /note="Early growth response N-terminal domain; pfam11928"
                     /db_xref="CDD:463400"
     Region          353..377
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          355..377
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(362,364,366,368..369,372..373,376,390,392,396..397,
                     400..401,404,418,420,422,424..425,428..429,432)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          381..>449
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          385..405
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          413..433
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..489
                     /gene="EGR2"
                     /gene_synonym="AT591; CMT1D; CMT4E; KROX20"
                     /coded_by="NM_001410931.1:137..1606"
                     /note="isoform c is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS91248.1"
                     /db_xref="GeneID:1959"
                     /db_xref="HGNC:HGNC:3239"
                     /db_xref="MIM:129010"
ORIGIN      
        1 mrvglpseas scpwsargpr dpperrrsgl ahvlsdniyp vedlaatsvt ifpnaelggp
       61 fdqmngvagd gminidmtge krsldlpyps sfapvsaprn qtftymgkfs idpqypgasc
      121 ypegiinivs agilqgvtsp asttasssvt saspnplatg plgvctmsqt qpdldhlysp
      181 ppppppysgc agdlyqdpsa flsaattsts sslaypppps ypspkpatdp glfpmipdyp
      241 gffpsqcqrd lhgtagpdrk pfpcpldtlr vpppltplst irnftlggps agvtgpgasg
      301 gsegprlpgs ssaaaaaaaa aaynphhlpl rpilrprkyp nrpsktpvhe rpypcpaegc
      361 drrfsrsdel trhirihtgh kpfqcricmr nfsrsdhltt hirthtgekp facdycgrkf
      421 arsderkrht kihlrqkerk ssapsasvpa pstascsggv qpggtlcssn ssslgggpla
      481 pcssrtrtp
//
LOCUS       NP_001129649             476 aa            linear   PRI 08-JAN-2026
DEFINITION  E3 SUMO-protein ligase EGR2 isoform a [Homo sapiens].
ACCESSION   NP_001129649
VERSION     NP_001129649.1
DBSOURCE    REFSEQ: accession NM_001136177.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Li,W., He,S., Tan,J., Li,N., Zhao,C., Wang,X., Zhang,Z., Liu,J.,
            Huang,J., Li,X., Zhou,Q., Hu,K., Yang,P. and Hou,S.
  TITLE     Transcription factor EGR2 alleviates autoimmune uveitis via
            activation of GDF15 to modulate the retinal microglial phenotype
  JOURNAL   Proc Natl Acad Sci U S A 121 (39), e2316161121 (2024)
   PUBMED   39298490
  REMARK    GeneRIF: Transcription factor EGR2 alleviates autoimmune uveitis
            via activation of GDF15 to modulate the retinal microglial
            phenotype.
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Song,A., Yan,R., Xiong,W., Xiang,H., Huang,J., Jiang,A. and
            Zhang,C.
  TITLE     Early growth response protein 2 promotes partial
            epithelial-mesenchymal transition by phosphorylating Smad3 during
            renal fibrosis
  JOURNAL   Transl Res 271, 13-25 (2024)
   PUBMED   38679230
  REMARK    GeneRIF: Early growth response protein 2 promotes partial
            epithelial-mesenchymal transition by phosphorylating Smad3 during
            renal fibrosis.
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Jian,H., Feng,H., Zhu,L., Li,X. and Ma,Z.
  TITLE     MicroRNA-150-5P regulates Th1/Th2 cytokines expression levels by
            targeting EGR2 in allergic rhinitis
  JOURNAL   Rhinology 62 (2), 250-256 (2024)
   PUBMED   38165680
  REMARK    GeneRIF: MicroRNA-150-5P regulates Th1/Th2 cytokines expression
            levels by targeting EGR2 in allergic rhinitis.
REFERENCE   4  (residues 1 to 476)
  AUTHORS   .
  TITLE     EGR2 drives TH17 cell pathogenicity in autoimmune neuroinflammation
  JOURNAL   Nat Immunol 24 (8), 1230-1231 (2023)
   PUBMED   37474655
  REMARK    GeneRIF: EGR2 drives TH17 cell pathogenicity in autoimmune
            neuroinflammation.
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 4 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301641
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301384
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Rangnekar,V.M., Aplin,A.C. and Sukhatme,V.P.
  TITLE     The serum and TPA responsive promoter and intron-exon structure of
            EGR2, a human early growth response gene encoding a zinc finger
            protein
  JOURNAL   Nucleic Acids Res 18 (9), 2749-2757 (1990)
   PUBMED   2111009
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Chavrier,P., Janssen-Timmen,U., Mattei,M.G., Zerial,M., Bravo,R.
            and Charnay,P.
  TITLE     Structure, chromosome location, and expression of the mouse zinc
            finger gene Krox-20: multiple gene products and coregulation with
            the proto-oncogene c-fos
  JOURNAL   Mol Cell Biol 9 (2), 787-797 (1989)
   PUBMED   2496302
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Joseph,L.J., Le Beau,M.M., Jamieson,G.A. Jr., Acharya,S.,
            Shows,T.B., Rowley,J.D. and Sukhatme,V.P.
  TITLE     Molecular cloning, sequencing, and mapping of EGR2, a human early
            growth response gene encoding a protein with 'zinc-binding finger'
            structure
  JOURNAL   Proc Natl Acad Sci U S A 85 (19), 7164-7168 (1988)
   PUBMED   3140236
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1989 Jan;86(2):515]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133417.11 and KF459538.1.
            
            Summary: The protein encoded by this gene is a transcription factor
            with three tandem C2H2-type zinc fingers. Defects in this gene are
            associated with Charcot-Marie-Tooth disease type 1D (CMT1D),
            Charcot-Marie-Tooth disease type 4E (CMT4E), and with
            Dejerine-Sottas syndrome (DSS). Multiple transcript variants
            encoding two different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, and 3 all encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA813060.1, DB259927.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.3"
     Protein         1..476
                     /product="E3 SUMO-protein ligase EGR2 isoform a"
                     /note="KROX-20, Drosophila, homolog (early growth
                     response-2); early growth response protein 2; zinc finger
                     protein Krox-20; E3 SUMO-protein ligase EGR2; E3
                     SUMO-protein transferase ERG2"
                     /calculated_mol_wt=50171
     Region          94..188
                     /region_name="DUF3446"
                     /note="Early growth response N-terminal domain; pfam11928"
                     /db_xref="CDD:463400"
     Region          127..178
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11161.3)"
     Region          162..165
                     /region_name="HCFC1-binding-motif (HBM)"
                     /note="propagated from UniProtKB/Swiss-Prot (P11161.3)"
     Site            247
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000250|UniProtKB:P08152; propagated from
                     UniProtKB/Swiss-Prot (P11161.3)"
     Region          275..300
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11161.3)"
     Region          318..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11161.3)"
     Region          340..364
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          342..364
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(349,351,353,355..356,359..360,363,377,379,383..384,
                     387..388,391,405,407,409,411..412,415..416,419)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          368..>436
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          372..392
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          400..420
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          412..476
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11161.3)"
     CDS             1..476
                     /gene="EGR2"
                     /gene_synonym="AT591; CMT1D; CMT4E; KROX20"
                     /coded_by="NM_001136177.3:155..1585"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS7267.1"
                     /db_xref="GeneID:1959"
                     /db_xref="HGNC:HGNC:3239"
                     /db_xref="MIM:129010"
ORIGIN      
        1 mmtakavdki pvtlsgfvhq lsdniypved laatsvtifp naelggpfdq mngvagdgmi
       61 nidmtgekrs ldlpypssfa pvsaprnqtf tymgkfsidp qypgascype giinivsagi
      121 lqgvtspast tasssvtsas pnplatgplg vctmsqtqpd ldhlyspppp pppysgcagd
      181 lyqdpsafls aattstsssl ayppppsyps pkpatdpglf pmipdypgff psqcqrdlhg
      241 tagpdrkpfp cpldtlrvpp pltplstirn ftlggpsagv tgpgasggse gprlpgsssa
      301 aaaaaaaaay nphhlplrpi lrprkypnrp sktpvherpy pcpaegcdrr fsrsdeltrh
      361 irihtghkpf qcricmrnfs rsdhltthir thtgekpfac dycgrkfars derkrhtkih
      421 lrqkerkssa psasvpapst ascsggvqpg gtlcssnsss lgggplapcs srtrtp
//
LOCUS       NP_001129650             476 aa            linear   PRI 08-JAN-2026
DEFINITION  E3 SUMO-protein ligase EGR2 isoform a [Homo sapiens].
ACCESSION   NP_001129650
VERSION     NP_001129650.1
DBSOURCE    REFSEQ: accession NM_001136178.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Li,W., He,S., Tan,J., Li,N., Zhao,C., Wang,X., Zhang,Z., Liu,J.,
            Huang,J., Li,X., Zhou,Q., Hu,K., Yang,P. and Hou,S.
  TITLE     Transcription factor EGR2 alleviates autoimmune uveitis via
            activation of GDF15 to modulate the retinal microglial phenotype
  JOURNAL   Proc Natl Acad Sci U S A 121 (39), e2316161121 (2024)
   PUBMED   39298490
  REMARK    GeneRIF: Transcription factor EGR2 alleviates autoimmune uveitis
            via activation of GDF15 to modulate the retinal microglial
            phenotype.
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Song,A., Yan,R., Xiong,W., Xiang,H., Huang,J., Jiang,A. and
            Zhang,C.
  TITLE     Early growth response protein 2 promotes partial
            epithelial-mesenchymal transition by phosphorylating Smad3 during
            renal fibrosis
  JOURNAL   Transl Res 271, 13-25 (2024)
   PUBMED   38679230
  REMARK    GeneRIF: Early growth response protein 2 promotes partial
            epithelial-mesenchymal transition by phosphorylating Smad3 during
            renal fibrosis.
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Jian,H., Feng,H., Zhu,L., Li,X. and Ma,Z.
  TITLE     MicroRNA-150-5P regulates Th1/Th2 cytokines expression levels by
            targeting EGR2 in allergic rhinitis
  JOURNAL   Rhinology 62 (2), 250-256 (2024)
   PUBMED   38165680
  REMARK    GeneRIF: MicroRNA-150-5P regulates Th1/Th2 cytokines expression
            levels by targeting EGR2 in allergic rhinitis.
REFERENCE   4  (residues 1 to 476)
  AUTHORS   .
  TITLE     EGR2 drives TH17 cell pathogenicity in autoimmune neuroinflammation
  JOURNAL   Nat Immunol 24 (8), 1230-1231 (2023)
   PUBMED   37474655
  REMARK    GeneRIF: EGR2 drives TH17 cell pathogenicity in autoimmune
            neuroinflammation.
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 4 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301641
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301384
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Rangnekar,V.M., Aplin,A.C. and Sukhatme,V.P.
  TITLE     The serum and TPA responsive promoter and intron-exon structure of
            EGR2, a human early growth response gene encoding a zinc finger
            protein
  JOURNAL   Nucleic Acids Res 18 (9), 2749-2757 (1990)
   PUBMED   2111009
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Chavrier,P., Janssen-Timmen,U., Mattei,M.G., Zerial,M., Bravo,R.
            and Charnay,P.
  TITLE     Structure, chromosome location, and expression of the mouse zinc
            finger gene Krox-20: multiple gene products and coregulation with
            the proto-oncogene c-fos
  JOURNAL   Mol Cell Biol 9 (2), 787-797 (1989)
   PUBMED   2496302
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Joseph,L.J., Le Beau,M.M., Jamieson,G.A. Jr., Acharya,S.,
            Shows,T.B., Rowley,J.D. and Sukhatme,V.P.
  TITLE     Molecular cloning, sequencing, and mapping of EGR2, a human early
            growth response gene encoding a protein with 'zinc-binding finger'
            structure
  JOURNAL   Proc Natl Acad Sci U S A 85 (19), 7164-7168 (1988)
   PUBMED   3140236
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1989 Jan;86(2):515]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133417.11 and KF459538.1.
            
            Summary: The protein encoded by this gene is a transcription factor
            with three tandem C2H2-type zinc fingers. Defects in this gene are
            associated with Charcot-Marie-Tooth disease type 1D (CMT1D),
            Charcot-Marie-Tooth disease type 4E (CMT4E), and with
            Dejerine-Sottas syndrome (DSS). Multiple transcript variants
            encoding two different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, and 3 all encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK312813.1, DB086600.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2145743,
                                           SAMEA2147596 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.3"
     Protein         1..476
                     /product="E3 SUMO-protein ligase EGR2 isoform a"
                     /note="KROX-20, Drosophila, homolog (early growth
                     response-2); early growth response protein 2; zinc finger
                     protein Krox-20; E3 SUMO-protein ligase EGR2; E3
                     SUMO-protein transferase ERG2"
                     /calculated_mol_wt=50171
     Region          94..188
                     /region_name="DUF3446"
                     /note="Early growth response N-terminal domain; pfam11928"
                     /db_xref="CDD:463400"
     Region          127..178
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11161.3)"
     Region          162..165
                     /region_name="HCFC1-binding-motif (HBM)"
                     /note="propagated from UniProtKB/Swiss-Prot (P11161.3)"
     Site            247
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000250|UniProtKB:P08152; propagated from
                     UniProtKB/Swiss-Prot (P11161.3)"
     Region          275..300
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11161.3)"
     Region          318..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11161.3)"
     Region          340..420
                     /region_name="zinc finger domain"
                     /note="contains 3 tandem zinc fingers of the C2H2-type"
     Region          340..364
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          342..364
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(349,351,353,355..356,359..360,363,377,379,383..384,
                     387..388,391,405,407,409,411..412,415..416,419)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          368..>436
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          372..392
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          400..420
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          412..476
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11161.3)"
     CDS             1..476
                     /gene="EGR2"
                     /gene_synonym="AT591; CMT1D; CMT4E; KROX20"
                     /coded_by="NM_001136178.2:210..1640"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS7267.1"
                     /db_xref="GeneID:1959"
                     /db_xref="HGNC:HGNC:3239"
                     /db_xref="MIM:129010"
ORIGIN      
        1 mmtakavdki pvtlsgfvhq lsdniypved laatsvtifp naelggpfdq mngvagdgmi
       61 nidmtgekrs ldlpypssfa pvsaprnqtf tymgkfsidp qypgascype giinivsagi
      121 lqgvtspast tasssvtsas pnplatgplg vctmsqtqpd ldhlyspppp pppysgcagd
      181 lyqdpsafls aattstsssl ayppppsyps pkpatdpglf pmipdypgff psqcqrdlhg
      241 tagpdrkpfp cpldtlrvpp pltplstirn ftlggpsagv tgpgasggse gprlpgsssa
      301 aaaaaaaaay nphhlplrpi lrprkypnrp sktpvherpy pcpaegcdrr fsrsdeltrh
      361 irihtghkpf qcricmrnfs rsdhltthir thtgekpfac dycgrkfars derkrhtkih
      421 lrqkerkssa psasvpapst ascsggvqpg gtlcssnsss lgggplapcs srtrtp
//
LOCUS       NP_001307966             426 aa            linear   PRI 08-JAN-2026
DEFINITION  E3 SUMO-protein ligase EGR2 isoform b [Homo sapiens].
ACCESSION   NP_001307966 XP_011537731
VERSION     NP_001307966.1
DBSOURCE    REFSEQ: accession NM_001321037.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Li,W., He,S., Tan,J., Li,N., Zhao,C., Wang,X., Zhang,Z., Liu,J.,
            Huang,J., Li,X., Zhou,Q., Hu,K., Yang,P. and Hou,S.
  TITLE     Transcription factor EGR2 alleviates autoimmune uveitis via
            activation of GDF15 to modulate the retinal microglial phenotype
  JOURNAL   Proc Natl Acad Sci U S A 121 (39), e2316161121 (2024)
   PUBMED   39298490
  REMARK    GeneRIF: Transcription factor EGR2 alleviates autoimmune uveitis
            via activation of GDF15 to modulate the retinal microglial
            phenotype.
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Song,A., Yan,R., Xiong,W., Xiang,H., Huang,J., Jiang,A. and
            Zhang,C.
  TITLE     Early growth response protein 2 promotes partial
            epithelial-mesenchymal transition by phosphorylating Smad3 during
            renal fibrosis
  JOURNAL   Transl Res 271, 13-25 (2024)
   PUBMED   38679230
  REMARK    GeneRIF: Early growth response protein 2 promotes partial
            epithelial-mesenchymal transition by phosphorylating Smad3 during
            renal fibrosis.
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Jian,H., Feng,H., Zhu,L., Li,X. and Ma,Z.
  TITLE     MicroRNA-150-5P regulates Th1/Th2 cytokines expression levels by
            targeting EGR2 in allergic rhinitis
  JOURNAL   Rhinology 62 (2), 250-256 (2024)
   PUBMED   38165680
  REMARK    GeneRIF: MicroRNA-150-5P regulates Th1/Th2 cytokines expression
            levels by targeting EGR2 in allergic rhinitis.
REFERENCE   4  (residues 1 to 426)
  AUTHORS   .
  TITLE     EGR2 drives TH17 cell pathogenicity in autoimmune neuroinflammation
  JOURNAL   Nat Immunol 24 (8), 1230-1231 (2023)
   PUBMED   37474655
  REMARK    GeneRIF: EGR2 drives TH17 cell pathogenicity in autoimmune
            neuroinflammation.
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 4 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301641
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301384
REFERENCE   8  (residues 1 to 426)
  AUTHORS   Rangnekar,V.M., Aplin,A.C. and Sukhatme,V.P.
  TITLE     The serum and TPA responsive promoter and intron-exon structure of
            EGR2, a human early growth response gene encoding a zinc finger
            protein
  JOURNAL   Nucleic Acids Res 18 (9), 2749-2757 (1990)
   PUBMED   2111009
REFERENCE   9  (residues 1 to 426)
  AUTHORS   Chavrier,P., Janssen-Timmen,U., Mattei,M.G., Zerial,M., Bravo,R.
            and Charnay,P.
  TITLE     Structure, chromosome location, and expression of the mouse zinc
            finger gene Krox-20: multiple gene products and coregulation with
            the proto-oncogene c-fos
  JOURNAL   Mol Cell Biol 9 (2), 787-797 (1989)
   PUBMED   2496302
REFERENCE   10 (residues 1 to 426)
  AUTHORS   Joseph,L.J., Le Beau,M.M., Jamieson,G.A. Jr., Acharya,S.,
            Shows,T.B., Rowley,J.D. and Sukhatme,V.P.
  TITLE     Molecular cloning, sequencing, and mapping of EGR2, a human early
            growth response gene encoding a protein with 'zinc-binding finger'
            structure
  JOURNAL   Proc Natl Acad Sci U S A 85 (19), 7164-7168 (1988)
   PUBMED   3140236
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1989 Jan;86(2):515]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133417.11 and KF459538.1.
            
            On Mar 12, 2016 this sequence version replaced XP_011537731.1.
            
            Summary: The protein encoded by this gene is a transcription factor
            with three tandem C2H2-type zinc fingers. Defects in this gene are
            associated with Charcot-Marie-Tooth disease type 1D (CMT1D),
            Charcot-Marie-Tooth disease type 4E (CMT4E), and with
            Dejerine-Sottas syndrome (DSS). Multiple transcript variants
            encoding two different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.557705.1,
                                           SRR14038197.1825944.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.3"
     Protein         1..426
                     /product="E3 SUMO-protein ligase EGR2 isoform b"
                     /note="KROX-20, Drosophila, homolog (early growth
                     response-2); early growth response protein 2; zinc finger
                     protein Krox-20; E3 SUMO-protein ligase EGR2; E3
                     SUMO-protein transferase ERG2"
                     /calculated_mol_wt=44839
     Region          44..138
                     /region_name="DUF3446"
                     /note="Early growth response N-terminal domain; pfam11928"
                     /db_xref="CDD:463400"
     Region          290..314
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          292..314
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(299,301,303,305..306,309..310,313,327,329,333..334,
                     337..338,341,355,357,359,361..362,365..366,369)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          318..>386
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          322..342
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          350..370
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..426
                     /gene="EGR2"
                     /gene_synonym="AT591; CMT1D; CMT4E; KROX20"
                     /coded_by="NM_001321037.2:205..1485"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS44409.1"
                     /db_xref="GeneID:1959"
                     /db_xref="HGNC:HGNC:3239"
                     /db_xref="MIM:129010"
ORIGIN      
        1 mngvagdgmi nidmtgekrs ldlpypssfa pvsaprnqtf tymgkfsidp qypgascype
       61 giinivsagi lqgvtspast tasssvtsas pnplatgplg vctmsqtqpd ldhlyspppp
      121 pppysgcagd lyqdpsafls aattstsssl ayppppsyps pkpatdpglf pmipdypgff
      181 psqcqrdlhg tagpdrkpfp cpldtlrvpp pltplstirn ftlggpsagv tgpgasggse
      241 gprlpgsssa aaaaaaaaay nphhlplrpi lrprkypnrp sktpvherpy pcpaegcdrr
      301 fsrsdeltrh irihtghkpf qcricmrnfs rsdhltthir thtgekpfac dycgrkfars
      361 derkrhtkih lrqkerkssa psasvpapst ascsggvqpg gtlcssnsss lgggplapcs
      421 srtrtp
//
LOCUS       NP_001129651             426 aa            linear   PRI 08-JAN-2026
DEFINITION  E3 SUMO-protein ligase EGR2 isoform b [Homo sapiens].
ACCESSION   NP_001129651
VERSION     NP_001129651.1
DBSOURCE    REFSEQ: accession NM_001136179.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Li,W., He,S., Tan,J., Li,N., Zhao,C., Wang,X., Zhang,Z., Liu,J.,
            Huang,J., Li,X., Zhou,Q., Hu,K., Yang,P. and Hou,S.
  TITLE     Transcription factor EGR2 alleviates autoimmune uveitis via
            activation of GDF15 to modulate the retinal microglial phenotype
  JOURNAL   Proc Natl Acad Sci U S A 121 (39), e2316161121 (2024)
   PUBMED   39298490
  REMARK    GeneRIF: Transcription factor EGR2 alleviates autoimmune uveitis
            via activation of GDF15 to modulate the retinal microglial
            phenotype.
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Song,A., Yan,R., Xiong,W., Xiang,H., Huang,J., Jiang,A. and
            Zhang,C.
  TITLE     Early growth response protein 2 promotes partial
            epithelial-mesenchymal transition by phosphorylating Smad3 during
            renal fibrosis
  JOURNAL   Transl Res 271, 13-25 (2024)
   PUBMED   38679230
  REMARK    GeneRIF: Early growth response protein 2 promotes partial
            epithelial-mesenchymal transition by phosphorylating Smad3 during
            renal fibrosis.
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Jian,H., Feng,H., Zhu,L., Li,X. and Ma,Z.
  TITLE     MicroRNA-150-5P regulates Th1/Th2 cytokines expression levels by
            targeting EGR2 in allergic rhinitis
  JOURNAL   Rhinology 62 (2), 250-256 (2024)
   PUBMED   38165680
  REMARK    GeneRIF: MicroRNA-150-5P regulates Th1/Th2 cytokines expression
            levels by targeting EGR2 in allergic rhinitis.
REFERENCE   4  (residues 1 to 426)
  AUTHORS   .
  TITLE     EGR2 drives TH17 cell pathogenicity in autoimmune neuroinflammation
  JOURNAL   Nat Immunol 24 (8), 1230-1231 (2023)
   PUBMED   37474655
  REMARK    GeneRIF: EGR2 drives TH17 cell pathogenicity in autoimmune
            neuroinflammation.
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 4 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301641
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301384
REFERENCE   8  (residues 1 to 426)
  AUTHORS   Rangnekar,V.M., Aplin,A.C. and Sukhatme,V.P.
  TITLE     The serum and TPA responsive promoter and intron-exon structure of
            EGR2, a human early growth response gene encoding a zinc finger
            protein
  JOURNAL   Nucleic Acids Res 18 (9), 2749-2757 (1990)
   PUBMED   2111009
REFERENCE   9  (residues 1 to 426)
  AUTHORS   Chavrier,P., Janssen-Timmen,U., Mattei,M.G., Zerial,M., Bravo,R.
            and Charnay,P.
  TITLE     Structure, chromosome location, and expression of the mouse zinc
            finger gene Krox-20: multiple gene products and coregulation with
            the proto-oncogene c-fos
  JOURNAL   Mol Cell Biol 9 (2), 787-797 (1989)
   PUBMED   2496302
REFERENCE   10 (residues 1 to 426)
  AUTHORS   Joseph,L.J., Le Beau,M.M., Jamieson,G.A. Jr., Acharya,S.,
            Shows,T.B., Rowley,J.D. and Sukhatme,V.P.
  TITLE     Molecular cloning, sequencing, and mapping of EGR2, a human early
            growth response gene encoding a protein with 'zinc-binding finger'
            structure
  JOURNAL   Proc Natl Acad Sci U S A 85 (19), 7164-7168 (1988)
   PUBMED   3140236
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1989 Jan;86(2):515]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133417.11 and KF459538.1.
            
            Summary: The protein encoded by this gene is a transcription factor
            with three tandem C2H2-type zinc fingers. Defects in this gene are
            associated with Charcot-Marie-Tooth disease type 1D (CMT1D),
            Charcot-Marie-Tooth disease type 4E (CMT4E), and with
            Dejerine-Sottas syndrome (DSS). Multiple transcript variants
            encoding two different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (b) is
            shorter at the N-terminus compared to isoform a. Both variants 4
            and 5 encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK091399.1, SRR14038195.2254163.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.3"
     Protein         1..426
                     /product="E3 SUMO-protein ligase EGR2 isoform b"
                     /note="KROX-20, Drosophila, homolog (early growth
                     response-2); early growth response protein 2; zinc finger
                     protein Krox-20; E3 SUMO-protein ligase EGR2; E3
                     SUMO-protein transferase ERG2"
                     /calculated_mol_wt=44839
     Region          44..138
                     /region_name="DUF3446"
                     /note="Early growth response N-terminal domain; pfam11928"
                     /db_xref="CDD:463400"
     Region          290..314
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          292..314
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(299,301,303,305..306,309..310,313,327,329,333..334,
                     337..338,341,355,357,359,361..362,365..366,369)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          318..>386
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          322..342
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          350..370
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..426
                     /gene="EGR2"
                     /gene_synonym="AT591; CMT1D; CMT4E; KROX20"
                     /coded_by="NM_001136179.3:388..1668"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS44409.1"
                     /db_xref="GeneID:1959"
                     /db_xref="HGNC:HGNC:3239"
                     /db_xref="MIM:129010"
ORIGIN      
        1 mngvagdgmi nidmtgekrs ldlpypssfa pvsaprnqtf tymgkfsidp qypgascype
       61 giinivsagi lqgvtspast tasssvtsas pnplatgplg vctmsqtqpd ldhlyspppp
      121 pppysgcagd lyqdpsafls aattstsssl ayppppsyps pkpatdpglf pmipdypgff
      181 psqcqrdlhg tagpdrkpfp cpldtlrvpp pltplstirn ftlggpsagv tgpgasggse
      241 gprlpgsssa aaaaaaaaay nphhlplrpi lrprkypnrp sktpvherpy pcpaegcdrr
      301 fsrsdeltrh irihtghkpf qcricmrnfs rsdhltthir thtgekpfac dycgrkfars
      361 derkrhtkih lrqkerkssa psasvpapst ascsggvqpg gtlcssnsss lgggplapcs
      421 srtrtp
//
LOCUS       NP_000390                476 aa            linear   PRI 08-JAN-2026
DEFINITION  E3 SUMO-protein ligase EGR2 isoform a [Homo sapiens].
ACCESSION   NP_000390
VERSION     NP_000390.2
DBSOURCE    REFSEQ: accession NM_000399.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Li,W., He,S., Tan,J., Li,N., Zhao,C., Wang,X., Zhang,Z., Liu,J.,
            Huang,J., Li,X., Zhou,Q., Hu,K., Yang,P. and Hou,S.
  TITLE     Transcription factor EGR2 alleviates autoimmune uveitis via
            activation of GDF15 to modulate the retinal microglial phenotype
  JOURNAL   Proc Natl Acad Sci U S A 121 (39), e2316161121 (2024)
   PUBMED   39298490
  REMARK    GeneRIF: Transcription factor EGR2 alleviates autoimmune uveitis
            via activation of GDF15 to modulate the retinal microglial
            phenotype.
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Song,A., Yan,R., Xiong,W., Xiang,H., Huang,J., Jiang,A. and
            Zhang,C.
  TITLE     Early growth response protein 2 promotes partial
            epithelial-mesenchymal transition by phosphorylating Smad3 during
            renal fibrosis
  JOURNAL   Transl Res 271, 13-25 (2024)
   PUBMED   38679230
  REMARK    GeneRIF: Early growth response protein 2 promotes partial
            epithelial-mesenchymal transition by phosphorylating Smad3 during
            renal fibrosis.
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Jian,H., Feng,H., Zhu,L., Li,X. and Ma,Z.
  TITLE     MicroRNA-150-5P regulates Th1/Th2 cytokines expression levels by
            targeting EGR2 in allergic rhinitis
  JOURNAL   Rhinology 62 (2), 250-256 (2024)
   PUBMED   38165680
  REMARK    GeneRIF: MicroRNA-150-5P regulates Th1/Th2 cytokines expression
            levels by targeting EGR2 in allergic rhinitis.
REFERENCE   4  (residues 1 to 476)
  AUTHORS   .
  TITLE     EGR2 drives TH17 cell pathogenicity in autoimmune neuroinflammation
  JOURNAL   Nat Immunol 24 (8), 1230-1231 (2023)
   PUBMED   37474655
  REMARK    GeneRIF: EGR2 drives TH17 cell pathogenicity in autoimmune
            neuroinflammation.
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 4 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301641
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301384
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Rangnekar,V.M., Aplin,A.C. and Sukhatme,V.P.
  TITLE     The serum and TPA responsive promoter and intron-exon structure of
            EGR2, a human early growth response gene encoding a zinc finger
            protein
  JOURNAL   Nucleic Acids Res 18 (9), 2749-2757 (1990)
   PUBMED   2111009
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Chavrier,P., Janssen-Timmen,U., Mattei,M.G., Zerial,M., Bravo,R.
            and Charnay,P.
  TITLE     Structure, chromosome location, and expression of the mouse zinc
            finger gene Krox-20: multiple gene products and coregulation with
            the proto-oncogene c-fos
  JOURNAL   Mol Cell Biol 9 (2), 787-797 (1989)
   PUBMED   2496302
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Joseph,L.J., Le Beau,M.M., Jamieson,G.A. Jr., Acharya,S.,
            Shows,T.B., Rowley,J.D. and Sukhatme,V.P.
  TITLE     Molecular cloning, sequencing, and mapping of EGR2, a human early
            growth response gene encoding a protein with 'zinc-binding finger'
            structure
  JOURNAL   Proc Natl Acad Sci U S A 85 (19), 7164-7168 (1988)
   PUBMED   3140236
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1989 Jan;86(2):515]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL133417.11 and KF459538.1.
            
            On Aug 18, 2000 this sequence version replaced NP_000390.1.
            
            Summary: The protein encoded by this gene is a transcription factor
            with three tandem C2H2-type zinc fingers. Defects in this gene are
            associated with Charcot-Marie-Tooth disease type 1D (CMT1D),
            Charcot-Marie-Tooth disease type 4E (CMT4E), and with
            Dejerine-Sottas syndrome (DSS). Multiple transcript variants
            encoding two different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Variants 1, 2, and 3
            all encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749641.1, SRR1660805.72069.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154125
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000242480.4/ ENSP00000242480.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.3"
     Protein         1..476
                     /product="E3 SUMO-protein ligase EGR2 isoform a"
                     /note="KROX-20, Drosophila, homolog (early growth
                     response-2); early growth response protein 2; zinc finger
                     protein Krox-20; E3 SUMO-protein ligase EGR2; E3
                     SUMO-protein transferase ERG2"
                     /calculated_mol_wt=50171
     Region          94..188
                     /region_name="DUF3446"
                     /note="Early growth response N-terminal domain; pfam11928"
                     /db_xref="CDD:463400"
     Region          127..178
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11161.3)"
     Region          162..165
                     /region_name="HCFC1-binding-motif (HBM)"
                     /note="propagated from UniProtKB/Swiss-Prot (P11161.3)"
     Site            247
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000250|UniProtKB:P08152; propagated from
                     UniProtKB/Swiss-Prot (P11161.3)"
     Region          275..300
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11161.3)"
     Region          318..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11161.3)"
     Region          340..364
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          342..364
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(349,351,353,355..356,359..360,363,377,379,383..384,
                     387..388,391,405,407,409,411..412,415..416,419)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          368..>436
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          372..392
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          400..420
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          412..476
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11161.3)"
     CDS             1..476
                     /gene="EGR2"
                     /gene_synonym="AT591; CMT1D; CMT4E; KROX20"
                     /coded_by="NM_000399.5:338..1768"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7267.1"
                     /db_xref="GeneID:1959"
                     /db_xref="HGNC:HGNC:3239"
                     /db_xref="MIM:129010"
ORIGIN      
        1 mmtakavdki pvtlsgfvhq lsdniypved laatsvtifp naelggpfdq mngvagdgmi
       61 nidmtgekrs ldlpypssfa pvsaprnqtf tymgkfsidp qypgascype giinivsagi
      121 lqgvtspast tasssvtsas pnplatgplg vctmsqtqpd ldhlyspppp pppysgcagd
      181 lyqdpsafls aattstsssl ayppppsyps pkpatdpglf pmipdypgff psqcqrdlhg
      241 tagpdrkpfp cpldtlrvpp pltplstirn ftlggpsagv tgpgasggse gprlpgsssa
      301 aaaaaaaaay nphhlplrpi lrprkypnrp sktpvherpy pcpaegcdrr fsrsdeltrh
      361 irihtghkpf qcricmrnfs rsdhltthir thtgekpfac dycgrkfars derkrhtkih
      421 lrqkerkssa psasvpapst ascsggvqpg gtlcssnsss lgggplapcs srtrtp
//
LOCUS       NP_001308074             474 aa            linear   PRI 09-JAN-2026
DEFINITION  zinc finger protein interacting with ribonucleoprotein K isoform 2
            [Homo sapiens].
ACCESSION   NP_001308074 XP_011525062
VERSION     NP_001308074.1
DBSOURCE    REFSEQ: accession NM_001321145.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK128340.1, DB480028.2, BC103957.1 and AC003682.1.
            
            On Mar 16, 2016 this sequence version replaced XP_011525062.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.283003.1,
                                           SRR1803616.275461.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..474
                     /product="zinc finger protein interacting with
                     ribonucleoprotein K isoform 2"
                     /note="zinc finger protein interacting with
                     ribonucleoprotein K; zinc finger protein 762; zinc finger
                     protein interacting with K protein 1 homolog"
                     /calculated_mol_wt=53216
     Region          13..54
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          202..220
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          228..248
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          240..265
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          <256..436
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          256..276
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          284..304
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          312..332
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          340..360
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          368..388
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(373,375,377,379..380,383..384,387,401,403,407..408,
                     411..412,415,429,431,433,435..436,439..440,443)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          396..416
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          424..444
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          452..472
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..474
                     /gene="ZIK1"
                     /gene_synonym="ZNF762"
                     /coded_by="NM_001321145.2:213..1637"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS82407.1"
                     /db_xref="GeneID:284307"
                     /db_xref="HGNC:HGNC:33104"
                     /db_xref="MIM:621463"
ORIGIN      
        1 maaaalrapt qgcvtfedia iyfsqdewgl ldeaqrllyl evmlenfalv aslgcghgte
       61 deetpsdqnv svgvsqskag sstqktqsce mcvpvlkdil hladlpgqkp ylvgectnhh
      121 qhqkhhsakk slkrdmdras yvkcclfcms lkpfrkwevg kdlpamlrll rslvfpggkk
      181 pgtitecged irsqkshyks gecgkasrhk htpvyhprvy tgkklyecsk cgkafrgkys
      241 lvqhqrvhtg erpwecnecg kffsqtshln dhrrihtger pyecsecgkl frqnsslvdh
      301 qkihtgarpy ecsqcgksfs qkatlvkhqr vhtgerpykc gecgnsfsqs ailnqhrrih
      361 tgakpyecgq cgksfsqkat likhqrvhtg erpykcgdcg ksfsqssili qhrrihtgar
      421 pyecgqcgks fsqksgliqh qvvhtgerpy ecnkcgnsfs qcsslihhqk chnt
//
LOCUS       NP_001545                381 aa            linear   PRI 09-JAN-2026
DEFINITION  CCN family member 1 precursor [Homo sapiens].
ACCESSION   NP_001545
VERSION     NP_001545.2
DBSOURCE    REFSEQ: accession NM_001554.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Wang,C., Paiva,T.O., Speziale,P. and Dufrene,Y.F.
  TITLE     Nanomechanics of CCN1-Mediated Staphylococcus aureus Phagocytosis
  JOURNAL   Nano Lett 24 (28), 8567-8574 (2024)
   PUBMED   38959438
  REMARK    GeneRIF: Nanomechanics of CCN1-Mediated Staphylococcus aureus
            Phagocytosis.
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Kim,H., Son,S., Ko,Y., Lim,H., Lee,J., Lee,K.M. and Shin,I.
  TITLE     CYR61 confers chemoresistance by upregulating survivin expression
            in triple-negative breast cancer
  JOURNAL   Carcinogenesis 45 (7), 510-519 (2024)
   PUBMED   38446998
  REMARK    GeneRIF: CYR61 confers chemoresistance by upregulating survivin
            expression in triple-negative breast cancer.
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Hu,K., Xie,L., Wu,W., Zhang,J., Li,Y., He,J., Zhang,Y., Lu,D.,
            Koeffler,H.P., Lin,L. and Yin,D.
  TITLE     CYR61 Acts as an Intracellular Microtubule-Associated Protein and
            Coordinates Mitotic Progression via PLK1-FBW7 Pathway
  JOURNAL   Int J Biol Sci 20 (8), 3140-3155 (2024)
   PUBMED   38904029
  REMARK    GeneRIF: CYR61 Acts as an Intracellular Microtubule-Associated
            Protein and Coordinates Mitotic Progression via PLK1-FBW7 Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Li,T., Qian,Y., Li,H., Wang,T., Jiang,Q., Wang,Y., Zhu,Y., Li,S.,
            He,X., Shi,G., Su,W., Lu,Y. and Chen,Y.
  TITLE     Cellular communication network factor 1 promotes retinal leakage in
            diabetic retinopathy via inducing neutrophil stasis and neutrophil
            extracellular traps extrusion
  JOURNAL   Cell Commun Signal 22 (1), 275 (2024)
   PUBMED   38755602
  REMARK    GeneRIF: Cellular communication network factor 1 promotes retinal
            leakage in diabetic retinopathy via inducing neutrophil stasis and
            neutrophil extracellular traps extrusion.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Zhang,C., Wei,W., Tu,S., Liang,B., Li,C., Li,Y., Luo,W., Wu,Y.,
            Dai,X., Wang,Y., Zheng,L., Hao,L., Zhang,C., Luo,Z., Chen,Y.G. and
            Yan,X.
  TITLE     Upregulation of CYR61 by TGF-beta and YAP signaling exerts a
            counter-suppression of hepatocellular carcinoma
  JOURNAL   J Biol Chem 300 (4), 107208 (2024)
   PUBMED   38521502
  REMARK    GeneRIF: Upregulation of CYR61 by TGF-beta and YAP signaling exerts
            a counter-suppression of hepatocellular carcinoma.
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Schutze,N., Lechner,A., Groll,C., Siggelkow,H., Hufner,M.,
            Kohrle,J. and Jakob,F.
  TITLE     The human analog of murine cystein rich protein 61 [correction of
            16] is a 1alpha,25-dihydroxyvitamin D3 responsive immediate early
            gene in human fetal osteoblasts: regulation by cytokines, growth
            factors, and serum
  JOURNAL   Endocrinology 139 (4), 1761-1770 (1998)
   PUBMED   9528960
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Kolesnikova,T.V. and Lau,L.F.
  TITLE     Human CYR61-mediated enhancement of bFGF-induced DNA synthesis in
            human umbilical vein endothelial cells
  JOURNAL   Oncogene 16 (6), 747-754 (1998)
   PUBMED   9488038
REFERENCE   8  (residues 1 to 381)
  AUTHORS   Kireeva,M.L., Lam,S.C. and Lau,L.F.
  TITLE     Adhesion of human umbilical vein endothelial cells to the
            immediate-early gene product Cyr61 is mediated through integrin
            alphavbeta3
  JOURNAL   J Biol Chem 273 (5), 3090-3096 (1998)
   PUBMED   9446626
REFERENCE   9  (residues 1 to 381)
  AUTHORS   Jay,P., Berge-Lefranc,J.L., Marsollier,C., Mejean,C., Taviaux,S.
            and Berta,P.
  TITLE     The human growth factor-inducible immediate early gene, CYR61, maps
            to chromosome 1p
  JOURNAL   Oncogene 14 (14), 1753-1757 (1997)
   PUBMED   9135077
REFERENCE   10 (residues 1 to 381)
  AUTHORS   Genini,M., Schwalbe,P., Scholl,F.A. and Schafer,B.W.
  TITLE     Isolation of genes differentially expressed in human primary
            myoblasts and embryonal rhabdomyosarcoma
  JOURNAL   Int J Cancer 66 (4), 571-577 (1996)
   PUBMED   8635876
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA764894.1, BC009199.2 and
            BP387218.1.
            
            On Jun 9, 2003 this sequence version replaced NP_001545.1.
            
            Summary: The secreted protein encoded by this gene is growth
            factor-inducible and promotes the adhesion of endothelial cells.
            The encoded protein interacts with several integrins and with
            heparan sulfate proteoglycan. This protein also plays a role in
            cell proliferation, differentiation, angiogenesis, apoptosis, and
            extracellular matrix formation. [provided by RefSeq, Sep 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314571.1, SRR1803615.101477.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000451137.7/ ENSP00000398736.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.3"
     Protein         1..381
                     /product="CCN family member 1 precursor"
                     /note="cysteine-rich, anigogenic inducer, 61;
                     cysteine-rich heparin-binding protein 61; protein CYR61;
                     CCN family member 1; cysteine rich angiogenic inducer 61;
                     IGF-binding protein 10; insulin-like growth factor-binding
                     protein 10"
                     /calculated_mol_wt=39439
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2606
     mat_peptide     25..381
                     /product="CCN family member 1. /id=PRO_0000014398"
                     /note="propagated from UniProtKB/Swiss-Prot (O00622.1)"
                     /calculated_mol_wt=39439
     Region          26..78
                     /region_name="IGFBP"
                     /note="Insulin-like growth factor binding protein;
                     pfam00219"
                     /db_xref="CDD:459717"
     Region          100..159
                     /region_name="VWC"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00214"
                     /db_xref="CDD:214564"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (O00622.1)"
     Region          229..272
                     /region_name="TSP1_CCN"
                     /note="CCN3 Nov like TSP1 domain; pfam19035"
                     /db_xref="CDD:465952"
     Region          279..315
                     /region_name="Heparin-binding.
                     /evidence=ECO:0000250|UniProtKB:P18406"
                     /note="propagated from UniProtKB/Swiss-Prot (O00622.1)"
     Region          293..375
                     /region_name="GHB_like"
                     /note="Glycoprotein hormone beta chain homologues;
                     cl21545"
                     /db_xref="CDD:473907"
     CDS             1..381
                     /gene="CCN1"
                     /gene_synonym="CYR61; GIG1; IBP-10; IGFBP-10; IGFBP10"
                     /coded_by="NM_001554.5:225..1370"
                     /db_xref="CCDS:CCDS706.1"
                     /db_xref="GeneID:3491"
                     /db_xref="HGNC:HGNC:2654"
                     /db_xref="MIM:602369"
ORIGIN      
        1 mssriarala lvvtllhltr lalstcpaac hcpleapkca pgvglvrdgc gcckvcakql
       61 nedcsktqpc dhtkglecnf gasstalkgi craqsegrpc eynsriyqng esfqpnckhq
      121 ctcidgavgc iplcpqelsl pnlgcpnprl vkvtgqccee wvcdedsikd pmedqdgllg
      181 kelgfdasev eltrnnelia vgkgsslkrl pvfgmepril ynplqgqkci vqttswsqcs
      241 ktcgtgistr vtndnpecrl vketricevr pcgqpvyssl kkgkkcsktk kspepvrfty
      301 agclsvkkyr pkycgscvdg rcctpqltrt vkmrfrcedg etfsknvmmi qsckcnyncp
      361 haneaafpfy rlfndihkfr d
//
LOCUS       NP_001350518             192 aa            linear   PRI 09-JAN-2026
DEFINITION  deoxyribonuclease TATDN3 isoform 6 [Homo sapiens].
ACCESSION   NP_001350518 XP_011507504
VERSION     NP_001350518.1
DBSOURCE    REFSEQ: accession NM_001363589.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Dorival,J. and Eichman,B.F.
  TITLE     Human and bacterial TatD enzymes exhibit apurinic/apyrimidinic (AP)
            endonuclease activity
  JOURNAL   Nucleic Acids Res 51 (6), 2838-2849 (2023)
   PUBMED   36881763
  REMARK    GeneRIF: Human and bacterial TatD enzymes exhibit
            apurinic/apyrimidinic (AP) endonuclease activity.
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Kutsenko,A.S., Gizatullin,R.Z., Al-Amin,A.N., Wang,F., Kvasha,S.M.,
            Podowski,R.M., Matushkin,Y.G., Gyanchandani,A., Muravenko,O.V.,
            Levitsky,V.G., Kolchanov,N.A., Protopopov,A.I., Kashuba,V.I.,
            Kisselev,L.L., Wasserman,W., Wahlestedt,C. and Zabarovsky,E.R.
  TITLE     NotI flanking sequences: a tool for gene discovery and verification
            of the human genome
  JOURNAL   Nucleic Acids Res 30 (14), 3163-3170 (2002)
   PUBMED   12136098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104333.2.
            
            On May 24, 2018 this sequence version replaced XP_011507504.1.
            
            Transcript Variant: This variant (6) lacks an exon in the 3' coding
            region which causes a frameshift compared to variant 1. The encoded
            isoform (6) has a shorter and distinct C-terminus compared to
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.14347.1,
                                           SRR14038193.122591.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..192
                     /product="deoxyribonuclease TATDN3 isoform 6"
                     /note="putative deoxyribonuclease TATDN3; DNA-(apurinic or
                     apyrimidinic site) endonuclease TATDN3"
                     /calculated_mol_wt=21398
     Region          8..>161
                     /region_name="metallo-dependent_hydrolases"
                     /note="Superfamily of metallo-dependent hydrolases (also
                     called amidohydrolase superfamily) is a large group of
                     proteins that show conservation in their 3-dimensional
                     fold (TIM barrel) and in details of their active site. The
                     vast majority of the members have a...; cl00281"
                     /db_xref="CDD:469705"
     CDS             1..192
                     /gene="TATDN3"
                     /coded_by="NM_001363589.2:29..607"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:128387"
                     /db_xref="HGNC:HGNC:27010"
                     /db_xref="MIM:621462"
ORIGIN      
        1 mraagvglvd chchlsapdf drdlddvlek akkanvvalv avaehsgefe kimqlseryn
       61 gfvlpclgvh pvqglppedq rsvtlkdldv alpiienykd rllaigevgl dfsprfagtg
      121 eqkeeqrqvl irqiqlakrl nlpvnvhsrs agrptinllq eqeaetceti afnfymlrnr
      181 ftctrtrktg te
//
LOCUS       NP_001362788             598 aa            linear   PRI 09-JAN-2026
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily A containing DEAD/H box 1 isoform f [Homo
            sapiens].
ACCESSION   NP_001362788
VERSION     NP_001362788.1
DBSOURCE    REFSEQ: accession NM_001375859.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Aboulache,B.L., Hoitsma,N.M. and Luger,K.
  TITLE     Phosphorylation regulates the chromatin remodeler SMARCAD1 in
            nucleosome binding, ATP hydrolysis, and histone exchange
  JOURNAL   J Biol Chem 300 (12), 107893 (2024)
   PUBMED   39424143
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Mathews,I., Wagh,S., Baby,A., Chandrashekar,L. and Dalal,A.
  TITLE     Basan syndrome in a family from South India: a novel SMARCAD1
            variant
  JOURNAL   Clin Exp Dermatol 49 (4), 437-440 (2024)
   PUBMED   37966719
  REMARK    GeneRIF: Basan syndrome in a family from South India: a novel
            SMARCAD1 variant.
REFERENCE   3  (residues 1 to 598)
  AUTHORS   Sachs,P., Bergmaier,P., Treutwein,K. and Mermoud,J.E.
  TITLE     The Conserved Chromatin Remodeler SMARCAD1 Interacts with TFIIIC
            and Architectural Proteins in Human and Mouse
  JOURNAL   Genes (Basel) 14 (9), 1793 (2023)
   PUBMED   37761933
  REMARK    GeneRIF: The Conserved Chromatin Remodeler SMARCAD1 Interacts with
            TFIIIC and Architectural Proteins in Human and Mouse.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 598)
  AUTHORS   Oh,J.M., Kang,Y., Park,J., Sung,Y., Kim,D., Seo,Y., Lee,E.A.,
            Ra,J.S., Amarsanaa,E., Park,Y.U., Lee,S.Y., Hwang,J.M., Kim,H.,
            Scharer,O., Cho,S.W., Lee,C., Takata,K.I., Lee,J.Y. and Myung,K.
  TITLE     MSH2-MSH3 promotes DNA end resection during homologous
            recombination and blocks polymerase theta-mediated end-joining
            through interaction with SMARCAD1 and EXO1
  JOURNAL   Nucleic Acids Res 51 (11), 5584-5602 (2023)
   PUBMED   37140056
  REMARK    GeneRIF: MSH2-MSH3 promotes DNA end resection during homologous
            recombination and blocks polymerase theta-mediated end-joining
            through interaction with SMARCAD1 and EXO1.
REFERENCE   5  (residues 1 to 598)
  AUTHORS   Mermoud,J.E., Rowbotham,S.P. and Varga-Weisz,P.D.
  TITLE     Keeping chromatin quiet: how nucleosome remodeling restores
            heterochromatin after replication
  JOURNAL   Cell Cycle 10 (23), 4017-4025 (2011)
   PUBMED   22101266
  REMARK    Review article
REFERENCE   6  (residues 1 to 598)
  AUTHORS   Nousbeck,J., Burger,B., Fuchs-Telem,D., Pavlovsky,M., Fenig,S.,
            Sarig,O., Itin,P. and Sprecher,E.
  TITLE     A mutation in a skin-specific isoform of SMARCAD1 causes
            autosomal-dominant adermatoglyphia
  JOURNAL   Am J Hum Genet 89 (2), 302-307 (2011)
   PUBMED   21820097
  REMARK    GeneRIF: The existence of a short isoform of SMARCAD1 exclusively
            expressed in the skin, is demonstrated.
REFERENCE   7  (residues 1 to 598)
  AUTHORS   Rowbotham,S.P., Barki,L., Neves-Costa,A., Santos,F., Dean,W.,
            Hawkes,N., Choudhary,P., Will,W.R., Webster,J., Oxley,D.,
            Green,C.M., Varga-Weisz,P. and Mermoud,J.E.
  TITLE     Maintenance of silent chromatin through replication requires
            SWI/SNF-like chromatin remodeler SMARCAD1
  JOURNAL   Mol Cell 42 (3), 285-296 (2011)
   PUBMED   21549307
  REMARK    GeneRIF: Findings suggest that chromatin remodeling by SMARCAD1
            ensures that silenced loci, such as pericentric heterochromatin,
            are correctly perpetuated.
REFERENCE   8  (residues 1 to 598)
  AUTHORS   Okazaki,N., Ikeda,S., Ohara,R., Shimada,K., Yanagawa,T., Nagase,T.,
            Ohara,O. and Koga,H.
  TITLE     The novel protein complex with SMARCAD1/KIAA1122 binds to the
            vicinity of TSS
  JOURNAL   J Mol Biol 382 (2), 257-265 (2008)
   PUBMED   18675275
  REMARK    GeneRIF: Results suggest a novel model for gene regulation via the
            SMARCAD1/KIAA1122 protein complex.
REFERENCE   9  (residues 1 to 598)
  AUTHORS   Adra,C.N., Donato,J.L., Badovinac,R., Syed,F., Kheraj,R., Cai,H.,
            Moran,C., Kolker,M.T., Turner,H., Weremowicz,S., Shirakawa,T.,
            Morton,C.C., Schnipper,L.E. and Drews,R.
  TITLE     SMARCAD1, a novel human helicase family-defining member associated
            with genetic instability: cloning, expression, and mapping to
            4q22-q23, a band rich in breakpoints and deletion mutants involved
            in several human diseases
  JOURNAL   Genomics 69 (2), 162-173 (2000)
   PUBMED   11031099
REFERENCE   10 (residues 1 to 598)
  AUTHORS   Lee,Y.A., Stevens,H.P., Delaporte,E., Wahn,U. and Reis,A.
  TITLE     A gene for an autosomal dominant scleroatrophic syndrome
            predisposing to skin cancer (Huriez syndrome) maps to chromosome
            4q23
  JOURNAL   Am J Hum Genet 66 (1), 326-330 (2000)
   PUBMED   10631162
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC096746.3.
            
            Summary: This gene encodes a member of the SNF subfamily of
            helicase proteins. The encoded protein plays a critical role in the
            restoration of heterochromatin organization and propagation of
            epigenetic patterns following DNA replication by mediating histone
            H3/H4 deacetylation. Mutations in this gene are associated with
            adermatoglyphia. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.154346.1,
                                           SRR11853559.25002.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q22.3"
     Protein         1..598
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily A
                     containing DEAD/H box 1 isoform f"
                     /EC_number="3.6.4.12"
                     /note="SWI/SNF-related, matrix-associated actin-dependent
                     regulator of chromatin, subfamily a, containing DEAD/H box
                     1; ATP-dependent helicase 1; sclerotylosis; HPGDS
                     antisense RNA 1"
                     /calculated_mol_wt=68843
     Region          <66..569
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
     CDS             1..598
                     /gene="SMARCAD1"
                     /gene_synonym="ADERM; BASNS; ETL1; HEL1; HPGDS-AS1; HRZ;
                     TYS"
                     /coded_by="NM_001375859.1:373..2169"
                     /note="isoform f is encoded by transcript variant 10"
                     /db_xref="GeneID:56916"
                     /db_xref="HGNC:HGNC:18398"
                     /db_xref="MIM:612761"
ORIGIN      
        1 msktnglsed liwhcktliq erdvvirlmn kcedisnklt kqvtmltgng ggwnieqpsi
       61 lnqslslkpy qkvglnwlal vhkhglngil ademglgkti qaiaflayly qegnngphli
      121 vvpastidnw lrevnlwcpt lkvlcyygsq eerkqirfni hsryedynvi vttyncaiss
      181 sddrslfrrl klnyaifdeg hmlknmgsir yqhlmtinan nrllltgtpv qnnllelmsl
      241 lnfvmphmfs sstseirrmf ssktksadeq siyekeriah akqiikpfil rrvkeevlkq
      301 lppkkdriel camsekqeql ylglfnrlkk sinnlvtekn temcnvmmql rkmanhpllh
      361 rqyytaeklk emsqlmlkep thceanpdli fedmevmtdf elhvlckqyr hinnfqldmd
      421 lildsgkfrv lgcilselkq kgdrvvlfsq ftmmldilev llkhhqhryl rldgktqise
      481 rihlidefnt dmdifvflls tkagglginl tsanvvilhd idcnpyndkq aedrchrvgq
      541 tkevlvikli sqgtieesml kinqqklkle qdmttvdegd egsmpadiat llktsmgl
//
LOCUS       NP_001241878             596 aa            linear   PRI 09-JAN-2026
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily A containing DEAD/H box 1 isoform c [Homo
            sapiens].
ACCESSION   NP_001241878
VERSION     NP_001241878.1
DBSOURCE    REFSEQ: accession NM_001254949.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Aboulache,B.L., Hoitsma,N.M. and Luger,K.
  TITLE     Phosphorylation regulates the chromatin remodeler SMARCAD1 in
            nucleosome binding, ATP hydrolysis, and histone exchange
  JOURNAL   J Biol Chem 300 (12), 107893 (2024)
   PUBMED   39424143
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Mathews,I., Wagh,S., Baby,A., Chandrashekar,L. and Dalal,A.
  TITLE     Basan syndrome in a family from South India: a novel SMARCAD1
            variant
  JOURNAL   Clin Exp Dermatol 49 (4), 437-440 (2024)
   PUBMED   37966719
  REMARK    GeneRIF: Basan syndrome in a family from South India: a novel
            SMARCAD1 variant.
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Sachs,P., Bergmaier,P., Treutwein,K. and Mermoud,J.E.
  TITLE     The Conserved Chromatin Remodeler SMARCAD1 Interacts with TFIIIC
            and Architectural Proteins in Human and Mouse
  JOURNAL   Genes (Basel) 14 (9), 1793 (2023)
   PUBMED   37761933
  REMARK    GeneRIF: The Conserved Chromatin Remodeler SMARCAD1 Interacts with
            TFIIIC and Architectural Proteins in Human and Mouse.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 596)
  AUTHORS   Oh,J.M., Kang,Y., Park,J., Sung,Y., Kim,D., Seo,Y., Lee,E.A.,
            Ra,J.S., Amarsanaa,E., Park,Y.U., Lee,S.Y., Hwang,J.M., Kim,H.,
            Scharer,O., Cho,S.W., Lee,C., Takata,K.I., Lee,J.Y. and Myung,K.
  TITLE     MSH2-MSH3 promotes DNA end resection during homologous
            recombination and blocks polymerase theta-mediated end-joining
            through interaction with SMARCAD1 and EXO1
  JOURNAL   Nucleic Acids Res 51 (11), 5584-5602 (2023)
   PUBMED   37140056
  REMARK    GeneRIF: MSH2-MSH3 promotes DNA end resection during homologous
            recombination and blocks polymerase theta-mediated end-joining
            through interaction with SMARCAD1 and EXO1.
REFERENCE   5  (residues 1 to 596)
  AUTHORS   Mermoud,J.E., Rowbotham,S.P. and Varga-Weisz,P.D.
  TITLE     Keeping chromatin quiet: how nucleosome remodeling restores
            heterochromatin after replication
  JOURNAL   Cell Cycle 10 (23), 4017-4025 (2011)
   PUBMED   22101266
  REMARK    Review article
REFERENCE   6  (residues 1 to 596)
  AUTHORS   Nousbeck,J., Burger,B., Fuchs-Telem,D., Pavlovsky,M., Fenig,S.,
            Sarig,O., Itin,P. and Sprecher,E.
  TITLE     A mutation in a skin-specific isoform of SMARCAD1 causes
            autosomal-dominant adermatoglyphia
  JOURNAL   Am J Hum Genet 89 (2), 302-307 (2011)
   PUBMED   21820097
  REMARK    GeneRIF: The existence of a short isoform of SMARCAD1 exclusively
            expressed in the skin, is demonstrated.
REFERENCE   7  (residues 1 to 596)
  AUTHORS   Rowbotham,S.P., Barki,L., Neves-Costa,A., Santos,F., Dean,W.,
            Hawkes,N., Choudhary,P., Will,W.R., Webster,J., Oxley,D.,
            Green,C.M., Varga-Weisz,P. and Mermoud,J.E.
  TITLE     Maintenance of silent chromatin through replication requires
            SWI/SNF-like chromatin remodeler SMARCAD1
  JOURNAL   Mol Cell 42 (3), 285-296 (2011)
   PUBMED   21549307
  REMARK    GeneRIF: Findings suggest that chromatin remodeling by SMARCAD1
            ensures that silenced loci, such as pericentric heterochromatin,
            are correctly perpetuated.
REFERENCE   8  (residues 1 to 596)
  AUTHORS   Okazaki,N., Ikeda,S., Ohara,R., Shimada,K., Yanagawa,T., Nagase,T.,
            Ohara,O. and Koga,H.
  TITLE     The novel protein complex with SMARCAD1/KIAA1122 binds to the
            vicinity of TSS
  JOURNAL   J Mol Biol 382 (2), 257-265 (2008)
   PUBMED   18675275
  REMARK    GeneRIF: Results suggest a novel model for gene regulation via the
            SMARCAD1/KIAA1122 protein complex.
REFERENCE   9  (residues 1 to 596)
  AUTHORS   Adra,C.N., Donato,J.L., Badovinac,R., Syed,F., Kheraj,R., Cai,H.,
            Moran,C., Kolker,M.T., Turner,H., Weremowicz,S., Shirakawa,T.,
            Morton,C.C., Schnipper,L.E. and Drews,R.
  TITLE     SMARCAD1, a novel human helicase family-defining member associated
            with genetic instability: cloning, expression, and mapping to
            4q22-q23, a band rich in breakpoints and deletion mutants involved
            in several human diseases
  JOURNAL   Genomics 69 (2), 162-173 (2000)
   PUBMED   11031099
REFERENCE   10 (residues 1 to 596)
  AUTHORS   Lee,Y.A., Stevens,H.P., Delaporte,E., Wahn,U. and Reis,A.
  TITLE     A gene for an autosomal dominant scleroatrophic syndrome
            predisposing to skin cancer (Huriez syndrome) maps to chromosome
            4q23
  JOURNAL   Am J Hum Genet 66 (1), 326-330 (2000)
   PUBMED   10631162
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK301668.1, AL359929.1,
            AB032948.2 and AY008271.1.
            
            Summary: This gene encodes a member of the SNF subfamily of
            helicase proteins. The encoded protein plays a critical role in the
            restoration of heterochromatin organization and propagation of
            epigenetic patterns following DNA replication by mediating histone
            H3/H4 deacetylation. Mutations in this gene are associated with
            adermatoglyphia. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301668.1, SRR1803616.113265.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q22.3"
     Protein         1..596
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily A
                     containing DEAD/H box 1 isoform c"
                     /EC_number="3.6.4.12"
                     /note="SWI/SNF-related, matrix-associated actin-dependent
                     regulator of chromatin, subfamily a, containing DEAD/H box
                     1; ATP-dependent helicase 1; sclerotylosis; HPGDS
                     antisense RNA 1"
                     /calculated_mol_wt=68643
     Region          <66..567
                     /region_name="HepA"
                     /note="Superfamily II DNA or RNA helicase, SNF2 family
                     [Transcription, Replication, recombination, and repair];
                     COG0553"
                     /db_xref="CDD:440319"
     CDS             1..596
                     /gene="SMARCAD1"
                     /gene_synonym="ADERM; BASNS; ETL1; HEL1; HPGDS-AS1; HRZ;
                     TYS"
                     /coded_by="NM_001254949.2:373..2163"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS58914.1"
                     /db_xref="GeneID:56916"
                     /db_xref="HGNC:HGNC:18398"
                     /db_xref="MIM:612761"
ORIGIN      
        1 msktnglsed liwhcktliq erdvvirlmn kcedisnklt kqvtmltgng ggwnieqpsi
       61 lnqslslkpy qkvglnwlal vhkhglngil ademglgkti qaiaflayly qegnngphli
      121 vvpastidnw lrevnlwcpt lkvlcyygsq eerkqirfni hsryedynvi vttyncaiss
      181 sddrslfrrl klnyaifdeg hmlknmgsir yqhlmtinan nrllltgtpv qnnllelmsl
      241 lnfvmphmfs sstseirrmf ssktksadeq siyekeriah akqiikpfil rrvkeevlkq
      301 lppkkdriel camsekqeql ylglfnrlkk sinnleknte mcnvmmqlrk manhpllhrq
      361 yytaeklkem sqlmlkepth ceanpdlife dmevmtdfel hvlckqyrhi nnfqldmdli
      421 ldsgkfrvlg cilselkqkg drvvlfsqft mmldilevll khhqhrylrl dgktqiseri
      481 hlidefntdm difvfllstk agglginlts anvvilhdid cnpyndkqae drchrvgqtk
      541 evlviklisq gtieesmlki nqqklkleqd mttvdegdeg smpadiatll ktsmgl
//
LOCUS       NP_001139643             281 aa            linear   PRI 09-JAN-2026
DEFINITION  deoxyribonuclease TATDN3 isoform 5 [Homo sapiens].
ACCESSION   NP_001139643
VERSION     NP_001139643.1
DBSOURCE    REFSEQ: accession NM_001146171.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Dorival,J. and Eichman,B.F.
  TITLE     Human and bacterial TatD enzymes exhibit apurinic/apyrimidinic (AP)
            endonuclease activity
  JOURNAL   Nucleic Acids Res 51 (6), 2838-2849 (2023)
   PUBMED   36881763
  REMARK    GeneRIF: Human and bacterial TatD enzymes exhibit
            apurinic/apyrimidinic (AP) endonuclease activity.
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Kutsenko,A.S., Gizatullin,R.Z., Al-Amin,A.N., Wang,F., Kvasha,S.M.,
            Podowski,R.M., Matushkin,Y.G., Gyanchandani,A., Muravenko,O.V.,
            Levitsky,V.G., Kolchanov,N.A., Protopopov,A.I., Kashuba,V.I.,
            Kisselev,L.L., Wasserman,W., Wahlestedt,C. and Zabarovsky,E.R.
  TITLE     NotI flanking sequences: a tool for gene discovery and verification
            of the human genome
  JOURNAL   Nucleic Acids Res 30 (14), 3163-3170 (2002)
   PUBMED   12136098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK293129.1, BC143957.1, AC104333.2 and DB351940.1.
            
            Transcript Variant: This variant (5) uses an alternate in-frame
            splice site in the 3' coding region compared to variant 1. This
            results in a longer protein (isoform 5) compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1854207.1,
                                           SRR1803614.201524.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..281
                     /product="deoxyribonuclease TATDN3 isoform 5"
                     /note="putative deoxyribonuclease TATDN3; DNA-(apurinic or
                     apyrimidinic site) endonuclease TATDN3"
                     /calculated_mol_wt=30991
     Region          8..274
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
     CDS             1..281
                     /gene="TATDN3"
                     /coded_by="NM_001146171.2:29..874"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS53475.1"
                     /db_xref="GeneID:128387"
                     /db_xref="HGNC:HGNC:27010"
                     /db_xref="MIM:621462"
ORIGIN      
        1 mraagvglvd chchlsapdf drdlddvlek akkanvvalv avaehsgefe kimqlseryn
       61 gfvlpclgvh pvqglppedq rsvtlkdldv alpiienykd rllaigevgl dfsprfagtg
      121 eqkeeqrqvl irqiqlakrl nlpvnvhsrs agrptinllq eqgaekvllh afdgrpsvam
      181 egvragyffs ippsiirsgq llslfskkqk lvkqlpltsi cletdspalg pekqvrnepw
      241 nisisaeyia qvkgisveev ievttqnalk lfpklrhllq k
//
LOCUS       NP_001036018             273 aa            linear   PRI 09-JAN-2026
DEFINITION  deoxyribonuclease TATDN3 isoform 2 [Homo sapiens].
ACCESSION   NP_001036018
VERSION     NP_001036018.1
DBSOURCE    REFSEQ: accession NM_001042553.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Dorival,J. and Eichman,B.F.
  TITLE     Human and bacterial TatD enzymes exhibit apurinic/apyrimidinic (AP)
            endonuclease activity
  JOURNAL   Nucleic Acids Res 51 (6), 2838-2849 (2023)
   PUBMED   36881763
  REMARK    GeneRIF: Human and bacterial TatD enzymes exhibit
            apurinic/apyrimidinic (AP) endonuclease activity.
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Kutsenko,A.S., Gizatullin,R.Z., Al-Amin,A.N., Wang,F., Kvasha,S.M.,
            Podowski,R.M., Matushkin,Y.G., Gyanchandani,A., Muravenko,O.V.,
            Levitsky,V.G., Kolchanov,N.A., Protopopov,A.I., Kashuba,V.I.,
            Kisselev,L.L., Wasserman,W., Wahlestedt,C. and Zabarovsky,E.R.
  TITLE     NotI flanking sequences: a tool for gene discovery and verification
            of the human genome
  JOURNAL   Nucleic Acids Res 30 (14), 3163-3170 (2002)
   PUBMED   12136098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC143956.1, AC104333.2 and DB351940.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region compared to variant 1. This
            results in a shorter protein (isoform 2) compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL832248.1, SRR14038196.2101731.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..273
                     /product="deoxyribonuclease TATDN3 isoform 2"
                     /note="putative deoxyribonuclease TATDN3; DNA-(apurinic or
                     apyrimidinic site) endonuclease TATDN3"
                     /calculated_mol_wt=30074
     Region          9..264
                     /region_name="TatD_DNase"
                     /note="TatD related DNase; pfam01026"
                     /db_xref="CDD:425997"
     Site            order(12,14,147,170,217)
                     /site_type="active"
                     /db_xref="CDD:238635"
     CDS             1..273
                     /gene="TATDN3"
                     /coded_by="NM_001042553.3:29..850"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS41465.1"
                     /db_xref="GeneID:128387"
                     /db_xref="HGNC:HGNC:27010"
                     /db_xref="MIM:621462"
ORIGIN      
        1 mraagvglvd chchlsapdf drdlddvlek akkanvvalv avaehsgefe kimqlseryn
       61 gfvlpclgvh pvqglppedq rsvtlkdldv alpiienykd rllaigevgl dfsprfagtg
      121 eqkeeqrqvl irqiqlakrl nlpvnvhsrs agrptinllq eqgaekvllh afdgrpsvam
      181 egvragyffs ippsiirsgq qklvkqlplt sicletdspa lgpekqvrne pwnisisaey
      241 iaqvkgisve evievttqna lklfpklrhl lqk
//
LOCUS       NP_001030013             535 aa            linear   PRI 09-JAN-2026
DEFINITION  inositol 1,4,5-trisphosphate receptor-interacting protein-like 2
            precursor [Homo sapiens].
ACCESSION   NP_001030013 XP_091331
VERSION     NP_001030013.1
DBSOURCE    REFSEQ: accession NM_001034841.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Brandenberger,R., Wei,H., Zhang,S., Lei,S., Murage,J., Fisk,G.J.,
            Li,Y., Xu,C., Fang,R., Guegler,K., Rao,M.S., Mandalam,R.,
            Lebkowski,J. and Stanton,L.W.
  TITLE     Transcriptome characterization elucidates signaling networks that
            control human ES cell growth and differentiation
  JOURNAL   Nat Biotechnol 22 (6), 707-716 (2004)
   PUBMED   15146197
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Ota,T., Suzuki,Y., Nishikawa,T., Otsuki,T., Sugiyama,T., Irie,R.,
            Wakamatsu,A., Hayashi,K., Sato,H., Nagai,K., Kimura,K., Makita,H.,
            Sekine,M., Obayashi,M., Nishi,T., Shibahara,T., Tanaka,T.,
            Ishii,S., Yamamoto,J., Saito,K., Kawai,Y., Isono,Y., Nakamura,Y.,
            Nagahari,K., Murakami,K., Yasuda,T., Iwayanagi,T., Wagatsuma,M.,
            Shiratori,A., Sudo,H., Hosoiri,T., Kaku,Y., Kodaira,H., Kondo,H.,
            Sugawara,M., Takahashi,M., Kanda,K., Yokoi,T., Furuya,T.,
            Kikkawa,E., Omura,Y., Abe,K., Kamihara,K., Katsuta,N., Sato,K.,
            Tanikawa,M., Yamazaki,M., Ninomiya,K., Ishibashi,T., Yamashita,H.,
            Murakawa,K., Fujimori,K., Tanai,H., Kimata,M., Watanabe,M.,
            Hiraoka,S., Chiba,Y., Ishida,S., Ono,Y., Takiguchi,S., Watanabe,S.,
            Yosida,M., Hotuta,T., Kusano,J., Kanehori,K., Takahashi-Fujii,A.,
            Hara,H., Tanase,T.O., Nomura,Y., Togiya,S., Komai,F., Hara,R.,
            Takeuchi,K., Arita,M., Imose,N., Musashino,K., Yuuki,H., Oshima,A.,
            Sasaki,N., Aotsuka,S., Yoshikawa,Y., Matsunawa,H., Ichihara,T.,
            Shiohata,N., Sano,S., Moriya,S., Momiyama,H., Satoh,N., Takami,S.,
            Terashima,Y., Suzuki,O., Nakagawa,S., Senoh,A., Mizoguchi,H.,
            Goto,Y., Shimizu,F., Wakebe,H., Hishigaki,H., Watanabe,T.,
            Sugiyama,A., Takemoto,M., Kawakami,B., Yamazaki,M., Watanabe,K.,
            Kumagai,A., Itakura,S., Fukuzumi,Y., Fujimori,Y., Komiyama,M.,
            Tashiro,H., Tanigami,A., Fujiwara,T., Ono,T., Yamada,K., Fujii,Y.,
            Ozaki,K., Hirao,M., Ohmori,Y., Kawabata,A., Hikiji,T., Kobatake,N.,
            Inagaki,H., Ikema,Y., Okamoto,S., Okitani,R., Kawakami,T.,
            Noguchi,S., Itoh,T., Shigeta,K., Senba,T., Matsumura,K.,
            Nakajima,Y., Mizuno,T., Morinaga,M., Sasaki,M., Togashi,T.,
            Oyama,M., Hata,H., Watanabe,M., Komatsu,T., Mizushima-Sugano,J.,
            Satoh,T., Shirai,Y., Takahashi,Y., Nakagawa,K., Okumura,K.,
            Nagase,T., Nomura,N., Kikuchi,H., Masuho,Y., Yamashita,R.,
            Nakai,K., Yada,T., Nakamura,Y., Ohara,O., Isogai,T. and Sugano,S.
  TITLE     Complete sequencing and characterization of 21,243 full-length
            human cDNAs
  JOURNAL   Nat Genet 36 (1), 40-45 (2004)
   PUBMED   14702039
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099518.3.
            
            On Oct 19, 2005 this sequence version replaced XP_091331.3.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the functional protein.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AK097274.1, BC101751.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381440.5/ ENSP00000370849.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.3"
     Protein         1..535
                     /product="inositol 1,4,5-trisphosphate
                     receptor-interacting protein-like 2 precursor"
                     /note="inositol 1,4,5-triphosphate receptor-interacting
                     protein-like 2; inositol 1,4,5-trisphosphate receptor
                     interacting protein like 2; DANGER family member 1C"
                     /calculated_mol_wt=54289
     sig_peptide     1..38
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q3MIP1.1)"
                     /calculated_mol_wt=4176
     mat_peptide     39..535
                     /product="Inositol 1,4,5-trisphosphate
                     receptor-interacting protein-like 2. /id=PRO_0000336093"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MIP1.1)"
                     /calculated_mol_wt=54289
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3MIP1.1)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q3MIP1.1)"
     Region          163..>266
                     /region_name="Mab-21"
                     /note="Mab-21 protein nucleotidyltransferase domain;
                     pfam03281"
                     /db_xref="CDD:460873"
     Region          374..>453
                     /region_name="Mab-21_C"
                     /note="Mab-21 protein HhH/H2TH-like domain; pfam20266"
                     /db_xref="CDD:466416"
     CDS             1..535
                     /gene="ITPRIPL2"
                     /gene_synonym="D1C"
                     /coded_by="NM_001034841.4:499..2106"
                     /db_xref="CCDS:CCDS32395.1"
                     /db_xref="GeneID:162073"
                     /db_xref="HGNC:HGNC:27257"
                     /db_xref="MIM:621465"
ORIGIN      
        1 msvhytlnlr vfwplvtglc talvclyhvl rgsggaraep adgvdggfpl lkvavlllls
       61 yvllrcrhav rqrflpgspr leghaafssr hfrepglsil lesyyehevr lsphvlghsk
      121 ahvsrivgel vragrargsp glipggalal afrgdfiqvg sayeqhkirr pdsfdvlvpl
      181 rlpplvalep rslgeepala pafrgcflca lkappspsga sgghwlrdck pfadafcvdv
      241 rgrrhlsatl vlrwfqshlq rslatvrysl egrcrvtltp ggleqpptlh ilpcrtdygc
      301 crlsmavrli pavhlgdgvf lvappppplp sapllelpeg lraealwgvn tarqeqklls
      361 wlqeraapga cylkclqllk alrdlgargl dsaaatqwgr ilssyvlktv llavllrkga
      421 pgqgwdeehl grcleelvqf lrdcllrrht lfhcvlgpgg aaaevgplpk alreaapvdl
      481 laafdghare laaarllstw qrlpqllray ggprylarcp pprsqrtqgf legep
//
LOCUS       NP_714924                337 aa            linear   PRI 09-JAN-2026
DEFINITION  LIX1-like protein [Homo sapiens].
ACCESSION   NP_714924
VERSION     NP_714924.1
DBSOURCE    REFSEQ: accession NM_153713.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Nakamura,S., Kahyo,T., Tao,H., Shibata,K., Kurabe,N., Yamada,H.,
            Shinmura,K., Ohnishi,K. and Sugimura,H.
  TITLE     Novel roles for LIX1L in promoting cancer cell proliferation
            through ROS1-mediated LIX1L phosphorylation
  JOURNAL   Sci Rep 5, 13474 (2015)
   PUBMED   26310847
  REMARK    GeneRIF: LIX1L is an RNA-binding protein, with implications for
            therapeutic approaches for targeting LIX1L in LIX1L-expressing
            cancer cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Mao,Y., Kucuk,B. and Irvine,K.D.
  TITLE     Drosophila lowfat, a novel modulator of Fat signaling
  JOURNAL   Development 136 (19), 3223-3233 (2009)
   PUBMED   19710173
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK128733.1, BC035727.1 and AC243547.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR627381.1, SRR18074969.3019264.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000604000.4/ ENSP00000474487.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.1"
     Protein         1..337
                     /product="LIX1-like protein"
                     /note="Lix1 homolog-like"
                     /calculated_mol_wt=36432
     Region          1..64
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVB5.1)"
     Region          87..328
                     /region_name="LIX1"
                     /note="Limb expression 1; pfam14954"
                     /db_xref="CDD:464400"
     CDS             1..337
                     /gene="LIX1L"
                     /coded_by="NM_153713.3:91..1104"
                     /db_xref="CCDS:CCDS72873.1"
                     /db_xref="GeneID:128077"
                     /db_xref="HGNC:HGNC:28715"
                     /db_xref="MIM:621464"
ORIGIN      
        1 metmraqrlq pgvgtsgrgt lralrpgvtg aaaatatppa gpppappppa ppppplllsg
       61 apglplppga agspavlrea veavvrsfak htqgygrvnv vealqefwqm kqsrgadlkn
      121 galvvyemvp snsppyvcyv tlpggscfgs fqfcptkaea rrsaakialm nsvfnehpsr
      181 ritdefieks vsealasfng nreeadnpnt gigafrfmle snkgksmlef qelmtvfqll
      241 hwngslkamr erqcsrqevl ahyshraldd dirhqmaldw vsreqsvpga lsrelaster
      301 eldearlagk elrfhkekkd ilvlaagqlg nmhssnc
//
LOCUS       NP_001308075             432 aa            linear   PRI 09-JAN-2026
DEFINITION  zinc finger protein interacting with ribonucleoprotein K isoform 3
            [Homo sapiens].
ACCESSION   NP_001308075 XP_005258826
VERSION     NP_001308075.1
DBSOURCE    REFSEQ: accession NM_001321146.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB277510.1, BC103959.2, BC103957.1 and AC003682.1.
            
            On Mar 16, 2016 this sequence version replaced XP_005258826.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.238930.1,
                                           SRR1803611.27600.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..432
                     /product="zinc finger protein interacting with
                     ribonucleoprotein K isoform 3"
                     /note="zinc finger protein interacting with
                     ribonucleoprotein K; zinc finger protein 762; zinc finger
                     protein interacting with K protein 1 homolog"
                     /calculated_mol_wt=48514
     Region          160..178
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          186..206
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          198..223
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          <214..394
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          214..234
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          242..262
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          270..290
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          298..318
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          326..346
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(331,333,335,337..338,341..342,345,359,361,365..366,
                     369..370,373,387,389,391,393..394,397..398,401)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          354..374
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          382..402
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          410..430
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..432
                     /gene="ZIK1"
                     /gene_synonym="ZNF762"
                     /coded_by="NM_001321146.2:562..1860"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82408.1"
                     /db_xref="GeneID:284307"
                     /db_xref="HGNC:HGNC:33104"
                     /db_xref="MIM:621463"
ORIGIN      
        1 mlenfalvas lgcghgtede etpsdqnvsv gvsqskagss tqktqscemc vpvlkdilhl
       61 adlpgqkpyl vgectnhhqh qkhhsakksl krdmdrasyv kcclfcmslk pfrkwevgkd
      121 lpamlrllrs lvfpggkkpg titecgedir sqkshyksge cgkasrhkht pvyhprvytg
      181 kklyecskcg kafrgkyslv qhqrvhtger pwecnecgkf fsqtshlndh rrihtgerpy
      241 ecsecgklfr qnsslvdhqk ihtgarpyec sqcgksfsqk atlvkhqrvh tgerpykcge
      301 cgnsfsqsai lnqhrrihtg akpyecgqcg ksfsqkatli khqrvhtger pykcgdcgks
      361 fsqssiliqh rrihtgarpy ecgqcgksfs qksgliqhqv vhtgerpyec nkcgnsfsqc
      421 sslihhqkch nt
//
LOCUS       NP_001350519             191 aa            linear   PRI 09-JAN-2026
DEFINITION  deoxyribonuclease TATDN3 isoform 7 [Homo sapiens].
ACCESSION   NP_001350519 XP_016855820
VERSION     NP_001350519.1
DBSOURCE    REFSEQ: accession NM_001363590.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Dorival,J. and Eichman,B.F.
  TITLE     Human and bacterial TatD enzymes exhibit apurinic/apyrimidinic (AP)
            endonuclease activity
  JOURNAL   Nucleic Acids Res 51 (6), 2838-2849 (2023)
   PUBMED   36881763
  REMARK    GeneRIF: Human and bacterial TatD enzymes exhibit
            apurinic/apyrimidinic (AP) endonuclease activity.
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Kutsenko,A.S., Gizatullin,R.Z., Al-Amin,A.N., Wang,F., Kvasha,S.M.,
            Podowski,R.M., Matushkin,Y.G., Gyanchandani,A., Muravenko,O.V.,
            Levitsky,V.G., Kolchanov,N.A., Protopopov,A.I., Kashuba,V.I.,
            Kisselev,L.L., Wasserman,W., Wahlestedt,C. and Zabarovsky,E.R.
  TITLE     NotI flanking sequences: a tool for gene discovery and verification
            of the human genome
  JOURNAL   Nucleic Acids Res 30 (14), 3163-3170 (2002)
   PUBMED   12136098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104333.2.
            
            On May 24, 2018 this sequence version replaced XP_016855820.1.
            
            Transcript Variant: This variant (7)  uses an alternate splice site
            and lacks an exon in the 3' coding region which causes a frameshift
            compared to variant 1. The encoded isoform (7) has a shorter and
            distinct C-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.66942.1,
                                           SRR14038194.619973.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..191
                     /product="deoxyribonuclease TATDN3 isoform 7"
                     /note="putative deoxyribonuclease TATDN3; DNA-(apurinic or
                     apyrimidinic site) endonuclease TATDN3"
                     /calculated_mol_wt=21268
     Region          8..>161
                     /region_name="metallo-dependent_hydrolases"
                     /note="Superfamily of metallo-dependent hydrolases (also
                     called amidohydrolase superfamily) is a large group of
                     proteins that show conservation in their 3-dimensional
                     fold (TIM barrel) and in details of their active site. The
                     vast majority of the members have a...; cl00281"
                     /db_xref="CDD:469705"
     CDS             1..191
                     /gene="TATDN3"
                     /coded_by="NM_001363590.2:29..604"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS86050.1"
                     /db_xref="GeneID:128387"
                     /db_xref="HGNC:HGNC:27010"
                     /db_xref="MIM:621462"
ORIGIN      
        1 mraagvglvd chchlsapdf drdlddvlek akkanvvalv avaehsgefe kimqlseryn
       61 gfvlpclgvh pvqglppedq rsvtlkdldv alpiienykd rllaigevgl dfsprfagtg
      121 eqkeeqrqvl irqiqlakrl nlpvnvhsrs agrptinllq eqaetcetia fnfymlrnrf
      181 tctrtrktgt e
//
LOCUS       NP_001139642             253 aa            linear   PRI 09-JAN-2026
DEFINITION  deoxyribonuclease TATDN3 isoform 4 [Homo sapiens].
ACCESSION   NP_001139642
VERSION     NP_001139642.1
DBSOURCE    REFSEQ: accession NM_001146170.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Dorival,J. and Eichman,B.F.
  TITLE     Human and bacterial TatD enzymes exhibit apurinic/apyrimidinic (AP)
            endonuclease activity
  JOURNAL   Nucleic Acids Res 51 (6), 2838-2849 (2023)
   PUBMED   36881763
  REMARK    GeneRIF: Human and bacterial TatD enzymes exhibit
            apurinic/apyrimidinic (AP) endonuclease activity.
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Kutsenko,A.S., Gizatullin,R.Z., Al-Amin,A.N., Wang,F., Kvasha,S.M.,
            Podowski,R.M., Matushkin,Y.G., Gyanchandani,A., Muravenko,O.V.,
            Levitsky,V.G., Kolchanov,N.A., Protopopov,A.I., Kashuba,V.I.,
            Kisselev,L.L., Wasserman,W., Wahlestedt,C. and Zabarovsky,E.R.
  TITLE     NotI flanking sequences: a tool for gene discovery and verification
            of the human genome
  JOURNAL   Nucleic Acids Res 30 (14), 3163-3170 (2002)
   PUBMED   12136098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK304557.1, AC104333.2 and DB351940.1.
            
            Transcript Variant: This variant (4) lacks an in-frame exon in the
            5' coding region compared to variant 1. The encoded isoform (4) is
            shorter than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK304557.1, SRR1803617.20299.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..253
                     /product="deoxyribonuclease TATDN3 isoform 4"
                     /note="putative deoxyribonuclease TATDN3; DNA-(apurinic or
                     apyrimidinic site) endonuclease TATDN3"
                     /calculated_mol_wt=27849
     Region          9..244
                     /region_name="TatD_DNase"
                     /note="TatD related DNase; pfam01026"
                     /db_xref="CDD:425997"
     Site            order(12,14,126,149,197)
                     /site_type="active"
                     /db_xref="CDD:238635"
     CDS             1..253
                     /gene="TATDN3"
                     /coded_by="NM_001146170.2:29..790"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS53477.1"
                     /db_xref="GeneID:128387"
                     /db_xref="HGNC:HGNC:27010"
                     /db_xref="MIM:621462"
ORIGIN      
        1 mraagvglvd chchlsapdf drdlddvlek akkanvvalv avaehsgefe kimqlseryn
       61 gfvlpclgvh pvqglppedq rsvtlkvgld fsprfagtge qkeeqrqvli rqiqlakrln
      121 lpvnvhsrsa grptinllqe qgaekvllha fdgrpsvame gvragyffsi ppsiirsgqk
      181 qklvkqlplt sicletdspa lgpekqvrne pwnisisaey iaqvkgisve evievttqna
      241 lklfpklrhl lqk
//
LOCUS       NP_001010879             487 aa            linear   PRI 09-JAN-2026
DEFINITION  zinc finger protein interacting with ribonucleoprotein K isoform 1
            [Homo sapiens].
ACCESSION   NP_001010879 XP_209111
VERSION     NP_001010879.2
DBSOURCE    REFSEQ: accession NM_001010879.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK092538.1, BC103958.1 and AC003682.1.
            
            On Oct 16, 2005 this sequence version replaced NP_001010879.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.241080.1,
                                           SRR1803614.212101.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000597850.2/ ENSP00000472867.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..487
                     /product="zinc finger protein interacting with
                     ribonucleoprotein K isoform 1"
                     /note="zinc finger protein interacting with
                     ribonucleoprotein K; zinc finger protein 762; zinc finger
                     protein interacting with K protein 1 homolog"
                     /calculated_mol_wt=54655
     Region          26..67
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          71..94
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SY52.1)"
     Region          215..233
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          241..261
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          253..278
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          <269..449
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          269..289
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          297..317
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          325..345
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          353..373
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          381..401
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(386,388,390,392..393,396..397,400,414,416,420..421,
                     424..425,428,442,444,446,448..449,452..453,456)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          409..429
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          437..457
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          465..485
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..487
                     /gene="ZIK1"
                     /gene_synonym="ZNF762"
                     /coded_by="NM_001010879.4:213..1676"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33135.1"
                     /db_xref="GeneID:284307"
                     /db_xref="HGNC:HGNC:33104"
                     /db_xref="MIM:621463"
ORIGIN      
        1 maaaalrapt qvtvspethm dltkgcvtfe diaiyfsqde wglldeaqrl lylevmlenf
       61 alvaslgcgh gtedeetpsd qnvsvgvsqs kagsstqktq scemcvpvlk dilhladlpg
      121 qkpylvgect nhhqhqkhhs akkslkrdmd rasyvkcclf cmslkpfrkw evgkdlpaml
      181 rllrslvfpg gkkpgtitec gedirsqksh yksgecgkas rhkhtpvyhp rvytgkklye
      241 cskcgkafrg kyslvqhqrv htgerpwecn ecgkffsqts hlndhrriht gerpyecsec
      301 gklfrqnssl vdhqkihtga rpyecsqcgk sfsqkatlvk hqrvhtgerp ykcgecgnsf
      361 sqsailnqhr rihtgakpye cgqcgksfsq katlikhqrv htgerpykcg dcgksfsqss
      421 iliqhrriht garpyecgqc gksfsqksgl iqhqvvhtge rpyecnkcgn sfsqcsslih
      481 hqkchnt
//
LOCUS       NP_001431988             257 aa            linear   PRI 09-JAN-2026
DEFINITION  RPS19-CD79A readthrough [Homo sapiens].
ACCESSION   NP_001431988
VERSION     NP_001431988.1
DBSOURCE    REFSEQ: accession NM_001445059.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC243967.3.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..257
                     /product="RPS19-CD79A readthrough"
                     /calculated_mol_wt=28798
     Region          5..>57
                     /region_name="Ribosomal_S19e"
                     /note="Ribosomal protein S19e; cl00969"
                     /db_xref="CDD:470014"
     Region          70..156
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          81..85
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          94..98
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          120..124
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          134..139
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          216..236
                     /region_name="ITAM"
                     /note="Immunoreceptor tyrosine-based activation motif;
                     smart00077"
                     /db_xref="CDD:128390"
     CDS             1..257
                     /gene="RPS19-CD79A"
                     /coded_by="NM_001445059.1:36..809"
                     /db_xref="GeneID:144667541"
ORIGIN      
        1 mpgvtvkdvn qqefvralaa flkksgklkv pewvdtvkla khkelapyde nwfytragpg
       61 cqalwmhkvp aslmvslged ahfqcphnss nnanvtwwrv lhgnytwppe flgpgedpng
      121 tliiqnvnks hggiyvcrvq egnesyqqsc gtylrvrqpp prpfldmgeg tknriitaeg
      181 iillfcavvp gtlllfrkrw qneklgldag deyedenlye glnlddcsmy edisrglqgt
      241 yqdvgslnig dvqlekp
//
LOCUS       NP_001139641             240 aa            linear   PRI 09-JAN-2026
DEFINITION  deoxyribonuclease TATDN3 isoform 3 [Homo sapiens].
ACCESSION   NP_001139641
VERSION     NP_001139641.1
DBSOURCE    REFSEQ: accession NM_001146169.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Dorival,J. and Eichman,B.F.
  TITLE     Human and bacterial TatD enzymes exhibit apurinic/apyrimidinic (AP)
            endonuclease activity
  JOURNAL   Nucleic Acids Res 51 (6), 2838-2849 (2023)
   PUBMED   36881763
  REMARK    GeneRIF: Human and bacterial TatD enzymes exhibit
            apurinic/apyrimidinic (AP) endonuclease activity.
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Kutsenko,A.S., Gizatullin,R.Z., Al-Amin,A.N., Wang,F., Kvasha,S.M.,
            Podowski,R.M., Matushkin,Y.G., Gyanchandani,A., Muravenko,O.V.,
            Levitsky,V.G., Kolchanov,N.A., Protopopov,A.I., Kashuba,V.I.,
            Kisselev,L.L., Wasserman,W., Wahlestedt,C. and Zabarovsky,E.R.
  TITLE     NotI flanking sequences: a tool for gene discovery and verification
            of the human genome
  JOURNAL   Nucleic Acids Res 30 (14), 3163-3170 (2002)
   PUBMED   12136098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC143957.1, AC104333.2 and DB351940.1.
            
            Transcript Variant: This variant (3) uses two alternate splice
            sites in the 3' coding region compared to variant 1, one of which
            results in a frameshift. The encoded isoform (3) has a shorter and
            distinct C-terminus compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143957.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..240
                     /product="deoxyribonuclease TATDN3 isoform 3"
                     /note="putative deoxyribonuclease TATDN3; DNA-(apurinic or
                     apyrimidinic site) endonuclease TATDN3"
                     /calculated_mol_wt=26327
     Region          8..233
                     /region_name="TatD_DNAse"
                     /note="TatD like proteins; E.coli TatD is a cytoplasmic
                     protein, shown to have magnesium dependent DNase activity;
                     cd01310"
                     /db_xref="CDD:238635"
     Site            order(12,14,147,170,225)
                     /site_type="active"
                     /db_xref="CDD:238635"
     CDS             1..240
                     /gene="TATDN3"
                     /coded_by="NM_001146169.2:29..751"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS53476.1"
                     /db_xref="GeneID:128387"
                     /db_xref="HGNC:HGNC:27010"
                     /db_xref="MIM:621462"
ORIGIN      
        1 mraagvglvd chchlsapdf drdlddvlek akkanvvalv avaehsgefe kimqlseryn
       61 gfvlpclgvh pvqglppedq rsvtlkdldv alpiienykd rllaigevgl dfsprfagtg
      121 eqkeeqrqvl irqiqlakrl nlpvnvhsrs agrptinllq eqgaekvllh afdgrpsvam
      181 egvragyffs ippsiirsgq llslfskkqk lvkqlpltsi cletdspalg pekqqnilpr
//
LOCUS       NP_001308076             384 aa            linear   PRI 09-JAN-2026
DEFINITION  zinc finger protein interacting with ribonucleoprotein K isoform 4
            [Homo sapiens].
ACCESSION   NP_001308076
VERSION     NP_001308076.1
DBSOURCE    REFSEQ: accession NM_001321147.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 384)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA101277.1, DN993640.1, BC103957.1 and AC003682.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.173558.1,
                                           SRR1803611.158972.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145240, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..384
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..384
                     /product="zinc finger protein interacting with
                     ribonucleoprotein K isoform 4"
                     /note="zinc finger protein interacting with
                     ribonucleoprotein K; zinc finger protein 762; zinc finger
                     protein interacting with K protein 1 homolog"
                     /calculated_mol_wt=43587
     Region          112..130
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          138..158
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          150..175
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          <166..346
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          166..186
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          194..214
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          222..242
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          250..270
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          278..298
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(283,285,287,289..290,293..294,297,311,313,317..318,
                     321..322,325,339,341,343,345..346,349..350,353)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          306..326
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          334..354
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          362..382
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..384
                     /gene="ZIK1"
                     /gene_synonym="ZNF762"
                     /coded_by="NM_001321147.2:356..1510"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:284307"
                     /db_xref="HGNC:HGNC:33104"
                     /db_xref="MIM:621463"
ORIGIN      
        1 mcvpvlkdil hladlpgqkp ylvgectnhh qhqkhhsakk slkrdmdras yvkcclfcms
       61 lkpfrkwevg kdlpamlrll rslvfpggkk pgtitecged irsqkshyks gecgkasrhk
      121 htpvyhprvy tgkklyecsk cgkafrgkys lvqhqrvhtg erpwecnecg kffsqtshln
      181 dhrrihtger pyecsecgkl frqnsslvdh qkihtgarpy ecsqcgksfs qkatlvkhqr
      241 vhtgerpykc gecgnsfsqs ailnqhrrih tgakpyecgq cgksfsqkat likhqrvhtg
      301 erpykcgdcg ksfsqssili qhrrihtgar pyecgqcgks fsqksgliqh qvvhtgerpy
      361 ecnkcgnsfs qcsslihhqk chnt
//
LOCUS       NP_001036017             274 aa            linear   PRI 09-JAN-2026
DEFINITION  deoxyribonuclease TATDN3 isoform 1 [Homo sapiens].
ACCESSION   NP_001036017 XP_375838 XP_936950 XP_942805 XP_948501
VERSION     NP_001036017.1
DBSOURCE    REFSEQ: accession NM_001042552.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Dorival,J. and Eichman,B.F.
  TITLE     Human and bacterial TatD enzymes exhibit apurinic/apyrimidinic (AP)
            endonuclease activity
  JOURNAL   Nucleic Acids Res 51 (6), 2838-2849 (2023)
   PUBMED   36881763
  REMARK    GeneRIF: Human and bacterial TatD enzymes exhibit
            apurinic/apyrimidinic (AP) endonuclease activity.
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Kutsenko,A.S., Gizatullin,R.Z., Al-Amin,A.N., Wang,F., Kvasha,S.M.,
            Podowski,R.M., Matushkin,Y.G., Gyanchandani,A., Muravenko,O.V.,
            Levitsky,V.G., Kolchanov,N.A., Protopopov,A.I., Kashuba,V.I.,
            Kisselev,L.L., Wasserman,W., Wahlestedt,C. and Zabarovsky,E.R.
  TITLE     NotI flanking sequences: a tool for gene discovery and verification
            of the human genome
  JOURNAL   Nucleic Acids Res 30 (14), 3163-3170 (2002)
   PUBMED   12136098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC113638.1, AC104333.2 and DB351940.1.
            
            On or before Sep 20, 2006 this sequence version replaced
            XP_936950.1, XP_375838.1, XP_948501.1, XP_942805.1.
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.49027.1,
                                           SRR3476690.409040.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366974.9/ ENSP00000355941.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..274
                     /product="deoxyribonuclease TATDN3 isoform 1"
                     /note="putative deoxyribonuclease TATDN3; DNA-(apurinic or
                     apyrimidinic site) endonuclease TATDN3"
                     /calculated_mol_wt=30202
     Region          8..267
                     /region_name="TatD"
                     /note="3'->5' ssDNA/RNA exonuclease TatD [Cell motility];
                     COG0084"
                     /db_xref="CDD:439854"
     CDS             1..274
                     /gene="TATDN3"
                     /coded_by="NM_001042552.3:29..853"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31019.1"
                     /db_xref="GeneID:128387"
                     /db_xref="HGNC:HGNC:27010"
                     /db_xref="MIM:621462"
ORIGIN      
        1 mraagvglvd chchlsapdf drdlddvlek akkanvvalv avaehsgefe kimqlseryn
       61 gfvlpclgvh pvqglppedq rsvtlkdldv alpiienykd rllaigevgl dfsprfagtg
      121 eqkeeqrqvl irqiqlakrl nlpvnvhsrs agrptinllq eqgaekvllh afdgrpsvam
      181 egvragyffs ippsiirsgq kqklvkqlpl tsicletdsp algpekqvrn epwnisisae
      241 yiaqvkgisv eevievttqn alklfpklrh llqk
//
LOCUS       NP_001397683             273 aa            linear   PRI 09-JAN-2026
DEFINITION  COUP transcription factor 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001397683 XP_016865286
VERSION     NP_001397683.1
DBSOURCE    REFSEQ: accession NM_001410754.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Zhang,K., Zhang,H., Wang,B., Gao,S., Sun,C., Jia,C. and Cui,J.
  TITLE     NR2F1 overexpression alleviates trophoblast cell dysfunction by
            inhibiting GDF15/MAPK axis in preeclampsia
  JOURNAL   Hum Cell 37 (5), 1405-1420 (2024)
   PUBMED   39007956
  REMARK    GeneRIF: NR2F1 overexpression alleviates trophoblast cell
            dysfunction by inhibiting GDF15/MAPK axis in preeclampsia.
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Tran,T.T.T. and Hung,J.J.
  TITLE     PTEN decreases NR2F1 expression to inhibit ciliogenesis during
            EGFRL858R-induced lung cancer progression
  JOURNAL   Cell Death Dis 15 (3), 225 (2024)
   PUBMED   38499532
  REMARK    GeneRIF: PTEN decreases NR2F1 expression to inhibit ciliogenesis
            during EGFR[L858R]-induced lung cancer progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Liang,Y., Wan,L., Liu,X., Zhang,J., Zhu,G. and Yang,G.
  TITLE     Infantile epileptic spasm syndrome as a new NR2F1 gene phenotype
  JOURNAL   Int J Dev Neurosci 84 (1), 75-83 (2024)
   PUBMED   38010976
  REMARK    GeneRIF: Infantile epileptic spasm syndrome as a new NR2F1 gene
            phenotype.
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Santo,M., Rigoldi,L., Falcone,C., Tuccillo,M., Calabrese,M.,
            Martinez-Cerdeno,V. and Mallamaci,A.
  TITLE     Spatial control of astrogenesis progression by cortical
            arealization genes
  JOURNAL   Cereb Cortex 33 (6), 3107-3123 (2023)
   PUBMED   35818636
  REMARK    GeneRIF: Spatial control of astrogenesis progression by cortical
            arealization genes.
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Meng,J., Liu,X., Tang,S., Liu,Y., Zhao,C., Zhou,Q., Li,N. and
            Hou,S.
  TITLE     METTL3 inhibits inflammation of retinal pigment epithelium cells by
            regulating NR2F1 in an m6A-dependent manner
  JOURNAL   Front Immunol 13, 905211 (2022)
   PUBMED   35936005
  REMARK    GeneRIF: METTL3 inhibits inflammation of retinal pigment epithelium
            cells by regulating NR2F1 in an m(6)A-dependent manner.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Schaaf,C.P., Yu-Wai-Man,P. and Valentin,I.
  TITLE     NR2F1-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36508512
REFERENCE   7  (residues 1 to 273)
  AUTHORS   Ing,N.H., Beekman,J.M., Tsai,S.Y., Tsai,M.J. and O'Malley,B.W.
  TITLE     Members of the steroid hormone receptor superfamily interact with
            TFIIB (S300-II)
  JOURNAL   J Biol Chem 267 (25), 17617-17623 (1992)
   PUBMED   1517211
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Berrodin,T.J., Marks,M.S., Ozato,K., Linney,E. and Lazar,M.A.
  TITLE     Heterodimerization among thyroid hormone receptor, retinoic acid
            receptor, retinoid X receptor, chicken ovalbumin upstream promoter
            transcription factor, and an endogenous liver protein
  JOURNAL   Mol Endocrinol 6 (9), 1468-1478 (1992)
   PUBMED   1331778
REFERENCE   9  (residues 1 to 273)
  AUTHORS   Kliewer,S.A., Umesono,K., Heyman,R.A., Mangelsdorf,D.J., Dyck,J.A.
            and Evans,R.M.
  TITLE     Retinoid X receptor-COUP-TF interactions modulate retinoic acid
            signaling
  JOURNAL   Proc Natl Acad Sci U S A 89 (4), 1448-1452 (1992)
   PUBMED   1311101
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Wang,L.H., Tsai,S.Y., Cook,R.G., Beattie,W.G., Tsai,M.J. and
            O'Malley,B.W.
  TITLE     COUP transcription factor is a member of the steroid receptor
            superfamily
  JOURNAL   Nature 340 (6229), 163-166 (1989)
   PUBMED   2739739
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106818.2.
            
            On Aug 15, 2022 this sequence version replaced XP_016865286.1.
            
            Summary: The protein encoded by this gene is a nuclear hormone
            receptor and transcriptional regulator. The encoded protein acts as
            a homodimer and binds to 5'-AGGTCA-3' repeats. Defects in this gene
            are a cause of Bosch-Boonstra optic atrophy syndrome (BBOAS).
            [provided by RefSeq, Apr 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4281182.1,
                                           ERR4352444.788015.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q15"
     Protein         1..273
                     /product="COUP transcription factor 1 isoform 2"
                     /note="transcription factor COUP 1 (chicken ovalbumin
                     upstream promoter 1, v-erb-a homolog-like 3); COUP-TF1;
                     COUP-TF I; V-erbA-related protein 3; COUP transcription
                     factor I; chicken ovalbumin upstream
                     promoter-transcription factor I"
                     /calculated_mol_wt=30365
     Region          34..269
                     /region_name="NR_LBD_COUP-TF"
                     /note="Ligand binding domain of chicken ovalbumin upstream
                     promoter transcription factors, a member of the nuclear
                     receptor family; cd06948"
                     /db_xref="CDD:132746"
     Site            order(68..69,73,107,111,114,128,149)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:132746"
     Site            order(78,81,85,90,95..96,98..99,102..103)
                     /site_type="active"
                     /note="putative coactivator recognition site [active]"
                     /db_xref="CDD:132746"
     CDS             1..273
                     /gene="NR2F1"
                     /gene_synonym="BBOAS; BBSOAS; COUP-TFI; COUPTF1; EAR-3;
                     EAR3; ERBAL3; SVP44; TCFCOUP1; TFCOUP1"
                     /coded_by="NM_001410754.1:133..954"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS93743.1"
                     /db_xref="GeneID:7025"
                     /db_xref="HGNC:HGNC:7975"
                     /db_xref="MIM:132890"
ORIGIN      
        1 mfgysvqrgr mpptqpnpgq yaltngdpln ghcylsgyis lllraepypt srygsqcmqp
       61 nnimgienic elaarllfsa vewarnipff pdlqitdqvs llrltwself vlnaaqcsmp
      121 lhvapllaaa glhaspmsad rvvafmdhir ifqeqveklk alhvdsaeys clkaivlfts
      181 dacglsdaah ieslqeksqc aleeyvrsqy pnqpsrfgkl llrlpslrtv sssvieqlff
      241 vrlvgktpie tlirdmllsg ssfnwpymsi qcs
//
LOCUS       NP_005645                423 aa            linear   PRI 09-JAN-2026
DEFINITION  COUP transcription factor 1 isoform 1 [Homo sapiens].
ACCESSION   NP_005645
VERSION     NP_005645.1
DBSOURCE    REFSEQ: accession NM_005654.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Zhang,K., Zhang,H., Wang,B., Gao,S., Sun,C., Jia,C. and Cui,J.
  TITLE     NR2F1 overexpression alleviates trophoblast cell dysfunction by
            inhibiting GDF15/MAPK axis in preeclampsia
  JOURNAL   Hum Cell 37 (5), 1405-1420 (2024)
   PUBMED   39007956
  REMARK    GeneRIF: NR2F1 overexpression alleviates trophoblast cell
            dysfunction by inhibiting GDF15/MAPK axis in preeclampsia.
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Tran,T.T.T. and Hung,J.J.
  TITLE     PTEN decreases NR2F1 expression to inhibit ciliogenesis during
            EGFRL858R-induced lung cancer progression
  JOURNAL   Cell Death Dis 15 (3), 225 (2024)
   PUBMED   38499532
  REMARK    GeneRIF: PTEN decreases NR2F1 expression to inhibit ciliogenesis
            during EGFR[L858R]-induced lung cancer progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Liang,Y., Wan,L., Liu,X., Zhang,J., Zhu,G. and Yang,G.
  TITLE     Infantile epileptic spasm syndrome as a new NR2F1 gene phenotype
  JOURNAL   Int J Dev Neurosci 84 (1), 75-83 (2024)
   PUBMED   38010976
  REMARK    GeneRIF: Infantile epileptic spasm syndrome as a new NR2F1 gene
            phenotype.
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Santo,M., Rigoldi,L., Falcone,C., Tuccillo,M., Calabrese,M.,
            Martinez-Cerdeno,V. and Mallamaci,A.
  TITLE     Spatial control of astrogenesis progression by cortical
            arealization genes
  JOURNAL   Cereb Cortex 33 (6), 3107-3123 (2023)
   PUBMED   35818636
  REMARK    GeneRIF: Spatial control of astrogenesis progression by cortical
            arealization genes.
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Meng,J., Liu,X., Tang,S., Liu,Y., Zhao,C., Zhou,Q., Li,N. and
            Hou,S.
  TITLE     METTL3 inhibits inflammation of retinal pigment epithelium cells by
            regulating NR2F1 in an m6A-dependent manner
  JOURNAL   Front Immunol 13, 905211 (2022)
   PUBMED   35936005
  REMARK    GeneRIF: METTL3 inhibits inflammation of retinal pigment epithelium
            cells by regulating NR2F1 in an m(6)A-dependent manner.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Schaaf,C.P., Yu-Wai-Man,P. and Valentin,I.
  TITLE     NR2F1-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36508512
REFERENCE   7  (residues 1 to 423)
  AUTHORS   Ing,N.H., Beekman,J.M., Tsai,S.Y., Tsai,M.J. and O'Malley,B.W.
  TITLE     Members of the steroid hormone receptor superfamily interact with
            TFIIB (S300-II)
  JOURNAL   J Biol Chem 267 (25), 17617-17623 (1992)
   PUBMED   1517211
REFERENCE   8  (residues 1 to 423)
  AUTHORS   Berrodin,T.J., Marks,M.S., Ozato,K., Linney,E. and Lazar,M.A.
  TITLE     Heterodimerization among thyroid hormone receptor, retinoic acid
            receptor, retinoid X receptor, chicken ovalbumin upstream promoter
            transcription factor, and an endogenous liver protein
  JOURNAL   Mol Endocrinol 6 (9), 1468-1478 (1992)
   PUBMED   1331778
REFERENCE   9  (residues 1 to 423)
  AUTHORS   Kliewer,S.A., Umesono,K., Heyman,R.A., Mangelsdorf,D.J., Dyck,J.A.
            and Evans,R.M.
  TITLE     Retinoid X receptor-COUP-TF interactions modulate retinoic acid
            signaling
  JOURNAL   Proc Natl Acad Sci U S A 89 (4), 1448-1452 (1992)
   PUBMED   1311101
REFERENCE   10 (residues 1 to 423)
  AUTHORS   Wang,L.H., Tsai,S.Y., Cook,R.G., Beattie,W.G., Tsai,M.J. and
            O'Malley,B.W.
  TITLE     COUP transcription factor is a member of the steroid receptor
            superfamily
  JOURNAL   Nature 340 (6229), 163-166 (1989)
   PUBMED   2739739
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106818.2, BC017493.1 and
            AF087978.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a nuclear hormone
            receptor and transcriptional regulator. The encoded protein acts as
            a homodimer and binds to 5'-AGGTCA-3' repeats. Defects in this gene
            are a cause of Bosch-Boonstra optic atrophy syndrome (BBOAS).
            [provided by RefSeq, Apr 2014].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017493.1, SRR3476690.165042.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327111.8/ ENSP00000325819.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q15"
     Protein         1..423
                     /product="COUP transcription factor 1 isoform 1"
                     /note="transcription factor COUP 1 (chicken ovalbumin
                     upstream promoter 1, v-erb-a homolog-like 3); COUP-TF1;
                     COUP-TF I; V-erbA-related protein 3; COUP transcription
                     factor I; chicken ovalbumin upstream
                     promoter-transcription factor I"
                     /calculated_mol_wt=46025
     Region          1..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10589.1)"
     Region          86..158
                     /region_name="NR_DBD_COUP_TF"
                     /note="DNA-binding domain of chicken ovalbumin upstream
                     promoter transcription factors (COUP-TFs) is composed of
                     two C4-type zinc fingers; cd06958"
                     /db_xref="CDD:143516"
     Site            order(86,89,103,106,122,128,138,141)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143516"
     Site            order(95..98,104..105,107,109,112,115,123,135..136,139,
                     142,153)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143516"
     Region          184..419
                     /region_name="NR_LBD_COUP-TF"
                     /note="Ligand binding domain of chicken ovalbumin upstream
                     promoter transcription factors, a member of the nuclear
                     receptor family; cd06948"
                     /db_xref="CDD:132746"
     Site            order(218..219,223,257,261,264,278,299)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:132746"
     Site            order(228,231,235,240,245..246,248..249,252..253)
                     /site_type="active"
                     /note="putative coactivator recognition site [active]"
                     /db_xref="CDD:132746"
     CDS             1..423
                     /gene="NR2F1"
                     /gene_synonym="BBOAS; BBSOAS; COUP-TFI; COUPTF1; EAR-3;
                     EAR3; ERBAL3; SVP44; TCFCOUP1; TFCOUP1"
                     /coded_by="NM_005654.6:1803..3074"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4068.1"
                     /db_xref="GeneID:7025"
                     /db_xref="HGNC:HGNC:7975"
                     /db_xref="MIM:132890"
ORIGIN      
        1 mamvvsswrd pqddvaggnp ggpnpaaqaa rgggggageq qqqagsgaph tpqtpgqpga
       61 patpgtagdk gqgppgsgqs qqhiecvvcg dkssgkhygq ftcegcksff krsvrrnlty
      121 tcranrncpi dqhhrnqcqy crlkkclkvg mrreavqrgr mpptqpnpgq yaltngdpln
      181 ghcylsgyis lllraepypt srygsqcmqp nnimgienic elaarllfsa vewarnipff
      241 pdlqitdqvs llrltwself vlnaaqcsmp lhvapllaaa glhaspmsad rvvafmdhir
      301 ifqeqveklk alhvdsaeys clkaivlfts dacglsdaah ieslqeksqc aleeyvrsqy
      361 pnqpsrfgkl llrlpslrtv sssvieqlff vrlvgktpie tlirdmllsg ssfnwpymsi
      421 qcs
//
LOCUS       NP_004047                290 aa            linear   PRI 11-JAN-2026
DEFINITION  carbonic anhydrase-related protein isoform a [Homo sapiens].
ACCESSION   NP_004047
VERSION     NP_004047.3
DBSOURCE    REFSEQ: accession NM_004056.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Wu,C.Y., Yu,J.Y., Chen,Y.S., Chang,H.P., Hsieh,B.Y., Lin,Y.H.,
            Ma,C.Y., Tsai,S.F. and Hsieh,M.
  TITLE     Effects of down-regulated carbonic anhydrase 8 on cell survival and
            glucose metabolism in human colorectal cancer cell lines
  JOURNAL   Cell Biochem Funct 42 (3), e4001 (2024)
   PUBMED   38571370
  REMARK    GeneRIF: Effects of down-regulated carbonic anhydrase 8 on cell
            survival and glucose metabolism in human colorectal cancer cell
            lines.
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Lin,G.Y., Ma,C.Y., Kuo,L.C., Hsieh,B.Y., Wang,H., Liu,C.S. and
            Hsieh,M.
  TITLE     Altered glucose metabolism and its association with carbonic
            anhydrase 8 in Machado-Joseph Disease
  JOURNAL   Metab Brain Dis 37 (6), 2103-2120 (2022)
   PUBMED   35488942
  REMARK    GeneRIF: Altered glucose metabolism and its association with
            carbonic anhydrase 8 in Machado-Joseph Disease.
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Hiepp,L., Mayr,D., Gartner,K., Schmoeckel,E., Klauschen,F.,
            Burges,A., Mahner,S., Zeidler,R. and Czogalla,B.
  TITLE     Carbonic anhydrase XII as biomarker and therapeutic target in
            ovarian carcinomas
  JOURNAL   PLoS One 17 (7), e0271630 (2022)
   PUBMED   35901081
  REMARK    GeneRIF: Carbonic anhydrase XII as biomarker and therapeutic target
            in ovarian carcinomas.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Wang,T.K., Lin,Y.M., Lo,C.M., Tang,C.H., Teng,C.L., Chao,W.T.,
            Wu,M.H., Liu,C.S. and Hsieh,M.
  TITLE     Oncogenic roles of carbonic anhydrase 8 in human osteosarcoma cells
  JOURNAL   Tumour Biol 37 (6), 7989-8005 (2016)
   PUBMED   26711783
  REMARK    GeneRIF: we observed increased expression of CA8 in more aggressive
            types of human osteosarcoma (OS) cells and found that CA8
            expression is correlated with disease stages, such that more
            intense expression occurs in the disease late stage
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Turkmen,S., Guo,G., Garshasbi,M., Hoffmann,K., Alshalah,A.J.,
            Mischung,C., Kuss,A., Humphrey,N., Mundlos,S. and Robinson,P.N.
  TITLE     CA8 mutations cause a novel syndrome characterized by ataxia and
            mild mental retardation with predisposition to quadrupedal gait
  JOURNAL   PLoS Genet 5 (5), e1000487 (2009)
   PUBMED   19461874
  REMARK    GeneRIF: Consanguineous Iraqi family in which affected siblings had
            mild mental retardation and congenital ataxia characterized by
            quadrupedal gait. The mutation S100P is associated with
            proteasome-mediated degradation, and presumably represents a null
            mutation.
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Mori,S., Kou,I., Sato,H., Emi,M., Ito,H., Hosoi,T. and Ikegawa,S.
  TITLE     Nucleotide variations in genes encoding carbonic anhydrase 8 and 10
            associated with femoral bone mineral density in Japanese female
            with osteoporosis
  JOURNAL   J Bone Miner Metab 27 (2), 213-216 (2009)
   PUBMED   19172221
  REMARK    GeneRIF: The results suggest that the variations of CA8 and CA10
            loci may be important determinants of osteoporosis in Japanese
            women.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Bergenhem,N.C., Hallberg,M. and Wisen,S.
  TITLE     Molecular characterization of the human carbonic anhydrase-related
            protein (HCA-RP VIII)
  JOURNAL   Biochim Biophys Acta 1384 (2), 294-298 (1998)
   PUBMED   9659390
REFERENCE   8  (residues 1 to 290)
  AUTHORS   Bergenhem,N.C., Sait,S.S., Eddy,R.L., Shows,T.B. and Tashian,R.E.
  TITLE     Assignment of the gene for human carbonic anhydrase VIII(CA8) to
            chromosome 8q11-->q12
  JOURNAL   Cytogenet Cell Genet 71 (3), 299-300 (1995)
   PUBMED   7587398
REFERENCE   9  (residues 1 to 290)
  AUTHORS   Kelly,C., Nogradi,A., Walker,R., Caddy,K., Peters,J. and Carter,N.
  TITLE     Lurching, reeling, waddling and staggering in mice--is carbonic
            anhydrase (CA) VIII a candidate gene?
  JOURNAL   Biochem Soc Trans 22 (3), 359S (1994)
   PUBMED   7821612
REFERENCE   10 (residues 1 to 290)
  AUTHORS   Skaggs,L.A., Bergenhem,N.C., Venta,P.J. and Tashian,R.E.
  TITLE     The deduced amino acid sequence of human carbonic anhydrase-related
            protein (CARP) is 98% identical to the mouse homologue
  JOURNAL   Gene 126 (2), 291-292 (1993)
   PUBMED   8482548
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC400671.1, BC108929.2,
            AC021393.10 and HY307263.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 31, 2002 this sequence version replaced NP_004047.2.
            
            Summary: The protein encoded by this gene was initially named
            CA-related protein because of sequence similarity to other known
            carbonic anhydrase genes. However, the gene product lacks carbonic
            anhydrase activity (i.e., the reversible hydration of carbon
            dioxide). The gene product continues to carry a carbonic anhydrase
            designation based on clear sequence identity to other members of
            the carbonic anhydrase gene family. The absence of CA8 gene
            transcription in the cerebellum of the lurcher mutant in mice with
            a neurologic defect suggests an important role for this acatalytic
            form. Mutations in this gene are associated with cerebellar ataxia,
            mental retardation, and dysequilibrium syndrome 3 (CMARQ3).
            Polymorphisms in this gene are associated with osteoporosis, and
            overexpression of this gene in osteosarcoma cells suggests an
            oncogenic role. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Mar 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.6627.1,
                                           SRR1660805.45671.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000317995.5/ ENSP00000314407.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.1"
     Protein         1..290
                     /product="carbonic anhydrase-related protein isoform a"
                     /EC_number="4.2.1.1"
                     /note="CA-related protein; carbonic anhydrase-related
                     protein; carbonic anhydrase VIII; carbonic anhydrase-like
                     sequence; carbonate dehydratase"
                     /calculated_mol_wt=32842
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35219.3)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5PPN4; propagated from
                     UniProtKB/Swiss-Prot (P35219.3)"
     Region          35..289
                     /region_name="alpha_CARP_VIII"
                     /note="Carbonic anhydrase alpha related protein, group
                     VIII. Carbonic anhydrase related proteins (CARPs) are
                     sequence similar to carbonic anhydrases. Carbonic
                     anhydrases are zinc-containing enzymes that catalyze the
                     reversible hydration of carbon dioxide in a...; cd03120"
                     /db_xref="CDD:239394"
     Site            116
                     /site_type="other"
                     /note="Ancestral zinc ligand; propagated from
                     UniProtKB/Swiss-Prot (P35219.3)"
     CDS             1..290
                     /gene="CA8"
                     /gene_synonym="CA-RP; CA-VIII; CALS; CAMRQ3; CARP; SCAR34"
                     /coded_by="NM_004056.6:254..1126"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6174.1"
                     /db_xref="GeneID:767"
                     /db_xref="HGNC:HGNC:1382"
                     /db_xref="MIM:114815"
ORIGIN      
        1 madlsfiedt vafpekeede eeeeegvewg yeegvewglv fpdangeyqs pinlnsrear
       61 ydpslldvrl spnyvvcrdc evtndghtiq vilksksvls ggplpqghef elyevrfhwg
      121 renqrgseht vnfkafpmel hlihwnstlf gsideavgkp hgiaiialfv qigkehvglk
      181 avteilqdiq ykgksktipc fnpntllpdp llrdywvyeg sltippcseg vtwilfrypl
      241 tisqlqieef rrlrthvkga elvegcdgil gdnfrptqpl sdrviraafq
//
LOCUS       NP_001308766             290 aa            linear   PRI 11-JAN-2026
DEFINITION  carbonic anhydrase-related protein isoform a [Homo sapiens].
ACCESSION   NP_001308766
VERSION     NP_001308766.1
DBSOURCE    REFSEQ: accession NM_001321837.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Wu,C.Y., Yu,J.Y., Chen,Y.S., Chang,H.P., Hsieh,B.Y., Lin,Y.H.,
            Ma,C.Y., Tsai,S.F. and Hsieh,M.
  TITLE     Effects of down-regulated carbonic anhydrase 8 on cell survival and
            glucose metabolism in human colorectal cancer cell lines
  JOURNAL   Cell Biochem Funct 42 (3), e4001 (2024)
   PUBMED   38571370
  REMARK    GeneRIF: Effects of down-regulated carbonic anhydrase 8 on cell
            survival and glucose metabolism in human colorectal cancer cell
            lines.
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Lin,G.Y., Ma,C.Y., Kuo,L.C., Hsieh,B.Y., Wang,H., Liu,C.S. and
            Hsieh,M.
  TITLE     Altered glucose metabolism and its association with carbonic
            anhydrase 8 in Machado-Joseph Disease
  JOURNAL   Metab Brain Dis 37 (6), 2103-2120 (2022)
   PUBMED   35488942
  REMARK    GeneRIF: Altered glucose metabolism and its association with
            carbonic anhydrase 8 in Machado-Joseph Disease.
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Hiepp,L., Mayr,D., Gartner,K., Schmoeckel,E., Klauschen,F.,
            Burges,A., Mahner,S., Zeidler,R. and Czogalla,B.
  TITLE     Carbonic anhydrase XII as biomarker and therapeutic target in
            ovarian carcinomas
  JOURNAL   PLoS One 17 (7), e0271630 (2022)
   PUBMED   35901081
  REMARK    GeneRIF: Carbonic anhydrase XII as biomarker and therapeutic target
            in ovarian carcinomas.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Wang,T.K., Lin,Y.M., Lo,C.M., Tang,C.H., Teng,C.L., Chao,W.T.,
            Wu,M.H., Liu,C.S. and Hsieh,M.
  TITLE     Oncogenic roles of carbonic anhydrase 8 in human osteosarcoma cells
  JOURNAL   Tumour Biol 37 (6), 7989-8005 (2016)
   PUBMED   26711783
  REMARK    GeneRIF: we observed increased expression of CA8 in more aggressive
            types of human osteosarcoma (OS) cells and found that CA8
            expression is correlated with disease stages, such that more
            intense expression occurs in the disease late stage
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Turkmen,S., Guo,G., Garshasbi,M., Hoffmann,K., Alshalah,A.J.,
            Mischung,C., Kuss,A., Humphrey,N., Mundlos,S. and Robinson,P.N.
  TITLE     CA8 mutations cause a novel syndrome characterized by ataxia and
            mild mental retardation with predisposition to quadrupedal gait
  JOURNAL   PLoS Genet 5 (5), e1000487 (2009)
   PUBMED   19461874
  REMARK    GeneRIF: Consanguineous Iraqi family in which affected siblings had
            mild mental retardation and congenital ataxia characterized by
            quadrupedal gait. The mutation S100P is associated with
            proteasome-mediated degradation, and presumably represents a null
            mutation.
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Mori,S., Kou,I., Sato,H., Emi,M., Ito,H., Hosoi,T. and Ikegawa,S.
  TITLE     Nucleotide variations in genes encoding carbonic anhydrase 8 and 10
            associated with femoral bone mineral density in Japanese female
            with osteoporosis
  JOURNAL   J Bone Miner Metab 27 (2), 213-216 (2009)
   PUBMED   19172221
  REMARK    GeneRIF: The results suggest that the variations of CA8 and CA10
            loci may be important determinants of osteoporosis in Japanese
            women.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Bergenhem,N.C., Hallberg,M. and Wisen,S.
  TITLE     Molecular characterization of the human carbonic anhydrase-related
            protein (HCA-RP VIII)
  JOURNAL   Biochim Biophys Acta 1384 (2), 294-298 (1998)
   PUBMED   9659390
REFERENCE   8  (residues 1 to 290)
  AUTHORS   Bergenhem,N.C., Sait,S.S., Eddy,R.L., Shows,T.B. and Tashian,R.E.
  TITLE     Assignment of the gene for human carbonic anhydrase VIII(CA8) to
            chromosome 8q11-->q12
  JOURNAL   Cytogenet Cell Genet 71 (3), 299-300 (1995)
   PUBMED   7587398
REFERENCE   9  (residues 1 to 290)
  AUTHORS   Kelly,C., Nogradi,A., Walker,R., Caddy,K., Peters,J. and Carter,N.
  TITLE     Lurching, reeling, waddling and staggering in mice--is carbonic
            anhydrase (CA) VIII a candidate gene?
  JOURNAL   Biochem Soc Trans 22 (3), 359S (1994)
   PUBMED   7821612
REFERENCE   10 (residues 1 to 290)
  AUTHORS   Skaggs,L.A., Bergenhem,N.C., Venta,P.J. and Tashian,R.E.
  TITLE     The deduced amino acid sequence of human carbonic anhydrase-related
            protein (CARP) is 98% identical to the mouse homologue
  JOURNAL   Gene 126 (2), 291-292 (1993)
   PUBMED   8482548
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC400671.1, BC108929.2,
            AC132834.4 and BX098118.1.
            
            Summary: The protein encoded by this gene was initially named
            CA-related protein because of sequence similarity to other known
            carbonic anhydrase genes. However, the gene product lacks carbonic
            anhydrase activity (i.e., the reversible hydration of carbon
            dioxide). The gene product continues to carry a carbonic anhydrase
            designation based on clear sequence identity to other members of
            the carbonic anhydrase gene family. The absence of CA8 gene
            transcription in the cerebellum of the lurcher mutant in mice with
            a neurologic defect suggests an important role for this acatalytic
            form. Mutations in this gene are associated with cerebellar ataxia,
            mental retardation, and dysequilibrium syndrome 3 (CMARQ3).
            Polymorphisms in this gene are associated with osteoporosis, and
            overexpression of this gene in osteosarcoma cells suggests an
            oncogenic role. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Mar 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.230829.1,
                                           SRR1803613.214566.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.1"
     Protein         1..290
                     /product="carbonic anhydrase-related protein isoform a"
                     /EC_number="4.2.1.1"
                     /note="CA-related protein; carbonic anhydrase-related
                     protein; carbonic anhydrase VIII; carbonic anhydrase-like
                     sequence; carbonate dehydratase"
                     /calculated_mol_wt=32842
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35219.3)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5PPN4; propagated from
                     UniProtKB/Swiss-Prot (P35219.3)"
     Region          35..289
                     /region_name="alpha_CARP_VIII"
                     /note="Carbonic anhydrase alpha related protein, group
                     VIII. Carbonic anhydrase related proteins (CARPs) are
                     sequence similar to carbonic anhydrases. Carbonic
                     anhydrases are zinc-containing enzymes that catalyze the
                     reversible hydration of carbon dioxide in a...; cd03120"
                     /db_xref="CDD:239394"
     Site            116
                     /site_type="other"
                     /note="Ancestral zinc ligand; propagated from
                     UniProtKB/Swiss-Prot (P35219.3)"
     CDS             1..290
                     /gene="CA8"
                     /gene_synonym="CA-RP; CA-VIII; CALS; CAMRQ3; CARP; SCAR34"
                     /coded_by="NM_001321837.2:254..1126"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6174.1"
                     /db_xref="GeneID:767"
                     /db_xref="HGNC:HGNC:1382"
                     /db_xref="MIM:114815"
ORIGIN      
        1 madlsfiedt vafpekeede eeeeegvewg yeegvewglv fpdangeyqs pinlnsrear
       61 ydpslldvrl spnyvvcrdc evtndghtiq vilksksvls ggplpqghef elyevrfhwg
      121 renqrgseht vnfkafpmel hlihwnstlf gsideavgkp hgiaiialfv qigkehvglk
      181 avteilqdiq ykgksktipc fnpntllpdp llrdywvyeg sltippcseg vtwilfrypl
      241 tisqlqieef rrlrthvkga elvegcdgil gdnfrptqpl sdrviraafq
//
LOCUS       NP_001308768             258 aa            linear   PRI 11-JAN-2026
DEFINITION  carbonic anhydrase-related protein isoform c [Homo sapiens].
ACCESSION   NP_001308768
VERSION     NP_001308768.1
DBSOURCE    REFSEQ: accession NM_001321839.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Wu,C.Y., Yu,J.Y., Chen,Y.S., Chang,H.P., Hsieh,B.Y., Lin,Y.H.,
            Ma,C.Y., Tsai,S.F. and Hsieh,M.
  TITLE     Effects of down-regulated carbonic anhydrase 8 on cell survival and
            glucose metabolism in human colorectal cancer cell lines
  JOURNAL   Cell Biochem Funct 42 (3), e4001 (2024)
   PUBMED   38571370
  REMARK    GeneRIF: Effects of down-regulated carbonic anhydrase 8 on cell
            survival and glucose metabolism in human colorectal cancer cell
            lines.
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Lin,G.Y., Ma,C.Y., Kuo,L.C., Hsieh,B.Y., Wang,H., Liu,C.S. and
            Hsieh,M.
  TITLE     Altered glucose metabolism and its association with carbonic
            anhydrase 8 in Machado-Joseph Disease
  JOURNAL   Metab Brain Dis 37 (6), 2103-2120 (2022)
   PUBMED   35488942
  REMARK    GeneRIF: Altered glucose metabolism and its association with
            carbonic anhydrase 8 in Machado-Joseph Disease.
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Hiepp,L., Mayr,D., Gartner,K., Schmoeckel,E., Klauschen,F.,
            Burges,A., Mahner,S., Zeidler,R. and Czogalla,B.
  TITLE     Carbonic anhydrase XII as biomarker and therapeutic target in
            ovarian carcinomas
  JOURNAL   PLoS One 17 (7), e0271630 (2022)
   PUBMED   35901081
  REMARK    GeneRIF: Carbonic anhydrase XII as biomarker and therapeutic target
            in ovarian carcinomas.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Wang,T.K., Lin,Y.M., Lo,C.M., Tang,C.H., Teng,C.L., Chao,W.T.,
            Wu,M.H., Liu,C.S. and Hsieh,M.
  TITLE     Oncogenic roles of carbonic anhydrase 8 in human osteosarcoma cells
  JOURNAL   Tumour Biol 37 (6), 7989-8005 (2016)
   PUBMED   26711783
  REMARK    GeneRIF: we observed increased expression of CA8 in more aggressive
            types of human osteosarcoma (OS) cells and found that CA8
            expression is correlated with disease stages, such that more
            intense expression occurs in the disease late stage
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Turkmen,S., Guo,G., Garshasbi,M., Hoffmann,K., Alshalah,A.J.,
            Mischung,C., Kuss,A., Humphrey,N., Mundlos,S. and Robinson,P.N.
  TITLE     CA8 mutations cause a novel syndrome characterized by ataxia and
            mild mental retardation with predisposition to quadrupedal gait
  JOURNAL   PLoS Genet 5 (5), e1000487 (2009)
   PUBMED   19461874
  REMARK    GeneRIF: Consanguineous Iraqi family in which affected siblings had
            mild mental retardation and congenital ataxia characterized by
            quadrupedal gait. The mutation S100P is associated with
            proteasome-mediated degradation, and presumably represents a null
            mutation.
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Mori,S., Kou,I., Sato,H., Emi,M., Ito,H., Hosoi,T. and Ikegawa,S.
  TITLE     Nucleotide variations in genes encoding carbonic anhydrase 8 and 10
            associated with femoral bone mineral density in Japanese female
            with osteoporosis
  JOURNAL   J Bone Miner Metab 27 (2), 213-216 (2009)
   PUBMED   19172221
  REMARK    GeneRIF: The results suggest that the variations of CA8 and CA10
            loci may be important determinants of osteoporosis in Japanese
            women.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Bergenhem,N.C., Hallberg,M. and Wisen,S.
  TITLE     Molecular characterization of the human carbonic anhydrase-related
            protein (HCA-RP VIII)
  JOURNAL   Biochim Biophys Acta 1384 (2), 294-298 (1998)
   PUBMED   9659390
REFERENCE   8  (residues 1 to 258)
  AUTHORS   Bergenhem,N.C., Sait,S.S., Eddy,R.L., Shows,T.B. and Tashian,R.E.
  TITLE     Assignment of the gene for human carbonic anhydrase VIII(CA8) to
            chromosome 8q11-->q12
  JOURNAL   Cytogenet Cell Genet 71 (3), 299-300 (1995)
   PUBMED   7587398
REFERENCE   9  (residues 1 to 258)
  AUTHORS   Kelly,C., Nogradi,A., Walker,R., Caddy,K., Peters,J. and Carter,N.
  TITLE     Lurching, reeling, waddling and staggering in mice--is carbonic
            anhydrase (CA) VIII a candidate gene?
  JOURNAL   Biochem Soc Trans 22 (3), 359S (1994)
   PUBMED   7821612
REFERENCE   10 (residues 1 to 258)
  AUTHORS   Skaggs,L.A., Bergenhem,N.C., Venta,P.J. and Tashian,R.E.
  TITLE     The deduced amino acid sequence of human carbonic anhydrase-related
            protein (CARP) is 98% identical to the mouse homologue
  JOURNAL   Gene 126 (2), 291-292 (1993)
   PUBMED   8482548
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC400671.1, BC108929.2,
            AC021393.10 and HY307263.1.
            
            Summary: The protein encoded by this gene was initially named
            CA-related protein because of sequence similarity to other known
            carbonic anhydrase genes. However, the gene product lacks carbonic
            anhydrase activity (i.e., the reversible hydration of carbon
            dioxide). The gene product continues to carry a carbonic anhydrase
            designation based on clear sequence identity to other members of
            the carbonic anhydrase gene family. The absence of CA8 gene
            transcription in the cerebellum of the lurcher mutant in mice with
            a neurologic defect suggests an important role for this acatalytic
            form. Mutations in this gene are associated with cerebellar ataxia,
            mental retardation, and dysequilibrium syndrome 3 (CMARQ3).
            Polymorphisms in this gene are associated with osteoporosis, and
            overexpression of this gene in osteosarcoma cells suggests an
            oncogenic role. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Mar 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.169501.1,
                                           SRR1660807.265226.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.1"
     Protein         1..258
                     /product="carbonic anhydrase-related protein isoform c"
                     /EC_number="4.2.1.1"
                     /note="CA-related protein; carbonic anhydrase-related
                     protein; carbonic anhydrase VIII; carbonic anhydrase-like
                     sequence; carbonate dehydratase"
                     /calculated_mol_wt=29362
     Region          35..257
                     /region_name="alpha_CA"
                     /note="Carbonic anhydrase alpha (vertebrate-like) group.
                     Carbonic anhydrases (CAs) are zinc-containing enzymes that
                     catalyze the reversible hydration of carbon dioxide in a
                     two-step mechanism: a nucleophilic attack of a zinc-bound
                     hydroxide ion on carbon...; cl00012"
                     /db_xref="CDD:469577"
     Site            order(87,114,116,118,128,191)
                     /site_type="active"
                     /db_xref="CDD:239394"
     CDS             1..258
                     /gene="CA8"
                     /gene_synonym="CA-RP; CA-VIII; CALS; CAMRQ3; CARP; SCAR34"
                     /coded_by="NM_001321839.2:254..1030"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="GeneID:767"
                     /db_xref="HGNC:HGNC:1382"
                     /db_xref="MIM:114815"
ORIGIN      
        1 madlsfiedt vafpekeede eeeeegvewg yeegvewglv fpdangeyqs pinlnsrear
       61 ydpslldvrl spnyvvcrdc evtndghtiq vilksksvls ggplpqghef elyevrfhwg
      121 renqrgseht vnfkafpmei gkehvglkav teilqdiqyk gksktipcfn pntllpdpll
      181 rdywvyegsl tippcsegvt wilfryplti sqlqieefrr lrthvkgael vegcdgilgd
      241 nfrptqplsd rviraafq
//
LOCUS       NP_056232                236 aa            linear   PRI 11-JAN-2026
DEFINITION  sperm flagellar protein 1 [Homo sapiens].
ACCESSION   NP_056232
VERSION     NP_056232.2
DBSOURCE    REFSEQ: accession NM_015417.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Tapia,R. and Hecht,G.A.
  TITLE     Spef1/CLAMP binds microtubules and actin-based structures and
            regulates cell migration and epithelia cell polarity
  JOURNAL   Ann N Y Acad Sci 1515 (1), 97-104 (2022)
   PUBMED   35710871
  REMARK    GeneRIF: Spef1/CLAMP binds microtubules and actin-based structures
            and regulates cell migration and epithelia cell polarity.
            Review article
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Tapia,R., Perez-Yepez,E.A., Carlino,M.J., Karandikar,U.C.,
            Kralicek,S.E., Estes,M.K. and Hecht,G.A.
  TITLE     Sperm Flagellar 1 Binds Actin in Intestinal Epithelial Cells and
            Contributes to Formation of Filopodia and Lamellipodia
  JOURNAL   Gastroenterology 157 (6), 1544-1555 (2019)
   PUBMED   31473225
  REMARK    GeneRIF: Sperm flagellar 1 (also called CLAMP) is an actin-binding
            protein, rather than a microtubule-binding protein, in intestinal
            epithelial cells (IECs). CLAMP distribution changes during
            intestinal epithelial cell polarization, regulates the formation of
            filopodia, and appears to assist in the organization of actin
            bundles within lamellipodia of migrating IECs.
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Werner,M.E., Mitchell,J.W., Putzbach,W., Bacon,E., Kim,S.K. and
            Mitchell,B.J.
  TITLE     Radial intercalation is regulated by the Par complex and the
            microtubule-stabilizing protein CLAMP/Spef1
  JOURNAL   J Cell Biol 206 (3), 367-376 (2014)
   PUBMED   25070955
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Dougherty,G.W., Adler,H.J., Rzadzinska,A., Gimona,M., Tomita,Y.,
            Lattig,M.C., Merritt,R.C. Jr. and Kachar,B.
  TITLE     CLAMP, a novel microtubule-associated protein with EB-type calponin
            homology
  JOURNAL   Cell Motil Cytoskeleton 62 (3), 141-156 (2005)
   PUBMED   16206169
  REMARK    GeneRIF: a.k.a. Spef1 (sperm flagella) and CLAMP (CaLponin-homology
            And Microtubule associated Protein) CLAMP/Spef1 expression also in
            brain, lung, and inner ear MT association of CLAMP requires the CH
            domain, which has highest similarity with EB family proteins
            Erratum:[Cell Motil Cytoskeleton. 2005 Dec;62(4):259]
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Chan,S.W., Fowler,K.J., Choo,K.H. and Kalitsis,P.
  TITLE     Spef1, a conserved novel testis protein found in mouse sperm
            flagella
  JOURNAL   Gene 353 (2), 189-199 (2005)
   PUBMED   15979255
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB030684.1, DB033051.1, AL040853.1, AL080154.1 and AI925267.1.
            
            On Mar 10, 2006 this sequence version replaced NP_056232.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF560745.1, BI520334.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA1970526 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379756.3/ ENSP00000369080.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..236
                     /product="sperm flagellar protein 1"
                     /note="calponin-homology and microtubule-associated
                     protein; sperm flagellar 1"
                     /calculated_mol_wt=26856
     Region          13..104
                     /region_name="CH_2"
                     /note="CH-like domain in sperm protein; pfam06294"
                     /db_xref="CDD:461871"
     Region          115..176
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4P9.3)"
     Region          183..236
                     /region_name="Essential for homodimerization and
                     microtubule bundling activity.
                     /evidence=ECO:0000250|UniProtKB:Q99JL1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y4P9.3)"
     CDS             1..236
                     /gene="SPEF1"
                     /gene_synonym="C20orf28; CLAMP; SPEF1A"
                     /coded_by="NM_015417.5:162..872"
                     /db_xref="CCDS:CCDS13063.2"
                     /db_xref="GeneID:25876"
                     /db_xref="HGNC:HGNC:15874"
                     /db_xref="MIM:610674"
ORIGIN      
        1 massvdeeal hqlylwvdni plsrpkrnls rdfsdgvlva evikfyfpkm vemhnyvpan
       61 slqqklsnwg hlnrkvlkrl nfsvpddvmr kiaqcapgvv elvliplrqr leerqrrrkq
      121 gagslqelap qdgsgymdvg vsqkargegv pdpqgggqls wdrppaprpp aynralqgdp
      181 sfvlqiaeke qellasqetv qvlqmkvrrl ehllqlknvr iedlsrrlqq aerkqr
//
LOCUS       NP_001308767             263 aa            linear   PRI 11-JAN-2026
DEFINITION  carbonic anhydrase-related protein isoform b [Homo sapiens].
ACCESSION   NP_001308767 XP_011515887
VERSION     NP_001308767.1
DBSOURCE    REFSEQ: accession NM_001321838.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Wu,C.Y., Yu,J.Y., Chen,Y.S., Chang,H.P., Hsieh,B.Y., Lin,Y.H.,
            Ma,C.Y., Tsai,S.F. and Hsieh,M.
  TITLE     Effects of down-regulated carbonic anhydrase 8 on cell survival and
            glucose metabolism in human colorectal cancer cell lines
  JOURNAL   Cell Biochem Funct 42 (3), e4001 (2024)
   PUBMED   38571370
  REMARK    GeneRIF: Effects of down-regulated carbonic anhydrase 8 on cell
            survival and glucose metabolism in human colorectal cancer cell
            lines.
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Lin,G.Y., Ma,C.Y., Kuo,L.C., Hsieh,B.Y., Wang,H., Liu,C.S. and
            Hsieh,M.
  TITLE     Altered glucose metabolism and its association with carbonic
            anhydrase 8 in Machado-Joseph Disease
  JOURNAL   Metab Brain Dis 37 (6), 2103-2120 (2022)
   PUBMED   35488942
  REMARK    GeneRIF: Altered glucose metabolism and its association with
            carbonic anhydrase 8 in Machado-Joseph Disease.
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Hiepp,L., Mayr,D., Gartner,K., Schmoeckel,E., Klauschen,F.,
            Burges,A., Mahner,S., Zeidler,R. and Czogalla,B.
  TITLE     Carbonic anhydrase XII as biomarker and therapeutic target in
            ovarian carcinomas
  JOURNAL   PLoS One 17 (7), e0271630 (2022)
   PUBMED   35901081
  REMARK    GeneRIF: Carbonic anhydrase XII as biomarker and therapeutic target
            in ovarian carcinomas.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Wang,T.K., Lin,Y.M., Lo,C.M., Tang,C.H., Teng,C.L., Chao,W.T.,
            Wu,M.H., Liu,C.S. and Hsieh,M.
  TITLE     Oncogenic roles of carbonic anhydrase 8 in human osteosarcoma cells
  JOURNAL   Tumour Biol 37 (6), 7989-8005 (2016)
   PUBMED   26711783
  REMARK    GeneRIF: we observed increased expression of CA8 in more aggressive
            types of human osteosarcoma (OS) cells and found that CA8
            expression is correlated with disease stages, such that more
            intense expression occurs in the disease late stage
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Turkmen,S., Guo,G., Garshasbi,M., Hoffmann,K., Alshalah,A.J.,
            Mischung,C., Kuss,A., Humphrey,N., Mundlos,S. and Robinson,P.N.
  TITLE     CA8 mutations cause a novel syndrome characterized by ataxia and
            mild mental retardation with predisposition to quadrupedal gait
  JOURNAL   PLoS Genet 5 (5), e1000487 (2009)
   PUBMED   19461874
  REMARK    GeneRIF: Consanguineous Iraqi family in which affected siblings had
            mild mental retardation and congenital ataxia characterized by
            quadrupedal gait. The mutation S100P is associated with
            proteasome-mediated degradation, and presumably represents a null
            mutation.
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Mori,S., Kou,I., Sato,H., Emi,M., Ito,H., Hosoi,T. and Ikegawa,S.
  TITLE     Nucleotide variations in genes encoding carbonic anhydrase 8 and 10
            associated with femoral bone mineral density in Japanese female
            with osteoporosis
  JOURNAL   J Bone Miner Metab 27 (2), 213-216 (2009)
   PUBMED   19172221
  REMARK    GeneRIF: The results suggest that the variations of CA8 and CA10
            loci may be important determinants of osteoporosis in Japanese
            women.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Bergenhem,N.C., Hallberg,M. and Wisen,S.
  TITLE     Molecular characterization of the human carbonic anhydrase-related
            protein (HCA-RP VIII)
  JOURNAL   Biochim Biophys Acta 1384 (2), 294-298 (1998)
   PUBMED   9659390
REFERENCE   8  (residues 1 to 263)
  AUTHORS   Bergenhem,N.C., Sait,S.S., Eddy,R.L., Shows,T.B. and Tashian,R.E.
  TITLE     Assignment of the gene for human carbonic anhydrase VIII(CA8) to
            chromosome 8q11-->q12
  JOURNAL   Cytogenet Cell Genet 71 (3), 299-300 (1995)
   PUBMED   7587398
REFERENCE   9  (residues 1 to 263)
  AUTHORS   Kelly,C., Nogradi,A., Walker,R., Caddy,K., Peters,J. and Carter,N.
  TITLE     Lurching, reeling, waddling and staggering in mice--is carbonic
            anhydrase (CA) VIII a candidate gene?
  JOURNAL   Biochem Soc Trans 22 (3), 359S (1994)
   PUBMED   7821612
REFERENCE   10 (residues 1 to 263)
  AUTHORS   Skaggs,L.A., Bergenhem,N.C., Venta,P.J. and Tashian,R.E.
  TITLE     The deduced amino acid sequence of human carbonic anhydrase-related
            protein (CARP) is 98% identical to the mouse homologue
  JOURNAL   Gene 126 (2), 291-292 (1993)
   PUBMED   8482548
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC400671.1, BC108929.2,
            AC132834.4 and BX098118.1.
            
            On Mar 31, 2016 this sequence version replaced XP_011515887.1.
            
            Summary: The protein encoded by this gene was initially named
            CA-related protein because of sequence similarity to other known
            carbonic anhydrase genes. However, the gene product lacks carbonic
            anhydrase activity (i.e., the reversible hydration of carbon
            dioxide). The gene product continues to carry a carbonic anhydrase
            designation based on clear sequence identity to other members of
            the carbonic anhydrase gene family. The absence of CA8 gene
            transcription in the cerebellum of the lurcher mutant in mice with
            a neurologic defect suggests an important role for this acatalytic
            form. Mutations in this gene are associated with cerebellar ataxia,
            mental retardation, and dysequilibrium syndrome 3 (CMARQ3).
            Polymorphisms in this gene are associated with osteoporosis, and
            overexpression of this gene in osteosarcoma cells suggests an
            oncogenic role. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (3) represents the allele encoded
            by the GRCh38 reference genome and encodes isoform (b).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.359208.1,
                                           SRR1660809.300422.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.1"
     Protein         1..263
                     /product="carbonic anhydrase-related protein isoform b"
                     /EC_number="4.2.1.1"
                     /note="CA-related protein; carbonic anhydrase-related
                     protein; carbonic anhydrase VIII; carbonic anhydrase-like
                     sequence; carbonate dehydratase"
                     /calculated_mol_wt=29969
     Region          35..247
                     /region_name="alpha_CA"
                     /note="Carbonic anhydrase alpha (vertebrate-like) group.
                     Carbonic anhydrases (CAs) are zinc-containing enzymes that
                     catalyze the reversible hydration of carbon dioxide in a
                     two-step mechanism: a nucleophilic attack of a zinc-bound
                     hydroxide ion on carbon...; cl00012"
                     /db_xref="CDD:469577"
     Site            order(87,114,116,118,128,141,223)
                     /site_type="active"
                     /db_xref="CDD:238200"
     Site            order(116,118,141)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238200"
     CDS             1..263
                     /gene="CA8"
                     /gene_synonym="CA-RP; CA-VIII; CALS; CAMRQ3; CARP; SCAR34"
                     /coded_by="NM_001321838.2:254..1045"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:767"
                     /db_xref="HGNC:HGNC:1382"
                     /db_xref="MIM:114815"
ORIGIN      
        1 madlsfiedt vafpekeede eeeeegvewg yeegvewglv fpdangeyqs pinlnsrear
       61 ydpslldvrl spnyvvcrdc evtndghtiq vilksksvls ggplpqghef elyevrfhwg
      121 renqrgseht vnfkafpmel hlihwnstlf gsideavgkp hgiaiialfv qigkehvglk
      181 avteilqdiq ykgksktipc fnpntllpdp llrdywvyeg sltippcseg vtwilfrypl
      241 tisqlqvwrm esldvkwgcr lfl
//
LOCUS       NP_001403891             306 aa            linear   PRI 11-JAN-2026
DEFINITION  carbonic anhydrase-related protein isoform d [Homo sapiens].
ACCESSION   NP_001403891
VERSION     NP_001403891.1
DBSOURCE    REFSEQ: accession NM_001416962.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Wu,C.Y., Yu,J.Y., Chen,Y.S., Chang,H.P., Hsieh,B.Y., Lin,Y.H.,
            Ma,C.Y., Tsai,S.F. and Hsieh,M.
  TITLE     Effects of down-regulated carbonic anhydrase 8 on cell survival and
            glucose metabolism in human colorectal cancer cell lines
  JOURNAL   Cell Biochem Funct 42 (3), e4001 (2024)
   PUBMED   38571370
  REMARK    GeneRIF: Effects of down-regulated carbonic anhydrase 8 on cell
            survival and glucose metabolism in human colorectal cancer cell
            lines.
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Lin,G.Y., Ma,C.Y., Kuo,L.C., Hsieh,B.Y., Wang,H., Liu,C.S. and
            Hsieh,M.
  TITLE     Altered glucose metabolism and its association with carbonic
            anhydrase 8 in Machado-Joseph Disease
  JOURNAL   Metab Brain Dis 37 (6), 2103-2120 (2022)
   PUBMED   35488942
  REMARK    GeneRIF: Altered glucose metabolism and its association with
            carbonic anhydrase 8 in Machado-Joseph Disease.
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Hiepp,L., Mayr,D., Gartner,K., Schmoeckel,E., Klauschen,F.,
            Burges,A., Mahner,S., Zeidler,R. and Czogalla,B.
  TITLE     Carbonic anhydrase XII as biomarker and therapeutic target in
            ovarian carcinomas
  JOURNAL   PLoS One 17 (7), e0271630 (2022)
   PUBMED   35901081
  REMARK    GeneRIF: Carbonic anhydrase XII as biomarker and therapeutic target
            in ovarian carcinomas.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Wang,T.K., Lin,Y.M., Lo,C.M., Tang,C.H., Teng,C.L., Chao,W.T.,
            Wu,M.H., Liu,C.S. and Hsieh,M.
  TITLE     Oncogenic roles of carbonic anhydrase 8 in human osteosarcoma cells
  JOURNAL   Tumour Biol 37 (6), 7989-8005 (2016)
   PUBMED   26711783
  REMARK    GeneRIF: we observed increased expression of CA8 in more aggressive
            types of human osteosarcoma (OS) cells and found that CA8
            expression is correlated with disease stages, such that more
            intense expression occurs in the disease late stage
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Turkmen,S., Guo,G., Garshasbi,M., Hoffmann,K., Alshalah,A.J.,
            Mischung,C., Kuss,A., Humphrey,N., Mundlos,S. and Robinson,P.N.
  TITLE     CA8 mutations cause a novel syndrome characterized by ataxia and
            mild mental retardation with predisposition to quadrupedal gait
  JOURNAL   PLoS Genet 5 (5), e1000487 (2009)
   PUBMED   19461874
  REMARK    GeneRIF: Consanguineous Iraqi family in which affected siblings had
            mild mental retardation and congenital ataxia characterized by
            quadrupedal gait. The mutation S100P is associated with
            proteasome-mediated degradation, and presumably represents a null
            mutation.
REFERENCE   6  (residues 1 to 306)
  AUTHORS   Mori,S., Kou,I., Sato,H., Emi,M., Ito,H., Hosoi,T. and Ikegawa,S.
  TITLE     Nucleotide variations in genes encoding carbonic anhydrase 8 and 10
            associated with femoral bone mineral density in Japanese female
            with osteoporosis
  JOURNAL   J Bone Miner Metab 27 (2), 213-216 (2009)
   PUBMED   19172221
  REMARK    GeneRIF: The results suggest that the variations of CA8 and CA10
            loci may be important determinants of osteoporosis in Japanese
            women.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 306)
  AUTHORS   Bergenhem,N.C., Hallberg,M. and Wisen,S.
  TITLE     Molecular characterization of the human carbonic anhydrase-related
            protein (HCA-RP VIII)
  JOURNAL   Biochim Biophys Acta 1384 (2), 294-298 (1998)
   PUBMED   9659390
REFERENCE   8  (residues 1 to 306)
  AUTHORS   Bergenhem,N.C., Sait,S.S., Eddy,R.L., Shows,T.B. and Tashian,R.E.
  TITLE     Assignment of the gene for human carbonic anhydrase VIII(CA8) to
            chromosome 8q11-->q12
  JOURNAL   Cytogenet Cell Genet 71 (3), 299-300 (1995)
   PUBMED   7587398
REFERENCE   9  (residues 1 to 306)
  AUTHORS   Kelly,C., Nogradi,A., Walker,R., Caddy,K., Peters,J. and Carter,N.
  TITLE     Lurching, reeling, waddling and staggering in mice--is carbonic
            anhydrase (CA) VIII a candidate gene?
  JOURNAL   Biochem Soc Trans 22 (3), 359S (1994)
   PUBMED   7821612
REFERENCE   10 (residues 1 to 306)
  AUTHORS   Skaggs,L.A., Bergenhem,N.C., Venta,P.J. and Tashian,R.E.
  TITLE     The deduced amino acid sequence of human carbonic anhydrase-related
            protein (CARP) is 98% identical to the mouse homologue
  JOURNAL   Gene 126 (2), 291-292 (1993)
   PUBMED   8482548
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CP068270.2.
            
            Summary: The protein encoded by this gene was initially named
            CA-related protein because of sequence similarity to other known
            carbonic anhydrase genes. However, the gene product lacks carbonic
            anhydrase activity (i.e., the reversible hydration of carbon
            dioxide). The gene product continues to carry a carbonic anhydrase
            designation based on clear sequence identity to other members of
            the carbonic anhydrase gene family. The absence of CA8 gene
            transcription in the cerebellum of the lurcher mutant in mice with
            a neurologic defect suggests an important role for this acatalytic
            form. Mutations in this gene are associated with cerebellar ataxia,
            mental retardation, and dysequilibrium syndrome 3 (CMARQ3).
            Polymorphisms in this gene are associated with osteoporosis, and
            overexpression of this gene in osteosarcoma cells suggests an
            oncogenic role. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Mar 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.403576.1,
                                           SRR1803615.154542.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.1"
     Protein         1..306
                     /product="carbonic anhydrase-related protein isoform d"
                     /EC_number="4.2.1.1"
                     /note="CA-related protein; carbonic anhydrase-related
                     protein; carbonic anhydrase VIII; carbonic anhydrase-like
                     sequence; carbonate dehydratase"
                     /calculated_mol_wt=34656
     Region          35..305
                     /region_name="alpha_CARP_VIII"
                     /note="Carbonic anhydrase alpha related protein, group
                     VIII. Carbonic anhydrase related proteins (CARPs) are
                     sequence similar to carbonic anhydrases. Carbonic
                     anhydrases are zinc-containing enzymes that catalyze the
                     reversible hydration of carbon dioxide in a...; cd03120"
                     /db_xref="CDD:239394"
     CDS             1..306
                     /gene="CA8"
                     /gene_synonym="CA-RP; CA-VIII; CALS; CAMRQ3; CARP; SCAR34"
                     /coded_by="NM_001416962.1:254..1174"
                     /note="isoform d is encoded by transcript variant 7"
                     /db_xref="GeneID:767"
                     /db_xref="HGNC:HGNC:1382"
                     /db_xref="MIM:114815"
ORIGIN      
        1 madlsfiedt vafpekeede eeeeegvewg yeegvewglv fpdangeyqs pinlnsrear
       61 ydpslldvrl spnyvvcrdc evtndghtiq vilksksvls ggplpqghef elyevrfhwg
      121 renqrgseht vnfkafpmel hlihwnstlf gsideavgkp hgiaiialfv qigkehvglk
      181 avteilqdiq ykgksktipc fnpntllpdp llrdywvyeg sltippcseg vtwilfrypl
      241 tisqlqvwrm esgrkvgmpv isieefrrlr thvkgaelve gcdgilgdnf rptqplsdrv
      301 iraafq
//
LOCUS       NP_079143               1822 aa            linear   PRI 11-JAN-2026
DEFINITION  sperm flagellar protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_079143
VERSION     NP_079143.3
DBSOURCE    REFSEQ: accession NM_024867.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1822)
  AUTHORS   Lu,W., Li,Y., Meng,L., Tan,C., Nie,H., Zhang,Q., Song,Y., Zhang,H.,
            Tan,Y.Q., Tu,C., Guo,H., Wu,L. and Du,J.
  TITLE     Novel SPEF2 variants cause male infertility and likely primary
            ciliary dyskinesia
  JOURNAL   J Assist Reprod Genet 41 (6), 1485-1498 (2024)
   PUBMED   38568462
  REMARK    GeneRIF: Novel SPEF2 variants cause male infertility and likely
            primary ciliary dyskinesia.
REFERENCE   2  (residues 1 to 1822)
  AUTHORS   Li,D.Y., Yang,X.X., Tu,C.F., Wang,W.L., Meng,L.L., Lu,G.X.,
            Tan,Y.Q., Zhang,Q.J. and Du,J.
  TITLE     Sperm flagellar 2 (SPEF2) is essential for sperm flagellar assembly
            in humans
  JOURNAL   Asian J Androl 24 (4), 359-366 (2022)
   PUBMED   34755699
  REMARK    GeneRIF: Sperm flagellar 2 (SPEF2) is essential for sperm flagellar
            assembly in humans.
REFERENCE   3  (residues 1 to 1822)
  AUTHORS   Cindric,S., Dougherty,G.W., Olbrich,H., Hjeij,R., Loges,N.T.,
            Amirav,I., Philipsen,M.C., Marthin,J.K., Nielsen,K.G.,
            Sutharsan,S., Raidt,J., Werner,C., Pennekamp,P., Dworniczak,B. and
            Omran,H.
  TITLE     SPEF2- and HYDIN-Mutant Cilia Lack the Central Pair-associated
            Protein SPEF2, Aiding Primary Ciliary Dyskinesia Diagnostics
  JOURNAL   Am J Respir Cell Mol Biol 62 (3), 382-396 (2020)
   PUBMED   31545650
  REMARK    GeneRIF: In individuals with primary ciliary dyskinesia and central
            pair defects, the CP-associated protein SPEF2 is absent in
            HYDIN-mutant cells. 41 of 189 individuals had undetectable SPEF2
            and were subjected to a genetic analysis, which revealed one novel
            loss-of-function mutation in SPEF2 and 3 reported and 13 novel
            HYDIN mutations in 15 individuals. A mutation of SPEF2 is causative
            for PCD with a CP defect.
REFERENCE   4  (residues 1 to 1822)
  AUTHORS   Tu,C., Nie,H., Meng,L., Wang,W., Li,H., Yuan,S., Cheng,D., He,W.,
            Liu,G., Du,J., Gong,F., Lu,G., Lin,G., Zhang,Q. and Tan,Y.Q.
  TITLE     Novel mutations in SPEF2 causing different defects between flagella
            and cilia bridge: the phenotypic link between MMAF and PCD
  JOURNAL   Hum Genet 139 (2), 257-271 (2020)
   PUBMED   31942643
  REMARK    GeneRIF: Mutations in SPEF2 are associated with multiple
            morphological abnormalities of the sperm flagella and primary
            ciliary dyskinesia.
REFERENCE   5  (residues 1 to 1822)
  AUTHORS   Sha,Y., Liu,W., Wei,X., Zhu,X., Luo,X., Liang,L. and Guo,T.
  TITLE     Biallelic mutations in Sperm flagellum 2 cause human multiple
            morphological abnormalities of the sperm flagella (MMAF) phenotype
  JOURNAL   Clin Genet 96 (5), 385-393 (2019)
   PUBMED   31278745
  REMARK    GeneRIF: Biallelic mutations in Sperm flagellum 2 cause human
            multiple morphological abnormalities of the sperm flagella (MMAF)
            phenotype.
REFERENCE   6  (residues 1 to 1822)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1822)
  AUTHORS   Sironen,A., Vilkki,J., Bendixen,C. and Thomsen,B.
  TITLE     Infertile Finnish Yorkshire boars carry a full-length LINE-1
            retrotransposon within the KPL2 gene
  JOURNAL   Mol Genet Genomics 278 (4), 385-391 (2007)
   PUBMED   17610085
REFERENCE   8  (residues 1 to 1822)
  AUTHORS   Sironen,A., Thomsen,B., Andersson,M., Ahola,V. and Vilkki,J.
  TITLE     An intronic insertion in KPL2 results in aberrant splicing and
            causes the immotile short-tail sperm defect in the pig
  JOURNAL   Proc Natl Acad Sci U S A 103 (13), 5006-5011 (2006)
   PUBMED   16549801
REFERENCE   9  (residues 1 to 1822)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   10 (residues 1 to 1822)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC025448.6, BC067761.1, BC016773.1, BC110984.1, AL832607.1,
            AK097547.1, AB051557.1, DA295300.1 and BX648691.1.
            
            On Apr 25, 2007 this sequence version replaced NP_079143.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005670.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356031.8/ ENSP00000348314.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1822
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..1822
                     /product="sperm flagellar protein 2 isoform 1"
                     /note="cancer/testis antigen 122; sperm flagellar protein
                     2; testis tissue sperm-binding protein Li 47a; sperm
                     flagellar 2"
                     /calculated_mol_wt=209681
     Region          5..97
                     /region_name="CH_2"
                     /note="CH-like domain in sperm protein; pfam06294"
                     /db_xref="CDD:461871"
     Region          <176..>447
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          <686..868
                     /region_name="NK"
                     /note="Nucleoside/nucleotide kinase (NK) is a protein
                     superfamily consisting of multiple families of enzymes
                     that share structural similarity and are functionally
                     related to the catalysis of the reversible phosphate group
                     transfer from nucleoside triphosphates...; cl17190"
                     /db_xref="CDD:450170"
     Region          896..1004
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C093.2)"
     Region          1278..1327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C093.2)"
     Region          1324..1676
                     /region_name="Interaction with IFT20.
                     /evidence=ECO:0000269|PubMed:19889948"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C093.2)"
     Region          1664..1718
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C093.2)"
     Region          1803..1822
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C093.2)"
     CDS             1..1822
                     /gene="SPEF2"
                     /gene_synonym="CT122; KPL2; SPGF43"
                     /coded_by="NM_024867.4:136..5604"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43309.1"
                     /db_xref="GeneID:79925"
                     /db_xref="HGNC:HGNC:26293"
                     /db_xref="MIM:610172"
ORIGIN      
        1 mseilcqwln kelkvsrtvs pksfakafss gyllgevlhk felqddfsef ldsrvssakl
       61 nnfsrleptl nllgvqfdqn vahgiitekp gvatkllyql yialqkkkks gltgvemqtm
      121 qrltnlrlqn mksdtfqerl rhmiprqtdf nlmrityrfq ekykhvkedl ahlhfekler
      181 fqklkeeqrc fdiekqylnr rrqneimaki qaaiiqipkp asnrtlkale aqkmmkkkke
      241 aedvadeikk fealikkdlq akesasktsl dtagqtttdl lntysddeyi kkiqkrleed
      301 afareqrekr rrkllmdqli aheaqeeayr eeqlinrlmr qsqqerriav qlmhvrheke
      361 vlwqnrifre kqheerrlkd fqdaldreaa lakqakidfe eqflkekrfh dqiaveraqa
      421 ryekhysvca eildqivdls tkvadyrmlt nnlipyklmh dwkelffnak piyeqasvkt
      481 lpanpsreql telekrdlld tndyeeyknm vgewalpeem vdnlppsnnc ilghilhrla
      541 ekslppraes ttpelpsfav kgcllgktls gkttilrslq kdfpiqilsi dtlvqeaiqa
      601 fhdnekvsev lpiqkndeed alpvlqeeik esqdpqhvfs agpvsdevlp etegetmlsa
      661 nadktpkaee vkssdsflkl ttraqlgaks eqllkkgksi pdvllvdiiv naineipvnq
      721 dcildgfpmt lnqaqlleea ltgcnrnlte verkkaqkst laidpatske iplpspafdf
      781 villdvsdts smsrmndiia eelsyktahe disqrvaaen qdkdgdqnlr dqiqhriigf
      841 ldnwplleqw fsepenilik inaeidkesl cekvkeiltt eiakkknkve kkleekeaek
      901 kaaaslaelp lptpppappp epekekeihq shvasktpta kgkpqseaph gkqeslqegk
      961 gkkgetalkr kgspkgkssg gkvpvkkspa dstdtspvai vpqppkpgse ewvyvnepvp
     1021 eemplflvpy weliensyin tiktvlrhlr edqhtvlayl yeirtsfqef lkrpdhkqdf
     1081 vaqwqadfns lpddlwddee tkaelhqrvn dlrdrlwdic darkeeaeqe rldiineswl
     1141 qdtlgmtmnh ffslmqaeln rfqdtkrllq dyywgmeski pvednkrftr iplvqldskd
     1201 nsesqlripl vprisislet vtpkpktksv lkgkmdnsle nvesnfeade klvmdtwqqa
     1261 slavshmvaa eihqrlmeee kenqpadpke kspqmgankk vkkeppkkkq edkkpkgksp
     1321 pmaeatpviv tteeiaeikr knelrvkike ehlaalqfee iatqfrleli ktkalalled
     1381 lvtkvvdvyk lmekwlgery lnemastekl tdvaryhiet stkiqnelyl sqedffingn
     1441 ikvfpdppps irpppvekee dgtltieqld slrdqfldma pkgiignkaf tdilidlvtl
     1501 nlgtnnfpsn wmhltqpelq eltslltvns efvdwrkfll vtsmpwpipl eeelletlqk
     1561 fkavdkeqlg titfeqymqa glwftgdedi kipenplepl pfnrqehlie fffrlfadye
     1621 kdppqldytq mllyfachpd tvegvyrals vavgthvfqq vkasipsaek tsstdagpae
     1681 efpepeenaa reerklkddt ekreqkdeei penannekms metllkvfkg gseaqdsnrf
     1741 ashlkieniy aegfiktfqd lgaknlepie vavllkhpfi qdlisnysdy kfpdikiilq
     1801 rsehvqgsdg erspsrhtee kk
//
LOCUS       NP_653323                514 aa            linear   PRI 11-JAN-2026
DEFINITION  sperm flagellar protein 2 isoform 2 [Homo sapiens].
ACCESSION   NP_653323
VERSION     NP_653323.1
DBSOURCE    REFSEQ: accession NM_144722.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Lu,W., Li,Y., Meng,L., Tan,C., Nie,H., Zhang,Q., Song,Y., Zhang,H.,
            Tan,Y.Q., Tu,C., Guo,H., Wu,L. and Du,J.
  TITLE     Novel SPEF2 variants cause male infertility and likely primary
            ciliary dyskinesia
  JOURNAL   J Assist Reprod Genet 41 (6), 1485-1498 (2024)
   PUBMED   38568462
  REMARK    GeneRIF: Novel SPEF2 variants cause male infertility and likely
            primary ciliary dyskinesia.
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Li,D.Y., Yang,X.X., Tu,C.F., Wang,W.L., Meng,L.L., Lu,G.X.,
            Tan,Y.Q., Zhang,Q.J. and Du,J.
  TITLE     Sperm flagellar 2 (SPEF2) is essential for sperm flagellar assembly
            in humans
  JOURNAL   Asian J Androl 24 (4), 359-366 (2022)
   PUBMED   34755699
  REMARK    GeneRIF: Sperm flagellar 2 (SPEF2) is essential for sperm flagellar
            assembly in humans.
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Cindric,S., Dougherty,G.W., Olbrich,H., Hjeij,R., Loges,N.T.,
            Amirav,I., Philipsen,M.C., Marthin,J.K., Nielsen,K.G.,
            Sutharsan,S., Raidt,J., Werner,C., Pennekamp,P., Dworniczak,B. and
            Omran,H.
  TITLE     SPEF2- and HYDIN-Mutant Cilia Lack the Central Pair-associated
            Protein SPEF2, Aiding Primary Ciliary Dyskinesia Diagnostics
  JOURNAL   Am J Respir Cell Mol Biol 62 (3), 382-396 (2020)
   PUBMED   31545650
  REMARK    GeneRIF: In individuals with primary ciliary dyskinesia and central
            pair defects, the CP-associated protein SPEF2 is absent in
            HYDIN-mutant cells. 41 of 189 individuals had undetectable SPEF2
            and were subjected to a genetic analysis, which revealed one novel
            loss-of-function mutation in SPEF2 and 3 reported and 13 novel
            HYDIN mutations in 15 individuals. A mutation of SPEF2 is causative
            for PCD with a CP defect.
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Tu,C., Nie,H., Meng,L., Wang,W., Li,H., Yuan,S., Cheng,D., He,W.,
            Liu,G., Du,J., Gong,F., Lu,G., Lin,G., Zhang,Q. and Tan,Y.Q.
  TITLE     Novel mutations in SPEF2 causing different defects between flagella
            and cilia bridge: the phenotypic link between MMAF and PCD
  JOURNAL   Hum Genet 139 (2), 257-271 (2020)
   PUBMED   31942643
  REMARK    GeneRIF: Mutations in SPEF2 are associated with multiple
            morphological abnormalities of the sperm flagella and primary
            ciliary dyskinesia.
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Sha,Y., Liu,W., Wei,X., Zhu,X., Luo,X., Liang,L. and Guo,T.
  TITLE     Biallelic mutations in Sperm flagellum 2 cause human multiple
            morphological abnormalities of the sperm flagella (MMAF) phenotype
  JOURNAL   Clin Genet 96 (5), 385-393 (2019)
   PUBMED   31278745
  REMARK    GeneRIF: Biallelic mutations in Sperm flagellum 2 cause human
            multiple morphological abnormalities of the sperm flagella (MMAF)
            phenotype.
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Sironen,A., Vilkki,J., Bendixen,C. and Thomsen,B.
  TITLE     Infertile Finnish Yorkshire boars carry a full-length LINE-1
            retrotransposon within the KPL2 gene
  JOURNAL   Mol Genet Genomics 278 (4), 385-391 (2007)
   PUBMED   17610085
REFERENCE   8  (residues 1 to 514)
  AUTHORS   Sironen,A., Thomsen,B., Andersson,M., Ahola,V. and Vilkki,J.
  TITLE     An intronic insertion in KPL2 results in aberrant splicing and
            causes the immotile short-tail sperm defect in the pig
  JOURNAL   Proc Natl Acad Sci U S A 103 (13), 5006-5011 (2006)
   PUBMED   16549801
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   10 (residues 1 to 514)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC025448.6, BC016773.1 and AK058124.1.
            
            Transcript Variant: This variant (2) lacks more than half of the
            3'-most exons and has a 3' end that extends into an intron compared
            to variant 1. The resulting isoform (2) has a shorter and distinct
            C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.68671.1, BC067761.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..514
                     /product="sperm flagellar protein 2 isoform 2"
                     /note="cancer/testis antigen 122; sperm flagellar protein
                     2; testis tissue sperm-binding protein Li 47a; sperm
                     flagellar 2"
                     /calculated_mol_wt=61027
     Region          5..97
                     /region_name="CH_2"
                     /note="CH-like domain in sperm protein; pfam06294"
                     /db_xref="CDD:461871"
     Region          <176..>447
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..514
                     /gene="SPEF2"
                     /gene_synonym="CT122; KPL2; SPGF43"
                     /coded_by="NM_144722.4:136..1680"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3910.1"
                     /db_xref="GeneID:79925"
                     /db_xref="HGNC:HGNC:26293"
                     /db_xref="MIM:610172"
ORIGIN      
        1 mseilcqwln kelkvsrtvs pksfakafss gyllgevlhk felqddfsef ldsrvssakl
       61 nnfsrleptl nllgvqfdqn vahgiitekp gvatkllyql yialqkkkks gltgvemqtm
      121 qrltnlrlqn mksdtfqerl rhmiprqtdf nlmrityrfq ekykhvkedl ahlhfekler
      181 fqklkeeqrc fdiekqylnr rrqneimaki qaaiiqipkp asnrtlkale aqkmmkkkke
      241 aedvadeikk fealikkdlq akesasktsl dtagqtttdl lntysddeyi kkiqkrleed
      301 afareqrekr rrkllmdqli aheaqeeayr eeqlinrlmr qsqqerriav qlmhvrheke
      361 vlwqnrifre kqheerrlkd fqdaldreaa lakqakidfe eqflkekrfh dqiaveraqa
      421 ryekhysvca eildqivdls tkvadyrmlt nnlipyklmh dwkelffnak piyeqasvkt
      481 lpanpsreql telekrdlld tndyeeykvp tdmk
//
LOCUS       NP_001399060             306 aa            linear   PRI 11-JAN-2026
DEFINITION  carbonic anhydrase-related protein isoform d [Homo sapiens].
ACCESSION   NP_001399060
VERSION     NP_001399060.1
DBSOURCE    REFSEQ: accession NM_001412131.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 306)
  AUTHORS   Wu,C.Y., Yu,J.Y., Chen,Y.S., Chang,H.P., Hsieh,B.Y., Lin,Y.H.,
            Ma,C.Y., Tsai,S.F. and Hsieh,M.
  TITLE     Effects of down-regulated carbonic anhydrase 8 on cell survival and
            glucose metabolism in human colorectal cancer cell lines
  JOURNAL   Cell Biochem Funct 42 (3), e4001 (2024)
   PUBMED   38571370
  REMARK    GeneRIF: Effects of down-regulated carbonic anhydrase 8 on cell
            survival and glucose metabolism in human colorectal cancer cell
            lines.
REFERENCE   2  (residues 1 to 306)
  AUTHORS   Lin,G.Y., Ma,C.Y., Kuo,L.C., Hsieh,B.Y., Wang,H., Liu,C.S. and
            Hsieh,M.
  TITLE     Altered glucose metabolism and its association with carbonic
            anhydrase 8 in Machado-Joseph Disease
  JOURNAL   Metab Brain Dis 37 (6), 2103-2120 (2022)
   PUBMED   35488942
  REMARK    GeneRIF: Altered glucose metabolism and its association with
            carbonic anhydrase 8 in Machado-Joseph Disease.
REFERENCE   3  (residues 1 to 306)
  AUTHORS   Hiepp,L., Mayr,D., Gartner,K., Schmoeckel,E., Klauschen,F.,
            Burges,A., Mahner,S., Zeidler,R. and Czogalla,B.
  TITLE     Carbonic anhydrase XII as biomarker and therapeutic target in
            ovarian carcinomas
  JOURNAL   PLoS One 17 (7), e0271630 (2022)
   PUBMED   35901081
  REMARK    GeneRIF: Carbonic anhydrase XII as biomarker and therapeutic target
            in ovarian carcinomas.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 306)
  AUTHORS   Wang,T.K., Lin,Y.M., Lo,C.M., Tang,C.H., Teng,C.L., Chao,W.T.,
            Wu,M.H., Liu,C.S. and Hsieh,M.
  TITLE     Oncogenic roles of carbonic anhydrase 8 in human osteosarcoma cells
  JOURNAL   Tumour Biol 37 (6), 7989-8005 (2016)
   PUBMED   26711783
  REMARK    GeneRIF: we observed increased expression of CA8 in more aggressive
            types of human osteosarcoma (OS) cells and found that CA8
            expression is correlated with disease stages, such that more
            intense expression occurs in the disease late stage
REFERENCE   5  (residues 1 to 306)
  AUTHORS   Turkmen,S., Guo,G., Garshasbi,M., Hoffmann,K., Alshalah,A.J.,
            Mischung,C., Kuss,A., Humphrey,N., Mundlos,S. and Robinson,P.N.
  TITLE     CA8 mutations cause a novel syndrome characterized by ataxia and
            mild mental retardation with predisposition to quadrupedal gait
  JOURNAL   PLoS Genet 5 (5), e1000487 (2009)
   PUBMED   19461874
  REMARK    GeneRIF: Consanguineous Iraqi family in which affected siblings had
            mild mental retardation and congenital ataxia characterized by
            quadrupedal gait. The mutation S100P is associated with
            proteasome-mediated degradation, and presumably represents a null
            mutation.
REFERENCE   6  (residues 1 to 306)
  AUTHORS   Mori,S., Kou,I., Sato,H., Emi,M., Ito,H., Hosoi,T. and Ikegawa,S.
  TITLE     Nucleotide variations in genes encoding carbonic anhydrase 8 and 10
            associated with femoral bone mineral density in Japanese female
            with osteoporosis
  JOURNAL   J Bone Miner Metab 27 (2), 213-216 (2009)
   PUBMED   19172221
  REMARK    GeneRIF: The results suggest that the variations of CA8 and CA10
            loci may be important determinants of osteoporosis in Japanese
            women.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 306)
  AUTHORS   Bergenhem,N.C., Hallberg,M. and Wisen,S.
  TITLE     Molecular characterization of the human carbonic anhydrase-related
            protein (HCA-RP VIII)
  JOURNAL   Biochim Biophys Acta 1384 (2), 294-298 (1998)
   PUBMED   9659390
REFERENCE   8  (residues 1 to 306)
  AUTHORS   Bergenhem,N.C., Sait,S.S., Eddy,R.L., Shows,T.B. and Tashian,R.E.
  TITLE     Assignment of the gene for human carbonic anhydrase VIII(CA8) to
            chromosome 8q11-->q12
  JOURNAL   Cytogenet Cell Genet 71 (3), 299-300 (1995)
   PUBMED   7587398
REFERENCE   9  (residues 1 to 306)
  AUTHORS   Kelly,C., Nogradi,A., Walker,R., Caddy,K., Peters,J. and Carter,N.
  TITLE     Lurching, reeling, waddling and staggering in mice--is carbonic
            anhydrase (CA) VIII a candidate gene?
  JOURNAL   Biochem Soc Trans 22 (3), 359S (1994)
   PUBMED   7821612
REFERENCE   10 (residues 1 to 306)
  AUTHORS   Skaggs,L.A., Bergenhem,N.C., Venta,P.J. and Tashian,R.E.
  TITLE     The deduced amino acid sequence of human carbonic anhydrase-related
            protein (CARP) is 98% identical to the mouse homologue
  JOURNAL   Gene 126 (2), 291-292 (1993)
   PUBMED   8482548
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CP068270.2.
            
            Summary: The protein encoded by this gene was initially named
            CA-related protein because of sequence similarity to other known
            carbonic anhydrase genes. However, the gene product lacks carbonic
            anhydrase activity (i.e., the reversible hydration of carbon
            dioxide). The gene product continues to carry a carbonic anhydrase
            designation based on clear sequence identity to other members of
            the carbonic anhydrase gene family. The absence of CA8 gene
            transcription in the cerebellum of the lurcher mutant in mice with
            a neurologic defect suggests an important role for this acatalytic
            form. Mutations in this gene are associated with cerebellar ataxia,
            mental retardation, and dysequilibrium syndrome 3 (CMARQ3).
            Polymorphisms in this gene are associated with osteoporosis, and
            overexpression of this gene in osteosarcoma cells suggests an
            oncogenic role. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (6) uses the same exon combination
            as variant 3 but represents the allele encoded by the T2T-CHM13v2.0
            genome assembly. The encoded isoform (d) has a frameshifted
            C-terminus compared to isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.359208.1,
                                           SRR1660809.300422.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..306
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.1"
     Protein         1..306
                     /product="carbonic anhydrase-related protein isoform d"
                     /EC_number="4.2.1.1"
                     /note="CA-related protein; carbonic anhydrase-related
                     protein; carbonic anhydrase VIII; carbonic anhydrase-like
                     sequence; carbonate dehydratase"
                     /calculated_mol_wt=34656
     Region          35..305
                     /region_name="alpha_CARP_VIII"
                     /note="Carbonic anhydrase alpha related protein, group
                     VIII. Carbonic anhydrase related proteins (CARPs) are
                     sequence similar to carbonic anhydrases. Carbonic
                     anhydrases are zinc-containing enzymes that catalyze the
                     reversible hydration of carbon dioxide in a...; cd03120"
                     /db_xref="CDD:239394"
     CDS             1..306
                     /gene="CA8"
                     /gene_synonym="CA-RP; CA-VIII; CALS; CAMRQ3; CARP; SCAR34"
                     /coded_by="NM_001412131.1:254..1174"
                     /note="isoform d is encoded by transcript variant 6"
                     /db_xref="GeneID:767"
                     /db_xref="HGNC:HGNC:1382"
                     /db_xref="MIM:114815"
ORIGIN      
        1 madlsfiedt vafpekeede eeeeegvewg yeegvewglv fpdangeyqs pinlnsrear
       61 ydpslldvrl spnyvvcrdc evtndghtiq vilksksvls ggplpqghef elyevrfhwg
      121 renqrgseht vnfkafpmel hlihwnstlf gsideavgkp hgiaiialfv qigkehvglk
      181 avteilqdiq ykgksktipc fnpntllpdp llrdywvyeg sltippcseg vtwilfrypl
      241 tisqlqvwrm esgrkvgmpv isieefrrlr thvkgaelve gcdgilgdnf rptqplsdrv
      301 iraafq
//
LOCUS       NP_001336596             601 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform d [Homo sapiens].
ACCESSION   NP_001336596
VERSION     NP_001336596.1
DBSOURCE    REFSEQ: accession NM_001349667.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 601)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 601)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 601)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 601)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 601)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (26), as well as variants 5,
            23-25, and 27-30, encodes isoform d.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803616.40462.1 [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..601
                     /product="ribosomal protein S6 kinase delta-1 isoform d"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=66008
     Region          <414..591
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(464,466,468,485,496..501,528,534,537)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            481..501
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..601
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349667.2:1258..3063"
                     /note="isoform d is encoded by transcript variant 26"
                     /db_xref="CCDS:CCDS73030.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mlkalplkss ltpssqddsn qeddgqdssp kwpdsgssse eecttsyltl cneygqekie
       61 pgslneepfm ktegngvdtk aiksfpahla adsdspstql rahelkffpn ddpeavsspr
      121 tsdslsrskn spmeffrids kdsasellgl dfgeklyslk seplkpfftl pdgdsasrsf
      181 ntseskvefk aqdtisrgsd dsvpvisfkd aafddvsgtd egrpdllvnl pgelestrea
      241 aamgptkftq tnigiienkl leapdvlclr lsteqcqahe ekgieelsdp sgpksysite
      301 khyaqedprm lfvaavdhss sgdmsllpss dpkfqglgvv esavtannte eslfricspl
      361 sganeyiast dtlkteevll ftdqtddlak eeptslfqrd setkgesglv legdkeihqi
      421 fedldkklal asrfyipegc iqrwaaemvv aldalhregi vcrdlnpnni llndrghiql
      481 tyfsrwseve dscdsdaier mycapevgai teeteacdww slgavlfell tgktlvechp
      541 aginthttln mpecvseear sliqqllqfn plerlgagva gvedikshpf ftpvdwaelm
      601 r
//
LOCUS       NP_001336589             714 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform i [Homo sapiens].
ACCESSION   NP_001336589 XP_016856520
VERSION     NP_001336589.1
DBSOURCE    REFSEQ: accession NM_001349660.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 714)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 714)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 714)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 714)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 714)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 714)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            On Mar 22, 2017 this sequence version replaced XP_016856520.1.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (19), as well as variants 18, 20,
            and 21, encodes isoform i.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.95523.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..714
                     /product="ribosomal protein S6 kinase delta-1 isoform i"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=78840
     Region          1..>69
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <527..704
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(577,579,581,598,609..614,641,647,650)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            594..614
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..714
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349660.2:1567..3711"
                     /note="isoform i is encoded by transcript variant 19"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mdtrteqtfi lkglrkssey srnrktiipr cvpnmvclhk yiiseesvfl vlqhaeggkl
       61 wsyiskflnr speesfdike vkkptlakvh lqqptsspqd sssfesrgsd ggsmlkalpl
      121 kssltpssqd dsnqeddgqd sspkwpdsgs sseeecttsy ltlcneygqe kiepgslnee
      181 pfmktegngv dtkaiksfpa hlaadsdsps tqlrahelkf fpnddpeavs sprtsdslsr
      241 sknspmeffr idskdsasel lgldfgekly slkseplkpf ftlpdgdsas rsfntseskv
      301 efkaqdtisr gsddsvpvis fkdaafddvs gtdegrpdll vnlpgelest reaaamgptk
      361 ftqtnigiie nklleapdvl clrlsteqcq aheekgieel sdpsgpksys itekhyaqed
      421 prmlfvaavd hsssgdmsll pssdpkfqgl gvvesavtan nteeslfric splsganeyi
      481 astdtlktee vllftdqtdd lakeeptslf qrdsetkges glvlegdkei hqifedldkk
      541 lalasrfyip egciqrwaae mvvaldalhr egivcrdlnp nnillndrgh iqltyfsrws
      601 evedscdsda iermycapev gaiteeteac dwwslgavlf elltgktlve chpagintht
      661 tlnmpecvse earsliqqll qfnplerlga gvagvediks hpfftpvdwa elmr
//
LOCUS       NP_001336579             885 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform e [Homo sapiens].
ACCESSION   NP_001336579 XP_016856516
VERSION     NP_001336579.1
DBSOURCE    REFSEQ: accession NM_001349650.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 885)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 885)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 885)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 885)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 885)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 885)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 885)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 885)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            On Mar 22, 2017 this sequence version replaced XP_016856516.1.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (11), as well as variants 6, 9,
            10, and 12-14, encodes isoform e.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803611.86512.1, SRR1803612.127939.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..885
                     /product="ribosomal protein S6 kinase delta-1 isoform e"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=97742
     Region          57..131
                     /region_name="MIT_SNX15"
                     /note="MIT: domain contained within Microtubule
                     Interacting and Trafficking molecules. This MIT domain
                     sub-family is found in sorting nexin 15 and related
                     proteins. The molecular function of the MIT domain is
                     unclear; cd02677"
                     /db_xref="CDD:239140"
     Region          154..>240
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <698..875
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(748,750,752,769,780..785,812,818,821)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            765..785
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..885
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349650.2:903..3560"
                     /note="isoform e is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS73028.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 masnqnspir tfglnlssds salgavasds eqskteeere srslfpgslk pklgkrdyle
       61 kageliklal kkeeeddyea asdfyrkgvd lllegvqges sptrreavkr rtaeylmrae
      121 sisslygkpq lddvsqppgs lssrplwnlr spaeelkafr vlgvidkvll vmdtrteqtf
      181 ilkglrksse ysrnrktiip rcvpnmvclh kyiiseesvf lvlqhaeggk lwsyiskfln
      241 rspeesfdik evkkptlakv hlqqptsspq dsssfesrgs dggsmlkalp lkssltpssq
      301 ddsnqeddgq dsspkwpdsg ssseeectts yltlcneygq ekiepgslne epfmktegng
      361 vdtkaiksfp ahlaadsdsp stqlrahelk ffpnddpeav ssprtsdsls rsknspmeff
      421 ridskdsase llgldfgekl yslkseplkp fftlpdgdsa srsfntsesk vefkaqdtis
      481 rgsddsvpvi sfkdaafddv sgtdegrpdl lvnlpgeles treaaamgpt kftqtnigii
      541 enklleapdv lclrlsteqc qaheekgiee lsdpsgpksy sitekhyaqe dprmlfvaav
      601 dhsssgdmsl lpssdpkfqg lgvvesavta nnteeslfri csplsganey iastdtlkte
      661 evllftdqtd dlakeeptsl fqrdsetkge sglvlegdke ihqifedldk klalasrfyi
      721 pegciqrwaa emvvaldalh regivcrdln pnnillndrg hiqltyfsrw sevedscdsd
      781 aiermycape vgaiteetea cdwwslgavl felltgktlv echpaginth ttlnmpecvs
      841 eearsliqql lqfnplerlg agvagvedik shpfftpvdw aelmr
//
LOCUS       NP_001336587             769 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform h [Homo sapiens].
ACCESSION   NP_001336587 XP_016856518
VERSION     NP_001336587.1
DBSOURCE    REFSEQ: accession NM_001349658.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 769)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 769)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 769)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 769)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 769)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 769)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            On Mar 22, 2017 this sequence version replaced XP_016856518.1.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (17), as well as variant 16,
            encodes isoform h.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803611.11034.1, SRR1803612.98453.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..769
                     /product="ribosomal protein S6 kinase delta-1 isoform h"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=84887
     Region          38..>124
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <582..759
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(632,634,636,653,664..669,696,702,705)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            649..669
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..769
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349658.2:810..3119"
                     /note="isoform h is encoded by transcript variant 17"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mraesissly gkpqlddvsq ppgslssrpl wnlrspaeel kafrvlgvid kvllvmdtrt
       61 eqtfilkglr ksseysrnrk tiiprcvpnm vclhkyiise esvflvlqha eggklwsyis
      121 kflnrspees fdikevkkpt lakvhlqqpt sspqdsssfe srgsdggsml kalplksslt
      181 pssqddsnqe ddgqdsspkw pdsgssseee cttsyltlcn eygqekiepg slneepfmkt
      241 egngvdtkai ksfpahlaad sdspstqlra helkffpndd peavssprts dslsrsknsp
      301 meffridskd sasellgldf geklyslkse plkpfftlpd gdsasrsfnt seskvefkaq
      361 dtisrgsdds vpvisfkdaa fddvsgtdeg rpdllvnlpg elestreaaa mgptkftqtn
      421 igiienklle apdvlclrls teqcqaheek gieelsdpsg pksysitekh yaqedprmlf
      481 vaavdhsssg dmsllpssdp kfqglgvves avtanntees lfricsplsg aneyiastdt
      541 lkteevllft dqtddlakee ptslfqrdse tkgesglvle gdkeihqife dldkklalas
      601 rfyipegciq rwaaemvval dalhregivc rdlnpnnill ndrghiqlty fsrwseveds
      661 cdsdaiermy capevgaite eteacdwwsl gavlfelltg ktlvechpag inthttlnmp
      721 ecvseearsl iqqllqfnpl erlgagvagv edikshpfft pvdwaelmr
//
LOCUS       NP_001336601             571 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform j [Homo sapiens].
ACCESSION   NP_001336601
VERSION     NP_001336601.1
DBSOURCE    REFSEQ: accession NM_001349672.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 571)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 571)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 571)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 571)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 571)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 571)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (31) encodes isoform j.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.130869.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..571
                     /product="ribosomal protein S6 kinase delta-1 isoform j"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=62517
     Region          <414..561
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     CDS             1..571
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349672.2:1258..2973"
                     /note="isoform j is encoded by transcript variant 31"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mlkalplkss ltpssqddsn qeddgqdssp kwpdsgssse eecttsyltl cneygqekie
       61 pgslneepfm ktegngvdtk aiksfpahla adsdspstql rahelkffpn ddpeavsspr
      121 tsdslsrskn spmeffrids kdsasellgl dfgeklyslk seplkpfftl pdgdsasrsf
      181 ntseskvefk aqdtisrgsd dsvpvisfkd aafddvsgtd egrpdllvnl pgelestrea
      241 aamgptkftq tnigiienkl leapdvlclr lsteqcqahe ekgieelsdp sgpksysite
      301 khyaqedprm lfvaavdhss sgdmsllpss dpkfqglgvv esavtannte eslfricspl
      361 sganeyiast dtlkteevll ftdqtddlak eeptslfqrd setkgesglv legdkeihqi
      421 fedldkklal asrfyipegc iqrwaaemvv aldalhregi vcrdlnpnni llndrevgai
      481 teeteacdww slgavlfell tgktlvechp aginthttln mpecvseear sliqqllqfn
      541 plerlgagva gvedikshpf ftpvdwaelm r
//
LOCUS       NP_001336593             601 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform d [Homo sapiens].
ACCESSION   NP_001336593
VERSION     NP_001336593.1
DBSOURCE    REFSEQ: accession NM_001349664.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 601)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 601)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 601)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 601)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 601)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (23), as well as variants 5, 22,
            and 24-30, encodes isoform d.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.147380.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..601
                     /product="ribosomal protein S6 kinase delta-1 isoform d"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=66008
     Region          <414..591
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(464,466,468,485,496..501,528,534,537)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            481..501
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..601
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349664.2:1403..3208"
                     /note="isoform d is encoded by transcript variant 23"
                     /db_xref="CCDS:CCDS73030.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mlkalplkss ltpssqddsn qeddgqdssp kwpdsgssse eecttsyltl cneygqekie
       61 pgslneepfm ktegngvdtk aiksfpahla adsdspstql rahelkffpn ddpeavsspr
      121 tsdslsrskn spmeffrids kdsasellgl dfgeklyslk seplkpfftl pdgdsasrsf
      181 ntseskvefk aqdtisrgsd dsvpvisfkd aafddvsgtd egrpdllvnl pgelestrea
      241 aamgptkftq tnigiienkl leapdvlclr lsteqcqahe ekgieelsdp sgpksysite
      301 khyaqedprm lfvaavdhss sgdmsllpss dpkfqglgvv esavtannte eslfricspl
      361 sganeyiast dtlkteevll ftdqtddlak eeptslfqrd setkgesglv legdkeihqi
      421 fedldkklal asrfyipegc iqrwaaemvv aldalhregi vcrdlnpnni llndrghiql
      481 tyfsrwseve dscdsdaier mycapevgai teeteacdww slgavlfell tgktlvechp
      541 aginthttln mpecvseear sliqqllqfn plerlgagva gvedikshpf ftpvdwaelm
      601 r
//
LOCUS       NP_001336578             885 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform e [Homo sapiens].
ACCESSION   NP_001336578 XP_005273153
VERSION     NP_001336578.1
DBSOURCE    REFSEQ: accession NM_001349649.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 885)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 885)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 885)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 885)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 885)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 885)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 885)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 885)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            On Mar 22, 2017 this sequence version replaced XP_005273153.1.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (10), as well as variants 6, 9,
            and 11-14, encodes isoform e.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.141105.1,
                                           SRR1803616.25062.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..885
                     /product="ribosomal protein S6 kinase delta-1 isoform e"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=97742
     Region          57..131
                     /region_name="MIT_SNX15"
                     /note="MIT: domain contained within Microtubule
                     Interacting and Trafficking molecules. This MIT domain
                     sub-family is found in sorting nexin 15 and related
                     proteins. The molecular function of the MIT domain is
                     unclear; cd02677"
                     /db_xref="CDD:239140"
     Region          154..>240
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <698..875
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(748,750,752,769,780..785,812,818,821)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            765..785
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..885
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349649.2:825..3482"
                     /note="isoform e is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS73028.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 masnqnspir tfglnlssds salgavasds eqskteeere srslfpgslk pklgkrdyle
       61 kageliklal kkeeeddyea asdfyrkgvd lllegvqges sptrreavkr rtaeylmrae
      121 sisslygkpq lddvsqppgs lssrplwnlr spaeelkafr vlgvidkvll vmdtrteqtf
      181 ilkglrksse ysrnrktiip rcvpnmvclh kyiiseesvf lvlqhaeggk lwsyiskfln
      241 rspeesfdik evkkptlakv hlqqptsspq dsssfesrgs dggsmlkalp lkssltpssq
      301 ddsnqeddgq dsspkwpdsg ssseeectts yltlcneygq ekiepgslne epfmktegng
      361 vdtkaiksfp ahlaadsdsp stqlrahelk ffpnddpeav ssprtsdsls rsknspmeff
      421 ridskdsase llgldfgekl yslkseplkp fftlpdgdsa srsfntsesk vefkaqdtis
      481 rgsddsvpvi sfkdaafddv sgtdegrpdl lvnlpgeles treaaamgpt kftqtnigii
      541 enklleapdv lclrlsteqc qaheekgiee lsdpsgpksy sitekhyaqe dprmlfvaav
      601 dhsssgdmsl lpssdpkfqg lgvvesavta nnteeslfri csplsganey iastdtlkte
      661 evllftdqtd dlakeeptsl fqrdsetkge sglvlegdke ihqifedldk klalasrfyi
      721 pegciqrwaa emvvaldalh regivcrdln pnnillndrg hiqltyfsrw sevedscdsd
      781 aiermycape vgaiteetea cdwwslgavl felltgktlv echpaginth ttlnmpecvs
      841 eearsliqql lqfnplerlg agvagvedik shpfftpvdw aelmr
//
LOCUS       NP_001129610            1054 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform b [Homo sapiens].
ACCESSION   NP_001129610
VERSION     NP_001129610.1
DBSOURCE    REFSEQ: accession NM_001136138.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1054)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 1054)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 1054)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 1054)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 1054)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC323473.1, AK122921.1,
            AL645860.5 and AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            5' coding region, compared to variant 1. The encoded isoform (b) is
            shorter, compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK122921.1, SRR1803614.13804.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..1054
                     /product="ribosomal protein S6 kinase delta-1 isoform b"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=117142
     Region          11..116
                     /region_name="PX_domain"
                     /note="The Phox Homology domain, a phosphoinositide
                     binding module; cl02563"
                     /db_xref="CDD:470617"
     Site            order(41..43,72..73,86)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132768"
     Region          195..216
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S38.2)"
     Region          226..300
                     /region_name="MIT_SNX15"
                     /note="MIT: domain contained within Microtubule
                     Interacting and Trafficking molecules. This MIT domain
                     sub-family is found in sorting nexin 15 and related
                     proteins. The molecular function of the MIT domain is
                     unclear; cd02677"
                     /db_xref="CDD:239140"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Region          323..>409
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Region          429..497
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BLK9; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BLK9; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Region          541..584
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            596
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BLK9; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BLK9; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            782
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BLK9; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            860
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Region          <867..1044
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(917,919,921,938,949..954,981,987,990)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            934..954
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..1054
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001136138.4:165..3329"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44317.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mtsyrersad larfytvtep qrhprgytvy kvtariivwk rysdfkklhk elwqihknlf
       61 rhselfppfa kgivfgrfde tvieerrqca edllqfsani palynskqle dffkggiind
      121 sseligpaea hsdslidtfp ecstegfssd sdlvsltvdv dslaelddgm asnqnspirt
      181 fglnlssdss algavasdse qskteeeres rslfpgslkp klgkrdylek ageliklalk
      241 keeeddyeaa sdfyrkgvdl llegvqgess ptrreavkrr taeylmraes isslygkpql
      301 ddvsqppgsl ssrplwnlrs paeelkafrv lgvidkvllv mdtrteqtfi lkglrkssey
      361 srnrktiipr cvpnmvclhk yiiseesvfl vlqhaeggkl wsyiskflnr speesfdike
      421 vkkptlakvh lqqptsspqd sssfesrgsd ggsmlkalpl kssltpssqd dsnqeddgqd
      481 sspkwpdsgs sseeecttsy ltlcneygqe kiepgslnee pfmktegngv dtkaiksfpa
      541 hlaadsdsps tqlrahelkf fpnddpeavs sprtsdslsr sknspmeffr idskdsasel
      601 lgldfgekly slkseplkpf ftlpdgdsas rsfntseskv efkaqdtisr gsddsvpvis
      661 fkdaafddvs gtdegrpdll vnlpgelest reaaamgptk ftqtnigiie nklleapdvl
      721 clrlsteqcq aheekgieel sdpsgpksys itekhyaqed prmlfvaavd hsssgdmsll
      781 pssdpkfqgl gvvesavtan nteeslfric splsganeyi astdtlktee vllftdqtdd
      841 lakeeptslf qrdsetkges glvlegdkei hqifedldkk lalasrfyip egciqrwaae
      901 mvvaldalhr egivcrdlnp nnillndrgh iqltyfsrws evedscdsda iermycapev
      961 gaiteeteac dwwslgavlf elltgktlve chpagintht tlnmpecvse earsliqqll
     1021 qfnplerlga gvagvediks hpfftpvdwa elmr
//
LOCUS       NP_001336583             854 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform c [Homo sapiens].
ACCESSION   NP_001336583 XP_016856517
VERSION     NP_001336583.1
DBSOURCE    REFSEQ: accession NM_001349654.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 854)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 854)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 854)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 854)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 854)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 854)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 854)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            On Mar 22, 2017 this sequence version replaced XP_016856517.1.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (15), as well as variants 3 and 4,
            encodes isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.106098.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..854
                     /product="ribosomal protein S6 kinase delta-1 isoform c"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=94326
     Region          57..131
                     /region_name="MIT_SNX15"
                     /note="MIT: domain contained within Microtubule
                     Interacting and Trafficking molecules. This MIT domain
                     sub-family is found in sorting nexin 15 and related
                     proteins. The molecular function of the MIT domain is
                     unclear; cd02677"
                     /db_xref="CDD:239140"
     Region          134..>209
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <667..844
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(717,719,721,738,749..754,781,787,790)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            734..754
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..854
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349654.2:903..3467"
                     /note="isoform c is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS73029.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 masnqnspir tfglnlssds salgavasds eqskteeere srslfpgslk pklgkrdyle
       61 kageliklal kkeeeddyea asdfyrkgvd lllegvqges sptrreavkr rtaeylmrae
      121 sisslygkpq lddvsqvllv mdtrteqtfi lkglrkssey srnrktiipr cvpnmvclhk
      181 yiiseesvfl vlqhaeggkl wsyiskflnr speesfdike vkkptlakvh lqqptsspqd
      241 sssfesrgsd ggsmlkalpl kssltpssqd dsnqeddgqd sspkwpdsgs sseeecttsy
      301 ltlcneygqe kiepgslnee pfmktegngv dtkaiksfpa hlaadsdsps tqlrahelkf
      361 fpnddpeavs sprtsdslsr sknspmeffr idskdsasel lgldfgekly slkseplkpf
      421 ftlpdgdsas rsfntseskv efkaqdtisr gsddsvpvis fkdaafddvs gtdegrpdll
      481 vnlpgelest reaaamgptk ftqtnigiie nklleapdvl clrlsteqcq aheekgieel
      541 sdpsgpksys itekhyaqed prmlfvaavd hsssgdmsll pssdpkfqgl gvvesavtan
      601 nteeslfric splsganeyi astdtlktee vllftdqtdd lakeeptslf qrdsetkges
      661 glvlegdkei hqifedldkk lalasrfyip egciqrwaae mvvaldalhr egivcrdlnp
      721 nnillndrgh iqltyfsrws evedscdsda iermycapev gaiteeteac dwwslgavlf
      781 elltgktlve chpagintht tlnmpecvse earsliqqll qfnplerlga gvagvediks
      841 hpfftpvdwa elmr
//
LOCUS       NP_001274147             854 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform c [Homo sapiens].
ACCESSION   NP_001274147
VERSION     NP_001274147.1
DBSOURCE    REFSEQ: accession NM_001287218.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 854)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 854)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 854)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 854)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 854)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 854)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 854)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC323473.1, BC143449.1,
            AL645860.5 and AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (3) differs in its 5' UTR,
            initiates translation at a downstream start codon, and lacks an
            in-frame exon in the central coding region, compared to variant 1.
            The encoded isoform (c) is shorter, compared to isoform a. Variants
            3, 4, and 15 all encode the same isoform (c).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143449.1, SRR1803614.75393.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..854
                     /product="ribosomal protein S6 kinase delta-1 isoform c"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=94326
     Region          57..131
                     /region_name="MIT_SNX15"
                     /note="MIT: domain contained within Microtubule
                     Interacting and Trafficking molecules. This MIT domain
                     sub-family is found in sorting nexin 15 and related
                     proteins. The molecular function of the MIT domain is
                     unclear; cd02677"
                     /db_xref="CDD:239140"
     Region          134..>209
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <667..844
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(717,719,721,738,749..754,781,787,790)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            734..754
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..854
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001287218.3:786..3350"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS73029.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 masnqnspir tfglnlssds salgavasds eqskteeere srslfpgslk pklgkrdyle
       61 kageliklal kkeeeddyea asdfyrkgvd lllegvqges sptrreavkr rtaeylmrae
      121 sisslygkpq lddvsqvllv mdtrteqtfi lkglrkssey srnrktiipr cvpnmvclhk
      181 yiiseesvfl vlqhaeggkl wsyiskflnr speesfdike vkkptlakvh lqqptsspqd
      241 sssfesrgsd ggsmlkalpl kssltpssqd dsnqeddgqd sspkwpdsgs sseeecttsy
      301 ltlcneygqe kiepgslnee pfmktegngv dtkaiksfpa hlaadsdsps tqlrahelkf
      361 fpnddpeavs sprtsdslsr sknspmeffr idskdsasel lgldfgekly slkseplkpf
      421 ftlpdgdsas rsfntseskv efkaqdtisr gsddsvpvis fkdaafddvs gtdegrpdll
      481 vnlpgelest reaaamgptk ftqtnigiie nklleapdvl clrlsteqcq aheekgieel
      541 sdpsgpksys itekhyaqed prmlfvaavd hsssgdmsll pssdpkfqgl gvvesavtan
      601 nteeslfric splsganeyi astdtlktee vllftdqtdd lakeeptslf qrdsetkges
      661 glvlegdkei hqifedldkk lalasrfyip egciqrwaae mvvaldalhr egivcrdlnp
      721 nnillndrgh iqltyfsrws evedscdsda iermycapev gaiteeteac dwwslgavlf
      781 elltgktlve chpagintht tlnmpecvse earsliqqll qfnplerlga gvagvediks
      841 hpfftpvdwa elmr
//
LOCUS       NP_001336586             769 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform h [Homo sapiens].
ACCESSION   NP_001336586
VERSION     NP_001336586.1
DBSOURCE    REFSEQ: accession NM_001349657.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 769)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 769)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 769)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 769)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 769)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 769)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (16), as well as variant 17,
            encodes isoform h.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.18529.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..769
                     /product="ribosomal protein S6 kinase delta-1 isoform h"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=84887
     Region          38..>124
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <582..759
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(632,634,636,653,664..669,696,702,705)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            649..669
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..769
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349657.2:599..2908"
                     /note="isoform h is encoded by transcript variant 16"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mraesissly gkpqlddvsq ppgslssrpl wnlrspaeel kafrvlgvid kvllvmdtrt
       61 eqtfilkglr ksseysrnrk tiiprcvpnm vclhkyiise esvflvlqha eggklwsyis
      121 kflnrspees fdikevkkpt lakvhlqqpt sspqdsssfe srgsdggsml kalplksslt
      181 pssqddsnqe ddgqdsspkw pdsgssseee cttsyltlcn eygqekiepg slneepfmkt
      241 egngvdtkai ksfpahlaad sdspstqlra helkffpndd peavssprts dslsrsknsp
      301 meffridskd sasellgldf geklyslkse plkpfftlpd gdsasrsfnt seskvefkaq
      361 dtisrgsdds vpvisfkdaa fddvsgtdeg rpdllvnlpg elestreaaa mgptkftqtn
      421 igiienklle apdvlclrls teqcqaheek gieelsdpsg pksysitekh yaqedprmlf
      481 vaavdhsssg dmsllpssdp kfqglgvves avtanntees lfricsplsg aneyiastdt
      541 lkteevllft dqtddlakee ptslfqrdse tkgesglvle gdkeihqife dldkklalas
      601 rfyipegciq rwaaemvval dalhregivc rdlnpnnill ndrghiqlty fsrwseveds
      661 cdsdaiermy capevgaite eteacdwwsl gavlfelltg ktlvechpag inthttlnmp
      721 ecvseearsl iqqllqfnpl erlgagvagv edikshpfft pvdwaelmr
//
LOCUS       NP_036556               1066 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform a [Homo sapiens].
ACCESSION   NP_036556 NP_490654
VERSION     NP_036556.2
DBSOURCE    REFSEQ: accession NM_012424.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1066)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 1066)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 1066)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 1066)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 1066)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC323473.1, AK122989.1,
            AL645860.5, AL512449.6 and AL583826.16.
            
            On or before Nov 4, 2002 this sequence version replaced
            NP_490654.1, NP_036556.1.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK122989.1, AF477978.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366960.8/ ENSP00000355927.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..1066
                     /product="ribosomal protein S6 kinase delta-1 isoform a"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=118552
     Region          11..128
                     /region_name="PX_RPK118_like"
                     /note="The phosphoinositide binding Phox Homology domain
                     of RPK118-like proteins; cd07287"
                     /db_xref="CDD:132820"
     Site            order(53..55,83..84,98)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132820"
     Region          207..228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S38.2)"
     Region          238..312
                     /region_name="MIT_SNX15"
                     /note="MIT: domain contained within Microtubule
                     Interacting and Trafficking molecules. This MIT domain
                     sub-family is found in sorting nexin 15 and related
                     proteins. The molecular function of the MIT domain is
                     unclear; cd02677"
                     /db_xref="CDD:239140"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Region          335..>421
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Region          441..509
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BLK9; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            494
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BLK9; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Region          553..596
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BLK9; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BLK9; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            794
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BLK9; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Site            872
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96S38.2)"
     Region          <879..1056
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(929,931,933,950,961..966,993,999,1002)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            946..966
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..1066
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_012424.6:165..3365"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1513.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mtsyrersad larfytvtep qrhprgytvy kvtarvvsrr npedvqeiiv wkrysdfkkl
       61 hkelwqihkn lfrhselfpp fakgivfgrf detvieerrq caedllqfsa nipalynskq
      121 ledffkggii ndsseligpa eahsdslidt fpecstegfs sdsdlvsltv dvdslaeldd
      181 gmasnqnspi rtfglnlssd ssalgavasd seqskteeer esrslfpgsl kpklgkrdyl
      241 ekagelikla lkkeeeddye aasdfyrkgv dlllegvqge ssptrreavk rrtaeylmra
      301 esisslygkp qlddvsqppg slssrplwnl rspaeelkaf rvlgvidkvl lvmdtrteqt
      361 filkglrkss eysrnrktii prcvpnmvcl hkyiiseesv flvlqhaegg klwsyiskfl
      421 nrspeesfdi kevkkptlak vhlqqptssp qdsssfesrg sdggsmlkal plkssltpss
      481 qddsnqeddg qdsspkwpds gssseeectt syltlcneyg qekiepgsln eepfmktegn
      541 gvdtkaiksf pahlaadsds pstqlrahel kffpnddpea vssprtsdsl srsknspmef
      601 fridskdsas ellgldfgek lyslkseplk pfftlpdgds asrsfntses kvefkaqdti
      661 srgsddsvpv isfkdaafdd vsgtdegrpd llvnlpgele streaaamgp tkftqtnigi
      721 ienklleapd vlclrlsteq cqaheekgie elsdpsgpks ysitekhyaq edprmlfvaa
      781 vdhsssgdms llpssdpkfq glgvvesavt annteeslfr icsplsgane yiastdtlkt
      841 eevllftdqt ddlakeepts lfqrdsetkg esglvlegdk eihqifedld kklalasrfy
      901 ipegciqrwa aemvvaldal hregivcrdl npnnillndr ghiqltyfsr wsevedscds
      961 daiermycap evgaiteete acdwwslgav lfelltgktl vechpagint httlnmpecv
     1021 seearsliqq llqfnplerl gagvagvedi kshpfftpvd waelmr
//
LOCUS       NP_001336598             601 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform d [Homo sapiens].
ACCESSION   NP_001336598 XP_016856523
VERSION     NP_001336598.1
DBSOURCE    REFSEQ: accession NM_001349669.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 601)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 601)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 601)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 601)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 601)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            On Mar 22, 2017 this sequence version replaced XP_016856523.1.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (28), as well as variants 5,
            23-27, 29, and 30, encodes isoform d.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.95761.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..601
                     /product="ribosomal protein S6 kinase delta-1 isoform d"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=66008
     Region          <414..591
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(464,466,468,485,496..501,528,534,537)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            481..501
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..601
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349669.2:1574..3379"
                     /note="isoform d is encoded by transcript variant 28"
                     /db_xref="CCDS:CCDS73030.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mlkalplkss ltpssqddsn qeddgqdssp kwpdsgssse eecttsyltl cneygqekie
       61 pgslneepfm ktegngvdtk aiksfpahla adsdspstql rahelkffpn ddpeavsspr
      121 tsdslsrskn spmeffrids kdsasellgl dfgeklyslk seplkpfftl pdgdsasrsf
      181 ntseskvefk aqdtisrgsd dsvpvisfkd aafddvsgtd egrpdllvnl pgelestrea
      241 aamgptkftq tnigiienkl leapdvlclr lsteqcqahe ekgieelsdp sgpksysite
      301 khyaqedprm lfvaavdhss sgdmsllpss dpkfqglgvv esavtannte eslfricspl
      361 sganeyiast dtlkteevll ftdqtddlak eeptslfqrd setkgesglv legdkeihqi
      421 fedldkklal asrfyipegc iqrwaaemvv aldalhregi vcrdlnpnni llndrghiql
      481 tyfsrwseve dscdsdaier mycapevgai teeteacdww slgavlfell tgktlvechp
      541 aginthttln mpecvseear sliqqllqfn plerlgagva gvedikshpf ftpvdwaelm
      601 r
//
LOCUS       NP_001336590             714 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform i [Homo sapiens].
ACCESSION   NP_001336590
VERSION     NP_001336590.1
DBSOURCE    REFSEQ: accession NM_001349661.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 714)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 714)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 714)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 714)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 714)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 714)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (20), as well as variants 18, 19,
            and 21, encodes isoform i.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.46354.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..714
                     /product="ribosomal protein S6 kinase delta-1 isoform i"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=78840
     Region          1..>69
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <527..704
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(577,579,581,598,609..614,641,647,650)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            594..614
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..714
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349661.2:1251..3395"
                     /note="isoform i is encoded by transcript variant 20"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mdtrteqtfi lkglrkssey srnrktiipr cvpnmvclhk yiiseesvfl vlqhaeggkl
       61 wsyiskflnr speesfdike vkkptlakvh lqqptsspqd sssfesrgsd ggsmlkalpl
      121 kssltpssqd dsnqeddgqd sspkwpdsgs sseeecttsy ltlcneygqe kiepgslnee
      181 pfmktegngv dtkaiksfpa hlaadsdsps tqlrahelkf fpnddpeavs sprtsdslsr
      241 sknspmeffr idskdsasel lgldfgekly slkseplkpf ftlpdgdsas rsfntseskv
      301 efkaqdtisr gsddsvpvis fkdaafddvs gtdegrpdll vnlpgelest reaaamgptk
      361 ftqtnigiie nklleapdvl clrlsteqcq aheekgieel sdpsgpksys itekhyaqed
      421 prmlfvaavd hsssgdmsll pssdpkfqgl gvvesavtan nteeslfric splsganeyi
      481 astdtlktee vllftdqtdd lakeeptslf qrdsetkges glvlegdkei hqifedldkk
      541 lalasrfyip egciqrwaae mvvaldalhr egivcrdlnp nnillndrgh iqltyfsrws
      601 evedscdsda iermycapev gaiteeteac dwwslgavlf elltgktlve chpagintht
      661 tlnmpecvse earsliqqll qfnplerlga gvagvediks hpfftpvdwa elmr
//
LOCUS       NP_001336581             885 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform e [Homo sapiens].
ACCESSION   NP_001336581
VERSION     NP_001336581.1
DBSOURCE    REFSEQ: accession NM_001349652.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 885)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 885)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 885)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 885)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 885)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 885)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 885)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 885)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (13), as well as variants 6, 9-12,
            and 14, encodes isoform e.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.56982.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..885
                     /product="ribosomal protein S6 kinase delta-1 isoform e"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=97742
     Region          57..131
                     /region_name="MIT_SNX15"
                     /note="MIT: domain contained within Microtubule
                     Interacting and Trafficking molecules. This MIT domain
                     sub-family is found in sorting nexin 15 and related
                     proteins. The molecular function of the MIT domain is
                     unclear; cd02677"
                     /db_xref="CDD:239140"
     Region          154..>240
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <698..875
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(748,750,752,769,780..785,812,818,821)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            765..785
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..885
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349652.2:857..3514"
                     /note="isoform e is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS73028.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 masnqnspir tfglnlssds salgavasds eqskteeere srslfpgslk pklgkrdyle
       61 kageliklal kkeeeddyea asdfyrkgvd lllegvqges sptrreavkr rtaeylmrae
      121 sisslygkpq lddvsqppgs lssrplwnlr spaeelkafr vlgvidkvll vmdtrteqtf
      181 ilkglrksse ysrnrktiip rcvpnmvclh kyiiseesvf lvlqhaeggk lwsyiskfln
      241 rspeesfdik evkkptlakv hlqqptsspq dsssfesrgs dggsmlkalp lkssltpssq
      301 ddsnqeddgq dsspkwpdsg ssseeectts yltlcneygq ekiepgslne epfmktegng
      361 vdtkaiksfp ahlaadsdsp stqlrahelk ffpnddpeav ssprtsdsls rsknspmeff
      421 ridskdsase llgldfgekl yslkseplkp fftlpdgdsa srsfntsesk vefkaqdtis
      481 rgsddsvpvi sfkdaafddv sgtdegrpdl lvnlpgeles treaaamgpt kftqtnigii
      541 enklleapdv lclrlsteqc qaheekgiee lsdpsgpksy sitekhyaqe dprmlfvaav
      601 dhsssgdmsl lpssdpkfqg lgvvesavta nnteeslfri csplsganey iastdtlkte
      661 evllftdqtd dlakeeptsl fqrdsetkge sglvlegdke ihqifedldk klalasrfyi
      721 pegciqrwaa emvvaldalh regivcrdln pnnillndrg hiqltyfsrw sevedscdsd
      781 aiermycape vgaiteetea cdwwslgavl felltgktlv echpaginth ttlnmpecvs
      841 eearsliqql lqfnplerlg agvagvedik shpfftpvdw aelmr
//
LOCUS       NP_001274148             854 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform c [Homo sapiens].
ACCESSION   NP_001274148 XP_005273154
VERSION     NP_001274148.1
DBSOURCE    REFSEQ: accession NM_001287219.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 854)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 854)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 854)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 854)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 854)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 854)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 854)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC323473.1, AK299298.1,
            AL645860.5, AL512449.6 and AL583826.16.
            
            On Dec 10, 2013 this sequence version replaced XP_005273154.1.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (4) differs in its 5' UTR,
            initiates translation at a downstream start codon, and lacks an
            in-frame exon in the central coding region, compared to variant 1.
            The encoded isoform (c) is shorter, compared to isoform a. Variants
            3, 4, and 15 all encode the same isoform (c).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK299298.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..854
                     /product="ribosomal protein S6 kinase delta-1 isoform c"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=94326
     Region          57..131
                     /region_name="MIT_SNX15"
                     /note="MIT: domain contained within Microtubule
                     Interacting and Trafficking molecules. This MIT domain
                     sub-family is found in sorting nexin 15 and related
                     proteins. The molecular function of the MIT domain is
                     unclear; cd02677"
                     /db_xref="CDD:239140"
     Region          134..>209
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <667..844
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(717,719,721,738,749..754,781,787,790)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            734..754
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..854
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001287219.3:825..3389"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS73029.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 masnqnspir tfglnlssds salgavasds eqskteeere srslfpgslk pklgkrdyle
       61 kageliklal kkeeeddyea asdfyrkgvd lllegvqges sptrreavkr rtaeylmrae
      121 sisslygkpq lddvsqvllv mdtrteqtfi lkglrkssey srnrktiipr cvpnmvclhk
      181 yiiseesvfl vlqhaeggkl wsyiskflnr speesfdike vkkptlakvh lqqptsspqd
      241 sssfesrgsd ggsmlkalpl kssltpssqd dsnqeddgqd sspkwpdsgs sseeecttsy
      301 ltlcneygqe kiepgslnee pfmktegngv dtkaiksfpa hlaadsdsps tqlrahelkf
      361 fpnddpeavs sprtsdslsr sknspmeffr idskdsasel lgldfgekly slkseplkpf
      421 ftlpdgdsas rsfntseskv efkaqdtisr gsddsvpvis fkdaafddvs gtdegrpdll
      481 vnlpgelest reaaamgptk ftqtnigiie nklleapdvl clrlsteqcq aheekgieel
      541 sdpsgpksys itekhyaqed prmlfvaavd hsssgdmsll pssdpkfqgl gvvesavtan
      601 nteeslfric splsganeyi astdtlktee vllftdqtdd lakeeptslf qrdsetkges
      661 glvlegdkei hqifedldkk lalasrfyip egciqrwaae mvvaldalhr egivcrdlnp
      721 nnillndrgh iqltyfsrws evedscdsda iermycapev gaiteeteac dwwslgavlf
      781 elltgktlve chpagintht tlnmpecvse earsliqqll qfnplerlga gvagvediks
      841 hpfftpvdwa elmr
//
LOCUS       NP_001336580             885 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform e [Homo sapiens].
ACCESSION   NP_001336580
VERSION     NP_001336580.1
DBSOURCE    REFSEQ: accession NM_001349651.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 885)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 885)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 885)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 885)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 885)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 885)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 885)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 885)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (12), as well as variants 6, 9-11,
            13, and 14, encodes isoform e.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.237310.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..885
                     /product="ribosomal protein S6 kinase delta-1 isoform e"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=97742
     Region          57..131
                     /region_name="MIT_SNX15"
                     /note="MIT: domain contained within Microtubule
                     Interacting and Trafficking molecules. This MIT domain
                     sub-family is found in sorting nexin 15 and related
                     proteins. The molecular function of the MIT domain is
                     unclear; cd02677"
                     /db_xref="CDD:239140"
     Region          154..>240
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <698..875
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(748,750,752,769,780..785,812,818,821)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            765..785
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..885
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349651.2:1024..3681"
                     /note="isoform e is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS73028.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 masnqnspir tfglnlssds salgavasds eqskteeere srslfpgslk pklgkrdyle
       61 kageliklal kkeeeddyea asdfyrkgvd lllegvqges sptrreavkr rtaeylmrae
      121 sisslygkpq lddvsqppgs lssrplwnlr spaeelkafr vlgvidkvll vmdtrteqtf
      181 ilkglrksse ysrnrktiip rcvpnmvclh kyiiseesvf lvlqhaeggk lwsyiskfln
      241 rspeesfdik evkkptlakv hlqqptsspq dsssfesrgs dggsmlkalp lkssltpssq
      301 ddsnqeddgq dsspkwpdsg ssseeectts yltlcneygq ekiepgslne epfmktegng
      361 vdtkaiksfp ahlaadsdsp stqlrahelk ffpnddpeav ssprtsdsls rsknspmeff
      421 ridskdsase llgldfgekl yslkseplkp fftlpdgdsa srsfntsesk vefkaqdtis
      481 rgsddsvpvi sfkdaafddv sgtdegrpdl lvnlpgeles treaaamgpt kftqtnigii
      541 enklleapdv lclrlsteqc qaheekgiee lsdpsgpksy sitekhyaqe dprmlfvaav
      601 dhsssgdmsl lpssdpkfqg lgvvesavta nnteeslfri csplsganey iastdtlkte
      661 evllftdqtd dlakeeptsl fqrdsetkge sglvlegdke ihqifedldk klalasrfyi
      721 pegciqrwaa emvvaldalh regivcrdln pnnillndrg hiqltyfsrw sevedscdsd
      781 aiermycape vgaiteetea cdwwslgavl felltgktlv echpaginth ttlnmpecvs
      841 eearsliqql lqfnplerlg agvagvedik shpfftpvdw aelmr
//
LOCUS       NP_001274150             885 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform e [Homo sapiens].
ACCESSION   NP_001274150
VERSION     NP_001274150.1
DBSOURCE    REFSEQ: accession NM_001287221.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 885)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 885)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 885)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 885)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 885)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 885)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 885)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 885)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC323473.1, BC143474.1 and
            AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (6) differs in its 5' UTR and
            initiates translation at a downstream start codon, compared to
            variant 1. The encoded isoform (e) has a shorter N-terminus,
            compared to isoform a. Variants 6 and 9-14 all encode the same
            isoform (e).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143474.1, SRR1803616.82418.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..885
                     /product="ribosomal protein S6 kinase delta-1 isoform e"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=97742
     Region          57..131
                     /region_name="MIT_SNX15"
                     /note="MIT: domain contained within Microtubule
                     Interacting and Trafficking molecules. This MIT domain
                     sub-family is found in sorting nexin 15 and related
                     proteins. The molecular function of the MIT domain is
                     unclear; cd02677"
                     /db_xref="CDD:239140"
     Region          154..>240
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <698..875
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(748,750,752,769,780..785,812,818,821)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            765..785
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..885
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001287221.3:587..3244"
                     /note="isoform e is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS73028.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 masnqnspir tfglnlssds salgavasds eqskteeere srslfpgslk pklgkrdyle
       61 kageliklal kkeeeddyea asdfyrkgvd lllegvqges sptrreavkr rtaeylmrae
      121 sisslygkpq lddvsqppgs lssrplwnlr spaeelkafr vlgvidkvll vmdtrteqtf
      181 ilkglrksse ysrnrktiip rcvpnmvclh kyiiseesvf lvlqhaeggk lwsyiskfln
      241 rspeesfdik evkkptlakv hlqqptsspq dsssfesrgs dggsmlkalp lkssltpssq
      301 ddsnqeddgq dsspkwpdsg ssseeectts yltlcneygq ekiepgslne epfmktegng
      361 vdtkaiksfp ahlaadsdsp stqlrahelk ffpnddpeav ssprtsdsls rsknspmeff
      421 ridskdsase llgldfgekl yslkseplkp fftlpdgdsa srsfntsesk vefkaqdtis
      481 rgsddsvpvi sfkdaafddv sgtdegrpdl lvnlpgeles treaaamgpt kftqtnigii
      541 enklleapdv lclrlsteqc qaheekgiee lsdpsgpksy sitekhyaqe dprmlfvaav
      601 dhsssgdmsl lpssdpkfqg lgvvesavta nnteeslfri csplsganey iastdtlkte
      661 evllftdqtd dlakeeptsl fqrdsetkge sglvlegdke ihqifedldk klalasrfyi
      721 pegciqrwaa emvvaldalh regivcrdln pnnillndrg hiqltyfsrw sevedscdsd
      781 aiermycape vgaiteetea cdwwslgavl felltgktlv echpaginth ttlnmpecvs
      841 eearsliqql lqfnplerlg agvagvedik shpfftpvdw aelmr
//
LOCUS       NP_001336576             945 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform g [Homo sapiens].
ACCESSION   NP_001336576 XP_006711335
VERSION     NP_001336576.1
DBSOURCE    REFSEQ: accession NM_001349647.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 945)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 945)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 945)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 945)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 945)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 945)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 945)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 945)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            On Mar 22, 2017 this sequence version replaced XP_006711335.1.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (8) encodes isoform g.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
FEATURES             Location/Qualifiers
     source          1..945
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..945
                     /product="ribosomal protein S6 kinase delta-1 isoform g"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=105446
     Region          11..128
                     /region_name="PX_RPK118_like"
                     /note="The phosphoinositide binding Phox Homology domain
                     of RPK118-like proteins; cd07287"
                     /db_xref="CDD:132820"
     Site            order(53..55,83..84,98)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132820"
     Region          <158..191
                     /region_name="MIT"
                     /note="domain contained within Microtubule Interacting and
                     Trafficking molecules. The MIT domain is found in sorting
                     nexins, the nuclear thiol protease PalBH, the AAA protein
                     spastin and archaebacterial proteins with similar domain
                     architecture, vacuolar...; cl00299"
                     /db_xref="CDD:469712"
     Region          214..>300
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <758..935
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(808,810,812,829,840..845,872,878,881)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            825..845
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..945
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349647.2:165..3002"
                     /note="isoform g is encoded by transcript variant 8"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mtsyrersad larfytvtep qrhprgytvy kvtarvvsrr npedvqeiiv wkrysdfkkl
       61 hkelwqihkn lfrhselfpp fakgivfgrf detvieerrq caedllqfsa nipalynskq
      121 ledffkggii ndsseligpa eahsdslidt fpecsteges sptrreavkr rtaeylmrae
      181 sisslygkpq lddvsqppgs lssrplwnlr spaeelkafr vlgvidkvll vmdtrteqtf
      241 ilkglrksse ysrnrktiip rcvpnmvclh kyiiseesvf lvlqhaeggk lwsyiskfln
      301 rspeesfdik evkkptlakv hlqqptsspq dsssfesrgs dggsmlkalp lkssltpssq
      361 ddsnqeddgq dsspkwpdsg ssseeectts yltlcneygq ekiepgslne epfmktegng
      421 vdtkaiksfp ahlaadsdsp stqlrahelk ffpnddpeav ssprtsdsls rsknspmeff
      481 ridskdsase llgldfgekl yslkseplkp fftlpdgdsa srsfntsesk vefkaqdtis
      541 rgsddsvpvi sfkdaafddv sgtdegrpdl lvnlpgeles treaaamgpt kftqtnigii
      601 enklleapdv lclrlsteqc qaheekgiee lsdpsgpksy sitekhyaqe dprmlfvaav
      661 dhsssgdmsl lpssdpkfqg lgvvesavta nnteeslfri csplsganey iastdtlkte
      721 evllftdqtd dlakeeptsl fqrdsetkge sglvlegdke ihqifedldk klalasrfyi
      781 pegciqrwaa emvvaldalh regivcrdln pnnillndrg hiqltyfsrw sevedscdsd
      841 aiermycape vgaiteetea cdwwslgavl felltgktlv echpaginth ttlnmpecvs
      901 eearsliqql lqfnplerlg agvagvedik shpfftpvdw aelmr
//
LOCUS       NP_001336577             885 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform e [Homo sapiens].
ACCESSION   NP_001336577 XP_016856515
VERSION     NP_001336577.1
DBSOURCE    REFSEQ: accession NM_001349648.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 885)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 885)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 885)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 885)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 885)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 885)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 885)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 885)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            On Mar 22, 2017 this sequence version replaced XP_016856515.1.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (9), as well as variants 6 and
            10-14, encodes isoform e.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.99359.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..885
                     /product="ribosomal protein S6 kinase delta-1 isoform e"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=97742
     Region          57..131
                     /region_name="MIT_SNX15"
                     /note="MIT: domain contained within Microtubule
                     Interacting and Trafficking molecules. This MIT domain
                     sub-family is found in sorting nexin 15 and related
                     proteins. The molecular function of the MIT domain is
                     unclear; cd02677"
                     /db_xref="CDD:239140"
     Region          154..>240
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <698..875
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(748,750,752,769,780..785,812,818,821)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            765..785
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..885
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349648.2:777..3434"
                     /note="isoform e is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS73028.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 masnqnspir tfglnlssds salgavasds eqskteeere srslfpgslk pklgkrdyle
       61 kageliklal kkeeeddyea asdfyrkgvd lllegvqges sptrreavkr rtaeylmrae
      121 sisslygkpq lddvsqppgs lssrplwnlr spaeelkafr vlgvidkvll vmdtrteqtf
      181 ilkglrksse ysrnrktiip rcvpnmvclh kyiiseesvf lvlqhaeggk lwsyiskfln
      241 rspeesfdik evkkptlakv hlqqptsspq dsssfesrgs dggsmlkalp lkssltpssq
      301 ddsnqeddgq dsspkwpdsg ssseeectts yltlcneygq ekiepgslne epfmktegng
      361 vdtkaiksfp ahlaadsdsp stqlrahelk ffpnddpeav ssprtsdsls rsknspmeff
      421 ridskdsase llgldfgekl yslkseplkp fftlpdgdsa srsfntsesk vefkaqdtis
      481 rgsddsvpvi sfkdaafddv sgtdegrpdl lvnlpgeles treaaamgpt kftqtnigii
      541 enklleapdv lclrlsteqc qaheekgiee lsdpsgpksy sitekhyaqe dprmlfvaav
      601 dhsssgdmsl lpssdpkfqg lgvvesavta nnteeslfri csplsganey iastdtlkte
      661 evllftdqtd dlakeeptsl fqrdsetkge sglvlegdke ihqifedldk klalasrfyi
      721 pegciqrwaa emvvaldalh regivcrdln pnnillndrg hiqltyfsrw sevedscdsd
      781 aiermycape vgaiteetea cdwwslgavl felltgktlv echpaginth ttlnmpecvs
      841 eearsliqql lqfnplerlg agvagvedik shpfftpvdw aelmr
//
LOCUS       NP_001336575            1035 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform f [Homo sapiens].
ACCESSION   NP_001336575 XP_005273152
VERSION     NP_001336575.1
DBSOURCE    REFSEQ: accession NM_001349646.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1035)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 1035)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 1035)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 1035)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 1035)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            On Mar 22, 2017 this sequence version replaced XP_005273152.1.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (7) encodes isoform f.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.124466.1,
                                           SRR1803612.181216.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..1035
                     /product="ribosomal protein S6 kinase delta-1 isoform f"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=115136
     Region          11..128
                     /region_name="PX_RPK118_like"
                     /note="The phosphoinositide binding Phox Homology domain
                     of RPK118-like proteins; cd07287"
                     /db_xref="CDD:132820"
     Site            order(53..55,83..84,98)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132820"
     Region          238..312
                     /region_name="MIT_SNX15"
                     /note="MIT: domain contained within Microtubule
                     Interacting and Trafficking molecules. This MIT domain
                     sub-family is found in sorting nexin 15 and related
                     proteins. The molecular function of the MIT domain is
                     unclear; cd02677"
                     /db_xref="CDD:239140"
     Region          315..>390
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <848..1025
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(898,900,902,919,930..935,962,968,971)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            915..935
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..1035
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349646.2:165..3272"
                     /note="isoform f is encoded by transcript variant 7"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mtsyrersad larfytvtep qrhprgytvy kvtarvvsrr npedvqeiiv wkrysdfkkl
       61 hkelwqihkn lfrhselfpp fakgivfgrf detvieerrq caedllqfsa nipalynskq
      121 ledffkggii ndsseligpa eahsdslidt fpecstegfs sdsdlvsltv dvdslaeldd
      181 gmasnqnspi rtfglnlssd ssalgavasd seqskteeer esrslfpgsl kpklgkrdyl
      241 ekagelikla lkkeeeddye aasdfyrkgv dlllegvqge ssptrreavk rrtaeylmra
      301 esisslygkp qlddvsqvll vmdtrteqtf ilkglrksse ysrnrktiip rcvpnmvclh
      361 kyiiseesvf lvlqhaeggk lwsyiskfln rspeesfdik evkkptlakv hlqqptsspq
      421 dsssfesrgs dggsmlkalp lkssltpssq ddsnqeddgq dsspkwpdsg ssseeectts
      481 yltlcneygq ekiepgslne epfmktegng vdtkaiksfp ahlaadsdsp stqlrahelk
      541 ffpnddpeav ssprtsdsls rsknspmeff ridskdsase llgldfgekl yslkseplkp
      601 fftlpdgdsa srsfntsesk vefkaqdtis rgsddsvpvi sfkdaafddv sgtdegrpdl
      661 lvnlpgeles treaaamgpt kftqtnigii enklleapdv lclrlsteqc qaheekgiee
      721 lsdpsgpksy sitekhyaqe dprmlfvaav dhsssgdmsl lpssdpkfqg lgvvesavta
      781 nnteeslfri csplsganey iastdtlkte evllftdqtd dlakeeptsl fqrdsetkge
      841 sglvlegdke ihqifedldk klalasrfyi pegciqrwaa emvvaldalh regivcrdln
      901 pnnillndrg hiqltyfsrw sevedscdsd aiermycape vgaiteetea cdwwslgavl
      961 felltgktlv echpaginth ttlnmpecvs eearsliqql lqfnplerlg agvagvedik
     1021 shpfftpvdw aelmr
//
LOCUS       NP_001336588             714 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform i [Homo sapiens].
ACCESSION   NP_001336588
VERSION     NP_001336588.1
DBSOURCE    REFSEQ: accession NM_001349659.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 714)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 714)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 714)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 714)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 714)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 714)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (18), as well as variants 19-21,
            encodes isoform i.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.607.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..714
                     /product="ribosomal protein S6 kinase delta-1 isoform i"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=78840
     Region          1..>69
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <527..704
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(577,579,581,598,609..614,641,647,650)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            594..614
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..714
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349659.2:1452..3596"
                     /note="isoform i is encoded by transcript variant 18"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mdtrteqtfi lkglrkssey srnrktiipr cvpnmvclhk yiiseesvfl vlqhaeggkl
       61 wsyiskflnr speesfdike vkkptlakvh lqqptsspqd sssfesrgsd ggsmlkalpl
      121 kssltpssqd dsnqeddgqd sspkwpdsgs sseeecttsy ltlcneygqe kiepgslnee
      181 pfmktegngv dtkaiksfpa hlaadsdsps tqlrahelkf fpnddpeavs sprtsdslsr
      241 sknspmeffr idskdsasel lgldfgekly slkseplkpf ftlpdgdsas rsfntseskv
      301 efkaqdtisr gsddsvpvis fkdaafddvs gtdegrpdll vnlpgelest reaaamgptk
      361 ftqtnigiie nklleapdvl clrlsteqcq aheekgieel sdpsgpksys itekhyaqed
      421 prmlfvaavd hsssgdmsll pssdpkfqgl gvvesavtan nteeslfric splsganeyi
      481 astdtlktee vllftdqtdd lakeeptslf qrdsetkges glvlegdkei hqifedldkk
      541 lalasrfyip egciqrwaae mvvaldalhr egivcrdlnp nnillndrgh iqltyfsrws
      601 evedscdsda iermycapev gaiteeteac dwwslgavlf elltgktlve chpagintht
      661 tlnmpecvse earsliqqll qfnplerlga gvagvediks hpfftpvdwa elmr
//
LOCUS       NP_001336600             601 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform d [Homo sapiens].
ACCESSION   NP_001336600
VERSION     NP_001336600.1
DBSOURCE    REFSEQ: accession NM_001349671.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 601)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 601)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 601)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 601)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 601)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (30), as well as variants 5 and
            23-29, encodes isoform d.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.268771.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..601
                     /product="ribosomal protein S6 kinase delta-1 isoform d"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=66008
     Region          <414..591
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(464,466,468,485,496..501,528,534,537)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            481..501
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..601
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349671.2:1354..3159"
                     /note="isoform d is encoded by transcript variant 30"
                     /db_xref="CCDS:CCDS73030.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mlkalplkss ltpssqddsn qeddgqdssp kwpdsgssse eecttsyltl cneygqekie
       61 pgslneepfm ktegngvdtk aiksfpahla adsdspstql rahelkffpn ddpeavsspr
      121 tsdslsrskn spmeffrids kdsasellgl dfgeklyslk seplkpfftl pdgdsasrsf
      181 ntseskvefk aqdtisrgsd dsvpvisfkd aafddvsgtd egrpdllvnl pgelestrea
      241 aamgptkftq tnigiienkl leapdvlclr lsteqcqahe ekgieelsdp sgpksysite
      301 khyaqedprm lfvaavdhss sgdmsllpss dpkfqglgvv esavtannte eslfricspl
      361 sganeyiast dtlkteevll ftdqtddlak eeptslfqrd setkgesglv legdkeihqi
      421 fedldkklal asrfyipegc iqrwaaemvv aldalhregi vcrdlnpnni llndrghiql
      481 tyfsrwseve dscdsdaier mycapevgai teeteacdww slgavlfell tgktlvechp
      541 aginthttln mpecvseear sliqqllqfn plerlgagva gvedikshpf ftpvdwaelm
      601 r
//
LOCUS       NP_001274149             601 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform d [Homo sapiens].
ACCESSION   NP_001274149
VERSION     NP_001274149.1
DBSOURCE    REFSEQ: accession NM_001287220.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 601)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 601)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 601)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 601)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 601)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC323473.1, BC143473.1,
            AL645860.5 and AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (5) differs in its 5' UTR and
            initiates translation at a downstream start codon, compared to
            variant 1. The encoded isoform (d) has a shorter N-terminus,
            compared to isoform a. Variants 5 and 22-30 all encode the same
            isoform (d).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143473.1, SRR1660809.52191.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..601
                     /product="ribosomal protein S6 kinase delta-1 isoform d"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=66008
     Region          <414..591
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(464,466,468,485,496..501,528,534,537)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            481..501
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..601
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001287220.3:1379..3184"
                     /note="isoform d is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS73030.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mlkalplkss ltpssqddsn qeddgqdssp kwpdsgssse eecttsyltl cneygqekie
       61 pgslneepfm ktegngvdtk aiksfpahla adsdspstql rahelkffpn ddpeavsspr
      121 tsdslsrskn spmeffrids kdsasellgl dfgeklyslk seplkpfftl pdgdsasrsf
      181 ntseskvefk aqdtisrgsd dsvpvisfkd aafddvsgtd egrpdllvnl pgelestrea
      241 aamgptkftq tnigiienkl leapdvlclr lsteqcqahe ekgieelsdp sgpksysite
      301 khyaqedprm lfvaavdhss sgdmsllpss dpkfqglgvv esavtannte eslfricspl
      361 sganeyiast dtlkteevll ftdqtddlak eeptslfqrd setkgesglv legdkeihqi
      421 fedldkklal asrfyipegc iqrwaaemvv aldalhregi vcrdlnpnni llndrghiql
      481 tyfsrwseve dscdsdaier mycapevgai teeteacdww slgavlfell tgktlvechp
      541 aginthttln mpecvseear sliqqllqfn plerlgagva gvedikshpf ftpvdwaelm
      601 r
//
LOCUS       NP_001336595             601 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform d [Homo sapiens].
ACCESSION   NP_001336595 XP_016856522
VERSION     NP_001336595.1
DBSOURCE    REFSEQ: accession NM_001349666.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 601)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 601)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 601)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 601)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 601)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            On Mar 22, 2017 this sequence version replaced XP_016856522.1.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (25), as well as variants 5, 23,
            24, and 26-30, encodes isoform d.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.23302.1,
                                           SRR1803614.234057.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..601
                     /product="ribosomal protein S6 kinase delta-1 isoform d"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=66008
     Region          <414..591
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(464,466,468,485,496..501,528,534,537)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            481..501
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..601
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349666.2:1496..3301"
                     /note="isoform d is encoded by transcript variant 25"
                     /db_xref="CCDS:CCDS73030.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mlkalplkss ltpssqddsn qeddgqdssp kwpdsgssse eecttsyltl cneygqekie
       61 pgslneepfm ktegngvdtk aiksfpahla adsdspstql rahelkffpn ddpeavsspr
      121 tsdslsrskn spmeffrids kdsasellgl dfgeklyslk seplkpfftl pdgdsasrsf
      181 ntseskvefk aqdtisrgsd dsvpvisfkd aafddvsgtd egrpdllvnl pgelestrea
      241 aamgptkftq tnigiienkl leapdvlclr lsteqcqahe ekgieelsdp sgpksysite
      301 khyaqedprm lfvaavdhss sgdmsllpss dpkfqglgvv esavtannte eslfricspl
      361 sganeyiast dtlkteevll ftdqtddlak eeptslfqrd setkgesglv legdkeihqi
      421 fedldkklal asrfyipegc iqrwaaemvv aldalhregi vcrdlnpnni llndrghiql
      481 tyfsrwseve dscdsdaier mycapevgai teeteacdww slgavlfell tgktlvechp
      541 aginthttln mpecvseear sliqqllqfn plerlgagva gvedikshpf ftpvdwaelm
      601 r
//
LOCUS       NP_001336599             601 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform d [Homo sapiens].
ACCESSION   NP_001336599
VERSION     NP_001336599.1
DBSOURCE    REFSEQ: accession NM_001349670.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 601)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 601)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 601)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 601)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 601)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (29), as well as variants 5,
            23-28, and 30, encodes isoform d.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.171855.1,
                                           SRR1660803.134115.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..601
                     /product="ribosomal protein S6 kinase delta-1 isoform d"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=66008
     Region          <414..591
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(464,466,468,485,496..501,528,534,537)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            481..501
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..601
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349670.2:1286..3091"
                     /note="isoform d is encoded by transcript variant 29"
                     /db_xref="CCDS:CCDS73030.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mlkalplkss ltpssqddsn qeddgqdssp kwpdsgssse eecttsyltl cneygqekie
       61 pgslneepfm ktegngvdtk aiksfpahla adsdspstql rahelkffpn ddpeavsspr
      121 tsdslsrskn spmeffrids kdsasellgl dfgeklyslk seplkpfftl pdgdsasrsf
      181 ntseskvefk aqdtisrgsd dsvpvisfkd aafddvsgtd egrpdllvnl pgelestrea
      241 aamgptkftq tnigiienkl leapdvlclr lsteqcqahe ekgieelsdp sgpksysite
      301 khyaqedprm lfvaavdhss sgdmsllpss dpkfqglgvv esavtannte eslfricspl
      361 sganeyiast dtlkteevll ftdqtddlak eeptslfqrd setkgesglv legdkeihqi
      421 fedldkklal asrfyipegc iqrwaaemvv aldalhregi vcrdlnpnni llndrghiql
      481 tyfsrwseve dscdsdaier mycapevgai teeteacdww slgavlfell tgktlvechp
      541 aginthttln mpecvseear sliqqllqfn plerlgagva gvedikshpf ftpvdwaelm
      601 r
//
LOCUS       NP_001336582             885 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform e [Homo sapiens].
ACCESSION   NP_001336582 XP_016856514
VERSION     NP_001336582.1
DBSOURCE    REFSEQ: accession NM_001349653.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 885)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 885)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 885)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 885)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 885)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 885)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 885)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 885)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            On Mar 22, 2017 this sequence version replaced XP_016856514.1.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (14), as well as variants 6 and
            9-13, encodes isoform e.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.2576.1,
                                           SRR1803613.53667.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..885
                     /product="ribosomal protein S6 kinase delta-1 isoform e"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=97742
     Region          57..131
                     /region_name="MIT_SNX15"
                     /note="MIT: domain contained within Microtubule
                     Interacting and Trafficking molecules. This MIT domain
                     sub-family is found in sorting nexin 15 and related
                     proteins. The molecular function of the MIT domain is
                     unclear; cd02677"
                     /db_xref="CDD:239140"
     Region          154..>240
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <698..875
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(748,750,752,769,780..785,812,818,821)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            765..785
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..885
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349653.2:786..3443"
                     /note="isoform e is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS73028.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 masnqnspir tfglnlssds salgavasds eqskteeere srslfpgslk pklgkrdyle
       61 kageliklal kkeeeddyea asdfyrkgvd lllegvqges sptrreavkr rtaeylmrae
      121 sisslygkpq lddvsqppgs lssrplwnlr spaeelkafr vlgvidkvll vmdtrteqtf
      181 ilkglrksse ysrnrktiip rcvpnmvclh kyiiseesvf lvlqhaeggk lwsyiskfln
      241 rspeesfdik evkkptlakv hlqqptsspq dsssfesrgs dggsmlkalp lkssltpssq
      301 ddsnqeddgq dsspkwpdsg ssseeectts yltlcneygq ekiepgslne epfmktegng
      361 vdtkaiksfp ahlaadsdsp stqlrahelk ffpnddpeav ssprtsdsls rsknspmeff
      421 ridskdsase llgldfgekl yslkseplkp fftlpdgdsa srsfntsesk vefkaqdtis
      481 rgsddsvpvi sfkdaafddv sgtdegrpdl lvnlpgeles treaaamgpt kftqtnigii
      541 enklleapdv lclrlsteqc qaheekgiee lsdpsgpksy sitekhyaqe dprmlfvaav
      601 dhsssgdmsl lpssdpkfqg lgvvesavta nnteeslfri csplsganey iastdtlkte
      661 evllftdqtd dlakeeptsl fqrdsetkge sglvlegdke ihqifedldk klalasrfyi
      721 pegciqrwaa emvvaldalh regivcrdln pnnillndrg hiqltyfsrw sevedscdsd
      781 aiermycape vgaiteetea cdwwslgavl felltgktlv echpaginth ttlnmpecvs
      841 eearsliqql lqfnplerlg agvagvedik shpfftpvdw aelmr
//
LOCUS       NP_001336592             601 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform d [Homo sapiens].
ACCESSION   NP_001336592
VERSION     NP_001336592.1
DBSOURCE    REFSEQ: accession NM_001349663.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 601)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 601)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 601)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 601)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 601)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (22), as well as variants 5 and
            23-30, encodes isoform d.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: AL356893.1, AF037447.1 [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..601
                     /product="ribosomal protein S6 kinase delta-1 isoform d"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=66008
     Region          <414..591
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(464,466,468,485,496..501,528,534,537)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            481..501
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..601
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349663.2:829..2634"
                     /note="isoform d is encoded by transcript variant 22"
                     /db_xref="CCDS:CCDS73030.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mlkalplkss ltpssqddsn qeddgqdssp kwpdsgssse eecttsyltl cneygqekie
       61 pgslneepfm ktegngvdtk aiksfpahla adsdspstql rahelkffpn ddpeavsspr
      121 tsdslsrskn spmeffrids kdsasellgl dfgeklyslk seplkpfftl pdgdsasrsf
      181 ntseskvefk aqdtisrgsd dsvpvisfkd aafddvsgtd egrpdllvnl pgelestrea
      241 aamgptkftq tnigiienkl leapdvlclr lsteqcqahe ekgieelsdp sgpksysite
      301 khyaqedprm lfvaavdhss sgdmsllpss dpkfqglgvv esavtannte eslfricspl
      361 sganeyiast dtlkteevll ftdqtddlak eeptslfqrd setkgesglv legdkeihqi
      421 fedldkklal asrfyipegc iqrwaaemvv aldalhregi vcrdlnpnni llndrghiql
      481 tyfsrwseve dscdsdaier mycapevgai teeteacdww slgavlfell tgktlvechp
      541 aginthttln mpecvseear sliqqllqfn plerlgagva gvedikshpf ftpvdwaelm
      601 r
//
LOCUS       NP_001336594             601 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform d [Homo sapiens].
ACCESSION   NP_001336594
VERSION     NP_001336594.1
DBSOURCE    REFSEQ: accession NM_001349665.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 601)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 601)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 601)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 601)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 601)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (24), as well as variants 5, 23,
            and 25-30, encodes isoform d.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.3413.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..601
                     /product="ribosomal protein S6 kinase delta-1 isoform d"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=66008
     Region          <414..591
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(464,466,468,485,496..501,528,534,537)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            481..501
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..601
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349665.2:980..2785"
                     /note="isoform d is encoded by transcript variant 24"
                     /db_xref="CCDS:CCDS73030.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mlkalplkss ltpssqddsn qeddgqdssp kwpdsgssse eecttsyltl cneygqekie
       61 pgslneepfm ktegngvdtk aiksfpahla adsdspstql rahelkffpn ddpeavsspr
      121 tsdslsrskn spmeffrids kdsasellgl dfgeklyslk seplkpfftl pdgdsasrsf
      181 ntseskvefk aqdtisrgsd dsvpvisfkd aafddvsgtd egrpdllvnl pgelestrea
      241 aamgptkftq tnigiienkl leapdvlclr lsteqcqahe ekgieelsdp sgpksysite
      301 khyaqedprm lfvaavdhss sgdmsllpss dpkfqglgvv esavtannte eslfricspl
      361 sganeyiast dtlkteevll ftdqtddlak eeptslfqrd setkgesglv legdkeihqi
      421 fedldkklal asrfyipegc iqrwaaemvv aldalhregi vcrdlnpnni llndrghiql
      481 tyfsrwseve dscdsdaier mycapevgai teeteacdww slgavlfell tgktlvechp
      541 aginthttln mpecvseear sliqqllqfn plerlgagva gvedikshpf ftpvdwaelm
      601 r
//
LOCUS       NP_001336597             601 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform d [Homo sapiens].
ACCESSION   NP_001336597 XP_016856521
VERSION     NP_001336597.1
DBSOURCE    REFSEQ: accession NM_001349668.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 601)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 601)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 601)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 601)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 601)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            On Mar 22, 2017 this sequence version replaced XP_016856521.1.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (27), as well as variants 5,
            23-26, and 28-30, encodes isoform d.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.126617.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..601
                     /product="ribosomal protein S6 kinase delta-1 isoform d"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=66008
     Region          <414..591
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(464,466,468,485,496..501,528,534,537)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            481..501
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..601
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349668.2:1457..3262"
                     /note="isoform d is encoded by transcript variant 27"
                     /db_xref="CCDS:CCDS73030.1"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mlkalplkss ltpssqddsn qeddgqdssp kwpdsgssse eecttsyltl cneygqekie
       61 pgslneepfm ktegngvdtk aiksfpahla adsdspstql rahelkffpn ddpeavsspr
      121 tsdslsrskn spmeffrids kdsasellgl dfgeklyslk seplkpfftl pdgdsasrsf
      181 ntseskvefk aqdtisrgsd dsvpvisfkd aafddvsgtd egrpdllvnl pgelestrea
      241 aamgptkftq tnigiienkl leapdvlclr lsteqcqahe ekgieelsdp sgpksysite
      301 khyaqedprm lfvaavdhss sgdmsllpss dpkfqglgvv esavtannte eslfricspl
      361 sganeyiast dtlkteevll ftdqtddlak eeptslfqrd setkgesglv legdkeihqi
      421 fedldkklal asrfyipegc iqrwaaemvv aldalhregi vcrdlnpnni llndrghiql
      481 tyfsrwseve dscdsdaier mycapevgai teeteacdww slgavlfell tgktlvechp
      541 aginthttln mpecvseear sliqqllqfn plerlgagva gvedikshpf ftpvdwaelm
      601 r
//
LOCUS       NP_001336591             714 aa            linear   PRI 12-JAN-2026
DEFINITION  ribosomal protein S6 kinase delta-1 isoform i [Homo sapiens].
ACCESSION   NP_001336591
VERSION     NP_001336591.1
DBSOURCE    REFSEQ: accession NM_001349662.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 714)
  AUTHORS   So,J., Pasculescu,A., Dai,A.Y., Williton,K., James,A., Nguyen,V.,
            Creixell,P., Schoof,E.M., Sinclair,J., Barrios-Rodiles,M., Gu,J.,
            Krizus,A., Williams,R., Olhovsky,M., Dennis,J.W., Wrana,J.L.,
            Linding,R., Jorgensen,C., Pawson,T. and Colwill,K.
  TITLE     Integrative analysis of kinase networks in TRAIL-induced apoptosis
            provides a source of potential targets for combination therapy
  JOURNAL   Sci Signal 8 (371), rs3 (2015)
   PUBMED   25852190
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 714)
  AUTHORS   Leparc,G.G. and Mitra,R.D.
  TITLE     Non-EST-based prediction of novel alternatively spliced cassette
            exons with cell signaling function in Caenorhabditis elegans and
            human
  JOURNAL   Nucleic Acids Res 35 (10), 3192-3202 (2007)
   PUBMED   17452356
REFERENCE   5  (residues 1 to 714)
  AUTHORS   Liu,L., Yang,C., Yuan,J., Chen,X., Xu,J., Wei,Y., Yang,J., Lin,G.
            and Yu,L.
  TITLE     RPK118, a PX domain-containing protein, interacts with
            peroxiredoxin-3 through pseudo-kinase domains
  JOURNAL   Mol Cells 19 (1), 39-45 (2005)
   PUBMED   15750338
  REMARK    GeneRIF: findings indicate that RPK118 is a PRDX3-binding protein
            that may be involved in transporting PRDX3 from the cytoplasm to
            its mitochondrial site of function or to other membrane structures
            via endosome trafficking.
REFERENCE   6  (residues 1 to 714)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    GeneRIF: Identified as a pseudokinase and named RSKL1
            Review article
REFERENCE   7  (residues 1 to 714)
  AUTHORS   Hayashi,S., Okada,T., Igarashi,N., Fujita,T., Jahangeer,S. and
            Nakamura,S.
  TITLE     Identification and characterization of RPK118, a novel sphingosine
            kinase-1-binding protein
  JOURNAL   J Biol Chem 277 (36), 33319-33324 (2002)
   PUBMED   12077123
  REMARK    GeneRIF: cloning and characterization of RPK118 as a sphingosine
            kinase-1-binding protein
REFERENCE   8  (residues 1 to 714)
  AUTHORS   Zhang,H., Yu,L., Mao,N., Fu,Q., Tu,Q., Gao,J. and Zhao,S.
  TITLE     Cloning, characterization, and chromosome mapping of RPS6KC1, a
            novel putative member of the ribosome protein S6 kinase family, to
            chromosome 12q12-q13.1
  JOURNAL   Genomics 61 (3), 314-318 (1999)
   PUBMED   10552933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645860.5, AL512449.6 and
            AL583826.16.
            
            Summary: Sphingosine kinase catalyzes the formation of sphingosine
            1 phosphate, a lipid cellular messenger. The protein encoded by
            this gene can bind to sphingosine kinase and to
            phosphatidylinositol 3-phosphate, suggesting a role in sphingosine
            1 phophate signaling. The encoded protein can also bind to
            peroxiredoxin-3 and may help transport it to mitochondria.
            [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (21), as well as variants 18-20,
            encodes isoform i.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.195687.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..714
                     /product="ribosomal protein S6 kinase delta-1 isoform i"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein S6 kinase delta-1; SPHK1-binding
                     protein; 52 kDa ribosomal protein S6 kinase; ribosomal S6
                     kinase-like protein with two PSK domains 118 kDa protein;
                     ribosomal protein S6 kinase, 52kDa, polypeptide 1"
                     /calculated_mol_wt=78840
     Region          1..>69
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          <527..704
                     /region_name="STKc_RPK118_like"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     RPK118, and similar proteins; cd05576"
                     /db_xref="CDD:270728"
     Site            order(577,579,581,598,609..614,641,647,650)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270728"
     Site            594..614
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270728"
     CDS             1..714
                     /gene="RPS6KC1"
                     /gene_synonym="humS6PKh1; NEDSCW; RPK118; RSKL1;
                     S6K-delta-1; S6PKh1"
                     /coded_by="NM_001349662.2:1372..3516"
                     /note="isoform i is encoded by transcript variant 21"
                     /db_xref="GeneID:26750"
                     /db_xref="HGNC:HGNC:10439"
                     /db_xref="MIM:617517"
ORIGIN      
        1 mdtrteqtfi lkglrkssey srnrktiipr cvpnmvclhk yiiseesvfl vlqhaeggkl
       61 wsyiskflnr speesfdike vkkptlakvh lqqptsspqd sssfesrgsd ggsmlkalpl
      121 kssltpssqd dsnqeddgqd sspkwpdsgs sseeecttsy ltlcneygqe kiepgslnee
      181 pfmktegngv dtkaiksfpa hlaadsdsps tqlrahelkf fpnddpeavs sprtsdslsr
      241 sknspmeffr idskdsasel lgldfgekly slkseplkpf ftlpdgdsas rsfntseskv
      301 efkaqdtisr gsddsvpvis fkdaafddvs gtdegrpdll vnlpgelest reaaamgptk
      361 ftqtnigiie nklleapdvl clrlsteqcq aheekgieel sdpsgpksys itekhyaqed
      421 prmlfvaavd hsssgdmsll pssdpkfqgl gvvesavtan nteeslfric splsganeyi
      481 astdtlktee vllftdqtdd lakeeptslf qrdsetkges glvlegdkei hqifedldkk
      541 lalasrfyip egciqrwaae mvvaldalhr egivcrdlnp nnillndrgh iqltyfsrws
      601 evedscdsda iermycapev gaiteeteac dwwslgavlf elltgktlve chpagintht
      661 tlnmpecvse earsliqqll qfnplerlga gvagvediks hpfftpvdwa elmr
//
LOCUS       NP_001432043             395 aa            linear   PRI 12-JAN-2026
DEFINITION  ING4-ACRBP readthrough [Homo sapiens].
ACCESSION   NP_001432043
VERSION     NP_001432043.1
DBSOURCE    REFSEQ: accession NM_001445114.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125494.2 and AC135892.1.
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..395
                     /product="ING4-ACRBP readthrough"
                     /calculated_mol_wt=44942
     Region          <1..63
                     /region_name="PBP_sp32"
                     /note="Proacrosin binding protein sp32; pfam07222"
                     /db_xref="CDD:429354"
     CDS             1..395
                     /gene="ING4-ACRBP"
                     /coded_by="NM_001445114.1:1306..2493"
                     /db_xref="GeneID:144699907"
ORIGIN      
        1 mtspisphft vterqtfqpw perlsnnvee llqsslslgg qeqapehkqe qgvehrqept
       61 qehkqeegqk qeeqeeeqee egkqeegqgt kegreavsql qtdsepkfhs eslssnpssf
      121 aprvrevest pmimeniqel irsaqeidem neiydensyw rnqnpgsllq lphteallvl
      181 cysiventci itptakawky meeeilgfgk svcdslgrrh mstcalcdfc slkleqchse
      241 aslqrqqcdt shktpfvspl lasqslsign qvgspesgrf ygldlygglh mdfwcarlat
      301 kgcedvrvsg wlqteflsfq dgdfptkicd tdyiqypnyc sfksqqclmr nrnrkvsrmr
      361 clqnetysal spgksedvvl rwsqefstlt lgqfg
//
LOCUS       NP_004156                308 aa            linear   PRI 12-JAN-2026
DEFINITION  GTP-binding protein RAD [Homo sapiens].
ACCESSION   NP_004156
VERSION     NP_004156.1
DBSOURCE    REFSEQ: accession NM_004165.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Sun,Z., Li,Y., Tan,X., Liu,W., He,X., Pan,D., Li,E., Xu,L. and
            Long,L.
  TITLE     Friend or Foe: Regulation, Downstream Effectors of RRAD in Cancer
  JOURNAL   Biomolecules 13 (3), 477 (2023)
   PUBMED   36979412
  REMARK    GeneRIF: Friend or Foe: Regulation, Downstream Effectors of RRAD in
            Cancer.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Katz,M., Subramaniam,S., Chomsky-Hecht,O., Tsemakhovich,V.,
            Flockerzi,V., Klussmann,E., Hirsch,J.A., Weiss,S. and Dascal,N.
  TITLE     Reconstitution of beta-adrenergic regulation of CaV1.2:
            Rad-dependent and Rad-independent protein kinase A mechanisms
  JOURNAL   Proc Natl Acad Sci U S A 118 (21) (2021)
   PUBMED   34001616
  REMARK    GeneRIF: Reconstitution of beta-adrenergic regulation of CaV1.2:
            Rad-dependent and Rad-independent protein kinase A mechanisms.
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Kim,H.K., Lee,I., Kim,S.T., Lee,J., Kim,K.M., Park,J.O. and
            Kang,W.K.
  TITLE     RRAD expression in gastric and colorectal cancer with peritoneal
            carcinomatosis
  JOURNAL   Sci Rep 9 (1), 19439 (2019)
   PUBMED   31857616
  REMARK    GeneRIF: RRAD expression in gastric and colorectal cancer with
            peritoneal carcinomatosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Belbachir,N., Portero,V., Al Sayed,Z.R., Gourraud,J.B.,
            Dilasser,F., Jesel,L., Guo,H., Wu,H., Gaborit,N., Guilluy,C.,
            Girardeau,A., Bonnaud,S., Simonet,F., Karakachoff,M., Pattier,S.,
            Scott,C., Burel,S., Marionneau,C., Chariau,C., Gaignerie,A.,
            David,L., Genin,E., Deleuze,J.F., Dina,C., Sauzeau,V., Loirand,G.,
            Baro,I., Schott,J.J., Probst,V., Wu,J.C., Redon,R., Charpentier,F.
            and Le Scouarnec,S.
  TITLE     RRAD mutation causes electrical and cytoskeletal defects in
            cardiomyocytes derived from a familial case of Brugada syndrome
  JOURNAL   Eur Heart J 40 (37), 3081-3094 (2019)
   PUBMED   31114854
  REMARK    GeneRIF: RRAD mutation causes electrical and cytoskeletal defects
            in cardiomyocytes derived from a familial case of Brugada syndrome.
REFERENCE   5  (residues 1 to 308)
  AUTHORS   Wei,Z., Guo,H., Qin,J., Lu,S., Liu,Q., Zhang,X., Zou,Y., Gong,Y.
            and Shao,C.
  TITLE     Pan-senescence transcriptome analysis identified RRAD as a marker
            and negative regulator of cellular senescence
  JOURNAL   Free Radic Biol Med 130, 267-277 (2019)
   PUBMED   30391675
  REMARK    GeneRIF: this study established RRAD to be a biomarker as well as a
            novel negative regulator of cellular senescence.
REFERENCE   6  (residues 1 to 308)
  AUTHORS   Caldwell,J.S., Moyers,J.S., Doria,A., Reynet,C. and Kahn,R.C.
  TITLE     Molecular cloning of the human rad gene: gene structure and
            complete nucleotide sequence
  JOURNAL   Biochim Biophys Acta 1316 (3), 145-148 (1996)
   PUBMED   8781531
REFERENCE   7  (residues 1 to 308)
  AUTHORS   Zhu,J., Bilan,P.J., Moyers,J.S., Antonetti,D.A. and Kahn,C.R.
  TITLE     Rad, a novel Ras-related GTPase, interacts with skeletal muscle
            beta-tropomyosin
  JOURNAL   J Biol Chem 271 (2), 768-773 (1996)
   PUBMED   8557685
REFERENCE   8  (residues 1 to 308)
  AUTHORS   Zhu,J., Reynet,C., Caldwell,J.S. and Kahn,C.R.
  TITLE     Characterization of Rad, a new member of Ras/GTPase superfamily,
            and its regulation by a unique GTPase-activating protein (GAP)-like
            activity
  JOURNAL   J Biol Chem 270 (9), 4805-4812 (1995)
   PUBMED   7876254
REFERENCE   9  (residues 1 to 308)
  AUTHORS   Doria,A., Caldwell,J.S., Ji,L., Reynet,C., Rich,S.S.,
            Weremowicz,S., Morton,C.C., Warram,J.H., Kahn,C.R. and
            Krolewski,A.S.
  TITLE     Trinucleotide repeats at the rad locus. Allele distributions in
            NIDDM and mapping to a 3-cM region on chromosome 16q
  JOURNAL   Diabetes 44 (2), 243-247 (1995)
   PUBMED   7859947
REFERENCE   10 (residues 1 to 308)
  AUTHORS   Reynet,C. and Kahn,C.R.
  TITLE     Rad: a member of the Ras family overexpressed in muscle of type II
            diabetic humans
  JOURNAL   Science 262 (5138), 1441-1444 (1993)
   PUBMED   8248782
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP257026.1, L24564.1 and N93445.1.
            
            Transcript Variant: This variant (2) uses an alternate splice
            junction in the 5' UTR compared to variant 1. Variants 1 and 2 both
            encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC011645.2, ERR279839.8212.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000299759.11/ ENSP00000299759.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..308
                     /product="GTP-binding protein RAD"
                     /EC_number="3.6.5.2"
                     /note="RAS (RAD and GEM) like GTP binding 3; Ras-related
                     associated with diabetes; RRAD, Ras related glycolysis
                     inihibitor and calcium channel regulator; ras associated
                     with diabetes"
                     /calculated_mol_wt=33114
     Region          1..88
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55042.2)"
     Site            24
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88667; propagated from
                     UniProtKB/Swiss-Prot (P55042.2)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88667; propagated from
                     UniProtKB/Swiss-Prot (P55042.2)"
     Region          92..308
                     /region_name="RGK"
                     /note="Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras
                     GTPases; cd04148"
                     /db_xref="CDD:206715"
     Site            98..105
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206715"
     Site            order(99..100,146..147)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206715"
     Site            order(100..106,144,147,203..204,206,233..234)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206715"
     Site            order(105..106,118,120,127..128,141..142,144,146..147,235)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206715"
     Site            order(119..120,125..128)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206715"
     Site            order(119..124,125..127)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206715"
     Site            121
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206715"
     Site            144..147
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206715"
     Site            order(146..147,155..158,161..164)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206715"
     Site            203..206
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206715"
     Site            233..235
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206715"
     Region          278..297
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P55042.2)"
     Site            302..305
                     /site_type="other"
                     /note="putative lipid modification site [posttranslational
                     modification]"
                     /db_xref="CDD:206715"
     CDS             1..308
                     /gene="RRAD"
                     /gene_synonym="RAD; REM3"
                     /coded_by="NM_004165.3:143..1069"
                     /db_xref="CCDS:CCDS10824.1"
                     /db_xref="GeneID:6236"
                     /db_xref="HGNC:HGNC:10446"
                     /db_xref="MIM:179503"
ORIGIN      
        1 mtlngggsga ggsrgggqer errrgstpwg papplhrrsm pvderdlqaa ltpgaltaaa
       61 agtgtqgprl dwpedsedsl ssggsdsdes vykvlllgap gvgksalari fggvedgpea
      121 eaaghtydrs ivvdgeeasl mvydiweqdg grwlpghcma mgdayvivys vtdkgsfeka
      181 selrvqlrra rqtddvpiil vgnksdlvrs revsvdegra cavvfdckfi etsaalhhnv
      241 qalfegvvrq irlrrdskea narrqagtrr reslgkkakr flgrivarns rkmafraksk
      301 schdlsvl
//
LOCUS       NP_000935                521 aa            linear   PRI 12-JAN-2026
DEFINITION  protein phosphatase 3 catalytic subunit alpha isoform 1 [Homo
            sapiens].
ACCESSION   NP_000935
VERSION     NP_000935.1
DBSOURCE    REFSEQ: accession NM_000944.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Masaki,T., Habara,M., Shibutani,S., Hanaki,S., Sato,Y., Tomiyasu,H.
            and Shimada,M.
  TITLE     Dephosphorylation of the EGFR protein by calcineurin at serine
            1046/1047 enhances its stability
  JOURNAL   Biochem Biophys Res Commun 641, 84-92 (2023)
   PUBMED   36525928
  REMARK    GeneRIF: Dephosphorylation of the EGFR protein by calcineurin at
            serine 1046/1047 enhances its stability.
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Wang,Z., Li,H., Wang,H., Li,X., Zhang,Q., Wang,H., Li,K. and Qiu,Y.
  TITLE     TRIM72 exerts antitumor effects in breast cancer and modulates
            lactate production and MCT4 promoter activity by interacting with
            PPP3CA
  JOURNAL   Anticancer Drugs 33 (5), 489-501 (2022)
   PUBMED   35324524
  REMARK    GeneRIF: TRIM72 exerts antitumor effects in breast cancer and
            modulates lactate production and MCT4 promoter activity by
            interacting with PPP3CA.
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Etges,A., Hellmig,N., Walenda,G., Haddad,B.G., Machtens,J.P.,
            Morosan,T., Rump,L.C. and Scholl,U.I.
  TITLE     A Novel Homozygous KLHL3 Mutation as a Cause of Autosomal Recessive
            Pseudohypoaldosteronism Type II Diagnosed Late in Life
  JOURNAL   Nephron 146 (4), 418-428 (2022)
   PUBMED   35093948
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Vymazal,O., Bendickova,K., De Zuani,M., Vlkova,M.,
            Hortova-Kohoutkova,M. and Fric,J.
  TITLE     Immunosuppression Affects Neutrophil Functions: Does
            Calcineurin-NFAT Signaling Matter?
  JOURNAL   Front Immunol 12, 770515 (2021)
   PUBMED   34795676
  REMARK    GeneRIF: Immunosuppression Affects Neutrophil Functions: Does
            Calcineurin-NFAT Signaling Matter?
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Giri,P.R., Higuchi,S. and Kincaid,R.L.
  TITLE     Chromosomal mapping of the human genes for the calmodulin-dependent
            protein phosphatase (calcineurin) catalytic subunit
  JOURNAL   Biochem Biophys Res Commun 181 (1), 252-258 (1991)
   PUBMED   1659808
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Kincaid,R.L., Giri,P.R., Higuchi,S., Tamura,J., Dixon,S.C.,
            Marietta,C.A., Amorese,D.A. and Martin,B.M.
  TITLE     Cloning and characterization of molecular isoforms of the catalytic
            subunit of calcineurin using nonisotopic methods
  JOURNAL   J Biol Chem 265 (19), 11312-11319 (1990)
   PUBMED   2162844
REFERENCE   8  (residues 1 to 521)
  AUTHORS   Guerini,D. and Klee,C.B.
  TITLE     Cloning of human calcineurin A: evidence for two isozymes and
            identification of a polyproline structural domain
  JOURNAL   Proc Natl Acad Sci U S A 86 (23), 9183-9187 (1989)
   PUBMED   2556704
REFERENCE   9  (residues 1 to 521)
  AUTHORS   Kincaid,R.L., Nightingale,M.S. and Martin,B.M.
  TITLE     Characterization of a cDNA clone encoding the calmodulin-binding
            domain of mouse brain calcineurin
  JOURNAL   Proc Natl Acad Sci U S A 85 (23), 8983-8987 (1988)
   PUBMED   2848250
REFERENCE   10 (residues 1 to 521)
  AUTHORS   King,M.M., Huang,C.Y., Chock,P.B., Nairn,A.C., Hemmings,H.C. Jr.,
            Chan,K.F. and Greengard,P.
  TITLE     Mammalian brain phosphoproteins as substrates for calcineurin
  JOURNAL   J Biol Chem 259 (13), 8080-8083 (1984)
   PUBMED   6330098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001816.2, EU192652.1, AL353950.1, AW973358.1 and AP001870.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL353950.1, L14778.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394854.8/ ENSP00000378323.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..521
                     /product="protein phosphatase 3 catalytic subunit alpha
                     isoform 1"
                     /EC_number="3.1.3.16"
                     /note="calcineurin A alpha; CAM-PRP catalytic subunit;
                     protein phosphatase 3 catalytic subunit alpha isozyme; CNA
                     alpha"
                     /calculated_mol_wt=58557
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q08209.1)"
     Region          41..345
                     /region_name="MPP_PP2B"
                     /note="PP2B, metallophosphatase domain; cd07416"
                     /db_xref="CDD:277361"
     Site            order(53,55,90,92,118,150,159,199,281,314,341)
                     /site_type="other"
                     /note="CN-CyPA-CsA complex [polypeptide binding]"
                     /db_xref="CDD:277361"
     Region          56..340
                     /region_name="Catalytic. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08209.1)"
     Site            order(90,92,118,122,150..151,199,232,254,281,283)
                     /site_type="active"
                     /db_xref="CDD:277361"
     Site            order(90,92,118,150,199,281)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277361"
     Region          307..311
                     /region_name="SAPNY motif.
                     /evidence=ECO:0000305|PubMed:26248042"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08209.1)"
     Region          327..336
                     /region_name="Interaction with PxIxIF motif in substrate.
                     /evidence=ECO:0000269|PubMed:17498738,
                     ECO:0000269|PubMed:17502104, ECO:0000269|PubMed:22343722,
                     ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26248042"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08209.1)"
     Region          341..369
                     /region_name="Calcineurin B binding.
                     /evidence=ECO:0000269|PubMed:12218175,
                     ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738,
                     ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:27974827,
                     ECO:0000269|PubMed:8524402"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08209.1)"
     Site            352
                     /site_type="other"
                     /note="Interaction with PxVP motif in substrate.
                     /evidence=ECO:0000269|PubMed:23468591,
                     ECO:0000269|PubMed:27974827; propagated from
                     UniProtKB/Swiss-Prot (Q08209.1)"
     Region          392..406
                     /region_name="Calmodulin-binding.
                     /evidence=ECO:0000269|PubMed:18384083,
                     ECO:0000269|PubMed:19404396, ECO:0000269|PubMed:25144868,
                     ECO:0000269|Ref.34"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08209.1)"
     Region          407..414
                     /region_name="Autoinhibitory segment.
                     /evidence=ECO:0000250|UniProtKB:P16298"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08209.1)"
     Region          465..487
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000269|PubMed:8524402"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08209.1)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63329; propagated from
                     UniProtKB/Swiss-Prot (Q08209.1)"
     Region          475..521
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08209.1)"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08209.1)"
     CDS             1..521
                     /gene="PPP3CA"
                     /gene_synonym="ACCIID; CALN; CALNA; CALNA1; CNA1; DEE91;
                     IECEE; IECEE1; PPP2B"
                     /coded_by="NM_000944.5:731..2296"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34037.1"
                     /db_xref="GeneID:5530"
                     /db_xref="HGNC:HGNC:9314"
                     /db_xref="MIM:114105"
ORIGIN      
        1 msepkaidpk lsttdrvvka vpfppshrlt akevfdndgk prvdilkahl mkegrleesv
       61 alriitegas ilrqeknlld idapvtvcgd ihgqffdlmk lfevggspan trylflgdyv
      121 drgyfsiecv lylwalkily pktlfllrgn hecrhlteyf tfkqeckiky servydacmd
      181 afdclplaal mnqqflcvhg glspeintld dirkldrfke ppaygpmcdi lwsdpledfg
      241 nektqehfth ntvrgcsyfy sypavceflq hnnllsilra heaqdagyrm yrksqttgfp
      301 slitifsapn yldvynnkaa vlkyennvmn irqfncsphp ywlpnfmdvf twslpfvgek
      361 vtemlvnvln icsddelgse edgfdgataa arkevirnki raigkmarvf svlreesesv
      421 ltlkgltptg mlpsgvlsgg kqtlqsatve aieadeaikg fspqhkitsf eeakgldrin
      481 ermpprrdam psdanlnsin kaltsetngt dsngsnssni q
//
LOCUS       NP_001123538            1292 aa            linear   PRI 12-JAN-2026
DEFINITION  ras/Rap GTPase-activating protein SynGAP isoform 2 [Homo sapiens].
ACCESSION   NP_001123538
VERSION     NP_001123538.1
DBSOURCE    REFSEQ: accession NM_001130066.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1292)
  AUTHORS   Bednarczuk,N., Housby,H., Lee,I.O., Consortium,I., Skuse,D. and
            Wolstencroft,J.
  TITLE     Behavioural and neurodevelopmental characteristics of SYNGAP1
  JOURNAL   J Neurodev Disord 16 (1), 46 (2024)
   PUBMED   39148034
  REMARK    GeneRIF: Behavioural and neurodevelopmental characteristics of
            SYNGAP1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1292)
  AUTHORS   Kim,H.J., Kim,M., Jang,S., Cho,J.S., Kim,S.Y., Cho,A., Kim,H.,
            Lim,B.C., Chae,J.H., Choi,J., Kim,K.J. and Kim,W.
  TITLE     SYNGAP1-related developmental and epileptic encephalopathy:
            Genotypic and phenotypic characteristics and longitudinal insights
  JOURNAL   Am J Med Genet A 194 (8), e63606 (2024)
   PUBMED   38563110
  REMARK    GeneRIF: SYNGAP1-related developmental and epileptic
            encephalopathy: Genotypic and phenotypic characteristics and
            longitudinal insights.
REFERENCE   3  (residues 1 to 1292)
  AUTHORS   Wright,D., Kenny,A., Eley,S., McKechanie,A.G. and Stanfield,A.C.
  TITLE     Visual social attention in SYNGAP1-related intellectual disability
  JOURNAL   Autism Res 17 (6), 1083-1093 (2024)
   PUBMED   38698724
  REMARK    GeneRIF: Visual social attention in SYNGAP1-related intellectual
            disability.
REFERENCE   4  (residues 1 to 1292)
  AUTHORS   Wright,D., Kenny,A., Mizen,L.A.M., McKechanie,A.G. and
            Stanfield,A.C.
  TITLE     The Behavioral Profile of SYNGAP1-Related Intellectual Disability
  JOURNAL   Am J Intellect Dev Disabil 129 (3), 199-214 (2024)
   PUBMED   38657965
  REMARK    GeneRIF: The Behavioral Profile of SYNGAP1-Related Intellectual
            Disability.
REFERENCE   5  (residues 1 to 1292)
  AUTHORS   Carvill,G.L., Heavin,S.B., Yendle,S.C., McMahon,J.M., O'Roak,B.J.,
            Cook,J., Khan,A., Dorschner,M.O., Weaver,M., Calvert,S., Malone,S.,
            Wallace,G., Stanley,T., Bye,A.M., Bleasel,A., Howell,K.B.,
            Kivity,S., Mackay,M.T., Rodriguez-Casero,V., Webster,R.,
            Korczyn,A., Afawi,Z., Zelnick,N., Lerman-Sagie,T., Lev,D.,
            Moller,R.S., Gill,D., Andrade,D.M., Freeman,J.L., Sadleir,L.G.,
            Shendure,J., Berkovic,S.F., Scheffer,I.E. and Mefford,H.C.
  TITLE     Targeted resequencing in epileptic encephalopathies identifies de
            novo mutations in CHD2 and SYNGAP1
  JOURNAL   Nat Genet 45 (7), 825-830 (2013)
   PUBMED   23708187
  REMARK    GeneRIF: De novo CHD2 and SYNGAP1 mutations are new causes of
            epileptic encephalopathies, accounting for 1.2% and 1% of cases,
            respectively.
REFERENCE   6  (residues 1 to 1292)
  AUTHORS   Berryer,M.H., Hamdan,F.F., Klitten,L.L., Moller,R.S., Carmant,L.,
            Schwartzentruber,J., Patry,L., Dobrzeniecka,S., Rochefort,D.,
            Neugnot-Cerioli,M., Lacaille,J.C., Niu,Z., Eng,C.M., Yang,Y.,
            Palardy,S., Belhumeur,C., Rouleau,G.A., Tommerup,N., Immken,L.,
            Beauchamp,M.H., Patel,G.S., Majewski,J., Tarnopolsky,M.A.,
            Scheffzek,K., Hjalgrim,H., Michaud,J.L. and Di Cristo,G.
  TITLE     Mutations in SYNGAP1 cause intellectual disability, autism, and a
            specific form of epilepsy by inducing haploinsufficiency
  JOURNAL   Hum Mutat 34 (2), 385-394 (2013)
   PUBMED   23161826
  REMARK    GeneRIF: De novo missense mutations, p.R579X, and possibly all the
            other truncating mutations in SYNGAP1 result in a loss of its
            function, causing intellectual disability, autism, and a specific
            form of epilepsy.
REFERENCE   7  (residues 1 to 1292)
  AUTHORS   Kim,J.H., Liao,D., Lau,L.F. and Huganir,R.L.
  TITLE     SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90
            protein family
  JOURNAL   Neuron 20 (4), 683-691 (1998)
   PUBMED   9581761
REFERENCE   8  (residues 1 to 1292)
  AUTHORS   Kroll,J. and Waltenberger,J.
  TITLE     The vascular endothelial growth factor receptor KDR activates
            multiple signal transduction pathways in porcine aortic endothelial
            cells
  JOURNAL   J Biol Chem 272 (51), 32521-32527 (1997)
   PUBMED   9405464
REFERENCE   9  (residues 1 to 1292)
  AUTHORS   Holder,J.L. Jr., Hamdan,F.F. and Michaud,J.L.
  TITLE     SYNGAP1-Related Intellectual Disability
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30789692
REFERENCE   10 (residues 1 to 1292)
  AUTHORS   Fantl,W.J., Escobedo,J.A., Martin,G.A., Turck,C.W., del Rosario,M.,
            McCormick,F. and Williams,L.T.
  TITLE     Distinct phosphotyrosines on a growth factor receptor bind to
            specific molecules that mediate different signaling pathways
  JOURNAL   Cell 69 (3), 413-423 (1992)
   PUBMED   1374684
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL662799.16, DA057307.1,
            AK307888.1, AK094225.1, AL713634.1 and AK124666.1.
            
            Summary: This gene encodes a Ras GTPase activating protein that is
            a member of the N-methyl-D-aspartate receptor complex. The
            N-terminal domain of the protein contains a Ras-GAP domain, a
            pleckstrin homology domain, and a C2 domain that may be involved in
            binding of calcium and phospholipids. The C-terminal domain
            consists of a ten histidine repeat region, serine and tyrosine
            phosphorylation sites, and a T/SXV motif required for postsynaptic
            scaffold protein interaction. The encoded protein negatively
            regulates Ras, Rap and
            alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor
            trafficking to the postsynaptic membrane to regulate synaptic
            plasticity and neuronal homeostasis. Allelic variants of this gene
            are associated with intellectual disability and autism spectrum
            disorder. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Nov 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK307888.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.32"
     Protein         1..1292
                     /product="ras/Rap GTPase-activating protein SynGAP isoform
                     2"
                     /note="synaptic Ras GTPase activating protein, 135kDa; Ras
                     GTPase-activating protein SynGAP; neuronal RasGAP;
                     synaptic Ras GTPase activating protein 1 homolog; ras/Rap
                     GTPase-activating protein SynGAP; Ras/Rap
                     GTPase-activating protein 1"
                     /calculated_mol_wt=142734
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          92..129
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          122..313
                     /region_name="PH_SynGAP"
                     /note="Synaptic Ras-GTPase activating protein Pleckstrin
                     homology (PH) domain; cd13375"
                     /db_xref="CDD:270178"
     Region          252..414
                     /region_name="C2_SynGAP_like"
                     /note="C2 domain present in Ras GTPase activating protein
                     (GAP) family; cd04013"
                     /db_xref="CDD:175980"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          373..394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          405..728
                     /region_name="RasGAP_DAB2IP"
                     /note="Ras-GTPase Activating Domain of DAB2IP and similar
                     proteins; cd05136"
                     /db_xref="CDD:213338"
     Site            order(444,481,483,485..486,488,491,495,587,595..596,
                     599..600,603,624,627..628,631,635,637,642..643)
                     /site_type="other"
                     /note="putative RAS interface [polypeptide binding]"
                     /db_xref="CDD:213338"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            485
                     /site_type="other"
                     /note="Arginine finger, crucial for GTP hydrolysis by
                     stabilizing the transition state.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00167; propagated
                     from UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          718..1279
                     /region_name="DUF3498"
                     /note="Domain of unknown function (DUF3498); pfam12004"
                     /db_xref="CDD:463427"
     Region          725..753
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            752
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          767..791
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          771..801
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            809
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            811
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            814
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            822
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            826
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            828
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            862
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            878
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            881
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            884
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          919..1003
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            971
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          1019..1140
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            1104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            1107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            1151
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            1188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     CDS             1..1292
                     /gene="SYNGAP1"
                     /gene_synonym="MRD5; RASA5; SYNGAP"
                     /coded_by="NM_001130066.2:201..4079"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS93894.1"
                     /db_xref="GeneID:8831"
                     /db_xref="HGNC:HGNC:11497"
                     /db_xref="MIM:603384"
ORIGIN      
        1 msrsrasihr gsipamsyap frdvrgpsmh rtqyvhspyd rpgwnprfci isgnqllmld
       61 edeihpllir drrsessrnk llrrtvsvpv egrphgehey hlgrsrrksv pggkqysmeg
      121 apaapfrpsq gflsrrlkss ikrtksqpkl drtssfrqil prfrsadhdr arlmqsfkes
      181 hshesllsps saaealelnl dedsiikpvh ssilgqefcf evttssgtkc facrsaaerd
      241 kwienlqrav kpnkdnsrrv dnvlklwiie arelppkkry ycelclddml yarttskprs
      301 asgdtvfwge hfefnnlpav ralrlhlyrd sdkkrkkdka gyvglvtvpv atlagrhfte
      361 qwypvtlptg sggsggmgsg ggggsgggsg gkgkggcpav rlkaryqtms ilpmelykef
      421 aeyvtnhyrm lcavlepaln vkgkeevasa lvhilqstgk akdflsdmam sevdrfmere
      481 hlifrentla tkaieeymrl igqkylkdai gefiralyes eencevdpik ctasslaehq
      541 anlrmccela lckvvnshcv fprelkevfa swrlrcaerg rediadrlis aslflrflcp
      601 aimspslfgl mqeypdeqts rtltliakvi qnlanfskft skedflgfmn eflelewgsm
      661 qqflyeisnl dtltnsssfe gyidlgrels tlhallwevl pqlskeallk lgplprllnd
      721 istalrnpni qrqpsrqser prpqpvvlrg psaemqgymm rdlnssmdma rlpsptkekp
      781 pppppgggkd lfyvsrppla rsspayctss sditepeqkm lsvnksvsml dlqgdgpggr
      841 lnsssvsnla avgdllhssq asltaalglr papagrlsqg sgssitaagm rlsqmgvttd
      901 gvpaqqlrip lsfqnplfhm aadgpgppgg hggggghgpp sshhhhhhhh hhrggeppgd
      961 tfapfhgysk sedlssgvpk ppaasilhsh sysdefgpsg tdftrrqlsl qdnlqhmlsp
     1021 pqitigpqrp apsgpgggsg ggsggggggq ppplqrgksq qltvsaaqkp rpssgnllqs
     1081 pepsygparp rqqslskegs iggsggsggg gggglkpsit kqhsqtpstl nptmpasert
     1141 vawvsnmphl sadiesahie reeyklkeys ksmdesrldr eyeeeihslk erlhmsnrkl
     1201 eeyerrllsq eeqtskilmq yqarleqsek rlrqqqaekd sqiksiigrl mlveeelrrd
     1261 hpamaeplpe pkkrlldaqr gsfppwvqqt rv
//
LOCUS       NP_001124164             469 aa            linear   PRI 12-JAN-2026
DEFINITION  protein phosphatase 3 catalytic subunit alpha isoform 3 [Homo
            sapiens].
ACCESSION   NP_001124164
VERSION     NP_001124164.1
DBSOURCE    REFSEQ: accession NM_001130692.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Masaki,T., Habara,M., Shibutani,S., Hanaki,S., Sato,Y., Tomiyasu,H.
            and Shimada,M.
  TITLE     Dephosphorylation of the EGFR protein by calcineurin at serine
            1046/1047 enhances its stability
  JOURNAL   Biochem Biophys Res Commun 641, 84-92 (2023)
   PUBMED   36525928
  REMARK    GeneRIF: Dephosphorylation of the EGFR protein by calcineurin at
            serine 1046/1047 enhances its stability.
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Wang,Z., Li,H., Wang,H., Li,X., Zhang,Q., Wang,H., Li,K. and Qiu,Y.
  TITLE     TRIM72 exerts antitumor effects in breast cancer and modulates
            lactate production and MCT4 promoter activity by interacting with
            PPP3CA
  JOURNAL   Anticancer Drugs 33 (5), 489-501 (2022)
   PUBMED   35324524
  REMARK    GeneRIF: TRIM72 exerts antitumor effects in breast cancer and
            modulates lactate production and MCT4 promoter activity by
            interacting with PPP3CA.
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Etges,A., Hellmig,N., Walenda,G., Haddad,B.G., Machtens,J.P.,
            Morosan,T., Rump,L.C. and Scholl,U.I.
  TITLE     A Novel Homozygous KLHL3 Mutation as a Cause of Autosomal Recessive
            Pseudohypoaldosteronism Type II Diagnosed Late in Life
  JOURNAL   Nephron 146 (4), 418-428 (2022)
   PUBMED   35093948
REFERENCE   5  (residues 1 to 469)
  AUTHORS   Vymazal,O., Bendickova,K., De Zuani,M., Vlkova,M.,
            Hortova-Kohoutkova,M. and Fric,J.
  TITLE     Immunosuppression Affects Neutrophil Functions: Does
            Calcineurin-NFAT Signaling Matter?
  JOURNAL   Front Immunol 12, 770515 (2021)
   PUBMED   34795676
  REMARK    GeneRIF: Immunosuppression Affects Neutrophil Functions: Does
            Calcineurin-NFAT Signaling Matter?
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 469)
  AUTHORS   Giri,P.R., Higuchi,S. and Kincaid,R.L.
  TITLE     Chromosomal mapping of the human genes for the calmodulin-dependent
            protein phosphatase (calcineurin) catalytic subunit
  JOURNAL   Biochem Biophys Res Commun 181 (1), 252-258 (1991)
   PUBMED   1659808
REFERENCE   7  (residues 1 to 469)
  AUTHORS   Kincaid,R.L., Giri,P.R., Higuchi,S., Tamura,J., Dixon,S.C.,
            Marietta,C.A., Amorese,D.A. and Martin,B.M.
  TITLE     Cloning and characterization of molecular isoforms of the catalytic
            subunit of calcineurin using nonisotopic methods
  JOURNAL   J Biol Chem 265 (19), 11312-11319 (1990)
   PUBMED   2162844
REFERENCE   8  (residues 1 to 469)
  AUTHORS   Guerini,D. and Klee,C.B.
  TITLE     Cloning of human calcineurin A: evidence for two isozymes and
            identification of a polyproline structural domain
  JOURNAL   Proc Natl Acad Sci U S A 86 (23), 9183-9187 (1989)
   PUBMED   2556704
REFERENCE   9  (residues 1 to 469)
  AUTHORS   Kincaid,R.L., Nightingale,M.S. and Martin,B.M.
  TITLE     Characterization of a cDNA clone encoding the calmodulin-binding
            domain of mouse brain calcineurin
  JOURNAL   Proc Natl Acad Sci U S A 85 (23), 8983-8987 (1988)
   PUBMED   2848250
REFERENCE   10 (residues 1 to 469)
  AUTHORS   King,M.M., Huang,C.Y., Chock,P.B., Nairn,A.C., Hemmings,H.C. Jr.,
            Chan,K.F. and Greengard,P.
  TITLE     Mammalian brain phosphoproteins as substrates for calcineurin
  JOURNAL   J Biol Chem 259 (13), 8080-8083 (1984)
   PUBMED   6330098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001816.2, EU192652.1, AW973358.1 and AP001870.2.
            
            Transcript Variant: This variant (3) lacks multiple in-frame exons
            in the 3' coding region, compared to variant 1, and encodes a
            shorter protein (isoform 3), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU192652.1, SRR14038195.1760450.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..469
                     /product="protein phosphatase 3 catalytic subunit alpha
                     isoform 3"
                     /EC_number="3.1.3.16"
                     /note="calcineurin A alpha; CAM-PRP catalytic subunit;
                     protein phosphatase 3 catalytic subunit alpha isozyme; CNA
                     alpha"
                     /calculated_mol_wt=52541
     Region          41..329
                     /region_name="MPP_PP2B"
                     /note="PP2B, metallophosphatase domain; cd07416"
                     /db_xref="CDD:277361"
     Site            order(53,55,90,92,118,150,159,199,281,314)
                     /site_type="other"
                     /note="CN-CyPA-CsA complex [polypeptide binding]"
                     /db_xref="CDD:277361"
     Site            order(90,92,118,122,150..151,199,232,254,281,283)
                     /site_type="active"
                     /db_xref="CDD:277361"
     Site            order(90,92,118,150,199,281)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277361"
     CDS             1..469
                     /gene="PPP3CA"
                     /gene_synonym="ACCIID; CALN; CALNA; CALNA1; CNA1; DEE91;
                     IECEE; IECEE1; PPP2B"
                     /coded_by="NM_001130692.2:731..2140"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS47113.1"
                     /db_xref="GeneID:5530"
                     /db_xref="HGNC:HGNC:9314"
                     /db_xref="MIM:114105"
ORIGIN      
        1 msepkaidpk lsttdrvvka vpfppshrlt akevfdndgk prvdilkahl mkegrleesv
       61 alriitegas ilrqeknlld idapvtvcgd ihgqffdlmk lfevggspan trylflgdyv
      121 drgyfsiecv lylwalkily pktlfllrgn hecrhlteyf tfkqeckiky servydacmd
      181 afdclplaal mnqqflcvhg glspeintld dirkldrfke ppaygpmcdi lwsdpledfg
      241 nektqehfth ntvrgcsyfy sypavceflq hnnllsilra heaqdagyrm yrksqttgfp
      301 slitifsapn yldvynnkvt emlvnvlnic sddelgseed gfdgataaar kevirnkira
      361 igkmarvfsv lreesesvlt lkgltptgml psgvlsggkq tlqsaikgfs pqhkitsfee
      421 akgldriner mpprrdamps danlnsinka ltsetngtds ngsnssniq
//
LOCUS       NP_000776                508 aa            linear   PRI 12-JAN-2026
DEFINITION  25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial [Homo
            sapiens].
ACCESSION   NP_000776
VERSION     NP_000776.1
DBSOURCE    REFSEQ: accession NM_000785.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Murugesan,H., Sampath,P., A,V.K., R,S., Veerasamy,A.,
            Ranganathan,U.D., Paramasivam,S. and Bethunaickan,R.
  TITLE     Association of CYP27B1 gene polymorphisms with pulmonary
            tuberculosis and vitamin D levels
  JOURNAL   Gene 927, 148679 (2024)
   PUBMED   38876405
  REMARK    GeneRIF: Association of CYP27B1 gene polymorphisms with pulmonary
            tuberculosis and vitamin D levels.
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Dennis,C., Dillon,J., Cohen,D.J., Halquist,M.S., Pearcy,A.C.,
            Schwartz,Z. and Boyan,B.D.
  TITLE     Local production of active vitamin D3 metabolites in breast cancer
            cells by CYP24A1 and CYP27B1
  JOURNAL   J Steroid Biochem Mol Biol 232, 106331 (2023)
   PUBMED   37244301
  REMARK    GeneRIF: Local production of active vitamin D3 metabolites in
            breast cancer cells by CYP24A1 and CYP27B1.
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Meaux,M.N., Harambat,J., Rothenbuhler,A., Leger,J., Kamenicky,P.,
            Soskin,S., Boyer,O., Boros,E., D'Anella,P., Mignot,B., Gebhart,M.,
            Vic,P., Richard,N., Thivichon-Prince,B., Francou,B., Linglart,A.,
            Bacchetta,J. and Molin,A.
  TITLE     Genotype-phenotype Description of Vitamin D-dependent Rickets 1A:
            CYP27B1 p.(Ala129Thr) Variant Induces a Milder Disease
  JOURNAL   J Clin Endocrinol Metab 108 (4), 812-826 (2023)
   PUBMED   36321535
  REMARK    GeneRIF: Genotype-phenotype Description of Vitamin D-dependent
            Rickets 1A: CYP27B1 p.(Ala129Thr) Variant Induces a Milder Disease.
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Aftab,S., Khan,S.A., Malik,M.I., Imran,A., Anjum,M.N., Saeed,A.,
            Qureshi,A.A. and Cheema,H.A.
  TITLE     Clinical spectrum and diagnostic challenges of vitamin D dependent
            rickets type 1A (VDDR1A) caused by CYP27B1 mutation in resource
            limited countries
  JOURNAL   J Pediatr Endocrinol Metab 36 (2), 152-157 (2022)
   PUBMED   36524979
  REMARK    GeneRIF: Clinical spectrum and diagnostic challenges of vitamin D
            dependent rickets type 1A (VDDR1A) caused by CYP27B1 mutation in
            resource limited countries.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Luo,M., Liu,J., Yuan,Y., Chen,Y. and Yuan,G.
  TITLE     The role of vitamin D-synthesizing enzyme CYP27B1 in systemic lupus
            erythematosus
  JOURNAL   Turk J Med Sci 52 (4), 984-989 (2022)
   PUBMED   36326421
  REMARK    GeneRIF: The role of vitamin D-synthesizing enzyme CYP27B1 in
            systemic lupus erythematosus.
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Takeyama,K., Kitanaka,S., Sato,T., Kobori,M., Yanagisawa,J. and
            Kato,S.
  TITLE     25-Hydroxyvitamin D3 1alpha-hydroxylase and vitamin D synthesis
  JOURNAL   Science 277 (5333), 1827-1830 (1997)
   PUBMED   9295274
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Besancon,F., Just,J., Bourgeade,M.F., Van Weyenbergh,J.,
            Solomon,D., Guillozo,H., Wietzerbin,J. and Cayre,Y.E.
  TITLE     HIV-1 p17 and IFN-gamma both induce fructose 1,6-bisphosphatase
  JOURNAL   J Interferon Cytokine Res 17 (8), 461-467 (1997)
   PUBMED   9282826
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Szpirer,J., Szpirer,C., Riviere,M., Levan,G., Marynen,P.,
            Cassiman,J.J., Wiese,R. and DeLuca,H.F.
  TITLE     The Sp1 transcription factor gene (SP1) and the
            1,25-dihydroxyvitamin D3 receptor gene (VDR) are colocalized on
            human chromosome arm 12q and rat chromosome 7
  JOURNAL   Genomics 11 (1), 168-173 (1991)
   PUBMED   1662663
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Labuda,M., Morgan,K. and Glorieux,F.H.
  TITLE     Mapping autosomal recessive vitamin D dependency type I to
            chromosome 12q14 by linkage analysis
  JOURNAL   Am J Hum Genet 47 (1), 28-36 (1990)
   PUBMED   1971995
REFERENCE   10 (residues 1 to 508)
  AUTHORS   Pryke,A.M., Duggan,C., White,C.P., Posen,S. and Mason,R.S.
  TITLE     Tumor necrosis factor-alpha induces vitamin D-1-hydroxylase
            activity in normal human alveolar macrophages
  JOURNAL   J Cell Physiol 142 (3), 652-656 (1990)
   PUBMED   1690216
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB005038.1 and AW449645.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the cytochrome P450
            superfamily of enzymes. The cytochrome P450 proteins are
            monooxygenases which catalyze many reactions involved in drug
            metabolism and synthesis of cholesterol, steroids and other lipids.
            The protein encoded by this gene localizes to the inner
            mitochondrial membrane where it hydroxylates 25-hydroxyvitamin D3
            at the 1alpha position. This reaction synthesizes
            1alpha,25-dihydroxyvitamin D3, the active form of vitamin D3, which
            binds to the vitamin D receptor and regulates calcium metabolism.
            Thus this enzyme regulates the level of biologically active vitamin
            D and plays an important role in calcium homeostasis. Mutations in
            this gene can result in vitamin D-dependent rickets type I.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB005038.1, AF020192.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145774
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000228606.9/
                                                  ENSP00000228606.4
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q14.1"
     Protein         1..508
                     /product="25-hydroxyvitamin D-1 alpha hydroxylase,
                     mitochondrial"
                     /EC_number="1.14.15.18"
                     /note="25-OHD-1 alpha-hydroxylase; VD3 1A hydroxylase;
                     1alpha(OH)ase; 25 hydroxyvitamin D3-1-alpha hydroxylase;
                     calcidiol 1-monooxygenase; cytochrome p450 27B1;
                     cytochrome P450C1 alpha; cytochrome P450VD1-alpha;
                     cytochrome P450 subfamily XXVIIB polypeptide 1; cytochrome
                     P450, family 27, subfamily B, polypeptide 1"
                     /calculated_mol_wt=56373
     Region          68..503
                     /region_name="CYP27B1"
                     /note="cytochrome P450 family 27, subfamily B, polypeptide
                     1, also called calcidiol 1-monooxygenase; cd20648"
                     /db_xref="CDD:410741"
     Site            order(107,113,127,187..188,191,226,228..229,257,313,
                     316..317,320..321,383..388,493..494)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:410741"
     Site            order(107,126..127,134,138,314,317..318,321..322,325,
                     383..384,387,389,447..450,453..457,461)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410741"
     Site            455
                     /site_type="binding"
                     /note="heme binding site"
     CDS             1..508
                     /gene="CYP27B1"
                     /gene_synonym="CP2B; CYP1; CYP1alpha; CYP27B; P450c1;
                     PDDR; VDD1; VDDR; VDDRI"
                     /coded_by="NM_000785.4:38..1564"
                     /db_xref="CCDS:CCDS8954.1"
                     /db_xref="GeneID:1594"
                     /db_xref="HGNC:HGNC:2606"
                     /db_xref="MIM:609506"
ORIGIN      
        1 mtqtlkyasr vfhrvrwape lgaslgyrey hsarrsladi pgpstpsfla elfckgglsr
       61 lhelqvqgaa hfgpvwlasf gtvrtvyvaa palveellrq egprpercsf spwtehrrcr
      121 qracglltae geewqrlrsl laplllrpqa aaryagtlnn vvcdlvrrlr rqrgrgtgpp
      181 alvrdvagef ykfglegiaa vllgsrlgcl eaqvppdtet firavgsvfv stlltmamph
      241 wlrhlvpgpw grlcrdwdqm fafaqrhver reaeaamrng gqpekdlesg ahlthflfre
      301 elpaqsilgn vtelllagvd tvsntlswal yelsrhpevq talhseitaa lspgssayps
      361 atvlsqlpll kavvkevlrl ypvvpgnsrv pdkdihvgdy iipkntlvtl chyatsrdpa
      421 qfpepnsfrp arwlgegptp hpfaslpfgf gkrscmgrrl aelelqmala qilthfevqp
      481 epgaapvrpk trtvlvpers inlqfldr
//
LOCUS       NP_001122322             308 aa            linear   PRI 12-JAN-2026
DEFINITION  GTP-binding protein RAD [Homo sapiens].
ACCESSION   NP_001122322
VERSION     NP_001122322.1
DBSOURCE    REFSEQ: accession NM_001128850.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Sun,Z., Li,Y., Tan,X., Liu,W., He,X., Pan,D., Li,E., Xu,L. and
            Long,L.
  TITLE     Friend or Foe: Regulation, Downstream Effectors of RRAD in Cancer
  JOURNAL   Biomolecules 13 (3), 477 (2023)
   PUBMED   36979412
  REMARK    GeneRIF: Friend or Foe: Regulation, Downstream Effectors of RRAD in
            Cancer.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Katz,M., Subramaniam,S., Chomsky-Hecht,O., Tsemakhovich,V.,
            Flockerzi,V., Klussmann,E., Hirsch,J.A., Weiss,S. and Dascal,N.
  TITLE     Reconstitution of beta-adrenergic regulation of CaV1.2:
            Rad-dependent and Rad-independent protein kinase A mechanisms
  JOURNAL   Proc Natl Acad Sci U S A 118 (21) (2021)
   PUBMED   34001616
  REMARK    GeneRIF: Reconstitution of beta-adrenergic regulation of CaV1.2:
            Rad-dependent and Rad-independent protein kinase A mechanisms.
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Kim,H.K., Lee,I., Kim,S.T., Lee,J., Kim,K.M., Park,J.O. and
            Kang,W.K.
  TITLE     RRAD expression in gastric and colorectal cancer with peritoneal
            carcinomatosis
  JOURNAL   Sci Rep 9 (1), 19439 (2019)
   PUBMED   31857616
  REMARK    GeneRIF: RRAD expression in gastric and colorectal cancer with
            peritoneal carcinomatosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Belbachir,N., Portero,V., Al Sayed,Z.R., Gourraud,J.B.,
            Dilasser,F., Jesel,L., Guo,H., Wu,H., Gaborit,N., Guilluy,C.,
            Girardeau,A., Bonnaud,S., Simonet,F., Karakachoff,M., Pattier,S.,
            Scott,C., Burel,S., Marionneau,C., Chariau,C., Gaignerie,A.,
            David,L., Genin,E., Deleuze,J.F., Dina,C., Sauzeau,V., Loirand,G.,
            Baro,I., Schott,J.J., Probst,V., Wu,J.C., Redon,R., Charpentier,F.
            and Le Scouarnec,S.
  TITLE     RRAD mutation causes electrical and cytoskeletal defects in
            cardiomyocytes derived from a familial case of Brugada syndrome
  JOURNAL   Eur Heart J 40 (37), 3081-3094 (2019)
   PUBMED   31114854
  REMARK    GeneRIF: RRAD mutation causes electrical and cytoskeletal defects
            in cardiomyocytes derived from a familial case of Brugada syndrome.
REFERENCE   5  (residues 1 to 308)
  AUTHORS   Wei,Z., Guo,H., Qin,J., Lu,S., Liu,Q., Zhang,X., Zou,Y., Gong,Y.
            and Shao,C.
  TITLE     Pan-senescence transcriptome analysis identified RRAD as a marker
            and negative regulator of cellular senescence
  JOURNAL   Free Radic Biol Med 130, 267-277 (2019)
   PUBMED   30391675
  REMARK    GeneRIF: this study established RRAD to be a biomarker as well as a
            novel negative regulator of cellular senescence.
REFERENCE   6  (residues 1 to 308)
  AUTHORS   Caldwell,J.S., Moyers,J.S., Doria,A., Reynet,C. and Kahn,R.C.
  TITLE     Molecular cloning of the human rad gene: gene structure and
            complete nucleotide sequence
  JOURNAL   Biochim Biophys Acta 1316 (3), 145-148 (1996)
   PUBMED   8781531
REFERENCE   7  (residues 1 to 308)
  AUTHORS   Zhu,J., Bilan,P.J., Moyers,J.S., Antonetti,D.A. and Kahn,C.R.
  TITLE     Rad, a novel Ras-related GTPase, interacts with skeletal muscle
            beta-tropomyosin
  JOURNAL   J Biol Chem 271 (2), 768-773 (1996)
   PUBMED   8557685
REFERENCE   8  (residues 1 to 308)
  AUTHORS   Zhu,J., Reynet,C., Caldwell,J.S. and Kahn,C.R.
  TITLE     Characterization of Rad, a new member of Ras/GTPase superfamily,
            and its regulation by a unique GTPase-activating protein (GAP)-like
            activity
  JOURNAL   J Biol Chem 270 (9), 4805-4812 (1995)
   PUBMED   7876254
REFERENCE   9  (residues 1 to 308)
  AUTHORS   Doria,A., Caldwell,J.S., Ji,L., Reynet,C., Rich,S.S.,
            Weremowicz,S., Morton,C.C., Warram,J.H., Kahn,C.R. and
            Krolewski,A.S.
  TITLE     Trinucleotide repeats at the rad locus. Allele distributions in
            NIDDM and mapping to a 3-cM region on chromosome 16q
  JOURNAL   Diabetes 44 (2), 243-247 (1995)
   PUBMED   7859947
REFERENCE   10 (residues 1 to 308)
  AUTHORS   Reynet,C. and Kahn,C.R.
  TITLE     Rad: a member of the Ras family overexpressed in muscle of type II
            diabetic humans
  JOURNAL   Science 262 (5138), 1441-1444 (1993)
   PUBMED   8248782
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC057815.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 both encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC057815.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267757 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..308
                     /product="GTP-binding protein RAD"
                     /EC_number="3.6.5.2"
                     /note="RAS (RAD and GEM) like GTP binding 3; Ras-related
                     associated with diabetes; RRAD, Ras related glycolysis
                     inihibitor and calcium channel regulator; ras associated
                     with diabetes"
                     /calculated_mol_wt=33114
     Region          1..88
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55042.2)"
     Site            24
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88667; propagated from
                     UniProtKB/Swiss-Prot (P55042.2)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88667; propagated from
                     UniProtKB/Swiss-Prot (P55042.2)"
     Region          92..308
                     /region_name="RGK"
                     /note="Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras
                     GTPases; cd04148"
                     /db_xref="CDD:206715"
     Site            98..105
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206715"
     Site            order(99..100,146..147)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206715"
     Site            order(100..106,144,147,203..204,206,233..234)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206715"
     Site            order(105..106,118,120,127..128,141..142,144,146..147,235)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206715"
     Site            order(119..120,125..128)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206715"
     Site            order(119..124,125..127)
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206715"
     Site            121
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206715"
     Site            144..147
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206715"
     Site            order(146..147,155..158,161..164)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206715"
     Site            203..206
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206715"
     Site            233..235
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206715"
     Region          278..297
                     /region_name="Calmodulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P55042.2)"
     Site            302..305
                     /site_type="other"
                     /note="putative lipid modification site [posttranslational
                     modification]"
                     /db_xref="CDD:206715"
     CDS             1..308
                     /gene="RRAD"
                     /gene_synonym="RAD; REM3"
                     /coded_by="NM_001128850.2:152..1078"
                     /db_xref="CCDS:CCDS10824.1"
                     /db_xref="GeneID:6236"
                     /db_xref="HGNC:HGNC:10446"
                     /db_xref="MIM:179503"
ORIGIN      
        1 mtlngggsga ggsrgggqer errrgstpwg papplhrrsm pvderdlqaa ltpgaltaaa
       61 agtgtqgprl dwpedsedsl ssggsdsdes vykvlllgap gvgksalari fggvedgpea
      121 eaaghtydrs ivvdgeeasl mvydiweqdg grwlpghcma mgdayvivys vtdkgsfeka
      181 selrvqlrra rqtddvpiil vgnksdlvrs revsvdegra cavvfdckfi etsaalhhnv
      241 qalfegvvrq irlrrdskea narrqagtrr reslgkkakr flgrivarns rkmafraksk
      301 schdlsvl
//
LOCUS       NP_000413                432 aa            linear   PRI 12-JAN-2026
DEFINITION  keratin, type I cytoskeletal 17 [Homo sapiens].
ACCESSION   NP_000413
VERSION     NP_000413.1
DBSOURCE    REFSEQ: accession NM_000422.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Xu,Y., Cohen,E., Johnson,C.N., Parent,C.A. and Coulombe,P.A.
  TITLE     Repeated stress to the skin amplifies neutrophil infiltration in a
            keratin 17- and PKCalpha-dependent manner
  JOURNAL   PLoS Biol 22 (8), e3002779 (2024)
   PUBMED   39159283
  REMARK    GeneRIF: Repeated stress to the skin amplifies neutrophil
            infiltration in a keratin 17- and PKCalpha-dependent manner.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Romashin,D., Rusanov,A., Tolstova,T., Varshaver,A., Netrusov,A.,
            Kozhin,P. and Luzgina,N.
  TITLE     Loss of mutant p53 in HaCaT keratinocytes promotes cadmium-induced
            keratin 17 expression and cell death
  JOURNAL   Biochem Biophys Res Commun 709, 149834 (2024)
   PUBMED   38547608
  REMARK    GeneRIF: Loss of mutant p53 in HaCaT keratinocytes promotes
            cadmium-induced keratin 17 expression and cell death.
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Delgado-Coka,L., Horowitz,M., Torrente-Goncalves,M., Roa-Pena,L.,
            Leiton,C.V., Hasan,M., Babu,S., Fassler,D., Oentoro,J., Bai,J.K.,
            Petricoin,E.F. 3rd, Matrisian,L.M., Blais,E.M., Marchenko,N.,
            Allard,F.D., Jiang,W., Larson,B., Hendifar,A., Chen,C.,
            Abousamra,S., Samaras,D., Kurc,T., Saltz,J., Escobar-Hoyos,L.F. and
            Shroyer,K.R.
  TITLE     Keratin 17 modulates the immune topography of pancreatic cancer
  JOURNAL   J Transl Med 22 (1), 443 (2024)
   PUBMED   38730319
  REMARK    GeneRIF: Keratin 17 modulates the immune topography of pancreatic
            cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Lozar,T., Wang,W., Gavrielatou,N., Christensen,L., Lambert,P.F.,
            Harari,P.M., Rimm,D.L., Burtness,B., Grasic Kuhar,C. and
            Carchman,E.H.
  TITLE     Emerging Prognostic and Predictive Significance of Stress Keratin
            17 in HPV-Associated and Non HPV-Associated Human Cancers: A
            Scoping Review
  JOURNAL   Viruses 15 (12), 2320 (2023)
   PUBMED   38140561
  REMARK    GeneRIF: Emerging Prognostic and Predictive Significance of Stress
            Keratin 17 in HPV-Associated and Non HPV-Associated Human Cancers:
            A Scoping Review.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Wu,L., Ding,W., Wang,X., Li,X. and Yang,J.
  TITLE     Interference KRT17 reverses doxorubicin resistance in
            triple-negative breast cancer cells by Wnt/beta-catenin signaling
            pathway
  JOURNAL   Genes Genomics 45 (10), 1329-1338 (2023)
   PUBMED   37634232
  REMARK    GeneRIF: Interference KRT17 reverses doxorubicin resistance in
            triple-negative breast cancer cells by Wnt/beta-catenin signaling
            pathway.
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Smith,F.J.D., Hansen,C.D., Hull,P.R., Kaspar,R.L., McLean,W.H.I.,
            O'Toole,E. and Sprecher,E.
  TITLE     Pachyonychia Congenita
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301457
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Troyanovsky,S.M., Leube,R.E. and Franke,W.W.
  TITLE     Characterization of the human gene encoding cytokeratin 17 and its
            expression pattern
  JOURNAL   Eur J Cell Biol 59 (1), 127-137 (1992)
   PUBMED   1281771
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Flohr,T., Buwitt,U., Bonnekoh,B., Decker,T. and Bottger,E.C.
  TITLE     Interferon-gamma regulates expression of a novel keratin class I
            gene
  JOURNAL   Eur J Immunol 22 (4), 975-979 (1992)
   PUBMED   1372562
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Trask,D.K., Band,V., Zajchowski,D.A., Yaswen,P., Suh,T. and
            Sager,R.
  TITLE     Keratins as markers that distinguish normal and tumor-derived
            mammary epithelial cells
  JOURNAL   Proc Natl Acad Sci U S A 87 (6), 2319-2323 (1990)
   PUBMED   1690428
REFERENCE   10 (residues 1 to 432)
  AUTHORS   Kartasova,T., Cornelissen,B.J., Belt,P. and van de Putte,P.
  TITLE     Effects of UV, 4-NQO and TPA on gene expression in cultured human
            epidermal keratinocytes
  JOURNAL   Nucleic Acids Res 15 (15), 5945-5962 (1987)
   PUBMED   2442723
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP226061.1 and BC011901.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the type I intermediate filament chain
            keratin 17, expressed in nail bed, hair follicle, sebaceous glands,
            and other epidermal appendages. Mutations in this gene lead to
            Jackson-Lawler type pachyonychia congenita and steatocystoma
            multiplex. [provided by RefSeq, Aug 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.58324.1,
                                           SRR5189658.113620.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000311208.13/ ENSP00000308452.8
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..432
                     /product="keratin, type I cytoskeletal 17"
                     /note="cytokeratin-17; keratin 17, type I"
                     /calculated_mol_wt=47975
     Region          1..83
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04695.2)"
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04695.2)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q04695.2)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q04695.2)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61414; propagated from
                     UniProtKB/Swiss-Prot (Q04695.2)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q04695.2)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q04695.2)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA1.
                     /evidence=ECO:0000269|PubMed:22006917; propagated from
                     UniProtKB/Swiss-Prot (Q04695.2)"
     Region          84..394
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          84..120
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04695.2)"
     Region          102..116
                     /region_name="Peptide epitope S1, induces T-cell and
                     keratinocyte proliferation and IFN-gamma production"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04695.2)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q04695.2)"
     Region          121..138
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04695.2)"
     Region          139..230
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04695.2)"
     Region          153..167
                     /region_name="Peptide epitope S2, induces T-cell
                     proliferation and IFN-gamma production"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04695.2)"
     Region          231..250
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04695.2)"
     Region          251..392
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04695.2)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6IFV3; propagated from
                     UniProtKB/Swiss-Prot (Q04695.2)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q04695.2)"
     Region          332..346
                     /region_name="Peptide epitope S4, induces T-cell and
                     keratinocyte proliferation and IFN-gamma production"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04695.2)"
     Region          393..432
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04695.2)"
     CDS             1..432
                     /gene="KRT17"
                     /gene_synonym="39.1; CK-17; K17; PC2; PCHC1"
                     /coded_by="NM_000422.3:67..1365"
                     /db_xref="CCDS:CCDS11402.1"
                     /db_xref="GeneID:3872"
                     /db_xref="HGNC:HGNC:6427"
                     /db_xref="MIM:148069"
ORIGIN      
        1 mttsirqfts sssikgssgl gggssrtscr lsgglgagsc rlgsagglgs tlggssyssc
       61 ysfgsgggyg ssfggvdgll aggekatmqn lndrlasyld kvraleeant elevkirdwy
      121 qrqapgpard ysqyyrtiee lqnkiltatv dnanillqid narlaaddfr tkfeteqalr
      181 lsveadingl rrvldeltla radlemqien lkeelaylkk nheeemnalr gqvggeinve
      241 mdaapgvdls rilnemrdqy ekmaeknrkd aedwffskte elnrevatns elvqsgksei
      301 selrrtmqal eielqsqlsm kaslegnlae tenrycvqls qiqgligsve eqlaqlrcem
      361 eqqnqeykil ldvktrleqe iatyrrlleg edahltqykk epvttrqvrt iveevqdgkv
      421 issreqvhqt tr
//
LOCUS       NP_006763               1343 aa            linear   PRI 12-JAN-2026
DEFINITION  ras/Rap GTPase-activating protein SynGAP isoform 1 [Homo sapiens].
ACCESSION   NP_006763
VERSION     NP_006763.2
DBSOURCE    REFSEQ: accession NM_006772.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1343)
  AUTHORS   Bednarczuk,N., Housby,H., Lee,I.O., Consortium,I., Skuse,D. and
            Wolstencroft,J.
  TITLE     Behavioural and neurodevelopmental characteristics of SYNGAP1
  JOURNAL   J Neurodev Disord 16 (1), 46 (2024)
   PUBMED   39148034
  REMARK    GeneRIF: Behavioural and neurodevelopmental characteristics of
            SYNGAP1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1343)
  AUTHORS   Kim,H.J., Kim,M., Jang,S., Cho,J.S., Kim,S.Y., Cho,A., Kim,H.,
            Lim,B.C., Chae,J.H., Choi,J., Kim,K.J. and Kim,W.
  TITLE     SYNGAP1-related developmental and epileptic encephalopathy:
            Genotypic and phenotypic characteristics and longitudinal insights
  JOURNAL   Am J Med Genet A 194 (8), e63606 (2024)
   PUBMED   38563110
  REMARK    GeneRIF: SYNGAP1-related developmental and epileptic
            encephalopathy: Genotypic and phenotypic characteristics and
            longitudinal insights.
REFERENCE   3  (residues 1 to 1343)
  AUTHORS   Wright,D., Kenny,A., Eley,S., McKechanie,A.G. and Stanfield,A.C.
  TITLE     Visual social attention in SYNGAP1-related intellectual disability
  JOURNAL   Autism Res 17 (6), 1083-1093 (2024)
   PUBMED   38698724
  REMARK    GeneRIF: Visual social attention in SYNGAP1-related intellectual
            disability.
REFERENCE   4  (residues 1 to 1343)
  AUTHORS   Wright,D., Kenny,A., Mizen,L.A.M., McKechanie,A.G. and
            Stanfield,A.C.
  TITLE     The Behavioral Profile of SYNGAP1-Related Intellectual Disability
  JOURNAL   Am J Intellect Dev Disabil 129 (3), 199-214 (2024)
   PUBMED   38657965
  REMARK    GeneRIF: The Behavioral Profile of SYNGAP1-Related Intellectual
            Disability.
REFERENCE   5  (residues 1 to 1343)
  AUTHORS   Carvill,G.L., Heavin,S.B., Yendle,S.C., McMahon,J.M., O'Roak,B.J.,
            Cook,J., Khan,A., Dorschner,M.O., Weaver,M., Calvert,S., Malone,S.,
            Wallace,G., Stanley,T., Bye,A.M., Bleasel,A., Howell,K.B.,
            Kivity,S., Mackay,M.T., Rodriguez-Casero,V., Webster,R.,
            Korczyn,A., Afawi,Z., Zelnick,N., Lerman-Sagie,T., Lev,D.,
            Moller,R.S., Gill,D., Andrade,D.M., Freeman,J.L., Sadleir,L.G.,
            Shendure,J., Berkovic,S.F., Scheffer,I.E. and Mefford,H.C.
  TITLE     Targeted resequencing in epileptic encephalopathies identifies de
            novo mutations in CHD2 and SYNGAP1
  JOURNAL   Nat Genet 45 (7), 825-830 (2013)
   PUBMED   23708187
  REMARK    GeneRIF: De novo CHD2 and SYNGAP1 mutations are new causes of
            epileptic encephalopathies, accounting for 1.2% and 1% of cases,
            respectively.
REFERENCE   6  (residues 1 to 1343)
  AUTHORS   Berryer,M.H., Hamdan,F.F., Klitten,L.L., Moller,R.S., Carmant,L.,
            Schwartzentruber,J., Patry,L., Dobrzeniecka,S., Rochefort,D.,
            Neugnot-Cerioli,M., Lacaille,J.C., Niu,Z., Eng,C.M., Yang,Y.,
            Palardy,S., Belhumeur,C., Rouleau,G.A., Tommerup,N., Immken,L.,
            Beauchamp,M.H., Patel,G.S., Majewski,J., Tarnopolsky,M.A.,
            Scheffzek,K., Hjalgrim,H., Michaud,J.L. and Di Cristo,G.
  TITLE     Mutations in SYNGAP1 cause intellectual disability, autism, and a
            specific form of epilepsy by inducing haploinsufficiency
  JOURNAL   Hum Mutat 34 (2), 385-394 (2013)
   PUBMED   23161826
  REMARK    GeneRIF: De novo missense mutations, p.R579X, and possibly all the
            other truncating mutations in SYNGAP1 result in a loss of its
            function, causing intellectual disability, autism, and a specific
            form of epilepsy.
REFERENCE   7  (residues 1 to 1343)
  AUTHORS   Kim,J.H., Liao,D., Lau,L.F. and Huganir,R.L.
  TITLE     SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90
            protein family
  JOURNAL   Neuron 20 (4), 683-691 (1998)
   PUBMED   9581761
REFERENCE   8  (residues 1 to 1343)
  AUTHORS   Kroll,J. and Waltenberger,J.
  TITLE     The vascular endothelial growth factor receptor KDR activates
            multiple signal transduction pathways in porcine aortic endothelial
            cells
  JOURNAL   J Biol Chem 272 (51), 32521-32527 (1997)
   PUBMED   9405464
REFERENCE   9  (residues 1 to 1343)
  AUTHORS   Holder,J.L. Jr., Hamdan,F.F. and Michaud,J.L.
  TITLE     SYNGAP1-Related Intellectual Disability
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30789692
REFERENCE   10 (residues 1 to 1343)
  AUTHORS   Fantl,W.J., Escobedo,J.A., Martin,G.A., Turck,C.W., del Rosario,M.,
            McCormick,F. and Williams,L.T.
  TITLE     Distinct phosphotyrosines on a growth factor receptor bind to
            specific molecules that mediate different signaling pathways
  JOURNAL   Cell 69 (3), 413-423 (1992)
   PUBMED   1374684
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL662799.16, DA057307.1,
            AK307888.1, AK094225.1, AL713634.1, BX282051.1 and AK124666.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 15, 2008 this sequence version replaced NP_006763.1.
            
            Summary: This gene encodes a Ras GTPase activating protein that is
            a member of the N-methyl-D-aspartate receptor complex. The
            N-terminal domain of the protein contains a Ras-GAP domain, a
            pleckstrin homology domain, and a C2 domain that may be involved in
            binding of calcium and phospholipids. The C-terminal domain
            consists of a ten histidine repeat region, serine and tyrosine
            phosphorylation sites, and a T/SXV motif required for postsynaptic
            scaffold protein interaction. The encoded protein negatively
            regulates Ras, Rap and
            alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor
            trafficking to the postsynaptic membrane to regulate synaptic
            plasticity and neuronal homeostasis. Allelic variants of this gene
            are associated with intellectual disability and autism spectrum
            disorder. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Nov 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1966682,
                              SAMEA1968189 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000646630.1/ ENSP00000496007.1
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1343
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.32"
     Protein         1..1343
                     /product="ras/Rap GTPase-activating protein SynGAP isoform
                     1"
                     /note="synaptic Ras GTPase activating protein, 135kDa; Ras
                     GTPase-activating protein SynGAP; neuronal RasGAP;
                     synaptic Ras GTPase activating protein 1 homolog; ras/Rap
                     GTPase-activating protein SynGAP; Ras/Rap
                     GTPase-activating protein 1"
                     /calculated_mol_wt=148154
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          92..129
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          122..313
                     /region_name="PH_SynGAP"
                     /note="Synaptic Ras-GTPase activating protein Pleckstrin
                     homology (PH) domain; cd13375"
                     /db_xref="CDD:270178"
     Region          252..414
                     /region_name="C2_SynGAP_like"
                     /note="C2 domain present in Ras GTPase activating protein
                     (GAP) family; cd04013"
                     /db_xref="CDD:175980"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          373..394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          405..728
                     /region_name="RasGAP_DAB2IP"
                     /note="Ras-GTPase Activating Domain of DAB2IP and similar
                     proteins; cd05136"
                     /db_xref="CDD:213338"
     Site            order(444,481,483,485..486,488,491,495,587,595..596,
                     599..600,603,624,627..628,631,635,637,642..643)
                     /site_type="other"
                     /note="putative RAS interface [polypeptide binding]"
                     /db_xref="CDD:213338"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            485
                     /site_type="other"
                     /note="Arginine finger, crucial for GTP hydrolysis by
                     stabilizing the transition state.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00167; propagated
                     from UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          718..1316
                     /region_name="DUF3498"
                     /note="Domain of unknown function (DUF3498); pfam12004"
                     /db_xref="CDD:463427"
     Region          725..753
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            752
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            780
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          781..805
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          785..815
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            823
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            825
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            828
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            836
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            840
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            842
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            876
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            892
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            895
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK2.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            898
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          933..1017
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            985
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          1033..1154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            1114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            1118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            1121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QUH6; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            1165
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Site            1204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:F6SEU4; propagated from
                     UniProtKB/Swiss-Prot (Q96PV0.4)"
     Region          1274..1343
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PV0.4)"
     CDS             1..1343
                     /gene="SYNGAP1"
                     /gene_synonym="MRD5; RASA5; SYNGAP"
                     /coded_by="NM_006772.3:201..4232"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34434.2"
                     /db_xref="GeneID:8831"
                     /db_xref="HGNC:HGNC:11497"
                     /db_xref="MIM:603384"
ORIGIN      
        1 msrsrasihr gsipamsyap frdvrgpsmh rtqyvhspyd rpgwnprfci isgnqllmld
       61 edeihpllir drrsessrnk llrrtvsvpv egrphgehey hlgrsrrksv pggkqysmeg
      121 apaapfrpsq gflsrrlkss ikrtksqpkl drtssfrqil prfrsadhdr arlmqsfkes
      181 hshesllsps saaealelnl dedsiikpvh ssilgqefcf evttssgtkc facrsaaerd
      241 kwienlqrav kpnkdnsrrv dnvlklwiie arelppkkry ycelclddml yarttskprs
      301 asgdtvfwge hfefnnlpav ralrlhlyrd sdkkrkkdka gyvglvtvpv atlagrhfte
      361 qwypvtlptg sggsggmgsg ggggsgggsg gkgkggcpav rlkaryqtms ilpmelykef
      421 aeyvtnhyrm lcavlepaln vkgkeevasa lvhilqstgk akdflsdmam sevdrfmere
      481 hlifrentla tkaieeymrl igqkylkdai gefiralyes eencevdpik ctasslaehq
      541 anlrmccela lckvvnshcv fprelkevfa swrlrcaerg rediadrlis aslflrflcp
      601 aimspslfgl mqeypdeqts rtltliakvi qnlanfskft skedflgfmn eflelewgsm
      661 qqflyeisnl dtltnsssfe gyidlgrels tlhallwevl pqlskeallk lgplprllnd
      721 istalrnpni qrqpsrqser prpqpvvlrg psaemqgymm rdlnssidlq sfmarglnss
      781 mdmarlpspt kekppppppg ggkdlfyvsr pplarsspay ctsssditep eqkmlsvnks
      841 vsmldlqgdg pggrlnsssv snlaavgdll hssqasltaa lglrpapagr lsqgsgssit
      901 aagmrlsqmg vttdgvpaqq lriplsfqnp lfhmaadgpg ppgghggggg hgppsshhhh
      961 hhhhhhrgge ppgdtfapfh gysksedlss gvpkppaasi lhshsysdef gpsgtdftrr
     1021 qlslqdnlqh mlsppqitig pqrpapsgpg ggsgggsggg gggqppplqr gksqqltvsa
     1081 aqkprpssgn llqspepsyg parprqqsls kegsiggsgg sggggggglk psitkqhsqt
     1141 pstlnptmpa sertvawvsn mphlsadies ahiereeykl keysksmdes rldrvkeyee
     1201 eihslkerlh msnrkleeye rrllsqeeqt skilmqyqar leqsekrlrq qqaekdsqik
     1261 siigrlmlve eelrrdhpam aeplpepkkr lldaqerqlp plgptnprvt lappwnglap
     1321 pappppprlq itengefrnt adh
//
LOCUS       NP_004155                134 aa            linear   PRI 12-JAN-2026
DEFINITION  retinol-binding protein 2 [Homo sapiens].
ACCESSION   NP_004155
VERSION     NP_004155.2
DBSOURCE    REFSEQ: accession NM_004164.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 134)
  AUTHORS   Feng,T.F., Yao,D.M., Zheng,R., Jiang,D.S., Zhang,L.L., Xing,Q. and
            Li,L.
  TITLE     [Effect of RBP2 gene silencing on proliferation, migration and
            invasion of ovarian epithelial cancer SKOV3/DDP cells and its
            mechanism]
  JOURNAL   Zhonghua Zhong Liu Za Zhi 44 (2), 139-146 (2022)
   PUBMED   35184457
  REMARK    GeneRIF: [Effect of RBP2 gene silencing on proliferation, migration
            and invasion of ovarian epithelial cancer SKOV3/DDP cells and its
            mechanism].
REFERENCE   2  (residues 1 to 134)
  AUTHORS   Silvaroli,J.A., Plau,J., Adams,C.H., Banerjee,S.,
            Widjaja-Adhi,M.A.K., Blaner,W.S. and Golczak,M.
  TITLE     Molecular basis for the interaction of cellular retinol binding
            protein 2 (CRBP2) with nonretinoid ligands
  JOURNAL   J Lipid Res 62, 100054 (2021)
   PUBMED   33631211
  REMARK    GeneRIF: Molecular basis for the interaction of cellular retinol
            binding protein 2 (CRBP2) with nonretinoid ligands.
REFERENCE   3  (residues 1 to 134)
  AUTHORS   Menozzi,I., Polverini,E. and Berni,R.
  TITLE     Deciphering protein dynamics changes along the pathway of retinol
            uptake by cellular retinol-binding proteins 1 and 2
  JOURNAL   Arch Biochem Biophys 645, 107-116 (2018)
   PUBMED   29567208
  REMARK    GeneRIF: molecular dynamics simulations for the uptake of retinol
            by CRBP 1 and 2
REFERENCE   4  (residues 1 to 134)
  AUTHORS   Yu,X., Chen,H., Zuo,C., Jin,X., Yin,Y., Wang,H., Jin,M., Ozato,K.
            and Xu,S.
  TITLE     Chromatin remodeling: demethylating H3K4me3 of type I IFNs gene by
            Rbp2 through interacting with Piasy for transcriptional attenuation
  JOURNAL   FASEB J 32 (2), 552-567 (2018)
   PUBMED   28970247
  REMARK    GeneRIF: study demonstrates that Piasy may prevent exaggerated
            transcription of IFNI by Rbp2-mediated demethylation of H3K4me3 of
            IFNI, avoiding excessive immune responses
REFERENCE   5  (residues 1 to 134)
  AUTHORS   Zargar,Z.U., Kimidi,M.R. and Tyagi,S.
  TITLE     Dynamic site-specific recruitment of RBP2 by pocket protein p130
            modulates H3K4 methylation on E2F-responsive promoters
  JOURNAL   Nucleic Acids Res 46 (1), 174-188 (2018)
   PUBMED   29059406
REFERENCE   6  (residues 1 to 134)
  AUTHORS   Herr,F.M. and Ong,D.E.
  TITLE     Differential interaction of lecithin-retinol acyltransferase with
            cellular retinol binding proteins
  JOURNAL   Biochemistry 31 (29), 6748-6755 (1992)
   PUBMED   1322170
REFERENCE   7  (residues 1 to 134)
  AUTHORS   Inagami,S. and Ong,D.E.
  TITLE     Purification and partial characterization of cellular
            retinol-binding protein, type two, from human small intestine
  JOURNAL   J Nutr 122 (3), 450-456 (1992)
   PUBMED   1542003
REFERENCE   8  (residues 1 to 134)
  AUTHORS   Astrom,A., Tavakkol,A., Pettersson,U., Cromie,M., Elder,J.T. and
            Voorhees,J.J.
  TITLE     Molecular cloning of two human cellular retinoic acid-binding
            proteins (CRABP). Retinoic acid-induced expression of CRABP-II but
            not CRABP-I in adult human skin in vivo and in skin fibroblasts in
            vitro
  JOURNAL   J Biol Chem 266 (26), 17662-17666 (1991)
   PUBMED   1654334
REFERENCE   9  (residues 1 to 134)
  AUTHORS   Colantuoni,V., Cortese,R., Nilsson,M., Lundvall,J., Bavik,C.O.,
            Eriksson,U., Peterson,P.A. and Sundelin,J.
  TITLE     Cloning and sequencing of a full length cDNA corresponding to human
            cellular retinol-binding protein
  JOURNAL   Biochem Biophys Res Commun 130 (1), 431-439 (1985)
   PUBMED   2992469
REFERENCE   10 (residues 1 to 134)
  AUTHORS   van Eijk,H.G., Tio,T.H. and Bos,G.
  TITLE     Iron in skin biopsies
  JOURNAL   Arch Dermatol Forsch 251 (3), 245-248 (1975)
   PUBMED   1115525
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC097103.8, BX282005.1 and
            AW772327.1.
            
            On Dec 24, 2003 this sequence version replaced NP_004155.1.
            
            Summary: This gene encodes an abundant protein present in the small
            intestinal epithelium. It is thought to participate in the uptake
            and/or intracellular metabolism of vitamin A. Vitamin A is a
            fat-soluble vitamin necessary for growth, reproduction,
            differentiation of epithelial tissues, and vision. This protein may
            also modulate the supply of retinoic acid to the nuclei of
            endometrial cells during the menstrual cycle. [provided by RefSeq,
            Aug 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AW772327.1, AK291978.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144835, SAMEA2152474
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000232217.6/ ENSP00000232217.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..134
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q23"
     Protein         1..134
                     /product="retinol-binding protein 2"
                     /note="cellular retinol-binding protein II; retinol
                     binding protein 2, cellular"
                     /calculated_mol_wt=15576
     Region          4..134
                     /region_name="CRBP2"
                     /note="cellular retinol-binding protein 2; cd19463"
                     /db_xref="CDD:381238"
     Site            order(5,11,17,20..21,24,26,30..31,33..34,37,39,41,43,50,
                     52,54,56,58..61,63,65,73,75,77..78,94,96,105,107,109,116,
                     118,120,129,131)
                     /site_type="other"
                     /note="ligand binding cavity [chemical binding]"
                     /db_xref="CDD:381238"
     Site            order(5,11,17,20..21,24,26,30,33..34,39,41,43,50,52,54,56,
                     58..61,63,77..78,94,105,107,109,118,120,131)
                     /site_type="other"
                     /note="retinol binding site [chemical binding]"
                     /db_xref="CDD:381238"
     CDS             1..134
                     /gene="RBP2"
                     /gene_synonym="CRABP-II; CRBP-II; CRBP2; CRBPII; RBPC2"
                     /coded_by="NM_004164.3:58..462"
                     /db_xref="CCDS:CCDS3109.1"
                     /db_xref="GeneID:5948"
                     /db_xref="HGNC:HGNC:9920"
                     /db_xref="MIM:180280"
ORIGIN      
        1 mtrdqngtwe mesnenfegy mkaldidfat rkiavrltqt kvidqdgdnf ktkttstfrn
       61 ydvdftvgve fdeytksldn rhvkalvtwe gdvlvcvqkg ekenrgwkqw iegdklylel
      121 tcgdqvcrqv fkkk
//
LOCUS       NP_001124163             511 aa            linear   PRI 12-JAN-2026
DEFINITION  protein phosphatase 3 catalytic subunit alpha isoform 2 [Homo
            sapiens].
ACCESSION   NP_001124163
VERSION     NP_001124163.1
DBSOURCE    REFSEQ: accession NM_001130691.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Masaki,T., Habara,M., Shibutani,S., Hanaki,S., Sato,Y., Tomiyasu,H.
            and Shimada,M.
  TITLE     Dephosphorylation of the EGFR protein by calcineurin at serine
            1046/1047 enhances its stability
  JOURNAL   Biochem Biophys Res Commun 641, 84-92 (2023)
   PUBMED   36525928
  REMARK    GeneRIF: Dephosphorylation of the EGFR protein by calcineurin at
            serine 1046/1047 enhances its stability.
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Wang,Z., Li,H., Wang,H., Li,X., Zhang,Q., Wang,H., Li,K. and Qiu,Y.
  TITLE     TRIM72 exerts antitumor effects in breast cancer and modulates
            lactate production and MCT4 promoter activity by interacting with
            PPP3CA
  JOURNAL   Anticancer Drugs 33 (5), 489-501 (2022)
   PUBMED   35324524
  REMARK    GeneRIF: TRIM72 exerts antitumor effects in breast cancer and
            modulates lactate production and MCT4 promoter activity by
            interacting with PPP3CA.
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Etges,A., Hellmig,N., Walenda,G., Haddad,B.G., Machtens,J.P.,
            Morosan,T., Rump,L.C. and Scholl,U.I.
  TITLE     A Novel Homozygous KLHL3 Mutation as a Cause of Autosomal Recessive
            Pseudohypoaldosteronism Type II Diagnosed Late in Life
  JOURNAL   Nephron 146 (4), 418-428 (2022)
   PUBMED   35093948
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Vymazal,O., Bendickova,K., De Zuani,M., Vlkova,M.,
            Hortova-Kohoutkova,M. and Fric,J.
  TITLE     Immunosuppression Affects Neutrophil Functions: Does
            Calcineurin-NFAT Signaling Matter?
  JOURNAL   Front Immunol 12, 770515 (2021)
   PUBMED   34795676
  REMARK    GeneRIF: Immunosuppression Affects Neutrophil Functions: Does
            Calcineurin-NFAT Signaling Matter?
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Giri,P.R., Higuchi,S. and Kincaid,R.L.
  TITLE     Chromosomal mapping of the human genes for the calmodulin-dependent
            protein phosphatase (calcineurin) catalytic subunit
  JOURNAL   Biochem Biophys Res Commun 181 (1), 252-258 (1991)
   PUBMED   1659808
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Kincaid,R.L., Giri,P.R., Higuchi,S., Tamura,J., Dixon,S.C.,
            Marietta,C.A., Amorese,D.A. and Martin,B.M.
  TITLE     Cloning and characterization of molecular isoforms of the catalytic
            subunit of calcineurin using nonisotopic methods
  JOURNAL   J Biol Chem 265 (19), 11312-11319 (1990)
   PUBMED   2162844
REFERENCE   8  (residues 1 to 511)
  AUTHORS   Guerini,D. and Klee,C.B.
  TITLE     Cloning of human calcineurin A: evidence for two isozymes and
            identification of a polyproline structural domain
  JOURNAL   Proc Natl Acad Sci U S A 86 (23), 9183-9187 (1989)
   PUBMED   2556704
REFERENCE   9  (residues 1 to 511)
  AUTHORS   Kincaid,R.L., Nightingale,M.S. and Martin,B.M.
  TITLE     Characterization of a cDNA clone encoding the calmodulin-binding
            domain of mouse brain calcineurin
  JOURNAL   Proc Natl Acad Sci U S A 85 (23), 8983-8987 (1988)
   PUBMED   2848250
REFERENCE   10 (residues 1 to 511)
  AUTHORS   King,M.M., Huang,C.Y., Chock,P.B., Nairn,A.C., Hemmings,H.C. Jr.,
            Chan,K.F. and Greengard,P.
  TITLE     Mammalian brain phosphoproteins as substrates for calcineurin
  JOURNAL   J Biol Chem 259 (13), 8080-8083 (1984)
   PUBMED   6330098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001816.2, EU192652.1, BC025714.1, AW973358.1 and AP001870.2.
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            3' coding region, compared to variant 1, and encodes a shorter
            protein (isoform 2), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025714.1, AK290532.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..511
                     /product="protein phosphatase 3 catalytic subunit alpha
                     isoform 2"
                     /EC_number="3.1.3.16"
                     /note="calcineurin A alpha; CAM-PRP catalytic subunit;
                     protein phosphatase 3 catalytic subunit alpha isozyme; CNA
                     alpha"
                     /calculated_mol_wt=57528
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q08209.1)"
     Region          41..345
                     /region_name="MPP_PP2B"
                     /note="PP2B, metallophosphatase domain; cd07416"
                     /db_xref="CDD:277361"
     Site            order(53,55,90,92,118,150,159,199,281,314,341)
                     /site_type="other"
                     /note="CN-CyPA-CsA complex [polypeptide binding]"
                     /db_xref="CDD:277361"
     Region          56..340
                     /region_name="Catalytic. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08209.1)"
     Site            order(90,92,118,122,150..151,199,232,254,281,283)
                     /site_type="active"
                     /db_xref="CDD:277361"
     Site            order(90,92,118,150,199,281)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277361"
     Region          307..311
                     /region_name="SAPNY motif.
                     /evidence=ECO:0000305|PubMed:26248042"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08209.1)"
     Region          327..336
                     /region_name="Interaction with PxIxIF motif in substrate.
                     /evidence=ECO:0000269|PubMed:17498738,
                     ECO:0000269|PubMed:17502104, ECO:0000269|PubMed:22343722,
                     ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26248042"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08209.1)"
     Region          341..369
                     /region_name="Calcineurin B binding.
                     /evidence=ECO:0000269|PubMed:12218175,
                     ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738,
                     ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:27974827,
                     ECO:0000269|PubMed:8524402"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08209.1)"
     Site            352
                     /site_type="other"
                     /note="Interaction with PxVP motif in substrate.
                     /evidence=ECO:0000269|PubMed:23468591,
                     ECO:0000269|PubMed:27974827; propagated from
                     UniProtKB/Swiss-Prot (Q08209.1)"
     Region          392..406
                     /region_name="Calmodulin-binding.
                     /evidence=ECO:0000269|PubMed:18384083,
                     ECO:0000269|PubMed:19404396, ECO:0000269|PubMed:25144868,
                     ECO:0000269|Ref.34"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08209.1)"
     Region          407..414
                     /region_name="Autoinhibitory segment.
                     /evidence=ECO:0000250|UniProtKB:P16298"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08209.1)"
     Region          455..477
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000269|PubMed:8524402"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08209.1)"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63329; propagated from
                     UniProtKB/Swiss-Prot (Q08209.1)"
     Region          465..511
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08209.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08209.1)"
     CDS             1..511
                     /gene="PPP3CA"
                     /gene_synonym="ACCIID; CALN; CALNA; CALNA1; CNA1; DEE91;
                     IECEE; IECEE1; PPP2B"
                     /coded_by="NM_001130691.2:731..2266"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47114.1"
                     /db_xref="GeneID:5530"
                     /db_xref="HGNC:HGNC:9314"
                     /db_xref="MIM:114105"
ORIGIN      
        1 msepkaidpk lsttdrvvka vpfppshrlt akevfdndgk prvdilkahl mkegrleesv
       61 alriitegas ilrqeknlld idapvtvcgd ihgqffdlmk lfevggspan trylflgdyv
      121 drgyfsiecv lylwalkily pktlfllrgn hecrhlteyf tfkqeckiky servydacmd
      181 afdclplaal mnqqflcvhg glspeintld dirkldrfke ppaygpmcdi lwsdpledfg
      241 nektqehfth ntvrgcsyfy sypavceflq hnnllsilra heaqdagyrm yrksqttgfp
      301 slitifsapn yldvynnkaa vlkyennvmn irqfncsphp ywlpnfmdvf twslpfvgek
      361 vtemlvnvln icsddelgse edgfdgataa arkevirnki raigkmarvf svlreesesv
      421 ltlkgltptg mlpsgvlsgg kqtlqsaikg fspqhkitsf eeakgldrin ermpprrdam
      481 psdanlnsin kaltsetngt dsngsnssni q
//
LOCUS       NP_001093241            1075 aa            linear   PRI 12-JAN-2026
DEFINITION  POTE ankyrin domain family member F [Homo sapiens].
ACCESSION   NP_001093241 XP_001130062
VERSION     NP_001093241.1
DBSOURCE    REFSEQ: accession NM_001099771.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1075)
  AUTHORS   Reed,A.E., Peraza,J., van den Haak,F., Hernandez,E.R., Gibbs,R.A.,
            Chinn,I.K., Lupski,J.R., Marchi,E., Reshef,R., Alobeid,B.,
            Mace,E.M. and Orange,J.S.
  TITLE     beta-Actin G342D as a Cause of NK Cell Deficiency Impairing Lytic
            Synapse Termination
  JOURNAL   J Immunol 212 (6), 962-973 (2024)
   PUBMED   38315012
  REMARK    GeneRIF: beta-Actin G342D as a Cause of NK Cell Deficiency
            Impairing Lytic Synapse Termination.
REFERENCE   2  (residues 1 to 1075)
  AUTHORS   Al-Fakhar,M.S.Q., Bilgin,N., Moesgaard,L., Witecka,A., Drozak,J.,
            Kongsted,J. and Mecinovic,J.
  TITLE     The Role of Trp79 in beta-Actin on Histidine Methyltransferase
            SETD3 Catalysis
  JOURNAL   Chembiochem 24 (21), e202300490 (2023)
   PUBMED   37581408
  REMARK    GeneRIF: The Role of Trp79 in beta-Actin on Histidine
            Methyltransferase SETD3 Catalysis.
REFERENCE   3  (residues 1 to 1075)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1075)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 1075)
  AUTHORS   Pieragostino,D., Agnifili,L., Fasanella,V., D'Aguanno,S.,
            Mastropasqua,R., Di Ilio,C., Sacchetta,P., Urbani,A. and Del
            Boccio,P.
  TITLE     Shotgun proteomics reveals specific modulated protein patterns in
            tears of patients with primary open angle glaucoma naive to therapy
  JOURNAL   Mol Biosyst 9 (6), 1108-1116 (2013)
   PUBMED   23580065
REFERENCE   6  (residues 1 to 1075)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   7  (residues 1 to 1075)
  AUTHORS   Bastos-Amador,P., Royo,F., Gonzalez,E., Conde-Vancells,J.,
            Palomo-Diez,L., Borras,F.E. and Falcon-Perez,J.M.
  TITLE     Proteomic analysis of microvesicles from plasma of healthy donors
            reveals high individual variability
  JOURNAL   J Proteomics 75 (12), 3574-3584 (2012)
   PUBMED   22516433
REFERENCE   8  (residues 1 to 1075)
  AUTHORS   Liu,X.F., Bera,T.K., Liu,L.J. and Pastan,I.
  TITLE     A primate-specific POTE-actin fusion protein plays a role in
            apoptosis
  JOURNAL   Apoptosis 14 (10), 1237-1244 (2009)
   PUBMED   19669888
  REMARK    GeneRIF: POTE gene family encodes a new family of proapoptotic
            proteins.
REFERENCE   9  (residues 1 to 1075)
  AUTHORS   Lee,Y., Ise,T., Ha,D., Saint Fleur,A., Hahn,Y., Liu,X.F.,
            Nagata,S., Lee,B., Bera,T.K. and Pastan,I.
  TITLE     Evolution and expression of chimeric POTE-actin genes in the human
            genome
  JOURNAL   Proc Natl Acad Sci U S A 103 (47), 17885-17890 (2006)
   PUBMED   17101985
REFERENCE   10 (residues 1 to 1075)
  AUTHORS   Chang,K.W., Yang,P.Y., Lai,H.Y., Yeh,T.S., Chen,T.C. and Yeh,C.T.
  TITLE     Identification of a novel actin isoform in hepatocellular carcinoma
  JOURNAL   Hepatol Res 36 (1), 33-39 (2006)
   PUBMED   16824795
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC018804.9 and AC018865.4.
            
            On Jul 26, 2007 this sequence version replaced XP_001130062.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF523384.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA2142853 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000409914.7/ ENSP00000386786.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1075
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q21.1"
     Protein         1..1075
                     /product="POTE ankyrin domain family member F"
                     /note="prostate, ovary, testis expressed protein on
                     chromosome 2; POTE-2 alpha-actin; chimeric POTE-actin
                     protein; ANKRD26-like family C member 1B; beta actin"
                     /calculated_mol_wt=121314
     Region          138..368
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          172..201
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (A5A3E0.2)"
     Region          174..203
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          205..236
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          205..234
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (A5A3E0.2)"
     Site            order(238,240,244..245,248..250,252..253,257,260,269,271,
                     273,277..278,281..283,285..286,290,293,302,304,306,
                     310..311,314..316,318..319,323,326,335)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          238..269
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          238..267
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (A5A3E0.2)"
     Region          271..302
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          271..300
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (A5A3E0.2)"
     Region          304..335
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          304..333
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (A5A3E0.2)"
     Region          369..530
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A5A3E0.2)"
     Region          544..596
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A5A3E0.2)"
     Region          648..>701
                     /region_name="CCDC144C"
                     /note="CCDC144C protein coiled-coil region; pfam14915"
                     /db_xref="CDD:464371"
     Region          702..1075
                     /region_name="Actin-like"
                     /note="propagated from UniProtKB/Swiss-Prot (A5A3E0.2)"
     Region          706..1070
                     /region_name="ASKHA_NBD_actin"
                     /note="nucleotide-binding domain (NBD) of actin and
                     similar proteins; cd10224"
                     /db_xref="CDD:466823"
     CDS             1..1075
                     /gene="POTEF"
                     /gene_synonym="A26C1B; POTE2alpha; POTEACTIN"
                     /coded_by="NM_001099771.2:401..3628"
                     /db_xref="CCDS:CCDS46409.1"
                     /db_xref="GeneID:728378"
                     /db_xref="HGNC:HGNC:33905"
ORIGIN      
        1 mvvevdsmpa assvkkpfgl rskmgkwccr cfpccresgk snvgtsgdhd dsamktlrsk
       61 mgkwcrhcfp ccrgsgksnv gasgdhddsa mktlrnkmgk wcchcfpccr gsskskvgaw
      121 gdyddsafme pryhvrgedl dklhraawwg kvprkdlivm lrdtdvnkqd kqkrtalhla
      181 sangnsevvk llldrrcqln vldnkkrtal ikavqcqede calmllehgt dpnipdeygn
      241 ttlhyaiyne dklmakalll ygadiesknk hgltplllgv heqkqqvvkf likkkanlna
      301 ldrygrtali lavccgsasi vsllleqnid vssqdlsgqt areyavsshh hvicqllsdy
      361 kekqmlkiss ensnpeqdlk ltseeesqrf kgsensqpek msqepeinkd gdreveeemk
      421 khesnnvgll enltngvtag ngdnglipqr ksrtpenqqf pdneseeyhr icellsdyke
      481 kqmpkyssen snpeqdlklt seeesqrlkg sengqpekrs qepeinkdgd relenfmaie
      541 emkkhrsthv gfpenltnga tagngddgli pprksrtpes qqfpdtenee yhsdeqndtq
      601 kqfceeqntg ilhdeilihe ekqievvekm nselslsckk ekdilhenst lreeiamlrl
      661 eldtmkhqsq lrekkyledi esvkkrndnl lkalqlnelt mdddtavlvi dngsgmckag
      721 fagddaprav fpsivgrprq qgmmggmhqk esyvgkeaqs krgiltlkyp mehgiitnwd
      781 dmekiwhhtf ynelrvapee hpvllteatl npkanrekmt qimfetfntp amyvaiqavl
      841 slytsgrttg ivmdsgdgvt htvpiyegna lphatlrldl agrelpdylm kiltehgyrf
      901 ttmaereivr dikeklcyva ldfeqematv assssleksy elpdgqviti gnerfrcpea
      961 lfqpcflgme scgihettfn simksdvdir kdlytntvls ggttmypgma hrmqkeiaal
     1021 apsmmkirii appkrkysvw vggsilasls tfqqmwiskq eydesgpsiv hrkcl
//
LOCUS       NP_001342172              99 aa            linear   PRI 13-JAN-2026
DEFINITION  protein NCBP2AS2 [Homo sapiens].
ACCESSION   NP_001342172
VERSION     NP_001342172.1
DBSOURCE    REFSEQ: accession NM_001355243.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Xu,W., Deng,B., Lin,P., Liu,C., Li,B., Huang,Q., Zhou,H., Yang,J.
            and Qu,L.
  TITLE     Ribosome profiling analysis identified a KRAS-interacting
            microprotein that represses oncogenic signaling in hepatocellular
            carcinoma cells
  JOURNAL   Sci China Life Sci 63 (4), 529-542 (2020)
   PUBMED   31240521
REFERENCE   5  (residues 1 to 99)
  AUTHORS   Kugeratski,F.G., Atkinson,S.J., Neilson,L.J., Lilla,S.,
            Knight,J.R.P., Serneels,J., Juin,A., Ismail,S., Bryant,D.M.,
            Markert,E.K., Machesky,L.M., Mazzone,M., Sansom,O.J. and Zanivan,S.
  TITLE     Hypoxic cancer-associated fibroblasts increase NCBP2-AS2/HIAR to
            promote endothelial sprouting through enhanced VEGF signaling
  JOURNAL   Sci Signal 12 (567) (2019)
   PUBMED   30723174
  REMARK    GeneRIF: The uncharacterized protein hypoxia-induced angiogenesis
            regulator (NCBP2-AS2) that was renamed HIAR (hypoxia-induced
            angiogenesis regulator) was the protein most increased in abundance
            in hypoxic cancer-associated fibroblasts (CAFs).
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC062368.1 and AC011322.29.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AK123020.1, AL832915.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000602845.2/ ENSP00000488305.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..99
                     /product="protein NCBP2AS2"
                     /note="NCBP2 antisense gene protein 2; hypoxia-induced
                     angiogenesis regulator; NCBP2 antisense RNA 2 (head to
                     head); KRAS-interacting microprotein"
                     /calculated_mol_wt=10759
     Region          76..99
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q69YL0.1)"
     CDS             1..99
                     /gene="NCBP2AS2"
                     /gene_synonym="HIAR; KRASIM; NCBP2-AS2"
                     /coded_by="NM_001355243.2:44..343"
                     /db_xref="CCDS:CCDS87189.1"
                     /db_xref="GeneID:152217"
                     /db_xref="HGNC:HGNC:25121"
                     /db_xref="MIM:621467"
ORIGIN      
        1 mvlrrllaal lhspqlverl sesrpirraa qltafallqa qlrgqdaarr lqdlaagpvg
       61 slcrraerfr daftqelrrg lrgrsgpppg sqrgpgani
//
LOCUS       NP_066012                456 aa            linear   PRI 14-JAN-2026
DEFINITION  N(6)-adenosine-methyltransferase non-catalytic subunit METTL14
            [Homo sapiens].
ACCESSION   NP_066012
VERSION     NP_066012.1
DBSOURCE    REFSEQ: accession NM_020961.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Zhang,M., Xie,Z., Tan,Y., Wu,Y., Wang,M., Zhang,P., Yuan,Y. and
            Li,J.
  TITLE     METTL14-mediated N6-methyladenosine modification of TCP1 mRNA
            promotes acute myeloid leukemia progression
  JOURNAL   Cell Signal 122, 111304 (2024)
   PUBMED   39033992
  REMARK    GeneRIF: METTL14-mediated N6-methyladenosine modification of TCP1
            mRNA promotes acute myeloid leukemia progression.
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Chen,J.H., Li,J.J., Yuan,Y., Tian,Q., Feng,D.D., Zhuang,L.L.,
            Cao,Q., Zhou,G.P. and Jin,R.
  TITLE     ETS1 and RBPJ transcriptionally regulate METTL14 to suppress
            TGF-beta1-induced epithelial-mesenchymal transition in human
            bronchial epithelial cells
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (7), 167349 (2024)
   PUBMED   39002703
  REMARK    GeneRIF: ETS1 and RBPJ transcriptionally regulate METTL14 to
            suppress TGF-beta1-induced epithelial-mesenchymal transition in
            human bronchial epithelial cells.
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Zhang,Z., Mao,H., Li,F., Wang,D. and Liu,Y.
  TITLE     METTL14-mediated lncRNA-FAS-AS1 promotes osteoarthritis progression
            by up-regulating ADAM8
  JOURNAL   Int J Rheum Dis 27 (9), e15323 (2024)
   PUBMED   39221886
  REMARK    GeneRIF: METTL14-mediated lncRNA-FAS-AS1 promotes osteoarthritis
            progression by up-regulating ADAM8.
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Gu,X., Song,Y., Liu,X., Cheng,Z., Min,J. and Zhang,Y.
  TITLE     METTL14-Mediated m6A Modification of TUG1 Represses Ferroptosis in
            Alzheimer's Disease via Inhibiting GDF15 Ubiquitination
  JOURNAL   Front Biosci (Landmark Ed) 29 (8), 298 (2024)
   PUBMED   39206905
  REMARK    GeneRIF: METTL14-Mediated m6A Modification of TUG1 Represses
            Ferroptosis in Alzheimer's Disease via Inhibiting GDF15
            Ubiquitination.
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Hu,C., Song,S., Zhao,S., Xue,Z. and Zhu,X.
  TITLE     METTL14 contributes to the progression of nasopharyngeal carcinoma
            through regulating the stability of AOC1 mRNA
  JOURNAL   Hereditas 161 (1), 20 (2024)
   PUBMED   38956710
  REMARK    GeneRIF: METTL14 contributes to the progression of nasopharyngeal
            carcinoma through regulating the stability of AOC1 mRNA.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Bystrom,S., Ayoglu,B., Haggmark,A., Mitsios,N., Hong,M.G.,
            Drobin,K., Forsstrom,B., Fredolini,C., Khademi,M., Amor,S.,
            Uhlen,M., Olsson,T., Mulder,J., Nilsson,P. and Schwenk,J.M.
  TITLE     Affinity proteomic profiling of plasma, cerebrospinal fluid, and
            brain tissue within multiple sclerosis
  JOURNAL   J Proteome Res 13 (11), 4607-4619 (2014)
   PUBMED   25231264
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Schwartz,S., Mumbach,M.R., Jovanovic,M., Wang,T., Maciag,K.,
            Bushkin,G.G., Mertins,P., Ter-Ovanesyan,D., Habib,N.,
            Cacchiarelli,D., Sanjana,N.E., Freinkman,E., Pacold,M.E.,
            Satija,R., Mikkelsen,T.S., Hacohen,N., Zhang,F., Carr,S.A.,
            Lander,E.S. and Regev,A.
  TITLE     Perturbation of m6A writers reveals two distinct classes of mRNA
            methylation at internal and 5' sites
  JOURNAL   Cell Rep 8 (1), 284-296 (2014)
   PUBMED   24981863
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Wang,Y., Li,Y., Toth,J.I., Petroski,M.D., Zhang,Z. and Zhao,J.C.
  TITLE     N6-methyladenosine modification destabilizes developmental
            regulators in embryonic stem cells
  JOURNAL   Nat Cell Biol 16 (2), 191-198 (2014)
   PUBMED   24394384
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Liu,J., Yue,Y., Han,D., Wang,X., Fu,Y., Zhang,L., Jia,G., Yu,M.,
            Lu,Z., Deng,X., Dai,Q., Chen,W. and He,C.
  TITLE     A METTL3-METTL14 complex mediates mammalian nuclear RNA
            N6-adenosine methylation
  JOURNAL   Nat Chem Biol 10 (2), 93-95 (2014)
   PUBMED   24316715
  REMARK    GeneRIF: methyltransferase-like protein 14 in a complex with METTL3
            mediates nuclear RNA methylation
REFERENCE   10 (residues 1 to 456)
  AUTHORS   Kalsi,G., Kuo,P.H., Aliev,F., Alexander,J., McMichael,O.,
            Patterson,D.G., Walsh,D., Zhao,Z., Schuckit,M., Nurnberger,J. Jr.,
            Edenberg,H., Kramer,J., Hesselbrock,V., Tischfield,J.A.,
            Vladimirov,V., Prescott,C.A., Dick,D.M., Kendler,K.S. and
            Riley,B.P.
  TITLE     A systematic gene-based screen of chr4q22-q32 identifies
            association of a novel susceptibility gene, DKK2, with the
            quantitative trait of alcohol dependence symptom counts
  JOURNAL   Hum Mol Genet 19 (12), 2497-2506 (2010)
   PUBMED   20332099
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Erratum:[Hum Mol Genet. 2010 Oct 15;19(20):4121. Hesselbrock,
            Victor [added]; Tischfield, Jay A [added]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG773151.1, AB046847.1, AC110079.3 and AW206149.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.236387.1,
                                           SRR1803614.73332.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000388822.10/ ENSP00000373474.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..456
                     /product="N(6)-adenosine-methyltransferase non-catalytic
                     subunit METTL14"
                     /EC_number="2.1.1.62"
                     /note="methyltransferase-like protein 14;
                     N6-adenosine-methyltransferase subunit METTL14;
                     N6-adenosine-methyltransferase non-catalytic subunit;
                     methyltransferase like 14; methyltransferase 14,
                     N6-adenosine-methyltransferase subunit; methyltransferase
                     14, N6-adenosine-methyltransferase complex catalytic
                     subunit"
                     /calculated_mol_wt=52020
     Region          50..75
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE5.2)"
     Region          135..136
                     /region_name="Interaction with METTL3.
                     /evidence=ECO:0000269|PubMed:27281194,
                     ECO:0007744|PDB:5IL0, ECO:0007744|PDB:5IL1,
                     ECO:0007744|PDB:5IL2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE5.2)"
     Site            146
                     /site_type="other"
                     /note="Interaction with METTL3.
                     /evidence=ECO:0000269|PubMed:27281194,
                     ECO:0007744|PDB:5IL0, ECO:0007744|PDB:5IL1,
                     ECO:0007744|PDB:5IL2; propagated from UniProtKB/Swiss-Prot
                     (Q9HCE5.2)"
     Region          186..363
                     /region_name="MT-A70"
                     /note="pfam05063"
                     /db_xref="CDD:368270"
     Region          237..238
                     /region_name="Interaction with METTL3.
                     /evidence=ECO:0000269|PubMed:27281194,
                     ECO:0007744|PDB:5IL0, ECO:0007744|PDB:5IL1,
                     ECO:0007744|PDB:5IL2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE5.2)"
     Site            242
                     /site_type="other"
                     /note="Interaction with METTL3.
                     /evidence=ECO:0000269|PubMed:27281194,
                     ECO:0007744|PDB:5IL0, ECO:0007744|PDB:5IL1,
                     ECO:0007744|PDB:5IL2; propagated from UniProtKB/Swiss-Prot
                     (Q9HCE5.2)"
     Region          245..254
                     /region_name="Positively charged region required for
                     RNA-binding. /evidence=ECO:0000269|PubMed:27281194"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE5.2)"
     Site            245
                     /site_type="other"
                     /note="Interaction with METTL3.
                     /evidence=ECO:0000269|PubMed:27281194,
                     ECO:0007744|PDB:5IL0, ECO:0007744|PDB:5IL1,
                     ECO:0007744|PDB:5IL2; propagated from UniProtKB/Swiss-Prot
                     (Q9HCE5.2)"
     Region          255..258
                     /region_name="Interaction with METTL3.
                     /evidence=ECO:0000269|PubMed:27281194,
                     ECO:0007744|PDB:5IL0, ECO:0007744|PDB:5IL1,
                     ECO:0007744|PDB:5IL2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE5.2)"
     Region          278..287
                     /region_name="Interaction with METTL3.
                     /evidence=ECO:0000269|PubMed:27281194,
                     ECO:0007744|PDB:5IL0, ECO:0007744|PDB:5IL1,
                     ECO:0007744|PDB:5IL2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE5.2)"
     Region          297..298
                     /region_name="Positively charged region required for
                     RNA-binding. /evidence=ECO:0000269|PubMed:27281194"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE5.2)"
     Site            298
                     /site_type="other"
                     /note="Interaction with METTL3.
                     /evidence=ECO:0000269|PubMed:27281194,
                     ECO:0007744|PDB:5IL0, ECO:0007744|PDB:5IL1,
                     ECO:0007744|PDB:5IL2; propagated from UniProtKB/Swiss-Prot
                     (Q9HCE5.2)"
     Region          308..312
                     /region_name="Interaction with METTL3.
                     /evidence=ECO:0000269|PubMed:27281194,
                     ECO:0007744|PDB:5IL0, ECO:0007744|PDB:5IL1,
                     ECO:0007744|PDB:5IL2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE5.2)"
     Region          393..456
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCE5.2)"
     Site            399
                     /site_type="other"
                     /note="Interaction with METTL3.
                     /evidence=ECO:0000269|PubMed:27281194,
                     ECO:0007744|PDB:5IL0, ECO:0007744|PDB:5IL1,
                     ECO:0007744|PDB:5IL2; propagated from UniProtKB/Swiss-Prot
                     (Q9HCE5.2)"
     Site            399
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:27281194,
                     ECO:0000269|PubMed:29348140, ECO:0007744|PDB:5IL0,
                     ECO:0007744|PDB:5IL1, ECO:0007744|PDB:5IL2,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9HCE5.2)"
     CDS             1..456
                     /gene="METTL14"
                     /gene_synonym="hMETTL14"
                     /coded_by="NM_020961.4:144..1514"
                     /db_xref="CCDS:CCDS34053.1"
                     /db_xref="GeneID:57721"
                     /db_xref="HGNC:HGNC:29330"
                     /db_xref="MIM:616504"
ORIGIN      
        1 mdsrlqeire rqklrrqlla qqlgaesads igavlnskde qreiaetret crasydtsap
       61 nakrkyldeg etdedkmeey kdelemqqde enlpyeeeiy kdsstflkgt qslnphndyc
      121 qhfvdtghrp qnfirdvgla drfeeypklr elirlkdeli aksntppmyl qadieafdir
      181 eltpkfdvil leppleeyyr etgitanekc wtwddimkle ideiaaprsf iflwcgsgeg
      241 ldlgrvclrk wgyrrcedic wiktnknnpg ktktldpkav fqrtkehclm gikgtvkrst
      301 dgdfihanvd idliiteepe igniekpvei fhiiehfclg rrrlhlfgrd stirpgwltv
      361 gptltnsnyn aetyasyfsa pnsyltgcte eierlrpksp ppksksdrgg gaprgggrgg
      421 tsagrgrern rsnfrgergg frggrggahr ggfppr
//
LOCUS       NP_064563                328 aa            linear   PRI 14-JAN-2026
DEFINITION  carbonic anhydrase-related protein 10 precursor [Homo sapiens].
ACCESSION   NP_064563
VERSION     NP_064563.1
DBSOURCE    REFSEQ: accession NM_020178.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Li,Q., Zhang,L., Zhang,Z., Fan,Y. and Zhang,Q.
  TITLE     Carbonic anhydrase 10 functions as a tumor suppressor in renal cell
            carcinoma and its methylation is a risk factor for survival outcome
  JOURNAL   Urol Oncol 40 (4), 168 (2022)
   PUBMED   34980544
  REMARK    GeneRIF: Carbonic anhydrase 10 functions as a tumor suppressor in
            renal cell carcinoma and its methylation is a risk factor for
            survival outcome.
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kreuzer,M., Banerjee,A., Birts,C.N., Darley,M., Tavassoli,A.,
            Ivan,M. and Blaydes,J.P.
  TITLE     Glycolysis, via NADH-dependent dimerisation of CtBPs, regulates
            hypoxia-induced expression of CAIX and stem-like breast cancer cell
            survival
  JOURNAL   FEBS Lett 594 (18), 2988-3001 (2020)
   PUBMED   32618367
  REMARK    GeneRIF: Glycolysis, via NADH-dependent dimerisation of CtBPs,
            regulates hypoxia-induced expression of CAIX and stem-like breast
            cancer cell survival.
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Ge,A., Gao,S., Liu,Y., Zhang,H., Wang,X., Zhang,L., Pang,D. and
            Zhao,Y.
  TITLE     Methylation of WT1, CA10 in peripheral blood leukocyte is
            associated with breast cancer risk: a case-control study
  JOURNAL   BMC Cancer 20 (1), 713 (2020)
   PUBMED   32736539
  REMARK    GeneRIF: Methylation of WT1, CA10 in peripheral blood leukocyte is
            associated with breast cancer risk: a case-control study.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Aspatwar,A., Tolvanen,M.E.E., Schneider,H.P., Becker,H.M.,
            Narkilahti,S., Parkkila,S. and Deitmer,J.W.
  TITLE     Catalytically inactive carbonic anhydrase-related proteins enhance
            transport of lactate by MCT1
  JOURNAL   FEBS Open Bio 9 (7), 1204-1211 (2019)
   PUBMED   31033227
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Tao,B., Ling,Y., Zhang,Y., Li,S., Zhou,P., Wang,X., Li,B., Jun,Z.,
            Zhang,W., Xu,C., Shi,J., Wang,L., Zhang,W. and Li,S.
  TITLE     CA10 and CA11 negatively regulate neuronal activity-dependent
            growth of gliomas
  JOURNAL   Mol Oncol 13 (5), 1018-1032 (2019)
   PUBMED   30636076
  REMARK    GeneRIF: results suggest that CA11 and CA10 negatively regulate
            neuronal activity-dependent glioma growth and inhibit glioma
            aggression. Thus, CA11/CA10 may represent a potential therapeutic
            target for the treatment of gliomas.
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Supuran,C.T., Scozzafava,A. and Casini,A.
  TITLE     Carbonic anhydrase inhibitors
  JOURNAL   Med Res Rev 23 (2), 146-189 (2003)
   PUBMED   12500287
  REMARK    Review article
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Taniuchi,K., Nishimori,I., Takeuchi,T., Fujikawa-Adachi,K.,
            Ohtsuki,Y. and Onishi,S.
  TITLE     Developmental expression of carbonic anhydrase-related proteins
            VIII, X, and XI in the human brain
  JOURNAL   Neuroscience 112 (1), 93-99 (2002)
   PUBMED   12044474
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Okamoto,N., Fujikawa-Adachi,K., Nishimori,I., Taniuchi,K. and
            Onishi,S.
  TITLE     cDNA sequence of human carbonic anhydrase-related protein, CA-RP X:
            mRNA expressions of CA-RP X and XI in human brain
  JOURNAL   Biochim Biophys Acta 1518 (3), 311-316 (2001)
   PUBMED   11311946
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Kleiderlein,J.J., Nisson,P.E., Jessee,J., Li,W.B., Becker,K.G.,
            Derby,M.L., Ross,C.A. and Margolis,R.L.
  TITLE     CCG repeats in cDNAs from human brain
  JOURNAL   Hum Genet 103 (6), 666-673 (1998)
   PUBMED   9921901
  REMARK    GeneRIF: Identifies a string of seven CCG repeats in the 5' UTR of
            a carbonic anhydrase X cDNA from human brain.
            Erratum:[Hum Genet 1999 Jan;104(1):113]
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Hewett-Emmett,D. and Tashian,R.E.
  TITLE     Functional diversity, conservation, and convergence in the
            evolution of the alpha-, beta-, and gamma-carbonic anhydrase gene
            families
  JOURNAL   Mol Phylogenet Evol 5 (1), 50-77 (1996)
   PUBMED   8673298
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA128892.1, BC047456.1,
            AW135066.1 and AC005883.14.
            
            Summary: This gene encodes a protein that belongs to the carbonic
            anhydrase family of zinc metalloenzymes, which catalyze the
            reversible hydration of carbon dioxide in various biological
            processes. The protein encoded by this gene is an acatalytic member
            of the alpha-carbonic anhydrase subgroup, and it is thought to play
            a role in the central nervous system, especially in brain
            development. Multiple transcript variants encoding the same protein
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.459666.1, BC068462.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000451037.7/ ENSP00000405388.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.33-q22"
     Protein         1..328
                     /product="carbonic anhydrase-related protein 10 precursor"
                     /note="carbonic anhydrase-related protein 10; carbonic
                     anhydrase-related protein X; cerebral protein-15; CARP X;
                     CA-RP X; carbonic anhydrase X; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=35142
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2439
     Region          46..302
                     /region_name="alpha_CARP_X_XI_like"
                     /note="Carbonic anhydrase alpha related protein: groups X,
                     XI and related proteins. This subgroup contains carbonic
                     anhydrase related proteins (CARPs) X and XI, which have
                     been implicated in various biological processes of the
                     central nervous system. CARPs are...; cd03121"
                     /db_xref="CDD:239395"
     CDS             1..328
                     /gene="CA10"
                     /gene_synonym="CA-RPX; CARPX; HUCEP-15"
                     /coded_by="NM_020178.5:929..1915"
                     /db_xref="CCDS:CCDS32684.1"
                     /db_xref="GeneID:56934"
                     /db_xref="HGNC:HGNC:1369"
                     /db_xref="MIM:604642"
ORIGIN      
        1 meivwevlfl lqanfivcis aqqnspkihe gwwaykevvq gsfvpvpsfw glvnsawnlc
       61 svgkrqspvn ietshmifdp fltplrintg grkvsgtmyn tgrhvslrld kehlvnisgg
      121 pmtyshrlee irlhfgseds qgsehllngq afsgevqlih ynhelytnvt eaakspnglv
      181 vvsifikvsd ssnpflnrml nrdtitrity kndayllqgl nieelypets sfitydgsmt
      241 ippcyetasw iimnkpvyit rmqmhslrll sqnqpsqifl smsdnfrpvq plnnrcirtn
      301 infslqgkdc pnnraqklqy rvnewllk
//
LOCUS       NP_001076003             328 aa            linear   PRI 14-JAN-2026
DEFINITION  carbonic anhydrase-related protein 10 precursor [Homo sapiens].
ACCESSION   NP_001076003
VERSION     NP_001076003.1
DBSOURCE    REFSEQ: accession NM_001082534.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Li,Q., Zhang,L., Zhang,Z., Fan,Y. and Zhang,Q.
  TITLE     Carbonic anhydrase 10 functions as a tumor suppressor in renal cell
            carcinoma and its methylation is a risk factor for survival outcome
  JOURNAL   Urol Oncol 40 (4), 168 (2022)
   PUBMED   34980544
  REMARK    GeneRIF: Carbonic anhydrase 10 functions as a tumor suppressor in
            renal cell carcinoma and its methylation is a risk factor for
            survival outcome.
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kreuzer,M., Banerjee,A., Birts,C.N., Darley,M., Tavassoli,A.,
            Ivan,M. and Blaydes,J.P.
  TITLE     Glycolysis, via NADH-dependent dimerisation of CtBPs, regulates
            hypoxia-induced expression of CAIX and stem-like breast cancer cell
            survival
  JOURNAL   FEBS Lett 594 (18), 2988-3001 (2020)
   PUBMED   32618367
  REMARK    GeneRIF: Glycolysis, via NADH-dependent dimerisation of CtBPs,
            regulates hypoxia-induced expression of CAIX and stem-like breast
            cancer cell survival.
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Ge,A., Gao,S., Liu,Y., Zhang,H., Wang,X., Zhang,L., Pang,D. and
            Zhao,Y.
  TITLE     Methylation of WT1, CA10 in peripheral blood leukocyte is
            associated with breast cancer risk: a case-control study
  JOURNAL   BMC Cancer 20 (1), 713 (2020)
   PUBMED   32736539
  REMARK    GeneRIF: Methylation of WT1, CA10 in peripheral blood leukocyte is
            associated with breast cancer risk: a case-control study.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Aspatwar,A., Tolvanen,M.E.E., Schneider,H.P., Becker,H.M.,
            Narkilahti,S., Parkkila,S. and Deitmer,J.W.
  TITLE     Catalytically inactive carbonic anhydrase-related proteins enhance
            transport of lactate by MCT1
  JOURNAL   FEBS Open Bio 9 (7), 1204-1211 (2019)
   PUBMED   31033227
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Tao,B., Ling,Y., Zhang,Y., Li,S., Zhou,P., Wang,X., Li,B., Jun,Z.,
            Zhang,W., Xu,C., Shi,J., Wang,L., Zhang,W. and Li,S.
  TITLE     CA10 and CA11 negatively regulate neuronal activity-dependent
            growth of gliomas
  JOURNAL   Mol Oncol 13 (5), 1018-1032 (2019)
   PUBMED   30636076
  REMARK    GeneRIF: results suggest that CA11 and CA10 negatively regulate
            neuronal activity-dependent glioma growth and inhibit glioma
            aggression. Thus, CA11/CA10 may represent a potential therapeutic
            target for the treatment of gliomas.
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Supuran,C.T., Scozzafava,A. and Casini,A.
  TITLE     Carbonic anhydrase inhibitors
  JOURNAL   Med Res Rev 23 (2), 146-189 (2003)
   PUBMED   12500287
  REMARK    Review article
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Taniuchi,K., Nishimori,I., Takeuchi,T., Fujikawa-Adachi,K.,
            Ohtsuki,Y. and Onishi,S.
  TITLE     Developmental expression of carbonic anhydrase-related proteins
            VIII, X, and XI in the human brain
  JOURNAL   Neuroscience 112 (1), 93-99 (2002)
   PUBMED   12044474
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Okamoto,N., Fujikawa-Adachi,K., Nishimori,I., Taniuchi,K. and
            Onishi,S.
  TITLE     cDNA sequence of human carbonic anhydrase-related protein, CA-RP X:
            mRNA expressions of CA-RP X and XI in human brain
  JOURNAL   Biochim Biophys Acta 1518 (3), 311-316 (2001)
   PUBMED   11311946
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Kleiderlein,J.J., Nisson,P.E., Jessee,J., Li,W.B., Becker,K.G.,
            Derby,M.L., Ross,C.A. and Margolis,R.L.
  TITLE     CCG repeats in cDNAs from human brain
  JOURNAL   Hum Genet 103 (6), 666-673 (1998)
   PUBMED   9921901
  REMARK    GeneRIF: Identifies a string of seven CCG repeats in the 5' UTR of
            a carbonic anhydrase X cDNA from human brain.
            Erratum:[Hum Genet 1999 Jan;104(1):113]
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Hewett-Emmett,D. and Tashian,R.E.
  TITLE     Functional diversity, conservation, and convergence in the
            evolution of the alpha-, beta-, and gamma-carbonic anhydrase gene
            families
  JOURNAL   Mol Phylogenet Evol 5 (1), 50-77 (1996)
   PUBMED   8673298
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092713.2, DA518921.1,
            AF288385.1, AC005883.14 and AW135066.1.
            
            Summary: This gene encodes a protein that belongs to the carbonic
            anhydrase family of zinc metalloenzymes, which catalyze the
            reversible hydration of carbon dioxide in various biological
            processes. The protein encoded by this gene is an acatalytic member
            of the alpha-carbonic anhydrase subgroup, and it is thought to play
            a role in the central nervous system, especially in brain
            development. Multiple transcript variants encoding the same protein
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: GQ901003.1, AF288385.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.33-q22"
     Protein         1..328
                     /product="carbonic anhydrase-related protein 10 precursor"
                     /note="carbonic anhydrase-related protein 10; carbonic
                     anhydrase-related protein X; cerebral protein-15; CARP X;
                     CA-RP X; carbonic anhydrase X; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=35142
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2439
     Region          46..302
                     /region_name="alpha_CARP_X_XI_like"
                     /note="Carbonic anhydrase alpha related protein: groups X,
                     XI and related proteins. This subgroup contains carbonic
                     anhydrase related proteins (CARPs) X and XI, which have
                     been implicated in various biological processes of the
                     central nervous system. CARPs are...; cd03121"
                     /db_xref="CDD:239395"
     CDS             1..328
                     /gene="CA10"
                     /gene_synonym="CA-RPX; CARPX; HUCEP-15"
                     /coded_by="NM_001082534.2:684..1670"
                     /db_xref="CCDS:CCDS32684.1"
                     /db_xref="GeneID:56934"
                     /db_xref="HGNC:HGNC:1369"
                     /db_xref="MIM:604642"
ORIGIN      
        1 meivwevlfl lqanfivcis aqqnspkihe gwwaykevvq gsfvpvpsfw glvnsawnlc
       61 svgkrqspvn ietshmifdp fltplrintg grkvsgtmyn tgrhvslrld kehlvnisgg
      121 pmtyshrlee irlhfgseds qgsehllngq afsgevqlih ynhelytnvt eaakspnglv
      181 vvsifikvsd ssnpflnrml nrdtitrity kndayllqgl nieelypets sfitydgsmt
      241 ippcyetasw iimnkpvyit rmqmhslrll sqnqpsqifl smsdnfrpvq plnnrcirtn
      301 infslqgkdc pnnraqklqy rvnewllk
//
LOCUS       NP_001076002             328 aa            linear   PRI 14-JAN-2026
DEFINITION  carbonic anhydrase-related protein 10 precursor [Homo sapiens].
ACCESSION   NP_001076002
VERSION     NP_001076002.1
DBSOURCE    REFSEQ: accession NM_001082533.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Li,Q., Zhang,L., Zhang,Z., Fan,Y. and Zhang,Q.
  TITLE     Carbonic anhydrase 10 functions as a tumor suppressor in renal cell
            carcinoma and its methylation is a risk factor for survival outcome
  JOURNAL   Urol Oncol 40 (4), 168 (2022)
   PUBMED   34980544
  REMARK    GeneRIF: Carbonic anhydrase 10 functions as a tumor suppressor in
            renal cell carcinoma and its methylation is a risk factor for
            survival outcome.
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Kreuzer,M., Banerjee,A., Birts,C.N., Darley,M., Tavassoli,A.,
            Ivan,M. and Blaydes,J.P.
  TITLE     Glycolysis, via NADH-dependent dimerisation of CtBPs, regulates
            hypoxia-induced expression of CAIX and stem-like breast cancer cell
            survival
  JOURNAL   FEBS Lett 594 (18), 2988-3001 (2020)
   PUBMED   32618367
  REMARK    GeneRIF: Glycolysis, via NADH-dependent dimerisation of CtBPs,
            regulates hypoxia-induced expression of CAIX and stem-like breast
            cancer cell survival.
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Ge,A., Gao,S., Liu,Y., Zhang,H., Wang,X., Zhang,L., Pang,D. and
            Zhao,Y.
  TITLE     Methylation of WT1, CA10 in peripheral blood leukocyte is
            associated with breast cancer risk: a case-control study
  JOURNAL   BMC Cancer 20 (1), 713 (2020)
   PUBMED   32736539
  REMARK    GeneRIF: Methylation of WT1, CA10 in peripheral blood leukocyte is
            associated with breast cancer risk: a case-control study.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Aspatwar,A., Tolvanen,M.E.E., Schneider,H.P., Becker,H.M.,
            Narkilahti,S., Parkkila,S. and Deitmer,J.W.
  TITLE     Catalytically inactive carbonic anhydrase-related proteins enhance
            transport of lactate by MCT1
  JOURNAL   FEBS Open Bio 9 (7), 1204-1211 (2019)
   PUBMED   31033227
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Tao,B., Ling,Y., Zhang,Y., Li,S., Zhou,P., Wang,X., Li,B., Jun,Z.,
            Zhang,W., Xu,C., Shi,J., Wang,L., Zhang,W. and Li,S.
  TITLE     CA10 and CA11 negatively regulate neuronal activity-dependent
            growth of gliomas
  JOURNAL   Mol Oncol 13 (5), 1018-1032 (2019)
   PUBMED   30636076
  REMARK    GeneRIF: results suggest that CA11 and CA10 negatively regulate
            neuronal activity-dependent glioma growth and inhibit glioma
            aggression. Thus, CA11/CA10 may represent a potential therapeutic
            target for the treatment of gliomas.
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Supuran,C.T., Scozzafava,A. and Casini,A.
  TITLE     Carbonic anhydrase inhibitors
  JOURNAL   Med Res Rev 23 (2), 146-189 (2003)
   PUBMED   12500287
  REMARK    Review article
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Taniuchi,K., Nishimori,I., Takeuchi,T., Fujikawa-Adachi,K.,
            Ohtsuki,Y. and Onishi,S.
  TITLE     Developmental expression of carbonic anhydrase-related proteins
            VIII, X, and XI in the human brain
  JOURNAL   Neuroscience 112 (1), 93-99 (2002)
   PUBMED   12044474
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Okamoto,N., Fujikawa-Adachi,K., Nishimori,I., Taniuchi,K. and
            Onishi,S.
  TITLE     cDNA sequence of human carbonic anhydrase-related protein, CA-RP X:
            mRNA expressions of CA-RP X and XI in human brain
  JOURNAL   Biochim Biophys Acta 1518 (3), 311-316 (2001)
   PUBMED   11311946
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Kleiderlein,J.J., Nisson,P.E., Jessee,J., Li,W.B., Becker,K.G.,
            Derby,M.L., Ross,C.A. and Margolis,R.L.
  TITLE     CCG repeats in cDNAs from human brain
  JOURNAL   Hum Genet 103 (6), 666-673 (1998)
   PUBMED   9921901
  REMARK    GeneRIF: Identifies a string of seven CCG repeats in the 5' UTR of
            a carbonic anhydrase X cDNA from human brain.
            Erratum:[Hum Genet 1999 Jan;104(1):113]
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Hewett-Emmett,D. and Tashian,R.E.
  TITLE     Functional diversity, conservation, and convergence in the
            evolution of the alpha-, beta-, and gamma-carbonic anhydrase gene
            families
  JOURNAL   Mol Phylogenet Evol 5 (1), 50-77 (1996)
   PUBMED   8673298
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA110822.1, BC047456.1,
            AW135066.1 and AC005883.14.
            
            Summary: This gene encodes a protein that belongs to the carbonic
            anhydrase family of zinc metalloenzymes, which catalyze the
            reversible hydration of carbon dioxide in various biological
            processes. The protein encoded by this gene is an acatalytic member
            of the alpha-carbonic anhydrase subgroup, and it is thought to play
            a role in the central nervous system, especially in brain
            development. Multiple transcript variants encoding the same protein
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.167830.1,
                                           SRR1660805.69880.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.33-q22"
     Protein         1..328
                     /product="carbonic anhydrase-related protein 10 precursor"
                     /note="carbonic anhydrase-related protein 10; carbonic
                     anhydrase-related protein X; cerebral protein-15; CARP X;
                     CA-RP X; carbonic anhydrase X; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=35142
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2439
     Region          46..302
                     /region_name="alpha_CARP_X_XI_like"
                     /note="Carbonic anhydrase alpha related protein: groups X,
                     XI and related proteins. This subgroup contains carbonic
                     anhydrase related proteins (CARPs) X and XI, which have
                     been implicated in various biological processes of the
                     central nervous system. CARPs are...; cd03121"
                     /db_xref="CDD:239395"
     CDS             1..328
                     /gene="CA10"
                     /gene_synonym="CA-RPX; CARPX; HUCEP-15"
                     /coded_by="NM_001082533.1:1113..2099"
                     /db_xref="CCDS:CCDS32684.1"
                     /db_xref="GeneID:56934"
                     /db_xref="HGNC:HGNC:1369"
                     /db_xref="MIM:604642"
ORIGIN      
        1 meivwevlfl lqanfivcis aqqnspkihe gwwaykevvq gsfvpvpsfw glvnsawnlc
       61 svgkrqspvn ietshmifdp fltplrintg grkvsgtmyn tgrhvslrld kehlvnisgg
      121 pmtyshrlee irlhfgseds qgsehllngq afsgevqlih ynhelytnvt eaakspnglv
      181 vvsifikvsd ssnpflnrml nrdtitrity kndayllqgl nieelypets sfitydgsmt
      241 ippcyetasw iimnkpvyit rmqmhslrll sqnqpsqifl smsdnfrpvq plnnrcirtn
      301 infslqgkdc pnnraqklqy rvnewllk
//
LOCUS       NP_001208                328 aa            linear   PRI 14-JAN-2026
DEFINITION  carbonic anhydrase-related protein 11 precursor [Homo sapiens].
ACCESSION   NP_001208
VERSION     NP_001208.2
DBSOURCE    REFSEQ: accession NM_001217.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Aspatwar,A., Tolvanen,M.E.E., Schneider,H.P., Becker,H.M.,
            Narkilahti,S., Parkkila,S. and Deitmer,J.W.
  TITLE     Catalytically inactive carbonic anhydrase-related proteins enhance
            transport of lactate by MCT1
  JOURNAL   FEBS Open Bio 9 (7), 1204-1211 (2019)
   PUBMED   31033227
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Tao,B., Ling,Y., Zhang,Y., Li,S., Zhou,P., Wang,X., Li,B., Jun,Z.,
            Zhang,W., Xu,C., Shi,J., Wang,L., Zhang,W. and Li,S.
  TITLE     CA10 and CA11 negatively regulate neuronal activity-dependent
            growth of gliomas
  JOURNAL   Mol Oncol 13 (5), 1018-1032 (2019)
   PUBMED   30636076
  REMARK    GeneRIF: results suggest that CA11 and CA10 negatively regulate
            neuronal activity-dependent glioma growth and inhibit glioma
            aggression. Thus, CA11/CA10 may represent a potential therapeutic
            target for the treatment of gliomas.
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Karjalainen,S.L., Haapasalo,H.K., Aspatwar,A., Barker,H.,
            Parkkila,S. and Haapasalo,J.A.
  TITLE     Carbonic anhydrase related protein expression in astrocytomas and
            oligodendroglial tumors
  JOURNAL   BMC Cancer 18 (1), 584 (2018)
   PUBMED   29792187
  REMARK    GeneRIF: The CARP VIII and XI proteins were associated to
            non-hypoxic conditions and CARP XI also to the expression of
            cytoplasmic CA II staining suggesting that the CARPs play a role in
            tumorigenesis of diffusively infiltrating gliomas
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Liang,Y., Tang,W., Huang,T., Gao,Y., Tan,A., Yang,X., Zhang,H.,
            Hu,Y., Qin,X., Li,S., Zhang,S., Mo,L., Liang,Z., Shi,D., Huang,Z.,
            Guan,Y., Zhou,J., Winkler,C., O'Brien,S.J., Xu,J., Mo,Z. and
            Peng,T.
  TITLE     Genetic variations affecting serum carcinoembryonic antigen levels
            and status of regional lymph nodes in patients with sporadic
            colorectal cancer from Southern China
  JOURNAL   PLoS One 9 (6), e97923 (2014)
   PUBMED   24941225
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 328)
  AUTHORS   He,M., Wu,C., Xu,J., Guo,H., Yang,H., Zhang,X., Sun,J., Yu,D.,
            Zhou,L., Peng,T., He,Y., Gao,Y., Yuan,J., Deng,Q., Dai,X., Tan,A.,
            Feng,Y., Zhang,H., Min,X., Yang,X., Zhu,J., Zhai,K., Chang,J.,
            Qin,X., Tan,W., Hu,Y., Lang,M., Tao,S., Li,Y., Li,Y., Feng,J.,
            Li,D., Kim,S.T., Zhang,S., Zhang,H., Zheng,S.L., Gui,L., Wang,Y.,
            Wei,S., Wang,F., Fang,W., Liang,Y., Zhai,Y., Chen,W., Miao,X.,
            Zhou,G., Hu,F.B., Lin,D., Mo,Z. and Wu,T.
  TITLE     A genome wide association study of genetic loci that influence
            tumour biomarkers cancer antigen 19-9, carcinoembryonic antigen and
            alpha fetoprotein and their associations with cancer risk
  JOURNAL   Gut 63 (1), 143-151 (2014)
   PUBMED   23300138
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Taniuchi,K., Nishimori,I., Takeuchi,T., Fujikawa-Adachi,K.,
            Ohtsuki,Y. and Onishi,S.
  TITLE     Developmental expression of carbonic anhydrase-related proteins
            VIII, X, and XI in the human brain
  JOURNAL   Neuroscience 112 (1), 93-99 (2002)
   PUBMED   12044474
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Okamoto,N., Fujikawa-Adachi,K., Nishimori,I., Taniuchi,K. and
            Onishi,S.
  TITLE     cDNA sequence of human carbonic anhydrase-related protein, CA-RP X:
            mRNA expressions of CA-RP X and XI in human brain
  JOURNAL   Biochim Biophys Acta 1518 (3), 311-316 (2001)
   PUBMED   11311946
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Fujikawa-Adachi,K., Nishimori,I., Taguchi,T., Yuri,K. and Onishi,S.
  TITLE     cDNA sequence, mRNA expression, and chromosomal localization of
            human carbonic anhydrase-related protein, CA-RP XI
  JOURNAL   Biochim Biophys Acta 1431 (2), 518-524 (1999)
   PUBMED   10350627
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Bellingham,J., Gregory-Evans,K. and Gregory-Evans,C.Y.
  TITLE     Sequence and tissue expression of a novel human carbonic
            anhydrase-related protein, CARP-2, mapping to chromosome 19q13.3
  JOURNAL   Biochem Biophys Res Commun 253 (2), 364-367 (1998)
   PUBMED   9878543
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Lovejoy,D.A., Hewett-Emmett,D., Porter,C.A., Cepoi,D.,
            Sheffield,A., Vale,W.W. and Tashian,R.E.
  TITLE     Evolutionarily conserved, 'acatalytic' carbonic anhydrase-related
            protein XI contains a sequence motif present in the neuropeptide
            sauvagine: the human CA-RP XI gene (CA11) is embedded between the
            secretor gene cluster and the DBP gene at 19q13.3
  JOURNAL   Genomics 54 (3), 484-493 (1998)
   PUBMED   9878252
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008888.7, AY358967.2,
            DR978420.1 and AI568635.1.
            
            On Aug 30, 2000 this sequence version replaced NP_001208.1.
            
            Summary:  Carbonic anhydrases (CAs) are a large family of zinc
            metalloenzymes that catalyze the reversible hydration of carbon
            dioxide.  They participate in a variety of biological processes,
            including respiration, calcification, acid-base balance, bone
            resorption, and the formation of aqueous humor, cerebrospinal
            fluid, saliva, and gastric acid.  They show extensive diversity in
            tissue distribution and in their subcellular localization.  CA XI
            is likely a secreted protein, however, radical changes at active
            site residues completely conserved in CA isozymes with catalytic
            activity, make it unlikely that it has carbonic anhydrase activity.
            It shares properties in common with two other acatalytic CA
            isoforms, CA VIII and CA X.  CA XI is most abundantly expressed in
            brain, and may play a general role in the central nervous system.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.681089.1,
                                           SRR3476690.1112426.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000084798.9/ ENSP00000084798.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..328
                     /product="carbonic anhydrase-related protein 11 precursor"
                     /note="carbonic anhydrase-related protein XI; carbonic
                     anhydrase-related protein 2; carbonic anhydrase-related
                     protein 11; carbonic anhydrase XI"
                     /calculated_mol_wt=34048
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2209
     mat_peptide     24..328
                     /product="Carbonic anhydrase-related protein 11.
                     /id=PRO_0000004245"
                     /note="propagated from UniProtKB/Swiss-Prot (O75493.2)"
                     /calculated_mol_wt=34048
     Region          48..304
                     /region_name="alpha_CARP_X_XI_like"
                     /note="Carbonic anhydrase alpha related protein: groups X,
                     XI and related proteins. This subgroup contains carbonic
                     anhydrase related proteins (CARPs) X and XI, which have
                     been implicated in various biological processes of the
                     central nervous system. CARPs are...; cd03121"
                     /db_xref="CDD:239395"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (O75493.2)"
     Site            170
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75493.2)"
     Site            260
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75493.2)"
     Region          299..328
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75493.2)"
     CDS             1..328
                     /gene="CA11"
                     /gene_synonym="CA-RP; CA-RP II; CA-XI; CARP-2; CARPX1"
                     /coded_by="NM_001217.5:556..1542"
                     /db_xref="CCDS:CCDS12729.1"
                     /db_xref="GeneID:770"
                     /db_xref="HGNC:HGNC:1370"
                     /db_xref="MIM:604644"
ORIGIN      
        1 mgaaarlsap ralvlwaalg aaahigpapd pedwwsykdn lqgnfvpgpp fwglvnaaws
       61 lcavgkrqsp vdvelkrvly dpflpplrls tggeklrgtl yntgrhvsfl paprpvvnvs
      121 ggpllyshrl selrllfgar dgagsehqin hqgfsaevql ihfnqelygn fsaasrgpng
      181 lailslfvnv astsnpflsr llnrdtitri sykndayflq dlslellfpe sfgfityqgs
      241 lstppcsetv twilidraln itslqmhslr llsqnppsqi fqslsgnsrp lqplahralr
      301 gnrdprhper rcrgpnyrlh vdgvphgr
//
LOCUS       NP_001338460             609 aa            linear   PRI 14-JAN-2026
DEFINITION  protein CFAP20DC isoform 2 [Homo sapiens].
ACCESSION   NP_001338460 XP_016861338
VERSION     NP_001338460.1
DBSOURCE    REFSEQ: accession NM_001351531.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Alkhadidi,F., AlSharif,H., AlQthami,A., Alkhaldi,S.H.,
            Alsuwat,S.A., Abosabie,S.A., Abosabie,S.A. and Kamal,N.M.
  TITLE     Novel homozygous C3orf67 gene variant associated with primary
            ciliary dyskinesia in a Saudi pediatric patient: A case report
  JOURNAL   World J Exp Med 15 (4), 108404 (2025)
   PUBMED   41497680
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Alghamdi,A.O., AlKhadidi,F.J., Alawur,A.H., Alkhaldi,S., Habib,L.,
            Alharbe,R., Algethami,A.S., Aljaed,N.M., Abosabie,S.A.,
            Abosabie,S.A. and Kamal,N.M.
  TITLE     Beyond bacteria and breaking the norm: Pulmonary mucormycosis due
            to Absidia corymbifera in a child with primary ciliary dyskinesia
  JOURNAL   J Int Med Res 53 (11), 3000605251381480 (2025)
   PUBMED   41224705
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104300.2, AC104303.2 and AC119424.2.
            
            On May 12, 2017 this sequence version replaced XP_016861338.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1002251.1,
                                           SRR14038195.1451641.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.2"
     Protein         1..609
                     /product="protein CFAP20DC isoform 2"
                     /note="uncharacterized protein C3orf67; protein CFAP20DC"
                     /calculated_mol_wt=67219
     CDS             1..609
                     /gene="CFAP20DC"
                     /gene_synonym="C3orf67"
                     /coded_by="NM_001351531.2:853..2682"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:200844"
                     /db_xref="HGNC:HGNC:24763"
ORIGIN      
        1 mtdvphvtql lnmtklrqte ikfgghplrs aesdqfinrg tsitrnsknq dvchiafgsk
       61 vlgppplsgr rnnmkisset vrsvgsknnr scqpstvekc vngtemsall ipeseeqgnk
      121 enihqikqtv pihaanlhim hphppqepsa dknnnrrrlr lkstsrerte tpsgsssgnn
      181 riedkastil ttvsqqgael lnsgtlgpqs pdqsdewifp enadhisyla ssrqslllgd
      241 dscnpshlwl easkesehdq qaeesqsvpk diftfssrpr saphgktqtm speelsfild
      301 lkednsvtsr dtqseddfyg gdsseegnhs iqgsrgpttg pseltqltle sllgkaakrt
      361 skeylrsayt eagatesqds smeqidrnnf emsllpttcl sptgrrcgsc qktpepvika
      421 kdlsaqqvpa slnktslkei sgerlssipe aseydwrnyq psqmseselq mlaslrwqqn
      481 eeledagtsh glsasqvdnc nvsistssdd tttwnsclpp pvnqgrhyqk emnppspsnp
      541 rdwlnmlspp ivppsqqpae qrpdscesls vqgeedlsve edeevltlly dpclncyfdp
      601 qtgkyyelv
//
LOCUS       NP_001338463             199 aa            linear   PRI 14-JAN-2026
DEFINITION  protein CFAP20DC isoform 6 [Homo sapiens].
ACCESSION   NP_001338463
VERSION     NP_001338463.1
DBSOURCE    REFSEQ: accession NM_001351534.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Alkhadidi,F., AlSharif,H., AlQthami,A., Alkhaldi,S.H.,
            Alsuwat,S.A., Abosabie,S.A., Abosabie,S.A. and Kamal,N.M.
  TITLE     Novel homozygous C3orf67 gene variant associated with primary
            ciliary dyskinesia in a Saudi pediatric patient: A case report
  JOURNAL   World J Exp Med 15 (4), 108404 (2025)
   PUBMED   41497680
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Alghamdi,A.O., AlKhadidi,F.J., Alawur,A.H., Alkhaldi,S., Habib,L.,
            Alharbe,R., Algethami,A.S., Aljaed,N.M., Abosabie,S.A.,
            Abosabie,S.A. and Kamal,N.M.
  TITLE     Beyond bacteria and breaking the norm: Pulmonary mucormycosis due
            to Absidia corymbifera in a child with primary ciliary dyskinesia
  JOURNAL   J Int Med Res 53 (11), 3000605251381480 (2025)
   PUBMED   41224705
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104300.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1901529.1,
                                           SRR14372080.889427.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2150385, SAMEA2158188
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.2"
     Protein         1..199
                     /product="protein CFAP20DC isoform 6"
                     /note="uncharacterized protein C3orf67; protein CFAP20DC"
                     /calculated_mol_wt=22596
     Region          1..188
                     /region_name="CFA20_dom"
                     /note="CFA20 domain; pfam05018"
                     /db_xref="CDD:461521"
     CDS             1..199
                     /gene="CFAP20DC"
                     /gene_synonym="C3orf67"
                     /coded_by="NM_001351534.2:395..994"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:200844"
                     /db_xref="HGNC:HGNC:24763"
ORIGIN      
        1 mfkneyqgga fveifsaqgk npgakwkilg spsviwkefd kevksfvfvl egssqtnkiq
       61 lpkenkqslg liqrflvlqi yvplgqdfst ellitdlgni krrlylstvh kelsstplha
      121 kiplfmikrk iwcnlcidlv aftseifkga vfqsldgivv sancklrkif tlkskpqdta
      181 dkdgmfrlls rffnslmyf
//
LOCUS       NP_001338461             433 aa            linear   PRI 14-JAN-2026
DEFINITION  protein CFAP20DC isoform 4 [Homo sapiens].
ACCESSION   NP_001338461
VERSION     NP_001338461.1
DBSOURCE    REFSEQ: accession NM_001351532.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Alkhadidi,F., AlSharif,H., AlQthami,A., Alkhaldi,S.H.,
            Alsuwat,S.A., Abosabie,S.A., Abosabie,S.A. and Kamal,N.M.
  TITLE     Novel homozygous C3orf67 gene variant associated with primary
            ciliary dyskinesia in a Saudi pediatric patient: A case report
  JOURNAL   World J Exp Med 15 (4), 108404 (2025)
   PUBMED   41497680
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Alghamdi,A.O., AlKhadidi,F.J., Alawur,A.H., Alkhaldi,S., Habib,L.,
            Alharbe,R., Algethami,A.S., Aljaed,N.M., Abosabie,S.A.,
            Abosabie,S.A. and Kamal,N.M.
  TITLE     Beyond bacteria and breaking the norm: Pulmonary mucormycosis due
            to Absidia corymbifera in a child with primary ciliary dyskinesia
  JOURNAL   J Int Med Res 53 (11), 3000605251381480 (2025)
   PUBMED   41224705
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104300.2, AC104303.2 and AC119424.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC050317.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2148874
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.2"
     Protein         1..433
                     /product="protein CFAP20DC isoform 4"
                     /note="uncharacterized protein C3orf67; protein CFAP20DC"
                     /calculated_mol_wt=47398
     CDS             1..433
                     /gene="CFAP20DC"
                     /gene_synonym="C3orf67"
                     /coded_by="NM_001351532.2:1346..2647"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:200844"
                     /db_xref="HGNC:HGNC:24763"
ORIGIN      
        1 msallipese eqgnkenihq ikqtvpihaa nlhimhphpp qepsadknnn rrrlrlksts
       61 rertetpsgs ssgnnriedk astilttvsq qgaellnsgt lgpqspdqsd ewifpenadh
      121 isylassrqs lllgddscnp shlwleaske sehdqqaees qsvpkdiftf ssrprsaphg
      181 ktqtmspeel sfildlkedn svtsrdtqse ddfyggdsse egnhsiqgsr gpttgpselt
      241 qltlesllgk aakrtskeyl rsayteagat esqdssmeqi drnnfemsll pttclsptgr
      301 rcgscqktpe pvikakdlsa qqvpaslnkt slkeisgerl ssipeaseyd wrnyqpsqms
      361 eselqmlasl rwqqneeled agtshglsas qvdncnvsis tssddtttwn sclppglvky
      421 veptnrssqs tag
//
LOCUS       NP_001380992             814 aa            linear   PRI 14-JAN-2026
DEFINITION  protein CFAP20DC isoform 7 [Homo sapiens].
ACCESSION   NP_001380992 XP_006713076
VERSION     NP_001380992.1
DBSOURCE    REFSEQ: accession NM_001394063.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 814)
  AUTHORS   Alkhadidi,F., AlSharif,H., AlQthami,A., Alkhaldi,S.H.,
            Alsuwat,S.A., Abosabie,S.A., Abosabie,S.A. and Kamal,N.M.
  TITLE     Novel homozygous C3orf67 gene variant associated with primary
            ciliary dyskinesia in a Saudi pediatric patient: A case report
  JOURNAL   World J Exp Med 15 (4), 108404 (2025)
   PUBMED   41497680
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 814)
  AUTHORS   Alghamdi,A.O., AlKhadidi,F.J., Alawur,A.H., Alkhaldi,S., Habib,L.,
            Alharbe,R., Algethami,A.S., Aljaed,N.M., Abosabie,S.A.,
            Abosabie,S.A. and Kamal,N.M.
  TITLE     Beyond bacteria and breaking the norm: Pulmonary mucormycosis due
            to Absidia corymbifera in a child with primary ciliary dyskinesia
  JOURNAL   J Int Med Res 53 (11), 3000605251381480 (2025)
   PUBMED   41224705
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104300.2, AC104303.2 and AC119424.2.
            
            On Mar 30, 2021 this sequence version replaced XP_006713076.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.4943.1,
                                           SRR14038195.111394.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000482387.7/ ENSP00000417122.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..814
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.2"
     Protein         1..814
                     /product="protein CFAP20DC isoform 7"
                     /note="uncharacterized protein C3orf67; protein CFAP20DC"
                     /calculated_mol_wt=90307
     Region          1..183
                     /region_name="CFA20_dom"
                     /note="CFA20 domain; pfam05018"
                     /db_xref="CDD:461521"
     CDS             1..814
                     /gene="CFAP20DC"
                     /gene_synonym="C3orf67"
                     /coded_by="NM_001394063.1:395..2839"
                     /note="isoform 7 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS93302.1"
                     /db_xref="GeneID:200844"
                     /db_xref="HGNC:HGNC:24763"
ORIGIN      
        1 mfkneyqgga fveifsaqgk npgakwkilg spsviwkefd kevksfvfvl egssqtnkiq
       61 lpkenkqslg liqrflvlqi yvplgqdfst ellitdlgni krrlylstvh kelsstplha
      121 kiplfmikrk iwcnlcidlv aftseifkga vfqsldgivv sancklrkif tlkskpqdta
      181 dkdavygvpf stdeptdiip rscqlmtdvp hvtqllnmtk lrqteikfgg hplrsaesdq
      241 finrgtsitr nsknqdvchi afgskvlgpp plsgrrnnmk issetvrsvg sknnrscqps
      301 tvekcvngte msallipese eqgnkenihq ikqtvpihaa nlhimhphpp qepsadknnn
      361 rrrlrlksts rertetpsgs ssgnnriedk astilttvsq qgaellnsgt lgpqspdqsd
      421 ewifpenadh isylassrqs lllgddscnp shlwleaske sehdqqaees qsvpkdiftf
      481 ssrprsaphg ktqtmspeel sfildlkedn svtsrdtqse ddfyggdsse egnhsiqgsr
      541 gpttgpselt qltlesllgk aakrtskeyl rsayteagat esqdssmeqi drnnfemsll
      601 pttclsptgr rcgscqktpe pvikakdlsa qqvpaslnkt slkeisgerl ssipeaseyd
      661 wrnyqpsqms eselqmlasl rwqqneeled agtshglsas qvdncnvsis tssddtttwn
      721 sclpppvnqg rhyqkemnpp spsnprdwln mlsppivpps qqpaeqrpds ceslsvqgee
      781 dlsveedeev ltllydpcln cyfdpqtgky yelv
//
LOCUS       NP_001338459             759 aa            linear   PRI 14-JAN-2026
DEFINITION  protein CFAP20DC isoform 1 [Homo sapiens].
ACCESSION   NP_001338459 XP_011531753
VERSION     NP_001338459.1
DBSOURCE    REFSEQ: accession NM_001351530.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Alkhadidi,F., AlSharif,H., AlQthami,A., Alkhaldi,S.H.,
            Alsuwat,S.A., Abosabie,S.A., Abosabie,S.A. and Kamal,N.M.
  TITLE     Novel homozygous C3orf67 gene variant associated with primary
            ciliary dyskinesia in a Saudi pediatric patient: A case report
  JOURNAL   World J Exp Med 15 (4), 108404 (2025)
   PUBMED   41497680
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Alghamdi,A.O., AlKhadidi,F.J., Alawur,A.H., Alkhaldi,S., Habib,L.,
            Alharbe,R., Algethami,A.S., Aljaed,N.M., Abosabie,S.A.,
            Abosabie,S.A. and Kamal,N.M.
  TITLE     Beyond bacteria and breaking the norm: Pulmonary mucormycosis due
            to Absidia corymbifera in a child with primary ciliary dyskinesia
  JOURNAL   J Int Med Res 53 (11), 3000605251381480 (2025)
   PUBMED   41224705
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104300.2, AC104303.2 and AC119424.2.
            
            On May 12, 2017 this sequence version replaced XP_011531753.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3740906.1,
                                           SRR14038194.1760028.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.2"
     Protein         1..759
                     /product="protein CFAP20DC isoform 1"
                     /note="uncharacterized protein C3orf67; protein CFAP20DC"
                     /calculated_mol_wt=84198
     Region          1..183
                     /region_name="CFA20_dom"
                     /note="CFA20 domain; pfam05018"
                     /db_xref="CDD:461521"
     CDS             1..759
                     /gene="CFAP20DC"
                     /gene_synonym="C3orf67"
                     /coded_by="NM_001351530.2:395..2674"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:200844"
                     /db_xref="HGNC:HGNC:24763"
ORIGIN      
        1 mfkneyqgga fveifsaqgk npgakwkilg spsviwkefd kevksfvfvl egssqtnkiq
       61 lpkenkqslg liqrflvlqi yvplgqdfst ellitdlgni krrlylstvh kelsstplha
      121 kiplfmikrk iwcnlcidlv aftseifkga vfqsldgivv sancklrkif tlkskpqdta
      181 dkddqfinrg tsitrnsknq dvchiafgsk vlgppplsgr rnnmkisset vrsvgsknnr
      241 scqpstvekc vngtemsall ipeseeqgnk enihqikqtv pihaanlhim hphppqepsa
      301 dknnnrrrlr lkstsrerte tpsgsssgnn riedkastil ttvsqqgael lnsgtlgpqs
      361 pdqsdewifp enadhisyla ssrqslllgd dscnpshlwl easkesehdq qaeesqsvpk
      421 diftfssrpr saphgktqtm speelsfild lkednsvtsr dtqseddfyg gdsseegnhs
      481 iqgsrgpttg pseltqltle sllgkaakrt skeylrsayt eagatesqds smeqidrnnf
      541 emsllpttcl sptgrrcgsc qktpepvika kdlsaqqvpa slnktslkei sgerlssipe
      601 aseydwrnyq psqmseselq mlaslrwqqn eeledagtsh glsasqvdnc nvsistssdd
      661 tttwnsclpp pvnqgrhyqk emnppspsnp rdwlnmlspp ivppsqqpae qrpdscesls
      721 vqgeedlsve edeevltlly dpclncyfdp qtgkyyelv
//
LOCUS       NP_940865                563 aa            linear   PRI 14-JAN-2026
DEFINITION  protein CFAP20DC isoform 3 [Homo sapiens].
ACCESSION   NP_940865 XP_114306
VERSION     NP_940865.1
DBSOURCE    REFSEQ: accession NM_198463.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Alkhadidi,F., AlSharif,H., AlQthami,A., Alkhaldi,S.H.,
            Alsuwat,S.A., Abosabie,S.A., Abosabie,S.A. and Kamal,N.M.
  TITLE     Novel homozygous C3orf67 gene variant associated with primary
            ciliary dyskinesia in a Saudi pediatric patient: A case report
  JOURNAL   World J Exp Med 15 (4), 108404 (2025)
   PUBMED   41497680
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Alghamdi,A.O., AlKhadidi,F.J., Alawur,A.H., Alkhaldi,S., Habib,L.,
            Alharbe,R., Algethami,A.S., Aljaed,N.M., Abosabie,S.A.,
            Abosabie,S.A. and Kamal,N.M.
  TITLE     Beyond bacteria and breaking the norm: Pulmonary mucormycosis due
            to Absidia corymbifera in a child with primary ciliary dyskinesia
  JOURNAL   J Int Med Res 53 (11), 3000605251381480 (2025)
   PUBMED   41224705
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC050317.1, AK124111.1 and AA521262.1.
            
            On Dec 17, 2003 this sequence version replaced XP_114306.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK124111.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.2"
     Protein         1..563
                     /product="protein CFAP20DC isoform 3"
                     /note="uncharacterized protein C3orf67; protein CFAP20DC"
                     /calculated_mol_wt=62688
     Region          <7..58
                     /region_name="CFA20_dom"
                     /note="CFA20 domain; pfam05018"
                     /db_xref="CDD:461521"
     Region          241..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZVT6.2)"
     CDS             1..563
                     /gene="CFAP20DC"
                     /gene_synonym="C3orf67"
                     /coded_by="NM_198463.4:446..2137"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS33776.1"
                     /db_xref="GeneID:200844"
                     /db_xref="HGNC:HGNC:24763"
ORIGIN      
        1 mikrkiwcnl cidlvaftse ifkgavfqsl dgivvsanck lrkiftlksk pqdtadkdav
       61 ygvpfstdep tdiiprscql mtdvphvtql lnmtklrqte ikfgghplrs aesdqfinrg
      121 tsitrnsknq dvchiafgsk vlgppplsgr rnnmkisset vrsvgsknnr scqpstvekc
      181 vngtemsall ipeseeqgnk enihqikqtv pihaanlhim hphppqepsa dknnnrrrlr
      241 lkstsrerte tpsgsssgnn riedkastil ttvsqqgael lnsgtlgpqs pdqsdewifp
      301 enadhisyla ssrqslllgd dscnpshlwl easkesehdq qaeesqsvpk diftfssrpr
      361 saphgktqtm speelsfild lkednsvtsr dtqseddfyg gdsseeeydw rnyqpsqmse
      421 selqmlaslr wqqneeleda gtshglsasq vdncnvsist ssddtttwns clpppvnqgr
      481 hyqkemnpps psnprdwlnm lsppivppsq qpaeqrpdsc eslsvqgeed lsveedeevl
      541 tllydpclnc yfdpqtgkyy elv
//
LOCUS       NP_001338462             244 aa            linear   PRI 14-JAN-2026
DEFINITION  protein CFAP20DC isoform 5 [Homo sapiens].
ACCESSION   NP_001338462
VERSION     NP_001338462.1
DBSOURCE    REFSEQ: accession NM_001351533.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Alkhadidi,F., AlSharif,H., AlQthami,A., Alkhaldi,S.H.,
            Alsuwat,S.A., Abosabie,S.A., Abosabie,S.A. and Kamal,N.M.
  TITLE     Novel homozygous C3orf67 gene variant associated with primary
            ciliary dyskinesia in a Saudi pediatric patient: A case report
  JOURNAL   World J Exp Med 15 (4), 108404 (2025)
   PUBMED   41497680
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Alghamdi,A.O., AlKhadidi,F.J., Alawur,A.H., Alkhaldi,S., Habib,L.,
            Alharbe,R., Algethami,A.S., Aljaed,N.M., Abosabie,S.A.,
            Abosabie,S.A. and Kamal,N.M.
  TITLE     Beyond bacteria and breaking the norm: Pulmonary mucormycosis due
            to Absidia corymbifera in a child with primary ciliary dyskinesia
  JOURNAL   J Int Med Res 53 (11), 3000605251381480 (2025)
   PUBMED   41224705
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104300.2 and AC104303.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.166311.1,
                                           SRR14038192.792196.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158188 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p14.2"
     Protein         1..244
                     /product="protein CFAP20DC isoform 5"
                     /note="uncharacterized protein C3orf67; protein CFAP20DC"
                     /calculated_mol_wt=27289
     Region          1..183
                     /region_name="CFA20_dom"
                     /note="CFA20 domain; pfam05018"
                     /db_xref="CDD:461521"
     CDS             1..244
                     /gene="CFAP20DC"
                     /gene_synonym="C3orf67"
                     /coded_by="NM_001351533.2:395..1129"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:200844"
                     /db_xref="HGNC:HGNC:24763"
ORIGIN      
        1 mfkneyqgga fveifsaqgk npgakwkilg spsviwkefd kevksfvfvl egssqtnkiq
       61 lpkenkqslg liqrflvlqi yvplgqdfst ellitdlgni krrlylstvh kelsstplha
      121 kiplfmikrk iwcnlcidlv aftseifkga vfqsldgivv sancklrkif tlkskpqdta
      181 dkdavygvpf stdeptdiip rscqlmtdvp hvtqllnmtk lrqteikfgg hplrsaesgr
      241 hsgt
//
LOCUS       NP_001003693             297 aa            linear   PRI 15-JAN-2026
DEFINITION  lymphocyte antigen 6 complex locus protein G6f isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_001003693
VERSION     NP_001003693.1
DBSOURCE    REFSEQ: accession NM_001003693.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Ucisik-Akkaya,E., Davis,C.F., Do,T.N., Morrison,B.A., Stemmer,S.M.,
            Amadio,W.J. and Dorak,M.T.
  TITLE     Examination of genetic polymorphisms in newborns for signatures of
            sex-specific prenatal selection
  JOURNAL   Mol Hum Reprod 16 (10), 770-777 (2010)
   PUBMED   20587610
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Barcellos,L.F., May,S.L., Ramsay,P.P., Quach,H.L., Lane,J.A.,
            Nititham,J., Noble,J.A., Taylor,K.E., Quach,D.L., Chung,S.A.,
            Kelly,J.A., Moser,K.L., Behrens,T.W., Seldin,M.F., Thomson,G.,
            Harley,J.B., Gaffney,P.M. and Criswell,L.A.
  TITLE     High-density SNP screening of the major histocompatibility complex
            in systemic lupus erythematosus demonstrates strong evidence for
            independent susceptibility regions
  JOURNAL   PLoS Genet 5 (10), e1000696 (2009)
   PUBMED   19851445
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Macaulay,I.C., Tijssen,M.R., Thijssen-Timmer,D.C., Gusnanto,A.,
            Steward,M., Burns,P., Langford,C.F., Ellis,P.D., Dudbridge,F.,
            Zwaginga,J.J., Watkins,N.A., van der Schoot,C.E. and Ouwehand,W.H.
  TITLE     Comparative gene expression profiling of in vitro differentiated
            megakaryocytes and erythroblasts identifies novel activatory and
            inhibitory platelet membrane proteins
  JOURNAL   Blood 109 (8), 3260-3269 (2007)
   PUBMED   17192395
REFERENCE   4  (residues 1 to 297)
  AUTHORS   De Vet,E.C., Aguado,B. and Campbell,R.D.
  TITLE     Adaptor signalling proteins Grb2 and Grb7 are recruited by human
            G6f, a novel member of the immunoglobulin superfamily encoded in
            the MHC
  JOURNAL   Biochem J 375 (Pt 1), 207-213 (2003)
   PUBMED   12852788
  REMARK    GeneRIF: G6f recruits adaptor signalling proteins Grb2 and Grb7.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC137212.1 and AJ496460.1.
            
            Summary: The human G6f protein is a type I transmembrane protein
            belonging to the immunoglobin (Ig) superfamily, which is comprised
            of cell-surface proteins involved in the immune system and cellular
            recognition (de Vet et al., 2003 [PubMed 12852788]).[supplied by
            OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC137212.1, KU253635.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375832.5/ ENSP00000364992.5
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..297
                     /product="lymphocyte antigen 6 complex locus protein G6f
                     isoform 1 precursor"
                     /note="lymphocyte antigen 6 complex locus protein G6f;
                     lymphocyte antigen 6 complex, locus G6D; lymphocyte
                     antigen 6 complex, locus G6F"
                     /calculated_mol_wt=30746
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1737
     mat_peptide     17..297
                     /product="Lymphocyte antigen 6 complex locus protein G6f.
                     /id=PRO_0000318923"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SQ64.2)"
                     /calculated_mol_wt=30746
     Region          20..116
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          31..35
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          45..51
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            88
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16263699; propagated from
                     UniProtKB/Swiss-Prot (Q5SQ64.2)"
     Region          89..93
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          103..108
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            236..256
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SQ64.2)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:12852788; propagated from
                     UniProtKB/Swiss-Prot (Q5SQ64.2)"
     CDS             1..297
                     /gene="LY6G6F"
                     /gene_synonym="C6orf21; G6f; LY6G6; LY6G6D; NG32"
                     /coded_by="NM_001003693.3:42..935"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS34403.1"
                     /db_xref="GeneID:259215"
                     /db_xref="HGNC:HGNC:13933"
                     /db_xref="MIM:611404"
ORIGIN      
        1 mavlflllfl cgtpqaadnm qaiyvalgea velpcpsppt lhgdehlswf cspaagsftt
       61 lvaqvqvgrp apdpgkpgre srlrllgnys lwlegskeed agrywcavlg qhhnyqnwrv
      121 ydvlvlkgsq lsaraadgsp cnvllcsvvp srrmdsvtwq egkgpvrgrv qsfwgseaal
      181 llvcpgegls eprsrrprii rclmthnkgv sfslaasida spalcapstg wdmpwilmll
      241 ltmgqgvvil alsivlwrqr vrgapgrdas ipqfkpeiqv yenihlarlg ppahkpr
//
LOCUS       NP_005610                545 aa            linear   PRI 15-JAN-2026
DEFINITION  reticulon-2 isoform A [Homo sapiens].
ACCESSION   NP_005610
VERSION     NP_005610.1
DBSOURCE    REFSEQ: accession NM_005619.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Wang,G., Xu,Z., Sun,J., Liu,B., Ruan,Y., Gu,J. and Song,S.
  TITLE     O-GlcNAcylation enhances Reticulon 2 protein stability and its
            promotive effects on gastric cancer progression
  JOURNAL   Cell Signal 108, 110718 (2023)
   PUBMED   37196774
  REMARK    GeneRIF: O-GlcNAcylation enhances Reticulon 2 protein stability and
            its promotive effects on gastric cancer progression.
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Zheng,X., Lv,X., Chai,J., Huang,Y., Zhu,L. and Zhang,X.
  TITLE     RTN2, a new member of circadian clock genes identified by database
            mining and bioinformatics prediction, is highly expressed in
            ovarian cancer
  JOURNAL   Mol Med Rep 26 (5) (2022)
   PUBMED   36177918
  REMARK    GeneRIF: RTN2, a new member of circadian clock genes identified by
            database mining and bioinformatics prediction, is highly expressed
            in ovarian cancer.
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Tian,W., Zheng,H., Zhu,Z., Zhang,C., Luan,X. and Cao,L.
  TITLE     New phenotype of RTN2-related spectrum: Complicated form of spastic
            paraplegia-12
  JOURNAL   Ann Clin Transl Neurol 9 (8), 1108-1115 (2022)
   PUBMED   35684947
  REMARK    GeneRIF: New phenotype of RTN2-related spectrum: Complicated form
            of spastic paraplegia-12.
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 545)
  AUTHORS   Reid,E., Dearlove,A.M., Osborn,O., Rogers,M.T. and Rubinsztein,D.C.
  TITLE     A locus for autosomal dominant 'pure' hereditary spastic paraplegia
            maps to chromosome 19q13
  JOURNAL   Am J Hum Genet 66 (2), 728-732 (2000)
   PUBMED   10677333
REFERENCE   7  (residues 1 to 545)
  AUTHORS   Geisler,J.G., Palmer,R.J., Stubbs,L.J. and Mucenski,M.L.
  TITLE     Nspl1, a new Z-band-associated protein
  JOURNAL   J Muscle Res Cell Motil 20 (7), 661-668 (1999)
   PUBMED   10672514
REFERENCE   8  (residues 1 to 545)
  AUTHORS   Roebroek,A.J., Contreras,B., Pauli,I.G. and Van de Ven,W.J.
  TITLE     cDNA cloning, genomic organization, and expression of the human
            RTN2 gene, a member of a gene family encoding reticulons
  JOURNAL   Genomics 51 (1), 98-106 (1998)
   PUBMED   9693037
REFERENCE   9  (residues 1 to 545)
  AUTHORS   Geisler,J.G., Stubbs,L.J., Wasserman,W.W. and Mucenski,M.L.
  TITLE     Molecular cloning of a novel mouse gene with predominant muscle and
            neural expression
  JOURNAL   Mamm Genome 9 (4), 274-282 (1998)
   PUBMED   9530622
  REMARK    GeneRIF: Discusses cloning of mouse neuroendocrine-specific
            protein-like 1, in addition to partial cloning of the human
            ortholog. Also studies expression of both the mouse and human
            genes.
REFERENCE   10 (residues 1 to 545)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BK001687.1, BC073874.1 and
            AF004222.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene belongs to the family of reticulon encoding
            genes. Reticulons are associated with the endoplasmic reticulum,
            and are involved in neuroendocrine secretion or in membrane
            trafficking in neuroendocrine cells. Reticulon proteins also play
            an important role in the replication of positive-strand RNA (ssRNA)
            viruses. Mutations at this locus have been associated with
            autosomal dominant spastic paraplegia-12. [provided by RefSeq, Aug
            2020].
            
            Transcript Variant: This variant (1) represents the longest
            transcript, and encodes the longest isoform (A).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK001687.1, BC073874.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000245923.9/ ENSP00000245923.3
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..545
                     /product="reticulon-2 isoform A"
                     /note="NSP-like protein 1; NSP-like protein I;
                     neuroendocrine-specific protein-like I"
                     /calculated_mol_wt=59133
     Region          1..183
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75298.1)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70622; propagated from
                     UniProtKB/Swiss-Prot (O75298.1)"
     Region          <58..227
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          199..250
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75298.1)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70622; propagated from
                     UniProtKB/Swiss-Prot (O75298.1)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70622; propagated from
                     UniProtKB/Swiss-Prot (O75298.1)"
     Region          345..509
                     /region_name="Reticulon"
                     /note="pfam02453"
                     /db_xref="CDD:460562"
     Site            368..388
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75298.1)"
     Site            463..483
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75298.1)"
     CDS             1..545
                     /gene="RTN2"
                     /gene_synonym="HMNR11; NSP2; NSPL1; NSPLI; SPG12"
                     /coded_by="NM_005619.5:223..1860"
                     /note="isoform A is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12665.1"
                     /db_xref="GeneID:6253"
                     /db_xref="HGNC:HGNC:10468"
                     /db_xref="MIM:603183"
ORIGIN      
        1 mgqvlpvfah ckeapstass tpdsteggnd dsdfrelhta refseedeee ttsqdwgtpr
       61 eltfsyiafd gvvgsggrrd starrprpqg rsvseprdqh pqpslgdsle sipslsqspe
      121 pgrrgdpdta ppserpledl rlrldhlgwv argtgsgeds stssstpled eepqepnrle
      181 tgeageeldl rlrlaqpssp evltpqlspg sgtpqagtps psrsrdsnsg peeplleeee
      241 kqwgplerep vrgqcldstd qleftveprl lgtamewlkt slllavyktv pilelspplw
      301 taigwvqrgp tpptpvlrvl lkwaksprss gvpslslgad mgskvadlly wkdtrtsgvv
      361 ftglmvsllc llhfsivsva ahlallllcg tislrvyrkv lqavhrgdga npfqayldvd
      421 ltltreqter lshqitsrvv saatqlrhff lvedlvdslk lallfyiltf vgaifngltl
      481 lilgviglft ipllyrqhqa qidqyvglvt nqlshikaki rakipgtgal asaaaavsgs
      541 kakae
//
LOCUS       NP_001432042             395 aa            linear   PRI 15-JAN-2026
DEFINITION  ING4-ACRBP readthrough [Homo sapiens].
ACCESSION   NP_001432042
VERSION     NP_001432042.1
DBSOURCE    REFSEQ: accession NM_001445113.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125494.2 and AC135892.1.
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..395
                     /product="ING4-ACRBP readthrough"
                     /calculated_mol_wt=44942
     Region          <1..63
                     /region_name="PBP_sp32"
                     /note="Proacrosin binding protein sp32; pfam07222"
                     /db_xref="CDD:429354"
     CDS             1..395
                     /gene="ING4-ACRBP"
                     /coded_by="NM_001445113.1:1200..2387"
                     /db_xref="GeneID:144699907"
ORIGIN      
        1 mtspisphft vterqtfqpw perlsnnvee llqsslslgg qeqapehkqe qgvehrqept
       61 qehkqeegqk qeeqeeeqee egkqeegqgt kegreavsql qtdsepkfhs eslssnpssf
      121 aprvrevest pmimeniqel irsaqeidem neiydensyw rnqnpgsllq lphteallvl
      181 cysiventci itptakawky meeeilgfgk svcdslgrrh mstcalcdfc slkleqchse
      241 aslqrqqcdt shktpfvspl lasqslsign qvgspesgrf ygldlygglh mdfwcarlat
      301 kgcedvrvsg wlqteflsfq dgdfptkicd tdyiqypnyc sfksqqclmr nrnrkvsrmr
      361 clqnetysal spgksedvvl rwsqefstlt lgqfg
//
LOCUS       NP_060517                420 aa            linear   PRI 15-JAN-2026
DEFINITION  pre-mRNA-splicing factor RBM22 [Homo sapiens].
ACCESSION   NP_060517
VERSION     NP_060517.1
DBSOURCE    REFSEQ: accession NM_018047.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Le Hir-Reynaud,E., Soubise,B., Mendoza,A.M., Konan,C., Commet,S.,
            Gueganic,N., Tous,C., Corcos,L., Douet-Guilbert,N. and Troadec,M.B.
  TITLE     RBM22-depletion delays progression through all steps of cell cycle
            and increases ploidy in myeloid cells
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1872 (6), 119965 (2025)
   PUBMED   40268057
  REMARK    GeneRIF: RBM22 is implicated in cell cycle progression
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Du,X., Qin,W., Yang,C., Dai,L., San,M., Xia,Y., Zhou,S., Wang,M.,
            Wu,S., Zhang,S., Zhou,H., Li,F., He,F., Tang,J., Chen,J.Y., Zhou,Y.
            and Xiao,R.
  TITLE     RBM22 regulates RNA polymerase II 5' pausing, elongation rate, and
            termination by coordinating 7SK-P-TEFb complex and SPT5
  JOURNAL   Genome Biol 25 (1), 102 (2024)
   PUBMED   38641822
  REMARK    GeneRIF: RBM22 regulates RNA polymerase II 5' pausing, elongation
            rate, and termination by coordinating 7SK-P-TEFb complex and SPT5.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Jimenez-Vacas,J.M., Montero-Hidalgo,A.J., Gomez-Gomez,E.,
            Saez-Martinez,P., Fuentes-Fayos,A.C., Closa,A.,
            Gonzalez-Serrano,T., Martinez-Lopez,A., Sanchez-Sanchez,R.,
            Lopez-Casas,P.P., Sarmento-Cabral,A., Olmos,D., Eyras,E.,
            Castano,J.P., Gahete,M.D. and Luque,R.M.
  TITLE     Tumor suppressor role of RBM22 in prostate cancer acting as a
            dual-factor regulating alternative splicing and transcription of
            key oncogenic genes
  JOURNAL   Transl Res 253, 68-79 (2023)
   PUBMED   36089245
  REMARK    GeneRIF: Tumor suppressor role of RBM22 in prostate cancer acting
            as a dual-factor regulating alternative splicing and transcription
            of key oncogenic genes.
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Chai,G., Webb,A., Li,C., Antaki,D., Lee,S., Breuss,M.W., Lang,N.,
            Stanley,V., Anzenberg,P., Yang,X., Marshall,T., Gaffney,P.,
            Wierenga,K.J., Chung,B.H., Tsang,M.H., Pais,L.S., Lovgren,A.K.,
            VanNoy,G.E., Rehm,H.L., Mirzaa,G., Leon,E., Diaz,J., Neumann,A.,
            Kalverda,A.P., Manfield,I.W., Parry,D.A., Logan,C.V., Johnson,C.A.,
            Bonthron,D.T., Valleley,E.M.A., Issa,M.Y., Abdel-Ghafar,S.F.,
            Abdel-Hamid,M.S., Jennings,P., Zaki,M.S., Sheridan,E. and
            Gleeson,J.G.
  TITLE     Mutations in Spliceosomal Genes PPIL1 and PRP17 Cause
            Neurodegenerative Pontocerebellar Hypoplasia with Microcephaly
  JOURNAL   Neuron 109 (2), 241-256 (2021)
   PUBMED   33220177
REFERENCE   7  (residues 1 to 420)
  AUTHORS   Satoh,J., Obayashi,S., Misawa,T., Sumiyoshi,K., Oosumi,K. and
            Tabunoki,H.
  TITLE     Protein microarray analysis identifies human cellular prion protein
            interactors
  JOURNAL   Neuropathol Appl Neurobiol 35 (1), 16-35 (2009)
   PUBMED   18482256
REFERENCE   8  (residues 1 to 420)
  AUTHORS   Montaville,P., Dai,Y., Cheung,C.Y., Giller,K., Becker,S.,
            Michalak,M., Webb,S.E., Miller,A.L. and Krebs,J.
  TITLE     Nuclear translocation of the calcium-binding protein ALG-2 induced
            by the RNA-binding protein RBM22
  JOURNAL   Biochim Biophys Acta 1763 (11), 1335-1343 (2006)
   PUBMED   17045351
  REMARK    GeneRIF: ALG-2 alone evenly distributed within the cell, whereas in
            the presence of RBM22 the two proteins co-localized within the
            nucleus.
REFERENCE   9  (residues 1 to 420)
  AUTHORS   Kittler,R., Putz,G., Pelletier,L., Poser,I., Heninger,A.K.,
            Drechsel,D., Fischer,S., Konstantinova,I., Habermann,B.,
            Grabner,H., Yaspo,M.L., Himmelbauer,H., Korn,B., Neugebauer,K.,
            Pisabarro,M.T. and Buchholz,F.
  TITLE     An endoribonuclease-prepared siRNA screen in human cells identifies
            genes essential for cell division
  JOURNAL   Nature 432 (7020), 1036-1040 (2004)
   PUBMED   15616564
REFERENCE   10 (residues 1 to 420)
  AUTHORS   Hartmuth,K., Urlaub,H., Vornlocher,H.P., Will,C.L., Gentzel,M.,
            Wilm,M. and Luhrmann,R.
  TITLE     Protein composition of human prespliceosomes isolated by a
            tobramycin affinity-selection method
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16719-16724 (2002)
   PUBMED   12477934
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA534416.1, BC003402.1 and
            N23415.1.
            
            Summary: This gene encodes an RNA binding protein. The encoded
            protein may play a role in cell division and may be involved in
            pre-mRNA splicing. Related pseudogenes exist on chromosomes 6, 7,
            9, 13, 16, 18, and X. [provided by RefSeq, Mar 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001152.1, SRR3476690.115598.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000199814.9/ ENSP00000199814.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..420
                     /product="pre-mRNA-splicing factor RBM22"
                     /note="functional spliceosome-associated protein 47; zinc
                     finger CCCH domain-containing protein 16"
                     /calculated_mol_wt=46765
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9NW64.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NW64.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NW64.1)"
     Region          159..185
                     /region_name="ZnF_C3H1"
                     /note="zinc finger; smart00356"
                     /db_xref="CDD:214632"
     Site            212
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NW64.1)"
     Region          231..304
                     /region_name="RRM_RBM22"
                     /note="RNA recognition motif (RRM) found in
                     Pre-mRNA-splicing factor RBM22 and similar proteins;
                     cd12224"
                     /db_xref="CDD:409671"
     Region          303..343
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW64.1)"
     Region          372..420
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW64.1)"
     CDS             1..420
                     /gene="RBM22"
                     /gene_synonym="Cwc2; fSAP47; ZC3H16"
                     /coded_by="NM_018047.3:78..1340"
                     /db_xref="CCDS:CCDS34278.1"
                     /db_xref="GeneID:55696"
                     /db_xref="HGNC:HGNC:25503"
                     /db_xref="MIM:612430"
ORIGIN      
        1 matslgsnty nrqnwedadf pilcqtclge npyirmtkek ygkeckicar pftvfrwcpg
       61 vrmrfkktev cqtcsklknv cqtclldley glpiqvrdag lsfkddmpks dvnkeyytqn
      121 mereisnsdg trpvgmlgka tstsdmllkl arttpyykrn rphicsfwvk geckrgeecp
      181 yrhekptdpd dpladqnikd ryygindpva dkllkrastm prldppedkt ittlyvgglg
      241 dtitetdlrn hfyqfgeirt itvvqrqqca fiqfatrqaa evaaeksfnk livngrrlnv
      301 kwgrsqaarg kekekdgttd sgiklepvpg lpgalppppa aeeeasanyf nlppsgppav
      361 vnialppppg iapppppgfg phmfhpmgpp ppfmrapgpi hypsqdpqrm gahagkhssp
//
LOCUS       NP_001416914             326 aa            linear   PRI 20-JAN-2026
DEFINITION  olfactory receptor 4F17 isoform 2 [Homo sapiens].
ACCESSION   NP_001416914
VERSION     NP_001416914.1
DBSOURCE    REFSEQ: accession NM_001429985.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Linardopoulou,E., Mefford,H.C., Nguyen,O., Friedman,C., van den
            Engh,G., Farwell,D.G., Coltrera,M. and Trask,B.J.
  TITLE     Transcriptional activity of multiple copies of a subtelomerically
            located olfactory receptor gene that is polymorphic in number and
            location
  JOURNAL   Hum Mol Genet 10 (21), 2373-2383 (2001)
   PUBMED   11689484
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Mefford,H.C., Linardopoulou,E., Coil,D., van den Engh,G. and
            Trask,B.J.
  TITLE     Comparative sequencing of a multicopy subtelomeric region
            containing olfactory receptor genes reveals multiple interactions
            between non-homologous chromosomes
  JOURNAL   Hum Mol Genet 10 (21), 2363-2372 (2001)
   PUBMED   11689483
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Trask,B.J., Friedman,C., Martin-Gallardo,A., Rowen,L., Akinbami,C.,
            Blankenship,J., Collins,C., Giorgi,D., Iadonato,S., Johnson,F.,
            Kuo,W.L., Massa,H., Morrish,T., Naylor,S., Nguyen,O.T.,
            Rouquier,S., Smith,T., Wong,D.J., Youngblom,J. and van den Engh,G.
  TITLE     Members of the olfactory receptor gene family are contained in
            large blocks of DNA duplicated polymorphically near the ends of
            human chromosomes
  JOURNAL   Hum Mol Genet 7 (1), 13-26 (1998)
   PUBMED   9384599
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008977.9.
            
            Summary: Olfactory receptors interact with odorant molecules in the
            nose, to initiate a neuronal response that triggers the perception
            of a smell. The olfactory receptor proteins are members of a large
            family of G-protein-coupled receptors (GPCR) arising from single
            coding-exon genes. Olfactory receptors share a 7-transmembrane
            domain structure with many neurotransmitter and hormone receptors
            and are responsible for the recognition and G protein-mediated
            transduction of odorant signals. The olfactory receptor gene family
            is the largest in the genome. [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2148093
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..326
                     /product="olfactory receptor 4F17 isoform 2"
                     /note="olfactory receptor, family 4, subfamily F, member
                     11 pseudogene; olfactory receptor, family 4, subfamily F,
                     member 19; olfactory receptor 4F17; olfactory receptor
                     4F11; olfactory receptor 4F18; olfactory receptor 4F19"
                     /calculated_mol_wt=36390
     Region          40..305
                     /region_name="7tmA_OR4-like"
                     /note="olfactory receptor family 4 and related proteins,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15226"
                     /db_xref="CDD:320354"
     Region          40..66
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320354"
     Region          73..99
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320354"
     Site            order(95,98..99,111..116,118..119,122,167,169..173,209,
                     212..214,216..218,220..221,265,268..269,271..272,275,
                     279..280,282..284,287,290..291)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320354"
     Region          111..141
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320354"
     Region          154..175
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320354"
     Region          209..239
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320354"
     Region          245..275
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320354"
     Region          280..305
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320354"
     CDS             1..326
                     /gene="OR4F17"
                     /gene_synonym="OR4F11P; OR4F18; OR4F19"
                     /coded_by="NM_001429985.1:46..1026"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:81099"
                     /db_xref="HGNC:HGNC:15381"
ORIGIN      
        1 mkkvtaeais wnestsetnn smvtefiflg lsdsqglqtf lfmlffvfyg givfgnlliv
       61 itvvsdshlh spmyfllanl slidlslssv tapkmitdff sqrkvisfkg clvqifllhf
      121 fggsemvili amgfdryiai ckplhyttim cgnacvgima vawgigflhs vsqlafavhl
      181 pfcgpnevds fycdlprvik lactdtyrld imviansgvl tvcsfvllii sytiilmtiq
      241 hrpldksska lstltahitv vllffgpcvf iyawpfpiks ldkflavfys vitpllnpii
      301 ytlrnkdmkt airqlrkwda hssvkf
//
LOCUS       NP_001243143            1026 aa            linear   PRI 20-JAN-2026
DEFINITION  sodium/potassium-transporting ATPase subunit alpha-3 isoform 3
            [Homo sapiens].
ACCESSION   NP_001243143
VERSION     NP_001243143.1
DBSOURCE    REFSEQ: accession NM_001256214.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1026)
  AUTHORS   Depierre,P., Ginet,V., Truttmann,A.C. and Puyal,J.
  TITLE     Neuronal autosis is Na+/K+-ATPase alpha 3-dependent and involved in
            hypoxic-ischemic neuronal death
  JOURNAL   Cell Death Dis 15 (5), 363 (2024)
   PUBMED   38796484
  REMARK    GeneRIF: Neuronal autosis is Na[+]/K[+]-ATPase alpha 3-dependent
            and involved in hypoxic-ischemic neuronal death.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1026)
  AUTHORS   Muthaffar,O.Y., Alqarni,A., Shafei,J.A., Bahowarth,S.Y.,
            Alyazidi,A.S. and Naseer,M.I.
  TITLE     Childhood-related neural genotype-phenotype in ATP1A3 mutations:
            comprehensive analysis
  JOURNAL   Genes Genomics 46 (4), 475-487 (2024)
   PUBMED   38243045
  REMARK    GeneRIF: Childhood-related neural genotype-phenotype in ATP1A3
            mutations: comprehensive analysis.
REFERENCE   3  (residues 1 to 1026)
  AUTHORS   You,Y., Zhang,Z., Sultana,N., Ericsson,M., Martens,Y.A., Sun,M.,
            Kanekiyo,T., Ikezu,S., Shaffer,S.A. and Ikezu,T.
  TITLE     ATP1A3 as a target for isolating neuron-specific extracellular
            vesicles from human brain and biofluids
  JOURNAL   Sci Adv 9 (37), eadi3647 (2023)
   PUBMED   37713494
  REMARK    GeneRIF: ATP1A3 as a target for isolating neuron-specific
            extracellular vesicles from human brain and biofluids.
REFERENCE   4  (residues 1 to 1026)
  AUTHORS   Alyamani,S.A., Aldhalaan,H.M., Almuhaizea,M.A. and Abukhalid,M.F.
  TITLE     Expanding the Allelic spectrum in ATP1A3-related disorders with 3
            novel mutations and clinic features
  JOURNAL   Neurosciences (Riyadh) 28 (3), 195-198 (2023)
   PUBMED   37482377
  REMARK    GeneRIF: Expanding the Allelic spectrum in ATP1A3-related disorders
            with 3 novel mutations and clinic features.
REFERENCE   5  (residues 1 to 1026)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   6  (residues 1 to 1026)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
REFERENCE   7  (residues 1 to 1026)
  AUTHORS   Brashear,A., Sweadner,K.J., Haq,I., Napoli,E. and Ozelius,L.
  TITLE     ATP1A3-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301294
REFERENCE   8  (residues 1 to 1026)
  AUTHORS   Lingrel,J.B., Orlowski,J., Shull,M.M. and Price,E.M.
  TITLE     Molecular genetics of Na,K-ATPase
  JOURNAL   Prog Nucleic Acid Res Mol Biol 38, 37-89 (1990)
   PUBMED   2158121
  REMARK    Review article
REFERENCE   9  (residues 1 to 1026)
  AUTHORS   Ovchinnikov,Yu.A., Monastyrskaya,G.S., Broude,N.E.,
            Ushkaryov,Yu.A., Melkov,A.M., Smirnov,Yu.V., Malyshev,I.V.,
            Allikmets,R.L., Kostina,M.B., Dulubova,I.E. et al.
  TITLE     Family of human Na+, K+-ATPase genes. Structure of the gene for the
            catalytic subunit (alpha III-form) and its relationship with
            structural features of the protein
  JOURNAL   FEBS Lett 233 (1), 87-94 (1988)
   PUBMED   2838329
REFERENCE   10 (residues 1 to 1026)
  AUTHORS   Sverdlov,E.D., Monastyrskaia,G.S., Broude,N.E., Ushkarev,Iu.A. and
            Melkov,A.M.
  TITLE     [The family of human Na+,K+-ATPase genes. Structure of the gene for
            isozyme alphaII]
  JOURNAL   Dokl Akad Nauk SSSR 297 (6), 1488-1494 (1987)
   PUBMED   2834163
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK295078.1, AK223569.1 and
            BC009282.2.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type cation transport ATPases, and to the subfamily of Na+/K+
            -ATPases. Na+/K+ -ATPase is an integral membrane protein
            responsible for establishing and maintaining the electrochemical
            gradients of Na and K ions across the plasma membrane. These
            gradients are essential for osmoregulation, for sodium-coupled
            transport of a variety of organic and inorganic molecules, and for
            electrical excitability of nerve and muscle. This enzyme is
            composed of two subunits, a large catalytic subunit (alpha) and a
            smaller glycoprotein subunit (beta). The catalytic subunit of
            Na+/K+ -ATPase is encoded by multiple genes. This gene encodes an
            alpha 3 subunit. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jan 2012].
            
            Transcript Variant: This variant (3) has an additional in-frame
            segment in the 5' coding region, compared to variant 1. The
            resulting isoform (3) is longer than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295078.1, SRR14038197.2239696.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1026
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..1026
                     /product="sodium/potassium-transporting ATPase subunit
                     alpha-3 isoform 3"
                     /EC_number="7.2.2.13"
                     /note="sodium-potassium-ATPase, alpha 3 polypeptide;
                     Na+/K+ ATPase 3; sodium/potassium-transporting ATPase
                     alpha-3 chain; sodium/potassium-transporting ATPase
                     subunit alpha-3; sodium pump subunit alpha-3; Na(+)/K(+)
                     ATPase alpha-3 subunit; Na(+)/K(+) ATPase alpha(III)
                     subunit; sodium-potassium ATPase catalytic subunit
                     alpha-3; ATPase, Na+/K+ transporting, alpha 3 polypeptide;
                     Na+, K+ activated adenosine triphosphatase alpha subunit"
                     /calculated_mol_wt=112928
     Region          30..1026
                     /region_name="ATPase-IIC_X-K"
                     /note="sodium or proton efflux -- potassium uptake
                     antiporter, P-type ATPase, alpha subunit; TIGR01106"
                     /db_xref="CDD:273445"
     CDS             1..1026
                     /gene="ATP1A3"
                     /gene_synonym="AHC2; CAPOS; DEE99; DYT12; RDP"
                     /coded_by="NM_001256214.2:155..3235"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58664.1"
                     /db_xref="GeneID:478"
                     /db_xref="HGNC:HGNC:801"
                     /db_xref="MIM:182350"
ORIGIN      
        1 mgsggsdsyr iatsqdkkdd kdspkknkgk errdlddlkk evamtehkms veevcrkynt
       61 dcvqglthsk aqeilardgp naltpppttp ewvkfcrqlf ggfsillwig ailcflaygi
      121 qagteddpsg dnlylgivla avviitgcfs yyqeaksski mesfknmvpq qalviregek
      181 mqvnaeevvv gdlveikggd rvpadlriis ahgckvdnss ltgesepqtr spdcthdnpl
      241 etrnitffst ncvegtargv vvatgdrtvm griatlasgl evgktpiaie iehfiqlitg
      301 vavflgvsff ilslilgytw leavifligi ivanvpegll atvtvcltlt akrmarkncl
      361 vknleavetl gststicsdk tgtltqnrmt vahmwfdnqi headttedqs gtsfdkssht
      421 wvalshiagl cnravfkggq dnipvlkrdv agdasesall kcielssgsv klmrernkkv
      481 aeipfnstnk yqlsiheted pndnryllvm kgaperildr cstillqgke qpldeemkea
      541 fqnaylelgg lgervlgfch yylpeeqfpk gfafdcddvn fttdnlcfvg lmsmidppra
      601 avpdavgkcr sagikvimvt gdhpitakai akgvgiiseg netvediaar lnipvsqvnp
      661 rdakacvihg tdlkdftseq ideilqnhte ivfartspqq kliivegcqr qgaivavtgd
      721 gvndspalkk adigvamgia gsdvskqaad millddnfas ivtgveegrl ifdnlkksia
      781 ytltsnipei tpfllfiman iplplgtiti lcidlgtdmv paislayeaa esdimkrqpr
      841 nprtdklvne rlismaygqi gmiqalggff syfvilaeng flpgnlvgir lnwddrtvnd
      901 ledsygqqwt yeqrkvveft chtaffvsiv vvqwadliic ktrrnsvfqq gmknkilifg
      961 lfeetalaaf lsycpgmdva lrmyplkpsw wfcafpysfl ifvydeirkl ilrrnpggwv
     1021 eketyy
//
LOCUS       NP_001387108             191 aa            linear   PRI 20-JAN-2026
DEFINITION  large ribosomal subunit protein uL23m isoform 5 [Homo sapiens].
ACCESSION   NP_001387108 XP_011518578
VERSION     NP_001387108.1
DBSOURCE    REFSEQ: accession NM_001400179.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Zhang,Z. and Gerstein,M.
  TITLE     Identification and characterization of over 100 mitochondrial
            ribosomal protein pseudogenes in the human genome
  JOURNAL   Genomics 81 (5), 468-480 (2003)
   PUBMED   12706105
REFERENCE   7  (residues 1 to 191)
  AUTHORS   O'Brien,T.W.
  TITLE     Evolution of a protein-rich mitochondrial ribosome: implications
            for human genetic disease
  JOURNAL   Gene 286 (1), 73-79 (2002)
   PUBMED   11943462
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Kenmochi,N., Suzuki,T., Uechi,T., Magoori,M., Kuniba,M., Higa,S.,
            Watanabe,K. and Tanaka,T.
  TITLE     The human mitochondrial ribosomal protein genes: mapping of 54
            genes to the chromosomes and implications for human disorders
  JOURNAL   Genomics 77 (1-2), 65-70 (2001)
   PUBMED   11543634
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Suzuki,T., Terasaki,M., Takemoto-Hori,C., Hanada,T., Ueda,T.,
            Wada,A. and Watanabe,K.
  TITLE     Structural compensation for the deficit of rRNA with proteins in
            the mammalian mitochondrial ribosome. Systematic analysis of
            protein components of the large ribosomal subunit from mammalian
            mitochondria
  JOURNAL   J Biol Chem 276 (24), 21724-21736 (2001)
   PUBMED   11279069
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Tsang,P., Gilles,F., Yuan,L., Kuo,Y.H., Lupu,F., Samara,G.,
            Moosikasuwan,J., Goye,A., Zelenetz,A.D., Selleri,L. et al.
  TITLE     A novel L23-related gene 40 kb downstream of the imprinted H19 gene
            is biallelically expressed in mid-fetal and adult human tissues
  JOURNAL   Hum Mol Genet 4 (9), 1499-1507 (1995)
   PUBMED   8541832
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC051649.21.
            
            On Jan 20, 2022 this sequence version replaced XP_011518578.1.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 39S subunit protein. The gene is
            biallelically expressed, despite its location within a region of
            imprinted genes on chromosome 11. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2384967.1,
                                           SRR18074968.2721717.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..191
                     /product="large ribosomal subunit protein uL23m isoform 5"
                     /note="L23 mitochondrial-related protein; ribosomal
                     protein related to L23 (mitochondrial); 39S ribosomal
                     protein L23, mitochondrial; mitochondrial large ribosomal
                     subunit protein uL23m"
                     /calculated_mol_wt=21711
     Region          <42..99
                     /region_name="Ribosomal_L23"
                     /note="Ribosomal protein L23; pfam00276"
                     /db_xref="CDD:459743"
     CDS             1..191
                     /gene="MRPL23"
                     /gene_synonym="L23MRP; L23mt; MRP-L23; RPL23L; uL23m"
                     /coded_by="NM_001400179.1:32..607"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS91408.1"
                     /db_xref="GeneID:6150"
                     /db_xref="HGNC:HGNC:10322"
                     /db_xref="MIM:600789"
ORIGIN      
        1 marnvvyply rlggpqlrvf rtnffiqlvr pgvaqpedtv qfripmemtr vdlrnylegi
       61 ynvpvaavrt rvqhgsnkrr dhrnvrikkp dykvayvqlp sqtpskeqng qgstlcfrss
      121 cskgwstwgt rdprpawspv ggriprkags ggpanriaqd grlllknlrp rvprreqpat
      181 rfplwrrgvl a
//
LOCUS       NP_001243426             535 aa            linear   PRI 20-JAN-2026
DEFINITION  CYP3A7-CYP3A51P protein [Homo sapiens].
ACCESSION   NP_001243426
VERSION     NP_001243426.2
DBSOURCE    REFSEQ: accession NM_001256497.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Rodriguez-Antona,C., Axelson,M., Otter,C., Rane,A. and
            Ingelman-Sundberg,M.
  TITLE     A novel polymorphic cytochrome P450 formed by splicing of CYP3A7
            and the pseudogene CYP3AP1
  JOURNAL   J Biol Chem 280 (31), 28324-28331 (2005)
   PUBMED   15937338
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Finta,C. and Zaphiropoulos,P.G.
  TITLE     The human cytochrome P450 3A locus. Gene evolution by capture of
            downstream exons
  JOURNAL   Gene 260 (1-2), 13-23 (2000)
   PUBMED   11137287
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Itoh,S., Yanagimoto,T., Tagawa,S., Hashimoto,H., Kitamura,R.,
            Nakajima,Y., Okochi,T., Fujimoto,S., Uchino,J. and Kamataki,T.
  TITLE     Genomic organization of human fetal specific P-450IIIA7 (cytochrome
            P-450HFLa)-related gene(s) and interaction of transcriptional
            regulatory factor with its DNA element in the 5' flanking region
  JOURNAL   Biochim Biophys Acta 1130 (2), 133-138 (1992)
   PUBMED   1562592
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC069294.5, AF315325.1 and AC005020.5.
            
            On Apr 10, 2014 this sequence version replaced NP_001243426.1.
            
            Summary: This locus represents readthrough transcription between
            the neighboring CYP3A7 (cytochrome P450, family 3, subfamily A,
            polypeptide 7) and CYP3A51P (cytochrome P450, family 3, subfamily
            A, polypeptide 51, pseudogene) genes, which are members of the
            CYP3A gene cluster on chromosome 7. The downstream pseudogene is
            not known to be independently transcribed. The readthrough
            transcript includes CYP3A7 exons 1-13 and exons 2 and 13 of the
            pseudogene. It encodes a CYP3A isoform with a novel C-terminus.
            This isoform is only expressed in alleles containing a T nucleotide
            at the -6 position of a splice acceptor in the pseudogene, which
            enables correct splicing of the upstream CYP3A7 exons to the
            pseudogene exons. It should be noted that the reference genome
            sequence represents the CYP3A7_39256 T->A allele, and thus this
            haplotype is unlikely to produce the readthrough transcript.
            [provided by RefSeq, Jan 2015].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF315325.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            readthrough transcript :: includes exons from GeneID 1551, 1578
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..535
                     /product="CYP3A7-CYP3A51P protein"
                     /EC_number="1.14.14.1"
                     /note="CYP3A7-CYP3AP1 readthrough; Cytochrome P450-HFLA"
                     /calculated_mol_wt=61361
     Region          67..492
                     /region_name="CYP3A"
                     /note="cytochrome P450 family 3, subfamily A; cd20650"
                     /db_xref="CDD:410743"
     Site            order(76,105..108,119..120,210,212..213,215,220,241,301,
                     304..305,309,370..372,374,481..482)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410743"
     Site            order(105,118..119,126,130,137,302,305..306,309,370,373,
                     375,434..437,440..444,448)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410743"
     CDS             1..535
                     /gene="CYP3A7-CYP3A51P"
                     /gene_synonym="CYP3A7-3AP1; CYP3A7-CYP3AP1; CYP3A7.1L"
                     /coded_by="NM_001256497.3:104..1711"
                     /db_xref="GeneID:100861540"
                     /db_xref="HGNC:HGNC:51504"
ORIGIN      
        1 mdlipnlave twlllavsli llylygtrth glfkklgipg ptplpflgna lsfrkgywtf
       61 dmecykkyrk vwgiydcqqp mlaitdpdmi ktvlvkecys vftnrrpfgp vgfmknaisi
      121 aedeewkrir sllsptftsg klkemvpiia qygdvlvrnl rreaetgkpv tlkhvfgays
      181 mdvitstsfg vsidslnnpq dpfventkkl lrfnpldpfv lsikvfpflt pilealnitv
      241 fprkvisflt ksvkqikegr lketqkhrvd flqlmidsqn skdsethkal sdlelmaqsi
      301 ififagyett ssvlsfiiye lathpdvqqk vqkeidtvlp nkapptydtv lqleyldmvv
      361 netlrlfpva mrlervckkd veingmfipk gvvvmipsyv lhhdpkywte pekflperfs
      421 kknkdnidpy iytpfgsgpr ncigmrfalv nmklalvrvl qnfsfkpcke tqiplklrfg
      481 gllltekpiv lkaesrdetf vdmepihmdf lrslafqgph lcffwellcp tirsr
//
LOCUS       NP_001308001             446 aa            linear   PRI 20-JAN-2026
DEFINITION  cystathionine beta-synthase isoform 2 [Homo sapiens].
ACCESSION   NP_001308001 XP_011528086
VERSION     NP_001308001.1
DBSOURCE    REFSEQ: accession NM_001321072.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Hu,X.J., Sun,Y., Liu,G.J., Zhang,J., Zhang,L.X. and Peng,Y.H.
  TITLE     Cystathionine-beta-synthase expression correlates with tumour
            progression and adverse prognosis in patients with colon cancer
  JOURNAL   J Int Med Res 52 (9), 3000605241263726 (2024)
   PUBMED   39324183
  REMARK    GeneRIF: Cystathionine-beta-synthase expression correlates with
            tumour progression and adverse prognosis in patients with colon
            cancer.
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Mijatovic,E., Ascencao,K., Szabo,C. and Majtan,T.
  TITLE     Cellular turnover and degradation of the most common missense
            cystathionine beta-synthase variants causing homocystinuria
  JOURNAL   Protein Sci 33 (8), e5123 (2024)
   PUBMED   39041895
  REMARK    GeneRIF: Cellular turnover and degradation of the most common
            missense cystathionine beta-synthase variants causing
            homocystinuria.
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Al-Sadeq,D.W., Conter,C., Thanassoulas,A., Al-Dewik,N.,
            Safieh-Garabedian,B., Martinez-Cruz,L.A., Nasrallah,G.K.,
            Astegno,A. and Nomikos,M.
  TITLE     Biochemical and structural impact of two novel missense mutations
            in cystathionine beta-synthase gene associated with homocystinuria
  JOURNAL   Biochem J 481 (8), 569-585 (2024)
   PUBMED   38563463
  REMARK    GeneRIF: Biochemical and structural impact of two novel missense
            mutations in cystathionine beta-synthase gene associated with
            homocystinuria.
REFERENCE   4  (residues 1 to 446)
  AUTHORS   McCorvie,T.J., Adamoski,D., Machado,R.A.C., Tang,J., Bailey,H.J.,
            Ferreira,D.S.M., Strain-Damerell,C., Basle,A., Ambrosio,A.L.B.,
            Dias,S.M.G. and Yue,W.W.
  TITLE     Architecture and regulation of filamentous human cystathionine
            beta-synthase
  JOURNAL   Nat Commun 15 (1), 2931 (2024)
   PUBMED   38575566
  REMARK    GeneRIF: Architecture and regulation of filamentous human
            cystathionine beta-synthase.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Sacharow,S.J. and Levy,H.L.
  TITLE     Homocystinuria due to Cystathionine Beta-Synthase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301697
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Milewicz,D.M. and Cecchi,A.C.
  TITLE     Heritable Thoracic Aortic Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301299
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Kraus,J., Packman,S., Fowler,B. and Rosenberg,L.E.
  TITLE     Purification and properties of cystathionine beta-synthase from
            human liver. Evidence for identical subunits
  JOURNAL   J Biol Chem 253 (18), 6523-6528 (1978)
   PUBMED   681363
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Griffiths,R. and Tudball,N.
  TITLE     The molecular defect in a case of (cystathionine
            beta-synthase)-deficient homocystinuria
  JOURNAL   Eur J Biochem 74 (2), 269-273 (1977)
   PUBMED   404147
REFERENCE   10 (residues 1 to 446)
  AUTHORS   Longhi,R.C., Fleisher,L.D., Tallan,H.H. and Gaull,G.E.
  TITLE     Cystathionine beta-synthase deficiency: a qualitative abnormality
            of the deficient enzyme modified by vitamin B6 therapy
  JOURNAL   Pediatr Res 11 (2), 100-103 (1977)
   PUBMED   840498
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001630.1.
            
            On Mar 18, 2016 this sequence version replaced XP_011528086.1.
            
            Summary: The protein encoded by this gene acts as a homotetramer to
            catalyze the conversion of homocysteine to cystathionine, the first
            step in the transsulfuration pathway. The encoded protein is
            allosterically activated by adenosyl-methionine and uses pyridoxal
            phosphate as a cofactor. Defects in this gene can cause
            cystathionine beta-synthase deficiency (CBSD), which can lead to
            homocystinuria. This gene is a major contributor to cellular
            hydrogen sulfide production. Multiple alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Feb 2016].
            
            Transcript Variant: This variant (5) initiates translation at an
            alternate start codon compared to variant 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.765353.1,
                                           SRR3476690.870767.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..446
                     /product="cystathionine beta-synthase isoform 2"
                     /EC_number="4.2.1.22"
                     /note="serine sulfhydrase; beta-thionase; methylcysteine
                     synthase"
                     /calculated_mol_wt=49088
     Region          1..439
                     /region_name="cysta_beta"
                     /note="cystathionine beta-synthase; TIGR01137"
                     /db_xref="CDD:273464"
     CDS             1..446
                     /gene="CBS"
                     /gene_synonym="HIP4"
                     /coded_by="NM_001321072.1:627..1967"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:875"
                     /db_xref="HGNC:HGNC:1550"
                     /db_xref="MIM:613381"
ORIGIN      
        1 makceffnag gsvkdrislr miedaerdgt lkpgdtiiep tsgntgigla laaavrgyrc
       61 iivmpekmss ekvdvlralg aeivrtptna rfdspeshvg vawrlkneip nshildqyrn
      121 asnplahydt tadeilqqcd gkldmlvasv gtggtitgia rklkekcpgc riigvdpegs
      181 ilaepeelnq teqttyeveg igydfiptvl drtvvdkwfk sndeeaftfa rmliaqegll
      241 cggsagstva vavkaaqelq egqrcvvilp dsvrnymtkf lsdrwmlqkg flkeedltek
      301 kpwwwhlrvq elglsapltv lptitcghti eilrekgfdq apvvdeagvi lgmvtlgnml
      361 ssllagkvqp sdqvgkviyk qfkqirltdt lgrlshilem dhfalvvheq iqyhstgkss
      421 qrqmvfgvvt aidllnfvaa qerdqk
//
LOCUS       NP_001340938             551 aa            linear   PRI 20-JAN-2026
DEFINITION  cystathionine beta-synthase isoform a [Homo sapiens].
ACCESSION   NP_001340938 XP_011544401
VERSION     NP_001340938.1
DBSOURCE    REFSEQ: accession NM_001354009.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Kumar,A., Wissbrock,A., Goradia,N., Bellstedt,P., Ramachandran,R.,
            Imhof,D. and Ohlenschlager,O.
  TITLE     Heme interaction of the intrinsically disordered N-terminal peptide
            segment of human cystathionine-beta-synthase
  JOURNAL   Sci Rep 8 (1), 2474 (2018)
   PUBMED   29410458
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Kabil,O., Zhou,Y. and Banerjee,R.
  TITLE     Human cystathionine beta-synthase is a target for sumoylation
  JOURNAL   Biochemistry 45 (45), 13528-13536 (2006)
   PUBMED   17087506
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Hu,Y.H., Warnatz,H.J., Vanhecke,D., Wagner,F., Fiebitz,A.,
            Thamm,S., Kahlem,P., Lehrach,H., Yaspo,M.L. and Janitz,M.
  TITLE     Cell array-based intracellular localization screening reveals novel
            functional features of human chromosome 21 proteins
  JOURNAL   BMC Genomics 7, 155 (2006)
   PUBMED   16780588
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Chen,X., Jhee,K.H. and Kruger,W.D.
  TITLE     Production of the neuromodulator H2S by cystathionine beta-synthase
            via the condensation of cysteine and homocysteine
  JOURNAL   J Biol Chem 279 (50), 52082-52086 (2004)
   PUBMED   15520012
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Meier,M., Janosik,M., Kery,V., Kraus,J.P. and Burkhard,P.
  TITLE     Structure of human cystathionine beta-synthase: a unique pyridoxal
            5'-phosphate-dependent heme protein
  JOURNAL   EMBO J 20 (15), 3910-3916 (2001)
   PUBMED   11483494
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Kery,V., Bukovska,G. and Kraus,J.P.
  TITLE     Transsulfuration depends on heme in addition to pyridoxal
            5'-phosphate. Cystathionine beta-synthase is a heme protein
  JOURNAL   J Biol Chem 269 (41), 25283-25288 (1994)
   PUBMED   7929220
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FP236240.8.
            
            On Aug 29, 2017 this sequence version replaced XP_011544401.1.
            
            Sequence Note: NM_001354009 is annotated on a scaffold that is
            thought to be a false duplication and thus this accession is likely
            redundant with NM_000071.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.202756.1,
                                           SRR1803613.124526.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21p12"
     Protein         1..551
                     /product="cystathionine beta-synthase isoform a"
                     /EC_number="4.2.1.22"
                     /note="cystathionine beta-synthase-like protein"
                     /calculated_mol_wt=60456
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35520.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     Region          76..544
                     /region_name="cysta_beta"
                     /note="cystathionine beta-synthase; TIGR01137"
                     /db_xref="CDD:273464"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     CDS             1..551
                     /gene="LOC102724560"
                     /gene_synonym="CBSL"
                     /coded_by="NM_001354009.3:151..1806"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="GeneID:102724560"
ORIGIN      
        1 mpsetpqaev gptgcphrsg phsakgslek gspedkeake plwirpdaps rctwqlgrpa
       61 sesphhhtap akspkilpdi lkkigdtpmv rinkigkkfg lkcellakce ffnaggsvkd
      121 rislrmieda erdgtlkpgd tiieptsgnt giglalaaav rgyrciivmp ekmssekvdv
      181 lralgaeivr tptnarfdsp eshvgvawrl kneipnshil dqyrnasnpl ahydttadei
      241 lqqcdgkldm lvasvgtggt itgiarklke kcpgcriigv dpegsilaep eelnqteqtt
      301 yevegigydf iptvldrtvv dkwfksndee aftfarmlia qegllcggsa gstvavavka
      361 aqelqegqrc vvilpdsvrn ymtkflsdrw mlqkgflkee dltekkpwww hlrvqelgls
      421 apltvlptit cghtieilre kgfdqapvvd eagvilgmvt lgnmlsslla gkvqpsdqvg
      481 kviykqfkqi rltdtlgrls hilemdhfal vvheqiqyhs tgkssqrqmv fgvvtaidll
      541 nfvaaqerdq k
//
LOCUS       NP_001340943             565 aa            linear   PRI 20-JAN-2026
DEFINITION  cystathionine beta-synthase isoform b [Homo sapiens].
ACCESSION   NP_001340943 XP_011544396
VERSION     NP_001340943.1
DBSOURCE    REFSEQ: accession NM_001354014.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 565)
  AUTHORS   Kumar,A., Wissbrock,A., Goradia,N., Bellstedt,P., Ramachandran,R.,
            Imhof,D. and Ohlenschlager,O.
  TITLE     Heme interaction of the intrinsically disordered N-terminal peptide
            segment of human cystathionine-beta-synthase
  JOURNAL   Sci Rep 8 (1), 2474 (2018)
   PUBMED   29410458
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 565)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 565)
  AUTHORS   Kabil,O., Zhou,Y. and Banerjee,R.
  TITLE     Human cystathionine beta-synthase is a target for sumoylation
  JOURNAL   Biochemistry 45 (45), 13528-13536 (2006)
   PUBMED   17087506
REFERENCE   7  (residues 1 to 565)
  AUTHORS   Hu,Y.H., Warnatz,H.J., Vanhecke,D., Wagner,F., Fiebitz,A.,
            Thamm,S., Kahlem,P., Lehrach,H., Yaspo,M.L. and Janitz,M.
  TITLE     Cell array-based intracellular localization screening reveals novel
            functional features of human chromosome 21 proteins
  JOURNAL   BMC Genomics 7, 155 (2006)
   PUBMED   16780588
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 565)
  AUTHORS   Chen,X., Jhee,K.H. and Kruger,W.D.
  TITLE     Production of the neuromodulator H2S by cystathionine beta-synthase
            via the condensation of cysteine and homocysteine
  JOURNAL   J Biol Chem 279 (50), 52082-52086 (2004)
   PUBMED   15520012
REFERENCE   9  (residues 1 to 565)
  AUTHORS   Meier,M., Janosik,M., Kery,V., Kraus,J.P. and Burkhard,P.
  TITLE     Structure of human cystathionine beta-synthase: a unique pyridoxal
            5'-phosphate-dependent heme protein
  JOURNAL   EMBO J 20 (15), 3910-3916 (2001)
   PUBMED   11483494
REFERENCE   10 (residues 1 to 565)
  AUTHORS   Kery,V., Bukovska,G. and Kraus,J.P.
  TITLE     Transsulfuration depends on heme in addition to pyridoxal
            5'-phosphate. Cystathionine beta-synthase is a heme protein
  JOURNAL   J Biol Chem 269 (41), 25283-25288 (1994)
   PUBMED   7929220
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FP236240.8.
            
            On Aug 29, 2017 this sequence version replaced XP_011544396.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments. NM_001354014 is annotated on a
            scaffold that is thought to be a false duplication and thus this
            accession is possibly redundant with other RefSeq accessions.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.175179.1,
                                           SRR3476690.500455.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21p12"
     Protein         1..565
                     /product="cystathionine beta-synthase isoform b"
                     /EC_number="4.2.1.22"
                     /note="cystathionine beta-synthase-like protein"
                     /calculated_mol_wt=61732
     Region          76..558
                     /region_name="cysta_beta"
                     /note="cystathionine beta-synthase; TIGR01137"
                     /db_xref="CDD:273464"
     CDS             1..565
                     /gene="LOC102724560"
                     /gene_synonym="CBSL"
                     /coded_by="NM_001354014.1:261..1958"
                     /note="isoform b is encoded by transcript variant 8"
                     /db_xref="GeneID:102724560"
ORIGIN      
        1 mpsetpqaev gptgcphrsg phsakgslek gspedkeake plwirpdaps rctwqlgrpa
       61 sesphhhtap akspkilpdi lkkigdtpmv rinkigkkfg lkcellakce ffnaggsvkd
      121 rislrmieda erdgtlkpgd tiieptsgnt giglalaaav rgyrciivmp ekmssekvdv
      181 lralgaeivr tptnarfdsp eshvgvawrl kneipnshil dqyrnasnpl ahydttadei
      241 lqqcdgkldm lvasvgtggt itgiarklke kcpgcriigv dpegsilaep eelnqteqtt
      301 yevegigydf iptvldrtvv dkwfksndee aftfarmlia qegllcggsa gstvavavka
      361 aqelqegqrc vvilpdsvrn ymtkflsdrw mlqkgflkee dltekkpwww hlrvqelgls
      421 apltvlptit cghtieilre kgfdqapvvd eagvilgmvt lgnmlsslla gkvqpsdqvg
      481 kviykqfkqi rltdtlgrls hilemdhfal vvheqiqsqd qawagvvggp adhstgkssq
      541 rqmvfgvvta idllnfvaaq erdqk
//
LOCUS       NP_077294                481 aa            linear   PRI 20-JAN-2026
DEFINITION  leukocyte immunoglobulin-like receptor subfamily A member 6 isoform
            1 precursor [Homo sapiens].
ACCESSION   NP_077294 XP_003960831 XP_005276712 XP_006726338 XP_024308293
            XP_047298871
VERSION     NP_077294.3
DBSOURCE    REFSEQ: accession NM_024318.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Bashirova,A.A., Kasprzak,W., O'hUigin,C. and Carrington,M.
  TITLE     Distinct frequency patterns of LILRB3 and LILRA6 allelic variants
            in Europeans
  JOURNAL   Immunogenetics 75 (3), 263-267 (2023)
   PUBMED   36449053
  REMARK    GeneRIF: Distinct frequency patterns of LILRB3 and LILRA6 allelic
            variants in Europeans.
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Al-Moussawy,M., Abdelsamed,H.A. and Lakkis,F.G.
  TITLE     Immunoglobulin-like receptors and the generation of innate immune
            memory
  JOURNAL   Immunogenetics 74 (1), 179-195 (2022)
   PUBMED   35034136
  REMARK    Review article
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Hirayasu,K., Sun,J., Hasegawa,G., Hashikawa,Y., Hosomichi,K.,
            Tajima,A., Tokunaga,K., Ohashi,J. and Hanayama,R.
  TITLE     Characterization of LILRB3 and LILRA6 allelic variants in the
            Japanese population
  JOURNAL   J Hum Genet 66 (7), 739-748 (2021)
   PUBMED   33526815
  REMARK    GeneRIF: Characterization of LILRB3 and LILRA6 allelic variants in
            the Japanese population.
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Lopez-Alvarez,M.R., Jiang,W., Jones,D.C., Jayaraman,J., Johnson,C.,
            Cookson,W.O., Moffatt,M.F., Trowsdale,J. and Traherne,J.A.
  TITLE     LILRA6 copy number variation correlates with susceptibility to
            atopic dermatitis
  JOURNAL   Immunogenetics 68 (9), 743-747 (2016)
   PUBMED   27333811
  REMARK    GeneRIF: LILRA6 copy number variation correlates with
            susceptibility to atopic dermatitis.
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Bashirova,A.A., Apps,R., Vince,N., Mochalova,Y., Yu,X.G. and
            Carrington,M.
  TITLE     Diversity of the human LILRB3/A6 locus encoding a myeloid
            inhibitory and activating receptor pair
  JOURNAL   Immunogenetics 66 (1), 1-8 (2014)
   PUBMED   24096970
  REMARK    GeneRIF: LILRA6 copy number variation may influence the level of
            the activating receptor on the cell surface, potentially affecting
            signaling upon LILRB3/A6 ligation
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Mosbruger,T.L., Duggal,P., Goedert,J.J., Kirk,G.D., Hoots,W.K.,
            Tobler,L.H., Busch,M., Peters,M.G., Rosen,H.R., Thomas,D.L. and
            Thio,C.L.
  TITLE     Large-scale candidate gene analysis of spontaneous clearance of
            hepatitis C virus
  JOURNAL   J Infect Dis 201 (9), 1371-1380 (2010)
   PUBMED   20331378
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 481)
  AUTHORS   Pfistershammer,K., Lawitschka,A., Klauser,C., Leitner,J., Weigl,R.,
            Heemskerk,M.H., Pickl,W.F., Majdic,O., Bohmig,G.A., Fischer,G.F.,
            Greinix,H.T. and Steinberger,P.
  TITLE     Allogeneic disparities in immunoglobulin-like transcript 5 induce
            potent antibody responses in hematopoietic stem cell transplant
            recipients
  JOURNAL   Blood 114 (11), 2323-2332 (2009)
   PUBMED   19617579
  REMARK    GeneRIF: Allogeneic disparities in immunoglobulin-like transcript 5
            induce potent antibody responses in hematopoietic stem cell
            transplant recipients
REFERENCE   8  (residues 1 to 481)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC245052.3.
            
            On or before Mar 2, 2023 this sequence version replaced
            XP_047298871.1, XP_024308293.1, XP_006726338.1, XP_005276712.1,
            NP_077294.2.
            
            Transcript Variant: This variant (1) encodes the supported protein.
            
            CCDS Note: This CCDS representation lacks full-length transcript
            support that is specifically derived from the annotated location.
            The represented exon combination is inferred from a mixture of
            partial best hit transcript alignments and paralogous transcript
            alignments, e.g., from the related LILRA2 locus.
            
            ##Evidence-Data-START##
            Transcript exon combination :: KC918865.1, KC918869.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154529 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396365.7/ ENSP00000379651.2
            RefSeq Select criteria :: based on manual assertion
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..481
                     /product="leukocyte immunoglobulin-like receptor subfamily
                     A member 6 isoform 1 precursor"
                     /note="leukocyte immunoglobulin-like receptor, subfamily B
                     (with TM and ITIM domains), member 6; immunoglobulin-like
                     transcript 8; immunoglobulin-like transcript 5; leukocyte
                     immunoglobulin-like receptor, subfamily A (with TM
                     domain), member 6; leukocyte Ig-like receptor; leucocyte
                     Ig-like receptor A6"
                     /calculated_mol_wt=50155
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2364
     Region          28..116
                     /region_name="IgC2_D1_LILR_KIR_like"
                     /note="First immunoglobulin (Ig)-like domain found in
                     Leukocyte Ig-like receptors (LILRs), Natural killer
                     inhibitory receptors (KIRs) and similar domains; member of
                     Immunoglobulin Constant-2 set of IgSF domains; cd05751"
                     /db_xref="CDD:409409"
     Region          29..33
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409409"
     Region          37..40
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409409"
     Region          43..50
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409409"
     Region          57..62
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409409"
     Site            order(61,99,106)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:409409"
     Region          70..73
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409409"
     Region          82..86
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409409"
     Region          94..100
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409409"
     Region          110..116
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409409"
     Region          123..217
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          140..144
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          152..156
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          179..183
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          193..198
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          211..214
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          224..316
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          241..245
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          253..257
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          279..283
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          293..298
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          310..313
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          326..418
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          341..345
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          353..357
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          379..383
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          393..398
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          411..414
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..481
                     /gene="LILRA6"
                     /gene_synonym="CD85b; ILT-8; ILT5; ILT8; LILRB6"
                     /coded_by="NM_024318.5:40..1485"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS42610.1"
                     /db_xref="GeneID:79168"
                     /db_xref="HGNC:HGNC:15495"
ORIGIN      
        1 mtptlaallc lglslgprth vqagpfpkpt lwaepgsvis wgspvtiwcq gsleaqeyrl
       61 dkegspepwd rnnplepknk arfsipsite hhagryrchy yssagwseps dplelvmtga
      121 yskptlsalp spvvasggnm tlqcgsqkgy hhfvlmkege hqlprtldsq qlhsggfqal
      181 fpvgpvnpsh rwrftcyyyy mntprvwshp sdpleilpsg vsrkpslltl qgpvlapgqs
      241 ltlqcgsdvg ydrfvlykeg erdflqrpgq qpqaglsqan ftlgpvspsh ggqyrcygah
      301 nlssewsaps dplnilmagq iydtvslsaq pgptvasgen vtllcqswwq fdtflltkeg
      361 aahpplrlrs mygahkyqae fpmspvtsah agtyrcygsy ssnphllsfp seplelmvsg
      421 hsggsslppt gppstpasha kdytvenlir mgmaglvlvf lgillfeaqh sqrnpqdaag
      481 r
//
LOCUS       NP_001288638             240 aa            linear   PRI 20-JAN-2026
DEFINITION  pregnancy-specific beta-1-glycoprotein 9 isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001288638 XP_005259136
VERSION     NP_001288638.1
DBSOURCE    REFSEQ: accession NM_001301709.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Kandel,M., MacDonald,T.M., Walker,S.P., Cluver,C., Bergman,L.,
            Myers,J., Hastie,R., Keenan,E., Hannan,N.J., Cannon,P.,
            Nguyen,T.V., Pritchard,N., Tong,S. and Kaitu'u-Lino,T.J.
  TITLE     PSG7 and 9 (Pregnancy-Specific beta-1 Glycoproteins 7 and 9): Novel
            Biomarkers for Preeclampsia
  JOURNAL   J Am Heart Assoc 11 (7), e024536 (2022)
   PUBMED   35322669
  REMARK    GeneRIF: PSG7 and 9 (Pregnancy-Specific beta-1 Glycoproteins 7 and
            9): Novel Biomarkers for Preeclampsia.
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Rong,W., Zhang,Y., Yang,L., Feng,L., Wei,B., Wu,F., Wang,L.,
            Gao,Y., Cheng,S., Wu,J. and Xiao,T.
  TITLE     Post-surgical resection prognostic value of combined OPN, MMP7, and
            PSG9 plasma biomarkers in hepatocellular carcinoma
  JOURNAL   Front Med 13 (2), 250-258 (2019)
   PUBMED   29770948
  REMARK    GeneRIF: Plasma OPN + MMP7 + PSG9 elevation in combination was a
            prognostic factor for overall survival in hepatocellular carcinoma
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Rong,W., Yang,L., Yin,L., Gao,Y., Xiao,T. and Cheng,S.
  TITLE     PSG9 promotes angiogenesis by stimulating VEGFA production and is
            associated with poor prognosis in hepatocellular carcinoma
  JOURNAL   Sci China Life Sci 60 (5), 528-535 (2017)
   PUBMED   28078509
  REMARK    GeneRIF: Results indicate that pregnancy-specific glycoprotein 9
            (PSG9) may facilitate the development of hepatocellular carcinoma
            (HCC) by fostering angiogenesis via promoting VEGFA production in
            cancer HCC.
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Yang,L., Hu,S., Tan,J., Zhang,X., Yuan,W., Wang,Q., Xu,L., Liu,J.,
            Liu,Z., Jia,Y. and Huang,X.
  TITLE     Pregnancy-specific glycoprotein 9 (PSG9), a driver for colorectal
            cancer, enhances angiogenesis via activation of SMAD4
  JOURNAL   Oncotarget 7 (38), 61562-61574 (2016)
   PUBMED   27528036
  REMARK    GeneRIF: Findings illustrate the innovative mechanism by which PSG9
            drives the progression of colorectal cancer and tumor angiogenesis.
            This occurs via nuclear translocation of PSG9/SMAD4, which
            activates angiogenic cytokines.
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Brophy,B.K., MacDonald,R.E., McLenachan,P.A. and Mansfield,B.C.
  TITLE     cDNA sequence of the pregnancy-specific beta 1-glycoprotein-11s
            (PSG-11s)
  JOURNAL   Biochim Biophys Acta 1131 (1), 119-121 (1992)
   PUBMED   1581354
REFERENCE   7  (residues 1 to 240)
  AUTHORS   Chan,W.Y., Zheng,Q.X., McMahon,J. and Tease,L.A.
  TITLE     Characterization of new members of the pregnancy-specific beta
            1-glycoprotein family
  JOURNAL   Mol Cell Biochem 106 (2), 161-170 (1991)
   PUBMED   1922019
REFERENCE   8  (residues 1 to 240)
  AUTHORS   Khan,W.N. and Hammarstrom,S.
  TITLE     Identification of a new carcinoembryonic antigen (CEA) family
            member in human fetal liver--cloning and sequence determination of
            pregnancy-specific glycoprotein 7
  JOURNAL   Biochem Biophys Res Commun 168 (1), 214-225 (1990)
   PUBMED   2328001
REFERENCE   9  (residues 1 to 240)
  AUTHORS   Arakawa,F., Kuroki,M., Misumi,Y., Matsuo,Y. and Matsuoka,Y.
  TITLE     The nucleotide and deduced amino acid sequences of a cDNA encoding
            a new species of pregnancy-specific beta 1-glycoprotein (PS beta G)
  JOURNAL   Biochim Biophys Acta 1048 (2-3), 303-305 (1990)
   PUBMED   2322584
REFERENCE   10 (residues 1 to 240)
  AUTHORS   Thompson,J., Koumari,R., Wagner,K., Barnert,S., Schleussner,C.,
            Schrewe,H., Zimmermann,W., Muller,G., Schempp,W., Zaninetta,D. et
            al.
  TITLE     The human pregnancy-specific glycoprotein genes are tightly linked
            on the long arm of chromosome 19 and are coordinately expressed
  JOURNAL   Biochem Biophys Res Commun 167 (2), 848-859 (1990)
   PUBMED   1690992
  REMARK    Erratum:[Biochem Biophys Res Commun 1990 May 16;168(3):1325]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC380417.1, M34481.1, U25987.1 and BC005925.1.
            
            On Sep 11, 2014 this sequence version replaced XP_005259136.1.
            
            Summary: The protein encoded by this gene is a member of the
            pregnancy-specific glycoprotein (PSG) family. This protein family
            and the closely related carcinoembryonic antigen cell adhesion
            molecule (CEACAM) gene family are both members of the
            immunoglobulin superfamily, and are organized as a large gene
            cluster. This protein is thought to inhibit platelet-fibrinogen
            interactions. Several studies suggest that reduced serum
            concentrations of PSGs are associated with fetal growth
            restrictions, while up-regulation of this gene has been observed in
            colorectal cancers. Several pseudogenes of this gene are found on
            chromosome 19. Alternative splicing results in multiple transcript
            variants that encode multiple protein isoforms. [provided by
            RefSeq, Sep 2014].
            
            Transcript Variant: This variant (4) lacks two consecutive,
            alternate in-frame exons in the coding region, compared to variant
            1. It encodes isoform 4 which is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U25987.1, ERR279867.1338.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162568, SAMN03465410
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..240
                     /product="pregnancy-specific beta-1-glycoprotein 9 isoform
                     4 precursor"
                     /note="pregnancy-specific beta-1 glycoprotein B"
                     /calculated_mol_wt=23394
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3697
     Region          36..138
                     /region_name="IgV_CEACAM_D1"
                     /note="First immunoglobulin (Ig)-like domain of
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM); cd05774"
                     /db_xref="CDD:409430"
     Region          37..55
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          37..39
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409430"
     Region          44..46
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409430"
     Region          49..56
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409430"
     Region          56..63
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..69
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..68
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409430"
     Region          70..91
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          78..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          88..91
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..124
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..103
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409430"
     Region          105..109
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409430"
     Region          119..124
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409430"
     Region          125..132
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          133..138
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409430"
     Region          152..227
                     /region_name="IgC2_CEACAM5-like"
                     /note="Fifth immunoglobulin (Ig)-like domain of the
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule 5 (CEACAM5) and similar domains; member of the
                     C2-set IgSF domains; cd20948"
                     /db_xref="CDD:409540"
     Region          152..158
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409540"
     Region          163..170
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409540"
     Region          176..182
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409540"
     Region          185..190
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409540"
     Region          193..199
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409540"
     Region          202..213
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409540"
     Region          216..227
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409540"
     CDS             1..240
                     /gene="PSG9"
                     /gene_synonym="PS-beta-B; PS-beta-G-9; PS34; PSBG-9;
                     PSG11; PSGII"
                     /coded_by="NM_001301709.2:100..822"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS77311.1"
                     /db_xref="GeneID:5678"
                     /db_xref="HGNC:HGNC:9526"
                     /db_xref="MIM:176398"
ORIGIN      
        1 mgplpapsct qritwkglll tasllnfwnp pttaevtiea qppkvsegkd vlllvhnlpq
       61 nlpgyfwykg emtdlyhyii syivdgkiii ygpaysgret vysnaslliq nvtrkdagty
      121 tlhiikrgde treeirhftf tlyygpdlpr iypsftyyrs genldlscft esnppaeyfw
      181 tingkfqqsg qklfipqitr nhsglyacsv hnsatgkeis ksmtvkvsgp chgdltesqs
//
LOCUS       NP_001347096             481 aa            linear   PRI 20-JAN-2026
DEFINITION  leukocyte immunoglobulin-like receptor subfamily A member 6 isoform
            2 precursor [Homo sapiens].
ACCESSION   NP_001347096 XP_016885726
VERSION     NP_001347096.1
DBSOURCE    REFSEQ: accession NM_001360167.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 481)
  AUTHORS   Bashirova,A.A., Kasprzak,W., O'hUigin,C. and Carrington,M.
  TITLE     Distinct frequency patterns of LILRB3 and LILRA6 allelic variants
            in Europeans
  JOURNAL   Immunogenetics 75 (3), 263-267 (2023)
   PUBMED   36449053
  REMARK    GeneRIF: Distinct frequency patterns of LILRB3 and LILRA6 allelic
            variants in Europeans.
REFERENCE   2  (residues 1 to 481)
  AUTHORS   Al-Moussawy,M., Abdelsamed,H.A. and Lakkis,F.G.
  TITLE     Immunoglobulin-like receptors and the generation of innate immune
            memory
  JOURNAL   Immunogenetics 74 (1), 179-195 (2022)
   PUBMED   35034136
  REMARK    Review article
REFERENCE   3  (residues 1 to 481)
  AUTHORS   Hirayasu,K., Sun,J., Hasegawa,G., Hashikawa,Y., Hosomichi,K.,
            Tajima,A., Tokunaga,K., Ohashi,J. and Hanayama,R.
  TITLE     Characterization of LILRB3 and LILRA6 allelic variants in the
            Japanese population
  JOURNAL   J Hum Genet 66 (7), 739-748 (2021)
   PUBMED   33526815
  REMARK    GeneRIF: Characterization of LILRB3 and LILRA6 allelic variants in
            the Japanese population.
REFERENCE   4  (residues 1 to 481)
  AUTHORS   Lopez-Alvarez,M.R., Jiang,W., Jones,D.C., Jayaraman,J., Johnson,C.,
            Cookson,W.O., Moffatt,M.F., Trowsdale,J. and Traherne,J.A.
  TITLE     LILRA6 copy number variation correlates with susceptibility to
            atopic dermatitis
  JOURNAL   Immunogenetics 68 (9), 743-747 (2016)
   PUBMED   27333811
  REMARK    GeneRIF: LILRA6 copy number variation correlates with
            susceptibility to atopic dermatitis.
REFERENCE   5  (residues 1 to 481)
  AUTHORS   Bashirova,A.A., Apps,R., Vince,N., Mochalova,Y., Yu,X.G. and
            Carrington,M.
  TITLE     Diversity of the human LILRB3/A6 locus encoding a myeloid
            inhibitory and activating receptor pair
  JOURNAL   Immunogenetics 66 (1), 1-8 (2014)
   PUBMED   24096970
  REMARK    GeneRIF: LILRA6 copy number variation may influence the level of
            the activating receptor on the cell surface, potentially affecting
            signaling upon LILRB3/A6 ligation
REFERENCE   6  (residues 1 to 481)
  AUTHORS   Mosbruger,T.L., Duggal,P., Goedert,J.J., Kirk,G.D., Hoots,W.K.,
            Tobler,L.H., Busch,M., Peters,M.G., Rosen,H.R., Thomas,D.L. and
            Thio,C.L.
  TITLE     Large-scale candidate gene analysis of spontaneous clearance of
            hepatitis C virus
  JOURNAL   J Infect Dis 201 (9), 1371-1380 (2010)
   PUBMED   20331378
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 481)
  AUTHORS   Pfistershammer,K., Lawitschka,A., Klauser,C., Leitner,J., Weigl,R.,
            Heemskerk,M.H., Pickl,W.F., Majdic,O., Bohmig,G.A., Fischer,G.F.,
            Greinix,H.T. and Steinberger,P.
  TITLE     Allogeneic disparities in immunoglobulin-like transcript 5 induce
            potent antibody responses in hematopoietic stem cell transplant
            recipients
  JOURNAL   Blood 114 (11), 2323-2332 (2009)
   PUBMED   19617579
  REMARK    GeneRIF: Allogeneic disparities in immunoglobulin-like transcript 5
            induce potent antibody responses in hematopoietic stem cell
            transplant recipients
REFERENCE   8  (residues 1 to 481)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            KC918866.1.
            
            On Jan 27, 2018 this sequence version replaced XP_016885726.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: KC918870.1, KC918874.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2154529
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..481
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..481
                     /product="leukocyte immunoglobulin-like receptor subfamily
                     A member 6 isoform 2 precursor"
                     /note="leukocyte immunoglobulin-like receptor, subfamily B
                     (with TM and ITIM domains), member 6; immunoglobulin-like
                     transcript 8; immunoglobulin-like transcript 5; leukocyte
                     immunoglobulin-like receptor, subfamily A (with TM
                     domain), member 6; leukocyte Ig-like receptor; leucocyte
                     Ig-like receptor A6"
                     /calculated_mol_wt=50035
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2383
     mat_peptide     24..481
                     /product="Leukocyte immunoglobulin-like receptor subfamily
                     A member 6. /id=PRO_0000294367"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PI73.2)"
                     /calculated_mol_wt=50035
     Region          28..116
                     /region_name="IgC2_D1_LILR_KIR_like"
                     /note="First immunoglobulin (Ig)-like domain found in
                     Leukocyte Ig-like receptors (LILRs), Natural killer
                     inhibitory receptors (KIRs) and similar domains; member of
                     Immunoglobulin Constant-2 set of IgSF domains; cd05751"
                     /db_xref="CDD:409409"
     Region          29..33
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409409"
     Region          37..40
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409409"
     Region          43..50
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409409"
     Region          57..62
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409409"
     Region          59..78
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PI73.2)"
     Site            order(61,99,106)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:409409"
     Region          70..73
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409409"
     Region          82..86
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409409"
     Region          94..100
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409409"
     Region          110..116
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409409"
     Region          123..217
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            139
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PI73.2)"
     Region          140..144
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409376"
     Region          152..156
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409376"
     Region          179..183
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409376"
     Region          193..198
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409376"
     Region          211..214
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409376"
     Region          224..316
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          241..245
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409376"
     Region          253..257
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409376"
     Region          279..283
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409376"
     Region          293..298
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409376"
     Site            301
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PI73.2)"
     Region          310..313
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409376"
     Region          326..418
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            340
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PI73.2)"
     Region          341..345
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409376"
     Region          353..357
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409376"
     Region          379..383
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409376"
     Region          393..398
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409376"
     Region          411..414
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409376"
     Region          419..439
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PI73.2)"
     Site            448..468
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PI73.2)"
     CDS             1..481
                     /gene="LILRA6"
                     /gene_synonym="CD85b; ILT-8; ILT5; ILT8; LILRB6"
                     /coded_by="NM_001360167.1:45..1490"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:79168"
                     /db_xref="HGNC:HGNC:15495"
ORIGIN      
        1 mtpaltallc lglslgprtr vqagpfpkpt lwaepgsvis wgspvtiwcq gsleaqeyql
       61 dkegspepld rnnplepknk arfsipsmtq hhagryrchy yssagwseps dplelvmtgf
      121 ynkptlsalp spvvasggnm tlrcgsqkgy hhfvlmkege hqlprtldsq qlhsggfqal
      181 fpvgpvtpsh rwrftcyyyy tntprvwshp sdpleilpsg vsrkpslltl qgpvlapgqs
      241 ltlqcgsdvg ydrfvlykeg erdflqrpgq qpqaglsqan ftlgpvspsh ggqyrcygah
      301 nlssewsaps dplnilmagq iydtvslsaq pgptvasgen vtllcqsrgy fdtflltkeg
      361 aahpplrlrs mygahkyqae fpmspvtsah agtyrcygsy ssnphllsfp seplelmvsg
      421 hsggsslppt gppstpasha kdytvenlir mgmaglvlvf lgillfeaqh sqrnpqdaag
      481 r
//
LOCUS       NP_006855                631 aa            linear   PRI 20-JAN-2026
DEFINITION  leukocyte immunoglobulin-like receptor subfamily B member 3 isoform
            2 precursor [Homo sapiens].
ACCESSION   NP_006855 XP_003960816 XP_003960817 XP_003960818 XP_003960819
            XP_003960820 XP_003960821 XP_003960822 XP_003960823 XP_003960824
            XP_005277284 XP_005277344 XP_011546973
VERSION     NP_006855.3
DBSOURCE    REFSEQ: accession NM_006864.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Hirayasu,K., Khor,S.S., Kawai,Y., Shimada,M., Omae,Y., Hasegawa,G.,
            Hashikawa,Y., Tanimoto,H., Ohashi,J., Hosomichi,K., Tajima,A.,
            Nakamura,H., Nakamura,M., Tokunaga,K., Hanayama,R. and Nagasaki,M.
  TITLE     Identification of the hybrid gene LILRB5-3 by long-read sequencing
            and implication of its novel signaling function
  JOURNAL   Front Immunol 15, 1398935 (2024)
   PUBMED   38807600
  REMARK    GeneRIF: Identification of the hybrid gene LILRB5-3 by long-read
            sequencing and implication of its novel signaling function.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Bashirova,A.A., Kasprzak,W., O'hUigin,C. and Carrington,M.
  TITLE     Distinct frequency patterns of LILRB3 and LILRA6 allelic variants
            in Europeans
  JOURNAL   Immunogenetics 75 (3), 263-267 (2023)
   PUBMED   36449053
  REMARK    GeneRIF: Distinct frequency patterns of LILRB3 and LILRA6 allelic
            variants in Europeans.
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Zhou,J., Wang,Y., Huang,G., Yang,M., Zhu,Y., Jin,C., Jing,D., Ji,K.
            and Shi,Y.
  TITLE     LilrB3 is a putative cell surface receptor of APOE4
  JOURNAL   Cell Res 33 (2), 116-130 (2023)
   PUBMED   36588123
  REMARK    GeneRIF: LilrB3 is a putative cell surface receptor of APOE4.
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Wu,G., Xu,Y., Schultz,R.D., Chen,H., Xie,J., Deng,M., Liu,X.,
            Gui,X., John,S., Lu,Z., Arase,H., Zhang,N., An,Z. and Zhang,C.C.
  TITLE     LILRB3 supports acute myeloid leukemia development and regulates
            T-cell antitumor immune responses through the TRAF2-cFLIP-NF-kappaB
            signaling axis
  JOURNAL   Nat Cancer 2 (11), 1170-1184 (2021)
   PUBMED   35122056
  REMARK    GeneRIF: LILRB3 supports acute myeloid leukemia development and
            regulates T-cell antitumor immune responses through the
            TRAF2-cFLIP-NF-kappaB signaling axis.
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Ayukawa,S., Kamoshita,N., Nakayama,J., Teramoto,R., Pishesha,N.,
            Ohba,K., Sato,N., Kozawa,K., Abe,H., Semba,K., Goda,N., Fujita,Y.
            and Maruyama,T.
  TITLE     Epithelial cells remove precancerous cells by cell competition via
            MHC class I-LILRB3 interaction
  JOURNAL   Nat Immunol 22 (11), 1391-1402 (2021)
   PUBMED   34686865
  REMARK    GeneRIF: Epithelial cells remove precancerous cells by cell
            competition via MHC class I-LILRB3 interaction.
REFERENCE   6  (residues 1 to 631)
  AUTHORS   Bashirova,A.A., Apps,R., Vince,N., Mochalova,Y., Yu,X.G. and
            Carrington,M.
  TITLE     Diversity of the human LILRB3/A6 locus encoding a myeloid
            inhibitory and activating receptor pair
  JOURNAL   Immunogenetics 66 (1), 1-8 (2014)
   PUBMED   24096970
REFERENCE   7  (residues 1 to 631)
  AUTHORS   Colonna,M., Navarro,F., Bellon,T., Llano,M., Garcia,P.,
            Samaridis,J., Angman,L., Cella,M. and Lopez-Botet,M.
  TITLE     A common inhibitory receptor for major histocompatibility complex
            class I molecules on human lymphoid and myelomonocytic cells
  JOURNAL   J Exp Med 186 (11), 1809-1818 (1997)
   PUBMED   9382880
REFERENCE   8  (residues 1 to 631)
  AUTHORS   Arm,J.P., Nwankwo,C. and Austen,K.F.
  TITLE     Molecular identification of a novel family of human Ig superfamily
            members that possess immunoreceptor tyrosine-based inhibition
            motifs and homology to the mouse gp49B1 inhibitory receptor
  JOURNAL   J Immunol 159 (5), 2342-2349 (1997)
   PUBMED   9278324
REFERENCE   9  (residues 1 to 631)
  AUTHORS   Cella,M., Dohring,C., Samaridis,J., Dessing,M., Brockhaus,M.,
            Lanzavecchia,A. and Colonna,M.
  TITLE     A novel inhibitory receptor (ILT3) expressed on monocytes,
            macrophages, and dendritic cells involved in antigen processing
  JOURNAL   J Exp Med 185 (10), 1743-1751 (1997)
   PUBMED   9151699
REFERENCE   10 (residues 1 to 631)
  AUTHORS   Samaridis,J. and Colonna,M.
  TITLE     Cloning of novel immunoglobulin superfamily receptors expressed on
            human myeloid and lymphoid cells: structural evidence for new
            stimulatory and inhibitory pathways
  JOURNAL   Eur J Immunol 27 (3), 660-665 (1997)
   PUBMED   9079806
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA620532.1, AF009633.1,
            BC028153.1 and CA434108.1.
            
            On or before Mar 22, 2015 this sequence version replaced
            XP_011546973.1, XP_005277344.1, NP_006855.2.
            
            Summary: This gene is a member of the leukocyte immunoglobulin-like
            receptor (LIR) family, which is found in a gene cluster at
            chromosomal region 19q13.4. The encoded protein belongs to the
            subfamily B class of LIR receptors which contain two or four
            extracellular immunoglobulin domains, a transmembrane domain, and
            two to four cytoplasmic immunoreceptor tyrosine-based inhibitory
            motifs (ITIMs). The receptor is expressed on immune cells where it
            binds to MHC class I molecules on antigen-presenting cells and
            transduces a negative signal that inhibits stimulation of an immune
            response. It is thought to control inflammatory responses and
            cytotoxicity to help focus the immune response and limit
            autoreactivity. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF009633.1, AK223265.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000445347.2/ ENSP00000388199.2
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..631
                     /product="leukocyte immunoglobulin-like receptor subfamily
                     B member 3 isoform 2 precursor"
                     /note="monocyte inhibitory receptor HL9;
                     immunoglobulin-like transcript 5; CD85 antigen-like family
                     member A; leukocyte immunoglobulin-like receptor,
                     subfamily B (with TM and ITIM domains), member 3;
                     leucocyte Ig-like receptor B3; leukocyte
                     immunoglobulin-like receptor subfamily B member 3"
                     /calculated_mol_wt=67036
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2415
     Region          28..116
                     /region_name="IgC2_D1_LILR_KIR_like"
                     /note="First immunoglobulin (Ig)-like domain found in
                     Leukocyte Ig-like receptors (LILRs), Natural killer
                     inhibitory receptors (KIRs) and similar domains; member of
                     Immunoglobulin Constant-2 set of IgSF domains; cd05751"
                     /db_xref="CDD:409409"
     Region          29..33
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409409"
     Region          37..40
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409409"
     Region          43..50
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409409"
     Region          57..62
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409409"
     Site            order(61,99,106)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:409409"
     Region          70..73
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409409"
     Region          82..86
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409409"
     Region          94..100
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409409"
     Region          110..116
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409409"
     Region          123..217
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          140..144
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409376"
     Region          152..156
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409376"
     Region          179..183
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409376"
     Region          193..198
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409376"
     Region          211..214
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409376"
     Region          224..317
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          241..245
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409376"
     Region          253..257
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409376"
     Region          279..283
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409376"
     Region          293..298
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409376"
     Region          310..313
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409376"
     Region          326..418
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          341..345
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409376"
     Region          353..357
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409376"
     Region          379..383
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409376"
     Region          393..398
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409376"
     Region          411..414
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409376"
     CDS             1..631
                     /gene="LILRB3"
                     /gene_synonym="CD85A; HL9; ILT-5; ILT5; LIR-3; LIR3;
                     PIR-B; PIRB"
                     /coded_by="NM_006864.4:32..1927"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS33105.1"
                     /db_xref="GeneID:11025"
                     /db_xref="HGNC:HGNC:6607"
                     /db_xref="MIM:604820"
ORIGIN      
        1 mtpaltallc lglslgprtr mqagpfpkpt lwaepgsvis wgspvtiwcq gsleaqeyql
       61 dkegspepwd rnnplepknk arfsipsmtq hhagryrchy yssagwseps dplelvmtgf
      121 ynkptlsalp spvvasggnm tlrcgsqkgy hhfvlmkege hqlprtldsq qlhsggfqal
      181 fpvgpvtpsh rwrftcyyyy tntpwvwshp sdpleilpsg vsrkpslltl qgpvlapgqs
      241 ltlqcgsdvg ydrfvlykeg erdflqrpgq qpqaglsqan ftlgpvsrsy ggqyrcygah
      301 nlssewsaps dpldilitgq iydtvslsaq pgptvasgen mtllcqsrgy fdtflltkeg
      361 aahpplrlrs mygahkyqae fpmspvtsah agtyrcygsr ssnphllsfp seplelmvsg
      421 hsggsslppt gppstpglgr ylevligvsv afvlllflll fllllrqrhs khrtsdqrkt
      481 dfqrpagaae tepkdrgllr rsspaadvqe enlyaavkdt qsedrvelds qsphdedpqa
      541 vtyapvkhss prremaspps slsgefldtk drqveedrqm dteaaaseas qdvtyaqlhs
      601 ltlrrkatep ppsqegeppa epsiyatlai h
//
LOCUS       NP_001074919             632 aa            linear   PRI 20-JAN-2026
DEFINITION  leukocyte immunoglobulin-like receptor subfamily B member 3 isoform
            1 precursor [Homo sapiens].
ACCESSION   NP_001074919 XP_005277283 XP_005277343 XP_011546972
VERSION     NP_001074919.2
DBSOURCE    REFSEQ: accession NM_001081450.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Hirayasu,K., Khor,S.S., Kawai,Y., Shimada,M., Omae,Y., Hasegawa,G.,
            Hashikawa,Y., Tanimoto,H., Ohashi,J., Hosomichi,K., Tajima,A.,
            Nakamura,H., Nakamura,M., Tokunaga,K., Hanayama,R. and Nagasaki,M.
  TITLE     Identification of the hybrid gene LILRB5-3 by long-read sequencing
            and implication of its novel signaling function
  JOURNAL   Front Immunol 15, 1398935 (2024)
   PUBMED   38807600
  REMARK    GeneRIF: Identification of the hybrid gene LILRB5-3 by long-read
            sequencing and implication of its novel signaling function.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Bashirova,A.A., Kasprzak,W., O'hUigin,C. and Carrington,M.
  TITLE     Distinct frequency patterns of LILRB3 and LILRA6 allelic variants
            in Europeans
  JOURNAL   Immunogenetics 75 (3), 263-267 (2023)
   PUBMED   36449053
  REMARK    GeneRIF: Distinct frequency patterns of LILRB3 and LILRA6 allelic
            variants in Europeans.
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Zhou,J., Wang,Y., Huang,G., Yang,M., Zhu,Y., Jin,C., Jing,D., Ji,K.
            and Shi,Y.
  TITLE     LilrB3 is a putative cell surface receptor of APOE4
  JOURNAL   Cell Res 33 (2), 116-130 (2023)
   PUBMED   36588123
  REMARK    GeneRIF: LilrB3 is a putative cell surface receptor of APOE4.
REFERENCE   4  (residues 1 to 632)
  AUTHORS   Wu,G., Xu,Y., Schultz,R.D., Chen,H., Xie,J., Deng,M., Liu,X.,
            Gui,X., John,S., Lu,Z., Arase,H., Zhang,N., An,Z. and Zhang,C.C.
  TITLE     LILRB3 supports acute myeloid leukemia development and regulates
            T-cell antitumor immune responses through the TRAF2-cFLIP-NF-kappaB
            signaling axis
  JOURNAL   Nat Cancer 2 (11), 1170-1184 (2021)
   PUBMED   35122056
  REMARK    GeneRIF: LILRB3 supports acute myeloid leukemia development and
            regulates T-cell antitumor immune responses through the
            TRAF2-cFLIP-NF-kappaB signaling axis.
REFERENCE   5  (residues 1 to 632)
  AUTHORS   Ayukawa,S., Kamoshita,N., Nakayama,J., Teramoto,R., Pishesha,N.,
            Ohba,K., Sato,N., Kozawa,K., Abe,H., Semba,K., Goda,N., Fujita,Y.
            and Maruyama,T.
  TITLE     Epithelial cells remove precancerous cells by cell competition via
            MHC class I-LILRB3 interaction
  JOURNAL   Nat Immunol 22 (11), 1391-1402 (2021)
   PUBMED   34686865
  REMARK    GeneRIF: Epithelial cells remove precancerous cells by cell
            competition via MHC class I-LILRB3 interaction.
REFERENCE   6  (residues 1 to 632)
  AUTHORS   Bashirova,A.A., Apps,R., Vince,N., Mochalova,Y., Yu,X.G. and
            Carrington,M.
  TITLE     Diversity of the human LILRB3/A6 locus encoding a myeloid
            inhibitory and activating receptor pair
  JOURNAL   Immunogenetics 66 (1), 1-8 (2014)
   PUBMED   24096970
REFERENCE   7  (residues 1 to 632)
  AUTHORS   Colonna,M., Navarro,F., Bellon,T., Llano,M., Garcia,P.,
            Samaridis,J., Angman,L., Cella,M. and Lopez-Botet,M.
  TITLE     A common inhibitory receptor for major histocompatibility complex
            class I molecules on human lymphoid and myelomonocytic cells
  JOURNAL   J Exp Med 186 (11), 1809-1818 (1997)
   PUBMED   9382880
REFERENCE   8  (residues 1 to 632)
  AUTHORS   Arm,J.P., Nwankwo,C. and Austen,K.F.
  TITLE     Molecular identification of a novel family of human Ig superfamily
            members that possess immunoreceptor tyrosine-based inhibition
            motifs and homology to the mouse gp49B1 inhibitory receptor
  JOURNAL   J Immunol 159 (5), 2342-2349 (1997)
   PUBMED   9278324
REFERENCE   9  (residues 1 to 632)
  AUTHORS   Cella,M., Dohring,C., Samaridis,J., Dessing,M., Brockhaus,M.,
            Lanzavecchia,A. and Colonna,M.
  TITLE     A novel inhibitory receptor (ILT3) expressed on monocytes,
            macrophages, and dendritic cells involved in antigen processing
  JOURNAL   J Exp Med 185 (10), 1743-1751 (1997)
   PUBMED   9151699
REFERENCE   10 (residues 1 to 632)
  AUTHORS   Samaridis,J. and Colonna,M.
  TITLE     Cloning of novel immunoglobulin superfamily receptors expressed on
            human myeloid and lymphoid cells: structural evidence for new
            stimulatory and inhibitory pathways
  JOURNAL   Eur J Immunol 27 (3), 660-665 (1997)
   PUBMED   9079806
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA620532.1, AF009633.1,
            AF009635.1, BC028153.1 and CA434108.1.
            
            On or before Mar 22, 2015 this sequence version replaced
            XP_011546972.1, XP_005277343.1, NP_001074919.1.
            
            Summary: This gene is a member of the leukocyte immunoglobulin-like
            receptor (LIR) family, which is found in a gene cluster at
            chromosomal region 19q13.4. The encoded protein belongs to the
            subfamily B class of LIR receptors which contain two or four
            extracellular immunoglobulin domains, a transmembrane domain, and
            two to four cytoplasmic immunoreceptor tyrosine-based inhibitory
            motifs (ITIMs). The receptor is expressed on immune cells where it
            binds to MHC class I molecules on antigen-presenting cells and
            transduces a negative signal that inhibits stimulation of an immune
            response. It is thought to control inflammatory responses and
            cytotoxicity to help focus the immune response and limit
            autoreactivity. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF009642.1, AF009635.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154529 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..632
                     /product="leukocyte immunoglobulin-like receptor subfamily
                     B member 3 isoform 1 precursor"
                     /note="monocyte inhibitory receptor HL9;
                     immunoglobulin-like transcript 5; CD85 antigen-like family
                     member A; leukocyte immunoglobulin-like receptor,
                     subfamily B (with TM and ITIM domains), member 3;
                     leucocyte Ig-like receptor B3; leukocyte
                     immunoglobulin-like receptor subfamily B member 3"
                     /calculated_mol_wt=67164
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2415
     Region          28..116
                     /region_name="IgC2_D1_LILR_KIR_like"
                     /note="First immunoglobulin (Ig)-like domain found in
                     Leukocyte Ig-like receptors (LILRs), Natural killer
                     inhibitory receptors (KIRs) and similar domains; member of
                     Immunoglobulin Constant-2 set of IgSF domains; cd05751"
                     /db_xref="CDD:409409"
     Region          29..33
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409409"
     Region          37..40
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409409"
     Region          43..50
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409409"
     Region          57..62
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409409"
     Site            order(61,99,106)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:409409"
     Region          70..73
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409409"
     Region          82..86
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409409"
     Region          94..100
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409409"
     Region          110..116
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409409"
     Region          123..217
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          140..144
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          152..156
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          179..183
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          193..198
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          211..214
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          224..317
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          241..245
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          253..257
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          279..283
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          293..298
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          310..313
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          326..418
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          341..345
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          353..357
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          379..383
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          393..398
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          411..414
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..632
                     /gene="LILRB3"
                     /gene_synonym="CD85A; HL9; ILT-5; ILT5; LIR-3; LIR3;
                     PIR-B; PIRB"
                     /coded_by="NM_001081450.3:32..1930"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS46175.1"
                     /db_xref="GeneID:11025"
                     /db_xref="HGNC:HGNC:6607"
                     /db_xref="MIM:604820"
ORIGIN      
        1 mtpaltallc lglslgprtr mqagpfpkpt lwaepgsvis wgspvtiwcq gsleaqeyql
       61 dkegspepwd rnnplepknk arfsipsmtq hhagryrchy yssagwseps dplelvmtgf
      121 ynkptlsalp spvvasggnm tlrcgsqkgy hhfvlmkege hqlprtldsq qlhsggfqal
      181 fpvgpvtpsh rwrftcyyyy tntpwvwshp sdpleilpsg vsrkpslltl qgpvlapgqs
      241 ltlqcgsdvg ydrfvlykeg erdflqrpgq qpqaglsqan ftlgpvsrsy ggqyrcygah
      301 nlssewsaps dpldilitgq iydtvslsaq pgptvasgen mtllcqsrgy fdtflltkeg
      361 aahpplrlrs mygahkyqae fpmspvtsah agtyrcygsr ssnphllsfp seplelmvsg
      421 hsggsslppt gppstpglgr ylevligvsv afvlllflll fllllrqrhs khrtsdqrkt
      481 dfqrpagaae tepkdrgllr rsspaadvqe enlyaavkdt qsedrvelds qqsphdedpq
      541 avtyapvkhs sprremaspp sslsgefldt kdrqveedrq mdteaaasea sqdvtyaqlh
      601 sltlrrkate pppsqegepp aepsiyatla ih
//
LOCUS       NP_001093162             154 aa            linear   PRI 20-JAN-2026
DEFINITION  eukaryotic translation initiation factor 5A-1-like [Homo sapiens].
ACCESSION   NP_001093162 XP_934040
VERSION     NP_001093162.1
DBSOURCE    REFSEQ: accession NM_001099692.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Wu,Y.Y., Wu,G.Q., Cai,N.L., Xu,Y.M. and Lau,A.T.Y.
  TITLE     Comparison of Human Eukaryotic Translation Initiation Factors 5A1
            and 5AL1: Identification of Amino Acid Residues Important for
            EIF5A1 Lysine 50 Hypusination and Its Protein Stability
  JOURNAL   Int J Mol Sci 24 (7), 6067 (2023)
   PUBMED   37047039
  REMARK    GeneRIF: Comparison of Human Eukaryotic Translation Initiation
            Factors 5A1 and 5AL1: Identification of Amino Acid Residues
            Important for EIF5A1 Lysine 50 Hypusination and Its Protein
            Stability.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Zhou,B. and Guo,R.
  TITLE     Integrative analysis of significant RNA-binding proteins in
            colorectal cancer metastasis
  JOURNAL   J Cell Biochem 119 (12), 9730-9741 (2018)
   PUBMED   30132996
  REMARK    GeneRIF: EIF5AL1 expression is associated with colorectal cancer
            metastasis.
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Kim,S.C., Sprung,R., Chen,Y., Xu,Y., Ball,H., Pei,J., Cheng,T.,
            Kho,Y., Xiao,H., Xiao,L., Grishin,N.V., White,M., Yang,X.J. and
            Zhao,Y.
  TITLE     Substrate and functional diversity of lysine acetylation revealed
            by a proteomics survey
  JOURNAL   Mol Cell 23 (4), 607-618 (2006)
   PUBMED   16916647
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Clement,P.M., Johansson,H.E., Wolff,E.C. and Park,M.H.
  TITLE     Differential expression of eIF5A-1 and eIF5A-2 in human cancer
            cells
  JOURNAL   FEBS J 273 (6), 1102-1114 (2006)
   PUBMED   16519677
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Facchiano,A.M., Stiuso,P., Chiusano,M.L., Caraglia,M., Giuberti,G.,
            Marra,M., Abbruzzese,A. and Colonna,G.
  TITLE     Homology modelling of the human eukaryotic initiation factor 5A
            (eIF-5A)
  JOURNAL   Protein Eng 14 (11), 881-890 (2001)
   PUBMED   11742107
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Koettnitz,K., Wohl,T., Kappel,B., Lottspeich,F., Hauber,J. and
            Bevec,D.
  TITLE     Identification of a new member of the human eIF-5A gene family
  JOURNAL   Gene 159 (2), 283-284 (1995)
   PUBMED   7622067
REFERENCE   7  (residues 1 to 154)
  AUTHORS   Steinkasserer,A., Jones,T., Sheer,D., Koettnitz,K., Hauber,J. and
            Bevec,D.
  TITLE     The eukaryotic cofactor for the human immunodeficiency virus type 1
            (HIV-1) rev protein, eIF-5A, maps to chromosome 17p12-p13: three
            eIF-5A pseudogenes map to 10q23.3, 17q25, and 19q13.2
  JOURNAL   Genomics 25 (3), 749-752 (1995)
   PUBMED   7759117
REFERENCE   8  (residues 1 to 154)
  AUTHORS   Koettnitz,K., Kappel,B., Baumruker,T., Hauber,J. and Bevec,D.
  TITLE     The genomic structure encoding human initiation factor eIF-5A
  JOURNAL   Gene 144 (2), 249-252 (1994)
   PUBMED   7545941
REFERENCE   9  (residues 1 to 154)
  AUTHORS   Smit-McBride,Z., Dever,T.E., Hershey,J.W. and Merrick,W.C.
  TITLE     Sequence determination and cDNA cloning of eukaryotic initiation
            factor 4D, the hypusine-containing protein
  JOURNAL   J Biol Chem 264 (3), 1578-1583 (1989)
   PUBMED   2492279
REFERENCE   10 (residues 1 to 154)
  AUTHORS   Park,M.H., Liu,T.Y., Neece,S.H. and Swiggard,W.J.
  TITLE     Eukaryotic initiation factor 4D. Purification from human red blood
            cells and the sequence of amino acids around its single hypusine
            residue
  JOURNAL   J Biol Chem 261 (31), 14515-14519 (1986)
   PUBMED   3095320
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL133481.14.
            
            On Jul 26, 2007 this sequence version replaced XP_934040.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC070048.1, BX400276.2 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000520547.4/ ENSP00000430706.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.3"
     Protein         1..154
                     /product="eukaryotic translation initiation factor
                     5A-1-like"
                     /calculated_mol_wt=16642
     Region          1..150
                     /region_name="PLN03107"
                     /note="eukaryotic translation initiation factor 5A;
                     Provisional"
                     /db_xref="CDD:215580"
     CDS             1..154
                     /gene="EIF5AL1"
                     /gene_synonym="EIF5AP1"
                     /coded_by="NM_001099692.2:118..582"
                     /db_xref="CCDS:CCDS53546.1"
                     /db_xref="GeneID:143244"
                     /db_xref="HGNC:HGNC:17419"
ORIGIN      
        1 maddldfetg dagasatfpm qcsalrkngf vvlkgwpcki vemsasktgk hghakvhlvg
       61 idiftgkkye dicpsthnmd vpnikrndfq ligiqdgyls llqdsgevpe dlrlpegdlg
      121 keieqkydcg eeilitvlsa mteeaavaik amak
//
LOCUS       NP_001186284             228 aa            linear   PRI 20-JAN-2026
DEFINITION  RPL17-C18orf32 protein isoform 1 [Homo sapiens].
ACCESSION   NP_001186284
VERSION     NP_001186284.1
DBSOURCE    REFSEQ: accession NM_001199355.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Prakash,T., Sharma,V.K., Adati,N., Ozawa,R., Kumar,N., Nishida,Y.,
            Fujikake,T., Takeda,T. and Taylor,T.D.
  TITLE     Expression of conjoined genes: another mechanism for gene
            regulation in eukaryotes
  JOURNAL   PLoS One 5 (10), e13284 (2010)
   PUBMED   20967262
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX393840.2 and AC100778.5.
            
            Summary: This locus represents naturally occurring read-through
            transcription between the neighboring RPL17 (ribosomal protein L17)
            and C18orf32 (chromosome 18 open reading frame 32) genes.
            Alternative splicing results in multiple transcript variants. The
            encoded isoforms share sequence identity with the RPL17 protein,
            but they include frameshifted C-terminal regions derived from the
            downstream gene exons. [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript but encodes the longer isoform (1). The 5' UTR of this
            variant is incomplete due to lack of full-length transcript support
            for this exon combination, and the presence of ambiguous splicing
            in the 5' region.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.391157.1,
                                           SRR1163657.19400.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267778 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            readthrough transcript :: includes exons from GeneID 6139, 497661
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..228
                     /product="RPL17-C18orf32 protein isoform 1"
                     /note="60S ribosomal protein L17; 60S ribosomal protein
                     L23; Large ribosomal subunit protein uL22"
                     /calculated_mol_wt=26242
     Region          1..175
                     /region_name="PTZ00178"
                     /note="60S ribosomal protein L17; Provisional"
                     /db_xref="CDD:240306"
     Site            order(15..16,38..40,42..43,45..46,99..104,112..117,
                     149..150)
                     /site_type="active"
                     /note="putative translocon binding site [active]"
                     /db_xref="CDD:238205"
     Site            order(18,20,23,25..27,30,34,37,97,101,104,116,118..120,
                     122,125,137..142)
                     /site_type="other"
                     /note="protein-rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238205"
     CDS             1..228
                     /gene="RPL17-C18orf32"
                     /gene_synonym="PD-1"
                     /coded_by="NM_001199355.1:14..700"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:100526842"
                     /db_xref="HGNC:HGNC:44661"
ORIGIN      
        1 mvrysldpen ptkscksrgs nlrvhfkntr etaqaikgmh irkatkylkd vtlqkqcvpf
       61 rrynggvgrc aqakqwgwtq grwpkksaef llhmlknaes naelkgldvd slviehiqvn
      121 kapkmrrrty rahgrinpym sspchiemil tekeqivpkp eeevaqkkkl rssslgkwca
      181 flvssfqfcs gstknswshi ytlwfppslv vyglrkqykn pmiqtkak
//
LOCUS       NP_001335315             516 aa            linear   PRI 20-JAN-2026
DEFINITION  cytochrome P450 2D7 [Homo sapiens].
ACCESSION   NP_001335315
VERSION     NP_001335315.1
DBSOURCE    REFSEQ: accession NM_001348386.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 516)
  AUTHORS   Zhang,W., Wan,P., Zhang,M., Chang,Y., Du,S., Jin,T. and Wang,Y.
  TITLE     Association Between CYP2D7 and TCF20 Polymorphisms and Coronary
            Heart Disease
  JOURNAL   Cardiovasc Toxicol 24 (10), 1037-1046 (2024)
   PUBMED   39060884
  REMARK    GeneRIF: Association Between CYP2D7 and TCF20 Polymorphisms and
            Coronary Heart Disease.
REFERENCE   2  (residues 1 to 516)
  AUTHORS   Jukic,M.M., Lauschke,V.M., Saito,T., Hiratsuka,M. and
            Ingelman-Sundberg,M.
  TITLE     Functional characterization of CYP2D7 gene variants
  JOURNAL   Pharmacogenomics 19 (12), 931-936 (2018)
   PUBMED   30040020
  REMARK    GeneRIF: The loss of the stop codon in CYP2D7 does not result in
            the generation of enzymatically active protein in human liver.
REFERENCE   3  (residues 1 to 516)
  AUTHORS   Nofziger,C. and Paulmichl,M.
  TITLE     Accurately genotyping CYP2D6: not for the faint of heart
  JOURNAL   Pharmacogenomics 19 (13), 999-1002 (2018)
   PUBMED   30020016
REFERENCE   4  (residues 1 to 516)
  AUTHORS   Wang,J., Xie,H., Ling,Q., Lu,D., Lv,Z., Zhuang,R., Liu,Z., Wei,X.,
            Zhou,L., Xu,X. and Zheng,S.
  TITLE     Coding-noncoding gene expression in intrahepatic cholangiocarcinoma
  JOURNAL   Transl Res 168, 107-121 (2016)
   PUBMED   26297049
REFERENCE   5  (residues 1 to 516)
  AUTHORS   Gaedigk,A., Twist,G.P. and Leeder,J.S.
  TITLE     CYP2D6, SULT1A1 and UGT2B17 copy number variation: quantitative
            detection by multiplex PCR
  JOURNAL   Pharmacogenomics 13 (1), 91-111 (2012)
   PUBMED   22111604
REFERENCE   6  (residues 1 to 516)
  AUTHORS   Zhang,W.Y., Tu,Y.B., Haining,R.L. and Yu,A.M.
  TITLE     Expression and functional analysis of CYP2D6.24, CYP2D6.26,
            CYP2D6.27, and CYP2D7 isozymes
  JOURNAL   Drug Metab Dispos 37 (1), 1-4 (2009)
   PUBMED   18838503
REFERENCE   7  (residues 1 to 516)
  AUTHORS   Pai,H.V., Kommaddi,R.P., Chinta,S.J., Mori,T., Boyd,M.R. and
            Ravindranath,V.
  TITLE     A frameshift mutation and alternate splicing in human brain
            generate a functional form of the pseudogene cytochrome P4502D7
            that demethylates codeine to morphine
  JOURNAL   J Biol Chem 279 (26), 27383-27389 (2004)
   PUBMED   15051713
REFERENCE   8  (residues 1 to 516)
  AUTHORS   Heim,M.H. and Meyer,U.A.
  TITLE     Evolution of a highly polymorphic human cytochrome P450 gene
            cluster: CYP2D6
  JOURNAL   Genomics 14 (1), 49-58 (1992)
   PUBMED   1358797
REFERENCE   9  (residues 1 to 516)
  AUTHORS   Gough,A.C., Miles,J.S., Spurr,N.K., Moss,J.E., Gaedigk,A.,
            Eichelbaum,M. and Wolf,C.R.
  TITLE     Identification of the primary gene defect at the cytochrome P450
            CYP2D locus
  JOURNAL   Nature 347 (6295), 773-776 (1990)
   PUBMED   1978251
REFERENCE   10 (residues 1 to 516)
  AUTHORS   Gonzalez,F.J., Skoda,R.C., Kimura,S., Umeno,M., Zanger,U.M.,
            Nebert,D.W., Gelboin,H.V., Hardwick,J.P. and Meyer,U.A.
  TITLE     Characterization of the common genetic defect in humans deficient
            in debrisoquine metabolism
  JOURNAL   Nature 331 (6155), 442-446 (1988)
   PUBMED   3123997
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY220845.1, BC108679.1, AC254562.1 and X16866.1.
            
            Summary: This gene is a member of the cytochrome P450 gene
            superfamily. The cytochrome P450 proteins are monooxygenases which
            catalyze many reactions involved in drug metabolism and synthesis
            of cholesterol, steroids and other lipids. This gene is a
            segregating pseudogene, where some individuals may have an allele
            that encodes a functional enzyme, while other individuals have an
            allele encoding a protein that is predicted to be non-functional.
            In this case, the functional allele is thought to be rare. This
            locus is part of a cluster of cytochrome P450 genes on chromosome
            22. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (3) uses an alternate splice site
            resulting in a longer transcript compared to variant 1. This
            variant represents the allele which encodes the full-length protein
            but whether this protein has enzymatic activity is disputed.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY220845.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154529, SAMEA2155628
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            polymorphic pseudogene :: PMID: 15051713
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..516
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..516
                     /product="cytochrome P450 2D7"
                     /EC_number="1.14.14.1"
                     /note="cytochrome P450, subfamily IID (debrisoquine,
                     sparteine, etc., -metabolizing) cluster; cytochrome P450,
                     subfamily II (debrisoquine, sparteine, etc.,
                     -metabolising), polypeptide 7 pseudogene 1; cytochrome
                     P450, family 2, subfamily D, polypeptide 7 pseudogene 1;
                     Putative cytochrome P450 2D7"
                     /calculated_mol_wt=57445
     Site            3..23
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A087X1C5.1)"
     Region          65..511
                     /region_name="CYP2D"
                     /note="cytochrome P450 family 2, subfamily D; cd20663"
                     /db_xref="CDD:410756"
     Site            order(101,119..120,128,132,302,305..306,309..310,313,383,
                     393,395,418,454..456,460,462..464,467)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410756"
     Site            order(110,120,212..213,216,244,247..248,300..301,304..305,
                     309,502)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410756"
     Site            302..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot
                     (A0A087X1C5.1)"
     Site            417
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (A0A087X1C5.1)"
     CDS             1..516
                     /gene="CYP2D7"
                     /gene_synonym="CYP2D; CYP2D7AP; CYP2D7P; CYP2D7P1; CYP2D@;
                     P450C2D; P450DB1; RNA40057"
                     /coded_by="NM_001348386.3:20..1570"
                     /db_xref="GeneID:1564"
                     /db_xref="HGNC:HGNC:2624"
ORIGIN      
        1 mglealvpla mivaiflllv dlmhrhqrwa aryppgplpl pglgnllhvd fqntpycfdq
       61 lrrrfgdvfs lqlawtpvvv lnglaavrea mvtrgedtad rppapiyqvl gfgprsqgvi
      121 lsrygpawre qrrfsvstlr nlglgkksle qwvteeaacl caafadqagr pfrpnglldk
      181 avsnviaslt cgrrfeyddp rflrlldlaq eglkeesgfl revlnavpvl phipalagkv
      241 lrfqkafltq ldelltehrm twdpaqpprd lteaflakke kakgspessf ndenlrivvg
      301 nlflagmvtt sttlawglll milhldvqrg rrvspgcspi vgthvcpvrv qqeiddvigq
      361 vrrpemgdqa hmpcttavih evqhfgdivp lgvthmtsrd ievqgfripk gttlitnlss
      421 vlkdeavwkk pfrfhpehfl daqghfvkpe aflpfsagrr aclgeplarm elflfftsll
      481 qhfsfsvaag qprpshsrvv sflvtpspye lcavpr
//
LOCUS       NP_001003799              58 aa            linear   PRI 20-JAN-2026
DEFINITION  T-cell receptor gamma alternate reading frame protein isoform 1
            [Homo sapiens].
ACCESSION   NP_001003799
VERSION     NP_001003799.1
DBSOURCE    REFSEQ: accession NM_001003799.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 58)
  AUTHORS   Shi,Y., He,Z., Bei,L., Tao,H., Ding,B., Tao,S., Wang,C. and Yu,L.
  TITLE     High expression of TARP correlates with inferior FLT3 mutations in
            non-adolescents and young adults with acute myeloid leukaemia
  JOURNAL   Hematology 26 (1), 380-387 (2021)
   PUBMED   33971801
  REMARK    GeneRIF: High expression of TARP correlates with inferior FLT3
            mutations in non-adolescents and young adults with acute myeloid
            leukaemia.
REFERENCE   2  (residues 1 to 58)
  AUTHORS   Depreter,B., Weening,K.E., Vandepoele,K., Essand,M., De
            Moerloose,B., Themeli,M., Cloos,J., Hanekamp,D., Moors,I.,
            D'hont,I., Denys,B., Uyttebroeck,A., Van Damme,A., Dedeken,L.,
            Snauwaert,S., Goetgeluk,G., De Munter,S., Kerre,T.,
            Vandekerckhove,B., Lammens,T. and Philippe,J.
  TITLE     TARP is an immunotherapeutic target in acute myeloid leukemia
            expressed in the leukemic stem cell compartment
  JOURNAL   Haematologica 105 (5), 1306-1316 (2020)
   PUBMED   31371409
REFERENCE   3  (residues 1 to 58)
  AUTHORS   Yue,H., Cai,Y., Song,Y., Meng,L., Chen,X., Wang,M., Bian,Z. and
            Wang,R.
  TITLE     Elevated TARP promotes proliferation and metastasis of salivary
            adenoid cystic carcinoma
  JOURNAL   Oral Surg Oral Med Oral Pathol Oral Radiol 123 (4), 468-476 (2017)
   PUBMED   28153567
REFERENCE   4  (residues 1 to 58)
  AUTHORS   Zhao,L.J., Li,X.P., Qi,W.J., Wang,J.L. and Wei,L.H.
  TITLE     Value of T cell receptor gamma alternate reading frame protein and
            keratin 5 in endometrial carcinoma
  JOURNAL   Chin Med J (Engl) 126 (22), 4260-4264 (2013)
   PUBMED   24238509
  REMARK    GeneRIF: The expression of TARP and KRT5 was correlated with the
            progress of endometrial cancer
REFERENCE   5  (residues 1 to 58)
  AUTHORS   Maeda,H., Nagata,S., Wolfgang,C.D., Bratthauer,G.L., Bera,T.K. and
            Pastan,I.
  TITLE     The T cell receptor gamma chain alternate reading frame protein
            (TARP), a prostate-specific protein localized in mitochondria
  JOURNAL   J Biol Chem 279 (23), 24561-24568 (2004)
   PUBMED   15150260
REFERENCE   6  (residues 1 to 58)
  AUTHORS   Wolfgang,C.D., Essand,M., Vincent,J.J., Lee,B. and Pastan,I.
  TITLE     TARP: a nuclear protein expressed in prostate and breast cancer
            cells derived from an alternate reading frame of the T cell
            receptor gamma chain locus
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9437-9442 (2000)
   PUBMED   10931945
REFERENCE   7  (residues 1 to 58)
  AUTHORS   Mami-Chouaib,F., Del Porto,P., Delorme,D. and Hercend,T.
  TITLE     Further evidence for a gamma/delta T cell receptor-mediated
            TCT.1/CD48 recognition
  JOURNAL   J Immunol 147 (9), 2864-2867 (1991)
   PUBMED   1655899
REFERENCE   8  (residues 1 to 58)
  AUTHORS   Tighe,L., Forster,A., Clark,D.M., Boylston,A.W., Lavenir,I. and
            Rabbitts,T.H.
  TITLE     Unusual forms of T cell gamma mRNA in a human T cell leukemia cell
            line: implications for gamma gene expression
  JOURNAL   Eur J Immunol 17 (12), 1729-1736 (1987)
   PUBMED   2961573
REFERENCE   9  (residues 1 to 58)
  AUTHORS   Krangel,M.S., Band,H., Hata,S., McLean,J. and Brenner,M.B.
  TITLE     Structurally divergent human T cell receptor gamma proteins encoded
            by distinct C gamma genes
  JOURNAL   Science 237 (4810), 64-67 (1987)
   PUBMED   2955517
REFERENCE   10 (residues 1 to 58)
  AUTHORS   Yoshikai,Y., Toyonaga,B., Koga,Y., Kimura,N., Griesser,H. and
            Mak,T.W.
  TITLE     Repertoire of the human T cell gamma genes: high frequency of
            nonfunctional transcripts in thymus and mature T cells
  JOURNAL   Eur J Immunol 17 (1), 119-126 (1987)
   PUBMED   2949984
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF151103.1 and BF674593.1.
            
            Summary: In some non-lymphoid tissues, the unrearranged T cell
            receptor gamma (TRG@) locus is expressed. The resulting transcript
            contains a subset of the TRG@ gene segments and is shorter than
            TRG@ transcripts expressed in lymphoid tissues. This RefSeq record
            represents the unrearranged TRG@ locus transcript; the complete
            TRG@ locus is represented by the genomic RefSeq NG_001336. The
            transcript represented by this RefSeq has two open reading frames
            (ORFs) that encode different proteins. The downstream ORF is in the
            same frame as TRG@ and its protein product is similar to TRG@
            proteins. The upstream ORF uses a different reading frame and
            encodes a novel protein. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) uses the upstream ORF. The
            resulting protein (isoform 1) localizes to the outer mitochondrial
            membrane.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF151103.1, BF679123.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153427 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000698248.1/
                                                  ENSP00000513628.1
            NMD candidate                      :: PMID: 10931945, 15150260
            RefSeq Select criteria             :: based on manual assertion,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..58
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.1"
     Protein         1..58
                     /product="T-cell receptor gamma alternate reading frame
                     protein isoform 1"
                     /note="TCR- gamma V-IV; antigen, T-cell receptor"
                     /calculated_mol_wt=7030
     CDS             1..58
                     /gene="TARP"
                     /coded_by="NM_001003799.2:63..239"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS94087.1"
                     /db_xref="GeneID:445347"
                     /db_xref="MIM:609642"
ORIGIN      
        1 mqmfppsplf fflqllkqss rrlehtfvfl rnfslmllry igkkrratrf wdprrgtp
//
LOCUS       NP_002479                 99 aa            linear   PRI 20-JAN-2026
DEFINITION  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
            isoform 1 [Homo sapiens].
ACCESSION   NP_002479
VERSION     NP_002479.1
DBSOURCE    REFSEQ: accession NM_002488.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Signes,A. and Fernandez-Vizarra,E.
  TITLE     Assembly of mammalian oxidative phosphorylation complexes I-V and
            supercomplexes
  JOURNAL   Essays Biochem 62 (3), 255-270 (2018)
   PUBMED   30030361
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Perrier,S., Gauquelin,L., Tetreault,M., Tran,L.T., Webb,N.,
            Srour,M., Mitchell,J.J., Brunel-Guitton,C., Majewski,J., Long,V.,
            Keller,S., Gambello,M.J., Simons,C., Vanderver,A. and Bernard,G.
  CONSRTM   Care4Rare Canada Consortium
  TITLE     Recessive mutations in NDUFA2 cause mitochondrial
            leukoencephalopathy
  JOURNAL   Clin Genet 93 (2), 396-400 (2018)
   PUBMED   28857146
  REMARK    GeneRIF: Review of a biorepository of patients with unsolved
            genetic leukoencephalopathies who underwent whole-exome or genome
            sequencing allowed us to identify a second patient with compound
            heterozygous mutations in NDUFA2. Only 1 other patient with
            mutations in NDUFA2 and a different phenotype (Leigh syndrome) has
            previously been reported. This is the first report of cystic
            leukoencephalopathy caused by mutations in NDUFA2.
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Hoefs,S.J., Dieteren,C.E., Distelmaier,F., Janssen,R.J., Epplen,A.,
            Swarts,H.G., Forkink,M., Rodenburg,R.J., Nijtmans,L.G.,
            Willems,P.H., Smeitink,J.A. and van den Heuvel,L.P.
  TITLE     NDUFA2 complex I mutation leads to Leigh disease
  JOURNAL   Am J Hum Genet 82 (6), 1306-1315 (2008)
   PUBMED   18513682
REFERENCE   5  (residues 1 to 99)
  AUTHORS   Brockmann,C., Diehl,A., Rehbein,K., Strauss,H., Schmieder,P.,
            Korn,B., Kuhne,R. and Oschkinat,H.
  TITLE     The oxidized subunit B8 from human complex I adopts a thioredoxin
            fold
  JOURNAL   Structure 12 (9), 1645-1654 (2004)
   PUBMED   15341729
  REMARK    GeneRIF: solution structure shows a thioredoxin fold with highest
            similarities to the human thioredoxin mutant C73S and thioredoxin 2
            from Anabeana sp
REFERENCE   6  (residues 1 to 99)
  AUTHORS   Murray,J., Zhang,B., Taylor,S.W., Oglesbee,D., Fahy,E.,
            Marusich,M.F., Ghosh,S.S. and Capaldi,R.A.
  TITLE     The subunit composition of the human NADH dehydrogenase obtained by
            rapid one-step immunopurification
  JOURNAL   J Biol Chem 278 (16), 13619-13622 (2003)
   PUBMED   12611891
REFERENCE   7  (residues 1 to 99)
  AUTHORS   Loeffen,J.L., Triepels,R.H., van den Heuvel,L.P., Schuelke,M.,
            Buskens,C.A., Smeets,R.J., Trijbels,J.M. and Smeitink,J.A.
  TITLE     cDNA of eight nuclear encoded subunits of NADH:ubiquinone
            oxidoreductase: human complex I cDNA characterization completed
  JOURNAL   Biochem Biophys Res Commun 253 (2), 415-422 (1998)
   PUBMED   9878551
REFERENCE   8  (residues 1 to 99)
  AUTHORS   Emahazion,T. and Brookes,A.J.
  TITLE     Mapping of the NDUFA2, NDUFA6, NDUFA7, NDUFB8, and NDUFS8 electron
            transport chain genes by intron based radiation hybrid mapping
  JOURNAL   Cytogenet Cell Genet 82 (1-2), 114 (1998)
   PUBMED   9763676
REFERENCE   9  (residues 1 to 99)
  AUTHORS   Ton,C., Hwang,D.M., Dempsey,A.A. and Liew,C.C.
  TITLE     Identification and primary structure of five human NADH-ubiquinone
            oxidoreductase subunits
  JOURNAL   Biochem Biophys Res Commun 241 (2), 589-594 (1997)
   PUBMED   9425316
REFERENCE   10 (residues 1 to 99)
  AUTHORS   Rahman,S., Thorburn,D.R. and Ball,M.
  TITLE     Nuclear Gene-Encoded Leigh Syndrome Spectrum Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26425749
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC003674.1, AA993683.1 and
            AC116353.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The encoded protein is a subunit of the hydrophobic
            protein fraction of the NADH:ubiquinone oxidoreductase (complex 1),
            the first enzyme complex in the electron transport chain located in
            the inner mitochondrial membrane, and may be involved in regulating
            complex I activity or its assembly via assistance in redox
            processes. Mutations in this gene are associated with Leigh
            syndrome, an early-onset progressive neurodegenerative disorder.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (1) represents the shortest
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC003674.1, BJ995924.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000252102.9/
                                                  ENSP00000252102.5
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.3"
     Protein         1..99
                     /product="NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex subunit 2 isoform 1"
                     /EC_number="7.1.1.2"
                     /note="NADH-ubiquinone oxidoreductase subunit CI-B8;
                     complex I B8 subunit; NADH dehydrogenase (ubiquinone) 1
                     alpha subcomplex, 2, 8kDa"
                     /calculated_mol_wt=10790
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O43678.3)"
     Region          28..97
                     /region_name="L51_S25_CI-B8"
                     /note="Mitochondrial ribosomal protein L51 / S25 / CI-B8
                     domain; smart00916"
                     /db_xref="CDD:197984"
     Site            64
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CQ75; propagated from
                     UniProtKB/Swiss-Prot (O43678.3)"
     CDS             1..99
                     /gene="NDUFA2"
                     /gene_synonym="B8; CIB8; MC1DN13"
                     /coded_by="NM_002488.5:48..347"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4234.1"
                     /db_xref="GeneID:4695"
                     /db_xref="HGNC:HGNC:7685"
                     /db_xref="MIM:602137"
ORIGIN      
        1 maaaaasrgv gaklglreir ihlcqrspgs qgvrdfiekr yvelkkanpd lpilirecsd
       61 vqpklwarya fgqetnvpln nfsadqvtra lenvlsgka
//
LOCUS       NP_001263424             326 aa            linear   PRI 20-JAN-2026
DEFINITION  pregnancy-specific beta-1-glycoprotein 4 isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_001263424
VERSION     NP_001263424.1
DBSOURCE    REFSEQ: accession NM_001276495.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Shanley,D.K., Kiely,P.A., Golla,K., Allen,S., Martin,K.,
            O'Riordan,R.T., Ball,M., Aplin,J.D., Singer,B.B., Caplice,N.,
            Moran,N. and Moore,T.
  TITLE     Pregnancy-specific glycoproteins bind integrin alphaIIbbeta3 and
            inhibit the platelet-fibrinogen interaction
  JOURNAL   PLoS One 8 (2), e57491 (2013)
   PUBMED   23469002
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kimoto,Y.
  TITLE     A single human cell expresses all messenger ribonucleic acids: the
            arrow of time in a cell
  JOURNAL   Mol Gen Genet 258 (3), 233-239 (1998)
   PUBMED   9645429
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Teglund,S., Olsen,A., Khan,W.N., Frangsmyr,L. and Hammarstrom,S.
  TITLE     The pregnancy-specific glycoprotein (PSG) gene cluster on human
            chromosome 19: fine structure of the 11 PSG genes and
            identification of 6 new genes forming a third subgroup within the
            carcinoembryonic antigen (CEA) family
  JOURNAL   Genomics 23 (3), 669-684 (1994)
   PUBMED   7851896
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Olsen,A., Teglund,S., Nelson,D., Gordon,L., Copeland,A.,
            Georgescu,A., Carrano,A. and Hammarstrom,S.
  TITLE     Gene organization of the pregnancy-specific glycoprotein region on
            human chromosome 19: assembly and analysis of a 700-kb cosmid
            contig spanning the region
  JOURNAL   Genomics 23 (3), 659-668 (1994)
   PUBMED   7851895
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Pan,C.J., Chamberlin,M.E., Wu,S.M., Chan,W.Y. and Chou,J.Y.
  TITLE     Pregnancy-specific glycoprotein gene expression and the induction
            by 5-bromo-2'-deoxyuridine
  JOURNAL   Biochemistry 33 (23), 7260-7266 (1994)
   PUBMED   8003489
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Chan,W.Y., Zheng,Q.X., McMahon,J. and Tease,L.A.
  TITLE     Characterization of new members of the pregnancy-specific beta
            1-glycoprotein family
  JOURNAL   Mol Cell Biochem 106 (2), 161-170 (1991)
   PUBMED   1922019
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Barnett,T.R., Pickle,W. 2nd and Elting,J.J.
  TITLE     Characterization of two new members of the pregnancy-specific beta
            1-glycoprotein family from the myeloid cell line KG-1 and
            suggestion of two distinct classes of transcription unit
  JOURNAL   Biochemistry 29 (44), 10213-10218 (1990)
   PUBMED   2271648
REFERENCE   8  (residues 1 to 326)
  AUTHORS   .
  TITLE     The human pregnancy-specific glycoprotein genes are tightly linked
            on the long arm of chromosome 19 and are coordinately expressed
  JOURNAL   Biochem Biophys Res Commun 168 (3), 1325 (1990)
   PUBMED   2346490
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Thompson,J., Koumari,R., Wagner,K., Barnert,S., Schleussner,C.,
            Schrewe,H., Zimmermann,W., Muller,G., Schempp,W., Zaninetta,D. et
            al.
  TITLE     The human pregnancy-specific glycoprotein genes are tightly linked
            on the long arm of chromosome 19 and are coordinately expressed
  JOURNAL   Biochem Biophys Res Commun 167 (2), 848-859 (1990)
   PUBMED   1690992
  REMARK    Erratum:[Biochem Biophys Res Commun 1990 May 16;168(3):1325]
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Thompson,J.A., Mauch,E.M., Chen,F.S., Hinoda,Y., Schrewe,H.,
            Berling,B., Barnert,S., von Kleist,S., Shively,J.E. and
            Zimmermann,W.
  TITLE     Analysis of the size of the carcinoembryonic antigen (CEA) gene
            family: isolation and sequencing of N-terminal domain exons
  JOURNAL   Biochem Biophys Res Commun 158 (3), 996-1004 (1989)
   PUBMED   2537643
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005392.2, AK075149.1 and
            BC008405.1.
            
            Summary: The protein encoded by this gene is a pregnancy-specific
            glycoprotein (PSG), one of several encoded by a cluster of similar
            genes on chromosome 19. This gene is a member of the
            carcinoembryonic antigen (CEA) gene family and may play a role in
            regulation of the innate immune system. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (3) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK075149.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162568 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..326
                     /product="pregnancy-specific beta-1-glycoprotein 4 isoform
                     3 precursor"
                     /note="Pregnancy-specific beta-1-glycoprotein-4;
                     PS-beta-G-4; pregnancy-specific glycoprotein 4"
                     /calculated_mol_wt=33128
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3683
     Region          36..138
                     /region_name="IgV_CEACAM_D1"
                     /note="First immunoglobulin (Ig)-like domain of
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM); cd05774"
                     /db_xref="CDD:409430"
     Region          37..55
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          37..39
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409430"
     Region          44..46
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409430"
     Region          49..56
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409430"
     Region          56..63
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..69
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..68
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409430"
     Region          70..91
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          78..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          88..91
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..124
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..103
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409430"
     Region          105..109
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409430"
     Region          119..124
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409430"
     Region          125..132
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          133..138
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409430"
     Region          148..236
                     /region_name="IgI_hCEACAM_2_4_6_like"
                     /note="Immunoglobulin (Ig)-like domain of human
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM) domains 2, 4, and 6, and similar
                     domains; cd05740"
                     /db_xref="CDD:409402"
     Region          148..152
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409402"
     Region          155..160
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409402"
     Region          165..171
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409402"
     Region          178..183
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409402"
     Region          185..188
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409402"
     Region          192..196
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409402"
     Region          199..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409402"
     Region          214..222
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409402"
     Region          226..235
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409402"
     Region          245..320
                     /region_name="IgC2_CEACAM5-like"
                     /note="Fifth immunoglobulin (Ig)-like domain of the
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule 5 (CEACAM5) and similar domains; member of the
                     C2-set IgSF domains; cd20948"
                     /db_xref="CDD:409540"
     Region          245..251
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409540"
     Region          256..263
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409540"
     Region          269..275
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409540"
     Region          278..283
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409540"
     Region          286..292
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409540"
     Region          295..306
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409540"
     Region          309..320
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409540"
     CDS             1..326
                     /gene="PSG4"
                     /gene_synonym="PSBG-4"
                     /coded_by="NM_001276495.2:103..1083"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS62695.1"
                     /db_xref="GeneID:5672"
                     /db_xref="HGNC:HGNC:9521"
                     /db_xref="MIM:176393"
ORIGIN      
        1 mgplsappct qritwkgvll tasllnfwnp pttaqvtiea qppkvsegkd vlllvhnlpq
       61 nlagyiwykg qmtylyhyit syvvdgqrii ygpaysgrer vysnaslliq nvtqedagsy
      121 tlhiikrrdg tggvtghftf tlhpklskpy itinnlnpre nkdvltftce pksknytyiw
      181 wlngqslpvs prvkrpienr ililpnvtrn etgpyqceir dryggirsdp vtlnvlygpd
      241 lpsiypsfty yrsgenlyls cfaesnpraq yswtingkfq lsgqklsipq ittkhsglya
      301 csvrnsatgk essksitvkv sdwilp
//
LOCUS       NP_002775                426 aa            linear   PRI 20-JAN-2026
DEFINITION  pregnancy-specific beta-1-glycoprotein 9 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_002775
VERSION     NP_002775.3
DBSOURCE    REFSEQ: accession NM_002784.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Kandel,M., MacDonald,T.M., Walker,S.P., Cluver,C., Bergman,L.,
            Myers,J., Hastie,R., Keenan,E., Hannan,N.J., Cannon,P.,
            Nguyen,T.V., Pritchard,N., Tong,S. and Kaitu'u-Lino,T.J.
  TITLE     PSG7 and 9 (Pregnancy-Specific beta-1 Glycoproteins 7 and 9): Novel
            Biomarkers for Preeclampsia
  JOURNAL   J Am Heart Assoc 11 (7), e024536 (2022)
   PUBMED   35322669
  REMARK    GeneRIF: PSG7 and 9 (Pregnancy-Specific beta-1 Glycoproteins 7 and
            9): Novel Biomarkers for Preeclampsia.
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Rong,W., Zhang,Y., Yang,L., Feng,L., Wei,B., Wu,F., Wang,L.,
            Gao,Y., Cheng,S., Wu,J. and Xiao,T.
  TITLE     Post-surgical resection prognostic value of combined OPN, MMP7, and
            PSG9 plasma biomarkers in hepatocellular carcinoma
  JOURNAL   Front Med 13 (2), 250-258 (2019)
   PUBMED   29770948
  REMARK    GeneRIF: Plasma OPN + MMP7 + PSG9 elevation in combination was a
            prognostic factor for overall survival in hepatocellular carcinoma
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Rong,W., Yang,L., Yin,L., Gao,Y., Xiao,T. and Cheng,S.
  TITLE     PSG9 promotes angiogenesis by stimulating VEGFA production and is
            associated with poor prognosis in hepatocellular carcinoma
  JOURNAL   Sci China Life Sci 60 (5), 528-535 (2017)
   PUBMED   28078509
  REMARK    GeneRIF: Results indicate that pregnancy-specific glycoprotein 9
            (PSG9) may facilitate the development of hepatocellular carcinoma
            (HCC) by fostering angiogenesis via promoting VEGFA production in
            cancer HCC.
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Yang,L., Hu,S., Tan,J., Zhang,X., Yuan,W., Wang,Q., Xu,L., Liu,J.,
            Liu,Z., Jia,Y. and Huang,X.
  TITLE     Pregnancy-specific glycoprotein 9 (PSG9), a driver for colorectal
            cancer, enhances angiogenesis via activation of SMAD4
  JOURNAL   Oncotarget 7 (38), 61562-61574 (2016)
   PUBMED   27528036
  REMARK    GeneRIF: Findings illustrate the innovative mechanism by which PSG9
            drives the progression of colorectal cancer and tumor angiogenesis.
            This occurs via nuclear translocation of PSG9/SMAD4, which
            activates angiogenic cytokines.
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Brophy,B.K., MacDonald,R.E., McLenachan,P.A. and Mansfield,B.C.
  TITLE     cDNA sequence of the pregnancy-specific beta 1-glycoprotein-11s
            (PSG-11s)
  JOURNAL   Biochim Biophys Acta 1131 (1), 119-121 (1992)
   PUBMED   1581354
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Chan,W.Y., Zheng,Q.X., McMahon,J. and Tease,L.A.
  TITLE     Characterization of new members of the pregnancy-specific beta
            1-glycoprotein family
  JOURNAL   Mol Cell Biochem 106 (2), 161-170 (1991)
   PUBMED   1922019
REFERENCE   8  (residues 1 to 426)
  AUTHORS   Khan,W.N. and Hammarstrom,S.
  TITLE     Identification of a new carcinoembryonic antigen (CEA) family
            member in human fetal liver--cloning and sequence determination of
            pregnancy-specific glycoprotein 7
  JOURNAL   Biochem Biophys Res Commun 168 (1), 214-225 (1990)
   PUBMED   2328001
REFERENCE   9  (residues 1 to 426)
  AUTHORS   Arakawa,F., Kuroki,M., Misumi,Y., Matsuo,Y. and Matsuoka,Y.
  TITLE     The nucleotide and deduced amino acid sequences of a cDNA encoding
            a new species of pregnancy-specific beta 1-glycoprotein (PS beta G)
  JOURNAL   Biochim Biophys Acta 1048 (2-3), 303-305 (1990)
   PUBMED   2322584
REFERENCE   10 (residues 1 to 426)
  AUTHORS   Thompson,J., Koumari,R., Wagner,K., Barnert,S., Schleussner,C.,
            Schrewe,H., Zimmermann,W., Muller,G., Schempp,W., Zaninetta,D. et
            al.
  TITLE     The human pregnancy-specific glycoprotein genes are tightly linked
            on the long arm of chromosome 19 and are coordinately expressed
  JOURNAL   Biochem Biophys Res Commun 167 (2), 848-859 (1990)
   PUBMED   1690992
  REMARK    Erratum:[Biochem Biophys Res Commun 1990 May 16;168(3):1325]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC380417.1, M34481.1 and BC005925.1.
            
            On Aug 30, 2007 this sequence version replaced NP_002775.2.
            
            Summary: The protein encoded by this gene is a member of the
            pregnancy-specific glycoprotein (PSG) family. This protein family
            and the closely related carcinoembryonic antigen cell adhesion
            molecule (CEACAM) gene family are both members of the
            immunoglobulin superfamily, and are organized as a large gene
            cluster. This protein is thought to inhibit platelet-fibrinogen
            interactions. Several studies suggest that reduced serum
            concentrations of PSGs are associated with fetal growth
            restrictions, while up-regulation of this gene has been observed in
            colorectal cancers. Several pseudogenes of this gene are found on
            chromosome 19. Alternative splicing results in multiple transcript
            variants that encode multiple protein isoforms. [provided by
            RefSeq, Sep 2014].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279829.5656.1, BC020759.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162568, SAMN03465410
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000270077.8/ ENSP00000270077.3
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..426
                     /product="pregnancy-specific beta-1-glycoprotein 9 isoform
                     1 precursor"
                     /note="pregnancy-specific beta-1 glycoprotein B"
                     /calculated_mol_wt=44593
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3697
     mat_peptide     35..426
                     /product="Pregnancy-specific beta-1-glycoprotein 9.
                     /id=PRO_0000014916"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00887.2)"
                     /calculated_mol_wt=44593
     Region          36..138
                     /region_name="IgV_CEACAM_D1"
                     /note="First immunoglobulin (Ig)-like domain of
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM); cd05774"
                     /db_xref="CDD:409430"
     Region          37..55
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          37..39
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409430"
     Region          44..46
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409430"
     Region          49..56
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409430"
     Region          56..63
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..69
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..68
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409430"
     Region          70..91
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          78..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          88..91
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..124
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..103
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409430"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q00887.2)"
     Region          105..109
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409430"
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q00887.2)"
     Region          119..124
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409430"
     Region          125..132
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          127..129
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00887.2)"
     Region          133..138
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409430"
     Region          148..236
                     /region_name="IgI_hCEACAM_2_4_6_like"
                     /note="Immunoglobulin (Ig)-like domain of human
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM) domains 2, 4, and 6, and similar
                     domains; cd05740"
                     /db_xref="CDD:409402"
     Region          148..152
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409402"
     Region          155..160
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409402"
     Region          165..171
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409402"
     Region          178..183
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409402"
     Region          185..188
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409402"
     Region          192..196
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409402"
     Region          199..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409402"
     Site            199
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q00887.2)"
     Region          214..222
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409402"
     Region          226..235
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409402"
     Region          242..329
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          258..262
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            268
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q00887.2)"
     Region          271..275
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          293..297
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            303
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q00887.2)"
     Region          307..312
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          322..325
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          338..413
                     /region_name="IgC2_CEACAM5-like"
                     /note="Fifth immunoglobulin (Ig)-like domain of the
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule 5 (CEACAM5) and similar domains; member of the
                     C2-set IgSF domains; cd20948"
                     /db_xref="CDD:409540"
     Region          338..344
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409540"
     Region          349..356
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409540"
     Region          362..368
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409540"
     Region          371..376
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409540"
     Region          379..385
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409540"
     Site            387
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q00887.2)"
     Region          388..399
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409540"
     Region          402..413
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409540"
     CDS             1..426
                     /gene="PSG9"
                     /gene_synonym="PS-beta-B; PS-beta-G-9; PS34; PSBG-9;
                     PSG11; PSGII"
                     /coded_by="NM_002784.5:100..1380"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS12618.1"
                     /db_xref="GeneID:5678"
                     /db_xref="HGNC:HGNC:9526"
                     /db_xref="MIM:176398"
ORIGIN      
        1 mgplpapsct qritwkglll tasllnfwnp pttaevtiea qppkvsegkd vlllvhnlpq
       61 nlpgyfwykg emtdlyhyii syivdgkiii ygpaysgret vysnaslliq nvtrkdagty
      121 tlhiikrgde treeirhftf tlyletpkpy isssnlnpre ameavrlicd petldasylw
      181 wmngqslpvt hrlqlsktnr tlylfgvtky iagpyeceir npvsasrsdp vtlnllpklp
      241 ipyitinnln prenkdvlaf tcepksenyt yiwwlngqsl pvspgvkrpi enrililpsv
      301 trnetgpyqc eirdrygglr snpvilnvly gpdlpriyps ftyyrsgenl dlscftesnp
      361 paeyfwting kfqqsgqklf ipqitrnhsg lyacsvhnsa tgkeisksmt vkvsgpchgd
      421 ltesqs
//
LOCUS       NP_689785                479 aa            linear   PRI 20-JAN-2026
DEFINITION  adenylate kinase 8 isoform 1 [Homo sapiens].
ACCESSION   NP_689785
VERSION     NP_689785.1
DBSOURCE    REFSEQ: accession NM_152572.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Dougherty,G.W., Mizuno,K., Nothe-Menchen,T., Ikawa,Y., Boldt,K.,
            Ta-Shma,A., Aprea,I., Minegishi,K., Pang,Y.P., Pennekamp,P.,
            Loges,N.T., Raidt,J., Hjeij,R., Wallmeier,J., Mussaffi,H.,
            Perles,Z., Elpeleg,O., Rabert,F., Shiratori,H., Letteboer,S.J.,
            Horn,N., Young,S., Strunker,T., Stumme,F., Werner,C., Olbrich,H.,
            Takaoka,K., Ide,T., Twan,W.K., Biebach,L., Grosse-Onnebrink,J.,
            Klinkenbusch,J.A., Praveen,K., Bracht,D.C., Hoben,I.M., Junger,K.,
            Gutzlaff,J., Cindric,S., Aviram,M., Kaiser,T., Memari,Y.,
            Dzeja,P.P., Dworniczak,B., Ueffing,M., Roepman,R., Bartscherer,K.,
            Katsanis,N., Davis,E.E., Amirav,I., Hamada,H. and Omran,H.
  TITLE     CFAP45 deficiency causes situs abnormalities and asthenospermia by
            disrupting an axonemal adenine nucleotide homeostasis module
  JOURNAL   Nat Commun 11 (1), 5520 (2020)
   PUBMED   33139725
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Amiri,M., Conserva,F., Panayiotou,C., Karlsson,A. and Solaroli,N.
  TITLE     The human adenylate kinase 9 is a nucleoside mono- and diphosphate
            kinase
  JOURNAL   Int J Biochem Cell Biol 45 (5), 925-931 (2013)
   PUBMED   23416111
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   7  (residues 1 to 479)
  AUTHORS   Panayiotou,C., Solaroli,N., Xu,Y., Johansson,M. and Karlsson,A.
  TITLE     The characterization of human adenylate kinases 7 and 8
            demonstrates differences in kinetic parameters and structural
            organization among the family of adenylate kinase isoenzymes
  JOURNAL   Biochem J 433 (3), 527-534 (2011)
   PUBMED   21080915
  REMARK    GeneRIF: Both AK7 and full-length AK8 showed highest affinity for
            AMP with ATP as the phosphate donor, and proved to be more
            efficient in AMP phosphorylation as compared with the major
            cytosolic isoform AK1
REFERENCE   8  (residues 1 to 479)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 479)
  AUTHORS   Lesch,K.P., Timmesfeld,N., Renner,T.J., Halperin,R., Roser,C.,
            Nguyen,T.T., Craig,D.W., Romanos,J., Heine,M., Meyer,J.,
            Freitag,C., Warnke,A., Romanos,M., Schafer,H., Walitza,S., Reif,A.,
            Stephan,D.A. and Jacob,C.
  TITLE     Molecular genetics of adult ADHD: converging evidence from
            genome-wide association and extended pedigree linkage studies
  JOURNAL   J Neural Transm (Vienna) 115 (11), 1573-1585 (2008)
   PUBMED   18839057
REFERENCE   10 (residues 1 to 479)
  AUTHORS   Van Rompay,A.R., Johansson,M. and Karlsson,A.
  TITLE     Identification of a novel human adenylate kinase. cDNA cloning,
            expression analysis, chromosome localization and characterization
            of the recombinant protein
  JOURNAL   Eur J Biochem 261 (2), 509-517 (1999)
   PUBMED   10215863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445645.10 and AL160165.17.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK057266.1, BC050576.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000298545.4/ ENSP00000298545.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..479
                     /product="adenylate kinase 8 isoform 1"
                     /EC_number="2.7.4.3"
                     /EC_number="2.7.4.6"
                     /note="putative adenylate kinase-like protein C9orf98;
                     ATP-AMP transphosphorylase 8"
                     /calculated_mol_wt=54795
     Region          9..53
                     /region_name="DD_AK8"
                     /note="dimerization/docking (D/D) domain found in
                     adenylate kinase isoenzyme 8 (AK8) and similar proteins;
                     cd22979"
                     /db_xref="CDD:438548"
     Region          58..258
                     /region_name="Adenylate kinase 1.
                     /evidence=ECO:0000305|PubMed:21080915"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MA6.1)"
     Region          59..249
                     /region_name="ADK"
                     /note="Adenylate kinase (ADK) catalyzes the reversible
                     phosphoryl transfer from adenosine triphosphates (ATP) to
                     adenosine monophosphates (AMP) and to yield adenosine
                     diphosphates (ADP). This enzyme is required for the
                     biosynthesis of ADP and is essential for...; cd01428"
                     /db_xref="CDD:238713"
     Region          87..113
                     /region_name="NMP 1.
                     /evidence=ECO:0000250|UniProtKB:P69441"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MA6.1)"
     Site            order(89,139,143,178,219,222)
                     /site_type="other"
                     /note="ATP-AMP (Ap5A)-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     Site            order(89,113,139..140,142..143,147)
                     /site_type="other"
                     /note="AMP-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     Region          177..206
                     /region_name="LID 1.
                     /evidence=ECO:0000250|UniProtKB:P69441"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MA6.1)"
     Region          269..471
                     /region_name="Adenylate kinase 2.
                     /evidence=ECO:0000305|PubMed:21080915"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MA6.1)"
     Region          270..462
                     /region_name="ADK"
                     /note="Adenylate kinase (ADK) catalyzes the reversible
                     phosphoryl transfer from adenosine triphosphates (ATP) to
                     adenosine monophosphates (AMP) and to yield adenosine
                     diphosphates (ADP). This enzyme is required for the
                     biosynthesis of ADP and is essential for...; cd01428"
                     /db_xref="CDD:238713"
     Region          298..327
                     /region_name="NMP 2.
                     /evidence=ECO:0000250|UniProtKB:P69441"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MA6.1)"
     Site            order(299,304,327,353..354,356..357,361)
                     /site_type="other"
                     /note="AMP-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     Site            order(304,353,357,392,432,436)
                     /site_type="other"
                     /note="ATP-AMP (Ap5A)-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     Region          391..424
                     /region_name="LID 2.
                     /evidence=ECO:0000250|UniProtKB:P69441"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MA6.1)"
     CDS             1..479
                     /gene="AK8"
                     /gene_synonym="AK 8; C9orf98"
                     /coded_by="NM_152572.3:30..1469"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6954.1"
                     /db_xref="GeneID:158067"
                     /db_xref="HGNC:HGNC:26526"
                     /db_xref="MIM:615365"
ORIGIN      
        1 mdatiaphri ppempqygee nhifelmqnm leqllihqpe dpipfmiqhl hrdndnvpri
       61 vilgppasgk ttiamwlckh lnsslltlen lilnefsyta tearrlylqr ktvpsallvq
      121 liqerlaeed cikqgwildg ipetreqalr iqtlgitprh vivlsapdtv liernlgkri
      181 dpqtgeiyht tfdwppesei qnrlmvpedi seletaqkll eyhrnivrvi psypkilkvi
      241 sadqpcvdvf yqaltyvqsn hrtnapftpr vlllgpvgsg kslqaallaq kyrlvnvccg
      301 qllkeavadr ttfgeliqpf fekemavpds llmkvlsqrl dqqdciqkgw vlhgvprdld
      361 qahllnrlgy npnrvfflnv pfdsimerlt lrridpvtge ryhlmykppp tmeiqarllq
      421 npkdaeeqvk lkmdlfyrns adleqlygsa itlngdqdpy tvfeyiesgi inplpkkip
//
LOCUS       NP_001288636             333 aa            linear   PRI 20-JAN-2026
DEFINITION  pregnancy-specific beta-1-glycoprotein 9 isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_001288636 XP_005259135
VERSION     NP_001288636.1
DBSOURCE    REFSEQ: accession NM_001301707.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Kandel,M., MacDonald,T.M., Walker,S.P., Cluver,C., Bergman,L.,
            Myers,J., Hastie,R., Keenan,E., Hannan,N.J., Cannon,P.,
            Nguyen,T.V., Pritchard,N., Tong,S. and Kaitu'u-Lino,T.J.
  TITLE     PSG7 and 9 (Pregnancy-Specific beta-1 Glycoproteins 7 and 9): Novel
            Biomarkers for Preeclampsia
  JOURNAL   J Am Heart Assoc 11 (7), e024536 (2022)
   PUBMED   35322669
  REMARK    GeneRIF: PSG7 and 9 (Pregnancy-Specific beta-1 Glycoproteins 7 and
            9): Novel Biomarkers for Preeclampsia.
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Rong,W., Zhang,Y., Yang,L., Feng,L., Wei,B., Wu,F., Wang,L.,
            Gao,Y., Cheng,S., Wu,J. and Xiao,T.
  TITLE     Post-surgical resection prognostic value of combined OPN, MMP7, and
            PSG9 plasma biomarkers in hepatocellular carcinoma
  JOURNAL   Front Med 13 (2), 250-258 (2019)
   PUBMED   29770948
  REMARK    GeneRIF: Plasma OPN + MMP7 + PSG9 elevation in combination was a
            prognostic factor for overall survival in hepatocellular carcinoma
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Rong,W., Yang,L., Yin,L., Gao,Y., Xiao,T. and Cheng,S.
  TITLE     PSG9 promotes angiogenesis by stimulating VEGFA production and is
            associated with poor prognosis in hepatocellular carcinoma
  JOURNAL   Sci China Life Sci 60 (5), 528-535 (2017)
   PUBMED   28078509
  REMARK    GeneRIF: Results indicate that pregnancy-specific glycoprotein 9
            (PSG9) may facilitate the development of hepatocellular carcinoma
            (HCC) by fostering angiogenesis via promoting VEGFA production in
            cancer HCC.
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Yang,L., Hu,S., Tan,J., Zhang,X., Yuan,W., Wang,Q., Xu,L., Liu,J.,
            Liu,Z., Jia,Y. and Huang,X.
  TITLE     Pregnancy-specific glycoprotein 9 (PSG9), a driver for colorectal
            cancer, enhances angiogenesis via activation of SMAD4
  JOURNAL   Oncotarget 7 (38), 61562-61574 (2016)
   PUBMED   27528036
  REMARK    GeneRIF: Findings illustrate the innovative mechanism by which PSG9
            drives the progression of colorectal cancer and tumor angiogenesis.
            This occurs via nuclear translocation of PSG9/SMAD4, which
            activates angiogenic cytokines.
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Brophy,B.K., MacDonald,R.E., McLenachan,P.A. and Mansfield,B.C.
  TITLE     cDNA sequence of the pregnancy-specific beta 1-glycoprotein-11s
            (PSG-11s)
  JOURNAL   Biochim Biophys Acta 1131 (1), 119-121 (1992)
   PUBMED   1581354
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Chan,W.Y., Zheng,Q.X., McMahon,J. and Tease,L.A.
  TITLE     Characterization of new members of the pregnancy-specific beta
            1-glycoprotein family
  JOURNAL   Mol Cell Biochem 106 (2), 161-170 (1991)
   PUBMED   1922019
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Khan,W.N. and Hammarstrom,S.
  TITLE     Identification of a new carcinoembryonic antigen (CEA) family
            member in human fetal liver--cloning and sequence determination of
            pregnancy-specific glycoprotein 7
  JOURNAL   Biochem Biophys Res Commun 168 (1), 214-225 (1990)
   PUBMED   2328001
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Arakawa,F., Kuroki,M., Misumi,Y., Matsuo,Y. and Matsuoka,Y.
  TITLE     The nucleotide and deduced amino acid sequences of a cDNA encoding
            a new species of pregnancy-specific beta 1-glycoprotein (PS beta G)
  JOURNAL   Biochim Biophys Acta 1048 (2-3), 303-305 (1990)
   PUBMED   2322584
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Thompson,J., Koumari,R., Wagner,K., Barnert,S., Schleussner,C.,
            Schrewe,H., Zimmermann,W., Muller,G., Schempp,W., Zaninetta,D. et
            al.
  TITLE     The human pregnancy-specific glycoprotein genes are tightly linked
            on the long arm of chromosome 19 and are coordinately expressed
  JOURNAL   Biochem Biophys Res Commun 167 (2), 848-859 (1990)
   PUBMED   1690992
  REMARK    Erratum:[Biochem Biophys Res Commun 1990 May 16;168(3):1325]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC380417.1, M34481.1, AK300229.1 and BC005925.1.
            
            On Sep 11, 2014 this sequence version replaced XP_005259135.1.
            
            Summary: The protein encoded by this gene is a member of the
            pregnancy-specific glycoprotein (PSG) family. This protein family
            and the closely related carcinoembryonic antigen cell adhesion
            molecule (CEACAM) gene family are both members of the
            immunoglobulin superfamily, and are organized as a large gene
            cluster. This protein is thought to inhibit platelet-fibrinogen
            interactions. Several studies suggest that reduced serum
            concentrations of PSGs are associated with fetal growth
            restrictions, while up-regulation of this gene has been observed in
            colorectal cancers. Several pseudogenes of this gene are found on
            chromosome 19. Alternative splicing results in multiple transcript
            variants that encode multiple protein isoforms. [provided by
            RefSeq, Sep 2014].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the coding region, compared to variant 1. It encodes
            isoform 2 which is shorter than isoform 1. Variants 2 and 3 encode
            isoforms of the same size, but contain internal differences.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK300229.1, ERR279844.4687.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162568, SAMN03465410
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..333
                     /product="pregnancy-specific beta-1-glycoprotein 9 isoform
                     2 precursor"
                     /note="pregnancy-specific beta-1 glycoprotein B"
                     /calculated_mol_wt=34045
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3697
     Region          36..138
                     /region_name="IgV_CEACAM_D1"
                     /note="First immunoglobulin (Ig)-like domain of
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM); cd05774"
                     /db_xref="CDD:409430"
     Region          37..55
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          37..39
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409430"
     Region          44..46
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409430"
     Region          49..56
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409430"
     Region          56..63
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..69
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..68
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409430"
     Region          70..91
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          78..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          88..91
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..124
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..103
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409430"
     Region          105..109
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409430"
     Region          119..124
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409430"
     Region          125..132
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          133..138
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409430"
     Region          149..236
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          165..169
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409402"
     Region          178..182
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409402"
     Region          200..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409402"
     Region          214..219
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409402"
     Region          229..232
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409402"
     Region          245..320
                     /region_name="IgC2_CEACAM5-like"
                     /note="Fifth immunoglobulin (Ig)-like domain of the
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule 5 (CEACAM5) and similar domains; member of the
                     C2-set IgSF domains; cd20948"
                     /db_xref="CDD:409540"
     Region          245..251
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409540"
     Region          256..263
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409540"
     Region          269..275
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409540"
     Region          278..283
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409540"
     Region          286..292
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409540"
     Region          295..306
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409540"
     Region          309..320
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409540"
     CDS             1..333
                     /gene="PSG9"
                     /gene_synonym="PS-beta-B; PS-beta-G-9; PS34; PSBG-9;
                     PSG11; PSGII"
                     /coded_by="NM_001301707.2:100..1101"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS77312.1"
                     /db_xref="GeneID:5678"
                     /db_xref="HGNC:HGNC:9526"
                     /db_xref="MIM:176398"
ORIGIN      
        1 mgplpapsct qritwkglll tasllnfwnp pttaevtiea qppkvsegkd vlllvhnlpq
       61 nlpgyfwykg emtdlyhyii syivdgkiii ygpaysgret vysnaslliq nvtrkdagty
      121 tlhiikrgde treeirhftf tlysklpipy itinnlnpre nkdvlaftce pksenytyiw
      181 wlngqslpvs pgvkrpienr ililpsvtrn etgpyqceir drygglrsnp vilnvlygpd
      241 lpriypsfty yrsgenldls cftesnppae yfwtingkfq qsgqklfipq itrnhsglya
      301 csvhnsatgk eisksmtvkv sgpchgdlte sqs
//
LOCUS       NP_001191777             195 aa            linear   PRI 20-JAN-2026
DEFINITION  TNFAIP8L2-SCNM1 protein [Homo sapiens].
ACCESSION   NP_001191777
VERSION     NP_001191777.1
DBSOURCE    REFSEQ: accession NM_001204848.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Prakash,T., Sharma,V.K., Adati,N., Ozawa,R., Kumar,N., Nishida,Y.,
            Fujikake,T., Takeda,T. and Taylor,T.D.
  TITLE     Expression of conjoined genes: another mechanism for gene
            regulation in eukaryotes
  JOURNAL   PLoS One 5 (10), e13284 (2010)
   PUBMED   20967262
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL592424.13 and BG531092.1.
            
            Summary: This locus represents naturally occurring read-through
            transcription between the neighboring TNFAIP8L2 (tumor necrosis
            factor, alpha-induced protein 8-like 2) and SCNM1 (sodium channel
            modifier 1) genes on chromosome 1. The protein-coding read-through
            transcript variant encodes a protein that shares sequence identity
            with the downstream gene product but its N-terminal region is
            shorter due to alternate exon use relative to the downstream gene.
            [provided by RefSeq, Dec 2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR999387.1, BG531092.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            readthrough transcript :: includes exons from GeneID 79005, 79626
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..195
                     /product="TNFAIP8L2-SCNM1 protein"
                     /note="Sodium channel modifier 1"
                     /calculated_mol_wt=21756
     Region          9..35
                     /region_name="zf-SCNM1"
                     /note="Zinc-finger of sodium channel modifier 1;
                     pfam15803"
                     /db_xref="CDD:464882"
     Region          148..193
                     /region_name="SCNM1_acidic"
                     /note="Acidic C-terminal region of sodium channel modifier
                     1 SCNM1; pfam15805"
                     /db_xref="CDD:464884"
     CDS             1..195
                     /gene="TNFAIP8L2-SCNM1"
                     /coded_by="NM_001204848.2:129..716"
                     /db_xref="GeneID:100534012"
ORIGIN      
        1 mlrdgrfaca icphrpvldt lamltahrag kkhlsslqlf ygkkqpgker kqnpkhqnel
       61 rreetkaeap lltqtrlitq salhraphyn sccrrkyrpe apgpsvslsp mppsevklqs
      121 gkisrepepa agpqaeesat vsapapmspt rrraldhylt lrssgwipdg rgrwvkdenv
      181 efdsdeeepp dlpld
//
LOCUS       NP_009146                485 aa            linear   PRI 20-JAN-2026
DEFINITION  DNA polymerase subunit gamma-2 [Homo sapiens].
ACCESSION   NP_009146
VERSION     NP_009146.2
DBSOURCE    REFSEQ: accession NM_007215.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Borsche,M., Dulovic-Mahlow,M., Baumann,H., Tunc,S., Luth,T.,
            Schaake,S., Ozcakir,S., Westenberger,A., Munchau,A., Knappe,E.,
            Trinh,J., Bruggemann,N. and Lohmann,K.
  TITLE     POLG2-Linked Mitochondrial Disease: Functional Insights from New
            Mutation Carriers and Review of the Literature
  JOURNAL   Cerebellum 23 (2), 479-488 (2024)
   PUBMED   37085601
  REMARK    GeneRIF: POLG2-Linked Mitochondrial Disease: Functional Insights
            from New Mutation Carriers and Review of the Literature.
            Review article
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Wojtaszek,J.L., Hoff,K.E., Longley,M.J., Kaur,P., Andres,S.N.,
            Wang,H., Williams,R.S. and Copeland,W.C.
  TITLE     Structure-specific roles for PolG2-DNA complexes in maintenance and
            replication of mitochondrial DNA
  JOURNAL   Nucleic Acids Res 51 (18), 9716-9732 (2023)
   PUBMED   37592734
  REMARK    GeneRIF: Structure-specific roles for PolG2-DNA complexes in
            maintenance and replication of mitochondrial DNA.
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Park,J., Herrmann,G.K., Mitchell,P.G., Sherman,M.B. and Yin,Y.W.
  TITLE     Polgamma coordinates DNA synthesis and proofreading to ensure
            mitochondrial genome integrity
  JOURNAL   Nat Struct Mol Biol 30 (6), 812-823 (2023)
   PUBMED   37202477
REFERENCE   5  (residues 1 to 485)
  AUTHORS   Longley,M.J., Clark,S., Yu Wai Man,C., Hudson,G., Durham,S.E.,
            Taylor,R.W., Nightingale,S., Turnbull,D.M., Copeland,W.C. and
            Chinnery,P.F.
  TITLE     Mutant POLG2 disrupts DNA polymerase gamma subunits and causes
            progressive external ophthalmoplegia
  JOURNAL   Am J Hum Genet 78 (6), 1026-1034 (2006)
   PUBMED   16685652
REFERENCE   6  (residues 1 to 485)
  AUTHORS   Carrodeguas,J.A., Pinz,K.G. and Bogenhagen,D.F.
  TITLE     DNA binding properties of human pol gammaB
  JOURNAL   J Biol Chem 277 (51), 50008-50014 (2002)
   PUBMED   12379656
  REMARK    GeneRIF: PolB gamma can bind double-stranded DNA and may play a
            role in DNA replication or repair
REFERENCE   7  (residues 1 to 485)
  AUTHORS   Carrodeguas,J.A. and Bogenhagen,D.F.
  TITLE     Protein sequences conserved in prokaryotic aminoacyl-tRNA
            synthetases are important for the activity of the processivity
            factor of human mitochondrial DNA polymerase
  JOURNAL   Nucleic Acids Res 28 (5), 1237-1244 (2000)
   PUBMED   10666468
REFERENCE   8  (residues 1 to 485)
  AUTHORS   Johnson,A.A., Tsai,Yc., Graves,S.W. and Johnson,K.A.
  TITLE     Human mitochondrial DNA polymerase holoenzyme: reconstitution and
            characterization
  JOURNAL   Biochemistry 39 (7), 1702-1708 (2000)
   PUBMED   10677218
REFERENCE   9  (residues 1 to 485)
  AUTHORS   Lim,S.E., Longley,M.J. and Copeland,W.C.
  TITLE     The mitochondrial p55 accessory subunit of human DNA polymerase
            gamma enhances DNA binding, promotes processive DNA synthesis, and
            confers N-ethylmaleimide resistance
  JOURNAL   J Biol Chem 274 (53), 38197-38203 (1999)
   PUBMED   10608893
REFERENCE   10 (residues 1 to 485)
  AUTHORS   Wang,Y., Farr,C.L. and Kaguni,L.S.
  TITLE     Accessory subunit of mitochondrial DNA polymerase from Drosophila
            embryos. Cloning, molecular analysis, and association in the native
            enzyme
  JOURNAL   J Biol Chem 272 (21), 13640-13646 (1997)
   PUBMED   9153213
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI826587.1, BC009194.2 and
            BC000913.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 15, 2005 this sequence version replaced NP_009146.1.
            
            Summary: This gene encodes the processivity subunit of the
            mitochondrial DNA polymerase gamma. The encoded protein forms a
            heterotrimer containing one catalytic subunit and two processivity
            subunits. This protein enhances DNA binding and promotes processive
            DNA synthesis. Mutations in this gene result in autosomal dominant
            progressive external ophthalmoplegia with mitochondrial DNA
            deletions.[provided by RefSeq, Sep 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC009194.2, AF142992.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000539111.7/
                                                  ENSP00000442563.2
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.3"
     Protein         1..485
                     /product="DNA polymerase subunit gamma-2"
                     /EC_number="2.7.7.7"
                     /note="mitochondrial DNA polymerase, accessory subunit;
                     DNA polymerase subunit gamma-2, mitochondrial;
                     mitochondrial DNA polymerase subunit gamma-2; DNA
                     polymerase gamma accessory 55 kDa subunit; polymerase (DNA
                     directed), gamma 2, accessory subunit; polymerase (DNA)
                     gamma 2, accessory subunit"
                     /calculated_mol_wt=54780
     Region          28..65
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHN1.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UHN1.1)"
     Region          69..350
                     /region_name="class_II_aaRS-like_core"
                     /note="Class II tRNA amino-acyl synthetase-like catalytic
                     core domain. Class II amino acyl-tRNA synthetases (aaRS)
                     share a common fold and generally attach an amino acid to
                     the 3' OH of ribose of the appropriate tRNA. PheRS is an
                     exception in that it attaches...; cl00268"
                     /db_xref="CDD:444800"
     Site            125..129
                     /site_type="other"
                     /note="motif 1"
                     /db_xref="CDD:238397"
     Site            order(126..127,129,191..192,215,217,260)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238397"
     Site            order(184,186,216,234,236,238..240,299..300,304,337..338,
                     340..341,344)
                     /site_type="active"
                     /db_xref="CDD:238397"
     Site            215..217
                     /site_type="other"
                     /note="motif 2"
                     /db_xref="CDD:238397"
     Site            order(341,344)
                     /site_type="other"
                     /note="motif 3"
                     /db_xref="CDD:238397"
     Region          354..481
                     /region_name="Pol_gamma_b_Cterm"
                     /note="C-terminal domain of mitochondrial DNA polymerase
                     gamma B subunit, which is required for processivity.
                     Polymerase gamma replicates and repairs mitochondrial DNA.
                     The c-terminal domain of its B subunit is strikingly
                     similar to the anticodon-binding domain...; cd02426"
                     /db_xref="CDD:239106"
     Site            363..365
                     /site_type="other"
                     /note="putative DNA-binding site [nucleotide binding]"
                     /db_xref="CDD:239106"
     Site            order(400,403..404,407..408,410,414..415,417..420)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:239106"
     CDS             1..485
                     /gene="POLG2"
                     /gene_synonym="HP55; MTDPS16; MTDPS16A; MTDPS16B; MTPOLB;
                     PEOA4; POLG-BETA; POLGB"
                     /coded_by="NM_007215.4:87..1544"
                     /db_xref="CCDS:CCDS32706.1"
                     /db_xref="GeneID:11232"
                     /db_xref="HGNC:HGNC:9180"
                     /db_xref="MIM:604983"
ORIGIN      
        1 mrsrvavrac hkvcrcllsg fggrvdagqp elltersspk gghvkshael egngehpeap
       61 gsgegseall eicqrrhfls gskqqlsrds llsgchpgfg plgvelrknl aaewwtsvvv
      121 freqvfpvda lhhkpgpllp gdsafrlvsa etlreilqdk elskeqlvaf lenvlktsgk
      181 lrenllhgal ehyvncldlv nkrlpyglaq igvcfhpvfd tkqirngvks igekteaslv
      241 wftpprtsnq wldfwlrhrl qwwrkfamsp snfsssdcqd eegrkgnkly ynfpwgkeli
      301 etlwnlgdhe llhmypgnvs klhgrdgrkn vvpcvlsvng dldrgmlayl ydsfqltens
      361 ftrkknlhrk vlklhpclap ikvaldvgrg ptlelrqvcq glfnelleng isvwpgylet
      421 mqssleqlys kydemsilft vlvtettlen glihlrsrdt tmkemmhisk lkdflikyis
      481 saknv
//
LOCUS       NP_001307878             459 aa            linear   PRI 20-JAN-2026
DEFINITION  RNA-binding motif protein, Y chromosome, family 1 member D isoform
            2 [Homo sapiens].
ACCESSION   NP_001307878 XP_005262642
VERSION     NP_001307878.1
DBSOURCE    REFSEQ: accession NM_001320949.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 459)
  AUTHORS   Tsuei,D.J., Hsu,H.C., Lee,P.H., Jeng,Y.M., Pu,Y.S., Chen,C.N.,
            Lee,Y.C., Chou,W.C., Chang,C.J., Ni,Y.H. and Chang,M.H.
  TITLE     RBMY, a male germ cell-specific RNA-binding protein, activated in
            human liver cancers and transforms rodent fibroblasts
  JOURNAL   Oncogene 23 (34), 5815-5822 (2004)
   PUBMED   15184870
REFERENCE   2  (residues 1 to 459)
  AUTHORS   Skaletsky,H., Kuroda-Kawaguchi,T., Minx,P.J., Cordum,H.S.,
            Hillier,L., Brown,L.G., Repping,S., Pyntikova,T., Ali,J., Bieri,T.,
            Chinwalla,A., Delehaunty,A., Delehaunty,K., Du,H., Fewell,G.,
            Fulton,L., Fulton,R., Graves,T., Hou,S.F., Latrielle,P.,
            Leonard,S., Mardis,E., Maupin,R., McPherson,J., Miner,T., Nash,W.,
            Nguyen,C., Ozersky,P., Pepin,K., Rock,S., Rohlfing,T., Scott,K.,
            Schultz,B., Strong,C., Tin-Wollam,A., Yang,S.P., Waterston,R.H.,
            Wilson,R.K., Rozen,S. and Page,D.C.
  TITLE     The male-specific region of the human Y chromosome is a mosaic of
            discrete sequence classes
  JOURNAL   Nature 423 (6942), 825-837 (2003)
   PUBMED   12815422
REFERENCE   3  (residues 1 to 459)
  AUTHORS   Chai,N.N., Zhou,H., Hernandez,J., Najmabadi,H., Bhasin,S. and
            Yen,P.H.
  TITLE     Structure and organization of the RBMY genes on the human Y
            chromosome: transposition and amplification of an ancestral
            autosomal hnRNPG gene
  JOURNAL   Genomics 49 (2), 283-289 (1998)
   PUBMED   9598316
REFERENCE   4  (residues 1 to 459)
  AUTHORS   Prosser,J., Inglis,J.D., Condie,A., Ma,K., Kerr,S., Thakrar,R.,
            Taylor,K., Cameron,J.M. and Cooke,H.J.
  TITLE     Degeneracy in human multicopy RBM (YRRM), a candidate
            spermatogenesis gene
  JOURNAL   Mamm Genome 7 (11), 835-842 (1996)
   PUBMED   8875892
REFERENCE   5  (residues 1 to 459)
  AUTHORS   Ma,K., Inglis,J.D., Sharkey,A., Bickmore,W.A., Hill,R.E.,
            Prosser,E.J., Speed,R.M., Thomson,E.J., Jobling,M., Taylor,K. et
            al.
  TITLE     A Y chromosome gene family with RNA-binding protein homology:
            candidates for the azoospermia factor AZF controlling human
            spermatogenesis
  JOURNAL   Cell 75 (7), 1287-1295 (1993)
   PUBMED   8269511
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007322.4.
            
            On Mar 10, 2016 this sequence version replaced XP_005262642.1.
            
            Summary: This gene encodes a protein containing an RNA-binding
            motif in the N-terminus and four SRGY (serine, arginine, glycine,
            tyrosine) boxes in the C-terminus. This protein likely functions as
            a splicing factor during spermatogenesis. Multiple closely related
            paralogs of this gene are found in a gene cluster in the AZFb
            azoospermia factor region of chromosome Y. Most of these related
            copies are thought to be pseudogenes, though several likely encode
            functional proteins. [provided by RefSeq, Mar 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1968968, SAMEA2144333
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..459
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.223"
     Protein         1..459
                     /product="RNA-binding motif protein, Y chromosome, family
                     1 member D isoform 2"
                     /note="RNA-binding motif protein, Y chromosome, family 1
                     member D; RNA-binding motif protein 1; RNA-binding motif
                     protein 2; Y chromosome RNA recognition motif 1"
                     /calculated_mol_wt=51152
     Region          7..85
                     /region_name="RRM_RBMX_like"
                     /note="RNA recognition motif (RRM) found in heterogeneous
                     nuclear ribonucleoprotein G (hnRNP G), Y chromosome RNA
                     recognition motif 1 (hRBMY), testis-specific heterogeneous
                     nuclear ribonucleoprotein G-T (hnRNP G-T) and similar
                     proteins; cd12382"
                     /db_xref="CDD:409816"
     Site            order(9,11,13..17,38,40..43,44..50,52,77,79,81..85)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409816"
     Region          <10..>182
                     /region_name="ELAV_HUD_SF"
                     /note="ELAV/HuD family splicing factor; TIGR01661"
                     /db_xref="CDD:273741"
     Region          158..>316
                     /region_name="dnaA"
                     /note="chromosomal replication initiator protein DnaA;
                     cl42516"
                     /db_xref="CDD:455861"
     Region          174..218
                     /region_name="RBM1CTR"
                     /note="RBM1CTR (NUC064) family; pfam08081"
                     /db_xref="CDD:400429"
     CDS             1..459
                     /gene="RBMY1D"
                     /gene_synonym="hRBMY; RBM1; RBM2; YRRM1; YRRM2"
                     /coded_by="NM_001320949.1:153..1532"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS83521.1"
                     /db_xref="GeneID:378949"
                     /db_xref="HGNC:HGNC:23915"
ORIGIN      
        1 mveadhpgkl figglnretn ekmlkavfgk hgpisevlli kdrtsksrgf afitfenpad
       61 aknaakdmng kslhgkaikv eqakkpsfqs ggrrrppass rnrspsgslr sargsrggtr
      121 gwlpsqeghl ddggytpdlk msysrglipv krgpssrsgg pppkksapsa varsnswmgs
      181 qgpmsqrren ygvpprrati sswrndrmst rhdgyatndg nhpscqetrd yappsrgyay
      241 rdnghsnrde hssrgyrnhr ssretrdyap psrghayrdy ghsrrdesys rgyrnrrssr
      301 etreyappsr ghgyrdyghs rrhesysrgy syhdgygeal grdhsehlsg ssyrdalqry
      361 gtshgappar gprmsyggst chaysntrdr ygrswesyss cgdfhycdre hvcrkdqrnp
      421 pslgrvlpdp reacgsssyv asivdggesr sekgdssry
//
LOCUS       NP_001387105             234 aa            linear   PRI 20-JAN-2026
DEFINITION  large ribosomal subunit protein uL23m isoform 4 [Homo sapiens].
ACCESSION   NP_001387105 XP_011518577
VERSION     NP_001387105.1
DBSOURCE    REFSEQ: accession NM_001400176.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   5  (residues 1 to 234)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   6  (residues 1 to 234)
  AUTHORS   Zhang,Z. and Gerstein,M.
  TITLE     Identification and characterization of over 100 mitochondrial
            ribosomal protein pseudogenes in the human genome
  JOURNAL   Genomics 81 (5), 468-480 (2003)
   PUBMED   12706105
REFERENCE   7  (residues 1 to 234)
  AUTHORS   O'Brien,T.W.
  TITLE     Evolution of a protein-rich mitochondrial ribosome: implications
            for human genetic disease
  JOURNAL   Gene 286 (1), 73-79 (2002)
   PUBMED   11943462
REFERENCE   8  (residues 1 to 234)
  AUTHORS   Kenmochi,N., Suzuki,T., Uechi,T., Magoori,M., Kuniba,M., Higa,S.,
            Watanabe,K. and Tanaka,T.
  TITLE     The human mitochondrial ribosomal protein genes: mapping of 54
            genes to the chromosomes and implications for human disorders
  JOURNAL   Genomics 77 (1-2), 65-70 (2001)
   PUBMED   11543634
REFERENCE   9  (residues 1 to 234)
  AUTHORS   Suzuki,T., Terasaki,M., Takemoto-Hori,C., Hanada,T., Ueda,T.,
            Wada,A. and Watanabe,K.
  TITLE     Structural compensation for the deficit of rRNA with proteins in
            the mammalian mitochondrial ribosome. Systematic analysis of
            protein components of the large ribosomal subunit from mammalian
            mitochondria
  JOURNAL   J Biol Chem 276 (24), 21724-21736 (2001)
   PUBMED   11279069
REFERENCE   10 (residues 1 to 234)
  AUTHORS   Tsang,P., Gilles,F., Yuan,L., Kuo,Y.H., Lupu,F., Samara,G.,
            Moosikasuwan,J., Goye,A., Zelenetz,A.D., Selleri,L. et al.
  TITLE     A novel L23-related gene 40 kb downstream of the imprinted H19 gene
            is biallelically expressed in mid-fetal and adult human tissues
  JOURNAL   Hum Mol Genet 4 (9), 1499-1507 (1995)
   PUBMED   8541832
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC051649.21 and AC123789.6.
            
            On Jan 20, 2022 this sequence version replaced XP_011518577.1.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 39S subunit protein. The gene is
            biallelically expressed, despite its location within a region of
            imprinted genes on chromosome 11. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2154665,
                              SAMEA2157437 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..234
                     /product="large ribosomal subunit protein uL23m isoform 4"
                     /note="L23 mitochondrial-related protein; ribosomal
                     protein related to L23 (mitochondrial); 39S ribosomal
                     protein L23, mitochondrial; mitochondrial large ribosomal
                     subunit protein uL23m"
                     /calculated_mol_wt=25815
     Region          <42..99
                     /region_name="Ribosomal_L23"
                     /note="Ribosomal protein L23; pfam00276"
                     /db_xref="CDD:459743"
     CDS             1..234
                     /gene="MRPL23"
                     /gene_synonym="L23MRP; L23mt; MRP-L23; RPL23L; uL23m"
                     /coded_by="NM_001400176.1:32..736"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:6150"
                     /db_xref="HGNC:HGNC:10322"
                     /db_xref="MIM:600789"
ORIGIN      
        1 marnvvyply rlggpqlrvf rtnffiqlvr pgvaqpedtv qfripmemtr vdlrnylegi
       61 ynvpvaavrt rvqhgsnkrr dhrnvrikkp dykvayvqlp sqtpskeqng qgstlcfrss
      121 cskgwstwgt rdprpawspv ggriprkags ggpanriaqd grlllnsfrs aepqgcrslg
      181 pqspggdpah tilrppsqng dcaemhacrl hpailghgsp dpttsewacl evdl
//
LOCUS       NP_001387101             108 aa            linear   PRI 20-JAN-2026
DEFINITION  large ribosomal subunit protein uL23m isoform 2 [Homo sapiens].
ACCESSION   NP_001387101
VERSION     NP_001387101.1
DBSOURCE    REFSEQ: accession NM_001400172.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Zhang,Z. and Gerstein,M.
  TITLE     Identification and characterization of over 100 mitochondrial
            ribosomal protein pseudogenes in the human genome
  JOURNAL   Genomics 81 (5), 468-480 (2003)
   PUBMED   12706105
REFERENCE   7  (residues 1 to 108)
  AUTHORS   O'Brien,T.W.
  TITLE     Evolution of a protein-rich mitochondrial ribosome: implications
            for human genetic disease
  JOURNAL   Gene 286 (1), 73-79 (2002)
   PUBMED   11943462
REFERENCE   8  (residues 1 to 108)
  AUTHORS   Kenmochi,N., Suzuki,T., Uechi,T., Magoori,M., Kuniba,M., Higa,S.,
            Watanabe,K. and Tanaka,T.
  TITLE     The human mitochondrial ribosomal protein genes: mapping of 54
            genes to the chromosomes and implications for human disorders
  JOURNAL   Genomics 77 (1-2), 65-70 (2001)
   PUBMED   11543634
REFERENCE   9  (residues 1 to 108)
  AUTHORS   Suzuki,T., Terasaki,M., Takemoto-Hori,C., Hanada,T., Ueda,T.,
            Wada,A. and Watanabe,K.
  TITLE     Structural compensation for the deficit of rRNA with proteins in
            the mammalian mitochondrial ribosome. Systematic analysis of
            protein components of the large ribosomal subunit from mammalian
            mitochondria
  JOURNAL   J Biol Chem 276 (24), 21724-21736 (2001)
   PUBMED   11279069
REFERENCE   10 (residues 1 to 108)
  AUTHORS   Tsang,P., Gilles,F., Yuan,L., Kuo,Y.H., Lupu,F., Samara,G.,
            Moosikasuwan,J., Goye,A., Zelenetz,A.D., Selleri,L. et al.
  TITLE     A novel L23-related gene 40 kb downstream of the imprinted H19 gene
            is biallelically expressed in mid-fetal and adult human tissues
  JOURNAL   Hum Mol Genet 4 (9), 1499-1507 (1995)
   PUBMED   8541832
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC051649.21.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 39S subunit protein. The gene is
            biallelically expressed, despite its location within a region of
            imprinted genes on chromosome 11. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AV690724.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119, SAMN03267773
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..108
                     /product="large ribosomal subunit protein uL23m isoform 2"
                     /note="L23 mitochondrial-related protein; ribosomal
                     protein related to L23 (mitochondrial); 39S ribosomal
                     protein L23, mitochondrial; mitochondrial large ribosomal
                     subunit protein uL23m"
                     /calculated_mol_wt=12407
     Region          <3..60
                     /region_name="Ribosomal_L23"
                     /note="Ribosomal protein L23; pfam00276"
                     /db_xref="CDD:459743"
     CDS             1..108
                     /gene="MRPL23"
                     /gene_synonym="L23MRP; L23mt; MRP-L23; RPL23L; uL23m"
                     /coded_by="NM_001400172.1:366..692"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:6150"
                     /db_xref="HGNC:HGNC:10322"
                     /db_xref="MIM:600789"
ORIGIN      
        1 memtrvdlrn ylegiynvpv aavrtrvqhg snkrrdhrnv rikkpdykva yvqlahgqtf
       61 tfpdlfpekd espegsaadd lysmleeerq qrqssdprrg gvpswfgl
//
LOCUS       NP_001304888             307 aa            linear   PRI 20-JAN-2026
DEFINITION  adenylate kinase 8 isoform 3 [Homo sapiens].
ACCESSION   NP_001304888 XP_011516581
VERSION     NP_001304888.1
DBSOURCE    REFSEQ: accession NM_001317959.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Dougherty,G.W., Mizuno,K., Nothe-Menchen,T., Ikawa,Y., Boldt,K.,
            Ta-Shma,A., Aprea,I., Minegishi,K., Pang,Y.P., Pennekamp,P.,
            Loges,N.T., Raidt,J., Hjeij,R., Wallmeier,J., Mussaffi,H.,
            Perles,Z., Elpeleg,O., Rabert,F., Shiratori,H., Letteboer,S.J.,
            Horn,N., Young,S., Strunker,T., Stumme,F., Werner,C., Olbrich,H.,
            Takaoka,K., Ide,T., Twan,W.K., Biebach,L., Grosse-Onnebrink,J.,
            Klinkenbusch,J.A., Praveen,K., Bracht,D.C., Hoben,I.M., Junger,K.,
            Gutzlaff,J., Cindric,S., Aviram,M., Kaiser,T., Memari,Y.,
            Dzeja,P.P., Dworniczak,B., Ueffing,M., Roepman,R., Bartscherer,K.,
            Katsanis,N., Davis,E.E., Amirav,I., Hamada,H. and Omran,H.
  TITLE     CFAP45 deficiency causes situs abnormalities and asthenospermia by
            disrupting an axonemal adenine nucleotide homeostasis module
  JOURNAL   Nat Commun 11 (1), 5520 (2020)
   PUBMED   33139725
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Amiri,M., Conserva,F., Panayiotou,C., Karlsson,A. and Solaroli,N.
  TITLE     The human adenylate kinase 9 is a nucleoside mono- and diphosphate
            kinase
  JOURNAL   Int J Biochem Cell Biol 45 (5), 925-931 (2013)
   PUBMED   23416111
REFERENCE   6  (residues 1 to 307)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   7  (residues 1 to 307)
  AUTHORS   Panayiotou,C., Solaroli,N., Xu,Y., Johansson,M. and Karlsson,A.
  TITLE     The characterization of human adenylate kinases 7 and 8
            demonstrates differences in kinetic parameters and structural
            organization among the family of adenylate kinase isoenzymes
  JOURNAL   Biochem J 433 (3), 527-534 (2011)
   PUBMED   21080915
  REMARK    GeneRIF: Both AK7 and full-length AK8 showed highest affinity for
            AMP with ATP as the phosphate donor, and proved to be more
            efficient in AMP phosphorylation as compared with the major
            cytosolic isoform AK1
REFERENCE   8  (residues 1 to 307)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 307)
  AUTHORS   Lesch,K.P., Timmesfeld,N., Renner,T.J., Halperin,R., Roser,C.,
            Nguyen,T.T., Craig,D.W., Romanos,J., Heine,M., Meyer,J.,
            Freitag,C., Warnke,A., Romanos,M., Schafer,H., Walitza,S., Reif,A.,
            Stephan,D.A. and Jacob,C.
  TITLE     Molecular genetics of adult ADHD: converging evidence from
            genome-wide association and extended pedigree linkage studies
  JOURNAL   J Neural Transm (Vienna) 115 (11), 1573-1585 (2008)
   PUBMED   18839057
REFERENCE   10 (residues 1 to 307)
  AUTHORS   Van Rompay,A.R., Johansson,M. and Karlsson,A.
  TITLE     Identification of a novel human adenylate kinase. cDNA cloning,
            expression analysis, chromosome localization and characterization
            of the recombinant protein
  JOURNAL   Eur J Biochem 261 (2), 509-517 (1999)
   PUBMED   10215863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445645.10 and AL160165.17.
            
            On Dec 17, 2015 this sequence version replaced XP_011516581.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC037402.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..307
                     /product="adenylate kinase 8 isoform 3"
                     /EC_number="2.7.4.3"
                     /EC_number="2.7.4.6"
                     /note="putative adenylate kinase-like protein C9orf98;
                     ATP-AMP transphosphorylase 8"
                     /calculated_mol_wt=35159
     Region          <14..>78
                     /region_name="PLN02842"
                     /note="nucleotide kinase"
                     /db_xref="CDD:178435"
     Region          98..290
                     /region_name="ADK"
                     /note="Adenylate kinase (ADK) catalyzes the reversible
                     phosphoryl transfer from adenosine triphosphates (ATP) to
                     adenosine monophosphates (AMP) and to yield adenosine
                     diphosphates (ADP). This enzyme is required for the
                     biosynthesis of ADP and is essential for...; cd01428"
                     /db_xref="CDD:238713"
     Site            order(127,132,155,181..182,184..185,189)
                     /site_type="other"
                     /note="AMP-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     Site            order(132,181,185,220,260,264)
                     /site_type="other"
                     /note="ATP-AMP (Ap5A)-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     CDS             1..307
                     /gene="AK8"
                     /gene_synonym="AK 8; C9orf98"
                     /coded_by="NM_001317959.2:939..1862"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:158067"
                     /db_xref="HGNC:HGNC:26526"
                     /db_xref="MIM:615365"
ORIGIN      
        1 mgvcrclsew laqkiyhttf dwppeseiqn rlmvpedise letaqklley hrnivrvips
       61 ypkilkvisa dqpcvdvfyq altyvqsnhr tnapftprvl llgpvgsgks lqaallaqky
      121 rlvnvccgql lkeavadrtt fgeliqpffe kemavpdsll mkvlsqrldq qdciqkgwvl
      181 hgvprdldqa hllnrlgynp nrvfflnvpf dsimerltlr ridpvtgery hlmykppptm
      241 eiqarllqnp kdaeeqvklk mdlfyrnsad leqlygsait lngdqdpytv feyiesgiin
      301 plpkkip
//
LOCUS       NP_001310222            1029 aa            linear   PRI 20-JAN-2026
DEFINITION  zinc finger protein 197 isoform 1 [Homo sapiens].
ACCESSION   NP_001310222 XP_005264840 XP_011547029
VERSION     NP_001310222.1
DBSOURCE    REFSEQ: accession NM_001323293.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Li,Z., Wang,D., Na,X., Schoen,S.R., Messing,E.M. and Wu,G.
  TITLE     The VHL protein recruits a novel KRAB-A domain protein to repress
            HIF-1alpha transcriptional activity
  JOURNAL   EMBO J 22 (8), 1857-1867 (2003)
   PUBMED   12682018
  REMARK    GeneRIF: a novel pVHL-interacting protein that functions as a
            negative regulator of hypoxia-inducible factor-1a (HIF-1alpha)
            transactivation; demonstrate that the KRAB-A domain in VHLaK
            mediates pVHL binding and functions as a transcriptional repression
            module
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Gonsky,R., Knauf,J.A., Elisei,R., Wang,J.W., Su,S. and Fagin,J.A.
  TITLE     Identification of rapid turnover transcripts overexpressed in
            thyroid tumors and thyroid cancer cell lines: use of a targeted
            differential RNA display method to select for mRNA subsets
  JOURNAL   Nucleic Acids Res 25 (19), 3823-3831 (1997)
   PUBMED   9380504
REFERENCE   4  (residues 1 to 1029)
  AUTHORS   Calabro,V., Pengue,G., Bartoli,P.C., Pagliuca,A., Featherstone,T.
            and Lania,L.
  TITLE     Positional cloning of cDNAs from the human chromosome 3p21-22
            region identifies a clustered organization of zinc-finger genes
  JOURNAL   Hum Genet 95 (1), 18-21 (1995)
   PUBMED   7814019
REFERENCE   5  (residues 1 to 1029)
  AUTHORS   Pengue,G., Calabro,V., Cannada-Bartoli,P., De Luca,P., Esposito,T.,
            Taillon-Miller,P., LaForgia,S., Druck,T., Huebner,K., D'Urso,M. et
            al.
  TITLE     YAC-assisted cloning of transcribed sequences from the human
            chromosome 3p21 region
  JOURNAL   Hum Mol Genet 2 (6), 791-796 (1993)
   PUBMED   8353497
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099669.2 and BQ002665.1.
            
            On or before Jul 8, 2016 this sequence version replaced
            XP_005264840.1, XP_011547029.1.
            
            Summary: This gene product belongs to the zinc finger protein
            superfamily, members of which are regulatory proteins characterized
            by nucleic acid-binding zinc finger domains. The encoded protein
            contains 20 tandemly arrayed C2H2-type zinc fingers, a
            Kruppel-associated box (KRAB) domain, and a SCAN box. This
            transcript turns over rapidly and contains 3' UTR AUUUA motifs,
            which are often a hallmark of rapid turnover. It is overexpressed
            in some thyroid papillary carcinomas. This gene is located in a
            cluster of zinc finger genes at 3p21. Naturally-occurring
            readthrough transcription is observed between this gene and the
            upstream zinc finger protein 660 gene and is represented by
            GeneID:110354863. [provided by RefSeq, May 2017].
            
            Transcript Variant: Variants 1 and 3 encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.276749.1,
                                           SRR1660803.233453.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1029
                     /product="zinc finger protein 197 isoform 1"
                     /note="zinc finger protein 166; VHL-associated KRAB-A
                     domain-containing protein; zinc finger protein with KRAB
                     and SCAN domains 9; pVHL-associated KRAB domain-containing
                     protein"
                     /calculated_mol_wt=118717
     Region          38..150
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          216..256
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          262..290
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14709.1)"
     Region          372..392
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          384..409
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          400..420
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(405,407,409,411..412,415..416,419,433,435,439..440,
                     443..444,447,461,463,465,467..468,471..472,475)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          424..853
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          428..448
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          456..476
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          484..504
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          512..532
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          540..560
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          568..588
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          596..616
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(601,603,605,607..608,611..612,615,629,631,635..636,
                     639..640,643,657,659,661,663..664,667..668,671)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          624..644
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          652..672
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          680..700
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          708..728
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          736..756
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          760..>1026
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          764..784
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          792..812
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(797,799,801,803..804,807..808,811,825,827,831..832,
                     835..836,839,853,855,857,859..860,863..864,867)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          820..840
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          848..868
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          876..896
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          904..924
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          932..952
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          960..980
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          988..1008
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..1029
                     /gene="ZNF197"
                     /gene_synonym="D3S1363E; P18; VHLaK; ZKSCAN9; ZNF166;
                     ZSCAN41"
                     /coded_by="NM_001323293.2:199..3288"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="GeneID:10168"
                     /db_xref="HGNC:HGNC:12988"
                     /db_xref="MIM:618359"
ORIGIN      
        1 mtrenvahna lrqeglvkgk ddtwkwgtsf qgssssvwet shlhfrqlry hetsgpqeal
       61 srlrelcrrw lrpeartkaq ilellvleqf lsilpgeirt wvqlhhpgsg eeavalveel
      121 qkdldgpaiq vpvlvkdqdt lqkvvsapgt tlppvlpgsh iaaeicphpp tdlvafnlqd
      181 pqhdspapea salsqeenpr nqlmalmllt aqpqelvmfe evsvcftsee waclgpiqra
      241 lywdvmleny gnvtslewet mteneevtsk psssqradsh kgtskrlqgs vpqvldfeee
      301 cewqvlasqw gnetderadt vkkvslcerd kkkrtppekq gqkwkelgds ltfgsaises
      361 ligtegkkfy kcdmcckhfn kishlinhrr ihtgekphkc kecgkgfiqr ssllmhlrnh
      421 sgekpykcne cgkafsqsay llnhqrihtg ekpykckecg kgfyrhsgli ihlrrhsger
      481 pykcnecgkv fsqnaylidh qrlhkgeepy kcnkcqkafi lkkslilhqr ihsgekpykc
      541 decgktfaqt tylidhqrlh saenpykcke cgkvfirsks lllhqrvhte kktfgckkcg
      601 kifssksnfi dhkrmhsrek pykctecgka ftqsaylfdh qrlhngekpy ecnecgkvfi
      661 lkkslilhqr fhtgenlyec kdcgkvfgsn rnlidherlh ngekpyecre cgktfimsks
      721 fmvhqklhtq ekaykcedcg kafsynssll vhrrihtgek pfecsecgra fssnrnlieh
      781 krihsgekpy ecdecgkcfi lkkslighqr ihtreksykc ndcgkvfsyr snliahqrih
      841 tgekpyacse cgkgftynrn liehqrihsg ektyechvcr kvltssrnlm vhqrihtgek
      901 pykcnecgkd fsqnknlvvh qrmhtgekpy ecdkcrksft skrnlvghqr ihtgekpygc
      961 ndcskvfrqr knltvhqkih tdekpcecdv sekefsqtsn lhlqqkihti eefswlqntn
     1021 eskieiqki
//
LOCUS       NP_001020026             267 aa            linear   PRI 20-JAN-2026
DEFINITION  zinc finger protein 197 isoform 2 [Homo sapiens].
ACCESSION   NP_001020026
VERSION     NP_001020026.1
DBSOURCE    REFSEQ: accession NM_001024855.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Li,Z., Wang,D., Na,X., Schoen,S.R., Messing,E.M. and Wu,G.
  TITLE     The VHL protein recruits a novel KRAB-A domain protein to repress
            HIF-1alpha transcriptional activity
  JOURNAL   EMBO J 22 (8), 1857-1867 (2003)
   PUBMED   12682018
  REMARK    GeneRIF: a novel pVHL-interacting protein that functions as a
            negative regulator of hypoxia-inducible factor-1a (HIF-1alpha)
            transactivation; demonstrate that the KRAB-A domain in VHLaK
            mediates pVHL binding and functions as a transcriptional repression
            module
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Gonsky,R., Knauf,J.A., Elisei,R., Wang,J.W., Su,S. and Fagin,J.A.
  TITLE     Identification of rapid turnover transcripts overexpressed in
            thyroid tumors and thyroid cancer cell lines: use of a targeted
            differential RNA display method to select for mRNA subsets
  JOURNAL   Nucleic Acids Res 25 (19), 3823-3831 (1997)
   PUBMED   9380504
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Calabro,V., Pengue,G., Bartoli,P.C., Pagliuca,A., Featherstone,T.
            and Lania,L.
  TITLE     Positional cloning of cDNAs from the human chromosome 3p21-22
            region identifies a clustered organization of zinc-finger genes
  JOURNAL   Hum Genet 95 (1), 18-21 (1995)
   PUBMED   7814019
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Pengue,G., Calabro,V., Cannada-Bartoli,P., De Luca,P., Esposito,T.,
            Taillon-Miller,P., LaForgia,S., Druck,T., Huebner,K., D'Urso,M. et
            al.
  TITLE     YAC-assisted cloning of transcribed sequences from the human
            chromosome 3p21 region
  JOURNAL   Hum Mol Genet 2 (6), 791-796 (1993)
   PUBMED   8353497
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY279353.1 and AY074878.1.
            
            Summary: This gene product belongs to the zinc finger protein
            superfamily, members of which are regulatory proteins characterized
            by nucleic acid-binding zinc finger domains. The encoded protein
            contains 20 tandemly arrayed C2H2-type zinc fingers, a
            Kruppel-associated box (KRAB) domain, and a SCAN box. This
            transcript turns over rapidly and contains 3' UTR AUUUA motifs,
            which are often a hallmark of rapid turnover. It is overexpressed
            in some thyroid papillary carcinomas. This gene is located in a
            cluster of zinc finger genes at 3p21. Naturally-occurring
            readthrough transcription is observed between this gene and the
            upstream zinc finger protein 660 gene and is represented by
            GeneID:110354863. [provided by RefSeq, May 2017].
            
            Transcript Variant: Variants 2 and 4 encode the same isoform (2).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY074878.1, SRR1660807.63541.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..267
                     /product="zinc finger protein 197 isoform 2"
                     /note="zinc finger protein 166; VHL-associated KRAB-A
                     domain-containing protein; zinc finger protein with KRAB
                     and SCAN domains 9; pVHL-associated KRAB domain-containing
                     protein"
                     /calculated_mol_wt=30098
     Region          38..150
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          216..257
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     CDS             1..267
                     /gene="ZNF197"
                     /gene_synonym="D3S1363E; P18; VHLaK; ZKSCAN9; ZNF166;
                     ZSCAN41"
                     /coded_by="NM_001024855.3:199..1002"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:10168"
                     /db_xref="HGNC:HGNC:12988"
                     /db_xref="MIM:618359"
ORIGIN      
        1 mtrenvahna lrqeglvkgk ddtwkwgtsf qgssssvwet shlhfrqlry hetsgpqeal
       61 srlrelcrrw lrpeartkaq ilellvleqf lsilpgeirt wvqlhhpgsg eeavalveel
      121 qkdldgpaiq vpvlvkdqdt lqkvvsapgt tlppvlpgsh iaaeicphpp tdlvafnlqd
      181 pqhdspapea salsqeenpr nqlmalmllt aqpqelvmfe evsvcftsee waclgpiqra
      241 lywdvmleny gnvtslgyrk yrrqrnk
//
LOCUS       NP_001358700             450 aa            linear   PRI 20-JAN-2026
DEFINITION  adenylate kinase 8 isoform 4 [Homo sapiens].
ACCESSION   NP_001358700
VERSION     NP_001358700.1
DBSOURCE    REFSEQ: accession NM_001371771.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Dougherty,G.W., Mizuno,K., Nothe-Menchen,T., Ikawa,Y., Boldt,K.,
            Ta-Shma,A., Aprea,I., Minegishi,K., Pang,Y.P., Pennekamp,P.,
            Loges,N.T., Raidt,J., Hjeij,R., Wallmeier,J., Mussaffi,H.,
            Perles,Z., Elpeleg,O., Rabert,F., Shiratori,H., Letteboer,S.J.,
            Horn,N., Young,S., Strunker,T., Stumme,F., Werner,C., Olbrich,H.,
            Takaoka,K., Ide,T., Twan,W.K., Biebach,L., Grosse-Onnebrink,J.,
            Klinkenbusch,J.A., Praveen,K., Bracht,D.C., Hoben,I.M., Junger,K.,
            Gutzlaff,J., Cindric,S., Aviram,M., Kaiser,T., Memari,Y.,
            Dzeja,P.P., Dworniczak,B., Ueffing,M., Roepman,R., Bartscherer,K.,
            Katsanis,N., Davis,E.E., Amirav,I., Hamada,H. and Omran,H.
  TITLE     CFAP45 deficiency causes situs abnormalities and asthenospermia by
            disrupting an axonemal adenine nucleotide homeostasis module
  JOURNAL   Nat Commun 11 (1), 5520 (2020)
   PUBMED   33139725
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Amiri,M., Conserva,F., Panayiotou,C., Karlsson,A. and Solaroli,N.
  TITLE     The human adenylate kinase 9 is a nucleoside mono- and diphosphate
            kinase
  JOURNAL   Int J Biochem Cell Biol 45 (5), 925-931 (2013)
   PUBMED   23416111
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Panayiotou,C., Solaroli,N., Xu,Y., Johansson,M. and Karlsson,A.
  TITLE     The characterization of human adenylate kinases 7 and 8
            demonstrates differences in kinetic parameters and structural
            organization among the family of adenylate kinase isoenzymes
  JOURNAL   Biochem J 433 (3), 527-534 (2011)
   PUBMED   21080915
  REMARK    GeneRIF: Both AK7 and full-length AK8 showed highest affinity for
            AMP with ATP as the phosphate donor, and proved to be more
            efficient in AMP phosphorylation as compared with the major
            cytosolic isoform AK1
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 450)
  AUTHORS   Lesch,K.P., Timmesfeld,N., Renner,T.J., Halperin,R., Roser,C.,
            Nguyen,T.T., Craig,D.W., Romanos,J., Heine,M., Meyer,J.,
            Freitag,C., Warnke,A., Romanos,M., Schafer,H., Walitza,S., Reif,A.,
            Stephan,D.A. and Jacob,C.
  TITLE     Molecular genetics of adult ADHD: converging evidence from
            genome-wide association and extended pedigree linkage studies
  JOURNAL   J Neural Transm (Vienna) 115 (11), 1573-1585 (2008)
   PUBMED   18839057
REFERENCE   10 (residues 1 to 450)
  AUTHORS   Van Rompay,A.R., Johansson,M. and Karlsson,A.
  TITLE     Identification of a novel human adenylate kinase. cDNA cloning,
            expression analysis, chromosome localization and characterization
            of the recombinant protein
  JOURNAL   Eur J Biochem 261 (2), 509-517 (1999)
   PUBMED   10215863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445645.10 and AL160165.17.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.402160.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..450
                     /product="adenylate kinase 8 isoform 4"
                     /EC_number="2.7.4.3"
                     /EC_number="2.7.4.6"
                     /note="putative adenylate kinase-like protein C9orf98;
                     ATP-AMP transphosphorylase 8"
                     /calculated_mol_wt=51403
     Region          <1..24
                     /region_name="DD_AK8"
                     /note="dimerization/docking (D/D) domain found in
                     adenylate kinase isoenzyme 8 (AK8) and similar proteins;
                     cd22979"
                     /db_xref="CDD:438548"
     Region          30..220
                     /region_name="ADK"
                     /note="Adenylate kinase (ADK) catalyzes the reversible
                     phosphoryl transfer from adenosine triphosphates (ATP) to
                     adenosine monophosphates (AMP) and to yield adenosine
                     diphosphates (ADP). This enzyme is required for the
                     biosynthesis of ADP and is essential for...; cd01428"
                     /db_xref="CDD:238713"
     Site            order(60,110,114,149,190,193)
                     /site_type="other"
                     /note="ATP-AMP (Ap5A)-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     Site            order(60,84,110..111,113..114,118)
                     /site_type="other"
                     /note="AMP-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     Region          241..433
                     /region_name="ADK"
                     /note="Adenylate kinase (ADK) catalyzes the reversible
                     phosphoryl transfer from adenosine triphosphates (ATP) to
                     adenosine monophosphates (AMP) and to yield adenosine
                     diphosphates (ADP). This enzyme is required for the
                     biosynthesis of ADP and is essential for...; cd01428"
                     /db_xref="CDD:238713"
     Site            order(270,275,298,324..325,327..328,332)
                     /site_type="other"
                     /note="AMP-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     Site            order(275,324,328,363,403,407)
                     /site_type="other"
                     /note="ATP-AMP (Ap5A)-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     CDS             1..450
                     /gene="AK8"
                     /gene_synonym="AK 8; C9orf98"
                     /coded_by="NM_001371771.1:97..1449"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:158067"
                     /db_xref="HGNC:HGNC:26526"
                     /db_xref="MIM:615365"
ORIGIN      
        1 mleqllihqp edpipfmiqh lhrdndnvpr ivilgppasg kttiamwlck hlnsslltle
       61 nlilnefsyt atearrlylq rktvpsallv qliqerlaee dcikqgwild gipetreqal
      121 riqtlgitpr hvivlsapdt vliernlgkr idpqtgeiyh ttfdwppese iqnrlmvped
      181 iseletaqkl leyhrnivrv ipsypkilkv isadqpcvdv fyqaltyvqs nhrtnapftp
      241 rvlllgpvgs gkslqaalla qkyrlvnvcc gqllkeavad rttfgeliqp ffekemavpd
      301 sllmkvlsqr ldqqdciqkg wvlhgvprdl dqahllnrlg ynpnrvffln vpfdsimerl
      361 tlrridpvtg eryhlmykpp ptmeiqarll qnpkdaeeqv klkmdlfyrn sadleqlygs
      421 aitlngdqdp ytvfeyiesg iinplpkkip
//
LOCUS       NP_001358703             275 aa            linear   PRI 20-JAN-2026
DEFINITION  adenylate kinase 8 isoform 2 [Homo sapiens].
ACCESSION   NP_001358703 XP_024303188
VERSION     NP_001358703.1
DBSOURCE    REFSEQ: accession NM_001371774.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Dougherty,G.W., Mizuno,K., Nothe-Menchen,T., Ikawa,Y., Boldt,K.,
            Ta-Shma,A., Aprea,I., Minegishi,K., Pang,Y.P., Pennekamp,P.,
            Loges,N.T., Raidt,J., Hjeij,R., Wallmeier,J., Mussaffi,H.,
            Perles,Z., Elpeleg,O., Rabert,F., Shiratori,H., Letteboer,S.J.,
            Horn,N., Young,S., Strunker,T., Stumme,F., Werner,C., Olbrich,H.,
            Takaoka,K., Ide,T., Twan,W.K., Biebach,L., Grosse-Onnebrink,J.,
            Klinkenbusch,J.A., Praveen,K., Bracht,D.C., Hoben,I.M., Junger,K.,
            Gutzlaff,J., Cindric,S., Aviram,M., Kaiser,T., Memari,Y.,
            Dzeja,P.P., Dworniczak,B., Ueffing,M., Roepman,R., Bartscherer,K.,
            Katsanis,N., Davis,E.E., Amirav,I., Hamada,H. and Omran,H.
  TITLE     CFAP45 deficiency causes situs abnormalities and asthenospermia by
            disrupting an axonemal adenine nucleotide homeostasis module
  JOURNAL   Nat Commun 11 (1), 5520 (2020)
   PUBMED   33139725
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Amiri,M., Conserva,F., Panayiotou,C., Karlsson,A. and Solaroli,N.
  TITLE     The human adenylate kinase 9 is a nucleoside mono- and diphosphate
            kinase
  JOURNAL   Int J Biochem Cell Biol 45 (5), 925-931 (2013)
   PUBMED   23416111
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Panayiotou,C., Solaroli,N., Xu,Y., Johansson,M. and Karlsson,A.
  TITLE     The characterization of human adenylate kinases 7 and 8
            demonstrates differences in kinetic parameters and structural
            organization among the family of adenylate kinase isoenzymes
  JOURNAL   Biochem J 433 (3), 527-534 (2011)
   PUBMED   21080915
  REMARK    GeneRIF: Both AK7 and full-length AK8 showed highest affinity for
            AMP with ATP as the phosphate donor, and proved to be more
            efficient in AMP phosphorylation as compared with the major
            cytosolic isoform AK1
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Lesch,K.P., Timmesfeld,N., Renner,T.J., Halperin,R., Roser,C.,
            Nguyen,T.T., Craig,D.W., Romanos,J., Heine,M., Meyer,J.,
            Freitag,C., Warnke,A., Romanos,M., Schafer,H., Walitza,S., Reif,A.,
            Stephan,D.A. and Jacob,C.
  TITLE     Molecular genetics of adult ADHD: converging evidence from
            genome-wide association and extended pedigree linkage studies
  JOURNAL   J Neural Transm (Vienna) 115 (11), 1573-1585 (2008)
   PUBMED   18839057
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Van Rompay,A.R., Johansson,M. and Karlsson,A.
  TITLE     Identification of a novel human adenylate kinase. cDNA cloning,
            expression analysis, chromosome localization and characterization
            of the recombinant protein
  JOURNAL   Eur J Biochem 261 (2), 509-517 (1999)
   PUBMED   10215863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445645.10 and AL160165.17.
            
            On Jul 25, 2019 this sequence version replaced XP_024303188.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.332887.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..275
                     /product="adenylate kinase 8 isoform 2"
                     /EC_number="2.7.4.3"
                     /EC_number="2.7.4.6"
                     /note="putative adenylate kinase-like protein C9orf98;
                     ATP-AMP transphosphorylase 8"
                     /calculated_mol_wt=31324
     Region          66..258
                     /region_name="ADK"
                     /note="Adenylate kinase (ADK) catalyzes the reversible
                     phosphoryl transfer from adenosine triphosphates (ATP) to
                     adenosine monophosphates (AMP) and to yield adenosine
                     diphosphates (ADP). This enzyme is required for the
                     biosynthesis of ADP and is essential for...; cd01428"
                     /db_xref="CDD:238713"
     Site            order(95,100,123,149..150,152..153,157)
                     /site_type="other"
                     /note="AMP-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     Site            order(100,149,153,188,228,232)
                     /site_type="other"
                     /note="ATP-AMP (Ap5A)-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     CDS             1..275
                     /gene="AK8"
                     /gene_synonym="AK 8; C9orf98"
                     /coded_by="NM_001371774.1:684..1511"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:158067"
                     /db_xref="HGNC:HGNC:26526"
                     /db_xref="MIM:615365"
ORIGIN      
        1 mvpedisele taqklleyhr nivrvipsyp kilkvisadq pcvdvfyqal tyvqsnhrtn
       61 apftprvlll gpvgsgkslq aallaqkyrl vnvccgqllk eavadrttfg eliqpffeke
      121 mavpdsllmk vlsqrldqqd ciqkgwvlhg vprdldqahl lnrlgynpnr vfflnvpfds
      181 imerltlrri dpvtgeryhl mykppptmei qarllqnpkd aeeqvklkmd lfyrnsadle
      241 qlygsaitln gdqdpytvfe yiesgiinpl pkkip
//
LOCUS       NP_001001734             165 aa            linear   PRI 20-JAN-2026
DEFINITION  sodium/potassium-transporting ATPase subunit alpha-4 isoform 2
            [Homo sapiens].
ACCESSION   NP_001001734
VERSION     NP_001001734.1
DBSOURCE    REFSEQ: accession NM_001001734.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Sweeney,M.D., Zhao,Z., Montagne,A., Nelson,A.R. and Zlokovic,B.V.
  TITLE     Blood-Brain Barrier: From Physiology to Disease and Back
  JOURNAL   Physiol Rev 99 (1), 21-78 (2019)
   PUBMED   30280653
  REMARK    Review article
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Laird,J.G., Pan,Y., Modestou,M., Yamaguchi,D.M., Song,H.,
            Sokolov,M. and Baker,S.A.
  TITLE     Identification of a VxP Targeting Signal in the Flagellar Na+ /K+
            -ATPase
  JOURNAL   Traffic 16 (12), 1239-1253 (2015)
   PUBMED   26373354
REFERENCE   4  (residues 1 to 165)
  AUTHORS   McDermott,J., Sanchez,G., Nangia,A.K. and Blanco,G.
  TITLE     Role of human Na,K-ATPase alpha 4 in sperm function, derived from
            studies in transgenic mice
  JOURNAL   Mol Reprod Dev 82 (3), 167-181 (2015)
   PUBMED   25640246
  REMARK    GeneRIF: Human ATP1A4 enhances mouse sperm motility and
            hyperactivity during capacitation.
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Rodova,M., Nguyen,A.N. and Blanco,G.
  TITLE     The transcription factor CREMtau and cAMP regulate promoter
            activity of the Na,K-ATPase alpha4 isoform
  JOURNAL   Mol Reprod Dev 73 (11), 1435-1447 (2006)
   PUBMED   16894555
  REMARK    GeneRIF: These results constitute the first demonstration of the
            transcriptional control of ATP1A4 gene expression by cAMP and by
            CREMtau, a transcription factor essential for male germ cell gene
            expression.
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Shamraj,O.I. and Lingrel,J.B.
  TITLE     A putative fourth Na+,K(+)-ATPase alpha-subunit gene is expressed
            in testis
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 12952-12956 (1994)
   PUBMED   7809153
REFERENCE   7  (residues 1 to 165)
  AUTHORS   Lingrel,J.B., Orlowski,J., Shull,M.M. and Price,E.M.
  TITLE     Molecular genetics of Na,K-ATPase
  JOURNAL   Prog Nucleic Acid Res Mol Biol 38, 37-89 (1990)
   PUBMED   2158121
  REMARK    Review article
REFERENCE   8  (residues 1 to 165)
  AUTHORS   Sverdlov,E.D., Broude,N.E., Sverdlov,V.E., Monastyrskaya,G.S.,
            Grishin,A.V., Petrukhin,K.E., Akopyanz,N.S., Modyanov,N.N. and
            Ovchinnikov,Yu.A.
  TITLE     Family of Na+,K+-ATPase genes. Intra-individual tissue-specific
            restriction fragment length polymorphism
  JOURNAL   FEBS Lett 221 (1), 129-133 (1987)
   PUBMED   2887455
  REMARK    Erratum:[FEBS Lett 1988 Jan 18;227(1):85]
REFERENCE   9  (residues 1 to 165)
  AUTHORS   Sverdlov,E.D., Monastyrskaya,G.S., Broude,N.E., Ushkaryov,Yu.A.,
            Allikmets,R.L., Melkov,A.M., Smirnov,Yu.V., Malyshev,I.V.,
            Dulobova,I.E., Petrukhin,K.E. et al.
  TITLE     The family of human Na+,K+-ATPase genes. No less than five genes
            and/or pseudogenes related to the alpha-subunit
  JOURNAL   FEBS Lett 217 (2), 275-278 (1987)
   PUBMED   3036582
REFERENCE   10 (residues 1 to 165)
  AUTHORS   Shull,M.M. and Lingrel,J.B.
  TITLE     Multiple genes encode the human Na+,K+-ATPase catalytic subunit
  JOURNAL   Proc Natl Acad Sci U S A 84 (12), 4039-4043 (1987)
   PUBMED   3035563
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121987.34 and BC028297.1.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type cation transport ATPases, and to the subfamily of Na+/K+
            -ATPases. Na+/K+ -ATPase is an integral membrane protein
            responsible for establishing and maintaining the electrochemical
            gradients of Na and K ions across the plasma membrane. These
            gradients are essential for osmoregulation, for sodium-coupled
            transport of a variety of organic and inorganic molecules, and for
            electrical excitability of nerve and muscle. This enzyme is
            composed of two subunits, a large catalytic subunit (alpha) and a
            smaller glycoprotein subunit (beta). The catalytic subunit of
            Na+/K+ -ATPase is encoded by multiple genes. This gene encodes an
            alpha 4 subunit. Alternatively spliced transcript variants encoding
            different isoforms have been identified. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (2) contains a distinct 5' UTR and
            lacks an in-frame portion of the 5' coding region, compared to
            variant 1. The resulting isoform (2), which has not been
            experimentally confirmed, has a shorter N-terminus when compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028297.1, BX402599.2 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.2"
     Protein         1..165
                     /product="sodium/potassium-transporting ATPase subunit
                     alpha-4 isoform 2"
                     /EC_number="7.2.2.13"
                     /note="ATPase, Na+/K+ transporting, alpha polypeptide-like
                     2; sodium/potassium-transporting ATPase alpha-4 chain;
                     sodium pump 4; Na+/K+ ATPase 4; Na+/K+ ATPase, alpha-D
                     polypeptide; sodium/potassium-transporting ATPase subunit
                     alpha-4; Na,K-ATPase subunit alpha-C; sodium pump subunit
                     alpha-4; ATPase, Na+/K+ transporting, alpha 4 polypeptide;
                     Na(+)/K(+) ATPase alpha-4 subunit; sodium-potassium ATPase
                     catalytic subunit alpha-4"
                     /calculated_mol_wt=19478
     Region          <1..162
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     CDS             1..165
                     /gene="ATP1A4"
                     /gene_synonym="ATP1AL2"
                     /coded_by="NM_001001734.2:118..615"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44255.1"
                     /db_xref="GeneID:480"
                     /db_xref="HGNC:HGNC:14073"
                     /db_xref="MIM:607321"
ORIGIN      
        1 miqalagfft yfvilaengf rpvdllgirl hwedkylndl edsygqqwty eqrkvveftc
       61 qtaffvtivv vqwadliisk trrnslfqqg mrnkvlifgi leetllaafl sytpgmdval
      121 rmyplkitww lcaipysili fvydeirkll irqhpdgwve retyy
//
LOCUS       NP_000062                551 aa            linear   PRI 20-JAN-2026
DEFINITION  cystathionine beta-synthase isoform 1 [Homo sapiens].
ACCESSION   NP_000062
VERSION     NP_000062.1
DBSOURCE    REFSEQ: accession NM_000071.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Hu,X.J., Sun,Y., Liu,G.J., Zhang,J., Zhang,L.X. and Peng,Y.H.
  TITLE     Cystathionine-beta-synthase expression correlates with tumour
            progression and adverse prognosis in patients with colon cancer
  JOURNAL   J Int Med Res 52 (9), 3000605241263726 (2024)
   PUBMED   39324183
  REMARK    GeneRIF: Cystathionine-beta-synthase expression correlates with
            tumour progression and adverse prognosis in patients with colon
            cancer.
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Mijatovic,E., Ascencao,K., Szabo,C. and Majtan,T.
  TITLE     Cellular turnover and degradation of the most common missense
            cystathionine beta-synthase variants causing homocystinuria
  JOURNAL   Protein Sci 33 (8), e5123 (2024)
   PUBMED   39041895
  REMARK    GeneRIF: Cellular turnover and degradation of the most common
            missense cystathionine beta-synthase variants causing
            homocystinuria.
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Al-Sadeq,D.W., Conter,C., Thanassoulas,A., Al-Dewik,N.,
            Safieh-Garabedian,B., Martinez-Cruz,L.A., Nasrallah,G.K.,
            Astegno,A. and Nomikos,M.
  TITLE     Biochemical and structural impact of two novel missense mutations
            in cystathionine beta-synthase gene associated with homocystinuria
  JOURNAL   Biochem J 481 (8), 569-585 (2024)
   PUBMED   38563463
  REMARK    GeneRIF: Biochemical and structural impact of two novel missense
            mutations in cystathionine beta-synthase gene associated with
            homocystinuria.
REFERENCE   4  (residues 1 to 551)
  AUTHORS   McCorvie,T.J., Adamoski,D., Machado,R.A.C., Tang,J., Bailey,H.J.,
            Ferreira,D.S.M., Strain-Damerell,C., Basle,A., Ambrosio,A.L.B.,
            Dias,S.M.G. and Yue,W.W.
  TITLE     Architecture and regulation of filamentous human cystathionine
            beta-synthase
  JOURNAL   Nat Commun 15 (1), 2931 (2024)
   PUBMED   38575566
  REMARK    GeneRIF: Architecture and regulation of filamentous human
            cystathionine beta-synthase.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Sacharow,S.J. and Levy,H.L.
  TITLE     Homocystinuria due to Cystathionine Beta-Synthase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301697
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Milewicz,D.M. and Cecchi,A.C.
  TITLE     Heritable Thoracic Aortic Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301299
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Kraus,J., Packman,S., Fowler,B. and Rosenberg,L.E.
  TITLE     Purification and properties of cystathionine beta-synthase from
            human liver. Evidence for identical subunits
  JOURNAL   J Biol Chem 253 (18), 6523-6528 (1978)
   PUBMED   681363
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Griffiths,R. and Tudball,N.
  TITLE     The molecular defect in a case of (cystathionine
            beta-synthase)-deficient homocystinuria
  JOURNAL   Eur J Biochem 74 (2), 269-273 (1977)
   PUBMED   404147
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Longhi,R.C., Fleisher,L.D., Tallan,H.H. and Gaull,G.E.
  TITLE     Cystathionine beta-synthase deficiency: a qualitative abnormality
            of the deficient enzyme modified by vitamin B6 therapy
  JOURNAL   Pediatr Res 11 (2), 100-103 (1977)
   PUBMED   840498
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC300040.1, BC000440.2,
            AL137314.1 and X82166.1.
            
            Summary: The protein encoded by this gene acts as a homotetramer to
            catalyze the conversion of homocysteine to cystathionine, the first
            step in the transsulfuration pathway. The encoded protein is
            allosterically activated by adenosyl-methionine and uses pyridoxal
            phosphate as a cofactor. Defects in this gene can cause
            cystathionine beta-synthase deficiency (CBSD), which can lead to
            homocystinuria. This gene is a major contributor to cellular
            hydrogen sulfide production. Multiple alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Feb 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X82166.1, BC000440.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398165.8/ ENSP00000381231.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..551
                     /product="cystathionine beta-synthase isoform 1"
                     /EC_number="4.2.1.22"
                     /note="serine sulfhydrase; beta-thionase; methylcysteine
                     synthase"
                     /calculated_mol_wt=60456
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35520.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     Region          76..544
                     /region_name="cysta_beta"
                     /note="cystathionine beta-synthase; TIGR01137"
                     /db_xref="CDD:273464"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     CDS             1..551
                     /gene="CBS"
                     /gene_synonym="HIP4"
                     /coded_by="NM_000071.3:151..1806"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13693.1"
                     /db_xref="GeneID:875"
                     /db_xref="HGNC:HGNC:1550"
                     /db_xref="MIM:613381"
ORIGIN      
        1 mpsetpqaev gptgcphrsg phsakgslek gspedkeake plwirpdaps rctwqlgrpa
       61 sesphhhtap akspkilpdi lkkigdtpmv rinkigkkfg lkcellakce ffnaggsvkd
      121 rislrmieda erdgtlkpgd tiieptsgnt giglalaaav rgyrciivmp ekmssekvdv
      181 lralgaeivr tptnarfdsp eshvgvawrl kneipnshil dqyrnasnpl ahydttadei
      241 lqqcdgkldm lvasvgtggt itgiarklke kcpgcriigv dpegsilaep eelnqteqtt
      301 yevegigydf iptvldrtvv dkwfksndee aftfarmlia qegllcggsa gstvavavka
      361 aqelqegqrc vvilpdsvrn ymtkflsdrw mlqkgflkee dltekkpwww hlrvqelgls
      421 apltvlptit cghtieilre kgfdqapvvd eagvilgmvt lgnmlsslla gkvqpsdqvg
      481 kviykqfkqi rltdtlgrls hilemdhfal vvheqiqyhs tgkssqrqmv fgvvtaidll
      541 nfvaaqerdq k
//
LOCUS       NP_001352236             139 aa            linear   PRI 20-JAN-2026
DEFINITION  uncharacterized protein LOC112694756 isoform 1 [Homo sapiens].
ACCESSION   NP_001352236
VERSION     NP_001352236.1
DBSOURCE    REFSEQ: accession NM_001365307.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Kimura,K., Wakamatsu,A., Suzuki,Y., Ota,T., Nishikawa,T.,
            Yamashita,R., Yamamoto,J., Sekine,M., Tsuritani,K., Wakaguri,H.,
            Ishii,S., Sugiyama,T., Saito,K., Isono,Y., Irie,R., Kushida,N.,
            Yoneyama,T., Otsuka,R., Kanda,K., Yokoi,T., Kondo,H., Wagatsuma,M.,
            Murakawa,K., Ishida,S., Ishibashi,T., Takahashi-Fujii,A.,
            Tanase,T., Nagai,K., Kikuchi,H., Nakai,K., Isogai,T. and Sugano,S.
  TITLE     Diversification of transcriptional modulation: large-scale
            identification and characterization of putative alternative
            promoters of human genes
  JOURNAL   Genome Res 16 (1), 55-65 (2006)
   PUBMED   16344560
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093512.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.604106.1,
                                           SRR1803611.44158.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: translation inferred from conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..139
                     /product="uncharacterized protein LOC112694756 isoform 1"
                     /calculated_mol_wt=14667
     CDS             1..139
                     /gene="LOC112694756"
                     /coded_by="NM_001365307.2:344..763"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92136.1"
                     /db_xref="GeneID:112694756"
ORIGIN      
        1 mdassspwnp tpapvssppl llpipaivfi avgiyllllg lvlltrncll aqgccadgss
       61 pcrkqgssgp pdccwtcaea cnfplpspah fldaccpqpt radwaprcpr ccplcdcact
      121 cqlpdcqsln clcfeiklr
//
LOCUS       NP_000097                497 aa            linear   PRI 20-JAN-2026
DEFINITION  cytochrome P450 2D6 isoform 1 [Homo sapiens].
ACCESSION   NP_000097
VERSION     NP_000097.3
DBSOURCE    REFSEQ: accession NM_000106.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 497)
  AUTHORS   Luo,X., Du,J., Zhao,J., Fan,M., Luo,X., Zhao,P., Zheng,P., Mo,L.
            and Li,Y.
  TITLE     Genetic susceptibility and clinical features of CYP2D6 associated
            with systemic lupus erythematosus in a Chinese population
  JOURNAL   Lupus 33 (12), 1328-1335 (2024)
   PUBMED   39287122
  REMARK    GeneRIF: Genetic susceptibility and clinical features of CYP2D6
            associated with systemic lupus erythematosus in a Chinese
            population.
REFERENCE   2  (residues 1 to 497)
  AUTHORS   Datkhile,K.D., More,A.L., Patil,M.N., Gudur,R.A. and Gudur,A.K.
  TITLE     CYP2D6, CYP2E1 Gene Polymorphisms and Gastrointestinal Cancer Risk
            in Rural Maharashtra: A Hospital Based Case-Control Study
  JOURNAL   Asian Pac J Cancer Prev 25 (9), 3059-3065 (2024)
   PUBMED   39342583
  REMARK    GeneRIF: CYP2D6, CYP2E1 Gene Polymorphisms and Gastrointestinal
            Cancer Risk in Rural Maharashtra: A Hospital Based Case-Control
            Study.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 497)
  AUTHORS   Becker,D., Bharatam,P.V. and Gohlke,H.
  TITLE     Molecular Mechanisms Underlying Single Nucleotide
            Polymorphism-Induced Reactivity Decrease in CYP2D6
  JOURNAL   J Chem Inf Model 64 (15), 6026-6040 (2024)
   PUBMED   38994927
  REMARK    GeneRIF: Molecular Mechanisms Underlying Single Nucleotide
            Polymorphism-Induced Reactivity Decrease in CYP2D6.
REFERENCE   4  (residues 1 to 497)
  AUTHORS   Wei,Y.J., Winterstein,A.G., Schmidt,S., Fillingim,R.B.,
            Daniels,M.J., DeKosky,S.T. and Schmidt,S.
  TITLE     Clinical and Adverse Outcomes Associated With Concomitant Use of
            CYP2D6-Metabolized Opioids With Antidepressants in Older Nursing
            Home Residents : A Target Trial Emulation Study
  JOURNAL   Ann Intern Med 177 (8), 1058-1068 (2024)
   PUBMED   39038293
  REMARK    GeneRIF: Clinical and Adverse Outcomes Associated With Concomitant
            Use of CYP2D6-Metabolized Opioids With Antidepressants in Older
            Nursing Home Residents : A Target Trial Emulation Study.
REFERENCE   5  (residues 1 to 497)
  AUTHORS   Li,D., Pain,O., Fabbri,C., Wong,W.L.E., Lo,C.W.H., Ripke,S.,
            Cattaneo,A., Souery,D., Dernovsek,M.Z., Henigsberg,N., Hauser,J.,
            Lewis,G., Mors,O., Perroud,N., Rietschel,M., Uher,R., Maier,W.,
            Baune,B.T., Biernacka,J.M., Bondolfi,G., Domschke,K., Kato,M.,
            Liu,Y.L., Serretti,A., Tsai,S.J., Weinshilboum,R., McIntosh,A.M.
            and Lewis,C.M.
  CONSRTM   GSRD Consortium, the Major Depressive Disorder Working Group of the
            Psychiatric Genomics Consortium
  TITLE     Metabolic activity of CYP2C19 and CYP2D6 on antidepressant response
            from 13 clinical studies using genotype imputation: a meta-analysis
  JOURNAL   Transl Psychiatry 14 (1), 296 (2024)
   PUBMED   39025838
  REMARK    GeneRIF: Metabolic activity of CYP2C19 and CYP2D6 on antidepressant
            response from 13 clinical studies using genotype imputation: a
            meta-analysis.
            Erratum:[Transl Psychiatry. 2024 Aug 31;14(1):350. doi:
            10.1038/s41398-024-03064-x. PMID: 39217139]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 497)
  AUTHORS   Nelson,D.R., Zeldin,D.C., Hoffman,S.M., Maltais,L.J., Wain,H.M. and
            Nebert,D.W.
  TITLE     Comparison of cytochrome P450 (CYP) genes from the mouse and human
            genomes, including nomenclature recommendations for genes,
            pseudogenes and alternative-splice variants
  JOURNAL   Pharmacogenetics 14 (1), 1-18 (2004)
   PUBMED   15128046
  REMARK    Review article
REFERENCE   7  (residues 1 to 497)
  AUTHORS   Tyndale,R., Aoyama,T., Broly,F., Matsunaga,T., Inaba,T., Kalow,W.,
            Gelboin,H.V., Meyer,U.A. and Gonzalez,F.J.
  TITLE     Identification of a new variant CYP2D6 allele lacking the codon
            encoding Lys-281: possible association with the poor metabolizer
            phenotype
  JOURNAL   Pharmacogenetics 1 (1), 26-32 (1991)
   PUBMED   1844820
REFERENCE   8  (residues 1 to 497)
  AUTHORS   Gaedigk,A., Blum,M., Gaedigk,R., Eichelbaum,M. and Meyer,U.A.
  TITLE     Deletion of the entire cytochrome P450 CYP2D6 gene as a cause of
            impaired drug metabolism in poor metabolizers of the
            debrisoquine/sparteine polymorphism
  JOURNAL   Am J Hum Genet 48 (5), 943-950 (1991)
   PUBMED   1673290
REFERENCE   9  (residues 1 to 497)
  AUTHORS   Hanioka,N., Kimura,S., Meyer,U.A. and Gonzalez,F.J.
  TITLE     The human CYP2D locus associated with a common genetic defect in
            drug oxidation: a G1934----A base change in intron 3 of a mutant
            CYP2D6 allele results in an aberrant 3' splice recognition site
  JOURNAL   Am J Hum Genet 47 (6), 994-1001 (1990)
   PUBMED   1978565
REFERENCE   10 (residues 1 to 497)
  AUTHORS   Gough,A.C., Miles,J.S., Spurr,N.K., Moss,J.E., Gaedigk,A.,
            Eichelbaum,M. and Wolf,C.R.
  TITLE     Identification of the primary gene defect at the cytochrome P450
            CYP2D locus
  JOURNAL   Nature 347 (6295), 773-776 (1990)
   PUBMED   1978251
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC075023.2 and AW297258.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 22, 2012 this sequence version replaced NP_000097.2.
            
            Summary: This gene encodes a member of the cytochrome P450
            superfamily of enzymes. The cytochrome P450 proteins are
            monooxygenases which catalyze many reactions involved in drug
            metabolism and synthesis of cholesterol, steroids and other lipids.
            This protein localizes to the endoplasmic reticulum and is known to
            metabolize as many as 25% of commonly prescribed drugs. Its
            substrates include antidepressants, antipsychotics, analgesics and
            antitussives, beta adrenergic blocking agents, antiarrythmics and
            antiemetics. The gene is highly polymorphic in the human
            population; certain alleles result in the poor metabolizer
            phenotype, characterized by a decreased ability to metabolize the
            enzyme's substrates. Some individuals with the poor metabolizer
            phenotype have no functional protein since they carry 2 null
            alleles whereas in other individuals the gene is absent. This gene
            can vary in copy number and individuals with the ultrarapid
            metabolizer phenotype can have 3 or more active copies of the gene.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jul
            2014].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC075023.2, M20403.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000645361.2/ ENSP00000496150.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..497
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..497
                     /product="cytochrome P450 2D6 isoform 1"
                     /EC_number="1.14.14.1"
                     /note="debrisoquine 4-hydroxylase; microsomal
                     monooxygenase; xenobiotic monooxygenase;
                     flavoprotein-linked monooxygenase; cytochrome P450,
                     subfamily IID (debrisoquine, sparteine, etc.,
                     -metabolizing), polypeptide 6; cholesterol 25-hydroxylase;
                     nonfunctional cytochrome P450 2D6; cytochrome P450,
                     subfamily IID (debrisoquine, sparteine, etc.,
                     -metabolizing)-like 1; cytochrome P450-DB1; cytochrome
                     P450, family 2, subfamily D, polypeptide 6"
                     /calculated_mol_wt=55639
     Region          65..492
                     /region_name="CYP2D"
                     /note="cytochrome P450 family 2, subfamily D; cd20663"
                     /db_xref="CDD:410756"
     Site            order(101,119..120,128,132,302,305..306,309..310,313,364,
                     374,376,399,435..437,441,443..445,448)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410756"
     Site            order(110,120,212..213,216,244,247..248,300..301,304..305,
                     309,483)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410756"
     CDS             1..497
                     /gene="CYP2D6"
                     /gene_synonym="CPD6; CYP2D; CYP2D7AP; CYP2D7BP; CYP2D7P2;
                     CYP2D8P2; CYP2DL1; CYPIID6; P450-DB1; P450C2D; P450DB1"
                     /coded_by="NM_000106.6:20..1513"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46721.1"
                     /db_xref="GeneID:1565"
                     /db_xref="HGNC:HGNC:2625"
                     /db_xref="MIM:124030"
ORIGIN      
        1 mglealvpla vivaiflllv dlmhrrqrwa aryppgplpl pglgnllhvd fqntpycfdq
       61 lrrrfgdvfs lqlawtpvvv lnglaavrea lvthgedtad rppvpitqil gfgprsqgvf
      121 larygpawre qrrfsvstlr nlglgkksle qwvteeaacl caafanhsgr pfrpnglldk
      181 avsnviaslt cgrrfeyddp rflrlldlaq eglkeesgfl revlnavpvl lhipalagkv
      241 lrfqkafltq ldelltehrm twdpaqpprd lteaflaeme kakgnpessf ndenlrivva
      301 dlfsagmvtt sttlawglll milhpdvqrr vqqeiddvig qvrrpemgdq ahmpyttavi
      361 hevqrfgdiv plgvthmtsr dievqgfrip kgttlitnls svlkdeavwe kpfrfhpehf
      421 ldaqghfvkp eaflpfsagr raclgeplar melflfftsl lqhfsfsvpt gqprpshhgv
      481 faflvspspy elcavpr
//
LOCUS       NP_653300               1029 aa            linear   PRI 20-JAN-2026
DEFINITION  sodium/potassium-transporting ATPase subunit alpha-4 isoform 1
            [Homo sapiens].
ACCESSION   NP_653300 XP_086379
VERSION     NP_653300.2
DBSOURCE    REFSEQ: accession NM_144699.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Sweeney,M.D., Zhao,Z., Montagne,A., Nelson,A.R. and Zlokovic,B.V.
  TITLE     Blood-Brain Barrier: From Physiology to Disease and Back
  JOURNAL   Physiol Rev 99 (1), 21-78 (2019)
   PUBMED   30280653
  REMARK    Review article
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Laird,J.G., Pan,Y., Modestou,M., Yamaguchi,D.M., Song,H.,
            Sokolov,M. and Baker,S.A.
  TITLE     Identification of a VxP Targeting Signal in the Flagellar Na+ /K+
            -ATPase
  JOURNAL   Traffic 16 (12), 1239-1253 (2015)
   PUBMED   26373354
REFERENCE   4  (residues 1 to 1029)
  AUTHORS   McDermott,J., Sanchez,G., Nangia,A.K. and Blanco,G.
  TITLE     Role of human Na,K-ATPase alpha 4 in sperm function, derived from
            studies in transgenic mice
  JOURNAL   Mol Reprod Dev 82 (3), 167-181 (2015)
   PUBMED   25640246
  REMARK    GeneRIF: Human ATP1A4 enhances mouse sperm motility and
            hyperactivity during capacitation.
REFERENCE   5  (residues 1 to 1029)
  AUTHORS   Rodova,M., Nguyen,A.N. and Blanco,G.
  TITLE     The transcription factor CREMtau and cAMP regulate promoter
            activity of the Na,K-ATPase alpha4 isoform
  JOURNAL   Mol Reprod Dev 73 (11), 1435-1447 (2006)
   PUBMED   16894555
  REMARK    GeneRIF: These results constitute the first demonstration of the
            transcriptional control of ATP1A4 gene expression by cAMP and by
            CREMtau, a transcription factor essential for male germ cell gene
            expression.
REFERENCE   6  (residues 1 to 1029)
  AUTHORS   Shamraj,O.I. and Lingrel,J.B.
  TITLE     A putative fourth Na+,K(+)-ATPase alpha-subunit gene is expressed
            in testis
  JOURNAL   Proc Natl Acad Sci U S A 91 (26), 12952-12956 (1994)
   PUBMED   7809153
REFERENCE   7  (residues 1 to 1029)
  AUTHORS   Lingrel,J.B., Orlowski,J., Shull,M.M. and Price,E.M.
  TITLE     Molecular genetics of Na,K-ATPase
  JOURNAL   Prog Nucleic Acid Res Mol Biol 38, 37-89 (1990)
   PUBMED   2158121
  REMARK    Review article
REFERENCE   8  (residues 1 to 1029)
  AUTHORS   Sverdlov,E.D., Broude,N.E., Sverdlov,V.E., Monastyrskaya,G.S.,
            Grishin,A.V., Petrukhin,K.E., Akopyanz,N.S., Modyanov,N.N. and
            Ovchinnikov,Yu.A.
  TITLE     Family of Na+,K+-ATPase genes. Intra-individual tissue-specific
            restriction fragment length polymorphism
  JOURNAL   FEBS Lett 221 (1), 129-133 (1987)
   PUBMED   2887455
  REMARK    Erratum:[FEBS Lett 1988 Jan 18;227(1):85]
REFERENCE   9  (residues 1 to 1029)
  AUTHORS   Sverdlov,E.D., Monastyrskaya,G.S., Broude,N.E., Ushkaryov,Yu.A.,
            Allikmets,R.L., Melkov,A.M., Smirnov,Yu.V., Malyshev,I.V.,
            Dulobova,I.E., Petrukhin,K.E. et al.
  TITLE     The family of human Na+,K+-ATPase genes. No less than five genes
            and/or pseudogenes related to the alpha-subunit
  JOURNAL   FEBS Lett 217 (2), 275-278 (1987)
   PUBMED   3036582
REFERENCE   10 (residues 1 to 1029)
  AUTHORS   Shull,M.M. and Lingrel,J.B.
  TITLE     Multiple genes encode the human Na+,K+-ATPase catalytic subunit
  JOURNAL   Proc Natl Acad Sci U S A 84 (12), 4039-4043 (1987)
   PUBMED   3035563
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB094047.1, BC094801.1,
            BC036052.1, BX647234.1, AL121987.34 and BC028297.1.
            
            On Jul 26, 2007 this sequence version replaced NP_653300.1.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type cation transport ATPases, and to the subfamily of Na+/K+
            -ATPases. Na+/K+ -ATPase is an integral membrane protein
            responsible for establishing and maintaining the electrochemical
            gradients of Na and K ions across the plasma membrane. These
            gradients are essential for osmoregulation, for sodium-coupled
            transport of a variety of organic and inorganic molecules, and for
            electrical excitability of nerve and muscle. This enzyme is
            composed of two subunits, a large catalytic subunit (alpha) and a
            smaller glycoprotein subunit (beta). The catalytic subunit of
            Na+/K+ -ATPase is encoded by multiple genes. This gene encodes an
            alpha 4 subunit. Alternatively spliced transcript variants encoding
            different isoforms have been identified. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript, and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647234.1, AF506797.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368081.9/ ENSP00000357060.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.2"
     Protein         1..1029
                     /product="sodium/potassium-transporting ATPase subunit
                     alpha-4 isoform 1"
                     /EC_number="7.2.2.13"
                     /note="ATPase, Na+/K+ transporting, alpha polypeptide-like
                     2; sodium/potassium-transporting ATPase alpha-4 chain;
                     sodium pump 4; Na+/K+ ATPase 4; Na+/K+ ATPase, alpha-D
                     polypeptide; sodium/potassium-transporting ATPase subunit
                     alpha-4; Na,K-ATPase subunit alpha-C; sodium pump subunit
                     alpha-4; ATPase, Na+/K+ transporting, alpha 4 polypeptide;
                     Na(+)/K(+) ATPase alpha-4 subunit; sodium-potassium ATPase
                     catalytic subunit alpha-4"
                     /calculated_mol_wt=114036
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13733.3)"
     Region          70..1026
                     /region_name="P-type_ATPase_Na-K_like"
                     /note="alpha-subunit of Na(+)/K(+)-ATPases and of gastric
                     H(+)/K(+)-ATPase, similar to the human Na(+)/K(+)-ATPase
                     alpha subunits 1-4; cd02608"
                     /db_xref="CDD:319794"
     Region          90..92
                     /region_name="Interaction with phosphoinositide-3 kinase.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13733.3)"
     Site            96..116
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13733.3)"
     Site            140..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13733.3)"
     Region          223..242
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13733.3)"
     Site            297..316
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13733.3)"
     Site            329..346
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13733.3)"
     Site            order(337,340,342,789,792,817)
                     /site_type="other"
                     /note="K binding site [ion binding]"
                     /db_xref="CDD:319794"
     Site            order(342,789,792,817)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:319794"
     Site            order(384..386,458,461,489..490,492,495,497,515..517,
                     558..560,623..625,698,701,704,723..727)
                     /site_type="other"
                     /note="ATP-binding site [chemical binding]"
                     /db_xref="CDD:319794"
     Site            779..798
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13733.3)"
     Site            order(784,788,821,936)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:319794"
     Site            order(788..789,792,817,821)
                     /site_type="other"
                     /note="K binding site [ion binding]"
                     /db_xref="CDD:319794"
     Site            order(788..789,792,817)
                     /site_type="other"
                     /note="Na binding site [ion binding]"
                     /db_xref="CDD:319794"
     Site            809..829
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13733.3)"
     Site            850..872
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13733.3)"
     Site            order(861..862,865..866,869,873,877,881..882,898..900,
                     902..903,907..916,919..920,990,992..993,1000,1003,1007,
                     1022,1025..1026)
                     /site_type="other"
                     /note="alpha-subunit/beta-subunit interface [polypeptide
                     binding]"
                     /db_xref="CDD:319794"
     Site            925..944
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13733.3)"
     Site            949
                     /site_type="phosphorylation"
                     /note="phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:319794"
     Site            949
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q13733.3)"
     Site            958..976
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13733.3)"
     Site            992..1012
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13733.3)"
     CDS             1..1029
                     /gene="ATP1A4"
                     /gene_synonym="ATP1AL2"
                     /coded_by="NM_144699.4:439..3528"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1197.1"
                     /db_xref="GeneID:480"
                     /db_xref="HGNC:HGNC:14073"
                     /db_xref="MIM:607321"
ORIGIN      
        1 mglwgkkgtv aphdqsprrr pkkglikkkm vkrekqkrnm eelkkevvmd dhkltleels
       61 tkysvdltkg hshqrakeil trggpntvtp ppttpewvkf ckqlfggfsl llwtgailcf
      121 vaysiqiyfn eeptkdnlyl sivlsvvviv tgcfsyyqea ksskimesfk nmvpqqalvi
      181 rggekmqinv qevvlgdlve ikggdrvpad lrlisaqgck vdnssltges epqsrspdft
      241 henpletrni cffstncveg targiviatg dstvmgrias ltsglavgqt piaaeiehfi
      301 hlitvvavfl gvtffalsll lgygwleaii fligiivanv pegllatvtv cltltakrma
      361 rknclvknle avetlgstst icsdktgtlt qnrmtvahmw fdmtvyeadt teeqtgktft
      421 kssdtwfmla riaglcnrad fkanqeilpi akrattgdas esallkfieq syssvaemre
      481 knpkvaeipf nstnkyqmsi hlredssqth vlmmkgaper ilefcstfll ngqeysmnde
      541 mkeafqnayl elgglgervl gfcflnlpss fskgfpfntd einfpmdnlc fvglismidp
      601 praavpdavs kcrsagikvi mvtgdhpita kaiakgvgii segtetaeev aarlkipisk
      661 vdasaakaiv vhgaelkdiq skqldqilqn hpeivfarts pqqkliiveg cqrlgavvav
      721 tgdgvndspa lkkadigiam gisgsdvskq aadmillddn fasivtgvee grlifdnlkk
      781 simytltsni peitpflmfi ilgiplplgt itilcidlgt dmvpaislay esaesdimkr
      841 lprnpktdnl vnhrligmay gqigmiqala gfftyfvila engfrpvdll girlhwedky
      901 lndledsygq qwtyeqrkvv eftcqtaffv tivvvqwadl iisktrrnsl fqqgmrnkvl
      961 ifgileetll aaflsytpgm dvalrmyplk itwwlcaipy silifvydei rkllirqhpd
     1021 gwveretyy
//
LOCUS       NP_001307889             648 aa            linear   PRI 20-JAN-2026
DEFINITION  leukocyte immunoglobulin-like receptor subfamily B member 3 isoform
            3 precursor [Homo sapiens].
ACCESSION   NP_001307889 XP_011524685
VERSION     NP_001307889.1
DBSOURCE    REFSEQ: accession NM_001320960.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Hirayasu,K., Khor,S.S., Kawai,Y., Shimada,M., Omae,Y., Hasegawa,G.,
            Hashikawa,Y., Tanimoto,H., Ohashi,J., Hosomichi,K., Tajima,A.,
            Nakamura,H., Nakamura,M., Tokunaga,K., Hanayama,R. and Nagasaki,M.
  TITLE     Identification of the hybrid gene LILRB5-3 by long-read sequencing
            and implication of its novel signaling function
  JOURNAL   Front Immunol 15, 1398935 (2024)
   PUBMED   38807600
  REMARK    GeneRIF: Identification of the hybrid gene LILRB5-3 by long-read
            sequencing and implication of its novel signaling function.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Bashirova,A.A., Kasprzak,W., O'hUigin,C. and Carrington,M.
  TITLE     Distinct frequency patterns of LILRB3 and LILRA6 allelic variants
            in Europeans
  JOURNAL   Immunogenetics 75 (3), 263-267 (2023)
   PUBMED   36449053
  REMARK    GeneRIF: Distinct frequency patterns of LILRB3 and LILRA6 allelic
            variants in Europeans.
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Zhou,J., Wang,Y., Huang,G., Yang,M., Zhu,Y., Jin,C., Jing,D., Ji,K.
            and Shi,Y.
  TITLE     LilrB3 is a putative cell surface receptor of APOE4
  JOURNAL   Cell Res 33 (2), 116-130 (2023)
   PUBMED   36588123
  REMARK    GeneRIF: LilrB3 is a putative cell surface receptor of APOE4.
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Wu,G., Xu,Y., Schultz,R.D., Chen,H., Xie,J., Deng,M., Liu,X.,
            Gui,X., John,S., Lu,Z., Arase,H., Zhang,N., An,Z. and Zhang,C.C.
  TITLE     LILRB3 supports acute myeloid leukemia development and regulates
            T-cell antitumor immune responses through the TRAF2-cFLIP-NF-kappaB
            signaling axis
  JOURNAL   Nat Cancer 2 (11), 1170-1184 (2021)
   PUBMED   35122056
  REMARK    GeneRIF: LILRB3 supports acute myeloid leukemia development and
            regulates T-cell antitumor immune responses through the
            TRAF2-cFLIP-NF-kappaB signaling axis.
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Ayukawa,S., Kamoshita,N., Nakayama,J., Teramoto,R., Pishesha,N.,
            Ohba,K., Sato,N., Kozawa,K., Abe,H., Semba,K., Goda,N., Fujita,Y.
            and Maruyama,T.
  TITLE     Epithelial cells remove precancerous cells by cell competition via
            MHC class I-LILRB3 interaction
  JOURNAL   Nat Immunol 22 (11), 1391-1402 (2021)
   PUBMED   34686865
  REMARK    GeneRIF: Epithelial cells remove precancerous cells by cell
            competition via MHC class I-LILRB3 interaction.
REFERENCE   6  (residues 1 to 648)
  AUTHORS   Bashirova,A.A., Apps,R., Vince,N., Mochalova,Y., Yu,X.G. and
            Carrington,M.
  TITLE     Diversity of the human LILRB3/A6 locus encoding a myeloid
            inhibitory and activating receptor pair
  JOURNAL   Immunogenetics 66 (1), 1-8 (2014)
   PUBMED   24096970
REFERENCE   7  (residues 1 to 648)
  AUTHORS   Colonna,M., Navarro,F., Bellon,T., Llano,M., Garcia,P.,
            Samaridis,J., Angman,L., Cella,M. and Lopez-Botet,M.
  TITLE     A common inhibitory receptor for major histocompatibility complex
            class I molecules on human lymphoid and myelomonocytic cells
  JOURNAL   J Exp Med 186 (11), 1809-1818 (1997)
   PUBMED   9382880
REFERENCE   8  (residues 1 to 648)
  AUTHORS   Arm,J.P., Nwankwo,C. and Austen,K.F.
  TITLE     Molecular identification of a novel family of human Ig superfamily
            members that possess immunoreceptor tyrosine-based inhibition
            motifs and homology to the mouse gp49B1 inhibitory receptor
  JOURNAL   J Immunol 159 (5), 2342-2349 (1997)
   PUBMED   9278324
REFERENCE   9  (residues 1 to 648)
  AUTHORS   Cella,M., Dohring,C., Samaridis,J., Dessing,M., Brockhaus,M.,
            Lanzavecchia,A. and Colonna,M.
  TITLE     A novel inhibitory receptor (ILT3) expressed on monocytes,
            macrophages, and dendritic cells involved in antigen processing
  JOURNAL   J Exp Med 185 (10), 1743-1751 (1997)
   PUBMED   9151699
REFERENCE   10 (residues 1 to 648)
  AUTHORS   Samaridis,J. and Colonna,M.
  TITLE     Cloning of novel immunoglobulin superfamily receptors expressed on
            human myeloid and lymphoid cells: structural evidence for new
            stimulatory and inhibitory pathways
  JOURNAL   Eur J Immunol 27 (3), 660-665 (1997)
   PUBMED   9079806
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA843308.1, AF009633.1,
            AF009637.1, AC245052.3, BC028153.1 and CA434108.1.
            
            On Mar 12, 2016 this sequence version replaced XP_011524685.1.
            
            Summary: This gene is a member of the leukocyte immunoglobulin-like
            receptor (LIR) family, which is found in a gene cluster at
            chromosomal region 19q13.4. The encoded protein belongs to the
            subfamily B class of LIR receptors which contain two or four
            extracellular immunoglobulin domains, a transmembrane domain, and
            two to four cytoplasmic immunoreceptor tyrosine-based inhibitory
            motifs (ITIMs). The receptor is expressed on immune cells where it
            binds to MHC class I molecules on antigen-presenting cells and
            transduces a negative signal that inhibits stimulation of an immune
            response. It is thought to control inflammatory responses and
            cytotoxicity to help focus the immune response and limit
            autoreactivity. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF009637.1, DRR138517.417252.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..648
                     /product="leukocyte immunoglobulin-like receptor subfamily
                     B member 3 isoform 3 precursor"
                     /note="monocyte inhibitory receptor HL9;
                     immunoglobulin-like transcript 5; CD85 antigen-like family
                     member A; leukocyte immunoglobulin-like receptor,
                     subfamily B (with TM and ITIM domains), member 3;
                     leucocyte Ig-like receptor B3; leukocyte
                     immunoglobulin-like receptor subfamily B member 3"
                     /calculated_mol_wt=68679
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2415
     Region          28..116
                     /region_name="IgC2_D1_LILR_KIR_like"
                     /note="First immunoglobulin (Ig)-like domain found in
                     Leukocyte Ig-like receptors (LILRs), Natural killer
                     inhibitory receptors (KIRs) and similar domains; member of
                     Immunoglobulin Constant-2 set of IgSF domains; cd05751"
                     /db_xref="CDD:409409"
     Region          29..33
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409409"
     Region          37..40
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409409"
     Region          43..50
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409409"
     Region          57..62
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409409"
     Site            order(61,99,106)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:409409"
     Region          70..73
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409409"
     Region          82..86
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409409"
     Region          94..100
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409409"
     Region          110..116
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409409"
     Region          123..217
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          140..144
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          152..156
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          179..183
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          193..198
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          211..214
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          224..317
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          241..245
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          253..257
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          279..283
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          293..298
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          310..313
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          326..418
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          341..345
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          353..357
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          379..383
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          393..398
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          411..414
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..648
                     /gene="LILRB3"
                     /gene_synonym="CD85A; HL9; ILT-5; ILT5; LIR-3; LIR3;
                     PIR-B; PIRB"
                     /coded_by="NM_001320960.2:32..1978"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:11025"
                     /db_xref="HGNC:HGNC:6607"
                     /db_xref="MIM:604820"
ORIGIN      
        1 mtpaltallc lglslgprtr mqagpfpkpt lwaepgsvis wgspvtiwcq gsleaqeyql
       61 dkegspepwd rnnplepknk arfsipsmtq hhagryrchy yssagwseps dplelvmtgf
      121 ynkptlsalp spvvasggnm tlrcgsqkgy hhfvlmkege hqlprtldsq qlhsggfqal
      181 fpvgpvtpsh rwrftcyyyy tntpwvwshp sdpleilpsg vsrkpslltl qgpvlapgqs
      241 ltlqcgsdvg ydrfvlykeg erdflqrpgq qpqaglsqan ftlgpvsrsy ggqyrcygah
      301 nlssewsaps dpldilitgq iydtvslsaq pgptvasgen mtllcqsrgy fdtflltkeg
      361 aahpplrlrs mygahkyqae fpmspvtsah agtyrcygsr ssnphllsfp seplelmvsg
      421 hsggsslppt gppstpggpe dqplnppgsg pqnglgryle vligvsvafv lllflllfll
      481 llrqrhskhr tsdqrktdfq rpagaaetep kdrgllrrss paadvqeenl yaavkdtqse
      541 drveldsqsp hdedpqavty apvkhssprr emasppssls gefldtkdrq veedrqmdte
      601 aaaseasqdv tyaqlhsltl rrkateppps qegeppaeps iyatlaih
//
LOCUS       NP_008922               1029 aa            linear   PRI 20-JAN-2026
DEFINITION  zinc finger protein 197 isoform 1 [Homo sapiens].
ACCESSION   NP_008922
VERSION     NP_008922.1
DBSOURCE    REFSEQ: accession NM_006991.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Li,Z., Wang,D., Na,X., Schoen,S.R., Messing,E.M. and Wu,G.
  TITLE     The VHL protein recruits a novel KRAB-A domain protein to repress
            HIF-1alpha transcriptional activity
  JOURNAL   EMBO J 22 (8), 1857-1867 (2003)
   PUBMED   12682018
  REMARK    GeneRIF: a novel pVHL-interacting protein that functions as a
            negative regulator of hypoxia-inducible factor-1a (HIF-1alpha)
            transactivation; demonstrate that the KRAB-A domain in VHLaK
            mediates pVHL binding and functions as a transcriptional repression
            module
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Gonsky,R., Knauf,J.A., Elisei,R., Wang,J.W., Su,S. and Fagin,J.A.
  TITLE     Identification of rapid turnover transcripts overexpressed in
            thyroid tumors and thyroid cancer cell lines: use of a targeted
            differential RNA display method to select for mRNA subsets
  JOURNAL   Nucleic Acids Res 25 (19), 3823-3831 (1997)
   PUBMED   9380504
REFERENCE   4  (residues 1 to 1029)
  AUTHORS   Calabro,V., Pengue,G., Bartoli,P.C., Pagliuca,A., Featherstone,T.
            and Lania,L.
  TITLE     Positional cloning of cDNAs from the human chromosome 3p21-22
            region identifies a clustered organization of zinc-finger genes
  JOURNAL   Hum Genet 95 (1), 18-21 (1995)
   PUBMED   7814019
REFERENCE   5  (residues 1 to 1029)
  AUTHORS   Pengue,G., Calabro,V., Cannada-Bartoli,P., De Luca,P., Esposito,T.,
            Taillon-Miller,P., LaForgia,S., Druck,T., Huebner,K., D'Urso,M. et
            al.
  TITLE     YAC-assisted cloning of transcribed sequences from the human
            chromosome 3p21 region
  JOURNAL   Hum Mol Genet 2 (6), 791-796 (1993)
   PUBMED   8353497
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY279353.1, AY261677.1,
            AC099669.2 and BQ002665.1.
            
            Summary: This gene product belongs to the zinc finger protein
            superfamily, members of which are regulatory proteins characterized
            by nucleic acid-binding zinc finger domains. The encoded protein
            contains 20 tandemly arrayed C2H2-type zinc fingers, a
            Kruppel-associated box (KRAB) domain, and a SCAN box. This
            transcript turns over rapidly and contains 3' UTR AUUUA motifs,
            which are often a hallmark of rapid turnover. It is overexpressed
            in some thyroid papillary carcinomas. This gene is located in a
            cluster of zinc finger genes at 3p21. Naturally-occurring
            readthrough transcription is observed between this gene and the
            upstream zinc finger protein 660 gene and is represented by
            GeneID:110354863. [provided by RefSeq, May 2017].
            
            Transcript Variant: Variants 1 and 3 encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.122047.1,
                                           SRR1803611.49467.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000344387.9/ ENSP00000345809.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1029
                     /product="zinc finger protein 197 isoform 1"
                     /note="zinc finger protein 166; VHL-associated KRAB-A
                     domain-containing protein; zinc finger protein with KRAB
                     and SCAN domains 9; pVHL-associated KRAB domain-containing
                     protein"
                     /calculated_mol_wt=118717
     Region          38..150
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          216..256
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          262..290
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14709.1)"
     Region          372..392
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          384..409
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          400..420
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(405,407,409,411..412,415..416,419,433,435,439..440,
                     443..444,447,461,463,465,467..468,471..472,475)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          424..853
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          428..448
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          456..476
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          484..504
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          512..532
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          540..560
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          568..588
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          596..616
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(601,603,605,607..608,611..612,615,629,631,635..636,
                     639..640,643,657,659,661,663..664,667..668,671)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          624..644
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          652..672
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          680..700
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          708..728
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          736..756
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          760..>1026
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          764..784
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          792..812
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(797,799,801,803..804,807..808,811,825,827,831..832,
                     835..836,839,853,855,857,859..860,863..864,867)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          820..840
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          848..868
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          876..896
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          904..924
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          932..952
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          960..980
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          988..1008
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..1029
                     /gene="ZNF197"
                     /gene_synonym="D3S1363E; P18; VHLaK; ZKSCAN9; ZNF166;
                     ZSCAN41"
                     /coded_by="NM_006991.5:190..3279"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:10168"
                     /db_xref="HGNC:HGNC:12988"
                     /db_xref="MIM:618359"
ORIGIN      
        1 mtrenvahna lrqeglvkgk ddtwkwgtsf qgssssvwet shlhfrqlry hetsgpqeal
       61 srlrelcrrw lrpeartkaq ilellvleqf lsilpgeirt wvqlhhpgsg eeavalveel
      121 qkdldgpaiq vpvlvkdqdt lqkvvsapgt tlppvlpgsh iaaeicphpp tdlvafnlqd
      181 pqhdspapea salsqeenpr nqlmalmllt aqpqelvmfe evsvcftsee waclgpiqra
      241 lywdvmleny gnvtslewet mteneevtsk psssqradsh kgtskrlqgs vpqvldfeee
      301 cewqvlasqw gnetderadt vkkvslcerd kkkrtppekq gqkwkelgds ltfgsaises
      361 ligtegkkfy kcdmcckhfn kishlinhrr ihtgekphkc kecgkgfiqr ssllmhlrnh
      421 sgekpykcne cgkafsqsay llnhqrihtg ekpykckecg kgfyrhsgli ihlrrhsger
      481 pykcnecgkv fsqnaylidh qrlhkgeepy kcnkcqkafi lkkslilhqr ihsgekpykc
      541 decgktfaqt tylidhqrlh saenpykcke cgkvfirsks lllhqrvhte kktfgckkcg
      601 kifssksnfi dhkrmhsrek pykctecgka ftqsaylfdh qrlhngekpy ecnecgkvfi
      661 lkkslilhqr fhtgenlyec kdcgkvfgsn rnlidherlh ngekpyecre cgktfimsks
      721 fmvhqklhtq ekaykcedcg kafsynssll vhrrihtgek pfecsecgra fssnrnlieh
      781 krihsgekpy ecdecgkcfi lkkslighqr ihtreksykc ndcgkvfsyr snliahqrih
      841 tgekpyacse cgkgftynrn liehqrihsg ektyechvcr kvltssrnlm vhqrihtgek
      901 pykcnecgkd fsqnknlvvh qrmhtgekpy ecdkcrksft skrnlvghqr ihtgekpygc
      961 ndcskvfrqr knltvhqkih tdekpcecdv sekefsqtsn lhlqqkihti eefswlqntn
     1021 eskieiqki
//
LOCUS       NP_001310225             816 aa            linear   PRI 20-JAN-2026
DEFINITION  zinc finger protein 197 isoform 4 [Homo sapiens].
ACCESSION   NP_001310225 XP_011531562 XP_011547031
VERSION     NP_001310225.1
DBSOURCE    REFSEQ: accession NM_001323296.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   2  (residues 1 to 816)
  AUTHORS   Li,Z., Wang,D., Na,X., Schoen,S.R., Messing,E.M. and Wu,G.
  TITLE     The VHL protein recruits a novel KRAB-A domain protein to repress
            HIF-1alpha transcriptional activity
  JOURNAL   EMBO J 22 (8), 1857-1867 (2003)
   PUBMED   12682018
  REMARK    GeneRIF: a novel pVHL-interacting protein that functions as a
            negative regulator of hypoxia-inducible factor-1a (HIF-1alpha)
            transactivation; demonstrate that the KRAB-A domain in VHLaK
            mediates pVHL binding and functions as a transcriptional repression
            module
REFERENCE   3  (residues 1 to 816)
  AUTHORS   Gonsky,R., Knauf,J.A., Elisei,R., Wang,J.W., Su,S. and Fagin,J.A.
  TITLE     Identification of rapid turnover transcripts overexpressed in
            thyroid tumors and thyroid cancer cell lines: use of a targeted
            differential RNA display method to select for mRNA subsets
  JOURNAL   Nucleic Acids Res 25 (19), 3823-3831 (1997)
   PUBMED   9380504
REFERENCE   4  (residues 1 to 816)
  AUTHORS   Calabro,V., Pengue,G., Bartoli,P.C., Pagliuca,A., Featherstone,T.
            and Lania,L.
  TITLE     Positional cloning of cDNAs from the human chromosome 3p21-22
            region identifies a clustered organization of zinc-finger genes
  JOURNAL   Hum Genet 95 (1), 18-21 (1995)
   PUBMED   7814019
REFERENCE   5  (residues 1 to 816)
  AUTHORS   Pengue,G., Calabro,V., Cannada-Bartoli,P., De Luca,P., Esposito,T.,
            Taillon-Miller,P., LaForgia,S., Druck,T., Huebner,K., D'Urso,M. et
            al.
  TITLE     YAC-assisted cloning of transcribed sequences from the human
            chromosome 3p21 region
  JOURNAL   Hum Mol Genet 2 (6), 791-796 (1993)
   PUBMED   8353497
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099669.2 and BQ002665.1.
            
            On or before Jul 8, 2016 this sequence version replaced
            XP_011531562.1, XP_011547031.1.
            
            Summary: This gene product belongs to the zinc finger protein
            superfamily, members of which are regulatory proteins characterized
            by nucleic acid-binding zinc finger domains. The encoded protein
            contains 20 tandemly arrayed C2H2-type zinc fingers, a
            Kruppel-associated box (KRAB) domain, and a SCAN box. This
            transcript turns over rapidly and contains 3' UTR AUUUA motifs,
            which are often a hallmark of rapid turnover. It is overexpressed
            in some thyroid papillary carcinomas. This gene is located in a
            cluster of zinc finger genes at 3p21. Naturally-occurring
            readthrough transcription is observed between this gene and the
            upstream zinc finger protein 660 gene and is represented by
            GeneID:110354863. [provided by RefSeq, May 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.72566.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..816
                     /product="zinc finger protein 197 isoform 4"
                     /note="zinc finger protein 166; VHL-associated KRAB-A
                     domain-containing protein; zinc finger protein with KRAB
                     and SCAN domains 9; pVHL-associated KRAB domain-containing
                     protein"
                     /calculated_mol_wt=94999
     Region          3..43
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          159..179
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          171..196
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          187..207
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(192,194,196,198..199,202..203,206,220,222,226..227,
                     230..231,234,248,250,252,254..255,258..259,262)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          211..640
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          215..235
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          243..263
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          271..291
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          299..319
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          327..347
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          355..375
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          383..403
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(388,390,392,394..395,398..399,402,416,418,422..423,
                     426..427,430,444,446,448,450..451,454..455,458)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          411..431
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          439..459
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          467..487
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          495..515
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          523..543
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          547..>796
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          551..571
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          579..599
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(584,586,588,590..591,594..595,598,612,614,618..619,
                     622..623,626,640,642,644,646..647,650..651,654)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          607..627
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          635..655
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          663..683
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          691..711
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          719..739
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          747..767
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          775..795
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..816
                     /gene="ZNF197"
                     /gene_synonym="D3S1363E; P18; VHLaK; ZKSCAN9; ZNF166;
                     ZSCAN41"
                     /coded_by="NM_001323296.2:737..3187"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:10168"
                     /db_xref="HGNC:HGNC:12988"
                     /db_xref="MIM:618359"
ORIGIN      
        1 melvmfeevs vcftseewac lgpiqralyw dvmlenygnv tslewetmte neevtskpss
       61 sqradshkgt skrlqgsvpq vldfeeecew qvlasqwgne tderadtvkk vslcerdkkk
      121 rtppekqgqk wkelgdsltf gsaiseslig tegkkfykcd mcckhfnkis hlinhrriht
      181 gekphkckec gkgfiqrssl lmhlrnhsge kpykcnecgk afsqsaylln hqrihtgekp
      241 ykckecgkgf yrhsgliihl rrhsgerpyk cnecgkvfsq naylidhqrl hkgeepykcn
      301 kcqkafilkk slilhqrihs gekpykcdec gktfaqttyl idhqrlhsae npykckecgk
      361 vfirskslll hqrvhtekkt fgckkcgkif ssksnfidhk rmhsrekpyk ctecgkaftq
      421 saylfdhqrl hngekpyecn ecgkvfilkk slilhqrfht genlyeckdc gkvfgsnrnl
      481 idherlhnge kpyecrecgk tfimsksfmv hqklhtqeka ykcedcgkaf synssllvhr
      541 rihtgekpfe csecgrafss nrnliehkri hsgekpyecd ecgkcfilkk slighqriht
      601 reksykcndc gkvfsyrsnl iahqrihtge kpyacsecgk gftynrnlie hqrihsgekt
      661 yechvcrkvl tssrnlmvhq rihtgekpyk cnecgkdfsq nknlvvhqrm htgekpyecd
      721 kcrksftskr nlvghqriht gekpygcndc skvfrqrknl tvhqkihtde kpcecdvsek
      781 efsqtsnlhl qqkihtieef swlqntnesk ieiqki
//
LOCUS       NP_001303268             297 aa            linear   PRI 20-JAN-2026
DEFINITION  pregnancy-specific beta-1-glycoprotein 4 isoform 4 [Homo sapiens].
ACCESSION   NP_001303268
VERSION     NP_001303268.1
DBSOURCE    REFSEQ: accession NM_001316339.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Shanley,D.K., Kiely,P.A., Golla,K., Allen,S., Martin,K.,
            O'Riordan,R.T., Ball,M., Aplin,J.D., Singer,B.B., Caplice,N.,
            Moran,N. and Moore,T.
  TITLE     Pregnancy-specific glycoproteins bind integrin alphaIIbbeta3 and
            inhibit the platelet-fibrinogen interaction
  JOURNAL   PLoS One 8 (2), e57491 (2013)
   PUBMED   23469002
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Kimoto,Y.
  TITLE     A single human cell expresses all messenger ribonucleic acids: the
            arrow of time in a cell
  JOURNAL   Mol Gen Genet 258 (3), 233-239 (1998)
   PUBMED   9645429
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Teglund,S., Olsen,A., Khan,W.N., Frangsmyr,L. and Hammarstrom,S.
  TITLE     The pregnancy-specific glycoprotein (PSG) gene cluster on human
            chromosome 19: fine structure of the 11 PSG genes and
            identification of 6 new genes forming a third subgroup within the
            carcinoembryonic antigen (CEA) family
  JOURNAL   Genomics 23 (3), 669-684 (1994)
   PUBMED   7851896
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Olsen,A., Teglund,S., Nelson,D., Gordon,L., Copeland,A.,
            Georgescu,A., Carrano,A. and Hammarstrom,S.
  TITLE     Gene organization of the pregnancy-specific glycoprotein region on
            human chromosome 19: assembly and analysis of a 700-kb cosmid
            contig spanning the region
  JOURNAL   Genomics 23 (3), 659-668 (1994)
   PUBMED   7851895
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Pan,C.J., Chamberlin,M.E., Wu,S.M., Chan,W.Y. and Chou,J.Y.
  TITLE     Pregnancy-specific glycoprotein gene expression and the induction
            by 5-bromo-2'-deoxyuridine
  JOURNAL   Biochemistry 33 (23), 7260-7266 (1994)
   PUBMED   8003489
REFERENCE   6  (residues 1 to 297)
  AUTHORS   Chan,W.Y., Zheng,Q.X., McMahon,J. and Tease,L.A.
  TITLE     Characterization of new members of the pregnancy-specific beta
            1-glycoprotein family
  JOURNAL   Mol Cell Biochem 106 (2), 161-170 (1991)
   PUBMED   1922019
REFERENCE   7  (residues 1 to 297)
  AUTHORS   Barnett,T.R., Pickle,W. 2nd and Elting,J.J.
  TITLE     Characterization of two new members of the pregnancy-specific beta
            1-glycoprotein family from the myeloid cell line KG-1 and
            suggestion of two distinct classes of transcription unit
  JOURNAL   Biochemistry 29 (44), 10213-10218 (1990)
   PUBMED   2271648
REFERENCE   8  (residues 1 to 297)
  AUTHORS   .
  TITLE     The human pregnancy-specific glycoprotein genes are tightly linked
            on the long arm of chromosome 19 and are coordinately expressed
  JOURNAL   Biochem Biophys Res Commun 168 (3), 1325 (1990)
   PUBMED   2346490
REFERENCE   9  (residues 1 to 297)
  AUTHORS   Thompson,J., Koumari,R., Wagner,K., Barnert,S., Schleussner,C.,
            Schrewe,H., Zimmermann,W., Muller,G., Schempp,W., Zaninetta,D. et
            al.
  TITLE     The human pregnancy-specific glycoprotein genes are tightly linked
            on the long arm of chromosome 19 and are coordinately expressed
  JOURNAL   Biochem Biophys Res Commun 167 (2), 848-859 (1990)
   PUBMED   1690992
  REMARK    Erratum:[Biochem Biophys Res Commun 1990 May 16;168(3):1325]
REFERENCE   10 (residues 1 to 297)
  AUTHORS   Thompson,J.A., Mauch,E.M., Chen,F.S., Hinoda,Y., Schrewe,H.,
            Berling,B., Barnert,S., von Kleist,S., Shively,J.E. and
            Zimmermann,W.
  TITLE     Analysis of the size of the carcinoembryonic antigen (CEA) gene
            family: isolation and sequencing of N-terminal domain exons
  JOURNAL   Biochem Biophys Res Commun 158 (3), 996-1004 (1989)
   PUBMED   2537643
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA837940.1, DA838139.1,
            AC005392.2, BC063127.1 and BC008405.1.
            
            Summary: The protein encoded by this gene is a pregnancy-specific
            glycoprotein (PSG), one of several encoded by a cluster of similar
            genes on chromosome 19. This gene is a member of the
            carcinoembryonic antigen (CEA) gene family and may play a role in
            regulation of the innate immune system. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (4) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2162568
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..297
                     /product="pregnancy-specific beta-1-glycoprotein 4 isoform
                     4"
                     /note="Pregnancy-specific beta-1-glycoprotein-4;
                     PS-beta-G-4; pregnancy-specific glycoprotein 4"
                     /calculated_mol_wt=33268
     Region          26..114
                     /region_name="IgI_hCEACAM_2_4_6_like"
                     /note="Immunoglobulin (Ig)-like domain of human
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM) domains 2, 4, and 6, and similar
                     domains; cd05740"
                     /db_xref="CDD:409402"
     Region          26..30
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409402"
     Region          33..38
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409402"
     Region          43..49
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409402"
     Region          56..61
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409402"
     Region          63..66
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409402"
     Region          70..74
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409402"
     Region          77..82
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409402"
     Region          92..100
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409402"
     Region          104..113
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409402"
     Region          119..207
                     /region_name="IgI_hCEACAM_2_4_6_like"
                     /note="Immunoglobulin (Ig)-like domain of human
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM) domains 2, 4, and 6, and similar
                     domains; cd05740"
                     /db_xref="CDD:409402"
     Region          119..123
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409402"
     Region          126..131
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409402"
     Region          136..142
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409402"
     Region          149..154
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409402"
     Region          156..159
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409402"
     Region          163..167
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409402"
     Region          170..175
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409402"
     Region          185..193
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409402"
     Region          197..206
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409402"
     Region          216..291
                     /region_name="IgC2_CEACAM5-like"
                     /note="Fifth immunoglobulin (Ig)-like domain of the
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule 5 (CEACAM5) and similar domains; member of the
                     C2-set IgSF domains; cd20948"
                     /db_xref="CDD:409540"
     Region          216..222
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409540"
     Region          227..234
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409540"
     Region          240..246
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409540"
     Region          249..254
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409540"
     Region          257..263
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409540"
     Region          266..277
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409540"
     Region          280..291
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409540"
     CDS             1..297
                     /gene="PSG4"
                     /gene_synonym="PSBG-4"
                     /coded_by="NM_001316339.2:103..996"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:5672"
                     /db_xref="HGNC:HGNC:9521"
                     /db_xref="MIM:176393"
ORIGIN      
        1 mgplsappct qritwkgvll tvetpkpsis ssnlnpream eaviltcdpa tpaasyqwwm
       61 ngqslpmthr lqlsktnrtl fifgvtkyia gpyeceirnp vsasrsdpvt lnllpklskp
      121 yitinnlnpr enkdvltftc epksknytyi wwlngqslpv sprvkrpien rililpnvtr
      181 netgpyqcei rdryggirsd pvtlnvlygp dlpsiypsft yyrsgenlyl scfaesnpra
      241 qyswtingkf qlsgqklsip qittkhsgly acsvrnsatg kessksitvk vsdwilp
//
LOCUS       NP_001310993            1743 aa            linear   PRI 20-JAN-2026
DEFINITION  transport and Golgi organization protein 1 homolog isoform 5 [Homo
            sapiens].
ACCESSION   NP_001310993
VERSION     NP_001310993.1
DBSOURCE    REFSEQ: accession NM_001324064.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1743)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1743)
  AUTHORS   Wanbiao,Z., Jing,M., Shi,Z., Tengxiang,C., Xueke,Z. and Haiyang,L.
  TITLE     MIA3 promotes the degradation of GSH (glutathione) by binding to
            CHAC1, thereby promoting the progression of hepatocellular
            carcinoma
  JOURNAL   Mol Cell Biochem 479 (10), 2769-2784 (2024)
   PUBMED   37948019
  REMARK    GeneRIF: MIA3 promotes the degradation of GSH (glutathione) by
            binding to CHAC1, thereby promoting the progression of
            hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 1743)
  AUTHORS   Connolly,L.M., McFalls,C.M., McMahon,I.G., Bhat,A.M. and
            Artlett,C.M.
  TITLE     Caspase 1 Enhances Transport and Golgi Organization Protein 1
            Expression to Promote Procollagen Export From the Endoplasmic
            Reticulum in Systemic Sclerosis Contributing to Fibrosis
  JOURNAL   Arthritis Rheumatol 75 (10), 1831-1841 (2023)
   PUBMED   37067501
  REMARK    GeneRIF: Caspase 1 Enhances Transport and Golgi Organization
            Protein 1 Expression to Promote Procollagen Export From the
            Endoplasmic Reticulum in Systemic Sclerosis Contributing to
            Fibrosis.
REFERENCE   4  (residues 1 to 1743)
  AUTHORS   Man,J., Zhou,W., Zuo,S., Zhao,X., Wang,Q., Ma,H. and Li,H.Y.
  TITLE     TANGO1 interacts with NRTN to promote hepatocellular carcinoma
            progression by regulating the PI3K/AKT/mTOR signaling pathway
  JOURNAL   Biochem Pharmacol 213, 115615 (2023)
   PUBMED   37211171
  REMARK    GeneRIF: TANGO1 interacts with NRTN to promote hepatocellular
            carcinoma progression by regulating the PI3K/AKT/mTOR signaling
            pathway.
REFERENCE   5  (residues 1 to 1743)
  AUTHORS   Junkiert-Czarnecka,A., Pilarska-Deltow,M., Bak,A., Heise,M. and
            Haus,O.
  TITLE     A novel mutation in collagen transport protein, MIA3 gene, detected
            in a patient with clinical symptoms of Ehlers-Danlos hypermobile
            syndrome
  JOURNAL   Adv Clin Exp Med 32 (7), 777-781 (2023)
   PUBMED   36603143
  REMARK    GeneRIF: A novel mutation in collagen transport protein, MIA3 gene,
            detected in a patient with clinical symptoms of Ehlers-Danlos
            hypermobile syndrome.
REFERENCE   6  (residues 1 to 1743)
  AUTHORS   Saito,K., Chen,M., Bard,F., Chen,S., Zhou,H., Woodley,D.,
            Polischuk,R., Schekman,R. and Malhotra,V.
  TITLE     TANGO1 facilitates cargo loading at endoplasmic reticulum exit
            sites
  JOURNAL   Cell 136 (5), 891-902 (2009)
   PUBMED   19269366
REFERENCE   7  (residues 1 to 1743)
  AUTHORS   Arndt,S., Melle,C., Mondal,K., Klein,G., von Eggeling,F. and
            Bosserhoff,A.K.
  TITLE     Interactions of TANGO and leukocyte integrin CD11c/CD18 regulate
            the migration of human monocytes
  JOURNAL   J Leukoc Biol 82 (6), 1466-1472 (2007)
   PUBMED   17726152
  REMARK    GeneRIF: The results from this study present TANGO as a novel
            ligand for CD11c, regulating migratory processes of hematopoietic
            cells.
REFERENCE   8  (residues 1 to 1743)
  AUTHORS   Arndt,S. and Bosserhoff,A.K.
  TITLE     Reduced expression of TANGO in colon and hepatocellular carcinomas
  JOURNAL   Oncol Rep 18 (4), 885-891 (2007)
   PUBMED   17786351
  REMARK    GeneRIF: Reduced expression of TANGO is associated with colon and
            hepatocellular carcinomas
REFERENCE   9  (residues 1 to 1743)
  AUTHORS   Arndt,S. and Bosserhoff,A.K.
  TITLE     TANGO is a tumor suppressor of malignant melanoma
  JOURNAL   Int J Cancer 119 (12), 2812-2820 (2006)
   PUBMED   17044017
  REMARK    GeneRIF: TANGO transfected cell lines revealed that TANGO
            expression reduces motility, whereas reduction of TANGO enhances
            migration.
REFERENCE   10 (residues 1 to 1743)
  AUTHORS   Bosserhoff,A.K., Moser,M. and Buettner,R.
  TITLE     Characterization and expression pattern of the novel MIA homolog
            TANGO
  JOURNAL   Gene Expr Patterns 4 (4), 473-479 (2004)
   PUBMED   15183315
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL592148.7 and KF459535.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.484763.1,
                                           SRR11853564.2819.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1743
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..1743
                     /product="transport and Golgi organization protein 1
                     homolog isoform 5"
                     /note="C219-reactive peptide; melanoma inhibitory activity
                     protein 3; MIA family member 3, ER export factor; melanoma
                     inhibitory activity family, member 3; transport and Golgi
                     organization protein 1 homolog"
                     /calculated_mol_wt=194818
     Region          <1053..1362
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          <1306..>1475
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          <1483..1728
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1743
                     /gene="MIA3"
                     /gene_synonym="D320; ODCD2; TANGO; TANGO1; UNQ6077"
                     /coded_by="NM_001324064.2:552..5783"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:375056"
                     /db_xref="HGNC:HGNC:24008"
                     /db_xref="MIM:613455"
ORIGIN      
        1 meknpelske repepepvea nseesdsvfs entedlqeqf ttqkhhshan sqanhaqgeq
       61 asfesfeeml qdklkvpese nnktsnssqv sneqdkiday kllkkemtld lktkfgstad
      121 alvsddettr lvtsleddfd eeldteyyav gkedeenqed fdelplltft dgedmktpak
      181 sgvekyptdk eqnsneedkv qltvppgikn ddknilttwg dtifsivtgg eetrdtmdle
      241 sssseeeked dddalvpdsk qgkpqsatdy sdpdnvddgl fivdipktnn dkevnaehhi
      301 kgkgrgvqes krglvqdkte ledenqegmt vhssvhsnnl nsmpaaekgk dtlksayddt
      361 endlkgaaih iskgmlheek pgeqileggs esesaqkaag nqmndrkiqq eslgsaplmg
      421 ddhpnasrds vegdalvnga klhtlsvehq reelkeelvl ktqnqprfss pdeidlprel
      481 edevpilgrn lpwqqerdva ataskqmsek irlsegeake dsldeeffhh kamqgtevgq
      541 tdqtdstggp aflskveedd ypseellede nainakrske knpgnqgrqf dvnlqvpdra
      601 vlgtihpdpe ieeskqetsm ildsektset aakgvntggr epntmveker pladkkaqrp
      661 fersdfsdsi kiqtpelgev fqnkdsdylk ndnpeehlkt sglagepege lskedhente
      721 kymgtesqgs aaaepeddsf hwtphtsvep ghsdkredll iissffkeqq slqrfqkyfn
      781 vheleallqe mssklksaqq eslpynmekv ldkvfrases qilsiaekml dtrvaenrdl
      841 gmnennifee aavlddiqdl iyfvrykhst aeetatlvma ppleeglgga meemqplhed
      901 nfsrektael nvqvpeepth ldqrvigdth asevsqkpnt ekdldpgpvt tedtpmdaid
      961 ankqpetaae epasvtplen ailliysfmf yltkslvatl pddvqpgpdf yglpwkpvfi
     1021 taflgiasfa iflwrtvlvv kdrvyqvteq qiseklktim kentelvqkl snyeqkikes
     1081 kkhvqetrkq nmilsdeaik ykdkiktlek nqeilddtak nlrvmleser eqnvknqdli
     1141 senkksiekl kdvismnase fsevqialne aklseekvks echrvqeena rlkkkkeqlq
     1201 qeiedwsklh aelseqiksf eksqkdleva lthkddnina ltncitqlnl lecesesegq
     1261 nkggndsdel angevggdrn ekmknqikqm mdvsrtqtai svveedlkll qlklrasvst
     1321 kcnledqvkk leddrnslqa akagledeck tlrqkveiln elyqqkemal qkklsqeeye
     1381 rqerehrlsa adekavsaae evktykrrie emedelqkte rsfknqiath ekkahenwlk
     1441 araaeraiae ekreaanlrh klleltqkma mlqeepvivk pmpgkpntqn pprrgplsqn
     1501 gsfgpspvsg gecsppltve ppvrplsatl nrrdmprsef gsvdgplphp rwsaeasgkp
     1561 spsdpgsgta tmmnsssrgs sptrvldegk vnmapkgppp fpgvplmstp mggpvpppir
     1621 ygpppqlcgp fgprplpppf gpgmrpplgl refapgvppg rrdlplhprg flpghapfrp
     1681 lgslgpreyf ipgtrlpppt hgpqeypppp avrdllpsgs rdepppasqs tsqdcsqalk
     1741 qsp
//
LOCUS       NP_001171941              76 aa            linear   PRI 20-JAN-2026
DEFINITION  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2
            isoform 2 [Homo sapiens].
ACCESSION   NP_001171941
VERSION     NP_001171941.1
DBSOURCE    REFSEQ: accession NM_001185012.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Signes,A. and Fernandez-Vizarra,E.
  TITLE     Assembly of mammalian oxidative phosphorylation complexes I-V and
            supercomplexes
  JOURNAL   Essays Biochem 62 (3), 255-270 (2018)
   PUBMED   30030361
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Perrier,S., Gauquelin,L., Tetreault,M., Tran,L.T., Webb,N.,
            Srour,M., Mitchell,J.J., Brunel-Guitton,C., Majewski,J., Long,V.,
            Keller,S., Gambello,M.J., Simons,C., Vanderver,A. and Bernard,G.
  CONSRTM   Care4Rare Canada Consortium
  TITLE     Recessive mutations in NDUFA2 cause mitochondrial
            leukoencephalopathy
  JOURNAL   Clin Genet 93 (2), 396-400 (2018)
   PUBMED   28857146
  REMARK    GeneRIF: Review of a biorepository of patients with unsolved
            genetic leukoencephalopathies who underwent whole-exome or genome
            sequencing allowed us to identify a second patient with compound
            heterozygous mutations in NDUFA2. Only 1 other patient with
            mutations in NDUFA2 and a different phenotype (Leigh syndrome) has
            previously been reported. This is the first report of cystic
            leukoencephalopathy caused by mutations in NDUFA2.
REFERENCE   4  (residues 1 to 76)
  AUTHORS   Hoefs,S.J., Dieteren,C.E., Distelmaier,F., Janssen,R.J., Epplen,A.,
            Swarts,H.G., Forkink,M., Rodenburg,R.J., Nijtmans,L.G.,
            Willems,P.H., Smeitink,J.A. and van den Heuvel,L.P.
  TITLE     NDUFA2 complex I mutation leads to Leigh disease
  JOURNAL   Am J Hum Genet 82 (6), 1306-1315 (2008)
   PUBMED   18513682
REFERENCE   5  (residues 1 to 76)
  AUTHORS   Brockmann,C., Diehl,A., Rehbein,K., Strauss,H., Schmieder,P.,
            Korn,B., Kuhne,R. and Oschkinat,H.
  TITLE     The oxidized subunit B8 from human complex I adopts a thioredoxin
            fold
  JOURNAL   Structure 12 (9), 1645-1654 (2004)
   PUBMED   15341729
  REMARK    GeneRIF: solution structure shows a thioredoxin fold with highest
            similarities to the human thioredoxin mutant C73S and thioredoxin 2
            from Anabeana sp
REFERENCE   6  (residues 1 to 76)
  AUTHORS   Murray,J., Zhang,B., Taylor,S.W., Oglesbee,D., Fahy,E.,
            Marusich,M.F., Ghosh,S.S. and Capaldi,R.A.
  TITLE     The subunit composition of the human NADH dehydrogenase obtained by
            rapid one-step immunopurification
  JOURNAL   J Biol Chem 278 (16), 13619-13622 (2003)
   PUBMED   12611891
REFERENCE   7  (residues 1 to 76)
  AUTHORS   Loeffen,J.L., Triepels,R.H., van den Heuvel,L.P., Schuelke,M.,
            Buskens,C.A., Smeets,R.J., Trijbels,J.M. and Smeitink,J.A.
  TITLE     cDNA of eight nuclear encoded subunits of NADH:ubiquinone
            oxidoreductase: human complex I cDNA characterization completed
  JOURNAL   Biochem Biophys Res Commun 253 (2), 415-422 (1998)
   PUBMED   9878551
REFERENCE   8  (residues 1 to 76)
  AUTHORS   Emahazion,T. and Brookes,A.J.
  TITLE     Mapping of the NDUFA2, NDUFA6, NDUFA7, NDUFB8, and NDUFS8 electron
            transport chain genes by intron based radiation hybrid mapping
  JOURNAL   Cytogenet Cell Genet 82 (1-2), 114 (1998)
   PUBMED   9763676
REFERENCE   9  (residues 1 to 76)
  AUTHORS   Ton,C., Hwang,D.M., Dempsey,A.A. and Liew,C.C.
  TITLE     Identification and primary structure of five human NADH-ubiquinone
            oxidoreductase subunits
  JOURNAL   Biochem Biophys Res Commun 241 (2), 589-594 (1997)
   PUBMED   9425316
REFERENCE   10 (residues 1 to 76)
  AUTHORS   Rahman,S., Thorburn,D.R. and Ball,M.
  TITLE     Nuclear Gene-Encoded Leigh Syndrome Spectrum Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26425749
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ054127.1 and AA993683.1.
            
            Summary: The encoded protein is a subunit of the hydrophobic
            protein fraction of the NADH:ubiquinone oxidoreductase (complex 1),
            the first enzyme complex in the electron transport chain located in
            the inner mitochondrial membrane, and may be involved in regulating
            complex I activity or its assembly via assistance in redox
            processes. Mutations in this gene are associated with Leigh
            syndrome, an early-onset progressive neurodegenerative disorder.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 3' coding region, compared to variant 1. This results in a
            protein with a shorter and distinct C-terminus (isoform 2),
            compared to isoform 1. It is unknown if isoform 2 is located to the
            mitochondria and/or if it is functional.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AV705564.1, SRR18074967.353075.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.3"
     Protein         1..76
                     /product="NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex subunit 2 isoform 2"
                     /EC_number="7.1.1.2"
                     /note="NADH-ubiquinone oxidoreductase subunit CI-B8;
                     complex I B8 subunit; NADH dehydrogenase (ubiquinone) 1
                     alpha subcomplex, 2, 8kDa"
                     /calculated_mol_wt=8360
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O43678.3)"
     Region          28..>69
                     /region_name="L51_S25_CI-B8"
                     /note="Mitochondrial ribosomal protein L51 / S25 / CI-B8
                     domain; smart00916"
                     /db_xref="CDD:197984"
     Site            64
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CQ75; propagated from
                     UniProtKB/Swiss-Prot (O43678.3)"
     CDS             1..76
                     /gene="NDUFA2"
                     /gene_synonym="B8; CIB8; MC1DN13"
                     /coded_by="NM_001185012.2:48..278"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54911.1"
                     /db_xref="GeneID:4695"
                     /db_xref="HGNC:HGNC:7685"
                     /db_xref="MIM:602137"
ORIGIN      
        1 maaaaasrgv gaklglreir ihlcqrspgs qgvrdfiekr yvelkkanpd lpilirecsd
       61 vqpklwarya srvqns
//
LOCUS       NP_001310992            1848 aa            linear   PRI 20-JAN-2026
DEFINITION  transport and Golgi organization protein 1 homolog isoform 4
            precursor [Homo sapiens].
ACCESSION   NP_001310992
VERSION     NP_001310992.1
DBSOURCE    REFSEQ: accession NM_001324063.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1848)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1848)
  AUTHORS   Wanbiao,Z., Jing,M., Shi,Z., Tengxiang,C., Xueke,Z. and Haiyang,L.
  TITLE     MIA3 promotes the degradation of GSH (glutathione) by binding to
            CHAC1, thereby promoting the progression of hepatocellular
            carcinoma
  JOURNAL   Mol Cell Biochem 479 (10), 2769-2784 (2024)
   PUBMED   37948019
  REMARK    GeneRIF: MIA3 promotes the degradation of GSH (glutathione) by
            binding to CHAC1, thereby promoting the progression of
            hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 1848)
  AUTHORS   Connolly,L.M., McFalls,C.M., McMahon,I.G., Bhat,A.M. and
            Artlett,C.M.
  TITLE     Caspase 1 Enhances Transport and Golgi Organization Protein 1
            Expression to Promote Procollagen Export From the Endoplasmic
            Reticulum in Systemic Sclerosis Contributing to Fibrosis
  JOURNAL   Arthritis Rheumatol 75 (10), 1831-1841 (2023)
   PUBMED   37067501
  REMARK    GeneRIF: Caspase 1 Enhances Transport and Golgi Organization
            Protein 1 Expression to Promote Procollagen Export From the
            Endoplasmic Reticulum in Systemic Sclerosis Contributing to
            Fibrosis.
REFERENCE   4  (residues 1 to 1848)
  AUTHORS   Man,J., Zhou,W., Zuo,S., Zhao,X., Wang,Q., Ma,H. and Li,H.Y.
  TITLE     TANGO1 interacts with NRTN to promote hepatocellular carcinoma
            progression by regulating the PI3K/AKT/mTOR signaling pathway
  JOURNAL   Biochem Pharmacol 213, 115615 (2023)
   PUBMED   37211171
  REMARK    GeneRIF: TANGO1 interacts with NRTN to promote hepatocellular
            carcinoma progression by regulating the PI3K/AKT/mTOR signaling
            pathway.
REFERENCE   5  (residues 1 to 1848)
  AUTHORS   Junkiert-Czarnecka,A., Pilarska-Deltow,M., Bak,A., Heise,M. and
            Haus,O.
  TITLE     A novel mutation in collagen transport protein, MIA3 gene, detected
            in a patient with clinical symptoms of Ehlers-Danlos hypermobile
            syndrome
  JOURNAL   Adv Clin Exp Med 32 (7), 777-781 (2023)
   PUBMED   36603143
  REMARK    GeneRIF: A novel mutation in collagen transport protein, MIA3 gene,
            detected in a patient with clinical symptoms of Ehlers-Danlos
            hypermobile syndrome.
REFERENCE   6  (residues 1 to 1848)
  AUTHORS   Saito,K., Chen,M., Bard,F., Chen,S., Zhou,H., Woodley,D.,
            Polischuk,R., Schekman,R. and Malhotra,V.
  TITLE     TANGO1 facilitates cargo loading at endoplasmic reticulum exit
            sites
  JOURNAL   Cell 136 (5), 891-902 (2009)
   PUBMED   19269366
REFERENCE   7  (residues 1 to 1848)
  AUTHORS   Arndt,S., Melle,C., Mondal,K., Klein,G., von Eggeling,F. and
            Bosserhoff,A.K.
  TITLE     Interactions of TANGO and leukocyte integrin CD11c/CD18 regulate
            the migration of human monocytes
  JOURNAL   J Leukoc Biol 82 (6), 1466-1472 (2007)
   PUBMED   17726152
  REMARK    GeneRIF: The results from this study present TANGO as a novel
            ligand for CD11c, regulating migratory processes of hematopoietic
            cells.
REFERENCE   8  (residues 1 to 1848)
  AUTHORS   Arndt,S. and Bosserhoff,A.K.
  TITLE     Reduced expression of TANGO in colon and hepatocellular carcinomas
  JOURNAL   Oncol Rep 18 (4), 885-891 (2007)
   PUBMED   17786351
  REMARK    GeneRIF: Reduced expression of TANGO is associated with colon and
            hepatocellular carcinomas
REFERENCE   9  (residues 1 to 1848)
  AUTHORS   Arndt,S. and Bosserhoff,A.K.
  TITLE     TANGO is a tumor suppressor of malignant melanoma
  JOURNAL   Int J Cancer 119 (12), 2812-2820 (2006)
   PUBMED   17044017
  REMARK    GeneRIF: TANGO transfected cell lines revealed that TANGO
            expression reduces motility, whereas reduction of TANGO enhances
            migration.
REFERENCE   10 (residues 1 to 1848)
  AUTHORS   Bosserhoff,A.K., Moser,M. and Buettner,R.
  TITLE     Characterization and expression pattern of the novel MIA homolog
            TANGO
  JOURNAL   Gene Expr Patterns 4 (4), 473-479 (2004)
   PUBMED   15183315
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL592148.7 and KF459535.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.867745.1,
                                           SRR14038196.2294792.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1848
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..1848
                     /product="transport and Golgi organization protein 1
                     homolog isoform 4 precursor"
                     /note="C219-reactive peptide; melanoma inhibitory activity
                     protein 3; MIA family member 3, ER export factor; melanoma
                     inhibitory activity family, member 3; transport and Golgi
                     organization protein 1 homolog"
                     /calculated_mol_wt=204480
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2429
     Region          37..109
                     /region_name="SH3_MIA3"
                     /note="Src Homology 3 domain of Melanoma Inhibitory
                     Activity 3 protein; cd11893"
                     /db_xref="CDD:212826"
     Site            order(54..56,59..63,84..85,96..98,100..101)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:212826"
     Region          1185..1322
                     /region_name="ATP-synt_Fo_b"
                     /note="F-type ATP synthase, membrane subunit b; cl21478"
                     /db_xref="CDD:473877"
     Region          <1262..>1522
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          <1588..1833
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1848
                     /gene="MIA3"
                     /gene_synonym="D320; ODCD2; TANGO; TANGO1; UNQ6077"
                     /coded_by="NM_001324063.2:15..5561"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:375056"
                     /db_xref="HGNC:HGNC:24008"
                     /db_xref="MIM:613455"
ORIGIN      
        1 maaapgllvw llvlrlpwrv pgqldpstgr rfsehklcad decsmlmyrg ealedftgpd
       61 crfvnfkkgd pvyvyyklar gwpevwagsv grtfgyfpkd liqvvheytk eelqvptdet
      121 dfvcfdggrd dfhnynveel lgflelynsa atdsekavek tlqdmeknpe lskerepepe
      181 pveanseesd svfsentedl qeqfttqkhh shansqanha qgeqasfesf eemlqdklkv
      241 pesennktsn ssqvsneqdk idaykllkke mtldlktkfg stadalvsdd ettrlvtsle
      301 ddfdeeldte yyavgkedee nqedfdelpl ltftdgedmk tpaksgveky ptdkeqnsne
      361 edkvqltvpp giknddknil ttwgdtifsi vtggeetrdt mdlessssee ekeddddalv
      421 pdskqgkpqs atdysdpdnv ddglfivdip ktnndkevna ehhikgkgrg vqeskrglvq
      481 dkteledenq egmtvhssvh snnlnsmpaa ekgkdtlksa yddtendlkg aaihiskgml
      541 heekpgeqil eggsesesaq kaagnqmndr kiqqeslgsa plmgddhpna srdsvegdal
      601 vngaklhtls vehqreelke elvlktqnqp rfsspdeidl preledevpi lgrnlpwqqe
      661 rdvaataskq msekirlseg eakedsldee ffhhkamqgt evgqtdqtds tggpaflskv
      721 eeddypseel ledenainak rskeknpgnq grqfdvnlqv pdravlgtih pdpeieeskq
      781 etsmildsek tsetaakgvn tggrepntmv ekerpladkk aqrpfersdf sdsikiqtpe
      841 lgevfqnkds dylkndnpee hlktsglage pegelskedh entekymgte sqgsaaaepe
      901 ddsfhwtpht svepghsdkr edlliissff keqqslqrfq kyfnvhelea llqemssklk
      961 saqqeslpyn mekvldkvfr asesqilsia ekmldtrvae nrdlgmnenn ifeeaavldd
     1021 iqdliyfvry khstaeetat lvmappleeg lggameemqp lhednfsrek taelnvqvpe
     1081 epthldqrvi gdthasevsq kpntekdldp gpvttedtpm daidankqpe taaeepasvt
     1141 plenailliy sfmfyltksl vatlpddvqp gpdfyglpwk pvfitaflgi asfaiflwrt
     1201 vlvvkdrvyq vteqqisekl ktimkentel vqklsnyeqk ikeskkhvqe trkqnmilsd
     1261 eaikykdkik tleknqeild dtaknlrvml esereqnvkn qdllqqeied wsklhaelse
     1321 qiksfeksqk dlevalthkd dninaltnci tqlnlleces esegqnkggn dsdelangev
     1381 ggdrnekmkn qikqmmdvsr tqtaisvvee dlkllqlklr asvstkcnle dqvkkleddr
     1441 nslqaakagl edecktlrqk veilnelyqq kemalqkkls qeeyerqere hrlsaadeka
     1501 vsaaeevkty krrieemede lqktersfkn qiathekkah enwlkaraae raiaeekrea
     1561 anlrhkllel tqkmamlqee pvivkpmpgk pntqnpprrg plsqngsfgp spvsggecsp
     1621 pltveppvrp lsatlnrrdm prsefgsvdg plphprwsae asgkpspsdp gsgtatmmns
     1681 ssrgssptrv ldegkvnmap kgpppfpgvp lmstpmggpv pppirygppp qlcgpfgprp
     1741 lpppfgpgmr pplglrefap gvppgrrdlp lhprgflpgh apfrplgslg preyfipgtr
     1801 lpppthgpqe yppppavrdl lpsgsrdepp pasqstsqdc sqalkqsp
//
LOCUS       NP_001304887             275 aa            linear   PRI 20-JAN-2026
DEFINITION  adenylate kinase 8 isoform 2 [Homo sapiens].
ACCESSION   NP_001304887 XP_011516582
VERSION     NP_001304887.1
DBSOURCE    REFSEQ: accession NM_001317958.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Dougherty,G.W., Mizuno,K., Nothe-Menchen,T., Ikawa,Y., Boldt,K.,
            Ta-Shma,A., Aprea,I., Minegishi,K., Pang,Y.P., Pennekamp,P.,
            Loges,N.T., Raidt,J., Hjeij,R., Wallmeier,J., Mussaffi,H.,
            Perles,Z., Elpeleg,O., Rabert,F., Shiratori,H., Letteboer,S.J.,
            Horn,N., Young,S., Strunker,T., Stumme,F., Werner,C., Olbrich,H.,
            Takaoka,K., Ide,T., Twan,W.K., Biebach,L., Grosse-Onnebrink,J.,
            Klinkenbusch,J.A., Praveen,K., Bracht,D.C., Hoben,I.M., Junger,K.,
            Gutzlaff,J., Cindric,S., Aviram,M., Kaiser,T., Memari,Y.,
            Dzeja,P.P., Dworniczak,B., Ueffing,M., Roepman,R., Bartscherer,K.,
            Katsanis,N., Davis,E.E., Amirav,I., Hamada,H. and Omran,H.
  TITLE     CFAP45 deficiency causes situs abnormalities and asthenospermia by
            disrupting an axonemal adenine nucleotide homeostasis module
  JOURNAL   Nat Commun 11 (1), 5520 (2020)
   PUBMED   33139725
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Amiri,M., Conserva,F., Panayiotou,C., Karlsson,A. and Solaroli,N.
  TITLE     The human adenylate kinase 9 is a nucleoside mono- and diphosphate
            kinase
  JOURNAL   Int J Biochem Cell Biol 45 (5), 925-931 (2013)
   PUBMED   23416111
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Panayiotou,C., Solaroli,N., Xu,Y., Johansson,M. and Karlsson,A.
  TITLE     The characterization of human adenylate kinases 7 and 8
            demonstrates differences in kinetic parameters and structural
            organization among the family of adenylate kinase isoenzymes
  JOURNAL   Biochem J 433 (3), 527-534 (2011)
   PUBMED   21080915
  REMARK    GeneRIF: Both AK7 and full-length AK8 showed highest affinity for
            AMP with ATP as the phosphate donor, and proved to be more
            efficient in AMP phosphorylation as compared with the major
            cytosolic isoform AK1
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Lesch,K.P., Timmesfeld,N., Renner,T.J., Halperin,R., Roser,C.,
            Nguyen,T.T., Craig,D.W., Romanos,J., Heine,M., Meyer,J.,
            Freitag,C., Warnke,A., Romanos,M., Schafer,H., Walitza,S., Reif,A.,
            Stephan,D.A. and Jacob,C.
  TITLE     Molecular genetics of adult ADHD: converging evidence from
            genome-wide association and extended pedigree linkage studies
  JOURNAL   J Neural Transm (Vienna) 115 (11), 1573-1585 (2008)
   PUBMED   18839057
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Van Rompay,A.R., Johansson,M. and Karlsson,A.
  TITLE     Identification of a novel human adenylate kinase. cDNA cloning,
            expression analysis, chromosome localization and characterization
            of the recombinant protein
  JOURNAL   Eur J Biochem 261 (2), 509-517 (1999)
   PUBMED   10215863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445645.10 and AL160165.17.
            
            On Dec 17, 2015 this sequence version replaced XP_011516582.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK093446.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..275
                     /product="adenylate kinase 8 isoform 2"
                     /EC_number="2.7.4.3"
                     /EC_number="2.7.4.6"
                     /note="putative adenylate kinase-like protein C9orf98;
                     ATP-AMP transphosphorylase 8"
                     /calculated_mol_wt=31324
     Region          66..258
                     /region_name="ADK"
                     /note="Adenylate kinase (ADK) catalyzes the reversible
                     phosphoryl transfer from adenosine triphosphates (ATP) to
                     adenosine monophosphates (AMP) and to yield adenosine
                     diphosphates (ADP). This enzyme is required for the
                     biosynthesis of ADP and is essential for...; cd01428"
                     /db_xref="CDD:238713"
     Site            order(95,100,123,149..150,152..153,157)
                     /site_type="other"
                     /note="AMP-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     Site            order(100,149,153,188,228,232)
                     /site_type="other"
                     /note="ATP-AMP (Ap5A)-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     CDS             1..275
                     /gene="AK8"
                     /gene_synonym="AK 8; C9orf98"
                     /coded_by="NM_001317958.2:649..1476"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:158067"
                     /db_xref="HGNC:HGNC:26526"
                     /db_xref="MIM:615365"
ORIGIN      
        1 mvpedisele taqklleyhr nivrvipsyp kilkvisadq pcvdvfyqal tyvqsnhrtn
       61 apftprvlll gpvgsgkslq aallaqkyrl vnvccgqllk eavadrttfg eliqpffeke
      121 mavpdsllmk vlsqrldqqd ciqkgwvlhg vprdldqahl lnrlgynpnr vfflnvpfds
      181 imerltlrri dpvtgeryhl mykppptmei qarllqnpkd aeeqvklkmd lfyrnsadle
      241 qlygsaitln gdqdpytvfe yiesgiinpl pkkip
//
LOCUS       NP_001310224             826 aa            linear   PRI 20-JAN-2026
DEFINITION  zinc finger protein 197 isoform 3 [Homo sapiens].
ACCESSION   NP_001310224 XP_011531561 XP_011547030
VERSION     NP_001310224.1
DBSOURCE    REFSEQ: accession NM_001323295.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   2  (residues 1 to 826)
  AUTHORS   Li,Z., Wang,D., Na,X., Schoen,S.R., Messing,E.M. and Wu,G.
  TITLE     The VHL protein recruits a novel KRAB-A domain protein to repress
            HIF-1alpha transcriptional activity
  JOURNAL   EMBO J 22 (8), 1857-1867 (2003)
   PUBMED   12682018
  REMARK    GeneRIF: a novel pVHL-interacting protein that functions as a
            negative regulator of hypoxia-inducible factor-1a (HIF-1alpha)
            transactivation; demonstrate that the KRAB-A domain in VHLaK
            mediates pVHL binding and functions as a transcriptional repression
            module
REFERENCE   3  (residues 1 to 826)
  AUTHORS   Gonsky,R., Knauf,J.A., Elisei,R., Wang,J.W., Su,S. and Fagin,J.A.
  TITLE     Identification of rapid turnover transcripts overexpressed in
            thyroid tumors and thyroid cancer cell lines: use of a targeted
            differential RNA display method to select for mRNA subsets
  JOURNAL   Nucleic Acids Res 25 (19), 3823-3831 (1997)
   PUBMED   9380504
REFERENCE   4  (residues 1 to 826)
  AUTHORS   Calabro,V., Pengue,G., Bartoli,P.C., Pagliuca,A., Featherstone,T.
            and Lania,L.
  TITLE     Positional cloning of cDNAs from the human chromosome 3p21-22
            region identifies a clustered organization of zinc-finger genes
  JOURNAL   Hum Genet 95 (1), 18-21 (1995)
   PUBMED   7814019
REFERENCE   5  (residues 1 to 826)
  AUTHORS   Pengue,G., Calabro,V., Cannada-Bartoli,P., De Luca,P., Esposito,T.,
            Taillon-Miller,P., LaForgia,S., Druck,T., Huebner,K., D'Urso,M. et
            al.
  TITLE     YAC-assisted cloning of transcribed sequences from the human
            chromosome 3p21 region
  JOURNAL   Hum Mol Genet 2 (6), 791-796 (1993)
   PUBMED   8353497
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099669.2 and BQ002665.1.
            
            On or before Jul 8, 2016 this sequence version replaced
            XP_011531561.1, XP_011547030.1.
            
            Summary: This gene product belongs to the zinc finger protein
            superfamily, members of which are regulatory proteins characterized
            by nucleic acid-binding zinc finger domains. The encoded protein
            contains 20 tandemly arrayed C2H2-type zinc fingers, a
            Kruppel-associated box (KRAB) domain, and a SCAN box. This
            transcript turns over rapidly and contains 3' UTR AUUUA motifs,
            which are often a hallmark of rapid turnover. It is overexpressed
            in some thyroid papillary carcinomas. This gene is located in a
            cluster of zinc finger genes at 3p21. Naturally-occurring
            readthrough transcription is observed between this gene and the
            upstream zinc finger protein 660 gene and is represented by
            GeneID:110354863. [provided by RefSeq, May 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.37936.1,
                                           SRR1803612.140225.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..826
                     /product="zinc finger protein 197 isoform 3"
                     /note="zinc finger protein 166; VHL-associated KRAB-A
                     domain-containing protein; zinc finger protein with KRAB
                     and SCAN domains 9; pVHL-associated KRAB domain-containing
                     protein"
                     /calculated_mol_wt=96066
     Region          13..53
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     Region          169..189
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          181..206
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          197..217
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(202,204,206,208..209,212..213,216,230,232,236..237,
                     240..241,244,258,260,262,264..265,268..269,272)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          221..650
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          225..245
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          253..273
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          281..301
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          309..329
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          337..357
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          365..385
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          393..413
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(398,400,402,404..405,408..409,412,426,428,432..433,
                     436..437,440,454,456,458,460..461,464..465,468)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          421..441
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          449..469
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          477..497
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          505..525
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          533..553
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          557..>806
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          561..581
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          589..609
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(594,596,598,600..601,604..605,608,622,624,628..629,
                     632..633,636,650,652,654,656..657,660..661,664)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          617..637
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          645..665
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          673..693
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          701..721
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          729..749
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          757..777
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          785..805
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..826
                     /gene="ZNF197"
                     /gene_synonym="D3S1363E; P18; VHLaK; ZKSCAN9; ZNF166;
                     ZSCAN41"
                     /coded_by="NM_001323295.2:932..3412"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:10168"
                     /db_xref="HGNC:HGNC:12988"
                     /db_xref="MIM:618359"
ORIGIN      
        1 malmlltaqp qelvmfeevs vcftseewac lgpiqralyw dvmlenygnv tslewetmte
       61 neevtskpss sqradshkgt skrlqgsvpq vldfeeecew qvlasqwgne tderadtvkk
      121 vslcerdkkk rtppekqgqk wkelgdsltf gsaiseslig tegkkfykcd mcckhfnkis
      181 hlinhrriht gekphkckec gkgfiqrssl lmhlrnhsge kpykcnecgk afsqsaylln
      241 hqrihtgekp ykckecgkgf yrhsgliihl rrhsgerpyk cnecgkvfsq naylidhqrl
      301 hkgeepykcn kcqkafilkk slilhqrihs gekpykcdec gktfaqttyl idhqrlhsae
      361 npykckecgk vfirskslll hqrvhtekkt fgckkcgkif ssksnfidhk rmhsrekpyk
      421 ctecgkaftq saylfdhqrl hngekpyecn ecgkvfilkk slilhqrfht genlyeckdc
      481 gkvfgsnrnl idherlhnge kpyecrecgk tfimsksfmv hqklhtqeka ykcedcgkaf
      541 synssllvhr rihtgekpfe csecgrafss nrnliehkri hsgekpyecd ecgkcfilkk
      601 slighqriht reksykcndc gkvfsyrsnl iahqrihtge kpyacsecgk gftynrnlie
      661 hqrihsgekt yechvcrkvl tssrnlmvhq rihtgekpyk cnecgkdfsq nknlvvhqrm
      721 htgekpyecd kcrksftskr nlvghqriht gekpygcndc skvfrqrknl tvhqkihtde
      781 kpcecdvsek efsqtsnlhl qqkihtieef swlqntnesk ieiqki
//
LOCUS       NP_940953               1907 aa            linear   PRI 20-JAN-2026
DEFINITION  transport and Golgi organization protein 1 homolog isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_940953 XP_046126
VERSION     NP_940953.2
DBSOURCE    REFSEQ: accession NM_198551.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1907)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1907)
  AUTHORS   Wanbiao,Z., Jing,M., Shi,Z., Tengxiang,C., Xueke,Z. and Haiyang,L.
  TITLE     MIA3 promotes the degradation of GSH (glutathione) by binding to
            CHAC1, thereby promoting the progression of hepatocellular
            carcinoma
  JOURNAL   Mol Cell Biochem 479 (10), 2769-2784 (2024)
   PUBMED   37948019
  REMARK    GeneRIF: MIA3 promotes the degradation of GSH (glutathione) by
            binding to CHAC1, thereby promoting the progression of
            hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 1907)
  AUTHORS   Connolly,L.M., McFalls,C.M., McMahon,I.G., Bhat,A.M. and
            Artlett,C.M.
  TITLE     Caspase 1 Enhances Transport and Golgi Organization Protein 1
            Expression to Promote Procollagen Export From the Endoplasmic
            Reticulum in Systemic Sclerosis Contributing to Fibrosis
  JOURNAL   Arthritis Rheumatol 75 (10), 1831-1841 (2023)
   PUBMED   37067501
  REMARK    GeneRIF: Caspase 1 Enhances Transport and Golgi Organization
            Protein 1 Expression to Promote Procollagen Export From the
            Endoplasmic Reticulum in Systemic Sclerosis Contributing to
            Fibrosis.
REFERENCE   4  (residues 1 to 1907)
  AUTHORS   Man,J., Zhou,W., Zuo,S., Zhao,X., Wang,Q., Ma,H. and Li,H.Y.
  TITLE     TANGO1 interacts with NRTN to promote hepatocellular carcinoma
            progression by regulating the PI3K/AKT/mTOR signaling pathway
  JOURNAL   Biochem Pharmacol 213, 115615 (2023)
   PUBMED   37211171
  REMARK    GeneRIF: TANGO1 interacts with NRTN to promote hepatocellular
            carcinoma progression by regulating the PI3K/AKT/mTOR signaling
            pathway.
REFERENCE   5  (residues 1 to 1907)
  AUTHORS   Junkiert-Czarnecka,A., Pilarska-Deltow,M., Bak,A., Heise,M. and
            Haus,O.
  TITLE     A novel mutation in collagen transport protein, MIA3 gene, detected
            in a patient with clinical symptoms of Ehlers-Danlos hypermobile
            syndrome
  JOURNAL   Adv Clin Exp Med 32 (7), 777-781 (2023)
   PUBMED   36603143
  REMARK    GeneRIF: A novel mutation in collagen transport protein, MIA3 gene,
            detected in a patient with clinical symptoms of Ehlers-Danlos
            hypermobile syndrome.
REFERENCE   6  (residues 1 to 1907)
  AUTHORS   Saito,K., Chen,M., Bard,F., Chen,S., Zhou,H., Woodley,D.,
            Polischuk,R., Schekman,R. and Malhotra,V.
  TITLE     TANGO1 facilitates cargo loading at endoplasmic reticulum exit
            sites
  JOURNAL   Cell 136 (5), 891-902 (2009)
   PUBMED   19269366
REFERENCE   7  (residues 1 to 1907)
  AUTHORS   Arndt,S., Melle,C., Mondal,K., Klein,G., von Eggeling,F. and
            Bosserhoff,A.K.
  TITLE     Interactions of TANGO and leukocyte integrin CD11c/CD18 regulate
            the migration of human monocytes
  JOURNAL   J Leukoc Biol 82 (6), 1466-1472 (2007)
   PUBMED   17726152
  REMARK    GeneRIF: The results from this study present TANGO as a novel
            ligand for CD11c, regulating migratory processes of hematopoietic
            cells.
REFERENCE   8  (residues 1 to 1907)
  AUTHORS   Arndt,S. and Bosserhoff,A.K.
  TITLE     Reduced expression of TANGO in colon and hepatocellular carcinomas
  JOURNAL   Oncol Rep 18 (4), 885-891 (2007)
   PUBMED   17786351
  REMARK    GeneRIF: Reduced expression of TANGO is associated with colon and
            hepatocellular carcinomas
REFERENCE   9  (residues 1 to 1907)
  AUTHORS   Arndt,S. and Bosserhoff,A.K.
  TITLE     TANGO is a tumor suppressor of malignant melanoma
  JOURNAL   Int J Cancer 119 (12), 2812-2820 (2006)
   PUBMED   17044017
  REMARK    GeneRIF: TANGO transfected cell lines revealed that TANGO
            expression reduces motility, whereas reduction of TANGO enhances
            migration.
REFERENCE   10 (residues 1 to 1907)
  AUTHORS   Bosserhoff,A.K., Moser,M. and Buettner,R.
  TITLE     Characterization and expression pattern of the novel MIA homolog
            TANGO
  JOURNAL   Gene Expr Patterns 4 (4), 473-479 (2004)
   PUBMED   15183315
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL592148.7, DA040423.1, AK096526.1, D87742.1, BP423646.1 and
            CK724924.1.
            
            On Jan 17, 2007 this sequence version replaced NP_940953.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.49234.1,
                                           SRR1803617.42223.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000344922.10/ ENSP00000340900.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1907
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..1907
                     /product="transport and Golgi organization protein 1
                     homolog isoform 1 precursor"
                     /note="C219-reactive peptide; melanoma inhibitory activity
                     protein 3; MIA family member 3, ER export factor; melanoma
                     inhibitory activity family, member 3; transport and Golgi
                     organization protein 1 homolog"
                     /calculated_mol_wt=211292
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2429
     mat_peptide     23..1907
                     /product="Transport and Golgi organization protein 1
                     homolog. /id=PRO_0000288998"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JRA6.1)"
                     /calculated_mol_wt=211292
     Region          37..109
                     /region_name="SH3_MIA3"
                     /note="Src Homology 3 domain of Melanoma Inhibitory
                     Activity 3 protein; cd11893"
                     /db_xref="CDD:212826"
     Site            order(54..56,59..63,84..85,96..98,100..101)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:212826"
     Region          155..258
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            246
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Region          314..378
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Region          390..601
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            589
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Region          659..918
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            727
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            876
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            1067
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Region          1093..1121
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            1177..1197
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Region          1211..1650
                     /region_name="Mediates interaction with MIA2.
                     /evidence=ECO:0000269|PubMed:21525241"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Region          <1217..1526
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          1420..1443
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            1431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BI84; propagated from
                     UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Region          <1470..>1639
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1642..1907
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Region          <1647..1892
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BI84; propagated from
                     UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            1678
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BI84; propagated from
                     UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            1706
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            1727
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BI84; propagated from
                     UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            1741
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BI84; propagated from
                     UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            1745
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Region          1751..1907
                     /region_name="Proline-rich domain (PRD), mediates
                     interaction with the COPII coat subunits SEC23A and
                     SEC23B. /evidence=ECO:0000269|PubMed:19269366,
                     ECO:0000269|PubMed:27551091, ECO:0000269|PubMed:28442536"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            1784
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BI84; propagated from
                     UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Region          1788..1847
                     /region_name="SEC16A-interacting region (SIR), required
                     for its localization to endoplasmic reticulum exit sites
                     and for its interaction with SEC16A.
                     /evidence=ECO:0000269|PubMed:28442536"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            1892
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BI84; propagated from
                     UniProtKB/Swiss-Prot (Q5JRA6.1)"
     Site            1906
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q5JRA6.1)"
     CDS             1..1907
                     /gene="MIA3"
                     /gene_synonym="D320; ODCD2; TANGO; TANGO1; UNQ6077"
                     /coded_by="NM_198551.4:15..5738"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS41470.1"
                     /db_xref="GeneID:375056"
                     /db_xref="HGNC:HGNC:24008"
                     /db_xref="MIM:613455"
ORIGIN      
        1 maaapgllvw llvlrlpwrv pgqldpstgr rfsehklcad decsmlmyrg ealedftgpd
       61 crfvnfkkgd pvyvyyklar gwpevwagsv grtfgyfpkd liqvvheytk eelqvptdet
      121 dfvcfdggrd dfhnynveel lgflelynsa atdsekavek tlqdmeknpe lskerepepe
      181 pveanseesd svfsentedl qeqfttqkhh shansqanha qgeqasfesf eemlqdklkv
      241 pesennktsn ssqvsneqdk idaykllkke mtldlktkfg stadalvsdd ettrlvtsle
      301 ddfdeeldte yyavgkedee nqedfdelpl ltftdgedmk tpaksgveky ptdkeqnsne
      361 edkvqltvpp giknddknil ttwgdtifsi vtggeetrdt mdlessssee ekeddddalv
      421 pdskqgkpqs atdysdpdnv ddglfivdip ktnndkevna ehhikgkgrg vqeskrglvq
      481 dkteledenq egmtvhssvh snnlnsmpaa ekgkdtlksa yddtendlkg aaihiskgml
      541 heekpgeqil eggsesesaq kaagnqmndr kiqqeslgsa plmgddhpna srdsvegdal
      601 vngaklhtls vehqreelke elvlktqnqp rfsspdeidl preledevpi lgrnlpwqqe
      661 rdvaataskq msekirlseg eakedsldee ffhhkamqgt evgqtdqtds tggpaflskv
      721 eeddypseel ledenainak rskeknpgnq grqfdvnlqv pdravlgtih pdpeieeskq
      781 etsmildsek tsetaakgvn tggrepntmv ekerpladkk aqrpfersdf sdsikiqtpe
      841 lgevfqnkds dylkndnpee hlktsglage pegelskedh entekymgte sqgsaaaepe
      901 ddsfhwtpht svepghsdkr edlliissff keqqslqrfq kyfnvhelea llqemssklk
      961 saqqeslpyn mekvldkvfr asesqilsia ekmldtrvae nrdlgmnenn ifeeaavldd
     1021 iqdliyfvry khstaeetat lvmappleeg lggameemqp lhednfsrek taelnvqvpe
     1081 epthldqrvi gdthasevsq kpntekdldp gpvttedtpm daidankqpe taaeepasvt
     1141 plenailliy sfmfyltksl vatlpddvqp gpdfyglpwk pvfitaflgi asfaiflwrt
     1201 vlvvkdrvyq vteqqisekl ktimkentel vqklsnyeqk ikeskkhvqe trkqnmilsd
     1261 eaikykdkik tleknqeild dtaknlrvml esereqnvkn qdlisenkks ieklkdvism
     1321 nasefsevqi alneaklsee kvksechrvq eenarlkkkk eqlqqeiedw sklhaelseq
     1381 iksfeksqkd levalthkdd ninaltncit qlnllecese segqnkggnd sdelangevg
     1441 gdrnekmknq ikqmmdvsrt qtaisvveed lkllqlklra svstkcnled qvkkleddrn
     1501 slqaakagle decktlrqkv eilnelyqqk emalqkklsq eeyerqereh rlsaadekav
     1561 saaeevktyk rrieemedel qktersfknq iathekkahe nwlkaraaer aiaeekreaa
     1621 nlrhkllelt qkmamlqeep vivkpmpgkp ntqnpprrgp lsqngsfgps pvsggecspp
     1681 ltveppvrpl satlnrrdmp rsefgsvdgp lphprwsaea sgkpspsdpg sgtatmmnss
     1741 srgssptrvl degkvnmapk gpppfpgvpl mstpmggpvp ppirygpppq lcgpfgprpl
     1801 pppfgpgmrp plglrefapg vppgrrdlpl hprgflpgha pfrplgslgp reyfipgtrl
     1861 pppthgpqey ppppavrdll psgsrdeppp asqstsqdcs qalkqsp
//
LOCUS       NP_001352233             139 aa            linear   PRI 20-JAN-2026
DEFINITION  uncharacterized protein LOC112694756 isoform 1 [Homo sapiens].
ACCESSION   NP_001352233
VERSION     NP_001352233.1
DBSOURCE    REFSEQ: accession NM_001365304.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Kimura,K., Wakamatsu,A., Suzuki,Y., Ota,T., Nishikawa,T.,
            Yamashita,R., Yamamoto,J., Sekine,M., Tsuritani,K., Wakaguri,H.,
            Ishii,S., Sugiyama,T., Saito,K., Isono,Y., Irie,R., Kushida,N.,
            Yoneyama,T., Otsuka,R., Kanda,K., Yokoi,T., Kondo,H., Wagatsuma,M.,
            Murakawa,K., Ishida,S., Ishibashi,T., Takahashi-Fujii,A.,
            Tanase,T., Nagai,K., Kikuchi,H., Nakai,K., Isogai,T. and Sugano,S.
  TITLE     Diversification of transcriptional modulation: large-scale
            identification and characterization of putative alternative
            promoters of human genes
  JOURNAL   Genome Res 16 (1), 55-65 (2006)
   PUBMED   16344560
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093512.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC004333.1, SRR1803616.127242.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000338110.11/ ENSP00000336927.6
            NMD candidate          :: translation inferred from conservation
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..139
                     /product="uncharacterized protein LOC112694756 isoform 1"
                     /calculated_mol_wt=14667
     CDS             1..139
                     /gene="LOC112694756"
                     /coded_by="NM_001365304.2:98..517"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS92136.1"
                     /db_xref="GeneID:112694756"
ORIGIN      
        1 mdassspwnp tpapvssppl llpipaivfi avgiyllllg lvlltrncll aqgccadgss
       61 pcrkqgssgp pdccwtcaea cnfplpspah fldaccpqpt radwaprcpr ccplcdcact
      121 cqlpdcqsln clcfeiklr
//
LOCUS       NP_647536                412 aa            linear   PRI 20-JAN-2026
DEFINITION  CHRNA7-FAM7A fusion protein isoform 1 [Homo sapiens].
ACCESSION   NP_647536
VERSION     NP_647536.1
DBSOURCE    REFSEQ: accession NM_139320.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Gorgulu,I., Jagannath,V., Pons,S., Koniuszewski,F., Groszer,M.,
            Maskos,U., Huck,S. and Scholze,P.
  TITLE     The human-specific nicotinic receptor subunit CHRFAM7A reduces
            alpha7 receptor function in human induced pluripotent stem
            cells-derived and transgenic mouse neurons
  JOURNAL   Eur J Neurosci 60 (5), 4893-4906 (2024)
   PUBMED   39073048
  REMARK    GeneRIF: The human-specific nicotinic receptor subunit CHRFAM7A
            reduces alpha7 receptor function in human induced pluripotent stem
            cells-derived and transgenic mouse neurons.
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Szigeti,K., Ihnatovych,I., Notari,E., Dorn,R.P., Maly,I., He,M.,
            Birkaya,B., Prasad,S., Byrne,R.S., Indurthi,D.C., Nimmer,E.,
            Heo,Y., Retfalvi,K., Chaves,L., Sule,N., Hofmann,W.A., Auerbach,A.,
            Wilding,G., Bae,Y. and Reynolds,J.
  TITLE     CHRFAM7A diversifies human immune adaption through Ca2+ signalling
            and actin cytoskeleton reorganization
  JOURNAL   EBioMedicine 103, 105093 (2024)
   PUBMED   38569318
  REMARK    GeneRIF: CHRFAM7A diversifies human immune adaption through Ca[2+]
            signalling and actin cytoskeleton reorganization.
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Pradhan,A., Mounford,H., Peixinho,J., Rea,E., Epeslidou,E.,
            Scott,J.S., Cull,J., Maxwell,S., Webster,R., Beeson,D., Dong,Y.Y.,
            Prekovic,S., Bermudez,I. and Newbury,D.F.
  TITLE     Unraveling the molecular interactions between alpha7 nicotinic
            receptor and a RIC3 variant associated with backward speech
  JOURNAL   Cell Mol Life Sci 81 (1), 129 (2024)
   PUBMED   38472514
  REMARK    GeneRIF: Unraveling the molecular interactions between alpha7
            nicotinic receptor and a RIC3 variant associated with backward
            speech.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Burke,S.M., Avstrikova,M., Noviello,C.M., Mukhtasimova,N.,
            Changeux,J.P., Thakur,G.A., Sine,S.M., Cecchini,M. and Hibbs,R.E.
  TITLE     Structural mechanisms of alpha7 nicotinic receptor allosteric
            modulation and activation
  JOURNAL   Cell 187 (5), 1160-1176 (2024)
   PUBMED   38382524
  REMARK    GeneRIF: Structural mechanisms of alpha7 nicotinic receptor
            allosteric modulation and activation.
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Prevost,M.S., Barilone,N., Dejean de la Batie,G., Pons,S., Ayme,G.,
            England,P., Gielen,M., Bontems,F., Pehau-Arnaudet,G., Maskos,U.,
            Lafaye,P. and Corringer,P.J.
  TITLE     An original potentiating mechanism revealed by the cryo-EM
            structures of the human alpha7 nicotinic receptor in complex with
            nanobodies
  JOURNAL   Nat Commun 14 (1), 5964 (2023)
   PUBMED   37749098
  REMARK    GeneRIF: An original potentiating mechanism revealed by the cryo-EM
            structures of the human alpha7 nicotinic receptor in complex with
            nanobodies.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 412)
  AUTHORS   Bale,A.S., Meacham,C.A., Benignus,V.A., Bushnell,P.J. and
            Shafer,T.J.
  TITLE     Volatile organic compounds inhibit human and rat neuronal nicotinic
            acetylcholine receptors expressed in Xenopus oocytes
  JOURNAL   Toxicol Appl Pharmacol 205 (1), 77-88 (2005)
   PUBMED   15885267
  REMARK    GeneRIF: Results demonstrate that human and rat nicotinic
            acetylcholine receptors are senstive targets for volatile organic
            compounds in industrial products and are used in the risk
            assessment of these compounds.
REFERENCE   7  (residues 1 to 412)
  AUTHORS   Trombino,S., Cesario,A., Margaritora,S., Granone,P., Motta,G.,
            Falugi,C. and Russo,P.
  TITLE     Alpha7-nicotinic acetylcholine receptors affect growth regulation
            of human mesothelioma cells: role of mitogen-activated protein
            kinase pathway
  JOURNAL   Cancer Res 64 (1), 135-145 (2004)
   PUBMED   14729617
  REMARK    GeneRIF: Human mesothelioma cells and human biopsies of
            mesothelioma as well as of normal pleural mesothelial cells
            functionally express CHRNA7.
            Erratum:[Cancer Res. 2004 Feb 15;64(4):1559]
REFERENCE   8  (residues 1 to 412)
  AUTHORS   Riley,B., Williamson,M., Collier,D., Wilkie,H. and Makoff,A.
  TITLE     A 3-Mb map of a large Segmental duplication overlapping the
            alpha7-nicotinic acetylcholine receptor gene (CHRNA7) at human
            15q13-q14
  JOURNAL   Genomics 79 (2), 197-209 (2002)
   PUBMED   11829490
  REMARK    GeneRIF: 3-Mb map of 15q13-q14 showing that CHRFAM7A is part of a
            large segmental duplication in the opposite orientation to CHRNA7
            and revealing several other duplications
REFERENCE   9  (residues 1 to 412)
  AUTHORS   Freedman,R., Leonard,S., Gault,J.M., Hopkins,J., Cloninger,C.R.,
            Kaufmann,C.A., Tsuang,M.T., Farone,S.V., Malaspina,D.,
            Svrakic,D.M., Sanders,A. and Gejman,P.
  TITLE     Linkage disequilibrium for schizophrenia at the chromosome 15q13-14
            locus of the alpha7-nicotinic acetylcholine receptor subunit gene
            (CHRNA7)
  JOURNAL   Am J Med Genet 105 (1), 20-22 (2001)
   PUBMED   11424985
REFERENCE   10 (residues 1 to 412)
  AUTHORS   Gault,J., Robinson,M., Berger,R., Drebing,C., Logel,J., Hopkins,J.,
            Moore,T., Jacobs,S., Meriwether,J., Choi,M.J., Kim,E.J., Walton,K.,
            Buiting,K., Davis,A., Breese,C., Freedman,R. and Leonard,S.
  TITLE     Genomic organization and partial duplication of the human alpha7
            neuronal nicotinic acetylcholine receptor gene (CHRNA7)
  JOURNAL   Genomics 52 (2), 173-185 (1998)
   PUBMED   9782083
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC019322.8.
            
            Summary: The nicotinic acetylcholine receptors (nAChRs) are members
            of a superfamily of ligand-gated ion channels that mediate fast
            signal transmission at synapses. The family member CHRNA7, which is
            located on chromosome 15 in a region associated with several
            neuropsychiatric disorders, is partially duplicated and forms a
            hybrid with a novel gene from the family with sequence similarity 7
            (FAM7A). Alternative splicing has been observed, and two variants
            exist, for this hybrid gene. The N-terminally truncated products
            predicted by the largest open reading frames for each variant would
            lack the majority of the neurotransmitter-gated ion-channel ligand
            binding domain but retain the transmembrane region that forms the
            ion channel. Although current evidence supports transcription of
            this hybrid gene, translation of the nicotinic acetylcholine
            receptor-like protein-encoding open reading frames has not been
            confirmed. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) is the full-length variant and
            encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC101346.2, SRR18074969.3042069.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000299847.7/ ENSP00000299847.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q13.2"
     Protein         1..412
                     /product="CHRNA7-FAM7A fusion protein isoform 1"
                     /note="CHRNA7 (cholinergic receptor, nicotinic, alpha
                     polypeptide 7, exons 5-10) and FAM7A (family with sequence
                     similarity 7A, exons A-E) fusion; alpha 7 neuronal
                     nicotinic acetylcholine receptor-FAM7A hybrid;
                     CHRNA7-FAM7A fusion protein; alpha-7 nicotinic cholinergic
                     receptor subunit; CHRNA7 (cholinergic receptor, nicotinic,
                     alpha 7, exons 5-10) and FAM7A (family with sequence
                     similarity 7A, exons A-E) fusion"
                     /calculated_mol_wt=46087
     Region          <28..400
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q494W8.1)"
     Site            172..192
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q494W8.1)"
     Site            205..225
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q494W8.1)"
     Site            240..254
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q494W8.1)"
     Site            380..400
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q494W8.1)"
     CDS             1..412
                     /gene="CHRFAM7A"
                     /gene_synonym="CHRNA7; CHRNA7-DR1; D-10"
                     /coded_by="NM_139320.2:446..1684"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32184.1"
                     /db_xref="GeneID:89832"
                     /db_xref="HGNC:HGNC:15781"
                     /db_xref="MIM:609756"
ORIGIN      
        1 mqkyciyqhf qfqlliqhlw iaancdiade rfdatfhtnv lvnssghcqy lppgifkssc
       61 yidvrwfpfd vqhcklkfgs wsyggwsldl qmqeadisgy ipngewdlvg ipgkrserfy
      121 ecckepypdv tftvtmrrrt lyyglnllip cvlisalall vfllpadsge kislgitvll
      181 sltvfmllva eimpatsdsv pliaqyfast miivglsvvv tvivlqyhhh dpdggkmpkw
      241 trvillnwca wflrmkrpge dkvrpacqhk qrrcslasve msavapppas ngnllyigfr
      301 gldgvhcvpt pdsgvvcgrm acspthdehl lhggqppegd pdlakileev ryianrfrcq
      361 deseavcsew kfaacvvdrl clmafsvfti ictigilmsa pnfveavskd fa
//
LOCUS       NP_001005240             305 aa            linear   PRI 20-JAN-2026
DEFINITION  olfactory receptor 4F17 isoform 1 [Homo sapiens].
ACCESSION   NP_001005240 XP_005259705
VERSION     NP_001005240.1
DBSOURCE    REFSEQ: accession NM_001005240.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Linardopoulou,E., Mefford,H.C., Nguyen,O., Friedman,C., van den
            Engh,G., Farwell,D.G., Coltrera,M. and Trask,B.J.
  TITLE     Transcriptional activity of multiple copies of a subtelomerically
            located olfactory receptor gene that is polymorphic in number and
            location
  JOURNAL   Hum Mol Genet 10 (21), 2373-2383 (2001)
   PUBMED   11689484
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Mefford,H.C., Linardopoulou,E., Coil,D., van den Engh,G. and
            Trask,B.J.
  TITLE     Comparative sequencing of a multicopy subtelomeric region
            containing olfactory receptor genes reveals multiple interactions
            between non-homologous chromosomes
  JOURNAL   Hum Mol Genet 10 (21), 2363-2372 (2001)
   PUBMED   11689483
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Trask,B.J., Friedman,C., Martin-Gallardo,A., Rowen,L., Akinbami,C.,
            Blankenship,J., Collins,C., Giorgi,D., Iadonato,S., Johnson,F.,
            Kuo,W.L., Massa,H., Morrish,T., Naylor,S., Nguyen,O.T.,
            Rouquier,S., Smith,T., Wong,D.J., Youngblom,J. and van den Engh,G.
  TITLE     Members of the olfactory receptor gene family are contained in
            large blocks of DNA duplicated polymorphically near the ends of
            human chromosomes
  JOURNAL   Hum Mol Genet 7 (1), 13-26 (1998)
   PUBMED   9384599
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008977.9.
            
            On Apr 26, 2019 this sequence version replaced XP_005259705.1.
            
            Summary: Olfactory receptors interact with odorant molecules in the
            nose, to initiate a neuronal response that triggers the perception
            of a smell. The olfactory receptor proteins are members of a large
            family of G-protein-coupled receptors (GPCR) arising from single
            coding-exon genes. Olfactory receptors share a 7-transmembrane
            domain structure with many neurotransmitter and hormone receptors
            and are responsible for the recognition and G protein-mediated
            transduction of odorant signals. The olfactory receptor gene family
            is the largest in the genome. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY972817.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000585993.3/
                                                ENSP00000467301.1
            RefSeq Select criteria           :: based on manual assertion,
                                                conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..305
                     /product="olfactory receptor 4F17 isoform 1"
                     /note="olfactory receptor, family 4, subfamily F, member
                     11 pseudogene; olfactory receptor, family 4, subfamily F,
                     member 19; olfactory receptor 4F17; olfactory receptor
                     4F11; olfactory receptor 4F18; olfactory receptor 4F19"
                     /calculated_mol_wt=34081
     Region          19..284
                     /region_name="7tmA_OR4-like"
                     /note="olfactory receptor family 4 and related proteins,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15226"
                     /db_xref="CDD:320354"
     Region          19..45
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320354"
     Site            19..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NGA8.1)"
     Site            51..72
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NGA8.1)"
     Region          52..78
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320354"
     Site            order(74,77..78,90..95,97..98,101,146,148..152,188,
                     191..193,195..197,199..200,244,247..248,250..251,254,
                     258..259,261..263,266,269..270)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320354"
     Region          90..120
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320354"
     Site            94..113
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NGA8.1)"
     Region          133..154
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320354"
     Site            133..151
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NGA8.1)"
     Region          188..218
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320354"
     Site            189..212
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NGA8.1)"
     Region          224..254
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320354"
     Site            229..251
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NGA8.1)"
     Region          259..284
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320354"
     Site            263..282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NGA8.1)"
     CDS             1..305
                     /gene="OR4F17"
                     /gene_synonym="OR4F11P; OR4F18; OR4F19"
                     /coded_by="NM_001005240.3:192..1109"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32854.1"
                     /db_xref="GeneID:81099"
                     /db_xref="HGNC:HGNC:15381"
ORIGIN      
        1 mvtefiflgl sdsqglqtfl fmlffvfygg ivfgnllivi tvvsdshlhs pmyfllanls
       61 lidlslssvt apkmitdffs qrkvisfkgc lvqifllhff ggsemvilia mgfdryiaic
      121 kplhyttimc gnacvgimav awgigflhsv sqlafavhlp fcgpnevdsf ycdlprvikl
      181 actdtyrldi mviansgvlt vcsfvlliis ytiilmtiqh rpldksskal stltahitvv
      241 llffgpcvfi yawpfpiksl dkflavfysv itpllnpiiy tlrnkdmkta irqlrkwdah
      301 ssvkf
//
LOCUS       NP_001288637             333 aa            linear   PRI 20-JAN-2026
DEFINITION  pregnancy-specific beta-1-glycoprotein 9 isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_001288637 XP_005259134
VERSION     NP_001288637.1
DBSOURCE    REFSEQ: accession NM_001301708.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Kandel,M., MacDonald,T.M., Walker,S.P., Cluver,C., Bergman,L.,
            Myers,J., Hastie,R., Keenan,E., Hannan,N.J., Cannon,P.,
            Nguyen,T.V., Pritchard,N., Tong,S. and Kaitu'u-Lino,T.J.
  TITLE     PSG7 and 9 (Pregnancy-Specific beta-1 Glycoproteins 7 and 9): Novel
            Biomarkers for Preeclampsia
  JOURNAL   J Am Heart Assoc 11 (7), e024536 (2022)
   PUBMED   35322669
  REMARK    GeneRIF: PSG7 and 9 (Pregnancy-Specific beta-1 Glycoproteins 7 and
            9): Novel Biomarkers for Preeclampsia.
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Rong,W., Zhang,Y., Yang,L., Feng,L., Wei,B., Wu,F., Wang,L.,
            Gao,Y., Cheng,S., Wu,J. and Xiao,T.
  TITLE     Post-surgical resection prognostic value of combined OPN, MMP7, and
            PSG9 plasma biomarkers in hepatocellular carcinoma
  JOURNAL   Front Med 13 (2), 250-258 (2019)
   PUBMED   29770948
  REMARK    GeneRIF: Plasma OPN + MMP7 + PSG9 elevation in combination was a
            prognostic factor for overall survival in hepatocellular carcinoma
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Rong,W., Yang,L., Yin,L., Gao,Y., Xiao,T. and Cheng,S.
  TITLE     PSG9 promotes angiogenesis by stimulating VEGFA production and is
            associated with poor prognosis in hepatocellular carcinoma
  JOURNAL   Sci China Life Sci 60 (5), 528-535 (2017)
   PUBMED   28078509
  REMARK    GeneRIF: Results indicate that pregnancy-specific glycoprotein 9
            (PSG9) may facilitate the development of hepatocellular carcinoma
            (HCC) by fostering angiogenesis via promoting VEGFA production in
            cancer HCC.
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Yang,L., Hu,S., Tan,J., Zhang,X., Yuan,W., Wang,Q., Xu,L., Liu,J.,
            Liu,Z., Jia,Y. and Huang,X.
  TITLE     Pregnancy-specific glycoprotein 9 (PSG9), a driver for colorectal
            cancer, enhances angiogenesis via activation of SMAD4
  JOURNAL   Oncotarget 7 (38), 61562-61574 (2016)
   PUBMED   27528036
  REMARK    GeneRIF: Findings illustrate the innovative mechanism by which PSG9
            drives the progression of colorectal cancer and tumor angiogenesis.
            This occurs via nuclear translocation of PSG9/SMAD4, which
            activates angiogenic cytokines.
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Brophy,B.K., MacDonald,R.E., McLenachan,P.A. and Mansfield,B.C.
  TITLE     cDNA sequence of the pregnancy-specific beta 1-glycoprotein-11s
            (PSG-11s)
  JOURNAL   Biochim Biophys Acta 1131 (1), 119-121 (1992)
   PUBMED   1581354
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Chan,W.Y., Zheng,Q.X., McMahon,J. and Tease,L.A.
  TITLE     Characterization of new members of the pregnancy-specific beta
            1-glycoprotein family
  JOURNAL   Mol Cell Biochem 106 (2), 161-170 (1991)
   PUBMED   1922019
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Khan,W.N. and Hammarstrom,S.
  TITLE     Identification of a new carcinoembryonic antigen (CEA) family
            member in human fetal liver--cloning and sequence determination of
            pregnancy-specific glycoprotein 7
  JOURNAL   Biochem Biophys Res Commun 168 (1), 214-225 (1990)
   PUBMED   2328001
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Arakawa,F., Kuroki,M., Misumi,Y., Matsuo,Y. and Matsuoka,Y.
  TITLE     The nucleotide and deduced amino acid sequences of a cDNA encoding
            a new species of pregnancy-specific beta 1-glycoprotein (PS beta G)
  JOURNAL   Biochim Biophys Acta 1048 (2-3), 303-305 (1990)
   PUBMED   2322584
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Thompson,J., Koumari,R., Wagner,K., Barnert,S., Schleussner,C.,
            Schrewe,H., Zimmermann,W., Muller,G., Schempp,W., Zaninetta,D. et
            al.
  TITLE     The human pregnancy-specific glycoprotein genes are tightly linked
            on the long arm of chromosome 19 and are coordinately expressed
  JOURNAL   Biochem Biophys Res Commun 167 (2), 848-859 (1990)
   PUBMED   1690992
  REMARK    Erratum:[Biochem Biophys Res Commun 1990 May 16;168(3):1325]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC380417.1, M34481.1 and BC005925.1.
            
            On Sep 11, 2014 this sequence version replaced XP_005259134.1.
            
            Summary: The protein encoded by this gene is a member of the
            pregnancy-specific glycoprotein (PSG) family. This protein family
            and the closely related carcinoembryonic antigen cell adhesion
            molecule (CEACAM) gene family are both members of the
            immunoglobulin superfamily, and are organized as a large gene
            cluster. This protein is thought to inhibit platelet-fibrinogen
            interactions. Several studies suggest that reduced serum
            concentrations of PSGs are associated with fetal growth
            restrictions, while up-regulation of this gene has been observed in
            colorectal cancers. Several pseudogenes of this gene are found on
            chromosome 19. Alternative splicing results in multiple transcript
            variants that encode multiple protein isoforms. [provided by
            RefSeq, Sep 2014].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon in the 3' coding region, compared to variant 1. It encodes
            isoform 3 which is shorter than isoform 1. Variants 2 and 3 encode
            isoforms of the same size, but contain internal differences.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC005925.1, DRR138506.38524.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162568 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..333
                     /product="pregnancy-specific beta-1-glycoprotein 9 isoform
                     3 precursor"
                     /note="pregnancy-specific beta-1 glycoprotein B"
                     /calculated_mol_wt=33907
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3697
     Region          36..138
                     /region_name="IgV_CEACAM_D1"
                     /note="First immunoglobulin (Ig)-like domain of
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM); cd05774"
                     /db_xref="CDD:409430"
     Region          37..55
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          37..39
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409430"
     Region          44..46
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409430"
     Region          49..56
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409430"
     Region          56..63
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..69
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..68
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409430"
     Region          70..91
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          78..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          88..91
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..124
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..103
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409430"
     Region          105..109
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409430"
     Region          119..124
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409430"
     Region          125..132
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          133..138
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409430"
     Region          148..236
                     /region_name="IgI_hCEACAM_2_4_6_like"
                     /note="Immunoglobulin (Ig)-like domain of human
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM) domains 2, 4, and 6, and similar
                     domains; cd05740"
                     /db_xref="CDD:409402"
     Region          148..152
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409402"
     Region          155..160
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409402"
     Region          165..171
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409402"
     Region          178..183
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409402"
     Region          185..188
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409402"
     Region          192..196
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409402"
     Region          199..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409402"
     Region          214..222
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409402"
     Region          226..235
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409402"
     Region          245..320
                     /region_name="IgC2_CEACAM5-like"
                     /note="Fifth immunoglobulin (Ig)-like domain of the
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule 5 (CEACAM5) and similar domains; member of the
                     C2-set IgSF domains; cd20948"
                     /db_xref="CDD:409540"
     Region          245..251
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409540"
     Region          256..263
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409540"
     Region          269..275
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409540"
     Region          278..283
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409540"
     Region          286..292
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409540"
     Region          295..306
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409540"
     Region          309..320
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409540"
     CDS             1..333
                     /gene="PSG9"
                     /gene_synonym="PS-beta-B; PS-beta-G-9; PS34; PSBG-9;
                     PSG11; PSGII"
                     /coded_by="NM_001301708.2:100..1101"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS77314.1"
                     /db_xref="GeneID:5678"
                     /db_xref="HGNC:HGNC:9526"
                     /db_xref="MIM:176398"
ORIGIN      
        1 mgplpapsct qritwkglll tasllnfwnp pttaevtiea qppkvsegkd vlllvhnlpq
       61 nlpgyfwykg emtdlyhyii syivdgkiii ygpaysgret vysnaslliq nvtrkdagty
      121 tlhiikrgde treeirhftf tlyletpkpy isssnlnpre ameavrlicd petldasylw
      181 wmngqslpvt hrlqlsktnr tlylfgvtky iagpyeceir npvsasrsdp vtlnllhgpd
      241 lpriypsfty yrsgenldls cftesnppae yfwtingkfq qsgqklfipq itrnhsglya
      301 csvhnsatgk eisksmtvkv sgpchgdlte sqs
//
LOCUS       NP_001340944             565 aa            linear   PRI 20-JAN-2026
DEFINITION  cystathionine beta-synthase isoform b [Homo sapiens].
ACCESSION   NP_001340944 XP_016883702
VERSION     NP_001340944.1
DBSOURCE    REFSEQ: accession NM_001354015.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 565)
  AUTHORS   Kumar,A., Wissbrock,A., Goradia,N., Bellstedt,P., Ramachandran,R.,
            Imhof,D. and Ohlenschlager,O.
  TITLE     Heme interaction of the intrinsically disordered N-terminal peptide
            segment of human cystathionine-beta-synthase
  JOURNAL   Sci Rep 8 (1), 2474 (2018)
   PUBMED   29410458
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 565)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 565)
  AUTHORS   Kabil,O., Zhou,Y. and Banerjee,R.
  TITLE     Human cystathionine beta-synthase is a target for sumoylation
  JOURNAL   Biochemistry 45 (45), 13528-13536 (2006)
   PUBMED   17087506
REFERENCE   7  (residues 1 to 565)
  AUTHORS   Hu,Y.H., Warnatz,H.J., Vanhecke,D., Wagner,F., Fiebitz,A.,
            Thamm,S., Kahlem,P., Lehrach,H., Yaspo,M.L. and Janitz,M.
  TITLE     Cell array-based intracellular localization screening reveals novel
            functional features of human chromosome 21 proteins
  JOURNAL   BMC Genomics 7, 155 (2006)
   PUBMED   16780588
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 565)
  AUTHORS   Chen,X., Jhee,K.H. and Kruger,W.D.
  TITLE     Production of the neuromodulator H2S by cystathionine beta-synthase
            via the condensation of cysteine and homocysteine
  JOURNAL   J Biol Chem 279 (50), 52082-52086 (2004)
   PUBMED   15520012
REFERENCE   9  (residues 1 to 565)
  AUTHORS   Meier,M., Janosik,M., Kery,V., Kraus,J.P. and Burkhard,P.
  TITLE     Structure of human cystathionine beta-synthase: a unique pyridoxal
            5'-phosphate-dependent heme protein
  JOURNAL   EMBO J 20 (15), 3910-3916 (2001)
   PUBMED   11483494
REFERENCE   10 (residues 1 to 565)
  AUTHORS   Kery,V., Bukovska,G. and Kraus,J.P.
  TITLE     Transsulfuration depends on heme in addition to pyridoxal
            5'-phosphate. Cystathionine beta-synthase is a heme protein
  JOURNAL   J Biol Chem 269 (41), 25283-25288 (1994)
   PUBMED   7929220
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FP236240.8.
            
            On Aug 3, 2017 this sequence version replaced XP_016883702.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments. NM_001354015 is annotated on a
            scaffold that is thought to be a false duplication and thus this
            accession is possibly redundant with other RefSeq accessions.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.203160.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21p12"
     Protein         1..565
                     /product="cystathionine beta-synthase isoform b"
                     /EC_number="4.2.1.22"
                     /note="cystathionine beta-synthase-like protein"
                     /calculated_mol_wt=61732
     Region          76..558
                     /region_name="cysta_beta"
                     /note="cystathionine beta-synthase; TIGR01137"
                     /db_xref="CDD:273464"
     CDS             1..565
                     /gene="LOC102724560"
                     /gene_synonym="CBSL"
                     /coded_by="NM_001354015.1:261..1958"
                     /note="isoform b is encoded by transcript variant 9"
                     /db_xref="GeneID:102724560"
ORIGIN      
        1 mpsetpqaev gptgcphrsg phsakgslek gspedkeake plwirpdaps rctwqlgrpa
       61 sesphhhtap akspkilpdi lkkigdtpmv rinkigkkfg lkcellakce ffnaggsvkd
      121 rislrmieda erdgtlkpgd tiieptsgnt giglalaaav rgyrciivmp ekmssekvdv
      181 lralgaeivr tptnarfdsp eshvgvawrl kneipnshil dqyrnasnpl ahydttadei
      241 lqqcdgkldm lvasvgtggt itgiarklke kcpgcriigv dpegsilaep eelnqteqtt
      301 yevegigydf iptvldrtvv dkwfksndee aftfarmlia qegllcggsa gstvavavka
      361 aqelqegqrc vvilpdsvrn ymtkflsdrw mlqkgflkee dltekkpwww hlrvqelgls
      421 apltvlptit cghtieilre kgfdqapvvd eagvilgmvt lgnmlsslla gkvqpsdqvg
      481 kviykqfkqi rltdtlgrls hilemdhfal vvheqiqsqd qawagvvggp adhstgkssq
      541 rqmvfgvvta idllnfvaaq erdqk
//
LOCUS       NP_660286                524 aa            linear   PRI 20-JAN-2026
DEFINITION  metalloendopeptidase OMA1, mitochondrial precursor [Homo sapiens].
ACCESSION   NP_660286
VERSION     NP_660286.1
DBSOURCE    REFSEQ: accession NM_145243.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Wei,Y.Y., Ye,J.J., Zhang,D.W., Hu,L., Wu,H.M. and Fei,G.H.
  TITLE     Melatonin Rescues Influenza A Virus-Induced Cellular Energy
            Exhaustion via OMA1-OPA1-S in Acute Exacerbation of COPD
  JOURNAL   J Pineal Res 76 (5), e12991 (2024)
   PUBMED   39039850
  REMARK    GeneRIF: Melatonin Rescues Influenza A Virus-Induced Cellular
            Energy Exhaustion via OMA1-OPA1-S in Acute Exacerbation of COPD.
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Krakowczyk,M., Lenkiewicz,A.M., Sitarz,T., Malinska,D., Borrero,M.,
            Mussulini,B.H.M., Linke,V., Szczepankiewicz,A.A., Biazik,J.M.,
            Wydrych,A., Nieznanska,H., Serwa,R.A., Chacinska,A. and
            Bragoszewski,P.
  TITLE     OMA1 protease eliminates arrested protein import intermediates upon
            mitochondrial depolarization
  JOURNAL   J Cell Biol 223 (5) (2024)
   PUBMED   38530280
  REMARK    GeneRIF: OMA1 protease eliminates arrested protein import
            intermediates upon mitochondrial depolarization.
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Zhu,W., Rao,J., Zhang,L.H., Xue,K.M., Li,L., Li,J.J., Chen,Q.Z. and
            Fu,R.
  TITLE     OMA1 competitively binds to HSPA9 to promote mitophagy and activate
            the cGAS-STING pathway to mediate GBM immune escape
  JOURNAL   J Immunother Cancer 12 (4), e008718 (2024)
   PUBMED   38604814
  REMARK    GeneRIF: OMA1 competitively binds to HSPA9 to promote mitophagy and
            activate the cGAS-STING pathway to mediate GBM immune escape.
            Erratum:[J Immunother Cancer. 2024 Nov 20;12(11):e008718corr1. doi:
            10.1136/jitc-2023-008718corr1. PMID: 39572161]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Chakrabarty,Y., Yang,Z., Chen,H. and Chan,D.C.
  TITLE     The HRI branch of the integrated stress response selectively
            triggers mitophagy
  JOURNAL   Mol Cell 84 (6), 1090-1100 (2024)
   PUBMED   38340717
REFERENCE   5  (residues 1 to 524)
  AUTHORS   Purohit,G., Ghosh,P. and Khalimonchuk,O.
  TITLE     Mitochondrial metallopeptidase OMA1 in cancer
  JOURNAL   Adv Cancer Res 162, 75-97 (2024)
   PUBMED   39069370
  REMARK    GeneRIF: Mitochondrial metallopeptidase OMA1 in cancer.
            Review article
REFERENCE   6  (residues 1 to 524)
  AUTHORS   Head,B., Griparic,L., Amiri,M., Gandre-Babbe,S. and van der
            Bliek,A.M.
  TITLE     Inducible proteolytic inactivation of OPA1 mediated by the OMA1
            protease in mammalian cells
  JOURNAL   J Cell Biol 187 (7), 959-966 (2009)
   PUBMED   20038677
  REMARK    GeneRIF: OMA1 controls OPA1 cleavage and function.
REFERENCE   7  (residues 1 to 524)
  AUTHORS   Duvezin-Caubet,S., Koppen,M., Wagener,J., Zick,M., Israel,L.,
            Bernacchia,A., Jagasia,R., Rugarli,E.I., Imhof,A., Neupert,W.,
            Langer,T. and Reichert,A.S.
  TITLE     OPA1 processing reconstituted in yeast depends on the subunit
            composition of the m-AAA protease in mitochondria
  JOURNAL   Mol Biol Cell 18 (9), 3582-3590 (2007)
   PUBMED   17615298
  REMARK    GeneRIF: These results provide evidence for different substrate
            specificities of m-AAA proteases composed of different subunits and
            reveal a striking evolutionary switch of proteases involved in the
            proteolytic processing of dynamin-like GTPases in mitochondria.
REFERENCE   8  (residues 1 to 524)
  AUTHORS   Mikami,S., Masutani,M., Sonenberg,N., Yokoyama,S. and Imataka,H.
  TITLE     An efficient mammalian cell-free translation system supplemented
            with translation factors
  JOURNAL   Protein Expr Purif 46 (2), 348-357 (2006)
   PUBMED   16289705
REFERENCE   9  (residues 1 to 524)
  AUTHORS   Kaser,M., Kambacheld,M., Kisters-Woike,B. and Langer,T.
  TITLE     Oma1, a novel membrane-bound metallopeptidase in mitochondria with
            activities overlapping with the m-AAA protease
  JOURNAL   J Biol Chem 278 (47), 46414-46423 (2003)
   PUBMED   12963738
REFERENCE   10 (residues 1 to 524)
  AUTHORS   Bao,Y.C., Tsuruga,H., Hirai,M., Yasuda,K., Yokoi,N., Kitamura,T.
            and Kumagai,H.
  TITLE     Identification of a human cDNA sequence which encodes a novel
            membrane-associated protein containing a zinc metalloprotease motif
  JOURNAL   DNA Res 10 (3), 123-128 (2003)
   PUBMED   12886954
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL365187.19 and AL109845.8.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012915.1, AB048348.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371226.8/ ENSP00000360270.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.2-p32.1"
     Protein         1..524
                     /product="metalloendopeptidase OMA1, mitochondrial
                     precursor"
                     /note="overlapping activity with M-AAA protease;
                     metalloendopeptidase OMA1, mitochondrial;
                     metalloprotease-related protein 1; OMA1 homolog, zinc
                     metallopeptidase; overlapping with the m-AAA protease 1
                     homolog; zinc metallopeptidase OMA1; OMA1 zinc
                     metallopeptidase homolog"
                     /calculated_mol_wt=58741
     transit_peptide 1..13
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q96E52.1)"
                     /calculated_mol_wt=1398
     Region          148..167
                     /region_name="Cardiolipin-binding.
                     /evidence=ECO:0000250|UniProtKB:Q9D8H7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96E52.1)"
     Region          165..195
                     /region_name="Stress-sensor region.
                     /evidence=ECO:0000250|UniProtKB:Q9D8H7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96E52.1)"
     Site            196..216
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96E52.1)"
     Region          263..456
                     /region_name="M48C_Oma1_like"
                     /note="Peptidase M48C, integral membrane endopeptidase;
                     cd07331"
                     /db_xref="CDD:320690"
     Site            order(327..328,331,392,396,439)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:320690"
     Site            order(327,331,392,439)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:320690"
     CDS             1..524
                     /gene="OMA1"
                     /gene_synonym="2010001O09Rik; MPRP-1; MPRP1; peptidase;
                     YKR087C; ZMPOMA1"
                     /coded_by="NM_145243.5:41..1615"
                     /db_xref="CCDS:CCDS608.1"
                     /db_xref="GeneID:115209"
                     /db_xref="HGNC:HGNC:29661"
                     /db_xref="MIM:617081"
ORIGIN      
        1 msficglqsa arnhvffrfn slsnwrkcnt lastsrgchq vqvnhivnky qglgvnqcdr
       61 wsflpgnfhf ystfnnkrtg glsstkskei writskctvw ndafsrqlli kevtavpsls
      121 vlhplspasi rairnfhtsp rfqaapvpll lmilkpvqkl faiivgrgir kwwqalppnk
      181 kevvkenirk nkwklflgls sfgllfvvfy fthlevspit grskllllgk eqfrllsele
      241 yeawmeefkn dmltekdary lavkevlchl iecnkdvpgi sqinwvihvv dspiinafvl
      301 pngqmfvftg flnsvtdihq lsfllgheia havlghaaek agmvhlldfl gmifltmiwa
      361 icprdslall cqwiqsklqe ymfnrpysrk leaeadkigl llaakacadi rassvfwqqm
      421 efvdslhgqp kmpewlsthp shgnrveyld rlipqalkir emcncpplsn pdprllfkls
      481 tkhfleesek edlnitkkqk mdtlpiqkqe qipltyivek rtgs
//
LOCUS       NP_998798                326 aa            linear   PRI 20-JAN-2026
DEFINITION  pregnancy-specific beta-1-glycoprotein 4 isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_998798
VERSION     NP_998798.1
DBSOURCE    REFSEQ: accession NM_213633.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Shanley,D.K., Kiely,P.A., Golla,K., Allen,S., Martin,K.,
            O'Riordan,R.T., Ball,M., Aplin,J.D., Singer,B.B., Caplice,N.,
            Moran,N. and Moore,T.
  TITLE     Pregnancy-specific glycoproteins bind integrin alphaIIbbeta3 and
            inhibit the platelet-fibrinogen interaction
  JOURNAL   PLoS One 8 (2), e57491 (2013)
   PUBMED   23469002
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Kimoto,Y.
  TITLE     A single human cell expresses all messenger ribonucleic acids: the
            arrow of time in a cell
  JOURNAL   Mol Gen Genet 258 (3), 233-239 (1998)
   PUBMED   9645429
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Teglund,S., Olsen,A., Khan,W.N., Frangsmyr,L. and Hammarstrom,S.
  TITLE     The pregnancy-specific glycoprotein (PSG) gene cluster on human
            chromosome 19: fine structure of the 11 PSG genes and
            identification of 6 new genes forming a third subgroup within the
            carcinoembryonic antigen (CEA) family
  JOURNAL   Genomics 23 (3), 669-684 (1994)
   PUBMED   7851896
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Olsen,A., Teglund,S., Nelson,D., Gordon,L., Copeland,A.,
            Georgescu,A., Carrano,A. and Hammarstrom,S.
  TITLE     Gene organization of the pregnancy-specific glycoprotein region on
            human chromosome 19: assembly and analysis of a 700-kb cosmid
            contig spanning the region
  JOURNAL   Genomics 23 (3), 659-668 (1994)
   PUBMED   7851895
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Pan,C.J., Chamberlin,M.E., Wu,S.M., Chan,W.Y. and Chou,J.Y.
  TITLE     Pregnancy-specific glycoprotein gene expression and the induction
            by 5-bromo-2'-deoxyuridine
  JOURNAL   Biochemistry 33 (23), 7260-7266 (1994)
   PUBMED   8003489
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Chan,W.Y., Zheng,Q.X., McMahon,J. and Tease,L.A.
  TITLE     Characterization of new members of the pregnancy-specific beta
            1-glycoprotein family
  JOURNAL   Mol Cell Biochem 106 (2), 161-170 (1991)
   PUBMED   1922019
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Barnett,T.R., Pickle,W. 2nd and Elting,J.J.
  TITLE     Characterization of two new members of the pregnancy-specific beta
            1-glycoprotein family from the myeloid cell line KG-1 and
            suggestion of two distinct classes of transcription unit
  JOURNAL   Biochemistry 29 (44), 10213-10218 (1990)
   PUBMED   2271648
REFERENCE   8  (residues 1 to 326)
  AUTHORS   .
  TITLE     The human pregnancy-specific glycoprotein genes are tightly linked
            on the long arm of chromosome 19 and are coordinately expressed
  JOURNAL   Biochem Biophys Res Commun 168 (3), 1325 (1990)
   PUBMED   2346490
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Thompson,J., Koumari,R., Wagner,K., Barnert,S., Schleussner,C.,
            Schrewe,H., Zimmermann,W., Muller,G., Schempp,W., Zaninetta,D. et
            al.
  TITLE     The human pregnancy-specific glycoprotein genes are tightly linked
            on the long arm of chromosome 19 and are coordinately expressed
  JOURNAL   Biochem Biophys Res Commun 167 (2), 848-859 (1990)
   PUBMED   1690992
  REMARK    Erratum:[Biochem Biophys Res Commun 1990 May 16;168(3):1325]
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Thompson,J.A., Mauch,E.M., Chen,F.S., Hinoda,Y., Schrewe,H.,
            Berling,B., Barnert,S., von Kleist,S., Shively,J.E. and
            Zimmermann,W.
  TITLE     Analysis of the size of the carcinoembryonic antigen (CEA) gene
            family: isolation and sequencing of N-terminal domain exons
  JOURNAL   Biochem Biophys Res Commun 158 (3), 996-1004 (1989)
   PUBMED   2537643
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005392.2, U18469.1 and
            BC008405.1.
            
            Summary: The protein encoded by this gene is a pregnancy-specific
            glycoprotein (PSG), one of several encoded by a cluster of similar
            genes on chromosome 19. This gene is a member of the
            carcinoembryonic antigen (CEA) gene family and may play a role in
            regulation of the innate immune system. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (2) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U18469.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2142853,
                                           SAMEA2149398 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..326
                     /product="pregnancy-specific beta-1-glycoprotein 4 isoform
                     2 precursor"
                     /note="Pregnancy-specific beta-1-glycoprotein-4;
                     PS-beta-G-4; pregnancy-specific glycoprotein 4"
                     /calculated_mol_wt=32612
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3683
     Region          36..138
                     /region_name="IgV_CEACAM_D1"
                     /note="First immunoglobulin (Ig)-like domain of
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM); cd05774"
                     /db_xref="CDD:409430"
     Region          37..55
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          37..39
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409430"
     Region          44..46
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409430"
     Region          49..56
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409430"
     Region          56..63
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..69
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..68
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409430"
     Region          70..91
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          78..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          88..91
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..124
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..103
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409430"
     Region          105..109
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409430"
     Region          119..124
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409430"
     Region          125..132
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          133..138
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409430"
     Region          148..236
                     /region_name="IgI_hCEACAM_2_4_6_like"
                     /note="Immunoglobulin (Ig)-like domain of human
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM) domains 2, 4, and 6, and similar
                     domains; cd05740"
                     /db_xref="CDD:409402"
     Region          148..152
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409402"
     Region          155..160
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409402"
     Region          165..171
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409402"
     Region          178..183
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409402"
     Region          185..188
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409402"
     Region          192..196
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409402"
     Region          199..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409402"
     Region          214..222
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409402"
     Region          226..235
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409402"
     Region          245..320
                     /region_name="IgC2_CEACAM5-like"
                     /note="Fifth immunoglobulin (Ig)-like domain of the
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule 5 (CEACAM5) and similar domains; member of the
                     C2-set IgSF domains; cd20948"
                     /db_xref="CDD:409540"
     Region          245..251
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409540"
     Region          256..263
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409540"
     Region          269..275
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409540"
     Region          278..283
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409540"
     Region          286..292
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409540"
     Region          295..306
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409540"
     Region          309..320
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409540"
     CDS             1..326
                     /gene="PSG4"
                     /gene_synonym="PSBG-4"
                     /coded_by="NM_213633.3:103..1083"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS33039.1"
                     /db_xref="GeneID:5672"
                     /db_xref="HGNC:HGNC:9521"
                     /db_xref="MIM:176393"
ORIGIN      
        1 mgplsappct qritwkgvll tasllnfwnp pttaqvtiea qppkvsegkd vlllvhnlpq
       61 nlagyiwykg qmtylyhyit syvvdgqrii ygpaysgrer vysnaslliq nvtqedagsy
      121 tlhiikrrdg tggvtghftf tlhletpkps isssnlnpre ameaviltcd patpaasyqw
      181 wmngqslpmt hrlqlsktnr tlfifgvtky iagpyeceir npvsasrsdp vtlnllhgpd
      241 lpsiypsfty yrsgenlyls cfaesnpraq yswtingkfq lsgqklsipq ittkhsglya
      301 csvrnsatgk essksitvkv sdwilp
//
LOCUS       NP_066957                153 aa            linear   PRI 20-JAN-2026
DEFINITION  large ribosomal subunit protein uL23m isoform 1 [Homo sapiens].
ACCESSION   NP_066957
VERSION     NP_066957.3
DBSOURCE    REFSEQ: accession NM_021134.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   6  (residues 1 to 153)
  AUTHORS   Zhang,Z. and Gerstein,M.
  TITLE     Identification and characterization of over 100 mitochondrial
            ribosomal protein pseudogenes in the human genome
  JOURNAL   Genomics 81 (5), 468-480 (2003)
   PUBMED   12706105
REFERENCE   7  (residues 1 to 153)
  AUTHORS   O'Brien,T.W.
  TITLE     Evolution of a protein-rich mitochondrial ribosome: implications
            for human genetic disease
  JOURNAL   Gene 286 (1), 73-79 (2002)
   PUBMED   11943462
REFERENCE   8  (residues 1 to 153)
  AUTHORS   Kenmochi,N., Suzuki,T., Uechi,T., Magoori,M., Kuniba,M., Higa,S.,
            Watanabe,K. and Tanaka,T.
  TITLE     The human mitochondrial ribosomal protein genes: mapping of 54
            genes to the chromosomes and implications for human disorders
  JOURNAL   Genomics 77 (1-2), 65-70 (2001)
   PUBMED   11543634
REFERENCE   9  (residues 1 to 153)
  AUTHORS   Suzuki,T., Terasaki,M., Takemoto-Hori,C., Hanada,T., Ueda,T.,
            Wada,A. and Watanabe,K.
  TITLE     Structural compensation for the deficit of rRNA with proteins in
            the mammalian mitochondrial ribosome. Systematic analysis of
            protein components of the large ribosomal subunit from mammalian
            mitochondria
  JOURNAL   J Biol Chem 276 (24), 21724-21736 (2001)
   PUBMED   11279069
REFERENCE   10 (residues 1 to 153)
  AUTHORS   Tsang,P., Gilles,F., Yuan,L., Kuo,Y.H., Lupu,F., Samara,G.,
            Moosikasuwan,J., Goye,A., Zelenetz,A.D., Selleri,L. et al.
  TITLE     A novel L23-related gene 40 kb downstream of the imprinted H19 gene
            is biallelically expressed in mid-fetal and adult human tissues
  JOURNAL   Hum Mol Genet 4 (9), 1499-1507 (1995)
   PUBMED   8541832
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN310387.1 and BC027710.2.
            
            On Feb 12, 2009 this sequence version replaced NP_066957.2.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 39S subunit protein. The gene is
            biallelically expressed, despite its location within a region of
            imprinted genes on chromosome 11. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD248886.1, U26596.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000397298.8/
                                                  ENSP00000380466.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..153
                     /product="large ribosomal subunit protein uL23m isoform 1"
                     /note="L23 mitochondrial-related protein; ribosomal
                     protein related to L23 (mitochondrial); 39S ribosomal
                     protein L23, mitochondrial; mitochondrial large ribosomal
                     subunit protein uL23m"
                     /calculated_mol_wt=17650
     Region          <42..105
                     /region_name="Ribosomal_L23"
                     /note="Ribosomal protein L23; pfam00276"
                     /db_xref="CDD:459743"
     Region          108..153
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16540.1)"
     CDS             1..153
                     /gene="MRPL23"
                     /gene_synonym="L23MRP; L23mt; MRP-L23; RPL23L; uL23m"
                     /coded_by="NM_021134.4:32..493"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31336.1"
                     /db_xref="GeneID:6150"
                     /db_xref="HGNC:HGNC:10322"
                     /db_xref="MIM:600789"
ORIGIN      
        1 marnvvyply rlggpqlrvf rtnffiqlvr pgvaqpedtv qfripmemtr vdlrnylegi
       61 ynvpvaavrt rvqhgsnkrr dhrnvrikkp dykvayvqla hgqtftfpdl fpekdespeg
      121 saaddlysml eeerqqrqss dprrggvpsw fgl
//
LOCUS       NP_001623                535 aa            linear   PRI 20-JAN-2026
DEFINITION  alkaline phosphatase, placental type preproprotein [Homo sapiens].
ACCESSION   NP_001623
VERSION     NP_001623.3
DBSOURCE    REFSEQ: accession NM_001632.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Wu,G., Li,S., Luo,M., Li,X., Zhu,X., Zhang,J., He,Q., Yang,Q.,
            Zhao,G., Luo,S. and Yang,Z.
  TITLE     Role of serum alkaline phosphatase as a potential biomarker of
            severity and prognosis in intracerebral hemorrhage
  JOURNAL   J Stroke Cerebrovasc Dis 33 (1), 107478 (2024)
   PUBMED   37952310
  REMARK    GeneRIF: Role of serum alkaline phosphatase as a potential
            biomarker of severity and prognosis in intracerebral hemorrhage.
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Lung,B.E., Kim,M., McLellan,M., Callan,K., Wang,E.D., McMaster,W.,
            Yang,S. and So,D.H.
  TITLE     Alkaline Phosphatase is an Independent Risk Factor for
            Periprosthetic Fractures in Total Joint Arthroplasty
  JOURNAL   J Am Acad Orthop Surg Glob Res Rev 7 (2) (2023)
   PUBMED   36763725
  REMARK    GeneRIF: Alkaline Phosphatase is an Independent Risk Factor for
            Periprosthetic Fractures in Total Joint Arthroplasty.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Cui,X.A., Zhang,Y., Hong,S.J. and Palazzo,A.F.
  TITLE     Identification of a region within the placental alkaline
            phosphatase mRNA that mediates p180-dependent targeting to the
            endoplasmic reticulum
  JOURNAL   J Biol Chem 288 (41), 29633-29641 (2013)
   PUBMED   24019514
  REMARK    GeneRIF: Data indicate that p180 is required for the efficient
            targeting of placental alkaline phosphatase (ALPP) mRNA to the
            endoplasmic reticulum (ER).
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Bellazi,L., Germond,S., Dupont,C., Brun-Heath,I., Taillandier,A.,
            De Mazancourt,P., Dieudonne,M.N. and Mornet,E.
  TITLE     A sequence variation in the promoter of the placental alkaline
            phosphatase gene (ALPP) is associated with allele-specific
            expression in human term placenta
  JOURNAL   Placenta 31 (9), 764-769 (2010)
   PUBMED   20663553
  REMARK    GeneRIF: differential expression of Pl(1) and Pl(2) probably
            results from linkage disequilibrium with the sequence variation
            rs2014683G>A in the ALPP gene promoter that was shown to have
            allele-specific binding patterns to placental nuclear proteins.
REFERENCE   5  (residues 1 to 535)
  AUTHORS   Stec,B., Cheltsov,A. and Millan,J.L.
  TITLE     Refined structures of placental alkaline phosphatase show a
            consistent pattern of interactions at the peripheral site
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (Pt 8), 866-870
            (2010)
   PUBMED   20693656
  REMARK    GeneRIF: structure of placental alkaline phosphatase with pNPP
            contained only p-nitrophenol in three distinct sites, while the
            structure with 5'-AMP contained the p-nitrophenyl group in two of
            the sites instead of 5'-AMP
REFERENCE   6  (residues 1 to 535)
  AUTHORS   Lowe,M.E.
  TITLE     Site-specific mutations in the COOH-terminus of placental alkaline
            phosphatase: a single amino acid change converts a
            phosphatidylinositol-glycan-anchored protein to a secreted protein
  JOURNAL   J Cell Biol 116 (3), 799-807 (1992)
   PUBMED   1730777
REFERENCE   7  (residues 1 to 535)
  AUTHORS   Knoll,B.J., Rothblum,K.N. and Longley,M.
  TITLE     Nucleotide sequence of the human placental alkaline phosphatase
            gene. Evolution of the 5' flanking region by deletion/substitution
  JOURNAL   J Biol Chem 263 (24), 12020-12027 (1988)
   PUBMED   3042787
  REMARK    Erratum:[J Biol Chem 1989 Feb 5;264(4):2391]
REFERENCE   8  (residues 1 to 535)
  AUTHORS   Kam,W., Clauser,E., Kim,Y.S., Kan,Y.W. and Rutter,W.J.
  TITLE     Cloning, sequencing, and chromosomal localization of human term
            placental alkaline phosphatase cDNA
  JOURNAL   Proc Natl Acad Sci U S A 82 (24), 8715-8719 (1985)
   PUBMED   3001717
REFERENCE   9  (residues 1 to 535)
  AUTHORS   Ezra,E., Blacher,R. and Udenfriend,S.
  TITLE     Purification and partial sequencing of human placental alkaline
            phosphatase
  JOURNAL   Biochem Biophys Res Commun 116 (3), 1076-1083 (1983)
   PUBMED   6651840
REFERENCE   10 (residues 1 to 535)
  AUTHORS   Palmarino,R., Corbo,R.M., Scacchi,R. and Lucarelli,P.
  TITLE     Human placental alkaline phosphatase: analysis of genetically
            determined rare variants
  JOURNAL   Hum Biol 51 (3), 341-352 (1979)
   PUBMED   533715
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC094743.1, BC009647.1 and
            AF217992.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 5, 2006 this sequence version replaced NP_001623.2.
            
            Summary: The protein encoded by this gene is an alkaline
            phosphatase, a metalloenzyme that catalyzes the hydrolysis of
            phosphoric acid monoesters. It belongs to a multigene family
            composed of four alkaline phosphatase isoenzymes. The enzyme
            functions as a homodimer and has a catalytic site containing one
            magnesium and two zinc ions, which are required for its enzymatic
            function. One of the main sources of this enzyme is the liver, and
            thus, it's one of several indicators of liver injury in different
            clinical conditions. In pregnant women, this protein is primarily
            expressed in placental and endometrial tissue, however, strong
            ectopic expression has been detected in ovarian adenocarcinoma,
            serous cystadenocarcinoma, and other ovarian cancer cells.
            [provided by RefSeq, Aug 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC068501.1, BC094743.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2149398
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            coronavirus related              :: relevant for disease process
            MANE Ensembl match               :: ENST00000392027.3/
                                                ENSP00000375881.2
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..535
                     /product="alkaline phosphatase, placental type
                     preproprotein"
                     /EC_number="3.1.3.1"
                     /note="alkaline phosphomonoesterase; glycerophosphatase;
                     alkaline phosphatase, placental type; placental alkaline
                     phosphatase 1; alkaline phosphatase Regan isozyme"
                     /calculated_mol_wt=55591
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2381
     proprotein      23..535
                     /product="alkaline phosphatase, placental type proprotein"
                     /calculated_mol_wt=55591
     mat_peptide     23..506
                     /product="Alkaline phosphatase, placental type.
                     /id=PRO_0000024031"
                     /note="propagated from UniProtKB/Swiss-Prot (P05187.2)"
                     /calculated_mol_wt=52746
     Region          55..490
                     /region_name="Alk_phosphatase"
                     /note="Alkaline phosphatase; pfam00245"
                     /db_xref="CDD:395188"
     Site            order(64,113..114,177,188,333,338,342,379..380,454)
                     /site_type="active"
                     /db_xref="CDD:293736"
     Site            order(64,113..114,188,338,342,380,454)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:293736"
     Site            order(68..69,72,75..76,99..101,103,105,107,111,124..126,
                     136,151,453,455..458,460,470,472..476,478..479,482)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:293736"
     Site            144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15946677,
                     ECO:0000269|PubMed:16815919, ECO:0000269|PubMed:20693656;
                     propagated from UniProtKB/Swiss-Prot (P05187.2)"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15946677,
                     ECO:0000269|PubMed:16815919, ECO:0000269|PubMed:20693656;
                     propagated from UniProtKB/Swiss-Prot (P05187.2)"
     Region          425..449
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05187.2)"
     Site            513..529
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05187.2)"
     CDS             1..535
                     /gene="ALPP"
                     /gene_synonym="ALP; PALP; PLAP; PLAP-1"
                     /coded_by="NM_001632.5:53..1660"
                     /db_xref="CCDS:CCDS2490.1"
                     /db_xref="GeneID:250"
                     /db_xref="HGNC:HGNC:439"
                     /db_xref="MIM:171800"
ORIGIN      
        1 mlgpcmllll lllglrlqls lgiipveeen pdfwnreaae algaakklqp aqtaaknlii
       61 flgdgmgvst vtaarilkgq kkdklgpeip lamdrfpyva lsktynvdkh vpdsgatata
      121 ylcgvkgnfq tiglsaaarf nqcnttrgne visvmnrakk agksvgvvtt trvqhaspag
      181 tyahtvnrnw ysdadvpasa rqegcqdiat qlisnmdidv ilgggrkymf rmgtpdpeyp
      241 ddysqggtrl dgknlvqewl akrqgaryvw nrtelmqasl dpsvthlmgl fepgdmkyei
      301 hrdstldpsl memteaalrl lsrnprgffl fveggridhg hhesrayral tetimfddai
      361 eragqltsee dtlslvtadh shvfsfggyp lrgssifgla pgkardrkay tvllygngpg
      421 yvlkdgarpd vtesesgspe yrqqsavpld eethagedva vfargpqahl vhgvqeqtfi
      481 ahvmafaacl epytacdlap pagttdaahp grsvvpallp llagtlllle tatap
//
LOCUS       NP_001384291             188 aa            linear   PRI 20-JAN-2026
DEFINITION  protein CRIPTO3 precursor [Homo sapiens].
ACCESSION   NP_001384291
VERSION     NP_001384291.1
DBSOURCE    REFSEQ: accession NM_001397362.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Ni,Q., An,M., Luo,S., Li,X., He,G., Shen,M., Xu,L., Huang,J.,
            Yan,M., Fan,Y. and Gao,Z.
  TITLE     Pseudogene TDGF1P3 regulates the proliferation and metastasis of
            colorectal cancer cells via the miR-338-3p-PKM2 axis
  JOURNAL   Biochem Biophys Res Commun 638, 7-13 (2023)
   PUBMED   36436343
  REMARK    GeneRIF: Pseudogene TDGF1P3 regulates the proliferation and
            metastasis of colorectal cancer cells via the miR-338-3p-PKM2 axis.
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Sun,C., Orozco,O., Olson,D.L., Choi,E., Garber,E., Tizard,R.,
            Szak,S., Sanicola,M. and Carulli,J.P.
  TITLE     CRIPTO3, a presumed pseudogene, is expressed in cancer
  JOURNAL   Biochem Biophys Res Commun 377 (1), 215-220 (2008)
   PUBMED   18835250
  REMARK    GeneRIF: These data indicate that CRIPTO3 is an expressed gene,
            particularly in certain cancers, and suggest a potentially novel
            mechanism of oncogenesis through activation of a retrogene.
REFERENCE   3  (residues 1 to 188)
  AUTHORS   Hentschke,M., Kurth,I., Borgmeyer,U. and Hubner,C.A.
  TITLE     Germ cell nuclear factor is a repressor of CRIPTO-1 and CRIPTO-3
  JOURNAL   J Biol Chem 281 (44), 33497-33504 (2006)
   PUBMED   16954206
  REMARK    GeneRIF: CRIPTO-3, a processed pseudogene of CRIPTO-1 on the X
            chromosome, is expressed in undifferentiated NT2 cells and is
            regulated by germ cell nuclear factor in parallel to CRIPTO-1
REFERENCE   4  (residues 1 to 188)
  AUTHORS   Ross,M.T., Grafham,D.V., Coffey,A.J., Scherer,S., McLay,K.,
            Muzny,D., Platzer,M., Howell,G.R., Burrows,C., Bird,C.P.,
            Frankish,A., Lovell,F.L., Howe,K.L., Ashurst,J.L., Fulton,R.S.,
            Sudbrak,R., Wen,G., Jones,M.C., Hurles,M.E., Andrews,T.D.,
            Scott,C.E., Searle,S., Ramser,J., Whittaker,A., Deadman,R.,
            Carter,N.P., Hunt,S.E., Chen,R., Cree,A., Gunaratne,P., Havlak,P.,
            Hodgson,A., Metzker,M.L., Richards,S., Scott,G., Steffen,D.,
            Sodergren,E., Wheeler,D.A., Worley,K.C., Ainscough,R.,
            Ambrose,K.D., Ansari-Lari,M.A., Aradhya,S., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Ballabio,A., Banerjee,R., Barker,G.E.,
            Barlow,K.F., Barrett,I.P., Bates,K.N., Beare,D.M., Beasley,H.,
            Beasley,O., Beck,A., Bethel,G., Blechschmidt,K., Brady,N.,
            Bray-Allen,S., Bridgeman,A.M., Brown,A.J., Brown,M.J., Bonnin,D.,
            Bruford,E.A., Buhay,C., Burch,P., Burford,D., Burgess,J.,
            Burrill,W., Burton,J., Bye,J.M., Carder,C., Carrel,L., Chako,J.,
            Chapman,J.C., Chavez,D., Chen,E., Chen,G., Chen,Y., Chen,Z.,
            Chinault,C., Ciccodicola,A., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S., Clerc-Blankenburg,K., Clifford,K., Cobley,V., Cole,C.G.,
            Conquer,J.S., Corby,N., Connor,R.E., David,R., Davies,J., Davis,C.,
            Davis,J., Delgado,O., Deshazo,D., Dhami,P., Ding,Y., Dinh,H.,
            Dodsworth,S., Draper,H., Dugan-Rocha,S., Dunham,A., Dunn,M.,
            Durbin,K.J., Dutta,I., Eades,T., Ellwood,M., Emery-Cohen,A.,
            Errington,H., Evans,K.L., Faulkner,L., Francis,F., Frankland,J.,
            Fraser,A.E., Galgoczy,P., Gilbert,J., Gill,R., Glockner,G.,
            Gregory,S.G., Gribble,S., Griffiths,C., Grocock,R., Gu,Y.,
            Gwilliam,R., Hamilton,C., Hart,E.A., Hawes,A., Heath,P.D.,
            Heitmann,K., Hennig,S., Hernandez,J., Hinzmann,B., Ho,S., Hoffs,M.,
            Howden,P.J., Huckle,E.J., Hume,J., Hunt,P.J., Hunt,A.R.,
            Isherwood,J., Jacob,L., Johnson,D., Jones,S., de Jong,P.J.,
            Joseph,S.S., Keenan,S., Kelly,S., Kershaw,J.K., Khan,Z.,
            Kioschis,P., Klages,S., Knights,A.J., Kosiura,A., Kovar-Smith,C.,
            Laird,G.K., Langford,C., Lawlor,S., Leversha,M., Lewis,L., Liu,W.,
            Lloyd,C., Lloyd,D.M., Loulseged,H., Loveland,J.E., Lovell,J.D.,
            Lozado,R., Lu,J., Lyne,R., Ma,J., Maheshwari,M., Matthews,L.H.,
            McDowall,J., McLaren,S., McMurray,A., Meidl,P., Meitinger,T.,
            Milne,S., Miner,G., Mistry,S.L., Morgan,M., Morris,S., Muller,I.,
            Mullikin,J.C., Nguyen,N., Nordsiek,G., Nyakatura,G., O'Dell,C.N.,
            Okwuonu,G., Palmer,S., Pandian,R., Parker,D., Parrish,J.,
            Pasternak,S., Patel,D., Pearce,A.V., Pearson,D.M., Pelan,S.E.,
            Perez,L., Porter,K.M., Ramsey,Y., Reichwald,K., Rhodes,S.,
            Ridler,K.A., Schlessinger,D., Schueler,M.G., Sehra,H.K.,
            Shaw-Smith,C., Shen,H., Sheridan,E.M., Shownkeen,R., Skuce,C.D.,
            Smith,M.L., Sotheran,E.C., Steingruber,H.E., Steward,C.A.,
            Storey,R., Swann,R.M., Swarbreck,D., Tabor,P.E., Taudien,S.,
            Taylor,T., Teague,B., Thomas,K., Thorpe,A., Timms,K., Tracey,A.,
            Trevanion,S., Tromans,A.C., d'Urso,M., Verduzco,D., Villasana,D.,
            Waldron,L., Wall,M., Wang,Q., Warren,J., Warry,G.L., Wei,X.,
            West,A., Whitehead,S.L., Whiteley,M.N., Wilkinson,J.E.,
            Willey,D.L., Williams,G., Williams,L., Williamson,A.,
            Williamson,H., Wilming,L., Woodmansey,R.L., Wray,P.W., Yen,J.,
            Zhang,J., Zhou,J., Zoghbi,H., Zorilla,S., Buck,D., Reinhardt,R.,
            Poustka,A., Rosenthal,A., Lehrach,H., Meindl,A., Minx,P.J.,
            Hillier,L.W., Willard,H.F., Wilson,R.K., Waterston,R.H., Rice,C.M.,
            Vaudin,M., Coulson,A., Nelson,D.L., Weinstock,G., Sulston,J.E.,
            Durbin,R., Hubbard,T., Gibbs,R.A., Beck,S., Rogers,J. and
            Bentley,D.R.
  TITLE     The DNA sequence of the human X chromosome
  JOURNAL   Nature 434 (7031), 325-337 (2005)
   PUBMED   15772651
REFERENCE   5  (residues 1 to 188)
  AUTHORS   Scognamiglio,B., Baldassarre,G., Cassano,C., Tucci,M., Montuori,N.,
            Dono,R., Lembo,G., Barra,A., Lago,C.T., Viglietto,G., Rocchi,M. and
            Persico,M.G.
  TITLE     Assignment of human teratocarcinoma derived growth factor (TDGF)
            sequences to chromosomes 2q37, 3q22, 6p25 and 19q13.1
  JOURNAL   Cytogenet Cell Genet 84 (3-4), 220-224 (1999)
   PUBMED   10393436
REFERENCE   6  (residues 1 to 188)
  AUTHORS   Dono,R., Montuori,N., Rocchi,M., De Ponti-Zilli,L., Ciccodicola,A.
            and Persico,M.G.
  TITLE     Isolation and characterization of the CRIPTO autosomal gene and its
            X-linked related sequence
  JOURNAL   Am J Hum Genet 49 (3), 555-565 (1991)
   PUBMED   1882841
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC000113.1.
            
            Summary: The TDGF3 locus has characteristics of a retrotransposon,
            including lack of introns and a poly(A) sequence. [provided by
            RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript is intronless :: M96956.1, BI598827.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000602699.2/ ENSP00000507999.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq23"
     Protein         1..188
                     /product="protein CRIPTO3 precursor"
                     /note="Teratocarcinoma-derived growth factor-2;
                     teratocarcinoma-derived growth factor 2 (retroposin,
                     possibly expressed); cripto-3 growth factor; epidermal
                     growth factor-like cripto protein CR3; putative
                     teratocarcinoma-derived growth factor 3; putative protein
                     CRIPTO3"
                     /calculated_mol_wt=17776
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3423
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51864.1)"
     Region          115..149
                     /region_name="CFC"
                     /note="Cripto_Frl-1_Cryptic (CFC); pfam09443"
                     /db_xref="CDD:462800"
     CDS             1..188
                     /gene="CRIPTO3"
                     /gene_synonym="CR-3; CRIPTO-3; TDGF1; TDGF1P3; TDGF2;
                     TDGF3"
                     /coded_by="NM_001397362.1:235..801"
                     /db_xref="CCDS:CCDS94651.1"
                     /db_xref="GeneID:6998"
                     /db_xref="HGNC:HGNC:11703"
ORIGIN      
        1 mdcrkmvrfs ysviwimais kafelglvag lghqefarps rgdlafrdds iwpqeepair
       61 prssqrvlpm giqhskelnr tcclnggtcm lesfcacpps fygrncehdv rkencgsvph
      121 dtwlpkkcsl ckcwhgqlrc fpqaflpgcd glvmdehlva srtpelppsa rtttfmlagi
      181 clsiqsyy
//
LOCUS       NP_001387103             123 aa            linear   PRI 20-JAN-2026
DEFINITION  large ribosomal subunit protein uL23m isoform 3 [Homo sapiens].
ACCESSION   NP_001387103
VERSION     NP_001387103.1
DBSOURCE    REFSEQ: accession NM_001400174.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   5  (residues 1 to 123)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   6  (residues 1 to 123)
  AUTHORS   Zhang,Z. and Gerstein,M.
  TITLE     Identification and characterization of over 100 mitochondrial
            ribosomal protein pseudogenes in the human genome
  JOURNAL   Genomics 81 (5), 468-480 (2003)
   PUBMED   12706105
REFERENCE   7  (residues 1 to 123)
  AUTHORS   O'Brien,T.W.
  TITLE     Evolution of a protein-rich mitochondrial ribosome: implications
            for human genetic disease
  JOURNAL   Gene 286 (1), 73-79 (2002)
   PUBMED   11943462
REFERENCE   8  (residues 1 to 123)
  AUTHORS   Kenmochi,N., Suzuki,T., Uechi,T., Magoori,M., Kuniba,M., Higa,S.,
            Watanabe,K. and Tanaka,T.
  TITLE     The human mitochondrial ribosomal protein genes: mapping of 54
            genes to the chromosomes and implications for human disorders
  JOURNAL   Genomics 77 (1-2), 65-70 (2001)
   PUBMED   11543634
REFERENCE   9  (residues 1 to 123)
  AUTHORS   Suzuki,T., Terasaki,M., Takemoto-Hori,C., Hanada,T., Ueda,T.,
            Wada,A. and Watanabe,K.
  TITLE     Structural compensation for the deficit of rRNA with proteins in
            the mammalian mitochondrial ribosome. Systematic analysis of
            protein components of the large ribosomal subunit from mammalian
            mitochondria
  JOURNAL   J Biol Chem 276 (24), 21724-21736 (2001)
   PUBMED   11279069
REFERENCE   10 (residues 1 to 123)
  AUTHORS   Tsang,P., Gilles,F., Yuan,L., Kuo,Y.H., Lupu,F., Samara,G.,
            Moosikasuwan,J., Goye,A., Zelenetz,A.D., Selleri,L. et al.
  TITLE     A novel L23-related gene 40 kb downstream of the imprinted H19 gene
            is biallelically expressed in mid-fetal and adult human tissues
  JOURNAL   Hum Mol Genet 4 (9), 1499-1507 (1995)
   PUBMED   8541832
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC051649.21.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 39S subunit protein. The gene is
            biallelically expressed, despite its location within a region of
            imprinted genes on chromosome 11. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2145245 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..123
                     /product="large ribosomal subunit protein uL23m isoform 3"
                     /note="L23 mitochondrial-related protein; ribosomal
                     protein related to L23 (mitochondrial); 39S ribosomal
                     protein L23, mitochondrial; mitochondrial large ribosomal
                     subunit protein uL23m"
                     /calculated_mol_wt=14209
     Region          <42..103
                     /region_name="Ribosomal_L23"
                     /note="Ribosomal protein L23; pfam00276"
                     /db_xref="CDD:459743"
     CDS             1..123
                     /gene="MRPL23"
                     /gene_synonym="L23MRP; L23mt; MRP-L23; RPL23L; uL23m"
                     /coded_by="NM_001400174.1:32..403"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:6150"
                     /db_xref="HGNC:HGNC:10322"
                     /db_xref="MIM:600789"
ORIGIN      
        1 marnvvyply rlggpqlrvf rtnffiqlvr pgvaqpedtv qfripmemtr vdlrnylegi
       61 ynvpvaavrt rvqhgsnkrr dhrnvrikkp dykvayvqlv pkeqyplllv npshmlwpgl
      121 glg
//
LOCUS       NP_001387111             163 aa            linear   PRI 20-JAN-2026
DEFINITION  large ribosomal subunit protein uL23m isoform 6 [Homo sapiens].
ACCESSION   NP_001387111
VERSION     NP_001387111.1
DBSOURCE    REFSEQ: accession NM_001400182.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   5  (residues 1 to 163)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   6  (residues 1 to 163)
  AUTHORS   Zhang,Z. and Gerstein,M.
  TITLE     Identification and characterization of over 100 mitochondrial
            ribosomal protein pseudogenes in the human genome
  JOURNAL   Genomics 81 (5), 468-480 (2003)
   PUBMED   12706105
REFERENCE   7  (residues 1 to 163)
  AUTHORS   O'Brien,T.W.
  TITLE     Evolution of a protein-rich mitochondrial ribosome: implications
            for human genetic disease
  JOURNAL   Gene 286 (1), 73-79 (2002)
   PUBMED   11943462
REFERENCE   8  (residues 1 to 163)
  AUTHORS   Kenmochi,N., Suzuki,T., Uechi,T., Magoori,M., Kuniba,M., Higa,S.,
            Watanabe,K. and Tanaka,T.
  TITLE     The human mitochondrial ribosomal protein genes: mapping of 54
            genes to the chromosomes and implications for human disorders
  JOURNAL   Genomics 77 (1-2), 65-70 (2001)
   PUBMED   11543634
REFERENCE   9  (residues 1 to 163)
  AUTHORS   Suzuki,T., Terasaki,M., Takemoto-Hori,C., Hanada,T., Ueda,T.,
            Wada,A. and Watanabe,K.
  TITLE     Structural compensation for the deficit of rRNA with proteins in
            the mammalian mitochondrial ribosome. Systematic analysis of
            protein components of the large ribosomal subunit from mammalian
            mitochondria
  JOURNAL   J Biol Chem 276 (24), 21724-21736 (2001)
   PUBMED   11279069
REFERENCE   10 (residues 1 to 163)
  AUTHORS   Tsang,P., Gilles,F., Yuan,L., Kuo,Y.H., Lupu,F., Samara,G.,
            Moosikasuwan,J., Goye,A., Zelenetz,A.D., Selleri,L. et al.
  TITLE     A novel L23-related gene 40 kb downstream of the imprinted H19 gene
            is biallelically expressed in mid-fetal and adult human tissues
  JOURNAL   Hum Mol Genet 4 (9), 1499-1507 (1995)
   PUBMED   8541832
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC051649.21.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 39S subunit protein. The gene is
            biallelically expressed, despite its location within a region of
            imprinted genes on chromosome 11. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD675974.1, SRR14038197.815916.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245, SAMEA2149178
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..163
                     /product="large ribosomal subunit protein uL23m isoform 6"
                     /note="L23 mitochondrial-related protein; ribosomal
                     protein related to L23 (mitochondrial); 39S ribosomal
                     protein L23, mitochondrial; mitochondrial large ribosomal
                     subunit protein uL23m"
                     /calculated_mol_wt=18399
     Region          <42..101
                     /region_name="Ribosomal_L23"
                     /note="Ribosomal protein L23; pfam00276"
                     /db_xref="CDD:459743"
     CDS             1..163
                     /gene="MRPL23"
                     /gene_synonym="L23MRP; L23mt; MRP-L23; RPL23L; uL23m"
                     /coded_by="NM_001400182.1:32..523"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS91407.1"
                     /db_xref="GeneID:6150"
                     /db_xref="HGNC:HGNC:10322"
                     /db_xref="MIM:600789"
ORIGIN      
        1 marnvvyply rlggpqlrvf rtnffiqlvr pgvaqpedtv qfripmemtr vdlrnylegi
       61 ynvpvaavrt rvqhgsnkrr dhrnvrikkp dykvayvqlv phprslplcl qhrsqlrtpr
      121 ipcivafasw gpgskhdacs alcvvarawa avyvsarlis vag
//
LOCUS       NP_001340939             551 aa            linear   PRI 20-JAN-2026
DEFINITION  cystathionine beta-synthase isoform a [Homo sapiens].
ACCESSION   NP_001340939 XP_016883706
VERSION     NP_001340939.1
DBSOURCE    REFSEQ: accession NM_001354010.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Kumar,A., Wissbrock,A., Goradia,N., Bellstedt,P., Ramachandran,R.,
            Imhof,D. and Ohlenschlager,O.
  TITLE     Heme interaction of the intrinsically disordered N-terminal peptide
            segment of human cystathionine-beta-synthase
  JOURNAL   Sci Rep 8 (1), 2474 (2018)
   PUBMED   29410458
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Kabil,O., Zhou,Y. and Banerjee,R.
  TITLE     Human cystathionine beta-synthase is a target for sumoylation
  JOURNAL   Biochemistry 45 (45), 13528-13536 (2006)
   PUBMED   17087506
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Hu,Y.H., Warnatz,H.J., Vanhecke,D., Wagner,F., Fiebitz,A.,
            Thamm,S., Kahlem,P., Lehrach,H., Yaspo,M.L. and Janitz,M.
  TITLE     Cell array-based intracellular localization screening reveals novel
            functional features of human chromosome 21 proteins
  JOURNAL   BMC Genomics 7, 155 (2006)
   PUBMED   16780588
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Chen,X., Jhee,K.H. and Kruger,W.D.
  TITLE     Production of the neuromodulator H2S by cystathionine beta-synthase
            via the condensation of cysteine and homocysteine
  JOURNAL   J Biol Chem 279 (50), 52082-52086 (2004)
   PUBMED   15520012
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Meier,M., Janosik,M., Kery,V., Kraus,J.P. and Burkhard,P.
  TITLE     Structure of human cystathionine beta-synthase: a unique pyridoxal
            5'-phosphate-dependent heme protein
  JOURNAL   EMBO J 20 (15), 3910-3916 (2001)
   PUBMED   11483494
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Kery,V., Bukovska,G. and Kraus,J.P.
  TITLE     Transsulfuration depends on heme in addition to pyridoxal
            5'-phosphate. Cystathionine beta-synthase is a heme protein
  JOURNAL   J Biol Chem 269 (41), 25283-25288 (1994)
   PUBMED   7929220
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FP236240.8.
            
            On Aug 3, 2017 this sequence version replaced XP_016883706.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.NM_001354010 is annotated on a
            scaffold that is thought to be a false duplication and thus this
            accession is possibly redundant with other RefSeq accessions.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.77088.1,
                                           SRR1660803.161076.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21p12"
     Protein         1..551
                     /product="cystathionine beta-synthase isoform a"
                     /EC_number="4.2.1.22"
                     /note="cystathionine beta-synthase-like protein"
                     /calculated_mol_wt=60456
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35520.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     Region          76..544
                     /region_name="cysta_beta"
                     /note="cystathionine beta-synthase; TIGR01137"
                     /db_xref="CDD:273464"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     CDS             1..551
                     /gene="LOC102724560"
                     /gene_synonym="CBSL"
                     /coded_by="NM_001354010.1:261..1916"
                     /note="isoform a is encoded by transcript variant 6"
                     /db_xref="GeneID:102724560"
ORIGIN      
        1 mpsetpqaev gptgcphrsg phsakgslek gspedkeake plwirpdaps rctwqlgrpa
       61 sesphhhtap akspkilpdi lkkigdtpmv rinkigkkfg lkcellakce ffnaggsvkd
      121 rislrmieda erdgtlkpgd tiieptsgnt giglalaaav rgyrciivmp ekmssekvdv
      181 lralgaeivr tptnarfdsp eshvgvawrl kneipnshil dqyrnasnpl ahydttadei
      241 lqqcdgkldm lvasvgtggt itgiarklke kcpgcriigv dpegsilaep eelnqteqtt
      301 yevegigydf iptvldrtvv dkwfksndee aftfarmlia qegllcggsa gstvavavka
      361 aqelqegqrc vvilpdsvrn ymtkflsdrw mlqkgflkee dltekkpwww hlrvqelgls
      421 apltvlptit cghtieilre kgfdqapvvd eagvilgmvt lgnmlsslla gkvqpsdqvg
      481 kviykqfkqi rltdtlgrls hilemdhfal vvheqiqyhs tgkssqrqmv fgvvtaidll
      541 nfvaaqerdq k
//
LOCUS       NP_001171480             551 aa            linear   PRI 20-JAN-2026
DEFINITION  cystathionine beta-synthase isoform 1 [Homo sapiens].
ACCESSION   NP_001171480
VERSION     NP_001171480.1
DBSOURCE    REFSEQ: accession NM_001178009.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Hu,X.J., Sun,Y., Liu,G.J., Zhang,J., Zhang,L.X. and Peng,Y.H.
  TITLE     Cystathionine-beta-synthase expression correlates with tumour
            progression and adverse prognosis in patients with colon cancer
  JOURNAL   J Int Med Res 52 (9), 3000605241263726 (2024)
   PUBMED   39324183
  REMARK    GeneRIF: Cystathionine-beta-synthase expression correlates with
            tumour progression and adverse prognosis in patients with colon
            cancer.
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Mijatovic,E., Ascencao,K., Szabo,C. and Majtan,T.
  TITLE     Cellular turnover and degradation of the most common missense
            cystathionine beta-synthase variants causing homocystinuria
  JOURNAL   Protein Sci 33 (8), e5123 (2024)
   PUBMED   39041895
  REMARK    GeneRIF: Cellular turnover and degradation of the most common
            missense cystathionine beta-synthase variants causing
            homocystinuria.
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Al-Sadeq,D.W., Conter,C., Thanassoulas,A., Al-Dewik,N.,
            Safieh-Garabedian,B., Martinez-Cruz,L.A., Nasrallah,G.K.,
            Astegno,A. and Nomikos,M.
  TITLE     Biochemical and structural impact of two novel missense mutations
            in cystathionine beta-synthase gene associated with homocystinuria
  JOURNAL   Biochem J 481 (8), 569-585 (2024)
   PUBMED   38563463
  REMARK    GeneRIF: Biochemical and structural impact of two novel missense
            mutations in cystathionine beta-synthase gene associated with
            homocystinuria.
REFERENCE   4  (residues 1 to 551)
  AUTHORS   McCorvie,T.J., Adamoski,D., Machado,R.A.C., Tang,J., Bailey,H.J.,
            Ferreira,D.S.M., Strain-Damerell,C., Basle,A., Ambrosio,A.L.B.,
            Dias,S.M.G. and Yue,W.W.
  TITLE     Architecture and regulation of filamentous human cystathionine
            beta-synthase
  JOURNAL   Nat Commun 15 (1), 2931 (2024)
   PUBMED   38575566
  REMARK    GeneRIF: Architecture and regulation of filamentous human
            cystathionine beta-synthase.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Sacharow,S.J. and Levy,H.L.
  TITLE     Homocystinuria due to Cystathionine Beta-Synthase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301697
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Milewicz,D.M. and Cecchi,A.C.
  TITLE     Heritable Thoracic Aortic Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301299
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Kraus,J., Packman,S., Fowler,B. and Rosenberg,L.E.
  TITLE     Purification and properties of cystathionine beta-synthase from
            human liver. Evidence for identical subunits
  JOURNAL   J Biol Chem 253 (18), 6523-6528 (1978)
   PUBMED   681363
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Griffiths,R. and Tudball,N.
  TITLE     The molecular defect in a case of (cystathionine
            beta-synthase)-deficient homocystinuria
  JOURNAL   Eur J Biochem 74 (2), 269-273 (1977)
   PUBMED   404147
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Longhi,R.C., Fleisher,L.D., Tallan,H.H. and Gaull,G.E.
  TITLE     Cystathionine beta-synthase deficiency: a qualitative abnormality
            of the deficient enzyme modified by vitamin B6 therapy
  JOURNAL   Pediatr Res 11 (2), 100-103 (1977)
   PUBMED   840498
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY151461.1, L19501.1,
            BC000440.2 and BC010242.1.
            
            Summary: The protein encoded by this gene acts as a homotetramer to
            catalyze the conversion of homocysteine to cystathionine, the first
            step in the transsulfuration pathway. The encoded protein is
            allosterically activated by adenosyl-methionine and uses pyridoxal
            phosphate as a cofactor. Defects in this gene can cause
            cystathionine beta-synthase deficiency (CBSD), which can lead to
            homocystinuria. This gene is a major contributor to cellular
            hydrogen sulfide production. Multiple alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Feb 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2948466.1,
                                           SRR14038191.2778596.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..551
                     /product="cystathionine beta-synthase isoform 1"
                     /EC_number="4.2.1.22"
                     /note="serine sulfhydrase; beta-thionase; methylcysteine
                     synthase"
                     /calculated_mol_wt=60456
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35520.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     Region          76..544
                     /region_name="cysta_beta"
                     /note="cystathionine beta-synthase; TIGR01137"
                     /db_xref="CDD:273464"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     CDS             1..551
                     /gene="CBS"
                     /gene_synonym="HIP4"
                     /coded_by="NM_001178009.3:238..1893"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS13693.1"
                     /db_xref="GeneID:875"
                     /db_xref="HGNC:HGNC:1550"
                     /db_xref="MIM:613381"
ORIGIN      
        1 mpsetpqaev gptgcphrsg phsakgslek gspedkeake plwirpdaps rctwqlgrpa
       61 sesphhhtap akspkilpdi lkkigdtpmv rinkigkkfg lkcellakce ffnaggsvkd
      121 rislrmieda erdgtlkpgd tiieptsgnt giglalaaav rgyrciivmp ekmssekvdv
      181 lralgaeivr tptnarfdsp eshvgvawrl kneipnshil dqyrnasnpl ahydttadei
      241 lqqcdgkldm lvasvgtggt itgiarklke kcpgcriigv dpegsilaep eelnqteqtt
      301 yevegigydf iptvldrtvv dkwfksndee aftfarmlia qegllcggsa gstvavavka
      361 aqelqegqrc vvilpdsvrn ymtkflsdrw mlqkgflkee dltekkpwww hlrvqelgls
      421 apltvlptit cghtieilre kgfdqapvvd eagvilgmvt lgnmlsslla gkvqpsdqvg
      481 kviykqfkqi rltdtlgrls hilemdhfal vvheqiqyhs tgkssqrqmv fgvvtaidll
      541 nfvaaqerdq k
//
LOCUS       NP_001358701             434 aa            linear   PRI 20-JAN-2026
DEFINITION  adenylate kinase 8 isoform 5 [Homo sapiens].
ACCESSION   NP_001358701
VERSION     NP_001358701.1
DBSOURCE    REFSEQ: accession NM_001371772.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Dougherty,G.W., Mizuno,K., Nothe-Menchen,T., Ikawa,Y., Boldt,K.,
            Ta-Shma,A., Aprea,I., Minegishi,K., Pang,Y.P., Pennekamp,P.,
            Loges,N.T., Raidt,J., Hjeij,R., Wallmeier,J., Mussaffi,H.,
            Perles,Z., Elpeleg,O., Rabert,F., Shiratori,H., Letteboer,S.J.,
            Horn,N., Young,S., Strunker,T., Stumme,F., Werner,C., Olbrich,H.,
            Takaoka,K., Ide,T., Twan,W.K., Biebach,L., Grosse-Onnebrink,J.,
            Klinkenbusch,J.A., Praveen,K., Bracht,D.C., Hoben,I.M., Junger,K.,
            Gutzlaff,J., Cindric,S., Aviram,M., Kaiser,T., Memari,Y.,
            Dzeja,P.P., Dworniczak,B., Ueffing,M., Roepman,R., Bartscherer,K.,
            Katsanis,N., Davis,E.E., Amirav,I., Hamada,H. and Omran,H.
  TITLE     CFAP45 deficiency causes situs abnormalities and asthenospermia by
            disrupting an axonemal adenine nucleotide homeostasis module
  JOURNAL   Nat Commun 11 (1), 5520 (2020)
   PUBMED   33139725
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Amiri,M., Conserva,F., Panayiotou,C., Karlsson,A. and Solaroli,N.
  TITLE     The human adenylate kinase 9 is a nucleoside mono- and diphosphate
            kinase
  JOURNAL   Int J Biochem Cell Biol 45 (5), 925-931 (2013)
   PUBMED   23416111
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Panayiotou,C., Solaroli,N., Xu,Y., Johansson,M. and Karlsson,A.
  TITLE     The characterization of human adenylate kinases 7 and 8
            demonstrates differences in kinetic parameters and structural
            organization among the family of adenylate kinase isoenzymes
  JOURNAL   Biochem J 433 (3), 527-534 (2011)
   PUBMED   21080915
  REMARK    GeneRIF: Both AK7 and full-length AK8 showed highest affinity for
            AMP with ATP as the phosphate donor, and proved to be more
            efficient in AMP phosphorylation as compared with the major
            cytosolic isoform AK1
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Lesch,K.P., Timmesfeld,N., Renner,T.J., Halperin,R., Roser,C.,
            Nguyen,T.T., Craig,D.W., Romanos,J., Heine,M., Meyer,J.,
            Freitag,C., Warnke,A., Romanos,M., Schafer,H., Walitza,S., Reif,A.,
            Stephan,D.A. and Jacob,C.
  TITLE     Molecular genetics of adult ADHD: converging evidence from
            genome-wide association and extended pedigree linkage studies
  JOURNAL   J Neural Transm (Vienna) 115 (11), 1573-1585 (2008)
   PUBMED   18839057
REFERENCE   10 (residues 1 to 434)
  AUTHORS   Van Rompay,A.R., Johansson,M. and Karlsson,A.
  TITLE     Identification of a novel human adenylate kinase. cDNA cloning,
            expression analysis, chromosome localization and characterization
            of the recombinant protein
  JOURNAL   Eur J Biochem 261 (2), 509-517 (1999)
   PUBMED   10215863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445645.10 and AL160165.17.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..434
                     /product="adenylate kinase 8 isoform 5"
                     /EC_number="2.7.4.3"
                     /EC_number="2.7.4.6"
                     /note="putative adenylate kinase-like protein C9orf98;
                     ATP-AMP transphosphorylase 8"
                     /calculated_mol_wt=49703
     Region          9..>30
                     /region_name="DD_R_PKA_DPY30-like"
                     /note="dimerization/docking (D/D) domains found in the
                     cAMP-dependent protein kinase regulatory subunit (PRKAR)
                     and the DPY30/SDC1-like family; cl02594"
                     /db_xref="CDD:445844"
     Region          58..>205
                     /region_name="PLN02842"
                     /note="nucleotide kinase"
                     /db_xref="CDD:178435"
     Region          225..417
                     /region_name="ADK"
                     /note="Adenylate kinase (ADK) catalyzes the reversible
                     phosphoryl transfer from adenosine triphosphates (ATP) to
                     adenosine monophosphates (AMP) and to yield adenosine
                     diphosphates (ADP). This enzyme is required for the
                     biosynthesis of ADP and is essential for...; cd01428"
                     /db_xref="CDD:238713"
     Site            order(254,259,282,308..309,311..312,316)
                     /site_type="other"
                     /note="AMP-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     Site            order(259,308,312,347,387,391)
                     /site_type="other"
                     /note="ATP-AMP (Ap5A)-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     CDS             1..434
                     /gene="AK8"
                     /gene_synonym="AK 8; C9orf98"
                     /coded_by="NM_001371772.1:30..1334"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:158067"
                     /db_xref="HGNC:HGNC:26526"
                     /db_xref="MIM:615365"
ORIGIN      
        1 mdatiaphri ppempqygee nhifelmqam wlckhlnssl ltlenlilne fsytatearr
       61 lylqrktvps allvqliqer laeedcikqg wildgipetr eqalriqtlg itprhvivls
      121 apdtvliern lgkridpqtg eiyhttfdwp peseiqnrlm vpediselet aqklleyhrn
      181 ivrvipsypk ilkvisadqp cvdvfyqalt yvqsnhrtna pftprvlllg pvgsgkslqa
      241 allaqkyrlv nvccgqllke avadrttfge liqpffekem avpdsllmkv lsqrldqqdc
      301 iqkgwvlhgv prdldqahll nrlgynpnrv fflnvpfdsi merltlrrid pvtgeryhlm
      361 ykppptmeiq arllqnpkda eeqvklkmdl fyrnsadleq lygsaitlng dqdpytvfey
      421 iesgiinplp kkip
//
LOCUS       NP_001358702             275 aa            linear   PRI 20-JAN-2026
DEFINITION  adenylate kinase 8 isoform 2 [Homo sapiens].
ACCESSION   NP_001358702 XP_024303187
VERSION     NP_001358702.1
DBSOURCE    REFSEQ: accession NM_001371773.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Dougherty,G.W., Mizuno,K., Nothe-Menchen,T., Ikawa,Y., Boldt,K.,
            Ta-Shma,A., Aprea,I., Minegishi,K., Pang,Y.P., Pennekamp,P.,
            Loges,N.T., Raidt,J., Hjeij,R., Wallmeier,J., Mussaffi,H.,
            Perles,Z., Elpeleg,O., Rabert,F., Shiratori,H., Letteboer,S.J.,
            Horn,N., Young,S., Strunker,T., Stumme,F., Werner,C., Olbrich,H.,
            Takaoka,K., Ide,T., Twan,W.K., Biebach,L., Grosse-Onnebrink,J.,
            Klinkenbusch,J.A., Praveen,K., Bracht,D.C., Hoben,I.M., Junger,K.,
            Gutzlaff,J., Cindric,S., Aviram,M., Kaiser,T., Memari,Y.,
            Dzeja,P.P., Dworniczak,B., Ueffing,M., Roepman,R., Bartscherer,K.,
            Katsanis,N., Davis,E.E., Amirav,I., Hamada,H. and Omran,H.
  TITLE     CFAP45 deficiency causes situs abnormalities and asthenospermia by
            disrupting an axonemal adenine nucleotide homeostasis module
  JOURNAL   Nat Commun 11 (1), 5520 (2020)
   PUBMED   33139725
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Amiri,M., Conserva,F., Panayiotou,C., Karlsson,A. and Solaroli,N.
  TITLE     The human adenylate kinase 9 is a nucleoside mono- and diphosphate
            kinase
  JOURNAL   Int J Biochem Cell Biol 45 (5), 925-931 (2013)
   PUBMED   23416111
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Panayiotou,C., Solaroli,N., Xu,Y., Johansson,M. and Karlsson,A.
  TITLE     The characterization of human adenylate kinases 7 and 8
            demonstrates differences in kinetic parameters and structural
            organization among the family of adenylate kinase isoenzymes
  JOURNAL   Biochem J 433 (3), 527-534 (2011)
   PUBMED   21080915
  REMARK    GeneRIF: Both AK7 and full-length AK8 showed highest affinity for
            AMP with ATP as the phosphate donor, and proved to be more
            efficient in AMP phosphorylation as compared with the major
            cytosolic isoform AK1
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Lesch,K.P., Timmesfeld,N., Renner,T.J., Halperin,R., Roser,C.,
            Nguyen,T.T., Craig,D.W., Romanos,J., Heine,M., Meyer,J.,
            Freitag,C., Warnke,A., Romanos,M., Schafer,H., Walitza,S., Reif,A.,
            Stephan,D.A. and Jacob,C.
  TITLE     Molecular genetics of adult ADHD: converging evidence from
            genome-wide association and extended pedigree linkage studies
  JOURNAL   J Neural Transm (Vienna) 115 (11), 1573-1585 (2008)
   PUBMED   18839057
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Van Rompay,A.R., Johansson,M. and Karlsson,A.
  TITLE     Identification of a novel human adenylate kinase. cDNA cloning,
            expression analysis, chromosome localization and characterization
            of the recombinant protein
  JOURNAL   Eur J Biochem 261 (2), 509-517 (1999)
   PUBMED   10215863
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445645.10 and AL160165.17.
            
            On Jul 25, 2019 this sequence version replaced XP_024303187.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.647894.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..275
                     /product="adenylate kinase 8 isoform 2"
                     /EC_number="2.7.4.3"
                     /EC_number="2.7.4.6"
                     /note="putative adenylate kinase-like protein C9orf98;
                     ATP-AMP transphosphorylase 8"
                     /calculated_mol_wt=31324
     Region          66..258
                     /region_name="ADK"
                     /note="Adenylate kinase (ADK) catalyzes the reversible
                     phosphoryl transfer from adenosine triphosphates (ATP) to
                     adenosine monophosphates (AMP) and to yield adenosine
                     diphosphates (ADP). This enzyme is required for the
                     biosynthesis of ADP and is essential for...; cd01428"
                     /db_xref="CDD:238713"
     Site            order(95,100,123,149..150,152..153,157)
                     /site_type="other"
                     /note="AMP-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     Site            order(100,149,153,188,228,232)
                     /site_type="other"
                     /note="ATP-AMP (Ap5A)-binding site [chemical binding]"
                     /db_xref="CDD:238713"
     CDS             1..275
                     /gene="AK8"
                     /gene_synonym="AK 8; C9orf98"
                     /coded_by="NM_001371773.1:714..1541"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:158067"
                     /db_xref="HGNC:HGNC:26526"
                     /db_xref="MIM:615365"
ORIGIN      
        1 mvpedisele taqklleyhr nivrvipsyp kilkvisadq pcvdvfyqal tyvqsnhrtn
       61 apftprvlll gpvgsgkslq aallaqkyrl vnvccgqllk eavadrttfg eliqpffeke
      121 mavpdsllmk vlsqrldqqd ciqkgwvlhg vprdldqahl lnrlgynpnr vfflnvpfds
      181 imerltlrri dpvtgeryhl mykppptmei qarllqnpkd aeeqvklkmd lfyrnsadle
      241 qlygsaitln gdqdpytvfe yiesgiinpl pkkip
//
LOCUS       NP_001340936             551 aa            linear   PRI 20-JAN-2026
DEFINITION  cystathionine beta-synthase isoform a [Homo sapiens].
ACCESSION   NP_001340936 XP_016883707
VERSION     NP_001340936.1
DBSOURCE    REFSEQ: accession NM_001354007.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Kumar,A., Wissbrock,A., Goradia,N., Bellstedt,P., Ramachandran,R.,
            Imhof,D. and Ohlenschlager,O.
  TITLE     Heme interaction of the intrinsically disordered N-terminal peptide
            segment of human cystathionine-beta-synthase
  JOURNAL   Sci Rep 8 (1), 2474 (2018)
   PUBMED   29410458
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Kabil,O., Zhou,Y. and Banerjee,R.
  TITLE     Human cystathionine beta-synthase is a target for sumoylation
  JOURNAL   Biochemistry 45 (45), 13528-13536 (2006)
   PUBMED   17087506
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Hu,Y.H., Warnatz,H.J., Vanhecke,D., Wagner,F., Fiebitz,A.,
            Thamm,S., Kahlem,P., Lehrach,H., Yaspo,M.L. and Janitz,M.
  TITLE     Cell array-based intracellular localization screening reveals novel
            functional features of human chromosome 21 proteins
  JOURNAL   BMC Genomics 7, 155 (2006)
   PUBMED   16780588
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Chen,X., Jhee,K.H. and Kruger,W.D.
  TITLE     Production of the neuromodulator H2S by cystathionine beta-synthase
            via the condensation of cysteine and homocysteine
  JOURNAL   J Biol Chem 279 (50), 52082-52086 (2004)
   PUBMED   15520012
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Meier,M., Janosik,M., Kery,V., Kraus,J.P. and Burkhard,P.
  TITLE     Structure of human cystathionine beta-synthase: a unique pyridoxal
            5'-phosphate-dependent heme protein
  JOURNAL   EMBO J 20 (15), 3910-3916 (2001)
   PUBMED   11483494
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Kery,V., Bukovska,G. and Kraus,J.P.
  TITLE     Transsulfuration depends on heme in addition to pyridoxal
            5'-phosphate. Cystathionine beta-synthase is a heme protein
  JOURNAL   J Biol Chem 269 (41), 25283-25288 (1994)
   PUBMED   7929220
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FP236240.8.
            
            On Aug 3, 2017 this sequence version replaced XP_016883707.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments. NM_001354007 is annotated on a
            scaffold that is thought to be a false duplication and thus this
            accession is possibly redundant with other RefSeq accessions.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.206614.1,
                                           SRR1660803.121318.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21p12"
     Protein         1..551
                     /product="cystathionine beta-synthase isoform a"
                     /EC_number="4.2.1.22"
                     /note="cystathionine beta-synthase-like protein"
                     /calculated_mol_wt=60456
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35520.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     Region          76..544
                     /region_name="cysta_beta"
                     /note="cystathionine beta-synthase; TIGR01137"
                     /db_xref="CDD:273464"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     CDS             1..551
                     /gene="LOC102724560"
                     /gene_synonym="CBSL"
                     /coded_by="NM_001354007.1:329..1984"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="GeneID:102724560"
ORIGIN      
        1 mpsetpqaev gptgcphrsg phsakgslek gspedkeake plwirpdaps rctwqlgrpa
       61 sesphhhtap akspkilpdi lkkigdtpmv rinkigkkfg lkcellakce ffnaggsvkd
      121 rislrmieda erdgtlkpgd tiieptsgnt giglalaaav rgyrciivmp ekmssekvdv
      181 lralgaeivr tptnarfdsp eshvgvawrl kneipnshil dqyrnasnpl ahydttadei
      241 lqqcdgkldm lvasvgtggt itgiarklke kcpgcriigv dpegsilaep eelnqteqtt
      301 yevegigydf iptvldrtvv dkwfksndee aftfarmlia qegllcggsa gstvavavka
      361 aqelqegqrc vvilpdsvrn ymtkflsdrw mlqkgflkee dltekkpwww hlrvqelgls
      421 apltvlptit cghtieilre kgfdqapvvd eagvilgmvt lgnmlsslla gkvqpsdqvg
      481 kviykqfkqi rltdtlgrls hilemdhfal vvheqiqyhs tgkssqrqmv fgvvtaidll
      541 nfvaaqerdq k
//
LOCUS       NP_001310994             809 aa            linear   PRI 20-JAN-2026
DEFINITION  transport and Golgi organization protein 1 homolog isoform 6 [Homo
            sapiens].
ACCESSION   NP_001310994
VERSION     NP_001310994.1
DBSOURCE    REFSEQ: accession NM_001324065.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Wanbiao,Z., Jing,M., Shi,Z., Tengxiang,C., Xueke,Z. and Haiyang,L.
  TITLE     MIA3 promotes the degradation of GSH (glutathione) by binding to
            CHAC1, thereby promoting the progression of hepatocellular
            carcinoma
  JOURNAL   Mol Cell Biochem 479 (10), 2769-2784 (2024)
   PUBMED   37948019
  REMARK    GeneRIF: MIA3 promotes the degradation of GSH (glutathione) by
            binding to CHAC1, thereby promoting the progression of
            hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Connolly,L.M., McFalls,C.M., McMahon,I.G., Bhat,A.M. and
            Artlett,C.M.
  TITLE     Caspase 1 Enhances Transport and Golgi Organization Protein 1
            Expression to Promote Procollagen Export From the Endoplasmic
            Reticulum in Systemic Sclerosis Contributing to Fibrosis
  JOURNAL   Arthritis Rheumatol 75 (10), 1831-1841 (2023)
   PUBMED   37067501
  REMARK    GeneRIF: Caspase 1 Enhances Transport and Golgi Organization
            Protein 1 Expression to Promote Procollagen Export From the
            Endoplasmic Reticulum in Systemic Sclerosis Contributing to
            Fibrosis.
REFERENCE   4  (residues 1 to 809)
  AUTHORS   Man,J., Zhou,W., Zuo,S., Zhao,X., Wang,Q., Ma,H. and Li,H.Y.
  TITLE     TANGO1 interacts with NRTN to promote hepatocellular carcinoma
            progression by regulating the PI3K/AKT/mTOR signaling pathway
  JOURNAL   Biochem Pharmacol 213, 115615 (2023)
   PUBMED   37211171
  REMARK    GeneRIF: TANGO1 interacts with NRTN to promote hepatocellular
            carcinoma progression by regulating the PI3K/AKT/mTOR signaling
            pathway.
REFERENCE   5  (residues 1 to 809)
  AUTHORS   Junkiert-Czarnecka,A., Pilarska-Deltow,M., Bak,A., Heise,M. and
            Haus,O.
  TITLE     A novel mutation in collagen transport protein, MIA3 gene, detected
            in a patient with clinical symptoms of Ehlers-Danlos hypermobile
            syndrome
  JOURNAL   Adv Clin Exp Med 32 (7), 777-781 (2023)
   PUBMED   36603143
  REMARK    GeneRIF: A novel mutation in collagen transport protein, MIA3 gene,
            detected in a patient with clinical symptoms of Ehlers-Danlos
            hypermobile syndrome.
REFERENCE   6  (residues 1 to 809)
  AUTHORS   Saito,K., Chen,M., Bard,F., Chen,S., Zhou,H., Woodley,D.,
            Polischuk,R., Schekman,R. and Malhotra,V.
  TITLE     TANGO1 facilitates cargo loading at endoplasmic reticulum exit
            sites
  JOURNAL   Cell 136 (5), 891-902 (2009)
   PUBMED   19269366
REFERENCE   7  (residues 1 to 809)
  AUTHORS   Arndt,S., Melle,C., Mondal,K., Klein,G., von Eggeling,F. and
            Bosserhoff,A.K.
  TITLE     Interactions of TANGO and leukocyte integrin CD11c/CD18 regulate
            the migration of human monocytes
  JOURNAL   J Leukoc Biol 82 (6), 1466-1472 (2007)
   PUBMED   17726152
  REMARK    GeneRIF: The results from this study present TANGO as a novel
            ligand for CD11c, regulating migratory processes of hematopoietic
            cells.
REFERENCE   8  (residues 1 to 809)
  AUTHORS   Arndt,S. and Bosserhoff,A.K.
  TITLE     Reduced expression of TANGO in colon and hepatocellular carcinomas
  JOURNAL   Oncol Rep 18 (4), 885-891 (2007)
   PUBMED   17786351
  REMARK    GeneRIF: Reduced expression of TANGO is associated with colon and
            hepatocellular carcinomas
REFERENCE   9  (residues 1 to 809)
  AUTHORS   Arndt,S. and Bosserhoff,A.K.
  TITLE     TANGO is a tumor suppressor of malignant melanoma
  JOURNAL   Int J Cancer 119 (12), 2812-2820 (2006)
   PUBMED   17044017
  REMARK    GeneRIF: TANGO transfected cell lines revealed that TANGO
            expression reduces motility, whereas reduction of TANGO enhances
            migration.
REFERENCE   10 (residues 1 to 809)
  AUTHORS   Bosserhoff,A.K., Moser,M. and Buettner,R.
  TITLE     Characterization and expression pattern of the novel MIA homolog
            TANGO
  JOURNAL   Gene Expr Patterns 4 (4), 473-479 (2004)
   PUBMED   15183315
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL592148.7 and KF459535.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1717973.1,
                                           SRR14038194.2107895.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..809
                     /product="transport and Golgi organization protein 1
                     homolog isoform 6"
                     /note="C219-reactive peptide; melanoma inhibitory activity
                     protein 3; MIA family member 3, ER export factor; melanoma
                     inhibitory activity family, member 3; transport and Golgi
                     organization protein 1 homolog"
                     /calculated_mol_wt=89837
     Region          <90..469
                     /region_name="Mplasa_alph_rch"
                     /note="helix-rich Mycoplasma protein; TIGR04523"
                     /db_xref="CDD:275316"
     Region          <522..795
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..809
                     /gene="MIA3"
                     /gene_synonym="D320; ODCD2; TANGO; TANGO1; UNQ6077"
                     /coded_by="NM_001324065.2:148..2577"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:375056"
                     /db_xref="HGNC:HGNC:24008"
                     /db_xref="MIM:613455"
ORIGIN      
        1 mdsvpatvps iaatpgdpel vgplsvlyaa fiakllelva tlpddvqpgp dfyglpwkpv
       61 fitaflgias faiflwrtvl vvkdrvyqvt eqqiseklkt imkentelvq klsnyeqkik
      121 eskkhvqetr kqnmilsdea ikykdkiktl eknqeilddt aknlrvmles ereqnvknqd
      181 lisenkksie klkdvismna sefsevqial neaklseekv ksechrvqee narlkkkkeq
      241 lqqeiedwsk lhaelseqik sfeksqkdle valthkddni naltncitql nllecesese
      301 gqnkggndsd elangevggd rnekmknqik qmmdvsrtqt aisvveedlk llqlklrasv
      361 stkcnledqv kkleddrnsl qaakaglede cktlrqkvei lnelyqqkem alqkklsqee
      421 yerqerehrl saadekavsa aeevktykrr ieemedelqk tersfknqia thekkahenw
      481 lkaraaerai aeekreaanl rhklleltqk mamlqeepvi vkpmpgkpnt qnpprrgpls
      541 qngsfgpspv sggecspplt veppvrplsa tlnrrdmprs efgsvdgplp hprwsaeasg
      601 kpspsdpgsg tatmmnsssr gssptrvlde gkqtvlqepe vpsvpsitsl aerpvavnma
      661 pkgpppfpgv plmstpmggp vpppirygpp pqlcgpfgpr plpppfgpgm rpplglrefa
      721 pgvppgrrdl plhprgflpg hapfrplgsl gpreyfipgt rlpppthgpq eyppppavrd
      781 llpsgsrdep ppasqstsqd csqalkqsp
//
LOCUS       NP_001310223             267 aa            linear   PRI 20-JAN-2026
DEFINITION  zinc finger protein 197 isoform 2 [Homo sapiens].
ACCESSION   NP_001310223 XP_016860984
VERSION     NP_001310223.1
DBSOURCE    REFSEQ: accession NM_001323294.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Li,Z., Wang,D., Na,X., Schoen,S.R., Messing,E.M. and Wu,G.
  TITLE     The VHL protein recruits a novel KRAB-A domain protein to repress
            HIF-1alpha transcriptional activity
  JOURNAL   EMBO J 22 (8), 1857-1867 (2003)
   PUBMED   12682018
  REMARK    GeneRIF: a novel pVHL-interacting protein that functions as a
            negative regulator of hypoxia-inducible factor-1a (HIF-1alpha)
            transactivation; demonstrate that the KRAB-A domain in VHLaK
            mediates pVHL binding and functions as a transcriptional repression
            module
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Gonsky,R., Knauf,J.A., Elisei,R., Wang,J.W., Su,S. and Fagin,J.A.
  TITLE     Identification of rapid turnover transcripts overexpressed in
            thyroid tumors and thyroid cancer cell lines: use of a targeted
            differential RNA display method to select for mRNA subsets
  JOURNAL   Nucleic Acids Res 25 (19), 3823-3831 (1997)
   PUBMED   9380504
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Calabro,V., Pengue,G., Bartoli,P.C., Pagliuca,A., Featherstone,T.
            and Lania,L.
  TITLE     Positional cloning of cDNAs from the human chromosome 3p21-22
            region identifies a clustered organization of zinc-finger genes
  JOURNAL   Hum Genet 95 (1), 18-21 (1995)
   PUBMED   7814019
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Pengue,G., Calabro,V., Cannada-Bartoli,P., De Luca,P., Esposito,T.,
            Taillon-Miller,P., LaForgia,S., Druck,T., Huebner,K., D'Urso,M. et
            al.
  TITLE     YAC-assisted cloning of transcribed sequences from the human
            chromosome 3p21 region
  JOURNAL   Hum Mol Genet 2 (6), 791-796 (1993)
   PUBMED   8353497
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY279353.1, AC099669.2 and
            BQ002665.1.
            
            On Jul 8, 2016 this sequence version replaced XP_016860984.1.
            
            Summary: This gene product belongs to the zinc finger protein
            superfamily, members of which are regulatory proteins characterized
            by nucleic acid-binding zinc finger domains. The encoded protein
            contains 20 tandemly arrayed C2H2-type zinc fingers, a
            Kruppel-associated box (KRAB) domain, and a SCAN box. This
            transcript turns over rapidly and contains 3' UTR AUUUA motifs,
            which are often a hallmark of rapid turnover. It is overexpressed
            in some thyroid papillary carcinomas. This gene is located in a
            cluster of zinc finger genes at 3p21. Naturally-occurring
            readthrough transcription is observed between this gene and the
            upstream zinc finger protein 660 gene and is represented by
            GeneID:110354863. [provided by RefSeq, May 2017].
            
            Transcript Variant: Variants 2 and 4 encode the same isoform (2).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.241014.1,
                                           SRR1803611.242939.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..267
                     /product="zinc finger protein 197 isoform 2"
                     /note="zinc finger protein 166; VHL-associated KRAB-A
                     domain-containing protein; zinc finger protein with KRAB
                     and SCAN domains 9; pVHL-associated KRAB domain-containing
                     protein"
                     /calculated_mol_wt=30098
     Region          38..150
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          216..257
                     /region_name="KRAB"
                     /note="KRAB box; pfam01352"
                     /db_xref="CDD:460171"
     CDS             1..267
                     /gene="ZNF197"
                     /gene_synonym="D3S1363E; P18; VHLaK; ZKSCAN9; ZNF166;
                     ZSCAN41"
                     /coded_by="NM_001323294.2:190..993"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:10168"
                     /db_xref="HGNC:HGNC:12988"
                     /db_xref="MIM:618359"
ORIGIN      
        1 mtrenvahna lrqeglvkgk ddtwkwgtsf qgssssvwet shlhfrqlry hetsgpqeal
       61 srlrelcrrw lrpeartkaq ilellvleqf lsilpgeirt wvqlhhpgsg eeavalveel
      121 qkdldgpaiq vpvlvkdqdt lqkvvsapgt tlppvlpgsh iaaeicphpp tdlvafnlqd
      181 pqhdspapea salsqeenpr nqlmalmllt aqpqelvmfe evsvcftsee waclgpiqra
      241 lywdvmleny gnvtslgyrk yrrqrnk
//
LOCUS       NP_683709                321 aa            linear   PRI 20-JAN-2026
DEFINITION  CHRNA7-FAM7A fusion protein isoform 2 [Homo sapiens].
ACCESSION   NP_683709
VERSION     NP_683709.1
DBSOURCE    REFSEQ: accession NM_148911.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Gorgulu,I., Jagannath,V., Pons,S., Koniuszewski,F., Groszer,M.,
            Maskos,U., Huck,S. and Scholze,P.
  TITLE     The human-specific nicotinic receptor subunit CHRFAM7A reduces
            alpha7 receptor function in human induced pluripotent stem
            cells-derived and transgenic mouse neurons
  JOURNAL   Eur J Neurosci 60 (5), 4893-4906 (2024)
   PUBMED   39073048
  REMARK    GeneRIF: The human-specific nicotinic receptor subunit CHRFAM7A
            reduces alpha7 receptor function in human induced pluripotent stem
            cells-derived and transgenic mouse neurons.
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Szigeti,K., Ihnatovych,I., Notari,E., Dorn,R.P., Maly,I., He,M.,
            Birkaya,B., Prasad,S., Byrne,R.S., Indurthi,D.C., Nimmer,E.,
            Heo,Y., Retfalvi,K., Chaves,L., Sule,N., Hofmann,W.A., Auerbach,A.,
            Wilding,G., Bae,Y. and Reynolds,J.
  TITLE     CHRFAM7A diversifies human immune adaption through Ca2+ signalling
            and actin cytoskeleton reorganization
  JOURNAL   EBioMedicine 103, 105093 (2024)
   PUBMED   38569318
  REMARK    GeneRIF: CHRFAM7A diversifies human immune adaption through Ca[2+]
            signalling and actin cytoskeleton reorganization.
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Pradhan,A., Mounford,H., Peixinho,J., Rea,E., Epeslidou,E.,
            Scott,J.S., Cull,J., Maxwell,S., Webster,R., Beeson,D., Dong,Y.Y.,
            Prekovic,S., Bermudez,I. and Newbury,D.F.
  TITLE     Unraveling the molecular interactions between alpha7 nicotinic
            receptor and a RIC3 variant associated with backward speech
  JOURNAL   Cell Mol Life Sci 81 (1), 129 (2024)
   PUBMED   38472514
  REMARK    GeneRIF: Unraveling the molecular interactions between alpha7
            nicotinic receptor and a RIC3 variant associated with backward
            speech.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Burke,S.M., Avstrikova,M., Noviello,C.M., Mukhtasimova,N.,
            Changeux,J.P., Thakur,G.A., Sine,S.M., Cecchini,M. and Hibbs,R.E.
  TITLE     Structural mechanisms of alpha7 nicotinic receptor allosteric
            modulation and activation
  JOURNAL   Cell 187 (5), 1160-1176 (2024)
   PUBMED   38382524
  REMARK    GeneRIF: Structural mechanisms of alpha7 nicotinic receptor
            allosteric modulation and activation.
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Prevost,M.S., Barilone,N., Dejean de la Batie,G., Pons,S., Ayme,G.,
            England,P., Gielen,M., Bontems,F., Pehau-Arnaudet,G., Maskos,U.,
            Lafaye,P. and Corringer,P.J.
  TITLE     An original potentiating mechanism revealed by the cryo-EM
            structures of the human alpha7 nicotinic receptor in complex with
            nanobodies
  JOURNAL   Nat Commun 14 (1), 5964 (2023)
   PUBMED   37749098
  REMARK    GeneRIF: An original potentiating mechanism revealed by the cryo-EM
            structures of the human alpha7 nicotinic receptor in complex with
            nanobodies.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Bale,A.S., Meacham,C.A., Benignus,V.A., Bushnell,P.J. and
            Shafer,T.J.
  TITLE     Volatile organic compounds inhibit human and rat neuronal nicotinic
            acetylcholine receptors expressed in Xenopus oocytes
  JOURNAL   Toxicol Appl Pharmacol 205 (1), 77-88 (2005)
   PUBMED   15885267
  REMARK    GeneRIF: Results demonstrate that human and rat nicotinic
            acetylcholine receptors are senstive targets for volatile organic
            compounds in industrial products and are used in the risk
            assessment of these compounds.
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Trombino,S., Cesario,A., Margaritora,S., Granone,P., Motta,G.,
            Falugi,C. and Russo,P.
  TITLE     Alpha7-nicotinic acetylcholine receptors affect growth regulation
            of human mesothelioma cells: role of mitogen-activated protein
            kinase pathway
  JOURNAL   Cancer Res 64 (1), 135-145 (2004)
   PUBMED   14729617
  REMARK    GeneRIF: Human mesothelioma cells and human biopsies of
            mesothelioma as well as of normal pleural mesothelial cells
            functionally express CHRNA7.
            Erratum:[Cancer Res. 2004 Feb 15;64(4):1559]
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Riley,B., Williamson,M., Collier,D., Wilkie,H. and Makoff,A.
  TITLE     A 3-Mb map of a large Segmental duplication overlapping the
            alpha7-nicotinic acetylcholine receptor gene (CHRNA7) at human
            15q13-q14
  JOURNAL   Genomics 79 (2), 197-209 (2002)
   PUBMED   11829490
  REMARK    GeneRIF: 3-Mb map of 15q13-q14 showing that CHRFAM7A is part of a
            large segmental duplication in the opposite orientation to CHRNA7
            and revealing several other duplications
REFERENCE   9  (residues 1 to 321)
  AUTHORS   Freedman,R., Leonard,S., Gault,J.M., Hopkins,J., Cloninger,C.R.,
            Kaufmann,C.A., Tsuang,M.T., Farone,S.V., Malaspina,D.,
            Svrakic,D.M., Sanders,A. and Gejman,P.
  TITLE     Linkage disequilibrium for schizophrenia at the chromosome 15q13-14
            locus of the alpha7-nicotinic acetylcholine receptor subunit gene
            (CHRNA7)
  JOURNAL   Am J Med Genet 105 (1), 20-22 (2001)
   PUBMED   11424985
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Gault,J., Robinson,M., Berger,R., Drebing,C., Logel,J., Hopkins,J.,
            Moore,T., Jacobs,S., Meriwether,J., Choi,M.J., Kim,E.J., Walton,K.,
            Buiting,K., Davis,A., Breese,C., Freedman,R. and Leonard,S.
  TITLE     Genomic organization and partial duplication of the human alpha7
            neuronal nicotinic acetylcholine receptor gene (CHRNA7)
  JOURNAL   Genomics 52 (2), 173-185 (1998)
   PUBMED   9782083
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC019322.8.
            
            Summary: The nicotinic acetylcholine receptors (nAChRs) are members
            of a superfamily of ligand-gated ion channels that mediate fast
            signal transmission at synapses. The family member CHRNA7, which is
            located on chromosome 15 in a region associated with several
            neuropsychiatric disorders, is partially duplicated and forms a
            hybrid with a novel gene from the family with sequence similarity 7
            (FAM7A). Alternative splicing has been observed, and two variants
            exist, for this hybrid gene. The N-terminally truncated products
            predicted by the largest open reading frames for each variant would
            lack the majority of the neurotransmitter-gated ion-channel ligand
            binding domain but retain the transmembrane region that forms the
            ion channel. Although current evidence supports transcription of
            this hybrid gene, translation of the nicotinic acetylcholine
            receptor-like protein-encoding open reading frames has not been
            confirmed. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an internal exon
            compared to variant 1, and is missing the translation initiation
            site used by the longer variant. Translation from variant 2
            initiates at a downstream site relative to variant 1, resulting in
            isoform (2), which is truncated at the N-terminus compared to
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF036903.1, SRR5189652.135903.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2161674 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q13.2"
     Protein         1..321
                     /product="CHRNA7-FAM7A fusion protein isoform 2"
                     /note="CHRNA7 (cholinergic receptor, nicotinic, alpha
                     polypeptide 7, exons 5-10) and FAM7A (family with sequence
                     similarity 7A, exons A-E) fusion; alpha 7 neuronal
                     nicotinic acetylcholine receptor-FAM7A hybrid;
                     CHRNA7-FAM7A fusion protein; alpha-7 nicotinic cholinergic
                     receptor subunit; CHRNA7 (cholinergic receptor, nicotinic,
                     alpha 7, exons 5-10) and FAM7A (family with sequence
                     similarity 7A, exons A-E) fusion"
                     /calculated_mol_wt=35351
     Region          <3..309
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     CDS             1..321
                     /gene="CHRFAM7A"
                     /gene_synonym="CHRNA7; CHRNA7-DR1; D-10"
                     /coded_by="NM_148911.1:776..1741"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42008.1"
                     /db_xref="GeneID:89832"
                     /db_xref="HGNC:HGNC:15781"
                     /db_xref="MIM:609756"
ORIGIN      
        1 mqeadisgyi pngewdlvgi pgkrserfye cckepypdvt ftvtmrrrtl yyglnllipc
       61 vlisalallv fllpadsgek islgitvlls ltvfmllvae impatsdsvp liaqyfastm
      121 iivglsvvvt vivlqyhhhd pdggkmpkwt rvillnwcaw flrmkrpged kvrpacqhkq
      181 rrcslasvem savapppasn gnllyigfrg ldgvhcvptp dsgvvcgrma cspthdehll
      241 hggqppegdp dlakileevr yianrfrcqd eseavcsewk faacvvdrlc lmafsvftii
      301 ctigilmsap nfveavskdf a
//
LOCUS       NP_001171479             551 aa            linear   PRI 20-JAN-2026
DEFINITION  cystathionine beta-synthase isoform 1 [Homo sapiens].
ACCESSION   NP_001171479
VERSION     NP_001171479.1
DBSOURCE    REFSEQ: accession NM_001178008.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Hu,X.J., Sun,Y., Liu,G.J., Zhang,J., Zhang,L.X. and Peng,Y.H.
  TITLE     Cystathionine-beta-synthase expression correlates with tumour
            progression and adverse prognosis in patients with colon cancer
  JOURNAL   J Int Med Res 52 (9), 3000605241263726 (2024)
   PUBMED   39324183
  REMARK    GeneRIF: Cystathionine-beta-synthase expression correlates with
            tumour progression and adverse prognosis in patients with colon
            cancer.
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Mijatovic,E., Ascencao,K., Szabo,C. and Majtan,T.
  TITLE     Cellular turnover and degradation of the most common missense
            cystathionine beta-synthase variants causing homocystinuria
  JOURNAL   Protein Sci 33 (8), e5123 (2024)
   PUBMED   39041895
  REMARK    GeneRIF: Cellular turnover and degradation of the most common
            missense cystathionine beta-synthase variants causing
            homocystinuria.
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Al-Sadeq,D.W., Conter,C., Thanassoulas,A., Al-Dewik,N.,
            Safieh-Garabedian,B., Martinez-Cruz,L.A., Nasrallah,G.K.,
            Astegno,A. and Nomikos,M.
  TITLE     Biochemical and structural impact of two novel missense mutations
            in cystathionine beta-synthase gene associated with homocystinuria
  JOURNAL   Biochem J 481 (8), 569-585 (2024)
   PUBMED   38563463
  REMARK    GeneRIF: Biochemical and structural impact of two novel missense
            mutations in cystathionine beta-synthase gene associated with
            homocystinuria.
REFERENCE   4  (residues 1 to 551)
  AUTHORS   McCorvie,T.J., Adamoski,D., Machado,R.A.C., Tang,J., Bailey,H.J.,
            Ferreira,D.S.M., Strain-Damerell,C., Basle,A., Ambrosio,A.L.B.,
            Dias,S.M.G. and Yue,W.W.
  TITLE     Architecture and regulation of filamentous human cystathionine
            beta-synthase
  JOURNAL   Nat Commun 15 (1), 2931 (2024)
   PUBMED   38575566
  REMARK    GeneRIF: Architecture and regulation of filamentous human
            cystathionine beta-synthase.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Sacharow,S.J. and Levy,H.L.
  TITLE     Homocystinuria due to Cystathionine Beta-Synthase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301697
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Milewicz,D.M. and Cecchi,A.C.
  TITLE     Heritable Thoracic Aortic Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301299
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Kraus,J., Packman,S., Fowler,B. and Rosenberg,L.E.
  TITLE     Purification and properties of cystathionine beta-synthase from
            human liver. Evidence for identical subunits
  JOURNAL   J Biol Chem 253 (18), 6523-6528 (1978)
   PUBMED   681363
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Griffiths,R. and Tudball,N.
  TITLE     The molecular defect in a case of (cystathionine
            beta-synthase)-deficient homocystinuria
  JOURNAL   Eur J Biochem 74 (2), 269-273 (1977)
   PUBMED   404147
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Longhi,R.C., Fleisher,L.D., Tallan,H.H. and Gaull,G.E.
  TITLE     Cystathionine beta-synthase deficiency: a qualitative abnormality
            of the deficient enzyme modified by vitamin B6 therapy
  JOURNAL   Pediatr Res 11 (2), 100-103 (1977)
   PUBMED   840498
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY151461.1, L19501.1,
            BC000440.2 and BC010242.1.
            
            Summary: The protein encoded by this gene acts as a homotetramer to
            catalyze the conversion of homocysteine to cystathionine, the first
            step in the transsulfuration pathway. The encoded protein is
            allosterically activated by adenosyl-methionine and uses pyridoxal
            phosphate as a cofactor. Defects in this gene can cause
            cystathionine beta-synthase deficiency (CBSD), which can lead to
            homocystinuria. This gene is a major contributor to cellular
            hydrogen sulfide production. Multiple alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Feb 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L19501.1, SRR14038193.3293609.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..551
                     /product="cystathionine beta-synthase isoform 1"
                     /EC_number="4.2.1.22"
                     /note="serine sulfhydrase; beta-thionase; methylcysteine
                     synthase"
                     /calculated_mol_wt=60456
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35520.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     Region          76..544
                     /region_name="cysta_beta"
                     /note="cystathionine beta-synthase; TIGR01137"
                     /db_xref="CDD:273464"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     CDS             1..551
                     /gene="CBS"
                     /gene_synonym="HIP4"
                     /coded_by="NM_001178008.3:238..1893"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS13693.1"
                     /db_xref="GeneID:875"
                     /db_xref="HGNC:HGNC:1550"
                     /db_xref="MIM:613381"
ORIGIN      
        1 mpsetpqaev gptgcphrsg phsakgslek gspedkeake plwirpdaps rctwqlgrpa
       61 sesphhhtap akspkilpdi lkkigdtpmv rinkigkkfg lkcellakce ffnaggsvkd
      121 rislrmieda erdgtlkpgd tiieptsgnt giglalaaav rgyrciivmp ekmssekvdv
      181 lralgaeivr tptnarfdsp eshvgvawrl kneipnshil dqyrnasnpl ahydttadei
      241 lqqcdgkldm lvasvgtggt itgiarklke kcpgcriigv dpegsilaep eelnqteqtt
      301 yevegigydf iptvldrtvv dkwfksndee aftfarmlia qegllcggsa gstvavavka
      361 aqelqegqrc vvilpdsvrn ymtkflsdrw mlqkgflkee dltekkpwww hlrvqelgls
      421 apltvlptit cghtieilre kgfdqapvvd eagvilgmvt lgnmlsslla gkvqpsdqvg
      481 kviykqfkqi rltdtlgrls hilemdhfal vvheqiqyhs tgkssqrqmv fgvvtaidll
      541 nfvaaqerdq k
//
LOCUS       NP_001308002             551 aa            linear   PRI 20-JAN-2026
DEFINITION  cystathionine beta-synthase isoform a [Homo sapiens].
ACCESSION   NP_001308002 XP_011544402
VERSION     NP_001308002.1
DBSOURCE    REFSEQ: accession NM_001321073.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Kumar,A., Wissbrock,A., Goradia,N., Bellstedt,P., Ramachandran,R.,
            Imhof,D. and Ohlenschlager,O.
  TITLE     Heme interaction of the intrinsically disordered N-terminal peptide
            segment of human cystathionine-beta-synthase
  JOURNAL   Sci Rep 8 (1), 2474 (2018)
   PUBMED   29410458
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Kabil,O., Zhou,Y. and Banerjee,R.
  TITLE     Human cystathionine beta-synthase is a target for sumoylation
  JOURNAL   Biochemistry 45 (45), 13528-13536 (2006)
   PUBMED   17087506
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Hu,Y.H., Warnatz,H.J., Vanhecke,D., Wagner,F., Fiebitz,A.,
            Thamm,S., Kahlem,P., Lehrach,H., Yaspo,M.L. and Janitz,M.
  TITLE     Cell array-based intracellular localization screening reveals novel
            functional features of human chromosome 21 proteins
  JOURNAL   BMC Genomics 7, 155 (2006)
   PUBMED   16780588
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Chen,X., Jhee,K.H. and Kruger,W.D.
  TITLE     Production of the neuromodulator H2S by cystathionine beta-synthase
            via the condensation of cysteine and homocysteine
  JOURNAL   J Biol Chem 279 (50), 52082-52086 (2004)
   PUBMED   15520012
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Meier,M., Janosik,M., Kery,V., Kraus,J.P. and Burkhard,P.
  TITLE     Structure of human cystathionine beta-synthase: a unique pyridoxal
            5'-phosphate-dependent heme protein
  JOURNAL   EMBO J 20 (15), 3910-3916 (2001)
   PUBMED   11483494
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Kery,V., Bukovska,G. and Kraus,J.P.
  TITLE     Transsulfuration depends on heme in addition to pyridoxal
            5'-phosphate. Cystathionine beta-synthase is a heme protein
  JOURNAL   J Biol Chem 269 (41), 25283-25288 (1994)
   PUBMED   7929220
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FP236240.8 and BC007257.1.
            
            On Mar 18, 2016 this sequence version replaced XP_011544402.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments. NM_001321073
            is annotated on a scaffold that is thought to be a false
            duplication and thus this accession is likely redundant with
            NM_001178009.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC007257.1, SRR1803615.37309.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21p12"
     Protein         1..551
                     /product="cystathionine beta-synthase isoform a"
                     /EC_number="4.2.1.22"
                     /note="cystathionine beta-synthase-like protein"
                     /calculated_mol_wt=60456
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35520.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     Region          76..544
                     /region_name="cysta_beta"
                     /note="cystathionine beta-synthase; TIGR01137"
                     /db_xref="CDD:273464"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     CDS             1..551
                     /gene="LOC102724560"
                     /gene_synonym="CBSL"
                     /coded_by="NM_001321073.3:292..1947"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:102724560"
ORIGIN      
        1 mpsetpqaev gptgcphrsg phsakgslek gspedkeake plwirpdaps rctwqlgrpa
       61 sesphhhtap akspkilpdi lkkigdtpmv rinkigkkfg lkcellakce ffnaggsvkd
      121 rislrmieda erdgtlkpgd tiieptsgnt giglalaaav rgyrciivmp ekmssekvdv
      181 lralgaeivr tptnarfdsp eshvgvawrl kneipnshil dqyrnasnpl ahydttadei
      241 lqqcdgkldm lvasvgtggt itgiarklke kcpgcriigv dpegsilaep eelnqteqtt
      301 yevegigydf iptvldrtvv dkwfksndee aftfarmlia qegllcggsa gstvavavka
      361 aqelqegqrc vvilpdsvrn ymtkflsdrw mlqkgflkee dltekkpwww hlrvqelgls
      421 apltvlptit cghtieilre kgfdqapvvd eagvilgmvt lgnmlsslla gkvqpsdqvg
      481 kviykqfkqi rltdtlgrls hilemdhfal vvheqiqyhs tgkssqrqmv fgvvtaidll
      541 nfvaaqerdq k
//
LOCUS       NP_001352234              91 aa            linear   PRI 20-JAN-2026
DEFINITION  uncharacterized protein LOC112694756 isoform 2 [Homo sapiens].
ACCESSION   NP_001352234
VERSION     NP_001352234.1
DBSOURCE    REFSEQ: accession NM_001365305.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Kimura,K., Wakamatsu,A., Suzuki,Y., Ota,T., Nishikawa,T.,
            Yamashita,R., Yamamoto,J., Sekine,M., Tsuritani,K., Wakaguri,H.,
            Ishii,S., Sugiyama,T., Saito,K., Isono,Y., Irie,R., Kushida,N.,
            Yoneyama,T., Otsuka,R., Kanda,K., Yokoi,T., Kondo,H., Wagatsuma,M.,
            Murakawa,K., Ishida,S., Ishibashi,T., Takahashi-Fujii,A.,
            Tanase,T., Nagai,K., Kikuchi,H., Nakai,K., Isogai,T. and Sugano,S.
  TITLE     Diversification of transcriptional modulation: large-scale
            identification and characterization of putative alternative
            promoters of human genes
  JOURNAL   Genome Res 16 (1), 55-65 (2006)
   PUBMED   16344560
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G.,
            Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D.,
            Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K.,
            Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F.,
            Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L.,
            Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L.,
            Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S.,
            Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J.,
            Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J.,
            McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S.,
            Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W.,
            Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A.,
            Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S.,
            Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y.,
            Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D.,
            Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M.,
            Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E.,
            Schnerch,A., Schein,J.E., Jones,S.J. and Marra,M.A.
  CONSRTM   Mammalian Gene Collection Program Team
  TITLE     Generation and initial analysis of more than 15,000 full-length
            human and mouse cDNA sequences
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16899-16903 (2002)
   PUBMED   12477932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093512.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK098778.1, SRR1803611.176115.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145893, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: translation inferred from conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..91
                     /product="uncharacterized protein LOC112694756 isoform 2"
                     /calculated_mol_wt=9663
     Region          38..>83
                     /region_name="2A060601"
                     /note="Niemann-Pick C type protein family; TIGR00917"
                     /db_xref="CDD:273337"
     CDS             1..91
                     /gene="LOC112694756"
                     /coded_by="NM_001365305.2:344..619"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS92137.1"
                     /db_xref="GeneID:112694756"
ORIGIN      
        1 mdaqgccadg sspcrkqgss gppdccwtca eacnfplpsp ahfldaccpq ptradwaprc
       61 prccplcdca ctcqlpdcqs lnclcfeikl r
//
LOCUS       NP_001300979             173 aa            linear   PRI 20-JAN-2026
DEFINITION  alpha-crystallin A2 chain isoform 1 [Homo sapiens].
ACCESSION   NP_001300979 XP_006723993 XP_006726864
VERSION     NP_001300979.1
DBSOURCE    REFSEQ: accession NM_001314050.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Yuan,L., Yao,H., Xu,Y., Chen,M., Deng,J., Song,Y., Sui,T., Wang,Y.,
            Huang,Y., Li,Z. and Lai,L.
  TITLE     CRISPR/Cas9-Mediated Mutation of alphaA-Crystallin Gene Induces
            Congenital Cataracts in Rabbits
  JOURNAL   Invest Ophthalmol Vis Sci 58 (6), BIO34-BIO41 (2017)
   PUBMED   28475701
  REMARK    GeneRIF: CRISPR/Cas9-mediated mutation of the alphaA-crystallin
            gene in rabbits recapitulates phenotypes of congenital cataracts,
            microphthalmia, obscurity, and early atrophy of the lens, and
            failed differentiation of lens fibers.
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Ray,S., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human retina for the NEIBank
            Project: retbindin, an abundant, novel retinal cDNA and alternative
            splicing of other retina-preferred gene transcripts
  JOURNAL   Mol Vis 8, 196-204 (2002)
   PUBMED   12107411
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FP236240.8.
            
            On or before Sep 29, 2015 this sequence version replaced
            XP_006723993.1, XP_006726864.1.
            
            Sequence Note: NM_001314050 is annotated on a scaffold that is
            thought to be a false duplication and thus this accession is likely
            redundant with NM_000394.
            
            ##Evidence-Data-START##
            CDS exon combination :: KM220589.1, ERR279875.6795.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1968540,
                                    SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21p12"
     Protein         1..173
                     /product="alpha-crystallin A2 chain isoform 1"
                     /note="alpha-crystallin A2 chain"
                     /calculated_mol_wt=19778
     Region          1..54
                     /region_name="Crystallin"
                     /note="Alpha crystallin A chain, N terminal; pfam00525"
                     /db_xref="CDD:425732"
     Region          60..145
                     /region_name="ACD_alphaA-crystallin_HspB4"
                     /note="Alpha-crystallin domain found in the small heat
                     shock protein (sHsp) alphaA-crystallin (HspB4, 20kDa).
                     sHsps are molecular chaperones that suppress protein
                     aggregation and protect against cell stress, and are
                     generally active as large oligomers...; cd06497"
                     /db_xref="CDD:107245"
     Site            order(64..68,74,76,78..79,116,137..138)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:107245"
     CDS             1..173
                     /gene="LOC102724652"
                     /gene_synonym="CRYAA2"
                     /coded_by="NM_001314050.5:1458..1979"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:102724652"
ORIGIN      
        1 mdvtiqhpwf krtlgpfyps rlfdqffgeg lfeydllpfl sstispyyrq slfrtvldsg
       61 isevrsdrdk fvifldvkhf spedltvkvq ddfveihgkh nerqddhgyi srefhrryrl
      121 psnvdqsals cslsadgmlt fcgpkiqtgl dathaeraip vsreekptsa pss
//
LOCUS       NP_001243142            1024 aa            linear   PRI 20-JAN-2026
DEFINITION  sodium/potassium-transporting ATPase subunit alpha-3 isoform 2
            [Homo sapiens].
ACCESSION   NP_001243142
VERSION     NP_001243142.1
DBSOURCE    REFSEQ: accession NM_001256213.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Depierre,P., Ginet,V., Truttmann,A.C. and Puyal,J.
  TITLE     Neuronal autosis is Na+/K+-ATPase alpha 3-dependent and involved in
            hypoxic-ischemic neuronal death
  JOURNAL   Cell Death Dis 15 (5), 363 (2024)
   PUBMED   38796484
  REMARK    GeneRIF: Neuronal autosis is Na[+]/K[+]-ATPase alpha 3-dependent
            and involved in hypoxic-ischemic neuronal death.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Muthaffar,O.Y., Alqarni,A., Shafei,J.A., Bahowarth,S.Y.,
            Alyazidi,A.S. and Naseer,M.I.
  TITLE     Childhood-related neural genotype-phenotype in ATP1A3 mutations:
            comprehensive analysis
  JOURNAL   Genes Genomics 46 (4), 475-487 (2024)
   PUBMED   38243045
  REMARK    GeneRIF: Childhood-related neural genotype-phenotype in ATP1A3
            mutations: comprehensive analysis.
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   You,Y., Zhang,Z., Sultana,N., Ericsson,M., Martens,Y.A., Sun,M.,
            Kanekiyo,T., Ikezu,S., Shaffer,S.A. and Ikezu,T.
  TITLE     ATP1A3 as a target for isolating neuron-specific extracellular
            vesicles from human brain and biofluids
  JOURNAL   Sci Adv 9 (37), eadi3647 (2023)
   PUBMED   37713494
  REMARK    GeneRIF: ATP1A3 as a target for isolating neuron-specific
            extracellular vesicles from human brain and biofluids.
REFERENCE   4  (residues 1 to 1024)
  AUTHORS   Alyamani,S.A., Aldhalaan,H.M., Almuhaizea,M.A. and Abukhalid,M.F.
  TITLE     Expanding the Allelic spectrum in ATP1A3-related disorders with 3
            novel mutations and clinic features
  JOURNAL   Neurosciences (Riyadh) 28 (3), 195-198 (2023)
   PUBMED   37482377
  REMARK    GeneRIF: Expanding the Allelic spectrum in ATP1A3-related disorders
            with 3 novel mutations and clinic features.
REFERENCE   5  (residues 1 to 1024)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   6  (residues 1 to 1024)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
REFERENCE   7  (residues 1 to 1024)
  AUTHORS   Brashear,A., Sweadner,K.J., Haq,I., Napoli,E. and Ozelius,L.
  TITLE     ATP1A3-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301294
REFERENCE   8  (residues 1 to 1024)
  AUTHORS   Lingrel,J.B., Orlowski,J., Shull,M.M. and Price,E.M.
  TITLE     Molecular genetics of Na,K-ATPase
  JOURNAL   Prog Nucleic Acid Res Mol Biol 38, 37-89 (1990)
   PUBMED   2158121
  REMARK    Review article
REFERENCE   9  (residues 1 to 1024)
  AUTHORS   Ovchinnikov,Yu.A., Monastyrskaya,G.S., Broude,N.E.,
            Ushkaryov,Yu.A., Melkov,A.M., Smirnov,Yu.V., Malyshev,I.V.,
            Allikmets,R.L., Kostina,M.B., Dulubova,I.E. et al.
  TITLE     Family of human Na+, K+-ATPase genes. Structure of the gene for the
            catalytic subunit (alpha III-form) and its relationship with
            structural features of the protein
  JOURNAL   FEBS Lett 233 (1), 87-94 (1988)
   PUBMED   2838329
REFERENCE   10 (residues 1 to 1024)
  AUTHORS   Sverdlov,E.D., Monastyrskaia,G.S., Broude,N.E., Ushkarev,Iu.A. and
            Melkov,A.M.
  TITLE     [The family of human Na+,K+-ATPase genes. Structure of the gene for
            isozyme alphaII]
  JOURNAL   Dokl Akad Nauk SSSR 297 (6), 1488-1494 (1987)
   PUBMED   2834163
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK296557.1, AK223569.1,
            AK295078.1 and BC009282.2.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type cation transport ATPases, and to the subfamily of Na+/K+
            -ATPases. Na+/K+ -ATPase is an integral membrane protein
            responsible for establishing and maintaining the electrochemical
            gradients of Na and K ions across the plasma membrane. These
            gradients are essential for osmoregulation, for sodium-coupled
            transport of a variety of organic and inorganic molecules, and for
            electrical excitability of nerve and muscle. This enzyme is
            composed of two subunits, a large catalytic subunit (alpha) and a
            smaller glycoprotein subunit (beta). The catalytic subunit of
            Na+/K+ -ATPase is encoded by multiple genes. This gene encodes an
            alpha 3 subunit. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jan 2012].
            
            Transcript Variant: This variant (2) has an alternate 5' exon,
            compared to variant 1. The resulting isoform (2) has a different
            and longer N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296557.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..1024
                     /product="sodium/potassium-transporting ATPase subunit
                     alpha-3 isoform 2"
                     /EC_number="7.2.2.13"
                     /note="sodium-potassium-ATPase, alpha 3 polypeptide;
                     Na+/K+ ATPase 3; sodium/potassium-transporting ATPase
                     alpha-3 chain; sodium/potassium-transporting ATPase
                     subunit alpha-3; sodium pump subunit alpha-3; Na(+)/K(+)
                     ATPase alpha-3 subunit; Na(+)/K(+) ATPase alpha(III)
                     subunit; sodium-potassium ATPase catalytic subunit
                     alpha-3; ATPase, Na+/K+ transporting, alpha 3 polypeptide;
                     Na+, K+ activated adenosine triphosphatase alpha subunit"
                     /calculated_mol_wt=113003
     Region          28..1024
                     /region_name="ATPase-IIC_X-K"
                     /note="sodium or proton efflux -- potassium uptake
                     antiporter, P-type ATPase, alpha subunit; TIGR01106"
                     /db_xref="CDD:273445"
     CDS             1..1024
                     /gene="ATP1A3"
                     /gene_synonym="AHC2; CAPOS; DEE99; DYT12; RDP"
                     /coded_by="NM_001256213.2:37..3111"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58663.1"
                     /db_xref="GeneID:478"
                     /db_xref="HGNC:HGNC:801"
                     /db_xref="MIM:182350"
ORIGIN      
        1 mggweeernr ratdkkddkd spkknkgker rdlddlkkev amtehkmsve evcrkyntdc
       61 vqglthskaq eilardgpna ltpppttpew vkfcrqlfgg fsillwigai lcflaygiqa
      121 gteddpsgdn lylgivlaav viitgcfsyy qeaksskime sfknmvpqqa lviregekmq
      181 vnaeevvvgd lveikggdrv padlriisah gckvdnsslt gesepqtrsp dcthdnplet
      241 rnitffstnc vegtargvvv atgdrtvmgr iatlasglev gktpiaieie hfiqlitgva
      301 vflgvsffil slilgytwle avifligiiv anvpegllat vtvcltltak rmarknclvk
      361 nleavetlgs tsticsdktg tltqnrmtva hmwfdnqihe adttedqsgt sfdksshtwv
      421 alshiaglcn ravfkggqdn ipvlkrdvag dasesallkc ielssgsvkl mrernkkvae
      481 ipfnstnkyq lsihetedpn dnryllvmkg aperildrcs tillqgkeqp ldeemkeafq
      541 naylelgglg ervlgfchyy lpeeqfpkgf afdcddvnft tdnlcfvglm smidppraav
      601 pdavgkcrsa gikvimvtgd hpitakaiak gvgiisegne tvediaarln ipvsqvnprd
      661 akacvihgtd lkdftseqid eilqnhteiv fartspqqkl iivegcqrqg aivavtgdgv
      721 ndspalkkad igvamgiags dvskqaadmi llddnfasiv tgveegrlif dnlkksiayt
      781 ltsnipeitp fllfimanip lplgtitilc idlgtdmvpa islayeaaes dimkrqprnp
      841 rtdklvnerl ismaygqigm iqalggffsy fvilaengfl pgnlvgirln wddrtvndle
      901 dsygqqwtye qrkvveftch taffvsivvv qwadliickt rrnsvfqqgm knkilifglf
      961 eetalaafls ycpgmdvalr myplkpswwf cafpysflif vydeirklil rrnpggwvek
     1021 etyy
//
LOCUS       NP_001340935             551 aa            linear   PRI 20-JAN-2026
DEFINITION  cystathionine beta-synthase isoform a [Homo sapiens].
ACCESSION   NP_001340935 XP_016883704
VERSION     NP_001340935.1
DBSOURCE    REFSEQ: accession NM_001354006.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Kumar,A., Wissbrock,A., Goradia,N., Bellstedt,P., Ramachandran,R.,
            Imhof,D. and Ohlenschlager,O.
  TITLE     Heme interaction of the intrinsically disordered N-terminal peptide
            segment of human cystathionine-beta-synthase
  JOURNAL   Sci Rep 8 (1), 2474 (2018)
   PUBMED   29410458
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Kabil,O., Zhou,Y. and Banerjee,R.
  TITLE     Human cystathionine beta-synthase is a target for sumoylation
  JOURNAL   Biochemistry 45 (45), 13528-13536 (2006)
   PUBMED   17087506
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Hu,Y.H., Warnatz,H.J., Vanhecke,D., Wagner,F., Fiebitz,A.,
            Thamm,S., Kahlem,P., Lehrach,H., Yaspo,M.L. and Janitz,M.
  TITLE     Cell array-based intracellular localization screening reveals novel
            functional features of human chromosome 21 proteins
  JOURNAL   BMC Genomics 7, 155 (2006)
   PUBMED   16780588
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Chen,X., Jhee,K.H. and Kruger,W.D.
  TITLE     Production of the neuromodulator H2S by cystathionine beta-synthase
            via the condensation of cysteine and homocysteine
  JOURNAL   J Biol Chem 279 (50), 52082-52086 (2004)
   PUBMED   15520012
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Meier,M., Janosik,M., Kery,V., Kraus,J.P. and Burkhard,P.
  TITLE     Structure of human cystathionine beta-synthase: a unique pyridoxal
            5'-phosphate-dependent heme protein
  JOURNAL   EMBO J 20 (15), 3910-3916 (2001)
   PUBMED   11483494
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Kery,V., Bukovska,G. and Kraus,J.P.
  TITLE     Transsulfuration depends on heme in addition to pyridoxal
            5'-phosphate. Cystathionine beta-synthase is a heme protein
  JOURNAL   J Biol Chem 269 (41), 25283-25288 (1994)
   PUBMED   7929220
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            FP236240.8.
            
            On Aug 29, 2017 this sequence version replaced XP_016883704.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments. NM_001354006 is annotated on a
            scaffold that is thought to be a false duplication and thus this
            accession is likely redundant with NM_001320298.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.175334.1,
                                           SRR1803613.43391.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21p12"
     Protein         1..551
                     /product="cystathionine beta-synthase isoform a"
                     /EC_number="4.2.1.22"
                     /note="cystathionine beta-synthase-like protein"
                     /calculated_mol_wt=60456
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35520.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     Region          76..544
                     /region_name="cysta_beta"
                     /note="cystathionine beta-synthase; TIGR01137"
                     /db_xref="CDD:273464"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     CDS             1..551
                     /gene="LOC102724560"
                     /gene_synonym="CBSL"
                     /coded_by="NM_001354006.1:329..1984"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:102724560"
ORIGIN      
        1 mpsetpqaev gptgcphrsg phsakgslek gspedkeake plwirpdaps rctwqlgrpa
       61 sesphhhtap akspkilpdi lkkigdtpmv rinkigkkfg lkcellakce ffnaggsvkd
      121 rislrmieda erdgtlkpgd tiieptsgnt giglalaaav rgyrciivmp ekmssekvdv
      181 lralgaeivr tptnarfdsp eshvgvawrl kneipnshil dqyrnasnpl ahydttadei
      241 lqqcdgkldm lvasvgtggt itgiarklke kcpgcriigv dpegsilaep eelnqteqtt
      301 yevegigydf iptvldrtvv dkwfksndee aftfarmlia qegllcggsa gstvavavka
      361 aqelqegqrc vvilpdsvrn ymtkflsdrw mlqkgflkee dltekkpwww hlrvqelgls
      421 apltvlptit cghtieilre kgfdqapvvd eagvilgmvt lgnmlsslla gkvqpsdqvg
      481 kviykqfkqi rltdtlgrls hilemdhfal vvheqiqyhs tgkssqrqmv fgvvtaidll
      541 nfvaaqerdq k
//
LOCUS       NP_002771                419 aa            linear   PRI 20-JAN-2026
DEFINITION  pregnancy-specific beta-1-glycoprotein 4 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_002771
VERSION     NP_002771.2
DBSOURCE    REFSEQ: accession NM_002780.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Shanley,D.K., Kiely,P.A., Golla,K., Allen,S., Martin,K.,
            O'Riordan,R.T., Ball,M., Aplin,J.D., Singer,B.B., Caplice,N.,
            Moran,N. and Moore,T.
  TITLE     Pregnancy-specific glycoproteins bind integrin alphaIIbbeta3 and
            inhibit the platelet-fibrinogen interaction
  JOURNAL   PLoS One 8 (2), e57491 (2013)
   PUBMED   23469002
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Kimoto,Y.
  TITLE     A single human cell expresses all messenger ribonucleic acids: the
            arrow of time in a cell
  JOURNAL   Mol Gen Genet 258 (3), 233-239 (1998)
   PUBMED   9645429
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Teglund,S., Olsen,A., Khan,W.N., Frangsmyr,L. and Hammarstrom,S.
  TITLE     The pregnancy-specific glycoprotein (PSG) gene cluster on human
            chromosome 19: fine structure of the 11 PSG genes and
            identification of 6 new genes forming a third subgroup within the
            carcinoembryonic antigen (CEA) family
  JOURNAL   Genomics 23 (3), 669-684 (1994)
   PUBMED   7851896
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Olsen,A., Teglund,S., Nelson,D., Gordon,L., Copeland,A.,
            Georgescu,A., Carrano,A. and Hammarstrom,S.
  TITLE     Gene organization of the pregnancy-specific glycoprotein region on
            human chromosome 19: assembly and analysis of a 700-kb cosmid
            contig spanning the region
  JOURNAL   Genomics 23 (3), 659-668 (1994)
   PUBMED   7851895
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Pan,C.J., Chamberlin,M.E., Wu,S.M., Chan,W.Y. and Chou,J.Y.
  TITLE     Pregnancy-specific glycoprotein gene expression and the induction
            by 5-bromo-2'-deoxyuridine
  JOURNAL   Biochemistry 33 (23), 7260-7266 (1994)
   PUBMED   8003489
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Chan,W.Y., Zheng,Q.X., McMahon,J. and Tease,L.A.
  TITLE     Characterization of new members of the pregnancy-specific beta
            1-glycoprotein family
  JOURNAL   Mol Cell Biochem 106 (2), 161-170 (1991)
   PUBMED   1922019
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Barnett,T.R., Pickle,W. 2nd and Elting,J.J.
  TITLE     Characterization of two new members of the pregnancy-specific beta
            1-glycoprotein family from the myeloid cell line KG-1 and
            suggestion of two distinct classes of transcription unit
  JOURNAL   Biochemistry 29 (44), 10213-10218 (1990)
   PUBMED   2271648
REFERENCE   8  (residues 1 to 419)
  AUTHORS   .
  TITLE     The human pregnancy-specific glycoprotein genes are tightly linked
            on the long arm of chromosome 19 and are coordinately expressed
  JOURNAL   Biochem Biophys Res Commun 168 (3), 1325 (1990)
   PUBMED   2346490
REFERENCE   9  (residues 1 to 419)
  AUTHORS   Thompson,J., Koumari,R., Wagner,K., Barnert,S., Schleussner,C.,
            Schrewe,H., Zimmermann,W., Muller,G., Schempp,W., Zaninetta,D. et
            al.
  TITLE     The human pregnancy-specific glycoprotein genes are tightly linked
            on the long arm of chromosome 19 and are coordinately expressed
  JOURNAL   Biochem Biophys Res Commun 167 (2), 848-859 (1990)
   PUBMED   1690992
  REMARK    Erratum:[Biochem Biophys Res Commun 1990 May 16;168(3):1325]
REFERENCE   10 (residues 1 to 419)
  AUTHORS   Thompson,J.A., Mauch,E.M., Chen,F.S., Hinoda,Y., Schrewe,H.,
            Berling,B., Barnert,S., von Kleist,S., Shively,J.E. and
            Zimmermann,W.
  TITLE     Analysis of the size of the carcinoembryonic antigen (CEA) gene
            family: isolation and sequencing of N-terminal domain exons
  JOURNAL   Biochem Biophys Res Commun 158 (3), 996-1004 (1989)
   PUBMED   2537643
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005392.2, BC013431.1 and
            BC008405.1.
            
            On Feb 17, 2004 this sequence version replaced NP_002771.1.
            
            Summary: The protein encoded by this gene is a pregnancy-specific
            glycoprotein (PSG), one of several encoded by a cluster of similar
            genes on chromosome 19. This gene is a member of the
            carcinoembryonic antigen (CEA) gene family and may play a role in
            regulation of the innate immune system. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC063127.1, BC013431.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2142853,
                                           SAMEA2149398 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000405312.8/ ENSP00000384770.3
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..419
                     /product="pregnancy-specific beta-1-glycoprotein 4 isoform
                     1 precursor"
                     /note="Pregnancy-specific beta-1-glycoprotein-4;
                     PS-beta-G-4; pregnancy-specific glycoprotein 4"
                     /calculated_mol_wt=43448
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3683
     Region          36..138
                     /region_name="IgV_CEACAM_D1"
                     /note="First immunoglobulin (Ig)-like domain of
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM); cd05774"
                     /db_xref="CDD:409430"
     Region          37..55
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          37..39
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409430"
     Region          44..46
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409430"
     Region          49..56
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409430"
     Region          56..63
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..69
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..68
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409430"
     Region          70..91
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          78..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          88..91
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..124
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..103
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409430"
     Region          105..109
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409430"
     Region          119..124
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409430"
     Region          125..132
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          133..138
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409430"
     Region          148..236
                     /region_name="IgI_hCEACAM_2_4_6_like"
                     /note="Immunoglobulin (Ig)-like domain of human
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM) domains 2, 4, and 6, and similar
                     domains; cd05740"
                     /db_xref="CDD:409402"
     Region          148..152
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409402"
     Region          155..160
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409402"
     Region          165..171
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409402"
     Region          178..183
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409402"
     Region          185..188
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409402"
     Region          192..196
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409402"
     Region          199..204
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409402"
     Region          214..222
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409402"
     Region          226..235
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409402"
     Region          241..329
                     /region_name="IgI_hCEACAM_2_4_6_like"
                     /note="Immunoglobulin (Ig)-like domain of human
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM) domains 2, 4, and 6, and similar
                     domains; cd05740"
                     /db_xref="CDD:409402"
     Region          241..245
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409402"
     Region          248..253
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409402"
     Region          258..264
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409402"
     Region          271..276
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409402"
     Region          278..281
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409402"
     Region          285..289
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409402"
     Region          292..297
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409402"
     Region          307..315
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409402"
     Region          319..328
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409402"
     Region          338..413
                     /region_name="IgC2_CEACAM5-like"
                     /note="Fifth immunoglobulin (Ig)-like domain of the
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule 5 (CEACAM5) and similar domains; member of the
                     C2-set IgSF domains; cd20948"
                     /db_xref="CDD:409540"
     Region          338..344
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409540"
     Region          349..356
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409540"
     Region          362..368
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409540"
     Region          371..376
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409540"
     Region          379..385
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409540"
     Region          388..399
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409540"
     Region          402..413
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409540"
     CDS             1..419
                     /gene="PSG4"
                     /gene_synonym="PSBG-4"
                     /coded_by="NM_002780.5:103..1362"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS46093.1"
                     /db_xref="GeneID:5672"
                     /db_xref="HGNC:HGNC:9521"
                     /db_xref="MIM:176393"
ORIGIN      
        1 mgplsappct qritwkgvll tasllnfwnp pttaqvtiea qppkvsegkd vlllvhnlpq
       61 nlagyiwykg qmtylyhyit syvvdgqrii ygpaysgrer vysnaslliq nvtqedagsy
      121 tlhiikrrdg tggvtghftf tlhletpkps isssnlnpre ameaviltcd patpaasyqw
      181 wmngqslpmt hrlqlsktnr tlfifgvtky iagpyeceir npvsasrsdp vtlnllpkls
      241 kpyitinnln prenkdvltf tcepksknyt yiwwlngqsl pvsprvkrpi enrililpnv
      301 trnetgpyqc eirdryggir sdpvtlnvly gpdlpsiyps ftyyrsgenl ylscfaesnp
      361 raqyswting kfqlsgqkls ipqittkhsg lyacsvrnsa tgkessksit vkvsdwilp
//
LOCUS       NP_001006120             496 aa            linear   PRI 20-JAN-2026
DEFINITION  RNA-binding motif protein, Y chromosome, family 1 member D isoform
            1 [Homo sapiens].
ACCESSION   NP_001006120
VERSION     NP_001006120.2
DBSOURCE    REFSEQ: accession NM_001006120.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Tsuei,D.J., Hsu,H.C., Lee,P.H., Jeng,Y.M., Pu,Y.S., Chen,C.N.,
            Lee,Y.C., Chou,W.C., Chang,C.J., Ni,Y.H. and Chang,M.H.
  TITLE     RBMY, a male germ cell-specific RNA-binding protein, activated in
            human liver cancers and transforms rodent fibroblasts
  JOURNAL   Oncogene 23 (34), 5815-5822 (2004)
   PUBMED   15184870
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Skaletsky,H., Kuroda-Kawaguchi,T., Minx,P.J., Cordum,H.S.,
            Hillier,L., Brown,L.G., Repping,S., Pyntikova,T., Ali,J., Bieri,T.,
            Chinwalla,A., Delehaunty,A., Delehaunty,K., Du,H., Fewell,G.,
            Fulton,L., Fulton,R., Graves,T., Hou,S.F., Latrielle,P.,
            Leonard,S., Mardis,E., Maupin,R., McPherson,J., Miner,T., Nash,W.,
            Nguyen,C., Ozersky,P., Pepin,K., Rock,S., Rohlfing,T., Scott,K.,
            Schultz,B., Strong,C., Tin-Wollam,A., Yang,S.P., Waterston,R.H.,
            Wilson,R.K., Rozen,S. and Page,D.C.
  TITLE     The male-specific region of the human Y chromosome is a mosaic of
            discrete sequence classes
  JOURNAL   Nature 423 (6942), 825-837 (2003)
   PUBMED   12815422
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Chai,N.N., Zhou,H., Hernandez,J., Najmabadi,H., Bhasin,S. and
            Yen,P.H.
  TITLE     Structure and organization of the RBMY genes on the human Y
            chromosome: transposition and amplification of an ancestral
            autosomal hnRNPG gene
  JOURNAL   Genomics 49 (2), 283-289 (1998)
   PUBMED   9598316
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Prosser,J., Inglis,J.D., Condie,A., Ma,K., Kerr,S., Thakrar,R.,
            Taylor,K., Cameron,J.M. and Cooke,H.J.
  TITLE     Degeneracy in human multicopy RBM (YRRM), a candidate
            spermatogenesis gene
  JOURNAL   Mamm Genome 7 (11), 835-842 (1996)
   PUBMED   8875892
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Ma,K., Inglis,J.D., Sharkey,A., Bickmore,W.A., Hill,R.E.,
            Prosser,E.J., Speed,R.M., Thomson,E.J., Jobling,M., Taylor,K. et
            al.
  TITLE     A Y chromosome gene family with RNA-binding protein homology:
            candidates for the azoospermia factor AZF controlling human
            spermatogenesis
  JOURNAL   Cell 75 (7), 1287-1295 (1993)
   PUBMED   8269511
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007322.4.
            
            On Nov 26, 2004 this sequence version replaced NP_001006120.1.
            
            Summary: This gene encodes a protein containing an RNA-binding
            motif in the N-terminus and four SRGY (serine, arginine, glycine,
            tyrosine) boxes in the C-terminus. This protein likely functions as
            a splicing factor during spermatogenesis. Multiple closely related
            paralogs of this gene are found in a gene cluster in the AZFb
            azoospermia factor region of chromosome Y. Most of these related
            copies are thought to be pseudogenes, though several likely encode
            functional proteins. [provided by RefSeq, Mar 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.134962.1,
                                           SRR5189667.274280.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA1970526 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000382680.5/ ENSP00000372127.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="Y"
                     /map="Yq11.223"
     Protein         1..496
                     /product="RNA-binding motif protein, Y chromosome, family
                     1 member D isoform 1"
                     /note="RNA-binding motif protein, Y chromosome, family 1
                     member D; RNA-binding motif protein 1; RNA-binding motif
                     protein 2; Y chromosome RNA recognition motif 1"
                     /calculated_mol_wt=55644
     Region          7..85
                     /region_name="RRM_RBMX_like"
                     /note="RNA recognition motif (RRM) found in heterogeneous
                     nuclear ribonucleoprotein G (hnRNP G), Y chromosome RNA
                     recognition motif 1 (hRBMY), testis-specific heterogeneous
                     nuclear ribonucleoprotein G-T (hnRNP G-T) and similar
                     proteins; cd12382"
                     /db_xref="CDD:409816"
     Site            order(9,11,13..17,38,40..43,44..50,52,77,79,81..85)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409816"
     Region          <10..>182
                     /region_name="ELAV_HUD_SF"
                     /note="ELAV/HuD family splicing factor; TIGR01661"
                     /db_xref="CDD:273741"
     Region          67..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C7P1.1)"
     Region          158..>316
                     /region_name="dnaA"
                     /note="chromosomal replication initiator protein DnaA;
                     cl42516"
                     /db_xref="CDD:455861"
     Region          174..218
                     /region_name="RBM1CTR"
                     /note="RBM1CTR (NUC064) family; pfam08081"
                     /db_xref="CDD:400429"
     Region          452..496
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0C7P1.1)"
     CDS             1..496
                     /gene="RBMY1D"
                     /gene_synonym="hRBMY; RBM1; RBM2; YRRM1; YRRM2"
                     /coded_by="NM_001006120.3:153..1643"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS35480.1"
                     /db_xref="GeneID:378949"
                     /db_xref="HGNC:HGNC:23915"
ORIGIN      
        1 mveadhpgkl figglnretn ekmlkavfgk hgpisevlli kdrtsksrgf afitfenpad
       61 aknaakdmng kslhgkaikv eqakkpsfqs ggrrrppass rnrspsgslr sargsrggtr
      121 gwlpsqeghl ddggytpdlk msysrglipv krgpssrsgg pppkksapsa varsnswmgs
      181 qgpmsqrren ygvpprrati sswrndrmst rhdgyatndg nhpscqetrd yappsrgyay
      241 rdnghsnrde hssrgyrnhr ssretrdyap psrghayrdy ghsrrdesys rgyrnrrssr
      301 etreyappsr ghgyrdyghs rrhesysrgy rnhpssretr dyapphrdya yrdyghsswd
      361 ehssrgysyh dgygealgrd hsehlsgssy rdalqrygts hgappargpr msyggstcha
      421 ysntrdrygr swesysscgd fhycdrehvc rkdqrnppsl grvlpdprea cgsssyvasi
      481 vdggesrsek gdssry
//
LOCUS       NP_001287796             785 aa            linear   PRI 20-JAN-2026
DEFINITION  transport and Golgi organization protein 1 homolog isoform 2 [Homo
            sapiens].
ACCESSION   NP_001287796 XP_005273179
VERSION     NP_001287796.1
DBSOURCE    REFSEQ: accession NM_001300867.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 785)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 785)
  AUTHORS   Wanbiao,Z., Jing,M., Shi,Z., Tengxiang,C., Xueke,Z. and Haiyang,L.
  TITLE     MIA3 promotes the degradation of GSH (glutathione) by binding to
            CHAC1, thereby promoting the progression of hepatocellular
            carcinoma
  JOURNAL   Mol Cell Biochem 479 (10), 2769-2784 (2024)
   PUBMED   37948019
  REMARK    GeneRIF: MIA3 promotes the degradation of GSH (glutathione) by
            binding to CHAC1, thereby promoting the progression of
            hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 785)
  AUTHORS   Connolly,L.M., McFalls,C.M., McMahon,I.G., Bhat,A.M. and
            Artlett,C.M.
  TITLE     Caspase 1 Enhances Transport and Golgi Organization Protein 1
            Expression to Promote Procollagen Export From the Endoplasmic
            Reticulum in Systemic Sclerosis Contributing to Fibrosis
  JOURNAL   Arthritis Rheumatol 75 (10), 1831-1841 (2023)
   PUBMED   37067501
  REMARK    GeneRIF: Caspase 1 Enhances Transport and Golgi Organization
            Protein 1 Expression to Promote Procollagen Export From the
            Endoplasmic Reticulum in Systemic Sclerosis Contributing to
            Fibrosis.
REFERENCE   4  (residues 1 to 785)
  AUTHORS   Man,J., Zhou,W., Zuo,S., Zhao,X., Wang,Q., Ma,H. and Li,H.Y.
  TITLE     TANGO1 interacts with NRTN to promote hepatocellular carcinoma
            progression by regulating the PI3K/AKT/mTOR signaling pathway
  JOURNAL   Biochem Pharmacol 213, 115615 (2023)
   PUBMED   37211171
  REMARK    GeneRIF: TANGO1 interacts with NRTN to promote hepatocellular
            carcinoma progression by regulating the PI3K/AKT/mTOR signaling
            pathway.
REFERENCE   5  (residues 1 to 785)
  AUTHORS   Junkiert-Czarnecka,A., Pilarska-Deltow,M., Bak,A., Heise,M. and
            Haus,O.
  TITLE     A novel mutation in collagen transport protein, MIA3 gene, detected
            in a patient with clinical symptoms of Ehlers-Danlos hypermobile
            syndrome
  JOURNAL   Adv Clin Exp Med 32 (7), 777-781 (2023)
   PUBMED   36603143
  REMARK    GeneRIF: A novel mutation in collagen transport protein, MIA3 gene,
            detected in a patient with clinical symptoms of Ehlers-Danlos
            hypermobile syndrome.
REFERENCE   6  (residues 1 to 785)
  AUTHORS   Saito,K., Chen,M., Bard,F., Chen,S., Zhou,H., Woodley,D.,
            Polischuk,R., Schekman,R. and Malhotra,V.
  TITLE     TANGO1 facilitates cargo loading at endoplasmic reticulum exit
            sites
  JOURNAL   Cell 136 (5), 891-902 (2009)
   PUBMED   19269366
REFERENCE   7  (residues 1 to 785)
  AUTHORS   Arndt,S., Melle,C., Mondal,K., Klein,G., von Eggeling,F. and
            Bosserhoff,A.K.
  TITLE     Interactions of TANGO and leukocyte integrin CD11c/CD18 regulate
            the migration of human monocytes
  JOURNAL   J Leukoc Biol 82 (6), 1466-1472 (2007)
   PUBMED   17726152
  REMARK    GeneRIF: The results from this study present TANGO as a novel
            ligand for CD11c, regulating migratory processes of hematopoietic
            cells.
REFERENCE   8  (residues 1 to 785)
  AUTHORS   Arndt,S. and Bosserhoff,A.K.
  TITLE     Reduced expression of TANGO in colon and hepatocellular carcinomas
  JOURNAL   Oncol Rep 18 (4), 885-891 (2007)
   PUBMED   17786351
  REMARK    GeneRIF: Reduced expression of TANGO is associated with colon and
            hepatocellular carcinomas
REFERENCE   9  (residues 1 to 785)
  AUTHORS   Arndt,S. and Bosserhoff,A.K.
  TITLE     TANGO is a tumor suppressor of malignant melanoma
  JOURNAL   Int J Cancer 119 (12), 2812-2820 (2006)
   PUBMED   17044017
  REMARK    GeneRIF: TANGO transfected cell lines revealed that TANGO
            expression reduces motility, whereas reduction of TANGO enhances
            migration.
REFERENCE   10 (residues 1 to 785)
  AUTHORS   Bosserhoff,A.K., Moser,M. and Buettner,R.
  TITLE     Characterization and expression pattern of the novel MIA homolog
            TANGO
  JOURNAL   Gene Expr Patterns 4 (4), 473-479 (2004)
   PUBMED   15183315
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK296712.1, BC047116.1 and AL592148.7.
            
            On Jul 15, 2014 this sequence version replaced XP_005273179.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.233749.1,
                                           SRR14038193.853937.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..785
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..785
                     /product="transport and Golgi organization protein 1
                     homolog isoform 2"
                     /note="C219-reactive peptide; melanoma inhibitory activity
                     protein 3; MIA family member 3, ER export factor; melanoma
                     inhibitory activity family, member 3; transport and Golgi
                     organization protein 1 homolog"
                     /calculated_mol_wt=87307
     Region          <90..469
                     /region_name="Mplasa_alph_rch"
                     /note="helix-rich Mycoplasma protein; TIGR04523"
                     /db_xref="CDD:275316"
     Region          <525..770
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..785
                     /gene="MIA3"
                     /gene_synonym="D320; ODCD2; TANGO; TANGO1; UNQ6077"
                     /coded_by="NM_001300867.2:148..2505"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS73035.1"
                     /db_xref="GeneID:375056"
                     /db_xref="HGNC:HGNC:24008"
                     /db_xref="MIM:613455"
ORIGIN      
        1 mdsvpatvps iaatpgdpel vgplsvlyaa fiakllelva tlpddvqpgp dfyglpwkpv
       61 fitaflgias faiflwrtvl vvkdrvyqvt eqqiseklkt imkentelvq klsnyeqkik
      121 eskkhvqetr kqnmilsdea ikykdkiktl eknqeilddt aknlrvmles ereqnvknqd
      181 lisenkksie klkdvismna sefsevqial neaklseekv ksechrvqee narlkkkkeq
      241 lqqeiedwsk lhaelseqik sfeksqkdle valthkddni naltncitql nllecesese
      301 gqnkggndsd elangevggd rnekmknqik qmmdvsrtqt aisvveedlk llqlklrasv
      361 stkcnledqv kkleddrnsl qaakaglede cktlrqkvei lnelyqqkem alqkklsqee
      421 yerqerehrl saadekavsa aeevktykrr ieemedelqk tersfknqia thekkahenw
      481 lkaraaerai aeekreaanl rhklleltqk mamlqeepvi vkpmpgkpnt qnpprrgpls
      541 qngsfgpspv sggecspplt veppvrplsa tlnrrdmprs efgsvdgplp hprwsaeasg
      601 kpspsdpgsg tatmmnsssr gssptrvlde gkvnmapkgp ppfpgvplms tpmggpvppp
      661 irygpppqlc gpfgprplpp pfgpgmrppl glrefapgvp pgrrdlplhp rgflpghapf
      721 rplgslgpre yfipgtrlpp pthgpqeypp ppavrdllps gsrdepppas qstsqdcsqa
      781 lkqsp
//
LOCUS       NP_001307227             551 aa            linear   PRI 20-JAN-2026
DEFINITION  cystathionine beta-synthase isoform 1 [Homo sapiens].
ACCESSION   NP_001307227
VERSION     NP_001307227.1
DBSOURCE    REFSEQ: accession NM_001320298.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Hu,X.J., Sun,Y., Liu,G.J., Zhang,J., Zhang,L.X. and Peng,Y.H.
  TITLE     Cystathionine-beta-synthase expression correlates with tumour
            progression and adverse prognosis in patients with colon cancer
  JOURNAL   J Int Med Res 52 (9), 3000605241263726 (2024)
   PUBMED   39324183
  REMARK    GeneRIF: Cystathionine-beta-synthase expression correlates with
            tumour progression and adverse prognosis in patients with colon
            cancer.
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Mijatovic,E., Ascencao,K., Szabo,C. and Majtan,T.
  TITLE     Cellular turnover and degradation of the most common missense
            cystathionine beta-synthase variants causing homocystinuria
  JOURNAL   Protein Sci 33 (8), e5123 (2024)
   PUBMED   39041895
  REMARK    GeneRIF: Cellular turnover and degradation of the most common
            missense cystathionine beta-synthase variants causing
            homocystinuria.
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Al-Sadeq,D.W., Conter,C., Thanassoulas,A., Al-Dewik,N.,
            Safieh-Garabedian,B., Martinez-Cruz,L.A., Nasrallah,G.K.,
            Astegno,A. and Nomikos,M.
  TITLE     Biochemical and structural impact of two novel missense mutations
            in cystathionine beta-synthase gene associated with homocystinuria
  JOURNAL   Biochem J 481 (8), 569-585 (2024)
   PUBMED   38563463
  REMARK    GeneRIF: Biochemical and structural impact of two novel missense
            mutations in cystathionine beta-synthase gene associated with
            homocystinuria.
REFERENCE   4  (residues 1 to 551)
  AUTHORS   McCorvie,T.J., Adamoski,D., Machado,R.A.C., Tang,J., Bailey,H.J.,
            Ferreira,D.S.M., Strain-Damerell,C., Basle,A., Ambrosio,A.L.B.,
            Dias,S.M.G. and Yue,W.W.
  TITLE     Architecture and regulation of filamentous human cystathionine
            beta-synthase
  JOURNAL   Nat Commun 15 (1), 2931 (2024)
   PUBMED   38575566
  REMARK    GeneRIF: Architecture and regulation of filamentous human
            cystathionine beta-synthase.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Sacharow,S.J. and Levy,H.L.
  TITLE     Homocystinuria due to Cystathionine Beta-Synthase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301697
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Lohmann,K., Lange,L., Klein,C. and Zech,M.
  TITLE     Monogenic Isolated Dystonia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301334
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Milewicz,D.M. and Cecchi,A.C.
  TITLE     Heritable Thoracic Aortic Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301299
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Kraus,J., Packman,S., Fowler,B. and Rosenberg,L.E.
  TITLE     Purification and properties of cystathionine beta-synthase from
            human liver. Evidence for identical subunits
  JOURNAL   J Biol Chem 253 (18), 6523-6528 (1978)
   PUBMED   681363
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Griffiths,R. and Tudball,N.
  TITLE     The molecular defect in a case of (cystathionine
            beta-synthase)-deficient homocystinuria
  JOURNAL   Eur J Biochem 74 (2), 269-273 (1977)
   PUBMED   404147
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Longhi,R.C., Fleisher,L.D., Tallan,H.H. and Gaull,G.E.
  TITLE     Cystathionine beta-synthase deficiency: a qualitative abnormality
            of the deficient enzyme modified by vitamin B6 therapy
  JOURNAL   Pediatr Res 11 (2), 100-103 (1977)
   PUBMED   840498
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001630.1, AK294608.1,
            DC315340.1 and BC000440.2.
            
            Summary: The protein encoded by this gene acts as a homotetramer to
            catalyze the conversion of homocysteine to cystathionine, the first
            step in the transsulfuration pathway. The encoded protein is
            allosterically activated by adenosyl-methionine and uses pyridoxal
            phosphate as a cofactor. Defects in this gene can cause
            cystathionine beta-synthase deficiency (CBSD), which can lead to
            homocystinuria. This gene is a major contributor to cellular
            hydrogen sulfide production. Multiple alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Feb 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.253511.1,
                                           SRR1803615.233545.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..551
                     /product="cystathionine beta-synthase isoform 1"
                     /EC_number="4.2.1.22"
                     /note="serine sulfhydrase; beta-thionase; methylcysteine
                     synthase"
                     /calculated_mol_wt=60456
     Region          1..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35520.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     Region          76..544
                     /region_name="cysta_beta"
                     /note="cystathionine beta-synthase; TIGR01137"
                     /db_xref="CDD:273464"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35520.2)"
     CDS             1..551
                     /gene="CBS"
                     /gene_synonym="HIP4"
                     /coded_by="NM_001320298.2:259..1914"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS13693.1"
                     /db_xref="GeneID:875"
                     /db_xref="HGNC:HGNC:1550"
                     /db_xref="MIM:613381"
ORIGIN      
        1 mpsetpqaev gptgcphrsg phsakgslek gspedkeake plwirpdaps rctwqlgrpa
       61 sesphhhtap akspkilpdi lkkigdtpmv rinkigkkfg lkcellakce ffnaggsvkd
      121 rislrmieda erdgtlkpgd tiieptsgnt giglalaaav rgyrciivmp ekmssekvdv
      181 lralgaeivr tptnarfdsp eshvgvawrl kneipnshil dqyrnasnpl ahydttadei
      241 lqqcdgkldm lvasvgtggt itgiarklke kcpgcriigv dpegsilaep eelnqteqtt
      301 yevegigydf iptvldrtvv dkwfksndee aftfarmlia qegllcggsa gstvavavka
      361 aqelqegqrc vvilpdsvrn ymtkflsdrw mlqkgflkee dltekkpwww hlrvqelgls
      421 apltvlptit cghtieilre kgfdqapvvd eagvilgmvt lgnmlsslla gkvqpsdqvg
      481 kviykqfkqi rltdtlgrls hilemdhfal vvheqiqyhs tgkssqrqmv fgvvtaidll
      541 nfvaaqerdq k
//
LOCUS       NP_001186285             190 aa            linear   PRI 20-JAN-2026
DEFINITION  RPL17-C18orf32 protein isoform 2 [Homo sapiens].
ACCESSION   NP_001186285
VERSION     NP_001186285.1
DBSOURCE    REFSEQ: accession NM_001199356.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Prakash,T., Sharma,V.K., Adati,N., Ozawa,R., Kumar,N., Nishida,Y.,
            Fujikake,T., Takeda,T. and Taylor,T.D.
  TITLE     Expression of conjoined genes: another mechanism for gene
            regulation in eukaryotes
  JOURNAL   PLoS One 5 (10), e13284 (2010)
   PUBMED   20967262
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC100778.5.
            
            Summary: This locus represents naturally occurring read-through
            transcription between the neighboring RPL17 (ribosomal protein L17)
            and C18orf32 (chromosome 18 open reading frame 32) genes.
            Alternative splicing results in multiple transcript variants. The
            encoded isoforms share sequence identity with the RPL17 protein,
            but they include frameshifted C-terminal regions derived from the
            downstream gene exons. [provided by RefSeq, Dec 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI461805.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            readthrough transcript :: includes exons from GeneID 6139, 497661
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..190
                     /product="RPL17-C18orf32 protein isoform 2"
                     /note="60S ribosomal protein L17; 60S ribosomal protein
                     L23; Large ribosomal subunit protein uL22"
                     /calculated_mol_wt=21939
     Region          <1..137
                     /region_name="PTZ00178"
                     /note="60S ribosomal protein L17; Provisional"
                     /db_xref="CDD:240306"
     CDS             1..190
                     /gene="RPL17-C18orf32"
                     /gene_synonym="PD-1"
                     /coded_by="NM_001199356.2:95..667"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:100526842"
                     /db_xref="HGNC:HGNC:44661"
ORIGIN      
        1 mhirkatkyl kdvtlqkqcv pfrrynggvg rcaqakqwgw tqgrwpkksa efllhmlkna
       61 esnaelkgld vdslviehiq vnkapkmrrr tyrahgrinp ymsspchiem iltekeqivp
      121 kpeeevaqkk klrssslgkw caflvssfqf csgstknsws hiytlwfpps lvvyglrkqy
      181 knpmiqtkak
//
LOCUS       NP_001020332             446 aa            linear   PRI 20-JAN-2026
DEFINITION  cytochrome P450 2D6 isoform 2 [Homo sapiens].
ACCESSION   NP_001020332
VERSION     NP_001020332.2
DBSOURCE    REFSEQ: accession NM_001025161.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Luo,X., Du,J., Zhao,J., Fan,M., Luo,X., Zhao,P., Zheng,P., Mo,L.
            and Li,Y.
  TITLE     Genetic susceptibility and clinical features of CYP2D6 associated
            with systemic lupus erythematosus in a Chinese population
  JOURNAL   Lupus 33 (12), 1328-1335 (2024)
   PUBMED   39287122
  REMARK    GeneRIF: Genetic susceptibility and clinical features of CYP2D6
            associated with systemic lupus erythematosus in a Chinese
            population.
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Datkhile,K.D., More,A.L., Patil,M.N., Gudur,R.A. and Gudur,A.K.
  TITLE     CYP2D6, CYP2E1 Gene Polymorphisms and Gastrointestinal Cancer Risk
            in Rural Maharashtra: A Hospital Based Case-Control Study
  JOURNAL   Asian Pac J Cancer Prev 25 (9), 3059-3065 (2024)
   PUBMED   39342583
  REMARK    GeneRIF: CYP2D6, CYP2E1 Gene Polymorphisms and Gastrointestinal
            Cancer Risk in Rural Maharashtra: A Hospital Based Case-Control
            Study.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Becker,D., Bharatam,P.V. and Gohlke,H.
  TITLE     Molecular Mechanisms Underlying Single Nucleotide
            Polymorphism-Induced Reactivity Decrease in CYP2D6
  JOURNAL   J Chem Inf Model 64 (15), 6026-6040 (2024)
   PUBMED   38994927
  REMARK    GeneRIF: Molecular Mechanisms Underlying Single Nucleotide
            Polymorphism-Induced Reactivity Decrease in CYP2D6.
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Wei,Y.J., Winterstein,A.G., Schmidt,S., Fillingim,R.B.,
            Daniels,M.J., DeKosky,S.T. and Schmidt,S.
  TITLE     Clinical and Adverse Outcomes Associated With Concomitant Use of
            CYP2D6-Metabolized Opioids With Antidepressants in Older Nursing
            Home Residents : A Target Trial Emulation Study
  JOURNAL   Ann Intern Med 177 (8), 1058-1068 (2024)
   PUBMED   39038293
  REMARK    GeneRIF: Clinical and Adverse Outcomes Associated With Concomitant
            Use of CYP2D6-Metabolized Opioids With Antidepressants in Older
            Nursing Home Residents : A Target Trial Emulation Study.
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Li,D., Pain,O., Fabbri,C., Wong,W.L.E., Lo,C.W.H., Ripke,S.,
            Cattaneo,A., Souery,D., Dernovsek,M.Z., Henigsberg,N., Hauser,J.,
            Lewis,G., Mors,O., Perroud,N., Rietschel,M., Uher,R., Maier,W.,
            Baune,B.T., Biernacka,J.M., Bondolfi,G., Domschke,K., Kato,M.,
            Liu,Y.L., Serretti,A., Tsai,S.J., Weinshilboum,R., McIntosh,A.M.
            and Lewis,C.M.
  CONSRTM   GSRD Consortium, the Major Depressive Disorder Working Group of the
            Psychiatric Genomics Consortium
  TITLE     Metabolic activity of CYP2C19 and CYP2D6 on antidepressant response
            from 13 clinical studies using genotype imputation: a meta-analysis
  JOURNAL   Transl Psychiatry 14 (1), 296 (2024)
   PUBMED   39025838
  REMARK    GeneRIF: Metabolic activity of CYP2C19 and CYP2D6 on antidepressant
            response from 13 clinical studies using genotype imputation: a
            meta-analysis.
            Erratum:[Transl Psychiatry. 2024 Aug 31;14(1):350. doi:
            10.1038/s41398-024-03064-x. PMID: 39217139]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Nelson,D.R., Zeldin,D.C., Hoffman,S.M., Maltais,L.J., Wain,H.M. and
            Nebert,D.W.
  TITLE     Comparison of cytochrome P450 (CYP) genes from the mouse and human
            genomes, including nomenclature recommendations for genes,
            pseudogenes and alternative-splice variants
  JOURNAL   Pharmacogenetics 14 (1), 1-18 (2004)
   PUBMED   15128046
  REMARK    Review article
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Tyndale,R., Aoyama,T., Broly,F., Matsunaga,T., Inaba,T., Kalow,W.,
            Gelboin,H.V., Meyer,U.A. and Gonzalez,F.J.
  TITLE     Identification of a new variant CYP2D6 allele lacking the codon
            encoding Lys-281: possible association with the poor metabolizer
            phenotype
  JOURNAL   Pharmacogenetics 1 (1), 26-32 (1991)
   PUBMED   1844820
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Gaedigk,A., Blum,M., Gaedigk,R., Eichelbaum,M. and Meyer,U.A.
  TITLE     Deletion of the entire cytochrome P450 CYP2D6 gene as a cause of
            impaired drug metabolism in poor metabolizers of the
            debrisoquine/sparteine polymorphism
  JOURNAL   Am J Hum Genet 48 (5), 943-950 (1991)
   PUBMED   1673290
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Hanioka,N., Kimura,S., Meyer,U.A. and Gonzalez,F.J.
  TITLE     The human CYP2D locus associated with a common genetic defect in
            drug oxidation: a G1934----A base change in intron 3 of a mutant
            CYP2D6 allele results in an aberrant 3' splice recognition site
  JOURNAL   Am J Hum Genet 47 (6), 994-1001 (1990)
   PUBMED   1978565
REFERENCE   10 (residues 1 to 446)
  AUTHORS   Gough,A.C., Miles,J.S., Spurr,N.K., Moss,J.E., Gaedigk,A.,
            Eichelbaum,M. and Wolf,C.R.
  TITLE     Identification of the primary gene defect at the cytochrome P450
            CYP2D locus
  JOURNAL   Nature 347 (6295), 773-776 (1990)
   PUBMED   1978251
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB124853.1, BC066877.1,
            BC075023.2 and AY663390.1.
            
            On Jun 22, 2012 this sequence version replaced NP_001020332.1.
            
            Summary: This gene encodes a member of the cytochrome P450
            superfamily of enzymes. The cytochrome P450 proteins are
            monooxygenases which catalyze many reactions involved in drug
            metabolism and synthesis of cholesterol, steroids and other lipids.
            This protein localizes to the endoplasmic reticulum and is known to
            metabolize as many as 25% of commonly prescribed drugs. Its
            substrates include antidepressants, antipsychotics, analgesics and
            antitussives, beta adrenergic blocking agents, antiarrythmics and
            antiemetics. The gene is highly polymorphic in the human
            population; certain alleles result in the poor metabolizer
            phenotype, characterized by a decreased ability to metabolize the
            enzyme's substrates. Some individuals with the poor metabolizer
            phenotype have no functional protein since they carry 2 null
            alleles whereas in other individuals the gene is absent. This gene
            can vary in copy number and individuals with the ultrarapid
            metabolizer phenotype can have 3 or more active copies of the gene.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jul
            2014].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            CDS, as compared to variant 1, which results in a shorter isoform
            (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC106757.1, CR456430.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..446
                     /product="cytochrome P450 2D6 isoform 2"
                     /EC_number="1.14.14.1"
                     /note="debrisoquine 4-hydroxylase; microsomal
                     monooxygenase; xenobiotic monooxygenase;
                     flavoprotein-linked monooxygenase; cytochrome P450,
                     subfamily IID (debrisoquine, sparteine, etc.,
                     -metabolizing), polypeptide 6; cholesterol 25-hydroxylase;
                     nonfunctional cytochrome P450 2D6; cytochrome P450,
                     subfamily IID (debrisoquine, sparteine, etc.,
                     -metabolizing)-like 1; cytochrome P450-DB1; cytochrome
                     P450, family 2, subfamily D, polypeptide 6"
                     /calculated_mol_wt=49930
     Region          65..441
                     /region_name="cytochrome_P450"
                     /note="cytochrome P450 (CYP) superfamily; cl41757"
                     /db_xref="CDD:477761"
     Site            order(135,250..251,254..255,258..259,262,313,323,325,348,
                     384..386,390..394,397..398)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410651"
     Site            order(161..162,250,253..254,258,321..324)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410651"
     CDS             1..446
                     /gene="CYP2D6"
                     /gene_synonym="CPD6; CYP2D; CYP2D7AP; CYP2D7BP; CYP2D7P2;
                     CYP2D8P2; CYP2DL1; CYPIID6; P450-DB1; P450C2D; P450DB1"
                     /coded_by="NM_001025161.3:20..1360"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS33657.1"
                     /db_xref="GeneID:1565"
                     /db_xref="HGNC:HGNC:2625"
                     /db_xref="MIM:124030"
ORIGIN      
        1 mglealvpla vivaiflllv dlmhrrqrwa aryppgplpl pglgnllhvd fqntpycfdq
       61 lrrrfgdvfs lqlawtpvvv lnglaavrea lvthgedtad rppvpitqil gfgprsqgrp
      121 frpnglldka vsnviasltc grrfeyddpr flrlldlaqe glkeesgflr evlnavpvll
      181 hipalagkvl rfqkafltql delltehrmt wdpaqpprdl teaflaemek akgnpessfn
      241 denlrivvad lfsagmvtts ttlawglllm ilhpdvqrrv qqeiddvigq vrrpemgdqa
      301 hmpyttavih evqrfgdivp lgvthmtsrd ievqgfripk gttlitnlss vlkdeavwek
      361 pfrfhpehfl daqghfvkpe aflpfsagrr aclgeplarm elflfftsll qhfsfsvptg
      421 qprpshhgvf aflvspspye lcavpr
//
LOCUS       NP_000758                491 aa            linear   PRI 20-JAN-2026
DEFINITION  cytochrome P450 2B6 [Homo sapiens].
ACCESSION   NP_000758
VERSION     NP_000758.1
DBSOURCE    REFSEQ: accession NM_000767.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Yamazaki,S., Hishinuma,E., Suzuki,Y., Ueda,A., Kijogi,C.,
            Nakayoshi,T., Oda,A., Saito,S., Tadaka,S., Kinoshita,K.,
            Maekawa,M., Sato,Y., Kumondai,M., Mano,N., Hirasawa,N. and
            Hiratsuka,M.
  TITLE     Functional significance of CYP2B6 gene rare allelic variants
            identified in Japanese individuals
  JOURNAL   Biochem Pharmacol 229, 116515 (2024)
   PUBMED   39218044
  REMARK    GeneRIF: Functional significance of CYP2B6 gene rare allelic
            variants identified in Japanese individuals.
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Eniayewu,O., Akinloye,A., Shenkoya,B., Azuka,U., Bolaji,O.,
            Adejuyigbe,E., Owen,A. and Olagunju,A.
  TITLE     Prenatal efavirenz exposure is independently associated with
            maternal, but not fetal CYP2B6 genotype
  JOURNAL   Pharmacogenet Genomics 34 (8), 253-260 (2024)
   PUBMED   38934229
  REMARK    GeneRIF: Prenatal efavirenz exposure is independently associated
            with maternal, but not fetal CYP2B6 genotype.
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Al-Adl,M., Youssef,M.M., El-Sebaie,A., Refaat,S. and El-Said,A.
  TITLE     The role of polymorphic cytochrome P450 gene (CYP2B6) in B-chronic
            lymphocytic leukemia (B-CLL) incidence and outcome among Egyptian
            patients
  JOURNAL   Oncol Res 32 (4), 785-797 (2024)
   PUBMED   38560574
  REMARK    GeneRIF: The role of polymorphic cytochrome P450 gene (CYP2B6) in
            B-chronic lymphocytic leukemia (B-CLL) incidence and outcome among
            Egyptian patients.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Zhou,Y., Dong,H., Fan,J., Zhu,M., Liu,L., Wang,Y., Tang,P. and
            Chen,X.
  TITLE     Cytochrome P450 2B6 and UDP-Glucuronosyltransferase Enzyme-Mediated
            Clearance of Ciprofol (HSK3486) in Humans: The Role of Hepatic and
            Extrahepatic Metabolism
  JOURNAL   Drug Metab Dispos 52 (2), 106-117 (2024)
   PUBMED   38071562
  REMARK    GeneRIF: Cytochrome P450 2B6 and UDP-Glucuronosyltransferase
            Enzyme-Mediated Clearance of Ciprofol (HSK3486) in Humans: The Role
            of Hepatic and Extrahepatic Metabolism.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Ma,X., Zang,X., Yang,L., Zhou,W., Li,Y., Wei,J., Guo,J., Han,J.,
            Liang,J. and Jin,T.
  TITLE     Genetic polymorphisms in CYP2B6 may be associated with lung cancer
            risk in the Chinese Han population
  JOURNAL   Expert Rev Respir Med 17 (12), 1297-1305 (2023)
   PUBMED   38166557
  REMARK    GeneRIF: Genetic polymorphisms in CYP2B6 may be associated with
            lung cancer risk in the Chinese Han population.
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Fernandez-Salguero,P., Hoffman,S.M., Cholerton,S., Mohrenweiser,H.,
            Raunio,H., Rautio,A., Pelkonen,O., Huang,J.D., Evans,W.E.,
            Idle,J.R. et al.
  TITLE     A genetic polymorphism in coumarin 7-hydroxylation: sequence of the
            human CYP2A genes and identification of variant CYP2A6 alleles
  JOURNAL   Am J Hum Genet 57 (3), 651-660 (1995)
   PUBMED   7668294
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Miles,J.S., McLaren,A.W., Gonzalez,F.J. and Wolf,C.R.
  TITLE     Alternative splicing in the human cytochrome P450IIB6 gene: use of
            a cryptic exon within intron 3 and splice acceptor site within exon
            4
  JOURNAL   Nucleic Acids Res 18 (1), 189 (1990)
   PUBMED   2308828
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Miles,J.S., McLaren,A.W. and Wolf,C.R.
  TITLE     Alternative splicing in the human cytochrome P450IIB6 gene
            generates a high level of aberrant messages
  JOURNAL   Nucleic Acids Res 17 (20), 8241-8255 (1989)
   PUBMED   2813061
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Yamano,S., Nhamburo,P.T., Aoyama,T., Meyer,U.A., Inaba,T.,
            Kalow,W., Gelboin,H.V., McBride,O.W. and Gonzalez,F.J.
  TITLE     cDNA cloning and sequence and cDNA-directed expression of human
            P450 IIB1: identification of a normal and two variant cDNAs derived
            from the CYP2B locus on chromosome 19 and differential expression
            of the IIB mRNAs in human liver
  JOURNAL   Biochemistry 28 (18), 7340-7348 (1989)
   PUBMED   2573390
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Miles,J.S., Spurr,N.K., Gough,A.C., Jowett,T., McLaren,A.W.,
            Brook,J.D. and Wolf,C.R.
  TITLE     A novel human cytochrome P450 gene (P450IIB): chromosomal
            localization and evidence for alternative splicing
  JOURNAL   Nucleic Acids Res 16 (13), 5783-5795 (1988)
   PUBMED   2899870
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011541.7, BC067431.1 and
            AC023172.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene, CYP2B6, encodes a member of the cytochrome P450
            superfamily of enzymes. The cytochrome P450 proteins are
            monooxygenases which catalyze many reactions involved in drug
            metabolism and synthesis of cholesterol, steroids and other lipids.
            This protein localizes to the endoplasmic reticulum and its
            expression is induced by phenobarbital. The enzyme is known to
            metabolize some xenobiotics, such as the anti-cancer drugs
            cyclophosphamide and ifosphamide. Transcript variants for this gene
            have been described; however, it has not been resolved whether
            these transcripts are in fact produced by this gene or by a closely
            related pseudogene, CYP2B7. Both the gene and the pseudogene are
            located in the middle of a CYP2A pseudogene found in a large
            cluster of cytochrome P450 genes from the CYP2A, CYP2B and CYP2F
            subfamilies on chromosome 19q. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M29874.1, BC067431.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2145122
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000324071.10/ ENSP00000324648.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..491
                     /product="cytochrome P450 2B6"
                     /EC_number="1.14.14.1"
                     /note="cytochrome P450, subfamily IIB
                     (phenobarbital-inducible), polypeptide 6; cytochrome P450
                     I